data_9M5M
# 
_entry.id   9M5M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9M5M         pdb_00009m5m 10.2210/pdb9m5m/pdb 
WWPDB D_1300057205 ?            ?                   
# 
_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       2025-06-04 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9M5M 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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                 3 
_pdbx_contact_author.email              amit.icgeb@gmail.com 
_pdbx_contact_author.name_first         Amit 
_pdbx_contact_author.name_last          Sharma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3305-0034 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sharma, V.K.'       1 0000-0002-7638-0906 
'Manickam, Y.'       2 0000-0002-2119-062X 
'Bagale, S.'         3 0009-0005-1768-1193 
'Pradeepkumar, P.I.' 4 0000-0001-9104-3708 
'Sharma, A.'         5 0000-0002-3305-0034 
# 
_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                     
'Natural product-mediated reaction hijacking mechanism validates Plasmodium aspartyl-tRNA synthetase as an antimalarial drug target' 
_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 'Ketprasit, N.'      1  ?                   
primary 'Tai, C.W.'          2  ?                   
primary 'Sharma, V.K.'       3  0000-0002-7638-0906 
primary 'Manickam, Y.'       4  0000-0002-2119-062X 
primary 'Khandokar, Y.'      5  ?                   
primary 'Ye, W.'             6  ?                   
primary 'Dogovski, C.'       7  ?                   
primary 'Hilko, D.H.'        8  ?                   
primary 'Morton, C.'         9  ?                   
primary 'Braun, A.S.C.'      10 ?                   
primary 'Leeming, M.'        11 ?                   
primary 'Bagale, S.'         12 ?                   
primary 'Pradeepkumar, P.I.' 13 ?                   
primary 'Panjikar, S.'       14 ?                   
primary 'Poulsen, S.A.'      15 ?                   
primary 'Griffin, M.D.W.'    16 ?                   
primary 'Sharma, A.'         17 ?                   
primary 'Tilley, L.'         18 ?                   
primary 'Xie, S.C.'          19 ?                   
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'aspartate--tRNA ligase' 62128.812 2   6.1.1.12 ? ? ? 
2 non-polymer syn 'SULFATE ION'            96.063    4   ?        ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL           62.068    2   ?        ? ? ? 
4 water       nat water                    18.015    492 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Aspartyl-tRNA synthetase' 
# 
_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       
;AERENLKNEATKVLEHVCEDINKESYGFVKISKMKENEKEIRLFNLEEIYHSLMKVGGSGATDGGKREDDAASHSVVAES
NGAHLLQSDIWVRGRIHDIRSKGSLAFIILRHKLYSMQCILDIKHNDNDKNMMKWVSNLPLESIVDIKGKLSKPEVPIDS
TNIKYEAHIRKIFCISKTAKELPFLLKDANMKETNEEGSIKVNQDNRLNNRCVDLRTYANYSIFCLQSQICTIFKNFLLE
NNFIEIHTPKLLGESSEGGANAFQINYFNQKGFLAQSPQLYKQMCINSGFDRVFEVAPVFRAENSNTYRHLCEYVSLDVE
MTYKYDYLENVHFYDSMFKHIFTELSKGGKNEMLIKTVKGQYPCEDFQWLEETPIFTYEEAIKMLIQHGKLHLKEEEILA
YDMSTDMEKELGKIVKASHHTDYYIIINFPSALRPFYTMYKEDEPAISNSYDFFMRGEEILSGSQRISDVNLLLENIKRF
NLDANKLNFYIDSFAYSSYPHSGCGIGLERVLMLFLGLNNIRKTSLFPRDPKRLIP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AERENLKNEATKVLEHVCEDINKESYGFVKISKMKENEKEIRLFNLEEIYHSLMKVGGSGATDGGKREDDAASHSVVAES
NGAHLLQSDIWVRGRIHDIRSKGSLAFIILRHKLYSMQCILDIKHNDNDKNMMKWVSNLPLESIVDIKGKLSKPEVPIDS
TNIKYEAHIRKIFCISKTAKELPFLLKDANMKETNEEGSIKVNQDNRLNNRCVDLRTYANYSIFCLQSQICTIFKNFLLE
NNFIEIHTPKLLGESSEGGANAFQINYFNQKGFLAQSPQLYKQMCINSGFDRVFEVAPVFRAENSNTYRHLCEYVSLDVE
MTYKYDYLENVHFYDSMFKHIFTELSKGGKNEMLIKTVKGQYPCEDFQWLEETPIFTYEEAIKMLIQHGKLHLKEEEILA
YDMSTDMEKELGKIVKASHHTDYYIIINFPSALRPFYTMYKEDEPAISNSYDFFMRGEEILSGSQRISDVNLLLENIKRF
NLDANKLNFYIDSFAYSSYPHSGCGIGLERVLMLFLGLNNIRKTSLFPRDPKRLIP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'  SO4 
3 1,2-ETHANEDIOL EDO 
4 water          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   GLU n 
1 3   ARG n 
1 4   GLU n 
1 5   ASN n 
1 6   LEU n 
1 7   LYS n 
1 8   ASN n 
1 9   GLU n 
1 10  ALA n 
1 11  THR n 
1 12  LYS n 
1 13  VAL n 
1 14  LEU n 
1 15  GLU n 
1 16  HIS n 
1 17  VAL n 
1 18  CYS n 
1 19  GLU n 
1 20  ASP n 
1 21  ILE n 
1 22  ASN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  TYR n 
1 27  GLY n 
1 28  PHE n 
1 29  VAL n 
1 30  LYS n 
1 31  ILE n 
1 32  SER n 
1 33  LYS n 
1 34  MET n 
1 35  LYS n 
1 36  GLU n 
1 37  ASN n 
1 38  GLU n 
1 39  LYS n 
1 40  GLU n 
1 41  ILE n 
1 42  ARG n 
1 43  LEU n 
1 44  PHE n 
1 45  ASN n 
1 46  LEU n 
1 47  GLU n 
1 48  GLU n 
1 49  ILE n 
1 50  TYR n 
1 51  HIS n 
1 52  SER n 
1 53  LEU n 
1 54  MET n 
1 55  LYS n 
1 56  VAL n 
1 57  GLY n 
1 58  GLY n 
1 59  SER n 
1 60  GLY n 
1 61  ALA n 
1 62  THR n 
1 63  ASP n 
1 64  GLY n 
1 65  GLY n 
1 66  LYS n 
1 67  ARG n 
1 68  GLU n 
1 69  ASP n 
1 70  ASP n 
1 71  ALA n 
1 72  ALA n 
1 73  SER n 
1 74  HIS n 
1 75  SER n 
1 76  VAL n 
1 77  VAL n 
1 78  ALA n 
1 79  GLU n 
1 80  SER n 
1 81  ASN n 
1 82  GLY n 
1 83  ALA n 
1 84  HIS n 
1 85  LEU n 
1 86  LEU n 
1 87  GLN n 
1 88  SER n 
1 89  ASP n 
1 90  ILE n 
1 91  TRP n 
1 92  VAL n 
1 93  ARG n 
1 94  GLY n 
1 95  ARG n 
1 96  ILE n 
1 97  HIS n 
1 98  ASP n 
1 99  ILE n 
1 100 ARG n 
1 101 SER n 
1 102 LYS n 
1 103 GLY n 
1 104 SER n 
1 105 LEU n 
1 106 ALA n 
1 107 PHE n 
1 108 ILE n 
1 109 ILE n 
1 110 LEU n 
1 111 ARG n 
1 112 HIS n 
1 113 LYS n 
1 114 LEU n 
1 115 TYR n 
1 116 SER n 
1 117 MET n 
1 118 GLN n 
1 119 CYS n 
1 120 ILE n 
1 121 LEU n 
1 122 ASP n 
1 123 ILE n 
1 124 LYS n 
1 125 HIS n 
1 126 ASN n 
1 127 ASP n 
1 128 ASN n 
1 129 ASP n 
1 130 LYS n 
1 131 ASN n 
1 132 MET n 
1 133 MET n 
1 134 LYS n 
1 135 TRP n 
1 136 VAL n 
1 137 SER n 
1 138 ASN n 
1 139 LEU n 
1 140 PRO n 
1 141 LEU n 
1 142 GLU n 
1 143 SER n 
1 144 ILE n 
1 145 VAL n 
1 146 ASP n 
1 147 ILE n 
1 148 LYS n 
1 149 GLY n 
1 150 LYS n 
1 151 LEU n 
1 152 SER n 
1 153 LYS n 
1 154 PRO n 
1 155 GLU n 
1 156 VAL n 
1 157 PRO n 
1 158 ILE n 
1 159 ASP n 
1 160 SER n 
1 161 THR n 
1 162 ASN n 
1 163 ILE n 
1 164 LYS n 
1 165 TYR n 
1 166 GLU n 
1 167 ALA n 
1 168 HIS n 
1 169 ILE n 
1 170 ARG n 
1 171 LYS n 
1 172 ILE n 
1 173 PHE n 
1 174 CYS n 
1 175 ILE n 
1 176 SER n 
1 177 LYS n 
1 178 THR n 
1 179 ALA n 
1 180 LYS n 
1 181 GLU n 
1 182 LEU n 
1 183 PRO n 
1 184 PHE n 
1 185 LEU n 
1 186 LEU n 
1 187 LYS n 
1 188 ASP n 
1 189 ALA n 
1 190 ASN n 
1 191 MET n 
1 192 LYS n 
1 193 GLU n 
1 194 THR n 
1 195 ASN n 
1 196 GLU n 
1 197 GLU n 
1 198 GLY n 
1 199 SER n 
1 200 ILE n 
1 201 LYS n 
1 202 VAL n 
1 203 ASN n 
1 204 GLN n 
1 205 ASP n 
1 206 ASN n 
1 207 ARG n 
1 208 LEU n 
1 209 ASN n 
1 210 ASN n 
1 211 ARG n 
1 212 CYS n 
1 213 VAL n 
1 214 ASP n 
1 215 LEU n 
1 216 ARG n 
1 217 THR n 
1 218 TYR n 
1 219 ALA n 
1 220 ASN n 
1 221 TYR n 
1 222 SER n 
1 223 ILE n 
1 224 PHE n 
1 225 CYS n 
1 226 LEU n 
1 227 GLN n 
1 228 SER n 
1 229 GLN n 
1 230 ILE n 
1 231 CYS n 
1 232 THR n 
1 233 ILE n 
1 234 PHE n 
1 235 LYS n 
1 236 ASN n 
1 237 PHE n 
1 238 LEU n 
1 239 LEU n 
1 240 GLU n 
1 241 ASN n 
1 242 ASN n 
1 243 PHE n 
1 244 ILE n 
1 245 GLU n 
1 246 ILE n 
1 247 HIS n 
1 248 THR n 
1 249 PRO n 
1 250 LYS n 
1 251 LEU n 
1 252 LEU n 
1 253 GLY n 
1 254 GLU n 
1 255 SER n 
1 256 SER n 
1 257 GLU n 
1 258 GLY n 
1 259 GLY n 
1 260 ALA n 
1 261 ASN n 
1 262 ALA n 
1 263 PHE n 
1 264 GLN n 
1 265 ILE n 
1 266 ASN n 
1 267 TYR n 
1 268 PHE n 
1 269 ASN n 
1 270 GLN n 
1 271 LYS n 
1 272 GLY n 
1 273 PHE n 
1 274 LEU n 
1 275 ALA n 
1 276 GLN n 
1 277 SER n 
1 278 PRO n 
1 279 GLN n 
1 280 LEU n 
1 281 TYR n 
1 282 LYS n 
1 283 GLN n 
1 284 MET n 
1 285 CYS n 
1 286 ILE n 
1 287 ASN n 
1 288 SER n 
1 289 GLY n 
1 290 PHE n 
1 291 ASP n 
1 292 ARG n 
1 293 VAL n 
1 294 PHE n 
1 295 GLU n 
1 296 VAL n 
1 297 ALA n 
1 298 PRO n 
1 299 VAL n 
1 300 PHE n 
1 301 ARG n 
1 302 ALA n 
1 303 GLU n 
1 304 ASN n 
1 305 SER n 
1 306 ASN n 
1 307 THR n 
1 308 TYR n 
1 309 ARG n 
1 310 HIS n 
1 311 LEU n 
1 312 CYS n 
1 313 GLU n 
1 314 TYR n 
1 315 VAL n 
1 316 SER n 
1 317 LEU n 
1 318 ASP n 
1 319 VAL n 
1 320 GLU n 
1 321 MET n 
1 322 THR n 
1 323 TYR n 
1 324 LYS n 
1 325 TYR n 
1 326 ASP n 
1 327 TYR n 
1 328 LEU n 
1 329 GLU n 
1 330 ASN n 
1 331 VAL n 
1 332 HIS n 
1 333 PHE n 
1 334 TYR n 
1 335 ASP n 
1 336 SER n 
1 337 MET n 
1 338 PHE n 
1 339 LYS n 
1 340 HIS n 
1 341 ILE n 
1 342 PHE n 
1 343 THR n 
1 344 GLU n 
1 345 LEU n 
1 346 SER n 
1 347 LYS n 
1 348 GLY n 
1 349 GLY n 
1 350 LYS n 
1 351 ASN n 
1 352 GLU n 
1 353 MET n 
1 354 LEU n 
1 355 ILE n 
1 356 LYS n 
1 357 THR n 
1 358 VAL n 
1 359 LYS n 
1 360 GLY n 
1 361 GLN n 
1 362 TYR n 
1 363 PRO n 
1 364 CYS n 
1 365 GLU n 
1 366 ASP n 
1 367 PHE n 
1 368 GLN n 
1 369 TRP n 
1 370 LEU n 
1 371 GLU n 
1 372 GLU n 
1 373 THR n 
1 374 PRO n 
1 375 ILE n 
1 376 PHE n 
1 377 THR n 
1 378 TYR n 
1 379 GLU n 
1 380 GLU n 
1 381 ALA n 
1 382 ILE n 
1 383 LYS n 
1 384 MET n 
1 385 LEU n 
1 386 ILE n 
1 387 GLN n 
1 388 HIS n 
1 389 GLY n 
1 390 LYS n 
1 391 LEU n 
1 392 HIS n 
1 393 LEU n 
1 394 LYS n 
1 395 GLU n 
1 396 GLU n 
1 397 GLU n 
1 398 ILE n 
1 399 LEU n 
1 400 ALA n 
1 401 TYR n 
1 402 ASP n 
1 403 MET n 
1 404 SER n 
1 405 THR n 
1 406 ASP n 
1 407 MET n 
1 408 GLU n 
1 409 LYS n 
1 410 GLU n 
1 411 LEU n 
1 412 GLY n 
1 413 LYS n 
1 414 ILE n 
1 415 VAL n 
1 416 LYS n 
1 417 ALA n 
1 418 SER n 
1 419 HIS n 
1 420 HIS n 
1 421 THR n 
1 422 ASP n 
1 423 TYR n 
1 424 TYR n 
1 425 ILE n 
1 426 ILE n 
1 427 ILE n 
1 428 ASN n 
1 429 PHE n 
1 430 PRO n 
1 431 SER n 
1 432 ALA n 
1 433 LEU n 
1 434 ARG n 
1 435 PRO n 
1 436 PHE n 
1 437 TYR n 
1 438 THR n 
1 439 MET n 
1 440 TYR n 
1 441 LYS n 
1 442 GLU n 
1 443 ASP n 
1 444 GLU n 
1 445 PRO n 
1 446 ALA n 
1 447 ILE n 
1 448 SER n 
1 449 ASN n 
1 450 SER n 
1 451 TYR n 
1 452 ASP n 
1 453 PHE n 
1 454 PHE n 
1 455 MET n 
1 456 ARG n 
1 457 GLY n 
1 458 GLU n 
1 459 GLU n 
1 460 ILE n 
1 461 LEU n 
1 462 SER n 
1 463 GLY n 
1 464 SER n 
1 465 GLN n 
1 466 ARG n 
1 467 ILE n 
1 468 SER n 
1 469 ASP n 
1 470 VAL n 
1 471 ASN n 
1 472 LEU n 
1 473 LEU n 
1 474 LEU n 
1 475 GLU n 
1 476 ASN n 
1 477 ILE n 
1 478 LYS n 
1 479 ARG n 
1 480 PHE n 
1 481 ASN n 
1 482 LEU n 
1 483 ASP n 
1 484 ALA n 
1 485 ASN n 
1 486 LYS n 
1 487 LEU n 
1 488 ASN n 
1 489 PHE n 
1 490 TYR n 
1 491 ILE n 
1 492 ASP n 
1 493 SER n 
1 494 PHE n 
1 495 ALA n 
1 496 TYR n 
1 497 SER n 
1 498 SER n 
1 499 TYR n 
1 500 PRO n 
1 501 HIS n 
1 502 SER n 
1 503 GLY n 
1 504 CYS n 
1 505 GLY n 
1 506 ILE n 
1 507 GLY n 
1 508 LEU n 
1 509 GLU n 
1 510 ARG n 
1 511 VAL n 
1 512 LEU n 
1 513 MET n 
1 514 LEU n 
1 515 PHE n 
1 516 LEU n 
1 517 GLY n 
1 518 LEU n 
1 519 ASN n 
1 520 ASN n 
1 521 ILE n 
1 522 ARG n 
1 523 LYS n 
1 524 THR n 
1 525 SER n 
1 526 LEU n 
1 527 PHE n 
1 528 PRO n 
1 529 ARG n 
1 530 ASP n 
1 531 PRO n 
1 532 LYS n 
1 533 ARG n 
1 534 LEU n 
1 535 ILE n 
1 536 PRO 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                   536 
_entity_src_gen.gene_src_common_name               'malaria parasite P. vivax' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PVC01_020016700, PVW1_020019400' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Plasmodium vivax' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5855 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
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 
SO4 non-polymer         . 'SULFATE ION'   ?                 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ?                 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                 'C5 H11 N O2'    117.146 
# 
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   ALA 1   96  ?   ?   ?   A . n 
A 1 2   GLU 2   97  ?   ?   ?   A . n 
A 1 3   ARG 3   98  98  ARG ARG A . n 
A 1 4   GLU 4   99  99  GLU GLU A . n 
A 1 5   ASN 5   100 100 ASN ASN A . n 
A 1 6   LEU 6   101 101 LEU LEU A . n 
A 1 7   LYS 7   102 102 LYS LYS A . n 
A 1 8   ASN 8   103 103 ASN ASN A . n 
A 1 9   GLU 9   104 104 GLU GLU A . n 
A 1 10  ALA 10  105 105 ALA ALA A . n 
A 1 11  THR 11  106 106 THR THR A . n 
A 1 12  LYS 12  107 107 LYS LYS A . n 
A 1 13  VAL 13  108 108 VAL VAL A . n 
A 1 14  LEU 14  109 109 LEU LEU A . n 
A 1 15  GLU 15  110 110 GLU GLU A . n 
A 1 16  HIS 16  111 111 HIS HIS A . n 
A 1 17  VAL 17  112 112 VAL VAL A . n 
A 1 18  CYS 18  113 113 CYS CYS A . n 
A 1 19  GLU 19  114 114 GLU GLU A . n 
A 1 20  ASP 20  115 115 ASP ASP A . n 
A 1 21  ILE 21  116 116 ILE ILE A . n 
A 1 22  ASN 22  117 117 ASN ASN A . n 
A 1 23  LYS 23  118 118 LYS LYS A . n 
A 1 24  GLU 24  119 119 GLU GLU A . n 
A 1 25  SER 25  120 120 SER SER A . n 
A 1 26  TYR 26  121 121 TYR TYR A . n 
A 1 27  GLY 27  122 122 GLY GLY A . n 
A 1 28  PHE 28  123 123 PHE PHE A . n 
A 1 29  VAL 29  124 124 VAL VAL A . n 
A 1 30  LYS 30  125 125 LYS LYS A . n 
A 1 31  ILE 31  126 126 ILE ILE A . n 
A 1 32  SER 32  127 127 SER SER A . n 
A 1 33  LYS 33  128 128 LYS LYS A . n 
A 1 34  MET 34  129 129 MET MET A . n 
A 1 35  LYS 35  130 130 LYS LYS A . n 
A 1 36  GLU 36  131 131 GLU GLU A . n 
A 1 37  ASN 37  132 132 ASN ASN A . n 
A 1 38  GLU 38  133 133 GLU GLU A . n 
A 1 39  LYS 39  134 134 LYS LYS A . n 
A 1 40  GLU 40  135 135 GLU GLU A . n 
A 1 41  ILE 41  136 136 ILE ILE A . n 
A 1 42  ARG 42  137 137 ARG ARG A . n 
A 1 43  LEU 43  138 138 LEU LEU A . n 
A 1 44  PHE 44  139 139 PHE PHE A . n 
A 1 45  ASN 45  140 140 ASN ASN A . n 
A 1 46  LEU 46  141 141 LEU LEU A . n 
A 1 47  GLU 47  142 142 GLU GLU A . n 
A 1 48  GLU 48  143 143 GLU GLU A . n 
A 1 49  ILE 49  144 144 ILE ILE A . n 
A 1 50  TYR 50  145 145 TYR TYR A . n 
A 1 51  HIS 51  146 146 HIS HIS A . n 
A 1 52  SER 52  147 147 SER SER A . n 
A 1 53  LEU 53  148 148 LEU LEU A . n 
A 1 54  MET 54  149 149 MET MET A . n 
A 1 55  LYS 55  150 ?   ?   ?   A . n 
A 1 56  VAL 56  151 ?   ?   ?   A . n 
A 1 57  GLY 57  152 ?   ?   ?   A . n 
A 1 58  GLY 58  153 ?   ?   ?   A . n 
A 1 59  SER 59  154 ?   ?   ?   A . n 
A 1 60  GLY 60  155 ?   ?   ?   A . n 
A 1 61  ALA 61  156 ?   ?   ?   A . n 
A 1 62  THR 62  157 ?   ?   ?   A . n 
A 1 63  ASP 63  158 ?   ?   ?   A . n 
A 1 64  GLY 64  159 ?   ?   ?   A . n 
A 1 65  GLY 65  160 ?   ?   ?   A . n 
A 1 66  LYS 66  161 ?   ?   ?   A . n 
A 1 67  ARG 67  162 ?   ?   ?   A . n 
A 1 68  GLU 68  163 ?   ?   ?   A . n 
A 1 69  ASP 69  164 ?   ?   ?   A . n 
A 1 70  ASP 70  165 ?   ?   ?   A . n 
A 1 71  ALA 71  166 ?   ?   ?   A . n 
A 1 72  ALA 72  167 ?   ?   ?   A . n 
A 1 73  SER 73  168 ?   ?   ?   A . n 
A 1 74  HIS 74  169 ?   ?   ?   A . n 
A 1 75  SER 75  170 ?   ?   ?   A . n 
A 1 76  VAL 76  171 ?   ?   ?   A . n 
A 1 77  VAL 77  172 ?   ?   ?   A . n 
A 1 78  ALA 78  173 ?   ?   ?   A . n 
A 1 79  GLU 79  174 ?   ?   ?   A . n 
A 1 80  SER 80  175 ?   ?   ?   A . n 
A 1 81  ASN 81  176 ?   ?   ?   A . n 
A 1 82  GLY 82  177 ?   ?   ?   A . n 
A 1 83  ALA 83  178 ?   ?   ?   A . n 
A 1 84  HIS 84  179 179 HIS HIS A . n 
A 1 85  LEU 85  180 180 LEU LEU A . n 
A 1 86  LEU 86  181 181 LEU LEU A . n 
A 1 87  GLN 87  182 182 GLN GLN A . n 
A 1 88  SER 88  183 183 SER SER A . n 
A 1 89  ASP 89  184 184 ASP ASP A . n 
A 1 90  ILE 90  185 185 ILE ILE A . n 
A 1 91  TRP 91  186 186 TRP TRP A . n 
A 1 92  VAL 92  187 187 VAL VAL A . n 
A 1 93  ARG 93  188 188 ARG ARG A . n 
A 1 94  GLY 94  189 189 GLY GLY A . n 
A 1 95  ARG 95  190 190 ARG ARG A . n 
A 1 96  ILE 96  191 191 ILE ILE A . n 
A 1 97  HIS 97  192 192 HIS HIS A . n 
A 1 98  ASP 98  193 193 ASP ASP A . n 
A 1 99  ILE 99  194 194 ILE ILE A . n 
A 1 100 ARG 100 195 195 ARG ARG A . n 
A 1 101 SER 101 196 196 SER SER A . n 
A 1 102 LYS 102 197 197 LYS LYS A . n 
A 1 103 GLY 103 198 198 GLY GLY A . n 
A 1 104 SER 104 199 199 SER SER A . n 
A 1 105 LEU 105 200 200 LEU LEU A . n 
A 1 106 ALA 106 201 201 ALA ALA A . n 
A 1 107 PHE 107 202 202 PHE PHE A . n 
A 1 108 ILE 108 203 203 ILE ILE A . n 
A 1 109 ILE 109 204 204 ILE ILE A . n 
A 1 110 LEU 110 205 205 LEU LEU A . n 
A 1 111 ARG 111 206 206 ARG ARG A . n 
A 1 112 HIS 112 207 207 HIS HIS A . n 
A 1 113 LYS 113 208 208 LYS LYS A . n 
A 1 114 LEU 114 209 209 LEU LEU A . n 
A 1 115 TYR 115 210 210 TYR TYR A . n 
A 1 116 SER 116 211 211 SER SER A . n 
A 1 117 MET 117 212 212 MET MET A . n 
A 1 118 GLN 118 213 213 GLN GLN A . n 
A 1 119 CYS 119 214 214 CYS CYS A . n 
A 1 120 ILE 120 215 215 ILE ILE A . n 
A 1 121 LEU 121 216 216 LEU LEU A . n 
A 1 122 ASP 122 217 217 ASP ASP A . n 
A 1 123 ILE 123 218 218 ILE ILE A . n 
A 1 124 LYS 124 219 219 LYS LYS A . n 
A 1 125 HIS 125 220 220 HIS HIS A . n 
A 1 126 ASN 126 221 221 ASN ASN A . n 
A 1 127 ASP 127 222 222 ASP ASP A . n 
A 1 128 ASN 128 223 223 ASN ASN A . n 
A 1 129 ASP 129 224 224 ASP ASP A . n 
A 1 130 LYS 130 225 225 LYS LYS A . n 
A 1 131 ASN 131 226 226 ASN ASN A . n 
A 1 132 MET 132 227 227 MET MET A . n 
A 1 133 MET 133 228 228 MET MET A . n 
A 1 134 LYS 134 229 229 LYS LYS A . n 
A 1 135 TRP 135 230 230 TRP TRP A . n 
A 1 136 VAL 136 231 231 VAL VAL A . n 
A 1 137 SER 137 232 232 SER SER A . n 
A 1 138 ASN 138 233 233 ASN ASN A . n 
A 1 139 LEU 139 234 234 LEU LEU A . n 
A 1 140 PRO 140 235 235 PRO PRO A . n 
A 1 141 LEU 141 236 236 LEU LEU A . n 
A 1 142 GLU 142 237 237 GLU GLU A . n 
A 1 143 SER 143 238 238 SER SER A . n 
A 1 144 ILE 144 239 239 ILE ILE A . n 
A 1 145 VAL 145 240 240 VAL VAL A . n 
A 1 146 ASP 146 241 241 ASP ASP A . n 
A 1 147 ILE 147 242 242 ILE ILE A . n 
A 1 148 LYS 148 243 243 LYS LYS A . n 
A 1 149 GLY 149 244 244 GLY GLY A . n 
A 1 150 LYS 150 245 245 LYS LYS A . n 
A 1 151 LEU 151 246 246 LEU LEU A . n 
A 1 152 SER 152 247 247 SER SER A . n 
A 1 153 LYS 153 248 248 LYS LYS A . n 
A 1 154 PRO 154 249 249 PRO PRO A . n 
A 1 155 GLU 155 250 250 GLU GLU A . n 
A 1 156 VAL 156 251 251 VAL VAL A . n 
A 1 157 PRO 157 252 252 PRO PRO A . n 
A 1 158 ILE 158 253 253 ILE ILE A . n 
A 1 159 ASP 159 254 254 ASP ASP A . n 
A 1 160 SER 160 255 255 SER SER A . n 
A 1 161 THR 161 256 256 THR THR A . n 
A 1 162 ASN 162 257 257 ASN ASN A . n 
A 1 163 ILE 163 258 258 ILE ILE A . n 
A 1 164 LYS 164 259 259 LYS LYS A . n 
A 1 165 TYR 165 260 260 TYR TYR A . n 
A 1 166 GLU 166 261 261 GLU GLU A . n 
A 1 167 ALA 167 262 262 ALA ALA A . n 
A 1 168 HIS 168 263 263 HIS HIS A . n 
A 1 169 ILE 169 264 264 ILE ILE A . n 
A 1 170 ARG 170 265 265 ARG ARG A . n 
A 1 171 LYS 171 266 266 LYS LYS A . n 
A 1 172 ILE 172 267 267 ILE ILE A . n 
A 1 173 PHE 173 268 268 PHE PHE A . n 
A 1 174 CYS 174 269 269 CYS CYS A . n 
A 1 175 ILE 175 270 270 ILE ILE A . n 
A 1 176 SER 176 271 271 SER SER A . n 
A 1 177 LYS 177 272 272 LYS LYS A . n 
A 1 178 THR 178 273 273 THR THR A . n 
A 1 179 ALA 179 274 274 ALA ALA A . n 
A 1 180 LYS 180 275 275 LYS LYS A . n 
A 1 181 GLU 181 276 276 GLU GLU A . n 
A 1 182 LEU 182 277 277 LEU LEU A . n 
A 1 183 PRO 183 278 278 PRO PRO A . n 
A 1 184 PHE 184 279 279 PHE PHE A . n 
A 1 185 LEU 185 280 280 LEU LEU A . n 
A 1 186 LEU 186 281 281 LEU LEU A . n 
A 1 187 LYS 187 282 282 LYS LYS A . n 
A 1 188 ASP 188 283 283 ASP ASP A . n 
A 1 189 ALA 189 284 284 ALA ALA A . n 
A 1 190 ASN 190 285 285 ASN ASN A . n 
A 1 191 MET 191 286 286 MET MET A . n 
A 1 192 LYS 192 287 287 LYS LYS A . n 
A 1 193 GLU 193 288 288 GLU GLU A . n 
A 1 194 THR 194 289 289 THR THR A . n 
A 1 195 ASN 195 290 290 ASN ASN A . n 
A 1 196 GLU 196 291 291 GLU GLU A . n 
A 1 197 GLU 197 292 292 GLU GLU A . n 
A 1 198 GLY 198 293 293 GLY GLY A . n 
A 1 199 SER 199 294 294 SER SER A . n 
A 1 200 ILE 200 295 295 ILE ILE A . n 
A 1 201 LYS 201 296 296 LYS LYS A . n 
A 1 202 VAL 202 297 297 VAL VAL A . n 
A 1 203 ASN 203 298 298 ASN ASN A . n 
A 1 204 GLN 204 299 299 GLN GLN A . n 
A 1 205 ASP 205 300 300 ASP ASP A . n 
A 1 206 ASN 206 301 301 ASN ASN A . n 
A 1 207 ARG 207 302 302 ARG ARG A . n 
A 1 208 LEU 208 303 303 LEU LEU A . n 
A 1 209 ASN 209 304 304 ASN ASN A . n 
A 1 210 ASN 210 305 305 ASN ASN A . n 
A 1 211 ARG 211 306 306 ARG ARG A . n 
A 1 212 CYS 212 307 307 CYS CYS A . n 
A 1 213 VAL 213 308 308 VAL VAL A . n 
A 1 214 ASP 214 309 309 ASP ASP A . n 
A 1 215 LEU 215 310 310 LEU LEU A . n 
A 1 216 ARG 216 311 311 ARG ARG A . n 
A 1 217 THR 217 312 312 THR THR A . n 
A 1 218 TYR 218 313 313 TYR TYR A . n 
A 1 219 ALA 219 314 314 ALA ALA A . n 
A 1 220 ASN 220 315 315 ASN ASN A . n 
A 1 221 TYR 221 316 316 TYR TYR A . n 
A 1 222 SER 222 317 317 SER SER A . n 
A 1 223 ILE 223 318 318 ILE ILE A . n 
A 1 224 PHE 224 319 319 PHE PHE A . n 
A 1 225 CYS 225 320 320 CYS CYS A . n 
A 1 226 LEU 226 321 321 LEU LEU A . n 
A 1 227 GLN 227 322 322 GLN GLN A . n 
A 1 228 SER 228 323 323 SER SER A . n 
A 1 229 GLN 229 324 324 GLN GLN A . n 
A 1 230 ILE 230 325 325 ILE ILE A . n 
A 1 231 CYS 231 326 326 CYS CYS A . n 
A 1 232 THR 232 327 327 THR THR A . n 
A 1 233 ILE 233 328 328 ILE ILE A . n 
A 1 234 PHE 234 329 329 PHE PHE A . n 
A 1 235 LYS 235 330 330 LYS LYS A . n 
A 1 236 ASN 236 331 331 ASN ASN A . n 
A 1 237 PHE 237 332 332 PHE PHE A . n 
A 1 238 LEU 238 333 333 LEU LEU A . n 
A 1 239 LEU 239 334 334 LEU LEU A . n 
A 1 240 GLU 240 335 335 GLU GLU A . n 
A 1 241 ASN 241 336 336 ASN ASN A . n 
A 1 242 ASN 242 337 337 ASN ASN A . n 
A 1 243 PHE 243 338 338 PHE PHE A . n 
A 1 244 ILE 244 339 339 ILE ILE A . n 
A 1 245 GLU 245 340 340 GLU GLU A . n 
A 1 246 ILE 246 341 341 ILE ILE A . n 
A 1 247 HIS 247 342 342 HIS HIS A . n 
A 1 248 THR 248 343 343 THR THR A . n 
A 1 249 PRO 249 344 344 PRO PRO A . n 
A 1 250 LYS 250 345 345 LYS LYS A . n 
A 1 251 LEU 251 346 346 LEU LEU A . n 
A 1 252 LEU 252 347 347 LEU LEU A . n 
A 1 253 GLY 253 348 348 GLY GLY A . n 
A 1 254 GLU 254 349 349 GLU GLU A . n 
A 1 255 SER 255 350 350 SER SER A . n 
A 1 256 SER 256 351 ?   ?   ?   A . n 
A 1 257 GLU 257 352 ?   ?   ?   A . n 
A 1 258 GLY 258 353 ?   ?   ?   A . n 
A 1 259 GLY 259 354 ?   ?   ?   A . n 
A 1 260 ALA 260 355 355 ALA ALA A . n 
A 1 261 ASN 261 356 356 ASN ASN A . n 
A 1 262 ALA 262 357 357 ALA ALA A . n 
A 1 263 PHE 263 358 358 PHE PHE A . n 
A 1 264 GLN 264 359 359 GLN GLN A . n 
A 1 265 ILE 265 360 360 ILE ILE A . n 
A 1 266 ASN 266 361 361 ASN ASN A . n 
A 1 267 TYR 267 362 362 TYR TYR A . n 
A 1 268 PHE 268 363 363 PHE PHE A . n 
A 1 269 ASN 269 364 364 ASN ASN A . n 
A 1 270 GLN 270 365 365 GLN GLN A . n 
A 1 271 LYS 271 366 366 LYS LYS A . n 
A 1 272 GLY 272 367 367 GLY GLY A . n 
A 1 273 PHE 273 368 368 PHE PHE A . n 
A 1 274 LEU 274 369 369 LEU LEU A . n 
A 1 275 ALA 275 370 370 ALA ALA A . n 
A 1 276 GLN 276 371 371 GLN GLN A . n 
A 1 277 SER 277 372 372 SER SER A . n 
A 1 278 PRO 278 373 373 PRO PRO A . n 
A 1 279 GLN 279 374 374 GLN GLN A . n 
A 1 280 LEU 280 375 375 LEU LEU A . n 
A 1 281 TYR 281 376 376 TYR TYR A . n 
A 1 282 LYS 282 377 377 LYS LYS A . n 
A 1 283 GLN 283 378 378 GLN GLN A . n 
A 1 284 MET 284 379 379 MET MET A . n 
A 1 285 CYS 285 380 380 CYS CYS A . n 
A 1 286 ILE 286 381 381 ILE ILE A . n 
A 1 287 ASN 287 382 382 ASN ASN A . n 
A 1 288 SER 288 383 383 SER SER A . n 
A 1 289 GLY 289 384 384 GLY GLY A . n 
A 1 290 PHE 290 385 385 PHE PHE A . n 
A 1 291 ASP 291 386 386 ASP ASP A . n 
A 1 292 ARG 292 387 387 ARG ARG A . n 
A 1 293 VAL 293 388 388 VAL VAL A . n 
A 1 294 PHE 294 389 389 PHE PHE A . n 
A 1 295 GLU 295 390 390 GLU GLU A . n 
A 1 296 VAL 296 391 391 VAL VAL A . n 
A 1 297 ALA 297 392 392 ALA ALA A . n 
A 1 298 PRO 298 393 393 PRO PRO A . n 
A 1 299 VAL 299 394 394 VAL VAL A . n 
A 1 300 PHE 300 395 395 PHE PHE A . n 
A 1 301 ARG 301 396 396 ARG ARG A . n 
A 1 302 ALA 302 397 397 ALA ALA A . n 
A 1 303 GLU 303 398 398 GLU GLU A . n 
A 1 304 ASN 304 399 399 ASN ASN A . n 
A 1 305 SER 305 400 400 SER SER A . n 
A 1 306 ASN 306 401 401 ASN ASN A . n 
A 1 307 THR 307 402 402 THR THR A . n 
A 1 308 TYR 308 403 403 TYR TYR A . n 
A 1 309 ARG 309 404 404 ARG ARG A . n 
A 1 310 HIS 310 405 405 HIS HIS A . n 
A 1 311 LEU 311 406 406 LEU LEU A . n 
A 1 312 CYS 312 407 407 CYS CYS A . n 
A 1 313 GLU 313 408 408 GLU GLU A . n 
A 1 314 TYR 314 409 409 TYR TYR A . n 
A 1 315 VAL 315 410 410 VAL VAL A . n 
A 1 316 SER 316 411 411 SER SER A . n 
A 1 317 LEU 317 412 412 LEU LEU A . n 
A 1 318 ASP 318 413 413 ASP ASP A . n 
A 1 319 VAL 319 414 414 VAL VAL A . n 
A 1 320 GLU 320 415 415 GLU GLU A . n 
A 1 321 MET 321 416 416 MET MET A . n 
A 1 322 THR 322 417 417 THR THR A . n 
A 1 323 TYR 323 418 418 TYR TYR A . n 
A 1 324 LYS 324 419 419 LYS LYS A . n 
A 1 325 TYR 325 420 420 TYR TYR A . n 
A 1 326 ASP 326 421 421 ASP ASP A . n 
A 1 327 TYR 327 422 422 TYR TYR A . n 
A 1 328 LEU 328 423 423 LEU LEU A . n 
A 1 329 GLU 329 424 424 GLU GLU A . n 
A 1 330 ASN 330 425 425 ASN ASN A . n 
A 1 331 VAL 331 426 426 VAL VAL A . n 
A 1 332 HIS 332 427 427 HIS HIS A . n 
A 1 333 PHE 333 428 428 PHE PHE A . n 
A 1 334 TYR 334 429 429 TYR TYR A . n 
A 1 335 ASP 335 430 430 ASP ASP A . n 
A 1 336 SER 336 431 431 SER SER A . n 
A 1 337 MET 337 432 432 MET MET A . n 
A 1 338 PHE 338 433 433 PHE PHE A . n 
A 1 339 LYS 339 434 434 LYS LYS A . n 
A 1 340 HIS 340 435 435 HIS HIS A . n 
A 1 341 ILE 341 436 436 ILE ILE A . n 
A 1 342 PHE 342 437 437 PHE PHE A . n 
A 1 343 THR 343 438 438 THR THR A . n 
A 1 344 GLU 344 439 439 GLU GLU A . n 
A 1 345 LEU 345 440 440 LEU LEU A . n 
A 1 346 SER 346 441 441 SER SER A . n 
A 1 347 LYS 347 442 442 LYS LYS A . n 
A 1 348 GLY 348 443 443 GLY GLY A . n 
A 1 349 GLY 349 444 444 GLY GLY A . n 
A 1 350 LYS 350 445 445 LYS LYS A . n 
A 1 351 ASN 351 446 446 ASN ASN A . n 
A 1 352 GLU 352 447 447 GLU GLU A . n 
A 1 353 MET 353 448 448 MET MET A . n 
A 1 354 LEU 354 449 449 LEU LEU A . n 
A 1 355 ILE 355 450 450 ILE ILE A . n 
A 1 356 LYS 356 451 451 LYS LYS A . n 
A 1 357 THR 357 452 452 THR THR A . n 
A 1 358 VAL 358 453 453 VAL VAL A . n 
A 1 359 LYS 359 454 454 LYS LYS A . n 
A 1 360 GLY 360 455 455 GLY GLY A . n 
A 1 361 GLN 361 456 456 GLN GLN A . n 
A 1 362 TYR 362 457 457 TYR TYR A . n 
A 1 363 PRO 363 458 458 PRO PRO A . n 
A 1 364 CYS 364 459 459 CYS CYS A . n 
A 1 365 GLU 365 460 460 GLU GLU A . n 
A 1 366 ASP 366 461 461 ASP ASP A . n 
A 1 367 PHE 367 462 462 PHE PHE A . n 
A 1 368 GLN 368 463 463 GLN GLN A . n 
A 1 369 TRP 369 464 464 TRP TRP A . n 
A 1 370 LEU 370 465 465 LEU LEU A . n 
A 1 371 GLU 371 466 466 GLU GLU A . n 
A 1 372 GLU 372 467 467 GLU GLU A . n 
A 1 373 THR 373 468 468 THR THR A . n 
A 1 374 PRO 374 469 469 PRO PRO A . n 
A 1 375 ILE 375 470 470 ILE ILE A . n 
A 1 376 PHE 376 471 471 PHE PHE A . n 
A 1 377 THR 377 472 472 THR THR A . n 
A 1 378 TYR 378 473 473 TYR TYR A . n 
A 1 379 GLU 379 474 474 GLU GLU A . n 
A 1 380 GLU 380 475 475 GLU GLU A . n 
A 1 381 ALA 381 476 476 ALA ALA A . n 
A 1 382 ILE 382 477 477 ILE ILE A . n 
A 1 383 LYS 383 478 478 LYS LYS A . n 
A 1 384 MET 384 479 479 MET MET A . n 
A 1 385 LEU 385 480 480 LEU LEU A . n 
A 1 386 ILE 386 481 481 ILE ILE A . n 
A 1 387 GLN 387 482 482 GLN GLN A . n 
A 1 388 HIS 388 483 483 HIS HIS A . n 
A 1 389 GLY 389 484 484 GLY GLY A . n 
A 1 390 LYS 390 485 485 LYS LYS A . n 
A 1 391 LEU 391 486 486 LEU LEU A . n 
A 1 392 HIS 392 487 487 HIS HIS A . n 
A 1 393 LEU 393 488 488 LEU LEU A . n 
A 1 394 LYS 394 489 489 LYS LYS A . n 
A 1 395 GLU 395 490 490 GLU GLU A . n 
A 1 396 GLU 396 491 491 GLU GLU A . n 
A 1 397 GLU 397 492 492 GLU GLU A . n 
A 1 398 ILE 398 493 493 ILE ILE A . n 
A 1 399 LEU 399 494 494 LEU LEU A . n 
A 1 400 ALA 400 495 495 ALA ALA A . n 
A 1 401 TYR 401 496 496 TYR TYR A . n 
A 1 402 ASP 402 497 497 ASP ASP A . n 
A 1 403 MET 403 498 498 MET MET A . n 
A 1 404 SER 404 499 499 SER SER A . n 
A 1 405 THR 405 500 500 THR THR A . n 
A 1 406 ASP 406 501 501 ASP ASP A . n 
A 1 407 MET 407 502 502 MET MET A . n 
A 1 408 GLU 408 503 503 GLU GLU A . n 
A 1 409 LYS 409 504 504 LYS LYS A . n 
A 1 410 GLU 410 505 505 GLU GLU A . n 
A 1 411 LEU 411 506 506 LEU LEU A . n 
A 1 412 GLY 412 507 507 GLY GLY A . n 
A 1 413 LYS 413 508 508 LYS LYS A . n 
A 1 414 ILE 414 509 509 ILE ILE A . n 
A 1 415 VAL 415 510 510 VAL VAL A . n 
A 1 416 LYS 416 511 511 LYS LYS A . n 
A 1 417 ALA 417 512 512 ALA ALA A . n 
A 1 418 SER 418 513 513 SER SER A . n 
A 1 419 HIS 419 514 514 HIS HIS A . n 
A 1 420 HIS 420 515 515 HIS HIS A . n 
A 1 421 THR 421 516 516 THR THR A . n 
A 1 422 ASP 422 517 517 ASP ASP A . n 
A 1 423 TYR 423 518 518 TYR TYR A . n 
A 1 424 TYR 424 519 519 TYR TYR A . n 
A 1 425 ILE 425 520 520 ILE ILE A . n 
A 1 426 ILE 426 521 521 ILE ILE A . n 
A 1 427 ILE 427 522 522 ILE ILE A . n 
A 1 428 ASN 428 523 523 ASN ASN A . n 
A 1 429 PHE 429 524 524 PHE PHE A . n 
A 1 430 PRO 430 525 525 PRO PRO A . n 
A 1 431 SER 431 526 526 SER SER A . n 
A 1 432 ALA 432 527 527 ALA ALA A . n 
A 1 433 LEU 433 528 528 LEU LEU A . n 
A 1 434 ARG 434 529 529 ARG ARG A . n 
A 1 435 PRO 435 530 530 PRO PRO A . n 
A 1 436 PHE 436 531 531 PHE PHE A . n 
A 1 437 TYR 437 532 532 TYR TYR A . n 
A 1 438 THR 438 533 533 THR THR A . n 
A 1 439 MET 439 534 534 MET MET A . n 
A 1 440 TYR 440 535 535 TYR TYR A . n 
A 1 441 LYS 441 536 536 LYS LYS A . n 
A 1 442 GLU 442 537 537 GLU GLU A . n 
A 1 443 ASP 443 538 538 ASP ASP A . n 
A 1 444 GLU 444 539 539 GLU GLU A . n 
A 1 445 PRO 445 540 540 PRO PRO A . n 
A 1 446 ALA 446 541 541 ALA ALA A . n 
A 1 447 ILE 447 542 542 ILE ILE A . n 
A 1 448 SER 448 543 543 SER SER A . n 
A 1 449 ASN 449 544 544 ASN ASN A . n 
A 1 450 SER 450 545 545 SER SER A . n 
A 1 451 TYR 451 546 546 TYR TYR A . n 
A 1 452 ASP 452 547 547 ASP ASP A . n 
A 1 453 PHE 453 548 548 PHE PHE A . n 
A 1 454 PHE 454 549 549 PHE PHE A . n 
A 1 455 MET 455 550 550 MET MET A . n 
A 1 456 ARG 456 551 551 ARG ARG A . n 
A 1 457 GLY 457 552 552 GLY GLY A . n 
A 1 458 GLU 458 553 553 GLU GLU A . n 
A 1 459 GLU 459 554 554 GLU GLU A . n 
A 1 460 ILE 460 555 555 ILE ILE A . n 
A 1 461 LEU 461 556 556 LEU LEU A . n 
A 1 462 SER 462 557 557 SER SER A . n 
A 1 463 GLY 463 558 558 GLY GLY A . n 
A 1 464 SER 464 559 559 SER SER A . n 
A 1 465 GLN 465 560 560 GLN GLN A . n 
A 1 466 ARG 466 561 561 ARG ARG A . n 
A 1 467 ILE 467 562 562 ILE ILE A . n 
A 1 468 SER 468 563 563 SER SER A . n 
A 1 469 ASP 469 564 564 ASP ASP A . n 
A 1 470 VAL 470 565 565 VAL VAL A . n 
A 1 471 ASN 471 566 566 ASN ASN A . n 
A 1 472 LEU 472 567 567 LEU LEU A . n 
A 1 473 LEU 473 568 568 LEU LEU A . n 
A 1 474 LEU 474 569 569 LEU LEU A . n 
A 1 475 GLU 475 570 570 GLU GLU A . n 
A 1 476 ASN 476 571 571 ASN ASN A . n 
A 1 477 ILE 477 572 572 ILE ILE A . n 
A 1 478 LYS 478 573 573 LYS LYS A . n 
A 1 479 ARG 479 574 574 ARG ARG A . n 
A 1 480 PHE 480 575 575 PHE PHE A . n 
A 1 481 ASN 481 576 576 ASN ASN A . n 
A 1 482 LEU 482 577 577 LEU LEU A . n 
A 1 483 ASP 483 578 578 ASP ASP A . n 
A 1 484 ALA 484 579 579 ALA ALA A . n 
A 1 485 ASN 485 580 580 ASN ASN A . n 
A 1 486 LYS 486 581 581 LYS LYS A . n 
A 1 487 LEU 487 582 582 LEU LEU A . n 
A 1 488 ASN 488 583 583 ASN ASN A . n 
A 1 489 PHE 489 584 584 PHE PHE A . n 
A 1 490 TYR 490 585 585 TYR TYR A . n 
A 1 491 ILE 491 586 586 ILE ILE A . n 
A 1 492 ASP 492 587 587 ASP ASP A . n 
A 1 493 SER 493 588 588 SER SER A . n 
A 1 494 PHE 494 589 589 PHE PHE A . n 
A 1 495 ALA 495 590 590 ALA ALA A . n 
A 1 496 TYR 496 591 591 TYR TYR A . n 
A 1 497 SER 497 592 592 SER SER A . n 
A 1 498 SER 498 593 593 SER SER A . n 
A 1 499 TYR 499 594 594 TYR TYR A . n 
A 1 500 PRO 500 595 595 PRO PRO A . n 
A 1 501 HIS 501 596 596 HIS HIS A . n 
A 1 502 SER 502 597 597 SER SER A . n 
A 1 503 GLY 503 598 598 GLY GLY A . n 
A 1 504 CYS 504 599 599 CYS CYS A . n 
A 1 505 GLY 505 600 600 GLY GLY A . n 
A 1 506 ILE 506 601 601 ILE ILE A . n 
A 1 507 GLY 507 602 602 GLY GLY A . n 
A 1 508 LEU 508 603 603 LEU LEU A . n 
A 1 509 GLU 509 604 604 GLU GLU A . n 
A 1 510 ARG 510 605 605 ARG ARG A . n 
A 1 511 VAL 511 606 606 VAL VAL A . n 
A 1 512 LEU 512 607 607 LEU LEU A . n 
A 1 513 MET 513 608 608 MET MET A . n 
A 1 514 LEU 514 609 609 LEU LEU A . n 
A 1 515 PHE 515 610 610 PHE PHE A . n 
A 1 516 LEU 516 611 611 LEU LEU A . n 
A 1 517 GLY 517 612 612 GLY GLY A . n 
A 1 518 LEU 518 613 613 LEU LEU A . n 
A 1 519 ASN 519 614 614 ASN ASN A . n 
A 1 520 ASN 520 615 615 ASN ASN A . n 
A 1 521 ILE 521 616 616 ILE ILE A . n 
A 1 522 ARG 522 617 617 ARG ARG A . n 
A 1 523 LYS 523 618 618 LYS LYS A . n 
A 1 524 THR 524 619 619 THR THR A . n 
A 1 525 SER 525 620 620 SER SER A . n 
A 1 526 LEU 526 621 621 LEU LEU A . n 
A 1 527 PHE 527 622 622 PHE PHE A . n 
A 1 528 PRO 528 623 623 PRO PRO A . n 
A 1 529 ARG 529 624 624 ARG ARG A . n 
A 1 530 ASP 530 625 625 ASP ASP A . n 
A 1 531 PRO 531 626 626 PRO PRO A . n 
A 1 532 LYS 532 627 627 LYS LYS A . n 
A 1 533 ARG 533 628 628 ARG ARG A . n 
A 1 534 LEU 534 629 629 LEU LEU A . n 
A 1 535 ILE 535 630 630 ILE ILE A . n 
A 1 536 PRO 536 631 631 PRO PRO A . n 
B 1 1   ALA 1   96  ?   ?   ?   B . n 
B 1 2   GLU 2   97  ?   ?   ?   B . n 
B 1 3   ARG 3   98  ?   ?   ?   B . n 
B 1 4   GLU 4   99  ?   ?   ?   B . n 
B 1 5   ASN 5   100 100 ASN ASN B . n 
B 1 6   LEU 6   101 101 LEU LEU B . n 
B 1 7   LYS 7   102 102 LYS LYS B . n 
B 1 8   ASN 8   103 103 ASN ASN B . n 
B 1 9   GLU 9   104 104 GLU GLU B . n 
B 1 10  ALA 10  105 105 ALA ALA B . n 
B 1 11  THR 11  106 106 THR THR B . n 
B 1 12  LYS 12  107 107 LYS LYS B . n 
B 1 13  VAL 13  108 108 VAL VAL B . n 
B 1 14  LEU 14  109 109 LEU LEU B . n 
B 1 15  GLU 15  110 110 GLU GLU B . n 
B 1 16  HIS 16  111 111 HIS HIS B . n 
B 1 17  VAL 17  112 112 VAL VAL B . n 
B 1 18  CYS 18  113 113 CYS CYS B . n 
B 1 19  GLU 19  114 114 GLU GLU B . n 
B 1 20  ASP 20  115 115 ASP ASP B . n 
B 1 21  ILE 21  116 116 ILE ILE B . n 
B 1 22  ASN 22  117 117 ASN ASN B . n 
B 1 23  LYS 23  118 118 LYS LYS B . n 
B 1 24  GLU 24  119 119 GLU GLU B . n 
B 1 25  SER 25  120 120 SER SER B . n 
B 1 26  TYR 26  121 121 TYR TYR B . n 
B 1 27  GLY 27  122 122 GLY GLY B . n 
B 1 28  PHE 28  123 123 PHE PHE B . n 
B 1 29  VAL 29  124 124 VAL VAL B . n 
B 1 30  LYS 30  125 125 LYS LYS B . n 
B 1 31  ILE 31  126 126 ILE ILE B . n 
B 1 32  SER 32  127 127 SER SER B . n 
B 1 33  LYS 33  128 128 LYS LYS B . n 
B 1 34  MET 34  129 129 MET MET B . n 
B 1 35  LYS 35  130 130 LYS LYS B . n 
B 1 36  GLU 36  131 131 GLU GLU B . n 
B 1 37  ASN 37  132 132 ASN ASN B . n 
B 1 38  GLU 38  133 ?   ?   ?   B . n 
B 1 39  LYS 39  134 ?   ?   ?   B . n 
B 1 40  GLU 40  135 135 GLU GLU B . n 
B 1 41  ILE 41  136 136 ILE ILE B . n 
B 1 42  ARG 42  137 137 ARG ARG B . n 
B 1 43  LEU 43  138 138 LEU LEU B . n 
B 1 44  PHE 44  139 139 PHE PHE B . n 
B 1 45  ASN 45  140 140 ASN ASN B . n 
B 1 46  LEU 46  141 141 LEU LEU B . n 
B 1 47  GLU 47  142 142 GLU GLU B . n 
B 1 48  GLU 48  143 143 GLU GLU B . n 
B 1 49  ILE 49  144 144 ILE ILE B . n 
B 1 50  TYR 50  145 145 TYR TYR B . n 
B 1 51  HIS 51  146 146 HIS HIS B . n 
B 1 52  SER 52  147 147 SER SER B . n 
B 1 53  LEU 53  148 148 LEU LEU B . n 
B 1 54  MET 54  149 149 MET MET B . n 
B 1 55  LYS 55  150 ?   ?   ?   B . n 
B 1 56  VAL 56  151 ?   ?   ?   B . n 
B 1 57  GLY 57  152 ?   ?   ?   B . n 
B 1 58  GLY 58  153 ?   ?   ?   B . n 
B 1 59  SER 59  154 ?   ?   ?   B . n 
B 1 60  GLY 60  155 ?   ?   ?   B . n 
B 1 61  ALA 61  156 ?   ?   ?   B . n 
B 1 62  THR 62  157 ?   ?   ?   B . n 
B 1 63  ASP 63  158 ?   ?   ?   B . n 
B 1 64  GLY 64  159 ?   ?   ?   B . n 
B 1 65  GLY 65  160 ?   ?   ?   B . n 
B 1 66  LYS 66  161 ?   ?   ?   B . n 
B 1 67  ARG 67  162 ?   ?   ?   B . n 
B 1 68  GLU 68  163 ?   ?   ?   B . n 
B 1 69  ASP 69  164 ?   ?   ?   B . n 
B 1 70  ASP 70  165 ?   ?   ?   B . n 
B 1 71  ALA 71  166 ?   ?   ?   B . n 
B 1 72  ALA 72  167 ?   ?   ?   B . n 
B 1 73  SER 73  168 ?   ?   ?   B . n 
B 1 74  HIS 74  169 ?   ?   ?   B . n 
B 1 75  SER 75  170 ?   ?   ?   B . n 
B 1 76  VAL 76  171 ?   ?   ?   B . n 
B 1 77  VAL 77  172 ?   ?   ?   B . n 
B 1 78  ALA 78  173 ?   ?   ?   B . n 
B 1 79  GLU 79  174 ?   ?   ?   B . n 
B 1 80  SER 80  175 ?   ?   ?   B . n 
B 1 81  ASN 81  176 ?   ?   ?   B . n 
B 1 82  GLY 82  177 ?   ?   ?   B . n 
B 1 83  ALA 83  178 ?   ?   ?   B . n 
B 1 84  HIS 84  179 179 HIS HIS B . n 
B 1 85  LEU 85  180 180 LEU LEU B . n 
B 1 86  LEU 86  181 181 LEU LEU B . n 
B 1 87  GLN 87  182 182 GLN GLN B . n 
B 1 88  SER 88  183 183 SER SER B . n 
B 1 89  ASP 89  184 184 ASP ASP B . n 
B 1 90  ILE 90  185 185 ILE ILE B . n 
B 1 91  TRP 91  186 186 TRP TRP B . n 
B 1 92  VAL 92  187 187 VAL VAL B . n 
B 1 93  ARG 93  188 188 ARG ARG B . n 
B 1 94  GLY 94  189 189 GLY GLY B . n 
B 1 95  ARG 95  190 190 ARG ARG B . n 
B 1 96  ILE 96  191 191 ILE ILE B . n 
B 1 97  HIS 97  192 192 HIS HIS B . n 
B 1 98  ASP 98  193 193 ASP ASP B . n 
B 1 99  ILE 99  194 194 ILE ILE B . n 
B 1 100 ARG 100 195 195 ARG ARG B . n 
B 1 101 SER 101 196 196 SER SER B . n 
B 1 102 LYS 102 197 197 LYS LYS B . n 
B 1 103 GLY 103 198 198 GLY GLY B . n 
B 1 104 SER 104 199 199 SER SER B . n 
B 1 105 LEU 105 200 200 LEU LEU B . n 
B 1 106 ALA 106 201 201 ALA ALA B . n 
B 1 107 PHE 107 202 202 PHE PHE B . n 
B 1 108 ILE 108 203 203 ILE ILE B . n 
B 1 109 ILE 109 204 204 ILE ILE B . n 
B 1 110 LEU 110 205 205 LEU LEU B . n 
B 1 111 ARG 111 206 206 ARG ARG B . n 
B 1 112 HIS 112 207 207 HIS HIS B . n 
B 1 113 LYS 113 208 208 LYS LYS B . n 
B 1 114 LEU 114 209 209 LEU LEU B . n 
B 1 115 TYR 115 210 210 TYR TYR B . n 
B 1 116 SER 116 211 211 SER SER B . n 
B 1 117 MET 117 212 212 MET MET B . n 
B 1 118 GLN 118 213 213 GLN GLN B . n 
B 1 119 CYS 119 214 214 CYS CYS B . n 
B 1 120 ILE 120 215 215 ILE ILE B . n 
B 1 121 LEU 121 216 216 LEU LEU B . n 
B 1 122 ASP 122 217 217 ASP ASP B . n 
B 1 123 ILE 123 218 218 ILE ILE B . n 
B 1 124 LYS 124 219 219 LYS LYS B . n 
B 1 125 HIS 125 220 220 HIS HIS B . n 
B 1 126 ASN 126 221 221 ASN ASN B . n 
B 1 127 ASP 127 222 222 ASP ASP B . n 
B 1 128 ASN 128 223 223 ASN ASN B . n 
B 1 129 ASP 129 224 224 ASP ASP B . n 
B 1 130 LYS 130 225 225 LYS LYS B . n 
B 1 131 ASN 131 226 226 ASN ASN B . n 
B 1 132 MET 132 227 227 MET MET B . n 
B 1 133 MET 133 228 228 MET MET B . n 
B 1 134 LYS 134 229 229 LYS LYS B . n 
B 1 135 TRP 135 230 230 TRP TRP B . n 
B 1 136 VAL 136 231 231 VAL VAL B . n 
B 1 137 SER 137 232 232 SER SER B . n 
B 1 138 ASN 138 233 233 ASN ASN B . n 
B 1 139 LEU 139 234 234 LEU LEU B . n 
B 1 140 PRO 140 235 235 PRO PRO B . n 
B 1 141 LEU 141 236 236 LEU LEU B . n 
B 1 142 GLU 142 237 237 GLU GLU B . n 
B 1 143 SER 143 238 238 SER SER B . n 
B 1 144 ILE 144 239 239 ILE ILE B . n 
B 1 145 VAL 145 240 240 VAL VAL B . n 
B 1 146 ASP 146 241 241 ASP ASP B . n 
B 1 147 ILE 147 242 242 ILE ILE B . n 
B 1 148 LYS 148 243 243 LYS LYS B . n 
B 1 149 GLY 149 244 244 GLY GLY B . n 
B 1 150 LYS 150 245 245 LYS LYS B . n 
B 1 151 LEU 151 246 246 LEU LEU B . n 
B 1 152 SER 152 247 247 SER SER B . n 
B 1 153 LYS 153 248 248 LYS LYS B . n 
B 1 154 PRO 154 249 249 PRO PRO B . n 
B 1 155 GLU 155 250 250 GLU GLU B . n 
B 1 156 VAL 156 251 251 VAL VAL B . n 
B 1 157 PRO 157 252 252 PRO PRO B . n 
B 1 158 ILE 158 253 253 ILE ILE B . n 
B 1 159 ASP 159 254 254 ASP ASP B . n 
B 1 160 SER 160 255 255 SER SER B . n 
B 1 161 THR 161 256 256 THR THR B . n 
B 1 162 ASN 162 257 257 ASN ASN B . n 
B 1 163 ILE 163 258 258 ILE ILE B . n 
B 1 164 LYS 164 259 259 LYS LYS B . n 
B 1 165 TYR 165 260 260 TYR TYR B . n 
B 1 166 GLU 166 261 261 GLU GLU B . n 
B 1 167 ALA 167 262 262 ALA ALA B . n 
B 1 168 HIS 168 263 263 HIS HIS B . n 
B 1 169 ILE 169 264 264 ILE ILE B . n 
B 1 170 ARG 170 265 265 ARG ARG B . n 
B 1 171 LYS 171 266 266 LYS LYS B . n 
B 1 172 ILE 172 267 267 ILE ILE B . n 
B 1 173 PHE 173 268 268 PHE PHE B . n 
B 1 174 CYS 174 269 269 CYS CYS B . n 
B 1 175 ILE 175 270 270 ILE ILE B . n 
B 1 176 SER 176 271 271 SER SER B . n 
B 1 177 LYS 177 272 272 LYS LYS B . n 
B 1 178 THR 178 273 273 THR THR B . n 
B 1 179 ALA 179 274 274 ALA ALA B . n 
B 1 180 LYS 180 275 275 LYS LYS B . n 
B 1 181 GLU 181 276 276 GLU GLU B . n 
B 1 182 LEU 182 277 277 LEU LEU B . n 
B 1 183 PRO 183 278 278 PRO PRO B . n 
B 1 184 PHE 184 279 279 PHE PHE B . n 
B 1 185 LEU 185 280 280 LEU LEU B . n 
B 1 186 LEU 186 281 281 LEU LEU B . n 
B 1 187 LYS 187 282 282 LYS LYS B . n 
B 1 188 ASP 188 283 283 ASP ASP B . n 
B 1 189 ALA 189 284 284 ALA ALA B . n 
B 1 190 ASN 190 285 285 ASN ASN B . n 
B 1 191 MET 191 286 286 MET MET B . n 
B 1 192 LYS 192 287 287 LYS LYS B . n 
B 1 193 GLU 193 288 288 GLU GLU B . n 
B 1 194 THR 194 289 289 THR THR B . n 
B 1 195 ASN 195 290 290 ASN ASN B . n 
B 1 196 GLU 196 291 291 GLU GLU B . n 
B 1 197 GLU 197 292 292 GLU GLU B . n 
B 1 198 GLY 198 293 293 GLY GLY B . n 
B 1 199 SER 199 294 294 SER SER B . n 
B 1 200 ILE 200 295 295 ILE ILE B . n 
B 1 201 LYS 201 296 296 LYS LYS B . n 
B 1 202 VAL 202 297 297 VAL VAL B . n 
B 1 203 ASN 203 298 298 ASN ASN B . n 
B 1 204 GLN 204 299 299 GLN GLN B . n 
B 1 205 ASP 205 300 300 ASP ASP B . n 
B 1 206 ASN 206 301 301 ASN ASN B . n 
B 1 207 ARG 207 302 302 ARG ARG B . n 
B 1 208 LEU 208 303 303 LEU LEU B . n 
B 1 209 ASN 209 304 304 ASN ASN B . n 
B 1 210 ASN 210 305 305 ASN ASN B . n 
B 1 211 ARG 211 306 306 ARG ARG B . n 
B 1 212 CYS 212 307 307 CYS CYS B . n 
B 1 213 VAL 213 308 308 VAL VAL B . n 
B 1 214 ASP 214 309 309 ASP ASP B . n 
B 1 215 LEU 215 310 310 LEU LEU B . n 
B 1 216 ARG 216 311 311 ARG ARG B . n 
B 1 217 THR 217 312 312 THR THR B . n 
B 1 218 TYR 218 313 313 TYR TYR B . n 
B 1 219 ALA 219 314 314 ALA ALA B . n 
B 1 220 ASN 220 315 315 ASN ASN B . n 
B 1 221 TYR 221 316 316 TYR TYR B . n 
B 1 222 SER 222 317 317 SER SER B . n 
B 1 223 ILE 223 318 318 ILE ILE B . n 
B 1 224 PHE 224 319 319 PHE PHE B . n 
B 1 225 CYS 225 320 320 CYS CYS B . n 
B 1 226 LEU 226 321 321 LEU LEU B . n 
B 1 227 GLN 227 322 322 GLN GLN B . n 
B 1 228 SER 228 323 323 SER SER B . n 
B 1 229 GLN 229 324 324 GLN GLN B . n 
B 1 230 ILE 230 325 325 ILE ILE B . n 
B 1 231 CYS 231 326 326 CYS CYS B . n 
B 1 232 THR 232 327 327 THR THR B . n 
B 1 233 ILE 233 328 328 ILE ILE B . n 
B 1 234 PHE 234 329 329 PHE PHE B . n 
B 1 235 LYS 235 330 330 LYS LYS B . n 
B 1 236 ASN 236 331 331 ASN ASN B . n 
B 1 237 PHE 237 332 332 PHE PHE B . n 
B 1 238 LEU 238 333 333 LEU LEU B . n 
B 1 239 LEU 239 334 334 LEU LEU B . n 
B 1 240 GLU 240 335 335 GLU GLU B . n 
B 1 241 ASN 241 336 336 ASN ASN B . n 
B 1 242 ASN 242 337 337 ASN ASN B . n 
B 1 243 PHE 243 338 338 PHE PHE B . n 
B 1 244 ILE 244 339 339 ILE ILE B . n 
B 1 245 GLU 245 340 340 GLU GLU B . n 
B 1 246 ILE 246 341 341 ILE ILE B . n 
B 1 247 HIS 247 342 342 HIS HIS B . n 
B 1 248 THR 248 343 343 THR THR B . n 
B 1 249 PRO 249 344 344 PRO PRO B . n 
B 1 250 LYS 250 345 345 LYS LYS B . n 
B 1 251 LEU 251 346 346 LEU LEU B . n 
B 1 252 LEU 252 347 347 LEU LEU B . n 
B 1 253 GLY 253 348 348 GLY GLY B . n 
B 1 254 GLU 254 349 349 GLU GLU B . n 
B 1 255 SER 255 350 350 SER SER B . n 
B 1 256 SER 256 351 351 SER SER B . n 
B 1 257 GLU 257 352 352 GLU GLU B . n 
B 1 258 GLY 258 353 353 GLY GLY B . n 
B 1 259 GLY 259 354 354 GLY GLY B . n 
B 1 260 ALA 260 355 355 ALA ALA B . n 
B 1 261 ASN 261 356 356 ASN ASN B . n 
B 1 262 ALA 262 357 357 ALA ALA B . n 
B 1 263 PHE 263 358 358 PHE PHE B . n 
B 1 264 GLN 264 359 359 GLN GLN B . n 
B 1 265 ILE 265 360 360 ILE ILE B . n 
B 1 266 ASN 266 361 361 ASN ASN B . n 
B 1 267 TYR 267 362 362 TYR TYR B . n 
B 1 268 PHE 268 363 363 PHE PHE B . n 
B 1 269 ASN 269 364 364 ASN ASN B . n 
B 1 270 GLN 270 365 365 GLN GLN B . n 
B 1 271 LYS 271 366 366 LYS LYS B . n 
B 1 272 GLY 272 367 367 GLY GLY B . n 
B 1 273 PHE 273 368 368 PHE PHE B . n 
B 1 274 LEU 274 369 369 LEU LEU B . n 
B 1 275 ALA 275 370 370 ALA ALA B . n 
B 1 276 GLN 276 371 371 GLN GLN B . n 
B 1 277 SER 277 372 372 SER SER B . n 
B 1 278 PRO 278 373 373 PRO PRO B . n 
B 1 279 GLN 279 374 374 GLN GLN B . n 
B 1 280 LEU 280 375 375 LEU LEU B . n 
B 1 281 TYR 281 376 376 TYR TYR B . n 
B 1 282 LYS 282 377 377 LYS LYS B . n 
B 1 283 GLN 283 378 378 GLN GLN B . n 
B 1 284 MET 284 379 379 MET MET B . n 
B 1 285 CYS 285 380 380 CYS CYS B . n 
B 1 286 ILE 286 381 381 ILE ILE B . n 
B 1 287 ASN 287 382 382 ASN ASN B . n 
B 1 288 SER 288 383 383 SER SER B . n 
B 1 289 GLY 289 384 384 GLY GLY B . n 
B 1 290 PHE 290 385 385 PHE PHE B . n 
B 1 291 ASP 291 386 386 ASP ASP B . n 
B 1 292 ARG 292 387 387 ARG ARG B . n 
B 1 293 VAL 293 388 388 VAL VAL B . n 
B 1 294 PHE 294 389 389 PHE PHE B . n 
B 1 295 GLU 295 390 390 GLU GLU B . n 
B 1 296 VAL 296 391 391 VAL VAL B . n 
B 1 297 ALA 297 392 392 ALA ALA B . n 
B 1 298 PRO 298 393 393 PRO PRO B . n 
B 1 299 VAL 299 394 394 VAL VAL B . n 
B 1 300 PHE 300 395 395 PHE PHE B . n 
B 1 301 ARG 301 396 396 ARG ARG B . n 
B 1 302 ALA 302 397 397 ALA ALA B . n 
B 1 303 GLU 303 398 398 GLU GLU B . n 
B 1 304 ASN 304 399 399 ASN ASN B . n 
B 1 305 SER 305 400 400 SER SER B . n 
B 1 306 ASN 306 401 401 ASN ASN B . n 
B 1 307 THR 307 402 402 THR THR B . n 
B 1 308 TYR 308 403 403 TYR TYR B . n 
B 1 309 ARG 309 404 404 ARG ARG B . n 
B 1 310 HIS 310 405 405 HIS HIS B . n 
B 1 311 LEU 311 406 406 LEU LEU B . n 
B 1 312 CYS 312 407 407 CYS CYS B . n 
B 1 313 GLU 313 408 408 GLU GLU B . n 
B 1 314 TYR 314 409 409 TYR TYR B . n 
B 1 315 VAL 315 410 410 VAL VAL B . n 
B 1 316 SER 316 411 411 SER SER B . n 
B 1 317 LEU 317 412 412 LEU LEU B . n 
B 1 318 ASP 318 413 413 ASP ASP B . n 
B 1 319 VAL 319 414 414 VAL VAL B . n 
B 1 320 GLU 320 415 415 GLU GLU B . n 
B 1 321 MET 321 416 416 MET MET B . n 
B 1 322 THR 322 417 417 THR THR B . n 
B 1 323 TYR 323 418 418 TYR TYR B . n 
B 1 324 LYS 324 419 419 LYS LYS B . n 
B 1 325 TYR 325 420 420 TYR TYR B . n 
B 1 326 ASP 326 421 421 ASP ASP B . n 
B 1 327 TYR 327 422 422 TYR TYR B . n 
B 1 328 LEU 328 423 423 LEU LEU B . n 
B 1 329 GLU 329 424 424 GLU GLU B . n 
B 1 330 ASN 330 425 425 ASN ASN B . n 
B 1 331 VAL 331 426 426 VAL VAL B . n 
B 1 332 HIS 332 427 427 HIS HIS B . n 
B 1 333 PHE 333 428 428 PHE PHE B . n 
B 1 334 TYR 334 429 429 TYR TYR B . n 
B 1 335 ASP 335 430 430 ASP ASP B . n 
B 1 336 SER 336 431 431 SER SER B . n 
B 1 337 MET 337 432 432 MET MET B . n 
B 1 338 PHE 338 433 433 PHE PHE B . n 
B 1 339 LYS 339 434 434 LYS LYS B . n 
B 1 340 HIS 340 435 435 HIS HIS B . n 
B 1 341 ILE 341 436 436 ILE ILE B . n 
B 1 342 PHE 342 437 437 PHE PHE B . n 
B 1 343 THR 343 438 438 THR THR B . n 
B 1 344 GLU 344 439 439 GLU GLU B . n 
B 1 345 LEU 345 440 440 LEU LEU B . n 
B 1 346 SER 346 441 441 SER SER B . n 
B 1 347 LYS 347 442 442 LYS LYS B . n 
B 1 348 GLY 348 443 443 GLY GLY B . n 
B 1 349 GLY 349 444 444 GLY GLY B . n 
B 1 350 LYS 350 445 445 LYS LYS B . n 
B 1 351 ASN 351 446 446 ASN ASN B . n 
B 1 352 GLU 352 447 447 GLU GLU B . n 
B 1 353 MET 353 448 448 MET MET B . n 
B 1 354 LEU 354 449 449 LEU LEU B . n 
B 1 355 ILE 355 450 450 ILE ILE B . n 
B 1 356 LYS 356 451 451 LYS LYS B . n 
B 1 357 THR 357 452 452 THR THR B . n 
B 1 358 VAL 358 453 453 VAL VAL B . n 
B 1 359 LYS 359 454 454 LYS LYS B . n 
B 1 360 GLY 360 455 455 GLY GLY B . n 
B 1 361 GLN 361 456 456 GLN GLN B . n 
B 1 362 TYR 362 457 457 TYR TYR B . n 
B 1 363 PRO 363 458 458 PRO PRO B . n 
B 1 364 CYS 364 459 459 CYS CYS B . n 
B 1 365 GLU 365 460 460 GLU GLU B . n 
B 1 366 ASP 366 461 461 ASP ASP B . n 
B 1 367 PHE 367 462 462 PHE PHE B . n 
B 1 368 GLN 368 463 463 GLN GLN B . n 
B 1 369 TRP 369 464 464 TRP TRP B . n 
B 1 370 LEU 370 465 465 LEU LEU B . n 
B 1 371 GLU 371 466 466 GLU GLU B . n 
B 1 372 GLU 372 467 467 GLU GLU B . n 
B 1 373 THR 373 468 468 THR THR B . n 
B 1 374 PRO 374 469 469 PRO PRO B . n 
B 1 375 ILE 375 470 470 ILE ILE B . n 
B 1 376 PHE 376 471 471 PHE PHE B . n 
B 1 377 THR 377 472 472 THR THR B . n 
B 1 378 TYR 378 473 473 TYR TYR B . n 
B 1 379 GLU 379 474 474 GLU GLU B . n 
B 1 380 GLU 380 475 475 GLU GLU B . n 
B 1 381 ALA 381 476 476 ALA ALA B . n 
B 1 382 ILE 382 477 477 ILE ILE B . n 
B 1 383 LYS 383 478 478 LYS LYS B . n 
B 1 384 MET 384 479 479 MET MET B . n 
B 1 385 LEU 385 480 480 LEU LEU B . n 
B 1 386 ILE 386 481 481 ILE ILE B . n 
B 1 387 GLN 387 482 482 GLN GLN B . n 
B 1 388 HIS 388 483 483 HIS HIS B . n 
B 1 389 GLY 389 484 484 GLY GLY B . n 
B 1 390 LYS 390 485 485 LYS LYS B . n 
B 1 391 LEU 391 486 486 LEU LEU B . n 
B 1 392 HIS 392 487 487 HIS HIS B . n 
B 1 393 LEU 393 488 488 LEU LEU B . n 
B 1 394 LYS 394 489 489 LYS LYS B . n 
B 1 395 GLU 395 490 490 GLU GLU B . n 
B 1 396 GLU 396 491 491 GLU GLU B . n 
B 1 397 GLU 397 492 492 GLU GLU B . n 
B 1 398 ILE 398 493 493 ILE ILE B . n 
B 1 399 LEU 399 494 494 LEU LEU B . n 
B 1 400 ALA 400 495 495 ALA ALA B . n 
B 1 401 TYR 401 496 496 TYR TYR B . n 
B 1 402 ASP 402 497 497 ASP ASP B . n 
B 1 403 MET 403 498 498 MET MET B . n 
B 1 404 SER 404 499 499 SER SER B . n 
B 1 405 THR 405 500 500 THR THR B . n 
B 1 406 ASP 406 501 501 ASP ASP B . n 
B 1 407 MET 407 502 502 MET MET B . n 
B 1 408 GLU 408 503 503 GLU GLU B . n 
B 1 409 LYS 409 504 504 LYS LYS B . n 
B 1 410 GLU 410 505 505 GLU GLU B . n 
B 1 411 LEU 411 506 506 LEU LEU B . n 
B 1 412 GLY 412 507 507 GLY GLY B . n 
B 1 413 LYS 413 508 508 LYS LYS B . n 
B 1 414 ILE 414 509 509 ILE ILE B . n 
B 1 415 VAL 415 510 510 VAL VAL B . n 
B 1 416 LYS 416 511 511 LYS LYS B . n 
B 1 417 ALA 417 512 512 ALA ALA B . n 
B 1 418 SER 418 513 513 SER SER B . n 
B 1 419 HIS 419 514 514 HIS HIS B . n 
B 1 420 HIS 420 515 515 HIS HIS B . n 
B 1 421 THR 421 516 516 THR THR B . n 
B 1 422 ASP 422 517 517 ASP ASP B . n 
B 1 423 TYR 423 518 518 TYR TYR B . n 
B 1 424 TYR 424 519 519 TYR TYR B . n 
B 1 425 ILE 425 520 520 ILE ILE B . n 
B 1 426 ILE 426 521 521 ILE ILE B . n 
B 1 427 ILE 427 522 522 ILE ILE B . n 
B 1 428 ASN 428 523 523 ASN ASN B . n 
B 1 429 PHE 429 524 524 PHE PHE B . n 
B 1 430 PRO 430 525 525 PRO PRO B . n 
B 1 431 SER 431 526 526 SER SER B . n 
B 1 432 ALA 432 527 527 ALA ALA B . n 
B 1 433 LEU 433 528 528 LEU LEU B . n 
B 1 434 ARG 434 529 529 ARG ARG B . n 
B 1 435 PRO 435 530 530 PRO PRO B . n 
B 1 436 PHE 436 531 531 PHE PHE B . n 
B 1 437 TYR 437 532 532 TYR TYR B . n 
B 1 438 THR 438 533 533 THR THR B . n 
B 1 439 MET 439 534 534 MET MET B . n 
B 1 440 TYR 440 535 535 TYR TYR B . n 
B 1 441 LYS 441 536 536 LYS LYS B . n 
B 1 442 GLU 442 537 537 GLU GLU B . n 
B 1 443 ASP 443 538 538 ASP ASP B . n 
B 1 444 GLU 444 539 539 GLU GLU B . n 
B 1 445 PRO 445 540 540 PRO PRO B . n 
B 1 446 ALA 446 541 541 ALA ALA B . n 
B 1 447 ILE 447 542 542 ILE ILE B . n 
B 1 448 SER 448 543 543 SER SER B . n 
B 1 449 ASN 449 544 544 ASN ASN B . n 
B 1 450 SER 450 545 545 SER SER B . n 
B 1 451 TYR 451 546 546 TYR TYR B . n 
B 1 452 ASP 452 547 547 ASP ASP B . n 
B 1 453 PHE 453 548 548 PHE PHE B . n 
B 1 454 PHE 454 549 549 PHE PHE B . n 
B 1 455 MET 455 550 550 MET MET B . n 
B 1 456 ARG 456 551 551 ARG ARG B . n 
B 1 457 GLY 457 552 552 GLY GLY B . n 
B 1 458 GLU 458 553 553 GLU GLU B . n 
B 1 459 GLU 459 554 554 GLU GLU B . n 
B 1 460 ILE 460 555 555 ILE ILE B . n 
B 1 461 LEU 461 556 556 LEU LEU B . n 
B 1 462 SER 462 557 557 SER SER B . n 
B 1 463 GLY 463 558 558 GLY GLY B . n 
B 1 464 SER 464 559 559 SER SER B . n 
B 1 465 GLN 465 560 560 GLN GLN B . n 
B 1 466 ARG 466 561 561 ARG ARG B . n 
B 1 467 ILE 467 562 562 ILE ILE B . n 
B 1 468 SER 468 563 563 SER SER B . n 
B 1 469 ASP 469 564 564 ASP ASP B . n 
B 1 470 VAL 470 565 565 VAL VAL B . n 
B 1 471 ASN 471 566 566 ASN ASN B . n 
B 1 472 LEU 472 567 567 LEU LEU B . n 
B 1 473 LEU 473 568 568 LEU LEU B . n 
B 1 474 LEU 474 569 569 LEU LEU B . n 
B 1 475 GLU 475 570 570 GLU GLU B . n 
B 1 476 ASN 476 571 571 ASN ASN B . n 
B 1 477 ILE 477 572 572 ILE ILE B . n 
B 1 478 LYS 478 573 573 LYS LYS B . n 
B 1 479 ARG 479 574 574 ARG ARG B . n 
B 1 480 PHE 480 575 575 PHE PHE B . n 
B 1 481 ASN 481 576 576 ASN ASN B . n 
B 1 482 LEU 482 577 577 LEU LEU B . n 
B 1 483 ASP 483 578 578 ASP ASP B . n 
B 1 484 ALA 484 579 579 ALA ALA B . n 
B 1 485 ASN 485 580 580 ASN ASN B . n 
B 1 486 LYS 486 581 581 LYS LYS B . n 
B 1 487 LEU 487 582 582 LEU LEU B . n 
B 1 488 ASN 488 583 583 ASN ASN B . n 
B 1 489 PHE 489 584 584 PHE PHE B . n 
B 1 490 TYR 490 585 585 TYR TYR B . n 
B 1 491 ILE 491 586 586 ILE ILE B . n 
B 1 492 ASP 492 587 587 ASP ASP B . n 
B 1 493 SER 493 588 588 SER SER B . n 
B 1 494 PHE 494 589 589 PHE PHE B . n 
B 1 495 ALA 495 590 590 ALA ALA B . n 
B 1 496 TYR 496 591 591 TYR TYR B . n 
B 1 497 SER 497 592 592 SER SER B . n 
B 1 498 SER 498 593 593 SER SER B . n 
B 1 499 TYR 499 594 594 TYR TYR B . n 
B 1 500 PRO 500 595 595 PRO PRO B . n 
B 1 501 HIS 501 596 596 HIS HIS B . n 
B 1 502 SER 502 597 597 SER SER B . n 
B 1 503 GLY 503 598 598 GLY GLY B . n 
B 1 504 CYS 504 599 599 CYS CYS B . n 
B 1 505 GLY 505 600 600 GLY GLY B . n 
B 1 506 ILE 506 601 601 ILE ILE B . n 
B 1 507 GLY 507 602 602 GLY GLY B . n 
B 1 508 LEU 508 603 603 LEU LEU B . n 
B 1 509 GLU 509 604 604 GLU GLU B . n 
B 1 510 ARG 510 605 605 ARG ARG B . n 
B 1 511 VAL 511 606 606 VAL VAL B . n 
B 1 512 LEU 512 607 607 LEU LEU B . n 
B 1 513 MET 513 608 608 MET MET B . n 
B 1 514 LEU 514 609 609 LEU LEU B . n 
B 1 515 PHE 515 610 610 PHE PHE B . n 
B 1 516 LEU 516 611 611 LEU LEU B . n 
B 1 517 GLY 517 612 612 GLY GLY B . n 
B 1 518 LEU 518 613 613 LEU LEU B . n 
B 1 519 ASN 519 614 614 ASN ASN B . n 
B 1 520 ASN 520 615 615 ASN ASN B . n 
B 1 521 ILE 521 616 616 ILE ILE B . n 
B 1 522 ARG 522 617 617 ARG ARG B . n 
B 1 523 LYS 523 618 618 LYS LYS B . n 
B 1 524 THR 524 619 619 THR THR B . n 
B 1 525 SER 525 620 620 SER SER B . n 
B 1 526 LEU 526 621 621 LEU LEU B . n 
B 1 527 PHE 527 622 622 PHE PHE B . n 
B 1 528 PRO 528 623 623 PRO PRO B . n 
B 1 529 ARG 529 624 624 ARG ARG B . n 
B 1 530 ASP 530 625 625 ASP ASP B . n 
B 1 531 PRO 531 626 626 PRO PRO B . n 
B 1 532 LYS 532 627 627 LYS LYS B . n 
B 1 533 ARG 533 628 628 ARG ARG B . n 
B 1 534 LEU 534 629 629 LEU LEU B . n 
B 1 535 ILE 535 630 630 ILE ILE B . n 
B 1 536 PRO 536 631 631 PRO PRO B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 EDO ? ? EDO ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SO4 ? ? SO4 ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1   701  701 SO4 SO4 A . 
D 3 EDO 1   702  702 EDO EDO A . 
E 2 SO4 1   703  703 SO4 SO4 A . 
F 2 SO4 1   704  704 SO4 SO4 A . 
G 2 SO4 1   701  701 SO4 SO4 B . 
H 3 EDO 1   702  702 EDO EDO B . 
I 4 HOH 1   801  262 HOH HOH A . 
I 4 HOH 2   802  87  HOH HOH A . 
I 4 HOH 3   803  473 HOH HOH A . 
I 4 HOH 4   804  203 HOH HOH A . 
I 4 HOH 5   805  205 HOH HOH A . 
I 4 HOH 6   806  119 HOH HOH A . 
I 4 HOH 7   807  457 HOH HOH A . 
I 4 HOH 8   808  294 HOH HOH A . 
I 4 HOH 9   809  145 HOH HOH A . 
I 4 HOH 10  810  247 HOH HOH A . 
I 4 HOH 11  811  449 HOH HOH A . 
I 4 HOH 12  812  350 HOH HOH A . 
I 4 HOH 13  813  73  HOH HOH A . 
I 4 HOH 14  814  7   HOH HOH A . 
I 4 HOH 15  815  440 HOH HOH A . 
I 4 HOH 16  816  424 HOH HOH A . 
I 4 HOH 17  817  442 HOH HOH A . 
I 4 HOH 18  818  64  HOH HOH A . 
I 4 HOH 19  819  276 HOH HOH A . 
I 4 HOH 20  820  188 HOH HOH A . 
I 4 HOH 21  821  81  HOH HOH A . 
I 4 HOH 22  822  289 HOH HOH A . 
I 4 HOH 23  823  277 HOH HOH A . 
I 4 HOH 24  824  124 HOH HOH A . 
I 4 HOH 25  825  459 HOH HOH A . 
I 4 HOH 26  826  90  HOH HOH A . 
I 4 HOH 27  827  332 HOH HOH A . 
I 4 HOH 28  828  210 HOH HOH A . 
I 4 HOH 29  829  401 HOH HOH A . 
I 4 HOH 30  830  156 HOH HOH A . 
I 4 HOH 31  831  31  HOH HOH A . 
I 4 HOH 32  832  109 HOH HOH A . 
I 4 HOH 33  833  333 HOH HOH A . 
I 4 HOH 34  834  91  HOH HOH A . 
I 4 HOH 35  835  99  HOH HOH A . 
I 4 HOH 36  836  21  HOH HOH A . 
I 4 HOH 37  837  358 HOH HOH A . 
I 4 HOH 38  838  232 HOH HOH A . 
I 4 HOH 39  839  12  HOH HOH A . 
I 4 HOH 40  840  218 HOH HOH A . 
I 4 HOH 41  841  89  HOH HOH A . 
I 4 HOH 42  842  240 HOH HOH A . 
I 4 HOH 43  843  162 HOH HOH A . 
I 4 HOH 44  844  106 HOH HOH A . 
I 4 HOH 45  845  67  HOH HOH A . 
I 4 HOH 46  846  280 HOH HOH A . 
I 4 HOH 47  847  310 HOH HOH A . 
I 4 HOH 48  848  14  HOH HOH A . 
I 4 HOH 49  849  394 HOH HOH A . 
I 4 HOH 50  850  131 HOH HOH A . 
I 4 HOH 51  851  42  HOH HOH A . 
I 4 HOH 52  852  352 HOH HOH A . 
I 4 HOH 53  853  158 HOH HOH A . 
I 4 HOH 54  854  239 HOH HOH A . 
I 4 HOH 55  855  309 HOH HOH A . 
I 4 HOH 56  856  274 HOH HOH A . 
I 4 HOH 57  857  184 HOH HOH A . 
I 4 HOH 58  858  201 HOH HOH A . 
I 4 HOH 59  859  54  HOH HOH A . 
I 4 HOH 60  860  103 HOH HOH A . 
I 4 HOH 61  861  161 HOH HOH A . 
I 4 HOH 62  862  32  HOH HOH A . 
I 4 HOH 63  863  34  HOH HOH A . 
I 4 HOH 64  864  13  HOH HOH A . 
I 4 HOH 65  865  115 HOH HOH A . 
I 4 HOH 66  866  50  HOH HOH A . 
I 4 HOH 67  867  118 HOH HOH A . 
I 4 HOH 68  868  361 HOH HOH A . 
I 4 HOH 69  869  20  HOH HOH A . 
I 4 HOH 70  870  65  HOH HOH A . 
I 4 HOH 71  871  45  HOH HOH A . 
I 4 HOH 72  872  169 HOH HOH A . 
I 4 HOH 73  873  411 HOH HOH A . 
I 4 HOH 74  874  408 HOH HOH A . 
I 4 HOH 75  875  266 HOH HOH A . 
I 4 HOH 76  876  347 HOH HOH A . 
I 4 HOH 77  877  69  HOH HOH A . 
I 4 HOH 78  878  97  HOH HOH A . 
I 4 HOH 79  879  43  HOH HOH A . 
I 4 HOH 80  880  182 HOH HOH A . 
I 4 HOH 81  881  107 HOH HOH A . 
I 4 HOH 82  882  221 HOH HOH A . 
I 4 HOH 83  883  56  HOH HOH A . 
I 4 HOH 84  884  16  HOH HOH A . 
I 4 HOH 85  885  24  HOH HOH A . 
I 4 HOH 86  886  486 HOH HOH A . 
I 4 HOH 87  887  58  HOH HOH A . 
I 4 HOH 88  888  436 HOH HOH A . 
I 4 HOH 89  889  146 HOH HOH A . 
I 4 HOH 90  890  76  HOH HOH A . 
I 4 HOH 91  891  40  HOH HOH A . 
I 4 HOH 92  892  209 HOH HOH A . 
I 4 HOH 93  893  192 HOH HOH A . 
I 4 HOH 94  894  479 HOH HOH A . 
I 4 HOH 95  895  127 HOH HOH A . 
I 4 HOH 96  896  179 HOH HOH A . 
I 4 HOH 97  897  86  HOH HOH A . 
I 4 HOH 98  898  451 HOH HOH A . 
I 4 HOH 99  899  427 HOH HOH A . 
I 4 HOH 100 900  198 HOH HOH A . 
I 4 HOH 101 901  195 HOH HOH A . 
I 4 HOH 102 902  52  HOH HOH A . 
I 4 HOH 103 903  137 HOH HOH A . 
I 4 HOH 104 904  63  HOH HOH A . 
I 4 HOH 105 905  228 HOH HOH A . 
I 4 HOH 106 906  291 HOH HOH A . 
I 4 HOH 107 907  61  HOH HOH A . 
I 4 HOH 108 908  186 HOH HOH A . 
I 4 HOH 109 909  285 HOH HOH A . 
I 4 HOH 110 910  269 HOH HOH A . 
I 4 HOH 111 911  254 HOH HOH A . 
I 4 HOH 112 912  5   HOH HOH A . 
I 4 HOH 113 913  241 HOH HOH A . 
I 4 HOH 114 914  301 HOH HOH A . 
I 4 HOH 115 915  362 HOH HOH A . 
I 4 HOH 116 916  120 HOH HOH A . 
I 4 HOH 117 917  23  HOH HOH A . 
I 4 HOH 118 918  452 HOH HOH A . 
I 4 HOH 119 919  151 HOH HOH A . 
I 4 HOH 120 920  204 HOH HOH A . 
I 4 HOH 121 921  28  HOH HOH A . 
I 4 HOH 122 922  326 HOH HOH A . 
I 4 HOH 123 923  208 HOH HOH A . 
I 4 HOH 124 924  51  HOH HOH A . 
I 4 HOH 125 925  57  HOH HOH A . 
I 4 HOH 126 926  348 HOH HOH A . 
I 4 HOH 127 927  292 HOH HOH A . 
I 4 HOH 128 928  321 HOH HOH A . 
I 4 HOH 129 929  433 HOH HOH A . 
I 4 HOH 130 930  404 HOH HOH A . 
I 4 HOH 131 931  176 HOH HOH A . 
I 4 HOH 132 932  191 HOH HOH A . 
I 4 HOH 133 933  298 HOH HOH A . 
I 4 HOH 134 934  410 HOH HOH A . 
I 4 HOH 135 935  282 HOH HOH A . 
I 4 HOH 136 936  185 HOH HOH A . 
I 4 HOH 137 937  430 HOH HOH A . 
I 4 HOH 138 938  288 HOH HOH A . 
I 4 HOH 139 939  130 HOH HOH A . 
I 4 HOH 140 940  295 HOH HOH A . 
I 4 HOH 141 941  46  HOH HOH A . 
I 4 HOH 142 942  148 HOH HOH A . 
I 4 HOH 143 943  96  HOH HOH A . 
I 4 HOH 144 944  287 HOH HOH A . 
I 4 HOH 145 945  187 HOH HOH A . 
I 4 HOH 146 946  122 HOH HOH A . 
I 4 HOH 147 947  405 HOH HOH A . 
I 4 HOH 148 948  215 HOH HOH A . 
I 4 HOH 149 949  415 HOH HOH A . 
I 4 HOH 150 950  264 HOH HOH A . 
I 4 HOH 151 951  167 HOH HOH A . 
I 4 HOH 152 952  389 HOH HOH A . 
I 4 HOH 153 953  101 HOH HOH A . 
I 4 HOH 154 954  125 HOH HOH A . 
I 4 HOH 155 955  47  HOH HOH A . 
I 4 HOH 156 956  278 HOH HOH A . 
I 4 HOH 157 957  194 HOH HOH A . 
I 4 HOH 158 958  134 HOH HOH A . 
I 4 HOH 159 959  458 HOH HOH A . 
I 4 HOH 160 960  180 HOH HOH A . 
I 4 HOH 161 961  315 HOH HOH A . 
I 4 HOH 162 962  432 HOH HOH A . 
I 4 HOH 163 963  489 HOH HOH A . 
I 4 HOH 164 964  279 HOH HOH A . 
I 4 HOH 165 965  268 HOH HOH A . 
I 4 HOH 166 966  245 HOH HOH A . 
I 4 HOH 167 967  425 HOH HOH A . 
I 4 HOH 168 968  438 HOH HOH A . 
I 4 HOH 169 969  308 HOH HOH A . 
I 4 HOH 170 970  339 HOH HOH A . 
I 4 HOH 171 971  219 HOH HOH A . 
I 4 HOH 172 972  445 HOH HOH A . 
I 4 HOH 173 973  460 HOH HOH A . 
I 4 HOH 174 974  129 HOH HOH A . 
I 4 HOH 175 975  354 HOH HOH A . 
I 4 HOH 176 976  267 HOH HOH A . 
I 4 HOH 177 977  297 HOH HOH A . 
I 4 HOH 178 978  414 HOH HOH A . 
I 4 HOH 179 979  461 HOH HOH A . 
I 4 HOH 180 980  175 HOH HOH A . 
I 4 HOH 181 981  211 HOH HOH A . 
I 4 HOH 182 982  257 HOH HOH A . 
I 4 HOH 183 983  472 HOH HOH A . 
I 4 HOH 184 984  453 HOH HOH A . 
I 4 HOH 185 985  323 HOH HOH A . 
I 4 HOH 186 986  388 HOH HOH A . 
I 4 HOH 187 987  357 HOH HOH A . 
I 4 HOH 188 988  230 HOH HOH A . 
I 4 HOH 189 989  477 HOH HOH A . 
I 4 HOH 190 990  327 HOH HOH A . 
I 4 HOH 191 991  403 HOH HOH A . 
I 4 HOH 192 992  491 HOH HOH A . 
I 4 HOH 193 993  160 HOH HOH A . 
I 4 HOH 194 994  346 HOH HOH A . 
I 4 HOH 195 995  281 HOH HOH A . 
I 4 HOH 196 996  140 HOH HOH A . 
I 4 HOH 197 997  359 HOH HOH A . 
I 4 HOH 198 998  249 HOH HOH A . 
I 4 HOH 199 999  470 HOH HOH A . 
I 4 HOH 200 1000 409 HOH HOH A . 
I 4 HOH 201 1001 222 HOH HOH A . 
I 4 HOH 202 1002 416 HOH HOH A . 
I 4 HOH 203 1003 324 HOH HOH A . 
I 4 HOH 204 1004 353 HOH HOH A . 
I 4 HOH 205 1005 406 HOH HOH A . 
I 4 HOH 206 1006 412 HOH HOH A . 
I 4 HOH 207 1007 431 HOH HOH A . 
I 4 HOH 208 1008 300 HOH HOH A . 
I 4 HOH 209 1009 372 HOH HOH A . 
I 4 HOH 210 1010 260 HOH HOH A . 
I 4 HOH 211 1011 407 HOH HOH A . 
I 4 HOH 212 1012 193 HOH HOH A . 
I 4 HOH 213 1013 428 HOH HOH A . 
I 4 HOH 214 1014 303 HOH HOH A . 
I 4 HOH 215 1015 360 HOH HOH A . 
I 4 HOH 216 1016 320 HOH HOH A . 
I 4 HOH 217 1017 224 HOH HOH A . 
I 4 HOH 218 1018 351 HOH HOH A . 
I 4 HOH 219 1019 329 HOH HOH A . 
I 4 HOH 220 1020 417 HOH HOH A . 
I 4 HOH 221 1021 330 HOH HOH A . 
I 4 HOH 222 1022 170 HOH HOH A . 
I 4 HOH 223 1023 423 HOH HOH A . 
I 4 HOH 224 1024 272 HOH HOH A . 
I 4 HOH 225 1025 306 HOH HOH A . 
I 4 HOH 226 1026 108 HOH HOH A . 
I 4 HOH 227 1027 143 HOH HOH A . 
I 4 HOH 228 1028 391 HOH HOH A . 
I 4 HOH 229 1029 422 HOH HOH A . 
I 4 HOH 230 1030 304 HOH HOH A . 
I 4 HOH 231 1031 467 HOH HOH A . 
I 4 HOH 232 1032 331 HOH HOH A . 
I 4 HOH 233 1033 325 HOH HOH A . 
I 4 HOH 234 1034 490 HOH HOH A . 
I 4 HOH 235 1035 392 HOH HOH A . 
I 4 HOH 236 1036 213 HOH HOH A . 
I 4 HOH 237 1037 476 HOH HOH A . 
I 4 HOH 238 1038 393 HOH HOH A . 
I 4 HOH 239 1039 322 HOH HOH A . 
I 4 HOH 240 1040 286 HOH HOH A . 
I 4 HOH 241 1041 270 HOH HOH A . 
J 4 HOH 1   801  111 HOH HOH B . 
J 4 HOH 2   802  474 HOH HOH B . 
J 4 HOH 3   803  84  HOH HOH B . 
J 4 HOH 4   804  164 HOH HOH B . 
J 4 HOH 5   805  147 HOH HOH B . 
J 4 HOH 6   806  206 HOH HOH B . 
J 4 HOH 7   807  35  HOH HOH B . 
J 4 HOH 8   808  77  HOH HOH B . 
J 4 HOH 9   809  441 HOH HOH B . 
J 4 HOH 10  810  114 HOH HOH B . 
J 4 HOH 11  811  340 HOH HOH B . 
J 4 HOH 12  812  189 HOH HOH B . 
J 4 HOH 13  813  104 HOH HOH B . 
J 4 HOH 14  814  443 HOH HOH B . 
J 4 HOH 15  815  44  HOH HOH B . 
J 4 HOH 16  816  250 HOH HOH B . 
J 4 HOH 17  817  256 HOH HOH B . 
J 4 HOH 18  818  273 HOH HOH B . 
J 4 HOH 19  819  335 HOH HOH B . 
J 4 HOH 20  820  80  HOH HOH B . 
J 4 HOH 21  821  488 HOH HOH B . 
J 4 HOH 22  822  420 HOH HOH B . 
J 4 HOH 23  823  275 HOH HOH B . 
J 4 HOH 24  824  217 HOH HOH B . 
J 4 HOH 25  825  135 HOH HOH B . 
J 4 HOH 26  826  88  HOH HOH B . 
J 4 HOH 27  827  181 HOH HOH B . 
J 4 HOH 28  828  66  HOH HOH B . 
J 4 HOH 29  829  307 HOH HOH B . 
J 4 HOH 30  830  468 HOH HOH B . 
J 4 HOH 31  831  100 HOH HOH B . 
J 4 HOH 32  832  93  HOH HOH B . 
J 4 HOH 33  833  398 HOH HOH B . 
J 4 HOH 34  834  382 HOH HOH B . 
J 4 HOH 35  835  229 HOH HOH B . 
J 4 HOH 36  836  480 HOH HOH B . 
J 4 HOH 37  837  53  HOH HOH B . 
J 4 HOH 38  838  183 HOH HOH B . 
J 4 HOH 39  839  8   HOH HOH B . 
J 4 HOH 40  840  142 HOH HOH B . 
J 4 HOH 41  841  75  HOH HOH B . 
J 4 HOH 42  842  465 HOH HOH B . 
J 4 HOH 43  843  462 HOH HOH B . 
J 4 HOH 44  844  1   HOH HOH B . 
J 4 HOH 45  845  202 HOH HOH B . 
J 4 HOH 46  846  157 HOH HOH B . 
J 4 HOH 47  847  172 HOH HOH B . 
J 4 HOH 48  848  92  HOH HOH B . 
J 4 HOH 49  849  39  HOH HOH B . 
J 4 HOH 50  850  429 HOH HOH B . 
J 4 HOH 51  851  94  HOH HOH B . 
J 4 HOH 52  852  236 HOH HOH B . 
J 4 HOH 53  853  379 HOH HOH B . 
J 4 HOH 54  854  105 HOH HOH B . 
J 4 HOH 55  855  419 HOH HOH B . 
J 4 HOH 56  856  26  HOH HOH B . 
J 4 HOH 57  857  466 HOH HOH B . 
J 4 HOH 58  858  395 HOH HOH B . 
J 4 HOH 59  859  68  HOH HOH B . 
J 4 HOH 60  860  18  HOH HOH B . 
J 4 HOH 61  861  49  HOH HOH B . 
J 4 HOH 62  862  261 HOH HOH B . 
J 4 HOH 63  863  159 HOH HOH B . 
J 4 HOH 64  864  155 HOH HOH B . 
J 4 HOH 65  865  381 HOH HOH B . 
J 4 HOH 66  866  207 HOH HOH B . 
J 4 HOH 67  867  83  HOH HOH B . 
J 4 HOH 68  868  82  HOH HOH B . 
J 4 HOH 69  869  9   HOH HOH B . 
J 4 HOH 70  870  132 HOH HOH B . 
J 4 HOH 71  871  85  HOH HOH B . 
J 4 HOH 72  872  72  HOH HOH B . 
J 4 HOH 73  873  178 HOH HOH B . 
J 4 HOH 74  874  60  HOH HOH B . 
J 4 HOH 75  875  139 HOH HOH B . 
J 4 HOH 76  876  344 HOH HOH B . 
J 4 HOH 77  877  41  HOH HOH B . 
J 4 HOH 78  878  102 HOH HOH B . 
J 4 HOH 79  879  150 HOH HOH B . 
J 4 HOH 80  880  27  HOH HOH B . 
J 4 HOH 81  881  385 HOH HOH B . 
J 4 HOH 82  882  15  HOH HOH B . 
J 4 HOH 83  883  78  HOH HOH B . 
J 4 HOH 84  884  166 HOH HOH B . 
J 4 HOH 85  885  3   HOH HOH B . 
J 4 HOH 86  886  110 HOH HOH B . 
J 4 HOH 87  887  284 HOH HOH B . 
J 4 HOH 88  888  74  HOH HOH B . 
J 4 HOH 89  889  17  HOH HOH B . 
J 4 HOH 90  890  112 HOH HOH B . 
J 4 HOH 91  891  2   HOH HOH B . 
J 4 HOH 92  892  200 HOH HOH B . 
J 4 HOH 93  893  263 HOH HOH B . 
J 4 HOH 94  894  138 HOH HOH B . 
J 4 HOH 95  895  38  HOH HOH B . 
J 4 HOH 96  896  33  HOH HOH B . 
J 4 HOH 97  897  11  HOH HOH B . 
J 4 HOH 98  898  6   HOH HOH B . 
J 4 HOH 99  899  126 HOH HOH B . 
J 4 HOH 100 900  220 HOH HOH B . 
J 4 HOH 101 901  481 HOH HOH B . 
J 4 HOH 102 902  402 HOH HOH B . 
J 4 HOH 103 903  37  HOH HOH B . 
J 4 HOH 104 904  116 HOH HOH B . 
J 4 HOH 105 905  95  HOH HOH B . 
J 4 HOH 106 906  448 HOH HOH B . 
J 4 HOH 107 907  4   HOH HOH B . 
J 4 HOH 108 908  62  HOH HOH B . 
J 4 HOH 109 909  149 HOH HOH B . 
J 4 HOH 110 910  399 HOH HOH B . 
J 4 HOH 111 911  290 HOH HOH B . 
J 4 HOH 112 912  259 HOH HOH B . 
J 4 HOH 113 913  469 HOH HOH B . 
J 4 HOH 114 914  30  HOH HOH B . 
J 4 HOH 115 915  251 HOH HOH B . 
J 4 HOH 116 916  19  HOH HOH B . 
J 4 HOH 117 917  22  HOH HOH B . 
J 4 HOH 118 918  163 HOH HOH B . 
J 4 HOH 119 919  483 HOH HOH B . 
J 4 HOH 120 920  355 HOH HOH B . 
J 4 HOH 121 921  314 HOH HOH B . 
J 4 HOH 122 922  235 HOH HOH B . 
J 4 HOH 123 923  70  HOH HOH B . 
J 4 HOH 124 924  59  HOH HOH B . 
J 4 HOH 125 925  434 HOH HOH B . 
J 4 HOH 126 926  216 HOH HOH B . 
J 4 HOH 127 927  141 HOH HOH B . 
J 4 HOH 128 928  168 HOH HOH B . 
J 4 HOH 129 929  233 HOH HOH B . 
J 4 HOH 130 930  231 HOH HOH B . 
J 4 HOH 131 931  397 HOH HOH B . 
J 4 HOH 132 932  305 HOH HOH B . 
J 4 HOH 133 933  246 HOH HOH B . 
J 4 HOH 134 934  36  HOH HOH B . 
J 4 HOH 135 935  174 HOH HOH B . 
J 4 HOH 136 936  10  HOH HOH B . 
J 4 HOH 137 937  342 HOH HOH B . 
J 4 HOH 138 938  214 HOH HOH B . 
J 4 HOH 139 939  153 HOH HOH B . 
J 4 HOH 140 940  144 HOH HOH B . 
J 4 HOH 141 941  123 HOH HOH B . 
J 4 HOH 142 942  226 HOH HOH B . 
J 4 HOH 143 943  418 HOH HOH B . 
J 4 HOH 144 944  444 HOH HOH B . 
J 4 HOH 145 945  48  HOH HOH B . 
J 4 HOH 146 946  252 HOH HOH B . 
J 4 HOH 147 947  165 HOH HOH B . 
J 4 HOH 148 948  370 HOH HOH B . 
J 4 HOH 149 949  113 HOH HOH B . 
J 4 HOH 150 950  136 HOH HOH B . 
J 4 HOH 151 951  492 HOH HOH B . 
J 4 HOH 152 952  345 HOH HOH B . 
J 4 HOH 153 953  243 HOH HOH B . 
J 4 HOH 154 954  421 HOH HOH B . 
J 4 HOH 155 955  484 HOH HOH B . 
J 4 HOH 156 956  450 HOH HOH B . 
J 4 HOH 157 957  334 HOH HOH B . 
J 4 HOH 158 958  446 HOH HOH B . 
J 4 HOH 159 959  177 HOH HOH B . 
J 4 HOH 160 960  71  HOH HOH B . 
J 4 HOH 161 961  154 HOH HOH B . 
J 4 HOH 162 962  455 HOH HOH B . 
J 4 HOH 163 963  337 HOH HOH B . 
J 4 HOH 164 964  349 HOH HOH B . 
J 4 HOH 165 965  121 HOH HOH B . 
J 4 HOH 166 966  238 HOH HOH B . 
J 4 HOH 167 967  79  HOH HOH B . 
J 4 HOH 168 968  368 HOH HOH B . 
J 4 HOH 169 969  447 HOH HOH B . 
J 4 HOH 170 970  313 HOH HOH B . 
J 4 HOH 171 971  439 HOH HOH B . 
J 4 HOH 172 972  225 HOH HOH B . 
J 4 HOH 173 973  234 HOH HOH B . 
J 4 HOH 174 974  375 HOH HOH B . 
J 4 HOH 175 975  25  HOH HOH B . 
J 4 HOH 176 976  456 HOH HOH B . 
J 4 HOH 177 977  365 HOH HOH B . 
J 4 HOH 178 978  341 HOH HOH B . 
J 4 HOH 179 979  302 HOH HOH B . 
J 4 HOH 180 980  319 HOH HOH B . 
J 4 HOH 181 981  152 HOH HOH B . 
J 4 HOH 182 982  299 HOH HOH B . 
J 4 HOH 183 983  384 HOH HOH B . 
J 4 HOH 184 984  454 HOH HOH B . 
J 4 HOH 185 985  426 HOH HOH B . 
J 4 HOH 186 986  117 HOH HOH B . 
J 4 HOH 187 987  367 HOH HOH B . 
J 4 HOH 188 988  316 HOH HOH B . 
J 4 HOH 189 989  400 HOH HOH B . 
J 4 HOH 190 990  237 HOH HOH B . 
J 4 HOH 191 991  318 HOH HOH B . 
J 4 HOH 192 992  128 HOH HOH B . 
J 4 HOH 193 993  390 HOH HOH B . 
J 4 HOH 194 994  223 HOH HOH B . 
J 4 HOH 195 995  376 HOH HOH B . 
J 4 HOH 196 996  55  HOH HOH B . 
J 4 HOH 197 997  336 HOH HOH B . 
J 4 HOH 198 998  369 HOH HOH B . 
J 4 HOH 199 999  173 HOH HOH B . 
J 4 HOH 200 1000 265 HOH HOH B . 
J 4 HOH 201 1001 485 HOH HOH B . 
J 4 HOH 202 1002 311 HOH HOH B . 
J 4 HOH 203 1003 356 HOH HOH B . 
J 4 HOH 204 1004 463 HOH HOH B . 
J 4 HOH 205 1005 437 HOH HOH B . 
J 4 HOH 206 1006 471 HOH HOH B . 
J 4 HOH 207 1007 435 HOH HOH B . 
J 4 HOH 208 1008 377 HOH HOH B . 
J 4 HOH 209 1009 487 HOH HOH B . 
J 4 HOH 210 1010 366 HOH HOH B . 
J 4 HOH 211 1011 29  HOH HOH B . 
J 4 HOH 212 1012 363 HOH HOH B . 
J 4 HOH 213 1013 98  HOH HOH B . 
J 4 HOH 214 1014 464 HOH HOH B . 
J 4 HOH 215 1015 338 HOH HOH B . 
J 4 HOH 216 1016 373 HOH HOH B . 
J 4 HOH 217 1017 475 HOH HOH B . 
J 4 HOH 218 1018 244 HOH HOH B . 
J 4 HOH 219 1019 248 HOH HOH B . 
J 4 HOH 220 1020 271 HOH HOH B . 
J 4 HOH 221 1021 386 HOH HOH B . 
J 4 HOH 222 1022 242 HOH HOH B . 
J 4 HOH 223 1023 133 HOH HOH B . 
J 4 HOH 224 1024 378 HOH HOH B . 
J 4 HOH 225 1025 171 HOH HOH B . 
J 4 HOH 226 1026 413 HOH HOH B . 
J 4 HOH 227 1027 255 HOH HOH B . 
J 4 HOH 228 1028 212 HOH HOH B . 
J 4 HOH 229 1029 197 HOH HOH B . 
J 4 HOH 230 1030 312 HOH HOH B . 
J 4 HOH 231 1031 317 HOH HOH B . 
J 4 HOH 232 1032 199 HOH HOH B . 
J 4 HOH 233 1033 374 HOH HOH B . 
J 4 HOH 234 1034 371 HOH HOH B . 
J 4 HOH 235 1035 328 HOH HOH B . 
J 4 HOH 236 1036 196 HOH HOH B . 
J 4 HOH 237 1037 258 HOH HOH B . 
J 4 HOH 238 1038 383 HOH HOH B . 
J 4 HOH 239 1039 190 HOH HOH B . 
J 4 HOH 240 1040 293 HOH HOH B . 
J 4 HOH 241 1041 396 HOH HOH B . 
J 4 HOH 242 1042 380 HOH HOH B . 
J 4 HOH 243 1043 343 HOH HOH B . 
J 4 HOH 244 1044 478 HOH HOH B . 
J 4 HOH 245 1045 482 HOH HOH B . 
J 4 HOH 246 1046 283 HOH HOH B . 
J 4 HOH 247 1047 387 HOH HOH B . 
J 4 HOH 248 1048 364 HOH HOH B . 
J 4 HOH 249 1049 253 HOH HOH B . 
J 4 HOH 250 1050 227 HOH HOH B . 
J 4 HOH 251 1051 296 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 98  ? CG  ? A ARG 3   CG  
2   1 Y 1 A ARG 98  ? CD  ? A ARG 3   CD  
3   1 Y 1 A ARG 98  ? NE  ? A ARG 3   NE  
4   1 Y 1 A ARG 98  ? CZ  ? A ARG 3   CZ  
5   1 Y 1 A ARG 98  ? NH1 ? A ARG 3   NH1 
6   1 Y 1 A ARG 98  ? NH2 ? A ARG 3   NH2 
7   1 Y 1 A ASN 100 ? CG  ? A ASN 5   CG  
8   1 Y 1 A ASN 100 ? OD1 ? A ASN 5   OD1 
9   1 Y 1 A ASN 100 ? ND2 ? A ASN 5   ND2 
10  1 Y 1 A LEU 101 ? CG  ? A LEU 6   CG  
11  1 Y 1 A LEU 101 ? CD1 ? A LEU 6   CD1 
12  1 Y 1 A LEU 101 ? CD2 ? A LEU 6   CD2 
13  1 Y 1 A LYS 102 ? CG  ? A LYS 7   CG  
14  1 Y 1 A LYS 102 ? CD  ? A LYS 7   CD  
15  1 Y 1 A LYS 102 ? CE  ? A LYS 7   CE  
16  1 Y 1 A LYS 102 ? NZ  ? A LYS 7   NZ  
17  1 Y 1 A LYS 107 ? CG  ? A LYS 12  CG  
18  1 Y 1 A LYS 107 ? CD  ? A LYS 12  CD  
19  1 Y 1 A LYS 107 ? CE  ? A LYS 12  CE  
20  1 Y 1 A LYS 107 ? NZ  ? A LYS 12  NZ  
21  1 Y 1 A LYS 130 ? CE  ? A LYS 35  CE  
22  1 Y 1 A LYS 130 ? NZ  ? A LYS 35  NZ  
23  1 Y 1 A ASN 132 ? CG  ? A ASN 37  CG  
24  1 Y 1 A ASN 132 ? OD1 ? A ASN 37  OD1 
25  1 Y 1 A ASN 132 ? ND2 ? A ASN 37  ND2 
26  1 Y 1 A GLU 133 ? CG  ? A GLU 38  CG  
27  1 Y 1 A GLU 133 ? CD  ? A GLU 38  CD  
28  1 Y 1 A GLU 133 ? OE1 ? A GLU 38  OE1 
29  1 Y 1 A GLU 133 ? OE2 ? A GLU 38  OE2 
30  1 Y 1 A LYS 134 ? CG  ? A LYS 39  CG  
31  1 Y 1 A LYS 134 ? CD  ? A LYS 39  CD  
32  1 Y 1 A LYS 134 ? CE  ? A LYS 39  CE  
33  1 Y 1 A LYS 134 ? NZ  ? A LYS 39  NZ  
34  1 Y 1 A GLN 182 ? CG  ? A GLN 87  CG  
35  1 Y 1 A GLN 182 ? CD  ? A GLN 87  CD  
36  1 Y 1 A GLN 182 ? OE1 ? A GLN 87  OE1 
37  1 Y 1 A GLN 182 ? NE2 ? A GLN 87  NE2 
38  1 Y 1 A LYS 219 ? CG  ? A LYS 124 CG  
39  1 Y 1 A LYS 219 ? CD  ? A LYS 124 CD  
40  1 Y 1 A LYS 219 ? CE  ? A LYS 124 CE  
41  1 Y 1 A LYS 219 ? NZ  ? A LYS 124 NZ  
42  1 Y 1 A GLU 250 ? CG  ? A GLU 155 CG  
43  1 Y 1 A GLU 250 ? CD  ? A GLU 155 CD  
44  1 Y 1 A GLU 250 ? OE1 ? A GLU 155 OE1 
45  1 Y 1 A GLU 250 ? OE2 ? A GLU 155 OE2 
46  1 Y 1 A VAL 251 ? CG1 ? A VAL 156 CG1 
47  1 Y 1 A VAL 251 ? CG2 ? A VAL 156 CG2 
48  1 Y 1 A LYS 282 ? CE  ? A LYS 187 CE  
49  1 Y 1 A LYS 282 ? NZ  ? A LYS 187 NZ  
50  1 Y 1 A GLU 292 ? CG  ? A GLU 197 CG  
51  1 Y 1 A GLU 292 ? CD  ? A GLU 197 CD  
52  1 Y 1 A GLU 292 ? OE1 ? A GLU 197 OE1 
53  1 Y 1 A GLU 292 ? OE2 ? A GLU 197 OE2 
54  1 Y 1 A LYS 296 ? CG  ? A LYS 201 CG  
55  1 Y 1 A LYS 296 ? CD  ? A LYS 201 CD  
56  1 Y 1 A LYS 296 ? CE  ? A LYS 201 CE  
57  1 Y 1 A LYS 296 ? NZ  ? A LYS 201 NZ  
58  1 Y 1 A ARG 396 ? CZ  ? A ARG 301 CZ  
59  1 Y 1 A ARG 396 ? NH1 ? A ARG 301 NH1 
60  1 Y 1 A ARG 396 ? NH2 ? A ARG 301 NH2 
61  1 Y 1 A GLU 398 ? OE1 ? A GLU 303 OE1 
62  1 Y 1 A GLU 398 ? OE2 ? A GLU 303 OE2 
63  1 Y 1 A LYS 445 ? CE  ? A LYS 350 CE  
64  1 Y 1 A LYS 445 ? NZ  ? A LYS 350 NZ  
65  1 Y 1 A GLU 460 ? CG  ? A GLU 365 CG  
66  1 Y 1 A GLU 460 ? CD  ? A GLU 365 CD  
67  1 Y 1 A GLU 460 ? OE1 ? A GLU 365 OE1 
68  1 Y 1 A GLU 460 ? OE2 ? A GLU 365 OE2 
69  1 Y 1 A LYS 489 ? NZ  ? A LYS 394 NZ  
70  1 Y 1 A GLU 491 ? CG  ? A GLU 396 CG  
71  1 Y 1 A GLU 491 ? CD  ? A GLU 396 CD  
72  1 Y 1 A GLU 491 ? OE1 ? A GLU 396 OE1 
73  1 Y 1 A GLU 491 ? OE2 ? A GLU 396 OE2 
74  1 Y 1 A ILE 493 ? CG1 ? A ILE 398 CG1 
75  1 Y 1 A ILE 493 ? CG2 ? A ILE 398 CG2 
76  1 Y 1 A ILE 493 ? CD1 ? A ILE 398 CD1 
77  1 Y 1 A LEU 494 ? CG  ? A LEU 399 CG  
78  1 Y 1 A LEU 494 ? CD1 ? A LEU 399 CD1 
79  1 Y 1 A LEU 494 ? CD2 ? A LEU 399 CD2 
80  1 Y 1 B ASN 100 ? CG  ? B ASN 5   CG  
81  1 Y 1 B ASN 100 ? OD1 ? B ASN 5   OD1 
82  1 Y 1 B ASN 100 ? ND2 ? B ASN 5   ND2 
83  1 Y 1 B LEU 101 ? CG  ? B LEU 6   CG  
84  1 Y 1 B LEU 101 ? CD1 ? B LEU 6   CD1 
85  1 Y 1 B LEU 101 ? CD2 ? B LEU 6   CD2 
86  1 Y 1 B LYS 102 ? CG  ? B LYS 7   CG  
87  1 Y 1 B LYS 102 ? CD  ? B LYS 7   CD  
88  1 Y 1 B LYS 102 ? CE  ? B LYS 7   CE  
89  1 Y 1 B LYS 102 ? NZ  ? B LYS 7   NZ  
90  1 Y 1 B GLU 104 ? CG  ? B GLU 9   CG  
91  1 Y 1 B GLU 104 ? CD  ? B GLU 9   CD  
92  1 Y 1 B GLU 104 ? OE1 ? B GLU 9   OE1 
93  1 Y 1 B GLU 104 ? OE2 ? B GLU 9   OE2 
94  1 Y 1 B LYS 107 ? CG  ? B LYS 12  CG  
95  1 Y 1 B LYS 107 ? CD  ? B LYS 12  CD  
96  1 Y 1 B LYS 107 ? CE  ? B LYS 12  CE  
97  1 Y 1 B LYS 107 ? NZ  ? B LYS 12  NZ  
98  1 Y 1 B VAL 108 ? CG1 ? B VAL 13  CG1 
99  1 Y 1 B VAL 108 ? CG2 ? B VAL 13  CG2 
100 1 Y 1 B LYS 118 ? CE  ? B LYS 23  CE  
101 1 Y 1 B LYS 118 ? NZ  ? B LYS 23  NZ  
102 1 Y 1 B LYS 128 ? CG  ? B LYS 33  CG  
103 1 Y 1 B LYS 128 ? CD  ? B LYS 33  CD  
104 1 Y 1 B LYS 128 ? CE  ? B LYS 33  CE  
105 1 Y 1 B LYS 128 ? NZ  ? B LYS 33  NZ  
106 1 Y 1 B LYS 130 ? CE  ? B LYS 35  CE  
107 1 Y 1 B LYS 130 ? NZ  ? B LYS 35  NZ  
108 1 Y 1 B ASN 132 ? CG  ? B ASN 37  CG  
109 1 Y 1 B ASN 132 ? OD1 ? B ASN 37  OD1 
110 1 Y 1 B ASN 132 ? ND2 ? B ASN 37  ND2 
111 1 Y 1 B GLU 135 ? CG  ? B GLU 40  CG  
112 1 Y 1 B GLU 135 ? CD  ? B GLU 40  CD  
113 1 Y 1 B GLU 135 ? OE1 ? B GLU 40  OE1 
114 1 Y 1 B GLU 135 ? OE2 ? B GLU 40  OE2 
115 1 Y 1 B ARG 137 ? CG  ? B ARG 42  CG  
116 1 Y 1 B ARG 137 ? CD  ? B ARG 42  CD  
117 1 Y 1 B ARG 137 ? NE  ? B ARG 42  NE  
118 1 Y 1 B ARG 137 ? CZ  ? B ARG 42  CZ  
119 1 Y 1 B ARG 137 ? NH1 ? B ARG 42  NH1 
120 1 Y 1 B ARG 137 ? NH2 ? B ARG 42  NH2 
121 1 Y 1 B HIS 179 ? CG  ? B HIS 84  CG  
122 1 Y 1 B HIS 179 ? ND1 ? B HIS 84  ND1 
123 1 Y 1 B HIS 179 ? CD2 ? B HIS 84  CD2 
124 1 Y 1 B HIS 179 ? CE1 ? B HIS 84  CE1 
125 1 Y 1 B HIS 179 ? NE2 ? B HIS 84  NE2 
126 1 Y 1 B GLN 182 ? CG  ? B GLN 87  CG  
127 1 Y 1 B GLN 182 ? CD  ? B GLN 87  CD  
128 1 Y 1 B GLN 182 ? OE1 ? B GLN 87  OE1 
129 1 Y 1 B GLN 182 ? NE2 ? B GLN 87  NE2 
130 1 Y 1 B ARG 195 ? CZ  ? B ARG 100 CZ  
131 1 Y 1 B ARG 195 ? NH1 ? B ARG 100 NH1 
132 1 Y 1 B ARG 195 ? NH2 ? B ARG 100 NH2 
133 1 Y 1 B LYS 197 ? CG  ? B LYS 102 CG  
134 1 Y 1 B LYS 197 ? CD  ? B LYS 102 CD  
135 1 Y 1 B LYS 197 ? CE  ? B LYS 102 CE  
136 1 Y 1 B LYS 197 ? NZ  ? B LYS 102 NZ  
137 1 Y 1 B LEU 200 ? CG  ? B LEU 105 CG  
138 1 Y 1 B LEU 200 ? CD1 ? B LEU 105 CD1 
139 1 Y 1 B LEU 200 ? CD2 ? B LEU 105 CD2 
140 1 Y 1 B ILE 218 ? CG1 ? B ILE 123 CG1 
141 1 Y 1 B ILE 218 ? CG2 ? B ILE 123 CG2 
142 1 Y 1 B ILE 218 ? CD1 ? B ILE 123 CD1 
143 1 Y 1 B LYS 219 ? CG  ? B LYS 124 CG  
144 1 Y 1 B LYS 219 ? CD  ? B LYS 124 CD  
145 1 Y 1 B LYS 219 ? CE  ? B LYS 124 CE  
146 1 Y 1 B LYS 219 ? NZ  ? B LYS 124 NZ  
147 1 Y 1 B ASP 222 ? CG  ? B ASP 127 CG  
148 1 Y 1 B ASP 222 ? OD1 ? B ASP 127 OD1 
149 1 Y 1 B ASP 222 ? OD2 ? B ASP 127 OD2 
150 1 Y 1 B LYS 225 ? CG  ? B LYS 130 CG  
151 1 Y 1 B LYS 225 ? CD  ? B LYS 130 CD  
152 1 Y 1 B LYS 225 ? CE  ? B LYS 130 CE  
153 1 Y 1 B LYS 225 ? NZ  ? B LYS 130 NZ  
154 1 Y 1 B LYS 229 ? CG  ? B LYS 134 CG  
155 1 Y 1 B LYS 229 ? CD  ? B LYS 134 CD  
156 1 Y 1 B LYS 229 ? CE  ? B LYS 134 CE  
157 1 Y 1 B LYS 229 ? NZ  ? B LYS 134 NZ  
158 1 Y 1 B LYS 245 ? CG  ? B LYS 150 CG  
159 1 Y 1 B LYS 245 ? CD  ? B LYS 150 CD  
160 1 Y 1 B LYS 245 ? CE  ? B LYS 150 CE  
161 1 Y 1 B LYS 245 ? NZ  ? B LYS 150 NZ  
162 1 Y 1 B GLU 250 ? CG  ? B GLU 155 CG  
163 1 Y 1 B GLU 250 ? CD  ? B GLU 155 CD  
164 1 Y 1 B GLU 250 ? OE1 ? B GLU 155 OE1 
165 1 Y 1 B GLU 250 ? OE2 ? B GLU 155 OE2 
166 1 Y 1 B ILE 253 ? CG1 ? B ILE 158 CG1 
167 1 Y 1 B ILE 253 ? CG2 ? B ILE 158 CG2 
168 1 Y 1 B ILE 253 ? CD1 ? B ILE 158 CD1 
169 1 Y 1 B ASP 254 ? CG  ? B ASP 159 CG  
170 1 Y 1 B ASP 254 ? OD1 ? B ASP 159 OD1 
171 1 Y 1 B ASP 254 ? OD2 ? B ASP 159 OD2 
172 1 Y 1 B SER 255 ? OG  ? B SER 160 OG  
173 1 Y 1 B ARG 265 ? CZ  ? B ARG 170 CZ  
174 1 Y 1 B ARG 265 ? NH1 ? B ARG 170 NH1 
175 1 Y 1 B ARG 265 ? NH2 ? B ARG 170 NH2 
176 1 Y 1 B LYS 282 ? CG  ? B LYS 187 CG  
177 1 Y 1 B LYS 282 ? CD  ? B LYS 187 CD  
178 1 Y 1 B LYS 282 ? CE  ? B LYS 187 CE  
179 1 Y 1 B LYS 282 ? NZ  ? B LYS 187 NZ  
180 1 Y 1 B LYS 296 ? CE  ? B LYS 201 CE  
181 1 Y 1 B LYS 296 ? NZ  ? B LYS 201 NZ  
182 1 Y 1 B GLU 335 ? CG  ? B GLU 240 CG  
183 1 Y 1 B GLU 335 ? CD  ? B GLU 240 CD  
184 1 Y 1 B GLU 335 ? OE1 ? B GLU 240 OE1 
185 1 Y 1 B GLU 335 ? OE2 ? B GLU 240 OE2 
186 1 Y 1 B LYS 366 ? CG  ? B LYS 271 CG  
187 1 Y 1 B LYS 366 ? CD  ? B LYS 271 CD  
188 1 Y 1 B LYS 366 ? CE  ? B LYS 271 CE  
189 1 Y 1 B LYS 366 ? NZ  ? B LYS 271 NZ  
190 1 Y 1 B ARG 396 ? CZ  ? B ARG 301 CZ  
191 1 Y 1 B ARG 396 ? NH1 ? B ARG 301 NH1 
192 1 Y 1 B ARG 396 ? NH2 ? B ARG 301 NH2 
193 1 Y 1 B LYS 445 ? CE  ? B LYS 350 CE  
194 1 Y 1 B LYS 445 ? NZ  ? B LYS 350 NZ  
195 1 Y 1 B LYS 451 ? CD  ? B LYS 356 CD  
196 1 Y 1 B LYS 451 ? CE  ? B LYS 356 CE  
197 1 Y 1 B LYS 451 ? NZ  ? B LYS 356 NZ  
198 1 Y 1 B LYS 489 ? CE  ? B LYS 394 CE  
199 1 Y 1 B LYS 489 ? NZ  ? B LYS 394 NZ  
200 1 Y 1 B LYS 573 ? CE  ? B LYS 478 CE  
201 1 Y 1 B LYS 573 ? NZ  ? B LYS 478 NZ  
# 
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 ? ? ? '(1.21.2_5419: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    3 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9M5M 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     140.447 
_cell.length_a_esd                 ? 
_cell.length_b                     140.447 
_cell.length_b_esd                 ? 
_cell.length_c                     272.559 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9M5M 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                178 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61 2 2' 
_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                   9M5M 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.12 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          60.61 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M Lithium sulfate, 0.1M Bis-Tris pH 6.5, 25% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-27 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9763 
_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                        'DIAMOND BEAMLINE I03' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9763 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I03 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9M5M 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.06 
_reflns.d_resolution_low                               90.85 
_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                                     98198 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                33.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.4 
_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                                0.110 
_reflns.pdbx_Rpim_I_all                                0.018 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       3254813 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.109 
_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                                    2.06 
_reflns_shell.d_res_low                                     2.10 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           55961 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4723 
_reflns_shell.percent_possible_obs                          97.6 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               11.8 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.3 
_reflns_shell.pdbx_Rrim_I_all                               2.732 
_reflns_shell.pdbx_Rpim_I_all                               0.750 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.323 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.617 
_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                                 9M5M 
_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                            2.06 
_refine.ls_d_res_low                             72.79 
_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                     97555 
_refine.ls_number_reflns_R_free                  4843 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.28 
_refine.ls_percent_reflns_R_free                 4.96 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1844 
_refine.ls_R_factor_R_free                       0.2111 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1830 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.33 
_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                 20.92 
_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                            0.26 
_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.pdbx_number_atoms_protein        8058 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         28 
_refine_hist.number_atoms_solvent             492 
_refine_hist.number_atoms_total               8578 
_refine_hist.d_res_high                       2.06 
_refine_hist.d_res_low                        72.79 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007  ? 8263  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.847  ? 11156 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 21.662 ? 3048  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 1216  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 1431  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 2.06 2.08  . . 144 2630 86.00  . . . . 0.3769 . . . . . . . . . . . . . . . 0.3782 
'X-RAY DIFFRACTION' 2.08 2.11  . . 128 2898 94.00  . . . . 0.3471 . . . . . . . . . . . . . . . 0.3820 
'X-RAY DIFFRACTION' 2.11 2.13  . . 155 3038 98.00  . . . . 0.3285 . . . . . . . . . . . . . . . 0.3590 
'X-RAY DIFFRACTION' 2.13 2.16  . . 138 3068 100.00 . . . . 0.3013 . . . . . . . . . . . . . . . 0.3243 
'X-RAY DIFFRACTION' 2.16 2.19  . . 152 3053 100.00 . . . . 0.2793 . . . . . . . . . . . . . . . 0.2672 
'X-RAY DIFFRACTION' 2.19 2.22  . . 168 3045 100.00 . . . . 0.2498 . . . . . . . . . . . . . . . 0.2635 
'X-RAY DIFFRACTION' 2.22 2.25  . . 166 3076 100.00 . . . . 0.2333 . . . . . . . . . . . . . . . 0.2480 
'X-RAY DIFFRACTION' 2.25 2.28  . . 141 3069 100.00 . . . . 0.2194 . . . . . . . . . . . . . . . 0.2454 
'X-RAY DIFFRACTION' 2.28 2.32  . . 166 3063 100.00 . . . . 0.2087 . . . . . . . . . . . . . . . 0.2617 
'X-RAY DIFFRACTION' 2.32 2.36  . . 182 3063 100.00 . . . . 0.2077 . . . . . . . . . . . . . . . 0.2613 
'X-RAY DIFFRACTION' 2.36 2.40  . . 166 3069 100.00 . . . . 0.2040 . . . . . . . . . . . . . . . 0.2155 
'X-RAY DIFFRACTION' 2.40 2.44  . . 167 3060 100.00 . . . . 0.2027 . . . . . . . . . . . . . . . 0.2310 
'X-RAY DIFFRACTION' 2.44 2.49  . . 181 3078 100.00 . . . . 0.2038 . . . . . . . . . . . . . . . 0.2963 
'X-RAY DIFFRACTION' 2.49 2.54  . . 151 3077 100.00 . . . . 0.2080 . . . . . . . . . . . . . . . 0.2460 
'X-RAY DIFFRACTION' 2.54 2.60  . . 184 3087 100.00 . . . . 0.2066 . . . . . . . . . . . . . . . 0.2667 
'X-RAY DIFFRACTION' 2.60 2.66  . . 156 3070 100.00 . . . . 0.1826 . . . . . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 2.66 2.72  . . 144 3106 100.00 . . . . 0.1789 . . . . . . . . . . . . . . . 0.1993 
'X-RAY DIFFRACTION' 2.72 2.80  . . 169 3096 100.00 . . . . 0.1794 . . . . . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 2.80 2.88  . . 154 3112 100.00 . . . . 0.1894 . . . . . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 2.88 2.97  . . 176 3092 100.00 . . . . 0.1920 . . . . . . . . . . . . . . . 0.2574 
'X-RAY DIFFRACTION' 2.97 3.08  . . 148 3122 100.00 . . . . 0.1966 . . . . . . . . . . . . . . . 0.2158 
'X-RAY DIFFRACTION' 3.08 3.20  . . 162 3123 100.00 . . . . 0.1958 . . . . . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 3.20 3.35  . . 180 3110 100.00 . . . . 0.1862 . . . . . . . . . . . . . . . 0.2362 
'X-RAY DIFFRACTION' 3.35 3.52  . . 178 3107 100.00 . . . . 0.1780 . . . . . . . . . . . . . . . 0.1964 
'X-RAY DIFFRACTION' 3.52 3.74  . . 150 3155 100.00 . . . . 0.1689 . . . . . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 3.74 4.03  . . 153 3169 100.00 . . . . 0.1496 . . . . . . . . . . . . . . . 0.1678 
'X-RAY DIFFRACTION' 4.03 4.44  . . 155 3178 100.00 . . . . 0.1371 . . . . . . . . . . . . . . . 0.1467 
'X-RAY DIFFRACTION' 4.44 5.08  . . 151 3225 100.00 . . . . 0.1406 . . . . . . . . . . . . . . . 0.1725 
'X-RAY DIFFRACTION' 5.08 6.40  . . 173 3257 100.00 . . . . 0.1839 . . . . . . . . . . . . . . . 0.2259 
'X-RAY DIFFRACTION' 6.40 72.79 . . 205 3416 100.00 . . . . 0.1926 . . . . . . . . . . . . . . . 0.1873 
# 
_struct.entry_id                     9M5M 
_struct.title                        'Crystal structure of Plasmodium vivax aspartyl-tRNA synthetase (PvDRS)' 
_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        9M5M 
_struct_keywords.text            'AMINOACYLATION, AMINOACYL-TRNA SYNTHETASE, MALARIA, INHIBITOR, ATP-BINDING, L-ASP, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1G4H6Y1_PLAVI 
_struct_ref.pdbx_db_accession          A0A1G4H6Y1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;AERENLKNEATKVLEHVCEDINKESYGFVKISKMKENEKEIRLFNLEEIYHSLMKVGGSGATDGGKREDDAASHSVVAES
NGAHLLQSDIWVRGRIHDIRSKGSLAFIILRHKLYSMQCILDIKHNDNDKNMMKWVSNLPLESIVDIKGKLSKPEVPIDS
TNIKYEAHIRKIFCISKTAKELPFLLKDANMKETNEEGSIKVNQDNRLNNRCVDLRTYANYSIFCLQSQICTIFKNFLLE
NNFIEIHTPKLLGESSEGGANAFQINYFNQKGFLAQSPQLYKQMCINSGFDRVFEVAPVFRAENSNTYRHLCEYVSLDVE
MTYKYDYLENVHFYDSMFKHIFTELSKGGKNEMLIKTVKGQYPCEDFQWLEETPIFTYEEAIKMLIQHGKLHLKEEEILA
YDMSTDMEKELGKIVKASHHTDYYIIINFPSALRPFYTMYKEDEPAISNSYDFFMRGEEILSGSQRISDVNLLLENIKRF
NLDANKLNFYIDSFAYSSYPHSGCGIGLERVLMLFLGLNNIRKTSLFPRDPKRLIP
;
_struct_ref.pdbx_align_begin           96 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9M5M A 1 ? 536 ? A0A1G4H6Y1 96 ? 631 ? 96 631 
2 1 9M5M B 1 ? 536 ? A0A1G4H6Y1 96 ? 631 ? 96 631 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9740  ? 
1 MORE         -98   ? 
1 'SSA (A^2)'  40620 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 4   ? GLU A 15  ? GLU A 99  GLU A 110 1 ? 12 
HELX_P HELX_P2  AA2 LYS A 30  ? MET A 34  ? LYS A 125 MET A 129 5 ? 5  
HELX_P HELX_P3  AA3 ASN A 45  ? MET A 54  ? ASN A 140 MET A 149 1 ? 10 
HELX_P HELX_P4  AA4 LYS A 124 ? ASN A 126 ? LYS A 219 ASN A 221 5 ? 3  
HELX_P HELX_P5  AA5 ASP A 129 ? ASN A 138 ? ASP A 224 ASN A 233 1 ? 10 
HELX_P HELX_P6  AA6 LEU A 185 ? ASN A 190 ? LEU A 280 ASN A 285 1 ? 6  
HELX_P HELX_P7  AA7 ASN A 203 ? ASN A 210 ? ASN A 298 ASN A 305 1 ? 8  
HELX_P HELX_P8  AA8 ASN A 210 ? LEU A 215 ? ASN A 305 LEU A 310 1 ? 6  
HELX_P HELX_P9  AA9 THR A 217 ? ASN A 241 ? THR A 312 ASN A 336 1 ? 25 
HELX_P HELX_P10 AB1 PRO A 278 ? SER A 288 ? PRO A 373 SER A 383 1 ? 11 
HELX_P HELX_P11 AB2 TYR A 327 ? SER A 346 ? TYR A 422 SER A 441 1 ? 20 
HELX_P HELX_P12 AB3 GLY A 348 ? TYR A 362 ? GLY A 443 TYR A 457 1 ? 15 
HELX_P HELX_P13 AB4 TYR A 378 ? HIS A 388 ? TYR A 473 HIS A 483 1 ? 11 
HELX_P HELX_P14 AB5 SER A 404 ? HIS A 420 ? SER A 499 HIS A 515 1 ? 17 
HELX_P HELX_P15 AB6 PRO A 430 ? ARG A 434 ? PRO A 525 ARG A 529 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 469 ? PHE A 480 ? ASP A 564 PHE A 575 1 ? 12 
HELX_P HELX_P17 AB8 ASP A 483 ? LYS A 486 ? ASP A 578 LYS A 581 5 ? 4  
HELX_P HELX_P18 AB9 LEU A 487 ? SER A 493 ? LEU A 582 SER A 588 1 ? 7  
HELX_P HELX_P19 AC1 LEU A 508 ? GLY A 517 ? LEU A 603 GLY A 612 1 ? 10 
HELX_P HELX_P20 AC2 ASN A 520 ? THR A 524 ? ASN A 615 THR A 619 5 ? 5  
HELX_P HELX_P21 AC3 LEU B 6   ? GLU B 15  ? LEU B 101 GLU B 110 1 ? 10 
HELX_P HELX_P22 AC4 LYS B 30  ? MET B 34  ? LYS B 125 MET B 129 5 ? 5  
HELX_P HELX_P23 AC5 ASN B 45  ? MET B 54  ? ASN B 140 MET B 149 1 ? 10 
HELX_P HELX_P24 AC6 LYS B 124 ? ASN B 126 ? LYS B 219 ASN B 221 5 ? 3  
HELX_P HELX_P25 AC7 ASP B 129 ? ASN B 138 ? ASP B 224 ASN B 233 1 ? 10 
HELX_P HELX_P26 AC8 LEU B 185 ? MET B 191 ? LEU B 280 MET B 286 1 ? 7  
HELX_P HELX_P27 AC9 ASN B 203 ? ASN B 210 ? ASN B 298 ASN B 305 1 ? 8  
HELX_P HELX_P28 AD1 ASN B 210 ? LEU B 215 ? ASN B 305 LEU B 310 1 ? 6  
HELX_P HELX_P29 AD2 THR B 217 ? ASN B 241 ? THR B 312 ASN B 336 1 ? 25 
HELX_P HELX_P30 AD3 GLY B 258 ? ALA B 262 ? GLY B 353 ALA B 357 5 ? 5  
HELX_P HELX_P31 AD4 PRO B 278 ? SER B 288 ? PRO B 373 SER B 383 1 ? 11 
HELX_P HELX_P32 AD5 TYR B 327 ? SER B 346 ? TYR B 422 SER B 441 1 ? 20 
HELX_P HELX_P33 AD6 GLY B 349 ? TYR B 362 ? GLY B 444 TYR B 457 1 ? 14 
HELX_P HELX_P34 AD7 TYR B 378 ? HIS B 388 ? TYR B 473 HIS B 483 1 ? 11 
HELX_P HELX_P35 AD8 LYS B 394 ? ILE B 398 ? LYS B 489 ILE B 493 5 ? 5  
HELX_P HELX_P36 AD9 SER B 404 ? HIS B 420 ? SER B 499 HIS B 515 1 ? 17 
HELX_P HELX_P37 AE1 PRO B 430 ? ARG B 434 ? PRO B 525 ARG B 529 5 ? 5  
HELX_P HELX_P38 AE2 ASP B 469 ? PHE B 480 ? ASP B 564 PHE B 575 1 ? 12 
HELX_P HELX_P39 AE3 ASP B 483 ? LYS B 486 ? ASP B 578 LYS B 581 5 ? 4  
HELX_P HELX_P40 AE4 LEU B 487 ? SER B 493 ? LEU B 582 SER B 588 1 ? 7  
HELX_P HELX_P41 AE5 LEU B 508 ? GLY B 517 ? LEU B 603 GLY B 612 1 ? 10 
HELX_P HELX_P42 AE6 ASN B 520 ? THR B 524 ? ASN B 615 THR B 619 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 ILE 535 A . ? ILE 630 A PRO 536 A ? PRO 631 A 1 -12.41 
2 ILE 535 B . ? ILE 630 B PRO 536 B ? PRO 631 B 1 -8.37  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 5 ? 
AA3 ? 8 ? 
AA4 ? 3 ? 
AA5 ? 6 ? 
AA6 ? 5 ? 
AA7 ? 8 ? 
AA8 ? 3 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA5 5 6 ? parallel      
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? parallel      
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA7 7 8 ? parallel      
AA8 1 2 ? anti-parallel 
AA8 2 3 ? 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 TYR A 26  ? PHE A 28  ? TYR A 121 PHE A 123 
AA1 2 GLU A 166 ? SER A 176 ? GLU A 261 SER A 271 
AA1 3 TYR A 115 ? ASP A 122 ? TYR A 210 ASP A 217 
AA1 4 LEU A 105 ? HIS A 112 ? LEU A 200 HIS A 207 
AA1 5 ILE A 90  ? LYS A 102 ? ILE A 185 LYS A 197 
AA1 6 LEU A 43  ? PHE A 44  ? LEU A 138 PHE A 139 
AA2 1 TYR A 26  ? PHE A 28  ? TYR A 121 PHE A 123 
AA2 2 GLU A 166 ? SER A 176 ? GLU A 261 SER A 271 
AA2 3 ILE A 144 ? SER A 152 ? ILE A 239 SER A 247 
AA2 4 ILE A 90  ? LYS A 102 ? ILE A 185 LYS A 197 
AA2 5 LEU A 43  ? PHE A 44  ? LEU A 138 PHE A 139 
AA3 1 ILE A 244 ? GLU A 245 ? ILE A 339 GLU A 340 
AA3 2 ARG A 292 ? PHE A 300 ? ARG A 387 PHE A 395 
AA3 3 GLU A 313 ? THR A 322 ? GLU A 408 THR A 417 
AA3 4 HIS A 501 ? GLY A 507 ? HIS A 596 GLY A 602 
AA3 5 GLU A 458 ? GLN A 465 ? GLU A 553 GLN A 560 
AA3 6 SER A 450 ? MET A 455 ? SER A 545 MET A 550 
AA3 7 TYR A 423 ? ILE A 427 ? TYR A 518 ILE A 522 
AA3 8 ILE A 375 ? THR A 377 ? ILE A 470 THR A 472 
AA4 1 LEU A 251 ? LEU A 252 ? LEU A 346 LEU A 347 
AA4 2 GLN A 270 ? LEU A 274 ? GLN A 365 LEU A 369 
AA4 3 GLN A 264 ? TYR A 267 ? GLN A 359 TYR A 362 
AA5 1 TYR B 26  ? PHE B 28  ? TYR B 121 PHE B 123 
AA5 2 GLU B 166 ? SER B 176 ? GLU B 261 SER B 271 
AA5 3 TYR B 115 ? ASP B 122 ? TYR B 210 ASP B 217 
AA5 4 LEU B 105 ? HIS B 112 ? LEU B 200 HIS B 207 
AA5 5 ILE B 90  ? LYS B 102 ? ILE B 185 LYS B 197 
AA5 6 LEU B 43  ? PHE B 44  ? LEU B 138 PHE B 139 
AA6 1 TYR B 26  ? PHE B 28  ? TYR B 121 PHE B 123 
AA6 2 GLU B 166 ? SER B 176 ? GLU B 261 SER B 271 
AA6 3 ILE B 144 ? SER B 152 ? ILE B 239 SER B 247 
AA6 4 ILE B 90  ? LYS B 102 ? ILE B 185 LYS B 197 
AA6 5 LEU B 43  ? PHE B 44  ? LEU B 138 PHE B 139 
AA7 1 ILE B 244 ? GLU B 245 ? ILE B 339 GLU B 340 
AA7 2 ARG B 292 ? PHE B 300 ? ARG B 387 PHE B 395 
AA7 3 GLU B 313 ? THR B 322 ? GLU B 408 THR B 417 
AA7 4 HIS B 501 ? GLY B 507 ? HIS B 596 GLY B 602 
AA7 5 GLU B 458 ? GLN B 465 ? GLU B 553 GLN B 560 
AA7 6 SER B 450 ? MET B 455 ? SER B 545 MET B 550 
AA7 7 TYR B 423 ? ILE B 427 ? TYR B 518 ILE B 522 
AA7 8 ILE B 375 ? THR B 377 ? ILE B 470 THR B 472 
AA8 1 LEU B 251 ? LEU B 252 ? LEU B 346 LEU B 347 
AA8 2 GLN B 270 ? LEU B 274 ? GLN B 365 LEU B 369 
AA8 3 GLN B 264 ? TYR B 267 ? GLN B 359 TYR B 362 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 27  ? N GLY A 122 O CYS A 174 ? O CYS A 269 
AA1 2 3 O ALA A 167 ? O ALA A 262 N ILE A 120 ? N ILE A 215 
AA1 3 4 O CYS A 119 ? O CYS A 214 N ILE A 108 ? N ILE A 203 
AA1 4 5 O PHE A 107 ? O PHE A 202 N ARG A 100 ? N ARG A 195 
AA1 5 6 O TRP A 91  ? O TRP A 186 N PHE A 44  ? N PHE A 139 
AA2 1 2 N GLY A 27  ? N GLY A 122 O CYS A 174 ? O CYS A 269 
AA2 2 3 O ARG A 170 ? O ARG A 265 N LYS A 148 ? N LYS A 243 
AA2 3 4 O GLY A 149 ? O GLY A 244 N ILE A 90  ? N ILE A 185 
AA2 4 5 O TRP A 91  ? O TRP A 186 N PHE A 44  ? N PHE A 139 
AA3 1 2 N ILE A 244 ? N ILE A 339 O ARG A 292 ? O ARG A 387 
AA3 2 3 N GLU A 295 ? N GLU A 390 O ASP A 318 ? O ASP A 413 
AA3 3 4 N MET A 321 ? N MET A 416 O SER A 502 ? O SER A 597 
AA3 4 5 O GLY A 505 ? O GLY A 600 N SER A 462 ? N SER A 557 
AA3 5 6 O ILE A 460 ? O ILE A 555 N PHE A 453 ? N PHE A 548 
AA3 6 7 O ASP A 452 ? O ASP A 547 N ILE A 426 ? N ILE A 521 
AA3 7 8 O ILE A 425 ? O ILE A 520 N PHE A 376 ? N PHE A 471 
AA4 1 2 N LEU A 252 ? N LEU A 347 O PHE A 273 ? O PHE A 368 
AA4 2 3 O GLY A 272 ? O GLY A 367 N ILE A 265 ? N ILE A 360 
AA5 1 2 N GLY B 27  ? N GLY B 122 O CYS B 174 ? O CYS B 269 
AA5 2 3 O ALA B 167 ? O ALA B 262 N ILE B 120 ? N ILE B 215 
AA5 3 4 O CYS B 119 ? O CYS B 214 N ILE B 108 ? N ILE B 203 
AA5 4 5 O PHE B 107 ? O PHE B 202 N ARG B 100 ? N ARG B 195 
AA5 5 6 O TRP B 91  ? O TRP B 186 N PHE B 44  ? N PHE B 139 
AA6 1 2 N GLY B 27  ? N GLY B 122 O CYS B 174 ? O CYS B 269 
AA6 2 3 O GLU B 166 ? O GLU B 261 N SER B 152 ? N SER B 247 
AA6 3 4 O ILE B 147 ? O ILE B 242 N VAL B 92  ? N VAL B 187 
AA6 4 5 O TRP B 91  ? O TRP B 186 N PHE B 44  ? N PHE B 139 
AA7 1 2 N ILE B 244 ? N ILE B 339 O ARG B 292 ? O ARG B 387 
AA7 2 3 N GLU B 295 ? N GLU B 390 O ASP B 318 ? O ASP B 413 
AA7 3 4 N LEU B 317 ? N LEU B 412 O ILE B 506 ? O ILE B 601 
AA7 4 5 O GLY B 505 ? O GLY B 600 N SER B 462 ? N SER B 557 
AA7 5 6 O GLU B 458 ? O GLU B 553 N MET B 455 ? N MET B 550 
AA7 6 7 O ASP B 452 ? O ASP B 547 N ILE B 426 ? N ILE B 521 
AA7 7 8 O ILE B 427 ? O ILE B 522 N PHE B 376 ? N PHE B 471 
AA8 1 2 N LEU B 252 ? N LEU B 347 O PHE B 273 ? O PHE B 368 
AA8 2 3 O GLY B 272 ? O GLY B 367 N ILE B 265 ? N ILE B 360 
# 
_pdbx_entry_details.entry_id                   9M5M 
_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     Y 
_pdbx_entry_details.has_protein_modification   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 LYS A 208 ? ? 57.40   -115.52 
2  1 GLU A 237 ? ? 76.51   -2.61   
3  1 GLU A 250 ? ? -54.75  -70.07  
4  1 ASP A 386 ? ? 71.92   -51.71  
5  1 TYR A 420 ? ? -143.16 -21.61  
6  1 SER A 592 ? ? 80.83   154.25  
7  1 LYS B 208 ? ? 55.91   -123.87 
8  1 GLU B 237 ? ? 83.58   -2.30   
9  1 GLU B 352 ? ? -104.44 -159.80 
10 1 PHE B 363 ? ? 39.38   65.20   
11 1 ASP B 386 ? ? 74.19   -49.47  
12 1 SER B 592 ? ? 80.51   156.93  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         18.0167 
_pdbx_refine_tls.origin_y         55.3233 
_pdbx_refine_tls.origin_z         13.7756 
_pdbx_refine_tls.T[1][1]          0.2868 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.0436 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0732 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3180 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0127 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2839 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8543 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.1664 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1331 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9953 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0960 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.7316 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0469 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0498 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0906 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1026 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0036 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0184 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1135 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0452 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.0311 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
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 ALA 96  ? A ALA 1   
2  1 Y 1 A GLU 97  ? A GLU 2   
3  1 Y 1 A LYS 150 ? A LYS 55  
4  1 Y 1 A VAL 151 ? A VAL 56  
5  1 Y 1 A GLY 152 ? A GLY 57  
6  1 Y 1 A GLY 153 ? A GLY 58  
7  1 Y 1 A SER 154 ? A SER 59  
8  1 Y 1 A GLY 155 ? A GLY 60  
9  1 Y 1 A ALA 156 ? A ALA 61  
10 1 Y 1 A THR 157 ? A THR 62  
11 1 Y 1 A ASP 158 ? A ASP 63  
12 1 Y 1 A GLY 159 ? A GLY 64  
13 1 Y 1 A GLY 160 ? A GLY 65  
14 1 Y 1 A LYS 161 ? A LYS 66  
15 1 Y 1 A ARG 162 ? A ARG 67  
16 1 Y 1 A GLU 163 ? A GLU 68  
17 1 Y 1 A ASP 164 ? A ASP 69  
18 1 Y 1 A ASP 165 ? A ASP 70  
19 1 Y 1 A ALA 166 ? A ALA 71  
20 1 Y 1 A ALA 167 ? A ALA 72  
21 1 Y 1 A SER 168 ? A SER 73  
22 1 Y 1 A HIS 169 ? A HIS 74  
23 1 Y 1 A SER 170 ? A SER 75  
24 1 Y 1 A VAL 171 ? A VAL 76  
25 1 Y 1 A VAL 172 ? A VAL 77  
26 1 Y 1 A ALA 173 ? A ALA 78  
27 1 Y 1 A GLU 174 ? A GLU 79  
28 1 Y 1 A SER 175 ? A SER 80  
29 1 Y 1 A ASN 176 ? A ASN 81  
30 1 Y 1 A GLY 177 ? A GLY 82  
31 1 Y 1 A ALA 178 ? A ALA 83  
32 1 Y 1 A SER 351 ? A SER 256 
33 1 Y 1 A GLU 352 ? A GLU 257 
34 1 Y 1 A GLY 353 ? A GLY 258 
35 1 Y 1 A GLY 354 ? A GLY 259 
36 1 Y 1 B ALA 96  ? B ALA 1   
37 1 Y 1 B GLU 97  ? B GLU 2   
38 1 Y 1 B ARG 98  ? B ARG 3   
39 1 Y 1 B GLU 99  ? B GLU 4   
40 1 Y 1 B GLU 133 ? B GLU 38  
41 1 Y 1 B LYS 134 ? B LYS 39  
42 1 Y 1 B LYS 150 ? B LYS 55  
43 1 Y 1 B VAL 151 ? B VAL 56  
44 1 Y 1 B GLY 152 ? B GLY 57  
45 1 Y 1 B GLY 153 ? B GLY 58  
46 1 Y 1 B SER 154 ? B SER 59  
47 1 Y 1 B GLY 155 ? B GLY 60  
48 1 Y 1 B ALA 156 ? B ALA 61  
49 1 Y 1 B THR 157 ? B THR 62  
50 1 Y 1 B ASP 158 ? B ASP 63  
51 1 Y 1 B GLY 159 ? B GLY 64  
52 1 Y 1 B GLY 160 ? B GLY 65  
53 1 Y 1 B LYS 161 ? B LYS 66  
54 1 Y 1 B ARG 162 ? B ARG 67  
55 1 Y 1 B GLU 163 ? B GLU 68  
56 1 Y 1 B ASP 164 ? B ASP 69  
57 1 Y 1 B ASP 165 ? B ASP 70  
58 1 Y 1 B ALA 166 ? B ALA 71  
59 1 Y 1 B ALA 167 ? B ALA 72  
60 1 Y 1 B SER 168 ? B SER 73  
61 1 Y 1 B HIS 169 ? B HIS 74  
62 1 Y 1 B SER 170 ? B SER 75  
63 1 Y 1 B VAL 171 ? B VAL 76  
64 1 Y 1 B VAL 172 ? B VAL 77  
65 1 Y 1 B ALA 173 ? B ALA 78  
66 1 Y 1 B GLU 174 ? B GLU 79  
67 1 Y 1 B SER 175 ? B SER 80  
68 1 Y 1 B ASN 176 ? B ASN 81  
69 1 Y 1 B GLY 177 ? B GLY 82  
70 1 Y 1 B ALA 178 ? B ALA 83  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
EDO C1   C N N 88  
EDO O1   O N N 89  
EDO C2   C N N 90  
EDO O2   O N N 91  
EDO H11  H N N 92  
EDO H12  H N N 93  
EDO HO1  H N N 94  
EDO H21  H N N 95  
EDO H22  H N N 96  
EDO HO2  H N N 97  
GLN N    N N N 98  
GLN CA   C N S 99  
GLN C    C N N 100 
GLN O    O N N 101 
GLN CB   C N N 102 
GLN CG   C N N 103 
GLN CD   C N N 104 
GLN OE1  O N N 105 
GLN NE2  N N N 106 
GLN OXT  O N N 107 
GLN H    H N N 108 
GLN H2   H N N 109 
GLN HA   H N N 110 
GLN HB2  H N N 111 
GLN HB3  H N N 112 
GLN HG2  H N N 113 
GLN HG3  H N N 114 
GLN HE21 H N N 115 
GLN HE22 H N N 116 
GLN HXT  H N N 117 
GLU N    N N N 118 
GLU CA   C N S 119 
GLU C    C N N 120 
GLU O    O N N 121 
GLU CB   C N N 122 
GLU CG   C N N 123 
GLU CD   C N N 124 
GLU OE1  O N N 125 
GLU OE2  O N N 126 
GLU OXT  O N N 127 
GLU H    H N N 128 
GLU H2   H N N 129 
GLU HA   H N N 130 
GLU HB2  H N N 131 
GLU HB3  H N N 132 
GLU HG2  H N N 133 
GLU HG3  H N N 134 
GLU HE2  H N N 135 
GLU HXT  H N N 136 
GLY N    N N N 137 
GLY CA   C N N 138 
GLY C    C N N 139 
GLY O    O N N 140 
GLY OXT  O N N 141 
GLY H    H N N 142 
GLY H2   H N N 143 
GLY HA2  H N N 144 
GLY HA3  H N N 145 
GLY HXT  H N N 146 
HIS N    N N N 147 
HIS CA   C N S 148 
HIS C    C N N 149 
HIS O    O N N 150 
HIS CB   C N N 151 
HIS CG   C Y N 152 
HIS ND1  N Y N 153 
HIS CD2  C Y N 154 
HIS CE1  C Y N 155 
HIS NE2  N Y N 156 
HIS OXT  O N N 157 
HIS H    H N N 158 
HIS H2   H N N 159 
HIS HA   H N N 160 
HIS HB2  H N N 161 
HIS HB3  H N N 162 
HIS HD1  H N N 163 
HIS HD2  H N N 164 
HIS HE1  H N N 165 
HIS HE2  H N N 166 
HIS HXT  H N N 167 
HOH O    O N N 168 
HOH H1   H N N 169 
HOH H2   H N N 170 
ILE N    N N N 171 
ILE CA   C N S 172 
ILE C    C N N 173 
ILE O    O N N 174 
ILE CB   C N S 175 
ILE CG1  C N N 176 
ILE CG2  C N N 177 
ILE CD1  C N N 178 
ILE OXT  O N N 179 
ILE H    H N N 180 
ILE H2   H N N 181 
ILE HA   H N N 182 
ILE HB   H N N 183 
ILE HG12 H N N 184 
ILE HG13 H N N 185 
ILE HG21 H N N 186 
ILE HG22 H N N 187 
ILE HG23 H N N 188 
ILE HD11 H N N 189 
ILE HD12 H N N 190 
ILE HD13 H N N 191 
ILE HXT  H N N 192 
LEU N    N N N 193 
LEU CA   C N S 194 
LEU C    C N N 195 
LEU O    O N N 196 
LEU CB   C N N 197 
LEU CG   C N N 198 
LEU CD1  C N N 199 
LEU CD2  C N N 200 
LEU OXT  O N N 201 
LEU H    H N N 202 
LEU H2   H N N 203 
LEU HA   H N N 204 
LEU HB2  H N N 205 
LEU HB3  H N N 206 
LEU HG   H N N 207 
LEU HD11 H N N 208 
LEU HD12 H N N 209 
LEU HD13 H N N 210 
LEU HD21 H N N 211 
LEU HD22 H N N 212 
LEU HD23 H N N 213 
LEU HXT  H N N 214 
LYS N    N N N 215 
LYS CA   C N S 216 
LYS C    C N N 217 
LYS O    O N N 218 
LYS CB   C N N 219 
LYS CG   C N N 220 
LYS CD   C N N 221 
LYS CE   C N N 222 
LYS NZ   N N N 223 
LYS OXT  O N N 224 
LYS H    H N N 225 
LYS H2   H N N 226 
LYS HA   H N N 227 
LYS HB2  H N N 228 
LYS HB3  H N N 229 
LYS HG2  H N N 230 
LYS HG3  H N N 231 
LYS HD2  H N N 232 
LYS HD3  H N N 233 
LYS HE2  H N N 234 
LYS HE3  H N N 235 
LYS HZ1  H N N 236 
LYS HZ2  H N N 237 
LYS HZ3  H N N 238 
LYS HXT  H N N 239 
MET N    N N N 240 
MET CA   C N S 241 
MET C    C N N 242 
MET O    O N N 243 
MET CB   C N N 244 
MET CG   C N N 245 
MET SD   S N N 246 
MET CE   C N N 247 
MET OXT  O N N 248 
MET H    H N N 249 
MET H2   H N N 250 
MET HA   H N N 251 
MET HB2  H N N 252 
MET HB3  H N N 253 
MET HG2  H N N 254 
MET HG3  H N N 255 
MET HE1  H N N 256 
MET HE2  H N N 257 
MET HE3  H N N 258 
MET HXT  H N N 259 
PHE N    N N N 260 
PHE CA   C N S 261 
PHE C    C N N 262 
PHE O    O N N 263 
PHE CB   C N N 264 
PHE CG   C Y N 265 
PHE CD1  C Y N 266 
PHE CD2  C Y N 267 
PHE CE1  C Y N 268 
PHE CE2  C Y N 269 
PHE CZ   C Y N 270 
PHE OXT  O N N 271 
PHE H    H N N 272 
PHE H2   H N N 273 
PHE HA   H N N 274 
PHE HB2  H N N 275 
PHE HB3  H N N 276 
PHE HD1  H N N 277 
PHE HD2  H N N 278 
PHE HE1  H N N 279 
PHE HE2  H N N 280 
PHE HZ   H N N 281 
PHE HXT  H N N 282 
PRO N    N N N 283 
PRO CA   C N S 284 
PRO C    C N N 285 
PRO O    O N N 286 
PRO CB   C N N 287 
PRO CG   C N N 288 
PRO CD   C N N 289 
PRO OXT  O N N 290 
PRO H    H N N 291 
PRO HA   H N N 292 
PRO HB2  H N N 293 
PRO HB3  H N N 294 
PRO HG2  H N N 295 
PRO HG3  H N N 296 
PRO HD2  H N N 297 
PRO HD3  H N N 298 
PRO HXT  H N N 299 
SER N    N N N 300 
SER CA   C N S 301 
SER C    C N N 302 
SER O    O N N 303 
SER CB   C N N 304 
SER OG   O N N 305 
SER OXT  O N N 306 
SER H    H N N 307 
SER H2   H N N 308 
SER HA   H N N 309 
SER HB2  H N N 310 
SER HB3  H N N 311 
SER HG   H N N 312 
SER HXT  H N N 313 
SO4 S    S N N 314 
SO4 O1   O N N 315 
SO4 O2   O N N 316 
SO4 O3   O N N 317 
SO4 O4   O N N 318 
THR N    N N N 319 
THR CA   C N S 320 
THR C    C N N 321 
THR O    O N N 322 
THR CB   C N R 323 
THR OG1  O N N 324 
THR CG2  C N N 325 
THR OXT  O N N 326 
THR H    H N N 327 
THR H2   H N N 328 
THR HA   H N N 329 
THR HB   H N N 330 
THR HG1  H N N 331 
THR HG21 H N N 332 
THR HG22 H N N 333 
THR HG23 H N N 334 
THR HXT  H N N 335 
TRP N    N N N 336 
TRP CA   C N S 337 
TRP C    C N N 338 
TRP O    O N N 339 
TRP CB   C N N 340 
TRP CG   C Y N 341 
TRP CD1  C Y N 342 
TRP CD2  C Y N 343 
TRP NE1  N Y N 344 
TRP CE2  C Y N 345 
TRP CE3  C Y N 346 
TRP CZ2  C Y N 347 
TRP CZ3  C Y N 348 
TRP CH2  C Y N 349 
TRP OXT  O N N 350 
TRP H    H N N 351 
TRP H2   H N N 352 
TRP HA   H N N 353 
TRP HB2  H N N 354 
TRP HB3  H N N 355 
TRP HD1  H N N 356 
TRP HE1  H N N 357 
TRP HE3  H N N 358 
TRP HZ2  H N N 359 
TRP HZ3  H N N 360 
TRP HH2  H N N 361 
TRP HXT  H N N 362 
TYR N    N N N 363 
TYR CA   C N S 364 
TYR C    C N N 365 
TYR O    O N N 366 
TYR CB   C N N 367 
TYR CG   C Y N 368 
TYR CD1  C Y N 369 
TYR CD2  C Y N 370 
TYR CE1  C Y N 371 
TYR CE2  C Y N 372 
TYR CZ   C Y N 373 
TYR OH   O N N 374 
TYR OXT  O N N 375 
TYR H    H N N 376 
TYR H2   H N N 377 
TYR HA   H N N 378 
TYR HB2  H N N 379 
TYR HB3  H N N 380 
TYR HD1  H N N 381 
TYR HD2  H N N 382 
TYR HE1  H N N 383 
TYR HE2  H N N 384 
TYR HH   H N N 385 
TYR HXT  H N N 386 
VAL N    N N N 387 
VAL CA   C N S 388 
VAL C    C N N 389 
VAL O    O N N 390 
VAL CB   C N N 391 
VAL CG1  C N N 392 
VAL CG2  C N N 393 
VAL OXT  O N N 394 
VAL H    H N N 395 
VAL H2   H N N 396 
VAL HA   H N N 397 
VAL HB   H N N 398 
VAL HG11 H N N 399 
VAL HG12 H N N 400 
VAL HG13 H N N 401 
VAL HG21 H N N 402 
VAL HG22 H N N 403 
VAL HG23 H N N 404 
VAL HXT  H N N 405 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Department of Science & Technology (DST, India)' India CRG/2023/004351    1 
'Indian Council of Medical Research'              India CAR-2024-01-000140 2 
'Department of Biotechnology (DBT, India)'        India PR32713            3 
# 
_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   4J15 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9M5M 
_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]   0.007120 
_atom_sites.fract_transf_matrix[1][2]   0.004111 
_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]   0.008222 
_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]   0.003669 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
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   . ARG A 1 3   ? 17.537  19.615  -40.409 1.00 118.00 ? 98   ARG A N   1 
ATOM   2    C CA  . ARG A 1 3   ? 17.172  19.266  -39.040 1.00 115.58 ? 98   ARG A CA  1 
ATOM   3    C C   . ARG A 1 3   ? 17.512  20.398  -38.080 1.00 120.42 ? 98   ARG A C   1 
ATOM   4    O O   . ARG A 1 3   ? 18.683  20.753  -37.894 1.00 119.17 ? 98   ARG A O   1 
ATOM   5    C CB  . ARG A 1 3   ? 17.869  17.977  -38.602 1.00 112.13 ? 98   ARG A CB  1 
ATOM   6    N N   . GLU A 1 4   ? 16.463  20.955  -37.473 1.00 120.23 ? 99   GLU A N   1 
ATOM   7    C CA  . GLU A 1 4   ? 16.573  22.041  -36.512 1.00 115.75 ? 99   GLU A CA  1 
ATOM   8    C C   . GLU A 1 4   ? 15.792  21.751  -35.238 1.00 114.23 ? 99   GLU A C   1 
ATOM   9    O O   . GLU A 1 4   ? 15.939  22.491  -34.257 1.00 113.58 ? 99   GLU A O   1 
ATOM   10   C CB  . GLU A 1 4   ? 16.076  23.353  -37.143 1.00 121.50 ? 99   GLU A CB  1 
ATOM   11   C CG  . GLU A 1 4   ? 16.258  24.622  -36.328 1.00 124.38 ? 99   GLU A CG  1 
ATOM   12   C CD  . GLU A 1 4   ? 15.315  25.728  -36.785 1.00 126.66 ? 99   GLU A CD  1 
ATOM   13   O OE1 . GLU A 1 4   ? 14.173  25.795  -36.271 1.00 126.17 ? 99   GLU A OE1 1 
ATOM   14   O OE2 . GLU A 1 4   ? 15.701  26.515  -37.679 1.00 127.29 ? 99   GLU A OE2 1 
ATOM   15   N N   . ASN A 1 5   ? 14.975  20.691  -35.221 1.00 110.29 ? 100  ASN A N   1 
ATOM   16   C CA  . ASN A 1 5   ? 14.257  20.315  -34.007 1.00 108.13 ? 100  ASN A CA  1 
ATOM   17   C C   . ASN A 1 5   ? 15.214  19.934  -32.886 1.00 101.65 ? 100  ASN A C   1 
ATOM   18   O O   . ASN A 1 5   ? 14.845  19.999  -31.709 1.00 99.64  ? 100  ASN A O   1 
ATOM   19   C CB  . ASN A 1 5   ? 13.294  19.162  -34.295 1.00 109.10 ? 100  ASN A CB  1 
ATOM   20   N N   . LEU A 1 6   ? 16.440  19.530  -33.228 1.00 103.10 ? 101  LEU A N   1 
ATOM   21   C CA  . LEU A 1 6   ? 17.451  19.275  -32.205 1.00 96.68  ? 101  LEU A CA  1 
ATOM   22   C C   . LEU A 1 6   ? 17.749  20.542  -31.399 1.00 92.05  ? 101  LEU A C   1 
ATOM   23   O O   . LEU A 1 6   ? 17.831  20.505  -30.165 1.00 85.57  ? 101  LEU A O   1 
ATOM   24   C CB  . LEU A 1 6   ? 18.721  18.725  -32.863 1.00 88.14  ? 101  LEU A CB  1 
ATOM   25   N N   . LYS A 1 7   ? 17.895  21.682  -32.087 1.00 93.33  ? 102  LYS A N   1 
ATOM   26   C CA  . LYS A 1 7   ? 18.153  22.946  -31.402 1.00 88.99  ? 102  LYS A CA  1 
ATOM   27   C C   . LYS A 1 7   ? 16.961  23.376  -30.557 1.00 87.84  ? 102  LYS A C   1 
ATOM   28   O O   . LYS A 1 7   ? 17.133  23.951  -29.474 1.00 83.01  ? 102  LYS A O   1 
ATOM   29   C CB  . LYS A 1 7   ? 18.509  24.033  -32.416 1.00 90.80  ? 102  LYS A CB  1 
ATOM   30   N N   . ASN A 1 8   ? 15.742  23.106  -31.026 1.00 90.80  ? 103  ASN A N   1 
ATOM   31   C CA  . ASN A 1 8   ? 14.575  23.484  -30.237 1.00 89.39  ? 103  ASN A CA  1 
ATOM   32   C C   . ASN A 1 8   ? 14.394  22.581  -29.024 1.00 82.86  ? 103  ASN A C   1 
ATOM   33   O O   . ASN A 1 8   ? 13.936  23.045  -27.973 1.00 80.83  ? 103  ASN A O   1 
ATOM   34   C CB  . ASN A 1 8   ? 13.322  23.483  -31.111 1.00 99.43  ? 103  ASN A CB  1 
ATOM   35   C CG  . ASN A 1 8   ? 13.097  24.815  -31.795 1.00 104.58 ? 103  ASN A CG  1 
ATOM   36   O OD1 . ASN A 1 8   ? 14.025  25.415  -32.338 1.00 104.13 ? 103  ASN A OD1 1 
ATOM   37   N ND2 . ASN A 1 8   ? 11.857  25.299  -31.751 1.00 109.44 ? 103  ASN A ND2 1 
ATOM   38   N N   . GLU A 1 9   ? 14.852  21.355  -29.144 1.00 81.36  ? 104  GLU A N   1 
ATOM   39   C CA  . GLU A 1 9   ? 14.775  20.459  -28.037 1.00 82.88  ? 104  GLU A CA  1 
ATOM   40   C C   . GLU A 1 9   ? 15.813  20.930  -27.011 1.00 76.10  ? 104  GLU A C   1 
ATOM   41   O O   . GLU A 1 9   ? 15.533  20.932  -25.838 1.00 71.47  ? 104  GLU A O   1 
ATOM   42   C CB  . GLU A 1 9   ? 14.967  19.023  -28.491 1.00 86.33  ? 104  GLU A CB  1 
ATOM   43   C CG  . GLU A 1 9   ? 13.877  18.060  -28.016 1.00 93.82  ? 104  GLU A CG  1 
ATOM   44   C CD  . GLU A 1 9   ? 12.456  18.517  -28.335 1.00 96.33  ? 104  GLU A CD  1 
ATOM   45   O OE1 . GLU A 1 9   ? 11.552  18.270  -27.521 1.00 95.61  ? 104  GLU A OE1 1 
ATOM   46   O OE2 . GLU A 1 9   ? 12.227  19.125  -29.389 1.00 96.80  ? 104  GLU A OE2 1 
ATOM   47   N N   . ALA A 1 10  ? 16.999  21.323  -27.460 1.00 75.16  ? 105  ALA A N   1 
ATOM   48   C CA  . ALA A 1 10  ? 18.027  21.878  -26.585 1.00 72.43  ? 105  ALA A CA  1 
ATOM   49   C C   . ALA A 1 10  ? 17.529  23.128  -25.872 1.00 66.72  ? 105  ALA A C   1 
ATOM   50   O O   . ALA A 1 10  ? 17.788  23.314  -24.675 1.00 68.02  ? 105  ALA A O   1 
ATOM   51   C CB  . ALA A 1 10  ? 19.294  22.188  -27.386 1.00 71.28  ? 105  ALA A CB  1 
ATOM   52   N N   . THR A 1 11  ? 16.819  23.999  -26.591 1.00 67.15  ? 106  THR A N   1 
ATOM   53   C CA  . THR A 1 11  ? 16.231  25.175  -25.958 1.00 68.08  ? 106  THR A CA  1 
ATOM   54   C C   . THR A 1 11  ? 15.221  24.778  -24.886 1.00 67.32  ? 106  THR A C   1 
ATOM   55   O O   . THR A 1 11  ? 15.195  25.367  -23.797 1.00 63.84  ? 106  THR A O   1 
ATOM   56   C CB  . THR A 1 11  ? 15.580  26.071  -27.009 1.00 70.36  ? 106  THR A CB  1 
ATOM   57   O OG1 . THR A 1 11  ? 16.592  26.583  -27.879 1.00 71.60  ? 106  THR A OG1 1 
ATOM   58   C CG2 . THR A 1 11  ? 14.871  27.246  -26.349 1.00 68.24  ? 106  THR A CG2 1 
ATOM   59   N N   . LYS A 1 12  ? 14.394  23.767  -25.168 1.00 65.57  ? 107  LYS A N   1 
ATOM   60   C CA  . LYS A 1 12  ? 13.520  23.237  -24.126 1.00 65.49  ? 107  LYS A CA  1 
ATOM   61   C C   . LYS A 1 12  ? 14.323  22.840  -22.892 1.00 61.10  ? 107  LYS A C   1 
ATOM   62   O O   . LYS A 1 12  ? 13.891  23.075  -21.760 1.00 59.13  ? 107  LYS A O   1 
ATOM   63   C CB  . LYS A 1 12  ? 12.718  22.042  -24.649 1.00 64.36  ? 107  LYS A CB  1 
ATOM   64   N N   . VAL A 1 13  ? 15.497  22.240  -23.094 1.00 60.21  ? 108  VAL A N   1 
ATOM   65   C CA  . VAL A 1 13  ? 16.294  21.794  -21.951 1.00 58.94  ? 108  VAL A CA  1 
ATOM   66   C C   . VAL A 1 13  ? 16.846  22.984  -21.167 1.00 57.23  ? 108  VAL A C   1 
ATOM   67   O O   . VAL A 1 13  ? 16.787  23.010  -19.932 1.00 55.15  ? 108  VAL A O   1 
ATOM   68   C CB  . VAL A 1 13  ? 17.420  20.853  -22.417 1.00 62.10  ? 108  VAL A CB  1 
ATOM   69   C CG1 . VAL A 1 13  ? 18.381  20.575  -21.264 1.00 56.19  ? 108  VAL A CG1 1 
ATOM   70   C CG2 . VAL A 1 13  ? 16.827  19.551  -22.970 1.00 59.93  ? 108  VAL A CG2 1 
ATOM   71   N N   . LEU A 1 14  ? 17.390  23.986  -21.861 1.00 57.80  ? 109  LEU A N   1 
ATOM   72   C CA  . LEU A 1 14  ? 17.935  25.150  -21.161 1.00 55.00  ? 109  LEU A CA  1 
ATOM   73   C C   . LEU A 1 14  ? 16.875  25.875  -20.341 1.00 57.39  ? 109  LEU A C   1 
ATOM   74   O O   . LEU A 1 14  ? 17.185  26.439  -19.283 1.00 52.59  ? 109  LEU A O   1 
ATOM   75   C CB  . LEU A 1 14  ? 18.565  26.120  -22.156 1.00 55.35  ? 109  LEU A CB  1 
ATOM   76   C CG  . LEU A 1 14  ? 19.723  25.539  -22.969 1.00 58.82  ? 109  LEU A CG  1 
ATOM   77   C CD1 . LEU A 1 14  ? 20.295  26.565  -23.944 1.00 58.40  ? 109  LEU A CD1 1 
ATOM   78   C CD2 . LEU A 1 14  ? 20.790  25.058  -22.014 1.00 55.07  ? 109  LEU A CD2 1 
ATOM   79   N N   . GLU A 1 15  ? 15.629  25.880  -20.806 1.00 55.91  ? 110  GLU A N   1 
ATOM   80   C CA  . GLU A 1 15  ? 14.567  26.635  -20.161 1.00 58.12  ? 110  GLU A CA  1 
ATOM   81   C C   . GLU A 1 15  ? 13.711  25.774  -19.253 1.00 54.42  ? 110  GLU A C   1 
ATOM   82   O O   . GLU A 1 15  ? 12.675  26.246  -18.780 1.00 56.15  ? 110  GLU A O   1 
ATOM   83   C CB  . GLU A 1 15  ? 13.694  27.319  -21.220 1.00 61.44  ? 110  GLU A CB  1 
ATOM   84   C CG  . GLU A 1 15  ? 14.448  28.369  -22.049 1.00 66.26  ? 110  GLU A CG  1 
ATOM   85   C CD  . GLU A 1 15  ? 13.632  28.896  -23.217 1.00 76.61  ? 110  GLU A CD  1 
ATOM   86   O OE1 . GLU A 1 15  ? 12.620  28.252  -23.567 1.00 81.42  ? 110  GLU A OE1 1 
ATOM   87   O OE2 . GLU A 1 15  ? 14.000  29.951  -23.783 1.00 78.55  ? 110  GLU A OE2 1 
ATOM   88   N N   . HIS A 1 16  ? 14.142  24.546  -18.965 1.00 54.39  ? 111  HIS A N   1 
ATOM   89   C CA  . HIS A 1 16  ? 13.266  23.565  -18.335 1.00 55.28  ? 111  HIS A CA  1 
ATOM   90   C C   . HIS A 1 16  ? 12.707  24.040  -16.995 1.00 55.71  ? 111  HIS A C   1 
ATOM   91   O O   . HIS A 1 16  ? 13.451  24.389  -16.072 1.00 53.25  ? 111  HIS A O   1 
ATOM   92   C CB  . HIS A 1 16  ? 13.998  22.244  -18.136 1.00 53.33  ? 111  HIS A CB  1 
ATOM   93   C CG  . HIS A 1 16  ? 13.184  21.236  -17.392 1.00 56.08  ? 111  HIS A CG  1 
ATOM   94   N ND1 . HIS A 1 16  ? 12.051  20.660  -17.925 1.00 56.08  ? 111  HIS A ND1 1 
ATOM   95   C CD2 . HIS A 1 16  ? 13.309  20.734  -16.141 1.00 57.46  ? 111  HIS A CD2 1 
ATOM   96   C CE1 . HIS A 1 16  ? 11.525  19.830  -17.041 1.00 60.29  ? 111  HIS A CE1 1 
ATOM   97   N NE2 . HIS A 1 16  ? 12.269  19.855  -15.950 1.00 57.96  ? 111  HIS A NE2 1 
ATOM   98   N N   . VAL A 1 17  ? 11.382  24.029  -16.893 1.00 59.74  ? 112  VAL A N   1 
ATOM   99   C CA  . VAL A 1 17  ? 10.666  24.324  -15.660 1.00 57.29  ? 112  VAL A CA  1 
ATOM   100  C C   . VAL A 1 17  ? 10.327  23.005  -14.980 1.00 57.81  ? 112  VAL A C   1 
ATOM   101  O O   . VAL A 1 17  ? 9.730   22.114  -15.594 1.00 61.89  ? 112  VAL A O   1 
ATOM   102  C CB  . VAL A 1 17  ? 9.402   25.152  -15.945 1.00 60.90  ? 112  VAL A CB  1 
ATOM   103  C CG1 . VAL A 1 17  ? 8.492   25.218  -14.701 1.00 58.29  ? 112  VAL A CG1 1 
ATOM   104  C CG2 . VAL A 1 17  ? 9.792   26.562  -16.422 1.00 55.90  ? 112  VAL A CG2 1 
ATOM   105  N N   . CYS A 1 18  ? 10.729  22.871  -13.722 1.00 57.03  ? 113  CYS A N   1 
ATOM   106  C CA  . CYS A 1 18  ? 10.448  21.671  -12.947 1.00 61.20  ? 113  CYS A CA  1 
ATOM   107  C C   . CYS A 1 18  ? 9.044   21.754  -12.362 1.00 68.16  ? 113  CYS A C   1 
ATOM   108  O O   . CYS A 1 18  ? 8.690   22.748  -11.720 1.00 68.46  ? 113  CYS A O   1 
ATOM   109  C CB  . CYS A 1 18  ? 11.489  21.511  -11.834 1.00 60.02  ? 113  CYS A CB  1 
ATOM   110  S SG  . CYS A 1 18  ? 11.100  20.298  -10.528 1.00 66.26  ? 113  CYS A SG  1 
ATOM   111  N N   . GLU A 1 19  ? 8.244   20.710  -12.579 1.00 74.75  ? 114  GLU A N   1 
ATOM   112  C CA  . GLU A 1 19  ? 6.884   20.673  -12.057 1.00 76.57  ? 114  GLU A CA  1 
ATOM   113  C C   . GLU A 1 19  ? 6.741   19.828  -10.798 1.00 76.62  ? 114  GLU A C   1 
ATOM   114  O O   . GLU A 1 19  ? 5.743   19.980  -10.084 1.00 81.88  ? 114  GLU A O   1 
ATOM   115  C CB  . GLU A 1 19  ? 5.906   20.158  -13.125 1.00 78.93  ? 114  GLU A CB  1 
ATOM   116  C CG  . GLU A 1 19  ? 5.866   20.997  -14.414 1.00 82.78  ? 114  GLU A CG  1 
ATOM   117  C CD  . GLU A 1 19  ? 5.295   22.405  -14.215 1.00 86.96  ? 114  GLU A CD  1 
ATOM   118  O OE1 . GLU A 1 19  ? 4.862   22.753  -13.089 1.00 87.41  ? 114  GLU A OE1 1 
ATOM   119  O OE2 . GLU A 1 19  ? 5.279   23.171  -15.205 1.00 88.40  ? 114  GLU A OE2 1 
ATOM   120  N N   . ASP A 1 20  ? 7.712   18.963  -10.498 1.00 70.27  ? 115  ASP A N   1 
ATOM   121  C CA  . ASP A 1 20  ? 7.664   18.127  -9.301  1.00 69.53  ? 115  ASP A CA  1 
ATOM   122  C C   . ASP A 1 20  ? 9.098   17.891  -8.845  1.00 67.42  ? 115  ASP A C   1 
ATOM   123  O O   . ASP A 1 20  ? 9.826   17.120  -9.480  1.00 66.96  ? 115  ASP A O   1 
ATOM   124  C CB  . ASP A 1 20  ? 6.949   16.800  -9.590  1.00 71.33  ? 115  ASP A CB  1 
ATOM   125  C CG  . ASP A 1 20  ? 6.562   16.041  -8.319  1.00 74.11  ? 115  ASP A CG  1 
ATOM   126  O OD1 . ASP A 1 20  ? 7.282   16.143  -7.293  1.00 72.52  ? 115  ASP A OD1 1 
ATOM   127  O OD2 . ASP A 1 20  ? 5.532   15.335  -8.349  1.00 80.68  ? 115  ASP A OD2 1 
ATOM   128  N N   . ILE A 1 21  ? 9.506   18.538  -7.748  1.00 65.96  ? 116  ILE A N   1 
ATOM   129  C CA  . ILE A 1 21  ? 10.884  18.377  -7.279  1.00 64.68  ? 116  ILE A CA  1 
ATOM   130  C C   . ILE A 1 21  ? 11.122  17.017  -6.644  1.00 66.53  ? 116  ILE A C   1 
ATOM   131  O O   . ILE A 1 21  ? 12.270  16.695  -6.298  1.00 63.90  ? 116  ILE A O   1 
ATOM   132  C CB  . ILE A 1 21  ? 11.301  19.479  -6.284  1.00 65.36  ? 116  ILE A CB  1 
ATOM   133  C CG1 . ILE A 1 21  ? 10.867  19.143  -4.868  1.00 68.13  ? 116  ILE A CG1 1 
ATOM   134  C CG2 . ILE A 1 21  ? 10.730  20.833  -6.690  1.00 65.79  ? 116  ILE A CG2 1 
ATOM   135  C CD1 . ILE A 1 21  ? 11.191  20.240  -3.878  1.00 69.28  ? 116  ILE A CD1 1 
ATOM   136  N N   . ASN A 1 22  ? 10.069  16.208  -6.478  1.00 67.08  ? 117  ASN A N   1 
ATOM   137  C CA  . ASN A 1 22  ? 10.253  14.834  -6.028  1.00 68.44  ? 117  ASN A CA  1 
ATOM   138  C C   . ASN A 1 22  ? 10.632  13.905  -7.176  1.00 66.26  ? 117  ASN A C   1 
ATOM   139  O O   . ASN A 1 22  ? 11.333  12.911  -6.955  1.00 67.08  ? 117  ASN A O   1 
ATOM   140  C CB  . ASN A 1 22  ? 8.982   14.320  -5.343  1.00 68.45  ? 117  ASN A CB  1 
ATOM   141  C CG  . ASN A 1 22  ? 8.549   15.191  -4.175  1.00 73.65  ? 117  ASN A CG  1 
ATOM   142  O OD1 . ASN A 1 22  ? 9.250   15.302  -3.168  1.00 76.38  ? 117  ASN A OD1 1 
ATOM   143  N ND2 . ASN A 1 22  ? 7.377   15.805  -4.304  1.00 71.76  ? 117  ASN A ND2 1 
ATOM   144  N N   . LYS A 1 23  ? 10.202  14.217  -8.401  1.00 63.03  ? 118  LYS A N   1 
ATOM   145  C CA  . LYS A 1 23  ? 10.497  13.396  -9.566  1.00 65.64  ? 118  LYS A CA  1 
ATOM   146  C C   . LYS A 1 23  ? 11.666  13.918  -10.398 1.00 66.15  ? 118  LYS A C   1 
ATOM   147  O O   . LYS A 1 23  ? 12.142  13.198  -11.280 1.00 64.21  ? 118  LYS A O   1 
ATOM   148  C CB  . LYS A 1 23  ? 9.253   13.278  -10.462 1.00 69.10  ? 118  LYS A CB  1 
ATOM   149  C CG  . LYS A 1 23  ? 7.915   13.148  -9.706  1.00 71.29  ? 118  LYS A CG  1 
ATOM   150  C CD  . LYS A 1 23  ? 7.211   11.829  -10.003 1.00 79.14  ? 118  LYS A CD  1 
ATOM   151  C CE  . LYS A 1 23  ? 5.710   11.890  -9.683  1.00 83.94  ? 118  LYS A CE  1 
ATOM   152  N NZ  . LYS A 1 23  ? 4.921   12.635  -10.719 1.00 81.18  ? 118  LYS A NZ  1 
ATOM   153  N N   . GLU A 1 24  ? 12.146  15.131  -10.136 1.00 63.42  ? 119  GLU A N   1 
ATOM   154  C CA  . GLU A 1 24  ? 13.142  15.782  -10.970 1.00 60.32  ? 119  GLU A CA  1 
ATOM   155  C C   . GLU A 1 24  ? 14.357  16.161  -10.133 1.00 57.81  ? 119  GLU A C   1 
ATOM   156  O O   . GLU A 1 24  ? 14.295  16.202  -8.899  1.00 56.97  ? 119  GLU A O   1 
ATOM   157  C CB  . GLU A 1 24  ? 12.542  17.018  -11.653 1.00 59.72  ? 119  GLU A CB  1 
ATOM   158  C CG  . GLU A 1 24  ? 11.432  16.655  -12.645 1.00 64.99  ? 119  GLU A CG  1 
ATOM   159  C CD  . GLU A 1 24  ? 10.890  17.854  -13.399 1.00 67.64  ? 119  GLU A CD  1 
ATOM   160  O OE1 . GLU A 1 24  ? 9.647   18.005  -13.466 1.00 68.26  ? 119  GLU A OE1 1 
ATOM   161  O OE2 . GLU A 1 24  ? 11.706  18.648  -13.920 1.00 67.17  ? 119  GLU A OE2 1 
ATOM   162  N N   . SER A 1 25  ? 15.478  16.430  -10.817 1.00 54.66  ? 120  SER A N   1 
ATOM   163  C CA  . SER A 1 25  ? 16.684  16.887  -10.139 1.00 51.95  ? 120  SER A CA  1 
ATOM   164  C C   . SER A 1 25  ? 17.145  18.288  -10.521 1.00 49.96  ? 120  SER A C   1 
ATOM   165  O O   . SER A 1 25  ? 18.105  18.780  -9.916  1.00 50.20  ? 120  SER A O   1 
ATOM   166  C CB  . SER A 1 25  ? 17.844  15.911  -10.374 1.00 54.60  ? 120  SER A CB  1 
ATOM   167  O OG  . SER A 1 25  ? 17.705  14.750  -9.575  1.00 61.43  ? 120  SER A OG  1 
ATOM   168  N N   . TYR A 1 26  ? 16.517  18.946  -11.495 1.00 47.61  ? 121  TYR A N   1 
ATOM   169  C CA  . TYR A 1 26  ? 16.944  20.297  -11.853 1.00 48.12  ? 121  TYR A CA  1 
ATOM   170  C C   . TYR A 1 26  ? 15.798  21.031  -12.524 1.00 48.67  ? 121  TYR A C   1 
ATOM   171  O O   . TYR A 1 26  ? 14.865  20.416  -13.040 1.00 53.12  ? 121  TYR A O   1 
ATOM   172  C CB  . TYR A 1 26  ? 18.162  20.278  -12.787 1.00 48.00  ? 121  TYR A CB  1 
ATOM   173  C CG  . TYR A 1 26  ? 17.848  19.721  -14.162 1.00 46.01  ? 121  TYR A CG  1 
ATOM   174  C CD1 . TYR A 1 26  ? 17.823  18.342  -14.385 1.00 50.95  ? 121  TYR A CD1 1 
ATOM   175  C CD2 . TYR A 1 26  ? 17.553  20.565  -15.231 1.00 45.99  ? 121  TYR A CD2 1 
ATOM   176  C CE1 . TYR A 1 26  ? 17.533  17.818  -15.643 1.00 52.28  ? 121  TYR A CE1 1 
ATOM   177  C CE2 . TYR A 1 26  ? 17.253  20.044  -16.499 1.00 50.35  ? 121  TYR A CE2 1 
ATOM   178  C CZ  . TYR A 1 26  ? 17.246  18.674  -16.692 1.00 52.87  ? 121  TYR A CZ  1 
ATOM   179  O OH  . TYR A 1 26  ? 16.955  18.154  -17.936 1.00 53.69  ? 121  TYR A OH  1 
ATOM   180  N N   . GLY A 1 27  ? 15.896  22.350  -12.553 1.00 48.65  ? 122  GLY A N   1 
ATOM   181  C CA  . GLY A 1 27  ? 14.938  23.176  -13.259 1.00 46.66  ? 122  GLY A CA  1 
ATOM   182  C C   . GLY A 1 27  ? 14.642  24.476  -12.529 1.00 46.95  ? 122  GLY A C   1 
ATOM   183  O O   . GLY A 1 27  ? 14.974  24.667  -11.353 1.00 45.67  ? 122  GLY A O   1 
ATOM   184  N N   . PHE A 1 28  ? 14.055  25.420  -13.259 1.00 47.77  ? 123  PHE A N   1 
ATOM   185  C CA  . PHE A 1 28  ? 13.495  26.610  -12.643 1.00 48.50  ? 123  PHE A CA  1 
ATOM   186  C C   . PHE A 1 28  ? 12.219  26.218  -11.920 1.00 50.32  ? 123  PHE A C   1 
ATOM   187  O O   . PHE A 1 28  ? 11.426  25.425  -12.434 1.00 55.69  ? 123  PHE A O   1 
ATOM   188  C CB  . PHE A 1 28  ? 13.230  27.678  -13.697 1.00 49.34  ? 123  PHE A CB  1 
ATOM   189  C CG  . PHE A 1 28  ? 14.445  28.025  -14.505 1.00 48.73  ? 123  PHE A CG  1 
ATOM   190  C CD1 . PHE A 1 28  ? 15.420  28.863  -13.982 1.00 47.72  ? 123  PHE A CD1 1 
ATOM   191  C CD2 . PHE A 1 28  ? 14.630  27.491  -15.773 1.00 50.74  ? 123  PHE A CD2 1 
ATOM   192  C CE1 . PHE A 1 28  ? 16.563  29.175  -14.724 1.00 47.11  ? 123  PHE A CE1 1 
ATOM   193  C CE2 . PHE A 1 28  ? 15.765  27.793  -16.515 1.00 50.70  ? 123  PHE A CE2 1 
ATOM   194  C CZ  . PHE A 1 28  ? 16.735  28.635  -15.989 1.00 49.35  ? 123  PHE A CZ  1 
ATOM   195  N N   . VAL A 1 29  ? 12.068  26.703  -10.692 1.00 48.06  ? 124  VAL A N   1 
ATOM   196  C CA  . VAL A 1 29  ? 10.940  26.324  -9.852  1.00 53.34  ? 124  VAL A CA  1 
ATOM   197  C C   . VAL A 1 29  ? 10.317  27.569  -9.254  1.00 53.69  ? 124  VAL A C   1 
ATOM   198  O O   . VAL A 1 29  ? 11.007  28.541  -8.929  1.00 55.03  ? 124  VAL A O   1 
ATOM   199  C CB  . VAL A 1 29  ? 11.335  25.347  -8.719  1.00 53.57  ? 124  VAL A CB  1 
ATOM   200  C CG1 . VAL A 1 29  ? 11.750  24.019  -9.273  1.00 55.17  ? 124  VAL A CG1 1 
ATOM   201  C CG2 . VAL A 1 29  ? 12.433  25.936  -7.866  1.00 53.71  ? 124  VAL A CG2 1 
ATOM   202  N N   . LYS A 1 30  ? 8.997   27.537  -9.110  1.00 58.85  ? 125  LYS A N   1 
ATOM   203  C CA  . LYS A 1 30  ? 8.323   28.501  -8.259  1.00 58.87  ? 125  LYS A CA  1 
ATOM   204  C C   . LYS A 1 30  ? 8.520   28.097  -6.809  1.00 57.26  ? 125  LYS A C   1 
ATOM   205  O O   . LYS A 1 30  ? 8.644   26.912  -6.486  1.00 57.44  ? 125  LYS A O   1 
ATOM   206  C CB  . LYS A 1 30  ? 6.831   28.586  -8.587  1.00 63.86  ? 125  LYS A CB  1 
ATOM   207  C CG  . LYS A 1 30  ? 6.517   29.169  -9.960  1.00 65.87  ? 125  LYS A CG  1 
ATOM   208  C CD  . LYS A 1 30  ? 5.049   29.567  -10.068 1.00 74.15  ? 125  LYS A CD  1 
ATOM   209  C CE  . LYS A 1 30  ? 4.887   31.007  -10.570 1.00 75.42  ? 125  LYS A CE  1 
ATOM   210  N NZ  . LYS A 1 30  ? 4.862   31.096  -12.058 1.00 79.45  ? 125  LYS A NZ  1 
ATOM   211  N N   . ILE A 1 31  ? 8.586   29.105  -5.937  1.00 57.32  ? 126  ILE A N   1 
ATOM   212  C CA  . ILE A 1 31  ? 8.705   28.860  -4.504  1.00 58.59  ? 126  ILE A CA  1 
ATOM   213  C C   . ILE A 1 31  ? 7.569   27.973  -4.001  1.00 62.12  ? 126  ILE A C   1 
ATOM   214  O O   . ILE A 1 31  ? 7.769   27.141  -3.106  1.00 62.68  ? 126  ILE A O   1 
ATOM   215  C CB  . ILE A 1 31  ? 8.749   30.210  -3.760  1.00 60.62  ? 126  ILE A CB  1 
ATOM   216  C CG1 . ILE A 1 31  ? 10.081  30.905  -4.009  1.00 59.70  ? 126  ILE A CG1 1 
ATOM   217  C CG2 . ILE A 1 31  ? 8.571   30.009  -2.278  1.00 53.46  ? 126  ILE A CG2 1 
ATOM   218  C CD1 . ILE A 1 31  ? 11.249  30.154  -3.415  1.00 52.73  ? 126  ILE A CD1 1 
ATOM   219  N N   . SER A 1 32  ? 6.387   28.111  -4.567  1.00 61.75  ? 127  SER A N   1 
ATOM   220  C CA  . SER A 1 32  ? 5.259   27.318  -4.122  1.00 66.92  ? 127  SER A CA  1 
ATOM   221  C C   . SER A 1 32  ? 5.425   25.840  -4.365  1.00 68.82  ? 127  SER A C   1 
ATOM   222  O O   . SER A 1 32  ? 4.873   25.038  -3.663  1.00 71.80  ? 127  SER A O   1 
ATOM   223  C CB  . SER A 1 32  ? 3.970   27.803  -4.760  1.00 65.47  ? 127  SER A CB  1 
ATOM   224  O OG  . SER A 1 32  ? 4.004   27.684  -6.152  1.00 68.32  ? 127  SER A OG  1 
ATOM   225  N N   . LYS A 1 33  ? 6.219   25.478  -5.347  1.00 68.25  ? 128  LYS A N   1 
ATOM   226  C CA  . LYS A 1 33  ? 6.420   24.086  -5.661  1.00 69.28  ? 128  LYS A CA  1 
ATOM   227  C C   . LYS A 1 33  ? 7.512   23.430  -4.861  1.00 69.67  ? 128  LYS A C   1 
ATOM   228  O O   . LYS A 1 33  ? 7.703   22.256  -4.972  1.00 71.88  ? 128  LYS A O   1 
ATOM   229  C CB  . LYS A 1 33  ? 6.707   23.905  -7.138  1.00 70.78  ? 128  LYS A CB  1 
ATOM   230  C CG  . LYS A 1 33  ? 5.529   24.186  -8.029  1.00 71.84  ? 128  LYS A CG  1 
ATOM   231  C CD  . LYS A 1 33  ? 5.549   23.269  -9.233  1.00 77.86  ? 128  LYS A CD  1 
ATOM   232  C CE  . LYS A 1 33  ? 4.137   22.965  -9.695  1.00 80.93  ? 128  LYS A CE  1 
ATOM   233  N NZ  . LYS A 1 33  ? 4.040   21.819  -10.633 1.00 81.19  ? 128  LYS A NZ  1 
ATOM   234  N N   . MET A 1 34  ? 8.207   24.151  -4.005  1.00 69.11  ? 129  MET A N   1 
ATOM   235  C CA  . MET A 1 34  ? 9.283   23.534  -3.248  1.00 68.21  ? 129  MET A CA  1 
ATOM   236  C C   . MET A 1 34  ? 8.801   22.791  -2.010  1.00 73.48  ? 129  MET A C   1 
ATOM   237  O O   . MET A 1 34  ? 9.078   23.173  -0.902  1.00 74.14  ? 129  MET A O   1 
ATOM   238  C CB  . MET A 1 34  ? 10.303  24.583  -2.834  1.00 62.70  ? 129  MET A CB  1 
ATOM   239  C CG  . MET A 1 34  ? 11.051  25.246  -3.968  1.00 56.24  ? 129  MET A CG  1 
ATOM   240  S SD  . MET A 1 34  ? 12.259  24.167  -4.720  1.00 69.16  ? 129  MET A SD  1 
ATOM   241  C CE  . MET A 1 34  ? 13.535  24.102  -3.496  1.00 53.37  ? 129  MET A CE  1 
ATOM   242  N N   . LYS A 1 35  ? 8.133   21.676  -2.226  1.00 80.29  ? 130  LYS A N   1 
ATOM   243  C CA  . LYS A 1 35  ? 7.594   20.849  -1.179  1.00 85.65  ? 130  LYS A CA  1 
ATOM   244  C C   . LYS A 1 35  ? 8.125   19.467  -1.420  1.00 84.32  ? 130  LYS A C   1 
ATOM   245  O O   . LYS A 1 35  ? 7.746   18.808  -2.357  1.00 83.77  ? 130  LYS A O   1 
ATOM   246  C CB  . LYS A 1 35  ? 6.071   20.824  -1.267  1.00 88.39  ? 130  LYS A CB  1 
ATOM   247  C CG  . LYS A 1 35  ? 5.384   22.075  -0.772  1.00 85.77  ? 130  LYS A CG  1 
ATOM   248  C CD  . LYS A 1 35  ? 5.268   22.066  0.736   1.00 93.08  ? 130  LYS A CD  1 
ATOM   249  N N   . GLU A 1 36  ? 9.036   19.032  -0.561  1.00 85.86  ? 131  GLU A N   1 
ATOM   250  C CA  . GLU A 1 36  ? 9.652   17.716  -0.652  1.00 86.55  ? 131  GLU A CA  1 
ATOM   251  C C   . GLU A 1 36  ? 8.878   16.734  0.216   1.00 94.53  ? 131  GLU A C   1 
ATOM   252  O O   . GLU A 1 36  ? 8.824   16.875  1.429   1.00 97.35  ? 131  GLU A O   1 
ATOM   253  C CB  . GLU A 1 36  ? 11.120  17.773  -0.217  1.00 77.19  ? 131  GLU A CB  1 
ATOM   254  C CG  . GLU A 1 36  ? 11.957  16.593  -0.670  1.00 78.90  ? 131  GLU A CG  1 
ATOM   255  C CD  . GLU A 1 36  ? 13.362  16.542  -0.088  1.00 71.98  ? 131  GLU A CD  1 
ATOM   256  O OE1 . GLU A 1 36  ? 13.561  16.887  1.075   1.00 77.63  ? 131  GLU A OE1 1 
ATOM   257  O OE2 . GLU A 1 36  ? 14.275  16.107  -0.788  1.00 65.04  ? 131  GLU A OE2 1 
ATOM   258  N N   . ASN A 1 37  ? 8.265   15.750  -0.432  1.00 94.83  ? 132  ASN A N   1 
ATOM   259  C CA  . ASN A 1 37  ? 7.429   14.729  0.201   1.00 99.07  ? 132  ASN A CA  1 
ATOM   260  C C   . ASN A 1 37  ? 6.258   15.310  0.985   1.00 107.73 ? 132  ASN A C   1 
ATOM   261  O O   . ASN A 1 37  ? 5.955   14.852  2.076   1.00 108.62 ? 132  ASN A O   1 
ATOM   262  C CB  . ASN A 1 37  ? 8.234   13.749  1.053   1.00 100.93 ? 132  ASN A CB  1 
ATOM   263  N N   . GLU A 1 38  ? 5.668   16.379  0.437   1.00 109.67 ? 133  GLU A N   1 
ATOM   264  C CA  . GLU A 1 38  ? 4.506   17.112  0.972   1.00 110.82 ? 133  GLU A CA  1 
ATOM   265  C C   . GLU A 1 38  ? 4.725   17.773  2.333   1.00 111.60 ? 133  GLU A C   1 
ATOM   266  O O   . GLU A 1 38  ? 3.787   18.077  3.044   1.00 110.73 ? 133  GLU A O   1 
ATOM   267  C CB  . GLU A 1 38  ? 3.258   16.223  0.998   1.00 113.37 ? 133  GLU A CB  1 
ATOM   268  N N   . LYS A 1 39  ? 5.968   18.060  2.650   1.00 110.09 ? 134  LYS A N   1 
ATOM   269  C CA  . LYS A 1 39  ? 6.323   18.627  3.913   1.00 109.63 ? 134  LYS A CA  1 
ATOM   270  C C   . LYS A 1 39  ? 7.424   19.635  3.690   1.00 108.25 ? 134  LYS A C   1 
ATOM   271  O O   . LYS A 1 39  ? 8.014   19.718  2.618   1.00 107.63 ? 134  LYS A O   1 
ATOM   272  C CB  . LYS A 1 39  ? 6.767   17.529  4.871   1.00 110.43 ? 134  LYS A CB  1 
ATOM   273  N N   . GLU A 1 40  ? 7.663   20.449  4.693   1.00 106.04 ? 135  GLU A N   1 
ATOM   274  C CA  . GLU A 1 40  ? 8.677   21.458  4.574   1.00 98.61  ? 135  GLU A CA  1 
ATOM   275  C C   . GLU A 1 40  ? 10.103  20.926  4.484   1.00 93.59  ? 135  GLU A C   1 
ATOM   276  O O   . GLU A 1 40  ? 10.451  19.898  5.045   1.00 92.18  ? 135  GLU A O   1 
ATOM   277  C CB  . GLU A 1 40  ? 8.564   22.420  5.752   1.00 97.79  ? 135  GLU A CB  1 
ATOM   278  C CG  . GLU A 1 40  ? 9.216   23.768  5.527   1.00 97.29  ? 135  GLU A CG  1 
ATOM   279  C CD  . GLU A 1 40  ? 8.723   24.806  6.506   1.00 101.71 ? 135  GLU A CD  1 
ATOM   280  O OE1 . GLU A 1 40  ? 9.432   25.794  6.751   1.00 98.53  ? 135  GLU A OE1 1 
ATOM   281  O OE2 . GLU A 1 40  ? 7.616   24.628  7.030   1.00 106.65 ? 135  GLU A OE2 1 
ATOM   282  N N   . ILE A 1 41  ? 10.894  21.655  3.719   1.00 80.96  ? 136  ILE A N   1 
ATOM   283  C CA  . ILE A 1 41  ? 12.329  21.457  3.547   1.00 68.53  ? 136  ILE A CA  1 
ATOM   284  C C   . ILE A 1 41  ? 13.062  22.211  4.650   1.00 64.64  ? 136  ILE A C   1 
ATOM   285  O O   . ILE A 1 41  ? 12.760  23.379  4.915   1.00 68.50  ? 136  ILE A O   1 
ATOM   286  C CB  . ILE A 1 41  ? 12.775  21.954  2.161   1.00 64.33  ? 136  ILE A CB  1 
ATOM   287  C CG1 . ILE A 1 41  ? 12.285  21.020  1.049   1.00 67.31  ? 136  ILE A CG1 1 
ATOM   288  C CG2 . ILE A 1 41  ? 14.285  22.140  2.109   1.00 58.87  ? 136  ILE A CG2 1 
ATOM   289  C CD1 . ILE A 1 41  ? 12.439  21.615  -0.350  1.00 61.25  ? 136  ILE A CD1 1 
ATOM   290  N N   . ARG A 1 42  ? 14.038  21.561  5.281   1.00 57.48  ? 137  ARG A N   1 
ATOM   291  C CA  . ARG A 1 42  ? 14.920  22.240  6.231   1.00 56.87  ? 137  ARG A CA  1 
ATOM   292  C C   . ARG A 1 42  ? 16.049  22.933  5.472   1.00 55.86  ? 137  ARG A C   1 
ATOM   293  O O   . ARG A 1 42  ? 17.067  22.318  5.140   1.00 53.30  ? 137  ARG A O   1 
ATOM   294  C CB  . ARG A 1 42  ? 15.471  21.264  7.263   1.00 59.13  ? 137  ARG A CB  1 
ATOM   295  C CG  . ARG A 1 42  ? 16.144  21.982  8.436   1.00 63.66  ? 137  ARG A CG  1 
ATOM   296  C CD  . ARG A 1 42  ? 16.697  21.020  9.483   1.00 69.72  ? 137  ARG A CD  1 
ATOM   297  N NE  . ARG A 1 42  ? 17.540  21.725  10.445  1.00 76.04  ? 137  ARG A NE  1 
ATOM   298  C CZ  . ARG A 1 42  ? 18.227  21.140  11.419  1.00 77.76  ? 137  ARG A CZ  1 
ATOM   299  N NH1 . ARG A 1 42  ? 18.166  19.833  11.621  1.00 78.27  ? 137  ARG A NH1 1 
ATOM   300  N NH2 . ARG A 1 42  ? 19.005  21.885  12.205  1.00 78.18  ? 137  ARG A NH2 1 
ATOM   301  N N   . LEU A 1 43  ? 15.894  24.236  5.236   1.00 56.04  ? 138  LEU A N   1 
ATOM   302  C CA  . LEU A 1 43  ? 16.779  24.996  4.364   1.00 51.46  ? 138  LEU A CA  1 
ATOM   303  C C   . LEU A 1 43  ? 17.833  25.736  5.182   1.00 53.46  ? 138  LEU A C   1 
ATOM   304  O O   . LEU A 1 43  ? 17.489  26.519  6.068   1.00 54.55  ? 138  LEU A O   1 
ATOM   305  C CB  . LEU A 1 43  ? 15.970  25.990  3.536   1.00 49.51  ? 138  LEU A CB  1 
ATOM   306  C CG  . LEU A 1 43  ? 16.755  26.834  2.534   1.00 46.83  ? 138  LEU A CG  1 
ATOM   307  C CD1 . LEU A 1 43  ? 17.445  25.938  1.493   1.00 43.17  ? 138  LEU A CD1 1 
ATOM   308  C CD2 . LEU A 1 43  ? 15.854  27.877  1.878   1.00 40.85  ? 138  LEU A CD2 1 
ATOM   309  N N   . PHE A 1 44  ? 19.108  25.520  4.855   1.00 48.62  ? 139  PHE A N   1 
ATOM   310  C CA  . PHE A 1 44  ? 20.225  26.222  5.475   1.00 48.92  ? 139  PHE A CA  1 
ATOM   311  C C   . PHE A 1 44  ? 20.696  27.388  4.613   1.00 47.25  ? 139  PHE A C   1 
ATOM   312  O O   . PHE A 1 44  ? 20.501  27.407  3.398   1.00 45.55  ? 139  PHE A O   1 
ATOM   313  C CB  . PHE A 1 44  ? 21.397  25.270  5.713   1.00 48.47  ? 139  PHE A CB  1 
ATOM   314  C CG  . PHE A 1 44  ? 21.142  24.238  6.771   1.00 54.11  ? 139  PHE A CG  1 
ATOM   315  C CD1 . PHE A 1 44  ? 21.487  24.479  8.092   1.00 57.45  ? 139  PHE A CD1 1 
ATOM   316  C CD2 . PHE A 1 44  ? 20.571  23.019  6.445   1.00 51.47  ? 139  PHE A CD2 1 
ATOM   317  C CE1 . PHE A 1 44  ? 21.259  23.516  9.073   1.00 61.51  ? 139  PHE A CE1 1 
ATOM   318  C CE2 . PHE A 1 44  ? 20.336  22.064  7.415   1.00 58.70  ? 139  PHE A CE2 1 
ATOM   319  C CZ  . PHE A 1 44  ? 20.681  22.312  8.730   1.00 62.15  ? 139  PHE A CZ  1 
ATOM   320  N N   . ASN A 1 45  ? 21.318  28.371  5.258   1.00 47.62  ? 140  ASN A N   1 
ATOM   321  C CA  . ASN A 1 45  ? 22.082  29.400  4.564   1.00 50.03  ? 140  ASN A CA  1 
ATOM   322  C C   . ASN A 1 45  ? 23.562  29.208  4.878   1.00 47.62  ? 140  ASN A C   1 
ATOM   323  O O   . ASN A 1 45  ? 23.933  28.481  5.793   1.00 44.95  ? 140  ASN A O   1 
ATOM   324  C CB  . ASN A 1 45  ? 21.612  30.821  4.931   1.00 48.53  ? 140  ASN A CB  1 
ATOM   325  C CG  . ASN A 1 45  ? 21.833  31.172  6.401   1.00 49.71  ? 140  ASN A CG  1 
ATOM   326  O OD1 . ASN A 1 45  ? 22.964  31.280  6.860   1.00 49.94  ? 140  ASN A OD1 1 
ATOM   327  N ND2 . ASN A 1 45  ? 20.746  31.371  7.135   1.00 53.07  ? 140  ASN A ND2 1 
ATOM   328  N N   . LEU A 1 46  ? 24.414  29.860  4.089   1.00 44.66  ? 141  LEU A N   1 
ATOM   329  C CA  . LEU A 1 46  ? 25.845  29.629  4.214   1.00 47.30  ? 141  LEU A CA  1 
ATOM   330  C C   . LEU A 1 46  ? 26.426  30.160  5.524   1.00 48.81  ? 141  LEU A C   1 
ATOM   331  O O   . LEU A 1 46  ? 27.483  29.685  5.953   1.00 47.78  ? 141  LEU A O   1 
ATOM   332  C CB  . LEU A 1 46  ? 26.576  30.255  3.024   1.00 43.15  ? 141  LEU A CB  1 
ATOM   333  C CG  . LEU A 1 46  ? 26.387  29.515  1.691   1.00 47.27  ? 141  LEU A CG  1 
ATOM   334  C CD1 . LEU A 1 46  ? 27.215  30.164  0.594   1.00 45.89  ? 141  LEU A CD1 1 
ATOM   335  C CD2 . LEU A 1 46  ? 26.770  28.034  1.844   1.00 47.63  ? 141  LEU A CD2 1 
ATOM   336  N N   . GLU A 1 47  ? 25.792  31.158  6.143   1.00 44.62  ? 142  GLU A N   1 
ATOM   337  C CA  . GLU A 1 47  ? 26.283  31.669  7.421   1.00 50.66  ? 142  GLU A CA  1 
ATOM   338  C C   . GLU A 1 47  ? 26.125  30.628  8.531   1.00 47.33  ? 142  GLU A C   1 
ATOM   339  O O   . GLU A 1 47  ? 27.041  30.419  9.339   1.00 46.63  ? 142  GLU A O   1 
ATOM   340  C CB  . GLU A 1 47  ? 25.546  32.972  7.760   1.00 46.58  ? 142  GLU A CB  1 
ATOM   341  C CG  . GLU A 1 47  ? 25.786  33.482  9.169   1.00 49.93  ? 142  GLU A CG  1 
ATOM   342  C CD  . GLU A 1 47  ? 25.209  34.874  9.402   1.00 49.62  ? 142  GLU A CD  1 
ATOM   343  O OE1 . GLU A 1 47  ? 24.112  35.175  8.901   1.00 49.04  ? 142  GLU A OE1 1 
ATOM   344  O OE2 . GLU A 1 47  ? 25.871  35.682  10.072  1.00 54.89  ? 142  GLU A OE2 1 
ATOM   345  N N   . GLU A 1 48  ? 24.975  29.953  8.574   1.00 47.44  ? 143  GLU A N   1 
ATOM   346  C CA  . GLU A 1 48  ? 24.784  28.869  9.529   1.00 49.25  ? 143  GLU A CA  1 
ATOM   347  C C   . GLU A 1 48  ? 25.791  27.756  9.304   1.00 51.43  ? 143  GLU A C   1 
ATOM   348  O O   . GLU A 1 48  ? 26.351  27.214  10.263  1.00 51.46  ? 143  GLU A O   1 
ATOM   349  C CB  . GLU A 1 48  ? 23.364  28.312  9.418   1.00 51.00  ? 143  GLU A CB  1 
ATOM   350  C CG  . GLU A 1 48  ? 22.280  29.352  9.420   1.00 53.60  ? 143  GLU A CG  1 
ATOM   351  C CD  . GLU A 1 48  ? 20.897  28.750  9.182   1.00 60.91  ? 143  GLU A CD  1 
ATOM   352  O OE1 . GLU A 1 48  ? 20.178  28.492  10.175  1.00 64.32  ? 143  GLU A OE1 1 
ATOM   353  O OE2 . GLU A 1 48  ? 20.528  28.524  8.006   1.00 62.04  ? 143  GLU A OE2 1 
ATOM   354  N N   . ILE A 1 49  ? 26.011  27.378  8.044   1.00 50.12  ? 144  ILE A N   1 
ATOM   355  C CA  . ILE A 1 49  ? 26.974  26.322  7.748   1.00 52.36  ? 144  ILE A CA  1 
ATOM   356  C C   . ILE A 1 49  ? 28.359  26.731  8.219   1.00 51.47  ? 144  ILE A C   1 
ATOM   357  O O   . ILE A 1 49  ? 29.070  25.954  8.869   1.00 51.11  ? 144  ILE A O   1 
ATOM   358  C CB  . ILE A 1 49  ? 26.969  25.988  6.243   1.00 49.07  ? 144  ILE A CB  1 
ATOM   359  C CG1 . ILE A 1 49  ? 25.626  25.370  5.833   1.00 49.15  ? 144  ILE A CG1 1 
ATOM   360  C CG2 . ILE A 1 49  ? 28.143  25.071  5.901   1.00 49.13  ? 144  ILE A CG2 1 
ATOM   361  C CD1 . ILE A 1 49  ? 25.436  25.260  4.324   1.00 50.67  ? 144  ILE A CD1 1 
ATOM   362  N N   . TYR A 1 50  ? 28.766  27.959  7.892   1.00 48.72  ? 145  TYR A N   1 
ATOM   363  C CA  . TYR A 1 50  ? 30.077  28.422  8.328   1.00 52.20  ? 145  TYR A CA  1 
ATOM   364  C C   . TYR A 1 50  ? 30.213  28.327  9.845   1.00 55.70  ? 145  TYR A C   1 
ATOM   365  O O   . TYR A 1 50  ? 31.214  27.820  10.358  1.00 55.53  ? 145  TYR A O   1 
ATOM   366  C CB  . TYR A 1 50  ? 30.314  29.856  7.860   1.00 51.71  ? 145  TYR A CB  1 
ATOM   367  C CG  . TYR A 1 50  ? 31.620  30.437  8.369   1.00 55.47  ? 145  TYR A CG  1 
ATOM   368  C CD1 . TYR A 1 50  ? 32.811  30.236  7.675   1.00 51.85  ? 145  TYR A CD1 1 
ATOM   369  C CD2 . TYR A 1 50  ? 31.663  31.176  9.553   1.00 56.41  ? 145  TYR A CD2 1 
ATOM   370  C CE1 . TYR A 1 50  ? 34.003  30.750  8.134   1.00 54.74  ? 145  TYR A CE1 1 
ATOM   371  C CE2 . TYR A 1 50  ? 32.850  31.701  10.021  1.00 57.13  ? 145  TYR A CE2 1 
ATOM   372  C CZ  . TYR A 1 50  ? 34.020  31.483  9.311   1.00 59.79  ? 145  TYR A CZ  1 
ATOM   373  O OH  . TYR A 1 50  ? 35.196  32.006  9.786   1.00 55.16  ? 145  TYR A OH  1 
ATOM   374  N N   . HIS A 1 51  ? 29.203  28.793  10.585  1.00 54.19  ? 146  HIS A N   1 
ATOM   375  C CA  . HIS A 1 51  ? 29.371  28.834  12.037  1.00 57.16  ? 146  HIS A CA  1 
ATOM   376  C C   . HIS A 1 51  ? 29.283  27.447  12.659  1.00 56.19  ? 146  HIS A C   1 
ATOM   377  O O   . HIS A 1 51  ? 30.023  27.145  13.600  1.00 60.85  ? 146  HIS A O   1 
ATOM   378  C CB  . HIS A 1 51  ? 28.383  29.819  12.657  1.00 55.90  ? 146  HIS A CB  1 
ATOM   379  C CG  . HIS A 1 51  ? 28.833  31.239  12.497  1.00 60.21  ? 146  HIS A CG  1 
ATOM   380  N ND1 . HIS A 1 51  ? 28.298  32.092  11.556  1.00 59.15  ? 146  HIS A ND1 1 
ATOM   381  C CD2 . HIS A 1 51  ? 29.841  31.922  13.093  1.00 62.52  ? 146  HIS A CD2 1 
ATOM   382  C CE1 . HIS A 1 51  ? 28.924  33.255  11.612  1.00 62.37  ? 146  HIS A CE1 1 
ATOM   383  N NE2 . HIS A 1 51  ? 29.866  33.178  12.535  1.00 65.38  ? 146  HIS A NE2 1 
ATOM   384  N N   . SER A 1 52  ? 28.440  26.568  12.119  1.00 57.24  ? 147  SER A N   1 
ATOM   385  C CA  . SER A 1 52  ? 28.415  25.200  12.624  1.00 57.02  ? 147  SER A CA  1 
ATOM   386  C C   . SER A 1 52  ? 29.727  24.474  12.357  1.00 59.64  ? 147  SER A C   1 
ATOM   387  O O   . SER A 1 52  ? 30.172  23.672  13.185  1.00 62.02  ? 147  SER A O   1 
ATOM   388  C CB  . SER A 1 52  ? 27.255  24.418  12.014  1.00 58.23  ? 147  SER A CB  1 
ATOM   389  O OG  . SER A 1 52  ? 26.017  24.968  12.400  1.00 62.75  ? 147  SER A OG  1 
ATOM   390  N N   . LEU A 1 53  ? 30.365  24.728  11.209  1.00 59.38  ? 148  LEU A N   1 
ATOM   391  C CA  . LEU A 1 53  ? 31.490  23.891  10.798  1.00 58.30  ? 148  LEU A CA  1 
ATOM   392  C C   . LEU A 1 53  ? 32.860  24.517  11.018  1.00 60.36  ? 148  LEU A C   1 
ATOM   393  O O   . LEU A 1 53  ? 33.840  23.782  11.131  1.00 62.21  ? 148  LEU A O   1 
ATOM   394  C CB  . LEU A 1 53  ? 31.374  23.509  9.314   1.00 59.45  ? 148  LEU A CB  1 
ATOM   395  C CG  . LEU A 1 53  ? 30.166  22.701  8.829   1.00 62.22  ? 148  LEU A CG  1 
ATOM   396  C CD1 . LEU A 1 53  ? 30.363  22.261  7.391   1.00 61.09  ? 148  LEU A CD1 1 
ATOM   397  C CD2 . LEU A 1 53  ? 29.907  21.498  9.713   1.00 64.68  ? 148  LEU A CD2 1 
ATOM   398  N N   . MET A 1 54  ? 32.981  25.838  11.057  1.00 59.19  ? 149  MET A N   1 
ATOM   399  C CA  . MET A 1 54  ? 34.321  26.434  11.035  1.00 64.92  ? 149  MET A CA  1 
ATOM   400  C C   . MET A 1 54  ? 34.723  27.048  12.379  1.00 63.00  ? 149  MET A C   1 
ATOM   401  O O   . MET A 1 54  ? 33.884  27.591  13.099  1.00 70.43  ? 149  MET A O   1 
ATOM   402  C CB  . MET A 1 54  ? 34.413  27.489  9.916   1.00 62.74  ? 149  MET A CB  1 
ATOM   403  C CG  . MET A 1 54  ? 34.112  26.966  8.490   1.00 58.14  ? 149  MET A CG  1 
ATOM   404  S SD  . MET A 1 54  ? 35.188  25.615  7.898   1.00 67.82  ? 149  MET A SD  1 
ATOM   405  C CE  . MET A 1 54  ? 36.825  26.305  8.186   1.00 63.54  ? 149  MET A CE  1 
ATOM   406  N N   . HIS A 1 84  ? 25.265  17.093  12.364  1.00 86.87  ? 179  HIS A N   1 
ATOM   407  C CA  . HIS A 1 84  ? 23.929  17.120  11.763  1.00 90.40  ? 179  HIS A CA  1 
ATOM   408  C C   . HIS A 1 84  ? 23.974  17.562  10.296  1.00 89.69  ? 179  HIS A C   1 
ATOM   409  O O   . HIS A 1 84  ? 23.198  17.080  9.464   1.00 86.18  ? 179  HIS A O   1 
ATOM   410  C CB  . HIS A 1 84  ? 22.988  18.033  12.569  1.00 91.26  ? 179  HIS A CB  1 
ATOM   411  C CG  . HIS A 1 84  ? 23.417  19.471  12.625  1.00 93.20  ? 179  HIS A CG  1 
ATOM   412  N ND1 . HIS A 1 84  ? 24.657  19.867  13.084  1.00 92.93  ? 179  HIS A ND1 1 
ATOM   413  C CD2 . HIS A 1 84  ? 22.758  20.610  12.297  1.00 90.10  ? 179  HIS A CD2 1 
ATOM   414  C CE1 . HIS A 1 84  ? 24.746  21.185  13.024  1.00 91.09  ? 179  HIS A CE1 1 
ATOM   415  N NE2 . HIS A 1 84  ? 23.608  21.660  12.550  1.00 88.54  ? 179  HIS A NE2 1 
ATOM   416  N N   . LEU A 1 85  ? 24.889  18.484  9.986   1.00 81.72  ? 180  LEU A N   1 
ATOM   417  C CA  . LEU A 1 85  ? 25.115  18.903  8.609   1.00 75.21  ? 180  LEU A CA  1 
ATOM   418  C C   . LEU A 1 85  ? 25.904  17.882  7.808   1.00 74.22  ? 180  LEU A C   1 
ATOM   419  O O   . LEU A 1 85  ? 25.909  17.958  6.576   1.00 69.49  ? 180  LEU A O   1 
ATOM   420  C CB  . LEU A 1 85  ? 25.866  20.234  8.569   1.00 70.91  ? 180  LEU A CB  1 
ATOM   421  C CG  . LEU A 1 85  ? 25.101  21.476  8.996   1.00 70.69  ? 180  LEU A CG  1 
ATOM   422  C CD1 . LEU A 1 85  ? 26.058  22.634  9.175   1.00 64.67  ? 180  LEU A CD1 1 
ATOM   423  C CD2 . LEU A 1 85  ? 24.064  21.803  7.951   1.00 65.72  ? 180  LEU A CD2 1 
ATOM   424  N N   . LEU A 1 86  ? 26.575  16.943  8.475   1.00 73.22  ? 181  LEU A N   1 
ATOM   425  C CA  . LEU A 1 86  ? 27.460  15.998  7.810   1.00 74.01  ? 181  LEU A CA  1 
ATOM   426  C C   . LEU A 1 86  ? 26.869  14.600  7.680   1.00 73.68  ? 181  LEU A C   1 
ATOM   427  O O   . LEU A 1 86  ? 27.484  13.744  7.034   1.00 75.05  ? 181  LEU A O   1 
ATOM   428  C CB  . LEU A 1 86  ? 28.796  15.917  8.562   1.00 71.23  ? 181  LEU A CB  1 
ATOM   429  C CG  . LEU A 1 86  ? 29.520  17.253  8.749   1.00 72.08  ? 181  LEU A CG  1 
ATOM   430  C CD1 . LEU A 1 86  ? 30.770  17.071  9.589   1.00 68.58  ? 181  LEU A CD1 1 
ATOM   431  C CD2 . LEU A 1 86  ? 29.868  17.872  7.397   1.00 69.71  ? 181  LEU A CD2 1 
ATOM   432  N N   . GLN A 1 87  ? 25.694  14.351  8.256   1.00 73.11  ? 182  GLN A N   1 
ATOM   433  C CA  . GLN A 1 87  ? 25.156  12.995  8.287   1.00 75.64  ? 182  GLN A CA  1 
ATOM   434  C C   . GLN A 1 87  ? 24.509  12.616  6.959   1.00 74.12  ? 182  GLN A C   1 
ATOM   435  O O   . GLN A 1 87  ? 24.807  11.558  6.399   1.00 75.28  ? 182  GLN A O   1 
ATOM   436  C CB  . GLN A 1 87  ? 24.152  12.855  9.434   1.00 77.71  ? 182  GLN A CB  1 
ATOM   437  N N   . SER A 1 88  ? 23.618  13.457  6.440   1.00 72.69  ? 183  SER A N   1 
ATOM   438  C CA  . SER A 1 88  ? 22.864  13.110  5.240   1.00 70.28  ? 183  SER A CA  1 
ATOM   439  C C   . SER A 1 88  ? 22.839  14.314  4.304   1.00 63.36  ? 183  SER A C   1 
ATOM   440  O O   . SER A 1 88  ? 23.522  15.318  4.528   1.00 60.66  ? 183  SER A O   1 
ATOM   441  C CB  . SER A 1 88  ? 21.449  12.641  5.602   1.00 72.85  ? 183  SER A CB  1 
ATOM   442  O OG  . SER A 1 88  ? 20.828  12.023  4.484   1.00 74.43  ? 183  SER A OG  1 
ATOM   443  N N   . ASP A 1 89  ? 22.050  14.193  3.237   1.00 60.03  ? 184  ASP A N   1 
ATOM   444  C CA  . ASP A 1 89  ? 21.858  15.297  2.307   1.00 59.04  ? 184  ASP A CA  1 
ATOM   445  C C   . ASP A 1 89  ? 21.162  16.464  2.996   1.00 56.68  ? 184  ASP A C   1 
ATOM   446  O O   . ASP A 1 89  ? 20.218  16.277  3.767   1.00 58.62  ? 184  ASP A O   1 
ATOM   447  C CB  . ASP A 1 89  ? 21.024  14.852  1.109   1.00 57.33  ? 184  ASP A CB  1 
ATOM   448  C CG  . ASP A 1 89  ? 21.726  13.828  0.248   1.00 60.17  ? 184  ASP A CG  1 
ATOM   449  O OD1 . ASP A 1 89  ? 22.966  13.707  0.326   1.00 60.71  ? 184  ASP A OD1 1 
ATOM   450  O OD2 . ASP A 1 89  ? 21.025  13.149  -0.526  1.00 67.73  ? 184  ASP A OD2 1 
ATOM   451  N N   . ILE A 1 90  ? 21.611  17.676  2.690   1.00 52.27  ? 185  ILE A N   1 
ATOM   452  C CA  . ILE A 1 90  ? 20.998  18.886  3.217   1.00 53.03  ? 185  ILE A CA  1 
ATOM   453  C C   . ILE A 1 90  ? 20.599  19.787  2.052   1.00 51.02  ? 185  ILE A C   1 
ATOM   454  O O   . ILE A 1 90  ? 21.040  19.610  0.912   1.00 52.57  ? 185  ILE A O   1 
ATOM   455  C CB  . ILE A 1 90  ? 21.941  19.633  4.185   1.00 55.82  ? 185  ILE A CB  1 
ATOM   456  C CG1 . ILE A 1 90  ? 23.195  20.100  3.443   1.00 55.30  ? 185  ILE A CG1 1 
ATOM   457  C CG2 . ILE A 1 90  ? 22.324  18.729  5.367   1.00 56.51  ? 185  ILE A CG2 1 
ATOM   458  C CD1 . ILE A 1 90  ? 23.963  21.169  4.158   1.00 55.69  ? 185  ILE A CD1 1 
ATOM   459  N N   . TRP A 1 91  ? 19.751  20.765  2.357   1.00 47.91  ? 186  TRP A N   1 
ATOM   460  C CA  . TRP A 1 91  ? 19.330  21.795  1.419   1.00 48.21  ? 186  TRP A CA  1 
ATOM   461  C C   . TRP A 1 91  ? 19.982  23.116  1.796   1.00 48.87  ? 186  TRP A C   1 
ATOM   462  O O   . TRP A 1 91  ? 19.987  23.498  2.975   1.00 47.08  ? 186  TRP A O   1 
ATOM   463  C CB  . TRP A 1 91  ? 17.812  21.961  1.423   1.00 46.02  ? 186  TRP A CB  1 
ATOM   464  C CG  . TRP A 1 91  ? 17.056  20.883  0.703   1.00 52.49  ? 186  TRP A CG  1 
ATOM   465  C CD1 . TRP A 1 91  ? 16.557  19.716  1.237   1.00 51.39  ? 186  TRP A CD1 1 
ATOM   466  C CD2 . TRP A 1 91  ? 16.674  20.884  -0.678  1.00 51.16  ? 186  TRP A CD2 1 
ATOM   467  N NE1 . TRP A 1 91  ? 15.901  19.001  0.271   1.00 53.56  ? 186  TRP A NE1 1 
ATOM   468  C CE2 . TRP A 1 91  ? 15.954  19.692  -0.912  1.00 53.53  ? 186  TRP A CE2 1 
ATOM   469  C CE3 . TRP A 1 91  ? 16.884  21.770  -1.745  1.00 50.40  ? 186  TRP A CE3 1 
ATOM   470  C CZ2 . TRP A 1 91  ? 15.434  19.369  -2.165  1.00 55.83  ? 186  TRP A CZ2 1 
ATOM   471  C CZ3 . TRP A 1 91  ? 16.371  21.446  -2.993  1.00 49.76  ? 186  TRP A CZ3 1 
ATOM   472  C CH2 . TRP A 1 91  ? 15.652  20.254  -3.190  1.00 52.19  ? 186  TRP A CH2 1 
ATOM   473  N N   . VAL A 1 92  ? 20.525  23.810  0.798   1.00 44.88  ? 187  VAL A N   1 
ATOM   474  C CA  . VAL A 1 92  ? 21.178  25.100  1.007   1.00 43.15  ? 187  VAL A CA  1 
ATOM   475  C C   . VAL A 1 92  ? 20.777  26.037  -0.125  1.00 43.34  ? 187  VAL A C   1 
ATOM   476  O O   . VAL A 1 92  ? 20.684  25.624  -1.287  1.00 44.44  ? 187  VAL A O   1 
ATOM   477  C CB  . VAL A 1 92  ? 22.716  24.947  1.093   1.00 43.93  ? 187  VAL A CB  1 
ATOM   478  C CG1 . VAL A 1 92  ? 23.277  24.342  -0.197  1.00 46.87  ? 187  VAL A CG1 1 
ATOM   479  C CG2 . VAL A 1 92  ? 23.374  26.281  1.359   1.00 44.42  ? 187  VAL A CG2 1 
ATOM   480  N N   . ARG A 1 93  ? 20.544  27.295  0.211   1.00 39.38  ? 188  ARG A N   1 
ATOM   481  C CA  . ARG A 1 93  ? 20.233  28.339  -0.754  1.00 40.29  ? 188  ARG A CA  1 
ATOM   482  C C   . ARG A 1 93  ? 21.432  29.265  -0.897  1.00 44.32  ? 188  ARG A C   1 
ATOM   483  O O   . ARG A 1 93  ? 22.181  29.492  0.058   1.00 47.18  ? 188  ARG A O   1 
ATOM   484  C CB  . ARG A 1 93  ? 18.998  29.151  -0.325  1.00 41.63  ? 188  ARG A CB  1 
ATOM   485  C CG  . ARG A 1 93  ? 18.641  30.313  -1.257  1.00 40.87  ? 188  ARG A CG  1 
ATOM   486  C CD  . ARG A 1 93  ? 17.235  30.846  -0.995  1.00 40.92  ? 188  ARG A CD  1 
ATOM   487  N NE  . ARG A 1 93  ? 16.210  29.826  -1.214  1.00 41.66  ? 188  ARG A NE  1 
ATOM   488  C CZ  . ARG A 1 93  ? 14.940  29.953  -0.848  1.00 43.02  ? 188  ARG A CZ  1 
ATOM   489  N NH1 . ARG A 1 93  ? 14.500  31.052  -0.248  1.00 39.12  ? 188  ARG A NH1 1 
ATOM   490  N NH2 . ARG A 1 93  ? 14.086  28.959  -1.098  1.00 41.27  ? 188  ARG A NH2 1 
ATOM   491  N N   . GLY A 1 94  ? 21.618  29.807  -2.091  1.00 41.56  ? 189  GLY A N   1 
ATOM   492  C CA  . GLY A 1 94  ? 22.621  30.855  -2.216  1.00 42.17  ? 189  GLY A CA  1 
ATOM   493  C C   . GLY A 1 94  ? 22.652  31.443  -3.606  1.00 42.36  ? 189  GLY A C   1 
ATOM   494  O O   . GLY A 1 94  ? 21.937  30.995  -4.518  1.00 41.33  ? 189  GLY A O   1 
ATOM   495  N N   . ARG A 1 95  ? 23.527  32.442  -3.772  1.00 39.04  ? 190  ARG A N   1 
ATOM   496  C CA  . ARG A 1 95  ? 23.712  33.066  -5.076  1.00 41.89  ? 190  ARG A CA  1 
ATOM   497  C C   . ARG A 1 95  ? 24.890  32.428  -5.789  1.00 41.79  ? 190  ARG A C   1 
ATOM   498  O O   . ARG A 1 95  ? 25.909  32.114  -5.168  1.00 38.40  ? 190  ARG A O   1 
ATOM   499  C CB  . ARG A 1 95  ? 23.934  34.574  -4.960  1.00 39.53  ? 190  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 95  ? 22.653  35.355  -5.015  1.00 43.98  ? 190  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 95  ? 22.902  36.852  -5.126  1.00 42.36  ? 190  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 95  ? 21.673  37.555  -5.477  1.00 43.48  ? 190  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 95  ? 21.378  38.795  -5.108  1.00 42.47  ? 190  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 95  ? 22.177  39.493  -4.315  1.00 39.43  ? 190  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 95  ? 20.255  39.351  -5.549  1.00 41.60  ? 190  ARG A NH2 1 
ATOM   506  N N   . ILE A 1 96  ? 24.741  32.236  -7.095  1.00 38.65  ? 191  ILE A N   1 
ATOM   507  C CA  . ILE A 1 96  ? 25.841  31.706  -7.893  1.00 42.06  ? 191  ILE A CA  1 
ATOM   508  C C   . ILE A 1 96  ? 26.894  32.784  -8.113  1.00 42.42  ? 191  ILE A C   1 
ATOM   509  O O   . ILE A 1 96  ? 26.727  33.679  -8.949  1.00 40.76  ? 191  ILE A O   1 
ATOM   510  C CB  . ILE A 1 96  ? 25.335  31.130  -9.228  1.00 41.48  ? 191  ILE A CB  1 
ATOM   511  C CG1 . ILE A 1 96  ? 24.452  29.899  -8.964  1.00 41.55  ? 191  ILE A CG1 1 
ATOM   512  C CG2 . ILE A 1 96  ? 26.497  30.756  -10.102 1.00 41.23  ? 191  ILE A CG2 1 
ATOM   513  C CD1 . ILE A 1 96  ? 23.777  29.384  -10.211 1.00 41.80  ? 191  ILE A CD1 1 
ATOM   514  N N   . HIS A 1 97  ? 27.989  32.688  -7.356  1.00 40.10  ? 192  HIS A N   1 
ATOM   515  C CA  . HIS A 1 97  ? 29.106  33.615  -7.469  1.00 41.75  ? 192  HIS A CA  1 
ATOM   516  C C   . HIS A 1 97  ? 29.933  33.319  -8.712  1.00 45.96  ? 192  HIS A C   1 
ATOM   517  O O   . HIS A 1 97  ? 30.382  34.240  -9.402  1.00 44.94  ? 192  HIS A O   1 
ATOM   518  C CB  . HIS A 1 97  ? 29.963  33.504  -6.205  1.00 41.74  ? 192  HIS A CB  1 
ATOM   519  C CG  . HIS A 1 97  ? 31.055  34.518  -6.114  1.00 47.36  ? 192  HIS A CG  1 
ATOM   520  N ND1 . HIS A 1 97  ? 30.812  35.863  -5.912  1.00 45.24  ? 192  HIS A ND1 1 
ATOM   521  C CD2 . HIS A 1 97  ? 32.403  34.376  -6.140  1.00 44.56  ? 192  HIS A CD2 1 
ATOM   522  C CE1 . HIS A 1 97  ? 31.964  36.507  -5.851  1.00 45.91  ? 192  HIS A CE1 1 
ATOM   523  N NE2 . HIS A 1 97  ? 32.944  35.628  -5.988  1.00 47.08  ? 192  HIS A NE2 1 
ATOM   524  N N   . ASP A 1 98  ? 30.120  32.036  -9.021  1.00 43.00  ? 193  ASP A N   1 
ATOM   525  C CA  . ASP A 1 98  ? 30.949  31.581  -10.126 1.00 44.37  ? 193  ASP A CA  1 
ATOM   526  C C   . ASP A 1 98  ? 30.501  30.172  -10.495 1.00 46.34  ? 193  ASP A C   1 
ATOM   527  O O   . ASP A 1 98  ? 30.111  29.399  -9.612  1.00 42.35  ? 193  ASP A O   1 
ATOM   528  C CB  . ASP A 1 98  ? 32.436  31.586  -9.734  1.00 41.68  ? 193  ASP A CB  1 
ATOM   529  C CG  . ASP A 1 98  ? 33.377  31.347  -10.924 1.00 51.15  ? 193  ASP A CG  1 
ATOM   530  O OD1 . ASP A 1 98  ? 33.075  31.773  -12.068 1.00 53.06  ? 193  ASP A OD1 1 
ATOM   531  O OD2 . ASP A 1 98  ? 34.415  30.692  -10.706 1.00 50.63  ? 193  ASP A OD2 1 
ATOM   532  N N   . ILE A 1 99  ? 30.538  29.855  -11.798 1.00 46.02  ? 194  ILE A N   1 
ATOM   533  C CA  . ILE A 1 99  ? 30.386  28.496  -12.323 1.00 46.41  ? 194  ILE A CA  1 
ATOM   534  C C   . ILE A 1 99  ? 31.548  28.210  -13.254 1.00 46.56  ? 194  ILE A C   1 
ATOM   535  O O   . ILE A 1 99  ? 31.794  28.981  -14.189 1.00 52.53  ? 194  ILE A O   1 
ATOM   536  C CB  . ILE A 1 99  ? 29.089  28.283  -13.125 1.00 47.53  ? 194  ILE A CB  1 
ATOM   537  C CG1 . ILE A 1 99  ? 27.850  28.516  -12.319 1.00 49.51  ? 194  ILE A CG1 1 
ATOM   538  C CG2 . ILE A 1 99  ? 29.020  26.847  -13.631 1.00 47.82  ? 194  ILE A CG2 1 
ATOM   539  C CD1 . ILE A 1 99  ? 26.610  28.203  -13.138 1.00 53.02  ? 194  ILE A CD1 1 
ATOM   540  N N   . ARG A 1 100 ? 32.232  27.092  -13.042 1.00 46.53  ? 195  ARG A N   1 
ATOM   541  C CA  . ARG A 1 100 ? 33.280  26.651  -13.955 1.00 48.47  ? 195  ARG A CA  1 
ATOM   542  C C   . ARG A 1 100 ? 32.905  25.280  -14.502 1.00 49.32  ? 195  ARG A C   1 
ATOM   543  O O   . ARG A 1 100 ? 32.856  24.302  -13.746 1.00 47.78  ? 195  ARG A O   1 
ATOM   544  C CB  . ARG A 1 100 ? 34.639  26.595  -13.256 1.00 52.23  ? 195  ARG A CB  1 
ATOM   545  C CG  . ARG A 1 100 ? 35.231  27.980  -12.982 1.00 55.15  ? 195  ARG A CG  1 
ATOM   546  C CD  . ARG A 1 100 ? 35.942  28.057  -11.633 1.00 51.86  ? 195  ARG A CD  1 
ATOM   547  N NE  . ARG A 1 100 ? 36.701  26.859  -11.285 1.00 60.45  ? 195  ARG A NE  1 
ATOM   548  C CZ  . ARG A 1 100 ? 36.606  26.232  -10.118 1.00 61.17  ? 195  ARG A CZ  1 
ATOM   549  N NH1 . ARG A 1 100 ? 35.814  26.683  -9.151  1.00 58.36  ? 195  ARG A NH1 1 
ATOM   550  N NH2 . ARG A 1 100 ? 37.335  25.135  -9.908  1.00 59.04  ? 195  ARG A NH2 1 
ATOM   551  N N   . SER A 1 101 ? 32.659  25.216  -15.794 1.00 46.60  ? 196  SER A N   1 
ATOM   552  C CA  . SER A 1 101 ? 32.317  23.980  -16.452 1.00 44.53  ? 196  SER A CA  1 
ATOM   553  C C   . SER A 1 101 ? 33.569  23.242  -16.912 1.00 44.67  ? 196  SER A C   1 
ATOM   554  O O   . SER A 1 101 ? 34.425  23.807  -17.528 1.00 45.94  ? 196  SER A O   1 
ATOM   555  C CB  . SER A 1 101 ? 31.439  24.269  -17.635 1.00 45.24  ? 196  SER A CB  1 
ATOM   556  O OG  . SER A 1 101 ? 30.116  24.428  -17.259 1.00 45.17  ? 196  SER A OG  1 
ATOM   557  N N   . LYS A 1 102 ? 33.668  21.975  -16.558 1.00 43.62  ? 197  LYS A N   1 
ATOM   558  C CA  . LYS A 1 102 ? 34.797  21.142  -16.925 1.00 46.06  ? 197  LYS A CA  1 
ATOM   559  C C   . LYS A 1 102 ? 34.382  19.733  -17.360 1.00 47.95  ? 197  LYS A C   1 
ATOM   560  O O   . LYS A 1 102 ? 34.660  18.784  -16.697 1.00 46.33  ? 197  LYS A O   1 
ATOM   561  C CB  . LYS A 1 102 ? 35.799  21.078  -15.782 1.00 46.86  ? 197  LYS A CB  1 
ATOM   562  C CG  . LYS A 1 102 ? 36.523  22.378  -15.503 1.00 46.12  ? 197  LYS A CG  1 
ATOM   563  C CD  . LYS A 1 102 ? 37.578  22.252  -14.449 1.00 50.05  ? 197  LYS A CD  1 
ATOM   564  C CE  . LYS A 1 102 ? 38.231  23.584  -14.214 1.00 52.70  ? 197  LYS A CE  1 
ATOM   565  N NZ  . LYS A 1 102 ? 39.557  23.447  -13.589 1.00 54.56  ? 197  LYS A NZ  1 
ATOM   566  N N   . GLY A 1 103 ? 33.701  19.642  -18.484 1.00 47.66  ? 198  GLY A N   1 
ATOM   567  C CA  . GLY A 1 103 ? 33.243  18.387  -19.031 1.00 47.35  ? 198  GLY A CA  1 
ATOM   568  C C   . GLY A 1 103 ? 32.191  17.695  -18.214 1.00 47.49  ? 198  GLY A C   1 
ATOM   569  O O   . GLY A 1 103 ? 31.102  18.175  -18.107 1.00 45.79  ? 198  GLY A O   1 
ATOM   570  N N   . SER A 1 104 ? 32.520  16.536  -17.685 1.00 47.43  ? 199  SER A N   1 
ATOM   571  C CA  . SER A 1 104 ? 31.597  15.806  -16.825 1.00 47.33  ? 199  SER A CA  1 
ATOM   572  C C   . SER A 1 104 ? 31.507  16.387  -15.422 1.00 50.42  ? 199  SER A C   1 
ATOM   573  O O   . SER A 1 104 ? 30.688  15.912  -14.628 1.00 52.75  ? 199  SER A O   1 
ATOM   574  C CB  . SER A 1 104 ? 32.011  14.338  -16.744 1.00 48.35  ? 199  SER A CB  1 
ATOM   575  O OG  . SER A 1 104 ? 31.990  13.757  -18.039 1.00 54.48  ? 199  SER A OG  1 
ATOM   576  N N   . LEU A 1 105 ? 32.313  17.396  -15.100 1.00 48.08  ? 200  LEU A N   1 
ATOM   577  C CA  . LEU A 1 105 ? 32.225  18.104  -13.829 1.00 46.03  ? 200  LEU A CA  1 
ATOM   578  C C   . LEU A 1 105 ? 31.806  19.552  -14.047 1.00 48.71  ? 200  LEU A C   1 
ATOM   579  O O   . LEU A 1 105 ? 32.070  20.141  -15.098 1.00 46.89  ? 200  LEU A O   1 
ATOM   580  C CB  . LEU A 1 105 ? 33.574  18.059  -13.098 1.00 48.77  ? 200  LEU A CB  1 
ATOM   581  C CG  . LEU A 1 105 ? 34.097  16.652  -12.791 1.00 54.33  ? 200  LEU A CG  1 
ATOM   582  C CD1 . LEU A 1 105 ? 35.597  16.653  -12.477 1.00 55.66  ? 200  LEU A CD1 1 
ATOM   583  C CD2 . LEU A 1 105 ? 33.320  16.082  -11.616 1.00 55.91  ? 200  LEU A CD2 1 
ATOM   584  N N   . ALA A 1 106 ? 31.126  20.117  -13.048 1.00 46.31  ? 201  ALA A N   1 
ATOM   585  C CA  . ALA A 1 106 ? 30.862  21.544  -12.992 1.00 47.19  ? 201  ALA A CA  1 
ATOM   586  C C   . ALA A 1 106 ? 31.035  22.007  -11.555 1.00 50.01  ? 201  ALA A C   1 
ATOM   587  O O   . ALA A 1 106 ? 30.564  21.351  -10.620 1.00 49.17  ? 201  ALA A O   1 
ATOM   588  C CB  . ALA A 1 106 ? 29.457  21.910  -13.489 1.00 47.23  ? 201  ALA A CB  1 
ATOM   589  N N   . PHE A 1 107 ? 31.698  23.145  -11.386 1.00 46.31  ? 202  PHE A N   1 
ATOM   590  C CA  . PHE A 1 107 ? 32.011  23.692  -10.072 1.00 48.68  ? 202  PHE A CA  1 
ATOM   591  C C   . PHE A 1 107 ? 31.289  25.016  -9.915  1.00 48.52  ? 202  PHE A C   1 
ATOM   592  O O   . PHE A 1 107 ? 31.511  25.939  -10.704 1.00 47.85  ? 202  PHE A O   1 
ATOM   593  C CB  . PHE A 1 107 ? 33.520  23.881  -9.909  1.00 48.97  ? 202  PHE A CB  1 
ATOM   594  C CG  . PHE A 1 107 ? 34.300  22.631  -10.137 1.00 48.72  ? 202  PHE A CG  1 
ATOM   595  C CD1 . PHE A 1 107 ? 34.696  22.266  -11.415 1.00 51.55  ? 202  PHE A CD1 1 
ATOM   596  C CD2 . PHE A 1 107 ? 34.611  21.795  -9.080  1.00 51.66  ? 202  PHE A CD2 1 
ATOM   597  C CE1 . PHE A 1 107 ? 35.418  21.098  -11.637 1.00 51.63  ? 202  PHE A CE1 1 
ATOM   598  C CE2 . PHE A 1 107 ? 35.333  20.630  -9.291  1.00 52.19  ? 202  PHE A CE2 1 
ATOM   599  C CZ  . PHE A 1 107 ? 35.740  20.281  -10.576 1.00 51.91  ? 202  PHE A CZ  1 
ATOM   600  N N   . ILE A 1 108 ? 30.444  25.107  -8.888  1.00 47.24  ? 203  ILE A N   1 
ATOM   601  C CA  . ILE A 1 108 ? 29.662  26.290  -8.571  1.00 46.78  ? 203  ILE A CA  1 
ATOM   602  C C   . ILE A 1 108 ? 30.158  26.840  -7.246  1.00 49.56  ? 203  ILE A C   1 
ATOM   603  O O   . ILE A 1 108 ? 30.186  26.112  -6.251  1.00 48.91  ? 203  ILE A O   1 
ATOM   604  C CB  . ILE A 1 108 ? 28.165  25.948  -8.455  1.00 48.76  ? 203  ILE A CB  1 
ATOM   605  C CG1 . ILE A 1 108 ? 27.585  25.465  -9.787  1.00 52.31  ? 203  ILE A CG1 1 
ATOM   606  C CG2 . ILE A 1 108 ? 27.384  27.127  -7.915  1.00 46.83  ? 203  ILE A CG2 1 
ATOM   607  C CD1 . ILE A 1 108 ? 26.133  24.994  -9.654  1.00 50.72  ? 203  ILE A CD1 1 
ATOM   608  N N   . ILE A 1 109 ? 30.502  28.125  -7.205  1.00 49.97  ? 204  ILE A N   1 
ATOM   609  C CA  . ILE A 1 109 ? 30.722  28.804  -5.931  1.00 43.34  ? 204  ILE A CA  1 
ATOM   610  C C   . ILE A 1 109 ? 29.404  29.439  -5.518  1.00 48.05  ? 204  ILE A C   1 
ATOM   611  O O   . ILE A 1 109 ? 28.854  30.257  -6.260  1.00 45.85  ? 204  ILE A O   1 
ATOM   612  C CB  . ILE A 1 109 ? 31.831  29.861  -6.027  1.00 47.04  ? 204  ILE A CB  1 
ATOM   613  C CG1 . ILE A 1 109 ? 33.125  29.243  -6.571  1.00 47.37  ? 204  ILE A CG1 1 
ATOM   614  C CG2 . ILE A 1 109 ? 32.066  30.498  -4.654  1.00 44.65  ? 204  ILE A CG2 1 
ATOM   615  C CD1 . ILE A 1 109 ? 33.639  28.105  -5.736  1.00 49.42  ? 204  ILE A CD1 1 
ATOM   616  N N   . LEU A 1 110 ? 28.870  29.029  -4.362  1.00 44.75  ? 205  LEU A N   1 
ATOM   617  C CA  . LEU A 1 110 ? 27.711  29.677  -3.766  1.00 44.31  ? 205  LEU A CA  1 
ATOM   618  C C   . LEU A 1 110 ? 28.163  30.750  -2.787  1.00 44.56  ? 205  LEU A C   1 
ATOM   619  O O   . LEU A 1 110 ? 29.137  30.557  -2.049  1.00 44.08  ? 205  LEU A O   1 
ATOM   620  C CB  . LEU A 1 110 ? 26.831  28.679  -3.008  1.00 44.90  ? 205  LEU A CB  1 
ATOM   621  C CG  . LEU A 1 110 ? 25.706  27.861  -3.630  1.00 50.00  ? 205  LEU A CG  1 
ATOM   622  C CD1 . LEU A 1 110 ? 24.845  27.314  -2.477  1.00 47.40  ? 205  LEU A CD1 1 
ATOM   623  C CD2 . LEU A 1 110 ? 24.865  28.674  -4.608  1.00 43.51  ? 205  LEU A CD2 1 
ATOM   624  N N   . ARG A 1 111 ? 27.421  31.860  -2.755  1.00 39.18  ? 206  ARG A N   1 
ATOM   625  C CA  . ARG A 1 111 ? 27.765  33.026  -1.953  1.00 44.02  ? 206  ARG A CA  1 
ATOM   626  C C   . ARG A 1 111 ? 26.558  33.472  -1.139  1.00 44.20  ? 206  ARG A C   1 
ATOM   627  O O   . ARG A 1 111 ? 25.417  33.442  -1.627  1.00 40.48  ? 206  ARG A O   1 
ATOM   628  C CB  . ARG A 1 111 ? 28.247  34.194  -2.838  1.00 44.01  ? 206  ARG A CB  1 
ATOM   629  C CG  . ARG A 1 111 ? 28.734  35.430  -2.076  1.00 42.32  ? 206  ARG A CG  1 
ATOM   630  C CD  . ARG A 1 111 ? 29.054  36.594  -3.012  1.00 42.43  ? 206  ARG A CD  1 
ATOM   631  N NE  . ARG A 1 111 ? 27.852  37.321  -3.400  1.00 43.83  ? 206  ARG A NE  1 
ATOM   632  C CZ  . ARG A 1 111 ? 27.388  37.416  -4.640  1.00 44.93  ? 206  ARG A CZ  1 
ATOM   633  N NH1 . ARG A 1 111 ? 28.026  36.867  -5.666  1.00 41.56  ? 206  ARG A NH1 1 
ATOM   634  N NH2 . ARG A 1 111 ? 26.267  38.098  -4.858  1.00 44.03  ? 206  ARG A NH2 1 
ATOM   635  N N   . HIS A 1 112 ? 26.827  33.932  0.069   1.00 42.03  ? 207  HIS A N   1 
ATOM   636  C CA  . HIS A 1 112 ? 25.867  34.497  0.989   1.00 43.92  ? 207  HIS A CA  1 
ATOM   637  C C   . HIS A 1 112 ? 26.642  35.366  1.955   1.00 45.23  ? 207  HIS A C   1 
ATOM   638  O O   . HIS A 1 112 ? 27.512  34.884  2.630   1.00 46.11  ? 207  HIS A O   1 
ATOM   639  C CB  . HIS A 1 112 ? 25.121  33.413  1.724   1.00 44.49  ? 207  HIS A CB  1 
ATOM   640  C CG  . HIS A 1 112 ? 24.138  33.925  2.713   1.00 47.29  ? 207  HIS A CG  1 
ATOM   641  N ND1 . HIS A 1 112 ? 22.958  34.519  2.349   1.00 48.94  ? 207  HIS A ND1 1 
ATOM   642  C CD2 . HIS A 1 112 ? 24.153  33.917  4.059   1.00 46.60  ? 207  HIS A CD2 1 
ATOM   643  C CE1 . HIS A 1 112 ? 22.297  34.869  3.427   1.00 45.15  ? 207  HIS A CE1 1 
ATOM   644  N NE2 . HIS A 1 112 ? 23.000  34.513  4.477   1.00 46.12  ? 207  HIS A NE2 1 
ATOM   645  N N   . LYS A 1 113 ? 26.345  36.654  1.965   1.00 45.17  ? 208  LYS A N   1 
ATOM   646  C CA  . LYS A 1 113 ? 27.021  37.612  2.822   1.00 44.66  ? 208  LYS A CA  1 
ATOM   647  C C   . LYS A 1 113 ? 28.496  37.537  2.508   1.00 49.71  ? 208  LYS A C   1 
ATOM   648  O O   . LYS A 1 113 ? 28.890  37.845  1.419   1.00 50.33  ? 208  LYS A O   1 
ATOM   649  C CB  . LYS A 1 113 ? 26.671  37.475  4.301   1.00 43.16  ? 208  LYS A CB  1 
ATOM   650  C CG  . LYS A 1 113 ? 25.200  37.628  4.580   1.00 43.23  ? 208  LYS A CG  1 
ATOM   651  C CD  . LYS A 1 113 ? 24.891  37.359  6.025   1.00 44.28  ? 208  LYS A CD  1 
ATOM   652  C CE  . LYS A 1 113 ? 23.526  37.870  6.412   1.00 44.30  ? 208  LYS A CE  1 
ATOM   653  N NZ  . LYS A 1 113 ? 23.235  37.556  7.815   1.00 45.94  ? 208  LYS A NZ  1 
ATOM   654  N N   . LEU A 1 114 ? 29.287  37.115  3.479   1.00 44.07  ? 209  LEU A N   1 
ATOM   655  C CA  . LEU A 1 114 ? 30.732  37.005  3.398   1.00 51.43  ? 209  LEU A CA  1 
ATOM   656  C C   . LEU A 1 114 ? 31.219  35.615  3.235   1.00 49.03  ? 209  LEU A C   1 
ATOM   657  O O   . LEU A 1 114 ? 32.384  35.371  3.302   1.00 52.74  ? 209  LEU A O   1 
ATOM   658  C CB  . LEU A 1 114 ? 31.288  37.319  4.771   1.00 49.45  ? 209  LEU A CB  1 
ATOM   659  C CG  . LEU A 1 114 ? 31.400  38.733  5.148   1.00 49.65  ? 209  LEU A CG  1 
ATOM   660  C CD1 . LEU A 1 114 ? 32.404  38.813  6.256   1.00 55.50  ? 209  LEU A CD1 1 
ATOM   661  C CD2 . LEU A 1 114 ? 31.919  39.348  3.882   1.00 51.67  ? 209  LEU A CD2 1 
ATOM   662  N N   . TYR A 1 115 ? 30.311  34.706  3.059   1.00 48.29  ? 210  TYR A N   1 
ATOM   663  C CA  . TYR A 1 115 ? 30.633  33.291  3.073   1.00 48.83  ? 210  TYR A CA  1 
ATOM   664  C C   . TYR A 1 115 ? 30.433  32.688  1.690   1.00 49.75  ? 210  TYR A C   1 
ATOM   665  O O   . TYR A 1 115 ? 29.476  33.025  0.986   1.00 47.28  ? 210  TYR A O   1 
ATOM   666  C CB  . TYR A 1 115 ? 29.765  32.555  4.085   1.00 49.77  ? 210  TYR A CB  1 
ATOM   667  C CG  . TYR A 1 115 ? 29.681  33.258  5.415   1.00 50.90  ? 210  TYR A CG  1 
ATOM   668  C CD1 . TYR A 1 115 ? 30.672  33.082  6.377   1.00 52.60  ? 210  TYR A CD1 1 
ATOM   669  C CD2 . TYR A 1 115 ? 28.613  34.086  5.714   1.00 49.31  ? 210  TYR A CD2 1 
ATOM   670  C CE1 . TYR A 1 115 ? 30.599  33.716  7.596   1.00 54.71  ? 210  TYR A CE1 1 
ATOM   671  C CE2 . TYR A 1 115 ? 28.532  34.727  6.934   1.00 50.79  ? 210  TYR A CE2 1 
ATOM   672  C CZ  . TYR A 1 115 ? 29.526  34.531  7.873   1.00 52.79  ? 210  TYR A CZ  1 
ATOM   673  O OH  . TYR A 1 115 ? 29.456  35.167  9.083   1.00 55.14  ? 210  TYR A OH  1 
ATOM   674  N N   . SER A 1 116 ? 31.326  31.786  1.307   1.00 48.89  ? 211  SER A N   1 
ATOM   675  C CA  . SER A 1 116 ? 31.188  31.107  0.032   1.00 45.68  ? 211  SER A CA  1 
ATOM   676  C C   . SER A 1 116 ? 31.588  29.651  0.199   1.00 47.78  ? 211  SER A C   1 
ATOM   677  O O   . SER A 1 116 ? 32.370  29.309  1.089   1.00 48.93  ? 211  SER A O   1 
ATOM   678  C CB  . SER A 1 116 ? 32.017  31.799  -1.051  1.00 44.08  ? 211  SER A CB  1 
ATOM   679  O OG  . SER A 1 116 ? 33.402  31.710  -0.757  1.00 51.32  ? 211  SER A OG  1 
ATOM   680  N N   . MET A 1 117 ? 31.036  28.800  -0.670  1.00 44.89  ? 212  MET A N   1 
ATOM   681  C CA  . MET A 1 117 ? 31.238  27.361  -0.586  1.00 47.43  ? 212  MET A CA  1 
ATOM   682  C C   . MET A 1 117 ? 31.216  26.753  -1.984  1.00 45.19  ? 212  MET A C   1 
ATOM   683  O O   . MET A 1 117 ? 30.357  27.087  -2.801  1.00 47.72  ? 212  MET A O   1 
ATOM   684  C CB  . MET A 1 117 ? 30.158  26.714  0.295   1.00 45.68  ? 212  MET A CB  1 
ATOM   685  C CG  . MET A 1 117 ? 30.324  25.214  0.478   1.00 46.91  ? 212  MET A CG  1 
ATOM   686  S SD  . MET A 1 117 ? 29.066  24.435  1.531   1.00 51.17  ? 212  MET A SD  1 
ATOM   687  C CE  . MET A 1 117 ? 27.556  24.625  0.578   1.00 42.91  ? 212  MET A CE  1 
ATOM   688  N N   . GLN A 1 118 ? 32.143  25.846  -2.252  1.00 46.75  ? 213  GLN A N   1 
ATOM   689  C CA  . GLN A 1 118 ? 32.152  25.166  -3.538  1.00 48.17  ? 213  GLN A CA  1 
ATOM   690  C C   . GLN A 1 118 ? 31.178  23.988  -3.531  1.00 47.33  ? 213  GLN A C   1 
ATOM   691  O O   . GLN A 1 118 ? 31.157  23.173  -2.597  1.00 49.46  ? 213  GLN A O   1 
ATOM   692  C CB  . GLN A 1 118 ? 33.560  24.692  -3.905  1.00 48.81  ? 213  GLN A CB  1 
ATOM   693  C CG  . GLN A 1 118 ? 33.622  24.073  -5.316  1.00 49.32  ? 213  GLN A CG  1 
ATOM   694  C CD  . GLN A 1 118 ? 35.030  23.954  -5.887  1.00 55.74  ? 213  GLN A CD  1 
ATOM   695  O OE1 . GLN A 1 118 ? 35.385  24.637  -6.848  1.00 55.74  ? 213  GLN A OE1 1 
ATOM   696  N NE2 . GLN A 1 118 ? 35.825  23.072  -5.308  1.00 50.19  ? 213  GLN A NE2 1 
ATOM   697  N N   . CYS A 1 119 ? 30.373  23.906  -4.587  1.00 46.70  ? 214  CYS A N   1 
ATOM   698  C CA  . CYS A 1 119 ? 29.465  22.803  -4.847  1.00 47.33  ? 214  CYS A CA  1 
ATOM   699  C C   . CYS A 1 119 ? 29.848  22.163  -6.177  1.00 47.36  ? 214  CYS A C   1 
ATOM   700  O O   . CYS A 1 119 ? 30.220  22.852  -7.130  1.00 50.09  ? 214  CYS A O   1 
ATOM   701  C CB  . CYS A 1 119 ? 28.014  23.293  -4.857  1.00 45.23  ? 214  CYS A CB  1 
ATOM   702  S SG  . CYS A 1 119 ? 27.567  24.299  -3.408  1.00 47.44  ? 214  CYS A SG  1 
ATOM   703  N N   . ILE A 1 120 ? 29.781  20.840  -6.237  1.00 47.56  ? 215  ILE A N   1 
ATOM   704  C CA  . ILE A 1 120 ? 30.311  20.077  -7.357  1.00 47.13  ? 215  ILE A CA  1 
ATOM   705  C C   . ILE A 1 120 ? 29.201  19.227  -7.950  1.00 49.68  ? 215  ILE A C   1 
ATOM   706  O O   . ILE A 1 120 ? 28.523  18.486  -7.228  1.00 50.66  ? 215  ILE A O   1 
ATOM   707  C CB  . ILE A 1 120 ? 31.496  19.210  -6.919  1.00 49.00  ? 215  ILE A CB  1 
ATOM   708  C CG1 . ILE A 1 120 ? 32.563  20.120  -6.288  1.00 47.05  ? 215  ILE A CG1 1 
ATOM   709  C CG2 . ILE A 1 120 ? 32.018  18.403  -8.107  1.00 48.81  ? 215  ILE A CG2 1 
ATOM   710  C CD1 . ILE A 1 120 ? 33.780  19.392  -5.818  1.00 56.90  ? 215  ILE A CD1 1 
ATOM   711  N N   . LEU A 1 121 ? 28.995  19.364  -9.254  1.00 49.25  ? 216  LEU A N   1 
ATOM   712  C CA  . LEU A 1 121 ? 28.110  18.500  -10.008 1.00 50.36  ? 216  LEU A CA  1 
ATOM   713  C C   . LEU A 1 121 ? 28.979  17.570  -10.832 1.00 51.32  ? 216  LEU A C   1 
ATOM   714  O O   . LEU A 1 121 ? 29.868  18.020  -11.563 1.00 50.34  ? 216  LEU A O   1 
ATOM   715  C CB  . LEU A 1 121 ? 27.165  19.305  -10.900 1.00 49.95  ? 216  LEU A CB  1 
ATOM   716  C CG  . LEU A 1 121 ? 26.283  18.450  -11.812 1.00 54.41  ? 216  LEU A CG  1 
ATOM   717  C CD1 . LEU A 1 121 ? 25.267  17.659  -10.987 1.00 55.43  ? 216  LEU A CD1 1 
ATOM   718  C CD2 . LEU A 1 121 ? 25.591  19.315  -12.870 1.00 51.25  ? 216  LEU A CD2 1 
ATOM   719  N N   . ASP A 1 122 ? 28.745  16.276  -10.679 1.00 54.61  ? 217  ASP A N   1 
ATOM   720  C CA  . ASP A 1 122 ? 29.530  15.226  -11.318 1.00 56.73  ? 217  ASP A CA  1 
ATOM   721  C C   . ASP A 1 122 ? 28.504  14.265  -11.876 1.00 64.74  ? 217  ASP A C   1 
ATOM   722  O O   . ASP A 1 122 ? 27.838  13.568  -11.109 1.00 69.09  ? 217  ASP A O   1 
ATOM   723  C CB  . ASP A 1 122 ? 30.444  14.545  -10.302 1.00 57.29  ? 217  ASP A CB  1 
ATOM   724  C CG  . ASP A 1 122 ? 31.271  13.424  -10.890 1.00 67.56  ? 217  ASP A CG  1 
ATOM   725  O OD1 . ASP A 1 122 ? 31.035  12.989  -12.040 1.00 67.15  ? 217  ASP A OD1 1 
ATOM   726  O OD2 . ASP A 1 122 ? 32.193  12.982  -10.182 1.00 69.23  ? 217  ASP A OD2 1 
ATOM   727  N N   . ILE A 1 123 ? 28.330  14.244  -13.198 1.00 61.32  ? 218  ILE A N   1 
ATOM   728  C CA  . ILE A 1 123 ? 27.132  13.566  -13.671 1.00 71.20  ? 218  ILE A CA  1 
ATOM   729  C C   . ILE A 1 123 ? 27.314  12.065  -13.792 1.00 75.12  ? 218  ILE A C   1 
ATOM   730  O O   . ILE A 1 123 ? 26.322  11.365  -14.016 1.00 80.52  ? 218  ILE A O   1 
ATOM   731  C CB  . ILE A 1 123 ? 26.591  14.176  -14.977 1.00 70.52  ? 218  ILE A CB  1 
ATOM   732  C CG1 . ILE A 1 123 ? 27.632  14.174  -16.082 1.00 61.99  ? 218  ILE A CG1 1 
ATOM   733  C CG2 . ILE A 1 123 ? 26.022  15.611  -14.698 1.00 63.27  ? 218  ILE A CG2 1 
ATOM   734  C CD1 . ILE A 1 123 ? 26.997  14.322  -17.446 1.00 63.93  ? 218  ILE A CD1 1 
ATOM   735  N N   . LYS A 1 124 ? 28.529  11.541  -13.593 1.00 77.08  ? 219  LYS A N   1 
ATOM   736  C CA  . LYS A 1 124 ? 28.646  10.120  -13.268 1.00 79.19  ? 219  LYS A CA  1 
ATOM   737  C C   . LYS A 1 124 ? 27.803  9.778   -12.042 1.00 82.48  ? 219  LYS A C   1 
ATOM   738  O O   . LYS A 1 124 ? 27.237  8.683   -11.958 1.00 84.98  ? 219  LYS A O   1 
ATOM   739  C CB  . LYS A 1 124 ? 30.111  9.726   -13.037 1.00 77.77  ? 219  LYS A CB  1 
ATOM   740  N N   . HIS A 1 125 ? 27.595  10.739  -11.163 1.00 78.77  ? 220  HIS A N   1 
ATOM   741  C CA  . HIS A 1 125 ? 26.801  10.503  -9.972  1.00 80.41  ? 220  HIS A CA  1 
ATOM   742  C C   . HIS A 1 125 ? 25.364  10.968  -10.110 1.00 82.77  ? 220  HIS A C   1 
ATOM   743  O O   . HIS A 1 125 ? 24.626  10.991  -9.138  1.00 83.26  ? 220  HIS A O   1 
ATOM   744  C CB  . HIS A 1 125 ? 27.411  11.227  -8.797  1.00 80.03  ? 220  HIS A CB  1 
ATOM   745  C CG  . HIS A 1 125 ? 28.679  10.624  -8.305  1.00 86.53  ? 220  HIS A CG  1 
ATOM   746  N ND1 . HIS A 1 125 ? 28.744  9.350   -7.796  1.00 93.84  ? 220  HIS A ND1 1 
ATOM   747  C CD2 . HIS A 1 125 ? 29.923  11.136  -8.197  1.00 84.54  ? 220  HIS A CD2 1 
ATOM   748  C CE1 . HIS A 1 125 ? 29.979  9.095   -7.411  1.00 94.15  ? 220  HIS A CE1 1 
ATOM   749  N NE2 . HIS A 1 125 ? 30.714  10.162  -7.647  1.00 92.60  ? 220  HIS A NE2 1 
ATOM   750  N N   . ASN A 1 126 ? 24.978  11.338  -11.319 1.00 82.87  ? 221  ASN A N   1 
ATOM   751  C CA  . ASN A 1 126 ? 23.636  11.829  -11.563 1.00 83.90  ? 221  ASN A CA  1 
ATOM   752  C C   . ASN A 1 126 ? 22.951  11.212  -12.750 1.00 86.17  ? 221  ASN A C   1 
ATOM   753  O O   . ASN A 1 126 ? 22.328  11.897  -13.553 1.00 80.11  ? 221  ASN A O   1 
ATOM   754  C CB  . ASN A 1 126 ? 23.640  13.349  -11.647 1.00 75.75  ? 221  ASN A CB  1 
ATOM   755  C CG  . ASN A 1 126 ? 23.731  13.977  -10.291 1.00 73.52  ? 221  ASN A CG  1 
ATOM   756  O OD1 . ASN A 1 126 ? 22.729  14.163  -9.629  1.00 72.93  ? 221  ASN A OD1 1 
ATOM   757  N ND2 . ASN A 1 126 ? 24.933  14.239  -9.845  1.00 67.38  ? 221  ASN A ND2 1 
ATOM   758  N N   . ASP A 1 127 ? 23.088  9.893   -12.813 1.00 94.30  ? 222  ASP A N   1 
ATOM   759  C CA  . ASP A 1 127 ? 22.515  9.018   -13.846 1.00 96.43  ? 222  ASP A CA  1 
ATOM   760  C C   . ASP A 1 127 ? 22.924  9.402   -15.247 1.00 95.39  ? 222  ASP A C   1 
ATOM   761  O O   . ASP A 1 127 ? 22.158  9.217   -16.180 1.00 94.32  ? 222  ASP A O   1 
ATOM   762  C CB  . ASP A 1 127 ? 20.994  8.978   -13.761 1.00 98.52  ? 222  ASP A CB  1 
ATOM   763  C CG  . ASP A 1 127 ? 20.509  8.123   -12.643 1.00 107.50 ? 222  ASP A CG  1 
ATOM   764  O OD1 . ASP A 1 127 ? 20.307  8.669   -11.547 1.00 108.84 ? 222  ASP A OD1 1 
ATOM   765  O OD2 . ASP A 1 127 ? 20.336  6.903   -12.853 1.00 110.61 ? 222  ASP A OD2 1 
ATOM   766  N N   . ASN A 1 128 ? 24.145  9.904   -15.374 1.00 85.12  ? 223  ASN A N   1 
ATOM   767  C CA  . ASN A 1 128 ? 24.666  10.388  -16.621 1.00 81.28  ? 223  ASN A CA  1 
ATOM   768  C C   . ASN A 1 128 ? 23.706  11.260  -17.382 1.00 79.78  ? 223  ASN A C   1 
ATOM   769  O O   . ASN A 1 128 ? 23.572  11.125  -18.594 1.00 68.85  ? 223  ASN A O   1 
ATOM   770  C CB  . ASN A 1 128 ? 25.111  9.239   -17.465 1.00 80.68  ? 223  ASN A CB  1 
ATOM   771  C CG  . ASN A 1 128 ? 26.485  8.801   -17.110 1.00 87.12  ? 223  ASN A CG  1 
ATOM   772  O OD1 . ASN A 1 128 ? 26.814  8.622   -15.940 1.00 84.55  ? 223  ASN A OD1 1 
ATOM   773  N ND2 . ASN A 1 128 ? 27.319  8.653   -18.120 1.00 91.54  ? 223  ASN A ND2 1 
ATOM   774  N N   . ASP A 1 129 ? 23.028  12.147  -16.662 1.00 72.50  ? 224  ASP A N   1 
ATOM   775  C CA  . ASP A 1 129 ? 22.077  13.049  -17.308 1.00 65.82  ? 224  ASP A CA  1 
ATOM   776  C C   . ASP A 1 129 ? 22.833  14.236  -17.890 1.00 58.26  ? 224  ASP A C   1 
ATOM   777  O O   . ASP A 1 129 ? 23.157  15.198  -17.183 1.00 58.31  ? 224  ASP A O   1 
ATOM   778  C CB  . ASP A 1 129 ? 21.009  13.531  -16.336 1.00 69.75  ? 224  ASP A CB  1 
ATOM   779  C CG  . ASP A 1 129 ? 19.864  14.264  -17.048 1.00 63.28  ? 224  ASP A CG  1 
ATOM   780  O OD1 . ASP A 1 129 ? 18.777  14.418  -16.458 1.00 64.32  ? 224  ASP A OD1 1 
ATOM   781  O OD2 . ASP A 1 129 ? 20.031  14.655  -18.218 1.00 65.73  ? 224  ASP A OD2 1 
ATOM   782  N N   . LYS A 1 130 ? 23.062  14.180  -19.202 1.00 59.79  ? 225  LYS A N   1 
ATOM   783  C CA  . LYS A 1 130 ? 23.693  15.273  -19.928 1.00 56.61  ? 225  LYS A CA  1 
ATOM   784  C C   . LYS A 1 130 ? 22.822  16.522  -19.940 1.00 56.91  ? 225  LYS A C   1 
ATOM   785  O O   . LYS A 1 130 ? 23.348  17.644  -19.935 1.00 53.20  ? 225  LYS A O   1 
ATOM   786  C CB  . LYS A 1 130 ? 24.005  14.818  -21.357 1.00 57.70  ? 225  LYS A CB  1 
ATOM   787  C CG  . LYS A 1 130 ? 24.903  13.585  -21.435 1.00 57.03  ? 225  LYS A CG  1 
ATOM   788  C CD  . LYS A 1 130 ? 24.993  13.069  -22.859 1.00 63.53  ? 225  LYS A CD  1 
ATOM   789  C CE  . LYS A 1 130 ? 26.429  12.671  -23.216 1.00 73.66  ? 225  LYS A CE  1 
ATOM   790  N NZ  . LYS A 1 130 ? 26.979  11.691  -22.231 1.00 72.06  ? 225  LYS A NZ  1 
ATOM   791  N N   . ASN A 1 131 ? 21.493  16.356  -19.952 1.00 57.81  ? 226  ASN A N   1 
ATOM   792  C CA  . ASN A 1 131 ? 20.605  17.518  -19.939 1.00 55.37  ? 226  ASN A CA  1 
ATOM   793  C C   . ASN A 1 131 ? 20.757  18.305  -18.656 1.00 50.90  ? 226  ASN A C   1 
ATOM   794  O O   . ASN A 1 131 ? 20.707  19.538  -18.664 1.00 49.88  ? 226  ASN A O   1 
ATOM   795  C CB  . ASN A 1 131 ? 19.149  17.088  -20.104 1.00 55.61  ? 226  ASN A CB  1 
ATOM   796  C CG  . ASN A 1 131 ? 18.866  16.566  -21.479 1.00 58.39  ? 226  ASN A CG  1 
ATOM   797  O OD1 . ASN A 1 131 ? 19.535  16.947  -22.437 1.00 60.57  ? 226  ASN A OD1 1 
ATOM   798  N ND2 . ASN A 1 131 ? 17.875  15.689  -21.592 1.00 59.81  ? 226  ASN A ND2 1 
ATOM   799  N N   . MET A 1 132 ? 20.928  17.605  -17.537 1.00 50.50  ? 227  MET A N   1 
ATOM   800  C CA  . MET A 1 132 ? 21.135  18.286  -16.272 1.00 51.86  ? 227  MET A CA  1 
ATOM   801  C C   . MET A 1 132 ? 22.391  19.152  -16.324 1.00 48.42  ? 227  MET A C   1 
ATOM   802  O O   . MET A 1 132 ? 22.364  20.328  -15.937 1.00 47.48  ? 227  MET A O   1 
ATOM   803  C CB  . MET A 1 132 ? 21.222  17.264  -15.142 1.00 48.40  ? 227  MET A CB  1 
ATOM   804  C CG  . MET A 1 132 ? 21.353  17.918  -13.786 1.00 52.10  ? 227  MET A CG  1 
ATOM   805  S SD  . MET A 1 132 ? 21.410  16.736  -12.432 1.00 54.69  ? 227  MET A SD  1 
ATOM   806  C CE  . MET A 1 132 ? 21.516  17.875  -11.060 1.00 49.84  ? 227  MET A CE  1 
ATOM   807  N N   . MET A 1 133 ? 23.502  18.582  -16.810 1.00 49.29  ? 228  MET A N   1 
ATOM   808  C CA  . MET A 1 133 ? 24.739  19.348  -16.944 1.00 49.29  ? 228  MET A CA  1 
ATOM   809  C C   . MET A 1 133 ? 24.541  20.556  -17.855 1.00 46.87  ? 228  MET A C   1 
ATOM   810  O O   . MET A 1 133 ? 24.928  21.676  -17.511 1.00 45.49  ? 228  MET A O   1 
ATOM   811  C CB  . MET A 1 133 ? 25.874  18.453  -17.466 1.00 46.31  ? 228  MET A CB  1 
ATOM   812  C CG  . MET A 1 133 ? 27.235  19.179  -17.534 1.00 51.97  ? 228  MET A CG  1 
ATOM   813  S SD  . MET A 1 133 ? 27.807  19.893  -15.945 1.00 56.02  ? 228  MET A SD  1 
ATOM   814  C CE  . MET A 1 133 ? 28.485  18.384  -15.167 1.00 54.19  ? 228  MET A CE  1 
ATOM   815  N N   . LYS A 1 134 ? 23.897  20.358  -18.979 1.00 47.02  ? 229  LYS A N   1 
ATOM   816  C CA  . LYS A 1 134 ? 23.677  21.431  -19.909 1.00 48.60  ? 229  LYS A CA  1 
ATOM   817  C C   . LYS A 1 134 ? 22.895  22.556  -19.277 1.00 47.65  ? 229  LYS A C   1 
ATOM   818  O O   . LYS A 1 134 ? 23.190  23.702  -19.467 1.00 48.16  ? 229  LYS A O   1 
ATOM   819  C CB  . LYS A 1 134 ? 22.947  20.924  -21.134 1.00 54.51  ? 229  LYS A CB  1 
ATOM   820  C CG  . LYS A 1 134 ? 22.734  21.999  -22.151 1.00 57.01  ? 229  LYS A CG  1 
ATOM   821  C CD  . LYS A 1 134 ? 21.740  21.625  -23.223 1.00 62.96  ? 229  LYS A CD  1 
ATOM   822  C CE  . LYS A 1 134 ? 22.317  20.614  -24.178 1.00 68.80  ? 229  LYS A CE  1 
ATOM   823  N NZ  . LYS A 1 134 ? 22.574  19.356  -23.452 1.00 71.66  ? 229  LYS A NZ  1 
ATOM   824  N N   . TRP A 1 135 ? 21.889  22.199  -18.510 1.00 48.10  ? 230  TRP A N   1 
ATOM   825  C CA  . TRP A 1 135 ? 21.065  23.203  -17.849 1.00 45.67  ? 230  TRP A CA  1 
ATOM   826  C C   . TRP A 1 135 ? 21.859  23.951  -16.791 1.00 46.58  ? 230  TRP A C   1 
ATOM   827  O O   . TRP A 1 135 ? 21.733  25.176  -16.659 1.00 43.86  ? 230  TRP A O   1 
ATOM   828  C CB  . TRP A 1 135 ? 19.833  22.535  -17.225 1.00 45.73  ? 230  TRP A CB  1 
ATOM   829  C CG  . TRP A 1 135 ? 18.889  23.479  -16.505 1.00 48.37  ? 230  TRP A CG  1 
ATOM   830  C CD1 . TRP A 1 135 ? 17.811  24.129  -17.042 1.00 49.36  ? 230  TRP A CD1 1 
ATOM   831  C CD2 . TRP A 1 135 ? 18.936  23.863  -15.118 1.00 42.90  ? 230  TRP A CD2 1 
ATOM   832  N NE1 . TRP A 1 135 ? 17.190  24.900  -16.076 1.00 46.26  ? 230  TRP A NE1 1 
ATOM   833  C CE2 . TRP A 1 135 ? 17.854  24.748  -14.889 1.00 46.39  ? 230  TRP A CE2 1 
ATOM   834  C CE3 . TRP A 1 135 ? 19.774  23.534  -14.051 1.00 43.74  ? 230  TRP A CE3 1 
ATOM   835  C CZ2 . TRP A 1 135 ? 17.601  25.322  -13.636 1.00 45.09  ? 230  TRP A CZ2 1 
ATOM   836  C CZ3 . TRP A 1 135 ? 19.515  24.093  -12.803 1.00 45.89  ? 230  TRP A CZ3 1 
ATOM   837  C CH2 . TRP A 1 135 ? 18.433  24.980  -12.607 1.00 43.76  ? 230  TRP A CH2 1 
ATOM   838  N N   . VAL A 1 136 ? 22.669  23.229  -16.012 1.00 45.76  ? 231  VAL A N   1 
ATOM   839  C CA  . VAL A 1 136 ? 23.454  23.883  -14.959 1.00 44.49  ? 231  VAL A CA  1 
ATOM   840  C C   . VAL A 1 136 ? 24.463  24.848  -15.572 1.00 45.83  ? 231  VAL A C   1 
ATOM   841  O O   . VAL A 1 136 ? 24.595  25.993  -15.127 1.00 45.86  ? 231  VAL A O   1 
ATOM   842  C CB  . VAL A 1 136 ? 24.154  22.834  -14.075 1.00 47.99  ? 231  VAL A CB  1 
ATOM   843  C CG1 . VAL A 1 136 ? 25.212  23.496  -13.170 1.00 43.52  ? 231  VAL A CG1 1 
ATOM   844  C CG2 . VAL A 1 136 ? 23.120  22.073  -13.236 1.00 43.65  ? 231  VAL A CG2 1 
ATOM   845  N N   . SER A 1 137 ? 25.187  24.395  -16.608 1.00 44.21  ? 232  SER A N   1 
ATOM   846  C CA  . SER A 1 137 ? 26.232  25.215  -17.214 1.00 48.40  ? 232  SER A CA  1 
ATOM   847  C C   . SER A 1 137 ? 25.692  26.524  -17.757 1.00 48.78  ? 232  SER A C   1 
ATOM   848  O O   . SER A 1 137 ? 26.414  27.522  -17.772 1.00 46.57  ? 232  SER A O   1 
ATOM   849  C CB  . SER A 1 137 ? 26.925  24.470  -18.350 1.00 45.58  ? 232  SER A CB  1 
ATOM   850  O OG  . SER A 1 137 ? 27.709  23.403  -17.868 1.00 51.21  ? 232  SER A OG  1 
ATOM   851  N N   . ASN A 1 138 ? 24.434  26.537  -18.206 1.00 47.98  ? 233  ASN A N   1 
ATOM   852  C CA  . ASN A 1 138 ? 23.799  27.708  -18.802 1.00 47.03  ? 233  ASN A CA  1 
ATOM   853  C C   . ASN A 1 138 ? 23.262  28.688  -17.758 1.00 46.26  ? 233  ASN A C   1 
ATOM   854  O O   . ASN A 1 138 ? 22.801  29.772  -18.127 1.00 47.13  ? 233  ASN A O   1 
ATOM   855  C CB  . ASN A 1 138 ? 22.679  27.232  -19.747 1.00 51.01  ? 233  ASN A CB  1 
ATOM   856  C CG  . ASN A 1 138 ? 21.883  28.374  -20.375 1.00 52.79  ? 233  ASN A CG  1 
ATOM   857  O OD1 . ASN A 1 138 ? 20.729  28.601  -20.017 1.00 58.93  ? 233  ASN A OD1 1 
ATOM   858  N ND2 . ASN A 1 138 ? 22.487  29.077  -21.315 1.00 48.82  ? 233  ASN A ND2 1 
ATOM   859  N N   . LEU A 1 139 ? 23.338  28.368  -16.480 1.00 43.58  ? 234  LEU A N   1 
ATOM   860  C CA  . LEU A 1 139 ? 22.772  29.258  -15.472 1.00 48.38  ? 234  LEU A CA  1 
ATOM   861  C C   . LEU A 1 139 ? 23.595  30.538  -15.391 1.00 47.64  ? 234  LEU A C   1 
ATOM   862  O O   . LEU A 1 139 ? 24.826  30.465  -15.290 1.00 48.09  ? 234  LEU A O   1 
ATOM   863  C CB  . LEU A 1 139 ? 22.748  28.571  -14.110 1.00 45.19  ? 234  LEU A CB  1 
ATOM   864  C CG  . LEU A 1 139 ? 21.650  27.525  -13.872 1.00 48.35  ? 234  LEU A CG  1 
ATOM   865  C CD1 . LEU A 1 139 ? 21.863  26.843  -12.528 1.00 45.23  ? 234  LEU A CD1 1 
ATOM   866  C CD2 . LEU A 1 139 ? 20.253  28.164  -13.960 1.00 40.96  ? 234  LEU A CD2 1 
ATOM   867  N N   . PRO A 1 140 ? 22.966  31.712  -15.415 1.00 49.58  ? 235  PRO A N   1 
ATOM   868  C CA  . PRO A 1 140 ? 23.733  32.962  -15.331 1.00 47.44  ? 235  PRO A CA  1 
ATOM   869  C C   . PRO A 1 140 ? 24.213  33.237  -13.920 1.00 44.24  ? 235  PRO A C   1 
ATOM   870  O O   . PRO A 1 140 ? 23.558  32.882  -12.931 1.00 42.78  ? 235  PRO A O   1 
ATOM   871  C CB  . PRO A 1 140 ? 22.739  34.036  -15.795 1.00 48.02  ? 235  PRO A CB  1 
ATOM   872  C CG  . PRO A 1 140 ? 21.390  33.428  -15.677 1.00 47.15  ? 235  PRO A CG  1 
ATOM   873  C CD  . PRO A 1 140 ? 21.516  31.934  -15.560 1.00 47.63  ? 235  PRO A CD  1 
ATOM   874  N N   . LEU A 1 141 ? 25.378  33.887  -13.834 1.00 42.23  ? 236  LEU A N   1 
ATOM   875  C CA  . LEU A 1 141 ? 25.896  34.293  -12.531 1.00 43.76  ? 236  LEU A CA  1 
ATOM   876  C C   . LEU A 1 141 ? 24.892  35.183  -11.811 1.00 42.66  ? 236  LEU A C   1 
ATOM   877  O O   . LEU A 1 141 ? 24.091  35.889  -12.435 1.00 40.50  ? 236  LEU A O   1 
ATOM   878  C CB  . LEU A 1 141 ? 27.241  35.020  -12.664 1.00 42.19  ? 236  LEU A CB  1 
ATOM   879  C CG  . LEU A 1 141 ? 28.390  34.264  -13.346 1.00 48.32  ? 236  LEU A CG  1 
ATOM   880  C CD1 . LEU A 1 141 ? 29.698  35.081  -13.354 1.00 44.94  ? 236  LEU A CD1 1 
ATOM   881  C CD2 . LEU A 1 141 ? 28.605  32.906  -12.704 1.00 46.05  ? 236  LEU A CD2 1 
ATOM   882  N N   . GLU A 1 142 ? 24.935  35.115  -10.478 1.00 39.03  ? 237  GLU A N   1 
ATOM   883  C CA  . GLU A 1 142 ? 24.083  35.781  -9.498  1.00 41.27  ? 237  GLU A CA  1 
ATOM   884  C C   . GLU A 1 142 ? 22.699  35.135  -9.362  1.00 42.63  ? 237  GLU A C   1 
ATOM   885  O O   . GLU A 1 142 ? 21.928  35.577  -8.510  1.00 41.44  ? 237  GLU A O   1 
ATOM   886  C CB  . GLU A 1 142 ? 23.918  37.288  -9.769  1.00 42.98  ? 237  GLU A CB  1 
ATOM   887  C CG  . GLU A 1 142 ? 25.216  38.084  -9.605  1.00 45.28  ? 237  GLU A CG  1 
ATOM   888  C CD  . GLU A 1 142 ? 25.825  37.930  -8.222  1.00 46.66  ? 237  GLU A CD  1 
ATOM   889  O OE1 . GLU A 1 142 ? 26.864  37.233  -8.112  1.00 46.70  ? 237  GLU A OE1 1 
ATOM   890  O OE2 . GLU A 1 142 ? 25.257  38.490  -7.243  1.00 44.92  ? 237  GLU A OE2 1 
ATOM   891  N N   . SER A 1 143 ? 22.363  34.105  -10.138 1.00 40.41  ? 238  SER A N   1 
ATOM   892  C CA  . SER A 1 143 ? 21.085  33.432  -9.940  1.00 41.80  ? 238  SER A CA  1 
ATOM   893  C C   . SER A 1 143 ? 21.022  32.804  -8.549  1.00 41.16  ? 238  SER A C   1 
ATOM   894  O O   . SER A 1 143 ? 22.038  32.419  -7.968  1.00 39.42  ? 238  SER A O   1 
ATOM   895  C CB  . SER A 1 143 ? 20.861  32.357  -11.009 1.00 42.14  ? 238  SER A CB  1 
ATOM   896  O OG  . SER A 1 143 ? 20.771  32.930  -12.308 1.00 42.92  ? 238  SER A OG  1 
ATOM   897  N N   . ILE A 1 144 ? 19.813  32.715  -8.010  1.00 40.49  ? 239  ILE A N   1 
ATOM   898  C CA  . ILE A 1 144 ? 19.589  32.122  -6.699  1.00 40.93  ? 239  ILE A CA  1 
ATOM   899  C C   . ILE A 1 144 ? 19.103  30.692  -6.873  1.00 41.68  ? 239  ILE A C   1 
ATOM   900  O O   . ILE A 1 144 ? 18.128  30.427  -7.595  1.00 40.38  ? 239  ILE A O   1 
ATOM   901  C CB  . ILE A 1 144 ? 18.594  32.947  -5.872  1.00 41.40  ? 239  ILE A CB  1 
ATOM   902  C CG1 . ILE A 1 144 ? 19.100  34.393  -5.751  1.00 40.70  ? 239  ILE A CG1 1 
ATOM   903  C CG2 . ILE A 1 144 ? 18.408  32.284  -4.494  1.00 39.19  ? 239  ILE A CG2 1 
ATOM   904  C CD1 . ILE A 1 144 ? 18.091  35.356  -5.115  1.00 41.68  ? 239  ILE A CD1 1 
ATOM   905  N N   . VAL A 1 145 ? 19.789  29.764  -6.213  1.00 42.55  ? 240  VAL A N   1 
ATOM   906  C CA  . VAL A 1 145 ? 19.455  28.360  -6.352  1.00 40.46  ? 240  VAL A CA  1 
ATOM   907  C C   . VAL A 1 145 ? 19.301  27.731  -4.980  1.00 42.78  ? 240  VAL A C   1 
ATOM   908  O O   . VAL A 1 145 ? 19.917  28.161  -3.995  1.00 40.41  ? 240  VAL A O   1 
ATOM   909  C CB  . VAL A 1 145 ? 20.500  27.583  -7.184  1.00 41.51  ? 240  VAL A CB  1 
ATOM   910  C CG1 . VAL A 1 145 ? 20.542  28.120  -8.631  1.00 41.42  ? 240  VAL A CG1 1 
ATOM   911  C CG2 . VAL A 1 145 ? 21.879  27.620  -6.519  1.00 39.07  ? 240  VAL A CG2 1 
ATOM   912  N N   . ASP A 1 146 ? 18.440  26.710  -4.939  1.00 40.35  ? 241  ASP A N   1 
ATOM   913  C CA  . ASP A 1 146 ? 18.343  25.749  -3.853  1.00 40.52  ? 241  ASP A CA  1 
ATOM   914  C C   . ASP A 1 146 ? 19.005  24.452  -4.301  1.00 43.20  ? 241  ASP A C   1 
ATOM   915  O O   . ASP A 1 146 ? 18.628  23.872  -5.327  1.00 42.16  ? 241  ASP A O   1 
ATOM   916  C CB  . ASP A 1 146 ? 16.881  25.511  -3.466  1.00 43.70  ? 241  ASP A CB  1 
ATOM   917  C CG  . ASP A 1 146 ? 16.279  26.687  -2.691  1.00 46.79  ? 241  ASP A CG  1 
ATOM   918  O OD1 . ASP A 1 146 ? 16.994  27.704  -2.500  1.00 44.47  ? 241  ASP A OD1 1 
ATOM   919  O OD2 . ASP A 1 146 ? 15.095  26.596  -2.272  1.00 44.70  ? 241  ASP A OD2 1 
ATOM   920  N N   . ILE A 1 147 ? 20.002  24.018  -3.542  1.00 43.19  ? 242  ILE A N   1 
ATOM   921  C CA  . ILE A 1 147 ? 20.792  22.836  -3.833  1.00 43.43  ? 242  ILE A CA  1 
ATOM   922  C C   . ILE A 1 147 ? 20.519  21.796  -2.760  1.00 44.88  ? 242  ILE A C   1 
ATOM   923  O O   . ILE A 1 147 ? 20.575  22.099  -1.562  1.00 44.89  ? 242  ILE A O   1 
ATOM   924  C CB  . ILE A 1 147 ? 22.296  23.166  -3.885  1.00 46.53  ? 242  ILE A CB  1 
ATOM   925  C CG1 . ILE A 1 147 ? 22.641  23.905  -5.189  1.00 42.97  ? 242  ILE A CG1 1 
ATOM   926  C CG2 . ILE A 1 147 ? 23.130  21.886  -3.703  1.00 42.93  ? 242  ILE A CG2 1 
ATOM   927  C CD1 . ILE A 1 147 ? 24.057  24.434  -5.231  1.00 43.63  ? 242  ILE A CD1 1 
ATOM   928  N N   . LYS A 1 148 ? 20.241  20.572  -3.186  1.00 44.34  ? 243  LYS A N   1 
ATOM   929  C CA  . LYS A 1 148 ? 20.240  19.426  -2.292  1.00 45.96  ? 243  LYS A CA  1 
ATOM   930  C C   . LYS A 1 148 ? 21.532  18.658  -2.530  1.00 50.48  ? 243  LYS A C   1 
ATOM   931  O O   . LYS A 1 148 ? 21.805  18.219  -3.660  1.00 49.03  ? 243  LYS A O   1 
ATOM   932  C CB  . LYS A 1 148 ? 19.024  18.533  -2.527  1.00 50.61  ? 243  LYS A CB  1 
ATOM   933  C CG  . LYS A 1 148 ? 19.015  17.297  -1.646  1.00 53.16  ? 243  LYS A CG  1 
ATOM   934  C CD  . LYS A 1 148 ? 17.702  16.545  -1.772  1.00 57.07  ? 243  LYS A CD  1 
ATOM   935  C CE  . LYS A 1 148 ? 17.711  15.321  -0.870  1.00 60.68  ? 243  LYS A CE  1 
ATOM   936  N NZ  . LYS A 1 148 ? 16.356  14.723  -0.751  1.00 63.51  ? 243  LYS A NZ  1 
ATOM   937  N N   . GLY A 1 149 ? 22.327  18.503  -1.478  1.00 49.49  ? 244  GLY A N   1 
ATOM   938  C CA  . GLY A 1 149 ? 23.570  17.781  -1.661  1.00 53.88  ? 244  GLY A CA  1 
ATOM   939  C C   . GLY A 1 149 ? 24.176  17.343  -0.349  1.00 53.71  ? 244  GLY A C   1 
ATOM   940  O O   . GLY A 1 149 ? 23.673  17.645  0.732   1.00 52.78  ? 244  GLY A O   1 
ATOM   941  N N   . LYS A 1 150 ? 25.294  16.643  -0.463  1.00 53.79  ? 245  LYS A N   1 
ATOM   942  C CA  . LYS A 1 150 ? 25.981  16.102  0.700   1.00 54.61  ? 245  LYS A CA  1 
ATOM   943  C C   . LYS A 1 150 ? 27.273  16.873  0.929   1.00 53.94  ? 245  LYS A C   1 
ATOM   944  O O   . LYS A 1 150 ? 28.016  17.139  -0.013  1.00 55.65  ? 245  LYS A O   1 
ATOM   945  C CB  . LYS A 1 150 ? 26.262  14.606  0.508   1.00 58.57  ? 245  LYS A CB  1 
ATOM   946  C CG  . LYS A 1 150 ? 26.928  13.930  1.698   1.00 62.23  ? 245  LYS A CG  1 
ATOM   947  C CD  . LYS A 1 150 ? 26.194  12.656  2.111   1.00 70.39  ? 245  LYS A CD  1 
ATOM   948  C CE  . LYS A 1 150 ? 26.990  11.893  3.168   1.00 72.82  ? 245  LYS A CE  1 
ATOM   949  N NZ  . LYS A 1 150 ? 27.489  12.832  4.228   1.00 74.25  ? 245  LYS A NZ  1 
ATOM   950  N N   . LEU A 1 151 ? 27.548  17.240  2.173   1.00 55.78  ? 246  LEU A N   1 
ATOM   951  C CA  . LEU A 1 151 ? 28.784  17.953  2.469   1.00 54.80  ? 246  LEU A CA  1 
ATOM   952  C C   . LEU A 1 151 ? 29.905  16.978  2.801   1.00 58.18  ? 246  LEU A C   1 
ATOM   953  O O   . LEU A 1 151 ? 29.673  15.895  3.345   1.00 60.51  ? 246  LEU A O   1 
ATOM   954  C CB  . LEU A 1 151 ? 28.603  18.930  3.628   1.00 53.23  ? 246  LEU A CB  1 
ATOM   955  C CG  . LEU A 1 151 ? 27.472  19.950  3.493   1.00 56.60  ? 246  LEU A CG  1 
ATOM   956  C CD1 . LEU A 1 151 ? 27.556  20.964  4.617   1.00 57.88  ? 246  LEU A CD1 1 
ATOM   957  C CD2 . LEU A 1 151 ? 27.480  20.652  2.149   1.00 53.40  ? 246  LEU A CD2 1 
ATOM   958  N N   . SER A 1 152 ? 31.126  17.367  2.440   1.00 56.11  ? 247  SER A N   1 
ATOM   959  C CA  . SER A 1 152 ? 32.309  16.619  2.837   1.00 59.25  ? 247  SER A CA  1 
ATOM   960  C C   . SER A 1 152 ? 33.506  17.549  2.753   1.00 60.41  ? 247  SER A C   1 
ATOM   961  O O   . SER A 1 152 ? 33.444  18.608  2.133   1.00 60.79  ? 247  SER A O   1 
ATOM   962  C CB  . SER A 1 152 ? 32.526  15.382  1.968   1.00 58.31  ? 247  SER A CB  1 
ATOM   963  O OG  . SER A 1 152 ? 33.099  15.746  0.731   1.00 63.93  ? 247  SER A OG  1 
ATOM   964  N N   . LYS A 1 153 ? 34.601  17.137  3.381   1.00 63.02  ? 248  LYS A N   1 
ATOM   965  C CA  . LYS A 1 153 ? 35.790  17.971  3.465   1.00 65.39  ? 248  LYS A CA  1 
ATOM   966  C C   . LYS A 1 153 ? 36.831  17.456  2.491   1.00 67.45  ? 248  LYS A C   1 
ATOM   967  O O   . LYS A 1 153 ? 37.296  16.322  2.655   1.00 68.09  ? 248  LYS A O   1 
ATOM   968  C CB  . LYS A 1 153 ? 36.343  17.961  4.883   1.00 69.85  ? 248  LYS A CB  1 
ATOM   969  C CG  . LYS A 1 153 ? 37.430  18.980  5.145   1.00 73.44  ? 248  LYS A CG  1 
ATOM   970  C CD  . LYS A 1 153 ? 37.511  19.295  6.637   1.00 78.77  ? 248  LYS A CD  1 
ATOM   971  C CE  . LYS A 1 153 ? 38.311  20.566  6.904   1.00 82.66  ? 248  LYS A CE  1 
ATOM   972  N NZ  . LYS A 1 153 ? 38.023  21.120  8.263   1.00 84.60  ? 248  LYS A NZ  1 
ATOM   973  N N   . PRO A 1 154 ? 37.228  18.226  1.481   1.00 71.62  ? 249  PRO A N   1 
ATOM   974  C CA  . PRO A 1 154 ? 38.202  17.723  0.508   1.00 72.14  ? 249  PRO A CA  1 
ATOM   975  C C   . PRO A 1 154 ? 39.604  17.712  1.091   1.00 79.14  ? 249  PRO A C   1 
ATOM   976  O O   . PRO A 1 154 ? 39.897  18.374  2.090   1.00 80.58  ? 249  PRO A O   1 
ATOM   977  C CB  . PRO A 1 154 ? 38.099  18.729  -0.639  1.00 70.86  ? 249  PRO A CB  1 
ATOM   978  C CG  . PRO A 1 154 ? 37.747  20.024  0.067   1.00 70.55  ? 249  PRO A CG  1 
ATOM   979  C CD  . PRO A 1 154 ? 36.851  19.630  1.221   1.00 67.55  ? 249  PRO A CD  1 
ATOM   980  N N   . GLU A 1 155 ? 40.483  16.948  0.436   1.00 80.55  ? 250  GLU A N   1 
ATOM   981  C CA  . GLU A 1 155 ? 41.903  16.970  0.772   1.00 83.85  ? 250  GLU A CA  1 
ATOM   982  C C   . GLU A 1 155 ? 42.434  18.399  0.707   1.00 87.44  ? 250  GLU A C   1 
ATOM   983  O O   . GLU A 1 155 ? 42.730  19.007  1.743   1.00 87.75  ? 250  GLU A O   1 
ATOM   984  C CB  . GLU A 1 155 ? 42.696  16.057  -0.161  1.00 81.74  ? 250  GLU A CB  1 
ATOM   985  N N   . VAL A 1 156 ? 42.535  18.956  -0.499  1.00 85.95  ? 251  VAL A N   1 
ATOM   986  C CA  . VAL A 1 156 ? 42.955  20.338  -0.696  1.00 86.03  ? 251  VAL A CA  1 
ATOM   987  C C   . VAL A 1 156 ? 41.697  21.186  -0.870  1.00 85.24  ? 251  VAL A C   1 
ATOM   988  O O   . VAL A 1 156 ? 41.014  21.059  -1.904  1.00 81.81  ? 251  VAL A O   1 
ATOM   989  C CB  . VAL A 1 156 ? 43.896  20.474  -1.902  1.00 83.04  ? 251  VAL A CB  1 
ATOM   990  N N   . PRO A 1 157 ? 41.340  22.037  0.090   1.00 83.81  ? 252  PRO A N   1 
ATOM   991  C CA  . PRO A 1 157 ? 40.150  22.878  -0.057  1.00 81.43  ? 252  PRO A CA  1 
ATOM   992  C C   . PRO A 1 157 ? 40.441  24.165  -0.813  1.00 82.82  ? 252  PRO A C   1 
ATOM   993  O O   . PRO A 1 157 ? 41.562  24.672  -0.830  1.00 83.68  ? 252  PRO A O   1 
ATOM   994  C CB  . PRO A 1 157 ? 39.744  23.169  1.397   1.00 79.53  ? 252  PRO A CB  1 
ATOM   995  C CG  . PRO A 1 157 ? 40.974  22.867  2.238   1.00 83.14  ? 252  PRO A CG  1 
ATOM   996  C CD  . PRO A 1 157 ? 42.056  22.309  1.345   1.00 86.76  ? 252  PRO A CD  1 
ATOM   997  N N   . ILE A 1 158 ? 39.395  24.682  -1.464  1.00 78.71  ? 253  ILE A N   1 
ATOM   998  C CA  . ILE A 1 158 ? 39.539  25.868  -2.304  1.00 74.54  ? 253  ILE A CA  1 
ATOM   999  C C   . ILE A 1 158 ? 39.953  27.056  -1.449  1.00 70.15  ? 253  ILE A C   1 
ATOM   1000 O O   . ILE A 1 158 ? 39.305  27.374  -0.444  1.00 71.58  ? 253  ILE A O   1 
ATOM   1001 C CB  . ILE A 1 158 ? 38.224  26.144  -3.053  1.00 71.49  ? 253  ILE A CB  1 
ATOM   1002 C CG1 . ILE A 1 158 ? 37.935  25.010  -4.029  1.00 74.84  ? 253  ILE A CG1 1 
ATOM   1003 C CG2 . ILE A 1 158 ? 38.292  27.460  -3.819  1.00 70.20  ? 253  ILE A CG2 1 
ATOM   1004 C CD1 . ILE A 1 158 ? 38.957  24.913  -5.153  1.00 68.86  ? 253  ILE A CD1 1 
ATOM   1005 N N   . ASP A 1 159 ? 41.031  27.729  -1.851  1.00 70.26  ? 254  ASP A N   1 
ATOM   1006 C CA  . ASP A 1 159 ? 41.515  28.864  -1.068  1.00 72.28  ? 254  ASP A CA  1 
ATOM   1007 C C   . ASP A 1 159 ? 40.470  29.970  -0.985  1.00 71.21  ? 254  ASP A C   1 
ATOM   1008 O O   . ASP A 1 159 ? 40.325  30.617  0.060   1.00 70.52  ? 254  ASP A O   1 
ATOM   1009 C CB  . ASP A 1 159 ? 42.812  29.420  -1.663  1.00 75.24  ? 254  ASP A CB  1 
ATOM   1010 C CG  . ASP A 1 159 ? 43.916  28.378  -1.757  1.00 81.83  ? 254  ASP A CG  1 
ATOM   1011 O OD1 . ASP A 1 159 ? 43.837  27.342  -1.053  1.00 82.99  ? 254  ASP A OD1 1 
ATOM   1012 O OD2 . ASP A 1 159 ? 44.871  28.604  -2.538  1.00 83.55  ? 254  ASP A OD2 1 
ATOM   1013 N N   . SER A 1 160 ? 39.720  30.191  -2.071  1.00 68.25  ? 255  SER A N   1 
ATOM   1014 C CA  . SER A 1 160 ? 38.814  31.335  -2.134  1.00 68.56  ? 255  SER A CA  1 
ATOM   1015 C C   . SER A 1 160 ? 37.578  31.186  -1.252  1.00 63.90  ? 255  SER A C   1 
ATOM   1016 O O   . SER A 1 160 ? 36.956  32.203  -0.930  1.00 63.75  ? 255  SER A O   1 
ATOM   1017 C CB  . SER A 1 160 ? 38.363  31.583  -3.573  1.00 68.52  ? 255  SER A CB  1 
ATOM   1018 O OG  . SER A 1 160 ? 37.370  30.645  -3.946  1.00 69.10  ? 255  SER A OG  1 
ATOM   1019 N N   . THR A 1 161 ? 37.192  29.971  -0.861  1.00 62.60  ? 256  THR A N   1 
ATOM   1020 C CA  . THR A 1 161 ? 35.994  29.792  -0.043  1.00 58.27  ? 256  THR A CA  1 
ATOM   1021 C C   . THR A 1 161 ? 36.375  29.707  1.431   1.00 59.19  ? 256  THR A C   1 
ATOM   1022 O O   . THR A 1 161 ? 37.246  28.917  1.809   1.00 58.63  ? 256  THR A O   1 
ATOM   1023 C CB  . THR A 1 161 ? 35.212  28.542  -0.458  1.00 55.62  ? 256  THR A CB  1 
ATOM   1024 O OG1 . THR A 1 161 ? 36.027  27.374  -0.285  1.00 61.07  ? 256  THR A OG1 1 
ATOM   1025 C CG2 . THR A 1 161 ? 34.776  28.640  -1.913  1.00 53.97  ? 256  THR A CG2 1 
ATOM   1026 N N   . ASN A 1 162 ? 35.715  30.512  2.266   1.00 53.33  ? 257  ASN A N   1 
ATOM   1027 C CA  . ASN A 1 162 ? 36.020  30.437  3.686   1.00 54.45  ? 257  ASN A CA  1 
ATOM   1028 C C   . ASN A 1 162 ? 35.303  29.286  4.383   1.00 54.66  ? 257  ASN A C   1 
ATOM   1029 O O   . ASN A 1 162 ? 35.671  28.944  5.514   1.00 57.13  ? 257  ASN A O   1 
ATOM   1030 C CB  . ASN A 1 162 ? 35.718  31.771  4.378   1.00 52.87  ? 257  ASN A CB  1 
ATOM   1031 C CG  . ASN A 1 162 ? 34.313  32.265  4.128   1.00 56.29  ? 257  ASN A CG  1 
ATOM   1032 O OD1 . ASN A 1 162 ? 33.427  31.511  3.712   1.00 53.39  ? 257  ASN A OD1 1 
ATOM   1033 N ND2 . ASN A 1 162 ? 34.092  33.547  4.405   1.00 55.42  ? 257  ASN A ND2 1 
ATOM   1034 N N   . ILE A 1 163 ? 34.320  28.663  3.740   1.00 51.29  ? 258  ILE A N   1 
ATOM   1035 C CA  . ILE A 1 163 ? 33.821  27.361  4.171   1.00 51.51  ? 258  ILE A CA  1 
ATOM   1036 C C   . ILE A 1 163 ? 34.669  26.296  3.490   1.00 55.95  ? 258  ILE A C   1 
ATOM   1037 O O   . ILE A 1 163 ? 34.709  26.221  2.256   1.00 55.67  ? 258  ILE A O   1 
ATOM   1038 C CB  . ILE A 1 163 ? 32.334  27.191  3.828   1.00 50.79  ? 258  ILE A CB  1 
ATOM   1039 C CG1 . ILE A 1 163 ? 31.501  28.207  4.620   1.00 49.00  ? 258  ILE A CG1 1 
ATOM   1040 C CG2 . ILE A 1 163 ? 31.894  25.742  4.089   1.00 49.50  ? 258  ILE A CG2 1 
ATOM   1041 C CD1 . ILE A 1 163 ? 30.028  28.255  4.243   1.00 49.36  ? 258  ILE A CD1 1 
ATOM   1042 N N   . LYS A 1 164 ? 35.364  25.484  4.287   1.00 55.58  ? 259  LYS A N   1 
ATOM   1043 C CA  . LYS A 1 164 ? 36.322  24.524  3.762   1.00 57.67  ? 259  LYS A CA  1 
ATOM   1044 C C   . LYS A 1 164 ? 35.695  23.167  3.489   1.00 58.02  ? 259  LYS A C   1 
ATOM   1045 O O   . LYS A 1 164 ? 36.411  22.173  3.345   1.00 66.26  ? 259  LYS A O   1 
ATOM   1046 C CB  . LYS A 1 164 ? 37.507  24.392  4.720   1.00 60.17  ? 259  LYS A CB  1 
ATOM   1047 C CG  . LYS A 1 164 ? 38.225  25.722  4.954   1.00 61.30  ? 259  LYS A CG  1 
ATOM   1048 C CD  . LYS A 1 164 ? 38.789  26.288  3.647   1.00 61.51  ? 259  LYS A CD  1 
ATOM   1049 C CE  . LYS A 1 164 ? 39.312  27.707  3.828   1.00 61.46  ? 259  LYS A CE  1 
ATOM   1050 N NZ  . LYS A 1 164 ? 39.860  28.273  2.548   1.00 63.19  ? 259  LYS A NZ  1 
ATOM   1051 N N   . TYR A 1 165 ? 34.377  23.106  3.422   1.00 58.23  ? 260  TYR A N   1 
ATOM   1052 C CA  . TYR A 1 165 ? 33.640  21.933  2.991   1.00 56.83  ? 260  TYR A CA  1 
ATOM   1053 C C   . TYR A 1 165 ? 33.081  22.189  1.598   1.00 54.92  ? 260  TYR A C   1 
ATOM   1054 O O   . TYR A 1 165 ? 32.921  23.336  1.173   1.00 51.68  ? 260  TYR A O   1 
ATOM   1055 C CB  . TYR A 1 165 ? 32.498  21.622  3.966   1.00 58.86  ? 260  TYR A CB  1 
ATOM   1056 C CG  . TYR A 1 165 ? 32.961  21.043  5.283   1.00 65.70  ? 260  TYR A CG  1 
ATOM   1057 C CD1 . TYR A 1 165 ? 32.730  19.709  5.586   1.00 67.11  ? 260  TYR A CD1 1 
ATOM   1058 C CD2 . TYR A 1 165 ? 33.634  21.824  6.222   1.00 66.45  ? 260  TYR A CD2 1 
ATOM   1059 C CE1 . TYR A 1 165 ? 33.154  19.163  6.782   1.00 69.06  ? 260  TYR A CE1 1 
ATOM   1060 C CE2 . TYR A 1 165 ? 34.062  21.281  7.427   1.00 67.08  ? 260  TYR A CE2 1 
ATOM   1061 C CZ  . TYR A 1 165 ? 33.815  19.949  7.697   1.00 69.91  ? 260  TYR A CZ  1 
ATOM   1062 O OH  . TYR A 1 165 ? 34.233  19.381  8.883   1.00 76.55  ? 260  TYR A OH  1 
ATOM   1063 N N   . GLU A 1 166 ? 32.791  21.108  0.887   1.00 52.29  ? 261  GLU A N   1 
ATOM   1064 C CA  . GLU A 1 166 ? 32.127  21.181  -0.402  1.00 53.57  ? 261  GLU A CA  1 
ATOM   1065 C C   . GLU A 1 166 ? 30.827  20.403  -0.357  1.00 52.96  ? 261  GLU A C   1 
ATOM   1066 O O   . GLU A 1 166 ? 30.728  19.366  0.312   1.00 53.53  ? 261  GLU A O   1 
ATOM   1067 C CB  . GLU A 1 166 ? 32.988  20.604  -1.515  1.00 53.10  ? 261  GLU A CB  1 
ATOM   1068 C CG  . GLU A 1 166 ? 34.434  20.820  -1.297  1.00 58.50  ? 261  GLU A CG  1 
ATOM   1069 C CD  . GLU A 1 166 ? 35.249  20.315  -2.451  1.00 64.69  ? 261  GLU A CD  1 
ATOM   1070 O OE1 . GLU A 1 166 ? 35.782  21.169  -3.200  1.00 60.87  ? 261  GLU A OE1 1 
ATOM   1071 O OE2 . GLU A 1 166 ? 35.340  19.069  -2.604  1.00 64.87  ? 261  GLU A OE2 1 
ATOM   1072 N N   . ALA A 1 167 ? 29.853  20.891  -1.118  1.00 48.69  ? 262  ALA A N   1 
ATOM   1073 C CA  . ALA A 1 167 ? 28.606  20.168  -1.351  1.00 48.46  ? 262  ALA A CA  1 
ATOM   1074 C C   . ALA A 1 167 ? 28.714  19.405  -2.663  1.00 53.16  ? 262  ALA A C   1 
ATOM   1075 O O   . ALA A 1 167 ? 29.112  19.981  -3.675  1.00 51.87  ? 262  ALA A O   1 
ATOM   1076 C CB  . ALA A 1 167 ? 27.412  21.126  -1.394  1.00 47.67  ? 262  ALA A CB  1 
ATOM   1077 N N   . HIS A 1 168 ? 28.417  18.111  -2.633  1.00 47.61  ? 263  HIS A N   1 
ATOM   1078 C CA  . HIS A 1 168 ? 28.245  17.327  -3.847  1.00 50.13  ? 263  HIS A CA  1 
ATOM   1079 C C   . HIS A 1 168 ? 26.761  17.312  -4.199  1.00 52.49  ? 263  HIS A C   1 
ATOM   1080 O O   . HIS A 1 168 ? 25.930  16.842  -3.406  1.00 52.77  ? 263  HIS A O   1 
ATOM   1081 C CB  . HIS A 1 168 ? 28.810  15.922  -3.668  1.00 50.62  ? 263  HIS A CB  1 
ATOM   1082 C CG  . HIS A 1 168 ? 30.308  15.885  -3.713  1.00 53.64  ? 263  HIS A CG  1 
ATOM   1083 N ND1 . HIS A 1 168 ? 31.097  16.331  -2.673  1.00 55.17  ? 263  HIS A ND1 1 
ATOM   1084 C CD2 . HIS A 1 168 ? 31.161  15.517  -4.699  1.00 56.33  ? 263  HIS A CD2 1 
ATOM   1085 C CE1 . HIS A 1 168 ? 32.371  16.209  -3.004  1.00 55.98  ? 263  HIS A CE1 1 
ATOM   1086 N NE2 . HIS A 1 168 ? 32.438  15.723  -4.231  1.00 57.41  ? 263  HIS A NE2 1 
ATOM   1087 N N   . ILE A 1 169 ? 26.439  17.864  -5.371  1.00 49.95  ? 264  ILE A N   1 
ATOM   1088 C CA  . ILE A 1 169 ? 25.072  18.197  -5.756  1.00 50.69  ? 264  ILE A CA  1 
ATOM   1089 C C   . ILE A 1 169 ? 24.315  16.937  -6.154  1.00 54.31  ? 264  ILE A C   1 
ATOM   1090 O O   . ILE A 1 169 ? 24.748  16.184  -7.032  1.00 54.44  ? 264  ILE A O   1 
ATOM   1091 C CB  . ILE A 1 169 ? 25.077  19.218  -6.909  1.00 50.65  ? 264  ILE A CB  1 
ATOM   1092 C CG1 . ILE A 1 169 ? 25.687  20.550  -6.449  1.00 47.42  ? 264  ILE A CG1 1 
ATOM   1093 C CG2 . ILE A 1 169 ? 23.665  19.407  -7.497  1.00 45.35  ? 264  ILE A CG2 1 
ATOM   1094 C CD1 . ILE A 1 169 ? 25.900  21.532  -7.561  1.00 46.63  ? 264  ILE A CD1 1 
ATOM   1095 N N   . ARG A 1 170 ? 23.166  16.718  -5.524  1.00 52.28  ? 265  ARG A N   1 
ATOM   1096 C CA  . ARG A 1 170 ? 22.185  15.757  -6.010  1.00 52.10  ? 265  ARG A CA  1 
ATOM   1097 C C   . ARG A 1 170 ? 21.023  16.428  -6.734  1.00 49.81  ? 265  ARG A C   1 
ATOM   1098 O O   . ARG A 1 170 ? 20.552  15.907  -7.746  1.00 51.85  ? 265  ARG A O   1 
ATOM   1099 C CB  . ARG A 1 170 ? 21.648  14.902  -4.856  1.00 54.78  ? 265  ARG A CB  1 
ATOM   1100 C CG  . ARG A 1 170 ? 22.738  14.316  -3.935  1.00 61.21  ? 265  ARG A CG  1 
ATOM   1101 C CD  . ARG A 1 170 ? 23.914  13.660  -4.682  1.00 70.31  ? 265  ARG A CD  1 
ATOM   1102 N NE  . ARG A 1 170 ? 23.805  12.209  -4.805  1.00 78.25  ? 265  ARG A NE  1 
ATOM   1103 C CZ  . ARG A 1 170 ? 23.773  11.549  -5.957  1.00 82.38  ? 265  ARG A CZ  1 
ATOM   1104 N NH1 . ARG A 1 170 ? 23.608  10.233  -5.998  1.00 88.09  ? 265  ARG A NH1 1 
ATOM   1105 N NH2 . ARG A 1 170 ? 23.915  12.225  -7.096  1.00 79.15  ? 265  ARG A NH2 1 
ATOM   1106 N N   . LYS A 1 171 ? 20.552  17.578  -6.258  1.00 45.42  ? 266  LYS A N   1 
ATOM   1107 C CA  . LYS A 1 171 ? 19.529  18.326  -6.972  1.00 46.93  ? 266  LYS A CA  1 
ATOM   1108 C C   . LYS A 1 171 ? 19.902  19.796  -6.946  1.00 46.71  ? 266  LYS A C   1 
ATOM   1109 O O   . LYS A 1 171 ? 20.580  20.254  -6.025  1.00 46.05  ? 266  LYS A O   1 
ATOM   1110 C CB  . LYS A 1 171 ? 18.121  18.129  -6.369  1.00 48.38  ? 266  LYS A CB  1 
ATOM   1111 C CG  . LYS A 1 171 ? 17.596  16.697  -6.460  1.00 54.91  ? 266  LYS A CG  1 
ATOM   1112 C CD  . LYS A 1 171 ? 16.144  16.563  -5.999  1.00 53.56  ? 266  LYS A CD  1 
ATOM   1113 C CE  . LYS A 1 171 ? 15.673  15.101  -6.109  1.00 56.72  ? 266  LYS A CE  1 
ATOM   1114 N NZ  . LYS A 1 171 ? 14.181  14.977  -6.081  1.00 63.73  ? 266  LYS A NZ  1 
ATOM   1115 N N   . ILE A 1 172 ? 19.450  20.533  -7.960  1.00 44.53  ? 267  ILE A N   1 
ATOM   1116 C CA  . ILE A 1 172 ? 19.674  21.974  -8.002  1.00 42.68  ? 267  ILE A CA  1 
ATOM   1117 C C   . ILE A 1 172 ? 18.552  22.663  -8.766  1.00 45.78  ? 267  ILE A C   1 
ATOM   1118 O O   . ILE A 1 172 ? 18.339  22.399  -9.954  1.00 43.19  ? 267  ILE A O   1 
ATOM   1119 C CB  . ILE A 1 172 ? 21.041  22.308  -8.627  1.00 44.79  ? 267  ILE A CB  1 
ATOM   1120 C CG1 . ILE A 1 172 ? 21.192  23.832  -8.753  1.00 40.02  ? 267  ILE A CG1 1 
ATOM   1121 C CG2 . ILE A 1 172 ? 21.243  21.555  -9.968  1.00 38.90  ? 267  ILE A CG2 1 
ATOM   1122 C CD1 . ILE A 1 172 ? 22.565  24.259  -9.190  1.00 41.91  ? 267  ILE A CD1 1 
ATOM   1123 N N   . PHE A 1 173 ? 17.832  23.558  -8.095  1.00 42.87  ? 268  PHE A N   1 
ATOM   1124 C CA  . PHE A 1 173 ? 16.696  24.254  -8.679  1.00 42.84  ? 268  PHE A CA  1 
ATOM   1125 C C   . PHE A 1 173 ? 16.948  25.744  -8.577  1.00 44.36  ? 268  PHE A C   1 
ATOM   1126 O O   . PHE A 1 173 ? 17.531  26.209  -7.595  1.00 43.44  ? 268  PHE A O   1 
ATOM   1127 C CB  . PHE A 1 173 ? 15.381  23.891  -7.969  1.00 45.15  ? 268  PHE A CB  1 
ATOM   1128 C CG  . PHE A 1 173 ? 15.093  22.409  -7.954  1.00 49.74  ? 268  PHE A CG  1 
ATOM   1129 C CD1 . PHE A 1 173 ? 14.628  21.770  -9.095  1.00 48.19  ? 268  PHE A CD1 1 
ATOM   1130 C CD2 . PHE A 1 173 ? 15.296  21.658  -6.803  1.00 49.08  ? 268  PHE A CD2 1 
ATOM   1131 C CE1 . PHE A 1 173 ? 14.366  20.400  -9.087  1.00 50.97  ? 268  PHE A CE1 1 
ATOM   1132 C CE2 . PHE A 1 173 ? 15.044  20.287  -6.789  1.00 50.64  ? 268  PHE A CE2 1 
ATOM   1133 C CZ  . PHE A 1 173 ? 14.576  19.663  -7.926  1.00 52.65  ? 268  PHE A CZ  1 
ATOM   1134 N N   . CYS A 1 174 ? 16.545  26.486  -9.605  1.00 41.13  ? 269  CYS A N   1 
ATOM   1135 C CA  . CYS A 1 174 ? 16.769  27.926  -9.656  1.00 44.09  ? 269  CYS A CA  1 
ATOM   1136 C C   . CYS A 1 174 ? 15.455  28.631  -9.323  1.00 45.20  ? 269  CYS A C   1 
ATOM   1137 O O   . CYS A 1 174 ? 14.471  28.507  -10.060 1.00 46.36  ? 269  CYS A O   1 
ATOM   1138 C CB  . CYS A 1 174 ? 17.302  28.357  -11.021 1.00 42.32  ? 269  CYS A CB  1 
ATOM   1139 S SG  . CYS A 1 174 ? 17.573  30.153  -11.141 1.00 44.86  ? 269  CYS A SG  1 
ATOM   1140 N N   . ILE A 1 175 ? 15.433  29.354  -8.203  1.00 39.82  ? 270  ILE A N   1 
ATOM   1141 C CA  . ILE A 1 175 ? 14.225  30.070  -7.816  1.00 45.92  ? 270  ILE A CA  1 
ATOM   1142 C C   . ILE A 1 175 ? 14.224  31.523  -8.282  1.00 45.88  ? 270  ILE A C   1 
ATOM   1143 O O   . ILE A 1 175 ? 13.157  32.145  -8.307  1.00 45.30  ? 270  ILE A O   1 
ATOM   1144 C CB  . ILE A 1 175 ? 14.007  30.010  -6.294  1.00 47.96  ? 270  ILE A CB  1 
ATOM   1145 C CG1 . ILE A 1 175 ? 15.175  30.683  -5.567  1.00 43.49  ? 270  ILE A CG1 1 
ATOM   1146 C CG2 . ILE A 1 175 ? 13.814  28.556  -5.844  1.00 46.45  ? 270  ILE A CG2 1 
ATOM   1147 C CD1 . ILE A 1 175 ? 14.842  31.136  -4.176  1.00 44.19  ? 270  ILE A CD1 1 
ATOM   1148 N N   . SER A 1 176 ? 15.379  32.076  -8.655  1.00 42.02  ? 271  SER A N   1 
ATOM   1149 C CA  . SER A 1 176 ? 15.436  33.410  -9.245  1.00 42.15  ? 271  SER A CA  1 
ATOM   1150 C C   . SER A 1 176 ? 16.590  33.450  -10.240 1.00 44.45  ? 271  SER A C   1 
ATOM   1151 O O   . SER A 1 176 ? 17.761  33.403  -9.842  1.00 41.04  ? 271  SER A O   1 
ATOM   1152 C CB  . SER A 1 176 ? 15.610  34.482  -8.178  1.00 42.76  ? 271  SER A CB  1 
ATOM   1153 O OG  . SER A 1 176 ? 15.756  35.752  -8.794  1.00 41.97  ? 271  SER A OG  1 
ATOM   1154 N N   . LYS A 1 177 ? 16.265  33.562  -11.526 1.00 41.32  ? 272  LYS A N   1 
ATOM   1155 C CA  . LYS A 1 177 ? 17.273  33.595  -12.579 1.00 46.89  ? 272  LYS A CA  1 
ATOM   1156 C C   . LYS A 1 177 ? 17.669  35.036  -12.905 1.00 45.32  ? 272  LYS A C   1 
ATOM   1157 O O   . LYS A 1 177 ? 16.803  35.900  -13.067 1.00 45.38  ? 272  LYS A O   1 
ATOM   1158 C CB  . LYS A 1 177 ? 16.753  32.894  -13.838 1.00 43.24  ? 272  LYS A CB  1 
ATOM   1159 C CG  . LYS A 1 177 ? 17.772  32.898  -14.960 1.00 47.47  ? 272  LYS A CG  1 
ATOM   1160 C CD  . LYS A 1 177 ? 17.257  32.173  -16.181 1.00 48.96  ? 272  LYS A CD  1 
ATOM   1161 C CE  . LYS A 1 177 ? 17.500  32.974  -17.430 1.00 59.75  ? 272  LYS A CE  1 
ATOM   1162 N NZ  . LYS A 1 177 ? 16.320  33.828  -17.755 1.00 64.60  ? 272  LYS A NZ  1 
ATOM   1163 N N   . THR A 1 178 ? 18.978  35.293  -12.986 1.00 40.23  ? 273  THR A N   1 
ATOM   1164 C CA  . THR A 1 178 ? 19.459  36.588  -13.454 1.00 42.86  ? 273  THR A CA  1 
ATOM   1165 C C   . THR A 1 178 ? 18.863  36.893  -14.827 1.00 46.89  ? 273  THR A C   1 
ATOM   1166 O O   . THR A 1 178 ? 18.957  36.079  -15.752 1.00 49.45  ? 273  THR A O   1 
ATOM   1167 C CB  . THR A 1 178 ? 20.991  36.591  -13.523 1.00 43.14  ? 273  THR A CB  1 
ATOM   1168 O OG1 . THR A 1 178 ? 21.527  36.563  -12.196 1.00 44.42  ? 273  THR A OG1 1 
ATOM   1169 C CG2 . THR A 1 178 ? 21.528  37.830  -14.253 1.00 43.26  ? 273  THR A CG2 1 
ATOM   1170 N N   . ALA A 1 179 ? 18.238  38.064  -14.960 1.00 44.50  ? 274  ALA A N   1 
ATOM   1171 C CA  . ALA A 1 179 ? 17.531  38.398  -16.189 1.00 47.65  ? 274  ALA A CA  1 
ATOM   1172 C C   . ALA A 1 179 ? 18.340  39.260  -17.142 1.00 49.51  ? 274  ALA A C   1 
ATOM   1173 O O   . ALA A 1 179 ? 17.967  39.380  -18.308 1.00 49.14  ? 274  ALA A O   1 
ATOM   1174 C CB  . ALA A 1 179 ? 16.215  39.115  -15.874 1.00 44.89  ? 274  ALA A CB  1 
ATOM   1175 N N   . LYS A 1 180 ? 19.439  39.836  -16.686 1.00 48.99  ? 275  LYS A N   1 
ATOM   1176 C CA  . LYS A 1 180 ? 20.145  40.862  -17.435 1.00 50.29  ? 275  LYS A CA  1 
ATOM   1177 C C   . LYS A 1 180 ? 21.645  40.669  -17.283 1.00 50.79  ? 275  LYS A C   1 
ATOM   1178 O O   . LYS A 1 180 ? 22.128  40.252  -16.228 1.00 44.54  ? 275  LYS A O   1 
ATOM   1179 C CB  . LYS A 1 180 ? 19.723  42.248  -16.945 1.00 52.49  ? 275  LYS A CB  1 
ATOM   1180 C CG  . LYS A 1 180 ? 20.119  43.387  -17.836 1.00 57.88  ? 275  LYS A CG  1 
ATOM   1181 C CD  . LYS A 1 180 ? 19.276  44.605  -17.488 1.00 61.13  ? 275  LYS A CD  1 
ATOM   1182 C CE  . LYS A 1 180 ? 20.154  45.729  -16.986 1.00 64.29  ? 275  LYS A CE  1 
ATOM   1183 N NZ  . LYS A 1 180 ? 19.612  47.062  -17.393 1.00 67.75  ? 275  LYS A NZ  1 
ATOM   1184 N N   . GLU A 1 181 ? 22.371  40.971  -18.353 1.00 49.74  ? 276  GLU A N   1 
ATOM   1185 C CA  . GLU A 1 181 ? 23.822  40.934  -18.302 1.00 54.42  ? 276  GLU A CA  1 
ATOM   1186 C C   . GLU A 1 181 ? 24.326  41.926  -17.258 1.00 53.43  ? 276  GLU A C   1 
ATOM   1187 O O   . GLU A 1 181 ? 23.853  43.067  -17.184 1.00 50.74  ? 276  GLU A O   1 
ATOM   1188 C CB  . GLU A 1 181 ? 24.395  41.254  -19.685 1.00 56.15  ? 276  GLU A CB  1 
ATOM   1189 C CG  . GLU A 1 181 ? 25.862  41.627  -19.693 1.00 60.17  ? 276  GLU A CG  1 
ATOM   1190 C CD  . GLU A 1 181 ? 26.332  42.080  -21.073 1.00 67.97  ? 276  GLU A CD  1 
ATOM   1191 O OE1 . GLU A 1 181 ? 25.995  41.416  -22.077 1.00 69.87  ? 276  GLU A OE1 1 
ATOM   1192 O OE2 . GLU A 1 181 ? 27.031  43.112  -21.156 1.00 73.63  ? 276  GLU A OE2 1 
ATOM   1193 N N   . LEU A 1 182 ? 25.280  41.483  -16.442 1.00 50.47  ? 277  LEU A N   1 
ATOM   1194 C CA  . LEU A 1 182 ? 25.741  42.294  -15.330 1.00 51.79  ? 277  LEU A CA  1 
ATOM   1195 C C   . LEU A 1 182 ? 26.479  43.531  -15.841 1.00 52.98  ? 277  LEU A C   1 
ATOM   1196 O O   . LEU A 1 182 ? 27.158  43.474  -16.869 1.00 52.18  ? 277  LEU A O   1 
ATOM   1197 C CB  . LEU A 1 182 ? 26.648  41.472  -14.415 1.00 51.76  ? 277  LEU A CB  1 
ATOM   1198 C CG  . LEU A 1 182 ? 25.976  40.920  -13.146 1.00 54.82  ? 277  LEU A CG  1 
ATOM   1199 C CD1 . LEU A 1 182 ? 24.850  39.975  -13.489 1.00 52.33  ? 277  LEU A CD1 1 
ATOM   1200 C CD2 . LEU A 1 182 ? 27.007  40.199  -12.296 1.00 59.25  ? 277  LEU A CD2 1 
ATOM   1201 N N   . PRO A 1 183 ? 26.367  44.661  -15.145 1.00 51.76  ? 278  PRO A N   1 
ATOM   1202 C CA  . PRO A 1 183 ? 27.094  45.855  -15.596 1.00 50.38  ? 278  PRO A CA  1 
ATOM   1203 C C   . PRO A 1 183 ? 28.590  45.690  -15.491 1.00 50.84  ? 278  PRO A C   1 
ATOM   1204 O O   . PRO A 1 183 ? 29.328  46.340  -16.241 1.00 52.87  ? 278  PRO A O   1 
ATOM   1205 C CB  . PRO A 1 183 ? 26.580  46.957  -14.658 1.00 48.97  ? 278  PRO A CB  1 
ATOM   1206 C CG  . PRO A 1 183 ? 26.226  46.203  -13.403 1.00 49.69  ? 278  PRO A CG  1 
ATOM   1207 C CD  . PRO A 1 183 ? 25.657  44.888  -13.875 1.00 51.22  ? 278  PRO A CD  1 
ATOM   1208 N N   . PHE A 1 184 ? 29.053  44.834  -14.585 1.00 49.57  ? 279  PHE A N   1 
ATOM   1209 C CA  . PHE A 1 184 ? 30.459  44.475  -14.487 1.00 50.62  ? 279  PHE A CA  1 
ATOM   1210 C C   . PHE A 1 184 ? 30.542  43.145  -13.752 1.00 52.45  ? 279  PHE A C   1 
ATOM   1211 O O   . PHE A 1 184 ? 29.553  42.650  -13.213 1.00 52.84  ? 279  PHE A O   1 
ATOM   1212 C CB  . PHE A 1 184 ? 31.285  45.566  -13.789 1.00 51.62  ? 279  PHE A CB  1 
ATOM   1213 C CG  . PHE A 1 184 ? 30.655  46.111  -12.534 1.00 50.85  ? 279  PHE A CG  1 
ATOM   1214 C CD1 . PHE A 1 184 ? 29.982  47.323  -12.554 1.00 49.83  ? 279  PHE A CD1 1 
ATOM   1215 C CD2 . PHE A 1 184 ? 30.757  45.430  -11.329 1.00 51.17  ? 279  PHE A CD2 1 
ATOM   1216 C CE1 . PHE A 1 184 ? 29.410  47.846  -11.402 1.00 51.67  ? 279  PHE A CE1 1 
ATOM   1217 C CE2 . PHE A 1 184 ? 30.173  45.940  -10.161 1.00 49.83  ? 279  PHE A CE2 1 
ATOM   1218 C CZ  . PHE A 1 184 ? 29.500  47.150  -10.199 1.00 46.29  ? 279  PHE A CZ  1 
ATOM   1219 N N   . LEU A 1 185 ? 31.735  42.566  -13.742 1.00 50.36  ? 280  LEU A N   1 
ATOM   1220 C CA  . LEU A 1 185 ? 31.934  41.269  -13.118 1.00 52.25  ? 280  LEU A CA  1 
ATOM   1221 C C   . LEU A 1 185 ? 32.314  41.445  -11.656 1.00 51.71  ? 280  LEU A C   1 
ATOM   1222 O O   . LEU A 1 185 ? 33.155  42.287  -11.322 1.00 51.95  ? 280  LEU A O   1 
ATOM   1223 C CB  . LEU A 1 185 ? 33.001  40.477  -13.875 1.00 52.06  ? 280  LEU A CB  1 
ATOM   1224 C CG  . LEU A 1 185 ? 32.574  40.116  -15.304 1.00 51.68  ? 280  LEU A CG  1 
ATOM   1225 C CD1 . LEU A 1 185 ? 33.665  39.352  -16.003 1.00 49.47  ? 280  LEU A CD1 1 
ATOM   1226 C CD2 . LEU A 1 185 ? 31.279  39.304  -15.280 1.00 50.26  ? 280  LEU A CD2 1 
ATOM   1227 N N   . LEU A 1 186 ? 31.677  40.660  -10.783 1.00 50.46  ? 281  LEU A N   1 
ATOM   1228 C CA  . LEU A 1 186 ? 32.029  40.711  -9.365  1.00 50.40  ? 281  LEU A CA  1 
ATOM   1229 C C   . LEU A 1 186 ? 33.483  40.325  -9.133  1.00 51.04  ? 281  LEU A C   1 
ATOM   1230 O O   . LEU A 1 186 ? 34.131  40.847  -8.217  1.00 52.86  ? 281  LEU A O   1 
ATOM   1231 C CB  . LEU A 1 186 ? 31.103  39.805  -8.554  1.00 52.34  ? 281  LEU A CB  1 
ATOM   1232 C CG  . LEU A 1 186 ? 29.755  40.439  -8.223  1.00 49.42  ? 281  LEU A CG  1 
ATOM   1233 C CD1 . LEU A 1 186 ? 29.006  39.573  -7.240  1.00 47.70  ? 281  LEU A CD1 1 
ATOM   1234 C CD2 . LEU A 1 186 ? 29.979  41.832  -7.632  1.00 48.79  ? 281  LEU A CD2 1 
ATOM   1235 N N   . LYS A 1 187 ? 34.007  39.390  -9.931  1.00 50.20  ? 282  LYS A N   1 
ATOM   1236 C CA  . LYS A 1 187 ? 35.418  39.042  -9.821  1.00 52.82  ? 282  LYS A CA  1 
ATOM   1237 C C   . LYS A 1 187 ? 36.295  40.276  -10.001 1.00 53.98  ? 282  LYS A C   1 
ATOM   1238 O O   . LYS A 1 187 ? 37.305  40.446  -9.304  1.00 56.00  ? 282  LYS A O   1 
ATOM   1239 C CB  . LYS A 1 187 ? 35.768  37.970  -10.862 1.00 55.28  ? 282  LYS A CB  1 
ATOM   1240 C CG  . LYS A 1 187 ? 37.223  37.569  -10.887 1.00 59.89  ? 282  LYS A CG  1 
ATOM   1241 C CD  . LYS A 1 187 ? 37.601  36.864  -12.200 1.00 67.14  ? 282  LYS A CD  1 
ATOM   1242 N N   . ASP A 1 188 ? 35.914  41.155  -10.932 1.00 52.81  ? 283  ASP A N   1 
ATOM   1243 C CA  . ASP A 1 188 ? 36.632  42.411  -11.122 1.00 54.92  ? 283  ASP A CA  1 
ATOM   1244 C C   . ASP A 1 188 ? 36.332  43.413  -10.009 1.00 54.27  ? 283  ASP A C   1 
ATOM   1245 O O   . ASP A 1 188 ? 37.250  44.057  -9.488  1.00 53.77  ? 283  ASP A O   1 
ATOM   1246 C CB  . ASP A 1 188 ? 36.277  43.002  -12.482 1.00 54.13  ? 283  ASP A CB  1 
ATOM   1247 C CG  . ASP A 1 188 ? 36.774  42.148  -13.625 1.00 58.99  ? 283  ASP A CG  1 
ATOM   1248 O OD1 . ASP A 1 188 ? 37.798  41.468  -13.431 1.00 59.79  ? 283  ASP A OD1 1 
ATOM   1249 O OD2 . ASP A 1 188 ? 36.148  42.157  -14.709 1.00 56.18  ? 283  ASP A OD2 1 
ATOM   1250 N N   . ALA A 1 189 ? 35.058  43.562  -9.628  1.00 50.07  ? 284  ALA A N   1 
ATOM   1251 C CA  . ALA A 1 189 ? 34.731  44.523  -8.578  1.00 50.95  ? 284  ALA A CA  1 
ATOM   1252 C C   . ALA A 1 189 ? 35.369  44.148  -7.241  1.00 49.00  ? 284  ALA A C   1 
ATOM   1253 O O   . ALA A 1 189 ? 35.642  45.028  -6.417  1.00 49.36  ? 284  ALA A O   1 
ATOM   1254 C CB  . ALA A 1 189 ? 33.217  44.656  -8.445  1.00 51.21  ? 284  ALA A CB  1 
ATOM   1255 N N   . ASN A 1 190 ? 35.664  42.863  -7.025  1.00 50.00  ? 285  ASN A N   1 
ATOM   1256 C CA  . ASN A 1 190 ? 36.266  42.409  -5.771  1.00 50.76  ? 285  ASN A CA  1 
ATOM   1257 C C   . ASN A 1 190 ? 37.779  42.577  -5.709  1.00 52.29  ? 285  ASN A C   1 
ATOM   1258 O O   . ASN A 1 190 ? 38.346  42.471  -4.616  1.00 53.40  ? 285  ASN A O   1 
ATOM   1259 C CB  . ASN A 1 190 ? 35.933  40.934  -5.534  1.00 48.74  ? 285  ASN A CB  1 
ATOM   1260 C CG  . ASN A 1 190 ? 34.641  40.758  -4.784  1.00 48.54  ? 285  ASN A CG  1 
ATOM   1261 O OD1 . ASN A 1 190 ? 34.507  41.250  -3.663  1.00 46.96  ? 285  ASN A OD1 1 
ATOM   1262 N ND2 . ASN A 1 190 ? 33.662  40.094  -5.406  1.00 44.45  ? 285  ASN A ND2 1 
ATOM   1263 N N   . MET A 1 191 ? 38.445  42.825  -6.836  1.00 51.66  ? 286  MET A N   1 
ATOM   1264 C CA  . MET A 1 191 ? 39.900  42.765  -6.873  1.00 57.59  ? 286  MET A CA  1 
ATOM   1265 C C   . MET A 1 191 ? 40.527  43.966  -6.169  1.00 56.43  ? 286  MET A C   1 
ATOM   1266 O O   . MET A 1 191 ? 40.111  45.110  -6.364  1.00 56.48  ? 286  MET A O   1 
ATOM   1267 C CB  . MET A 1 191 ? 40.385  42.702  -8.325  1.00 61.74  ? 286  MET A CB  1 
ATOM   1268 C CG  . MET A 1 191 ? 41.754  42.063  -8.505  1.00 69.21  ? 286  MET A CG  1 
ATOM   1269 S SD  . MET A 1 191 ? 41.662  40.257  -8.528  1.00 91.73  ? 286  MET A SD  1 
ATOM   1270 C CE  . MET A 1 191 ? 40.864  39.968  -10.114 1.00 72.79  ? 286  MET A CE  1 
ATOM   1271 N N   . LYS A 1 192 ? 41.530  43.699  -5.335  1.00 59.36  ? 287  LYS A N   1 
ATOM   1272 C CA  . LYS A 1 192 ? 42.409  44.765  -4.871  1.00 63.40  ? 287  LYS A CA  1 
ATOM   1273 C C   . LYS A 1 192 ? 43.004  45.471  -6.085  1.00 70.38  ? 287  LYS A C   1 
ATOM   1274 O O   . LYS A 1 192 ? 43.458  44.820  -7.028  1.00 72.94  ? 287  LYS A O   1 
ATOM   1275 C CB  . LYS A 1 192 ? 43.512  44.187  -3.982  1.00 62.04  ? 287  LYS A CB  1 
ATOM   1276 C CG  . LYS A 1 192 ? 44.572  45.186  -3.589  1.00 67.03  ? 287  LYS A CG  1 
ATOM   1277 C CD  . LYS A 1 192 ? 45.167  44.855  -2.224  1.00 65.13  ? 287  LYS A CD  1 
ATOM   1278 C CE  . LYS A 1 192 ? 45.729  43.445  -2.185  1.00 69.66  ? 287  LYS A CE  1 
ATOM   1279 N NZ  . LYS A 1 192 ? 47.009  43.405  -1.415  1.00 71.23  ? 287  LYS A NZ  1 
ATOM   1280 N N   . GLU A 1 193 ? 42.959  46.799  -6.094  1.00 67.56  ? 288  GLU A N   1 
ATOM   1281 C CA  . GLU A 1 193 ? 43.263  47.516  -7.324  1.00 82.69  ? 288  GLU A CA  1 
ATOM   1282 C C   . GLU A 1 193 ? 44.768  47.565  -7.562  1.00 92.12  ? 288  GLU A C   1 
ATOM   1283 O O   . GLU A 1 193 ? 45.541  47.937  -6.673  1.00 88.77  ? 288  GLU A O   1 
ATOM   1284 C CB  . GLU A 1 193 ? 42.675  48.923  -7.300  1.00 88.29  ? 288  GLU A CB  1 
ATOM   1285 C CG  . GLU A 1 193 ? 41.962  49.254  -8.603  1.00 92.28  ? 288  GLU A CG  1 
ATOM   1286 C CD  . GLU A 1 193 ? 41.554  50.706  -8.709  1.00 94.53  ? 288  GLU A CD  1 
ATOM   1287 O OE1 . GLU A 1 193 ? 40.910  51.215  -7.761  1.00 88.26  ? 288  GLU A OE1 1 
ATOM   1288 O OE2 . GLU A 1 193 ? 41.887  51.331  -9.744  1.00 98.99  ? 288  GLU A OE2 1 
ATOM   1289 N N   . THR A 1 194 ? 45.175  47.180  -8.770  1.00 97.82  ? 289  THR A N   1 
ATOM   1290 C CA  . THR A 1 194 ? 46.574  46.959  -9.093  1.00 102.75 ? 289  THR A CA  1 
ATOM   1291 C C   . THR A 1 194 ? 46.843  47.469  -10.502 1.00 106.79 ? 289  THR A C   1 
ATOM   1292 O O   . THR A 1 194 ? 45.924  47.831  -11.241 1.00 106.97 ? 289  THR A O   1 
ATOM   1293 C CB  . THR A 1 194 ? 46.941  45.465  -8.972  1.00 105.35 ? 289  THR A CB  1 
ATOM   1294 O OG1 . THR A 1 194 ? 48.354  45.321  -8.805  1.00 111.19 ? 289  THR A OG1 1 
ATOM   1295 C CG2 . THR A 1 194 ? 46.507  44.696  -10.222 1.00 106.38 ? 289  THR A CG2 1 
ATOM   1296 N N   . ASN A 1 195 ? 48.124  47.517  -10.860 1.00 109.42 ? 290  ASN A N   1 
ATOM   1297 C CA  . ASN A 1 195 ? 48.534  47.786  -12.230 1.00 111.92 ? 290  ASN A CA  1 
ATOM   1298 C C   . ASN A 1 195 ? 49.067  46.541  -12.929 1.00 110.30 ? 290  ASN A C   1 
ATOM   1299 O O   . ASN A 1 195 ? 49.479  46.633  -14.092 1.00 110.55 ? 290  ASN A O   1 
ATOM   1300 C CB  . ASN A 1 195 ? 49.581  48.909  -12.271 1.00 110.49 ? 290  ASN A CB  1 
ATOM   1301 C CG  . ASN A 1 195 ? 48.957  50.295  -12.455 1.00 109.57 ? 290  ASN A CG  1 
ATOM   1302 O OD1 . ASN A 1 195 ? 48.029  50.477  -13.241 1.00 110.52 ? 290  ASN A OD1 1 
ATOM   1303 N ND2 . ASN A 1 195 ? 49.477  51.277  -11.728 1.00 108.87 ? 290  ASN A ND2 1 
ATOM   1304 N N   . GLU A 1 196 ? 49.067  45.386  -12.254 1.00 107.70 ? 291  GLU A N   1 
ATOM   1305 C CA  . GLU A 1 196 ? 49.473  44.128  -12.874 1.00 108.58 ? 291  GLU A CA  1 
ATOM   1306 C C   . GLU A 1 196 ? 48.705  43.897  -14.166 1.00 111.04 ? 291  GLU A C   1 
ATOM   1307 O O   . GLU A 1 196 ? 47.484  44.057  -14.206 1.00 111.65 ? 291  GLU A O   1 
ATOM   1308 C CB  . GLU A 1 196 ? 49.234  42.961  -11.911 1.00 106.38 ? 291  GLU A CB  1 
ATOM   1309 C CG  . GLU A 1 196 ? 49.943  43.063  -10.575 1.00 103.83 ? 291  GLU A CG  1 
ATOM   1310 C CD  . GLU A 1 196 ? 49.458  42.014  -9.587  1.00 103.67 ? 291  GLU A CD  1 
ATOM   1311 O OE1 . GLU A 1 196 ? 49.737  42.158  -8.376  1.00 103.10 ? 291  GLU A OE1 1 
ATOM   1312 O OE2 . GLU A 1 196 ? 48.789  41.049  -10.021 1.00 103.82 ? 291  GLU A OE2 1 
ATOM   1313 N N   . GLU A 1 197 ? 49.432  43.513  -15.218 1.00 111.93 ? 292  GLU A N   1 
ATOM   1314 C CA  . GLU A 1 197 ? 48.848  43.375  -16.547 1.00 113.67 ? 292  GLU A CA  1 
ATOM   1315 C C   . GLU A 1 197 ? 47.604  42.494  -16.519 1.00 113.45 ? 292  GLU A C   1 
ATOM   1316 O O   . GLU A 1 197 ? 47.564  41.467  -15.837 1.00 113.79 ? 292  GLU A O   1 
ATOM   1317 C CB  . GLU A 1 197 ? 49.883  42.798  -17.518 1.00 112.23 ? 292  GLU A CB  1 
ATOM   1318 N N   . GLY A 1 198 ? 46.581  42.914  -17.263 1.00 110.76 ? 293  GLY A N   1 
ATOM   1319 C CA  . GLY A 1 198 ? 45.327  42.190  -17.295 1.00 108.06 ? 293  GLY A CA  1 
ATOM   1320 C C   . GLY A 1 198 ? 44.358  42.541  -16.191 1.00 107.22 ? 293  GLY A C   1 
ATOM   1321 O O   . GLY A 1 198 ? 43.410  41.788  -15.954 1.00 103.74 ? 293  GLY A O   1 
ATOM   1322 N N   . SER A 1 199 ? 44.565  43.659  -15.502 1.00 105.58 ? 294  SER A N   1 
ATOM   1323 C CA  . SER A 1 199 ? 43.677  44.083  -14.428 1.00 101.32 ? 294  SER A CA  1 
ATOM   1324 C C   . SER A 1 199 ? 42.528  44.896  -15.003 1.00 95.07  ? 294  SER A C   1 
ATOM   1325 O O   . SER A 1 199 ? 42.742  45.801  -15.817 1.00 93.89  ? 294  SER A O   1 
ATOM   1326 C CB  . SER A 1 199 ? 44.430  44.908  -13.381 1.00 104.31 ? 294  SER A CB  1 
ATOM   1327 O OG  . SER A 1 199 ? 44.329  46.297  -13.656 1.00 104.08 ? 294  SER A OG  1 
ATOM   1328 N N   . ILE A 1 200 ? 41.311  44.565  -14.586 1.00 88.20  ? 295  ILE A N   1 
ATOM   1329 C CA  . ILE A 1 200 ? 40.130  45.347  -14.926 1.00 81.90  ? 295  ILE A CA  1 
ATOM   1330 C C   . ILE A 1 200 ? 39.734  46.144  -13.690 1.00 79.68  ? 295  ILE A C   1 
ATOM   1331 O O   . ILE A 1 200 ? 39.409  45.566  -12.643 1.00 74.99  ? 295  ILE A O   1 
ATOM   1332 C CB  . ILE A 1 200 ? 38.974  44.456  -15.414 1.00 79.01  ? 295  ILE A CB  1 
ATOM   1333 C CG1 . ILE A 1 200 ? 39.454  43.485  -16.500 1.00 78.30  ? 295  ILE A CG1 1 
ATOM   1334 C CG2 . ILE A 1 200 ? 37.826  45.307  -15.952 1.00 73.80  ? 295  ILE A CG2 1 
ATOM   1335 C CD1 . ILE A 1 200 ? 39.688  44.136  -17.842 1.00 82.01  ? 295  ILE A CD1 1 
ATOM   1336 N N   . LYS A 1 201 ? 39.790  47.468  -13.798 1.00 78.37  ? 296  LYS A N   1 
ATOM   1337 C CA  . LYS A 1 201 ? 39.283  48.342  -12.752 1.00 69.25  ? 296  LYS A CA  1 
ATOM   1338 C C   . LYS A 1 201 ? 37.822  48.666  -13.029 1.00 64.19  ? 296  LYS A C   1 
ATOM   1339 O O   . LYS A 1 201 ? 37.425  48.878  -14.179 1.00 64.19  ? 296  LYS A O   1 
ATOM   1340 C CB  . LYS A 1 201 ? 40.110  49.629  -12.670 1.00 67.91  ? 296  LYS A CB  1 
ATOM   1341 N N   . VAL A 1 202 ? 37.019  48.677  -11.971 1.00 59.36  ? 297  VAL A N   1 
ATOM   1342 C CA  . VAL A 1 202 ? 35.654  49.184  -12.024 1.00 56.71  ? 297  VAL A CA  1 
ATOM   1343 C C   . VAL A 1 202 ? 35.659  50.525  -11.303 1.00 52.50  ? 297  VAL A C   1 
ATOM   1344 O O   . VAL A 1 202 ? 35.975  50.588  -10.107 1.00 52.85  ? 297  VAL A O   1 
ATOM   1345 C CB  . VAL A 1 202 ? 34.662  48.202  -11.387 1.00 55.56  ? 297  VAL A CB  1 
ATOM   1346 C CG1 . VAL A 1 202 ? 33.232  48.565  -11.755 1.00 51.74  ? 297  VAL A CG1 1 
ATOM   1347 C CG2 . VAL A 1 202 ? 35.004  46.778  -11.817 1.00 54.07  ? 297  VAL A CG2 1 
ATOM   1348 N N   . ASN A 1 203 ? 35.336  51.595  -12.031 1.00 49.47  ? 298  ASN A N   1 
ATOM   1349 C CA  . ASN A 1 203 ? 35.527  52.928  -11.484 1.00 51.56  ? 298  ASN A CA  1 
ATOM   1350 C C   . ASN A 1 203 ? 34.319  53.348  -10.652 1.00 50.97  ? 298  ASN A C   1 
ATOM   1351 O O   . ASN A 1 203 ? 33.251  52.724  -10.679 1.00 47.61  ? 298  ASN A O   1 
ATOM   1352 C CB  . ASN A 1 203 ? 35.832  53.944  -12.592 1.00 52.42  ? 298  ASN A CB  1 
ATOM   1353 C CG  . ASN A 1 203 ? 34.717  54.080  -13.617 1.00 57.69  ? 298  ASN A CG  1 
ATOM   1354 O OD1 . ASN A 1 203 ? 33.526  54.064  -13.286 1.00 59.04  ? 298  ASN A OD1 1 
ATOM   1355 N ND2 . ASN A 1 203 ? 35.107  54.242  -14.883 1.00 63.33  ? 298  ASN A ND2 1 
ATOM   1356 N N   . GLN A 1 204 ? 34.522  54.417  -9.883  1.00 52.05  ? 299  GLN A N   1 
ATOM   1357 C CA  . GLN A 1 204 ? 33.528  54.833  -8.899  1.00 52.13  ? 299  GLN A CA  1 
ATOM   1358 C C   . GLN A 1 204 ? 32.187  55.130  -9.557  1.00 49.28  ? 299  GLN A C   1 
ATOM   1359 O O   . GLN A 1 204 ? 31.138  54.753  -9.035  1.00 51.05  ? 299  GLN A O   1 
ATOM   1360 C CB  . GLN A 1 204 ? 34.048  56.049  -8.130  1.00 50.24  ? 299  GLN A CB  1 
ATOM   1361 C CG  . GLN A 1 204 ? 33.007  56.803  -7.317  1.00 47.56  ? 299  GLN A CG  1 
ATOM   1362 C CD  . GLN A 1 204 ? 33.659  57.857  -6.440  1.00 50.77  ? 299  GLN A CD  1 
ATOM   1363 O OE1 . GLN A 1 204 ? 34.136  57.558  -5.339  1.00 48.85  ? 299  GLN A OE1 1 
ATOM   1364 N NE2 . GLN A 1 204 ? 33.719  59.089  -6.937  1.00 50.56  ? 299  GLN A NE2 1 
ATOM   1365 N N   . ASP A 1 205 ? 32.201  55.787  -10.713 1.00 48.79  ? 300  ASP A N   1 
ATOM   1366 C CA  . ASP A 1 205 ? 30.949  56.165  -11.360 1.00 51.79  ? 300  ASP A CA  1 
ATOM   1367 C C   . ASP A 1 205 ? 30.127  54.935  -11.729 1.00 49.74  ? 300  ASP A C   1 
ATOM   1368 O O   . ASP A 1 205 ? 28.919  54.884  -11.482 1.00 50.32  ? 300  ASP A O   1 
ATOM   1369 C CB  . ASP A 1 205 ? 31.249  57.007  -12.598 1.00 57.13  ? 300  ASP A CB  1 
ATOM   1370 C CG  . ASP A 1 205 ? 30.097  57.901  -12.979 1.00 68.14  ? 300  ASP A CG  1 
ATOM   1371 O OD1 . ASP A 1 205 ? 29.773  58.802  -12.173 1.00 71.95  ? 300  ASP A OD1 1 
ATOM   1372 O OD2 . ASP A 1 205 ? 29.516  57.718  -14.076 1.00 71.56  ? 300  ASP A OD2 1 
ATOM   1373 N N   . ASN A 1 206 ? 30.780  53.932  -12.316 1.00 51.12  ? 301  ASN A N   1 
ATOM   1374 C CA  . ASN A 1 206 ? 30.110  52.698  -12.714 1.00 50.65  ? 301  ASN A CA  1 
ATOM   1375 C C   . ASN A 1 206 ? 29.550  51.969  -11.498 1.00 48.97  ? 301  ASN A C   1 
ATOM   1376 O O   . ASN A 1 206 ? 28.400  51.502  -11.500 1.00 48.39  ? 301  ASN A O   1 
ATOM   1377 C CB  . ASN A 1 206 ? 31.124  51.826  -13.475 1.00 51.16  ? 301  ASN A CB  1 
ATOM   1378 C CG  . ASN A 1 206 ? 30.484  50.718  -14.281 1.00 57.08  ? 301  ASN A CG  1 
ATOM   1379 O OD1 . ASN A 1 206 ? 29.265  50.629  -14.370 1.00 61.54  ? 301  ASN A OD1 1 
ATOM   1380 N ND2 . ASN A 1 206 ? 31.317  49.873  -14.899 1.00 60.44  ? 301  ASN A ND2 1 
ATOM   1381 N N   . ARG A 1 207 ? 30.347  51.897  -10.431 1.00 48.46  ? 302  ARG A N   1 
ATOM   1382 C CA  . ARG A 1 207 ? 29.902  51.263  -9.195  1.00 47.50  ? 302  ARG A CA  1 
ATOM   1383 C C   . ARG A 1 207 ? 28.690  51.976  -8.610  1.00 48.46  ? 302  ARG A C   1 
ATOM   1384 O O   . ARG A 1 207 ? 27.698  51.335  -8.239  1.00 44.14  ? 302  ARG A O   1 
ATOM   1385 C CB  . ARG A 1 207 ? 31.053  51.242  -8.189  1.00 43.12  ? 302  ARG A CB  1 
ATOM   1386 C CG  . ARG A 1 207 ? 32.205  50.301  -8.568  1.00 46.86  ? 302  ARG A CG  1 
ATOM   1387 C CD  . ARG A 1 207 ? 33.314  50.373  -7.541  1.00 46.96  ? 302  ARG A CD  1 
ATOM   1388 N NE  . ARG A 1 207 ? 34.420  49.459  -7.814  1.00 48.11  ? 302  ARG A NE  1 
ATOM   1389 C CZ  . ARG A 1 207 ? 34.633  48.315  -7.178  1.00 48.78  ? 302  ARG A CZ  1 
ATOM   1390 N NH1 . ARG A 1 207 ? 33.782  47.854  -6.278  1.00 44.08  ? 302  ARG A NH1 1 
ATOM   1391 N NH2 . ARG A 1 207 ? 35.743  47.625  -7.438  1.00 50.87  ? 302  ARG A NH2 1 
ATOM   1392 N N   . LEU A 1 208 ? 28.768  53.286  -8.465  1.00 47.13  ? 303  LEU A N   1 
ATOM   1393 C CA  . LEU A 1 208 ? 27.676  54.023  -7.863  1.00 45.99  ? 303  LEU A CA  1 
ATOM   1394 C C   . LEU A 1 208 ? 26.439  54.002  -8.713  1.00 43.60  ? 303  LEU A C   1 
ATOM   1395 O O   . LEU A 1 208 ? 25.362  54.001  -8.210  1.00 44.84  ? 303  LEU A O   1 
ATOM   1396 C CB  . LEU A 1 208 ? 28.093  55.422  -7.485  1.00 44.24  ? 303  LEU A CB  1 
ATOM   1397 C CG  . LEU A 1 208 ? 29.202  55.480  -6.454  1.00 48.73  ? 303  LEU A CG  1 
ATOM   1398 C CD1 . LEU A 1 208 ? 29.553  56.903  -6.137  1.00 49.96  ? 303  LEU A CD1 1 
ATOM   1399 C CD2 . LEU A 1 208 ? 28.831  54.745  -5.197  1.00 41.41  ? 303  LEU A CD2 1 
ATOM   1400 N N   . ASN A 1 209 ? 26.613  53.983  -10.018 1.00 45.19  ? 304  ASN A N   1 
ATOM   1401 C CA  . ASN A 1 209 ? 25.504  53.886  -10.935 1.00 49.43  ? 304  ASN A CA  1 
ATOM   1402 C C   . ASN A 1 209 ? 24.791  52.531  -10.890 1.00 49.98  ? 304  ASN A C   1 
ATOM   1403 O O   . ASN A 1 209 ? 23.657  52.436  -11.259 1.00 54.50  ? 304  ASN A O   1 
ATOM   1404 C CB  . ASN A 1 209 ? 25.915  54.222  -12.355 1.00 47.11  ? 304  ASN A CB  1 
ATOM   1405 C CG  . ASN A 1 209 ? 26.119  55.695  -12.581 1.00 49.31  ? 304  ASN A CG  1 
ATOM   1406 O OD1 . ASN A 1 209 ? 25.716  56.525  -11.811 1.00 47.92  ? 304  ASN A OD1 1 
ATOM   1407 N ND2 . ASN A 1 209 ? 26.743  56.006  -13.667 1.00 49.10  ? 304  ASN A ND2 1 
ATOM   1408 N N   . ASN A 1 210 ? 25.498  51.481  -10.519 1.00 45.01  ? 305  ASN A N   1 
ATOM   1409 C CA  . ASN A 1 210 ? 24.958  50.137  -10.419 1.00 45.46  ? 305  ASN A CA  1 
ATOM   1410 C C   . ASN A 1 210 ? 25.140  49.633  -8.996  1.00 45.36  ? 305  ASN A C   1 
ATOM   1411 O O   . ASN A 1 210 ? 25.653  48.576  -8.761  1.00 42.30  ? 305  ASN A O   1 
ATOM   1412 C CB  . ASN A 1 210 ? 25.651  49.228  -11.417 1.00 47.05  ? 305  ASN A CB  1 
ATOM   1413 C CG  . ASN A 1 210 ? 25.498  49.707  -12.842 1.00 48.22  ? 305  ASN A CG  1 
ATOM   1414 O OD1 . ASN A 1 210 ? 24.513  49.456  -13.484 1.00 46.71  ? 305  ASN A OD1 1 
ATOM   1415 N ND2 . ASN A 1 210 ? 26.485  50.410  -13.323 1.00 48.20  ? 305  ASN A ND2 1 
ATOM   1416 N N   . ARG A 1 211 ? 24.903  50.529  -8.052  1.00 43.72  ? 306  ARG A N   1 
ATOM   1417 C CA  . ARG A 1 211 ? 25.098  50.285  -6.634  1.00 40.31  ? 306  ARG A CA  1 
ATOM   1418 C C   . ARG A 1 211 ? 24.593  48.969  -6.100  1.00 41.22  ? 306  ARG A C   1 
ATOM   1419 O O   . ARG A 1 211 ? 25.230  48.359  -5.298  1.00 40.18  ? 306  ARG A O   1 
ATOM   1420 C CB  . ARG A 1 211 ? 24.584  51.468  -5.820  1.00 38.86  ? 306  ARG A CB  1 
ATOM   1421 C CG  . ARG A 1 211 ? 25.005  51.524  -4.369  1.00 36.73  ? 306  ARG A CG  1 
ATOM   1422 C CD  . ARG A 1 211 ? 26.502  51.527  -4.170  1.00 39.90  ? 306  ARG A CD  1 
ATOM   1423 N NE  . ARG A 1 211 ? 26.894  52.176  -2.947  1.00 38.89  ? 306  ARG A NE  1 
ATOM   1424 C CZ  . ARG A 1 211 ? 28.086  52.099  -2.391  1.00 42.14  ? 306  ARG A CZ  1 
ATOM   1425 N NH1 . ARG A 1 211 ? 29.044  51.395  -2.931  1.00 40.85  ? 306  ARG A NH1 1 
ATOM   1426 N NH2 . ARG A 1 211 ? 28.324  52.740  -1.289  1.00 35.18  ? 306  ARG A NH2 1 
ATOM   1427 N N   . CYS A 1 212 ? 23.450  48.527  -6.556  1.00 41.98  ? 307  CYS A N   1 
ATOM   1428 C CA  . CYS A 1 212 ? 22.913  47.251  -6.073  1.00 39.65  ? 307  CYS A CA  1 
ATOM   1429 C C   . CYS A 1 212 ? 23.808  46.071  -6.441  1.00 42.49  ? 307  CYS A C   1 
ATOM   1430 O O   . CYS A 1 212 ? 23.786  45.039  -5.762  1.00 42.52  ? 307  CYS A O   1 
ATOM   1431 C CB  . CYS A 1 212 ? 21.508  47.001  -6.623  1.00 49.49  ? 307  CYS A CB  1 
ATOM   1432 S SG  . CYS A 1 212 ? 20.816  45.360  -6.125  1.00 58.91  ? 307  CYS A SG  1 
ATOM   1433 N N   . VAL A 1 213 ? 24.596  46.191  -7.506  1.00 40.52  ? 308  VAL A N   1 
ATOM   1434 C CA  . VAL A 1 213 ? 25.571  45.151  -7.812  1.00 42.61  ? 308  VAL A CA  1 
ATOM   1435 C C   . VAL A 1 213 ? 26.866  45.400  -7.046  1.00 42.52  ? 308  VAL A C   1 
ATOM   1436 O O   . VAL A 1 213 ? 27.434  44.484  -6.437  1.00 41.12  ? 308  VAL A O   1 
ATOM   1437 C CB  . VAL A 1 213 ? 25.805  45.097  -9.338  1.00 45.11  ? 308  VAL A CB  1 
ATOM   1438 C CG1 . VAL A 1 213 ? 26.953  44.139  -9.692  1.00 47.30  ? 308  VAL A CG1 1 
ATOM   1439 C CG2 . VAL A 1 213 ? 24.517  44.705  -10.042 1.00 42.78  ? 308  VAL A CG2 1 
ATOM   1440 N N   . ASP A 1 214 ? 27.325  46.655  -7.041  1.00 41.46  ? 309  ASP A N   1 
ATOM   1441 C CA  . ASP A 1 214 ? 28.545  47.023  -6.322  1.00 41.40  ? 309  ASP A CA  1 
ATOM   1442 C C   . ASP A 1 214 ? 28.505  46.576  -4.861  1.00 41.91  ? 309  ASP A C   1 
ATOM   1443 O O   . ASP A 1 214 ? 29.522  46.130  -4.314  1.00 36.57  ? 309  ASP A O   1 
ATOM   1444 C CB  . ASP A 1 214 ? 28.758  48.539  -6.413  1.00 40.98  ? 309  ASP A CB  1 
ATOM   1445 C CG  . ASP A 1 214 ? 30.044  48.997  -5.749  1.00 42.87  ? 309  ASP A CG  1 
ATOM   1446 O OD1 . ASP A 1 214 ? 31.092  48.343  -5.931  1.00 43.24  ? 309  ASP A OD1 1 
ATOM   1447 O OD2 . ASP A 1 214 ? 30.016  50.037  -5.055  1.00 45.16  ? 309  ASP A OD2 1 
ATOM   1448 N N   . LEU A 1 215 ? 27.332  46.668  -4.214  1.00 39.13  ? 310  LEU A N   1 
ATOM   1449 C CA  . LEU A 1 215 ? 27.222  46.330  -2.796  1.00 39.16  ? 310  LEU A CA  1 
ATOM   1450 C C   . LEU A 1 215 ? 27.419  44.849  -2.521  1.00 39.45  ? 310  LEU A C   1 
ATOM   1451 O O   . LEU A 1 215 ? 27.504  44.454  -1.348  1.00 39.94  ? 310  LEU A O   1 
ATOM   1452 C CB  . LEU A 1 215 ? 25.858  46.775  -2.232  1.00 38.98  ? 310  LEU A CB  1 
ATOM   1453 C CG  . LEU A 1 215 ? 25.720  48.289  -2.009  1.00 39.60  ? 310  LEU A CG  1 
ATOM   1454 C CD1 . LEU A 1 215 ? 24.287  48.681  -1.592  1.00 39.28  ? 310  LEU A CD1 1 
ATOM   1455 C CD2 . LEU A 1 215 ? 26.740  48.767  -0.976  1.00 37.83  ? 310  LEU A CD2 1 
ATOM   1456 N N   . ARG A 1 216 ? 27.482  44.022  -3.554  1.00 41.51  ? 311  ARG A N   1 
ATOM   1457 C CA  . ARG A 1 216 ? 27.682  42.598  -3.325  1.00 41.82  ? 311  ARG A CA  1 
ATOM   1458 C C   . ARG A 1 216 ? 29.143  42.208  -3.149  1.00 42.51  ? 311  ARG A C   1 
ATOM   1459 O O   . ARG A 1 216 ? 29.396  41.067  -2.755  1.00 44.52  ? 311  ARG A O   1 
ATOM   1460 C CB  . ARG A 1 216 ? 27.064  41.801  -4.470  1.00 42.54  ? 311  ARG A CB  1 
ATOM   1461 C CG  . ARG A 1 216 ? 25.622  42.196  -4.730  1.00 41.06  ? 311  ARG A CG  1 
ATOM   1462 C CD  . ARG A 1 216 ? 25.020  41.443  -5.885  1.00 38.10  ? 311  ARG A CD  1 
ATOM   1463 N NE  . ARG A 1 216 ? 23.770  42.077  -6.277  1.00 38.97  ? 311  ARG A NE  1 
ATOM   1464 C CZ  . ARG A 1 216 ? 22.895  41.555  -7.123  1.00 42.35  ? 311  ARG A CZ  1 
ATOM   1465 N NH1 . ARG A 1 216 ? 23.081  40.352  -7.660  1.00 40.85  ? 311  ARG A NH1 1 
ATOM   1466 N NH2 . ARG A 1 216 ? 21.801  42.252  -7.434  1.00 40.04  ? 311  ARG A NH2 1 
ATOM   1467 N N   . THR A 1 217 ? 30.108  43.096  -3.421  1.00 38.78  ? 312  THR A N   1 
ATOM   1468 C CA  . THR A 1 217 ? 31.495  42.749  -3.123  1.00 42.43  ? 312  THR A CA  1 
ATOM   1469 C C   . THR A 1 217 ? 31.666  42.452  -1.634  1.00 40.36  ? 312  THR A C   1 
ATOM   1470 O O   . THR A 1 217 ? 30.966  42.997  -0.776  1.00 39.01  ? 312  THR A O   1 
ATOM   1471 C CB  . THR A 1 217 ? 32.480  43.859  -3.542  1.00 40.95  ? 312  THR A CB  1 
ATOM   1472 O OG1 . THR A 1 217 ? 32.317  45.012  -2.702  1.00 41.32  ? 312  THR A OG1 1 
ATOM   1473 C CG2 . THR A 1 217 ? 32.307  44.247  -5.003  1.00 41.59  ? 312  THR A CG2 1 
ATOM   1474 N N   . TYR A 1 218 ? 32.619  41.575  -1.324  1.00 41.19  ? 313  TYR A N   1 
ATOM   1475 C CA  . TYR A 1 218 ? 32.826  41.193  0.069   1.00 42.54  ? 313  TYR A CA  1 
ATOM   1476 C C   . TYR A 1 218 ? 33.205  42.401  0.926   1.00 43.16  ? 313  TYR A C   1 
ATOM   1477 O O   . TYR A 1 218 ? 32.727  42.551  2.065   1.00 39.85  ? 313  TYR A O   1 
ATOM   1478 C CB  . TYR A 1 218 ? 33.891  40.109  0.139   1.00 41.95  ? 313  TYR A CB  1 
ATOM   1479 C CG  . TYR A 1 218 ? 33.502  38.820  -0.576  1.00 47.82  ? 313  TYR A CG  1 
ATOM   1480 C CD1 . TYR A 1 218 ? 32.390  38.098  -0.167  1.00 46.03  ? 313  TYR A CD1 1 
ATOM   1481 C CD2 . TYR A 1 218 ? 34.263  38.313  -1.639  1.00 45.22  ? 313  TYR A CD2 1 
ATOM   1482 C CE1 . TYR A 1 218 ? 32.032  36.915  -0.785  1.00 46.99  ? 313  TYR A CE1 1 
ATOM   1483 C CE2 . TYR A 1 218 ? 33.908  37.119  -2.277  1.00 44.06  ? 313  TYR A CE2 1 
ATOM   1484 C CZ  . TYR A 1 218 ? 32.792  36.429  -1.834  1.00 49.32  ? 313  TYR A CZ  1 
ATOM   1485 O OH  . TYR A 1 218 ? 32.401  35.251  -2.426  1.00 50.81  ? 313  TYR A OH  1 
ATOM   1486 N N   . ALA A 1 219 ? 34.046  43.289  0.385   1.00 39.62  ? 314  ALA A N   1 
ATOM   1487 C CA  . ALA A 1 219 ? 34.444  44.469  1.144   1.00 43.70  ? 314  ALA A CA  1 
ATOM   1488 C C   . ALA A 1 219 ? 33.257  45.391  1.400   1.00 39.79  ? 314  ALA A C   1 
ATOM   1489 O O   . ALA A 1 219 ? 33.127  45.934  2.497   1.00 41.07  ? 314  ALA A O   1 
ATOM   1490 C CB  . ALA A 1 219 ? 35.567  45.233  0.426   1.00 40.58  ? 314  ALA A CB  1 
ATOM   1491 N N   . ASN A 1 220 ? 32.392  45.604  0.400   1.00 38.24  ? 315  ASN A N   1 
ATOM   1492 C CA  . ASN A 1 220 ? 31.302  46.561  0.607   1.00 42.44  ? 315  ASN A CA  1 
ATOM   1493 C C   . ASN A 1 220 ? 30.279  46.026  1.604   1.00 38.86  ? 315  ASN A C   1 
ATOM   1494 O O   . ASN A 1 220 ? 29.818  46.767  2.488   1.00 41.18  ? 315  ASN A O   1 
ATOM   1495 C CB  . ASN A 1 220 ? 30.623  46.912  -0.721  1.00 36.01  ? 315  ASN A CB  1 
ATOM   1496 C CG  . ASN A 1 220 ? 31.470  47.851  -1.588  1.00 42.35  ? 315  ASN A CG  1 
ATOM   1497 O OD1 . ASN A 1 220 ? 32.314  48.595  -1.082  1.00 41.29  ? 315  ASN A OD1 1 
ATOM   1498 N ND2 . ASN A 1 220 ? 31.240  47.819  -2.899  1.00 38.46  ? 315  ASN A ND2 1 
ATOM   1499 N N   . TYR A 1 221 ? 29.902  44.743  1.467   1.00 39.08  ? 316  TYR A N   1 
ATOM   1500 C CA  . TYR A 1 221 ? 29.047  44.120  2.472   1.00 40.20  ? 316  TYR A CA  1 
ATOM   1501 C C   . TYR A 1 221 ? 29.635  44.322  3.866   1.00 41.31  ? 316  TYR A C   1 
ATOM   1502 O O   . TYR A 1 221 ? 28.919  44.688  4.810   1.00 37.26  ? 316  TYR A O   1 
ATOM   1503 C CB  . TYR A 1 221 ? 28.859  42.617  2.176   1.00 39.44  ? 316  TYR A CB  1 
ATOM   1504 C CG  . TYR A 1 221 ? 28.082  41.949  3.290   1.00 40.72  ? 316  TYR A CG  1 
ATOM   1505 C CD1 . TYR A 1 221 ? 26.705  42.076  3.356   1.00 41.87  ? 316  TYR A CD1 1 
ATOM   1506 C CD2 . TYR A 1 221 ? 28.724  41.257  4.306   1.00 38.74  ? 316  TYR A CD2 1 
ATOM   1507 C CE1 . TYR A 1 221 ? 25.980  41.522  4.398   1.00 45.17  ? 316  TYR A CE1 1 
ATOM   1508 C CE2 . TYR A 1 221 ? 28.004  40.684  5.349   1.00 43.88  ? 316  TYR A CE2 1 
ATOM   1509 C CZ  . TYR A 1 221 ? 26.624  40.823  5.381   1.00 41.80  ? 316  TYR A CZ  1 
ATOM   1510 O OH  . TYR A 1 221 ? 25.875  40.285  6.401   1.00 44.93  ? 316  TYR A OH  1 
ATOM   1511 N N   . SER A 1 222 ? 30.953  44.109  4.002   1.00 40.50  ? 317  SER A N   1 
ATOM   1512 C CA  . SER A 1 222 ? 31.589  44.238  5.311   1.00 39.02  ? 317  SER A CA  1 
ATOM   1513 C C   . SER A 1 222 ? 31.583  45.681  5.812   1.00 37.83  ? 317  SER A C   1 
ATOM   1514 O O   . SER A 1 222 ? 31.395  45.922  7.010   1.00 41.68  ? 317  SER A O   1 
ATOM   1515 C CB  . SER A 1 222 ? 33.019  43.712  5.240   1.00 39.78  ? 317  SER A CB  1 
ATOM   1516 O OG  . SER A 1 222 ? 33.036  42.348  4.879   1.00 42.55  ? 317  SER A OG  1 
ATOM   1517 N N   . ILE A 1 223 ? 31.829  46.649  4.920   1.00 36.64  ? 318  ILE A N   1 
ATOM   1518 C CA  . ILE A 1 223 ? 31.784  48.058  5.314   1.00 38.88  ? 318  ILE A CA  1 
ATOM   1519 C C   . ILE A 1 223 ? 30.438  48.393  5.942   1.00 39.73  ? 318  ILE A C   1 
ATOM   1520 O O   . ILE A 1 223 ? 30.369  49.040  6.996   1.00 39.48  ? 318  ILE A O   1 
ATOM   1521 C CB  . ILE A 1 223 ? 32.070  48.971  4.107   1.00 39.96  ? 318  ILE A CB  1 
ATOM   1522 C CG1 . ILE A 1 223 ? 33.547  48.913  3.720   1.00 35.59  ? 318  ILE A CG1 1 
ATOM   1523 C CG2 . ILE A 1 223 ? 31.640  50.434  4.409   1.00 35.87  ? 318  ILE A CG2 1 
ATOM   1524 C CD1 . ILE A 1 223 ? 33.854  49.586  2.386   1.00 38.75  ? 318  ILE A CD1 1 
ATOM   1525 N N   . PHE A 1 224 ? 29.339  47.960  5.311   1.00 35.60  ? 319  PHE A N   1 
ATOM   1526 C CA  . PHE A 1 224 ? 28.057  48.424  5.844   1.00 38.87  ? 319  PHE A CA  1 
ATOM   1527 C C   . PHE A 1 224 ? 27.581  47.636  7.066   1.00 40.12  ? 319  PHE A C   1 
ATOM   1528 O O   . PHE A 1 224 ? 26.860  48.206  7.912   1.00 35.87  ? 319  PHE A O   1 
ATOM   1529 C CB  . PHE A 1 224 ? 27.035  48.494  4.708   1.00 34.57  ? 319  PHE A CB  1 
ATOM   1530 C CG  . PHE A 1 224 ? 27.332  49.639  3.800   1.00 37.90  ? 319  PHE A CG  1 
ATOM   1531 C CD1 . PHE A 1 224 ? 27.078  50.946  4.222   1.00 37.38  ? 319  PHE A CD1 1 
ATOM   1532 C CD2 . PHE A 1 224 ? 28.005  49.441  2.607   1.00 34.49  ? 319  PHE A CD2 1 
ATOM   1533 C CE1 . PHE A 1 224 ? 27.440  52.034  3.418   1.00 37.62  ? 319  PHE A CE1 1 
ATOM   1534 C CE2 . PHE A 1 224 ? 28.351  50.516  1.792   1.00 38.20  ? 319  PHE A CE2 1 
ATOM   1535 C CZ  . PHE A 1 224 ? 28.075  51.812  2.195   1.00 36.61  ? 319  PHE A CZ  1 
ATOM   1536 N N   . CYS A 1 225 ? 28.046  46.389  7.240   1.00 37.89  ? 320  CYS A N   1 
ATOM   1537 C CA  . CYS A 1 225 ? 27.919  45.760  8.556   1.00 37.50  ? 320  CYS A CA  1 
ATOM   1538 C C   . CYS A 1 225 ? 28.691  46.525  9.628   1.00 39.79  ? 320  CYS A C   1 
ATOM   1539 O O   . CYS A 1 225 ? 28.217  46.657  10.765  1.00 39.80  ? 320  CYS A O   1 
ATOM   1540 C CB  . CYS A 1 225 ? 28.404  44.310  8.513   1.00 41.76  ? 320  CYS A CB  1 
ATOM   1541 S SG  . CYS A 1 225 ? 27.369  43.264  7.491   1.00 45.43  ? 320  CYS A SG  1 
ATOM   1542 N N   . LEU A 1 226 ? 29.894  47.014  9.302   1.00 40.01  ? 321  LEU A N   1 
ATOM   1543 C CA  . LEU A 1 226 ? 30.656  47.783  10.287  1.00 39.38  ? 321  LEU A CA  1 
ATOM   1544 C C   . LEU A 1 226 ? 29.986  49.109  10.600  1.00 38.72  ? 321  LEU A C   1 
ATOM   1545 O O   . LEU A 1 226 ? 30.089  49.609  11.729  1.00 37.84  ? 321  LEU A O   1 
ATOM   1546 C CB  . LEU A 1 226 ? 32.086  48.022  9.790   1.00 40.47  ? 321  LEU A CB  1 
ATOM   1547 C CG  . LEU A 1 226 ? 32.962  46.766  9.804   1.00 40.00  ? 321  LEU A CG  1 
ATOM   1548 C CD1 . LEU A 1 226 ? 34.250  46.995  9.029   1.00 39.86  ? 321  LEU A CD1 1 
ATOM   1549 C CD2 . LEU A 1 226 ? 33.257  46.382  11.239  1.00 39.31  ? 321  LEU A CD2 1 
ATOM   1550 N N   . GLN A 1 227 ? 29.305  49.692  9.613   1.00 37.84  ? 322  GLN A N   1 
ATOM   1551 C CA  . GLN A 1 227 ? 28.558  50.916  9.861   1.00 39.91  ? 322  GLN A CA  1 
ATOM   1552 C C   . GLN A 1 227 ? 27.445  50.668  10.861  1.00 40.01  ? 322  GLN A C   1 
ATOM   1553 O O   . GLN A 1 227 ? 27.266  51.436  11.824  1.00 40.22  ? 322  GLN A O   1 
ATOM   1554 C CB  . GLN A 1 227 ? 27.978  51.471  8.563   1.00 39.04  ? 322  GLN A CB  1 
ATOM   1555 C CG  . GLN A 1 227 ? 27.683  52.957  8.661   1.00 37.94  ? 322  GLN A CG  1 
ATOM   1556 C CD  . GLN A 1 227 ? 26.553  53.399  7.754   1.00 40.65  ? 322  GLN A CD  1 
ATOM   1557 O OE1 . GLN A 1 227 ? 25.372  53.142  8.030   1.00 39.90  ? 322  GLN A OE1 1 
ATOM   1558 N NE2 . GLN A 1 227 ? 26.905  54.077  6.669   1.00 34.57  ? 322  GLN A NE2 1 
ATOM   1559 N N   . SER A 1 228 ? 26.674  49.599  10.634  1.00 40.19  ? 323  SER A N   1 
ATOM   1560 C CA  . SER A 1 228 ? 25.662  49.204  11.614  1.00 39.85  ? 323  SER A CA  1 
ATOM   1561 C C   . SER A 1 228 ? 26.288  48.989  12.986  1.00 41.92  ? 323  SER A C   1 
ATOM   1562 O O   . SER A 1 228 ? 25.732  49.411  14.008  1.00 41.74  ? 323  SER A O   1 
ATOM   1563 C CB  . SER A 1 228 ? 24.942  47.938  11.147  1.00 36.51  ? 323  SER A CB  1 
ATOM   1564 O OG  . SER A 1 228 ? 24.005  47.505  12.116  1.00 36.34  ? 323  SER A OG  1 
ATOM   1565 N N   . GLN A 1 229 ? 27.460  48.354  13.024  1.00 41.19  ? 324  GLN A N   1 
ATOM   1566 C CA  . GLN A 1 229 ? 28.134  48.101  14.295  1.00 41.51  ? 324  GLN A CA  1 
ATOM   1567 C C   . GLN A 1 229 ? 28.488  49.401  15.033  1.00 43.72  ? 324  GLN A C   1 
ATOM   1568 O O   . GLN A 1 229 ? 28.345  49.490  16.261  1.00 39.79  ? 324  GLN A O   1 
ATOM   1569 C CB  . GLN A 1 229 ? 29.384  47.263  14.019  1.00 46.11  ? 324  GLN A CB  1 
ATOM   1570 C CG  . GLN A 1 229 ? 30.014  46.684  15.232  1.00 54.29  ? 324  GLN A CG  1 
ATOM   1571 C CD  . GLN A 1 229 ? 29.261  45.490  15.757  1.00 56.77  ? 324  GLN A CD  1 
ATOM   1572 O OE1 . GLN A 1 229 ? 28.381  44.935  15.078  1.00 55.22  ? 324  GLN A OE1 1 
ATOM   1573 N NE2 . GLN A 1 229 ? 29.593  45.091  16.983  1.00 55.50  ? 324  GLN A NE2 1 
ATOM   1574 N N   . ILE A 1 230 ? 28.965  50.420  14.307  1.00 40.26  ? 325  ILE A N   1 
ATOM   1575 C CA  . ILE A 1 230 ? 29.263  51.694  14.969  1.00 41.88  ? 325  ILE A CA  1 
ATOM   1576 C C   . ILE A 1 230 ? 27.994  52.309  15.556  1.00 44.74  ? 325  ILE A C   1 
ATOM   1577 O O   . ILE A 1 230 ? 27.993  52.805  16.697  1.00 41.84  ? 325  ILE A O   1 
ATOM   1578 C CB  . ILE A 1 230 ? 29.961  52.678  14.015  1.00 40.95  ? 325  ILE A CB  1 
ATOM   1579 C CG1 . ILE A 1 230 ? 31.387  52.210  13.715  1.00 43.40  ? 325  ILE A CG1 1 
ATOM   1580 C CG2 . ILE A 1 230 ? 29.975  54.088  14.644  1.00 40.75  ? 325  ILE A CG2 1 
ATOM   1581 C CD1 . ILE A 1 230 ? 32.096  53.013  12.619  1.00 43.64  ? 325  ILE A CD1 1 
ATOM   1582 N N   . CYS A 1 231 ? 26.894  52.298  14.788  1.00 42.85  ? 326  CYS A N   1 
ATOM   1583 C CA  . CYS A 1 231 ? 25.634  52.809  15.340  1.00 46.32  ? 326  CYS A CA  1 
ATOM   1584 C C   . CYS A 1 231 ? 25.260  52.085  16.629  1.00 44.44  ? 326  CYS A C   1 
ATOM   1585 O O   . CYS A 1 231 ? 24.859  52.707  17.627  1.00 44.85  ? 326  CYS A O   1 
ATOM   1586 C CB  . CYS A 1 231 ? 24.501  52.661  14.329  1.00 45.56  ? 326  CYS A CB  1 
ATOM   1587 S SG  . CYS A 1 231 ? 24.587  53.823  13.002  1.00 49.79  ? 326  CYS A SG  1 
ATOM   1588 N N   . THR A 1 232 ? 25.365  50.759  16.613  1.00 43.20  ? 327  THR A N   1 
ATOM   1589 C CA  . THR A 1 232 ? 24.965  49.979  17.776  1.00 44.09  ? 327  THR A CA  1 
ATOM   1590 C C   . THR A 1 232 ? 25.821  50.314  18.986  1.00 41.63  ? 327  THR A C   1 
ATOM   1591 O O   . THR A 1 232 ? 25.299  50.506  20.089  1.00 43.06  ? 327  THR A O   1 
ATOM   1592 C CB  . THR A 1 232 ? 25.064  48.493  17.453  1.00 44.16  ? 327  THR A CB  1 
ATOM   1593 O OG1 . THR A 1 232 ? 24.102  48.187  16.443  1.00 46.31  ? 327  THR A OG1 1 
ATOM   1594 C CG2 . THR A 1 232 ? 24.818  47.627  18.708  1.00 42.58  ? 327  THR A CG2 1 
ATOM   1595 N N   . ILE A 1 233 ? 27.145  50.349  18.803  1.00 42.98  ? 328  ILE A N   1 
ATOM   1596 C CA  . ILE A 1 233 ? 28.047  50.608  19.923  1.00 44.08  ? 328  ILE A CA  1 
ATOM   1597 C C   . ILE A 1 233 ? 27.788  51.990  20.499  1.00 43.17  ? 328  ILE A C   1 
ATOM   1598 O O   . ILE A 1 233 ? 27.740  52.169  21.723  1.00 43.75  ? 328  ILE A O   1 
ATOM   1599 C CB  . ILE A 1 233 ? 29.516  50.441  19.482  1.00 45.14  ? 328  ILE A CB  1 
ATOM   1600 C CG1 . ILE A 1 233 ? 29.779  48.996  19.030  1.00 45.92  ? 328  ILE A CG1 1 
ATOM   1601 C CG2 . ILE A 1 233 ? 30.470  50.841  20.606  1.00 41.91  ? 328  ILE A CG2 1 
ATOM   1602 C CD1 . ILE A 1 233 ? 31.018  48.858  18.168  1.00 45.71  ? 328  ILE A CD1 1 
ATOM   1603 N N   . PHE A 1 234 ? 27.589  52.981  19.620  1.00 44.14  ? 329  PHE A N   1 
ATOM   1604 C CA  . PHE A 1 234 ? 27.324  54.356  20.037  1.00 44.70  ? 329  PHE A CA  1 
ATOM   1605 C C   . PHE A 1 234 ? 26.069  54.433  20.894  1.00 44.98  ? 329  PHE A C   1 
ATOM   1606 O O   . PHE A 1 234 ? 26.086  54.952  22.032  1.00 44.67  ? 329  PHE A O   1 
ATOM   1607 C CB  . PHE A 1 234 ? 27.194  55.219  18.773  1.00 43.67  ? 329  PHE A CB  1 
ATOM   1608 C CG  . PHE A 1 234 ? 26.736  56.641  19.011  1.00 43.01  ? 329  PHE A CG  1 
ATOM   1609 C CD1 . PHE A 1 234 ? 25.410  57.005  18.774  1.00 41.62  ? 329  PHE A CD1 1 
ATOM   1610 C CD2 . PHE A 1 234 ? 27.641  57.628  19.412  1.00 41.56  ? 329  PHE A CD2 1 
ATOM   1611 C CE1 . PHE A 1 234 ? 24.972  58.325  18.973  1.00 40.10  ? 329  PHE A CE1 1 
ATOM   1612 C CE2 . PHE A 1 234 ? 27.225  58.951  19.606  1.00 43.89  ? 329  PHE A CE2 1 
ATOM   1613 C CZ  . PHE A 1 234 ? 25.889  59.304  19.383  1.00 41.55  ? 329  PHE A CZ  1 
ATOM   1614 N N   . LYS A 1 235 ? 24.976  53.869  20.382  1.00 43.76  ? 330  LYS A N   1 
ATOM   1615 C CA  . LYS A 1 235 ? 23.723  53.947  21.115  1.00 42.72  ? 330  LYS A CA  1 
ATOM   1616 C C   . LYS A 1 235 ? 23.802  53.189  22.429  1.00 45.84  ? 330  LYS A C   1 
ATOM   1617 O O   . LYS A 1 235 ? 23.331  53.686  23.457  1.00 44.32  ? 330  LYS A O   1 
ATOM   1618 C CB  . LYS A 1 235 ? 22.575  53.447  20.239  1.00 45.70  ? 330  LYS A CB  1 
ATOM   1619 C CG  . LYS A 1 235 ? 22.289  54.442  19.096  1.00 50.14  ? 330  LYS A CG  1 
ATOM   1620 C CD  . LYS A 1 235 ? 21.128  54.006  18.200  1.00 54.44  ? 330  LYS A CD  1 
ATOM   1621 C CE  . LYS A 1 235 ? 21.606  53.038  17.112  1.00 49.67  ? 330  LYS A CE  1 
ATOM   1622 N NZ  . LYS A 1 235 ? 20.558  52.836  16.091  1.00 55.44  ? 330  LYS A NZ  1 
ATOM   1623 N N   . ASN A 1 236 ? 24.408  51.998  22.431  1.00 42.04  ? 331  ASN A N   1 
ATOM   1624 C CA  . ASN A 1 236 ? 24.408  51.207  23.661  1.00 44.85  ? 331  ASN A CA  1 
ATOM   1625 C C   . ASN A 1 236 ? 25.297  51.829  24.725  1.00 43.94  ? 331  ASN A C   1 
ATOM   1626 O O   . ASN A 1 236 ? 24.970  51.785  25.917  1.00 44.01  ? 331  ASN A O   1 
ATOM   1627 C CB  . ASN A 1 236 ? 24.827  49.759  23.381  1.00 44.85  ? 331  ASN A CB  1 
ATOM   1628 C CG  . ASN A 1 236 ? 23.731  48.966  22.669  1.00 47.96  ? 331  ASN A CG  1 
ATOM   1629 O OD1 . ASN A 1 236 ? 22.578  49.383  22.626  1.00 47.88  ? 331  ASN A OD1 1 
ATOM   1630 N ND2 . ASN A 1 236 ? 24.090  47.811  22.126  1.00 49.71  ? 331  ASN A ND2 1 
ATOM   1631 N N   . PHE A 1 237 ? 26.422  52.422  24.325  1.00 45.30  ? 332  PHE A N   1 
ATOM   1632 C CA  . PHE A 1 237 ? 27.241  53.121  25.305  1.00 43.98  ? 332  PHE A CA  1 
ATOM   1633 C C   . PHE A 1 237 ? 26.459  54.263  25.939  1.00 44.24  ? 332  PHE A C   1 
ATOM   1634 O O   . PHE A 1 237 ? 26.471  54.432  27.167  1.00 44.94  ? 332  PHE A O   1 
ATOM   1635 C CB  . PHE A 1 237 ? 28.520  53.635  24.643  1.00 44.71  ? 332  PHE A CB  1 
ATOM   1636 C CG  . PHE A 1 237 ? 29.440  54.363  25.572  1.00 43.82  ? 332  PHE A CG  1 
ATOM   1637 C CD1 . PHE A 1 237 ? 30.414  53.678  26.288  1.00 49.20  ? 332  PHE A CD1 1 
ATOM   1638 C CD2 . PHE A 1 237 ? 29.346  55.737  25.718  1.00 45.68  ? 332  PHE A CD2 1 
ATOM   1639 C CE1 . PHE A 1 237 ? 31.287  54.361  27.157  1.00 49.49  ? 332  PHE A CE1 1 
ATOM   1640 C CE2 . PHE A 1 237 ? 30.216  56.424  26.565  1.00 45.53  ? 332  PHE A CE2 1 
ATOM   1641 C CZ  . PHE A 1 237 ? 31.187  55.734  27.286  1.00 50.05  ? 332  PHE A CZ  1 
ATOM   1642 N N   . LEU A 1 238 ? 25.761  55.058  25.118  1.00 42.99  ? 333  LEU A N   1 
ATOM   1643 C CA  . LEU A 1 238 ? 25.020  56.182  25.691  1.00 43.98  ? 333  LEU A CA  1 
ATOM   1644 C C   . LEU A 1 238 ? 23.850  55.706  26.554  1.00 45.42  ? 333  LEU A C   1 
ATOM   1645 O O   . LEU A 1 238 ? 23.633  56.231  27.653  1.00 45.12  ? 333  LEU A O   1 
ATOM   1646 C CB  . LEU A 1 238 ? 24.546  57.116  24.582  1.00 43.15  ? 333  LEU A CB  1 
ATOM   1647 C CG  . LEU A 1 238 ? 25.731  57.769  23.865  1.00 45.14  ? 333  LEU A CG  1 
ATOM   1648 C CD1 . LEU A 1 238 ? 25.260  58.574  22.683  1.00 41.68  ? 333  LEU A CD1 1 
ATOM   1649 C CD2 . LEU A 1 238 ? 26.549  58.651  24.830  1.00 44.02  ? 333  LEU A CD2 1 
ATOM   1650 N N   . LEU A 1 239 ? 23.105  54.698  26.090  1.00 43.93  ? 334  LEU A N   1 
ATOM   1651 C CA  . LEU A 1 239 ? 21.992  54.157  26.872  1.00 46.82  ? 334  LEU A CA  1 
ATOM   1652 C C   . LEU A 1 239 ? 22.468  53.610  28.205  1.00 47.17  ? 334  LEU A C   1 
ATOM   1653 O O   . LEU A 1 239 ? 21.824  53.815  29.241  1.00 47.65  ? 334  LEU A O   1 
ATOM   1654 C CB  . LEU A 1 239 ? 21.277  53.059  26.080  1.00 46.46  ? 334  LEU A CB  1 
ATOM   1655 C CG  . LEU A 1 239 ? 20.512  53.517  24.838  1.00 47.08  ? 334  LEU A CG  1 
ATOM   1656 C CD1 . LEU A 1 239 ? 20.135  52.326  23.949  1.00 44.13  ? 334  LEU A CD1 1 
ATOM   1657 C CD2 . LEU A 1 239 ? 19.273  54.323  25.241  1.00 41.78  ? 334  LEU A CD2 1 
ATOM   1658 N N   . GLU A 1 240 ? 23.597  52.909  28.198  1.00 46.83  ? 335  GLU A N   1 
ATOM   1659 C CA  . GLU A 1 240 ? 24.155  52.378  29.429  1.00 48.52  ? 335  GLU A CA  1 
ATOM   1660 C C   . GLU A 1 240 ? 24.594  53.494  30.364  1.00 48.68  ? 335  GLU A C   1 
ATOM   1661 O O   . GLU A 1 240 ? 24.735  53.270  31.566  1.00 47.67  ? 335  GLU A O   1 
ATOM   1662 C CB  . GLU A 1 240 ? 25.312  51.436  29.075  1.00 50.76  ? 335  GLU A CB  1 
ATOM   1663 C CG  . GLU A 1 240 ? 26.218  51.043  30.224  1.00 65.11  ? 335  GLU A CG  1 
ATOM   1664 C CD  . GLU A 1 240 ? 25.866  49.682  30.824  1.00 78.52  ? 335  GLU A CD  1 
ATOM   1665 O OE1 . GLU A 1 240 ? 26.777  49.035  31.398  1.00 80.98  ? 335  GLU A OE1 1 
ATOM   1666 O OE2 . GLU A 1 240 ? 24.687  49.259  30.713  1.00 78.79  ? 335  GLU A OE2 1 
ATOM   1667 N N   . ASN A 1 241 ? 24.792  54.703  29.843  1.00 47.52  ? 336  ASN A N   1 
ATOM   1668 C CA  . ASN A 1 241 ? 25.108  55.852  30.680  1.00 48.76  ? 336  ASN A CA  1 
ATOM   1669 C C   . ASN A 1 241 ? 23.906  56.763  30.891  1.00 47.35  ? 336  ASN A C   1 
ATOM   1670 O O   . ASN A 1 241 ? 24.088  57.965  31.132  1.00 46.33  ? 336  ASN A O   1 
ATOM   1671 C CB  . ASN A 1 241 ? 26.276  56.645  30.087  1.00 45.20  ? 336  ASN A CB  1 
ATOM   1672 C CG  . ASN A 1 241 ? 27.598  55.977  30.339  1.00 48.71  ? 336  ASN A CG  1 
ATOM   1673 O OD1 . ASN A 1 241 ? 28.185  56.141  31.408  1.00 49.81  ? 336  ASN A OD1 1 
ATOM   1674 N ND2 . ASN A 1 241 ? 28.077  55.209  29.361  1.00 49.09  ? 336  ASN A ND2 1 
ATOM   1675 N N   . ASN A 1 242 ? 22.687  56.222  30.770  1.00 44.54  ? 337  ASN A N   1 
ATOM   1676 C CA  . ASN A 1 242 ? 21.449  56.887  31.166  1.00 49.22  ? 337  ASN A CA  1 
ATOM   1677 C C   . ASN A 1 242 ? 21.018  57.983  30.195  1.00 49.32  ? 337  ASN A C   1 
ATOM   1678 O O   . ASN A 1 242 ? 20.302  58.905  30.591  1.00 47.90  ? 337  ASN A O   1 
ATOM   1679 C CB  . ASN A 1 242 ? 21.551  57.464  32.585  1.00 47.97  ? 337  ASN A CB  1 
ATOM   1680 C CG  . ASN A 1 242 ? 20.182  57.629  33.249  1.00 55.81  ? 337  ASN A CG  1 
ATOM   1681 O OD1 . ASN A 1 242 ? 19.238  56.867  32.977  1.00 54.88  ? 337  ASN A OD1 1 
ATOM   1682 N ND2 . ASN A 1 242 ? 20.068  58.631  34.117  1.00 54.47  ? 337  ASN A ND2 1 
ATOM   1683 N N   . PHE A 1 243 ? 21.450  57.919  28.938  1.00 44.79  ? 338  PHE A N   1 
ATOM   1684 C CA  . PHE A 1 243 ? 20.926  58.806  27.903  1.00 45.47  ? 338  PHE A CA  1 
ATOM   1685 C C   . PHE A 1 243 ? 19.572  58.311  27.396  1.00 45.33  ? 338  PHE A C   1 
ATOM   1686 O O   . PHE A 1 243 ? 19.275  57.112  27.422  1.00 41.03  ? 338  PHE A O   1 
ATOM   1687 C CB  . PHE A 1 243 ? 21.887  58.878  26.713  1.00 42.61  ? 338  PHE A CB  1 
ATOM   1688 C CG  . PHE A 1 243 ? 23.063  59.779  26.928  1.00 43.59  ? 338  PHE A CG  1 
ATOM   1689 C CD1 . PHE A 1 243 ? 24.055  59.448  27.837  1.00 41.84  ? 338  PHE A CD1 1 
ATOM   1690 C CD2 . PHE A 1 243 ? 23.182  60.956  26.203  1.00 43.22  ? 338  PHE A CD2 1 
ATOM   1691 C CE1 . PHE A 1 243 ? 25.150  60.273  28.022  1.00 44.67  ? 338  PHE A CE1 1 
ATOM   1692 C CE2 . PHE A 1 243 ? 24.258  61.791  26.395  1.00 43.83  ? 338  PHE A CE2 1 
ATOM   1693 C CZ  . PHE A 1 243 ? 25.254  61.448  27.302  1.00 43.84  ? 338  PHE A CZ  1 
ATOM   1694 N N   . ILE A 1 244 ? 18.765  59.236  26.881  1.00 43.18  ? 339  ILE A N   1 
ATOM   1695 C CA  . ILE A 1 244 ? 17.595  58.843  26.100  1.00 43.58  ? 339  ILE A CA  1 
ATOM   1696 C C   . ILE A 1 244 ? 17.773  59.293  24.662  1.00 42.36  ? 339  ILE A C   1 
ATOM   1697 O O   . ILE A 1 244 ? 18.404  60.316  24.372  1.00 41.60  ? 339  ILE A O   1 
ATOM   1698 C CB  . ILE A 1 244 ? 16.261  59.381  26.664  1.00 45.77  ? 339  ILE A CB  1 
ATOM   1699 C CG1 . ILE A 1 244 ? 16.160  60.893  26.481  1.00 43.76  ? 339  ILE A CG1 1 
ATOM   1700 C CG2 . ILE A 1 244 ? 16.093  58.956  28.115  1.00 45.47  ? 339  ILE A CG2 1 
ATOM   1701 C CD1 . ILE A 1 244 ? 14.765  61.425  26.746  1.00 49.25  ? 339  ILE A CD1 1 
ATOM   1702 N N   . GLU A 1 245 ? 17.207  58.506  23.752  1.00 40.80  ? 340  GLU A N   1 
ATOM   1703 C CA  . GLU A 1 245 ? 17.208  58.857  22.345  1.00 40.24  ? 340  GLU A CA  1 
ATOM   1704 C C   . GLU A 1 245 ? 16.095  59.859  22.047  1.00 39.65  ? 340  GLU A C   1 
ATOM   1705 O O   . GLU A 1 245 ? 14.950  59.670  22.471  1.00 40.96  ? 340  GLU A O   1 
ATOM   1706 C CB  . GLU A 1 245 ? 17.030  57.595  21.509  1.00 39.94  ? 340  GLU A CB  1 
ATOM   1707 C CG  . GLU A 1 245 ? 16.806  57.858  20.035  1.00 43.25  ? 340  GLU A CG  1 
ATOM   1708 C CD  . GLU A 1 245 ? 17.266  56.688  19.181  1.00 48.13  ? 340  GLU A CD  1 
ATOM   1709 O OE1 . GLU A 1 245 ? 17.581  56.894  17.986  1.00 50.44  ? 340  GLU A OE1 1 
ATOM   1710 O OE2 . GLU A 1 245 ? 17.326  55.564  19.726  1.00 47.96  ? 340  GLU A OE2 1 
ATOM   1711 N N   . ILE A 1 246 ? 16.415  60.895  21.278  1.00 36.54  ? 341  ILE A N   1 
ATOM   1712 C CA  . ILE A 1 246 ? 15.421  61.866  20.851  1.00 38.99  ? 341  ILE A CA  1 
ATOM   1713 C C   . ILE A 1 246 ? 15.357  61.878  19.333  1.00 42.18  ? 341  ILE A C   1 
ATOM   1714 O O   . ILE A 1 246 ? 16.267  61.413  18.640  1.00 42.00  ? 341  ILE A O   1 
ATOM   1715 C CB  . ILE A 1 246 ? 15.719  63.282  21.387  1.00 40.11  ? 341  ILE A CB  1 
ATOM   1716 C CG1 . ILE A 1 246 ? 17.070  63.781  20.866  1.00 37.45  ? 341  ILE A CG1 1 
ATOM   1717 C CG2 . ILE A 1 246 ? 15.652  63.310  22.924  1.00 38.47  ? 341  ILE A CG2 1 
ATOM   1718 C CD1 . ILE A 1 246 ? 17.356  65.248  21.231  1.00 42.42  ? 341  ILE A CD1 1 
ATOM   1719 N N   . HIS A 1 247 ? 14.254  62.427  18.823  1.00 40.52  ? 342  HIS A N   1 
ATOM   1720 C CA  . HIS A 1 247 ? 14.019  62.584  17.388  1.00 40.08  ? 342  HIS A CA  1 
ATOM   1721 C C   . HIS A 1 247 ? 13.451  63.972  17.179  1.00 41.26  ? 342  HIS A C   1 
ATOM   1722 O O   . HIS A 1 247 ? 12.331  64.256  17.628  1.00 38.85  ? 342  HIS A O   1 
ATOM   1723 C CB  . HIS A 1 247 ? 13.058  61.526  16.848  1.00 40.04  ? 342  HIS A CB  1 
ATOM   1724 C CG  . HIS A 1 247 ? 13.609  60.134  16.908  1.00 41.09  ? 342  HIS A CG  1 
ATOM   1725 N ND1 . HIS A 1 247 ? 14.496  59.648  15.973  1.00 41.07  ? 342  HIS A ND1 1 
ATOM   1726 C CD2 . HIS A 1 247 ? 13.432  59.141  17.811  1.00 39.11  ? 342  HIS A CD2 1 
ATOM   1727 C CE1 . HIS A 1 247 ? 14.833  58.407  16.289  1.00 39.88  ? 342  HIS A CE1 1 
ATOM   1728 N NE2 . HIS A 1 247 ? 14.193  58.071  17.392  1.00 44.48  ? 342  HIS A NE2 1 
ATOM   1729 N N   . THR A 1 248 ? 14.213  64.826  16.502  1.00 40.48  ? 343  THR A N   1 
ATOM   1730 C CA  . THR A 1 248 ? 13.842  66.215  16.298  1.00 40.39  ? 343  THR A CA  1 
ATOM   1731 C C   . THR A 1 248 ? 13.668  66.512  14.809  1.00 43.34  ? 343  THR A C   1 
ATOM   1732 O O   . THR A 1 248 ? 14.204  65.795  13.957  1.00 41.05  ? 343  THR A O   1 
ATOM   1733 C CB  . THR A 1 248 ? 14.901  67.136  16.924  1.00 43.28  ? 343  THR A CB  1 
ATOM   1734 O OG1 . THR A 1 248 ? 16.163  66.946  16.272  1.00 42.30  ? 343  THR A OG1 1 
ATOM   1735 C CG2 . THR A 1 248 ? 15.049  66.828  18.417  1.00 37.89  ? 343  THR A CG2 1 
ATOM   1736 N N   . PRO A 1 249 ? 12.895  67.540  14.458  1.00 42.33  ? 344  PRO A N   1 
ATOM   1737 C CA  . PRO A 1 249 ? 12.497  67.716  13.056  1.00 43.94  ? 344  PRO A CA  1 
ATOM   1738 C C   . PRO A 1 249 ? 13.643  68.152  12.154  1.00 44.93  ? 344  PRO A C   1 
ATOM   1739 O O   . PRO A 1 249 ? 14.545  68.882  12.567  1.00 44.18  ? 344  PRO A O   1 
ATOM   1740 C CB  . PRO A 1 249 ? 11.420  68.805  13.132  1.00 43.99  ? 344  PRO A CB  1 
ATOM   1741 C CG  . PRO A 1 249 ? 11.743  69.558  14.376  1.00 45.80  ? 344  PRO A CG  1 
ATOM   1742 C CD  . PRO A 1 249 ? 12.228  68.512  15.336  1.00 43.60  ? 344  PRO A CD  1 
ATOM   1743 N N   . LYS A 1 250 ? 13.580  67.708  10.891  1.00 43.44  ? 345  LYS A N   1 
ATOM   1744 C CA  . LYS A 1 250 ? 14.494  68.188  9.858   1.00 44.32  ? 345  LYS A CA  1 
ATOM   1745 C C   . LYS A 1 250 ? 13.883  69.277  8.987   1.00 45.10  ? 345  LYS A C   1 
ATOM   1746 O O   . LYS A 1 250 ? 14.622  69.959  8.274   1.00 46.72  ? 345  LYS A O   1 
ATOM   1747 C CB  . LYS A 1 250 ? 14.965  67.032  8.960   1.00 42.45  ? 345  LYS A CB  1 
ATOM   1748 C CG  . LYS A 1 250 ? 15.371  65.774  9.728   1.00 40.20  ? 345  LYS A CG  1 
ATOM   1749 C CD  . LYS A 1 250 ? 16.350  66.103  10.846  1.00 42.44  ? 345  LYS A CD  1 
ATOM   1750 C CE  . LYS A 1 250 ? 16.504  64.956  11.813  1.00 39.32  ? 345  LYS A CE  1 
ATOM   1751 N NZ  . LYS A 1 250 ? 17.139  65.418  13.094  1.00 41.55  ? 345  LYS A NZ  1 
ATOM   1752 N N   . LEU A 1 251 ? 12.564  69.439  9.010   1.00 41.62  ? 346  LEU A N   1 
ATOM   1753 C CA  . LEU A 1 251 ? 11.913  70.569  8.366   1.00 47.05  ? 346  LEU A CA  1 
ATOM   1754 C C   . LEU A 1 251 ? 11.922  71.755  9.326   1.00 49.74  ? 346  LEU A C   1 
ATOM   1755 O O   . LEU A 1 251 ? 11.349  71.677  10.416  1.00 49.53  ? 346  LEU A O   1 
ATOM   1756 C CB  . LEU A 1 251 ? 10.486  70.208  7.967   1.00 47.27  ? 346  LEU A CB  1 
ATOM   1757 C CG  . LEU A 1 251 ? 10.364  69.075  6.944   1.00 49.58  ? 346  LEU A CG  1 
ATOM   1758 C CD1 . LEU A 1 251 ? 8.915   68.898  6.499   1.00 47.44  ? 346  LEU A CD1 1 
ATOM   1759 C CD2 . LEU A 1 251 ? 11.258  69.351  5.740   1.00 50.38  ? 346  LEU A CD2 1 
ATOM   1760 N N   . LEU A 1 252 ? 12.579  72.845  8.927   1.00 49.42  ? 347  LEU A N   1 
ATOM   1761 C CA  . LEU A 1 252 ? 12.801  73.997  9.785   1.00 54.50  ? 347  LEU A CA  1 
ATOM   1762 C C   . LEU A 1 252 ? 12.133  75.221  9.186   1.00 55.81  ? 347  LEU A C   1 
ATOM   1763 O O   . LEU A 1 252 ? 11.999  75.335  7.961   1.00 54.85  ? 347  LEU A O   1 
ATOM   1764 C CB  . LEU A 1 252 ? 14.294  74.278  9.973   1.00 52.87  ? 347  LEU A CB  1 
ATOM   1765 C CG  . LEU A 1 252 ? 15.138  73.146  10.545  1.00 52.03  ? 347  LEU A CG  1 
ATOM   1766 C CD1 . LEU A 1 252 ? 16.531  73.647  10.874  1.00 53.09  ? 347  LEU A CD1 1 
ATOM   1767 C CD2 . LEU A 1 252 ? 14.472  72.543  11.778  1.00 48.58  ? 347  LEU A CD2 1 
ATOM   1768 N N   . GLY A 1 253 ? 11.689  76.127  10.062  1.00 58.03  ? 348  GLY A N   1 
ATOM   1769 C CA  . GLY A 1 253 ? 11.193  77.405  9.586   1.00 59.47  ? 348  GLY A CA  1 
ATOM   1770 C C   . GLY A 1 253 ? 12.316  78.338  9.197   1.00 66.08  ? 348  GLY A C   1 
ATOM   1771 O O   . GLY A 1 253 ? 12.150  79.185  8.316   1.00 69.06  ? 348  GLY A O   1 
ATOM   1772 N N   . GLU A 1 254 ? 13.459  78.172  9.820   1.00 67.27  ? 349  GLU A N   1 
ATOM   1773 C CA  . GLU A 1 254 ? 14.617  78.990  9.566   1.00 70.49  ? 349  GLU A CA  1 
ATOM   1774 C C   . GLU A 1 254 ? 15.842  78.084  9.662   1.00 75.73  ? 349  GLU A C   1 
ATOM   1775 O O   . GLU A 1 254 ? 15.786  77.049  10.289  1.00 73.30  ? 349  GLU A O   1 
ATOM   1776 C CB  . GLU A 1 254 ? 14.676  80.107  10.604  1.00 73.49  ? 349  GLU A CB  1 
ATOM   1777 C CG  . GLU A 1 254 ? 14.775  81.503  10.041  1.00 76.18  ? 349  GLU A CG  1 
ATOM   1778 C CD  . GLU A 1 254 ? 13.522  81.952  9.323   1.00 79.86  ? 349  GLU A CD  1 
ATOM   1779 O OE1 . GLU A 1 254 ? 12.476  82.083  9.960   1.00 80.07  ? 349  GLU A OE1 1 
ATOM   1780 O OE2 . GLU A 1 254 ? 13.588  82.210  8.116   1.00 78.86  ? 349  GLU A OE2 1 
ATOM   1781 N N   . SER A 1 255 ? 16.960  78.475  9.066   1.00 86.85  ? 350  SER A N   1 
ATOM   1782 C CA  . SER A 1 255 ? 18.151  77.638  9.070   1.00 90.65  ? 350  SER A CA  1 
ATOM   1783 C C   . SER A 1 255 ? 19.027  77.939  10.284  1.00 96.61  ? 350  SER A C   1 
ATOM   1784 O O   . SER A 1 255 ? 19.379  77.040  11.052  1.00 98.55  ? 350  SER A O   1 
ATOM   1785 C CB  . SER A 1 255 ? 18.956  77.834  7.784   1.00 93.68  ? 350  SER A CB  1 
ATOM   1786 O OG  . SER A 1 255 ? 19.643  79.070  7.813   1.00 97.07  ? 350  SER A OG  1 
ATOM   1787 N N   . ALA A 1 260 ? 21.857  79.678  4.111   1.00 111.20 ? 355  ALA A N   1 
ATOM   1788 C CA  . ALA A 1 260 ? 23.190  79.889  3.577   1.00 111.98 ? 355  ALA A CA  1 
ATOM   1789 C C   . ALA A 1 260 ? 23.621  78.644  2.834   1.00 108.84 ? 355  ALA A C   1 
ATOM   1790 O O   . ALA A 1 260 ? 23.695  78.629  1.613   1.00 111.54 ? 355  ALA A O   1 
ATOM   1791 C CB  . ALA A 1 260 ? 24.163  80.220  4.689   1.00 114.34 ? 355  ALA A CB  1 
ATOM   1792 N N   . ASN A 1 261 ? 23.905  77.593  3.577   1.00 87.46  ? 356  ASN A N   1 
ATOM   1793 C CA  . ASN A 1 261 ? 24.262  76.356  2.960   1.00 75.98  ? 356  ASN A CA  1 
ATOM   1794 C C   . ASN A 1 261 ? 23.169  75.375  3.286   1.00 69.57  ? 356  ASN A C   1 
ATOM   1795 O O   . ASN A 1 261 ? 23.434  74.265  3.646   1.00 63.21  ? 356  ASN A O   1 
ATOM   1796 C CB  . ASN A 1 261 ? 25.578  75.867  3.512   1.00 75.54  ? 356  ASN A CB  1 
ATOM   1797 C CG  . ASN A 1 261 ? 26.755  76.606  2.934   1.00 82.31  ? 356  ASN A CG  1 
ATOM   1798 O OD1 . ASN A 1 261 ? 26.720  77.065  1.801   1.00 83.13  ? 356  ASN A OD1 1 
ATOM   1799 N ND2 . ASN A 1 261 ? 27.806  76.721  3.713   1.00 82.29  ? 356  ASN A ND2 1 
ATOM   1800 N N   . ALA A 1 262 ? 21.929  75.805  3.161   1.00 68.27  ? 357  ALA A N   1 
ATOM   1801 C CA  . ALA A 1 262 ? 20.815  74.953  3.478   1.00 63.11  ? 357  ALA A CA  1 
ATOM   1802 C C   . ALA A 1 262 ? 19.833  74.823  2.355   1.00 59.91  ? 357  ALA A C   1 
ATOM   1803 O O   . ALA A 1 262 ? 19.544  75.784  1.693   1.00 59.16  ? 357  ALA A O   1 
ATOM   1804 C CB  . ALA A 1 262 ? 20.114  75.491  4.698   1.00 61.23  ? 357  ALA A CB  1 
ATOM   1805 N N   . PHE A 1 263 ? 19.345  73.619  2.124   1.00 53.53  ? 358  PHE A N   1 
ATOM   1806 C CA  . PHE A 1 263 ? 18.325  73.418  1.105   1.00 53.38  ? 358  PHE A CA  1 
ATOM   1807 C C   . PHE A 1 263 ? 17.037  74.120  1.518   1.00 58.19  ? 358  PHE A C   1 
ATOM   1808 O O   . PHE A 1 263 ? 16.623  74.064  2.681   1.00 53.37  ? 358  PHE A O   1 
ATOM   1809 C CB  . PHE A 1 263 ? 18.043  71.928  0.891   1.00 50.95  ? 358  PHE A CB  1 
ATOM   1810 C CG  . PHE A 1 263 ? 19.205  71.151  0.339   1.00 52.59  ? 358  PHE A CG  1 
ATOM   1811 C CD1 . PHE A 1 263 ? 19.468  71.139  -1.026  1.00 54.64  ? 358  PHE A CD1 1 
ATOM   1812 C CD2 . PHE A 1 263 ? 20.020  70.414  1.181   1.00 47.11  ? 358  PHE A CD2 1 
ATOM   1813 C CE1 . PHE A 1 263 ? 20.534  70.415  -1.533  1.00 50.83  ? 358  PHE A CE1 1 
ATOM   1814 C CE2 . PHE A 1 263 ? 21.082  69.689  0.680   1.00 46.16  ? 358  PHE A CE2 1 
ATOM   1815 C CZ  . PHE A 1 263 ? 21.335  69.682  -0.672  1.00 50.49  ? 358  PHE A CZ  1 
ATOM   1816 N N   . GLN A 1 264 ? 16.390  74.766  0.556   1.00 55.71  ? 359  GLN A N   1 
ATOM   1817 C CA  . GLN A 1 264 ? 15.103  75.402  0.781   1.00 54.63  ? 359  GLN A CA  1 
ATOM   1818 C C   . GLN A 1 264 ? 13.976  74.500  0.308   1.00 57.56  ? 359  GLN A C   1 
ATOM   1819 O O   . GLN A 1 264 ? 14.126  73.724  -0.638  1.00 60.37  ? 359  GLN A O   1 
ATOM   1820 C CB  . GLN A 1 264 ? 15.027  76.742  0.061   1.00 59.63  ? 359  GLN A CB  1 
ATOM   1821 C CG  . GLN A 1 264 ? 16.178  77.654  0.402   1.00 61.73  ? 359  GLN A CG  1 
ATOM   1822 C CD  . GLN A 1 264 ? 16.343  78.751  -0.617  1.00 71.18  ? 359  GLN A CD  1 
ATOM   1823 O OE1 . GLN A 1 264 ? 15.494  78.920  -1.492  1.00 73.80  ? 359  GLN A OE1 1 
ATOM   1824 N NE2 . GLN A 1 264 ? 17.443  79.498  -0.523  1.00 67.65  ? 359  GLN A NE2 1 
ATOM   1825 N N   . ILE A 1 265 ? 12.842  74.598  0.995   1.00 55.78  ? 360  ILE A N   1 
ATOM   1826 C CA  . ILE A 1 265 ? 11.636  73.870  0.640   1.00 58.15  ? 360  ILE A CA  1 
ATOM   1827 C C   . ILE A 1 265 ? 10.462  74.825  0.789   1.00 59.69  ? 360  ILE A C   1 
ATOM   1828 O O   . ILE A 1 265 ? 10.508  75.792  1.555   1.00 62.74  ? 360  ILE A O   1 
ATOM   1829 C CB  . ILE A 1 265 ? 11.419  72.616  1.521   1.00 62.07  ? 360  ILE A CB  1 
ATOM   1830 C CG1 . ILE A 1 265 ? 11.447  72.992  3.000   1.00 60.81  ? 360  ILE A CG1 1 
ATOM   1831 C CG2 . ILE A 1 265 ? 12.490  71.591  1.290   1.00 62.09  ? 360  ILE A CG2 1 
ATOM   1832 C CD1 . ILE A 1 265 ? 10.097  72.976  3.645   1.00 64.76  ? 360  ILE A CD1 1 
ATOM   1833 N N   . ASN A 1 266 ? 9.405   74.547  0.036   1.00 59.00  ? 361  ASN A N   1 
ATOM   1834 C CA  . ASN A 1 266 ? 8.120   75.206  0.221   1.00 60.85  ? 361  ASN A CA  1 
ATOM   1835 C C   . ASN A 1 266 ? 7.293   74.335  1.163   1.00 65.05  ? 361  ASN A C   1 
ATOM   1836 O O   . ASN A 1 266 ? 6.941   73.198  0.822   1.00 62.49  ? 361  ASN A O   1 
ATOM   1837 C CB  . ASN A 1 266 ? 7.404   75.419  -1.111  1.00 64.60  ? 361  ASN A CB  1 
ATOM   1838 C CG  . ASN A 1 266 ? 6.012   76.013  -0.937  1.00 76.37  ? 361  ASN A CG  1 
ATOM   1839 O OD1 . ASN A 1 266 ? 5.769   76.806  -0.022  1.00 78.89  ? 361  ASN A OD1 1 
ATOM   1840 N ND2 . ASN A 1 266 ? 5.084   75.620  -1.810  1.00 83.62  ? 361  ASN A ND2 1 
ATOM   1841 N N   . TYR A 1 267 ? 7.009   74.861  2.354   1.00 63.45  ? 362  TYR A N   1 
ATOM   1842 C CA  . TYR A 1 267 ? 6.221   74.176  3.372   1.00 60.43  ? 362  TYR A CA  1 
ATOM   1843 C C   . TYR A 1 267 ? 4.863   74.870  3.445   1.00 63.73  ? 362  TYR A C   1 
ATOM   1844 O O   . TYR A 1 267 ? 4.647   75.771  4.256   1.00 64.89  ? 362  TYR A O   1 
ATOM   1845 C CB  . TYR A 1 267 ? 6.953   74.199  4.709   1.00 56.05  ? 362  TYR A CB  1 
ATOM   1846 C CG  . TYR A 1 267 ? 6.329   73.319  5.756   1.00 56.59  ? 362  TYR A CG  1 
ATOM   1847 C CD1 . TYR A 1 267 ? 6.668   71.974  5.848   1.00 53.80  ? 362  TYR A CD1 1 
ATOM   1848 C CD2 . TYR A 1 267 ? 5.396   73.830  6.660   1.00 53.64  ? 362  TYR A CD2 1 
ATOM   1849 C CE1 . TYR A 1 267 ? 6.084   71.151  6.811   1.00 52.76  ? 362  TYR A CE1 1 
ATOM   1850 C CE2 . TYR A 1 267 ? 4.809   73.017  7.622   1.00 52.88  ? 362  TYR A CE2 1 
ATOM   1851 C CZ  . TYR A 1 267 ? 5.155   71.683  7.695   1.00 52.11  ? 362  TYR A CZ  1 
ATOM   1852 O OH  . TYR A 1 267 ? 4.583   70.887  8.652   1.00 48.88  ? 362  TYR A OH  1 
ATOM   1853 N N   . PHE A 1 268 ? 3.947   74.450  2.575   1.00 64.40  ? 363  PHE A N   1 
ATOM   1854 C CA  . PHE A 1 268 ? 2.570   74.953  2.559   1.00 67.02  ? 363  PHE A CA  1 
ATOM   1855 C C   . PHE A 1 268 ? 2.530   76.480  2.457   1.00 75.69  ? 363  PHE A C   1 
ATOM   1856 O O   . PHE A 1 268 ? 1.829   77.166  3.208   1.00 76.49  ? 363  PHE A O   1 
ATOM   1857 C CB  . PHE A 1 268 ? 1.795   74.452  3.781   1.00 61.42  ? 363  PHE A CB  1 
ATOM   1858 C CG  . PHE A 1 268 ? 1.687   72.954  3.848   1.00 59.88  ? 363  PHE A CG  1 
ATOM   1859 C CD1 . PHE A 1 268 ? 2.514   72.224  4.678   1.00 54.40  ? 363  PHE A CD1 1 
ATOM   1860 C CD2 . PHE A 1 268 ? 0.775   72.277  3.056   1.00 58.40  ? 363  PHE A CD2 1 
ATOM   1861 C CE1 . PHE A 1 268 ? 2.420   70.849  4.736   1.00 53.84  ? 363  PHE A CE1 1 
ATOM   1862 C CE2 . PHE A 1 268 ? 0.680   70.901  3.110   1.00 59.37  ? 363  PHE A CE2 1 
ATOM   1863 C CZ  . PHE A 1 268 ? 1.503   70.188  3.950   1.00 54.98  ? 363  PHE A CZ  1 
ATOM   1864 N N   . ASN A 1 269 ? 3.296   77.008  1.500   1.00 86.90  ? 364  ASN A N   1 
ATOM   1865 C CA  . ASN A 1 269 ? 3.442   78.438  1.234   1.00 87.59  ? 364  ASN A CA  1 
ATOM   1866 C C   . ASN A 1 269 ? 4.110   79.194  2.375   1.00 84.51  ? 364  ASN A C   1 
ATOM   1867 O O   . ASN A 1 269 ? 4.045   80.426  2.426   1.00 85.14  ? 364  ASN A O   1 
ATOM   1868 C CB  . ASN A 1 269 ? 2.106   79.091  0.868   1.00 92.58  ? 364  ASN A CB  1 
ATOM   1869 C CG  . ASN A 1 269 ? 1.783   78.939  -0.605  1.00 99.41  ? 364  ASN A CG  1 
ATOM   1870 O OD1 . ASN A 1 269 ? 1.082   78.006  -1.007  1.00 101.70 ? 364  ASN A OD1 1 
ATOM   1871 N ND2 . ASN A 1 269 ? 2.316   79.845  -1.425  1.00 105.68 ? 364  ASN A ND2 1 
ATOM   1872 N N   . GLN A 1 270 ? 4.751   78.480  3.290   1.00 72.81  ? 365  GLN A N   1 
ATOM   1873 C CA  . GLN A 1 270 ? 5.829   79.031  4.094   1.00 70.24  ? 365  GLN A CA  1 
ATOM   1874 C C   . GLN A 1 270 ? 7.150   78.656  3.442   1.00 69.36  ? 365  GLN A C   1 
ATOM   1875 O O   . GLN A 1 270 ? 7.246   77.676  2.707   1.00 70.73  ? 365  GLN A O   1 
ATOM   1876 C CB  . GLN A 1 270 ? 5.808   78.499  5.527   1.00 65.24  ? 365  GLN A CB  1 
ATOM   1877 C CG  . GLN A 1 270 ? 4.469   78.555  6.214   1.00 66.74  ? 365  GLN A CG  1 
ATOM   1878 C CD  . GLN A 1 270 ? 4.593   78.300  7.701   1.00 63.21  ? 365  GLN A CD  1 
ATOM   1879 O OE1 . GLN A 1 270 ? 5.454   78.886  8.375   1.00 60.52  ? 365  GLN A OE1 1 
ATOM   1880 N NE2 . GLN A 1 270 ? 3.738   77.419  8.226   1.00 58.50  ? 365  GLN A NE2 1 
ATOM   1881 N N   . LYS A 1 271 ? 8.175   79.438  3.722   1.00 63.08  ? 366  LYS A N   1 
ATOM   1882 C CA  . LYS A 1 271 ? 9.513   79.116  3.263   1.00 66.14  ? 366  LYS A CA  1 
ATOM   1883 C C   . LYS A 1 271 ? 10.238  78.421  4.406   1.00 66.69  ? 366  LYS A C   1 
ATOM   1884 O O   . LYS A 1 271 ? 10.317  78.964  5.514   1.00 64.49  ? 366  LYS A O   1 
ATOM   1885 C CB  . LYS A 1 271 ? 10.248  80.369  2.793   1.00 70.36  ? 366  LYS A CB  1 
ATOM   1886 C CG  . LYS A 1 271 ? 9.592   81.008  1.557   1.00 75.89  ? 366  LYS A CG  1 
ATOM   1887 C CD  . LYS A 1 271 ? 9.160   79.929  0.540   1.00 78.94  ? 366  LYS A CD  1 
ATOM   1888 C CE  . LYS A 1 271 ? 8.535   80.528  -0.722  1.00 81.85  ? 366  LYS A CE  1 
ATOM   1889 N NZ  . LYS A 1 271 ? 7.198   81.156  -0.470  1.00 83.95  ? 366  LYS A NZ  1 
ATOM   1890 N N   . GLY A 1 272 ? 10.722  77.202  4.150   1.00 63.93  ? 367  GLY A N   1 
ATOM   1891 C CA  . GLY A 1 272 ? 11.412  76.428  5.156   1.00 59.57  ? 367  GLY A CA  1 
ATOM   1892 C C   . GLY A 1 272 ? 12.730  75.896  4.624   1.00 60.26  ? 367  GLY A C   1 
ATOM   1893 O O   . GLY A 1 272 ? 13.077  76.089  3.458   1.00 58.33  ? 367  GLY A O   1 
ATOM   1894 N N   . PHE A 1 273 ? 13.437  75.193  5.504   1.00 56.75  ? 368  PHE A N   1 
ATOM   1895 C CA  . PHE A 1 273 ? 14.766  74.708  5.196   1.00 53.32  ? 368  PHE A CA  1 
ATOM   1896 C C   . PHE A 1 273 ? 14.935  73.322  5.800   1.00 54.67  ? 368  PHE A C   1 
ATOM   1897 O O   . PHE A 1 273 ? 14.203  72.927  6.712   1.00 52.80  ? 368  PHE A O   1 
ATOM   1898 C CB  . PHE A 1 273 ? 15.840  75.677  5.721   1.00 56.72  ? 368  PHE A CB  1 
ATOM   1899 C CG  . PHE A 1 273 ? 15.623  77.117  5.307   1.00 61.58  ? 368  PHE A CG  1 
ATOM   1900 C CD1 . PHE A 1 273 ? 16.222  77.629  4.160   1.00 60.26  ? 368  PHE A CD1 1 
ATOM   1901 C CD2 . PHE A 1 273 ? 14.824  77.960  6.067   1.00 61.03  ? 368  PHE A CD2 1 
ATOM   1902 C CE1 . PHE A 1 273 ? 16.017  78.961  3.775   1.00 60.92  ? 368  PHE A CE1 1 
ATOM   1903 C CE2 . PHE A 1 273 ? 14.618  79.285  5.693   1.00 62.69  ? 368  PHE A CE2 1 
ATOM   1904 C CZ  . PHE A 1 273 ? 15.219  79.787  4.551   1.00 60.27  ? 368  PHE A CZ  1 
ATOM   1905 N N   . LEU A 1 274 ? 15.914  72.582  5.280   1.00 48.86  ? 369  LEU A N   1 
ATOM   1906 C CA  . LEU A 1 274 ? 16.308  71.303  5.854   1.00 49.56  ? 369  LEU A CA  1 
ATOM   1907 C C   . LEU A 1 274 ? 17.377  71.525  6.914   1.00 48.02  ? 369  LEU A C   1 
ATOM   1908 O O   . LEU A 1 274 ? 18.296  72.331  6.728   1.00 46.28  ? 369  LEU A O   1 
ATOM   1909 C CB  . LEU A 1 274 ? 16.834  70.350  4.775   1.00 44.90  ? 369  LEU A CB  1 
ATOM   1910 C CG  . LEU A 1 274 ? 15.825  69.963  3.696   1.00 50.53  ? 369  LEU A CG  1 
ATOM   1911 C CD1 . LEU A 1 274 ? 16.433  69.056  2.628   1.00 49.66  ? 369  LEU A CD1 1 
ATOM   1912 C CD2 . LEU A 1 274 ? 14.636  69.286  4.341   1.00 50.96  ? 369  LEU A CD2 1 
ATOM   1913 N N   . ALA A 1 275 ? 17.243  70.816  8.035   1.00 44.74  ? 370  ALA A N   1 
ATOM   1914 C CA  . ALA A 1 275 ? 18.218  70.926  9.111   1.00 47.19  ? 370  ALA A CA  1 
ATOM   1915 C C   . ALA A 1 275 ? 19.610  70.494  8.655   1.00 46.87  ? 370  ALA A C   1 
ATOM   1916 O O   . ALA A 1 275 ? 19.797  69.399  8.113   1.00 44.76  ? 370  ALA A O   1 
ATOM   1917 C CB  . ALA A 1 275 ? 17.784  70.080  10.312  1.00 40.51  ? 370  ALA A CB  1 
ATOM   1918 N N   . GLN A 1 276 ? 20.598  71.349  8.908   1.00 45.09  ? 371  GLN A N   1 
ATOM   1919 C CA  . GLN A 1 276 ? 21.992  70.951  8.788   1.00 45.80  ? 371  GLN A CA  1 
ATOM   1920 C C   . GLN A 1 276 ? 22.493  70.238  10.036  1.00 44.22  ? 371  GLN A C   1 
ATOM   1921 O O   . GLN A 1 276 ? 23.498  69.528  9.970   1.00 43.06  ? 371  GLN A O   1 
ATOM   1922 C CB  . GLN A 1 276 ? 22.855  72.184  8.507   1.00 45.25  ? 371  GLN A CB  1 
ATOM   1923 C CG  . GLN A 1 276 ? 22.405  72.951  7.288   1.00 51.80  ? 371  GLN A CG  1 
ATOM   1924 C CD  . GLN A 1 276 ? 23.119  74.286  7.148   1.00 60.58  ? 371  GLN A CD  1 
ATOM   1925 O OE1 . GLN A 1 276 ? 22.491  75.335  7.169   1.00 64.03  ? 371  GLN A OE1 1 
ATOM   1926 N NE2 . GLN A 1 276 ? 24.431  74.246  7.018   1.00 62.13  ? 371  GLN A NE2 1 
ATOM   1927 N N   . SER A 1 277 ? 21.803  70.398  11.157  1.00 45.00  ? 372  SER A N   1 
ATOM   1928 C CA  . SER A 1 277 ? 22.163  69.838  12.451  1.00 43.07  ? 372  SER A CA  1 
ATOM   1929 C C   . SER A 1 277 ? 20.941  69.917  13.351  1.00 44.12  ? 372  SER A C   1 
ATOM   1930 O O   . SER A 1 277 ? 20.121  70.829  13.192  1.00 45.90  ? 372  SER A O   1 
ATOM   1931 C CB  . SER A 1 277 ? 23.319  70.633  13.055  1.00 44.76  ? 372  SER A CB  1 
ATOM   1932 O OG  . SER A 1 277 ? 23.429  70.382  14.447  1.00 49.09  ? 372  SER A OG  1 
ATOM   1933 N N   . PRO A 1 278 ? 20.746  68.992  14.290  1.00 43.00  ? 373  PRO A N   1 
ATOM   1934 C CA  . PRO A 1 278 ? 19.635  69.149  15.215  1.00 43.78  ? 373  PRO A CA  1 
ATOM   1935 C C   . PRO A 1 278 ? 20.087  69.963  16.430  1.00 43.55  ? 373  PRO A C   1 
ATOM   1936 O O   . PRO A 1 278 ? 19.485  69.906  17.462  1.00 44.54  ? 373  PRO A O   1 
ATOM   1937 C CB  . PRO A 1 278 ? 19.402  67.730  15.652  1.00 43.25  ? 373  PRO A CB  1 
ATOM   1938 C CG  . PRO A 1 278 ? 20.775  67.183  15.726  1.00 44.35  ? 373  PRO A CG  1 
ATOM   1939 C CD  . PRO A 1 278 ? 21.545  67.812  14.618  1.00 42.33  ? 373  PRO A CD  1 
ATOM   1940 N N   . GLN A 1 279 ? 21.065  70.820  16.251  1.00 44.91  ? 374  GLN A N   1 
ATOM   1941 C CA  . GLN A 1 279 ? 21.670  71.538  17.349  1.00 44.03  ? 374  GLN A CA  1 
ATOM   1942 C C   . GLN A 1 279 ? 20.717  72.352  18.202  1.00 43.93  ? 374  GLN A C   1 
ATOM   1943 O O   . GLN A 1 279 ? 20.739  72.238  19.395  1.00 45.96  ? 374  GLN A O   1 
ATOM   1944 C CB  . GLN A 1 279 ? 22.696  72.496  16.762  1.00 43.64  ? 374  GLN A CB  1 
ATOM   1945 C CG  . GLN A 1 279 ? 23.341  73.432  17.732  1.00 45.98  ? 374  GLN A CG  1 
ATOM   1946 C CD  . GLN A 1 279 ? 24.304  72.731  18.623  1.00 48.90  ? 374  GLN A CD  1 
ATOM   1947 O OE1 . GLN A 1 279 ? 25.109  71.964  18.172  1.00 51.36  ? 374  GLN A OE1 1 
ATOM   1948 N NE2 . GLN A 1 279 ? 24.215  72.983  19.888  1.00 47.00  ? 374  GLN A NE2 1 
ATOM   1949 N N   . LEU A 1 280 ? 19.829  73.098  17.599  1.00 42.94  ? 375  LEU A N   1 
ATOM   1950 C CA  . LEU A 1 280 ? 18.939  73.893  18.398  1.00 45.05  ? 375  LEU A CA  1 
ATOM   1951 C C   . LEU A 1 280 ? 17.979  73.049  19.235  1.00 44.67  ? 375  LEU A C   1 
ATOM   1952 O O   . LEU A 1 280 ? 17.764  73.333  20.379  1.00 47.57  ? 375  LEU A O   1 
ATOM   1953 C CB  . LEU A 1 280 ? 18.198  74.897  17.533  1.00 43.15  ? 375  LEU A CB  1 
ATOM   1954 C CG  . LEU A 1 280 ? 19.051  75.796  16.646  1.00 51.55  ? 375  LEU A CG  1 
ATOM   1955 C CD1 . LEU A 1 280 ? 18.248  76.816  15.890  1.00 49.51  ? 375  LEU A CD1 1 
ATOM   1956 C CD2 . LEU A 1 280 ? 20.141  76.464  17.421  1.00 46.08  ? 375  LEU A CD2 1 
ATOM   1957 N N   . TYR A 1 281 ? 17.458  71.984  18.665  1.00 44.23  ? 376  TYR A N   1 
ATOM   1958 C CA  . TYR A 1 281 ? 16.471  71.144  19.356  1.00 45.67  ? 376  TYR A CA  1 
ATOM   1959 C C   . TYR A 1 281 ? 17.094  70.312  20.474  1.00 43.86  ? 376  TYR A C   1 
ATOM   1960 O O   . TYR A 1 281 ? 16.453  70.088  21.505  1.00 45.50  ? 376  TYR A O   1 
ATOM   1961 C CB  . TYR A 1 281 ? 15.747  70.238  18.355  1.00 40.86  ? 376  TYR A CB  1 
ATOM   1962 C CG  . TYR A 1 281 ? 14.956  71.038  17.362  1.00 45.55  ? 376  TYR A CG  1 
ATOM   1963 C CD1 . TYR A 1 281 ? 13.837  71.748  17.754  1.00 45.06  ? 376  TYR A CD1 1 
ATOM   1964 C CD2 . TYR A 1 281 ? 15.360  71.125  16.041  1.00 48.28  ? 376  TYR A CD2 1 
ATOM   1965 C CE1 . TYR A 1 281 ? 13.125  72.516  16.854  1.00 48.30  ? 376  TYR A CE1 1 
ATOM   1966 C CE2 . TYR A 1 281 ? 14.655  71.884  15.133  1.00 52.13  ? 376  TYR A CE2 1 
ATOM   1967 C CZ  . TYR A 1 281 ? 13.542  72.578  15.545  1.00 53.80  ? 376  TYR A CZ  1 
ATOM   1968 O OH  . TYR A 1 281 ? 12.853  73.338  14.629  1.00 57.92  ? 376  TYR A OH  1 
ATOM   1969 N N   . LYS A 1 282 ? 18.328  69.822  20.301  1.00 41.20  ? 377  LYS A N   1 
ATOM   1970 C CA  . LYS A 1 282 ? 18.902  69.030  21.387  1.00 41.60  ? 377  LYS A CA  1 
ATOM   1971 C C   . LYS A 1 282 ? 19.250  69.911  22.583  1.00 46.21  ? 377  LYS A C   1 
ATOM   1972 O O   . LYS A 1 282 ? 19.049  69.495  23.743  1.00 45.89  ? 377  LYS A O   1 
ATOM   1973 C CB  . LYS A 1 282 ? 20.117  68.218  20.907  1.00 44.00  ? 377  LYS A CB  1 
ATOM   1974 C CG  . LYS A 1 282 ? 21.262  69.001  20.280  1.00 46.10  ? 377  LYS A CG  1 
ATOM   1975 C CD  . LYS A 1 282 ? 22.379  68.041  19.811  1.00 41.29  ? 377  LYS A CD  1 
ATOM   1976 C CE  . LYS A 1 282 ? 23.639  68.810  19.430  1.00 45.40  ? 377  LYS A CE  1 
ATOM   1977 N NZ  . LYS A 1 282 ? 24.859  67.951  19.449  1.00 46.08  ? 377  LYS A NZ  1 
ATOM   1978 N N   . GLN A 1 283 ? 19.683  71.157  22.335  1.00 43.72  ? 378  GLN A N   1 
ATOM   1979 C CA  . GLN A 1 283 ? 19.796  72.097  23.453  1.00 46.24  ? 378  GLN A CA  1 
ATOM   1980 C C   . GLN A 1 283 ? 18.434  72.413  24.078  1.00 46.89  ? 378  GLN A C   1 
ATOM   1981 O O   . GLN A 1 283 ? 18.329  72.551  25.300  1.00 47.70  ? 378  GLN A O   1 
ATOM   1982 C CB  . GLN A 1 283 ? 20.476  73.384  23.002  1.00 45.90  ? 378  GLN A CB  1 
ATOM   1983 C CG  . GLN A 1 283 ? 21.979  73.282  22.754  1.00 43.47  ? 378  GLN A CG  1 
ATOM   1984 C CD  . GLN A 1 283 ? 22.586  74.662  22.559  1.00 46.36  ? 378  GLN A CD  1 
ATOM   1985 O OE1 . GLN A 1 283 ? 22.778  75.113  21.427  1.00 44.29  ? 378  GLN A OE1 1 
ATOM   1986 N NE2 . GLN A 1 283 ? 22.826  75.372  23.669  1.00 46.67  ? 378  GLN A NE2 1 
ATOM   1987 N N   . MET A 1 284 ? 17.385  72.584  23.267  1.00 43.54  ? 379  MET A N   1 
ATOM   1988 C CA  . MET A 1 284 ? 16.070  72.843  23.862  1.00 45.25  ? 379  MET A CA  1 
ATOM   1989 C C   . MET A 1 284 ? 15.616  71.679  24.745  1.00 48.27  ? 379  MET A C   1 
ATOM   1990 O O   . MET A 1 284 ? 14.971  71.888  25.785  1.00 48.33  ? 379  MET A O   1 
ATOM   1991 C CB  . MET A 1 284 ? 15.041  73.124  22.771  1.00 44.34  ? 379  MET A CB  1 
ATOM   1992 C CG  . MET A 1 284 ? 15.158  74.513  22.144  1.00 50.67  ? 379  MET A CG  1 
ATOM   1993 S SD  . MET A 1 284 ? 14.178  74.684  20.629  1.00 62.66  ? 379  MET A SD  1 
ATOM   1994 C CE  . MET A 1 284 ? 12.546  74.717  21.348  1.00 55.75  ? 379  MET A CE  1 
ATOM   1995 N N   . CYS A 1 285 ? 15.947  70.443  24.347  1.00 45.80  ? 380  CYS A N   1 
ATOM   1996 C CA  . CYS A 1 285 ? 15.654  69.287  25.197  1.00 47.70  ? 380  CYS A CA  1 
ATOM   1997 C C   . CYS A 1 285 ? 16.434  69.347  26.502  1.00 46.69  ? 380  CYS A C   1 
ATOM   1998 O O   . CYS A 1 285 ? 15.908  68.988  27.563  1.00 46.59  ? 380  CYS A O   1 
ATOM   1999 C CB  . CYS A 1 285 ? 15.963  67.981  24.462  1.00 44.15  ? 380  CYS A CB  1 
ATOM   2000 S SG  . CYS A 1 285 ? 14.796  67.641  23.162  1.00 45.18  ? 380  CYS A SG  1 
ATOM   2001 N N   . ILE A 1 286 ? 17.697  69.781  26.451  1.00 45.21  ? 381  ILE A N   1 
ATOM   2002 C CA  . ILE A 1 286 ? 18.438  69.899  27.709  1.00 45.15  ? 381  ILE A CA  1 
ATOM   2003 C C   . ILE A 1 286 ? 17.820  70.985  28.584  1.00 50.04  ? 381  ILE A C   1 
ATOM   2004 O O   . ILE A 1 286 ? 17.698  70.828  29.809  1.00 45.64  ? 381  ILE A O   1 
ATOM   2005 C CB  . ILE A 1 286 ? 19.936  70.150  27.458  1.00 49.39  ? 381  ILE A CB  1 
ATOM   2006 C CG1 . ILE A 1 286 ? 20.562  68.932  26.777  1.00 49.28  ? 381  ILE A CG1 1 
ATOM   2007 C CG2 . ILE A 1 286 ? 20.668  70.448  28.778  1.00 48.05  ? 381  ILE A CG2 1 
ATOM   2008 C CD1 . ILE A 1 286 ? 20.452  67.672  27.601  1.00 47.83  ? 381  ILE A CD1 1 
ATOM   2009 N N   . ASN A 1 287 ? 17.392  72.090  27.973  1.00 47.23  ? 382  ASN A N   1 
ATOM   2010 C CA  . ASN A 1 287 ? 16.722  73.127  28.742  1.00 49.78  ? 382  ASN A CA  1 
ATOM   2011 C C   . ASN A 1 287 ? 15.380  72.662  29.280  1.00 51.39  ? 382  ASN A C   1 
ATOM   2012 O O   . ASN A 1 287 ? 14.839  73.321  30.166  1.00 52.19  ? 382  ASN A O   1 
ATOM   2013 C CB  . ASN A 1 287 ? 16.524  74.386  27.901  1.00 48.84  ? 382  ASN A CB  1 
ATOM   2014 C CG  . ASN A 1 287 ? 17.820  75.139  27.656  1.00 50.41  ? 382  ASN A CG  1 
ATOM   2015 O OD1 . ASN A 1 287 ? 18.745  75.100  28.471  1.00 51.29  ? 382  ASN A OD1 1 
ATOM   2016 N ND2 . ASN A 1 287 ? 17.883  75.850  26.533  1.00 49.19  ? 382  ASN A ND2 1 
ATOM   2017 N N   . SER A 1 288 ? 14.828  71.558  28.758  1.00 51.00  ? 383  SER A N   1 
ATOM   2018 C CA  . SER A 1 288 ? 13.573  71.005  29.251  1.00 48.50  ? 383  SER A CA  1 
ATOM   2019 C C   . SER A 1 288 ? 13.767  70.023  30.395  1.00 51.37  ? 383  SER A C   1 
ATOM   2020 O O   . SER A 1 288 ? 12.774  69.535  30.947  1.00 50.61  ? 383  SER A O   1 
ATOM   2021 C CB  . SER A 1 288 ? 12.818  70.296  28.126  1.00 48.59  ? 383  SER A CB  1 
ATOM   2022 O OG  . SER A 1 288 ? 12.407  71.212  27.135  1.00 51.74  ? 383  SER A OG  1 
ATOM   2023 N N   . GLY A 1 289 ? 15.009  69.710  30.747  1.00 50.58  ? 384  GLY A N   1 
ATOM   2024 C CA  . GLY A 1 289 ? 15.297  68.791  31.824  1.00 47.87  ? 384  GLY A CA  1 
ATOM   2025 C C   . GLY A 1 289 ? 15.637  67.370  31.411  1.00 49.70  ? 384  GLY A C   1 
ATOM   2026 O O   . GLY A 1 289 ? 15.717  66.505  32.289  1.00 47.92  ? 384  GLY A O   1 
ATOM   2027 N N   . PHE A 1 290 ? 15.843  67.097  30.111  1.00 47.07  ? 385  PHE A N   1 
ATOM   2028 C CA  . PHE A 1 290 ? 16.128  65.729  29.673  1.00 46.77  ? 385  PHE A CA  1 
ATOM   2029 C C   . PHE A 1 290 ? 17.516  65.254  30.091  1.00 47.13  ? 385  PHE A C   1 
ATOM   2030 O O   . PHE A 1 290 ? 17.776  64.045  30.039  1.00 47.88  ? 385  PHE A O   1 
ATOM   2031 C CB  . PHE A 1 290 ? 16.008  65.591  28.149  1.00 47.23  ? 385  PHE A CB  1 
ATOM   2032 C CG  . PHE A 1 290 ? 14.587  65.559  27.619  1.00 48.58  ? 385  PHE A CG  1 
ATOM   2033 C CD1 . PHE A 1 290 ? 14.338  65.133  26.320  1.00 51.68  ? 385  PHE A CD1 1 
ATOM   2034 C CD2 . PHE A 1 290 ? 13.518  65.956  28.394  1.00 49.87  ? 385  PHE A CD2 1 
ATOM   2035 C CE1 . PHE A 1 290 ? 13.039  65.103  25.818  1.00 52.32  ? 385  PHE A CE1 1 
ATOM   2036 C CE2 . PHE A 1 290 ? 12.219  65.933  27.895  1.00 50.07  ? 385  PHE A CE2 1 
ATOM   2037 C CZ  . PHE A 1 290 ? 11.974  65.512  26.625  1.00 46.40  ? 385  PHE A CZ  1 
ATOM   2038 N N   . ASP A 1 291 ? 18.421  66.178  30.431  1.00 44.60  ? 386  ASP A N   1 
ATOM   2039 C CA  . ASP A 1 291 ? 19.717  65.902  31.061  1.00 48.14  ? 386  ASP A CA  1 
ATOM   2040 C C   . ASP A 1 291 ? 20.750  65.253  30.139  1.00 48.03  ? 386  ASP A C   1 
ATOM   2041 O O   . ASP A 1 291 ? 21.882  65.751  30.053  1.00 49.07  ? 386  ASP A O   1 
ATOM   2042 C CB  . ASP A 1 291 ? 19.539  65.043  32.320  1.00 48.54  ? 386  ASP A CB  1 
ATOM   2043 C CG  . ASP A 1 291 ? 20.762  65.092  33.226  1.00 53.80  ? 386  ASP A CG  1 
ATOM   2044 O OD1 . ASP A 1 291 ? 21.508  64.086  33.289  1.00 54.65  ? 386  ASP A OD1 1 
ATOM   2045 O OD2 . ASP A 1 291 ? 21.003  66.160  33.843  1.00 53.26  ? 386  ASP A OD2 1 
ATOM   2046 N N   . ARG A 1 292 ? 20.396  64.154  29.460  1.00 43.41  ? 387  ARG A N   1 
ATOM   2047 C CA  . ARG A 1 292 ? 21.312  63.453  28.555  1.00 43.85  ? 387  ARG A CA  1 
ATOM   2048 C C   . ARG A 1 292 ? 20.531  62.943  27.362  1.00 44.38  ? 387  ARG A C   1 
ATOM   2049 O O   . ARG A 1 292 ? 19.666  62.076  27.519  1.00 42.55  ? 387  ARG A O   1 
ATOM   2050 C CB  . ARG A 1 292 ? 22.019  62.281  29.245  1.00 43.83  ? 387  ARG A CB  1 
ATOM   2051 C CG  . ARG A 1 292 ? 22.916  62.685  30.386  1.00 46.69  ? 387  ARG A CG  1 
ATOM   2052 C CD  . ARG A 1 292 ? 23.622  61.506  31.032  1.00 47.46  ? 387  ARG A CD  1 
ATOM   2053 N NE  . ARG A 1 292 ? 24.601  62.026  31.976  1.00 49.60  ? 387  ARG A NE  1 
ATOM   2054 C CZ  . ARG A 1 292 ? 25.642  61.355  32.442  1.00 51.68  ? 387  ARG A CZ  1 
ATOM   2055 N NH1 . ARG A 1 292 ? 25.835  60.080  32.138  1.00 51.11  ? 387  ARG A NH1 1 
ATOM   2056 N NH2 . ARG A 1 292 ? 26.516  61.981  33.229  1.00 48.72  ? 387  ARG A NH2 1 
ATOM   2057 N N   . VAL A 1 293 ? 20.841  63.459  26.170  1.00 42.40  ? 388  VAL A N   1 
ATOM   2058 C CA  . VAL A 1 293 ? 20.130  63.080  24.955  1.00 41.70  ? 388  VAL A CA  1 
ATOM   2059 C C   . VAL A 1 293 ? 21.124  62.776  23.842  1.00 42.42  ? 388  VAL A C   1 
ATOM   2060 O O   . VAL A 1 293 ? 22.225  63.343  23.779  1.00 41.52  ? 388  VAL A O   1 
ATOM   2061 C CB  . VAL A 1 293 ? 19.152  64.187  24.498  1.00 44.90  ? 388  VAL A CB  1 
ATOM   2062 C CG1 . VAL A 1 293 ? 18.115  64.467  25.579  1.00 39.19  ? 388  VAL A CG1 1 
ATOM   2063 C CG2 . VAL A 1 293 ? 19.924  65.466  24.133  1.00 40.91  ? 388  VAL A CG2 1 
ATOM   2064 N N   . PHE A 1 294 ? 20.716  61.882  22.943  1.00 40.11  ? 389  PHE A N   1 
ATOM   2065 C CA  . PHE A 1 294 ? 21.430  61.680  21.698  1.00 38.52  ? 389  PHE A CA  1 
ATOM   2066 C C   . PHE A 1 294 ? 20.413  61.494  20.582  1.00 41.32  ? 389  PHE A C   1 
ATOM   2067 O O   . PHE A 1 294 ? 19.261  61.112  20.812  1.00 40.53  ? 389  PHE A O   1 
ATOM   2068 C CB  . PHE A 1 294 ? 22.381  60.475  21.768  1.00 41.33  ? 389  PHE A CB  1 
ATOM   2069 C CG  . PHE A 1 294 ? 21.682  59.142  21.838  1.00 40.60  ? 389  PHE A CG  1 
ATOM   2070 C CD1 . PHE A 1 294 ? 21.299  58.475  20.683  1.00 43.86  ? 389  PHE A CD1 1 
ATOM   2071 C CD2 . PHE A 1 294 ? 21.436  58.543  23.060  1.00 40.42  ? 389  PHE A CD2 1 
ATOM   2072 C CE1 . PHE A 1 294 ? 20.669  57.243  20.744  1.00 43.19  ? 389  PHE A CE1 1 
ATOM   2073 C CE2 . PHE A 1 294 ? 20.807  57.313  23.134  1.00 42.88  ? 389  PHE A CE2 1 
ATOM   2074 C CZ  . PHE A 1 294 ? 20.413  56.666  21.972  1.00 44.02  ? 389  PHE A CZ  1 
ATOM   2075 N N   . GLU A 1 295 ? 20.863  61.765  19.365  1.00 39.33  ? 390  GLU A N   1 
ATOM   2076 C CA  . GLU A 1 295 ? 20.066  61.553  18.166  1.00 39.47  ? 390  GLU A CA  1 
ATOM   2077 C C   . GLU A 1 295 ? 20.954  60.918  17.108  1.00 41.97  ? 390  GLU A C   1 
ATOM   2078 O O   . GLU A 1 295 ? 22.135  61.258  17.000  1.00 41.81  ? 390  GLU A O   1 
ATOM   2079 C CB  . GLU A 1 295 ? 19.463  62.872  17.642  1.00 39.97  ? 390  GLU A CB  1 
ATOM   2080 C CG  . GLU A 1 295 ? 18.519  62.672  16.458  1.00 40.11  ? 390  GLU A CG  1 
ATOM   2081 C CD  . GLU A 1 295 ? 17.578  63.848  16.224  1.00 44.29  ? 390  GLU A CD  1 
ATOM   2082 O OE1 . GLU A 1 295 ? 17.703  64.876  16.941  1.00 42.24  ? 390  GLU A OE1 1 
ATOM   2083 O OE2 . GLU A 1 295 ? 16.707  63.737  15.316  1.00 41.24  ? 390  GLU A OE2 1 
ATOM   2084 N N   . VAL A 1 296 ? 20.397  59.975  16.352  1.00 40.90  ? 391  VAL A N   1 
ATOM   2085 C CA  . VAL A 1 296 ? 21.051  59.378  15.181  1.00 40.22  ? 391  VAL A CA  1 
ATOM   2086 C C   . VAL A 1 296 ? 20.117  59.639  14.010  1.00 40.41  ? 391  VAL A C   1 
ATOM   2087 O O   . VAL A 1 296 ? 19.016  59.072  13.968  1.00 37.95  ? 391  VAL A O   1 
ATOM   2088 C CB  . VAL A 1 296 ? 21.302  57.872  15.364  1.00 40.73  ? 391  VAL A CB  1 
ATOM   2089 C CG1 . VAL A 1 296 ? 21.888  57.250  14.082  1.00 38.09  ? 391  VAL A CG1 1 
ATOM   2090 C CG2 . VAL A 1 296 ? 22.229  57.632  16.545  1.00 39.20  ? 391  VAL A CG2 1 
ATOM   2091 N N   . ALA A 1 297 ? 20.505  60.519  13.090  1.00 39.21  ? 392  ALA A N   1 
ATOM   2092 C CA  . ALA A 1 297 ? 19.497  61.023  12.158  1.00 40.30  ? 392  ALA A CA  1 
ATOM   2093 C C   . ALA A 1 297 ? 20.186  61.720  10.984  1.00 38.87  ? 392  ALA A C   1 
ATOM   2094 O O   . ALA A 1 297 ? 21.319  62.199  11.118  1.00 40.71  ? 392  ALA A O   1 
ATOM   2095 C CB  . ALA A 1 297 ? 18.521  61.991  12.859  1.00 36.95  ? 392  ALA A CB  1 
ATOM   2096 N N   . PRO A 1 298 ? 19.509  61.797  9.833   1.00 38.76  ? 393  PRO A N   1 
ATOM   2097 C CA  . PRO A 1 298 ? 20.066  62.519  8.681   1.00 40.97  ? 393  PRO A CA  1 
ATOM   2098 C C   . PRO A 1 298 ? 20.221  64.008  8.946   1.00 41.18  ? 393  PRO A C   1 
ATOM   2099 O O   . PRO A 1 298 ? 19.497  64.605  9.748   1.00 40.12  ? 393  PRO A O   1 
ATOM   2100 C CB  . PRO A 1 298 ? 19.035  62.287  7.567   1.00 41.37  ? 393  PRO A CB  1 
ATOM   2101 C CG  . PRO A 1 298 ? 18.112  61.243  8.048   1.00 40.82  ? 393  PRO A CG  1 
ATOM   2102 C CD  . PRO A 1 298 ? 18.179  61.232  9.543   1.00 41.16  ? 393  PRO A CD  1 
ATOM   2103 N N   . VAL A 1 299 ? 21.199  64.594  8.254   1.00 40.00  ? 394  VAL A N   1 
ATOM   2104 C CA  . VAL A 1 299 ? 21.363  66.035  8.130   1.00 40.54  ? 394  VAL A CA  1 
ATOM   2105 C C   . VAL A 1 299 ? 21.701  66.322  6.673   1.00 43.22  ? 394  VAL A C   1 
ATOM   2106 O O   . VAL A 1 299 ? 22.174  65.448  5.927   1.00 43.70  ? 394  VAL A O   1 
ATOM   2107 C CB  . VAL A 1 299 ? 22.451  66.612  9.068   1.00 43.70  ? 394  VAL A CB  1 
ATOM   2108 C CG1 . VAL A 1 299 ? 22.101  66.361  10.539  1.00 41.52  ? 394  VAL A CG1 1 
ATOM   2109 C CG2 . VAL A 1 299 ? 23.828  66.032  8.739   1.00 43.65  ? 394  VAL A CG2 1 
ATOM   2110 N N   . PHE A 1 300 ? 21.462  67.573  6.281   1.00 40.56  ? 395  PHE A N   1 
ATOM   2111 C CA  . PHE A 1 300 ? 21.450  67.992  4.885   1.00 44.40  ? 395  PHE A CA  1 
ATOM   2112 C C   . PHE A 1 300 ? 22.248  69.278  4.727   1.00 48.98  ? 395  PHE A C   1 
ATOM   2113 O O   . PHE A 1 300 ? 21.962  70.270  5.407   1.00 45.89  ? 395  PHE A O   1 
ATOM   2114 C CB  . PHE A 1 300 ? 20.008  68.210  4.408   1.00 43.37  ? 395  PHE A CB  1 
ATOM   2115 C CG  . PHE A 1 300 ? 19.087  67.060  4.729   1.00 46.35  ? 395  PHE A CG  1 
ATOM   2116 C CD1 . PHE A 1 300 ? 18.880  66.038  3.808   1.00 44.80  ? 395  PHE A CD1 1 
ATOM   2117 C CD2 . PHE A 1 300 ? 18.436  66.992  5.955   1.00 45.85  ? 395  PHE A CD2 1 
ATOM   2118 C CE1 . PHE A 1 300 ? 18.042  64.981  4.102   1.00 44.42  ? 395  PHE A CE1 1 
ATOM   2119 C CE2 . PHE A 1 300 ? 17.592  65.931  6.259   1.00 42.17  ? 395  PHE A CE2 1 
ATOM   2120 C CZ  . PHE A 1 300 ? 17.395  64.922  5.335   1.00 42.71  ? 395  PHE A CZ  1 
ATOM   2121 N N   . ARG A 1 301 ? 23.224  69.266  3.808   1.00 44.82  ? 396  ARG A N   1 
ATOM   2122 C CA  . ARG A 1 301 ? 24.150  70.367  3.557   1.00 47.91  ? 396  ARG A CA  1 
ATOM   2123 C C   . ARG A 1 301 ? 24.115  70.717  2.076   1.00 52.00  ? 396  ARG A C   1 
ATOM   2124 O O   . ARG A 1 301 ? 24.308  69.836  1.234   1.00 51.76  ? 396  ARG A O   1 
ATOM   2125 C CB  . ARG A 1 301 ? 25.582  69.978  3.925   1.00 52.89  ? 396  ARG A CB  1 
ATOM   2126 C CG  . ARG A 1 301 ? 26.018  70.285  5.314   1.00 57.30  ? 396  ARG A CG  1 
ATOM   2127 C CD  . ARG A 1 301 ? 27.496  69.931  5.505   1.00 60.04  ? 396  ARG A CD  1 
ATOM   2128 N NE  . ARG A 1 301 ? 28.385  71.008  5.091   1.00 62.53  ? 396  ARG A NE  1 
ATOM   2129 N N   . ALA A 1 302 ? 23.916  71.995  1.749   1.00 53.96  ? 397  ALA A N   1 
ATOM   2130 C CA  . ALA A 1 302 ? 23.725  72.397  0.359   1.00 55.39  ? 397  ALA A CA  1 
ATOM   2131 C C   . ALA A 1 302 ? 24.950  73.074  -0.266  1.00 57.02  ? 397  ALA A C   1 
ATOM   2132 O O   . ALA A 1 302 ? 24.823  73.684  -1.333  1.00 60.18  ? 397  ALA A O   1 
ATOM   2133 C CB  . ALA A 1 302 ? 22.505  73.314  0.241   1.00 55.49  ? 397  ALA A CB  1 
ATOM   2134 N N   . GLU A 1 303 ? 26.122  72.946  0.315   1.00 54.43  ? 398  GLU A N   1 
ATOM   2135 C CA  . GLU A 1 303 ? 27.292  73.542  -0.289  1.00 58.48  ? 398  GLU A CA  1 
ATOM   2136 C C   . GLU A 1 303 ? 27.631  72.860  -1.589  1.00 57.99  ? 398  GLU A C   1 
ATOM   2137 O O   . GLU A 1 303 ? 27.601  71.663  -1.674  1.00 55.70  ? 398  GLU A O   1 
ATOM   2138 C CB  . GLU A 1 303 ? 28.494  73.412  0.607   1.00 61.83  ? 398  GLU A CB  1 
ATOM   2139 C CG  . GLU A 1 303 ? 28.198  73.510  2.072   1.00 71.54  ? 398  GLU A CG  1 
ATOM   2140 C CD  . GLU A 1 303 ? 29.406  73.157  2.895   1.00 79.21  ? 398  GLU A CD  1 
ATOM   2141 N N   . ASN A 1 304 ? 28.005  73.635  -2.588  1.00 57.91  ? 399  ASN A N   1 
ATOM   2142 C CA  . ASN A 1 304 ? 28.348  73.091  -3.904  1.00 59.03  ? 399  ASN A CA  1 
ATOM   2143 C C   . ASN A 1 304 ? 29.826  72.699  -3.924  1.00 57.12  ? 399  ASN A C   1 
ATOM   2144 O O   . ASN A 1 304 ? 30.678  73.339  -4.542  1.00 59.30  ? 399  ASN A O   1 
ATOM   2145 C CB  . ASN A 1 304 ? 28.016  74.087  -5.003  1.00 56.05  ? 399  ASN A CB  1 
ATOM   2146 C CG  . ASN A 1 304 ? 28.056  73.454  -6.377  1.00 61.44  ? 399  ASN A CG  1 
ATOM   2147 O OD1 . ASN A 1 304 ? 28.564  72.341  -6.548  1.00 61.86  ? 399  ASN A OD1 1 
ATOM   2148 N ND2 . ASN A 1 304 ? 27.519  74.155  -7.366  1.00 64.20  ? 399  ASN A ND2 1 
ATOM   2149 N N   . SER A 1 305 ? 30.113  71.599  -3.243  1.00 57.36  ? 400  SER A N   1 
ATOM   2150 C CA  . SER A 1 305 ? 31.468  71.130  -3.005  1.00 57.25  ? 400  SER A CA  1 
ATOM   2151 C C   . SER A 1 305 ? 31.575  69.696  -3.510  1.00 57.64  ? 400  SER A C   1 
ATOM   2152 O O   . SER A 1 305 ? 30.742  68.855  -3.160  1.00 52.14  ? 400  SER A O   1 
ATOM   2153 C CB  . SER A 1 305 ? 31.797  71.220  -1.510  1.00 59.27  ? 400  SER A CB  1 
ATOM   2154 O OG  . SER A 1 305 ? 33.136  70.866  -1.237  1.00 62.29  ? 400  SER A OG  1 
ATOM   2155 N N   . ASN A 1 306 ? 32.573  69.427  -4.355  1.00 56.09  ? 401  ASN A N   1 
ATOM   2156 C CA  . ASN A 1 306 ? 32.785  68.107  -4.960  1.00 56.83  ? 401  ASN A CA  1 
ATOM   2157 C C   . ASN A 1 306 ? 34.162  67.619  -4.531  1.00 58.49  ? 401  ASN A C   1 
ATOM   2158 O O   . ASN A 1 306 ? 35.166  67.919  -5.186  1.00 54.44  ? 401  ASN A O   1 
ATOM   2159 C CB  . ASN A 1 306 ? 32.655  68.168  -6.487  1.00 51.68  ? 401  ASN A CB  1 
ATOM   2160 C CG  . ASN A 1 306 ? 31.210  68.307  -6.935  1.00 58.25  ? 401  ASN A CG  1 
ATOM   2161 O OD1 . ASN A 1 306 ? 30.411  67.389  -6.750  1.00 55.92  ? 401  ASN A OD1 1 
ATOM   2162 N ND2 . ASN A 1 306 ? 30.863  69.457  -7.510  1.00 56.81  ? 401  ASN A ND2 1 
ATOM   2163 N N   . THR A 1 307 ? 34.214  66.896  -3.409  1.00 53.23  ? 402  THR A N   1 
ATOM   2164 C CA  . THR A 1 307 ? 35.478  66.410  -2.875  1.00 54.59  ? 402  THR A CA  1 
ATOM   2165 C C   . THR A 1 307 ? 35.330  64.959  -2.437  1.00 55.53  ? 402  THR A C   1 
ATOM   2166 O O   . THR A 1 307 ? 34.227  64.410  -2.359  1.00 52.67  ? 402  THR A O   1 
ATOM   2167 C CB  . THR A 1 307 ? 35.975  67.250  -1.682  1.00 55.35  ? 402  THR A CB  1 
ATOM   2168 O OG1 . THR A 1 307 ? 35.168  66.972  -0.529  1.00 51.75  ? 402  THR A OG1 1 
ATOM   2169 C CG2 . THR A 1 307 ? 35.947  68.762  -2.000  1.00 54.42  ? 402  THR A CG2 1 
ATOM   2170 N N   . TYR A 1 308 ? 36.475  64.351  -2.120  1.00 52.87  ? 403  TYR A N   1 
ATOM   2171 C CA  . TYR A 1 308 ? 36.514  62.987  -1.614  1.00 51.38  ? 403  TYR A CA  1 
ATOM   2172 C C   . TYR A 1 308 ? 35.793  62.822  -0.275  1.00 52.46  ? 403  TYR A C   1 
ATOM   2173 O O   . TYR A 1 308 ? 35.576  61.678  0.145   1.00 49.80  ? 403  TYR A O   1 
ATOM   2174 C CB  . TYR A 1 308 ? 37.982  62.532  -1.476  1.00 52.54  ? 403  TYR A CB  1 
ATOM   2175 C CG  . TYR A 1 308 ? 38.613  63.066  -0.220  1.00 56.20  ? 403  TYR A CG  1 
ATOM   2176 C CD1 . TYR A 1 308 ? 38.697  62.283  0.928   1.00 55.52  ? 403  TYR A CD1 1 
ATOM   2177 C CD2 . TYR A 1 308 ? 39.081  64.372  -0.161  1.00 56.88  ? 403  TYR A CD2 1 
ATOM   2178 C CE1 . TYR A 1 308 ? 39.243  62.782  2.097   1.00 57.25  ? 403  TYR A CE1 1 
ATOM   2179 C CE2 . TYR A 1 308 ? 39.632  64.883  1.007   1.00 58.92  ? 403  TYR A CE2 1 
ATOM   2180 C CZ  . TYR A 1 308 ? 39.709  64.086  2.133   1.00 60.45  ? 403  TYR A CZ  1 
ATOM   2181 O OH  . TYR A 1 308 ? 40.253  64.591  3.300   1.00 57.93  ? 403  TYR A OH  1 
ATOM   2182 N N   . ARG A 1 309 ? 35.448  63.900  0.408   1.00 49.75  ? 404  ARG A N   1 
ATOM   2183 C CA  . ARG A 1 309 ? 34.797  63.747  1.698   1.00 53.27  ? 404  ARG A CA  1 
ATOM   2184 C C   . ARG A 1 309 ? 33.512  64.488  1.988   1.00 52.57  ? 404  ARG A C   1 
ATOM   2185 O O   . ARG A 1 309 ? 32.991  64.368  3.052   1.00 54.47  ? 404  ARG A O   1 
ATOM   2186 C CB  . ARG A 1 309 ? 35.769  64.051  2.818   1.00 58.49  ? 404  ARG A CB  1 
ATOM   2187 C CG  . ARG A 1 309 ? 36.312  65.449  2.819   1.00 61.81  ? 404  ARG A CG  1 
ATOM   2188 C CD  . ARG A 1 309 ? 37.282  65.639  3.965   1.00 69.91  ? 404  ARG A CD  1 
ATOM   2189 N NE  . ARG A 1 309 ? 36.786  66.495  5.032   1.00 72.30  ? 404  ARG A NE  1 
ATOM   2190 C CZ  . ARG A 1 309 ? 37.471  66.758  6.131   1.00 72.00  ? 404  ARG A CZ  1 
ATOM   2191 N NH1 . ARG A 1 309 ? 38.656  66.223  6.305   1.00 67.90  ? 404  ARG A NH1 1 
ATOM   2192 N NH2 . ARG A 1 309 ? 36.980  67.550  7.053   1.00 74.41  ? 404  ARG A NH2 1 
ATOM   2193 N N   . HIS A 1 310 ? 32.984  65.219  1.044   1.00 51.63  ? 405  HIS A N   1 
ATOM   2194 C CA  . HIS A 1 310 ? 31.777  65.996  1.288   1.00 51.69  ? 405  HIS A CA  1 
ATOM   2195 C C   . HIS A 1 310 ? 30.556  65.285  0.718   1.00 47.27  ? 405  HIS A C   1 
ATOM   2196 O O   . HIS A 1 310 ? 30.537  64.912  -0.460  1.00 47.50  ? 405  HIS A O   1 
ATOM   2197 C CB  . HIS A 1 310 ? 31.886  67.402  0.684   1.00 53.56  ? 405  HIS A CB  1 
ATOM   2198 C CG  . HIS A 1 310 ? 30.649  68.225  0.885   1.00 57.68  ? 405  HIS A CG  1 
ATOM   2199 N ND1 . HIS A 1 310 ? 30.386  68.896  2.061   1.00 60.00  ? 405  HIS A ND1 1 
ATOM   2200 C CD2 . HIS A 1 310 ? 29.579  68.443  0.080   1.00 55.78  ? 405  HIS A CD2 1 
ATOM   2201 C CE1 . HIS A 1 310 ? 29.216  69.508  1.965   1.00 58.84  ? 405  HIS A CE1 1 
ATOM   2202 N NE2 . HIS A 1 310 ? 28.707  69.250  0.774   1.00 57.82  ? 405  HIS A NE2 1 
ATOM   2203 N N   . LEU A 1 311 ? 29.536  65.104  1.550   1.00 47.90  ? 406  LEU A N   1 
ATOM   2204 C CA  . LEU A 1 311 ? 28.238  64.628  1.093   1.00 47.17  ? 406  LEU A CA  1 
ATOM   2205 C C   . LEU A 1 311 ? 27.183  65.694  1.375   1.00 48.45  ? 406  LEU A C   1 
ATOM   2206 O O   . LEU A 1 311 ? 27.279  66.418  2.372   1.00 44.47  ? 406  LEU A O   1 
ATOM   2207 C CB  . LEU A 1 311 ? 27.864  63.310  1.783   1.00 42.78  ? 406  LEU A CB  1 
ATOM   2208 C CG  . LEU A 1 311 ? 28.776  62.115  1.469   1.00 43.65  ? 406  LEU A CG  1 
ATOM   2209 C CD1 . LEU A 1 311 ? 28.425  60.912  2.362   1.00 44.38  ? 406  LEU A CD1 1 
ATOM   2210 C CD2 . LEU A 1 311 ? 28.716  61.734  -0.010  1.00 45.29  ? 406  LEU A CD2 1 
ATOM   2211 N N   . CYS A 1 312 ? 26.184  65.802  0.488   1.00 42.85  ? 407  CYS A N   1 
ATOM   2212 C CA  . CYS A 1 312 ? 25.077  66.722  0.731   1.00 43.83  ? 407  CYS A CA  1 
ATOM   2213 C C   . CYS A 1 312 ? 24.074  66.182  1.746   1.00 46.28  ? 407  CYS A C   1 
ATOM   2214 O O   . CYS A 1 312 ? 23.274  66.950  2.285   1.00 40.66  ? 407  CYS A O   1 
ATOM   2215 C CB  . CYS A 1 312 ? 24.349  67.034  -0.570  1.00 44.54  ? 407  CYS A CB  1 
ATOM   2216 S SG  . CYS A 1 312 ? 25.375  67.854  -1.782  1.00 50.78  ? 407  CYS A SG  1 
ATOM   2217 N N   . GLU A 1 313 ? 24.091  64.878  1.995   1.00 41.24  ? 408  GLU A N   1 
ATOM   2218 C CA  . GLU A 1 313 ? 23.224  64.247  2.969   1.00 40.88  ? 408  GLU A CA  1 
ATOM   2219 C C   . GLU A 1 313 ? 24.036  63.179  3.676   1.00 42.61  ? 408  GLU A C   1 
ATOM   2220 O O   . GLU A 1 313 ? 24.701  62.373  3.017   1.00 42.58  ? 408  GLU A O   1 
ATOM   2221 C CB  . GLU A 1 313 ? 21.992  63.614  2.308   1.00 42.31  ? 408  GLU A CB  1 
ATOM   2222 C CG  . GLU A 1 313 ? 21.225  62.717  3.274   1.00 45.54  ? 408  GLU A CG  1 
ATOM   2223 C CD  . GLU A 1 313 ? 19.928  62.153  2.698   1.00 48.69  ? 408  GLU A CD  1 
ATOM   2224 O OE1 . GLU A 1 313 ? 19.235  61.441  3.456   1.00 45.20  ? 408  GLU A OE1 1 
ATOM   2225 O OE2 . GLU A 1 313 ? 19.604  62.413  1.506   1.00 46.57  ? 408  GLU A OE2 1 
ATOM   2226 N N   . TYR A 1 314 ? 23.990  63.164  5.004   1.00 41.01  ? 409  TYR A N   1 
ATOM   2227 C CA  . TYR A 1 314 ? 24.714  62.126  5.728   1.00 40.97  ? 409  TYR A CA  1 
ATOM   2228 C C   . TYR A 1 314 ? 24.030  61.917  7.070   1.00 41.13  ? 409  TYR A C   1 
ATOM   2229 O O   . TYR A 1 314 ? 23.006  62.536  7.360   1.00 42.59  ? 409  TYR A O   1 
ATOM   2230 C CB  . TYR A 1 314 ? 26.213  62.466  5.856   1.00 40.70  ? 409  TYR A CB  1 
ATOM   2231 C CG  . TYR A 1 314 ? 26.549  63.735  6.633   1.00 42.44  ? 409  TYR A CG  1 
ATOM   2232 C CD1 . TYR A 1 314 ? 26.884  63.674  7.976   1.00 44.94  ? 409  TYR A CD1 1 
ATOM   2233 C CD2 . TYR A 1 314 ? 26.540  64.985  6.019   1.00 44.86  ? 409  TYR A CD2 1 
ATOM   2234 C CE1 . TYR A 1 314 ? 27.197  64.823  8.697   1.00 47.17  ? 409  TYR A CE1 1 
ATOM   2235 C CE2 . TYR A 1 314 ? 26.848  66.150  6.742   1.00 46.06  ? 409  TYR A CE2 1 
ATOM   2236 C CZ  . TYR A 1 314 ? 27.177  66.048  8.076   1.00 47.56  ? 409  TYR A CZ  1 
ATOM   2237 O OH  . TYR A 1 314 ? 27.489  67.166  8.813   1.00 58.20  ? 409  TYR A OH  1 
ATOM   2238 N N   . VAL A 1 315 ? 24.573  61.002  7.874   1.00 38.58  ? 410  VAL A N   1 
ATOM   2239 C CA  . VAL A 1 315 ? 23.997  60.637  9.163   1.00 35.86  ? 410  VAL A CA  1 
ATOM   2240 C C   . VAL A 1 315 ? 24.849  61.257  10.256  1.00 41.73  ? 410  VAL A C   1 
ATOM   2241 O O   . VAL A 1 315 ? 26.073  61.049  10.302  1.00 38.08  ? 410  VAL A O   1 
ATOM   2242 C CB  . VAL A 1 315 ? 23.901  59.115  9.339   1.00 39.91  ? 410  VAL A CB  1 
ATOM   2243 C CG1 . VAL A 1 315 ? 23.449  58.756  10.790  1.00 38.84  ? 410  VAL A CG1 1 
ATOM   2244 C CG2 . VAL A 1 315 ? 22.934  58.524  8.309   1.00 38.05  ? 410  VAL A CG2 1 
ATOM   2245 N N   . SER A 1 316 ? 24.207  62.040  11.118  1.00 37.85  ? 411  SER A N   1 
ATOM   2246 C CA  . SER A 1 316 ? 24.864  62.680  12.244  1.00 41.56  ? 411  SER A CA  1 
ATOM   2247 C C   . SER A 1 316 ? 24.512  61.941  13.525  1.00 39.85  ? 411  SER A C   1 
ATOM   2248 O O   . SER A 1 316 ? 23.344  61.597  13.757  1.00 38.85  ? 411  SER A O   1 
ATOM   2249 C CB  . SER A 1 316 ? 24.465  64.151  12.364  1.00 43.12  ? 411  SER A CB  1 
ATOM   2250 O OG  . SER A 1 316 ? 25.239  64.811  13.364  1.00 45.07  ? 411  SER A OG  1 
ATOM   2251 N N   . LEU A 1 317 ? 25.544  61.651  14.314  1.00 39.17  ? 412  LEU A N   1 
ATOM   2252 C CA  . LEU A 1 317 ? 25.410  61.160  15.673  1.00 43.14  ? 412  LEU A CA  1 
ATOM   2253 C C   . LEU A 1 317 ? 25.596  62.372  16.587  1.00 43.50  ? 412  LEU A C   1 
ATOM   2254 O O   . LEU A 1 317 ? 26.668  62.977  16.616  1.00 42.80  ? 412  LEU A O   1 
ATOM   2255 C CB  . LEU A 1 317 ? 26.441  60.066  15.955  1.00 41.26  ? 412  LEU A CB  1 
ATOM   2256 C CG  . LEU A 1 317 ? 26.763  59.048  14.856  1.00 42.51  ? 412  LEU A CG  1 
ATOM   2257 C CD1 . LEU A 1 317 ? 27.900  58.143  15.316  1.00 41.96  ? 412  LEU A CD1 1 
ATOM   2258 C CD2 . LEU A 1 317 ? 25.539  58.215  14.464  1.00 37.16  ? 412  LEU A CD2 1 
ATOM   2259 N N   . ASP A 1 318 ? 24.551  62.749  17.301  1.00 43.05  ? 413  ASP A N   1 
ATOM   2260 C CA  . ASP A 1 318 ? 24.564  63.964  18.100  1.00 45.03  ? 413  ASP A CA  1 
ATOM   2261 C C   . ASP A 1 318 ? 24.372  63.617  19.560  1.00 43.81  ? 413  ASP A C   1 
ATOM   2262 O O   . ASP A 1 318 ? 23.553  62.756  19.897  1.00 43.23  ? 413  ASP A O   1 
ATOM   2263 C CB  . ASP A 1 318 ? 23.485  64.930  17.654  1.00 38.87  ? 413  ASP A CB  1 
ATOM   2264 C CG  . ASP A 1 318 ? 23.895  65.709  16.444  1.00 47.32  ? 413  ASP A CG  1 
ATOM   2265 O OD1 . ASP A 1 318 ? 23.603  65.237  15.313  1.00 44.31  ? 413  ASP A OD1 1 
ATOM   2266 O OD2 . ASP A 1 318 ? 24.522  66.789  16.628  1.00 46.41  ? 413  ASP A OD2 1 
ATOM   2267 N N   . VAL A 1 319 ? 25.154  64.278  20.412  1.00 44.79  ? 414  VAL A N   1 
ATOM   2268 C CA  . VAL A 1 319 ? 25.077  64.115  21.858  1.00 43.38  ? 414  VAL A CA  1 
ATOM   2269 C C   . VAL A 1 319 ? 24.945  65.496  22.478  1.00 45.52  ? 414  VAL A C   1 
ATOM   2270 O O   . VAL A 1 319 ? 25.568  66.455  22.002  1.00 46.11  ? 414  VAL A O   1 
ATOM   2271 C CB  . VAL A 1 319 ? 26.322  63.398  22.424  1.00 46.01  ? 414  VAL A CB  1 
ATOM   2272 C CG1 . VAL A 1 319 ? 26.097  63.028  23.877  1.00 42.36  ? 414  VAL A CG1 1 
ATOM   2273 C CG2 . VAL A 1 319 ? 26.675  62.155  21.582  1.00 43.11  ? 414  VAL A CG2 1 
ATOM   2274 N N   . GLU A 1 320 ? 24.139  65.594  23.541  1.00 44.99  ? 415  GLU A N   1 
ATOM   2275 C CA  . GLU A 1 320 ? 24.051  66.803  24.349  1.00 44.31  ? 415  GLU A CA  1 
ATOM   2276 C C   . GLU A 1 320 ? 23.766  66.381  25.786  1.00 46.92  ? 415  GLU A C   1 
ATOM   2277 O O   . GLU A 1 320 ? 22.970  65.460  26.027  1.00 43.17  ? 415  GLU A O   1 
ATOM   2278 C CB  . GLU A 1 320 ? 22.967  67.760  23.830  1.00 43.52  ? 415  GLU A CB  1 
ATOM   2279 C CG  . GLU A 1 320 ? 23.115  69.235  24.279  1.00 43.81  ? 415  GLU A CG  1 
ATOM   2280 C CD  . GLU A 1 320 ? 24.080  70.039  23.401  1.00 47.47  ? 415  GLU A CD  1 
ATOM   2281 O OE1 . GLU A 1 320 ? 24.494  69.554  22.316  1.00 44.35  ? 415  GLU A OE1 1 
ATOM   2282 O OE2 . GLU A 1 320 ? 24.434  71.168  23.804  1.00 46.28  ? 415  GLU A OE2 1 
ATOM   2283 N N   . MET A 1 321 ? 24.428  67.039  26.740  1.00 47.08  ? 416  MET A N   1 
ATOM   2284 C CA  . MET A 1 321 ? 24.331  66.569  28.118  1.00 46.88  ? 416  MET A CA  1 
ATOM   2285 C C   . MET A 1 321 ? 24.729  67.680  29.079  1.00 47.01  ? 416  MET A C   1 
ATOM   2286 O O   . MET A 1 321 ? 25.476  68.596  28.725  1.00 47.01  ? 416  MET A O   1 
ATOM   2287 C CB  . MET A 1 321 ? 25.216  65.337  28.346  1.00 45.48  ? 416  MET A CB  1 
ATOM   2288 C CG  . MET A 1 321 ? 26.710  65.662  28.326  1.00 45.85  ? 416  MET A CG  1 
ATOM   2289 S SD  . MET A 1 321 ? 27.805  64.217  28.260  1.00 47.56  ? 416  MET A SD  1 
ATOM   2290 C CE  . MET A 1 321 ? 27.570  63.549  29.904  1.00 43.11  ? 416  MET A CE  1 
ATOM   2291 N N   . THR A 1 322 ? 24.235  67.576  30.314  1.00 46.72  ? 417  THR A N   1 
ATOM   2292 C CA  . THR A 1 322 ? 24.638  68.522  31.342  1.00 50.62  ? 417  THR A CA  1 
ATOM   2293 C C   . THR A 1 322 ? 25.982  68.120  31.948  1.00 50.87  ? 417  THR A C   1 
ATOM   2294 O O   . THR A 1 322 ? 26.495  67.013  31.743  1.00 51.16  ? 417  THR A O   1 
ATOM   2295 C CB  . THR A 1 322 ? 23.590  68.626  32.460  1.00 52.06  ? 417  THR A CB  1 
ATOM   2296 O OG1 . THR A 1 322 ? 23.440  67.357  33.121  1.00 50.26  ? 417  THR A OG1 1 
ATOM   2297 C CG2 . THR A 1 322 ? 22.239  69.100  31.916  1.00 50.12  ? 417  THR A CG2 1 
ATOM   2298 N N   . TYR A 1 323 ? 26.520  69.034  32.734  1.00 53.59  ? 418  TYR A N   1 
ATOM   2299 C CA  . TYR A 1 323 ? 27.738  68.832  33.484  1.00 52.77  ? 418  TYR A CA  1 
ATOM   2300 C C   . TYR A 1 323 ? 27.568  69.460  34.854  1.00 55.17  ? 418  TYR A C   1 
ATOM   2301 O O   . TYR A 1 323 ? 26.753  70.318  35.027  1.00 53.33  ? 418  TYR A O   1 
ATOM   2302 C CB  . TYR A 1 323 ? 28.978  69.347  32.767  1.00 52.20  ? 418  TYR A CB  1 
ATOM   2303 C CG  . TYR A 1 323 ? 29.046  70.810  32.489  1.00 53.08  ? 418  TYR A CG  1 
ATOM   2304 C CD1 . TYR A 1 323 ? 29.545  71.685  33.417  1.00 55.86  ? 418  TYR A CD1 1 
ATOM   2305 C CD2 . TYR A 1 323 ? 28.658  71.312  31.283  1.00 52.00  ? 418  TYR A CD2 1 
ATOM   2306 C CE1 . TYR A 1 323 ? 29.620  73.028  33.155  1.00 53.63  ? 418  TYR A CE1 1 
ATOM   2307 C CE2 . TYR A 1 323 ? 28.732  72.643  31.018  1.00 52.13  ? 418  TYR A CE2 1 
ATOM   2308 C CZ  . TYR A 1 323 ? 29.217  73.498  31.958  1.00 54.58  ? 418  TYR A CZ  1 
ATOM   2309 O OH  . TYR A 1 323 ? 29.279  74.816  31.677  1.00 50.92  ? 418  TYR A OH  1 
ATOM   2310 N N   . LYS A 1 324 ? 28.251  68.937  35.849  1.00 53.87  ? 419  LYS A N   1 
ATOM   2311 C CA  . LYS A 1 324 ? 28.127  69.504  37.164  1.00 58.44  ? 419  LYS A CA  1 
ATOM   2312 C C   . LYS A 1 324 ? 28.811  70.830  37.407  1.00 59.78  ? 419  LYS A C   1 
ATOM   2313 O O   . LYS A 1 324 ? 28.160  71.793  37.698  1.00 60.25  ? 419  LYS A O   1 
ATOM   2314 C CB  . LYS A 1 324 ? 28.658  68.508  38.176  1.00 60.81  ? 419  LYS A CB  1 
ATOM   2315 C CG  . LYS A 1 324 ? 27.886  67.216  38.238  1.00 62.46  ? 419  LYS A CG  1 
ATOM   2316 C CD  . LYS A 1 324 ? 28.713  66.123  38.878  1.00 62.71  ? 419  LYS A CD  1 
ATOM   2317 C CE  . LYS A 1 324 ? 27.940  64.823  38.919  1.00 74.16  ? 419  LYS A CE  1 
ATOM   2318 N NZ  . LYS A 1 324 ? 28.720  63.689  39.463  1.00 79.31  ? 419  LYS A NZ  1 
ATOM   2319 N N   . TYR A 1 325 ? 30.101  70.930  37.140  1.00 59.83  ? 420  TYR A N   1 
ATOM   2320 C CA  . TYR A 1 325 ? 30.833  72.159  37.420  1.00 59.57  ? 420  TYR A CA  1 
ATOM   2321 C C   . TYR A 1 325 ? 31.885  72.487  36.389  1.00 60.13  ? 420  TYR A C   1 
ATOM   2322 O O   . TYR A 1 325 ? 32.275  73.612  36.263  1.00 62.39  ? 420  TYR A O   1 
ATOM   2323 C CB  . TYR A 1 325 ? 31.536  72.102  38.791  1.00 61.27  ? 420  TYR A CB  1 
ATOM   2324 C CG  . TYR A 1 325 ? 30.622  72.033  39.982  1.00 65.33  ? 420  TYR A CG  1 
ATOM   2325 C CD1 . TYR A 1 325 ? 29.756  73.051  40.254  1.00 65.52  ? 420  TYR A CD1 1 
ATOM   2326 C CD2 . TYR A 1 325 ? 30.575  70.913  40.771  1.00 65.21  ? 420  TYR A CD2 1 
ATOM   2327 C CE1 . TYR A 1 325 ? 28.895  72.977  41.303  1.00 69.60  ? 420  TYR A CE1 1 
ATOM   2328 C CE2 . TYR A 1 325 ? 29.712  70.831  41.822  1.00 67.70  ? 420  TYR A CE2 1 
ATOM   2329 C CZ  . TYR A 1 325 ? 28.880  71.871  42.072  1.00 70.83  ? 420  TYR A CZ  1 
ATOM   2330 O OH  . TYR A 1 325 ? 28.019  71.811  43.104  1.00 77.50  ? 420  TYR A OH  1 
ATOM   2331 N N   . ASP A 1 326 ? 32.334  71.495  35.646  1.00 61.36  ? 421  ASP A N   1 
ATOM   2332 C CA  . ASP A 1 326 ? 33.390  71.672  34.654  1.00 61.34  ? 421  ASP A CA  1 
ATOM   2333 C C   . ASP A 1 326 ? 32.979  70.982  33.365  1.00 57.51  ? 421  ASP A C   1 
ATOM   2334 O O   . ASP A 1 326 ? 32.675  69.789  33.378  1.00 58.36  ? 421  ASP A O   1 
ATOM   2335 C CB  . ASP A 1 326 ? 34.710  71.091  35.184  1.00 66.19  ? 421  ASP A CB  1 
ATOM   2336 C CG  . ASP A 1 326 ? 35.904  71.398  34.294  1.00 69.35  ? 421  ASP A CG  1 
ATOM   2337 O OD1 . ASP A 1 326 ? 35.734  72.003  33.213  1.00 68.13  ? 421  ASP A OD1 1 
ATOM   2338 O OD2 . ASP A 1 326 ? 37.027  71.018  34.693  1.00 72.58  ? 421  ASP A OD2 1 
ATOM   2339 N N   . TYR A 1 327 ? 32.979  71.717  32.249  1.00 58.50  ? 422  TYR A N   1 
ATOM   2340 C CA  . TYR A 1 327 ? 32.602  71.100  30.979  1.00 56.53  ? 422  TYR A CA  1 
ATOM   2341 C C   . TYR A 1 327 ? 33.570  69.995  30.568  1.00 56.77  ? 422  TYR A C   1 
ATOM   2342 O O   . TYR A 1 327 ? 33.189  69.109  29.797  1.00 53.39  ? 422  TYR A O   1 
ATOM   2343 C CB  . TYR A 1 327 ? 32.510  72.156  29.875  1.00 53.71  ? 422  TYR A CB  1 
ATOM   2344 C CG  . TYR A 1 327 ? 33.829  72.474  29.197  1.00 57.76  ? 422  TYR A CG  1 
ATOM   2345 C CD1 . TYR A 1 327 ? 34.127  71.962  27.947  1.00 53.14  ? 422  TYR A CD1 1 
ATOM   2346 C CD2 . TYR A 1 327 ? 34.776  73.293  29.810  1.00 58.74  ? 422  TYR A CD2 1 
ATOM   2347 C CE1 . TYR A 1 327 ? 35.330  72.243  27.323  1.00 55.68  ? 422  TYR A CE1 1 
ATOM   2348 C CE2 . TYR A 1 327 ? 35.989  73.581  29.189  1.00 58.96  ? 422  TYR A CE2 1 
ATOM   2349 C CZ  . TYR A 1 327 ? 36.255  73.055  27.945  1.00 57.60  ? 422  TYR A CZ  1 
ATOM   2350 O OH  . TYR A 1 327 ? 37.446  73.335  27.323  1.00 57.14  ? 422  TYR A OH  1 
ATOM   2351 N N   . LEU A 1 328 ? 34.805  70.017  31.078  1.00 57.79  ? 423  LEU A N   1 
ATOM   2352 C CA  . LEU A 1 328 ? 35.742  68.936  30.794  1.00 57.25  ? 423  LEU A CA  1 
ATOM   2353 C C   . LEU A 1 328 ? 35.225  67.592  31.300  1.00 56.63  ? 423  LEU A C   1 
ATOM   2354 O O   . LEU A 1 328 ? 35.597  66.549  30.753  1.00 55.87  ? 423  LEU A O   1 
ATOM   2355 C CB  . LEU A 1 328 ? 37.117  69.255  31.390  1.00 60.53  ? 423  LEU A CB  1 
ATOM   2356 C CG  . LEU A 1 328 ? 37.901  70.376  30.691  1.00 61.71  ? 423  LEU A CG  1 
ATOM   2357 C CD1 . LEU A 1 328 ? 39.221  70.681  31.410  1.00 59.35  ? 423  LEU A CD1 1 
ATOM   2358 C CD2 . LEU A 1 328 ? 38.152  70.047  29.237  1.00 54.22  ? 423  LEU A CD2 1 
ATOM   2359 N N   . GLU A 1 329 ? 34.356  67.594  32.322  1.00 57.06  ? 424  GLU A N   1 
ATOM   2360 C CA  . GLU A 1 329 ? 33.636  66.375  32.695  1.00 54.96  ? 424  GLU A CA  1 
ATOM   2361 C C   . GLU A 1 329 ? 33.065  65.686  31.462  1.00 54.31  ? 424  GLU A C   1 
ATOM   2362 O O   . GLU A 1 329 ? 33.212  64.472  31.283  1.00 52.44  ? 424  GLU A O   1 
ATOM   2363 C CB  . GLU A 1 329 ? 32.491  66.684  33.667  1.00 54.17  ? 424  GLU A CB  1 
ATOM   2364 C CG  . GLU A 1 329 ? 32.867  67.252  35.036  1.00 58.98  ? 424  GLU A CG  1 
ATOM   2365 C CD  . GLU A 1 329 ? 31.652  67.853  35.751  1.00 58.31  ? 424  GLU A CD  1 
ATOM   2366 O OE1 . GLU A 1 329 ? 30.523  67.371  35.503  1.00 57.50  ? 424  GLU A OE1 1 
ATOM   2367 O OE2 . GLU A 1 329 ? 31.816  68.808  36.549  1.00 60.11  ? 424  GLU A OE2 1 
ATOM   2368 N N   . ASN A 1 330 ? 32.383  66.455  30.608  1.00 54.09  ? 425  ASN A N   1 
ATOM   2369 C CA  . ASN A 1 330 ? 31.766  65.869  29.425  1.00 51.20  ? 425  ASN A CA  1 
ATOM   2370 C C   . ASN A 1 330 ? 32.816  65.518  28.376  1.00 52.28  ? 425  ASN A C   1 
ATOM   2371 O O   . ASN A 1 330 ? 32.673  64.513  27.668  1.00 49.48  ? 425  ASN A O   1 
ATOM   2372 C CB  . ASN A 1 330 ? 30.732  66.820  28.818  1.00 49.30  ? 425  ASN A CB  1 
ATOM   2373 C CG  . ASN A 1 330 ? 29.593  67.169  29.768  1.00 53.19  ? 425  ASN A CG  1 
ATOM   2374 O OD1 . ASN A 1 330 ? 28.908  68.186  29.560  1.00 52.11  ? 425  ASN A OD1 1 
ATOM   2375 N ND2 . ASN A 1 330 ? 29.373  66.343  30.806  1.00 48.02  ? 425  ASN A ND2 1 
ATOM   2376 N N   . VAL A 1 331 ? 33.871  66.337  28.251  1.00 51.66  ? 426  VAL A N   1 
ATOM   2377 C CA  . VAL A 1 331 ? 34.858  66.087  27.201  1.00 51.30  ? 426  VAL A CA  1 
ATOM   2378 C C   . VAL A 1 331 ? 35.468  64.712  27.400  1.00 49.44  ? 426  VAL A C   1 
ATOM   2379 O O   . VAL A 1 331 ? 35.481  63.880  26.490  1.00 48.45  ? 426  VAL A O   1 
ATOM   2380 C CB  . VAL A 1 331 ? 35.931  67.194  27.184  1.00 56.69  ? 426  VAL A CB  1 
ATOM   2381 C CG1 . VAL A 1 331 ? 37.094  66.828  26.260  1.00 52.05  ? 426  VAL A CG1 1 
ATOM   2382 C CG2 . VAL A 1 331 ? 35.314  68.519  26.742  1.00 54.56  ? 426  VAL A CG2 1 
ATOM   2383 N N   . HIS A 1 332 ? 35.898  64.425  28.627  1.00 52.03  ? 427  HIS A N   1 
ATOM   2384 C CA  . HIS A 1 332 ? 36.436  63.108  28.935  1.00 50.60  ? 427  HIS A CA  1 
ATOM   2385 C C   . HIS A 1 332 ? 35.404  62.024  28.683  1.00 48.48  ? 427  HIS A C   1 
ATOM   2386 O O   . HIS A 1 332 ? 35.735  60.960  28.142  1.00 49.70  ? 427  HIS A O   1 
ATOM   2387 C CB  . HIS A 1 332 ? 36.937  63.096  30.376  1.00 52.98  ? 427  HIS A CB  1 
ATOM   2388 C CG  . HIS A 1 332 ? 38.040  64.081  30.619  1.00 60.12  ? 427  HIS A CG  1 
ATOM   2389 N ND1 . HIS A 1 332 ? 39.140  64.179  29.790  1.00 61.16  ? 427  HIS A ND1 1 
ATOM   2390 C CD2 . HIS A 1 332 ? 38.210  65.022  31.581  1.00 61.67  ? 427  HIS A CD2 1 
ATOM   2391 C CE1 . HIS A 1 332 ? 39.942  65.129  30.236  1.00 61.43  ? 427  HIS A CE1 1 
ATOM   2392 N NE2 . HIS A 1 332 ? 39.403  65.655  31.322  1.00 61.52  ? 427  HIS A NE2 1 
ATOM   2393 N N   . PHE A 1 333 ? 34.134  62.298  28.996  1.00 50.20  ? 428  PHE A N   1 
ATOM   2394 C CA  . PHE A 1 333 ? 33.089  61.340  28.656  1.00 45.95  ? 428  PHE A CA  1 
ATOM   2395 C C   . PHE A 1 333 ? 33.077  61.056  27.160  1.00 48.73  ? 428  PHE A C   1 
ATOM   2396 O O   . PHE A 1 333 ? 33.139  59.889  26.742  1.00 48.86  ? 428  PHE A O   1 
ATOM   2397 C CB  . PHE A 1 333 ? 31.727  61.844  29.126  1.00 48.27  ? 428  PHE A CB  1 
ATOM   2398 C CG  . PHE A 1 333 ? 30.606  60.912  28.804  1.00 47.27  ? 428  PHE A CG  1 
ATOM   2399 C CD1 . PHE A 1 333 ? 30.439  59.734  29.518  1.00 44.76  ? 428  PHE A CD1 1 
ATOM   2400 C CD2 . PHE A 1 333 ? 29.732  61.200  27.768  1.00 44.72  ? 428  PHE A CD2 1 
ATOM   2401 C CE1 . PHE A 1 333 ? 29.412  58.865  29.205  1.00 49.16  ? 428  PHE A CE1 1 
ATOM   2402 C CE2 . PHE A 1 333 ? 28.706  60.339  27.452  1.00 46.97  ? 428  PHE A CE2 1 
ATOM   2403 C CZ  . PHE A 1 333 ? 28.540  59.169  28.173  1.00 47.76  ? 428  PHE A CZ  1 
ATOM   2404 N N   . TYR A 1 334 ? 33.045  62.111  26.327  1.00 47.04  ? 429  TYR A N   1 
ATOM   2405 C CA  . TYR A 1 334 ? 33.048  61.867  24.885  1.00 45.47  ? 429  TYR A CA  1 
ATOM   2406 C C   . TYR A 1 334 ? 34.306  61.109  24.481  1.00 46.74  ? 429  TYR A C   1 
ATOM   2407 O O   . TYR A 1 334 ? 34.250  60.199  23.642  1.00 45.51  ? 429  TYR A O   1 
ATOM   2408 C CB  . TYR A 1 334 ? 32.943  63.176  24.097  1.00 46.66  ? 429  TYR A CB  1 
ATOM   2409 C CG  . TYR A 1 334 ? 31.797  64.083  24.493  1.00 49.05  ? 429  TYR A CG  1 
ATOM   2410 C CD1 . TYR A 1 334 ? 30.526  63.576  24.732  1.00 46.26  ? 429  TYR A CD1 1 
ATOM   2411 C CD2 . TYR A 1 334 ? 31.995  65.455  24.634  1.00 50.12  ? 429  TYR A CD2 1 
ATOM   2412 C CE1 . TYR A 1 334 ? 29.482  64.417  25.091  1.00 48.19  ? 429  TYR A CE1 1 
ATOM   2413 C CE2 . TYR A 1 334 ? 30.971  66.294  25.002  1.00 47.01  ? 429  TYR A CE2 1 
ATOM   2414 C CZ  . TYR A 1 334 ? 29.715  65.772  25.232  1.00 50.38  ? 429  TYR A CZ  1 
ATOM   2415 O OH  . TYR A 1 334 ? 28.695  66.618  25.598  1.00 48.72  ? 429  TYR A OH  1 
ATOM   2416 N N   . ASP A 1 335 ? 35.439  61.427  25.124  1.00 45.87  ? 430  ASP A N   1 
ATOM   2417 C CA  . ASP A 1 335 ? 36.681  60.711  24.838  1.00 49.04  ? 430  ASP A CA  1 
ATOM   2418 C C   . ASP A 1 335 ? 36.517  59.230  25.140  1.00 50.26  ? 430  ASP A C   1 
ATOM   2419 O O   . ASP A 1 335 ? 36.815  58.372  24.293  1.00 49.28  ? 430  ASP A O   1 
ATOM   2420 C CB  . ASP A 1 335 ? 37.832  61.315  25.651  1.00 46.41  ? 430  ASP A CB  1 
ATOM   2421 C CG  . ASP A 1 335 ? 39.160  60.580  25.446  1.00 50.99  ? 430  ASP A CG  1 
ATOM   2422 O OD1 . ASP A 1 335 ? 39.509  60.249  24.284  1.00 48.65  ? 430  ASP A OD1 1 
ATOM   2423 O OD2 . ASP A 1 335 ? 39.877  60.364  26.453  1.00 52.73  ? 430  ASP A OD2 1 
ATOM   2424 N N   . SER A 1 336 ? 35.973  58.915  26.326  1.00 47.88  ? 431  SER A N   1 
ATOM   2425 C CA  . SER A 1 336 ? 35.721  57.521  26.668  1.00 48.46  ? 431  SER A CA  1 
ATOM   2426 C C   . SER A 1 336 ? 34.833  56.868  25.625  1.00 47.25  ? 431  SER A C   1 
ATOM   2427 O O   . SER A 1 336 ? 35.103  55.742  25.182  1.00 49.58  ? 431  SER A O   1 
ATOM   2428 C CB  . SER A 1 336 ? 35.078  57.426  28.052  1.00 49.89  ? 431  SER A CB  1 
ATOM   2429 O OG  . SER A 1 336 ? 35.914  58.053  29.009  1.00 60.18  ? 431  SER A OG  1 
ATOM   2430 N N   . MET A 1 337 ? 33.809  57.596  25.167  1.00 46.76  ? 432  MET A N   1 
ATOM   2431 C CA  . MET A 1 337 ? 32.924  57.056  24.139  1.00 49.54  ? 432  MET A CA  1 
ATOM   2432 C C   . MET A 1 337 ? 33.717  56.578  22.928  1.00 47.35  ? 432  MET A C   1 
ATOM   2433 O O   . MET A 1 337 ? 33.576  55.428  22.486  1.00 43.94  ? 432  MET A O   1 
ATOM   2434 C CB  . MET A 1 337 ? 31.912  58.112  23.723  1.00 45.30  ? 432  MET A CB  1 
ATOM   2435 C CG  . MET A 1 337 ? 30.881  57.568  22.783  1.00 47.76  ? 432  MET A CG  1 
ATOM   2436 S SD  . MET A 1 337 ? 29.681  58.835  22.445  1.00 47.90  ? 432  MET A SD  1 
ATOM   2437 C CE  . MET A 1 337 ? 30.598  59.934  21.386  1.00 48.20  ? 432  MET A CE  1 
ATOM   2438 N N   . PHE A 1 338 ? 34.621  57.422  22.420  1.00 45.55  ? 433  PHE A N   1 
ATOM   2439 C CA  . PHE A 1 338 ? 35.325  57.000  21.216  1.00 48.57  ? 433  PHE A CA  1 
ATOM   2440 C C   . PHE A 1 338 ? 36.285  55.867  21.513  1.00 48.15  ? 433  PHE A C   1 
ATOM   2441 O O   . PHE A 1 338 ? 36.357  54.902  20.734  1.00 46.34  ? 433  PHE A O   1 
ATOM   2442 C CB  . PHE A 1 338 ? 36.029  58.175  20.545  1.00 46.75  ? 433  PHE A CB  1 
ATOM   2443 C CG  . PHE A 1 338 ? 35.150  58.854  19.555  1.00 48.80  ? 433  PHE A CG  1 
ATOM   2444 C CD1 . PHE A 1 338 ? 35.037  58.359  18.265  1.00 50.31  ? 433  PHE A CD1 1 
ATOM   2445 C CD2 . PHE A 1 338 ? 34.358  59.923  19.933  1.00 47.02  ? 433  PHE A CD2 1 
ATOM   2446 C CE1 . PHE A 1 338 ? 34.189  58.954  17.351  1.00 52.27  ? 433  PHE A CE1 1 
ATOM   2447 C CE2 . PHE A 1 338 ? 33.507  60.511  19.029  1.00 49.79  ? 433  PHE A CE2 1 
ATOM   2448 C CZ  . PHE A 1 338 ? 33.426  60.029  17.735  1.00 50.99  ? 433  PHE A CZ  1 
ATOM   2449 N N   . LYS A 1 339 ? 36.961  55.911  22.672  1.00 46.54  ? 434  LYS A N   1 
ATOM   2450 C CA  . LYS A 1 339 ? 37.849  54.802  22.997  1.00 49.15  ? 434  LYS A CA  1 
ATOM   2451 C C   . LYS A 1 339 ? 37.052  53.509  23.039  1.00 50.37  ? 434  LYS A C   1 
ATOM   2452 O O   . LYS A 1 339 ? 37.473  52.487  22.474  1.00 49.20  ? 434  LYS A O   1 
ATOM   2453 C CB  . LYS A 1 339 ? 38.579  55.070  24.311  1.00 51.32  ? 434  LYS A CB  1 
ATOM   2454 C CG  . LYS A 1 339 ? 39.660  56.167  24.190  1.00 52.03  ? 434  LYS A CG  1 
ATOM   2455 C CD  . LYS A 1 339 ? 40.660  56.153  25.350  1.00 52.56  ? 434  LYS A CD  1 
ATOM   2456 C CE  . LYS A 1 339 ? 39.998  56.530  26.654  1.00 57.15  ? 434  LYS A CE  1 
ATOM   2457 N NZ  . LYS A 1 339 ? 41.014  56.665  27.736  1.00 57.75  ? 434  LYS A NZ  1 
ATOM   2458 N N   . HIS A 1 340 ? 35.830  53.582  23.575  1.00 47.18  ? 435  HIS A N   1 
ATOM   2459 C CA  . HIS A 1 340 ? 34.994  52.396  23.646  1.00 47.84  ? 435  HIS A CA  1 
ATOM   2460 C C   . HIS A 1 340 ? 34.605  51.931  22.248  1.00 47.67  ? 435  HIS A C   1 
ATOM   2461 O O   . HIS A 1 340 ? 34.726  50.738  21.931  1.00 48.90  ? 435  HIS A O   1 
ATOM   2462 C CB  . HIS A 1 340 ? 33.773  52.701  24.516  1.00 50.76  ? 435  HIS A CB  1 
ATOM   2463 C CG  . HIS A 1 340 ? 32.766  51.600  24.567  1.00 51.17  ? 435  HIS A CG  1 
ATOM   2464 N ND1 . HIS A 1 340 ? 32.855  50.552  25.457  1.00 53.95  ? 435  HIS A ND1 1 
ATOM   2465 C CD2 . HIS A 1 340 ? 31.637  51.395  23.850  1.00 47.17  ? 435  HIS A CD2 1 
ATOM   2466 C CE1 . HIS A 1 340 ? 31.820  49.748  25.288  1.00 51.55  ? 435  HIS A CE1 1 
ATOM   2467 N NE2 . HIS A 1 340 ? 31.064  50.238  24.322  1.00 51.35  ? 435  HIS A NE2 1 
ATOM   2468 N N   . ILE A 1 341 ? 34.212  52.870  21.376  1.00 45.94  ? 436  ILE A N   1 
ATOM   2469 C CA  . ILE A 1 341 ? 33.937  52.524  19.983  1.00 47.49  ? 436  ILE A CA  1 
ATOM   2470 C C   . ILE A 1 341 ? 35.154  51.833  19.367  1.00 48.61  ? 436  ILE A C   1 
ATOM   2471 O O   . ILE A 1 341 ? 35.050  50.742  18.781  1.00 48.08  ? 436  ILE A O   1 
ATOM   2472 C CB  . ILE A 1 341 ? 33.524  53.783  19.194  1.00 48.83  ? 436  ILE A CB  1 
ATOM   2473 C CG1 . ILE A 1 341 ? 32.125  54.250  19.616  1.00 49.60  ? 436  ILE A CG1 1 
ATOM   2474 C CG2 . ILE A 1 341 ? 33.547  53.531  17.686  1.00 48.52  ? 436  ILE A CG2 1 
ATOM   2475 C CD1 . ILE A 1 341 ? 31.767  55.669  19.166  1.00 44.26  ? 436  ILE A CD1 1 
ATOM   2476 N N   . PHE A 1 342 ? 36.344  52.407  19.571  1.00 47.95  ? 437  PHE A N   1 
ATOM   2477 C CA  . PHE A 1 342 ? 37.515  51.803  18.944  1.00 50.84  ? 437  PHE A CA  1 
ATOM   2478 C C   . PHE A 1 342 ? 37.706  50.392  19.477  1.00 53.34  ? 437  PHE A C   1 
ATOM   2479 O O   . PHE A 1 342 ? 37.796  49.426  18.699  1.00 50.38  ? 437  PHE A O   1 
ATOM   2480 C CB  . PHE A 1 342 ? 38.753  52.677  19.177  1.00 49.70  ? 437  PHE A CB  1 
ATOM   2481 C CG  . PHE A 1 342 ? 38.631  54.074  18.598  1.00 49.55  ? 437  PHE A CG  1 
ATOM   2482 C CD1 . PHE A 1 342 ? 37.839  54.316  17.486  1.00 46.67  ? 437  PHE A CD1 1 
ATOM   2483 C CD2 . PHE A 1 342 ? 39.301  55.138  19.176  1.00 49.27  ? 437  PHE A CD2 1 
ATOM   2484 C CE1 . PHE A 1 342 ? 37.719  55.587  16.967  1.00 47.30  ? 437  PHE A CE1 1 
ATOM   2485 C CE2 . PHE A 1 342 ? 39.188  56.419  18.658  1.00 47.37  ? 437  PHE A CE2 1 
ATOM   2486 C CZ  . PHE A 1 342 ? 38.400  56.644  17.551  1.00 46.68  ? 437  PHE A CZ  1 
ATOM   2487 N N   . THR A 1 343 ? 37.591  50.245  20.800  1.00 50.16  ? 438  THR A N   1 
ATOM   2488 C CA  . THR A 1 343 ? 37.821  48.949  21.411  1.00 52.19  ? 438  THR A CA  1 
ATOM   2489 C C   . THR A 1 343 ? 36.819  47.937  20.893  1.00 54.41  ? 438  THR A C   1 
ATOM   2490 O O   . THR A 1 343 ? 37.179  46.790  20.606  1.00 52.98  ? 438  THR A O   1 
ATOM   2491 C CB  . THR A 1 343 ? 37.727  49.054  22.931  1.00 54.26  ? 438  THR A CB  1 
ATOM   2492 O OG1 . THR A 1 343 ? 38.727  49.962  23.405  1.00 55.28  ? 438  THR A OG1 1 
ATOM   2493 C CG2 . THR A 1 343 ? 37.922  47.670  23.579  1.00 52.24  ? 438  THR A CG2 1 
ATOM   2494 N N   . GLU A 1 344 ? 35.558  48.354  20.729  1.00 52.00  ? 439  GLU A N   1 
ATOM   2495 C CA  . GLU A 1 344 ? 34.565  47.352  20.380  1.00 53.07  ? 439  GLU A CA  1 
ATOM   2496 C C   . GLU A 1 344 ? 34.648  47.005  18.901  1.00 54.89  ? 439  GLU A C   1 
ATOM   2497 O O   . GLU A 1 344 ? 34.298  45.886  18.512  1.00 54.01  ? 439  GLU A O   1 
ATOM   2498 C CB  . GLU A 1 344 ? 33.159  47.826  20.765  1.00 48.72  ? 439  GLU A CB  1 
ATOM   2499 C CG  . GLU A 1 344 ? 32.914  47.953  22.281  1.00 52.25  ? 439  GLU A CG  1 
ATOM   2500 C CD  . GLU A 1 344 ? 33.024  46.615  23.026  1.00 60.28  ? 439  GLU A CD  1 
ATOM   2501 O OE1 . GLU A 1 344 ? 32.458  45.612  22.548  1.00 64.26  ? 439  GLU A OE1 1 
ATOM   2502 O OE2 . GLU A 1 344 ? 33.699  46.567  24.084  1.00 64.12  ? 439  GLU A OE2 1 
ATOM   2503 N N   . LEU A 1 345 ? 35.140  47.925  18.063  1.00 52.76  ? 440  LEU A N   1 
ATOM   2504 C CA  . LEU A 1 345 ? 35.199  47.571  16.652  1.00 51.77  ? 440  LEU A CA  1 
ATOM   2505 C C   . LEU A 1 345 ? 36.317  46.578  16.398  1.00 55.36  ? 440  LEU A C   1 
ATOM   2506 O O   . LEU A 1 345 ? 36.241  45.791  15.449  1.00 58.02  ? 440  LEU A O   1 
ATOM   2507 C CB  . LEU A 1 345 ? 35.392  48.819  15.782  1.00 52.25  ? 440  LEU A CB  1 
ATOM   2508 C CG  . LEU A 1 345 ? 34.208  49.608  15.228  1.00 47.98  ? 440  LEU A CG  1 
ATOM   2509 C CD1 . LEU A 1 345 ? 34.734  50.756  14.388  1.00 47.20  ? 440  LEU A CD1 1 
ATOM   2510 C CD2 . LEU A 1 345 ? 33.223  48.753  14.412  1.00 48.50  ? 440  LEU A CD2 1 
ATOM   2511 N N   . SER A 1 346 ? 37.341  46.599  17.251  1.00 56.75  ? 441  SER A N   1 
ATOM   2512 C CA  . SER A 1 346 ? 38.561  45.828  17.091  1.00 58.07  ? 441  SER A CA  1 
ATOM   2513 C C   . SER A 1 346 ? 38.535  44.503  17.836  1.00 62.09  ? 441  SER A C   1 
ATOM   2514 O O   . SER A 1 346 ? 39.577  43.855  17.945  1.00 67.88  ? 441  SER A O   1 
ATOM   2515 C CB  . SER A 1 346 ? 39.759  46.645  17.581  1.00 57.53  ? 441  SER A CB  1 
ATOM   2516 O OG  . SER A 1 346 ? 39.811  47.916  16.963  1.00 59.03  ? 441  SER A OG  1 
ATOM   2517 N N   . LYS A 1 347 ? 37.389  44.086  18.359  1.00 67.14  ? 442  LYS A N   1 
ATOM   2518 C CA  . LYS A 1 347 ? 37.340  42.956  19.275  1.00 68.20  ? 442  LYS A CA  1 
ATOM   2519 C C   . LYS A 1 347 ? 36.312  41.926  18.827  1.00 73.92  ? 442  LYS A C   1 
ATOM   2520 O O   . LYS A 1 347 ? 35.225  42.275  18.350  1.00 69.28  ? 442  LYS A O   1 
ATOM   2521 C CB  . LYS A 1 347 ? 37.040  43.434  20.706  1.00 68.57  ? 442  LYS A CB  1 
ATOM   2522 C CG  . LYS A 1 347 ? 35.634  43.152  21.206  1.00 71.71  ? 442  LYS A CG  1 
ATOM   2523 C CD  . LYS A 1 347 ? 35.537  43.422  22.701  1.00 76.35  ? 442  LYS A CD  1 
ATOM   2524 C CE  . LYS A 1 347 ? 34.170  43.041  23.255  1.00 83.82  ? 442  LYS A CE  1 
ATOM   2525 N NZ  . LYS A 1 347 ? 33.999  43.516  24.662  1.00 83.85  ? 442  LYS A NZ  1 
ATOM   2526 N N   . GLY A 1 348 ? 36.667  40.654  18.980  1.00 77.86  ? 443  GLY A N   1 
ATOM   2527 C CA  . GLY A 1 348 ? 35.749  39.569  18.709  1.00 76.93  ? 443  GLY A CA  1 
ATOM   2528 C C   . GLY A 1 348 ? 35.894  39.024  17.298  1.00 73.47  ? 443  GLY A C   1 
ATOM   2529 O O   . GLY A 1 348 ? 36.438  39.666  16.395  1.00 75.87  ? 443  GLY A O   1 
ATOM   2530 N N   . GLY A 1 349 ? 35.377  37.806  17.111  1.00 68.47  ? 444  GLY A N   1 
ATOM   2531 C CA  . GLY A 1 349 ? 35.513  37.142  15.824  1.00 62.50  ? 444  GLY A CA  1 
ATOM   2532 C C   . GLY A 1 349 ? 34.814  37.878  14.695  1.00 55.86  ? 444  GLY A C   1 
ATOM   2533 O O   . GLY A 1 349 ? 35.409  38.129  13.642  1.00 54.82  ? 444  GLY A O   1 
ATOM   2534 N N   . LYS A 1 350 ? 33.547  38.252  14.906  1.00 54.25  ? 445  LYS A N   1 
ATOM   2535 C CA  . LYS A 1 350 ? 32.757  38.822  13.813  1.00 54.07  ? 445  LYS A CA  1 
ATOM   2536 C C   . LYS A 1 350 ? 33.365  40.117  13.287  1.00 48.82  ? 445  LYS A C   1 
ATOM   2537 O O   . LYS A 1 350 ? 33.520  40.295  12.072  1.00 49.93  ? 445  LYS A O   1 
ATOM   2538 C CB  . LYS A 1 350 ? 31.310  39.062  14.251  1.00 50.94  ? 445  LYS A CB  1 
ATOM   2539 C CG  . LYS A 1 350 ? 30.450  39.675  13.128  1.00 56.39  ? 445  LYS A CG  1 
ATOM   2540 C CD  . LYS A 1 350 ? 29.160  40.361  13.652  1.00 58.59  ? 445  LYS A CD  1 
ATOM   2541 N N   . ASN A 1 351 ? 33.701  41.043  14.184  1.00 49.78  ? 446  ASN A N   1 
ATOM   2542 C CA  . ASN A 1 351 ? 34.258  42.318  13.740  1.00 50.68  ? 446  ASN A CA  1 
ATOM   2543 C C   . ASN A 1 351 ? 35.639  42.141  13.126  1.00 51.01  ? 446  ASN A C   1 
ATOM   2544 O O   . ASN A 1 351 ? 35.978  42.813  12.140  1.00 46.72  ? 446  ASN A O   1 
ATOM   2545 C CB  . ASN A 1 351 ? 34.321  43.318  14.895  1.00 46.32  ? 446  ASN A CB  1 
ATOM   2546 C CG  . ASN A 1 351 ? 32.958  43.893  15.238  1.00 52.11  ? 446  ASN A CG  1 
ATOM   2547 O OD1 . ASN A 1 351 ? 32.000  43.704  14.492  1.00 49.28  ? 446  ASN A OD1 1 
ATOM   2548 N ND2 . ASN A 1 351 ? 32.873  44.615  16.352  1.00 44.42  ? 446  ASN A ND2 1 
ATOM   2549 N N   . GLU A 1 352 ? 36.456  41.267  13.710  1.00 48.31  ? 447  GLU A N   1 
ATOM   2550 C CA  . GLU A 1 352 ? 37.769  40.987  13.143  1.00 53.01  ? 447  GLU A CA  1 
ATOM   2551 C C   . GLU A 1 352 ? 37.643  40.485  11.710  1.00 49.28  ? 447  GLU A C   1 
ATOM   2552 O O   . GLU A 1 352 ? 38.362  40.945  10.821  1.00 49.55  ? 447  GLU A O   1 
ATOM   2553 C CB  . GLU A 1 352 ? 38.510  39.973  14.017  1.00 55.88  ? 447  GLU A CB  1 
ATOM   2554 C CG  . GLU A 1 352 ? 39.932  39.687  13.574  1.00 64.60  ? 447  GLU A CG  1 
ATOM   2555 C CD  . GLU A 1 352 ? 40.547  38.480  14.295  1.00 75.67  ? 447  GLU A CD  1 
ATOM   2556 O OE1 . GLU A 1 352 ? 39.965  37.994  15.292  1.00 75.59  ? 447  GLU A OE1 1 
ATOM   2557 O OE2 . GLU A 1 352 ? 41.625  38.012  13.852  1.00 82.29  ? 447  GLU A OE2 1 
ATOM   2558 N N   . MET A 1 353 ? 36.695  39.581  11.452  1.00 49.33  ? 448  MET A N   1 
ATOM   2559 C CA  . MET A 1 353 ? 36.518  39.088  10.090  1.00 48.20  ? 448  MET A CA  1 
ATOM   2560 C C   . MET A 1 353 ? 35.995  40.173  9.149   1.00 51.51  ? 448  MET A C   1 
ATOM   2561 O O   . MET A 1 353 ? 36.421  40.245  7.981   1.00 46.05  ? 448  MET A O   1 
ATOM   2562 C CB  . MET A 1 353 ? 35.572  37.896  10.072  1.00 51.90  ? 448  MET A CB  1 
ATOM   2563 C CG  . MET A 1 353 ? 35.336  37.378  8.655   1.00 59.44  ? 448  MET A CG  1 
ATOM   2564 S SD  . MET A 1 353 ? 34.863  35.645  8.600   1.00 79.51  ? 448  MET A SD  1 
ATOM   2565 C CE  . MET A 1 353 ? 33.379  35.712  9.608   1.00 64.96  ? 448  MET A CE  1 
ATOM   2566 N N   . LEU A 1 354 ? 35.046  41.000  9.618   1.00 44.20  ? 449  LEU A N   1 
ATOM   2567 C CA  . LEU A 1 354 ? 34.559  42.104  8.787   1.00 47.22  ? 449  LEU A CA  1 
ATOM   2568 C C   . LEU A 1 354 ? 35.704  43.035  8.398   1.00 42.71  ? 449  LEU A C   1 
ATOM   2569 O O   . LEU A 1 354 ? 35.864  43.397  7.224   1.00 42.10  ? 449  LEU A O   1 
ATOM   2570 C CB  . LEU A 1 354 ? 33.449  42.885  9.514   1.00 42.88  ? 449  LEU A CB  1 
ATOM   2571 C CG  . LEU A 1 354 ? 32.125  42.156  9.752   1.00 45.31  ? 449  LEU A CG  1 
ATOM   2572 C CD1 . LEU A 1 354 ? 31.170  42.997  10.627  1.00 42.75  ? 449  LEU A CD1 1 
ATOM   2573 C CD2 . LEU A 1 354 ? 31.460  41.788  8.425   1.00 40.74  ? 449  LEU A CD2 1 
ATOM   2574 N N   . ILE A 1 355 ? 36.523  43.424  9.374   1.00 45.54  ? 450  ILE A N   1 
ATOM   2575 C CA  . ILE A 1 355 ? 37.610  44.356  9.082   1.00 47.84  ? 450  ILE A CA  1 
ATOM   2576 C C   . ILE A 1 355 ? 38.611  43.712  8.131   1.00 47.60  ? 450  ILE A C   1 
ATOM   2577 O O   . ILE A 1 355 ? 39.055  44.338  7.158   1.00 43.24  ? 450  ILE A O   1 
ATOM   2578 C CB  . ILE A 1 355 ? 38.284  44.832  10.381  1.00 48.85  ? 450  ILE A CB  1 
ATOM   2579 C CG1 . ILE A 1 355 ? 37.361  45.798  11.125  1.00 45.46  ? 450  ILE A CG1 1 
ATOM   2580 C CG2 . ILE A 1 355 ? 39.647  45.490  10.080  1.00 45.17  ? 450  ILE A CG2 1 
ATOM   2581 C CD1 . ILE A 1 355 ? 37.680  45.927  12.612  1.00 47.34  ? 450  ILE A CD1 1 
ATOM   2582 N N   . LYS A 1 356 ? 38.973  42.449  8.396   1.00 45.72  ? 451  LYS A N   1 
ATOM   2583 C CA  . LYS A 1 356 ? 39.877  41.726  7.500   1.00 48.71  ? 451  LYS A CA  1 
ATOM   2584 C C   . LYS A 1 356 ? 39.339  41.697  6.080   1.00 48.37  ? 451  LYS A C   1 
ATOM   2585 O O   . LYS A 1 356 ? 40.091  41.876  5.120   1.00 47.85  ? 451  LYS A O   1 
ATOM   2586 C CB  . LYS A 1 356 ? 40.079  40.292  7.983   1.00 51.28  ? 451  LYS A CB  1 
ATOM   2587 C CG  . LYS A 1 356 ? 41.258  40.093  8.893   1.00 66.52  ? 451  LYS A CG  1 
ATOM   2588 C CD  . LYS A 1 356 ? 41.390  38.619  9.273   1.00 75.26  ? 451  LYS A CD  1 
ATOM   2589 C CE  . LYS A 1 356 ? 41.883  38.448  10.718  1.00 78.12  ? 451  LYS A CE  1 
ATOM   2590 N NZ  . LYS A 1 356 ? 41.906  37.004  11.138  1.00 81.54  ? 451  LYS A NZ  1 
ATOM   2591 N N   . THR A 1 357 ? 38.045  41.430  5.927   1.00 43.28  ? 452  THR A N   1 
ATOM   2592 C CA  . THR A 1 357 ? 37.467  41.337  4.589   1.00 47.79  ? 452  THR A CA  1 
ATOM   2593 C C   . THR A 1 357 ? 37.561  42.676  3.862   1.00 46.90  ? 452  THR A C   1 
ATOM   2594 O O   . THR A 1 357 ? 37.880  42.714  2.669   1.00 44.32  ? 452  THR A O   1 
ATOM   2595 C CB  . THR A 1 357 ? 36.008  40.857  4.666   1.00 45.60  ? 452  THR A CB  1 
ATOM   2596 O OG1 . THR A 1 357 ? 35.941  39.614  5.374   1.00 44.84  ? 452  THR A OG1 1 
ATOM   2597 C CG2 . THR A 1 357 ? 35.434  40.668  3.288   1.00 44.43  ? 452  THR A CG2 1 
ATOM   2598 N N   . VAL A 1 358 ? 37.295  43.789  4.562   1.00 47.24  ? 453  VAL A N   1 
ATOM   2599 C CA  . VAL A 1 358 ? 37.516  45.100  3.940   1.00 45.13  ? 453  VAL A CA  1 
ATOM   2600 C C   . VAL A 1 358 ? 38.978  45.256  3.530   1.00 46.09  ? 453  VAL A C   1 
ATOM   2601 O O   . VAL A 1 358 ? 39.289  45.719  2.431   1.00 44.46  ? 453  VAL A O   1 
ATOM   2602 C CB  . VAL A 1 358 ? 37.101  46.252  4.875   1.00 46.06  ? 453  VAL A CB  1 
ATOM   2603 C CG1 . VAL A 1 358 ? 37.496  47.595  4.223   1.00 40.37  ? 453  VAL A CG1 1 
ATOM   2604 C CG2 . VAL A 1 358 ? 35.601  46.227  5.194   1.00 41.15  ? 453  VAL A CG2 1 
ATOM   2605 N N   . LYS A 1 359 ? 39.882  44.949  4.439   1.00 45.55  ? 454  LYS A N   1 
ATOM   2606 C CA  . LYS A 1 359 ? 41.300  45.136  4.214   1.00 47.85  ? 454  LYS A CA  1 
ATOM   2607 C C   . LYS A 1 359 ? 41.851  44.336  3.057   1.00 52.00  ? 454  LYS A C   1 
ATOM   2608 O O   . LYS A 1 359 ? 42.810  44.727  2.455   1.00 49.98  ? 454  LYS A O   1 
ATOM   2609 C CB  . LYS A 1 359 ? 42.113  44.854  5.466   1.00 52.65  ? 454  LYS A CB  1 
ATOM   2610 C CG  . LYS A 1 359 ? 41.907  45.784  6.639   1.00 53.80  ? 454  LYS A CG  1 
ATOM   2611 C CD  . LYS A 1 359 ? 41.947  47.231  6.242   1.00 54.47  ? 454  LYS A CD  1 
ATOM   2612 C CE  . LYS A 1 359 ? 41.648  48.155  7.399   1.00 54.67  ? 454  LYS A CE  1 
ATOM   2613 N NZ  . LYS A 1 359 ? 42.568  48.003  8.538   1.00 55.60  ? 454  LYS A NZ  1 
ATOM   2614 N N   . GLY A 1 360 ? 41.217  43.226  2.749   1.00 49.97  ? 455  GLY A N   1 
ATOM   2615 C CA  . GLY A 1 360 ? 41.636  42.398  1.650   1.00 51.63  ? 455  GLY A CA  1 
ATOM   2616 C C   . GLY A 1 360 ? 41.607  43.154  0.348   1.00 53.39  ? 455  GLY A C   1 
ATOM   2617 O O   . GLY A 1 360 ? 42.450  42.951  -0.479  1.00 52.86  ? 455  GLY A O   1 
ATOM   2618 N N   . GLN A 1 361 ? 40.597  43.973  0.139   1.00 49.85  ? 456  GLN A N   1 
ATOM   2619 C CA  . GLN A 1 361 ? 40.534  44.783  -1.038  1.00 51.02  ? 456  GLN A CA  1 
ATOM   2620 C C   . GLN A 1 361 ? 41.104  46.173  -0.815  1.00 51.28  ? 456  GLN A C   1 
ATOM   2621 O O   . GLN A 1 361 ? 41.611  46.763  -1.723  1.00 52.88  ? 456  GLN A O   1 
ATOM   2622 C CB  . GLN A 1 361 ? 39.113  44.882  -1.545  1.00 49.44  ? 456  GLN A CB  1 
ATOM   2623 C CG  . GLN A 1 361 ? 38.958  45.704  -2.795  1.00 47.88  ? 456  GLN A CG  1 
ATOM   2624 C CD  . GLN A 1 361 ? 37.612  45.549  -3.442  1.00 49.05  ? 456  GLN A CD  1 
ATOM   2625 O OE1 . GLN A 1 361 ? 36.686  45.099  -2.834  1.00 47.96  ? 456  GLN A OE1 1 
ATOM   2626 N NE2 . GLN A 1 361 ? 37.515  45.918  -4.677  1.00 48.98  ? 456  GLN A NE2 1 
ATOM   2627 N N   . TYR A 1 362 ? 41.032  46.683  0.398   1.00 47.21  ? 457  TYR A N   1 
ATOM   2628 C CA  . TYR A 1 362 ? 41.513  48.023  0.684   1.00 48.42  ? 457  TYR A CA  1 
ATOM   2629 C C   . TYR A 1 362 ? 42.435  48.066  1.879   1.00 50.47  ? 457  TYR A C   1 
ATOM   2630 O O   . TYR A 1 362 ? 42.069  48.531  2.913   1.00 49.35  ? 457  TYR A O   1 
ATOM   2631 C CB  . TYR A 1 362 ? 40.349  48.977  0.930   1.00 48.84  ? 457  TYR A CB  1 
ATOM   2632 C CG  . TYR A 1 362 ? 39.329  49.040  -0.167  1.00 48.85  ? 457  TYR A CG  1 
ATOM   2633 C CD1 . TYR A 1 362 ? 38.071  48.529  0.006   1.00 47.90  ? 457  TYR A CD1 1 
ATOM   2634 C CD2 . TYR A 1 362 ? 39.622  49.614  -1.365  1.00 46.34  ? 457  TYR A CD2 1 
ATOM   2635 C CE1 . TYR A 1 362 ? 37.141  48.584  -0.990  1.00 47.50  ? 457  TYR A CE1 1 
ATOM   2636 C CE2 . TYR A 1 362 ? 38.701  49.673  -2.363  1.00 48.46  ? 457  TYR A CE2 1 
ATOM   2637 C CZ  . TYR A 1 362 ? 37.462  49.161  -2.167  1.00 49.70  ? 457  TYR A CZ  1 
ATOM   2638 O OH  . TYR A 1 362 ? 36.565  49.227  -3.161  1.00 48.24  ? 457  TYR A OH  1 
ATOM   2639 N N   . PRO A 1 363 ? 43.665  47.618  1.714   1.00 51.35  ? 458  PRO A N   1 
ATOM   2640 C CA  . PRO A 1 363 ? 44.611  47.564  2.822   1.00 53.06  ? 458  PRO A CA  1 
ATOM   2641 C C   . PRO A 1 363 ? 44.995  48.898  3.402   1.00 53.42  ? 458  PRO A C   1 
ATOM   2642 O O   . PRO A 1 363 ? 45.078  49.857  2.703   1.00 55.83  ? 458  PRO A O   1 
ATOM   2643 C CB  . PRO A 1 363 ? 45.825  46.890  2.207   1.00 52.35  ? 458  PRO A CB  1 
ATOM   2644 C CG  . PRO A 1 363 ? 45.707  47.148  0.768   1.00 54.51  ? 458  PRO A CG  1 
ATOM   2645 C CD  . PRO A 1 363 ? 44.261  47.195  0.449   1.00 51.11  ? 458  PRO A CD  1 
ATOM   2646 N N   . CYS A 1 364 ? 45.130  48.933  4.709   1.00 52.08  ? 459  CYS A N   1 
ATOM   2647 C CA  . CYS A 1 364 ? 45.541  50.091  5.453   1.00 53.67  ? 459  CYS A CA  1 
ATOM   2648 C C   . CYS A 1 364 ? 45.991  49.604  6.808   1.00 56.71  ? 459  CYS A C   1 
ATOM   2649 O O   . CYS A 1 364 ? 45.500  48.619  7.301   1.00 56.37  ? 459  CYS A O   1 
ATOM   2650 C CB  . CYS A 1 364 ? 44.393  51.060  5.607   1.00 55.04  ? 459  CYS A CB  1 
ATOM   2651 S SG  . CYS A 1 364 ? 44.811  52.516  6.532   1.00 58.49  ? 459  CYS A SG  1 
ATOM   2652 N N   . GLU A 1 365 ? 46.870  50.332  7.456   1.00 56.13  ? 460  GLU A N   1 
ATOM   2653 C CA  . GLU A 1 365 ? 47.348  49.917  8.750   1.00 56.85  ? 460  GLU A CA  1 
ATOM   2654 C C   . GLU A 1 365 ? 46.242  49.989  9.762   1.00 56.88  ? 460  GLU A C   1 
ATOM   2655 O O   . GLU A 1 365 ? 45.429  50.868  9.709   1.00 55.48  ? 460  GLU A O   1 
ATOM   2656 C CB  . GLU A 1 365 ? 48.500  50.802  9.186   1.00 57.41  ? 460  GLU A CB  1 
ATOM   2657 N N   . ASP A 1 366 ? 46.247  49.101  10.737  1.00 56.95  ? 461  ASP A N   1 
ATOM   2658 C CA  . ASP A 1 366 ? 45.198  49.090  11.747  1.00 56.20  ? 461  ASP A CA  1 
ATOM   2659 C C   . ASP A 1 366 ? 45.158  50.412  12.501  1.00 56.36  ? 461  ASP A C   1 
ATOM   2660 O O   . ASP A 1 366 ? 46.197  51.017  12.793  1.00 51.77  ? 461  ASP A O   1 
ATOM   2661 C CB  . ASP A 1 366 ? 45.397  47.932  12.730  1.00 57.47  ? 461  ASP A CB  1 
ATOM   2662 C CG  . ASP A 1 366 ? 44.969  46.589  12.145  1.00 64.56  ? 461  ASP A CG  1 
ATOM   2663 O OD1 . ASP A 1 366 ? 45.829  45.701  12.015  1.00 67.14  ? 461  ASP A OD1 1 
ATOM   2664 O OD2 . ASP A 1 366 ? 43.776  46.433  11.787  1.00 66.00  ? 461  ASP A OD2 1 
ATOM   2665 N N   . PHE A 1 367 ? 43.939  50.857  12.809  1.00 52.45  ? 462  PHE A N   1 
ATOM   2666 C CA  . PHE A 1 367 ? 43.747  52.102  13.536  1.00 51.07  ? 462  PHE A CA  1 
ATOM   2667 C C   . PHE A 1 367 ? 44.340  52.000  14.937  1.00 53.99  ? 462  PHE A C   1 
ATOM   2668 O O   . PHE A 1 367 ? 44.149  51.002  15.637  1.00 56.57  ? 462  PHE A O   1 
ATOM   2669 C CB  . PHE A 1 367 ? 42.251  52.442  13.613  1.00 50.01  ? 462  PHE A CB  1 
ATOM   2670 C CG  . PHE A 1 367 ? 41.989  53.813  14.139  1.00 48.82  ? 462  PHE A CG  1 
ATOM   2671 C CD1 . PHE A 1 367 ? 42.071  54.907  13.299  1.00 47.61  ? 462  PHE A CD1 1 
ATOM   2672 C CD2 . PHE A 1 367 ? 41.702  54.017  15.479  1.00 48.27  ? 462  PHE A CD2 1 
ATOM   2673 C CE1 . PHE A 1 367 ? 41.857  56.184  13.775  1.00 48.59  ? 462  PHE A CE1 1 
ATOM   2674 C CE2 . PHE A 1 367 ? 41.480  55.297  15.965  1.00 50.02  ? 462  PHE A CE2 1 
ATOM   2675 C CZ  . PHE A 1 367 ? 41.566  56.382  15.110  1.00 51.39  ? 462  PHE A CZ  1 
ATOM   2676 N N   . GLN A 1 368 ? 45.050  53.051  15.354  1.00 52.35  ? 463  GLN A N   1 
ATOM   2677 C CA  . GLN A 1 368 ? 45.852  53.045  16.575  1.00 54.21  ? 463  GLN A CA  1 
ATOM   2678 C C   . GLN A 1 368 ? 45.387  54.135  17.524  1.00 52.54  ? 463  GLN A C   1 
ATOM   2679 O O   . GLN A 1 368 ? 45.224  55.289  17.109  1.00 54.03  ? 463  GLN A O   1 
ATOM   2680 C CB  . GLN A 1 368 ? 47.330  53.286  16.266  1.00 58.61  ? 463  GLN A CB  1 
ATOM   2681 C CG  . GLN A 1 368 ? 48.187  52.061  16.065  1.00 62.84  ? 463  GLN A CG  1 
ATOM   2682 C CD  . GLN A 1 368 ? 49.664  52.425  16.135  1.00 78.02  ? 463  GLN A CD  1 
ATOM   2683 O OE1 . GLN A 1 368 ? 50.077  53.502  15.683  1.00 80.57  ? 463  GLN A OE1 1 
ATOM   2684 N NE2 . GLN A 1 368 ? 50.466  51.542  16.738  1.00 79.39  ? 463  GLN A NE2 1 
ATOM   2685 N N   . TRP A 1 369 ? 45.235  53.789  18.804  1.00 52.47  ? 464  TRP A N   1 
ATOM   2686 C CA  . TRP A 1 369 ? 44.893  54.780  19.817  1.00 54.46  ? 464  TRP A CA  1 
ATOM   2687 C C   . TRP A 1 369 ? 45.531  54.390  21.141  1.00 55.05  ? 464  TRP A C   1 
ATOM   2688 O O   . TRP A 1 369 ? 45.960  53.250  21.331  1.00 58.76  ? 464  TRP A O   1 
ATOM   2689 C CB  . TRP A 1 369 ? 43.370  54.947  19.956  1.00 54.14  ? 464  TRP A CB  1 
ATOM   2690 C CG  . TRP A 1 369 ? 42.634  53.810  20.623  1.00 53.57  ? 464  TRP A CG  1 
ATOM   2691 C CD1 . TRP A 1 369 ? 42.156  53.784  21.906  1.00 53.87  ? 464  TRP A CD1 1 
ATOM   2692 C CD2 . TRP A 1 369 ? 42.267  52.556  20.035  1.00 52.70  ? 464  TRP A CD2 1 
ATOM   2693 N NE1 . TRP A 1 369 ? 41.519  52.590  22.152  1.00 52.56  ? 464  TRP A NE1 1 
ATOM   2694 C CE2 . TRP A 1 369 ? 41.576  51.815  21.024  1.00 52.18  ? 464  TRP A CE2 1 
ATOM   2695 C CE3 . TRP A 1 369 ? 42.462  51.982  18.771  1.00 52.72  ? 464  TRP A CE3 1 
ATOM   2696 C CZ2 . TRP A 1 369 ? 41.082  50.530  20.790  1.00 49.86  ? 464  TRP A CZ2 1 
ATOM   2697 C CZ3 . TRP A 1 369 ? 41.964  50.708  18.537  1.00 53.51  ? 464  TRP A CZ3 1 
ATOM   2698 C CH2 . TRP A 1 369 ? 41.283  49.994  19.546  1.00 53.72  ? 464  TRP A CH2 1 
ATOM   2699 N N   . LEU A 1 370 ? 45.611  55.360  22.049  1.00 54.07  ? 465  LEU A N   1 
ATOM   2700 C CA  . LEU A 1 370 ? 46.305  55.204  23.321  1.00 55.21  ? 465  LEU A CA  1 
ATOM   2701 C C   . LEU A 1 370 ? 45.313  55.070  24.469  1.00 59.48  ? 465  LEU A C   1 
ATOM   2702 O O   . LEU A 1 370 ? 44.126  55.395  24.346  1.00 58.82  ? 465  LEU A O   1 
ATOM   2703 C CB  . LEU A 1 370 ? 47.233  56.394  23.589  1.00 56.84  ? 465  LEU A CB  1 
ATOM   2704 C CG  . LEU A 1 370 ? 48.243  56.778  22.515  1.00 56.14  ? 465  LEU A CG  1 
ATOM   2705 C CD1 . LEU A 1 370 ? 48.935  58.070  22.920  1.00 55.23  ? 465  LEU A CD1 1 
ATOM   2706 C CD2 . LEU A 1 370 ? 49.244  55.650  22.319  1.00 55.12  ? 465  LEU A CD2 1 
ATOM   2707 N N   . GLU A 1 371 ? 45.829  54.609  25.613  1.00 60.03  ? 466  GLU A N   1 
ATOM   2708 C CA  . GLU A 1 371 ? 44.997  54.529  26.809  1.00 65.25  ? 466  GLU A CA  1 
ATOM   2709 C C   . GLU A 1 371 ? 44.752  55.903  27.413  1.00 59.75  ? 466  GLU A C   1 
ATOM   2710 O O   . GLU A 1 371 ? 43.719  56.122  28.057  1.00 55.77  ? 466  GLU A O   1 
ATOM   2711 C CB  . GLU A 1 371 ? 45.635  53.597  27.833  1.00 69.31  ? 466  GLU A CB  1 
ATOM   2712 C CG  . GLU A 1 371 ? 45.643  52.148  27.381  1.00 76.67  ? 466  GLU A CG  1 
ATOM   2713 C CD  . GLU A 1 371 ? 45.570  51.179  28.539  1.00 88.48  ? 466  GLU A CD  1 
ATOM   2714 O OE1 . GLU A 1 371 ? 44.481  50.588  28.750  1.00 90.94  ? 466  GLU A OE1 1 
ATOM   2715 O OE2 . GLU A 1 371 ? 46.601  51.028  29.241  1.00 90.73  ? 466  GLU A OE2 1 
ATOM   2716 N N   . GLU A 1 372 ? 45.681  56.832  27.220  1.00 57.64  ? 467  GLU A N   1 
ATOM   2717 C CA  . GLU A 1 372 ? 45.473  58.241  27.525  1.00 60.34  ? 467  GLU A CA  1 
ATOM   2718 C C   . GLU A 1 372 ? 45.488  59.015  26.211  1.00 57.28  ? 467  GLU A C   1 
ATOM   2719 O O   . GLU A 1 372 ? 46.503  59.024  25.505  1.00 56.13  ? 467  GLU A O   1 
ATOM   2720 C CB  . GLU A 1 372 ? 46.545  58.765  28.480  1.00 60.87  ? 467  GLU A CB  1 
ATOM   2721 C CG  . GLU A 1 372 ? 46.175  60.075  29.164  1.00 67.17  ? 467  GLU A CG  1 
ATOM   2722 C CD  . GLU A 1 372 ? 47.308  60.632  30.021  1.00 78.50  ? 467  GLU A CD  1 
ATOM   2723 O OE1 . GLU A 1 372 ? 47.727  61.787  29.782  1.00 84.35  ? 467  GLU A OE1 1 
ATOM   2724 O OE2 . GLU A 1 372 ? 47.788  59.912  30.926  1.00 84.18  ? 467  GLU A OE2 1 
ATOM   2725 N N   . THR A 1 373 ? 44.366  59.654  25.889  1.00 54.77  ? 468  THR A N   1 
ATOM   2726 C CA  . THR A 1 373 ? 44.241  60.385  24.623  1.00 55.03  ? 468  THR A CA  1 
ATOM   2727 C C   . THR A 1 373 ? 44.989  61.710  24.706  1.00 54.51  ? 468  THR A C   1 
ATOM   2728 O O   . THR A 1 373 ? 44.762  62.484  25.643  1.00 52.49  ? 468  THR A O   1 
ATOM   2729 C CB  . THR A 1 373 ? 42.767  60.645  24.304  1.00 52.49  ? 468  THR A CB  1 
ATOM   2730 O OG1 . THR A 1 373 ? 42.047  59.406  24.300  1.00 52.21  ? 468  THR A OG1 1 
ATOM   2731 C CG2 . THR A 1 373 ? 42.615  61.320  22.935  1.00 49.29  ? 468  THR A CG2 1 
ATOM   2732 N N   . PRO A 1 374 ? 45.890  62.011  23.770  1.00 53.75  ? 469  PRO A N   1 
ATOM   2733 C CA  . PRO A 1 374 ? 46.573  63.310  23.828  1.00 50.78  ? 469  PRO A CA  1 
ATOM   2734 C C   . PRO A 1 374 ? 45.594  64.445  23.572  1.00 53.27  ? 469  PRO A C   1 
ATOM   2735 O O   . PRO A 1 374 ? 44.693  64.340  22.733  1.00 51.66  ? 469  PRO A O   1 
ATOM   2736 C CB  . PRO A 1 374 ? 47.648  63.226  22.737  1.00 51.35  ? 469  PRO A CB  1 
ATOM   2737 C CG  . PRO A 1 374 ? 47.594  61.873  22.168  1.00 51.92  ? 469  PRO A CG  1 
ATOM   2738 C CD  . PRO A 1 374 ? 46.535  61.059  22.853  1.00 52.63  ? 469  PRO A CD  1 
ATOM   2739 N N   . ILE A 1 375 ? 45.767  65.522  24.331  1.00 50.58  ? 470  ILE A N   1 
ATOM   2740 C CA  . ILE A 1 375 ? 44.951  66.725  24.236  1.00 50.75  ? 470  ILE A CA  1 
ATOM   2741 C C   . ILE A 1 375 ? 45.905  67.886  24.037  1.00 55.14  ? 470  ILE A C   1 
ATOM   2742 O O   . ILE A 1 375 ? 46.827  68.078  24.839  1.00 55.50  ? 470  ILE A O   1 
ATOM   2743 C CB  . ILE A 1 375 ? 44.099  66.949  25.498  1.00 52.34  ? 470  ILE A CB  1 
ATOM   2744 C CG1 . ILE A 1 375 ? 43.120  65.789  25.739  1.00 54.81  ? 470  ILE A CG1 1 
ATOM   2745 C CG2 . ILE A 1 375 ? 43.355  68.272  25.406  1.00 52.13  ? 470  ILE A CG2 1 
ATOM   2746 C CD1 . ILE A 1 375 ? 42.272  65.950  27.022  1.00 50.04  ? 470  ILE A CD1 1 
ATOM   2747 N N   . PHE A 1 376 ? 45.702  68.650  22.974  1.00 54.62  ? 471  PHE A N   1 
ATOM   2748 C CA  . PHE A 1 376 ? 46.488  69.850  22.743  1.00 55.17  ? 471  PHE A CA  1 
ATOM   2749 C C   . PHE A 1 376 ? 45.550  71.040  22.665  1.00 52.72  ? 471  PHE A C   1 
ATOM   2750 O O   . PHE A 1 376 ? 44.438  70.923  22.149  1.00 52.19  ? 471  PHE A O   1 
ATOM   2751 C CB  . PHE A 1 376 ? 47.303  69.748  21.445  1.00 56.01  ? 471  PHE A CB  1 
ATOM   2752 C CG  . PHE A 1 376 ? 48.028  68.442  21.275  1.00 56.13  ? 471  PHE A CG  1 
ATOM   2753 C CD1 . PHE A 1 376 ? 49.250  68.228  21.893  1.00 55.81  ? 471  PHE A CD1 1 
ATOM   2754 C CD2 . PHE A 1 376 ? 47.500  67.439  20.477  1.00 53.81  ? 471  PHE A CD2 1 
ATOM   2755 C CE1 . PHE A 1 376 ? 49.930  67.031  21.723  1.00 57.08  ? 471  PHE A CE1 1 
ATOM   2756 C CE2 . PHE A 1 376 ? 48.174  66.244  20.300  1.00 53.45  ? 471  PHE A CE2 1 
ATOM   2757 C CZ  . PHE A 1 376 ? 49.392  66.039  20.926  1.00 56.89  ? 471  PHE A CZ  1 
ATOM   2758 N N   . THR A 1 377 ? 45.989  72.180  23.174  1.00 54.93  ? 472  THR A N   1 
ATOM   2759 C CA  . THR A 1 377 ? 45.245  73.389  22.866  1.00 57.45  ? 472  THR A CA  1 
ATOM   2760 C C   . THR A 1 377 ? 45.532  73.822  21.426  1.00 57.97  ? 472  THR A C   1 
ATOM   2761 O O   . THR A 1 377 ? 46.516  73.403  20.810  1.00 55.96  ? 472  THR A O   1 
ATOM   2762 C CB  . THR A 1 377 ? 45.601  74.513  23.836  1.00 58.68  ? 472  THR A CB  1 
ATOM   2763 O OG1 . THR A 1 377 ? 46.897  75.023  23.510  1.00 58.49  ? 472  THR A OG1 1 
ATOM   2764 C CG2 . THR A 1 377 ? 45.617  74.002  25.274  1.00 57.67  ? 472  THR A CG2 1 
ATOM   2765 N N   . TYR A 1 378 ? 44.641  74.658  20.886  1.00 55.86  ? 473  TYR A N   1 
ATOM   2766 C CA  . TYR A 1 378 ? 44.847  75.208  19.545  1.00 57.70  ? 473  TYR A CA  1 
ATOM   2767 C C   . TYR A 1 378 ? 46.182  75.946  19.453  1.00 57.85  ? 473  TYR A C   1 
ATOM   2768 O O   . TYR A 1 378 ? 46.920  75.792  18.472  1.00 56.95  ? 473  TYR A O   1 
ATOM   2769 C CB  . TYR A 1 378 ? 43.678  76.138  19.185  1.00 56.41  ? 473  TYR A CB  1 
ATOM   2770 C CG  . TYR A 1 378 ? 43.596  76.633  17.741  1.00 57.08  ? 473  TYR A CG  1 
ATOM   2771 C CD1 . TYR A 1 378 ? 43.171  75.793  16.721  1.00 56.15  ? 473  TYR A CD1 1 
ATOM   2772 C CD2 . TYR A 1 378 ? 43.898  77.957  17.412  1.00 57.84  ? 473  TYR A CD2 1 
ATOM   2773 C CE1 . TYR A 1 378 ? 43.076  76.236  15.408  1.00 57.17  ? 473  TYR A CE1 1 
ATOM   2774 C CE2 . TYR A 1 378 ? 43.800  78.412  16.098  1.00 58.88  ? 473  TYR A CE2 1 
ATOM   2775 C CZ  . TYR A 1 378 ? 43.387  77.540  15.102  1.00 59.61  ? 473  TYR A CZ  1 
ATOM   2776 O OH  . TYR A 1 378 ? 43.275  77.966  13.792  1.00 60.99  ? 473  TYR A OH  1 
ATOM   2777 N N   . GLU A 1 379 ? 46.511  76.745  20.473  1.00 55.56  ? 474  GLU A N   1 
ATOM   2778 C CA  . GLU A 1 379 ? 47.791  77.451  20.491  1.00 59.61  ? 474  GLU A CA  1 
ATOM   2779 C C   . GLU A 1 379 ? 48.966  76.477  20.461  1.00 59.72  ? 474  GLU A C   1 
ATOM   2780 O O   . GLU A 1 379 ? 49.940  76.687  19.726  1.00 60.24  ? 474  GLU A O   1 
ATOM   2781 C CB  . GLU A 1 379 ? 47.868  78.345  21.727  1.00 61.27  ? 474  GLU A CB  1 
ATOM   2782 C CG  . GLU A 1 379 ? 49.160  79.155  21.840  1.00 66.71  ? 474  GLU A CG  1 
ATOM   2783 C CD  . GLU A 1 379 ? 49.240  79.969  23.126  1.00 69.06  ? 474  GLU A CD  1 
ATOM   2784 O OE1 . GLU A 1 379 ? 48.640  79.551  24.142  1.00 68.80  ? 474  GLU A OE1 1 
ATOM   2785 O OE2 . GLU A 1 379 ? 49.904  81.028  23.124  1.00 76.37  ? 474  GLU A OE2 1 
ATOM   2786 N N   . GLU A 1 380 ? 48.894  75.407  21.260  1.00 59.59  ? 475  GLU A N   1 
ATOM   2787 C CA  . GLU A 1 380 ? 49.939  74.385  21.240  1.00 61.49  ? 475  GLU A CA  1 
ATOM   2788 C C   . GLU A 1 380 ? 50.068  73.747  19.865  1.00 57.31  ? 475  GLU A C   1 
ATOM   2789 O O   . GLU A 1 380 ? 51.181  73.529  19.387  1.00 58.41  ? 475  GLU A O   1 
ATOM   2790 C CB  . GLU A 1 380 ? 49.656  73.301  22.283  1.00 60.99  ? 475  GLU A CB  1 
ATOM   2791 C CG  . GLU A 1 380 ? 49.852  73.735  23.723  1.00 68.76  ? 475  GLU A CG  1 
ATOM   2792 C CD  . GLU A 1 380 ? 49.285  72.722  24.709  1.00 73.54  ? 475  GLU A CD  1 
ATOM   2793 O OE1 . GLU A 1 380 ? 48.766  71.675  24.259  1.00 72.16  ? 475  GLU A OE1 1 
ATOM   2794 O OE2 . GLU A 1 380 ? 49.365  72.977  25.933  1.00 79.90  ? 475  GLU A OE2 1 
ATOM   2795 N N   . ALA A 1 381 ? 48.941  73.419  19.228  1.00 57.77  ? 476  ALA A N   1 
ATOM   2796 C CA  . ALA A 1 381 ? 48.973  72.804  17.903  1.00 57.55  ? 476  ALA A CA  1 
ATOM   2797 C C   . ALA A 1 381 ? 49.621  73.729  16.878  1.00 59.74  ? 476  ALA A C   1 
ATOM   2798 O O   . ALA A 1 381 ? 50.447  73.290  16.062  1.00 61.39  ? 476  ALA A O   1 
ATOM   2799 C CB  . ALA A 1 381 ? 47.554  72.432  17.474  1.00 56.04  ? 476  ALA A CB  1 
ATOM   2800 N N   . ILE A 1 382 ? 49.255  75.014  16.907  1.00 57.44  ? 477  ILE A N   1 
ATOM   2801 C CA  . ILE A 1 382 ? 49.885  75.997  16.033  1.00 57.67  ? 477  ILE A CA  1 
ATOM   2802 C C   . ILE A 1 382 ? 51.389  75.992  16.236  1.00 62.85  ? 477  ILE A C   1 
ATOM   2803 O O   . ILE A 1 382 ? 52.167  75.940  15.273  1.00 61.49  ? 477  ILE A O   1 
ATOM   2804 C CB  . ILE A 1 382 ? 49.313  77.402  16.293  1.00 59.90  ? 477  ILE A CB  1 
ATOM   2805 C CG1 . ILE A 1 382 ? 47.838  77.457  15.921  1.00 62.44  ? 477  ILE A CG1 1 
ATOM   2806 C CG2 . ILE A 1 382 ? 50.119  78.451  15.533  1.00 57.95  ? 477  ILE A CG2 1 
ATOM   2807 C CD1 . ILE A 1 382 ? 47.576  76.844  14.597  1.00 62.21  ? 477  ILE A CD1 1 
ATOM   2808 N N   . LYS A 1 383 ? 51.817  76.099  17.499  1.00 62.46  ? 478  LYS A N   1 
ATOM   2809 C CA  . LYS A 1 383 ? 53.243  76.143  17.794  1.00 61.76  ? 478  LYS A CA  1 
ATOM   2810 C C   . LYS A 1 383 ? 53.952  74.867  17.361  1.00 60.38  ? 478  LYS A C   1 
ATOM   2811 O O   . LYS A 1 383 ? 55.099  74.925  16.918  1.00 60.92  ? 478  LYS A O   1 
ATOM   2812 C CB  . LYS A 1 383 ? 53.451  76.419  19.279  1.00 60.94  ? 478  LYS A CB  1 
ATOM   2813 C CG  . LYS A 1 383 ? 53.409  77.901  19.582  1.00 67.67  ? 478  LYS A CG  1 
ATOM   2814 C CD  . LYS A 1 383 ? 53.013  78.194  21.011  1.00 69.53  ? 478  LYS A CD  1 
ATOM   2815 C CE  . LYS A 1 383 ? 52.948  79.697  21.227  1.00 71.71  ? 478  LYS A CE  1 
ATOM   2816 N NZ  . LYS A 1 383 ? 52.659  80.061  22.648  1.00 80.88  ? 478  LYS A NZ  1 
ATOM   2817 N N   . MET A 1 384 ? 53.285  73.713  17.455  1.00 58.07  ? 479  MET A N   1 
ATOM   2818 C CA  . MET A 1 384 ? 53.878  72.475  16.950  1.00 62.55  ? 479  MET A CA  1 
ATOM   2819 C C   . MET A 1 384 ? 54.086  72.537  15.443  1.00 63.04  ? 479  MET A C   1 
ATOM   2820 O O   . MET A 1 384 ? 55.145  72.137  14.940  1.00 63.72  ? 479  MET A O   1 
ATOM   2821 C CB  . MET A 1 384 ? 52.999  71.271  17.295  1.00 60.52  ? 479  MET A CB  1 
ATOM   2822 C CG  . MET A 1 384 ? 52.903  70.958  18.786  1.00 60.55  ? 479  MET A CG  1 
ATOM   2823 S SD  . MET A 1 384 ? 51.588  69.786  19.149  1.00 69.03  ? 479  MET A SD  1 
ATOM   2824 C CE  . MET A 1 384 ? 52.039  68.395  18.109  1.00 52.90  ? 479  MET A CE  1 
ATOM   2825 N N   . LEU A 1 385 ? 53.072  73.010  14.709  1.00 62.12  ? 480  LEU A N   1 
ATOM   2826 C CA  . LEU A 1 385 ? 53.171  73.091  13.251  1.00 61.27  ? 480  LEU A CA  1 
ATOM   2827 C C   . LEU A 1 385 ? 54.251  74.077  12.823  1.00 61.62  ? 480  LEU A C   1 
ATOM   2828 O O   . LEU A 1 385 ? 54.980  73.831  11.854  1.00 62.79  ? 480  LEU A O   1 
ATOM   2829 C CB  . LEU A 1 385 ? 51.820  73.488  12.656  1.00 58.83  ? 480  LEU A CB  1 
ATOM   2830 C CG  . LEU A 1 385 ? 50.733  72.432  12.837  1.00 58.75  ? 480  LEU A CG  1 
ATOM   2831 C CD1 . LEU A 1 385 ? 49.347  73.056  12.749  1.00 52.46  ? 480  LEU A CD1 1 
ATOM   2832 C CD2 . LEU A 1 385 ? 50.919  71.321  11.797  1.00 55.10  ? 480  LEU A CD2 1 
ATOM   2833 N N   . ILE A 1 386 ? 54.370  75.197  13.534  1.00 61.77  ? 481  ILE A N   1 
ATOM   2834 C CA  . ILE A 1 386 ? 55.423  76.154  13.224  1.00 63.18  ? 481  ILE A CA  1 
ATOM   2835 C C   . ILE A 1 386 ? 56.788  75.561  13.540  1.00 66.46  ? 481  ILE A C   1 
ATOM   2836 O O   . ILE A 1 386 ? 57.749  75.736  12.782  1.00 63.19  ? 481  ILE A O   1 
ATOM   2837 C CB  . ILE A 1 386 ? 55.186  77.471  13.981  1.00 62.15  ? 481  ILE A CB  1 
ATOM   2838 C CG1 . ILE A 1 386 ? 53.870  78.101  13.531  1.00 61.99  ? 481  ILE A CG1 1 
ATOM   2839 C CG2 . ILE A 1 386 ? 56.369  78.434  13.779  1.00 62.54  ? 481  ILE A CG2 1 
ATOM   2840 C CD1 . ILE A 1 386 ? 53.599  79.456  14.132  1.00 63.28  ? 481  ILE A CD1 1 
ATOM   2841 N N   . GLN A 1 387 ? 56.891  74.838  14.657  1.00 67.92  ? 482  GLN A N   1 
ATOM   2842 C CA  . GLN A 1 387 ? 58.166  74.251  15.054  1.00 68.30  ? 482  GLN A CA  1 
ATOM   2843 C C   . GLN A 1 387 ? 58.633  73.204  14.052  1.00 66.94  ? 482  GLN A C   1 
ATOM   2844 O O   . GLN A 1 387 ? 59.831  73.105  13.768  1.00 70.82  ? 482  GLN A O   1 
ATOM   2845 C CB  . GLN A 1 387 ? 58.043  73.649  16.454  1.00 73.42  ? 482  GLN A CB  1 
ATOM   2846 C CG  . GLN A 1 387 ? 59.093  72.604  16.778  1.00 81.59  ? 482  GLN A CG  1 
ATOM   2847 C CD  . GLN A 1 387 ? 58.917  72.011  18.160  1.00 89.61  ? 482  GLN A CD  1 
ATOM   2848 O OE1 . GLN A 1 387 ? 58.174  72.544  18.987  1.00 95.04  ? 482  GLN A OE1 1 
ATOM   2849 N NE2 . GLN A 1 387 ? 59.599  70.899  18.418  1.00 94.27  ? 482  GLN A NE2 1 
ATOM   2850 N N   . HIS A 1 388 ? 57.714  72.417  13.498  1.00 62.00  ? 483  HIS A N   1 
ATOM   2851 C CA  . HIS A 1 388 ? 58.105  71.429  12.501  1.00 62.62  ? 483  HIS A CA  1 
ATOM   2852 C C   . HIS A 1 388 ? 58.213  72.006  11.092  1.00 61.53  ? 483  HIS A C   1 
ATOM   2853 O O   . HIS A 1 388 ? 58.283  71.229  10.134  1.00 61.28  ? 483  HIS A O   1 
ATOM   2854 C CB  . HIS A 1 388 ? 57.125  70.257  12.487  1.00 62.01  ? 483  HIS A CB  1 
ATOM   2855 C CG  . HIS A 1 388 ? 57.294  69.301  13.630  1.00 64.73  ? 483  HIS A CG  1 
ATOM   2856 N ND1 . HIS A 1 388 ? 56.835  69.569  14.903  1.00 69.57  ? 483  HIS A ND1 1 
ATOM   2857 C CD2 . HIS A 1 388 ? 57.856  68.071  13.686  1.00 63.60  ? 483  HIS A CD2 1 
ATOM   2858 C CE1 . HIS A 1 388 ? 57.115  68.549  15.695  1.00 67.01  ? 483  HIS A CE1 1 
ATOM   2859 N NE2 . HIS A 1 388 ? 57.725  67.623  14.979  1.00 65.14  ? 483  HIS A NE2 1 
ATOM   2860 N N   . GLY A 1 389 ? 58.216  73.330  10.941  1.00 60.39  ? 484  GLY A N   1 
ATOM   2861 C CA  . GLY A 1 389 ? 58.300  73.950  9.624   1.00 61.33  ? 484  GLY A CA  1 
ATOM   2862 C C   . GLY A 1 389 ? 57.160  73.640  8.666   1.00 62.72  ? 484  GLY A C   1 
ATOM   2863 O O   . GLY A 1 389 ? 57.369  73.654  7.446   1.00 59.49  ? 484  GLY A O   1 
ATOM   2864 N N   . LYS A 1 390 ? 55.957  73.360  9.178   1.00 58.69  ? 485  LYS A N   1 
ATOM   2865 C CA  . LYS A 1 390 ? 54.793  73.129  8.326   1.00 60.43  ? 485  LYS A CA  1 
ATOM   2866 C C   . LYS A 1 390 ? 53.942  74.377  8.141   1.00 59.10  ? 485  LYS A C   1 
ATOM   2867 O O   . LYS A 1 390 ? 53.009  74.361  7.331   1.00 61.07  ? 485  LYS A O   1 
ATOM   2868 C CB  . LYS A 1 390 ? 53.910  72.007  8.897   1.00 57.69  ? 485  LYS A CB  1 
ATOM   2869 C CG  . LYS A 1 390 ? 54.613  70.673  9.015   1.00 60.25  ? 485  LYS A CG  1 
ATOM   2870 C CD  . LYS A 1 390 ? 55.234  70.291  7.695   1.00 59.65  ? 485  LYS A CD  1 
ATOM   2871 C CE  . LYS A 1 390 ? 55.927  68.948  7.764   1.00 63.65  ? 485  LYS A CE  1 
ATOM   2872 N NZ  . LYS A 1 390 ? 56.629  68.658  6.464   1.00 68.59  ? 485  LYS A NZ  1 
ATOM   2873 N N   . LEU A 1 391 ? 54.252  75.449  8.856   1.00 59.49  ? 486  LEU A N   1 
ATOM   2874 C CA  . LEU A 1 391 ? 53.405  76.624  8.925   1.00 59.53  ? 486  LEU A CA  1 
ATOM   2875 C C   . LEU A 1 391 ? 54.290  77.828  9.190   1.00 60.97  ? 486  LEU A C   1 
ATOM   2876 O O   . LEU A 1 391 ? 55.273  77.723  9.929   1.00 63.97  ? 486  LEU A O   1 
ATOM   2877 C CB  . LEU A 1 391 ? 52.357  76.453  10.028  1.00 61.94  ? 486  LEU A CB  1 
ATOM   2878 C CG  . LEU A 1 391 ? 51.498  77.639  10.442  1.00 62.64  ? 486  LEU A CG  1 
ATOM   2879 C CD1 . LEU A 1 391 ? 50.771  78.185  9.244   1.00 59.86  ? 486  LEU A CD1 1 
ATOM   2880 C CD2 . LEU A 1 391 ? 50.512  77.200  11.525  1.00 62.43  ? 486  LEU A CD2 1 
ATOM   2881 N N   . HIS A 1 392 ? 53.952  78.962  8.576   1.00 63.24  ? 487  HIS A N   1 
ATOM   2882 C CA  . HIS A 1 392 ? 54.716  80.193  8.744   1.00 61.57  ? 487  HIS A CA  1 
ATOM   2883 C C   . HIS A 1 392 ? 53.750  81.340  8.987   1.00 69.22  ? 487  HIS A C   1 
ATOM   2884 O O   . HIS A 1 392 ? 52.990  81.715  8.087   1.00 68.59  ? 487  HIS A O   1 
ATOM   2885 C CB  . HIS A 1 392 ? 55.598  80.474  7.528   1.00 62.04  ? 487  HIS A CB  1 
ATOM   2886 C CG  . HIS A 1 392 ? 56.697  79.479  7.354   1.00 62.31  ? 487  HIS A CG  1 
ATOM   2887 N ND1 . HIS A 1 392 ? 57.979  79.699  7.812   1.00 65.07  ? 487  HIS A ND1 1 
ATOM   2888 C CD2 . HIS A 1 392 ? 56.696  78.238  6.815   1.00 58.16  ? 487  HIS A CD2 1 
ATOM   2889 C CE1 . HIS A 1 392 ? 58.728  78.645  7.537   1.00 63.86  ? 487  HIS A CE1 1 
ATOM   2890 N NE2 . HIS A 1 392 ? 57.974  77.746  6.929   1.00 64.75  ? 487  HIS A NE2 1 
ATOM   2891 N N   . LEU A 1 393 ? 53.802  81.897  10.197  1.00 73.81  ? 488  LEU A N   1 
ATOM   2892 C CA  . LEU A 1 393 ? 52.933  82.979  10.639  1.00 80.63  ? 488  LEU A CA  1 
ATOM   2893 C C   . LEU A 1 393 ? 53.743  83.957  11.473  1.00 88.70  ? 488  LEU A C   1 
ATOM   2894 O O   . LEU A 1 393 ? 54.584  83.544  12.276  1.00 88.43  ? 488  LEU A O   1 
ATOM   2895 C CB  . LEU A 1 393 ? 51.775  82.464  11.499  1.00 73.44  ? 488  LEU A CB  1 
ATOM   2896 C CG  . LEU A 1 393 ? 50.789  81.436  10.958  1.00 71.63  ? 488  LEU A CG  1 
ATOM   2897 C CD1 . LEU A 1 393 ? 50.012  80.787  12.100  1.00 68.03  ? 488  LEU A CD1 1 
ATOM   2898 C CD2 . LEU A 1 393 ? 49.844  82.100  9.978   1.00 72.16  ? 488  LEU A CD2 1 
ATOM   2899 N N   . LYS A 1 394 ? 53.483  85.250  11.295  1.00 95.55  ? 489  LYS A N   1 
ATOM   2900 C CA  . LYS A 1 394 ? 53.965  86.214  12.272  1.00 99.60  ? 489  LYS A CA  1 
ATOM   2901 C C   . LYS A 1 394 ? 53.217  86.024  13.593  1.00 106.04 ? 489  LYS A C   1 
ATOM   2902 O O   . LYS A 1 394 ? 52.165  85.374  13.655  1.00 102.76 ? 489  LYS A O   1 
ATOM   2903 C CB  . LYS A 1 394 ? 53.793  87.642  11.754  1.00 99.23  ? 489  LYS A CB  1 
ATOM   2904 C CG  . LYS A 1 394 ? 54.507  87.899  10.438  1.00 96.72  ? 489  LYS A CG  1 
ATOM   2905 C CD  . LYS A 1 394 ? 54.658  89.384  10.155  1.00 96.32  ? 489  LYS A CD  1 
ATOM   2906 C CE  . LYS A 1 394 ? 55.540  89.622  8.942   1.00 91.46  ? 489  LYS A CE  1 
ATOM   2907 N N   . GLU A 1 395 ? 53.784  86.572  14.673  1.00 116.11 ? 490  GLU A N   1 
ATOM   2908 C CA  . GLU A 1 395 ? 53.061  86.542  15.943  1.00 118.84 ? 490  GLU A CA  1 
ATOM   2909 C C   . GLU A 1 395 ? 51.828  87.434  15.888  1.00 115.52 ? 490  GLU A C   1 
ATOM   2910 O O   . GLU A 1 395 ? 50.837  87.166  16.578  1.00 112.26 ? 490  GLU A O   1 
ATOM   2911 C CB  . GLU A 1 395 ? 53.976  86.957  17.097  1.00 122.09 ? 490  GLU A CB  1 
ATOM   2912 C CG  . GLU A 1 395 ? 53.366  86.743  18.486  1.00 127.08 ? 490  GLU A CG  1 
ATOM   2913 C CD  . GLU A 1 395 ? 53.691  85.381  19.086  1.00 128.78 ? 490  GLU A CD  1 
ATOM   2914 O OE1 . GLU A 1 395 ? 54.786  84.853  18.803  1.00 130.91 ? 490  GLU A OE1 1 
ATOM   2915 O OE2 . GLU A 1 395 ? 52.855  84.842  19.846  1.00 124.69 ? 490  GLU A OE2 1 
ATOM   2916 N N   . GLU A 1 396 ? 51.869  88.478  15.055  1.00 112.66 ? 491  GLU A N   1 
ATOM   2917 C CA  . GLU A 1 396 ? 50.684  89.287  14.791  1.00 111.02 ? 491  GLU A CA  1 
ATOM   2918 C C   . GLU A 1 396 ? 49.531  88.437  14.265  1.00 108.54 ? 491  GLU A C   1 
ATOM   2919 O O   . GLU A 1 396 ? 48.365  88.693  14.585  1.00 106.59 ? 491  GLU A O   1 
ATOM   2920 C CB  . GLU A 1 396 ? 51.031  90.399  13.796  1.00 109.13 ? 491  GLU A CB  1 
ATOM   2921 N N   . GLU A 1 397 ? 49.841  87.407  13.473  1.00 105.29 ? 492  GLU A N   1 
ATOM   2922 C CA  . GLU A 1 397 ? 48.839  86.619  12.763  1.00 101.14 ? 492  GLU A CA  1 
ATOM   2923 C C   . GLU A 1 397 ? 48.360  85.383  13.513  1.00 96.14  ? 492  GLU A C   1 
ATOM   2924 O O   . GLU A 1 397 ? 47.420  84.731  13.051  1.00 93.68  ? 492  GLU A O   1 
ATOM   2925 C CB  . GLU A 1 397 ? 49.387  86.168  11.405  1.00 99.22  ? 492  GLU A CB  1 
ATOM   2926 C CG  . GLU A 1 397 ? 49.736  87.275  10.434  1.00 98.23  ? 492  GLU A CG  1 
ATOM   2927 C CD  . GLU A 1 397 ? 50.505  86.742  9.241   1.00 96.11  ? 492  GLU A CD  1 
ATOM   2928 O OE1 . GLU A 1 397 ? 51.717  86.476  9.386   1.00 96.34  ? 492  GLU A OE1 1 
ATOM   2929 O OE2 . GLU A 1 397 ? 49.894  86.558  8.167   1.00 98.36  ? 492  GLU A OE2 1 
ATOM   2930 N N   . ILE A 1 398 ? 48.984  85.022  14.634  1.00 99.61  ? 493  ILE A N   1 
ATOM   2931 C CA  . ILE A 1 398 ? 48.624  83.767  15.288  1.00 95.47  ? 493  ILE A CA  1 
ATOM   2932 C C   . ILE A 1 398 ? 47.255  83.839  15.956  1.00 96.16  ? 493  ILE A C   1 
ATOM   2933 O O   . ILE A 1 398 ? 46.609  82.800  16.160  1.00 91.84  ? 493  ILE A O   1 
ATOM   2934 C CB  . ILE A 1 398 ? 49.702  83.353  16.310  1.00 93.47  ? 493  ILE A CB  1 
ATOM   2935 N N   . LEU A 1 399 ? 46.791  85.045  16.294  1.00 103.04 ? 494  LEU A N   1 
ATOM   2936 C CA  . LEU A 1 399 ? 45.490  85.191  16.940  1.00 98.75  ? 494  LEU A CA  1 
ATOM   2937 C C   . LEU A 1 399 ? 44.363  84.770  16.004  1.00 96.22  ? 494  LEU A C   1 
ATOM   2938 O O   . LEU A 1 399 ? 43.512  83.950  16.365  1.00 91.95  ? 494  LEU A O   1 
ATOM   2939 C CB  . LEU A 1 399 ? 45.298  86.639  17.404  1.00 100.16 ? 494  LEU A CB  1 
ATOM   2940 N N   . ALA A 1 400 ? 44.357  85.310  14.787  1.00 91.74  ? 495  ALA A N   1 
ATOM   2941 C CA  . ALA A 1 400 ? 43.262  85.133  13.843  1.00 85.85  ? 495  ALA A CA  1 
ATOM   2942 C C   . ALA A 1 400 ? 43.433  83.932  12.921  1.00 80.36  ? 495  ALA A C   1 
ATOM   2943 O O   . ALA A 1 400 ? 42.613  83.753  12.017  1.00 76.21  ? 495  ALA A O   1 
ATOM   2944 C CB  . ALA A 1 400 ? 43.099  86.400  12.992  1.00 84.01  ? 495  ALA A CB  1 
ATOM   2945 N N   . TYR A 1 401 ? 44.464  83.109  13.117  1.00 81.05  ? 496  TYR A N   1 
ATOM   2946 C CA  . TYR A 1 401 ? 44.756  82.055  12.153  1.00 72.19  ? 496  TYR A CA  1 
ATOM   2947 C C   . TYR A 1 401 ? 43.710  80.955  12.219  1.00 64.14  ? 496  TYR A C   1 
ATOM   2948 O O   . TYR A 1 401 ? 43.369  80.463  13.298  1.00 65.86  ? 496  TYR A O   1 
ATOM   2949 C CB  . TYR A 1 401 ? 46.145  81.461  12.385  1.00 69.19  ? 496  TYR A CB  1 
ATOM   2950 C CG  . TYR A 1 401 ? 46.381  80.194  11.589  1.00 61.84  ? 496  TYR A CG  1 
ATOM   2951 C CD1 . TYR A 1 401 ? 46.425  80.216  10.200  1.00 61.57  ? 496  TYR A CD1 1 
ATOM   2952 C CD2 . TYR A 1 401 ? 46.546  78.973  12.225  1.00 62.98  ? 496  TYR A CD2 1 
ATOM   2953 C CE1 . TYR A 1 401 ? 46.632  79.058  9.469   1.00 60.89  ? 496  TYR A CE1 1 
ATOM   2954 C CE2 . TYR A 1 401 ? 46.762  77.807  11.498  1.00 61.76  ? 496  TYR A CE2 1 
ATOM   2955 C CZ  . TYR A 1 401 ? 46.803  77.856  10.126  1.00 59.71  ? 496  TYR A CZ  1 
ATOM   2956 O OH  . TYR A 1 401 ? 47.010  76.694  9.414   1.00 60.65  ? 496  TYR A OH  1 
ATOM   2957 N N   . ASP A 1 402 ? 43.230  80.551  11.057  1.00 62.31  ? 497  ASP A N   1 
ATOM   2958 C CA  . ASP A 1 402 ? 42.177  79.554  10.924  1.00 63.11  ? 497  ASP A CA  1 
ATOM   2959 C C   . ASP A 1 402 ? 42.784  78.344  10.221  1.00 60.75  ? 497  ASP A C   1 
ATOM   2960 O O   . ASP A 1 402 ? 43.028  78.381  9.012   1.00 61.16  ? 497  ASP A O   1 
ATOM   2961 C CB  . ASP A 1 402 ? 41.007  80.161  10.150  1.00 65.70  ? 497  ASP A CB  1 
ATOM   2962 C CG  . ASP A 1 402 ? 39.836  79.224  9.994   1.00 63.36  ? 497  ASP A CG  1 
ATOM   2963 O OD1 . ASP A 1 402 ? 39.907  78.046  10.403  1.00 62.59  ? 497  ASP A OD1 1 
ATOM   2964 O OD2 . ASP A 1 402 ? 38.827  79.691  9.434   1.00 70.60  ? 497  ASP A OD2 1 
ATOM   2965 N N   . MET A 1 403 ? 43.011  77.269  10.975  1.00 61.80  ? 498  MET A N   1 
ATOM   2966 C CA  . MET A 1 403 ? 43.772  76.131  10.470  1.00 59.97  ? 498  MET A CA  1 
ATOM   2967 C C   . MET A 1 403 ? 43.052  75.441  9.315   1.00 60.90  ? 498  MET A C   1 
ATOM   2968 O O   . MET A 1 403 ? 41.880  75.076  9.430   1.00 59.90  ? 498  MET A O   1 
ATOM   2969 C CB  . MET A 1 403 ? 44.019  75.133  11.601  1.00 58.40  ? 498  MET A CB  1 
ATOM   2970 C CG  . MET A 1 403 ? 45.207  74.226  11.368  1.00 56.77  ? 498  MET A CG  1 
ATOM   2971 S SD  . MET A 1 403 ? 45.327  72.968  12.648  1.00 59.42  ? 498  MET A SD  1 
ATOM   2972 C CE  . MET A 1 403 ? 46.024  73.920  13.989  1.00 59.62  ? 498  MET A CE  1 
ATOM   2973 N N   . SER A 1 404 ? 43.770  75.223  8.214   1.00 59.13  ? 499  SER A N   1 
ATOM   2974 C CA  . SER A 1 404 ? 43.184  74.552  7.063   1.00 58.93  ? 499  SER A CA  1 
ATOM   2975 C C   . SER A 1 404 ? 43.077  73.044  7.302   1.00 59.63  ? 499  SER A C   1 
ATOM   2976 O O   . SER A 1 404 ? 43.615  72.492  8.267   1.00 59.28  ? 499  SER A O   1 
ATOM   2977 C CB  . SER A 1 404 ? 44.009  74.818  5.805   1.00 59.69  ? 499  SER A CB  1 
ATOM   2978 O OG  . SER A 1 404 ? 45.017  73.834  5.646   1.00 58.02  ? 499  SER A OG  1 
ATOM   2979 N N   . THR A 1 405 ? 42.381  72.371  6.381   1.00 57.93  ? 500  THR A N   1 
ATOM   2980 C CA  . THR A 1 405 ? 42.226  70.921  6.463   1.00 58.16  ? 500  THR A CA  1 
ATOM   2981 C C   . THR A 1 405 ? 43.536  70.195  6.167   1.00 57.76  ? 500  THR A C   1 
ATOM   2982 O O   . THR A 1 405 ? 43.875  69.210  6.842   1.00 56.55  ? 500  THR A O   1 
ATOM   2983 C CB  . THR A 1 405 ? 41.117  70.470  5.507   1.00 63.42  ? 500  THR A CB  1 
ATOM   2984 O OG1 . THR A 1 405 ? 39.849  70.875  6.034   1.00 66.91  ? 500  THR A OG1 1 
ATOM   2985 C CG2 . THR A 1 405 ? 41.113  68.955  5.337   1.00 61.22  ? 500  THR A CG2 1 
ATOM   2986 N N   . ASP A 1 406 ? 44.284  70.656  5.160   1.00 54.65  ? 501  ASP A N   1 
ATOM   2987 C CA  . ASP A 1 406 ? 45.623  70.115  4.941   1.00 58.40  ? 501  ASP A CA  1 
ATOM   2988 C C   . ASP A 1 406 ? 46.508  70.302  6.167   1.00 54.78  ? 501  ASP A C   1 
ATOM   2989 O O   . ASP A 1 406 ? 47.268  69.400  6.539   1.00 55.14  ? 501  ASP A O   1 
ATOM   2990 C CB  . ASP A 1 406 ? 46.272  70.775  3.728   1.00 58.22  ? 501  ASP A CB  1 
ATOM   2991 C CG  . ASP A 1 406 ? 45.619  70.365  2.433   1.00 64.36  ? 501  ASP A CG  1 
ATOM   2992 O OD1 . ASP A 1 406 ? 45.046  69.250  2.377   1.00 62.79  ? 501  ASP A OD1 1 
ATOM   2993 O OD2 . ASP A 1 406 ? 45.679  71.166  1.476   1.00 71.09  ? 501  ASP A OD2 1 
ATOM   2994 N N   . MET A 1 407 ? 46.448  71.478  6.792   1.00 53.12  ? 502  MET A N   1 
ATOM   2995 C CA  . MET A 1 407 ? 47.271  71.702  7.975   1.00 54.35  ? 502  MET A CA  1 
ATOM   2996 C C   . MET A 1 407 ? 46.904  70.722  9.083   1.00 55.48  ? 502  MET A C   1 
ATOM   2997 O O   . MET A 1 407 ? 47.783  70.234  9.809   1.00 52.90  ? 502  MET A O   1 
ATOM   2998 C CB  . MET A 1 407 ? 47.130  73.146  8.456   1.00 53.66  ? 502  MET A CB  1 
ATOM   2999 C CG  . MET A 1 407 ? 48.256  73.583  9.374   1.00 59.48  ? 502  MET A CG  1 
ATOM   3000 S SD  . MET A 1 407 ? 49.868  73.429  8.558   1.00 57.40  ? 502  MET A SD  1 
ATOM   3001 C CE  . MET A 1 407 ? 49.867  74.873  7.511   1.00 54.22  ? 502  MET A CE  1 
ATOM   3002 N N   . GLU A 1 408 ? 45.608  70.406  9.210   1.00 53.95  ? 503  GLU A N   1 
ATOM   3003 C CA  . GLU A 1 408 ? 45.170  69.440  10.213  1.00 51.45  ? 503  GLU A CA  1 
ATOM   3004 C C   . GLU A 1 408 ? 45.706  68.051  9.906   1.00 50.02  ? 503  GLU A C   1 
ATOM   3005 O O   . GLU A 1 408 ? 46.064  67.303  10.824  1.00 51.27  ? 503  GLU A O   1 
ATOM   3006 C CB  . GLU A 1 408 ? 43.641  69.433  10.311  1.00 52.11  ? 503  GLU A CB  1 
ATOM   3007 C CG  . GLU A 1 408 ? 43.091  70.730  10.922  1.00 55.31  ? 503  GLU A CG  1 
ATOM   3008 C CD  . GLU A 1 408 ? 41.572  70.791  10.968  1.00 57.25  ? 503  GLU A CD  1 
ATOM   3009 O OE1 . GLU A 1 408 ? 41.047  71.561  11.802  1.00 58.16  ? 503  GLU A OE1 1 
ATOM   3010 O OE2 . GLU A 1 408 ? 40.903  70.076  10.185  1.00 59.98  ? 503  GLU A OE2 1 
ATOM   3011 N N   . LYS A 1 409 ? 45.802  67.695  8.623   1.00 50.72  ? 504  LYS A N   1 
ATOM   3012 C CA  . LYS A 1 409 ? 46.481  66.444  8.271   1.00 53.63  ? 504  LYS A CA  1 
ATOM   3013 C C   . LYS A 1 409 ? 47.972  66.474  8.622   1.00 53.37  ? 504  LYS A C   1 
ATOM   3014 O O   . LYS A 1 409 ? 48.547  65.440  9.001   1.00 55.03  ? 504  LYS A O   1 
ATOM   3015 C CB  . LYS A 1 409 ? 46.302  66.140  6.782   1.00 49.93  ? 504  LYS A CB  1 
ATOM   3016 C CG  . LYS A 1 409 ? 44.865  65.843  6.398   1.00 58.46  ? 504  LYS A CG  1 
ATOM   3017 C CD  . LYS A 1 409 ? 44.745  65.500  4.914   1.00 62.64  ? 504  LYS A CD  1 
ATOM   3018 C CE  . LYS A 1 409 ? 43.293  65.309  4.499   1.00 63.15  ? 504  LYS A CE  1 
ATOM   3019 N NZ  . LYS A 1 409 ? 43.202  64.942  3.045   1.00 69.11  ? 504  LYS A NZ  1 
ATOM   3020 N N   . GLU A 1 410 ? 48.620  67.631  8.479   1.00 51.57  ? 505  GLU A N   1 
ATOM   3021 C CA  . GLU A 1 410 ? 50.032  67.725  8.856   1.00 55.52  ? 505  GLU A CA  1 
ATOM   3022 C C   . GLU A 1 410 ? 50.209  67.546  10.361  1.00 54.56  ? 505  GLU A C   1 
ATOM   3023 O O   . GLU A 1 410 ? 51.144  66.874  10.823  1.00 54.17  ? 505  GLU A O   1 
ATOM   3024 C CB  . GLU A 1 410 ? 50.608  69.066  8.408   1.00 54.33  ? 505  GLU A CB  1 
ATOM   3025 C CG  . GLU A 1 410 ? 50.749  69.230  6.899   1.00 59.81  ? 505  GLU A CG  1 
ATOM   3026 C CD  . GLU A 1 410 ? 51.720  68.235  6.267   1.00 64.13  ? 505  GLU A CD  1 
ATOM   3027 O OE1 . GLU A 1 410 ? 51.575  67.950  5.056   1.00 66.59  ? 505  GLU A OE1 1 
ATOM   3028 O OE2 . GLU A 1 410 ? 52.627  67.740  6.974   1.00 65.51  ? 505  GLU A OE2 1 
ATOM   3029 N N   . LEU A 1 411 ? 49.315  68.146  11.140  1.00 55.18  ? 506  LEU A N   1 
ATOM   3030 C CA  . LEU A 1 411 ? 49.303  67.879  12.570  1.00 52.52  ? 506  LEU A CA  1 
ATOM   3031 C C   . LEU A 1 411 ? 49.127  66.390  12.844  1.00 56.22  ? 506  LEU A C   1 
ATOM   3032 O O   . LEU A 1 411 ? 49.806  65.830  13.711  1.00 54.99  ? 506  LEU A O   1 
ATOM   3033 C CB  . LEU A 1 411 ? 48.206  68.689  13.247  1.00 51.15  ? 506  LEU A CB  1 
ATOM   3034 C CG  . LEU A 1 411 ? 48.295  68.686  14.769  1.00 52.64  ? 506  LEU A CG  1 
ATOM   3035 C CD1 . LEU A 1 411 ? 49.590  69.336  15.248  1.00 51.65  ? 506  LEU A CD1 1 
ATOM   3036 C CD2 . LEU A 1 411 ? 47.096  69.404  15.329  1.00 51.24  ? 506  LEU A CD2 1 
ATOM   3037 N N   . GLY A 1 412 ? 48.205  65.735  12.124  1.00 55.70  ? 507  GLY A N   1 
ATOM   3038 C CA  . GLY A 1 412 ? 48.023  64.302  12.302  1.00 52.11  ? 507  GLY A CA  1 
ATOM   3039 C C   . GLY A 1 412 ? 49.306  63.518  12.085  1.00 56.32  ? 507  GLY A C   1 
ATOM   3040 O O   . GLY A 1 412 ? 49.619  62.602  12.846  1.00 55.51  ? 507  GLY A O   1 
ATOM   3041 N N   . LYS A 1 413 ? 50.057  63.862  11.038  1.00 55.15  ? 508  LYS A N   1 
ATOM   3042 C CA  . LYS A 1 413 ? 51.344  63.206  10.790  1.00 59.74  ? 508  LYS A CA  1 
ATOM   3043 C C   . LYS A 1 413 ? 52.326  63.433  11.945  1.00 56.61  ? 508  LYS A C   1 
ATOM   3044 O O   . LYS A 1 413 ? 52.988  62.496  12.416  1.00 55.08  ? 508  LYS A O   1 
ATOM   3045 C CB  . LYS A 1 413 ? 51.952  63.721  9.487   1.00 57.60  ? 508  LYS A CB  1 
ATOM   3046 C CG  . LYS A 1 413 ? 51.265  63.284  8.210   1.00 61.98  ? 508  LYS A CG  1 
ATOM   3047 C CD  . LYS A 1 413 ? 52.215  63.536  7.037   1.00 66.74  ? 508  LYS A CD  1 
ATOM   3048 C CE  . LYS A 1 413 ? 51.555  64.307  5.907   1.00 70.90  ? 508  LYS A CE  1 
ATOM   3049 N NZ  . LYS A 1 413 ? 50.469  63.502  5.253   1.00 80.25  ? 508  LYS A NZ  1 
ATOM   3050 N N   . ILE A 1 414 ? 52.460  64.686  12.382  1.00 55.26  ? 509  ILE A N   1 
ATOM   3051 C CA  . ILE A 1 414 ? 53.351  65.001  13.499  1.00 57.31  ? 509  ILE A CA  1 
ATOM   3052 C C   . ILE A 1 414 ? 52.989  64.161  14.725  1.00 60.35  ? 509  ILE A C   1 
ATOM   3053 O O   . ILE A 1 414 ? 53.855  63.539  15.358  1.00 60.80  ? 509  ILE A O   1 
ATOM   3054 C CB  . ILE A 1 414 ? 53.298  66.510  13.804  1.00 56.12  ? 509  ILE A CB  1 
ATOM   3055 C CG1 . ILE A 1 414 ? 53.889  67.310  12.639  1.00 56.40  ? 509  ILE A CG1 1 
ATOM   3056 C CG2 . ILE A 1 414 ? 54.008  66.838  15.127  1.00 58.96  ? 509  ILE A CG2 1 
ATOM   3057 C CD1 . ILE A 1 414 ? 53.773  68.816  12.810  1.00 56.72  ? 509  ILE A CD1 1 
ATOM   3058 N N   . VAL A 1 415 ? 51.696  64.113  15.060  1.00 56.13  ? 510  VAL A N   1 
ATOM   3059 C CA  . VAL A 1 415 ? 51.262  63.433  16.277  1.00 57.86  ? 510  VAL A CA  1 
ATOM   3060 C C   . VAL A 1 415 ? 51.369  61.919  16.136  1.00 58.26  ? 510  VAL A C   1 
ATOM   3061 O O   . VAL A 1 415 ? 51.637  61.219  17.117  1.00 60.82  ? 510  VAL A O   1 
ATOM   3062 C CB  . VAL A 1 415 ? 49.830  63.870  16.643  1.00 56.11  ? 510  VAL A CB  1 
ATOM   3063 C CG1 . VAL A 1 415 ? 49.260  62.997  17.763  1.00 52.02  ? 510  VAL A CG1 1 
ATOM   3064 C CG2 . VAL A 1 415 ? 49.833  65.336  17.058  1.00 58.08  ? 510  VAL A CG2 1 
ATOM   3065 N N   . LYS A 1 416 ? 51.141  61.379  14.939  1.00 55.82  ? 511  LYS A N   1 
ATOM   3066 C CA  . LYS A 1 416 ? 51.399  59.960  14.726  1.00 58.53  ? 511  LYS A CA  1 
ATOM   3067 C C   . LYS A 1 416 ? 52.865  59.641  14.985  1.00 61.53  ? 511  LYS A C   1 
ATOM   3068 O O   . LYS A 1 416 ? 53.188  58.618  15.606  1.00 62.17  ? 511  LYS A O   1 
ATOM   3069 C CB  . LYS A 1 416 ? 50.999  59.556  13.303  1.00 56.94  ? 511  LYS A CB  1 
ATOM   3070 C CG  . LYS A 1 416 ? 51.182  58.073  12.980  1.00 57.22  ? 511  LYS A CG  1 
ATOM   3071 C CD  . LYS A 1 416 ? 50.242  57.210  13.799  1.00 62.04  ? 511  LYS A CD  1 
ATOM   3072 C CE  . LYS A 1 416 ? 50.216  55.742  13.346  1.00 62.58  ? 511  LYS A CE  1 
ATOM   3073 N NZ  . LYS A 1 416 ? 49.762  55.552  11.955  1.00 64.66  ? 511  LYS A NZ  1 
ATOM   3074 N N   . ALA A 1 417 ? 53.768  60.524  14.540  1.00 58.85  ? 512  ALA A N   1 
ATOM   3075 C CA  . ALA A 1 417 ? 55.192  60.258  14.720  1.00 61.53  ? 512  ALA A CA  1 
ATOM   3076 C C   . ALA A 1 417 ? 55.601  60.372  16.185  1.00 62.75  ? 512  ALA A C   1 
ATOM   3077 O O   . ALA A 1 417 ? 56.398  59.564  16.674  1.00 67.04  ? 512  ALA A O   1 
ATOM   3078 C CB  . ALA A 1 417 ? 56.026  61.210  13.859  1.00 61.88  ? 512  ALA A CB  1 
ATOM   3079 N N   . SER A 1 418 ? 55.078  61.366  16.903  1.00 61.66  ? 513  SER A N   1 
ATOM   3080 C CA  . SER A 1 418 ? 55.584  61.626  18.249  1.00 62.36  ? 513  SER A CA  1 
ATOM   3081 C C   . SER A 1 418 ? 54.829  60.869  19.340  1.00 61.75  ? 513  SER A C   1 
ATOM   3082 O O   . SER A 1 418 ? 55.440  60.469  20.340  1.00 62.08  ? 513  SER A O   1 
ATOM   3083 C CB  . SER A 1 418 ? 55.548  63.130  18.550  1.00 61.96  ? 513  SER A CB  1 
ATOM   3084 O OG  . SER A 1 418 ? 54.221  63.628  18.459  1.00 61.23  ? 513  SER A OG  1 
ATOM   3085 N N   . HIS A 1 419 ? 53.522  60.666  19.190  1.00 61.01  ? 514  HIS A N   1 
ATOM   3086 C CA  . HIS A 1 419 ? 52.718  59.999  20.202  1.00 60.78  ? 514  HIS A CA  1 
ATOM   3087 C C   . HIS A 1 419 ? 52.240  58.615  19.793  1.00 60.31  ? 514  HIS A C   1 
ATOM   3088 O O   . HIS A 1 419 ? 51.620  57.929  20.616  1.00 61.20  ? 514  HIS A O   1 
ATOM   3089 C CB  . HIS A 1 419 ? 51.491  60.851  20.559  1.00 57.51  ? 514  HIS A CB  1 
ATOM   3090 C CG  . HIS A 1 419 ? 51.822  62.124  21.272  1.00 58.75  ? 514  HIS A CG  1 
ATOM   3091 N ND1 . HIS A 1 419 ? 52.606  63.110  20.713  1.00 60.45  ? 514  HIS A ND1 1 
ATOM   3092 C CD2 . HIS A 1 419 ? 51.469  62.573  22.501  1.00 57.09  ? 514  HIS A CD2 1 
ATOM   3093 C CE1 . HIS A 1 419 ? 52.727  64.110  21.569  1.00 60.64  ? 514  HIS A CE1 1 
ATOM   3094 N NE2 . HIS A 1 419 ? 52.045  63.810  22.661  1.00 60.21  ? 514  HIS A NE2 1 
ATOM   3095 N N   . HIS A 1 420 ? 52.472  58.204  18.545  1.00 58.67  ? 515  HIS A N   1 
ATOM   3096 C CA  . HIS A 1 420 ? 52.125  56.860  18.067  1.00 60.28  ? 515  HIS A CA  1 
ATOM   3097 C C   . HIS A 1 420 ? 50.629  56.573  18.211  1.00 58.31  ? 515  HIS A C   1 
ATOM   3098 O O   . HIS A 1 420 ? 50.215  55.531  18.722  1.00 57.53  ? 515  HIS A O   1 
ATOM   3099 C CB  . HIS A 1 420 ? 52.964  55.802  18.787  1.00 61.70  ? 515  HIS A CB  1 
ATOM   3100 C CG  . HIS A 1 420 ? 54.411  56.163  18.886  1.00 64.99  ? 515  HIS A CG  1 
ATOM   3101 N ND1 . HIS A 1 420 ? 55.266  56.101  17.806  1.00 66.82  ? 515  HIS A ND1 1 
ATOM   3102 C CD2 . HIS A 1 420 ? 55.147  56.633  19.924  1.00 66.86  ? 515  HIS A CD2 1 
ATOM   3103 C CE1 . HIS A 1 420 ? 56.472  56.497  18.178  1.00 66.98  ? 515  HIS A CE1 1 
ATOM   3104 N NE2 . HIS A 1 420 ? 56.427  56.826  19.459  1.00 67.82  ? 515  HIS A NE2 1 
ATOM   3105 N N   . THR A 1 421 ? 49.812  57.504  17.727  1.00 56.82  ? 516  THR A N   1 
ATOM   3106 C CA  . THR A 1 421 ? 48.366  57.344  17.767  1.00 56.98  ? 516  THR A CA  1 
ATOM   3107 C C   . THR A 1 421 ? 47.753  58.008  16.539  1.00 53.99  ? 516  THR A C   1 
ATOM   3108 O O   . THR A 1 421 ? 48.339  58.920  15.948  1.00 54.89  ? 516  THR A O   1 
ATOM   3109 C CB  . THR A 1 421 ? 47.768  57.935  19.060  1.00 53.77  ? 516  THR A CB  1 
ATOM   3110 O OG1 . THR A 1 421 ? 46.353  57.736  19.074  1.00 53.72  ? 516  THR A OG1 1 
ATOM   3111 C CG2 . THR A 1 421 ? 48.058  59.425  19.173  1.00 53.98  ? 516  THR A CG2 1 
ATOM   3112 N N   . ASP A 1 422 ? 46.577  57.518  16.144  1.00 52.01  ? 517  ASP A N   1 
ATOM   3113 C CA  . ASP A 1 422 ? 45.772  58.119  15.088  1.00 48.36  ? 517  ASP A CA  1 
ATOM   3114 C C   . ASP A 1 422 ? 44.627  58.971  15.627  1.00 51.67  ? 517  ASP A C   1 
ATOM   3115 O O   . ASP A 1 422 ? 43.810  59.456  14.841  1.00 49.09  ? 517  ASP A O   1 
ATOM   3116 C CB  . ASP A 1 422 ? 45.183  57.032  14.183  1.00 50.87  ? 517  ASP A CB  1 
ATOM   3117 C CG  . ASP A 1 422 ? 46.234  56.273  13.407  1.00 54.00  ? 517  ASP A CG  1 
ATOM   3118 O OD1 . ASP A 1 422 ? 47.126  56.919  12.809  1.00 53.77  ? 517  ASP A OD1 1 
ATOM   3119 O OD2 . ASP A 1 422 ? 46.155  55.021  13.396  1.00 55.08  ? 517  ASP A OD2 1 
ATOM   3120 N N   . TYR A 1 423 ? 44.527  59.139  16.944  1.00 50.68  ? 518  TYR A N   1 
ATOM   3121 C CA  . TYR A 1 423 ? 43.357  59.753  17.562  1.00 48.89  ? 518  TYR A CA  1 
ATOM   3122 C C   . TYR A 1 423 ? 43.825  60.769  18.594  1.00 48.42  ? 518  TYR A C   1 
ATOM   3123 O O   . TYR A 1 423 ? 44.592  60.428  19.498  1.00 49.98  ? 518  TYR A O   1 
ATOM   3124 C CB  . TYR A 1 423 ? 42.483  58.669  18.195  1.00 49.77  ? 518  TYR A CB  1 
ATOM   3125 C CG  . TYR A 1 423 ? 41.418  59.143  19.155  1.00 49.71  ? 518  TYR A CG  1 
ATOM   3126 C CD1 . TYR A 1 423 ? 40.441  60.048  18.753  1.00 49.95  ? 518  TYR A CD1 1 
ATOM   3127 C CD2 . TYR A 1 423 ? 41.366  58.654  20.454  1.00 47.99  ? 518  TYR A CD2 1 
ATOM   3128 C CE1 . TYR A 1 423 ? 39.444  60.470  19.636  1.00 49.52  ? 518  TYR A CE1 1 
ATOM   3129 C CE2 . TYR A 1 423 ? 40.373  59.063  21.339  1.00 49.09  ? 518  TYR A CE2 1 
ATOM   3130 C CZ  . TYR A 1 423 ? 39.417  59.976  20.921  1.00 46.68  ? 518  TYR A CZ  1 
ATOM   3131 O OH  . TYR A 1 423 ? 38.440  60.401  21.787  1.00 46.94  ? 518  TYR A OH  1 
ATOM   3132 N N   . TYR A 1 424 ? 43.394  62.017  18.454  1.00 47.41  ? 519  TYR A N   1 
ATOM   3133 C CA  . TYR A 1 424 ? 43.755  63.009  19.468  1.00 48.50  ? 519  TYR A CA  1 
ATOM   3134 C C   . TYR A 1 424 ? 42.705  64.115  19.488  1.00 47.16  ? 519  TYR A C   1 
ATOM   3135 O O   . TYR A 1 424 ? 41.776  64.137  18.673  1.00 45.71  ? 519  TYR A O   1 
ATOM   3136 C CB  . TYR A 1 424 ? 45.175  63.569  19.246  1.00 49.23  ? 519  TYR A CB  1 
ATOM   3137 C CG  . TYR A 1 424 ? 45.366  64.129  17.863  1.00 49.92  ? 519  TYR A CG  1 
ATOM   3138 C CD1 . TYR A 1 424 ? 45.805  63.317  16.823  1.00 50.67  ? 519  TYR A CD1 1 
ATOM   3139 C CD2 . TYR A 1 424 ? 45.061  65.457  17.583  1.00 50.11  ? 519  TYR A CD2 1 
ATOM   3140 C CE1 . TYR A 1 424 ? 45.952  63.815  15.544  1.00 51.19  ? 519  TYR A CE1 1 
ATOM   3141 C CE2 . TYR A 1 424 ? 45.205  65.968  16.306  1.00 48.45  ? 519  TYR A CE2 1 
ATOM   3142 C CZ  . TYR A 1 424 ? 45.642  65.136  15.290  1.00 50.44  ? 519  TYR A CZ  1 
ATOM   3143 O OH  . TYR A 1 424 ? 45.781  65.628  14.016  1.00 53.91  ? 519  TYR A OH  1 
ATOM   3144 N N   . ILE A 1 425 ? 42.861  65.036  20.442  1.00 49.33  ? 520  ILE A N   1 
ATOM   3145 C CA  . ILE A 1 425 ? 41.875  66.065  20.759  1.00 48.77  ? 520  ILE A CA  1 
ATOM   3146 C C   . ILE A 1 425 ? 42.539  67.435  20.712  1.00 51.01  ? 520  ILE A C   1 
ATOM   3147 O O   . ILE A 1 425 ? 43.644  67.609  21.234  1.00 50.29  ? 520  ILE A O   1 
ATOM   3148 C CB  . ILE A 1 425 ? 41.261  65.843  22.156  1.00 48.73  ? 520  ILE A CB  1 
ATOM   3149 C CG1 . ILE A 1 425 ? 40.495  64.510  22.220  1.00 50.86  ? 520  ILE A CG1 1 
ATOM   3150 C CG2 . ILE A 1 425 ? 40.377  67.019  22.542  1.00 46.47  ? 520  ILE A CG2 1 
ATOM   3151 C CD1 . ILE A 1 425 ? 39.978  64.174  23.628  1.00 42.90  ? 520  ILE A CD1 1 
ATOM   3152 N N   . ILE A 1 426 ? 41.848  68.415  20.124  1.00 49.28  ? 521  ILE A N   1 
ATOM   3153 C CA  . ILE A 1 426 ? 42.239  69.817  20.183  1.00 47.38  ? 521  ILE A CA  1 
ATOM   3154 C C   . ILE A 1 426 ? 41.156  70.590  20.922  1.00 50.61  ? 521  ILE A C   1 
ATOM   3155 O O   . ILE A 1 426 ? 39.964  70.443  20.617  1.00 48.59  ? 521  ILE A O   1 
ATOM   3156 C CB  . ILE A 1 426 ? 42.467  70.405  18.778  1.00 48.78  ? 521  ILE A CB  1 
ATOM   3157 C CG1 . ILE A 1 426 ? 43.529  69.585  18.033  1.00 50.42  ? 521  ILE A CG1 1 
ATOM   3158 C CG2 . ILE A 1 426 ? 42.866  71.865  18.863  1.00 49.08  ? 521  ILE A CG2 1 
ATOM   3159 C CD1 . ILE A 1 426 ? 44.060  70.266  16.789  1.00 51.24  ? 521  ILE A CD1 1 
ATOM   3160 N N   . ILE A 1 427 ? 41.572  71.412  21.888  1.00 51.27  ? 522  ILE A N   1 
ATOM   3161 C CA  . ILE A 1 427 ? 40.670  72.221  22.699  1.00 50.36  ? 522  ILE A CA  1 
ATOM   3162 C C   . ILE A 1 427 ? 41.097  73.681  22.609  1.00 50.97  ? 522  ILE A C   1 
ATOM   3163 O O   . ILE A 1 427 ? 42.181  74.008  22.127  1.00 50.51  ? 522  ILE A O   1 
ATOM   3164 C CB  . ILE A 1 427 ? 40.639  71.772  24.178  1.00 53.92  ? 522  ILE A CB  1 
ATOM   3165 C CG1 . ILE A 1 427 ? 42.044  71.845  24.779  1.00 50.97  ? 522  ILE A CG1 1 
ATOM   3166 C CG2 . ILE A 1 427 ? 40.059  70.381  24.312  1.00 53.85  ? 522  ILE A CG2 1 
ATOM   3167 C CD1 . ILE A 1 427 ? 42.052  72.145  26.258  1.00 60.02  ? 522  ILE A CD1 1 
ATOM   3168 N N   . ASN A 1 428 ? 40.199  74.561  23.063  1.00 50.58  ? 523  ASN A N   1 
ATOM   3169 C CA  . ASN A 1 428 ? 40.460  75.996  23.242  1.00 52.96  ? 523  ASN A CA  1 
ATOM   3170 C C   . ASN A 1 428 ? 40.679  76.723  21.911  1.00 55.08  ? 523  ASN A C   1 
ATOM   3171 O O   . ASN A 1 428 ? 41.605  77.524  21.759  1.00 55.38  ? 523  ASN A O   1 
ATOM   3172 C CB  . ASN A 1 428 ? 41.638  76.228  24.196  1.00 55.28  ? 523  ASN A CB  1 
ATOM   3173 C CG  . ASN A 1 428 ? 41.325  75.815  25.636  1.00 55.95  ? 523  ASN A CG  1 
ATOM   3174 O OD1 . ASN A 1 428 ? 40.177  75.556  25.991  1.00 57.08  ? 523  ASN A OD1 1 
ATOM   3175 N ND2 . ASN A 1 428 ? 42.352  75.780  26.473  1.00 60.72  ? 523  ASN A ND2 1 
ATOM   3176 N N   . PHE A 1 429 ? 39.791  76.465  20.951  1.00 54.18  ? 524  PHE A N   1 
ATOM   3177 C CA  . PHE A 1 429 ? 39.794  77.229  19.711  1.00 54.63  ? 524  PHE A CA  1 
ATOM   3178 C C   . PHE A 1 429 ? 39.440  78.688  19.995  1.00 56.80  ? 524  PHE A C   1 
ATOM   3179 O O   . PHE A 1 429 ? 38.692  78.981  20.934  1.00 55.27  ? 524  PHE A O   1 
ATOM   3180 C CB  . PHE A 1 429 ? 38.786  76.656  18.711  1.00 54.90  ? 524  PHE A CB  1 
ATOM   3181 C CG  . PHE A 1 429 ? 39.172  75.312  18.148  1.00 53.90  ? 524  PHE A CG  1 
ATOM   3182 C CD1 . PHE A 1 429 ? 38.814  74.147  18.799  1.00 51.19  ? 524  PHE A CD1 1 
ATOM   3183 C CD2 . PHE A 1 429 ? 39.881  75.220  16.966  1.00 50.36  ? 524  PHE A CD2 1 
ATOM   3184 C CE1 . PHE A 1 429 ? 39.164  72.916  18.283  1.00 50.96  ? 524  PHE A CE1 1 
ATOM   3185 C CE2 . PHE A 1 429 ? 40.241  73.993  16.452  1.00 53.14  ? 524  PHE A CE2 1 
ATOM   3186 C CZ  . PHE A 1 429 ? 39.878  72.841  17.106  1.00 50.65  ? 524  PHE A CZ  1 
ATOM   3187 N N   . PRO A 1 430 ? 39.954  79.624  19.193  1.00 54.10  ? 525  PRO A N   1 
ATOM   3188 C CA  . PRO A 1 430 ? 39.543  81.023  19.350  1.00 57.10  ? 525  PRO A CA  1 
ATOM   3189 C C   . PRO A 1 430 ? 38.041  81.180  19.136  1.00 58.74  ? 525  PRO A C   1 
ATOM   3190 O O   . PRO A 1 430 ? 37.446  80.546  18.258  1.00 52.93  ? 525  PRO A O   1 
ATOM   3191 C CB  . PRO A 1 430 ? 40.361  81.763  18.280  1.00 56.44  ? 525  PRO A CB  1 
ATOM   3192 C CG  . PRO A 1 430 ? 40.877  80.723  17.375  1.00 61.71  ? 525  PRO A CG  1 
ATOM   3193 C CD  . PRO A 1 430 ? 40.982  79.459  18.158  1.00 58.50  ? 525  PRO A CD  1 
ATOM   3194 N N   . SER A 1 431 ? 37.432  82.018  19.987  1.00 57.14  ? 526  SER A N   1 
ATOM   3195 C CA  . SER A 1 431 ? 35.986  82.221  19.965  1.00 55.88  ? 526  SER A CA  1 
ATOM   3196 C C   . SER A 1 431 ? 35.504  82.728  18.616  1.00 57.97  ? 526  SER A C   1 
ATOM   3197 O O   . SER A 1 431 ? 34.416  82.350  18.156  1.00 55.02  ? 526  SER A O   1 
ATOM   3198 C CB  . SER A 1 431 ? 35.585  83.208  21.052  1.00 56.38  ? 526  SER A CB  1 
ATOM   3199 O OG  . SER A 1 431 ? 36.165  82.848  22.279  1.00 56.72  ? 526  SER A OG  1 
ATOM   3200 N N   . ALA A 1 432 ? 36.290  83.597  17.975  1.00 56.16  ? 527  ALA A N   1 
ATOM   3201 C CA  . ALA A 1 432 ? 35.880  84.177  16.704  1.00 56.36  ? 527  ALA A CA  1 
ATOM   3202 C C   . ALA A 1 432 ? 35.735  83.133  15.609  1.00 54.38  ? 527  ALA A C   1 
ATOM   3203 O O   . ALA A 1 432 ? 35.114  83.423  14.579  1.00 54.51  ? 527  ALA A O   1 
ATOM   3204 C CB  . ALA A 1 432 ? 36.874  85.256  16.273  1.00 56.08  ? 527  ALA A CB  1 
ATOM   3205 N N   . LEU A 1 433 ? 36.277  81.928  15.803  1.00 52.94  ? 528  LEU A N   1 
ATOM   3206 C CA  . LEU A 1 433 ? 36.222  80.881  14.788  1.00 52.81  ? 528  LEU A CA  1 
ATOM   3207 C C   . LEU A 1 433 ? 35.168  79.814  15.066  1.00 54.28  ? 528  LEU A C   1 
ATOM   3208 O O   . LEU A 1 433 ? 35.074  78.859  14.296  1.00 52.02  ? 528  LEU A O   1 
ATOM   3209 C CB  . LEU A 1 433 ? 37.590  80.196  14.636  1.00 53.81  ? 528  LEU A CB  1 
ATOM   3210 C CG  . LEU A 1 433 ? 38.813  81.000  14.182  1.00 61.96  ? 528  LEU A CG  1 
ATOM   3211 C CD1 . LEU A 1 433 ? 39.973  80.048  13.953  1.00 63.72  ? 528  LEU A CD1 1 
ATOM   3212 C CD2 . LEU A 1 433 ? 38.538  81.816  12.927  1.00 55.80  ? 528  LEU A CD2 1 
ATOM   3213 N N   . ARG A 1 434 ? 34.365  79.953  16.119  1.00 51.01  ? 529  ARG A N   1 
ATOM   3214 C CA  . ARG A 1 434 ? 33.400  78.944  16.531  1.00 50.31  ? 529  ARG A CA  1 
ATOM   3215 C C   . ARG A 1 434 ? 31.982  79.516  16.496  1.00 51.43  ? 529  ARG A C   1 
ATOM   3216 O O   . ARG A 1 434 ? 31.804  80.740  16.461  1.00 51.35  ? 529  ARG A O   1 
ATOM   3217 C CB  . ARG A 1 434 ? 33.740  78.434  17.944  1.00 50.18  ? 529  ARG A CB  1 
ATOM   3218 C CG  . ARG A 1 434 ? 35.173  77.908  18.097  1.00 51.75  ? 529  ARG A CG  1 
ATOM   3219 C CD  . ARG A 1 434 ? 35.453  76.676  17.224  1.00 49.37  ? 529  ARG A CD  1 
ATOM   3220 N NE  . ARG A 1 434 ? 34.900  75.463  17.810  1.00 52.22  ? 529  ARG A NE  1 
ATOM   3221 C CZ  . ARG A 1 434 ? 35.213  74.228  17.437  1.00 54.49  ? 529  ARG A CZ  1 
ATOM   3222 N NH1 . ARG A 1 434 ? 36.108  73.993  16.485  1.00 52.40  ? 529  ARG A NH1 1 
ATOM   3223 N NH2 . ARG A 1 434 ? 34.622  73.200  18.043  1.00 50.06  ? 529  ARG A NH2 1 
ATOM   3224 N N   . PRO A 1 435 ? 30.947  78.666  16.510  1.00 48.84  ? 530  PRO A N   1 
ATOM   3225 C CA  . PRO A 1 435 ? 29.571  79.170  16.340  1.00 51.27  ? 530  PRO A CA  1 
ATOM   3226 C C   . PRO A 1 435 ? 29.112  80.034  17.512  1.00 49.63  ? 530  PRO A C   1 
ATOM   3227 O O   . PRO A 1 435 ? 29.714  80.068  18.586  1.00 50.83  ? 530  PRO A O   1 
ATOM   3228 C CB  . PRO A 1 435 ? 28.727  77.894  16.223  1.00 50.26  ? 530  PRO A CB  1 
ATOM   3229 C CG  . PRO A 1 435 ? 29.714  76.833  15.802  1.00 52.55  ? 530  PRO A CG  1 
ATOM   3230 C CD  . PRO A 1 435 ? 30.995  77.193  16.478  1.00 47.90  ? 530  PRO A CD  1 
ATOM   3231 N N   . PHE A 1 436 ? 27.994  80.732  17.287  1.00 49.58  ? 531  PHE A N   1 
ATOM   3232 C CA  . PHE A 1 436 ? 27.512  81.725  18.248  1.00 52.85  ? 531  PHE A CA  1 
ATOM   3233 C C   . PHE A 1 436 ? 27.149  81.110  19.598  1.00 51.38  ? 531  PHE A C   1 
ATOM   3234 O O   . PHE A 1 436 ? 27.189  81.804  20.620  1.00 48.36  ? 531  PHE A O   1 
ATOM   3235 C CB  . PHE A 1 436 ? 26.293  82.467  17.684  1.00 52.69  ? 531  PHE A CB  1 
ATOM   3236 C CG  . PHE A 1 436 ? 25.037  81.628  17.661  1.00 52.33  ? 531  PHE A CG  1 
ATOM   3237 C CD1 . PHE A 1 436 ? 24.744  80.817  16.570  1.00 51.96  ? 531  PHE A CD1 1 
ATOM   3238 C CD2 . PHE A 1 436 ? 24.160  81.633  18.743  1.00 51.62  ? 531  PHE A CD2 1 
ATOM   3239 C CE1 . PHE A 1 436 ? 23.584  80.039  16.557  1.00 51.85  ? 531  PHE A CE1 1 
ATOM   3240 C CE2 . PHE A 1 436 ? 23.010  80.855  18.738  1.00 49.96  ? 531  PHE A CE2 1 
ATOM   3241 C CZ  . PHE A 1 436 ? 22.722  80.061  17.652  1.00 50.06  ? 531  PHE A CZ  1 
ATOM   3242 N N   . TYR A 1 437 ? 26.767  79.832  19.627  1.00 47.98  ? 532  TYR A N   1 
ATOM   3243 C CA  . TYR A 1 437 ? 26.321  79.216  20.873  1.00 51.66  ? 532  TYR A CA  1 
ATOM   3244 C C   . TYR A 1 437 ? 27.480  78.719  21.736  1.00 51.64  ? 532  TYR A C   1 
ATOM   3245 O O   . TYR A 1 437 ? 27.234  78.161  22.812  1.00 47.70  ? 532  TYR A O   1 
ATOM   3246 C CB  . TYR A 1 437 ? 25.347  78.064  20.574  1.00 46.52  ? 532  TYR A CB  1 
ATOM   3247 C CG  . TYR A 1 437 ? 25.853  77.101  19.533  1.00 48.41  ? 532  TYR A CG  1 
ATOM   3248 C CD1 . TYR A 1 437 ? 25.289  77.052  18.261  1.00 48.98  ? 532  TYR A CD1 1 
ATOM   3249 C CD2 . TYR A 1 437 ? 26.904  76.236  19.814  1.00 49.17  ? 532  TYR A CD2 1 
ATOM   3250 C CE1 . TYR A 1 437 ? 25.771  76.165  17.299  1.00 48.25  ? 532  TYR A CE1 1 
ATOM   3251 C CE2 . TYR A 1 437 ? 27.379  75.352  18.866  1.00 49.77  ? 532  TYR A CE2 1 
ATOM   3252 C CZ  . TYR A 1 437 ? 26.810  75.319  17.614  1.00 48.82  ? 532  TYR A CZ  1 
ATOM   3253 O OH  . TYR A 1 437 ? 27.298  74.432  16.680  1.00 56.36  ? 532  TYR A OH  1 
ATOM   3254 N N   . THR A 1 438 ? 28.724  78.916  21.284  1.00 52.80  ? 533  THR A N   1 
ATOM   3255 C CA  . THR A 1 438 ? 29.917  78.475  22.003  1.00 50.75  ? 533  THR A CA  1 
ATOM   3256 C C   . THR A 1 438 ? 30.248  79.414  23.163  1.00 51.90  ? 533  THR A C   1 
ATOM   3257 O O   . THR A 1 438 ? 30.428  80.621  22.969  1.00 53.78  ? 533  THR A O   1 
ATOM   3258 C CB  . THR A 1 438 ? 31.106  78.419  21.046  1.00 50.39  ? 533  THR A CB  1 
ATOM   3259 O OG1 . THR A 1 438 ? 30.833  77.485  19.998  1.00 49.80  ? 533  THR A OG1 1 
ATOM   3260 C CG2 . THR A 1 438 ? 32.384  78.020  21.780  1.00 49.02  ? 533  THR A CG2 1 
ATOM   3261 N N   . MET A 1 439 ? 30.372  78.854  24.363  1.00 52.82  ? 534  MET A N   1 
ATOM   3262 C CA  . MET A 1 439 ? 30.780  79.651  25.511  1.00 52.48  ? 534  MET A CA  1 
ATOM   3263 C C   . MET A 1 439 ? 32.268  79.992  25.423  1.00 55.91  ? 534  MET A C   1 
ATOM   3264 O O   . MET A 1 439 ? 33.101  79.126  25.135  1.00 54.32  ? 534  MET A O   1 
ATOM   3265 C CB  . MET A 1 439 ? 30.483  78.902  26.806  1.00 51.89  ? 534  MET A CB  1 
ATOM   3266 C CG  . MET A 1 439 ? 30.807  79.715  28.060  1.00 54.49  ? 534  MET A CG  1 
ATOM   3267 S SD  . MET A 1 439 ? 29.924  81.283  28.100  1.00 57.96  ? 534  MET A SD  1 
ATOM   3268 C CE  . MET A 1 439 ? 30.616  82.039  29.564  1.00 64.31  ? 534  MET A CE  1 
ATOM   3269 N N   . TYR A 1 440 ? 32.596  81.257  25.662  1.00 55.53  ? 535  TYR A N   1 
ATOM   3270 C CA  . TYR A 1 440 ? 33.970  81.731  25.716  1.00 58.41  ? 535  TYR A CA  1 
ATOM   3271 C C   . TYR A 1 440 ? 34.477  81.669  27.157  1.00 60.36  ? 535  TYR A C   1 
ATOM   3272 O O   . TYR A 1 440 ? 33.701  81.542  28.107  1.00 61.78  ? 535  TYR A O   1 
ATOM   3273 C CB  . TYR A 1 440 ? 34.057  83.165  25.181  1.00 59.61  ? 535  TYR A CB  1 
ATOM   3274 C CG  . TYR A 1 440 ? 33.021  84.069  25.812  1.00 61.52  ? 535  TYR A CG  1 
ATOM   3275 C CD1 . TYR A 1 440 ? 33.284  84.725  27.006  1.00 64.98  ? 535  TYR A CD1 1 
ATOM   3276 C CD2 . TYR A 1 440 ? 31.767  84.240  25.232  1.00 59.73  ? 535  TYR A CD2 1 
ATOM   3277 C CE1 . TYR A 1 440 ? 32.332  85.535  27.608  1.00 65.10  ? 535  TYR A CE1 1 
ATOM   3278 C CE2 . TYR A 1 440 ? 30.809  85.046  25.825  1.00 62.48  ? 535  TYR A CE2 1 
ATOM   3279 C CZ  . TYR A 1 440 ? 31.096  85.690  27.011  1.00 63.69  ? 535  TYR A CZ  1 
ATOM   3280 O OH  . TYR A 1 440 ? 30.146  86.491  27.596  1.00 68.37  ? 535  TYR A OH  1 
ATOM   3281 N N   . LYS A 1 441 ? 35.797  81.760  27.316  1.00 63.05  ? 536  LYS A N   1 
ATOM   3282 C CA  . LYS A 1 441 ? 36.382  81.815  28.652  1.00 68.36  ? 536  LYS A CA  1 
ATOM   3283 C C   . LYS A 1 441 ? 36.279  83.237  29.188  1.00 70.87  ? 536  LYS A C   1 
ATOM   3284 O O   . LYS A 1 441 ? 36.636  84.193  28.500  1.00 69.88  ? 536  LYS A O   1 
ATOM   3285 C CB  . LYS A 1 441 ? 37.842  81.362  28.632  1.00 67.48  ? 536  LYS A CB  1 
ATOM   3286 C CG  . LYS A 1 441 ? 38.083  80.045  27.908  1.00 65.21  ? 536  LYS A CG  1 
ATOM   3287 C CD  . LYS A 1 441 ? 39.549  79.649  27.966  1.00 67.20  ? 536  LYS A CD  1 
ATOM   3288 C CE  . LYS A 1 441 ? 39.850  78.775  29.167  1.00 69.22  ? 536  LYS A CE  1 
ATOM   3289 N NZ  . LYS A 1 441 ? 39.467  77.372  28.893  1.00 60.86  ? 536  LYS A NZ  1 
ATOM   3290 N N   . GLU A 1 442 ? 35.778  83.384  30.410  1.00 75.82  ? 537  GLU A N   1 
ATOM   3291 C CA  . GLU A 1 442 ? 35.556  84.731  30.916  1.00 80.07  ? 537  GLU A CA  1 
ATOM   3292 C C   . GLU A 1 442 ? 36.851  85.454  31.279  1.00 81.02  ? 537  GLU A C   1 
ATOM   3293 O O   . GLU A 1 442 ? 36.854  86.687  31.329  1.00 83.32  ? 537  GLU A O   1 
ATOM   3294 C CB  . GLU A 1 442 ? 34.605  84.682  32.107  1.00 80.02  ? 537  GLU A CB  1 
ATOM   3295 C CG  . GLU A 1 442 ? 33.286  84.006  31.764  1.00 80.02  ? 537  GLU A CG  1 
ATOM   3296 C CD  . GLU A 1 442 ? 32.269  84.052  32.896  1.00 92.50  ? 537  GLU A CD  1 
ATOM   3297 O OE1 . GLU A 1 442 ? 31.129  84.512  32.655  1.00 87.19  ? 537  GLU A OE1 1 
ATOM   3298 O OE2 . GLU A 1 442 ? 32.613  83.635  34.027  1.00 96.88  ? 537  GLU A OE2 1 
ATOM   3299 N N   . ASP A 1 443 ? 37.951  84.725  31.504  1.00 89.28  ? 538  ASP A N   1 
ATOM   3300 C CA  . ASP A 1 443 ? 39.253  85.361  31.699  1.00 88.77  ? 538  ASP A CA  1 
ATOM   3301 C C   . ASP A 1 443 ? 39.838  85.847  30.376  1.00 84.59  ? 538  ASP A C   1 
ATOM   3302 O O   . ASP A 1 443 ? 40.316  86.981  30.284  1.00 88.11  ? 538  ASP A O   1 
ATOM   3303 C CB  . ASP A 1 443 ? 40.224  84.393  32.382  1.00 98.06  ? 538  ASP A CB  1 
ATOM   3304 C CG  . ASP A 1 443 ? 39.845  84.107  33.828  1.00 108.36 ? 538  ASP A CG  1 
ATOM   3305 O OD1 . ASP A 1 443 ? 39.066  84.899  34.410  1.00 106.51 ? 538  ASP A OD1 1 
ATOM   3306 O OD2 . ASP A 1 443 ? 40.332  83.097  34.384  1.00 114.84 ? 538  ASP A OD2 1 
ATOM   3307 N N   . GLU A 1 444 ? 39.823  84.993  29.349  1.00 80.01  ? 539  GLU A N   1 
ATOM   3308 C CA  . GLU A 1 444 ? 40.251  85.335  27.992  1.00 78.88  ? 539  GLU A CA  1 
ATOM   3309 C C   . GLU A 1 444 ? 39.062  85.144  27.061  1.00 70.73  ? 539  GLU A C   1 
ATOM   3310 O O   . GLU A 1 444 ? 38.912  84.068  26.464  1.00 66.90  ? 539  GLU A O   1 
ATOM   3311 C CB  . GLU A 1 444 ? 41.412  84.461  27.521  1.00 79.56  ? 539  GLU A CB  1 
ATOM   3312 C CG  . GLU A 1 444 ? 42.527  84.232  28.506  1.00 86.57  ? 539  GLU A CG  1 
ATOM   3313 C CD  . GLU A 1 444 ? 43.392  83.048  28.100  1.00 88.76  ? 539  GLU A CD  1 
ATOM   3314 O OE1 . GLU A 1 444 ? 43.411  82.041  28.844  1.00 92.55  ? 539  GLU A OE1 1 
ATOM   3315 O OE2 . GLU A 1 444 ? 44.027  83.114  27.023  1.00 86.11  ? 539  GLU A OE2 1 
ATOM   3316 N N   . PRO A 1 445 ? 38.194  86.149  26.906  1.00 71.58  ? 540  PRO A N   1 
ATOM   3317 C CA  . PRO A 1 445 ? 37.025  85.973  26.023  1.00 66.99  ? 540  PRO A CA  1 
ATOM   3318 C C   . PRO A 1 445 ? 37.393  85.612  24.591  1.00 65.64  ? 540  PRO A C   1 
ATOM   3319 O O   . PRO A 1 445 ? 36.576  84.997  23.893  1.00 63.47  ? 540  PRO A O   1 
ATOM   3320 C CB  . PRO A 1 445 ? 36.312  87.329  26.104  1.00 68.82  ? 540  PRO A CB  1 
ATOM   3321 C CG  . PRO A 1 445 ? 36.740  87.895  27.440  1.00 73.17  ? 540  PRO A CG  1 
ATOM   3322 C CD  . PRO A 1 445 ? 38.164  87.436  27.625  1.00 73.40  ? 540  PRO A CD  1 
ATOM   3323 N N   . ALA A 1 446 ? 38.609  85.942  24.148  1.00 64.08  ? 541  ALA A N   1 
ATOM   3324 C CA  . ALA A 1 446 ? 39.072  85.559  22.821  1.00 62.49  ? 541  ALA A CA  1 
ATOM   3325 C C   . ALA A 1 446 ? 39.184  84.049  22.653  1.00 61.98  ? 541  ALA A C   1 
ATOM   3326 O O   . ALA A 1 446 ? 39.219  83.567  21.513  1.00 59.82  ? 541  ALA A O   1 
ATOM   3327 C CB  . ALA A 1 446 ? 40.420  86.218  22.537  1.00 60.40  ? 541  ALA A CB  1 
ATOM   3328 N N   . ILE A 1 447 ? 39.232  83.297  23.754  1.00 60.48  ? 542  ILE A N   1 
ATOM   3329 C CA  . ILE A 1 447 ? 39.396  81.848  23.736  1.00 59.17  ? 542  ILE A CA  1 
ATOM   3330 C C   . ILE A 1 447 ? 38.080  81.215  24.158  1.00 61.40  ? 542  ILE A C   1 
ATOM   3331 O O   . ILE A 1 447 ? 37.386  81.748  25.031  1.00 60.48  ? 542  ILE A O   1 
ATOM   3332 C CB  . ILE A 1 447 ? 40.543  81.409  24.667  1.00 63.53  ? 542  ILE A CB  1 
ATOM   3333 C CG1 . ILE A 1 447 ? 41.857  82.084  24.255  1.00 64.72  ? 542  ILE A CG1 1 
ATOM   3334 C CG2 . ILE A 1 447 ? 40.699  79.907  24.650  1.00 59.05  ? 542  ILE A CG2 1 
ATOM   3335 C CD1 . ILE A 1 447 ? 42.286  81.757  22.847  1.00 61.18  ? 542  ILE A CD1 1 
ATOM   3336 N N   . SER A 1 448 ? 37.729  80.085  23.540  1.00 55.71  ? 543  SER A N   1 
ATOM   3337 C CA  . SER A 1 448 ? 36.455  79.441  23.822  1.00 56.79  ? 543  SER A CA  1 
ATOM   3338 C C   . SER A 1 448 ? 36.665  78.040  24.389  1.00 55.63  ? 543  SER A C   1 
ATOM   3339 O O   . SER A 1 448 ? 37.740  77.446  24.260  1.00 55.28  ? 543  SER A O   1 
ATOM   3340 C CB  . SER A 1 448 ? 35.570  79.387  22.566  1.00 56.84  ? 543  SER A CB  1 
ATOM   3341 O OG  . SER A 1 448 ? 36.029  78.443  21.619  1.00 52.80  ? 543  SER A OG  1 
ATOM   3342 N N   . ASN A 1 449 ? 35.615  77.525  25.033  1.00 53.45  ? 544  ASN A N   1 
ATOM   3343 C CA  . ASN A 1 449 ? 35.634  76.185  25.617  1.00 53.89  ? 544  ASN A CA  1 
ATOM   3344 C C   . ASN A 1 449 ? 35.064  75.188  24.606  1.00 53.34  ? 544  ASN A C   1 
ATOM   3345 O O   . ASN A 1 449 ? 33.961  74.651  24.745  1.00 53.77  ? 544  ASN A O   1 
ATOM   3346 C CB  . ASN A 1 449 ? 34.873  76.169  26.934  1.00 55.03  ? 544  ASN A CB  1 
ATOM   3347 C CG  . ASN A 1 449 ? 35.659  76.806  28.058  1.00 59.41  ? 544  ASN A CG  1 
ATOM   3348 O OD1 . ASN A 1 449 ? 36.888  76.875  28.001  1.00 59.58  ? 544  ASN A OD1 1 
ATOM   3349 N ND2 . ASN A 1 449 ? 34.960  77.261  29.093  1.00 56.38  ? 544  ASN A ND2 1 
ATOM   3350 N N   . SER A 1 450 ? 35.870  74.935  23.578  1.00 51.67  ? 545  SER A N   1 
ATOM   3351 C CA  . SER A 1 450 ? 35.489  74.159  22.405  1.00 50.58  ? 545  SER A CA  1 
ATOM   3352 C C   . SER A 1 450 ? 36.505  73.041  22.199  1.00 52.59  ? 545  SER A C   1 
ATOM   3353 O O   . SER A 1 450 ? 37.603  73.069  22.770  1.00 52.26  ? 545  SER A O   1 
ATOM   3354 C CB  . SER A 1 450 ? 35.414  75.065  21.169  1.00 49.70  ? 545  SER A CB  1 
ATOM   3355 O OG  . SER A 1 450 ? 36.500  75.988  21.160  1.00 52.29  ? 545  SER A OG  1 
ATOM   3356 N N   . TYR A 1 451 ? 36.141  72.057  21.365  1.00 48.54  ? 546  TYR A N   1 
ATOM   3357 C CA  . TYR A 1 451 ? 36.978  70.880  21.143  1.00 47.93  ? 546  TYR A CA  1 
ATOM   3358 C C   . TYR A 1 451 ? 36.602  70.187  19.829  1.00 51.09  ? 546  TYR A C   1 
ATOM   3359 O O   . TYR A 1 451 ? 35.417  70.058  19.496  1.00 46.96  ? 546  TYR A O   1 
ATOM   3360 C CB  . TYR A 1 451 ? 36.856  69.897  22.323  1.00 47.40  ? 546  TYR A CB  1 
ATOM   3361 C CG  . TYR A 1 451 ? 35.428  69.772  22.822  1.00 49.92  ? 546  TYR A CG  1 
ATOM   3362 C CD1 . TYR A 1 451 ? 34.958  70.571  23.857  1.00 48.37  ? 546  TYR A CD1 1 
ATOM   3363 C CD2 . TYR A 1 451 ? 34.533  68.893  22.219  1.00 48.04  ? 546  TYR A CD2 1 
ATOM   3364 C CE1 . TYR A 1 451 ? 33.646  70.484  24.298  1.00 45.89  ? 546  TYR A CE1 1 
ATOM   3365 C CE2 . TYR A 1 451 ? 33.218  68.804  22.649  1.00 47.89  ? 546  TYR A CE2 1 
ATOM   3366 C CZ  . TYR A 1 451 ? 32.781  69.602  23.688  1.00 48.17  ? 546  TYR A CZ  1 
ATOM   3367 O OH  . TYR A 1 451 ? 31.471  69.510  24.100  1.00 47.21  ? 546  TYR A OH  1 
ATOM   3368 N N   . ASP A 1 452 ? 37.622  69.738  19.093  1.00 45.49  ? 547  ASP A N   1 
ATOM   3369 C CA  . ASP A 1 452 ? 37.455  68.805  17.983  1.00 47.84  ? 547  ASP A CA  1 
ATOM   3370 C C   . ASP A 1 452 ? 38.292  67.551  18.234  1.00 48.31  ? 547  ASP A C   1 
ATOM   3371 O O   . ASP A 1 452 ? 39.419  67.640  18.734  1.00 48.80  ? 547  ASP A O   1 
ATOM   3372 C CB  . ASP A 1 452 ? 37.872  69.421  16.631  1.00 47.89  ? 547  ASP A CB  1 
ATOM   3373 C CG  . ASP A 1 452 ? 37.023  70.626  16.221  1.00 51.72  ? 547  ASP A CG  1 
ATOM   3374 O OD1 . ASP A 1 452 ? 35.971  70.911  16.835  1.00 50.52  ? 547  ASP A OD1 1 
ATOM   3375 O OD2 . ASP A 1 452 ? 37.432  71.306  15.258  1.00 53.57  ? 547  ASP A OD2 1 
ATOM   3376 N N   . PHE A 1 453 ? 37.742  66.383  17.895  1.00 47.66  ? 548  PHE A N   1 
ATOM   3377 C CA  . PHE A 1 453 ? 38.476  65.123  17.911  1.00 44.84  ? 548  PHE A CA  1 
ATOM   3378 C C   . PHE A 1 453 ? 38.904  64.792  16.484  1.00 48.10  ? 548  PHE A C   1 
ATOM   3379 O O   . PHE A 1 453 ? 38.189  65.092  15.518  1.00 46.21  ? 548  PHE A O   1 
ATOM   3380 C CB  . PHE A 1 453 ? 37.643  63.945  18.452  1.00 46.30  ? 548  PHE A CB  1 
ATOM   3381 C CG  . PHE A 1 453 ? 37.189  64.066  19.907  1.00 46.30  ? 548  PHE A CG  1 
ATOM   3382 C CD1 . PHE A 1 453 ? 37.313  65.251  20.630  1.00 45.21  ? 548  PHE A CD1 1 
ATOM   3383 C CD2 . PHE A 1 453 ? 36.631  62.956  20.544  1.00 45.36  ? 548  PHE A CD2 1 
ATOM   3384 C CE1 . PHE A 1 453 ? 36.884  65.334  21.951  1.00 46.60  ? 548  PHE A CE1 1 
ATOM   3385 C CE2 . PHE A 1 453 ? 36.199  63.024  21.874  1.00 45.88  ? 548  PHE A CE2 1 
ATOM   3386 C CZ  . PHE A 1 453 ? 36.323  64.213  22.577  1.00 47.72  ? 548  PHE A CZ  1 
ATOM   3387 N N   . PHE A 1 454 ? 40.065  64.141  16.360  1.00 46.03  ? 549  PHE A N   1 
ATOM   3388 C CA  . PHE A 1 454 ? 40.647  63.802  15.073  1.00 45.71  ? 549  PHE A CA  1 
ATOM   3389 C C   . PHE A 1 454 ? 40.975  62.316  15.022  1.00 48.10  ? 549  PHE A C   1 
ATOM   3390 O O   . PHE A 1 454 ? 41.459  61.737  16.012  1.00 48.57  ? 549  PHE A O   1 
ATOM   3391 C CB  . PHE A 1 454 ? 41.927  64.634  14.793  1.00 45.96  ? 549  PHE A CB  1 
ATOM   3392 C CG  . PHE A 1 454 ? 41.665  66.109  14.691  1.00 47.76  ? 549  PHE A CG  1 
ATOM   3393 C CD1 . PHE A 1 454 ? 41.565  66.717  13.451  1.00 45.85  ? 549  PHE A CD1 1 
ATOM   3394 C CD2 . PHE A 1 454 ? 41.464  66.875  15.833  1.00 45.97  ? 549  PHE A CD2 1 
ATOM   3395 C CE1 . PHE A 1 454 ? 41.289  68.065  13.341  1.00 49.54  ? 549  PHE A CE1 1 
ATOM   3396 C CE2 . PHE A 1 454 ? 41.186  68.230  15.736  1.00 47.12  ? 549  PHE A CE2 1 
ATOM   3397 C CZ  . PHE A 1 454 ? 41.098  68.825  14.478  1.00 49.05  ? 549  PHE A CZ  1 
ATOM   3398 N N   . MET A 1 455 ? 40.706  61.731  13.849  1.00 43.52  ? 550  MET A N   1 
ATOM   3399 C CA  . MET A 1 455 ? 41.109  60.380  13.462  1.00 48.35  ? 550  MET A CA  1 
ATOM   3400 C C   . MET A 1 455 ? 41.932  60.473  12.180  1.00 49.47  ? 550  MET A C   1 
ATOM   3401 O O   . MET A 1 455 ? 41.480  61.059  11.184  1.00 47.80  ? 550  MET A O   1 
ATOM   3402 C CB  . MET A 1 455 ? 39.895  59.470  13.247  1.00 44.56  ? 550  MET A CB  1 
ATOM   3403 C CG  . MET A 1 455 ? 39.032  59.241  14.488  1.00 46.10  ? 550  MET A CG  1 
ATOM   3404 S SD  . MET A 1 455 ? 37.536  58.257  14.120  1.00 43.57  ? 550  MET A SD  1 
ATOM   3405 C CE  . MET A 1 455 ? 38.254  56.768  13.451  1.00 42.46  ? 550  MET A CE  1 
ATOM   3406 N N   . ARG A 1 456 ? 43.147  59.923  12.215  1.00 46.84  ? 551  ARG A N   1 
ATOM   3407 C CA  . ARG A 1 456 ? 44.076  59.971  11.084  1.00 49.14  ? 551  ARG A CA  1 
ATOM   3408 C C   . ARG A 1 456 ? 44.240  61.391  10.538  1.00 50.01  ? 551  ARG A C   1 
ATOM   3409 O O   . ARG A 1 456 ? 44.337  61.606  9.328   1.00 48.51  ? 551  ARG A O   1 
ATOM   3410 C CB  . ARG A 1 456 ? 43.643  59.009  9.973   1.00 49.25  ? 551  ARG A CB  1 
ATOM   3411 C CG  . ARG A 1 456 ? 43.693  57.533  10.354  1.00 47.99  ? 551  ARG A CG  1 
ATOM   3412 C CD  . ARG A 1 456 ? 43.468  56.642  9.131   1.00 46.01  ? 551  ARG A CD  1 
ATOM   3413 N NE  . ARG A 1 456 ? 43.038  55.293  9.494   1.00 51.08  ? 551  ARG A NE  1 
ATOM   3414 C CZ  . ARG A 1 456 ? 43.857  54.272  9.724   1.00 51.28  ? 551  ARG A CZ  1 
ATOM   3415 N NH1 . ARG A 1 456 ? 45.171  54.405  9.639   1.00 46.39  ? 551  ARG A NH1 1 
ATOM   3416 N NH2 . ARG A 1 456 ? 43.343  53.089  10.057  1.00 48.96  ? 551  ARG A NH2 1 
ATOM   3417 N N   . GLY A 1 457 ? 44.264  62.374  11.437  1.00 48.70  ? 552  GLY A N   1 
ATOM   3418 C CA  . GLY A 1 457 ? 44.463  63.754  11.039  1.00 46.70  ? 552  GLY A CA  1 
ATOM   3419 C C   . GLY A 1 457 ? 43.237  64.482  10.512  1.00 51.28  ? 552  GLY A C   1 
ATOM   3420 O O   . GLY A 1 457 ? 43.380  65.602  10.004  1.00 48.50  ? 552  GLY A O   1 
ATOM   3421 N N   . GLU A 1 458 ? 42.033  63.902  10.617  1.00 45.52  ? 553  GLU A N   1 
ATOM   3422 C CA  . GLU A 1 458 ? 40.836  64.569  10.111  1.00 48.26  ? 553  GLU A CA  1 
ATOM   3423 C C   . GLU A 1 458 ? 39.767  64.663  11.197  1.00 46.95  ? 553  GLU A C   1 
ATOM   3424 O O   . GLU A 1 458 ? 39.604  63.750  12.013  1.00 43.57  ? 553  GLU A O   1 
ATOM   3425 C CB  . GLU A 1 458 ? 40.305  63.858  8.861   1.00 47.63  ? 553  GLU A CB  1 
ATOM   3426 C CG  . GLU A 1 458 ? 41.361  63.845  7.749   1.00 51.88  ? 553  GLU A CG  1 
ATOM   3427 C CD  . GLU A 1 458 ? 40.903  63.259  6.426   1.00 54.18  ? 553  GLU A CD  1 
ATOM   3428 O OE1 . GLU A 1 458 ? 39.783  63.560  5.968   1.00 52.56  ? 553  GLU A OE1 1 
ATOM   3429 O OE2 . GLU A 1 458 ? 41.696  62.503  5.832   1.00 55.47  ? 553  GLU A OE2 1 
ATOM   3430 N N   . GLU A 1 459 ? 39.078  65.800  11.224  1.00 46.28  ? 554  GLU A N   1 
ATOM   3431 C CA  . GLU A 1 459 ? 38.072  66.075  12.245  1.00 49.84  ? 554  GLU A CA  1 
ATOM   3432 C C   . GLU A 1 459 ? 36.874  65.138  12.092  1.00 47.08  ? 554  GLU A C   1 
ATOM   3433 O O   . GLU A 1 459 ? 36.359  64.967  10.983  1.00 49.86  ? 554  GLU A O   1 
ATOM   3434 C CB  . GLU A 1 459 ? 37.621  67.535  12.134  1.00 48.12  ? 554  GLU A CB  1 
ATOM   3435 C CG  . GLU A 1 459 ? 36.587  67.942  13.177  1.00 53.04  ? 554  GLU A CG  1 
ATOM   3436 C CD  . GLU A 1 459 ? 35.410  68.688  12.571  1.00 59.81  ? 554  GLU A CD  1 
ATOM   3437 O OE1 . GLU A 1 459 ? 34.279  68.147  12.615  1.00 61.97  ? 554  GLU A OE1 1 
ATOM   3438 O OE2 . GLU A 1 459 ? 35.620  69.800  12.033  1.00 63.96  ? 554  GLU A OE2 1 
ATOM   3439 N N   . ILE A 1 460 ? 36.437  64.527  13.204  1.00 46.84  ? 555  ILE A N   1 
ATOM   3440 C CA  . ILE A 1 460 ? 35.318  63.574  13.224  1.00 47.65  ? 555  ILE A CA  1 
ATOM   3441 C C   . ILE A 1 460 ? 34.198  64.056  14.140  1.00 47.62  ? 555  ILE A C   1 
ATOM   3442 O O   . ILE A 1 460 ? 33.003  63.729  13.940  1.00 49.28  ? 555  ILE A O   1 
ATOM   3443 C CB  . ILE A 1 460 ? 35.770  62.173  13.691  1.00 47.02  ? 555  ILE A CB  1 
ATOM   3444 C CG1 . ILE A 1 460 ? 36.736  62.290  14.879  1.00 47.42  ? 555  ILE A CG1 1 
ATOM   3445 C CG2 . ILE A 1 460 ? 36.354  61.386  12.551  1.00 48.14  ? 555  ILE A CG2 1 
ATOM   3446 C CD1 . ILE A 1 460 ? 36.471  61.263  15.974  1.00 49.32  ? 555  ILE A CD1 1 
ATOM   3447 N N   . LEU A 1 461 ? 34.601  64.810  15.171  1.00 48.88  ? 556  LEU A N   1 
ATOM   3448 C CA  . LEU A 1 461 ? 33.718  65.321  16.212  1.00 46.77  ? 556  LEU A CA  1 
ATOM   3449 C C   . LEU A 1 461 ? 33.979  66.802  16.415  1.00 50.29  ? 556  LEU A C   1 
ATOM   3450 O O   . LEU A 1 461 ? 35.135  67.241  16.461  1.00 46.92  ? 556  LEU A O   1 
ATOM   3451 C CB  . LEU A 1 461 ? 33.916  64.593  17.547  1.00 41.98  ? 556  LEU A CB  1 
ATOM   3452 C CG  . LEU A 1 461 ? 33.120  65.083  18.768  1.00 46.42  ? 556  LEU A CG  1 
ATOM   3453 C CD1 . LEU A 1 461 ? 32.774  63.911  19.682  1.00 44.69  ? 556  LEU A CD1 1 
ATOM   3454 C CD2 . LEU A 1 461 ? 33.853  66.175  19.556  1.00 46.55  ? 556  LEU A CD2 1 
ATOM   3455 N N   . SER A 1 462 ? 32.898  67.560  16.570  1.00 47.89  ? 557  SER A N   1 
ATOM   3456 C CA  . SER A 1 462 ? 32.999  68.967  16.936  1.00 49.29  ? 557  SER A CA  1 
ATOM   3457 C C   . SER A 1 462 ? 31.990  69.272  18.030  1.00 47.71  ? 557  SER A C   1 
ATOM   3458 O O   . SER A 1 462 ? 30.845  68.818  17.958  1.00 44.07  ? 557  SER A O   1 
ATOM   3459 C CB  . SER A 1 462 ? 32.748  69.864  15.733  1.00 47.47  ? 557  SER A CB  1 
ATOM   3460 O OG  . SER A 1 462 ? 33.332  71.133  15.939  1.00 55.45  ? 557  SER A OG  1 
ATOM   3461 N N   . GLY A 1 463 ? 32.396  70.052  19.028  1.00 46.69  ? 558  GLY A N   1 
ATOM   3462 C CA  . GLY A 1 463 ? 31.442  70.430  20.055  1.00 47.62  ? 558  GLY A CA  1 
ATOM   3463 C C   . GLY A 1 463 ? 31.962  71.515  20.971  1.00 47.77  ? 558  GLY A C   1 
ATOM   3464 O O   . GLY A 1 463 ? 33.039  72.079  20.757  1.00 47.77  ? 558  GLY A O   1 
ATOM   3465 N N   . SER A 1 464 ? 31.173  71.800  22.006  1.00 46.37  ? 559  SER A N   1 
ATOM   3466 C CA  . SER A 1 464 ? 31.597  72.823  22.959  1.00 49.29  ? 559  SER A CA  1 
ATOM   3467 C C   . SER A 1 464 ? 30.689  72.857  24.180  1.00 48.79  ? 559  SER A C   1 
ATOM   3468 O O   . SER A 1 464 ? 29.577  72.317  24.177  1.00 43.42  ? 559  SER A O   1 
ATOM   3469 C CB  . SER A 1 464 ? 31.631  74.222  22.328  1.00 49.55  ? 559  SER A CB  1 
ATOM   3470 O OG  . SER A 1 464 ? 30.330  74.760  22.203  1.00 49.82  ? 559  SER A OG  1 
ATOM   3471 N N   . GLN A 1 465 ? 31.218  73.484  25.238  1.00 49.34  ? 560  GLN A N   1 
ATOM   3472 C CA  . GLN A 1 465 ? 30.381  74.081  26.266  1.00 47.70  ? 560  GLN A CA  1 
ATOM   3473 C C   . GLN A 1 465 ? 29.468  75.111  25.620  1.00 49.39  ? 560  GLN A C   1 
ATOM   3474 O O   . GLN A 1 465 ? 29.896  75.899  24.772  1.00 48.21  ? 560  GLN A O   1 
ATOM   3475 C CB  . GLN A 1 465 ? 31.245  74.746  27.344  1.00 50.21  ? 560  GLN A CB  1 
ATOM   3476 C CG  . GLN A 1 465 ? 30.474  75.478  28.449  1.00 50.18  ? 560  GLN A CG  1 
ATOM   3477 C CD  . GLN A 1 465 ? 31.400  76.251  29.392  1.00 54.95  ? 560  GLN A CD  1 
ATOM   3478 O OE1 . GLN A 1 465 ? 32.484  76.667  29.011  1.00 60.40  ? 560  GLN A OE1 1 
ATOM   3479 N NE2 . GLN A 1 465 ? 30.966  76.442  30.622  1.00 60.84  ? 560  GLN A NE2 1 
ATOM   3480 N N   . ARG A 1 466 ? 28.201  75.104  26.014  1.00 48.03  ? 561  ARG A N   1 
ATOM   3481 C CA  . ARG A 1 466 ? 27.237  76.030  25.443  1.00 48.67  ? 561  ARG A CA  1 
ATOM   3482 C C   . ARG A 1 466 ? 27.022  77.223  26.366  1.00 51.48  ? 561  ARG A C   1 
ATOM   3483 O O   . ARG A 1 466 ? 27.148  77.121  27.590  1.00 50.37  ? 561  ARG A O   1 
ATOM   3484 C CB  . ARG A 1 466 ? 25.907  75.323  25.184  1.00 47.47  ? 561  ARG A CB  1 
ATOM   3485 C CG  . ARG A 1 466 ? 26.045  73.892  24.655  1.00 48.39  ? 561  ARG A CG  1 
ATOM   3486 C CD  . ARG A 1 466 ? 26.728  73.826  23.290  1.00 45.17  ? 561  ARG A CD  1 
ATOM   3487 N NE  . ARG A 1 466 ? 26.430  72.573  22.613  1.00 46.17  ? 561  ARG A NE  1 
ATOM   3488 C CZ  . ARG A 1 466 ? 27.107  72.092  21.579  1.00 48.40  ? 561  ARG A CZ  1 
ATOM   3489 N NH1 . ARG A 1 466 ? 28.174  72.712  21.099  1.00 47.22  ? 561  ARG A NH1 1 
ATOM   3490 N NH2 . ARG A 1 466 ? 26.703  70.961  21.011  1.00 44.69  ? 561  ARG A NH2 1 
ATOM   3491 N N   . ILE A 1 467 ? 26.707  78.367  25.764  1.00 50.66  ? 562  ILE A N   1 
ATOM   3492 C CA  . ILE A 1 467 ? 26.212  79.489  26.550  1.00 51.98  ? 562  ILE A CA  1 
ATOM   3493 C C   . ILE A 1 467 ? 24.869  79.090  27.149  1.00 52.84  ? 562  ILE A C   1 
ATOM   3494 O O   . ILE A 1 467 ? 23.913  78.790  26.422  1.00 50.23  ? 562  ILE A O   1 
ATOM   3495 C CB  . ILE A 1 467 ? 26.087  80.752  25.692  1.00 51.95  ? 562  ILE A CB  1 
ATOM   3496 C CG1 . ILE A 1 467 ? 27.445  81.132  25.094  1.00 49.73  ? 562  ILE A CG1 1 
ATOM   3497 C CG2 . ILE A 1 467 ? 25.475  81.891  26.514  1.00 52.84  ? 562  ILE A CG2 1 
ATOM   3498 C CD1 . ILE A 1 467 ? 27.377  82.237  24.067  1.00 51.16  ? 562  ILE A CD1 1 
ATOM   3499 N N   . SER A 1 468 ? 24.797  79.057  28.479  1.00 50.85  ? 563  SER A N   1 
ATOM   3500 C CA  . SER A 1 468 ? 23.578  78.690  29.182  1.00 51.60  ? 563  SER A CA  1 
ATOM   3501 C C   . SER A 1 468 ? 23.025  79.851  30.007  1.00 54.32  ? 563  SER A C   1 
ATOM   3502 O O   . SER A 1 468 ? 22.320  79.635  31.000  1.00 59.58  ? 563  SER A O   1 
ATOM   3503 C CB  . SER A 1 468 ? 23.841  77.462  30.050  1.00 53.27  ? 563  SER A CB  1 
ATOM   3504 O OG  . SER A 1 468 ? 24.874  77.725  30.987  1.00 59.09  ? 563  SER A OG  1 
ATOM   3505 N N   . ASP A 1 469 ? 23.354  81.079  29.625  1.00 55.24  ? 564  ASP A N   1 
ATOM   3506 C CA  . ASP A 1 469 ? 22.799  82.287  30.223  1.00 55.63  ? 564  ASP A CA  1 
ATOM   3507 C C   . ASP A 1 469 ? 22.119  83.062  29.106  1.00 58.38  ? 564  ASP A C   1 
ATOM   3508 O O   . ASP A 1 469 ? 22.773  83.425  28.121  1.00 57.98  ? 564  ASP A O   1 
ATOM   3509 C CB  . ASP A 1 469 ? 23.891  83.123  30.882  1.00 59.45  ? 564  ASP A CB  1 
ATOM   3510 C CG  . ASP A 1 469 ? 23.361  84.435  31.463  1.00 63.20  ? 564  ASP A CG  1 
ATOM   3511 O OD1 . ASP A 1 469 ? 23.408  84.595  32.693  1.00 69.18  ? 564  ASP A OD1 1 
ATOM   3512 O OD2 . ASP A 1 469 ? 22.900  85.317  30.706  1.00 61.22  ? 564  ASP A OD2 1 
ATOM   3513 N N   . VAL A 1 470 ? 20.814  83.320  29.259  1.00 57.66  ? 565  VAL A N   1 
ATOM   3514 C CA  . VAL A 1 470 ? 20.032  83.834  28.138  1.00 58.60  ? 565  VAL A CA  1 
ATOM   3515 C C   . VAL A 1 470 ? 20.540  85.202  27.702  1.00 60.01  ? 565  VAL A C   1 
ATOM   3516 O O   . VAL A 1 470 ? 20.535  85.523  26.505  1.00 60.22  ? 565  VAL A O   1 
ATOM   3517 C CB  . VAL A 1 470 ? 18.536  83.856  28.512  1.00 56.75  ? 565  VAL A CB  1 
ATOM   3518 C CG1 . VAL A 1 470 ? 18.294  84.747  29.716  1.00 59.51  ? 565  VAL A CG1 1 
ATOM   3519 C CG2 . VAL A 1 470 ? 17.702  84.309  27.339  1.00 57.31  ? 565  VAL A CG2 1 
ATOM   3520 N N   . ASN A 1 471 ? 21.018  86.010  28.652  1.00 61.19  ? 566  ASN A N   1 
ATOM   3521 C CA  . ASN A 1 471 ? 21.506  87.347  28.324  1.00 61.11  ? 566  ASN A CA  1 
ATOM   3522 C C   . ASN A 1 471 ? 22.863  87.287  27.626  1.00 60.34  ? 566  ASN A C   1 
ATOM   3523 O O   . ASN A 1 471 ? 23.093  88.003  26.644  1.00 61.39  ? 566  ASN A O   1 
ATOM   3524 C CB  . ASN A 1 471 ? 21.579  88.202  29.591  1.00 61.94  ? 566  ASN A CB  1 
ATOM   3525 C CG  . ASN A 1 471 ? 20.258  88.231  30.366  1.00 69.59  ? 566  ASN A CG  1 
ATOM   3526 O OD1 . ASN A 1 471 ? 19.241  88.739  29.884  1.00 69.24  ? 566  ASN A OD1 1 
ATOM   3527 N ND2 . ASN A 1 471 ? 20.281  87.697  31.586  1.00 72.25  ? 566  ASN A ND2 1 
ATOM   3528 N N   . LEU A 1 472 ? 23.772  86.432  28.104  1.00 61.20  ? 567  LEU A N   1 
ATOM   3529 C CA  . LEU A 1 472 ? 25.027  86.241  27.383  1.00 61.13  ? 567  LEU A CA  1 
ATOM   3530 C C   . LEU A 1 472 ? 24.771  85.701  25.983  1.00 58.72  ? 567  LEU A C   1 
ATOM   3531 O O   . LEU A 1 472 ? 25.451  86.092  25.027  1.00 59.21  ? 567  LEU A O   1 
ATOM   3532 C CB  . LEU A 1 472 ? 25.958  85.303  28.153  1.00 61.01  ? 567  LEU A CB  1 
ATOM   3533 C CG  . LEU A 1 472 ? 26.510  85.794  29.492  1.00 66.50  ? 567  LEU A CG  1 
ATOM   3534 C CD1 . LEU A 1 472 ? 27.597  84.851  29.983  1.00 66.46  ? 567  LEU A CD1 1 
ATOM   3535 C CD2 . LEU A 1 472 ? 27.041  87.218  29.385  1.00 64.87  ? 567  LEU A CD2 1 
ATOM   3536 N N   . LEU A 1 473 ? 23.788  84.804  25.845  1.00 56.32  ? 568  LEU A N   1 
ATOM   3537 C CA  . LEU A 1 473 ? 23.457  84.255  24.533  1.00 58.14  ? 568  LEU A CA  1 
ATOM   3538 C C   . LEU A 1 473 ? 22.968  85.347  23.588  1.00 58.40  ? 568  LEU A C   1 
ATOM   3539 O O   . LEU A 1 473 ? 23.398  85.410  22.430  1.00 57.54  ? 568  LEU A O   1 
ATOM   3540 C CB  . LEU A 1 473 ? 22.408  83.145  24.674  1.00 53.48  ? 568  LEU A CB  1 
ATOM   3541 C CG  . LEU A 1 473 ? 21.909  82.472  23.391  1.00 54.47  ? 568  LEU A CG  1 
ATOM   3542 C CD1 . LEU A 1 473 ? 23.019  81.722  22.681  1.00 48.57  ? 568  LEU A CD1 1 
ATOM   3543 C CD2 . LEU A 1 473 ? 20.738  81.522  23.692  1.00 52.78  ? 568  LEU A CD2 1 
ATOM   3544 N N   . LEU A 1 474 ? 22.070  86.221  24.061  1.00 58.48  ? 569  LEU A N   1 
ATOM   3545 C CA  . LEU A 1 474 ? 21.637  87.338  23.223  1.00 58.12  ? 569  LEU A CA  1 
ATOM   3546 C C   . LEU A 1 474 ? 22.814  88.229  22.834  1.00 59.38  ? 569  LEU A C   1 
ATOM   3547 O O   . LEU A 1 474 ? 22.926  88.663  21.674  1.00 59.71  ? 569  LEU A O   1 
ATOM   3548 C CB  . LEU A 1 474 ? 20.565  88.148  23.948  1.00 59.54  ? 569  LEU A CB  1 
ATOM   3549 C CG  . LEU A 1 474 ? 19.165  87.528  23.995  1.00 62.48  ? 569  LEU A CG  1 
ATOM   3550 C CD1 . LEU A 1 474 ? 18.307  88.243  25.036  1.00 55.40  ? 569  LEU A CD1 1 
ATOM   3551 C CD2 . LEU A 1 474 ? 18.508  87.594  22.624  1.00 56.32  ? 569  LEU A CD2 1 
ATOM   3552 N N   . GLU A 1 475 ? 23.703  88.514  23.791  1.00 60.24  ? 570  GLU A N   1 
ATOM   3553 C CA  . GLU A 1 475 ? 24.885  89.313  23.474  1.00 60.98  ? 570  GLU A CA  1 
ATOM   3554 C C   . GLU A 1 475 ? 25.719  88.657  22.384  1.00 58.72  ? 570  GLU A C   1 
ATOM   3555 O O   . GLU A 1 475 ? 26.167  89.327  21.453  1.00 58.69  ? 570  GLU A O   1 
ATOM   3556 C CB  . GLU A 1 475 ? 25.735  89.527  24.722  1.00 65.07  ? 570  GLU A CB  1 
ATOM   3557 C CG  . GLU A 1 475 ? 25.159  90.524  25.720  1.00 72.40  ? 570  GLU A CG  1 
ATOM   3558 C CD  . GLU A 1 475 ? 26.048  90.676  26.941  1.00 79.10  ? 570  GLU A CD  1 
ATOM   3559 O OE1 . GLU A 1 475 ? 27.219  90.236  26.861  1.00 78.83  ? 570  GLU A OE1 1 
ATOM   3560 O OE2 . GLU A 1 475 ? 25.583  91.228  27.971  1.00 83.98  ? 570  GLU A OE2 1 
ATOM   3561 N N   . ASN A 1 476 ? 25.929  87.344  22.472  1.00 59.30  ? 571  ASN A N   1 
ATOM   3562 C CA  . ASN A 1 476 ? 26.776  86.679  21.484  1.00 61.07  ? 571  ASN A CA  1 
ATOM   3563 C C   . ASN A 1 476 ? 26.096  86.581  20.124  1.00 59.24  ? 571  ASN A C   1 
ATOM   3564 O O   . ASN A 1 476 ? 26.773  86.603  19.092  1.00 60.56  ? 571  ASN A O   1 
ATOM   3565 C CB  . ASN A 1 476 ? 27.183  85.286  21.970  1.00 56.06  ? 571  ASN A CB  1 
ATOM   3566 C CG  . ASN A 1 476 ? 28.641  84.989  21.691  1.00 58.49  ? 571  ASN A CG  1 
ATOM   3567 O OD1 . ASN A 1 476 ? 29.484  85.864  21.853  1.00 58.63  ? 571  ASN A OD1 1 
ATOM   3568 N ND2 . ASN A 1 476 ? 28.946  83.762  21.245  1.00 54.50  ? 571  ASN A ND2 1 
ATOM   3569 N N   . ILE A 1 477 ? 24.771  86.451  20.098  1.00 60.72  ? 572  ILE A N   1 
ATOM   3570 C CA  . ILE A 1 477 ? 24.057  86.462  18.826  1.00 59.10  ? 572  ILE A CA  1 
ATOM   3571 C C   . ILE A 1 477 ? 24.200  87.822  18.149  1.00 58.90  ? 572  ILE A C   1 
ATOM   3572 O O   . ILE A 1 477 ? 24.417  87.907  16.933  1.00 59.11  ? 572  ILE A O   1 
ATOM   3573 C CB  . ILE A 1 477 ? 22.580  86.085  19.045  1.00 59.13  ? 572  ILE A CB  1 
ATOM   3574 C CG1 . ILE A 1 477 ? 22.449  84.597  19.365  1.00 55.04  ? 572  ILE A CG1 1 
ATOM   3575 C CG2 . ILE A 1 477 ? 21.737  86.441  17.818  1.00 58.71  ? 572  ILE A CG2 1 
ATOM   3576 C CD1 . ILE A 1 477 ? 21.122  84.241  20.007  1.00 53.28  ? 572  ILE A CD1 1 
ATOM   3577 N N   . LYS A 1 478 ? 24.082  88.907  18.917  1.00 57.33  ? 573  LYS A N   1 
ATOM   3578 C CA  . LYS A 1 478 ? 24.323  90.224  18.330  1.00 62.06  ? 573  LYS A CA  1 
ATOM   3579 C C   . LYS A 1 478 ? 25.787  90.386  17.929  1.00 61.95  ? 573  LYS A C   1 
ATOM   3580 O O   . LYS A 1 478 ? 26.091  91.007  16.905  1.00 62.27  ? 573  LYS A O   1 
ATOM   3581 C CB  . LYS A 1 478 ? 23.904  91.333  19.296  1.00 63.64  ? 573  LYS A CB  1 
ATOM   3582 C CG  . LYS A 1 478 ? 24.042  92.734  18.706  1.00 65.00  ? 573  LYS A CG  1 
ATOM   3583 C CD  . LYS A 1 478 ? 23.000  93.692  19.272  1.00 70.52  ? 573  LYS A CD  1 
ATOM   3584 C CE  . LYS A 1 478 ? 22.891  94.984  18.435  1.00 81.53  ? 573  LYS A CE  1 
ATOM   3585 N NZ  . LYS A 1 478 ? 21.577  95.120  17.708  1.00 81.98  ? 573  LYS A NZ  1 
ATOM   3586 N N   . ARG A 1 479 ? 26.701  89.819  18.720  1.00 61.58  ? 574  ARG A N   1 
ATOM   3587 C CA  . ARG A 1 479 ? 28.127  89.867  18.406  1.00 62.40  ? 574  ARG A CA  1 
ATOM   3588 C C   . ARG A 1 479 ? 28.419  89.233  17.056  1.00 61.35  ? 574  ARG A C   1 
ATOM   3589 O O   . ARG A 1 479 ? 29.329  89.671  16.347  1.00 61.09  ? 574  ARG A O   1 
ATOM   3590 C CB  . ARG A 1 479 ? 28.916  89.163  19.519  1.00 64.06  ? 574  ARG A CB  1 
ATOM   3591 C CG  . ARG A 1 479 ? 30.400  89.501  19.581  1.00 67.79  ? 574  ARG A CG  1 
ATOM   3592 C CD  . ARG A 1 479 ? 31.050  89.026  20.890  1.00 68.86  ? 574  ARG A CD  1 
ATOM   3593 N NE  . ARG A 1 479 ? 30.715  89.867  22.040  1.00 67.93  ? 574  ARG A NE  1 
ATOM   3594 C CZ  . ARG A 1 479 ? 30.028  89.462  23.103  1.00 70.21  ? 574  ARG A CZ  1 
ATOM   3595 N NH1 . ARG A 1 479 ? 29.581  88.216  23.210  1.00 62.19  ? 574  ARG A NH1 1 
ATOM   3596 N NH2 . ARG A 1 479 ? 29.783  90.326  24.085  1.00 73.98  ? 574  ARG A NH2 1 
ATOM   3597 N N   . PHE A 1 480 ? 27.658  88.208  16.684  1.00 62.24  ? 575  PHE A N   1 
ATOM   3598 C CA  . PHE A 1 480 ? 27.842  87.511  15.424  1.00 58.48  ? 575  PHE A CA  1 
ATOM   3599 C C   . PHE A 1 480 ? 26.954  88.057  14.312  1.00 60.93  ? 575  PHE A C   1 
ATOM   3600 O O   . PHE A 1 480 ? 26.915  87.477  13.223  1.00 61.03  ? 575  PHE A O   1 
ATOM   3601 C CB  . PHE A 1 480 ? 27.584  86.017  15.617  1.00 60.56  ? 575  PHE A CB  1 
ATOM   3602 C CG  . PHE A 1 480 ? 28.761  85.262  16.178  1.00 59.98  ? 575  PHE A CG  1 
ATOM   3603 C CD1 . PHE A 1 480 ? 29.517  84.434  15.367  1.00 60.36  ? 575  PHE A CD1 1 
ATOM   3604 C CD2 . PHE A 1 480 ? 29.118  85.389  17.507  1.00 59.69  ? 575  PHE A CD2 1 
ATOM   3605 C CE1 . PHE A 1 480 ? 30.604  83.734  15.879  1.00 59.23  ? 575  PHE A CE1 1 
ATOM   3606 C CE2 . PHE A 1 480 ? 30.202  84.695  18.021  1.00 57.68  ? 575  PHE A CE2 1 
ATOM   3607 C CZ  . PHE A 1 480 ? 30.942  83.869  17.207  1.00 58.44  ? 575  PHE A CZ  1 
ATOM   3608 N N   . ASN A 1 481 ? 26.246  89.161  14.556  1.00 61.28  ? 576  ASN A N   1 
ATOM   3609 C CA  . ASN A 1 481 ? 25.354  89.767  13.560  1.00 64.28  ? 576  ASN A CA  1 
ATOM   3610 C C   . ASN A 1 481 ? 24.310  88.776  13.062  1.00 61.67  ? 576  ASN A C   1 
ATOM   3611 O O   . ASN A 1 481 ? 24.013  88.713  11.868  1.00 64.00  ? 576  ASN A O   1 
ATOM   3612 C CB  . ASN A 1 481 ? 26.136  90.349  12.383  1.00 64.54  ? 576  ASN A CB  1 
ATOM   3613 C CG  . ASN A 1 481 ? 27.080  91.432  12.817  1.00 72.61  ? 576  ASN A CG  1 
ATOM   3614 O OD1 . ASN A 1 481 ? 26.649  92.499  13.254  1.00 73.20  ? 576  ASN A OD1 1 
ATOM   3615 N ND2 . ASN A 1 481 ? 28.381  91.163  12.718  1.00 75.06  ? 576  ASN A ND2 1 
ATOM   3616 N N   . LEU A 1 482 ? 23.765  87.984  13.976  1.00 61.74  ? 577  LEU A N   1 
ATOM   3617 C CA  . LEU A 1 482 ? 22.704  87.049  13.646  1.00 63.75  ? 577  LEU A CA  1 
ATOM   3618 C C   . LEU A 1 482 ? 21.355  87.656  14.013  1.00 64.59  ? 577  LEU A C   1 
ATOM   3619 O O   . LEU A 1 482 ? 21.261  88.585  14.819  1.00 58.99  ? 577  LEU A O   1 
ATOM   3620 C CB  . LEU A 1 482 ? 22.907  85.710  14.364  1.00 60.39  ? 577  LEU A CB  1 
ATOM   3621 C CG  . LEU A 1 482 ? 24.209  84.957  14.067  1.00 60.71  ? 577  LEU A CG  1 
ATOM   3622 C CD1 . LEU A 1 482 ? 24.295  83.732  14.940  1.00 56.45  ? 577  LEU A CD1 1 
ATOM   3623 C CD2 . LEU A 1 482 ? 24.315  84.568  12.600  1.00 61.51  ? 577  LEU A CD2 1 
ATOM   3624 N N   . ASP A 1 483 ? 20.305  87.123  13.396  1.00 66.30  ? 578  ASP A N   1 
ATOM   3625 C CA  . ASP A 1 483 ? 18.959  87.654  13.568  1.00 65.30  ? 578  ASP A CA  1 
ATOM   3626 C C   . ASP A 1 483 ? 18.298  86.919  14.720  1.00 64.13  ? 578  ASP A C   1 
ATOM   3627 O O   . ASP A 1 483 ? 17.902  85.760  14.574  1.00 66.84  ? 578  ASP A O   1 
ATOM   3628 C CB  . ASP A 1 483 ? 18.143  87.502  12.290  1.00 67.27  ? 578  ASP A CB  1 
ATOM   3629 C CG  . ASP A 1 483 ? 16.841  88.286  12.337  1.00 69.99  ? 578  ASP A CG  1 
ATOM   3630 O OD1 . ASP A 1 483 ? 16.369  88.603  13.450  1.00 67.77  ? 578  ASP A OD1 1 
ATOM   3631 O OD2 . ASP A 1 483 ? 16.294  88.589  11.259  1.00 70.92  ? 578  ASP A OD2 1 
ATOM   3632 N N   . ALA A 1 484 ? 18.162  87.598  15.857  1.00 61.20  ? 579  ALA A N   1 
ATOM   3633 C CA  . ALA A 1 484 ? 17.553  86.970  17.018  1.00 64.43  ? 579  ALA A CA  1 
ATOM   3634 C C   . ALA A 1 484 ? 16.093  86.616  16.767  1.00 73.52  ? 579  ALA A C   1 
ATOM   3635 O O   . ALA A 1 484 ? 15.586  85.648  17.346  1.00 71.22  ? 579  ALA A O   1 
ATOM   3636 C CB  . ALA A 1 484 ? 17.669  87.886  18.230  1.00 60.31  ? 579  ALA A CB  1 
ATOM   3637 N N   . ASN A 1 485 ? 15.408  87.368  15.898  1.00 74.37  ? 580  ASN A N   1 
ATOM   3638 C CA  . ASN A 1 485 ? 14.006  87.075  15.606  1.00 76.35  ? 580  ASN A CA  1 
ATOM   3639 C C   . ASN A 1 485 ? 13.845  85.729  14.917  1.00 76.59  ? 580  ASN A C   1 
ATOM   3640 O O   . ASN A 1 485 ? 12.813  85.069  15.076  1.00 81.98  ? 580  ASN A O   1 
ATOM   3641 C CB  . ASN A 1 485 ? 13.402  88.181  14.741  1.00 76.78  ? 580  ASN A CB  1 
ATOM   3642 C CG  . ASN A 1 485 ? 13.511  89.542  15.388  1.00 79.14  ? 580  ASN A CG  1 
ATOM   3643 O OD1 . ASN A 1 485 ? 13.046  89.748  16.508  1.00 83.60  ? 580  ASN A OD1 1 
ATOM   3644 N ND2 . ASN A 1 485 ? 14.141  90.480  14.691  1.00 83.11  ? 580  ASN A ND2 1 
ATOM   3645 N N   . LYS A 1 486 ? 14.835  85.313  14.139  1.00 69.27  ? 581  LYS A N   1 
ATOM   3646 C CA  . LYS A 1 486 ? 14.820  83.993  13.534  1.00 69.42  ? 581  LYS A CA  1 
ATOM   3647 C C   . LYS A 1 486 ? 15.234  82.892  14.508  1.00 66.47  ? 581  LYS A C   1 
ATOM   3648 O O   . LYS A 1 486 ? 15.209  81.716  14.135  1.00 66.27  ? 581  LYS A O   1 
ATOM   3649 C CB  . LYS A 1 486 ? 15.722  83.990  12.294  1.00 71.33  ? 581  LYS A CB  1 
ATOM   3650 C CG  . LYS A 1 486 ? 15.164  84.852  11.144  1.00 77.20  ? 581  LYS A CG  1 
ATOM   3651 C CD  . LYS A 1 486 ? 16.136  84.950  9.958   1.00 80.21  ? 581  LYS A CD  1 
ATOM   3652 C CE  . LYS A 1 486 ? 15.420  85.313  8.641   1.00 80.16  ? 581  LYS A CE  1 
ATOM   3653 N NZ  . LYS A 1 486 ? 14.409  86.411  8.783   1.00 84.36  ? 581  LYS A NZ  1 
ATOM   3654 N N   . LEU A 1 487 ? 15.593  83.237  15.748  1.00 65.51  ? 582  LEU A N   1 
ATOM   3655 C CA  . LEU A 1 487 ? 16.019  82.257  16.742  1.00 63.54  ? 582  LEU A CA  1 
ATOM   3656 C C   . LEU A 1 487 ? 15.197  82.344  18.022  1.00 61.17  ? 582  LEU A C   1 
ATOM   3657 O O   . LEU A 1 487 ? 15.549  81.691  19.015  1.00 56.25  ? 582  LEU A O   1 
ATOM   3658 C CB  . LEU A 1 487 ? 17.512  82.431  17.071  1.00 59.18  ? 582  LEU A CB  1 
ATOM   3659 C CG  . LEU A 1 487 ? 18.538  82.107  15.976  1.00 59.43  ? 582  LEU A CG  1 
ATOM   3660 C CD1 . LEU A 1 487 ? 19.825  82.897  16.193  1.00 55.36  ? 582  LEU A CD1 1 
ATOM   3661 C CD2 . LEU A 1 487 ? 18.855  80.616  15.932  1.00 52.13  ? 582  LEU A CD2 1 
ATOM   3662 N N   . ASN A 1 488 ? 14.105  83.116  18.012  1.00 60.16  ? 583  ASN A N   1 
ATOM   3663 C CA  . ASN A 1 488 ? 13.343  83.398  19.227  1.00 60.04  ? 583  ASN A CA  1 
ATOM   3664 C C   . ASN A 1 488 ? 13.021  82.125  20.012  1.00 54.38  ? 583  ASN A C   1 
ATOM   3665 O O   . ASN A 1 488 ? 13.316  82.036  21.210  1.00 55.02  ? 583  ASN A O   1 
ATOM   3666 C CB  . ASN A 1 488 ? 12.063  84.175  18.872  1.00 66.86  ? 583  ASN A CB  1 
ATOM   3667 C CG  . ASN A 1 488 ? 11.109  83.379  17.965  1.00 71.02  ? 583  ASN A CG  1 
ATOM   3668 O OD1 . ASN A 1 488 ? 11.540  82.682  17.031  1.00 69.28  ? 583  ASN A OD1 1 
ATOM   3669 N ND2 . ASN A 1 488 ? 9.809   83.465  18.257  1.00 70.74  ? 583  ASN A ND2 1 
ATOM   3670 N N   . PHE A 1 489 ? 12.470  81.108  19.339  1.00 54.80  ? 584  PHE A N   1 
ATOM   3671 C CA  . PHE A 1 489 ? 12.081  79.882  20.036  1.00 55.34  ? 584  PHE A CA  1 
ATOM   3672 C C   . PHE A 1 489 ? 13.270  79.279  20.774  1.00 56.12  ? 584  PHE A C   1 
ATOM   3673 O O   . PHE A 1 489 ? 13.190  78.962  21.970  1.00 55.49  ? 584  PHE A O   1 
ATOM   3674 C CB  . PHE A 1 489 ? 11.490  78.880  19.041  1.00 54.43  ? 584  PHE A CB  1 
ATOM   3675 C CG  . PHE A 1 489 ? 12.508  78.308  18.075  1.00 60.65  ? 584  PHE A CG  1 
ATOM   3676 C CD1 . PHE A 1 489 ? 13.099  79.118  17.105  1.00 59.29  ? 584  PHE A CD1 1 
ATOM   3677 C CD2 . PHE A 1 489 ? 12.888  76.969  18.146  1.00 58.22  ? 584  PHE A CD2 1 
ATOM   3678 C CE1 . PHE A 1 489 ? 14.031  78.607  16.237  1.00 58.02  ? 584  PHE A CE1 1 
ATOM   3679 C CE2 . PHE A 1 489 ? 13.825  76.442  17.261  1.00 57.63  ? 584  PHE A CE2 1 
ATOM   3680 C CZ  . PHE A 1 489 ? 14.394  77.259  16.309  1.00 58.26  ? 584  PHE A CZ  1 
ATOM   3681 N N   . TYR A 1 490 ? 14.410  79.197  20.093  1.00 54.36  ? 585  TYR A N   1 
ATOM   3682 C CA  . TYR A 1 490 ? 15.610  78.674  20.719  1.00 52.92  ? 585  TYR A CA  1 
ATOM   3683 C C   . TYR A 1 490 ? 16.029  79.555  21.879  1.00 49.58  ? 585  TYR A C   1 
ATOM   3684 O O   . TYR A 1 490 ? 16.245  79.067  22.995  1.00 52.12  ? 585  TYR A O   1 
ATOM   3685 C CB  . TYR A 1 490 ? 16.712  78.572  19.669  1.00 54.30  ? 585  TYR A CB  1 
ATOM   3686 C CG  . TYR A 1 490 ? 18.107  78.317  20.181  1.00 49.57  ? 585  TYR A CG  1 
ATOM   3687 C CD1 . TYR A 1 490 ? 18.499  77.045  20.578  1.00 46.78  ? 585  TYR A CD1 1 
ATOM   3688 C CD2 . TYR A 1 490 ? 19.047  79.344  20.232  1.00 50.57  ? 585  TYR A CD2 1 
ATOM   3689 C CE1 . TYR A 1 490 ? 19.789  76.795  21.011  1.00 45.74  ? 585  TYR A CE1 1 
ATOM   3690 C CE2 . TYR A 1 490 ? 20.346  79.105  20.673  1.00 48.83  ? 585  TYR A CE2 1 
ATOM   3691 C CZ  . TYR A 1 490 ? 20.708  77.827  21.051  1.00 47.80  ? 585  TYR A CZ  1 
ATOM   3692 O OH  . TYR A 1 490 ? 21.989  77.579  21.477  1.00 47.89  ? 585  TYR A OH  1 
ATOM   3693 N N   . ILE A 1 491 ? 16.103  80.869  21.647  1.00 49.78  ? 586  ILE A N   1 
ATOM   3694 C CA  . ILE A 1 491 ? 16.499  81.769  22.727  1.00 52.53  ? 586  ILE A CA  1 
ATOM   3695 C C   . ILE A 1 491 ? 15.516  81.641  23.878  1.00 56.43  ? 586  ILE A C   1 
ATOM   3696 O O   . ILE A 1 491 ? 15.900  81.650  25.056  1.00 55.65  ? 586  ILE A O   1 
ATOM   3697 C CB  . ILE A 1 491 ? 16.579  83.220  22.219  1.00 55.39  ? 586  ILE A CB  1 
ATOM   3698 C CG1 . ILE A 1 491 ? 17.645  83.360  21.129  1.00 54.02  ? 586  ILE A CG1 1 
ATOM   3699 C CG2 . ILE A 1 491 ? 16.792  84.208  23.387  1.00 52.70  ? 586  ILE A CG2 1 
ATOM   3700 C CD1 . ILE A 1 491 ? 17.434  84.609  20.273  1.00 57.61  ? 586  ILE A CD1 1 
ATOM   3701 N N   . ASP A 1 492 ? 14.231  81.458  23.559  1.00 61.34  ? 587  ASP A N   1 
ATOM   3702 C CA  . ASP A 1 492 ? 13.275  81.512  24.650  1.00 59.47  ? 587  ASP A CA  1 
ATOM   3703 C C   . ASP A 1 492 ? 13.379  80.265  25.509  1.00 59.78  ? 587  ASP A C   1 
ATOM   3704 O O   . ASP A 1 492 ? 12.989  80.301  26.685  1.00 60.34  ? 587  ASP A O   1 
ATOM   3705 C CB  . ASP A 1 492 ? 11.856  81.722  24.111  1.00 62.25  ? 587  ASP A CB  1 
ATOM   3706 C CG  . ASP A 1 492 ? 10.834  81.884  25.213  1.00 70.75  ? 587  ASP A CG  1 
ATOM   3707 O OD1 . ASP A 1 492 ? 9.959   80.996  25.343  1.00 77.34  ? 587  ASP A OD1 1 
ATOM   3708 O OD2 . ASP A 1 492 ? 10.914  82.879  25.963  1.00 78.49  ? 587  ASP A OD2 1 
ATOM   3709 N N   . SER A 1 493 ? 13.982  79.193  24.974  1.00 54.12  ? 588  SER A N   1 
ATOM   3710 C CA  . SER A 1 493 ? 14.158  78.010  25.806  1.00 53.05  ? 588  SER A CA  1 
ATOM   3711 C C   . SER A 1 493 ? 15.190  78.216  26.913  1.00 54.76  ? 588  SER A C   1 
ATOM   3712 O O   . SER A 1 493 ? 15.268  77.380  27.820  1.00 52.24  ? 588  SER A O   1 
ATOM   3713 C CB  . SER A 1 493 ? 14.546  76.809  24.948  1.00 53.43  ? 588  SER A CB  1 
ATOM   3714 O OG  . SER A 1 493 ? 15.900  76.910  24.543  1.00 50.95  ? 588  SER A OG  1 
ATOM   3715 N N   . PHE A 1 494 ? 15.972  79.302  26.878  1.00 52.80  ? 589  PHE A N   1 
ATOM   3716 C CA  . PHE A 1 494 ? 16.923  79.577  27.953  1.00 52.08  ? 589  PHE A CA  1 
ATOM   3717 C C   . PHE A 1 494 ? 16.385  80.549  29.002  1.00 55.32  ? 589  PHE A C   1 
ATOM   3718 O O   . PHE A 1 494 ? 17.083  80.822  29.983  1.00 56.55  ? 589  PHE A O   1 
ATOM   3719 C CB  . PHE A 1 494 ? 18.236  80.153  27.391  1.00 50.95  ? 589  PHE A CB  1 
ATOM   3720 C CG  . PHE A 1 494 ? 18.947  79.244  26.435  1.00 48.79  ? 589  PHE A CG  1 
ATOM   3721 C CD1 . PHE A 1 494 ? 20.039  78.498  26.850  1.00 49.51  ? 589  PHE A CD1 1 
ATOM   3722 C CD2 . PHE A 1 494 ? 18.540  79.157  25.115  1.00 48.81  ? 589  PHE A CD2 1 
ATOM   3723 C CE1 . PHE A 1 494 ? 20.701  77.653  25.961  1.00 51.32  ? 589  PHE A CE1 1 
ATOM   3724 C CE2 . PHE A 1 494 ? 19.192  78.322  24.225  1.00 50.65  ? 589  PHE A CE2 1 
ATOM   3725 C CZ  . PHE A 1 494 ? 20.278  77.571  24.643  1.00 48.06  ? 589  PHE A CZ  1 
ATOM   3726 N N   . ALA A 1 495 ? 15.179  81.083  28.820  1.00 55.38  ? 590  ALA A N   1 
ATOM   3727 C CA  . ALA A 1 495 ? 14.683  82.160  29.669  1.00 58.26  ? 590  ALA A CA  1 
ATOM   3728 C C   . ALA A 1 495 ? 14.009  81.665  30.949  1.00 59.68  ? 590  ALA A C   1 
ATOM   3729 O O   . ALA A 1 495 ? 13.568  82.496  31.756  1.00 59.76  ? 590  ALA A O   1 
ATOM   3730 C CB  . ALA A 1 495 ? 13.710  83.036  28.878  1.00 57.78  ? 590  ALA A CB  1 
ATOM   3731 N N   . TYR A 1 496 ? 13.906  80.349  31.160  1.00 55.12  ? 591  TYR A N   1 
ATOM   3732 C CA  . TYR A 1 496 ? 13.315  79.849  32.399  1.00 56.92  ? 591  TYR A CA  1 
ATOM   3733 C C   . TYR A 1 496 ? 14.306  78.910  33.065  1.00 57.05  ? 591  TYR A C   1 
ATOM   3734 O O   . TYR A 1 496 ? 13.950  77.795  33.469  1.00 54.28  ? 591  TYR A O   1 
ATOM   3735 C CB  . TYR A 1 496 ? 11.972  79.157  32.138  1.00 56.77  ? 591  TYR A CB  1 
ATOM   3736 C CG  . TYR A 1 496 ? 11.152  79.845  31.070  1.00 58.87  ? 591  TYR A CG  1 
ATOM   3737 C CD1 . TYR A 1 496 ? 10.363  80.950  31.371  1.00 62.25  ? 591  TYR A CD1 1 
ATOM   3738 C CD2 . TYR A 1 496 ? 11.190  79.409  29.746  1.00 58.58  ? 591  TYR A CD2 1 
ATOM   3739 C CE1 . TYR A 1 496 ? 9.623   81.588  30.390  1.00 62.78  ? 591  TYR A CE1 1 
ATOM   3740 C CE2 . TYR A 1 496 ? 10.453  80.045  28.762  1.00 59.75  ? 591  TYR A CE2 1 
ATOM   3741 C CZ  . TYR A 1 496 ? 9.672   81.130  29.093  1.00 62.40  ? 591  TYR A CZ  1 
ATOM   3742 O OH  . TYR A 1 496 ? 8.939   81.755  28.113  1.00 66.67  ? 591  TYR A OH  1 
ATOM   3743 N N   . SER A 1 497 ? 15.554  79.385  33.161  1.00 54.50  ? 592  SER A N   1 
ATOM   3744 C CA  . SER A 1 497 ? 16.722  78.711  33.714  1.00 54.17  ? 592  SER A CA  1 
ATOM   3745 C C   . SER A 1 497 ? 17.312  77.760  32.687  1.00 55.14  ? 592  SER A C   1 
ATOM   3746 O O   . SER A 1 497 ? 16.621  77.295  31.775  1.00 53.29  ? 592  SER A O   1 
ATOM   3747 C CB  . SER A 1 497 ? 16.405  77.967  35.017  1.00 56.28  ? 592  SER A CB  1 
ATOM   3748 O OG  . SER A 1 497 ? 15.741  76.739  34.765  1.00 56.75  ? 592  SER A OG  1 
ATOM   3749 N N   . SER A 1 498 ? 18.604  77.493  32.815  1.00 55.83  ? 593  SER A N   1 
ATOM   3750 C CA  . SER A 1 498 ? 19.294  76.600  31.901  1.00 53.14  ? 593  SER A CA  1 
ATOM   3751 C C   . SER A 1 498 ? 20.399  75.898  32.671  1.00 54.25  ? 593  SER A C   1 
ATOM   3752 O O   . SER A 1 498 ? 21.174  76.550  33.382  1.00 53.14  ? 593  SER A O   1 
ATOM   3753 C CB  . SER A 1 498 ? 19.871  77.366  30.705  1.00 54.93  ? 593  SER A CB  1 
ATOM   3754 O OG  . SER A 1 498 ? 20.635  76.508  29.873  1.00 52.24  ? 593  SER A OG  1 
ATOM   3755 N N   . TYR A 1 499 ? 20.447  74.577  32.542  1.00 51.31  ? 594  TYR A N   1 
ATOM   3756 C CA  . TYR A 1 499 ? 21.512  73.795  33.142  1.00 50.23  ? 594  TYR A CA  1 
ATOM   3757 C C   . TYR A 1 499 ? 22.818  74.029  32.386  1.00 52.79  ? 594  TYR A C   1 
ATOM   3758 O O   . TYR A 1 499 ? 22.810  74.249  31.173  1.00 51.40  ? 594  TYR A O   1 
ATOM   3759 C CB  . TYR A 1 499 ? 21.171  72.309  33.096  1.00 52.12  ? 594  TYR A CB  1 
ATOM   3760 C CG  . TYR A 1 499 ? 19.945  71.886  33.885  1.00 53.47  ? 594  TYR A CG  1 
ATOM   3761 C CD1 . TYR A 1 499 ? 20.029  71.634  35.248  1.00 53.81  ? 594  TYR A CD1 1 
ATOM   3762 C CD2 . TYR A 1 499 ? 18.714  71.703  33.258  1.00 55.37  ? 594  TYR A CD2 1 
ATOM   3763 C CE1 . TYR A 1 499 ? 18.918  71.238  35.976  1.00 54.35  ? 594  TYR A CE1 1 
ATOM   3764 C CE2 . TYR A 1 499 ? 17.586  71.298  33.989  1.00 56.59  ? 594  TYR A CE2 1 
ATOM   3765 C CZ  . TYR A 1 499 ? 17.700  71.067  35.342  1.00 54.76  ? 594  TYR A CZ  1 
ATOM   3766 O OH  . TYR A 1 499 ? 16.596  70.668  36.083  1.00 62.91  ? 594  TYR A OH  1 
ATOM   3767 N N   . PRO A 1 500 ? 23.954  74.010  33.080  1.00 52.67  ? 595  PRO A N   1 
ATOM   3768 C CA  . PRO A 1 500 ? 25.231  74.007  32.367  1.00 51.65  ? 595  PRO A CA  1 
ATOM   3769 C C   . PRO A 1 500 ? 25.326  72.761  31.508  1.00 52.12  ? 595  PRO A C   1 
ATOM   3770 O O   . PRO A 1 500 ? 25.062  71.648  31.969  1.00 52.29  ? 595  PRO A O   1 
ATOM   3771 C CB  . PRO A 1 500 ? 26.277  74.016  33.489  1.00 54.39  ? 595  PRO A CB  1 
ATOM   3772 C CG  . PRO A 1 500 ? 25.544  73.686  34.737  1.00 55.52  ? 595  PRO A CG  1 
ATOM   3773 C CD  . PRO A 1 500 ? 24.131  74.113  34.537  1.00 53.79  ? 595  PRO A CD  1 
ATOM   3774 N N   . HIS A 1 501 ? 25.666  72.948  30.239  1.00 50.66  ? 596  HIS A N   1 
ATOM   3775 C CA  . HIS A 1 501 ? 25.639  71.805  29.347  1.00 49.95  ? 596  HIS A CA  1 
ATOM   3776 C C   . HIS A 1 501 ? 26.646  71.987  28.220  1.00 49.31  ? 596  HIS A C   1 
ATOM   3777 O O   . HIS A 1 501 ? 27.218  73.061  28.012  1.00 49.32  ? 596  HIS A O   1 
ATOM   3778 C CB  . HIS A 1 501 ? 24.212  71.543  28.826  1.00 48.24  ? 596  HIS A CB  1 
ATOM   3779 C CG  . HIS A 1 501 ? 23.637  72.647  27.989  1.00 50.66  ? 596  HIS A CG  1 
ATOM   3780 N ND1 . HIS A 1 501 ? 23.108  73.801  28.533  1.00 50.12  ? 596  HIS A ND1 1 
ATOM   3781 C CD2 . HIS A 1 501 ? 23.462  72.750  26.648  1.00 47.53  ? 596  HIS A CD2 1 
ATOM   3782 C CE1 . HIS A 1 501 ? 22.659  74.578  27.563  1.00 48.81  ? 596  HIS A CE1 1 
ATOM   3783 N NE2 . HIS A 1 501 ? 22.861  73.965  26.409  1.00 47.54  ? 596  HIS A NE2 1 
ATOM   3784 N N   . SER A 1 502 ? 26.884  70.884  27.530  1.00 48.52  ? 597  SER A N   1 
ATOM   3785 C CA  . SER A 1 502 ? 27.822  70.822  26.425  1.00 47.13  ? 597  SER A CA  1 
ATOM   3786 C C   . SER A 1 502 ? 27.284  69.804  25.434  1.00 46.86  ? 597  SER A C   1 
ATOM   3787 O O   . SER A 1 502 ? 26.324  69.075  25.719  1.00 44.48  ? 597  SER A O   1 
ATOM   3788 C CB  . SER A 1 502 ? 29.216  70.408  26.891  1.00 46.54  ? 597  SER A CB  1 
ATOM   3789 O OG  . SER A 1 502 ? 29.245  69.005  27.117  1.00 48.50  ? 597  SER A OG  1 
ATOM   3790 N N   . GLY A 1 503 ? 27.911  69.757  24.265  1.00 46.55  ? 598  GLY A N   1 
ATOM   3791 C CA  . GLY A 1 503 ? 27.556  68.694  23.341  1.00 46.81  ? 598  GLY A CA  1 
ATOM   3792 C C   . GLY A 1 503 ? 28.538  68.560  22.195  1.00 47.13  ? 598  GLY A C   1 
ATOM   3793 O O   . GLY A 1 503 ? 29.576  69.233  22.150  1.00 46.49  ? 598  GLY A O   1 
ATOM   3794 N N   . CYS A 1 504 ? 28.174  67.678  21.256  1.00 45.94  ? 599  CYS A N   1 
ATOM   3795 C CA  . CYS A 1 504 ? 29.019  67.381  20.102  1.00 46.89  ? 599  CYS A CA  1 
ATOM   3796 C C   . CYS A 1 504 ? 28.202  66.746  18.978  1.00 46.57  ? 599  CYS A C   1 
ATOM   3797 O O   . CYS A 1 504 ? 27.155  66.129  19.211  1.00 46.27  ? 599  CYS A O   1 
ATOM   3798 C CB  . CYS A 1 504 ? 30.180  66.454  20.490  1.00 44.64  ? 599  CYS A CB  1 
ATOM   3799 S SG  . CYS A 1 504 ? 29.695  64.808  21.172  1.00 50.34  ? 599  CYS A SG  1 
ATOM   3800 N N   . GLY A 1 505 ? 28.712  66.913  17.764  1.00 44.39  ? 600  GLY A N   1 
ATOM   3801 C CA  . GLY A 1 505 ? 28.171  66.250  16.585  1.00 44.32  ? 600  GLY A CA  1 
ATOM   3802 C C   . GLY A 1 505 ? 29.265  65.490  15.862  1.00 47.23  ? 600  GLY A C   1 
ATOM   3803 O O   . GLY A 1 505 ? 30.420  65.945  15.804  1.00 43.27  ? 600  GLY A O   1 
ATOM   3804 N N   . ILE A 1 506 ? 28.900  64.316  15.335  1.00 43.60  ? 601  ILE A N   1 
ATOM   3805 C CA  . ILE A 1 506 ? 29.837  63.345  14.780  1.00 44.52  ? 601  ILE A CA  1 
ATOM   3806 C C   . ILE A 1 506 ? 29.337  62.885  13.419  1.00 47.55  ? 601  ILE A C   1 
ATOM   3807 O O   . ILE A 1 506 ? 28.178  62.461  13.292  1.00 41.97  ? 601  ILE A O   1 
ATOM   3808 C CB  . ILE A 1 506 ? 29.982  62.111  15.690  1.00 43.46  ? 601  ILE A CB  1 
ATOM   3809 C CG1 . ILE A 1 506 ? 30.507  62.494  17.073  1.00 44.12  ? 601  ILE A CG1 1 
ATOM   3810 C CG2 . ILE A 1 506 ? 30.855  61.053  15.014  1.00 45.05  ? 601  ILE A CG2 1 
ATOM   3811 C CD1 . ILE A 1 506 ? 30.156  61.447  18.133  1.00 44.96  ? 601  ILE A CD1 1 
ATOM   3812 N N   . GLY A 1 507 ? 30.227  62.881  12.423  1.00 47.24  ? 602  GLY A N   1 
ATOM   3813 C CA  . GLY A 1 507 ? 29.797  62.255  11.168  1.00 42.59  ? 602  GLY A CA  1 
ATOM   3814 C C   . GLY A 1 507 ? 29.925  60.728  11.132  1.00 43.71  ? 602  GLY A C   1 
ATOM   3815 O O   . GLY A 1 507 ? 31.047  60.219  11.243  1.00 39.13  ? 602  GLY A O   1 
ATOM   3816 N N   . LEU A 1 508 ? 28.823  59.977  10.952  1.00 40.71  ? 603  LEU A N   1 
ATOM   3817 C CA  . LEU A 1 508 ? 28.891  58.506  11.027  1.00 42.58  ? 603  LEU A CA  1 
ATOM   3818 C C   . LEU A 1 508 ? 29.761  57.912  9.921   1.00 41.70  ? 603  LEU A C   1 
ATOM   3819 O O   . LEU A 1 508 ? 30.705  57.143  10.182  1.00 41.54  ? 603  LEU A O   1 
ATOM   3820 C CB  . LEU A 1 508 ? 27.486  57.892  10.943  1.00 40.94  ? 603  LEU A CB  1 
ATOM   3821 C CG  . LEU A 1 508 ? 27.399  56.367  10.657  1.00 41.62  ? 603  LEU A CG  1 
ATOM   3822 C CD1 . LEU A 1 508 ? 28.043  55.495  11.760  1.00 36.65  ? 603  LEU A CD1 1 
ATOM   3823 C CD2 . LEU A 1 508 ? 25.952  55.926  10.452  1.00 39.16  ? 603  LEU A CD2 1 
ATOM   3824 N N   . GLU A 1 509 ? 29.400  58.206  8.668   1.00 42.15  ? 604  GLU A N   1 
ATOM   3825 C CA  . GLU A 1 509 ? 30.133  57.680  7.523   1.00 42.64  ? 604  GLU A CA  1 
ATOM   3826 C C   . GLU A 1 509 ? 31.594  58.095  7.570   1.00 44.36  ? 604  GLU A C   1 
ATOM   3827 O O   . GLU A 1 509 ? 32.477  57.315  7.184   1.00 44.41  ? 604  GLU A O   1 
ATOM   3828 C CB  . GLU A 1 509 ? 29.476  58.153  6.221   1.00 41.54  ? 604  GLU A CB  1 
ATOM   3829 C CG  . GLU A 1 509 ? 27.973  57.809  6.150   1.00 42.81  ? 604  GLU A CG  1 
ATOM   3830 C CD  . GLU A 1 509 ? 27.063  58.918  6.704   1.00 43.22  ? 604  GLU A CD  1 
ATOM   3831 O OE1 . GLU A 1 509 ? 27.519  59.724  7.558   1.00 40.79  ? 604  GLU A OE1 1 
ATOM   3832 O OE2 . GLU A 1 509 ? 25.888  58.982  6.261   1.00 42.43  ? 604  GLU A OE2 1 
ATOM   3833 N N   . ARG A 1 510 ? 31.868  59.302  8.068   1.00 43.36  ? 605  ARG A N   1 
ATOM   3834 C CA  . ARG A 1 510 ? 33.247  59.762  8.155   1.00 46.37  ? 605  ARG A CA  1 
ATOM   3835 C C   . ARG A 1 510 ? 34.028  58.986  9.208   1.00 43.52  ? 605  ARG A C   1 
ATOM   3836 O O   . ARG A 1 510 ? 35.196  58.635  8.986   1.00 45.51  ? 605  ARG A O   1 
ATOM   3837 C CB  . ARG A 1 510 ? 33.296  61.269  8.445   1.00 46.35  ? 605  ARG A CB  1 
ATOM   3838 C CG  . ARG A 1 510 ? 34.658  61.862  8.074   1.00 56.50  ? 605  ARG A CG  1 
ATOM   3839 C CD  . ARG A 1 510 ? 34.897  63.255  8.635   1.00 58.29  ? 605  ARG A CD  1 
ATOM   3840 N NE  . ARG A 1 510 ? 34.233  64.283  7.843   1.00 66.34  ? 605  ARG A NE  1 
ATOM   3841 C CZ  . ARG A 1 510 ? 34.526  65.578  7.886   1.00 68.86  ? 605  ARG A CZ  1 
ATOM   3842 N NH1 . ARG A 1 510 ? 33.817  66.464  7.203   1.00 69.73  ? 605  ARG A NH1 1 
ATOM   3843 N NH2 . ARG A 1 510 ? 35.564  65.991  8.622   1.00 64.19  ? 605  ARG A NH2 1 
ATOM   3844 N N   . VAL A 1 511 ? 33.423  58.723  10.369  1.00 41.69  ? 606  VAL A N   1 
ATOM   3845 C CA  . VAL A 1 511 ? 34.112  57.897  11.360  1.00 42.98  ? 606  VAL A CA  1 
ATOM   3846 C C   . VAL A 1 511 ? 34.479  56.541  10.761  1.00 44.13  ? 606  VAL A C   1 
ATOM   3847 O O   . VAL A 1 511 ? 35.601  56.048  10.955  1.00 43.47  ? 606  VAL A O   1 
ATOM   3848 C CB  . VAL A 1 511 ? 33.266  57.737  12.637  1.00 46.26  ? 606  VAL A CB  1 
ATOM   3849 C CG1 . VAL A 1 511 ? 33.874  56.662  13.531  1.00 45.03  ? 606  VAL A CG1 1 
ATOM   3850 C CG2 . VAL A 1 511 ? 33.220  59.036  13.384  1.00 45.87  ? 606  VAL A CG2 1 
ATOM   3851 N N   . LEU A 1 512 ? 33.547  55.917  10.025  1.00 40.96  ? 607  LEU A N   1 
ATOM   3852 C CA  . LEU A 1 512 ? 33.848  54.615  9.428   1.00 43.71  ? 607  LEU A CA  1 
ATOM   3853 C C   . LEU A 1 512 ? 34.958  54.720  8.376   1.00 42.96  ? 607  LEU A C   1 
ATOM   3854 O O   . LEU A 1 512 ? 35.897  53.906  8.353   1.00 40.01  ? 607  LEU A O   1 
ATOM   3855 C CB  . LEU A 1 512 ? 32.573  54.021  8.822   1.00 41.38  ? 607  LEU A CB  1 
ATOM   3856 C CG  . LEU A 1 512 ? 32.727  52.617  8.221   1.00 42.70  ? 607  LEU A CG  1 
ATOM   3857 C CD1 . LEU A 1 512 ? 33.343  51.663  9.242   1.00 37.83  ? 607  LEU A CD1 1 
ATOM   3858 C CD2 . LEU A 1 512 ? 31.381  52.086  7.726   1.00 38.93  ? 607  LEU A CD2 1 
ATOM   3859 N N   . MET A 1 513 ? 34.857  55.717  7.490   1.00 43.81  ? 608  MET A N   1 
ATOM   3860 C CA  . MET A 1 513 ? 35.874  55.950  6.469   1.00 42.13  ? 608  MET A CA  1 
ATOM   3861 C C   . MET A 1 513 ? 37.260  56.067  7.085   1.00 44.92  ? 608  MET A C   1 
ATOM   3862 O O   . MET A 1 513 ? 38.210  55.398  6.653   1.00 44.94  ? 608  MET A O   1 
ATOM   3863 C CB  . MET A 1 513 ? 35.536  57.225  5.695   1.00 42.49  ? 608  MET A CB  1 
ATOM   3864 C CG  . MET A 1 513 ? 36.615  57.661  4.745   1.00 46.58  ? 608  MET A CG  1 
ATOM   3865 S SD  . MET A 1 513 ? 36.264  59.250  3.948   1.00 51.77  ? 608  MET A SD  1 
ATOM   3866 C CE  . MET A 1 513 ? 36.683  60.412  5.250   1.00 57.88  ? 608  MET A CE  1 
ATOM   3867 N N   . LEU A 1 514 ? 37.388  56.904  8.115   1.00 42.54  ? 609  LEU A N   1 
ATOM   3868 C CA  . LEU A 1 514 ? 38.701  57.172  8.691   1.00 45.76  ? 609  LEU A CA  1 
ATOM   3869 C C   . LEU A 1 514 ? 39.210  55.989  9.501   1.00 47.54  ? 609  LEU A C   1 
ATOM   3870 O O   . LEU A 1 514 ? 40.414  55.699  9.483   1.00 47.83  ? 609  LEU A O   1 
ATOM   3871 C CB  . LEU A 1 514 ? 38.649  58.434  9.550   1.00 46.18  ? 609  LEU A CB  1 
ATOM   3872 C CG  . LEU A 1 514 ? 38.488  59.683  8.689   1.00 48.54  ? 609  LEU A CG  1 
ATOM   3873 C CD1 . LEU A 1 514 ? 38.013  60.852  9.543   1.00 45.81  ? 609  LEU A CD1 1 
ATOM   3874 C CD2 . LEU A 1 514 ? 39.814  59.999  7.989   1.00 44.43  ? 609  LEU A CD2 1 
ATOM   3875 N N   . PHE A 1 515 ? 38.320  55.292  10.220  1.00 42.98  ? 610  PHE A N   1 
ATOM   3876 C CA  . PHE A 1 515 ? 38.749  54.096  10.937  1.00 44.92  ? 610  PHE A CA  1 
ATOM   3877 C C   . PHE A 1 515 ? 39.366  53.090  9.979   1.00 46.38  ? 610  PHE A C   1 
ATOM   3878 O O   . PHE A 1 515 ? 40.427  52.525  10.264  1.00 45.72  ? 610  PHE A O   1 
ATOM   3879 C CB  . PHE A 1 515 ? 37.581  53.456  11.697  1.00 44.62  ? 610  PHE A CB  1 
ATOM   3880 C CG  . PHE A 1 515 ? 37.983  52.264  12.527  1.00 45.28  ? 610  PHE A CG  1 
ATOM   3881 C CD1 . PHE A 1 515 ? 38.552  52.431  13.777  1.00 46.69  ? 610  PHE A CD1 1 
ATOM   3882 C CD2 . PHE A 1 515 ? 37.812  50.981  12.052  1.00 48.51  ? 610  PHE A CD2 1 
ATOM   3883 C CE1 . PHE A 1 515 ? 38.929  51.330  14.536  1.00 49.83  ? 610  PHE A CE1 1 
ATOM   3884 C CE2 . PHE A 1 515 ? 38.199  49.879  12.814  1.00 47.23  ? 610  PHE A CE2 1 
ATOM   3885 C CZ  . PHE A 1 515 ? 38.751  50.059  14.043  1.00 47.19  ? 610  PHE A CZ  1 
ATOM   3886 N N   . LEU A 1 516 ? 38.722  52.866  8.823   1.00 46.38  ? 611  LEU A N   1 
ATOM   3887 C CA  . LEU A 1 516 ? 39.263  51.900  7.867   1.00 46.32  ? 611  LEU A CA  1 
ATOM   3888 C C   . LEU A 1 516 ? 40.299  52.502  6.915   1.00 48.12  ? 611  LEU A C   1 
ATOM   3889 O O   . LEU A 1 516 ? 40.895  51.765  6.120   1.00 45.51  ? 611  LEU A O   1 
ATOM   3890 C CB  . LEU A 1 516 ? 38.121  51.260  7.072   1.00 44.44  ? 611  LEU A CB  1 
ATOM   3891 C CG  . LEU A 1 516 ? 37.082  50.476  7.908   1.00 43.15  ? 611  LEU A CG  1 
ATOM   3892 C CD1 . LEU A 1 516 ? 35.843  50.197  7.071   1.00 41.36  ? 611  LEU A CD1 1 
ATOM   3893 C CD2 . LEU A 1 516 ? 37.638  49.165  8.474   1.00 40.02  ? 611  LEU A CD2 1 
ATOM   3894 N N   . GLY A 1 517 ? 40.543  53.807  6.973   1.00 46.56  ? 612  GLY A N   1 
ATOM   3895 C CA  . GLY A 1 517 ? 41.498  54.385  6.049   1.00 48.30  ? 612  GLY A CA  1 
ATOM   3896 C C   . GLY A 1 517 ? 41.030  54.414  4.610   1.00 50.09  ? 612  GLY A C   1 
ATOM   3897 O O   . GLY A 1 517 ? 41.852  54.537  3.699   1.00 47.16  ? 612  GLY A O   1 
ATOM   3898 N N   . LEU A 1 518 ? 39.727  54.299  4.377   1.00 46.14  ? 613  LEU A N   1 
ATOM   3899 C CA  . LEU A 1 518 ? 39.202  54.332  3.021   1.00 45.48  ? 613  LEU A CA  1 
ATOM   3900 C C   . LEU A 1 518 ? 39.417  55.709  2.400   1.00 48.09  ? 613  LEU A C   1 
ATOM   3901 O O   . LEU A 1 518 ? 39.514  56.725  3.099   1.00 46.89  ? 613  LEU A O   1 
ATOM   3902 C CB  . LEU A 1 518 ? 37.719  53.951  3.033   1.00 46.10  ? 613  LEU A CB  1 
ATOM   3903 C CG  . LEU A 1 518 ? 37.502  52.501  3.499   1.00 44.83  ? 613  LEU A CG  1 
ATOM   3904 C CD1 . LEU A 1 518 ? 36.034  52.205  3.712   1.00 40.56  ? 613  LEU A CD1 1 
ATOM   3905 C CD2 . LEU A 1 518 ? 38.092  51.511  2.481   1.00 42.95  ? 613  LEU A CD2 1 
ATOM   3906 N N   . ASN A 1 519 ? 39.485  55.741  1.066   1.00 45.09  ? 614  ASN A N   1 
ATOM   3907 C CA  . ASN A 1 519 ? 39.927  56.938  0.368   1.00 48.21  ? 614  ASN A CA  1 
ATOM   3908 C C   . ASN A 1 519 ? 38.797  57.893  0.007   1.00 48.43  ? 614  ASN A C   1 
ATOM   3909 O O   . ASN A 1 519 ? 39.075  58.981  -0.503  1.00 47.84  ? 614  ASN A O   1 
ATOM   3910 C CB  . ASN A 1 519 ? 40.691  56.553  -0.912  1.00 48.28  ? 614  ASN A CB  1 
ATOM   3911 C CG  . ASN A 1 519 ? 39.765  56.107  -2.043  1.00 52.02  ? 614  ASN A CG  1 
ATOM   3912 O OD1 . ASN A 1 519 ? 38.627  55.677  -1.816  1.00 48.34  ? 614  ASN A OD1 1 
ATOM   3913 N ND2 . ASN A 1 519 ? 40.257  56.200  -3.271  1.00 56.88  ? 614  ASN A ND2 1 
ATOM   3914 N N   . ASN A 1 520 ? 37.536  57.528  0.241   1.00 46.81  ? 615  ASN A N   1 
ATOM   3915 C CA  . ASN A 1 520 ? 36.438  58.351  -0.253  1.00 45.35  ? 615  ASN A CA  1 
ATOM   3916 C C   . ASN A 1 520 ? 35.183  58.075  0.564   1.00 47.50  ? 615  ASN A C   1 
ATOM   3917 O O   . ASN A 1 520 ? 34.824  56.912  0.785   1.00 46.14  ? 615  ASN A O   1 
ATOM   3918 C CB  . ASN A 1 520 ? 36.203  58.060  -1.740  1.00 46.65  ? 615  ASN A CB  1 
ATOM   3919 C CG  . ASN A 1 520 ? 35.317  59.082  -2.410  1.00 45.88  ? 615  ASN A CG  1 
ATOM   3920 O OD1 . ASN A 1 520 ? 34.148  59.218  -2.069  1.00 45.81  ? 615  ASN A OD1 1 
ATOM   3921 N ND2 . ASN A 1 520 ? 35.862  59.789  -3.395  1.00 44.71  ? 615  ASN A ND2 1 
ATOM   3922 N N   . ILE A 1 521 ? 34.506  59.144  0.991   1.00 46.59  ? 616  ILE A N   1 
ATOM   3923 C CA  . ILE A 1 521 ? 33.297  59.018  1.794   1.00 43.58  ? 616  ILE A CA  1 
ATOM   3924 C C   . ILE A 1 521 ? 32.188  58.267  1.058   1.00 44.51  ? 616  ILE A C   1 
ATOM   3925 O O   . ILE A 1 521 ? 31.288  57.711  1.691   1.00 43.36  ? 616  ILE A O   1 
ATOM   3926 C CB  . ILE A 1 521 ? 32.822  60.421  2.231   1.00 45.73  ? 616  ILE A CB  1 
ATOM   3927 C CG1 . ILE A 1 521 ? 31.777  60.316  3.343   1.00 46.84  ? 616  ILE A CG1 1 
ATOM   3928 C CG2 . ILE A 1 521 ? 32.257  61.193  1.053   1.00 42.23  ? 616  ILE A CG2 1 
ATOM   3929 C CD1 . ILE A 1 521 ? 32.376  60.100  4.678   1.00 47.94  ? 616  ILE A CD1 1 
ATOM   3930 N N   . ARG A 1 522 ? 32.215  58.237  -0.271  1.00 42.12  ? 617  ARG A N   1 
ATOM   3931 C CA  . ARG A 1 522 ? 31.187  57.481  -0.976  1.00 44.39  ? 617  ARG A CA  1 
ATOM   3932 C C   . ARG A 1 522 ? 31.304  55.970  -0.763  1.00 45.57  ? 617  ARG A C   1 
ATOM   3933 O O   . ARG A 1 522 ? 30.363  55.241  -1.103  1.00 43.96  ? 617  ARG A O   1 
ATOM   3934 C CB  . ARG A 1 522 ? 31.225  57.849  -2.465  1.00 41.99  ? 617  ARG A CB  1 
ATOM   3935 C CG  . ARG A 1 522 ? 30.897  59.344  -2.699  1.00 42.81  ? 617  ARG A CG  1 
ATOM   3936 C CD  . ARG A 1 522 ? 31.382  59.862  -4.065  1.00 45.84  ? 617  ARG A CD  1 
ATOM   3937 N NE  . ARG A 1 522 ? 31.256  61.311  -4.195  1.00 45.66  ? 617  ARG A NE  1 
ATOM   3938 C CZ  . ARG A 1 522 ? 32.008  62.204  -3.555  1.00 47.34  ? 617  ARG A CZ  1 
ATOM   3939 N NH1 . ARG A 1 522 ? 32.937  61.839  -2.682  1.00 44.82  ? 617  ARG A NH1 1 
ATOM   3940 N NH2 . ARG A 1 522 ? 31.816  63.500  -3.791  1.00 49.12  ? 617  ARG A NH2 1 
ATOM   3941 N N   . LYS A 1 523 ? 32.405  55.485  -0.181  1.00 40.96  ? 618  LYS A N   1 
ATOM   3942 C CA  . LYS A 1 523 ? 32.500  54.069  0.147   1.00 42.65  ? 618  LYS A CA  1 
ATOM   3943 C C   . LYS A 1 523 ? 31.779  53.693  1.435   1.00 43.81  ? 618  LYS A C   1 
ATOM   3944 O O   . LYS A 1 523 ? 31.557  52.501  1.663   1.00 40.12  ? 618  LYS A O   1 
ATOM   3945 C CB  . LYS A 1 523 ? 33.964  53.642  0.241   1.00 41.66  ? 618  LYS A CB  1 
ATOM   3946 C CG  . LYS A 1 523 ? 34.660  53.521  -1.145  1.00 42.31  ? 618  LYS A CG  1 
ATOM   3947 C CD  . LYS A 1 523 ? 36.138  53.187  -0.997  1.00 44.85  ? 618  LYS A CD  1 
ATOM   3948 C CE  . LYS A 1 523 ? 36.792  52.933  -2.368  1.00 45.29  ? 618  LYS A CE  1 
ATOM   3949 N NZ  . LYS A 1 523 ? 36.885  54.179  -3.177  1.00 42.57  ? 618  LYS A NZ  1 
ATOM   3950 N N   . THR A 1 524 ? 31.412  54.661  2.286   1.00 40.07  ? 619  THR A N   1 
ATOM   3951 C CA  . THR A 1 524 ? 30.761  54.371  3.563   1.00 38.32  ? 619  THR A CA  1 
ATOM   3952 C C   . THR A 1 524 ? 29.372  55.004  3.704   1.00 39.56  ? 619  THR A C   1 
ATOM   3953 O O   . THR A 1 524 ? 28.833  55.054  4.819   1.00 37.57  ? 619  THR A O   1 
ATOM   3954 C CB  . THR A 1 524 ? 31.645  54.818  4.731   1.00 41.61  ? 619  THR A CB  1 
ATOM   3955 O OG1 . THR A 1 524 ? 31.864  56.234  4.648   1.00 40.77  ? 619  THR A OG1 1 
ATOM   3956 C CG2 . THR A 1 524 ? 33.000  54.076  4.701   1.00 41.55  ? 619  THR A CG2 1 
ATOM   3957 N N   . SER A 1 525 ? 28.790  55.493  2.616   1.00 38.44  ? 620  SER A N   1 
ATOM   3958 C CA  . SER A 1 525 ? 27.387  55.892  2.542   1.00 41.34  ? 620  SER A CA  1 
ATOM   3959 C C   . SER A 1 525 ? 26.711  55.008  1.495   1.00 40.85  ? 620  SER A C   1 
ATOM   3960 O O   . SER A 1 525 ? 27.241  54.856  0.392   1.00 40.90  ? 620  SER A O   1 
ATOM   3961 C CB  . SER A 1 525 ? 27.282  57.387  2.175   1.00 40.04  ? 620  SER A CB  1 
ATOM   3962 O OG  . SER A 1 525 ? 25.956  57.784  1.884   1.00 43.91  ? 620  SER A OG  1 
ATOM   3963 N N   . LEU A 1 526 ? 25.552  54.418  1.836   1.00 40.51  ? 621  LEU A N   1 
ATOM   3964 C CA  . LEU A 1 526 ? 24.959  53.375  0.989   1.00 40.17  ? 621  LEU A CA  1 
ATOM   3965 C C   . LEU A 1 526 ? 24.627  53.890  -0.399  1.00 41.76  ? 621  LEU A C   1 
ATOM   3966 O O   . LEU A 1 526 ? 24.979  53.269  -1.411  1.00 42.32  ? 621  LEU A O   1 
ATOM   3967 C CB  . LEU A 1 526 ? 23.693  52.808  1.634   1.00 37.29  ? 621  LEU A CB  1 
ATOM   3968 C CG  . LEU A 1 526 ? 23.763  51.544  2.491   1.00 41.84  ? 621  LEU A CG  1 
ATOM   3969 C CD1 . LEU A 1 526 ? 22.363  51.222  3.096   1.00 37.52  ? 621  LEU A CD1 1 
ATOM   3970 C CD2 . LEU A 1 526 ? 24.302  50.361  1.695   1.00 35.64  ? 621  LEU A CD2 1 
ATOM   3971 N N   . PHE A 1 527 ? 23.902  54.996  -0.471  1.00 39.61  ? 622  PHE A N   1 
ATOM   3972 C CA  . PHE A 1 527 ? 23.502  55.584  -1.746  1.00 39.29  ? 622  PHE A CA  1 
ATOM   3973 C C   . PHE A 1 527 ? 23.905  57.049  -1.644  1.00 42.98  ? 622  PHE A C   1 
ATOM   3974 O O   . PHE A 1 527 ? 23.093  57.903  -1.251  1.00 40.18  ? 622  PHE A O   1 
ATOM   3975 C CB  . PHE A 1 527 ? 22.010  55.375  -2.012  1.00 40.28  ? 622  PHE A CB  1 
ATOM   3976 C CG  . PHE A 1 527 ? 21.592  53.912  -1.969  1.00 42.61  ? 622  PHE A CG  1 
ATOM   3977 C CD1 . PHE A 1 527 ? 21.820  53.071  -3.061  1.00 41.86  ? 622  PHE A CD1 1 
ATOM   3978 C CD2 . PHE A 1 527 ? 21.027  53.374  -0.824  1.00 39.87  ? 622  PHE A CD2 1 
ATOM   3979 C CE1 . PHE A 1 527 ? 21.463  51.730  -3.013  1.00 40.29  ? 622  PHE A CE1 1 
ATOM   3980 C CE2 . PHE A 1 527 ? 20.662  52.030  -0.770  1.00 42.79  ? 622  PHE A CE2 1 
ATOM   3981 C CZ  . PHE A 1 527 ? 20.886  51.206  -1.868  1.00 40.21  ? 622  PHE A CZ  1 
ATOM   3982 N N   . PRO A 1 528 ? 25.169  57.367  -1.960  1.00 39.18  ? 623  PRO A N   1 
ATOM   3983 C CA  . PRO A 1 528 ? 25.709  58.701  -1.648  1.00 37.80  ? 623  PRO A CA  1 
ATOM   3984 C C   . PRO A 1 528 ? 24.966  59.817  -2.368  1.00 43.57  ? 623  PRO A C   1 
ATOM   3985 O O   . PRO A 1 528 ? 24.491  59.659  -3.498  1.00 41.72  ? 623  PRO A O   1 
ATOM   3986 C CB  . PRO A 1 528 ? 27.171  58.618  -2.118  1.00 42.36  ? 623  PRO A CB  1 
ATOM   3987 C CG  . PRO A 1 528 ? 27.479  57.126  -2.236  1.00 43.60  ? 623  PRO A CG  1 
ATOM   3988 C CD  . PRO A 1 528 ? 26.161  56.491  -2.618  1.00 41.79  ? 623  PRO A CD  1 
ATOM   3989 N N   . ARG A 1 529 ? 24.862  60.952  -1.680  1.00 41.53  ? 624  ARG A N   1 
ATOM   3990 C CA  . ARG A 1 529 ? 24.342  62.196  -2.237  1.00 43.66  ? 624  ARG A CA  1 
ATOM   3991 C C   . ARG A 1 529 ? 25.476  63.213  -2.317  1.00 43.82  ? 624  ARG A C   1 
ATOM   3992 O O   . ARG A 1 529 ? 26.071  63.568  -1.291  1.00 42.69  ? 624  ARG A O   1 
ATOM   3993 C CB  . ARG A 1 529 ? 23.211  62.750  -1.370  1.00 44.33  ? 624  ARG A CB  1 
ATOM   3994 C CG  . ARG A 1 529 ? 21.910  61.986  -1.446  1.00 44.97  ? 624  ARG A CG  1 
ATOM   3995 C CD  . ARG A 1 529 ? 21.296  62.117  -2.826  1.00 47.69  ? 624  ARG A CD  1 
ATOM   3996 N NE  . ARG A 1 529 ? 20.122  61.264  -2.955  1.00 47.30  ? 624  ARG A NE  1 
ATOM   3997 C CZ  . ARG A 1 529 ? 20.134  60.034  -3.444  1.00 47.72  ? 624  ARG A CZ  1 
ATOM   3998 N NH1 . ARG A 1 529 ? 21.257  59.466  -3.868  1.00 50.07  ? 624  ARG A NH1 1 
ATOM   3999 N NH2 . ARG A 1 529 ? 18.989  59.365  -3.536  1.00 43.40  ? 624  ARG A NH2 1 
ATOM   4000 N N   . ASP A 1 530 ? 25.767  63.689  -3.517  1.00 45.14  ? 625  ASP A N   1 
ATOM   4001 C CA  . ASP A 1 530 ? 26.722  64.784  -3.626  1.00 45.93  ? 625  ASP A CA  1 
ATOM   4002 C C   . ASP A 1 530 ? 26.174  65.742  -4.679  1.00 49.45  ? 625  ASP A C   1 
ATOM   4003 O O   . ASP A 1 530 ? 25.154  65.421  -5.306  1.00 46.69  ? 625  ASP A O   1 
ATOM   4004 C CB  . ASP A 1 530 ? 28.134  64.251  -3.928  1.00 48.74  ? 625  ASP A CB  1 
ATOM   4005 C CG  . ASP A 1 530 ? 28.262  63.584  -5.303  1.00 50.93  ? 625  ASP A CG  1 
ATOM   4006 O OD1 . ASP A 1 530 ? 27.858  64.169  -6.334  1.00 50.59  ? 625  ASP A OD1 1 
ATOM   4007 O OD2 . ASP A 1 530 ? 28.826  62.475  -5.346  1.00 51.82  ? 625  ASP A OD2 1 
ATOM   4008 N N   . PRO A 1 531 ? 26.781  66.918  -4.903  1.00 49.34  ? 626  PRO A N   1 
ATOM   4009 C CA  . PRO A 1 531 ? 26.133  67.903  -5.787  1.00 52.39  ? 626  PRO A CA  1 
ATOM   4010 C C   . PRO A 1 531 ? 25.885  67.393  -7.191  1.00 53.85  ? 626  PRO A C   1 
ATOM   4011 O O   . PRO A 1 531 ? 25.020  67.939  -7.885  1.00 55.76  ? 626  PRO A O   1 
ATOM   4012 C CB  . PRO A 1 531 ? 27.116  69.083  -5.784  1.00 52.43  ? 626  PRO A CB  1 
ATOM   4013 C CG  . PRO A 1 531 ? 27.828  68.960  -4.489  1.00 52.72  ? 626  PRO A CG  1 
ATOM   4014 C CD  . PRO A 1 531 ? 27.976  67.486  -4.251  1.00 49.66  ? 626  PRO A CD  1 
ATOM   4015 N N   . LYS A 1 532 ? 26.600  66.357  -7.628  1.00 49.68  ? 627  LYS A N   1 
ATOM   4016 C CA  . LYS A 1 532 ? 26.452  65.807  -8.968  1.00 54.57  ? 627  LYS A CA  1 
ATOM   4017 C C   . LYS A 1 532 ? 25.778  64.440  -8.974  1.00 54.71  ? 627  LYS A C   1 
ATOM   4018 O O   . LYS A 1 532 ? 25.734  63.789  -10.022 1.00 57.82  ? 627  LYS A O   1 
ATOM   4019 C CB  . LYS A 1 532 ? 27.821  65.725  -9.654  1.00 57.52  ? 627  LYS A CB  1 
ATOM   4020 C CG  . LYS A 1 532 ? 28.478  67.087  -9.836  1.00 59.66  ? 627  LYS A CG  1 
ATOM   4021 C CD  . LYS A 1 532 ? 29.846  66.980  -10.473 1.00 67.18  ? 627  LYS A CD  1 
ATOM   4022 C CE  . LYS A 1 532 ? 29.723  66.537  -11.910 1.00 73.97  ? 627  LYS A CE  1 
ATOM   4023 N NZ  . LYS A 1 532 ? 28.660  67.300  -12.635 1.00 83.83  ? 627  LYS A NZ  1 
ATOM   4024 N N   . ARG A 1 533 ? 25.264  63.981  -7.833  1.00 53.67  ? 628  ARG A N   1 
ATOM   4025 C CA  . ARG A 1 533 ? 24.658  62.655  -7.743  1.00 51.76  ? 628  ARG A CA  1 
ATOM   4026 C C   . ARG A 1 533 ? 23.395  62.713  -6.890  1.00 50.64  ? 628  ARG A C   1 
ATOM   4027 O O   . ARG A 1 533 ? 23.468  62.852  -5.662  1.00 45.23  ? 628  ARG A O   1 
ATOM   4028 C CB  . ARG A 1 533 ? 25.647  61.637  -7.178  1.00 50.48  ? 628  ARG A CB  1 
ATOM   4029 C CG  . ARG A 1 533 ? 25.054  60.252  -6.985  1.00 48.98  ? 628  ARG A CG  1 
ATOM   4030 C CD  . ARG A 1 533 ? 26.138  59.207  -6.694  1.00 48.85  ? 628  ARG A CD  1 
ATOM   4031 N NE  . ARG A 1 533 ? 27.004  58.988  -7.850  1.00 52.19  ? 628  ARG A NE  1 
ATOM   4032 C CZ  . ARG A 1 533 ? 26.666  58.256  -8.903  1.00 51.60  ? 628  ARG A CZ  1 
ATOM   4033 N NH1 . ARG A 1 533 ? 25.487  57.652  -8.977  1.00 44.48  ? 628  ARG A NH1 1 
ATOM   4034 N NH2 . ARG A 1 533 ? 27.531  58.121  -9.905  1.00 49.75  ? 628  ARG A NH2 1 
ATOM   4035 N N   . LEU A 1 534 ? 22.243  62.577  -7.540  1.00 50.76  ? 629  LEU A N   1 
ATOM   4036 C CA  . LEU A 1 534 ? 20.966  62.418  -6.863  1.00 51.39  ? 629  LEU A CA  1 
ATOM   4037 C C   . LEU A 1 534 ? 20.394  61.014  -7.025  1.00 53.46  ? 629  LEU A C   1 
ATOM   4038 O O   . LEU A 1 534 ? 19.381  60.694  -6.390  1.00 51.71  ? 629  LEU A O   1 
ATOM   4039 C CB  . LEU A 1 534 ? 19.964  63.467  -7.387  1.00 51.33  ? 629  LEU A CB  1 
ATOM   4040 C CG  . LEU A 1 534 ? 18.598  63.656  -6.705  1.00 53.53  ? 629  LEU A CG  1 
ATOM   4041 C CD1 . LEU A 1 534 ? 18.740  63.798  -5.179  1.00 49.09  ? 629  LEU A CD1 1 
ATOM   4042 C CD2 . LEU A 1 534 ? 17.863  64.853  -7.297  1.00 51.77  ? 629  LEU A CD2 1 
ATOM   4043 N N   . ILE A 1 535 ? 21.040  60.168  -7.821  1.00 53.53  ? 630  ILE A N   1 
ATOM   4044 C CA  . ILE A 1 535 ? 20.566  58.828  -8.163  1.00 53.19  ? 630  ILE A CA  1 
ATOM   4045 C C   . ILE A 1 535 ? 21.668  57.806  -7.897  1.00 54.88  ? 630  ILE A C   1 
ATOM   4046 O O   . ILE A 1 535 ? 22.854  58.159  -7.929  1.00 56.66  ? 630  ILE A O   1 
ATOM   4047 C CB  . ILE A 1 535 ? 20.124  58.767  -9.633  1.00 55.86  ? 630  ILE A CB  1 
ATOM   4048 C CG1 . ILE A 1 535 ? 21.222  59.341  -10.533 1.00 62.50  ? 630  ILE A CG1 1 
ATOM   4049 C CG2 . ILE A 1 535 ? 18.829  59.521  -9.819  1.00 56.58  ? 630  ILE A CG2 1 
ATOM   4050 C CD1 . ILE A 1 535 ? 22.157  58.300  -11.102 1.00 64.31  ? 630  ILE A CD1 1 
ATOM   4051 N N   . PRO A 1 536 ? 21.346  56.541  -7.610  1.00 53.19  ? 631  PRO A N   1 
ATOM   4052 C CA  . PRO A 1 536 ? 20.035  55.987  -7.261  1.00 53.11  ? 631  PRO A CA  1 
ATOM   4053 C C   . PRO A 1 536 ? 19.486  56.578  -5.952  1.00 54.96  ? 631  PRO A C   1 
ATOM   4054 O O   . PRO A 1 536 ? 20.218  57.098  -5.098  1.00 50.51  ? 631  PRO A O   1 
ATOM   4055 C CB  . PRO A 1 536 ? 20.319  54.489  -7.102  1.00 53.84  ? 631  PRO A CB  1 
ATOM   4056 C CG  . PRO A 1 536 ? 21.810  54.394  -6.897  1.00 51.58  ? 631  PRO A CG  1 
ATOM   4057 C CD  . PRO A 1 536 ? 22.380  55.495  -7.717  1.00 51.70  ? 631  PRO A CD  1 
ATOM   4058 O OXT . PRO A 1 536 ? 18.281  56.552  -5.715  1.00 56.41  ? 631  PRO A OXT 1 
ATOM   4059 N N   . ASN B 1 5   ? 15.783  105.951 53.778  1.00 124.95 ? 100  ASN B N   1 
ATOM   4060 C CA  . ASN B 1 5   ? 15.118  104.801 53.169  1.00 127.37 ? 100  ASN B CA  1 
ATOM   4061 C C   . ASN B 1 5   ? 16.011  103.554 53.169  1.00 129.75 ? 100  ASN B C   1 
ATOM   4062 O O   . ASN B 1 5   ? 17.014  103.492 52.451  1.00 128.40 ? 100  ASN B O   1 
ATOM   4063 C CB  . ASN B 1 5   ? 14.683  105.134 51.740  1.00 123.01 ? 100  ASN B CB  1 
ATOM   4064 N N   . LEU B 1 6   ? 15.628  102.559 53.971  1.00 129.57 ? 101  LEU B N   1 
ATOM   4065 C CA  . LEU B 1 6   ? 16.392  101.329 54.138  1.00 126.68 ? 101  LEU B CA  1 
ATOM   4066 C C   . LEU B 1 6   ? 15.952  100.221 53.189  1.00 130.65 ? 101  LEU B C   1 
ATOM   4067 O O   . LEU B 1 6   ? 16.329  99.060  53.389  1.00 127.76 ? 101  LEU B O   1 
ATOM   4068 C CB  . LEU B 1 6   ? 16.289  100.835 55.583  1.00 125.31 ? 101  LEU B CB  1 
ATOM   4069 N N   . LYS B 1 7   ? 15.163  100.545 52.165  1.00 131.52 ? 102  LYS B N   1 
ATOM   4070 C CA  . LYS B 1 7   ? 14.737  99.521  51.220  1.00 127.87 ? 102  LYS B CA  1 
ATOM   4071 C C   . LYS B 1 7   ? 15.865  99.112  50.280  1.00 127.02 ? 102  LYS B C   1 
ATOM   4072 O O   . LYS B 1 7   ? 15.851  97.991  49.752  1.00 125.75 ? 102  LYS B O   1 
ATOM   4073 C CB  . LYS B 1 7   ? 13.529  100.015 50.421  1.00 131.93 ? 102  LYS B CB  1 
ATOM   4074 N N   . ASN B 1 8   ? 16.846  99.994  50.063  1.00 123.92 ? 103  ASN B N   1 
ATOM   4075 C CA  . ASN B 1 8   ? 17.952  99.652  49.173  1.00 122.30 ? 103  ASN B CA  1 
ATOM   4076 C C   . ASN B 1 8   ? 18.790  98.517  49.755  1.00 118.87 ? 103  ASN B C   1 
ATOM   4077 O O   . ASN B 1 8   ? 19.211  97.609  49.027  1.00 112.67 ? 103  ASN B O   1 
ATOM   4078 C CB  . ASN B 1 8   ? 18.811  100.892 48.898  1.00 119.79 ? 103  ASN B CB  1 
ATOM   4079 C CG  . ASN B 1 8   ? 19.258  100.987 47.438  1.00 121.62 ? 103  ASN B CG  1 
ATOM   4080 O OD1 . ASN B 1 8   ? 18.492  100.690 46.516  1.00 121.69 ? 103  ASN B OD1 1 
ATOM   4081 N ND2 . ASN B 1 8   ? 20.507  101.392 47.227  1.00 119.27 ? 103  ASN B ND2 1 
ATOM   4082 N N   . GLU B 1 9   ? 19.021  98.540  51.072  1.00 119.12 ? 104  GLU B N   1 
ATOM   4083 C CA  . GLU B 1 9   ? 19.737  97.446  51.719  1.00 117.56 ? 104  GLU B CA  1 
ATOM   4084 C C   . GLU B 1 9   ? 18.949  96.143  51.647  1.00 114.93 ? 104  GLU B C   1 
ATOM   4085 O O   . GLU B 1 9   ? 19.543  95.059  51.659  1.00 113.37 ? 104  GLU B O   1 
ATOM   4086 C CB  . GLU B 1 9   ? 20.045  97.807  53.173  1.00 120.27 ? 104  GLU B CB  1 
ATOM   4087 N N   . ALA B 1 10  ? 17.617  96.225  51.566  1.00 115.99 ? 105  ALA B N   1 
ATOM   4088 C CA  . ALA B 1 10  ? 16.795  95.024  51.443  1.00 110.79 ? 105  ALA B CA  1 
ATOM   4089 C C   . ALA B 1 10  ? 16.853  94.446  50.034  1.00 109.91 ? 105  ALA B C   1 
ATOM   4090 O O   . ALA B 1 10  ? 16.946  93.220  49.859  1.00 105.62 ? 105  ALA B O   1 
ATOM   4091 C CB  . ALA B 1 10  ? 15.349  95.334  51.837  1.00 105.77 ? 105  ALA B CB  1 
ATOM   4092 N N   . THR B 1 11  ? 16.791  95.311  49.018  1.00 111.06 ? 106  THR B N   1 
ATOM   4093 C CA  . THR B 1 11  ? 16.954  94.835  47.646  1.00 108.88 ? 106  THR B CA  1 
ATOM   4094 C C   . THR B 1 11  ? 18.345  94.255  47.431  1.00 106.18 ? 106  THR B C   1 
ATOM   4095 O O   . THR B 1 11  ? 18.507  93.279  46.691  1.00 101.42 ? 106  THR B O   1 
ATOM   4096 C CB  . THR B 1 11  ? 16.693  95.958  46.641  1.00 110.28 ? 106  THR B CB  1 
ATOM   4097 O OG1 . THR B 1 11  ? 17.745  96.926  46.715  1.00 115.30 ? 106  THR B OG1 1 
ATOM   4098 C CG2 . THR B 1 11  ? 15.362  96.630  46.927  1.00 113.31 ? 106  THR B CG2 1 
ATOM   4099 N N   . LYS B 1 12  ? 19.362  94.841  48.072  1.00 106.04 ? 107  LYS B N   1 
ATOM   4100 C CA  . LYS B 1 12  ? 20.706  94.277  47.990  1.00 106.69 ? 107  LYS B CA  1 
ATOM   4101 C C   . LYS B 1 12  ? 20.755  92.864  48.558  1.00 104.28 ? 107  LYS B C   1 
ATOM   4102 O O   . LYS B 1 12  ? 21.603  92.061  48.149  1.00 102.12 ? 107  LYS B O   1 
ATOM   4103 C CB  . LYS B 1 12  ? 21.705  95.180  48.716  1.00 109.34 ? 107  LYS B CB  1 
ATOM   4104 N N   . VAL B 1 13  ? 19.858  92.542  49.496  1.00 103.63 ? 108  VAL B N   1 
ATOM   4105 C CA  . VAL B 1 13  ? 19.755  91.176  50.003  1.00 100.62 ? 108  VAL B CA  1 
ATOM   4106 C C   . VAL B 1 13  ? 19.011  90.286  49.014  1.00 98.57  ? 108  VAL B C   1 
ATOM   4107 O O   . VAL B 1 13  ? 19.390  89.128  48.800  1.00 93.42  ? 108  VAL B O   1 
ATOM   4108 C CB  . VAL B 1 13  ? 19.080  91.166  51.387  1.00 101.15 ? 108  VAL B CB  1 
ATOM   4109 N N   . LEU B 1 14  ? 17.941  90.801  48.398  1.00 98.55  ? 109  LEU B N   1 
ATOM   4110 C CA  . LEU B 1 14  ? 17.180  89.979  47.453  1.00 95.28  ? 109  LEU B CA  1 
ATOM   4111 C C   . LEU B 1 14  ? 18.006  89.619  46.221  1.00 94.45  ? 109  LEU B C   1 
ATOM   4112 O O   . LEU B 1 14  ? 17.917  88.494  45.709  1.00 92.02  ? 109  LEU B O   1 
ATOM   4113 C CB  . LEU B 1 14  ? 15.895  90.694  47.034  1.00 94.67  ? 109  LEU B CB  1 
ATOM   4114 C CG  . LEU B 1 14  ? 14.773  90.782  48.066  1.00 92.51  ? 109  LEU B CG  1 
ATOM   4115 C CD1 . LEU B 1 14  ? 13.453  91.074  47.379  1.00 91.22  ? 109  LEU B CD1 1 
ATOM   4116 C CD2 . LEU B 1 14  ? 14.681  89.503  48.880  1.00 92.38  ? 109  LEU B CD2 1 
ATOM   4117 N N   . GLU B 1 15  ? 18.797  90.560  45.716  1.00 94.05  ? 110  GLU B N   1 
ATOM   4118 C CA  . GLU B 1 15  ? 19.634  90.324  44.549  1.00 94.92  ? 110  GLU B CA  1 
ATOM   4119 C C   . GLU B 1 15  ? 21.050  89.910  44.920  1.00 92.52  ? 110  GLU B C   1 
ATOM   4120 O O   . GLU B 1 15  ? 21.973  90.100  44.119  1.00 94.29  ? 110  GLU B O   1 
ATOM   4121 C CB  . GLU B 1 15  ? 19.654  91.572  43.664  1.00 98.13  ? 110  GLU B CB  1 
ATOM   4122 C CG  . GLU B 1 15  ? 18.271  92.019  43.238  1.00 102.19 ? 110  GLU B CG  1 
ATOM   4123 C CD  . GLU B 1 15  ? 18.261  93.393  42.602  1.00 109.91 ? 110  GLU B CD  1 
ATOM   4124 O OE1 . GLU B 1 15  ? 17.192  93.820  42.124  1.00 112.43 ? 110  GLU B OE1 1 
ATOM   4125 O OE2 . GLU B 1 15  ? 19.328  94.049  42.583  1.00 110.08 ? 110  GLU B OE2 1 
ATOM   4126 N N   . HIS B 1 16  ? 21.205  89.385  46.108  1.00 91.43  ? 111  HIS B N   1 
ATOM   4127 C CA  . HIS B 1 16  ? 22.507  89.034  46.581  1.00 91.14  ? 111  HIS B CA  1 
ATOM   4128 C C   . HIS B 1 16  ? 23.302  88.028  45.782  1.00 90.43  ? 111  HIS B C   1 
ATOM   4129 O O   . HIS B 1 16  ? 22.833  86.956  45.477  1.00 88.11  ? 111  HIS B O   1 
ATOM   4130 C CB  . HIS B 1 16  ? 22.417  88.545  48.001  1.00 92.79  ? 111  HIS B CB  1 
ATOM   4131 C CG  . HIS B 1 16  ? 23.743  88.406  48.641  1.00 93.04  ? 111  HIS B CG  1 
ATOM   4132 N ND1 . HIS B 1 16  ? 24.679  89.407  48.593  1.00 94.17  ? 111  HIS B ND1 1 
ATOM   4133 C CD2 . HIS B 1 16  ? 24.306  87.391  49.322  1.00 93.28  ? 111  HIS B CD2 1 
ATOM   4134 C CE1 . HIS B 1 16  ? 25.764  89.016  49.225  1.00 97.14  ? 111  HIS B CE1 1 
ATOM   4135 N NE2 . HIS B 1 16  ? 25.559  87.800  49.681  1.00 96.04  ? 111  HIS B NE2 1 
ATOM   4136 N N   . VAL B 1 17  ? 24.536  88.381  45.490  1.00 89.80  ? 112  VAL B N   1 
ATOM   4137 C CA  . VAL B 1 17  ? 25.425  87.517  44.773  1.00 88.52  ? 112  VAL B CA  1 
ATOM   4138 C C   . VAL B 1 17  ? 26.452  87.017  45.739  1.00 91.52  ? 112  VAL B C   1 
ATOM   4139 O O   . VAL B 1 17  ? 27.237  87.776  46.238  1.00 96.91  ? 112  VAL B O   1 
ATOM   4140 C CB  . VAL B 1 17  ? 26.195  88.286  43.719  1.00 89.32  ? 112  VAL B CB  1 
ATOM   4141 C CG1 . VAL B 1 17  ? 27.443  87.530  43.342  1.00 90.18  ? 112  VAL B CG1 1 
ATOM   4142 C CG2 . VAL B 1 17  ? 25.333  88.582  42.518  1.00 84.87  ? 112  VAL B CG2 1 
ATOM   4143 N N   . CYS B 1 18  ? 26.459  85.732  46.012  1.00 90.00  ? 113  CYS B N   1 
ATOM   4144 C CA  . CYS B 1 18  ? 27.440  85.192  46.918  1.00 95.12  ? 113  CYS B CA  1 
ATOM   4145 C C   . CYS B 1 18  ? 28.809  85.295  46.307  1.00 98.97  ? 113  CYS B C   1 
ATOM   4146 O O   . CYS B 1 18  ? 28.963  85.111  45.127  1.00 99.14  ? 113  CYS B O   1 
ATOM   4147 C CB  . CYS B 1 18  ? 27.141  83.749  47.222  1.00 93.92  ? 113  CYS B CB  1 
ATOM   4148 S SG  . CYS B 1 18  ? 28.620  82.893  47.734  1.00 101.31 ? 113  CYS B SG  1 
ATOM   4149 N N   . GLU B 1 19  ? 29.822  85.569  47.108  1.00 102.54 ? 114  GLU B N   1 
ATOM   4150 C CA  . GLU B 1 19  ? 31.164  85.708  46.567  1.00 105.54 ? 114  GLU B CA  1 
ATOM   4151 C C   . GLU B 1 19  ? 32.130  84.682  47.115  1.00 107.32 ? 114  GLU B C   1 
ATOM   4152 O O   . GLU B 1 19  ? 33.220  84.512  46.600  1.00 108.68 ? 114  GLU B O   1 
ATOM   4153 C CB  . GLU B 1 19  ? 31.691  87.108  46.808  1.00 108.65 ? 114  GLU B CB  1 
ATOM   4154 C CG  . GLU B 1 19  ? 32.748  87.523  45.814  1.00 111.33 ? 114  GLU B CG  1 
ATOM   4155 C CD  . GLU B 1 19  ? 32.150  87.910  44.494  1.00 110.68 ? 114  GLU B CD  1 
ATOM   4156 O OE1 . GLU B 1 19  ? 32.849  87.805  43.471  1.00 112.52 ? 114  GLU B OE1 1 
ATOM   4157 O OE2 . GLU B 1 19  ? 30.979  88.316  44.492  1.00 107.21 ? 114  GLU B OE2 1 
ATOM   4158 N N   . ASP B 1 20  ? 31.751  84.036  48.198  1.00 106.53 ? 115  ASP B N   1 
ATOM   4159 C CA  . ASP B 1 20  ? 32.564  82.967  48.734  1.00 108.88 ? 115  ASP B CA  1 
ATOM   4160 C C   . ASP B 1 20  ? 31.660  81.972  49.399  1.00 107.91 ? 115  ASP B C   1 
ATOM   4161 O O   . ASP B 1 20  ? 31.121  82.239  50.444  1.00 108.99 ? 115  ASP B O   1 
ATOM   4162 C CB  . ASP B 1 20  ? 33.575  83.492  49.727  1.00 114.42 ? 115  ASP B CB  1 
ATOM   4163 C CG  . ASP B 1 20  ? 34.496  82.426  50.223  1.00 114.72 ? 115  ASP B CG  1 
ATOM   4164 O OD1 . ASP B 1 20  ? 34.031  81.309  50.494  1.00 112.36 ? 115  ASP B OD1 1 
ATOM   4165 O OD2 . ASP B 1 20  ? 35.694  82.709  50.357  1.00 118.95 ? 115  ASP B OD2 1 
ATOM   4166 N N   . ILE B 1 21  ? 31.553  80.790  48.832  1.00 109.31 ? 116  ILE B N   1 
ATOM   4167 C CA  . ILE B 1 21  ? 30.679  79.781  49.395  1.00 107.35 ? 116  ILE B CA  1 
ATOM   4168 C C   . ILE B 1 21  ? 31.080  79.283  50.770  1.00 106.69 ? 116  ILE B C   1 
ATOM   4169 O O   . ILE B 1 21  ? 30.236  78.918  51.564  1.00 106.30 ? 116  ILE B O   1 
ATOM   4170 C CB  . ILE B 1 21  ? 30.383  78.632  48.416  1.00 102.79 ? 116  ILE B CB  1 
ATOM   4171 C CG1 . ILE B 1 21  ? 31.597  77.743  48.225  1.00 104.77 ? 116  ILE B CG1 1 
ATOM   4172 C CG2 . ILE B 1 21  ? 29.927  79.203  47.096  1.00 96.48  ? 116  ILE B CG2 1 
ATOM   4173 C CD1 . ILE B 1 21  ? 31.229  76.347  47.790  1.00 102.77 ? 116  ILE B CD1 1 
ATOM   4174 N N   . ASN B 1 22  ? 32.368  79.218  51.042  1.00 107.07 ? 117  ASN B N   1 
ATOM   4175 C CA  . ASN B 1 22  ? 32.805  78.736  52.336  1.00 109.22 ? 117  ASN B CA  1 
ATOM   4176 C C   . ASN B 1 22  ? 32.325  79.604  53.477  1.00 109.71 ? 117  ASN B C   1 
ATOM   4177 O O   . ASN B 1 22  ? 31.920  79.117  54.521  1.00 109.29 ? 117  ASN B O   1 
ATOM   4178 C CB  . ASN B 1 22  ? 34.315  78.735  52.400  1.00 108.91 ? 117  ASN B CB  1 
ATOM   4179 C CG  . ASN B 1 22  ? 34.939  78.265  51.134  1.00 109.19 ? 117  ASN B CG  1 
ATOM   4180 O OD1 . ASN B 1 22  ? 34.955  77.078  50.852  1.00 112.60 ? 117  ASN B OD1 1 
ATOM   4181 N ND2 . ASN B 1 22  ? 35.476  79.189  50.369  1.00 109.61 ? 117  ASN B ND2 1 
ATOM   4182 N N   . LYS B 1 23  ? 32.377  80.904  53.259  1.00 110.21 ? 118  LYS B N   1 
ATOM   4183 C CA  . LYS B 1 23  ? 32.024  81.863  54.268  1.00 111.32 ? 118  LYS B CA  1 
ATOM   4184 C C   . LYS B 1 23  ? 30.595  82.319  54.176  1.00 112.04 ? 118  LYS B C   1 
ATOM   4185 O O   . LYS B 1 23  ? 30.193  83.228  54.881  1.00 113.31 ? 118  LYS B O   1 
ATOM   4186 C CB  . LYS B 1 23  ? 32.975  83.048  54.172  1.00 112.57 ? 118  LYS B CB  1 
ATOM   4187 C CG  . LYS B 1 23  ? 34.420  82.661  54.438  1.00 112.44 ? 118  LYS B CG  1 
ATOM   4188 C CD  . LYS B 1 23  ? 35.360  83.838  54.283  1.00 111.34 ? 118  LYS B CD  1 
ATOM   4189 N N   . GLU B 1 24  ? 29.814  81.706  53.307  1.00 109.22 ? 119  GLU B N   1 
ATOM   4190 C CA  . GLU B 1 24  ? 28.447  82.147  53.176  1.00 107.11 ? 119  GLU B CA  1 
ATOM   4191 C C   . GLU B 1 24  ? 27.466  81.005  53.133  1.00 103.77 ? 119  GLU B C   1 
ATOM   4192 O O   . GLU B 1 24  ? 27.850  79.854  53.223  1.00 102.32 ? 119  GLU B O   1 
ATOM   4193 C CB  . GLU B 1 24  ? 28.349  82.940  51.910  1.00 106.51 ? 119  GLU B CB  1 
ATOM   4194 C CG  . GLU B 1 24  ? 27.456  84.129  51.993  1.00 106.89 ? 119  GLU B CG  1 
ATOM   4195 C CD  . GLU B 1 24  ? 27.840  85.134  50.962  1.00 106.85 ? 119  GLU B CD  1 
ATOM   4196 O OE1 . GLU B 1 24  ? 29.021  85.197  50.599  1.00 106.30 ? 119  GLU B OE1 1 
ATOM   4197 O OE2 . GLU B 1 24  ? 26.957  85.851  50.518  1.00 106.42 ? 119  GLU B OE2 1 
ATOM   4198 N N   . SER B 1 25  ? 26.187  81.316  53.005  1.00 99.91  ? 120  SER B N   1 
ATOM   4199 C CA  . SER B 1 25  ? 25.207  80.237  52.943  1.00 94.56  ? 120  SER B CA  1 
ATOM   4200 C C   . SER B 1 25  ? 24.106  80.432  51.907  1.00 91.98  ? 120  SER B C   1 
ATOM   4201 O O   . SER B 1 25  ? 23.249  79.551  51.779  1.00 87.58  ? 120  SER B O   1 
ATOM   4202 C CB  . SER B 1 25  ? 24.561  80.022  54.324  1.00 95.59  ? 120  SER B CB  1 
ATOM   4203 O OG  . SER B 1 25  ? 25.443  79.365  55.214  1.00 98.42  ? 120  SER B OG  1 
ATOM   4204 N N   . TYR B 1 26  ? 24.102  81.531  51.161  1.00 90.90  ? 121  TYR B N   1 
ATOM   4205 C CA  . TYR B 1 26  ? 23.072  81.755  50.156  1.00 86.33  ? 121  TYR B CA  1 
ATOM   4206 C C   . TYR B 1 26  ? 23.566  82.790  49.157  1.00 87.96  ? 121  TYR B C   1 
ATOM   4207 O O   . TYR B 1 26  ? 24.605  83.424  49.353  1.00 89.76  ? 121  TYR B O   1 
ATOM   4208 C CB  . TYR B 1 26  ? 21.752  82.191  50.792  1.00 85.21  ? 121  TYR B CB  1 
ATOM   4209 C CG  . TYR B 1 26  ? 21.830  83.499  51.559  1.00 91.72  ? 121  TYR B CG  1 
ATOM   4210 C CD1 . TYR B 1 26  ? 22.417  83.559  52.818  1.00 91.22  ? 121  TYR B CD1 1 
ATOM   4211 C CD2 . TYR B 1 26  ? 21.289  84.667  51.033  1.00 90.04  ? 121  TYR B CD2 1 
ATOM   4212 C CE1 . TYR B 1 26  ? 22.477  84.743  53.523  1.00 96.34  ? 121  TYR B CE1 1 
ATOM   4213 C CE2 . TYR B 1 26  ? 21.341  85.858  51.733  1.00 94.22  ? 121  TYR B CE2 1 
ATOM   4214 C CZ  . TYR B 1 26  ? 21.936  85.889  52.978  1.00 96.06  ? 121  TYR B CZ  1 
ATOM   4215 O OH  . TYR B 1 26  ? 21.991  87.068  53.679  1.00 101.63 ? 121  TYR B OH  1 
ATOM   4216 N N   . GLY B 1 27  ? 22.794  82.955  48.081  1.00 85.69  ? 122  GLY B N   1 
ATOM   4217 C CA  . GLY B 1 27  ? 23.105  83.932  47.057  1.00 84.52  ? 122  GLY B CA  1 
ATOM   4218 C C   . GLY B 1 27  ? 23.229  83.332  45.668  1.00 84.88  ? 122  GLY B C   1 
ATOM   4219 O O   . GLY B 1 27  ? 23.468  82.129  45.524  1.00 80.86  ? 122  GLY B O   1 
ATOM   4220 N N   . PHE B 1 28  ? 23.037  84.157  44.639  1.00 81.52  ? 123  PHE B N   1 
ATOM   4221 C CA  . PHE B 1 28  ? 23.381  83.754  43.283  1.00 79.70  ? 123  PHE B CA  1 
ATOM   4222 C C   . PHE B 1 28  ? 24.891  83.620  43.159  1.00 81.75  ? 123  PHE B C   1 
ATOM   4223 O O   . PHE B 1 28  ? 25.652  84.423  43.707  1.00 83.69  ? 123  PHE B O   1 
ATOM   4224 C CB  . PHE B 1 28  ? 22.863  84.767  42.266  1.00 78.07  ? 123  PHE B CB  1 
ATOM   4225 C CG  . PHE B 1 28  ? 21.400  85.040  42.384  1.00 78.83  ? 123  PHE B CG  1 
ATOM   4226 C CD1 . PHE B 1 28  ? 20.473  84.120  41.918  1.00 76.88  ? 123  PHE B CD1 1 
ATOM   4227 C CD2 . PHE B 1 28  ? 20.947  86.217  42.960  1.00 81.12  ? 123  PHE B CD2 1 
ATOM   4228 C CE1 . PHE B 1 28  ? 19.121  84.364  42.024  1.00 76.91  ? 123  PHE B CE1 1 
ATOM   4229 C CE2 . PHE B 1 28  ? 19.596  86.473  43.071  1.00 81.61  ? 123  PHE B CE2 1 
ATOM   4230 C CZ  . PHE B 1 28  ? 18.678  85.545  42.603  1.00 80.25  ? 123  PHE B CZ  1 
ATOM   4231 N N   . VAL B 1 29  ? 25.325  82.601  42.430  1.00 77.69  ? 124  VAL B N   1 
ATOM   4232 C CA  . VAL B 1 29  ? 26.743  82.281  42.359  1.00 80.10  ? 124  VAL B CA  1 
ATOM   4233 C C   . VAL B 1 29  ? 27.053  81.777  40.958  1.00 81.16  ? 124  VAL B C   1 
ATOM   4234 O O   . VAL B 1 29  ? 26.298  80.982  40.392  1.00 79.31  ? 124  VAL B O   1 
ATOM   4235 C CB  . VAL B 1 29  ? 27.117  81.244  43.434  1.00 83.48  ? 124  VAL B CB  1 
ATOM   4236 C CG1 . VAL B 1 29  ? 26.125  80.121  43.410  1.00 82.60  ? 124  VAL B CG1 1 
ATOM   4237 C CG2 . VAL B 1 29  ? 28.517  80.712  43.212  1.00 87.74  ? 124  VAL B CG2 1 
ATOM   4238 N N   . LYS B 1 30  ? 28.145  82.270  40.383  1.00 82.63  ? 125  LYS B N   1 
ATOM   4239 C CA  . LYS B 1 30  ? 28.601  81.742  39.109  1.00 82.60  ? 125  LYS B CA  1 
ATOM   4240 C C   . LYS B 1 30  ? 29.274  80.394  39.327  1.00 81.93  ? 125  LYS B C   1 
ATOM   4241 O O   . LYS B 1 30  ? 29.864  80.134  40.378  1.00 81.97  ? 125  LYS B O   1 
ATOM   4242 C CB  . LYS B 1 30  ? 29.544  82.731  38.424  1.00 86.03  ? 125  LYS B CB  1 
ATOM   4243 C CG  . LYS B 1 30  ? 28.807  83.690  37.500  1.00 90.80  ? 125  LYS B CG  1 
ATOM   4244 C CD  . LYS B 1 30  ? 29.491  85.042  37.393  1.00 95.20  ? 125  LYS B CD  1 
ATOM   4245 C CE  . LYS B 1 30  ? 30.809  84.945  36.634  1.00 101.53 ? 125  LYS B CE  1 
ATOM   4246 N NZ  . LYS B 1 30  ? 31.109  86.190  35.864  1.00 103.05 ? 125  LYS B NZ  1 
ATOM   4247 N N   . ILE B 1 31  ? 29.160  79.522  38.322  1.00 82.50  ? 126  ILE B N   1 
ATOM   4248 C CA  . ILE B 1 31  ? 29.535  78.125  38.510  1.00 80.07  ? 126  ILE B CA  1 
ATOM   4249 C C   . ILE B 1 31  ? 31.012  77.996  38.866  1.00 82.32  ? 126  ILE B C   1 
ATOM   4250 O O   . ILE B 1 31  ? 31.400  77.084  39.607  1.00 81.63  ? 126  ILE B O   1 
ATOM   4251 C CB  . ILE B 1 31  ? 29.165  77.309  37.254  1.00 78.42  ? 126  ILE B CB  1 
ATOM   4252 C CG1 . ILE B 1 31  ? 28.953  75.837  37.610  1.00 71.81  ? 126  ILE B CG1 1 
ATOM   4253 C CG2 . ILE B 1 31  ? 30.216  77.453  36.179  1.00 81.28  ? 126  ILE B CG2 1 
ATOM   4254 C CD1 . ILE B 1 31  ? 27.696  75.592  38.432  1.00 68.85  ? 126  ILE B CD1 1 
ATOM   4255 N N   . SER B 1 32  ? 31.854  78.913  38.374  1.00 81.99  ? 127  SER B N   1 
ATOM   4256 C CA  . SER B 1 32  ? 33.275  78.871  38.709  1.00 80.62  ? 127  SER B CA  1 
ATOM   4257 C C   . SER B 1 32  ? 33.501  79.104  40.199  1.00 87.37  ? 127  SER B C   1 
ATOM   4258 O O   . SER B 1 32  ? 34.378  78.478  40.808  1.00 89.05  ? 127  SER B O   1 
ATOM   4259 C CB  . SER B 1 32  ? 34.034  79.907  37.884  1.00 81.77  ? 127  SER B CB  1 
ATOM   4260 O OG  . SER B 1 32  ? 33.453  81.191  38.021  1.00 85.35  ? 127  SER B OG  1 
ATOM   4261 N N   . LYS B 1 33  ? 32.709  79.990  40.809  1.00 86.91  ? 128  LYS B N   1 
ATOM   4262 C CA  . LYS B 1 33  ? 32.866  80.285  42.228  1.00 88.84  ? 128  LYS B CA  1 
ATOM   4263 C C   . LYS B 1 33  ? 32.496  79.112  43.125  1.00 92.41  ? 128  LYS B C   1 
ATOM   4264 O O   . LYS B 1 33  ? 32.708  79.200  44.336  1.00 96.20  ? 128  LYS B O   1 
ATOM   4265 C CB  . LYS B 1 33  ? 32.027  81.507  42.611  1.00 85.23  ? 128  LYS B CB  1 
ATOM   4266 N N   . MET B 1 34  ? 31.964  78.019  42.576  1.00 91.30  ? 129  MET B N   1 
ATOM   4267 C CA  . MET B 1 34  ? 31.491  76.905  43.400  1.00 96.18  ? 129  MET B CA  1 
ATOM   4268 C C   . MET B 1 34  ? 32.660  75.977  43.724  1.00 101.83 ? 129  MET B C   1 
ATOM   4269 O O   . MET B 1 34  ? 32.883  74.951  43.079  1.00 100.93 ? 129  MET B O   1 
ATOM   4270 C CB  . MET B 1 34  ? 30.362  76.161  42.702  1.00 90.59  ? 129  MET B CB  1 
ATOM   4271 C CG  . MET B 1 34  ? 29.478  75.389  43.661  1.00 91.02  ? 129  MET B CG  1 
ATOM   4272 S SD  . MET B 1 34  ? 28.184  76.448  44.335  1.00 97.02  ? 129  MET B SD  1 
ATOM   4273 C CE  . MET B 1 34  ? 27.503  77.034  42.791  1.00 91.17  ? 129  MET B CE  1 
ATOM   4274 N N   . LYS B 1 35  ? 33.408  76.344  44.770  1.00 109.79 ? 130  LYS B N   1 
ATOM   4275 C CA  . LYS B 1 35  ? 34.581  75.585  45.230  1.00 114.63 ? 130  LYS B CA  1 
ATOM   4276 C C   . LYS B 1 35  ? 34.530  75.512  46.756  1.00 116.03 ? 130  LYS B C   1 
ATOM   4277 O O   . LYS B 1 35  ? 35.023  76.410  47.439  1.00 115.95 ? 130  LYS B O   1 
ATOM   4278 C CB  . LYS B 1 35  ? 35.879  76.227  44.745  1.00 111.61 ? 130  LYS B CB  1 
ATOM   4279 C CG  . LYS B 1 35  ? 36.189  76.025  43.268  1.00 110.23 ? 130  LYS B CG  1 
ATOM   4280 C CD  . LYS B 1 35  ? 37.121  74.844  43.051  1.00 113.31 ? 130  LYS B CD  1 
ATOM   4281 N N   . GLU B 1 36  ? 33.945  74.433  47.283  1.00 119.85 ? 131  GLU B N   1 
ATOM   4282 C CA  . GLU B 1 36  ? 33.846  74.230  48.732  1.00 119.51 ? 131  GLU B CA  1 
ATOM   4283 C C   . GLU B 1 36  ? 35.177  73.679  49.241  1.00 126.50 ? 131  GLU B C   1 
ATOM   4284 O O   . GLU B 1 36  ? 35.357  72.474  49.441  1.00 129.02 ? 131  GLU B O   1 
ATOM   4285 C CB  . GLU B 1 36  ? 32.686  73.301  49.088  1.00 117.19 ? 131  GLU B CB  1 
ATOM   4286 C CG  . GLU B 1 36  ? 32.346  73.305  50.585  1.00 121.31 ? 131  GLU B CG  1 
ATOM   4287 C CD  . GLU B 1 36  ? 31.488  72.121  51.023  1.00 116.92 ? 131  GLU B CD  1 
ATOM   4288 O OE1 . GLU B 1 36  ? 31.646  71.020  50.456  1.00 117.01 ? 131  GLU B OE1 1 
ATOM   4289 O OE2 . GLU B 1 36  ? 30.660  72.293  51.946  1.00 110.41 ? 131  GLU B OE2 1 
ATOM   4290 N N   . ASN B 1 37  ? 36.119  74.596  49.464  1.00 119.01 ? 132  ASN B N   1 
ATOM   4291 C CA  . ASN B 1 37  ? 37.469  74.263  49.924  1.00 114.36 ? 132  ASN B CA  1 
ATOM   4292 C C   . ASN B 1 37  ? 38.145  73.236  49.015  1.00 115.30 ? 132  ASN B C   1 
ATOM   4293 O O   . ASN B 1 37  ? 38.100  72.032  49.275  1.00 115.63 ? 132  ASN B O   1 
ATOM   4294 C CB  . ASN B 1 37  ? 37.434  73.748  51.367  1.00 112.23 ? 132  ASN B CB  1 
ATOM   4295 N N   . GLU B 1 40  ? 36.609  68.763  46.283  1.00 108.51 ? 135  GLU B N   1 
ATOM   4296 C CA  . GLU B 1 40  ? 35.526  69.149  45.387  1.00 104.84 ? 135  GLU B CA  1 
ATOM   4297 C C   . GLU B 1 40  ? 34.178  68.678  45.930  1.00 101.00 ? 135  GLU B C   1 
ATOM   4298 O O   . GLU B 1 40  ? 34.114  67.943  46.920  1.00 99.95  ? 135  GLU B O   1 
ATOM   4299 C CB  . GLU B 1 40  ? 35.758  68.588  43.981  1.00 104.88 ? 135  GLU B CB  1 
ATOM   4300 N N   . ILE B 1 41  ? 33.103  69.101  45.267  1.00 96.74  ? 136  ILE B N   1 
ATOM   4301 C CA  . ILE B 1 41  ? 31.742  68.860  45.732  1.00 90.46  ? 136  ILE B CA  1 
ATOM   4302 C C   . ILE B 1 41  ? 31.207  67.575  45.113  1.00 85.69  ? 136  ILE B C   1 
ATOM   4303 O O   . ILE B 1 41  ? 31.380  67.324  43.916  1.00 85.73  ? 136  ILE B O   1 
ATOM   4304 C CB  . ILE B 1 41  ? 30.838  70.061  45.395  1.00 85.10  ? 136  ILE B CB  1 
ATOM   4305 C CG1 . ILE B 1 41  ? 31.274  71.296  46.195  1.00 91.84  ? 136  ILE B CG1 1 
ATOM   4306 C CG2 . ILE B 1 41  ? 29.379  69.733  45.662  1.00 82.53  ? 136  ILE B CG2 1 
ATOM   4307 C CD1 . ILE B 1 41  ? 30.322  72.475  46.097  1.00 88.03  ? 136  ILE B CD1 1 
ATOM   4308 N N   . ARG B 1 42  ? 30.556  66.754  45.934  1.00 82.24  ? 137  ARG B N   1 
ATOM   4309 C CA  . ARG B 1 42  ? 29.887  65.541  45.464  1.00 81.36  ? 137  ARG B CA  1 
ATOM   4310 C C   . ARG B 1 42  ? 28.431  65.884  45.166  1.00 78.00  ? 137  ARG B C   1 
ATOM   4311 O O   . ARG B 1 42  ? 27.581  65.871  46.060  1.00 78.07  ? 137  ARG B O   1 
ATOM   4312 C CB  . ARG B 1 42  ? 30.000  64.431  46.503  1.00 82.58  ? 137  ARG B CB  1 
ATOM   4313 N N   . LEU B 1 43  ? 28.134  66.191  43.904  1.00 77.39  ? 138  LEU B N   1 
ATOM   4314 C CA  . LEU B 1 43  ? 26.818  66.689  43.524  1.00 73.77  ? 138  LEU B CA  1 
ATOM   4315 C C   . LEU B 1 43  ? 25.907  65.536  43.119  1.00 74.49  ? 138  LEU B C   1 
ATOM   4316 O O   . LEU B 1 43  ? 26.244  64.757  42.224  1.00 74.61  ? 138  LEU B O   1 
ATOM   4317 C CB  . LEU B 1 43  ? 26.937  67.693  42.379  1.00 71.46  ? 138  LEU B CB  1 
ATOM   4318 C CG  . LEU B 1 43  ? 25.662  68.477  42.085  1.00 69.83  ? 138  LEU B CG  1 
ATOM   4319 C CD1 . LEU B 1 43  ? 25.195  69.230  43.333  1.00 67.04  ? 138  LEU B CD1 1 
ATOM   4320 C CD2 . LEU B 1 43  ? 25.876  69.423  40.914  1.00 64.30  ? 138  LEU B CD2 1 
ATOM   4321 N N   . PHE B 1 44  ? 24.750  65.444  43.771  1.00 70.81  ? 139  PHE B N   1 
ATOM   4322 C CA  . PHE B 1 44  ? 23.751  64.421  43.506  1.00 71.46  ? 139  PHE B CA  1 
ATOM   4323 C C   . PHE B 1 44  ? 22.574  65.003  42.733  1.00 68.93  ? 139  PHE B C   1 
ATOM   4324 O O   . PHE B 1 44  ? 22.239  66.183  42.878  1.00 69.52  ? 139  PHE B O   1 
ATOM   4325 C CB  . PHE B 1 44  ? 23.225  63.817  44.811  1.00 72.66  ? 139  PHE B CB  1 
ATOM   4326 C CG  . PHE B 1 44  ? 24.181  62.885  45.480  1.00 77.78  ? 139  PHE B CG  1 
ATOM   4327 C CD1 . PHE B 1 44  ? 24.129  61.524  45.228  1.00 80.75  ? 139  PHE B CD1 1 
ATOM   4328 C CD2 . PHE B 1 44  ? 25.123  63.365  46.375  1.00 79.56  ? 139  PHE B CD2 1 
ATOM   4329 C CE1 . PHE B 1 44  ? 25.007  60.652  45.850  1.00 84.14  ? 139  PHE B CE1 1 
ATOM   4330 C CE2 . PHE B 1 44  ? 26.007  62.503  47.004  1.00 84.03  ? 139  PHE B CE2 1 
ATOM   4331 C CZ  . PHE B 1 44  ? 25.947  61.142  46.741  1.00 87.05  ? 139  PHE B CZ  1 
ATOM   4332 N N   . ASN B 1 45  ? 21.932  64.163  41.929  1.00 65.99  ? 140  ASN B N   1 
ATOM   4333 C CA  . ASN B 1 45  ? 20.647  64.514  41.345  1.00 66.60  ? 140  ASN B CA  1 
ATOM   4334 C C   . ASN B 1 45  ? 19.548  63.678  41.988  1.00 66.04  ? 140  ASN B C   1 
ATOM   4335 O O   . ASN B 1 45  ? 19.806  62.644  42.611  1.00 66.65  ? 140  ASN B O   1 
ATOM   4336 C CB  . ASN B 1 45  ? 20.642  64.340  39.818  1.00 64.98  ? 140  ASN B CB  1 
ATOM   4337 C CG  . ASN B 1 45  ? 20.804  62.893  39.382  1.00 66.85  ? 140  ASN B CG  1 
ATOM   4338 O OD1 . ASN B 1 45  ? 19.979  62.036  39.700  1.00 65.06  ? 140  ASN B OD1 1 
ATOM   4339 N ND2 . ASN B 1 45  ? 21.858  62.623  38.616  1.00 68.67  ? 140  ASN B ND2 1 
ATOM   4340 N N   . LEU B 1 46  ? 18.303  64.137  41.817  1.00 65.49  ? 141  LEU B N   1 
ATOM   4341 C CA  . LEU B 1 46  ? 17.173  63.503  42.490  1.00 64.38  ? 141  LEU B CA  1 
ATOM   4342 C C   . LEU B 1 46  ? 16.905  62.090  41.984  1.00 64.23  ? 141  LEU B C   1 
ATOM   4343 O O   . LEU B 1 46  ? 16.298  61.292  42.700  1.00 64.18  ? 141  LEU B O   1 
ATOM   4344 C CB  . LEU B 1 46  ? 15.919  64.357  42.326  1.00 60.65  ? 141  LEU B CB  1 
ATOM   4345 C CG  . LEU B 1 46  ? 16.037  65.743  42.939  1.00 63.00  ? 141  LEU B CG  1 
ATOM   4346 C CD1 . LEU B 1 46  ? 14.787  66.539  42.664  1.00 64.08  ? 141  LEU B CD1 1 
ATOM   4347 C CD2 . LEU B 1 46  ? 16.279  65.621  44.425  1.00 63.67  ? 141  LEU B CD2 1 
ATOM   4348 N N   . GLU B 1 47  ? 17.306  61.767  40.754  1.00 63.64  ? 142  GLU B N   1 
ATOM   4349 C CA  . GLU B 1 47  ? 17.135  60.400  40.262  1.00 64.02  ? 142  GLU B CA  1 
ATOM   4350 C C   . GLU B 1 47  ? 18.028  59.433  41.036  1.00 65.81  ? 142  GLU B C   1 
ATOM   4351 O O   . GLU B 1 47  ? 17.581  58.359  41.462  1.00 69.20  ? 142  GLU B O   1 
ATOM   4352 C CB  . GLU B 1 47  ? 17.424  60.347  38.754  1.00 62.21  ? 142  GLU B CB  1 
ATOM   4353 C CG  . GLU B 1 47  ? 17.486  58.938  38.145  1.00 63.71  ? 142  GLU B CG  1 
ATOM   4354 C CD  . GLU B 1 47  ? 17.542  58.936  36.609  1.00 62.10  ? 142  GLU B CD  1 
ATOM   4355 O OE1 . GLU B 1 47  ? 16.792  58.162  35.980  1.00 67.86  ? 142  GLU B OE1 1 
ATOM   4356 O OE2 . GLU B 1 47  ? 18.320  59.712  36.018  1.00 59.81  ? 142  GLU B OE2 1 
ATOM   4357 N N   . GLU B 1 48  ? 19.295  59.808  41.243  1.00 62.95  ? 143  GLU B N   1 
ATOM   4358 C CA  . GLU B 1 48  ? 20.197  58.989  42.044  1.00 66.06  ? 143  GLU B CA  1 
ATOM   4359 C C   . GLU B 1 48  ? 19.669  58.813  43.458  1.00 71.55  ? 143  GLU B C   1 
ATOM   4360 O O   . GLU B 1 48  ? 19.720  57.711  44.016  1.00 74.52  ? 143  GLU B O   1 
ATOM   4361 C CB  . GLU B 1 48  ? 21.589  59.621  42.079  1.00 69.77  ? 143  GLU B CB  1 
ATOM   4362 C CG  . GLU B 1 48  ? 22.222  59.847  40.710  1.00 70.90  ? 143  GLU B CG  1 
ATOM   4363 C CD  . GLU B 1 48  ? 23.596  60.485  40.811  1.00 73.46  ? 143  GLU B CD  1 
ATOM   4364 O OE1 . GLU B 1 48  ? 23.910  61.030  41.892  1.00 73.31  ? 143  GLU B OE1 1 
ATOM   4365 O OE2 . GLU B 1 48  ? 24.364  60.434  39.822  1.00 73.99  ? 143  GLU B OE2 1 
ATOM   4366 N N   . ILE B 1 49  ? 19.165  59.897  44.055  1.00 68.74  ? 144  ILE B N   1 
ATOM   4367 C CA  . ILE B 1 49  ? 18.623  59.832  45.407  1.00 71.17  ? 144  ILE B CA  1 
ATOM   4368 C C   . ILE B 1 49  ? 17.423  58.894  45.451  1.00 74.64  ? 144  ILE B C   1 
ATOM   4369 O O   . ILE B 1 49  ? 17.319  58.031  46.336  1.00 76.63  ? 144  ILE B O   1 
ATOM   4370 C CB  . ILE B 1 49  ? 18.261  61.243  45.901  1.00 68.11  ? 144  ILE B CB  1 
ATOM   4371 C CG1 . ILE B 1 49  ? 19.532  62.075  46.085  1.00 68.62  ? 144  ILE B CG1 1 
ATOM   4372 C CG2 . ILE B 1 49  ? 17.448  61.173  47.186  1.00 71.78  ? 144  ILE B CG2 1 
ATOM   4373 C CD1 . ILE B 1 49  ? 19.268  63.522  46.418  1.00 68.94  ? 144  ILE B CD1 1 
ATOM   4374 N N   . TYR B 1 50  ? 16.494  59.053  44.500  1.00 70.36  ? 145  TYR B N   1 
ATOM   4375 C CA  . TYR B 1 50  ? 15.326  58.182  44.461  1.00 71.70  ? 145  TYR B CA  1 
ATOM   4376 C C   . TYR B 1 50  ? 15.749  56.724  44.393  1.00 76.45  ? 145  TYR B C   1 
ATOM   4377 O O   . TYR B 1 50  ? 15.263  55.887  45.160  1.00 74.90  ? 145  TYR B O   1 
ATOM   4378 C CB  . TYR B 1 50  ? 14.428  58.529  43.269  1.00 70.40  ? 145  TYR B CB  1 
ATOM   4379 C CG  . TYR B 1 50  ? 13.254  57.578  43.124  1.00 69.54  ? 145  TYR B CG  1 
ATOM   4380 C CD1 . TYR B 1 50  ? 12.093  57.764  43.861  1.00 69.16  ? 145  TYR B CD1 1 
ATOM   4381 C CD2 . TYR B 1 50  ? 13.319  56.484  42.271  1.00 73.01  ? 145  TYR B CD2 1 
ATOM   4382 C CE1 . TYR B 1 50  ? 11.029  56.897  43.752  1.00 70.10  ? 145  TYR B CE1 1 
ATOM   4383 C CE2 . TYR B 1 50  ? 12.252  55.606  42.152  1.00 73.50  ? 145  TYR B CE2 1 
ATOM   4384 C CZ  . TYR B 1 50  ? 11.115  55.817  42.901  1.00 71.32  ? 145  TYR B CZ  1 
ATOM   4385 O OH  . TYR B 1 50  ? 10.054  54.955  42.791  1.00 75.31  ? 145  TYR B OH  1 
ATOM   4386 N N   . HIS B 1 51  ? 16.680  56.405  43.492  1.00 71.27  ? 146  HIS B N   1 
ATOM   4387 C CA  . HIS B 1 51  ? 17.042  55.006  43.312  1.00 74.35  ? 146  HIS B CA  1 
ATOM   4388 C C   . HIS B 1 51  ? 17.856  54.453  44.479  1.00 78.08  ? 146  HIS B C   1 
ATOM   4389 O O   . HIS B 1 51  ? 17.758  53.259  44.777  1.00 82.30  ? 146  HIS B O   1 
ATOM   4390 C CB  . HIS B 1 51  ? 17.772  54.829  41.991  1.00 74.55  ? 146  HIS B CB  1 
ATOM   4391 C CG  . HIS B 1 51  ? 16.855  54.899  40.813  1.00 75.33  ? 146  HIS B CG  1 
ATOM   4392 N ND1 . HIS B 1 51  ? 15.743  54.093  40.696  1.00 76.84  ? 146  HIS B ND1 1 
ATOM   4393 C CD2 . HIS B 1 51  ? 16.857  55.700  39.722  1.00 74.42  ? 146  HIS B CD2 1 
ATOM   4394 C CE1 . HIS B 1 51  ? 15.109  54.382  39.573  1.00 78.32  ? 146  HIS B CE1 1 
ATOM   4395 N NE2 . HIS B 1 51  ? 15.764  55.354  38.964  1.00 74.80  ? 146  HIS B NE2 1 
ATOM   4396 N N   . SER B 1 52  ? 18.645  55.284  45.166  1.00 75.55  ? 147  SER B N   1 
ATOM   4397 C CA  . SER B 1 52  ? 19.369  54.775  46.329  1.00 79.67  ? 147  SER B CA  1 
ATOM   4398 C C   . SER B 1 52  ? 18.450  54.585  47.525  1.00 80.28  ? 147  SER B C   1 
ATOM   4399 O O   . SER B 1 52  ? 18.650  53.656  48.313  1.00 83.35  ? 147  SER B O   1 
ATOM   4400 C CB  . SER B 1 52  ? 20.520  55.707  46.702  1.00 79.79  ? 147  SER B CB  1 
ATOM   4401 O OG  . SER B 1 52  ? 21.623  55.517  45.834  1.00 80.82  ? 147  SER B OG  1 
ATOM   4402 N N   . LEU B 1 53  ? 17.441  55.442  47.680  1.00 80.73  ? 148  LEU B N   1 
ATOM   4403 C CA  . LEU B 1 53  ? 16.557  55.362  48.834  1.00 80.18  ? 148  LEU B CA  1 
ATOM   4404 C C   . LEU B 1 53  ? 15.342  54.469  48.619  1.00 83.67  ? 148  LEU B C   1 
ATOM   4405 O O   . LEU B 1 53  ? 14.800  53.950  49.602  1.00 87.98  ? 148  LEU B O   1 
ATOM   4406 C CB  . LEU B 1 53  ? 16.082  56.762  49.240  1.00 84.69  ? 148  LEU B CB  1 
ATOM   4407 C CG  . LEU B 1 53  ? 17.160  57.788  49.610  1.00 83.35  ? 148  LEU B CG  1 
ATOM   4408 C CD1 . LEU B 1 53  ? 16.528  59.072  50.133  1.00 86.89  ? 148  LEU B CD1 1 
ATOM   4409 C CD2 . LEU B 1 53  ? 18.145  57.226  50.624  1.00 85.05  ? 148  LEU B CD2 1 
ATOM   4410 N N   . MET B 1 54  ? 14.894  54.277  47.380  1.00 85.50  ? 149  MET B N   1 
ATOM   4411 C CA  . MET B 1 54  ? 13.684  53.493  47.131  1.00 87.06  ? 149  MET B CA  1 
ATOM   4412 C C   . MET B 1 54  ? 13.978  52.270  46.263  1.00 89.70  ? 149  MET B C   1 
ATOM   4413 O O   . MET B 1 54  ? 13.935  51.135  46.740  1.00 97.18  ? 149  MET B O   1 
ATOM   4414 C CB  . MET B 1 54  ? 12.603  54.361  46.467  1.00 85.04  ? 149  MET B CB  1 
ATOM   4415 C CG  . MET B 1 54  ? 12.606  55.849  46.868  1.00 82.66  ? 149  MET B CG  1 
ATOM   4416 S SD  . MET B 1 54  ? 12.376  56.233  48.627  1.00 98.35  ? 149  MET B SD  1 
ATOM   4417 C CE  . MET B 1 54  ? 10.695  56.837  48.667  1.00 84.12  ? 149  MET B CE  1 
ATOM   4418 N N   . HIS B 1 84  ? 23.662  55.421  53.200  1.00 102.89 ? 179  HIS B N   1 
ATOM   4419 C CA  . HIS B 1 84  ? 24.882  56.007  52.657  1.00 105.70 ? 179  HIS B CA  1 
ATOM   4420 C C   . HIS B 1 84  ? 24.739  57.521  52.530  1.00 106.79 ? 179  HIS B C   1 
ATOM   4421 O O   . HIS B 1 84  ? 25.529  58.283  53.094  1.00 109.72 ? 179  HIS B O   1 
ATOM   4422 C CB  . HIS B 1 84  ? 25.212  55.384  51.299  1.00 109.61 ? 179  HIS B CB  1 
ATOM   4423 N N   . LEU B 1 85  ? 23.714  57.948  51.784  1.00 105.21 ? 180  LEU B N   1 
ATOM   4424 C CA  . LEU B 1 85  ? 23.351  59.358  51.649  1.00 98.84  ? 180  LEU B CA  1 
ATOM   4425 C C   . LEU B 1 85  ? 22.895  59.981  52.961  1.00 100.66 ? 180  LEU B C   1 
ATOM   4426 O O   . LEU B 1 85  ? 22.699  61.199  53.014  1.00 98.67  ? 180  LEU B O   1 
ATOM   4427 C CB  . LEU B 1 85  ? 22.224  59.507  50.618  1.00 95.52  ? 180  LEU B CB  1 
ATOM   4428 C CG  . LEU B 1 85  ? 22.494  59.341  49.121  1.00 91.34  ? 180  LEU B CG  1 
ATOM   4429 C CD1 . LEU B 1 85  ? 21.284  58.750  48.418  1.00 85.37  ? 180  LEU B CD1 1 
ATOM   4430 C CD2 . LEU B 1 85  ? 22.832  60.685  48.524  1.00 89.28  ? 180  LEU B CD2 1 
ATOM   4431 N N   . LEU B 1 86  ? 22.715  59.184  54.013  1.00 102.57 ? 181  LEU B N   1 
ATOM   4432 C CA  . LEU B 1 86  ? 22.074  59.640  55.236  1.00 103.59 ? 181  LEU B CA  1 
ATOM   4433 C C   . LEU B 1 86  ? 23.040  59.803  56.398  1.00 104.31 ? 181  LEU B C   1 
ATOM   4434 O O   . LEU B 1 86  ? 22.616  60.215  57.483  1.00 105.85 ? 181  LEU B O   1 
ATOM   4435 C CB  . LEU B 1 86  ? 20.955  58.669  55.624  1.00 101.87 ? 181  LEU B CB  1 
ATOM   4436 C CG  . LEU B 1 86  ? 19.882  58.476  54.548  1.00 100.65 ? 181  LEU B CG  1 
ATOM   4437 C CD1 . LEU B 1 86  ? 19.398  57.033  54.496  1.00 97.74  ? 181  LEU B CD1 1 
ATOM   4438 C CD2 . LEU B 1 86  ? 18.719  59.424  54.795  1.00 99.64  ? 181  LEU B CD2 1 
ATOM   4439 N N   . GLN B 1 87  ? 24.326  59.497  56.206  1.00 107.35 ? 182  GLN B N   1 
ATOM   4440 C CA  . GLN B 1 87  ? 25.289  59.637  57.295  1.00 106.71 ? 182  GLN B CA  1 
ATOM   4441 C C   . GLN B 1 87  ? 25.659  61.093  57.549  1.00 106.88 ? 182  GLN B C   1 
ATOM   4442 O O   . GLN B 1 87  ? 25.987  61.452  58.685  1.00 105.97 ? 182  GLN B O   1 
ATOM   4443 C CB  . GLN B 1 87  ? 26.550  58.821  56.997  1.00 106.63 ? 182  GLN B CB  1 
ATOM   4444 N N   . SER B 1 88  ? 25.611  61.943  56.523  1.00 107.16 ? 183  SER B N   1 
ATOM   4445 C CA  . SER B 1 88  ? 26.019  63.334  56.667  1.00 106.87 ? 183  SER B CA  1 
ATOM   4446 C C   . SER B 1 88  ? 25.274  64.200  55.655  1.00 102.88 ? 183  SER B C   1 
ATOM   4447 O O   . SER B 1 88  ? 24.376  63.737  54.944  1.00 100.44 ? 183  SER B O   1 
ATOM   4448 C CB  . SER B 1 88  ? 27.535  63.479  56.496  1.00 109.09 ? 183  SER B CB  1 
ATOM   4449 O OG  . SER B 1 88  ? 27.932  64.828  56.666  1.00 110.48 ? 183  SER B OG  1 
ATOM   4450 N N   . ASP B 1 89  ? 25.657  65.476  55.605  1.00 100.62 ? 184  ASP B N   1 
ATOM   4451 C CA  . ASP B 1 89  ? 25.102  66.405  54.631  1.00 96.01  ? 184  ASP B CA  1 
ATOM   4452 C C   . ASP B 1 89  ? 25.542  66.020  53.224  1.00 91.82  ? 184  ASP B C   1 
ATOM   4453 O O   . ASP B 1 89  ? 26.613  65.445  53.021  1.00 92.82  ? 184  ASP B O   1 
ATOM   4454 C CB  . ASP B 1 89  ? 25.544  67.840  54.945  1.00 96.49  ? 184  ASP B CB  1 
ATOM   4455 C CG  . ASP B 1 89  ? 25.065  68.323  56.309  1.00 98.29  ? 184  ASP B CG  1 
ATOM   4456 O OD1 . ASP B 1 89  ? 23.963  67.906  56.733  1.00 97.96  ? 184  ASP B OD1 1 
ATOM   4457 O OD2 . ASP B 1 89  ? 25.787  69.120  56.954  1.00 97.82  ? 184  ASP B OD2 1 
ATOM   4458 N N   . ILE B 1 90  ? 24.693  66.327  52.243  1.00 89.20  ? 185  ILE B N   1 
ATOM   4459 C CA  . ILE B 1 90  ? 24.982  66.069  50.836  1.00 83.71  ? 185  ILE B CA  1 
ATOM   4460 C C   . ILE B 1 90  ? 24.581  67.292  50.024  1.00 80.83  ? 185  ILE B C   1 
ATOM   4461 O O   . ILE B 1 90  ? 23.846  68.167  50.490  1.00 81.44  ? 185  ILE B O   1 
ATOM   4462 C CB  . ILE B 1 90  ? 24.254  64.822  50.287  1.00 84.29  ? 185  ILE B CB  1 
ATOM   4463 C CG1 . ILE B 1 90  ? 22.779  65.145  50.031  1.00 82.73  ? 185  ILE B CG1 1 
ATOM   4464 C CG2 . ILE B 1 90  ? 24.391  63.640  51.234  1.00 86.69  ? 185  ILE B CG2 1 
ATOM   4465 C CD1 . ILE B 1 90  ? 21.956  63.962  49.599  1.00 83.13  ? 185  ILE B CD1 1 
ATOM   4466 N N   . TRP B 1 91  ? 25.078  67.341  48.792  1.00 78.57  ? 186  TRP B N   1 
ATOM   4467 C CA  . TRP B 1 91  ? 24.706  68.361  47.824  1.00 74.54  ? 186  TRP B CA  1 
ATOM   4468 C C   . TRP B 1 91  ? 23.781  67.758  46.776  1.00 73.64  ? 186  TRP B C   1 
ATOM   4469 O O   . TRP B 1 91  ? 23.996  66.633  46.313  1.00 73.36  ? 186  TRP B O   1 
ATOM   4470 C CB  . TRP B 1 91  ? 25.937  68.959  47.139  1.00 75.16  ? 186  TRP B CB  1 
ATOM   4471 C CG  . TRP B 1 91  ? 26.742  69.872  48.011  1.00 78.56  ? 186  TRP B CG  1 
ATOM   4472 C CD1 . TRP B 1 91  ? 27.720  69.511  48.887  1.00 81.90  ? 186  TRP B CD1 1 
ATOM   4473 C CD2 . TRP B 1 91  ? 26.651  71.302  48.078  1.00 80.62  ? 186  TRP B CD2 1 
ATOM   4474 N NE1 . TRP B 1 91  ? 28.243  70.627  49.503  1.00 85.55  ? 186  TRP B NE1 1 
ATOM   4475 C CE2 . TRP B 1 91  ? 27.603  71.739  49.023  1.00 84.16  ? 186  TRP B CE2 1 
ATOM   4476 C CE3 . TRP B 1 91  ? 25.856  72.256  47.434  1.00 79.32  ? 186  TRP B CE3 1 
ATOM   4477 C CZ2 . TRP B 1 91  ? 27.781  73.085  49.337  1.00 87.67  ? 186  TRP B CZ2 1 
ATOM   4478 C CZ3 . TRP B 1 91  ? 26.035  73.594  47.748  1.00 78.43  ? 186  TRP B CZ3 1 
ATOM   4479 C CH2 . TRP B 1 91  ? 26.989  73.995  48.691  1.00 83.13  ? 186  TRP B CH2 1 
ATOM   4480 N N   . VAL B 1 92  ? 22.755  68.515  46.408  1.00 71.38  ? 187  VAL B N   1 
ATOM   4481 C CA  . VAL B 1 92  ? 21.811  68.111  45.374  1.00 68.81  ? 187  VAL B CA  1 
ATOM   4482 C C   . VAL B 1 92  ? 21.430  69.338  44.555  1.00 68.94  ? 187  VAL B C   1 
ATOM   4483 O O   . VAL B 1 92  ? 21.250  70.434  45.098  1.00 67.40  ? 187  VAL B O   1 
ATOM   4484 C CB  . VAL B 1 92  ? 20.564  67.426  45.976  1.00 67.38  ? 187  VAL B CB  1 
ATOM   4485 C CG1 . VAL B 1 92  ? 19.898  68.324  46.995  1.00 68.54  ? 187  VAL B CG1 1 
ATOM   4486 C CG2 . VAL B 1 92  ? 19.582  67.029  44.875  1.00 67.59  ? 187  VAL B CG2 1 
ATOM   4487 N N   . ARG B 1 93  ? 21.324  69.155  43.244  1.00 65.42  ? 188  ARG B N   1 
ATOM   4488 C CA  . ARG B 1 93  ? 20.931  70.205  42.319  1.00 63.12  ? 188  ARG B CA  1 
ATOM   4489 C C   . ARG B 1 93  ? 19.530  69.923  41.795  1.00 64.35  ? 188  ARG B C   1 
ATOM   4490 O O   . ARG B 1 93  ? 19.155  68.763  41.596  1.00 65.61  ? 188  ARG B O   1 
ATOM   4491 C CB  . ARG B 1 93  ? 21.921  70.296  41.154  1.00 61.97  ? 188  ARG B CB  1 
ATOM   4492 C CG  . ARG B 1 93  ? 21.495  71.243  40.044  1.00 60.43  ? 188  ARG B CG  1 
ATOM   4493 C CD  . ARG B 1 93  ? 22.586  71.385  38.998  1.00 59.52  ? 188  ARG B CD  1 
ATOM   4494 N NE  . ARG B 1 93  ? 23.784  72.003  39.553  1.00 59.91  ? 188  ARG B NE  1 
ATOM   4495 C CZ  . ARG B 1 93  ? 24.945  72.078  38.916  1.00 62.09  ? 188  ARG B CZ  1 
ATOM   4496 N NH1 . ARG B 1 93  ? 25.102  71.574  37.700  1.00 59.70  ? 188  ARG B NH1 1 
ATOM   4497 N NH2 . ARG B 1 93  ? 25.972  72.676  39.512  1.00 64.22  ? 188  ARG B NH2 1 
ATOM   4498 N N   . GLY B 1 94  ? 18.756  70.979  41.571  1.00 62.22  ? 189  GLY B N   1 
ATOM   4499 C CA  . GLY B 1 94  ? 17.435  70.756  41.006  1.00 59.20  ? 189  GLY B CA  1 
ATOM   4500 C C   . GLY B 1 94  ? 16.727  72.046  40.663  1.00 61.51  ? 189  GLY B C   1 
ATOM   4501 O O   . GLY B 1 94  ? 17.216  73.146  40.941  1.00 60.60  ? 189  GLY B O   1 
ATOM   4502 N N   . ARG B 1 95  ? 15.542  71.896  40.062  1.00 59.28  ? 190  ARG B N   1 
ATOM   4503 C CA  . ARG B 1 95  ? 14.704  73.046  39.743  1.00 60.44  ? 190  ARG B CA  1 
ATOM   4504 C C   . ARG B 1 95  ? 13.677  73.266  40.844  1.00 61.30  ? 190  ARG B C   1 
ATOM   4505 O O   . ARG B 1 95  ? 13.152  72.313  41.426  1.00 60.74  ? 190  ARG B O   1 
ATOM   4506 C CB  . ARG B 1 95  ? 13.996  72.876  38.394  1.00 61.12  ? 190  ARG B CB  1 
ATOM   4507 C CG  . ARG B 1 95  ? 14.829  73.375  37.224  1.00 56.86  ? 190  ARG B CG  1 
ATOM   4508 C CD  . ARG B 1 95  ? 14.178  73.184  35.865  1.00 55.27  ? 190  ARG B CD  1 
ATOM   4509 N NE  . ARG B 1 95  ? 14.969  73.866  34.843  1.00 54.50  ? 190  ARG B NE  1 
ATOM   4510 C CZ  . ARG B 1 95  ? 14.961  73.575  33.549  1.00 53.89  ? 190  ARG B CZ  1 
ATOM   4511 N NH1 . ARG B 1 95  ? 14.224  72.590  33.063  1.00 48.99  ? 190  ARG B NH1 1 
ATOM   4512 N NH2 . ARG B 1 95  ? 15.710  74.295  32.721  1.00 52.40  ? 190  ARG B NH2 1 
ATOM   4513 N N   . ILE B 1 96  ? 13.404  74.536  41.137  1.00 62.97  ? 191  ILE B N   1 
ATOM   4514 C CA  . ILE B 1 96  ? 12.397  74.906  42.128  1.00 62.56  ? 191  ILE B CA  1 
ATOM   4515 C C   . ILE B 1 96  ? 11.040  74.768  41.446  1.00 62.84  ? 191  ILE B C   1 
ATOM   4516 O O   . ILE B 1 96  ? 10.648  75.613  40.642  1.00 61.89  ? 191  ILE B O   1 
ATOM   4517 C CB  . ILE B 1 96  ? 12.618  76.318  42.673  1.00 64.23  ? 191  ILE B CB  1 
ATOM   4518 C CG1 . ILE B 1 96  ? 13.995  76.413  43.334  1.00 65.15  ? 191  ILE B CG1 1 
ATOM   4519 C CG2 . ILE B 1 96  ? 11.512  76.687  43.670  1.00 64.94  ? 191  ILE B CG2 1 
ATOM   4520 C CD1 . ILE B 1 96  ? 14.298  77.777  43.948  1.00 64.66  ? 191  ILE B CD1 1 
ATOM   4521 N N   . HIS B 1 97  ? 10.337  73.675  41.743  1.00 64.03  ? 192  HIS B N   1 
ATOM   4522 C CA  . HIS B 1 97  ? 9.028   73.400  41.166  1.00 64.58  ? 192  HIS B CA  1 
ATOM   4523 C C   . HIS B 1 97  ? 7.928   74.127  41.934  1.00 62.67  ? 192  HIS B C   1 
ATOM   4524 O O   . HIS B 1 97  ? 6.946   74.590  41.347  1.00 63.52  ? 192  HIS B O   1 
ATOM   4525 C CB  . HIS B 1 97  ? 8.802   71.884  41.166  1.00 61.48  ? 192  HIS B CB  1 
ATOM   4526 C CG  . HIS B 1 97  ? 7.454   71.458  40.684  1.00 59.77  ? 192  HIS B CG  1 
ATOM   4527 N ND1 . HIS B 1 97  ? 7.174   71.253  39.352  1.00 57.80  ? 192  HIS B ND1 1 
ATOM   4528 C CD2 . HIS B 1 97  ? 6.316   71.162  41.360  1.00 61.73  ? 192  HIS B CD2 1 
ATOM   4529 C CE1 . HIS B 1 97  ? 5.916   70.870  39.223  1.00 60.86  ? 192  HIS B CE1 1 
ATOM   4530 N NE2 . HIS B 1 97  ? 5.372   70.809  40.426  1.00 62.16  ? 192  HIS B NE2 1 
ATOM   4531 N N   . ASP B 1 98  ? 8.077   74.239  43.246  1.00 65.69  ? 193  ASP B N   1 
ATOM   4532 C CA  . ASP B 1 98  ? 7.124   74.965  44.064  1.00 68.20  ? 193  ASP B CA  1 
ATOM   4533 C C   . ASP B 1 98  ? 7.885   75.569  45.228  1.00 72.59  ? 193  ASP B C   1 
ATOM   4534 O O   . ASP B 1 98  ? 8.882   75.006  45.691  1.00 73.38  ? 193  ASP B O   1 
ATOM   4535 C CB  . ASP B 1 98  ? 5.998   74.059  44.573  1.00 70.02  ? 193  ASP B CB  1 
ATOM   4536 C CG  . ASP B 1 98  ? 4.893   74.837  45.248  1.00 76.03  ? 193  ASP B CG  1 
ATOM   4537 O OD1 . ASP B 1 98  ? 4.081   75.456  44.522  1.00 74.44  ? 193  ASP B OD1 1 
ATOM   4538 O OD2 . ASP B 1 98  ? 4.855   74.856  46.502  1.00 78.83  ? 193  ASP B OD2 1 
ATOM   4539 N N   . ILE B 1 99  ? 7.421   76.728  45.686  1.00 73.61  ? 194  ILE B N   1 
ATOM   4540 C CA  . ILE B 1 99  ? 8.052   77.418  46.804  1.00 78.70  ? 194  ILE B CA  1 
ATOM   4541 C C   . ILE B 1 99  ? 6.949   77.991  47.683  1.00 82.52  ? 194  ILE B C   1 
ATOM   4542 O O   . ILE B 1 99  ? 5.997   78.602  47.186  1.00 81.08  ? 194  ILE B O   1 
ATOM   4543 C CB  . ILE B 1 99  ? 9.050   78.501  46.332  1.00 80.78  ? 194  ILE B CB  1 
ATOM   4544 C CG1 . ILE B 1 99  ? 10.021  78.864  47.456  1.00 81.51  ? 194  ILE B CG1 1 
ATOM   4545 C CG2 . ILE B 1 99  ? 8.347   79.756  45.805  1.00 79.80  ? 194  ILE B CG2 1 
ATOM   4546 C CD1 . ILE B 1 99  ? 11.291  79.500  46.940  1.00 78.49  ? 194  ILE B CD1 1 
ATOM   4547 N N   . ARG B 1 100 ? 7.026   77.691  48.971  1.00 87.24  ? 195  ARG B N   1 
ATOM   4548 C CA  . ARG B 1 100 ? 6.014   78.072  49.956  1.00 87.18  ? 195  ARG B CA  1 
ATOM   4549 C C   . ARG B 1 100 ? 6.681   78.703  51.144  1.00 90.81  ? 195  ARG B C   1 
ATOM   4550 O O   . ARG B 1 100 ? 7.528   78.069  51.750  1.00 88.22  ? 195  ARG B O   1 
ATOM   4551 C CB  . ARG B 1 100 ? 5.370   76.799  50.467  1.00 87.40  ? 195  ARG B CB  1 
ATOM   4552 C CG  . ARG B 1 100 ? 3.874   76.822  50.612  1.00 92.39  ? 195  ARG B CG  1 
ATOM   4553 C CD  . ARG B 1 100 ? 3.356   75.396  50.723  1.00 93.31  ? 195  ARG B CD  1 
ATOM   4554 N NE  . ARG B 1 100 ? 4.036   74.611  51.748  1.00 88.88  ? 195  ARG B NE  1 
ATOM   4555 N N   . SER B 1 101 ? 6.311   79.938  51.479  1.00 95.07  ? 196  SER B N   1 
ATOM   4556 C CA  . SER B 1 101 ? 6.923   80.624  52.617  1.00 97.04  ? 196  SER B CA  1 
ATOM   4557 C C   . SER B 1 101 ? 6.012   81.316  53.636  1.00 100.99 ? 196  SER B C   1 
ATOM   4558 O O   . SER B 1 101 ? 5.151   82.096  53.271  1.00 104.58 ? 196  SER B O   1 
ATOM   4559 C CB  . SER B 1 101 ? 7.904   81.662  52.098  1.00 94.10  ? 196  SER B CB  1 
ATOM   4560 O OG  . SER B 1 101 ? 8.845   81.977  53.089  1.00 95.23  ? 196  SER B OG  1 
ATOM   4561 N N   . LYS B 1 102 ? 6.195   81.012  54.912  1.00 103.18 ? 197  LYS B N   1 
ATOM   4562 C CA  . LYS B 1 102 ? 5.461   81.707  55.983  1.00 106.90 ? 197  LYS B CA  1 
ATOM   4563 C C   . LYS B 1 102 ? 6.271   81.732  57.278  1.00 106.43 ? 197  LYS B C   1 
ATOM   4564 O O   . LYS B 1 102 ? 6.759   80.709  57.739  1.00 104.93 ? 197  LYS B O   1 
ATOM   4565 C CB  . LYS B 1 102 ? 4.069   81.122  56.214  1.00 102.65 ? 197  LYS B CB  1 
ATOM   4566 N N   . GLY B 1 103 ? 6.364   82.895  57.898  1.00 114.77 ? 198  GLY B N   1 
ATOM   4567 C CA  . GLY B 1 103 ? 7.115   83.000  59.130  1.00 114.04 ? 198  GLY B CA  1 
ATOM   4568 C C   . GLY B 1 103 ? 8.569   82.630  58.980  1.00 114.70 ? 198  GLY B C   1 
ATOM   4569 O O   . GLY B 1 103 ? 9.268   83.207  58.189  1.00 118.09 ? 198  GLY B O   1 
ATOM   4570 N N   . SER B 1 104 ? 9.030   81.700  59.795  1.00 109.04 ? 199  SER B N   1 
ATOM   4571 C CA  . SER B 1 104 ? 10.413  81.269  59.767  1.00 107.51 ? 199  SER B CA  1 
ATOM   4572 C C   . SER B 1 104 ? 10.631  79.934  59.036  1.00 103.91 ? 199  SER B C   1 
ATOM   4573 O O   . SER B 1 104 ? 11.713  79.352  59.093  1.00 99.72  ? 199  SER B O   1 
ATOM   4574 C CB  . SER B 1 104 ? 10.942  81.183  61.186  1.00 107.33 ? 199  SER B CB  1 
ATOM   4575 O OG  . SER B 1 104 ? 10.226  80.208  61.912  1.00 108.79 ? 199  SER B OG  1 
ATOM   4576 N N   . LEU B 1 105 ? 9.594   79.434  58.383  1.00 101.88 ? 200  LEU B N   1 
ATOM   4577 C CA  . LEU B 1 105 ? 9.703   78.177  57.650  1.00 100.42 ? 200  LEU B CA  1 
ATOM   4578 C C   . LEU B 1 105 ? 9.456   78.355  56.142  1.00 94.69  ? 200  LEU B C   1 
ATOM   4579 O O   . LEU B 1 105 ? 8.590   79.120  55.726  1.00 95.68  ? 200  LEU B O   1 
ATOM   4580 C CB  . LEU B 1 105 ? 8.790   77.111  58.255  1.00 97.11  ? 200  LEU B CB  1 
ATOM   4581 N N   . ALA B 1 106 ? 10.237  77.646  55.337  1.00 89.95  ? 201  ALA B N   1 
ATOM   4582 C CA  . ALA B 1 106 ? 10.151  77.724  53.883  1.00 88.69  ? 201  ALA B CA  1 
ATOM   4583 C C   . ALA B 1 106 ? 10.196  76.322  53.289  1.00 84.98  ? 201  ALA B C   1 
ATOM   4584 O O   . ALA B 1 106 ? 11.037  75.503  53.673  1.00 83.30  ? 201  ALA B O   1 
ATOM   4585 C CB  . ALA B 1 106 ? 11.289  78.571  53.301  1.00 84.33  ? 201  ALA B CB  1 
ATOM   4586 N N   . PHE B 1 107 ? 9.294   76.046  52.347  1.00 82.73  ? 202  PHE B N   1 
ATOM   4587 C CA  . PHE B 1 107 ? 9.192   74.728  51.731  1.00 81.66  ? 202  PHE B CA  1 
ATOM   4588 C C   . PHE B 1 107 ? 9.445   74.853  50.234  1.00 79.66  ? 202  PHE B C   1 
ATOM   4589 O O   . PHE B 1 107 ? 8.743   75.594  49.535  1.00 78.66  ? 202  PHE B O   1 
ATOM   4590 C CB  . PHE B 1 107 ? 7.825   74.095  52.008  1.00 83.78  ? 202  PHE B CB  1 
ATOM   4591 C CG  . PHE B 1 107 ? 7.440   74.100  53.468  1.00 84.75  ? 202  PHE B CG  1 
ATOM   4592 C CD1 . PHE B 1 107 ? 6.738   75.166  54.010  1.00 84.50  ? 202  PHE B CD1 1 
ATOM   4593 C CD2 . PHE B 1 107 ? 7.795   73.048  54.296  1.00 80.84  ? 202  PHE B CD2 1 
ATOM   4594 C CE1 . PHE B 1 107 ? 6.390   75.182  55.354  1.00 88.02  ? 202  PHE B CE1 1 
ATOM   4595 C CE2 . PHE B 1 107 ? 7.455   73.049  55.628  1.00 83.77  ? 202  PHE B CE2 1 
ATOM   4596 C CZ  . PHE B 1 107 ? 6.749   74.122  56.167  1.00 88.21  ? 202  PHE B CZ  1 
ATOM   4597 N N   . ILE B 1 108 ? 10.451  74.136  49.749  1.00 74.99  ? 203  ILE B N   1 
ATOM   4598 C CA  . ILE B 1 108 ? 10.783  74.073  48.334  1.00 72.93  ? 203  ILE B CA  1 
ATOM   4599 C C   . ILE B 1 108 ? 10.520  72.654  47.864  1.00 72.83  ? 203  ILE B C   1 
ATOM   4600 O O   . ILE B 1 108 ? 10.971  71.696  48.495  1.00 73.52  ? 203  ILE B O   1 
ATOM   4601 C CB  . ILE B 1 108 ? 12.252  74.459  48.091  1.00 74.29  ? 203  ILE B CB  1 
ATOM   4602 C CG1 . ILE B 1 108 ? 12.430  75.977  48.141  1.00 74.88  ? 203  ILE B CG1 1 
ATOM   4603 C CG2 . ILE B 1 108 ? 12.761  73.859  46.785  1.00 72.27  ? 203  ILE B CG2 1 
ATOM   4604 C CD1 . ILE B 1 108 ? 13.874  76.405  48.080  1.00 74.88  ? 203  ILE B CD1 1 
ATOM   4605 N N   . ILE B 1 109 ? 9.792   72.503  46.771  1.00 71.23  ? 204  ILE B N   1 
ATOM   4606 C CA  . ILE B 1 109 ? 9.716   71.213  46.106  1.00 68.66  ? 204  ILE B CA  1 
ATOM   4607 C C   . ILE B 1 109 ? 10.714  71.251  44.961  1.00 67.32  ? 204  ILE B C   1 
ATOM   4608 O O   . ILE B 1 109 ? 10.640  72.121  44.089  1.00 66.03  ? 204  ILE B O   1 
ATOM   4609 C CB  . ILE B 1 109 ? 8.288   70.891  45.648  1.00 68.43  ? 204  ILE B CB  1 
ATOM   4610 C CG1 . ILE B 1 109 ? 7.447   70.578  46.893  1.00 69.66  ? 204  ILE B CG1 1 
ATOM   4611 C CG2 . ILE B 1 109 ? 8.290   69.721  44.683  1.00 65.86  ? 204  ILE B CG2 1 
ATOM   4612 C CD1 . ILE B 1 109 ? 6.044   70.130  46.617  1.00 74.24  ? 204  ILE B CD1 1 
ATOM   4613 N N   . LEU B 1 110 ? 11.709  70.378  45.025  1.00 66.53  ? 205  LEU B N   1 
ATOM   4614 C CA  . LEU B 1 110 ? 12.798  70.333  44.069  1.00 62.75  ? 205  LEU B CA  1 
ATOM   4615 C C   . LEU B 1 110 ? 12.519  69.213  43.081  1.00 63.93  ? 205  LEU B C   1 
ATOM   4616 O O   . LEU B 1 110 ? 12.081  68.128  43.474  1.00 65.04  ? 205  LEU B O   1 
ATOM   4617 C CB  . LEU B 1 110 ? 14.123  70.095  44.788  1.00 63.77  ? 205  LEU B CB  1 
ATOM   4618 C CG  . LEU B 1 110 ? 15.360  70.592  44.064  1.00 65.84  ? 205  LEU B CG  1 
ATOM   4619 C CD1 . LEU B 1 110 ? 15.333  72.114  44.034  1.00 63.72  ? 205  LEU B CD1 1 
ATOM   4620 C CD2 . LEU B 1 110 ? 16.617  70.070  44.749  1.00 66.62  ? 205  LEU B CD2 1 
ATOM   4621 N N   . ARG B 1 111 ? 12.768  69.479  41.802  1.00 61.76  ? 206  ARG B N   1 
ATOM   4622 C CA  . ARG B 1 111 ? 12.342  68.598  40.723  1.00 58.62  ? 206  ARG B CA  1 
ATOM   4623 C C   . ARG B 1 111 ? 13.504  68.301  39.786  1.00 59.61  ? 206  ARG B C   1 
ATOM   4624 O O   . ARG B 1 111 ? 14.361  69.165  39.544  1.00 57.92  ? 206  ARG B O   1 
ATOM   4625 C CB  . ARG B 1 111 ? 11.188  69.223  39.922  1.00 58.84  ? 206  ARG B CB  1 
ATOM   4626 C CG  . ARG B 1 111 ? 10.498  68.270  38.969  1.00 57.66  ? 206  ARG B CG  1 
ATOM   4627 C CD  . ARG B 1 111 ? 9.499   68.981  38.062  1.00 58.62  ? 206  ARG B CD  1 
ATOM   4628 N NE  . ARG B 1 111 ? 10.161  69.669  36.958  1.00 58.14  ? 206  ARG B NE  1 
ATOM   4629 C CZ  . ARG B 1 111 ? 10.297  70.984  36.868  1.00 59.40  ? 206  ARG B CZ  1 
ATOM   4630 N NH1 . ARG B 1 111 ? 9.769   71.797  37.772  1.00 59.91  ? 206  ARG B NH1 1 
ATOM   4631 N NH2 . ARG B 1 111 ? 10.970  71.498  35.840  1.00 56.55  ? 206  ARG B NH2 1 
ATOM   4632 N N   . HIS B 1 112 ? 13.507  67.065  39.277  1.00 57.90  ? 207  HIS B N   1 
ATOM   4633 C CA  . HIS B 1 112 ? 14.449  66.566  38.273  1.00 60.05  ? 207  HIS B CA  1 
ATOM   4634 C C   . HIS B 1 112 ? 13.772  65.393  37.581  1.00 58.97  ? 207  HIS B C   1 
ATOM   4635 O O   . HIS B 1 112 ? 13.420  64.414  38.247  1.00 54.52  ? 207  HIS B O   1 
ATOM   4636 C CB  . HIS B 1 112 ? 15.762  66.128  38.923  1.00 58.85  ? 207  HIS B CB  1 
ATOM   4637 C CG  . HIS B 1 112 ? 16.790  65.626  37.955  1.00 60.52  ? 207  HIS B CG  1 
ATOM   4638 N ND1 . HIS B 1 112 ? 17.398  66.442  37.024  1.00 62.26  ? 207  HIS B ND1 1 
ATOM   4639 C CD2 . HIS B 1 112 ? 17.340  64.398  37.794  1.00 60.77  ? 207  HIS B CD2 1 
ATOM   4640 C CE1 . HIS B 1 112 ? 18.265  65.734  36.322  1.00 58.76  ? 207  HIS B CE1 1 
ATOM   4641 N NE2 . HIS B 1 112 ? 18.252  64.493  36.772  1.00 59.13  ? 207  HIS B NE2 1 
ATOM   4642 N N   . LYS B 1 113 ? 13.562  65.497  36.266  1.00 57.42  ? 208  LYS B N   1 
ATOM   4643 C CA  . LYS B 1 113 ? 12.872  64.469  35.476  1.00 57.66  ? 208  LYS B CA  1 
ATOM   4644 C C   . LYS B 1 113 ? 11.502  64.233  36.104  1.00 58.56  ? 208  LYS B C   1 
ATOM   4645 O O   . LYS B 1 113 ? 10.738  65.201  36.257  1.00 58.11  ? 208  LYS B O   1 
ATOM   4646 C CB  . LYS B 1 113 ? 13.777  63.240  35.367  1.00 56.01  ? 208  LYS B CB  1 
ATOM   4647 C CG  . LYS B 1 113 ? 15.095  63.489  34.651  1.00 55.90  ? 208  LYS B CG  1 
ATOM   4648 C CD  . LYS B 1 113 ? 15.981  62.241  34.675  1.00 56.08  ? 208  LYS B CD  1 
ATOM   4649 C CE  . LYS B 1 113 ? 17.145  62.372  33.695  1.00 58.74  ? 208  LYS B CE  1 
ATOM   4650 N NZ  . LYS B 1 113 ? 18.011  61.161  33.657  1.00 55.73  ? 208  LYS B NZ  1 
ATOM   4651 N N   . LEU B 1 114 ? 11.144  63.009  36.490  1.00 56.59  ? 209  LEU B N   1 
ATOM   4652 C CA  . LEU B 1 114 ? 9.858   62.759  37.125  1.00 57.61  ? 209  LEU B CA  1 
ATOM   4653 C C   . LEU B 1 114 ? 9.976   62.614  38.639  1.00 61.22  ? 209  LEU B C   1 
ATOM   4654 O O   . LEU B 1 114 ? 9.033   62.150  39.291  1.00 59.25  ? 209  LEU B O   1 
ATOM   4655 C CB  . LEU B 1 114 ? 9.193   61.526  36.505  1.00 58.91  ? 209  LEU B CB  1 
ATOM   4656 C CG  . LEU B 1 114 ? 9.740   60.119  36.757  1.00 62.44  ? 209  LEU B CG  1 
ATOM   4657 C CD1 . LEU B 1 114 ? 8.665   59.095  36.429  1.00 61.74  ? 209  LEU B CD1 1 
ATOM   4658 C CD2 . LEU B 1 114 ? 10.972  59.845  35.913  1.00 61.25  ? 209  LEU B CD2 1 
ATOM   4659 N N   . TYR B 1 115 ? 11.105  63.021  39.211  1.00 61.31  ? 210  TYR B N   1 
ATOM   4660 C CA  . TYR B 1 115 ? 11.384  62.888  40.634  1.00 61.35  ? 210  TYR B CA  1 
ATOM   4661 C C   . TYR B 1 115 ? 11.296  64.246  41.318  1.00 62.60  ? 210  TYR B C   1 
ATOM   4662 O O   . TYR B 1 115 ? 11.740  65.263  40.770  1.00 62.73  ? 210  TYR B O   1 
ATOM   4663 C CB  . TYR B 1 115 ? 12.776  62.280  40.859  1.00 59.67  ? 210  TYR B CB  1 
ATOM   4664 C CG  . TYR B 1 115 ? 13.028  61.050  40.020  1.00 62.05  ? 210  TYR B CG  1 
ATOM   4665 C CD1 . TYR B 1 115 ? 12.444  59.833  40.349  1.00 64.76  ? 210  TYR B CD1 1 
ATOM   4666 C CD2 . TYR B 1 115 ? 13.833  61.104  38.895  1.00 61.10  ? 210  TYR B CD2 1 
ATOM   4667 C CE1 . TYR B 1 115 ? 12.663  58.703  39.583  1.00 64.49  ? 210  TYR B CE1 1 
ATOM   4668 C CE2 . TYR B 1 115 ? 14.050  59.981  38.117  1.00 61.99  ? 210  TYR B CE2 1 
ATOM   4669 C CZ  . TYR B 1 115 ? 13.467  58.782  38.470  1.00 65.24  ? 210  TYR B CZ  1 
ATOM   4670 O OH  . TYR B 1 115 ? 13.680  57.656  37.705  1.00 71.12  ? 210  TYR B OH  1 
ATOM   4671 N N   . SER B 1 116 ? 10.720  64.265  42.514  1.00 63.48  ? 211  SER B N   1 
ATOM   4672 C CA  . SER B 1 116 ? 10.638  65.494  43.286  1.00 67.54  ? 211  SER B CA  1 
ATOM   4673 C C   . SER B 1 116 ? 10.835  65.174  44.759  1.00 69.77  ? 211  SER B C   1 
ATOM   4674 O O   . SER B 1 116 ? 10.518  64.075  45.223  1.00 72.75  ? 211  SER B O   1 
ATOM   4675 C CB  . SER B 1 116 ? 9.303   66.209  43.078  1.00 66.72  ? 211  SER B CB  1 
ATOM   4676 O OG  . SER B 1 116 ? 8.232   65.390  43.495  1.00 72.20  ? 211  SER B OG  1 
ATOM   4677 N N   . MET B 1 117 ? 11.357  66.158  45.486  1.00 69.68  ? 212  MET B N   1 
ATOM   4678 C CA  . MET B 1 117 ? 11.700  65.999  46.892  1.00 72.17  ? 212  MET B CA  1 
ATOM   4679 C C   . MET B 1 117 ? 11.505  67.331  47.601  1.00 72.54  ? 212  MET B C   1 
ATOM   4680 O O   . MET B 1 117 ? 11.842  68.380  47.049  1.00 72.45  ? 212  MET B O   1 
ATOM   4681 C CB  . MET B 1 117 ? 13.145  65.518  47.048  1.00 71.14  ? 212  MET B CB  1 
ATOM   4682 C CG  . MET B 1 117 ? 13.695  65.698  48.454  1.00 75.65  ? 212  MET B CG  1 
ATOM   4683 S SD  . MET B 1 117 ? 15.238  64.815  48.721  1.00 78.56  ? 212  MET B SD  1 
ATOM   4684 C CE  . MET B 1 117 ? 16.465  66.072  48.371  1.00 72.08  ? 212  MET B CE  1 
ATOM   4685 N N   . GLN B 1 118 ? 10.976  67.290  48.823  1.00 76.04  ? 213  GLN B N   1 
ATOM   4686 C CA  . GLN B 1 118 ? 10.732  68.511  49.587  1.00 72.92  ? 213  GLN B CA  1 
ATOM   4687 C C   . GLN B 1 118 ? 11.954  68.878  50.423  1.00 75.68  ? 213  GLN B C   1 
ATOM   4688 O O   . GLN B 1 118 ? 12.493  68.044  51.155  1.00 81.53  ? 213  GLN B O   1 
ATOM   4689 C CB  . GLN B 1 118 ? 9.508   68.366  50.491  1.00 73.65  ? 213  GLN B CB  1 
ATOM   4690 C CG  . GLN B 1 118 ? 9.374   69.531  51.469  1.00 79.53  ? 213  GLN B CG  1 
ATOM   4691 C CD  . GLN B 1 118 ? 8.085   69.520  52.270  1.00 83.02  ? 213  GLN B CD  1 
ATOM   4692 O OE1 . GLN B 1 118 ? 7.118   70.199  51.918  1.00 81.13  ? 213  GLN B OE1 1 
ATOM   4693 N NE2 . GLN B 1 118 ? 8.072   68.762  53.362  1.00 80.68  ? 213  GLN B NE2 1 
ATOM   4694 N N   . CYS B 1 119 ? 12.378  70.131  50.315  1.00 74.08  ? 214  CYS B N   1 
ATOM   4695 C CA  . CYS B 1 119 ? 13.479  70.689  51.077  1.00 75.14  ? 214  CYS B CA  1 
ATOM   4696 C C   . CYS B 1 119 ? 12.945  71.790  51.988  1.00 77.83  ? 214  CYS B C   1 
ATOM   4697 O O   . CYS B 1 119 ? 12.058  72.559  51.602  1.00 78.67  ? 214  CYS B O   1 
ATOM   4698 C CB  . CYS B 1 119 ? 14.562  71.244  50.146  1.00 75.93  ? 214  CYS B CB  1 
ATOM   4699 S SG  . CYS B 1 119 ? 14.987  70.167  48.736  1.00 72.94  ? 214  CYS B SG  1 
ATOM   4700 N N   . ILE B 1 120 ? 13.499  71.867  53.198  1.00 78.24  ? 215  ILE B N   1 
ATOM   4701 C CA  . ILE B 1 120 ? 12.960  72.689  54.282  1.00 76.81  ? 215  ILE B CA  1 
ATOM   4702 C C   . ILE B 1 120 ? 14.019  73.693  54.713  1.00 77.89  ? 215  ILE B C   1 
ATOM   4703 O O   . ILE B 1 120 ? 15.149  73.310  55.046  1.00 79.46  ? 215  ILE B O   1 
ATOM   4704 C CB  . ILE B 1 120 ? 12.519  71.825  55.474  1.00 80.95  ? 215  ILE B CB  1 
ATOM   4705 C CG1 . ILE B 1 120 ? 11.319  70.956  55.090  1.00 83.00  ? 215  ILE B CG1 1 
ATOM   4706 C CG2 . ILE B 1 120 ? 12.219  72.692  56.703  1.00 79.63  ? 215  ILE B CG2 1 
ATOM   4707 C CD1 . ILE B 1 120 ? 11.389  69.558  55.648  1.00 85.66  ? 215  ILE B CD1 1 
ATOM   4708 N N   . LEU B 1 121 ? 13.660  74.977  54.693  1.00 77.90  ? 216  LEU B N   1 
ATOM   4709 C CA  . LEU B 1 121 ? 14.497  76.047  55.227  1.00 82.83  ? 216  LEU B CA  1 
ATOM   4710 C C   . LEU B 1 121 ? 13.894  76.474  56.560  1.00 85.37  ? 216  LEU B C   1 
ATOM   4711 O O   . LEU B 1 121 ? 12.791  77.029  56.599  1.00 87.44  ? 216  LEU B O   1 
ATOM   4712 C CB  . LEU B 1 121 ? 14.593  77.230  54.263  1.00 78.97  ? 216  LEU B CB  1 
ATOM   4713 C CG  . LEU B 1 121 ? 15.429  78.411  54.785  1.00 87.98  ? 216  LEU B CG  1 
ATOM   4714 C CD1 . LEU B 1 121 ? 16.880  77.992  55.018  1.00 85.71  ? 216  LEU B CD1 1 
ATOM   4715 C CD2 . LEU B 1 121 ? 15.355  79.643  53.876  1.00 87.07  ? 216  LEU B CD2 1 
ATOM   4716 N N   . ASP B 1 122 ? 14.611  76.220  57.638  1.00 88.84  ? 217  ASP B N   1 
ATOM   4717 C CA  . ASP B 1 122 ? 14.164  76.620  58.963  1.00 91.99  ? 217  ASP B CA  1 
ATOM   4718 C C   . ASP B 1 122 ? 15.196  77.576  59.493  1.00 94.65  ? 217  ASP B C   1 
ATOM   4719 O O   . ASP B 1 122 ? 16.293  77.173  59.847  1.00 98.46  ? 217  ASP B O   1 
ATOM   4720 C CB  . ASP B 1 122 ? 14.055  75.427  59.898  1.00 91.34  ? 217  ASP B CB  1 
ATOM   4721 C CG  . ASP B 1 122 ? 13.261  75.743  61.148  1.00 100.48 ? 217  ASP B CG  1 
ATOM   4722 O OD1 . ASP B 1 122 ? 12.859  76.904  61.310  1.00 101.74 ? 217  ASP B OD1 1 
ATOM   4723 O OD2 . ASP B 1 122 ? 13.033  74.833  61.960  1.00 98.91  ? 217  ASP B OD2 1 
ATOM   4724 N N   . ILE B 1 123 ? 14.799  78.824  59.694  1.00 96.28  ? 218  ILE B N   1 
ATOM   4725 C CA  . ILE B 1 123 ? 15.717  79.879  60.137  1.00 102.84 ? 218  ILE B CA  1 
ATOM   4726 C C   . ILE B 1 123 ? 16.414  79.623  61.472  1.00 109.63 ? 218  ILE B C   1 
ATOM   4727 O O   . ILE B 1 123 ? 17.553  80.011  61.648  1.00 112.56 ? 218  ILE B O   1 
ATOM   4728 C CB  . ILE B 1 123 ? 15.036  81.252  60.165  1.00 100.48 ? 218  ILE B CB  1 
ATOM   4729 N N   . LYS B 1 124 ? 15.761  78.897  62.372  1.00 110.94 ? 219  LYS B N   1 
ATOM   4730 C CA  . LYS B 1 124 ? 16.266  78.545  63.688  1.00 114.79 ? 219  LYS B CA  1 
ATOM   4731 C C   . LYS B 1 124 ? 17.581  77.783  63.634  1.00 115.97 ? 219  LYS B C   1 
ATOM   4732 O O   . LYS B 1 124 ? 18.399  77.918  64.522  1.00 118.53 ? 219  LYS B O   1 
ATOM   4733 C CB  . LYS B 1 124 ? 15.225  77.728  64.432  1.00 113.63 ? 219  LYS B CB  1 
ATOM   4734 N N   . HIS B 1 125 ? 17.773  76.940  62.631  1.00 113.58 ? 220  HIS B N   1 
ATOM   4735 C CA  . HIS B 1 125 ? 19.015  76.209  62.478  1.00 116.26 ? 220  HIS B CA  1 
ATOM   4736 C C   . HIS B 1 125 ? 20.034  76.963  61.630  1.00 116.84 ? 220  HIS B C   1 
ATOM   4737 O O   . HIS B 1 125 ? 21.084  76.429  61.316  1.00 117.43 ? 220  HIS B O   1 
ATOM   4738 C CB  . HIS B 1 125 ? 18.753  74.838  61.876  1.00 120.40 ? 220  HIS B CB  1 
ATOM   4739 C CG  . HIS B 1 125 ? 17.820  73.993  62.680  1.00 121.34 ? 220  HIS B CG  1 
ATOM   4740 N ND1 . HIS B 1 125 ? 16.521  73.748  62.297  1.00 117.59 ? 220  HIS B ND1 1 
ATOM   4741 C CD2 . HIS B 1 125 ? 18.001  73.329  63.844  1.00 124.80 ? 220  HIS B CD2 1 
ATOM   4742 C CE1 . HIS B 1 125 ? 15.941  72.971  63.190  1.00 121.63 ? 220  HIS B CE1 1 
ATOM   4743 N NE2 . HIS B 1 125 ? 16.818  72.704  64.139  1.00 125.37 ? 220  HIS B NE2 1 
ATOM   4744 N N   . ASN B 1 126 ? 19.700  78.181  61.221  1.00 113.10 ? 221  ASN B N   1 
ATOM   4745 C CA  . ASN B 1 126 ? 20.577  79.012  60.410  1.00 109.58 ? 221  ASN B CA  1 
ATOM   4746 C C   . ASN B 1 126 ? 20.956  80.347  61.021  1.00 111.73 ? 221  ASN B C   1 
ATOM   4747 O O   . ASN B 1 126 ? 21.003  81.346  60.320  1.00 110.31 ? 221  ASN B O   1 
ATOM   4748 C CB  . ASN B 1 126 ? 19.948  79.253  59.054  1.00 106.86 ? 221  ASN B CB  1 
ATOM   4749 C CG  . ASN B 1 126 ? 20.268  78.159  58.082  1.00 104.07 ? 221  ASN B CG  1 
ATOM   4750 O OD1 . ASN B 1 126 ? 21.364  78.115  57.541  1.00 100.58 ? 221  ASN B OD1 1 
ATOM   4751 N ND2 . ASN B 1 126 ? 19.333  77.256  57.883  1.00 99.32  ? 221  ASN B ND2 1 
ATOM   4752 N N   . ASP B 1 127 ? 21.115  80.370  62.343  1.00 112.40 ? 222  ASP B N   1 
ATOM   4753 C CA  . ASP B 1 127 ? 21.454  81.569  63.125  1.00 113.53 ? 222  ASP B CA  1 
ATOM   4754 C C   . ASP B 1 127 ? 20.408  82.684  63.008  1.00 118.19 ? 222  ASP B C   1 
ATOM   4755 O O   . ASP B 1 127 ? 20.732  83.857  63.003  1.00 119.04 ? 222  ASP B O   1 
ATOM   4756 C CB  . ASP B 1 127 ? 22.866  82.087  62.822  1.00 107.44 ? 222  ASP B CB  1 
ATOM   4757 N N   . ASN B 1 128 ? 19.150  82.294  62.858  1.00 120.55 ? 223  ASN B N   1 
ATOM   4758 C CA  . ASN B 1 128 ? 18.043  83.217  62.752  1.00 119.75 ? 223  ASN B CA  1 
ATOM   4759 C C   . ASN B 1 128 ? 18.207  84.292  61.710  1.00 120.12 ? 223  ASN B C   1 
ATOM   4760 O O   . ASN B 1 128 ? 17.843  85.429  61.948  1.00 121.24 ? 223  ASN B O   1 
ATOM   4761 C CB  . ASN B 1 128 ? 17.710  83.815  64.100  1.00 123.90 ? 223  ASN B CB  1 
ATOM   4762 C CG  . ASN B 1 128 ? 17.030  82.825  64.998  1.00 127.31 ? 223  ASN B CG  1 
ATOM   4763 O OD1 . ASN B 1 128 ? 15.822  82.887  65.178  1.00 134.03 ? 223  ASN B OD1 1 
ATOM   4764 N ND2 . ASN B 1 128 ? 17.794  81.886  65.547  1.00 124.35 ? 223  ASN B ND2 1 
ATOM   4765 N N   . ASP B 1 129 ? 18.725  83.943  60.543  1.00 117.84 ? 224  ASP B N   1 
ATOM   4766 C CA  . ASP B 1 129 ? 18.895  84.947  59.532  1.00 113.76 ? 224  ASP B CA  1 
ATOM   4767 C C   . ASP B 1 129 ? 17.591  85.136  58.822  1.00 112.43 ? 224  ASP B C   1 
ATOM   4768 O O   . ASP B 1 129 ? 16.944  84.193  58.436  1.00 111.98 ? 224  ASP B O   1 
ATOM   4769 C CB  . ASP B 1 129 ? 19.968  84.563  58.539  1.00 115.58 ? 224  ASP B CB  1 
ATOM   4770 C CG  . ASP B 1 129 ? 20.263  85.669  57.569  1.00 112.08 ? 224  ASP B CG  1 
ATOM   4771 O OD1 . ASP B 1 129 ? 21.447  85.888  57.250  1.00 111.25 ? 224  ASP B OD1 1 
ATOM   4772 O OD2 . ASP B 1 129 ? 19.312  86.341  57.136  1.00 112.90 ? 224  ASP B OD2 1 
ATOM   4773 N N   . LYS B 1 130 ? 17.193  86.381  58.693  1.00 109.16 ? 225  LYS B N   1 
ATOM   4774 C CA  . LYS B 1 130 ? 15.974  86.715  57.969  1.00 104.03 ? 225  LYS B CA  1 
ATOM   4775 C C   . LYS B 1 130 ? 16.262  87.154  56.542  1.00 99.16  ? 225  LYS B C   1 
ATOM   4776 O O   . LYS B 1 130 ? 15.386  87.032  55.676  1.00 94.31  ? 225  LYS B O   1 
ATOM   4777 C CB  . LYS B 1 130 ? 15.201  87.815  58.706  1.00 94.96  ? 225  LYS B CB  1 
ATOM   4778 N N   . ASN B 1 131 ? 17.468  87.675  56.293  1.00 98.87  ? 226  ASN B N   1 
ATOM   4779 C CA  . ASN B 1 131 ? 17.896  87.963  54.928  1.00 99.50  ? 226  ASN B CA  1 
ATOM   4780 C C   . ASN B 1 131 ? 17.903  86.698  54.087  1.00 96.93  ? 226  ASN B C   1 
ATOM   4781 O O   . ASN B 1 131 ? 17.498  86.719  52.919  1.00 95.78  ? 226  ASN B O   1 
ATOM   4782 C CB  . ASN B 1 131 ? 19.286  88.601  54.930  1.00 100.59 ? 226  ASN B CB  1 
ATOM   4783 C CG  . ASN B 1 131 ? 19.339  89.869  55.740  1.00 103.86 ? 226  ASN B CG  1 
ATOM   4784 O OD1 . ASN B 1 131 ? 18.488  90.745  55.587  1.00 102.29 ? 226  ASN B OD1 1 
ATOM   4785 N ND2 . ASN B 1 131 ? 20.330  89.974  56.623  1.00 106.98 ? 226  ASN B ND2 1 
ATOM   4786 N N   . MET B 1 132 ? 18.372  85.587  54.661  1.00 96.81  ? 227  MET B N   1 
ATOM   4787 C CA  . MET B 1 132 ? 18.361  84.322  53.937  1.00 97.08  ? 227  MET B CA  1 
ATOM   4788 C C   . MET B 1 132 ? 16.939  83.909  53.584  1.00 93.06  ? 227  MET B C   1 
ATOM   4789 O O   . MET B 1 132 ? 16.666  83.472  52.458  1.00 91.41  ? 227  MET B O   1 
ATOM   4790 C CB  . MET B 1 132 ? 19.044  83.228  54.759  1.00 98.04  ? 227  MET B CB  1 
ATOM   4791 C CG  . MET B 1 132 ? 19.042  81.880  54.047  1.00 95.17  ? 227  MET B CG  1 
ATOM   4792 S SD  . MET B 1 132 ? 19.811  80.537  54.965  1.00 97.90  ? 227  MET B SD  1 
ATOM   4793 C CE  . MET B 1 132 ? 21.458  81.184  55.173  1.00 98.68  ? 227  MET B CE  1 
ATOM   4794 N N   . MET B 1 133 ? 16.019  84.034  54.544  1.00 93.36  ? 228  MET B N   1 
ATOM   4795 C CA  . MET B 1 133 ? 14.621  83.697  54.292  1.00 91.45  ? 228  MET B CA  1 
ATOM   4796 C C   . MET B 1 133 ? 14.040  84.565  53.182  1.00 89.36  ? 228  MET B C   1 
ATOM   4797 O O   . MET B 1 133 ? 13.354  84.066  52.283  1.00 86.94  ? 228  MET B O   1 
ATOM   4798 C CB  . MET B 1 133 ? 13.808  83.849  55.579  1.00 93.66  ? 228  MET B CB  1 
ATOM   4799 C CG  . MET B 1 133 ? 12.324  83.555  55.413  1.00 94.62  ? 228  MET B CG  1 
ATOM   4800 S SD  . MET B 1 133 ? 12.051  81.864  54.862  1.00 96.53  ? 228  MET B SD  1 
ATOM   4801 C CE  . MET B 1 133 ? 12.819  80.964  56.208  1.00 94.83  ? 228  MET B CE  1 
ATOM   4802 N N   . LYS B 1 134 ? 14.320  85.869  53.222  1.00 89.22  ? 229  LYS B N   1 
ATOM   4803 C CA  . LYS B 1 134 ? 13.817  86.766  52.187  1.00 90.11  ? 229  LYS B CA  1 
ATOM   4804 C C   . LYS B 1 134 ? 14.366  86.382  50.816  1.00 86.38  ? 229  LYS B C   1 
ATOM   4805 O O   . LYS B 1 134 ? 13.611  86.263  49.840  1.00 89.06  ? 229  LYS B O   1 
ATOM   4806 C CB  . LYS B 1 134 ? 14.176  88.212  52.537  1.00 89.11  ? 229  LYS B CB  1 
ATOM   4807 N N   . TRP B 1 135 ? 15.683  86.167  50.731  1.00 87.30  ? 230  TRP B N   1 
ATOM   4808 C CA  . TRP B 1 135 ? 16.307  85.834  49.454  1.00 86.84  ? 230  TRP B CA  1 
ATOM   4809 C C   . TRP B 1 135 ? 15.769  84.523  48.895  1.00 83.80  ? 230  TRP B C   1 
ATOM   4810 O O   . TRP B 1 135 ? 15.467  84.433  47.699  1.00 84.23  ? 230  TRP B O   1 
ATOM   4811 C CB  . TRP B 1 135 ? 17.827  85.759  49.606  1.00 86.90  ? 230  TRP B CB  1 
ATOM   4812 C CG  . TRP B 1 135 ? 18.527  85.396  48.327  1.00 85.36  ? 230  TRP B CG  1 
ATOM   4813 C CD1 . TRP B 1 135 ? 18.928  86.251  47.343  1.00 86.45  ? 230  TRP B CD1 1 
ATOM   4814 C CD2 . TRP B 1 135 ? 18.898  84.082  47.890  1.00 83.54  ? 230  TRP B CD2 1 
ATOM   4815 N NE1 . TRP B 1 135 ? 19.530  85.556  46.324  1.00 85.36  ? 230  TRP B NE1 1 
ATOM   4816 C CE2 . TRP B 1 135 ? 19.523  84.221  46.633  1.00 84.66  ? 230  TRP B CE2 1 
ATOM   4817 C CE3 . TRP B 1 135 ? 18.767  82.803  48.440  1.00 82.08  ? 230  TRP B CE3 1 
ATOM   4818 C CZ2 . TRP B 1 135 ? 20.008  83.127  45.913  1.00 80.94  ? 230  TRP B CZ2 1 
ATOM   4819 C CZ3 . TRP B 1 135 ? 19.256  81.719  47.728  1.00 80.22  ? 230  TRP B CZ3 1 
ATOM   4820 C CH2 . TRP B 1 135 ? 19.870  81.889  46.478  1.00 80.67  ? 230  TRP B CH2 1 
ATOM   4821 N N   . VAL B 1 136 ? 15.644  83.497  49.739  1.00 84.59  ? 231  VAL B N   1 
ATOM   4822 C CA  . VAL B 1 136 ? 15.153  82.206  49.267  1.00 84.62  ? 231  VAL B CA  1 
ATOM   4823 C C   . VAL B 1 136 ? 13.701  82.317  48.826  1.00 83.66  ? 231  VAL B C   1 
ATOM   4824 O O   . VAL B 1 136 ? 13.313  81.768  47.787  1.00 79.99  ? 231  VAL B O   1 
ATOM   4825 C CB  . VAL B 1 136 ? 15.323  81.131  50.356  1.00 81.94  ? 231  VAL B CB  1 
ATOM   4826 C CG1 . VAL B 1 136 ? 14.599  79.856  49.950  1.00 78.67  ? 231  VAL B CG1 1 
ATOM   4827 C CG2 . VAL B 1 136 ? 16.796  80.848  50.606  1.00 80.62  ? 231  VAL B CG2 1 
ATOM   4828 N N   . SER B 1 137 ? 12.877  83.039  49.597  1.00 82.39  ? 232  SER B N   1 
ATOM   4829 C CA  . SER B 1 137 ? 11.464  83.169  49.274  1.00 81.00  ? 232  SER B CA  1 
ATOM   4830 C C   . SER B 1 137 ? 11.230  83.997  48.023  1.00 80.69  ? 232  SER B C   1 
ATOM   4831 O O   . SER B 1 137 ? 10.160  83.885  47.421  1.00 83.40  ? 232  SER B O   1 
ATOM   4832 C CB  . SER B 1 137 ? 10.709  83.796  50.445  1.00 85.47  ? 232  SER B CB  1 
ATOM   4833 O OG  . SER B 1 137 ? 11.102  83.197  51.664  1.00 85.77  ? 232  SER B OG  1 
ATOM   4834 N N   . ASN B 1 138 ? 12.189  84.831  47.624  1.00 80.57  ? 233  ASN B N   1 
ATOM   4835 C CA  . ASN B 1 138 ? 12.039  85.600  46.394  1.00 82.01  ? 233  ASN B CA  1 
ATOM   4836 C C   . ASN B 1 138 ? 12.496  84.854  45.131  1.00 77.70  ? 233  ASN B C   1 
ATOM   4837 O O   . ASN B 1 138 ? 12.402  85.411  44.030  1.00 74.81  ? 233  ASN B O   1 
ATOM   4838 C CB  . ASN B 1 138 ? 12.800  86.924  46.515  1.00 83.54  ? 233  ASN B CB  1 
ATOM   4839 C CG  . ASN B 1 138 ? 12.320  87.957  45.522  1.00 85.42  ? 233  ASN B CG  1 
ATOM   4840 O OD1 . ASN B 1 138 ? 11.117  88.095  45.289  1.00 85.13  ? 233  ASN B OD1 1 
ATOM   4841 N ND2 . ASN B 1 138 ? 13.257  88.679  44.914  1.00 87.31  ? 233  ASN B ND2 1 
ATOM   4842 N N   . LEU B 1 139 ? 12.970  83.621  45.240  1.00 76.30  ? 234  LEU B N   1 
ATOM   4843 C CA  . LEU B 1 139 ? 13.476  82.925  44.057  1.00 74.73  ? 234  LEU B CA  1 
ATOM   4844 C C   . LEU B 1 139 ? 12.328  82.582  43.111  1.00 73.67  ? 234  LEU B C   1 
ATOM   4845 O O   . LEU B 1 139 ? 11.317  82.022  43.555  1.00 74.79  ? 234  LEU B O   1 
ATOM   4846 C CB  . LEU B 1 139 ? 14.220  81.651  44.461  1.00 73.10  ? 234  LEU B CB  1 
ATOM   4847 C CG  . LEU B 1 139 ? 15.617  81.848  45.050  1.00 76.74  ? 234  LEU B CG  1 
ATOM   4848 C CD1 . LEU B 1 139 ? 16.164  80.532  45.564  1.00 72.53  ? 234  LEU B CD1 1 
ATOM   4849 C CD2 . LEU B 1 139 ? 16.548  82.451  44.012  1.00 74.61  ? 234  LEU B CD2 1 
ATOM   4850 N N   . PRO B 1 140 ? 12.438  82.894  41.817  1.00 68.54  ? 235  PRO B N   1 
ATOM   4851 C CA  . PRO B 1 140 ? 11.378  82.516  40.872  1.00 66.39  ? 235  PRO B CA  1 
ATOM   4852 C C   . PRO B 1 140 ? 11.303  81.007  40.692  1.00 66.51  ? 235  PRO B C   1 
ATOM   4853 O O   . PRO B 1 140 ? 12.302  80.292  40.809  1.00 64.20  ? 235  PRO B O   1 
ATOM   4854 C CB  . PRO B 1 140 ? 11.798  83.185  39.555  1.00 68.50  ? 235  PRO B CB  1 
ATOM   4855 C CG  . PRO B 1 140 ? 13.040  83.939  39.833  1.00 70.89  ? 235  PRO B CG  1 
ATOM   4856 C CD  . PRO B 1 140 ? 13.598  83.499  41.147  1.00 70.71  ? 235  PRO B CD  1 
ATOM   4857 N N   . LEU B 1 141 ? 10.099  80.524  40.390  1.00 64.11  ? 236  LEU B N   1 
ATOM   4858 C CA  . LEU B 1 141 ? 9.944   79.111  40.089  1.00 63.03  ? 236  LEU B CA  1 
ATOM   4859 C C   . LEU B 1 141 ? 10.710  78.764  38.814  1.00 62.01  ? 236  LEU B C   1 
ATOM   4860 O O   . LEU B 1 141 ? 10.830  79.582  37.897  1.00 60.42  ? 236  LEU B O   1 
ATOM   4861 C CB  . LEU B 1 141 ? 8.464   78.752  39.940  1.00 60.32  ? 236  LEU B CB  1 
ATOM   4862 C CG  . LEU B 1 141 ? 7.620   78.809  41.221  1.00 67.66  ? 236  LEU B CG  1 
ATOM   4863 C CD1 . LEU B 1 141 ? 6.194   78.352  40.936  1.00 65.69  ? 236  LEU B CD1 1 
ATOM   4864 C CD2 . LEU B 1 141 ? 8.239   77.947  42.309  1.00 67.47  ? 236  LEU B CD2 1 
ATOM   4865 N N   . GLU B 1 142 ? 11.233  77.536  38.777  1.00 61.68  ? 237  GLU B N   1 
ATOM   4866 C CA  . GLU B 1 142 ? 12.070  76.916  37.741  1.00 58.51  ? 237  GLU B CA  1 
ATOM   4867 C C   . GLU B 1 142 ? 13.547  77.272  37.891  1.00 58.91  ? 237  GLU B C   1 
ATOM   4868 O O   . GLU B 1 142 ? 14.350  76.764  37.111  1.00 58.93  ? 237  GLU B O   1 
ATOM   4869 C CB  . GLU B 1 142 ? 11.632  77.247  36.304  1.00 53.85  ? 237  GLU B CB  1 
ATOM   4870 C CG  . GLU B 1 142 ? 10.308  76.621  35.909  1.00 57.86  ? 237  GLU B CG  1 
ATOM   4871 C CD  . GLU B 1 142 ? 10.275  75.124  36.189  1.00 58.98  ? 237  GLU B CD  1 
ATOM   4872 O OE1 . GLU B 1 142 ? 9.641   74.721  37.186  1.00 60.32  ? 237  GLU B OE1 1 
ATOM   4873 O OE2 . GLU B 1 142 ? 10.909  74.355  35.428  1.00 57.70  ? 237  GLU B OE2 1 
ATOM   4874 N N   . SER B 1 143 ? 13.936  78.103  38.857  1.00 59.83  ? 238  SER B N   1 
ATOM   4875 C CA  . SER B 1 143 ? 15.351  78.403  39.050  1.00 60.82  ? 238  SER B CA  1 
ATOM   4876 C C   . SER B 1 143 ? 16.116  77.144  39.447  1.00 59.16  ? 238  SER B C   1 
ATOM   4877 O O   . SER B 1 143 ? 15.609  76.288  40.173  1.00 60.89  ? 238  SER B O   1 
ATOM   4878 C CB  . SER B 1 143 ? 15.534  79.475  40.131  1.00 64.04  ? 238  SER B CB  1 
ATOM   4879 O OG  . SER B 1 143 ? 14.819  80.666  39.836  1.00 65.24  ? 238  SER B OG  1 
ATOM   4880 N N   . ILE B 1 144 ? 17.352  77.033  38.977  1.00 59.21  ? 239  ILE B N   1 
ATOM   4881 C CA  . ILE B 1 144 ? 18.185  75.874  39.273  1.00 61.13  ? 239  ILE B CA  1 
ATOM   4882 C C   . ILE B 1 144 ? 19.083  76.213  40.453  1.00 61.78  ? 239  ILE B C   1 
ATOM   4883 O O   . ILE B 1 144 ? 19.835  77.196  40.408  1.00 63.53  ? 239  ILE B O   1 
ATOM   4884 C CB  . ILE B 1 144 ? 19.012  75.444  38.053  1.00 57.71  ? 239  ILE B CB  1 
ATOM   4885 C CG1 . ILE B 1 144 ? 18.088  75.043  36.906  1.00 54.74  ? 239  ILE B CG1 1 
ATOM   4886 C CG2 . ILE B 1 144 ? 19.919  74.296  38.432  1.00 57.88  ? 239  ILE B CG2 1 
ATOM   4887 C CD1 . ILE B 1 144 ? 18.802  74.875  35.574  1.00 56.51  ? 239  ILE B CD1 1 
ATOM   4888 N N   . VAL B 1 145 ? 19.018  75.385  41.503  1.00 63.74  ? 240  VAL B N   1 
ATOM   4889 C CA  . VAL B 1 145 ? 19.742  75.626  42.746  1.00 63.98  ? 240  VAL B CA  1 
ATOM   4890 C C   . VAL B 1 145 ? 20.583  74.411  43.125  1.00 65.23  ? 240  VAL B C   1 
ATOM   4891 O O   . VAL B 1 145 ? 20.250  73.259  42.814  1.00 63.71  ? 240  VAL B O   1 
ATOM   4892 C CB  . VAL B 1 145 ? 18.796  75.990  43.926  1.00 67.32  ? 240  VAL B CB  1 
ATOM   4893 C CG1 . VAL B 1 145 ? 17.946  77.212  43.596  1.00 65.34  ? 240  VAL B CG1 1 
ATOM   4894 C CG2 . VAL B 1 145 ? 17.916  74.806  44.313  1.00 63.53  ? 240  VAL B CG2 1 
ATOM   4895 N N   . ASP B 1 146 ? 21.682  74.696  43.825  1.00 66.02  ? 241  ASP B N   1 
ATOM   4896 C CA  . ASP B 1 146 ? 22.490  73.705  44.519  1.00 67.18  ? 241  ASP B CA  1 
ATOM   4897 C C   . ASP B 1 146 ? 22.241  73.842  46.018  1.00 71.50  ? 241  ASP B C   1 
ATOM   4898 O O   . ASP B 1 146 ? 22.450  74.918  46.594  1.00 74.82  ? 241  ASP B O   1 
ATOM   4899 C CB  . ASP B 1 146 ? 23.973  73.886  44.196  1.00 66.07  ? 241  ASP B CB  1 
ATOM   4900 C CG  . ASP B 1 146 ? 24.321  73.421  42.791  1.00 67.81  ? 241  ASP B CG  1 
ATOM   4901 O OD1 . ASP B 1 146 ? 23.390  73.018  42.063  1.00 64.73  ? 241  ASP B OD1 1 
ATOM   4902 O OD2 . ASP B 1 146 ? 25.516  73.445  42.420  1.00 68.40  ? 241  ASP B OD2 1 
ATOM   4903 N N   . ILE B 1 147 ? 21.793  72.759  46.644  1.00 72.35  ? 242  ILE B N   1 
ATOM   4904 C CA  . ILE B 1 147 ? 21.435  72.737  48.057  1.00 74.00  ? 242  ILE B CA  1 
ATOM   4905 C C   . ILE B 1 147 ? 22.393  71.800  48.772  1.00 75.91  ? 242  ILE B C   1 
ATOM   4906 O O   . ILE B 1 147 ? 22.668  70.700  48.284  1.00 76.82  ? 242  ILE B O   1 
ATOM   4907 C CB  . ILE B 1 147 ? 19.975  72.285  48.258  1.00 73.65  ? 242  ILE B CB  1 
ATOM   4908 C CG1 . ILE B 1 147 ? 19.013  73.382  47.807  1.00 71.48  ? 242  ILE B CG1 1 
ATOM   4909 C CG2 . ILE B 1 147 ? 19.704  71.888  49.700  1.00 71.97  ? 242  ILE B CG2 1 
ATOM   4910 C CD1 . ILE B 1 147 ? 17.596  72.905  47.651  1.00 73.38  ? 242  ILE B CD1 1 
ATOM   4911 N N   . LYS B 1 148 ? 22.924  72.250  49.905  1.00 77.90  ? 243  LYS B N   1 
ATOM   4912 C CA  . LYS B 1 148 ? 23.630  71.398  50.852  1.00 80.11  ? 243  LYS B CA  1 
ATOM   4913 C C   . LYS B 1 148 ? 22.698  71.173  52.030  1.00 81.52  ? 243  LYS B C   1 
ATOM   4914 O O   . LYS B 1 148 ? 22.220  72.136  52.638  1.00 83.86  ? 243  LYS B O   1 
ATOM   4915 C CB  . LYS B 1 148 ? 24.944  72.032  51.312  1.00 83.16  ? 243  LYS B CB  1 
ATOM   4916 C CG  . LYS B 1 148 ? 25.702  71.218  52.361  1.00 85.61  ? 243  LYS B CG  1 
ATOM   4917 C CD  . LYS B 1 148 ? 27.085  71.812  52.616  1.00 93.06  ? 243  LYS B CD  1 
ATOM   4918 C CE  . LYS B 1 148 ? 27.814  71.115  53.760  1.00 98.31  ? 243  LYS B CE  1 
ATOM   4919 N NZ  . LYS B 1 148 ? 29.253  71.510  53.817  1.00 103.23 ? 243  LYS B NZ  1 
ATOM   4920 N N   . GLY B 1 149 ? 22.424  69.912  52.340  1.00 83.83  ? 244  GLY B N   1 
ATOM   4921 C CA  . GLY B 1 149 ? 21.443  69.656  53.373  1.00 85.34  ? 244  GLY B CA  1 
ATOM   4922 C C   . GLY B 1 149 ? 21.535  68.243  53.897  1.00 87.11  ? 244  GLY B C   1 
ATOM   4923 O O   . GLY B 1 149 ? 22.284  67.409  53.384  1.00 86.94  ? 244  GLY B O   1 
ATOM   4924 N N   . LYS B 1 150 ? 20.746  67.992  54.936  1.00 87.20  ? 245  LYS B N   1 
ATOM   4925 C CA  . LYS B 1 150 ? 20.700  66.698  55.604  1.00 86.17  ? 245  LYS B CA  1 
ATOM   4926 C C   . LYS B 1 150 ? 19.404  65.990  55.240  1.00 88.20  ? 245  LYS B C   1 
ATOM   4927 O O   . LYS B 1 150 ? 18.326  66.587  55.321  1.00 86.54  ? 245  LYS B O   1 
ATOM   4928 C CB  . LYS B 1 150 ? 20.809  66.852  57.126  1.00 85.03  ? 245  LYS B CB  1 
ATOM   4929 N N   . LEU B 1 151 ? 19.517  64.722  54.840  1.00 90.38  ? 246  LEU B N   1 
ATOM   4930 C CA  . LEU B 1 151 ? 18.371  63.907  54.453  1.00 89.81  ? 246  LEU B CA  1 
ATOM   4931 C C   . LEU B 1 151 ? 17.818  63.149  55.655  1.00 92.76  ? 246  LEU B C   1 
ATOM   4932 O O   . LEU B 1 151 ? 18.550  62.417  56.328  1.00 95.84  ? 246  LEU B O   1 
ATOM   4933 C CB  . LEU B 1 151 ? 18.768  62.917  53.361  1.00 90.38  ? 246  LEU B CB  1 
ATOM   4934 C CG  . LEU B 1 151 ? 18.403  63.237  51.911  1.00 89.90  ? 246  LEU B CG  1 
ATOM   4935 C CD1 . LEU B 1 151 ? 18.790  64.655  51.520  1.00 84.83  ? 246  LEU B CD1 1 
ATOM   4936 C CD2 . LEU B 1 151 ? 19.094  62.244  51.010  1.00 88.47  ? 246  LEU B CD2 1 
ATOM   4937 N N   . SER B 1 152 ? 16.522  63.315  55.911  1.00 91.79  ? 247  SER B N   1 
ATOM   4938 C CA  . SER B 1 152 ? 15.852  62.589  56.982  1.00 98.10  ? 247  SER B CA  1 
ATOM   4939 C C   . SER B 1 152 ? 14.483  62.123  56.504  1.00 98.29  ? 247  SER B C   1 
ATOM   4940 O O   . SER B 1 152 ? 13.872  62.740  55.628  1.00 93.82  ? 247  SER B O   1 
ATOM   4941 C CB  . SER B 1 152 ? 15.717  63.444  58.256  1.00 95.43  ? 247  SER B CB  1 
ATOM   4942 O OG  . SER B 1 152 ? 15.195  64.730  57.965  1.00 94.31  ? 247  SER B OG  1 
ATOM   4943 N N   . LYS B 1 153 ? 14.009  61.013  57.079  1.00 99.50  ? 248  LYS B N   1 
ATOM   4944 C CA  . LYS B 1 153 ? 12.701  60.474  56.728  1.00 97.27  ? 248  LYS B CA  1 
ATOM   4945 C C   . LYS B 1 153 ? 11.660  61.032  57.685  1.00 96.79  ? 248  LYS B C   1 
ATOM   4946 O O   . LYS B 1 153 ? 11.667  60.672  58.870  1.00 100.93 ? 248  LYS B O   1 
ATOM   4947 C CB  . LYS B 1 153 ? 12.708  58.953  56.786  1.00 100.00 ? 248  LYS B CB  1 
ATOM   4948 C CG  . LYS B 1 153 ? 11.330  58.336  56.586  1.00 101.50 ? 248  LYS B CG  1 
ATOM   4949 C CD  . LYS B 1 153 ? 11.338  57.306  55.460  1.00 103.25 ? 248  LYS B CD  1 
ATOM   4950 C CE  . LYS B 1 153 ? 9.920   56.948  55.040  1.00 101.84 ? 248  LYS B CE  1 
ATOM   4951 N NZ  . LYS B 1 153 ? 9.891   55.862  54.018  1.00 106.16 ? 248  LYS B NZ  1 
ATOM   4952 N N   . PRO B 1 154 ? 10.749  61.892  57.232  1.00 100.28 ? 249  PRO B N   1 
ATOM   4953 C CA  . PRO B 1 154 ? 9.781   62.490  58.155  1.00 98.19  ? 249  PRO B CA  1 
ATOM   4954 C C   . PRO B 1 154 ? 8.706   61.490  58.552  1.00 104.91 ? 249  PRO B C   1 
ATOM   4955 O O   . PRO B 1 154 ? 8.532   60.436  57.933  1.00 104.20 ? 249  PRO B O   1 
ATOM   4956 C CB  . PRO B 1 154 ? 9.189   63.641  57.340  1.00 97.32  ? 249  PRO B CB  1 
ATOM   4957 C CG  . PRO B 1 154 ? 9.236   63.122  55.922  1.00 96.88  ? 249  PRO B CG  1 
ATOM   4958 C CD  . PRO B 1 154 ? 10.505  62.295  55.832  1.00 94.45  ? 249  PRO B CD  1 
ATOM   4959 N N   . GLU B 1 155 ? 7.972   61.849  59.611  1.00 111.92 ? 250  GLU B N   1 
ATOM   4960 C CA  . GLU B 1 155 ? 6.880   61.002  60.084  1.00 113.69 ? 250  GLU B CA  1 
ATOM   4961 C C   . GLU B 1 155 ? 5.822   60.823  59.001  1.00 115.37 ? 250  GLU B C   1 
ATOM   4962 O O   . GLU B 1 155 ? 5.469   59.694  58.638  1.00 116.01 ? 250  GLU B O   1 
ATOM   4963 C CB  . GLU B 1 155 ? 6.265   61.604  61.349  1.00 113.30 ? 250  GLU B CB  1 
ATOM   4964 N N   . VAL B 1 156 ? 5.316   61.926  58.465  1.00 113.87 ? 251  VAL B N   1 
ATOM   4965 C CA  . VAL B 1 156 ? 4.316   61.912  57.406  1.00 112.41 ? 251  VAL B CA  1 
ATOM   4966 C C   . VAL B 1 156 ? 4.901   62.602  56.176  1.00 109.91 ? 251  VAL B C   1 
ATOM   4967 O O   . VAL B 1 156 ? 5.026   63.827  56.134  1.00 110.48 ? 251  VAL B O   1 
ATOM   4968 C CB  . VAL B 1 156 ? 3.007   62.586  57.860  1.00 113.01 ? 251  VAL B CB  1 
ATOM   4969 C CG1 . VAL B 1 156 ? 2.091   62.830  56.674  1.00 113.63 ? 251  VAL B CG1 1 
ATOM   4970 C CG2 . VAL B 1 156 ? 2.316   61.731  58.908  1.00 116.81 ? 251  VAL B CG2 1 
ATOM   4971 N N   . PRO B 1 157 ? 5.310   61.840  55.164  1.00 105.93 ? 252  PRO B N   1 
ATOM   4972 C CA  . PRO B 1 157 ? 5.867   62.448  53.954  1.00 99.41  ? 252  PRO B CA  1 
ATOM   4973 C C   . PRO B 1 157 ? 4.782   63.008  53.044  1.00 98.95  ? 252  PRO B C   1 
ATOM   4974 O O   . PRO B 1 157 ? 3.617   62.605  53.086  1.00 100.46 ? 252  PRO B O   1 
ATOM   4975 C CB  . PRO B 1 157 ? 6.601   61.282  53.284  1.00 96.24  ? 252  PRO B CB  1 
ATOM   4976 C CG  . PRO B 1 157 ? 5.864   60.065  53.749  1.00 98.37  ? 252  PRO B CG  1 
ATOM   4977 C CD  . PRO B 1 157 ? 5.403   60.368  55.143  1.00 104.55 ? 252  PRO B CD  1 
ATOM   4978 N N   . ILE B 1 158 ? 5.200   63.955  52.200  1.00 96.03  ? 253  ILE B N   1 
ATOM   4979 C CA  . ILE B 1 158 ? 4.269   64.636  51.308  1.00 94.27  ? 253  ILE B CA  1 
ATOM   4980 C C   . ILE B 1 158 ? 3.761   63.666  50.248  1.00 89.83  ? 253  ILE B C   1 
ATOM   4981 O O   . ILE B 1 158 ? 4.472   62.750  49.811  1.00 89.23  ? 253  ILE B O   1 
ATOM   4982 C CB  . ILE B 1 158 ? 4.930   65.867  50.660  1.00 89.85  ? 253  ILE B CB  1 
ATOM   4983 N N   . ASP B 1 159 ? 2.512   63.868  49.827  1.00 90.15  ? 254  ASP B N   1 
ATOM   4984 C CA  . ASP B 1 159 ? 1.925   62.979  48.830  1.00 91.01  ? 254  ASP B CA  1 
ATOM   4985 C C   . ASP B 1 159 ? 2.487   63.249  47.441  1.00 88.32  ? 254  ASP B C   1 
ATOM   4986 O O   . ASP B 1 159 ? 2.575   62.328  46.621  1.00 88.93  ? 254  ASP B O   1 
ATOM   4987 C CB  . ASP B 1 159 ? 0.401   63.124  48.831  1.00 91.57  ? 254  ASP B CB  1 
ATOM   4988 N N   . SER B 1 160 ? 2.887   64.494  47.170  1.00 94.57  ? 255  SER B N   1 
ATOM   4989 C CA  . SER B 1 160 ? 3.334   64.871  45.831  1.00 92.66  ? 255  SER B CA  1 
ATOM   4990 C C   . SER B 1 160 ? 4.686   64.250  45.501  1.00 90.31  ? 255  SER B C   1 
ATOM   4991 O O   . SER B 1 160 ? 4.862   63.655  44.431  1.00 89.72  ? 255  SER B O   1 
ATOM   4992 C CB  . SER B 1 160 ? 3.402   66.396  45.713  1.00 89.61  ? 255  SER B CB  1 
ATOM   4993 N N   . THR B 1 161 ? 5.652   64.376  46.407  1.00 84.51  ? 256  THR B N   1 
ATOM   4994 C CA  . THR B 1 161 ? 7.023   63.959  46.137  1.00 78.74  ? 256  THR B CA  1 
ATOM   4995 C C   . THR B 1 161 ? 7.135   62.439  46.131  1.00 78.55  ? 256  THR B C   1 
ATOM   4996 O O   . THR B 1 161 ? 6.726   61.781  47.092  1.00 80.35  ? 256  THR B O   1 
ATOM   4997 C CB  . THR B 1 161 ? 7.952   64.543  47.196  1.00 77.03  ? 256  THR B CB  1 
ATOM   4998 O OG1 . THR B 1 161 ? 7.650   63.943  48.465  1.00 78.43  ? 256  THR B OG1 1 
ATOM   4999 C CG2 . THR B 1 161 ? 7.747   66.047  47.308  1.00 74.87  ? 256  THR B CG2 1 
ATOM   5000 N N   . ASN B 1 162 ? 7.697   61.872  45.059  1.00 74.17  ? 257  ASN B N   1 
ATOM   5001 C CA  . ASN B 1 162 ? 7.910   60.431  45.093  1.00 72.54  ? 257  ASN B CA  1 
ATOM   5002 C C   . ASN B 1 162 ? 9.187   60.048  45.830  1.00 73.82  ? 257  ASN B C   1 
ATOM   5003 O O   . ASN B 1 162 ? 9.415   58.855  46.066  1.00 76.97  ? 257  ASN B O   1 
ATOM   5004 C CB  . ASN B 1 162 ? 7.893   59.823  43.676  1.00 70.47  ? 257  ASN B CB  1 
ATOM   5005 C CG  . ASN B 1 162 ? 8.916   60.443  42.730  1.00 69.03  ? 257  ASN B CG  1 
ATOM   5006 O OD1 . ASN B 1 162 ? 9.808   61.189  43.140  1.00 69.73  ? 257  ASN B OD1 1 
ATOM   5007 N ND2 . ASN B 1 162 ? 8.793   60.117  41.448  1.00 67.83  ? 257  ASN B ND2 1 
ATOM   5008 N N   . ILE B 1 163 ? 10.014  61.020  46.198  1.00 72.33  ? 258  ILE B N   1 
ATOM   5009 C CA  . ILE B 1 163 ? 11.094  60.805  47.154  1.00 74.99  ? 258  ILE B CA  1 
ATOM   5010 C C   . ILE B 1 163 ? 10.532  61.147  48.529  1.00 78.66  ? 258  ILE B C   1 
ATOM   5011 O O   . ILE B 1 163 ? 10.241  62.311  48.815  1.00 79.33  ? 258  ILE B O   1 
ATOM   5012 C CB  . ILE B 1 163 ? 12.325  61.657  46.821  1.00 73.52  ? 258  ILE B CB  1 
ATOM   5013 C CG1 . ILE B 1 163 ? 12.954  61.215  45.495  1.00 68.73  ? 258  ILE B CG1 1 
ATOM   5014 C CG2 . ILE B 1 163 ? 13.347  61.594  47.947  1.00 73.91  ? 258  ILE B CG2 1 
ATOM   5015 C CD1 . ILE B 1 163 ? 14.201  61.976  45.152  1.00 65.63  ? 258  ILE B CD1 1 
ATOM   5016 N N   . LYS B 1 164 ? 10.360  60.132  49.378  1.00 79.97  ? 259  LYS B N   1 
ATOM   5017 C CA  . LYS B 1 164 ? 9.715   60.306  50.674  1.00 81.81  ? 259  LYS B CA  1 
ATOM   5018 C C   . LYS B 1 164 ? 10.690  60.717  51.766  1.00 83.83  ? 259  LYS B C   1 
ATOM   5019 O O   . LYS B 1 164 ? 10.388  60.546  52.949  1.00 88.78  ? 259  LYS B O   1 
ATOM   5020 C CB  . LYS B 1 164 ? 8.983   59.028  51.083  1.00 80.69  ? 259  LYS B CB  1 
ATOM   5021 C CG  . LYS B 1 164 ? 7.922   58.585  50.098  1.00 79.11  ? 259  LYS B CG  1 
ATOM   5022 C CD  . LYS B 1 164 ? 6.866   59.658  49.879  1.00 78.93  ? 259  LYS B CD  1 
ATOM   5023 C CE  . LYS B 1 164 ? 5.892   59.240  48.776  1.00 76.30  ? 259  LYS B CE  1 
ATOM   5024 N NZ  . LYS B 1 164 ? 4.833   60.267  48.558  1.00 79.58  ? 259  LYS B NZ  1 
ATOM   5025 N N   . TYR B 1 165 ? 11.852  61.233  51.398  1.00 84.54  ? 260  TYR B N   1 
ATOM   5026 C CA  . TYR B 1 165 ? 12.776  61.836  52.341  1.00 86.76  ? 260  TYR B CA  1 
ATOM   5027 C C   . TYR B 1 165 ? 12.764  63.345  52.148  1.00 84.68  ? 260  TYR B C   1 
ATOM   5028 O O   . TYR B 1 165 ? 12.370  63.850  51.094  1.00 83.17  ? 260  TYR B O   1 
ATOM   5029 C CB  . TYR B 1 165 ? 14.193  61.287  52.159  1.00 89.90  ? 260  TYR B CB  1 
ATOM   5030 C CG  . TYR B 1 165 ? 14.374  59.864  52.647  1.00 94.27  ? 260  TYR B CG  1 
ATOM   5031 C CD1 . TYR B 1 165 ? 13.662  58.816  52.074  1.00 93.35  ? 260  TYR B CD1 1 
ATOM   5032 C CD2 . TYR B 1 165 ? 15.275  59.564  53.667  1.00 95.44  ? 260  TYR B CD2 1 
ATOM   5033 C CE1 . TYR B 1 165 ? 13.832  57.511  52.510  1.00 97.33  ? 260  TYR B CE1 1 
ATOM   5034 C CE2 . TYR B 1 165 ? 15.454  58.261  54.108  1.00 97.09  ? 260  TYR B CE2 1 
ATOM   5035 C CZ  . TYR B 1 165 ? 14.729  57.239  53.524  1.00 99.34  ? 260  TYR B CZ  1 
ATOM   5036 O OH  . TYR B 1 165 ? 14.892  55.939  53.955  1.00 104.42 ? 260  TYR B OH  1 
ATOM   5037 N N   . GLU B 1 166 ? 13.183  64.058  53.181  1.00 86.95  ? 261  GLU B N   1 
ATOM   5038 C CA  . GLU B 1 166 ? 13.236  65.507  53.172  1.00 86.21  ? 261  GLU B CA  1 
ATOM   5039 C C   . GLU B 1 166 ? 14.672  65.959  53.370  1.00 85.96  ? 261  GLU B C   1 
ATOM   5040 O O   . GLU B 1 166 ? 15.478  65.270  54.003  1.00 89.38  ? 261  GLU B O   1 
ATOM   5041 C CB  . GLU B 1 166 ? 12.347  66.103  54.266  1.00 86.78  ? 261  GLU B CB  1 
ATOM   5042 C CG  . GLU B 1 166 ? 10.951  66.441  53.790  1.00 87.02  ? 261  GLU B CG  1 
ATOM   5043 C CD  . GLU B 1 166 ? 9.920   66.403  54.900  1.00 91.12  ? 261  GLU B CD  1 
ATOM   5044 O OE1 . GLU B 1 166 ? 8.734   66.167  54.579  1.00 94.00  ? 261  GLU B OE1 1 
ATOM   5045 O OE2 . GLU B 1 166 ? 10.289  66.595  56.084  1.00 89.15  ? 261  GLU B OE2 1 
ATOM   5046 N N   . ALA B 1 167 ? 14.986  67.119  52.812  1.00 82.89  ? 262  ALA B N   1 
ATOM   5047 C CA  . ALA B 1 167 ? 16.310  67.711  52.923  1.00 83.41  ? 262  ALA B CA  1 
ATOM   5048 C C   . ALA B 1 167 ? 16.192  68.985  53.740  1.00 83.75  ? 262  ALA B C   1 
ATOM   5049 O O   . ALA B 1 167 ? 15.451  69.901  53.369  1.00 82.74  ? 262  ALA B O   1 
ATOM   5050 C CB  . ALA B 1 167 ? 16.907  67.999  51.545  1.00 82.65  ? 262  ALA B CB  1 
ATOM   5051 N N   . HIS B 1 168 ? 16.895  69.033  54.858  1.00 83.40  ? 263  HIS B N   1 
ATOM   5052 C CA  . HIS B 1 168 ? 16.957  70.241  55.659  1.00 82.43  ? 263  HIS B CA  1 
ATOM   5053 C C   . HIS B 1 168 ? 18.139  71.063  55.180  1.00 81.58  ? 263  HIS B C   1 
ATOM   5054 O O   . HIS B 1 168 ? 19.262  70.552  55.091  1.00 83.47  ? 263  HIS B O   1 
ATOM   5055 C CB  . HIS B 1 168 ? 17.058  69.888  57.139  1.00 82.72  ? 263  HIS B CB  1 
ATOM   5056 C CG  . HIS B 1 168 ? 15.942  69.010  57.599  1.00 84.91  ? 263  HIS B CG  1 
ATOM   5057 N ND1 . HIS B 1 168 ? 14.815  69.501  58.223  1.00 87.74  ? 263  HIS B ND1 1 
ATOM   5058 C CD2 . HIS B 1 168 ? 15.750  67.676  57.469  1.00 89.95  ? 263  HIS B CD2 1 
ATOM   5059 C CE1 . HIS B 1 168 ? 13.991  68.503  58.487  1.00 90.47  ? 263  HIS B CE1 1 
ATOM   5060 N NE2 . HIS B 1 168 ? 14.533  67.384  58.037  1.00 92.28  ? 263  HIS B NE2 1 
ATOM   5061 N N   . ILE B 1 169 ? 17.867  72.321  54.847  1.00 79.94  ? 264  ILE B N   1 
ATOM   5062 C CA  . ILE B 1 169 ? 18.758  73.126  54.019  1.00 83.08  ? 264  ILE B CA  1 
ATOM   5063 C C   . ILE B 1 169 ? 19.851  73.723  54.896  1.00 85.25  ? 264  ILE B C   1 
ATOM   5064 O O   . ILE B 1 169 ? 19.605  74.650  55.670  1.00 86.02  ? 264  ILE B O   1 
ATOM   5065 C CB  . ILE B 1 169 ? 17.982  74.219  53.277  1.00 82.64  ? 264  ILE B CB  1 
ATOM   5066 C CG1 . ILE B 1 169 ? 17.073  73.588  52.220  1.00 78.25  ? 264  ILE B CG1 1 
ATOM   5067 C CG2 . ILE B 1 169 ? 18.934  75.230  52.659  1.00 80.13  ? 264  ILE B CG2 1 
ATOM   5068 C CD1 . ILE B 1 169 ? 16.114  74.554  51.580  1.00 76.47  ? 264  ILE B CD1 1 
ATOM   5069 N N   . ARG B 1 170 ? 21.065  73.187  54.774  1.00 85.21  ? 265  ARG B N   1 
ATOM   5070 C CA  . ARG B 1 170 ? 22.218  73.807  55.413  1.00 86.22  ? 265  ARG B CA  1 
ATOM   5071 C C   . ARG B 1 170 ? 22.723  74.996  54.603  1.00 88.26  ? 265  ARG B C   1 
ATOM   5072 O O   . ARG B 1 170 ? 23.179  75.989  55.182  1.00 89.32  ? 265  ARG B O   1 
ATOM   5073 C CB  . ARG B 1 170 ? 23.328  72.769  55.602  1.00 88.59  ? 265  ARG B CB  1 
ATOM   5074 C CG  . ARG B 1 170 ? 24.085  72.873  56.919  1.00 95.86  ? 265  ARG B CG  1 
ATOM   5075 C CD  . ARG B 1 170 ? 23.986  71.574  57.714  1.00 97.02  ? 265  ARG B CD  1 
ATOM   5076 N NE  . ARG B 1 170 ? 24.928  71.545  58.828  1.00 93.77  ? 265  ARG B NE  1 
ATOM   5077 N N   . LYS B 1 171 ? 22.629  74.917  53.274  1.00 87.60  ? 266  LYS B N   1 
ATOM   5078 C CA  . LYS B 1 171 ? 22.995  75.995  52.363  1.00 85.30  ? 266  LYS B CA  1 
ATOM   5079 C C   . LYS B 1 171 ? 22.180  75.847  51.085  1.00 81.22  ? 266  LYS B C   1 
ATOM   5080 O O   . LYS B 1 171 ? 21.764  74.744  50.726  1.00 78.28  ? 266  LYS B O   1 
ATOM   5081 C CB  . LYS B 1 171 ? 24.495  75.980  52.036  1.00 89.29  ? 266  LYS B CB  1 
ATOM   5082 C CG  . LYS B 1 171 ? 25.376  76.586  53.120  1.00 94.79  ? 266  LYS B CG  1 
ATOM   5083 C CD  . LYS B 1 171 ? 26.755  75.938  53.158  1.00 98.08  ? 266  LYS B CD  1 
ATOM   5084 C CE  . LYS B 1 171 ? 27.841  76.895  52.703  1.00 100.96 ? 266  LYS B CE  1 
ATOM   5085 N NZ  . LYS B 1 171 ? 29.034  76.869  53.595  1.00 100.68 ? 266  LYS B NZ  1 
ATOM   5086 N N   . ILE B 1 172 ? 21.961  76.968  50.401  1.00 83.66  ? 267  ILE B N   1 
ATOM   5087 C CA  . ILE B 1 172 ? 21.298  76.950  49.101  1.00 77.87  ? 267  ILE B CA  1 
ATOM   5088 C C   . ILE B 1 172 ? 21.807  78.102  48.242  1.00 80.89  ? 267  ILE B C   1 
ATOM   5089 O O   . ILE B 1 172 ? 21.739  79.273  48.635  1.00 81.73  ? 267  ILE B O   1 
ATOM   5090 C CB  . ILE B 1 172 ? 19.765  77.005  49.238  1.00 75.39  ? 267  ILE B CB  1 
ATOM   5091 C CG1 . ILE B 1 172 ? 19.135  77.317  47.880  1.00 70.76  ? 267  ILE B CG1 1 
ATOM   5092 C CG2 . ILE B 1 172 ? 19.337  78.034  50.301  1.00 75.41  ? 267  ILE B CG2 1 
ATOM   5093 C CD1 . ILE B 1 172 ? 17.671  76.965  47.778  1.00 72.46  ? 267  ILE B CD1 1 
ATOM   5094 N N   . PHE B 1 173 ? 22.315  77.776  47.059  1.00 79.10  ? 268  PHE B N   1 
ATOM   5095 C CA  . PHE B 1 173 ? 22.788  78.763  46.103  1.00 78.43  ? 268  PHE B CA  1 
ATOM   5096 C C   . PHE B 1 173 ? 22.039  78.573  44.793  1.00 73.87  ? 268  PHE B C   1 
ATOM   5097 O O   . PHE B 1 173 ? 21.595  77.468  44.476  1.00 72.73  ? 268  PHE B O   1 
ATOM   5098 C CB  . PHE B 1 173 ? 24.301  78.634  45.881  1.00 80.25  ? 268  PHE B CB  1 
ATOM   5099 C CG  . PHE B 1 173 ? 25.119  78.721  47.149  1.00 84.44  ? 268  PHE B CG  1 
ATOM   5100 C CD1 . PHE B 1 173 ? 25.167  79.897  47.885  1.00 86.94  ? 268  PHE B CD1 1 
ATOM   5101 C CD2 . PHE B 1 173 ? 25.858  77.633  47.590  1.00 85.47  ? 268  PHE B CD2 1 
ATOM   5102 C CE1 . PHE B 1 173 ? 25.928  79.981  49.045  1.00 89.39  ? 268  PHE B CE1 1 
ATOM   5103 C CE2 . PHE B 1 173 ? 26.619  77.712  48.749  1.00 92.02  ? 268  PHE B CE2 1 
ATOM   5104 C CZ  . PHE B 1 173 ? 26.653  78.887  49.477  1.00 92.08  ? 268  PHE B CZ  1 
ATOM   5105 N N   . CYS B 1 174 ? 21.887  79.647  44.029  1.00 72.57  ? 269  CYS B N   1 
ATOM   5106 C CA  . CYS B 1 174 ? 21.165  79.592  42.761  1.00 71.91  ? 269  CYS B CA  1 
ATOM   5107 C C   . CYS B 1 174 ? 22.139  79.807  41.608  1.00 70.42  ? 269  CYS B C   1 
ATOM   5108 O O   . CYS B 1 174 ? 22.753  80.876  41.498  1.00 73.12  ? 269  CYS B O   1 
ATOM   5109 C CB  . CYS B 1 174 ? 20.042  80.628  42.727  1.00 70.11  ? 269  CYS B CB  1 
ATOM   5110 S SG  . CYS B 1 174 ? 19.211  80.743  41.133  1.00 67.41  ? 269  CYS B SG  1 
ATOM   5111 N N   . ILE B 1 175 ? 22.278  78.796  40.749  1.00 66.68  ? 270  ILE B N   1 
ATOM   5112 C CA  . ILE B 1 175 ? 23.225  78.902  39.644  1.00 66.28  ? 270  ILE B CA  1 
ATOM   5113 C C   . ILE B 1 175 ? 22.570  79.372  38.352  1.00 63.68  ? 270  ILE B C   1 
ATOM   5114 O O   . ILE B 1 175 ? 23.271  79.852  37.451  1.00 61.00  ? 270  ILE B O   1 
ATOM   5115 C CB  . ILE B 1 175 ? 23.949  77.570  39.387  1.00 65.74  ? 270  ILE B CB  1 
ATOM   5116 C CG1 . ILE B 1 175 ? 22.963  76.498  38.931  1.00 64.26  ? 270  ILE B CG1 1 
ATOM   5117 C CG2 . ILE B 1 175 ? 24.675  77.122  40.635  1.00 66.77  ? 270  ILE B CG2 1 
ATOM   5118 C CD1 . ILE B 1 175 ? 23.640  75.269  38.388  1.00 63.76  ? 270  ILE B CD1 1 
ATOM   5119 N N   . SER B 1 176 ? 21.250  79.261  38.234  1.00 62.97  ? 271  SER B N   1 
ATOM   5120 C CA  . SER B 1 176 ? 20.539  79.757  37.061  1.00 61.54  ? 271  SER B CA  1 
ATOM   5121 C C   . SER B 1 176 ? 19.172  80.245  37.513  1.00 62.89  ? 271  SER B C   1 
ATOM   5122 O O   . SER B 1 176 ? 18.333  79.457  37.962  1.00 62.15  ? 271  SER B O   1 
ATOM   5123 C CB  . SER B 1 176 ? 20.407  78.686  35.983  1.00 59.94  ? 271  SER B CB  1 
ATOM   5124 O OG  . SER B 1 176 ? 19.759  79.209  34.840  1.00 57.81  ? 271  SER B OG  1 
ATOM   5125 N N   . LYS B 1 177 ? 18.953  81.543  37.394  1.00 64.65  ? 272  LYS B N   1 
ATOM   5126 C CA  . LYS B 1 177 ? 17.724  82.174  37.836  1.00 65.56  ? 272  LYS B CA  1 
ATOM   5127 C C   . LYS B 1 177 ? 16.786  82.327  36.648  1.00 62.42  ? 272  LYS B C   1 
ATOM   5128 O O   . LYS B 1 177 ? 17.190  82.836  35.597  1.00 61.19  ? 272  LYS B O   1 
ATOM   5129 C CB  . LYS B 1 177 ? 18.030  83.532  38.462  1.00 67.01  ? 272  LYS B CB  1 
ATOM   5130 C CG  . LYS B 1 177 ? 16.815  84.373  38.797  1.00 70.74  ? 272  LYS B CG  1 
ATOM   5131 C CD  . LYS B 1 177 ? 17.238  85.754  39.274  1.00 75.50  ? 272  LYS B CD  1 
ATOM   5132 C CE  . LYS B 1 177 ? 16.411  86.841  38.606  1.00 81.45  ? 272  LYS B CE  1 
ATOM   5133 N NZ  . LYS B 1 177 ? 14.947  86.606  38.789  1.00 81.86  ? 272  LYS B NZ  1 
ATOM   5134 N N   . THR B 1 178 ? 15.545  81.864  36.807  1.00 63.82  ? 273  THR B N   1 
ATOM   5135 C CA  . THR B 1 178 ? 14.523  82.128  35.801  1.00 63.45  ? 273  THR B CA  1 
ATOM   5136 C C   . THR B 1 178 ? 14.504  83.619  35.484  1.00 63.66  ? 273  THR B C   1 
ATOM   5137 O O   . THR B 1 178 ? 14.445  84.449  36.387  1.00 66.00  ? 273  THR B O   1 
ATOM   5138 C CB  . THR B 1 178 ? 13.150  81.672  36.309  1.00 60.61  ? 273  THR B CB  1 
ATOM   5139 O OG1 . THR B 1 178 ? 13.155  80.255  36.529  1.00 63.91  ? 273  THR B OG1 1 
ATOM   5140 C CG2 . THR B 1 178 ? 12.072  82.009  35.297  1.00 58.76  ? 273  THR B CG2 1 
ATOM   5141 N N   . ALA B 1 179 ? 14.595  83.958  34.202  1.00 64.73  ? 274  ALA B N   1 
ATOM   5142 C CA  . ALA B 1 179 ? 14.688  85.360  33.810  1.00 67.33  ? 274  ALA B CA  1 
ATOM   5143 C C   . ALA B 1 179 ? 13.342  85.976  33.456  1.00 66.09  ? 274  ALA B C   1 
ATOM   5144 O O   . ALA B 1 179 ? 13.205  87.202  33.486  1.00 67.87  ? 274  ALA B O   1 
ATOM   5145 C CB  . ALA B 1 179 ? 15.634  85.514  32.612  1.00 61.75  ? 274  ALA B CB  1 
ATOM   5146 N N   . LYS B 1 180 ? 12.353  85.158  33.131  1.00 67.12  ? 275  LYS B N   1 
ATOM   5147 C CA  . LYS B 1 180 ? 11.122  85.614  32.511  1.00 67.65  ? 275  LYS B CA  1 
ATOM   5148 C C   . LYS B 1 180 ? 9.948   84.861  33.123  1.00 67.36  ? 275  LYS B C   1 
ATOM   5149 O O   . LYS B 1 180 ? 10.077  83.696  33.505  1.00 65.51  ? 275  LYS B O   1 
ATOM   5150 C CB  . LYS B 1 180 ? 11.191  85.382  30.991  1.00 66.50  ? 275  LYS B CB  1 
ATOM   5151 C CG  . LYS B 1 180 ? 9.913   85.664  30.249  1.00 70.81  ? 275  LYS B CG  1 
ATOM   5152 C CD  . LYS B 1 180 ? 9.837   84.823  28.992  1.00 69.97  ? 275  LYS B CD  1 
ATOM   5153 C CE  . LYS B 1 180 ? 10.383  85.561  27.806  1.00 73.97  ? 275  LYS B CE  1 
ATOM   5154 N NZ  . LYS B 1 180 ? 9.350   85.696  26.755  1.00 76.97  ? 275  LYS B NZ  1 
ATOM   5155 N N   . GLU B 1 181 ? 8.805   85.537  33.219  1.00 67.15  ? 276  GLU B N   1 
ATOM   5156 C CA  . GLU B 1 181 ? 7.589   84.886  33.691  1.00 70.11  ? 276  GLU B CA  1 
ATOM   5157 C C   . GLU B 1 181 ? 7.212   83.725  32.771  1.00 68.93  ? 276  GLU B C   1 
ATOM   5158 O O   . GLU B 1 181 ? 7.309   83.818  31.544  1.00 65.73  ? 276  GLU B O   1 
ATOM   5159 C CB  . GLU B 1 181 ? 6.447   85.898  33.762  1.00 70.18  ? 276  GLU B CB  1 
ATOM   5160 C CG  . GLU B 1 181 ? 5.289   85.474  34.643  1.00 76.95  ? 276  GLU B CG  1 
ATOM   5161 C CD  . GLU B 1 181 ? 5.587   85.663  36.115  1.00 83.54  ? 276  GLU B CD  1 
ATOM   5162 O OE1 . GLU B 1 181 ? 6.353   86.592  36.450  1.00 86.51  ? 276  GLU B OE1 1 
ATOM   5163 O OE2 . GLU B 1 181 ? 5.058   84.884  36.938  1.00 85.48  ? 276  GLU B OE2 1 
ATOM   5164 N N   . LEU B 1 182 ? 6.785   82.620  33.370  1.00 63.81  ? 277  LEU B N   1 
ATOM   5165 C CA  . LEU B 1 182 ? 6.469   81.444  32.579  1.00 66.85  ? 277  LEU B CA  1 
ATOM   5166 C C   . LEU B 1 182 ? 5.211   81.679  31.740  1.00 61.97  ? 277  LEU B C   1 
ATOM   5167 O O   . LEU B 1 182 ? 4.328   82.438  32.130  1.00 65.40  ? 277  LEU B O   1 
ATOM   5168 C CB  . LEU B 1 182 ? 6.286   80.228  33.485  1.00 62.49  ? 277  LEU B CB  1 
ATOM   5169 C CG  . LEU B 1 182 ? 7.571   79.410  33.655  1.00 64.30  ? 277  LEU B CG  1 
ATOM   5170 C CD1 . LEU B 1 182 ? 8.338   79.832  34.900  1.00 63.81  ? 277  LEU B CD1 1 
ATOM   5171 C CD2 . LEU B 1 182 ? 7.257   77.927  33.678  1.00 63.23  ? 277  LEU B CD2 1 
ATOM   5172 N N   . PRO B 1 183 ? 5.112   81.040  30.575  1.00 63.27  ? 278  PRO B N   1 
ATOM   5173 C CA  . PRO B 1 183 ? 3.900   81.210  29.758  1.00 61.36  ? 278  PRO B CA  1 
ATOM   5174 C C   . PRO B 1 183 ? 2.664   80.624  30.414  1.00 62.32  ? 278  PRO B C   1 
ATOM   5175 O O   . PRO B 1 183 ? 1.542   81.037  30.098  1.00 63.39  ? 278  PRO B O   1 
ATOM   5176 C CB  . PRO B 1 183 ? 4.254   80.476  28.459  1.00 58.91  ? 278  PRO B CB  1 
ATOM   5177 C CG  . PRO B 1 183 ? 5.285   79.471  28.874  1.00 57.85  ? 278  PRO B CG  1 
ATOM   5178 C CD  . PRO B 1 183 ? 6.084   80.130  29.948  1.00 59.15  ? 278  PRO B CD  1 
ATOM   5179 N N   . PHE B 1 184 ? 2.849   79.658  31.306  1.00 59.67  ? 279  PHE B N   1 
ATOM   5180 C CA  . PHE B 1 184 ? 1.795   79.099  32.138  1.00 59.31  ? 279  PHE B CA  1 
ATOM   5181 C C   . PHE B 1 184 ? 2.488   78.438  33.319  1.00 59.44  ? 279  PHE B C   1 
ATOM   5182 O O   . PHE B 1 184 ? 3.704   78.234  33.307  1.00 58.43  ? 279  PHE B O   1 
ATOM   5183 C CB  . PHE B 1 184 ? 0.928   78.101  31.363  1.00 59.44  ? 279  PHE B CB  1 
ATOM   5184 C CG  . PHE B 1 184 ? 1.716   77.141  30.508  1.00 58.82  ? 279  PHE B CG  1 
ATOM   5185 C CD1 . PHE B 1 184 ? 1.738   77.285  29.129  1.00 57.43  ? 279  PHE B CD1 1 
ATOM   5186 C CD2 . PHE B 1 184 ? 2.431   76.099  31.082  1.00 55.71  ? 279  PHE B CD2 1 
ATOM   5187 C CE1 . PHE B 1 184 ? 2.447   76.419  28.336  1.00 56.57  ? 279  PHE B CE1 1 
ATOM   5188 C CE2 . PHE B 1 184 ? 3.155   75.218  30.291  1.00 54.49  ? 279  PHE B CE2 1 
ATOM   5189 C CZ  . PHE B 1 184 ? 3.162   75.377  28.917  1.00 57.36  ? 279  PHE B CZ  1 
ATOM   5190 N N   . LEU B 1 185 ? 1.708   78.103  34.339  1.00 59.19  ? 280  LEU B N   1 
ATOM   5191 C CA  . LEU B 1 185 ? 2.256   77.471  35.532  1.00 59.98  ? 280  LEU B CA  1 
ATOM   5192 C C   . LEU B 1 185 ? 2.347   75.961  35.348  1.00 58.20  ? 280  LEU B C   1 
ATOM   5193 O O   . LEU B 1 185 ? 1.420   75.334  34.829  1.00 59.45  ? 280  LEU B O   1 
ATOM   5194 C CB  . LEU B 1 185 ? 1.390   77.796  36.744  1.00 55.40  ? 280  LEU B CB  1 
ATOM   5195 C CG  . LEU B 1 185 ? 1.186   79.288  36.999  1.00 61.10  ? 280  LEU B CG  1 
ATOM   5196 C CD1 . LEU B 1 185 ? -0.060  79.541  37.864  1.00 57.15  ? 280  LEU B CD1 1 
ATOM   5197 C CD2 . LEU B 1 185 ? 2.420   79.865  37.664  1.00 59.01  ? 280  LEU B CD2 1 
ATOM   5198 N N   . LEU B 1 186 ? 3.469   75.377  35.784  1.00 55.51  ? 281  LEU B N   1 
ATOM   5199 C CA  . LEU B 1 186 ? 3.599   73.923  35.717  1.00 57.53  ? 281  LEU B CA  1 
ATOM   5200 C C   . LEU B 1 186 ? 2.527   73.229  36.550  1.00 58.95  ? 281  LEU B C   1 
ATOM   5201 O O   . LEU B 1 186 ? 2.123   72.107  36.228  1.00 57.47  ? 281  LEU B O   1 
ATOM   5202 C CB  . LEU B 1 186 ? 4.996   73.481  36.161  1.00 55.71  ? 281  LEU B CB  1 
ATOM   5203 C CG  . LEU B 1 186 ? 6.044   73.630  35.051  1.00 59.97  ? 281  LEU B CG  1 
ATOM   5204 C CD1 . LEU B 1 186 ? 7.403   73.086  35.476  1.00 60.95  ? 281  LEU B CD1 1 
ATOM   5205 C CD2 . LEU B 1 186 ? 5.560   72.932  33.795  1.00 54.48  ? 281  LEU B CD2 1 
ATOM   5206 N N   . LYS B 1 187 ? 2.050   73.874  37.613  1.00 57.39  ? 282  LYS B N   1 
ATOM   5207 C CA  . LYS B 1 187 ? 0.953   73.290  38.375  1.00 56.52  ? 282  LYS B CA  1 
ATOM   5208 C C   . LYS B 1 187 ? -0.289  73.159  37.506  1.00 60.50  ? 282  LYS B C   1 
ATOM   5209 O O   . LYS B 1 187 ? -0.989  72.141  37.549  1.00 61.54  ? 282  LYS B O   1 
ATOM   5210 C CB  . LYS B 1 187 ? 0.665   74.139  39.612  1.00 58.29  ? 282  LYS B CB  1 
ATOM   5211 N N   . ASP B 1 188 ? -0.563  74.176  36.691  1.00 60.76  ? 283  ASP B N   1 
ATOM   5212 C CA  . ASP B 1 188 ? -1.686  74.109  35.768  1.00 57.58  ? 283  ASP B CA  1 
ATOM   5213 C C   . ASP B 1 188 ? -1.437  73.090  34.659  1.00 59.28  ? 283  ASP B C   1 
ATOM   5214 O O   . ASP B 1 188 ? -2.352  72.354  34.267  1.00 60.57  ? 283  ASP B O   1 
ATOM   5215 C CB  . ASP B 1 188 ? -1.949  75.498  35.187  1.00 58.65  ? 283  ASP B CB  1 
ATOM   5216 C CG  . ASP B 1 188 ? -2.541  76.458  36.216  1.00 63.88  ? 283  ASP B CG  1 
ATOM   5217 O OD1 . ASP B 1 188 ? -2.843  76.007  37.342  1.00 61.29  ? 283  ASP B OD1 1 
ATOM   5218 O OD2 . ASP B 1 188 ? -2.717  77.655  35.897  1.00 63.53  ? 283  ASP B OD2 1 
ATOM   5219 N N   . ALA B 1 189 ? -0.209  73.029  34.143  1.00 55.20  ? 284  ALA B N   1 
ATOM   5220 C CA  . ALA B 1 189 ? 0.070   72.163  33.000  1.00 58.24  ? 284  ALA B CA  1 
ATOM   5221 C C   . ALA B 1 189 ? 0.057   70.684  33.386  1.00 56.03  ? 284  ALA B C   1 
ATOM   5222 O O   . ALA B 1 189 ? -0.233  69.826  32.542  1.00 53.80  ? 284  ALA B O   1 
ATOM   5223 C CB  . ALA B 1 189 ? 1.412   72.546  32.373  1.00 56.71  ? 284  ALA B CB  1 
ATOM   5224 N N   . ASN B 1 190 ? 0.350   70.373  34.649  1.00 56.08  ? 285  ASN B N   1 
ATOM   5225 C CA  . ASN B 1 190 ? 0.394   68.999  35.132  1.00 56.74  ? 285  ASN B CA  1 
ATOM   5226 C C   . ASN B 1 190 ? -0.979  68.434  35.474  1.00 57.80  ? 285  ASN B C   1 
ATOM   5227 O O   . ASN B 1 190 ? -1.128  67.212  35.553  1.00 55.23  ? 285  ASN B O   1 
ATOM   5228 C CB  . ASN B 1 190 ? 1.282   68.918  36.376  1.00 55.80  ? 285  ASN B CB  1 
ATOM   5229 C CG  . ASN B 1 190 ? 2.727   68.608  36.039  1.00 54.49  ? 285  ASN B CG  1 
ATOM   5230 O OD1 . ASN B 1 190 ? 3.020   67.608  35.375  1.00 53.50  ? 285  ASN B OD1 1 
ATOM   5231 N ND2 . ASN B 1 190 ? 3.639   69.456  36.496  1.00 54.56  ? 285  ASN B ND2 1 
ATOM   5232 N N   . MET B 1 191 ? -1.979  69.282  35.676  1.00 57.65  ? 286  MET B N   1 
ATOM   5233 C CA  . MET B 1 191 ? -3.247  68.823  36.226  1.00 60.28  ? 286  MET B CA  1 
ATOM   5234 C C   . MET B 1 191 ? -4.081  68.093  35.185  1.00 59.68  ? 286  MET B C   1 
ATOM   5235 O O   . MET B 1 191 ? -4.064  68.430  33.997  1.00 62.79  ? 286  MET B O   1 
ATOM   5236 C CB  . MET B 1 191 ? -4.038  70.001  36.795  1.00 63.10  ? 286  MET B CB  1 
ATOM   5237 C CG  . MET B 1 191 ? -3.765  70.251  38.261  1.00 63.08  ? 286  MET B CG  1 
ATOM   5238 S SD  . MET B 1 191 ? -4.485  71.809  38.772  1.00 89.99  ? 286  MET B SD  1 
ATOM   5239 C CE  . MET B 1 191 ? -6.125  71.696  38.034  1.00 77.28  ? 286  MET B CE  1 
ATOM   5240 N N   . LYS B 1 192 ? -4.803  67.075  35.640  1.00 61.62  ? 287  LYS B N   1 
ATOM   5241 C CA  . LYS B 1 192 ? -5.736  66.374  34.774  1.00 64.74  ? 287  LYS B CA  1 
ATOM   5242 C C   . LYS B 1 192 ? -6.903  67.298  34.457  1.00 68.80  ? 287  LYS B C   1 
ATOM   5243 O O   . LYS B 1 192 ? -7.395  68.018  35.332  1.00 74.67  ? 287  LYS B O   1 
ATOM   5244 C CB  . LYS B 1 192 ? -6.207  65.083  35.450  1.00 61.93  ? 287  LYS B CB  1 
ATOM   5245 C CG  . LYS B 1 192 ? -7.304  64.343  34.723  1.00 67.71  ? 287  LYS B CG  1 
ATOM   5246 C CD  . LYS B 1 192 ? -7.468  62.933  35.264  1.00 69.10  ? 287  LYS B CD  1 
ATOM   5247 C CE  . LYS B 1 192 ? -7.159  62.862  36.747  1.00 73.71  ? 287  LYS B CE  1 
ATOM   5248 N NZ  . LYS B 1 192 ? -7.533  61.528  37.312  1.00 83.35  ? 287  LYS B NZ  1 
ATOM   5249 N N   . GLU B 1 193 ? -7.293  67.314  33.207  1.00 66.55  ? 288  GLU B N   1 
ATOM   5250 C CA  . GLU B 1 193 ? -8.319  68.206  32.764  1.00 76.83  ? 288  GLU B CA  1 
ATOM   5251 C C   . GLU B 1 193 ? -9.738  67.791  33.030  1.00 85.26  ? 288  GLU B C   1 
ATOM   5252 O O   . GLU B 1 193 ? -10.161 66.711  32.677  1.00 90.07  ? 288  GLU B O   1 
ATOM   5253 C CB  . GLU B 1 193 ? -8.179  68.464  31.275  1.00 81.31  ? 288  GLU B CB  1 
ATOM   5254 C CG  . GLU B 1 193 ? -6.948  69.255  30.883  1.00 80.59  ? 288  GLU B CG  1 
ATOM   5255 C CD  . GLU B 1 193 ? -6.870  69.504  29.395  1.00 83.35  ? 288  GLU B CD  1 
ATOM   5256 O OE1 . GLU B 1 193 ? -7.854  69.235  28.688  1.00 85.12  ? 288  GLU B OE1 1 
ATOM   5257 O OE2 . GLU B 1 193 ? -5.824  69.972  28.936  1.00 76.14  ? 288  GLU B OE2 1 
ATOM   5258 N N   . THR B 1 194 ? -10.461 68.689  33.669  1.00 86.49  ? 289  THR B N   1 
ATOM   5259 C CA  . THR B 1 194 ? -11.872 68.521  33.927  1.00 92.99  ? 289  THR B CA  1 
ATOM   5260 C C   . THR B 1 194 ? -12.551 69.449  32.936  1.00 96.51  ? 289  THR B C   1 
ATOM   5261 O O   . THR B 1 194 ? -12.009 70.448  32.496  1.00 96.01  ? 289  THR B O   1 
ATOM   5262 C CB  . THR B 1 194 ? -12.274 68.942  35.347  1.00 88.26  ? 289  THR B CB  1 
ATOM   5263 O OG1 . THR B 1 194 ? -12.411 70.358  35.411  1.00 88.64  ? 289  THR B OG1 1 
ATOM   5264 C CG2 . THR B 1 194 ? -11.240 68.527  36.350  1.00 85.22  ? 289  THR B CG2 1 
ATOM   5265 N N   . ASN B 1 195 ? -13.779 69.153  32.594  1.00 99.44  ? 290  ASN B N   1 
ATOM   5266 C CA  . ASN B 1 195 ? -14.481 70.007  31.660  1.00 101.06 ? 290  ASN B CA  1 
ATOM   5267 C C   . ASN B 1 195 ? -15.375 71.020  32.340  1.00 100.05 ? 290  ASN B C   1 
ATOM   5268 O O   . ASN B 1 195 ? -16.292 71.533  31.734  1.00 102.37 ? 290  ASN B O   1 
ATOM   5269 C CB  . ASN B 1 195 ? -15.233 69.207  30.617  1.00 105.63 ? 290  ASN B CB  1 
ATOM   5270 C CG  . ASN B 1 195 ? -14.301 68.470  29.701  1.00 108.18 ? 290  ASN B CG  1 
ATOM   5271 O OD1 . ASN B 1 195 ? -13.090 68.587  29.822  1.00 106.88 ? 290  ASN B OD1 1 
ATOM   5272 N ND2 . ASN B 1 195 ? -14.856 67.708  28.779  1.00 113.24 ? 290  ASN B ND2 1 
ATOM   5273 N N   . GLU B 1 196 ? -15.147 71.235  33.627  1.00 99.12  ? 291  GLU B N   1 
ATOM   5274 C CA  . GLU B 1 196 ? -15.867 72.221  34.389  1.00 101.15 ? 291  GLU B CA  1 
ATOM   5275 C C   . GLU B 1 196 ? -15.534 73.612  33.857  1.00 100.73 ? 291  GLU B C   1 
ATOM   5276 O O   . GLU B 1 196 ? -14.434 73.900  33.412  1.00 96.32  ? 291  GLU B O   1 
ATOM   5277 C CB  . GLU B 1 196 ? -15.493 72.152  35.868  1.00 99.54  ? 291  GLU B CB  1 
ATOM   5278 C CG  . GLU B 1 196 ? -15.612 70.786  36.508  1.00 99.92  ? 291  GLU B CG  1 
ATOM   5279 C CD  . GLU B 1 196 ? -17.003 70.206  36.407  1.00 105.86 ? 291  GLU B CD  1 
ATOM   5280 O OE1 . GLU B 1 196 ? -17.962 70.990  36.299  1.00 106.21 ? 291  GLU B OE1 1 
ATOM   5281 O OE2 . GLU B 1 196 ? -17.138 68.968  36.439  1.00 106.34 ? 291  GLU B OE2 1 
ATOM   5282 N N   . GLU B 1 197 ? -16.513 74.483  33.933  1.00 104.68 ? 292  GLU B N   1 
ATOM   5283 C CA  . GLU B 1 197 ? -16.367 75.857  33.481  1.00 107.33 ? 292  GLU B CA  1 
ATOM   5284 C C   . GLU B 1 197 ? -15.384 76.602  34.375  1.00 105.61 ? 292  GLU B C   1 
ATOM   5285 O O   . GLU B 1 197 ? -15.395 76.454  35.603  1.00 102.95 ? 292  GLU B O   1 
ATOM   5286 C CB  . GLU B 1 197 ? -17.720 76.564  33.461  1.00 112.83 ? 292  GLU B CB  1 
ATOM   5287 C CG  . GLU B 1 197 ? -18.628 76.091  32.340  1.00 119.34 ? 292  GLU B CG  1 
ATOM   5288 C CD  . GLU B 1 197 ? -19.704 77.101  32.005  1.00 127.17 ? 292  GLU B CD  1 
ATOM   5289 O OE1 . GLU B 1 197 ? -19.630 78.238  32.518  1.00 126.23 ? 292  GLU B OE1 1 
ATOM   5290 O OE2 . GLU B 1 197 ? -20.622 76.761  31.230  1.00 132.50 ? 292  GLU B OE2 1 
ATOM   5291 N N   . GLY B 1 198 ? -14.524 77.402  33.747  1.00 94.00  ? 293  GLY B N   1 
ATOM   5292 C CA  . GLY B 1 198 ? -13.465 78.084  34.458  1.00 86.60  ? 293  GLY B CA  1 
ATOM   5293 C C   . GLY B 1 198 ? -12.371 77.181  34.971  1.00 89.04  ? 293  GLY B C   1 
ATOM   5294 O O   . GLY B 1 198 ? -11.511 77.644  35.727  1.00 88.14  ? 293  GLY B O   1 
ATOM   5295 N N   . SER B 1 199 ? -12.378 75.906  34.586  1.00 88.22  ? 294  SER B N   1 
ATOM   5296 C CA  . SER B 1 199 ? -11.391 74.965  35.083  1.00 87.19  ? 294  SER B CA  1 
ATOM   5297 C C   . SER B 1 199 ? -10.018 75.270  34.496  1.00 81.43  ? 294  SER B C   1 
ATOM   5298 O O   . SER B 1 199 ? -9.879  75.897  33.441  1.00 80.65  ? 294  SER B O   1 
ATOM   5299 C CB  . SER B 1 199 ? -11.783 73.526  34.742  1.00 88.17  ? 294  SER B CB  1 
ATOM   5300 O OG  . SER B 1 199 ? -11.763 73.303  33.343  1.00 85.30  ? 294  SER B OG  1 
ATOM   5301 N N   . ILE B 1 200 ? -8.993  74.809  35.213  1.00 76.48  ? 295  ILE B N   1 
ATOM   5302 C CA  . ILE B 1 200 ? -7.621  74.933  34.746  1.00 76.15  ? 295  ILE B CA  1 
ATOM   5303 C C   . ILE B 1 200 ? -7.451  74.142  33.455  1.00 76.42  ? 295  ILE B C   1 
ATOM   5304 O O   . ILE B 1 200 ? -7.753  72.943  33.401  1.00 74.04  ? 295  ILE B O   1 
ATOM   5305 C CB  . ILE B 1 200 ? -6.657  74.439  35.833  1.00 74.78  ? 295  ILE B CB  1 
ATOM   5306 C CG1 . ILE B 1 200 ? -6.884  75.181  37.163  1.00 74.39  ? 295  ILE B CG1 1 
ATOM   5307 C CG2 . ILE B 1 200 ? -5.231  74.540  35.351  1.00 72.40  ? 295  ILE B CG2 1 
ATOM   5308 C CD1 . ILE B 1 200 ? -6.281  76.576  37.227  1.00 72.17  ? 295  ILE B CD1 1 
ATOM   5309 N N   . LYS B 1 201 ? -6.952  74.805  32.408  1.00 71.75  ? 296  LYS B N   1 
ATOM   5310 C CA  . LYS B 1 201 ? -6.806  74.160  31.099  1.00 71.37  ? 296  LYS B CA  1 
ATOM   5311 C C   . LYS B 1 201 ? -5.715  74.887  30.324  1.00 67.56  ? 296  LYS B C   1 
ATOM   5312 O O   . LYS B 1 201 ? -5.886  76.059  29.976  1.00 70.62  ? 296  LYS B O   1 
ATOM   5313 C CB  . LYS B 1 201 ? -8.133  74.191  30.339  1.00 73.36  ? 296  LYS B CB  1 
ATOM   5314 C CG  . LYS B 1 201 ? -8.384  73.012  29.404  1.00 75.09  ? 296  LYS B CG  1 
ATOM   5315 C CD  . LYS B 1 201 ? -7.561  73.092  28.124  1.00 71.96  ? 296  LYS B CD  1 
ATOM   5316 N N   . VAL B 1 202 ? -4.610  74.204  30.049  1.00 65.44  ? 297  VAL B N   1 
ATOM   5317 C CA  . VAL B 1 202 ? -3.542  74.767  29.231  1.00 62.95  ? 297  VAL B CA  1 
ATOM   5318 C C   . VAL B 1 202 ? -3.694  74.224  27.816  1.00 61.81  ? 297  VAL B C   1 
ATOM   5319 O O   . VAL B 1 202 ? -3.561  73.018  27.586  1.00 60.04  ? 297  VAL B O   1 
ATOM   5320 C CB  . VAL B 1 202 ? -2.155  74.463  29.815  1.00 60.66  ? 297  VAL B CB  1 
ATOM   5321 C CG1 . VAL B 1 202 ? -1.094  75.216  29.048  1.00 59.69  ? 297  VAL B CG1 1 
ATOM   5322 C CG2 . VAL B 1 202 ? -2.116  74.873  31.272  1.00 60.39  ? 297  VAL B CG2 1 
ATOM   5323 N N   . ASN B 1 203 ? -4.036  75.097  26.896  1.00 61.58  ? 298  ASN B N   1 
ATOM   5324 C CA  . ASN B 1 203 ? -4.277  74.747  25.518  1.00 62.70  ? 298  ASN B CA  1 
ATOM   5325 C C   . ASN B 1 203 ? -3.154  74.128  24.721  1.00 58.99  ? 298  ASN B C   1 
ATOM   5326 O O   . ASN B 1 203 ? -2.015  74.456  24.908  1.00 58.03  ? 298  ASN B O   1 
ATOM   5327 C CB  . ASN B 1 203 ? -4.719  75.982  24.785  1.00 66.75  ? 298  ASN B CB  1 
ATOM   5328 C CG  . ASN B 1 203 ? -6.163  75.944  24.449  1.00 76.15  ? 298  ASN B CG  1 
ATOM   5329 O OD1 . ASN B 1 203 ? -6.662  74.927  23.987  1.00 77.05  ? 298  ASN B OD1 1 
ATOM   5330 N ND2 . ASN B 1 203 ? -6.854  77.039  24.682  1.00 69.41  ? 298  ASN B ND2 1 
ATOM   5331 N N   . GLN B 1 204 ? -3.506  73.259  23.789  1.00 58.78  ? 299  GLN B N   1 
ATOM   5332 C CA  . GLN B 1 204 ? -2.522  72.588  22.952  1.00 60.46  ? 299  GLN B CA  1 
ATOM   5333 C C   . GLN B 1 204 ? -1.676  73.586  22.236  1.00 57.74  ? 299  GLN B C   1 
ATOM   5334 O O   . GLN B 1 204 ? -0.493  73.472  22.191  1.00 58.15  ? 299  GLN B O   1 
ATOM   5335 C CB  . GLN B 1 204 ? -3.181  71.679  21.940  1.00 58.90  ? 299  GLN B CB  1 
ATOM   5336 C CG  . GLN B 1 204 ? -2.194  71.059  20.980  1.00 58.69  ? 299  GLN B CG  1 
ATOM   5337 C CD  . GLN B 1 204 ? -2.824  70.076  20.042  1.00 57.94  ? 299  GLN B CD  1 
ATOM   5338 O OE1 . GLN B 1 204 ? -3.395  70.450  19.051  1.00 63.25  ? 299  GLN B OE1 1 
ATOM   5339 N NE2 . GLN B 1 204 ? -2.703  68.819  20.348  1.00 51.63  ? 299  GLN B NE2 1 
ATOM   5340 N N   . ASP B 1 205 ? -2.313  74.630  21.768  1.00 59.51  ? 300  ASP B N   1 
ATOM   5341 C CA  . ASP B 1 205 ? -1.666  75.684  21.049  1.00 60.64  ? 300  ASP B CA  1 
ATOM   5342 C C   . ASP B 1 205 ? -0.606  76.341  21.889  1.00 58.36  ? 300  ASP B C   1 
ATOM   5343 O O   . ASP B 1 205 ? 0.496   76.535  21.451  1.00 56.07  ? 300  ASP B O   1 
ATOM   5344 C CB  . ASP B 1 205 ? -2.725  76.719  20.791  1.00 64.37  ? 300  ASP B CB  1 
ATOM   5345 C CG  . ASP B 1 205 ? -2.772  77.143  19.406  1.00 67.91  ? 300  ASP B CG  1 
ATOM   5346 O OD1 . ASP B 1 205 ? -2.459  76.348  18.532  1.00 79.58  ? 300  ASP B OD1 1 
ATOM   5347 O OD2 . ASP B 1 205 ? -3.141  78.289  19.184  1.00 67.62  ? 300  ASP B OD2 1 
ATOM   5348 N N   . ASN B 1 206 ? -0.929  76.615  23.130  1.00 56.15  ? 301  ASN B N   1 
ATOM   5349 C CA  . ASN B 1 206 ? -0.013  77.265  24.022  1.00 55.01  ? 301  ASN B CA  1 
ATOM   5350 C C   . ASN B 1 206 ? 1.117   76.352  24.402  1.00 56.37  ? 301  ASN B C   1 
ATOM   5351 O O   . ASN B 1 206 ? 2.252   76.760  24.464  1.00 55.38  ? 301  ASN B O   1 
ATOM   5352 C CB  . ASN B 1 206 ? -0.759  77.755  25.254  1.00 63.91  ? 301  ASN B CB  1 
ATOM   5353 C CG  . ASN B 1 206 ? -0.194  79.026  25.797  1.00 69.35  ? 301  ASN B CG  1 
ATOM   5354 O OD1 . ASN B 1 206 ? 0.181   79.104  26.944  1.00 72.24  ? 301  ASN B OD1 1 
ATOM   5355 N ND2 . ASN B 1 206 ? -0.111  80.027  24.957  1.00 71.48  ? 301  ASN B ND2 1 
ATOM   5356 N N   . ARG B 1 207 ? 0.778   75.120  24.727  1.00 56.27  ? 302  ARG B N   1 
ATOM   5357 C CA  . ARG B 1 207 ? 1.776   74.097  25.019  1.00 54.19  ? 302  ARG B CA  1 
ATOM   5358 C C   . ARG B 1 207 ? 2.793   73.976  23.883  1.00 53.98  ? 302  ARG B C   1 
ATOM   5359 O O   . ARG B 1 207 ? 4.005   73.980  24.115  1.00 50.31  ? 302  ARG B O   1 
ATOM   5360 C CB  . ARG B 1 207 ? 1.079   72.756  25.277  1.00 52.21  ? 302  ARG B CB  1 
ATOM   5361 C CG  . ARG B 1 207 ? 0.203   72.743  26.536  1.00 54.61  ? 302  ARG B CG  1 
ATOM   5362 C CD  . ARG B 1 207 ? -0.528  71.419  26.734  1.00 53.18  ? 302  ARG B CD  1 
ATOM   5363 N NE  . ARG B 1 207 ? -1.222  71.356  28.021  1.00 57.94  ? 302  ARG B NE  1 
ATOM   5364 C CZ  . ARG B 1 207 ? -0.744  70.752  29.102  1.00 54.40  ? 302  ARG B CZ  1 
ATOM   5365 N NH1 . ARG B 1 207 ? 0.449   70.173  29.104  1.00 51.58  ? 302  ARG B NH1 1 
ATOM   5366 N NH2 . ARG B 1 207 ? -1.488  70.707  30.203  1.00 56.02  ? 302  ARG B NH2 1 
ATOM   5367 N N   . LEU B 1 208 ? 2.324   73.848  22.644  1.00 51.83  ? 303  LEU B N   1 
ATOM   5368 C CA  . LEU B 1 208 ? 3.270   73.576  21.564  1.00 53.69  ? 303  LEU B CA  1 
ATOM   5369 C C   . LEU B 1 208 ? 4.076   74.817  21.192  1.00 55.56  ? 303  LEU B C   1 
ATOM   5370 O O   . LEU B 1 208 ? 5.237   74.692  20.779  1.00 53.97  ? 303  LEU B O   1 
ATOM   5371 C CB  . LEU B 1 208 ? 2.538   73.004  20.346  1.00 51.55  ? 303  LEU B CB  1 
ATOM   5372 C CG  . LEU B 1 208 ? 1.885   71.622  20.517  1.00 53.06  ? 303  LEU B CG  1 
ATOM   5373 C CD1 . LEU B 1 208 ? 1.230   71.190  19.216  1.00 52.59  ? 303  LEU B CD1 1 
ATOM   5374 C CD2 . LEU B 1 208 ? 2.879   70.568  20.987  1.00 46.95  ? 303  LEU B CD2 1 
ATOM   5375 N N   . ASN B 1 209 ? 3.509   75.992  21.400  1.00 53.12  ? 304  ASN B N   1 
ATOM   5376 C CA  . ASN B 1 209 ? 4.243   77.216  21.155  1.00 56.73  ? 304  ASN B CA  1 
ATOM   5377 C C   . ASN B 1 209 ? 5.254   77.428  22.248  1.00 57.38  ? 304  ASN B C   1 
ATOM   5378 O O   . ASN B 1 209 ? 6.144   78.223  22.108  1.00 59.82  ? 304  ASN B O   1 
ATOM   5379 C CB  . ASN B 1 209 ? 3.338   78.431  21.075  1.00 54.73  ? 304  ASN B CB  1 
ATOM   5380 C CG  . ASN B 1 209 ? 2.422   78.398  19.897  1.00 56.97  ? 304  ASN B CG  1 
ATOM   5381 O OD1 . ASN B 1 209 ? 2.611   77.646  18.977  1.00 58.17  ? 304  ASN B OD1 1 
ATOM   5382 N ND2 . ASN B 1 209 ? 1.411   79.217  19.931  1.00 58.75  ? 304  ASN B ND2 1 
ATOM   5383 N N   . ASN B 1 210 ? 5.109   76.723  23.351  1.00 53.31  ? 305  ASN B N   1 
ATOM   5384 C CA  . ASN B 1 210 ? 6.034   76.838  24.443  1.00 52.51  ? 305  ASN B CA  1 
ATOM   5385 C C   . ASN B 1 210 ? 6.521   75.472  24.850  1.00 53.91  ? 305  ASN B C   1 
ATOM   5386 O O   . ASN B 1 210 ? 6.680   75.186  26.009  1.00 55.62  ? 305  ASN B O   1 
ATOM   5387 C CB  . ASN B 1 210 ? 5.360   77.518  25.612  1.00 58.28  ? 305  ASN B CB  1 
ATOM   5388 C CG  . ASN B 1 210 ? 5.096   78.984  25.360  1.00 57.87  ? 305  ASN B CG  1 
ATOM   5389 O OD1 . ASN B 1 210 ? 5.948   79.806  25.569  1.00 55.87  ? 305  ASN B OD1 1 
ATOM   5390 N ND2 . ASN B 1 210 ? 3.927   79.293  24.892  1.00 56.18  ? 305  ASN B ND2 1 
ATOM   5391 N N   . ARG B 1 211 ? 6.802   74.647  23.861  1.00 51.50  ? 306  ARG B N   1 
ATOM   5392 C CA  . ARG B 1 211 ? 7.227   73.281  24.069  1.00 49.83  ? 306  ARG B CA  1 
ATOM   5393 C C   . ARG B 1 211 ? 8.300   73.045  25.083  1.00 49.66  ? 306  ARG B C   1 
ATOM   5394 O O   . ARG B 1 211 ? 8.298   72.051  25.727  1.00 50.03  ? 306  ARG B O   1 
ATOM   5395 C CB  . ARG B 1 211 ? 7.615   72.639  22.748  1.00 51.68  ? 306  ARG B CB  1 
ATOM   5396 C CG  . ARG B 1 211 ? 7.658   71.134  22.787  1.00 49.38  ? 306  ARG B CG  1 
ATOM   5397 C CD  . ARG B 1 211 ? 6.339   70.532  23.205  1.00 45.83  ? 306  ARG B CD  1 
ATOM   5398 N NE  . ARG B 1 211 ? 6.116   69.270  22.549  1.00 46.80  ? 306  ARG B NE  1 
ATOM   5399 C CZ  . ARG B 1 211 ? 5.282   68.341  22.962  1.00 47.20  ? 306  ARG B CZ  1 
ATOM   5400 N NH1 . ARG B 1 211 ? 4.563   68.528  24.033  1.00 43.64  ? 306  ARG B NH1 1 
ATOM   5401 N NH2 . ARG B 1 211 ? 5.155   67.232  22.284  1.00 41.11  ? 306  ARG B NH2 1 
ATOM   5402 N N   . CYS B 1 212 ? 9.204   73.969  25.258  1.00 48.87  ? 307  CYS B N   1 
ATOM   5403 C CA  . CYS B 1 212 ? 10.289  73.746  26.207  1.00 47.74  ? 307  CYS B CA  1 
ATOM   5404 C C   . CYS B 1 212 ? 9.830   73.849  27.657  1.00 55.03  ? 307  CYS B C   1 
ATOM   5405 O O   . CYS B 1 212 ? 10.494  73.298  28.548  1.00 53.07  ? 307  CYS B O   1 
ATOM   5406 C CB  . CYS B 1 212 ? 11.422  74.739  25.971  1.00 56.70  ? 307  CYS B CB  1 
ATOM   5407 S SG  . CYS B 1 212 ? 12.810  74.479  27.116  1.00 64.78  ? 307  CYS B SG  1 
ATOM   5408 N N   . VAL B 1 213 ? 8.733   74.561  27.920  1.00 50.62  ? 308  VAL B N   1 
ATOM   5409 C CA  . VAL B 1 213 ? 8.098   74.502  29.233  1.00 53.83  ? 308  VAL B CA  1 
ATOM   5410 C C   . VAL B 1 213 ? 7.143   73.317  29.319  1.00 50.24  ? 308  VAL B C   1 
ATOM   5411 O O   . VAL B 1 213 ? 7.080   72.630  30.343  1.00 50.89  ? 308  VAL B O   1 
ATOM   5412 C CB  . VAL B 1 213 ? 7.370   75.834  29.514  1.00 49.56  ? 308  VAL B CB  1 
ATOM   5413 C CG1 . VAL B 1 213 ? 6.651   75.786  30.854  1.00 50.39  ? 308  VAL B CG1 1 
ATOM   5414 C CG2 . VAL B 1 213 ? 8.357   76.993  29.470  1.00 54.50  ? 308  VAL B CG2 1 
ATOM   5415 N N   . ASP B 1 214 ? 6.401   73.067  28.234  1.00 51.31  ? 309  ASP B N   1 
ATOM   5416 C CA  . ASP B 1 214 ? 5.416   71.985  28.221  1.00 52.50  ? 309  ASP B CA  1 
ATOM   5417 C C   . ASP B 1 214 ? 6.059   70.630  28.516  1.00 48.71  ? 309  ASP B C   1 
ATOM   5418 O O   . ASP B 1 214 ? 5.447   69.779  29.173  1.00 50.38  ? 309  ASP B O   1 
ATOM   5419 C CB  . ASP B 1 214 ? 4.695   71.964  26.866  1.00 49.80  ? 309  ASP B CB  1 
ATOM   5420 C CG  . ASP B 1 214 ? 3.612   70.891  26.782  1.00 50.20  ? 309  ASP B CG  1 
ATOM   5421 O OD1 . ASP B 1 214 ? 2.779   70.804  27.709  1.00 52.36  ? 309  ASP B OD1 1 
ATOM   5422 O OD2 . ASP B 1 214 ? 3.572   70.159  25.769  1.00 51.47  ? 309  ASP B OD2 1 
ATOM   5423 N N   . LEU B 1 215 ? 7.294   70.420  28.053  1.00 51.43  ? 310  LEU B N   1 
ATOM   5424 C CA  . LEU B 1 215 ? 7.988   69.143  28.188  1.00 47.89  ? 310  LEU B CA  1 
ATOM   5425 C C   . LEU B 1 215 ? 8.458   68.866  29.608  1.00 50.04  ? 310  LEU B C   1 
ATOM   5426 O O   . LEU B 1 215 ? 8.918   67.751  29.876  1.00 45.03  ? 310  LEU B O   1 
ATOM   5427 C CB  . LEU B 1 215 ? 9.188   69.100  27.242  1.00 49.17  ? 310  LEU B CB  1 
ATOM   5428 C CG  . LEU B 1 215 ? 8.872   68.905  25.761  1.00 50.35  ? 310  LEU B CG  1 
ATOM   5429 C CD1 . LEU B 1 215 ? 10.147  68.968  24.909  1.00 46.06  ? 310  LEU B CD1 1 
ATOM   5430 C CD2 . LEU B 1 215 ? 8.147   67.573  25.555  1.00 46.18  ? 310  LEU B CD2 1 
ATOM   5431 N N   . ARG B 1 216 ? 8.344   69.842  30.522  1.00 49.79  ? 311  ARG B N   1 
ATOM   5432 C CA  . ARG B 1 216 ? 8.716   69.656  31.920  1.00 49.69  ? 311  ARG B CA  1 
ATOM   5433 C C   . ARG B 1 216 ? 7.607   69.044  32.769  1.00 51.22  ? 311  ARG B C   1 
ATOM   5434 O O   . ARG B 1 216 ? 7.866   68.704  33.933  1.00 49.04  ? 311  ARG B O   1 
ATOM   5435 C CB  . ARG B 1 216 ? 9.143   70.993  32.548  1.00 50.89  ? 311  ARG B CB  1 
ATOM   5436 C CG  . ARG B 1 216 ? 10.318  71.648  31.829  1.00 50.78  ? 311  ARG B CG  1 
ATOM   5437 C CD  . ARG B 1 216 ? 10.555  73.088  32.269  1.00 50.31  ? 311  ARG B CD  1 
ATOM   5438 N NE  . ARG B 1 216 ? 11.412  73.788  31.309  1.00 56.24  ? 311  ARG B NE  1 
ATOM   5439 C CZ  . ARG B 1 216 ? 12.051  74.923  31.561  1.00 54.72  ? 311  ARG B CZ  1 
ATOM   5440 N NH1 . ARG B 1 216 ? 11.992  75.502  32.753  1.00 53.27  ? 311  ARG B NH1 1 
ATOM   5441 N NH2 . ARG B 1 216 ? 12.769  75.490  30.597  1.00 53.03  ? 311  ARG B NH2 1 
ATOM   5442 N N   . THR B 1 217 ? 6.384   68.911  32.251  1.00 48.22  ? 312  THR B N   1 
ATOM   5443 C CA  . THR B 1 217 ? 5.378   68.189  33.026  1.00 51.46  ? 312  THR B CA  1 
ATOM   5444 C C   . THR B 1 217 ? 5.817   66.743  33.180  1.00 51.26  ? 312  THR B C   1 
ATOM   5445 O O   . THR B 1 217 ? 6.536   66.198  32.338  1.00 48.18  ? 312  THR B O   1 
ATOM   5446 C CB  . THR B 1 217 ? 3.990   68.212  32.374  1.00 49.99  ? 312  THR B CB  1 
ATOM   5447 O OG1 . THR B 1 217 ? 4.000   67.417  31.175  1.00 44.06  ? 312  THR B OG1 1 
ATOM   5448 C CG2 . THR B 1 217 ? 3.556   69.620  32.076  1.00 46.87  ? 312  THR B CG2 1 
ATOM   5449 N N   . TYR B 1 218 ? 5.377   66.126  34.279  1.00 52.49  ? 313  TYR B N   1 
ATOM   5450 C CA  . TYR B 1 218 ? 5.777   64.753  34.562  1.00 50.27  ? 313  TYR B CA  1 
ATOM   5451 C C   . TYR B 1 218 ? 5.319   63.797  33.463  1.00 47.50  ? 313  TYR B C   1 
ATOM   5452 O O   . TYR B 1 218 ? 6.067   62.890  33.066  1.00 48.36  ? 313  TYR B O   1 
ATOM   5453 C CB  . TYR B 1 218 ? 5.223   64.336  35.920  1.00 51.16  ? 313  TYR B CB  1 
ATOM   5454 C CG  . TYR B 1 218 ? 5.733   65.180  37.073  1.00 53.67  ? 313  TYR B CG  1 
ATOM   5455 C CD1 . TYR B 1 218 ? 7.092   65.255  37.356  1.00 55.67  ? 313  TYR B CD1 1 
ATOM   5456 C CD2 . TYR B 1 218 ? 4.855   65.881  37.893  1.00 55.03  ? 313  TYR B CD2 1 
ATOM   5457 C CE1 . TYR B 1 218 ? 7.563   66.009  38.425  1.00 58.87  ? 313  TYR B CE1 1 
ATOM   5458 C CE2 . TYR B 1 218 ? 5.317   66.645  38.967  1.00 54.97  ? 313  TYR B CE2 1 
ATOM   5459 C CZ  . TYR B 1 218 ? 6.671   66.703  39.225  1.00 57.21  ? 313  TYR B CZ  1 
ATOM   5460 O OH  . TYR B 1 218 ? 7.136   67.448  40.285  1.00 60.77  ? 313  TYR B OH  1 
ATOM   5461 N N   . ALA B 1 219 ? 4.104   64.000  32.937  1.00 44.83  ? 314  ALA B N   1 
ATOM   5462 C CA  . ALA B 1 219 ? 3.585   63.098  31.910  1.00 45.65  ? 314  ALA B CA  1 
ATOM   5463 C C   . ALA B 1 219 ? 4.331   63.261  30.591  1.00 45.00  ? 314  ALA B C   1 
ATOM   5464 O O   . ALA B 1 219 ? 4.596   62.269  29.901  1.00 44.79  ? 314  ALA B O   1 
ATOM   5465 C CB  . ALA B 1 219 ? 2.082   63.321  31.709  1.00 45.53  ? 314  ALA B CB  1 
ATOM   5466 N N   . ASN B 1 220 ? 4.697   64.492  30.220  1.00 43.19  ? 315  ASN B N   1 
ATOM   5467 C CA  . ASN B 1 220 ? 5.385   64.686  28.941  1.00 44.91  ? 315  ASN B CA  1 
ATOM   5468 C C   . ASN B 1 220 ? 6.802   64.133  28.983  1.00 43.70  ? 315  ASN B C   1 
ATOM   5469 O O   . ASN B 1 220 ? 7.261   63.470  28.032  1.00 43.40  ? 315  ASN B O   1 
ATOM   5470 C CB  . ASN B 1 220 ? 5.385   66.167  28.566  1.00 46.94  ? 315  ASN B CB  1 
ATOM   5471 C CG  . ASN B 1 220 ? 4.050   66.615  28.012  1.00 46.29  ? 315  ASN B CG  1 
ATOM   5472 O OD1 . ASN B 1 220 ? 3.290   65.796  27.497  1.00 45.32  ? 315  ASN B OD1 1 
ATOM   5473 N ND2 . ASN B 1 220 ? 3.752   67.907  28.116  1.00 44.12  ? 315  ASN B ND2 1 
ATOM   5474 N N   . TYR B 1 221 ? 7.508   64.377  30.086  1.00 46.80  ? 316  TYR B N   1 
ATOM   5475 C CA  . TYR B 1 221 ? 8.802   63.740  30.269  1.00 46.06  ? 316  TYR B CA  1 
ATOM   5476 C C   . TYR B 1 221 ? 8.672   62.231  30.150  1.00 45.78  ? 316  TYR B C   1 
ATOM   5477 O O   . TYR B 1 221 ? 9.467   61.573  29.466  1.00 42.67  ? 316  TYR B O   1 
ATOM   5478 C CB  . TYR B 1 221 ? 9.393   64.112  31.628  1.00 45.47  ? 316  TYR B CB  1 
ATOM   5479 C CG  . TYR B 1 221 ? 10.665  63.341  31.847  1.00 50.59  ? 316  TYR B CG  1 
ATOM   5480 C CD1 . TYR B 1 221 ? 11.845  63.727  31.212  1.00 51.05  ? 316  TYR B CD1 1 
ATOM   5481 C CD2 . TYR B 1 221 ? 10.678  62.191  32.624  1.00 48.02  ? 316  TYR B CD2 1 
ATOM   5482 C CE1 . TYR B 1 221 ? 13.010  62.996  31.366  1.00 52.45  ? 316  TYR B CE1 1 
ATOM   5483 C CE2 . TYR B 1 221 ? 11.827  61.464  32.791  1.00 50.32  ? 316  TYR B CE2 1 
ATOM   5484 C CZ  . TYR B 1 221 ? 12.993  61.873  32.168  1.00 53.66  ? 316  TYR B CZ  1 
ATOM   5485 O OH  . TYR B 1 221 ? 14.134  61.133  32.327  1.00 58.37  ? 316  TYR B OH  1 
ATOM   5486 N N   . SER B 1 222 ? 7.675   61.662  30.833  1.00 46.26  ? 317  SER B N   1 
ATOM   5487 C CA  . SER B 1 222 ? 7.508   60.216  30.800  1.00 45.03  ? 317  SER B CA  1 
ATOM   5488 C C   . SER B 1 222 ? 7.199   59.720  29.392  1.00 42.48  ? 317  SER B C   1 
ATOM   5489 O O   . SER B 1 222 ? 7.748   58.697  28.959  1.00 43.96  ? 317  SER B O   1 
ATOM   5490 C CB  . SER B 1 222 ? 6.425   59.809  31.792  1.00 42.51  ? 317  SER B CB  1 
ATOM   5491 O OG  . SER B 1 222 ? 6.875   60.124  33.102  1.00 44.39  ? 317  SER B OG  1 
ATOM   5492 N N   . ILE B 1 223 ? 6.357   60.453  28.655  1.00 40.42  ? 318  ILE B N   1 
ATOM   5493 C CA  . ILE B 1 223 ? 6.030   60.075  27.280  1.00 41.23  ? 318  ILE B CA  1 
ATOM   5494 C C   . ILE B 1 223 ? 7.300   59.936  26.452  1.00 43.39  ? 318  ILE B C   1 
ATOM   5495 O O   . ILE B 1 223 ? 7.473   58.972  25.690  1.00 42.33  ? 318  ILE B O   1 
ATOM   5496 C CB  . ILE B 1 223 ? 5.076   61.105  26.647  1.00 41.95  ? 318  ILE B CB  1 
ATOM   5497 C CG1 . ILE B 1 223 ? 3.666   60.985  27.208  1.00 43.99  ? 318  ILE B CG1 1 
ATOM   5498 C CG2 . ILE B 1 223 ? 5.052   60.941  25.120  1.00 41.08  ? 318  ILE B CG2 1 
ATOM   5499 C CD1 . ILE B 1 223 ? 2.725   62.087  26.744  1.00 41.94  ? 318  ILE B CD1 1 
ATOM   5500 N N   . PHE B 1 224 ? 8.214   60.894  26.582  1.00 41.60  ? 319  PHE B N   1 
ATOM   5501 C CA  . PHE B 1 224 ? 9.352   60.826  25.660  1.00 42.42  ? 319  PHE B CA  1 
ATOM   5502 C C   . PHE B 1 224 ? 10.462  59.880  26.129  1.00 44.04  ? 319  PHE B C   1 
ATOM   5503 O O   . PHE B 1 224 ? 11.215  59.349  25.287  1.00 40.57  ? 319  PHE B O   1 
ATOM   5504 C CB  . PHE B 1 224 ? 9.825   62.245  25.349  1.00 42.77  ? 319  PHE B CB  1 
ATOM   5505 C CG  . PHE B 1 224 ? 8.867   62.951  24.433  1.00 42.88  ? 319  PHE B CG  1 
ATOM   5506 C CD1 . PHE B 1 224 ? 8.820   62.614  23.086  1.00 39.21  ? 319  PHE B CD1 1 
ATOM   5507 C CD2 . PHE B 1 224 ? 7.919   63.842  24.937  1.00 42.59  ? 319  PHE B CD2 1 
ATOM   5508 C CE1 . PHE B 1 224 ? 7.890   63.203  22.240  1.00 41.96  ? 319  PHE B CE1 1 
ATOM   5509 C CE2 . PHE B 1 224 ? 6.993   64.452  24.092  1.00 40.46  ? 319  PHE B CE2 1 
ATOM   5510 C CZ  . PHE B 1 224 ? 6.974   64.120  22.745  1.00 42.00  ? 319  PHE B CZ  1 
ATOM   5511 N N   . CYS B 1 225 ? 10.556  59.603  27.436  1.00 42.74  ? 320  CYS B N   1 
ATOM   5512 C CA  A CYS B 1 225 ? 11.353  58.456  27.864  0.49 45.43  ? 320  CYS B CA  1 
ATOM   5513 C CA  B CYS B 1 225 ? 11.356  58.461  27.872  0.51 43.44  ? 320  CYS B CA  1 
ATOM   5514 C C   . CYS B 1 225 ? 10.805  57.166  27.277  1.00 44.68  ? 320  CYS B C   1 
ATOM   5515 O O   . CYS B 1 225 ? 11.570  56.292  26.849  1.00 43.28  ? 320  CYS B O   1 
ATOM   5516 C CB  A CYS B 1 225 ? 11.378  58.358  29.384  0.49 46.78  ? 320  CYS B CB  1 
ATOM   5517 C CB  B CYS B 1 225 ? 11.382  58.402  29.405  0.51 48.95  ? 320  CYS B CB  1 
ATOM   5518 S SG  A CYS B 1 225 ? 12.273  59.670  30.149  0.49 41.52  ? 320  CYS B SG  1 
ATOM   5519 S SG  B CYS B 1 225 ? 12.709  57.412  30.179  0.51 52.67  ? 320  CYS B SG  1 
ATOM   5520 N N   . LEU B 1 226 ? 9.471   57.034  27.230  1.00 43.90  ? 321  LEU B N   1 
ATOM   5521 C CA  . LEU B 1 226 ? 8.849   55.838  26.670  1.00 42.48  ? 321  LEU B CA  1 
ATOM   5522 C C   . LEU B 1 226 ? 9.066   55.728  25.163  1.00 41.40  ? 321  LEU B C   1 
ATOM   5523 O O   . LEU B 1 226 ? 9.206   54.614  24.640  1.00 39.43  ? 321  LEU B O   1 
ATOM   5524 C CB  . LEU B 1 226 ? 7.355   55.838  27.006  1.00 40.15  ? 321  LEU B CB  1 
ATOM   5525 C CG  . LEU B 1 226 ? 7.027   55.444  28.451  1.00 42.38  ? 321  LEU B CG  1 
ATOM   5526 C CD1 . LEU B 1 226 ? 5.565   55.765  28.821  1.00 40.14  ? 321  LEU B CD1 1 
ATOM   5527 C CD2 . LEU B 1 226 ? 7.345   53.960  28.719  1.00 39.57  ? 321  LEU B CD2 1 
ATOM   5528 N N   . GLN B 1 227 ? 9.082   56.863  24.449  1.00 38.43  ? 322  GLN B N   1 
ATOM   5529 C CA  . GLN B 1 227 ? 9.404   56.829  23.025  1.00 40.18  ? 322  GLN B CA  1 
ATOM   5530 C C   . GLN B 1 227 ? 10.819  56.299  22.811  1.00 42.16  ? 322  GLN B C   1 
ATOM   5531 O O   . GLN B 1 227 ? 11.065  55.457  21.921  1.00 40.09  ? 322  GLN B O   1 
ATOM   5532 C CB  . GLN B 1 227 ? 9.260   58.228  22.405  1.00 41.85  ? 322  GLN B CB  1 
ATOM   5533 C CG  . GLN B 1 227 ? 9.181   58.219  20.865  1.00 40.32  ? 322  GLN B CG  1 
ATOM   5534 C CD  . GLN B 1 227 ? 9.632   59.527  20.226  1.00 39.86  ? 322  GLN B CD  1 
ATOM   5535 O OE1 . GLN B 1 227 ? 8.828   60.404  19.910  1.00 43.30  ? 322  GLN B OE1 1 
ATOM   5536 N NE2 . GLN B 1 227 ? 10.922  59.658  20.035  1.00 40.68  ? 322  GLN B NE2 1 
ATOM   5537 N N   . SER B 1 228 ? 11.771  56.778  23.628  1.00 41.24  ? 323  SER B N   1 
ATOM   5538 C CA  . SER B 1 228 ? 13.118  56.203  23.571  1.00 41.13  ? 323  SER B CA  1 
ATOM   5539 C C   . SER B 1 228 ? 13.098  54.694  23.850  1.00 42.49  ? 323  SER B C   1 
ATOM   5540 O O   . SER B 1 228 ? 13.739  53.912  23.133  1.00 40.29  ? 323  SER B O   1 
ATOM   5541 C CB  . SER B 1 228 ? 14.026  56.917  24.565  1.00 40.87  ? 323  SER B CB  1 
ATOM   5542 O OG  . SER B 1 228 ? 15.343  56.406  24.508  1.00 41.39  ? 323  SER B OG  1 
ATOM   5543 N N   . GLN B 1 229 ? 12.366  54.276  24.888  1.00 40.09  ? 324  GLN B N   1 
ATOM   5544 C CA  . GLN B 1 229 ? 12.248  52.851  25.216  1.00 42.28  ? 324  GLN B CA  1 
ATOM   5545 C C   . GLN B 1 229 ? 11.758  52.020  24.023  1.00 41.27  ? 324  GLN B C   1 
ATOM   5546 O O   . GLN B 1 229 ? 12.264  50.921  23.763  1.00 41.93  ? 324  GLN B O   1 
ATOM   5547 C CB  . GLN B 1 229 ? 11.306  52.686  26.415  1.00 44.53  ? 324  GLN B CB  1 
ATOM   5548 C CG  . GLN B 1 229 ? 11.621  51.479  27.263  1.00 54.76  ? 324  GLN B CG  1 
ATOM   5549 C CD  . GLN B 1 229 ? 13.021  51.551  27.829  1.00 60.52  ? 324  GLN B CD  1 
ATOM   5550 O OE1 . GLN B 1 229 ? 13.276  52.328  28.753  1.00 59.74  ? 324  GLN B OE1 1 
ATOM   5551 N NE2 . GLN B 1 229 ? 13.950  50.770  27.254  1.00 55.49  ? 324  GLN B NE2 1 
ATOM   5552 N N   . ILE B 1 230 ? 10.770  52.522  23.282  1.00 38.90  ? 325  ILE B N   1 
ATOM   5553 C CA  . ILE B 1 230 ? 10.287  51.781  22.114  1.00 40.09  ? 325  ILE B CA  1 
ATOM   5554 C C   . ILE B 1 230 ? 11.395  51.642  21.065  1.00 43.71  ? 325  ILE B C   1 
ATOM   5555 O O   . ILE B 1 230 ? 11.613  50.554  20.504  1.00 43.02  ? 325  ILE B O   1 
ATOM   5556 C CB  . ILE B 1 230 ? 9.038   52.454  21.522  1.00 38.96  ? 325  ILE B CB  1 
ATOM   5557 C CG1 . ILE B 1 230 ? 7.849   52.320  22.475  1.00 39.98  ? 325  ILE B CG1 1 
ATOM   5558 C CG2 . ILE B 1 230 ? 8.705   51.855  20.159  1.00 39.79  ? 325  ILE B CG2 1 
ATOM   5559 C CD1 . ILE B 1 230 ? 6.626   53.142  22.046  1.00 39.58  ? 325  ILE B CD1 1 
ATOM   5560 N N   . CYS B 1 231 ? 12.101  52.741  20.768  1.00 39.99  ? 326  CYS B N   1 
ATOM   5561 C CA  . CYS B 1 231 ? 13.209  52.642  19.813  1.00 41.78  ? 326  CYS B CA  1 
ATOM   5562 C C   . CYS B 1 231 ? 14.219  51.582  20.239  1.00 41.90  ? 326  CYS B C   1 
ATOM   5563 O O   . CYS B 1 231 ? 14.666  50.767  19.422  1.00 40.51  ? 326  CYS B O   1 
ATOM   5564 C CB  . CYS B 1 231 ? 13.913  53.994  19.653  1.00 43.58  ? 326  CYS B CB  1 
ATOM   5565 S SG  . CYS B 1 231 ? 12.980  55.156  18.670  1.00 49.67  ? 326  CYS B SG  1 
ATOM   5566 N N   . THR B 1 232 ? 14.601  51.601  21.521  1.00 40.03  ? 327  THR B N   1 
ATOM   5567 C CA  . THR B 1 232 ? 15.592  50.665  22.043  1.00 40.21  ? 327  THR B CA  1 
ATOM   5568 C C   . THR B 1 232 ? 15.124  49.218  21.919  1.00 42.38  ? 327  THR B C   1 
ATOM   5569 O O   . THR B 1 232 ? 15.877  48.349  21.454  1.00 38.49  ? 327  THR B O   1 
ATOM   5570 C CB  . THR B 1 232 ? 15.878  51.013  23.506  1.00 42.06  ? 327  THR B CB  1 
ATOM   5571 O OG1 . THR B 1 232 ? 16.567  52.259  23.561  1.00 42.35  ? 327  THR B OG1 1 
ATOM   5572 C CG2 . THR B 1 232 ? 16.718  49.930  24.209  1.00 42.64  ? 327  THR B CG2 1 
ATOM   5573 N N   . ILE B 1 233 ? 13.889  48.935  22.363  1.00 40.80  ? 328  ILE B N   1 
ATOM   5574 C CA  . ILE B 1 233 ? 13.360  47.568  22.314  1.00 38.94  ? 328  ILE B CA  1 
ATOM   5575 C C   . ILE B 1 233 ? 13.303  47.070  20.881  1.00 37.42  ? 328  ILE B C   1 
ATOM   5576 O O   . ILE B 1 233 ? 13.709  45.934  20.591  1.00 40.31  ? 328  ILE B O   1 
ATOM   5577 C CB  . ILE B 1 233 ? 11.972  47.489  22.983  1.00 37.92  ? 328  ILE B CB  1 
ATOM   5578 C CG1 . ILE B 1 233 ? 12.059  47.856  24.471  1.00 40.22  ? 328  ILE B CG1 1 
ATOM   5579 C CG2 . ILE B 1 233 ? 11.366  46.085  22.809  1.00 35.40  ? 328  ILE B CG2 1 
ATOM   5580 C CD1 . ILE B 1 233 ? 10.713  48.294  25.075  1.00 39.83  ? 328  ILE B CD1 1 
ATOM   5581 N N   . PHE B 1 234 ? 12.804  47.910  19.964  1.00 38.50  ? 329  PHE B N   1 
ATOM   5582 C CA  . PHE B 1 234 ? 12.701  47.559  18.542  1.00 39.86  ? 329  PHE B CA  1 
ATOM   5583 C C   . PHE B 1 234 ? 14.073  47.222  17.955  1.00 40.28  ? 329  PHE B C   1 
ATOM   5584 O O   . PHE B 1 234 ? 14.280  46.129  17.388  1.00 37.19  ? 329  PHE B O   1 
ATOM   5585 C CB  . PHE B 1 234 ? 12.029  48.731  17.799  1.00 36.54  ? 329  PHE B CB  1 
ATOM   5586 C CG  . PHE B 1 234 ? 12.091  48.675  16.275  1.00 39.29  ? 329  PHE B CG  1 
ATOM   5587 C CD1 . PHE B 1 234 ? 13.080  49.374  15.575  1.00 36.76  ? 329  PHE B CD1 1 
ATOM   5588 C CD2 . PHE B 1 234 ? 11.118  47.992  15.540  1.00 38.92  ? 329  PHE B CD2 1 
ATOM   5589 C CE1 . PHE B 1 234 ? 13.141  49.360  14.166  1.00 36.23  ? 329  PHE B CE1 1 
ATOM   5590 C CE2 . PHE B 1 234 ? 11.147  47.986  14.127  1.00 40.33  ? 329  PHE B CE2 1 
ATOM   5591 C CZ  . PHE B 1 234 ? 12.162  48.677  13.433  1.00 37.69  ? 329  PHE B CZ  1 
ATOM   5592 N N   . LYS B 1 235 ? 15.037  48.137  18.111  1.00 39.58  ? 330  LYS B N   1 
ATOM   5593 C CA  . LYS B 1 235 ? 16.364  47.890  17.543  1.00 39.31  ? 330  LYS B CA  1 
ATOM   5594 C C   . LYS B 1 235 ? 17.010  46.646  18.144  1.00 37.93  ? 330  LYS B C   1 
ATOM   5595 O O   . LYS B 1 235 ? 17.617  45.849  17.417  1.00 39.05  ? 330  LYS B O   1 
ATOM   5596 C CB  . LYS B 1 235 ? 17.263  49.112  17.739  1.00 39.96  ? 330  LYS B CB  1 
ATOM   5597 C CG  . LYS B 1 235 ? 16.827  50.291  16.883  1.00 48.85  ? 330  LYS B CG  1 
ATOM   5598 C CD  . LYS B 1 235 ? 17.731  51.523  17.060  1.00 55.91  ? 330  LYS B CD  1 
ATOM   5599 C CE  . LYS B 1 235 ? 17.047  52.602  17.918  1.00 52.65  ? 330  LYS B CE  1 
ATOM   5600 N NZ  . LYS B 1 235 ? 17.953  53.781  18.063  1.00 58.48  ? 330  LYS B NZ  1 
ATOM   5601 N N   . ASN B 1 236 ? 16.894  46.452  19.461  1.00 37.82  ? 331  ASN B N   1 
ATOM   5602 C CA  . ASN B 1 236 ? 17.597  45.329  20.078  1.00 38.38  ? 331  ASN B CA  1 
ATOM   5603 C C   . ASN B 1 236 ? 16.949  43.993  19.722  1.00 40.92  ? 331  ASN B C   1 
ATOM   5604 O O   . ASN B 1 236 ? 17.657  42.996  19.545  1.00 39.87  ? 331  ASN B O   1 
ATOM   5605 C CB  . ASN B 1 236 ? 17.674  45.509  21.596  1.00 38.58  ? 331  ASN B CB  1 
ATOM   5606 C CG  . ASN B 1 236 ? 18.730  46.528  22.009  1.00 43.75  ? 331  ASN B CG  1 
ATOM   5607 O OD1 . ASN B 1 236 ? 19.595  46.897  21.213  1.00 46.27  ? 331  ASN B OD1 1 
ATOM   5608 N ND2 . ASN B 1 236 ? 18.664  46.989  23.262  1.00 41.95  ? 331  ASN B ND2 1 
ATOM   5609 N N   . PHE B 1 237 ? 15.614  43.938  19.603  1.00 36.44  ? 332  PHE B N   1 
ATOM   5610 C CA  . PHE B 1 237 ? 14.985  42.710  19.109  1.00 38.46  ? 332  PHE B CA  1 
ATOM   5611 C C   . PHE B 1 237 ? 15.526  42.356  17.724  1.00 36.51  ? 332  PHE B C   1 
ATOM   5612 O O   . PHE B 1 237 ? 15.916  41.204  17.462  1.00 38.03  ? 332  PHE B O   1 
ATOM   5613 C CB  . PHE B 1 237 ? 13.455  42.869  19.078  1.00 36.63  ? 332  PHE B CB  1 
ATOM   5614 C CG  . PHE B 1 237 ? 12.707  41.613  18.669  1.00 37.85  ? 332  PHE B CG  1 
ATOM   5615 C CD1 . PHE B 1 237 ? 12.383  40.642  19.605  1.00 39.30  ? 332  PHE B CD1 1 
ATOM   5616 C CD2 . PHE B 1 237 ? 12.325  41.415  17.349  1.00 36.02  ? 332  PHE B CD2 1 
ATOM   5617 C CE1 . PHE B 1 237 ? 11.683  39.491  19.230  1.00 41.57  ? 332  PHE B CE1 1 
ATOM   5618 C CE2 . PHE B 1 237 ? 11.643  40.278  16.971  1.00 37.93  ? 332  PHE B CE2 1 
ATOM   5619 C CZ  . PHE B 1 237 ? 11.313  39.312  17.900  1.00 37.18  ? 332  PHE B CZ  1 
ATOM   5620 N N   . LEU B 1 238 ? 15.604  43.346  16.831  1.00 35.40  ? 333  LEU B N   1 
ATOM   5621 C CA  . LEU B 1 238 ? 16.056  43.020  15.480  1.00 34.54  ? 333  LEU B CA  1 
ATOM   5622 C C   . LEU B 1 238 ? 17.533  42.632  15.475  1.00 38.78  ? 333  LEU B C   1 
ATOM   5623 O O   . LEU B 1 238 ? 17.915  41.617  14.878  1.00 37.55  ? 333  LEU B O   1 
ATOM   5624 C CB  . LEU B 1 238 ? 15.778  44.184  14.534  1.00 33.49  ? 333  LEU B CB  1 
ATOM   5625 C CG  . LEU B 1 238 ? 14.269  44.451  14.388  1.00 38.28  ? 333  LEU B CG  1 
ATOM   5626 C CD1 . LEU B 1 238 ? 14.028  45.785  13.683  1.00 33.62  ? 333  LEU B CD1 1 
ATOM   5627 C CD2 . LEU B 1 238 ? 13.573  43.296  13.633  1.00 38.12  ? 333  LEU B CD2 1 
ATOM   5628 N N   . LEU B 1 239 ? 18.376  43.408  16.163  1.00 36.66  ? 334  LEU B N   1 
ATOM   5629 C CA  . LEU B 1 239 ? 19.795  43.067  16.256  1.00 40.02  ? 334  LEU B CA  1 
ATOM   5630 C C   . LEU B 1 239 ? 20.008  41.668  16.808  1.00 39.23  ? 334  LEU B C   1 
ATOM   5631 O O   . LEU B 1 239 ? 20.854  40.924  16.296  1.00 38.00  ? 334  LEU B O   1 
ATOM   5632 C CB  . LEU B 1 239 ? 20.536  44.078  17.121  1.00 36.89  ? 334  LEU B CB  1 
ATOM   5633 C CG  . LEU B 1 239 ? 20.655  45.457  16.469  1.00 41.96  ? 334  LEU B CG  1 
ATOM   5634 C CD1 . LEU B 1 239 ? 21.138  46.453  17.521  1.00 43.78  ? 334  LEU B CD1 1 
ATOM   5635 C CD2 . LEU B 1 239 ? 21.595  45.431  15.236  1.00 37.21  ? 334  LEU B CD2 1 
ATOM   5636 N N   . GLU B 1 240 ? 19.280  41.293  17.872  1.00 36.34  ? 335  GLU B N   1 
ATOM   5637 C CA  . GLU B 1 240 ? 19.419  39.940  18.391  1.00 37.02  ? 335  GLU B CA  1 
ATOM   5638 C C   . GLU B 1 240 ? 18.953  38.915  17.376  1.00 41.68  ? 335  GLU B C   1 
ATOM   5639 O O   . GLU B 1 240 ? 19.270  37.737  17.521  1.00 37.42  ? 335  GLU B O   1 
ATOM   5640 C CB  . GLU B 1 240 ? 18.626  39.747  19.692  1.00 37.00  ? 335  GLU B CB  1 
ATOM   5641 N N   . ASN B 1 241 ? 18.177  39.331  16.367  1.00 35.30  ? 336  ASN B N   1 
ATOM   5642 C CA  . ASN B 1 241 ? 17.769  38.409  15.319  1.00 37.95  ? 336  ASN B CA  1 
ATOM   5643 C C   . ASN B 1 241 ? 18.566  38.584  14.028  1.00 38.51  ? 336  ASN B C   1 
ATOM   5644 O O   . ASN B 1 241 ? 18.071  38.268  12.944  1.00 37.39  ? 336  ASN B O   1 
ATOM   5645 C CB  . ASN B 1 241 ? 16.271  38.556  15.078  1.00 37.75  ? 336  ASN B CB  1 
ATOM   5646 C CG  . ASN B 1 241 ? 15.468  37.804  16.122  1.00 40.13  ? 336  ASN B CG  1 
ATOM   5647 O OD1 . ASN B 1 241 ? 15.359  36.587  16.049  1.00 40.35  ? 336  ASN B OD1 1 
ATOM   5648 N ND2 . ASN B 1 241 ? 14.947  38.517  17.128  1.00 38.15  ? 336  ASN B ND2 1 
ATOM   5649 N N   . ASN B 1 242 ? 19.781  39.123  14.129  1.00 39.69  ? 337  ASN B N   1 
ATOM   5650 C CA  . ASN B 1 242 ? 20.763  39.144  13.042  1.00 40.76  ? 337  ASN B CA  1 
ATOM   5651 C C   . ASN B 1 242 ? 20.421  40.169  11.957  1.00 41.72  ? 337  ASN B C   1 
ATOM   5652 O O   . ASN B 1 242 ? 20.781  39.976  10.793  1.00 41.93  ? 337  ASN B O   1 
ATOM   5653 C CB  . ASN B 1 242 ? 20.935  37.748  12.419  1.00 38.87  ? 337  ASN B CB  1 
ATOM   5654 C CG  . ASN B 1 242 ? 22.330  37.533  11.816  1.00 46.23  ? 337  ASN B CG  1 
ATOM   5655 O OD1 . ASN B 1 242 ? 23.273  38.258  12.139  1.00 43.51  ? 337  ASN B OD1 1 
ATOM   5656 N ND2 . ASN B 1 242 ? 22.460  36.528  10.947  1.00 45.11  ? 337  ASN B ND2 1 
ATOM   5657 N N   . PHE B 1 243 ? 19.714  41.248  12.316  1.00 37.69  ? 338  PHE B N   1 
ATOM   5658 C CA  . PHE B 1 243 ? 19.504  42.381  11.421  1.00 36.78  ? 338  PHE B CA  1 
ATOM   5659 C C   . PHE B 1 243 ? 20.708  43.311  11.469  1.00 40.80  ? 338  PHE B C   1 
ATOM   5660 O O   . PHE B 1 243 ? 21.415  43.389  12.480  1.00 40.03  ? 338  PHE B O   1 
ATOM   5661 C CB  . PHE B 1 243 ? 18.247  43.183  11.820  1.00 35.08  ? 338  PHE B CB  1 
ATOM   5662 C CG  . PHE B 1 243 ? 16.967  42.592  11.301  1.00 33.99  ? 338  PHE B CG  1 
ATOM   5663 C CD1 . PHE B 1 243 ? 16.451  41.420  11.849  1.00 33.14  ? 338  PHE B CD1 1 
ATOM   5664 C CD2 . PHE B 1 243 ? 16.293  43.185  10.246  1.00 35.31  ? 338  PHE B CD2 1 
ATOM   5665 C CE1 . PHE B 1 243 ? 15.274  40.862  11.357  1.00 36.81  ? 338  PHE B CE1 1 
ATOM   5666 C CE2 . PHE B 1 243 ? 15.117  42.628  9.736   1.00 36.29  ? 338  PHE B CE2 1 
ATOM   5667 C CZ  . PHE B 1 243 ? 14.602  41.474  10.295  1.00 34.80  ? 338  PHE B CZ  1 
ATOM   5668 N N   . ILE B 1 244 ? 20.910  44.063  10.392  1.00 35.22  ? 339  ILE B N   1 
ATOM   5669 C CA  . ILE B 1 244 ? 21.805  45.215  10.444  1.00 37.96  ? 339  ILE B CA  1 
ATOM   5670 C C   . ILE B 1 244 ? 20.986  46.474  10.221  1.00 37.02  ? 339  ILE B C   1 
ATOM   5671 O O   . ILE B 1 244 ? 19.963  46.464  9.530   1.00 38.12  ? 339  ILE B O   1 
ATOM   5672 C CB  . ILE B 1 244 ? 22.962  45.163  9.422   1.00 40.18  ? 339  ILE B CB  1 
ATOM   5673 C CG1 . ILE B 1 244 ? 22.433  45.350  7.998   1.00 38.53  ? 339  ILE B CG1 1 
ATOM   5674 C CG2 . ILE B 1 244 ? 23.785  43.882  9.577   1.00 41.24  ? 339  ILE B CG2 1 
ATOM   5675 C CD1 . ILE B 1 244 ? 23.561  45.622  6.995   1.00 40.89  ? 339  ILE B CD1 1 
ATOM   5676 N N   . GLU B 1 245 ? 21.438  47.567  10.832  1.00 36.14  ? 340  GLU B N   1 
ATOM   5677 C CA  . GLU B 1 245 ? 20.824  48.865  10.625  1.00 36.96  ? 340  GLU B CA  1 
ATOM   5678 C C   . GLU B 1 245 ? 21.373  49.495  9.351   1.00 37.49  ? 340  GLU B C   1 
ATOM   5679 O O   . GLU B 1 245 ? 22.582  49.448  9.094   1.00 39.66  ? 340  GLU B O   1 
ATOM   5680 C CB  . GLU B 1 245 ? 21.105  49.772  11.831  1.00 37.89  ? 340  GLU B CB  1 
ATOM   5681 C CG  . GLU B 1 245 ? 20.584  51.199  11.678  1.00 39.95  ? 340  GLU B CG  1 
ATOM   5682 C CD  . GLU B 1 245 ? 20.478  51.961  13.008  1.00 46.58  ? 340  GLU B CD  1 
ATOM   5683 O OE1 . GLU B 1 245 ? 21.093  51.532  14.008  1.00 46.40  ? 340  GLU B OE1 1 
ATOM   5684 O OE2 . GLU B 1 245 ? 19.770  52.998  13.055  1.00 52.39  ? 340  GLU B OE2 1 
ATOM   5685 N N   . ILE B 1 246 ? 20.483  50.080  8.543   1.00 35.17  ? 341  ILE B N   1 
ATOM   5686 C CA  . ILE B 1 246 ? 20.883  50.799  7.339   1.00 36.10  ? 341  ILE B CA  1 
ATOM   5687 C C   . ILE B 1 246 ? 20.401  52.243  7.425   1.00 38.98  ? 341  ILE B C   1 
ATOM   5688 O O   . ILE B 1 246 ? 19.472  52.580  8.172   1.00 38.34  ? 341  ILE B O   1 
ATOM   5689 C CB  . ILE B 1 246 ? 20.341  50.138  6.052   1.00 40.13  ? 341  ILE B CB  1 
ATOM   5690 C CG1 . ILE B 1 246 ? 18.797  50.144  6.066   1.00 37.42  ? 341  ILE B CG1 1 
ATOM   5691 C CG2 . ILE B 1 246 ? 20.935  48.730  5.893   1.00 35.54  ? 341  ILE B CG2 1 
ATOM   5692 C CD1 . ILE B 1 246 ? 18.143  49.749  4.713   1.00 37.59  ? 341  ILE B CD1 1 
ATOM   5693 N N   . HIS B 1 247 ? 21.043  53.098  6.635   1.00 36.64  ? 342  HIS B N   1 
ATOM   5694 C CA  . HIS B 1 247 ? 20.671  54.507  6.510   1.00 38.85  ? 342  HIS B CA  1 
ATOM   5695 C C   . HIS B 1 247 ? 20.627  54.838  5.034   1.00 38.53  ? 342  HIS B C   1 
ATOM   5696 O O   . HIS B 1 247 ? 21.653  54.754  4.350   1.00 38.68  ? 342  HIS B O   1 
ATOM   5697 C CB  . HIS B 1 247 ? 21.667  55.421  7.227   1.00 37.70  ? 342  HIS B CB  1 
ATOM   5698 C CG  . HIS B 1 247 ? 21.689  55.216  8.702   1.00 39.41  ? 342  HIS B CG  1 
ATOM   5699 N ND1 . HIS B 1 247 ? 20.745  55.768  9.543   1.00 41.40  ? 342  HIS B ND1 1 
ATOM   5700 C CD2 . HIS B 1 247 ? 22.529  54.504  9.489   1.00 39.64  ? 342  HIS B CD2 1 
ATOM   5701 C CE1 . HIS B 1 247 ? 21.002  55.399  10.785  1.00 39.70  ? 342  HIS B CE1 1 
ATOM   5702 N NE2 . HIS B 1 247 ? 22.080  54.634  10.780  1.00 40.97  ? 342  HIS B NE2 1 
ATOM   5703 N N   . THR B 1 248 ? 19.448  55.196  4.542   1.00 38.47  ? 343  THR B N   1 
ATOM   5704 C CA  . THR B 1 248 ? 19.215  55.426  3.129   1.00 37.32  ? 343  THR B CA  1 
ATOM   5705 C C   . THR B 1 248 ? 18.744  56.859  2.931   1.00 40.25  ? 343  THR B C   1 
ATOM   5706 O O   . THR B 1 248 ? 18.256  57.488  3.877   1.00 40.54  ? 343  THR B O   1 
ATOM   5707 C CB  . THR B 1 248 ? 18.180  54.424  2.593   1.00 38.34  ? 343  THR B CB  1 
ATOM   5708 O OG1 . THR B 1 248 ? 16.936  54.617  3.279   1.00 38.73  ? 343  THR B OG1 1 
ATOM   5709 C CG2 . THR B 1 248 ? 18.676  52.987  2.843   1.00 37.96  ? 343  THR B CG2 1 
ATOM   5710 N N   . PRO B 1 249 ? 18.881  57.408  1.723   1.00 39.00  ? 344  PRO B N   1 
ATOM   5711 C CA  . PRO B 1 249 ? 18.717  58.856  1.542   1.00 43.00  ? 344  PRO B CA  1 
ATOM   5712 C C   . PRO B 1 249 ? 17.274  59.314  1.596   1.00 42.38  ? 344  PRO B C   1 
ATOM   5713 O O   . PRO B 1 249 ? 16.355  58.614  1.168   1.00 38.83  ? 344  PRO B O   1 
ATOM   5714 C CB  . PRO B 1 249 ? 19.294  59.106  0.138   1.00 41.39  ? 344  PRO B CB  1 
ATOM   5715 C CG  . PRO B 1 249 ? 19.102  57.812  -0.575  1.00 42.47  ? 344  PRO B CG  1 
ATOM   5716 C CD  . PRO B 1 249 ? 19.372  56.760  0.486   1.00 41.06  ? 344  PRO B CD  1 
ATOM   5717 N N   . LYS B 1 250 ? 17.095  60.538  2.095   1.00 42.58  ? 345  LYS B N   1 
ATOM   5718 C CA  . LYS B 1 250 ? 15.790  61.186  2.107   1.00 42.61  ? 345  LYS B CA  1 
ATOM   5719 C C   . LYS B 1 250 ? 15.629  62.195  0.985   1.00 44.29  ? 345  LYS B C   1 
ATOM   5720 O O   . LYS B 1 250 ? 14.500  62.645  0.739   1.00 44.64  ? 345  LYS B O   1 
ATOM   5721 C CB  . LYS B 1 250 ? 15.543  61.873  3.459   1.00 37.71  ? 345  LYS B CB  1 
ATOM   5722 C CG  . LYS B 1 250 ? 15.878  60.996  4.662   1.00 42.06  ? 345  LYS B CG  1 
ATOM   5723 C CD  . LYS B 1 250 ? 15.193  59.614  4.609   1.00 38.70  ? 345  LYS B CD  1 
ATOM   5724 C CE  . LYS B 1 250 ? 15.899  58.646  5.578   1.00 40.63  ? 345  LYS B CE  1 
ATOM   5725 N NZ  . LYS B 1 250 ? 15.562  57.201  5.365   1.00 38.09  ? 345  LYS B NZ  1 
ATOM   5726 N N   . LEU B 1 251 ? 16.723  62.570  0.317   1.00 40.41  ? 346  LEU B N   1 
ATOM   5727 C CA  . LEU B 1 251 ? 16.664  63.388  -0.888  1.00 45.26  ? 346  LEU B CA  1 
ATOM   5728 C C   . LEU B 1 251 ? 16.585  62.464  -2.099  1.00 46.28  ? 346  LEU B C   1 
ATOM   5729 O O   . LEU B 1 251 ? 17.500  61.667  -2.337  1.00 46.31  ? 346  LEU B O   1 
ATOM   5730 C CB  . LEU B 1 251 ? 17.882  64.311  -0.997  1.00 45.00  ? 346  LEU B CB  1 
ATOM   5731 C CG  . LEU B 1 251 ? 18.157  65.277  0.162   1.00 46.68  ? 346  LEU B CG  1 
ATOM   5732 C CD1 . LEU B 1 251 ? 19.412  66.112  -0.095  1.00 47.92  ? 346  LEU B CD1 1 
ATOM   5733 C CD2 . LEU B 1 251 ? 16.970  66.186  0.396   1.00 46.99  ? 346  LEU B CD2 1 
ATOM   5734 N N   . LEU B 1 252 ? 15.498  62.572  -2.855  1.00 41.93  ? 347  LEU B N   1 
ATOM   5735 C CA  . LEU B 1 252 ? 15.198  61.687  -3.970  1.00 50.34  ? 347  LEU B CA  1 
ATOM   5736 C C   . LEU B 1 252 ? 15.178  62.469  -5.273  1.00 53.46  ? 347  LEU B C   1 
ATOM   5737 O O   . LEU B 1 252 ? 14.841  63.655  -5.297  1.00 49.90  ? 347  LEU B O   1 
ATOM   5738 C CB  . LEU B 1 252 ? 13.836  61.002  -3.782  1.00 49.86  ? 347  LEU B CB  1 
ATOM   5739 C CG  . LEU B 1 252 ? 13.651  60.274  -2.452  1.00 49.50  ? 347  LEU B CG  1 
ATOM   5740 C CD1 . LEU B 1 252 ? 12.292  59.603  -2.385  1.00 53.68  ? 347  LEU B CD1 1 
ATOM   5741 C CD2 . LEU B 1 252 ? 14.791  59.274  -2.251  1.00 47.14  ? 347  LEU B CD2 1 
ATOM   5742 N N   . GLY B 1 253 ? 15.539  61.789  -6.364  1.00 55.47  ? 348  GLY B N   1 
ATOM   5743 C CA  . GLY B 1 253 ? 15.332  62.360  -7.679  1.00 55.94  ? 348  GLY B CA  1 
ATOM   5744 C C   . GLY B 1 253 ? 13.908  62.248  -8.162  1.00 63.45  ? 348  GLY B C   1 
ATOM   5745 O O   . GLY B 1 253 ? 13.479  63.042  -9.002  1.00 68.54  ? 348  GLY B O   1 
ATOM   5746 N N   . GLU B 1 254 ? 13.161  61.297  -7.622  1.00 68.39  ? 349  GLU B N   1 
ATOM   5747 C CA  . GLU B 1 254 ? 11.806  61.019  -8.051  1.00 70.77  ? 349  GLU B CA  1 
ATOM   5748 C C   . GLU B 1 254 ? 10.992  60.619  -6.834  1.00 73.17  ? 349  GLU B C   1 
ATOM   5749 O O   . GLU B 1 254 ? 11.530  60.122  -5.842  1.00 73.90  ? 349  GLU B O   1 
ATOM   5750 C CB  . GLU B 1 254 ? 11.782  59.905  -9.100  1.00 74.94  ? 349  GLU B CB  1 
ATOM   5751 C CG  . GLU B 1 254 ? 11.007  60.251  -10.327 1.00 76.47  ? 349  GLU B CG  1 
ATOM   5752 C CD  . GLU B 1 254 ? 11.642  61.362  -11.131 1.00 79.18  ? 349  GLU B CD  1 
ATOM   5753 O OE1 . GLU B 1 254 ? 11.101  62.486  -11.106 1.00 78.97  ? 349  GLU B OE1 1 
ATOM   5754 O OE2 . GLU B 1 254 ? 12.674  61.108  -11.794 1.00 81.02  ? 349  GLU B OE2 1 
ATOM   5755 N N   . SER B 1 255 ? 9.692   60.848  -6.881  0.88 75.37  ? 350  SER B N   1 
ATOM   5756 C CA  . SER B 1 255 ? 8.841   60.514  -5.749  0.88 78.01  ? 350  SER B CA  1 
ATOM   5757 C C   . SER B 1 255 ? 8.694   59.001  -5.535  0.88 83.94  ? 350  SER B C   1 
ATOM   5758 O O   . SER B 1 255 ? 8.246   58.286  -6.426  0.88 84.03  ? 350  SER B O   1 
ATOM   5759 C CB  . SER B 1 255 ? 7.482   61.158  -5.926  0.88 78.98  ? 350  SER B CB  1 
ATOM   5760 O OG  . SER B 1 255 ? 6.588   60.700  -4.956  0.88 81.59  ? 350  SER B OG  1 
ATOM   5761 N N   . SER B 1 256 ? 9.073   58.521  -4.351  0.88 90.60  ? 351  SER B N   1 
ATOM   5762 C CA  . SER B 1 256 ? 8.995   57.093  -4.045  0.88 84.65  ? 351  SER B CA  1 
ATOM   5763 C C   . SER B 1 256 ? 7.549   56.624  -4.087  0.88 87.02  ? 351  SER B C   1 
ATOM   5764 O O   . SER B 1 256 ? 7.240   55.547  -4.605  0.88 83.72  ? 351  SER B O   1 
ATOM   5765 C CB  . SER B 1 256 ? 9.633   56.779  -2.689  0.88 76.93  ? 351  SER B CB  1 
ATOM   5766 O OG  . SER B 1 256 ? 9.062   57.541  -1.644  0.88 73.03  ? 351  SER B OG  1 
ATOM   5767 N N   . GLU B 1 257 ? 6.675   57.446  -3.519  0.62 82.46  ? 352  GLU B N   1 
ATOM   5768 C CA  . GLU B 1 257 ? 5.242   57.197  -3.504  0.62 81.09  ? 352  GLU B CA  1 
ATOM   5769 C C   . GLU B 1 257 ? 4.612   58.131  -4.537  0.62 84.42  ? 352  GLU B C   1 
ATOM   5770 O O   . GLU B 1 257 ? 5.287   58.583  -5.454  0.62 85.60  ? 352  GLU B O   1 
ATOM   5771 C CB  . GLU B 1 257 ? 4.661   57.391  -2.103  0.62 77.68  ? 352  GLU B CB  1 
ATOM   5772 C CG  . GLU B 1 257 ? 5.353   56.549  -1.038  0.62 74.39  ? 352  GLU B CG  1 
ATOM   5773 C CD  . GLU B 1 257 ? 4.487   56.284  0.185   0.62 73.62  ? 352  GLU B CD  1 
ATOM   5774 O OE1 . GLU B 1 257 ? 3.519   57.027  0.419   0.62 74.49  ? 352  GLU B OE1 1 
ATOM   5775 O OE2 . GLU B 1 257 ? 4.771   55.322  0.920   0.62 72.82  ? 352  GLU B OE2 1 
ATOM   5776 N N   . GLY B 1 258 ? 3.318   58.391  -4.433  0.80 89.23  ? 353  GLY B N   1 
ATOM   5777 C CA  . GLY B 1 258 ? 2.705   59.292  -5.385  0.80 90.07  ? 353  GLY B CA  1 
ATOM   5778 C C   . GLY B 1 258 ? 3.348   60.648  -5.202  0.80 96.06  ? 353  GLY B C   1 
ATOM   5779 O O   . GLY B 1 258 ? 3.496   61.116  -4.075  0.80 94.48  ? 353  GLY B O   1 
ATOM   5780 N N   . GLY B 1 259 ? 3.685   61.302  -6.306  0.79 91.81  ? 354  GLY B N   1 
ATOM   5781 C CA  . GLY B 1 259 ? 4.337   62.596  -6.260  0.79 86.87  ? 354  GLY B CA  1 
ATOM   5782 C C   . GLY B 1 259 ? 3.530   63.756  -5.719  0.79 83.35  ? 354  GLY B C   1 
ATOM   5783 O O   . GLY B 1 259 ? 4.089   64.785  -5.373  0.79 78.99  ? 354  GLY B O   1 
ATOM   5784 N N   . ALA B 1 260 ? 2.221   63.599  -5.632  1.00 90.58  ? 355  ALA B N   1 
ATOM   5785 C CA  . ALA B 1 260 ? 1.392   64.682  -5.163  1.00 93.41  ? 355  ALA B CA  1 
ATOM   5786 C C   . ALA B 1 260 ? 1.476   64.891  -3.669  1.00 92.48  ? 355  ALA B C   1 
ATOM   5787 O O   . ALA B 1 260 ? 1.116   65.953  -3.176  1.00 91.24  ? 355  ALA B O   1 
ATOM   5788 C CB  . ALA B 1 260 ? -0.042  64.448  -5.578  1.00 95.03  ? 355  ALA B CB  1 
ATOM   5789 N N   . ASN B 1 261 ? 1.951   63.890  -2.944  1.00 78.98  ? 356  ASN B N   1 
ATOM   5790 C CA  . ASN B 1 261 ? 2.050   64.047  -1.500  1.00 71.49  ? 356  ASN B CA  1 
ATOM   5791 C C   . ASN B 1 261 ? 3.491   64.199  -1.034  1.00 66.69  ? 356  ASN B C   1 
ATOM   5792 O O   . ASN B 1 261 ? 3.783   63.976  0.146   1.00 60.07  ? 356  ASN B O   1 
ATOM   5793 C CB  . ASN B 1 261 ? 1.390   62.866  -0.788  1.00 73.81  ? 356  ASN B CB  1 
ATOM   5794 C CG  . ASN B 1 261 ? -0.103  62.789  -1.051  1.00 78.62  ? 356  ASN B CG  1 
ATOM   5795 O OD1 . ASN B 1 261 ? -0.798  63.808  -1.055  1.00 80.17  ? 356  ASN B OD1 1 
ATOM   5796 N ND2 . ASN B 1 261 ? -0.602  61.575  -1.290  1.00 74.88  ? 356  ASN B ND2 1 
ATOM   5797 N N   . ALA B 1 262 ? 4.402   64.546  -1.939  1.00 65.84  ? 357  ALA B N   1 
ATOM   5798 C CA  . ALA B 1 262 ? 5.812   64.669  -1.608  1.00 62.63  ? 357  ALA B CA  1 
ATOM   5799 C C   . ALA B 1 262 ? 6.214   66.135  -1.611  1.00 56.44  ? 357  ALA B C   1 
ATOM   5800 O O   . ALA B 1 262 ? 5.753   66.907  -2.450  1.00 58.79  ? 357  ALA B O   1 
ATOM   5801 C CB  . ALA B 1 262 ? 6.685   63.880  -2.592  1.00 62.21  ? 357  ALA B CB  1 
ATOM   5802 N N   . PHE B 1 263 ? 7.060   66.516  -0.657  1.00 50.14  ? 358  PHE B N   1 
ATOM   5803 C CA  . PHE B 1 263 ? 7.681   67.834  -0.692  1.00 53.04  ? 358  PHE B CA  1 
ATOM   5804 C C   . PHE B 1 263 ? 8.732   67.906  -1.796  1.00 55.91  ? 358  PHE B C   1 
ATOM   5805 O O   . PHE B 1 263 ? 9.516   66.971  -1.994  1.00 52.70  ? 358  PHE B O   1 
ATOM   5806 C CB  . PHE B 1 263 ? 8.334   68.162  0.649   1.00 49.73  ? 358  PHE B CB  1 
ATOM   5807 C CG  . PHE B 1 263 ? 7.361   68.297  1.794   1.00 52.22  ? 358  PHE B CG  1 
ATOM   5808 C CD1 . PHE B 1 263 ? 6.609   69.455  1.959   1.00 52.38  ? 358  PHE B CD1 1 
ATOM   5809 C CD2 . PHE B 1 263 ? 7.219   67.275  2.725   1.00 49.50  ? 358  PHE B CD2 1 
ATOM   5810 C CE1 . PHE B 1 263 ? 5.721   69.587  3.033   1.00 49.82  ? 358  PHE B CE1 1 
ATOM   5811 C CE2 . PHE B 1 263 ? 6.331   67.404  3.803   1.00 49.60  ? 358  PHE B CE2 1 
ATOM   5812 C CZ  . PHE B 1 263 ? 5.586   68.570  3.948   1.00 49.38  ? 358  PHE B CZ  1 
ATOM   5813 N N   . GLN B 1 264 ? 8.766   69.034  -2.497  1.00 54.31  ? 359  GLN B N   1 
ATOM   5814 C CA  . GLN B 1 264 ? 9.708   69.256  -3.585  1.00 56.36  ? 359  GLN B CA  1 
ATOM   5815 C C   . GLN B 1 264 ? 10.876  70.103  -3.106  1.00 56.16  ? 359  GLN B C   1 
ATOM   5816 O O   . GLN B 1 264 ? 10.706  70.995  -2.273  1.00 58.12  ? 359  GLN B O   1 
ATOM   5817 C CB  . GLN B 1 264 ? 9.022   69.946  -4.760  1.00 56.05  ? 359  GLN B CB  1 
ATOM   5818 C CG  . GLN B 1 264 ? 7.754   69.251  -5.207  1.00 61.18  ? 359  GLN B CG  1 
ATOM   5819 C CD  . GLN B 1 264 ? 6.952   70.082  -6.198  1.00 71.37  ? 359  GLN B CD  1 
ATOM   5820 O OE1 . GLN B 1 264 ? 6.699   69.643  -7.319  1.00 73.13  ? 359  GLN B OE1 1 
ATOM   5821 N NE2 . GLN B 1 264 ? 6.541   71.284  -5.784  1.00 71.37  ? 359  GLN B NE2 1 
ATOM   5822 N N   . ILE B 1 265 ? 12.033  69.884  -3.686  1.00 56.64  ? 360  ILE B N   1 
ATOM   5823 C CA  . ILE B 1 265 ? 13.176  70.706  -3.384  1.00 59.46  ? 360  ILE B CA  1 
ATOM   5824 C C   . ILE B 1 265 ? 14.030  70.869  -4.617  1.00 60.14  ? 360  ILE B C   1 
ATOM   5825 O O   . ILE B 1 265 ? 14.002  70.052  -5.496  1.00 58.39  ? 360  ILE B O   1 
ATOM   5826 C CB  . ILE B 1 265 ? 14.118  70.092  -2.349  1.00 63.92  ? 360  ILE B CB  1 
ATOM   5827 C CG1 . ILE B 1 265 ? 14.576  68.733  -2.820  1.00 62.50  ? 360  ILE B CG1 1 
ATOM   5828 C CG2 . ILE B 1 265 ? 13.509  70.023  -0.969  1.00 61.45  ? 360  ILE B CG2 1 
ATOM   5829 C CD1 . ILE B 1 265 ? 16.049  68.559  -2.616  1.00 61.44  ? 360  ILE B CD1 1 
ATOM   5830 N N   . ASN B 1 266 ? 14.755  71.964  -4.678  1.00 66.70  ? 361  ASN B N   1 
ATOM   5831 C CA  . ASN B 1 266 ? 15.733  72.194  -5.732  1.00 66.58  ? 361  ASN B CA  1 
ATOM   5832 C C   . ASN B 1 266 ? 17.062  71.600  -5.286  1.00 64.86  ? 361  ASN B C   1 
ATOM   5833 O O   . ASN B 1 266 ? 17.639  72.039  -4.287  1.00 65.36  ? 361  ASN B O   1 
ATOM   5834 C CB  . ASN B 1 266 ? 15.888  73.683  -6.045  1.00 65.55  ? 361  ASN B CB  1 
ATOM   5835 C CG  . ASN B 1 266 ? 17.070  73.965  -6.973  1.00 76.55  ? 361  ASN B CG  1 
ATOM   5836 O OD1 . ASN B 1 266 ? 17.959  74.767  -6.655  1.00 79.76  ? 361  ASN B OD1 1 
ATOM   5837 N ND2 . ASN B 1 266 ? 17.094  73.287  -8.118  1.00 73.12  ? 361  ASN B ND2 1 
ATOM   5838 N N   . TYR B 1 267 ? 17.547  70.615  -6.010  1.00 62.28  ? 362  TYR B N   1 
ATOM   5839 C CA  . TYR B 1 267 ? 18.817  70.003  -5.703  1.00 62.87  ? 362  TYR B CA  1 
ATOM   5840 C C   . TYR B 1 267 ? 19.790  70.351  -6.812  1.00 63.02  ? 362  TYR B C   1 
ATOM   5841 O O   . TYR B 1 267 ? 19.853  69.625  -7.772  1.00 62.25  ? 362  TYR B O   1 
ATOM   5842 C CB  . TYR B 1 267 ? 18.663  68.486  -5.625  1.00 53.16  ? 362  TYR B CB  1 
ATOM   5843 C CG  . TYR B 1 267 ? 19.861  67.751  -5.086  1.00 53.54  ? 362  TYR B CG  1 
ATOM   5844 C CD1 . TYR B 1 267 ? 20.115  67.714  -3.743  1.00 49.43  ? 362  TYR B CD1 1 
ATOM   5845 C CD2 . TYR B 1 267 ? 20.726  67.090  -5.918  1.00 52.17  ? 362  TYR B CD2 1 
ATOM   5846 C CE1 . TYR B 1 267 ? 21.196  67.056  -3.242  1.00 46.84  ? 362  TYR B CE1 1 
ATOM   5847 C CE2 . TYR B 1 267 ? 21.814  66.421  -5.417  1.00 50.18  ? 362  TYR B CE2 1 
ATOM   5848 C CZ  . TYR B 1 267 ? 22.040  66.411  -4.071  1.00 47.37  ? 362  TYR B CZ  1 
ATOM   5849 O OH  . TYR B 1 267 ? 23.098  65.766  -3.535  1.00 44.40  ? 362  TYR B OH  1 
ATOM   5850 N N   . PHE B 1 268 ? 20.531  71.445  -6.651  1.00 61.58  ? 363  PHE B N   1 
ATOM   5851 C CA  . PHE B 1 268 ? 21.522  71.942  -7.611  1.00 66.24  ? 363  PHE B CA  1 
ATOM   5852 C C   . PHE B 1 268 ? 21.083  71.803  -9.054  1.00 71.57  ? 363  PHE B C   1 
ATOM   5853 O O   . PHE B 1 268 ? 21.645  71.005  -9.788  1.00 75.48  ? 363  PHE B O   1 
ATOM   5854 C CB  . PHE B 1 268 ? 22.846  71.218  -7.453  1.00 60.43  ? 363  PHE B CB  1 
ATOM   5855 C CG  . PHE B 1 268 ? 23.376  71.208  -6.071  1.00 59.43  ? 363  PHE B CG  1 
ATOM   5856 C CD1 . PHE B 1 268 ? 23.122  70.158  -5.240  1.00 52.58  ? 363  PHE B CD1 1 
ATOM   5857 C CD2 . PHE B 1 268 ? 24.155  72.224  -5.623  1.00 54.36  ? 363  PHE B CD2 1 
ATOM   5858 C CE1 . PHE B 1 268 ? 23.629  70.131  -3.978  1.00 54.17  ? 363  PHE B CE1 1 
ATOM   5859 C CE2 . PHE B 1 268 ? 24.665  72.209  -4.359  1.00 57.03  ? 363  PHE B CE2 1 
ATOM   5860 C CZ  . PHE B 1 268 ? 24.398  71.160  -3.530  1.00 54.17  ? 363  PHE B CZ  1 
ATOM   5861 N N   . ASN B 1 269 ? 20.037  72.528  -9.403  1.00 69.90  ? 364  ASN B N   1 
ATOM   5862 C CA  . ASN B 1 269 ? 19.409  72.528  -10.724 1.00 76.28  ? 364  ASN B CA  1 
ATOM   5863 C C   . ASN B 1 269 ? 18.653  71.269  -11.116 1.00 73.98  ? 364  ASN B C   1 
ATOM   5864 O O   . ASN B 1 269 ? 18.325  71.089  -12.270 1.00 76.28  ? 364  ASN B O   1 
ATOM   5865 C CB  . ASN B 1 269 ? 20.315  73.016  -11.872 1.00 79.53  ? 364  ASN B CB  1 
ATOM   5866 C CG  . ASN B 1 269 ? 20.599  74.501  -11.816 1.00 84.89  ? 364  ASN B CG  1 
ATOM   5867 O OD1 . ASN B 1 269 ? 20.035  75.239  -11.017 1.00 83.97  ? 364  ASN B OD1 1 
ATOM   5868 N ND2 . ASN B 1 269 ? 21.484  74.943  -12.689 1.00 89.11  ? 364  ASN B ND2 1 
ATOM   5869 N N   . GLN B 1 270 ? 18.376  70.403  -10.160 1.00 70.89  ? 365  GLN B N   1 
ATOM   5870 C CA  . GLN B 1 270 ? 17.587  69.231  -10.436 1.00 66.98  ? 365  GLN B CA  1 
ATOM   5871 C C   . GLN B 1 270 ? 16.335  69.313  -9.608  1.00 65.72  ? 365  GLN B C   1 
ATOM   5872 O O   . GLN B 1 270 ? 16.287  69.987  -8.611  1.00 66.45  ? 365  GLN B O   1 
ATOM   5873 C CB  . GLN B 1 270 ? 18.321  67.963  -10.062 1.00 62.58  ? 365  GLN B CB  1 
ATOM   5874 C CG  . GLN B 1 270 ? 19.493  67.645  -10.937 1.00 67.20  ? 365  GLN B CG  1 
ATOM   5875 C CD  . GLN B 1 270 ? 20.012  66.258  -10.728 1.00 65.66  ? 365  GLN B CD  1 
ATOM   5876 O OE1 . GLN B 1 270 ? 21.130  66.079  -10.300 1.00 66.15  ? 365  GLN B OE1 1 
ATOM   5877 N NE2 . GLN B 1 270 ? 19.204  65.271  -11.036 1.00 61.94  ? 365  GLN B NE2 1 
ATOM   5878 N N   . LYS B 1 271 ? 15.299  68.654  -10.067 1.00 64.96  ? 366  LYS B N   1 
ATOM   5879 C CA  . LYS B 1 271 ? 14.052  68.561  -9.315  1.00 63.74  ? 366  LYS B CA  1 
ATOM   5880 C C   . LYS B 1 271 ? 14.133  67.360  -8.384  1.00 61.06  ? 366  LYS B C   1 
ATOM   5881 O O   . LYS B 1 271 ? 14.252  66.222  -8.855  1.00 61.24  ? 366  LYS B O   1 
ATOM   5882 C CB  . LYS B 1 271 ? 12.861  68.420  -10.262 1.00 61.16  ? 366  LYS B CB  1 
ATOM   5883 N N   . GLY B 1 272 ? 14.067  67.603  -7.073  1.00 59.13  ? 367  GLY B N   1 
ATOM   5884 C CA  . GLY B 1 272 ? 14.111  66.548  -6.090  1.00 55.60  ? 367  GLY B CA  1 
ATOM   5885 C C   . GLY B 1 272 ? 12.884  66.535  -5.191  1.00 56.09  ? 367  GLY B C   1 
ATOM   5886 O O   . GLY B 1 272 ? 12.034  67.429  -5.233  1.00 56.47  ? 367  GLY B O   1 
ATOM   5887 N N   . PHE B 1 273 ? 12.833  65.501  -4.352  1.00 52.00  ? 368  PHE B N   1 
ATOM   5888 C CA  . PHE B 1 273 ? 11.709  65.268  -3.464  1.00 50.48  ? 368  PHE B CA  1 
ATOM   5889 C C   . PHE B 1 273 ? 12.244  64.693  -2.164  1.00 50.72  ? 368  PHE B C   1 
ATOM   5890 O O   . PHE B 1 273 ? 13.300  64.054  -2.143  1.00 47.41  ? 368  PHE B O   1 
ATOM   5891 C CB  . PHE B 1 273 ? 10.672  64.307  -4.071  1.00 53.56  ? 368  PHE B CB  1 
ATOM   5892 C CG  . PHE B 1 273 ? 10.198  64.702  -5.451  1.00 58.96  ? 368  PHE B CG  1 
ATOM   5893 C CD1 . PHE B 1 273 ? 9.018   65.419  -5.622  1.00 58.94  ? 368  PHE B CD1 1 
ATOM   5894 C CD2 . PHE B 1 273 ? 10.921  64.335  -6.583  1.00 59.85  ? 368  PHE B CD2 1 
ATOM   5895 C CE1 . PHE B 1 273 ? 8.575   65.784  -6.894  1.00 57.61  ? 368  PHE B CE1 1 
ATOM   5896 C CE2 . PHE B 1 273 ? 10.484  64.698  -7.858  1.00 60.14  ? 368  PHE B CE2 1 
ATOM   5897 C CZ  . PHE B 1 273 ? 9.310   65.419  -8.012  1.00 57.30  ? 368  PHE B CZ  1 
ATOM   5898 N N   . LEU B 1 274 ? 11.503  64.920  -1.082  1.00 45.30  ? 369  LEU B N   1 
ATOM   5899 C CA  . LEU B 1 274 ? 11.790  64.293  0.198   1.00 44.13  ? 369  LEU B CA  1 
ATOM   5900 C C   . LEU B 1 274 ? 11.116  62.932  0.268   1.00 44.93  ? 369  LEU B C   1 
ATOM   5901 O O   . LEU B 1 274 ? 9.975   62.772  -0.171  1.00 43.03  ? 369  LEU B O   1 
ATOM   5902 C CB  . LEU B 1 274 ? 11.312  65.175  1.353   1.00 45.54  ? 369  LEU B CB  1 
ATOM   5903 C CG  . LEU B 1 274 ? 12.051  66.512  1.493   1.00 48.01  ? 369  LEU B CG  1 
ATOM   5904 C CD1 . LEU B 1 274 ? 11.553  67.276  2.715   1.00 44.82  ? 369  LEU B CD1 1 
ATOM   5905 C CD2 . LEU B 1 274 ? 13.544  66.255  1.607   1.00 49.25  ? 369  LEU B CD2 1 
ATOM   5906 N N   . ALA B 1 275 ? 11.818  61.965  0.807   1.00 40.61  ? 370  ALA B N   1 
ATOM   5907 C CA  . ALA B 1 275 ? 11.296  60.632  0.911   1.00 43.64  ? 370  ALA B CA  1 
ATOM   5908 C C   . ALA B 1 275 ? 10.098  60.489  1.822   1.00 44.26  ? 370  ALA B C   1 
ATOM   5909 O O   . ALA B 1 275 ? 10.061  61.027  2.890   1.00 42.55  ? 370  ALA B O   1 
ATOM   5910 C CB  . ALA B 1 275 ? 12.382  59.685  1.351   1.00 39.98  ? 370  ALA B CB  1 
ATOM   5911 N N   . GLN B 1 276 ? 9.098   59.789  1.342   1.00 46.05  ? 371  GLN B N   1 
ATOM   5912 C CA  . GLN B 1 276 ? 7.936   59.488  2.135   1.00 49.66  ? 371  GLN B CA  1 
ATOM   5913 C C   . GLN B 1 276 ? 8.130   58.157  2.848   1.00 48.73  ? 371  GLN B C   1 
ATOM   5914 O O   . GLN B 1 276 ? 7.449   57.865  3.786   1.00 47.17  ? 371  GLN B O   1 
ATOM   5915 C CB  . GLN B 1 276 ? 6.697   59.447  1.261   1.00 50.09  ? 371  GLN B CB  1 
ATOM   5916 C CG  . GLN B 1 276 ? 6.342   60.774  0.660   1.00 55.55  ? 371  GLN B CG  1 
ATOM   5917 C CD  . GLN B 1 276 ? 5.274   60.672  -0.379  1.00 65.96  ? 371  GLN B CD  1 
ATOM   5918 O OE1 . GLN B 1 276 ? 5.521   60.874  -1.536  1.00 67.80  ? 371  GLN B OE1 1 
ATOM   5919 N NE2 . GLN B 1 276 ? 4.088   60.336  0.033   1.00 67.47  ? 371  GLN B NE2 1 
ATOM   5920 N N   . SER B 1 277 ? 9.056   57.356  2.352   1.00 43.32  ? 372  SER B N   1 
ATOM   5921 C CA  . SER B 1 277 ? 9.361   56.052  2.885   1.00 45.27  ? 372  SER B CA  1 
ATOM   5922 C C   . SER B 1 277 ? 10.701  55.612  2.344   1.00 45.18  ? 372  SER B C   1 
ATOM   5923 O O   . SER B 1 277 ? 11.058  56.010  1.285   1.00 43.16  ? 372  SER B O   1 
ATOM   5924 C CB  . SER B 1 277 ? 8.303   55.115  2.351   1.00 45.78  ? 372  SER B CB  1 
ATOM   5925 O OG  . SER B 1 277 ? 8.568   53.788  2.606   1.00 46.99  ? 372  SER B OG  1 
ATOM   5926 N N   . PRO B 1 278 ? 11.428  54.756  3.050   1.00 41.60  ? 373  PRO B N   1 
ATOM   5927 C CA  . PRO B 1 278 ? 12.671  54.265  2.483   1.00 41.13  ? 373  PRO B CA  1 
ATOM   5928 C C   . PRO B 1 278 ? 12.426  52.966  1.741   1.00 42.15  ? 373  PRO B C   1 
ATOM   5929 O O   . PRO B 1 278 ? 13.355  52.253  1.501   1.00 42.27  ? 373  PRO B O   1 
ATOM   5930 C CB  . PRO B 1 278 ? 13.502  53.997  3.709   1.00 38.38  ? 373  PRO B CB  1 
ATOM   5931 C CG  . PRO B 1 278 ? 12.513  53.566  4.710   1.00 39.87  ? 373  PRO B CG  1 
ATOM   5932 C CD  . PRO B 1 278 ? 11.291  54.373  4.454   1.00 39.08  ? 373  PRO B CD  1 
ATOM   5933 N N   . GLN B 1 279 ? 11.186  52.710  1.371   1.00 38.86  ? 374  GLN B N   1 
ATOM   5934 C CA  . GLN B 1 279 ? 10.738  51.485  0.701   1.00 43.56  ? 374  GLN B CA  1 
ATOM   5935 C C   . GLN B 1 279 ? 11.680  50.986  -0.405  1.00 39.81  ? 374  GLN B C   1 
ATOM   5936 O O   . GLN B 1 279 ? 12.188  49.843  -0.368  1.00 41.47  ? 374  GLN B O   1 
ATOM   5937 C CB  . GLN B 1 279 ? 9.337   51.735  0.116   1.00 40.53  ? 374  GLN B CB  1 
ATOM   5938 C CG  . GLN B 1 279 ? 8.776   50.556  -0.655  1.00 39.57  ? 374  GLN B CG  1 
ATOM   5939 C CD  . GLN B 1 279 ? 8.485   49.402  0.273   1.00 44.17  ? 374  GLN B CD  1 
ATOM   5940 O OE1 . GLN B 1 279 ? 7.941   49.607  1.360   1.00 44.44  ? 374  GLN B OE1 1 
ATOM   5941 N NE2 . GLN B 1 279 ? 8.853   48.188  -0.132  1.00 41.42  ? 374  GLN B NE2 1 
ATOM   5942 N N   . LEU B 1 280 ? 11.921  51.848  -1.396  1.00 37.40  ? 375  LEU B N   1 
ATOM   5943 C CA  . LEU B 1 280 ? 12.700  51.438  -2.560  1.00 43.64  ? 375  LEU B CA  1 
ATOM   5944 C C   . LEU B 1 280 ? 14.109  51.034  -2.153  1.00 38.63  ? 375  LEU B C   1 
ATOM   5945 O O   . LEU B 1 280 ? 14.635  50.019  -2.632  1.00 41.08  ? 375  LEU B O   1 
ATOM   5946 C CB  . LEU B 1 280 ? 12.718  52.561  -3.606  1.00 43.21  ? 375  LEU B CB  1 
ATOM   5947 C CG  . LEU B 1 280 ? 11.343  53.077  -4.067  1.00 45.90  ? 375  LEU B CG  1 
ATOM   5948 C CD1 . LEU B 1 280 ? 11.468  54.081  -5.225  1.00 46.75  ? 375  LEU B CD1 1 
ATOM   5949 C CD2 . LEU B 1 280 ? 10.395  51.941  -4.439  1.00 42.00  ? 375  LEU B CD2 1 
ATOM   5950 N N   . TYR B 1 281 ? 14.707  51.773  -1.209  1.00 38.56  ? 376  TYR B N   1 
ATOM   5951 C CA  . TYR B 1 281 ? 16.110  51.551  -0.873  1.00 38.26  ? 376  TYR B CA  1 
ATOM   5952 C C   . TYR B 1 281 ? 16.292  50.325  -0.000  1.00 38.63  ? 376  TYR B C   1 
ATOM   5953 O O   . TYR B 1 281 ? 17.297  49.609  -0.135  1.00 38.80  ? 376  TYR B O   1 
ATOM   5954 C CB  . TYR B 1 281 ? 16.696  52.788  -0.187  1.00 38.92  ? 376  TYR B CB  1 
ATOM   5955 C CG  . TYR B 1 281 ? 16.784  53.941  -1.138  1.00 43.98  ? 376  TYR B CG  1 
ATOM   5956 C CD1 . TYR B 1 281 ? 17.776  53.986  -2.120  1.00 42.02  ? 376  TYR B CD1 1 
ATOM   5957 C CD2 . TYR B 1 281 ? 15.853  54.975  -1.087  1.00 44.27  ? 376  TYR B CD2 1 
ATOM   5958 C CE1 . TYR B 1 281 ? 17.846  55.042  -3.019  1.00 47.52  ? 376  TYR B CE1 1 
ATOM   5959 C CE2 . TYR B 1 281 ? 15.914  56.029  -1.983  1.00 46.99  ? 376  TYR B CE2 1 
ATOM   5960 C CZ  . TYR B 1 281 ? 16.910  56.060  -2.942  1.00 50.67  ? 376  TYR B CZ  1 
ATOM   5961 O OH  . TYR B 1 281 ? 16.960  57.111  -3.834  1.00 52.38  ? 376  TYR B OH  1 
ATOM   5962 N N   . LYS B 1 282 ? 15.364  50.083  0.931   1.00 36.21  ? 377  LYS B N   1 
ATOM   5963 C CA  . LYS B 1 282 ? 15.522  48.891  1.750   1.00 39.10  ? 377  LYS B CA  1 
ATOM   5964 C C   . LYS B 1 282 ? 15.338  47.641  0.904   1.00 37.74  ? 377  LYS B C   1 
ATOM   5965 O O   . LYS B 1 282 ? 16.036  46.635  1.131   1.00 37.05  ? 377  LYS B O   1 
ATOM   5966 C CB  . LYS B 1 282 ? 14.568  48.907  2.968   1.00 36.85  ? 377  LYS B CB  1 
ATOM   5967 C CG  . LYS B 1 282 ? 13.065  48.914  2.692   1.00 38.30  ? 377  LYS B CG  1 
ATOM   5968 C CD  . LYS B 1 282 ? 12.279  49.117  4.017   1.00 40.55  ? 377  LYS B CD  1 
ATOM   5969 C CE  . LYS B 1 282 ? 10.771  49.150  3.778   1.00 40.58  ? 377  LYS B CE  1 
ATOM   5970 N NZ  . LYS B 1 282 ? 9.988   48.701  4.957   1.00 39.44  ? 377  LYS B NZ  1 
ATOM   5971 N N   . GLN B 1 283 ? 14.453  47.694  -0.111  1.00 36.99  ? 378  GLN B N   1 
ATOM   5972 C CA  . GLN B 1 283 ? 14.390  46.549  -1.021  1.00 36.36  ? 378  GLN B CA  1 
ATOM   5973 C C   . GLN B 1 283 ? 15.667  46.433  -1.847  1.00 39.63  ? 378  GLN B C   1 
ATOM   5974 O O   . GLN B 1 283 ? 16.129  45.319  -2.123  1.00 40.20  ? 378  GLN B O   1 
ATOM   5975 C CB  . GLN B 1 283 ? 13.177  46.637  -1.948  1.00 35.73  ? 378  GLN B CB  1 
ATOM   5976 C CG  . GLN B 1 283 ? 11.821  46.453  -1.279  1.00 34.47  ? 378  GLN B CG  1 
ATOM   5977 C CD  . GLN B 1 283 ? 10.743  46.369  -2.323  1.00 39.61  ? 378  GLN B CD  1 
ATOM   5978 O OE1 . GLN B 1 283 ? 10.094  47.374  -2.656  1.00 37.74  ? 378  GLN B OE1 1 
ATOM   5979 N NE2 . GLN B 1 283 ? 10.581  45.176  -2.905  1.00 38.22  ? 378  GLN B NE2 1 
ATOM   5980 N N   . MET B 1 284 ? 16.252  47.559  -2.274  1.00 38.33  ? 379  MET B N   1 
ATOM   5981 C CA  . MET B 1 284 ? 17.517  47.441  -3.004  1.00 40.52  ? 379  MET B CA  1 
ATOM   5982 C C   . MET B 1 284 ? 18.585  46.792  -2.141  1.00 40.23  ? 379  MET B C   1 
ATOM   5983 O O   . MET B 1 284 ? 19.404  46.021  -2.653  1.00 42.41  ? 379  MET B O   1 
ATOM   5984 C CB  . MET B 1 284 ? 17.991  48.804  -3.522  1.00 37.84  ? 379  MET B CB  1 
ATOM   5985 C CG  . MET B 1 284 ? 17.205  49.282  -4.745  1.00 44.99  ? 379  MET B CG  1 
ATOM   5986 S SD  . MET B 1 284 ? 17.369  51.072  -5.033  1.00 55.54  ? 379  MET B SD  1 
ATOM   5987 C CE  . MET B 1 284 ? 19.032  51.159  -5.595  1.00 45.89  ? 379  MET B CE  1 
ATOM   5988 N N   . CYS B 1 285 ? 18.577  47.069  -0.829  1.00 37.22  ? 380  CYS B N   1 
ATOM   5989 C CA  . CYS B 1 285 ? 19.544  46.424  0.063   1.00 38.44  ? 380  CYS B CA  1 
ATOM   5990 C C   . CYS B 1 285 ? 19.292  44.927  0.161   1.00 39.54  ? 380  CYS B C   1 
ATOM   5991 O O   . CYS B 1 285 ? 20.239  44.143  0.231   1.00 38.38  ? 380  CYS B O   1 
ATOM   5992 C CB  . CYS B 1 285 ? 19.504  47.060  1.457   1.00 38.73  ? 380  CYS B CB  1 
ATOM   5993 S SG  . CYS B 1 285 ? 20.137  48.759  1.441   1.00 40.39  ? 380  CYS B SG  1 
ATOM   5994 N N   . ILE B 1 286 ? 18.021  44.509  0.194   1.00 40.11  ? 381  ILE B N   1 
ATOM   5995 C CA  . ILE B 1 286 ? 17.750  43.069  0.180   1.00 37.19  ? 381  ILE B CA  1 
ATOM   5996 C C   . ILE B 1 286 ? 18.215  42.453  -1.141  1.00 37.53  ? 381  ILE B C   1 
ATOM   5997 O O   . ILE B 1 286 ? 18.859  41.398  -1.163  1.00 35.94  ? 381  ILE B O   1 
ATOM   5998 C CB  . ILE B 1 286 ? 16.256  42.791  0.437   1.00 39.69  ? 381  ILE B CB  1 
ATOM   5999 C CG1 . ILE B 1 286 ? 15.847  43.279  1.835   1.00 34.60  ? 381  ILE B CG1 1 
ATOM   6000 C CG2 . ILE B 1 286 ? 15.945  41.286  0.238   1.00 36.41  ? 381  ILE B CG2 1 
ATOM   6001 C CD1 . ILE B 1 286 ? 16.592  42.586  2.997   1.00 35.74  ? 381  ILE B CD1 1 
ATOM   6002 N N   . ASN B 1 287 ? 17.960  43.141  -2.237  1.00 36.71  ? 382  ASN B N   1 
ATOM   6003 C CA  . ASN B 1 287 ? 18.402  42.700  -3.538  1.00 39.73  ? 382  ASN B CA  1 
ATOM   6004 C C   . ASN B 1 287 ? 19.939  42.657  -3.607  1.00 41.05  ? 382  ASN B C   1 
ATOM   6005 O O   . ASN B 1 287 ? 20.499  41.966  -4.403  1.00 40.12  ? 382  ASN B O   1 
ATOM   6006 C CB  . ASN B 1 287 ? 17.801  43.563  -4.636  1.00 37.62  ? 382  ASN B CB  1 
ATOM   6007 C CG  . ASN B 1 287 ? 16.356  43.218  -4.930  1.00 37.55  ? 382  ASN B CG  1 
ATOM   6008 O OD1 . ASN B 1 287 ? 15.890  42.190  -4.561  1.00 37.34  ? 382  ASN B OD1 1 
ATOM   6009 N ND2 . ASN B 1 287 ? 15.672  44.082  -5.594  1.00 36.60  ? 382  ASN B ND2 1 
ATOM   6010 N N   . SER B 1 288 ? 20.598  43.376  -2.724  1.00 38.62  ? 383  SER B N   1 
ATOM   6011 C CA  . SER B 1 288 ? 22.041  43.384  -2.662  1.00 42.15  ? 383  SER B CA  1 
ATOM   6012 C C   . SER B 1 288 ? 22.582  42.327  -1.739  1.00 42.90  ? 383  SER B C   1 
ATOM   6013 O O   . SER B 1 288 ? 23.749  42.228  -1.576  1.00 44.96  ? 383  SER B O   1 
ATOM   6014 C CB  . SER B 1 288 ? 22.580  44.713  -2.203  1.00 40.57  ? 383  SER B CB  1 
ATOM   6015 O OG  . SER B 1 288 ? 22.363  45.713  -3.127  1.00 43.22  ? 383  SER B OG  1 
ATOM   6016 N N   . GLY B 1 289 ? 21.725  41.535  -1.136  1.00 41.66  ? 384  GLY B N   1 
ATOM   6017 C CA  . GLY B 1 289 ? 22.159  40.510  -0.226  1.00 40.51  ? 384  GLY B CA  1 
ATOM   6018 C C   . GLY B 1 289 ? 22.253  40.810  1.254   1.00 42.62  ? 384  GLY B C   1 
ATOM   6019 O O   . GLY B 1 289 ? 22.721  39.979  1.982   1.00 38.62  ? 384  GLY B O   1 
ATOM   6020 N N   . PHE B 1 290 ? 21.800  41.975  1.695   1.00 37.96  ? 385  PHE B N   1 
ATOM   6021 C CA  . PHE B 1 290 ? 21.842  42.330  3.109   1.00 38.01  ? 385  PHE B CA  1 
ATOM   6022 C C   . PHE B 1 290 ? 20.996  41.444  4.013   1.00 36.41  ? 385  PHE B C   1 
ATOM   6023 O O   . PHE B 1 290 ? 21.187  41.518  5.200   1.00 39.45  ? 385  PHE B O   1 
ATOM   6024 C CB  . PHE B 1 290 ? 21.589  43.802  3.353   1.00 36.39  ? 385  PHE B CB  1 
ATOM   6025 C CG  . PHE B 1 290 ? 22.687  44.686  2.883   1.00 43.37  ? 385  PHE B CG  1 
ATOM   6026 C CD1 . PHE B 1 290 ? 23.738  44.188  2.199   1.00 46.89  ? 385  PHE B CD1 1 
ATOM   6027 C CD2 . PHE B 1 290 ? 22.640  46.023  3.090   1.00 47.96  ? 385  PHE B CD2 1 
ATOM   6028 C CE1 . PHE B 1 290 ? 24.738  44.999  1.745   1.00 46.43  ? 385  PHE B CE1 1 
ATOM   6029 C CE2 . PHE B 1 290 ? 23.642  46.844  2.639   1.00 48.88  ? 385  PHE B CE2 1 
ATOM   6030 C CZ  . PHE B 1 290 ? 24.696  46.326  1.961   1.00 43.25  ? 385  PHE B CZ  1 
ATOM   6031 N N   . ASP B 1 291 ? 19.999  40.774  3.430   1.00 36.93  ? 386  ASP B N   1 
ATOM   6032 C CA  . ASP B 1 291 ? 19.212  39.689  4.028   1.00 39.33  ? 386  ASP B CA  1 
ATOM   6033 C C   . ASP B 1 291 ? 18.197  40.150  5.077   1.00 36.69  ? 386  ASP B C   1 
ATOM   6034 O O   . ASP B 1 291 ? 17.029  39.747  5.014   1.00 37.14  ? 386  ASP B O   1 
ATOM   6035 C CB  . ASP B 1 291 ? 20.130  38.608  4.634   1.00 36.05  ? 386  ASP B CB  1 
ATOM   6036 C CG  . ASP B 1 291 ? 19.366  37.334  4.960   1.00 40.40  ? 386  ASP B CG  1 
ATOM   6037 O OD1 . ASP B 1 291 ? 18.876  36.667  4.018   1.00 40.37  ? 386  ASP B OD1 1 
ATOM   6038 O OD2 . ASP B 1 291 ? 19.213  37.017  6.162   1.00 42.39  ? 386  ASP B OD2 1 
ATOM   6039 N N   . ARG B 1 292 ? 18.615  40.969  6.045   1.00 34.75  ? 387  ARG B N   1 
ATOM   6040 C CA  . ARG B 1 292 ? 17.718  41.446  7.098   1.00 35.17  ? 387  ARG B CA  1 
ATOM   6041 C C   . ARG B 1 292 ? 18.152  42.854  7.473   1.00 34.68  ? 387  ARG B C   1 
ATOM   6042 O O   . ARG B 1 292 ? 19.240  43.023  8.034   1.00 35.92  ? 387  ARG B O   1 
ATOM   6043 C CB  . ARG B 1 292 ? 17.766  40.523  8.328   1.00 37.84  ? 387  ARG B CB  1 
ATOM   6044 C CG  . ARG B 1 292 ? 17.017  39.187  8.164   1.00 38.92  ? 387  ARG B CG  1 
ATOM   6045 C CD  . ARG B 1 292 ? 17.171  38.263  9.382   1.00 38.66  ? 387  ARG B CD  1 
ATOM   6046 N NE  . ARG B 1 292 ? 16.411  37.030  9.192   1.00 40.46  ? 387  ARG B NE  1 
ATOM   6047 C CZ  . ARG B 1 292 ? 15.968  36.256  10.173  1.00 44.73  ? 387  ARG B CZ  1 
ATOM   6048 N NH1 . ARG B 1 292 ? 16.237  36.522  11.448  1.00 43.61  ? 387  ARG B NH1 1 
ATOM   6049 N NH2 . ARG B 1 292 ? 15.239  35.190  9.872   1.00 43.71  ? 387  ARG B NH2 1 
ATOM   6050 N N   . VAL B 1 293 ? 17.315  43.858  7.194   1.00 32.26  ? 388  VAL B N   1 
ATOM   6051 C CA  . VAL B 1 293 ? 17.678  45.243  7.468   1.00 35.42  ? 388  VAL B CA  1 
ATOM   6052 C C   . VAL B 1 293 ? 16.539  45.973  8.166   1.00 36.17  ? 388  VAL B C   1 
ATOM   6053 O O   . VAL B 1 293 ? 15.354  45.636  8.020   1.00 34.93  ? 388  VAL B O   1 
ATOM   6054 C CB  . VAL B 1 293 ? 18.091  46.002  6.183   1.00 37.64  ? 388  VAL B CB  1 
ATOM   6055 C CG1 . VAL B 1 293 ? 19.287  45.308  5.503   1.00 29.85  ? 388  VAL B CG1 1 
ATOM   6056 C CG2 . VAL B 1 293 ? 16.878  46.196  5.212   1.00 33.14  ? 388  VAL B CG2 1 
ATOM   6057 N N   . PHE B 1 294 ? 16.916  46.987  8.938   1.00 36.01  ? 389  PHE B N   1 
ATOM   6058 C CA  . PHE B 1 294 ? 15.950  47.927  9.486   1.00 34.60  ? 389  PHE B CA  1 
ATOM   6059 C C   . PHE B 1 294 ? 16.535  49.327  9.401   1.00 37.34  ? 389  PHE B C   1 
ATOM   6060 O O   . PHE B 1 294 ? 17.751  49.514  9.316   1.00 35.98  ? 389  PHE B O   1 
ATOM   6061 C CB  . PHE B 1 294 ? 15.556  47.591  10.931  1.00 31.32  ? 389  PHE B CB  1 
ATOM   6062 C CG  . PHE B 1 294 ? 16.666  47.770  11.942  1.00 35.47  ? 389  PHE B CG  1 
ATOM   6063 C CD1 . PHE B 1 294 ? 16.874  49.000  12.558  1.00 35.75  ? 389  PHE B CD1 1 
ATOM   6064 C CD2 . PHE B 1 294 ? 17.458  46.690  12.327  1.00 37.56  ? 389  PHE B CD2 1 
ATOM   6065 C CE1 . PHE B 1 294 ? 17.882  49.172  13.505  1.00 39.16  ? 389  PHE B CE1 1 
ATOM   6066 C CE2 . PHE B 1 294 ? 18.471  46.844  13.293  1.00 38.68  ? 389  PHE B CE2 1 
ATOM   6067 C CZ  . PHE B 1 294 ? 18.680  48.096  13.882  1.00 37.07  ? 389  PHE B CZ  1 
ATOM   6068 N N   . GLU B 1 295 ? 15.635  50.310  9.419   1.00 39.00  ? 390  GLU B N   1 
ATOM   6069 C CA  . GLU B 1 295 ? 15.998  51.720  9.470   1.00 36.97  ? 390  GLU B CA  1 
ATOM   6070 C C   . GLU B 1 295 ? 15.068  52.414  10.461  1.00 38.37  ? 390  GLU B C   1 
ATOM   6071 O O   . GLU B 1 295 ? 13.879  52.084  10.556  1.00 39.34  ? 390  GLU B O   1 
ATOM   6072 C CB  . GLU B 1 295 ? 15.916  52.372  8.080   1.00 34.51  ? 390  GLU B CB  1 
ATOM   6073 C CG  . GLU B 1 295 ? 16.503  53.808  8.030   1.00 38.74  ? 390  GLU B CG  1 
ATOM   6074 C CD  . GLU B 1 295 ? 16.711  54.338  6.621   1.00 40.66  ? 390  GLU B CD  1 
ATOM   6075 O OE1 . GLU B 1 295 ? 17.113  55.513  6.441   1.00 41.13  ? 390  GLU B OE1 1 
ATOM   6076 O OE2 . GLU B 1 295 ? 16.463  53.559  5.667   1.00 41.36  ? 390  GLU B OE2 1 
ATOM   6077 N N   . VAL B 1 296 ? 15.621  53.330  11.245  1.00 37.14  ? 391  VAL B N   1 
ATOM   6078 C CA  . VAL B 1 296 ? 14.842  54.200  12.123  1.00 39.97  ? 391  VAL B CA  1 
ATOM   6079 C C   . VAL B 1 296 ? 15.173  55.616  11.691  1.00 39.08  ? 391  VAL B C   1 
ATOM   6080 O O   . VAL B 1 296 ? 16.290  56.092  11.944  1.00 37.22  ? 391  VAL B O   1 
ATOM   6081 C CB  . VAL B 1 296 ? 15.170  53.984  13.610  1.00 43.26  ? 391  VAL B CB  1 
ATOM   6082 C CG1 . VAL B 1 296 ? 14.410  54.992  14.463  1.00 38.64  ? 391  VAL B CG1 1 
ATOM   6083 C CG2 . VAL B 1 296 ? 14.828  52.551  14.055  1.00 34.77  ? 391  VAL B CG2 1 
ATOM   6084 N N   . ALA B 1 297 ? 14.237  56.290  11.017  1.00 34.34  ? 392  ALA B N   1 
ATOM   6085 C CA  . ALA B 1 297 ? 14.640  57.538  10.376  1.00 34.44  ? 392  ALA B CA  1 
ATOM   6086 C C   . ALA B 1 297 ? 13.408  58.362  10.055  1.00 38.83  ? 392  ALA B C   1 
ATOM   6087 O O   . ALA B 1 297 ? 12.293  57.822  9.992   1.00 39.33  ? 392  ALA B O   1 
ATOM   6088 C CB  . ALA B 1 297 ? 15.460  57.262  9.093   1.00 37.50  ? 392  ALA B CB  1 
ATOM   6089 N N   . PRO B 1 298 ? 13.578  59.674  9.841   1.00 39.19  ? 393  PRO B N   1 
ATOM   6090 C CA  . PRO B 1 298 ? 12.438  60.508  9.439   1.00 41.41  ? 393  PRO B CA  1 
ATOM   6091 C C   . PRO B 1 298 ? 11.910  60.151  8.063   1.00 41.96  ? 393  PRO B C   1 
ATOM   6092 O O   . PRO B 1 298 ? 12.641  59.685  7.183   1.00 39.86  ? 393  PRO B O   1 
ATOM   6093 C CB  . PRO B 1 298 ? 13.008  61.936  9.426   1.00 42.50  ? 393  PRO B CB  1 
ATOM   6094 C CG  . PRO B 1 298 ? 14.372  61.868  10.000  1.00 40.77  ? 393  PRO B CG  1 
ATOM   6095 C CD  . PRO B 1 298 ? 14.811  60.453  10.057  1.00 40.32  ? 393  PRO B CD  1 
ATOM   6096 N N   . VAL B 1 299 ? 10.610  60.399  7.898   1.00 36.02  ? 394  VAL B N   1 
ATOM   6097 C CA  . VAL B 1 299 ? 9.937   60.474  6.612   1.00 39.89  ? 394  VAL B CA  1 
ATOM   6098 C C   . VAL B 1 299 ? 9.097   61.751  6.615   1.00 43.02  ? 394  VAL B C   1 
ATOM   6099 O O   . VAL B 1 299 ? 8.749   62.298  7.673   1.00 38.78  ? 394  VAL B O   1 
ATOM   6100 C CB  . VAL B 1 299 ? 9.052   59.233  6.326   1.00 42.53  ? 394  VAL B CB  1 
ATOM   6101 C CG1 . VAL B 1 299 ? 9.888   57.958  6.331   1.00 36.65  ? 394  VAL B CG1 1 
ATOM   6102 C CG2 . VAL B 1 299 ? 7.944   59.124  7.368   1.00 41.29  ? 394  VAL B CG2 1 
ATOM   6103 N N   . PHE B 1 300 ? 8.767   62.214  5.402   1.00 41.04  ? 395  PHE B N   1 
ATOM   6104 C CA  . PHE B 1 300 ? 8.123   63.501  5.166   1.00 42.52  ? 395  PHE B CA  1 
ATOM   6105 C C   . PHE B 1 300 ? 6.977   63.307  4.189   1.00 47.36  ? 395  PHE B C   1 
ATOM   6106 O O   . PHE B 1 300 ? 7.161   62.693  3.128   1.00 47.01  ? 395  PHE B O   1 
ATOM   6107 C CB  . PHE B 1 300 ? 9.116   64.524  4.594   1.00 39.90  ? 395  PHE B CB  1 
ATOM   6108 C CG  . PHE B 1 300 ? 10.452  64.535  5.298   1.00 40.78  ? 395  PHE B CG  1 
ATOM   6109 C CD1 . PHE B 1 300 ? 10.687  65.404  6.349   1.00 42.54  ? 395  PHE B CD1 1 
ATOM   6110 C CD2 . PHE B 1 300 ? 11.458  63.666  4.922   1.00 38.05  ? 395  PHE B CD2 1 
ATOM   6111 C CE1 . PHE B 1 300 ? 11.910  65.421  7.001   1.00 42.92  ? 395  PHE B CE1 1 
ATOM   6112 C CE2 . PHE B 1 300 ? 12.679  63.673  5.567   1.00 38.71  ? 395  PHE B CE2 1 
ATOM   6113 C CZ  . PHE B 1 300 ? 12.903  64.546  6.616   1.00 40.92  ? 395  PHE B CZ  1 
ATOM   6114 N N   . ARG B 1 301 ? 5.798   63.822  4.535   1.00 42.11  ? 396  ARG B N   1 
ATOM   6115 C CA  . ARG B 1 301 ? 4.664   63.708  3.630   1.00 51.44  ? 396  ARG B CA  1 
ATOM   6116 C C   . ARG B 1 301 ? 3.881   65.014  3.617   1.00 52.58  ? 396  ARG B C   1 
ATOM   6117 O O   . ARG B 1 301 ? 3.712   65.666  4.651   1.00 48.00  ? 396  ARG B O   1 
ATOM   6118 C CB  . ARG B 1 301 ? 3.762   62.522  3.996   1.00 53.66  ? 396  ARG B CB  1 
ATOM   6119 C CG  . ARG B 1 301 ? 3.064   62.608  5.321   1.00 56.74  ? 396  ARG B CG  1 
ATOM   6120 C CD  . ARG B 1 301 ? 2.357   61.281  5.636   1.00 64.22  ? 396  ARG B CD  1 
ATOM   6121 N NE  . ARG B 1 301 ? 1.389   60.891  4.612   1.00 65.88  ? 396  ARG B NE  1 
ATOM   6122 N N   . ALA B 1 302 ? 3.410   65.387  2.430   1.00 55.45  ? 397  ALA B N   1 
ATOM   6123 C CA  . ALA B 1 302 ? 2.917   66.725  2.153   1.00 56.40  ? 397  ALA B CA  1 
ATOM   6124 C C   . ALA B 1 302 ? 1.401   66.773  1.954   1.00 58.73  ? 397  ALA B C   1 
ATOM   6125 O O   . ALA B 1 302 ? 0.904   67.646  1.241   1.00 63.09  ? 397  ALA B O   1 
ATOM   6126 C CB  . ALA B 1 302 ? 3.635   67.291  0.926   1.00 55.19  ? 397  ALA B CB  1 
ATOM   6127 N N   . GLU B 1 303 ? 0.648   65.854  2.565   1.00 60.95  ? 398  GLU B N   1 
ATOM   6128 C CA  . GLU B 1 303 ? -0.810  65.960  2.542   1.00 62.23  ? 398  GLU B CA  1 
ATOM   6129 C C   . GLU B 1 303 ? -1.252  67.155  3.376   1.00 60.82  ? 398  GLU B C   1 
ATOM   6130 O O   . GLU B 1 303 ? -0.781  67.346  4.499   1.00 62.26  ? 398  GLU B O   1 
ATOM   6131 C CB  . GLU B 1 303 ? -1.483  64.695  3.092   1.00 66.23  ? 398  GLU B CB  1 
ATOM   6132 C CG  . GLU B 1 303 ? -1.366  63.418  2.251   1.00 74.83  ? 398  GLU B CG  1 
ATOM   6133 C CD  . GLU B 1 303 ? -0.251  62.505  2.746   1.00 69.71  ? 398  GLU B CD  1 
ATOM   6134 O OE1 . GLU B 1 303 ? 0.860   63.026  2.952   1.00 67.37  ? 398  GLU B OE1 1 
ATOM   6135 O OE2 . GLU B 1 303 ? -0.479  61.286  2.956   1.00 70.69  ? 398  GLU B OE2 1 
ATOM   6136 N N   . ASN B 1 304 ? -2.177  67.952  2.841   1.00 62.39  ? 399  ASN B N   1 
ATOM   6137 C CA  . ASN B 1 304 ? -2.759  69.065  3.594   1.00 62.68  ? 399  ASN B CA  1 
ATOM   6138 C C   . ASN B 1 304 ? -3.954  68.570  4.418   1.00 64.26  ? 399  ASN B C   1 
ATOM   6139 O O   . ASN B 1 304 ? -5.120  68.834  4.110   1.00 67.82  ? 399  ASN B O   1 
ATOM   6140 C CB  . ASN B 1 304 ? -3.160  70.190  2.646   1.00 62.95  ? 399  ASN B CB  1 
ATOM   6141 C CG  . ASN B 1 304 ? -3.429  71.493  3.367   1.00 64.45  ? 399  ASN B CG  1 
ATOM   6142 O OD1 . ASN B 1 304 ? -3.476  71.537  4.596   1.00 63.25  ? 399  ASN B OD1 1 
ATOM   6143 N ND2 . ASN B 1 304 ? -3.615  72.568  2.604   1.00 64.19  ? 399  ASN B ND2 1 
ATOM   6144 N N   . SER B 1 305 ? -3.649  67.848  5.503   1.00 61.86  ? 400  SER B N   1 
ATOM   6145 C CA  . SER B 1 305 ? -4.661  67.395  6.461   1.00 61.50  ? 400  SER B CA  1 
ATOM   6146 C C   . SER B 1 305 ? -4.297  67.872  7.860   1.00 60.91  ? 400  SER B C   1 
ATOM   6147 O O   . SER B 1 305 ? -3.152  67.715  8.298   1.00 57.78  ? 400  SER B O   1 
ATOM   6148 C CB  . SER B 1 305 ? -4.807  65.867  6.485   1.00 65.54  ? 400  SER B CB  1 
ATOM   6149 O OG  . SER B 1 305 ? -4.627  65.283  5.207   1.00 71.33  ? 400  SER B OG  1 
ATOM   6150 N N   . ASN B 1 306 ? -5.269  68.437  8.560   1.00 58.77  ? 401  ASN B N   1 
ATOM   6151 C CA  . ASN B 1 306 ? -5.124  68.829  9.961   1.00 59.66  ? 401  ASN B CA  1 
ATOM   6152 C C   . ASN B 1 306 ? -6.062  67.946  10.780  1.00 59.40  ? 401  ASN B C   1 
ATOM   6153 O O   . ASN B 1 306 ? -7.235  68.273  10.969  1.00 63.02  ? 401  ASN B O   1 
ATOM   6154 C CB  . ASN B 1 306 ? -5.431  70.308  10.151  1.00 61.96  ? 401  ASN B CB  1 
ATOM   6155 C CG  . ASN B 1 306 ? -4.468  71.187  9.402   1.00 63.25  ? 401  ASN B CG  1 
ATOM   6156 O OD1 . ASN B 1 306 ? -3.333  71.396  9.839   1.00 62.41  ? 401  ASN B OD1 1 
ATOM   6157 N ND2 . ASN B 1 306 ? -4.900  71.694  8.253   1.00 63.25  ? 401  ASN B ND2 1 
ATOM   6158 N N   . THR B 1 307 ? -5.540  66.814  11.255  1.00 56.96  ? 402  THR B N   1 
ATOM   6159 C CA  . THR B 1 307 ? -6.293  65.870  12.066  1.00 54.35  ? 402  THR B CA  1 
ATOM   6160 C C   . THR B 1 307 ? -5.537  65.583  13.357  1.00 55.90  ? 402  THR B C   1 
ATOM   6161 O O   . THR B 1 307 ? -4.391  66.006  13.550  1.00 55.06  ? 402  THR B O   1 
ATOM   6162 C CB  . THR B 1 307 ? -6.550  64.546  11.324  1.00 57.62  ? 402  THR B CB  1 
ATOM   6163 O OG1 . THR B 1 307 ? -5.324  63.809  11.203  1.00 56.89  ? 402  THR B OG1 1 
ATOM   6164 C CG2 . THR B 1 307 ? -7.135  64.795  9.934   1.00 57.28  ? 402  THR B CG2 1 
ATOM   6165 N N   . TYR B 1 308 ? -6.197  64.819  14.235  1.00 55.96  ? 403  TYR B N   1 
ATOM   6166 C CA  . TYR B 1 308 ? -5.598  64.403  15.500  1.00 56.02  ? 403  TYR B CA  1 
ATOM   6167 C C   . TYR B 1 308 ? -4.403  63.474  15.302  1.00 50.81  ? 403  TYR B C   1 
ATOM   6168 O O   . TYR B 1 308 ? -3.620  63.289  16.234  1.00 51.10  ? 403  TYR B O   1 
ATOM   6169 C CB  . TYR B 1 308 ? -6.661  63.716  16.386  1.00 56.00  ? 403  TYR B CB  1 
ATOM   6170 C CG  . TYR B 1 308 ? -6.949  62.270  15.991  1.00 59.57  ? 403  TYR B CG  1 
ATOM   6171 C CD1 . TYR B 1 308 ? -6.290  61.206  16.612  1.00 59.88  ? 403  TYR B CD1 1 
ATOM   6172 C CD2 . TYR B 1 308 ? -7.862  61.973  14.983  1.00 58.62  ? 403  TYR B CD2 1 
ATOM   6173 C CE1 . TYR B 1 308 ? -6.529  59.885  16.237  1.00 61.03  ? 403  TYR B CE1 1 
ATOM   6174 C CE2 . TYR B 1 308 ? -8.119  60.664  14.609  1.00 61.66  ? 403  TYR B CE2 1 
ATOM   6175 C CZ  . TYR B 1 308 ? -7.451  59.623  15.234  1.00 65.82  ? 403  TYR B CZ  1 
ATOM   6176 O OH  . TYR B 1 308 ? -7.706  58.326  14.845  1.00 63.97  ? 403  TYR B OH  1 
ATOM   6177 N N   . ARG B 1 309 ? -4.238  62.887  14.121  1.00 51.05  ? 404  ARG B N   1 
ATOM   6178 C CA  . ARG B 1 309 ? -3.223  61.860  13.946  1.00 55.23  ? 404  ARG B CA  1 
ATOM   6179 C C   . ARG B 1 309 ? -2.246  62.074  12.798  1.00 53.73  ? 404  ARG B C   1 
ATOM   6180 O O   . ARG B 1 309 ? -1.326  61.270  12.652  1.00 54.01  ? 404  ARG B O   1 
ATOM   6181 C CB  . ARG B 1 309 ? -3.884  60.491  13.765  1.00 59.20  ? 404  ARG B CB  1 
ATOM   6182 C CG  . ARG B 1 309 ? -4.589  60.312  12.441  1.00 64.66  ? 404  ARG B CG  1 
ATOM   6183 C CD  . ARG B 1 309 ? -5.299  58.962  12.453  1.00 71.26  ? 404  ARG B CD  1 
ATOM   6184 N NE  . ARG B 1 309 ? -5.081  58.185  11.237  1.00 75.14  ? 404  ARG B NE  1 
ATOM   6185 C CZ  . ARG B 1 309 ? -5.082  56.860  11.197  1.00 74.17  ? 404  ARG B CZ  1 
ATOM   6186 N NH1 . ARG B 1 309 ? -5.193  56.136  12.303  1.00 68.49  ? 404  ARG B NH1 1 
ATOM   6187 N NH2 . ARG B 1 309 ? -4.976  56.245  10.020  1.00 73.93  ? 404  ARG B NH2 1 
ATOM   6188 N N   . HIS B 1 310 ? -2.392  63.118  11.994  1.00 55.27  ? 405  HIS B N   1 
ATOM   6189 C CA  . HIS B 1 310 ? -1.520  63.294  10.838  1.00 56.40  ? 405  HIS B CA  1 
ATOM   6190 C C   . HIS B 1 310 ? -0.406  64.286  11.154  1.00 51.46  ? 405  HIS B C   1 
ATOM   6191 O O   . HIS B 1 310 ? -0.661  65.361  11.705  1.00 50.23  ? 405  HIS B O   1 
ATOM   6192 C CB  . HIS B 1 310 ? -2.313  63.745  9.605   1.00 53.42  ? 405  HIS B CB  1 
ATOM   6193 C CG  . HIS B 1 310 ? -1.482  63.822  8.364   1.00 60.63  ? 405  HIS B CG  1 
ATOM   6194 N ND1 . HIS B 1 310 ? -0.945  65.007  7.898   1.00 62.31  ? 405  HIS B ND1 1 
ATOM   6195 C CD2 . HIS B 1 310 ? -1.065  62.858  7.510   1.00 61.72  ? 405  HIS B CD2 1 
ATOM   6196 C CE1 . HIS B 1 310 ? -0.242  64.768  6.804   1.00 62.72  ? 405  HIS B CE1 1 
ATOM   6197 N NE2 . HIS B 1 310 ? -0.299  63.472  6.546   1.00 62.30  ? 405  HIS B NE2 1 
ATOM   6198 N N   . LEU B 1 311 ? 0.825   63.915  10.806  1.00 52.57  ? 406  LEU B N   1 
ATOM   6199 C CA  . LEU B 1 311 ? 1.986   64.790  10.879  1.00 49.85  ? 406  LEU B CA  1 
ATOM   6200 C C   . LEU B 1 311 ? 2.664   64.830  9.513   1.00 52.46  ? 406  LEU B C   1 
ATOM   6201 O O   . LEU B 1 311 ? 2.669   63.835  8.781   1.00 49.46  ? 406  LEU B O   1 
ATOM   6202 C CB  . LEU B 1 311 ? 2.984   64.311  11.943  1.00 46.29  ? 406  LEU B CB  1 
ATOM   6203 C CG  . LEU B 1 311 ? 2.556   64.292  13.419  1.00 49.28  ? 406  LEU B CG  1 
ATOM   6204 C CD1 . LEU B 1 311 ? 3.574   63.522  14.269  1.00 43.89  ? 406  LEU B CD1 1 
ATOM   6205 C CD2 . LEU B 1 311 ? 2.384   65.714  13.945  1.00 48.10  ? 406  LEU B CD2 1 
ATOM   6206 N N   . CYS B 1 312 ? 3.226   65.994  9.165   1.00 48.19  ? 407  CYS B N   1 
ATOM   6207 C CA  . CYS B 1 312 ? 3.957   66.129  7.906   1.00 47.29  ? 407  CYS B CA  1 
ATOM   6208 C C   . CYS B 1 312 ? 5.341   65.520  7.978   1.00 45.58  ? 407  CYS B C   1 
ATOM   6209 O O   . CYS B 1 312 ? 5.920   65.189  6.938   1.00 44.94  ? 407  CYS B O   1 
ATOM   6210 C CB  . CYS B 1 312 ? 4.081   67.599  7.507   1.00 45.95  ? 407  CYS B CB  1 
ATOM   6211 S SG  . CYS B 1 312 ? 2.493   68.373  7.259   1.00 50.27  ? 407  CYS B SG  1 
ATOM   6212 N N   . GLU B 1 313 ? 5.871   65.356  9.180   1.00 44.15  ? 408  GLU B N   1 
ATOM   6213 C CA  . GLU B 1 313 ? 7.153   64.703  9.380   1.00 44.00  ? 408  GLU B CA  1 
ATOM   6214 C C   . GLU B 1 313 ? 7.040   63.793  10.593  1.00 42.33  ? 408  GLU B C   1 
ATOM   6215 O O   . GLU B 1 313 ? 6.475   64.188  11.619  1.00 40.99  ? 408  GLU B O   1 
ATOM   6216 C CB  . GLU B 1 313 ? 8.270   65.734  9.575   1.00 40.86  ? 408  GLU B CB  1 
ATOM   6217 C CG  . GLU B 1 313 ? 9.639   65.106  9.759   1.00 46.37  ? 408  GLU B CG  1 
ATOM   6218 C CD  . GLU B 1 313 ? 10.687  66.130  10.146  1.00 49.60  ? 408  GLU B CD  1 
ATOM   6219 O OE1 . GLU B 1 313 ? 11.802  65.704  10.520  1.00 47.35  ? 408  GLU B OE1 1 
ATOM   6220 O OE2 . GLU B 1 313 ? 10.390  67.353  10.073  1.00 48.09  ? 408  GLU B OE2 1 
ATOM   6221 N N   . TYR B 1 314 ? 7.557   62.575  10.482  1.00 40.04  ? 409  TYR B N   1 
ATOM   6222 C CA  . TYR B 1 314 ? 7.562   61.712  11.660  1.00 41.83  ? 409  TYR B CA  1 
ATOM   6223 C C   . TYR B 1 314 ? 8.670   60.684  11.491  1.00 40.38  ? 409  TYR B C   1 
ATOM   6224 O O   . TYR B 1 314 ? 9.425   60.718  10.517  1.00 42.78  ? 409  TYR B O   1 
ATOM   6225 C CB  . TYR B 1 314 ? 6.184   61.076  11.890  1.00 41.43  ? 409  TYR B CB  1 
ATOM   6226 C CG  . TYR B 1 314 ? 5.722   60.233  10.736  1.00 41.28  ? 409  TYR B CG  1 
ATOM   6227 C CD1 . TYR B 1 314 ? 5.918   58.849  10.740  1.00 44.05  ? 409  TYR B CD1 1 
ATOM   6228 C CD2 . TYR B 1 314 ? 5.119   60.814  9.630   1.00 44.82  ? 409  TYR B CD2 1 
ATOM   6229 C CE1 . TYR B 1 314 ? 5.506   58.067  9.678   1.00 42.96  ? 409  TYR B CE1 1 
ATOM   6230 C CE2 . TYR B 1 314 ? 4.703   60.039  8.556   1.00 48.50  ? 409  TYR B CE2 1 
ATOM   6231 C CZ  . TYR B 1 314 ? 4.902   58.672  8.588   1.00 49.31  ? 409  TYR B CZ  1 
ATOM   6232 O OH  . TYR B 1 314 ? 4.501   57.897  7.526   1.00 57.24  ? 409  TYR B OH  1 
ATOM   6233 N N   . VAL B 1 315 ? 8.804   59.803  12.476  1.00 40.73  ? 410  VAL B N   1 
ATOM   6234 C CA  . VAL B 1 315 ? 9.865   58.798  12.478  1.00 40.18  ? 410  VAL B CA  1 
ATOM   6235 C C   . VAL B 1 315 ? 9.258   57.465  12.075  1.00 38.48  ? 410  VAL B C   1 
ATOM   6236 O O   . VAL B 1 315 ? 8.318   56.983  12.722  1.00 38.47  ? 410  VAL B O   1 
ATOM   6237 C CB  . VAL B 1 315 ? 10.560  58.705  13.847  1.00 41.05  ? 410  VAL B CB  1 
ATOM   6238 C CG1 . VAL B 1 315 ? 11.569  57.566  13.862  1.00 38.62  ? 410  VAL B CG1 1 
ATOM   6239 C CG2 . VAL B 1 315 ? 11.246  60.024  14.167  1.00 39.49  ? 410  VAL B CG2 1 
ATOM   6240 N N   . SER B 1 316 ? 9.783   56.882  10.997  1.00 37.30  ? 411  SER B N   1 
ATOM   6241 C CA  . SER B 1 316 ? 9.371   55.567  10.526  1.00 40.49  ? 411  SER B CA  1 
ATOM   6242 C C   . SER B 1 316 ? 10.359  54.515  11.011  1.00 37.98  ? 411  SER B C   1 
ATOM   6243 O O   . SER B 1 316 ? 11.583  54.714  10.939  1.00 37.08  ? 411  SER B O   1 
ATOM   6244 C CB  . SER B 1 316 ? 9.277   55.531  8.997   1.00 40.58  ? 411  SER B CB  1 
ATOM   6245 O OG  . SER B 1 316 ? 8.652   54.331  8.557   1.00 41.19  ? 411  SER B OG  1 
ATOM   6246 N N   . LEU B 1 317 ? 9.813   53.422  11.551  1.00 37.86  ? 412  LEU B N   1 
ATOM   6247 C CA  . LEU B 1 317 ? 10.554  52.205  11.852  1.00 36.21  ? 412  LEU B CA  1 
ATOM   6248 C C   . LEU B 1 317 ? 10.285  51.245  10.693  1.00 39.48  ? 412  LEU B C   1 
ATOM   6249 O O   . LEU B 1 317 ? 9.136   50.834  10.471  1.00 41.31  ? 412  LEU B O   1 
ATOM   6250 C CB  . LEU B 1 317 ? 10.128  51.610  13.198  1.00 34.29  ? 412  LEU B CB  1 
ATOM   6251 C CG  . LEU B 1 317 ? 9.840   52.593  14.343  1.00 40.38  ? 412  LEU B CG  1 
ATOM   6252 C CD1 . LEU B 1 317 ? 9.323   51.876  15.579  1.00 36.65  ? 412  LEU B CD1 1 
ATOM   6253 C CD2 . LEU B 1 317 ? 11.075  53.409  14.691  1.00 36.78  ? 412  LEU B CD2 1 
ATOM   6254 N N   . ASP B 1 318 ? 11.325  50.937  9.918   1.00 36.44  ? 413  ASP B N   1 
ATOM   6255 C CA  . ASP B 1 318 ? 11.184  50.140  8.708   1.00 36.44  ? 413  ASP B CA  1 
ATOM   6256 C C   . ASP B 1 318 ? 11.968  48.848  8.827   1.00 36.60  ? 413  ASP B C   1 
ATOM   6257 O O   . ASP B 1 318 ? 13.086  48.843  9.354   1.00 37.65  ? 413  ASP B O   1 
ATOM   6258 C CB  . ASP B 1 318 ? 11.648  50.919  7.511   1.00 35.85  ? 413  ASP B CB  1 
ATOM   6259 C CG  . ASP B 1 318 ? 10.577  51.833  6.991   1.00 41.26  ? 413  ASP B CG  1 
ATOM   6260 O OD1 . ASP B 1 318 ? 10.494  52.996  7.451   1.00 40.71  ? 413  ASP B OD1 1 
ATOM   6261 O OD2 . ASP B 1 318 ? 9.788   51.369  6.139   1.00 42.64  ? 413  ASP B OD2 1 
ATOM   6262 N N   . VAL B 1 319 ? 11.359  47.755  8.365   1.00 36.07  ? 414  VAL B N   1 
ATOM   6263 C CA  . VAL B 1 319 ? 11.974  46.430  8.375   1.00 35.13  ? 414  VAL B CA  1 
ATOM   6264 C C   . VAL B 1 319 ? 11.814  45.836  6.981   1.00 38.84  ? 414  VAL B C   1 
ATOM   6265 O O   . VAL B 1 319 ? 10.781  46.048  6.330   1.00 36.89  ? 414  VAL B O   1 
ATOM   6266 C CB  . VAL B 1 319 ? 11.336  45.509  9.439   1.00 38.96  ? 414  VAL B CB  1 
ATOM   6267 C CG1 . VAL B 1 319 ? 12.091  44.151  9.552   1.00 34.84  ? 414  VAL B CG1 1 
ATOM   6268 C CG2 . VAL B 1 319 ? 11.277  46.211  10.800  1.00 39.70  ? 414  VAL B CG2 1 
ATOM   6269 N N   . GLU B 1 320 ? 12.845  45.128  6.511   1.00 31.39  ? 415  GLU B N   1 
ATOM   6270 C CA  . GLU B 1 320 ? 12.769  44.367  5.265   1.00 34.07  ? 415  GLU B CA  1 
ATOM   6271 C C   . GLU B 1 320 ? 13.658  43.131  5.430   1.00 36.49  ? 415  GLU B C   1 
ATOM   6272 O O   . GLU B 1 320 ? 14.731  43.208  6.039   1.00 33.95  ? 415  GLU B O   1 
ATOM   6273 C CB  . GLU B 1 320 ? 13.199  45.230  4.060   1.00 35.97  ? 415  GLU B CB  1 
ATOM   6274 C CG  . GLU B 1 320 ? 12.722  44.748  2.670   1.00 35.98  ? 415  GLU B CG  1 
ATOM   6275 C CD  . GLU B 1 320 ? 11.283  45.157  2.341   1.00 39.05  ? 415  GLU B CD  1 
ATOM   6276 O OE1 . GLU B 1 320 ? 10.706  46.081  2.972   1.00 38.31  ? 415  GLU B OE1 1 
ATOM   6277 O OE2 . GLU B 1 320 ? 10.710  44.544  1.430   1.00 38.38  ? 415  GLU B OE2 1 
ATOM   6278 N N   . MET B 1 321 ? 13.197  41.982  4.936   1.00 36.02  ? 416  MET B N   1 
ATOM   6279 C CA  . MET B 1 321 ? 13.916  40.740  5.221   1.00 34.64  ? 416  MET B CA  1 
ATOM   6280 C C   . MET B 1 321 ? 13.469  39.664  4.247   1.00 35.75  ? 416  MET B C   1 
ATOM   6281 O O   . MET B 1 321 ? 12.360  39.711  3.710   1.00 37.88  ? 416  MET B O   1 
ATOM   6282 C CB  . MET B 1 321 ? 13.680  40.253  6.670   1.00 32.99  ? 416  MET B CB  1 
ATOM   6283 C CG  . MET B 1 321 ? 12.236  39.737  6.929   1.00 34.70  ? 416  MET B CG  1 
ATOM   6284 S SD  . MET B 1 321 ? 11.720  39.449  8.669   1.00 36.92  ? 416  MET B SD  1 
ATOM   6285 C CE  . MET B 1 321 ? 12.884  38.124  9.177   1.00 33.22  ? 416  MET B CE  1 
ATOM   6286 N N   . THR B 1 322 ? 14.326  38.665  4.062   1.00 34.45  ? 417  THR B N   1 
ATOM   6287 C CA  . THR B 1 322 ? 13.996  37.532  3.210   1.00 37.86  ? 417  THR B CA  1 
ATOM   6288 C C   . THR B 1 322 ? 13.181  36.499  3.981   1.00 37.17  ? 417  THR B C   1 
ATOM   6289 O O   . THR B 1 322 ? 13.113  36.506  5.214   1.00 34.56  ? 417  THR B O   1 
ATOM   6290 C CB  . THR B 1 322 ? 15.271  36.861  2.653   1.00 38.61  ? 417  THR B CB  1 
ATOM   6291 O OG1 . THR B 1 322 ? 16.047  36.303  3.719   1.00 35.97  ? 417  THR B OG1 1 
ATOM   6292 C CG2 . THR B 1 322 ? 16.122  37.855  1.933   1.00 36.19  ? 417  THR B CG2 1 
ATOM   6293 N N   . TYR B 1 323 ? 12.574  35.575  3.242   1.00 39.26  ? 418  TYR B N   1 
ATOM   6294 C CA  . TYR B 1 323 ? 11.980  34.389  3.844   1.00 39.96  ? 418  TYR B CA  1 
ATOM   6295 C C   . TYR B 1 323 ? 12.402  33.172  3.021   1.00 39.24  ? 418  TYR B C   1 
ATOM   6296 O O   . TYR B 1 323 ? 13.011  33.291  1.952   1.00 40.65  ? 418  TYR B O   1 
ATOM   6297 C CB  . TYR B 1 323 ? 10.442  34.506  3.951   1.00 35.58  ? 418  TYR B CB  1 
ATOM   6298 C CG  . TYR B 1 323 ? 9.733   34.767  2.632   1.00 38.26  ? 418  TYR B CG  1 
ATOM   6299 C CD1 . TYR B 1 323 ? 9.299   33.704  1.821   1.00 38.66  ? 418  TYR B CD1 1 
ATOM   6300 C CD2 . TYR B 1 323 ? 9.459   36.066  2.216   1.00 35.42  ? 418  TYR B CD2 1 
ATOM   6301 C CE1 . TYR B 1 323 ? 8.643   33.937  0.606   1.00 37.70  ? 418  TYR B CE1 1 
ATOM   6302 C CE2 . TYR B 1 323 ? 8.808   36.306  1.016   1.00 39.79  ? 418  TYR B CE2 1 
ATOM   6303 C CZ  . TYR B 1 323 ? 8.408   35.237  0.209   1.00 38.66  ? 418  TYR B CZ  1 
ATOM   6304 O OH  . TYR B 1 323 ? 7.775   35.486  -0.990  1.00 39.73  ? 418  TYR B OH  1 
ATOM   6305 N N   . LYS B 1 324 ? 12.089  31.985  3.533   1.00 37.93  ? 419  LYS B N   1 
ATOM   6306 C CA  . LYS B 1 324 ? 12.515  30.742  2.892   1.00 40.75  ? 419  LYS B CA  1 
ATOM   6307 C C   . LYS B 1 324 ? 11.516  30.279  1.837   1.00 42.99  ? 419  LYS B C   1 
ATOM   6308 O O   . LYS B 1 324 ? 11.853  30.209  0.649   1.00 41.27  ? 419  LYS B O   1 
ATOM   6309 C CB  . LYS B 1 324 ? 12.720  29.653  3.950   1.00 42.45  ? 419  LYS B CB  1 
ATOM   6310 C CG  . LYS B 1 324 ? 13.813  29.987  4.950   1.00 43.37  ? 419  LYS B CG  1 
ATOM   6311 C CD  . LYS B 1 324 ? 13.800  29.007  6.118   1.00 49.62  ? 419  LYS B CD  1 
ATOM   6312 C CE  . LYS B 1 324 ? 14.980  29.270  7.030   1.00 56.63  ? 419  LYS B CE  1 
ATOM   6313 N NZ  . LYS B 1 324 ? 14.921  28.453  8.280   1.00 67.05  ? 419  LYS B NZ  1 
ATOM   6314 N N   . TYR B 1 325 ? 10.280  29.968  2.257   1.00 39.04  ? 420  TYR B N   1 
ATOM   6315 C CA  . TYR B 1 325 ? 9.277   29.428  1.343   1.00 42.30  ? 420  TYR B CA  1 
ATOM   6316 C C   . TYR B 1 325 ? 7.928   30.144  1.434   1.00 43.61  ? 420  TYR B C   1 
ATOM   6317 O O   . TYR B 1 325 ? 7.184   30.178  0.449   1.00 47.19  ? 420  TYR B O   1 
ATOM   6318 C CB  . TYR B 1 325 ? 9.120   27.913  1.595   1.00 42.93  ? 420  TYR B CB  1 
ATOM   6319 C CG  . TYR B 1 325 ? 10.387  27.162  1.238   1.00 45.34  ? 420  TYR B CG  1 
ATOM   6320 C CD1 . TYR B 1 325 ? 10.762  27.009  -0.094  1.00 48.30  ? 420  TYR B CD1 1 
ATOM   6321 C CD2 . TYR B 1 325 ? 11.241  26.647  2.229   1.00 47.27  ? 420  TYR B CD2 1 
ATOM   6322 C CE1 . TYR B 1 325 ? 11.935  26.358  -0.449  1.00 46.86  ? 420  TYR B CE1 1 
ATOM   6323 C CE2 . TYR B 1 325 ? 12.431  25.967  1.870   1.00 49.63  ? 420  TYR B CE2 1 
ATOM   6324 C CZ  . TYR B 1 325 ? 12.759  25.831  0.526   1.00 47.81  ? 420  TYR B CZ  1 
ATOM   6325 O OH  . TYR B 1 325 ? 13.920  25.184  0.113   1.00 55.69  ? 420  TYR B OH  1 
ATOM   6326 N N   . ASP B 1 326 ? 7.609   30.745  2.583   1.00 42.49  ? 421  ASP B N   1 
ATOM   6327 C CA  . ASP B 1 326 ? 6.274   31.284  2.841   1.00 42.50  ? 421  ASP B CA  1 
ATOM   6328 C C   . ASP B 1 326 ? 6.418   32.651  3.496   1.00 40.06  ? 421  ASP B C   1 
ATOM   6329 O O   . ASP B 1 326 ? 7.074   32.764  4.531   1.00 38.94  ? 421  ASP B O   1 
ATOM   6330 C CB  . ASP B 1 326 ? 5.497   30.316  3.748   1.00 43.84  ? 421  ASP B CB  1 
ATOM   6331 C CG  . ASP B 1 326 ? 4.013   30.634  3.841   1.00 49.68  ? 421  ASP B CG  1 
ATOM   6332 O OD1 . ASP B 1 326 ? 3.605   31.811  3.730   1.00 46.53  ? 421  ASP B OD1 1 
ATOM   6333 O OD2 . ASP B 1 326 ? 3.248   29.672  4.060   1.00 56.43  ? 421  ASP B OD2 1 
ATOM   6334 N N   . TYR B 1 327 ? 5.817   33.691  2.900   1.00 39.75  ? 422  TYR B N   1 
ATOM   6335 C CA  . TYR B 1 327 ? 5.926   35.032  3.481   1.00 42.56  ? 422  TYR B CA  1 
ATOM   6336 C C   . TYR B 1 327 ? 5.348   35.098  4.899   1.00 40.61  ? 422  TYR B C   1 
ATOM   6337 O O   . TYR B 1 327 ? 5.735   35.982  5.679   1.00 39.74  ? 422  TYR B O   1 
ATOM   6338 C CB  . TYR B 1 327 ? 5.233   36.065  2.575   1.00 40.04  ? 422  TYR B CB  1 
ATOM   6339 C CG  . TYR B 1 327 ? 3.730   36.201  2.814   1.00 40.83  ? 422  TYR B CG  1 
ATOM   6340 C CD1 . TYR B 1 327 ? 3.203   37.314  3.467   1.00 39.16  ? 422  TYR B CD1 1 
ATOM   6341 C CD2 . TYR B 1 327 ? 2.842   35.205  2.399   1.00 45.72  ? 422  TYR B CD2 1 
ATOM   6342 C CE1 . TYR B 1 327 ? 1.827   37.436  3.689   1.00 43.70  ? 422  TYR B CE1 1 
ATOM   6343 C CE2 . TYR B 1 327 ? 1.464   35.313  2.625   1.00 44.38  ? 422  TYR B CE2 1 
ATOM   6344 C CZ  . TYR B 1 327 ? 0.966   36.431  3.272   1.00 45.22  ? 422  TYR B CZ  1 
ATOM   6345 O OH  . TYR B 1 327 ? -0.397  36.539  3.499   1.00 45.85  ? 422  TYR B OH  1 
ATOM   6346 N N   . LEU B 1 328 ? 4.469   34.159  5.267   1.00 39.51  ? 423  LEU B N   1 
ATOM   6347 C CA  . LEU B 1 328 ? 3.938   34.130  6.628   1.00 41.54  ? 423  LEU B CA  1 
ATOM   6348 C C   . LEU B 1 328 ? 5.035   33.901  7.665   1.00 41.25  ? 423  LEU B C   1 
ATOM   6349 O O   . LEU B 1 328 ? 4.887   34.342  8.810   1.00 39.85  ? 423  LEU B O   1 
ATOM   6350 C CB  . LEU B 1 328 ? 2.835   33.062  6.759   1.00 40.39  ? 423  LEU B CB  1 
ATOM   6351 C CG  . LEU B 1 328 ? 1.551   33.420  6.000   1.00 47.30  ? 423  LEU B CG  1 
ATOM   6352 C CD1 . LEU B 1 328 ? 0.536   32.273  6.007   1.00 46.56  ? 423  LEU B CD1 1 
ATOM   6353 C CD2 . LEU B 1 328 ? 0.923   34.686  6.588   1.00 42.85  ? 423  LEU B CD2 1 
ATOM   6354 N N   . GLU B 1 329 ? 6.151   33.253  7.288   1.00 39.31  ? 424  GLU B N   1 
ATOM   6355 C CA  . GLU B 1 329 ? 7.311   33.209  8.183   1.00 40.46  ? 424  GLU B CA  1 
ATOM   6356 C C   . GLU B 1 329 ? 7.640   34.605  8.710   1.00 41.91  ? 424  GLU B C   1 
ATOM   6357 O O   . GLU B 1 329 ? 7.892   34.790  9.907   1.00 37.93  ? 424  GLU B O   1 
ATOM   6358 C CB  . GLU B 1 329 ? 8.549   32.642  7.475   1.00 40.83  ? 424  GLU B CB  1 
ATOM   6359 C CG  . GLU B 1 329 ? 8.456   31.225  6.914   1.00 43.55  ? 424  GLU B CG  1 
ATOM   6360 C CD  . GLU B 1 329 ? 9.520   30.967  5.821   1.00 44.41  ? 424  GLU B CD  1 
ATOM   6361 O OE1 . GLU B 1 329 ? 10.623  31.579  5.890   1.00 40.10  ? 424  GLU B OE1 1 
ATOM   6362 O OE2 . GLU B 1 329 ? 9.237   30.169  4.886   1.00 42.58  ? 424  GLU B OE2 1 
ATOM   6363 N N   . ASN B 1 330 ? 7.666   35.597  7.813   1.00 38.45  ? 425  ASN B N   1 
ATOM   6364 C CA  . ASN B 1 330 ? 7.990   36.960  8.223   1.00 37.15  ? 425  ASN B CA  1 
ATOM   6365 C C   . ASN B 1 330 ? 6.854   37.586  9.031   1.00 39.30  ? 425  ASN B C   1 
ATOM   6366 O O   . ASN B 1 330 ? 7.103   38.335  9.985   1.00 36.99  ? 425  ASN B O   1 
ATOM   6367 C CB  . ASN B 1 330 ? 8.299   37.826  6.995   1.00 34.51  ? 425  ASN B CB  1 
ATOM   6368 C CG  . ASN B 1 330 ? 9.557   37.373  6.238   1.00 37.21  ? 425  ASN B CG  1 
ATOM   6369 O OD1 . ASN B 1 330 ? 10.304  36.492  6.665   1.00 39.00  ? 425  ASN B OD1 1 
ATOM   6370 N ND2 . ASN B 1 330 ? 9.810   38.018  5.142   1.00 36.82  ? 425  ASN B ND2 1 
ATOM   6371 N N   . VAL B 1 331 ? 5.601   37.296  8.671   1.00 39.03  ? 426  VAL B N   1 
ATOM   6372 C CA  . VAL B 1 331 ? 4.485   37.925  9.378   1.00 37.61  ? 426  VAL B CA  1 
ATOM   6373 C C   . VAL B 1 331 ? 4.504   37.521  10.843  1.00 39.39  ? 426  VAL B C   1 
ATOM   6374 O O   . VAL B 1 331 ? 4.434   38.366  11.746  1.00 37.10  ? 426  VAL B O   1 
ATOM   6375 C CB  . VAL B 1 331 ? 3.147   37.571  8.710   1.00 37.23  ? 426  VAL B CB  1 
ATOM   6376 C CG1 . VAL B 1 331 ? 1.976   38.136  9.544   1.00 37.04  ? 426  VAL B CG1 1 
ATOM   6377 C CG2 . VAL B 1 331 ? 3.111   38.133  7.291   1.00 37.53  ? 426  VAL B CG2 1 
ATOM   6378 N N   . HIS B 1 332 ? 4.652   36.222  11.101  1.00 38.13  ? 427  HIS B N   1 
ATOM   6379 C CA  . HIS B 1 332 ? 4.779   35.763  12.476  1.00 41.99  ? 427  HIS B CA  1 
ATOM   6380 C C   . HIS B 1 332 ? 5.975   36.414  13.165  1.00 40.07  ? 427  HIS B C   1 
ATOM   6381 O O   . HIS B 1 332 ? 5.883   36.823  14.331  1.00 38.82  ? 427  HIS B O   1 
ATOM   6382 C CB  . HIS B 1 332 ? 4.866   34.238  12.493  1.00 43.80  ? 427  HIS B CB  1 
ATOM   6383 C CG  . HIS B 1 332 ? 3.632   33.576  11.958  1.00 49.41  ? 427  HIS B CG  1 
ATOM   6384 N ND1 . HIS B 1 332 ? 2.360   33.934  12.367  1.00 49.76  ? 427  HIS B ND1 1 
ATOM   6385 C CD2 . HIS B 1 332 ? 3.469   32.590  11.043  1.00 48.58  ? 427  HIS B CD2 1 
ATOM   6386 C CE1 . HIS B 1 332 ? 1.472   33.191  11.730  1.00 49.08  ? 427  HIS B CE1 1 
ATOM   6387 N NE2 . HIS B 1 332 ? 2.118   32.370  10.920  1.00 49.52  ? 427  HIS B NE2 1 
ATOM   6388 N N   . PHE B 1 333 ? 7.061   36.636  12.429  1.00 38.72  ? 428  PHE B N   1 
ATOM   6389 C CA  . PHE B 1 333 ? 8.195   37.330  13.035  1.00 39.73  ? 428  PHE B CA  1 
ATOM   6390 C C   . PHE B 1 333 ? 7.823   38.766  13.403  1.00 36.03  ? 428  PHE B C   1 
ATOM   6391 O O   . PHE B 1 333 ? 8.062   39.201  14.538  1.00 36.80  ? 428  PHE B O   1 
ATOM   6392 C CB  . PHE B 1 333 ? 9.424   37.282  12.114  1.00 35.78  ? 428  PHE B CB  1 
ATOM   6393 C CG  . PHE B 1 333 ? 10.611  38.035  12.667  1.00 38.73  ? 428  PHE B CG  1 
ATOM   6394 C CD1 . PHE B 1 333 ? 11.436  37.453  13.620  1.00 38.71  ? 428  PHE B CD1 1 
ATOM   6395 C CD2 . PHE B 1 333 ? 10.870  39.344  12.267  1.00 36.19  ? 428  PHE B CD2 1 
ATOM   6396 C CE1 . PHE B 1 333 ? 12.515  38.156  14.150  1.00 43.46  ? 428  PHE B CE1 1 
ATOM   6397 C CE2 . PHE B 1 333 ? 11.936  40.052  12.792  1.00 36.96  ? 428  PHE B CE2 1 
ATOM   6398 C CZ  . PHE B 1 333 ? 12.768  39.463  13.723  1.00 35.99  ? 428  PHE B CZ  1 
ATOM   6399 N N   . TYR B 1 334 ? 7.156   39.498  12.497  1.00 36.78  ? 429  TYR B N   1 
ATOM   6400 C CA  . TYR B 1 334 ? 6.743   40.855  12.873  1.00 35.41  ? 429  TYR B CA  1 
ATOM   6401 C C   . TYR B 1 334 ? 5.794   40.812  14.061  1.00 37.45  ? 429  TYR B C   1 
ATOM   6402 O O   . TYR B 1 334 ? 5.881   41.652  14.979  1.00 36.52  ? 429  TYR B O   1 
ATOM   6403 C CB  . TYR B 1 334 ? 6.082   41.583  11.701  1.00 37.82  ? 429  TYR B CB  1 
ATOM   6404 C CG  . TYR B 1 334 ? 6.910   41.592  10.438  1.00 37.34  ? 429  TYR B CG  1 
ATOM   6405 C CD1 . TYR B 1 334 ? 8.290   41.739  10.497  1.00 36.51  ? 429  TYR B CD1 1 
ATOM   6406 C CD2 . TYR B 1 334 ? 6.311   41.469  9.186   1.00 37.98  ? 429  TYR B CD2 1 
ATOM   6407 C CE1 . TYR B 1 334 ? 9.056   41.741  9.358   1.00 40.14  ? 429  TYR B CE1 1 
ATOM   6408 C CE2 . TYR B 1 334 ? 7.084   41.461  8.020   1.00 36.07  ? 429  TYR B CE2 1 
ATOM   6409 C CZ  . TYR B 1 334 ? 8.452   41.601  8.124   1.00 37.51  ? 429  TYR B CZ  1 
ATOM   6410 O OH  . TYR B 1 334 ? 9.237   41.604  7.001   1.00 37.36  ? 429  TYR B OH  1 
ATOM   6411 N N   . ASP B 1 335 ? 4.923   39.795  14.103  1.00 37.82  ? 430  ASP B N   1 
ATOM   6412 C CA  . ASP B 1 335 ? 3.990   39.697  15.215  1.00 36.59  ? 430  ASP B CA  1 
ATOM   6413 C C   . ASP B 1 335 ? 4.764   39.509  16.514  1.00 40.24  ? 430  ASP B C   1 
ATOM   6414 O O   . ASP B 1 335 ? 4.522   40.210  17.515  1.00 37.03  ? 430  ASP B O   1 
ATOM   6415 C CB  . ASP B 1 335 ? 3.012   38.548  14.948  1.00 38.47  ? 430  ASP B CB  1 
ATOM   6416 C CG  . ASP B 1 335 ? 2.109   38.235  16.117  1.00 38.56  ? 430  ASP B CG  1 
ATOM   6417 O OD1 . ASP B 1 335 ? 1.582   39.174  16.769  1.00 38.61  ? 430  ASP B OD1 1 
ATOM   6418 O OD2 . ASP B 1 335 ? 1.866   37.026  16.351  1.00 40.95  ? 430  ASP B OD2 1 
ATOM   6419 N N   . SER B 1 336 ? 5.767   38.621  16.483  1.00 36.17  ? 431  SER B N   1 
ATOM   6420 C CA  . SER B 1 336 ? 6.522   38.374  17.705  1.00 38.85  ? 431  SER B CA  1 
ATOM   6421 C C   . SER B 1 336 ? 7.268   39.636  18.129  1.00 37.24  ? 431  SER B C   1 
ATOM   6422 O O   . SER B 1 336 ? 7.304   39.965  19.326  1.00 40.26  ? 431  SER B O   1 
ATOM   6423 C CB  . SER B 1 336 ? 7.471   37.185  17.512  1.00 37.57  ? 431  SER B CB  1 
ATOM   6424 O OG  . SER B 1 336 ? 8.534   37.567  16.660  1.00 48.25  ? 431  SER B OG  1 
ATOM   6425 N N   . MET B 1 337 ? 7.727   40.429  17.156  1.00 34.88  ? 432  MET B N   1 
ATOM   6426 C CA  . MET B 1 337 ? 8.366   41.695  17.481  1.00 37.25  ? 432  MET B CA  1 
ATOM   6427 C C   . MET B 1 337 ? 7.419   42.595  18.273  1.00 35.34  ? 432  MET B C   1 
ATOM   6428 O O   . MET B 1 337 ? 7.765   43.091  19.360  1.00 36.43  ? 432  MET B O   1 
ATOM   6429 C CB  . MET B 1 337 ? 8.829   42.370  16.191  1.00 35.06  ? 432  MET B CB  1 
ATOM   6430 C CG  . MET B 1 337 ? 9.466   43.737  16.394  1.00 37.00  ? 432  MET B CG  1 
ATOM   6431 S SD  . MET B 1 337 ? 10.027  44.393  14.829  1.00 44.04  ? 432  MET B SD  1 
ATOM   6432 C CE  . MET B 1 337 ? 8.529   44.884  13.991  1.00 39.21  ? 432  MET B CE  1 
ATOM   6433 N N   . PHE B 1 338 ? 6.183   42.748  17.799  1.00 35.91  ? 433  PHE B N   1 
ATOM   6434 C CA  . PHE B 1 338 ? 5.284   43.637  18.537  1.00 36.51  ? 433  PHE B CA  1 
ATOM   6435 C C   . PHE B 1 338 ? 4.928   43.061  19.895  1.00 38.29  ? 433  PHE B C   1 
ATOM   6436 O O   . PHE B 1 338 ? 4.893   43.803  20.889  1.00 36.09  ? 433  PHE B O   1 
ATOM   6437 C CB  . PHE B 1 338 ? 4.033   43.953  17.728  1.00 38.66  ? 433  PHE B CB  1 
ATOM   6438 C CG  . PHE B 1 338 ? 4.174   45.209  16.952  1.00 40.02  ? 433  PHE B CG  1 
ATOM   6439 C CD1 . PHE B 1 338 ? 3.874   46.435  17.538  1.00 42.52  ? 433  PHE B CD1 1 
ATOM   6440 C CD2 . PHE B 1 338 ? 4.711   45.189  15.676  1.00 39.07  ? 433  PHE B CD2 1 
ATOM   6441 C CE1 . PHE B 1 338 ? 4.055   47.620  16.834  1.00 44.77  ? 433  PHE B CE1 1 
ATOM   6442 C CE2 . PHE B 1 338 ? 4.890   46.365  14.965  1.00 39.99  ? 433  PHE B CE2 1 
ATOM   6443 C CZ  . PHE B 1 338 ? 4.548   47.583  15.541  1.00 39.40  ? 433  PHE B CZ  1 
ATOM   6444 N N   . LYS B 1 339 ? 4.739   41.734  19.982  1.00 36.63  ? 434  LYS B N   1 
ATOM   6445 C CA  . LYS B 1 339 ? 4.390   41.182  21.281  1.00 38.39  ? 434  LYS B CA  1 
ATOM   6446 C C   . LYS B 1 339 ? 5.509   41.481  22.258  1.00 40.94  ? 434  LYS B C   1 
ATOM   6447 O O   . LYS B 1 339 ? 5.260   41.879  23.407  1.00 40.25  ? 434  LYS B O   1 
ATOM   6448 C CB  . LYS B 1 339 ? 4.122   39.669  21.180  1.00 37.95  ? 434  LYS B CB  1 
ATOM   6449 C CG  . LYS B 1 339 ? 3.045   39.291  20.163  1.00 40.37  ? 434  LYS B CG  1 
ATOM   6450 C CD  . LYS B 1 339 ? 2.321   37.985  20.459  1.00 42.37  ? 434  LYS B CD  1 
ATOM   6451 C CE  . LYS B 1 339 ? 3.231   36.813  20.743  1.00 44.79  ? 434  LYS B CE  1 
ATOM   6452 N NZ  . LYS B 1 339 ? 2.608   35.466  20.490  1.00 42.20  ? 434  LYS B NZ  1 
ATOM   6453 N N   . HIS B 1 340 ? 6.751   41.415  21.760  1.00 39.06  ? 435  HIS B N   1 
ATOM   6454 C CA  . HIS B 1 340 ? 7.922   41.667  22.589  1.00 40.05  ? 435  HIS B CA  1 
ATOM   6455 C C   . HIS B 1 340 ? 7.954   43.121  23.044  1.00 37.94  ? 435  HIS B C   1 
ATOM   6456 O O   . HIS B 1 340 ? 8.159   43.403  24.234  1.00 39.28  ? 435  HIS B O   1 
ATOM   6457 C CB  . HIS B 1 340 ? 9.188   41.271  21.801  1.00 38.72  ? 435  HIS B CB  1 
ATOM   6458 C CG  . HIS B 1 340 ? 10.467  41.609  22.496  1.00 42.88  ? 435  HIS B CG  1 
ATOM   6459 N ND1 . HIS B 1 340 ? 10.941  40.888  23.573  1.00 45.38  ? 435  HIS B ND1 1 
ATOM   6460 C CD2 . HIS B 1 340 ? 11.364  42.601  22.281  1.00 40.88  ? 435  HIS B CD2 1 
ATOM   6461 C CE1 . HIS B 1 340 ? 12.076  41.423  23.991  1.00 42.10  ? 435  HIS B CE1 1 
ATOM   6462 N NE2 . HIS B 1 340 ? 12.354  42.462  23.225  1.00 41.55  ? 435  HIS B NE2 1 
ATOM   6463 N N   . ILE B 1 341 ? 7.662   44.050  22.131  1.00 38.36  ? 436  ILE B N   1 
ATOM   6464 C CA  . ILE B 1 341 ? 7.568   45.451  22.522  1.00 38.91  ? 436  ILE B CA  1 
ATOM   6465 C C   . ILE B 1 341 ? 6.524   45.613  23.620  1.00 40.30  ? 436  ILE B C   1 
ATOM   6466 O O   . ILE B 1 341 ? 6.803   46.184  24.685  1.00 37.87  ? 436  ILE B O   1 
ATOM   6467 C CB  . ILE B 1 341 ? 7.253   46.333  21.299  1.00 38.46  ? 436  ILE B CB  1 
ATOM   6468 C CG1 . ILE B 1 341 ? 8.450   46.380  20.349  1.00 35.41  ? 436  ILE B CG1 1 
ATOM   6469 C CG2 . ILE B 1 341 ? 6.876   47.758  21.731  1.00 38.62  ? 436  ILE B CG2 1 
ATOM   6470 C CD1 . ILE B 1 341 ? 8.098   46.890  18.915  1.00 37.36  ? 436  ILE B CD1 1 
ATOM   6471 N N   . PHE B 1 342 ? 5.333   45.023  23.425  1.00 37.25  ? 437  PHE B N   1 
ATOM   6472 C CA  . PHE B 1 342 ? 4.308   45.205  24.446  1.00 42.13  ? 437  PHE B CA  1 
ATOM   6473 C C   . PHE B 1 342 ? 4.788   44.603  25.755  1.00 41.75  ? 437  PHE B C   1 
ATOM   6474 O O   . PHE B 1 342 ? 4.727   45.259  26.807  1.00 38.25  ? 437  PHE B O   1 
ATOM   6475 C CB  . PHE B 1 342 ? 2.972   44.587  24.014  1.00 39.87  ? 437  PHE B CB  1 
ATOM   6476 C CG  . PHE B 1 342 ? 2.446   45.102  22.691  1.00 40.86  ? 437  PHE B CG  1 
ATOM   6477 C CD1 . PHE B 1 342 ? 2.634   46.432  22.309  1.00 36.60  ? 437  PHE B CD1 1 
ATOM   6478 C CD2 . PHE B 1 342 ? 1.761   44.241  21.819  1.00 39.73  ? 437  PHE B CD2 1 
ATOM   6479 C CE1 . PHE B 1 342 ? 2.150   46.903  21.086  1.00 37.38  ? 437  PHE B CE1 1 
ATOM   6480 C CE2 . PHE B 1 342 ? 1.270   44.702  20.592  1.00 39.46  ? 437  PHE B CE2 1 
ATOM   6481 C CZ  . PHE B 1 342 ? 1.463   46.039  20.225  1.00 36.86  ? 437  PHE B CZ  1 
ATOM   6482 N N   . THR B 1 343 ? 5.400   43.410  25.682  1.00 41.01  ? 438  THR B N   1 
ATOM   6483 C CA  . THR B 1 343 ? 5.823   42.744  26.909  1.00 39.56  ? 438  THR B CA  1 
ATOM   6484 C C   . THR B 1 343 ? 6.818   43.610  27.644  1.00 42.32  ? 438  THR B C   1 
ATOM   6485 O O   . THR B 1 343 ? 6.723   43.792  28.864  1.00 41.92  ? 438  THR B O   1 
ATOM   6486 C CB  . THR B 1 343 ? 6.442   41.381  26.590  1.00 40.04  ? 438  THR B CB  1 
ATOM   6487 O OG1 . THR B 1 343 ? 5.447   40.541  26.004  1.00 39.80  ? 438  THR B OG1 1 
ATOM   6488 C CG2 . THR B 1 343 ? 6.988   40.706  27.869  1.00 38.99  ? 438  THR B CG2 1 
ATOM   6489 N N   . GLU B 1 344 ? 7.743   44.209  26.897  1.00 41.58  ? 439  GLU B N   1 
ATOM   6490 C CA  . GLU B 1 344 ? 8.821   44.945  27.539  1.00 42.79  ? 439  GLU B CA  1 
ATOM   6491 C C   . GLU B 1 344 ? 8.319   46.278  28.057  1.00 46.37  ? 439  GLU B C   1 
ATOM   6492 O O   . GLU B 1 344 ? 8.751   46.727  29.127  1.00 46.66  ? 439  GLU B O   1 
ATOM   6493 C CB  . GLU B 1 344 ? 9.985   45.121  26.557  1.00 43.82  ? 439  GLU B CB  1 
ATOM   6494 C CG  . GLU B 1 344 ? 10.716  43.820  26.253  1.00 40.93  ? 439  GLU B CG  1 
ATOM   6495 C CD  . GLU B 1 344 ? 11.389  43.254  27.495  1.00 51.79  ? 439  GLU B CD  1 
ATOM   6496 O OE1 . GLU B 1 344 ? 12.184  43.996  28.113  1.00 52.83  ? 439  GLU B OE1 1 
ATOM   6497 O OE2 . GLU B 1 344 ? 11.095  42.093  27.879  1.00 53.43  ? 439  GLU B OE2 1 
ATOM   6498 N N   . LEU B 1 345 ? 7.357   46.891  27.355  1.00 41.71  ? 440  LEU B N   1 
ATOM   6499 C CA  . LEU B 1 345 ? 6.815   48.149  27.862  1.00 46.34  ? 440  LEU B CA  1 
ATOM   6500 C C   . LEU B 1 345 ? 6.028   47.932  29.148  1.00 44.89  ? 440  LEU B C   1 
ATOM   6501 O O   . LEU B 1 345 ? 6.085   48.759  30.061  1.00 49.67  ? 440  LEU B O   1 
ATOM   6502 C CB  . LEU B 1 345 ? 5.934   48.820  26.808  1.00 42.88  ? 440  LEU B CB  1 
ATOM   6503 C CG  . LEU B 1 345 ? 6.621   49.546  25.661  1.00 43.60  ? 440  LEU B CG  1 
ATOM   6504 C CD1 . LEU B 1 345 ? 5.561   50.044  24.672  1.00 44.72  ? 440  LEU B CD1 1 
ATOM   6505 C CD2 . LEU B 1 345 ? 7.456   50.722  26.178  1.00 42.51  ? 440  LEU B CD2 1 
ATOM   6506 N N   . SER B 1 346 ? 5.255   46.879  29.178  1.00 46.98  ? 441  SER B N   1 
ATOM   6507 C CA  . SER B 1 346 ? 4.369   46.592  30.269  1.00 46.67  ? 441  SER B CA  1 
ATOM   6508 C C   . SER B 1 346 ? 4.971   45.965  31.500  1.00 52.63  ? 441  SER B C   1 
ATOM   6509 O O   . SER B 1 346 ? 4.265   45.671  32.425  1.00 55.11  ? 441  SER B O   1 
ATOM   6510 C CB  . SER B 1 346 ? 3.261   45.701  29.763  1.00 41.56  ? 441  SER B CB  1 
ATOM   6511 O OG  . SER B 1 346 ? 2.689   46.225  28.608  1.00 48.40  ? 441  SER B OG  1 
ATOM   6512 N N   . LYS B 1 347 ? 6.268   45.773  31.536  1.00 51.30  ? 442  LYS B N   1 
ATOM   6513 C CA  . LYS B 1 347 ? 6.833   45.130  32.687  1.00 57.94  ? 442  LYS B CA  1 
ATOM   6514 C C   . LYS B 1 347 ? 7.085   46.065  33.832  1.00 64.31  ? 442  LYS B C   1 
ATOM   6515 O O   . LYS B 1 347 ? 6.910   47.245  33.726  1.00 60.27  ? 442  LYS B O   1 
ATOM   6516 C CB  . LYS B 1 347 ? 8.046   44.293  32.334  1.00 55.26  ? 442  LYS B CB  1 
ATOM   6517 C CG  . LYS B 1 347 ? 9.267   45.063  31.954  1.00 57.37  ? 442  LYS B CG  1 
ATOM   6518 C CD  . LYS B 1 347 ? 10.235  44.118  31.277  1.00 61.76  ? 442  LYS B CD  1 
ATOM   6519 C CE  . LYS B 1 347 ? 11.627  44.705  31.230  1.00 64.77  ? 442  LYS B CE  1 
ATOM   6520 N NZ  . LYS B 1 347 ? 11.535  46.119  30.823  1.00 57.25  ? 442  LYS B NZ  1 
ATOM   6521 N N   . GLY B 1 348 ? 7.473   45.511  34.954  1.00 81.11  ? 443  GLY B N   1 
ATOM   6522 C CA  . GLY B 1 348 ? 7.700   46.314  36.126  1.00 78.33  ? 443  GLY B CA  1 
ATOM   6523 C C   . GLY B 1 348 ? 9.016   47.026  36.121  1.00 79.41  ? 443  GLY B C   1 
ATOM   6524 O O   . GLY B 1 348 ? 9.880   46.719  35.342  1.00 83.35  ? 443  GLY B O   1 
ATOM   6525 N N   . GLY B 1 349 ? 9.155   47.968  37.029  1.00 69.60  ? 444  GLY B N   1 
ATOM   6526 C CA  . GLY B 1 349 ? 10.361  48.727  37.168  1.00 64.51  ? 444  GLY B CA  1 
ATOM   6527 C C   . GLY B 1 349 ? 10.192  50.122  36.652  1.00 59.00  ? 444  GLY B C   1 
ATOM   6528 O O   . GLY B 1 349 ? 9.234   50.792  36.928  1.00 59.56  ? 444  GLY B O   1 
ATOM   6529 N N   . LYS B 1 350 ? 11.164  50.547  35.884  1.00 56.29  ? 445  LYS B N   1 
ATOM   6530 C CA  . LYS B 1 350 ? 11.164  51.855  35.300  1.00 56.88  ? 445  LYS B CA  1 
ATOM   6531 C C   . LYS B 1 350 ? 9.956   52.101  34.408  1.00 52.81  ? 445  LYS B C   1 
ATOM   6532 O O   . LYS B 1 350 ? 9.304   53.097  34.535  1.00 50.57  ? 445  LYS B O   1 
ATOM   6533 C CB  . LYS B 1 350 ? 12.456  52.037  34.524  1.00 53.85  ? 445  LYS B CB  1 
ATOM   6534 C CG  . LYS B 1 350 ? 12.748  53.452  34.094  1.00 59.37  ? 445  LYS B CG  1 
ATOM   6535 C CD  . LYS B 1 350 ? 13.880  53.509  33.089  1.00 57.19  ? 445  LYS B CD  1 
ATOM   6536 N N   . ASN B 1 351 ? 9.639   51.176  33.529  1.00 49.53  ? 446  ASN B N   1 
ATOM   6537 C CA  . ASN B 1 351 ? 8.548   51.391  32.618  1.00 47.93  ? 446  ASN B CA  1 
ATOM   6538 C C   . ASN B 1 351 ? 7.193   51.567  33.249  1.00 52.06  ? 446  ASN B C   1 
ATOM   6539 O O   . ASN B 1 351 ? 6.428   52.385  32.832  1.00 46.51  ? 446  ASN B O   1 
ATOM   6540 C CB  . ASN B 1 351 ? 8.518   50.320  31.557  1.00 47.36  ? 446  ASN B CB  1 
ATOM   6541 C CG  . ASN B 1 351 ? 9.663   50.439  30.591  1.00 49.84  ? 446  ASN B CG  1 
ATOM   6542 O OD1 . ASN B 1 351 ? 10.343  51.423  30.560  1.00 46.79  ? 446  ASN B OD1 1 
ATOM   6543 N ND2 . ASN B 1 351 ? 9.875   49.426  29.823  1.00 44.39  ? 446  ASN B ND2 1 
ATOM   6544 N N   . GLU B 1 352 ? 6.895   50.779  34.255  1.00 49.88  ? 447  GLU B N   1 
ATOM   6545 C CA  . GLU B 1 352 ? 5.605   50.918  34.918  1.00 54.71  ? 447  GLU B CA  1 
ATOM   6546 C C   . GLU B 1 352 ? 5.495   52.253  35.639  1.00 51.86  ? 447  GLU B C   1 
ATOM   6547 O O   . GLU B 1 352 ? 4.418   52.848  35.659  1.00 51.15  ? 447  GLU B O   1 
ATOM   6548 C CB  . GLU B 1 352 ? 5.340   49.751  35.881  1.00 58.87  ? 447  GLU B CB  1 
ATOM   6549 C CG  . GLU B 1 352 ? 5.971   49.892  37.246  1.00 65.96  ? 447  GLU B CG  1 
ATOM   6550 C CD  . GLU B 1 352 ? 5.491   48.841  38.252  1.00 74.33  ? 447  GLU B CD  1 
ATOM   6551 O OE1 . GLU B 1 352 ? 4.260   48.620  38.361  1.00 75.68  ? 447  GLU B OE1 1 
ATOM   6552 O OE2 . GLU B 1 352 ? 6.352   48.242  38.937  1.00 78.44  ? 447  GLU B OE2 1 
ATOM   6553 N N   . MET B 1 353 ? 6.594   52.764  36.185  1.00 49.60  ? 448  MET B N   1 
ATOM   6554 C CA  . MET B 1 353 ? 6.568   54.107  36.749  1.00 52.24  ? 448  MET B CA  1 
ATOM   6555 C C   . MET B 1 353 ? 6.292   55.161  35.678  1.00 52.65  ? 448  MET B C   1 
ATOM   6556 O O   . MET B 1 353 ? 5.469   56.062  35.888  1.00 50.35  ? 448  MET B O   1 
ATOM   6557 C CB  . MET B 1 353 ? 7.890   54.405  37.455  1.00 56.78  ? 448  MET B CB  1 
ATOM   6558 C CG  . MET B 1 353 ? 8.049   55.879  37.810  1.00 65.18  ? 448  MET B CG  1 
ATOM   6559 S SD  . MET B 1 353 ? 9.085   56.163  39.260  1.00 81.91  ? 448  MET B SD  1 
ATOM   6560 C CE  . MET B 1 353 ? 10.584  55.307  38.767  1.00 68.96  ? 448  MET B CE  1 
ATOM   6561 N N   . LEU B 1 354 ? 6.970   55.060  34.528  1.00 47.83  ? 449  LEU B N   1 
ATOM   6562 C CA  . LEU B 1 354 ? 6.734   55.983  33.417  1.00 49.52  ? 449  LEU B CA  1 
ATOM   6563 C C   . LEU B 1 354 ? 5.272   55.957  32.968  1.00 46.49  ? 449  LEU B C   1 
ATOM   6564 O O   . LEU B 1 354 ? 4.631   57.006  32.809  1.00 47.75  ? 449  LEU B O   1 
ATOM   6565 C CB  . LEU B 1 354 ? 7.667   55.641  32.237  1.00 43.96  ? 449  LEU B CB  1 
ATOM   6566 C CG  . LEU B 1 354 ? 9.171   55.899  32.407  1.00 46.28  ? 449  LEU B CG  1 
ATOM   6567 C CD1 . LEU B 1 354 ? 9.990   55.372  31.214  1.00 47.59  ? 449  LEU B CD1 1 
ATOM   6568 C CD2 . LEU B 1 354 ? 9.461   57.395  32.614  1.00 47.27  ? 449  LEU B CD2 1 
ATOM   6569 N N   . ILE B 1 355 ? 4.731   54.758  32.749  1.00 46.83  ? 450  ILE B N   1 
ATOM   6570 C CA  . ILE B 1 355 ? 3.349   54.621  32.301  1.00 46.35  ? 450  ILE B CA  1 
ATOM   6571 C C   . ILE B 1 355 ? 2.383   55.146  33.352  1.00 49.05  ? 450  ILE B C   1 
ATOM   6572 O O   . ILE B 1 355 ? 1.391   55.812  33.027  1.00 47.41  ? 450  ILE B O   1 
ATOM   6573 C CB  . ILE B 1 355 ? 3.055   53.155  31.948  1.00 48.54  ? 450  ILE B CB  1 
ATOM   6574 C CG1 . ILE B 1 355 ? 3.889   52.734  30.730  1.00 44.30  ? 450  ILE B CG1 1 
ATOM   6575 C CG2 . ILE B 1 355 ? 1.555   52.930  31.731  1.00 47.55  ? 450  ILE B CG2 1 
ATOM   6576 C CD1 . ILE B 1 355 ? 3.907   51.231  30.542  1.00 49.20  ? 450  ILE B CD1 1 
ATOM   6577 N N   . LYS B 1 356 ? 2.648   54.856  34.626  1.00 47.15  ? 451  LYS B N   1 
ATOM   6578 C CA  . LYS B 1 356 ? 1.778   55.338  35.688  1.00 50.76  ? 451  LYS B CA  1 
ATOM   6579 C C   . LYS B 1 356 ? 1.788   56.868  35.754  1.00 51.87  ? 451  LYS B C   1 
ATOM   6580 O O   . LYS B 1 356 ? 0.746   57.502  35.983  1.00 48.79  ? 451  LYS B O   1 
ATOM   6581 C CB  . LYS B 1 356 ? 2.217   54.715  37.013  1.00 49.10  ? 451  LYS B CB  1 
ATOM   6582 C CG  . LYS B 1 356 ? 1.375   55.117  38.198  1.00 55.90  ? 451  LYS B CG  1 
ATOM   6583 N N   . THR B 1 357 ? 2.955   57.478  35.540  1.00 47.61  ? 452  THR B N   1 
ATOM   6584 C CA  . THR B 1 357 ? 3.026   58.934  35.532  1.00 48.28  ? 452  THR B CA  1 
ATOM   6585 C C   . THR B 1 357 ? 2.240   59.513  34.355  1.00 49.03  ? 452  THR B C   1 
ATOM   6586 O O   . THR B 1 357 ? 1.584   60.551  34.488  1.00 49.06  ? 452  THR B O   1 
ATOM   6587 C CB  . THR B 1 357 ? 4.488   59.372  35.476  1.00 50.12  ? 452  THR B CB  1 
ATOM   6588 O OG1 . THR B 1 357 ? 5.220   58.710  36.512  1.00 47.85  ? 452  THR B OG1 1 
ATOM   6589 C CG2 . THR B 1 357 ? 4.605   60.876  35.644  1.00 48.97  ? 452  THR B CG2 1 
ATOM   6590 N N   . VAL B 1 358 ? 2.291   58.856  33.190  1.00 48.28  ? 453  VAL B N   1 
ATOM   6591 C CA  . VAL B 1 358 ? 1.463   59.317  32.071  1.00 47.80  ? 453  VAL B CA  1 
ATOM   6592 C C   . VAL B 1 358 ? -0.022  59.187  32.400  1.00 47.67  ? 453  VAL B C   1 
ATOM   6593 O O   . VAL B 1 358 ? -0.812  60.108  32.143  1.00 50.02  ? 453  VAL B O   1 
ATOM   6594 C CB  . VAL B 1 358 ? 1.816   58.557  30.781  1.00 46.39  ? 453  VAL B CB  1 
ATOM   6595 C CG1 . VAL B 1 358 ? 0.848   58.956  29.652  1.00 43.87  ? 453  VAL B CG1 1 
ATOM   6596 C CG2 . VAL B 1 358 ? 3.262   58.824  30.387  1.00 44.60  ? 453  VAL B CG2 1 
ATOM   6597 N N   . LYS B 1 359 ? -0.428  58.049  32.984  1.00 45.24  ? 454  LYS B N   1 
ATOM   6598 C CA  . LYS B 1 359 ? -1.839  57.817  33.286  1.00 49.23  ? 454  LYS B CA  1 
ATOM   6599 C C   . LYS B 1 359 ? -2.374  58.755  34.360  1.00 50.15  ? 454  LYS B C   1 
ATOM   6600 O O   . LYS B 1 359 ? -3.584  58.991  34.405  1.00 50.40  ? 454  LYS B O   1 
ATOM   6601 C CB  . LYS B 1 359 ? -2.075  56.364  33.729  1.00 48.98  ? 454  LYS B CB  1 
ATOM   6602 C CG  . LYS B 1 359 ? -1.543  55.323  32.750  1.00 53.74  ? 454  LYS B CG  1 
ATOM   6603 C CD  . LYS B 1 359 ? -2.578  54.891  31.746  1.00 53.19  ? 454  LYS B CD  1 
ATOM   6604 C CE  . LYS B 1 359 ? -1.929  54.386  30.461  1.00 55.37  ? 454  LYS B CE  1 
ATOM   6605 N NZ  . LYS B 1 359 ? -2.647  53.190  29.962  1.00 53.13  ? 454  LYS B NZ  1 
ATOM   6606 N N   . GLY B 1 360 ? -1.517  59.283  35.235  1.00 49.07  ? 455  GLY B N   1 
ATOM   6607 C CA  . GLY B 1 360 ? -2.013  60.221  36.236  1.00 49.48  ? 455  GLY B CA  1 
ATOM   6608 C C   . GLY B 1 360 ? -2.675  61.449  35.627  1.00 51.34  ? 455  GLY B C   1 
ATOM   6609 O O   . GLY B 1 360 ? -3.654  61.965  36.164  1.00 52.39  ? 455  GLY B O   1 
ATOM   6610 N N   . GLN B 1 361 ? -2.168  61.931  34.498  1.00 46.80  ? 456  GLN B N   1 
ATOM   6611 C CA  . GLN B 1 361 ? -2.787  63.064  33.821  1.00 50.59  ? 456  GLN B CA  1 
ATOM   6612 C C   . GLN B 1 361 ? -3.732  62.648  32.696  1.00 52.09  ? 456  GLN B C   1 
ATOM   6613 O O   . GLN B 1 361 ? -4.786  63.272  32.512  1.00 51.57  ? 456  GLN B O   1 
ATOM   6614 C CB  . GLN B 1 361 ? -1.707  63.996  33.264  1.00 47.58  ? 456  GLN B CB  1 
ATOM   6615 C CG  . GLN B 1 361 ? -2.268  65.245  32.618  1.00 51.43  ? 456  GLN B CG  1 
ATOM   6616 C CD  . GLN B 1 361 ? -1.218  66.317  32.389  1.00 53.89  ? 456  GLN B CD  1 
ATOM   6617 O OE1 . GLN B 1 361 ? -0.022  66.036  32.308  1.00 51.53  ? 456  GLN B OE1 1 
ATOM   6618 N NE2 . GLN B 1 361 ? -1.666  67.559  32.287  1.00 53.53  ? 456  GLN B NE2 1 
ATOM   6619 N N   . TYR B 1 362 ? -3.387  61.600  31.944  1.00 49.29  ? 457  TYR B N   1 
ATOM   6620 C CA  . TYR B 1 362 ? -4.180  61.123  30.812  1.00 50.33  ? 457  TYR B CA  1 
ATOM   6621 C C   . TYR B 1 362 ? -4.587  59.674  31.058  1.00 51.87  ? 457  TYR B C   1 
ATOM   6622 O O   . TYR B 1 362 ? -3.939  58.745  30.551  1.00 47.33  ? 457  TYR B O   1 
ATOM   6623 C CB  . TYR B 1 362 ? -3.386  61.245  29.515  1.00 49.40  ? 457  TYR B CB  1 
ATOM   6624 C CG  . TYR B 1 362 ? -2.788  62.623  29.291  1.00 51.50  ? 457  TYR B CG  1 
ATOM   6625 C CD1 . TYR B 1 362 ? -1.415  62.805  29.272  1.00 47.88  ? 457  TYR B CD1 1 
ATOM   6626 C CD2 . TYR B 1 362 ? -3.601  63.732  29.099  1.00 48.38  ? 457  TYR B CD2 1 
ATOM   6627 C CE1 . TYR B 1 362 ? -0.859  64.058  29.052  1.00 49.73  ? 457  TYR B CE1 1 
ATOM   6628 C CE2 . TYR B 1 362 ? -3.055  64.996  28.888  1.00 51.15  ? 457  TYR B CE2 1 
ATOM   6629 C CZ  . TYR B 1 362 ? -1.680  65.143  28.861  1.00 49.70  ? 457  TYR B CZ  1 
ATOM   6630 O OH  . TYR B 1 362 ? -1.106  66.374  28.655  1.00 54.57  ? 457  TYR B OH  1 
ATOM   6631 N N   . PRO B 1 363 ? -5.652  59.440  31.820  1.00 52.05  ? 458  PRO B N   1 
ATOM   6632 C CA  . PRO B 1 363 ? -6.014  58.061  32.163  1.00 52.73  ? 458  PRO B CA  1 
ATOM   6633 C C   . PRO B 1 363 ? -6.502  57.279  30.955  1.00 51.97  ? 458  PRO B C   1 
ATOM   6634 O O   . PRO B 1 363 ? -7.123  57.817  30.035  1.00 51.15  ? 458  PRO B O   1 
ATOM   6635 C CB  . PRO B 1 363 ? -7.131  58.225  33.206  1.00 52.84  ? 458  PRO B CB  1 
ATOM   6636 C CG  . PRO B 1 363 ? -7.676  59.593  32.974  1.00 54.52  ? 458  PRO B CG  1 
ATOM   6637 C CD  . PRO B 1 363 ? -6.537  60.428  32.458  1.00 54.30  ? 458  PRO B CD  1 
ATOM   6638 N N   . CYS B 1 364 ? -6.205  55.984  30.974  1.00 47.59  ? 459  CYS B N   1 
ATOM   6639 C CA  . CYS B 1 364 ? -6.620  55.072  29.924  1.00 49.13  ? 459  CYS B CA  1 
ATOM   6640 C C   . CYS B 1 364 ? -6.336  53.653  30.388  1.00 51.82  ? 459  CYS B C   1 
ATOM   6641 O O   . CYS B 1 364 ? -5.308  53.395  31.022  1.00 50.29  ? 459  CYS B O   1 
ATOM   6642 C CB  . CYS B 1 364 ? -5.892  55.350  28.599  1.00 52.17  ? 459  CYS B CB  1 
ATOM   6643 S SG  . CYS B 1 364 ? -6.546  54.387  27.192  1.00 55.89  ? 459  CYS B SG  1 
ATOM   6644 N N   . GLU B 1 365 ? -7.264  52.754  30.069  1.00 49.37  ? 460  GLU B N   1 
ATOM   6645 C CA  . GLU B 1 365 ? -7.114  51.323  30.304  1.00 52.12  ? 460  GLU B CA  1 
ATOM   6646 C C   . GLU B 1 365 ? -5.772  50.808  29.785  1.00 51.35  ? 460  GLU B C   1 
ATOM   6647 O O   . GLU B 1 365 ? -5.295  51.230  28.727  1.00 47.43  ? 460  GLU B O   1 
ATOM   6648 C CB  . GLU B 1 365 ? -8.277  50.624  29.599  1.00 55.98  ? 460  GLU B CB  1 
ATOM   6649 C CG  . GLU B 1 365 ? -8.496  49.154  29.871  1.00 67.76  ? 460  GLU B CG  1 
ATOM   6650 C CD  . GLU B 1 365 ? -9.444  48.528  28.835  1.00 72.35  ? 460  GLU B CD  1 
ATOM   6651 O OE1 . GLU B 1 365 ? -9.720  49.183  27.796  1.00 74.91  ? 460  GLU B OE1 1 
ATOM   6652 O OE2 . GLU B 1 365 ? -9.903  47.385  29.058  1.00 71.09  ? 460  GLU B OE2 1 
ATOM   6653 N N   . ASP B 1 366 ? -5.157  49.898  30.546  1.00 52.83  ? 461  ASP B N   1 
ATOM   6654 C CA  . ASP B 1 366 ? -3.920  49.245  30.115  1.00 51.23  ? 461  ASP B CA  1 
ATOM   6655 C C   . ASP B 1 366 ? -4.083  48.627  28.733  1.00 48.69  ? 461  ASP B C   1 
ATOM   6656 O O   . ASP B 1 366 ? -5.127  48.055  28.414  1.00 43.54  ? 461  ASP B O   1 
ATOM   6657 C CB  . ASP B 1 366 ? -3.519  48.133  31.092  1.00 53.75  ? 461  ASP B CB  1 
ATOM   6658 C CG  . ASP B 1 366 ? -3.025  48.663  32.419  1.00 61.14  ? 461  ASP B CG  1 
ATOM   6659 O OD1 . ASP B 1 366 ? -2.900  49.903  32.573  1.00 64.64  ? 461  ASP B OD1 1 
ATOM   6660 O OD2 . ASP B 1 366 ? -2.750  47.824  33.302  1.00 59.24  ? 461  ASP B OD2 1 
ATOM   6661 N N   . PHE B 1 367 ? -3.034  48.739  27.920  1.00 45.46  ? 462  PHE B N   1 
ATOM   6662 C CA  . PHE B 1 367 ? -3.017  48.084  26.624  1.00 44.24  ? 462  PHE B CA  1 
ATOM   6663 C C   . PHE B 1 367 ? -2.990  46.578  26.822  1.00 42.82  ? 462  PHE B C   1 
ATOM   6664 O O   . PHE B 1 367 ? -2.194  46.069  27.617  1.00 39.93  ? 462  PHE B O   1 
ATOM   6665 C CB  . PHE B 1 367 ? -1.801  48.523  25.810  1.00 41.13  ? 462  PHE B CB  1 
ATOM   6666 C CG  . PHE B 1 367 ? -1.826  48.027  24.395  1.00 42.05  ? 462  PHE B CG  1 
ATOM   6667 C CD1 . PHE B 1 367 ? -2.579  48.695  23.426  1.00 42.32  ? 462  PHE B CD1 1 
ATOM   6668 C CD2 . PHE B 1 367 ? -1.114  46.898  24.026  1.00 39.96  ? 462  PHE B CD2 1 
ATOM   6669 C CE1 . PHE B 1 367 ? -2.622  48.244  22.116  1.00 40.26  ? 462  PHE B CE1 1 
ATOM   6670 C CE2 . PHE B 1 367 ? -1.143  46.439  22.715  1.00 40.97  ? 462  PHE B CE2 1 
ATOM   6671 C CZ  . PHE B 1 367 ? -1.900  47.111  21.757  1.00 40.64  ? 462  PHE B CZ  1 
ATOM   6672 N N   . GLN B 1 368 ? -3.852  45.870  26.089  1.00 40.75  ? 463  GLN B N   1 
ATOM   6673 C CA  . GLN B 1 368 ? -4.034  44.430  26.224  1.00 41.84  ? 463  GLN B CA  1 
ATOM   6674 C C   . GLN B 1 368 ? -3.764  43.725  24.902  1.00 42.84  ? 463  GLN B C   1 
ATOM   6675 O O   . GLN B 1 368 ? -4.104  44.243  23.830  1.00 37.90  ? 463  GLN B O   1 
ATOM   6676 C CB  . GLN B 1 368 ? -5.451  44.111  26.694  1.00 42.61  ? 463  GLN B CB  1 
ATOM   6677 C CG  . GLN B 1 368 ? -5.689  44.476  28.124  1.00 45.51  ? 463  GLN B CG  1 
ATOM   6678 C CD  . GLN B 1 368 ? -7.140  44.367  28.475  1.00 50.15  ? 463  GLN B CD  1 
ATOM   6679 O OE1 . GLN B 1 368 ? -7.708  43.281  28.472  1.00 49.20  ? 463  GLN B OE1 1 
ATOM   6680 N NE2 . GLN B 1 368 ? -7.765  45.501  28.733  1.00 50.62  ? 463  GLN B NE2 1 
ATOM   6681 N N   . TRP B 1 369 ? -3.133  42.549  24.997  1.00 38.79  ? 464  TRP B N   1 
ATOM   6682 C CA  . TRP B 1 369 ? -2.852  41.691  23.860  1.00 41.08  ? 464  TRP B CA  1 
ATOM   6683 C C   . TRP B 1 369 ? -2.833  40.246  24.350  1.00 41.79  ? 464  TRP B C   1 
ATOM   6684 O O   . TRP B 1 369 ? -2.537  39.968  25.522  1.00 38.39  ? 464  TRP B O   1 
ATOM   6685 C CB  . TRP B 1 369 ? -1.534  42.076  23.148  1.00 41.82  ? 464  TRP B CB  1 
ATOM   6686 C CG  . TRP B 1 369 ? -0.262  41.703  23.877  1.00 42.53  ? 464  TRP B CG  1 
ATOM   6687 C CD1 . TRP B 1 369 ? 0.594   40.682  23.567  1.00 40.88  ? 464  TRP B CD1 1 
ATOM   6688 C CD2 . TRP B 1 369 ? 0.292   42.352  25.034  1.00 41.75  ? 464  TRP B CD2 1 
ATOM   6689 N NE1 . TRP B 1 369 ? 1.642   40.655  24.458  1.00 38.87  ? 464  TRP B NE1 1 
ATOM   6690 C CE2 . TRP B 1 369 ? 1.481   41.664  25.370  1.00 43.52  ? 464  TRP B CE2 1 
ATOM   6691 C CE3 . TRP B 1 369 ? -0.092  43.454  25.809  1.00 40.58  ? 464  TRP B CE3 1 
ATOM   6692 C CZ2 . TRP B 1 369 ? 2.278   42.032  26.452  1.00 38.92  ? 464  TRP B CZ2 1 
ATOM   6693 C CZ3 . TRP B 1 369 ? 0.713   43.825  26.881  1.00 41.41  ? 464  TRP B CZ3 1 
ATOM   6694 C CH2 . TRP B 1 369 ? 1.884   43.112  27.189  1.00 39.32  ? 464  TRP B CH2 1 
ATOM   6695 N N   . LEU B 1 370 ? -3.203  39.339  23.456  1.00 38.80  ? 465  LEU B N   1 
ATOM   6696 C CA  . LEU B 1 370 ? -3.328  37.930  23.790  1.00 44.62  ? 465  LEU B CA  1 
ATOM   6697 C C   . LEU B 1 370 ? -2.005  37.202  23.580  1.00 44.29  ? 465  LEU B C   1 
ATOM   6698 O O   . LEU B 1 370 ? -1.124  37.650  22.844  1.00 41.99  ? 465  LEU B O   1 
ATOM   6699 C CB  . LEU B 1 370 ? -4.399  37.256  22.930  1.00 44.77  ? 465  LEU B CB  1 
ATOM   6700 C CG  . LEU B 1 370 ? -5.784  37.894  22.860  1.00 45.00  ? 465  LEU B CG  1 
ATOM   6701 C CD1 . LEU B 1 370 ? -6.674  37.072  21.919  1.00 41.46  ? 465  LEU B CD1 1 
ATOM   6702 C CD2 . LEU B 1 370 ? -6.352  37.977  24.245  1.00 41.56  ? 465  LEU B CD2 1 
ATOM   6703 N N   . GLU B 1 371 ? -1.914  36.027  24.200  1.00 46.84  ? 466  GLU B N   1 
ATOM   6704 C CA  . GLU B 1 371 ? -0.763  35.155  24.017  1.00 45.42  ? 466  GLU B CA  1 
ATOM   6705 C C   . GLU B 1 371 ? -0.621  34.725  22.564  1.00 47.90  ? 466  GLU B C   1 
ATOM   6706 O O   . GLU B 1 371 ? 0.499   34.559  22.069  1.00 42.53  ? 466  GLU B O   1 
ATOM   6707 C CB  . GLU B 1 371 ? -0.897  33.942  24.941  1.00 44.80  ? 466  GLU B CB  1 
ATOM   6708 C CG  . GLU B 1 371 ? 0.421   33.219  25.197  1.00 47.15  ? 466  GLU B CG  1 
ATOM   6709 C CD  . GLU B 1 371 ? 0.791   32.271  24.084  1.00 53.55  ? 466  GLU B CD  1 
ATOM   6710 O OE1 . GLU B 1 371 ? -0.142  31.738  23.434  1.00 54.19  ? 466  GLU B OE1 1 
ATOM   6711 O OE2 . GLU B 1 371 ? 2.010   32.061  23.855  1.00 56.09  ? 466  GLU B OE2 1 
ATOM   6712 N N   . GLU B 1 372 ? -1.736  34.577  21.856  1.00 44.73  ? 467  GLU B N   1 
ATOM   6713 C CA  . GLU B 1 372 ? -1.738  34.272  20.431  1.00 45.89  ? 467  GLU B CA  1 
ATOM   6714 C C   . GLU B 1 372 ? -2.540  35.350  19.711  1.00 44.75  ? 467  GLU B C   1 
ATOM   6715 O O   . GLU B 1 372 ? -3.738  35.507  19.969  1.00 42.37  ? 467  GLU B O   1 
ATOM   6716 C CB  . GLU B 1 372 ? -2.342  32.889  20.182  1.00 48.57  ? 467  GLU B CB  1 
ATOM   6717 C CG  . GLU B 1 372 ? -2.222  32.404  18.756  1.00 53.18  ? 467  GLU B CG  1 
ATOM   6718 C CD  . GLU B 1 372 ? -0.908  31.691  18.495  1.00 67.63  ? 467  GLU B CD  1 
ATOM   6719 O OE1 . GLU B 1 372 ? 0.090   32.372  18.144  1.00 66.86  ? 467  GLU B OE1 1 
ATOM   6720 O OE2 . GLU B 1 372 ? -0.879  30.443  18.653  1.00 77.45  ? 467  GLU B OE2 1 
ATOM   6721 N N   . THR B 1 373 ? -1.891  36.072  18.808  1.00 40.47  ? 468  THR B N   1 
ATOM   6722 C CA  . THR B 1 373 ? -2.521  37.224  18.174  1.00 41.71  ? 468  THR B CA  1 
ATOM   6723 C C   . THR B 1 373 ? -3.621  36.767  17.217  1.00 43.62  ? 468  THR B C   1 
ATOM   6724 O O   . THR B 1 373 ? -3.379  35.886  16.384  1.00 42.74  ? 468  THR B O   1 
ATOM   6725 C CB  . THR B 1 373 ? -1.475  38.048  17.414  1.00 39.63  ? 468  THR B CB  1 
ATOM   6726 O OG1 . THR B 1 373 ? -0.366  38.368  18.277  1.00 37.77  ? 468  THR B OG1 1 
ATOM   6727 C CG2 . THR B 1 373 ? -2.102  39.334  16.882  1.00 37.68  ? 468  THR B CG2 1 
ATOM   6728 N N   . PRO B 1 374 ? -4.826  37.336  17.289  1.00 41.83  ? 469  PRO B N   1 
ATOM   6729 C CA  . PRO B 1 374 ? -5.841  37.013  16.278  1.00 42.17  ? 469  PRO B CA  1 
ATOM   6730 C C   . PRO B 1 374 ? -5.447  37.530  14.901  1.00 44.52  ? 469  PRO B C   1 
ATOM   6731 O O   . PRO B 1 374 ? -4.914  38.638  14.752  1.00 40.17  ? 469  PRO B O   1 
ATOM   6732 C CB  . PRO B 1 374 ? -7.104  37.709  16.802  1.00 45.42  ? 469  PRO B CB  1 
ATOM   6733 C CG  . PRO B 1 374 ? -6.848  37.931  18.288  1.00 42.04  ? 469  PRO B CG  1 
ATOM   6734 C CD  . PRO B 1 374 ? -5.360  38.211  18.351  1.00 38.80  ? 469  PRO B CD  1 
ATOM   6735 N N   . ILE B 1 375 ? -5.705  36.703  13.887  1.00 45.05  ? 470  ILE B N   1 
ATOM   6736 C CA  . ILE B 1 375 ? -5.449  37.033  12.483  1.00 41.85  ? 470  ILE B CA  1 
ATOM   6737 C C   . ILE B 1 375 ? -6.757  36.863  11.722  1.00 44.30  ? 470  ILE B C   1 
ATOM   6738 O O   . ILE B 1 375 ? -7.365  35.787  11.765  1.00 46.44  ? 470  ILE B O   1 
ATOM   6739 C CB  . ILE B 1 375 ? -4.346  36.151  11.874  1.00 43.74  ? 470  ILE B CB  1 
ATOM   6740 C CG1 . ILE B 1 375 ? -3.022  36.360  12.613  1.00 43.48  ? 470  ILE B CG1 1 
ATOM   6741 C CG2 . ILE B 1 375 ? -4.148  36.475  10.403  1.00 42.59  ? 470  ILE B CG2 1 
ATOM   6742 C CD1 . ILE B 1 375 ? -1.849  35.503  12.065  1.00 45.86  ? 470  ILE B CD1 1 
ATOM   6743 N N   . PHE B 1 376 ? -7.197  37.924  11.042  1.00 41.42  ? 471  PHE B N   1 
ATOM   6744 C CA  . PHE B 1 376 ? -8.390  37.892  10.207  1.00 45.58  ? 471  PHE B CA  1 
ATOM   6745 C C   . PHE B 1 376 ? -8.001  38.145  8.760   1.00 45.70  ? 471  PHE B C   1 
ATOM   6746 O O   . PHE B 1 376 ? -7.087  38.929  8.489   1.00 44.85  ? 471  PHE B O   1 
ATOM   6747 C CB  . PHE B 1 376 ? -9.420  38.955  10.655  1.00 43.73  ? 471  PHE B CB  1 
ATOM   6748 C CG  . PHE B 1 376 ? -9.731  38.918  12.126  1.00 45.76  ? 471  PHE B CG  1 
ATOM   6749 C CD1 . PHE B 1 376 ? -10.564 37.937  12.650  1.00 45.27  ? 471  PHE B CD1 1 
ATOM   6750 C CD2 . PHE B 1 376 ? -9.176  39.852  12.986  1.00 42.30  ? 471  PHE B CD2 1 
ATOM   6751 C CE1 . PHE B 1 376 ? -10.844 37.895  14.011  1.00 47.37  ? 471  PHE B CE1 1 
ATOM   6752 C CE2 . PHE B 1 376 ? -9.464  39.827  14.342  1.00 43.59  ? 471  PHE B CE2 1 
ATOM   6753 C CZ  . PHE B 1 376 ? -10.293 38.846  14.858  1.00 43.64  ? 471  PHE B CZ  1 
ATOM   6754 N N   . THR B 1 377 ? -8.685  37.488  7.824   1.00 43.31  ? 472  THR B N   1 
ATOM   6755 C CA  . THR B 1 377 ? -8.555  37.965  6.455   1.00 44.52  ? 472  THR B CA  1 
ATOM   6756 C C   . THR B 1 377 ? -9.356  39.257  6.300   1.00 45.26  ? 472  THR B C   1 
ATOM   6757 O O   . THR B 1 377 ? -10.263 39.547  7.081   1.00 46.73  ? 472  THR B O   1 
ATOM   6758 C CB  . THR B 1 377 ? -9.038  36.928  5.441   1.00 46.39  ? 472  THR B CB  1 
ATOM   6759 O OG1 . THR B 1 377 ? -10.453 36.746  5.577   1.00 47.74  ? 472  THR B OG1 1 
ATOM   6760 C CG2 . THR B 1 377 ? -8.301  35.581  5.625   1.00 47.26  ? 472  THR B CG2 1 
ATOM   6761 N N   . TYR B 1 378 ? -9.000  40.044  5.287   1.00 46.07  ? 473  TYR B N   1 
ATOM   6762 C CA  . TYR B 1 378 ? -9.754  41.258  5.008   1.00 44.74  ? 473  TYR B CA  1 
ATOM   6763 C C   . TYR B 1 378 ? -11.215 40.935  4.769   1.00 48.03  ? 473  TYR B C   1 
ATOM   6764 O O   . TYR B 1 378 ? -12.112 41.645  5.256   1.00 45.81  ? 473  TYR B O   1 
ATOM   6765 C CB  . TYR B 1 378 ? -9.153  41.957  3.803   1.00 44.08  ? 473  TYR B CB  1 
ATOM   6766 C CG  . TYR B 1 378 ? -9.748  43.299  3.488   1.00 48.32  ? 473  TYR B CG  1 
ATOM   6767 C CD1 . TYR B 1 378 ? -9.339  44.436  4.181   1.00 47.57  ? 473  TYR B CD1 1 
ATOM   6768 C CD2 . TYR B 1 378 ? -10.700 43.444  2.481   1.00 46.65  ? 473  TYR B CD2 1 
ATOM   6769 C CE1 . TYR B 1 378 ? -9.862  45.674  3.892   1.00 49.14  ? 473  TYR B CE1 1 
ATOM   6770 C CE2 . TYR B 1 378 ? -11.218 44.683  2.179   1.00 49.60  ? 473  TYR B CE2 1 
ATOM   6771 C CZ  . TYR B 1 378 ? -10.799 45.793  2.891   1.00 48.91  ? 473  TYR B CZ  1 
ATOM   6772 O OH  . TYR B 1 378 ? -11.315 47.030  2.599   1.00 50.03  ? 473  TYR B OH  1 
ATOM   6773 N N   . GLU B 1 379 ? -11.475 39.840  4.051   1.00 45.82  ? 474  GLU B N   1 
ATOM   6774 C CA  . GLU B 1 379 ? -12.853 39.462  3.769   1.00 50.80  ? 474  GLU B CA  1 
ATOM   6775 C C   . GLU B 1 379 ? -13.605 39.146  5.057   1.00 48.81  ? 474  GLU B C   1 
ATOM   6776 O O   . GLU B 1 379 ? -14.766 39.550  5.217   1.00 49.46  ? 474  GLU B O   1 
ATOM   6777 C CB  . GLU B 1 379 ? -12.889 38.271  2.805   1.00 48.77  ? 474  GLU B CB  1 
ATOM   6778 C CG  . GLU B 1 379 ? -14.302 37.728  2.559   1.00 58.10  ? 474  GLU B CG  1 
ATOM   6779 C CD  . GLU B 1 379 ? -14.307 36.410  1.794   1.00 65.22  ? 474  GLU B CD  1 
ATOM   6780 O OE1 . GLU B 1 379 ? -13.212 35.868  1.525   1.00 64.25  ? 474  GLU B OE1 1 
ATOM   6781 O OE2 . GLU B 1 379 ? -15.407 35.920  1.468   1.00 68.08  ? 474  GLU B OE2 1 
ATOM   6782 N N   . GLU B 1 380 ? -12.958 38.431  5.991   1.00 46.71  ? 475  GLU B N   1 
ATOM   6783 C CA  . GLU B 1 380 ? -13.575 38.160  7.291   1.00 47.31  ? 475  GLU B CA  1 
ATOM   6784 C C   . GLU B 1 380 ? -13.845 39.451  8.054   1.00 46.99  ? 475  GLU B C   1 
ATOM   6785 O O   . GLU B 1 380 ? -14.903 39.600  8.669   1.00 48.26  ? 475  GLU B O   1 
ATOM   6786 C CB  . GLU B 1 380 ? -12.683 37.248  8.144   1.00 48.42  ? 475  GLU B CB  1 
ATOM   6787 C CG  . GLU B 1 380 ? -12.740 35.765  7.821   1.00 52.19  ? 475  GLU B CG  1 
ATOM   6788 C CD  . GLU B 1 380 ? -11.472 35.020  8.260   1.00 53.49  ? 475  GLU B CD  1 
ATOM   6789 O OE1 . GLU B 1 380 ? -10.578 35.650  8.874   1.00 54.70  ? 475  GLU B OE1 1 
ATOM   6790 O OE2 . GLU B 1 380 ? -11.360 33.801  7.979   1.00 60.34  ? 475  GLU B OE2 1 
ATOM   6791 N N   . ALA B 1 381 ? -12.882 40.376  8.055   1.00 46.34  ? 476  ALA B N   1 
ATOM   6792 C CA  . ALA B 1 381 ? -13.057 41.631  8.780   1.00 50.37  ? 476  ALA B CA  1 
ATOM   6793 C C   . ALA B 1 381 ? -14.259 42.399  8.244   1.00 48.36  ? 476  ALA B C   1 
ATOM   6794 O O   . ALA B 1 381 ? -15.109 42.877  9.011   1.00 51.16  ? 476  ALA B O   1 
ATOM   6795 C CB  . ALA B 1 381 ? -11.773 42.468  8.682   1.00 43.63  ? 476  ALA B CB  1 
ATOM   6796 N N   . ILE B 1 382 ? -14.366 42.490  6.914   1.00 49.54  ? 477  ILE B N   1 
ATOM   6797 C CA  . ILE B 1 382 ? -15.503 43.171  6.303   1.00 50.45  ? 477  ILE B CA  1 
ATOM   6798 C C   . ILE B 1 382 ? -16.802 42.462  6.655   1.00 52.45  ? 477  ILE B C   1 
ATOM   6799 O O   . ILE B 1 382 ? -17.809 43.106  6.970   1.00 49.79  ? 477  ILE B O   1 
ATOM   6800 C CB  . ILE B 1 382 ? -15.314 43.278  4.779   1.00 50.08  ? 477  ILE B CB  1 
ATOM   6801 C CG1 . ILE B 1 382 ? -14.066 44.105  4.456   1.00 49.18  ? 477  ILE B CG1 1 
ATOM   6802 C CG2 . ILE B 1 382 ? -16.533 43.913  4.143   1.00 49.67  ? 477  ILE B CG2 1 
ATOM   6803 C CD1 . ILE B 1 382 ? -14.030 45.428  5.176   1.00 50.90  ? 477  ILE B CD1 1 
ATOM   6804 N N   . LYS B 1 383 ? -16.807 41.126  6.612   1.00 51.25  ? 478  LYS B N   1 
ATOM   6805 C CA  . LYS B 1 383 ? -18.041 40.416  6.921   1.00 52.54  ? 478  LYS B CA  1 
ATOM   6806 C C   . LYS B 1 383 ? -18.413 40.557  8.394   1.00 54.25  ? 478  LYS B C   1 
ATOM   6807 O O   . LYS B 1 383 ? -19.597 40.527  8.736   1.00 54.77  ? 478  LYS B O   1 
ATOM   6808 C CB  . LYS B 1 383 ? -17.918 38.950  6.515   1.00 54.35  ? 478  LYS B CB  1 
ATOM   6809 C CG  . LYS B 1 383 ? -17.847 38.748  5.009   1.00 55.90  ? 478  LYS B CG  1 
ATOM   6810 C CD  . LYS B 1 383 ? -17.920 37.267  4.650   1.00 63.40  ? 478  LYS B CD  1 
ATOM   6811 C CE  . LYS B 1 383 ? -17.986 37.069  3.135   1.00 67.41  ? 478  LYS B CE  1 
ATOM   6812 N NZ  . LYS B 1 383 ? -18.194 35.638  2.749   1.00 70.04  ? 478  LYS B NZ  1 
ATOM   6813 N N   . MET B 1 384 ? -17.421 40.726  9.271   1.00 52.46  ? 479  MET B N   1 
ATOM   6814 C CA  . MET B 1 384 ? -17.706 41.089  10.656  1.00 55.49  ? 479  MET B CA  1 
ATOM   6815 C C   . MET B 1 384 ? -18.417 42.431  10.726  1.00 52.33  ? 479  MET B C   1 
ATOM   6816 O O   . MET B 1 384 ? -19.413 42.580  11.437  1.00 55.30  ? 479  MET B O   1 
ATOM   6817 C CB  . MET B 1 384 ? -16.413 41.138  11.470  1.00 51.66  ? 479  MET B CB  1 
ATOM   6818 C CG  . MET B 1 384 ? -15.817 39.779  11.745  1.00 55.71  ? 479  MET B CG  1 
ATOM   6819 S SD  . MET B 1 384 ? -14.131 39.893  12.378  1.00 62.26  ? 479  MET B SD  1 
ATOM   6820 C CE  . MET B 1 384 ? -14.421 40.712  13.927  1.00 49.21  ? 479  MET B CE  1 
ATOM   6821 N N   . LEU B 1 385 ? -17.894 43.432  10.014  1.00 51.99  ? 480  LEU B N   1 
ATOM   6822 C CA  . LEU B 1 385 ? -18.538 44.745  10.024  1.00 55.02  ? 480  LEU B CA  1 
ATOM   6823 C C   . LEU B 1 385 ? -19.952 44.678  9.461   1.00 56.63  ? 480  LEU B C   1 
ATOM   6824 O O   . LEU B 1 385 ? -20.849 45.392  9.922   1.00 58.34  ? 480  LEU B O   1 
ATOM   6825 C CB  . LEU B 1 385 ? -17.711 45.753  9.238   1.00 53.29  ? 480  LEU B CB  1 
ATOM   6826 C CG  . LEU B 1 385 ? -16.457 46.264  9.929   1.00 53.47  ? 480  LEU B CG  1 
ATOM   6827 C CD1 . LEU B 1 385 ? -15.508 46.830  8.891   1.00 53.33  ? 480  LEU B CD1 1 
ATOM   6828 C CD2 . LEU B 1 385 ? -16.815 47.323  10.963  1.00 54.38  ? 480  LEU B CD2 1 
ATOM   6829 N N   . ILE B 1 386 ? -20.166 43.841  8.450   1.00 56.25  ? 481  ILE B N   1 
ATOM   6830 C CA  . ILE B 1 386 ? -21.505 43.668  7.903   1.00 58.50  ? 481  ILE B CA  1 
ATOM   6831 C C   . ILE B 1 386 ? -22.415 43.016  8.933   1.00 60.00  ? 481  ILE B C   1 
ATOM   6832 O O   . ILE B 1 386 ? -23.565 43.430  9.118   1.00 57.47  ? 481  ILE B O   1 
ATOM   6833 C CB  . ILE B 1 386 ? -21.459 42.847  6.602   1.00 57.21  ? 481  ILE B CB  1 
ATOM   6834 C CG1 . ILE B 1 386 ? -20.680 43.597  5.522   1.00 56.12  ? 481  ILE B CG1 1 
ATOM   6835 C CG2 . ILE B 1 386 ? -22.885 42.531  6.121   1.00 55.56  ? 481  ILE B CG2 1 
ATOM   6836 C CD1 . ILE B 1 386 ? -20.418 42.766  4.284   1.00 60.61  ? 481  ILE B CD1 1 
ATOM   6837 N N   . GLN B 1 387 ? -21.917 41.979  9.613   1.00 56.77  ? 482  GLN B N   1 
ATOM   6838 C CA  . GLN B 1 387 ? -22.737 41.250  10.571  1.00 59.76  ? 482  GLN B CA  1 
ATOM   6839 C C   . GLN B 1 387 ? -23.182 42.144  11.715  1.00 61.40  ? 482  GLN B C   1 
ATOM   6840 O O   . GLN B 1 387 ? -24.269 41.955  12.264  1.00 62.09  ? 482  GLN B O   1 
ATOM   6841 C CB  . GLN B 1 387 ? -21.959 40.051  11.110  1.00 62.38  ? 482  GLN B CB  1 
ATOM   6842 C CG  . GLN B 1 387 ? -22.736 39.203  12.102  1.00 70.54  ? 482  GLN B CG  1 
ATOM   6843 C CD  . GLN B 1 387 ? -21.840 38.226  12.842  1.00 79.37  ? 482  GLN B CD  1 
ATOM   6844 O OE1 . GLN B 1 387 ? -20.772 37.843  12.347  1.00 85.98  ? 482  GLN B OE1 1 
ATOM   6845 N NE2 . GLN B 1 387 ? -22.260 37.829  14.040  1.00 81.12  ? 482  GLN B NE2 1 
ATOM   6846 N N   . HIS B 1 388 ? -22.363 43.120  12.087  1.00 61.98  ? 483  HIS B N   1 
ATOM   6847 C CA  . HIS B 1 388 ? -22.702 44.039  13.160  1.00 60.82  ? 483  HIS B CA  1 
ATOM   6848 C C   . HIS B 1 388 ? -23.448 45.271  12.670  1.00 59.04  ? 483  HIS B C   1 
ATOM   6849 O O   . HIS B 1 388 ? -23.598 46.226  13.431  1.00 59.50  ? 483  HIS B O   1 
ATOM   6850 C CB  . HIS B 1 388 ? -21.427 44.439  13.910  1.00 59.67  ? 483  HIS B CB  1 
ATOM   6851 C CG  . HIS B 1 388 ? -20.938 43.378  14.850  1.00 59.26  ? 483  HIS B CG  1 
ATOM   6852 N ND1 . HIS B 1 388 ? -21.271 43.359  16.189  1.00 58.32  ? 483  HIS B ND1 1 
ATOM   6853 C CD2 . HIS B 1 388 ? -20.182 42.276  14.635  1.00 60.40  ? 483  HIS B CD2 1 
ATOM   6854 C CE1 . HIS B 1 388 ? -20.726 42.301  16.762  1.00 59.81  ? 483  HIS B CE1 1 
ATOM   6855 N NE2 . HIS B 1 388 ? -20.056 41.629  15.843  1.00 61.48  ? 483  HIS B NE2 1 
ATOM   6856 N N   . GLY B 1 389 ? -23.913 45.275  11.422  1.00 60.52  ? 484  GLY B N   1 
ATOM   6857 C CA  . GLY B 1 389 ? -24.693 46.379  10.890  1.00 59.76  ? 484  GLY B CA  1 
ATOM   6858 C C   . GLY B 1 389 ? -23.917 47.639  10.577  1.00 63.55  ? 484  GLY B C   1 
ATOM   6859 O O   . GLY B 1 389 ? -24.532 48.681  10.334  1.00 60.17  ? 484  GLY B O   1 
ATOM   6860 N N   . LYS B 1 390 ? -22.590 47.584  10.561  1.00 60.29  ? 485  LYS B N   1 
ATOM   6861 C CA  . LYS B 1 390 ? -21.785 48.769  10.298  1.00 60.09  ? 485  LYS B CA  1 
ATOM   6862 C C   . LYS B 1 390 ? -21.591 49.029  8.813   1.00 64.04  ? 485  LYS B C   1 
ATOM   6863 O O   . LYS B 1 390 ? -21.175 50.130  8.434   1.00 62.71  ? 485  LYS B O   1 
ATOM   6864 C CB  . LYS B 1 390 ? -20.414 48.634  10.982  1.00 57.54  ? 485  LYS B CB  1 
ATOM   6865 C CG  . LYS B 1 390 ? -20.505 48.365  12.484  1.00 58.50  ? 485  LYS B CG  1 
ATOM   6866 C CD  . LYS B 1 390 ? -21.223 49.514  13.206  1.00 62.03  ? 485  LYS B CD  1 
ATOM   6867 C CE  . LYS B 1 390 ? -21.511 49.195  14.664  1.00 63.32  ? 485  LYS B CE  1 
ATOM   6868 N NZ  . LYS B 1 390 ? -22.178 50.359  15.349  1.00 64.80  ? 485  LYS B NZ  1 
ATOM   6869 N N   . LEU B 1 391 ? -21.886 48.043  7.971   1.00 63.72  ? 486  LEU B N   1 
ATOM   6870 C CA  . LEU B 1 391 ? -21.585 48.086  6.550   1.00 62.33  ? 486  LEU B CA  1 
ATOM   6871 C C   . LEU B 1 391 ? -22.660 47.292  5.825   1.00 65.05  ? 486  LEU B C   1 
ATOM   6872 O O   . LEU B 1 391 ? -23.145 46.280  6.339   1.00 64.97  ? 486  LEU B O   1 
ATOM   6873 C CB  . LEU B 1 391 ? -20.196 47.498  6.270   1.00 61.53  ? 486  LEU B CB  1 
ATOM   6874 C CG  . LEU B 1 391 ? -19.157 48.260  5.445   1.00 61.94  ? 486  LEU B CG  1 
ATOM   6875 C CD1 . LEU B 1 391 ? -18.982 49.696  5.904   1.00 62.03  ? 486  LEU B CD1 1 
ATOM   6876 C CD2 . LEU B 1 391 ? -17.820 47.525  5.511   1.00 59.35  ? 486  LEU B CD2 1 
ATOM   6877 N N   . HIS B 1 392 ? -23.051 47.767  4.649   1.00 66.21  ? 487  HIS B N   1 
ATOM   6878 C CA  . HIS B 1 392 ? -23.988 47.052  3.787   1.00 68.30  ? 487  HIS B CA  1 
ATOM   6879 C C   . HIS B 1 392 ? -23.314 46.868  2.435   1.00 69.27  ? 487  HIS B C   1 
ATOM   6880 O O   . HIS B 1 392 ? -23.085 47.841  1.705   1.00 70.20  ? 487  HIS B O   1 
ATOM   6881 C CB  . HIS B 1 392 ? -25.317 47.797  3.690   1.00 71.74  ? 487  HIS B CB  1 
ATOM   6882 C CG  . HIS B 1 392 ? -25.934 48.050  5.029   1.00 74.59  ? 487  HIS B CG  1 
ATOM   6883 N ND1 . HIS B 1 392 ? -25.546 49.098  5.840   1.00 75.20  ? 487  HIS B ND1 1 
ATOM   6884 C CD2 . HIS B 1 392 ? -26.853 47.349  5.733   1.00 75.49  ? 487  HIS B CD2 1 
ATOM   6885 C CE1 . HIS B 1 392 ? -26.226 49.049  6.971   1.00 73.17  ? 487  HIS B CE1 1 
ATOM   6886 N NE2 . HIS B 1 392 ? -27.026 47.998  6.931   1.00 76.45  ? 487  HIS B NE2 1 
ATOM   6887 N N   . LEU B 1 393 ? -22.954 45.624  2.134   1.00 65.81  ? 488  LEU B N   1 
ATOM   6888 C CA  . LEU B 1 393 ? -22.188 45.298  0.945   1.00 64.71  ? 488  LEU B CA  1 
ATOM   6889 C C   . LEU B 1 393 ? -22.646 43.940  0.451   1.00 64.87  ? 488  LEU B C   1 
ATOM   6890 O O   . LEU B 1 393 ? -22.768 43.001  1.243   1.00 67.41  ? 488  LEU B O   1 
ATOM   6891 C CB  . LEU B 1 393 ? -20.688 45.264  1.240   1.00 62.43  ? 488  LEU B CB  1 
ATOM   6892 C CG  . LEU B 1 393 ? -19.997 46.582  1.573   1.00 63.92  ? 488  LEU B CG  1 
ATOM   6893 C CD1 . LEU B 1 393 ? -18.614 46.326  2.162   1.00 56.06  ? 488  LEU B CD1 1 
ATOM   6894 C CD2 . LEU B 1 393 ? -19.909 47.446  0.329   1.00 61.15  ? 488  LEU B CD2 1 
ATOM   6895 N N   . LYS B 1 394 ? -22.901 43.843  -0.846  1.00 63.08  ? 489  LYS B N   1 
ATOM   6896 C CA  . LYS B 1 394 ? -23.126 42.554  -1.472  1.00 62.23  ? 489  LYS B CA  1 
ATOM   6897 C C   . LYS B 1 394 ? -21.793 41.841  -1.680  1.00 62.48  ? 489  LYS B C   1 
ATOM   6898 O O   . LYS B 1 394 ? -20.720 42.455  -1.691  1.00 62.05  ? 489  LYS B O   1 
ATOM   6899 C CB  . LYS B 1 394 ? -23.869 42.730  -2.796  1.00 61.08  ? 489  LYS B CB  1 
ATOM   6900 C CG  . LYS B 1 394 ? -25.373 42.671  -2.639  1.00 63.44  ? 489  LYS B CG  1 
ATOM   6901 C CD  . LYS B 1 394 ? -26.086 43.713  -3.483  1.00 68.91  ? 489  LYS B CD  1 
ATOM   6902 N N   . GLU B 1 395 ? -21.876 40.519  -1.840  1.00 62.57  ? 490  GLU B N   1 
ATOM   6903 C CA  . GLU B 1 395 ? -20.678 39.694  -1.946  1.00 61.39  ? 490  GLU B CA  1 
ATOM   6904 C C   . GLU B 1 395 ? -19.704 40.254  -2.971  1.00 61.42  ? 490  GLU B C   1 
ATOM   6905 O O   . GLU B 1 395 ? -18.496 40.356  -2.713  1.00 59.04  ? 490  GLU B O   1 
ATOM   6906 C CB  . GLU B 1 395 ? -21.066 38.265  -2.315  1.00 69.68  ? 490  GLU B CB  1 
ATOM   6907 C CG  . GLU B 1 395 ? -19.965 37.255  -2.049  1.00 74.12  ? 490  GLU B CG  1 
ATOM   6908 C CD  . GLU B 1 395 ? -19.898 36.875  -0.587  1.00 78.00  ? 490  GLU B CD  1 
ATOM   6909 O OE1 . GLU B 1 395 ? -20.982 36.749  0.033   1.00 79.46  ? 490  GLU B OE1 1 
ATOM   6910 O OE2 . GLU B 1 395 ? -18.772 36.714  -0.065  1.00 74.77  ? 490  GLU B OE2 1 
ATOM   6911 N N   . GLU B 1 396 ? -20.220 40.649  -4.136  1.00 60.44  ? 491  GLU B N   1 
ATOM   6912 C CA  . GLU B 1 396 ? -19.385 41.098  -5.243  1.00 60.82  ? 491  GLU B CA  1 
ATOM   6913 C C   . GLU B 1 396 ? -18.856 42.514  -5.051  1.00 59.67  ? 491  GLU B C   1 
ATOM   6914 O O   . GLU B 1 396 ? -18.166 43.031  -5.940  1.00 56.86  ? 491  GLU B O   1 
ATOM   6915 C CB  . GLU B 1 396 ? -20.166 40.994  -6.557  1.00 59.68  ? 491  GLU B CB  1 
ATOM   6916 C CG  . GLU B 1 396 ? -21.328 41.960  -6.662  1.00 60.13  ? 491  GLU B CG  1 
ATOM   6917 C CD  . GLU B 1 396 ? -22.597 41.459  -6.001  1.00 61.28  ? 491  GLU B CD  1 
ATOM   6918 O OE1 . GLU B 1 396 ? -23.636 42.124  -6.174  1.00 63.46  ? 491  GLU B OE1 1 
ATOM   6919 O OE2 . GLU B 1 396 ? -22.564 40.417  -5.314  1.00 65.76  ? 491  GLU B OE2 1 
ATOM   6920 N N   . GLU B 1 397 ? -19.148 43.141  -3.910  1.00 58.39  ? 492  GLU B N   1 
ATOM   6921 C CA  . GLU B 1 397 ? -18.667 44.477  -3.602  1.00 57.20  ? 492  GLU B CA  1 
ATOM   6922 C C   . GLU B 1 397 ? -17.623 44.502  -2.492  1.00 55.78  ? 492  GLU B C   1 
ATOM   6923 O O   . GLU B 1 397 ? -17.009 45.553  -2.270  1.00 55.93  ? 492  GLU B O   1 
ATOM   6924 C CB  . GLU B 1 397 ? -19.854 45.383  -3.219  1.00 59.56  ? 492  GLU B CB  1 
ATOM   6925 C CG  . GLU B 1 397 ? -20.961 45.421  -4.285  1.00 59.47  ? 492  GLU B CG  1 
ATOM   6926 C CD  . GLU B 1 397 ? -22.226 46.123  -3.825  1.00 60.90  ? 492  GLU B CD  1 
ATOM   6927 O OE1 . GLU B 1 397 ? -23.004 46.573  -4.693  1.00 59.50  ? 492  GLU B OE1 1 
ATOM   6928 O OE2 . GLU B 1 397 ? -22.452 46.221  -2.600  1.00 62.70  ? 492  GLU B OE2 1 
ATOM   6929 N N   . ILE B 1 398 ? -17.373 43.370  -1.822  1.00 56.41  ? 493  ILE B N   1 
ATOM   6930 C CA  . ILE B 1 398 ? -16.548 43.379  -0.613  1.00 56.01  ? 493  ILE B CA  1 
ATOM   6931 C C   . ILE B 1 398 ? -15.092 43.694  -0.946  1.00 54.55  ? 493  ILE B C   1 
ATOM   6932 O O   . ILE B 1 398 ? -14.478 44.572  -0.329  1.00 54.07  ? 493  ILE B O   1 
ATOM   6933 C CB  . ILE B 1 398 ? -16.680 42.045  0.145   1.00 58.69  ? 493  ILE B CB  1 
ATOM   6934 C CG1 . ILE B 1 398 ? -18.043 41.966  0.835   1.00 54.10  ? 493  ILE B CG1 1 
ATOM   6935 C CG2 . ILE B 1 398 ? -15.523 41.887  1.147   1.00 56.30  ? 493  ILE B CG2 1 
ATOM   6936 C CD1 . ILE B 1 398 ? -18.426 40.589  1.292   1.00 61.32  ? 493  ILE B CD1 1 
ATOM   6937 N N   . LEU B 1 399 ? -14.518 42.994  -1.928  1.00 54.07  ? 494  LEU B N   1 
ATOM   6938 C CA  . LEU B 1 399 ? -13.128 43.250  -2.305  1.00 53.85  ? 494  LEU B CA  1 
ATOM   6939 C C   . LEU B 1 399 ? -12.926 44.637  -2.900  1.00 54.78  ? 494  LEU B C   1 
ATOM   6940 O O   . LEU B 1 399 ? -11.791 45.133  -2.930  1.00 53.50  ? 494  LEU B O   1 
ATOM   6941 C CB  . LEU B 1 399 ? -12.652 42.191  -3.297  1.00 57.72  ? 494  LEU B CB  1 
ATOM   6942 C CG  . LEU B 1 399 ? -12.657 40.766  -2.756  1.00 58.88  ? 494  LEU B CG  1 
ATOM   6943 C CD1 . LEU B 1 399 ? -12.050 39.807  -3.781  1.00 53.95  ? 494  LEU B CD1 1 
ATOM   6944 C CD2 . LEU B 1 399 ? -11.903 40.727  -1.422  1.00 54.58  ? 494  LEU B CD2 1 
ATOM   6945 N N   . ALA B 1 400 ? -13.989 45.272  -3.378  1.00 53.90  ? 495  ALA B N   1 
ATOM   6946 C CA  . ALA B 1 400 ? -13.854 46.621  -3.897  1.00 56.95  ? 495  ALA B CA  1 
ATOM   6947 C C   . ALA B 1 400 ? -13.904 47.664  -2.794  1.00 56.90  ? 495  ALA B C   1 
ATOM   6948 O O   . ALA B 1 400 ? -13.560 48.827  -3.042  1.00 56.44  ? 495  ALA B O   1 
ATOM   6949 C CB  . ALA B 1 400 ? -14.950 46.907  -4.928  1.00 54.74  ? 495  ALA B CB  1 
ATOM   6950 N N   . TYR B 1 401 ? -14.324 47.279  -1.589  1.00 54.27  ? 496  TYR B N   1 
ATOM   6951 C CA  . TYR B 1 401 ? -14.505 48.240  -0.513  1.00 53.80  ? 496  TYR B CA  1 
ATOM   6952 C C   . TYR B 1 401 ? -13.172 48.521  0.171   1.00 54.14  ? 496  TYR B C   1 
ATOM   6953 O O   . TYR B 1 401 ? -12.469 47.593  0.582   1.00 54.86  ? 496  TYR B O   1 
ATOM   6954 C CB  . TYR B 1 401 ? -15.537 47.744  0.506   1.00 56.43  ? 496  TYR B CB  1 
ATOM   6955 C CG  . TYR B 1 401 ? -15.570 48.646  1.708   1.00 57.00  ? 496  TYR B CG  1 
ATOM   6956 C CD1 . TYR B 1 401 ? -16.156 49.905  1.639   1.00 58.31  ? 496  TYR B CD1 1 
ATOM   6957 C CD2 . TYR B 1 401 ? -14.966 48.268  2.897   1.00 56.14  ? 496  TYR B CD2 1 
ATOM   6958 C CE1 . TYR B 1 401 ? -16.146 50.749  2.735   1.00 60.12  ? 496  TYR B CE1 1 
ATOM   6959 C CE2 . TYR B 1 401 ? -14.961 49.096  3.988   1.00 55.86  ? 496  TYR B CE2 1 
ATOM   6960 C CZ  . TYR B 1 401 ? -15.538 50.334  3.903   1.00 57.59  ? 496  TYR B CZ  1 
ATOM   6961 O OH  . TYR B 1 401 ? -15.503 51.155  5.001   1.00 60.11  ? 496  TYR B OH  1 
ATOM   6962 N N   . ASP B 1 402 ? -12.826 49.803  0.283   1.00 51.49  ? 497  ASP B N   1 
ATOM   6963 C CA  . ASP B 1 402 ? -11.589 50.264  0.920   1.00 55.11  ? 497  ASP B CA  1 
ATOM   6964 C C   . ASP B 1 402 ? -11.933 50.753  2.330   1.00 57.15  ? 497  ASP B C   1 
ATOM   6965 O O   . ASP B 1 402 ? -12.607 51.774  2.495   1.00 57.19  ? 497  ASP B O   1 
ATOM   6966 C CB  . ASP B 1 402 ? -10.952 51.368  0.074   1.00 50.31  ? 497  ASP B CB  1 
ATOM   6967 C CG  . ASP B 1 402 ? -9.479  51.640  0.426   1.00 58.12  ? 497  ASP B CG  1 
ATOM   6968 O OD1 . ASP B 1 402 ? -8.858  50.902  1.229   1.00 51.13  ? 497  ASP B OD1 1 
ATOM   6969 O OD2 . ASP B 1 402 ? -8.936  52.622  -0.125  1.00 58.17  ? 497  ASP B OD2 1 
ATOM   6970 N N   . MET B 1 403 ? -11.505 50.010  3.340   1.00 56.47  ? 498  MET B N   1 
ATOM   6971 C CA  . MET B 1 403 ? -11.901 50.315  4.709   1.00 54.87  ? 498  MET B CA  1 
ATOM   6972 C C   . MET B 1 403 ? -11.373 51.678  5.143   1.00 51.81  ? 498  MET B C   1 
ATOM   6973 O O   . MET B 1 403 ? -10.172 51.937  5.066   1.00 53.92  ? 498  MET B O   1 
ATOM   6974 C CB  . MET B 1 403 ? -11.396 49.228  5.654   1.00 54.03  ? 498  MET B CB  1 
ATOM   6975 C CG  . MET B 1 403 ? -12.014 49.312  7.028   1.00 56.22  ? 498  MET B CG  1 
ATOM   6976 S SD  . MET B 1 403 ? -11.676 47.883  8.054   1.00 57.18  ? 498  MET B SD  1 
ATOM   6977 C CE  . MET B 1 403 ? -9.925  47.616  7.773   1.00 55.62  ? 498  MET B CE  1 
ATOM   6978 N N   . SER B 1 404 ? -12.272 52.545  5.611   1.00 57.18  ? 499  SER B N   1 
ATOM   6979 C CA  . SER B 1 404 ? -11.892 53.854  6.126   1.00 56.95  ? 499  SER B CA  1 
ATOM   6980 C C   . SER B 1 404 ? -11.384 53.760  7.566   1.00 59.45  ? 499  SER B C   1 
ATOM   6981 O O   . SER B 1 404 ? -11.551 52.749  8.254   1.00 56.17  ? 499  SER B O   1 
ATOM   6982 C CB  . SER B 1 404 ? -13.070 54.816  6.068   1.00 58.10  ? 499  SER B CB  1 
ATOM   6983 O OG  . SER B 1 404 ? -14.132 54.367  6.893   1.00 61.85  ? 499  SER B OG  1 
ATOM   6984 N N   . THR B 1 405 ? -10.762 54.855  8.020   1.00 57.24  ? 500  THR B N   1 
ATOM   6985 C CA  . THR B 1 405 ? -10.222 54.916  9.376   1.00 60.46  ? 500  THR B CA  1 
ATOM   6986 C C   . THR B 1 405 ? -11.327 54.778  10.429  1.00 61.95  ? 500  THR B C   1 
ATOM   6987 O O   . THR B 1 405 ? -11.145 54.094  11.453  1.00 59.70  ? 500  THR B O   1 
ATOM   6988 C CB  . THR B 1 405 ? -9.452  56.226  9.552   1.00 62.20  ? 500  THR B CB  1 
ATOM   6989 O OG1 . THR B 1 405 ? -10.293 57.315  9.154   1.00 74.17  ? 500  THR B OG1 1 
ATOM   6990 C CG2 . THR B 1 405 ? -8.226  56.243  8.680   1.00 60.40  ? 500  THR B CG2 1 
ATOM   6991 N N   . ASP B 1 406 ? -12.489 55.403  10.186  1.00 59.70  ? 501  ASP B N   1 
ATOM   6992 C CA  . ASP B 1 406 ? -13.631 55.205  11.073  1.00 60.31  ? 501  ASP B CA  1 
ATOM   6993 C C   . ASP B 1 406 ? -14.055 53.747  11.106  1.00 57.07  ? 501  ASP B C   1 
ATOM   6994 O O   . ASP B 1 406 ? -14.358 53.200  12.175  1.00 58.18  ? 501  ASP B O   1 
ATOM   6995 C CB  . ASP B 1 406 ? -14.812 56.074  10.635  1.00 65.78  ? 501  ASP B CB  1 
ATOM   6996 C CG  . ASP B 1 406 ? -14.570 57.545  10.877  1.00 72.27  ? 501  ASP B CG  1 
ATOM   6997 O OD1 . ASP B 1 406 ? -13.471 57.895  11.368  1.00 74.79  ? 501  ASP B OD1 1 
ATOM   6998 O OD2 . ASP B 1 406 ? -15.478 58.350  10.574  1.00 77.92  ? 501  ASP B OD2 1 
ATOM   6999 N N   . MET B 1 407 ? -14.120 53.110  9.942   1.00 58.42  ? 502  MET B N   1 
ATOM   7000 C CA  . MET B 1 407 ? -14.495 51.705  9.917   1.00 58.19  ? 502  MET B CA  1 
ATOM   7001 C C   . MET B 1 407 ? -13.450 50.845  10.619  1.00 55.48  ? 502  MET B C   1 
ATOM   7002 O O   . MET B 1 407 ? -13.815 49.871  11.290  1.00 53.97  ? 502  MET B O   1 
ATOM   7003 C CB  . MET B 1 407 ? -14.717 51.256  8.473   1.00 57.64  ? 502  MET B CB  1 
ATOM   7004 C CG  . MET B 1 407 ? -15.906 50.334  8.270   1.00 59.99  ? 502  MET B CG  1 
ATOM   7005 S SD  . MET B 1 407 ? -17.427 50.770  9.137   1.00 63.42  ? 502  MET B SD  1 
ATOM   7006 C CE  . MET B 1 407 ? -17.993 52.224  8.264   1.00 66.03  ? 502  MET B CE  1 
ATOM   7007 N N   . GLU B 1 408 ? -12.159 51.194  10.495  1.00 53.00  ? 503  GLU B N   1 
ATOM   7008 C CA  . GLU B 1 408 ? -11.130 50.504  11.270  1.00 53.21  ? 503  GLU B CA  1 
ATOM   7009 C C   . GLU B 1 408 ? -11.434 50.579  12.763  1.00 53.26  ? 503  GLU B C   1 
ATOM   7010 O O   . GLU B 1 408 ? -11.334 49.572  13.471  1.00 50.90  ? 503  GLU B O   1 
ATOM   7011 C CB  . GLU B 1 408 ? -9.733  51.081  10.977  1.00 51.58  ? 503  GLU B CB  1 
ATOM   7012 C CG  . GLU B 1 408 ? -9.158  50.760  9.583   1.00 56.19  ? 503  GLU B CG  1 
ATOM   7013 C CD  . GLU B 1 408 ? -7.758  51.370  9.333   1.00 62.91  ? 503  GLU B CD  1 
ATOM   7014 O OE1 . GLU B 1 408 ? -7.100  50.972  8.338   1.00 61.66  ? 503  GLU B OE1 1 
ATOM   7015 O OE2 . GLU B 1 408 ? -7.300  52.224  10.135  1.00 66.27  ? 503  GLU B OE2 1 
ATOM   7016 N N   . LYS B 1 409 ? -11.837 51.758  13.256  1.00 53.04  ? 504  LYS B N   1 
ATOM   7017 C CA  . LYS B 1 409 ? -12.113 51.884  14.691  1.00 55.64  ? 504  LYS B CA  1 
ATOM   7018 C C   . LYS B 1 409 ? -13.343 51.083  15.110  1.00 51.14  ? 504  LYS B C   1 
ATOM   7019 O O   . LYS B 1 409 ? -13.363 50.482  16.195  1.00 51.71  ? 504  LYS B O   1 
ATOM   7020 C CB  . LYS B 1 409 ? -12.258 53.357  15.082  1.00 56.72  ? 504  LYS B CB  1 
ATOM   7021 C CG  . LYS B 1 409 ? -10.940 53.947  15.609  1.00 59.94  ? 504  LYS B CG  1 
ATOM   7022 C CD  . LYS B 1 409 ? -10.434 55.109  14.760  1.00 62.35  ? 504  LYS B CD  1 
ATOM   7023 C CE  . LYS B 1 409 ? -11.176 56.399  15.084  1.00 69.32  ? 504  LYS B CE  1 
ATOM   7024 N NZ  . LYS B 1 409 ? -10.682 57.548  14.252  1.00 69.37  ? 504  LYS B NZ  1 
ATOM   7025 N N   . GLU B 1 410 ? -14.376 51.052  14.268  1.00 51.57  ? 505  GLU B N   1 
ATOM   7026 C CA  . GLU B 1 410 ? -15.534 50.211  14.569  1.00 53.76  ? 505  GLU B CA  1 
ATOM   7027 C C   . GLU B 1 410 ? -15.151 48.735  14.618  1.00 52.30  ? 505  GLU B C   1 
ATOM   7028 O O   . GLU B 1 410 ? -15.640 47.975  15.472  1.00 50.06  ? 505  GLU B O   1 
ATOM   7029 C CB  . GLU B 1 410 ? -16.631 50.429  13.529  1.00 53.84  ? 505  GLU B CB  1 
ATOM   7030 C CG  . GLU B 1 410 ? -17.086 51.849  13.437  1.00 56.80  ? 505  GLU B CG  1 
ATOM   7031 C CD  . GLU B 1 410 ? -18.028 52.205  14.567  1.00 61.75  ? 505  GLU B CD  1 
ATOM   7032 O OE1 . GLU B 1 410 ? -18.644 51.282  15.150  1.00 59.34  ? 505  GLU B OE1 1 
ATOM   7033 O OE2 . GLU B 1 410 ? -18.142 53.408  14.877  1.00 68.93  ? 505  GLU B OE2 1 
ATOM   7034 N N   . LEU B 1 411 ? -14.293 48.302  13.693  1.00 48.91  ? 506  LEU B N   1 
ATOM   7035 C CA  . LEU B 1 411 ? -13.832 46.924  13.738  1.00 50.23  ? 506  LEU B CA  1 
ATOM   7036 C C   . LEU B 1 411 ? -13.044 46.675  15.013  1.00 48.46  ? 506  LEU B C   1 
ATOM   7037 O O   . LEU B 1 411 ? -13.168 45.611  15.631  1.00 47.47  ? 506  LEU B O   1 
ATOM   7038 C CB  . LEU B 1 411 ? -13.002 46.604  12.499  1.00 46.71  ? 506  LEU B CB  1 
ATOM   7039 C CG  . LEU B 1 411 ? -12.391 45.203  12.458  1.00 46.92  ? 506  LEU B CG  1 
ATOM   7040 C CD1 . LEU B 1 411 ? -13.482 44.142  12.330  1.00 50.41  ? 506  LEU B CD1 1 
ATOM   7041 C CD2 . LEU B 1 411 ? -11.394 45.101  11.307  1.00 48.70  ? 506  LEU B CD2 1 
ATOM   7042 N N   . GLY B 1 412 ? -12.243 47.658  15.429  1.00 46.64  ? 507  GLY B N   1 
ATOM   7043 C CA  . GLY B 1 412 ? -11.503 47.521  16.673  1.00 47.10  ? 507  GLY B CA  1 
ATOM   7044 C C   . GLY B 1 412 ? -12.414 47.319  17.870  1.00 50.30  ? 507  GLY B C   1 
ATOM   7045 O O   . GLY B 1 412 ? -12.115 46.518  18.761  1.00 45.68  ? 507  GLY B O   1 
ATOM   7046 N N   . LYS B 1 413 ? -13.549 48.028  17.901  1.00 46.43  ? 508  LYS B N   1 
ATOM   7047 C CA  . LYS B 1 413 ? -14.480 47.840  19.010  1.00 51.37  ? 508  LYS B CA  1 
ATOM   7048 C C   . LYS B 1 413 ? -15.108 46.449  18.984  1.00 49.76  ? 508  LYS B C   1 
ATOM   7049 O O   . LYS B 1 413 ? -15.284 45.812  20.037  1.00 47.51  ? 508  LYS B O   1 
ATOM   7050 C CB  . LYS B 1 413 ? -15.571 48.909  18.981  1.00 52.44  ? 508  LYS B CB  1 
ATOM   7051 C CG  . LYS B 1 413 ? -15.059 50.341  19.046  1.00 54.95  ? 508  LYS B CG  1 
ATOM   7052 C CD  . LYS B 1 413 ? -16.249 51.301  19.085  1.00 64.30  ? 508  LYS B CD  1 
ATOM   7053 C CE  . LYS B 1 413 ? -15.811 52.760  19.015  1.00 71.20  ? 508  LYS B CE  1 
ATOM   7054 N NZ  . LYS B 1 413 ? -16.986 53.661  19.206  1.00 75.07  ? 508  LYS B NZ  1 
ATOM   7055 N N   . ILE B 1 414 ? -15.482 45.975  17.793  1.00 50.37  ? 509  ILE B N   1 
ATOM   7056 C CA  . ILE B 1 414 ? -16.019 44.619  17.682  1.00 49.85  ? 509  ILE B CA  1 
ATOM   7057 C C   . ILE B 1 414 ? -15.002 43.598  18.185  1.00 47.10  ? 509  ILE B C   1 
ATOM   7058 O O   . ILE B 1 414 ? -15.341 42.674  18.939  1.00 49.03  ? 509  ILE B O   1 
ATOM   7059 C CB  . ILE B 1 414 ? -16.436 44.328  16.229  1.00 49.09  ? 509  ILE B CB  1 
ATOM   7060 C CG1 . ILE B 1 414 ? -17.682 45.140  15.859  1.00 52.96  ? 509  ILE B CG1 1 
ATOM   7061 C CG2 . ILE B 1 414 ? -16.668 42.831  16.039  1.00 49.65  ? 509  ILE B CG2 1 
ATOM   7062 C CD1 . ILE B 1 414 ? -17.934 45.214  14.372  1.00 53.24  ? 509  ILE B CD1 1 
ATOM   7063 N N   . VAL B 1 415 ? -13.744 43.748  17.777  1.00 46.05  ? 510  VAL B N   1 
ATOM   7064 C CA  . VAL B 1 415 ? -12.736 42.751  18.130  1.00 47.64  ? 510  VAL B CA  1 
ATOM   7065 C C   . VAL B 1 415 ? -12.388 42.833  19.608  1.00 46.19  ? 510  VAL B C   1 
ATOM   7066 O O   . VAL B 1 415 ? -12.136 41.815  20.249  1.00 45.24  ? 510  VAL B O   1 
ATOM   7067 C CB  . VAL B 1 415 ? -11.489 42.914  17.249  1.00 44.39  ? 510  VAL B CB  1 
ATOM   7068 C CG1 . VAL B 1 415 ? -10.397 41.983  17.714  1.00 43.35  ? 510  VAL B CG1 1 
ATOM   7069 C CG2 . VAL B 1 415 ? -11.849 42.624  15.794  1.00 45.85  ? 510  VAL B CG2 1 
ATOM   7070 N N   . LYS B 1 416 ? -12.362 44.039  20.174  1.00 45.71  ? 511  LYS B N   1 
ATOM   7071 C CA  . LYS B 1 416 ? -12.176 44.176  21.612  1.00 46.77  ? 511  LYS B CA  1 
ATOM   7072 C C   . LYS B 1 416 ? -13.274 43.452  22.378  1.00 49.44  ? 511  LYS B C   1 
ATOM   7073 O O   . LYS B 1 416 ? -12.998 42.780  23.381  1.00 48.93  ? 511  LYS B O   1 
ATOM   7074 C CB  . LYS B 1 416 ? -12.144 45.659  21.980  1.00 48.99  ? 511  LYS B CB  1 
ATOM   7075 C CG  . LYS B 1 416 ? -12.134 45.960  23.454  1.00 50.43  ? 511  LYS B CG  1 
ATOM   7076 C CD  . LYS B 1 416 ? -10.744 45.823  24.049  1.00 52.01  ? 511  LYS B CD  1 
ATOM   7077 C CE  . LYS B 1 416 ? -10.597 46.843  25.182  1.00 55.28  ? 511  LYS B CE  1 
ATOM   7078 N NZ  . LYS B 1 416 ? -9.320  46.693  25.907  1.00 54.86  ? 511  LYS B NZ  1 
ATOM   7079 N N   . ALA B 1 417 ? -14.526 43.554  21.915  1.00 46.94  ? 512  ALA B N   1 
ATOM   7080 C CA  . ALA B 1 417 ? -15.615 42.913  22.659  1.00 49.14  ? 512  ALA B CA  1 
ATOM   7081 C C   . ALA B 1 417 ? -15.614 41.393  22.480  1.00 50.69  ? 512  ALA B C   1 
ATOM   7082 O O   . ALA B 1 417 ? -15.964 40.656  23.408  1.00 52.57  ? 512  ALA B O   1 
ATOM   7083 C CB  . ALA B 1 417 ? -16.970 43.499  22.240  1.00 46.20  ? 512  ALA B CB  1 
ATOM   7084 N N   . SER B 1 418 ? -15.242 40.900  21.302  1.00 47.91  ? 513  SER B N   1 
ATOM   7085 C CA  . SER B 1 418 ? -15.295 39.461  21.049  1.00 49.20  ? 513  SER B CA  1 
ATOM   7086 C C   . SER B 1 418 ? -14.005 38.716  21.414  1.00 49.44  ? 513  SER B C   1 
ATOM   7087 O O   . SER B 1 418 ? -14.062 37.543  21.794  1.00 52.43  ? 513  SER B O   1 
ATOM   7088 C CB  . SER B 1 418 ? -15.583 39.210  19.567  1.00 49.01  ? 513  SER B CB  1 
ATOM   7089 O OG  . SER B 1 418 ? -14.469 39.659  18.786  1.00 46.71  ? 513  SER B OG  1 
ATOM   7090 N N   . HIS B 1 419 ? -12.846 39.342  21.266  1.00 45.26  ? 514  HIS B N   1 
ATOM   7091 C CA  . HIS B 1 419 ? -11.552 38.696  21.465  1.00 45.55  ? 514  HIS B CA  1 
ATOM   7092 C C   . HIS B 1 419 ? -10.778 39.246  22.656  1.00 44.96  ? 514  HIS B C   1 
ATOM   7093 O O   . HIS B 1 419 ? -9.731  38.681  23.006  1.00 45.25  ? 514  HIS B O   1 
ATOM   7094 C CB  . HIS B 1 419 ? -10.698 38.844  20.188  1.00 44.28  ? 514  HIS B CB  1 
ATOM   7095 C CG  . HIS B 1 419 ? -11.180 38.006  19.044  1.00 47.28  ? 514  HIS B CG  1 
ATOM   7096 N ND1 . HIS B 1 419 ? -12.440 38.141  18.497  1.00 47.77  ? 514  HIS B ND1 1 
ATOM   7097 C CD2 . HIS B 1 419 ? -10.583 36.996  18.367  1.00 47.99  ? 514  HIS B CD2 1 
ATOM   7098 C CE1 . HIS B 1 419 ? -12.591 37.257  17.525  1.00 47.88  ? 514  HIS B CE1 1 
ATOM   7099 N NE2 . HIS B 1 419 ? -11.479 36.552  17.425  1.00 48.85  ? 514  HIS B NE2 1 
ATOM   7100 N N   . HIS B 1 420 ? -11.236 40.353  23.255  1.00 42.96  ? 515  HIS B N   1 
ATOM   7101 C CA  . HIS B 1 420 ? -10.680 40.889  24.504  1.00 43.64  ? 515  HIS B CA  1 
ATOM   7102 C C   . HIS B 1 420 ? -9.227  41.318  24.333  1.00 43.13  ? 515  HIS B C   1 
ATOM   7103 O O   . HIS B 1 420 ? -8.376  41.033  25.175  1.00 44.92  ? 515  HIS B O   1 
ATOM   7104 C CB  . HIS B 1 420 ? -10.816 39.880  25.650  1.00 43.62  ? 515  HIS B CB  1 
ATOM   7105 C CG  . HIS B 1 420 ? -12.204 39.348  25.820  1.00 47.24  ? 515  HIS B CG  1 
ATOM   7106 N ND1 . HIS B 1 420 ? -13.324 40.119  25.606  1.00 48.71  ? 515  HIS B ND1 1 
ATOM   7107 C CD2 . HIS B 1 420 ? -12.657 38.119  26.162  1.00 52.02  ? 515  HIS B CD2 1 
ATOM   7108 C CE1 . HIS B 1 420 ? -14.407 39.392  25.814  1.00 52.47  ? 515  HIS B CE1 1 
ATOM   7109 N NE2 . HIS B 1 420 ? -14.030 38.173  26.152  1.00 52.78  ? 515  HIS B NE2 1 
ATOM   7110 N N   . THR B 1 421 ? -8.932  42.003  23.233  1.00 43.56  ? 516  THR B N   1 
ATOM   7111 C CA  . THR B 1 421 ? -7.573  42.416  22.940  1.00 41.21  ? 516  THR B CA  1 
ATOM   7112 C C   . THR B 1 421 ? -7.595  43.759  22.222  1.00 44.78  ? 516  THR B C   1 
ATOM   7113 O O   . THR B 1 421 ? -8.571  44.099  21.550  1.00 44.59  ? 516  THR B O   1 
ATOM   7114 C CB  . THR B 1 421 ? -6.841  41.377  22.087  1.00 39.20  ? 516  THR B CB  1 
ATOM   7115 O OG1 . THR B 1 421 ? -5.504  41.826  21.862  1.00 39.70  ? 516  THR B OG1 1 
ATOM   7116 C CG2 . THR B 1 421 ? -7.532  41.181  20.717  1.00 40.21  ? 516  THR B CG2 1 
ATOM   7117 N N   . ASP B 1 422 ? -6.506  44.517  22.373  1.00 39.52  ? 517  ASP B N   1 
ATOM   7118 C CA  . ASP B 1 422 ? -6.284  45.773  21.662  1.00 39.65  ? 517  ASP B CA  1 
ATOM   7119 C C   . ASP B 1 422 ? -5.380  45.615  20.445  1.00 42.54  ? 517  ASP B C   1 
ATOM   7120 O O   . ASP B 1 422 ? -5.046  46.613  19.791  1.00 40.84  ? 517  ASP B O   1 
ATOM   7121 C CB  . ASP B 1 422 ? -5.682  46.822  22.604  1.00 40.62  ? 517  ASP B CB  1 
ATOM   7122 C CG  . ASP B 1 422 ? -6.623  47.199  23.731  1.00 46.23  ? 517  ASP B CG  1 
ATOM   7123 O OD1 . ASP B 1 422 ? -7.832  47.412  23.454  1.00 46.49  ? 517  ASP B OD1 1 
ATOM   7124 O OD2 . ASP B 1 422 ? -6.163  47.262  24.900  1.00 45.13  ? 517  ASP B OD2 1 
ATOM   7125 N N   . TYR B 1 423 ? -4.992  44.393  20.106  1.00 37.64  ? 518  TYR B N   1 
ATOM   7126 C CA  . TYR B 1 423 ? -3.971  44.187  19.091  1.00 38.74  ? 518  TYR B CA  1 
ATOM   7127 C C   . TYR B 1 423 ? -4.385  43.033  18.190  1.00 38.33  ? 518  TYR B C   1 
ATOM   7128 O O   . TYR B 1 423 ? -4.684  41.940  18.683  1.00 36.66  ? 518  TYR B O   1 
ATOM   7129 C CB  . TYR B 1 423 ? -2.619  43.916  19.764  1.00 37.59  ? 518  TYR B CB  1 
ATOM   7130 C CG  . TYR B 1 423 ? -1.531  43.378  18.868  1.00 39.03  ? 518  TYR B CG  1 
ATOM   7131 C CD1 . TYR B 1 423 ? -1.068  44.116  17.773  1.00 39.25  ? 518  TYR B CD1 1 
ATOM   7132 C CD2 . TYR B 1 423 ? -0.928  42.158  19.145  1.00 37.27  ? 518  TYR B CD2 1 
ATOM   7133 C CE1 . TYR B 1 423 ? -0.043  43.642  16.954  1.00 38.58  ? 518  TYR B CE1 1 
ATOM   7134 C CE2 . TYR B 1 423 ? 0.078   41.664  18.342  1.00 36.22  ? 518  TYR B CE2 1 
ATOM   7135 C CZ  . TYR B 1 423 ? 0.521   42.408  17.244  1.00 39.33  ? 518  TYR B CZ  1 
ATOM   7136 O OH  . TYR B 1 423 ? 1.520   41.919  16.448  1.00 37.90  ? 518  TYR B OH  1 
ATOM   7137 N N   . TYR B 1 424 ? -4.413  43.270  16.876  1.00 38.48  ? 519  TYR B N   1 
ATOM   7138 C CA  . TYR B 1 424 ? -4.733  42.155  15.977  1.00 39.13  ? 519  TYR B CA  1 
ATOM   7139 C C   . TYR B 1 424 ? -4.207  42.456  14.584  1.00 37.86  ? 519  TYR B C   1 
ATOM   7140 O O   . TYR B 1 424 ? -3.702  43.547  14.310  1.00 37.59  ? 519  TYR B O   1 
ATOM   7141 C CB  . TYR B 1 424 ? -6.253  41.844  15.940  1.00 38.15  ? 519  TYR B CB  1 
ATOM   7142 C CG  . TYR B 1 424 ? -7.098  43.041  15.572  1.00 41.14  ? 519  TYR B CG  1 
ATOM   7143 C CD1 . TYR B 1 424 ? -7.611  43.875  16.555  1.00 42.27  ? 519  TYR B CD1 1 
ATOM   7144 C CD2 . TYR B 1 424 ? -7.372  43.350  14.244  1.00 42.51  ? 519  TYR B CD2 1 
ATOM   7145 C CE1 . TYR B 1 424 ? -8.360  44.990  16.231  1.00 44.46  ? 519  TYR B CE1 1 
ATOM   7146 C CE2 . TYR B 1 424 ? -8.133  44.483  13.907  1.00 41.88  ? 519  TYR B CE2 1 
ATOM   7147 C CZ  . TYR B 1 424 ? -8.608  45.292  14.912  1.00 44.78  ? 519  TYR B CZ  1 
ATOM   7148 O OH  . TYR B 1 424 ? -9.362  46.400  14.613  1.00 49.48  ? 519  TYR B OH  1 
ATOM   7149 N N   . ILE B 1 425 ? -4.329  41.458  13.701  1.00 36.10  ? 520  ILE B N   1 
ATOM   7150 C CA  . ILE B 1 425 ? -3.706  41.461  12.378  1.00 37.87  ? 520  ILE B CA  1 
ATOM   7151 C C   . ILE B 1 425 ? -4.779  41.195  11.330  1.00 39.76  ? 520  ILE B C   1 
ATOM   7152 O O   . ILE B 1 425 ? -5.654  40.341  11.533  1.00 37.53  ? 520  ILE B O   1 
ATOM   7153 C CB  . ILE B 1 425 ? -2.586  40.393  12.282  1.00 38.93  ? 520  ILE B CB  1 
ATOM   7154 C CG1 . ILE B 1 425 ? -1.429  40.732  13.229  1.00 37.33  ? 520  ILE B CG1 1 
ATOM   7155 C CG2 . ILE B 1 425 ? -2.079  40.232  10.844  1.00 35.80  ? 520  ILE B CG2 1 
ATOM   7156 C CD1 . ILE B 1 425 ? -0.456  39.567  13.454  1.00 35.75  ? 520  ILE B CD1 1 
ATOM   7157 N N   . ILE B 1 426 ? -4.719  41.922  10.210  1.00 39.13  ? 521  ILE B N   1 
ATOM   7158 C CA  . ILE B 1 426 ? -5.527  41.614  9.032   1.00 39.18  ? 521  ILE B CA  1 
ATOM   7159 C C   . ILE B 1 426 ? -4.584  41.249  7.882   1.00 41.83  ? 521  ILE B C   1 
ATOM   7160 O O   . ILE B 1 426 ? -3.578  41.935  7.655   1.00 42.70  ? 521  ILE B O   1 
ATOM   7161 C CB  . ILE B 1 426 ? -6.466  42.781  8.661   1.00 38.03  ? 521  ILE B CB  1 
ATOM   7162 C CG1 . ILE B 1 426 ? -7.440  43.057  9.817   1.00 42.14  ? 521  ILE B CG1 1 
ATOM   7163 C CG2 . ILE B 1 426 ? -7.303  42.448  7.420   1.00 39.68  ? 521  ILE B CG2 1 
ATOM   7164 C CD1 . ILE B 1 426 ? -8.376  44.237  9.590   1.00 40.31  ? 521  ILE B CD1 1 
ATOM   7165 N N   . ILE B 1 427 ? -4.889  40.150  7.184   1.00 40.43  ? 522  ILE B N   1 
ATOM   7166 C CA  . ILE B 1 427 ? -4.128  39.721  6.012   1.00 40.33  ? 522  ILE B CA  1 
ATOM   7167 C C   . ILE B 1 427 ? -5.051  39.682  4.792   1.00 43.03  ? 522  ILE B C   1 
ATOM   7168 O O   . ILE B 1 427 ? -6.277  39.769  4.903   1.00 41.16  ? 522  ILE B O   1 
ATOM   7169 C CB  . ILE B 1 427 ? -3.470  38.336  6.197   1.00 41.80  ? 522  ILE B CB  1 
ATOM   7170 C CG1 . ILE B 1 427 ? -4.545  37.254  6.406   1.00 41.73  ? 522  ILE B CG1 1 
ATOM   7171 C CG2 . ILE B 1 427 ? -2.411  38.341  7.295   1.00 40.35  ? 522  ILE B CG2 1 
ATOM   7172 C CD1 . ILE B 1 427 ? -3.963  35.814  6.495   1.00 42.99  ? 522  ILE B CD1 1 
ATOM   7173 N N   . ASN B 1 428 ? -4.431  39.509  3.612   1.00 40.76  ? 523  ASN B N   1 
ATOM   7174 C CA  . ASN B 1 428 ? -5.146  39.184  2.376   1.00 40.89  ? 523  ASN B CA  1 
ATOM   7175 C C   . ASN B 1 428 ? -5.989  40.369  1.910   1.00 43.40  ? 523  ASN B C   1 
ATOM   7176 O O   . ASN B 1 428 ? -7.167  40.227  1.562   1.00 45.35  ? 523  ASN B O   1 
ATOM   7177 C CB  . ASN B 1 428 ? -6.008  37.928  2.544   1.00 43.38  ? 523  ASN B CB  1 
ATOM   7178 C CG  . ASN B 1 428 ? -5.179  36.653  2.640   1.00 45.67  ? 523  ASN B CG  1 
ATOM   7179 O OD1 . ASN B 1 428 ? -3.939  36.680  2.636   1.00 45.16  ? 523  ASN B OD1 1 
ATOM   7180 N ND2 . ASN B 1 428 ? -5.865  35.523  2.700   1.00 47.00  ? 523  ASN B ND2 1 
ATOM   7181 N N   . PHE B 1 429 ? -5.385  41.552  1.949   1.00 40.54  ? 524  PHE B N   1 
ATOM   7182 C CA  . PHE B 1 429 ? -6.035  42.733  1.416   1.00 43.76  ? 524  PHE B CA  1 
ATOM   7183 C C   . PHE B 1 429 ? -6.206  42.591  -0.096  1.00 44.41  ? 524  PHE B C   1 
ATOM   7184 O O   . PHE B 1 429 ? -5.433  41.889  -0.752  1.00 44.04  ? 524  PHE B O   1 
ATOM   7185 C CB  . PHE B 1 429 ? -5.217  43.988  1.726   1.00 42.36  ? 524  PHE B CB  1 
ATOM   7186 C CG  . PHE B 1 429 ? -5.346  44.480  3.147   1.00 45.24  ? 524  PHE B CG  1 
ATOM   7187 C CD1 . PHE B 1 429 ? -4.584  43.921  4.168   1.00 45.29  ? 524  PHE B CD1 1 
ATOM   7188 C CD2 . PHE B 1 429 ? -6.214  45.523  3.455   1.00 46.72  ? 524  PHE B CD2 1 
ATOM   7189 C CE1 . PHE B 1 429 ? -4.702  44.382  5.475   1.00 43.36  ? 524  PHE B CE1 1 
ATOM   7190 C CE2 . PHE B 1 429 ? -6.326  45.994  4.747   1.00 45.86  ? 524  PHE B CE2 1 
ATOM   7191 C CZ  . PHE B 1 429 ? -5.569  45.426  5.760   1.00 44.86  ? 524  PHE B CZ  1 
ATOM   7192 N N   . PRO B 1 430 ? -7.198  43.257  -0.675  1.00 45.46  ? 525  PRO B N   1 
ATOM   7193 C CA  . PRO B 1 430 ? -7.362  43.198  -2.131  1.00 45.70  ? 525  PRO B CA  1 
ATOM   7194 C C   . PRO B 1 430 ? -6.205  43.879  -2.841  1.00 48.04  ? 525  PRO B C   1 
ATOM   7195 O O   . PRO B 1 430 ? -5.722  44.933  -2.416  1.00 46.88  ? 525  PRO B O   1 
ATOM   7196 C CB  . PRO B 1 430 ? -8.692  43.918  -2.392  1.00 46.50  ? 525  PRO B CB  1 
ATOM   7197 C CG  . PRO B 1 430 ? -9.186  44.399  -1.088  1.00 49.24  ? 525  PRO B CG  1 
ATOM   7198 C CD  . PRO B 1 430 ? -8.362  43.830  0.016   1.00 48.64  ? 525  PRO B CD  1 
ATOM   7199 N N   . SER B 1 431 ? -5.769  43.248  -3.938  1.00 45.92  ? 526  SER B N   1 
ATOM   7200 C CA  . SER B 1 431 ? -4.567  43.678  -4.641  1.00 48.87  ? 526  SER B CA  1 
ATOM   7201 C C   . SER B 1 431 ? -4.687  45.110  -5.128  1.00 47.94  ? 526  SER B C   1 
ATOM   7202 O O   . SER B 1 431 ? -3.721  45.879  -5.050  1.00 46.38  ? 526  SER B O   1 
ATOM   7203 C CB  . SER B 1 431 ? -4.295  42.742  -5.819  1.00 46.16  ? 526  SER B CB  1 
ATOM   7204 O OG  . SER B 1 431 ? -4.075  41.427  -5.349  1.00 48.70  ? 526  SER B OG  1 
ATOM   7205 N N   . ALA B 1 432 ? -5.861  45.483  -5.646  1.00 44.45  ? 527  ALA B N   1 
ATOM   7206 C CA  . ALA B 1 432 ? -6.054  46.818  -6.202  1.00 50.50  ? 527  ALA B CA  1 
ATOM   7207 C C   . ALA B 1 432 ? -5.959  47.916  -5.150  1.00 50.98  ? 527  ALA B C   1 
ATOM   7208 O O   . ALA B 1 432 ? -5.830  49.093  -5.510  1.00 51.45  ? 527  ALA B O   1 
ATOM   7209 C CB  . ALA B 1 432 ? -7.405  46.902  -6.919  1.00 47.77  ? 527  ALA B CB  1 
ATOM   7210 N N   . LEU B 1 433 ? -6.017  47.568  -3.864  1.00 50.32  ? 528  LEU B N   1 
ATOM   7211 C CA  . LEU B 1 433 ? -6.006  48.558  -2.795  1.00 47.93  ? 528  LEU B CA  1 
ATOM   7212 C C   . LEU B 1 433 ? -4.646  48.675  -2.120  1.00 47.65  ? 528  LEU B C   1 
ATOM   7213 O O   . LEU B 1 433 ? -4.530  49.351  -1.096  1.00 50.33  ? 528  LEU B O   1 
ATOM   7214 C CB  . LEU B 1 433 ? -7.079  48.218  -1.767  1.00 47.51  ? 528  LEU B CB  1 
ATOM   7215 C CG  . LEU B 1 433 ? -8.506  48.162  -2.334  1.00 50.57  ? 528  LEU B CG  1 
ATOM   7216 C CD1 . LEU B 1 433 ? -9.520  47.936  -1.233  1.00 52.66  ? 528  LEU B CD1 1 
ATOM   7217 C CD2 . LEU B 1 433 ? -8.825  49.451  -3.093  1.00 50.00  ? 528  LEU B CD2 1 
ATOM   7218 N N   . ARG B 1 434 ? -3.624  48.029  -2.658  1.00 43.56  ? 529  ARG B N   1 
ATOM   7219 C CA  . ARG B 1 434 ? -2.300  47.975  -2.061  1.00 46.40  ? 529  ARG B CA  1 
ATOM   7220 C C   . ARG B 1 434 ? -1.273  48.486  -3.061  1.00 43.98  ? 529  ARG B C   1 
ATOM   7221 O O   . ARG B 1 434 ? -1.560  48.565  -4.261  1.00 44.76  ? 529  ARG B O   1 
ATOM   7222 C CB  . ARG B 1 434 ? -1.962  46.542  -1.618  1.00 43.74  ? 529  ARG B CB  1 
ATOM   7223 C CG  . ARG B 1 434 ? -2.978  45.944  -0.638  1.00 43.43  ? 529  ARG B CG  1 
ATOM   7224 C CD  . ARG B 1 434 ? -3.051  46.735  0.667   1.00 43.46  ? 529  ARG B CD  1 
ATOM   7225 N NE  . ARG B 1 434 ? -1.924  46.451  1.553   1.00 43.93  ? 529  ARG B NE  1 
ATOM   7226 C CZ  . ARG B 1 434 ? -1.951  46.599  2.872   1.00 45.50  ? 529  ARG B CZ  1 
ATOM   7227 N NH1 . ARG B 1 434 ? -3.037  47.041  3.496   1.00 45.66  ? 529  ARG B NH1 1 
ATOM   7228 N NH2 . ARG B 1 434 ? -0.874  46.269  3.588   1.00 42.04  ? 529  ARG B NH2 1 
ATOM   7229 N N   . PRO B 1 435 ? -0.079  48.867  -2.605  1.00 43.75  ? 530  PRO B N   1 
ATOM   7230 C CA  . PRO B 1 435 ? 0.900   49.478  -3.520  1.00 44.35  ? 530  PRO B CA  1 
ATOM   7231 C C   . PRO B 1 435 ? 1.354   48.513  -4.613  1.00 42.80  ? 530  PRO B C   1 
ATOM   7232 O O   . PRO B 1 435 ? 1.159   47.299  -4.543  1.00 42.31  ? 530  PRO B O   1 
ATOM   7233 C CB  . PRO B 1 435 ? 2.066   49.863  -2.600  1.00 42.44  ? 530  PRO B CB  1 
ATOM   7234 C CG  . PRO B 1 435 ? 1.454   49.958  -1.211  1.00 44.56  ? 530  PRO B CG  1 
ATOM   7235 C CD  . PRO B 1 435 ? 0.349   48.941  -1.191  1.00 41.56  ? 530  PRO B CD  1 
ATOM   7236 N N   . PHE B 1 436 ? 2.015   49.081  -5.626  1.00 42.16  ? 531  PHE B N   1 
ATOM   7237 C CA  . PHE B 1 436 ? 2.391   48.325  -6.824  1.00 47.17  ? 531  PHE B CA  1 
ATOM   7238 C C   . PHE B 1 436 ? 3.411   47.219  -6.545  1.00 45.68  ? 531  PHE B C   1 
ATOM   7239 O O   . PHE B 1 436 ? 3.511   46.273  -7.333  1.00 44.20  ? 531  PHE B O   1 
ATOM   7240 C CB  . PHE B 1 436 ? 2.963   49.268  -7.883  1.00 43.06  ? 531  PHE B CB  1 
ATOM   7241 C CG  . PHE B 1 436 ? 4.346   49.778  -7.553  1.00 44.19  ? 531  PHE B CG  1 
ATOM   7242 C CD1 . PHE B 1 436 ? 4.515   50.901  -6.761  1.00 43.54  ? 531  PHE B CD1 1 
ATOM   7243 C CD2 . PHE B 1 436 ? 5.473   49.132  -8.038  1.00 44.89  ? 531  PHE B CD2 1 
ATOM   7244 C CE1 . PHE B 1 436 ? 5.783   51.368  -6.449  1.00 45.91  ? 531  PHE B CE1 1 
ATOM   7245 C CE2 . PHE B 1 436 ? 6.745   49.589  -7.727  1.00 46.64  ? 531  PHE B CE2 1 
ATOM   7246 C CZ  . PHE B 1 436 ? 6.901   50.713  -6.933  1.00 44.41  ? 531  PHE B CZ  1 
ATOM   7247 N N   . TYR B 1 437 ? 4.188   47.322  -5.469  1.00 42.37  ? 532  TYR B N   1 
ATOM   7248 C CA  . TYR B 1 437 ? 5.219   46.326  -5.196  1.00 41.52  ? 532  TYR B CA  1 
ATOM   7249 C C   . TYR B 1 437 ? 4.686   45.127  -4.416  1.00 43.01  ? 532  TYR B C   1 
ATOM   7250 O O   . TYR B 1 437 ? 5.466   44.224  -4.086  1.00 42.06  ? 532  TYR B O   1 
ATOM   7251 C CB  . TYR B 1 437 ? 6.392   46.977  -4.444  1.00 42.91  ? 532  TYR B CB  1 
ATOM   7252 C CG  . TYR B 1 437 ? 5.952   47.810  -3.253  1.00 41.08  ? 532  TYR B CG  1 
ATOM   7253 C CD1 . TYR B 1 437 ? 6.027   49.205  -3.275  1.00 41.76  ? 532  TYR B CD1 1 
ATOM   7254 C CD2 . TYR B 1 437 ? 5.439   47.199  -2.115  1.00 41.35  ? 532  TYR B CD2 1 
ATOM   7255 C CE1 . TYR B 1 437 ? 5.608   49.971  -2.172  1.00 42.86  ? 532  TYR B CE1 1 
ATOM   7256 C CE2 . TYR B 1 437 ? 5.012   47.948  -1.030  1.00 44.52  ? 532  TYR B CE2 1 
ATOM   7257 C CZ  . TYR B 1 437 ? 5.106   49.326  -1.055  1.00 42.56  ? 532  TYR B CZ  1 
ATOM   7258 O OH  . TYR B 1 437 ? 4.679   50.038  0.046   1.00 47.59  ? 532  TYR B OH  1 
ATOM   7259 N N   . THR B 1 438 ? 3.383   45.111  -4.110  1.00 41.83  ? 533  THR B N   1 
ATOM   7260 C CA  . THR B 1 438 ? 2.745   44.035  -3.357  1.00 40.15  ? 533  THR B CA  1 
ATOM   7261 C C   . THR B 1 438 ? 2.539   42.824  -4.248  1.00 41.47  ? 533  THR B C   1 
ATOM   7262 O O   . THR B 1 438 ? 1.928   42.932  -5.315  1.00 41.30  ? 533  THR B O   1 
ATOM   7263 C CB  . THR B 1 438 ? 1.376   44.489  -2.816  1.00 40.84  ? 533  THR B CB  1 
ATOM   7264 O OG1 . THR B 1 438 ? 1.534   45.653  -2.004  1.00 40.40  ? 533  THR B OG1 1 
ATOM   7265 C CG2 . THR B 1 438 ? 0.717   43.389  -1.973  1.00 38.47  ? 533  THR B CG2 1 
ATOM   7266 N N   . MET B 1 439 ? 3.003   41.660  -3.801  1.00 41.76  ? 534  MET B N   1 
ATOM   7267 C CA  . MET B 1 439 ? 2.771   40.443  -4.576  1.00 42.44  ? 534  MET B CA  1 
ATOM   7268 C C   . MET B 1 439 ? 1.332   39.967  -4.377  1.00 46.47  ? 534  MET B C   1 
ATOM   7269 O O   . MET B 1 439 ? 0.857   39.827  -3.242  1.00 42.10  ? 534  MET B O   1 
ATOM   7270 C CB  . MET B 1 439 ? 3.768   39.342  -4.198  1.00 43.02  ? 534  MET B CB  1 
ATOM   7271 C CG  . MET B 1 439 ? 3.663   38.054  -5.065  1.00 40.12  ? 534  MET B CG  1 
ATOM   7272 S SD  . MET B 1 439 ? 3.728   38.392  -6.846  1.00 48.42  ? 534  MET B SD  1 
ATOM   7273 C CE  . MET B 1 439 ? 3.144   36.827  -7.513  1.00 52.37  ? 534  MET B CE  1 
ATOM   7274 N N   . TYR B 1 440 ? 0.632   39.749  -5.487  1.00 45.42  ? 535  TYR B N   1 
ATOM   7275 C CA  . TYR B 1 440 ? -0.718  39.212  -5.467  1.00 48.10  ? 535  TYR B CA  1 
ATOM   7276 C C   . TYR B 1 440 ? -0.666  37.689  -5.351  1.00 49.45  ? 535  TYR B C   1 
ATOM   7277 O O   . TYR B 1 440 ? 0.365   37.061  -5.607  1.00 46.49  ? 535  TYR B O   1 
ATOM   7278 C CB  . TYR B 1 440 ? -1.468  39.643  -6.732  1.00 47.30  ? 535  TYR B CB  1 
ATOM   7279 C CG  . TYR B 1 440 ? -0.677  39.356  -7.993  1.00 52.45  ? 535  TYR B CG  1 
ATOM   7280 C CD1 . TYR B 1 440 ? -0.754  38.115  -8.616  1.00 51.55  ? 535  TYR B CD1 1 
ATOM   7281 C CD2 . TYR B 1 440 ? 0.172   40.318  -8.547  1.00 50.74  ? 535  TYR B CD2 1 
ATOM   7282 C CE1 . TYR B 1 440 ? -0.017  37.843  -9.761  1.00 54.87  ? 535  TYR B CE1 1 
ATOM   7283 C CE2 . TYR B 1 440 ? 0.910   40.052  -9.692  1.00 51.21  ? 535  TYR B CE2 1 
ATOM   7284 C CZ  . TYR B 1 440 ? 0.814   38.812  -10.289 1.00 54.42  ? 535  TYR B CZ  1 
ATOM   7285 O OH  . TYR B 1 440 ? 1.542   38.534  -11.424 1.00 59.90  ? 535  TYR B OH  1 
ATOM   7286 N N   . LYS B 1 441 ? -1.787  37.092  -4.939  1.00 50.11  ? 536  LYS B N   1 
ATOM   7287 C CA  . LYS B 1 441 ? -1.897  35.632  -4.940  1.00 52.64  ? 536  LYS B CA  1 
ATOM   7288 C C   . LYS B 1 441 ? -2.091  35.146  -6.372  1.00 56.37  ? 536  LYS B C   1 
ATOM   7289 O O   . LYS B 1 441 ? -3.018  35.581  -7.060  1.00 54.79  ? 536  LYS B O   1 
ATOM   7290 C CB  . LYS B 1 441 ? -3.060  35.170  -4.064  1.00 53.13  ? 536  LYS B CB  1 
ATOM   7291 C CG  . LYS B 1 441 ? -2.845  35.305  -2.562  1.00 51.84  ? 536  LYS B CG  1 
ATOM   7292 C CD  . LYS B 1 441 ? -3.986  34.652  -1.791  1.00 52.99  ? 536  LYS B CD  1 
ATOM   7293 C CE  . LYS B 1 441 ? -3.756  34.742  -0.287  1.00 50.38  ? 536  LYS B CE  1 
ATOM   7294 N NZ  . LYS B 1 441 ? -2.406  34.232  0.119   1.00 50.62  ? 536  LYS B NZ  1 
ATOM   7295 N N   . GLU B 1 442 ? -1.209  34.305  -6.867  1.00 57.50  ? 537  GLU B N   1 
ATOM   7296 C CA  . GLU B 1 442 ? -1.315  33.901  -8.257  1.00 62.48  ? 537  GLU B CA  1 
ATOM   7297 C C   . GLU B 1 442 ? -2.589  33.205  -8.643  1.00 63.00  ? 537  GLU B C   1 
ATOM   7298 O O   . GLU B 1 442 ? -3.068  33.381  -9.729  1.00 62.62  ? 537  GLU B O   1 
ATOM   7299 C CB  . GLU B 1 442 ? -0.061  33.185  -8.762  1.00 66.48  ? 537  GLU B CB  1 
ATOM   7300 C CG  . GLU B 1 442 ? 0.686   34.056  -9.764  1.00 70.00  ? 537  GLU B CG  1 
ATOM   7301 C CD  . GLU B 1 442 ? 2.177   33.793  -9.867  1.00 74.66  ? 537  GLU B CD  1 
ATOM   7302 O OE1 . GLU B 1 442 ? 2.753   33.215  -8.946  1.00 75.41  ? 537  GLU B OE1 1 
ATOM   7303 O OE2 . GLU B 1 442 ? 2.778   34.198  -10.877 1.00 74.71  ? 537  GLU B OE2 1 
ATOM   7304 N N   . ASP B 1 443 ? -3.073  32.357  -7.768  1.00 63.43  ? 538  ASP B N   1 
ATOM   7305 C CA  . ASP B 1 443 ? -4.335  31.673  -7.932  1.00 63.99  ? 538  ASP B CA  1 
ATOM   7306 C C   . ASP B 1 443 ? -5.577  32.570  -7.814  1.00 62.08  ? 538  ASP B C   1 
ATOM   7307 O O   . ASP B 1 443 ? -6.565  32.303  -8.433  1.00 63.27  ? 538  ASP B O   1 
ATOM   7308 C CB  . ASP B 1 443 ? -4.405  30.483  -7.001  1.00 70.65  ? 538  ASP B CB  1 
ATOM   7309 C CG  . ASP B 1 443 ? -3.423  29.401  -7.376  1.00 80.47  ? 538  ASP B CG  1 
ATOM   7310 O OD1 . ASP B 1 443 ? -3.076  29.276  -8.560  1.00 85.78  ? 538  ASP B OD1 1 
ATOM   7311 O OD2 . ASP B 1 443 ? -2.988  28.660  -6.486  1.00 88.52  ? 538  ASP B OD2 1 
ATOM   7312 N N   . GLU B 1 444 ? -5.540  33.568  -6.944  1.00 59.19  ? 539  GLU B N   1 
ATOM   7313 C CA  . GLU B 1 444 ? -6.649  34.489  -6.718  1.00 58.13  ? 539  GLU B CA  1 
ATOM   7314 C C   . GLU B 1 444 ? -6.129  35.911  -6.715  1.00 53.64  ? 539  GLU B C   1 
ATOM   7315 O O   . GLU B 1 444 ? -5.939  36.503  -5.695  1.00 52.11  ? 539  GLU B O   1 
ATOM   7316 C CB  . GLU B 1 444 ? -7.266  34.164  -5.375  1.00 58.04  ? 539  GLU B CB  1 
ATOM   7317 C CG  . GLU B 1 444 ? -8.689  34.625  -5.197  1.00 62.49  ? 539  GLU B CG  1 
ATOM   7318 C CD  . GLU B 1 444 ? -9.208  34.337  -3.816  1.00 65.37  ? 539  GLU B CD  1 
ATOM   7319 O OE1 . GLU B 1 444 ? -10.248 34.889  -3.453  1.00 69.32  ? 539  GLU B OE1 1 
ATOM   7320 O OE2 . GLU B 1 444 ? -8.569  33.577  -3.087  1.00 64.95  ? 539  GLU B OE2 1 
ATOM   7321 N N   . PRO B 1 445 ? -5.853  36.458  -7.881  1.00 52.16  ? 540  PRO B N   1 
ATOM   7322 C CA  . PRO B 1 445 ? -5.184  37.738  -8.082  1.00 52.82  ? 540  PRO B CA  1 
ATOM   7323 C C   . PRO B 1 445 ? -5.812  38.962  -7.477  1.00 52.62  ? 540  PRO B C   1 
ATOM   7324 O O   . PRO B 1 445 ? -5.131  39.938  -7.317  1.00 50.88  ? 540  PRO B O   1 
ATOM   7325 C CB  . PRO B 1 445 ? -5.135  37.871  -9.584  1.00 54.37  ? 540  PRO B CB  1 
ATOM   7326 C CG  . PRO B 1 445 ? -5.230  36.497  -10.079 1.00 55.69  ? 540  PRO B CG  1 
ATOM   7327 C CD  . PRO B 1 445 ? -6.116  35.787  -9.144  1.00 54.59  ? 540  PRO B CD  1 
ATOM   7328 N N   . ALA B 1 446 ? -7.101  38.962  -7.252  1.00 49.93  ? 541  ALA B N   1 
ATOM   7329 C CA  . ALA B 1 446 ? -7.710  40.101  -6.627  1.00 51.26  ? 541  ALA B CA  1 
ATOM   7330 C C   . ALA B 1 446 ? -7.266  40.237  -5.176  1.00 50.47  ? 541  ALA B C   1 
ATOM   7331 O O   . ALA B 1 446 ? -7.456  41.258  -4.588  1.00 50.68  ? 541  ALA B O   1 
ATOM   7332 C CB  . ALA B 1 446 ? -9.210  39.962  -6.696  1.00 53.43  ? 541  ALA B CB  1 
ATOM   7333 N N   . ILE B 1 447 ? -6.646  39.199  -4.638  1.00 46.69  ? 542  ILE B N   1 
ATOM   7334 C CA  . ILE B 1 447 ? -6.220  39.118  -3.245  1.00 49.99  ? 542  ILE B CA  1 
ATOM   7335 C C   . ILE B 1 447 ? -4.697  39.147  -3.231  1.00 47.41  ? 542  ILE B C   1 
ATOM   7336 O O   . ILE B 1 447 ? -4.061  38.623  -4.149  1.00 48.32  ? 542  ILE B O   1 
ATOM   7337 C CB  . ILE B 1 447 ? -6.766  37.820  -2.608  1.00 52.34  ? 542  ILE B CB  1 
ATOM   7338 C CG1 . ILE B 1 447 ? -8.298  37.851  -2.540  1.00 57.21  ? 542  ILE B CG1 1 
ATOM   7339 C CG2 . ILE B 1 447 ? -6.172  37.559  -1.240  1.00 51.72  ? 542  ILE B CG2 1 
ATOM   7340 C CD1 . ILE B 1 447 ? -8.844  38.955  -1.675  1.00 52.96  ? 542  ILE B CD1 1 
ATOM   7341 N N   . SER B 1 448 ? -4.106  39.770  -2.211  1.00 45.40  ? 543  SER B N   1 
ATOM   7342 C CA  . SER B 1 448 ? -2.655  39.894  -2.154  1.00 45.75  ? 543  SER B CA  1 
ATOM   7343 C C   . SER B 1 448 ? -2.105  39.371  -0.830  1.00 44.17  ? 543  SER B C   1 
ATOM   7344 O O   . SER B 1 448 ? -2.833  39.178  0.148   1.00 42.22  ? 543  SER B O   1 
ATOM   7345 C CB  . SER B 1 448 ? -2.221  41.344  -2.373  1.00 44.33  ? 543  SER B CB  1 
ATOM   7346 O OG  . SER B 1 448 ? -2.743  42.172  -1.356  1.00 40.62  ? 543  SER B OG  1 
ATOM   7347 N N   . ASN B 1 449 ? -0.794  39.131  -0.819  1.00 42.72  ? 544  ASN B N   1 
ATOM   7348 C CA  . ASN B 1 449 ? -0.091  38.647  0.369   1.00 43.19  ? 544  ASN B CA  1 
ATOM   7349 C C   . ASN B 1 449 ? 0.416   39.850  1.168   1.00 44.39  ? 544  ASN B C   1 
ATOM   7350 O O   . ASN B 1 449 ? 1.604   40.196  1.172   1.00 40.17  ? 544  ASN B O   1 
ATOM   7351 C CB  . ASN B 1 449 ? 1.032   37.706  -0.031  1.00 41.56  ? 544  ASN B CB  1 
ATOM   7352 C CG  . ASN B 1 449 ? 0.504   36.364  -0.500  1.00 46.77  ? 544  ASN B CG  1 
ATOM   7353 O OD1 . ASN B 1 449 ? -0.634  36.010  -0.202  1.00 44.45  ? 544  ASN B OD1 1 
ATOM   7354 N ND2 . ASN B 1 449 ? 1.323   35.612  -1.231  1.00 45.28  ? 544  ASN B ND2 1 
ATOM   7355 N N   . SER B 1 450 ? -0.520  40.463  1.890   1.00 41.54  ? 545  SER B N   1 
ATOM   7356 C CA  . SER B 1 450 ? -0.341  41.761  2.519   1.00 42.71  ? 545  SER B CA  1 
ATOM   7357 C C   . SER B 1 450 ? -0.968  41.714  3.904   1.00 41.92  ? 545  SER B C   1 
ATOM   7358 O O   . SER B 1 450 ? -1.796  40.844  4.192   1.00 41.33  ? 545  SER B O   1 
ATOM   7359 C CB  . SER B 1 450 ? -0.990  42.862  1.674   1.00 42.62  ? 545  SER B CB  1 
ATOM   7360 O OG  . SER B 1 450 ? -2.343  42.516  1.409   1.00 42.52  ? 545  SER B OG  1 
ATOM   7361 N N   . TYR B 1 451 ? -0.575  42.662  4.762   1.00 39.10  ? 546  TYR B N   1 
ATOM   7362 C CA  . TYR B 1 451 ? -0.977  42.621  6.167   1.00 40.48  ? 546  TYR B CA  1 
ATOM   7363 C C   . TYR B 1 451 ? -0.888  44.014  6.775   1.00 41.41  ? 546  TYR B C   1 
ATOM   7364 O O   . TYR B 1 451 ? 0.041   44.772  6.476   1.00 40.57  ? 546  TYR B O   1 
ATOM   7365 C CB  . TYR B 1 451 ? -0.109  41.633  6.979   1.00 34.08  ? 546  TYR B CB  1 
ATOM   7366 C CG  . TYR B 1 451 ? 1.340   41.696  6.557   1.00 39.89  ? 546  TYR B CG  1 
ATOM   7367 C CD1 . TYR B 1 451 ? 1.820   40.889  5.522   1.00 39.51  ? 546  TYR B CD1 1 
ATOM   7368 C CD2 . TYR B 1 451 ? 2.222   42.600  7.150   1.00 36.92  ? 546  TYR B CD2 1 
ATOM   7369 C CE1 . TYR B 1 451 ? 3.146   40.962  5.106   1.00 36.42  ? 546  TYR B CE1 1 
ATOM   7370 C CE2 . TYR B 1 451 ? 3.548   42.680  6.741   1.00 38.83  ? 546  TYR B CE2 1 
ATOM   7371 C CZ  . TYR B 1 451 ? 3.999   41.860  5.705   1.00 38.60  ? 546  TYR B CZ  1 
ATOM   7372 O OH  . TYR B 1 451 ? 5.302   41.952  5.283   1.00 38.03  ? 546  TYR B OH  1 
ATOM   7373 N N   . ASP B 1 452 ? -1.870  44.334  7.625   1.00 40.97  ? 547  ASP B N   1 
ATOM   7374 C CA  . ASP B 1 452 ? -1.847  45.480  8.537   1.00 40.41  ? 547  ASP B CA  1 
ATOM   7375 C C   . ASP B 1 452 ? -1.964  44.970  9.977   1.00 39.78  ? 547  ASP B C   1 
ATOM   7376 O O   . ASP B 1 452 ? -2.704  44.015  10.243  1.00 40.70  ? 547  ASP B O   1 
ATOM   7377 C CB  . ASP B 1 452 ? -3.021  46.464  8.263   1.00 41.34  ? 547  ASP B CB  1 
ATOM   7378 C CG  . ASP B 1 452 ? -2.827  47.316  7.002   1.00 47.68  ? 547  ASP B CG  1 
ATOM   7379 O OD1 . ASP B 1 452 ? -1.774  47.211  6.345   1.00 46.50  ? 547  ASP B OD1 1 
ATOM   7380 O OD2 . ASP B 1 452 ? -3.747  48.105  6.668   1.00 50.83  ? 547  ASP B OD2 1 
ATOM   7381 N N   . PHE B 1 453 ? -1.221  45.579  10.904  1.00 38.21  ? 548  PHE B N   1 
ATOM   7382 C CA  . PHE B 1 453 ? -1.403  45.328  12.334  1.00 38.37  ? 548  PHE B CA  1 
ATOM   7383 C C   . PHE B 1 453 ? -2.135  46.524  12.929  1.00 39.98  ? 548  PHE B C   1 
ATOM   7384 O O   . PHE B 1 453 ? -1.970  47.655  12.461  1.00 41.03  ? 548  PHE B O   1 
ATOM   7385 C CB  . PHE B 1 453 ? -0.079  45.148  13.093  1.00 35.07  ? 548  PHE B CB  1 
ATOM   7386 C CG  . PHE B 1 453 ? 0.748   43.945  12.678  1.00 36.62  ? 548  PHE B CG  1 
ATOM   7387 C CD1 . PHE B 1 453 ? 0.424   43.172  11.564  1.00 37.57  ? 548  PHE B CD1 1 
ATOM   7388 C CD2 . PHE B 1 453 ? 1.883   43.607  13.407  1.00 34.76  ? 548  PHE B CD2 1 
ATOM   7389 C CE1 . PHE B 1 453 ? 1.223   42.057  11.193  1.00 39.30  ? 548  PHE B CE1 1 
ATOM   7390 C CE2 . PHE B 1 453 ? 2.670   42.519  13.051  1.00 37.27  ? 548  PHE B CE2 1 
ATOM   7391 C CZ  . PHE B 1 453 ? 2.337   41.734  11.948  1.00 36.75  ? 548  PHE B CZ  1 
ATOM   7392 N N   . PHE B 1 454 ? -2.901  46.276  13.997  1.00 38.12  ? 549  PHE B N   1 
ATOM   7393 C CA  . PHE B 1 454 ? -3.758  47.275  14.621  1.00 42.42  ? 549  PHE B CA  1 
ATOM   7394 C C   . PHE B 1 454 ? -3.573  47.291  16.134  1.00 42.13  ? 549  PHE B C   1 
ATOM   7395 O O   . PHE B 1 454 ? -3.449  46.227  16.769  1.00 40.48  ? 549  PHE B O   1 
ATOM   7396 C CB  . PHE B 1 454 ? -5.256  47.024  14.289  1.00 40.47  ? 549  PHE B CB  1 
ATOM   7397 C CG  . PHE B 1 454 ? -5.562  47.123  12.816  1.00 42.87  ? 549  PHE B CG  1 
ATOM   7398 C CD1 . PHE B 1 454 ? -6.052  48.299  12.279  1.00 42.74  ? 549  PHE B CD1 1 
ATOM   7399 C CD2 . PHE B 1 454 ? -5.309  46.057  11.965  1.00 40.58  ? 549  PHE B CD2 1 
ATOM   7400 C CE1 . PHE B 1 454 ? -6.298  48.414  10.924  1.00 45.67  ? 549  PHE B CE1 1 
ATOM   7401 C CE2 . PHE B 1 454 ? -5.568  46.154  10.606  1.00 39.71  ? 549  PHE B CE2 1 
ATOM   7402 C CZ  . PHE B 1 454 ? -6.056  47.340  10.084  1.00 43.64  ? 549  PHE B CZ  1 
ATOM   7403 N N   . MET B 1 455 ? -3.582  48.521  16.679  1.00 38.10  ? 550  MET B N   1 
ATOM   7404 C CA  . MET B 1 455 ? -3.556  48.832  18.108  1.00 41.08  ? 550  MET B CA  1 
ATOM   7405 C C   . MET B 1 455 ? -4.737  49.747  18.419  1.00 42.83  ? 550  MET B C   1 
ATOM   7406 O O   . MET B 1 455 ? -4.886  50.808  17.800  1.00 41.89  ? 550  MET B O   1 
ATOM   7407 C CB  . MET B 1 455 ? -2.240  49.506  18.523  1.00 37.66  ? 550  MET B CB  1 
ATOM   7408 C CG  . MET B 1 455 ? -0.986  48.634  18.359  1.00 38.90  ? 550  MET B CG  1 
ATOM   7409 S SD  . MET B 1 455 ? 0.540   49.514  18.793  1.00 38.82  ? 550  MET B SD  1 
ATOM   7410 C CE  . MET B 1 455 ? 0.121   50.100  20.398  1.00 37.30  ? 550  MET B CE  1 
ATOM   7411 N N   . ARG B 1 456 ? -5.571  49.340  19.373  1.00 40.57  ? 551  ARG B N   1 
ATOM   7412 C CA  . ARG B 1 456 ? -6.781  50.084  19.713  1.00 46.19  ? 551  ARG B CA  1 
ATOM   7413 C C   . ARG B 1 456 ? -7.573  50.432  18.455  1.00 46.42  ? 551  ARG B C   1 
ATOM   7414 O O   . ARG B 1 456 ? -8.077  51.549  18.298  1.00 48.26  ? 551  ARG B O   1 
ATOM   7415 C CB  . ARG B 1 456 ? -6.458  51.345  20.527  1.00 44.77  ? 551  ARG B CB  1 
ATOM   7416 C CG  . ARG B 1 456 ? -5.730  51.060  21.839  1.00 46.27  ? 551  ARG B CG  1 
ATOM   7417 C CD  . ARG B 1 456 ? -5.744  52.276  22.765  1.00 46.05  ? 551  ARG B CD  1 
ATOM   7418 N NE  . ARG B 1 456 ? -4.857  52.089  23.909  1.00 43.33  ? 551  ARG B NE  1 
ATOM   7419 C CZ  . ARG B 1 456 ? -5.231  51.597  25.083  1.00 45.81  ? 551  ARG B CZ  1 
ATOM   7420 N NH1 . ARG B 1 456 ? -6.493  51.256  25.327  1.00 44.68  ? 551  ARG B NH1 1 
ATOM   7421 N NH2 . ARG B 1 456 ? -4.314  51.432  26.035  1.00 44.62  ? 551  ARG B NH2 1 
ATOM   7422 N N   . GLY B 1 457 ? -7.659  49.467  17.539  1.00 43.67  ? 552  GLY B N   1 
ATOM   7423 C CA  . GLY B 1 457 ? -8.443  49.625  16.331  1.00 43.20  ? 552  GLY B CA  1 
ATOM   7424 C C   . GLY B 1 457 ? -7.828  50.472  15.233  1.00 50.00  ? 552  GLY B C   1 
ATOM   7425 O O   . GLY B 1 457 ? -8.494  50.701  14.217  1.00 51.03  ? 552  GLY B O   1 
ATOM   7426 N N   . GLU B 1 458 ? -6.586  50.942  15.381  1.00 43.60  ? 553  GLU B N   1 
ATOM   7427 C CA  . GLU B 1 458 ? -5.984  51.826  14.393  1.00 45.99  ? 553  GLU B CA  1 
ATOM   7428 C C   . GLU B 1 458 ? -4.718  51.188  13.840  1.00 42.96  ? 553  GLU B C   1 
ATOM   7429 O O   . GLU B 1 458 ? -3.971  50.526  14.568  1.00 39.62  ? 553  GLU B O   1 
ATOM   7430 C CB  . GLU B 1 458 ? -5.689  53.228  14.990  1.00 45.45  ? 553  GLU B CB  1 
ATOM   7431 C CG  . GLU B 1 458 ? -6.949  53.865  15.605  1.00 52.18  ? 553  GLU B CG  1 
ATOM   7432 C CD  . GLU B 1 458 ? -6.786  55.322  16.054  1.00 57.39  ? 553  GLU B CD  1 
ATOM   7433 O OE1 . GLU B 1 458 ? -6.193  56.129  15.303  1.00 57.65  ? 553  GLU B OE1 1 
ATOM   7434 O OE2 . GLU B 1 458 ? -7.262  55.655  17.166  1.00 54.38  ? 553  GLU B OE2 1 
ATOM   7435 N N   . GLU B 1 459 ? -4.487  51.389  12.548  1.00 44.52  ? 554  GLU B N   1 
ATOM   7436 C CA  . GLU B 1 459 ? -3.364  50.754  11.868  1.00 46.56  ? 554  GLU B CA  1 
ATOM   7437 C C   . GLU B 1 459 ? -2.021  51.333  12.325  1.00 42.10  ? 554  GLU B C   1 
ATOM   7438 O O   . GLU B 1 459 ? -1.840  52.554  12.334  1.00 43.75  ? 554  GLU B O   1 
ATOM   7439 C CB  . GLU B 1 459 ? -3.538  50.928  10.363  1.00 44.86  ? 554  GLU B CB  1 
ATOM   7440 C CG  . GLU B 1 459 ? -2.437  50.254  9.564   1.00 50.12  ? 554  GLU B CG  1 
ATOM   7441 C CD  . GLU B 1 459 ? -1.508  51.273  8.955   1.00 54.39  ? 554  GLU B CD  1 
ATOM   7442 O OE1 . GLU B 1 459 ? -0.327  51.350  9.382   1.00 56.77  ? 554  GLU B OE1 1 
ATOM   7443 O OE2 . GLU B 1 459 ? -1.981  52.015  8.067   1.00 57.61  ? 554  GLU B OE2 1 
ATOM   7444 N N   . ILE B 1 460 ? -1.080  50.480  12.681  1.00 39.96  ? 555  ILE B N   1 
ATOM   7445 C CA  . ILE B 1 460 ? 0.239   50.913  13.119  1.00 44.61  ? 555  ILE B CA  1 
ATOM   7446 C C   . ILE B 1 460 ? 1.379   50.386  12.259  1.00 41.57  ? 555  ILE B C   1 
ATOM   7447 O O   . ILE B 1 460 ? 2.430   50.960  12.197  1.00 43.08  ? 555  ILE B O   1 
ATOM   7448 C CB  . ILE B 1 460 ? 0.548   50.449  14.529  1.00 41.34  ? 555  ILE B CB  1 
ATOM   7449 C CG1 . ILE B 1 460 ? 0.065   49.039  14.712  1.00 38.72  ? 555  ILE B CG1 1 
ATOM   7450 C CG2 . ILE B 1 460 ? -0.107  51.331  15.533  1.00 46.40  ? 555  ILE B CG2 1 
ATOM   7451 C CD1 . ILE B 1 460 ? 0.981   48.222  15.549  1.00 43.96  ? 555  ILE B CD1 1 
ATOM   7452 N N   . LEU B 1 461 ? 1.140   49.267  11.623  1.00 42.39  ? 556  LEU B N   1 
ATOM   7453 C CA  . LEU B 1 461 ? 2.094   48.567  10.769  1.00 40.76  ? 556  LEU B CA  1 
ATOM   7454 C C   . LEU B 1 461 ? 1.418   48.210  9.452   1.00 42.67  ? 556  LEU B C   1 
ATOM   7455 O O   . LEU B 1 461 ? 0.305   47.670  9.443   1.00 42.41  ? 556  LEU B O   1 
ATOM   7456 C CB  . LEU B 1 461 ? 2.626   47.280  11.438  1.00 35.25  ? 556  LEU B CB  1 
ATOM   7457 C CG  . LEU B 1 461 ? 3.624   46.406  10.637  1.00 39.97  ? 556  LEU B CG  1 
ATOM   7458 C CD1 . LEU B 1 461 ? 4.534   45.587  11.573  1.00 33.63  ? 556  LEU B CD1 1 
ATOM   7459 C CD2 . LEU B 1 461 ? 2.936   45.464  9.635   1.00 39.27  ? 556  LEU B CD2 1 
ATOM   7460 N N   . SER B 1 462 ? 2.112   48.454  8.352   1.00 38.80  ? 557  SER B N   1 
ATOM   7461 C CA  . SER B 1 462 ? 1.617   48.065  7.040   1.00 42.34  ? 557  SER B CA  1 
ATOM   7462 C C   . SER B 1 462 ? 2.754   47.410  6.274   1.00 39.80  ? 557  SER B C   1 
ATOM   7463 O O   . SER B 1 462 ? 3.882   47.899  6.321   1.00 39.08  ? 557  SER B O   1 
ATOM   7464 C CB  . SER B 1 462 ? 1.111   49.275  6.271   1.00 44.01  ? 557  SER B CB  1 
ATOM   7465 O OG  . SER B 1 462 ? 0.374   48.863  5.143   1.00 50.12  ? 557  SER B OG  1 
ATOM   7466 N N   . GLY B 1 463 ? 2.472   46.325  5.564   1.00 37.40  ? 558  GLY B N   1 
ATOM   7467 C CA  . GLY B 1 463 ? 3.532   45.721  4.775   1.00 38.66  ? 558  GLY B CA  1 
ATOM   7468 C C   . GLY B 1 463 ? 3.020   44.604  3.888   1.00 40.83  ? 558  GLY B C   1 
ATOM   7469 O O   . GLY B 1 463 ? 1.810   44.370  3.783   1.00 40.10  ? 558  GLY B O   1 
ATOM   7470 N N   . SER B 1 464 ? 3.968   43.897  3.267   1.00 38.46  ? 559  SER B N   1 
ATOM   7471 C CA  . SER B 1 464 ? 3.584   42.822  2.340   1.00 39.77  ? 559  SER B CA  1 
ATOM   7472 C C   . SER B 1 464 ? 4.791   41.993  1.915   1.00 39.51  ? 559  SER B C   1 
ATOM   7473 O O   . SER B 1 464 ? 5.956   42.402  2.066   1.00 39.14  ? 559  SER B O   1 
ATOM   7474 C CB  . SER B 1 464 ? 2.881   43.356  1.077   1.00 38.85  ? 559  SER B CB  1 
ATOM   7475 O OG  . SER B 1 464 ? 3.807   43.913  0.141   1.00 39.74  ? 559  SER B OG  1 
ATOM   7476 N N   . GLN B 1 465 ? 4.475   40.792  1.417   1.00 39.80  ? 560  GLN B N   1 
ATOM   7477 C CA  . GLN B 1 465 ? 5.348   40.091  0.482   1.00 39.68  ? 560  GLN B CA  1 
ATOM   7478 C C   . GLN B 1 465 ? 5.558   40.971  -0.746  1.00 40.96  ? 560  GLN B C   1 
ATOM   7479 O O   . GLN B 1 465 ? 4.607   41.555  -1.274  1.00 40.21  ? 560  GLN B O   1 
ATOM   7480 C CB  . GLN B 1 465 ? 4.727   38.742  0.072   1.00 40.16  ? 560  GLN B CB  1 
ATOM   7481 C CG  . GLN B 1 465 ? 5.576   37.915  -0.920  1.00 40.06  ? 560  GLN B CG  1 
ATOM   7482 C CD  . GLN B 1 465 ? 4.894   36.631  -1.397  1.00 45.27  ? 560  GLN B CD  1 
ATOM   7483 O OE1 . GLN B 1 465 ? 4.031   36.079  -0.727  1.00 48.87  ? 560  GLN B OE1 1 
ATOM   7484 N NE2 . GLN B 1 465 ? 5.299   36.149  -2.558  1.00 47.02  ? 560  GLN B NE2 1 
ATOM   7485 N N   . ARG B 1 466 ? 6.807   41.090  -1.185  1.00 38.85  ? 561  ARG B N   1 
ATOM   7486 C CA  . ARG B 1 466 ? 7.152   41.936  -2.318  1.00 36.92  ? 561  ARG B CA  1 
ATOM   7487 C C   . ARG B 1 466 ? 7.221   41.088  -3.574  1.00 40.96  ? 561  ARG B C   1 
ATOM   7488 O O   . ARG B 1 466 ? 7.581   39.906  -3.527  1.00 39.48  ? 561  ARG B O   1 
ATOM   7489 C CB  . ARG B 1 466 ? 8.499   42.646  -2.111  1.00 38.41  ? 561  ARG B CB  1 
ATOM   7490 C CG  . ARG B 1 466 ? 8.734   43.184  -0.696  1.00 39.60  ? 561  ARG B CG  1 
ATOM   7491 C CD  . ARG B 1 466 ? 7.653   44.200  -0.270  1.00 37.70  ? 561  ARG B CD  1 
ATOM   7492 N NE  . ARG B 1 466 ? 8.089   44.910  0.934   1.00 39.63  ? 561  ARG B NE  1 
ATOM   7493 C CZ  . ARG B 1 466 ? 7.323   45.712  1.661   1.00 39.39  ? 561  ARG B CZ  1 
ATOM   7494 N NH1 . ARG B 1 466 ? 6.041   45.892  1.375   1.00 38.68  ? 561  ARG B NH1 1 
ATOM   7495 N NH2 . ARG B 1 466 ? 7.858   46.349  2.703   1.00 39.79  ? 561  ARG B NH2 1 
ATOM   7496 N N   . ILE B 1 467 ? 6.857   41.703  -4.697  1.00 40.22  ? 562  ILE B N   1 
ATOM   7497 C CA  . ILE B 1 467 ? 7.137   41.130  -6.007  1.00 41.27  ? 562  ILE B CA  1 
ATOM   7498 C C   . ILE B 1 467 ? 8.650   41.038  -6.172  1.00 42.79  ? 562  ILE B C   1 
ATOM   7499 O O   . ILE B 1 467 ? 9.354   42.053  -6.161  1.00 39.53  ? 562  ILE B O   1 
ATOM   7500 C CB  . ILE B 1 467 ? 6.501   41.987  -7.114  1.00 40.81  ? 562  ILE B CB  1 
ATOM   7501 C CG1 . ILE B 1 467 ? 4.976   42.025  -6.951  1.00 42.29  ? 562  ILE B CG1 1 
ATOM   7502 C CG2 . ILE B 1 467 ? 6.884   41.453  -8.484  1.00 41.86  ? 562  ILE B CG2 1 
ATOM   7503 C CD1 . ILE B 1 467 ? 4.267   42.915  -7.954  1.00 43.95  ? 562  ILE B CD1 1 
ATOM   7504 N N   . SER B 1 468 ? 9.164   39.821  -6.311  1.00 42.83  ? 563  SER B N   1 
ATOM   7505 C CA  . SER B 1 468 ? 10.604  39.611  -6.416  1.00 41.37  ? 563  SER B CA  1 
ATOM   7506 C C   . SER B 1 468 ? 10.987  39.023  -7.774  1.00 45.12  ? 563  SER B C   1 
ATOM   7507 O O   . SER B 1 468 ? 12.004  38.340  -7.912  1.00 48.23  ? 563  SER B O   1 
ATOM   7508 C CB  . SER B 1 468 ? 11.091  38.727  -5.269  1.00 43.14  ? 563  SER B CB  1 
ATOM   7509 O OG  . SER B 1 468 ? 10.346  37.527  -5.246  1.00 45.30  ? 563  SER B OG  1 
ATOM   7510 N N   . ASP B 1 469 ? 10.171  39.280  -8.787  1.00 47.10  ? 564  ASP B N   1 
ATOM   7511 C CA  . ASP B 1 469 ? 10.445  38.880  -10.160 1.00 43.18  ? 564  ASP B CA  1 
ATOM   7512 C C   . ASP B 1 469 ? 10.364  40.127  -11.025 1.00 47.20  ? 564  ASP B C   1 
ATOM   7513 O O   . ASP B 1 469 ? 9.328   40.804  -11.032 1.00 46.93  ? 564  ASP B O   1 
ATOM   7514 C CB  . ASP B 1 469 ? 9.439   37.834  -10.638 1.00 44.08  ? 564  ASP B CB  1 
ATOM   7515 C CG  . ASP B 1 469 ? 9.663   37.436  -12.084 1.00 49.52  ? 564  ASP B CG  1 
ATOM   7516 O OD1 . ASP B 1 469 ? 10.312  36.400  -12.314 1.00 54.78  ? 564  ASP B OD1 1 
ATOM   7517 O OD2 . ASP B 1 469 ? 9.222   38.169  -12.991 1.00 50.46  ? 564  ASP B OD2 1 
ATOM   7518 N N   . VAL B 1 470 ? 11.448  40.433  -11.749 1.00 42.54  ? 565  VAL B N   1 
ATOM   7519 C CA  . VAL B 1 470 ? 11.544  41.736  -12.401 1.00 43.93  ? 565  VAL B CA  1 
ATOM   7520 C C   . VAL B 1 470 ? 10.464  41.898  -13.466 1.00 46.85  ? 565  VAL B C   1 
ATOM   7521 O O   . VAL B 1 470 ? 9.920   43.002  -13.651 1.00 45.43  ? 565  VAL B O   1 
ATOM   7522 C CB  . VAL B 1 470 ? 12.967  41.949  -12.959 1.00 43.54  ? 565  VAL B CB  1 
ATOM   7523 C CG1 . VAL B 1 470 ? 13.268  41.006  -14.129 1.00 44.35  ? 565  VAL B CG1 1 
ATOM   7524 C CG2 . VAL B 1 470 ? 13.149  43.390  -13.366 1.00 44.20  ? 565  VAL B CG2 1 
ATOM   7525 N N   . ASN B 1 471 ? 10.080  40.800  -14.129 1.00 45.89  ? 566  ASN B N   1 
ATOM   7526 C CA  . ASN B 1 471 ? 9.048   40.874  -15.163 1.00 49.07  ? 566  ASN B CA  1 
ATOM   7527 C C   . ASN B 1 471 ? 7.659   41.074  -14.561 1.00 49.99  ? 566  ASN B C   1 
ATOM   7528 O O   . ASN B 1 471 ? 6.879   41.907  -15.048 1.00 50.73  ? 566  ASN B O   1 
ATOM   7529 C CB  . ASN B 1 471 ? 9.095   39.615  -16.023 1.00 45.97  ? 566  ASN B CB  1 
ATOM   7530 C CG  . ASN B 1 471 ? 10.395  39.496  -16.796 1.00 53.15  ? 566  ASN B CG  1 
ATOM   7531 O OD1 . ASN B 1 471 ? 11.125  38.518  -16.653 1.00 59.50  ? 566  ASN B OD1 1 
ATOM   7532 N ND2 . ASN B 1 471 ? 10.703  40.505  -17.590 1.00 50.17  ? 566  ASN B ND2 1 
ATOM   7533 N N   . LEU B 1 472 ? 7.330   40.329  -13.499 1.00 47.96  ? 567  LEU B N   1 
ATOM   7534 C CA  . LEU B 1 472 ? 6.073   40.582  -12.803 1.00 50.26  ? 567  LEU B CA  1 
ATOM   7535 C C   . LEU B 1 472 ? 6.040   41.997  -12.245 1.00 46.21  ? 567  LEU B C   1 
ATOM   7536 O O   . LEU B 1 472 ? 4.994   42.656  -12.273 1.00 46.84  ? 567  LEU B O   1 
ATOM   7537 C CB  . LEU B 1 472 ? 5.860   39.561  -11.684 1.00 46.37  ? 567  LEU B CB  1 
ATOM   7538 C CG  . LEU B 1 472 ? 5.781   38.115  -12.170 1.00 52.78  ? 567  LEU B CG  1 
ATOM   7539 C CD1 . LEU B 1 472 ? 5.450   37.191  -11.007 1.00 51.29  ? 567  LEU B CD1 1 
ATOM   7540 C CD2 . LEU B 1 472 ? 4.755   37.981  -13.302 1.00 49.96  ? 567  LEU B CD2 1 
ATOM   7541 N N   . LEU B 1 473 ? 7.184   42.489  -11.758 1.00 44.51  ? 568  LEU B N   1 
ATOM   7542 C CA  . LEU B 1 473 ? 7.247   43.844  -11.225 1.00 45.54  ? 568  LEU B CA  1 
ATOM   7543 C C   . LEU B 1 473 ? 6.912   44.869  -12.302 1.00 47.23  ? 568  LEU B C   1 
ATOM   7544 O O   . LEU B 1 473 ? 6.119   45.791  -12.071 1.00 45.32  ? 568  LEU B O   1 
ATOM   7545 C CB  . LEU B 1 473 ? 8.633   44.111  -10.631 1.00 45.51  ? 568  LEU B CB  1 
ATOM   7546 C CG  . LEU B 1 473 ? 8.854   45.491  -9.974  1.00 43.28  ? 568  LEU B CG  1 
ATOM   7547 C CD1 . LEU B 1 473 ? 7.933   45.696  -8.778  1.00 40.04  ? 568  LEU B CD1 1 
ATOM   7548 C CD2 . LEU B 1 473 ? 10.299  45.700  -9.547  1.00 42.24  ? 568  LEU B CD2 1 
ATOM   7549 N N   . LEU B 1 474 ? 7.510   44.722  -13.489 1.00 48.62  ? 569  LEU B N   1 
ATOM   7550 C CA  . LEU B 1 474 ? 7.204   45.637  -14.586 1.00 49.39  ? 569  LEU B CA  1 
ATOM   7551 C C   . LEU B 1 474 ? 5.738   45.556  -14.984 1.00 48.62  ? 569  LEU B C   1 
ATOM   7552 O O   . LEU B 1 474 ? 5.103   46.588  -15.247 1.00 51.50  ? 569  LEU B O   1 
ATOM   7553 C CB  . LEU B 1 474 ? 8.101   45.343  -15.788 1.00 50.30  ? 569  LEU B CB  1 
ATOM   7554 C CG  . LEU B 1 474 ? 9.519   45.905  -15.692 1.00 52.64  ? 569  LEU B CG  1 
ATOM   7555 C CD1 . LEU B 1 474 ? 10.417  45.198  -16.706 1.00 50.81  ? 569  LEU B CD1 1 
ATOM   7556 C CD2 . LEU B 1 474 ? 9.509   47.413  -15.953 1.00 51.32  ? 569  LEU B CD2 1 
ATOM   7557 N N   . GLU B 1 475 ? 5.188   44.339  -15.056 1.00 51.02  ? 570  GLU B N   1 
ATOM   7558 C CA  . GLU B 1 475 ? 3.766   44.185  -15.372 1.00 49.04  ? 570  GLU B CA  1 
ATOM   7559 C C   . GLU B 1 475 ? 2.898   44.929  -14.370 1.00 51.31  ? 570  GLU B C   1 
ATOM   7560 O O   . GLU B 1 475 ? 1.930   45.594  -14.749 1.00 50.51  ? 570  GLU B O   1 
ATOM   7561 C CB  . GLU B 1 475 ? 3.370   42.709  -15.381 1.00 50.53  ? 570  GLU B CB  1 
ATOM   7562 C CG  . GLU B 1 475 ? 3.497   41.995  -16.726 1.00 62.23  ? 570  GLU B CG  1 
ATOM   7563 C CD  . GLU B 1 475 ? 3.669   40.483  -16.563 1.00 69.29  ? 570  GLU B CD  1 
ATOM   7564 O OE1 . GLU B 1 475 ? 2.881   39.858  -15.805 1.00 67.04  ? 570  GLU B OE1 1 
ATOM   7565 O OE2 . GLU B 1 475 ? 4.614   39.925  -17.174 1.00 71.10  ? 570  GLU B OE2 1 
ATOM   7566 N N   . ASN B 1 476 ? 3.227   44.826  -13.082 1.00 49.93  ? 571  ASN B N   1 
ATOM   7567 C CA  . ASN B 1 476 ? 2.385   45.458  -12.073 1.00 51.01  ? 571  ASN B CA  1 
ATOM   7568 C C   . ASN B 1 476 ? 2.547   46.967  -12.090 1.00 50.55  ? 571  ASN B C   1 
ATOM   7569 O O   . ASN B 1 476 ? 1.582   47.700  -11.856 1.00 51.72  ? 571  ASN B O   1 
ATOM   7570 C CB  . ASN B 1 476 ? 2.704   44.911  -10.687 1.00 50.33  ? 571  ASN B CB  1 
ATOM   7571 C CG  . ASN B 1 476 ? 1.463   44.604  -9.908  1.00 50.01  ? 571  ASN B CG  1 
ATOM   7572 O OD1 . ASN B 1 476 ? 0.500   44.074  -10.456 1.00 52.92  ? 571  ASN B OD1 1 
ATOM   7573 N ND2 . ASN B 1 476 ? 1.464   44.945  -8.629  1.00 50.13  ? 571  ASN B ND2 1 
ATOM   7574 N N   . ILE B 1 477 ? 3.765   47.445  -12.359 1.00 50.40  ? 572  ILE B N   1 
ATOM   7575 C CA  . ILE B 1 477 ? 4.010   48.876  -12.528 1.00 50.94  ? 572  ILE B CA  1 
ATOM   7576 C C   . ILE B 1 477 ? 3.161   49.436  -13.663 1.00 56.11  ? 572  ILE B C   1 
ATOM   7577 O O   . ILE B 1 477 ? 2.597   50.532  -13.551 1.00 56.35  ? 572  ILE B O   1 
ATOM   7578 C CB  . ILE B 1 477 ? 5.512   49.118  -12.767 1.00 51.05  ? 572  ILE B CB  1 
ATOM   7579 C CG1 . ILE B 1 477 ? 6.293   48.867  -11.481 1.00 46.42  ? 572  ILE B CG1 1 
ATOM   7580 C CG2 . ILE B 1 477 ? 5.780   50.521  -13.309 1.00 51.80  ? 572  ILE B CG2 1 
ATOM   7581 C CD1 . ILE B 1 477 ? 7.816   48.877  -11.695 1.00 47.11  ? 572  ILE B CD1 1 
ATOM   7582 N N   . LYS B 1 478 ? 3.059   48.697  -14.775 1.00 54.17  ? 573  LYS B N   1 
ATOM   7583 C CA  . LYS B 1 478 ? 2.177   49.118  -15.868 1.00 53.09  ? 573  LYS B CA  1 
ATOM   7584 C C   . LYS B 1 478 ? 0.708   49.015  -15.462 1.00 57.70  ? 573  LYS B C   1 
ATOM   7585 O O   . LYS B 1 478 ? -0.116  49.859  -15.837 1.00 57.74  ? 573  LYS B O   1 
ATOM   7586 C CB  . LYS B 1 478 ? 2.450   48.266  -17.113 1.00 54.21  ? 573  LYS B CB  1 
ATOM   7587 C CG  . LYS B 1 478 ? 1.598   48.610  -18.327 1.00 61.31  ? 573  LYS B CG  1 
ATOM   7588 C CD  . LYS B 1 478 ? 1.796   47.616  -19.472 1.00 66.43  ? 573  LYS B CD  1 
ATOM   7589 N N   . ARG B 1 479 ? 0.365   47.979  -14.697 1.00 56.24  ? 574  ARG B N   1 
ATOM   7590 C CA  . ARG B 1 479 ? -1.010  47.776  -14.254 1.00 56.06  ? 574  ARG B CA  1 
ATOM   7591 C C   . ARG B 1 479 ? -1.491  48.941  -13.394 1.00 57.17  ? 574  ARG B C   1 
ATOM   7592 O O   . ARG B 1 479 ? -2.669  49.307  -13.437 1.00 56.53  ? 574  ARG B O   1 
ATOM   7593 C CB  . ARG B 1 479 ? -1.099  46.445  -13.493 1.00 56.57  ? 574  ARG B CB  1 
ATOM   7594 C CG  . ARG B 1 479 ? -2.403  45.679  -13.664 1.00 65.12  ? 574  ARG B CG  1 
ATOM   7595 C CD  . ARG B 1 479 ? -2.371  44.281  -13.003 1.00 65.91  ? 574  ARG B CD  1 
ATOM   7596 N NE  . ARG B 1 479 ? -2.154  43.202  -13.970 1.00 70.15  ? 574  ARG B NE  1 
ATOM   7597 C CZ  . ARG B 1 479 ? -1.059  42.448  -14.046 1.00 70.10  ? 574  ARG B CZ  1 
ATOM   7598 N NH1 . ARG B 1 479 ? -0.046  42.596  -13.194 1.00 57.72  ? 574  ARG B NH1 1 
ATOM   7599 N NH2 . ARG B 1 479 ? -0.981  41.516  -14.998 1.00 72.65  ? 574  ARG B NH2 1 
ATOM   7600 N N   . PHE B 1 480 ? -0.588  49.553  -12.629 1.00 58.16  ? 575  PHE B N   1 
ATOM   7601 C CA  . PHE B 1 480 ? -0.900  50.710  -11.798 1.00 56.86  ? 575  PHE B CA  1 
ATOM   7602 C C   . PHE B 1 480 ? -0.642  52.037  -12.507 1.00 59.56  ? 575  PHE B C   1 
ATOM   7603 O O   . PHE B 1 480 ? -0.724  53.089  -11.864 1.00 59.00  ? 575  PHE B O   1 
ATOM   7604 C CB  . PHE B 1 480 ? -0.102  50.648  -10.490 1.00 54.69  ? 575  PHE B CB  1 
ATOM   7605 C CG  . PHE B 1 480 ? -0.691  49.706  -9.472  1.00 52.82  ? 575  PHE B CG  1 
ATOM   7606 C CD1 . PHE B 1 480 ? -1.583  50.167  -8.516  1.00 57.77  ? 575  PHE B CD1 1 
ATOM   7607 C CD2 . PHE B 1 480 ? -0.380  48.356  -9.489  1.00 50.11  ? 575  PHE B CD2 1 
ATOM   7608 C CE1 . PHE B 1 480 ? -2.149  49.289  -7.581  1.00 56.21  ? 575  PHE B CE1 1 
ATOM   7609 C CE2 . PHE B 1 480 ? -0.938  47.478  -8.565  1.00 51.46  ? 575  PHE B CE2 1 
ATOM   7610 C CZ  . PHE B 1 480 ? -1.818  47.946  -7.609  1.00 52.57  ? 575  PHE B CZ  1 
ATOM   7611 N N   . ASN B 1 481 ? -0.332  52.006  -13.808 1.00 58.38  ? 576  ASN B N   1 
ATOM   7612 C CA  . ASN B 1 481 ? -0.125  53.211  -14.620 1.00 60.15  ? 576  ASN B CA  1 
ATOM   7613 C C   . ASN B 1 481 ? 1.024   54.065  -14.084 1.00 60.52  ? 576  ASN B C   1 
ATOM   7614 O O   . ASN B 1 481 ? 0.997   55.293  -14.153 1.00 60.39  ? 576  ASN B O   1 
ATOM   7615 C CB  . ASN B 1 481 ? -1.404  54.048  -14.729 1.00 63.48  ? 576  ASN B CB  1 
ATOM   7616 C CG  . ASN B 1 481 ? -2.606  53.234  -15.176 1.00 68.75  ? 576  ASN B CG  1 
ATOM   7617 O OD1 . ASN B 1 481 ? -2.592  52.595  -16.234 1.00 74.72  ? 576  ASN B OD1 1 
ATOM   7618 N ND2 . ASN B 1 481 ? -3.663  53.253  -14.364 1.00 71.01  ? 576  ASN B ND2 1 
ATOM   7619 N N   . LEU B 1 482 ? 2.048   53.421  -13.551 1.00 60.19  ? 577  LEU B N   1 
ATOM   7620 C CA  . LEU B 1 482 ? 3.198   54.164  -13.065 1.00 60.10  ? 577  LEU B CA  1 
ATOM   7621 C C   . LEU B 1 482 ? 4.242   54.322  -14.171 1.00 59.60  ? 577  LEU B C   1 
ATOM   7622 O O   . LEU B 1 482 ? 4.245   53.595  -15.167 1.00 58.61  ? 577  LEU B O   1 
ATOM   7623 C CB  . LEU B 1 482 ? 3.796   53.471  -11.838 1.00 56.27  ? 577  LEU B CB  1 
ATOM   7624 C CG  . LEU B 1 482 ? 2.845   53.491  -10.636 1.00 59.47  ? 577  LEU B CG  1 
ATOM   7625 C CD1 . LEU B 1 482 ? 3.497   52.894  -9.395  1.00 54.44  ? 577  LEU B CD1 1 
ATOM   7626 C CD2 . LEU B 1 482 ? 2.398   54.911  -10.362 1.00 59.62  ? 577  LEU B CD2 1 
ATOM   7627 N N   . ASP B 1 483 ? 5.137   55.290  -13.979 1.00 60.48  ? 578  ASP B N   1 
ATOM   7628 C CA  . ASP B 1 483 ? 6.185   55.608  -14.951 1.00 64.03  ? 578  ASP B CA  1 
ATOM   7629 C C   . ASP B 1 483 ? 7.427   54.791  -14.615 1.00 59.89  ? 578  ASP B C   1 
ATOM   7630 O O   . ASP B 1 483 ? 8.209   55.166  -13.739 1.00 59.46  ? 578  ASP B O   1 
ATOM   7631 C CB  . ASP B 1 483 ? 6.479   57.106  -14.942 1.00 65.43  ? 578  ASP B CB  1 
ATOM   7632 C CG  . ASP B 1 483 ? 7.444   57.533  -16.041 1.00 68.56  ? 578  ASP B CG  1 
ATOM   7633 O OD1 . ASP B 1 483 ? 8.181   56.681  -16.584 1.00 66.59  ? 578  ASP B OD1 1 
ATOM   7634 O OD2 . ASP B 1 483 ? 7.468   58.744  -16.357 1.00 74.32  ? 578  ASP B OD2 1 
ATOM   7635 N N   . ALA B 1 484 ? 7.624   53.684  -15.340 1.00 59.05  ? 579  ALA B N   1 
ATOM   7636 C CA  . ALA B 1 484 ? 8.765   52.807  -15.082 1.00 58.74  ? 579  ALA B CA  1 
ATOM   7637 C C   . ALA B 1 484 ? 10.098  53.542  -15.182 1.00 61.60  ? 579  ALA B C   1 
ATOM   7638 O O   . ALA B 1 484 ? 11.060  53.168  -14.499 1.00 58.65  ? 579  ALA B O   1 
ATOM   7639 C CB  . ALA B 1 484 ? 8.750   51.627  -16.046 1.00 56.91  ? 579  ALA B CB  1 
ATOM   7640 N N   . ASN B 1 485 ? 10.182  54.587  -16.013 1.00 59.97  ? 580  ASN B N   1 
ATOM   7641 C CA  . ASN B 1 485 ? 11.450  55.305  -16.133 1.00 61.07  ? 580  ASN B CA  1 
ATOM   7642 C C   . ASN B 1 485 ? 11.814  56.018  -14.840 1.00 60.62  ? 580  ASN B C   1 
ATOM   7643 O O   . ASN B 1 485 ? 13.003  56.184  -14.538 1.00 61.22  ? 580  ASN B O   1 
ATOM   7644 C CB  . ASN B 1 485 ? 11.399  56.294  -17.292 1.00 64.99  ? 580  ASN B CB  1 
ATOM   7645 C CG  . ASN B 1 485 ? 11.776  55.651  -18.599 1.00 68.20  ? 580  ASN B CG  1 
ATOM   7646 O OD1 . ASN B 1 485 ? 10.939  55.491  -19.486 1.00 70.84  ? 580  ASN B OD1 1 
ATOM   7647 N ND2 . ASN B 1 485 ? 13.039  55.263  -18.726 1.00 75.80  ? 580  ASN B ND2 1 
ATOM   7648 N N   . LYS B 1 486 ? 10.815  56.416  -14.057 1.00 60.35  ? 581  LYS B N   1 
ATOM   7649 C CA  . LYS B 1 486 ? 11.050  57.010  -12.750 1.00 61.72  ? 581  LYS B CA  1 
ATOM   7650 C C   . LYS B 1 486 ? 11.421  55.982  -11.686 1.00 59.68  ? 581  LYS B C   1 
ATOM   7651 O O   . LYS B 1 486 ? 11.728  56.375  -10.557 1.00 60.07  ? 581  LYS B O   1 
ATOM   7652 C CB  . LYS B 1 486 ? 9.810   57.793  -12.317 1.00 64.07  ? 581  LYS B CB  1 
ATOM   7653 C CG  . LYS B 1 486 ? 9.495   58.982  -13.229 1.00 69.02  ? 581  LYS B CG  1 
ATOM   7654 C CD  . LYS B 1 486 ? 8.284   59.763  -12.748 1.00 74.04  ? 581  LYS B CD  1 
ATOM   7655 C CE  . LYS B 1 486 ? 8.067   61.015  -13.597 1.00 78.59  ? 581  LYS B CE  1 
ATOM   7656 N NZ  . LYS B 1 486 ? 6.860   61.763  -13.156 1.00 80.48  ? 581  LYS B NZ  1 
ATOM   7657 N N   . LEU B 1 487 ? 11.403  54.686  -12.011 1.00 54.84  ? 582  LEU B N   1 
ATOM   7658 C CA  . LEU B 1 487 ? 11.727  53.641  -11.050 1.00 52.90  ? 582  LEU B CA  1 
ATOM   7659 C C   . LEU B 1 487 ? 12.881  52.763  -11.527 1.00 51.16  ? 582  LEU B C   1 
ATOM   7660 O O   . LEU B 1 487 ? 13.129  51.706  -10.931 1.00 48.74  ? 582  LEU B O   1 
ATOM   7661 C CB  . LEU B 1 487 ? 10.484  52.780  -10.769 1.00 51.68  ? 582  LEU B CB  1 
ATOM   7662 C CG  . LEU B 1 487 ? 9.345   53.452  -9.997  1.00 53.09  ? 582  LEU B CG  1 
ATOM   7663 C CD1 . LEU B 1 487 ? 7.994   52.800  -10.265 1.00 48.77  ? 582  LEU B CD1 1 
ATOM   7664 C CD2 . LEU B 1 487 ? 9.651   53.442  -8.504  1.00 48.20  ? 582  LEU B CD2 1 
ATOM   7665 N N   . ASN B 1 488 ? 13.615  53.192  -12.556 1.00 48.99  ? 583  ASN B N   1 
ATOM   7666 C CA  . ASN B 1 488 ? 14.480  52.268  -13.278 1.00 49.27  ? 583  ASN B CA  1 
ATOM   7667 C C   . ASN B 1 488 ? 15.588  51.722  -12.384 1.00 49.13  ? 583  ASN B C   1 
ATOM   7668 O O   . ASN B 1 488 ? 15.836  50.509  -12.373 1.00 48.83  ? 583  ASN B O   1 
ATOM   7669 C CB  . ASN B 1 488 ? 15.041  52.939  -14.535 1.00 57.04  ? 583  ASN B CB  1 
ATOM   7670 C CG  . ASN B 1 488 ? 15.935  54.112  -14.221 1.00 61.80  ? 583  ASN B CG  1 
ATOM   7671 O OD1 . ASN B 1 488 ? 15.512  55.078  -13.585 1.00 63.55  ? 583  ASN B OD1 1 
ATOM   7672 N ND2 . ASN B 1 488 ? 17.197  54.019  -14.635 1.00 63.46  ? 583  ASN B ND2 1 
ATOM   7673 N N   . PHE B 1 489 ? 16.200  52.575  -11.557 1.00 47.88  ? 584  PHE B N   1 
ATOM   7674 C CA  . PHE B 1 489 ? 17.219  52.079  -10.635 1.00 53.02  ? 584  PHE B CA  1 
ATOM   7675 C C   . PHE B 1 489 ? 16.638  51.025  -9.706  1.00 48.71  ? 584  PHE B C   1 
ATOM   7676 O O   . PHE B 1 489 ? 17.181  49.919  -9.581  1.00 48.15  ? 584  PHE B O   1 
ATOM   7677 C CB  . PHE B 1 489 ? 17.846  53.238  -9.858  1.00 48.46  ? 584  PHE B CB  1 
ATOM   7678 C CG  . PHE B 1 489 ? 18.694  54.122  -10.734 1.00 62.35  ? 584  PHE B CG  1 
ATOM   7679 C CD1 . PHE B 1 489 ? 19.975  53.726  -11.112 1.00 59.82  ? 584  PHE B CD1 1 
ATOM   7680 C CD2 . PHE B 1 489 ? 18.186  55.318  -11.244 1.00 63.29  ? 584  PHE B CD2 1 
ATOM   7681 C CE1 . PHE B 1 489 ? 20.747  54.526  -11.951 1.00 64.39  ? 584  PHE B CE1 1 
ATOM   7682 C CE2 . PHE B 1 489 ? 18.952  56.117  -12.084 1.00 63.23  ? 584  PHE B CE2 1 
ATOM   7683 C CZ  . PHE B 1 489 ? 20.230  55.721  -12.438 1.00 63.49  ? 584  PHE B CZ  1 
ATOM   7684 N N   . TYR B 1 490 ? 15.482  51.318  -9.119  1.00 45.74  ? 585  TYR B N   1 
ATOM   7685 C CA  . TYR B 1 490 ? 14.812  50.329  -8.290  1.00 45.74  ? 585  TYR B CA  1 
ATOM   7686 C C   . TYR B 1 490 ? 14.519  49.069  -9.091  1.00 42.87  ? 585  TYR B C   1 
ATOM   7687 O O   . TYR B 1 490 ? 14.859  47.961  -8.659  1.00 41.39  ? 585  TYR B O   1 
ATOM   7688 C CB  . TYR B 1 490 ? 13.532  50.930  -7.721  1.00 43.38  ? 585  TYR B CB  1 
ATOM   7689 C CG  . TYR B 1 490 ? 12.556  49.970  -7.090  1.00 40.63  ? 585  TYR B CG  1 
ATOM   7690 C CD1 . TYR B 1 490 ? 12.736  49.510  -5.784  1.00 39.30  ? 585  TYR B CD1 1 
ATOM   7691 C CD2 . TYR B 1 490 ? 11.400  49.595  -7.765  1.00 41.84  ? 585  TYR B CD2 1 
ATOM   7692 C CE1 . TYR B 1 490 ? 11.804  48.665  -5.185  1.00 38.53  ? 585  TYR B CE1 1 
ATOM   7693 C CE2 . TYR B 1 490 ? 10.462  48.759  -7.172  1.00 38.79  ? 585  TYR B CE2 1 
ATOM   7694 C CZ  . TYR B 1 490 ? 10.669  48.306  -5.888  1.00 39.74  ? 585  TYR B CZ  1 
ATOM   7695 O OH  . TYR B 1 490 ? 9.740   47.475  -5.314  1.00 39.09  ? 585  TYR B OH  1 
ATOM   7696 N N   . ILE B 1 491 ? 13.942  49.230  -10.290 1.00 42.88  ? 586  ILE B N   1 
ATOM   7697 C CA  . ILE B 1 491 ? 13.595  48.069  -11.106 1.00 46.24  ? 586  ILE B CA  1 
ATOM   7698 C C   . ILE B 1 491 ? 14.854  47.285  -11.425 1.00 45.87  ? 586  ILE B C   1 
ATOM   7699 O O   . ILE B 1 491 ? 14.879  46.045  -11.347 1.00 41.67  ? 586  ILE B O   1 
ATOM   7700 C CB  . ILE B 1 491 ? 12.876  48.503  -12.400 1.00 47.24  ? 586  ILE B CB  1 
ATOM   7701 C CG1 . ILE B 1 491 ? 11.451  48.964  -12.112 1.00 45.90  ? 586  ILE B CG1 1 
ATOM   7702 C CG2 . ILE B 1 491 ? 12.866  47.365  -13.446 1.00 42.34  ? 586  ILE B CG2 1 
ATOM   7703 C CD1 . ILE B 1 491 ? 10.901  49.825  -13.238 1.00 45.69  ? 586  ILE B CD1 1 
ATOM   7704 N N   . ASP B 1 492 ? 15.936  48.004  -11.738 1.00 44.08  ? 587  ASP B N   1 
ATOM   7705 C CA  . ASP B 1 492 ? 17.141  47.326  -12.172 1.00 45.57  ? 587  ASP B CA  1 
ATOM   7706 C C   . ASP B 1 492 ? 17.758  46.535  -11.026 1.00 46.18  ? 587  ASP B C   1 
ATOM   7707 O O   . ASP B 1 492 ? 18.463  45.545  -11.276 1.00 41.92  ? 587  ASP B O   1 
ATOM   7708 C CB  . ASP B 1 492 ? 18.108  48.353  -12.751 1.00 48.83  ? 587  ASP B CB  1 
ATOM   7709 C CG  . ASP B 1 492 ? 19.212  47.722  -13.535 1.00 56.78  ? 587  ASP B CG  1 
ATOM   7710 O OD1 . ASP B 1 492 ? 20.363  47.748  -13.040 1.00 57.77  ? 587  ASP B OD1 1 
ATOM   7711 O OD2 . ASP B 1 492 ? 18.921  47.196  -14.636 1.00 59.34  ? 587  ASP B OD2 1 
ATOM   7712 N N   . SER B 1 493 ? 17.434  46.897  -9.777  1.00 37.76  ? 588  SER B N   1 
ATOM   7713 C CA  . SER B 1 493 ? 17.948  46.120  -8.654  1.00 42.26  ? 588  SER B CA  1 
ATOM   7714 C C   . SER B 1 493 ? 17.357  44.715  -8.591  1.00 39.01  ? 588  SER B C   1 
ATOM   7715 O O   . SER B 1 493 ? 17.864  43.884  -7.835  1.00 37.78  ? 588  SER B O   1 
ATOM   7716 C CB  . SER B 1 493 ? 17.676  46.841  -7.334  1.00 42.58  ? 588  SER B CB  1 
ATOM   7717 O OG  . SER B 1 493 ? 16.325  46.642  -6.922  1.00 37.71  ? 588  SER B OG  1 
ATOM   7718 N N   . PHE B 1 494 ? 16.306  44.429  -9.357  1.00 39.19  ? 589  PHE B N   1 
ATOM   7719 C CA  . PHE B 1 494 ? 15.745  43.084  -9.419  1.00 40.93  ? 589  PHE B CA  1 
ATOM   7720 C C   . PHE B 1 494 ? 16.262  42.279  -10.606 1.00 42.31  ? 589  PHE B C   1 
ATOM   7721 O O   . PHE B 1 494 ? 15.922  41.097  -10.714 1.00 44.50  ? 589  PHE B O   1 
ATOM   7722 C CB  . PHE B 1 494 ? 14.203  43.134  -9.505  1.00 38.33  ? 589  PHE B CB  1 
ATOM   7723 C CG  . PHE B 1 494 ? 13.539  43.779  -8.307  1.00 39.68  ? 589  PHE B CG  1 
ATOM   7724 C CD1 . PHE B 1 494 ? 12.936  43.001  -7.322  1.00 38.96  ? 589  PHE B CD1 1 
ATOM   7725 C CD2 . PHE B 1 494 ? 13.510  45.164  -8.172  1.00 37.78  ? 589  PHE B CD2 1 
ATOM   7726 C CE1 . PHE B 1 494 ? 12.311  43.605  -6.205  1.00 40.53  ? 589  PHE B CE1 1 
ATOM   7727 C CE2 . PHE B 1 494 ? 12.884  45.776  -7.063  1.00 40.00  ? 589  PHE B CE2 1 
ATOM   7728 C CZ  . PHE B 1 494 ? 12.293  44.994  -6.079  1.00 38.05  ? 589  PHE B CZ  1 
ATOM   7729 N N   . ALA B 1 495 ? 17.053  42.882  -11.500 1.00 39.05  ? 590  ALA B N   1 
ATOM   7730 C CA  . ALA B 1 495 ? 17.393  42.237  -12.765 1.00 45.50  ? 590  ALA B CA  1 
ATOM   7731 C C   . ALA B 1 495 ? 18.536  41.236  -12.652 1.00 43.59  ? 590  ALA B C   1 
ATOM   7732 O O   . ALA B 1 495 ? 18.846  40.576  -13.653 1.00 45.33  ? 590  ALA B O   1 
ATOM   7733 C CB  . ALA B 1 495 ? 17.748  43.282  -13.831 1.00 43.52  ? 590  ALA B CB  1 
ATOM   7734 N N   . TYR B 1 496 ? 19.174  41.118  -11.487 1.00 38.67  ? 591  TYR B N   1 
ATOM   7735 C CA  . TYR B 1 496 ? 20.272  40.174  -11.293 1.00 40.32  ? 591  TYR B CA  1 
ATOM   7736 C C   . TYR B 1 496 ? 19.927  39.247  -10.138 1.00 40.67  ? 591  TYR B C   1 
ATOM   7737 O O   . TYR B 1 496 ? 20.746  39.027  -9.233  1.00 38.62  ? 591  TYR B O   1 
ATOM   7738 C CB  . TYR B 1 496 ? 21.582  40.921  -11.049 1.00 41.65  ? 591  TYR B CB  1 
ATOM   7739 C CG  . TYR B 1 496 ? 21.695  42.170  -11.901 1.00 44.41  ? 591  TYR B CG  1 
ATOM   7740 C CD1 . TYR B 1 496 ? 22.099  42.100  -13.231 1.00 48.15  ? 591  TYR B CD1 1 
ATOM   7741 C CD2 . TYR B 1 496 ? 21.371  43.416  -11.379 1.00 42.22  ? 591  TYR B CD2 1 
ATOM   7742 C CE1 . TYR B 1 496 ? 22.195  43.243  -14.017 1.00 50.05  ? 591  TYR B CE1 1 
ATOM   7743 C CE2 . TYR B 1 496 ? 21.451  44.559  -12.154 1.00 47.57  ? 591  TYR B CE2 1 
ATOM   7744 C CZ  . TYR B 1 496 ? 21.865  44.468  -13.468 1.00 51.62  ? 591  TYR B CZ  1 
ATOM   7745 O OH  . TYR B 1 496 ? 21.945  45.614  -14.220 1.00 51.20  ? 591  TYR B OH  1 
ATOM   7746 N N   . SER B 1 497 ? 18.690  38.728  -10.177 1.00 37.69  ? 592  SER B N   1 
ATOM   7747 C CA  . SER B 1 497 ? 18.069  37.853  -9.185  1.00 39.07  ? 592  SER B CA  1 
ATOM   7748 C C   . SER B 1 497 ? 17.541  38.651  -8.006  1.00 40.18  ? 592  SER B C   1 
ATOM   7749 O O   . SER B 1 497 ? 18.004  39.771  -7.737  1.00 36.32  ? 592  SER B O   1 
ATOM   7750 C CB  . SER B 1 497 ? 19.022  36.768  -8.678  1.00 41.35  ? 592  SER B CB  1 
ATOM   7751 O OG  . SER B 1 497 ? 19.833  37.272  -7.618  1.00 42.61  ? 592  SER B OG  1 
ATOM   7752 N N   . SER B 1 498 ? 16.571  38.064  -7.306  1.00 40.19  ? 593  SER B N   1 
ATOM   7753 C CA  . SER B 1 498 ? 15.916  38.689  -6.168  1.00 40.41  ? 593  SER B CA  1 
ATOM   7754 C C   . SER B 1 498 ? 15.457  37.599  -5.209  1.00 42.18  ? 593  SER B C   1 
ATOM   7755 O O   . SER B 1 498 ? 14.728  36.690  -5.618  1.00 39.88  ? 593  SER B O   1 
ATOM   7756 C CB  . SER B 1 498 ? 14.727  39.530  -6.639  1.00 38.91  ? 593  SER B CB  1 
ATOM   7757 O OG  . SER B 1 498 ? 14.126  40.178  -5.545  1.00 38.53  ? 593  SER B OG  1 
ATOM   7758 N N   . TYR B 1 499 ? 15.905  37.671  -3.954  1.00 37.81  ? 594  TYR B N   1 
ATOM   7759 C CA  . TYR B 1 499 ? 15.428  36.762  -2.935  1.00 38.95  ? 594  TYR B CA  1 
ATOM   7760 C C   . TYR B 1 499 ? 13.952  37.012  -2.668  1.00 39.67  ? 594  TYR B C   1 
ATOM   7761 O O   . TYR B 1 499 ? 13.469  38.139  -2.793  1.00 39.28  ? 594  TYR B O   1 
ATOM   7762 C CB  . TYR B 1 499 ? 16.191  36.945  -1.626  1.00 40.55  ? 594  TYR B CB  1 
ATOM   7763 C CG  . TYR B 1 499 ? 17.682  36.720  -1.719  1.00 43.18  ? 594  TYR B CG  1 
ATOM   7764 C CD1 . TYR B 1 499 ? 18.225  35.454  -1.538  1.00 41.13  ? 594  TYR B CD1 1 
ATOM   7765 C CD2 . TYR B 1 499 ? 18.547  37.785  -1.963  1.00 41.35  ? 594  TYR B CD2 1 
ATOM   7766 C CE1 . TYR B 1 499 ? 19.601  35.246  -1.623  1.00 43.79  ? 594  TYR B CE1 1 
ATOM   7767 C CE2 . TYR B 1 499 ? 19.912  37.591  -2.050  1.00 44.70  ? 594  TYR B CE2 1 
ATOM   7768 C CZ  . TYR B 1 499 ? 20.434  36.320  -1.877  1.00 44.93  ? 594  TYR B CZ  1 
ATOM   7769 O OH  . TYR B 1 499 ? 21.799  36.139  -1.966  1.00 51.75  ? 594  TYR B OH  1 
ATOM   7770 N N   . PRO B 1 500 ? 13.213  35.977  -2.298  1.00 42.42  ? 595  PRO B N   1 
ATOM   7771 C CA  . PRO B 1 500 ? 11.865  36.206  -1.767  1.00 39.77  ? 595  PRO B CA  1 
ATOM   7772 C C   . PRO B 1 500 ? 11.966  37.016  -0.484  1.00 40.42  ? 595  PRO B C   1 
ATOM   7773 O O   . PRO B 1 500 ? 12.758  36.712  0.403   1.00 38.05  ? 595  PRO B O   1 
ATOM   7774 C CB  . PRO B 1 500 ? 11.311  34.792  -1.529  1.00 40.36  ? 595  PRO B CB  1 
ATOM   7775 C CG  . PRO B 1 500 ? 12.445  33.820  -1.789  1.00 41.93  ? 595  PRO B CG  1 
ATOM   7776 C CD  . PRO B 1 500 ? 13.625  34.559  -2.328  1.00 39.86  ? 595  PRO B CD  1 
ATOM   7777 N N   . HIS B 1 501 ? 11.203  38.099  -0.417  1.00 38.49  ? 596  HIS B N   1 
ATOM   7778 C CA  . HIS B 1 501 ? 11.334  38.981  0.727   1.00 38.71  ? 596  HIS B CA  1 
ATOM   7779 C C   . HIS B 1 501 ? 10.001  39.658  1.000   1.00 38.86  ? 596  HIS B C   1 
ATOM   7780 O O   . HIS B 1 501 ? 9.072   39.621  0.189   1.00 37.53  ? 596  HIS B O   1 
ATOM   7781 C CB  . HIS B 1 501 ? 12.472  40.010  0.537   1.00 40.46  ? 596  HIS B CB  1 
ATOM   7782 C CG  . HIS B 1 501 ? 12.311  40.936  -0.640  1.00 39.51  ? 596  HIS B CG  1 
ATOM   7783 N ND1 . HIS B 1 501 ? 12.571  40.548  -1.938  1.00 37.70  ? 596  HIS B ND1 1 
ATOM   7784 C CD2 . HIS B 1 501 ? 11.993  42.255  -0.703  1.00 35.46  ? 596  HIS B CD2 1 
ATOM   7785 C CE1 . HIS B 1 501 ? 12.389  41.575  -2.753  1.00 37.62  ? 596  HIS B CE1 1 
ATOM   7786 N NE2 . HIS B 1 501 ? 12.044  42.624  -2.029  1.00 34.61  ? 596  HIS B NE2 1 
ATOM   7787 N N   . SER B 1 502 ? 9.910   40.223  2.195   1.00 36.81  ? 597  SER B N   1 
ATOM   7788 C CA  . SER B 1 502 ? 8.768   40.998  2.615   1.00 38.31  ? 597  SER B CA  1 
ATOM   7789 C C   . SER B 1 502 ? 9.293   42.147  3.450   1.00 37.79  ? 597  SER B C   1 
ATOM   7790 O O   . SER B 1 502 ? 10.486  42.210  3.774   1.00 36.47  ? 597  SER B O   1 
ATOM   7791 C CB  . SER B 1 502 ? 7.777   40.164  3.439   1.00 37.80  ? 597  SER B CB  1 
ATOM   7792 O OG  . SER B 1 502 ? 8.316   39.957  4.731   1.00 37.10  ? 597  SER B OG  1 
ATOM   7793 N N   . GLY B 1 503 ? 8.385   43.049  3.815   1.00 36.77  ? 598  GLY B N   1 
ATOM   7794 C CA  . GLY B 1 503 ? 8.771   44.109  4.736   1.00 36.13  ? 598  GLY B CA  1 
ATOM   7795 C C   . GLY B 1 503 ? 7.569   44.825  5.322   1.00 39.31  ? 598  GLY B C   1 
ATOM   7796 O O   . GLY B 1 503 ? 6.410   44.474  5.058   1.00 36.97  ? 598  GLY B O   1 
ATOM   7797 N N   . CYS B 1 504 ? 7.872   45.856  6.117   1.00 37.99  ? 599  CYS B N   1 
ATOM   7798 C CA  . CYS B 1 504 ? 6.827   46.627  6.784   1.00 39.00  ? 599  CYS B CA  1 
ATOM   7799 C C   . CYS B 1 504 ? 7.344   47.992  7.226   1.00 40.78  ? 599  CYS B C   1 
ATOM   7800 O O   . CYS B 1 504 ? 8.546   48.214  7.422   1.00 39.01  ? 599  CYS B O   1 
ATOM   7801 C CB  . CYS B 1 504 ? 6.250   45.874  7.987   1.00 37.63  ? 599  CYS B CB  1 
ATOM   7802 S SG  . CYS B 1 504 ? 7.453   45.472  9.260   1.00 42.55  ? 599  CYS B SG  1 
ATOM   7803 N N   . GLY B 1 505 ? 6.392   48.897  7.363   1.00 37.04  ? 600  GLY B N   1 
ATOM   7804 C CA  . GLY B 1 505 ? 6.662   50.237  7.849   1.00 38.86  ? 600  GLY B CA  1 
ATOM   7805 C C   . GLY B 1 505 ? 5.744   50.546  9.013   1.00 40.66  ? 600  GLY B C   1 
ATOM   7806 O O   . GLY B 1 505 ? 4.574   50.136  9.027   1.00 35.84  ? 600  GLY B O   1 
ATOM   7807 N N   . ILE B 1 506 ? 6.297   51.253  10.005  1.00 38.23  ? 601  ILE B N   1 
ATOM   7808 C CA  . ILE B 1 506 ? 5.671   51.443  11.313  1.00 38.41  ? 601  ILE B CA  1 
ATOM   7809 C C   . ILE B 1 506 ? 5.861   52.885  11.736  1.00 39.68  ? 601  ILE B C   1 
ATOM   7810 O O   . ILE B 1 506 ? 6.987   53.392  11.748  1.00 37.83  ? 601  ILE B O   1 
ATOM   7811 C CB  . ILE B 1 506 ? 6.293   50.537  12.392  1.00 36.29  ? 601  ILE B CB  1 
ATOM   7812 C CG1 . ILE B 1 506 ? 6.057   49.051  12.094  1.00 38.11  ? 601  ILE B CG1 1 
ATOM   7813 C CG2 . ILE B 1 506 ? 5.755   50.954  13.783  1.00 42.08  ? 601  ILE B CG2 1 
ATOM   7814 C CD1 . ILE B 1 506 ? 7.269   48.224  12.548  1.00 37.38  ? 601  ILE B CD1 1 
ATOM   7815 N N   . GLY B 1 507 ? 4.783   53.526  12.137  1.00 38.54  ? 602  GLY B N   1 
ATOM   7816 C CA  . GLY B 1 507 ? 5.031   54.866  12.667  1.00 38.54  ? 602  GLY B CA  1 
ATOM   7817 C C   . GLY B 1 507 ? 5.381   54.915  14.161  1.00 40.88  ? 602  GLY B C   1 
ATOM   7818 O O   . GLY B 1 507 ? 4.593   54.459  14.989  1.00 38.56  ? 602  GLY B O   1 
ATOM   7819 N N   . LEU B 1 508 ? 6.524   55.491  14.548  1.00 39.96  ? 603  LEU B N   1 
ATOM   7820 C CA  . LEU B 1 508 ? 6.948   55.436  15.954  1.00 40.96  ? 603  LEU B CA  1 
ATOM   7821 C C   . LEU B 1 508 ? 5.997   56.212  16.866  1.00 41.84  ? 603  LEU B C   1 
ATOM   7822 O O   . LEU B 1 508 ? 5.484   55.685  17.877  1.00 41.12  ? 603  LEU B O   1 
ATOM   7823 C CB  . LEU B 1 508 ? 8.382   55.972  16.083  1.00 38.83  ? 603  LEU B CB  1 
ATOM   7824 C CG  . LEU B 1 508 ? 8.873   56.318  17.497  1.00 42.30  ? 603  LEU B CG  1 
ATOM   7825 C CD1 . LEU B 1 508 ? 8.983   55.069  18.393  1.00 40.17  ? 603  LEU B CD1 1 
ATOM   7826 C CD2 . LEU B 1 508 ? 10.224  57.050  17.435  1.00 36.37  ? 603  LEU B CD2 1 
ATOM   7827 N N   . GLU B 1 509 ? 5.771   57.484  16.534  1.00 39.48  ? 604  GLU B N   1 
ATOM   7828 C CA  . GLU B 1 509 ? 4.926   58.321  17.372  1.00 40.26  ? 604  GLU B CA  1 
ATOM   7829 C C   . GLU B 1 509 ? 3.526   57.731  17.513  1.00 41.40  ? 604  GLU B C   1 
ATOM   7830 O O   . GLU B 1 509 ? 2.901   57.845  18.576  1.00 38.00  ? 604  GLU B O   1 
ATOM   7831 C CB  . GLU B 1 509 ? 4.864   59.737  16.788  1.00 39.78  ? 604  GLU B CB  1 
ATOM   7832 C CG  . GLU B 1 509 ? 6.228   60.443  16.673  1.00 40.83  ? 604  GLU B CG  1 
ATOM   7833 C CD  . GLU B 1 509 ? 6.914   60.168  15.326  1.00 43.07  ? 604  GLU B CD  1 
ATOM   7834 O OE1 . GLU B 1 509 ? 7.812   60.965  14.930  1.00 41.94  ? 604  GLU B OE1 1 
ATOM   7835 O OE2 . GLU B 1 509 ? 6.543   59.171  14.646  1.00 41.70  ? 604  GLU B OE2 1 
ATOM   7836 N N   . ARG B 1 510 ? 3.031   57.068  16.468  1.00 41.44  ? 605  ARG B N   1 
ATOM   7837 C CA  . ARG B 1 510 ? 1.681   56.525  16.500  1.00 41.07  ? 605  ARG B CA  1 
ATOM   7838 C C   . ARG B 1 510 ? 1.587   55.263  17.354  1.00 41.74  ? 605  ARG B C   1 
ATOM   7839 O O   . ARG B 1 510 ? 0.568   55.045  18.024  1.00 42.95  ? 605  ARG B O   1 
ATOM   7840 C CB  . ARG B 1 510 ? 1.200   56.241  15.075  1.00 46.06  ? 605  ARG B CB  1 
ATOM   7841 C CG  . ARG B 1 510 ? -0.301  55.938  15.040  1.00 54.85  ? 605  ARG B CG  1 
ATOM   7842 C CD  . ARG B 1 510 ? -0.797  55.736  13.617  1.00 61.47  ? 605  ARG B CD  1 
ATOM   7843 N NE  . ARG B 1 510 ? -0.883  57.010  12.918  1.00 69.52  ? 605  ARG B NE  1 
ATOM   7844 C CZ  . ARG B 1 510 ? -1.223  57.143  11.643  1.00 70.83  ? 605  ARG B CZ  1 
ATOM   7845 N NH1 . ARG B 1 510 ? -1.192  58.322  11.038  1.00 72.55  ? 605  ARG B NH1 1 
ATOM   7846 N NH2 . ARG B 1 510 ? -1.604  56.066  10.958  1.00 68.95  ? 605  ARG B NH2 1 
ATOM   7847 N N   . VAL B 1 511 ? 2.621   54.420  17.332  1.00 41.96  ? 606  VAL B N   1 
ATOM   7848 C CA  . VAL B 1 511 ? 2.662   53.283  18.246  1.00 42.04  ? 606  VAL B CA  1 
ATOM   7849 C C   . VAL B 1 511 ? 2.591   53.768  19.680  1.00 41.10  ? 606  VAL B C   1 
ATOM   7850 O O   . VAL B 1 511 ? 1.835   53.232  20.496  1.00 41.46  ? 606  VAL B O   1 
ATOM   7851 C CB  . VAL B 1 511 ? 3.925   52.437  18.021  1.00 40.61  ? 606  VAL B CB  1 
ATOM   7852 C CG1 . VAL B 1 511 ? 4.050   51.433  19.148  1.00 37.46  ? 606  VAL B CG1 1 
ATOM   7853 C CG2 . VAL B 1 511 ? 3.841   51.726  16.699  1.00 43.75  ? 606  VAL B CG2 1 
ATOM   7854 N N   . LEU B 1 512 ? 3.396   54.782  20.017  1.00 41.70  ? 607  LEU B N   1 
ATOM   7855 C CA  . LEU B 1 512 ? 3.381   55.271  21.395  1.00 39.43  ? 607  LEU B CA  1 
ATOM   7856 C C   . LEU B 1 512 ? 2.016   55.850  21.757  1.00 41.47  ? 607  LEU B C   1 
ATOM   7857 O O   . LEU B 1 512 ? 1.466   55.569  22.842  1.00 42.14  ? 607  LEU B O   1 
ATOM   7858 C CB  . LEU B 1 512 ? 4.497   56.305  21.583  1.00 40.43  ? 607  LEU B CB  1 
ATOM   7859 C CG  . LEU B 1 512 ? 4.650   56.861  22.996  1.00 42.84  ? 607  LEU B CG  1 
ATOM   7860 C CD1 . LEU B 1 512 ? 4.802   55.726  24.016  1.00 36.13  ? 607  LEU B CD1 1 
ATOM   7861 C CD2 . LEU B 1 512 ? 5.811   57.841  23.050  1.00 37.91  ? 607  LEU B CD2 1 
ATOM   7862 N N   . MET B 1 513 ? 1.439   56.639  20.843  1.00 39.76  ? 608  MET B N   1 
ATOM   7863 C CA  . MET B 1 513 ? 0.135   57.238  21.085  1.00 42.17  ? 608  MET B CA  1 
ATOM   7864 C C   . MET B 1 513 ? -0.937  56.179  21.340  1.00 42.49  ? 608  MET B C   1 
ATOM   7865 O O   . MET B 1 513 ? -1.730  56.297  22.278  1.00 45.22  ? 608  MET B O   1 
ATOM   7866 C CB  . MET B 1 513 ? -0.236  58.114  19.890  1.00 40.02  ? 608  MET B CB  1 
ATOM   7867 C CG  . MET B 1 513 ? -1.646  58.617  19.879  1.00 45.43  ? 608  MET B CG  1 
ATOM   7868 S SD  . MET B 1 513 ? -2.039  59.289  18.249  1.00 50.03  ? 608  MET B SD  1 
ATOM   7869 C CE  . MET B 1 513 ? -3.765  59.677  18.434  1.00 52.67  ? 608  MET B CE  1 
ATOM   7870 N N   . LEU B 1 514 ? -0.989  55.141  20.506  1.00 41.81  ? 609  LEU B N   1 
ATOM   7871 C CA  . LEU B 1 514 ? -2.013  54.117  20.683  1.00 42.50  ? 609  LEU B CA  1 
ATOM   7872 C C   . LEU B 1 514 ? -1.734  53.235  21.903  1.00 44.91  ? 609  LEU B C   1 
ATOM   7873 O O   . LEU B 1 514 ? -2.677  52.825  22.588  1.00 42.31  ? 609  LEU B O   1 
ATOM   7874 C CB  . LEU B 1 514 ? -2.130  53.290  19.393  1.00 42.48  ? 609  LEU B CB  1 
ATOM   7875 C CG  . LEU B 1 514 ? -2.651  54.144  18.214  1.00 45.07  ? 609  LEU B CG  1 
ATOM   7876 C CD1 . LEU B 1 514 ? -2.390  53.482  16.902  1.00 42.10  ? 609  LEU B CD1 1 
ATOM   7877 C CD2 . LEU B 1 514 ? -4.160  54.451  18.373  1.00 43.67  ? 609  LEU B CD2 1 
ATOM   7878 N N   . PHE B 1 515 ? -0.460  52.945  22.206  1.00 41.78  ? 610  PHE B N   1 
ATOM   7879 C CA  . PHE B 1 515 ? -0.159  52.184  23.416  1.00 44.60  ? 610  PHE B CA  1 
ATOM   7880 C C   . PHE B 1 515 ? -0.712  52.884  24.644  1.00 42.78  ? 610  PHE B C   1 
ATOM   7881 O O   . PHE B 1 515 ? -1.382  52.263  25.477  1.00 42.49  ? 610  PHE B O   1 
ATOM   7882 C CB  . PHE B 1 515 ? 1.352   51.965  23.588  1.00 39.04  ? 610  PHE B CB  1 
ATOM   7883 C CG  . PHE B 1 515 ? 1.687   51.055  24.748  1.00 42.32  ? 610  PHE B CG  1 
ATOM   7884 C CD1 . PHE B 1 515 ? 1.674   49.671  24.588  1.00 43.52  ? 610  PHE B CD1 1 
ATOM   7885 C CD2 . PHE B 1 515 ? 1.986   51.565  25.995  1.00 43.22  ? 610  PHE B CD2 1 
ATOM   7886 C CE1 . PHE B 1 515 ? 1.958   48.825  25.649  1.00 40.68  ? 610  PHE B CE1 1 
ATOM   7887 C CE2 . PHE B 1 515 ? 2.271   50.711  27.067  1.00 43.55  ? 610  PHE B CE2 1 
ATOM   7888 C CZ  . PHE B 1 515 ? 2.254   49.345  26.884  1.00 40.85  ? 610  PHE B CZ  1 
ATOM   7889 N N   . LEU B 1 516 ? -0.442  54.186  24.773  1.00 42.70  ? 611  LEU B N   1 
ATOM   7890 C CA  . LEU B 1 516 ? -0.925  54.931  25.935  1.00 44.28  ? 611  LEU B CA  1 
ATOM   7891 C C   . LEU B 1 516 ? -2.367  55.409  25.786  1.00 46.99  ? 611  LEU B C   1 
ATOM   7892 O O   . LEU B 1 516 ? -2.940  55.927  26.758  1.00 44.77  ? 611  LEU B O   1 
ATOM   7893 C CB  . LEU B 1 516 ? -0.004  56.128  26.203  1.00 43.00  ? 611  LEU B CB  1 
ATOM   7894 C CG  . LEU B 1 516 ? 1.469   55.773  26.489  1.00 44.26  ? 611  LEU B CG  1 
ATOM   7895 C CD1 . LEU B 1 516 ? 2.365   56.996  26.424  1.00 40.50  ? 611  LEU B CD1 1 
ATOM   7896 C CD2 . LEU B 1 516 ? 1.551   55.149  27.876  1.00 43.82  ? 611  LEU B CD2 1 
ATOM   7897 N N   . GLY B 1 517 ? -2.968  55.264  24.606  1.00 45.58  ? 612  GLY B N   1 
ATOM   7898 C CA  . GLY B 1 517 ? -4.325  55.766  24.424  1.00 46.00  ? 612  GLY B CA  1 
ATOM   7899 C C   . GLY B 1 517 ? -4.437  57.278  24.387  1.00 48.77  ? 612  GLY B C   1 
ATOM   7900 O O   . GLY B 1 517 ? -5.505  57.818  24.690  1.00 46.59  ? 612  GLY B O   1 
ATOM   7901 N N   . LEU B 1 518 ? -3.362  57.982  24.028  1.00 42.91  ? 613  LEU B N   1 
ATOM   7902 C CA  . LEU B 1 518 ? -3.416  59.441  23.996  1.00 48.75  ? 613  LEU B CA  1 
ATOM   7903 C C   . LEU B 1 518 ? -4.289  59.928  22.830  1.00 48.80  ? 613  LEU B C   1 
ATOM   7904 O O   . LEU B 1 518 ? -4.466  59.248  21.814  1.00 46.26  ? 613  LEU B O   1 
ATOM   7905 C CB  . LEU B 1 518 ? -1.997  60.022  23.901  1.00 45.60  ? 613  LEU B CB  1 
ATOM   7906 C CG  . LEU B 1 518 ? -1.099  59.691  25.102  1.00 45.05  ? 613  LEU B CG  1 
ATOM   7907 C CD1 . LEU B 1 518 ? 0.371   59.919  24.812  1.00 43.43  ? 613  LEU B CD1 1 
ATOM   7908 C CD2 . LEU B 1 518 ? -1.526  60.461  26.351  1.00 45.42  ? 613  LEU B CD2 1 
ATOM   7909 N N   . ASN B 1 519 ? -4.821  61.140  22.980  1.00 45.34  ? 614  ASN B N   1 
ATOM   7910 C CA  . ASN B 1 519 ? -5.845  61.637  22.077  1.00 49.71  ? 614  ASN B CA  1 
ATOM   7911 C C   . ASN B 1 519 ? -5.297  62.332  20.834  1.00 49.70  ? 614  ASN B C   1 
ATOM   7912 O O   . ASN B 1 519 ? -6.094  62.697  19.960  1.00 54.55  ? 614  ASN B O   1 
ATOM   7913 C CB  . ASN B 1 519 ? -6.793  62.599  22.832  1.00 47.01  ? 614  ASN B CB  1 
ATOM   7914 C CG  . ASN B 1 519 ? -6.173  63.984  23.087  1.00 52.83  ? 614  ASN B CG  1 
ATOM   7915 O OD1 . ASN B 1 519 ? -4.955  64.178  22.984  1.00 50.74  ? 614  ASN B OD1 1 
ATOM   7916 N ND2 . ASN B 1 519 ? -7.020  64.953  23.432  1.00 54.23  ? 614  ASN B ND2 1 
ATOM   7917 N N   . ASN B 1 520 ? -3.982  62.543  20.731  1.00 48.24  ? 615  ASN B N   1 
ATOM   7918 C CA  . ASN B 1 520 ? -3.449  63.375  19.655  1.00 47.85  ? 615  ASN B CA  1 
ATOM   7919 C C   . ASN B 1 520 ? -1.985  63.033  19.424  1.00 47.38  ? 615  ASN B C   1 
ATOM   7920 O O   . ASN B 1 520 ? -1.201  62.956  20.378  1.00 44.98  ? 615  ASN B O   1 
ATOM   7921 C CB  . ASN B 1 520 ? -3.613  64.869  19.986  1.00 47.74  ? 615  ASN B CB  1 
ATOM   7922 C CG  . ASN B 1 520 ? -3.389  65.774  18.775  1.00 50.80  ? 615  ASN B CG  1 
ATOM   7923 O OD1 . ASN B 1 520 ? -2.299  65.815  18.216  1.00 49.47  ? 615  ASN B OD1 1 
ATOM   7924 N ND2 . ASN B 1 520 ? -4.425  66.511  18.377  1.00 51.68  ? 615  ASN B ND2 1 
ATOM   7925 N N   . ILE B 1 521 ? -1.624  62.845  18.150  1.00 45.25  ? 616  ILE B N   1 
ATOM   7926 C CA  . ILE B 1 521 ? -0.264  62.485  17.778  1.00 47.28  ? 616  ILE B CA  1 
ATOM   7927 C C   . ILE B 1 521 ? 0.738   63.555  18.185  1.00 46.75  ? 616  ILE B C   1 
ATOM   7928 O O   . ILE B 1 521 ? 1.931   63.258  18.345  1.00 44.44  ? 616  ILE B O   1 
ATOM   7929 C CB  . ILE B 1 521 ? -0.197  62.208  16.259  1.00 49.60  ? 616  ILE B CB  1 
ATOM   7930 C CG1 . ILE B 1 521 ? 1.148   61.602  15.867  1.00 48.69  ? 616  ILE B CG1 1 
ATOM   7931 C CG2 . ILE B 1 521 ? -0.437  63.469  15.462  1.00 45.21  ? 616  ILE B CG2 1 
ATOM   7932 C CD1 . ILE B 1 521 ? 1.277   60.202  16.259  1.00 46.97  ? 616  ILE B CD1 1 
ATOM   7933 N N   . ARG B 1 522 ? 0.288   64.803  18.352  1.00 43.81  ? 617  ARG B N   1 
ATOM   7934 C CA  . ARG B 1 522 ? 1.199   65.845  18.807  1.00 46.49  ? 617  ARG B CA  1 
ATOM   7935 C C   . ARG B 1 522 ? 1.684   65.625  20.233  1.00 42.77  ? 617  ARG B C   1 
ATOM   7936 O O   . ARG B 1 522 ? 2.624   66.296  20.664  1.00 40.66  ? 617  ARG B O   1 
ATOM   7937 C CB  . ARG B 1 522 ? 0.526   67.208  18.673  1.00 46.21  ? 617  ARG B CB  1 
ATOM   7938 C CG  . ARG B 1 522 ? 0.284   67.574  17.217  1.00 48.02  ? 617  ARG B CG  1 
ATOM   7939 C CD  . ARG B 1 522 ? -0.828  68.595  17.057  1.00 50.46  ? 617  ARG B CD  1 
ATOM   7940 N NE  . ARG B 1 522 ? -1.140  68.780  15.650  1.00 47.52  ? 617  ARG B NE  1 
ATOM   7941 C CZ  . ARG B 1 522 ? -1.912  67.964  14.946  1.00 51.54  ? 617  ARG B CZ  1 
ATOM   7942 N NH1 . ARG B 1 522 ? -2.469  66.894  15.492  1.00 50.37  ? 617  ARG B NH1 1 
ATOM   7943 N NH2 . ARG B 1 522 ? -2.145  68.235  13.664  1.00 49.71  ? 617  ARG B NH2 1 
ATOM   7944 N N   . LYS B 1 523 ? 1.085   64.702  20.974  1.00 43.47  ? 618  LYS B N   1 
ATOM   7945 C CA  . LYS B 1 523 ? 1.595   64.415  22.307  1.00 43.61  ? 618  LYS B CA  1 
ATOM   7946 C C   . LYS B 1 523 ? 2.814   63.499  22.286  1.00 43.41  ? 618  LYS B C   1 
ATOM   7947 O O   . LYS B 1 523 ? 3.542   63.445  23.280  1.00 42.83  ? 618  LYS B O   1 
ATOM   7948 C CB  . LYS B 1 523 ? 0.478   63.819  23.165  1.00 42.34  ? 618  LYS B CB  1 
ATOM   7949 C CG  . LYS B 1 523 ? -0.533  64.897  23.665  1.00 41.12  ? 618  LYS B CG  1 
ATOM   7950 C CD  . LYS B 1 523 ? -1.630  64.298  24.545  1.00 47.65  ? 618  LYS B CD  1 
ATOM   7951 C CE  . LYS B 1 523 ? -2.532  65.397  25.188  1.00 46.94  ? 618  LYS B CE  1 
ATOM   7952 N NZ  . LYS B 1 523 ? -3.173  66.247  24.133  1.00 43.01  ? 618  LYS B NZ  1 
ATOM   7953 N N   . THR B 1 524 ? 3.069   62.798  21.178  1.00 39.91  ? 619  THR B N   1 
ATOM   7954 C CA  . THR B 1 524 ? 4.153   61.823  21.104  1.00 41.78  ? 619  THR B CA  1 
ATOM   7955 C C   . THR B 1 524 ? 5.223   62.178  20.066  1.00 39.87  ? 619  THR B C   1 
ATOM   7956 O O   . THR B 1 524 ? 6.063   61.338  19.741  1.00 37.46  ? 619  THR B O   1 
ATOM   7957 C CB  . THR B 1 524 ? 3.571   60.437  20.828  1.00 40.70  ? 619  THR B CB  1 
ATOM   7958 O OG1 . THR B 1 524 ? 2.805   60.478  19.616  1.00 38.60  ? 619  THR B OG1 1 
ATOM   7959 C CG2 . THR B 1 524 ? 2.651   60.009  22.000  1.00 41.52  ? 619  THR B CG2 1 
ATOM   7960 N N   . SER B 1 525 ? 5.222   63.406  19.559  1.00 42.98  ? 620  SER B N   1 
ATOM   7961 C CA  . SER B 1 525 ? 6.279   63.956  18.712  1.00 41.63  ? 620  SER B CA  1 
ATOM   7962 C C   . SER B 1 525 ? 6.856   65.170  19.436  1.00 41.17  ? 620  SER B C   1 
ATOM   7963 O O   . SER B 1 525 ? 6.093   66.024  19.893  1.00 41.63  ? 620  SER B O   1 
ATOM   7964 C CB  . SER B 1 525 ? 5.713   64.360  17.336  1.00 40.13  ? 620  SER B CB  1 
ATOM   7965 O OG  . SER B 1 525 ? 6.714   64.908  16.474  1.00 43.62  ? 620  SER B OG  1 
ATOM   7966 N N   . LEU B 1 526 ? 8.192   65.239  19.563  1.00 40.06  ? 621  LEU B N   1 
ATOM   7967 C CA  . LEU B 1 526 ? 8.810   66.270  20.413  1.00 44.66  ? 621  LEU B CA  1 
ATOM   7968 C C   . LEU B 1 526 ? 8.476   67.675  19.933  1.00 42.53  ? 621  LEU B C   1 
ATOM   7969 O O   . LEU B 1 526 ? 8.032   68.524  20.717  1.00 47.29  ? 621  LEU B O   1 
ATOM   7970 C CB  . LEU B 1 526 ? 10.334  66.097  20.462  1.00 43.11  ? 621  LEU B CB  1 
ATOM   7971 C CG  . LEU B 1 526 ? 10.990  65.257  21.562  1.00 43.48  ? 621  LEU B CG  1 
ATOM   7972 C CD1 . LEU B 1 526 ? 12.502  65.268  21.358  1.00 42.54  ? 621  LEU B CD1 1 
ATOM   7973 C CD2 . LEU B 1 526 ? 10.638  65.765  22.944  1.00 40.73  ? 621  LEU B CD2 1 
ATOM   7974 N N   . PHE B 1 527 ? 8.706   67.954  18.653  1.00 41.66  ? 622  PHE B N   1 
ATOM   7975 C CA  . PHE B 1 527 ? 8.421   69.269  18.072  1.00 46.32  ? 622  PHE B CA  1 
ATOM   7976 C C   . PHE B 1 527 ? 7.562   69.038  16.838  1.00 45.40  ? 622  PHE B C   1 
ATOM   7977 O O   . PHE B 1 527 ? 8.077   68.906  15.720  1.00 45.39  ? 622  PHE B O   1 
ATOM   7978 C CB  . PHE B 1 527 ? 9.719   70.023  17.776  1.00 43.46  ? 622  PHE B CB  1 
ATOM   7979 C CG  . PHE B 1 527 ? 10.577  70.223  18.999  1.00 43.43  ? 622  PHE B CG  1 
ATOM   7980 C CD1 . PHE B 1 527 ? 10.260  71.208  19.935  1.00 47.12  ? 622  PHE B CD1 1 
ATOM   7981 C CD2 . PHE B 1 527 ? 11.681  69.408  19.237  1.00 42.82  ? 622  PHE B CD2 1 
ATOM   7982 C CE1 . PHE B 1 527 ? 11.041  71.395  21.085  1.00 43.56  ? 622  PHE B CE1 1 
ATOM   7983 C CE2 . PHE B 1 527 ? 12.466  69.583  20.381  1.00 41.75  ? 622  PHE B CE2 1 
ATOM   7984 C CZ  . PHE B 1 527 ? 12.145  70.575  21.305  1.00 46.23  ? 622  PHE B CZ  1 
ATOM   7985 N N   . PRO B 1 528 ? 6.244   68.920  17.019  1.00 42.28  ? 623  PRO B N   1 
ATOM   7986 C CA  . PRO B 1 528 ? 5.395   68.389  15.947  1.00 42.70  ? 623  PRO B CA  1 
ATOM   7987 C C   . PRO B 1 528 ? 5.421   69.267  14.705  1.00 48.13  ? 623  PRO B C   1 
ATOM   7988 O O   . PRO B 1 528 ? 5.543   70.493  14.784  1.00 45.33  ? 623  PRO B O   1 
ATOM   7989 C CB  . PRO B 1 528 ? 3.999   68.358  16.585  1.00 45.67  ? 623  PRO B CB  1 
ATOM   7990 C CG  . PRO B 1 528 ? 4.266   68.236  18.084  1.00 43.77  ? 623  PRO B CG  1 
ATOM   7991 C CD  . PRO B 1 528 ? 5.535   69.013  18.312  1.00 45.10  ? 623  PRO B CD  1 
ATOM   7992 N N   . ARG B 1 529 ? 5.303   68.612  13.548  1.00 44.64  ? 624  ARG B N   1 
ATOM   7993 C CA  . ARG B 1 529 ? 5.190   69.261  12.248  1.00 45.39  ? 624  ARG B CA  1 
ATOM   7994 C C   . ARG B 1 529 ? 3.845   68.898  11.644  1.00 47.98  ? 624  ARG B C   1 
ATOM   7995 O O   . ARG B 1 529 ? 3.583   67.718  11.393  1.00 48.42  ? 624  ARG B O   1 
ATOM   7996 C CB  . ARG B 1 529 ? 6.302   68.802  11.302  1.00 47.40  ? 624  ARG B CB  1 
ATOM   7997 C CG  . ARG B 1 529 ? 7.656   69.354  11.609  1.00 50.12  ? 624  ARG B CG  1 
ATOM   7998 C CD  . ARG B 1 529 ? 7.735   70.841  11.298  1.00 45.70  ? 624  ARG B CD  1 
ATOM   7999 N NE  . ARG B 1 529 ? 9.004   71.380  11.764  1.00 46.18  ? 624  ARG B NE  1 
ATOM   8000 C CZ  . ARG B 1 529 ? 9.183   71.951  12.944  1.00 49.58  ? 624  ARG B CZ  1 
ATOM   8001 N NH1 . ARG B 1 529 ? 8.176   72.120  13.793  1.00 50.02  ? 624  ARG B NH1 1 
ATOM   8002 N NH2 . ARG B 1 529 ? 10.399  72.377  13.278  1.00 46.93  ? 624  ARG B NH2 1 
ATOM   8003 N N   . ASP B 1 530 ? 2.999   69.902  11.396  1.00 50.81  ? 625  ASP B N   1 
ATOM   8004 C CA  . ASP B 1 530 ? 1.753   69.651  10.673  1.00 48.89  ? 625  ASP B CA  1 
ATOM   8005 C C   . ASP B 1 530 ? 1.522   70.818  9.714   1.00 48.53  ? 625  ASP B C   1 
ATOM   8006 O O   . ASP B 1 530 ? 2.284   71.790  9.766   1.00 47.64  ? 625  ASP B O   1 
ATOM   8007 C CB  . ASP B 1 530 ? 0.595   69.438  11.659  1.00 51.29  ? 625  ASP B CB  1 
ATOM   8008 C CG  . ASP B 1 530 ? 0.314   70.662  12.523  1.00 55.85  ? 625  ASP B CG  1 
ATOM   8009 O OD1 . ASP B 1 530 ? 0.063   71.745  11.960  1.00 51.41  ? 625  ASP B OD1 1 
ATOM   8010 O OD2 . ASP B 1 530 ? 0.326   70.531  13.770  1.00 56.89  ? 625  ASP B OD2 1 
ATOM   8011 N N   . PRO B 1 531 ? 0.510   70.783  8.835   1.00 49.20  ? 626  PRO B N   1 
ATOM   8012 C CA  . PRO B 1 531 ? 0.391   71.848  7.823   1.00 53.29  ? 626  PRO B CA  1 
ATOM   8013 C C   . PRO B 1 531 ? 0.322   73.260  8.386   1.00 55.08  ? 626  PRO B C   1 
ATOM   8014 O O   . PRO B 1 531 ? 0.567   74.215  7.640   1.00 56.05  ? 626  PRO B O   1 
ATOM   8015 C CB  . PRO B 1 531 ? -0.900  71.481  7.083   1.00 55.68  ? 626  PRO B CB  1 
ATOM   8016 C CG  . PRO B 1 531 ? -0.985  69.998  7.232   1.00 56.68  ? 626  PRO B CG  1 
ATOM   8017 C CD  . PRO B 1 531 ? -0.487  69.718  8.603   1.00 53.37  ? 626  PRO B CD  1 
ATOM   8018 N N   . LYS B 1 532 ? 0.023   73.430  9.672   1.00 52.55  ? 627  LYS B N   1 
ATOM   8019 C CA  . LYS B 1 532 ? -0.092  74.755  10.264  1.00 57.64  ? 627  LYS B CA  1 
ATOM   8020 C C   . LYS B 1 532 ? 0.992   75.034  11.294  1.00 54.10  ? 627  LYS B C   1 
ATOM   8021 O O   . LYS B 1 532 ? 0.909   76.033  12.010  1.00 56.88  ? 627  LYS B O   1 
ATOM   8022 C CB  . LYS B 1 532 ? -1.477  74.928  10.891  1.00 54.09  ? 627  LYS B CB  1 
ATOM   8023 C CG  . LYS B 1 532 ? -2.563  75.218  9.878   1.00 58.59  ? 627  LYS B CG  1 
ATOM   8024 C CD  . LYS B 1 532 ? -2.712  76.735  9.687   1.00 65.40  ? 627  LYS B CD  1 
ATOM   8025 C CE  . LYS B 1 532 ? -3.389  77.095  8.372   1.00 62.82  ? 627  LYS B CE  1 
ATOM   8026 N NZ  . LYS B 1 532 ? -3.601  78.566  8.251   1.00 65.84  ? 627  LYS B NZ  1 
ATOM   8027 N N   . ARG B 1 533 ? 1.995   74.175  11.405  1.00 51.30  ? 628  ARG B N   1 
ATOM   8028 C CA  . ARG B 1 533 ? 3.017   74.350  12.430  1.00 52.41  ? 628  ARG B CA  1 
ATOM   8029 C C   . ARG B 1 533 ? 4.377   73.960  11.868  1.00 54.04  ? 628  ARG B C   1 
ATOM   8030 O O   . ARG B 1 533 ? 4.635   72.780  11.605  1.00 50.38  ? 628  ARG B O   1 
ATOM   8031 C CB  . ARG B 1 533 ? 2.698   73.533  13.680  1.00 51.40  ? 628  ARG B CB  1 
ATOM   8032 C CG  . ARG B 1 533 ? 3.754   73.673  14.761  1.00 50.61  ? 628  ARG B CG  1 
ATOM   8033 C CD  . ARG B 1 533 ? 3.291   73.040  16.071  1.00 56.04  ? 628  ARG B CD  1 
ATOM   8034 N NE  . ARG B 1 533 ? 2.193   73.776  16.687  1.00 54.25  ? 628  ARG B NE  1 
ATOM   8035 C CZ  . ARG B 1 533 ? 2.342   74.890  17.393  1.00 54.73  ? 628  ARG B CZ  1 
ATOM   8036 N NH1 . ARG B 1 533 ? 3.533   75.433  17.589  1.00 53.70  ? 628  ARG B NH1 1 
ATOM   8037 N NH2 . ARG B 1 533 ? 1.268   75.472  17.917  1.00 56.76  ? 628  ARG B NH2 1 
ATOM   8038 N N   . LEU B 1 534 ? 5.247   74.954  11.731  1.00 51.89  ? 629  LEU B N   1 
ATOM   8039 C CA  . LEU B 1 534 ? 6.633   74.778  11.338  1.00 53.82  ? 629  LEU B CA  1 
ATOM   8040 C C   . LEU B 1 534 ? 7.595   75.205  12.437  1.00 54.88  ? 629  LEU B C   1 
ATOM   8041 O O   . LEU B 1 534 ? 8.804   74.982  12.306  1.00 50.34  ? 629  LEU B O   1 
ATOM   8042 C CB  . LEU B 1 534 ? 6.916   75.586  10.055  1.00 51.40  ? 629  LEU B CB  1 
ATOM   8043 C CG  . LEU B 1 534 ? 8.232   75.420  9.292   1.00 54.40  ? 629  LEU B CG  1 
ATOM   8044 C CD1 . LEU B 1 534 ? 8.505   73.947  8.963   1.00 50.26  ? 629  LEU B CD1 1 
ATOM   8045 C CD2 . LEU B 1 534 ? 8.202   76.282  8.022   1.00 58.15  ? 629  LEU B CD2 1 
ATOM   8046 N N   . ILE B 1 535 ? 7.086   75.788  13.518  1.00 54.18  ? 630  ILE B N   1 
ATOM   8047 C CA  . ILE B 1 535 ? 7.865   76.386  14.601  1.00 55.53  ? 630  ILE B CA  1 
ATOM   8048 C C   . ILE B 1 535 ? 7.288   75.884  15.922  1.00 56.45  ? 630  ILE B C   1 
ATOM   8049 O O   . ILE B 1 535 ? 6.064   75.747  16.037  1.00 58.34  ? 630  ILE B O   1 
ATOM   8050 C CB  . ILE B 1 535 ? 7.821   77.924  14.532  1.00 57.36  ? 630  ILE B CB  1 
ATOM   8051 C CG1 . ILE B 1 535 ? 8.357   78.440  13.200  1.00 61.81  ? 630  ILE B CG1 1 
ATOM   8052 C CG2 . ILE B 1 535 ? 8.626   78.553  15.667  1.00 62.56  ? 630  ILE B CG2 1 
ATOM   8053 C CD1 . ILE B 1 535 ? 9.881   78.482  13.137  1.00 66.77  ? 630  ILE B CD1 1 
ATOM   8054 N N   . PRO B 1 536 ? 8.102   75.566  16.936  1.00 55.58  ? 631  PRO B N   1 
ATOM   8055 C CA  . PRO B 1 536 ? 9.559   75.468  16.933  1.00 54.27  ? 631  PRO B CA  1 
ATOM   8056 C C   . PRO B 1 536 ? 10.024  74.399  15.970  1.00 56.63  ? 631  PRO B C   1 
ATOM   8057 O O   . PRO B 1 536 ? 9.275   73.456  15.707  1.00 54.57  ? 631  PRO B O   1 
ATOM   8058 C CB  . PRO B 1 536 ? 9.901   75.096  18.382  1.00 56.45  ? 631  PRO B CB  1 
ATOM   8059 C CG  . PRO B 1 536 ? 8.609   74.663  19.003  1.00 55.02  ? 631  PRO B CG  1 
ATOM   8060 C CD  . PRO B 1 536 ? 7.536   75.380  18.282  1.00 55.40  ? 631  PRO B CD  1 
ATOM   8061 O OXT . PRO B 1 536 ? 11.135  74.461  15.432  1.00 57.57  ? 631  PRO B OXT 1 
HETATM 8062 S S   . SO4 C 2 .   ? 30.010  60.951  -8.598  0.75 81.58  ? 701  SO4 A S   1 
HETATM 8063 O O1  . SO4 C 2 .   ? 31.472  60.964  -8.265  0.75 80.09  ? 701  SO4 A O1  1 
HETATM 8064 O O2  . SO4 C 2 .   ? 29.789  59.929  -9.678  0.75 71.59  ? 701  SO4 A O2  1 
HETATM 8065 O O3  . SO4 C 2 .   ? 29.228  60.625  -7.346  0.75 64.55  ? 701  SO4 A O3  1 
HETATM 8066 O O4  . SO4 C 2 .   ? 29.607  62.303  -9.122  0.75 78.51  ? 701  SO4 A O4  1 
HETATM 8067 C C1  . EDO D 3 .   ? 36.268  35.364  1.413   0.97 65.19  ? 702  EDO A C1  1 
HETATM 8068 O O1  . EDO D 3 .   ? 35.588  36.601  1.528   0.97 62.51  ? 702  EDO A O1  1 
HETATM 8069 C C2  . EDO D 3 .   ? 35.497  34.451  0.478   0.97 68.30  ? 702  EDO A C2  1 
HETATM 8070 O O2  . EDO D 3 .   ? 34.375  33.854  1.108   0.97 66.49  ? 702  EDO A O2  1 
HETATM 8071 S S   . SO4 E 2 .   ? 40.038  74.278  3.870   0.61 78.99  ? 703  SO4 A S   1 
HETATM 8072 O O1  . SO4 E 2 .   ? 39.868  75.485  2.998   0.61 79.14  ? 703  SO4 A O1  1 
HETATM 8073 O O2  . SO4 E 2 .   ? 38.974  73.270  3.547   0.61 77.83  ? 703  SO4 A O2  1 
HETATM 8074 O O3  . SO4 E 2 .   ? 41.379  73.663  3.627   0.61 73.03  ? 703  SO4 A O3  1 
HETATM 8075 O O4  . SO4 E 2 .   ? 39.952  74.689  5.308   0.61 72.52  ? 703  SO4 A O4  1 
HETATM 8076 S S   . SO4 F 2 .   ? 36.880  78.895  32.183  0.56 76.71  ? 704  SO4 A S   1 
HETATM 8077 O O1  . SO4 F 2 .   ? 38.359  78.643  32.115  0.56 76.59  ? 704  SO4 A O1  1 
HETATM 8078 O O2  . SO4 F 2 .   ? 36.170  77.922  31.303  0.56 67.60  ? 704  SO4 A O2  1 
HETATM 8079 O O3  . SO4 F 2 .   ? 36.393  78.730  33.594  0.56 84.76  ? 704  SO4 A O3  1 
HETATM 8080 O O4  . SO4 F 2 .   ? 36.596  80.305  31.749  0.56 77.21  ? 704  SO4 A O4  1 
HETATM 8081 S S   . SO4 G 2 .   ? -1.625  73.281  15.713  0.66 83.14  ? 701  SO4 B S   1 
HETATM 8082 O O1  . SO4 G 2 .   ? -0.389  72.463  15.696  0.66 66.40  ? 701  SO4 B O1  1 
HETATM 8083 O O2  . SO4 G 2 .   ? -1.410  74.583  15.073  0.66 78.53  ? 701  SO4 B O2  1 
HETATM 8084 O O3  . SO4 G 2 .   ? -2.684  72.594  14.965  0.66 82.95  ? 701  SO4 B O3  1 
HETATM 8085 O O4  . SO4 G 2 .   ? -2.045  73.516  17.101  0.66 73.21  ? 701  SO4 B O4  1 
HETATM 8086 C C1  . EDO H 3 .   ? 5.120   62.590  40.803  1.00 74.68  ? 702  EDO B C1  1 
HETATM 8087 O O1  . EDO H 3 .   ? 5.547   62.447  39.462  1.00 71.57  ? 702  EDO B O1  1 
HETATM 8088 C C2  . EDO H 3 .   ? 6.002   63.590  41.518  1.00 77.10  ? 702  EDO B C2  1 
HETATM 8089 O O2  . EDO H 3 .   ? 7.278   63.042  41.785  1.00 80.57  ? 702  EDO B O2  1 
HETATM 8090 O O   . HOH I 4 .   ? 44.619  67.482  13.238  1.00 50.29  ? 801  HOH A O   1 
HETATM 8091 O O   . HOH I 4 .   ? 46.610  76.875  7.086   1.00 59.43  ? 802  HOH A O   1 
HETATM 8092 O O   . HOH I 4 .   ? 18.912  54.502  15.659  0.74 53.66  ? 803  HOH A O   1 
HETATM 8093 O O   . HOH I 4 .   ? 43.389  72.445  3.219   1.00 62.61  ? 804  HOH A O   1 
HETATM 8094 O O   . HOH I 4 .   ? 59.416  73.383  6.221   1.00 60.77  ? 805  HOH A O   1 
HETATM 8095 O O   . HOH I 4 .   ? 18.585  14.587  -14.037 1.00 60.49  ? 806  HOH A O   1 
HETATM 8096 O O   . HOH I 4 .   ? 24.172  17.810  -24.460 0.82 58.41  ? 807  HOH A O   1 
HETATM 8097 O O   . HOH I 4 .   ? 8.932   18.277  -15.787 1.00 70.78  ? 808  HOH A O   1 
HETATM 8098 O O   . HOH I 4 .   ? 25.510  68.341  15.009  1.00 47.34  ? 809  HOH A O   1 
HETATM 8099 O O   . HOH I 4 .   ? 17.991  55.399  28.633  1.00 55.78  ? 810  HOH A O   1 
HETATM 8100 O O   . HOH I 4 .   ? 38.859  23.198  -10.085 0.94 60.30  ? 811  HOH A O   1 
HETATM 8101 O O   . HOH I 4 .   ? 30.756  64.937  -6.545  1.00 60.21  ? 812  HOH A O   1 
HETATM 8102 O O   . HOH I 4 .   ? 23.025  30.995  1.863   1.00 47.67  ? 813  HOH A O   1 
HETATM 8103 O O   . HOH I 4 .   ? 17.676  59.245  17.132  1.00 36.75  ? 814  HOH A O   1 
HETATM 8104 O O   . HOH I 4 .   ? 20.004  9.718   -17.385 1.00 81.29  ? 815  HOH A O   1 
HETATM 8105 O O   . HOH I 4 .   ? 54.458  66.140  18.673  1.00 62.73  ? 816  HOH A O   1 
HETATM 8106 O O   . HOH I 4 .   ? 44.209  61.862  14.141  0.63 48.08  ? 817  HOH A O   1 
HETATM 8107 O O   . HOH I 4 .   ? 41.933  59.119  27.271  1.00 52.90  ? 818  HOH A O   1 
HETATM 8108 O O   . HOH I 4 .   ? 20.757  60.457  5.246   1.00 53.24  ? 819  HOH A O   1 
HETATM 8109 O O   . HOH I 4 .   ? 39.860  67.951  9.236   1.00 55.78  ? 820  HOH A O   1 
HETATM 8110 O O   . HOH I 4 .   ? 45.085  58.233  21.232  1.00 52.45  ? 821  HOH A O   1 
HETATM 8111 O O   . HOH I 4 .   ? 53.664  60.487  10.994  1.00 60.59  ? 822  HOH A O   1 
HETATM 8112 O O   . HOH I 4 .   ? 29.563  65.116  34.756  1.00 59.24  ? 823  HOH A O   1 
HETATM 8113 O O   . HOH I 4 .   ? 15.432  61.836  14.150  1.00 44.59  ? 824  HOH A O   1 
HETATM 8114 O O   . HOH I 4 .   ? 18.366  29.412  6.931   0.87 54.66  ? 825  HOH A O   1 
HETATM 8115 O O   . HOH I 4 .   ? 18.320  20.075  4.992   1.00 51.91  ? 826  HOH A O   1 
HETATM 8116 O O   A HOH I 4 .   ? 19.780  35.961  -18.189 0.61 49.40  ? 827  HOH A O   1 
HETATM 8117 O O   B HOH I 4 .   ? 21.706  36.754  -18.762 0.39 51.88  ? 827  HOH A O   1 
HETATM 8118 O O   . HOH I 4 .   ? 27.085  39.906  8.643   1.00 51.96  ? 828  HOH A O   1 
HETATM 8119 O O   . HOH I 4 .   ? 40.064  41.466  -2.975  1.00 66.22  ? 829  HOH A O   1 
HETATM 8120 O O   . HOH I 4 .   ? 40.520  57.784  5.241   1.00 53.40  ? 830  HOH A O   1 
HETATM 8121 O O   . HOH I 4 .   ? 14.444  77.741  30.260  1.00 53.78  ? 831  HOH A O   1 
HETATM 8122 O O   . HOH I 4 .   ? 43.070  57.423  22.959  1.00 54.25  ? 832  HOH A O   1 
HETATM 8123 O O   . HOH I 4 .   ? 23.406  38.047  -16.846 1.00 57.22  ? 833  HOH A O   1 
HETATM 8124 O O   . HOH I 4 .   ? 25.869  16.493  4.371   1.00 63.09  ? 834  HOH A O   1 
HETATM 8125 O O   . HOH I 4 .   ? 33.856  49.867  -2.800  1.00 45.68  ? 835  HOH A O   1 
HETATM 8126 O O   . HOH I 4 .   ? 23.764  52.220  6.153   1.00 37.94  ? 836  HOH A O   1 
HETATM 8127 O O   . HOH I 4 .   ? 31.787  67.299  12.807  1.00 61.04  ? 837  HOH A O   1 
HETATM 8128 O O   . HOH I 4 .   ? 36.502  17.012  -16.032 1.00 51.12  ? 838  HOH A O   1 
HETATM 8129 O O   . HOH I 4 .   ? 24.645  57.516  4.441   1.00 40.94  ? 839  HOH A O   1 
HETATM 8130 O O   . HOH I 4 .   ? 31.764  82.685  21.979  1.00 55.00  ? 840  HOH A O   1 
HETATM 8131 O O   . HOH I 4 .   ? 34.041  43.680  -15.236 1.00 55.98  ? 841  HOH A O   1 
HETATM 8132 O O   . HOH I 4 .   ? 43.521  60.883  6.890   1.00 51.21  ? 842  HOH A O   1 
HETATM 8133 O O   . HOH I 4 .   ? 19.376  81.507  31.151  1.00 66.55  ? 843  HOH A O   1 
HETATM 8134 O O   . HOH I 4 .   ? 19.965  73.435  30.184  1.00 54.43  ? 844  HOH A O   1 
HETATM 8135 O O   . HOH I 4 .   ? 31.455  66.127  -2.647  1.00 50.63  ? 845  HOH A O   1 
HETATM 8136 O O   . HOH I 4 .   ? 44.513  54.338  3.741   1.00 59.43  ? 846  HOH A O   1 
HETATM 8137 O O   . HOH I 4 .   ? 28.558  49.935  23.455  1.00 46.71  ? 847  HOH A O   1 
HETATM 8138 O O   . HOH I 4 .   ? 35.848  42.768  -1.840  1.00 43.04  ? 848  HOH A O   1 
HETATM 8139 O O   . HOH I 4 .   ? 32.052  85.240  21.477  1.00 58.73  ? 849  HOH A O   1 
HETATM 8140 O O   . HOH I 4 .   ? 22.074  34.850  7.200   1.00 47.75  ? 850  HOH A O   1 
HETATM 8141 O O   . HOH I 4 .   ? 16.730  68.158  13.953  1.00 43.49  ? 851  HOH A O   1 
HETATM 8142 O O   . HOH I 4 .   ? 37.456  69.136  -5.858  0.90 73.64  ? 852  HOH A O   1 
HETATM 8143 O O   . HOH I 4 .   ? 57.846  77.216  10.488  1.00 63.62  ? 853  HOH A O   1 
HETATM 8144 O O   . HOH I 4 .   ? 47.073  59.510  12.109  1.00 53.04  ? 854  HOH A O   1 
HETATM 8145 O O   A HOH I 4 .   ? 25.509  69.391  8.196   0.48 48.92  ? 855  HOH A O   1 
HETATM 8146 O O   B HOH I 4 .   ? 26.675  71.690  8.050   0.52 48.07  ? 855  HOH A O   1 
HETATM 8147 O O   . HOH I 4 .   ? 28.847  69.963  16.576  1.00 50.49  ? 856  HOH A O   1 
HETATM 8148 O O   . HOH I 4 .   ? 19.159  74.409  8.196   1.00 58.56  ? 857  HOH A O   1 
HETATM 8149 O O   . HOH I 4 .   ? 16.741  15.276  -17.989 1.00 58.12  ? 858  HOH A O   1 
HETATM 8150 O O   . HOH I 4 .   ? 26.686  69.796  18.375  1.00 46.71  ? 859  HOH A O   1 
HETATM 8151 O O   . HOH I 4 .   ? 24.930  24.398  -21.395 1.00 48.19  ? 860  HOH A O   1 
HETATM 8152 O O   . HOH I 4 .   ? 52.505  57.708  23.149  1.00 61.26  ? 861  HOH A O   1 
HETATM 8153 O O   . HOH I 4 .   ? 34.387  46.535  -3.507  1.00 43.12  ? 862  HOH A O   1 
HETATM 8154 O O   . HOH I 4 .   ? 21.563  63.789  14.312  1.00 42.38  ? 863  HOH A O   1 
HETATM 8155 O O   . HOH I 4 .   ? 34.095  55.261  -3.926  1.00 43.54  ? 864  HOH A O   1 
HETATM 8156 O O   . HOH I 4 .   ? 33.184  41.014  17.112  1.00 59.50  ? 865  HOH A O   1 
HETATM 8157 O O   . HOH I 4 .   ? 20.042  71.970  4.562   1.00 50.69  ? 866  HOH A O   1 
HETATM 8158 O O   . HOH I 4 .   ? 20.634  48.705  24.378  1.00 47.98  ? 867  HOH A O   1 
HETATM 8159 O O   . HOH I 4 .   ? 35.094  68.697  1.556   1.00 63.49  ? 868  HOH A O   1 
HETATM 8160 O O   . HOH I 4 .   ? 34.263  25.035  -0.455  1.00 50.52  ? 869  HOH A O   1 
HETATM 8161 O O   . HOH I 4 .   ? 32.160  81.326  19.252  1.00 52.74  ? 870  HOH A O   1 
HETATM 8162 O O   . HOH I 4 .   ? 25.055  60.353  1.243   1.00 39.33  ? 871  HOH A O   1 
HETATM 8163 O O   . HOH I 4 .   ? 19.078  72.654  14.906  1.00 47.96  ? 872  HOH A O   1 
HETATM 8164 O O   . HOH I 4 .   ? 38.021  29.812  6.558   1.00 60.66  ? 873  HOH A O   1 
HETATM 8165 O O   . HOH I 4 .   ? 17.226  80.870  7.811   1.00 77.18  ? 874  HOH A O   1 
HETATM 8166 O O   . HOH I 4 .   ? 10.650  31.156  -7.956  1.00 55.49  ? 875  HOH A O   1 
HETATM 8167 O O   . HOH I 4 .   ? 23.634  77.641  33.788  1.00 61.50  ? 876  HOH A O   1 
HETATM 8168 O O   . HOH I 4 .   ? 27.032  15.637  -8.408  1.00 52.85  ? 877  HOH A O   1 
HETATM 8169 O O   . HOH I 4 .   ? 28.187  39.009  -0.939  1.00 47.99  ? 878  HOH A O   1 
HETATM 8170 O O   . HOH I 4 .   ? 29.639  61.396  7.919   1.00 43.78  ? 879  HOH A O   1 
HETATM 8171 O O   . HOH I 4 .   ? 17.104  59.198  -6.412  1.00 49.72  ? 880  HOH A O   1 
HETATM 8172 O O   . HOH I 4 .   ? 11.396  67.186  31.041  1.00 52.02  ? 881  HOH A O   1 
HETATM 8173 O O   . HOH I 4 .   ? 13.349  63.246  13.512  1.00 45.75  ? 882  HOH A O   1 
HETATM 8174 O O   . HOH I 4 .   ? 32.239  51.436  -4.324  1.00 40.07  ? 883  HOH A O   1 
HETATM 8175 O O   . HOH I 4 .   ? 18.515  68.738  31.368  1.00 47.86  ? 884  HOH A O   1 
HETATM 8176 O O   . HOH I 4 .   ? 28.892  36.750  -9.883  1.00 41.48  ? 885  HOH A O   1 
HETATM 8177 O O   . HOH I 4 .   ? 52.311  72.750  5.229   0.93 57.57  ? 886  HOH A O   1 
HETATM 8178 O O   . HOH I 4 .   ? 26.947  75.596  29.859  1.00 51.19  ? 887  HOH A O   1 
HETATM 8179 O O   . HOH I 4 .   ? 35.661  72.373  13.457  1.00 59.94  ? 888  HOH A O   1 
HETATM 8180 O O   . HOH I 4 .   ? 25.162  66.918  35.218  1.00 55.34  ? 889  HOH A O   1 
HETATM 8181 O O   . HOH I 4 .   ? 12.554  60.729  23.312  1.00 38.03  ? 890  HOH A O   1 
HETATM 8182 O O   . HOH I 4 .   ? 31.239  51.097  -0.689  1.00 43.47  ? 891  HOH A O   1 
HETATM 8183 O O   . HOH I 4 .   ? 36.995  50.357  -5.638  1.00 60.74  ? 892  HOH A O   1 
HETATM 8184 O O   . HOH I 4 .   ? 12.982  30.423  -11.379 1.00 49.33  ? 893  HOH A O   1 
HETATM 8185 O O   . HOH I 4 .   ? 27.445  66.137  12.352  0.86 58.18  ? 894  HOH A O   1 
HETATM 8186 O O   . HOH I 4 .   ? 28.333  21.334  -19.601 1.00 53.14  ? 895  HOH A O   1 
HETATM 8187 O O   . HOH I 4 .   ? 15.434  15.689  -13.487 1.00 57.14  ? 896  HOH A O   1 
HETATM 8188 O O   . HOH I 4 .   ? 23.450  41.534  6.902   1.00 45.34  ? 897  HOH A O   1 
HETATM 8189 O O   . HOH I 4 .   ? 36.858  23.604  -1.149  1.00 70.73  ? 898  HOH A O   1 
HETATM 8190 O O   . HOH I 4 .   ? 27.922  58.353  33.063  1.00 58.27  ? 899  HOH A O   1 
HETATM 8191 O O   . HOH I 4 .   ? 47.661  61.075  14.336  1.00 54.19  ? 900  HOH A O   1 
HETATM 8192 O O   . HOH I 4 .   ? 15.983  61.932  30.328  1.00 57.32  ? 901  HOH A O   1 
HETATM 8193 O O   . HOH I 4 .   ? 32.232  75.205  19.216  1.00 47.69  ? 902  HOH A O   1 
HETATM 8194 O O   . HOH I 4 .   ? 16.688  81.925  32.928  1.00 57.19  ? 903  HOH A O   1 
HETATM 8195 O O   . HOH I 4 .   ? 23.805  78.044  23.734  1.00 47.30  ? 904  HOH A O   1 
HETATM 8196 O O   . HOH I 4 .   ? 38.672  84.895  19.118  1.00 58.31  ? 905  HOH A O   1 
HETATM 8197 O O   . HOH I 4 .   ? 12.251  25.963  5.846   1.00 62.43  ? 906  HOH A O   1 
HETATM 8198 O O   . HOH I 4 .   ? 23.790  57.271  -4.767  1.00 44.18  ? 907  HOH A O   1 
HETATM 8199 O O   . HOH I 4 .   ? 22.667  59.131  1.223   1.00 46.19  ? 908  HOH A O   1 
HETATM 8200 O O   . HOH I 4 .   ? 17.938  56.507  14.290  1.00 67.44  ? 909  HOH A O   1 
HETATM 8201 O O   . HOH I 4 .   ? 24.864  64.783  32.400  1.00 51.51  ? 910  HOH A O   1 
HETATM 8202 O O   . HOH I 4 .   ? 44.288  77.901  22.474  1.00 60.25  ? 911  HOH A O   1 
HETATM 8203 O O   . HOH I 4 .   ? 24.208  51.616  10.085  1.00 40.66  ? 912  HOH A O   1 
HETATM 8204 O O   . HOH I 4 .   ? 28.123  70.751  -8.826  1.00 59.57  ? 913  HOH A O   1 
HETATM 8205 O O   . HOH I 4 .   ? 47.552  77.228  25.305  1.00 66.06  ? 914  HOH A O   1 
HETATM 8206 O O   . HOH I 4 .   ? 33.990  71.475  -5.679  1.00 60.51  ? 915  HOH A O   1 
HETATM 8207 O O   . HOH I 4 .   ? 14.389  17.850  -14.300 1.00 55.81  ? 916  HOH A O   1 
HETATM 8208 O O   . HOH I 4 .   ? 19.909  65.002  12.519  1.00 41.39  ? 917  HOH A O   1 
HETATM 8209 O O   . HOH I 4 .   ? 7.354   19.777  -6.381  1.00 70.29  ? 918  HOH A O   1 
HETATM 8210 O O   . HOH I 4 .   ? 21.912  62.750  -10.350 1.00 57.15  ? 919  HOH A O   1 
HETATM 8211 O O   . HOH I 4 .   ? 27.376  81.065  14.536  1.00 51.95  ? 920  HOH A O   1 
HETATM 8212 O O   . HOH I 4 .   ? 24.528  49.529  6.960   1.00 37.96  ? 921  HOH A O   1 
HETATM 8213 O O   . HOH I 4 .   ? 20.580  49.566  20.592  1.00 51.30  ? 922  HOH A O   1 
HETATM 8214 O O   . HOH I 4 .   ? 19.142  68.326  34.035  1.00 50.61  ? 923  HOH A O   1 
HETATM 8215 O O   . HOH I 4 .   ? 34.837  61.413  -5.686  1.00 52.21  ? 924  HOH A O   1 
HETATM 8216 O O   . HOH I 4 .   ? 31.471  39.274  -3.595  1.00 41.74  ? 925  HOH A O   1 
HETATM 8217 O O   . HOH I 4 .   ? 36.924  63.419  6.159   1.00 77.05  ? 926  HOH A O   1 
HETATM 8218 O O   . HOH I 4 .   ? 36.435  54.042  27.079  1.00 54.32  ? 927  HOH A O   1 
HETATM 8219 O O   . HOH I 4 .   ? 38.881  53.336  -5.068  1.00 69.44  ? 928  HOH A O   1 
HETATM 8220 O O   . HOH I 4 .   ? 38.485  59.670  28.888  1.00 54.61  ? 929  HOH A O   1 
HETATM 8221 O O   . HOH I 4 .   ? 35.294  49.002  25.631  1.00 62.17  ? 930  HOH A O   1 
HETATM 8222 O O   . HOH I 4 .   ? 39.981  53.197  -0.227  1.00 48.76  ? 931  HOH A O   1 
HETATM 8223 O O   . HOH I 4 .   ? 41.406  49.815  10.618  1.00 51.76  ? 932  HOH A O   1 
HETATM 8224 O O   . HOH I 4 .   ? 56.691  64.180  15.408  1.00 62.07  ? 933  HOH A O   1 
HETATM 8225 O O   . HOH I 4 .   ? 41.694  30.445  3.194   0.98 76.28  ? 934  HOH A O   1 
HETATM 8226 O O   . HOH I 4 .   ? 20.893  89.488  19.749  1.00 62.09  ? 935  HOH A O   1 
HETATM 8227 O O   . HOH I 4 .   ? 19.674  26.904  -17.827 1.00 49.45  ? 936  HOH A O   1 
HETATM 8228 O O   . HOH I 4 .   ? 32.191  37.832  17.461  1.00 70.78  ? 937  HOH A O   1 
HETATM 8229 O O   . HOH I 4 .   ? 17.138  29.357  -19.454 1.00 57.42  ? 938  HOH A O   1 
HETATM 8230 O O   . HOH I 4 .   ? 13.435  33.129  -12.127 1.00 46.09  ? 939  HOH A O   1 
HETATM 8231 O O   . HOH I 4 .   ? 14.314  25.697  7.229   1.00 57.84  ? 940  HOH A O   1 
HETATM 8232 O O   . HOH I 4 .   ? 24.698  54.684  4.633   1.00 38.55  ? 941  HOH A O   1 
HETATM 8233 O O   . HOH I 4 .   ? 38.012  48.337  -9.228  1.00 61.29  ? 942  HOH A O   1 
HETATM 8234 O O   . HOH I 4 .   ? 34.467  57.323  -11.784 1.00 56.05  ? 943  HOH A O   1 
HETATM 8235 O O   . HOH I 4 .   ? 21.107  32.990  0.646   1.00 63.54  ? 944  HOH A O   1 
HETATM 8236 O O   . HOH I 4 .   ? 30.284  63.866  32.113  1.00 54.73  ? 945  HOH A O   1 
HETATM 8237 O O   . HOH I 4 .   ? 9.708   23.610  -19.281 1.00 57.70  ? 946  HOH A O   1 
HETATM 8238 O O   . HOH I 4 .   ? 48.611  53.640  25.729  1.00 66.86  ? 947  HOH A O   1 
HETATM 8239 O O   . HOH I 4 .   ? 42.129  48.675  15.305  1.00 59.25  ? 948  HOH A O   1 
HETATM 8240 O O   . HOH I 4 .   ? 48.491  52.143  5.784   1.00 62.42  ? 949  HOH A O   1 
HETATM 8241 O O   . HOH I 4 .   ? 30.151  20.930  -17.645 1.00 51.94  ? 950  HOH A O   1 
HETATM 8242 O O   . HOH I 4 .   ? 26.941  44.297  12.007  1.00 45.61  ? 951  HOH A O   1 
HETATM 8243 O O   . HOH I 4 .   ? 30.176  38.195  -11.453 1.00 52.58  ? 952  HOH A O   1 
HETATM 8244 O O   . HOH I 4 .   ? 24.539  38.860  -2.572  1.00 42.81  ? 953  HOH A O   1 
HETATM 8245 O O   . HOH I 4 .   ? 26.325  34.703  -16.526 1.00 52.14  ? 954  HOH A O   1 
HETATM 8246 O O   . HOH I 4 .   ? 10.186  66.146  16.791  1.00 40.81  ? 955  HOH A O   1 
HETATM 8247 O O   . HOH I 4 .   ? 26.566  38.825  -17.012 1.00 57.77  ? 956  HOH A O   1 
HETATM 8248 O O   . HOH I 4 .   ? 45.777  46.112  5.528   1.00 58.43  ? 957  HOH A O   1 
HETATM 8249 O O   . HOH I 4 .   ? 5.702   30.689  -5.969  1.00 63.77  ? 958  HOH A O   1 
HETATM 8250 O O   . HOH I 4 .   ? 40.793  87.525  25.492  1.00 71.24  ? 959  HOH A O   1 
HETATM 8251 O O   . HOH I 4 .   ? 40.877  51.949  25.027  1.00 58.96  ? 960  HOH A O   1 
HETATM 8252 O O   . HOH I 4 .   ? 35.626  36.979  -6.361  1.00 59.88  ? 961  HOH A O   1 
HETATM 8253 O O   . HOH I 4 .   ? 34.577  51.217  -14.938 1.00 57.13  ? 962  HOH A O   1 
HETATM 8254 O O   . HOH I 4 .   ? 25.743  60.882  -10.905 1.00 65.59  ? 963  HOH A O   1 
HETATM 8255 O O   . HOH I 4 .   ? 28.771  72.149  18.059  1.00 51.45  ? 964  HOH A O   1 
HETATM 8256 O O   A HOH I 4 .   ? 39.006  65.731  -3.111  0.66 53.77  ? 965  HOH A O   1 
HETATM 8257 O O   B HOH I 4 .   ? 38.841  65.410  -3.914  0.34 53.15  ? 965  HOH A O   1 
HETATM 8258 O O   . HOH I 4 .   ? 38.640  59.120  -4.468  1.00 56.46  ? 966  HOH A O   1 
HETATM 8259 O O   . HOH I 4 .   ? 32.004  73.713  14.991  0.99 68.97  ? 967  HOH A O   1 
HETATM 8260 O O   . HOH I 4 .   ? 40.832  41.161  17.170  1.00 70.66  ? 968  HOH A O   1 
HETATM 8261 O O   . HOH I 4 .   ? 22.375  48.084  -9.402  1.00 50.76  ? 969  HOH A O   1 
HETATM 8262 O O   . HOH I 4 .   ? 27.262  80.453  29.689  1.00 55.99  ? 970  HOH A O   1 
HETATM 8263 O O   . HOH I 4 .   ? 41.532  48.403  12.562  1.00 54.53  ? 971  HOH A O   1 
HETATM 8264 O O   . HOH I 4 .   ? 16.115  59.449  12.978  0.54 43.24  ? 972  HOH A O   1 
HETATM 8265 O O   . HOH I 4 .   ? 35.948  41.269  25.504  0.98 81.58  ? 973  HOH A O   1 
HETATM 8266 O O   . HOH I 4 .   ? 25.012  54.929  -5.282  1.00 41.74  ? 974  HOH A O   1 
HETATM 8267 O O   . HOH I 4 .   ? 24.990  65.404  -12.566 1.00 73.51  ? 975  HOH A O   1 
HETATM 8268 O O   . HOH I 4 .   ? 37.364  75.905  14.383  1.00 57.97  ? 976  HOH A O   1 
HETATM 8269 O O   . HOH I 4 .   ? 33.625  12.777  -13.744 0.99 72.70  ? 977  HOH A O   1 
HETATM 8270 O O   . HOH I 4 .   ? 48.381  46.737  10.552  1.00 63.43  ? 978  HOH A O   1 
HETATM 8271 O O   . HOH I 4 .   ? 22.725  60.185  34.717  1.00 62.53  ? 979  HOH A O   1 
HETATM 8272 O O   . HOH I 4 .   ? 25.161  36.765  -15.254 1.00 49.85  ? 980  HOH A O   1 
HETATM 8273 O O   . HOH I 4 .   ? 20.490  73.673  11.052  1.00 52.49  ? 981  HOH A O   1 
HETATM 8274 O O   . HOH I 4 .   ? 30.152  65.379  4.645   1.00 58.81  ? 982  HOH A O   1 
HETATM 8275 O O   . HOH I 4 .   ? 16.107  54.603  -6.946  1.00 71.64  ? 983  HOH A O   1 
HETATM 8276 O O   . HOH I 4 .   ? 42.111  27.487  -4.834  1.00 73.18  ? 984  HOH A O   1 
HETATM 8277 O O   A HOH I 4 .   ? 25.326  45.792  14.628  0.37 44.17  ? 985  HOH A O   1 
HETATM 8278 O O   B HOH I 4 .   ? 24.800  45.162  13.482  0.63 39.99  ? 985  HOH A O   1 
HETATM 8279 O O   . HOH I 4 .   ? 32.355  37.359  -11.785 1.00 49.47  ? 986  HOH A O   1 
HETATM 8280 O O   . HOH I 4 .   ? 18.203  75.285  -2.048  1.00 64.19  ? 987  HOH A O   1 
HETATM 8281 O O   . HOH I 4 .   ? 32.106  54.024  -3.525  1.00 46.84  ? 988  HOH A O   1 
HETATM 8282 O O   . HOH I 4 .   ? 21.124  42.394  -20.962 0.90 60.68  ? 989  HOH A O   1 
HETATM 8283 O O   . HOH I 4 .   ? 7.896   32.061  -7.034  1.00 73.70  ? 990  HOH A O   1 
HETATM 8284 O O   . HOH I 4 .   ? 30.379  53.135  30.266  1.00 57.11  ? 991  HOH A O   1 
HETATM 8285 O O   . HOH I 4 .   ? 43.194  57.544  -3.481  1.00 68.38  ? 992  HOH A O   1 
HETATM 8286 O O   . HOH I 4 .   ? 45.899  50.670  19.375  1.00 62.92  ? 993  HOH A O   1 
HETATM 8287 O O   . HOH I 4 .   ? 33.062  78.558  32.024  1.00 77.28  ? 994  HOH A O   1 
HETATM 8288 O O   . HOH I 4 .   ? 16.818  56.676  30.809  1.00 58.08  ? 995  HOH A O   1 
HETATM 8289 O O   . HOH I 4 .   ? 42.150  52.432  1.192   1.00 52.89  ? 996  HOH A O   1 
HETATM 8290 O O   . HOH I 4 .   ? 32.033  65.187  10.929  1.00 73.43  ? 997  HOH A O   1 
HETATM 8291 O O   A HOH I 4 .   ? 26.040  52.109  -16.115 0.39 49.02  ? 998  HOH A O   1 
HETATM 8292 O O   B HOH I 4 .   ? 27.412  53.730  -15.542 0.61 50.92  ? 998  HOH A O   1 
HETATM 8293 O O   . HOH I 4 .   ? 27.355  47.242  22.031  0.95 58.66  ? 999  HOH A O   1 
HETATM 8294 O O   . HOH I 4 .   ? 39.689  31.154  4.203   1.00 65.63  ? 1000 HOH A O   1 
HETATM 8295 O O   . HOH I 4 .   ? 31.309  73.350  17.644  1.00 51.85  ? 1001 HOH A O   1 
HETATM 8296 O O   . HOH I 4 .   ? 48.287  47.930  5.252   1.00 68.79  ? 1002 HOH A O   1 
HETATM 8297 O O   . HOH I 4 .   ? 3.885   71.821  0.287   1.00 62.34  ? 1003 HOH A O   1 
HETATM 8298 O O   . HOH I 4 .   ? 37.427  56.835  -5.796  1.00 68.63  ? 1004 HOH A O   1 
HETATM 8299 O O   . HOH I 4 .   ? 48.900  51.668  20.672  1.00 68.24  ? 1005 HOH A O   1 
HETATM 8300 O O   . HOH I 4 .   ? 40.792  30.183  -5.301  1.00 76.13  ? 1006 HOH A O   1 
HETATM 8301 O O   . HOH I 4 .   ? 33.661  36.221  19.589  1.00 75.43  ? 1007 HOH A O   1 
HETATM 8302 O O   . HOH I 4 .   ? 40.887  52.854  -2.946  1.00 57.17  ? 1008 HOH A O   1 
HETATM 8303 O O   . HOH I 4 .   ? 17.810  25.070  9.615   1.00 69.69  ? 1009 HOH A O   1 
HETATM 8304 O O   . HOH I 4 .   ? 32.616  15.498  -20.993 1.00 50.79  ? 1010 HOH A O   1 
HETATM 8305 O O   . HOH I 4 .   ? 44.926  49.946  21.625  1.00 65.71  ? 1011 HOH A O   1 
HETATM 8306 O O   . HOH I 4 .   ? 37.923  51.876  26.221  1.00 57.23  ? 1012 HOH A O   1 
HETATM 8307 O O   A HOH I 4 .   ? 29.590  60.251  33.750  0.44 55.18  ? 1013 HOH A O   1 
HETATM 8308 O O   B HOH I 4 .   ? 30.535  61.225  32.873  0.56 52.02  ? 1013 HOH A O   1 
HETATM 8309 O O   . HOH I 4 .   ? 54.548  58.078  12.008  1.00 62.83  ? 1014 HOH A O   1 
HETATM 8310 O O   . HOH I 4 .   ? 33.635  68.353  4.095   1.00 63.10  ? 1015 HOH A O   1 
HETATM 8311 O O   A HOH I 4 .   ? 37.418  56.538  -10.607 0.40 52.30  ? 1016 HOH A O   1 
HETATM 8312 O O   B HOH I 4 .   ? 37.315  55.543  -9.699  0.60 50.84  ? 1016 HOH A O   1 
HETATM 8313 O O   . HOH I 4 .   ? 48.524  60.577  9.971   1.00 56.94  ? 1017 HOH A O   1 
HETATM 8314 O O   . HOH I 4 .   ? 34.234  63.936  -6.549  1.00 74.57  ? 1018 HOH A O   1 
HETATM 8315 O O   . HOH I 4 .   ? 9.918   30.208  -12.073 1.00 72.88  ? 1019 HOH A O   1 
HETATM 8316 O O   . HOH I 4 .   ? 45.724  43.280  4.273   1.00 66.56  ? 1020 HOH A O   1 
HETATM 8317 O O   . HOH I 4 .   ? 14.632  30.646  -18.769 1.00 59.33  ? 1021 HOH A O   1 
HETATM 8318 O O   . HOH I 4 .   ? 13.263  31.768  -16.868 1.00 57.40  ? 1022 HOH A O   1 
HETATM 8319 O O   . HOH I 4 .   ? 23.460  53.359  -15.051 1.00 69.56  ? 1023 HOH A O   1 
HETATM 8320 O O   . HOH I 4 .   ? 61.627  78.335  8.296   1.00 66.23  ? 1024 HOH A O   1 
HETATM 8321 O O   . HOH I 4 .   ? 10.348  64.281  14.206  1.00 44.09  ? 1025 HOH A O   1 
HETATM 8322 O O   . HOH I 4 .   ? 33.670  53.291  -5.426  1.00 49.28  ? 1026 HOH A O   1 
HETATM 8323 O O   . HOH I 4 .   ? 30.259  64.147  7.176   1.00 54.00  ? 1027 HOH A O   1 
HETATM 8324 O O   . HOH I 4 .   ? 33.506  86.142  19.484  1.00 62.30  ? 1028 HOH A O   1 
HETATM 8325 O O   A HOH I 4 .   ? 21.461  52.232  -14.720 0.55 56.67  ? 1029 HOH A O   1 
HETATM 8326 O O   B HOH I 4 .   ? 20.545  51.644  -14.093 0.45 56.73  ? 1029 HOH A O   1 
HETATM 8327 O O   . HOH I 4 .   ? 34.579  46.423  -15.891 1.00 60.95  ? 1030 HOH A O   1 
HETATM 8328 O O   . HOH I 4 .   ? 8.563   26.015  -19.760 0.88 70.72  ? 1031 HOH A O   1 
HETATM 8329 O O   . HOH I 4 .   ? 20.287  32.992  -19.268 1.00 67.81  ? 1032 HOH A O   1 
HETATM 8330 O O   . HOH I 4 .   ? 46.987  58.113  8.627   1.00 67.20  ? 1033 HOH A O   1 
HETATM 8331 O O   . HOH I 4 .   ? 38.231  54.518  -7.524  1.00 71.73  ? 1034 HOH A O   1 
HETATM 8332 O O   . HOH I 4 .   ? 32.876  87.159  14.659  1.00 70.36  ? 1035 HOH A O   1 
HETATM 8333 O O   . HOH I 4 .   ? 19.140  18.584  7.532   1.00 63.20  ? 1036 HOH A O   1 
HETATM 8334 O O   . HOH I 4 .   ? 26.486  37.761  -19.681 1.00 66.52  ? 1037 HOH A O   1 
HETATM 8335 O O   . HOH I 4 .   ? 33.037  87.343  17.026  1.00 70.40  ? 1038 HOH A O   1 
HETATM 8336 O O   A HOH I 4 .   ? 26.856  41.659  10.787  0.45 45.32  ? 1039 HOH A O   1 
HETATM 8337 O O   B HOH I 4 .   ? 24.740  40.935  11.924  0.55 41.66  ? 1039 HOH A O   1 
HETATM 8338 O O   . HOH I 4 .   ? 35.998  14.287  -14.681 1.00 57.55  ? 1040 HOH A O   1 
HETATM 8339 O O   . HOH I 4 .   ? 11.527  30.418  -16.020 1.00 65.92  ? 1041 HOH A O   1 
HETATM 8340 O O   . HOH J 4 .   ? 22.785  34.335  -0.899  1.00 46.35  ? 801  HOH B O   1 
HETATM 8341 O O   . HOH J 4 .   ? -6.213  49.195  7.050   0.79 58.50  ? 802  HOH B O   1 
HETATM 8342 O O   . HOH J 4 .   ? -9.234  47.556  12.524  1.00 48.14  ? 803  HOH B O   1 
HETATM 8343 O O   . HOH J 4 .   ? 10.195  64.426  50.230  1.00 78.85  ? 804  HOH B O   1 
HETATM 8344 O O   . HOH J 4 .   ? 22.581  48.100  -12.148 1.00 52.30  ? 805  HOH B O   1 
HETATM 8345 O O   . HOH J 4 .   ? -7.813  48.930  2.191   1.00 57.52  ? 806  HOH B O   1 
HETATM 8346 O O   . HOH J 4 .   ? -1.607  67.700  22.215  1.00 49.35  ? 807  HOH B O   1 
HETATM 8347 O O   . HOH J 4 .   ? -1.947  34.704  3.051   1.00 47.63  ? 808  HOH B O   1 
HETATM 8348 O O   . HOH J 4 .   ? 18.422  66.701  40.496  1.00 62.38  ? 809  HOH B O   1 
HETATM 8349 O O   . HOH J 4 .   ? -4.306  71.378  30.265  1.00 64.69  ? 810  HOH B O   1 
HETATM 8350 O O   . HOH J 4 .   ? 1.631   36.120  -11.960 1.00 63.03  ? 811  HOH B O   1 
HETATM 8351 O O   . HOH J 4 .   ? 14.027  58.732  32.953  1.00 56.94  ? 812  HOH B O   1 
HETATM 8352 O O   . HOH J 4 .   ? -7.011  48.684  26.753  1.00 52.18  ? 813  HOH B O   1 
HETATM 8353 O O   . HOH J 4 .   ? -9.822  71.599  32.226  1.00 82.79  ? 814  HOH B O   1 
HETATM 8354 O O   . HOH J 4 .   ? 1.128   35.595  14.456  1.00 45.46  ? 815  HOH B O   1 
HETATM 8355 O O   . HOH J 4 .   ? 8.086   28.033  5.446   1.00 54.70  ? 816  HOH B O   1 
HETATM 8356 O O   . HOH J 4 .   ? -3.979  71.081  32.873  1.00 62.86  ? 817  HOH B O   1 
HETATM 8357 O O   . HOH J 4 .   ? -3.632  73.467  6.167   1.00 59.84  ? 818  HOH B O   1 
HETATM 8358 O O   . HOH J 4 .   ? -2.741  70.933  12.217  0.81 57.44  ? 819  HOH B O   1 
HETATM 8359 O O   . HOH J 4 .   ? 7.960   52.743  5.134   1.00 46.18  ? 820  HOH B O   1 
HETATM 8360 O O   . HOH J 4 .   ? 13.715  45.767  27.221  0.81 56.69  ? 821  HOH B O   1 
HETATM 8361 O O   . HOH J 4 .   ? 22.558  68.091  -9.807  1.00 73.74  ? 822  HOH B O   1 
HETATM 8362 O O   . HOH J 4 .   ? 2.055   52.125  8.987   1.00 53.76  ? 823  HOH B O   1 
HETATM 8363 O O   . HOH J 4 .   ? -24.708 47.259  -2.055  1.00 64.87  ? 824  HOH B O   1 
HETATM 8364 O O   . HOH J 4 .   ? 11.722  34.841  -10.883 1.00 50.20  ? 825  HOH B O   1 
HETATM 8365 O O   . HOH J 4 .   ? -7.980  54.274  19.193  1.00 53.26  ? 826  HOH B O   1 
HETATM 8366 O O   . HOH J 4 .   ? 10.476  67.483  35.131  1.00 56.16  ? 827  HOH B O   1 
HETATM 8367 O O   . HOH J 4 .   ? 5.237   48.796  32.559  1.00 57.27  ? 828  HOH B O   1 
HETATM 8368 O O   . HOH J 4 .   ? -8.025  40.808  27.875  1.00 49.37  ? 829  HOH B O   1 
HETATM 8369 O O   . HOH J 4 .   ? -4.301  51.866  6.968   0.94 69.94  ? 830  HOH B O   1 
HETATM 8370 O O   . HOH J 4 .   ? 11.435  63.564  11.902  1.00 51.73  ? 831  HOH B O   1 
HETATM 8371 O O   . HOH J 4 .   ? 5.164   76.783  37.120  1.00 56.47  ? 832  HOH B O   1 
HETATM 8372 O O   . HOH J 4 .   ? -17.684 53.729  21.687  0.97 80.21  ? 833  HOH B O   1 
HETATM 8373 O O   . HOH J 4 .   ? -16.653 53.463  5.081   1.00 68.71  ? 834  HOH B O   1 
HETATM 8374 O O   . HOH J 4 .   ? -21.345 39.279  7.297   1.00 57.75  ? 835  HOH B O   1 
HETATM 8375 O O   . HOH J 4 .   ? -3.705  62.939  4.616   0.80 69.58  ? 836  HOH B O   1 
HETATM 8376 O O   . HOH J 4 .   ? 22.068  46.137  21.170  1.00 46.47  ? 837  HOH B O   1 
HETATM 8377 O O   . HOH J 4 .   ? -18.277 48.938  16.188  1.00 55.12  ? 838  HOH B O   1 
HETATM 8378 O O   . HOH J 4 .   ? 18.514  53.612  10.875  1.00 38.35  ? 839  HOH B O   1 
HETATM 8379 O O   . HOH J 4 .   ? 0.834   66.855  27.008  1.00 51.32  ? 840  HOH B O   1 
HETATM 8380 O O   . HOH J 4 .   ? -1.151  45.562  -4.981  1.00 41.54  ? 841  HOH B O   1 
HETATM 8381 O O   . HOH J 4 .   ? -1.576  78.610  33.770  1.00 61.76  ? 842  HOH B O   1 
HETATM 8382 O O   . HOH J 4 .   ? 20.388  61.500  32.667  0.71 52.46  ? 843  HOH B O   1 
HETATM 8383 O O   . HOH J 4 .   ? 19.273  41.804  -8.748  1.00 36.31  ? 844  HOH B O   1 
HETATM 8384 O O   . HOH J 4 .   ? 21.229  80.725  33.318  1.00 58.51  ? 845  HOH B O   1 
HETATM 8385 O O   . HOH J 4 .   ? 11.249  75.756  12.802  1.00 55.85  ? 846  HOH B O   1 
HETATM 8386 O O   . HOH J 4 .   ? -10.182 45.646  -4.934  1.00 54.62  ? 847  HOH B O   1 
HETATM 8387 O O   . HOH J 4 .   ? -1.325  34.569  15.426  1.00 45.15  ? 848  HOH B O   1 
HETATM 8388 O O   . HOH J 4 .   ? 8.717   63.175  16.016  1.00 41.76  ? 849  HOH B O   1 
HETATM 8389 O O   . HOH J 4 .   ? -3.665  56.735  14.925  1.00 68.96  ? 850  HOH B O   1 
HETATM 8390 O O   . HOH J 4 .   ? 1.818   65.573  34.128  1.00 49.87  ? 851  HOH B O   1 
HETATM 8391 O O   . HOH J 4 .   ? -16.519 55.471  6.933   1.00 67.57  ? 852  HOH B O   1 
HETATM 8392 O O   . HOH J 4 .   ? 7.445   75.477  38.431  1.00 59.77  ? 853  HOH B O   1 
HETATM 8393 O O   . HOH J 4 .   ? -16.854 41.615  25.697  1.00 54.66  ? 854  HOH B O   1 
HETATM 8394 O O   . HOH J 4 .   ? -6.418  72.568  22.834  1.00 66.71  ? 855  HOH B O   1 
HETATM 8395 O O   . HOH J 4 .   ? -2.512  67.082  10.951  1.00 53.70  ? 856  HOH B O   1 
HETATM 8396 O O   . HOH J 4 .   ? -8.159  67.441  37.790  1.00 72.82  ? 857  HOH B O   1 
HETATM 8397 O O   . HOH J 4 .   ? -25.253 45.013  7.842   1.00 65.51  ? 858  HOH B O   1 
HETATM 8398 O O   . HOH J 4 .   ? 20.612  37.992  8.188   1.00 45.00  ? 859  HOH B O   1 
HETATM 8399 O O   . HOH J 4 .   ? -6.600  47.044  17.391  1.00 45.40  ? 860  HOH B O   1 
HETATM 8400 O O   . HOH J 4 .   ? -1.259  39.254  20.728  1.00 41.30  ? 861  HOH B O   1 
HETATM 8401 O O   A HOH J 4 .   ? 23.302  41.641  15.545  0.48 39.76  ? 862  HOH B O   1 
HETATM 8402 O O   B HOH J 4 .   ? 23.539  42.826  13.569  0.52 39.88  ? 862  HOH B O   1 
HETATM 8403 O O   . HOH J 4 .   ? 12.095  32.613  7.849   1.00 48.08  ? 863  HOH B O   1 
HETATM 8404 O O   . HOH J 4 .   ? -17.907 41.994  19.110  1.00 54.59  ? 864  HOH B O   1 
HETATM 8405 O O   . HOH J 4 .   ? 15.817  55.000  26.719  1.00 50.02  ? 865  HOH B O   1 
HETATM 8406 O O   . HOH J 4 .   ? 3.560   33.831  22.603  1.00 51.82  ? 866  HOH B O   1 
HETATM 8407 O O   . HOH J 4 .   ? 6.502   65.791  13.750  1.00 45.49  ? 867  HOH B O   1 
HETATM 8408 O O   . HOH J 4 .   ? 8.996   37.857  -2.565  1.00 40.92  ? 868  HOH B O   1 
HETATM 8409 O O   . HOH J 4 .   ? 0.979   35.409  18.371  1.00 39.52  ? 869  HOH B O   1 
HETATM 8410 O O   . HOH J 4 .   ? 12.494  35.219  -5.586  1.00 47.12  ? 870  HOH B O   1 
HETATM 8411 O O   . HOH J 4 .   ? 15.160  56.578  2.428   1.00 38.33  ? 871  HOH B O   1 
HETATM 8412 O O   . HOH J 4 .   ? 11.983  62.038  20.661  1.00 41.02  ? 872  HOH B O   1 
HETATM 8413 O O   . HOH J 4 .   ? 13.203  36.571  -9.535  1.00 43.64  ? 873  HOH B O   1 
HETATM 8414 O O   . HOH J 4 .   ? 7.985   64.267  0.854   1.00 48.56  ? 874  HOH B O   1 
HETATM 8415 O O   . HOH J 4 .   ? -9.909  36.174  23.977  1.00 50.22  ? 875  HOH B O   1 
HETATM 8416 O O   . HOH J 4 .   ? -11.227 35.024  3.641   1.00 52.86  ? 876  HOH B O   1 
HETATM 8417 O O   . HOH J 4 .   ? 25.974  42.576  -0.079  1.00 42.40  ? 877  HOH B O   1 
HETATM 8418 O O   . HOH J 4 .   ? 18.584  57.054  8.110   1.00 43.07  ? 878  HOH B O   1 
HETATM 8419 O O   . HOH J 4 .   ? 15.327  35.083  13.798  1.00 49.87  ? 879  HOH B O   1 
HETATM 8420 O O   . HOH J 4 .   ? -0.119  47.065  29.049  1.00 45.71  ? 880  HOH B O   1 
HETATM 8421 O O   . HOH J 4 .   ? -12.184 50.357  -4.807  1.00 62.31  ? 881  HOH B O   1 
HETATM 8422 O O   . HOH J 4 .   ? 1.263   67.487  30.410  1.00 50.28  ? 882  HOH B O   1 
HETATM 8423 O O   . HOH J 4 .   ? 12.591  54.528  8.266   1.00 38.10  ? 883  HOH B O   1 
HETATM 8424 O O   . HOH J 4 .   ? -1.379  51.601  28.141  1.00 45.71  ? 884  HOH B O   1 
HETATM 8425 O O   . HOH J 4 .   ? -3.733  40.136  20.649  1.00 38.35  ? 885  HOH B O   1 
HETATM 8426 O O   . HOH J 4 .   ? 15.399  36.438  6.724   1.00 43.78  ? 886  HOH B O   1 
HETATM 8427 O O   . HOH J 4 .   ? 19.747  58.385  5.985   1.00 50.26  ? 887  HOH B O   1 
HETATM 8428 O O   . HOH J 4 .   ? 6.498   71.976  16.877  1.00 47.80  ? 888  HOH B O   1 
HETATM 8429 O O   . HOH J 4 .   ? 7.375   48.881  3.938   1.00 43.24  ? 889  HOH B O   1 
HETATM 8430 O O   . HOH J 4 .   ? -9.258  45.834  19.545  1.00 41.14  ? 890  HOH B O   1 
HETATM 8431 O O   . HOH J 4 .   ? 19.402  39.705  0.923   1.00 35.43  ? 891  HOH B O   1 
HETATM 8432 O O   . HOH J 4 .   ? -16.038 41.086  -3.692  1.00 56.43  ? 892  HOH B O   1 
HETATM 8433 O O   . HOH J 4 .   ? -4.077  58.375  27.834  1.00 52.95  ? 893  HOH B O   1 
HETATM 8434 O O   . HOH J 4 .   ? -2.816  31.158  23.661  1.00 49.65  ? 894  HOH B O   1 
HETATM 8435 O O   . HOH J 4 .   ? 8.841   66.682  14.302  1.00 46.34  ? 895  HOH B O   1 
HETATM 8436 O O   . HOH J 4 .   ? 11.786  54.650  -0.989  1.00 46.65  ? 896  HOH B O   1 
HETATM 8437 O O   . HOH J 4 .   ? 3.556   65.811  24.759  1.00 42.96  ? 897  HOH B O   1 
HETATM 8438 O O   . HOH J 4 .   ? 14.426  44.206  22.741  1.00 41.43  ? 898  HOH B O   1 
HETATM 8439 O O   . HOH J 4 .   ? 4.021   35.312  16.420  1.00 45.52  ? 899  HOH B O   1 
HETATM 8440 O O   . HOH J 4 .   ? 5.946   54.300  8.038   1.00 46.93  ? 900  HOH B O   1 
HETATM 8441 O O   . HOH J 4 .   ? 1.241   59.538  -1.522  0.91 74.49  ? 901  HOH B O   1 
HETATM 8442 O O   . HOH J 4 .   ? 8.700   60.970  -1.828  1.00 59.59  ? 902  HOH B O   1 
HETATM 8443 O O   . HOH J 4 .   ? 13.078  58.162  20.891  1.00 41.55  ? 903  HOH B O   1 
HETATM 8444 O O   . HOH J 4 .   ? -0.492  43.457  -6.542  1.00 43.46  ? 904  HOH B O   1 
HETATM 8445 O O   . HOH J 4 .   ? 6.375   68.737  36.272  1.00 52.54  ? 905  HOH B O   1 
HETATM 8446 O O   . HOH J 4 .   ? 4.923   49.834  4.626   0.75 43.98  ? 906  HOH B O   1 
HETATM 8447 O O   . HOH J 4 .   ? 13.050  56.942  6.517   1.00 39.57  ? 907  HOH B O   1 
HETATM 8448 O O   . HOH J 4 .   ? 4.154   57.992  13.861  1.00 40.79  ? 908  HOH B O   1 
HETATM 8449 O O   . HOH J 4 .   ? -9.072  48.163  21.085  1.00 45.00  ? 909  HOH B O   1 
HETATM 8450 O O   . HOH J 4 .   ? 2.784   69.856  40.068  1.00 61.51  ? 910  HOH B O   1 
HETATM 8451 O O   . HOH J 4 .   ? 12.994  70.267  34.370  1.00 52.71  ? 911  HOH B O   1 
HETATM 8452 O O   . HOH J 4 .   ? 8.452   32.633  11.593  1.00 56.09  ? 912  HOH B O   1 
HETATM 8453 O O   . HOH J 4 .   ? -2.981  50.309  5.130   1.00 62.38  ? 913  HOH B O   1 
HETATM 8454 O O   . HOH J 4 .   ? 7.428   37.859  21.159  1.00 42.23  ? 914  HOH B O   1 
HETATM 8455 O O   . HOH J 4 .   ? 15.327  33.720  4.511   1.00 44.75  ? 915  HOH B O   1 
HETATM 8456 O O   . HOH J 4 .   ? 8.864   44.642  -5.222  1.00 37.85  ? 916  HOH B O   1 
HETATM 8457 O O   . HOH J 4 .   ? 0.888   45.962  0.702   1.00 43.20  ? 917  HOH B O   1 
HETATM 8458 O O   . HOH J 4 .   ? 23.204  37.377  1.070   1.00 53.88  ? 918  HOH B O   1 
HETATM 8459 O O   . HOH J 4 .   ? 1.156   31.834  2.357   0.95 64.56  ? 919  HOH B O   1 
HETATM 8460 O O   . HOH J 4 .   ? 21.955  70.018  -12.405 1.00 74.95  ? 920  HOH B O   1 
HETATM 8461 O O   . HOH J 4 .   ? 3.177   58.695  2.665   1.00 60.85  ? 921  HOH B O   1 
HETATM 8462 O O   . HOH J 4 .   ? 4.839   42.430  30.458  1.00 47.73  ? 922  HOH B O   1 
HETATM 8463 O O   . HOH J 4 .   ? -9.461  38.679  2.165   1.00 46.31  ? 923  HOH B O   1 
HETATM 8464 O O   . HOH J 4 .   ? 19.697  37.042  1.333   1.00 38.02  ? 924  HOH B O   1 
HETATM 8465 O O   . HOH J 4 .   ? 5.109   59.226  4.641   1.00 60.15  ? 925  HOH B O   1 
HETATM 8466 O O   . HOH J 4 .   ? 6.421   48.805  -16.434 1.00 53.33  ? 926  HOH B O   1 
HETATM 8467 O O   . HOH J 4 .   ? -11.456 51.058  18.221  1.00 52.05  ? 927  HOH B O   1 
HETATM 8468 O O   A HOH J 4 .   ? -4.986  56.601  20.920  0.65 45.76  ? 928  HOH B O   1 
HETATM 8469 O O   B HOH J 4 .   ? -6.563  55.462  21.382  0.35 46.96  ? 928  HOH B O   1 
HETATM 8470 O O   . HOH J 4 .   ? 7.335   71.279  -1.493  1.00 59.75  ? 929  HOH B O   1 
HETATM 8471 O O   . HOH J 4 .   ? -17.639 48.295  -2.709  1.00 55.12  ? 930  HOH B O   1 
HETATM 8472 O O   . HOH J 4 .   ? -21.967 49.231  17.956  1.00 70.25  ? 931  HOH B O   1 
HETATM 8473 O O   . HOH J 4 .   ? -6.083  33.903  20.181  1.00 62.77  ? 932  HOH B O   1 
HETATM 8474 O O   . HOH J 4 .   ? 21.290  83.137  37.021  1.00 67.14  ? 933  HOH B O   1 
HETATM 8475 O O   . HOH J 4 .   ? 4.311   38.335  27.415  1.00 40.69  ? 934  HOH B O   1 
HETATM 8476 O O   . HOH J 4 .   ? -8.903  36.817  -7.816  1.00 61.76  ? 935  HOH B O   1 
HETATM 8477 O O   . HOH J 4 .   ? 16.748  38.725  -12.275 1.00 41.73  ? 936  HOH B O   1 
HETATM 8478 O O   . HOH J 4 .   ? -3.060  31.496  -0.398  1.00 65.94  ? 937  HOH B O   1 
HETATM 8479 O O   . HOH J 4 .   ? 4.720   33.267  0.291   1.00 46.40  ? 938  HOH B O   1 
HETATM 8480 O O   . HOH J 4 .   ? 10.858  48.625  33.070  1.00 55.01  ? 939  HOH B O   1 
HETATM 8481 O O   . HOH J 4 .   ? -15.793 39.154  16.295  1.00 54.32  ? 940  HOH B O   1 
HETATM 8482 O O   . HOH J 4 .   ? 1.432   51.883  -5.819  1.00 47.83  ? 941  HOH B O   1 
HETATM 8483 O O   . HOH J 4 .   ? -1.697  56.596  37.183  1.00 53.99  ? 942  HOH B O   1 
HETATM 8484 O O   . HOH J 4 .   ? -6.947  77.552  33.239  1.00 71.32  ? 943  HOH B O   1 
HETATM 8485 O O   . HOH J 4 .   ? 19.850  62.219  36.034  0.89 60.06  ? 944  HOH B O   1 
HETATM 8486 O O   . HOH J 4 .   ? -8.150  43.744  -5.883  1.00 48.10  ? 945  HOH B O   1 
HETATM 8487 O O   . HOH J 4 .   ? 14.012  38.939  -10.930 1.00 55.81  ? 946  HOH B O   1 
HETATM 8488 O O   . HOH J 4 .   ? 23.633  70.295  35.564  1.00 54.68  ? 947  HOH B O   1 
HETATM 8489 O O   . HOH J 4 .   ? 18.496  34.445  7.299   1.00 59.58  ? 948  HOH B O   1 
HETATM 8490 O O   . HOH J 4 .   ? 1.137   68.747  25.051  1.00 47.43  ? 949  HOH B O   1 
HETATM 8491 O O   . HOH J 4 .   ? 6.046   72.186  19.552  1.00 49.81  ? 950  HOH B O   1 
HETATM 8492 O O   . HOH J 4 .   ? -8.364  70.823  35.294  0.99 79.76  ? 951  HOH B O   1 
HETATM 8493 O O   A HOH J 4 .   ? -8.470  33.712  9.387   0.48 52.33  ? 952  HOH B O   1 
HETATM 8494 O O   B HOH J 4 .   ? -7.193  32.304  7.716   0.52 63.81  ? 952  HOH B O   1 
HETATM 8495 O O   . HOH J 4 .   ? -4.808  62.161  25.705  1.00 49.25  ? 953  HOH B O   1 
HETATM 8496 O O   . HOH J 4 .   ? 15.794  64.540  -10.662 1.00 68.17  ? 954  HOH B O   1 
HETATM 8497 O O   . HOH J 4 .   ? 3.802   34.020  -3.865  1.00 64.30  ? 955  HOH B O   1 
HETATM 8498 O O   . HOH J 4 .   ? 29.471  84.176  42.150  1.00 84.40  ? 956  HOH B O   1 
HETATM 8499 O O   . HOH J 4 .   ? 13.425  48.702  35.894  1.00 66.05  ? 957  HOH B O   1 
HETATM 8500 O O   . HOH J 4 .   ? -18.296 39.515  16.823  1.00 75.59  ? 958  HOH B O   1 
HETATM 8501 O O   . HOH J 4 .   ? -1.936  43.510  -8.945  1.00 52.28  ? 959  HOH B O   1 
HETATM 8502 O O   . HOH J 4 .   ? 22.674  56.135  1.983   1.00 41.00  ? 960  HOH B O   1 
HETATM 8503 O O   . HOH J 4 .   ? -5.649  54.901  33.635  1.00 55.60  ? 961  HOH B O   1 
HETATM 8504 O O   . HOH J 4 .   ? 1.154   66.615  48.211  1.00 85.37  ? 962  HOH B O   1 
HETATM 8505 O O   . HOH J 4 .   ? -6.946  66.710  19.863  1.00 63.15  ? 963  HOH B O   1 
HETATM 8506 O O   . HOH J 4 .   ? 0.762   50.049  2.486   1.00 60.59  ? 964  HOH B O   1 
HETATM 8507 O O   . HOH J 4 .   ? 15.732  33.535  0.855   1.00 44.61  ? 965  HOH B O   1 
HETATM 8508 O O   . HOH J 4 .   ? -15.329 47.284  22.588  1.00 50.51  ? 966  HOH B O   1 
HETATM 8509 O O   . HOH J 4 .   ? 3.648   38.497  24.482  1.00 40.21  ? 967  HOH B O   1 
HETATM 8510 O O   . HOH J 4 .   ? -7.269  60.624  29.144  1.00 68.43  ? 968  HOH B O   1 
HETATM 8511 O O   . HOH J 4 .   ? 5.578   67.497  42.801  1.00 73.75  ? 969  HOH B O   1 
HETATM 8512 O O   . HOH J 4 .   ? -3.039  59.933  9.372   1.00 66.21  ? 970  HOH B O   1 
HETATM 8513 O O   . HOH J 4 .   ? -24.557 39.346  -1.348  0.88 68.92  ? 971  HOH B O   1 
HETATM 8514 O O   . HOH J 4 .   ? 4.383   48.055  2.552   1.00 44.64  ? 972  HOH B O   1 
HETATM 8515 O O   . HOH J 4 .   ? 9.251   76.937  25.094  1.00 60.02  ? 973  HOH B O   1 
HETATM 8516 O O   . HOH J 4 .   ? 14.072  36.991  19.544  1.00 52.68  ? 974  HOH B O   1 
HETATM 8517 O O   . HOH J 4 .   ? 9.759   62.910  18.514  1.00 40.60  ? 975  HOH B O   1 
HETATM 8518 O O   . HOH J 4 .   ? 7.662   82.302  40.235  0.85 61.90  ? 976  HOH B O   1 
HETATM 8519 O O   . HOH J 4 .   ? -8.966  51.168  23.594  1.00 56.21  ? 977  HOH B O   1 
HETATM 8520 O O   . HOH J 4 .   ? 3.061   30.811  -7.140  1.00 69.73  ? 978  HOH B O   1 
HETATM 8521 O O   . HOH J 4 .   ? 2.888   42.989  32.647  1.00 52.50  ? 979  HOH B O   1 
HETATM 8522 O O   . HOH J 4 .   ? -11.089 34.016  15.799  1.00 65.08  ? 980  HOH B O   1 
HETATM 8523 O O   . HOH J 4 .   ? -5.292  48.717  2.335   1.00 52.08  ? 981  HOH B O   1 
HETATM 8524 O O   . HOH J 4 .   ? 6.148   51.905  2.238   1.00 65.12  ? 982  HOH B O   1 
HETATM 8525 O O   . HOH J 4 .   ? -14.332 52.152  -0.979  1.00 62.01  ? 983  HOH B O   1 
HETATM 8526 O O   . HOH J 4 .   ? -8.757  79.448  24.490  1.00 68.33  ? 984  HOH B O   1 
HETATM 8527 O O   . HOH J 4 .   ? 1.910   76.991  14.764  1.00 67.49  ? 985  HOH B O   1 
HETATM 8528 O O   . HOH J 4 .   ? 7.098   37.714  -7.251  1.00 47.05  ? 986  HOH B O   1 
HETATM 8529 O O   . HOH J 4 .   ? -6.582  48.759  33.049  1.00 58.87  ? 987  HOH B O   1 
HETATM 8530 O O   A HOH J 4 .   ? -6.914  33.932  14.566  0.55 48.74  ? 988  HOH B O   1 
HETATM 8531 O O   B HOH J 4 .   ? -5.573  33.634  14.416  0.45 46.86  ? 988  HOH B O   1 
HETATM 8532 O O   . HOH J 4 .   ? 3.539   76.120  39.151  1.00 57.31  ? 989  HOH B O   1 
HETATM 8533 O O   . HOH J 4 .   ? 18.499  57.900  10.713  1.00 43.28  ? 990  HOH B O   1 
HETATM 8534 O O   . HOH J 4 .   ? -9.647  34.101  13.072  1.00 69.76  ? 991  HOH B O   1 
HETATM 8535 O O   . HOH J 4 .   ? -4.152  33.517  23.547  1.00 47.67  ? 992  HOH B O   1 
HETATM 8536 O O   . HOH J 4 .   ? -22.541 37.608  -6.704  1.00 74.89  ? 993  HOH B O   1 
HETATM 8537 O O   . HOH J 4 .   ? -18.577 81.148  31.934  1.00 73.55  ? 994  HOH B O   1 
HETATM 8538 O O   . HOH J 4 .   ? 18.395  33.590  3.537   1.00 62.48  ? 995  HOH B O   1 
HETATM 8539 O O   . HOH J 4 .   ? 11.084  35.011  9.340   1.00 45.28  ? 996  HOH B O   1 
HETATM 8540 O O   A HOH J 4 .   ? -5.221  68.943  16.530  0.63 51.86  ? 997  HOH B O   1 
HETATM 8541 O O   B HOH J 4 .   ? -5.455  69.811  14.420  0.37 52.27  ? 997  HOH B O   1 
HETATM 8542 O O   . HOH J 4 .   ? 19.797  35.046  10.096  1.00 50.84  ? 998  HOH B O   1 
HETATM 8543 O O   . HOH J 4 .   ? 23.741  40.337  9.734   1.00 55.82  ? 999  HOH B O   1 
HETATM 8544 O O   . HOH J 4 .   ? 1.529   44.949  33.853  1.00 57.35  ? 1000 HOH B O   1 
HETATM 8545 O O   . HOH J 4 .   ? 1.600   34.165  -5.110  1.00 62.31  ? 1001 HOH B O   1 
HETATM 8546 O O   . HOH J 4 .   ? 1.423   60.908  9.899   1.00 57.56  ? 1002 HOH B O   1 
HETATM 8547 O O   . HOH J 4 .   ? 20.371  73.705  -4.227  1.00 62.53  ? 1003 HOH B O   1 
HETATM 8548 O O   . HOH J 4 .   ? 3.904   33.259  18.568  0.93 74.95  ? 1004 HOH B O   1 
HETATM 8549 O O   A HOH J 4 .   ? 8.687   39.119  25.043  0.49 41.09  ? 1005 HOH B O   1 
HETATM 8550 O O   B HOH J 4 .   ? 10.050  40.031  26.351  0.51 42.74  ? 1005 HOH B O   1 
HETATM 8551 O O   . HOH J 4 .   ? 20.403  49.964  -9.638  1.00 66.69  ? 1006 HOH B O   1 
HETATM 8552 O O   . HOH J 4 .   ? 6.604   55.417  5.710   1.00 65.78  ? 1007 HOH B O   1 
HETATM 8553 O O   . HOH J 4 .   ? 0.212   32.944  -2.683  1.00 57.78  ? 1008 HOH B O   1 
HETATM 8554 O O   . HOH J 4 .   ? -5.035  73.472  18.336  1.00 67.67  ? 1009 HOH B O   1 
HETATM 8555 O O   . HOH J 4 .   ? -12.840 43.336  26.568  1.00 57.07  ? 1010 HOH B O   1 
HETATM 8556 O O   . HOH J 4 .   ? 6.413   38.341  23.820  1.00 40.12  ? 1011 HOH B O   1 
HETATM 8557 O O   . HOH J 4 .   ? -9.068  61.624  19.189  1.00 63.89  ? 1012 HOH B O   1 
HETATM 8558 O O   . HOH J 4 .   ? -5.767  60.223  26.881  1.00 52.64  ? 1013 HOH B O   1 
HETATM 8559 O O   . HOH J 4 .   ? 5.852   35.352  20.129  0.73 58.23  ? 1014 HOH B O   1 
HETATM 8560 O O   . HOH J 4 .   ? -5.286  67.771  22.058  1.00 68.32  ? 1015 HOH B O   1 
HETATM 8561 O O   . HOH J 4 .   ? 14.921  32.693  11.967  1.00 69.79  ? 1016 HOH B O   1 
HETATM 8562 O O   . HOH J 4 .   ? -16.590 36.050  23.266  1.00 71.57  ? 1017 HOH B O   1 
HETATM 8563 O O   . HOH J 4 .   ? -7.786  49.720  4.606   1.00 59.50  ? 1018 HOH B O   1 
HETATM 8564 O O   . HOH J 4 .   ? -9.095  35.720  1.813   1.00 55.03  ? 1019 HOH B O   1 
HETATM 8565 O O   . HOH J 4 .   ? -17.300 38.760  26.624  1.00 58.77  ? 1020 HOH B O   1 
HETATM 8566 O O   A HOH J 4 .   ? -2.585  40.221  -12.330 0.47 59.51  ? 1021 HOH B O   1 
HETATM 8567 O O   B HOH J 4 .   ? -3.299  40.781  -11.369 0.53 58.77  ? 1021 HOH B O   1 
HETATM 8568 O O   . HOH J 4 .   ? -0.204  49.704  29.523  1.00 48.65  ? 1022 HOH B O   1 
HETATM 8569 O O   . HOH J 4 .   ? 12.788  34.265  12.042  1.00 64.98  ? 1023 HOH B O   1 
HETATM 8570 O O   . HOH J 4 .   ? -1.579  31.734  -4.588  1.00 67.42  ? 1024 HOH B O   1 
HETATM 8571 O O   . HOH J 4 .   ? 1.876   47.796  2.011   1.00 46.82  ? 1025 HOH B O   1 
HETATM 8572 O O   . HOH J 4 .   ? 8.502   82.091  37.061  1.00 66.10  ? 1026 HOH B O   1 
HETATM 8573 O O   . HOH J 4 .   ? -9.318  38.261  -9.948  1.00 65.90  ? 1027 HOH B O   1 
HETATM 8574 O O   . HOH J 4 .   ? 15.909  41.904  22.541  1.00 48.28  ? 1028 HOH B O   1 
HETATM 8575 O O   . HOH J 4 .   ? -15.411 45.702  24.760  1.00 58.50  ? 1029 HOH B O   1 
HETATM 8576 O O   . HOH J 4 .   ? 2.524   58.472  11.330  1.00 54.47  ? 1030 HOH B O   1 
HETATM 8577 O O   . HOH J 4 .   ? -8.518  34.226  17.799  1.00 69.19  ? 1031 HOH B O   1 
HETATM 8578 O O   . HOH J 4 .   ? -1.243  69.533  24.068  1.00 54.78  ? 1032 HOH B O   1 
HETATM 8579 O O   . HOH J 4 .   ? 6.322   33.161  15.301  1.00 69.36  ? 1033 HOH B O   1 
HETATM 8580 O O   . HOH J 4 .   ? 12.602  30.881  10.144  1.00 71.13  ? 1034 HOH B O   1 
HETATM 8581 O O   . HOH J 4 .   ? 8.780   33.992  -5.526  0.95 61.43  ? 1035 HOH B O   1 
HETATM 8582 O O   . HOH J 4 .   ? 22.273  58.582  3.867   1.00 45.47  ? 1036 HOH B O   1 
HETATM 8583 O O   . HOH J 4 .   ? 10.199  37.301  22.192  1.00 54.64  ? 1037 HOH B O   1 
HETATM 8584 O O   . HOH J 4 .   ? -16.790 50.824  -2.066  1.00 61.43  ? 1038 HOH B O   1 
HETATM 8585 O O   . HOH J 4 .   ? -11.346 49.845  20.700  1.00 55.17  ? 1039 HOH B O   1 
HETATM 8586 O O   . HOH J 4 .   ? -9.097  40.663  -10.223 1.00 62.74  ? 1040 HOH B O   1 
HETATM 8587 O O   . HOH J 4 .   ? -19.599 44.306  19.669  1.00 59.42  ? 1041 HOH B O   1 
HETATM 8588 O O   . HOH J 4 .   ? 15.403  45.491  25.074  1.00 52.74  ? 1042 HOH B O   1 
HETATM 8589 O O   A HOH J 4 .   ? -5.861  31.760  1.226   0.51 54.61  ? 1043 HOH B O   1 
HETATM 8590 O O   B HOH J 4 .   ? -5.204  32.567  2.515   0.49 51.13  ? 1043 HOH B O   1 
HETATM 8591 O O   . HOH J 4 .   ? -8.117  59.122  19.458  1.00 73.32  ? 1044 HOH B O   1 
HETATM 8592 O O   . HOH J 4 .   ? 2.290   31.476  -0.241  1.00 79.95  ? 1045 HOH B O   1 
HETATM 8593 O O   . HOH J 4 .   ? -3.943  44.848  -9.342  1.00 62.53  ? 1046 HOH B O   1 
HETATM 8594 O O   . HOH J 4 .   ? -5.133  47.740  -10.310 1.00 64.34  ? 1047 HOH B O   1 
HETATM 8595 O O   . HOH J 4 .   ? -8.837  54.383  23.580  1.00 78.58  ? 1048 HOH B O   1 
HETATM 8596 O O   . HOH J 4 .   ? 20.025  49.368  26.780  1.00 59.01  ? 1049 HOH B O   1 
HETATM 8597 O O   . HOH J 4 .   ? 24.610  43.347  17.260  1.00 49.58  ? 1050 HOH B O   1 
HETATM 8598 O O   . HOH J 4 .   ? -13.607 49.153  22.778  1.00 59.92  ? 1051 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ARG A 3   ? 1.6663 1.6412 1.1761 -0.1017 0.1349  -0.3552 98   ARG A N   
2    C CA  . ARG A 3   ? 1.6258 1.6002 1.1656 -0.0987 0.1324  -0.3546 98   ARG A CA  
3    C C   . ARG A 3   ? 1.6797 1.6640 1.2318 -0.0925 0.1336  -0.3393 98   ARG A C   
4    O O   . ARG A 3   ? 1.6615 1.6458 1.2208 -0.0855 0.1462  -0.3345 98   ARG A O   
5    C CB  . ARG A 3   ? 1.5787 1.5398 1.1421 -0.0941 0.1448  -0.3662 98   ARG A CB  
6    N N   . GLU A 4   ? 1.6732 1.6665 1.2284 -0.0952 0.1200  -0.3319 99   GLU A N   
7    C CA  . GLU A 4   ? 1.6076 1.6098 1.1807 -0.0876 0.1163  -0.3117 99   GLU A CA  
8    C C   . GLU A 4   ? 1.5776 1.5804 1.1824 -0.0843 0.1068  -0.3049 99   GLU A C   
9    O O   . GLU A 4   ? 1.5610 1.5694 1.1851 -0.0773 0.1052  -0.2896 99   GLU A O   
10   C CB  . GLU A 4   ? 1.6848 1.6983 1.2332 -0.0908 0.1058  -0.2989 99   GLU A CB  
11   C CG  . GLU A 4   ? 1.7140 1.7363 1.2757 -0.0836 0.1029  -0.2783 99   GLU A CG  
12   C CD  . GLU A 4   ? 1.7457 1.7783 1.2885 -0.0872 0.0875  -0.2657 99   GLU A CD  
13   O OE1 . GLU A 4   ? 1.7337 1.7714 1.2887 -0.0880 0.0727  -0.2597 99   GLU A OE1 
14   O OE2 . GLU A 4   ? 1.7618 1.7972 1.2776 -0.0895 0.0901  -0.2619 99   GLU A OE2 
15   N N   . ASN A 5   ? 1.5277 1.5245 1.1382 -0.0895 0.1009  -0.3162 100  ASN A N   
16   C CA  . ASN A 5   ? 1.4904 1.4868 1.1314 -0.0869 0.0933  -0.3106 100  ASN A CA  
17   C C   . ASN A 5   ? 1.4010 1.3903 1.0709 -0.0774 0.1052  -0.3082 100  ASN A C   
18   O O   . ASN A 5   ? 1.3666 1.3575 1.0619 -0.0730 0.1002  -0.2981 100  ASN A O   
19   C CB  . ASN A 5   ? 1.5049 1.4948 1.1454 -0.0952 0.0865  -0.3250 100  ASN A CB  
20   N N   . LEU A 6   ? 1.4230 1.4047 1.0895 -0.0743 0.1210  -0.3172 101  LEU A N   
21   C CA  . LEU A 6   ? 1.3345 1.3111 1.0280 -0.0645 0.1321  -0.3137 101  LEU A CA  
22   C C   . LEU A 6   ? 1.2686 1.2560 0.9729 -0.0575 0.1297  -0.2941 101  LEU A C   
23   O O   . LEU A 6   ? 1.1778 1.1646 0.9090 -0.0510 0.1290  -0.2854 101  LEU A O   
24   C CB  . LEU A 6   ? 1.2315 1.2001 0.9175 -0.0625 0.1493  -0.3270 101  LEU A CB  
25   N N   . LYS A 7   ? 1.2888 1.2857 0.9715 -0.0592 0.1282  -0.2868 102  LYS A N   
26   C CA  . LYS A 7   ? 1.2278 1.2345 0.9188 -0.0533 0.1258  -0.2686 102  LYS A CA  
27   C C   . LYS A 7   ? 1.2069 1.2197 0.9110 -0.0533 0.1105  -0.2563 102  LYS A C   
28   O O   . LYS A 7   ? 1.1377 1.1544 0.8617 -0.0467 0.1094  -0.2433 102  LYS A O   
29   C CB  . LYS A 7   ? 1.2577 1.2716 0.9207 -0.0560 0.1276  -0.2641 102  LYS A CB  
30   N N   . ASN A 8   ? 1.2475 1.2616 0.9410 -0.0606 0.0986  -0.2604 103  ASN A N   
31   C CA  . ASN A 8   ? 1.2228 1.2435 0.9302 -0.0607 0.0845  -0.2494 103  ASN A CA  
32   C C   . ASN A 8   ? 1.1323 1.1463 0.8698 -0.0573 0.0853  -0.2507 103  ASN A C   
33   O O   . ASN A 8   ? 1.0987 1.1176 0.8548 -0.0535 0.0790  -0.2383 103  ASN A O   
34   C CB  . ASN A 8   ? 1.3546 1.3803 1.0430 -0.0697 0.0711  -0.2533 103  ASN A CB  
35   C CG  . ASN A 8   ? 1.4236 1.4601 1.0900 -0.0710 0.0639  -0.2425 103  ASN A CG  
36   O OD1 . ASN A 8   ? 1.4230 1.4598 1.0738 -0.0692 0.0723  -0.2405 103  ASN A OD1 
37   N ND2 . ASN A 8   ? 1.4822 1.5278 1.1483 -0.0739 0.0485  -0.2351 103  ASN A ND2 
38   N N   . GLU A 9   ? 1.1157 1.1176 0.8580 -0.0584 0.0935  -0.2652 104  GLU A N   
39   C CA  . GLU A 9   ? 1.1281 1.1218 0.8989 -0.0543 0.0960  -0.2655 104  GLU A CA  
40   C C   . GLU A 9   ? 1.0361 1.0302 0.8251 -0.0442 0.1042  -0.2551 104  GLU A C   
41   O O   . GLU A 9   ? 0.9701 0.9640 0.7816 -0.0397 0.1011  -0.2459 104  GLU A O   
42   C CB  . GLU A 9   ? 1.1766 1.1561 0.9476 -0.0576 0.1034  -0.2838 104  GLU A CB  
43   C CG  . GLU A 9   ? 1.2686 1.2413 1.0550 -0.0619 0.0965  -0.2884 104  GLU A CG  
44   C CD  . GLU A 9   ? 1.3001 1.2826 1.0775 -0.0702 0.0810  -0.2858 104  GLU A CD  
45   O OE1 . GLU A 9   ? 1.2844 1.2685 1.0800 -0.0709 0.0732  -0.2797 104  GLU A OE1 
46   O OE2 . GLU A 9   ? 1.3123 1.3012 1.0645 -0.0759 0.0766  -0.2898 104  GLU A OE2 
47   N N   . ALA A 10  ? 1.0271 1.0224 0.8062 -0.0408 0.1144  -0.2560 105  ALA A N   
48   C CA  . ALA A 10  ? 0.9864 0.9841 0.7816 -0.0317 0.1214  -0.2457 105  ALA A CA  
49   C C   . ALA A 10  ? 0.9086 0.9173 0.7090 -0.0295 0.1120  -0.2281 105  ALA A C   
50   O O   . ALA A 10  ? 0.9177 0.9271 0.7395 -0.0231 0.1123  -0.2186 105  ALA A O   
51   C CB  . ALA A 10  ? 0.9759 0.9746 0.7580 -0.0298 0.1339  -0.2502 105  ALA A CB  
52   N N   . THR A 11  ? 0.9178 0.9351 0.6984 -0.0346 0.1034  -0.2236 106  THR A N   
53   C CA  . THR A 11  ? 0.9247 0.9519 0.7102 -0.0326 0.0938  -0.2074 106  THR A CA  
54   C C   . THR A 11  ? 0.9084 0.9349 0.7147 -0.0323 0.0851  -0.2032 106  THR A C   
55   O O   . THR A 11  ? 0.8575 0.8878 0.6801 -0.0270 0.0828  -0.1911 106  THR A O   
56   C CB  . THR A 11  ? 0.9592 0.9946 0.7193 -0.0383 0.0855  -0.2042 106  THR A CB  
57   O OG1 . THR A 11  ? 0.9809 1.0172 0.7224 -0.0381 0.0945  -0.2057 106  THR A OG1 
58   C CG2 . THR A 11  ? 0.9271 0.9720 0.6937 -0.0360 0.0751  -0.1879 106  THR A CG2 
59   N N   . LYS A 12  ? 0.8881 0.9095 0.6939 -0.0381 0.0807  -0.2134 107  LYS A N   
60   C CA  . LYS A 12  ? 0.8807 0.9001 0.7076 -0.0381 0.0745  -0.2106 107  LYS A CA  
61   C C   . LYS A 12  ? 0.8197 0.8321 0.6698 -0.0304 0.0825  -0.2069 107  LYS A C   
62   O O   . LYS A 12  ? 0.7882 0.8028 0.6556 -0.0274 0.0781  -0.1969 107  LYS A O   
63   C CB  . LYS A 12  ? 0.8696 0.8824 0.6935 -0.0459 0.0711  -0.2244 107  LYS A CB  
64   N N   . VAL A 13  ? 0.8110 0.8152 0.6617 -0.0271 0.0942  -0.2148 108  VAL A N   
65   C CA  . VAL A 13  ? 0.7896 0.7871 0.6626 -0.0194 0.1013  -0.2115 108  VAL A CA  
66   C C   . VAL A 13  ? 0.7627 0.7688 0.6431 -0.0128 0.1015  -0.1967 108  VAL A C   
67   O O   . VAL A 13  ? 0.7304 0.7357 0.6295 -0.0082 0.0998  -0.1880 108  VAL A O   
68   C CB  . VAL A 13  ? 0.8331 0.8203 0.7060 -0.0171 0.1138  -0.2241 108  VAL A CB  
69   C CG1 . VAL A 13  ? 0.7524 0.7348 0.6479 -0.0080 0.1207  -0.2189 108  VAL A CG1 
70   C CG2 . VAL A 13  ? 0.8104 0.7867 0.6799 -0.0234 0.1137  -0.2389 108  VAL A CG2 
71   N N   . LEU A 14  ? 0.7724 0.7862 0.6377 -0.0125 0.1037  -0.1936 109  LEU A N   
72   C CA  . LEU A 14  ? 0.7321 0.7537 0.6039 -0.0068 0.1042  -0.1800 109  LEU A CA  
73   C C   . LEU A 14  ? 0.7580 0.7859 0.6368 -0.0070 0.0932  -0.1678 109  LEU A C   
74   O O   . LEU A 14  ? 0.6917 0.7223 0.5843 -0.0015 0.0932  -0.1574 109  LEU A O   
75   C CB  . LEU A 14  ? 0.7408 0.7691 0.5931 -0.0078 0.1079  -0.1789 109  LEU A CB  
76   C CG  . LEU A 14  ? 0.7887 0.8122 0.6340 -0.0073 0.1204  -0.1905 109  LEU A CG  
77   C CD1 . LEU A 14  ? 0.7879 0.8183 0.6128 -0.0090 0.1244  -0.1884 109  LEU A CD1 
78   C CD2 . LEU A 14  ? 0.7352 0.7544 0.6029 0.0004  0.1288  -0.1900 109  LEU A CD2 
79   N N   . GLU A 15  ? 0.7412 0.7720 0.6112 -0.0132 0.0838  -0.1692 110  GLU A N   
80   C CA  . GLU A 15  ? 0.7648 0.8030 0.6407 -0.0136 0.0734  -0.1581 110  GLU A CA  
81   C C   . GLU A 15  ? 0.7135 0.7472 0.6070 -0.0146 0.0692  -0.1589 110  GLU A C   
82   O O   . GLU A 15  ? 0.7316 0.7715 0.6305 -0.0159 0.0606  -0.1515 110  GLU A O   
83   C CB  . GLU A 15  ? 0.8107 0.8569 0.6670 -0.0193 0.0647  -0.1574 110  GLU A CB  
84   C CG  . GLU A 15  ? 0.8763 0.9273 0.7141 -0.0184 0.0681  -0.1538 110  GLU A CG  
85   C CD  . GLU A 15  ? 1.0125 1.0698 0.8285 -0.0244 0.0596  -0.1542 110  GLU A CD  
86   O OE1 . GLU A 15  ? 1.0741 1.1316 0.8878 -0.0298 0.0524  -0.1606 110  GLU A OE1 
87   O OE2 . GLU A 15  ? 1.0405 1.1025 0.8416 -0.0238 0.0600  -0.1480 110  GLU A OE2 
88   N N   . HIS A 16  ? 0.7136 0.7363 0.6168 -0.0137 0.0757  -0.1672 111  HIS A N   
89   C CA  . HIS A 16  ? 0.7223 0.7389 0.6390 -0.0165 0.0721  -0.1700 111  HIS A CA  
90   C C   . HIS A 16  ? 0.7210 0.7415 0.6542 -0.0134 0.0674  -0.1575 111  HIS A C   
91   O O   . HIS A 16  ? 0.6867 0.7065 0.6300 -0.0068 0.0715  -0.1497 111  HIS A O   
92   C CB  . HIS A 16  ? 0.6993 0.7021 0.6249 -0.0146 0.0809  -0.1794 111  HIS A CB  
93   C CG  . HIS A 16  ? 0.7318 0.7268 0.6723 -0.0171 0.0783  -0.1812 111  HIS A CG  
94   N ND1 . HIS A 16  ? 0.7333 0.7275 0.6698 -0.0254 0.0722  -0.1887 111  HIS A ND1 
95   C CD2 . HIS A 16  ? 0.7455 0.7332 0.7045 -0.0130 0.0806  -0.1761 111  HIS A CD2 
96   C CE1 . HIS A 16  ? 0.7839 0.7703 0.7365 -0.0264 0.0716  -0.1883 111  HIS A CE1 
97   N NE2 . HIS A 16  ? 0.7516 0.7336 0.7173 -0.0189 0.0767  -0.1804 111  HIS A NE2 
98   N N   . VAL A 17  ? 0.7696 0.7946 0.7056 -0.0185 0.0587  -0.1562 112  VAL A N   
99   C CA  . VAL A 17  ? 0.7323 0.7605 0.6841 -0.0169 0.0544  -0.1460 112  VAL A CA  
100  C C   . VAL A 17  ? 0.7377 0.7550 0.7040 -0.0189 0.0565  -0.1508 112  VAL A C   
101  O O   . VAL A 17  ? 0.7915 0.8046 0.7553 -0.0254 0.0547  -0.1609 112  VAL A O   
102  C CB  . VAL A 17  ? 0.7750 0.8159 0.7230 -0.0210 0.0439  -0.1412 112  VAL A CB  
103  C CG1 . VAL A 17  ? 0.7351 0.7786 0.7009 -0.0206 0.0400  -0.1331 112  VAL A CG1 
104  C CG2 . VAL A 17  ? 0.7128 0.7631 0.6481 -0.0177 0.0421  -0.1338 112  VAL A CG2 
105  N N   . CYS A 18  ? 0.7247 0.7367 0.7053 -0.0135 0.0604  -0.1438 113  CYS A N   
106  C CA  . CYS A 18  ? 0.7767 0.7773 0.7712 -0.0149 0.0628  -0.1463 113  CYS A CA  
107  C C   . CYS A 18  ? 0.8601 0.8661 0.8636 -0.0196 0.0559  -0.1416 113  CYS A C   
108  O O   . CYS A 18  ? 0.8595 0.8749 0.8667 -0.0172 0.0523  -0.1311 113  CYS A O   
109  C CB  . CYS A 18  ? 0.7609 0.7537 0.7660 -0.0069 0.0694  -0.1399 113  CYS A CB  
110  S SG  . CYS A 18  ? 0.8384 0.8176 0.8615 -0.0072 0.0716  -0.1378 113  CYS A SG  
111  N N   . GLU A 19  ? 0.9441 0.9442 0.9517 -0.0266 0.0543  -0.1496 114  GLU A N   
112  C CA  . GLU A 19  ? 0.9620 0.9676 0.9798 -0.0320 0.0484  -0.1462 114  GLU A CA  
113  C C   . GLU A 19  ? 0.9610 0.9554 0.9947 -0.0315 0.0526  -0.1427 114  GLU A C   
114  O O   . GLU A 19  ? 1.0226 1.0222 1.0664 -0.0344 0.0491  -0.1369 114  GLU A O   
115  C CB  . GLU A 19  ? 0.9925 1.0013 1.0053 -0.0414 0.0426  -0.1570 114  GLU A CB  
116  C CG  . GLU A 19  ? 1.0430 1.0636 1.0385 -0.0429 0.0370  -0.1601 114  GLU A CG  
117  C CD  . GLU A 19  ? 1.0907 1.1275 1.0860 -0.0406 0.0301  -0.1491 114  GLU A CD  
118  O OE1 . GLU A 19  ? 1.0908 1.1308 1.0996 -0.0382 0.0296  -0.1396 114  GLU A OE1 
119  O OE2 . GLU A 19  ? 1.1107 1.1567 1.0916 -0.0411 0.0253  -0.1498 114  GLU A OE2 
120  N N   . ASP A 20  ? 0.8848 0.8642 0.9211 -0.0278 0.0601  -0.1455 115  ASP A N   
121  C CA  . ASP A 20  ? 0.8749 0.8419 0.9249 -0.0269 0.0642  -0.1413 115  ASP A CA  
122  C C   . ASP A 20  ? 0.8514 0.8079 0.9022 -0.0181 0.0713  -0.1388 115  ASP A C   
123  O O   . ASP A 20  ? 0.8502 0.7966 0.8975 -0.0172 0.0758  -0.1478 115  ASP A O   
124  C CB  . ASP A 20  ? 0.8996 0.8558 0.9548 -0.0352 0.0647  -0.1512 115  ASP A CB  
125  C CG  . ASP A 20  ? 0.9337 0.8789 1.0033 -0.0361 0.0677  -0.1454 115  ASP A CG  
126  O OD1 . ASP A 20  ? 0.9140 0.8535 0.9881 -0.0288 0.0718  -0.1363 115  ASP A OD1 
127  O OD2 . ASP A 20  ? 1.0158 0.9580 1.0918 -0.0445 0.0660  -0.1499 115  ASP A OD2 
128  N N   . ILE A 21  ? 0.8305 0.7895 0.8861 -0.0116 0.0722  -0.1269 116  ILE A N   
129  C CA  . ILE A 21  ? 0.8164 0.7673 0.8739 -0.0030 0.0780  -0.1239 116  ILE A CA  
130  C C   . ILE A 21  ? 0.8427 0.7752 0.9097 -0.0022 0.0828  -0.1254 116  ILE A C   
131  O O   . ILE A 21  ? 0.8111 0.7355 0.8811 0.0051  0.0875  -0.1239 116  ILE A O   
132  C CB  . ILE A 21  ? 0.8216 0.7807 0.8809 0.0035  0.0771  -0.1111 116  ILE A CB  
133  C CG1 . ILE A 21  ? 0.8554 0.8081 0.9251 0.0040  0.0775  -0.1022 116  ILE A CG1 
134  C CG2 . ILE A 21  ? 0.8239 0.8001 0.8759 0.0017  0.0715  -0.1078 116  ILE A CG2 
135  C CD1 . ILE A 21  ? 0.8671 0.8278 0.9374 0.0095  0.0763  -0.0903 116  ILE A CD1 
136  N N   . ASN A 22  ? 0.8500 0.7758 0.9228 -0.0095 0.0818  -0.1282 117  ASN A N   
137  C CA  . ASN A 22  ? 0.8709 0.7774 0.9519 -0.0096 0.0867  -0.1308 117  ASN A CA  
138  C C   . ASN A 22  ? 0.8479 0.7445 0.9252 -0.0118 0.0900  -0.1450 117  ASN A C   
139  O O   . ASN A 22  ? 0.8619 0.7421 0.9446 -0.0080 0.0955  -0.1476 117  ASN A O   
140  C CB  . ASN A 22  ? 0.8697 0.7721 0.9590 -0.0172 0.0850  -0.1278 117  ASN A CB  
141  C CG  . ASN A 22  ? 0.9313 0.8428 1.0241 -0.0155 0.0826  -0.1143 117  ASN A CG  
142  O OD1 . ASN A 22  ? 0.9666 0.8733 1.0622 -0.0085 0.0850  -0.1050 117  ASN A OD1 
143  N ND2 . ASN A 22  ? 0.9029 0.8278 0.9959 -0.0219 0.0777  -0.1135 117  ASN A ND2 
144  N N   . LYS A 23  ? 0.8071 0.7130 0.8748 -0.0174 0.0869  -0.1543 118  LYS A N   
145  C CA  . LYS A 23  ? 0.8449 0.7422 0.9068 -0.0203 0.0900  -0.1689 118  LYS A CA  
146  C C   . LYS A 23  ? 0.8530 0.7555 0.9048 -0.0142 0.0930  -0.1732 118  LYS A C   
147  O O   . LYS A 23  ? 0.8327 0.7267 0.8801 -0.0150 0.0974  -0.1852 118  LYS A O   
148  C CB  . LYS A 23  ? 0.8885 0.7919 0.9451 -0.0316 0.0846  -0.1780 118  LYS A CB  
149  C CG  . LYS A 23  ? 0.9123 0.8178 0.9787 -0.0386 0.0802  -0.1725 118  LYS A CG  
150  C CD  . LYS A 23  ? 1.0146 0.9064 1.0861 -0.0476 0.0814  -0.1830 118  LYS A CD  
151  C CE  . LYS A 23  ? 1.0702 0.9701 1.1490 -0.0570 0.0755  -0.1805 118  LYS A CE  
152  N NZ  . LYS A 23  ? 1.0320 0.9504 1.1021 -0.0633 0.0675  -0.1859 118  LYS A NZ  
153  N N   . GLU A 24  ? 0.8151 0.7311 0.8635 -0.0085 0.0913  -0.1640 119  GLU A N   
154  C CA  . GLU A 24  ? 0.7768 0.7002 0.8149 -0.0039 0.0938  -0.1674 119  GLU A CA  
155  C C   . GLU A 24  ? 0.7429 0.6660 0.7876 0.0064  0.0977  -0.1583 119  GLU A C   
156  O O   . GLU A 24  ? 0.7298 0.6506 0.7844 0.0098  0.0967  -0.1477 119  GLU A O   
157  C CB  . GLU A 24  ? 0.7673 0.7086 0.7932 -0.0079 0.0873  -0.1658 119  GLU A CB  
158  C CG  . GLU A 24  ? 0.8360 0.7790 0.8542 -0.0181 0.0827  -0.1760 119  GLU A CG  
159  C CD  . GLU A 24  ? 0.8680 0.8285 0.8734 -0.0214 0.0758  -0.1743 119  GLU A CD  
160  O OE1 . GLU A 24  ? 0.8734 0.8408 0.8794 -0.0282 0.0687  -0.1737 119  GLU A OE1 
161  O OE2 . GLU A 24  ? 0.8631 0.8305 0.8585 -0.0171 0.0776  -0.1733 119  GLU A OE2 
162  N N   . SER A 25  ? 0.7040 0.6300 0.7429 0.0113  0.1024  -0.1628 120  SER A N   
163  C CA  . SER A 25  ? 0.6668 0.5952 0.7120 0.0208  0.1057  -0.1549 120  SER A CA  
164  C C   . SER A 25  ? 0.6391 0.5839 0.6752 0.0229  0.1044  -0.1505 120  SER A C   
165  O O   . SER A 25  ? 0.6390 0.5876 0.6808 0.0302  0.1065  -0.1434 120  SER A O   
166  C CB  . SER A 25  ? 0.7023 0.6187 0.7537 0.0267  0.1138  -0.1625 120  SER A CB  
167  O OG  . SER A 25  ? 0.7900 0.6903 0.8537 0.0281  0.1153  -0.1616 120  SER A OG  
168  N N   . TYR A 26  ? 0.6107 0.5652 0.6331 0.0168  0.1008  -0.1543 121  TYR A N   
169  C CA  . TYR A 26  ? 0.6154 0.5843 0.6287 0.0186  0.0997  -0.1493 121  TYR A CA  
170  C C   . TYR A 26  ? 0.6232 0.6020 0.6240 0.0113  0.0926  -0.1493 121  TYR A C   
171  O O   . TYR A 26  ? 0.6819 0.6573 0.6791 0.0045  0.0897  -0.1564 121  TYR A O   
172  C CB  . TYR A 26  ? 0.6158 0.5852 0.6229 0.0218  0.1072  -0.1572 121  TYR A CB  
173  C CG  . TYR A 26  ? 0.5960 0.5621 0.5901 0.0155  0.1090  -0.1709 121  TYR A CG  
174  C CD1 . TYR A 26  ? 0.6619 0.6137 0.6604 0.0141  0.1131  -0.1815 121  TYR A CD1 
175  C CD2 . TYR A 26  ? 0.5981 0.5745 0.5746 0.0107  0.1065  -0.1732 121  TYR A CD2 
176  C CE1 . TYR A 26  ? 0.6842 0.6325 0.6698 0.0078  0.1147  -0.1950 121  TYR A CE1 
177  C CE2 . TYR A 26  ? 0.6590 0.6323 0.6217 0.0045  0.1077  -0.1861 121  TYR A CE2 
178  C CZ  . TYR A 26  ? 0.6940 0.6535 0.6614 0.0029  0.1118  -0.1973 121  TYR A CZ  
179  O OH  . TYR A 26  ? 0.7103 0.6664 0.6634 -0.0037 0.1131  -0.2108 121  TYR A OH  
180  N N   . GLY A 27  ? 0.6209 0.6121 0.6155 0.0127  0.0898  -0.1416 122  GLY A N   
181  C CA  . GLY A 27  ? 0.5964 0.5979 0.5787 0.0069  0.0830  -0.1407 122  GLY A CA  
182  C C   . GLY A 27  ? 0.5959 0.6079 0.5802 0.0092  0.0781  -0.1278 122  GLY A C   
183  O O   . GLY A 27  ? 0.5762 0.5871 0.5718 0.0141  0.0790  -0.1194 122  GLY A O   
184  N N   . PHE A 28  ? 0.6070 0.6290 0.5792 0.0057  0.0727  -0.1260 123  PHE A N   
185  C CA  . PHE A 28  ? 0.6124 0.6438 0.5865 0.0069  0.0670  -0.1146 123  PHE A CA  
186  C C   . PHE A 28  ? 0.6322 0.6631 0.6166 0.0036  0.0615  -0.1122 123  PHE A C   
187  O O   . PHE A 28  ? 0.7014 0.7298 0.6847 -0.0022 0.0588  -0.1197 123  PHE A O   
188  C CB  . PHE A 28  ? 0.6251 0.6663 0.5834 0.0044  0.0629  -0.1135 123  PHE A CB  
189  C CG  . PHE A 28  ? 0.6210 0.6626 0.5680 0.0065  0.0691  -0.1165 123  PHE A CG  
190  C CD1 . PHE A 28  ? 0.6063 0.6506 0.5562 0.0120  0.0730  -0.1091 123  PHE A CD1 
191  C CD2 . PHE A 28  ? 0.6517 0.6909 0.5852 0.0026  0.0714  -0.1271 123  PHE A CD2 
192  C CE1 . PHE A 28  ? 0.6014 0.6466 0.5420 0.0135  0.0795  -0.1119 123  PHE A CE1 
193  C CE2 . PHE A 28  ? 0.6545 0.6941 0.5777 0.0043  0.0783  -0.1301 123  PHE A CE2 
194  C CZ  . PHE A 28  ? 0.6349 0.6778 0.5622 0.0098  0.0825  -0.1224 123  PHE A CZ  
195  N N   . VAL A 29  ? 0.5994 0.6321 0.5944 0.0070  0.0605  -0.1024 124  VAL A N   
196  C CA  . VAL A 29  ? 0.6630 0.6948 0.6690 0.0043  0.0567  -0.0994 124  VAL A CA  
197  C C   . VAL A 29  ? 0.6632 0.7052 0.6716 0.0058  0.0520  -0.0892 124  VAL A C   
198  O O   . VAL A 29  ? 0.6797 0.7252 0.6859 0.0106  0.0534  -0.0825 124  VAL A O   
199  C CB  . VAL A 29  ? 0.6655 0.6859 0.6842 0.0070  0.0616  -0.0983 124  VAL A CB  
200  C CG1 . VAL A 29  ? 0.6895 0.6987 0.7079 0.0053  0.0660  -0.1088 124  VAL A CG1 
201  C CG2 . VAL A 29  ? 0.6663 0.6863 0.6882 0.0143  0.0654  -0.0906 124  VAL A CG2 
202  N N   . LYS A 30  ? 0.7252 0.7720 0.7388 0.0014  0.0465  -0.0883 125  LYS A N   
203  C CA  . LYS A 30  ? 0.7208 0.7752 0.7409 0.0031  0.0432  -0.0787 125  LYS A CA  
204  C C   . LYS A 30  ? 0.6988 0.7462 0.7307 0.0059  0.0475  -0.0736 125  LYS A C   
205  O O   . LYS A 30  ? 0.7025 0.7400 0.7399 0.0044  0.0508  -0.0776 125  LYS A O   
206  C CB  . LYS A 30  ? 0.7800 0.8430 0.8034 -0.0024 0.0361  -0.0797 125  LYS A CB  
207  C CG  . LYS A 30  ? 0.8067 0.8784 0.8178 -0.0049 0.0302  -0.0828 125  LYS A CG  
208  C CD  . LYS A 30  ? 0.9058 0.9888 0.9227 -0.0085 0.0222  -0.0808 125  LYS A CD  
209  C CE  . LYS A 30  ? 0.9211 1.0145 0.9302 -0.0057 0.0170  -0.0744 125  LYS A CE  
210  N NZ  . LYS A 30  ? 0.9759 1.0732 0.9697 -0.0088 0.0121  -0.0799 125  LYS A NZ  
211  N N   . ILE A 31  ? 0.6971 0.7489 0.7318 0.0100  0.0474  -0.0645 126  ILE A N   
212  C CA  . ILE A 31  ? 0.7120 0.7581 0.7562 0.0125  0.0508  -0.0587 126  ILE A CA  
213  C C   . ILE A 31  ? 0.7542 0.7976 0.8083 0.0075  0.0501  -0.0601 126  ILE A C   
214  O O   . ILE A 31  ? 0.7625 0.7964 0.8229 0.0079  0.0541  -0.0588 126  ILE A O   
215  C CB  . ILE A 31  ? 0.7354 0.7881 0.7798 0.0166  0.0500  -0.0496 126  ILE A CB  
216  C CG1 . ILE A 31  ? 0.7263 0.7790 0.7630 0.0215  0.0523  -0.0480 126  ILE A CG1 
217  C CG2 . ILE A 31  ? 0.6432 0.6915 0.6965 0.0180  0.0527  -0.0437 126  ILE A CG2 
218  C CD1 . ILE A 31  ? 0.6405 0.6835 0.6796 0.0249  0.0575  -0.0485 126  ILE A CD1 
219  N N   . SER A 32  ? 0.7462 0.7979 0.8020 0.0025  0.0451  -0.0626 127  SER A N   
220  C CA  . SER A 32  ? 0.8084 0.8593 0.8750 -0.0029 0.0445  -0.0639 127  SER A CA  
221  C C   . SER A 32  ? 0.8359 0.8746 0.9043 -0.0066 0.0476  -0.0714 127  SER A C   
222  O O   . SER A 32  ? 0.8725 0.9052 0.9502 -0.0099 0.0498  -0.0708 127  SER A O   
223  C CB  . SER A 32  ? 0.7850 0.8490 0.8538 -0.0074 0.0377  -0.0657 127  SER A CB  
224  O OG  . SER A 32  ? 0.8233 0.8895 0.8829 -0.0101 0.0339  -0.0734 127  SER A OG  
225  N N   . LYS A 33  ? 0.8332 0.8673 0.8929 -0.0063 0.0483  -0.0784 128  LYS A N   
226  C CA  . LYS A 33  ? 0.8497 0.8717 0.9110 -0.0098 0.0513  -0.0866 128  LYS A CA  
227  C C   . LYS A 33  ? 0.8585 0.8667 0.9217 -0.0047 0.0579  -0.0846 128  LYS A C   
228  O O   . LYS A 33  ? 0.8898 0.8862 0.9552 -0.0067 0.0610  -0.0909 128  LYS A O   
229  C CB  . LYS A 33  ? 0.8717 0.8953 0.9225 -0.0126 0.0491  -0.0965 128  LYS A CB  
230  C CG  . LYS A 33  ? 0.8816 0.9180 0.9302 -0.0183 0.0416  -0.0993 128  LYS A CG  
231  C CD  . LYS A 33  ? 0.9615 0.9955 1.0014 -0.0235 0.0398  -0.1112 128  LYS A CD  
232  C CE  . LYS A 33  ? 0.9965 1.0360 1.0426 -0.0321 0.0340  -0.1164 128  LYS A CE  
233  N NZ  . LYS A 33  ? 1.0040 1.0340 1.0467 -0.0381 0.0352  -0.1289 128  LYS A NZ  
234  N N   . MET A 34  ? 0.8511 0.8604 0.9142 0.0018  0.0598  -0.0761 129  MET A N   
235  C CA  . MET A 34  ? 0.8429 0.8404 0.9083 0.0072  0.0650  -0.0734 129  MET A CA  
236  C C   . MET A 34  ? 0.9096 0.8981 0.9844 0.0057  0.0672  -0.0686 129  MET A C   
237  O O   . MET A 34  ? 0.9177 0.9045 0.9948 0.0098  0.0687  -0.0600 129  MET A O   
238  C CB  . MET A 34  ? 0.7727 0.7756 0.8339 0.0142  0.0656  -0.0667 129  MET A CB  
239  C CG  . MET A 34  ? 0.6920 0.7011 0.7436 0.0163  0.0651  -0.0711 129  MET A CG  
240  S SD  . MET A 34  ? 0.8600 0.8580 0.9098 0.0182  0.0702  -0.0805 129  MET A SD  
241  C CE  . MET A 34  ? 0.6602 0.6514 0.7164 0.0264  0.0743  -0.0732 129  MET A CE  
242  N N   . LYS A 35  ? 0.9963 0.9785 1.0759 -0.0007 0.0674  -0.0743 130  LYS A N   
243  C CA  . LYS A 35  ? 1.0647 1.0367 1.1529 -0.0034 0.0702  -0.0706 130  LYS A CA  
244  C C   . LYS A 35  ? 1.0527 1.0080 1.1430 -0.0038 0.0741  -0.0767 130  LYS A C   
245  O O   . LYS A 35  ? 1.0467 0.9991 1.1371 -0.0094 0.0735  -0.0863 130  LYS A O   
246  C CB  . LYS A 35  ? 1.0950 1.0742 1.1892 -0.0115 0.0675  -0.0715 130  LYS A CB  
247  C CG  . LYS A 35  ? 1.0567 1.0504 1.1519 -0.0107 0.0647  -0.0641 130  LYS A CG  
248  C CD  . LYS A 35  ? 1.1493 1.1380 1.2493 -0.0090 0.0684  -0.0545 130  LYS A CD  
249  N N   . GLU A 36  ? 1.0754 1.0193 1.1674 0.0021  0.0777  -0.0712 131  GLU A N   
250  C CA  . GLU A 36  ? 1.0889 1.0156 1.1840 0.0032  0.0817  -0.0758 131  GLU A CA  
251  C C   . GLU A 36  ? 1.1917 1.1058 1.2942 -0.0013 0.0841  -0.0721 131  GLU A C   
252  O O   . GLU A 36  ? 1.2273 1.1397 1.3317 0.0008  0.0850  -0.0618 131  GLU A O   
253  C CB  . GLU A 36  ? 0.9724 0.8944 1.0661 0.0129  0.0839  -0.0718 131  GLU A CB  
254  C CG  . GLU A 36  ? 0.9982 0.9051 1.0945 0.0157  0.0879  -0.0787 131  GLU A CG  
255  C CD  . GLU A 36  ? 0.9116 0.8136 1.0097 0.0257  0.0898  -0.0731 131  GLU A CD  
256  O OE1 . GLU A 36  ? 0.9821 0.8871 1.0805 0.0294  0.0885  -0.0624 131  GLU A OE1 
257  O OE2 . GLU A 36  ? 0.8254 0.7207 0.9249 0.0298  0.0927  -0.0796 131  GLU A OE2 
258  N N   . ASN A 37  ? 1.1973 1.1023 1.3034 -0.0079 0.0854  -0.0806 132  ASN A N   
259  C CA  . ASN A 37  ? 1.2526 1.1454 1.3662 -0.0140 0.0880  -0.0782 132  ASN A CA  
260  C C   . ASN A 37  ? 1.3574 1.2619 1.4740 -0.0192 0.0861  -0.0717 132  ASN A C   
261  O O   . ASN A 37  ? 1.3698 1.2669 1.4905 -0.0206 0.0889  -0.0638 132  ASN A O   
262  C CB  . ASN A 37  ? 1.2814 1.1562 1.3975 -0.0081 0.0922  -0.0710 132  ASN A CB  
263  N N   . GLU A 38  ? 1.3766 1.2994 1.4908 -0.0217 0.0816  -0.0749 133  GLU A N   
264  C CA  . GLU A 38  ? 1.3853 1.3217 1.5035 -0.0265 0.0793  -0.0706 133  GLU A CA  
265  C C   . GLU A 38  ? 1.3944 1.3345 1.5113 -0.0212 0.0806  -0.0584 133  GLU A C   
266  O O   . GLU A 38  ? 1.3782 1.3311 1.4978 -0.0236 0.0791  -0.0544 133  GLU A O   
267  C CB  . GLU A 38  ? 1.4165 1.3468 1.5442 -0.0364 0.0812  -0.0733 133  GLU A CB  
268  N N   . LYS A 39  ? 1.3801 1.3096 1.4931 -0.0138 0.0832  -0.0526 134  LYS A N   
269  C CA  . LYS A 39  ? 1.3745 1.3061 1.4848 -0.0087 0.0842  -0.0415 134  LYS A CA  
270  C C   . LYS A 39  ? 1.3561 1.2977 1.4592 -0.0009 0.0813  -0.0403 134  LYS A C   
271  O O   . LYS A 39  ? 1.3466 1.2960 1.4468 -0.0004 0.0785  -0.0475 134  LYS A O   
272  C CB  . LYS A 39  ? 1.3906 1.3036 1.5016 -0.0062 0.0884  -0.0350 134  LYS A CB  
273  N N   . GLU A 40  ? 1.3294 1.2708 1.4290 0.0049  0.0820  -0.0312 135  GLU A N   
274  C CA  . GLU A 40  ? 1.2340 1.1853 1.3275 0.0116  0.0794  -0.0293 135  GLU A CA  
275  C C   . GLU A 40  ? 1.1740 1.1166 1.2653 0.0186  0.0802  -0.0302 135  GLU A C   
276  O O   . GLU A 40  ? 1.1602 1.0881 1.2541 0.0200  0.0827  -0.0283 135  GLU A O   
277  C CB  . GLU A 40  ? 1.2226 1.1798 1.3133 0.0137  0.0795  -0.0198 135  GLU A CB  
278  C CG  . GLU A 40  ? 1.2139 1.1837 1.2991 0.0188  0.0766  -0.0186 135  GLU A CG  
279  C CD  . GLU A 40  ? 1.2683 1.2449 1.3512 0.0196  0.0766  -0.0109 135  GLU A CD  
280  O OE1 . GLU A 40  ? 1.2265 1.2121 1.3049 0.0236  0.0746  -0.0093 135  GLU A OE1 
281  O OE2 . GLU A 40  ? 1.3314 1.3040 1.4167 0.0160  0.0792  -0.0066 135  GLU A OE2 
282  N N   . ILE A 41  ? 1.0123 0.9642 1.0995 0.0229  0.0781  -0.0329 136  ILE A N   
283  C CA  . ILE A 41  ? 0.8568 0.8042 0.9429 0.0300  0.0788  -0.0337 136  ILE A CA  
284  C C   . ILE A 41  ? 0.8074 0.7577 0.8910 0.0358  0.0779  -0.0244 136  ILE A C   
285  O O   . ILE A 41  ? 0.8538 0.8153 0.9338 0.0354  0.0760  -0.0208 136  ILE A O   
286  C CB  . ILE A 41  ? 0.8018 0.7581 0.8845 0.0307  0.0778  -0.0420 136  ILE A CB  
287  C CG1 . ILE A 41  ? 0.8407 0.7918 0.9249 0.0256  0.0788  -0.0522 136  ILE A CG1 
288  C CG2 . ILE A 41  ? 0.7328 0.6892 0.8148 0.0385  0.0786  -0.0414 136  ILE A CG2 
289  C CD1 . ILE A 41  ? 0.7625 0.7239 0.8409 0.0246  0.0774  -0.0602 136  ILE A CD1 
290  N N   . ARG A 42  ? 0.7193 0.6596 0.8050 0.0413  0.0789  -0.0206 137  ARG A N   
291  C CA  . ARG A 42  ? 0.7113 0.6549 0.7946 0.0473  0.0772  -0.0127 137  ARG A CA  
292  C C   . ARG A 42  ? 0.6956 0.6485 0.7784 0.0522  0.0761  -0.0165 137  ARG A C   
293  O O   . ARG A 42  ? 0.6635 0.6115 0.7504 0.0570  0.0772  -0.0193 137  ARG A O   
294  C CB  . ARG A 42  ? 0.7437 0.6733 0.8297 0.0512  0.0778  -0.0062 137  ARG A CB  
295  C CG  . ARG A 42  ? 0.8012 0.7344 0.8833 0.0560  0.0752  0.0030  137  ARG A CG  
296  C CD  . ARG A 42  ? 0.8819 0.8013 0.9656 0.0602  0.0750  0.0103  137  ARG A CD  
297  N NE  . ARG A 42  ? 0.9616 0.8860 1.0416 0.0653  0.0715  0.0178  137  ARG A NE  
298  C CZ  . ARG A 42  ? 0.9863 0.9017 1.0665 0.0702  0.0696  0.0253  137  ARG A CZ  
299  N NH1 . ARG A 42  ? 0.9968 0.8965 1.0806 0.0710  0.0712  0.0272  137  ARG A NH1 
300  N NH2 . ARG A 42  ? 0.9906 0.9127 1.0672 0.0744  0.0658  0.0311  137  ARG A NH2 
301  N N   . LEU A 43  ? 0.6950 0.6613 0.7731 0.0512  0.0744  -0.0163 138  LEU A N   
302  C CA  . LEU A 43  ? 0.6342 0.6101 0.7109 0.0541  0.0740  -0.0204 138  LEU A CA  
303  C C   . LEU A 43  ? 0.6581 0.6388 0.7344 0.0596  0.0722  -0.0142 138  LEU A C   
304  O O   . LEU A 43  ? 0.6718 0.6564 0.7444 0.0588  0.0704  -0.0079 138  LEU A O   
305  C CB  . LEU A 43  ? 0.6075 0.5945 0.6791 0.0495  0.0729  -0.0238 138  LEU A CB  
306  C CG  . LEU A 43  ? 0.5713 0.5681 0.6398 0.0514  0.0729  -0.0280 138  LEU A CG  
307  C CD1 . LEU A 43  ? 0.5257 0.5179 0.5966 0.0529  0.0757  -0.0362 138  LEU A CD1 
308  C CD2 . LEU A 43  ? 0.4943 0.5010 0.5570 0.0471  0.0711  -0.0293 138  LEU A CD2 
309  N N   . PHE A 44  ? 0.5953 0.5764 0.6758 0.0649  0.0729  -0.0164 139  PHE A N   
310  C CA  . PHE A 44  ? 0.5966 0.5840 0.6782 0.0699  0.0710  -0.0117 139  PHE A CA  
311  C C   . PHE A 44  ? 0.5721 0.5722 0.6511 0.0697  0.0713  -0.0154 139  PHE A C   
312  O O   . PHE A 44  ? 0.5502 0.5530 0.6275 0.0673  0.0735  -0.0224 139  PHE A O   
313  C CB  . PHE A 44  ? 0.5903 0.5712 0.6801 0.0764  0.0714  -0.0114 139  PHE A CB  
314  C CG  . PHE A 44  ? 0.6654 0.6333 0.7572 0.0777  0.0704  -0.0055 139  PHE A CG  
315  C CD1 . PHE A 44  ? 0.7084 0.6757 0.7988 0.0805  0.0669  0.0035  139  PHE A CD1 
316  C CD2 . PHE A 44  ? 0.6352 0.5908 0.7296 0.0759  0.0730  -0.0088 139  PHE A CD2 
317  C CE1 . PHE A 44  ? 0.7640 0.7185 0.8548 0.0817  0.0660  0.0097  139  PHE A CE1 
318  C CE2 . PHE A 44  ? 0.7306 0.6731 0.8265 0.0769  0.0724  -0.0028 139  PHE A CE2 
319  C CZ  . PHE A 44  ? 0.7753 0.7171 0.8689 0.0799  0.0690  0.0069  139  PHE A CZ  
320  N N   . ASN A 45  ? 0.5746 0.5821 0.6525 0.0718  0.0691  -0.0106 140  ASN A N   
321  C CA  . ASN A 45  ? 0.6017 0.6203 0.6790 0.0725  0.0698  -0.0133 140  ASN A CA  
322  C C   . ASN A 45  ? 0.5677 0.5886 0.6531 0.0784  0.0694  -0.0124 140  ASN A C   
323  O O   . ASN A 45  ? 0.5343 0.5491 0.6245 0.0821  0.0675  -0.0082 140  ASN A O   
324  C CB  . ASN A 45  ? 0.5824 0.6085 0.6527 0.0695  0.0677  -0.0093 140  ASN A CB  
325  C CG  . ASN A 45  ? 0.5977 0.6233 0.6676 0.0713  0.0645  -0.0018 140  ASN A CG  
326  O OD1 . ASN A 45  ? 0.5983 0.6268 0.6725 0.0751  0.0630  0.0002  140  ASN A OD1 
327  N ND2 . ASN A 45  ? 0.6431 0.6655 0.7076 0.0682  0.0634  0.0023  140  ASN A ND2 
328  N N   . LEU A 46  ? 0.5265 0.5566 0.6137 0.0792  0.0714  -0.0162 141  LEU A N   
329  C CA  . LEU A 46  ? 0.5554 0.5893 0.6525 0.0848  0.0717  -0.0166 141  LEU A CA  
330  C C   . LEU A 46  ? 0.5724 0.6101 0.6719 0.0873  0.0669  -0.0092 141  LEU A C   
331  O O   . LEU A 46  ? 0.5559 0.5946 0.6649 0.0926  0.0655  -0.0079 141  LEU A O   
332  C CB  . LEU A 46  ? 0.4993 0.5427 0.5976 0.0842  0.0757  -0.0227 141  LEU A CB  
333  C CG  . LEU A 46  ? 0.5529 0.5928 0.6505 0.0831  0.0809  -0.0311 141  LEU A CG  
334  C CD1 . LEU A 46  ? 0.5320 0.5816 0.6300 0.0826  0.0853  -0.0365 141  LEU A CD1 
335  C CD2 . LEU A 46  ? 0.5572 0.5879 0.6644 0.0880  0.0821  -0.0333 141  LEU A CD2 
336  N N   . GLU A 47  ? 0.5214 0.5615 0.6124 0.0836  0.0643  -0.0048 142  GLU A N   
337  C CA  . GLU A 47  ? 0.5968 0.6398 0.6883 0.0853  0.0596  0.0017  142  GLU A CA  
338  C C   . GLU A 47  ? 0.5575 0.5907 0.6501 0.0883  0.0564  0.0072  142  GLU A C   
339  O O   . GLU A 47  ? 0.5462 0.5809 0.6445 0.0927  0.0527  0.0111  142  GLU A O   
340  C CB  . GLU A 47  ? 0.5472 0.5939 0.6287 0.0805  0.0585  0.0043  142  GLU A CB  
341  C CG  . GLU A 47  ? 0.5902 0.6380 0.6691 0.0811  0.0537  0.0107  142  GLU A CG  
342  C CD  . GLU A 47  ? 0.5878 0.6397 0.6580 0.0765  0.0534  0.0120  142  GLU A CD  
343  O OE1 . GLU A 47  ? 0.5832 0.6329 0.6473 0.0730  0.0558  0.0105  142  GLU A OE1 
344  O OE2 . GLU A 47  ? 0.6528 0.7101 0.7226 0.0766  0.0507  0.0142  142  GLU A OE2 
345  N N   . GLU A 48  ? 0.5639 0.5872 0.6516 0.0859  0.0577  0.0077  143  GLU A N   
346  C CA  . GLU A 48  ? 0.5902 0.6025 0.6786 0.0883  0.0556  0.0130  143  GLU A CA  
347  C C   . GLU A 48  ? 0.6152 0.6238 0.7150 0.0946  0.0558  0.0114  143  GLU A C   
348  O O   . GLU A 48  ? 0.6159 0.6204 0.7191 0.0990  0.0520  0.0172  143  GLU A O   
349  C CB  . GLU A 48  ? 0.6176 0.6202 0.7001 0.0839  0.0581  0.0126  143  GLU A CB  
350  C CG  . GLU A 48  ? 0.6520 0.6590 0.7256 0.0780  0.0587  0.0128  143  GLU A CG  
351  C CD  . GLU A 48  ? 0.7482 0.7474 0.8186 0.0735  0.0613  0.0115  143  GLU A CD  
352  O OE1 . GLU A 48  ? 0.7951 0.7877 0.8611 0.0717  0.0607  0.0169  143  GLU A OE1 
353  O OE2 . GLU A 48  ? 0.7617 0.7615 0.8338 0.0714  0.0640  0.0050  143  GLU A OE2 
354  N N   . ILE A 49  ? 0.5965 0.6061 0.7019 0.0951  0.0602  0.0037  144  ILE A N   
355  C CA  . ILE A 49  ? 0.6220 0.6281 0.7394 0.1014  0.0613  0.0012  144  ILE A CA  
356  C C   . ILE A 49  ? 0.6045 0.6206 0.7306 0.1067  0.0579  0.0038  144  ILE A C   
357  O O   . ILE A 49  ? 0.5985 0.6105 0.7328 0.1128  0.0548  0.0077  144  ILE A O   
358  C CB  . ILE A 49  ? 0.5791 0.5857 0.6997 0.1003  0.0674  -0.0087 144  ILE A CB  
359  C CG1 . ILE A 49  ? 0.5861 0.5819 0.6997 0.0953  0.0700  -0.0114 144  ILE A CG1 
360  C CG2 . ILE A 49  ? 0.5757 0.5809 0.7101 0.1074  0.0693  -0.0122 144  ILE A CG2 
361  C CD1 . ILE A 49  ? 0.6051 0.6025 0.7179 0.0925  0.0753  -0.0214 144  ILE A CD1 
362  N N   . TYR A 50  ? 0.5658 0.5949 0.6907 0.1044  0.0581  0.0018  145  TYR A N   
363  C CA  . TYR A 50  ? 0.6032 0.6432 0.7372 0.1086  0.0547  0.0038  145  TYR A CA  
364  C C   . TYR A 50  ? 0.6491 0.6861 0.7812 0.1110  0.0474  0.0129  145  TYR A C   
365  O O   . TYR A 50  ? 0.6427 0.6816 0.7854 0.1173  0.0437  0.0158  145  TYR A O   
366  C CB  . TYR A 50  ? 0.5936 0.6466 0.7244 0.1043  0.0560  0.0011  145  TYR A CB  
367  C CG  . TYR A 50  ? 0.6340 0.6992 0.7742 0.1073  0.0522  0.0030  145  TYR A CG  
368  C CD1 . TYR A 50  ? 0.5806 0.6543 0.7352 0.1114  0.0550  -0.0018 145  TYR A CD1 
369  C CD2 . TYR A 50  ? 0.6467 0.7150 0.7817 0.1060  0.0460  0.0094  145  TYR A CD2 
370  C CE1 . TYR A 50  ? 0.6096 0.6956 0.7746 0.1139  0.0514  -0.0003 145  TYR A CE1 
371  C CE2 . TYR A 50  ? 0.6490 0.7289 0.7929 0.1082  0.0420  0.0108  145  TYR A CE2 
372  C CZ  . TYR A 50  ? 0.6743 0.7635 0.8339 0.1122  0.0445  0.0061  145  TYR A CZ  
373  O OH  . TYR A 50  ? 0.6080 0.7099 0.7780 0.1141  0.0403  0.0073  145  TYR A OH  
374  N N   . HIS A 51  ? 0.6359 0.6684 0.7547 0.1063  0.0453  0.0176  146  HIS A N   
375  C CA  . HIS A 51  ? 0.6755 0.7061 0.7902 0.1079  0.0386  0.0261  146  HIS A CA  
376  C C   . HIS A 51  ? 0.6669 0.6843 0.7839 0.1125  0.0365  0.0312  146  HIS A C   
377  O O   . HIS A 51  ? 0.7247 0.7422 0.8452 0.1173  0.0305  0.0373  146  HIS A O   
378  C CB  . HIS A 51  ? 0.6646 0.6950 0.7644 0.1015  0.0377  0.0290  146  HIS A CB  
379  C CG  . HIS A 51  ? 0.7151 0.7586 0.8139 0.0986  0.0372  0.0266  146  HIS A CG  
380  N ND1 . HIS A 51  ? 0.7015 0.7493 0.7965 0.0937  0.0419  0.0213  146  HIS A ND1 
381  C CD2 . HIS A 51  ? 0.7399 0.7932 0.8423 0.0999  0.0323  0.0285  146  HIS A CD2 
382  C CE1 . HIS A 51  ? 0.7386 0.7971 0.8341 0.0920  0.0405  0.0204  146  HIS A CE1 
383  N NE2 . HIS A 51  ? 0.7739 0.8362 0.8741 0.0955  0.0348  0.0243  146  HIS A NE2 
384  N N   . SER A 52  ? 0.6845 0.6904 0.8000 0.1113  0.0411  0.0288  147  SER A N   
385  C CA  . SER A 52  ? 0.6853 0.6773 0.8040 0.1157  0.0398  0.0334  147  SER A CA  
386  C C   . SER A 52  ? 0.7122 0.7064 0.8473 0.1241  0.0385  0.0321  147  SER A C   
387  O O   . SER A 52  ? 0.7436 0.7306 0.8825 0.1297  0.0339  0.0388  147  SER A O   
388  C CB  . SER A 52  ? 0.7061 0.6855 0.8210 0.1120  0.0455  0.0300  147  SER A CB  
389  O OG  . SER A 52  ? 0.7685 0.7456 0.8700 0.1049  0.0464  0.0323  147  SER A OG  
390  N N   . LEU A 53  ? 0.7025 0.7062 0.8474 0.1252  0.0426  0.0236  148  LEU A N   
391  C CA  . LEU A 53  ? 0.6829 0.6875 0.8448 0.1332  0.0432  0.0209  148  LEU A CA  
392  C C   . LEU A 53  ? 0.6998 0.7206 0.8732 0.1377  0.0391  0.0215  148  LEU A C   
393  O O   . LEU A 53  ? 0.7181 0.7394 0.9061 0.1457  0.0370  0.0224  148  LEU A O   
394  C CB  . LEU A 53  ? 0.6961 0.6994 0.8632 0.1323  0.0516  0.0102  148  LEU A CB  
395  C CG  . LEU A 53  ? 0.7387 0.7267 0.8985 0.1283  0.0565  0.0072  148  LEU A CG  
396  C CD1 . LEU A 53  ? 0.7220 0.7101 0.8889 0.1288  0.0640  -0.0038 148  LEU A CD1 
397  C CD2 . LEU A 53  ? 0.7752 0.7467 0.9357 0.1321  0.0536  0.0143  148  LEU A CD2 
398  N N   . MET A 54  ? 0.6823 0.7162 0.8506 0.1331  0.0379  0.0207  149  MET A N   
399  C CA  . MET A 54  ? 0.7450 0.7954 0.9264 0.1365  0.0353  0.0193  149  MET A CA  
400  C C   . MET A 54  ? 0.7198 0.7763 0.8978 0.1369  0.0260  0.0275  149  MET A C   
401  O O   . MET A 54  ? 0.8205 0.8729 0.9827 0.1315  0.0234  0.0319  149  MET A O   
402  C CB  . MET A 54  ? 0.7135 0.7757 0.8946 0.1312  0.0415  0.0111  149  MET A CB  
403  C CG  . MET A 54  ? 0.6559 0.7138 0.8394 0.1304  0.0507  0.0022  149  MET A CG  
404  S SD  . MET A 54  ? 0.7720 0.8284 0.9767 0.1400  0.0541  -0.0026 149  MET A SD  
405  C CE  . MET A 54  ? 0.7051 0.7820 0.9273 0.1445  0.0503  -0.0020 149  MET A CE  
406  N N   . HIS A 84  ? 1.0955 0.9805 1.2248 0.1197  0.0566  0.0383  179  HIS A N   
407  C CA  . HIS A 84  ? 1.1437 1.0252 1.2660 0.1104  0.0619  0.0325  179  HIS A CA  
408  C C   . HIS A 84  ? 1.1296 1.0218 1.2564 0.1082  0.0661  0.0197  179  HIS A C   
409  O O   . HIS A 84  ? 1.0872 0.9732 1.2139 0.1031  0.0710  0.0124  179  HIS A O   
410  C CB  . HIS A 84  ? 1.1574 1.0441 1.2658 0.1034  0.0603  0.0384  179  HIS A CB  
411  C CG  . HIS A 84  ? 1.1768 1.0826 1.2817 0.1034  0.0571  0.0379  179  HIS A CG  
412  N ND1 . HIS A 84  ? 1.1692 1.0834 1.2783 0.1103  0.0520  0.0417  179  HIS A ND1 
413  C CD2 . HIS A 84  ? 1.1359 1.0537 1.2338 0.0971  0.0584  0.0342  179  HIS A CD2 
414  C CE1 . HIS A 84  ? 1.1422 1.0721 1.2468 0.1078  0.0505  0.0400  179  HIS A CE1 
415  N NE2 . HIS A 84  ? 1.1115 1.0434 1.2091 0.1001  0.0544  0.0357  179  HIS A NE2 
416  N N   . LEU A 85  ? 1.0220 0.9306 1.1522 0.1116  0.0643  0.0172  180  LEU A N   
417  C CA  . LEU A 85  ? 0.9349 0.8536 1.0690 0.1103  0.0684  0.0058  180  LEU A CA  
418  C C   . LEU A 85  ? 0.9204 0.8326 1.0672 0.1163  0.0720  -0.0011 180  LEU A C   
419  O O   . LEU A 85  ? 0.8583 0.7749 1.0070 0.1142  0.0768  -0.0116 180  LEU A O   
420  C CB  . LEU A 85  ? 0.8742 0.8120 1.0080 0.1117  0.0657  0.0058  180  LEU A CB  
421  C CG  . LEU A 85  ? 0.8725 0.8194 0.9941 0.1051  0.0636  0.0092  180  LEU A CG  
422  C CD1 . LEU A 85  ? 0.7904 0.7535 0.9135 0.1078  0.0603  0.0106  180  LEU A CD1 
423  C CD2 . LEU A 85  ? 0.8107 0.7599 0.9263 0.0976  0.0679  0.0014  180  LEU A CD2 
424  N N   . LEU A 86  ? 0.9084 0.8100 1.0636 0.1237  0.0699  0.0045  181  LEU A N   
425  C CA  . LEU A 86  ? 0.9157 0.8114 1.0849 0.1309  0.0733  -0.0017 181  LEU A CA  
426  C C   . LEU A 86  ? 0.9179 0.7921 1.0893 0.1303  0.0769  -0.0034 181  LEU A C   
427  O O   . LEU A 86  ? 0.9339 0.8011 1.1165 0.1357  0.0808  -0.0099 181  LEU A O   
428  C CB  . LEU A 86  ? 0.8754 0.7754 1.0558 0.1412  0.0682  0.0053  181  LEU A CB  
429  C CG  . LEU A 86  ? 0.8789 0.8003 1.0593 0.1421  0.0642  0.0069  181  LEU A CG  
430  C CD1 . LEU A 86  ? 0.8296 0.7546 1.0216 0.1519  0.0582  0.0144  181  LEU A CD1 
431  C CD2 . LEU A 86  ? 0.8433 0.7782 1.0272 0.1402  0.0699  -0.0050 181  LEU A CD2 
432  N N   . GLN A 87  ? 0.9178 0.7811 1.0790 0.1237  0.0764  0.0018  182  GLN A N   
433  C CA  . GLN A 87  ? 0.9563 0.7978 1.1199 0.1229  0.0795  0.0016  182  GLN A CA  
434  C C   . GLN A 87  ? 0.9384 0.7760 1.1018 0.1167  0.0862  -0.0119 182  GLN A C   
435  O O   . GLN A 87  ? 0.9544 0.7793 1.1266 0.1200  0.0903  -0.0181 182  GLN A O   
436  C CB  . GLN A 87  ? 0.9894 0.8208 1.1424 0.1176  0.0769  0.0124  182  GLN A CB  
437  N N   . SER A 88  ? 0.9201 0.7682 1.0737 0.1078  0.0871  -0.0166 183  SER A N   
438  C CA  . SER A 88  ? 0.8913 0.7359 1.0431 0.1008  0.0924  -0.0287 183  SER A CA  
439  C C   . SER A 88  ? 0.7990 0.6633 0.9452 0.0971  0.0929  -0.0361 183  SER A C   
440  O O   . SER A 88  ? 0.7599 0.6393 0.9056 0.1006  0.0900  -0.0325 183  SER A O   
441  C CB  . SER A 88  ? 0.9301 0.7628 1.0750 0.0919  0.0930  -0.0263 183  SER A CB  
442  O OG  . SER A 88  ? 0.9522 0.7782 1.0976 0.0860  0.0978  -0.0382 183  SER A OG  
443  N N   . ASP A 89  ? 0.7585 0.6222 0.9003 0.0898  0.0964  -0.0464 184  ASP A N   
444  C CA  . ASP A 89  ? 0.7426 0.6234 0.8771 0.0853  0.0967  -0.0529 184  ASP A CA  
445  C C   . ASP A 89  ? 0.7117 0.6042 0.8376 0.0808  0.0921  -0.0447 184  ASP A C   
446  O O   . ASP A 89  ? 0.7397 0.6256 0.8621 0.0764  0.0904  -0.0385 184  ASP A O   
447  C CB  . ASP A 89  ? 0.7237 0.6004 0.8542 0.0778  0.1004  -0.0648 184  ASP A CB  
448  C CG  . ASP A 89  ? 0.7605 0.6272 0.8983 0.0816  0.1059  -0.0752 184  ASP A CG  
449  O OD1 . ASP A 89  ? 0.7642 0.6320 0.9105 0.0905  0.1072  -0.0747 184  ASP A OD1 
450  O OD2 . ASP A 89  ? 0.8600 0.7180 0.9954 0.0756  0.1088  -0.0844 184  ASP A OD2 
451  N N   . ILE A 90  ? 0.6514 0.5608 0.7737 0.0817  0.0907  -0.0450 185  ILE A N   
452  C CA  . ILE A 90  ? 0.6600 0.5810 0.7741 0.0777  0.0868  -0.0386 185  ILE A CA  
453  C C   . ILE A 90  ? 0.6326 0.5664 0.7397 0.0725  0.0877  -0.0461 185  ILE A C   
454  O O   . ILE A 90  ? 0.6513 0.5869 0.7591 0.0730  0.0911  -0.0554 185  ILE A O   
455  C CB  . ILE A 90  ? 0.6920 0.6210 0.8080 0.0839  0.0832  -0.0296 185  ILE A CB  
456  C CG1 . ILE A 90  ? 0.6802 0.6200 0.8010 0.0891  0.0848  -0.0347 185  ILE A CG1 
457  C CG2 . ILE A 90  ? 0.7030 0.6192 0.8249 0.0893  0.0814  -0.0212 185  ILE A CG2 
458  C CD1 . ILE A 90  ? 0.6809 0.6331 0.8020 0.0928  0.0810  -0.0277 185  ILE A CD1 
459  N N   . TRP A 91  ? 0.5928 0.5351 0.6924 0.0676  0.0847  -0.0417 186  TRP A N   
460  C CA  . TRP A 91  ? 0.5948 0.5499 0.6870 0.0631  0.0843  -0.0464 186  TRP A CA  
461  C C   . TRP A 91  ? 0.5995 0.5677 0.6894 0.0661  0.0820  -0.0409 186  TRP A C   
462  O O   . TRP A 91  ? 0.5767 0.5455 0.6668 0.0678  0.0792  -0.0320 186  TRP A O   
463  C CB  . TRP A 91  ? 0.5687 0.5243 0.6556 0.0553  0.0825  -0.0460 186  TRP A CB  
464  C CG  . TRP A 91  ? 0.6535 0.5996 0.7413 0.0502  0.0846  -0.0539 186  TRP A CG  
465  C CD1 . TRP A 91  ? 0.6427 0.5746 0.7353 0.0484  0.0857  -0.0529 186  TRP A CD1 
466  C CD2 . TRP A 91  ? 0.6369 0.5869 0.7201 0.0456  0.0855  -0.0641 186  TRP A CD2 
467  N NE1 . TRP A 91  ? 0.6721 0.5989 0.7642 0.0429  0.0874  -0.0623 186  TRP A NE1 
468  C CE2 . TRP A 91  ? 0.6700 0.6080 0.7560 0.0410  0.0870  -0.0694 186  TRP A CE2 
469  C CE3 . TRP A 91  ? 0.6256 0.5875 0.7019 0.0447  0.0852  -0.0690 186  TRP A CE3 
470  C CZ2 . TRP A 91  ? 0.7003 0.6386 0.7823 0.0355  0.0878  -0.0801 186  TRP A CZ2 
471  C CZ3 . TRP A 91  ? 0.6191 0.5811 0.6904 0.0394  0.0860  -0.0790 186  TRP A CZ3 
472  C CH2 . TRP A 91  ? 0.6528 0.6033 0.7270 0.0348  0.0870  -0.0847 186  TRP A CH2 
473  N N   . VAL A 92  ? 0.5468 0.5248 0.6338 0.0664  0.0835  -0.0462 187  VAL A N   
474  C CA  . VAL A 92  ? 0.5214 0.5118 0.6063 0.0686  0.0819  -0.0419 187  VAL A CA  
475  C C   . VAL A 92  ? 0.5234 0.5236 0.5997 0.0640  0.0824  -0.0466 187  VAL A C   
476  O O   . VAL A 92  ? 0.5387 0.5377 0.6123 0.0618  0.0851  -0.0549 187  VAL A O   
477  C CB  . VAL A 92  ? 0.5279 0.5203 0.6211 0.0757  0.0837  -0.0422 187  VAL A CB  
478  C CG1 . VAL A 92  ? 0.5647 0.5559 0.6601 0.0766  0.0889  -0.0525 187  VAL A CG1 
479  C CG2 . VAL A 92  ? 0.5303 0.5355 0.6220 0.0771  0.0820  -0.0379 187  VAL A CG2 
480  N N   . ARG A 93  ? 0.4719 0.4811 0.5433 0.0626  0.0796  -0.0412 188  ARG A N   
481  C CA  . ARG A 93  ? 0.4832 0.5017 0.5461 0.0590  0.0795  -0.0438 188  ARG A CA  
482  C C   . ARG A 93  ? 0.5311 0.5583 0.5944 0.0622  0.0808  -0.0426 188  ARG A C   
483  O O   . ARG A 93  ? 0.5651 0.5936 0.6340 0.0662  0.0798  -0.0373 188  ARG A O   
484  C CB  . ARG A 93  ? 0.5008 0.5227 0.5584 0.0549  0.0756  -0.0387 188  ARG A CB  
485  C CG  . ARG A 93  ? 0.4909 0.5221 0.5400 0.0518  0.0747  -0.0399 188  ARG A CG  
486  C CD  . ARG A 93  ? 0.4918 0.5253 0.5375 0.0478  0.0710  -0.0364 188  ARG A CD  
487  N NE  . ARG A 93  ? 0.5027 0.5304 0.5498 0.0441  0.0703  -0.0402 188  ARG A NE  
488  C CZ  . ARG A 93  ? 0.5194 0.5480 0.5670 0.0406  0.0676  -0.0377 188  ARG A CZ  
489  N NH1 . ARG A 93  ? 0.4685 0.5031 0.5148 0.0407  0.0654  -0.0315 188  ARG A NH1 
490  N NH2 . ARG A 93  ? 0.4982 0.5218 0.5481 0.0367  0.0673  -0.0419 188  ARG A NH2 
491  N N   . GLY A 94  ? 0.4963 0.5296 0.5532 0.0602  0.0830  -0.0474 189  GLY A N   
492  C CA  . GLY A 94  ? 0.5011 0.5433 0.5577 0.0619  0.0844  -0.0455 189  GLY A CA  
493  C C   . GLY A 94  ? 0.5049 0.5525 0.5521 0.0587  0.0871  -0.0505 189  GLY A C   
494  O O   . GLY A 94  ? 0.4950 0.5399 0.5356 0.0552  0.0875  -0.0560 189  GLY A O   
495  N N   . ARG A 95  ? 0.4606 0.5160 0.5069 0.0595  0.0889  -0.0486 190  ARG A N   
496  C CA  . ARG A 95  ? 0.4982 0.5587 0.5349 0.0565  0.0921  -0.0525 190  ARG A CA  
497  C C   . ARG A 95  ? 0.4951 0.5565 0.5362 0.0588  0.0987  -0.0596 190  ARG A C   
498  O O   . ARG A 95  ? 0.4479 0.5104 0.5008 0.0634  0.1005  -0.0590 190  ARG A O   
499  C CB  . ARG A 95  ? 0.4672 0.5351 0.4997 0.0553  0.0911  -0.0466 190  ARG A CB  
500  C CG  . ARG A 95  ? 0.5267 0.5946 0.5498 0.0517  0.0863  -0.0424 190  ARG A CG  
501  C CD  . ARG A 95  ? 0.5060 0.5798 0.5237 0.0502  0.0862  -0.0373 190  ARG A CD  
502  N NE  . ARG A 95  ? 0.5234 0.5973 0.5314 0.0471  0.0821  -0.0343 190  ARG A NE  
503  C CZ  . ARG A 95  ? 0.5108 0.5870 0.5159 0.0464  0.0796  -0.0279 190  ARG A CZ  
504  N NH1 . ARG A 95  ? 0.4697 0.5481 0.4804 0.0480  0.0806  -0.0240 190  ARG A NH1 
505  N NH2 . ARG A 95  ? 0.5023 0.5788 0.4995 0.0440  0.0759  -0.0256 190  ARG A NH2 
506  N N   . ILE A 96  ? 0.4587 0.5198 0.4902 0.0557  0.1021  -0.0664 191  ILE A N   
507  C CA  . ILE A 96  ? 0.5004 0.5628 0.5347 0.0575  0.1096  -0.0740 191  ILE A CA  
508  C C   . ILE A 96  ? 0.5018 0.5735 0.5364 0.0577  0.1134  -0.0717 191  ILE A C   
509  O O   . ILE A 96  ? 0.4836 0.5592 0.5056 0.0535  0.1146  -0.0712 191  ILE A O   
510  C CB  . ILE A 96  ? 0.4984 0.5570 0.5207 0.0536  0.1124  -0.0827 191  ILE A CB  
511  C CG1 . ILE A 96  ? 0.5016 0.5505 0.5266 0.0534  0.1094  -0.0861 191  ILE A CG1 
512  C CG2 . ILE A 96  ? 0.4940 0.5548 0.5177 0.0550  0.1212  -0.0906 191  ILE A CG2 
513  C CD1 . ILE A 96  ? 0.5103 0.5555 0.5226 0.0486  0.1107  -0.0946 191  ILE A CD1 
514  N N   . HIS A 97  ? 0.4664 0.5416 0.5156 0.0624  0.1152  -0.0700 192  HIS A N   
515  C CA  . HIS A 97  ? 0.4829 0.5676 0.5357 0.0626  0.1192  -0.0683 192  HIS A CA  
516  C C   . HIS A 97  ? 0.5359 0.6237 0.5868 0.0620  0.1283  -0.0767 192  HIS A C   
517  O O   . HIS A 97  ? 0.5230 0.6172 0.5671 0.0588  0.1325  -0.0765 192  HIS A O   
518  C CB  . HIS A 97  ? 0.4759 0.5639 0.5462 0.0679  0.1172  -0.0642 192  HIS A CB  
519  C CG  . HIS A 97  ? 0.5417 0.6401 0.6177 0.0677  0.1199  -0.0616 192  HIS A CG  
520  N ND1 . HIS A 97  ? 0.5160 0.6181 0.5848 0.0638  0.1172  -0.0553 192  HIS A ND1 
521  C CD2 . HIS A 97  ? 0.4991 0.6052 0.5889 0.0709  0.1250  -0.0645 192  HIS A CD2 
522  C CE1 . HIS A 97  ? 0.5187 0.6300 0.5958 0.0640  0.1207  -0.0546 192  HIS A CE1 
523  N NE2 . HIS A 97  ? 0.5280 0.6425 0.6182 0.0682  0.1254  -0.0601 192  HIS A NE2 
524  N N   . ASP A 98  ? 0.4983 0.5810 0.5546 0.0649  0.1318  -0.0844 193  ASP A N   
525  C CA  . ASP A 98  ? 0.5149 0.5998 0.5711 0.0651  0.1413  -0.0936 193  ASP A CA  
526  C C   . ASP A 98  ? 0.5433 0.6182 0.5992 0.0666  0.1427  -0.1017 193  ASP A C   
527  O O   . ASP A 98  ? 0.4922 0.5602 0.5569 0.0699  0.1378  -0.0998 193  ASP A O   
528  C CB  . ASP A 98  ? 0.4717 0.5652 0.5466 0.0702  0.1463  -0.0941 193  ASP A CB  
529  C CG  . ASP A 98  ? 0.5901 0.6882 0.6650 0.0698  0.1576  -0.1033 193  ASP A CG  
530  O OD1 . ASP A 98  ? 0.6202 0.7184 0.6775 0.0642  0.1618  -0.1067 193  ASP A OD1 
531  O OD2 . ASP A 98  ? 0.5765 0.6779 0.6691 0.0755  0.1623  -0.1073 193  ASP A OD2 
532  N N   . ILE A 99  ? 0.5434 0.6168 0.5883 0.0635  0.1495  -0.1108 194  ILE A N   
533  C CA  . ILE A 99  ? 0.5512 0.6155 0.5966 0.0648  0.1533  -0.1209 194  ILE A CA  
534  C C   . ILE A 99  ? 0.5507 0.6192 0.5990 0.0663  0.1647  -0.1301 194  ILE A C   
535  O O   . ILE A 99  ? 0.6284 0.7032 0.6641 0.0618  0.1697  -0.1318 194  ILE A O   
536  C CB  . ILE A 99  ? 0.5743 0.6313 0.6002 0.0585  0.1502  -0.1248 194  ILE A CB  
537  C CG1 . ILE A 99  ? 0.6016 0.6548 0.6246 0.0566  0.1397  -0.1167 194  ILE A CG1 
538  C CG2 . ILE A 99  ? 0.5808 0.6278 0.6084 0.0597  0.1546  -0.1360 194  ILE A CG2 
539  C CD1 . ILE A 99  ? 0.6537 0.7009 0.6599 0.0505  0.1366  -0.1215 194  ILE A CD1 
540  N N   . ARG A 100 ? 0.5462 0.6110 0.6107 0.0724  0.1692  -0.1362 195  ARG A N   
541  C CA  . ARG A 100 ? 0.5684 0.6362 0.6369 0.0743  0.1810  -0.1465 195  ARG A CA  
542  C C   . ARG A 100 ? 0.5842 0.6394 0.6505 0.0751  0.1844  -0.1575 195  ARG A C   
543  O O   . ARG A 100 ? 0.5626 0.6097 0.6432 0.0805  0.1816  -0.1577 195  ARG A O   
544  C CB  . ARG A 100 ? 0.6050 0.6813 0.6981 0.0819  0.1846  -0.1447 195  ARG A CB  
545  C CG  . ARG A 100 ? 0.6368 0.7268 0.7317 0.0801  0.1840  -0.1365 195  ARG A CG  
546  C CD  . ARG A 100 ? 0.5854 0.6815 0.7033 0.0867  0.1791  -0.1288 195  ARG A CD  
547  N NE  . ARG A 100 ? 0.6881 0.7818 0.8270 0.0951  0.1823  -0.1339 195  ARG A NE  
548  C CZ  . ARG A 100 ? 0.6943 0.7827 0.8471 0.1011  0.1748  -0.1287 195  ARG A CZ  
549  N NH1 . ARG A 100 ? 0.6613 0.7468 0.8093 0.0995  0.1642  -0.1186 195  ARG A NH1 
550  N NH2 . ARG A 100 ? 0.6619 0.7475 0.8336 0.1091  0.1783  -0.1335 195  ARG A NH2 
551  N N   . SER A 101 ? 0.5565 0.6096 0.6044 0.0695  0.1904  -0.1667 196  SER A N   
552  C CA  . SER A 101 ? 0.5357 0.5769 0.5795 0.0692  0.1946  -0.1788 196  SER A CA  
553  C C   . SER A 101 ? 0.5324 0.5748 0.5900 0.0749  0.2068  -0.1889 196  SER A C   
554  O O   . SER A 101 ? 0.5456 0.5982 0.6015 0.0741  0.2154  -0.1916 196  SER A O   
555  C CB  . SER A 101 ? 0.5549 0.5930 0.5711 0.0601  0.1945  -0.1843 196  SER A CB  
556  O OG  . SER A 101 ? 0.5583 0.5931 0.5649 0.0557  0.1827  -0.1765 196  SER A OG  
557  N N   . LYS A 102 ? 0.5181 0.5496 0.5898 0.0806  0.2081  -0.1947 197  LYS A N   
558  C CA  . LYS A 102 ? 0.5439 0.5752 0.6310 0.0870  0.2196  -0.2047 197  LYS A CA  
559  C C   . LYS A 102 ? 0.5740 0.5887 0.6593 0.0876  0.2228  -0.2167 197  LYS A C   
560  O O   . LYS A 102 ? 0.5498 0.5561 0.6545 0.0952  0.2235  -0.2187 197  LYS A O   
561  C CB  . LYS A 102 ? 0.5424 0.5802 0.6579 0.0967  0.2182  -0.1974 197  LYS A CB  
562  C CG  . LYS A 102 ? 0.5264 0.5805 0.6455 0.0960  0.2147  -0.1859 197  LYS A CG  
563  C CD  . LYS A 102 ? 0.5638 0.6278 0.7101 0.1049  0.2194  -0.1849 197  LYS A CD  
564  C CE  . LYS A 102 ? 0.5903 0.6696 0.7424 0.1043  0.2146  -0.1732 197  LYS A CE  
565  N NZ  . LYS A 102 ? 0.6013 0.6924 0.7794 0.1121  0.2216  -0.1752 197  LYS A NZ  
566  N N   . GLY A 103 ? 0.5798 0.5895 0.6414 0.0795  0.2254  -0.2255 198  GLY A N   
567  C CA  . GLY A 103 ? 0.5825 0.5766 0.6397 0.0785  0.2293  -0.2386 198  GLY A CA  
568  C C   . GLY A 103 ? 0.5876 0.5684 0.6482 0.0782  0.2186  -0.2342 198  GLY A C   
569  O O   . GLY A 103 ? 0.5709 0.5516 0.6172 0.0715  0.2089  -0.2276 198  GLY A O   
570  N N   . SER A 104 ? 0.5845 0.5536 0.6642 0.0855  0.2208  -0.2379 199  SER A N   
571  C CA  . SER A 104 ? 0.5859 0.5414 0.6710 0.0857  0.2117  -0.2333 199  SER A CA  
572  C C   . SER A 104 ? 0.6191 0.5803 0.7163 0.0895  0.2015  -0.2164 199  SER A C   
573  O O   . SER A 104 ? 0.6510 0.6019 0.7514 0.0891  0.1936  -0.2109 199  SER A O   
574  C CB  . SER A 104 ? 0.5987 0.5384 0.6999 0.0925  0.2180  -0.2427 199  SER A CB  
575  O OG  . SER A 104 ? 0.6829 0.6157 0.7712 0.0882  0.2274  -0.2593 199  SER A OG  
576  N N   . LEU A 105 ? 0.5821 0.5591 0.6857 0.0927  0.2017  -0.2085 200  LEU A N   
577  C CA  . LEU A 105 ? 0.5510 0.5347 0.6632 0.0952  0.1920  -0.1928 200  LEU A CA  
578  C C   . LEU A 105 ? 0.5861 0.5831 0.6816 0.0881  0.1875  -0.1857 200  LEU A C   
579  O O   . LEU A 105 ? 0.5648 0.5696 0.6472 0.0838  0.1936  -0.1914 200  LEU A O   
580  C CB  . LEU A 105 ? 0.5751 0.5661 0.7118 0.1056  0.1949  -0.1885 200  LEU A CB  
581  C CG  . LEU A 105 ? 0.6433 0.6215 0.7995 0.1143  0.1990  -0.1942 200  LEU A CG  
582  C CD1 . LEU A 105 ? 0.6489 0.6374 0.8285 0.1243  0.2045  -0.1934 200  LEU A CD1 
583  C CD2 . LEU A 105 ? 0.6656 0.6313 0.8274 0.1159  0.1890  -0.1851 200  LEU A CD2 
584  N N   . ALA A 106 ? 0.5552 0.5539 0.6504 0.0868  0.1769  -0.1732 201  ALA A N   
585  C CA  . ALA A 106 ? 0.5659 0.5772 0.6499 0.0820  0.1721  -0.1645 201  ALA A CA  
586  C C   . ALA A 106 ? 0.5955 0.6113 0.6932 0.0866  0.1644  -0.1510 201  ALA A C   
587  O O   . ALA A 106 ? 0.5853 0.5918 0.6910 0.0893  0.1585  -0.1464 201  ALA A O   
588  C CB  . ALA A 106 ? 0.5747 0.5830 0.6369 0.0727  0.1662  -0.1643 201  ALA A CB  
589  N N   . PHE A 107 ? 0.5433 0.5732 0.6429 0.0871  0.1645  -0.1448 202  PHE A N   
590  C CA  . PHE A 107 ? 0.5672 0.6031 0.6793 0.0913  0.1577  -0.1328 202  PHE A CA  
591  C C   . PHE A 107 ? 0.5676 0.6104 0.6655 0.0849  0.1513  -0.1243 202  PHE A C   
592  O O   . PHE A 107 ? 0.5596 0.6113 0.6472 0.0807  0.1549  -0.1256 202  PHE A O   
593  C CB  . PHE A 107 ? 0.5613 0.6081 0.6911 0.0978  0.1632  -0.1329 202  PHE A CB  
594  C CG  . PHE A 107 ? 0.5550 0.5960 0.7001 0.1047  0.1703  -0.1417 202  PHE A CG  
595  C CD1 . PHE A 107 ? 0.5925 0.6333 0.7329 0.1034  0.1810  -0.1541 202  PHE A CD1 
596  C CD2 . PHE A 107 ? 0.5883 0.6231 0.7517 0.1126  0.1665  -0.1376 202  PHE A CD2 
597  C CE1 . PHE A 107 ? 0.5906 0.6253 0.7458 0.1103  0.1882  -0.1629 202  PHE A CE1 
598  C CE2 . PHE A 107 ? 0.5920 0.6206 0.7705 0.1197  0.1731  -0.1456 202  PHE A CE2 
599  C CZ  . PHE A 107 ? 0.5896 0.6182 0.7647 0.1187  0.1842  -0.1585 202  PHE A CZ  
600  N N   . ILE A 108 ? 0.5530 0.5913 0.6507 0.0844  0.1422  -0.1156 203  ILE A N   
601  C CA  . ILE A 108 ? 0.5492 0.5927 0.6354 0.0792  0.1355  -0.1071 203  ILE A CA  
602  C C   . ILE A 108 ? 0.5784 0.6277 0.6768 0.0834  0.1304  -0.0967 203  ILE A C   
603  O O   . ILE A 108 ? 0.5685 0.6116 0.6783 0.0882  0.1267  -0.0932 203  ILE A O   
604  C CB  . ILE A 108 ? 0.5810 0.6149 0.6567 0.0745  0.1294  -0.1059 203  ILE A CB  
605  C CG1 . ILE A 108 ? 0.6323 0.6610 0.6943 0.0693  0.1333  -0.1163 203  ILE A CG1 
606  C CG2 . ILE A 108 ? 0.5575 0.5966 0.6250 0.0706  0.1222  -0.0963 203  ILE A CG2 
607  C CD1 . ILE A 108 ? 0.6177 0.6372 0.6721 0.0647  0.1272  -0.1160 203  ILE A CD1 
608  N N   . ILE A 109 ? 0.5809 0.6414 0.6761 0.0813  0.1297  -0.0917 204  ILE A N   
609  C CA  . ILE A 109 ? 0.4928 0.5583 0.5957 0.0836  0.1234  -0.0816 204  ILE A CA  
610  C C   . ILE A 109 ? 0.5578 0.6200 0.6479 0.0786  0.1163  -0.0751 204  ILE A C   
611  O O   . ILE A 109 ? 0.5335 0.5988 0.6098 0.0730  0.1167  -0.0755 204  ILE A O   
612  C CB  . ILE A 109 ? 0.5335 0.6124 0.6413 0.0838  0.1265  -0.0798 204  ILE A CB  
613  C CG1 . ILE A 109 ? 0.5317 0.6152 0.6529 0.0884  0.1347  -0.0873 204  ILE A CG1 
614  C CG2 . ILE A 109 ? 0.4990 0.5825 0.6150 0.0859  0.1195  -0.0701 204  ILE A CG2 
615  C CD1 . ILE A 109 ? 0.5533 0.6322 0.6924 0.0963  0.1330  -0.0871 204  ILE A CD1 
616  N N   . LEU A 110 ? 0.5165 0.5724 0.6113 0.0806  0.1101  -0.0692 205  LEU A N   
617  C CA  . LEU A 110 ? 0.5147 0.5688 0.6002 0.0766  0.1036  -0.0623 205  LEU A CA  
618  C C   . LEU A 110 ? 0.5140 0.5758 0.6032 0.0777  0.0998  -0.0541 205  LEU A C   
619  O O   . LEU A 110 ? 0.5027 0.5675 0.6045 0.0826  0.0992  -0.0518 205  LEU A O   
620  C CB  . LEU A 110 ? 0.5253 0.5681 0.6128 0.0775  0.0995  -0.0603 205  LEU A CB  
621  C CG  . LEU A 110 ? 0.5954 0.6288 0.6755 0.0737  0.0998  -0.0656 205  LEU A CG  
622  C CD1 . LEU A 110 ? 0.5646 0.5893 0.6472 0.0740  0.0946  -0.0597 205  LEU A CD1 
623  C CD2 . LEU A 110 ? 0.5167 0.5543 0.5820 0.0672  0.0995  -0.0676 205  LEU A CD2 
624  N N   . ARG A 111 ? 0.4484 0.5132 0.5270 0.0730  0.0968  -0.0497 206  ARG A N   
625  C CA  . ARG A 111 ? 0.5069 0.5787 0.5868 0.0729  0.0936  -0.0428 206  ARG A CA  
626  C C   . ARG A 111 ? 0.5129 0.5807 0.5859 0.0704  0.0877  -0.0365 206  ARG A C   
627  O O   . ARG A 111 ? 0.4702 0.5340 0.5339 0.0668  0.0869  -0.0376 206  ARG A O   
628  C CB  . ARG A 111 ? 0.5059 0.5863 0.5799 0.0696  0.0974  -0.0440 206  ARG A CB  
629  C CG  . ARG A 111 ? 0.4814 0.5689 0.5578 0.0690  0.0949  -0.0378 206  ARG A CG  
630  C CD  . ARG A 111 ? 0.4830 0.5770 0.5520 0.0649  0.0988  -0.0385 206  ARG A CD  
631  N NE  . ARG A 111 ? 0.5066 0.5974 0.5613 0.0604  0.0966  -0.0360 206  ARG A NE  
632  C CZ  . ARG A 111 ? 0.5247 0.6144 0.5681 0.0571  0.0994  -0.0394 206  ARG A CZ  
633  N NH1 . ARG A 111 ? 0.4815 0.5729 0.5248 0.0572  0.1056  -0.0461 206  ARG A NH1 
634  N NH2 . ARG A 111 ? 0.5179 0.6051 0.5498 0.0538  0.0961  -0.0361 206  ARG A NH2 
635  N N   . HIS A 112 ? 0.4831 0.5527 0.5610 0.0723  0.0838  -0.0302 207  HIS A N   
636  C CA  . HIS A 112 ? 0.5099 0.5769 0.5818 0.0701  0.0789  -0.0239 207  HIS A CA  
637  C C   . HIS A 112 ? 0.5232 0.5963 0.5991 0.0712  0.0765  -0.0189 207  HIS A C   
638  O O   . HIS A 112 ? 0.5308 0.6051 0.6162 0.0752  0.0751  -0.0176 207  HIS A O   
639  C CB  . HIS A 112 ? 0.5197 0.5775 0.5934 0.0715  0.0762  -0.0221 207  HIS A CB  
640  C CG  . HIS A 112 ? 0.5577 0.6130 0.6261 0.0695  0.0721  -0.0160 207  HIS A CG  
641  N ND1 . HIS A 112 ? 0.5814 0.6369 0.6411 0.0652  0.0715  -0.0155 207  HIS A ND1 
642  C CD2 . HIS A 112 ? 0.5491 0.6018 0.6196 0.0712  0.0686  -0.0102 207  HIS A CD2 
643  C CE1 . HIS A 112 ? 0.5349 0.5881 0.5925 0.0645  0.0684  -0.0101 207  HIS A CE1 
644  N NE2 . HIS A 112 ? 0.5460 0.5973 0.6091 0.0678  0.0667  -0.0069 207  HIS A NE2 
645  N N   . LYS A 113 ? 0.5236 0.6003 0.5924 0.0677  0.0757  -0.0162 208  LYS A N   
646  C CA  . LYS A 113 ? 0.5143 0.5967 0.5859 0.0678  0.0737  -0.0123 208  LYS A CA  
647  C C   . LYS A 113 ? 0.5724 0.6625 0.6540 0.0699  0.0764  -0.0152 208  LYS A C   
648  O O   . LYS A 113 ? 0.5791 0.6735 0.6596 0.0682  0.0812  -0.0190 208  LYS A O   
649  C CB  . LYS A 113 ? 0.4962 0.5746 0.5691 0.0695  0.0686  -0.0071 208  LYS A CB  
650  C CG  . LYS A 113 ? 0.5022 0.5744 0.5658 0.0668  0.0668  -0.0044 208  LYS A CG  
651  C CD  . LYS A 113 ? 0.5171 0.5844 0.5809 0.0683  0.0628  0.0004  208  LYS A CD  
652  C CE  . LYS A 113 ? 0.5215 0.5849 0.5768 0.0651  0.0619  0.0032  208  LYS A CE  
653  N NZ  . LYS A 113 ? 0.5445 0.6030 0.5981 0.0659  0.0588  0.0079  208  LYS A NZ  
654  N N   . LEU A 114 ? 0.4968 0.5892 0.5884 0.0736  0.0735  -0.0133 209  LEU A N   
655  C CA  . LEU A 114 ? 0.5832 0.6841 0.6869 0.0762  0.0761  -0.0163 209  LEU A CA  
656  C C   . LEU A 114 ? 0.5502 0.6484 0.6643 0.0819  0.0764  -0.0186 209  LEU A C   
657  O O   . LEU A 114 ? 0.5905 0.6957 0.7175 0.0855  0.0766  -0.0197 209  LEU A O   
658  C CB  . LEU A 114 ? 0.5537 0.6624 0.6629 0.0758  0.0726  -0.0129 209  LEU A CB  
659  C CG  . LEU A 114 ? 0.5577 0.6633 0.6655 0.0768  0.0656  -0.0071 209  LEU A CG  
660  C CD1 . LEU A 114 ? 0.6305 0.7324 0.7460 0.0825  0.0624  -0.0058 209  LEU A CD1 
661  C CD2 . LEU A 114 ? 0.5784 0.6933 0.6913 0.0751  0.0632  -0.0056 209  LEU A CD2 
662  N N   . TYR A 115 ? 0.5456 0.6339 0.6552 0.0828  0.0762  -0.0193 210  TYR A N   
663  C CA  . TYR A 115 ? 0.5511 0.6344 0.6696 0.0880  0.0769  -0.0216 210  TYR A CA  
664  C C   . TYR A 115 ? 0.5644 0.6449 0.6810 0.0872  0.0834  -0.0290 210  TYR A C   
665  O O   . TYR A 115 ? 0.5381 0.6155 0.6428 0.0825  0.0850  -0.0307 210  TYR A O   
666  C CB  . TYR A 115 ? 0.5677 0.6404 0.6830 0.0893  0.0721  -0.0167 210  TYR A CB  
667  C CG  . TYR A 115 ? 0.5825 0.6567 0.6948 0.0887  0.0660  -0.0095 210  TYR A CG  
668  C CD1 . TYR A 115 ? 0.5995 0.6776 0.7214 0.0931  0.0617  -0.0059 210  TYR A CD1 
669  C CD2 . TYR A 115 ? 0.5672 0.6389 0.6673 0.0838  0.0645  -0.0065 210  TYR A CD2 
670  C CE1 . TYR A 115 ? 0.6273 0.7064 0.7449 0.0921  0.0560  0.0003  210  TYR A CE1 
671  C CE2 . TYR A 115 ? 0.5869 0.6594 0.6835 0.0831  0.0596  -0.0006 210  TYR A CE2 
672  C CZ  . TYR A 115 ? 0.6084 0.6844 0.7131 0.0869  0.0553  0.0026  210  TYR A CZ  
673  O OH  . TYR A 115 ? 0.6396 0.7162 0.7394 0.0858  0.0503  0.0079  210  TYR A OH  
674  N N   . SER A 116 ? 0.5493 0.6308 0.6775 0.0919  0.0868  -0.0336 211  SER A N   
675  C CA  . SER A 116 ? 0.5105 0.5884 0.6367 0.0914  0.0933  -0.0416 211  SER A CA  
676  C C   . SER A 116 ? 0.5355 0.6066 0.6733 0.0977  0.0942  -0.0442 211  SER A C   
677  O O   . SER A 116 ? 0.5453 0.6183 0.6955 0.1032  0.0909  -0.0406 211  SER A O   
678  C CB  . SER A 116 ? 0.4865 0.5748 0.6137 0.0895  0.0997  -0.0468 211  SER A CB  
679  O OG  . SER A 116 ? 0.5697 0.6669 0.7133 0.0943  0.1010  -0.0473 211  SER A OG  
680  N N   . MET A 117 ? 0.5032 0.5659 0.6367 0.0968  0.0984  -0.0506 212  MET A N   
681  C CA  . MET A 117 ? 0.5353 0.5886 0.6783 0.1022  0.0997  -0.0537 212  MET A CA  
682  C C   . MET A 117 ? 0.5089 0.5588 0.6493 0.1009  0.1075  -0.0642 212  MET A C   
683  O O   . MET A 117 ? 0.5461 0.5944 0.6725 0.0947  0.1092  -0.0676 212  MET A O   
684  C CB  . MET A 117 ? 0.5190 0.5594 0.6573 0.1017  0.0943  -0.0484 212  MET A CB  
685  C CG  . MET A 117 ? 0.5352 0.5639 0.6833 0.1072  0.0953  -0.0505 212  MET A CG  
686  S SD  . MET A 117 ? 0.5963 0.6092 0.7388 0.1060  0.0897  -0.0437 212  MET A SD  
687  C CE  . MET A 117 ? 0.4986 0.5071 0.6248 0.0968  0.0919  -0.0489 212  MET A CE  
688  N N   . GLN A 118 ? 0.5244 0.5733 0.6783 0.1069  0.1120  -0.0695 213  GLN A N   
689  C CA  . GLN A 118 ? 0.5447 0.5892 0.6962 0.1061  0.1199  -0.0803 213  GLN A CA  
690  C C   . GLN A 118 ? 0.5409 0.5690 0.6884 0.1055  0.1190  -0.0828 213  GLN A C   
691  O O   . GLN A 118 ? 0.5679 0.5873 0.7242 0.1102  0.1153  -0.0784 213  GLN A O   
692  C CB  . GLN A 118 ? 0.5453 0.5956 0.7137 0.1128  0.1264  -0.0861 213  GLN A CB  
693  C CG  . GLN A 118 ? 0.5543 0.6008 0.7189 0.1114  0.1358  -0.0985 213  GLN A CG  
694  C CD  . GLN A 118 ? 0.6275 0.6836 0.8066 0.1165  0.1440  -0.1050 213  GLN A CD  
695  O OE1 . GLN A 118 ? 0.6266 0.6918 0.7996 0.1126  0.1504  -0.1101 213  GLN A OE1 
696  N NE2 . GLN A 118 ? 0.5515 0.6054 0.7501 0.1252  0.1440  -0.1048 213  GLN A NE2 
697  N N   . CYS A 119 ? 0.5389 0.5628 0.6729 0.0994  0.1224  -0.0899 214  CYS A N   
698  C CA  . CYS A 119 ? 0.5532 0.5623 0.6828 0.0975  0.1228  -0.0946 214  CYS A CA  
699  C C   . CYS A 119 ? 0.5548 0.5614 0.6835 0.0974  0.1316  -0.1074 214  CYS A C   
700  O O   . CYS A 119 ? 0.5884 0.6045 0.7104 0.0946  0.1364  -0.1123 214  CYS A O   
701  C CB  . CYS A 119 ? 0.5327 0.5394 0.6464 0.0895  0.1178  -0.0916 214  CYS A CB  
702  S SG  . CYS A 119 ? 0.5594 0.5713 0.6720 0.0889  0.1089  -0.0775 214  CYS A SG  
703  N N   . ILE A 120 ? 0.5596 0.5528 0.6948 0.1003  0.1341  -0.1129 215  ILE A N   
704  C CA  . ILE A 120 ? 0.5547 0.5440 0.6920 0.1018  0.1431  -0.1256 215  ILE A CA  
705  C C   . ILE A 120 ? 0.5951 0.5704 0.7220 0.0962  0.1438  -0.1330 215  ILE A C   
706  O O   . ILE A 120 ? 0.6106 0.5736 0.7405 0.0964  0.1395  -0.1294 215  ILE A O   
707  C CB  . ILE A 120 ? 0.5723 0.5585 0.7308 0.1119  0.1467  -0.1267 215  ILE A CB  
708  C CG1 . ILE A 120 ? 0.5389 0.5408 0.7082 0.1167  0.1448  -0.1191 215  ILE A CG1 
709  C CG2 . ILE A 120 ? 0.5707 0.5523 0.7315 0.1134  0.1570  -0.1408 215  ILE A CG2 
710  C CD1 . ILE A 120 ? 0.6562 0.6580 0.8479 0.1271  0.1472  -0.1192 215  ILE A CD1 
711  N N   . LEU A 121 ? 0.5935 0.5707 0.7072 0.0906  0.1490  -0.1431 216  LEU A N   
712  C CA  . LEU A 121 ? 0.6149 0.5797 0.7190 0.0852  0.1508  -0.1526 216  LEU A CA  
713  C C   . LEU A 121 ? 0.6268 0.5858 0.7375 0.0893  0.1608  -0.1653 216  LEU A C   
714  O O   . LEU A 121 ? 0.6112 0.5802 0.7213 0.0907  0.1675  -0.1704 216  LEU A O   
715  C CB  . LEU A 121 ? 0.6146 0.5855 0.6976 0.0755  0.1486  -0.1551 216  LEU A CB  
716  C CG  . LEU A 121 ? 0.6786 0.6382 0.7506 0.0691  0.1503  -0.1664 216  LEU A CG  
717  C CD1 . LEU A 121 ? 0.6943 0.6410 0.7707 0.0674  0.1442  -0.1627 216  LEU A CD1 
718  C CD2 . LEU A 121 ? 0.6429 0.6109 0.6937 0.0604  0.1488  -0.1696 216  LEU A CD2 
719  N N   . ASP A 122 ? 0.6714 0.6141 0.7893 0.0913  0.1622  -0.1703 217  ASP A N   
720  C CA  . ASP A 122 ? 0.6982 0.6323 0.8248 0.0962  0.1717  -0.1824 217  ASP A CA  
721  C C   . ASP A 122 ? 0.8082 0.7263 0.9254 0.0898  0.1722  -0.1918 217  ASP A C   
722  O O   . ASP A 122 ? 0.8659 0.7712 0.9882 0.0897  0.1673  -0.1874 217  ASP A O   
723  C CB  . ASP A 122 ? 0.6994 0.6282 0.8493 0.1073  0.1721  -0.1770 217  ASP A CB  
724  C CG  . ASP A 122 ? 0.8287 0.7480 0.9903 0.1135  0.1820  -0.1892 217  ASP A CG  
725  O OD1 . ASP A 122 ? 0.8289 0.7423 0.9800 0.1088  0.1888  -0.2027 217  ASP A OD1 
726  O OD2 . ASP A 122 ? 0.8436 0.7615 1.0253 0.1236  0.1830  -0.1851 217  ASP A OD2 
727  N N   . ILE A 123 ? 0.7696 0.6882 0.8720 0.0838  0.1779  -0.2044 218  ILE A N   
728  C CA  . ILE A 123 ? 0.9030 0.8089 0.9935 0.0755  0.1758  -0.2118 218  ILE A CA  
729  C C   . ILE A 123 ? 0.9556 0.8422 1.0563 0.0788  0.1818  -0.2221 218  ILE A C   
730  O O   . ILE A 123 ? 1.0306 0.9045 1.1244 0.0722  0.1798  -0.2277 218  ILE A O   
731  C CB  . ILE A 123 ? 0.8995 0.8130 0.9668 0.0659  0.1769  -0.2202 218  ILE A CB  
732  C CG1 . ILE A 123 ? 0.7912 0.7091 0.8549 0.0681  0.1880  -0.2319 218  ILE A CG1 
733  C CG2 . ILE A 123 ? 0.8061 0.7353 0.8626 0.0614  0.1683  -0.2081 218  ILE A CG2 
734  C CD1 . ILE A 123 ? 0.8234 0.7423 0.8632 0.0582  0.1898  -0.2433 218  ILE A CD1 
735  N N   . LYS A 124 ? 0.9757 0.8594 1.0938 0.0890  0.1889  -0.2242 219  LYS A N   
736  C CA  . LYS A 124 ? 1.0044 0.8678 1.1367 0.0940  0.1922  -0.2291 219  LYS A CA  
737  C C   . LYS A 124 ? 1.0475 0.9008 1.1856 0.0933  0.1829  -0.2172 219  LYS A C   
738  O O   . LYS A 124 ? 1.0846 0.9192 1.2253 0.0914  0.1834  -0.2218 219  LYS A O   
739  C CB  . LYS A 124 ? 0.9792 0.8431 1.1324 0.1066  0.1996  -0.2301 219  LYS A CB  
740  N N   . HIS A 125 ? 0.9961 0.8613 1.1353 0.0941  0.1748  -0.2021 220  HIS A N   
741  C CA  . HIS A 125 ? 1.0181 0.8756 1.1616 0.0933  0.1663  -0.1898 220  HIS A CA  
742  C C   . HIS A 125 ? 1.0529 0.9128 1.1794 0.0816  0.1596  -0.1879 220  HIS A C   
743  O O   . HIS A 125 ? 1.0590 0.9172 1.1872 0.0800  0.1522  -0.1764 220  HIS A O   
744  C CB  . HIS A 125 ? 1.0060 0.8744 1.1604 0.1010  0.1613  -0.1745 220  HIS A CB  
745  C CG  . HIS A 125 ? 1.0833 0.9459 1.2583 0.1132  0.1652  -0.1729 220  HIS A CG  
746  N ND1 . HIS A 125 ? 1.1787 1.0214 1.3654 0.1177  0.1654  -0.1717 220  HIS A ND1 
747  C CD2 . HIS A 125 ? 1.0503 0.9246 1.2371 0.1219  0.1687  -0.1721 220  HIS A CD2 
748  C CE1 . HIS A 125 ? 1.1767 1.0190 1.3815 0.1293  0.1685  -0.1700 220  HIS A CE1 
749  N NE2 . HIS A 125 ? 1.1501 1.0122 1.3559 0.1319  0.1706  -0.1704 220  HIS A NE2 
750  N N   . ASN A 126 ? 1.0580 0.9221 1.1686 0.0734  0.1618  -0.1990 221  ASN A N   
751  C CA  . ASN A 126 ? 1.0746 0.9433 1.1698 0.0625  0.1548  -0.1975 221  ASN A CA  
752  C C   . ASN A 126 ? 1.1102 0.9707 1.1933 0.0540  0.1579  -0.2130 221  ASN A C   
753  O O   . ASN A 126 ? 1.0356 0.9060 1.1020 0.0459  0.1552  -0.2169 221  ASN A O   
754  C CB  . ASN A 126 ? 0.9679 0.8577 1.0527 0.0606  0.1508  -0.1906 221  ASN A CB  
755  C CG  . ASN A 126 ? 0.9341 0.8311 1.0282 0.0658  0.1451  -0.1744 221  ASN A CG  
756  O OD1 . ASN A 126 ? 0.9214 0.8233 1.0262 0.0744  0.1477  -0.1700 221  ASN A OD1 
757  N ND2 . ASN A 126 ? 0.8573 0.7547 0.9480 0.0607  0.1373  -0.1657 221  ASN A ND2 
758  N N   . ASP A 127 ? 1.2166 1.0583 1.3079 0.0558  0.1634  -0.2219 222  ASP A N   
759  C CA  . ASP A 127 ? 1.2506 1.0809 1.3324 0.0481  0.1669  -0.2379 222  ASP A CA  
760  C C   . ASP A 127 ? 1.2392 1.0782 1.3069 0.0459  0.1731  -0.2506 222  ASP A C   
761  O O   . ASP A 127 ? 1.2316 1.0669 1.2852 0.0370  0.1737  -0.2628 222  ASP A O   
762  C CB  . ASP A 127 ? 1.2806 1.1097 1.3529 0.0366  0.1587  -0.2366 222  ASP A CB  
763  C CG  . ASP A 127 ? 1.3955 1.2082 1.4808 0.0366  0.1560  -0.2305 222  ASP A CG  
764  O OD1 . ASP A 127 ? 1.4087 1.2266 1.5000 0.0386  0.1499  -0.2156 222  ASP A OD1 
765  O OD2 . ASP A 127 ? 1.4398 1.2339 1.5291 0.0346  0.1603  -0.2407 222  ASP A OD2 
766  N N   . ASN A 128 ? 1.1041 0.9547 1.1754 0.0536  0.1778  -0.2480 223  ASN A N   
767  C CA  . ASN A 128 ? 1.0567 0.9170 1.1144 0.0520  0.1846  -0.2587 223  ASN A CA  
768  C C   . ASN A 128 ? 1.0419 0.9129 1.0765 0.0407  0.1786  -0.2605 223  ASN A C   
769  O O   . ASN A 128 ? 0.9091 0.7794 0.9277 0.0348  0.1828  -0.2739 223  ASN A O   
770  C CB  . ASN A 128 ? 1.0534 0.8989 1.1131 0.0536  0.1953  -0.2759 223  ASN A CB  
771  C CG  . ASN A 128 ? 1.1292 0.9723 1.2088 0.0662  0.2037  -0.2755 223  ASN A CG  
772  O OD1 . ASN A 128 ? 1.0913 0.9323 1.1890 0.0739  0.2004  -0.2634 223  ASN A OD1 
773  N ND2 . ASN A 128 ? 1.1858 1.0300 1.2623 0.0685  0.2145  -0.2884 223  ASN A ND2 
774  N N   . ASP A 129 ? 0.9470 0.8281 0.9796 0.0380  0.1686  -0.2468 224  ASP A N   
775  C CA  . ASP A 129 ? 0.8651 0.7579 0.8777 0.0286  0.1617  -0.2461 224  ASP A CA  
776  C C   . ASP A 129 ? 0.7672 0.6768 0.7697 0.0304  0.1645  -0.2438 224  ASP A C   
777  O O   . ASP A 129 ? 0.7623 0.6833 0.7701 0.0347  0.1613  -0.2308 224  ASP A O   
778  C CB  . ASP A 129 ? 0.9124 0.8095 0.9282 0.0254  0.1506  -0.2327 224  ASP A CB  
779  C CG  . ASP A 129 ? 0.8334 0.7407 0.8302 0.0152  0.1429  -0.2334 224  ASP A CG  
780  O OD1 . ASP A 129 ? 0.8455 0.7541 0.8442 0.0107  0.1343  -0.2262 224  ASP A OD1 
781  O OD2 . ASP A 129 ? 0.8680 0.7817 0.8480 0.0116  0.1454  -0.2414 224  ASP A OD2 
782  N N   . LYS A 130 ? 0.7915 0.7020 0.7780 0.0263  0.1706  -0.2567 225  LYS A N   
783  C CA  . LYS A 130 ? 0.7507 0.6760 0.7241 0.0264  0.1740  -0.2558 225  LYS A CA  
784  C C   . LYS A 130 ? 0.7546 0.6934 0.7144 0.0205  0.1637  -0.2453 225  LYS A C   
785  O O   . LYS A 130 ? 0.7044 0.6563 0.6607 0.0228  0.1640  -0.2373 225  LYS A O   
786  C CB  . LYS A 130 ? 0.7712 0.6926 0.7284 0.0222  0.1828  -0.2729 225  LYS A CB  
787  C CG  . LYS A 130 ? 0.7628 0.6705 0.7336 0.0284  0.1941  -0.2846 225  LYS A CG  
788  C CD  . LYS A 130 ? 0.8530 0.7552 0.8056 0.0228  0.2021  -0.3027 225  LYS A CD  
789  C CE  . LYS A 130 ? 0.9791 0.8793 0.9405 0.0307  0.2167  -0.3114 225  LYS A CE  
790  N NZ  . LYS A 130 ? 0.9536 0.8418 0.9427 0.0402  0.2201  -0.3103 225  LYS A NZ  
791  N N   . ASN A 131 ? 0.7692 0.7052 0.7221 0.0129  0.1545  -0.2453 226  ASN A N   
792  C CA  . ASN A 131 ? 0.7378 0.6866 0.6794 0.0079  0.1443  -0.2352 226  ASN A CA  
793  C C   . ASN A 131 ? 0.6740 0.6300 0.6301 0.0139  0.1400  -0.2188 226  ASN A C   
794  O O   . ASN A 131 ? 0.6592 0.6281 0.6080 0.0135  0.1360  -0.2096 226  ASN A O   
795  C CB  . ASN A 131 ? 0.7443 0.6890 0.6797 -0.0008 0.1354  -0.2386 226  ASN A CB  
796  C CG  . ASN A 131 ? 0.7871 0.7276 0.7036 -0.0084 0.1376  -0.2542 226  ASN A CG  
797  O OD1 . ASN A 131 ? 0.8181 0.7632 0.7199 -0.0087 0.1435  -0.2599 226  ASN A OD1 
798  N ND2 . ASN A 131 ? 0.8081 0.7399 0.7245 -0.0151 0.1331  -0.2616 226  ASN A ND2 
799  N N   . MET A 132 ? 0.6651 0.6124 0.6413 0.0194  0.1405  -0.2148 227  MET A N   
800  C CA  . MET A 132 ? 0.6758 0.6292 0.6654 0.0252  0.1367  -0.1997 227  MET A CA  
801  C C   . MET A 132 ? 0.6285 0.5922 0.6192 0.0313  0.1423  -0.1954 227  MET A C   
802  O O   . MET A 132 ? 0.6134 0.5885 0.6021 0.0319  0.1378  -0.1844 227  MET A O   
803  C CB  . MET A 132 ? 0.6295 0.5703 0.6390 0.0302  0.1373  -0.1972 227  MET A CB  
804  C CG  . MET A 132 ? 0.6705 0.6168 0.6924 0.0356  0.1327  -0.1817 227  MET A CG  
805  S SD  . MET A 132 ? 0.7013 0.6322 0.7442 0.0411  0.1327  -0.1774 227  MET A SD  
806  C CE  . MET A 132 ? 0.6338 0.5757 0.6843 0.0457  0.1265  -0.1594 227  MET A CE  
807  N N   . MET A 133 ? 0.6395 0.5991 0.6341 0.0357  0.1524  -0.2044 228  MET A N   
808  C CA  . MET A 133 ? 0.6354 0.6054 0.6321 0.0409  0.1587  -0.2017 228  MET A CA  
809  C C   . MET A 133 ? 0.6076 0.5898 0.5836 0.0351  0.1573  -0.2003 228  MET A C   
810  O O   . MET A 133 ? 0.5861 0.5795 0.5629 0.0372  0.1558  -0.1902 228  MET A O   
811  C CB  . MET A 133 ? 0.5975 0.5610 0.6012 0.0458  0.1705  -0.2135 228  MET A CB  
812  C CG  . MET A 133 ? 0.6634 0.6385 0.6729 0.0516  0.1778  -0.2108 228  MET A CG  
813  S SD  . MET A 133 ? 0.7049 0.6883 0.7353 0.0596  0.1727  -0.1938 228  MET A SD  
814  C CE  . MET A 133 ? 0.6779 0.6476 0.7334 0.0690  0.1771  -0.1978 228  MET A CE  
815  N N   . LYS A 134 ? 0.6166 0.5964 0.5735 0.0277  0.1574  -0.2100 229  LYS A N   
816  C CA  . LYS A 134 ? 0.6402 0.6307 0.5758 0.0221  0.1558  -0.2085 229  LYS A CA  
817  C C   . LYS A 134 ? 0.6259 0.6250 0.5596 0.0204  0.1450  -0.1943 229  LYS A C   
818  O O   . LYS A 134 ? 0.6316 0.6411 0.5570 0.0200  0.1445  -0.1872 229  LYS A O   
819  C CB  . LYS A 134 ? 0.7235 0.7090 0.6385 0.0140  0.1559  -0.2212 229  LYS A CB  
820  C CG  . LYS A 134 ? 0.7597 0.7554 0.6508 0.0076  0.1519  -0.2185 229  LYS A CG  
821  C CD  . LYS A 134 ? 0.8437 0.8349 0.7135 -0.0010 0.1497  -0.2304 229  LYS A CD  
822  C CE  . LYS A 134 ? 0.9218 0.9038 0.7883 -0.0010 0.1612  -0.2466 229  LYS A CE  
823  N NZ  . LYS A 134 ? 0.9572 0.9258 0.8397 0.0003  0.1612  -0.2537 229  LYS A NZ  
824  N N   . TRP A 135 ? 0.6304 0.6249 0.5721 0.0192  0.1366  -0.1900 230  TRP A N   
825  C CA  . TRP A 135 ? 0.5972 0.5995 0.5387 0.0178  0.1267  -0.1770 230  TRP A CA  
826  C C   . TRP A 135 ? 0.6020 0.6103 0.5575 0.0248  0.1277  -0.1654 230  TRP A C   
827  O O   . TRP A 135 ? 0.5662 0.5840 0.5163 0.0243  0.1237  -0.1559 230  TRP A O   
828  C CB  . TRP A 135 ? 0.5977 0.5936 0.5461 0.0148  0.1188  -0.1761 230  TRP A CB  
829  C CG  . TRP A 135 ? 0.6282 0.6318 0.5780 0.0135  0.1090  -0.1635 230  TRP A CG  
830  C CD1 . TRP A 135 ? 0.6429 0.6532 0.5794 0.0074  0.1010  -0.1614 230  TRP A CD1 
831  C CD2 . TRP A 135 ? 0.5531 0.5584 0.5184 0.0185  0.1061  -0.1516 230  TRP A CD2 
832  N NE1 . TRP A 135 ? 0.5991 0.6153 0.5432 0.0086  0.0940  -0.1492 230  TRP A NE1 
833  C CE2 . TRP A 135 ? 0.5962 0.6091 0.5571 0.0151  0.0972  -0.1433 230  TRP A CE2 
834  C CE3 . TRP A 135 ? 0.5595 0.5607 0.5419 0.0256  0.1101  -0.1474 230  TRP A CE3 
835  C CZ2 . TRP A 135 ? 0.5750 0.5911 0.5472 0.0183  0.0930  -0.1315 230  TRP A CZ2 
836  C CZ3 . TRP A 135 ? 0.5823 0.5867 0.5748 0.0284  0.1051  -0.1353 230  TRP A CZ3 
837  C CH2 . TRP A 135 ? 0.5547 0.5663 0.5418 0.0247  0.0971  -0.1279 230  TRP A CH2 
838  N N   . VAL A 136 ? 0.5876 0.5900 0.5611 0.0314  0.1326  -0.1659 231  VAL A N   
839  C CA  . VAL A 136 ? 0.5649 0.5732 0.5523 0.0380  0.1330  -0.1552 231  VAL A CA  
840  C C   . VAL A 136 ? 0.5807 0.5992 0.5615 0.0390  0.1388  -0.1544 231  VAL A C   
841  O O   . VAL A 136 ? 0.5781 0.6053 0.5590 0.0399  0.1358  -0.1443 231  VAL A O   
842  C CB  . VAL A 136 ? 0.6053 0.6051 0.6130 0.0450  0.1368  -0.1564 231  VAL A CB  
843  C CG1 . VAL A 136 ? 0.5417 0.5490 0.5629 0.0519  0.1382  -0.1472 231  VAL A CG1 
844  C CG2 . VAL A 136 ? 0.5511 0.5413 0.5660 0.0439  0.1302  -0.1538 231  VAL A CG2 
845  N N   . SER A 137 ? 0.5627 0.5796 0.5376 0.0387  0.1479  -0.1654 232  SER A N   
846  C CA  . SER A 137 ? 0.6143 0.6406 0.5840 0.0395  0.1551  -0.1655 232  SER A CA  
847  C C   . SER A 137 ? 0.6226 0.6571 0.5736 0.0338  0.1505  -0.1591 232  SER A C   
848  O O   . SER A 137 ? 0.5919 0.6352 0.5423 0.0349  0.1535  -0.1533 232  SER A O   
849  C CB  . SER A 137 ? 0.5819 0.6045 0.5455 0.0389  0.1659  -0.1795 232  SER A CB  
850  O OG  . SER A 137 ? 0.6488 0.6651 0.6319 0.0457  0.1719  -0.1848 232  SER A OG  
851  N N   . ASN A 138 ? 0.6182 0.6502 0.5546 0.0277  0.1432  -0.1598 233  ASN A N   
852  C CA  . ASN A 138 ? 0.6101 0.6491 0.5278 0.0224  0.1379  -0.1539 233  ASN A CA  
853  C C   . ASN A 138 ? 0.5963 0.6404 0.5209 0.0238  0.1291  -0.1400 233  ASN A C   
854  O O   . ASN A 138 ? 0.6097 0.6596 0.5212 0.0205  0.1246  -0.1335 233  ASN A O   
855  C CB  . ASN A 138 ? 0.6677 0.7024 0.5680 0.0155  0.1331  -0.1614 233  ASN A CB  
856  C CG  . ASN A 138 ? 0.6945 0.7360 0.5754 0.0102  0.1259  -0.1550 233  ASN A CG  
857  O OD1 . ASN A 138 ? 0.7720 0.8145 0.6526 0.0080  0.1158  -0.1494 233  ASN A OD1 
858  N ND2 . ASN A 138 ? 0.6479 0.6939 0.5130 0.0081  0.1313  -0.1555 233  ASN A ND2 
859  N N   . LEU A 139 ? 0.5566 0.5985 0.5007 0.0287  0.1269  -0.1351 234  LEU A N   
860  C CA  . LEU A 139 ? 0.6142 0.6602 0.5638 0.0298  0.1190  -0.1228 234  LEU A CA  
861  C C   . LEU A 139 ? 0.6024 0.6569 0.5509 0.0314  0.1216  -0.1152 234  LEU A C   
862  O O   . LEU A 139 ? 0.6045 0.6610 0.5616 0.0351  0.1293  -0.1170 234  LEU A O   
863  C CB  . LEU A 139 ? 0.5688 0.6098 0.5383 0.0345  0.1168  -0.1196 234  LEU A CB  
864  C CG  . LEU A 139 ? 0.6107 0.6434 0.5830 0.0323  0.1118  -0.1233 234  LEU A CG  
865  C CD1 . LEU A 139 ? 0.5666 0.5936 0.5582 0.0376  0.1113  -0.1197 234  LEU A CD1 
866  C CD2 . LEU A 139 ? 0.5191 0.5553 0.4819 0.0272  0.1026  -0.1182 234  LEU A CD2 
867  N N   . PRO A 140 ? 0.6283 0.6879 0.5677 0.0288  0.1157  -0.1067 235  PRO A N   
868  C CA  . PRO A 140 ? 0.5993 0.6657 0.5376 0.0298  0.1184  -0.0994 235  PRO A CA  
869  C C   . PRO A 140 ? 0.5519 0.6202 0.5088 0.0349  0.1172  -0.0920 235  PRO A C   
870  O O   . PRO A 140 ? 0.5313 0.5964 0.4979 0.0367  0.1114  -0.0887 235  PRO A O   
871  C CB  . PRO A 140 ? 0.6108 0.6802 0.5334 0.0255  0.1114  -0.0928 235  PRO A CB  
872  C CG  . PRO A 140 ? 0.6015 0.6671 0.5229 0.0235  0.1033  -0.0942 235  PRO A CG  
873  C CD  . PRO A 140 ? 0.6068 0.6659 0.5371 0.0247  0.1064  -0.1038 235  PRO A CD  
874  N N   . LEU A 141 ? 0.5231 0.5968 0.4846 0.0368  0.1230  -0.0896 236  LEU A N   
875  C CA  . LEU A 141 ? 0.5361 0.6127 0.5139 0.0411  0.1215  -0.0824 236  LEU A CA  
876  C C   . LEU A 141 ? 0.5228 0.5997 0.4984 0.0400  0.1128  -0.0729 236  LEU A C   
877  O O   . LEU A 141 ? 0.4999 0.5774 0.4613 0.0361  0.1092  -0.0701 236  LEU A O   
878  C CB  . LEU A 141 ? 0.5126 0.5962 0.4943 0.0420  0.1286  -0.0812 236  LEU A CB  
879  C CG  . LEU A 141 ? 0.5882 0.6733 0.5743 0.0435  0.1386  -0.0905 236  LEU A CG  
880  C CD1 . LEU A 141 ? 0.5404 0.6341 0.5329 0.0441  0.1453  -0.0883 236  LEU A CD1 
881  C CD2 . LEU A 141 ? 0.5558 0.6362 0.5578 0.0487  0.1390  -0.0956 236  LEU A CD2 
882  N N   . GLU A 142 ? 0.4723 0.5486 0.4622 0.0437  0.1094  -0.0680 237  GLU A N   
883  C CA  . GLU A 142 ? 0.5000 0.5760 0.4919 0.0439  0.1020  -0.0595 237  GLU A CA  
884  C C   . GLU A 142 ? 0.5198 0.5906 0.5094 0.0424  0.0959  -0.0603 237  GLU A C   
885  O O   . GLU A 142 ? 0.5038 0.5744 0.4962 0.0427  0.0902  -0.0539 237  GLU A O   
886  C CB  . GLU A 142 ? 0.5235 0.6039 0.5058 0.0412  0.1004  -0.0527 237  GLU A CB  
887  C CG  . GLU A 142 ? 0.5492 0.6349 0.5364 0.0422  0.1055  -0.0502 237  GLU A CG  
888  C CD  . GLU A 142 ? 0.5607 0.6475 0.5647 0.0464  0.1045  -0.0474 237  GLU A CD  
889  O OE1 . GLU A 142 ? 0.5572 0.6457 0.5715 0.0493  0.1092  -0.0517 237  GLU A OE1 
890  O OE2 . GLU A 142 ? 0.5380 0.6239 0.5447 0.0470  0.0990  -0.0408 237  GLU A OE2 
891  N N   . SER A 143 ? 0.4945 0.5613 0.4796 0.0407  0.0971  -0.0682 238  SER A N   
892  C CA  . SER A 143 ? 0.5137 0.5758 0.4987 0.0389  0.0915  -0.0692 238  SER A CA  
893  C C   . SER A 143 ? 0.5021 0.5599 0.5020 0.0425  0.0896  -0.0662 238  SER A C   
894  O O   . SER A 143 ? 0.4768 0.5336 0.4872 0.0466  0.0933  -0.0666 238  SER A O   
895  C CB  . SER A 143 ? 0.5217 0.5795 0.4999 0.0362  0.0937  -0.0794 238  SER A CB  
896  O OG  . SER A 143 ? 0.5359 0.5973 0.4977 0.0322  0.0945  -0.0819 238  SER A OG  
897  N N   . ILE A 144 ? 0.4938 0.5496 0.4950 0.0409  0.0837  -0.0630 239  ILE A N   
898  C CA  . ILE A 144 ? 0.4970 0.5481 0.5102 0.0435  0.0819  -0.0597 239  ILE A CA  
899  C C   . ILE A 144 ? 0.5080 0.5512 0.5243 0.0421  0.0822  -0.0664 239  ILE A C   
900  O O   . ILE A 144 ? 0.4940 0.5366 0.5036 0.0376  0.0797  -0.0704 239  ILE A O   
901  C CB  . ILE A 144 ? 0.5019 0.5556 0.5157 0.0425  0.0763  -0.0516 239  ILE A CB  
902  C CG1 . ILE A 144 ? 0.4920 0.5522 0.5023 0.0437  0.0763  -0.0455 239  ILE A CG1 
903  C CG2 . ILE A 144 ? 0.4719 0.5201 0.4968 0.0449  0.0751  -0.0482 239  ILE A CG2 
904  C CD1 . ILE A 144 ? 0.5037 0.5667 0.5133 0.0427  0.0712  -0.0383 239  ILE A CD1 
905  N N   . VAL A 145 ? 0.5176 0.5547 0.5443 0.0459  0.0852  -0.0677 240  VAL A N   
906  C CA  . VAL A 145 ? 0.4931 0.5209 0.5235 0.0450  0.0863  -0.0742 240  VAL A CA  
907  C C   . VAL A 145 ? 0.5209 0.5419 0.5626 0.0477  0.0848  -0.0690 240  VAL A C   
908  O O   . VAL A 145 ? 0.4883 0.5111 0.5359 0.0518  0.0844  -0.0622 240  VAL A O   
909  C CB  . VAL A 145 ? 0.5072 0.5317 0.5384 0.0470  0.0928  -0.0831 240  VAL A CB  
910  C CG1 . VAL A 145 ? 0.5088 0.5390 0.5262 0.0432  0.0947  -0.0889 240  VAL A CG1 
911  C CG2 . VAL A 145 ? 0.4724 0.4980 0.5139 0.0535  0.0964  -0.0802 240  VAL A CG2 
912  N N   . ASP A 146 ? 0.4922 0.5051 0.5359 0.0448  0.0838  -0.0724 241  ASP A N   
913  C CA  . ASP A 146 ? 0.4943 0.4975 0.5479 0.0469  0.0837  -0.0695 241  ASP A CA  
914  C C   . ASP A 146 ? 0.5298 0.5232 0.5883 0.0490  0.0885  -0.0775 241  ASP A C   
915  O O   . ASP A 146 ? 0.5193 0.5094 0.5731 0.0451  0.0900  -0.0863 241  ASP A O   
916  C CB  . ASP A 146 ? 0.5355 0.5359 0.5890 0.0416  0.0799  -0.0675 241  ASP A CB  
917  C CG  . ASP A 146 ? 0.5724 0.5809 0.6244 0.0410  0.0759  -0.0585 241  ASP A CG  
918  O OD1 . ASP A 146 ? 0.5413 0.5569 0.5914 0.0442  0.0758  -0.0542 241  ASP A OD1 
919  O OD2 . ASP A 146 ? 0.5459 0.5536 0.5991 0.0371  0.0731  -0.0562 241  ASP A OD2 
920  N N   . ILE A 147 ? 0.5281 0.5169 0.5959 0.0552  0.0906  -0.0745 242  ILE A N   
921  C CA  . ILE A 147 ? 0.5320 0.5114 0.6067 0.0589  0.0954  -0.0810 242  ILE A CA  
922  C C   . ILE A 147 ? 0.5517 0.5184 0.6351 0.0608  0.0944  -0.0769 242  ILE A C   
923  O O   . ILE A 147 ? 0.5505 0.5176 0.6377 0.0634  0.0914  -0.0673 242  ILE A O   
924  C CB  . ILE A 147 ? 0.5675 0.5528 0.6476 0.0656  0.0988  -0.0809 242  ILE A CB  
925  C CG1 . ILE A 147 ? 0.5222 0.5172 0.5933 0.0633  0.1019  -0.0874 242  ILE A CG1 
926  C CG2 . ILE A 147 ? 0.5217 0.4961 0.6134 0.0715  0.1028  -0.0846 242  ILE A CG2 
927  C CD1 . ILE A 147 ? 0.5261 0.5292 0.6025 0.0688  0.1054  -0.0867 242  ILE A CD1 
928  N N   . LYS A 148 ? 0.5481 0.5028 0.6340 0.0591  0.0971  -0.0841 243  LYS A N   
929  C CA  . LYS A 148 ? 0.5703 0.5105 0.6654 0.0619  0.0975  -0.0810 243  LYS A CA  
930  C C   . LYS A 148 ? 0.6267 0.5608 0.7306 0.0692  0.1024  -0.0857 243  LYS A C   
931  O O   . LYS A 148 ? 0.6094 0.5415 0.7119 0.0684  0.1069  -0.0965 243  LYS A O   
932  C CB  . LYS A 148 ? 0.6333 0.5628 0.7267 0.0549  0.0974  -0.0857 243  LYS A CB  
933  C CG  . LYS A 148 ? 0.6683 0.5809 0.7707 0.0573  0.0985  -0.0824 243  LYS A CG  
934  C CD  . LYS A 148 ? 0.7214 0.6246 0.8224 0.0492  0.0981  -0.0859 243  LYS A CD  
935  C CE  . LYS A 148 ? 0.7703 0.6553 0.8798 0.0514  0.0996  -0.0819 243  LYS A CE  
936  N NZ  . LYS A 148 ? 0.8091 0.6860 0.9179 0.0427  0.0990  -0.0829 243  LYS A NZ  
937  N N   . GLY A 149 ? 0.6119 0.5435 0.7250 0.0764  0.1013  -0.0777 244  GLY A N   
938  C CA  . GLY A 149 ? 0.6657 0.5923 0.7893 0.0841  0.1056  -0.0817 244  GLY A CA  
939  C C   . GLY A 149 ? 0.6622 0.5823 0.7962 0.0915  0.1030  -0.0718 244  GLY A C   
940  O O   . GLY A 149 ? 0.6513 0.5710 0.7831 0.0903  0.0982  -0.0618 244  GLY A O   
941  N N   . LYS A 150 ? 0.6609 0.5765 0.8064 0.0993  0.1065  -0.0749 245  LYS A N   
942  C CA  . LYS A 150 ? 0.6698 0.5785 0.8264 0.1073  0.1038  -0.0660 245  LYS A CA  
943  C C   . LYS A 150 ? 0.6539 0.5775 0.8179 0.1143  0.1026  -0.0626 245  LYS A C   
944  O O   . LYS A 150 ? 0.6716 0.6041 0.8389 0.1161  0.1072  -0.0707 245  LYS A O   
945  C CB  . LYS A 150 ? 0.7226 0.6134 0.8893 0.1118  0.1080  -0.0711 245  LYS A CB  
946  C CG  . LYS A 150 ? 0.7682 0.6498 0.9464 0.1206  0.1048  -0.0613 245  LYS A CG  
947  C CD  . LYS A 150 ? 0.8787 0.7380 1.0579 0.1192  0.1054  -0.0596 245  LYS A CD  
948  C CE  . LYS A 150 ? 0.9088 0.7578 1.1001 0.1291  0.1026  -0.0502 245  LYS A CE  
949  N NZ  . LYS A 150 ? 0.9227 0.7849 1.1134 0.1327  0.0957  -0.0383 245  LYS A NZ  
950  N N   . LEU A 151 ? 0.6753 0.6020 0.8419 0.1178  0.0966  -0.0510 246  LEU A N   
951  C CA  . LEU A 151 ? 0.6555 0.5965 0.8301 0.1242  0.0946  -0.0476 246  LEU A CA  
952  C C   . LEU A 151 ? 0.6948 0.6296 0.8863 0.1345  0.0952  -0.0466 246  LEU A C   
953  O O   . LEU A 151 ? 0.7284 0.6468 0.9239 0.1374  0.0942  -0.0431 246  LEU A O   
954  C CB  . LEU A 151 ? 0.6350 0.5841 0.8036 0.1227  0.0874  -0.0361 246  LEU A CB  
955  C CG  . LEU A 151 ? 0.6808 0.6360 0.8339 0.1134  0.0861  -0.0355 246  LEU A CG  
956  C CD1 . LEU A 151 ? 0.6953 0.6595 0.8444 0.1133  0.0798  -0.0252 246  LEU A CD1 
957  C CD2 . LEU A 151 ? 0.6383 0.6041 0.7866 0.1091  0.0909  -0.0451 246  LEU A CD2 
958  N N   . SER A 152 ? 0.6606 0.6086 0.8628 0.1401  0.0971  -0.0498 247  SER A N   
959  C CA  . SER A 152 ? 0.6949 0.6408 0.9154 0.1509  0.0966  -0.0479 247  SER A CA  
960  C C   . SER A 152 ? 0.6997 0.6661 0.9294 0.1547  0.0961  -0.0481 247  SER A C   
961  O O   . SER A 152 ? 0.7027 0.6824 0.9247 0.1490  0.0982  -0.0520 247  SER A O   
962  C CB  . SER A 152 ? 0.6843 0.6175 0.9138 0.1547  0.1041  -0.0580 247  SER A CB  
963  O OG  . SER A 152 ? 0.7507 0.6951 0.9831 0.1541  0.1116  -0.0695 247  SER A OG  
964  N N   . LYS A 153 ? 0.7264 0.6951 0.9731 0.1645  0.0930  -0.0435 248  LYS A N   
965  C CA  . LYS A 153 ? 0.7460 0.7348 1.0039 0.1685  0.0915  -0.0427 248  LYS A CA  
966  C C   . LYS A 153 ? 0.7647 0.7581 1.0399 0.1749  0.0996  -0.0530 248  LYS A C   
967  O O   . LYS A 153 ? 0.7715 0.7547 1.0609 0.1834  0.1004  -0.0533 248  LYS A O   
968  C CB  . LYS A 153 ? 0.7990 0.7902 1.0649 0.1749  0.0815  -0.0302 248  LYS A CB  
969  C CG  . LYS A 153 ? 0.8340 0.8469 1.1094 0.1772  0.0781  -0.0280 248  LYS A CG  
970  C CD  . LYS A 153 ? 0.9015 0.9164 1.1750 0.1791  0.0666  -0.0148 248  LYS A CD  
971  C CE  . LYS A 153 ? 0.9421 0.9789 1.2197 0.1778  0.0627  -0.0129 248  LYS A CE  
972  N NZ  . LYS A 153 ? 0.9697 1.0074 1.2372 0.1758  0.0522  -0.0013 248  LYS A NZ  
973  N N   . PRO A 154 ? 0.8128 0.8206 1.0877 0.1713  0.1061  -0.0615 249  PRO A N   
974  C CA  . PRO A 154 ? 0.8127 0.8248 1.1035 0.1771  0.1152  -0.0721 249  PRO A CA  
975  C C   . PRO A 154 ? 0.8893 0.9143 1.2035 0.1871  0.1121  -0.0682 249  PRO A C   
976  O O   . PRO A 154 ? 0.9035 0.9383 1.2199 0.1879  0.1032  -0.0584 249  PRO A O   
977  C CB  . PRO A 154 ? 0.7961 0.8204 1.0758 0.1687  0.1223  -0.0805 249  PRO A CB  
978  C CG  . PRO A 154 ? 0.7925 0.8273 1.0608 0.1625  0.1146  -0.0714 249  PRO A CG  
979  C CD  . PRO A 154 ? 0.7618 0.7827 1.0220 0.1622  0.1056  -0.0612 249  PRO A CD  
980  N N   . GLU A 155 ? 0.9007 0.9263 1.2333 0.1947  0.1196  -0.0766 250  GLU A N   
981  C CA  . GLU A 155 ? 0.9291 0.9700 1.2868 0.2042  0.1182  -0.0750 250  GLU A CA  
982  C C   . GLU A 155 ? 0.9670 1.0311 1.3242 0.1992  0.1173  -0.0741 250  GLU A C   
983  O O   . GLU A 155 ? 0.9667 1.0404 1.3271 0.2001  0.1074  -0.0641 250  GLU A O   
984  C CB  . GLU A 155 ? 0.8968 0.9360 1.2729 0.2118  0.1289  -0.0866 250  GLU A CB  
985  N N   . VAL A 156 ? 0.9469 1.0196 1.2991 0.1933  0.1274  -0.0843 251  VAL A N   
986  C CA  . VAL A 156 ? 0.9420 1.0350 1.2917 0.1872  0.1280  -0.0841 251  VAL A CA  
987  C C   . VAL A 156 ? 0.9431 1.0311 1.2645 0.1753  0.1264  -0.0822 251  VAL A C   
988  O O   . VAL A 156 ? 0.9072 0.9872 1.2140 0.1697  0.1341  -0.0902 251  VAL A O   
989  C CB  . VAL A 156 ? 0.8957 1.0018 1.2575 0.1881  0.1405  -0.0959 251  VAL A CB  
990  N N   . PRO A 157 ? 0.9266 1.0187 1.2392 0.1714  0.1167  -0.0720 252  PRO A N   
991  C CA  . PRO A 157 ? 0.9062 0.9942 1.1935 0.1607  0.1153  -0.0701 252  PRO A CA  
992  C C   . PRO A 157 ? 0.9206 1.0241 1.2021 0.1535  0.1205  -0.0739 252  PRO A C   
993  O O   . PRO A 157 ? 0.9209 1.0409 1.2175 0.1558  0.1220  -0.0747 252  PRO A O   
994  C CB  . PRO A 157 ? 0.8846 0.9700 1.1672 0.1607  0.1029  -0.0575 252  PRO A CB  
995  C CG  . PRO A 157 ? 0.9194 1.0141 1.2253 0.1702  0.0975  -0.0528 252  PRO A CG  
996  C CD  . PRO A 157 ? 0.9562 1.0581 1.2823 0.1766  0.1066  -0.0622 252  PRO A CD  
997  N N   . ILE A 158 ? 0.8778 0.9757 1.1372 0.1445  0.1231  -0.0762 253  ILE A N   
998  C CA  . ILE A 158 ? 0.8238 0.9337 1.0747 0.1372  0.1287  -0.0798 253  ILE A CA  
999  C C   . ILE A 158 ? 0.7629 0.8861 1.0165 0.1350  0.1219  -0.0717 253  ILE A C   
1000 O O   . ILE A 158 ? 0.7852 0.9039 1.0308 0.1333  0.1127  -0.0631 253  ILE A O   
1001 C CB  . ILE A 158 ? 0.7969 0.8968 1.0228 0.1286  0.1309  -0.0824 253  ILE A CB  
1002 C CG1 . ILE A 158 ? 0.8439 0.9323 1.0675 0.1299  0.1386  -0.0921 253  ILE A CG1 
1003 C CG2 . ILE A 158 ? 0.7804 0.8914 0.9954 0.1208  0.1353  -0.0841 253  ILE A CG2 
1004 C CD1 . ILE A 158 ? 0.7621 0.8594 0.9949 0.1316  0.1500  -0.1023 253  ILE A CD1 
1005 N N   . ASP A 159 ? 0.7550 0.8945 1.0199 0.1346  0.1267  -0.0747 254  ASP A N   
1006 C CA  . ASP A 159 ? 0.7749 0.9276 1.0439 0.1322  0.1206  -0.0679 254  ASP A CA  
1007 C C   . ASP A 159 ? 0.7701 0.9191 1.0163 0.1230  0.1172  -0.0633 254  ASP A C   
1008 O O   . ASP A 159 ? 0.7614 0.9128 1.0054 0.1215  0.1085  -0.0555 254  ASP A O   
1009 C CB  . ASP A 159 ? 0.8010 0.9720 1.0859 0.1321  0.1278  -0.0729 254  ASP A CB  
1010 C CG  . ASP A 159 ? 0.8741 1.0507 1.1843 0.1417  0.1316  -0.0779 254  ASP A CG  
1011 O OD1 . ASP A 159 ? 0.8890 1.0570 1.2072 0.1494  0.1259  -0.0750 254  ASP A OD1 
1012 O OD2 . ASP A 159 ? 0.8874 1.0771 1.2099 0.1417  0.1407  -0.0845 254  ASP A OD2 
1013 N N   . SER A 160 ? 0.7405 0.8835 0.9693 0.1170  0.1238  -0.0681 255  SER A N   
1014 C CA  . SER A 160 ? 0.7517 0.8929 0.9604 0.1085  0.1215  -0.0642 255  SER A CA  
1015 C C   . SER A 160 ? 0.7012 0.8297 0.8972 0.1076  0.1127  -0.0574 255  SER A C   
1016 O O   . SER A 160 ? 0.7034 0.8320 0.8869 0.1019  0.1087  -0.0524 255  SER A O   
1017 C CB  . SER A 160 ? 0.7572 0.8957 0.9507 0.1026  0.1304  -0.0709 255  SER A CB  
1018 O OG  . SER A 160 ? 0.7728 0.8970 0.9557 0.1030  0.1309  -0.0740 255  SER A OG  
1019 N N   . THR A 161 ? 0.6874 0.8047 0.8864 0.1127  0.1100  -0.0572 256  THR A N   
1020 C CA  . THR A 161 ? 0.6406 0.7458 0.8276 0.1113  0.1026  -0.0509 256  THR A CA  
1021 C C   . THR A 161 ? 0.6484 0.7553 0.8451 0.1159  0.0936  -0.0428 256  THR A C   
1022 O O   . THR A 161 ? 0.6351 0.7440 0.8485 0.1232  0.0926  -0.0429 256  THR A O   
1023 C CB  . THR A 161 ? 0.6135 0.7039 0.7959 0.1129  0.1048  -0.0550 256  THR A CB  
1024 O OG1 . THR A 161 ? 0.6774 0.7658 0.8772 0.1211  0.1061  -0.0574 256  THR A OG1 
1025 C CG2 . THR A 161 ? 0.5971 0.6859 0.7679 0.1077  0.1129  -0.0632 256  THR A CG2 
1026 N N   . ASN A 162 ? 0.5782 0.6840 0.7640 0.1118  0.0871  -0.0358 257  ASN A N   
1027 C CA  . ASN A 162 ? 0.5900 0.6966 0.7822 0.1156  0.0783  -0.0280 257  ASN A CA  
1028 C C   . ASN A 162 ? 0.5985 0.6903 0.7880 0.1193  0.0742  -0.0241 257  ASN A C   
1029 O O   . ASN A 162 ? 0.6278 0.7189 0.8239 0.1239  0.0673  -0.0179 257  ASN A O   
1030 C CB  . ASN A 162 ? 0.5716 0.6832 0.7540 0.1099  0.0734  -0.0225 257  ASN A CB  
1031 C CG  . ASN A 162 ? 0.6243 0.7273 0.7872 0.1034  0.0741  -0.0217 257  ASN A CG  
1032 O OD1 . ASN A 162 ? 0.5936 0.6856 0.7495 0.1031  0.0763  -0.0236 257  ASN A OD1 
1033 N ND2 . ASN A 162 ? 0.6144 0.7224 0.7690 0.0980  0.0721  -0.0188 257  ASN A ND2 
1034 N N   . ILE A 163 ? 0.5629 0.6429 0.7431 0.1172  0.0781  -0.0276 258  ILE A N   
1035 C CA  . ILE A 163 ? 0.5702 0.6356 0.7513 0.1212  0.0762  -0.0257 258  ILE A CA  
1036 C C   . ILE A 163 ? 0.6217 0.6862 0.8181 0.1278  0.0815  -0.0322 258  ILE A C   
1037 O O   . ILE A 163 ? 0.6180 0.6837 0.8136 0.1259  0.0892  -0.0408 258  ILE A O   
1038 C CB  . ILE A 163 ? 0.5705 0.6240 0.7354 0.1154  0.0777  -0.0267 258  ILE A CB  
1039 C CG1 . ILE A 163 ? 0.5519 0.6063 0.7036 0.1098  0.0726  -0.0199 258  ILE A CG1 
1040 C CG2 . ILE A 163 ? 0.5584 0.5963 0.7260 0.1191  0.0774  -0.0262 258  ILE A CG2 
1041 C CD1 . ILE A 163 ? 0.5644 0.6101 0.7011 0.1035  0.0740  -0.0210 258  ILE A CD1 
1042 N N   . LYS A 164 ? 0.6132 0.6755 0.8232 0.1356  0.0773  -0.0282 259  LYS A N   
1043 C CA  . LYS A 164 ? 0.6336 0.6963 0.8613 0.1431  0.0819  -0.0338 259  LYS A CA  
1044 C C   . LYS A 164 ? 0.6444 0.6891 0.8710 0.1455  0.0848  -0.0367 259  LYS A C   
1045 O O   . LYS A 164 ? 0.7449 0.7861 0.9867 0.1532  0.0871  -0.0396 259  LYS A O   
1046 C CB  . LYS A 164 ? 0.6565 0.7277 0.9018 0.1510  0.0756  -0.0281 259  LYS A CB  
1047 C CG  . LYS A 164 ? 0.6637 0.7535 0.9119 0.1482  0.0729  -0.0263 259  LYS A CG  
1048 C CD  . LYS A 164 ? 0.6608 0.7625 0.9136 0.1454  0.0823  -0.0358 259  LYS A CD  
1049 C CE  . LYS A 164 ? 0.6548 0.7731 0.9075 0.1406  0.0803  -0.0339 259  LYS A CE  
1050 N NZ  . LYS A 164 ? 0.6717 0.8010 0.9281 0.1373  0.0900  -0.0426 259  LYS A NZ  
1051 N N   . TYR A 165 ? 0.6565 0.6897 0.8663 0.1392  0.0848  -0.0361 260  TYR A N   
1052 C CA  . TYR A 165 ? 0.6453 0.6617 0.8521 0.1393  0.0885  -0.0403 260  TYR A CA  
1053 C C   . TYR A 165 ? 0.6244 0.6413 0.8210 0.1326  0.0961  -0.0504 260  TYR A C   
1054 O O   . TYR A 165 ? 0.5828 0.6105 0.7704 0.1267  0.0970  -0.0515 260  TYR A O   
1055 C CB  . TYR A 165 ? 0.6793 0.6823 0.8748 0.1364  0.0827  -0.0321 260  TYR A CB  
1056 C CG  . TYR A 165 ? 0.7648 0.7626 0.9688 0.1435  0.0756  -0.0224 260  TYR A CG  
1057 C CD1 . TYR A 165 ? 0.7870 0.7676 0.9953 0.1477  0.0756  -0.0207 260  TYR A CD1 
1058 C CD2 . TYR A 165 ? 0.7693 0.7788 0.9766 0.1457  0.0689  -0.0148 260  TYR A CD2 
1059 C CE1 . TYR A 165 ? 0.8113 0.7863 1.0264 0.1544  0.0688  -0.0110 260  TYR A CE1 
1060 C CE2 . TYR A 165 ? 0.7767 0.7816 0.9906 0.1521  0.0617  -0.0056 260  TYR A CE2 
1061 C CZ  . TYR A 165 ? 0.8171 0.8046 1.0346 0.1566  0.0617  -0.0033 260  TYR A CZ  
1062 O OH  . TYR A 165 ? 0.9013 0.8830 1.1243 0.1633  0.0543  0.0066  260  TYR A OH  
1063 N N   . GLU A 166 ? 0.5948 0.5996 0.7925 0.1334  0.1015  -0.0577 261  GLU A N   
1064 C CA  . GLU A 166 ? 0.6154 0.6183 0.8016 0.1267  0.1080  -0.0674 261  GLU A CA  
1065 C C   . GLU A 166 ? 0.6166 0.6028 0.7930 0.1224  0.1070  -0.0677 261  GLU A C   
1066 O O   . GLU A 166 ? 0.6260 0.5990 0.8088 0.1266  0.1050  -0.0644 261  GLU A O   
1067 C CB  . GLU A 166 ? 0.6058 0.6101 0.8016 0.1305  0.1168  -0.0785 261  GLU A CB  
1068 C CG  . GLU A 166 ? 0.6642 0.6812 0.8775 0.1379  0.1177  -0.0776 261  GLU A CG  
1069 C CD  . GLU A 166 ? 0.7388 0.7581 0.9613 0.1412  0.1276  -0.0894 261  GLU A CD  
1070 O OE1 . GLU A 166 ? 0.6861 0.7194 0.9072 0.1385  0.1325  -0.0939 261  GLU A OE1 
1071 O OE2 . GLU A 166 ? 0.7425 0.7490 0.9733 0.1463  0.1309  -0.0941 261  GLU A OE2 
1072 N N   . ALA A 167 ? 0.5672 0.5542 0.7284 0.1140  0.1086  -0.0720 262  ALA A N   
1073 C CA  . ALA A 167 ? 0.5720 0.5449 0.7242 0.1087  0.1088  -0.0748 262  ALA A CA  
1074 C C   . ALA A 167 ? 0.6334 0.6007 0.7856 0.1080  0.1165  -0.0878 262  ALA A C   
1075 O O   . ALA A 167 ? 0.6151 0.5924 0.7633 0.1061  0.1212  -0.0947 262  ALA A O   
1076 C CB  . ALA A 167 ? 0.5659 0.5433 0.7022 0.1000  0.1052  -0.0719 262  ALA A CB  
1077 N N   . HIS A 168 ? 0.5671 0.5182 0.7238 0.1096  0.1182  -0.0912 263  HIS A N   
1078 C CA  . HIS A 168 ? 0.6025 0.5456 0.7565 0.1072  0.1252  -0.1042 263  HIS A CA  
1079 C C   . HIS A 168 ? 0.6393 0.5765 0.7784 0.0974  0.1231  -0.1064 263  HIS A C   
1080 O O   . HIS A 168 ? 0.6466 0.5733 0.7852 0.0955  0.1188  -0.1006 263  HIS A O   
1081 C CB  . HIS A 168 ? 0.6089 0.5372 0.7774 0.1146  0.1287  -0.1075 263  HIS A CB  
1082 C CG  . HIS A 168 ? 0.6394 0.5753 0.8234 0.1240  0.1325  -0.1090 263  HIS A CG  
1083 N ND1 . HIS A 168 ? 0.6523 0.5967 0.8470 0.1305  0.1276  -0.0986 263  HIS A ND1 
1084 C CD2 . HIS A 168 ? 0.6706 0.6083 0.8614 0.1276  0.1409  -0.1201 263  HIS A CD2 
1085 C CE1 . HIS A 168 ? 0.6556 0.6071 0.8644 0.1379  0.1324  -0.1030 263  HIS A CE1 
1086 N NE2 . HIS A 168 ? 0.6756 0.6233 0.8826 0.1364  0.1410  -0.1160 263  HIS A NE2 
1087 N N   . ILE A 169 ? 0.6088 0.5533 0.7358 0.0912  0.1259  -0.1144 264  ILE A N   
1088 C CA  . ILE A 169 ? 0.6232 0.5674 0.7353 0.0817  0.1226  -0.1155 264  ILE A CA  
1089 C C   . ILE A 169 ? 0.6749 0.6028 0.7859 0.0780  0.1246  -0.1236 264  ILE A C   
1090 O O   . ILE A 169 ? 0.6781 0.5998 0.7908 0.0791  0.1310  -0.1347 264  ILE A O   
1091 C CB  . ILE A 169 ? 0.6225 0.5801 0.7217 0.0768  0.1246  -0.1210 264  ILE A CB  
1092 C CG1 . ILE A 169 ? 0.5764 0.5493 0.6759 0.0793  0.1221  -0.1122 264  ILE A CG1 
1093 C CG2 . ILE A 169 ? 0.5607 0.5175 0.6450 0.0672  0.1212  -0.1240 264  ILE A CG2 
1094 C CD1 . ILE A 169 ? 0.5662 0.5514 0.6543 0.0755  0.1251  -0.1168 264  ILE A CD1 
1095 N N   . ARG A 170 ? 0.6523 0.5735 0.7606 0.0731  0.1195  -0.1184 265  ARG A N   
1096 C CA  . ARG A 170 ? 0.6556 0.5639 0.7601 0.0667  0.1204  -0.1262 265  ARG A CA  
1097 C C   . ARG A 170 ? 0.6288 0.5451 0.7187 0.0569  0.1170  -0.1294 265  ARG A C   
1098 O O   . ARG A 170 ? 0.6584 0.5700 0.7418 0.0514  0.1193  -0.1404 265  ARG A O   
1099 C CB  . ARG A 170 ? 0.6916 0.5855 0.8042 0.0673  0.1177  -0.1190 265  ARG A CB  
1100 C CG  . ARG A 170 ? 0.7708 0.6570 0.8977 0.0775  0.1192  -0.1129 265  ARG A CG  
1101 C CD  . ARG A 170 ? 0.8849 0.7669 1.0196 0.0841  0.1263  -0.1227 265  ARG A CD  
1102 N NE  . ARG A 170 ? 0.9899 0.8518 1.1314 0.0850  0.1303  -0.1292 265  ARG A NE  
1103 C CZ  . ARG A 170 ? 1.0454 0.9004 1.1841 0.0821  0.1362  -0.1433 265  ARG A CZ  
1104 N NH1 . ARG A 170 ? 1.1222 0.9575 1.2671 0.0824  0.1396  -0.1490 265  ARG A NH1 
1105 N NH2 . ARG A 170 ? 1.0037 0.8712 1.1325 0.0787  0.1389  -0.1519 265  ARG A NH2 
1106 N N   . LYS A 171 ? 0.5708 0.4993 0.6557 0.0548  0.1115  -0.1202 266  LYS A N   
1107 C CA  . LYS A 171 ? 0.5912 0.5289 0.6631 0.0466  0.1079  -0.1225 266  LYS A CA  
1108 C C   . LYS A 171 ? 0.5847 0.5388 0.6511 0.0483  0.1056  -0.1159 266  LYS A C   
1109 O O   . LYS A 171 ? 0.5730 0.5307 0.6462 0.0541  0.1049  -0.1071 266  LYS A O   
1110 C CB  . LYS A 171 ? 0.6109 0.5447 0.6827 0.0403  0.1026  -0.1181 266  LYS A CB  
1111 C CG  . LYS A 171 ? 0.6976 0.6148 0.7740 0.0369  0.1046  -0.1251 266  LYS A CG  
1112 C CD  . LYS A 171 ? 0.6812 0.5964 0.7574 0.0293  0.0998  -0.1217 266  LYS A CD  
1113 C CE  . LYS A 171 ? 0.7253 0.6231 0.8068 0.0253  0.1024  -0.1290 266  LYS A CE  
1114 N NZ  . LYS A 171 ? 0.8144 0.7126 0.8942 0.0157  0.0982  -0.1295 266  LYS A NZ  
1115 N N   . ILE A 172 ? 0.5582 0.5217 0.6120 0.0429  0.1043  -0.1201 267  ILE A N   
1116 C CA  . ILE A 172 ? 0.5320 0.5100 0.5794 0.0435  0.1020  -0.1137 267  ILE A CA  
1117 C C   . ILE A 172 ? 0.5732 0.5587 0.6075 0.0361  0.0973  -0.1151 267  ILE A C   
1118 O O   . ILE A 172 ? 0.5437 0.5289 0.5685 0.0317  0.0987  -0.1247 267  ILE A O   
1119 C CB  . ILE A 172 ? 0.5573 0.5407 0.6038 0.0482  0.1079  -0.1174 267  ILE A CB  
1120 C CG1 . ILE A 172 ? 0.4947 0.4924 0.5335 0.0477  0.1056  -0.1110 267  ILE A CG1 
1121 C CG2 . ILE A 172 ? 0.4866 0.4651 0.5264 0.0457  0.1135  -0.1310 267  ILE A CG2 
1122 C CD1 . ILE A 172 ? 0.5162 0.5201 0.5559 0.0521  0.1116  -0.1129 267  ILE A CD1 
1123 N N   . PHE A 173 ? 0.5342 0.5269 0.5679 0.0346  0.0916  -0.1058 268  PHE A N   
1124 C CA  . PHE A 173 ? 0.5346 0.5350 0.5582 0.0283  0.0861  -0.1056 268  PHE A CA  
1125 C C   . PHE A 173 ? 0.5516 0.5639 0.5701 0.0302  0.0840  -0.0977 268  PHE A C   
1126 O O   . PHE A 173 ? 0.5370 0.5510 0.5625 0.0351  0.0845  -0.0898 268  PHE A O   
1127 C CB  . PHE A 173 ? 0.5630 0.5604 0.5921 0.0243  0.0812  -0.1023 268  PHE A CB  
1128 C CG  . PHE A 173 ? 0.6235 0.6078 0.6586 0.0219  0.0833  -0.1093 268  PHE A CG  
1129 C CD1 . PHE A 173 ? 0.6071 0.5884 0.6354 0.0162  0.0835  -0.1203 268  PHE A CD1 
1130 C CD2 . PHE A 173 ? 0.6146 0.5888 0.6615 0.0253  0.0852  -0.1050 268  PHE A CD2 
1131 C CE1 . PHE A 173 ? 0.6448 0.6130 0.6790 0.0136  0.0857  -0.1274 268  PHE A CE1 
1132 C CE2 . PHE A 173 ? 0.6369 0.5975 0.6895 0.0231  0.0875  -0.1111 268  PHE A CE2 
1133 C CZ  . PHE A 173 ? 0.6655 0.6229 0.7121 0.0172  0.0880  -0.1225 268  PHE A CZ  
1134 N N   . CYS A 174 ? 0.5122 0.5324 0.5182 0.0263  0.0816  -0.0997 269  CYS A N   
1135 C CA  . CYS A 174 ? 0.5483 0.5786 0.5481 0.0277  0.0799  -0.0926 269  CYS A CA  
1136 C C   . CYS A 174 ? 0.5609 0.5970 0.5597 0.0245  0.0725  -0.0862 269  CYS A C   
1137 O O   . CYS A 174 ? 0.5770 0.6151 0.5693 0.0193  0.0684  -0.0901 269  CYS A O   
1138 C CB  . CYS A 174 ? 0.5291 0.5639 0.5151 0.0260  0.0826  -0.0981 269  CYS A CB  
1139 S SG  . CYS A 174 ? 0.5602 0.6061 0.5380 0.0272  0.0808  -0.0888 269  CYS A SG  
1140 N N   . ILE A 175 ? 0.4895 0.5285 0.4951 0.0276  0.0709  -0.0768 270  ILE A N   
1141 C CA  . ILE A 175 ? 0.5646 0.6093 0.5707 0.0253  0.0648  -0.0706 270  ILE A CA  
1142 C C   . ILE A 175 ? 0.5641 0.6178 0.5612 0.0257  0.0623  -0.0656 270  ILE A C   
1143 O O   . ILE A 175 ? 0.5554 0.6147 0.5511 0.0235  0.0568  -0.0619 270  ILE A O   
1144 C CB  . ILE A 175 ? 0.5875 0.6294 0.6054 0.0279  0.0644  -0.0635 270  ILE A CB  
1145 C CG1 . ILE A 175 ? 0.5298 0.5725 0.5501 0.0334  0.0674  -0.0576 270  ILE A CG1 
1146 C CG2 . ILE A 175 ? 0.5689 0.6009 0.5951 0.0268  0.0662  -0.0677 270  ILE A CG2 
1147 C CD1 . ILE A 175 ? 0.5361 0.5792 0.5637 0.0354  0.0657  -0.0492 270  ILE A CD1 
1148 N N   . SER A 176 ? 0.5165 0.5717 0.5082 0.0283  0.0663  -0.0652 271  SER A N   
1149 C CA  . SER A 176 ? 0.5191 0.5815 0.5008 0.0281  0.0646  -0.0608 271  SER A CA  
1150 C C   . SER A 176 ? 0.5512 0.6136 0.5239 0.0283  0.0701  -0.0656 271  SER A C   
1151 O O   . SER A 176 ? 0.5068 0.5677 0.4848 0.0318  0.0756  -0.0654 271  SER A O   
1152 C CB  . SER A 176 ? 0.5240 0.5893 0.5114 0.0315  0.0639  -0.0514 271  SER A CB  
1153 O OG  . SER A 176 ? 0.5154 0.5861 0.4932 0.0313  0.0629  -0.0473 271  SER A OG  
1154 N N   . LYS A 177 ? 0.5153 0.5801 0.4744 0.0245  0.0687  -0.0698 272  LYS A N   
1155 C CA  . LYS A 177 ? 0.5894 0.6543 0.5378 0.0239  0.0745  -0.0749 272  LYS A CA  
1156 C C   . LYS A 177 ? 0.5707 0.6411 0.5103 0.0244  0.0748  -0.0679 272  LYS A C   
1157 O O   . LYS A 177 ? 0.5721 0.6462 0.5058 0.0230  0.0687  -0.0622 272  LYS A O   
1158 C CB  . LYS A 177 ? 0.5478 0.6113 0.4839 0.0190  0.0733  -0.0839 272  LYS A CB  
1159 C CG  . LYS A 177 ? 0.6056 0.6689 0.5293 0.0181  0.0802  -0.0898 272  LYS A CG  
1160 C CD  . LYS A 177 ? 0.6296 0.6910 0.5398 0.0129  0.0790  -0.0993 272  LYS A CD  
1161 C CE  . LYS A 177 ? 0.7716 0.8370 0.6617 0.0100  0.0799  -0.0993 272  LYS A CE  
1162 N NZ  . LYS A 177 ? 0.8343 0.9050 0.7152 0.0072  0.0702  -0.0928 272  LYS A NZ  
1163 N N   . THR A 178 ? 0.5061 0.5767 0.4458 0.0265  0.0820  -0.0683 273  THR A N   
1164 C CA  . THR A 178 ? 0.5411 0.6160 0.4713 0.0261  0.0836  -0.0627 273  THR A CA  
1165 C C   . THR A 178 ? 0.5980 0.6745 0.5090 0.0216  0.0808  -0.0644 273  THR A C   
1166 O O   . THR A 178 ? 0.6340 0.7085 0.5364 0.0189  0.0834  -0.0731 273  THR A O   
1167 C CB  . THR A 178 ? 0.5434 0.6189 0.4767 0.0280  0.0927  -0.0651 273  THR A CB  
1168 O OG1 . THR A 178 ? 0.5540 0.6294 0.5044 0.0324  0.0937  -0.0615 273  THR A OG1 
1169 C CG2 . THR A 178 ? 0.5478 0.6270 0.4689 0.0262  0.0957  -0.0607 273  THR A CG2 
1170 N N   . ALA A 179 ? 0.5691 0.6487 0.4730 0.0208  0.0754  -0.0562 274  ALA A N   
1171 C CA  . ALA A 179 ? 0.6145 0.6957 0.5002 0.0168  0.0709  -0.0565 274  ALA A CA  
1172 C C   . ALA A 179 ? 0.6431 0.7251 0.5129 0.0151  0.0759  -0.0542 274  ALA A C   
1173 O O   . ALA A 179 ? 0.6442 0.7268 0.4962 0.0115  0.0736  -0.0557 274  ALA A O   
1174 C CB  . ALA A 179 ? 0.5783 0.6623 0.4651 0.0171  0.0610  -0.0487 274  ALA A CB  
1175 N N   . LYS A 180 ? 0.6345 0.7166 0.5102 0.0173  0.0826  -0.0508 275  LYS A N   
1176 C CA  . LYS A 180 ? 0.6551 0.7380 0.5175 0.0155  0.0872  -0.0466 275  LYS A CA  
1177 C C   . LYS A 180 ? 0.6590 0.7424 0.5283 0.0165  0.0980  -0.0503 275  LYS A C   
1178 O O   . LYS A 180 ? 0.5738 0.6574 0.4611 0.0200  0.1002  -0.0515 275  LYS A O   
1179 C CB  . LYS A 180 ? 0.6825 0.7661 0.5459 0.0169  0.0822  -0.0349 275  LYS A CB  
1180 C CG  . LYS A 180 ? 0.7565 0.8395 0.6032 0.0144  0.0848  -0.0291 275  LYS A CG  
1181 C CD  . LYS A 180 ? 0.7981 0.8805 0.6443 0.0158  0.0772  -0.0181 275  LYS A CD  
1182 C CE  . LYS A 180 ? 0.8370 0.9180 0.6878 0.0167  0.0824  -0.0112 275  LYS A CE  
1183 N NZ  . LYS A 180 ? 0.8854 0.9639 0.7248 0.0162  0.0778  -0.0010 275  LYS A NZ  
1184 N N   . GLU A 181 ? 0.6505 0.7342 0.5051 0.0134  0.1048  -0.0521 276  GLU A N   
1185 C CA  . GLU A 181 ? 0.7070 0.7926 0.5682 0.0140  0.1156  -0.0552 276  GLU A CA  
1186 C C   . GLU A 181 ? 0.6894 0.7768 0.5640 0.0164  0.1161  -0.0468 276  GLU A C   
1187 O O   . GLU A 181 ? 0.6575 0.7440 0.5263 0.0156  0.1115  -0.0377 276  GLU A O   
1188 C CB  . GLU A 181 ? 0.7356 0.8214 0.5766 0.0094  0.1228  -0.0575 276  GLU A CB  
1189 C CG  . GLU A 181 ? 0.7836 0.8724 0.6302 0.0092  0.1341  -0.0579 276  GLU A CG  
1190 C CD  . GLU A 181 ? 0.8897 0.9784 0.7143 0.0040  0.1414  -0.0588 276  GLU A CD  
1191 O OE1 . GLU A 181 ? 0.9197 1.0065 0.7284 0.0013  0.1421  -0.0657 276  GLU A OE1 
1192 O OE2 . GLU A 181 ? 0.9617 1.0517 0.7842 0.0023  0.1465  -0.0526 276  GLU A OE2 
1193 N N   . LEU A 182 ? 0.6451 0.7348 0.5378 0.0195  0.1213  -0.0499 277  LEU A N   
1194 C CA  . LEU A 182 ? 0.6564 0.7481 0.5632 0.0217  0.1208  -0.0430 277  LEU A CA  
1195 C C   . LEU A 182 ? 0.6737 0.7670 0.5724 0.0185  0.1264  -0.0377 277  LEU A C   
1196 O O   . LEU A 182 ? 0.6665 0.7610 0.5550 0.0154  0.1342  -0.0416 277  LEU A O   
1197 C CB  . LEU A 182 ? 0.6483 0.7427 0.5756 0.0256  0.1247  -0.0479 277  LEU A CB  
1198 C CG  . LEU A 182 ? 0.6830 0.7754 0.6244 0.0297  0.1173  -0.0467 277  LEU A CG  
1199 C CD1 . LEU A 182 ? 0.6549 0.7433 0.5902 0.0294  0.1122  -0.0510 277  LEU A CD1 
1200 C CD2 . LEU A 182 ? 0.7318 0.8271 0.6924 0.0337  0.1213  -0.0505 277  LEU A CD2 
1201 N N   . PRO A 183 ? 0.6571 0.7497 0.5597 0.0188  0.1230  -0.0290 278  PRO A N   
1202 C CA  . PRO A 183 ? 0.6418 0.7349 0.5376 0.0153  0.1286  -0.0237 278  PRO A CA  
1203 C C   . PRO A 183 ? 0.6418 0.7406 0.5491 0.0148  0.1386  -0.0282 278  PRO A C   
1204 O O   . PRO A 183 ? 0.6698 0.7698 0.5690 0.0108  0.1461  -0.0269 278  PRO A O   
1205 C CB  . PRO A 183 ? 0.6231 0.7135 0.5241 0.0165  0.1222  -0.0145 278  PRO A CB  
1206 C CG  . PRO A 183 ? 0.6261 0.7177 0.5442 0.0211  0.1168  -0.0168 278  PRO A CG  
1207 C CD  . PRO A 183 ? 0.6468 0.7380 0.5612 0.0222  0.1150  -0.0241 278  PRO A CD  
1208 N N   . PHE A 184 ? 0.6182 0.7207 0.5445 0.0188  0.1388  -0.0331 279  PHE A N   
1209 C CA  . PHE A 184 ? 0.6248 0.7341 0.5646 0.0193  0.1477  -0.0385 279  PHE A CA  
1210 C C   . PHE A 184 ? 0.6420 0.7529 0.5978 0.0245  0.1458  -0.0450 279  PHE A C   
1211 O O   . PHE A 184 ? 0.6480 0.7547 0.6048 0.0272  0.1379  -0.0443 279  PHE A O   
1212 C CB  . PHE A 184 ? 0.6326 0.7456 0.5831 0.0180  0.1498  -0.0328 279  PHE A CB  
1213 C CG  . PHE A 184 ? 0.6212 0.7315 0.5795 0.0203  0.1407  -0.0263 279  PHE A CG  
1214 C CD1 . PHE A 184 ? 0.6136 0.7185 0.5613 0.0178  0.1367  -0.0181 279  PHE A CD1 
1215 C CD2 . PHE A 184 ? 0.6186 0.7313 0.5944 0.0250  0.1366  -0.0283 279  PHE A CD2 
1216 C CE1 . PHE A 184 ? 0.6354 0.7376 0.5902 0.0199  0.1292  -0.0128 279  PHE A CE1 
1217 C CE2 . PHE A 184 ? 0.6006 0.7104 0.5821 0.0267  0.1288  -0.0226 279  PHE A CE2 
1218 C CZ  . PHE A 184 ? 0.5609 0.6657 0.5322 0.0242  0.1254  -0.0152 279  PHE A CZ  
1219 N N   . LEU A 185 ? 0.6092 0.7263 0.5780 0.0260  0.1534  -0.0511 280  LEU A N   
1220 C CA  . LEU A 185 ? 0.6275 0.7458 0.6120 0.0314  0.1524  -0.0573 280  LEU A CA  
1221 C C   . LEU A 185 ? 0.6131 0.7347 0.6170 0.0351  0.1477  -0.0531 280  LEU A C   
1222 O O   . LEU A 185 ? 0.6116 0.7391 0.6233 0.0336  0.1504  -0.0499 280  LEU A O   
1223 C CB  . LEU A 185 ? 0.6219 0.7450 0.6113 0.0320  0.1630  -0.0664 280  LEU A CB  
1224 C CG  . LEU A 185 ? 0.6253 0.7442 0.5942 0.0285  0.1675  -0.0719 280  LEU A CG  
1225 C CD1 . LEU A 185 ? 0.5938 0.7175 0.5683 0.0292  0.1789  -0.0816 280  LEU A CD1 
1226 C CD2 . LEU A 185 ? 0.6126 0.7234 0.5737 0.0299  0.1595  -0.0738 280  LEU A CD2 
1227 N N   . LEU A 186 ? 0.5962 0.7139 0.6073 0.0394  0.1406  -0.0532 281  LEU A N   
1228 C CA  . LEU A 186 ? 0.5888 0.7093 0.6171 0.0430  0.1358  -0.0496 281  LEU A CA  
1229 C C   . LEU A 186 ? 0.5878 0.7170 0.6344 0.0457  0.1417  -0.0537 281  LEU A C   
1230 O O   . LEU A 186 ? 0.6048 0.7395 0.6640 0.0466  0.1397  -0.0500 281  LEU A O   
1231 C CB  . LEU A 186 ? 0.6143 0.7284 0.6460 0.0469  0.1281  -0.0493 281  LEU A CB  
1232 C CG  . LEU A 186 ? 0.5831 0.6911 0.6035 0.0450  0.1204  -0.0429 281  LEU A CG  
1233 C CD1 . LEU A 186 ? 0.5609 0.6638 0.5876 0.0487  0.1138  -0.0423 281  LEU A CD1 
1234 C CD2 . LEU A 186 ? 0.5739 0.6846 0.5953 0.0429  0.1186  -0.0358 281  LEU A CD2 
1235 N N   . LYS A 187 ? 0.5759 0.7067 0.6249 0.0472  0.1488  -0.0617 282  LYS A N   
1236 C CA  . LYS A 187 ? 0.5997 0.7400 0.6672 0.0501  0.1552  -0.0660 282  LYS A CA  
1237 C C   . LYS A 187 ? 0.6108 0.7596 0.6805 0.0456  0.1602  -0.0630 282  LYS A C   
1238 O O   . LYS A 187 ? 0.6273 0.7851 0.7153 0.0474  0.1608  -0.0624 282  LYS A O   
1239 C CB  . LYS A 187 ? 0.6313 0.7712 0.6981 0.0515  0.1636  -0.0757 282  LYS A CB  
1240 C CG  . LYS A 187 ? 0.6796 0.8299 0.7662 0.0548  0.1715  -0.0811 282  LYS A CG  
1241 C CD  . LYS A 187 ? 0.7730 0.9235 0.8545 0.0543  0.1825  -0.0909 282  LYS A CD  
1242 N N   . ASP A 188 ? 0.6031 0.7492 0.6542 0.0395  0.1634  -0.0609 283  ASP A N   
1243 C CA  . ASP A 188 ? 0.6278 0.7800 0.6789 0.0344  0.1681  -0.0571 283  ASP A CA  
1244 C C   . ASP A 188 ? 0.6189 0.7701 0.6731 0.0333  0.1598  -0.0488 283  ASP A C   
1245 O O   . ASP A 188 ? 0.6057 0.7646 0.6728 0.0320  0.1613  -0.0470 283  ASP A O   
1246 C CB  . ASP A 188 ? 0.6266 0.7747 0.6553 0.0283  0.1740  -0.0568 283  ASP A CB  
1247 C CG  . ASP A 188 ? 0.6885 0.8389 0.7139 0.0283  0.1840  -0.0658 283  ASP A CG  
1248 O OD1 . ASP A 188 ? 0.6897 0.8481 0.7338 0.0318  0.1893  -0.0716 283  ASP A OD1 
1249 O OD2 . ASP A 188 ? 0.6620 0.8063 0.6662 0.0249  0.1865  -0.0671 283  ASP A OD2 
1250 N N   . ALA A 189 ? 0.5725 0.7144 0.6154 0.0338  0.1513  -0.0441 284  ALA A N   
1251 C CA  . ALA A 189 ? 0.5835 0.7237 0.6285 0.0329  0.1440  -0.0368 284  ALA A CA  
1252 C C   . ALA A 189 ? 0.5501 0.6961 0.6157 0.0372  0.1396  -0.0369 284  ALA A C   
1253 O O   . ALA A 189 ? 0.5519 0.7002 0.6232 0.0355  0.1364  -0.0325 284  ALA A O   
1254 C CB  . ALA A 189 ? 0.5952 0.7250 0.6255 0.0331  0.1363  -0.0324 284  ALA A CB  
1255 N N   . ASN A 190 ? 0.5583 0.7066 0.6350 0.0426  0.1396  -0.0420 285  ASN A N   
1256 C CA  . ASN A 190 ? 0.5598 0.7134 0.6555 0.0473  0.1347  -0.0418 285  ASN A CA  
1257 C C   . ASN A 190 ? 0.5688 0.7354 0.6826 0.0472  0.1400  -0.0444 285  ASN A C   
1258 O O   . ASN A 190 ? 0.5758 0.7481 0.7052 0.0502  0.1350  -0.0431 285  ASN A O   
1259 C CB  . ASN A 190 ? 0.5338 0.6835 0.6344 0.0536  0.1321  -0.0454 285  ASN A CB  
1260 C CG  . ASN A 190 ? 0.5375 0.6771 0.6296 0.0550  0.1233  -0.0411 285  ASN A CG  
1261 O OD1 . ASN A 190 ? 0.5163 0.6559 0.6120 0.0553  0.1168  -0.0359 285  ASN A OD1 
1262 N ND2 . ASN A 190 ? 0.4924 0.6237 0.5728 0.0553  0.1233  -0.0433 285  ASN A ND2 
1263 N N   . MET A 191 ? 0.5595 0.7313 0.6718 0.0437  0.1499  -0.0482 286  MET A N   
1264 C CA  . MET A 191 ? 0.6237 0.8090 0.7556 0.0442  0.1561  -0.0521 286  MET A CA  
1265 C C   . MET A 191 ? 0.6038 0.7962 0.7440 0.0400  0.1539  -0.0476 286  MET A C   
1266 O O   . MET A 191 ? 0.6104 0.7981 0.7374 0.0340  0.1540  -0.0431 286  MET A O   
1267 C CB  . MET A 191 ? 0.6769 0.8654 0.8034 0.0411  0.1684  -0.0577 286  MET A CB  
1268 C CG  . MET A 191 ? 0.7599 0.9616 0.9082 0.0442  0.1759  -0.0644 286  MET A CG  
1269 S SD  . MET A 191 ? 1.0433 1.2421 1.2000 0.0534  0.1757  -0.0714 286  MET A SD  
1270 C CE  . MET A 191 ? 0.8152 1.0038 0.9465 0.0499  0.1838  -0.0762 286  MET A CE  
1271 N N   . LYS A 192 ? 0.6299 0.8334 0.7922 0.0432  0.1516  -0.0489 287  LYS A N   
1272 C CA  . LYS A 192 ? 0.6741 0.8874 0.8475 0.0385  0.1518  -0.0468 287  LYS A CA  
1273 C C   . LYS A 192 ? 0.7621 0.9801 0.9319 0.0318  0.1637  -0.0490 287  LYS A C   
1274 O O   . LYS A 192 ? 0.7921 1.0143 0.9648 0.0330  0.1726  -0.0547 287  LYS A O   
1275 C CB  . LYS A 192 ? 0.6435 0.8703 0.8432 0.0435  0.1483  -0.0491 287  LYS A CB  
1276 C CG  . LYS A 192 ? 0.6978 0.9372 0.9119 0.0383  0.1491  -0.0483 287  LYS A CG  
1277 C CD  . LYS A 192 ? 0.6642 0.9126 0.8980 0.0430  0.1393  -0.0473 287  LYS A CD  
1278 C CE  . LYS A 192 ? 0.7133 0.9687 0.9646 0.0519  0.1396  -0.0518 287  LYS A CE  
1279 N NZ  . LYS A 192 ? 0.7185 0.9913 0.9967 0.0540  0.1360  -0.0530 287  LYS A NZ  
1280 N N   . GLU A 193 ? 0.7296 0.9457 0.8917 0.0244  0.1643  -0.0445 288  GLU A N   
1281 C CA  . GLU A 193 ? 0.9241 1.1408 1.0770 0.0174  0.1755  -0.0451 288  GLU A CA  
1282 C C   . GLU A 193 ? 1.0308 1.2641 1.2052 0.0153  0.1840  -0.0499 288  GLU A C   
1283 O O   . GLU A 193 ? 0.9788 1.2223 1.1717 0.0144  0.1803  -0.0493 288  GLU A O   
1284 C CB  . GLU A 193 ? 1.0035 1.2108 1.1404 0.0103  0.1736  -0.0383 288  GLU A CB  
1285 C CG  . GLU A 193 ? 1.0655 1.2623 1.1783 0.0065  0.1802  -0.0366 288  GLU A CG  
1286 C CD  . GLU A 193 ? 1.1016 1.2898 1.2003 -0.0007 0.1799  -0.0297 288  GLU A CD  
1287 O OE1 . GLU A 193 ? 1.0252 1.2068 1.1216 -0.0001 0.1707  -0.0251 288  GLU A OE1 
1288 O OE2 . GLU A 193 ? 1.1612 1.3488 1.2511 -0.0069 0.1894  -0.0289 288  GLU A OE2 
1289 N N   . THR A 194 ? 1.1027 1.3394 1.2747 0.0142  0.1957  -0.0548 289  THR A N   
1290 C CA  . THR A 194 ? 1.1522 1.4057 1.3463 0.0136  0.2051  -0.0607 289  THR A CA  
1291 C C   . THR A 194 ? 1.2077 1.4608 1.3891 0.0064  0.2191  -0.0623 289  THR A C   
1292 O O   . THR A 194 ? 1.2231 1.4626 1.3785 0.0031  0.2207  -0.0590 289  THR A O   
1293 C CB  . THR A 194 ? 1.1775 1.4376 1.3877 0.0231  0.2050  -0.0674 289  THR A CB  
1294 O OG1 . THR A 194 ? 1.2358 1.5146 1.4744 0.0238  0.2102  -0.0720 289  THR A OG1 
1295 C CG2 . THR A 194 ? 1.1982 1.4511 1.3928 0.0246  0.2137  -0.0723 289  THR A CG2 
1296 N N   . ASN A 195 ? 1.2295 1.4980 1.4299 0.0039  0.2293  -0.0670 290  ASN A N   
1297 C CA  . ASN A 195 ? 1.2638 1.5339 1.4547 -0.0022 0.2445  -0.0699 290  ASN A CA  
1298 C C   . ASN A 195 ? 1.2377 1.5154 1.4378 0.0034  0.2536  -0.0791 290  ASN A C   
1299 O O   . ASN A 195 ? 1.2436 1.5219 1.4348 -0.0009 0.2651  -0.0817 290  ASN A O   
1300 C CB  . ASN A 195 ? 1.2378 1.5190 1.4412 -0.0110 0.2517  -0.0685 290  ASN A CB  
1301 C CG  . ASN A 195 ? 1.2379 1.5062 1.4192 -0.0199 0.2507  -0.0600 290  ASN A CG  
1302 O OD1 . ASN A 195 ? 1.2640 1.5176 1.4175 -0.0219 0.2523  -0.0568 290  ASN A OD1 
1303 N ND2 . ASN A 195 ? 1.2229 1.4967 1.4168 -0.0253 0.2477  -0.0565 290  ASN A ND2 
1304 N N   . GLU A 196 ? 1.1986 1.4795 1.4139 0.0131  0.2467  -0.0830 291  GLU A N   
1305 C CA  . GLU A 196 ? 1.2062 1.4907 1.4285 0.0196  0.2532  -0.0911 291  GLU A CA  
1306 C C   . GLU A 196 ? 1.2520 1.5227 1.4442 0.0173  0.2597  -0.0928 291  GLU A C   
1307 O O   . GLU A 196 ? 1.2717 1.5288 1.4418 0.0161  0.2551  -0.0894 291  GLU A O   
1308 C CB  . GLU A 196 ? 1.1731 1.4581 1.4108 0.0303  0.2437  -0.0937 291  GLU A CB  
1309 C CG  . GLU A 196 ? 1.1273 1.4249 1.3929 0.0338  0.2344  -0.0913 291  GLU A CG  
1310 C CD  . GLU A 196 ? 1.1246 1.4172 1.3972 0.0439  0.2218  -0.0906 291  GLU A CD  
1311 O OE1 . GLU A 196 ? 1.1099 1.4088 1.3987 0.0464  0.2112  -0.0868 291  GLU A OE1 
1312 O OE2 . GLU A 196 ? 1.1338 1.4157 1.3952 0.0488  0.2226  -0.0940 291  GLU A OE2 
1313 N N   . GLU A 197 ? 1.2627 1.5364 1.4535 0.0167  0.2690  -0.0976 292  GLU A N   
1314 C CA  . GLU A 197 ? 1.2984 1.5603 1.4603 0.0135  0.2759  -0.0995 292  GLU A CA  
1315 C C   . GLU A 197 ? 1.3049 1.5539 1.4519 0.0187  0.2703  -0.1018 292  GLU A C   
1316 O O   . GLU A 197 ? 1.3036 1.5539 1.4660 0.0272  0.2648  -0.1056 292  GLU A O   
1317 C CB  . GLU A 197 ? 1.2761 1.5445 1.4436 0.0144  0.2860  -0.1060 292  GLU A CB  
1318 N N   . GLY A 198 ? 1.2851 1.5214 1.4018 0.0135  0.2716  -0.0992 293  GLY A N   
1319 C CA  . GLY A 198 ? 1.2604 1.4843 1.3610 0.0171  0.2663  -0.1012 293  GLY A CA  
1320 C C   . GLY A 198 ? 1.2530 1.4696 1.3514 0.0188  0.2518  -0.0934 293  GLY A C   
1321 O O   . GLY A 198 ? 1.2147 1.4215 1.3055 0.0235  0.2435  -0.0940 293  GLY A O   
1322 N N   . SER A 199 ? 1.2290 1.4491 1.3335 0.0150  0.2473  -0.0856 294  SER A N   
1323 C CA  . SER A 199 ? 1.1786 1.3910 1.2801 0.0164  0.2327  -0.0774 294  SER A CA  
1324 C C   . SER A 199 ? 1.1141 1.3127 1.1854 0.0108  0.2296  -0.0707 294  SER A C   
1325 O O   . SER A 199 ? 1.1037 1.3017 1.1621 0.0034  0.2373  -0.0681 294  SER A O   
1326 C CB  . SER A 199 ? 1.2064 1.4286 1.3285 0.0149  0.2289  -0.0728 294  SER A CB  
1327 O OG  . SER A 199 ? 1.2089 1.4277 1.3179 0.0064  0.2308  -0.0659 294  SER A OG  
1328 N N   . ILE A 200 ? 1.0344 1.2221 1.0949 0.0143  0.2186  -0.0678 295  ILE A N   
1329 C CA  . ILE A 200 ? 0.9672 1.1424 1.0022 0.0102  0.2132  -0.0606 295  ILE A CA  
1330 C C   . ILE A 200 ? 0.9379 1.1106 0.9791 0.0105  0.2022  -0.0525 295  ILE A C   
1331 O O   . ILE A 200 ? 0.8748 1.0471 0.9275 0.0163  0.1932  -0.0525 295  ILE A O   
1332 C CB  . ILE A 200 ? 0.9397 1.1047 0.9575 0.0132  0.2089  -0.0634 295  ILE A CB  
1333 C CG1 . ILE A 200 ? 0.9309 1.0988 0.9455 0.0137  0.2196  -0.0733 295  ILE A CG1 
1334 C CG2 . ILE A 200 ? 0.8864 1.0401 0.8776 0.0085  0.2043  -0.0561 295  ILE A CG2 
1335 C CD1 . ILE A 200 ? 0.9848 1.1517 0.9794 0.0063  0.2303  -0.0733 295  ILE A CD1 
1336 N N   . LYS A 201 ? 0.9245 1.0952 0.9581 0.0042  0.2035  -0.0457 296  LYS A N   
1337 C CA  . LYS A 201 ? 0.8099 0.9759 0.8453 0.0037  0.1937  -0.0380 296  LYS A CA  
1338 C C   . LYS A 201 ? 0.7581 0.9104 0.7703 0.0034  0.1866  -0.0323 296  LYS A C   
1339 O O   . LYS A 201 ? 0.7668 0.9133 0.7587 -0.0001 0.1910  -0.0313 296  LYS A O   
1340 C CB  . LYS A 201 ? 0.7897 0.9600 0.8306 -0.0030 0.1986  -0.0338 296  LYS A CB  
1341 N N   . VAL A 202 ? 0.6976 0.8450 0.7129 0.0071  0.1755  -0.0287 297  VAL A N   
1342 C CA  . VAL A 202 ? 0.6739 0.8095 0.6711 0.0069  0.1680  -0.0224 297  VAL A CA  
1343 C C   . VAL A 202 ? 0.6209 0.7535 0.6204 0.0037  0.1647  -0.0151 297  VAL A C   
1344 O O   . VAL A 202 ? 0.6186 0.7551 0.6343 0.0057  0.1601  -0.0150 297  VAL A O   
1345 C CB  . VAL A 202 ? 0.6601 0.7919 0.6588 0.0132  0.1587  -0.0240 297  VAL A CB  
1346 C CG1 . VAL A 202 ? 0.6220 0.7430 0.6009 0.0128  0.1525  -0.0188 297  VAL A CG1 
1347 C CG2 . VAL A 202 ? 0.6380 0.7745 0.6418 0.0168  0.1627  -0.0327 297  VAL A CG2 
1348 N N   . ASN A 203 ? 0.5903 0.7157 0.5734 -0.0014 0.1671  -0.0091 298  ASN A N   
1349 C CA  . ASN A 203 ? 0.6171 0.7393 0.6028 -0.0054 0.1661  -0.0028 298  ASN A CA  
1350 C C   . ASN A 203 ? 0.6141 0.7271 0.5956 -0.0023 0.1554  0.0025  298  ASN A C   
1351 O O   . ASN A 203 ? 0.5754 0.6841 0.5494 0.0020  0.1492  0.0025  298  ASN A O   
1352 C CB  . ASN A 203 ? 0.6342 0.7520 0.6055 -0.0124 0.1743  0.0017  298  ASN A CB  
1353 C CG  . ASN A 203 ? 0.7126 0.8200 0.6592 -0.0126 0.1724  0.0062  298  ASN A CG  
1354 O OD1 . ASN A 203 ? 0.7344 0.8346 0.6743 -0.0087 0.1632  0.0095  298  ASN A OD1 
1355 N ND2 . ASN A 203 ? 0.7889 0.8958 0.7218 -0.0173 0.1812  0.0064  298  ASN A ND2 
1356 N N   . GLN A 204 ? 0.6265 0.7370 0.6141 -0.0049 0.1537  0.0067  299  GLN A N   
1357 C CA  . GLN A 204 ? 0.6301 0.7331 0.6173 -0.0019 0.1443  0.0108  299  GLN A CA  
1358 C C   . GLN A 204 ? 0.6041 0.6962 0.5721 -0.0006 0.1404  0.0163  299  GLN A C   
1359 O O   . GLN A 204 ? 0.6281 0.7167 0.5949 0.0041  0.1327  0.0169  299  GLN A O   
1360 C CB  . GLN A 204 ? 0.6043 0.7054 0.5993 -0.0060 0.1446  0.0140  299  GLN A CB  
1361 C CG  . GLN A 204 ? 0.5751 0.6659 0.5661 -0.0042 0.1369  0.0190  299  GLN A CG  
1362 C CD  . GLN A 204 ? 0.6127 0.7027 0.6137 -0.0083 0.1374  0.0202  299  GLN A CD  
1363 O OE1 . GLN A 204 ? 0.5814 0.6780 0.5968 -0.0071 0.1342  0.0163  299  GLN A OE1 
1364 N NE2 . GLN A 204 ? 0.6156 0.6972 0.6084 -0.0135 0.1413  0.0255  299  GLN A NE2 
1365 N N   . ASP A 205 ? 0.6045 0.6915 0.5576 -0.0049 0.1456  0.0204  300  ASP A N   
1366 C CA  . ASP A 205 ? 0.6519 0.7289 0.5869 -0.0037 0.1411  0.0265  300  ASP A CA  
1367 C C   . ASP A 205 ? 0.6272 0.7063 0.5565 0.0010  0.1367  0.0226  300  ASP A C   
1368 O O   . ASP A 205 ? 0.6378 0.7118 0.5625 0.0048  0.1288  0.0253  300  ASP A O   
1369 C CB  . ASP A 205 ? 0.7267 0.7983 0.6458 -0.0094 0.1480  0.0316  300  ASP A CB  
1370 C CG  . ASP A 205 ? 0.8754 0.9348 0.7787 -0.0087 0.1427  0.0404  300  ASP A CG  
1371 O OD1 . ASP A 205 ? 0.9241 0.9770 0.8326 -0.0081 0.1389  0.0449  300  ASP A OD1 
1372 O OD2 . ASP A 205 ? 0.9256 0.9818 0.8116 -0.0087 0.1422  0.0428  300  ASP A OD2 
1373 N N   . ASN A 206 ? 0.6417 0.7284 0.5721 0.0006  0.1421  0.0160  301  ASN A N   
1374 C CA  . ASN A 206 ? 0.6368 0.7253 0.5622 0.0043  0.1389  0.0112  301  ASN A CA  
1375 C C   . ASN A 206 ? 0.6105 0.7008 0.5493 0.0099  0.1311  0.0084  301  ASN A C   
1376 O O   . ASN A 206 ? 0.6061 0.6931 0.5393 0.0131  0.1243  0.0088  301  ASN A O   
1377 C CB  . ASN A 206 ? 0.6404 0.7366 0.5670 0.0026  0.1477  0.0037  301  ASN A CB  
1378 C CG  . ASN A 206 ? 0.7190 0.8151 0.6349 0.0046  0.1464  -0.0011 301  ASN A CG  
1379 O OD1 . ASN A 206 ? 0.7804 0.8711 0.6869 0.0068  0.1386  0.0015  301  ASN A OD1 
1380 N ND2 . ASN A 206 ? 0.7589 0.8612 0.6764 0.0038  0.1542  -0.0087 301  ASN A ND2 
1381 N N   . ARG A 207 ? 0.5963 0.6919 0.5529 0.0108  0.1319  0.0060  302  ARG A N   
1382 C CA  . ARG A 207 ? 0.5797 0.6765 0.5485 0.0157  0.1249  0.0040  302  ARG A CA  
1383 C C   . ARG A 207 ? 0.5961 0.6851 0.5602 0.0173  0.1173  0.0101  302  ARG A C   
1384 O O   . ARG A 207 ? 0.5420 0.6292 0.5060 0.0212  0.1111  0.0094  302  ARG A O   
1385 C CB  . ARG A 207 ? 0.5157 0.6196 0.5029 0.0157  0.1268  0.0013  302  ARG A CB  
1386 C CG  . ARG A 207 ? 0.5570 0.6703 0.5534 0.0159  0.1334  -0.0057 302  ARG A CG  
1387 C CD  . ARG A 207 ? 0.5492 0.6703 0.5647 0.0160  0.1341  -0.0076 302  ARG A CD  
1388 N NE  . ARG A 207 ? 0.5565 0.6876 0.5838 0.0170  0.1400  -0.0143 302  ARG A NE  
1389 C CZ  . ARG A 207 ? 0.5592 0.6951 0.5991 0.0222  0.1373  -0.0188 302  ARG A CZ  
1390 N NH1 . ARG A 207 ? 0.5008 0.6322 0.5417 0.0264  0.1290  -0.0175 302  ARG A NH1 
1391 N NH2 . ARG A 207 ? 0.5785 0.7238 0.6307 0.0232  0.1432  -0.0246 302  ARG A NH2 
1392 N N   . LEU A 208 ? 0.5819 0.6658 0.5430 0.0144  0.1179  0.0159  303  LEU A N   
1393 C CA  . LEU A 208 ? 0.5707 0.6471 0.5297 0.0164  0.1113  0.0212  303  LEU A CA  
1394 C C   . LEU A 208 ? 0.5470 0.6180 0.4914 0.0179  0.1073  0.0248  303  LEU A C   
1395 O O   . LEU A 208 ? 0.5635 0.6315 0.5085 0.0215  0.1007  0.0265  303  LEU A O   
1396 C CB  . LEU A 208 ? 0.5497 0.6213 0.5100 0.0128  0.1134  0.0260  303  LEU A CB  
1397 C CG  . LEU A 208 ? 0.5995 0.6766 0.5754 0.0113  0.1155  0.0225  303  LEU A CG  
1398 C CD1 . LEU A 208 ? 0.6169 0.6879 0.5933 0.0073  0.1172  0.0270  303  LEU A CD1 
1399 C CD2 . LEU A 208 ? 0.5022 0.5825 0.4888 0.0160  0.1094  0.0192  303  LEU A CD2 
1400 N N   . ASN A 209 ? 0.5718 0.6421 0.5030 0.0151  0.1112  0.0257  304  ASN A N   
1401 C CA  . ASN A 209 ? 0.6315 0.6981 0.5483 0.0164  0.1068  0.0285  304  ASN A CA  
1402 C C   . ASN A 209 ? 0.6362 0.7074 0.5553 0.0197  0.1028  0.0225  304  ASN A C   
1403 O O   . ASN A 209 ? 0.6969 0.7658 0.6082 0.0216  0.0968  0.0245  304  ASN A O   
1404 C CB  . ASN A 209 ? 0.6082 0.6730 0.5086 0.0121  0.1122  0.0307  304  ASN A CB  
1405 C CG  . ASN A 209 ? 0.6404 0.6981 0.5351 0.0086  0.1153  0.0384  304  ASN A CG  
1406 O OD1 . ASN A 209 ? 0.6227 0.6751 0.5231 0.0099  0.1120  0.0430  304  ASN A OD1 
1407 N ND2 . ASN A 209 ? 0.6421 0.6989 0.5246 0.0039  0.1221  0.0398  304  ASN A ND2 
1408 N N   . ASN A 210 ? 0.5675 0.6452 0.4974 0.0204  0.1060  0.0153  305  ASN A N   
1409 C CA  . ASN A 210 ? 0.5708 0.6518 0.5045 0.0234  0.1028  0.0093  305  ASN A CA  
1410 C C   . ASN A 210 ? 0.5631 0.6466 0.5139 0.0266  0.1006  0.0068  305  ASN A C   
1411 O O   . ASN A 210 ? 0.5200 0.6080 0.4793 0.0281  0.1025  0.0007  305  ASN A O   
1412 C CB  . ASN A 210 ? 0.5912 0.6763 0.5202 0.0217  0.1089  0.0028  305  ASN A CB  
1413 C CG  . ASN A 210 ? 0.6135 0.6957 0.5230 0.0182  0.1109  0.0053  305  ASN A CG  
1414 O OD1 . ASN A 210 ? 0.5987 0.6785 0.4975 0.0188  0.1055  0.0062  305  ASN A OD1 
1415 N ND2 . ASN A 210 ? 0.6147 0.6974 0.5193 0.0142  0.1186  0.0066  305  ASN A ND2 
1416 N N   . ARG A 211 ? 0.5418 0.6220 0.4974 0.0276  0.0971  0.0117  306  ARG A N   
1417 C CA  . ARG A 211 ? 0.4932 0.5752 0.4632 0.0299  0.0951  0.0103  306  ARG A CA  
1418 C C   . ARG A 211 ? 0.5021 0.5860 0.4781 0.0334  0.0915  0.0060  306  ARG A C   
1419 O O   . ARG A 211 ? 0.4841 0.5713 0.4713 0.0351  0.0920  0.0028  306  ARG A O   
1420 C CB  . ARG A 211 ? 0.4765 0.5531 0.4471 0.0303  0.0916  0.0161  306  ARG A CB  
1421 C CG  . ARG A 211 ? 0.4448 0.5227 0.4280 0.0315  0.0904  0.0152  306  ARG A CG  
1422 C CD  . ARG A 211 ? 0.4805 0.5638 0.4716 0.0291  0.0956  0.0124  306  ARG A CD  
1423 N NE  . ARG A 211 ? 0.4650 0.5480 0.4647 0.0288  0.0942  0.0133  306  ARG A NE  
1424 C CZ  . ARG A 211 ? 0.5009 0.5896 0.5107 0.0274  0.0964  0.0106  306  ARG A CZ  
1425 N NH1 . ARG A 211 ? 0.4806 0.5764 0.4953 0.0269  0.1005  0.0066  306  ARG A NH1 
1426 N NH2 . ARG A 211 ? 0.4113 0.4989 0.4267 0.0264  0.0945  0.0117  306  ARG A NH2 
1427 N N   . CYS A 212 ? 0.5148 0.5966 0.4838 0.0345  0.0875  0.0061  307  CYS A N   
1428 C CA  . CYS A 212 ? 0.4828 0.5657 0.4579 0.0372  0.0844  0.0020  307  CYS A CA  
1429 C C   . CYS A 212 ? 0.5163 0.6028 0.4953 0.0374  0.0886  -0.0047 307  CYS A C   
1430 O O   . CYS A 212 ? 0.5136 0.6007 0.5012 0.0399  0.0873  -0.0080 307  CYS A O   
1431 C CB  . CYS A 212 ? 0.6107 0.6916 0.5783 0.0376  0.0794  0.0028  307  CYS A CB  
1432 S SG  . CYS A 212 ? 0.7272 0.8087 0.7022 0.0399  0.0762  -0.0026 307  CYS A SG  
1433 N N   . VAL A 213 ? 0.4927 0.5813 0.4655 0.0349  0.0941  -0.0068 308  VAL A N   
1434 C CA  . VAL A 213 ? 0.5161 0.6085 0.4943 0.0355  0.0992  -0.0135 308  VAL A CA  
1435 C C   . VAL A 213 ? 0.5092 0.6061 0.5001 0.0360  0.1028  -0.0137 308  VAL A C   
1436 O O   . VAL A 213 ? 0.4867 0.5864 0.4894 0.0389  0.1034  -0.0176 308  VAL A O   
1437 C CB  . VAL A 213 ? 0.5518 0.6449 0.5171 0.0324  0.1042  -0.0164 308  VAL A CB  
1438 C CG1 . VAL A 213 ? 0.5760 0.6734 0.5477 0.0329  0.1111  -0.0239 308  VAL A CG1 
1439 C CG2 . VAL A 213 ? 0.5275 0.6171 0.4810 0.0319  0.0995  -0.0170 308  VAL A CG2 
1440 N N   . ASP A 214 ? 0.4963 0.5937 0.4853 0.0333  0.1048  -0.0093 309  ASP A N   
1441 C CA  . ASP A 214 ? 0.4899 0.5922 0.4911 0.0330  0.1077  -0.0094 309  ASP A CA  
1442 C C   . ASP A 214 ? 0.4919 0.5948 0.5057 0.0366  0.1026  -0.0093 309  ASP A C   
1443 O O   . ASP A 214 ? 0.4181 0.5267 0.4445 0.0381  0.1042  -0.0121 309  ASP A O   
1444 C CB  . ASP A 214 ? 0.4867 0.5873 0.4832 0.0291  0.1092  -0.0040 309  ASP A CB  
1445 C CG  . ASP A 214 ? 0.5045 0.6109 0.5136 0.0277  0.1123  -0.0045 309  ASP A CG  
1446 O OD1 . ASP A 214 ? 0.5037 0.6172 0.5218 0.0281  0.1169  -0.0093 309  ASP A OD1 
1447 O OD2 . ASP A 214 ? 0.5338 0.6377 0.5443 0.0261  0.1102  -0.0002 309  ASP A OD2 
1448 N N   . LEU A 215 ? 0.4595 0.5571 0.4702 0.0381  0.0965  -0.0061 310  LEU A N   
1449 C CA  . LEU A 215 ? 0.4568 0.5541 0.4771 0.0410  0.0919  -0.0053 310  LEU A CA  
1450 C C   . LEU A 215 ? 0.4573 0.5562 0.4854 0.0446  0.0913  -0.0097 310  LEU A C   
1451 O O   . LEU A 215 ? 0.4607 0.5597 0.4970 0.0472  0.0878  -0.0090 310  LEU A O   
1452 C CB  . LEU A 215 ? 0.4583 0.5495 0.4730 0.0416  0.0865  -0.0010 310  LEU A CB  
1453 C CG  . LEU A 215 ? 0.4686 0.5570 0.4792 0.0391  0.0862  0.0038  310  LEU A CG  
1454 C CD1 . LEU A 215 ? 0.4680 0.5507 0.4736 0.0403  0.0815  0.0075  310  LEU A CD1 
1455 C CD2 . LEU A 215 ? 0.4421 0.5335 0.4618 0.0385  0.0865  0.0041  310  LEU A CD2 
1456 N N   . ARG A 216 ? 0.4842 0.5838 0.5094 0.0449  0.0946  -0.0142 311  ARG A N   
1457 C CA  . ARG A 216 ? 0.4853 0.5852 0.5185 0.0484  0.0945  -0.0186 311  ARG A CA  
1458 C C   . ARG A 216 ? 0.4876 0.5942 0.5335 0.0503  0.0982  -0.0219 311  ARG A C   
1459 O O   . ARG A 216 ? 0.5102 0.6166 0.5648 0.0541  0.0975  -0.0247 311  ARG A O   
1460 C CB  . ARG A 216 ? 0.4982 0.5951 0.5231 0.0479  0.0962  -0.0230 311  ARG A CB  
1461 C CG  . ARG A 216 ? 0.4849 0.5768 0.4984 0.0461  0.0920  -0.0199 311  ARG A CG  
1462 C CD  . ARG A 216 ? 0.4511 0.5408 0.4559 0.0449  0.0930  -0.0245 311  ARG A CD  
1463 N NE  . ARG A 216 ? 0.4667 0.5536 0.4604 0.0427  0.0889  -0.0209 311  ARG A NE  
1464 C CZ  . ARG A 216 ? 0.5130 0.5978 0.4983 0.0414  0.0873  -0.0237 311  ARG A CZ  
1465 N NH1 . ARG A 216 ? 0.4941 0.5781 0.4800 0.0416  0.0897  -0.0306 311  ARG A NH1 
1466 N NH2 . ARG A 216 ? 0.4871 0.5706 0.4637 0.0397  0.0829  -0.0197 311  ARG A NH2 
1467 N N   . THR A 217 ? 0.4376 0.5500 0.4858 0.0477  0.1022  -0.0214 312  THR A N   
1468 C CA  . THR A 217 ? 0.4763 0.5967 0.5393 0.0497  0.1051  -0.0243 312  THR A CA  
1469 C C   . THR A 217 ? 0.4462 0.5673 0.5201 0.0532  0.0989  -0.0218 312  THR A C   
1470 O O   . THR A 217 ? 0.4318 0.5487 0.5015 0.0525  0.0936  -0.0172 312  THR A O   
1471 C CB  . THR A 217 ? 0.4547 0.5818 0.5195 0.0456  0.1102  -0.0237 312  THR A CB  
1472 O OG1 . THR A 217 ? 0.4601 0.5862 0.5238 0.0432  0.1061  -0.0183 312  THR A OG1 
1473 C CG2 . THR A 217 ? 0.4676 0.5932 0.5194 0.0416  0.1164  -0.0252 312  THR A CG2 
1474 N N   . TYR A 218 ? 0.4502 0.5766 0.5381 0.0571  0.0997  -0.0249 313  TYR A N   
1475 C CA  . TYR A 218 ? 0.4639 0.5909 0.5614 0.0608  0.0934  -0.0222 313  TYR A CA  
1476 C C   . TYR A 218 ? 0.4699 0.6009 0.5693 0.0579  0.0901  -0.0182 313  TYR A C   
1477 O O   . TYR A 218 ? 0.4297 0.5571 0.5274 0.0586  0.0839  -0.0142 313  TYR A O   
1478 C CB  . TYR A 218 ? 0.4494 0.5822 0.5625 0.0658  0.0949  -0.0260 313  TYR A CB  
1479 C CG  . TYR A 218 ? 0.5259 0.6531 0.6378 0.0689  0.0978  -0.0305 313  TYR A CG  
1480 C CD1 . TYR A 218 ? 0.5087 0.6259 0.6142 0.0707  0.0936  -0.0289 313  TYR A CD1 
1481 C CD2 . TYR A 218 ? 0.4896 0.6213 0.6071 0.0700  0.1052  -0.0368 313  TYR A CD2 
1482 C CE1 . TYR A 218 ? 0.5231 0.6344 0.6278 0.0731  0.0961  -0.0334 313  TYR A CE1 
1483 C CE2 . TYR A 218 ? 0.4774 0.6031 0.5935 0.0727  0.1080  -0.0417 313  TYR A CE2 
1484 C CZ  . TYR A 218 ? 0.5496 0.6650 0.6594 0.0741  0.1032  -0.0399 313  TYR A CZ  
1485 O OH  . TYR A 218 ? 0.5712 0.6797 0.6796 0.0762  0.1057  -0.0450 313  TYR A OH  
1486 N N   . ALA A 219 ? 0.4216 0.5598 0.5239 0.0542  0.0947  -0.0193 314  ALA A N   
1487 C CA  . ALA A 219 ? 0.4715 0.6131 0.5759 0.0507  0.0920  -0.0161 314  ALA A CA  
1488 C C   . ALA A 219 ? 0.4298 0.5623 0.5196 0.0476  0.0893  -0.0119 314  ALA A C   
1489 O O   . ALA A 219 ? 0.4465 0.5777 0.5363 0.0469  0.0842  -0.0089 314  ALA A O   
1490 C CB  . ALA A 219 ? 0.4268 0.5775 0.5375 0.0466  0.0984  -0.0183 314  ALA A CB  
1491 N N   . ASN A 220 ? 0.4164 0.5428 0.4936 0.0457  0.0925  -0.0116 315  ASN A N   
1492 C CA  . ASN A 220 ? 0.4763 0.5948 0.5414 0.0431  0.0900  -0.0074 315  ASN A CA  
1493 C C   . ASN A 220 ? 0.4340 0.5462 0.4963 0.0463  0.0838  -0.0053 315  ASN A C   
1494 O O   . ASN A 220 ? 0.4657 0.5744 0.5247 0.0451  0.0803  -0.0021 315  ASN A O   
1495 C CB  . ASN A 220 ? 0.4005 0.5146 0.4531 0.0407  0.0941  -0.0071 315  ASN A CB  
1496 C CG  . ASN A 220 ? 0.4797 0.5978 0.5315 0.0361  0.1002  -0.0074 315  ASN A CG  
1497 O OD1 . ASN A 220 ? 0.4625 0.5849 0.5214 0.0336  0.1007  -0.0067 315  ASN A OD1 
1498 N ND2 . ASN A 220 ? 0.4341 0.5506 0.4766 0.0345  0.1049  -0.0084 315  ASN A ND2 
1499 N N   . TYR A 221 ? 0.4371 0.5474 0.5005 0.0500  0.0831  -0.0072 316  TYR A N   
1500 C CA  . TYR A 221 ? 0.4534 0.5582 0.5156 0.0528  0.0779  -0.0052 316  TYR A CA  
1501 C C   . TYR A 221 ? 0.4645 0.5718 0.5334 0.0537  0.0735  -0.0031 316  TYR A C   
1502 O O   . TYR A 221 ? 0.4164 0.5189 0.4803 0.0533  0.0697  0.0000  316  TYR A O   
1503 C CB  . TYR A 221 ? 0.4435 0.5464 0.5088 0.0565  0.0782  -0.0080 316  TYR A CB  
1504 C CG  . TYR A 221 ? 0.4618 0.5589 0.5266 0.0591  0.0732  -0.0054 316  TYR A CG  
1505 C CD1 . TYR A 221 ? 0.4817 0.5721 0.5373 0.0579  0.0716  -0.0034 316  TYR A CD1 
1506 C CD2 . TYR A 221 ? 0.4334 0.5318 0.5067 0.0624  0.0699  -0.0046 316  TYR A CD2 
1507 C CE1 . TYR A 221 ? 0.5254 0.6105 0.5803 0.0595  0.0679  -0.0009 316  TYR A CE1 
1508 C CE2 . TYR A 221 ? 0.5011 0.5935 0.5725 0.0643  0.0657  -0.0015 316  TYR A CE2 
1509 C CZ  . TYR A 221 ? 0.4802 0.5658 0.5421 0.0625  0.0652  0.0002  316  TYR A CZ  
1510 O OH  . TYR A 221 ? 0.5227 0.6023 0.5823 0.0637  0.0620  0.0032  316  TYR A OH  
1511 N N   . SER A 222 ? 0.4477 0.5631 0.5280 0.0547  0.0740  -0.0050 317  SER A N   
1512 C CA  . SER A 222 ? 0.4256 0.5445 0.5126 0.0556  0.0689  -0.0032 317  SER A CA  
1513 C C   . SER A 222 ? 0.4121 0.5309 0.4945 0.0510  0.0678  -0.0013 317  SER A C   
1514 O O   . SER A 222 ? 0.4622 0.5788 0.5426 0.0509  0.0628  0.0010  317  SER A O   
1515 C CB  . SER A 222 ? 0.4268 0.5558 0.5287 0.0579  0.0695  -0.0059 317  SER A CB  
1516 O OG  . SER A 222 ? 0.4606 0.5886 0.5675 0.0627  0.0705  -0.0079 317  SER A OG  
1517 N N   . ILE A 223 ? 0.3970 0.5177 0.4774 0.0469  0.0725  -0.0022 318  ILE A N   
1518 C CA  . ILE A 223 ? 0.4275 0.5464 0.5034 0.0422  0.0720  -0.0005 318  ILE A CA  
1519 C C   . ILE A 223 ? 0.4453 0.5544 0.5099 0.0423  0.0692  0.0024  318  ILE A C   
1520 O O   . ILE A 223 ? 0.4435 0.5505 0.5061 0.0408  0.0659  0.0037  318  ILE A O   
1521 C CB  . ILE A 223 ? 0.4416 0.5616 0.5151 0.0379  0.0782  -0.0013 318  ILE A CB  
1522 C CG1 . ILE A 223 ? 0.3784 0.5094 0.4645 0.0366  0.0814  -0.0043 318  ILE A CG1 
1523 C CG2 . ILE A 223 ? 0.3944 0.5084 0.4602 0.0335  0.0781  0.0012  318  ILE A CG2 
1524 C CD1 . ILE A 223 ? 0.4190 0.5511 0.5022 0.0325  0.0888  -0.0051 318  ILE A CD1 
1525 N N   . PHE A 224 ? 0.3974 0.5006 0.4547 0.0440  0.0706  0.0032  319  PHE A N   
1526 C CA  . PHE A 224 ? 0.4446 0.5395 0.4927 0.0438  0.0686  0.0059  319  PHE A CA  
1527 C C   . PHE A 224 ? 0.4615 0.5537 0.5094 0.0467  0.0641  0.0070  319  PHE A C   
1528 O O   . PHE A 224 ? 0.4112 0.4983 0.4533 0.0459  0.0623  0.0088  319  PHE A O   
1529 C CB  . PHE A 224 ? 0.3942 0.4846 0.4348 0.0437  0.0714  0.0066  319  PHE A CB  
1530 C CG  . PHE A 224 ? 0.4374 0.5279 0.4748 0.0401  0.0752  0.0071  319  PHE A CG  
1531 C CD1 . PHE A 224 ? 0.4336 0.5196 0.4670 0.0375  0.0750  0.0093  319  PHE A CD1 
1532 C CD2 . PHE A 224 ? 0.3922 0.4870 0.4311 0.0391  0.0793  0.0053  319  PHE A CD2 
1533 C CE1 . PHE A 224 ? 0.4379 0.5229 0.4686 0.0338  0.0787  0.0103  319  PHE A CE1 
1534 C CE2 . PHE A 224 ? 0.4405 0.5350 0.4758 0.0353  0.0832  0.0063  319  PHE A CE2 
1535 C CZ  . PHE A 224 ? 0.4234 0.5127 0.4547 0.0326  0.0828  0.0091  319  PHE A CZ  
1536 N N   . CYS A 225 ? 0.4300 0.5254 0.4842 0.0500  0.0625  0.0060  320  CYS A N   
1537 C CA  . CYS A 225 ? 0.4257 0.5191 0.4802 0.0523  0.0579  0.0078  320  CYS A CA  
1538 C C   . CYS A 225 ? 0.4531 0.5497 0.5091 0.0503  0.0546  0.0082  320  CYS A C   
1539 O O   . CYS A 225 ? 0.4565 0.5488 0.5068 0.0501  0.0514  0.0101  320  CYS A O   
1540 C CB  . CYS A 225 ? 0.4764 0.5721 0.5383 0.0564  0.0566  0.0070  320  CYS A CB  
1541 S SG  . CYS A 225 ? 0.5256 0.6160 0.5847 0.0584  0.0597  0.0060  320  CYS A SG  
1542 N N   . LEU A 226 ? 0.4508 0.5550 0.5144 0.0484  0.0553  0.0063  321  LEU A N   
1543 C CA  . LEU A 226 ? 0.4410 0.5489 0.5066 0.0458  0.0518  0.0061  321  LEU A CA  
1544 C C   . LEU A 226 ? 0.4378 0.5394 0.4941 0.0417  0.0529  0.0066  321  LEU A C   
1545 O O   . LEU A 226 ? 0.4281 0.5285 0.4812 0.0399  0.0493  0.0068  321  LEU A O   
1546 C CB  . LEU A 226 ? 0.4473 0.5657 0.5248 0.0442  0.0529  0.0036  321  LEU A CB  
1547 C CG  . LEU A 226 ? 0.4349 0.5608 0.5241 0.0488  0.0506  0.0029  321  LEU A CG  
1548 C CD1 . LEU A 226 ? 0.4252 0.5621 0.5272 0.0473  0.0537  -0.0002 321  LEU A CD1 
1549 C CD2 . LEU A 226 ? 0.4255 0.5527 0.5156 0.0506  0.0431  0.0048  321  LEU A CD2 
1550 N N   . GLN A 227 ? 0.4296 0.5268 0.4813 0.0403  0.0576  0.0067  322  GLN A N   
1551 C CA  . GLN A 227 ? 0.4610 0.5510 0.5044 0.0373  0.0589  0.0075  322  GLN A CA  
1552 C C   . GLN A 227 ? 0.4671 0.5502 0.5028 0.0391  0.0567  0.0091  322  GLN A C   
1553 O O   . GLN A 227 ? 0.4728 0.5521 0.5035 0.0370  0.0553  0.0088  322  GLN A O   
1554 C CB  . GLN A 227 ? 0.4523 0.5387 0.4922 0.0363  0.0638  0.0082  322  GLN A CB  
1555 C CG  . GLN A 227 ? 0.4421 0.5226 0.4769 0.0326  0.0657  0.0087  322  GLN A CG  
1556 C CD  . GLN A 227 ? 0.4808 0.5546 0.5091 0.0333  0.0688  0.0109  322  GLN A CD  
1557 O OE1 . GLN A 227 ? 0.4744 0.5434 0.4980 0.0359  0.0679  0.0122  322  GLN A OE1 
1558 N NE2 . GLN A 227 ? 0.4039 0.4777 0.4321 0.0309  0.0724  0.0115  322  GLN A NE2 
1559 N N   . SER A 228 ? 0.4705 0.5517 0.5049 0.0427  0.0567  0.0104  323  SER A N   
1560 C CA  . SER A 228 ? 0.4702 0.5456 0.4982 0.0443  0.0550  0.0120  323  SER A CA  
1561 C C   . SER A 228 ? 0.4962 0.5731 0.5236 0.0441  0.0505  0.0122  323  SER A C   
1562 O O   . SER A 228 ? 0.4980 0.5699 0.5179 0.0430  0.0496  0.0127  323  SER A O   
1563 C CB  . SER A 228 ? 0.4280 0.5022 0.4568 0.0477  0.0555  0.0132  323  SER A CB  
1564 O OG  . SER A 228 ? 0.4295 0.4984 0.4528 0.0488  0.0544  0.0149  323  SER A OG  
1565 N N   . GLN A 229 ? 0.4821 0.5659 0.5170 0.0452  0.0475  0.0117  324  GLN A N   
1566 C CA  . GLN A 229 ? 0.4854 0.5717 0.5200 0.0453  0.0421  0.0124  324  GLN A CA  
1567 C C   . GLN A 229 ? 0.5149 0.6010 0.5454 0.0408  0.0408  0.0105  324  GLN A C   
1568 O O   . GLN A 229 ? 0.4685 0.5517 0.4917 0.0399  0.0374  0.0111  324  GLN A O   
1569 C CB  . GLN A 229 ? 0.5369 0.6320 0.5830 0.0477  0.0392  0.0120  324  GLN A CB  
1570 C CG  . GLN A 229 ? 0.6395 0.7372 0.6861 0.0493  0.0326  0.0137  324  GLN A CG  
1571 C CD  . GLN A 229 ? 0.6747 0.7662 0.7162 0.0532  0.0312  0.0173  324  GLN A CD  
1572 O OE1 . GLN A 229 ? 0.6571 0.7436 0.6974 0.0549  0.0351  0.0179  324  GLN A OE1 
1573 N NE2 . GLN A 229 ? 0.6599 0.7512 0.6978 0.0542  0.0252  0.0198  324  GLN A NE2 
1574 N N   . ILE A 230 ? 0.4688 0.5574 0.5033 0.0375  0.0435  0.0082  325  ILE A N   
1575 C CA  . ILE A 230 ? 0.4910 0.5782 0.5218 0.0327  0.0428  0.0059  325  ILE A CA  
1576 C C   . ILE A 230 ? 0.5347 0.6115 0.5537 0.0319  0.0450  0.0062  325  ILE A C   
1577 O O   . ILE A 230 ? 0.5012 0.5751 0.5134 0.0295  0.0426  0.0049  325  ILE A O   
1578 C CB  . ILE A 230 ? 0.4760 0.5665 0.5133 0.0289  0.0462  0.0038  325  ILE A CB  
1579 C CG1 . ILE A 230 ? 0.4989 0.6013 0.5489 0.0288  0.0438  0.0026  325  ILE A CG1 
1580 C CG2 . ILE A 230 ? 0.4769 0.5625 0.5088 0.0237  0.0465  0.0013  325  ILE A CG2 
1581 C CD1 . ILE A 230 ? 0.4981 0.6046 0.5555 0.0251  0.0483  0.0008  325  ILE A CD1 
1582 N N   . CYS A 231 ? 0.5133 0.5847 0.5300 0.0338  0.0496  0.0076  326  CYS A N   
1583 C CA  . CYS A 231 ? 0.5633 0.6258 0.5707 0.0337  0.0520  0.0078  326  CYS A CA  
1584 C C   . CYS A 231 ? 0.5425 0.6029 0.5430 0.0350  0.0490  0.0088  326  CYS A C   
1585 O O   . CYS A 231 ? 0.5522 0.6074 0.5444 0.0331  0.0493  0.0074  326  CYS A O   
1586 C CB  . CYS A 231 ? 0.5549 0.6138 0.5625 0.0363  0.0562  0.0097  326  CYS A CB  
1587 S SG  . CYS A 231 ? 0.6078 0.6655 0.6187 0.0344  0.0602  0.0092  326  CYS A SG  
1588 N N   . THR A 232 ? 0.5248 0.5884 0.5280 0.0383  0.0466  0.0113  327  THR A N   
1589 C CA  . THR A 232 ? 0.5395 0.6002 0.5354 0.0396  0.0442  0.0133  327  THR A CA  
1590 C C   . THR A 232 ? 0.5094 0.5718 0.5005 0.0370  0.0392  0.0121  327  THR A C   
1591 O O   . THR A 232 ? 0.5329 0.5900 0.5132 0.0357  0.0390  0.0120  327  THR A O   
1592 C CB  . THR A 232 ? 0.5379 0.6012 0.5388 0.0436  0.0424  0.0163  327  THR A CB  
1593 O OG1 . THR A 232 ? 0.5650 0.6260 0.5686 0.0453  0.0468  0.0169  327  THR A OG1 
1594 C CG2 . THR A 232 ? 0.5216 0.5815 0.5147 0.0447  0.0393  0.0192  327  THR A CG2 
1595 N N   . ILE A 233 ? 0.5212 0.5916 0.5201 0.0362  0.0351  0.0110  328  ILE A N   
1596 C CA  . ILE A 233 ? 0.5353 0.6088 0.5307 0.0336  0.0291  0.0098  328  ILE A CA  
1597 C C   . ILE A 233 ? 0.5282 0.5966 0.5153 0.0287  0.0310  0.0059  328  ILE A C   
1598 O O   . ILE A 233 ? 0.5402 0.6055 0.5166 0.0267  0.0282  0.0050  328  ILE A O   
1599 C CB  . ILE A 233 ? 0.5407 0.6253 0.5490 0.0335  0.0248  0.0089  328  ILE A CB  
1600 C CG1 . ILE A 233 ? 0.5464 0.6354 0.5628 0.0389  0.0229  0.0125  328  ILE A CG1 
1601 C CG2 . ILE A 233 ? 0.4991 0.5883 0.5048 0.0302  0.0179  0.0072  328  ILE A CG2 
1602 C CD1 . ILE A 233 ? 0.5350 0.6347 0.5670 0.0396  0.0216  0.0111  328  ILE A CD1 
1603 N N   . PHE A 234 ? 0.5399 0.6062 0.5309 0.0267  0.0361  0.0035  329  PHE A N   
1604 C CA  . PHE A 234 ? 0.5513 0.6113 0.5358 0.0223  0.0388  -0.0005 329  PHE A CA  
1605 C C   . PHE A 234 ? 0.5621 0.6129 0.5340 0.0230  0.0418  -0.0004 329  PHE A C   
1606 O O   . PHE A 234 ? 0.5629 0.6099 0.5247 0.0199  0.0404  -0.0032 329  PHE A O   
1607 C CB  . PHE A 234 ? 0.5365 0.5948 0.5279 0.0214  0.0442  -0.0014 329  PHE A CB  
1608 C CG  . PHE A 234 ? 0.5330 0.5826 0.5187 0.0177  0.0482  -0.0049 329  PHE A CG  
1609 C CD1 . PHE A 234 ? 0.5197 0.5607 0.5011 0.0199  0.0539  -0.0042 329  PHE A CD1 
1610 C CD2 . PHE A 234 ? 0.5142 0.5644 0.5003 0.0122  0.0465  -0.0091 329  PHE A CD2 
1611 C CE1 . PHE A 234 ? 0.5047 0.5369 0.4819 0.0172  0.0579  -0.0074 329  PHE A CE1 
1612 C CE2 . PHE A 234 ? 0.5485 0.5893 0.5297 0.0089  0.0506  -0.0127 329  PHE A CE2 
1613 C CZ  . PHE A 234 ? 0.5235 0.5549 0.5003 0.0117  0.0565  -0.0117 329  PHE A CZ  
1614 N N   . LYS A 235 ? 0.5477 0.5951 0.5198 0.0269  0.0459  0.0025  330  LYS A N   
1615 C CA  . LYS A 235 ? 0.5405 0.5800 0.5026 0.0275  0.0498  0.0024  330  LYS A CA  
1616 C C   . LYS A 235 ? 0.5835 0.6226 0.5354 0.0273  0.0460  0.0037  330  LYS A C   
1617 O O   . LYS A 235 ? 0.5700 0.6032 0.5105 0.0251  0.0477  0.0014  330  LYS A O   
1618 C CB  . LYS A 235 ? 0.5775 0.6152 0.5439 0.0314  0.0545  0.0053  330  LYS A CB  
1619 C CG  . LYS A 235 ? 0.6321 0.6680 0.6052 0.0314  0.0586  0.0041  330  LYS A CG  
1620 C CD  . LYS A 235 ? 0.6854 0.7203 0.6629 0.0351  0.0624  0.0068  330  LYS A CD  
1621 C CE  . LYS A 235 ? 0.6200 0.6615 0.6058 0.0372  0.0602  0.0095  330  LYS A CE  
1622 N NZ  . LYS A 235 ? 0.6918 0.7326 0.6819 0.0400  0.0635  0.0113  330  LYS A NZ  
1623 N N   . ASN A 236 ? 0.5325 0.5773 0.4877 0.0296  0.0409  0.0074  331  ASN A N   
1624 C CA  . ASN A 236 ? 0.5721 0.6154 0.5167 0.0298  0.0371  0.0099  331  ASN A CA  
1625 C C   . ASN A 236 ? 0.5628 0.6074 0.4993 0.0257  0.0318  0.0068  331  ASN A C   
1626 O O   . ASN A 236 ? 0.5700 0.6098 0.4924 0.0241  0.0311  0.0068  331  ASN A O   
1627 C CB  . ASN A 236 ? 0.5685 0.6164 0.5192 0.0338  0.0329  0.0150  331  ASN A CB  
1628 C CG  . ASN A 236 ? 0.6076 0.6524 0.5621 0.0373  0.0381  0.0180  331  ASN A CG  
1629 O OD1 . ASN A 236 ? 0.6097 0.6490 0.5605 0.0368  0.0442  0.0169  331  ASN A OD1 
1630 N ND2 . ASN A 236 ? 0.6260 0.6743 0.5884 0.0407  0.0356  0.0215  331  ASN A ND2 
1631 N N   . PHE A 237 ? 0.5751 0.6262 0.5200 0.0235  0.0281  0.0041  332  PHE A N   
1632 C CA  . PHE A 237 ? 0.5602 0.6128 0.4981 0.0188  0.0230  0.0003  332  PHE A CA  
1633 C C   . PHE A 237 ? 0.5706 0.6138 0.4965 0.0150  0.0283  -0.0046 332  PHE A C   
1634 O O   . PHE A 237 ? 0.5853 0.6252 0.4971 0.0121  0.0258  -0.0065 332  PHE A O   
1635 C CB  . PHE A 237 ? 0.5620 0.6236 0.5133 0.0165  0.0193  -0.0023 332  PHE A CB  
1636 C CG  . PHE A 237 ? 0.5515 0.6160 0.4976 0.0111  0.0133  -0.0066 332  PHE A CG  
1637 C CD1 . PHE A 237 ? 0.6170 0.6895 0.5627 0.0112  0.0039  -0.0047 332  PHE A CD1 
1638 C CD2 . PHE A 237 ? 0.5780 0.6372 0.5202 0.0057  0.0168  -0.0128 332  PHE A CD2 
1639 C CE1 . PHE A 237 ? 0.6210 0.6973 0.5621 0.0057  -0.0026 -0.0091 332  PHE A CE1 
1640 C CE2 . PHE A 237 ? 0.5768 0.6387 0.5145 0.0000  0.0110  -0.0176 332  PHE A CE2 
1641 C CZ  . PHE A 237 ? 0.6313 0.7023 0.5682 -0.0003 0.0011  -0.0159 332  PHE A CZ  
1642 N N   . LEU A 238 ? 0.5548 0.5931 0.4857 0.0150  0.0357  -0.0068 333  LEU A N   
1643 C CA  . LEU A 238 ? 0.5736 0.6026 0.4947 0.0120  0.0412  -0.0119 333  LEU A CA  
1644 C C   . LEU A 238 ? 0.5985 0.6208 0.5067 0.0136  0.0452  -0.0105 333  LEU A C   
1645 O O   . LEU A 238 ? 0.6011 0.6177 0.4956 0.0103  0.0462  -0.0144 333  LEU A O   
1646 C CB  . LEU A 238 ? 0.5613 0.5865 0.4917 0.0124  0.0478  -0.0137 333  LEU A CB  
1647 C CG  . LEU A 238 ? 0.5812 0.6117 0.5222 0.0094  0.0449  -0.0157 333  LEU A CG  
1648 C CD1 . LEU A 238 ? 0.5360 0.5622 0.4855 0.0102  0.0512  -0.0160 333  LEU A CD1 
1649 C CD2 . LEU A 238 ? 0.5697 0.5992 0.5038 0.0030  0.0412  -0.0217 333  LEU A CD2 
1650 N N   . LEU A 239 ? 0.5781 0.6010 0.4901 0.0183  0.0476  -0.0052 334  LEU A N   
1651 C CA  . LEU A 239 ? 0.6202 0.6374 0.5212 0.0195  0.0518  -0.0034 334  LEU A CA  
1652 C C   . LEU A 239 ? 0.6297 0.6467 0.5159 0.0174  0.0463  -0.0023 334  LEU A C   
1653 O O   . LEU A 239 ? 0.6427 0.6533 0.5144 0.0154  0.0499  -0.0042 334  LEU A O   
1654 C CB  . LEU A 239 ? 0.6123 0.6313 0.5217 0.0243  0.0541  0.0022  334  LEU A CB  
1655 C CG  . LEU A 239 ? 0.6163 0.6347 0.5378 0.0267  0.0600  0.0016  334  LEU A CG  
1656 C CD1 . LEU A 239 ? 0.5745 0.5967 0.5054 0.0308  0.0600  0.0069  334  LEU A CD1 
1657 C CD2 . LEU A 239 ? 0.5534 0.5644 0.4695 0.0262  0.0681  -0.0017 334  LEU A CD2 
1658 N N   . GLU A 240 ? 0.6217 0.6460 0.5115 0.0179  0.0377  0.0009  335  GLU A N   
1659 C CA  . GLU A 240 ? 0.6475 0.6723 0.5235 0.0162  0.0309  0.0027  335  GLU A CA  
1660 C C   . GLU A 240 ? 0.6543 0.6768 0.5185 0.0105  0.0290  -0.0039 335  GLU A C   
1661 O O   . GLU A 240 ? 0.6476 0.6679 0.4955 0.0082  0.0253  -0.0035 335  GLU A O   
1662 C CB  . GLU A 240 ? 0.6696 0.7036 0.5555 0.0188  0.0218  0.0075  335  GLU A CB  
1663 C CG  . GLU A 240 ? 0.8540 0.8909 0.7288 0.0171  0.0123  0.0093  335  GLU A CG  
1664 C CD  . GLU A 240 ? 1.0277 1.0617 0.8939 0.0204  0.0103  0.0170  335  GLU A CD  
1665 O OE1 . GLU A 240 ? 1.0584 1.0969 0.9215 0.0212  0.0008  0.0209  335  GLU A OE1 
1666 O OE2 . GLU A 240 ? 1.0345 1.0616 0.8975 0.0221  0.0180  0.0194  335  GLU A OE2 
1667 N N   . ASN A 241 ? 0.6374 0.6595 0.5086 0.0079  0.0316  -0.0099 336  ASN A N   
1668 C CA  . ASN A 241 ? 0.6581 0.6764 0.5184 0.0020  0.0310  -0.0173 336  ASN A CA  
1669 C C   . ASN A 241 ? 0.6460 0.6536 0.4993 0.0009  0.0414  -0.0224 336  ASN A C   
1670 O O   . ASN A 241 ? 0.6356 0.6390 0.4857 -0.0035 0.0432  -0.0296 336  ASN A O   
1671 C CB  . ASN A 241 ? 0.6068 0.6314 0.4794 -0.0011 0.0264  -0.0212 336  ASN A CB  
1672 C CG  . ASN A 241 ? 0.6466 0.6819 0.5223 -0.0016 0.0150  -0.0184 336  ASN A CG  
1673 O OD1 . ASN A 241 ? 0.6641 0.7006 0.5279 -0.0057 0.0086  -0.0210 336  ASN A OD1 
1674 N ND2 . ASN A 241 ? 0.6432 0.6868 0.5351 0.0026  0.0123  -0.0133 336  ASN A ND2 
1675 N N   . ASN A 242 ? 0.6123 0.6156 0.4643 0.0047  0.0486  -0.0190 337  ASN A N   
1676 C CA  . ASN A 242 ? 0.6773 0.6712 0.5216 0.0043  0.0586  -0.0232 337  ASN A CA  
1677 C C   . ASN A 242 ? 0.6754 0.6660 0.5326 0.0053  0.0651  -0.0271 337  ASN A C   
1678 O O   . ASN A 242 ? 0.6619 0.6444 0.5135 0.0039  0.0723  -0.0328 337  ASN A O   
1679 C CB  . ASN A 242 ? 0.6702 0.6582 0.4942 -0.0010 0.0586  -0.0292 337  ASN A CB  
1680 C CG  . ASN A 242 ? 0.7762 0.7555 0.5891 -0.0006 0.0690  -0.0315 337  ASN A CG  
1681 O OD1 . ASN A 242 ? 0.7631 0.7424 0.5798 0.0034  0.0741  -0.0265 337  ASN A OD1 
1682 N ND2 . ASN A 242 ? 0.7660 0.7379 0.5658 -0.0050 0.0727  -0.0396 337  ASN A ND2 
1683 N N   . PHE A 243 ? 0.6105 0.6067 0.4846 0.0076  0.0627  -0.0242 338  PHE A N   
1684 C CA  . PHE A 243 ? 0.6162 0.6090 0.5024 0.0094  0.0688  -0.0261 338  PHE A CA  
1685 C C   . PHE A 243 ? 0.6131 0.6045 0.5047 0.0146  0.0756  -0.0223 338  PHE A C   
1686 O O   . PHE A 243 ? 0.5573 0.5528 0.4487 0.0172  0.0744  -0.0169 338  PHE A O   
1687 C CB  . PHE A 243 ? 0.5728 0.5723 0.4738 0.0097  0.0641  -0.0240 338  PHE A CB  
1688 C CG  . PHE A 243 ? 0.5853 0.5852 0.4856 0.0042  0.0597  -0.0290 338  PHE A CG  
1689 C CD1 . PHE A 243 ? 0.5643 0.5689 0.4564 0.0005  0.0520  -0.0302 338  PHE A CD1 
1690 C CD2 . PHE A 243 ? 0.5793 0.5751 0.4877 0.0027  0.0630  -0.0324 338  PHE A CD2 
1691 C CE1 . PHE A 243 ? 0.5994 0.6055 0.4923 -0.0051 0.0476  -0.0352 338  PHE A CE1 
1692 C CE2 . PHE A 243 ? 0.5870 0.5829 0.4955 -0.0031 0.0594  -0.0372 338  PHE A CE2 
1693 C CZ  . PHE A 243 ? 0.5876 0.5893 0.4889 -0.0072 0.0515  -0.0390 338  PHE A CZ  
1694 N N   . ILE A 244 ? 0.5856 0.5715 0.4835 0.0163  0.0825  -0.0249 339  ILE A N   
1695 C CA  . ILE A 244 ? 0.5872 0.5740 0.4948 0.0215  0.0877  -0.0211 339  ILE A CA  
1696 C C   . ILE A 244 ? 0.5661 0.5549 0.4885 0.0237  0.0870  -0.0192 339  ILE A C   
1697 O O   . ILE A 244 ? 0.5568 0.5424 0.4815 0.0214  0.0863  -0.0223 339  ILE A O   
1698 C CB  . ILE A 244 ? 0.6185 0.5983 0.5223 0.0229  0.0968  -0.0246 339  ILE A CB  
1699 C CG1 . ILE A 244 ? 0.5947 0.5667 0.5015 0.0222  0.1010  -0.0303 339  ILE A CG1 
1700 C CG2 . ILE A 244 ? 0.6211 0.5983 0.5082 0.0201  0.0983  -0.0266 339  ILE A CG2 
1701 C CD1 . ILE A 244 ? 0.6657 0.6318 0.5738 0.0252  0.1105  -0.0331 339  ILE A CD1 
1702 N N   . GLU A 245 ? 0.5415 0.5353 0.4734 0.0279  0.0872  -0.0139 340  GLU A N   
1703 C CA  . GLU A 245 ? 0.5295 0.5251 0.4741 0.0303  0.0870  -0.0115 340  GLU A CA  
1704 C C   . GLU A 245 ? 0.5227 0.5119 0.4720 0.0330  0.0937  -0.0133 340  GLU A C   
1705 O O   . GLU A 245 ? 0.5399 0.5278 0.4886 0.0354  0.0987  -0.0136 340  GLU A O   
1706 C CB  . GLU A 245 ? 0.5208 0.5242 0.4727 0.0334  0.0844  -0.0057 340  GLU A CB  
1707 C CG  . GLU A 245 ? 0.5581 0.5634 0.5216 0.0363  0.0846  -0.0030 340  GLU A CG  
1708 C CD  . GLU A 245 ? 0.6155 0.6287 0.5845 0.0375  0.0801  0.0014  340  GLU A CD  
1709 O OE1 . GLU A 245 ? 0.6416 0.6572 0.6179 0.0384  0.0788  0.0032  340  GLU A OE1 
1710 O OE2 . GLU A 245 ? 0.6133 0.6299 0.5789 0.0375  0.0780  0.0030  340  GLU A OE2 
1711 N N   . ILE A 246 ? 0.4826 0.4681 0.4376 0.0328  0.0940  -0.0141 341  ILE A N   
1712 C CA  . ILE A 246 ? 0.5137 0.4929 0.4748 0.0361  0.0996  -0.0149 341  ILE A CA  
1713 C C   . ILE A 246 ? 0.5494 0.5318 0.5213 0.0392  0.0976  -0.0097 341  ILE A C   
1714 O O   . ILE A 246 ? 0.5447 0.5326 0.5186 0.0377  0.0927  -0.0069 341  ILE A O   
1715 C CB  . ILE A 246 ? 0.5329 0.5016 0.4896 0.0333  0.1027  -0.0207 341  ILE A CB  
1716 C CG1 . ILE A 246 ? 0.4991 0.4673 0.4566 0.0291  0.0982  -0.0209 341  ILE A CG1 
1717 C CG2 . ILE A 246 ? 0.5174 0.4824 0.4618 0.0302  0.1052  -0.0266 341  ILE A CG2 
1718 C CD1 . ILE A 246 ? 0.5667 0.5236 0.5216 0.0260  0.1014  -0.0265 341  ILE A CD1 
1719 N N   . HIS A 247 ? 0.5271 0.5063 0.5061 0.0436  0.1016  -0.0085 342  HIS A N   
1720 C CA  . HIS A 247 ? 0.5178 0.4989 0.5060 0.0469  0.0999  -0.0034 342  HIS A CA  
1721 C C   . HIS A 247 ? 0.5347 0.5062 0.5270 0.0493  0.1041  -0.0045 342  HIS A C   
1722 O O   . HIS A 247 ? 0.5040 0.4728 0.4993 0.0529  0.1088  -0.0062 342  HIS A O   
1723 C CB  . HIS A 247 ? 0.5123 0.5019 0.5069 0.0509  0.0991  0.0007  342  HIS A CB  
1724 C CG  . HIS A 247 ? 0.5238 0.5218 0.5155 0.0489  0.0949  0.0023  342  HIS A CG  
1725 N ND1 . HIS A 247 ? 0.5215 0.5243 0.5146 0.0477  0.0901  0.0053  342  HIS A ND1 
1726 C CD2 . HIS A 247 ? 0.4991 0.5007 0.4863 0.0480  0.0952  0.0013  342  HIS A CD2 
1727 C CE1 . HIS A 247 ? 0.5052 0.5142 0.4958 0.0465  0.0875  0.0059  342  HIS A CE1 
1728 N NE2 . HIS A 247 ? 0.5650 0.5732 0.5518 0.0466  0.0902  0.0039  342  HIS A NE2 
1729 N N   . THR A 248 ? 0.5264 0.4925 0.5193 0.0475  0.1029  -0.0035 343  THR A N   
1730 C CA  . THR A 248 ? 0.5280 0.4828 0.5240 0.0494  0.1067  -0.0042 343  THR A CA  
1731 C C   . THR A 248 ? 0.5630 0.5177 0.5659 0.0526  0.1045  0.0025  343  THR A C   
1732 O O   . THR A 248 ? 0.5315 0.4937 0.5347 0.0515  0.1001  0.0066  343  THR A O   
1733 C CB  . THR A 248 ? 0.5698 0.5155 0.5592 0.0435  0.1078  -0.0094 343  THR A CB  
1734 O OG1 . THR A 248 ? 0.5565 0.5059 0.5447 0.0390  0.1033  -0.0071 343  THR A OG1 
1735 C CG2 . THR A 248 ? 0.5042 0.4502 0.4851 0.0402  0.1093  -0.0161 343  THR A CG2 
1736 N N   . PRO A 249 ? 0.5512 0.4974 0.5596 0.0569  0.1075  0.0039  344  PRO A N   
1737 C CA  . PRO A 249 ? 0.5693 0.5164 0.5839 0.0611  0.1049  0.0113  344  PRO A CA  
1738 C C   . PRO A 249 ? 0.5843 0.5276 0.5954 0.0570  0.1025  0.0146  344  PRO A C   
1739 O O   . PRO A 249 ? 0.5788 0.5141 0.5855 0.0520  0.1043  0.0112  344  PRO A O   
1740 C CB  . PRO A 249 ? 0.5709 0.5085 0.5921 0.0668  0.1090  0.0113  344  PRO A CB  
1741 C CG  . PRO A 249 ? 0.5986 0.5263 0.6152 0.0637  0.1142  0.0038  344  PRO A CG  
1742 C CD  . PRO A 249 ? 0.5704 0.5064 0.5799 0.0590  0.1134  -0.0009 344  PRO A CD  
1743 N N   . LYS A 250 ? 0.5628 0.5120 0.5758 0.0588  0.0986  0.0211  345  LYS A N   
1744 C CA  . LYS A 250 ? 0.5762 0.5216 0.5863 0.0556  0.0971  0.0254  345  LYS A CA  
1745 C C   . LYS A 250 ? 0.5883 0.5237 0.6015 0.0599  0.0978  0.0312  345  LYS A C   
1746 O O   . LYS A 250 ? 0.6123 0.5406 0.6222 0.0569  0.0980  0.0346  345  LYS A O   
1747 C CB  . LYS A 250 ? 0.5491 0.5065 0.5573 0.0541  0.0927  0.0288  345  LYS A CB  
1748 C CG  . LYS A 250 ? 0.5176 0.4856 0.5241 0.0515  0.0913  0.0243  345  LYS A CG  
1749 C CD  . LYS A 250 ? 0.5486 0.5128 0.5512 0.0459  0.0933  0.0182  345  LYS A CD  
1750 C CE  . LYS A 250 ? 0.5067 0.4798 0.5074 0.0446  0.0919  0.0141  345  LYS A CE  
1751 N NZ  . LYS A 250 ? 0.5380 0.5062 0.5344 0.0402  0.0938  0.0077  345  LYS A NZ  
1752 N N   . LEU A 251 ? 0.5422 0.4771 0.5621 0.0669  0.0982  0.0328  346  LEU A N   
1753 C CA  . LEU A 251 ? 0.6132 0.5374 0.6371 0.0720  0.0989  0.0380  346  LEU A CA  
1754 C C   . LEU A 251 ? 0.6517 0.5616 0.6767 0.0717  0.1046  0.0330  346  LEU A C   
1755 O O   . LEU A 251 ? 0.6477 0.5583 0.6760 0.0734  0.1079  0.0269  346  LEU A O   
1756 C CB  . LEU A 251 ? 0.6108 0.5422 0.6432 0.0799  0.0963  0.0417  346  LEU A CB  
1757 C CG  . LEU A 251 ? 0.6359 0.5808 0.6672 0.0803  0.0903  0.0465  346  LEU A CG  
1758 C CD1 . LEU A 251 ? 0.6035 0.5547 0.6443 0.0881  0.0873  0.0503  346  LEU A CD1 
1759 C CD2 . LEU A 251 ? 0.6498 0.5910 0.6735 0.0770  0.0878  0.0525  346  LEU A CD2 
1760 N N   . LEU A 252 ? 0.6531 0.5496 0.6750 0.0690  0.1063  0.0353  347  LEU A N   
1761 C CA  . LEU A 252 ? 0.7225 0.6039 0.7443 0.0672  0.1118  0.0300  347  LEU A CA  
1762 C C   . LEU A 252 ? 0.7423 0.6093 0.7691 0.0731  0.1134  0.0356  347  LEU A C   
1763 O O   . LEU A 252 ? 0.7301 0.5967 0.7570 0.0757  0.1098  0.0445  347  LEU A O   
1764 C CB  . LEU A 252 ? 0.7060 0.5826 0.7201 0.0577  0.1130  0.0267  347  LEU A CB  
1765 C CG  . LEU A 252 ? 0.6926 0.5826 0.7019 0.0516  0.1110  0.0216  347  LEU A CG  
1766 C CD1 . LEU A 252 ? 0.7097 0.5938 0.7138 0.0425  0.1126  0.0175  347  LEU A CD1 
1767 C CD2 . LEU A 252 ? 0.6464 0.5426 0.6570 0.0538  0.1123  0.0147  347  LEU A CD2 
1768 N N   . GLY A 253 ? 0.7731 0.6280 0.8039 0.0754  0.1187  0.0303  348  GLY A N   
1769 C CA  . GLY A 253 ? 0.7951 0.6337 0.8309 0.0806  0.1208  0.0351  348  GLY A CA  
1770 C C   . GLY A 253 ? 0.8859 0.7097 0.9151 0.0740  0.1225  0.0370  348  GLY A C   
1771 O O   . GLY A 253 ? 0.9271 0.7391 0.9577 0.0771  0.1222  0.0448  348  GLY A O   
1772 N N   . GLU A 254 ? 0.9031 0.7276 0.9253 0.0645  0.1241  0.0302  349  GLU A N   
1773 C CA  . GLU A 254 ? 0.9498 0.7620 0.9665 0.0566  0.1262  0.0305  349  GLU A CA  
1774 C C   . GLU A 254 ? 1.0139 0.8394 1.0240 0.0476  0.1237  0.0274  349  GLU A C   
1775 O O   . GLU A 254 ? 0.9784 0.8187 0.9880 0.0474  0.1217  0.0227  349  GLU A O   
1776 C CB  . GLU A 254 ? 0.9935 0.7878 1.0111 0.0545  0.1325  0.0226  349  GLU A CB  
1777 C CG  . GLU A 254 ? 1.0342 0.8075 1.0526 0.0543  0.1354  0.0280  349  GLU A CG  
1778 C CD  . GLU A 254 ? 1.0808 0.8470 1.1064 0.0656  0.1347  0.0366  349  GLU A CD  
1779 O OE1 . GLU A 254 ? 1.0810 0.8472 1.1140 0.0733  0.1366  0.0330  349  GLU A OE1 
1780 O OE2 . GLU A 254 ? 1.0705 0.8312 1.0946 0.0667  0.1324  0.0472  349  GLU A OE2 
1781 N N   . SER A 255 ? 1.1579 0.9782 1.1637 0.0404  0.1240  0.0303  350  SER A N   
1782 C CA  . SER A 255 ? 1.2030 1.0366 1.2045 0.0323  0.1217  0.0278  350  SER A CA  
1783 C C   . SER A 255 ? 1.2802 1.1107 1.2799 0.0242  0.1243  0.0173  350  SER A C   
1784 O O   . SER A 255 ? 1.3009 1.1445 1.2990 0.0215  0.1222  0.0111  350  SER A O   
1785 C CB  . SER A 255 ? 1.2431 1.0751 1.2414 0.0280  0.1210  0.0359  350  SER A CB  
1786 O OG  . SER A 255 ? 1.2920 1.1070 1.2893 0.0219  0.1255  0.0350  350  SER A OG  
1787 N N   . ALA A 260 ? 1.4775 1.2830 1.4644 0.0081  0.1284  0.0555  355  ALA A N   
1788 C CA  . ALA A 260 ? 1.4867 1.2963 1.4718 -0.0025 0.1307  0.0548  355  ALA A CA  
1789 C C   . ALA A 260 ? 1.4425 1.2692 1.4239 -0.0021 0.1278  0.0600  355  ALA A C   
1790 O O   . ALA A 260 ? 1.4798 1.3025 1.4558 0.0003  0.1277  0.0698  355  ALA A O   
1791 C CB  . ALA A 260 ? 1.5130 1.3291 1.5023 -0.0098 0.1314  0.0429  355  ALA A CB  
1792 N N   . ASN A 261 ? 1.1647 1.0099 1.1486 -0.0045 0.1253  0.0533  356  ASN A N   
1793 C CA  . ASN A 261 ? 1.0143 0.8769 0.9957 -0.0035 0.1224  0.0564  356  ASN A CA  
1794 C C   . ASN A 261 ? 0.9292 0.8025 0.9114 0.0056  0.1172  0.0556  356  ASN A C   
1795 O O   . ASN A 261 ? 0.8427 0.7325 0.8264 0.0056  0.1143  0.0518  356  ASN A O   
1796 C CB  . ASN A 261 ? 1.0030 0.8793 0.9879 -0.0120 0.1232  0.0500  356  ASN A CB  
1797 C CG  . ASN A 261 ? 1.0912 0.9606 1.0758 -0.0215 0.1286  0.0520  356  ASN A CG  
1798 O OD1 . ASN A 261 ? 1.1068 0.9661 1.0856 -0.0218 0.1315  0.0606  356  ASN A OD1 
1799 N ND2 . ASN A 261 ? 1.0871 0.9620 1.0777 -0.0297 0.1300  0.0442  356  ASN A ND2 
1800 N N   . ALA A 262 ? 0.9160 0.7798 0.8981 0.0136  0.1159  0.0592  357  ALA A N   
1801 C CA  . ALA A 262 ? 0.8469 0.7199 0.8311 0.0220  0.1115  0.0583  357  ALA A CA  
1802 C C   . ALA A 262 ? 0.8075 0.6809 0.7878 0.0285  0.1084  0.0680  357  ALA A C   
1803 O O   . ALA A 262 ? 0.8037 0.6634 0.7806 0.0296  0.1099  0.0756  357  ALA A O   
1804 C CB  . ALA A 262 ? 0.8244 0.6885 0.8136 0.0264  0.1124  0.0534  357  ALA A CB  
1805 N N   . PHE A 263 ? 0.7217 0.6103 0.7020 0.0327  0.1040  0.0679  358  PHE A N   
1806 C CA  . PHE A 263 ? 0.7203 0.6101 0.6978 0.0396  0.1000  0.0760  358  PHE A CA  
1807 C C   . PHE A 263 ? 0.7826 0.6629 0.7655 0.0477  0.0990  0.0777  358  PHE A C   
1808 O O   . PHE A 263 ? 0.7189 0.6001 0.7086 0.0498  0.0999  0.0708  358  PHE A O   
1809 C CB  . PHE A 263 ? 0.6835 0.5916 0.6608 0.0419  0.0956  0.0742  358  PHE A CB  
1810 C CG  . PHE A 263 ? 0.7025 0.6207 0.6751 0.0354  0.0964  0.0731  358  PHE A CG  
1811 C CD1 . PHE A 263 ? 0.7314 0.6493 0.6954 0.0339  0.0962  0.0802  358  PHE A CD1 
1812 C CD2 . PHE A 263 ? 0.6286 0.5565 0.6049 0.0310  0.0974  0.0649  358  PHE A CD2 
1813 C CE1 . PHE A 263 ? 0.6811 0.6087 0.6414 0.0281  0.0978  0.0785  358  PHE A CE1 
1814 C CE2 . PHE A 263 ? 0.6141 0.5519 0.5878 0.0256  0.0984  0.0636  358  PHE A CE2 
1815 C CZ  . PHE A 263 ? 0.6715 0.6092 0.6375 0.0242  0.0990  0.0700  358  PHE A CZ  
1816 N N   . GLN A 264 ? 0.7550 0.6265 0.7351 0.0523  0.0973  0.0870  359  GLN A N   
1817 C CA  . GLN A 264 ? 0.7418 0.6054 0.7284 0.0611  0.0958  0.0897  359  GLN A CA  
1818 C C   . GLN A 264 ? 0.7737 0.6506 0.7628 0.0685  0.0893  0.0927  359  GLN A C   
1819 O O   . GLN A 264 ? 0.8082 0.6950 0.7907 0.0673  0.0857  0.0965  359  GLN A O   
1820 C CB  . GLN A 264 ? 0.8127 0.6574 0.7958 0.0625  0.0972  0.0987  359  GLN A CB  
1821 C CG  . GLN A 264 ? 0.8446 0.6756 0.8251 0.0543  0.1037  0.0962  359  GLN A CG  
1822 C CD  . GLN A 264 ? 0.9723 0.7862 0.9461 0.0537  0.1051  0.1067  359  GLN A CD  
1823 O OE1 . GLN A 264 ? 1.0071 0.8183 0.9786 0.0606  0.1008  0.1160  359  GLN A OE1 
1824 N NE2 . GLN A 264 ? 0.9325 0.7348 0.9030 0.0452  0.1109  0.1056  359  GLN A NE2 
1825 N N   . ILE A 265 ? 0.7477 0.6250 0.7466 0.0757  0.0883  0.0904  360  ILE A N   
1826 C CA  . ILE A 265 ? 0.7720 0.6614 0.7760 0.0831  0.0823  0.0930  360  ILE A CA  
1827 C C   . ILE A 265 ? 0.7915 0.6714 0.8049 0.0920  0.0818  0.0967  360  ILE A C   
1828 O O   . ILE A 265 ? 0.8332 0.6996 0.8509 0.0926  0.0869  0.0937  360  ILE A O   
1829 C CB  . ILE A 265 ? 0.8145 0.7201 0.8239 0.0826  0.0818  0.0842  360  ILE A CB  
1830 C CG1 . ILE A 265 ? 0.7980 0.6984 0.8140 0.0819  0.0874  0.0755  360  ILE A CG1 
1831 C CG2 . ILE A 265 ? 0.8139 0.7298 0.8154 0.0751  0.0815  0.0812  360  ILE A CG2 
1832 C CD1 . ILE A 265 ? 0.8431 0.7467 0.8707 0.0898  0.0870  0.0733  360  ILE A CD1 
1833 N N   . ASN A 266 ? 0.7793 0.6663 0.7961 0.0991  0.0753  0.1029  361  ASN A N   
1834 C CA  . ASN A 266 ? 0.8001 0.6828 0.8291 0.1088  0.0738  0.1057  361  ASN A CA  
1835 C C   . ASN A 266 ? 0.8445 0.7419 0.8853 0.1120  0.0738  0.0977  361  ASN A C   
1836 O O   . ASN A 266 ? 0.8065 0.7203 0.8476 0.1120  0.0689  0.0973  361  ASN A O   
1837 C CB  . ASN A 266 ? 0.8480 0.7312 0.8753 0.1149  0.0661  0.1173  361  ASN A CB  
1838 C CG  . ASN A 266 ? 0.9926 0.8740 1.0350 0.1259  0.0636  0.1203  361  ASN A CG  
1839 O OD1 . ASN A 266 ? 1.0250 0.8959 1.0765 0.1290  0.0692  0.1163  361  ASN A OD1 
1840 N ND2 . ASN A 266 ? 1.0799 0.9719 1.1254 0.1318  0.0552  0.1269  361  ASN A ND2 
1841 N N   . TYR A 267 ? 0.8234 0.7144 0.8731 0.1141  0.0797  0.0910  362  TYR A N   
1842 C CA  . TYR A 267 ? 0.7776 0.6804 0.8382 0.1169  0.0814  0.0831  362  TYR A CA  
1843 C C   . TYR A 267 ? 0.8153 0.7154 0.8909 0.1274  0.0807  0.0859  362  TYR A C   
1844 O O   . TYR A 267 ? 0.8317 0.7200 0.9138 0.1303  0.0867  0.0822  362  TYR A O   
1845 C CB  . TYR A 267 ? 0.7245 0.6226 0.7827 0.1108  0.0890  0.0728  362  TYR A CB  
1846 C CG  . TYR A 267 ? 0.7245 0.6354 0.7903 0.1118  0.0911  0.0646  362  TYR A CG  
1847 C CD1 . TYR A 267 ? 0.6858 0.6115 0.7470 0.1068  0.0889  0.0614  362  TYR A CD1 
1848 C CD2 . TYR A 267 ? 0.6843 0.5919 0.7619 0.1177  0.0958  0.0602  362  TYR A CD2 
1849 C CE1 . TYR A 267 ? 0.6668 0.6034 0.7343 0.1074  0.0911  0.0546  362  TYR A CE1 
1850 C CE2 . TYR A 267 ? 0.6687 0.5880 0.7526 0.1182  0.0984  0.0530  362  TYR A CE2 
1851 C CZ  . TYR A 267 ? 0.6559 0.5894 0.7344 0.1128  0.0959  0.0505  362  TYR A CZ  
1852 O OH  . TYR A 267 ? 0.6098 0.5537 0.6938 0.1129  0.0989  0.0440  362  TYR A OH  
1853 N N   . PHE A 268 ? 0.8181 0.7294 0.8994 0.1331  0.0732  0.0924  363  PHE A N   
1854 C CA  . PHE A 268 ? 0.8453 0.7581 0.9432 0.1438  0.0712  0.0954  363  PHE A CA  
1855 C C   . PHE A 268 ? 0.9610 0.8532 1.0615 0.1489  0.0738  0.1004  363  PHE A C   
1856 O O   . PHE A 268 ? 0.9688 0.8551 1.0824 0.1552  0.0786  0.0970  363  PHE A O   
1857 C CB  . PHE A 268 ? 0.7664 0.6894 0.8779 0.1460  0.0760  0.0859  363  PHE A CB  
1858 C CG  . PHE A 268 ? 0.7407 0.6834 0.8513 0.1418  0.0731  0.0820  363  PHE A CG  
1859 C CD1 . PHE A 268 ? 0.6732 0.6186 0.7754 0.1335  0.0780  0.0739  363  PHE A CD1 
1860 C CD2 . PHE A 268 ? 0.7142 0.6724 0.8322 0.1459  0.0651  0.0866  363  PHE A CD2 
1861 C CE1 . PHE A 268 ? 0.6607 0.6227 0.7621 0.1298  0.0755  0.0706  363  PHE A CE1 
1862 C CE2 . PHE A 268 ? 0.7211 0.6962 0.8384 0.1416  0.0628  0.0828  363  PHE A CE2 
1863 C CZ  . PHE A 268 ? 0.6678 0.6442 0.7768 0.1337  0.0682  0.0749  363  PHE A CZ  
1864 N N   . ASN A 269 ? 1.1111 0.9919 1.1987 0.1460  0.0712  0.1085  364  ASN A N   
1865 C CA  . ASN A 269 ? 1.1273 0.9865 1.2141 0.1495  0.0733  0.1147  364  ASN A CA  
1866 C C   . ASN A 269 ? 1.0940 0.9372 1.1800 0.1454  0.0835  0.1062  364  ASN A C   
1867 O O   . ASN A 269 ? 1.1071 0.9315 1.1963 0.1493  0.0868  0.1092  364  ASN A O   
1868 C CB  . ASN A 269 ? 1.1859 1.0437 1.2881 0.1620  0.0689  0.1216  364  ASN A CB  
1869 C CG  . ASN A 269 ? 1.2723 1.1354 1.3694 0.1653  0.0582  0.1342  364  ASN A CG  
1870 O OD1 . ASN A 269 ? 1.2932 1.1756 1.3952 0.1677  0.0512  0.1352  364  ASN A OD1 
1871 N ND2 . ASN A 269 ? 1.3611 1.2069 1.4475 0.1649  0.0569  0.1438  364  ASN A ND2 
1872 N N   . GLN A 270 ? 0.9450 0.7949 1.0266 0.1376  0.0883  0.0959  365  GLN A N   
1873 C CA  . GLN A 270 ? 0.9196 0.7555 0.9938 0.1299  0.0961  0.0889  365  GLN A CA  
1874 C C   . GLN A 270 ? 0.9138 0.7499 0.9716 0.1200  0.0944  0.0915  365  GLN A C   
1875 O O   . GLN A 270 ? 0.9281 0.7786 0.9805 0.1180  0.0886  0.0950  365  GLN A O   
1876 C CB  . GLN A 270 ? 0.8526 0.6955 0.9307 0.1270  0.1021  0.0760  365  GLN A CB  
1877 C CG  . GLN A 270 ? 0.8645 0.7125 0.9589 0.1361  0.1043  0.0721  365  GLN A CG  
1878 C CD  . GLN A 270 ? 0.8189 0.6685 0.9143 0.1323  0.1120  0.0593  365  GLN A CD  
1879 O OE1 . GLN A 270 ? 0.7917 0.6280 0.8797 0.1263  0.1179  0.0534  365  GLN A OE1 
1880 N NE2 . GLN A 270 ? 0.7509 0.6169 0.8549 0.1354  0.1121  0.0549  365  GLN A NE2 
1881 N N   . LYS A 271 ? 0.8420 0.6622 0.8925 0.1134  0.0999  0.0893  366  LYS A N   
1882 C CA  . LYS A 271 ? 0.8852 0.7059 0.9218 0.1032  0.0997  0.0902  366  LYS A CA  
1883 C C   . LYS A 271 ? 0.8903 0.7190 0.9247 0.0955  0.1038  0.0783  366  LYS A C   
1884 O O   . LYS A 271 ? 0.8641 0.6842 0.9020 0.0943  0.1097  0.0702  366  LYS A O   
1885 C CB  . LYS A 271 ? 0.9479 0.7472 0.9781 0.0998  0.1029  0.0957  366  LYS A CB  
1886 C CG  . LYS A 271 ? 1.0208 0.8118 1.0510 0.1072  0.0981  0.1091  366  LYS A CG  
1887 C CD  . LYS A 271 ? 1.0543 0.8639 1.0812 0.1097  0.0896  0.1156  366  LYS A CD  
1888 C CE  . LYS A 271 ? 1.0942 0.8965 1.1192 0.1167  0.0837  0.1294  366  LYS A CE  
1889 N NZ  . LYS A 271 ? 1.1173 0.9150 1.1575 0.1286  0.0821  0.1317  366  LYS A NZ  
1890 N N   . GLY A 272 ? 0.8517 0.6971 0.8803 0.0907  0.1004  0.0772  367  GLY A N   
1891 C CA  . GLY A 272 ? 0.7943 0.6486 0.8205 0.0839  0.1029  0.0671  367  GLY A CA  
1892 C C   . GLY A 272 ? 0.8048 0.6642 0.8205 0.0749  0.1018  0.0680  367  GLY A C   
1893 O O   . GLY A 272 ? 0.7834 0.6399 0.7931 0.0737  0.0996  0.0761  367  GLY A O   
1894 N N   . PHE A 273 ? 0.7583 0.6260 0.7720 0.0688  0.1035  0.0594  368  PHE A N   
1895 C CA  . PHE A 273 ? 0.7156 0.5887 0.7216 0.0601  0.1033  0.0586  368  PHE A CA  
1896 C C   . PHE A 273 ? 0.7268 0.6174 0.7330 0.0582  0.1012  0.0523  368  PHE A C   
1897 O O   . PHE A 273 ? 0.6998 0.5952 0.7110 0.0617  0.1016  0.0472  368  PHE A O   
1898 C CB  . PHE A 273 ? 0.7641 0.6238 0.7673 0.0527  0.1084  0.0544  368  PHE A CB  
1899 C CG  . PHE A 273 ? 0.8320 0.6719 0.8358 0.0546  0.1113  0.0598  368  PHE A CG  
1900 C CD1 . PHE A 273 ? 0.8197 0.6521 0.8176 0.0514  0.1113  0.0679  368  PHE A CD1 
1901 C CD2 . PHE A 273 ? 0.8269 0.6550 0.8369 0.0597  0.1144  0.0567  368  PHE A CD2 
1902 C CE1 . PHE A 273 ? 0.8346 0.6473 0.8326 0.0533  0.1140  0.0737  368  PHE A CE1 
1903 C CE2 . PHE A 273 ? 0.8540 0.6626 0.8652 0.0620  0.1171  0.0617  368  PHE A CE2 
1904 C CZ  . PHE A 273 ? 0.8282 0.6287 0.8332 0.0588  0.1167  0.0705  368  PHE A CZ  
1905 N N   . LEU A 274 ? 0.6520 0.5515 0.6528 0.0525  0.0995  0.0530  369  LEU A N   
1906 C CA  . LEU A 274 ? 0.6560 0.5705 0.6565 0.0498  0.0979  0.0471  369  LEU A CA  
1907 C C   . LEU A 274 ? 0.6377 0.5498 0.6370 0.0427  0.1010  0.0394  369  LEU A C   
1908 O O   . LEU A 274 ? 0.6194 0.5229 0.6162 0.0370  0.1036  0.0397  369  LEU A O   
1909 C CB  . LEU A 274 ? 0.5947 0.5205 0.5910 0.0476  0.0946  0.0511  369  LEU A CB  
1910 C CG  . LEU A 274 ? 0.6644 0.5948 0.6606 0.0539  0.0905  0.0581  369  LEU A CG  
1911 C CD1 . LEU A 274 ? 0.6519 0.5924 0.6424 0.0510  0.0879  0.0610  369  LEU A CD1 
1912 C CD2 . LEU A 274 ? 0.6651 0.6032 0.6679 0.0598  0.0884  0.0553  369  LEU A CD2 
1913 N N   . ALA A 275 ? 0.5932 0.5128 0.5941 0.0427  0.1006  0.0327  370  ALA A N   
1914 C CA  . ALA A 275 ? 0.6250 0.5438 0.6242 0.0361  0.1024  0.0251  370  ALA A CA  
1915 C C   . ALA A 275 ? 0.6194 0.5454 0.6161 0.0291  0.1011  0.0252  370  ALA A C   
1916 O O   . ALA A 275 ? 0.5886 0.5270 0.5850 0.0296  0.0981  0.0273  370  ALA A O   
1917 C CB  . ALA A 275 ? 0.5375 0.4643 0.5372 0.0377  0.1016  0.0190  370  ALA A CB  
1918 N N   . GLN A 276 ? 0.5997 0.5181 0.5955 0.0225  0.1037  0.0224  371  GLN A N   
1919 C CA  . GLN A 276 ? 0.6061 0.5327 0.6015 0.0152  0.1028  0.0205  371  GLN A CA  
1920 C C   . GLN A 276 ? 0.5828 0.5186 0.5787 0.0124  0.1007  0.0129  371  GLN A C   
1921 O O   . GLN A 276 ? 0.5640 0.5109 0.5611 0.0083  0.0985  0.0115  371  GLN A O   
1922 C CB  . GLN A 276 ? 0.6030 0.5182 0.5982 0.0086  0.1065  0.0208  371  GLN A CB  
1923 C CG  . GLN A 276 ? 0.6900 0.5945 0.6836 0.0111  0.1087  0.0292  371  GLN A CG  
1924 C CD  . GLN A 276 ? 0.8062 0.6962 0.7994 0.0047  0.1130  0.0294  371  GLN A CD  
1925 O OE1 . GLN A 276 ? 0.8552 0.7296 0.8481 0.0071  0.1157  0.0313  371  GLN A OE1 
1926 N NE2 . GLN A 276 ? 0.8237 0.7189 0.8180 -0.0036 0.1140  0.0274  371  GLN A NE2 
1927 N N   . SER A 277 ? 0.5946 0.5260 0.5892 0.0147  0.1012  0.0081  372  SER A N   
1928 C CA  . SER A 277 ? 0.5685 0.5064 0.5614 0.0122  0.0992  0.0011  372  SER A CA  
1929 C C   . SER A 277 ? 0.5842 0.5170 0.5751 0.0173  0.1007  -0.0018 372  SER A C   
1930 O O   . SER A 277 ? 0.6104 0.5313 0.6022 0.0207  0.1042  -0.0005 372  SER A O   
1931 C CB  . SER A 277 ? 0.5917 0.5250 0.5839 0.0038  0.1000  -0.0046 372  SER A CB  
1932 O OG  . SER A 277 ? 0.6470 0.5827 0.6357 0.0019  0.0984  -0.0118 372  SER A OG  
1933 N N   . PRO A 278 ? 0.5682 0.5091 0.5565 0.0182  0.0986  -0.0055 373  PRO A N   
1934 C CA  . PRO A 278 ? 0.5808 0.5163 0.5664 0.0218  0.1012  -0.0094 373  PRO A CA  
1935 C C   . PRO A 278 ? 0.5826 0.5090 0.5633 0.0168  0.1035  -0.0173 373  PRO A C   
1936 O O   . PRO A 278 ? 0.5974 0.5208 0.5742 0.0188  0.1057  -0.0218 373  PRO A O   
1937 C CB  . PRO A 278 ? 0.5702 0.5187 0.5542 0.0241  0.0979  -0.0092 373  PRO A CB  
1938 C CG  . PRO A 278 ? 0.5813 0.5391 0.5646 0.0184  0.0934  -0.0100 373  PRO A CG  
1939 C CD  . PRO A 278 ? 0.5551 0.5104 0.5429 0.0161  0.0939  -0.0061 373  PRO A CD  
1940 N N   . GLN A 279 ? 0.6012 0.5233 0.5817 0.0100  0.1032  -0.0196 374  GLN A N   
1941 C CA  . GLN A 279 ? 0.5944 0.5082 0.5704 0.0036  0.1047  -0.0276 374  GLN A CA  
1942 C C   . GLN A 279 ? 0.5985 0.5001 0.5706 0.0066  0.1098  -0.0328 374  GLN A C   
1943 O O   . GLN A 279 ? 0.6264 0.5287 0.5914 0.0046  0.1097  -0.0395 374  GLN A O   
1944 C CB  . GLN A 279 ? 0.5910 0.4967 0.5705 -0.0021 0.1061  -0.0270 374  GLN A CB  
1945 C CG  . GLN A 279 ? 0.6244 0.5223 0.6003 -0.0102 0.1070  -0.0356 374  GLN A CG  
1946 C CD  . GLN A 279 ? 0.6586 0.5690 0.6303 -0.0153 0.1015  -0.0408 374  GLN A CD  
1947 O OE1 . GLN A 279 ? 0.6933 0.6004 0.6577 -0.0177 0.1015  -0.0482 374  GLN A OE1 
1948 N NE2 . GLN A 279 ? 0.6283 0.5531 0.6044 -0.0168 0.0968  -0.0369 374  GLN A NE2 
1949 N N   . LEU A 280 ? 0.5882 0.4787 0.5648 0.0116  0.1143  -0.0295 375  LEU A N   
1950 C CA  . LEU A 280 ? 0.6197 0.4976 0.5945 0.0146  0.1200  -0.0348 375  LEU A CA  
1951 C C   . LEU A 280 ? 0.6135 0.4986 0.5852 0.0195  0.1207  -0.0367 375  LEU A C   
1952 O O   . LEU A 280 ? 0.6541 0.5340 0.6193 0.0181  0.1239  -0.0445 375  LEU A O   
1953 C CB  . LEU A 280 ? 0.5974 0.4629 0.5793 0.0201  0.1240  -0.0296 375  LEU A CB  
1954 C CG  . LEU A 280 ? 0.7057 0.5626 0.6904 0.0155  0.1241  -0.0262 375  LEU A CG  
1955 C CD1 . LEU A 280 ? 0.6831 0.5246 0.6733 0.0211  0.1285  -0.0217 375  LEU A CD1 
1956 C CD2 . LEU A 280 ? 0.6400 0.4910 0.6199 0.0056  0.1244  -0.0342 375  LEU A CD2 
1957 N N   . TYR A 281 ? 0.6026 0.4997 0.5782 0.0247  0.1179  -0.0301 376  TYR A N   
1958 C CA  . TYR A 281 ? 0.6193 0.5230 0.5930 0.0293  0.1192  -0.0313 376  TYR A CA  
1959 C C   . TYR A 281 ? 0.5969 0.5086 0.5610 0.0242  0.1162  -0.0362 376  TYR A C   
1960 O O   . TYR A 281 ? 0.6198 0.5309 0.5782 0.0253  0.1193  -0.0407 376  TYR A O   
1961 C CB  . TYR A 281 ? 0.5525 0.4665 0.5337 0.0357  0.1168  -0.0230 376  TYR A CB  
1962 C CG  . TYR A 281 ? 0.6114 0.5178 0.6014 0.0415  0.1193  -0.0181 376  TYR A CG  
1963 C CD1 . TYR A 281 ? 0.6068 0.5046 0.6006 0.0467  0.1251  -0.0206 376  TYR A CD1 
1964 C CD2 . TYR A 281 ? 0.6441 0.5517 0.6384 0.0418  0.1161  -0.0109 376  TYR A CD2 
1965 C CE1 . TYR A 281 ? 0.6473 0.5380 0.6498 0.0527  0.1268  -0.0156 376  TYR A CE1 
1966 C CE2 . TYR A 281 ? 0.6931 0.5932 0.6943 0.0472  0.1177  -0.0057 376  TYR A CE2 
1967 C CZ  . TYR A 281 ? 0.7156 0.6073 0.7213 0.0528  0.1227  -0.0078 376  TYR A CZ  
1968 O OH  . TYR A 281 ? 0.7677 0.6520 0.7810 0.0588  0.1236  -0.0020 376  TYR A OH  
1969 N N   . LYS A 282 ? 0.5613 0.4806 0.5233 0.0188  0.1104  -0.0352 377  LYS A N   
1970 C CA  . LYS A 282 ? 0.5670 0.4938 0.5199 0.0146  0.1068  -0.0392 377  LYS A CA  
1971 C C   . LYS A 282 ? 0.6317 0.5489 0.5754 0.0090  0.1091  -0.0484 377  LYS A C   
1972 O O   . LYS A 282 ? 0.6304 0.5491 0.5643 0.0078  0.1094  -0.0530 377  LYS A O   
1973 C CB  . LYS A 282 ? 0.5929 0.5315 0.5476 0.0110  0.0997  -0.0357 377  LYS A CB  
1974 C CG  . LYS A 282 ? 0.6190 0.5549 0.5778 0.0056  0.0980  -0.0359 377  LYS A CG  
1975 C CD  . LYS A 282 ? 0.5523 0.5022 0.5145 0.0030  0.0914  -0.0324 377  LYS A CD  
1976 C CE  . LYS A 282 ? 0.6035 0.5519 0.5694 -0.0039 0.0900  -0.0341 377  LYS A CE  
1977 N NZ  . LYS A 282 ? 0.6067 0.5691 0.5749 -0.0076 0.0835  -0.0336 377  LYS A NZ  
1978 N N   . GLN A 283 ? 0.6030 0.5091 0.5490 0.0056  0.1113  -0.0515 378  GLN A N   
1979 C CA  . GLN A 283 ? 0.6416 0.5363 0.5791 0.0008  0.1148  -0.0611 378  GLN A CA  
1980 C C   . GLN A 283 ? 0.6536 0.5398 0.5882 0.0062  0.1223  -0.0647 378  GLN A C   
1981 O O   . GLN A 283 ? 0.6688 0.5511 0.5926 0.0033  0.1246  -0.0725 378  GLN A O   
1982 C CB  . GLN A 283 ? 0.6397 0.5229 0.5812 -0.0040 0.1163  -0.0635 378  GLN A CB  
1983 C CG  . GLN A 283 ? 0.6062 0.4965 0.5488 -0.0118 0.1098  -0.0634 378  GLN A CG  
1984 C CD  . GLN A 283 ? 0.6466 0.5234 0.5917 -0.0178 0.1124  -0.0676 378  GLN A CD  
1985 O OE1 . GLN A 283 ? 0.6186 0.4919 0.5724 -0.0173 0.1135  -0.0620 378  GLN A OE1 
1986 N NE2 . GLN A 283 ? 0.6562 0.5242 0.5929 -0.0236 0.1140  -0.0775 378  GLN A NE2 
1987 N N   . MET A 284 ? 0.6089 0.4922 0.5533 0.0139  0.1264  -0.0594 379  MET A N   
1988 C CA  . MET A 284 ? 0.6329 0.5099 0.5766 0.0194  0.1338  -0.0629 379  MET A CA  
1989 C C   . MET A 284 ? 0.6703 0.5576 0.6063 0.0204  0.1335  -0.0638 379  MET A C   
1990 O O   . MET A 284 ? 0.6751 0.5572 0.6040 0.0207  0.1394  -0.0705 379  MET A O   
1991 C CB  . MET A 284 ? 0.6176 0.4921 0.5749 0.0279  0.1369  -0.0561 379  MET A CB  
1992 C CG  . MET A 284 ? 0.7007 0.5602 0.6643 0.0282  0.1399  -0.0563 379  MET A CG  
1993 S SD  . MET A 284 ? 0.8475 0.7067 0.8266 0.0379  0.1404  -0.0456 379  MET A SD  
1994 C CE  . MET A 284 ? 0.7592 0.6167 0.7423 0.0460  0.1481  -0.0493 379  MET A CE  
1995 N N   . CYS A 285 ? 0.6339 0.5353 0.5709 0.0206  0.1272  -0.0573 380  CYS A N   
1996 C CA  . CYS A 285 ? 0.6577 0.5682 0.5864 0.0206  0.1263  -0.0576 380  CYS A CA  
1997 C C   . CYS A 285 ? 0.6509 0.5592 0.5639 0.0133  0.1246  -0.0652 380  CYS A C   
1998 O O   . CYS A 285 ? 0.6531 0.5614 0.5559 0.0131  0.1280  -0.0690 380  CYS A O   
1999 C CB  . CYS A 285 ? 0.6066 0.5312 0.5398 0.0221  0.1195  -0.0492 380  CYS A CB  
2000 S SG  . CYS A 285 ? 0.6129 0.5420 0.5615 0.0308  0.1214  -0.0410 380  CYS A SG  
2001 N N   . ILE A 286 ? 0.6334 0.5404 0.5441 0.0070  0.1194  -0.0674 381  ILE A N   
2002 C CA  . ILE A 286 ? 0.6381 0.5433 0.5338 -0.0003 0.1171  -0.0751 381  ILE A CA  
2003 C C   . ILE A 286 ? 0.7074 0.5983 0.5956 -0.0014 0.1254  -0.0846 381  ILE A C   
2004 O O   . ILE A 286 ? 0.6571 0.5464 0.5307 -0.0043 0.1271  -0.0907 381  ILE A O   
2005 C CB  . ILE A 286 ? 0.6906 0.5987 0.5872 -0.0073 0.1095  -0.0759 381  ILE A CB  
2006 C CG1 . ILE A 286 ? 0.6822 0.6055 0.5847 -0.0062 0.1017  -0.0674 381  ILE A CG1 
2007 C CG2 . ILE A 286 ? 0.6798 0.5851 0.5610 -0.0152 0.1069  -0.0849 381  ILE A CG2 
2008 C CD1 . ILE A 286 ? 0.6641 0.5966 0.5567 -0.0055 0.0982  -0.0657 381  ILE A CD1 
2009 N N   . ASN A 287 ? 0.6724 0.5520 0.5701 0.0013  0.1311  -0.0859 382  ASN A N   
2010 C CA  . ASN A 287 ? 0.7112 0.5764 0.6037 0.0013  0.1399  -0.0950 382  ASN A CA  
2011 C C   . ASN A 287 ? 0.7320 0.5985 0.6223 0.0074  0.1470  -0.0955 382  ASN A C   
2012 O O   . ASN A 287 ? 0.7479 0.6042 0.6307 0.0069  0.1547  -0.1041 382  ASN A O   
2013 C CB  . ASN A 287 ? 0.6996 0.5519 0.6042 0.0037  0.1443  -0.0953 382  ASN A CB  
2014 C CG  . ASN A 287 ? 0.7213 0.5682 0.6257 -0.0040 0.1398  -0.0979 382  ASN A CG  
2015 O OD1 . ASN A 287 ? 0.7357 0.5843 0.6288 -0.0121 0.1355  -0.1040 382  ASN A OD1 
2016 N ND2 . ASN A 287 ? 0.7037 0.5442 0.6208 -0.0019 0.1406  -0.0934 382  ASN A ND2 
2017 N N   . SER A 288 ? 0.7207 0.5993 0.6176 0.0128  0.1452  -0.0868 383  SER A N   
2018 C CA  . SER A 288 ? 0.6885 0.5700 0.5843 0.0179  0.1519  -0.0867 383  SER A CA  
2019 C C   . SER A 288 ? 0.7282 0.6164 0.6072 0.0137  0.1500  -0.0886 383  SER A C   
2020 O O   . SER A 288 ? 0.7189 0.6094 0.5948 0.0167  0.1561  -0.0891 383  SER A O   
2021 C CB  . SER A 288 ? 0.6812 0.5723 0.5929 0.0254  0.1510  -0.0768 383  SER A CB  
2022 O OG  . SER A 288 ? 0.7183 0.6026 0.6448 0.0304  0.1536  -0.0747 383  SER A OG  
2023 N N   . GLY A 289 ? 0.7204 0.6123 0.5890 0.0069  0.1416  -0.0892 384  GLY A N   
2024 C CA  . GLY A 289 ? 0.6898 0.5877 0.5415 0.0028  0.1385  -0.0902 384  GLY A CA  
2025 C C   . GLY A 289 ? 0.7075 0.6194 0.5615 0.0040  0.1306  -0.0805 384  GLY A C   
2026 O O   . GLY A 289 ? 0.6880 0.6045 0.5284 0.0017  0.1286  -0.0799 384  GLY A O   
2027 N N   . PHE A 290 ? 0.6668 0.5849 0.5369 0.0075  0.1262  -0.0728 385  PHE A N   
2028 C CA  . PHE A 290 ? 0.6577 0.5885 0.5309 0.0091  0.1194  -0.0641 385  PHE A CA  
2029 C C   . PHE A 290 ? 0.6634 0.5999 0.5275 0.0031  0.1095  -0.0638 385  PHE A C   
2030 O O   . PHE A 290 ? 0.6700 0.6160 0.5332 0.0040  0.1040  -0.0575 385  PHE A O   
2031 C CB  . PHE A 290 ? 0.6557 0.5914 0.5476 0.0141  0.1175  -0.0567 385  PHE A CB  
2032 C CG  . PHE A 290 ? 0.6692 0.6045 0.5720 0.0211  0.1247  -0.0539 385  PHE A CG  
2033 C CD1 . PHE A 290 ? 0.7014 0.6432 0.6190 0.0258  0.1223  -0.0464 385  PHE A CD1 
2034 C CD2 . PHE A 290 ? 0.6891 0.6181 0.5878 0.0228  0.1337  -0.0590 385  PHE A CD2 
2035 C CE1 . PHE A 290 ? 0.7057 0.6482 0.6340 0.0321  0.1280  -0.0439 385  PHE A CE1 
2036 C CE2 . PHE A 290 ? 0.6872 0.6172 0.5980 0.0294  0.1400  -0.0565 385  PHE A CE2 
2037 C CZ  . PHE A 290 ? 0.6334 0.5704 0.5591 0.0339  0.1367  -0.0489 385  PHE A CZ  
2038 N N   . ASP A 291 ? 0.6348 0.5660 0.4938 -0.0027 0.1069  -0.0703 386  ASP A N   
2039 C CA  . ASP A 291 ? 0.6813 0.6174 0.5303 -0.0091 0.0978  -0.0719 386  ASP A CA  
2040 C C   . ASP A 291 ? 0.6723 0.6197 0.5327 -0.0090 0.0886  -0.0651 386  ASP A C   
2041 O O   . ASP A 291 ? 0.6845 0.6333 0.5466 -0.0141 0.0830  -0.0679 386  ASP A O   
2042 C CB  . ASP A 291 ? 0.6915 0.6301 0.5225 -0.0107 0.0965  -0.0723 386  ASP A CB  
2043 C CG  . ASP A 291 ? 0.7620 0.7027 0.5795 -0.0180 0.0880  -0.0765 386  ASP A CG  
2044 O OD1 . ASP A 291 ? 0.7698 0.7207 0.5858 -0.0185 0.0790  -0.0709 386  ASP A OD1 
2045 O OD2 . ASP A 291 ? 0.7607 0.6929 0.5698 -0.0233 0.0899  -0.0857 386  ASP A OD2 
2046 N N   . ARG A 292 ? 0.6084 0.5640 0.4768 -0.0036 0.0873  -0.0566 387  ARG A N   
2047 C CA  . ARG A 292 ? 0.6067 0.5730 0.4861 -0.0029 0.0796  -0.0502 387  ARG A CA  
2048 C C   . ARG A 292 ? 0.6079 0.5773 0.5009 0.0038  0.0828  -0.0433 387  ARG A C   
2049 O O   . ARG A 292 ? 0.5848 0.5562 0.4758 0.0077  0.0853  -0.0396 387  ARG A O   
2050 C CB  . ARG A 292 ? 0.6062 0.5816 0.4774 -0.0044 0.0714  -0.0471 387  ARG A CB  
2051 C CG  . ARG A 292 ? 0.6473 0.6217 0.5051 -0.0112 0.0661  -0.0532 387  ARG A CG  
2052 C CD  . ARG A 292 ? 0.6565 0.6401 0.5067 -0.0120 0.0571  -0.0491 387  ARG A CD  
2053 N NE  . ARG A 292 ? 0.6871 0.6709 0.5265 -0.0189 0.0508  -0.0552 387  ARG A NE  
2054 C CZ  . ARG A 292 ? 0.7116 0.7046 0.5474 -0.0211 0.0404  -0.0530 387  ARG A CZ  
2055 N NH1 . ARG A 292 ? 0.6997 0.7014 0.5407 -0.0166 0.0355  -0.0447 387  ARG A NH1 
2056 N NH2 . ARG A 292 ? 0.6769 0.6702 0.5042 -0.0279 0.0346  -0.0595 387  ARG A NH2 
2057 N N   . VAL A 293 ? 0.5783 0.5481 0.4846 0.0046  0.0828  -0.0416 388  VAL A N   
2058 C CA  . VAL A 293 ? 0.5644 0.5369 0.4831 0.0106  0.0854  -0.0354 388  VAL A CA  
2059 C C   . VAL A 293 ? 0.5673 0.5477 0.4967 0.0102  0.0798  -0.0310 388  VAL A C   
2060 O O   . VAL A 293 ? 0.5553 0.5364 0.4861 0.0055  0.0764  -0.0337 388  VAL A O   
2061 C CB  . VAL A 293 ? 0.6066 0.5691 0.5305 0.0133  0.0931  -0.0373 388  VAL A CB  
2062 C CG1 . VAL A 293 ? 0.5397 0.4950 0.4543 0.0141  0.0997  -0.0421 388  VAL A CG1 
2063 C CG2 . VAL A 293 ? 0.5571 0.5131 0.4844 0.0092  0.0931  -0.0411 388  VAL A CG2 
2064 N N   . PHE A 294 ? 0.5334 0.5199 0.4707 0.0150  0.0794  -0.0247 389  PHE A N   
2065 C CA  . PHE A 294 ? 0.5076 0.5004 0.4558 0.0155  0.0762  -0.0207 389  PHE A CA  
2066 C C   . PHE A 294 ? 0.5403 0.5329 0.4966 0.0211  0.0799  -0.0160 389  PHE A C   
2067 O O   . PHE A 294 ? 0.5314 0.5225 0.4862 0.0248  0.0833  -0.0148 389  PHE A O   
2068 C CB  . PHE A 294 ? 0.5392 0.5430 0.4883 0.0149  0.0693  -0.0179 389  PHE A CB  
2069 C CG  . PHE A 294 ? 0.5287 0.5369 0.4769 0.0194  0.0688  -0.0134 389  PHE A CG  
2070 C CD1 . PHE A 294 ? 0.5656 0.5781 0.5228 0.0235  0.0694  -0.0085 389  PHE A CD1 
2071 C CD2 . PHE A 294 ? 0.5302 0.5379 0.4677 0.0190  0.0677  -0.0141 389  PHE A CD2 
2072 C CE1 . PHE A 294 ? 0.5561 0.5721 0.5128 0.0270  0.0691  -0.0048 389  PHE A CE1 
2073 C CE2 . PHE A 294 ? 0.5606 0.5714 0.4973 0.0225  0.0677  -0.0098 389  PHE A CE2 
2074 C CZ  . PHE A 294 ? 0.5702 0.5851 0.5171 0.0265  0.0684  -0.0053 389  PHE A CZ  
2075 N N   . GLU A 295 ? 0.5117 0.5062 0.4766 0.0212  0.0792  -0.0133 390  GLU A N   
2076 C CA  . GLU A 295 ? 0.5107 0.5062 0.4829 0.0260  0.0813  -0.0084 390  GLU A CA  
2077 C C   . GLU A 295 ? 0.5374 0.5413 0.5160 0.0257  0.0775  -0.0048 390  GLU A C   
2078 O O   . GLU A 295 ? 0.5342 0.5402 0.5143 0.0215  0.0753  -0.0062 390  GLU A O   
2079 C CB  . GLU A 295 ? 0.5192 0.5050 0.4944 0.0271  0.0861  -0.0088 390  GLU A CB  
2080 C CG  . GLU A 295 ? 0.5184 0.5053 0.5004 0.0325  0.0876  -0.0035 390  GLU A CG  
2081 C CD  . GLU A 295 ? 0.5738 0.5508 0.5581 0.0352  0.0924  -0.0036 390  GLU A CD  
2082 O OE1 . GLU A 295 ? 0.5520 0.5200 0.5328 0.0328  0.0952  -0.0082 390  GLU A OE1 
2083 O OE2 . GLU A 295 ? 0.5330 0.5111 0.5230 0.0399  0.0931  0.0008  390  GLU A OE2 
2084 N N   . VAL A 296 ? 0.5207 0.5299 0.5035 0.0298  0.0770  -0.0005 391  VAL A N   
2085 C CA  . VAL A 296 ? 0.5077 0.5241 0.4965 0.0302  0.0746  0.0028  391  VAL A CA  
2086 C C   . VAL A 296 ? 0.5097 0.5236 0.5023 0.0337  0.0772  0.0064  391  VAL A C   
2087 O O   . VAL A 296 ? 0.4780 0.4927 0.4712 0.0376  0.0780  0.0081  391  VAL A O   
2088 C CB  . VAL A 296 ? 0.5111 0.5360 0.5005 0.0316  0.0710  0.0042  391  VAL A CB  
2089 C CG1 . VAL A 296 ? 0.4732 0.5049 0.4691 0.0324  0.0694  0.0070  391  VAL A CG1 
2090 C CG2 . VAL A 296 ? 0.4923 0.5197 0.4775 0.0285  0.0675  0.0014  391  VAL A CG2 
2091 N N   . ALA A 297 ? 0.4946 0.5055 0.4897 0.0323  0.0785  0.0077  392  ALA A N   
2092 C CA  . ALA A 297 ? 0.5092 0.5156 0.5063 0.0358  0.0808  0.0111  392  ALA A CA  
2093 C C   . ALA A 297 ? 0.4912 0.4957 0.4899 0.0337  0.0815  0.0137  392  ALA A C   
2094 O O   . ALA A 297 ? 0.5148 0.5187 0.5134 0.0290  0.0816  0.0117  392  ALA A O   
2095 C CB  . ALA A 297 ? 0.4704 0.4674 0.4659 0.0375  0.0842  0.0094  392  ALA A CB  
2096 N N   . PRO A 298 ? 0.4896 0.4934 0.4898 0.0369  0.0819  0.0181  393  PRO A N   
2097 C CA  . PRO A 298 ? 0.5187 0.5193 0.5187 0.0349  0.0830  0.0214  393  PRO A CA  
2098 C C   . PRO A 298 ? 0.5255 0.5147 0.5244 0.0325  0.0861  0.0207  393  PRO A C   
2099 O O   . PRO A 298 ? 0.5146 0.4967 0.5131 0.0343  0.0877  0.0188  393  PRO A O   
2100 C CB  . PRO A 298 ? 0.5234 0.5249 0.5237 0.0396  0.0822  0.0264  393  PRO A CB  
2101 C CG  . PRO A 298 ? 0.5139 0.5211 0.5160 0.0433  0.0804  0.0253  393  PRO A CG  
2102 C CD  . PRO A 298 ? 0.5188 0.5246 0.5205 0.0422  0.0812  0.0206  393  PRO A CD  
2103 N N   . VAL A 299 ? 0.5115 0.4985 0.5099 0.0282  0.0874  0.0221  394  VAL A N   
2104 C CA  . VAL A 299 ? 0.5226 0.4976 0.5201 0.0257  0.0906  0.0230  394  VAL A CA  
2105 C C   . VAL A 299 ? 0.5574 0.5312 0.5535 0.0247  0.0917  0.0288  394  VAL A C   
2106 O O   . VAL A 299 ? 0.5604 0.5436 0.5563 0.0240  0.0904  0.0302  394  VAL A O   
2107 C CB  . VAL A 299 ? 0.5634 0.5358 0.5613 0.0193  0.0918  0.0174  394  VAL A CB  
2108 C CG1 . VAL A 299 ? 0.5359 0.5088 0.5329 0.0201  0.0907  0.0117  394  VAL A CG1 
2109 C CG2 . VAL A 299 ? 0.5586 0.5412 0.5588 0.0142  0.0906  0.0164  394  VAL A CG2 
2110 N N   . PHE A 300 ? 0.5285 0.4898 0.5230 0.0244  0.0944  0.0320  395  PHE A N   
2111 C CA  . PHE A 300 ? 0.5795 0.5367 0.5707 0.0246  0.0954  0.0390  395  PHE A CA  
2112 C C   . PHE A 300 ? 0.6417 0.5875 0.6318 0.0188  0.0995  0.0399  395  PHE A C   
2113 O O   . PHE A 300 ? 0.6061 0.5404 0.5972 0.0187  0.1014  0.0382  395  PHE A O   
2114 C CB  . PHE A 300 ? 0.5686 0.5207 0.5588 0.0319  0.0939  0.0442  395  PHE A CB  
2115 C CG  . PHE A 300 ? 0.6021 0.5642 0.5947 0.0372  0.0903  0.0426  395  PHE A CG  
2116 C CD1 . PHE A 300 ? 0.5799 0.5517 0.5707 0.0392  0.0874  0.0455  395  PHE A CD1 
2117 C CD2 . PHE A 300 ? 0.5948 0.5563 0.5910 0.0398  0.0903  0.0380  395  PHE A CD2 
2118 C CE1 . PHE A 300 ? 0.5712 0.5518 0.5649 0.0434  0.0844  0.0439  395  PHE A CE1 
2119 C CE2 . PHE A 300 ? 0.5443 0.5148 0.5431 0.0441  0.0876  0.0367  395  PHE A CE2 
2120 C CZ  . PHE A 300 ? 0.5483 0.5282 0.5462 0.0458  0.0846  0.0397  395  PHE A CZ  
2121 N N   . ARG A 301 ? 0.5887 0.5374 0.5769 0.0139  0.1013  0.0425  396  ARG A N   
2122 C CA  . ARG A 301 ? 0.6311 0.5706 0.6186 0.0071  0.1057  0.0435  396  ARG A CA  
2123 C C   . ARG A 301 ? 0.6865 0.6212 0.6679 0.0070  0.1076  0.0519  396  ARG A C   
2124 O O   . ARG A 301 ? 0.6810 0.6258 0.6596 0.0075  0.1066  0.0540  396  ARG A O   
2125 C CB  . ARG A 301 ? 0.6893 0.6388 0.6814 -0.0003 0.1068  0.0379  396  ARG A CB  
2126 C CG  . ARG A 301 ? 0.7439 0.6924 0.7407 -0.0038 0.1064  0.0303  396  ARG A CG  
2127 C CD  . ARG A 301 ? 0.7731 0.7328 0.7755 -0.0112 0.1069  0.0257  396  ARG A CD  
2128 N NE  . ARG A 301 ? 0.8068 0.7589 0.8103 -0.0189 0.1116  0.0267  396  ARG A NE  
2129 N N   . ALA A 302 ? 0.7177 0.6365 0.6962 0.0061  0.1105  0.0567  397  ALA A N   
2130 C CA  . ALA A 302 ? 0.7405 0.6527 0.7112 0.0068  0.1118  0.0659  397  ALA A CA  
2131 C C   . ALA A 302 ? 0.7637 0.6709 0.7319 -0.0020 0.1174  0.0682  397  ALA A C   
2132 O O   . ALA A 302 ? 0.8093 0.7072 0.7700 -0.0023 0.1195  0.0765  397  ALA A O   
2133 C CB  . ALA A 302 ? 0.7476 0.6448 0.7161 0.0132  0.1107  0.0718  397  ALA A CB  
2134 N N   . GLU A 303 ? 0.7267 0.6403 0.7011 -0.0092 0.1199  0.0614  398  GLU A N   
2135 C CA  . GLU A 303 ? 0.7792 0.6899 0.7528 -0.0181 0.1258  0.0632  398  GLU A CA  
2136 C C   . GLU A 303 ? 0.7722 0.6919 0.7395 -0.0189 0.1272  0.0679  398  GLU A C   
2137 O O   . GLU A 303 ? 0.7377 0.6726 0.7062 -0.0160 0.1243  0.0650  398  GLU A O   
2138 C CB  . GLU A 303 ? 0.8158 0.7344 0.7991 -0.0256 0.1273  0.0542  398  GLU A CB  
2139 C CG  . GLU A 303 ? 0.9370 0.8551 0.9262 -0.0234 0.1237  0.0466  398  GLU A CG  
2140 C CD  . GLU A 303 ? 1.0267 0.9581 1.0249 -0.0295 0.1230  0.0379  398  GLU A CD  
2141 N N   . ASN A 304 ? 0.7768 0.6866 0.7370 -0.0232 0.1322  0.0751  399  ASN A N   
2142 C CA  . ASN A 304 ? 0.7915 0.7080 0.7435 -0.0247 0.1346  0.0800  399  ASN A CA  
2143 C C   . ASN A 304 ? 0.7609 0.6899 0.7197 -0.0332 0.1397  0.0744  399  ASN A C   
2144 O O   . ASN A 304 ? 0.7907 0.7151 0.7474 -0.0408 0.1464  0.0774  399  ASN A O   
2145 C CB  . ASN A 304 ? 0.7632 0.6633 0.7031 -0.0254 0.1376  0.0908  399  ASN A CB  
2146 C CG  . ASN A 304 ? 0.8333 0.7396 0.7615 -0.0251 0.1387  0.0963  399  ASN A CG  
2147 O OD1 . ASN A 304 ? 0.8324 0.7552 0.7628 -0.0260 0.1390  0.0913  399  ASN A OD1 
2148 N ND2 . ASN A 304 ? 0.8770 0.7699 0.7923 -0.0237 0.1393  0.1067  399  ASN A ND2 
2149 N N   . SER A 305 ? 0.7555 0.7009 0.7230 -0.0316 0.1365  0.0665  400  SER A N   
2150 C CA  . SER A 305 ? 0.7460 0.7054 0.7236 -0.0383 0.1399  0.0598  400  SER A CA  
2151 C C   . SER A 305 ? 0.7456 0.7216 0.7229 -0.0348 0.1385  0.0576  400  SER A C   
2152 O O   . SER A 305 ? 0.6745 0.6554 0.6513 -0.0273 0.1324  0.0559  400  SER A O   
2153 C CB  . SER A 305 ? 0.7664 0.7292 0.7564 -0.0398 0.1368  0.0516  400  SER A CB  
2154 O OG  . SER A 305 ? 0.7964 0.7729 0.7976 -0.0464 0.1394  0.0454  400  SER A OG  
2155 N N   . ASN A 306 ? 0.7232 0.7073 0.7008 -0.0402 0.1446  0.0577  401  ASN A N   
2156 C CA  . ASN A 306 ? 0.7277 0.7267 0.7049 -0.0375 0.1447  0.0552  401  ASN A CA  
2157 C C   . ASN A 306 ? 0.7386 0.7531 0.7308 -0.0427 0.1479  0.0477  401  ASN A C   
2158 O O   . ASN A 306 ? 0.6856 0.7033 0.6797 -0.0498 0.1554  0.0482  401  ASN A O   
2159 C CB  . ASN A 306 ? 0.6688 0.6636 0.6311 -0.0385 0.1496  0.0622  401  ASN A CB  
2160 C CG  . ASN A 306 ? 0.7605 0.7441 0.7088 -0.0316 0.1444  0.0691  401  ASN A CG  
2161 O OD1 . ASN A 306 ? 0.7292 0.7185 0.6768 -0.0245 0.1382  0.0671  401  ASN A OD1 
2162 N ND2 . ASN A 306 ? 0.7509 0.7186 0.6888 -0.0335 0.1467  0.0774  401  ASN A ND2 
2163 N N   . THR A 307 ? 0.6650 0.6893 0.6683 -0.0393 0.1421  0.0410  402  THR A N   
2164 C CA  . THR A 307 ? 0.6717 0.7115 0.6909 -0.0433 0.1435  0.0338  402  THR A CA  
2165 C C   . THR A 307 ? 0.6773 0.7304 0.7022 -0.0364 0.1380  0.0289  402  THR A C   
2166 O O   . THR A 307 ? 0.6447 0.6944 0.6622 -0.0292 0.1328  0.0303  402  THR A O   
2167 C CB  . THR A 307 ? 0.6788 0.7161 0.7083 -0.0483 0.1417  0.0301  402  THR A CB  
2168 O OG1 . THR A 307 ? 0.6336 0.6689 0.6638 -0.0423 0.1335  0.0275  402  THR A OG1 
2169 C CG2 . THR A 307 ? 0.6745 0.6952 0.6978 -0.0547 0.1465  0.0352  402  THR A CG2 
2170 N N   . TYR A 308 ? 0.6337 0.7022 0.6731 -0.0388 0.1391  0.0230  403  TYR A N   
2171 C CA  . TYR A 308 ? 0.6079 0.6893 0.6549 -0.0327 0.1340  0.0181  403  TYR A CA  
2172 C C   . TYR A 308 ? 0.6221 0.7005 0.6705 -0.0279 0.1252  0.0162  403  TYR A C   
2173 O O   . TYR A 308 ? 0.5847 0.6708 0.6366 -0.0220 0.1204  0.0134  403  TYR A O   
2174 C CB  . TYR A 308 ? 0.6111 0.7095 0.6755 -0.0366 0.1369  0.0124  403  TYR A CB  
2175 C CG  . TYR A 308 ? 0.6522 0.7541 0.7290 -0.0405 0.1330  0.0085  403  TYR A CG  
2176 C CD1 . TYR A 308 ? 0.6377 0.7483 0.7236 -0.0362 0.1252  0.0041  403  TYR A CD1 
2177 C CD2 . TYR A 308 ? 0.6626 0.7579 0.7408 -0.0488 0.1367  0.0095  403  TYR A CD2 
2178 C CE1 . TYR A 308 ? 0.6554 0.7690 0.7509 -0.0400 0.1208  0.0005  403  TYR A CE1 
2179 C CE2 . TYR A 308 ? 0.6838 0.7820 0.7727 -0.0530 0.1327  0.0053  403  TYR A CE2 
2180 C CZ  . TYR A 308 ? 0.6974 0.8050 0.7944 -0.0486 0.1245  0.0007  403  TYR A CZ  
2181 O OH  . TYR A 308 ? 0.6615 0.7721 0.7676 -0.0529 0.1198  -0.0036 403  TYR A OH  
2182 N N   . ARG A 309 ? 0.5925 0.6597 0.6381 -0.0304 0.1232  0.0174  404  ARG A N   
2183 C CA  . ARG A 309 ? 0.6373 0.7026 0.6841 -0.0263 0.1156  0.0149  404  ARG A CA  
2184 C C   . ARG A 309 ? 0.6378 0.6869 0.6729 -0.0234 0.1134  0.0187  404  ARG A C   
2185 O O   . ARG A 309 ? 0.6624 0.7095 0.6976 -0.0200 0.1078  0.0165  404  ARG A O   
2186 C CB  . ARG A 309 ? 0.6974 0.7689 0.7563 -0.0314 0.1132  0.0095  404  ARG A CB  
2187 C CG  . ARG A 309 ? 0.7417 0.8051 0.8017 -0.0399 0.1175  0.0100  404  ARG A CG  
2188 C CD  . ARG A 309 ? 0.8373 0.9090 0.9100 -0.0449 0.1139  0.0036  404  ARG A CD  
2189 N NE  . ARG A 309 ? 0.8730 0.9328 0.9414 -0.0467 0.1106  0.0022  404  ARG A NE  
2190 C CZ  . ARG A 309 ? 0.8651 0.9292 0.9415 -0.0515 0.1068  -0.0034 404  ARG A CZ  
2191 N NH1 . ARG A 309 ? 0.8028 0.8840 0.8931 -0.0543 0.1048  -0.0077 404  ARG A NH1 
2192 N NH2 . ARG A 309 ? 0.9018 0.9531 0.9725 -0.0535 0.1050  -0.0050 404  ARG A NH2 
2193 N N   . HIS A 310 ? 0.6331 0.6705 0.6583 -0.0244 0.1176  0.0244  405  HIS A N   
2194 C CA  . HIS A 310 ? 0.6420 0.6640 0.6581 -0.0214 0.1156  0.0281  405  HIS A CA  
2195 C C   . HIS A 310 ? 0.5895 0.6098 0.5968 -0.0136 0.1129  0.0319  405  HIS A C   
2196 O O   . HIS A 310 ? 0.5935 0.6160 0.5952 -0.0130 0.1156  0.0352  405  HIS A O   
2197 C CB  . HIS A 310 ? 0.6718 0.6802 0.6828 -0.0268 0.1210  0.0328  405  HIS A CB  
2198 C CG  . HIS A 310 ? 0.7322 0.7243 0.7350 -0.0230 0.1192  0.0369  405  HIS A CG  
2199 N ND1 . HIS A 310 ? 0.7631 0.7478 0.7687 -0.0235 0.1169  0.0336  405  HIS A ND1 
2200 C CD2 . HIS A 310 ? 0.7147 0.6974 0.7071 -0.0183 0.1190  0.0436  405  HIS A CD2 
2201 C CE1 . HIS A 310 ? 0.7555 0.7266 0.7537 -0.0190 0.1161  0.0381  405  HIS A CE1 
2202 N NE2 . HIS A 310 ? 0.7455 0.7154 0.7361 -0.0156 0.1170  0.0444  405  HIS A NE2 
2203 N N   . LEU A 311 ? 0.5993 0.6158 0.6050 -0.0082 0.1078  0.0311  406  LEU A N   
2204 C CA  . LEU A 311 ? 0.5935 0.6070 0.5917 -0.0012 0.1051  0.0348  406  LEU A CA  
2205 C C   . LEU A 311 ? 0.6163 0.6151 0.6093 0.0011  0.1042  0.0383  406  LEU A C   
2206 O O   . LEU A 311 ? 0.5668 0.5598 0.5632 -0.0009 0.1040  0.0356  406  LEU A O   
2207 C CB  . LEU A 311 ? 0.5334 0.5567 0.5354 0.0039  0.1001  0.0308  406  LEU A CB  
2208 C CG  . LEU A 311 ? 0.5379 0.5752 0.5453 0.0033  0.1006  0.0275  406  LEU A CG  
2209 C CD1 . LEU A 311 ? 0.5432 0.5880 0.5549 0.0081  0.0954  0.0237  406  LEU A CD1 
2210 C CD2 . LEU A 311 ? 0.5602 0.5994 0.5612 0.0038  0.1036  0.0309  406  LEU A CD2 
2211 N N   . CYS A 312 ? 0.5501 0.5430 0.5351 0.0053  0.1036  0.0442  407  CYS A N   
2212 C CA  . CYS A 312 ? 0.5679 0.5478 0.5496 0.0089  0.1023  0.0478  407  CYS A CA  
2213 C C   . CYS A 312 ? 0.5972 0.5792 0.5821 0.0148  0.0977  0.0446  407  CYS A C   
2214 O O   . CYS A 312 ? 0.5293 0.5015 0.5142 0.0174  0.0972  0.0455  407  CYS A O   
2215 C CB  . CYS A 312 ? 0.5820 0.5556 0.5546 0.0116  0.1024  0.0557  407  CYS A CB  
2216 S SG  . CYS A 312 ? 0.6651 0.6329 0.6313 0.0045  0.1086  0.0609  407  CYS A SG  
2217 N N   . GLU A 313 ? 0.5284 0.5226 0.5162 0.0169  0.0949  0.0410  408  GLU A N   
2218 C CA  . GLU A 313 ? 0.5218 0.5189 0.5126 0.0217  0.0912  0.0380  408  GLU A CA  
2219 C C   . GLU A 313 ? 0.5381 0.5467 0.5342 0.0201  0.0898  0.0322  408  GLU A C   
2220 O O   . GLU A 313 ? 0.5346 0.5519 0.5314 0.0188  0.0902  0.0318  408  GLU A O   
2221 C CB  . GLU A 313 ? 0.5403 0.5394 0.5279 0.0278  0.0882  0.0415  408  GLU A CB  
2222 C CG  . GLU A 313 ? 0.5781 0.5825 0.5696 0.0319  0.0849  0.0379  408  GLU A CG  
2223 C CD  . GLU A 313 ? 0.6178 0.6244 0.6078 0.0375  0.0818  0.0409  408  GLU A CD  
2224 O OE1 . GLU A 313 ? 0.5711 0.5817 0.5646 0.0405  0.0797  0.0383  408  GLU A OE1 
2225 O OE2 . GLU A 313 ? 0.5933 0.5977 0.5784 0.0385  0.0814  0.0459  408  GLU A OE2 
2226 N N   . TYR A 314 ? 0.5168 0.5252 0.5162 0.0202  0.0883  0.0279  409  TYR A N   
2227 C CA  . TYR A 314 ? 0.5113 0.5303 0.5153 0.0192  0.0861  0.0232  409  TYR A CA  
2228 C C   . TYR A 314 ? 0.5136 0.5311 0.5179 0.0219  0.0835  0.0202  409  TYR A C   
2229 O O   . TYR A 314 ? 0.5357 0.5449 0.5374 0.0245  0.0841  0.0213  409  TYR A O   
2230 C CB  . TYR A 314 ? 0.5051 0.5279 0.5136 0.0128  0.0878  0.0204  409  TYR A CB  
2231 C CG  . TYR A 314 ? 0.5298 0.5441 0.5387 0.0084  0.0892  0.0183  409  TYR A CG  
2232 C CD1 . TYR A 314 ? 0.5599 0.5763 0.5713 0.0068  0.0867  0.0132  409  TYR A CD1 
2233 C CD2 . TYR A 314 ? 0.5648 0.5686 0.5710 0.0056  0.0931  0.0213  409  TYR A CD2 
2234 C CE1 . TYR A 314 ? 0.5909 0.5993 0.6022 0.0022  0.0880  0.0103  409  TYR A CE1 
2235 C CE2 . TYR A 314 ? 0.5828 0.5777 0.5896 0.0012  0.0947  0.0188  409  TYR A CE2 
2236 C CZ  . TYR A 314 ? 0.6000 0.5976 0.6094 -0.0006 0.0921  0.0129  409  TYR A CZ  
2237 O OH  . TYR A 314 ? 0.7376 0.7264 0.7471 -0.0054 0.0935  0.0094  409  TYR A OH  
2238 N N   . VAL A 315 ? 0.4776 0.5034 0.4850 0.0215  0.0809  0.0165  410  VAL A N   
2239 C CA  . VAL A 315 ? 0.4437 0.4689 0.4500 0.0236  0.0785  0.0139  410  VAL A CA  
2240 C C   . VAL A 315 ? 0.5183 0.5421 0.5252 0.0189  0.0780  0.0096  410  VAL A C   
2241 O O   . VAL A 315 ? 0.4683 0.4991 0.4795 0.0152  0.0768  0.0076  410  VAL A O   
2242 C CB  . VAL A 315 ? 0.4913 0.5256 0.4993 0.0268  0.0755  0.0135  410  VAL A CB  
2243 C CG1 . VAL A 315 ? 0.4789 0.5123 0.4847 0.0280  0.0733  0.0109  410  VAL A CG1 
2244 C CG2 . VAL A 315 ? 0.4679 0.5029 0.4749 0.0310  0.0758  0.0170  410  VAL A CG2 
2245 N N   . SER A 316 ? 0.4733 0.4884 0.4764 0.0190  0.0789  0.0078  411  SER A N   
2246 C CA  . SER A 316 ? 0.5215 0.5340 0.5236 0.0143  0.0783  0.0030  411  SER A CA  
2247 C C   . SER A 316 ? 0.5001 0.5153 0.4986 0.0161  0.0753  0.0002  411  SER A C   
2248 O O   . SER A 316 ? 0.4895 0.5019 0.4849 0.0206  0.0761  0.0014  411  SER A O   
2249 C CB  . SER A 316 ? 0.5465 0.5459 0.5459 0.0125  0.0820  0.0020  411  SER A CB  
2250 O OG  . SER A 316 ? 0.5724 0.5692 0.5707 0.0069  0.0814  -0.0034 411  SER A OG  
2251 N N   . LEU A 317 ? 0.4892 0.5105 0.4885 0.0125  0.0718  -0.0031 412  LEU A N   
2252 C CA  . LEU A 317 ? 0.5410 0.5635 0.5349 0.0128  0.0687  -0.0060 412  LEU A CA  
2253 C C   . LEU A 317 ? 0.5498 0.5642 0.5390 0.0080  0.0697  -0.0111 412  LEU A C   
2254 O O   . LEU A 317 ? 0.5394 0.5553 0.5316 0.0025  0.0686  -0.0137 412  LEU A O   
2255 C CB  . LEU A 317 ? 0.5119 0.5463 0.5095 0.0122  0.0633  -0.0062 412  LEU A CB  
2256 C CG  . LEU A 317 ? 0.5224 0.5656 0.5273 0.0151  0.0626  -0.0024 412  LEU A CG  
2257 C CD1 . LEU A 317 ? 0.5101 0.5643 0.5197 0.0143  0.0572  -0.0034 412  LEU A CD1 
2258 C CD2 . LEU A 317 ? 0.4559 0.4975 0.4586 0.0210  0.0640  0.0011  412  LEU A CD2 
2259 N N   . ASP A 318 ? 0.5492 0.5549 0.5314 0.0098  0.0723  -0.0127 413  ASP A N   
2260 C CA  . ASP A 318 ? 0.5793 0.5752 0.5563 0.0057  0.0744  -0.0180 413  ASP A CA  
2261 C C   . ASP A 318 ? 0.5670 0.5628 0.5348 0.0050  0.0723  -0.0220 413  ASP A C   
2262 O O   . ASP A 318 ? 0.5603 0.5579 0.5245 0.0094  0.0724  -0.0200 413  ASP A O   
2263 C CB  . ASP A 318 ? 0.5054 0.4894 0.4822 0.0084  0.0805  -0.0172 413  ASP A CB  
2264 C CG  . ASP A 318 ? 0.6113 0.5920 0.5945 0.0067  0.0827  -0.0145 413  ASP A CG  
2265 O OD1 . ASP A 318 ? 0.5705 0.5549 0.5582 0.0105  0.0830  -0.0089 413  ASP A OD1 
2266 O OD2 . ASP A 318 ? 0.6020 0.5760 0.5852 0.0013  0.0840  -0.0181 413  ASP A OD2 
2267 N N   . VAL A 319 ? 0.5815 0.5752 0.5452 -0.0010 0.0704  -0.0277 414  VAL A N   
2268 C CA  . VAL A 319 ? 0.5677 0.5602 0.5203 -0.0028 0.0682  -0.0322 414  VAL A CA  
2269 C C   . VAL A 319 ? 0.6008 0.5811 0.5477 -0.0072 0.0720  -0.0390 414  VAL A C   
2270 O O   . VAL A 319 ? 0.6078 0.5842 0.5599 -0.0115 0.0731  -0.0410 414  VAL A O   
2271 C CB  . VAL A 319 ? 0.5974 0.6013 0.5496 -0.0064 0.0602  -0.0330 414  VAL A CB  
2272 C CG1 . VAL A 319 ? 0.5558 0.5588 0.4947 -0.0072 0.0575  -0.0361 414  VAL A CG1 
2273 C CG2 . VAL A 319 ? 0.5537 0.5695 0.5150 -0.0023 0.0568  -0.0266 414  VAL A CG2 
2274 N N   . GLU A 320 ? 0.5999 0.5736 0.5358 -0.0064 0.0746  -0.0426 415  GLU A N   
2275 C CA  . GLU A 320 ? 0.5977 0.5597 0.5260 -0.0109 0.0780  -0.0504 415  GLU A CA  
2276 C C   . GLU A 320 ? 0.6357 0.5974 0.5495 -0.0120 0.0768  -0.0545 415  GLU A C   
2277 O O   . GLU A 320 ? 0.5885 0.5532 0.4984 -0.0071 0.0777  -0.0509 415  GLU A O   
2278 C CB  . GLU A 320 ? 0.5909 0.5402 0.5225 -0.0074 0.0864  -0.0507 415  GLU A CB  
2279 C CG  . GLU A 320 ? 0.6002 0.5358 0.5283 -0.0125 0.0904  -0.0585 415  GLU A CG  
2280 C CD  . GLU A 320 ? 0.6442 0.5780 0.5816 -0.0172 0.0895  -0.0581 415  GLU A CD  
2281 O OE1 . GLU A 320 ? 0.5988 0.5408 0.5457 -0.0156 0.0870  -0.0515 415  GLU A OE1 
2282 O OE2 . GLU A 320 ? 0.6334 0.5569 0.5682 -0.0228 0.0915  -0.0648 415  GLU A OE2 
2283 N N   . MET A 321 ? 0.6419 0.5999 0.5470 -0.0188 0.0746  -0.0620 416  MET A N   
2284 C CA  . MET A 321 ? 0.6443 0.6031 0.5336 -0.0206 0.0721  -0.0656 416  MET A CA  
2285 C C   . MET A 321 ? 0.6524 0.6024 0.5315 -0.0280 0.0726  -0.0756 416  MET A C   
2286 O O   . MET A 321 ? 0.6512 0.5983 0.5367 -0.0330 0.0718  -0.0793 416  MET A O   
2287 C CB  . MET A 321 ? 0.6220 0.5952 0.5106 -0.0211 0.0625  -0.0611 416  MET A CB  
2288 C CG  . MET A 321 ? 0.6228 0.6029 0.5163 -0.0278 0.0548  -0.0639 416  MET A CG  
2289 S SD  . MET A 321 ? 0.6366 0.6351 0.5355 -0.0267 0.0436  -0.0574 416  MET A SD  
2290 C CE  . MET A 321 ? 0.5874 0.5857 0.4651 -0.0276 0.0393  -0.0592 416  MET A CE  
2291 N N   . THR A 322 ? 0.6557 0.6013 0.5183 -0.0291 0.0740  -0.0802 417  THR A N   
2292 C CA  . THR A 322 ? 0.7118 0.6495 0.5622 -0.0366 0.0739  -0.0904 417  THR A CA  
2293 C C   . THR A 322 ? 0.7131 0.6615 0.5583 -0.0430 0.0624  -0.0919 417  THR A C   
2294 O O   . THR A 322 ? 0.7110 0.6726 0.5602 -0.0408 0.0551  -0.0848 417  THR A O   
2295 C CB  . THR A 322 ? 0.7388 0.6672 0.5720 -0.0357 0.0805  -0.0956 417  THR A CB  
2296 O OG1 . THR A 322 ? 0.7167 0.6536 0.5393 -0.0336 0.0764  -0.0909 417  THR A OG1 
2297 C CG2 . THR A 322 ? 0.7154 0.6336 0.5552 -0.0292 0.0920  -0.0949 417  THR A CG2 
2298 N N   . TYR A 323 ? 0.7523 0.6949 0.5890 -0.0510 0.0608  -0.1014 418  TYR A N   
2299 C CA  . TYR A 323 ? 0.7415 0.6933 0.5701 -0.0577 0.0499  -0.1045 418  TYR A CA  
2300 C C   . TYR A 323 ? 0.7824 0.7238 0.5900 -0.0636 0.0517  -0.1150 418  TYR A C   
2301 O O   . TYR A 323 ? 0.7656 0.6924 0.5683 -0.0631 0.0618  -0.1208 418  TYR A O   
2302 C CB  . TYR A 323 ? 0.7268 0.6857 0.5707 -0.0633 0.0437  -0.1056 418  TYR A CB  
2303 C CG  . TYR A 323 ? 0.7405 0.6866 0.5898 -0.0686 0.0499  -0.1133 418  TYR A CG  
2304 C CD1 . TYR A 323 ? 0.7818 0.7207 0.6198 -0.0775 0.0485  -0.1244 418  TYR A CD1 
2305 C CD2 . TYR A 323 ? 0.7233 0.6640 0.5885 -0.0649 0.0570  -0.1093 418  TYR A CD2 
2306 C CE1 . TYR A 323 ? 0.7562 0.6820 0.5994 -0.0825 0.0545  -0.1317 418  TYR A CE1 
2307 C CE2 . TYR A 323 ? 0.7276 0.6555 0.5976 -0.0695 0.0627  -0.1156 418  TYR A CE2 
2308 C CZ  . TYR A 323 ? 0.7649 0.6849 0.6242 -0.0784 0.0617  -0.1269 418  TYR A CZ  
2309 O OH  . TYR A 323 ? 0.7214 0.6273 0.5859 -0.0831 0.0677  -0.1331 418  TYR A OH  
2310 N N   . LYS A 324 ? 0.7676 0.7167 0.5625 -0.0689 0.0418  -0.1175 419  LYS A N   
2311 C CA  . LYS A 324 ? 0.8360 0.7765 0.6079 -0.0749 0.0424  -0.1274 419  LYS A CA  
2312 C C   . LYS A 324 ? 0.8552 0.7881 0.6280 -0.0841 0.0423  -0.1388 419  LYS A C   
2313 O O   . LYS A 324 ? 0.8682 0.7853 0.6356 -0.0857 0.0521  -0.1469 419  LYS A O   
2314 C CB  . LYS A 324 ? 0.8675 0.8191 0.6239 -0.0768 0.0311  -0.1247 419  LYS A CB  
2315 C CG  . LYS A 324 ? 0.8883 0.8444 0.6406 -0.0683 0.0324  -0.1143 419  LYS A CG  
2316 C CD  . LYS A 324 ? 0.8903 0.8595 0.6330 -0.0692 0.0193  -0.1088 419  LYS A CD  
2317 C CE  . LYS A 324 ? 1.0353 1.0075 0.7749 -0.0609 0.0212  -0.0980 419  LYS A CE  
2318 N NZ  . LYS A 324 ? 1.0975 1.0829 0.8329 -0.0602 0.0081  -0.0905 419  LYS A NZ  
2319 N N   . TYR A 325 ? 0.8495 0.7936 0.6303 -0.0903 0.0315  -0.1397 420  TYR A N   
2320 C CA  . TYR A 325 ? 0.8477 0.7858 0.6299 -0.1002 0.0304  -0.1507 420  TYR A CA  
2321 C C   . TYR A 325 ? 0.8440 0.7907 0.6502 -0.1030 0.0262  -0.1481 420  TYR A C   
2322 O O   . TYR A 325 ? 0.8735 0.8117 0.6852 -0.1100 0.0290  -0.1561 420  TYR A O   
2323 C CB  . TYR A 325 ? 0.8745 0.8164 0.6369 -0.1087 0.0205  -0.1587 420  TYR A CB  
2324 C CG  . TYR A 325 ? 0.9382 0.8701 0.6739 -0.1077 0.0253  -0.1630 420  TYR A CG  
2325 C CD1 . TYR A 325 ? 0.9502 0.8631 0.6759 -0.1097 0.0371  -0.1729 420  TYR A CD1 
2326 C CD2 . TYR A 325 ? 0.9386 0.8797 0.6594 -0.1048 0.0184  -0.1570 420  TYR A CD2 
2327 C CE1 . TYR A 325 ? 1.0130 0.9170 0.7146 -0.1089 0.0425  -0.1772 420  TYR A CE1 
2328 C CE2 . TYR A 325 ? 0.9817 0.9135 0.6773 -0.1044 0.0236  -0.1606 420  TYR A CE2 
2329 C CZ  . TYR A 325 ? 1.0305 0.9442 0.7167 -0.1065 0.0359  -0.1710 420  TYR A CZ  
2330 O OH  . TYR A 325 ? 1.1262 1.0309 0.7876 -0.1062 0.0420  -0.1752 420  TYR A OH  
2331 N N   . ASP A 326 ? 0.8494 0.8118 0.6701 -0.0979 0.0204  -0.1374 421  ASP A N   
2332 C CA  . ASP A 326 ? 0.8382 0.8109 0.6816 -0.1008 0.0163  -0.1349 421  ASP A CA  
2333 C C   . ASP A 326 ? 0.7827 0.7599 0.6424 -0.0912 0.0208  -0.1233 421  ASP A C   
2334 O O   . ASP A 326 ? 0.7915 0.7770 0.6490 -0.0840 0.0179  -0.1152 421  ASP A O   
2335 C CB  . ASP A 326 ? 0.8928 0.8842 0.7378 -0.1059 0.0015  -0.1350 421  ASP A CB  
2336 C CG  . ASP A 326 ? 0.9212 0.9239 0.7897 -0.1107 -0.0026 -0.1344 421  ASP A CG  
2337 O OD1 . ASP A 326 ? 0.9034 0.8993 0.7862 -0.1099 0.0059  -0.1329 421  ASP A OD1 
2338 O OD2 . ASP A 326 ? 0.9554 0.9742 0.8279 -0.1153 -0.0146 -0.1352 421  ASP A OD2 
2339 N N   . TYR A 327 ? 0.7920 0.7633 0.6675 -0.0915 0.0277  -0.1224 422  TYR A N   
2340 C CA  . TYR A 327 ? 0.7607 0.7362 0.6509 -0.0829 0.0319  -0.1118 422  TYR A CA  
2341 C C   . TYR A 327 ? 0.7529 0.7490 0.6553 -0.0811 0.0225  -0.1046 422  TYR A C   
2342 O O   . TYR A 327 ? 0.7058 0.7074 0.6156 -0.0730 0.0242  -0.0955 422  TYR A O   
2343 C CB  . TYR A 327 ? 0.7241 0.6892 0.6276 -0.0843 0.0405  -0.1122 422  TYR A CB  
2344 C CG  . TYR A 327 ? 0.7663 0.7413 0.6870 -0.0910 0.0361  -0.1123 422  TYR A CG  
2345 C CD1 . TYR A 327 ? 0.6990 0.6835 0.6365 -0.0868 0.0369  -0.1036 422  TYR A CD1 
2346 C CD2 . TYR A 327 ? 0.7789 0.7541 0.6990 -0.1019 0.0316  -0.1217 422  TYR A CD2 
2347 C CE1 . TYR A 327 ? 0.7226 0.7167 0.6762 -0.0930 0.0338  -0.1038 422  TYR A CE1 
2348 C CE2 . TYR A 327 ? 0.7726 0.7579 0.7099 -0.1085 0.0281  -0.1220 422  TYR A CE2 
2349 C CZ  . TYR A 327 ? 0.7466 0.7413 0.7007 -0.1039 0.0296  -0.1129 422  TYR A CZ  
2350 O OH  . TYR A 327 ? 0.7315 0.7366 0.7030 -0.1106 0.0270  -0.1132 422  TYR A OH  
2351 N N   . LEU A 328 ? 0.7608 0.7687 0.6660 -0.0885 0.0126  -0.1088 423  LEU A N   
2352 C CA  . LEU A 328 ? 0.7432 0.7715 0.6606 -0.0863 0.0032  -0.1023 423  LEU A CA  
2353 C C   . LEU A 328 ? 0.7370 0.7708 0.6440 -0.0782 -0.0009 -0.0955 423  LEU A C   
2354 O O   . LEU A 328 ? 0.7192 0.7661 0.6374 -0.0727 -0.0051 -0.0876 423  LEU A O   
2355 C CB  . LEU A 328 ? 0.7793 0.8194 0.7011 -0.0959 -0.0074 -0.1088 423  LEU A CB  
2356 C CG  . LEU A 328 ? 0.7891 0.8284 0.7270 -0.1043 -0.0044 -0.1138 423  LEU A CG  
2357 C CD1 . LEU A 328 ? 0.7539 0.8057 0.6956 -0.1145 -0.0155 -0.1211 423  LEU A CD1 
2358 C CD2 . LEU A 328 ? 0.6849 0.7314 0.6437 -0.0999 -0.0001 -0.1059 423  LEU A CD2 
2359 N N   . GLU A 329 ? 0.7530 0.7763 0.6386 -0.0773 0.0008  -0.0984 424  GLU A N   
2360 C CA  . GLU A 329 ? 0.7292 0.7544 0.6044 -0.0692 -0.0003 -0.0912 424  GLU A CA  
2361 C C   . GLU A 329 ? 0.7161 0.7429 0.6047 -0.0603 0.0057  -0.0819 424  GLU A C   
2362 O O   . GLU A 329 ? 0.6875 0.7248 0.5803 -0.0544 0.0009  -0.0741 424  GLU A O   
2363 C CB  . GLU A 329 ? 0.7320 0.7419 0.5844 -0.0691 0.0057  -0.0957 424  GLU A CB  
2364 C CG  . GLU A 329 ? 0.8001 0.8068 0.6340 -0.0775 0.0003  -0.1052 424  GLU A CG  
2365 C CD  . GLU A 329 ? 0.8042 0.7930 0.6185 -0.0777 0.0100  -0.1112 424  GLU A CD  
2366 O OE1 . GLU A 329 ? 0.7969 0.7797 0.6083 -0.0700 0.0179  -0.1058 424  GLU A OE1 
2367 O OE2 . GLU A 329 ? 0.8336 0.8143 0.6359 -0.0855 0.0101  -0.1217 424  GLU A OE2 
2368 N N   . ASN A 330 ? 0.7150 0.7306 0.6098 -0.0590 0.0163  -0.0826 425  ASN A N   
2369 C CA  . ASN A 330 ? 0.6744 0.6907 0.5804 -0.0509 0.0221  -0.0742 425  ASN A CA  
2370 C C   . ASN A 330 ? 0.6768 0.7068 0.6030 -0.0508 0.0181  -0.0698 425  ASN A C   
2371 O O   . ASN A 330 ? 0.6362 0.6733 0.5704 -0.0440 0.0180  -0.0621 425  ASN A O   
2372 C CB  . ASN A 330 ? 0.6554 0.6559 0.5619 -0.0494 0.0338  -0.0759 425  ASN A CB  
2373 C CG  . ASN A 330 ? 0.7152 0.7020 0.6036 -0.0486 0.0394  -0.0803 425  ASN A CG  
2374 O OD1 . ASN A 330 ? 0.7065 0.6795 0.5941 -0.0491 0.0480  -0.0843 425  ASN A OD1 
2375 N ND2 . ASN A 330 ? 0.6536 0.6436 0.5276 -0.0472 0.0351  -0.0796 425  ASN A ND2 
2376 N N   . VAL A 331 ? 0.6647 0.6985 0.5998 -0.0586 0.0153  -0.0750 426  VAL A N   
2377 C CA  . VAL A 331 ? 0.6490 0.6958 0.6043 -0.0589 0.0131  -0.0714 426  VAL A CA  
2378 C C   . VAL A 331 ? 0.6184 0.6819 0.5782 -0.0546 0.0038  -0.0659 426  VAL A C   
2379 O O   . VAL A 331 ? 0.5999 0.6704 0.5708 -0.0484 0.0050  -0.0590 426  VAL A O   
2380 C CB  . VAL A 331 ? 0.7137 0.7627 0.6776 -0.0690 0.0113  -0.0785 426  VAL A CB  
2381 C CG1 . VAL A 331 ? 0.6424 0.7077 0.6275 -0.0700 0.0080  -0.0751 426  VAL A CG1 
2382 C CG2 . VAL A 331 ? 0.6933 0.7245 0.6554 -0.0723 0.0215  -0.0824 426  VAL A CG2 
2383 N N   . HIS A 332 ? 0.6529 0.7216 0.6026 -0.0573 -0.0053 -0.0688 427  HIS A N   
2384 C CA  . HIS A 332 ? 0.6289 0.7122 0.5815 -0.0527 -0.0147 -0.0631 427  HIS A CA  
2385 C C   . HIS A 332 ? 0.6051 0.6845 0.5523 -0.0430 -0.0109 -0.0552 427  HIS A C   
2386 O O   . HIS A 332 ? 0.6135 0.7033 0.5717 -0.0372 -0.0139 -0.0486 427  HIS A O   
2387 C CB  . HIS A 332 ? 0.6622 0.7494 0.6014 -0.0575 -0.0251 -0.0675 427  HIS A CB  
2388 C CG  . HIS A 332 ? 0.7483 0.8415 0.6945 -0.0674 -0.0300 -0.0756 427  HIS A CG  
2389 N ND1 . HIS A 332 ? 0.7494 0.8560 0.7183 -0.0699 -0.0323 -0.0754 427  HIS A ND1 
2390 C CD2 . HIS A 332 ? 0.7740 0.8614 0.7079 -0.0760 -0.0327 -0.0845 427  HIS A CD2 
2391 C CE1 . HIS A 332 ? 0.7512 0.8606 0.7223 -0.0798 -0.0364 -0.0835 427  HIS A CE1 
2392 N NE2 . HIS A 332 ? 0.7633 0.8610 0.7131 -0.0837 -0.0370 -0.0893 427  HIS A NE2 
2393 N N   . PHE A 333 ? 0.6371 0.7013 0.5689 -0.0412 -0.0035 -0.0560 428  PHE A N   
2394 C CA  . PHE A 333 ? 0.5858 0.6460 0.5142 -0.0327 0.0011  -0.0488 428  PHE A CA  
2395 C C   . PHE A 333 ? 0.6137 0.6777 0.5600 -0.0281 0.0062  -0.0438 428  PHE A C   
2396 O O   . PHE A 333 ? 0.6107 0.6823 0.5636 -0.0220 0.0039  -0.0372 428  PHE A O   
2397 C CB  . PHE A 333 ? 0.6261 0.6700 0.5381 -0.0321 0.0094  -0.0513 428  PHE A CB  
2398 C CG  . PHE A 333 ? 0.6155 0.6557 0.5247 -0.0240 0.0145  -0.0444 428  PHE A CG  
2399 C CD1 . PHE A 333 ? 0.5856 0.6293 0.4857 -0.0203 0.0096  -0.0395 428  PHE A CD1 
2400 C CD2 . PHE A 333 ? 0.5832 0.6164 0.4993 -0.0204 0.0238  -0.0426 428  PHE A CD2 
2401 C CE1 . PHE A 333 ? 0.6431 0.6832 0.5415 -0.0135 0.0145  -0.0334 428  PHE A CE1 
2402 C CE2 . PHE A 333 ? 0.6131 0.6439 0.5278 -0.0136 0.0281  -0.0367 428  PHE A CE2 
2403 C CZ  . PHE A 333 ? 0.6248 0.6589 0.5309 -0.0104 0.0237  -0.0323 428  PHE A CZ  
2404 N N   . TYR A 334 ? 0.5916 0.6501 0.5457 -0.0313 0.0130  -0.0468 429  TYR A N   
2405 C CA  . TYR A 334 ? 0.5655 0.6274 0.5349 -0.0274 0.0178  -0.0420 429  TYR A CA  
2406 C C   . TYR A 334 ? 0.5708 0.6496 0.5555 -0.0269 0.0109  -0.0394 429  TYR A C   
2407 O O   . TYR A 334 ? 0.5504 0.6348 0.5439 -0.0210 0.0121  -0.0337 429  TYR A O   
2408 C CB  . TYR A 334 ? 0.5817 0.6349 0.5564 -0.0316 0.0255  -0.0454 429  TYR A CB  
2409 C CG  . TYR A 334 ? 0.6219 0.6581 0.5836 -0.0323 0.0324  -0.0488 429  TYR A CG  
2410 C CD1 . TYR A 334 ? 0.5923 0.6213 0.5439 -0.0261 0.0361  -0.0458 429  TYR A CD1 
2411 C CD2 . TYR A 334 ? 0.6387 0.6662 0.5993 -0.0393 0.0354  -0.0554 429  TYR A CD2 
2412 C CE1 . TYR A 334 ? 0.6251 0.6395 0.5666 -0.0264 0.0429  -0.0493 429  TYR A CE1 
2413 C CE2 . TYR A 334 ? 0.6083 0.6199 0.5580 -0.0395 0.0420  -0.0589 429  TYR A CE2 
2414 C CZ  . TYR A 334 ? 0.6560 0.6616 0.5966 -0.0328 0.0458  -0.0559 429  TYR A CZ  
2415 O OH  . TYR A 334 ? 0.6430 0.6336 0.5744 -0.0326 0.0528  -0.0598 429  TYR A OH  
2416 N N   . ASP A 335 ? 0.5558 0.6433 0.5438 -0.0330 0.0034  -0.0438 430  ASP A N   
2417 C CA  . ASP A 335 ? 0.5847 0.6898 0.5888 -0.0324 -0.0037 -0.0417 430  ASP A CA  
2418 C C   . ASP A 335 ? 0.5990 0.7099 0.6008 -0.0245 -0.0089 -0.0353 430  ASP A C   
2419 O O   . ASP A 335 ? 0.5794 0.6987 0.5943 -0.0193 -0.0086 -0.0306 430  ASP A O   
2420 C CB  . ASP A 335 ? 0.5477 0.6613 0.5545 -0.0405 -0.0119 -0.0479 430  ASP A CB  
2421 C CG  . ASP A 335 ? 0.5929 0.7264 0.6181 -0.0397 -0.0200 -0.0460 430  ASP A CG  
2422 O OD1 . ASP A 335 ? 0.5555 0.6959 0.5970 -0.0369 -0.0159 -0.0429 430  ASP A OD1 
2423 O OD2 . ASP A 335 ? 0.6125 0.7551 0.6358 -0.0421 -0.0305 -0.0479 430  ASP A OD2 
2424 N N   . SER A 336 ? 0.5765 0.6818 0.5608 -0.0235 -0.0129 -0.0351 431  SER A N   
2425 C CA  . SER A 336 ? 0.5842 0.6927 0.5645 -0.0162 -0.0174 -0.0284 431  SER A CA  
2426 C C   . SER A 336 ? 0.5692 0.6727 0.5535 -0.0092 -0.0093 -0.0230 431  SER A C   
2427 O O   . SER A 336 ? 0.5930 0.7040 0.5866 -0.0034 -0.0117 -0.0177 431  SER A O   
2428 C CB  . SER A 336 ? 0.6125 0.7126 0.5705 -0.0169 -0.0206 -0.0290 431  SER A CB  
2429 O OG  . SER A 336 ? 0.7428 0.8477 0.6962 -0.0239 -0.0285 -0.0345 431  SER A OG  
2430 N N   . MET A 337 ? 0.5690 0.6601 0.5477 -0.0099 0.0002  -0.0246 432  MET A N   
2431 C CA  . MET A 337 ? 0.6044 0.6911 0.5868 -0.0039 0.0075  -0.0199 432  MET A CA  
2432 C C   . MET A 337 ? 0.5667 0.6642 0.5680 -0.0015 0.0076  -0.0175 432  MET A C   
2433 O O   . MET A 337 ? 0.5208 0.6219 0.5270 0.0047  0.0073  -0.0125 432  MET A O   
2434 C CB  . MET A 337 ? 0.5569 0.6306 0.5337 -0.0057 0.0168  -0.0225 432  MET A CB  
2435 C CG  . MET A 337 ? 0.5890 0.6579 0.5678 0.0004  0.0235  -0.0178 432  MET A CG  
2436 S SD  . MET A 337 ? 0.5979 0.6520 0.5702 -0.0012 0.0332  -0.0206 432  MET A SD  
2437 C CE  . MET A 337 ? 0.5964 0.6530 0.5818 -0.0062 0.0357  -0.0233 432  MET A CE  
2438 N N   . PHE A 338 ? 0.5384 0.6415 0.5508 -0.0067 0.0081  -0.0212 433  PHE A N   
2439 C CA  . PHE A 338 ? 0.5675 0.6806 0.5974 -0.0046 0.0098  -0.0192 433  PHE A CA  
2440 C C   . PHE A 338 ? 0.5543 0.6813 0.5938 -0.0012 0.0015  -0.0168 433  PHE A C   
2441 O O   . PHE A 338 ? 0.5266 0.6587 0.5753 0.0045  0.0029  -0.0129 433  PHE A O   
2442 C CB  . PHE A 338 ? 0.5404 0.6558 0.5801 -0.0113 0.0134  -0.0234 433  PHE A CB  
2443 C CG  . PHE A 338 ? 0.5711 0.6752 0.6081 -0.0114 0.0232  -0.0227 433  PHE A CG  
2444 C CD1 . PHE A 338 ? 0.5867 0.6931 0.6320 -0.0074 0.0283  -0.0191 433  PHE A CD1 
2445 C CD2 . PHE A 338 ? 0.5569 0.6474 0.5821 -0.0148 0.0271  -0.0255 433  PHE A CD2 
2446 C CE1 . PHE A 338 ? 0.6160 0.7121 0.6578 -0.0071 0.0365  -0.0178 433  PHE A CE1 
2447 C CE2 . PHE A 338 ? 0.5963 0.6762 0.6193 -0.0139 0.0355  -0.0241 433  PHE A CE2 
2448 C CZ  . PHE A 338 ? 0.6078 0.6907 0.6388 -0.0101 0.0397  -0.0200 433  PHE A CZ  
2449 N N   . LYS A 339 ? 0.5329 0.6658 0.5695 -0.0041 -0.0074 -0.0188 434  LYS A N   
2450 C CA  . LYS A 339 ? 0.5585 0.7045 0.6045 0.0001  -0.0162 -0.0157 434  LYS A CA  
2451 C C   . LYS A 339 ? 0.5778 0.7188 0.6174 0.0083  -0.0160 -0.0095 434  LYS A C   
2452 O O   . LYS A 339 ? 0.5563 0.7050 0.6083 0.0140  -0.0172 -0.0059 434  LYS A O   
2453 C CB  . LYS A 339 ? 0.5855 0.7376 0.6268 -0.0043 -0.0266 -0.0185 434  LYS A CB  
2454 C CG  . LYS A 339 ? 0.5875 0.7488 0.6406 -0.0125 -0.0282 -0.0248 434  LYS A CG  
2455 C CD  . LYS A 339 ? 0.5902 0.7627 0.6442 -0.0159 -0.0407 -0.0270 434  LYS A CD  
2456 C CE  . LYS A 339 ? 0.6598 0.8213 0.6902 -0.0190 -0.0443 -0.0288 434  LYS A CE  
2457 N NZ  . LYS A 339 ? 0.6637 0.8364 0.6943 -0.0235 -0.0568 -0.0318 434  LYS A NZ  
2458 N N   . HIS A 340 ? 0.5480 0.6752 0.5693 0.0088  -0.0129 -0.0084 435  HIS A N   
2459 C CA  . HIS A 340 ? 0.5605 0.6820 0.5752 0.0157  -0.0120 -0.0025 435  HIS A CA  
2460 C C   . HIS A 340 ? 0.5553 0.6759 0.5802 0.0201  -0.0044 -0.0004 435  HIS A C   
2461 O O   . HIS A 340 ? 0.5673 0.6916 0.5990 0.0261  -0.0059 0.0038  435  HIS A O   
2462 C CB  . HIS A 340 ? 0.6091 0.7168 0.6028 0.0144  -0.0094 -0.0026 435  HIS A CB  
2463 C CG  . HIS A 340 ? 0.6192 0.7195 0.6055 0.0204  -0.0070 0.0030  435  HIS A CG  
2464 N ND1 . HIS A 340 ? 0.6564 0.7574 0.6361 0.0238  -0.0137 0.0078  435  HIS A ND1 
2465 C CD2 . HIS A 340 ? 0.5719 0.6640 0.5564 0.0232  0.0013  0.0047  435  HIS A CD2 
2466 C CE1 . HIS A 340 ? 0.6306 0.7234 0.6048 0.0281  -0.0090 0.0121  435  HIS A CE1 
2467 N NE2 . HIS A 340 ? 0.6285 0.7165 0.6060 0.0278  -0.0001 0.0100  435  HIS A NE2 
2468 N N   . ILE A 341 ? 0.5343 0.6504 0.5610 0.0170  0.0036  -0.0034 436  ILE A N   
2469 C CA  . ILE A 341 ? 0.5508 0.6669 0.5866 0.0203  0.0104  -0.0018 436  ILE A CA  
2470 C C   . ILE A 341 ? 0.5544 0.6842 0.6082 0.0228  0.0075  -0.0012 436  ILE A C   
2471 O O   . ILE A 341 ? 0.5453 0.6768 0.6049 0.0285  0.0086  0.0019  436  ILE A O   
2472 C CB  . ILE A 341 ? 0.5702 0.6801 0.6052 0.0159  0.0182  -0.0049 436  ILE A CB  
2473 C CG1 . ILE A 341 ? 0.5898 0.6858 0.6090 0.0156  0.0224  -0.0048 436  ILE A CG1 
2474 C CG2 . ILE A 341 ? 0.5618 0.6743 0.6074 0.0182  0.0244  -0.0037 436  ILE A CG2 
2475 C CD1 . ILE A 341 ? 0.5254 0.6140 0.5422 0.0108  0.0286  -0.0081 436  ILE A CD1 
2476 N N   . PHE A 342 ? 0.5394 0.6796 0.6027 0.0184  0.0034  -0.0045 437  PHE A N   
2477 C CA  . PHE A 342 ? 0.5650 0.7193 0.6474 0.0208  0.0014  -0.0044 437  PHE A CA  
2478 C C   . PHE A 342 ? 0.5946 0.7529 0.6793 0.0278  -0.0053 -0.0001 437  PHE A C   
2479 O O   . PHE A 342 ? 0.5529 0.7142 0.6470 0.0335  -0.0029 0.0021  437  PHE A O   
2480 C CB  . PHE A 342 ? 0.5432 0.7090 0.6363 0.0144  -0.0024 -0.0089 437  PHE A CB  
2481 C CG  . PHE A 342 ? 0.5433 0.7042 0.6350 0.0072  0.0047  -0.0129 437  PHE A CG  
2482 C CD1 . PHE A 342 ? 0.5108 0.6629 0.5994 0.0079  0.0143  -0.0120 437  PHE A CD1 
2483 C CD2 . PHE A 342 ? 0.5382 0.7027 0.6313 -0.0004 0.0015  -0.0174 437  PHE A CD2 
2484 C CE1 . PHE A 342 ? 0.5212 0.6678 0.6082 0.0016  0.0205  -0.0148 437  PHE A CE1 
2485 C CE2 . PHE A 342 ? 0.5165 0.6751 0.6083 -0.0071 0.0082  -0.0208 437  PHE A CE2 
2486 C CZ  . PHE A 342 ? 0.5118 0.6611 0.6005 -0.0059 0.0178  -0.0192 437  PHE A CZ  
2487 N N   . THR A 343 ? 0.5588 0.7147 0.6324 0.0277  -0.0130 0.0015  438  THR A N   
2488 C CA  . THR A 343 ? 0.5831 0.7420 0.6579 0.0342  -0.0202 0.0064  438  THR A CA  
2489 C C   . THR A 343 ? 0.6159 0.7652 0.6862 0.0403  -0.0149 0.0106  438  THR A C   
2490 O O   . THR A 343 ? 0.5931 0.7466 0.6733 0.0466  -0.0168 0.0137  438  THR A O   
2491 C CB  . THR A 343 ? 0.6155 0.7712 0.6751 0.0323  -0.0287 0.0077  438  THR A CB  
2492 O OG1 . THR A 343 ? 0.6232 0.7890 0.6880 0.0262  -0.0344 0.0033  438  THR A OG1 
2493 C CG2 . THR A 343 ? 0.5893 0.7468 0.6489 0.0393  -0.0364 0.0141  438  THR A CG2 
2494 N N   . GLU A 344 ? 0.5942 0.7307 0.6507 0.0385  -0.0080 0.0104  439  GLU A N   
2495 C CA  . GLU A 344 ? 0.6124 0.7399 0.6641 0.0437  -0.0040 0.0143  439  GLU A CA  
2496 C C   . GLU A 344 ? 0.6301 0.7606 0.6948 0.0464  0.0027  0.0132  439  GLU A C   
2497 O O   . GLU A 344 ? 0.6192 0.7467 0.6863 0.0517  0.0042  0.0162  439  GLU A O   
2498 C CB  . GLU A 344 ? 0.5679 0.6819 0.6015 0.0413  0.0007  0.0146  439  GLU A CB  
2499 C CG  . GLU A 344 ? 0.6194 0.7285 0.6372 0.0394  -0.0050 0.0160  439  GLU A CG  
2500 C CD  . GLU A 344 ? 0.7223 0.8308 0.7373 0.0446  -0.0113 0.0220  439  GLU A CD  
2501 O OE1 . GLU A 344 ? 0.7736 0.8774 0.7904 0.0494  -0.0081 0.0254  439  GLU A OE1 
2502 O OE2 . GLU A 344 ? 0.7708 0.8835 0.7818 0.0439  -0.0199 0.0232  439  GLU A OE2 
2503 N N   . LEU A 345 ? 0.5986 0.7347 0.6716 0.0424  0.0069  0.0090  440  LEU A N   
2504 C CA  . LEU A 345 ? 0.5817 0.7202 0.6651 0.0447  0.0136  0.0081  440  LEU A CA  
2505 C C   . LEU A 345 ? 0.6179 0.7677 0.7180 0.0495  0.0102  0.0086  440  LEU A C   
2506 O O   . LEU A 345 ? 0.6493 0.7991 0.7562 0.0536  0.0146  0.0087  440  LEU A O   
2507 C CB  . LEU A 345 ? 0.5861 0.7266 0.6726 0.0390  0.0197  0.0041  440  LEU A CB  
2508 C CG  . LEU A 345 ? 0.5396 0.6688 0.6147 0.0362  0.0267  0.0036  440  LEU A CG  
2509 C CD1 . LEU A 345 ? 0.5266 0.6595 0.6074 0.0309  0.0316  0.0003  440  LEU A CD1 
2510 C CD2 . LEU A 345 ? 0.5495 0.6720 0.6212 0.0407  0.0315  0.0057  440  LEU A CD2 
2511 N N   . SER A 346 ? 0.6300 0.7893 0.7369 0.0492  0.0022  0.0086  441  SER A N   
2512 C CA  . SER A 346 ? 0.6361 0.8084 0.7617 0.0536  -0.0018 0.0087  441  SER A CA  
2513 C C   . SER A 346 ? 0.6879 0.8581 0.8129 0.0607  -0.0085 0.0138  441  SER A C   
2514 O O   . SER A 346 ? 0.7526 0.9336 0.8929 0.0650  -0.0137 0.0146  441  SER A O   
2515 C CB  . SER A 346 ? 0.6217 0.8073 0.7571 0.0490  -0.0074 0.0058  441  SER A CB  
2516 O OG  . SER A 346 ? 0.6403 0.8268 0.7759 0.0419  -0.0012 0.0013  441  SER A OG  
2517 N N   . LYS A 347 ? 0.7619 0.9186 0.8703 0.0621  -0.0085 0.0176  442  LYS A N   
2518 C CA  . LYS A 347 ? 0.7777 0.9308 0.8826 0.0678  -0.0156 0.0232  442  LYS A CA  
2519 C C   . LYS A 347 ? 0.8562 0.9971 0.9555 0.0722  -0.0104 0.0261  442  LYS A C   
2520 O O   . LYS A 347 ? 0.8039 0.9356 0.8930 0.0694  -0.0033 0.0249  442  LYS A O   
2521 C CB  . LYS A 347 ? 0.7895 0.9381 0.8777 0.0643  -0.0224 0.0256  442  LYS A CB  
2522 C CG  . LYS A 347 ? 0.8413 0.9739 0.9095 0.0642  -0.0197 0.0291  442  LYS A CG  
2523 C CD  . LYS A 347 ? 0.9063 1.0358 0.9589 0.0617  -0.0272 0.0318  442  LYS A CD  
2524 C CE  . LYS A 347 ? 1.0124 1.1266 1.0458 0.0617  -0.0240 0.0357  442  LYS A CE  
2525 N NZ  . LYS A 347 ? 1.0199 1.1305 1.0355 0.0579  -0.0297 0.0371  442  LYS A NZ  
2526 N N   . GLY A 348 ? 0.9035 1.0445 1.0103 0.0791  -0.0142 0.0300  443  GLY A N   
2527 C CA  . GLY A 348 ? 0.8975 1.0263 0.9992 0.0832  -0.0103 0.0331  443  GLY A CA  
2528 C C   . GLY A 348 ? 0.8485 0.9793 0.9638 0.0864  -0.0031 0.0295  443  GLY A C   
2529 O O   . GLY A 348 ? 0.8726 1.0123 0.9977 0.0841  0.0012  0.0243  443  GLY A O   
2530 N N   . GLY A 349 ? 0.7884 0.9099 0.9033 0.0913  -0.0014 0.0323  444  GLY A N   
2531 C CA  . GLY A 349 ? 0.7085 0.8307 0.8355 0.0947  0.0052  0.0286  444  GLY A CA  
2532 C C   . GLY A 349 ? 0.6265 0.7470 0.7489 0.0896  0.0142  0.0234  444  GLY A C   
2533 O O   . GLY A 349 ? 0.6070 0.7355 0.7404 0.0893  0.0190  0.0184  444  GLY A O   
2534 N N   . LYS A 350 ? 0.6150 0.7253 0.7211 0.0856  0.0166  0.0246  445  LYS A N   
2535 C CA  . LYS A 350 ? 0.6151 0.7227 0.7165 0.0816  0.0246  0.0205  445  LYS A CA  
2536 C C   . LYS A 350 ? 0.5441 0.6615 0.6494 0.0770  0.0268  0.0163  445  LYS A C   
2537 O O   . LYS A 350 ? 0.5552 0.6760 0.6660 0.0762  0.0329  0.0121  445  LYS A O   
2538 C CB  . LYS A 350 ? 0.5849 0.6812 0.6696 0.0783  0.0260  0.0228  445  LYS A CB  
2539 C CG  . LYS A 350 ? 0.6562 0.7501 0.7364 0.0745  0.0333  0.0190  445  LYS A CG  
2540 C CD  . LYS A 350 ? 0.6916 0.7777 0.7569 0.0704  0.0344  0.0208  445  LYS A CD  
2541 N N   . ASN A 351 ? 0.5562 0.6775 0.6577 0.0737  0.0222  0.0173  446  ASN A N   
2542 C CA  . ASN A 351 ? 0.5638 0.6933 0.6687 0.0687  0.0245  0.0135  446  ASN A CA  
2543 C C   . ASN A 351 ? 0.5574 0.6999 0.6806 0.0707  0.0248  0.0105  446  ASN A C   
2544 O O   . ASN A 351 ? 0.4997 0.6475 0.6279 0.0675  0.0305  0.0066  446  ASN A O   
2545 C CB  . ASN A 351 ? 0.5110 0.6412 0.6079 0.0644  0.0194  0.0147  446  ASN A CB  
2546 C CG  . ASN A 351 ? 0.5938 0.7126 0.6735 0.0609  0.0217  0.0158  446  ASN A CG  
2547 O OD1 . ASN A 351 ? 0.5619 0.6737 0.6369 0.0612  0.0274  0.0155  446  ASN A OD1 
2548 N ND2 . ASN A 351 ? 0.5001 0.6172 0.5706 0.0576  0.0176  0.0168  446  ASN A ND2 
2549 N N   . GLU A 352 ? 0.5180 0.6659 0.6515 0.0759  0.0189  0.0125  447  GLU A N   
2550 C CA  . GLU A 352 ? 0.5667 0.7277 0.7199 0.0786  0.0194  0.0096  447  GLU A CA  
2551 C C   . GLU A 352 ? 0.5180 0.6779 0.6768 0.0804  0.0283  0.0058  447  GLU A C   
2552 O O   . GLU A 352 ? 0.5150 0.6841 0.6838 0.0785  0.0334  0.0014  447  GLU A O   
2553 C CB  . GLU A 352 ? 0.5982 0.7634 0.7614 0.0852  0.0111  0.0132  447  GLU A CB  
2554 C CG  . GLU A 352 ? 0.6960 0.8765 0.8819 0.0887  0.0107  0.0102  447  GLU A CG  
2555 C CD  . GLU A 352 ? 0.8319 1.0148 1.0285 0.0970  0.0029  0.0143  447  GLU A CD  
2556 O OE1 . GLU A 352 ? 0.8379 1.0111 1.0229 0.0991  -0.0033 0.0200  447  GLU A OE1 
2557 O OE2 . GLU A 352 ? 0.9050 1.0994 1.1221 0.1015  0.0033  0.0120  447  GLU A OE2 
2558 N N   . MET A 353 ? 0.5249 0.6732 0.6763 0.0835  0.0307  0.0071  448  MET A N   
2559 C CA  . MET A 353 ? 0.5100 0.6564 0.6648 0.0848  0.0389  0.0030  448  MET A CA  
2560 C C   . MET A 353 ? 0.5553 0.7007 0.7013 0.0783  0.0458  -0.0001 448  MET A C   
2561 O O   . MET A 353 ? 0.4822 0.6327 0.6345 0.0776  0.0525  -0.0046 448  MET A O   
2562 C CB  . MET A 353 ? 0.5633 0.6970 0.7117 0.0887  0.0395  0.0049  448  MET A CB  
2563 C CG  . MET A 353 ? 0.6589 0.7901 0.8094 0.0895  0.0478  -0.0002 448  MET A CG  
2564 S SD  . MET A 353 ? 0.9161 1.0361 1.0686 0.0961  0.0480  0.0005  448  MET A SD  
2565 C CE  . MET A 353 ? 0.7426 0.8491 0.8764 0.0933  0.0438  0.0065  448  MET A CE  
2566 N N   . LEU A 354 ? 0.4699 0.6083 0.6010 0.0738  0.0445  0.0023  449  LEU A N   
2567 C CA  . LEU A 354 ? 0.5114 0.6484 0.6343 0.0680  0.0502  0.0001  449  LEU A CA  
2568 C C   . LEU A 354 ? 0.4472 0.5959 0.5797 0.0645  0.0524  -0.0027 449  LEU A C   
2569 O O   . LEU A 354 ? 0.4383 0.5895 0.5719 0.0620  0.0593  -0.0059 449  LEU A O   
2570 C CB  . LEU A 354 ? 0.4646 0.5929 0.5720 0.0643  0.0479  0.0033  449  LEU A CB  
2571 C CG  . LEU A 354 ? 0.5027 0.6193 0.5995 0.0663  0.0474  0.0058  449  LEU A CG  
2572 C CD1 . LEU A 354 ? 0.4769 0.5868 0.5606 0.0628  0.0452  0.0086  449  LEU A CD1 
2573 C CD2 . LEU A 354 ? 0.4471 0.5597 0.5412 0.0664  0.0537  0.0032  449  LEU A CD2 
2574 N N   . ILE A 355 ? 0.4784 0.6344 0.6175 0.0637  0.0466  -0.0017 450  ILE A N   
2575 C CA  . ILE A 355 ? 0.5003 0.6679 0.6494 0.0595  0.0484  -0.0045 450  ILE A CA  
2576 C C   . ILE A 355 ? 0.4886 0.6662 0.6540 0.0625  0.0533  -0.0082 450  ILE A C   
2577 O O   . ILE A 355 ? 0.4303 0.6132 0.5994 0.0586  0.0601  -0.0114 450  ILE A O   
2578 C CB  . ILE A 355 ? 0.5096 0.6836 0.6630 0.0580  0.0402  -0.0030 450  ILE A CB  
2579 C CG1 . ILE A 355 ? 0.4754 0.6399 0.6120 0.0533  0.0378  -0.0009 450  ILE A CG1 
2580 C CG2 . ILE A 355 ? 0.4527 0.6416 0.6220 0.0546  0.0416  -0.0065 450  ILE A CG2 
2581 C CD1 . ILE A 355 ? 0.4988 0.6656 0.6344 0.0530  0.0285  0.0013  450  ILE A CD1 
2582 N N   . LYS A 356 ? 0.4608 0.6406 0.6359 0.0695  0.0502  -0.0078 451  LYS A N   
2583 C CA  . LYS A 356 ? 0.4903 0.6789 0.6817 0.0733  0.0553  -0.0118 451  LYS A CA  
2584 C C   . LYS A 356 ? 0.4901 0.6734 0.6744 0.0715  0.0652  -0.0152 451  LYS A C   
2585 O O   . LYS A 356 ? 0.4777 0.6693 0.6710 0.0701  0.0722  -0.0194 451  LYS A O   
2586 C CB  . LYS A 356 ? 0.5202 0.7078 0.7204 0.0817  0.0508  -0.0103 451  LYS A CB  
2587 C CG  . LYS A 356 ? 0.7034 0.9034 0.9207 0.0852  0.0433  -0.0090 451  LYS A CG  
2588 C CD  . LYS A 356 ? 0.8124 1.0095 1.0378 0.0942  0.0392  -0.0069 451  LYS A CD  
2589 C CE  . LYS A 356 ? 0.8454 1.0469 1.0759 0.0973  0.0274  -0.0018 451  LYS A CE  
2590 N NZ  . LYS A 356 ? 0.8885 1.0846 1.1250 0.1064  0.0231  0.0015  451  LYS A NZ  
2591 N N   . THR A 357 ? 0.4356 0.6053 0.6037 0.0716  0.0658  -0.0135 452  THR A N   
2592 C CA  . THR A 357 ? 0.4971 0.6614 0.6572 0.0701  0.0741  -0.0166 452  THR A CA  
2593 C C   . THR A 357 ? 0.4867 0.6540 0.6413 0.0629  0.0795  -0.0178 452  THR A C   
2594 O O   . THR A 357 ? 0.4525 0.6230 0.6084 0.0614  0.0873  -0.0215 452  THR A O   
2595 C CB  . THR A 357 ? 0.4794 0.6294 0.6240 0.0710  0.0725  -0.0143 452  THR A CB  
2596 O OG1 . THR A 357 ? 0.4692 0.6155 0.6189 0.0772  0.0678  -0.0127 452  THR A OG1 
2597 C CG2 . THR A 357 ? 0.4687 0.6140 0.6054 0.0696  0.0800  -0.0178 452  THR A CG2 
2598 N N   . VAL A 358 ? 0.4939 0.6596 0.6415 0.0583  0.0757  -0.0146 453  VAL A N   
2599 C CA  . VAL A 358 ? 0.4675 0.6357 0.6114 0.0515  0.0807  -0.0153 453  VAL A CA  
2600 C C   . VAL A 358 ? 0.4693 0.6518 0.6303 0.0502  0.0848  -0.0189 453  VAL A C   
2601 O O   . VAL A 358 ? 0.4478 0.6331 0.6082 0.0465  0.0928  -0.0213 453  VAL A O   
2602 C CB  . VAL A 358 ? 0.4834 0.6474 0.6191 0.0471  0.0757  -0.0118 453  VAL A CB  
2603 C CG1 . VAL A 358 ? 0.4110 0.5778 0.5452 0.0400  0.0813  -0.0126 453  VAL A CG1 
2604 C CG2 . VAL A 358 ? 0.4313 0.5817 0.5504 0.0478  0.0730  -0.0085 453  VAL A CG2 
2605 N N   . LYS A 359 ? 0.4541 0.6461 0.6304 0.0531  0.0793  -0.0191 454  LYS A N   
2606 C CA  . LYS A 359 ? 0.4719 0.6794 0.6667 0.0515  0.0820  -0.0223 454  LYS A CA  
2607 C C   . LYS A 359 ? 0.5190 0.7325 0.7242 0.0550  0.0900  -0.0269 454  LYS A C   
2608 O O   . LYS A 359 ? 0.4856 0.7105 0.7028 0.0521  0.0962  -0.0302 454  LYS A O   
2609 C CB  . LYS A 359 ? 0.5251 0.7415 0.7338 0.0544  0.0726  -0.0210 454  LYS A CB  
2610 C CG  . LYS A 359 ? 0.5376 0.7590 0.7475 0.0478  0.0684  -0.0200 454  LYS A CG  
2611 C CD  . LYS A 359 ? 0.5578 0.7651 0.7468 0.0435  0.0663  -0.0167 454  LYS A CD  
2612 C CE  . LYS A 359 ? 0.5587 0.7700 0.7486 0.0365  0.0628  -0.0166 454  LYS A CE  
2613 N NZ  . LYS A 359 ? 0.5627 0.7844 0.7654 0.0383  0.0533  -0.0164 454  LYS A NZ  
2614 N N   . GLY A 360 ? 0.4975 0.7032 0.6981 0.0609  0.0905  -0.0274 455  GLY A N   
2615 C CA  . GLY A 360 ? 0.5146 0.7242 0.7229 0.0640  0.0989  -0.0325 455  GLY A CA  
2616 C C   . GLY A 360 ? 0.5402 0.7490 0.7392 0.0578  0.1092  -0.0352 455  GLY A C   
2617 O O   . GLY A 360 ? 0.5271 0.7447 0.7365 0.0578  0.1173  -0.0400 455  GLY A O   
2618 N N   . GLN A 361 ? 0.5054 0.7036 0.6849 0.0527  0.1091  -0.0320 456  GLN A N   
2619 C CA  . GLN A 361 ? 0.5241 0.7210 0.6934 0.0464  0.1179  -0.0331 456  GLN A CA  
2620 C C   . GLN A 361 ? 0.5245 0.7272 0.6966 0.0392  0.1188  -0.0313 456  GLN A C   
2621 O O   . GLN A 361 ? 0.5429 0.7504 0.7157 0.0344  0.1275  -0.0333 456  GLN A O   
2622 C CB  . GLN A 361 ? 0.5167 0.6986 0.6631 0.0449  0.1176  -0.0305 456  GLN A CB  
2623 C CG  . GLN A 361 ? 0.5020 0.6814 0.6359 0.0388  0.1261  -0.0309 456  GLN A CG  
2624 C CD  . GLN A 361 ? 0.5280 0.6945 0.6413 0.0386  0.1261  -0.0295 456  GLN A CD  
2625 O OE1 . GLN A 361 ? 0.5188 0.6773 0.6261 0.0419  0.1193  -0.0272 456  GLN A OE1 
2626 N NE2 . GLN A 361 ? 0.5313 0.6961 0.6337 0.0346  0.1339  -0.0306 456  GLN A NE2 
2627 N N   . TYR A 362 ? 0.4730 0.6748 0.6459 0.0380  0.1105  -0.0276 457  TYR A N   
2628 C CA  . TYR A 362 ? 0.4866 0.6921 0.6612 0.0307  0.1108  -0.0261 457  TYR A CA  
2629 C C   . TYR A 362 ? 0.5024 0.7197 0.6955 0.0318  0.1038  -0.0267 457  TYR A C   
2630 O O   . TYR A 362 ? 0.4909 0.7041 0.6801 0.0316  0.0953  -0.0237 457  TYR A O   
2631 C CB  . TYR A 362 ? 0.5029 0.6945 0.6582 0.0269  0.1076  -0.0214 457  TYR A CB  
2632 C CG  . TYR A 362 ? 0.5130 0.6932 0.6498 0.0262  0.1128  -0.0201 457  TYR A CG  
2633 C CD1 . TYR A 362 ? 0.5093 0.6780 0.6328 0.0300  0.1083  -0.0178 457  TYR A CD1 
2634 C CD2 . TYR A 362 ? 0.4824 0.6636 0.6149 0.0213  0.1222  -0.0211 457  TYR A CD2 
2635 C CE1 . TYR A 362 ? 0.5128 0.6721 0.6200 0.0292  0.1121  -0.0167 457  TYR A CE1 
2636 C CE2 . TYR A 362 ? 0.5186 0.6896 0.6331 0.0206  0.1262  -0.0197 457  TYR A CE2 
2637 C CZ  . TYR A 362 ? 0.5419 0.7024 0.6442 0.0246  0.1207  -0.0175 457  TYR A CZ  
2638 O OH  . TYR A 362 ? 0.5320 0.6835 0.6173 0.0238  0.1237  -0.0161 457  TYR A OH  
2639 N N   . PRO A 363 ? 0.5017 0.7342 0.7151 0.0328  0.1072  -0.0306 458  PRO A N   
2640 C CA  . PRO A 363 ? 0.5129 0.7580 0.7452 0.0345  0.0995  -0.0311 458  PRO A CA  
2641 C C   . PRO A 363 ? 0.5164 0.7642 0.7492 0.0265  0.0965  -0.0298 458  PRO A C   
2642 O O   . PRO A 363 ? 0.5498 0.7952 0.7765 0.0191  0.1035  -0.0299 458  PRO A O   
2643 C CB  . PRO A 363 ? 0.4911 0.7523 0.7455 0.0370  0.1058  -0.0361 458  PRO A CB  
2644 C CG  . PRO A 363 ? 0.5224 0.7803 0.7684 0.0330  0.1185  -0.0384 458  PRO A CG  
2645 C CD  . PRO A 363 ? 0.4944 0.7334 0.7143 0.0330  0.1181  -0.0350 458  PRO A CD  
2646 N N   . CYS A 364 ? 0.4955 0.7478 0.7354 0.0280  0.0860  -0.0286 459  CYS A N   
2647 C CA  . CYS A 364 ? 0.5143 0.7693 0.7554 0.0208  0.0814  -0.0280 459  CYS A CA  
2648 C C   . CYS A 364 ? 0.5473 0.8095 0.7980 0.0247  0.0691  -0.0272 459  CYS A C   
2649 O O   . CYS A 364 ? 0.5470 0.8031 0.7919 0.0320  0.0631  -0.0248 459  CYS A O   
2650 C CB  . CYS A 364 ? 0.5454 0.7829 0.7630 0.0160  0.0816  -0.0248 459  CYS A CB  
2651 S SG  . CYS A 364 ? 0.5886 0.8271 0.8065 0.0067  0.0765  -0.0249 459  CYS A SG  
2652 N N   . GLU A 365 ? 0.5312 0.8060 0.7957 0.0196  0.0652  -0.0291 460  GLU A N   
2653 C CA  . GLU A 365 ? 0.5344 0.8174 0.8081 0.0226  0.0528  -0.0284 460  GLU A CA  
2654 C C   . GLU A 365 ? 0.5473 0.8146 0.7995 0.0236  0.0450  -0.0245 460  GLU A C   
2655 O O   . GLU A 365 ? 0.5399 0.7938 0.7743 0.0182  0.0479  -0.0235 460  GLU A O   
2656 C CB  . GLU A 365 ? 0.5312 0.8292 0.8210 0.0150  0.0501  -0.0315 460  GLU A CB  
2657 N N   . ASP A 366 ? 0.5470 0.8158 0.8010 0.0306  0.0353  -0.0221 461  ASP A N   
2658 C CA  . ASP A 366 ? 0.5489 0.8035 0.7829 0.0318  0.0280  -0.0183 461  ASP A CA  
2659 C C   . ASP A 366 ? 0.5545 0.8066 0.7802 0.0231  0.0243  -0.0193 461  ASP A C   
2660 O O   . ASP A 366 ? 0.4873 0.7527 0.7270 0.0180  0.0214  -0.0223 461  ASP A O   
2661 C CB  . ASP A 366 ? 0.5619 0.8205 0.8011 0.0399  0.0176  -0.0154 461  ASP A CB  
2662 C CG  . ASP A 366 ? 0.6533 0.9067 0.8929 0.0489  0.0209  -0.0134 461  ASP A CG  
2663 O OD1 . ASP A 366 ? 0.6759 0.9410 0.9343 0.0550  0.0193  -0.0141 461  ASP A OD1 
2664 O OD2 . ASP A 366 ? 0.6827 0.9204 0.9046 0.0499  0.0254  -0.0116 461  ASP A OD2 
2665 N N   . PHE A 367 ? 0.5180 0.7531 0.7217 0.0214  0.0247  -0.0172 462  PHE A N   
2666 C CA  . PHE A 367 ? 0.5058 0.7355 0.6993 0.0136  0.0219  -0.0185 462  PHE A CA  
2667 C C   . PHE A 367 ? 0.5387 0.7766 0.7361 0.0135  0.0096  -0.0186 462  PHE A C   
2668 O O   . PHE A 367 ? 0.5723 0.8098 0.7671 0.0203  0.0025  -0.0154 462  PHE A O   
2669 C CB  . PHE A 367 ? 0.5069 0.7168 0.6767 0.0134  0.0247  -0.0160 462  PHE A CB  
2670 C CG  . PHE A 367 ? 0.4976 0.7002 0.6571 0.0053  0.0244  -0.0179 462  PHE A CG  
2671 C CD1 . PHE A 367 ? 0.4831 0.6827 0.6431 -0.0015 0.0325  -0.0200 462  PHE A CD1 
2672 C CD2 . PHE A 367 ? 0.4955 0.6938 0.6446 0.0042  0.0161  -0.0178 462  PHE A CD2 
2673 C CE1 . PHE A 367 ? 0.5010 0.6929 0.6523 -0.0089 0.0325  -0.0220 462  PHE A CE1 
2674 C CE2 . PHE A 367 ? 0.5233 0.7143 0.6630 -0.0034 0.0162  -0.0205 462  PHE A CE2 
2675 C CZ  . PHE A 367 ? 0.5411 0.7287 0.6826 -0.0099 0.0244  -0.0227 462  PHE A CZ  
2676 N N   . GLN A 368 ? 0.5138 0.7586 0.7167 0.0054  0.0070  -0.0223 463  GLN A N   
2677 C CA  . GLN A 368 ? 0.5313 0.7874 0.7411 0.0040  -0.0049 -0.0235 463  GLN A CA  
2678 C C   . GLN A 368 ? 0.5191 0.7654 0.7121 -0.0033 -0.0087 -0.0254 463  GLN A C   
2679 O O   . GLN A 368 ? 0.5414 0.7814 0.7303 -0.0110 -0.0020 -0.0284 463  GLN A O   
2680 C CB  . GLN A 368 ? 0.5715 0.8484 0.8071 0.0002  -0.0057 -0.0275 463  GLN A CB  
2681 C CG  . GLN A 368 ? 0.6128 0.9057 0.8692 0.0083  -0.0090 -0.0262 463  GLN A CG  
2682 C CD  . GLN A 368 ? 0.7892 1.1042 1.0710 0.0037  -0.0126 -0.0304 463  GLN A CD  
2683 O OE1 . GLN A 368 ? 0.8185 1.1369 1.1060 -0.0054 -0.0068 -0.0346 463  GLN A OE1 
2684 N NE2 . GLN A 368 ? 0.7963 1.1265 1.0939 0.0098  -0.0226 -0.0292 463  GLN A NE2 
2685 N N   . TRP A 369 ? 0.5217 0.7668 0.7053 -0.0013 -0.0194 -0.0238 464  TRP A N   
2686 C CA  . TRP A 369 ? 0.5547 0.7917 0.7226 -0.0083 -0.0237 -0.0265 464  TRP A CA  
2687 C C   . TRP A 369 ? 0.5585 0.8055 0.7276 -0.0075 -0.0377 -0.0262 464  TRP A C   
2688 O O   . TRP A 369 ? 0.5993 0.8557 0.7776 0.0000  -0.0440 -0.0225 464  TRP A O   
2689 C CB  . TRP A 369 ? 0.5662 0.7817 0.7093 -0.0070 -0.0187 -0.0242 464  TRP A CB  
2690 C CG  . TRP A 369 ? 0.5652 0.7742 0.6959 0.0012  -0.0237 -0.0188 464  TRP A CG  
2691 C CD1 . TRP A 369 ? 0.5771 0.7792 0.6905 0.0009  -0.0310 -0.0179 464  TRP A CD1 
2692 C CD2 . TRP A 369 ? 0.5535 0.7614 0.6873 0.0103  -0.0211 -0.0139 464  TRP A CD2 
2693 N NE1 . TRP A 369 ? 0.5648 0.7616 0.6707 0.0092  -0.0329 -0.0121 464  TRP A NE1 
2694 C CE2 . TRP A 369 ? 0.5547 0.7547 0.6733 0.0150  -0.0272 -0.0096 464  TRP A CE2 
2695 C CE3 . TRP A 369 ? 0.5478 0.7602 0.6953 0.0145  -0.0140 -0.0129 464  TRP A CE3 
2696 C CZ2 . TRP A 369 ? 0.5270 0.7231 0.6444 0.0237  -0.0265 -0.0043 464  TRP A CZ2 
2697 C CZ3 . TRP A 369 ? 0.5595 0.7681 0.7056 0.0233  -0.0135 -0.0082 464  TRP A CZ3 
2698 C CH2 . TRP A 369 ? 0.5697 0.7701 0.7013 0.0277  -0.0197 -0.0039 464  TRP A CH2 
2699 N N   . LEU A 370 ? 0.5501 0.7947 0.7098 -0.0155 -0.0427 -0.0303 465  LEU A N   
2700 C CA  . LEU A 370 ? 0.5609 0.8159 0.7210 -0.0167 -0.0566 -0.0312 465  LEU A CA  
2701 C C   . LEU A 370 ? 0.6288 0.8691 0.7621 -0.0154 -0.0615 -0.0289 465  LEU A C   
2702 O O   . LEU A 370 ? 0.6325 0.8547 0.7476 -0.0156 -0.0536 -0.0284 465  LEU A O   
2703 C CB  . LEU A 370 ? 0.5752 0.8399 0.7446 -0.0277 -0.0597 -0.0384 465  LEU A CB  
2704 C CG  . LEU A 370 ? 0.5529 0.8319 0.7483 -0.0316 -0.0539 -0.0417 465  LEU A CG  
2705 C CD1 . LEU A 370 ? 0.5380 0.8224 0.7379 -0.0438 -0.0566 -0.0492 465  LEU A CD1 
2706 C CD2 . LEU A 370 ? 0.5253 0.8247 0.7442 -0.0244 -0.0599 -0.0389 465  LEU A CD2 
2707 N N   . GLU A 371 ? 0.6338 0.8823 0.7647 -0.0141 -0.0747 -0.0276 466  GLU A N   
2708 C CA  . GLU A 371 ? 0.7130 0.9487 0.8176 -0.0139 -0.0799 -0.0258 466  GLU A CA  
2709 C C   . GLU A 371 ? 0.6511 0.8783 0.7409 -0.0244 -0.0791 -0.0330 466  GLU A C   
2710 O O   . GLU A 371 ? 0.6141 0.8251 0.6799 -0.0252 -0.0771 -0.0329 466  GLU A O   
2711 C CB  . GLU A 371 ? 0.7605 1.0071 0.8657 -0.0092 -0.0947 -0.0215 466  GLU A CB  
2712 C CG  . GLU A 371 ? 0.8493 1.0995 0.9645 0.0022  -0.0952 -0.0137 466  GLU A CG  
2713 C CD  . GLU A 371 ? 1.0034 1.2527 1.1059 0.0080  -0.1070 -0.0072 466  GLU A CD  
2714 O OE1 . GLU A 371 ? 1.0459 1.2795 1.1299 0.0127  -0.1033 -0.0021 466  GLU A OE1 
2715 O OE2 . GLU A 371 ? 1.0238 1.2883 1.1351 0.0075  -0.1200 -0.0070 466  GLU A OE2 
2716 N N   . GLU A 372 ? 0.6160 0.8538 0.7202 -0.0327 -0.0801 -0.0395 467  GLU A N   
2717 C CA  . GLU A 372 ? 0.6568 0.8854 0.7505 -0.0433 -0.0767 -0.0472 467  GLU A CA  
2718 C C   . GLU A 372 ? 0.6146 0.8405 0.7214 -0.0471 -0.0639 -0.0500 467  GLU A C   
2719 O O   . GLU A 372 ? 0.5869 0.8283 0.7175 -0.0486 -0.0637 -0.0512 467  GLU A O   
2720 C CB  . GLU A 372 ? 0.6576 0.8996 0.7556 -0.0513 -0.0890 -0.0530 467  GLU A CB  
2721 C CG  . GLU A 372 ? 0.7476 0.9769 0.8278 -0.0617 -0.0877 -0.0610 467  GLU A CG  
2722 C CD  . GLU A 372 ? 0.8842 1.1279 0.9705 -0.0706 -0.0999 -0.0676 467  GLU A CD  
2723 O OE1 . GLU A 372 ? 0.9558 1.1998 1.0494 -0.0806 -0.0963 -0.0752 467  GLU A OE1 
2724 O OE2 . GLU A 372 ? 0.9533 1.2079 1.0373 -0.0678 -0.1134 -0.0651 467  GLU A OE2 
2725 N N   . THR A 373 ? 0.5943 0.8008 0.6858 -0.0484 -0.0533 -0.0509 468  THR A N   
2726 C CA  . THR A 373 ? 0.5962 0.7975 0.6971 -0.0514 -0.0409 -0.0524 468  THR A CA  
2727 C C   . THR A 373 ? 0.5863 0.7906 0.6943 -0.0632 -0.0407 -0.0603 468  THR A C   
2728 O O   . THR A 373 ? 0.5685 0.7643 0.6618 -0.0695 -0.0439 -0.0655 468  THR A O   
2729 C CB  . THR A 373 ? 0.5775 0.7571 0.6598 -0.0486 -0.0305 -0.0504 468  THR A CB  
2730 O OG1 . THR A 373 ? 0.5771 0.7540 0.6525 -0.0384 -0.0310 -0.0434 468  THR A OG1 
2731 C CG2 . THR A 373 ? 0.5358 0.7099 0.6271 -0.0507 -0.0182 -0.0506 468  THR A CG2 
2732 N N   . PRO A 374 ? 0.5655 0.7812 0.6955 -0.0669 -0.0368 -0.0618 469  PRO A N   
2733 C CA  . PRO A 374 ? 0.5251 0.7424 0.6620 -0.0790 -0.0359 -0.0694 469  PRO A CA  
2734 C C   . PRO A 374 ? 0.5693 0.7638 0.6907 -0.0836 -0.0253 -0.0718 469  PRO A C   
2735 O O   . PRO A 374 ? 0.5551 0.7373 0.6706 -0.0783 -0.0155 -0.0673 469  PRO A O   
2736 C CB  . PRO A 374 ? 0.5176 0.7517 0.6819 -0.0806 -0.0321 -0.0690 469  PRO A CB  
2737 C CG  . PRO A 374 ? 0.5195 0.7617 0.6914 -0.0693 -0.0318 -0.0619 469  PRO A CG  
2738 C CD  . PRO A 374 ? 0.5392 0.7703 0.6901 -0.0606 -0.0357 -0.0572 469  PRO A CD  
2739 N N   . ILE A 375 ? 0.5395 0.7284 0.6540 -0.0933 -0.0279 -0.0793 470  ILE A N   
2740 C CA  . ILE A 375 ? 0.5535 0.7206 0.6542 -0.0986 -0.0189 -0.0828 470  ILE A CA  
2741 C C   . ILE A 375 ? 0.6034 0.7743 0.7176 -0.1109 -0.0173 -0.0898 470  ILE A C   
2742 O O   . ILE A 375 ? 0.6016 0.7849 0.7220 -0.1178 -0.0269 -0.0956 470  ILE A O   
2743 C CB  . ILE A 375 ? 0.5865 0.7396 0.6625 -0.0987 -0.0229 -0.0862 470  ILE A CB  
2744 C CG1 . ILE A 375 ? 0.6238 0.7726 0.6860 -0.0871 -0.0240 -0.0792 470  ILE A CG1 
2745 C CG2 . ILE A 375 ? 0.5951 0.7262 0.6594 -0.1046 -0.0134 -0.0908 470  ILE A CG2 
2746 C CD1 . ILE A 375 ? 0.5762 0.7119 0.6133 -0.0872 -0.0274 -0.0823 470  ILE A CD1 
2747 N N   . PHE A 376 ? 0.5987 0.7593 0.7175 -0.1139 -0.0055 -0.0890 471  PHE A N   
2748 C CA  . PHE A 376 ? 0.6018 0.7624 0.7319 -0.1263 -0.0022 -0.0953 471  PHE A CA  
2749 C C   . PHE A 376 ? 0.5847 0.7193 0.6992 -0.1302 0.0070  -0.0978 471  PHE A C   
2750 O O   . PHE A 376 ? 0.5868 0.7064 0.6898 -0.1227 0.0146  -0.0923 471  PHE A O   
2751 C CB  . PHE A 376 ? 0.6007 0.7738 0.7537 -0.1276 0.0042  -0.0919 471  PHE A CB  
2752 C CG  . PHE A 376 ? 0.5891 0.7859 0.7579 -0.1209 -0.0023 -0.0879 471  PHE A CG  
2753 C CD1 . PHE A 376 ? 0.5724 0.7909 0.7573 -0.1257 -0.0128 -0.0923 471  PHE A CD1 
2754 C CD2 . PHE A 376 ? 0.5596 0.7569 0.7281 -0.1097 0.0022  -0.0799 471  PHE A CD2 
2755 C CE1 . PHE A 376 ? 0.5758 0.8161 0.7769 -0.1187 -0.0187 -0.0884 471  PHE A CE1 
2756 C CE2 . PHE A 376 ? 0.5430 0.7609 0.7267 -0.1032 -0.0031 -0.0765 471  PHE A CE2 
2757 C CZ  . PHE A 376 ? 0.5740 0.8133 0.7744 -0.1074 -0.0135 -0.0807 471  PHE A CZ  
2758 N N   . THR A 377 ? 0.6145 0.7436 0.7290 -0.1417 0.0063  -0.1061 472  THR A N   
2759 C CA  . THR A 377 ? 0.6581 0.7625 0.7623 -0.1459 0.0167  -0.1081 472  THR A CA  
2760 C C   . THR A 377 ? 0.6605 0.7630 0.7790 -0.1483 0.0276  -0.1035 472  THR A C   
2761 O O   . THR A 377 ? 0.6224 0.7437 0.7602 -0.1500 0.0269  -0.1015 472  THR A O   
2762 C CB  . THR A 377 ? 0.6777 0.7748 0.7771 -0.1579 0.0133  -0.1189 472  THR A CB  
2763 O OG1 . THR A 377 ? 0.6640 0.7741 0.7841 -0.1689 0.0125  -0.1229 472  THR A OG1 
2764 C CG2 . THR A 377 ? 0.6665 0.7707 0.7539 -0.1570 0.0007  -0.1238 472  THR A CG2 
2765 N N   . TYR A 378 ? 0.6449 0.7243 0.7534 -0.1480 0.0380  -0.1016 473  TYR A N   
2766 C CA  . TYR A 378 ? 0.6664 0.7407 0.7852 -0.1511 0.0488  -0.0970 473  TYR A CA  
2767 C C   . TYR A 378 ? 0.6591 0.7431 0.7959 -0.1647 0.0487  -0.1028 473  TYR A C   
2768 O O   . TYR A 378 ? 0.6383 0.7339 0.7916 -0.1669 0.0532  -0.0991 473  TYR A O   
2769 C CB  . TYR A 378 ? 0.6644 0.7104 0.7684 -0.1495 0.0585  -0.0949 473  TYR A CB  
2770 C CG  . TYR A 378 ? 0.6741 0.7110 0.7838 -0.1502 0.0701  -0.0879 473  TYR A CG  
2771 C CD1 . TYR A 378 ? 0.6607 0.7019 0.7710 -0.1405 0.0739  -0.0785 473  TYR A CD1 
2772 C CD2 . TYR A 378 ? 0.6874 0.7100 0.8004 -0.1606 0.0772  -0.0907 473  TYR A CD2 
2773 C CE1 . TYR A 378 ? 0.6755 0.7080 0.7887 -0.1411 0.0841  -0.0719 473  TYR A CE1 
2774 C CE2 . TYR A 378 ? 0.7026 0.7158 0.8189 -0.1611 0.0877  -0.0834 473  TYR A CE2 
2775 C CZ  . TYR A 378 ? 0.7101 0.7287 0.8260 -0.1513 0.0909  -0.0739 473  TYR A CZ  
2776 O OH  . TYR A 378 ? 0.7303 0.7396 0.8476 -0.1518 0.1010  -0.0664 473  TYR A OH  
2777 N N   . GLU A 379 ? 0.6325 0.7120 0.7664 -0.1742 0.0439  -0.1124 474  GLU A N   
2778 C CA  . GLU A 379 ? 0.6746 0.7641 0.8261 -0.1881 0.0429  -0.1190 474  GLU A CA  
2779 C C   . GLU A 379 ? 0.6589 0.7796 0.8307 -0.1882 0.0349  -0.1186 474  GLU A C   
2780 O O   . GLU A 379 ? 0.6548 0.7875 0.8466 -0.1952 0.0389  -0.1183 474  GLU A O   
2781 C CB  . GLU A 379 ? 0.7017 0.7818 0.8445 -0.1976 0.0374  -0.1301 474  GLU A CB  
2782 C CG  . GLU A 379 ? 0.7615 0.8509 0.9222 -0.2132 0.0358  -0.1381 474  GLU A CG  
2783 C CD  . GLU A 379 ? 0.7973 0.8782 0.9484 -0.2227 0.0294  -0.1500 474  GLU A CD  
2784 O OE1 . GLU A 379 ? 0.8005 0.8789 0.9346 -0.2170 0.0218  -0.1528 474  GLU A OE1 
2785 O OE2 . GLU A 379 ? 0.8885 0.9648 1.0485 -0.2362 0.0321  -0.1569 474  GLU A OE2 
2786 N N   . GLU A 380 ? 0.6541 0.7884 0.8216 -0.1804 0.0239  -0.1184 475  GLU A N   
2787 C CA  . GLU A 380 ? 0.6620 0.8257 0.8489 -0.1785 0.0159  -0.1172 475  GLU A CA  
2788 C C   . GLU A 380 ? 0.6021 0.7737 0.8016 -0.1722 0.0243  -0.1084 475  GLU A C   
2789 O O   . GLU A 380 ? 0.6017 0.7937 0.8239 -0.1763 0.0241  -0.1088 475  GLU A O   
2790 C CB  . GLU A 380 ? 0.6558 0.8288 0.8327 -0.1696 0.0034  -0.1168 475  GLU A CB  
2791 C CG  . GLU A 380 ? 0.7575 0.9301 0.9251 -0.1766 -0.0075 -0.1261 475  GLU A CG  
2792 C CD  . GLU A 380 ? 0.8223 0.9979 0.9738 -0.1668 -0.0177 -0.1242 475  GLU A CD  
2793 O OE1 . GLU A 380 ? 0.8048 0.9830 0.9540 -0.1547 -0.0163 -0.1157 475  GLU A OE1 
2794 O OE2 . GLU A 380 ? 0.9067 1.0817 1.0473 -0.1716 -0.0271 -0.1313 475  GLU A OE2 
2795 N N   . ALA A 381 ? 0.6177 0.7742 0.8031 -0.1621 0.0316  -0.1009 476  ALA A N   
2796 C CA  . ALA A 381 ? 0.6099 0.7724 0.8045 -0.1559 0.0397  -0.0927 476  ALA A CA  
2797 C C   . ALA A 381 ? 0.6338 0.7942 0.8417 -0.1659 0.0505  -0.0928 476  ALA A C   
2798 O O   . ALA A 381 ? 0.6429 0.8205 0.8693 -0.1665 0.0539  -0.0903 476  ALA A O   
2799 C CB  . ALA A 381 ? 0.6032 0.7476 0.7782 -0.1444 0.0451  -0.0854 476  ALA A CB  
2800 N N   . ILE A 382 ? 0.6149 0.7538 0.8136 -0.1738 0.0564  -0.0956 477  ILE A N   
2801 C CA  . ILE A 382 ? 0.6153 0.7501 0.8256 -0.1848 0.0665  -0.0958 477  ILE A CA  
2802 C C   . ILE A 382 ? 0.6644 0.8242 0.8995 -0.1947 0.0619  -0.1019 477  ILE A C   
2803 O O   . ILE A 382 ? 0.6374 0.8090 0.8899 -0.1985 0.0688  -0.0994 477  ILE A O   
2804 C CB  . ILE A 382 ? 0.6572 0.7646 0.8540 -0.1923 0.0716  -0.0993 477  ILE A CB  
2805 C CG1 . ILE A 382 ? 0.7047 0.7881 0.8797 -0.1823 0.0775  -0.0925 477  ILE A CG1 
2806 C CG2 . ILE A 382 ? 0.6291 0.7333 0.8394 -0.2055 0.0810  -0.1004 477  ILE A CG2 
2807 C CD1 . ILE A 382 ? 0.7005 0.7861 0.8771 -0.1745 0.0853  -0.0825 477  ILE A CD1 
2808 N N   . LYS A 383 ? 0.6561 0.8240 0.8932 -0.1997 0.0503  -0.1103 478  LYS A N   
2809 C CA  . LYS A 383 ? 0.6308 0.8233 0.8923 -0.2097 0.0445  -0.1168 478  LYS A CA  
2810 C C   . LYS A 383 ? 0.5977 0.8182 0.8781 -0.2025 0.0413  -0.1128 478  LYS A C   
2811 O O   . LYS A 383 ? 0.5902 0.8299 0.8947 -0.2097 0.0433  -0.1148 478  LYS A O   
2812 C CB  . LYS A 383 ? 0.6210 0.8163 0.8779 -0.2153 0.0314  -0.1263 478  LYS A CB  
2813 C CG  . LYS A 383 ? 0.7150 0.8903 0.9658 -0.2286 0.0356  -0.1334 478  LYS A CG  
2814 C CD  . LYS A 383 ? 0.7470 0.9138 0.9810 -0.2305 0.0251  -0.1414 478  LYS A CD  
2815 C CE  . LYS A 383 ? 0.7839 0.9288 1.0120 -0.2438 0.0307  -0.1488 478  LYS A CE  
2816 N NZ  . LYS A 383 ? 0.9080 1.0450 1.1201 -0.2473 0.0207  -0.1582 478  LYS A NZ  
2817 N N   . MET A 384 ? 0.5710 0.7939 0.8414 -0.1882 0.0369  -0.1072 479  MET A N   
2818 C CA  . MET A 384 ? 0.6140 0.8610 0.9017 -0.1803 0.0351  -0.1030 479  MET A CA  
2819 C C   . MET A 384 ? 0.6168 0.8640 0.9144 -0.1809 0.0496  -0.0975 479  MET A C   
2820 O O   . MET A 384 ? 0.6099 0.8797 0.9315 -0.1830 0.0511  -0.0980 479  MET A O   
2821 C CB  . MET A 384 ? 0.5938 0.8393 0.8666 -0.1651 0.0289  -0.0977 479  MET A CB  
2822 C CG  . MET A 384 ? 0.5957 0.8452 0.8598 -0.1632 0.0138  -0.1022 479  MET A CG  
2823 S SD  . MET A 384 ? 0.7142 0.9537 0.9550 -0.1466 0.0095  -0.0954 479  MET A SD  
2824 C CE  . MET A 384 ? 0.4971 0.7566 0.7563 -0.1360 0.0123  -0.0882 479  MET A CE  
2825 N N   . LEU A 385 ? 0.6195 0.8420 0.8988 -0.1786 0.0603  -0.0922 480  LEU A N   
2826 C CA  . LEU A 385 ? 0.6077 0.8279 0.8924 -0.1790 0.0742  -0.0862 480  LEU A CA  
2827 C C   . LEU A 385 ? 0.6040 0.8301 0.9072 -0.1940 0.0812  -0.0902 480  LEU A C   
2828 O O   . LEU A 385 ? 0.6087 0.8486 0.9286 -0.1959 0.0891  -0.0880 480  LEU A O   
2829 C CB  . LEU A 385 ? 0.5947 0.7862 0.8546 -0.1739 0.0827  -0.0797 480  LEU A CB  
2830 C CG  . LEU A 385 ? 0.6008 0.7874 0.8441 -0.1590 0.0780  -0.0747 480  LEU A CG  
2831 C CD1 . LEU A 385 ? 0.5393 0.6965 0.7574 -0.1557 0.0825  -0.0709 480  LEU A CD1 
2832 C CD2 . LEU A 385 ? 0.5472 0.7475 0.7988 -0.1506 0.0827  -0.0689 480  LEU A CD2 
2833 N N   . ILE A 386 ? 0.6101 0.8259 0.9108 -0.2050 0.0789  -0.0965 481  ILE A N   
2834 C CA  . ILE A 386 ? 0.6200 0.8414 0.9390 -0.2203 0.0849  -0.1010 481  ILE A CA  
2835 C C   . ILE A 386 ? 0.6406 0.8959 0.9887 -0.2240 0.0776  -0.1064 481  ILE A C   
2836 O O   . ILE A 386 ? 0.5875 0.8568 0.9568 -0.2315 0.0854  -0.1068 481  ILE A O   
2837 C CB  . ILE A 386 ? 0.6172 0.8183 0.9260 -0.2312 0.0834  -0.1072 481  ILE A CB  
2838 C CG1 . ILE A 386 ? 0.6349 0.8027 0.9176 -0.2273 0.0920  -0.1013 481  ILE A CG1 
2839 C CG2 . ILE A 386 ? 0.6125 0.8214 0.9425 -0.2482 0.0884  -0.1129 481  ILE A CG2 
2840 C CD1 . ILE A 386 ? 0.6622 0.8071 0.9349 -0.2376 0.0929  -0.1069 481  ILE A CD1 
2841 N N   . GLN A 387 ? 0.6539 0.9232 1.0036 -0.2184 0.0627  -0.1103 482  GLN A N   
2842 C CA  . GLN A 387 ? 0.6385 0.9406 1.0161 -0.2210 0.0539  -0.1152 482  GLN A CA  
2843 C C   . GLN A 387 ? 0.6091 0.9306 1.0036 -0.2130 0.0597  -0.1098 482  GLN A C   
2844 O O   . GLN A 387 ? 0.6408 0.9867 1.0634 -0.2190 0.0610  -0.1130 482  GLN A O   
2845 C CB  . GLN A 387 ? 0.7025 1.0128 1.0743 -0.2152 0.0363  -0.1191 482  GLN A CB  
2846 C CG  . GLN A 387 ? 0.7863 1.1304 1.1835 -0.2112 0.0259  -0.1209 482  GLN A CG  
2847 C CD  . GLN A 387 ? 0.8886 1.2389 1.2772 -0.2053 0.0082  -0.1236 482  GLN A CD  
2848 O OE1 . GLN A 387 ? 0.9715 1.3025 1.3372 -0.2072 0.0034  -0.1263 482  GLN A OE1 
2849 N NE2 . GLN A 387 ? 0.9329 1.3096 1.3395 -0.1979 -0.0014 -0.1228 482  GLN A NE2 
2850 N N   . HIS A 388 ? 0.5553 0.8668 0.9338 -0.1997 0.0637  -0.1021 483  HIS A N   
2851 C CA  . HIS A 388 ? 0.5528 0.8807 0.9456 -0.1921 0.0702  -0.0975 483  HIS A CA  
2852 C C   . HIS A 388 ? 0.5409 0.8608 0.9360 -0.1980 0.0879  -0.0937 483  HIS A C   
2853 O O   . HIS A 388 ? 0.5335 0.8610 0.9338 -0.1909 0.0955  -0.0890 483  HIS A O   
2854 C CB  . HIS A 388 ? 0.5528 0.8748 0.9287 -0.1755 0.0667  -0.0913 483  HIS A CB  
2855 C CG  . HIS A 388 ? 0.5805 0.9182 0.9609 -0.1676 0.0504  -0.0936 483  HIS A CG  
2856 N ND1 . HIS A 388 ? 0.6496 0.9786 1.0153 -0.1683 0.0384  -0.0968 483  HIS A ND1 
2857 C CD2 . HIS A 388 ? 0.5528 0.9136 0.9501 -0.1586 0.0444  -0.0927 483  HIS A CD2 
2858 C CE1 . HIS A 388 ? 0.6092 0.9552 0.9817 -0.1603 0.0254  -0.0974 483  HIS A CE1 
2859 N NE2 . HIS A 388 ? 0.5726 0.9378 0.9646 -0.1540 0.0285  -0.0947 483  HIS A NE2 
2860 N N   . GLY A 389 ? 0.5335 0.8373 0.9238 -0.2108 0.0949  -0.0954 484  GLY A N   
2861 C CA  . GLY A 389 ? 0.5486 0.8427 0.9389 -0.2171 0.1118  -0.0911 484  GLY A CA  
2862 C C   . GLY A 389 ? 0.5809 0.8546 0.9475 -0.2071 0.1207  -0.0819 484  GLY A C   
2863 O O   . GLY A 389 ? 0.5388 0.8127 0.9087 -0.2087 0.1339  -0.0775 484  GLY A O   
2864 N N   . LYS A 390 ? 0.5437 0.8001 0.8864 -0.1971 0.1140  -0.0791 485  LYS A N   
2865 C CA  . LYS A 390 ? 0.5801 0.8164 0.8997 -0.1879 0.1215  -0.0706 485  LYS A CA  
2866 C C   . LYS A 390 ? 0.5805 0.7860 0.8791 -0.1934 0.1277  -0.0677 485  LYS A C   
2867 O O   . LYS A 390 ? 0.6176 0.8053 0.8976 -0.1873 0.1347  -0.0602 485  LYS A O   
2868 C CB  . LYS A 390 ? 0.5499 0.7858 0.8564 -0.1729 0.1114  -0.0686 485  LYS A CB  
2869 C CG  . LYS A 390 ? 0.5668 0.8303 0.8920 -0.1653 0.1054  -0.0702 485  LYS A CG  
2870 C CD  . LYS A 390 ? 0.5509 0.8262 0.8892 -0.1656 0.1175  -0.0674 485  LYS A CD  
2871 C CE  . LYS A 390 ? 0.5861 0.8883 0.9440 -0.1573 0.1124  -0.0691 485  LYS A CE  
2872 N NZ  . LYS A 390 ? 0.6397 0.9542 1.0121 -0.1588 0.1256  -0.0675 485  LYS A NZ  
2873 N N   . LEU A 391 ? 0.5867 0.7855 0.8882 -0.2047 0.1252  -0.0734 486  LEU A N   
2874 C CA  . LEU A 391 ? 0.6039 0.7725 0.8857 -0.2091 0.1290  -0.0717 486  LEU A CA  
2875 C C   . LEU A 391 ? 0.6180 0.7856 0.9129 -0.2257 0.1318  -0.0779 486  LEU A C   
2876 O O   . LEU A 391 ? 0.6425 0.8311 0.9570 -0.2320 0.1243  -0.0858 486  LEU A O   
2877 C CB  . LEU A 391 ? 0.6446 0.8009 0.9080 -0.2008 0.1181  -0.0734 486  LEU A CB  
2878 C CG  . LEU A 391 ? 0.6695 0.7962 0.9142 -0.2048 0.1194  -0.0740 486  LEU A CG  
2879 C CD1 . LEU A 391 ? 0.6465 0.7508 0.8771 -0.2034 0.1319  -0.0650 486  LEU A CD1 
2880 C CD2 . LEU A 391 ? 0.6748 0.7943 0.9031 -0.1949 0.1086  -0.0759 486  LEU A CD2 
2881 N N   . HIS A 392 ? 0.6582 0.8017 0.9428 -0.2329 0.1423  -0.0742 487  HIS A N   
2882 C CA  . HIS A 392 ? 0.6350 0.7738 0.9307 -0.2493 0.1464  -0.0796 487  HIS A CA  
2883 C C   . HIS A 392 ? 0.7503 0.8552 1.0247 -0.2518 0.1488  -0.0784 487  HIS A C   
2884 O O   . HIS A 392 ? 0.7547 0.8381 1.0133 -0.2486 0.1582  -0.0697 487  HIS A O   
2885 C CB  . HIS A 392 ? 0.6336 0.7798 0.9438 -0.2583 0.1600  -0.0760 487  HIS A CB  
2886 C CG  . HIS A 392 ? 0.6172 0.7979 0.9523 -0.2578 0.1583  -0.0788 487  HIS A CG  
2887 N ND1 . HIS A 392 ? 0.6359 0.8387 0.9976 -0.2696 0.1555  -0.0872 487  HIS A ND1 
2888 C CD2 . HIS A 392 ? 0.5581 0.7555 0.8963 -0.2464 0.1585  -0.0748 487  HIS A CD2 
2889 C CE1 . HIS A 392 ? 0.6045 0.8364 0.9854 -0.2651 0.1544  -0.0879 487  HIS A CE1 
2890 N NE2 . HIS A 392 ? 0.6216 0.8502 0.9884 -0.2511 0.1565  -0.0806 487  HIS A NE2 
2891 N N   . LEU A 393 ? 0.8098 0.9103 1.0843 -0.2576 0.1402  -0.0873 488  LEU A N   
2892 C CA  . LEU A 393 ? 0.9127 0.9821 1.1688 -0.2600 0.1412  -0.0884 488  LEU A CA  
2893 C C   . LEU A 393 ? 1.0110 1.0803 1.2790 -0.2758 0.1383  -0.0991 488  LEU A C   
2894 O O   . LEU A 393 ? 0.9943 1.0876 1.2781 -0.2798 0.1286  -0.1075 488  LEU A O   
2895 C CB  . LEU A 393 ? 0.8308 0.8917 1.0677 -0.2469 0.1316  -0.0890 488  LEU A CB  
2896 C CG  . LEU A 393 ? 0.8129 0.8728 1.0358 -0.2303 0.1316  -0.0799 488  LEU A CG  
2897 C CD1 . LEU A 393 ? 0.7712 0.8317 0.9820 -0.2200 0.1196  -0.0835 488  LEU A CD1 
2898 C CD2 . LEU A 393 ? 0.8346 0.8665 1.0406 -0.2273 0.1426  -0.0705 488  LEU A CD2 
2899 N N   . LYS A 394 ? 1.1094 1.1515 1.3697 -0.2845 0.1462  -0.0989 489  LYS A N   
2900 C CA  . LYS A 394 ? 1.1606 1.1971 1.4268 -0.2980 0.1421  -0.1102 489  LYS A CA  
2901 C C   . LYS A 394 ? 1.2489 1.2796 1.5005 -0.2910 0.1299  -0.1170 489  LYS A C   
2902 O O   . LYS A 394 ? 1.2152 1.2395 1.4498 -0.2764 0.1270  -0.1119 489  LYS A O   
2903 C CB  . LYS A 394 ? 1.1680 1.1739 1.4284 -0.3084 0.1541  -0.1080 489  LYS A CB  
2904 C CG  . LYS A 394 ? 1.1310 1.1404 1.4037 -0.3161 0.1672  -0.1006 489  LYS A CG  
2905 C CD  . LYS A 394 ? 1.1350 1.1178 1.4070 -0.3304 0.1775  -0.1011 489  LYS A CD  
2906 C CE  . LYS A 394 ? 1.0663 1.0559 1.3528 -0.3402 0.1903  -0.0949 489  LYS A CE  
2907 N N   . GLU A 395 ? 1.3732 1.4070 1.6316 -0.3021 0.1226  -0.1291 490  GLU A N   
2908 C CA  . GLU A 395 ? 1.4159 1.4411 1.6582 -0.2970 0.1122  -0.1362 490  GLU A CA  
2909 C C   . GLU A 395 ? 1.3939 1.3818 1.6137 -0.2935 0.1192  -0.1335 490  GLU A C   
2910 O O   . GLU A 395 ? 1.3618 1.3398 1.5637 -0.2833 0.1137  -0.1346 490  GLU A O   
2911 C CB  . GLU A 395 ? 1.4494 1.4864 1.7032 -0.3104 0.1026  -0.1502 490  GLU A CB  
2912 C CG  . GLU A 395 ? 1.5192 1.5526 1.7567 -0.3052 0.0904  -0.1582 490  GLU A CG  
2913 C CD  . GLU A 395 ? 1.5286 1.5929 1.7714 -0.2968 0.0770  -0.1592 490  GLU A CD  
2914 O OE1 . GLU A 395 ? 1.5388 1.6313 1.8041 -0.3009 0.0740  -0.1592 490  GLU A OE1 
2915 O OE2 . GLU A 395 ? 1.4841 1.5445 1.7091 -0.2862 0.0696  -0.1598 490  GLU A OE2 
2916 N N   . GLU A 396 ? 1.3641 1.3313 1.5851 -0.3014 0.1316  -0.1295 491  GLU A N   
2917 C CA  . GLU A 396 ? 1.3618 1.2935 1.5630 -0.2966 0.1394  -0.1246 491  GLU A CA  
2918 C C   . GLU A 396 ? 1.3368 1.2647 1.5226 -0.2782 0.1401  -0.1135 491  GLU A C   
2919 O O   . GLU A 396 ? 1.3255 1.2315 1.4931 -0.2697 0.1403  -0.1124 491  GLU A O   
2920 C CB  . GLU A 396 ? 1.3421 1.2552 1.5490 -0.3076 0.1529  -0.1197 491  GLU A CB  
2921 N N   . GLU A 397 ? 1.2858 1.2356 1.4793 -0.2720 0.1406  -0.1057 492  GLU A N   
2922 C CA  . GLU A 397 ? 1.2386 1.1853 1.4192 -0.2559 0.1427  -0.0945 492  GLU A CA  
2923 C C   . GLU A 397 ? 1.1717 1.1348 1.3462 -0.2432 0.1314  -0.0963 492  GLU A C   
2924 O O   . GLU A 397 ? 1.1458 1.1052 1.3085 -0.2297 0.1323  -0.0880 492  GLU A O   
2925 C CB  . GLU A 397 ? 1.2065 1.1661 1.3972 -0.2560 0.1505  -0.0849 492  GLU A CB  
2926 C CG  . GLU A 397 ? 1.1988 1.1410 1.3927 -0.2667 0.1634  -0.0799 492  GLU A CG  
2927 C CD  . GLU A 397 ? 1.1617 1.1221 1.3679 -0.2686 0.1703  -0.0726 492  GLU A CD  
2928 O OE1 . GLU A 397 ? 1.1497 1.1347 1.3763 -0.2776 0.1684  -0.0785 492  GLU A OE1 
2929 O OE2 . GLU A 397 ? 1.1969 1.1479 1.3925 -0.2609 0.1775  -0.0612 492  GLU A OE2 
2930 N N   . ILE A 398 ? 1.2070 1.1886 1.3891 -0.2472 0.1206  -0.1066 493  ILE A N   
2931 C CA  . ILE A 398 ? 1.1505 1.1492 1.3277 -0.2354 0.1100  -0.1072 493  ILE A CA  
2932 C C   . ILE A 398 ? 1.1735 1.1517 1.3284 -0.2255 0.1076  -0.1076 493  ILE A C   
2933 O O   . ILE A 398 ? 1.1189 1.1050 1.2657 -0.2129 0.1022  -0.1041 493  ILE A O   
2934 C CB  . ILE A 398 ? 1.1119 1.1364 1.3031 -0.2423 0.0985  -0.1174 493  ILE A CB  
2935 N N   . LEU A 399 ? 1.2725 1.2243 1.4181 -0.2309 0.1119  -0.1118 494  LEU A N   
2936 C CA  . LEU A 399 ? 1.2315 1.1634 1.3572 -0.2219 0.1106  -0.1128 494  LEU A CA  
2937 C C   . LEU A 399 ? 1.2064 1.1282 1.3216 -0.2079 0.1164  -0.1005 494  LEU A C   
2938 O O   . LEU A 399 ? 1.1548 1.0797 1.2594 -0.1959 0.1117  -0.0985 494  LEU A O   
2939 C CB  . LEU A 399 ? 1.2602 1.1651 1.3801 -0.2312 0.1153  -0.1201 494  LEU A CB  
2940 N N   . ALA A 400 ? 1.1526 1.0628 1.2705 -0.2097 0.1266  -0.0921 495  ALA A N   
2941 C CA  . ALA A 400 ? 1.0859 0.9830 1.1930 -0.1978 0.1325  -0.0804 495  ALA A CA  
2942 C C   . ALA A 400 ? 1.0078 0.9257 1.1199 -0.1903 0.1322  -0.0716 495  ALA A C   
2943 O O   . ALA A 400 ? 0.9611 0.8698 1.0648 -0.1813 0.1371  -0.0615 495  ALA A O   
2944 C CB  . ALA A 400 ? 1.0719 0.9429 1.1771 -0.2033 0.1436  -0.0751 495  ALA A CB  
2945 N N   . TYR A 401 ? 1.0029 0.9482 1.1283 -0.1937 0.1265  -0.0751 496  TYR A N   
2946 C CA  . TYR A 401 ? 0.8821 0.8465 1.0142 -0.1880 0.1277  -0.0673 496  TYR A CA  
2947 C C   . TYR A 401 ? 0.7828 0.7509 0.9034 -0.1726 0.1230  -0.0626 496  TYR A C   
2948 O O   . TYR A 401 ? 0.8045 0.7777 0.9201 -0.1680 0.1145  -0.0681 496  TYR A O   
2949 C CB  . TYR A 401 ? 0.8282 0.8214 0.9794 -0.1952 0.1227  -0.0728 496  TYR A CB  
2950 C CG  . TYR A 401 ? 0.7258 0.7402 0.8835 -0.1874 0.1226  -0.0662 496  TYR A CG  
2951 C CD1 . TYR A 401 ? 0.7230 0.7347 0.8818 -0.1868 0.1324  -0.0572 496  TYR A CD1 
2952 C CD2 . TYR A 401 ? 0.7317 0.7679 0.8935 -0.1805 0.1128  -0.0690 496  TYR A CD2 
2953 C CE1 . TYR A 401 ? 0.7064 0.7368 0.8704 -0.1798 0.1328  -0.0521 496  TYR A CE1 
2954 C CE2 . TYR A 401 ? 0.7079 0.7625 0.8761 -0.1733 0.1130  -0.0635 496  TYR A CE2 
2955 C CZ  . TYR A 401 ? 0.6826 0.7342 0.8518 -0.1730 0.1232  -0.0555 496  TYR A CZ  
2956 O OH  . TYR A 401 ? 0.6868 0.7561 0.8617 -0.1659 0.1238  -0.0509 496  TYR A OH  
2957 N N   . ASP A 402 ? 0.7617 0.7277 0.8780 -0.1652 0.1286  -0.0524 497  ASP A N   
2958 C CA  . ASP A 402 ? 0.7749 0.7427 0.8804 -0.1510 0.1255  -0.0469 497  ASP A CA  
2959 C C   . ASP A 402 ? 0.7339 0.7256 0.8488 -0.1475 0.1246  -0.0431 497  ASP A C   
2960 O O   . ASP A 402 ? 0.7381 0.7301 0.8556 -0.1487 0.1321  -0.0363 497  ASP A O   
2961 C CB  . ASP A 402 ? 0.8204 0.7639 0.9120 -0.1451 0.1324  -0.0385 497  ASP A CB  
2962 C CG  . ASP A 402 ? 0.7942 0.7383 0.8749 -0.1309 0.1294  -0.0330 497  ASP A CG  
2963 O OD1 . ASP A 402 ? 0.7774 0.7401 0.8605 -0.1252 0.1226  -0.0349 497  ASP A OD1 
2964 O OD2 . ASP A 402 ? 0.8957 0.8211 0.9657 -0.1254 0.1338  -0.0263 497  ASP A OD2 
2965 N N   . MET A 403 ? 0.7393 0.7504 0.8586 -0.1430 0.1157  -0.0473 498  MET A N   
2966 C CA  . MET A 403 ? 0.7039 0.7393 0.8353 -0.1407 0.1143  -0.0456 498  MET A CA  
2967 C C   . MET A 403 ? 0.7189 0.7524 0.8426 -0.1309 0.1190  -0.0361 498  MET A C   
2968 O O   . MET A 403 ? 0.7137 0.7381 0.8240 -0.1210 0.1168  -0.0328 498  MET A O   
2969 C CB  . MET A 403 ? 0.6765 0.7301 0.8123 -0.1366 0.1030  -0.0514 498  MET A CB  
2970 C CG  . MET A 403 ? 0.6407 0.7213 0.7949 -0.1380 0.1005  -0.0527 498  MET A CG  
2971 S SD  . MET A 403 ? 0.6670 0.7666 0.8239 -0.1310 0.0867  -0.0575 498  MET A SD  
2972 C CE  . MET A 403 ? 0.6680 0.7677 0.8296 -0.1429 0.0800  -0.0680 498  MET A CE  
2973 N N   . SER A 404 ? 0.6902 0.7336 0.8229 -0.1337 0.1255  -0.0323 499  SER A N   
2974 C CA  . SER A 404 ? 0.6905 0.7331 0.8156 -0.1254 0.1300  -0.0240 499  SER A CA  
2975 C C   . SER A 404 ? 0.6924 0.7532 0.8201 -0.1156 0.1232  -0.0246 499  SER A C   
2976 O O   . SER A 404 ? 0.6799 0.7557 0.8169 -0.1156 0.1154  -0.0308 499  SER A O   
2977 C CB  . SER A 404 ? 0.6961 0.7430 0.8287 -0.1322 0.1399  -0.0200 499  SER A CB  
2978 O OG  . SER A 404 ? 0.6613 0.7334 0.8097 -0.1324 0.1388  -0.0228 499  SER A OG  
2979 N N   . THR A 405 ? 0.6743 0.7333 0.7934 -0.1071 0.1262  -0.0178 500  THR A N   
2980 C CA  . THR A 405 ? 0.6716 0.7457 0.7925 -0.0977 0.1208  -0.0178 500  THR A CA  
2981 C C   . THR A 405 ? 0.6526 0.7502 0.7918 -0.1006 0.1216  -0.0207 500  THR A C   
2982 O O   . THR A 405 ? 0.6291 0.7427 0.7767 -0.0963 0.1143  -0.0245 500  THR A O   
2983 C CB  . THR A 405 ? 0.7460 0.8109 0.8526 -0.0888 0.1241  -0.0103 500  THR A CB  
2984 O OG1 . THR A 405 ? 0.8009 0.8482 0.8932 -0.0839 0.1210  -0.0087 500  THR A OG1 
2985 C CG2 . THR A 405 ? 0.7117 0.7927 0.8217 -0.0803 0.1206  -0.0101 500  THR A CG2 
2986 N N   . ASP A 406 ? 0.6103 0.7102 0.7560 -0.1078 0.1307  -0.0188 501  ASP A N   
2987 C CA  . ASP A 406 ? 0.6435 0.7662 0.8092 -0.1118 0.1323  -0.0225 501  ASP A CA  
2988 C C   . ASP A 406 ? 0.5884 0.7234 0.7695 -0.1178 0.1248  -0.0304 501  ASP A C   
2989 O O   . ASP A 406 ? 0.5810 0.7370 0.7772 -0.1156 0.1197  -0.0343 501  ASP A O   
2990 C CB  . ASP A 406 ? 0.6404 0.7617 0.8100 -0.1202 0.1443  -0.0195 501  ASP A CB  
2991 C CG  . ASP A 406 ? 0.7249 0.8394 0.8812 -0.1143 0.1514  -0.0121 501  ASP A CG  
2992 O OD1 . ASP A 406 ? 0.7050 0.8244 0.8564 -0.1040 0.1473  -0.0110 501  ASP A OD1 
2993 O OD2 . ASP A 406 ? 0.8156 0.9194 0.9660 -0.1203 0.1609  -0.0075 501  ASP A OD2 
2994 N N   . MET A 407 ? 0.5728 0.6949 0.7506 -0.1254 0.1240  -0.0330 502  MET A N   
2995 C CA  . MET A 407 ? 0.5802 0.7136 0.7714 -0.1318 0.1162  -0.0410 502  MET A CA  
2996 C C   . MET A 407 ? 0.5926 0.7339 0.7815 -0.1230 0.1042  -0.0438 502  MET A C   
2997 O O   . MET A 407 ? 0.5485 0.7091 0.7525 -0.1244 0.0969  -0.0491 502  MET A O   
2998 C CB  . MET A 407 ? 0.5795 0.6946 0.7648 -0.1412 0.1176  -0.0436 502  MET A CB  
2999 C CG  . MET A 407 ? 0.6434 0.7712 0.8454 -0.1515 0.1123  -0.0521 502  MET A CG  
3000 S SD  . MET A 407 ? 0.6001 0.7523 0.8285 -0.1602 0.1187  -0.0537 502  MET A SD  
3001 C CE  . MET A 407 ? 0.5686 0.7000 0.7917 -0.1711 0.1329  -0.0496 502  MET A CE  
3002 N N   . GLU A 408 ? 0.5840 0.7113 0.7545 -0.1137 0.1021  -0.0399 503  GLU A N   
3003 C CA  . GLU A 408 ? 0.5517 0.6849 0.7181 -0.1051 0.0917  -0.0417 503  GLU A CA  
3004 C C   . GLU A 408 ? 0.5227 0.6768 0.7010 -0.0984 0.0893  -0.0408 503  GLU A C   
3005 O O   . GLU A 408 ? 0.5318 0.6994 0.7170 -0.0952 0.0798  -0.0441 503  GLU A O   
3006 C CB  . GLU A 408 ? 0.5738 0.6873 0.7189 -0.0971 0.0915  -0.0375 503  GLU A CB  
3007 C CG  . GLU A 408 ? 0.6247 0.7182 0.7589 -0.1026 0.0920  -0.0398 503  GLU A CG  
3008 C CD  . GLU A 408 ? 0.6619 0.7363 0.7769 -0.0946 0.0926  -0.0357 503  GLU A CD  
3009 O OE1 . GLU A 408 ? 0.6811 0.7417 0.7872 -0.0967 0.0906  -0.0389 503  GLU A OE1 
3010 O OE2 . GLU A 408 ? 0.6988 0.7722 0.8080 -0.0864 0.0952  -0.0297 503  GLU A OE2 
3011 N N   . LYS A 409 ? 0.5298 0.6868 0.7108 -0.0963 0.0977  -0.0363 504  LYS A N   
3012 C CA  . LYS A 409 ? 0.5550 0.7327 0.7501 -0.0909 0.0966  -0.0365 504  LYS A CA  
3013 C C   . LYS A 409 ? 0.5367 0.7357 0.7555 -0.0980 0.0941  -0.0423 504  LYS A C   
3014 O O   . LYS A 409 ? 0.5472 0.7646 0.7791 -0.0930 0.0878  -0.0443 504  LYS A O   
3015 C CB  . LYS A 409 ? 0.5098 0.6853 0.7018 -0.0882 0.1071  -0.0314 504  LYS A CB  
3016 C CG  . LYS A 409 ? 0.6306 0.7891 0.8015 -0.0798 0.1082  -0.0258 504  LYS A CG  
3017 C CD  . LYS A 409 ? 0.6850 0.8426 0.8523 -0.0775 0.1179  -0.0211 504  LYS A CD  
3018 C CE  . LYS A 409 ? 0.7041 0.8448 0.8506 -0.0699 0.1185  -0.0155 504  LYS A CE  
3019 N NZ  . LYS A 409 ? 0.7811 0.9216 0.9230 -0.0680 0.1273  -0.0114 504  LYS A NZ  
3020 N N   . GLU A 410 ? 0.5121 0.7094 0.7378 -0.1096 0.0991  -0.0447 505  GLU A N   
3021 C CA  . GLU A 410 ? 0.5472 0.7656 0.7968 -0.1172 0.0963  -0.0507 505  GLU A CA  
3022 C C   . GLU A 410 ? 0.5316 0.7572 0.7844 -0.1167 0.0825  -0.0558 505  GLU A C   
3023 O O   . GLU A 410 ? 0.5130 0.7607 0.7844 -0.1158 0.0756  -0.0593 505  GLU A O   
3024 C CB  . GLU A 410 ? 0.5321 0.7450 0.7871 -0.1305 0.1048  -0.0522 505  GLU A CB  
3025 C CG  . GLU A 410 ? 0.6023 0.8125 0.8579 -0.1327 0.1188  -0.0475 505  GLU A CG  
3026 C CD  . GLU A 410 ? 0.6421 0.8766 0.9179 -0.1301 0.1220  -0.0485 505  GLU A CD  
3027 O OE1 . GLU A 410 ? 0.6754 0.9076 0.9470 -0.1276 0.1322  -0.0440 505  GLU A OE1 
3028 O OE2 . GLU A 410 ? 0.6459 0.9016 0.9416 -0.1304 0.1145  -0.0537 505  GLU A OE2 
3029 N N   . LEU A 411 ? 0.5515 0.7589 0.7861 -0.1171 0.0782  -0.0563 506  LEU A N   
3030 C CA  . LEU A 411 ? 0.5169 0.7290 0.7497 -0.1154 0.0651  -0.0605 506  LEU A CA  
3031 C C   . LEU A 411 ? 0.5596 0.7831 0.7934 -0.1032 0.0579  -0.0580 506  LEU A C   
3032 O O   . LEU A 411 ? 0.5346 0.7749 0.7798 -0.1021 0.0476  -0.0614 506  LEU A O   
3033 C CB  . LEU A 411 ? 0.5149 0.7033 0.7254 -0.1164 0.0635  -0.0610 506  LEU A CB  
3034 C CG  . LEU A 411 ? 0.5336 0.7255 0.7411 -0.1177 0.0509  -0.0666 506  LEU A CG  
3035 C CD1 . LEU A 411 ? 0.5103 0.7164 0.7359 -0.1295 0.0470  -0.0738 506  LEU A CD1 
3036 C CD2 . LEU A 411 ? 0.5317 0.6992 0.7161 -0.1175 0.0512  -0.0669 506  LEU A CD2 
3037 N N   . GLY A 412 ? 0.5600 0.7744 0.7819 -0.0940 0.0628  -0.0521 507  GLY A N   
3038 C CA  . GLY A 412 ? 0.5110 0.7349 0.7341 -0.0826 0.0570  -0.0496 507  GLY A CA  
3039 C C   . GLY A 412 ? 0.5475 0.7967 0.7957 -0.0817 0.0551  -0.0515 507  GLY A C   
3040 O O   . GLY A 412 ? 0.5307 0.7926 0.7858 -0.0759 0.0452  -0.0523 507  GLY A O   
3041 N N   . LYS A 413 ? 0.5256 0.7823 0.7877 -0.0872 0.0647  -0.0521 508  LYS A N   
3042 C CA  . LYS A 413 ? 0.5666 0.8485 0.8550 -0.0870 0.0641  -0.0546 508  LYS A CA  
3043 C C   . LYS A 413 ? 0.5161 0.8142 0.8205 -0.0926 0.0530  -0.0602 508  LYS A C   
3044 O O   . LYS A 413 ? 0.4853 0.8023 0.8052 -0.0872 0.0448  -0.0614 508  LYS A O   
3045 C CB  . LYS A 413 ? 0.5346 0.8202 0.8338 -0.0938 0.0778  -0.0546 508  LYS A CB  
3046 C CG  . LYS A 413 ? 0.5971 0.8727 0.8851 -0.0879 0.0886  -0.0494 508  LYS A CG  
3047 C CD  . LYS A 413 ? 0.6482 0.9349 0.9525 -0.0941 0.1007  -0.0503 508  LYS A CD  
3048 C CE  . LYS A 413 ? 0.7131 0.9806 1.0002 -0.0982 0.1133  -0.0460 508  LYS A CE  
3049 N NZ  . LYS A 413 ? 0.8414 1.0972 1.1104 -0.0878 0.1160  -0.0409 508  LYS A NZ  
3050 N N   . ILE A 414 ? 0.5023 0.7934 0.8037 -0.1037 0.0527  -0.0639 509  ILE A N   
3051 C CA  . ILE A 414 ? 0.5191 0.8246 0.8339 -0.1102 0.0417  -0.0699 509  ILE A CA  
3052 C C   . ILE A 414 ? 0.5594 0.8673 0.8662 -0.1018 0.0273  -0.0695 509  ILE A C   
3053 O O   . ILE A 414 ? 0.5525 0.8812 0.8764 -0.0999 0.0173  -0.0718 509  ILE A O   
3054 C CB  . ILE A 414 ? 0.5109 0.8030 0.8184 -0.1231 0.0440  -0.0739 509  ILE A CB  
3055 C CG1 . ILE A 414 ? 0.5102 0.8032 0.8295 -0.1325 0.0575  -0.0744 509  ILE A CG1 
3056 C CG2 . ILE A 414 ? 0.5401 0.8439 0.8561 -0.1297 0.0308  -0.0806 509  ILE A CG2 
3057 C CD1 . ILE A 414 ? 0.5224 0.7990 0.8336 -0.1451 0.0614  -0.0776 509  ILE A CD1 
3058 N N   . VAL A 415 ? 0.5216 0.8085 0.8024 -0.0965 0.0264  -0.0662 510  VAL A N   
3059 C CA  . VAL A 415 ? 0.5474 0.8336 0.8172 -0.0897 0.0136  -0.0657 510  VAL A CA  
3060 C C   . VAL A 415 ? 0.5457 0.8443 0.8235 -0.0774 0.0097  -0.0614 510  VAL A C   
3061 O O   . VAL A 415 ? 0.5739 0.8826 0.8544 -0.0729 -0.0025 -0.0615 510  VAL A O   
3062 C CB  . VAL A 415 ? 0.5438 0.8038 0.7843 -0.0881 0.0151  -0.0637 510  VAL A CB  
3063 C CG1 . VAL A 415 ? 0.4969 0.7553 0.7244 -0.0797 0.0038  -0.0618 510  VAL A CG1 
3064 C CG2 . VAL A 415 ? 0.5746 0.8235 0.8086 -0.1001 0.0164  -0.0690 510  VAL A CG2 
3065 N N   . LYS A 416 ? 0.5144 0.8115 0.7949 -0.0718 0.0198  -0.0574 511  LYS A N   
3066 C CA  . LYS A 416 ? 0.5408 0.8509 0.8323 -0.0609 0.0170  -0.0544 511  LYS A CA  
3067 C C   . LYS A 416 ? 0.5601 0.8971 0.8805 -0.0625 0.0106  -0.0579 511  LYS A C   
3068 O O   . LYS A 416 ? 0.5617 0.9106 0.8900 -0.0547 0.0006  -0.0566 511  LYS A O   
3069 C CB  . LYS A 416 ? 0.5229 0.8273 0.8133 -0.0562 0.0301  -0.0508 511  LYS A CB  
3070 C CG  . LYS A 416 ? 0.5194 0.8346 0.8200 -0.0447 0.0287  -0.0480 511  LYS A CG  
3071 C CD  . LYS A 416 ? 0.5894 0.8947 0.8730 -0.0353 0.0202  -0.0441 511  LYS A CD  
3072 C CE  . LYS A 416 ? 0.5920 0.9031 0.8826 -0.0236 0.0206  -0.0408 511  LYS A CE  
3073 N NZ  . LYS A 416 ? 0.6222 0.9256 0.9090 -0.0214 0.0338  -0.0392 511  LYS A NZ  
3074 N N   . ALA A 417 ? 0.5174 0.8643 0.8544 -0.0729 0.0161  -0.0624 512  ALA A N   
3075 C CA  . ALA A 417 ? 0.5322 0.9064 0.8994 -0.0749 0.0106  -0.0661 512  ALA A CA  
3076 C C   . ALA A 417 ? 0.5441 0.9270 0.9133 -0.0774 -0.0056 -0.0691 512  ALA A C   
3077 O O   . ALA A 417 ? 0.5854 0.9887 0.9730 -0.0723 -0.0156 -0.0694 512  ALA A O   
3078 C CB  . ALA A 417 ? 0.5282 0.9104 0.9125 -0.0863 0.0214  -0.0702 512  ALA A CB  
3079 N N   . SER A 418 ? 0.5415 0.9095 0.8919 -0.0852 -0.0088 -0.0715 513  SER A N   
3080 C CA  . SER A 418 ? 0.5464 0.9237 0.8992 -0.0898 -0.0237 -0.0756 513  SER A CA  
3081 C C   . SER A 418 ? 0.5481 0.9174 0.8809 -0.0810 -0.0355 -0.0720 513  SER A C   
3082 O O   . SER A 418 ? 0.5448 0.9288 0.8852 -0.0797 -0.0497 -0.0732 513  SER A O   
3083 C CB  . SER A 418 ? 0.5476 0.9143 0.8921 -0.1039 -0.0216 -0.0813 513  SER A CB  
3084 O OG  . SER A 418 ? 0.5574 0.8961 0.8730 -0.1036 -0.0149 -0.0791 513  SER A OG  
3085 N N   . HIS A 419 ? 0.5546 0.9013 0.8621 -0.0751 -0.0304 -0.0674 514  HIS A N   
3086 C CA  . HIS A 419 ? 0.5618 0.8990 0.8486 -0.0675 -0.0400 -0.0639 514  HIS A CA  
3087 C C   . HIS A 419 ? 0.5567 0.8927 0.8419 -0.0539 -0.0387 -0.0569 514  HIS A C   
3088 O O   . HIS A 419 ? 0.5755 0.9046 0.8450 -0.0470 -0.0466 -0.0532 514  HIS A O   
3089 C CB  . HIS A 419 ? 0.5389 0.8501 0.7961 -0.0716 -0.0362 -0.0645 514  HIS A CB  
3090 C CG  . HIS A 419 ? 0.5563 0.8656 0.8102 -0.0841 -0.0399 -0.0717 514  HIS A CG  
3091 N ND1 . HIS A 419 ? 0.5704 0.8862 0.8404 -0.0949 -0.0339 -0.0768 514  HIS A ND1 
3092 C CD2 . HIS A 419 ? 0.5441 0.8450 0.7799 -0.0881 -0.0486 -0.0748 514  HIS A CD2 
3093 C CE1 . HIS A 419 ? 0.5766 0.8880 0.8393 -0.1049 -0.0391 -0.0830 514  HIS A CE1 
3094 N NE2 . HIS A 419 ? 0.5812 0.8837 0.8228 -0.1010 -0.0480 -0.0822 514  HIS A NE2 
3095 N N   . HIS A 420 ? 0.5295 0.8707 0.8291 -0.0502 -0.0283 -0.0552 515  HIS A N   
3096 C CA  . HIS A 420 ? 0.5495 0.8907 0.8504 -0.0376 -0.0265 -0.0495 515  HIS A CA  
3097 C C   . HIS A 420 ? 0.5420 0.8594 0.8140 -0.0320 -0.0241 -0.0449 515  HIS A C   
3098 O O   . HIS A 420 ? 0.5353 0.8503 0.8001 -0.0229 -0.0306 -0.0404 515  HIS A O   
3099 C CB  . HIS A 420 ? 0.5554 0.9160 0.8728 -0.0305 -0.0395 -0.0480 515  HIS A CB  
3100 C CG  . HIS A 420 ? 0.5795 0.9646 0.9251 -0.0366 -0.0443 -0.0530 515  HIS A CG  
3101 N ND1 . HIS A 420 ? 0.5892 0.9894 0.9603 -0.0374 -0.0355 -0.0551 515  HIS A ND1 
3102 C CD2 . HIS A 420 ? 0.5968 0.9943 0.9492 -0.0429 -0.0566 -0.0567 515  HIS A CD2 
3103 C CE1 . HIS A 420 ? 0.5764 0.9980 0.9704 -0.0437 -0.0421 -0.0598 515  HIS A CE1 
3104 N NE2 . HIS A 420 ? 0.5911 1.0116 0.9742 -0.0472 -0.0554 -0.0608 515  HIS A NE2 
3105 N N   . THR A 421 ? 0.5344 0.8341 0.7906 -0.0376 -0.0145 -0.0457 516  THR A N   
3106 C CA  . THR A 421 ? 0.5523 0.8300 0.7828 -0.0329 -0.0111 -0.0418 516  THR A CA  
3107 C C   . THR A 421 ? 0.5208 0.7854 0.7451 -0.0360 0.0031  -0.0415 516  THR A C   
3108 O O   . THR A 421 ? 0.5277 0.7961 0.7619 -0.0442 0.0094  -0.0449 516  THR A O   
3109 C CB  . THR A 421 ? 0.5223 0.7885 0.7323 -0.0368 -0.0187 -0.0432 516  THR A CB  
3110 O OG1 . THR A 421 ? 0.5360 0.7820 0.7230 -0.0320 -0.0147 -0.0394 516  THR A OG1 
3111 C CG2 . THR A 421 ? 0.5262 0.7892 0.7356 -0.0491 -0.0162 -0.0491 516  THR A CG2 
3112 N N   . ASP A 422 ? 0.5062 0.7556 0.7144 -0.0293 0.0080  -0.0371 517  ASP A N   
3113 C CA  . ASP A 422 ? 0.4682 0.7028 0.6662 -0.0313 0.0200  -0.0358 517  ASP A CA  
3114 C C   . ASP A 422 ? 0.5246 0.7390 0.6998 -0.0343 0.0207  -0.0357 517  ASP A C   
3115 O O   . ASP A 422 ? 0.5000 0.7005 0.6648 -0.0349 0.0295  -0.0340 517  ASP A O   
3116 C CB  . ASP A 422 ? 0.5019 0.7332 0.6978 -0.0220 0.0255  -0.0313 517  ASP A CB  
3117 C CG  . ASP A 422 ? 0.5282 0.7772 0.7464 -0.0190 0.0280  -0.0319 517  ASP A CG  
3118 O OD1 . ASP A 422 ? 0.5173 0.7758 0.7498 -0.0257 0.0332  -0.0350 517  ASP A OD1 
3119 O OD2 . ASP A 422 ? 0.5394 0.7925 0.7609 -0.0101 0.0252  -0.0293 517  ASP A OD2 
3120 N N   . TYR A 423 ? 0.5154 0.7280 0.6821 -0.0359 0.0114  -0.0375 518  TYR A N   
3121 C CA  . TYR A 423 ? 0.5066 0.7001 0.6510 -0.0371 0.0118  -0.0375 518  TYR A CA  
3122 C C   . TYR A 423 ? 0.5012 0.6951 0.6434 -0.0460 0.0060  -0.0432 518  TYR A C   
3123 O O   . TYR A 423 ? 0.5146 0.7212 0.6632 -0.0468 -0.0041 -0.0452 518  TYR A O   
3124 C CB  . TYR A 423 ? 0.5239 0.7120 0.6553 -0.0281 0.0069  -0.0333 518  TYR A CB  
3125 C CG  . TYR A 423 ? 0.5356 0.7077 0.6453 -0.0291 0.0051  -0.0340 518  TYR A CG  
3126 C CD1 . TYR A 423 ? 0.5484 0.7035 0.6459 -0.0315 0.0134  -0.0343 518  TYR A CD1 
3127 C CD2 . TYR A 423 ? 0.5163 0.6899 0.6174 -0.0272 -0.0047 -0.0339 518  TYR A CD2 
3128 C CE1 . TYR A 423 ? 0.5540 0.6947 0.6326 -0.0320 0.0126  -0.0353 518  TYR A CE1 
3129 C CE2 . TYR A 423 ? 0.5419 0.7009 0.6225 -0.0281 -0.0054 -0.0348 518  TYR A CE2 
3130 C CZ  . TYR A 423 ? 0.5203 0.6631 0.5904 -0.0305 0.0036  -0.0358 518  TYR A CZ  
3131 O OH  . TYR A 423 ? 0.5346 0.6633 0.5857 -0.0312 0.0037  -0.0372 518  TYR A OH  
3132 N N   . TYR A 424 ? 0.4958 0.6760 0.6294 -0.0529 0.0122  -0.0460 519  TYR A N   
3133 C CA  . TYR A 424 ? 0.5116 0.6900 0.6413 -0.0617 0.0070  -0.0522 519  TYR A CA  
3134 C C   . TYR A 424 ? 0.5077 0.6641 0.6202 -0.0653 0.0139  -0.0536 519  TYR A C   
3135 O O   . TYR A 424 ? 0.4958 0.6400 0.6011 -0.0610 0.0223  -0.0495 519  TYR A O   
3136 C CB  . TYR A 424 ? 0.5086 0.7026 0.6591 -0.0705 0.0058  -0.0568 519  TYR A CB  
3137 C CG  . TYR A 424 ? 0.5150 0.7068 0.6751 -0.0739 0.0175  -0.0557 519  TYR A CG  
3138 C CD1 . TYR A 424 ? 0.5157 0.7192 0.6902 -0.0690 0.0216  -0.0520 519  TYR A CD1 
3139 C CD2 . TYR A 424 ? 0.5244 0.7013 0.6781 -0.0817 0.0248  -0.0582 519  TYR A CD2 
3140 C CE1 . TYR A 424 ? 0.5210 0.7220 0.7022 -0.0722 0.0327  -0.0507 519  TYR A CE1 
3141 C CE2 . TYR A 424 ? 0.5022 0.6758 0.6629 -0.0848 0.0356  -0.0563 519  TYR A CE2 
3142 C CZ  . TYR A 424 ? 0.5189 0.7048 0.6926 -0.0802 0.0396  -0.0524 519  TYR A CZ  
3143 O OH  . TYR A 424 ? 0.5623 0.7448 0.7412 -0.0835 0.0505  -0.0503 519  TYR A OH  
3144 N N   . ILE A 425 ? 0.5389 0.6904 0.6449 -0.0730 0.0101  -0.0598 520  ILE A N   
3145 C CA  . ILE A 425 ? 0.5447 0.6750 0.6333 -0.0761 0.0151  -0.0623 520  ILE A CA  
3146 C C   . ILE A 425 ? 0.5721 0.6992 0.6669 -0.0878 0.0179  -0.0687 520  ILE A C   
3147 O O   . ILE A 425 ? 0.5550 0.6954 0.6604 -0.0946 0.0110  -0.0737 520  ILE A O   
3148 C CB  . ILE A 425 ? 0.5521 0.6766 0.6229 -0.0741 0.0079  -0.0646 520  ILE A CB  
3149 C CG1 . ILE A 425 ? 0.5812 0.7066 0.6446 -0.0629 0.0059  -0.0579 520  ILE A CG1 
3150 C CG2 . ILE A 425 ? 0.5358 0.6393 0.5907 -0.0783 0.0133  -0.0688 520  ILE A CG2 
3151 C CD1 . ILE A 425 ? 0.4877 0.6089 0.5335 -0.0611 -0.0014 -0.0595 520  ILE A CD1 
3152 N N   . ILE A 426 ? 0.5583 0.6674 0.6465 -0.0901 0.0276  -0.0685 521  ILE A N   
3153 C CA  . ILE A 426 ? 0.5366 0.6370 0.6267 -0.1011 0.0311  -0.0745 521  ILE A CA  
3154 C C   . ILE A 426 ? 0.5911 0.6701 0.6616 -0.1015 0.0332  -0.0779 521  ILE A C   
3155 O O   . ILE A 426 ? 0.5737 0.6396 0.6329 -0.0940 0.0386  -0.0733 521  ILE A O   
3156 C CB  . ILE A 426 ? 0.5520 0.6487 0.6527 -0.1041 0.0415  -0.0711 521  ILE A CB  
3157 C CG1 . ILE A 426 ? 0.5591 0.6775 0.6792 -0.1033 0.0403  -0.0682 521  ILE A CG1 
3158 C CG2 . ILE A 426 ? 0.5587 0.6449 0.6612 -0.1158 0.0454  -0.0772 521  ILE A CG2 
3159 C CD1 . ILE A 426 ? 0.5657 0.6833 0.6978 -0.1092 0.0500  -0.0665 521  ILE A CD1 
3160 N N   . ILE A 427 ? 0.6016 0.6776 0.6688 -0.1104 0.0292  -0.0863 522  ILE A N   
3161 C CA  . ILE A 427 ? 0.6028 0.6589 0.6520 -0.1121 0.0312  -0.0913 522  ILE A CA  
3162 C C   . ILE A 427 ? 0.6130 0.6579 0.6659 -0.1234 0.0360  -0.0979 522  ILE A C   
3163 O O   . ILE A 427 ? 0.5985 0.6532 0.6675 -0.1310 0.0361  -0.0993 522  ILE A O   
3164 C CB  . ILE A 427 ? 0.6503 0.7111 0.6873 -0.1119 0.0211  -0.0964 522  ILE A CB  
3165 C CG1 . ILE A 427 ? 0.6035 0.6816 0.6514 -0.1210 0.0114  -0.1026 522  ILE A CG1 
3166 C CG2 . ILE A 427 ? 0.6491 0.7171 0.6800 -0.1005 0.0173  -0.0895 522  ILE A CG2 
3167 C CD1 . ILE A 427 ? 0.7240 0.7991 0.7573 -0.1261 0.0036  -0.1110 522  ILE A CD1 
3168 N N   . ASN A 428 ? 0.6200 0.6435 0.6583 -0.1244 0.0408  -0.1018 523  ASN A N   
3169 C CA  . ASN A 428 ? 0.6549 0.6641 0.6931 -0.1352 0.0450  -0.1095 523  ASN A CA  
3170 C C   . ASN A 428 ? 0.6802 0.6821 0.7303 -0.1385 0.0546  -0.1051 523  ASN A C   
3171 O O   . ASN A 428 ? 0.6802 0.6830 0.7409 -0.1493 0.0556  -0.1097 523  ASN A O   
3172 C CB  . ASN A 428 ? 0.6786 0.7000 0.7217 -0.1461 0.0357  -0.1189 523  ASN A CB  
3173 C CG  . ASN A 428 ? 0.6920 0.7151 0.7189 -0.1446 0.0270  -0.1245 523  ASN A CG  
3174 O OD1 . ASN A 428 ? 0.7154 0.7271 0.7263 -0.1367 0.0294  -0.1227 523  ASN A OD1 
3175 N ND2 . ASN A 428 ? 0.7464 0.7836 0.7771 -0.1526 0.0169  -0.1315 523  ASN A ND2 
3176 N N   . PHE A 429 ? 0.6724 0.6663 0.7199 -0.1294 0.0617  -0.0962 524  PHE A N   
3177 C CA  . PHE A 429 ? 0.6793 0.6625 0.7339 -0.1317 0.0714  -0.0913 524  PHE A CA  
3178 C C   . PHE A 429 ? 0.7170 0.6762 0.7649 -0.1383 0.0773  -0.0971 524  PHE A C   
3179 O O   . PHE A 429 ? 0.7061 0.6532 0.7407 -0.1365 0.0764  -0.1024 524  PHE A O   
3180 C CB  . PHE A 429 ? 0.6856 0.6641 0.7362 -0.1200 0.0768  -0.0808 524  PHE A CB  
3181 C CG  . PHE A 429 ? 0.6630 0.6628 0.7220 -0.1140 0.0731  -0.0745 524  PHE A CG  
3182 C CD1 . PHE A 429 ? 0.6270 0.6376 0.6803 -0.1062 0.0661  -0.0739 524  PHE A CD1 
3183 C CD2 . PHE A 429 ? 0.6110 0.6193 0.6830 -0.1163 0.0772  -0.0694 524  PHE A CD2 
3184 C CE1 . PHE A 429 ? 0.6155 0.6442 0.6767 -0.1006 0.0630  -0.0684 524  PHE A CE1 
3185 C CE2 . PHE A 429 ? 0.6374 0.6646 0.7171 -0.1107 0.0744  -0.0644 524  PHE A CE2 
3186 C CZ  . PHE A 429 ? 0.6043 0.6414 0.6790 -0.1026 0.0672  -0.0639 524  PHE A CZ  
3187 N N   . PRO A 430 ? 0.6825 0.6338 0.7394 -0.1460 0.0841  -0.0961 525  PRO A N   
3188 C CA  . PRO A 430 ? 0.7310 0.6569 0.7818 -0.1514 0.0907  -0.1006 525  PRO A CA  
3189 C C   . PRO A 430 ? 0.7625 0.6689 0.8003 -0.1406 0.0965  -0.0955 525  PRO A C   
3190 O O   . PRO A 430 ? 0.6882 0.5970 0.7257 -0.1311 0.0990  -0.0857 525  PRO A O   
3191 C CB  . PRO A 430 ? 0.7191 0.6423 0.7830 -0.1601 0.0974  -0.0974 525  PRO A CB  
3192 C CG  . PRO A 430 ? 0.7754 0.7196 0.8498 -0.1563 0.0962  -0.0894 525  PRO A CG  
3193 C CD  . PRO A 430 ? 0.7282 0.6932 0.8014 -0.1507 0.0861  -0.0915 525  PRO A CD  
3194 N N   . SER A 431 ? 0.7520 0.6397 0.7794 -0.1421 0.0983  -0.1029 526  SER A N   
3195 C CA  . SER A 431 ? 0.7459 0.6153 0.7619 -0.1319 0.1035  -0.0997 526  SER A CA  
3196 C C   . SER A 431 ? 0.7758 0.6315 0.7953 -0.1279 0.1121  -0.0895 526  SER A C   
3197 O O   . SER A 431 ? 0.7417 0.5927 0.7560 -0.1165 0.1146  -0.0821 526  SER A O   
3198 C CB  . SER A 431 ? 0.7618 0.6123 0.7681 -0.1360 0.1053  -0.1105 526  SER A CB  
3199 O OG  . SER A 431 ? 0.7633 0.6261 0.7656 -0.1416 0.0971  -0.1202 526  SER A OG  
3200 N N   . ALA A 432 ? 0.7523 0.6012 0.7803 -0.1373 0.1166  -0.0889 527  ALA A N   
3201 C CA  . ALA A 432 ? 0.7591 0.5932 0.7891 -0.1344 0.1248  -0.0790 527  ALA A CA  
3202 C C   . ALA A 432 ? 0.7282 0.5769 0.7612 -0.1262 0.1243  -0.0674 527  ALA A C   
3203 O O   . ALA A 432 ? 0.7342 0.5712 0.7656 -0.1208 0.1301  -0.0581 527  ALA A O   
3204 C CB  . ALA A 432 ? 0.7556 0.5809 0.7943 -0.1474 0.1297  -0.0807 527  ALA A CB  
3205 N N   . LEU A 433 ? 0.7003 0.5738 0.7374 -0.1250 0.1174  -0.0679 528  LEU A N   
3206 C CA  . LEU A 433 ? 0.6927 0.5808 0.7330 -0.1178 0.1169  -0.0581 528  LEU A CA  
3207 C C   . LEU A 433 ? 0.7120 0.6063 0.7442 -0.1052 0.1129  -0.0553 528  LEU A C   
3208 O O   . LEU A 433 ? 0.6786 0.5853 0.7129 -0.0990 0.1120  -0.0479 528  LEU A O   
3209 C CB  . LEU A 433 ? 0.6934 0.6054 0.7459 -0.1245 0.1129  -0.0595 528  LEU A CB  
3210 C CG  . LEU A 433 ? 0.7926 0.7049 0.8566 -0.1374 0.1168  -0.0613 528  LEU A CG  
3211 C CD1 . LEU A 433 ? 0.8017 0.7410 0.8785 -0.1406 0.1125  -0.0614 528  LEU A CD1 
3212 C CD2 . LEU A 433 ? 0.7207 0.6156 0.7838 -0.1380 0.1264  -0.0526 528  LEU A CD2 
3213 N N   . ARG A 434 ? 0.6765 0.5622 0.6996 -0.1016 0.1111  -0.0610 529  ARG A N   
3214 C CA  . ARG A 434 ? 0.6679 0.5601 0.6837 -0.0907 0.1074  -0.0593 529  ARG A CA  
3215 C C   . ARG A 434 ? 0.6916 0.5636 0.6990 -0.0828 0.1126  -0.0569 529  ARG A C   
3216 O O   . ARG A 434 ? 0.6974 0.5498 0.7038 -0.0863 0.1180  -0.0589 529  ARG A O   
3217 C CB  . ARG A 434 ? 0.6638 0.5669 0.6759 -0.0933 0.1000  -0.0686 529  ARG A CB  
3218 C CG  . ARG A 434 ? 0.6737 0.5974 0.6953 -0.1011 0.0939  -0.0716 529  ARG A CG  
3219 C CD  . ARG A 434 ? 0.6349 0.5775 0.6635 -0.0957 0.0915  -0.0635 529  ARG A CD  
3220 N NE  . ARG A 434 ? 0.6693 0.6227 0.6920 -0.0872 0.0858  -0.0627 529  ARG A NE  
3221 C CZ  . ARG A 434 ? 0.6903 0.6618 0.7181 -0.0827 0.0817  -0.0581 529  ARG A CZ  
3222 N NH1 . ARG A 434 ? 0.6563 0.6389 0.6958 -0.0857 0.0828  -0.0543 529  ARG A NH1 
3223 N NH2 . ARG A 434 ? 0.6341 0.6125 0.6554 -0.0753 0.0770  -0.0575 529  ARG A NH2 
3224 N N   . PRO A 435 ? 0.6591 0.5353 0.6614 -0.0721 0.1111  -0.0528 530  PRO A N   
3225 C CA  . PRO A 435 ? 0.6974 0.5563 0.6942 -0.0638 0.1161  -0.0496 530  PRO A CA  
3226 C C   . PRO A 435 ? 0.6840 0.5275 0.6744 -0.0655 0.1183  -0.0590 530  PRO A C   
3227 O O   . PRO A 435 ? 0.6989 0.5462 0.6864 -0.0722 0.1150  -0.0684 530  PRO A O   
3228 C CB  . PRO A 435 ? 0.6814 0.5527 0.6755 -0.0533 0.1129  -0.0444 530  PRO A CB  
3229 C CG  . PRO A 435 ? 0.7015 0.5939 0.7012 -0.0557 0.1079  -0.0417 530  PRO A CG  
3230 C CD  . PRO A 435 ? 0.6400 0.5370 0.6430 -0.0668 0.1053  -0.0496 530  PRO A CD  
3231 N N   . PHE A 436 ? 0.6901 0.5157 0.6780 -0.0591 0.1239  -0.0565 531  PHE A N   
3232 C CA  . PHE A 436 ? 0.7392 0.5468 0.7219 -0.0604 0.1279  -0.0653 531  PHE A CA  
3233 C C   . PHE A 436 ? 0.7209 0.5357 0.6954 -0.0587 0.1246  -0.0736 531  PHE A C   
3234 O O   . PHE A 436 ? 0.6880 0.4924 0.6571 -0.0635 0.1263  -0.0838 531  PHE A O   
3235 C CB  . PHE A 436 ? 0.7433 0.5321 0.7265 -0.0519 0.1343  -0.0599 531  PHE A CB  
3236 C CG  . PHE A 436 ? 0.7373 0.5325 0.7184 -0.0398 0.1336  -0.0553 531  PHE A CG  
3237 C CD1 . PHE A 436 ? 0.7278 0.5340 0.7126 -0.0333 0.1314  -0.0444 531  PHE A CD1 
3238 C CD2 . PHE A 436 ? 0.7317 0.5225 0.7072 -0.0354 0.1353  -0.0624 531  PHE A CD2 
3239 C CE1 . PHE A 436 ? 0.7245 0.5372 0.7083 -0.0228 0.1306  -0.0407 531  PHE A CE1 
3240 C CE2 . PHE A 436 ? 0.7087 0.5062 0.6834 -0.0249 0.1351  -0.0584 531  PHE A CE2 
3241 C CZ  . PHE A 436 ? 0.7048 0.5133 0.6841 -0.0187 0.1325  -0.0476 531  PHE A CZ  
3242 N N   . TYR A 437 ? 0.6729 0.5043 0.6457 -0.0521 0.1203  -0.0696 532  TYR A N   
3243 C CA  . TYR A 437 ? 0.7206 0.5578 0.6846 -0.0499 0.1179  -0.0763 532  TYR A CA  
3244 C C   . TYR A 437 ? 0.7168 0.5679 0.6775 -0.0586 0.1109  -0.0830 532  TYR A C   
3245 O O   . TYR A 437 ? 0.6680 0.5247 0.6198 -0.0577 0.1080  -0.0884 532  TYR A O   
3246 C CB  . TYR A 437 ? 0.6520 0.5000 0.6156 -0.0392 0.1166  -0.0690 532  TYR A CB  
3247 C CG  . TYR A 437 ? 0.6682 0.5325 0.6386 -0.0377 0.1122  -0.0598 532  TYR A CG  
3248 C CD1 . TYR A 437 ? 0.6741 0.5365 0.6503 -0.0312 0.1146  -0.0500 532  TYR A CD1 
3249 C CD2 . TYR A 437 ? 0.6720 0.5535 0.6428 -0.0427 0.1054  -0.0612 532  TYR A CD2 
3250 C CE1 . TYR A 437 ? 0.6583 0.5353 0.6398 -0.0302 0.1110  -0.0424 532  TYR A CE1 
3251 C CE2 . TYR A 437 ? 0.6724 0.5685 0.6499 -0.0411 0.1020  -0.0536 532  TYR A CE2 
3252 C CZ  . TYR A 437 ? 0.6598 0.5533 0.6421 -0.0351 0.1051  -0.0445 532  TYR A CZ  
3253 O OH  . TYR A 437 ? 0.7486 0.6563 0.7365 -0.0339 0.1022  -0.0377 532  TYR A OH  
3254 N N   . THR A 438 ? 0.7273 0.5841 0.6950 -0.0669 0.1081  -0.0827 533  THR A N   
3255 C CA  . THR A 438 ? 0.6966 0.5680 0.6637 -0.0752 0.1007  -0.0886 533  THR A CA  
3256 C C   . THR A 438 ? 0.7171 0.5777 0.6772 -0.0839 0.1010  -0.1009 533  THR A C   
3257 O O   . THR A 438 ? 0.7453 0.5899 0.7081 -0.0894 0.1060  -0.1044 533  THR A O   
3258 C CB  . THR A 438 ? 0.6846 0.5661 0.6638 -0.0811 0.0986  -0.0841 533  THR A CB  
3259 O OG1 . THR A 438 ? 0.6718 0.5640 0.6563 -0.0733 0.0981  -0.0735 533  THR A OG1 
3260 C CG2 . THR A 438 ? 0.6613 0.5589 0.6424 -0.0898 0.0905  -0.0904 533  THR A CG2 
3261 N N   . MET A 439 ? 0.7292 0.5981 0.6797 -0.0856 0.0954  -0.1075 534  MET A N   
3262 C CA  . MET A 439 ? 0.7303 0.5910 0.6727 -0.0946 0.0945  -0.1199 534  MET A CA  
3263 C C   . MET A 439 ? 0.7683 0.6369 0.7192 -0.1064 0.0894  -0.1236 534  MET A C   
3264 O O   . MET A 439 ? 0.7391 0.6275 0.6973 -0.1076 0.0825  -0.1193 534  MET A O   
3265 C CB  . MET A 439 ? 0.7251 0.5932 0.6533 -0.0930 0.0896  -0.1252 534  MET A CB  
3266 C CG  . MET A 439 ? 0.7648 0.6236 0.6818 -0.1023 0.0888  -0.1388 534  MET A CG  
3267 S SD  . MET A 439 ? 0.8198 0.6487 0.7336 -0.1025 0.1008  -0.1456 534  MET A SD  
3268 C CE  . MET A 439 ? 0.9067 0.7293 0.8076 -0.1153 0.0976  -0.1622 534  MET A CE  
3269 N N   . TYR A 440 ? 0.7686 0.6217 0.7195 -0.1151 0.0931  -0.1317 535  TYR A N   
3270 C CA  . TYR A 440 ? 0.8006 0.6594 0.7593 -0.1277 0.0888  -0.1371 535  TYR A CA  
3271 C C   . TYR A 440 ? 0.8269 0.6916 0.7749 -0.1352 0.0814  -0.1489 535  TYR A C   
3272 O O   . TYR A 440 ? 0.8519 0.7106 0.7850 -0.1315 0.0818  -0.1539 535  TYR A O   
3273 C CB  . TYR A 440 ? 0.8209 0.6585 0.7855 -0.1339 0.0971  -0.1397 535  TYR A CB  
3274 C CG  . TYR A 440 ? 0.8570 0.6705 0.8101 -0.1317 0.1043  -0.1467 535  TYR A CG  
3275 C CD1 . TYR A 440 ? 0.9066 0.7120 0.8502 -0.1403 0.1030  -0.1604 535  TYR A CD1 
3276 C CD2 . TYR A 440 ? 0.8393 0.6388 0.7912 -0.1207 0.1123  -0.1400 535  TYR A CD2 
3277 C CE1 . TYR A 440 ? 0.9191 0.7023 0.8521 -0.1381 0.1103  -0.1676 535  TYR A CE1 
3278 C CE2 . TYR A 440 ? 0.8843 0.6625 0.8273 -0.1180 0.1193  -0.1467 535  TYR A CE2 
3279 C CZ  . TYR A 440 ? 0.9055 0.6753 0.8390 -0.1266 0.1187  -0.1606 535  TYR A CZ  
3280 O OH  . TYR A 440 ? 0.9749 0.7231 0.8996 -0.1237 0.1264  -0.1679 535  TYR A OH  
3281 N N   . LYS A 441 ? 0.8544 0.7313 0.8101 -0.1460 0.0745  -0.1533 536  LYS A N   
3282 C CA  . LYS A 441 ? 0.9230 0.8053 0.8689 -0.1545 0.0666  -0.1649 536  LYS A CA  
3283 C C   . LYS A 441 ? 0.9645 0.8241 0.9041 -0.1631 0.0723  -0.1767 536  LYS A C   
3284 O O   . LYS A 441 ? 0.9521 0.8005 0.9024 -0.1691 0.0779  -0.1773 536  LYS A O   
3285 C CB  . LYS A 441 ? 0.9001 0.8056 0.8583 -0.1626 0.0563  -0.1653 536  LYS A CB  
3286 C CG  . LYS A 441 ? 0.8607 0.7880 0.8291 -0.1547 0.0517  -0.1535 536  LYS A CG  
3287 C CD  . LYS A 441 ? 0.8737 0.8241 0.8554 -0.1628 0.0416  -0.1550 536  LYS A CD  
3288 C CE  . LYS A 441 ? 0.8974 0.8637 0.8691 -0.1627 0.0296  -0.1588 536  LYS A CE  
3289 N NZ  . LYS A 441 ? 0.7870 0.7670 0.7585 -0.1507 0.0264  -0.1482 536  LYS A NZ  
3290 N N   . GLU A 442 ? 1.0359 0.8875 0.9575 -0.1638 0.0715  -0.1863 537  GLU A N   
3291 C CA  . GLU A 442 ? 1.0999 0.9277 1.0145 -0.1710 0.0781  -0.1980 537  GLU A CA  
3292 C C   . GLU A 442 ? 1.1093 0.9398 1.0294 -0.1867 0.0727  -0.2082 537  GLU A C   
3293 O O   . GLU A 442 ? 1.1452 0.9551 1.0655 -0.1939 0.0793  -0.2162 537  GLU A O   
3294 C CB  . GLU A 442 ? 1.1097 0.9279 1.0028 -0.1671 0.0798  -0.2058 537  GLU A CB  
3295 C CG  . GLU A 442 ? 1.1118 0.9275 1.0009 -0.1521 0.0858  -0.1962 537  GLU A CG  
3296 C CD  . GLU A 442 ? 1.2804 1.0850 1.1492 -0.1483 0.0897  -0.2041 537  GLU A CD  
3297 O OE1 . GLU A 442 ? 1.2196 1.0065 1.0867 -0.1405 0.1003  -0.2030 537  GLU A OE1 
3298 O OE2 . GLU A 442 ? 1.3376 1.1512 1.1921 -0.1530 0.0821  -0.2113 537  GLU A OE2 
3299 N N   . ASP A 443 ? 1.2038 1.0589 1.1297 -0.1921 0.0609  -0.2078 538  ASP A N   
3300 C CA  . ASP A 443 ? 1.1924 1.0531 1.1275 -0.2071 0.0553  -0.2164 538  ASP A CA  
3301 C C   . ASP A 443 ? 1.1325 0.9922 1.0894 -0.2107 0.0606  -0.2097 538  ASP A C   
3302 O O   . ASP A 443 ? 1.1794 1.0261 1.1423 -0.2217 0.0645  -0.2169 538  ASP A O   
3303 C CB  . ASP A 443 ? 1.3006 1.1893 1.2359 -0.2110 0.0404  -0.2178 538  ASP A CB  
3304 C CG  . ASP A 443 ? 1.4390 1.3272 1.3509 -0.2111 0.0343  -0.2266 538  ASP A CG  
3305 O OD1 . ASP A 443 ? 1.4282 1.2939 1.3248 -0.2120 0.0416  -0.2352 538  ASP A OD1 
3306 O OD2 . ASP A 443 ? 1.5150 1.4250 1.4234 -0.2101 0.0225  -0.2249 538  ASP A OD2 
3307 N N   . GLU A 444 ? 1.0660 0.9394 1.0346 -0.2020 0.0609  -0.1960 539  GLU A N   
3308 C CA  . GLU A 444 ? 1.0457 0.9183 1.0332 -0.2037 0.0670  -0.1878 539  GLU A CA  
3309 C C   . GLU A 444 ? 0.9471 0.8077 0.9328 -0.1901 0.0764  -0.1762 539  GLU A C   
3310 O O   . GLU A 444 ? 0.8920 0.7680 0.8821 -0.1807 0.0742  -0.1654 539  GLU A O   
3311 C CB  . GLU A 444 ? 1.0391 0.9406 1.0433 -0.2062 0.0587  -0.1822 539  GLU A CB  
3312 C CG  . GLU A 444 ? 1.1207 1.0415 1.1269 -0.2164 0.0462  -0.1915 539  GLU A CG  
3313 C CD  . GLU A 444 ? 1.1334 1.0845 1.1544 -0.2139 0.0376  -0.1839 539  GLU A CD  
3314 O OE1 . GLU A 444 ? 1.1786 1.1457 1.1922 -0.2090 0.0278  -0.1837 539  GLU A OE1 
3315 O OE2 . GLU A 444 ? 1.0912 1.0495 1.1310 -0.2164 0.0412  -0.1779 539  GLU A OE2 
3316 N N   . PRO A 445 ? 0.9688 0.8022 0.9486 -0.1883 0.0867  -0.1779 540  PRO A N   
3317 C CA  . PRO A 445 ? 0.9146 0.7374 0.8933 -0.1749 0.0949  -0.1666 540  PRO A CA  
3318 C C   . PRO A 445 ? 0.8893 0.7215 0.8833 -0.1721 0.0970  -0.1536 540  PRO A C   
3319 O O   . PRO A 445 ? 0.8617 0.6949 0.8550 -0.1601 0.1000  -0.1430 540  PRO A O   
3320 C CB  . PRO A 445 ? 0.9500 0.7417 0.9231 -0.1764 0.1050  -0.1721 540  PRO A CB  
3321 C CG  . PRO A 445 ? 1.0098 0.7968 0.9735 -0.1872 0.1011  -0.1881 540  PRO A CG  
3322 C CD  . PRO A 445 ? 1.0016 0.8129 0.9744 -0.1977 0.0908  -0.1908 540  PRO A CD  
3323 N N   . ALA A 446 ? 0.8623 0.7024 0.8701 -0.1831 0.0956  -0.1544 541  ALA A N   
3324 C CA  . ALA A 446 ? 0.8337 0.6847 0.8560 -0.1815 0.0978  -0.1428 541  ALA A CA  
3325 C C   . ALA A 446 ? 0.8176 0.6948 0.8424 -0.1732 0.0905  -0.1356 541  ALA A C   
3326 O O   . ALA A 446 ? 0.7850 0.6694 0.8182 -0.1681 0.0933  -0.1248 541  ALA A O   
3327 C CB  . ALA A 446 ? 0.8008 0.6564 0.8376 -0.1963 0.0977  -0.1468 541  ALA A CB  
3328 N N   . ILE A 447 ? 0.7968 0.6874 0.8139 -0.1718 0.0815  -0.1412 542  ILE A N   
3329 C CA  . ILE A 447 ? 0.7713 0.6864 0.7906 -0.1644 0.0738  -0.1353 542  ILE A CA  
3330 C C   . ILE A 447 ? 0.8065 0.7159 0.8103 -0.1518 0.0742  -0.1324 542  ILE A C   
3331 O O   . ILE A 447 ? 0.8046 0.6986 0.7948 -0.1517 0.0760  -0.1396 542  ILE A O   
3332 C CB  . ILE A 447 ? 0.8182 0.7544 0.8413 -0.1725 0.0622  -0.1430 542  ILE A CB  
3333 C CG1 . ILE A 447 ? 0.8254 0.7679 0.8658 -0.1858 0.0621  -0.1465 542  ILE A CG1 
3334 C CG2 . ILE A 447 ? 0.7525 0.7126 0.7783 -0.1642 0.0543  -0.1363 542  ILE A CG2 
3335 C CD1 . ILE A 447 ? 0.7720 0.7239 0.8286 -0.1838 0.0667  -0.1359 542  ILE A CD1 
3336 N N   . SER A 448 ? 0.7296 0.6514 0.7358 -0.1414 0.0730  -0.1223 543  SER A N   
3337 C CA  . SER A 448 ? 0.7491 0.6663 0.7424 -0.1295 0.0741  -0.1186 543  SER A CA  
3338 C C   . SER A 448 ? 0.7281 0.6670 0.7188 -0.1248 0.0645  -0.1168 543  SER A C   
3339 O O   . SER A 448 ? 0.7134 0.6720 0.7148 -0.1284 0.0577  -0.1157 543  SER A O   
3340 C CB  . SER A 448 ? 0.7516 0.6601 0.7479 -0.1201 0.0822  -0.1077 543  SER A CB  
3341 O OG  . SER A 448 ? 0.6909 0.6171 0.6980 -0.1164 0.0800  -0.0987 543  SER A OG  
3342 N N   . ASN A 449 ? 0.7065 0.6412 0.6832 -0.1166 0.0642  -0.1165 544  ASN A N   
3343 C CA  . ASN A 449 ? 0.7079 0.6599 0.6796 -0.1112 0.0559  -0.1141 544  ASN A CA  
3344 C C   . ASN A 449 ? 0.6970 0.6558 0.6740 -0.1002 0.0582  -0.1024 544  ASN A C   
3345 O O   . ASN A 449 ? 0.7069 0.6613 0.6747 -0.0912 0.0604  -0.0987 544  ASN A O   
3346 C CB  . ASN A 449 ? 0.7314 0.6755 0.6842 -0.1096 0.0546  -0.1206 544  ASN A CB  
3347 C CG  . ASN A 449 ? 0.7889 0.7327 0.7357 -0.1208 0.0489  -0.1323 544  ASN A CG  
3348 O OD1 . ASN A 449 ? 0.7833 0.7396 0.7408 -0.1288 0.0427  -0.1347 544  ASN A OD1 
3349 N ND2 . ASN A 449 ? 0.7608 0.6910 0.6905 -0.1216 0.0510  -0.1401 544  ASN A ND2 
3350 N N   . SER A 450 ? 0.6668 0.6371 0.6593 -0.1015 0.0577  -0.0969 545  SER A N   
3351 C CA  . SER A 450 ? 0.6490 0.6247 0.6482 -0.0928 0.0608  -0.0864 545  SER A CA  
3352 C C   . SER A 450 ? 0.6629 0.6621 0.6732 -0.0926 0.0533  -0.0831 545  SER A C   
3353 O O   . SER A 450 ? 0.6530 0.6637 0.6688 -0.1000 0.0465  -0.0885 545  SER A O   
3354 C CB  . SER A 450 ? 0.6391 0.6031 0.6462 -0.0945 0.0697  -0.0825 545  SER A CB  
3355 O OG  . SER A 450 ? 0.6693 0.6328 0.6848 -0.1059 0.0698  -0.0880 545  SER A OG  
3356 N N   . TYR A 451 ? 0.6079 0.6143 0.6221 -0.0839 0.0545  -0.0744 546  TYR A N   
3357 C CA  . TYR A 451 ? 0.5896 0.6174 0.6141 -0.0818 0.0480  -0.0708 546  TYR A CA  
3358 C C   . TYR A 451 ? 0.6265 0.6575 0.6572 -0.0741 0.0527  -0.0617 546  TYR A C   
3359 O O   . TYR A 451 ? 0.5805 0.6009 0.6030 -0.0669 0.0574  -0.0574 546  TYR A O   
3360 C CB  . TYR A 451 ? 0.5830 0.6194 0.5985 -0.0780 0.0393  -0.0723 546  TYR A CB  
3361 C CG  . TYR A 451 ? 0.6251 0.6478 0.6241 -0.0712 0.0423  -0.0713 546  TYR A CG  
3362 C CD1 . TYR A 451 ? 0.6142 0.6238 0.5998 -0.0749 0.0431  -0.0785 546  TYR A CD1 
3363 C CD2 . TYR A 451 ? 0.6018 0.6244 0.5991 -0.0614 0.0452  -0.0637 546  TYR A CD2 
3364 C CE1 . TYR A 451 ? 0.5915 0.5891 0.5632 -0.0687 0.0469  -0.0779 546  TYR A CE1 
3365 C CE2 . TYR A 451 ? 0.6082 0.6192 0.5921 -0.0556 0.0486  -0.0630 546  TYR A CE2 
3366 C CZ  . TYR A 451 ? 0.6200 0.6187 0.5915 -0.0591 0.0496  -0.0700 546  TYR A CZ  
3367 O OH  . TYR A 451 ? 0.6154 0.6034 0.5749 -0.0532 0.0538  -0.0694 546  TYR A OH  
3368 N N   . ASP A 452 ? 0.5455 0.5918 0.5910 -0.0758 0.0514  -0.0592 547  ASP A N   
3369 C CA  . ASP A 452 ? 0.5709 0.6245 0.6224 -0.0685 0.0541  -0.0514 547  ASP A CA  
3370 C C   . ASP A 452 ? 0.5668 0.6413 0.6273 -0.0660 0.0462  -0.0507 547  ASP A C   
3371 O O   . ASP A 452 ? 0.5660 0.6524 0.6356 -0.0723 0.0406  -0.0553 547  ASP A O   
3372 C CB  . ASP A 452 ? 0.5689 0.6205 0.6302 -0.0722 0.0618  -0.0483 547  ASP A CB  
3373 C CG  . ASP A 452 ? 0.6273 0.6574 0.6804 -0.0736 0.0698  -0.0474 547  ASP A CG  
3374 O OD1 . ASP A 452 ? 0.6207 0.6374 0.6613 -0.0702 0.0703  -0.0485 547  ASP A OD1 
3375 O OD2 . ASP A 452 ? 0.6498 0.6763 0.7095 -0.0782 0.0760  -0.0453 547  ASP A OD2 
3376 N N   . PHE A 453 ? 0.5577 0.6366 0.6164 -0.0568 0.0456  -0.0451 548  PHE A N   
3377 C CA  . PHE A 453 ? 0.5125 0.6100 0.5812 -0.0531 0.0395  -0.0432 548  PHE A CA  
3378 C C   . PHE A 453 ? 0.5472 0.6519 0.6284 -0.0515 0.0451  -0.0389 548  PHE A C   
3379 O O   . PHE A 453 ? 0.5281 0.6223 0.6052 -0.0494 0.0528  -0.0351 548  PHE A O   
3380 C CB  . PHE A 453 ? 0.5342 0.6318 0.5932 -0.0440 0.0353  -0.0398 548  PHE A CB  
3381 C CG  . PHE A 453 ? 0.5410 0.6325 0.5859 -0.0447 0.0297  -0.0434 548  PHE A CG  
3382 C CD1 . PHE A 453 ? 0.5317 0.6151 0.5708 -0.0525 0.0294  -0.0498 548  PHE A CD1 
3383 C CD2 . PHE A 453 ? 0.5312 0.6246 0.5679 -0.0377 0.0250  -0.0405 548  PHE A CD2 
3384 C CE1 . PHE A 453 ? 0.5561 0.6338 0.5808 -0.0532 0.0248  -0.0536 548  PHE A CE1 
3385 C CE2 . PHE A 453 ? 0.5444 0.6321 0.5667 -0.0384 0.0204  -0.0435 548  PHE A CE2 
3386 C CZ  . PHE A 453 ? 0.5723 0.6524 0.5882 -0.0461 0.0203  -0.0502 548  PHE A CZ  
3387 N N   . PHE A 454 ? 0.5099 0.6329 0.6064 -0.0523 0.0411  -0.0395 549  PHE A N   
3388 C CA  . PHE A 454 ? 0.4983 0.6303 0.6081 -0.0515 0.0466  -0.0365 549  PHE A CA  
3389 C C   . PHE A 454 ? 0.5210 0.6678 0.6387 -0.0439 0.0419  -0.0340 549  PHE A C   
3390 O O   . PHE A 454 ? 0.5224 0.6793 0.6436 -0.0427 0.0329  -0.0359 549  PHE A O   
3391 C CB  . PHE A 454 ? 0.4936 0.6343 0.6185 -0.0614 0.0485  -0.0406 549  PHE A CB  
3392 C CG  . PHE A 454 ? 0.5237 0.6488 0.6421 -0.0693 0.0542  -0.0427 549  PHE A CG  
3393 C CD1 . PHE A 454 ? 0.5016 0.6192 0.6211 -0.0717 0.0641  -0.0395 549  PHE A CD1 
3394 C CD2 . PHE A 454 ? 0.5067 0.6233 0.6165 -0.0740 0.0500  -0.0476 549  PHE A CD2 
3395 C CE1 . PHE A 454 ? 0.5557 0.6574 0.6691 -0.0784 0.0695  -0.0408 549  PHE A CE1 
3396 C CE2 . PHE A 454 ? 0.5286 0.6292 0.6325 -0.0808 0.0556  -0.0498 549  PHE A CE2 
3397 C CZ  . PHE A 454 ? 0.5549 0.6477 0.6610 -0.0828 0.0654  -0.0460 549  PHE A CZ  
3398 N N   . MET A 455 ? 0.4621 0.6093 0.5821 -0.0389 0.0481  -0.0297 550  MET A N   
3399 C CA  . MET A 455 ? 0.5155 0.6761 0.6455 -0.0321 0.0463  -0.0275 550  MET A CA  
3400 C C   . MET A 455 ? 0.5221 0.6914 0.6661 -0.0348 0.0538  -0.0273 550  MET A C   
3401 O O   . MET A 455 ? 0.5061 0.6656 0.6444 -0.0367 0.0623  -0.0252 550  MET A O   
3402 C CB  . MET A 455 ? 0.4744 0.6264 0.5924 -0.0231 0.0471  -0.0229 550  MET A CB  
3403 C CG  . MET A 455 ? 0.5012 0.6451 0.6053 -0.0198 0.0406  -0.0226 550  MET A CG  
3404 S SD  . MET A 455 ? 0.4770 0.6103 0.5680 -0.0104 0.0430  -0.0173 550  MET A SD  
3405 C CE  . MET A 455 ? 0.4532 0.6015 0.5586 -0.0041 0.0420  -0.0154 550  MET A CE  
3406 N N   . ARG A 456 ? 0.4766 0.6644 0.6388 -0.0352 0.0507  -0.0295 551  ARG A N   
3407 C CA  . ARG A 456 ? 0.4969 0.6956 0.6747 -0.0383 0.0580  -0.0302 551  ARG A CA  
3408 C C   . ARG A 456 ? 0.5109 0.7020 0.6873 -0.0480 0.0656  -0.0314 551  ARG A C   
3409 O O   . ARG A 456 ? 0.4918 0.6815 0.6700 -0.0498 0.0750  -0.0296 551  ARG A O   
3410 C CB  . ARG A 456 ? 0.4990 0.6971 0.6752 -0.0308 0.0640  -0.0266 551  ARG A CB  
3411 C CG  . ARG A 456 ? 0.4783 0.6853 0.6597 -0.0215 0.0577  -0.0257 551  ARG A CG  
3412 C CD  . ARG A 456 ? 0.4527 0.6605 0.6352 -0.0156 0.0648  -0.0234 551  ARG A CD  
3413 N NE  . ARG A 456 ? 0.5171 0.7259 0.6979 -0.0061 0.0594  -0.0216 551  ARG A NE  
3414 C CZ  . ARG A 456 ? 0.5096 0.7329 0.7060 -0.0013 0.0552  -0.0227 551  ARG A CZ  
3415 N NH1 . ARG A 456 ? 0.4355 0.6753 0.6518 -0.0046 0.0553  -0.0260 551  ARG A NH1 
3416 N NH2 . ARG A 456 ? 0.4822 0.7032 0.6748 0.0072  0.0506  -0.0204 551  ARG A NH2 
3417 N N   . GLY A 457 ? 0.4976 0.6828 0.6699 -0.0546 0.0617  -0.0344 552  GLY A N   
3418 C CA  . GLY A 457 ? 0.4752 0.6522 0.6468 -0.0643 0.0684  -0.0358 552  GLY A CA  
3419 C C   . GLY A 457 ? 0.5469 0.7018 0.6998 -0.0640 0.0750  -0.0319 552  GLY A C   
3420 O O   . GLY A 457 ? 0.5147 0.6614 0.6668 -0.0715 0.0817  -0.0320 552  GLY A O   
3421 N N   . GLU A 458 ? 0.4822 0.6271 0.6204 -0.0556 0.0733  -0.0284 553  GLU A N   
3422 C CA  . GLU A 458 ? 0.5290 0.6539 0.6508 -0.0545 0.0790  -0.0246 553  GLU A CA  
3423 C C   . GLU A 458 ? 0.5211 0.6341 0.6286 -0.0509 0.0734  -0.0251 553  GLU A C   
3424 O O   . GLU A 458 ? 0.4766 0.5957 0.5831 -0.0455 0.0662  -0.0259 553  GLU A O   
3425 C CB  . GLU A 458 ? 0.5227 0.6464 0.6405 -0.0481 0.0847  -0.0193 553  GLU A CB  
3426 C CG  . GLU A 458 ? 0.5687 0.7033 0.6993 -0.0523 0.0917  -0.0191 553  GLU A CG  
3427 C CD  . GLU A 458 ? 0.6002 0.7329 0.7255 -0.0473 0.0982  -0.0145 553  GLU A CD  
3428 O OE1 . GLU A 458 ? 0.5897 0.7073 0.7000 -0.0446 0.1009  -0.0102 553  GLU A OE1 
3429 O OE2 . GLU A 458 ? 0.6080 0.7549 0.7448 -0.0463 0.1007  -0.0154 553  GLU A OE2 
3430 N N   . GLU A 459 ? 0.5219 0.6177 0.6189 -0.0542 0.0770  -0.0247 554  GLU A N   
3431 C CA  . GLU A 459 ? 0.5755 0.6589 0.6593 -0.0517 0.0732  -0.0259 554  GLU A CA  
3432 C C   . GLU A 459 ? 0.5452 0.6245 0.6192 -0.0417 0.0724  -0.0215 554  GLU A C   
3433 O O   . GLU A 459 ? 0.5826 0.6579 0.6538 -0.0382 0.0777  -0.0166 554  GLU A O   
3434 C CB  . GLU A 459 ? 0.5622 0.6275 0.6387 -0.0571 0.0786  -0.0263 554  GLU A CB  
3435 C CG  . GLU A 459 ? 0.6334 0.6850 0.6968 -0.0549 0.0759  -0.0284 554  GLU A CG  
3436 C CD  . GLU A 459 ? 0.7289 0.7617 0.7819 -0.0522 0.0823  -0.0242 554  GLU A CD  
3437 O OE1 . GLU A 459 ? 0.7607 0.7887 0.8052 -0.0442 0.0816  -0.0212 554  GLU A OE1 
3438 O OE2 . GLU A 459 ? 0.7843 0.8074 0.8383 -0.0580 0.0879  -0.0237 554  GLU A OE2 
3439 N N   . ILE A 460 ? 0.5436 0.6240 0.6120 -0.0376 0.0658  -0.0231 555  ILE A N   
3440 C CA  . ILE A 460 ? 0.5578 0.6352 0.6177 -0.0287 0.0646  -0.0194 555  ILE A CA  
3441 C C   . ILE A 460 ? 0.5665 0.6300 0.6129 -0.0272 0.0637  -0.0206 555  ILE A C   
3442 O O   . ILE A 460 ? 0.5928 0.6486 0.6310 -0.0210 0.0655  -0.0172 555  ILE A O   
3443 C CB  . ILE A 460 ? 0.5431 0.6350 0.6086 -0.0241 0.0580  -0.0195 555  ILE A CB  
3444 C CG1 . ILE A 460 ? 0.5436 0.6441 0.6141 -0.0288 0.0509  -0.0246 555  ILE A CG1 
3445 C CG2 . ILE A 460 ? 0.5501 0.6529 0.6261 -0.0217 0.0607  -0.0169 555  ILE A CG2 
3446 C CD1 . ILE A 460 ? 0.5680 0.6727 0.6334 -0.0236 0.0432  -0.0245 555  ILE A CD1 
3447 N N   . LEU A 461 ? 0.5838 0.6449 0.6287 -0.0330 0.0608  -0.0259 556  LEU A N   
3448 C CA  . LEU A 461 ? 0.5652 0.6141 0.5977 -0.0327 0.0599  -0.0287 556  LEU A CA  
3449 C C   . LEU A 461 ? 0.6137 0.6520 0.6451 -0.0406 0.0630  -0.0332 556  LEU A C   
3450 O O   . LEU A 461 ? 0.5659 0.6109 0.6060 -0.0479 0.0616  -0.0366 556  LEU A O   
3451 C CB  . LEU A 461 ? 0.5034 0.5595 0.5320 -0.0318 0.0519  -0.0318 556  LEU A CB  
3452 C CG  . LEU A 461 ? 0.5680 0.6127 0.5828 -0.0323 0.0509  -0.0357 556  LEU A CG  
3453 C CD1 . LEU A 461 ? 0.5466 0.5968 0.5545 -0.0272 0.0450  -0.0346 556  LEU A CD1 
3454 C CD2 . LEU A 461 ? 0.5709 0.6127 0.5850 -0.0413 0.0490  -0.0428 556  LEU A CD2 
3455 N N   . SER A 462 ? 0.5919 0.6140 0.6136 -0.0392 0.0672  -0.0333 557  SER A N   
3456 C CA  . SER A 462 ? 0.6148 0.6242 0.6338 -0.0461 0.0702  -0.0382 557  SER A CA  
3457 C C   . SER A 462 ? 0.6028 0.6006 0.6092 -0.0439 0.0701  -0.0419 557  SER A C   
3458 O O   . SER A 462 ? 0.5603 0.5536 0.5605 -0.0364 0.0718  -0.0383 557  SER A O   
3459 C CB  . SER A 462 ? 0.5946 0.5929 0.6161 -0.0471 0.0779  -0.0342 557  SER A CB  
3460 O OG  . SER A 462 ? 0.6979 0.6877 0.7212 -0.0558 0.0802  -0.0390 557  SER A OG  
3461 N N   . GLY A 463 ? 0.5927 0.5858 0.5955 -0.0507 0.0683  -0.0493 558  GLY A N   
3462 C CA  . GLY A 463 ? 0.6128 0.5937 0.6029 -0.0491 0.0694  -0.0536 558  GLY A CA  
3463 C C   . GLY A 463 ? 0.6184 0.5918 0.6048 -0.0579 0.0687  -0.0625 558  GLY A C   
3464 O O   . GLY A 463 ? 0.6146 0.5912 0.6091 -0.0658 0.0678  -0.0653 558  GLY A O   
3465 N N   . SER A 464 ? 0.6082 0.5716 0.5822 -0.0568 0.0696  -0.0674 559  SER A N   
3466 C CA  . SER A 464 ? 0.6497 0.6049 0.6183 -0.0653 0.0691  -0.0770 559  SER A CA  
3467 C C   . SER A 464 ? 0.6514 0.5979 0.6045 -0.0631 0.0697  -0.0823 559  SER A C   
3468 O O   . SER A 464 ? 0.5861 0.5299 0.5339 -0.0548 0.0725  -0.0783 559  SER A O   
3469 C CB  . SER A 464 ? 0.6566 0.5962 0.6300 -0.0701 0.0762  -0.0787 559  SER A CB  
3470 O OG  . SER A 464 ? 0.6676 0.5903 0.6349 -0.0641 0.0836  -0.0776 559  SER A OG  
3471 N N   . GLN A 465 ? 0.6618 0.6049 0.6080 -0.0711 0.0669  -0.0917 560  GLN A N   
3472 C CA  . GLN A 465 ? 0.6507 0.5793 0.5825 -0.0713 0.0707  -0.0990 560  GLN A CA  
3473 C C   . GLN A 465 ? 0.6776 0.5873 0.6117 -0.0683 0.0809  -0.0983 560  GLN A C   
3474 O O   . GLN A 465 ? 0.6613 0.5652 0.6053 -0.0719 0.0840  -0.0971 560  GLN A O   
3475 C CB  . GLN A 465 ? 0.6852 0.6123 0.6104 -0.0820 0.0662  -0.1098 560  GLN A CB  
3476 C CG  . GLN A 465 ? 0.6955 0.6064 0.6048 -0.0835 0.0707  -0.1191 560  GLN A CG  
3477 C CD  . GLN A 465 ? 0.7586 0.6672 0.6619 -0.0951 0.0663  -0.1305 560  GLN A CD  
3478 O OE1 . GLN A 465 ? 0.8224 0.7359 0.7364 -0.1027 0.0629  -0.1321 560  GLN A OE1 
3479 N NE2 . GLN A 465 ? 0.8414 0.7427 0.7276 -0.0970 0.0666  -0.1388 560  GLN A NE2 
3480 N N   . ARG A 466 ? 0.6665 0.5667 0.5919 -0.0617 0.0862  -0.0988 561  ARG A N   
3481 C CA  . ARG A 466 ? 0.6795 0.5621 0.6076 -0.0574 0.0956  -0.0978 561  ARG A CA  
3482 C C   . ARG A 466 ? 0.7239 0.5890 0.6432 -0.0625 0.1004  -0.1089 561  ARG A C   
3483 O O   . ARG A 466 ? 0.7136 0.5798 0.6206 -0.0664 0.0977  -0.1169 561  ARG A O   
3484 C CB  . ARG A 466 ? 0.6645 0.5477 0.5914 -0.0463 0.0993  -0.0913 561  ARG A CB  
3485 C CG  . ARG A 466 ? 0.6685 0.5701 0.5999 -0.0414 0.0936  -0.0823 561  ARG A CG  
3486 C CD  . ARG A 466 ? 0.6211 0.5290 0.5661 -0.0419 0.0921  -0.0749 561  ARG A CD  
3487 N NE  . ARG A 466 ? 0.6280 0.5489 0.5773 -0.0348 0.0896  -0.0660 561  ARG A NE  
3488 C CZ  . ARG A 466 ? 0.6495 0.5808 0.6087 -0.0348 0.0868  -0.0596 561  ARG A CZ  
3489 N NH1 . ARG A 466 ? 0.6320 0.5637 0.5983 -0.0418 0.0860  -0.0606 561  ARG A NH1 
3490 N NH2 . ARG A 466 ? 0.5982 0.5396 0.5603 -0.0280 0.0851  -0.0523 561  ARG A NH2 
3491 N N   . ILE A 467 ? 0.7171 0.5655 0.6423 -0.0625 0.1075  -0.1093 562  ILE A N   
3492 C CA  . ILE A 467 ? 0.7427 0.5720 0.6602 -0.0649 0.1140  -0.1192 562  ILE A CA  
3493 C C   . ILE A 467 ? 0.7574 0.5836 0.6665 -0.0561 0.1186  -0.1199 562  ILE A C   
3494 O O   . ILE A 467 ? 0.7225 0.5483 0.6377 -0.0466 0.1224  -0.1119 562  ILE A O   
3495 C CB  . ILE A 467 ? 0.7453 0.5564 0.6720 -0.0654 0.1210  -0.1181 562  ILE A CB  
3496 C CG1 . ILE A 467 ? 0.7132 0.5278 0.6485 -0.0749 0.1171  -0.1173 562  ILE A CG1 
3497 C CG2 . ILE A 467 ? 0.7662 0.5561 0.6854 -0.0667 0.1285  -0.1287 562  ILE A CG2 
3498 C CD1 . ILE A 467 ? 0.7337 0.5316 0.6786 -0.0752 0.1236  -0.1135 562  ILE A CD1 
3499 N N   . SER A 468 ? 0.7375 0.5623 0.6322 -0.0596 0.1181  -0.1295 563  SER A N   
3500 C CA  . SER A 468 ? 0.7510 0.5731 0.6364 -0.0525 0.1232  -0.1314 563  SER A CA  
3501 C C   . SER A 468 ? 0.7948 0.5970 0.6720 -0.0545 0.1315  -0.1430 563  SER A C   
3502 O O   . SER A 468 ? 0.8663 0.6664 0.7311 -0.0525 0.1350  -0.1487 563  SER A O   
3503 C CB  . SER A 468 ? 0.7707 0.6091 0.6443 -0.0538 0.1160  -0.1315 563  SER A CB  
3504 O OG  . SER A 468 ? 0.8474 0.6871 0.7107 -0.0643 0.1103  -0.1407 563  SER A OG  
3505 N N   . ASP A 469 ? 0.8095 0.5964 0.6930 -0.0587 0.1352  -0.1468 564  ASP A N   
3506 C CA  . ASP A 469 ? 0.8233 0.5887 0.7018 -0.0598 0.1442  -0.1574 564  ASP A CA  
3507 C C   . ASP A 469 ? 0.8578 0.6095 0.7511 -0.0526 0.1514  -0.1511 564  ASP A C   
3508 O O   . ASP A 469 ? 0.8494 0.5997 0.7536 -0.0552 0.1492  -0.1453 564  ASP A O   
3509 C CB  . ASP A 469 ? 0.8764 0.6341 0.7482 -0.0726 0.1417  -0.1689 564  ASP A CB  
3510 C CG  . ASP A 469 ? 0.9337 0.6672 0.8005 -0.0742 0.1515  -0.1807 564  ASP A CG  
3511 O OD1 . ASP A 469 ? 1.0159 0.7456 0.8671 -0.0797 0.1522  -0.1926 564  ASP A OD1 
3512 O OD2 . ASP A 469 ? 0.9101 0.6279 0.7882 -0.0700 0.1585  -0.1781 564  ASP A OD2 
3513 N N   . VAL A 470 ? 0.8517 0.5936 0.7456 -0.0436 0.1601  -0.1521 565  VAL A N   
3514 C CA  . VAL A 470 ? 0.8619 0.5941 0.7707 -0.0346 0.1657  -0.1438 565  VAL A CA  
3515 C C   . VAL A 470 ? 0.8843 0.5968 0.7992 -0.0397 0.1690  -0.1468 565  VAL A C   
3516 O O   . VAL A 470 ? 0.8841 0.5925 0.8115 -0.0363 0.1693  -0.1371 565  VAL A O   
3517 C CB  . VAL A 470 ? 0.8403 0.5667 0.7492 -0.0241 0.1743  -0.1454 565  VAL A CB  
3518 C CG1 . VAL A 470 ? 0.8844 0.5941 0.7827 -0.0278 0.1819  -0.1605 565  VAL A CG1 
3519 C CG2 . VAL A 470 ? 0.8446 0.5631 0.7698 -0.0140 0.1787  -0.1359 565  VAL A CG2 
3520 N N   . ASN A 471 ? 0.9065 0.6065 0.8121 -0.0486 0.1714  -0.1602 566  ASN A N   
3521 C CA  . ASN A 471 ? 0.9105 0.5900 0.8214 -0.0545 0.1751  -0.1641 566  ASN A CA  
3522 C C   . ASN A 471 ? 0.8964 0.5837 0.8125 -0.0637 0.1673  -0.1591 566  ASN A C   
3523 O O   . ASN A 471 ? 0.9097 0.5863 0.8366 -0.0641 0.1693  -0.1532 566  ASN A O   
3524 C CB  . ASN A 471 ? 0.9303 0.5939 0.8292 -0.0616 0.1802  -0.1810 566  ASN A CB  
3525 C CG  . ASN A 471 ? 1.0315 0.6883 0.9245 -0.0529 0.1887  -0.1871 566  ASN A CG  
3526 O OD1 . ASN A 471 ? 1.0279 0.6724 0.9307 -0.0429 0.1965  -0.1835 566  ASN A OD1 
3527 N ND2 . ASN A 471 ? 1.0679 0.7326 0.9447 -0.0568 0.1874  -0.1963 566  ASN A ND2 
3528 N N   . LEU A 472 ? 0.9033 0.6096 0.8124 -0.0710 0.1585  -0.1611 567  LEU A N   
3529 C CA  . LEU A 472 ? 0.8965 0.6135 0.8128 -0.0787 0.1512  -0.1555 567  LEU A CA  
3530 C C   . LEU A 472 ? 0.8590 0.5845 0.7878 -0.0704 0.1500  -0.1397 567  LEU A C   
3531 O O   . LEU A 472 ? 0.8627 0.5859 0.8009 -0.0743 0.1492  -0.1338 567  LEU A O   
3532 C CB  . LEU A 472 ? 0.8908 0.6287 0.7985 -0.0862 0.1414  -0.1595 567  LEU A CB  
3533 C CG  . LEU A 472 ? 0.9667 0.6990 0.8612 -0.0969 0.1400  -0.1750 567  LEU A CG  
3534 C CD1 . LEU A 472 ? 0.9603 0.7152 0.8497 -0.1042 0.1285  -0.1761 567  LEU A CD1 
3535 C CD2 . LEU A 472 ? 0.9515 0.6633 0.8502 -0.1058 0.1444  -0.1825 567  LEU A CD2 
3536 N N   . LEU A 473 ? 0.8254 0.5606 0.7540 -0.0594 0.1502  -0.1330 568  LEU A N   
3537 C CA  . LEU A 473 ? 0.8421 0.5854 0.7814 -0.0514 0.1490  -0.1185 568  LEU A CA  
3538 C C   . LEU A 473 ? 0.8488 0.5725 0.7977 -0.0471 0.1558  -0.1133 568  LEU A C   
3539 O O   . LEU A 473 ? 0.8347 0.5597 0.7920 -0.0475 0.1542  -0.1037 568  LEU A O   
3540 C CB  . LEU A 473 ? 0.7796 0.5358 0.7167 -0.0408 0.1484  -0.1138 568  LEU A CB  
3541 C CG  . LEU A 473 ? 0.7857 0.5512 0.7328 -0.0318 0.1469  -0.0996 568  LEU A CG  
3542 C CD1 . LEU A 473 ? 0.7041 0.4864 0.6549 -0.0367 0.1392  -0.0928 568  LEU A CD1 
3543 C CD2 . LEU A 473 ? 0.7617 0.5370 0.7067 -0.0219 0.1476  -0.0970 568  LEU A CD2 
3544 N N   . LEU A 474 ? 0.8567 0.5613 0.8041 -0.0428 0.1637  -0.1194 569  LEU A N   
3545 C CA  . LEU A 474 ? 0.8559 0.5398 0.8125 -0.0388 0.1700  -0.1147 569  LEU A CA  
3546 C C   . LEU A 474 ? 0.8746 0.5476 0.8339 -0.0500 0.1697  -0.1160 569  LEU A C   
3547 O O   . LEU A 474 ? 0.8784 0.5442 0.8461 -0.0486 0.1708  -0.1061 569  LEU A O   
3548 C CB  . LEU A 474 ? 0.8809 0.5459 0.8356 -0.0330 0.1787  -0.1229 569  LEU A CB  
3549 C CG  . LEU A 474 ? 0.9152 0.5867 0.8722 -0.0196 0.1813  -0.1189 569  LEU A CG  
3550 C CD1 . LEU A 474 ? 0.8322 0.4877 0.7852 -0.0164 0.1901  -0.1307 569  LEU A CD1 
3551 C CD2 . LEU A 474 ? 0.8335 0.5031 0.8032 -0.0096 0.1818  -0.1045 569  LEU A CD2 
3552 N N   . GLU A 475 ? 0.8884 0.5601 0.8403 -0.0617 0.1682  -0.1282 570  GLU A N   
3553 C CA  . GLU A 475 ? 0.8995 0.5627 0.8548 -0.0736 0.1677  -0.1302 570  GLU A CA  
3554 C C   . GLU A 475 ? 0.8629 0.5429 0.8254 -0.0762 0.1616  -0.1187 570  GLU A C   
3555 O O   . GLU A 475 ? 0.8633 0.5335 0.8332 -0.0797 0.1638  -0.1126 570  GLU A O   
3556 C CB  . GLU A 475 ? 0.9541 0.6180 0.9003 -0.0860 0.1652  -0.1453 570  GLU A CB  
3557 C CG  . GLU A 475 ? 1.0566 0.6983 0.9959 -0.0867 0.1727  -0.1585 570  GLU A CG  
3558 C CD  . GLU A 475 ? 1.1443 0.7881 1.0730 -0.0997 0.1692  -0.1736 570  GLU A CD  
3559 O OE1 . GLU A 475 ? 1.1352 0.7949 1.0651 -0.1090 0.1613  -0.1730 570  GLU A OE1 
3560 O OE2 . GLU A 475 ? 1.2137 0.8438 1.1331 -0.1005 0.1742  -0.1861 570  GLU A OE2 
3561 N N   . ASN A 476 ? 0.8626 0.5675 0.8229 -0.0746 0.1544  -0.1155 571  ASN A N   
3562 C CA  . ASN A 476 ? 0.8772 0.5989 0.8443 -0.0774 0.1490  -0.1057 571  ASN A CA  
3563 C C   . ASN A 476 ? 0.8524 0.5717 0.8267 -0.0676 0.1514  -0.0913 571  ASN A C   
3564 O O   . ASN A 476 ? 0.8659 0.5885 0.8465 -0.0710 0.1504  -0.0833 571  ASN A O   
3565 C CB  . ASN A 476 ? 0.8063 0.5544 0.7694 -0.0778 0.1407  -0.1064 571  ASN A CB  
3566 C CG  . ASN A 476 ? 0.8305 0.5933 0.7986 -0.0883 0.1347  -0.1059 571  ASN A CG  
3567 O OD1 . ASN A 476 ? 0.8345 0.5885 0.8047 -0.0990 0.1358  -0.1121 571  ASN A OD1 
3568 N ND2 . ASN A 476 ? 0.7715 0.5566 0.7426 -0.0854 0.1287  -0.0987 571  ASN A ND2 
3569 N N   . ILE A 477 ? 0.8731 0.5875 0.8465 -0.0556 0.1546  -0.0880 572  ILE A N   
3570 C CA  . ILE A 477 ? 0.8516 0.5623 0.8315 -0.0461 0.1565  -0.0746 572  ILE A CA  
3571 C C   . ILE A 477 ? 0.8554 0.5424 0.8401 -0.0489 0.1624  -0.0717 572  ILE A C   
3572 O O   . ILE A 477 ? 0.8568 0.5429 0.8463 -0.0482 0.1622  -0.0605 572  ILE A O   
3573 C CB  . ILE A 477 ? 0.8522 0.5631 0.8315 -0.0329 0.1585  -0.0728 572  ILE A CB  
3574 C CG1 . ILE A 477 ? 0.7933 0.5289 0.7691 -0.0296 0.1524  -0.0718 572  ILE A CG1 
3575 C CG2 . ILE A 477 ? 0.8476 0.5491 0.8340 -0.0232 0.1612  -0.0604 572  ILE A CG2 
3576 C CD1 . ILE A 477 ? 0.7715 0.5078 0.7450 -0.0196 0.1549  -0.0743 572  ILE A CD1 
3577 N N   . LYS A 478 ? 0.8430 0.5096 0.8257 -0.0523 0.1678  -0.0815 573  LYS A N   
3578 C CA  . LYS A 478 ? 0.9094 0.5521 0.8965 -0.0562 0.1734  -0.0792 573  LYS A CA  
3579 C C   . LYS A 478 ? 0.9059 0.5527 0.8950 -0.0697 0.1712  -0.0788 573  LYS A C   
3580 O O   . LYS A 478 ? 0.9121 0.5478 0.9060 -0.0718 0.1739  -0.0703 573  LYS A O   
3581 C CB  . LYS A 478 ? 0.9381 0.5574 0.9227 -0.0573 0.1801  -0.0911 573  LYS A CB  
3582 C CG  . LYS A 478 ? 0.9628 0.5546 0.9524 -0.0603 0.1865  -0.0885 573  LYS A CG  
3583 C CD  . LYS A 478 ? 1.0406 0.6083 1.0305 -0.0533 0.1941  -0.0948 573  LYS A CD  
3584 C CE  . LYS A 478 ? 1.1873 0.7270 1.1835 -0.0525 0.2003  -0.0880 573  LYS A CE  
3585 N NZ  . LYS A 478 ? 1.1938 0.7252 1.1958 -0.0366 0.2027  -0.0767 573  LYS A NZ  
3586 N N   . ARG A 479 ? 0.8970 0.5602 0.8828 -0.0789 0.1661  -0.0877 574  ARG A N   
3587 C CA  . ARG A 479 ? 0.9036 0.5744 0.8930 -0.0918 0.1634  -0.0881 574  ARG A CA  
3588 C C   . ARG A 479 ? 0.8841 0.5679 0.8789 -0.0893 0.1612  -0.0739 574  ARG A C   
3589 O O   . ARG A 479 ? 0.8801 0.5612 0.8799 -0.0979 0.1627  -0.0701 574  ARG A O   
3590 C CB  . ARG A 479 ? 0.9195 0.6096 0.9048 -0.0997 0.1568  -0.0992 574  ARG A CB  
3591 C CG  . ARG A 479 ? 0.9638 0.6583 0.9535 -0.1150 0.1547  -0.1044 574  ARG A CG  
3592 C CD  . ARG A 479 ? 0.9743 0.6835 0.9587 -0.1226 0.1481  -0.1174 574  ARG A CD  
3593 N NE  . ARG A 479 ? 0.9710 0.6625 0.9478 -0.1258 0.1513  -0.1307 574  ARG A NE  
3594 C CZ  . ARG A 479 ? 1.0023 0.6964 0.9690 -0.1208 0.1498  -0.1381 574  ARG A CZ  
3595 N NH1 . ARG A 479 ? 0.8953 0.6090 0.8585 -0.1123 0.1449  -0.1334 574  ARG A NH1 
3596 N NH2 . ARG A 479 ? 1.0584 0.7347 1.0180 -0.1247 0.1537  -0.1507 574  ARG A NH2 
3597 N N   . PHE A 480 ? 0.8911 0.5891 0.8848 -0.0782 0.1581  -0.0662 575  PHE A N   
3598 C CA  . PHE A 480 ? 0.8378 0.5489 0.8352 -0.0750 0.1558  -0.0534 575  PHE A CA  
3599 C C   . PHE A 480 ? 0.8737 0.5687 0.8725 -0.0662 0.1603  -0.0413 575  PHE A C   
3600 O O   . PHE A 480 ? 0.8714 0.5761 0.8716 -0.0621 0.1585  -0.0301 575  PHE A O   
3601 C CB  . PHE A 480 ? 0.8564 0.5927 0.8517 -0.0686 0.1493  -0.0520 575  PHE A CB  
3602 C CG  . PHE A 480 ? 0.8419 0.5991 0.8379 -0.0776 0.1434  -0.0584 575  PHE A CG  
3603 C CD1 . PHE A 480 ? 0.8391 0.6149 0.8396 -0.0797 0.1399  -0.0517 575  PHE A CD1 
3604 C CD2 . PHE A 480 ? 0.8393 0.5973 0.8315 -0.0839 0.1414  -0.0713 575  PHE A CD2 
3605 C CE1 . PHE A 480 ? 0.8174 0.6129 0.8203 -0.0872 0.1342  -0.0574 575  PHE A CE1 
3606 C CE2 . PHE A 480 ? 0.8068 0.5846 0.8002 -0.0917 0.1350  -0.0767 575  PHE A CE2 
3607 C CZ  . PHE A 480 ? 0.8081 0.6048 0.8077 -0.0931 0.1314  -0.0696 575  PHE A CZ  
3608 N N   . ASN A 481 ? 0.8865 0.5571 0.8849 -0.0631 0.1659  -0.0435 576  ASN A N   
3609 C CA  . ASN A 481 ? 0.9294 0.5832 0.9296 -0.0540 0.1698  -0.0320 576  ASN A CA  
3610 C C   . ASN A 481 ? 0.8920 0.5596 0.8918 -0.0408 0.1660  -0.0233 576  ASN A C   
3611 O O   . ASN A 481 ? 0.9214 0.5881 0.9223 -0.0355 0.1657  -0.0107 576  ASN A O   
3612 C CB  . ASN A 481 ? 0.9349 0.5801 0.9373 -0.0607 0.1723  -0.0225 576  ASN A CB  
3613 C CG  . ASN A 481 ? 1.0419 0.6711 1.0459 -0.0739 0.1768  -0.0306 576  ASN A CG  
3614 O OD1 . ASN A 481 ? 1.0571 0.6627 1.0613 -0.0733 0.1819  -0.0352 576  ASN A OD1 
3615 N ND2 . ASN A 481 ? 1.0680 0.7101 1.0740 -0.0859 0.1750  -0.0329 576  ASN A ND2 
3616 N N   . LEU A 482 ? 0.8891 0.5697 0.8869 -0.0358 0.1631  -0.0302 577  LEU A N   
3617 C CA  . LEU A 482 ? 0.9103 0.6037 0.9084 -0.0236 0.1598  -0.0236 577  LEU A CA  
3618 C C   . LEU A 482 ? 0.9253 0.6033 0.9255 -0.0131 0.1639  -0.0248 577  LEU A C   
3619 O O   . LEU A 482 ? 0.8602 0.5209 0.8602 -0.0154 0.1688  -0.0337 577  LEU A O   
3620 C CB  . LEU A 482 ? 0.8604 0.5787 0.8556 -0.0244 0.1542  -0.0293 577  LEU A CB  
3621 C CG  . LEU A 482 ? 0.8585 0.5951 0.8532 -0.0335 0.1497  -0.0286 577  LEU A CG  
3622 C CD1 . LEU A 482 ? 0.7984 0.5562 0.7901 -0.0333 0.1444  -0.0348 577  LEU A CD1 
3623 C CD2 . LEU A 482 ? 0.8658 0.6088 0.8625 -0.0309 0.1481  -0.0153 577  LEU A CD2 
3624 N N   . ASP A 483 ? 0.9440 0.6285 0.9468 -0.0015 0.1618  -0.0160 578  ASP A N   
3625 C CA  . ASP A 483 ? 0.9340 0.6058 0.9412 0.0099  0.1653  -0.0153 578  ASP A CA  
3626 C C   . ASP A 483 ? 0.9155 0.5995 0.9217 0.0140  0.1649  -0.0246 578  ASP A C   
3627 O O   . ASP A 483 ? 0.9432 0.6471 0.9494 0.0188  0.1603  -0.0212 578  ASP A O   
3628 C CB  . ASP A 483 ? 0.9572 0.6302 0.9686 0.0202  0.1628  -0.0008 578  ASP A CB  
3629 C CG  . ASP A 483 ? 0.9947 0.6515 1.0129 0.0317  0.1667  0.0011  578  ASP A CG  
3630 O OD1 . ASP A 483 ? 0.9682 0.6188 0.9880 0.0335  0.1710  -0.0096 578  ASP A OD1 
3631 O OD2 . ASP A 483 ? 1.0074 0.6580 1.0293 0.0389  0.1654  0.0132  578  ASP A OD2 
3632 N N   . ALA A 484 ? 0.8830 0.5544 0.8879 0.0120  0.1701  -0.0364 579  ALA A N   
3633 C CA  . ALA A 484 ? 0.9215 0.6029 0.9238 0.0152  0.1707  -0.0458 579  ALA A CA  
3634 C C   . ALA A 484 ? 1.0327 0.7186 1.0419 0.0291  0.1713  -0.0403 579  ALA A C   
3635 O O   . ALA A 484 ? 0.9987 0.7009 1.0065 0.0324  0.1696  -0.0435 579  ALA A O   
3636 C CB  . ALA A 484 ? 0.8760 0.5407 0.8746 0.0102  0.1770  -0.0598 579  ALA A CB  
3637 N N   . ASN A 485 ? 1.0455 0.7178 1.0626 0.0371  0.1733  -0.0315 580  ASN A N   
3638 C CA  . ASN A 485 ? 1.0660 0.7433 1.0916 0.0505  0.1732  -0.0259 580  ASN A CA  
3639 C C   . ASN A 485 ? 1.0610 0.7625 1.0867 0.0535  0.1658  -0.0173 580  ASN A C   
3640 O O   . ASN A 485 ? 1.1237 0.8369 1.1544 0.0619  0.1651  -0.0166 580  ASN A O   
3641 C CB  . ASN A 485 ? 1.0752 0.7328 1.1093 0.0583  0.1758  -0.0172 580  ASN A CB  
3642 C CG  . ASN A 485 ? 1.1134 0.7451 1.1483 0.0559  0.1836  -0.0256 580  ASN A CG  
3643 O OD1 . ASN A 485 ? 1.1712 0.7987 1.2066 0.0574  0.1891  -0.0371 580  ASN A OD1 
3644 N ND2 . ASN A 485 ? 1.1699 0.7835 1.2043 0.0516  0.1846  -0.0201 580  ASN A ND2 
3645 N N   . LYS A 486 ? 0.9673 0.6764 0.9881 0.0467  0.1608  -0.0111 581  LYS A N   
3646 C CA  . LYS A 486 ? 0.9620 0.6937 0.9817 0.0482  0.1540  -0.0044 581  LYS A CA  
3647 C C   . LYS A 486 ? 0.9207 0.6703 0.9345 0.0429  0.1520  -0.0130 581  LYS A C   
3648 O O   . LYS A 486 ? 0.9121 0.6807 0.9251 0.0441  0.1467  -0.0086 581  LYS A O   
3649 C CB  . LYS A 486 ? 0.9870 0.7194 1.0037 0.0432  0.1501  0.0054  581  LYS A CB  
3650 C CG  . LYS A 486 ? 1.0645 0.7824 1.0862 0.0500  0.1506  0.0169  581  LYS A CG  
3651 C CD  . LYS A 486 ? 1.1048 0.8212 1.1216 0.0438  0.1480  0.0262  581  LYS A CD  
3652 C CE  . LYS A 486 ? 1.1054 0.8152 1.1252 0.0522  0.1457  0.0402  581  LYS A CE  
3653 N NZ  . LYS A 486 ? 1.1626 0.8530 1.1898 0.0611  0.1495  0.0415  581  LYS A NZ  
3654 N N   . LEU A 487 ? 0.9122 0.6557 0.9213 0.0371  0.1559  -0.0250 582  LEU A N   
3655 C CA  . LEU A 487 ? 0.8845 0.6434 0.8865 0.0318  0.1538  -0.0331 582  LEU A CA  
3656 C C   . LEU A 487 ? 0.8558 0.6117 0.8566 0.0352  0.1589  -0.0432 582  LEU A C   
3657 O O   . LEU A 487 ? 0.7929 0.5584 0.7859 0.0302  0.1580  -0.0510 582  LEU A O   
3658 C CB  . LEU A 487 ? 0.8320 0.5898 0.8268 0.0191  0.1522  -0.0385 582  LEU A CB  
3659 C CG  . LEU A 487 ? 0.8326 0.5980 0.8275 0.0138  0.1472  -0.0303 582  LEU A CG  
3660 C CD1 . LEU A 487 ? 0.7854 0.5411 0.7771 0.0021  0.1485  -0.0356 582  LEU A CD1 
3661 C CD2 . LEU A 487 ? 0.7331 0.5222 0.7254 0.0129  0.1409  -0.0283 582  LEU A CD2 
3662 N N   . ASN A 488 ? 0.8449 0.5880 0.8531 0.0437  0.1644  -0.0430 583  ASN A N   
3663 C CA  . ASN A 488 ? 0.8454 0.5829 0.8529 0.0467  0.1711  -0.0536 583  ASN A CA  
3664 C C   . ASN A 488 ? 0.7689 0.5257 0.7715 0.0470  0.1694  -0.0574 583  ASN A C   
3665 O O   . ASN A 488 ? 0.7803 0.5369 0.7734 0.0414  0.1719  -0.0681 583  ASN A O   
3666 C CB  . ASN A 488 ? 0.9318 0.6574 0.9514 0.0582  0.1763  -0.0502 583  ASN A CB  
3667 C CG  . ASN A 488 ? 0.9763 0.7167 1.0055 0.0681  0.1720  -0.0392 583  ASN A CG  
3668 O OD1 . ASN A 488 ? 0.9506 0.7028 0.9790 0.0667  0.1649  -0.0301 583  ASN A OD1 
3669 N ND2 . ASN A 488 ? 0.9696 0.7102 1.0082 0.0780  0.1765  -0.0405 583  ASN A ND2 
3670 N N   . PHE A 489 ? 0.7670 0.5403 0.7748 0.0529  0.1649  -0.0487 584  PHE A N   
3671 C CA  . PHE A 489 ? 0.7693 0.5601 0.7733 0.0536  0.1637  -0.0515 584  PHE A CA  
3672 C C   . PHE A 489 ? 0.7811 0.5792 0.7718 0.0430  0.1601  -0.0573 584  PHE A C   
3673 O O   . PHE A 489 ? 0.7750 0.5758 0.7575 0.0403  0.1628  -0.0660 584  PHE A O   
3674 C CB  . PHE A 489 ? 0.7498 0.5568 0.7615 0.0601  0.1583  -0.0406 584  PHE A CB  
3675 C CG  . PHE A 489 ? 0.8267 0.6423 0.8355 0.0551  0.1505  -0.0330 584  PHE A CG  
3676 C CD1 . PHE A 489 ? 0.8122 0.6174 0.8232 0.0534  0.1490  -0.0273 584  PHE A CD1 
3677 C CD2 . PHE A 489 ? 0.7916 0.6252 0.7955 0.0521  0.1452  -0.0315 584  PHE A CD2 
3678 C CE1 . PHE A 489 ? 0.7943 0.6075 0.8026 0.0487  0.1429  -0.0208 584  PHE A CE1 
3679 C CE2 . PHE A 489 ? 0.7820 0.6237 0.7840 0.0478  0.1387  -0.0251 584  PHE A CE2 
3680 C CZ  . PHE A 489 ? 0.7925 0.6244 0.7967 0.0461  0.1378  -0.0200 584  PHE A CZ  
3681 N N   . TYR A 490 ? 0.7588 0.5593 0.7473 0.0367  0.1544  -0.0529 585  TYR A N   
3682 C CA  . TYR A 490 ? 0.7416 0.5496 0.7194 0.0268  0.1502  -0.0579 585  TYR A CA  
3683 C C   . TYR A 490 ? 0.7066 0.5011 0.6762 0.0202  0.1547  -0.0699 585  TYR A C   
3684 O O   . TYR A 490 ? 0.7401 0.5404 0.6997 0.0159  0.1544  -0.0775 585  TYR A O   
3685 C CB  . TYR A 490 ? 0.7571 0.5692 0.7367 0.0218  0.1443  -0.0508 585  TYR A CB  
3686 C CG  . TYR A 490 ? 0.6982 0.5157 0.6696 0.0111  0.1400  -0.0559 585  TYR A CG  
3687 C CD1 . TYR A 490 ? 0.6586 0.4939 0.6250 0.0089  0.1346  -0.0560 585  TYR A CD1 
3688 C CD2 . TYR A 490 ? 0.7155 0.5207 0.6854 0.0032  0.1412  -0.0602 585  TYR A CD2 
3689 C CE1 . TYR A 490 ? 0.6453 0.4868 0.6057 -0.0003 0.1299  -0.0601 585  TYR A CE1 
3690 C CE2 . TYR A 490 ? 0.6931 0.5051 0.6573 -0.0068 0.1366  -0.0648 585  TYR A CE2 
3691 C CZ  . TYR A 490 ? 0.6753 0.5058 0.6351 -0.0082 0.1308  -0.0645 585  TYR A CZ  
3692 O OH  . TYR A 490 ? 0.6753 0.5135 0.6308 -0.0174 0.1256  -0.0687 585  TYR A OH  
3693 N N   . ILE A 491 ? 0.7141 0.4899 0.6873 0.0194  0.1591  -0.0719 586  ILE A N   
3694 C CA  . ILE A 491 ? 0.7564 0.5179 0.7217 0.0127  0.1637  -0.0842 586  ILE A CA  
3695 C C   . ILE A 491 ? 0.8077 0.5683 0.7683 0.0168  0.1696  -0.0924 586  ILE A C   
3696 O O   . ILE A 491 ? 0.8022 0.5615 0.7509 0.0103  0.1708  -0.1030 586  ILE A O   
3697 C CB  . ILE A 491 ? 0.7979 0.5375 0.7693 0.0124  0.1684  -0.0843 586  ILE A CB  
3698 C CG1 . ILE A 491 ? 0.7791 0.5195 0.7538 0.0068  0.1632  -0.0764 586  ILE A CG1 
3699 C CG2 . ILE A 491 ? 0.7718 0.4947 0.7357 0.0063  0.1743  -0.0982 586  ILE A CG2 
3700 C CD1 . ILE A 491 ? 0.8285 0.5488 0.8115 0.0097  0.1675  -0.0717 586  ILE A CD1 
3701 N N   . ASP A 492 ? 0.8662 0.6287 0.8356 0.0276  0.1732  -0.0877 587  ASP A N   
3702 C CA  . ASP A 492 ? 0.8446 0.6041 0.8107 0.0313  0.1806  -0.0964 587  ASP A CA  
3703 C C   . ASP A 492 ? 0.8467 0.6231 0.8017 0.0281  0.1777  -0.0992 587  ASP A C   
3704 O O   . ASP A 492 ? 0.8577 0.6313 0.8039 0.0270  0.1833  -0.1088 587  ASP A O   
3705 C CB  . ASP A 492 ? 0.8758 0.6331 0.8564 0.0437  0.1857  -0.0911 587  ASP A CB  
3706 C CG  . ASP A 492 ? 0.9853 0.7387 0.9643 0.0479  0.1948  -0.1005 587  ASP A CG  
3707 O OD1 . ASP A 492 ? 1.0630 0.8302 1.0455 0.0536  0.1957  -0.0979 587  ASP A OD1 
3708 O OD2 . ASP A 492 ? 1.0904 0.8271 1.0645 0.0451  0.2015  -0.1110 587  ASP A OD2 
3709 N N   . SER A 493 ? 0.7697 0.5627 0.7239 0.0258  0.1691  -0.0914 588  SER A N   
3710 C CA  . SER A 493 ? 0.7549 0.5627 0.6980 0.0225  0.1659  -0.0937 588  SER A CA  
3711 C C   . SER A 493 ? 0.7831 0.5872 0.7105 0.0119  0.1643  -0.1038 588  SER A C   
3712 O O   . SER A 493 ? 0.7518 0.5652 0.6677 0.0091  0.1627  -0.1071 588  SER A O   
3713 C CB  . SER A 493 ? 0.7527 0.5781 0.6995 0.0231  0.1573  -0.0830 588  SER A CB  
3714 O OG  . SER A 493 ? 0.7216 0.5481 0.6661 0.0155  0.1506  -0.0816 588  SER A OG  
3715 N N   . PHE A 494 ? 0.7631 0.5536 0.6895 0.0059  0.1647  -0.1087 589  PHE A N   
3716 C CA  . PHE A 494 ? 0.7601 0.5468 0.6720 -0.0046 0.1631  -0.1193 589  PHE A CA  
3717 C C   . PHE A 494 ? 0.8092 0.5792 0.7136 -0.0054 0.1723  -0.1318 589  PHE A C   
3718 O O   . PHE A 494 ? 0.8306 0.5965 0.7214 -0.0142 0.1714  -0.1419 589  PHE A O   
3719 C CB  . PHE A 494 ? 0.7463 0.5291 0.6607 -0.0127 0.1576  -0.1186 589  PHE A CB  
3720 C CG  . PHE A 494 ? 0.7114 0.5105 0.6319 -0.0133 0.1489  -0.1079 589  PHE A CG  
3721 C CD1 . PHE A 494 ? 0.7186 0.5309 0.6315 -0.0209 0.1407  -0.1091 589  PHE A CD1 
3722 C CD2 . PHE A 494 ? 0.7066 0.5076 0.6406 -0.0063 0.1487  -0.0969 589  PHE A CD2 
3723 C CE1 . PHE A 494 ? 0.7343 0.5616 0.6539 -0.0211 0.1333  -0.0997 589  PHE A CE1 
3724 C CE2 . PHE A 494 ? 0.7233 0.5388 0.6623 -0.0071 0.1413  -0.0877 589  PHE A CE2 
3725 C CZ  . PHE A 494 ? 0.6885 0.5170 0.6207 -0.0143 0.1340  -0.0893 589  PHE A CZ  
3726 N N   . ALA A 495 ? 0.8102 0.5706 0.7233 0.0035  0.1810  -0.1318 590  ALA A N   
3727 C CA  . ALA A 495 ? 0.8542 0.5964 0.7628 0.0033  0.1908  -0.1439 590  ALA A CA  
3728 C C   . ALA A 495 ? 0.8752 0.6213 0.7709 0.0038  0.1962  -0.1520 590  ALA A C   
3729 O O   . ALA A 495 ? 0.8830 0.6145 0.7732 0.0035  0.2051  -0.1632 590  ALA A O   
3730 C CB  . ALA A 495 ? 0.8469 0.5761 0.7723 0.0131  0.1979  -0.1402 590  ALA A CB  
3731 N N   . TYR A 496 ? 0.8132 0.5777 0.7035 0.0045  0.1916  -0.1469 591  TYR A N   
3732 C CA  . TYR A 496 ? 0.8394 0.6074 0.7157 0.0042  0.1969  -0.1541 591  TYR A CA  
3733 C C   . TYR A 496 ? 0.8428 0.6231 0.7019 -0.0046 0.1879  -0.1547 591  TYR A C   
3734 O O   . TYR A 496 ? 0.8055 0.5989 0.6581 -0.0030 0.1867  -0.1512 591  TYR A O   
3735 C CB  . TYR A 496 ? 0.8312 0.6083 0.7176 0.0146  0.2021  -0.1477 591  TYR A CB  
3736 C CG  . TYR A 496 ? 0.8529 0.6231 0.7608 0.0243  0.2066  -0.1422 591  TYR A CG  
3737 C CD1 . TYR A 496 ? 0.8993 0.6534 0.8125 0.0288  0.2174  -0.1501 591  TYR A CD1 
3738 C CD2 . TYR A 496 ? 0.8412 0.6206 0.7639 0.0289  0.1997  -0.1291 591  TYR A CD2 
3739 C CE1 . TYR A 496 ? 0.9014 0.6491 0.8347 0.0382  0.2208  -0.1444 591  TYR A CE1 
3740 C CE2 . TYR A 496 ? 0.8519 0.6251 0.7932 0.0378  0.2029  -0.1235 591  TYR A CE2 
3741 C CZ  . TYR A 496 ? 0.8889 0.6463 0.8357 0.0426  0.2131  -0.1309 591  TYR A CZ  
3742 O OH  . TYR A 496 ? 0.9387 0.6900 0.9044 0.0519  0.2156  -0.1246 591  TYR A OH  
3743 N N   . SER A 497 ? 0.8140 0.5899 0.6669 -0.0138 0.1815  -0.1588 592  SER A N   
3744 C CA  . SER A 497 ? 0.8111 0.5975 0.6497 -0.0230 0.1715  -0.1598 592  SER A CA  
3745 C C   . SER A 497 ? 0.8145 0.6172 0.6633 -0.0216 0.1613  -0.1467 592  SER A C   
3746 O O   . SER A 497 ? 0.7845 0.5933 0.6471 -0.0132 0.1624  -0.1369 592  SER A O   
3747 C CB  . SER A 497 ? 0.8424 0.6346 0.6614 -0.0251 0.1730  -0.1650 592  SER A CB  
3748 O OG  . SER A 497 ? 0.8423 0.6489 0.6649 -0.0184 0.1721  -0.1551 592  SER A OG  
3749 N N   . SER A 498 ? 0.8228 0.6327 0.6656 -0.0299 0.1514  -0.1469 593  SER A N   
3750 C CA  . SER A 498 ? 0.7806 0.6060 0.6326 -0.0294 0.1419  -0.1357 593  SER A CA  
3751 C C   . SER A 498 ? 0.7953 0.6320 0.6339 -0.0375 0.1320  -0.1378 593  SER A C   
3752 O O   . SER A 498 ? 0.7866 0.6173 0.6153 -0.0462 0.1298  -0.1471 593  SER A O   
3753 C CB  . SER A 498 ? 0.7997 0.6199 0.6674 -0.0303 0.1403  -0.1318 593  SER A CB  
3754 O OG  . SER A 498 ? 0.7580 0.5935 0.6334 -0.0306 0.1313  -0.1221 593  SER A OG  
3755 N N   . TYR A 499 ? 0.7529 0.6055 0.5911 -0.0346 0.1260  -0.1292 594  TYR A N   
3756 C CA  . TYR A 499 ? 0.7386 0.6035 0.5665 -0.0409 0.1155  -0.1291 594  TYR A CA  
3757 C C   . TYR A 499 ? 0.7656 0.6359 0.6043 -0.0462 0.1074  -0.1267 594  TYR A C   
3758 O O   . TYR A 499 ? 0.7425 0.6126 0.5977 -0.0427 0.1086  -0.1204 594  TYR A O   
3759 C CB  . TYR A 499 ? 0.7581 0.6375 0.5848 -0.0355 0.1119  -0.1196 594  TYR A CB  
3760 C CG  . TYR A 499 ? 0.7798 0.6564 0.5954 -0.0310 0.1194  -0.1210 594  TYR A CG  
3761 C CD1 . TYR A 499 ? 0.7914 0.6675 0.5858 -0.0358 0.1185  -0.1273 594  TYR A CD1 
3762 C CD2 . TYR A 499 ? 0.8007 0.6761 0.6271 -0.0222 0.1272  -0.1157 594  TYR A CD2 
3763 C CE1 . TYR A 499 ? 0.8025 0.6761 0.5863 -0.0323 0.1263  -0.1284 594  TYR A CE1 
3764 C CE2 . TYR A 499 ? 0.8196 0.6935 0.6371 -0.0185 0.1347  -0.1171 594  TYR A CE2 
3765 C CZ  . TYR A 499 ? 0.8039 0.6767 0.6000 -0.0237 0.1346  -0.1234 594  TYR A CZ  
3766 O OH  . TYR A 499 ? 0.9108 0.7820 0.6975 -0.0206 0.1429  -0.1248 594  TYR A OH  
3767 N N   . PRO A 500 ? 0.7653 0.6408 0.5951 -0.0548 0.0991  -0.1318 595  PRO A N   
3768 C CA  . PRO A 500 ? 0.7455 0.6300 0.5871 -0.0596 0.0907  -0.1285 595  PRO A CA  
3769 C C   . PRO A 500 ? 0.7425 0.6428 0.5949 -0.0534 0.0857  -0.1162 595  PRO A C   
3770 O O   . PRO A 500 ? 0.7442 0.6536 0.5889 -0.0500 0.0825  -0.1121 595  PRO A O   
3771 C CB  . PRO A 500 ? 0.7830 0.6723 0.6111 -0.0692 0.0821  -0.1364 595  PRO A CB  
3772 C CG  . PRO A 500 ? 0.8054 0.6910 0.6130 -0.0684 0.0847  -0.1411 595  PRO A CG  
3773 C CD  . PRO A 500 ? 0.7874 0.6599 0.5963 -0.0612 0.0974  -0.1416 595  PRO A CD  
3774 N N   . HIS A 501 ? 0.7176 0.6201 0.5872 -0.0519 0.0856  -0.1103 596  HIS A N   
3775 C CA  . HIS A 501 ? 0.7008 0.6167 0.5806 -0.0455 0.0822  -0.0991 596  HIS A CA  
3776 C C   . HIS A 501 ? 0.6852 0.6074 0.5809 -0.0481 0.0785  -0.0950 596  HIS A C   
3777 O O   . HIS A 501 ? 0.6864 0.6010 0.5866 -0.0543 0.0798  -0.0998 596  HIS A O   
3778 C CB  . HIS A 501 ? 0.6795 0.5906 0.5627 -0.0358 0.0902  -0.0935 596  HIS A CB  
3779 C CG  . HIS A 501 ? 0.7114 0.6091 0.6042 -0.0334 0.0982  -0.0937 596  HIS A CG  
3780 N ND1 . HIS A 501 ? 0.7120 0.5932 0.5992 -0.0350 0.1055  -0.1020 596  HIS A ND1 
3781 C CD2 . HIS A 501 ? 0.6670 0.5647 0.5742 -0.0289 0.1002  -0.0861 596  HIS A CD2 
3782 C CE1 . HIS A 501 ? 0.6948 0.5664 0.5934 -0.0314 0.1113  -0.0992 596  HIS A CE1 
3783 N NE2 . HIS A 501 ? 0.6715 0.5529 0.5817 -0.0279 0.1080  -0.0894 596  HIS A NE2 
3784 N N   . SER A 502 ? 0.6679 0.6040 0.5717 -0.0439 0.0739  -0.0861 597  SER A N   
3785 C CA  . SER A 502 ? 0.6425 0.5871 0.5613 -0.0455 0.0706  -0.0813 597  SER A CA  
3786 C C   . SER A 502 ? 0.6338 0.5860 0.5605 -0.0370 0.0714  -0.0712 597  SER A C   
3787 O O   . SER A 502 ? 0.6056 0.5582 0.5263 -0.0307 0.0730  -0.0683 597  SER A O   
3788 C CB  . SER A 502 ? 0.6300 0.5884 0.5497 -0.0522 0.0607  -0.0835 597  SER A CB  
3789 O OG  . SER A 502 ? 0.6512 0.6229 0.5688 -0.0475 0.0548  -0.0779 597  SER A OG  
3790 N N   . GLY A 503 ? 0.6235 0.5817 0.5636 -0.0372 0.0704  -0.0661 598  GLY A N   
3791 C CA  . GLY A 503 ? 0.6215 0.5885 0.5686 -0.0299 0.0700  -0.0572 598  GLY A CA  
3792 C C   . GLY A 503 ? 0.6180 0.5942 0.5786 -0.0317 0.0678  -0.0528 598  GLY A C   
3793 O O   . GLY A 503 ? 0.6078 0.5851 0.5734 -0.0390 0.0662  -0.0565 598  GLY A O   
3794 N N   . CYS A 504 ? 0.5988 0.5814 0.5654 -0.0252 0.0683  -0.0452 599  CYS A N   
3795 C CA  . CYS A 504 ? 0.6036 0.5957 0.5823 -0.0260 0.0670  -0.0407 599  CYS A CA  
3796 C C   . CYS A 504 ? 0.5979 0.5910 0.5805 -0.0184 0.0702  -0.0331 599  CYS A C   
3797 O O   . CYS A 504 ? 0.5964 0.5880 0.5736 -0.0123 0.0711  -0.0308 599  CYS A O   
3798 C CB  . CYS A 504 ? 0.5683 0.5767 0.5511 -0.0283 0.0591  -0.0412 599  CYS A CB  
3799 S SG  . CYS A 504 ? 0.6395 0.6571 0.6160 -0.0214 0.0538  -0.0377 599  CYS A SG  
3800 N N   . GLY A 505 ? 0.5664 0.5622 0.5581 -0.0193 0.0720  -0.0293 600  GLY A N   
3801 C CA  . GLY A 505 ? 0.5631 0.5621 0.5588 -0.0132 0.0741  -0.0223 600  GLY A CA  
3802 C C   . GLY A 505 ? 0.5923 0.6052 0.5971 -0.0145 0.0712  -0.0199 600  GLY A C   
3803 O O   . GLY A 505 ? 0.5386 0.5559 0.5495 -0.0209 0.0702  -0.0225 600  GLY A O   
3804 N N   . ILE A 506 ? 0.5433 0.5636 0.5497 -0.0085 0.0701  -0.0154 601  ILE A N   
3805 C CA  . ILE A 506 ? 0.5475 0.5819 0.5623 -0.0082 0.0672  -0.0135 601  ILE A CA  
3806 C C   . ILE A 506 ? 0.5848 0.6200 0.6020 -0.0036 0.0706  -0.0079 601  ILE A C   
3807 O O   . ILE A 506 ? 0.5172 0.5481 0.5294 0.0020  0.0716  -0.0051 601  ILE A O   
3808 C CB  . ILE A 506 ? 0.5313 0.5751 0.5450 -0.0053 0.0610  -0.0142 601  ILE A CB  
3809 C CG1 . ILE A 506 ? 0.5409 0.5849 0.5506 -0.0100 0.0566  -0.0197 601  ILE A CG1 
3810 C CG2 . ILE A 506 ? 0.5435 0.6010 0.5670 -0.0038 0.0586  -0.0120 601  ILE A CG2 
3811 C CD1 . ILE A 506 ? 0.5525 0.6001 0.5556 -0.0062 0.0515  -0.0195 601  ILE A CD1 
3812 N N   . GLY A 507 ? 0.5761 0.6176 0.6010 -0.0061 0.0723  -0.0065 602  GLY A N   
3813 C CA  . GLY A 507 ? 0.5162 0.5598 0.5420 -0.0017 0.0749  -0.0016 602  GLY A CA  
3814 C C   . GLY A 507 ? 0.5256 0.5804 0.5548 0.0030  0.0714  -0.0007 602  GLY A C   
3815 O O   . GLY A 507 ? 0.4613 0.5272 0.4984 0.0011  0.0690  -0.0026 602  GLY A O   
3816 N N   . LEU A 508 ? 0.4899 0.5425 0.5143 0.0090  0.0712  0.0020  603  LEU A N   
3817 C CA  . LEU A 508 ? 0.5097 0.5713 0.5370 0.0133  0.0679  0.0026  603  LEU A CA  
3818 C C   . LEU A 508 ? 0.4927 0.5637 0.5279 0.0132  0.0694  0.0034  603  LEU A C   
3819 O O   . LEU A 508 ? 0.4849 0.5660 0.5275 0.0133  0.0665  0.0017  603  LEU A O   
3820 C CB  . LEU A 508 ? 0.4926 0.5493 0.5138 0.0189  0.0681  0.0053  603  LEU A CB  
3821 C CG  . LEU A 508 ? 0.4978 0.5618 0.5218 0.0235  0.0661  0.0066  603  LEU A CG  
3822 C CD1 . LEU A 508 ? 0.4317 0.5024 0.4585 0.0242  0.0610  0.0048  603  LEU A CD1 
3823 C CD2 . LEU A 508 ? 0.4703 0.5290 0.4888 0.0280  0.0669  0.0091  603  LEU A CD2 
3824 N N   . GLU A 509 ? 0.5002 0.5677 0.5335 0.0135  0.0739  0.0061  604  GLU A N   
3825 C CA  . GLU A 509 ? 0.5019 0.5772 0.5408 0.0132  0.0765  0.0067  604  GLU A CA  
3826 C C   . GLU A 509 ? 0.5182 0.6011 0.5662 0.0078  0.0773  0.0040  604  GLU A C   
3827 O O   . GLU A 509 ? 0.5125 0.6061 0.5690 0.0083  0.0775  0.0027  604  GLU A O   
3828 C CB  . GLU A 509 ? 0.4922 0.5610 0.5250 0.0135  0.0811  0.0103  604  GLU A CB  
3829 C CG  . GLU A 509 ? 0.5131 0.5752 0.5382 0.0187  0.0798  0.0129  604  GLU A CG  
3830 C CD  . GLU A 509 ? 0.5241 0.5749 0.5431 0.0184  0.0800  0.0141  604  GLU A CD  
3831 O OE1 . GLU A 509 ? 0.4939 0.5418 0.5141 0.0148  0.0796  0.0119  604  GLU A OE1 
3832 O OE2 . GLU A 509 ? 0.5179 0.5629 0.5315 0.0218  0.0804  0.0171  604  GLU A OE2 
3833 N N   . ARG A 510 ? 0.5074 0.5854 0.5549 0.0027  0.0779  0.0027  605  ARG A N   
3834 C CA  . ARG A 510 ? 0.5397 0.6253 0.5968 -0.0033 0.0786  -0.0002 605  ARG A CA  
3835 C C   . ARG A 510 ? 0.4972 0.5939 0.5624 -0.0026 0.0724  -0.0036 605  ARG A C   
3836 O O   . ARG A 510 ? 0.5145 0.6233 0.5913 -0.0045 0.0723  -0.0055 605  ARG A O   
3837 C CB  . ARG A 510 ? 0.5437 0.6197 0.5977 -0.0095 0.0806  -0.0010 605  ARG A CB  
3838 C CG  . ARG A 510 ? 0.6666 0.7496 0.7307 -0.0167 0.0836  -0.0031 605  ARG A CG  
3839 C CD  . ARG A 510 ? 0.6923 0.7671 0.7554 -0.0237 0.0845  -0.0053 605  ARG A CD  
3840 N NE  . ARG A 510 ? 0.8017 0.8622 0.8567 -0.0252 0.0903  -0.0016 605  ARG A NE  
3841 C CZ  . ARG A 510 ? 0.8366 0.8884 0.8913 -0.0319 0.0935  -0.0024 605  ARG A CZ  
3842 N NH1 . ARG A 510 ? 0.8551 0.8926 0.9017 -0.0322 0.0983  0.0018  605  ARG A NH1 
3843 N NH2 . ARG A 510 ? 0.7727 0.8304 0.8358 -0.0386 0.0916  -0.0075 605  ARG A NH2 
3844 N N   . VAL A 511 ? 0.4771 0.5704 0.5367 0.0000  0.0672  -0.0043 606  VAL A N   
3845 C CA  . VAL A 511 ? 0.4880 0.5913 0.5538 0.0014  0.0606  -0.0065 606  VAL A CA  
3846 C C   . VAL A 511 ? 0.4966 0.6100 0.5702 0.0064  0.0602  -0.0053 606  VAL A C   
3847 O O   . VAL A 511 ? 0.4803 0.6059 0.5656 0.0060  0.0573  -0.0072 606  VAL A O   
3848 C CB  . VAL A 511 ? 0.5350 0.6317 0.5909 0.0038  0.0557  -0.0066 606  VAL A CB  
3849 C CG1 . VAL A 511 ? 0.5145 0.6212 0.5753 0.0065  0.0487  -0.0074 606  VAL A CG1 
3850 C CG2 . VAL A 511 ? 0.5344 0.6235 0.5849 -0.0019 0.0556  -0.0094 606  VAL A CG2 
3851 N N   . LEU A 512 ? 0.4600 0.5684 0.5278 0.0112  0.0629  -0.0025 607  LEU A N   
3852 C CA  . LEU A 512 ? 0.4899 0.6065 0.5646 0.0160  0.0630  -0.0019 607  LEU A CA  
3853 C C   . LEU A 512 ? 0.4738 0.5995 0.5592 0.0132  0.0678  -0.0034 607  LEU A C   
3854 O O   . LEU A 512 ? 0.4286 0.5657 0.5258 0.0150  0.0663  -0.0051 607  LEU A O   
3855 C CB  . LEU A 512 ? 0.4659 0.5747 0.5316 0.0207  0.0652  0.0008  607  LEU A CB  
3856 C CG  . LEU A 512 ? 0.4787 0.5936 0.5499 0.0257  0.0655  0.0009  607  LEU A CG  
3857 C CD1 . LEU A 512 ? 0.4122 0.5343 0.4908 0.0288  0.0593  0.0000  607  LEU A CD1 
3858 C CD2 . LEU A 512 ? 0.4369 0.5436 0.4986 0.0296  0.0669  0.0032  607  LEU A CD2 
3859 N N   . MET A 513 ? 0.4875 0.6081 0.5692 0.0089  0.0738  -0.0027 608  MET A N   
3860 C CA  . MET A 513 ? 0.4608 0.5890 0.5512 0.0053  0.0795  -0.0039 608  MET A CA  
3861 C C   . MET A 513 ? 0.4870 0.6277 0.5921 0.0017  0.0770  -0.0073 608  MET A C   
3862 O O   . MET A 513 ? 0.4790 0.6319 0.5967 0.0027  0.0785  -0.0092 608  MET A O   
3863 C CB  . MET A 513 ? 0.4712 0.5898 0.5535 0.0002  0.0855  -0.0018 608  MET A CB  
3864 C CG  . MET A 513 ? 0.5180 0.6434 0.6083 -0.0051 0.0920  -0.0028 608  MET A CG  
3865 S SD  . MET A 513 ? 0.5916 0.7039 0.6717 -0.0116 0.0987  0.0005  608  MET A SD  
3866 C CE  . MET A 513 ? 0.6685 0.7780 0.7525 -0.0177 0.0949  -0.0020 608  MET A CE  
3867 N N   . LEU A 514 ? 0.4579 0.5962 0.5621 -0.0024 0.0730  -0.0086 609  LEU A N   
3868 C CA  . LEU A 514 ? 0.4900 0.6403 0.6082 -0.0069 0.0701  -0.0121 609  LEU A CA  
3869 C C   . LEU A 514 ? 0.5058 0.6674 0.6331 -0.0018 0.0627  -0.0134 609  LEU A C   
3870 O O   . LEU A 514 ? 0.4993 0.6754 0.6427 -0.0029 0.0616  -0.0158 609  LEU A O   
3871 C CB  . LEU A 514 ? 0.4994 0.6427 0.6126 -0.0133 0.0678  -0.0137 609  LEU A CB  
3872 C CG  . LEU A 514 ? 0.5340 0.6680 0.6423 -0.0193 0.0756  -0.0126 609  LEU A CG  
3873 C CD1 . LEU A 514 ? 0.5064 0.6284 0.6058 -0.0238 0.0737  -0.0136 609  LEU A CD1 
3874 C CD2 . LEU A 514 ? 0.4732 0.6187 0.5961 -0.0252 0.0804  -0.0147 609  LEU A CD2 
3875 N N   . PHE A 515 ? 0.4532 0.6086 0.5713 0.0039  0.0575  -0.0114 610  PHE A N   
3876 C CA  . PHE A 515 ? 0.4722 0.6367 0.5978 0.0093  0.0506  -0.0115 610  PHE A CA  
3877 C C   . PHE A 515 ? 0.4833 0.6578 0.6213 0.0135  0.0540  -0.0119 610  PHE A C   
3878 O O   . PHE A 515 ? 0.4653 0.6533 0.6186 0.0151  0.0504  -0.0135 610  PHE A O   
3879 C CB  . PHE A 515 ? 0.4762 0.6308 0.5885 0.0147  0.0461  -0.0087 610  PHE A CB  
3880 C CG  . PHE A 515 ? 0.4800 0.6420 0.5984 0.0202  0.0386  -0.0079 610  PHE A CG  
3881 C CD1 . PHE A 515 ? 0.4954 0.6626 0.6158 0.0184  0.0305  -0.0089 610  PHE A CD1 
3882 C CD2 . PHE A 515 ? 0.5192 0.6827 0.6410 0.0270  0.0393  -0.0062 610  PHE A CD2 
3883 C CE1 . PHE A 515 ? 0.5314 0.7051 0.6569 0.0238  0.0229  -0.0073 610  PHE A CE1 
3884 C CE2 . PHE A 515 ? 0.4992 0.6684 0.6269 0.0324  0.0323  -0.0048 610  PHE A CE2 
3885 C CZ  . PHE A 515 ? 0.4964 0.6707 0.6258 0.0309  0.0240  -0.0050 610  PHE A CZ  
3886 N N   . LEU A 516 ? 0.4873 0.6555 0.6194 0.0154  0.0611  -0.0105 611  LEU A N   
3887 C CA  . LEU A 516 ? 0.4802 0.6569 0.6228 0.0193  0.0653  -0.0116 611  LEU A CA  
3888 C C   . LEU A 516 ? 0.4963 0.6820 0.6499 0.0141  0.0725  -0.0142 611  LEU A C   
3889 O O   . LEU A 516 ? 0.4570 0.6512 0.6209 0.0167  0.0768  -0.0159 611  LEU A O   
3890 C CB  . LEU A 516 ? 0.4637 0.6302 0.5946 0.0237  0.0692  -0.0095 611  LEU A CB  
3891 C CG  . LEU A 516 ? 0.4533 0.6115 0.5748 0.0292  0.0631  -0.0070 611  LEU A CG  
3892 C CD1 . LEU A 516 ? 0.4385 0.5859 0.5472 0.0314  0.0674  -0.0052 611  LEU A CD1 
3893 C CD2 . LEU A 516 ? 0.4075 0.5734 0.5397 0.0353  0.0579  -0.0073 611  LEU A CD2 
3894 N N   . GLY A 517 ? 0.4776 0.6616 0.6298 0.0065  0.0744  -0.0147 612  GLY A N   
3895 C CA  . GLY A 517 ? 0.4937 0.6857 0.6559 0.0009  0.0819  -0.0168 612  GLY A CA  
3896 C C   . GLY A 517 ? 0.5213 0.7069 0.6749 0.0007  0.0914  -0.0155 612  GLY A C   
3897 O O   . GLY A 517 ? 0.4787 0.6723 0.6410 -0.0025 0.0987  -0.0173 612  GLY A O   
3898 N N   . LEU A 518 ? 0.4816 0.6534 0.6181 0.0038  0.0914  -0.0123 613  LEU A N   
3899 C CA  . LEU A 518 ? 0.4786 0.6440 0.6052 0.0036  0.0993  -0.0107 613  LEU A CA  
3900 C C   . LEU A 518 ? 0.5147 0.6756 0.6370 -0.0045 0.1057  -0.0094 613  LEU A C   
3901 O O   . LEU A 518 ? 0.5008 0.6582 0.6229 -0.0093 0.1033  -0.0090 613  LEU A O   
3902 C CB  . LEU A 518 ? 0.4962 0.6486 0.6066 0.0085  0.0965  -0.0076 613  LEU A CB  
3903 C CG  . LEU A 518 ? 0.4777 0.6335 0.5920 0.0161  0.0914  -0.0087 613  LEU A CG  
3904 C CD1 . LEU A 518 ? 0.4326 0.5761 0.5323 0.0200  0.0881  -0.0057 613  LEU A CD1 
3905 C CD2 . LEU A 518 ? 0.4486 0.6127 0.5707 0.0190  0.0969  -0.0114 613  LEU A CD2 
3906 N N   . ASN A 519 ? 0.4783 0.6385 0.5963 -0.0061 0.1140  -0.0087 614  ASN A N   
3907 C CA  . ASN A 519 ? 0.5194 0.6770 0.6354 -0.0140 0.1213  -0.0074 614  ASN A CA  
3908 C C   . ASN A 519 ? 0.5341 0.6746 0.6313 -0.0159 0.1224  -0.0022 614  ASN A C   
3909 O O   . ASN A 519 ? 0.5292 0.6651 0.6233 -0.0226 0.1280  -0.0002 614  ASN A O   
3910 C CB  . ASN A 519 ? 0.5159 0.6820 0.6367 -0.0155 0.1307  -0.0092 614  ASN A CB  
3911 C CG  . ASN A 519 ? 0.5716 0.7291 0.6759 -0.0122 0.1346  -0.0068 614  ASN A CG  
3912 O OD1 . ASN A 519 ? 0.5315 0.6804 0.6249 -0.0069 0.1292  -0.0048 614  ASN A OD1 
3913 N ND2 . ASN A 519 ? 0.6329 0.7931 0.7351 -0.0157 0.1441  -0.0071 614  ASN A ND2 
3914 N N   . ASN A 520 ? 0.5208 0.6518 0.6061 -0.0103 0.1174  0.0002  615  ASN A N   
3915 C CA  . ASN A 520 ? 0.5129 0.6287 0.5814 -0.0112 0.1187  0.0053  615  ASN A CA  
3916 C C   . ASN A 520 ? 0.5453 0.6530 0.6063 -0.0055 0.1111  0.0067  615  ASN A C   
3917 O O   . ASN A 520 ? 0.5264 0.6380 0.5886 0.0004  0.1074  0.0052  615  ASN A O   
3918 C CB  . ASN A 520 ? 0.5332 0.6472 0.5920 -0.0108 0.1251  0.0073  615  ASN A CB  
3919 C CG  . ASN A 520 ? 0.5338 0.6332 0.5764 -0.0129 0.1272  0.0133  615  ASN A CG  
3920 O OD1 . ASN A 520 ? 0.5390 0.6289 0.5727 -0.0092 0.1222  0.0161  615  ASN A OD1 
3921 N ND2 . ASN A 520 ? 0.5207 0.6185 0.5596 -0.0187 0.1349  0.0155  615  ASN A ND2 
3922 N N   . ILE A 521 ? 0.5402 0.6362 0.5936 -0.0074 0.1094  0.0097  616  ILE A N   
3923 C CA  . ILE A 521 ? 0.5070 0.5952 0.5537 -0.0025 0.1033  0.0110  616  ILE A CA  
3924 C C   . ILE A 521 ? 0.5232 0.6076 0.5602 0.0031  0.1027  0.0135  616  ILE A C   
3925 O O   . ILE A 521 ? 0.5103 0.5923 0.5447 0.0080  0.0976  0.0135  616  ILE A O   
3926 C CB  . ILE A 521 ? 0.5404 0.6161 0.5812 -0.0058 0.1031  0.0134  616  ILE A CB  
3927 C CG1 . ILE A 521 ? 0.5578 0.6274 0.5947 -0.0014 0.0970  0.0133  616  ILE A CG1 
3928 C CG2 . ILE A 521 ? 0.5031 0.5685 0.5328 -0.0072 0.1078  0.0188  616  ILE A CG2 
3929 C CD1 . ILE A 521 ? 0.5668 0.6426 0.6122 -0.0022 0.0924  0.0089  616  ILE A CD1 
3930 N N   . ARG A 522 ? 0.4951 0.5791 0.5261 0.0021  0.1078  0.0155  617  ARG A N   
3931 C CA  . ARG A 522 ? 0.5279 0.6092 0.5497 0.0070  0.1066  0.0172  617  ARG A CA  
3932 C C   . ARG A 522 ? 0.5377 0.6280 0.5658 0.0116  0.1041  0.0131  617  ARG A C   
3933 O O   . ARG A 522 ? 0.5202 0.6082 0.5419 0.0159  0.1019  0.0137  617  ARG A O   
3934 C CB  . ARG A 522 ? 0.5017 0.5800 0.5138 0.0043  0.1125  0.0204  617  ARG A CB  
3935 C CG  . ARG A 522 ? 0.5186 0.5852 0.5227 0.0006  0.1143  0.0259  617  ARG A CG  
3936 C CD  . ARG A 522 ? 0.5603 0.6249 0.5566 -0.0041 0.1215  0.0290  617  ARG A CD  
3937 N NE  . ARG A 522 ? 0.5638 0.6169 0.5542 -0.0082 0.1236  0.0343  617  ARG A NE  
3938 C CZ  . ARG A 522 ? 0.5831 0.6345 0.5810 -0.0132 0.1256  0.0335  617  ARG A CZ  
3939 N NH1 . ARG A 522 ? 0.5432 0.6047 0.5552 -0.0149 0.1250  0.0277  617  ARG A NH1 
3940 N NH2 . ARG A 522 ? 0.6119 0.6511 0.6034 -0.0168 0.1279  0.0388  617  ARG A NH2 
3941 N N   . LYS A 523 ? 0.4716 0.5719 0.5126 0.0111  0.1040  0.0089  618  LYS A N   
3942 C CA  . LYS A 523 ? 0.4884 0.5959 0.5361 0.0160  0.1011  0.0055  618  LYS A CA  
3943 C C   . LYS A 523 ? 0.5038 0.6083 0.5523 0.0200  0.0940  0.0056  618  LYS A C   
3944 O O   . LYS A 523 ? 0.4552 0.5627 0.5065 0.0245  0.0913  0.0039  618  LYS A O   
3945 C CB  . LYS A 523 ? 0.4669 0.5869 0.5293 0.0147  0.1036  0.0013  618  LYS A CB  
3946 C CG  . LYS A 523 ? 0.4733 0.5983 0.5358 0.0122  0.1117  -0.0001 618  LYS A CG  
3947 C CD  . LYS A 523 ? 0.4954 0.6338 0.5748 0.0108  0.1144  -0.0045 618  LYS A CD  
3948 C CE  . LYS A 523 ? 0.4991 0.6429 0.5787 0.0088  0.1234  -0.0066 618  LYS A CE  
3949 N NZ  . LYS A 523 ? 0.4693 0.6080 0.5401 0.0021  0.1295  -0.0034 618  LYS A NZ  
3950 N N   . THR A 524 ? 0.4594 0.5577 0.5053 0.0181  0.0913  0.0075  619  THR A N   
3951 C CA  . THR A 524 ? 0.4383 0.5337 0.4839 0.0213  0.0852  0.0075  619  THR A CA  
3952 C C   . THR A 524 ? 0.4613 0.5455 0.4963 0.0224  0.0838  0.0108  619  THR A C   
3953 O O   . THR A 524 ? 0.4375 0.5183 0.4715 0.0239  0.0799  0.0108  619  THR A O   
3954 C CB  . THR A 524 ? 0.4760 0.5755 0.5296 0.0185  0.0825  0.0054  619  THR A CB  
3955 O OG1 . THR A 524 ? 0.4677 0.5622 0.5190 0.0131  0.0852  0.0064  619  THR A OG1 
3956 C CG2 . THR A 524 ? 0.4666 0.5789 0.5333 0.0184  0.0828  0.0021  619  THR A CG2 
3957 N N   . SER A 525 ? 0.4515 0.5302 0.4786 0.0218  0.0870  0.0137  620  SER A N   
3958 C CA  . SER A 525 ? 0.4942 0.5638 0.5125 0.0240  0.0854  0.0170  620  SER A CA  
3959 C C   . SER A 525 ? 0.4893 0.5601 0.5028 0.0271  0.0857  0.0178  620  SER A C   
3960 O O   . SER A 525 ? 0.4895 0.5634 0.5013 0.0255  0.0893  0.0177  620  SER A O   
3961 C CB  . SER A 525 ? 0.4823 0.5436 0.4954 0.0205  0.0882  0.0203  620  SER A CB  
3962 O OG  . SER A 525 ? 0.5366 0.5898 0.5420 0.0233  0.0870  0.0241  620  SER A OG  
3963 N N   . LEU A 526 ? 0.4865 0.5549 0.4976 0.0311  0.0821  0.0184  621  LEU A N   
3964 C CA  . LEU A 526 ? 0.4825 0.5531 0.4905 0.0337  0.0815  0.0180  621  LEU A CA  
3965 C C   . LEU A 526 ? 0.5066 0.5742 0.5059 0.0324  0.0838  0.0208  621  LEU A C   
3966 O O   . LEU A 526 ? 0.5132 0.5847 0.5100 0.0319  0.0860  0.0194  621  LEU A O   
3967 C CB  . LEU A 526 ? 0.4471 0.5153 0.4546 0.0374  0.0774  0.0183  621  LEU A CB  
3968 C CG  . LEU A 526 ? 0.5014 0.5734 0.5149 0.0399  0.0751  0.0154  621  LEU A CG  
3969 C CD1 . LEU A 526 ? 0.4485 0.5168 0.4604 0.0426  0.0720  0.0166  621  LEU A CD1 
3970 C CD2 . LEU A 526 ? 0.4204 0.4978 0.4360 0.0406  0.0764  0.0124  621  LEU A CD2 
3971 N N   . PHE A 527 ? 0.4835 0.5440 0.4775 0.0322  0.0832  0.0250  622  PHE A N   
3972 C CA  . PHE A 527 ? 0.4839 0.5405 0.4685 0.0313  0.0844  0.0290  622  PHE A CA  
3973 C C   . PHE A 527 ? 0.5333 0.5833 0.5164 0.0282  0.0870  0.0324  622  PHE A C   
3974 O O   . PHE A 527 ? 0.5007 0.5435 0.4823 0.0297  0.0851  0.0356  622  PHE A O   
3975 C CB  . PHE A 527 ? 0.4987 0.5527 0.4789 0.0350  0.0801  0.0314  622  PHE A CB  
3976 C CG  . PHE A 527 ? 0.5253 0.5853 0.5082 0.0375  0.0776  0.0275  622  PHE A CG  
3977 C CD1 . PHE A 527 ? 0.5159 0.5800 0.4944 0.0368  0.0787  0.0254  622  PHE A CD1 
3978 C CD2 . PHE A 527 ? 0.4882 0.5489 0.4777 0.0401  0.0748  0.0257  622  PHE A CD2 
3979 C CE1 . PHE A 527 ? 0.4938 0.5621 0.4750 0.0387  0.0767  0.0215  622  PHE A CE1 
3980 C CE2 . PHE A 527 ? 0.5229 0.5879 0.5151 0.0419  0.0729  0.0225  622  PHE A CE2 
3981 C CZ  . PHE A 527 ? 0.4903 0.5589 0.4788 0.0412  0.0738  0.0202  622  PHE A CZ  
3982 N N   . PRO A 528 ? 0.4840 0.5362 0.4685 0.0238  0.0916  0.0314  623  PRO A N   
3983 C CA  . PRO A 528 ? 0.4683 0.5144 0.4535 0.0200  0.0943  0.0336  623  PRO A CA  
3984 C C   . PRO A 528 ? 0.5479 0.5837 0.5237 0.0200  0.0947  0.0400  623  PRO A C   
3985 O O   . PRO A 528 ? 0.5277 0.5627 0.4947 0.0209  0.0946  0.0432  623  PRO A O   
3986 C CB  . PRO A 528 ? 0.5228 0.5753 0.5114 0.0152  0.0997  0.0312  623  PRO A CB  
3987 C CG  . PRO A 528 ? 0.5337 0.5964 0.5267 0.0174  0.0990  0.0264  623  PRO A CG  
3988 C CD  . PRO A 528 ? 0.5137 0.5743 0.4999 0.0221  0.0950  0.0278  623  PRO A CD  
3989 N N   . ARG A 529 ? 0.5243 0.5519 0.5018 0.0189  0.0949  0.0418  624  ARG A N   
3990 C CA  . ARG A 529 ? 0.5575 0.5737 0.5277 0.0185  0.0958  0.0482  624  ARG A CA  
3991 C C   . ARG A 529 ? 0.5608 0.5724 0.5317 0.0121  0.1013  0.0491  624  ARG A C   
3992 O O   . ARG A 529 ? 0.5440 0.5555 0.5227 0.0096  0.1021  0.0454  624  ARG A O   
3993 C CB  . ARG A 529 ? 0.5677 0.5765 0.5400 0.0228  0.0922  0.0495  624  ARG A CB  
3994 C CG  . ARG A 529 ? 0.5752 0.5870 0.5464 0.0289  0.0872  0.0502  624  ARG A CG  
3995 C CD  . ARG A 529 ? 0.6137 0.6230 0.5752 0.0304  0.0860  0.0561  624  ARG A CD  
3996 N NE  . ARG A 529 ? 0.6071 0.6213 0.5687 0.0355  0.0808  0.0560  624  ARG A NE  
3997 C CZ  . ARG A 529 ? 0.6100 0.6332 0.5701 0.0358  0.0794  0.0531  624  ARG A CZ  
3998 N NH1 . ARG A 529 ? 0.6383 0.6670 0.5970 0.0319  0.0829  0.0500  624  ARG A NH1 
3999 N NH2 . ARG A 529 ? 0.5538 0.5807 0.5146 0.0400  0.0746  0.0530  624  ARG A NH2 
4000 N N   . ASP A 530 ? 0.5816 0.5894 0.5441 0.0092  0.1049  0.0539  625  ASP A N   
4001 C CA  . ASP A 530 ? 0.5936 0.5951 0.5563 0.0027  0.1105  0.0556  625  ASP A CA  
4002 C C   . ASP A 530 ? 0.6463 0.6356 0.5970 0.0026  0.1118  0.0642  625  ASP A C   
4003 O O   . ASP A 530 ? 0.6142 0.6025 0.5573 0.0076  0.1079  0.0680  625  ASP A O   
4004 C CB  . ASP A 530 ? 0.6240 0.6363 0.5915 -0.0028 0.1156  0.0513  625  ASP A CB  
4005 C CG  . ASP A 530 ? 0.6531 0.6704 0.6116 -0.0031 0.1182  0.0532  625  ASP A CG  
4006 O OD1 . ASP A 530 ? 0.6556 0.6647 0.6018 -0.0037 0.1197  0.0599  625  ASP A OD1 
4007 O OD2 . ASP A 530 ? 0.6587 0.6880 0.6222 -0.0029 0.1190  0.0478  625  ASP A OD2 
4008 N N   . PRO A 531 ? 0.6487 0.6285 0.5974 -0.0028 0.1168  0.0678  626  PRO A N   
4009 C CA  . PRO A 531 ? 0.6960 0.6619 0.6329 -0.0020 0.1172  0.0770  626  PRO A CA  
4010 C C   . PRO A 531 ? 0.7178 0.6865 0.6418 -0.0011 0.1172  0.0817  626  PRO A C   
4011 O O   . PRO A 531 ? 0.7486 0.7078 0.6623 0.0020  0.1147  0.0895  626  PRO A O   
4012 C CB  . PRO A 531 ? 0.6991 0.6558 0.6371 -0.0097 0.1239  0.0789  626  PRO A CB  
4013 C CG  . PRO A 531 ? 0.6960 0.6589 0.6482 -0.0124 0.1244  0.0704  626  PRO A CG  
4014 C CD  . PRO A 531 ? 0.6498 0.6296 0.6073 -0.0097 0.1216  0.0639  626  PRO A CD  
4015 N N   . LYS A 532 ? 0.6608 0.6422 0.5848 -0.0034 0.1197  0.0771  627  LYS A N   
4016 C CA  . LYS A 532 ? 0.7261 0.7106 0.6367 -0.0032 0.1204  0.0804  627  LYS A CA  
4017 C C   . LYS A 532 ? 0.7240 0.7194 0.6354 0.0023  0.1148  0.0758  627  LYS A C   
4018 O O   . LYS A 532 ? 0.7652 0.7652 0.6664 0.0021  0.1153  0.0763  627  LYS A O   
4019 C CB  . LYS A 532 ? 0.7624 0.7519 0.6710 -0.0108 0.1291  0.0787  627  LYS A CB  
4020 C CG  . LYS A 532 ? 0.7943 0.7722 0.7004 -0.0173 0.1354  0.0841  627  LYS A CG  
4021 C CD  . LYS A 532 ? 0.8875 0.8717 0.7933 -0.0252 0.1447  0.0820  627  LYS A CD  
4022 C CE  . LYS A 532 ? 0.9788 0.9643 0.8675 -0.0256 0.1471  0.0858  627  LYS A CE  
4023 N NZ  . LYS A 532 ? 1.1140 1.0852 0.9860 -0.0229 0.1432  0.0963  627  LYS A NZ  
4024 N N   . ARG A 533 ? 0.7056 0.7051 0.6284 0.0068  0.1098  0.0710  628  ARG A N   
4025 C CA  . ARG A 533 ? 0.6775 0.6869 0.6023 0.0115  0.1048  0.0663  628  ARG A CA  
4026 C C   . ARG A 533 ? 0.6625 0.6689 0.5926 0.0177  0.0979  0.0669  628  ARG A C   
4027 O O   . ARG A 533 ? 0.5903 0.5967 0.5314 0.0185  0.0972  0.0633  628  ARG A O   
4028 C CB  . ARG A 533 ? 0.6537 0.6751 0.5893 0.0096  0.1075  0.0577  628  ARG A CB  
4029 C CG  . ARG A 533 ? 0.6307 0.6610 0.5694 0.0143  0.1028  0.0527  628  ARG A CG  
4030 C CD  . ARG A 533 ? 0.6222 0.6638 0.5700 0.0125  0.1061  0.0451  628  ARG A CD  
4031 N NE  . ARG A 533 ? 0.6656 0.7108 0.6066 0.0084  0.1123  0.0446  628  ARG A NE  
4032 C CZ  . ARG A 533 ? 0.6606 0.7085 0.5916 0.0093  0.1122  0.0442  628  ARG A CZ  
4033 N NH1 . ARG A 533 ? 0.5717 0.6195 0.4989 0.0140  0.1057  0.0443  628  ARG A NH1 
4034 N NH2 . ARG A 533 ? 0.6382 0.6891 0.5629 0.0051  0.1190  0.0432  628  ARG A NH2 
4035 N N   . LEU A 534 ? 0.6671 0.6719 0.5895 0.0220  0.0927  0.0711  629  LEU A N   
4036 C CA  . LEU A 534 ? 0.6733 0.6780 0.6014 0.0282  0.0861  0.0710  629  LEU A CA  
4037 C C   . LEU A 534 ? 0.6957 0.7109 0.6246 0.0311  0.0819  0.0666  629  LEU A C   
4038 O O   . LEU A 534 ? 0.6707 0.6879 0.6061 0.0357  0.0769  0.0654  629  LEU A O   
4039 C CB  . LEU A 534 ? 0.6782 0.6726 0.5994 0.0315  0.0826  0.0797  629  LEU A CB  
4040 C CG  . LEU A 534 ? 0.7044 0.6969 0.6328 0.0381  0.0766  0.0810  629  LEU A CG  
4041 C CD1 . LEU A 534 ? 0.6438 0.6357 0.5855 0.0387  0.0782  0.0756  629  LEU A CD1 
4042 C CD2 . LEU A 534 ? 0.6879 0.6691 0.6101 0.0410  0.0742  0.0903  629  LEU A CD2 
4043 N N   . ILE A 535 ? 0.6962 0.7182 0.6195 0.0282  0.0843  0.0636  630  ILE A N   
4044 C CA  . ILE A 535 ? 0.6893 0.7201 0.6116 0.0302  0.0809  0.0592  630  ILE A CA  
4045 C C   . ILE A 535 ? 0.7061 0.7450 0.6343 0.0275  0.0854  0.0515  630  ILE A C   
4046 O O   . ILE A 535 ? 0.7284 0.7671 0.6574 0.0234  0.0914  0.0507  630  ILE A O   
4047 C CB  . ILE A 535 ? 0.7284 0.7585 0.6354 0.0297  0.0789  0.0633  630  ILE A CB  
4048 C CG1 . ILE A 535 ? 0.8173 0.8437 0.7138 0.0243  0.0857  0.0661  630  ILE A CG1 
4049 C CG2 . ILE A 535 ? 0.7406 0.7649 0.6442 0.0339  0.0724  0.0704  630  ILE A CG2 
4050 C CD1 . ILE A 535 ? 0.8386 0.8729 0.7320 0.0208  0.0907  0.0596  630  ILE A CD1 
4051 N N   . PRO A 536 ? 0.6805 0.7267 0.6138 0.0297  0.0827  0.0458  631  PRO A N   
4052 C CA  . PRO A 536 ? 0.6777 0.7258 0.6145 0.0342  0.0761  0.0453  631  PRO A CA  
4053 C C   . PRO A 536 ? 0.6989 0.7434 0.6458 0.0371  0.0738  0.0466  631  PRO A C   
4054 O O   . PRO A 536 ? 0.6414 0.6835 0.5944 0.0356  0.0771  0.0458  631  PRO A O   
4055 C CB  . PRO A 536 ? 0.6826 0.7386 0.6243 0.0343  0.0765  0.0378  631  PRO A CB  
4056 C CG  . PRO A 536 ? 0.6519 0.7103 0.5977 0.0310  0.0830  0.0343  631  PRO A CG  
4057 C CD  . PRO A 536 ? 0.6581 0.7117 0.5947 0.0275  0.0870  0.0391  631  PRO A CD  
4058 O OXT . PRO A 536 ? 0.7167 0.7609 0.6659 0.0407  0.0688  0.0482  631  PRO A OXT 
4059 N N   . ASN B 5   ? 1.9143 1.2814 1.5517 -0.1361 0.3257  -0.5072 100  ASN B N   
4060 C CA  . ASN B 5   ? 1.9361 1.3211 1.5824 -0.1254 0.3259  -0.4922 100  ASN B CA  
4061 C C   . ASN B 5   ? 1.9638 1.3700 1.5960 -0.1334 0.3122  -0.4858 100  ASN B C   
4062 O O   . ASN B 5   ? 1.9441 1.3519 1.5825 -0.1400 0.3021  -0.4808 100  ASN B O   
4063 C CB  . ASN B 5   ? 1.8727 1.2505 1.5505 -0.1143 0.3295  -0.4795 100  ASN B CB  
4064 N N   . LEU B 6   ? 1.9623 1.3848 1.5758 -0.1325 0.3120  -0.4857 101  LEU B N   
4065 C CA  . LEU B 6   ? 1.9243 1.3673 1.5215 -0.1396 0.2993  -0.4802 101  LEU B CA  
4066 C C   . LEU B 6   ? 1.9648 1.4236 1.5759 -0.1299 0.2979  -0.4634 101  LEU B C   
4067 O O   . LEU B 6   ? 1.9266 1.4037 1.5239 -0.1333 0.2893  -0.4578 101  LEU B O   
4068 C CB  . LEU B 6   ? 1.9143 1.3658 1.4811 -0.1449 0.2990  -0.4890 101  LEU B CB  
4069 N N   . LYS B 7   ? 1.9690 1.4212 1.6069 -0.1178 0.3058  -0.4549 102  LYS B N   
4070 C CA  . LYS B 7   ? 1.9133 1.3801 1.5652 -0.1084 0.3043  -0.4390 102  LYS B CA  
4071 C C   . LYS B 7   ? 1.8983 1.3713 1.5565 -0.1145 0.2918  -0.4307 102  LYS B C   
4072 O O   . LYS B 7   ? 1.8760 1.3654 1.5367 -0.1110 0.2869  -0.4192 102  LYS B O   
4073 C CB  . LYS B 7   ? 1.9586 1.4169 1.6374 -0.0933 0.3160  -0.4325 102  LYS B CB  
4074 N N   . ASN B 8   ? 1.8625 1.3227 1.5234 -0.1239 0.2867  -0.4365 103  ASN B N   
4075 C CA  . ASN B 8   ? 1.8377 1.3037 1.5054 -0.1305 0.2752  -0.4292 103  ASN B CA  
4076 C C   . ASN B 8   ? 1.7950 1.2809 1.4406 -0.1400 0.2628  -0.4292 103  ASN B C   
4077 O O   . ASN B 8   ? 1.7102 1.2098 1.3609 -0.1399 0.2551  -0.4185 103  ASN B O   
4078 C CB  . ASN B 8   ? 1.8094 1.2573 1.4848 -0.1393 0.2729  -0.4361 103  ASN B CB  
4079 C CG  . ASN B 8   ? 1.8258 1.2707 1.5244 -0.1376 0.2693  -0.4245 103  ASN B CG  
4080 O OD1 . ASN B 8   ? 1.8203 1.2667 1.5368 -0.1253 0.2743  -0.4126 103  ASN B OD1 
4081 N ND2 . ASN B 8   ? 1.7973 1.2384 1.4959 -0.1501 0.2605  -0.4279 103  ASN B ND2 
4082 N N   . GLU B 9   ? 1.8057 1.2936 1.4266 -0.1481 0.2607  -0.4408 104  GLU B N   
4083 C CA  . GLU B 9   ? 1.7871 1.2941 1.3854 -0.1563 0.2489  -0.4404 104  GLU B CA  
4084 C C   . GLU B 9   ? 1.7491 1.2732 1.3444 -0.1467 0.2507  -0.4293 104  GLU B C   
4085 O O   . GLU B 9   ? 1.7270 1.2685 1.3121 -0.1508 0.2400  -0.4233 104  GLU B O   
4086 C CB  . GLU B 9   ? 1.8311 1.3354 1.4031 -0.1659 0.2470  -0.4550 104  GLU B CB  
4087 N N   . ALA B 10  ? 1.7608 1.2807 1.3658 -0.1341 0.2639  -0.4264 105  ALA B N   
4088 C CA  . ALA B 10  ? 1.6897 1.2255 1.2945 -0.1246 0.2665  -0.4155 105  ALA B CA  
4089 C C   . ALA B 10  ? 1.6689 1.2117 1.2954 -0.1183 0.2632  -0.4010 105  ALA B C   
4090 O O   . ALA B 10  ? 1.6106 1.1707 1.2318 -0.1170 0.2573  -0.3919 105  ALA B O   
4091 C CB  . ALA B 10  ? 1.6264 1.1563 1.2359 -0.1136 0.2816  -0.4176 105  ALA B CB  
4092 N N   . THR B 11  ? 1.6800 1.2091 1.3305 -0.1140 0.2671  -0.3986 106  THR B N   
4093 C CA  . THR B 11  ? 1.6439 1.1784 1.3145 -0.1090 0.2634  -0.3853 106  THR B CA  
4094 C C   . THR B 11  ? 1.6092 1.1539 1.2713 -0.1206 0.2489  -0.3835 106  THR B C   
4095 O O   . THR B 11  ? 1.5427 1.1005 1.2105 -0.1178 0.2436  -0.3725 106  THR B O   
4096 C CB  . THR B 11  ? 1.6591 1.1755 1.3555 -0.1031 0.2698  -0.3831 106  THR B CB  
4097 O OG1 . THR B 11  ? 1.7277 1.2310 1.4222 -0.1146 0.2649  -0.3917 106  THR B OG1 
4098 C CG2 . THR B 11  ? 1.6980 1.2041 1.4030 -0.0922 0.2836  -0.3860 106  THR B CG2 
4099 N N   . LYS B 12  ? 1.6135 1.1529 1.2627 -0.1337 0.2421  -0.3944 107  LYS B N   
4100 C CA  . LYS B 12  ? 1.6206 1.1718 1.2613 -0.1454 0.2274  -0.3935 107  LYS B CA  
4101 C C   . LYS B 12  ? 1.5894 1.1619 1.2108 -0.1461 0.2204  -0.3890 107  LYS B C   
4102 O O   . LYS B 12  ? 1.5580 1.1442 1.1780 -0.1511 0.2091  -0.3830 107  LYS B O   
4103 C CB  . LYS B 12  ? 1.6607 1.2035 1.2904 -0.1594 0.2214  -0.4069 107  LYS B CB  
4104 N N   . VAL B 13  ? 1.5850 1.1606 1.1918 -0.1412 0.2269  -0.3914 108  VAL B N   
4105 C CA  . VAL B 13  ? 1.5464 1.1411 1.1356 -0.1403 0.2217  -0.3854 108  VAL B CA  
4106 C C   . VAL B 13  ? 1.5121 1.1158 1.1173 -0.1284 0.2258  -0.3712 108  VAL B C   
4107 O O   . VAL B 13  ? 1.4434 1.0633 1.0427 -0.1292 0.2174  -0.3628 108  VAL B O   
4108 C CB  . VAL B 13  ? 1.5605 1.1548 1.1278 -0.1400 0.2276  -0.3931 108  VAL B CB  
4109 N N   . LEU B 14  ? 1.5084 1.1020 1.1340 -0.1169 0.2382  -0.3680 109  LEU B N   
4110 C CA  . LEU B 14  ? 1.4586 1.0611 1.1004 -0.1051 0.2421  -0.3544 109  LEU B CA  
4111 C C   . LEU B 14  ? 1.4421 1.0492 1.0976 -0.1068 0.2336  -0.3459 109  LEU B C   
4112 O O   . LEU B 14  ? 1.4058 1.0272 1.0635 -0.1025 0.2303  -0.3353 109  LEU B O   
4113 C CB  . LEU B 14  ? 1.4479 1.0389 1.1103 -0.0926 0.2562  -0.3529 109  LEU B CB  
4114 C CG  . LEU B 14  ? 1.4238 1.0140 1.0771 -0.0875 0.2666  -0.3581 109  LEU B CG  
4115 C CD1 . LEU B 14  ? 1.4007 0.9866 1.0786 -0.0730 0.2785  -0.3519 109  LEU B CD1 
4116 C CD2 . LEU B 14  ? 1.4235 1.0314 1.0550 -0.0894 0.2629  -0.3551 109  LEU B CD2 
4117 N N   . GLU B 15  ? 1.4377 1.0327 1.1032 -0.1130 0.2305  -0.3501 110  GLU B N   
4118 C CA  . GLU B 15  ? 1.4431 1.0412 1.1223 -0.1156 0.2230  -0.3428 110  GLU B CA  
4119 C C   . GLU B 15  ? 1.4143 1.0228 1.0781 -0.1299 0.2085  -0.3467 110  GLU B C   
4120 O O   . GLU B 15  ? 1.4321 1.0417 1.1087 -0.1350 0.2007  -0.3429 110  GLU B O   
4121 C CB  . GLU B 15  ? 1.4827 1.0617 1.1842 -0.1138 0.2282  -0.3434 110  GLU B CB  
4122 C CG  . GLU B 15  ? 1.5316 1.1009 1.2503 -0.0992 0.2414  -0.3387 110  GLU B CG  
4123 C CD  . GLU B 15  ? 1.6301 1.1786 1.3675 -0.0979 0.2467  -0.3407 110  GLU B CD  
4124 O OE1 . GLU B 15  ? 1.6592 1.1995 1.4131 -0.0858 0.2564  -0.3359 110  GLU B OE1 
4125 O OE2 . GLU B 15  ? 1.6354 1.1759 1.3712 -0.1092 0.2409  -0.3467 110  GLU B OE2 
4126 N N   . HIS B 16  ? 1.4051 1.0244 1.0445 -0.1353 0.2031  -0.3514 111  HIS B N   
4127 C CA  . HIS B 16  ? 1.4034 1.0321 1.0274 -0.1492 0.1886  -0.3565 111  HIS B CA  
4128 C C   . HIS B 16  ? 1.3840 1.0334 1.0186 -0.1493 0.1755  -0.3421 111  HIS B C   
4129 O O   . HIS B 16  ? 1.3485 1.0137 0.9856 -0.1405 0.1737  -0.3289 111  HIS B O   
4130 C CB  . HIS B 16  ? 1.4308 1.0679 1.0267 -0.1529 0.1853  -0.3619 111  HIS B CB  
4131 C CG  . HIS B 16  ? 1.4360 1.0838 1.0154 -0.1667 0.1696  -0.3669 111  HIS B CG  
4132 N ND1 . HIS B 16  ? 1.4523 1.0921 1.0335 -0.1777 0.1641  -0.3767 111  HIS B ND1 
4133 C CD2 . HIS B 16  ? 1.4386 1.1051 1.0005 -0.1710 0.1576  -0.3629 111  HIS B CD2 
4134 C CE1 . HIS B 16  ? 1.4902 1.1444 1.0564 -0.1882 0.1491  -0.3788 111  HIS B CE1 
4135 N NE2 . HIS B 16  ? 1.4749 1.1453 1.0289 -0.1842 0.1446  -0.3703 111  HIS B NE2 
4136 N N   . VAL B 17  ? 1.3720 1.0238 1.0162 -0.1585 0.1653  -0.3426 112  VAL B N   
4137 C CA  . VAL B 17  ? 1.3445 1.0195 0.9993 -0.1601 0.1500  -0.3290 112  VAL B CA  
4138 C C   . VAL B 17  ? 1.3857 1.0738 1.0176 -0.1716 0.1367  -0.3356 112  VAL B C   
4139 O O   . VAL B 17  ? 1.4613 1.1397 1.0811 -0.1836 0.1345  -0.3506 112  VAL B O   
4140 C CB  . VAL B 17  ? 1.3474 1.0187 1.0275 -0.1634 0.1470  -0.3251 112  VAL B CB  
4141 C CG1 . VAL B 17  ? 1.3474 1.0431 1.0359 -0.1676 0.1306  -0.3144 112  VAL B CG1 
4142 C CG2 . VAL B 17  ? 1.2868 0.9482 0.9896 -0.1509 0.1581  -0.3154 112  VAL B CG2 
4143 N N   . CYS B 18  ? 1.3615 1.0710 0.9870 -0.1679 0.1277  -0.3245 113  CYS B N   
4144 C CA  . CYS B 18  ? 1.4276 1.1524 1.0342 -0.1777 0.1127  -0.3275 113  CYS B CA  
4145 C C   . CYS B 18  ? 1.4660 1.2038 1.0906 -0.1849 0.0989  -0.3230 113  CYS B C   
4146 O O   . CYS B 18  ? 1.4572 1.2030 1.1068 -0.1787 0.0976  -0.3099 113  CYS B O   
4147 C CB  . CYS B 18  ? 1.4105 1.1529 1.0053 -0.1706 0.1081  -0.3160 113  CYS B CB  
4148 S SG  . CYS B 18  ? 1.5003 1.2674 1.0817 -0.1794 0.0863  -0.3124 113  CYS B SG  
4149 N N   . GLU B 19  ? 1.5147 1.2549 1.1265 -0.1985 0.0888  -0.3344 114  GLU B N   
4150 C CA  . GLU B 19  ? 1.5428 1.2960 1.1712 -0.2069 0.0755  -0.3322 114  GLU B CA  
4151 C C   . GLU B 19  ? 1.5608 1.3385 1.1784 -0.2117 0.0575  -0.3279 114  GLU B C   
4152 O O   . GLU B 19  ? 1.5674 1.3605 1.2016 -0.2168 0.0456  -0.3233 114  GLU B O   
4153 C CB  . GLU B 19  ? 1.5879 1.3242 1.2160 -0.2200 0.0773  -0.3491 114  GLU B CB  
4154 C CG  . GLU B 19  ? 1.6111 1.3513 1.2675 -0.2253 0.0725  -0.3455 114  GLU B CG  
4155 C CD  . GLU B 19  ? 1.5990 1.3271 1.2794 -0.2152 0.0853  -0.3364 114  GLU B CD  
4156 O OE1 . GLU B 19  ? 1.6111 1.3482 1.3159 -0.2153 0.0812  -0.3269 114  GLU B OE1 
4157 O OE2 . GLU B 19  ? 1.5629 1.2730 1.2377 -0.2073 0.0995  -0.3388 114  GLU B OE2 
4158 N N   . ASP B 20  ? 1.5584 1.3402 1.1493 -0.2101 0.0555  -0.3290 115  ASP B N   
4159 C CA  . ASP B 20  ? 1.5851 1.3889 1.1631 -0.2142 0.0382  -0.3248 115  ASP B CA  
4160 C C   . ASP B 20  ? 1.5799 1.3856 1.1346 -0.2061 0.0415  -0.3193 115  ASP B C   
4161 O O   . ASP B 20  ? 1.6070 1.3993 1.1350 -0.2093 0.0482  -0.3308 115  ASP B O   
4162 C CB  . ASP B 20  ? 1.6609 1.4638 1.2226 -0.2299 0.0281  -0.3408 115  ASP B CB  
4163 C CG  . ASP B 20  ? 1.6600 1.4873 1.2117 -0.2346 0.0082  -0.3360 115  ASP B CG  
4164 O OD1 . ASP B 20  ? 1.6301 1.4685 1.1705 -0.2268 0.0045  -0.3250 115  ASP B OD1 
4165 O OD2 . ASP B 20  ? 1.7095 1.5447 1.2651 -0.2464 -0.0040 -0.3433 115  ASP B OD2 
4166 N N   . ILE B 21  ? 1.5889 1.4107 1.1536 -0.1960 0.0374  -0.3022 116  ILE B N   
4167 C CA  . ILE B 21  ? 1.5702 1.3931 1.1153 -0.1878 0.0419  -0.2956 116  ILE B CA  
4168 C C   . ILE B 21  ? 1.5688 1.4013 1.0836 -0.1945 0.0293  -0.2987 116  ILE B C   
4169 O O   . ILE B 21  ? 1.5729 1.4019 1.0640 -0.1907 0.0344  -0.2974 116  ILE B O   
4170 C CB  . ILE B 21  ? 1.5014 1.3373 1.0668 -0.1750 0.0420  -0.2765 116  ILE B CB  
4171 C CG1 . ILE B 21  ? 1.5155 1.3753 1.0900 -0.1764 0.0235  -0.2660 116  ILE B CG1 
4172 C CG2 . ILE B 21  ? 1.4145 1.2418 1.0095 -0.1687 0.0530  -0.2730 116  ILE B CG2 
4173 C CD1 . ILE B 21  ? 1.4834 1.3563 1.0652 -0.1646 0.0219  -0.2483 116  ILE B CD1 
4174 N N   . ASN B 22  ? 1.5697 1.4144 1.0842 -0.2045 0.0129  -0.3024 117  ASN B N   
4175 C CA  . ASN B 22  ? 1.6042 1.4572 1.0884 -0.2115 0.0001  -0.3060 117  ASN B CA  
4176 C C   . ASN B 22  ? 1.6273 1.4610 1.0803 -0.2193 0.0086  -0.3238 117  ASN B C   
4177 O O   . ASN B 22  ? 1.6327 1.4654 1.0546 -0.2197 0.0079  -0.3248 117  ASN B O   
4178 C CB  . ASN B 22  ? 1.5910 1.4623 1.0847 -0.2207 -0.0197 -0.3067 117  ASN B CB  
4179 C CG  . ASN B 22  ? 1.5772 1.4626 1.1089 -0.2155 -0.0242 -0.2944 117  ASN B CG  
4180 O OD1 . ASN B 22  ? 1.6124 1.5121 1.1537 -0.2061 -0.0289 -0.2786 117  ASN B OD1 
4181 N ND2 . ASN B 22  ? 1.5769 1.4578 1.1300 -0.2218 -0.0225 -0.3019 117  ASN B ND2 
4182 N N   . LYS B 23  ? 1.6366 1.4539 1.0970 -0.2256 0.0171  -0.3379 118  LYS B N   
4183 C CA  . LYS B 23  ? 1.6634 1.4637 1.1025 -0.2315 0.0240  -0.3532 118  LYS B CA  
4184 C C   . LYS B 23  ? 1.6796 1.4594 1.1178 -0.2227 0.0458  -0.3558 118  LYS B C   
4185 O O   . LYS B 23  ? 1.7043 1.4697 1.1313 -0.2247 0.0534  -0.3665 118  LYS B O   
4186 C CB  . LYS B 23  ? 1.6765 1.4725 1.1281 -0.2426 0.0187  -0.3654 118  LYS B CB  
4187 C CG  . LYS B 23  ? 1.6653 1.4831 1.1239 -0.2515 -0.0027 -0.3630 118  LYS B CG  
4188 C CD  . LYS B 23  ? 1.6483 1.4614 1.1207 -0.2627 -0.0068 -0.3752 118  LYS B CD  
4189 N N   . GLU B 24  ? 1.6403 1.4191 1.0904 -0.2128 0.0557  -0.3463 119  GLU B N   
4190 C CA  . GLU B 24  ? 1.6179 1.3790 1.0728 -0.2035 0.0761  -0.3478 119  GLU B CA  
4191 C C   . GLU B 24  ? 1.5757 1.3431 1.0238 -0.1928 0.0816  -0.3351 119  GLU B C   
4192 O O   . GLU B 24  ? 1.5513 1.3377 0.9985 -0.1903 0.0691  -0.3218 119  GLU B O   
4193 C CB  . GLU B 24  ? 1.6035 1.3542 1.0893 -0.2013 0.0845  -0.3490 119  GLU B CB  
4194 C CG  . GLU B 24  ? 1.6146 1.3424 1.1044 -0.1981 0.1022  -0.3588 119  GLU B CG  
4195 C CD  . GLU B 24  ? 1.6088 1.3256 1.1254 -0.2003 0.1064  -0.3629 119  GLU B CD  
4196 O OE1 . GLU B 24  ? 1.5944 1.3212 1.1234 -0.2075 0.0936  -0.3612 119  GLU B OE1 
4197 O OE2 . GLU B 24  ? 1.6051 1.3048 1.1335 -0.1934 0.1218  -0.3653 119  GLU B OE2 
4198 N N   . SER B 25  ? 1.5304 1.2845 0.9811 -0.1838 0.0995  -0.3355 120  SER B N   
4199 C CA  . SER B 25  ? 1.4626 1.2219 0.9083 -0.1736 0.1064  -0.3239 120  SER B CA  
4200 C C   . SER B 25  ? 1.4242 1.1755 0.8952 -0.1617 0.1222  -0.3183 120  SER B C   
4201 O O   . SER B 25  ? 1.3664 1.1231 0.8381 -0.1524 0.1280  -0.3076 120  SER B O   
4202 C CB  . SER B 25  ? 1.4853 1.2424 0.9044 -0.1726 0.1105  -0.3260 120  SER B CB  
4203 O OG  . SER B 25  ? 1.5244 1.2942 0.9211 -0.1797 0.0941  -0.3240 120  SER B OG  
4204 N N   . TYR B 26  ? 1.4074 1.1464 0.9000 -0.1616 0.1287  -0.3244 121  TYR B N   
4205 C CA  . TYR B 26  ? 1.3435 1.0753 0.8612 -0.1498 0.1426  -0.3184 121  TYR B CA  
4206 C C   . TYR B 26  ? 1.3581 1.0818 0.9023 -0.1514 0.1426  -0.3210 121  TYR B C   
4207 O O   . TYR B 26  ? 1.3824 1.1040 0.9240 -0.1621 0.1341  -0.3296 121  TYR B O   
4208 C CB  . TYR B 26  ? 1.3380 1.0547 0.8448 -0.1450 0.1605  -0.3265 121  TYR B CB  
4209 C CG  . TYR B 26  ? 1.4273 1.1293 0.9283 -0.1508 0.1643  -0.3409 121  TYR B CG  
4210 C CD1 . TYR B 26  ? 1.4285 1.1331 0.9043 -0.1600 0.1559  -0.3482 121  TYR B CD1 
4211 C CD2 . TYR B 26  ? 1.4051 1.0903 0.9256 -0.1468 0.1763  -0.3467 121  TYR B CD2 
4212 C CE1 . TYR B 26  ? 1.4999 1.1909 0.9699 -0.1654 0.1597  -0.3617 121  TYR B CE1 
4213 C CE2 . TYR B 26  ? 1.4645 1.1358 0.9797 -0.1520 0.1801  -0.3598 121  TYR B CE2 
4214 C CZ  . TYR B 26  ? 1.4953 1.1696 0.9851 -0.1614 0.1720  -0.3676 121  TYR B CZ  
4215 O OH  . TYR B 26  ? 1.5724 1.2326 1.0564 -0.1667 0.1759  -0.3810 121  TYR B OH  
4216 N N   . GLY B 27  ? 1.3223 1.0415 0.8921 -0.1406 0.1523  -0.3133 122  GLY B N   
4217 C CA  . GLY B 27  ? 1.3021 1.0119 0.8974 -0.1406 0.1541  -0.3142 122  GLY B CA  
4218 C C   . GLY B 27  ? 1.2928 1.0158 0.9165 -0.1324 0.1491  -0.2965 122  GLY B C   
4219 O O   . GLY B 27  ? 1.2354 0.9776 0.8591 -0.1295 0.1399  -0.2841 122  GLY B O   
4220 N N   . PHE B 28  ? 1.2459 0.9580 0.8935 -0.1284 0.1556  -0.2950 123  PHE B N   
4221 C CA  . PHE B 28  ? 1.2103 0.9338 0.8841 -0.1230 0.1496  -0.2797 123  PHE B CA  
4222 C C   . PHE B 28  ? 1.2314 0.9672 0.9076 -0.1332 0.1339  -0.2786 123  PHE B C   
4223 O O   . PHE B 28  ? 1.2613 0.9894 0.9292 -0.1444 0.1306  -0.2910 123  PHE B O   
4224 C CB  . PHE B 28  ? 1.1876 0.8948 0.8840 -0.1173 0.1600  -0.2791 123  PHE B CB  
4225 C CG  . PHE B 28  ? 1.2014 0.8958 0.8980 -0.1073 0.1756  -0.2815 123  PHE B CG  
4226 C CD1 . PHE B 28  ? 1.1706 0.8753 0.8752 -0.0956 0.1789  -0.2690 123  PHE B CD1 
4227 C CD2 . PHE B 28  ? 1.2402 0.9122 0.9298 -0.1097 0.1870  -0.2966 123  PHE B CD2 
4228 C CE1 . PHE B 28  ? 1.1737 0.8682 0.8804 -0.0864 0.1932  -0.2712 123  PHE B CE1 
4229 C CE2 . PHE B 28  ? 1.2495 0.9104 0.9410 -0.1001 0.2018  -0.2990 123  PHE B CE2 
4230 C CZ  . PHE B 28  ? 1.2253 0.8981 0.9258 -0.0883 0.2048  -0.2862 123  PHE B CZ  
4231 N N   . VAL B 29  ? 1.1693 0.9247 0.8578 -0.1293 0.1243  -0.2639 124  VAL B N   
4232 C CA  . VAL B 29  ? 1.1938 0.9645 0.8851 -0.1380 0.1089  -0.2616 124  VAL B CA  
4233 C C   . VAL B 29  ? 1.1943 0.9774 0.9118 -0.1319 0.1047  -0.2463 124  VAL B C   
4234 O O   . VAL B 29  ? 1.1663 0.9558 0.8912 -0.1210 0.1080  -0.2346 124  VAL B O   
4235 C CB  . VAL B 29  ? 1.2390 1.0250 0.9079 -0.1415 0.0985  -0.2614 124  VAL B CB  
4236 C CG1 . VAL B 29  ? 1.2266 1.0201 0.8917 -0.1303 0.1024  -0.2505 124  VAL B CG1 
4237 C CG2 . VAL B 29  ? 1.2840 1.0895 0.9602 -0.1478 0.0819  -0.2561 124  VAL B CG2 
4238 N N   . LYS B 30  ? 1.2074 0.9932 0.9390 -0.1391 0.0981  -0.2468 125  LYS B N   
4239 C CA  . LYS B 30  ? 1.1948 0.9941 0.9495 -0.1347 0.0930  -0.2329 125  LYS B CA  
4240 C C   . LYS B 30  ? 1.1794 1.0029 0.9306 -0.1346 0.0797  -0.2246 125  LYS B C   
4241 O O   . LYS B 30  ? 1.1832 1.0137 0.9174 -0.1418 0.0710  -0.2310 125  LYS B O   
4242 C CB  . LYS B 30  ? 1.2346 1.0286 1.0057 -0.1429 0.0914  -0.2362 125  LYS B CB  
4243 C CG  . LYS B 30  ? 1.2966 1.0713 1.0822 -0.1376 0.1042  -0.2350 125  LYS B CG  
4244 C CD  . LYS B 30  ? 1.3553 1.1149 1.1470 -0.1482 0.1062  -0.2451 125  LYS B CD  
4245 C CE  . LYS B 30  ? 1.4251 1.1988 1.2336 -0.1551 0.0966  -0.2396 125  LYS B CE  
4246 N NZ  . LYS B 30  ? 1.4449 1.2020 1.2684 -0.1602 0.1027  -0.2423 125  LYS B NZ  
4247 N N   . ILE B 31  ? 1.1773 1.0132 0.9442 -0.1260 0.0780  -0.2102 126  ILE B N   
4248 C CA  . ILE B 31  ? 1.1406 0.9976 0.9040 -0.1231 0.0674  -0.2011 126  ILE B CA  
4249 C C   . ILE B 31  ? 1.1642 1.0356 0.9279 -0.1333 0.0531  -0.2041 126  ILE B C   
4250 O O   . ILE B 31  ? 1.1550 1.0402 0.9066 -0.1343 0.0432  -0.2022 126  ILE B O   
4251 C CB  . ILE B 31  ? 1.1104 0.9766 0.8927 -0.1124 0.0689  -0.1859 126  ILE B CB  
4252 C CG1 . ILE B 31  ? 1.0243 0.9058 0.7983 -0.1063 0.0629  -0.1770 126  ILE B CG1 
4253 C CG2 . ILE B 31  ? 1.1363 1.0114 0.9405 -0.1155 0.0634  -0.1809 126  ILE B CG2 
4254 C CD1 . ILE B 31  ? 0.9961 0.8686 0.7512 -0.1011 0.0710  -0.1793 126  ILE B CD1 
4255 N N   . SER B 32  ? 1.1564 1.0249 0.9339 -0.1411 0.0517  -0.2089 127  SER B N   
4256 C CA  . SER B 32  ? 1.1334 1.0163 0.9133 -0.1515 0.0383  -0.2127 127  SER B CA  
4257 C C   . SER B 32  ? 1.2281 1.1082 0.9832 -0.1601 0.0329  -0.2252 127  SER B C   
4258 O O   . SER B 32  ? 1.2458 1.1426 0.9949 -0.1649 0.0195  -0.2252 127  SER B O   
4259 C CB  . SER B 32  ? 1.1430 1.0212 0.9427 -0.1588 0.0399  -0.2160 127  SER B CB  
4260 O OG  . SER B 32  ? 1.1979 1.0521 0.9928 -0.1621 0.0512  -0.2263 127  SER B OG  
4261 N N   . LYS B 33  ? 1.2343 1.0935 0.9743 -0.1621 0.0430  -0.2361 128  LYS B N   
4262 C CA  . LYS B 33  ? 1.2688 1.1234 0.9832 -0.1707 0.0390  -0.2492 128  LYS B CA  
4263 C C   . LYS B 33  ? 1.3178 1.1824 1.0109 -0.1661 0.0337  -0.2447 128  LYS B C   
4264 O O   . LYS B 33  ? 1.3739 1.2374 1.0437 -0.1733 0.0285  -0.2543 128  LYS B O   
4265 C CB  . LYS B 33  ? 1.2353 1.0639 0.9392 -0.1730 0.0529  -0.2620 128  LYS B CB  
4266 N N   . MET B 34  ? 1.2984 1.1724 0.9982 -0.1547 0.0347  -0.2305 129  MET B N   
4267 C CA  . MET B 34  ? 1.3647 1.2458 1.0440 -0.1498 0.0313  -0.2255 129  MET B CA  
4268 C C   . MET B 34  ? 1.4291 1.3324 1.1076 -0.1532 0.0136  -0.2200 129  MET B C   
4269 O O   . MET B 34  ? 1.4081 1.3266 1.1002 -0.1463 0.0081  -0.2069 129  MET B O   
4270 C CB  . MET B 34  ? 1.2916 1.1719 0.9784 -0.1366 0.0406  -0.2134 129  MET B CB  
4271 C CG  . MET B 34  ? 1.3057 1.1845 0.9682 -0.1321 0.0434  -0.2118 129  MET B CG  
4272 S SD  . MET B 34  ? 1.3958 1.2495 1.0409 -0.1325 0.0609  -0.2250 129  MET B SD  
4273 C CE  . MET B 34  ? 1.3146 1.1594 0.9900 -0.1240 0.0733  -0.2196 129  MET B CE  
4274 N N   . LYS B 35  ? 1.5349 1.4399 1.1967 -0.1641 0.0044  -0.2307 130  LYS B N   
4275 C CA  . LYS B 35  ? 1.5900 1.5159 1.2495 -0.1685 -0.0137 -0.2272 130  LYS B CA  
4276 C C   . LYS B 35  ? 1.6201 1.5430 1.2456 -0.1746 -0.0191 -0.2356 130  LYS B C   
4277 O O   . LYS B 35  ? 1.6246 1.5417 1.2392 -0.1858 -0.0224 -0.2494 130  LYS B O   
4278 C CB  . LYS B 35  ? 1.5418 1.4766 1.2221 -0.1775 -0.0222 -0.2317 130  LYS B CB  
4279 C CG  . LYS B 35  ? 1.5105 1.4539 1.2237 -0.1718 -0.0205 -0.2212 130  LYS B CG  
4280 C CD  . LYS B 35  ? 1.5373 1.5058 1.2623 -0.1689 -0.0351 -0.2100 130  LYS B CD  
4281 N N   . GLU B 36  ? 1.6730 1.5996 1.2813 -0.1677 -0.0201 -0.2273 131  GLU B N   
4282 C CA  . GLU B 36  ? 1.6810 1.6051 1.2548 -0.1728 -0.0252 -0.2334 131  GLU B CA  
4283 C C   . GLU B 36  ? 1.7637 1.7079 1.3348 -0.1787 -0.0459 -0.2312 131  GLU B C   
4284 O O   . GLU B 36  ? 1.7926 1.7502 1.3592 -0.1732 -0.0553 -0.2193 131  GLU B O   
4285 C CB  . GLU B 36  ? 1.6588 1.5784 1.2153 -0.1634 -0.0175 -0.2249 131  GLU B CB  
4286 C CG  . GLU B 36  ? 1.7265 1.6383 1.2444 -0.1690 -0.0181 -0.2331 131  GLU B CG  
4287 C CD  . GLU B 36  ? 1.6765 1.5891 1.1767 -0.1607 -0.0149 -0.2220 131  GLU B CD  
4288 O OE1 . GLU B 36  ? 1.6686 1.5945 1.1826 -0.1527 -0.0209 -0.2070 131  GLU B OE1 
4289 O OE2 . GLU B 36  ? 1.6077 1.5073 1.0801 -0.1623 -0.0060 -0.2287 131  GLU B OE2 
4290 N N   . ASN B 37  ? 1.6673 1.6131 1.2415 -0.1903 -0.0532 -0.2430 132  ASN B N   
4291 C CA  . ASN B 37  ? 1.6017 1.5673 1.1763 -0.1973 -0.0734 -0.2430 132  ASN B CA  
4292 C C   . ASN B 37  ? 1.5972 1.5842 1.1995 -0.1897 -0.0829 -0.2274 132  ASN B C   
4293 O O   . ASN B 37  ? 1.6003 1.5977 1.1954 -0.1826 -0.0900 -0.2155 132  ASN B O   
4294 C CB  . ASN B 37  ? 1.5864 1.5534 1.1245 -0.2007 -0.0825 -0.2450 132  ASN B CB  
4295 N N   . GLU B 40  ? 1.4866 1.5000 1.1360 -0.1418 -0.0750 -0.1666 135  GLU B N   
4296 C CA  . GLU B 40  ? 1.4416 1.4407 1.1013 -0.1360 -0.0571 -0.1659 135  GLU B CA  
4297 C C   . GLU B 40  ? 1.4051 1.3910 1.0416 -0.1300 -0.0466 -0.1628 135  GLU B C   
4298 O O   . GLU B 40  ? 1.3987 1.3871 1.0120 -0.1298 -0.0533 -0.1595 135  GLU B O   
4299 C CB  . GLU B 40  ? 1.4279 1.4375 1.1197 -0.1279 -0.0562 -0.1548 135  GLU B CB  
4300 N N   . ILE B 41  ? 1.3534 1.3256 0.9968 -0.1252 -0.0303 -0.1635 136  ILE B N   
4301 C CA  . ILE B 41  ? 1.2849 1.2435 0.9088 -0.1203 -0.0180 -0.1625 136  ILE B CA  
4302 C C   . ILE B 41  ? 1.2192 1.1841 0.8525 -0.1091 -0.0161 -0.1473 136  ILE B C   
4303 O O   . ILE B 41  ? 1.2086 1.1803 0.8686 -0.1036 -0.0154 -0.1401 136  ILE B O   
4304 C CB  . ILE B 41  ? 1.2221 1.1623 0.8489 -0.1212 -0.0014 -0.1722 136  ILE B CB  
4305 C CG1 . ILE B 41  ? 1.3151 1.2465 0.9278 -0.1328 -0.0025 -0.1884 136  ILE B CG1 
4306 C CG2 . ILE B 41  ? 1.1982 1.1266 0.8112 -0.1145 0.0124  -0.1698 136  ILE B CG2 
4307 C CD1 . ILE B 41  ? 1.2742 1.1853 0.8851 -0.1337 0.0141  -0.1990 136  ILE B CD1 
4308 N N   . ARG B 42  ? 1.1840 1.1462 0.7947 -0.1061 -0.0151 -0.1424 137  ARG B N   
4309 C CA  . ARG B 42  ? 1.1697 1.1353 0.7864 -0.0960 -0.0117 -0.1288 137  ARG B CA  
4310 C C   . ARG B 42  ? 1.1323 1.0832 0.7484 -0.0914 0.0067  -0.1307 137  ARG B C   
4311 O O   . ARG B 42  ? 1.1444 1.0852 0.7369 -0.0923 0.0141  -0.1339 137  ARG B O   
4312 C CB  . ARG B 42  ? 1.1913 1.1618 0.7845 -0.0954 -0.0207 -0.1216 137  ARG B CB  
4313 N N   . LEU B 43  ? 1.1160 1.0660 0.7583 -0.0865 0.0140  -0.1286 138  LEU B N   
4314 C CA  . LEU B 43  ? 1.0735 1.0103 0.7190 -0.0823 0.0308  -0.1314 138  LEU B CA  
4315 C C   . LEU B 43  ? 1.0805 1.0196 0.7303 -0.0730 0.0361  -0.1194 138  LEU B C   
4316 O O   . LEU B 43  ? 1.0722 1.0218 0.7409 -0.0676 0.0310  -0.1093 138  LEU B O   
4317 C CB  . LEU B 43  ? 1.0370 0.9705 0.7074 -0.0820 0.0359  -0.1354 138  LEU B CB  
4318 C CG  . LEU B 43  ? 1.0206 0.9390 0.6937 -0.0787 0.0525  -0.1405 138  LEU B CG  
4319 C CD1 . LEU B 43  ? 0.9982 0.9034 0.6456 -0.0847 0.0590  -0.1529 138  LEU B CD1 
4320 C CD2 . LEU B 43  ? 0.9434 0.8587 0.6410 -0.0784 0.0560  -0.1430 138  LEU B CD2 
4321 N N   . PHE B 44  ? 1.0427 0.9720 0.6756 -0.0714 0.0470  -0.1211 139  PHE B N   
4322 C CA  . PHE B 44  ? 1.0499 0.9800 0.6852 -0.0636 0.0537  -0.1110 139  PHE B CA  
4323 C C   . PHE B 44  ? 1.0157 0.9373 0.6659 -0.0585 0.0688  -0.1133 139  PHE B C   
4324 O O   . PHE B 44  ? 1.0274 0.9384 0.6757 -0.0614 0.0769  -0.1241 139  PHE B O   
4325 C CB  . PHE B 44  ? 1.0764 1.0022 0.6821 -0.0655 0.0558  -0.1104 139  PHE B CB  
4326 C CG  . PHE B 44  ? 1.1429 1.0779 0.7346 -0.0679 0.0408  -0.1038 139  PHE B CG  
4327 C CD1 . PHE B 44  ? 1.1765 1.1192 0.7725 -0.0620 0.0364  -0.0903 139  PHE B CD1 
4328 C CD2 . PHE B 44  ? 1.1708 1.1067 0.7452 -0.0761 0.0309  -0.1111 139  PHE B CD2 
4329 C CE1 . PHE B 44  ? 1.2209 1.1715 0.8046 -0.0636 0.0223  -0.0836 139  PHE B CE1 
4330 C CE2 . PHE B 44  ? 1.2286 1.1736 0.7905 -0.0779 0.0162  -0.1045 139  PHE B CE2 
4331 C CZ  . PHE B 44  ? 1.2629 1.2151 0.8296 -0.0713 0.0119  -0.0904 139  PHE B CZ  
4332 N N   . ASN B 45  ? 0.9721 0.8981 0.6371 -0.0507 0.0725  -0.1033 140  ASN B N   
4333 C CA  . ASN B 45  ? 0.9783 0.8973 0.6548 -0.0453 0.0868  -0.1042 140  ASN B CA  
4334 C C   . ASN B 45  ? 0.9766 0.8933 0.6395 -0.0424 0.0947  -0.1000 140  ASN B C   
4335 O O   . ASN B 45  ? 0.9874 0.9089 0.6361 -0.0433 0.0884  -0.0935 140  ASN B O   
4336 C CB  . ASN B 45  ? 0.9459 0.8712 0.6517 -0.0389 0.0862  -0.0970 140  ASN B CB  
4337 C CG  . ASN B 45  ? 0.9637 0.9001 0.6761 -0.0342 0.0795  -0.0842 140  ASN B CG  
4338 O OD1 . ASN B 45  ? 0.9434 0.8797 0.6490 -0.0310 0.0842  -0.0789 140  ASN B OD1 
4339 N ND2 . ASN B 45  ? 0.9788 0.9247 0.7058 -0.0338 0.0690  -0.0795 140  ASN B ND2 
4340 N N   . LEU B 46  ? 0.9704 0.8795 0.6385 -0.0389 0.1089  -0.1035 141  LEU B N   
4341 C CA  . LEU B 46  ? 0.9615 0.8677 0.6169 -0.0370 0.1185  -0.1014 141  LEU B CA  
4342 C C   . LEU B 46  ? 0.9537 0.8690 0.6179 -0.0317 0.1157  -0.0880 141  LEU B C   
4343 O O   . LEU B 46  ? 0.9582 0.8727 0.6078 -0.0318 0.1199  -0.0842 141  LEU B O   
4344 C CB  . LEU B 46  ? 0.9145 0.8121 0.5777 -0.0339 0.1343  -0.1084 141  LEU B CB  
4345 C CG  . LEU B 46  ? 0.9515 0.8379 0.6044 -0.0390 0.1392  -0.1224 141  LEU B CG  
4346 C CD1 . LEU B 46  ? 0.9641 0.8424 0.6283 -0.0344 0.1546  -0.1284 141  LEU B CD1 
4347 C CD2 . LEU B 46  ? 0.9722 0.8543 0.5928 -0.0461 0.1383  -0.1277 141  LEU B CD2 
4348 N N   . GLU B 47  ? 0.9358 0.8590 0.6233 -0.0274 0.1094  -0.0811 142  GLU B N   
4349 C CA  . GLU B 47  ? 0.9353 0.8665 0.6309 -0.0227 0.1061  -0.0690 142  GLU B CA  
4350 C C   . GLU B 47  ? 0.9623 0.8980 0.6404 -0.0259 0.0947  -0.0631 142  GLU B C   
4351 O O   . GLU B 47  ? 1.0079 0.9445 0.6768 -0.0247 0.0959  -0.0559 142  GLU B O   
4352 C CB  . GLU B 47  ? 0.9007 0.8389 0.6242 -0.0177 0.1020  -0.0641 142  GLU B CB  
4353 C CG  . GLU B 47  ? 0.9135 0.8605 0.6467 -0.0133 0.0965  -0.0521 142  GLU B CG  
4354 C CD  . GLU B 47  ? 0.8822 0.8350 0.6424 -0.0082 0.0950  -0.0482 142  GLU B CD  
4355 O OE1 . GLU B 47  ? 0.9503 0.9064 0.7218 -0.0034 0.0986  -0.0417 142  GLU B OE1 
4356 O OE2 . GLU B 47  ? 0.8495 0.8036 0.6195 -0.0092 0.0904  -0.0516 142  GLU B OE2 
4357 N N   . GLU B 48  ? 0.9266 0.8650 0.6001 -0.0302 0.0834  -0.0661 143  GLU B N   
4358 C CA  . GLU B 48  ? 0.9702 0.9131 0.6267 -0.0333 0.0715  -0.0610 143  GLU B CA  
4359 C C   . GLU B 48  ? 1.0522 0.9876 0.6788 -0.0373 0.0763  -0.0632 143  GLU B C   
4360 O O   . GLU B 48  ? 1.0936 1.0309 0.7070 -0.0370 0.0720  -0.0548 143  GLU B O   
4361 C CB  . GLU B 48  ? 1.0155 0.9628 0.6727 -0.0379 0.0594  -0.0658 143  GLU B CB  
4362 C CG  . GLU B 48  ? 1.0177 0.9726 0.7034 -0.0347 0.0546  -0.0640 143  GLU B CG  
4363 C CD  . GLU B 48  ? 1.0482 1.0080 0.7348 -0.0401 0.0433  -0.0692 143  GLU B CD  
4364 O OE1 . GLU B 48  ? 1.0547 1.0101 0.7208 -0.0466 0.0408  -0.0766 143  GLU B OE1 
4365 O OE2 . GLU B 48  ? 1.0452 1.0134 0.7528 -0.0382 0.0369  -0.0661 143  GLU B OE2 
4366 N N   . ILE B 49  ? 1.0235 0.9499 0.6386 -0.0413 0.0855  -0.0745 144  ILE B N   
4367 C CA  . ILE B 49  ? 1.0667 0.9853 0.6522 -0.0456 0.0917  -0.0779 144  ILE B CA  
4368 C C   . ILE B 49  ? 1.1116 1.0286 0.6960 -0.0415 0.1019  -0.0704 144  ILE B C   
4369 O O   . ILE B 49  ? 1.1443 1.0600 0.7074 -0.0435 0.1008  -0.0647 144  ILE B O   
4370 C CB  . ILE B 49  ? 1.0342 0.9429 0.6108 -0.0500 0.1011  -0.0926 144  ILE B CB  
4371 C CG1 . ILE B 49  ? 1.0416 0.9512 0.6143 -0.0558 0.0898  -0.1001 144  ILE B CG1 
4372 C CG2 . ILE B 49  ? 1.0931 0.9932 0.6410 -0.0537 0.1111  -0.0965 144  ILE B CG2 
4373 C CD1 . ILE B 49  ? 1.0509 0.9501 0.6183 -0.0601 0.0985  -0.1150 144  ILE B CD1 
4374 N N   . TYR B 50  ? 1.0496 0.9668 0.6569 -0.0360 0.1120  -0.0701 145  TYR B N   
4375 C CA  . TYR B 50  ? 1.0659 0.9829 0.6755 -0.0324 0.1219  -0.0634 145  TYR B CA  
4376 C C   . TYR B 50  ? 1.1245 1.0476 0.7325 -0.0306 0.1125  -0.0501 145  TYR B C   
4377 O O   . TYR B 50  ? 1.1116 1.0318 0.7025 -0.0319 0.1162  -0.0447 145  TYR B O   
4378 C CB  . TYR B 50  ? 1.0392 0.9579 0.6777 -0.0263 0.1311  -0.0641 145  TYR B CB  
4379 C CG  . TYR B 50  ? 1.0259 0.9461 0.6701 -0.0227 0.1403  -0.0569 145  TYR B CG  
4380 C CD1 . TYR B 50  ? 1.0266 0.9409 0.6600 -0.0240 0.1549  -0.0615 145  TYR B CD1 
4381 C CD2 . TYR B 50  ? 1.0621 0.9897 0.7223 -0.0184 0.1347  -0.0460 145  TYR B CD2 
4382 C CE1 . TYR B 50  ? 1.0360 0.9523 0.6753 -0.0214 0.1635  -0.0551 145  TYR B CE1 
4383 C CE2 . TYR B 50  ? 1.0661 0.9949 0.7317 -0.0158 0.1430  -0.0397 145  TYR B CE2 
4384 C CZ  . TYR B 50  ? 1.0438 0.9672 0.6990 -0.0175 0.1573  -0.0442 145  TYR B CZ  
4385 O OH  . TYR B 50  ? 1.0914 1.0168 0.7531 -0.0156 0.1658  -0.0383 145  TYR B OH  
4386 N N   . HIS B 51  ? 1.0505 0.9815 0.6761 -0.0277 0.1005  -0.0447 146  HIS B N   
4387 C CA  . HIS B 51  ? 1.0871 1.0235 0.7145 -0.0250 0.0922  -0.0321 146  HIS B CA  
4388 C C   . HIS B 51  ? 1.1435 1.0788 0.7441 -0.0294 0.0821  -0.0283 146  HIS B C   
4389 O O   . HIS B 51  ? 1.1996 1.1350 0.7925 -0.0281 0.0797  -0.0181 146  HIS B O   
4390 C CB  . HIS B 51  ? 1.0776 1.0229 0.7321 -0.0205 0.0833  -0.0281 146  HIS B CB  
4391 C CG  . HIS B 51  ? 1.0786 1.0256 0.7580 -0.0153 0.0922  -0.0276 146  HIS B CG  
4392 N ND1 . HIS B 51  ? 1.0970 1.0428 0.7798 -0.0125 0.1010  -0.0220 146  HIS B ND1 
4393 C CD2 . HIS B 51  ? 1.0588 1.0084 0.7603 -0.0126 0.0938  -0.0320 146  HIS B CD2 
4394 C CE1 . HIS B 51  ? 1.1069 1.0554 0.8134 -0.0082 0.1068  -0.0231 146  HIS B CE1 
4395 N NE2 . HIS B 51  ? 1.0579 1.0085 0.7755 -0.0080 0.1026  -0.0288 146  HIS B NE2 
4396 N N   . SER B 52  ? 1.1170 1.0508 0.7026 -0.0346 0.0760  -0.0360 147  SER B N   
4397 C CA  . SER B 52  ? 1.1786 1.1116 0.7370 -0.0389 0.0661  -0.0324 147  SER B CA  
4398 C C   . SER B 52  ? 1.1990 1.1224 0.7288 -0.0427 0.0764  -0.0331 147  SER B C   
4399 O O   . SER B 52  ? 1.2452 1.1671 0.7548 -0.0441 0.0710  -0.0248 147  SER B O   
4400 C CB  . SER B 52  ? 1.1818 1.1170 0.7329 -0.0440 0.0556  -0.0408 147  SER B CB  
4401 O OG  . SER B 52  ? 1.1843 1.1299 0.7567 -0.0411 0.0426  -0.0368 147  SER B OG  
4402 N N   . LEU B 53  ? 1.2075 1.1243 0.7353 -0.0443 0.0914  -0.0427 148  LEU B N   
4403 C CA  . LEU B 53  ? 1.2126 1.1205 0.7132 -0.0483 0.1027  -0.0448 148  LEU B CA  
4404 C C   . LEU B 53  ? 1.2553 1.1616 0.7622 -0.0447 0.1147  -0.0371 148  LEU B C   
4405 O O   . LEU B 53  ? 1.3200 1.2202 0.8027 -0.0480 0.1209  -0.0341 148  LEU B O   
4406 C CB  . LEU B 53  ? 1.2745 1.1754 0.7678 -0.0522 0.1137  -0.0601 148  LEU B CB  
4407 C CG  . LEU B 53  ? 1.2609 1.1614 0.7448 -0.0574 0.1041  -0.0700 148  LEU B CG  
4408 C CD1 . LEU B 53  ? 1.3121 1.2034 0.7859 -0.0614 0.1172  -0.0851 148  LEU B CD1 
4409 C CD2 . LEU B 53  ? 1.2914 1.1928 0.7474 -0.0623 0.0901  -0.0654 148  LEU B CD2 
4410 N N   . MET B 54  ? 1.2664 1.1779 0.8043 -0.0387 0.1181  -0.0340 149  MET B N   
4411 C CA  . MET B 54  ? 1.2838 1.1944 0.8298 -0.0357 0.1299  -0.0278 149  MET B CA  
4412 C C   . MET B 54  ? 1.3090 1.2260 0.8731 -0.0307 0.1215  -0.0151 149  MET B C   
4413 O O   . MET B 54  ? 1.4088 1.3236 0.9602 -0.0313 0.1195  -0.0050 149  MET B O   
4414 C CB  . MET B 54  ? 1.2513 1.1618 0.8181 -0.0330 0.1441  -0.0363 149  MET B CB  
4415 C CG  . MET B 54  ? 1.2251 1.1307 0.7849 -0.0361 0.1494  -0.0507 149  MET B CG  
4416 S SD  . MET B 54  ? 1.4408 1.3360 0.9598 -0.0442 0.1570  -0.0583 149  MET B SD  
4417 C CE  . MET B 54  ? 1.2594 1.1504 0.7865 -0.0427 0.1798  -0.0666 149  MET B CE  
4418 N N   . HIS B 84  ? 1.5310 1.4568 0.9218 -0.0750 0.0086  -0.0443 179  HIS B N   
4419 C CA  . HIS B 84  ? 1.5566 1.4931 0.9666 -0.0758 -0.0050 -0.0491 179  HIS B CA  
4420 C C   . HIS B 84  ? 1.5703 1.5027 0.9846 -0.0809 0.0030  -0.0660 179  HIS B C   
4421 O O   . HIS B 84  ? 1.6108 1.5447 1.0132 -0.0877 -0.0056 -0.0751 179  HIS B O   
4422 C CB  . HIS B 84  ? 1.5905 1.5368 1.0374 -0.0675 -0.0093 -0.0401 179  HIS B CB  
4423 N N   . LEU B 85  ? 1.5464 1.4732 0.9780 -0.0776 0.0194  -0.0702 180  LEU B N   
4424 C CA  . LEU B 85  ? 1.4665 1.3868 0.9024 -0.0814 0.0299  -0.0856 180  LEU B CA  
4425 C C   . LEU B 85  ? 1.5049 1.4139 0.9057 -0.0890 0.0372  -0.0961 180  LEU B C   
4426 O O   . LEU B 85  ? 1.4819 1.3844 0.8826 -0.0931 0.0448  -0.1102 180  LEU B O   
4427 C CB  . LEU B 85  ? 1.4172 1.3340 0.8781 -0.0750 0.0461  -0.0856 180  LEU B CB  
4428 C CG  . LEU B 85  ? 1.3487 1.2743 0.8475 -0.0681 0.0432  -0.0801 180  LEU B CG  
4429 C CD1 . LEU B 85  ? 1.2689 1.1922 0.7827 -0.0610 0.0564  -0.0733 180  LEU B CD1 
4430 C CD2 . LEU B 85  ? 1.3172 1.2421 0.8327 -0.0705 0.0448  -0.0920 180  LEU B CD2 
4431 N N   . LEU B 86  ? 1.5403 1.4460 0.9108 -0.0911 0.0355  -0.0898 181  LEU B N   
4432 C CA  . LEU B 86  ? 1.5688 1.4628 0.9046 -0.0978 0.0454  -0.0987 181  LEU B CA  
4433 C C   . LEU B 86  ? 1.5882 1.4828 0.8924 -0.1061 0.0312  -0.1026 181  LEU B C   
4434 O O   . LEU B 86  ? 1.6216 1.5064 0.8937 -0.1126 0.0382  -0.1109 181  LEU B O   
4435 C CB  . LEU B 86  ? 1.5536 1.4415 0.8755 -0.0948 0.0572  -0.0893 181  LEU B CB  
4436 C CG  . LEU B 86  ? 1.5284 1.4159 0.8801 -0.0871 0.0719  -0.0858 181  LEU B CG  
4437 C CD1 . LEU B 86  ? 1.4914 1.3802 0.8422 -0.0822 0.0731  -0.0696 181  LEU B CD1 
4438 C CD2 . LEU B 86  ? 1.5208 1.3976 0.8674 -0.0891 0.0921  -0.0987 181  LEU B CD2 
4439 N N   . GLN B 87  ? 1.6201 1.5263 0.9324 -0.1061 0.0114  -0.0972 182  GLN B N   
4440 C CA  . GLN B 87  ? 1.6209 1.5293 0.9043 -0.1139 -0.0038 -0.1006 182  GLN B CA  
4441 C C   . GLN B 87  ? 1.6255 1.5306 0.9047 -0.1221 -0.0033 -0.1191 182  GLN B C   
4442 O O   . GLN B 87  ? 1.6262 1.5273 0.8728 -0.1304 -0.0086 -0.1265 182  GLN B O   
4443 C CB  . GLN B 87  ? 1.6108 1.5340 0.9068 -0.1109 -0.0255 -0.0886 182  GLN B CB  
4444 N N   . SER B 88  ? 1.6185 1.5242 0.9289 -0.1202 0.0029  -0.1269 183  SER B N   
4445 C CA  . SER B 88  ? 1.6164 1.5184 0.9260 -0.1278 0.0031  -0.1441 183  SER B CA  
4446 C C   . SER B 88  ? 1.5585 1.4542 0.8963 -0.1242 0.0194  -0.1518 183  SER B C   
4447 O O   . SER B 88  ? 1.5224 1.4165 0.8772 -0.1162 0.0309  -0.1444 183  SER B O   
4448 C CB  . SER B 88  ? 1.6362 1.5518 0.9568 -0.1314 -0.0180 -0.1444 183  SER B CB  
4449 O OG  . SER B 88  ? 1.6557 1.5670 0.9750 -0.1397 -0.0177 -0.1615 183  SER B OG  
4450 N N   . ASP B 89  ? 1.5297 1.4214 0.8720 -0.1303 0.0200  -0.1668 184  ASP B N   
4451 C CA  . ASP B 89  ? 1.4643 1.3496 0.8339 -0.1272 0.0335  -0.1743 184  ASP B CA  
4452 C C   . ASP B 89  ? 1.3944 1.2915 0.8030 -0.1198 0.0276  -0.1639 184  ASP B C   
4453 O O   . ASP B 89  ? 1.3999 1.3104 0.8165 -0.1197 0.0109  -0.1561 184  ASP B O   
4454 C CB  . ASP B 89  ? 1.4746 1.3525 0.8392 -0.1362 0.0339  -0.1924 184  ASP B CB  
4455 C CG  . ASP B 89  ? 1.5146 1.3795 0.8404 -0.1439 0.0413  -0.2046 184  ASP B CG  
4456 O OD1 . ASP B 89  ? 1.5181 1.3754 0.8287 -0.1407 0.0547  -0.2021 184  ASP B OD1 
4457 O OD2 . ASP B 89  ? 1.5146 1.3769 0.8252 -0.1535 0.0342  -0.2171 184  ASP B OD2 
4458 N N   . ILE B 90  ? 1.3546 1.2469 0.7876 -0.1133 0.0416  -0.1638 185  ILE B N   
4459 C CA  . ILE B 90  ? 1.2698 1.1715 0.7394 -0.1063 0.0383  -0.1551 185  ILE B CA  
4460 C C   . ILE B 90  ? 1.2290 1.1223 0.7199 -0.1056 0.0499  -0.1649 185  ILE B C   
4461 O O   . ILE B 90  ? 1.2450 1.1248 0.7244 -0.1083 0.0626  -0.1765 185  ILE B O   
4462 C CB  . ILE B 90  ? 1.2722 1.1784 0.7522 -0.0966 0.0426  -0.1399 185  ILE B CB  
4463 C CG1 . ILE B 90  ? 1.2546 1.1496 0.7390 -0.0920 0.0627  -0.1430 185  ILE B CG1 
4464 C CG2 . ILE B 90  ? 1.3097 1.2200 0.7642 -0.0972 0.0347  -0.1305 185  ILE B CG2 
4465 C CD1 . ILE B 90  ? 1.2559 1.1544 0.7483 -0.0837 0.0682  -0.1294 185  ILE B CD1 
4466 N N   . TRP B 91  ? 1.1873 1.0885 0.7096 -0.1017 0.0454  -0.1599 186  TRP B N   
4467 C CA  . TRP B 91  ? 1.1307 1.0248 0.6767 -0.0995 0.0555  -0.1660 186  TRP B CA  
4468 C C   . TRP B 91  ? 1.1115 1.0074 0.6792 -0.0890 0.0645  -0.1553 186  TRP B C   
4469 O O   . TRP B 91  ? 1.1010 1.0082 0.6780 -0.0838 0.0576  -0.1424 186  TRP B O   
4470 C CB  . TRP B 91  ? 1.1296 1.0307 0.6954 -0.1035 0.0448  -0.1686 186  TRP B CB  
4471 C CG  . TRP B 91  ? 1.1795 1.0766 0.7287 -0.1145 0.0384  -0.1820 186  TRP B CG  
4472 C CD1 . TRP B 91  ? 1.2250 1.1306 0.7562 -0.1212 0.0236  -0.1826 186  TRP B CD1 
4473 C CD2 . TRP B 91  ? 1.2101 1.0937 0.7595 -0.1203 0.0463  -0.1968 186  TRP B CD2 
4474 N NE1 . TRP B 91  ? 1.2772 1.1761 0.7972 -0.1313 0.0214  -0.1974 186  TRP B NE1 
4475 C CE2 . TRP B 91  ? 1.2607 1.1455 0.7915 -0.1311 0.0356  -0.2065 186  TRP B CE2 
4476 C CE3 . TRP B 91  ? 1.1933 1.0637 0.7570 -0.1174 0.0610  -0.2028 186  TRP B CE3 
4477 C CZ2 . TRP B 91  ? 1.3109 1.1834 0.8368 -0.1393 0.0397  -0.2224 186  TRP B CZ2 
4478 C CZ3 . TRP B 91  ? 1.1878 1.0454 0.7469 -0.1250 0.0652  -0.2180 186  TRP B CZ3 
4479 C CH2 . TRP B 91  ? 1.2532 1.1117 0.7936 -0.1361 0.0548  -0.2279 186  TRP B CH2 
4480 N N   . VAL B 92  ? 1.0838 0.9684 0.6598 -0.0858 0.0798  -0.1611 187  VAL B N   
4481 C CA  . VAL B 92  ? 1.0437 0.9293 0.6414 -0.0762 0.0889  -0.1525 187  VAL B CA  
4482 C C   . VAL B 92  ? 1.0419 0.9182 0.6594 -0.0745 0.0984  -0.1598 187  VAL B C   
4483 O O   . VAL B 92  ? 1.0297 0.8937 0.6374 -0.0792 0.1052  -0.1726 187  VAL B O   
4484 C CB  . VAL B 92  ? 1.0317 0.9134 0.6149 -0.0722 0.0997  -0.1492 187  VAL B CB  
4485 C CG1 . VAL B 92  ? 1.0582 0.9258 0.6203 -0.0768 0.1114  -0.1628 187  VAL B CG1 
4486 C CG2 . VAL B 92  ? 1.0256 0.9094 0.6330 -0.0626 0.1086  -0.1408 187  VAL B CG2 
4487 N N   . ARG B 93  ? 0.9864 0.8680 0.6311 -0.0678 0.0987  -0.1515 188  ARG B N   
4488 C CA  . ARG B 93  ? 0.9531 0.8266 0.6185 -0.0649 0.1071  -0.1558 188  ARG B CA  
4489 C C   . ARG B 93  ? 0.9659 0.8368 0.6424 -0.0557 0.1196  -0.1506 188  ARG B C   
4490 O O   . ARG B 93  ? 0.9781 0.8579 0.6570 -0.0507 0.1184  -0.1401 188  ARG B O   
4491 C CB  . ARG B 93  ? 0.9283 0.8098 0.6166 -0.0646 0.0977  -0.1504 188  ARG B CB  
4492 C CG  . ARG B 93  ? 0.9038 0.7775 0.6147 -0.0606 0.1058  -0.1519 188  ARG B CG  
4493 C CD  . ARG B 93  ? 0.8833 0.7645 0.6137 -0.0620 0.0966  -0.1475 188  ARG B CD  
4494 N NE  . ARG B 93  ? 0.8910 0.7719 0.6132 -0.0719 0.0882  -0.1558 188  ARG B NE  
4495 C CZ  . ARG B 93  ? 0.9115 0.8007 0.6470 -0.0754 0.0785  -0.1533 188  ARG B CZ  
4496 N NH1 . ARG B 93  ? 0.8712 0.7694 0.6277 -0.0699 0.0761  -0.1429 188  ARG B NH1 
4497 N NH2 . ARG B 93  ? 0.9412 0.8301 0.6689 -0.0850 0.0713  -0.1619 188  ARG B NH2 
4498 N N   . GLY B 94  ? 0.9405 0.7991 0.6245 -0.0535 0.1315  -0.1581 189  GLY B N   
4499 C CA  . GLY B 94  ? 0.8982 0.7557 0.5955 -0.0445 0.1428  -0.1532 189  GLY B CA  
4500 C C   . GLY B 94  ? 0.9282 0.7721 0.6367 -0.0418 0.1545  -0.1614 189  GLY B C   
4501 O O   . GLY B 94  ? 0.9216 0.7551 0.6257 -0.0473 0.1550  -0.1718 189  GLY B O   
4502 N N   . ARG B 95  ? 0.8949 0.7389 0.6185 -0.0332 0.1639  -0.1568 190  ARG B N   
4503 C CA  . ARG B 95  ? 0.9098 0.7412 0.6454 -0.0290 0.1758  -0.1636 190  ARG B CA  
4504 C C   . ARG B 95  ? 0.9284 0.7517 0.6489 -0.0288 0.1889  -0.1725 190  ARG B C   
4505 O O   . ARG B 95  ? 0.9228 0.7528 0.6324 -0.0279 0.1914  -0.1689 190  ARG B O   
4506 C CB  . ARG B 95  ? 0.9078 0.7440 0.6704 -0.0194 0.1782  -0.1538 190  ARG B CB  
4507 C CG  . ARG B 95  ? 0.8481 0.6844 0.6280 -0.0194 0.1705  -0.1498 190  ARG B CG  
4508 C CD  . ARG B 95  ? 0.8180 0.6592 0.6227 -0.0103 0.1719  -0.1398 190  ARG B CD  
4509 N NE  . ARG B 95  ? 0.8047 0.6429 0.6232 -0.0112 0.1661  -0.1375 190  ARG B NE  
4510 C CZ  . ARG B 95  ? 0.7885 0.6334 0.6256 -0.0060 0.1622  -0.1273 190  ARG B CZ  
4511 N NH1 . ARG B 95  ? 0.7201 0.5758 0.5656 0.0006  0.1626  -0.1184 190  ARG B NH1 
4512 N NH2 . ARG B 95  ? 0.7677 0.6083 0.6149 -0.0078 0.1580  -0.1263 190  ARG B NH2 
4513 N N   . ILE B 96  ? 0.9548 0.7631 0.6745 -0.0298 0.1978  -0.1843 191  ILE B N   
4514 C CA  . ILE B 96  ? 0.9568 0.7560 0.6641 -0.0291 0.2120  -0.1943 191  ILE B CA  
4515 C C   . ILE B 96  ? 0.9524 0.7541 0.6813 -0.0184 0.2223  -0.1889 191  ILE B C   
4516 O O   . ILE B 96  ? 0.9357 0.7307 0.6852 -0.0127 0.2269  -0.1898 191  ILE B O   
4517 C CB  . ILE B 96  ? 0.9864 0.7680 0.6858 -0.0340 0.2178  -0.2096 191  ILE B CB  
4518 C CG1 . ILE B 96  ? 1.0053 0.7860 0.6840 -0.0453 0.2063  -0.2149 191  ILE B CG1 
4519 C CG2 . ILE B 96  ? 1.0025 0.7747 0.6900 -0.0327 0.2338  -0.2203 191  ILE B CG2 
4520 C CD1 . ILE B 96  ? 1.0084 0.7714 0.6770 -0.0517 0.2112  -0.2310 191  ILE B CD1 
4521 N N   . HIS B 97  ? 0.9654 0.7774 0.6902 -0.0157 0.2255  -0.1827 192  HIS B N   
4522 C CA  . HIS B 97  ? 0.9639 0.7809 0.7089 -0.0061 0.2348  -0.1772 192  HIS B CA  
4523 C C   . HIS B 97  ? 0.9442 0.7510 0.6858 -0.0038 0.2516  -0.1887 192  HIS B C   
4524 O O   . HIS B 97  ? 0.9484 0.7534 0.7118 0.0045  0.2605  -0.1887 192  HIS B O   
4525 C CB  . HIS B 97  ? 0.9205 0.7528 0.6627 -0.0052 0.2307  -0.1658 192  HIS B CB  
4526 C CG  . HIS B 97  ? 0.8902 0.7294 0.6515 0.0034  0.2399  -0.1603 192  HIS B CG  
4527 N ND1 . HIS B 97  ? 0.8537 0.7006 0.6416 0.0106  0.2359  -0.1506 192  HIS B ND1 
4528 C CD2 . HIS B 97  ? 0.9157 0.7563 0.6734 0.0055  0.2527  -0.1632 192  HIS B CD2 
4529 C CE1 . HIS B 97  ? 0.8863 0.7391 0.6869 0.0169  0.2452  -0.1479 192  HIS B CE1 
4530 N NE2 . HIS B 97  ? 0.9096 0.7590 0.6931 0.0140  0.2558  -0.1554 192  HIS B NE2 
4531 N N   . ASP B 98  ? 0.9937 0.7939 0.7082 -0.0109 0.2563  -0.1987 193  ASP B N   
4532 C CA  . ASP B 98  ? 1.0311 0.8206 0.7397 -0.0096 0.2729  -0.2111 193  ASP B CA  
4533 C C   . ASP B 98  ? 1.0990 0.8784 0.7808 -0.0194 0.2706  -0.2225 193  ASP B C   
4534 O O   . ASP B 98  ? 1.1158 0.8975 0.7747 -0.0275 0.2614  -0.2220 193  ASP B O   
4535 C CB  . ASP B 98  ? 1.0502 0.8512 0.7593 -0.0064 0.2796  -0.2055 193  ASP B CB  
4536 C CG  . ASP B 98  ? 1.1257 0.9221 0.8410 -0.0032 0.2912  -0.2129 193  ASP B CG  
4537 O OD1 . ASP B 98  ? 1.0969 0.8923 0.8391 0.0054  0.2970  -0.2124 193  ASP B OD1 
4538 O OD2 . ASP B 98  ? 1.1694 0.9632 0.8627 -0.0090 0.2941  -0.2192 193  ASP B OD2 
4539 N N   . ILE B 99  ? 1.1142 0.8828 0.7998 -0.0184 0.2782  -0.2324 194  ILE B N   
4540 C CA  . ILE B 99  ? 1.1901 0.9483 0.8517 -0.0274 0.2768  -0.2442 194  ILE B CA  
4541 C C   . ILE B 99  ? 1.2397 0.9939 0.9017 -0.0247 0.2889  -0.2512 194  ILE B C   
4542 O O   . ILE B 99  ? 1.2142 0.9659 0.9005 -0.0163 0.2974  -0.2516 194  ILE B O   
4543 C CB  . ILE B 99  ? 1.2198 0.9651 0.8845 -0.0311 0.2714  -0.2514 194  ILE B CB  
4544 C CG1 . ILE B 99  ? 1.2409 0.9793 0.8767 -0.0428 0.2657  -0.2616 194  ILE B CG1 
4545 C CG2 . ILE B 99  ? 1.2029 0.9370 0.8921 -0.0238 0.2802  -0.2561 194  ILE B CG2 
4546 C CD1 . ILE B 99  ? 1.2056 0.9357 0.8409 -0.0489 0.2564  -0.2661 194  ILE B CD1 
4547 N N   . ARG B 100 ? 1.3083 1.0627 0.9436 -0.0317 0.2893  -0.2561 195  ARG B N   
4548 C CA  . ARG B 100 ? 1.3094 1.0622 0.9407 -0.0302 0.3008  -0.2619 195  ARG B CA  
4549 C C   . ARG B 100 ? 1.3682 1.1112 0.9711 -0.0398 0.2989  -0.2737 195  ARG B C   
4550 O O   . ARG B 100 ? 1.3425 1.0881 0.9212 -0.0481 0.2889  -0.2727 195  ARG B O   
4551 C CB  . ARG B 100 ? 1.3091 1.0760 0.9357 -0.0284 0.3042  -0.2528 195  ARG B CB  
4552 C CG  . ARG B 100 ? 1.3712 1.1388 1.0005 -0.0249 0.3175  -0.2568 195  ARG B CG  
4553 C CD  . ARG B 100 ? 1.3852 1.1638 0.9962 -0.0281 0.3185  -0.2502 195  ARG B CD  
4554 N NE  . ARG B 100 ? 1.3252 1.1146 0.9372 -0.0281 0.3094  -0.2375 195  ARG B NE  
4555 N N   . SER B 101 ? 1.4247 1.1567 1.0307 -0.0388 0.3080  -0.2847 196  SER B N   
4556 C CA  . SER B 101 ? 1.4615 1.1823 1.0432 -0.0479 0.3058  -0.2971 196  SER B CA  
4557 C C   . SER B 101 ? 1.5146 1.2286 1.0940 -0.0461 0.3190  -0.3068 196  SER B C   
4558 O O   . SER B 101 ? 1.5532 1.2633 1.1572 -0.0379 0.3287  -0.3086 196  SER B O   
4559 C CB  . SER B 101 ? 1.4257 1.1348 1.0147 -0.0507 0.2991  -0.3028 196  SER B CB  
4560 O OG  . SER B 101 ? 1.4514 1.1511 1.0160 -0.0607 0.2950  -0.3143 196  SER B OG  
4561 N N   . LYS B 102 ? 1.5527 1.2653 1.1026 -0.0539 0.3191  -0.3131 197  LYS B N   
4562 C CA  . LYS B 102 ? 1.6043 1.3093 1.1481 -0.0537 0.3314  -0.3239 197  LYS B CA  
4563 C C   . LYS B 102 ? 1.6119 1.3128 1.1192 -0.0647 0.3267  -0.3319 197  LYS B C   
4564 O O   . LYS B 102 ? 1.5968 1.3072 1.0830 -0.0692 0.3210  -0.3256 197  LYS B O   
4565 C CB  . LYS B 102 ? 1.5437 1.2584 1.0979 -0.0464 0.3433  -0.3183 197  LYS B CB  
4566 N N   . GLY B 103 ? 1.7245 1.4115 1.2246 -0.0688 0.3289  -0.3455 198  GLY B N   
4567 C CA  . GLY B 103 ? 1.7282 1.4105 1.1944 -0.0793 0.3245  -0.3544 198  GLY B CA  
4568 C C   . GLY B 103 ? 1.7415 1.4252 1.1913 -0.0881 0.3073  -0.3526 198  GLY B C   
4569 O O   . GLY B 103 ? 1.7837 1.4598 1.2435 -0.0901 0.3011  -0.3568 198  GLY B O   
4570 N N   . SER B 104 ? 1.6747 1.3685 1.1000 -0.0934 0.2993  -0.3462 199  SER B N   
4571 C CA  . SER B 104 ? 1.6594 1.3570 1.0684 -0.1016 0.2819  -0.3435 199  SER B CA  
4572 C C   . SER B 104 ? 1.6079 1.3202 1.0199 -0.0992 0.2739  -0.3276 199  SER B C   
4573 O O   . SER B 104 ? 1.5580 1.2757 0.9550 -0.1056 0.2591  -0.3235 199  SER B O   
4574 C CB  . SER B 104 ? 1.6700 1.3652 1.0430 -0.1116 0.2766  -0.3512 199  SER B CB  
4575 O OG  . SER B 104 ? 1.6917 1.3945 1.0472 -0.1109 0.2816  -0.3457 199  SER B OG  
4576 N N   . LEU B 105 ? 1.5734 1.2925 1.0049 -0.0901 0.2828  -0.3184 200  LEU B N   
4577 C CA  . LEU B 105 ? 1.5485 1.2809 0.9861 -0.0870 0.2765  -0.3033 200  LEU B CA  
4578 C C   . LEU B 105 ? 1.4642 1.1974 0.9361 -0.0790 0.2781  -0.2982 200  LEU B C   
4579 O O   . LEU B 105 ? 1.4711 1.1987 0.9655 -0.0720 0.2896  -0.3021 200  LEU B O   
4580 C CB  . LEU B 105 ? 1.5058 1.2470 0.9368 -0.0835 0.2848  -0.2956 200  LEU B CB  
4581 N N   . ALA B 106 ? 1.4006 1.1407 0.8764 -0.0800 0.2661  -0.2894 201  ALA B N   
4582 C CA  . ALA B 106 ? 1.3740 1.1157 0.8801 -0.0729 0.2661  -0.2835 201  ALA B CA  
4583 C C   . ALA B 106 ? 1.3214 1.0770 0.8305 -0.0701 0.2603  -0.2686 201  ALA B C   
4584 O O   . ALA B 106 ? 1.3051 1.0670 0.7931 -0.0763 0.2490  -0.2638 201  ALA B O   
4585 C CB  . ALA B 106 ? 1.3198 1.0534 0.8307 -0.0775 0.2571  -0.2896 201  ALA B CB  
4586 N N   . PHE B 107 ? 1.2823 1.0430 0.8180 -0.0607 0.2676  -0.2610 202  PHE B N   
4587 C CA  . PHE B 107 ? 1.2626 1.0362 0.8038 -0.0572 0.2637  -0.2469 202  PHE B CA  
4588 C C   . PHE B 107 ? 1.2281 1.0028 0.7958 -0.0519 0.2604  -0.2420 202  PHE B C   
4589 O O   . PHE B 107 ? 1.2084 0.9787 0.8014 -0.0447 0.2686  -0.2441 202  PHE B O   
4590 C CB  . PHE B 107 ? 1.2849 1.0657 0.8329 -0.0512 0.2752  -0.2412 202  PHE B CB  
4591 C CG  . PHE B 107 ? 1.3060 1.0844 0.8299 -0.0558 0.2808  -0.2470 202  PHE B CG  
4592 C CD1 . PHE B 107 ? 1.3045 1.0741 0.8319 -0.0545 0.2919  -0.2581 202  PHE B CD1 
4593 C CD2 . PHE B 107 ? 1.2632 1.0479 0.7606 -0.0615 0.2748  -0.2411 202  PHE B CD2 
4594 C CE1 . PHE B 107 ? 1.3576 1.1248 0.8620 -0.0589 0.2976  -0.2639 202  PHE B CE1 
4595 C CE2 . PHE B 107 ? 1.3088 1.0910 0.7832 -0.0658 0.2800  -0.2461 202  PHE B CE2 
4596 C CZ  . PHE B 107 ? 1.3668 1.1403 0.8444 -0.0647 0.2917  -0.2578 202  PHE B CZ  
4597 N N   . ILE B 108 ? 1.1691 0.9496 0.7307 -0.0553 0.2482  -0.2352 203  ILE B N   
4598 C CA  . ILE B 108 ? 1.1347 0.9176 0.7187 -0.0508 0.2442  -0.2293 203  ILE B CA  
4599 C C   . ILE B 108 ? 1.1267 0.9242 0.7164 -0.0467 0.2406  -0.2142 203  ILE B C   
4600 O O   . ILE B 108 ? 1.1401 0.9444 0.7089 -0.0516 0.2332  -0.2087 203  ILE B O   
4601 C CB  . ILE B 108 ? 1.1543 0.9351 0.7333 -0.0579 0.2295  -0.2316 203  ILE B CB  
4602 C CG1 . ILE B 108 ? 1.1664 0.9308 0.7481 -0.0605 0.2348  -0.2464 203  ILE B CG1 
4603 C CG2 . ILE B 108 ? 1.1163 0.9095 0.7203 -0.0531 0.2171  -0.2169 203  ILE B CG2 
4604 C CD1 . ILE B 108 ? 1.1686 0.9316 0.7448 -0.0687 0.2200  -0.2494 203  ILE B CD1 
4605 N N   . ILE B 109 ? 1.0946 0.8978 0.7141 -0.0374 0.2444  -0.2063 204  ILE B N   
4606 C CA  . ILE B 109 ? 1.0532 0.8714 0.6840 -0.0333 0.2372  -0.1905 204  ILE B CA  
4607 C C   . ILE B 109 ? 1.0285 0.8518 0.6775 -0.0322 0.2224  -0.1831 204  ILE B C   
4608 O O   . ILE B 109 ? 1.0065 0.8251 0.6771 -0.0279 0.2240  -0.1852 204  ILE B O   
4609 C CB  . ILE B 109 ? 1.0421 0.8650 0.6930 -0.0245 0.2499  -0.1860 204  ILE B CB  
4610 C CG1 . ILE B 109 ? 1.0650 0.8861 0.6956 -0.0269 0.2621  -0.1908 204  ILE B CG1 
4611 C CG2 . ILE B 109 ? 0.9989 0.8363 0.6670 -0.0198 0.2412  -0.1701 204  ILE B CG2 
4612 C CD1 . ILE B 109 ? 1.1134 0.9428 0.7647 -0.0192 0.2721  -0.1848 204  ILE B CD1 
4613 N N   . LEU B 110 ? 1.0190 0.8510 0.6578 -0.0365 0.2082  -0.1752 205  LEU B N   
4614 C CA  . LEU B 110 ? 0.9644 0.8024 0.6173 -0.0368 0.1937  -0.1686 205  LEU B CA  
4615 C C   . LEU B 110 ? 0.9686 0.8198 0.6407 -0.0301 0.1894  -0.1538 205  LEU B C   
4616 O O   . LEU B 110 ? 0.9833 0.8411 0.6470 -0.0293 0.1906  -0.1472 205  LEU B O   
4617 C CB  . LEU B 110 ? 0.9842 0.8241 0.6147 -0.0457 0.1804  -0.1700 205  LEU B CB  
4618 C CG  . LEU B 110 ? 1.0061 0.8476 0.6481 -0.0485 0.1678  -0.1696 205  LEU B CG  
4619 C CD1 . LEU B 110 ? 0.9824 0.8098 0.6289 -0.0504 0.1746  -0.1826 205  LEU B CD1 
4620 C CD2 . LEU B 110 ? 1.0206 0.8681 0.6425 -0.0564 0.1534  -0.1684 205  LEU B CD2 
4621 N N   . ARG B 111 ? 0.9317 0.7860 0.6289 -0.0256 0.1845  -0.1488 206  ARG B N   
4622 C CA  . ARG B 111 ? 0.8813 0.7466 0.5996 -0.0184 0.1823  -0.1363 206  ARG B CA  
4623 C C   . ARG B 111 ? 0.8875 0.7605 0.6170 -0.0190 0.1679  -0.1286 206  ARG B C   
4624 O O   . ARG B 111 ? 0.8668 0.7350 0.5988 -0.0224 0.1627  -0.1335 206  ARG B O   
4625 C CB  . ARG B 111 ? 0.8773 0.7393 0.6190 -0.0104 0.1933  -0.1372 206  ARG B CB  
4626 C CG  . ARG B 111 ? 0.8521 0.7255 0.6134 -0.0032 0.1930  -0.1254 206  ARG B CG  
4627 C CD  . ARG B 111 ? 0.8568 0.7276 0.6428 0.0048  0.2014  -0.1259 206  ARG B CD  
4628 N NE  . ARG B 111 ? 0.8461 0.7149 0.6481 0.0064  0.1944  -0.1240 206  ARG B NE  
4629 C CZ  . ARG B 111 ? 0.8648 0.7217 0.6706 0.0062  0.1979  -0.1321 206  ARG B CZ  
4630 N NH1 . ARG B 111 ? 0.8780 0.7238 0.6744 0.0050  0.2087  -0.1433 206  ARG B NH1 
4631 N NH2 . ARG B 111 ? 0.8246 0.6801 0.6439 0.0070  0.1908  -0.1290 206  ARG B NH2 
4632 N N   . HIS B 112 ? 0.8596 0.7443 0.5959 -0.0159 0.1620  -0.1169 207  HIS B N   
4633 C CA  . HIS B 112 ? 0.8794 0.7733 0.6289 -0.0150 0.1495  -0.1082 207  HIS B CA  
4634 C C   . HIS B 112 ? 0.8581 0.7619 0.6205 -0.0088 0.1499  -0.0971 207  HIS B C   
4635 O O   . HIS B 112 ? 0.8046 0.7120 0.5550 -0.0094 0.1511  -0.0933 207  HIS B O   
4636 C CB  . HIS B 112 ? 0.8686 0.7665 0.6010 -0.0220 0.1373  -0.1077 207  HIS B CB  
4637 C CG  . HIS B 112 ? 0.8819 0.7896 0.6280 -0.0212 0.1249  -0.0995 207  HIS B CG  
4638 N ND1 . HIS B 112 ? 0.8990 0.8057 0.6611 -0.0212 0.1215  -0.1011 207  HIS B ND1 
4639 C CD2 . HIS B 112 ? 0.8816 0.8000 0.6276 -0.0206 0.1155  -0.0900 207  HIS B CD2 
4640 C CE1 . HIS B 112 ? 0.8481 0.7652 0.6194 -0.0207 0.1110  -0.0931 207  HIS B CE1 
4641 N NE2 . HIS B 112 ? 0.8534 0.7777 0.6156 -0.0201 0.1071  -0.0865 207  HIS B NE2 
4642 N N   . LYS B 113 ? 0.8295 0.7368 0.6153 -0.0032 0.1492  -0.0920 208  LYS B N   
4643 C CA  . LYS B 113 ? 0.8248 0.7413 0.6249 0.0027  0.1497  -0.0822 208  LYS B CA  
4644 C C   . LYS B 113 ? 0.8379 0.7526 0.6343 0.0051  0.1617  -0.0839 208  LYS B C   
4645 O O   . LYS B 113 ? 0.8335 0.7408 0.6336 0.0070  0.1717  -0.0911 208  LYS B O   
4646 C CB  . LYS B 113 ? 0.8020 0.7280 0.5980 0.0009  0.1382  -0.0737 208  LYS B CB  
4647 C CG  . LYS B 113 ? 0.7973 0.7265 0.6003 -0.0010 0.1271  -0.0721 208  LYS B CG  
4648 C CD  . LYS B 113 ? 0.7979 0.7365 0.5964 -0.0024 0.1162  -0.0643 208  LYS B CD  
4649 C CE  . LYS B 113 ? 0.8254 0.7696 0.6368 -0.0028 0.1065  -0.0615 208  LYS B CE  
4650 N NZ  . LYS B 113 ? 0.7848 0.7385 0.5943 -0.0033 0.0961  -0.0540 208  LYS B NZ  
4651 N N   . LEU B 114 ? 0.8131 0.7340 0.6028 0.0051  0.1619  -0.0777 209  LEU B N   
4652 C CA  . LEU B 114 ? 0.8277 0.7475 0.6138 0.0066  0.1740  -0.0794 209  LEU B CA  
4653 C C   . LEU B 114 ? 0.8846 0.7989 0.6427 0.0004  0.1773  -0.0842 209  LEU B C   
4654 O O   . LEU B 114 ? 0.8618 0.7761 0.6131 0.0004  0.1866  -0.0842 209  LEU B O   
4655 C CB  . LEU B 114 ? 0.8368 0.7662 0.6354 0.0105  0.1740  -0.0695 209  LEU B CB  
4656 C CG  . LEU B 114 ? 0.8829 0.8183 0.6712 0.0080  0.1660  -0.0608 209  LEU B CG  
4657 C CD1 . LEU B 114 ? 0.8682 0.8102 0.6673 0.0113  0.1712  -0.0540 209  LEU B CD1 
4658 C CD2 . LEU B 114 ? 0.8640 0.8041 0.6590 0.0081  0.1523  -0.0555 209  LEU B CD2 
4659 N N   . TYR B 115 ? 0.8927 0.8026 0.6344 -0.0053 0.1699  -0.0886 210  TYR B N   
4660 C CA  . TYR B 115 ? 0.9044 0.8093 0.6173 -0.0118 0.1708  -0.0929 210  TYR B CA  
4661 C C   . TYR B 115 ? 0.9274 0.8211 0.6302 -0.0149 0.1782  -0.1062 210  TYR B C   
4662 O O   . TYR B 115 ? 0.9268 0.8165 0.6401 -0.0145 0.1759  -0.1113 210  TYR B O   
4663 C CB  . TYR B 115 ? 0.8860 0.7949 0.5864 -0.0163 0.1557  -0.0881 210  TYR B CB  
4664 C CG  . TYR B 115 ? 0.9084 0.8276 0.6218 -0.0127 0.1474  -0.0757 210  TYR B CG  
4665 C CD1 . TYR B 115 ? 0.9435 0.8662 0.6510 -0.0118 0.1499  -0.0680 210  TYR B CD1 
4666 C CD2 . TYR B 115 ? 0.8885 0.8133 0.6199 -0.0104 0.1377  -0.0718 210  TYR B CD2 
4667 C CE1 . TYR B 115 ? 0.9333 0.8643 0.6528 -0.0086 0.1426  -0.0572 210  TYR B CE1 
4668 C CE2 . TYR B 115 ? 0.8928 0.8265 0.6360 -0.0071 0.1308  -0.0612 210  TYR B CE2 
4669 C CZ  . TYR B 115 ? 0.9350 0.8715 0.6722 -0.0061 0.1331  -0.0541 210  TYR B CZ  
4670 O OH  . TYR B 115 ? 1.0029 0.9473 0.7519 -0.0029 0.1265  -0.0441 210  TYR B OH  
4671 N N   . SER B 116 ? 0.9473 0.8353 0.6294 -0.0182 0.1875  -0.1119 211  SER B N   
4672 C CA  . SER B 116 ? 1.0067 0.8833 0.6762 -0.0218 0.1951  -0.1254 211  SER B CA  
4673 C C   . SER B 116 ? 1.0476 0.9198 0.6837 -0.0291 0.1963  -0.1293 211  SER B C   
4674 O O   . SER B 116 ? 1.0874 0.9642 0.7125 -0.0298 0.1971  -0.1220 211  SER B O   
4675 C CB  . SER B 116 ? 0.9929 0.8649 0.6773 -0.0164 0.2109  -0.1314 211  SER B CB  
4676 O OG  . SER B 116 ? 1.0620 0.9380 0.7434 -0.0146 0.2207  -0.1277 211  SER B OG  
4677 N N   . MET B 117 ? 1.0550 0.9179 0.6745 -0.0347 0.1964  -0.1408 212  MET B N   
4678 C CA  . MET B 117 ? 1.0995 0.9576 0.6849 -0.0425 0.1959  -0.1456 212  MET B CA  
4679 C C   . MET B 117 ? 1.1125 0.9577 0.6861 -0.0463 0.2055  -0.1617 212  MET B C   
4680 O O   . MET B 117 ? 1.1084 0.9486 0.6958 -0.0456 0.2043  -0.1683 212  MET B O   
4681 C CB  . MET B 117 ? 1.0889 0.9521 0.6621 -0.0477 0.1777  -0.1406 212  MET B CB  
4682 C CG  . MET B 117 ? 1.1598 1.0167 0.6979 -0.0566 0.1751  -0.1481 212  MET B CG  
4683 S SD  . MET B 117 ? 1.1985 1.0642 0.7222 -0.0615 0.1535  -0.1393 212  MET B SD  
4684 C CE  . MET B 117 ? 1.1147 0.9780 0.6460 -0.0659 0.1433  -0.1492 212  MET B CE  
4685 N N   . GLN B 118 ? 1.1675 1.0066 0.7151 -0.0505 0.2153  -0.1680 213  GLN B N   
4686 C CA  . GLN B 118 ? 1.1368 0.9628 0.6709 -0.0543 0.2258  -0.1842 213  GLN B CA  
4687 C C   . GLN B 118 ? 1.1824 1.0035 0.6895 -0.0638 0.2147  -0.1911 213  GLN B C   
4688 O O   . GLN B 118 ? 1.2631 1.0882 0.7463 -0.0690 0.2063  -0.1859 213  GLN B O   
4689 C CB  . GLN B 118 ? 1.1489 0.9738 0.6757 -0.0531 0.2395  -0.1861 213  GLN B CB  
4690 C CG  . GLN B 118 ? 1.2304 1.0454 0.7461 -0.0567 0.2450  -0.1998 213  GLN B CG  
4691 C CD  . GLN B 118 ? 1.2747 1.0898 0.7899 -0.0543 0.2585  -0.2016 213  GLN B CD  
4692 O OE1 . GLN B 118 ? 1.2441 1.0571 0.7814 -0.0482 0.2698  -0.2060 213  GLN B OE1 
4693 N NE2 . GLN B 118 ? 1.2527 1.0702 0.7425 -0.0591 0.2573  -0.1981 213  GLN B NE2 
4694 N N   . CYS B 119 ? 1.1637 0.9760 0.6749 -0.0662 0.2147  -0.2029 214  CYS B N   
4695 C CA  . CYS B 119 ? 1.1869 0.9934 0.6748 -0.0756 0.2054  -0.2120 214  CYS B CA  
4696 C C   . CYS B 119 ? 1.2270 1.0227 0.7074 -0.0776 0.2154  -0.2254 214  CYS B C   
4697 O O   . CYS B 119 ? 1.2328 1.0228 0.7336 -0.0717 0.2275  -0.2303 214  CYS B O   
4698 C CB  . CYS B 119 ? 1.1895 0.9983 0.6973 -0.0761 0.1922  -0.2115 214  CYS B CB  
4699 S SG  . CYS B 119 ? 1.1361 0.9616 0.6735 -0.0690 0.1792  -0.1923 214  CYS B SG  
4700 N N   . ILE B 120 ? 1.2422 1.0357 0.6948 -0.0855 0.2094  -0.2306 215  ILE B N   
4701 C CA  . ILE B 120 ? 1.2308 1.0156 0.6719 -0.0877 0.2182  -0.2417 215  ILE B CA  
4702 C C   . ILE B 120 ? 1.2512 1.0282 0.6801 -0.0961 0.2099  -0.2538 215  ILE B C   
4703 O O   . ILE B 120 ? 1.2757 1.0570 0.6864 -0.1032 0.1952  -0.2522 215  ILE B O   
4704 C CB  . ILE B 120 ? 1.2898 1.0790 0.7067 -0.0897 0.2201  -0.2369 215  ILE B CB  
4705 C CG1 . ILE B 120 ? 1.3087 1.1047 0.7402 -0.0816 0.2305  -0.2263 215  ILE B CG1 
4706 C CG2 . ILE B 120 ? 1.2818 1.0620 0.6817 -0.0938 0.2269  -0.2494 215  ILE B CG2 
4707 C CD1 . ILE B 120 ? 1.3460 1.1506 0.7581 -0.0835 0.2250  -0.2143 215  ILE B CD1 
4708 N N   . LEU B 121 ? 1.2513 1.0171 0.6913 -0.0952 0.2188  -0.2656 216  LEU B N   
4709 C CA  . LEU B 121 ? 1.3207 1.0773 0.7493 -0.1033 0.2133  -0.2787 216  LEU B CA  
4710 C C   . LEU B 121 ? 1.3614 1.1115 0.7709 -0.1056 0.2217  -0.2873 216  LEU B C   
4711 O O   . LEU B 121 ? 1.3855 1.1296 0.8073 -0.0999 0.2365  -0.2917 216  LEU B O   
4712 C CB  . LEU B 121 ? 1.2666 1.0135 0.7204 -0.1011 0.2170  -0.2861 216  LEU B CB  
4713 C CG  . LEU B 121 ? 1.3874 1.1237 0.8316 -0.1098 0.2121  -0.3002 216  LEU B CG  
4714 C CD1 . LEU B 121 ? 1.3623 1.1055 0.7887 -0.1194 0.1936  -0.2991 216  LEU B CD1 
4715 C CD2 . LEU B 121 ? 1.3712 1.0957 0.8412 -0.1070 0.2180  -0.3073 216  LEU B CD2 
4716 N N   . ASP B 122 ? 1.4145 1.1666 0.7945 -0.1138 0.2121  -0.2895 217  ASP B N   
4717 C CA  . ASP B 122 ? 1.4637 1.2100 0.8213 -0.1174 0.2185  -0.2979 217  ASP B CA  
4718 C C   . ASP B 122 ? 1.5047 1.2435 0.8480 -0.1268 0.2094  -0.3106 217  ASP B C   
4719 O O   . ASP B 122 ? 1.5574 1.3021 0.8817 -0.1340 0.1939  -0.3086 217  ASP B O   
4720 C CB  . ASP B 122 ? 1.4606 1.2159 0.7940 -0.1186 0.2156  -0.2884 217  ASP B CB  
4721 C CG  . ASP B 122 ? 1.5856 1.3351 0.8972 -0.1211 0.2247  -0.2963 217  ASP B CG  
4722 O OD1 . ASP B 122 ? 1.6038 1.3423 0.9195 -0.1217 0.2337  -0.3093 217  ASP B OD1 
4723 O OD2 . ASP B 122 ? 1.5708 1.3263 0.8608 -0.1226 0.2230  -0.2891 217  ASP B OD2 
4724 N N   . ILE B 123 ? 1.5262 1.2523 0.8796 -0.1267 0.2186  -0.3234 218  ILE B N   
4725 C CA  . ILE B 123 ? 1.6149 1.3322 0.9602 -0.1352 0.2116  -0.3364 218  ILE B CA  
4726 C C   . ILE B 123 ? 1.7119 1.4312 1.0223 -0.1440 0.2029  -0.3406 218  ILE B C   
4727 O O   . ILE B 123 ? 1.7533 1.4702 1.0532 -0.1526 0.1914  -0.3483 218  ILE B O   
4728 C CB  . ILE B 123 ? 1.5850 1.2872 0.9456 -0.1325 0.2258  -0.3490 218  ILE B CB  
4729 N N   . LYS B 124 ? 1.7330 1.4568 1.0255 -0.1420 0.2083  -0.3355 219  LYS B N   
4730 C CA  . LYS B 124 ? 1.7927 1.5180 1.0507 -0.1497 0.2009  -0.3385 219  LYS B CA  
4731 C C   . LYS B 124 ? 1.8085 1.5450 1.0528 -0.1556 0.1801  -0.3307 219  LYS B C   
4732 O O   . LYS B 124 ? 1.8492 1.5861 1.0682 -0.1635 0.1699  -0.3359 219  LYS B O   
4733 C CB  . LYS B 124 ? 1.7820 1.5098 1.0256 -0.1458 0.2120  -0.3333 219  LYS B CB  
4734 N N   . HIS B 125 ? 1.7695 1.5156 1.0303 -0.1518 0.1733  -0.3185 220  HIS B N   
4735 C CA  . HIS B 125 ? 1.8026 1.5597 1.0549 -0.1568 0.1532  -0.3111 220  HIS B CA  
4736 C C   . HIS B 125 ? 1.8038 1.5600 1.0756 -0.1604 0.1443  -0.3165 220  HIS B C   
4737 O O   . HIS B 125 ? 1.8057 1.5723 1.0837 -0.1614 0.1307  -0.3079 220  HIS B O   
4738 C CB  . HIS B 125 ? 1.8499 1.6190 1.1056 -0.1509 0.1502  -0.2935 220  HIS B CB  
4739 C CG  . HIS B 125 ? 1.8672 1.6377 1.1055 -0.1475 0.1590  -0.2870 220  HIS B CG  
4740 N ND1 . HIS B 125 ? 1.8145 1.5852 1.0681 -0.1389 0.1740  -0.2802 220  HIS B ND1 
4741 C CD2 . HIS B 125 ? 1.9206 1.6928 1.1283 -0.1516 0.1549  -0.2859 220  HIS B CD2 
4742 C CE1 . HIS B 125 ? 1.8719 1.6441 1.1053 -0.1384 0.1791  -0.2754 220  HIS B CE1 
4743 N NE2 . HIS B 125 ? 1.9287 1.7014 1.1334 -0.1458 0.1679  -0.2786 220  HIS B NE2 
4744 N N   . ASN B 126 ? 1.7573 1.5009 1.0391 -0.1625 0.1518  -0.3304 221  ASN B N   
4745 C CA  . ASN B 126 ? 1.7068 1.4477 1.0092 -0.1658 0.1455  -0.3358 221  ASN B CA  
4746 C C   . ASN B 126 ? 1.7399 1.4684 1.0369 -0.1731 0.1466  -0.3527 221  ASN B C   
4747 O O   . ASN B 126 ? 1.7184 1.4366 1.0364 -0.1726 0.1531  -0.3604 221  ASN B O   
4748 C CB  . ASN B 126 ? 1.6628 1.4001 0.9973 -0.1570 0.1570  -0.3317 221  ASN B CB  
4749 C CG  . ASN B 126 ? 1.6195 1.3701 0.9647 -0.1527 0.1499  -0.3165 221  ASN B CG  
4750 O OD1 . ASN B 126 ? 1.5706 1.3278 0.9232 -0.1568 0.1366  -0.3141 221  ASN B OD1 
4751 N ND2 . ASN B 126 ? 1.5574 1.3122 0.9041 -0.1445 0.1588  -0.3062 221  ASN B ND2 
4752 N N   . ASP B 127 ? 1.7578 1.4866 1.0263 -0.1800 0.1401  -0.3585 222  ASP B N   
4753 C CA  . ASP B 127 ? 1.7790 1.4964 1.0381 -0.1877 0.1405  -0.3748 222  ASP B CA  
4754 C C   . ASP B 127 ? 1.8396 1.5406 1.1105 -0.1829 0.1606  -0.3847 222  ASP B C   
4755 O O   . ASP B 127 ? 1.8533 1.5425 1.1273 -0.1880 0.1627  -0.3982 222  ASP B O   
4756 C CB  . ASP B 127 ? 1.6978 1.4167 0.9678 -0.1958 0.1262  -0.3802 222  ASP B CB  
4757 N N   . ASN B 128 ? 1.8673 1.5676 1.1456 -0.1733 0.1753  -0.3780 223  ASN B N   
4758 C CA  . ASN B 128 ? 1.8574 1.5441 1.1484 -0.1673 0.1947  -0.3859 223  ASN B CA  
4759 C C   . ASN B 128 ? 1.8561 1.5322 1.1758 -0.1663 0.1983  -0.3922 223  ASN B C   
4760 O O   . ASN B 128 ? 1.8740 1.5359 1.1968 -0.1678 0.2067  -0.4050 223  ASN B O   
4761 C CB  . ASN B 128 ? 1.9213 1.5992 1.1873 -0.1720 0.2007  -0.3983 223  ASN B CB  
4762 C CG  . ASN B 128 ? 1.9685 1.6512 1.2176 -0.1675 0.2095  -0.3923 223  ASN B CG  
4763 O OD1 . ASN B 128 ? 2.0546 1.7295 1.3085 -0.1620 0.2263  -0.3968 223  ASN B OD1 
4764 N ND2 . ASN B 128 ? 1.9331 1.6287 1.1630 -0.1696 0.1982  -0.3818 223  ASN B ND2 
4765 N N   . ASP B 129 ? 1.8180 1.5008 1.1586 -0.1636 0.1921  -0.3830 224  ASP B N   
4766 C CA  . ASP B 129 ? 1.7601 1.4334 1.1291 -0.1620 0.1955  -0.3870 224  ASP B CA  
4767 C C   . ASP B 129 ? 1.7376 1.4046 1.1294 -0.1500 0.2132  -0.3837 224  ASP B C   
4768 O O   . ASP B 129 ? 1.7264 1.4029 1.1252 -0.1423 0.2165  -0.3715 224  ASP B O   
4769 C CB  . ASP B 129 ? 1.7755 1.4586 1.1573 -0.1645 0.1814  -0.3788 224  ASP B CB  
4770 C CG  . ASP B 129 ? 1.7268 1.3992 1.1324 -0.1665 0.1819  -0.3853 224  ASP B CG  
4771 O OD1 . ASP B 129 ? 1.7140 1.3911 1.1220 -0.1743 0.1680  -0.3859 224  ASP B OD1 
4772 O OD2 . ASP B 129 ? 1.7361 1.3951 1.1586 -0.1604 0.1961  -0.3898 224  ASP B OD2 
4773 N N   . LYS B 130 ? 1.6976 1.3489 1.1012 -0.1484 0.2243  -0.3943 225  LYS B N   
4774 C CA  . LYS B 130 ? 1.6264 1.2712 1.0552 -0.1369 0.2400  -0.3916 225  LYS B CA  
4775 C C   . LYS B 130 ? 1.5561 1.1968 1.0148 -0.1335 0.2387  -0.3878 225  LYS B C   
4776 O O   . LYS B 130 ? 1.4870 1.1279 0.9685 -0.1230 0.2477  -0.3803 225  LYS B O   
4777 C CB  . LYS B 130 ? 1.5173 1.1472 0.9437 -0.1357 0.2537  -0.4045 225  LYS B CB  
4778 N N   . ASN B 131 ? 1.5535 1.1906 1.0126 -0.1423 0.2275  -0.3928 226  ASN B N   
4779 C CA  . ASN B 131 ? 1.5535 1.1881 1.0389 -0.1404 0.2245  -0.3880 226  ASN B CA  
4780 C C   . ASN B 131 ? 1.5130 1.1632 1.0065 -0.1352 0.2193  -0.3728 226  ASN B C   
4781 O O   . ASN B 131 ? 1.4906 1.1394 1.0092 -0.1272 0.2242  -0.3657 226  ASN B O   
4782 C CB  . ASN B 131 ? 1.5699 1.2005 1.0516 -0.1524 0.2120  -0.3957 226  ASN B CB  
4783 C CG  . ASN B 131 ? 1.6192 1.2340 1.0931 -0.1582 0.2167  -0.4111 226  ASN B CG  
4784 O OD1 . ASN B 131 ? 1.5996 1.2003 1.0868 -0.1519 0.2302  -0.4158 226  ASN B OD1 
4785 N ND2 . ASN B 131 ? 1.6651 1.2823 1.1172 -0.1700 0.2054  -0.4190 226  ASN B ND2 
4786 N N   . MET B 132 ? 1.5137 1.1786 0.9860 -0.1395 0.2090  -0.3675 227  MET B N   
4787 C CA  . MET B 132 ? 1.5101 1.1900 0.9883 -0.1346 0.2041  -0.3531 227  MET B CA  
4788 C C   . MET B 132 ? 1.4546 1.1356 0.9458 -0.1220 0.2181  -0.3453 227  MET B C   
4789 O O   . MET B 132 ? 1.4252 1.1109 0.9370 -0.1148 0.2197  -0.3355 227  MET B O   
4790 C CB  . MET B 132 ? 1.5264 1.2209 0.9777 -0.1412 0.1910  -0.3488 227  MET B CB  
4791 C CG  . MET B 132 ? 1.4833 1.1930 0.9397 -0.1362 0.1858  -0.3336 227  MET B CG  
4792 S SD  . MET B 132 ? 1.5224 1.2491 0.9483 -0.1428 0.1700  -0.3266 227  MET B SD  
4793 C CE  . MET B 132 ? 1.5346 1.2614 0.9533 -0.1563 0.1528  -0.3358 227  MET B CE  
4794 N N   . MET B 133 ? 1.4633 1.1409 0.9432 -0.1194 0.2284  -0.3498 228  MET B N   
4795 C CA  . MET B 133 ? 1.4340 1.1135 0.9273 -0.1079 0.2421  -0.3433 228  MET B CA  
4796 C C   . MET B 133 ? 1.4002 1.0697 0.9253 -0.0996 0.2514  -0.3436 228  MET B C   
4797 O O   . MET B 133 ? 1.3611 1.0363 0.9061 -0.0902 0.2561  -0.3334 228  MET B O   
4798 C CB  . MET B 133 ? 1.4690 1.1452 0.9444 -0.1079 0.2517  -0.3502 228  MET B CB  
4799 C CG  . MET B 133 ? 1.4754 1.1543 0.9654 -0.0966 0.2663  -0.3446 228  MET B CG  
4800 S SD  . MET B 133 ? 1.4923 1.1901 0.9852 -0.0912 0.2623  -0.3267 228  MET B SD  
4801 C CE  . MET B 133 ? 1.4812 1.1874 0.9346 -0.1016 0.2512  -0.3265 228  MET B CE  
4802 N N   . LYS B 134 ? 1.4018 1.0560 0.9321 -0.1030 0.2537  -0.3548 229  LYS B N   
4803 C CA  . LYS B 134 ? 1.4068 1.0501 0.9668 -0.0952 0.2619  -0.3548 229  LYS B CA  
4804 C C   . LYS B 134 ? 1.3516 0.9999 0.9304 -0.0930 0.2545  -0.3447 229  LYS B C   
4805 O O   . LYS B 134 ? 1.3774 1.0268 0.9797 -0.0826 0.2609  -0.3364 229  LYS B O   
4806 C CB  . LYS B 134 ? 1.4002 1.0256 0.9598 -0.1008 0.2642  -0.3687 229  LYS B CB  
4807 N N   . TRP B 135 ? 1.3655 1.0175 0.9342 -0.1028 0.2409  -0.3453 230  TRP B N   
4808 C CA  . TRP B 135 ? 1.3525 1.0090 0.9379 -0.1019 0.2337  -0.3367 230  TRP B CA  
4809 C C   . TRP B 135 ? 1.3071 0.9787 0.8982 -0.0939 0.2339  -0.3228 230  TRP B C   
4810 O O   . TRP B 135 ? 1.3046 0.9767 0.9188 -0.0862 0.2365  -0.3148 230  TRP B O   
4811 C CB  . TRP B 135 ? 1.3567 1.0167 0.9285 -0.1148 0.2184  -0.3403 230  TRP B CB  
4812 C CG  . TRP B 135 ? 1.3299 0.9952 0.9181 -0.1148 0.2109  -0.3321 230  TRP B CG  
4813 C CD1 . TRP B 135 ? 1.3404 0.9950 0.9493 -0.1153 0.2112  -0.3334 230  TRP B CD1 
4814 C CD2 . TRP B 135 ? 1.3023 0.9844 0.8875 -0.1143 0.2023  -0.3212 230  TRP B CD2 
4815 N NE1 . TRP B 135 ? 1.3182 0.9850 0.9402 -0.1143 0.2018  -0.3216 230  TRP B NE1 
4816 C CE2 . TRP B 135 ? 1.3065 0.9927 0.9176 -0.1126 0.1948  -0.3119 230  TRP B CE2 
4817 C CE3 . TRP B 135 ? 1.2842 0.9820 0.8525 -0.1135 0.1978  -0.3140 230  TRP B CE3 
4818 C CZ2 . TRP B 135 ? 1.2489 0.9556 0.8710 -0.1097 0.1825  -0.2953 230  TRP B CZ2 
4819 C CZ3 . TRP B 135 ? 1.2503 0.9677 0.8300 -0.1105 0.1853  -0.2973 230  TRP B CZ3 
4820 C CH2 . TRP B 135 ? 1.2455 0.9674 0.8520 -0.1085 0.1779  -0.2885 230  TRP B CH2 
4821 N N   . VAL B 136 ? 1.3200 1.0039 0.8901 -0.0956 0.2310  -0.3195 231  VAL B N   
4822 C CA  . VAL B 136 ? 1.3141 1.0125 0.8885 -0.0886 0.2310  -0.3062 231  VAL B CA  
4823 C C   . VAL B 136 ? 1.2956 0.9921 0.8909 -0.0760 0.2452  -0.3018 231  VAL B C   
4824 O O   . VAL B 136 ? 1.2407 0.9437 0.8549 -0.0681 0.2466  -0.2914 231  VAL B O   
4825 C CB  . VAL B 136 ? 1.2856 0.9960 0.8318 -0.0935 0.2251  -0.3036 231  VAL B CB  
4826 C CG1 . VAL B 136 ? 1.2379 0.9617 0.7896 -0.0855 0.2276  -0.2900 231  VAL B CG1 
4827 C CG2 . VAL B 136 ? 1.2729 0.9886 0.8016 -0.1049 0.2088  -0.3052 231  VAL B CG2 
4828 N N   . SER B 137 ? 1.2830 0.9711 0.8762 -0.0739 0.2557  -0.3097 232  SER B N   
4829 C CA  . SER B 137 ? 1.2589 0.9464 0.8722 -0.0622 0.2689  -0.3061 232  SER B CA  
4830 C C   . SER B 137 ? 1.2479 0.9264 0.8913 -0.0549 0.2728  -0.3044 232  SER B C   
4831 O O   . SER B 137 ? 1.2742 0.9559 0.9387 -0.0441 0.2808  -0.2977 232  SER B O   
4832 C CB  . SER B 137 ? 1.3213 1.0018 0.9244 -0.0625 0.2790  -0.3161 232  SER B CB  
4833 O OG  . SER B 137 ? 1.3334 1.0196 0.9058 -0.0708 0.2744  -0.3192 232  SER B OG  
4834 N N   . ASN B 138 ? 1.2491 0.9167 0.8955 -0.0605 0.2671  -0.3098 233  ASN B N   
4835 C CA  . ASN B 138 ? 1.2612 0.9193 0.9354 -0.0539 0.2700  -0.3069 233  ASN B CA  
4836 C C   . ASN B 138 ? 1.1995 0.8662 0.8867 -0.0512 0.2629  -0.2952 233  ASN B C   
4837 O O   . ASN B 138 ? 1.1577 0.8171 0.8678 -0.0455 0.2646  -0.2914 233  ASN B O   
4838 C CB  . ASN B 138 ? 1.2868 0.9275 0.9599 -0.0612 0.2684  -0.3181 233  ASN B CB  
4839 C CG  . ASN B 138 ? 1.3057 0.9331 1.0067 -0.0530 0.2750  -0.3167 233  ASN B CG  
4840 O OD1 . ASN B 138 ? 1.2967 0.9241 1.0139 -0.0421 0.2846  -0.3131 233  ASN B OD1 
4841 N ND2 . ASN B 138 ? 1.3312 0.9478 1.0385 -0.0584 0.2696  -0.3191 233  ASN B ND2 
4842 N N   . LEU B 139 ? 1.1814 0.8628 0.8548 -0.0548 0.2550  -0.2890 234  LEU B N   
4843 C CA  . LEU B 139 ? 1.1532 0.8453 0.8410 -0.0523 0.2458  -0.2761 234  LEU B CA  
4844 C C   . LEU B 139 ? 1.1293 0.8274 0.8423 -0.0389 0.2524  -0.2647 234  LEU B C   
4845 O O   . LEU B 139 ? 1.1429 0.8463 0.8523 -0.0336 0.2612  -0.2641 234  LEU B O   
4846 C CB  . LEU B 139 ? 1.1321 0.8426 0.8029 -0.0583 0.2327  -0.2686 234  LEU B CB  
4847 C CG  . LEU B 139 ? 1.1847 0.8944 0.8366 -0.0714 0.2207  -0.2755 234  LEU B CG  
4848 C CD1 . LEU B 139 ? 1.1312 0.8589 0.7655 -0.0757 0.2092  -0.2680 234  LEU B CD1 
4849 C CD2 . LEU B 139 ? 1.1521 0.8595 0.8232 -0.0736 0.2119  -0.2719 234  LEU B CD2 
4850 N N   . PRO B 140 ? 1.0560 0.7539 0.7945 -0.0333 0.2485  -0.2556 235  PRO B N   
4851 C CA  . PRO B 140 ? 1.0184 0.7235 0.7807 -0.0207 0.2531  -0.2441 235  PRO B CA  
4852 C C   . PRO B 140 ? 1.0130 0.7401 0.7741 -0.0187 0.2458  -0.2310 235  PRO B C   
4853 O O   . PRO B 140 ? 0.9841 0.7216 0.7337 -0.0258 0.2335  -0.2265 235  PRO B O   
4854 C CB  . PRO B 140 ? 1.0392 0.7389 0.8245 -0.0177 0.2479  -0.2372 235  PRO B CB  
4855 C CG  . PRO B 140 ? 1.0767 0.7657 0.8511 -0.0288 0.2416  -0.2455 235  PRO B CG  
4856 C CD  . PRO B 140 ? 1.0828 0.7756 0.8284 -0.0391 0.2385  -0.2544 235  PRO B CD  
4857 N N   . LEU B 141 ? 0.9758 0.7099 0.7500 -0.0089 0.2534  -0.2248 236  LEU B N   
4858 C CA  . LEU B 141 ? 0.9550 0.7088 0.7311 -0.0063 0.2470  -0.2118 236  LEU B CA  
4859 C C   . LEU B 141 ? 0.9338 0.6966 0.7256 -0.0053 0.2337  -0.1989 236  LEU B C   
4860 O O   . LEU B 141 ? 0.9106 0.6655 0.7197 -0.0020 0.2329  -0.1971 236  LEU B O   
4861 C CB  . LEU B 141 ? 0.9142 0.6736 0.7042 0.0040  0.2581  -0.2083 236  LEU B CB  
4862 C CG  . LEU B 141 ? 1.0140 0.7686 0.7882 0.0032  0.2720  -0.2194 236  LEU B CG  
4863 C CD1 . LEU B 141 ? 0.9804 0.7436 0.7721 0.0134  0.2819  -0.2142 236  LEU B CD1 
4864 C CD2 . LEU B 141 ? 1.0194 0.7804 0.7639 -0.0064 0.2670  -0.2213 236  LEU B CD2 
4865 N N   . GLU B 142 ? 0.9267 0.7054 0.7115 -0.0081 0.2235  -0.1898 237  GLU B N   
4866 C CA  . GLU B 142 ? 0.8793 0.6695 0.6744 -0.0085 0.2101  -0.1776 237  GLU B CA  
4867 C C   . GLU B 142 ? 0.8888 0.6759 0.6735 -0.0184 0.1996  -0.1813 237  GLU B C   
4868 O O   . GLU B 142 ? 0.8834 0.6804 0.6755 -0.0195 0.1886  -0.1721 237  GLU B O   
4869 C CB  . GLU B 142 ? 0.8111 0.6013 0.6336 0.0003  0.2104  -0.1689 237  GLU B CB  
4870 C CG  . GLU B 142 ? 0.8544 0.6532 0.6909 0.0102  0.2168  -0.1619 237  GLU B CG  
4871 C CD  . GLU B 142 ? 0.8658 0.6814 0.6938 0.0092  0.2119  -0.1545 237  GLU B CD  
4872 O OE1 . GLU B 142 ? 0.8865 0.7035 0.7019 0.0085  0.2192  -0.1590 237  GLU B OE1 
4873 O OE2 . GLU B 142 ? 0.8440 0.6708 0.6775 0.0087  0.2011  -0.1442 237  GLU B OE2 
4874 N N   . SER B 143 ? 0.9102 0.6847 0.6785 -0.0258 0.2027  -0.1946 238  SER B N   
4875 C CA  . SER B 143 ? 0.9264 0.6995 0.6850 -0.0359 0.1922  -0.1984 238  SER B CA  
4876 C C   . SER B 143 ? 0.9044 0.6941 0.6494 -0.0408 0.1805  -0.1923 238  SER B C   
4877 O O   . SER B 143 ? 0.9284 0.7248 0.6602 -0.0398 0.1826  -0.1910 238  SER B O   
4878 C CB  . SER B 143 ? 0.9784 0.7350 0.7198 -0.0434 0.1981  -0.2150 238  SER B CB  
4879 O OG  . SER B 143 ? 0.9952 0.7348 0.7488 -0.0386 0.2096  -0.2215 238  SER B OG  
4880 N N   . ILE B 144 ? 0.9017 0.6979 0.6503 -0.0461 0.1681  -0.1883 239  ILE B N   
4881 C CA  . ILE B 144 ? 0.9241 0.7362 0.6624 -0.0503 0.1559  -0.1819 239  ILE B CA  
4882 C C   . ILE B 144 ? 0.9411 0.7495 0.6565 -0.0613 0.1507  -0.1929 239  ILE B C   
4883 O O   . ILE B 144 ? 0.9656 0.7656 0.6825 -0.0678 0.1483  -0.2006 239  ILE B O   
4884 C CB  . ILE B 144 ? 0.8708 0.6944 0.6275 -0.0491 0.1453  -0.1706 239  ILE B CB  
4885 C CG1 . ILE B 144 ? 0.8249 0.6527 0.6022 -0.0384 0.1499  -0.1598 239  ILE B CG1 
4886 C CG2 . ILE B 144 ? 0.8712 0.7105 0.6175 -0.0534 0.1327  -0.1651 239  ILE B CG2 
4887 C CD1 . ILE B 144 ? 0.8383 0.6740 0.6350 -0.0369 0.1419  -0.1500 239  ILE B CD1 
4888 N N   . VAL B 145 ? 0.9711 0.7857 0.6650 -0.0639 0.1486  -0.1935 240  VAL B N   
4889 C CA  . VAL B 145 ? 0.9836 0.7950 0.6523 -0.0741 0.1437  -0.2040 240  VAL B CA  
4890 C C   . VAL B 145 ? 0.9978 0.8256 0.6552 -0.0775 0.1298  -0.1963 240  VAL B C   
4891 O O   . VAL B 145 ? 0.9734 0.8125 0.6350 -0.0715 0.1277  -0.1844 240  VAL B O   
4892 C CB  . VAL B 145 ? 1.0370 0.8363 0.6845 -0.0751 0.1562  -0.2152 240  VAL B CB  
4893 C CG1 . VAL B 145 ? 1.0135 0.7961 0.6730 -0.0711 0.1704  -0.2234 240  VAL B CG1 
4894 C CG2 . VAL B 145 ? 0.9892 0.7967 0.6278 -0.0696 0.1602  -0.2074 240  VAL B CG2 
4895 N N   . ASP B 146 ? 1.0124 0.8409 0.6553 -0.0874 0.1202  -0.2034 241  ASP B N   
4896 C CA  . ASP B 146 ? 1.0282 0.8698 0.6545 -0.0920 0.1070  -0.1990 241  ASP B CA  
4897 C C   . ASP B 146 ? 1.0962 0.9302 0.6903 -0.0982 0.1103  -0.2095 241  ASP B C   
4898 O O   . ASP B 146 ? 1.1456 0.9678 0.7293 -0.1054 0.1132  -0.2234 241  ASP B O   
4899 C CB  . ASP B 146 ? 1.0086 0.8588 0.6430 -0.0988 0.0924  -0.1990 241  ASP B CB  
4900 C CG  . ASP B 146 ? 1.0174 0.8787 0.6803 -0.0928 0.0875  -0.1865 241  ASP B CG  
4901 O OD1 . ASP B 146 ? 0.9741 0.8355 0.6498 -0.0836 0.0953  -0.1784 241  ASP B OD1 
4902 O OD2 . ASP B 146 ? 1.0187 0.8891 0.6911 -0.0975 0.0759  -0.1849 241  ASP B OD2 
4903 N N   . ILE B 147 ? 1.1102 0.9504 0.6882 -0.0957 0.1101  -0.2030 242  ILE B N   
4904 C CA  . ILE B 147 ? 1.1442 0.9777 0.6899 -0.1008 0.1142  -0.2112 242  ILE B CA  
4905 C C   . ILE B 147 ? 1.1705 1.0162 0.6973 -0.1060 0.0984  -0.2058 242  ILE B C   
4906 O O   . ILE B 147 ? 1.1745 1.0336 0.7109 -0.1013 0.0900  -0.1920 242  ILE B O   
4907 C CB  . ILE B 147 ? 1.1427 0.9717 0.6838 -0.0935 0.1292  -0.2082 242  ILE B CB  
4908 C CG1 . ILE B 147 ? 1.1151 0.9301 0.6707 -0.0893 0.1454  -0.2165 242  ILE B CG1 
4909 C CG2 . ILE B 147 ? 1.1342 0.9601 0.6401 -0.0985 0.1315  -0.2127 242  ILE B CG2 
4910 C CD1 . ILE B 147 ? 1.1376 0.9517 0.6989 -0.0804 0.1593  -0.2113 242  ILE B CD1 
4911 N N   . LYS B 148 ? 1.2060 1.0470 0.7067 -0.1156 0.0939  -0.2168 243  LYS B N   
4912 C CA  . LYS B 148 ? 1.2391 1.0894 0.7151 -0.1208 0.0806  -0.2130 243  LYS B CA  
4913 C C   . LYS B 148 ? 1.2704 1.1118 0.7151 -0.1220 0.0908  -0.2172 243  LYS B C   
4914 O O   . LYS B 148 ? 1.3094 1.1366 0.7402 -0.1263 0.1017  -0.2314 243  LYS B O   
4915 C CB  . LYS B 148 ? 1.2798 1.1324 0.7474 -0.1315 0.0668  -0.2221 243  LYS B CB  
4916 C CG  . LYS B 148 ? 1.3167 1.1789 0.7574 -0.1371 0.0518  -0.2187 243  LYS B CG  
4917 C CD  . LYS B 148 ? 1.4097 1.2773 0.8487 -0.1471 0.0364  -0.2266 243  LYS B CD  
4918 C CE  . LYS B 148 ? 1.4831 1.3594 0.8930 -0.1532 0.0212  -0.2246 243  LYS B CE  
4919 N NZ  . LYS B 148 ? 1.5403 1.4266 0.9553 -0.1617 0.0038  -0.2294 243  LYS B NZ  
4920 N N   . GLY B 149 ? 1.3008 1.1499 0.7346 -0.1182 0.0881  -0.2050 244  GLY B N   
4921 C CA  . GLY B 149 ? 1.3321 1.1727 0.7378 -0.1189 0.0997  -0.2079 244  GLY B CA  
4922 C C   . GLY B 149 ? 1.3572 1.2071 0.7457 -0.1176 0.0917  -0.1944 244  GLY B C   
4923 O O   . GLY B 149 ? 1.3465 1.2094 0.7474 -0.1148 0.0777  -0.1821 244  GLY B O   
4924 N N   . LYS B 150 ? 1.3706 1.2128 0.7300 -0.1195 0.1014  -0.1969 245  LYS B N   
4925 C CA  . LYS B 150 ? 1.3628 1.2108 0.7006 -0.1191 0.0959  -0.1848 245  LYS B CA  
4926 C C   . LYS B 150 ? 1.3859 1.2324 0.7330 -0.1108 0.1108  -0.1760 245  LYS B C   
4927 O O   . LYS B 150 ? 1.3679 1.2046 0.7155 -0.1094 0.1288  -0.1843 245  LYS B O   
4928 C CB  . LYS B 150 ? 1.3625 1.2050 0.6633 -0.1266 0.0942  -0.1916 245  LYS B CB  
4929 N N   . LEU B 151 ? 1.4072 1.2639 0.7627 -0.1055 0.1034  -0.1594 246  LEU B N   
4930 C CA  . LEU B 151 ? 1.3966 1.2536 0.7621 -0.0980 0.1155  -0.1496 246  LEU B CA  
4931 C C   . LEU B 151 ? 1.4471 1.2994 0.7779 -0.1012 0.1209  -0.1459 246  LEU B C   
4932 O O   . LEU B 151 ? 1.4921 1.3483 0.8011 -0.1048 0.1076  -0.1387 246  LEU B O   
4933 C CB  . LEU B 151 ? 1.3906 1.2600 0.7836 -0.0908 0.1052  -0.1340 246  LEU B CB  
4934 C CG  . LEU B 151 ? 1.3700 1.2428 0.8028 -0.0833 0.1107  -0.1327 246  LEU B CG  
4935 C CD1 . LEU B 151 ? 1.3031 1.1716 0.7484 -0.0858 0.1114  -0.1462 246  LEU B CD1 
4936 C CD2 . LEU B 151 ? 1.3409 1.2262 0.7945 -0.0781 0.0972  -0.1183 246  LEU B CD2 
4937 N N   . SER B 152 ? 1.4368 1.2826 0.7681 -0.0986 0.1393  -0.1492 247  SER B N   
4938 C CA  . SER B 152 ? 1.5235 1.3684 0.8356 -0.0986 0.1445  -0.1430 247  SER B CA  
4939 C C   . SER B 152 ? 1.5199 1.3648 0.8500 -0.0919 0.1610  -0.1375 247  SER B C   
4940 O O   . SER B 152 ? 1.4554 1.2989 0.8106 -0.0875 0.1715  -0.1429 247  SER B O   
4941 C CB  . SER B 152 ? 1.4986 1.3368 0.7903 -0.1037 0.1485  -0.1550 247  SER B CB  
4942 O OG  . SER B 152 ? 1.4814 1.3132 0.7888 -0.1029 0.1604  -0.1692 247  SER B OG  
4943 N N   . LYS B 153 ? 1.5385 1.3854 0.8564 -0.0910 0.1629  -0.1262 248  LYS B N   
4944 C CA  . LYS B 153 ? 1.5046 1.3526 0.8387 -0.0854 0.1781  -0.1203 248  LYS B CA  
4945 C C   . LYS B 153 ? 1.5024 1.3455 0.8295 -0.0864 0.1930  -0.1288 248  LYS B C   
4946 O O   . LYS B 153 ? 1.5641 1.4054 0.8654 -0.0904 0.1917  -0.1267 248  LYS B O   
4947 C CB  . LYS B 153 ? 1.5402 1.3924 0.8669 -0.0841 0.1729  -0.1034 248  LYS B CB  
4948 C CG  . LYS B 153 ? 1.5539 1.4075 0.8952 -0.0796 0.1885  -0.0974 248  LYS B CG  
4949 C CD  . LYS B 153 ? 1.5682 1.4269 0.9277 -0.0750 0.1853  -0.0846 248  LYS B CD  
4950 C CE  . LYS B 153 ? 1.5424 1.4034 0.9236 -0.0703 0.2016  -0.0816 248  LYS B CE  
4951 N NZ  . LYS B 153 ? 1.5902 1.4557 0.9876 -0.0661 0.1986  -0.0687 248  LYS B NZ  
4952 N N   . PRO B 154 ? 1.5401 1.3811 0.8891 -0.0828 0.2071  -0.1379 249  PRO B N   
4953 C CA  . PRO B 154 ? 1.5172 1.3536 0.8600 -0.0838 0.2212  -0.1467 249  PRO B CA  
4954 C C   . PRO B 154 ? 1.6016 1.4412 0.9433 -0.0819 0.2314  -0.1373 249  PRO B C   
4955 O O   . PRO B 154 ? 1.5873 1.4324 0.9392 -0.0789 0.2299  -0.1249 249  PRO B O   
4956 C CB  . PRO B 154 ? 1.4975 1.3315 0.8688 -0.0792 0.2316  -0.1576 249  PRO B CB  
4957 C CG  . PRO B 154 ? 1.4812 1.3213 0.8785 -0.0736 0.2287  -0.1490 249  PRO B CG  
4958 C CD  . PRO B 154 ? 1.4547 1.2978 0.8363 -0.0770 0.2111  -0.1397 249  PRO B CD  
4959 N N   . GLU B 155 ? 1.6959 1.5317 1.0249 -0.0842 0.2422  -0.1438 250  GLU B N   
4960 C CA  . GLU B 155 ? 1.7179 1.5564 1.0454 -0.0833 0.2535  -0.1364 250  GLU B CA  
4961 C C   . GLU B 155 ? 1.7256 1.5697 1.0880 -0.0765 0.2644  -0.1334 250  GLU B C   
4962 O O   . GLU B 155 ? 1.7296 1.5792 1.0993 -0.0746 0.2649  -0.1210 250  GLU B O   
4963 C CB  . GLU B 155 ? 1.7207 1.5539 1.0304 -0.0868 0.2643  -0.1461 250  GLU B CB  
4964 N N   . VAL B 156 ? 1.6995 1.5424 1.0845 -0.0727 0.2728  -0.1443 251  VAL B N   
4965 C CA  . VAL B 156 ? 1.6674 1.5162 1.0875 -0.0658 0.2825  -0.1426 251  VAL B CA  
4966 C C   . VAL B 156 ? 1.6287 1.4773 1.0703 -0.0618 0.2761  -0.1464 251  VAL B C   
4967 O O   . VAL B 156 ? 1.6361 1.4792 1.0826 -0.0613 0.2782  -0.1584 251  VAL B O   
4968 C CB  . VAL B 156 ? 1.6717 1.5198 1.1023 -0.0638 0.2997  -0.1515 251  VAL B CB  
4969 C CG1 . VAL B 156 ? 1.6646 1.5187 1.1340 -0.0561 0.3078  -0.1517 251  VAL B CG1 
4970 C CG2 . VAL B 156 ? 1.7252 1.5748 1.1384 -0.0673 0.3071  -0.1458 251  VAL B CG2 
4971 N N   . PRO B 157 ? 1.5724 1.4263 1.0262 -0.0592 0.2682  -0.1362 252  PRO B N   
4972 C CA  . PRO B 157 ? 1.4829 1.3369 0.9571 -0.0555 0.2624  -0.1392 252  PRO B CA  
4973 C C   . PRO B 157 ? 1.4644 1.3217 0.9735 -0.0481 0.2739  -0.1428 252  PRO B C   
4974 O O   . PRO B 157 ? 1.4775 1.3400 0.9995 -0.0452 0.2846  -0.1397 252  PRO B O   
4975 C CB  . PRO B 157 ? 1.4415 1.3005 0.9146 -0.0553 0.2507  -0.1259 252  PRO B CB  
4976 C CG  . PRO B 157 ? 1.4688 1.3322 0.9365 -0.0558 0.2557  -0.1153 252  PRO B CG  
4977 C CD  . PRO B 157 ? 1.5556 1.4146 1.0021 -0.0602 0.2631  -0.1214 252  PRO B CD  
4978 N N   . ILE B 158 ? 1.4231 1.2775 0.9480 -0.0451 0.2711  -0.1494 253  ILE B N   
4979 C CA  . ILE B 158 ? 1.3889 1.2456 0.9471 -0.0376 0.2805  -0.1534 253  ILE B CA  
4980 C C   . ILE B 158 ? 1.3217 1.1884 0.9032 -0.0323 0.2809  -0.1418 253  ILE B C   
4981 O O   . ILE B 158 ? 1.3148 1.1847 0.8908 -0.0335 0.2714  -0.1323 253  ILE B O   
4982 C CB  . ILE B 158 ? 1.3320 1.1819 0.9000 -0.0361 0.2765  -0.1625 253  ILE B CB  
4983 N N   . ASP B 159 ? 1.3152 1.1870 0.9232 -0.0263 0.2918  -0.1426 254  ASP B N   
4984 C CA  . ASP B 159 ? 1.3147 1.1968 0.9465 -0.0213 0.2926  -0.1323 254  ASP B CA  
4985 C C   . ASP B 159 ? 1.2736 1.1568 0.9253 -0.0164 0.2855  -0.1304 254  ASP B C   
4986 O O   . ASP B 159 ? 1.2756 1.1657 0.9375 -0.0143 0.2810  -0.1205 254  ASP B O   
4987 C CB  . ASP B 159 ? 1.3122 1.2005 0.9666 -0.0166 0.3058  -0.1341 254  ASP B CB  
4988 N N   . SER B 160 ? 1.3534 1.2296 1.0102 -0.0148 0.2845  -0.1398 255  SER B N   
4989 C CA  . SER B 160 ? 1.3222 1.1989 0.9996 -0.0098 0.2790  -0.1386 255  SER B CA  
4990 C C   . SER B 160 ? 1.2963 1.1736 0.9615 -0.0134 0.2636  -0.1315 255  SER B C   
4991 O O   . SER B 160 ? 1.2792 1.1652 0.9645 -0.0093 0.2545  -0.1215 255  SER B O   
4992 C CB  . SER B 160 ? 1.2837 1.1514 0.9694 -0.0075 0.2819  -0.1503 255  SER B CB  
4993 N N   . THR B 161 ? 1.2348 1.1052 0.8709 -0.0206 0.2574  -0.1355 256  THR B N   
4994 C CA  . THR B 161 ? 1.1631 1.0361 0.7924 -0.0237 0.2391  -0.1288 256  THR B CA  
4995 C C   . THR B 161 ? 1.1597 1.0411 0.7839 -0.0245 0.2325  -0.1152 256  THR B C   
4996 O O   . THR B 161 ? 1.1898 1.0698 0.7933 -0.0283 0.2388  -0.1136 256  THR B O   
4997 C CB  . THR B 161 ? 1.1547 1.0184 0.7539 -0.0315 0.2348  -0.1377 256  THR B CB  
4998 O OG1 . THR B 161 ? 1.1832 1.0441 0.7529 -0.0370 0.2410  -0.1381 256  THR B OG1 
4999 C CG2 . THR B 161 ? 1.1295 0.9830 0.7321 -0.0312 0.2433  -0.1522 256  THR B CG2 
5000 N N   . ASN B 162 ? 1.0955 0.9848 0.7379 -0.0210 0.2200  -0.1054 257  ASN B N   
5001 C CA  . ASN B 162 ? 1.0745 0.9705 0.7111 -0.0220 0.2130  -0.0928 257  ASN B CA  
5002 C C   . ASN B 162 ? 1.1002 0.9940 0.7105 -0.0281 0.1999  -0.0903 257  ASN B C   
5003 O O   . ASN B 162 ? 1.1422 1.0395 0.7429 -0.0295 0.1941  -0.0802 257  ASN B O   
5004 C CB  . ASN B 162 ? 1.0352 0.9409 0.7014 -0.0158 0.2061  -0.0830 257  ASN B CB  
5005 C CG  . ASN B 162 ? 1.0117 0.9189 0.6921 -0.0138 0.1939  -0.0837 257  ASN B CG  
5006 O OD1 . ASN B 162 ? 1.0266 0.9284 0.6943 -0.0177 0.1883  -0.0902 257  ASN B OD1 
5007 N ND2 . ASN B 162 ? 0.9852 0.9000 0.6920 -0.0081 0.1899  -0.0770 257  ASN B ND2 
5008 N N   . ILE B 163 ? 1.0872 0.9752 0.6861 -0.0319 0.1949  -0.0992 258  ILE B N   
5009 C CA  . ILE B 163 ? 1.1313 1.0166 0.7014 -0.0387 0.1844  -0.0993 258  ILE B CA  
5010 C C   . ILE B 163 ? 1.1905 1.0667 0.7316 -0.0442 0.1961  -0.1079 258  ILE B C   
5011 O O   . ILE B 163 ? 1.2022 1.0711 0.7410 -0.0454 0.2048  -0.1205 258  ILE B O   
5012 C CB  . ILE B 163 ? 1.1117 0.9964 0.6852 -0.0406 0.1722  -0.1046 258  ILE B CB  
5013 C CG1 . ILE B 163 ? 1.0390 0.9332 0.6391 -0.0356 0.1604  -0.0954 258  ILE B CG1 
5014 C CG2 . ILE B 163 ? 1.1282 1.0098 0.6704 -0.0483 0.1624  -0.1069 258  ILE B CG2 
5015 C CD1 . ILE B 163 ? 0.9982 0.8929 0.6024 -0.0380 0.1485  -0.0999 258  ILE B CD1 
5016 N N   . LYS B 164 ? 1.2145 1.0905 0.7333 -0.0474 0.1971  -0.1011 259  LYS B N   
5017 C CA  . LYS B 164 ? 1.2501 1.1179 0.7404 -0.0526 0.2097  -0.1080 259  LYS B CA  
5018 C C   . LYS B 164 ? 1.2889 1.1502 0.7461 -0.0605 0.2018  -0.1144 259  LYS B C   
5019 O O   . LYS B 164 ? 1.3615 1.2185 0.7933 -0.0650 0.2067  -0.1160 259  LYS B O   
5020 C CB  . LYS B 164 ? 1.2383 1.1080 0.7194 -0.0529 0.2159  -0.0974 259  LYS B CB  
5021 C CG  . LYS B 164 ? 1.2057 1.0821 0.7182 -0.0461 0.2247  -0.0917 259  LYS B CG  
5022 C CD  . LYS B 164 ? 1.1985 1.0727 0.7277 -0.0429 0.2407  -0.1032 259  LYS B CD  
5023 C CE  . LYS B 164 ? 1.1512 1.0337 0.7142 -0.0358 0.2472  -0.0972 259  LYS B CE  
5024 N NZ  . LYS B 164 ? 1.1856 1.0683 0.7699 -0.0315 0.2602  -0.1070 259  LYS B NZ  
5025 N N   . TYR B 165 ? 1.2957 1.1587 0.7577 -0.0615 0.1875  -0.1169 260  TYR B N   
5026 C CA  . TYR B 165 ? 1.3350 1.1923 0.7693 -0.0691 0.1799  -0.1254 260  TYR B CA  
5027 C C   . TYR B 165 ? 1.3078 1.1586 0.7511 -0.0698 0.1856  -0.1408 260  TYR B C   
5028 O O   . TYR B 165 ? 1.2778 1.1303 0.7518 -0.0638 0.1903  -0.1423 260  TYR B O   
5029 C CB  . TYR B 165 ? 1.3731 1.2376 0.8052 -0.0706 0.1586  -0.1171 260  TYR B CB  
5030 C CG  . TYR B 165 ? 1.4328 1.3010 0.8481 -0.0713 0.1516  -0.1030 260  TYR B CG  
5031 C CD1 . TYR B 165 ? 1.4145 1.2873 0.8453 -0.0656 0.1562  -0.0911 260  TYR B CD1 
5032 C CD2 . TYR B 165 ? 1.4584 1.3254 0.8426 -0.0776 0.1397  -0.1015 260  TYR B CD2 
5033 C CE1 . TYR B 165 ? 1.4691 1.3440 0.8849 -0.0662 0.1499  -0.0780 260  TYR B CE1 
5034 C CE2 . TYR B 165 ? 1.4836 1.3531 0.8524 -0.0778 0.1328  -0.0878 260  TYR B CE2 
5035 C CZ  . TYR B 165 ? 1.5055 1.3784 0.8904 -0.0721 0.1383  -0.0761 260  TYR B CZ  
5036 O OH  . TYR B 165 ? 1.5746 1.4485 0.9445 -0.0722 0.1319  -0.0622 260  TYR B OH  
5037 N N   . GLU B 166 ? 1.3484 1.1911 0.7641 -0.0773 0.1853  -0.1521 261  GLU B N   
5038 C CA  . GLU B 166 ? 1.3396 1.1747 0.7612 -0.0789 0.1900  -0.1673 261  GLU B CA  
5039 C C   . GLU B 166 ? 1.3406 1.1754 0.7501 -0.0856 0.1737  -0.1721 261  GLU B C   
5040 O O   . GLU B 166 ? 1.3899 1.2287 0.7776 -0.0903 0.1608  -0.1663 261  GLU B O   
5041 C CB  . GLU B 166 ? 1.3521 1.1811 0.7641 -0.0799 0.2020  -0.1758 261  GLU B CB  
5042 C CG  . GLU B 166 ? 1.3470 1.1751 0.7843 -0.0725 0.2191  -0.1777 261  GLU B CG  
5043 C CD  . GLU B 166 ? 1.4033 1.2294 0.8295 -0.0728 0.2309  -0.1801 261  GLU B CD  
5044 O OE1 . GLU B 166 ? 1.4326 1.2618 0.8772 -0.0669 0.2431  -0.1768 261  GLU B OE1 
5045 O OE2 . GLU B 166 ? 1.3886 1.2106 0.7880 -0.0791 0.2278  -0.1852 261  GLU B OE2 
5046 N N   . ALA B 167 ? 1.2975 1.1282 0.7238 -0.0855 0.1735  -0.1819 262  ALA B N   
5047 C CA  . ALA B 167 ? 1.3058 1.1368 0.7264 -0.0919 0.1588  -0.1876 262  ALA B CA  
5048 C C   . ALA B 167 ? 1.3203 1.1379 0.7238 -0.0982 0.1671  -0.2057 262  ALA B C   
5049 O O   . ALA B 167 ? 1.3041 1.1144 0.7254 -0.0943 0.1797  -0.2135 262  ALA B O   
5050 C CB  . ALA B 167 ? 1.2823 1.1199 0.7381 -0.0873 0.1503  -0.1835 262  ALA B CB  
5051 N N   . HIS B 168 ? 1.3247 1.1420 0.7020 -0.1057 0.1576  -0.2094 263  HIS B N   
5052 C CA  . HIS B 168 ? 1.3187 1.1266 0.6867 -0.1107 0.1608  -0.2241 263  HIS B CA  
5053 C C   . HIS B 168 ? 1.3064 1.1127 0.6804 -0.1165 0.1498  -0.2322 263  HIS B C   
5054 O O   . HIS B 168 ? 1.3303 1.1447 0.6966 -0.1211 0.1335  -0.2274 263  HIS B O   
5055 C CB  . HIS B 168 ? 1.3328 1.1410 0.6691 -0.1159 0.1569  -0.2243 263  HIS B CB  
5056 C CG  . HIS B 168 ? 1.3620 1.1721 0.6923 -0.1109 0.1673  -0.2156 263  HIS B CG  
5057 N ND1 . HIS B 168 ? 1.4005 1.2037 0.7294 -0.1088 0.1832  -0.2222 263  HIS B ND1 
5058 C CD2 . HIS B 168 ? 1.4241 1.2422 0.7515 -0.1077 0.1647  -0.2007 263  HIS B CD2 
5059 C CE1 . HIS B 168 ? 1.4350 1.2426 0.7600 -0.1050 0.1898  -0.2119 263  HIS B CE1 
5060 N NE2 . HIS B 168 ? 1.4553 1.2715 0.7793 -0.1042 0.1789  -0.1987 263  HIS B NE2 
5061 N N   . ILE B 169 ? 1.2840 1.0802 0.6733 -0.1160 0.1587  -0.2441 264  ILE B N   
5062 C CA  . ILE B 169 ? 1.3196 1.1133 0.7238 -0.1194 0.1520  -0.2506 264  ILE B CA  
5063 C C   . ILE B 169 ? 1.3540 1.1461 0.7391 -0.1299 0.1398  -0.2603 264  ILE B C   
5064 O O   . ILE B 169 ? 1.3697 1.1519 0.7466 -0.1329 0.1459  -0.2718 264  ILE B O   
5065 C CB  . ILE B 169 ? 1.3092 1.0919 0.7388 -0.1140 0.1668  -0.2583 264  ILE B CB  
5066 C CG1 . ILE B 169 ? 1.2444 1.0315 0.6973 -0.1035 0.1756  -0.2472 264  ILE B CG1 
5067 C CG2 . ILE B 169 ? 1.2753 1.0526 0.7167 -0.1193 0.1604  -0.2671 264  ILE B CG2 
5068 C CD1 . ILE B 169 ? 1.2174 0.9940 0.6940 -0.0967 0.1911  -0.2534 264  ILE B CD1 
5069 N N   . ARG B 170 ? 1.3522 1.1545 0.7309 -0.1354 0.1222  -0.2556 265  ARG B N   
5070 C CA  . ARG B 170 ? 1.3692 1.1717 0.7352 -0.1455 0.1090  -0.2649 265  ARG B CA  
5071 C C   . ARG B 170 ? 1.3904 1.1860 0.7772 -0.1489 0.1094  -0.2754 265  ARG B C   
5072 O O   . ARG B 170 ? 1.4081 1.1968 0.7887 -0.1559 0.1071  -0.2876 265  ARG B O   
5073 C CB  . ARG B 170 ? 1.3984 1.2160 0.7517 -0.1498 0.0891  -0.2553 265  ARG B CB  
5074 C CG  . ARG B 170 ? 1.4983 1.3184 0.8253 -0.1580 0.0768  -0.2603 265  ARG B CG  
5075 C CD  . ARG B 170 ? 1.5177 1.3464 0.8223 -0.1560 0.0704  -0.2477 265  ARG B CD  
5076 N NE  . ARG B 170 ? 1.4826 1.3164 0.7639 -0.1636 0.0548  -0.2503 265  ARG B NE  
5077 N N   . LYS B 171 ? 1.3690 1.1693 0.7899 -0.1411 0.1106  -0.2665 266  LYS B N   
5078 C CA  . LYS B 171 ? 1.3330 1.1277 0.7805 -0.1417 0.1117  -0.2725 266  LYS B CA  
5079 C C   . LYS B 171 ? 1.2704 1.0658 0.7499 -0.1299 0.1213  -0.2624 266  LYS B C   
5080 O O   . LYS B 171 ? 1.2276 1.0334 0.7134 -0.1222 0.1207  -0.2483 266  LYS B O   
5081 C CB  . LYS B 171 ? 1.3763 1.1831 0.8332 -0.1481 0.0925  -0.2700 266  LYS B CB  
5082 C CG  . LYS B 171 ? 1.4556 1.2590 0.8871 -0.1612 0.0836  -0.2841 266  LYS B CG  
5083 C CD  . LYS B 171 ? 1.4909 1.3128 0.9229 -0.1663 0.0619  -0.2770 266  LYS B CD  
5084 C CE  . LYS B 171 ? 1.5215 1.3439 0.9705 -0.1741 0.0537  -0.2850 266  LYS B CE  
5085 N NZ  . LYS B 171 ? 1.5215 1.3527 0.9513 -0.1856 0.0364  -0.2909 266  LYS B NZ  
5086 N N   . ILE B 172 ? 1.2986 1.0824 0.7979 -0.1285 0.1298  -0.2697 267  ILE B N   
5087 C CA  . ILE B 172 ? 1.2145 0.9988 0.7455 -0.1178 0.1373  -0.2604 267  ILE B CA  
5088 C C   . ILE B 172 ? 1.2477 1.0242 0.8015 -0.1198 0.1371  -0.2659 267  ILE B C   
5089 O O   . ILE B 172 ? 1.2658 1.0262 0.8135 -0.1249 0.1442  -0.2806 267  ILE B O   
5090 C CB  . ILE B 172 ? 1.1866 0.9613 0.7166 -0.1098 0.1559  -0.2621 267  ILE B CB  
5091 C CG1 . ILE B 172 ? 1.1174 0.8900 0.6813 -0.0998 0.1635  -0.2555 267  ILE B CG1 
5092 C CG2 . ILE B 172 ? 1.2001 0.9568 0.7082 -0.1157 0.1675  -0.2804 267  ILE B CG2 
5093 C CD1 . ILE B 172 ? 1.1379 0.9083 0.7070 -0.0899 0.1784  -0.2515 267  ILE B CD1 
5094 N N   . PHE B 173 ? 1.2129 1.0001 0.7926 -0.1158 0.1293  -0.2541 268  PHE B N   
5095 C CA  . PHE B 173 ? 1.1987 0.9796 0.8018 -0.1170 0.1291  -0.2567 268  PHE B CA  
5096 C C   . PHE B 173 ? 1.1311 0.9135 0.7620 -0.1053 0.1359  -0.2450 268  PHE B C   
5097 O O   . PHE B 173 ? 1.1112 0.9056 0.7466 -0.0978 0.1348  -0.2326 268  PHE B O   
5098 C CB  . PHE B 173 ? 1.2159 1.0092 0.8241 -0.1249 0.1120  -0.2543 268  PHE B CB  
5099 C CG  . PHE B 173 ? 1.2775 1.0721 0.8587 -0.1366 0.1028  -0.2648 268  PHE B CG  
5100 C CD1 . PHE B 173 ? 1.3194 1.0974 0.8867 -0.1450 0.1082  -0.2820 268  PHE B CD1 
5101 C CD2 . PHE B 173 ? 1.2884 1.1006 0.8585 -0.1391 0.0883  -0.2574 268  PHE B CD2 
5102 C CE1 . PHE B 173 ? 1.3584 1.1380 0.9001 -0.1563 0.0990  -0.2919 268  PHE B CE1 
5103 C CE2 . PHE B 173 ? 1.3791 1.1932 0.9241 -0.1498 0.0787  -0.2665 268  PHE B CE2 
5104 C CZ  . PHE B 173 ? 1.3901 1.1882 0.9204 -0.1586 0.0839  -0.2840 268  PHE B CZ  
5105 N N   . CYS B 174 ? 1.1127 0.8826 0.7622 -0.1037 0.1428  -0.2488 269  CYS B N   
5106 C CA  . CYS B 174 ? 1.0956 0.8657 0.7712 -0.0928 0.1491  -0.2383 269  CYS B CA  
5107 C C   . CYS B 174 ? 1.0675 0.8431 0.7650 -0.0945 0.1403  -0.2316 269  CYS B C   
5108 O O   . CYS B 174 ? 1.1038 0.8688 0.8055 -0.1012 0.1399  -0.2399 269  CYS B O   
5109 C CB  . CYS B 174 ? 1.0775 0.8282 0.7581 -0.0878 0.1655  -0.2464 269  CYS B CB  
5110 S SG  . CYS B 174 ? 1.0328 0.7824 0.7461 -0.0749 0.1723  -0.2341 269  CYS B SG  
5111 N N   . ILE B 175 ? 1.0102 0.8018 0.7216 -0.0886 0.1337  -0.2169 270  ILE B N   
5112 C CA  . ILE B 175 ? 0.9961 0.7945 0.7277 -0.0902 0.1255  -0.2100 270  ILE B CA  
5113 C C   . ILE B 175 ? 0.9577 0.7490 0.7129 -0.0818 0.1335  -0.2034 270  ILE B C   
5114 O O   . ILE B 175 ? 0.9186 0.7093 0.6897 -0.0841 0.1299  -0.2006 270  ILE B O   
5115 C CB  . ILE B 175 ? 0.9811 0.8014 0.7152 -0.0896 0.1125  -0.1982 270  ILE B CB  
5116 C CG1 . ILE B 175 ? 0.9578 0.7862 0.6975 -0.0785 0.1162  -0.1862 270  ILE B CG1 
5117 C CG2 . ILE B 175 ? 0.9994 0.8270 0.7106 -0.0979 0.1032  -0.2039 270  ILE B CG2 
5118 C CD1 . ILE B 175 ? 0.9423 0.7904 0.6898 -0.0766 0.1047  -0.1737 270  ILE B CD1 
5119 N N   . SER B 176 ? 0.9495 0.7356 0.7074 -0.0723 0.1441  -0.2009 271  SER B N   
5120 C CA  . SER B 176 ? 0.9268 0.7054 0.7062 -0.0638 0.1516  -0.1949 271  SER B CA  
5121 C C   . SER B 176 ? 0.9495 0.7146 0.7254 -0.0575 0.1656  -0.2011 271  SER B C   
5122 O O   . SER B 176 ? 0.9403 0.7118 0.7091 -0.0522 0.1695  -0.1986 271  SER B O   
5123 C CB  . SER B 176 ? 0.8961 0.6907 0.6907 -0.0561 0.1468  -0.1792 271  SER B CB  
5124 O OG  . SER B 176 ? 0.8649 0.6523 0.6793 -0.0484 0.1531  -0.1735 271  SER B OG  
5125 N N   . LYS B 177 ? 0.9762 0.7226 0.7577 -0.0580 0.1736  -0.2092 272  LYS B N   
5126 C CA  . LYS B 177 ? 0.9932 0.7250 0.7729 -0.0522 0.1876  -0.2167 272  LYS B CA  
5127 C C   . LYS B 177 ? 0.9464 0.6758 0.7494 -0.0404 0.1937  -0.2070 272  LYS B C   
5128 O O   . LYS B 177 ? 0.9268 0.6523 0.7459 -0.0397 0.1909  -0.2014 272  LYS B O   
5129 C CB  . LYS B 177 ? 1.0210 0.7322 0.7928 -0.0597 0.1929  -0.2321 272  LYS B CB  
5130 C CG  . LYS B 177 ? 1.0736 0.7672 0.8469 -0.0533 0.2082  -0.2406 272  LYS B CG  
5131 C CD  . LYS B 177 ? 1.1431 0.8152 0.9105 -0.0611 0.2129  -0.2556 272  LYS B CD  
5132 C CE  . LYS B 177 ? 1.2185 0.8719 1.0044 -0.0529 0.2242  -0.2566 272  LYS B CE  
5133 N NZ  . LYS B 177 ? 1.2226 0.8756 1.0123 -0.0414 0.2357  -0.2559 272  LYS B NZ  
5134 N N   . THR B 178 ? 0.9625 0.6950 0.7673 -0.0315 0.2017  -0.2046 273  THR B N   
5135 C CA  . THR B 178 ? 0.9518 0.6808 0.7783 -0.0200 0.2083  -0.1971 273  THR B CA  
5136 C C   . THR B 178 ? 0.9585 0.6660 0.7943 -0.0198 0.2148  -0.2039 273  THR B C   
5137 O O   . THR B 178 ? 0.9968 0.6892 0.8216 -0.0241 0.2219  -0.2176 273  THR B O   
5138 C CB  . THR B 178 ? 0.9151 0.6473 0.7405 -0.0119 0.2183  -0.1981 273  THR B CB  
5139 O OG1 . THR B 178 ? 0.9530 0.7047 0.7708 -0.0120 0.2124  -0.1906 273  THR B OG1 
5140 C CG2 . THR B 178 ? 0.8849 0.6139 0.7340 0.0002  0.2249  -0.1910 273  THR B CG2 
5141 N N   . ALA B 179 ? 0.9663 0.6716 0.8214 -0.0153 0.2121  -0.1943 274  ALA B N   
5142 C CA  . ALA B 179 ? 1.0033 0.6874 0.8675 -0.0156 0.2172  -0.1991 274  ALA B CA  
5143 C C   . ALA B 179 ? 0.9863 0.6591 0.8656 -0.0035 0.2285  -0.1983 274  ALA B C   
5144 O O   . ALA B 179 ? 1.0143 0.6664 0.8979 -0.0032 0.2356  -0.2057 274  ALA B O   
5145 C CB  . ALA B 179 ? 0.9283 0.6140 0.8041 -0.0185 0.2083  -0.1892 274  ALA B CB  
5146 N N   . LYS B 180 ? 0.9922 0.6782 0.8801 0.0063  0.2301  -0.1899 275  LYS B N   
5147 C CA  . LYS B 180 ? 0.9946 0.6742 0.9015 0.0188  0.2382  -0.1857 275  LYS B CA  
5148 C C   . LYS B 180 ? 0.9876 0.6782 0.8934 0.0256  0.2450  -0.1869 275  LYS B C   
5149 O O   . LYS B 180 ? 0.9618 0.6698 0.8574 0.0227  0.2403  -0.1840 275  LYS B O   
5150 C CB  . LYS B 180 ? 0.9717 0.6584 0.8966 0.0245  0.2307  -0.1696 275  LYS B CB  
5151 C CG  . LYS B 180 ? 1.0203 0.7045 0.9656 0.0380  0.2367  -0.1629 275  LYS B CG  
5152 C CD  . LYS B 180 ? 1.0001 0.7008 0.9577 0.0433  0.2278  -0.1467 275  LYS B CD  
5153 C CE  . LYS B 180 ? 1.0507 0.7411 1.0186 0.0436  0.2232  -0.1387 275  LYS B CE  
5154 N NZ  . LYS B 180 ? 1.0818 0.7730 1.0697 0.0562  0.2245  -0.1281 275  LYS B NZ  
5155 N N   . GLU B 181 ? 0.9847 0.6650 0.9018 0.0347  0.2564  -0.1911 276  GLU B N   
5156 C CA  . GLU B 181 ? 1.0176 0.7086 0.9375 0.0420  0.2640  -0.1917 276  GLU B CA  
5157 C C   . GLU B 181 ? 0.9915 0.7039 0.9236 0.0481  0.2566  -0.1764 276  GLU B C   
5158 O O   . GLU B 181 ? 0.9453 0.6593 0.8928 0.0525  0.2502  -0.1652 276  GLU B O   
5159 C CB  . GLU B 181 ? 1.0185 0.6949 0.9530 0.0518  0.2771  -0.1978 276  GLU B CB  
5160 C CG  . GLU B 181 ? 1.1024 0.7858 1.0356 0.0568  0.2881  -0.2041 276  GLU B CG  
5161 C CD  . GLU B 181 ? 1.1952 0.8741 1.1049 0.0471  0.2919  -0.2176 276  GLU B CD  
5162 O OE1 . GLU B 181 ? 1.2415 0.9037 1.1417 0.0401  0.2917  -0.2262 276  GLU B OE1 
5163 O OE2 . GLU B 181 ? 1.2185 0.9104 1.1190 0.0462  0.2950  -0.2194 276  GLU B OE2 
5164 N N   . LEU B 182 ? 0.9239 0.6522 0.8483 0.0478  0.2576  -0.1759 277  LEU B N   
5165 C CA  . LEU B 182 ? 0.9523 0.7009 0.8867 0.0523  0.2506  -0.1623 277  LEU B CA  
5166 C C   . LEU B 182 ? 0.8814 0.6319 0.8411 0.0652  0.2554  -0.1558 277  LEU B C   
5167 O O   . LEU B 182 ? 0.9256 0.6662 0.8930 0.0712  0.2666  -0.1631 277  LEU B O   
5168 C CB  . LEU B 182 ? 0.8971 0.6606 0.8167 0.0485  0.2513  -0.1637 277  LEU B CB  
5169 C CG  . LEU B 182 ? 0.9231 0.6950 0.8249 0.0383  0.2396  -0.1606 277  LEU B CG  
5170 C CD1 . LEU B 182 ? 0.9283 0.6898 0.8062 0.0281  0.2415  -0.1736 277  LEU B CD1 
5171 C CD2 . LEU B 182 ? 0.9036 0.6955 0.8033 0.0391  0.2357  -0.1525 277  LEU B CD2 
5172 N N   . PRO B 183 ? 0.8891 0.6525 0.8623 0.0698  0.2469  -0.1422 278  PRO B N   
5173 C CA  . PRO B 183 ? 0.8557 0.6227 0.8532 0.0821  0.2502  -0.1355 278  PRO B CA  
5174 C C   . PRO B 183 ? 0.8624 0.6404 0.8650 0.0874  0.2592  -0.1386 278  PRO B C   
5175 O O   . PRO B 183 ? 0.8694 0.6472 0.8918 0.0976  0.2656  -0.1377 278  PRO B O   
5176 C CB  . PRO B 183 ? 0.8176 0.5976 0.8232 0.0834  0.2376  -0.1208 278  PRO B CB  
5177 C CG  . PRO B 183 ? 0.8073 0.5971 0.7935 0.0730  0.2302  -0.1203 278  PRO B CG  
5178 C CD  . PRO B 183 ? 0.8349 0.6104 0.8022 0.0642  0.2339  -0.1326 278  PRO B CD  
5179 N N   . PHE B 184 ? 0.8311 0.6192 0.8168 0.0806  0.2597  -0.1420 279  PHE B N   
5180 C CA  . PHE B 184 ? 0.8234 0.6207 0.8095 0.0832  0.2696  -0.1466 279  PHE B CA  
5181 C C   . PHE B 184 ? 0.8335 0.6328 0.7922 0.0723  0.2697  -0.1530 279  PHE B C   
5182 O O   . PHE B 184 ? 0.8262 0.6240 0.7698 0.0641  0.2603  -0.1515 279  PHE B O   
5183 C CB  . PHE B 184 ? 0.8125 0.6294 0.8164 0.0900  0.2664  -0.1354 279  PHE B CB  
5184 C CG  . PHE B 184 ? 0.8017 0.6303 0.8028 0.0862  0.2522  -0.1237 279  PHE B CG  
5185 C CD1 . PHE B 184 ? 0.7776 0.6088 0.7955 0.0917  0.2438  -0.1131 279  PHE B CD1 
5186 C CD2 . PHE B 184 ? 0.7663 0.6030 0.7476 0.0773  0.2474  -0.1232 279  PHE B CD2 
5187 C CE1 . PHE B 184 ? 0.7641 0.6058 0.7794 0.0883  0.2317  -0.1031 279  PHE B CE1 
5188 C CE2 . PHE B 184 ? 0.7478 0.5950 0.7277 0.0743  0.2349  -0.1129 279  PHE B CE2 
5189 C CZ  . PHE B 184 ? 0.7777 0.6274 0.7745 0.0797  0.2274  -0.1032 279  PHE B CZ  
5190 N N   . LEU B 185 ? 0.8310 0.6341 0.7837 0.0723  0.2804  -0.1600 280  LEU B N   
5191 C CA  . LEU B 185 ? 0.8497 0.6544 0.7750 0.0624  0.2813  -0.1660 280  LEU B CA  
5192 C C   . LEU B 185 ? 0.8221 0.6456 0.7436 0.0599  0.2735  -0.1556 280  LEU B C   
5193 O O   . LEU B 185 ? 0.8279 0.6643 0.7666 0.0664  0.2750  -0.1485 280  LEU B O   
5194 C CB  . LEU B 185 ? 0.7948 0.5961 0.7140 0.0624  0.2943  -0.1766 280  LEU B CB  
5195 C CG  . LEU B 185 ? 0.8706 0.6556 0.7953 0.0646  0.2995  -0.1854 280  LEU B CG  
5196 C CD1 . LEU B 185 ? 0.8176 0.6062 0.7475 0.0677  0.3092  -0.1907 280  LEU B CD1 
5197 C CD2 . LEU B 185 ? 0.8575 0.6269 0.7577 0.0547  0.2976  -0.1950 280  LEU B CD2 
5198 N N   . LEU B 186 ? 0.7949 0.6199 0.6943 0.0504  0.2651  -0.1549 281  LEU B N   
5199 C CA  . LEU B 186 ? 0.8169 0.6581 0.7108 0.0477  0.2581  -0.1457 281  LEU B CA  
5200 C C   . LEU B 186 ? 0.8335 0.6824 0.7241 0.0487  0.2689  -0.1480 281  LEU B C   
5201 O O   . LEU B 186 ? 0.8078 0.6712 0.7047 0.0502  0.2662  -0.1391 281  LEU B O   
5202 C CB  . LEU B 186 ? 0.8019 0.6424 0.6723 0.0376  0.2477  -0.1454 281  LEU B CB  
5203 C CG  . LEU B 186 ? 0.8534 0.6940 0.7311 0.0368  0.2344  -0.1382 281  LEU B CG  
5204 C CD1 . LEU B 186 ? 0.8722 0.7148 0.7290 0.0272  0.2238  -0.1374 281  LEU B CD1 
5205 C CD2 . LEU B 186 ? 0.7724 0.6260 0.6717 0.0437  0.2293  -0.1257 281  LEU B CD2 
5206 N N   . LYS B 187 ? 0.8201 0.6595 0.7011 0.0477  0.2817  -0.1599 282  LYS B N   
5207 C CA  . LYS B 187 ? 0.8067 0.6541 0.6867 0.0488  0.2924  -0.1617 282  LYS B CA  
5208 C C   . LYS B 187 ? 0.8429 0.7017 0.7541 0.0586  0.2948  -0.1547 282  LYS B C   
5209 O O   . LYS B 187 ? 0.8497 0.7226 0.7661 0.0594  0.2962  -0.1488 282  LYS B O   
5210 C CB  . LYS B 187 ? 0.8365 0.6741 0.7041 0.0455  0.3001  -0.1732 282  LYS B CB  
5211 N N   . ASP B 188 ? 0.8412 0.6941 0.7734 0.0660  0.2949  -0.1551 283  ASP B N   
5212 C CA  . ASP B 188 ? 0.7871 0.6510 0.7496 0.0757  0.2955  -0.1480 283  ASP B CA  
5213 C C   . ASP B 188 ? 0.8017 0.6774 0.7733 0.0777  0.2874  -0.1365 283  ASP B C   
5214 O O   . ASP B 188 ? 0.8076 0.6983 0.7957 0.0818  0.2877  -0.1300 283  ASP B O   
5215 C CB  . ASP B 188 ? 0.7982 0.6513 0.7790 0.0830  0.2967  -0.1508 283  ASP B CB  
5216 C CG  . ASP B 188 ? 0.8682 0.7126 0.8461 0.0829  0.3059  -0.1614 283  ASP B CG  
5217 O OD1 . ASP B 188 ? 0.8390 0.6874 0.8023 0.0777  0.3116  -0.1661 283  ASP B OD1 
5218 O OD2 . ASP B 188 ? 0.8634 0.6968 0.8536 0.0882  0.3075  -0.1647 283  ASP B OD2 
5219 N N   . ALA B 189 ? 0.7544 0.6265 0.7165 0.0732  0.2743  -0.1316 284  ALA B N   
5220 C CA  . ALA B 189 ? 0.7855 0.6700 0.7576 0.0743  0.2617  -0.1188 284  ALA B CA  
5221 C C   . ALA B 189 ? 0.7564 0.6542 0.7181 0.0692  0.2594  -0.1137 284  ALA B C   
5222 O O   . ALA B 189 ? 0.7195 0.6303 0.6944 0.0718  0.2531  -0.1042 284  ALA B O   
5223 C CB  . ALA B 189 ? 0.7710 0.6478 0.7360 0.0707  0.2495  -0.1157 284  ALA B CB  
5224 N N   . ASN B 190 ? 0.7662 0.6604 0.7042 0.0619  0.2643  -0.1200 285  ASN B N   
5225 C CA  . ASN B 190 ? 0.7753 0.6797 0.7007 0.0566  0.2626  -0.1152 285  ASN B CA  
5226 C C   . ASN B 190 ? 0.7819 0.6964 0.7180 0.0598  0.2739  -0.1153 285  ASN B C   
5227 O O   . ASN B 190 ? 0.7469 0.6720 0.6797 0.0569  0.2718  -0.1088 285  ASN B O   
5228 C CB  . ASN B 190 ? 0.7767 0.6727 0.6707 0.0474  0.2629  -0.1214 285  ASN B CB  
5229 C CG  . ASN B 190 ? 0.7646 0.6593 0.6463 0.0420  0.2480  -0.1163 285  ASN B CG  
5230 O OD1 . ASN B 190 ? 0.7473 0.6522 0.6335 0.0417  0.2387  -0.1064 285  ASN B OD1 
5231 N ND2 . ASN B 190 ? 0.7746 0.6570 0.6413 0.0374  0.2459  -0.1235 285  ASN B ND2 
5232 N N   . MET B 191 ? 0.7764 0.6880 0.7261 0.0656  0.2860  -0.1224 286  MET B N   
5233 C CA  . MET B 191 ? 0.8034 0.7254 0.7615 0.0665  0.2942  -0.1227 286  MET B CA  
5234 C C   . MET B 191 ? 0.7818 0.7197 0.7662 0.0723  0.2914  -0.1135 286  MET B C   
5235 O O   . MET B 191 ? 0.8141 0.7539 0.8176 0.0788  0.2859  -0.1091 286  MET B O   
5236 C CB  . MET B 191 ? 0.8387 0.7546 0.8044 0.0700  0.3025  -0.1315 286  MET B CB  
5237 C CG  . MET B 191 ? 0.8504 0.7568 0.7894 0.0626  0.3087  -0.1405 286  MET B CG  
5238 S SD  . MET B 191 ? 1.1916 1.0880 1.1396 0.0671  0.3176  -0.1514 286  MET B SD  
5239 C CE  . MET B 191 ? 1.0128 0.9255 0.9980 0.0769  0.3213  -0.1462 286  MET B CE  
5240 N N   . LYS B 192 ? 0.8024 0.7519 0.7871 0.0694  0.2951  -0.1105 287  LYS B N   
5241 C CA  . LYS B 192 ? 0.8280 0.7935 0.8382 0.0741  0.2933  -0.1030 287  LYS B CA  
5242 C C   . LYS B 192 ? 0.8693 0.8387 0.9060 0.0822  0.2974  -0.1059 287  LYS B C   
5243 O O   . LYS B 192 ? 0.9464 0.9106 0.9801 0.0822  0.3054  -0.1137 287  LYS B O   
5244 C CB  . LYS B 192 ? 0.7918 0.7671 0.7943 0.0680  0.2970  -0.0998 287  LYS B CB  
5245 C CG  . LYS B 192 ? 0.8505 0.8428 0.8792 0.0716  0.2964  -0.0934 287  LYS B CG  
5246 C CD  . LYS B 192 ? 0.8692 0.8689 0.8873 0.0645  0.2984  -0.0889 287  LYS B CD  
5247 C CE  . LYS B 192 ? 0.9403 0.9308 0.9293 0.0569  0.3052  -0.0942 287  LYS B CE  
5248 N NZ  . LYS B 192 ? 1.0626 1.0605 1.0437 0.0505  0.3084  -0.0895 287  LYS B NZ  
5249 N N   . GLU B 193 ? 0.8293 0.8077 0.8915 0.0892  0.2916  -0.0997 288  GLU B N   
5250 C CA  . GLU B 193 ? 0.9500 0.9311 1.0381 0.0980  0.2934  -0.1015 288  GLU B CA  
5251 C C   . GLU B 193 ? 1.0463 1.0421 1.1510 0.0991  0.2998  -0.1018 288  GLU B C   
5252 O O   . GLU B 193 ? 1.0974 1.1081 1.2168 0.0998  0.2964  -0.0952 288  GLU B O   
5253 C CB  . GLU B 193 ? 0.9990 0.9837 1.1068 0.1052  0.2837  -0.0942 288  GLU B CB  
5254 C CG  . GLU B 193 ? 0.9990 0.9678 1.0954 0.1059  0.2785  -0.0947 288  GLU B CG  
5255 C CD  . GLU B 193 ? 1.0259 0.9981 1.1428 0.1137  0.2694  -0.0871 288  GLU B CD  
5256 O OE1 . GLU B 193 ? 1.0357 1.0210 1.1773 0.1198  0.2677  -0.0830 288  GLU B OE1 
5257 O OE2 . GLU B 193 ? 0.9413 0.9036 1.0481 0.1125  0.2612  -0.0844 288  GLU B OE2 
5258 N N   . THR B 194 ? 1.0640 1.0556 1.1665 0.0991  0.3093  -0.1098 289  THR B N   
5259 C CA  . THR B 194 ? 1.1347 1.1395 1.2590 0.1028  0.3156  -0.1110 289  THR B CA  
5260 C C   . THR B 194 ? 1.1688 1.1765 1.3217 0.1135  0.3117  -0.1095 289  THR B C   
5261 O O   . THR B 194 ? 1.1672 1.1619 1.3187 0.1176  0.3090  -0.1116 289  THR B O   
5262 C CB  . THR B 194 ? 1.0810 1.0798 1.1927 0.0994  0.3276  -0.1203 289  THR B CB  
5263 O OG1 . THR B 194 ? 1.0870 1.0753 1.2055 0.1056  0.3306  -0.1268 289  THR B OG1 
5264 C CG2 . THR B 194 ? 1.0579 1.0457 1.1345 0.0896  0.3297  -0.1232 289  THR B CG2 
5265 N N   . ASN B 195 ? 1.1915 1.2164 1.3705 0.1179  0.3110  -0.1056 290  ASN B N   
5266 C CA  . ASN B 195 ? 1.2013 1.2303 1.4081 0.1284  0.3073  -0.1040 290  ASN B CA  
5267 C C   . ASN B 195 ? 1.1852 1.2135 1.4027 0.1326  0.3172  -0.1117 290  ASN B C   
5268 O O   . ASN B 195 ? 1.2016 1.2414 1.4464 0.1402  0.3164  -0.1101 290  ASN B O   
5269 C CB  . ASN B 195 ? 1.2448 1.2931 1.4756 0.1316  0.2997  -0.0955 290  ASN B CB  
5270 C CG  . ASN B 195 ? 1.2798 1.3282 1.5025 0.1287  0.2894  -0.0878 290  ASN B CG  
5271 O OD1 . ASN B 195 ? 1.2757 1.3123 1.4730 0.1226  0.2890  -0.0886 290  ASN B OD1 
5272 N ND2 . ASN B 195 ? 1.3321 1.3942 1.5764 0.1333  0.2806  -0.0804 290  ASN B ND2 
5273 N N   . GLU B 196 ? 1.1847 1.2002 1.3812 0.1280  0.3263  -0.1201 291  GLU B N   
5274 C CA  . GLU B 196 ? 1.2088 1.2211 1.4135 0.1322  0.3361  -0.1282 291  GLU B CA  
5275 C C   . GLU B 196 ? 1.2046 1.2041 1.4185 0.1407  0.3326  -0.1299 291  GLU B C   
5276 O O   . GLU B 196 ? 1.1556 1.1438 1.3604 0.1408  0.3249  -0.1269 291  GLU B O   
5277 C CB  . GLU B 196 ? 1.2007 1.2031 1.3784 0.1241  0.3468  -0.1369 291  GLU B CB  
5278 C CG  . GLU B 196 ? 1.2068 1.2188 1.3710 0.1149  0.3505  -0.1351 291  GLU B CG  
5279 C CD  . GLU B 196 ? 1.2671 1.2993 1.4557 0.1171  0.3543  -0.1326 291  GLU B CD  
5280 O OE1 . GLU B 196 ? 1.2629 1.2997 1.4727 0.1242  0.3595  -0.1364 291  GLU B OE1 
5281 O OE2 . GLU B 196 ? 1.2698 1.3134 1.4571 0.1118  0.3522  -0.1268 291  GLU B OE2 
5282 N N   . GLU B 197 ? 1.2479 1.2490 1.4804 0.1477  0.3387  -0.1345 292  GLU B N   
5283 C CA  . GLU B 197 ? 1.2831 1.2708 1.5241 0.1558  0.3365  -0.1364 292  GLU B CA  
5284 C C   . GLU B 197 ? 1.2776 1.2432 1.4917 0.1508  0.3418  -0.1448 292  GLU B C   
5285 O O   . GLU B 197 ? 1.2510 1.2132 1.4474 0.1442  0.3514  -0.1525 292  GLU B O   
5286 C CB  . GLU B 197 ? 1.3410 1.3365 1.6094 0.1650  0.3418  -0.1391 292  GLU B CB  
5287 C CG  . GLU B 197 ? 1.4068 1.4225 1.7050 0.1718  0.3341  -0.1303 292  GLU B CG  
5288 C CD  . GLU B 197 ? 1.4956 1.5147 1.8217 0.1832  0.3357  -0.1317 292  GLU B CD  
5289 O OE1 . GLU B 197 ? 1.4900 1.4937 1.8123 0.1863  0.3419  -0.1388 292  GLU B OE1 
5290 O OE2 . GLU B 197 ? 1.5484 1.5857 1.9003 0.1889  0.3306  -0.1257 292  GLU B OE2 
5291 N N   . GLY B 198 ? 1.1369 1.0874 1.3474 0.1537  0.3352  -0.1433 293  GLY B N   
5292 C CA  . GLY B 198 ? 1.0587 0.9881 1.2437 0.1483  0.3384  -0.1508 293  GLY B CA  
5293 C C   . GLY B 198 ? 1.1004 1.0266 1.2560 0.1372  0.3369  -0.1509 293  GLY B C   
5294 O O   . GLY B 198 ? 1.1024 1.0123 1.2343 0.1313  0.3401  -0.1581 293  GLY B O   
5295 N N   . SER B 199 ? 1.0850 1.0260 1.2411 0.1340  0.3319  -0.1433 294  SER B N   
5296 C CA  . SER B 199 ? 1.0817 1.0207 1.2105 0.1237  0.3303  -0.1428 294  SER B CA  
5297 C C   . SER B 199 ? 1.0178 0.9430 1.1333 0.1219  0.3219  -0.1404 294  SER B C   
5298 O O   . SER B 199 ? 1.0043 0.9254 1.1346 0.1287  0.3153  -0.1360 294  SER B O   
5299 C CB  . SER B 199 ? 1.0857 1.0439 1.2205 0.1212  0.3269  -0.1348 294  SER B CB  
5300 O OG  . SER B 199 ? 1.0405 1.0064 1.1941 0.1268  0.3165  -0.1253 294  SER B OG  
5301 N N   . ILE B 200 ? 0.9671 0.8849 1.0537 0.1124  0.3221  -0.1434 295  ILE B N   
5302 C CA  . ILE B 200 ? 0.9718 0.8779 1.0436 0.1093  0.3144  -0.1414 295  ILE B CA  
5303 C C   . ILE B 200 ? 0.9673 0.8844 1.0519 0.1122  0.3044  -0.1299 295  ILE B C   
5304 O O   . ILE B 200 ? 0.9318 0.8636 1.0176 0.1096  0.3030  -0.1246 295  ILE B O   
5305 C CB  . ILE B 200 ? 0.9680 0.8670 1.0065 0.0982  0.3163  -0.1465 295  ILE B CB  
5306 C CG1 . ILE B 200 ? 0.9708 0.8598 0.9958 0.0950  0.3264  -0.1581 295  ILE B CG1 
5307 C CG2 . ILE B 200 ? 0.9464 0.8343 0.9703 0.0947  0.3083  -0.1447 295  ILE B CG2 
5308 C CD1 . ILE B 200 ? 0.9508 0.8203 0.9710 0.0961  0.3270  -0.1654 295  ILE B CD1 
5309 N N   . LYS B 201 ? 0.9077 0.8171 1.0014 0.1173  0.2974  -0.1259 296  LYS B N   
5310 C CA  . LYS B 201 ? 0.8953 0.8145 1.0021 0.1209  0.2877  -0.1149 296  LYS B CA  
5311 C C   . LYS B 201 ? 0.8534 0.7577 0.9559 0.1223  0.2813  -0.1129 296  LYS B C   
5312 O O   . LYS B 201 ? 0.8919 0.7859 1.0055 0.1284  0.2816  -0.1144 296  LYS B O   
5313 C CB  . LYS B 201 ? 0.9053 0.8389 1.0430 0.1301  0.2864  -0.1095 296  LYS B CB  
5314 C CG  . LYS B 201 ? 0.9173 0.8688 1.0670 0.1312  0.2789  -0.0994 296  LYS B CG  
5315 C CD  . LYS B 201 ? 0.8779 0.8254 1.0308 0.1343  0.2685  -0.0913 296  LYS B CD  
5316 N N   . VAL B 202 ? 0.8321 0.7351 0.9192 0.1169  0.2757  -0.1093 297  VAL B N   
5317 C CA  . VAL B 202 ? 0.8059 0.6973 0.8886 0.1167  0.2667  -0.1054 297  VAL B CA  
5318 C C   . VAL B 202 ? 0.7817 0.6858 0.8810 0.1211  0.2547  -0.0926 297  VAL B C   
5319 O O   . VAL B 202 ? 0.7561 0.6737 0.8515 0.1170  0.2484  -0.0864 297  VAL B O   
5320 C CB  . VAL B 202 ? 0.7892 0.6730 0.8427 0.1054  0.2618  -0.1079 297  VAL B CB  
5321 C CG1 . VAL B 202 ? 0.7822 0.6537 0.8321 0.1043  0.2524  -0.1047 297  VAL B CG1 
5322 C CG2 . VAL B 202 ? 0.7950 0.6683 0.8311 0.1006  0.2737  -0.1208 297  VAL B CG2 
5323 N N   . ASN B 203 ? 0.7746 0.6734 0.8917 0.1294  0.2516  -0.0886 298  ASN B N   
5324 C CA  . ASN B 203 ? 0.7790 0.6895 0.9140 0.1351  0.2412  -0.0769 298  ASN B CA  
5325 C C   . ASN B 203 ? 0.7358 0.6482 0.8574 0.1285  0.2278  -0.0688 298  ASN B C   
5326 O O   . ASN B 203 ? 0.7339 0.6340 0.8368 0.1219  0.2252  -0.0711 298  ASN B O   
5327 C CB  . ASN B 203 ? 0.8268 0.7283 0.9810 0.1453  0.2411  -0.0748 298  ASN B CB  
5328 C CG  . ASN B 203 ? 0.9316 0.8478 1.1138 0.1553  0.2426  -0.0708 298  ASN B CG  
5329 O OD1 . ASN B 203 ? 0.9347 0.8692 1.1238 0.1549  0.2370  -0.0645 298  ASN B OD1 
5330 N ND2 . ASN B 203 ? 0.8434 0.7533 1.0405 0.1628  0.2473  -0.0739 298  ASN B ND2 
5331 N N   . GLN B 204 ? 0.7242 0.6524 0.8567 0.1306  0.2194  -0.0595 299  GLN B N   
5332 C CA  . GLN B 204 ? 0.7480 0.6791 0.8701 0.1253  0.2070  -0.0515 299  GLN B CA  
5333 C C   . GLN B 204 ? 0.7194 0.6358 0.8385 0.1264  0.2011  -0.0482 299  GLN B C   
5334 O O   . GLN B 204 ? 0.7324 0.6427 0.8345 0.1191  0.1955  -0.0472 299  GLN B O   
5335 C CB  . GLN B 204 ? 0.7173 0.6669 0.8538 0.1285  0.1996  -0.0426 299  GLN B CB  
5336 C CG  . GLN B 204 ? 0.7166 0.6681 0.8454 0.1248  0.1867  -0.0339 299  GLN B CG  
5337 C CD  . GLN B 204 ? 0.6966 0.6660 0.8387 0.1274  0.1792  -0.0259 299  GLN B CD  
5338 O OE1 . GLN B 204 ? 0.7575 0.7301 0.9155 0.1346  0.1744  -0.0200 299  GLN B OE1 
5339 N NE2 . GLN B 204 ? 0.6153 0.5958 0.7504 0.1215  0.1779  -0.0256 299  GLN B NE2 
5340 N N   . ASP B 205 ? 0.7380 0.6489 0.8744 0.1355  0.2020  -0.0459 300  ASP B N   
5341 C CA  . ASP B 205 ? 0.7585 0.6525 0.8932 0.1372  0.1988  -0.0435 300  ASP B CA  
5342 C C   . ASP B 205 ? 0.7420 0.6194 0.8560 0.1290  0.2025  -0.0514 300  ASP B C   
5343 O O   . ASP B 205 ? 0.7194 0.5899 0.8211 0.1233  0.1957  -0.0482 300  ASP B O   
5344 C CB  . ASP B 205 ? 0.8011 0.6885 0.9563 0.1483  0.2042  -0.0442 300  ASP B CB  
5345 C CG  . ASP B 205 ? 0.8404 0.7300 1.0099 0.1556  0.1949  -0.0327 300  ASP B CG  
5346 O OD1 . ASP B 205 ? 0.9843 0.8682 1.1712 0.1654  0.1981  -0.0319 300  ASP B OD1 
5347 O OD2 . ASP B 205 ? 0.8363 0.7332 0.9997 0.1519  0.1845  -0.0246 300  ASP B OD2 
5348 N N   . ASN B 206 ? 0.7172 0.5887 0.8276 0.1283  0.2136  -0.0622 301  ASN B N   
5349 C CA  . ASN B 206 ? 0.7145 0.5693 0.8065 0.1211  0.2183  -0.0713 301  ASN B CA  
5350 C C   . ASN B 206 ? 0.7371 0.5972 0.8075 0.1100  0.2134  -0.0722 301  ASN B C   
5351 O O   . ASN B 206 ? 0.7330 0.5823 0.7889 0.1031  0.2099  -0.0740 301  ASN B O   
5352 C CB  . ASN B 206 ? 0.8283 0.6773 0.9228 0.1238  0.2320  -0.0828 301  ASN B CB  
5353 C CG  . ASN B 206 ? 0.9074 0.7343 0.9932 0.1217  0.2378  -0.0915 301  ASN B CG  
5354 O OD1 . ASN B 206 ? 0.9517 0.7723 1.0208 0.1149  0.2442  -0.1018 301  ASN B OD1 
5355 N ND2 . ASN B 206 ? 0.9350 0.7492 1.0317 0.1274  0.2356  -0.0876 301  ASN B ND2 
5356 N N   . ARG B 207 ? 0.7309 0.6075 0.7997 0.1081  0.2129  -0.0708 302  ARG B N   
5357 C CA  . ARG B 207 ? 0.7086 0.5915 0.7589 0.0987  0.2069  -0.0697 302  ARG B CA  
5358 C C   . ARG B 207 ? 0.7067 0.5897 0.7546 0.0961  0.1950  -0.0611 302  ARG B C   
5359 O O   . ARG B 207 ? 0.6673 0.5447 0.6994 0.0883  0.1911  -0.0629 302  ARG B O   
5360 C CB  . ARG B 207 ? 0.6768 0.5775 0.7295 0.0985  0.2075  -0.0674 302  ARG B CB  
5361 C CG  . ARG B 207 ? 0.7073 0.6087 0.7589 0.0991  0.2200  -0.0764 302  ARG B CG  
5362 C CD  . ARG B 207 ? 0.6822 0.6010 0.7374 0.0987  0.2211  -0.0734 302  ARG B CD  
5363 N NE  . ARG B 207 ? 0.7441 0.6629 0.7946 0.0977  0.2335  -0.0821 302  ARG B NE  
5364 C CZ  . ARG B 207 ? 0.7064 0.6246 0.7359 0.0897  0.2363  -0.0867 302  ARG B CZ  
5365 N NH1 . ARG B 207 ? 0.6767 0.5943 0.6887 0.0823  0.2274  -0.0836 302  ARG B NH1 
5366 N NH2 . ARG B 207 ? 0.7279 0.6465 0.7540 0.0892  0.2484  -0.0941 302  ARG B NH2 
5367 N N   . LEU B 208 ? 0.6719 0.5620 0.7353 0.1023  0.1892  -0.0518 303  LEU B N   
5368 C CA  . LEU B 208 ? 0.6962 0.5881 0.7559 0.0993  0.1785  -0.0436 303  LEU B CA  
5369 C C   . LEU B 208 ? 0.7266 0.6013 0.7830 0.0982  0.1773  -0.0439 303  LEU B C   
5370 O O   . LEU B 208 ? 0.7104 0.5832 0.7569 0.0920  0.1708  -0.0410 303  LEU B O   
5371 C CB  . LEU B 208 ? 0.6595 0.5646 0.7346 0.1056  0.1722  -0.0337 303  LEU B CB  
5372 C CG  . LEU B 208 ? 0.6715 0.5948 0.7499 0.1054  0.1715  -0.0320 303  LEU B CG  
5373 C CD1 . LEU B 208 ? 0.6566 0.5915 0.7502 0.1112  0.1644  -0.0226 303  LEU B CD1 
5374 C CD2 . LEU B 208 ? 0.5982 0.5265 0.6593 0.0963  0.1679  -0.0330 303  LEU B CD2 
5375 N N   . ASN B 209 ? 0.6973 0.5590 0.7620 0.1037  0.1841  -0.0477 304  ASN B N   
5376 C CA  . ASN B 209 ? 0.7508 0.5938 0.8110 0.1016  0.1843  -0.0493 304  ASN B CA  
5377 C C   . ASN B 209 ? 0.7682 0.6021 0.8100 0.0920  0.1876  -0.0592 304  ASN B C   
5378 O O   . ASN B 209 ? 0.8057 0.6261 0.8412 0.0875  0.1862  -0.0605 304  ASN B O   
5379 C CB  . ASN B 209 ? 0.7250 0.5551 0.7995 0.1105  0.1909  -0.0509 304  ASN B CB  
5380 C CG  . ASN B 209 ? 0.7444 0.5824 0.8377 0.1204  0.1867  -0.0407 304  ASN B CG  
5381 O OD1 . ASN B 209 ? 0.7556 0.6049 0.8495 0.1198  0.1778  -0.0316 304  ASN B OD1 
5382 N ND2 . ASN B 209 ? 0.7638 0.5961 0.8726 0.1297  0.1929  -0.0423 304  ASN B ND2 
5383 N N   . ASN B 210 ? 0.7173 0.5579 0.7504 0.0886  0.1921  -0.0663 305  ASN B N   
5384 C CA  . ASN B 210 ? 0.7156 0.5497 0.7297 0.0791  0.1940  -0.0754 305  ASN B CA  
5385 C C   . ASN B 210 ? 0.7322 0.5816 0.7345 0.0729  0.1889  -0.0740 305  ASN B C   
5386 O O   . ASN B 210 ? 0.7578 0.6083 0.7473 0.0683  0.1930  -0.0814 305  ASN B O   
5387 C CB  . ASN B 210 ? 0.7931 0.6167 0.8046 0.0803  0.2055  -0.0871 305  ASN B CB  
5388 C CG  . ASN B 210 ? 0.7904 0.5961 0.8122 0.0856  0.2106  -0.0894 305  ASN B CG  
5389 O OD1 . ASN B 210 ? 0.7727 0.5633 0.7867 0.0804  0.2105  -0.0937 305  ASN B OD1 
5390 N ND2 . ASN B 210 ? 0.7624 0.5696 0.8027 0.0961  0.2147  -0.0862 305  ASN B ND2 
5391 N N   . ARG B 211 ? 0.6962 0.5573 0.7032 0.0735  0.1801  -0.0640 306  ARG B N   
5392 C CA  . ARG B 211 ? 0.6728 0.5489 0.6716 0.0689  0.1746  -0.0609 306  ARG B CA  
5393 C C   . ARG B 211 ? 0.6781 0.5515 0.6574 0.0595  0.1735  -0.0676 306  ARG B C   
5394 O O   . ARG B 211 ? 0.6826 0.5652 0.6530 0.0564  0.1733  -0.0687 306  ARG B O   
5395 C CB  . ARG B 211 ? 0.6913 0.5761 0.6961 0.0696  0.1650  -0.0504 306  ARG B CB  
5396 C CG  . ARG B 211 ? 0.6579 0.5589 0.6593 0.0677  0.1601  -0.0461 306  ARG B CG  
5397 C CD  . ARG B 211 ? 0.6079 0.5177 0.6157 0.0723  0.1657  -0.0470 306  ARG B CD  
5398 N NE  . ARG B 211 ? 0.6137 0.5387 0.6257 0.0730  0.1598  -0.0397 306  ARG B NE  
5399 C CZ  . ARG B 211 ? 0.6142 0.5496 0.6295 0.0746  0.1627  -0.0393 306  ARG B CZ  
5400 N NH1 . ARG B 211 ? 0.5703 0.5036 0.5843 0.0755  0.1718  -0.0458 306  ARG B NH1 
5401 N NH2 . ARG B 211 ? 0.5314 0.4793 0.5513 0.0750  0.1568  -0.0325 306  ARG B NH2 
5402 N N   . CYS B 212 ? 0.6745 0.5353 0.6470 0.0545  0.1728  -0.0720 307  CYS B N   
5403 C CA  . CYS B 212 ? 0.6666 0.5264 0.6211 0.0452  0.1703  -0.0781 307  CYS B CA  
5404 C C   . CYS B 212 ? 0.7641 0.6195 0.7071 0.0432  0.1784  -0.0882 307  CYS B C   
5405 O O   . CYS B 212 ? 0.7435 0.6022 0.6705 0.0363  0.1760  -0.0920 307  CYS B O   
5406 C CB  . CYS B 212 ? 0.7850 0.6331 0.7362 0.0396  0.1674  -0.0807 307  CYS B CB  
5407 S SG  . CYS B 212 ? 0.8941 0.7426 0.8245 0.0278  0.1629  -0.0882 307  CYS B SG  
5408 N N   . VAL B 213 ? 0.7084 0.5561 0.6588 0.0491  0.1880  -0.0927 308  VAL B N   
5409 C CA  . VAL B 213 ? 0.7530 0.5987 0.6935 0.0482  0.1969  -0.1017 308  VAL B CA  
5410 C C   . VAL B 213 ? 0.7011 0.5617 0.6460 0.0523  0.1988  -0.0969 308  VAL B C   
5411 O O   . VAL B 213 ? 0.7124 0.5775 0.6436 0.0483  0.2014  -0.1006 308  VAL B O   
5412 C CB  . VAL B 213 ? 0.7019 0.5322 0.6490 0.0527  0.2074  -0.1096 308  VAL B CB  
5413 C CG1 . VAL B 213 ? 0.7163 0.5448 0.6536 0.0521  0.2180  -0.1194 308  VAL B CG1 
5414 C CG2 . VAL B 213 ? 0.7714 0.5859 0.7135 0.0477  0.2057  -0.1147 308  VAL B CG2 
5415 N N   . ASP B 214 ? 0.7058 0.5741 0.6696 0.0599  0.1972  -0.0884 309  ASP B N   
5416 C CA  . ASP B 214 ? 0.7138 0.5964 0.6846 0.0638  0.1991  -0.0839 309  ASP B CA  
5417 C C   . ASP B 214 ? 0.6663 0.5602 0.6241 0.0577  0.1924  -0.0801 309  ASP B C   
5418 O O   . ASP B 214 ? 0.6863 0.5879 0.6401 0.0573  0.1965  -0.0805 309  ASP B O   
5419 C CB  . ASP B 214 ? 0.6699 0.5592 0.6628 0.0721  0.1961  -0.0750 309  ASP B CB  
5420 C CG  . ASP B 214 ? 0.6667 0.5713 0.6693 0.0761  0.1980  -0.0706 309  ASP B CG  
5421 O OD1 . ASP B 214 ? 0.6941 0.5997 0.6957 0.0770  0.2074  -0.0764 309  ASP B OD1 
5422 O OD2 . ASP B 214 ? 0.6763 0.5915 0.6879 0.0781  0.1904  -0.0617 309  ASP B OD2 
5423 N N   . LEU B 215 ? 0.7028 0.5973 0.6542 0.0528  0.1826  -0.0763 310  LEU B N   
5424 C CA  . LEU B 215 ? 0.6578 0.5628 0.5990 0.0479  0.1751  -0.0717 310  LEU B CA  
5425 C C   . LEU B 215 ? 0.6930 0.5953 0.6129 0.0409  0.1771  -0.0784 310  LEU B C   
5426 O O   . LEU B 215 ? 0.6298 0.5406 0.5407 0.0373  0.1717  -0.0746 310  LEU B O   
5427 C CB  . LEU B 215 ? 0.6731 0.5795 0.6156 0.0452  0.1646  -0.0661 310  LEU B CB  
5428 C CG  . LEU B 215 ? 0.6801 0.5930 0.6401 0.0510  0.1601  -0.0571 310  LEU B CG  
5429 C CD1 . LEU B 215 ? 0.6259 0.5390 0.5852 0.0475  0.1510  -0.0528 310  LEU B CD1 
5430 C CD2 . LEU B 215 ? 0.6209 0.5477 0.5861 0.0537  0.1590  -0.0512 310  LEU B CD2 
5431 N N   . ARG B 216 ? 0.6966 0.5872 0.6081 0.0390  0.1846  -0.0883 311  ARG B N   
5432 C CA  . ARG B 216 ? 0.7038 0.5910 0.5932 0.0322  0.1870  -0.0954 311  ARG B CA  
5433 C C   . ARG B 216 ? 0.7232 0.6146 0.6082 0.0338  0.1961  -0.0973 311  ARG B C   
5434 O O   . ARG B 216 ? 0.7028 0.5927 0.5679 0.0281  0.1979  -0.1019 311  ARG B O   
5435 C CB  . ARG B 216 ? 0.7270 0.5990 0.6076 0.0286  0.1911  -0.1061 311  ARG B CB  
5436 C CG  . ARG B 216 ? 0.7264 0.5933 0.6098 0.0255  0.1827  -0.1051 311  ARG B CG  
5437 C CD  . ARG B 216 ? 0.7273 0.5778 0.6064 0.0229  0.1878  -0.1156 311  ARG B CD  
5438 N NE  . ARG B 216 ? 0.8012 0.6466 0.6890 0.0217  0.1815  -0.1130 311  ARG B NE  
5439 C CZ  . ARG B 216 ? 0.7880 0.6200 0.6711 0.0170  0.1824  -0.1208 311  ARG B CZ  
5440 N NH1 . ARG B 216 ? 0.7778 0.5997 0.6465 0.0128  0.1889  -0.1323 311  ARG B NH1 
5441 N NH2 . ARG B 216 ? 0.7647 0.5928 0.6572 0.0161  0.1771  -0.1171 311  ARG B NH2 
5442 N N   . THR B 217 ? 0.6776 0.5742 0.5802 0.0411  0.2021  -0.0941 312  THR B N   
5443 C CA  . THR B 217 ? 0.7178 0.6202 0.6170 0.0418  0.2105  -0.0951 312  THR B CA  
5444 C C   . THR B 217 ? 0.7153 0.6280 0.6045 0.0377  0.2034  -0.0879 312  THR B C   
5445 O O   . THR B 217 ? 0.6727 0.5914 0.5664 0.0373  0.1928  -0.0803 312  THR B O   
5446 C CB  . THR B 217 ? 0.6894 0.5981 0.6120 0.0502  0.2172  -0.0923 312  THR B CB  
5447 O OG1 . THR B 217 ? 0.6058 0.5257 0.5427 0.0532  0.2085  -0.0816 312  THR B OG1 
5448 C CG2 . THR B 217 ? 0.6490 0.5476 0.5842 0.0556  0.2232  -0.0979 312  THR B CG2 
5449 N N   . TYR B 218 ? 0.7349 0.6492 0.6102 0.0346  0.2099  -0.0903 313  TYR B N   
5450 C CA  . TYR B 218 ? 0.7080 0.6302 0.5719 0.0305  0.2039  -0.0835 313  TYR B CA  
5451 C C   . TYR B 218 ? 0.6627 0.5968 0.5454 0.0349  0.1996  -0.0735 313  TYR B C   
5452 O O   . TYR B 218 ? 0.6725 0.6123 0.5525 0.0329  0.1897  -0.0663 313  TYR B O   
5453 C CB  . TYR B 218 ? 0.7257 0.6463 0.5718 0.0267  0.2133  -0.0877 313  TYR B CB  
5454 C CG  . TYR B 218 ? 0.7687 0.6775 0.5929 0.0214  0.2170  -0.0980 313  TYR B CG  
5455 C CD1 . TYR B 218 ? 0.8009 0.7057 0.6086 0.0156  0.2068  -0.0988 313  TYR B CD1 
5456 C CD2 . TYR B 218 ? 0.7895 0.6917 0.6096 0.0219  0.2307  -0.1073 313  TYR B CD2 
5457 C CE1 . TYR B 218 ? 0.8518 0.7461 0.6387 0.0100  0.2095  -0.1086 313  TYR B CE1 
5458 C CE2 . TYR B 218 ? 0.7997 0.6905 0.5982 0.0165  0.2343  -0.1175 313  TYR B CE2 
5459 C CZ  . TYR B 218 ? 0.8350 0.7220 0.6167 0.0104  0.2233  -0.1181 313  TYR B CZ  
5460 O OH  . TYR B 218 ? 0.8910 0.7671 0.6510 0.0045  0.2261  -0.1286 313  TYR B OH  
5461 N N   . ALA B 219 ? 0.6207 0.5591 0.5234 0.0411  0.2067  -0.0731 314  ALA B N   
5462 C CA  . ALA B 219 ? 0.6213 0.5714 0.5418 0.0450  0.2027  -0.0643 314  ALA B CA  
5463 C C   . ALA B 219 ? 0.6088 0.5608 0.5404 0.0473  0.1915  -0.0588 314  ALA B C   
5464 O O   . ALA B 219 ? 0.6018 0.5619 0.5379 0.0472  0.1838  -0.0512 314  ALA B O   
5465 C CB  . ALA B 219 ? 0.6116 0.5667 0.5515 0.0509  0.2128  -0.0657 314  ALA B CB  
5466 N N   . ASN B 220 ? 0.5871 0.5310 0.5227 0.0492  0.1906  -0.0627 315  ASN B N   
5467 C CA  . ASN B 220 ? 0.6052 0.5504 0.5509 0.0512  0.1808  -0.0572 315  ASN B CA  
5468 C C   . ASN B 220 ? 0.5944 0.5399 0.5260 0.0453  0.1708  -0.0544 315  ASN B C   
5469 O O   . ASN B 220 ? 0.5862 0.5386 0.5243 0.0459  0.1623  -0.0473 315  ASN B O   
5470 C CB  . ASN B 220 ? 0.6316 0.5669 0.5849 0.0545  0.1832  -0.0617 315  ASN B CB  
5471 C CG  . ASN B 220 ? 0.6156 0.5535 0.5895 0.0623  0.1895  -0.0612 315  ASN B CG  
5472 O OD1 . ASN B 220 ? 0.5956 0.5447 0.5815 0.0655  0.1889  -0.0557 315  ASN B OD1 
5473 N ND2 . ASN B 220 ? 0.5899 0.5176 0.5688 0.0655  0.1955  -0.0671 315  ASN B ND2 
5474 N N   . TYR B 221 ? 0.6424 0.5808 0.5548 0.0396  0.1715  -0.0602 316  TYR B N   
5475 C CA  . TYR B 221 ? 0.6369 0.5771 0.5360 0.0341  0.1619  -0.0575 316  TYR B CA  
5476 C C   . TYR B 221 ? 0.6300 0.5805 0.5291 0.0339  0.1582  -0.0499 316  TYR B C   
5477 O O   . TYR B 221 ? 0.5879 0.5438 0.4894 0.0333  0.1490  -0.0439 316  TYR B O   
5478 C CB  . TYR B 221 ? 0.6394 0.5717 0.5167 0.0278  0.1637  -0.0650 316  TYR B CB  
5479 C CG  . TYR B 221 ? 0.7071 0.6431 0.5721 0.0227  0.1533  -0.0614 316  TYR B CG  
5480 C CD1 . TYR B 221 ? 0.7121 0.6477 0.5798 0.0208  0.1445  -0.0605 316  TYR B CD1 
5481 C CD2 . TYR B 221 ? 0.6774 0.6177 0.5293 0.0200  0.1521  -0.0582 316  TYR B CD2 
5482 C CE1 . TYR B 221 ? 0.7312 0.6717 0.5901 0.0167  0.1347  -0.0571 316  TYR B CE1 
5483 C CE2 . TYR B 221 ? 0.7086 0.6527 0.5508 0.0162  0.1421  -0.0544 316  TYR B CE2 
5484 C CZ  . TYR B 221 ? 0.7493 0.6939 0.5956 0.0147  0.1333  -0.0541 316  TYR B CZ  
5485 O OH  . TYR B 221 ? 0.8099 0.7594 0.6485 0.0114  0.1232  -0.0502 316  TYR B OH  
5486 N N   . SER B 222 ? 0.6361 0.5890 0.5324 0.0343  0.1658  -0.0502 317  SER B N   
5487 C CA  . SER B 222 ? 0.6181 0.5793 0.5137 0.0337  0.1631  -0.0431 317  SER B CA  
5488 C C   . SER B 222 ? 0.5762 0.5458 0.4919 0.0383  0.1586  -0.0363 317  SER B C   
5489 O O   . SER B 222 ? 0.5932 0.5683 0.5088 0.0373  0.1511  -0.0301 317  SER B O   
5490 C CB  . SER B 222 ? 0.5881 0.5494 0.4776 0.0329  0.1735  -0.0451 317  SER B CB  
5491 O OG  . SER B 222 ? 0.6219 0.5754 0.4892 0.0277  0.1763  -0.0509 317  SER B OG  
5492 N N   . ILE B 223 ? 0.5442 0.5147 0.4770 0.0434  0.1627  -0.0374 318  ILE B N   
5493 C CA  . ILE B 223 ? 0.5456 0.5241 0.4969 0.0478  0.1580  -0.0313 318  ILE B CA  
5494 C C   . ILE B 223 ? 0.5731 0.5522 0.5233 0.0465  0.1473  -0.0274 318  ILE B C   
5495 O O   . ILE B 223 ? 0.5553 0.5416 0.5112 0.0470  0.1413  -0.0214 318  ILE B O   
5496 C CB  . ILE B 223 ? 0.5492 0.5270 0.5176 0.0537  0.1630  -0.0334 318  ILE B CB  
5497 C CG1 . ILE B 223 ? 0.5716 0.5528 0.5469 0.0559  0.1733  -0.0358 318  ILE B CG1 
5498 C CG2 . ILE B 223 ? 0.5307 0.5150 0.5152 0.0576  0.1559  -0.0272 318  ILE B CG2 
5499 C CD1 . ILE B 223 ? 0.5403 0.5205 0.5326 0.0623  0.1788  -0.0386 318  ILE B CD1 
5500 N N   . PHE B 224 ? 0.5552 0.5267 0.4985 0.0446  0.1450  -0.0312 319  PHE B N   
5501 C CA  . PHE B 224 ? 0.5644 0.5377 0.5098 0.0437  0.1355  -0.0274 319  PHE B CA  
5502 C C   . PHE B 224 ? 0.5883 0.5641 0.5209 0.0390  0.1288  -0.0252 319  PHE B C   
5503 O O   . PHE B 224 ? 0.5413 0.5220 0.4782 0.0389  0.1213  -0.0206 319  PHE B O   
5504 C CB  . PHE B 224 ? 0.5708 0.5359 0.5182 0.0440  0.1356  -0.0313 319  PHE B CB  
5505 C CG  . PHE B 224 ? 0.5670 0.5317 0.5307 0.0499  0.1390  -0.0302 319  PHE B CG  
5506 C CD1 . PHE B 224 ? 0.5143 0.4853 0.4902 0.0531  0.1337  -0.0238 319  PHE B CD1 
5507 C CD2 . PHE B 224 ? 0.5642 0.5228 0.5311 0.0527  0.1477  -0.0353 319  PHE B CD2 
5508 C CE1 . PHE B 224 ? 0.5440 0.5154 0.5347 0.0589  0.1360  -0.0220 319  PHE B CE1 
5509 C CE2 . PHE B 224 ? 0.5317 0.4906 0.5151 0.0590  0.1503  -0.0337 319  PHE B CE2 
5510 C CZ  . PHE B 224 ? 0.5451 0.5107 0.5401 0.0621  0.1440  -0.0267 319  PHE B CZ  
5511 N N   . CYS B 225 ? 0.5780 0.5509 0.4952 0.0352  0.1313  -0.0282 320  CYS B N   
5512 C CA  A CYS B 225 ? 0.6143 0.5908 0.5211 0.0319  0.1251  -0.0244 320  CYS B CA  
5513 C CA  B CYS B 225 ? 0.5891 0.5655 0.4957 0.0319  0.1251  -0.0244 320  CYS B CA  
5514 C C   . CYS B 225 ? 0.5993 0.5836 0.5147 0.0344  0.1239  -0.0177 320  CYS B C   
5515 O O   . CYS B 225 ? 0.5799 0.5687 0.4957 0.0338  0.1165  -0.0129 320  CYS B O   
5516 C CB  A CYS B 225 ? 0.6394 0.6111 0.5271 0.0277  0.1285  -0.0281 320  CYS B CB  
5517 C CB  B CYS B 225 ? 0.6670 0.6384 0.5544 0.0277  0.1286  -0.0284 320  CYS B CB  
5518 S SG  A CYS B 225 ? 0.5799 0.5429 0.4547 0.0234  0.1277  -0.0363 320  CYS B SG  
5519 S SG  B CYS B 225 ? 0.7193 0.6924 0.5896 0.0229  0.1192  -0.0251 320  CYS B SG  
5520 N N   . LEU B 226 ? 0.5862 0.5723 0.5095 0.0371  0.1312  -0.0175 321  LEU B N   
5521 C CA  . LEU B 226 ? 0.5628 0.5561 0.4952 0.0388  0.1306  -0.0118 321  LEU B CA  
5522 C C   . LEU B 226 ? 0.5423 0.5412 0.4897 0.0420  0.1245  -0.0080 321  LEU B C   
5523 O O   . LEU B 226 ? 0.5144 0.5184 0.4655 0.0421  0.1202  -0.0031 321  LEU B O   
5524 C CB  . LEU B 226 ? 0.5308 0.5255 0.4693 0.0406  0.1403  -0.0133 321  LEU B CB  
5525 C CG  . LEU B 226 ? 0.5653 0.5564 0.4884 0.0369  0.1467  -0.0151 321  LEU B CG  
5526 C CD1 . LEU B 226 ? 0.5342 0.5264 0.4644 0.0386  0.1580  -0.0184 321  LEU B CD1 
5527 C CD2 . LEU B 226 ? 0.5314 0.5250 0.4472 0.0342  0.1428  -0.0091 321  LEU B CD2 
5528 N N   . GLN B 227 ? 0.5026 0.4996 0.4581 0.0445  0.1245  -0.0102 322  GLN B N   
5529 C CA  . GLN B 227 ? 0.5194 0.5208 0.4865 0.0469  0.1185  -0.0066 322  GLN B CA  
5530 C C   . GLN B 227 ? 0.5462 0.5487 0.5070 0.0442  0.1105  -0.0043 322  GLN B C   
5531 O O   . GLN B 227 ? 0.5160 0.5242 0.4830 0.0452  0.1057  0.0000  322  GLN B O   
5532 C CB  . GLN B 227 ? 0.5393 0.5367 0.5139 0.0497  0.1200  -0.0090 322  GLN B CB  
5533 C CG  . GLN B 227 ? 0.5140 0.5163 0.5016 0.0530  0.1155  -0.0047 322  GLN B CG  
5534 C CD  . GLN B 227 ? 0.5091 0.5057 0.4996 0.0542  0.1143  -0.0058 322  GLN B CD  
5535 O OE1 . GLN B 227 ? 0.5508 0.5448 0.5495 0.0579  0.1180  -0.0066 322  GLN B OE1 
5536 N NE2 . GLN B 227 ? 0.5221 0.5168 0.5067 0.0511  0.1094  -0.0056 322  GLN B NE2 
5537 N N   . SER B 228 ? 0.5402 0.5376 0.4891 0.0408  0.1090  -0.0075 323  SER B N   
5538 C CA  . SER B 228 ? 0.5398 0.5395 0.4834 0.0383  0.1014  -0.0054 323  SER B CA  
5539 C C   . SER B 228 ? 0.5567 0.5606 0.4972 0.0379  0.0990  -0.0010 323  SER B C   
5540 O O   . SER B 228 ? 0.5257 0.5344 0.4709 0.0385  0.0933  0.0027  323  SER B O   
5541 C CB  . SER B 228 ? 0.5425 0.5368 0.4735 0.0343  0.1001  -0.0099 323  SER B CB  
5542 O OG  . SER B 228 ? 0.5490 0.5467 0.4768 0.0320  0.0924  -0.0079 323  SER B OG  
5543 N N   . GLN B 229 ? 0.5296 0.5314 0.4624 0.0368  0.1039  -0.0014 324  GLN B N   
5544 C CA  . GLN B 229 ? 0.5576 0.5619 0.4869 0.0362  0.1025  0.0032  324  GLN B CA  
5545 C C   . GLN B 229 ? 0.5381 0.5483 0.4815 0.0391  0.1013  0.0073  324  GLN B C   
5546 O O   . GLN B 229 ? 0.5455 0.5583 0.4894 0.0390  0.0965  0.0112  324  GLN B O   
5547 C CB  . GLN B 229 ? 0.5904 0.5910 0.5104 0.0346  0.1099  0.0020  324  GLN B CB  
5548 C CG  . GLN B 229 ? 0.7243 0.7238 0.6325 0.0322  0.1078  0.0061  324  GLN B CG  
5549 C CD  . GLN B 229 ? 0.8019 0.7994 0.6981 0.0299  0.1004  0.0059  324  GLN B CD  
5550 O OE1 . GLN B 229 ? 0.7976 0.7907 0.6816 0.0273  0.1018  0.0017  324  GLN B OE1 
5551 N NE2 . GLN B 229 ? 0.7355 0.7368 0.6359 0.0309  0.0925  0.0101  324  GLN B NE2 
5552 N N   . ILE B 230 ? 0.5036 0.5159 0.4587 0.0417  0.1053  0.0062  325  ILE B N   
5553 C CA  . ILE B 230 ? 0.5123 0.5306 0.4803 0.0440  0.1035  0.0095  325  ILE B CA  
5554 C C   . ILE B 230 ? 0.5559 0.5769 0.5278 0.0447  0.0961  0.0112  325  ILE B C   
5555 O O   . ILE B 230 ? 0.5449 0.5693 0.5205 0.0450  0.0926  0.0144  325  ILE B O   
5556 C CB  . ILE B 230 ? 0.4931 0.5140 0.4732 0.0469  0.1083  0.0080  325  ILE B CB  
5557 C CG1 . ILE B 230 ? 0.5067 0.5268 0.4857 0.0462  0.1162  0.0066  325  ILE B CG1 
5558 C CG2 . ILE B 230 ? 0.4973 0.5246 0.4901 0.0490  0.1048  0.0110  325  ILE B CG2 
5559 C CD1 . ILE B 230 ? 0.4964 0.5194 0.4882 0.0495  0.1214  0.0045  325  ILE B CD1 
5560 N N   . CYS B 231 ? 0.5097 0.5288 0.4811 0.0448  0.0943  0.0089  326  CYS B N   
5561 C CA  . CYS B 231 ? 0.5302 0.5521 0.5049 0.0450  0.0882  0.0103  326  CYS B CA  
5562 C C   . CYS B 231 ? 0.5334 0.5565 0.5022 0.0433  0.0834  0.0124  326  CYS B C   
5563 O O   . CYS B 231 ? 0.5126 0.5397 0.4867 0.0443  0.0795  0.0148  326  CYS B O   
5564 C CB  . CYS B 231 ? 0.5546 0.5733 0.5280 0.0442  0.0875  0.0075  326  CYS B CB  
5565 S SG  . CYS B 231 ? 0.6288 0.6463 0.6121 0.0473  0.0910  0.0068  326  CYS B SG  
5566 N N   . THR B 232 ? 0.5147 0.5341 0.4721 0.0409  0.0834  0.0113  327  THR B N   
5567 C CA  . THR B 232 ? 0.5188 0.5391 0.4700 0.0397  0.0782  0.0137  327  THR B CA  
5568 C C   . THR B 232 ? 0.5449 0.5667 0.4987 0.0409  0.0780  0.0179  327  THR B C   
5569 O O   . THR B 232 ? 0.4936 0.5182 0.4508 0.0419  0.0732  0.0205  327  THR B O   
5570 C CB  . THR B 232 ? 0.5485 0.5642 0.4855 0.0368  0.0786  0.0119  327  THR B CB  
5571 O OG1 . THR B 232 ? 0.5532 0.5676 0.4884 0.0352  0.0774  0.0077  327  THR B OG1 
5572 C CG2 . THR B 232 ? 0.5582 0.5744 0.4877 0.0360  0.0730  0.0154  327  THR B CG2 
5573 N N   . ILE B 233 ? 0.5260 0.5457 0.4785 0.0408  0.0837  0.0184  328  ILE B N   
5574 C CA  . ILE B 233 ? 0.5015 0.5216 0.4564 0.0411  0.0843  0.0223  328  ILE B CA  
5575 C C   . ILE B 233 ? 0.4764 0.5012 0.4442 0.0433  0.0820  0.0232  328  ILE B C   
5576 O O   . ILE B 233 ? 0.5120 0.5375 0.4820 0.0438  0.0787  0.0260  328  ILE B O   
5577 C CB  . ILE B 233 ? 0.4900 0.5079 0.4429 0.0400  0.0917  0.0221  328  ILE B CB  
5578 C CG1 . ILE B 233 ? 0.5261 0.5385 0.4637 0.0375  0.0944  0.0211  328  ILE B CG1 
5579 C CG2 . ILE B 233 ? 0.4565 0.4748 0.4136 0.0398  0.0927  0.0259  328  ILE B CG2 
5580 C CD1 . ILE B 233 ? 0.5221 0.5329 0.4585 0.0365  0.1033  0.0188  328  ILE B CD1 
5581 N N   . PHE B 234 ? 0.4862 0.5140 0.4625 0.0446  0.0837  0.0209  329  PHE B N   
5582 C CA  . PHE B 234 ? 0.4982 0.5307 0.4854 0.0464  0.0815  0.0214  329  PHE B CA  
5583 C C   . PHE B 234 ? 0.5028 0.5371 0.4906 0.0470  0.0757  0.0221  329  PHE B C   
5584 O O   . PHE B 234 ? 0.4618 0.4976 0.4538 0.0477  0.0734  0.0237  329  PHE B O   
5585 C CB  . PHE B 234 ? 0.4533 0.4879 0.4472 0.0478  0.0837  0.0192  329  PHE B CB  
5586 C CG  . PHE B 234 ? 0.4836 0.5228 0.4863 0.0495  0.0807  0.0196  329  PHE B CG  
5587 C CD1 . PHE B 234 ? 0.4513 0.4911 0.4541 0.0499  0.0777  0.0189  329  PHE B CD1 
5588 C CD2 . PHE B 234 ? 0.4750 0.5179 0.4857 0.0502  0.0813  0.0204  329  PHE B CD2 
5589 C CE1 . PHE B 234 ? 0.4414 0.4849 0.4504 0.0511  0.0754  0.0193  329  PHE B CE1 
5590 C CE2 . PHE B 234 ? 0.4895 0.5365 0.5066 0.0514  0.0783  0.0204  329  PHE B CE2 
5591 C CZ  . PHE B 234 ? 0.4564 0.5035 0.4720 0.0520  0.0755  0.0200  329  PHE B CZ  
5592 N N   . LYS B 235 ? 0.4953 0.5291 0.4795 0.0465  0.0737  0.0205  330  LYS B N   
5593 C CA  . LYS B 235 ? 0.4901 0.5268 0.4765 0.0469  0.0687  0.0207  330  LYS B CA  
5594 C C   . LYS B 235 ? 0.4739 0.5100 0.4572 0.0470  0.0655  0.0233  330  LYS B C   
5595 O O   . LYS B 235 ? 0.4854 0.5241 0.4742 0.0484  0.0626  0.0242  330  LYS B O   
5596 C CB  . LYS B 235 ? 0.4995 0.5361 0.4828 0.0455  0.0674  0.0184  330  LYS B CB  
5597 C CG  . LYS B 235 ? 0.6105 0.6472 0.5982 0.0458  0.0699  0.0166  330  LYS B CG  
5598 C CD  . LYS B 235 ? 0.7013 0.7367 0.6863 0.0439  0.0690  0.0141  330  LYS B CD  
5599 C CE  . LYS B 235 ? 0.6637 0.6934 0.6432 0.0428  0.0730  0.0118  330  LYS B CE  
5600 N NZ  . LYS B 235 ? 0.7391 0.7667 0.7162 0.0404  0.0721  0.0090  330  LYS B NZ  
5601 N N   . ASN B 236 ? 0.4769 0.5090 0.4510 0.0458  0.0659  0.0246  331  ASN B N   
5602 C CA  . ASN B 236 ? 0.4856 0.5164 0.4561 0.0462  0.0620  0.0278  331  ASN B CA  
5603 C C   . ASN B 236 ? 0.5170 0.5462 0.4918 0.0474  0.0632  0.0306  331  ASN B C   
5604 O O   . ASN B 236 ? 0.5027 0.5320 0.4802 0.0490  0.0596  0.0328  331  ASN B O   
5605 C CB  . ASN B 236 ? 0.4940 0.5204 0.4515 0.0443  0.0618  0.0288  331  ASN B CB  
5606 C CG  . ASN B 236 ? 0.5603 0.5886 0.5134 0.0429  0.0582  0.0262  331  ASN B CG  
5607 O OD1 . ASN B 236 ? 0.5881 0.6212 0.5486 0.0436  0.0552  0.0245  331  ASN B OD1 
5608 N ND2 . ASN B 236 ? 0.5429 0.5674 0.4837 0.0405  0.0587  0.0256  331  ASN B ND2 
5609 N N   . PHE B 237 ? 0.4601 0.4878 0.4366 0.0466  0.0684  0.0303  332  PHE B N   
5610 C CA  . PHE B 237 ? 0.4840 0.5108 0.4663 0.0471  0.0695  0.0322  332  PHE B CA  
5611 C C   . PHE B 237 ? 0.4548 0.4856 0.4468 0.0490  0.0667  0.0308  332  PHE B C   
5612 O O   . PHE B 237 ? 0.4734 0.5028 0.4686 0.0502  0.0646  0.0324  332  PHE B O   
5613 C CB  . PHE B 237 ? 0.4600 0.4867 0.4450 0.0456  0.0754  0.0313  332  PHE B CB  
5614 C CG  . PHE B 237 ? 0.4739 0.4994 0.4648 0.0451  0.0769  0.0329  332  PHE B CG  
5615 C CD1 . PHE B 237 ? 0.4960 0.5157 0.4816 0.0435  0.0788  0.0365  332  PHE B CD1 
5616 C CD2 . PHE B 237 ? 0.4458 0.4756 0.4471 0.0458  0.0764  0.0308  332  PHE B CD2 
5617 C CE1 . PHE B 237 ? 0.5234 0.5413 0.5150 0.0424  0.0806  0.0377  332  PHE B CE1 
5618 C CE2 . PHE B 237 ? 0.4686 0.4972 0.4755 0.0447  0.0777  0.0315  332  PHE B CE2 
5619 C CZ  . PHE B 237 ? 0.4625 0.4850 0.4652 0.0429  0.0799  0.0348  332  PHE B CZ  
5620 N N   . LEU B 238 ? 0.4377 0.4731 0.4342 0.0494  0.0667  0.0278  333  LEU B N   
5621 C CA  . LEU B 238 ? 0.4229 0.4622 0.4273 0.0509  0.0647  0.0262  333  LEU B CA  
5622 C C   . LEU B 238 ? 0.4761 0.5164 0.4809 0.0524  0.0605  0.0267  333  LEU B C   
5623 O O   . LEU B 238 ? 0.4588 0.4993 0.4686 0.0538  0.0591  0.0268  333  LEU B O   
5624 C CB  . LEU B 238 ? 0.4072 0.4505 0.4149 0.0508  0.0657  0.0237  333  LEU B CB  
5625 C CG  . LEU B 238 ? 0.4670 0.5104 0.4770 0.0501  0.0693  0.0233  333  LEU B CG  
5626 C CD1 . LEU B 238 ? 0.4064 0.4527 0.4184 0.0506  0.0700  0.0217  333  LEU B CD1 
5627 C CD2 . LEU B 238 ? 0.4626 0.5071 0.4788 0.0500  0.0695  0.0233  333  LEU B CD2 
5628 N N   . LEU B 239 ? 0.4505 0.4916 0.4507 0.0520  0.0585  0.0266  334  LEU B N   
5629 C CA  . LEU B 239 ? 0.4916 0.5352 0.4936 0.0534  0.0541  0.0271  334  LEU B CA  
5630 C C   . LEU B 239 ? 0.4831 0.5230 0.4847 0.0551  0.0519  0.0305  334  LEU B C   
5631 O O   . LEU B 239 ? 0.4647 0.5066 0.4727 0.0575  0.0495  0.0305  334  LEU B O   
5632 C CB  . LEU B 239 ? 0.4535 0.4983 0.4499 0.0520  0.0519  0.0266  334  LEU B CB  
5633 C CG  . LEU B 239 ? 0.5160 0.5641 0.5142 0.0504  0.0535  0.0233  334  LEU B CG  
5634 C CD1 . LEU B 239 ? 0.5416 0.5890 0.5329 0.0482  0.0520  0.0224  334  LEU B CD1 
5635 C CD2 . LEU B 239 ? 0.4509 0.5048 0.4580 0.0515  0.0523  0.0216  334  LEU B CD2 
5636 N N   . GLU B 240 ? 0.4509 0.4850 0.4449 0.0541  0.0531  0.0334  335  GLU B N   
5637 C CA  . GLU B 240 ? 0.4615 0.4905 0.4545 0.0556  0.0513  0.0374  335  GLU B CA  
5638 C C   . GLU B 240 ? 0.5184 0.5459 0.5196 0.0567  0.0533  0.0368  335  GLU B C   
5639 O O   . GLU B 240 ? 0.4651 0.4885 0.4682 0.0586  0.0516  0.0394  335  GLU B O   
5640 C CB  . GLU B 240 ? 0.4671 0.4895 0.4492 0.0536  0.0533  0.0410  335  GLU B CB  
5641 N N   . ASN B 241 ? 0.4350 0.4654 0.4409 0.0555  0.0566  0.0333  336  ASN B N   
5642 C CA  . ASN B 241 ? 0.4663 0.4960 0.4796 0.0560  0.0580  0.0317  336  ASN B CA  
5643 C C   . ASN B 241 ? 0.4692 0.5045 0.4896 0.0577  0.0568  0.0279  336  ASN B C   
5644 O O   . ASN B 241 ? 0.4530 0.4894 0.4783 0.0572  0.0585  0.0251  336  ASN B O   
5645 C CB  . ASN B 241 ? 0.4639 0.4929 0.4775 0.0533  0.0622  0.0307  336  ASN B CB  
5646 C CG  . ASN B 241 ? 0.4978 0.5200 0.5070 0.0516  0.0644  0.0344  336  ASN B CG  
5647 O OD1 . ASN B 241 ? 0.5013 0.5186 0.5131 0.0518  0.0645  0.0358  336  ASN B OD1 
5648 N ND2 . ASN B 241 ? 0.4754 0.4968 0.4774 0.0498  0.0665  0.0359  336  ASN B ND2 
5649 N N   . ASN B 242 ? 0.4825 0.5220 0.5035 0.0591  0.0540  0.0276  337  ASN B N   
5650 C CA  . ASN B 242 ? 0.4919 0.5368 0.5199 0.0608  0.0531  0.0244  337  ASN B CA  
5651 C C   . ASN B 242 ? 0.5022 0.5519 0.5310 0.0590  0.0554  0.0210  337  ASN B C   
5652 O O   . ASN B 242 ? 0.5022 0.5550 0.5359 0.0597  0.0562  0.0180  337  ASN B O   
5653 C CB  . ASN B 242 ? 0.4668 0.5088 0.5011 0.0631  0.0533  0.0235  337  ASN B CB  
5654 C CG  . ASN B 242 ? 0.5560 0.6030 0.5977 0.0660  0.0517  0.0213  337  ASN B CG  
5655 O OD1 . ASN B 242 ? 0.5195 0.5717 0.5619 0.0665  0.0496  0.0216  337  ASN B OD1 
5656 N ND2 . ASN B 242 ? 0.5403 0.5856 0.5880 0.0677  0.0531  0.0188  337  ASN B ND2 
5657 N N   . PHE B 243 ? 0.4528 0.5026 0.4765 0.0569  0.0566  0.0215  338  PHE B N   
5658 C CA  . PHE B 243 ? 0.4400 0.4936 0.4639 0.0556  0.0582  0.0192  338  PHE B CA  
5659 C C   . PHE B 243 ? 0.4895 0.5471 0.5136 0.0554  0.0569  0.0185  338  PHE B C   
5660 O O   . PHE B 243 ? 0.4803 0.5378 0.5027 0.0556  0.0546  0.0198  338  PHE B O   
5661 C CB  . PHE B 243 ? 0.4205 0.4721 0.4402 0.0538  0.0603  0.0201  338  PHE B CB  
5662 C CG  . PHE B 243 ? 0.4064 0.4569 0.4282 0.0534  0.0620  0.0198  338  PHE B CG  
5663 C CD1 . PHE B 243 ? 0.3967 0.4432 0.4190 0.0533  0.0624  0.0211  338  PHE B CD1 
5664 C CD2 . PHE B 243 ? 0.4215 0.4749 0.4451 0.0528  0.0629  0.0182  338  PHE B CD2 
5665 C CE1 . PHE B 243 ? 0.4424 0.4884 0.4678 0.0522  0.0640  0.0204  338  PHE B CE1 
5666 C CE2 . PHE B 243 ? 0.4329 0.4865 0.4593 0.0521  0.0638  0.0176  338  PHE B CE2 
5667 C CZ  . PHE B 243 ? 0.4148 0.4650 0.4426 0.0515  0.0644  0.0184  338  PHE B CZ  
5668 N N   . ILE B 244 ? 0.4171 0.4783 0.4428 0.0545  0.0583  0.0165  339  ILE B N   
5669 C CA  . ILE B 244 ? 0.4509 0.5152 0.4762 0.0532  0.0580  0.0159  339  ILE B CA  
5670 C C   . ILE B 244 ? 0.4410 0.5034 0.4622 0.0514  0.0600  0.0160  339  ILE B C   
5671 O O   . ILE B 244 ? 0.4554 0.5168 0.4761 0.0516  0.0615  0.0161  339  ILE B O   
5672 C CB  . ILE B 244 ? 0.4753 0.5451 0.5061 0.0534  0.0584  0.0137  339  ILE B CB  
5673 C CG1 . ILE B 244 ? 0.4544 0.5249 0.4847 0.0528  0.0611  0.0124  339  ILE B CG1 
5674 C CG2 . ILE B 244 ? 0.4862 0.5579 0.5229 0.0560  0.0567  0.0133  339  ILE B CG2 
5675 C CD1 . ILE B 244 ? 0.4814 0.5571 0.5152 0.0521  0.0628  0.0103  339  ILE B CD1 
5676 N N   . GLU B 245 ? 0.4308 0.4929 0.4496 0.0497  0.0598  0.0160  340  GLU B N   
5677 C CA  . GLU B 245 ? 0.4430 0.5026 0.4588 0.0483  0.0619  0.0161  340  GLU B CA  
5678 C C   . GLU B 245 ? 0.4482 0.5103 0.4658 0.0473  0.0632  0.0154  340  GLU B C   
5679 O O   . GLU B 245 ? 0.4732 0.5394 0.4941 0.0464  0.0627  0.0143  340  GLU B O   
5680 C CB  . GLU B 245 ? 0.4569 0.5138 0.4687 0.0465  0.0614  0.0158  340  GLU B CB  
5681 C CG  . GLU B 245 ? 0.4853 0.5383 0.4944 0.0452  0.0639  0.0155  340  GLU B CG  
5682 C CD  . GLU B 245 ? 0.5723 0.6210 0.5764 0.0437  0.0642  0.0145  340  GLU B CD  
5683 O OE1 . GLU B 245 ? 0.5706 0.6201 0.5724 0.0429  0.0618  0.0139  340  GLU B OE1 
5684 O OE2 . GLU B 245 ? 0.6483 0.6923 0.6502 0.0433  0.0667  0.0142  340  GLU B OE2 
5685 N N   . ILE B 246 ? 0.4201 0.4802 0.4360 0.0474  0.0649  0.0164  341  ILE B N   
5686 C CA  . ILE B 246 ? 0.4316 0.4929 0.4473 0.0462  0.0664  0.0166  341  ILE B CA  
5687 C C   . ILE B 246 ? 0.4707 0.5270 0.4833 0.0452  0.0678  0.0180  341  ILE B C   
5688 O O   . ILE B 246 ? 0.4644 0.5168 0.4755 0.0462  0.0679  0.0186  341  ILE B O   
5689 C CB  . ILE B 246 ? 0.4820 0.5452 0.4975 0.0474  0.0666  0.0168  341  ILE B CB  
5690 C CG1 . ILE B 246 ? 0.4490 0.5097 0.4633 0.0490  0.0660  0.0183  341  ILE B CG1 
5691 C CG2 . ILE B 246 ? 0.4213 0.4885 0.4404 0.0483  0.0659  0.0147  341  ILE B CG2 
5692 C CD1 . ILE B 246 ? 0.4509 0.5135 0.4641 0.0496  0.0654  0.0186  341  ILE B CD1 
5693 N N   . HIS B 247 ? 0.4416 0.4975 0.4532 0.0432  0.0693  0.0186  342  HIS B N   
5694 C CA  . HIS B 247 ? 0.4725 0.5225 0.4813 0.0423  0.0709  0.0204  342  HIS B CA  
5695 C C   . HIS B 247 ? 0.4692 0.5192 0.4756 0.0420  0.0720  0.0227  342  HIS B C   
5696 O O   . HIS B 247 ? 0.4700 0.5232 0.4766 0.0398  0.0734  0.0221  342  HIS B O   
5697 C CB  . HIS B 247 ? 0.4586 0.5064 0.4676 0.0391  0.0719  0.0190  342  HIS B CB  
5698 C CG  . HIS B 247 ? 0.4802 0.5275 0.4896 0.0390  0.0705  0.0168  342  HIS B CG  
5699 N ND1 . HIS B 247 ? 0.5083 0.5497 0.5150 0.0401  0.0711  0.0167  342  HIS B ND1 
5700 C CD2 . HIS B 247 ? 0.4810 0.5328 0.4924 0.0382  0.0684  0.0147  342  HIS B CD2 
5701 C CE1 . HIS B 247 ? 0.4869 0.5289 0.4927 0.0395  0.0697  0.0146  342  HIS B CE1 
5702 N NE2 . HIS B 247 ? 0.5000 0.5483 0.5085 0.0384  0.0676  0.0137  342  HIS B NE2 
5703 N N   . THR B 248 ? 0.4702 0.5170 0.4744 0.0442  0.0715  0.0254  343  THR B N   
5704 C CA  . THR B 248 ? 0.4570 0.5037 0.4573 0.0444  0.0716  0.0282  343  THR B CA  
5705 C C   . THR B 248 ? 0.4975 0.5367 0.4952 0.0447  0.0725  0.0319  343  THR B C   
5706 O O   . THR B 248 ? 0.5020 0.5366 0.5018 0.0458  0.0728  0.0317  343  THR B O   
5707 C CB  . THR B 248 ? 0.4686 0.5191 0.4691 0.0470  0.0690  0.0283  343  THR B CB  
5708 O OG1 . THR B 248 ? 0.4733 0.5218 0.4766 0.0498  0.0676  0.0292  343  THR B OG1 
5709 C CG2 . THR B 248 ? 0.4609 0.5172 0.4643 0.0468  0.0685  0.0246  343  THR B CG2 
5710 N N   . PRO B 249 ? 0.4840 0.5212 0.4767 0.0438  0.0732  0.0353  344  PRO B N   
5711 C CA  . PRO B 249 ? 0.5384 0.5669 0.5284 0.0435  0.0745  0.0392  344  PRO B CA  
5712 C C   . PRO B 249 ? 0.5314 0.5562 0.5227 0.0480  0.0722  0.0422  344  PRO B C   
5713 O O   . PRO B 249 ? 0.4846 0.5141 0.4765 0.0508  0.0691  0.0429  344  PRO B O   
5714 C CB  . PRO B 249 ? 0.5204 0.5486 0.5037 0.0411  0.0759  0.0424  344  PRO B CB  
5715 C CG  . PRO B 249 ? 0.5319 0.5681 0.5135 0.0420  0.0738  0.0408  344  PRO B CG  
5716 C CD  . PRO B 249 ? 0.5099 0.5518 0.4983 0.0423  0.0734  0.0354  344  PRO B CD  
5717 N N   . LYS B 250 ? 0.5365 0.5527 0.5286 0.0485  0.0739  0.0438  345  LYS B N   
5718 C CA  . LYS B 250 ? 0.5376 0.5493 0.5321 0.0532  0.0723  0.0471  345  LYS B CA  
5719 C C   . LYS B 250 ? 0.5629 0.5677 0.5523 0.0540  0.0719  0.0535  345  LYS B C   
5720 O O   . LYS B 250 ? 0.5674 0.5698 0.5589 0.0586  0.0695  0.0572  345  LYS B O   
5721 C CB  . LYS B 250 ? 0.4759 0.4816 0.4752 0.0541  0.0747  0.0444  345  LYS B CB  
5722 C CG  . LYS B 250 ? 0.5283 0.5393 0.5305 0.0525  0.0754  0.0384  345  LYS B CG  
5723 C CD  . LYS B 250 ? 0.4817 0.5022 0.4865 0.0546  0.0726  0.0372  345  LYS B CD  
5724 C CE  . LYS B 250 ? 0.5042 0.5295 0.5099 0.0521  0.0732  0.0323  345  LYS B CE  
5725 N NZ  . LYS B 250 ? 0.4688 0.5025 0.4761 0.0530  0.0708  0.0312  345  LYS B NZ  
5726 N N   . LEU B 251 ? 0.5168 0.5187 0.4999 0.0496  0.0742  0.0552  346  LEU B N   
5727 C CA  . LEU B 251 ? 0.5827 0.5782 0.5587 0.0497  0.0739  0.0620  346  LEU B CA  
5728 C C   . LEU B 251 ? 0.5951 0.5985 0.5648 0.0495  0.0710  0.0636  346  LEU B C   
5729 O O   . LEU B 251 ? 0.5943 0.6039 0.5616 0.0457  0.0727  0.0602  346  LEU B O   
5730 C CB  . LEU B 251 ? 0.5834 0.5710 0.5555 0.0444  0.0787  0.0630  346  LEU B CB  
5731 C CG  . LEU B 251 ? 0.6058 0.5847 0.5830 0.0432  0.0820  0.0606  346  LEU B CG  
5732 C CD1 . LEU B 251 ? 0.6249 0.5971 0.5985 0.0369  0.0866  0.0616  346  LEU B CD1 
5733 C CD2 . LEU B 251 ? 0.6118 0.5819 0.5919 0.0486  0.0807  0.0641  346  LEU B CD2 
5734 N N   . LEU B 252 ? 0.5409 0.5442 0.5082 0.0537  0.0665  0.0685  347  LEU B N   
5735 C CA  . LEU B 252 ? 0.6469 0.6578 0.6079 0.0538  0.0628  0.0696  347  LEU B CA  
5736 C C   . LEU B 252 ? 0.6922 0.6970 0.6421 0.0536  0.0616  0.0773  347  LEU B C   
5737 O O   . LEU B 252 ? 0.6505 0.6456 0.6000 0.0558  0.0615  0.0830  347  LEU B O   
5738 C CB  . LEU B 252 ? 0.6362 0.6543 0.6039 0.0587  0.0573  0.0685  347  LEU B CB  
5739 C CG  . LEU B 252 ? 0.6265 0.6496 0.6049 0.0594  0.0584  0.0619  347  LEU B CG  
5740 C CD1 . LEU B 252 ? 0.6747 0.7051 0.6598 0.0635  0.0534  0.0612  347  LEU B CD1 
5741 C CD2 . LEU B 252 ? 0.5953 0.6236 0.5722 0.0549  0.0614  0.0561  347  LEU B CD2 
5742 N N   . GLY B 253 ? 0.7193 0.7291 0.6594 0.0509  0.0608  0.0775  348  GLY B N   
5743 C CA  . GLY B 253 ? 0.7308 0.7361 0.6584 0.0509  0.0585  0.0851  348  GLY B CA  
5744 C C   . GLY B 253 ? 0.8248 0.8333 0.7525 0.0563  0.0505  0.0890  348  GLY B C   
5745 O O   . GLY B 253 ? 0.8939 0.8965 0.8138 0.0582  0.0473  0.0969  348  GLY B O   
5746 N N   . GLU B 254 ? 0.8812 0.8991 0.8184 0.0588  0.0470  0.0837  349  GLU B N   
5747 C CA  . GLU B 254 ? 0.9086 0.9323 0.8481 0.0634  0.0391  0.0861  349  GLU B CA  
5748 C C   . GLU B 254 ? 0.9318 0.9607 0.8876 0.0669  0.0381  0.0813  349  GLU B C   
5749 O O   . GLU B 254 ? 0.9383 0.9689 0.9005 0.0649  0.0427  0.0750  349  GLU B O   
5750 C CB  . GLU B 254 ? 0.9616 0.9940 0.8917 0.0607  0.0357  0.0837  349  GLU B CB  
5751 C CG  . GLU B 254 ? 0.9843 1.0167 0.9045 0.0628  0.0285  0.0908  349  GLU B CG  
5752 C CD  . GLU B 254 ? 1.0270 1.0485 0.9332 0.0613  0.0307  0.0988  349  GLU B CD  
5753 O OE1 . GLU B 254 ? 1.0261 1.0400 0.9343 0.0655  0.0283  0.1063  349  GLU B OE1 
5754 O OE2 . GLU B 254 ? 1.0549 1.0751 0.9485 0.0559  0.0352  0.0976  349  GLU B OE2 
5755 N N   . SER B 255 ? 0.9564 0.9885 0.9189 0.0721  0.0319  0.0846  350  SER B N   
5756 C CA  . SER B 255 ? 0.9828 1.0200 0.9613 0.0756  0.0316  0.0805  350  SER B CA  
5757 C C   . SER B 255 ? 1.0531 1.1012 1.0351 0.0730  0.0308  0.0731  350  SER B C   
5758 O O   . SER B 255 ? 1.0534 1.1087 1.0306 0.0720  0.0257  0.0727  350  SER B O   
5759 C CB  . SER B 255 ? 0.9920 1.0308 0.9782 0.0820  0.0253  0.0859  350  SER B CB  
5760 O OG  . SER B 255 ? 1.0176 1.0625 1.0197 0.0848  0.0257  0.0814  350  SER B OG  
5761 N N   . SER B 256 ? 1.1345 1.1833 1.1246 0.0718  0.0358  0.0671  351  SER B N   
5762 C CA  . SER B 256 ? 1.0549 1.1126 1.0490 0.0695  0.0356  0.0604  351  SER B CA  
5763 C C   . SER B 256 ? 1.0785 1.1450 1.0830 0.0726  0.0303  0.0599  351  SER B C   
5764 O O   . SER B 256 ? 1.0339 1.1083 1.0388 0.0704  0.0276  0.0560  351  SER B O   
5765 C CB  . SER B 256 ? 0.9562 1.0116 0.9554 0.0676  0.0420  0.0552  351  SER B CB  
5766 O OG  . SER B 256 ? 0.9045 0.9568 0.9135 0.0710  0.0440  0.0557  351  SER B OG  
5767 N N   . GLU B 257 ? 1.0179 1.0834 1.0316 0.0776  0.0287  0.0635  352  GLU B N   
5768 C CA  . GLU B 257 ? 0.9932 1.0679 1.0199 0.0809  0.0243  0.0629  352  GLU B CA  
5769 C C   . GLU B 257 ? 1.0343 1.1099 1.0632 0.0860  0.0178  0.0699  352  GLU B C   
5770 O O   . GLU B 257 ? 1.0434 1.1229 1.0861 0.0907  0.0162  0.0710  352  GLU B O   
5771 C CB  . GLU B 257 ? 0.9458 1.0203 0.9855 0.0827  0.0296  0.0594  352  GLU B CB  
5772 C CG  . GLU B 257 ? 0.9041 0.9790 0.9432 0.0782  0.0349  0.0529  352  GLU B CG  
5773 C CD  . GLU B 257 ? 0.8890 0.9671 0.9413 0.0797  0.0385  0.0494  352  GLU B CD  
5774 O OE1 . GLU B 257 ? 0.8963 0.9753 0.9586 0.0843  0.0381  0.0516  352  GLU B OE1 
5775 O OE2 . GLU B 257 ? 0.8782 0.9577 0.9309 0.0764  0.0419  0.0446  352  GLU B OE2 
5776 N N   . GLY B 258 ? 1.1008 1.1732 1.1164 0.0852  0.0139  0.0749  353  GLY B N   
5777 C CA  . GLY B 258 ? 1.1111 1.1837 1.1277 0.0904  0.0070  0.0825  353  GLY B CA  
5778 C C   . GLY B 258 ? 1.1898 1.2509 1.2092 0.0949  0.0104  0.0878  353  GLY B C   
5779 O O   . GLY B 258 ? 1.1665 1.2255 1.1979 0.0972  0.0154  0.0850  353  GLY B O   
5780 N N   . GLY B 259 ? 1.1425 1.1954 1.1504 0.0960  0.0079  0.0954  354  GLY B N   
5781 C CA  . GLY B 259 ? 1.0854 1.1240 1.0913 0.0982  0.0126  0.1002  354  GLY B CA  
5782 C C   . GLY B 259 ? 1.0364 1.0723 1.0582 0.1056  0.0124  0.1029  354  GLY B C   
5783 O O   . GLY B 259 ? 0.9853 1.0086 1.0074 0.1070  0.0178  0.1048  354  GLY B O   
5784 N N   . ALA B 260 ? 1.1195 1.1670 1.1551 0.1102  0.0066  0.1026  355  ALA B N   
5785 C CA  . ALA B 260 ? 1.1508 1.1963 1.2019 0.1183  0.0057  0.1062  355  ALA B CA  
5786 C C   . ALA B 260 ? 1.1368 1.1778 1.1994 0.1191  0.0149  0.1000  355  ALA B C   
5787 O O   . ALA B 260 ? 1.1207 1.1540 1.1921 0.1250  0.0172  0.1028  355  ALA B O   
5788 C CB  . ALA B 260 ? 1.1618 1.2228 1.2261 0.1228  -0.0031 0.1073  355  ALA B CB  
5789 N N   . ASN B 261 ? 0.9645 1.0098 1.0267 0.1135  0.0203  0.0917  356  ASN B N   
5790 C CA  . ASN B 261 ? 0.8680 0.9095 0.9388 0.1135  0.0289  0.0855  356  ASN B CA  
5791 C C   . ASN B 261 ? 0.8152 0.8454 0.8734 0.1076  0.0359  0.0826  356  ASN B C   
5792 O O   . ASN B 261 ? 0.7306 0.7595 0.7922 0.1054  0.0425  0.0762  356  ASN B O   
5793 C CB  . ASN B 261 ? 0.8892 0.9442 0.9710 0.1121  0.0298  0.0785  356  ASN B CB  
5794 C CG  . ASN B 261 ? 0.9407 1.0077 1.0387 0.1180  0.0238  0.0805  356  ASN B CG  
5795 O OD1 . ASN B 261 ? 0.9581 1.0220 1.0658 0.1249  0.0227  0.0848  356  ASN B OD1 
5796 N ND2 . ASN B 261 ? 0.8874 0.9683 0.9894 0.1153  0.0199  0.0773  356  ASN B ND2 
5797 N N   . ALA B 262 ? 0.8118 0.8346 0.8553 0.1047  0.0346  0.0872  357  ALA B N   
5798 C CA  . ALA B 262 ? 0.7779 0.7915 0.8102 0.0987  0.0408  0.0845  357  ALA B CA  
5799 C C   . ALA B 262 ? 0.7058 0.7037 0.7349 0.1005  0.0439  0.0894  357  ALA B C   
5800 O O   . ALA B 262 ? 0.7375 0.7308 0.7655 0.1048  0.0396  0.0971  357  ALA B O   
5801 C CB  . ALA B 262 ? 0.7761 0.7933 0.7943 0.0928  0.0385  0.0850  357  ALA B CB  
5802 N N   . PHE B 263 ? 0.6293 0.6188 0.6571 0.0971  0.0511  0.0849  358  PHE B N   
5803 C CA  . PHE B 263 ? 0.6729 0.6464 0.6958 0.0968  0.0548  0.0886  358  PHE B CA  
5804 C C   . PHE B 263 ? 0.7159 0.6851 0.7236 0.0917  0.0538  0.0933  358  PHE B C   
5805 O O   . PHE B 263 ? 0.6752 0.6513 0.6758 0.0859  0.0543  0.0899  358  PHE B O   
5806 C CB  . PHE B 263 ? 0.6327 0.5992 0.6578 0.0937  0.0625  0.0816  358  PHE B CB  
5807 C CG  . PHE B 263 ? 0.6592 0.6272 0.6978 0.0986  0.0650  0.0769  358  PHE B CG  
5808 C CD1 . PHE B 263 ? 0.6616 0.6203 0.7082 0.1050  0.0661  0.0800  358  PHE B CD1 
5809 C CD2 . PHE B 263 ? 0.6199 0.5979 0.6629 0.0967  0.0669  0.0695  358  PHE B CD2 
5810 C CE1 . PHE B 263 ? 0.6244 0.5847 0.6838 0.1094  0.0695  0.0750  358  PHE B CE1 
5811 C CE2 . PHE B 263 ? 0.6169 0.5963 0.6715 0.1007  0.0703  0.0650  358  PHE B CE2 
5812 C CZ  . PHE B 263 ? 0.6142 0.5850 0.6771 0.1071  0.0718  0.0675  358  PHE B CZ  
5813 N N   . GLN B 264 ? 0.7011 0.6584 0.7040 0.0937  0.0531  0.1012  359  GLN B N   
5814 C CA  . GLN B 264 ? 0.7340 0.6856 0.7218 0.0889  0.0529  0.1067  359  GLN B CA  
5815 C C   . GLN B 264 ? 0.7374 0.6755 0.7210 0.0836  0.0604  0.1053  359  GLN B C   
5816 O O   . GLN B 264 ? 0.7631 0.6912 0.7540 0.0859  0.0641  0.1040  359  GLN B O   
5817 C CB  . GLN B 264 ? 0.7333 0.6798 0.7166 0.0939  0.0469  0.1175  359  GLN B CB  
5818 C CG  . GLN B 264 ? 0.7917 0.7516 0.7812 0.0996  0.0386  0.1191  359  GLN B CG  
5819 C CD  . GLN B 264 ? 0.9232 0.8776 0.9108 0.1060  0.0319  0.1300  359  GLN B CD  
5820 O OE1 . GLN B 264 ? 0.9462 0.9072 0.9250 0.1061  0.0251  0.1350  359  GLN B OE1 
5821 N NE2 . GLN B 264 ? 0.9248 0.8668 0.9203 0.1116  0.0337  0.1339  359  GLN B NE2 
5822 N N   . ILE B 265 ? 0.7472 0.6853 0.7195 0.0764  0.0629  0.1051  360  ILE B N   
5823 C CA  . ILE B 265 ? 0.7883 0.7145 0.7563 0.0704  0.0696  0.1044  360  ILE B CA  
5824 C C   . ILE B 265 ? 0.8033 0.7249 0.7570 0.0660  0.0699  0.1115  360  ILE B C   
5825 O O   . ILE B 265 ? 0.7806 0.7112 0.7267 0.0655  0.0660  0.1138  360  ILE B O   
5826 C CB  . ILE B 265 ? 0.8418 0.7739 0.8129 0.0643  0.0744  0.0944  360  ILE B CB  
5827 C CG1 . ILE B 265 ? 0.8226 0.7662 0.7860 0.0591  0.0739  0.0925  360  ILE B CG1 
5828 C CG2 . ILE B 265 ? 0.8043 0.7438 0.7868 0.0681  0.0737  0.0873  360  ILE B CG2 
5829 C CD1 . ILE B 265 ? 0.8097 0.7529 0.7716 0.0513  0.0798  0.0872  360  ILE B CD1 
5830 N N   . ASN B 266 ? 0.8925 0.7996 0.8423 0.0622  0.0751  0.1145  361  ASN B N   
5831 C CA  . ASN B 266 ? 0.8970 0.7994 0.8334 0.0559  0.0778  0.1198  361  ASN B CA  
5832 C C   . ASN B 266 ? 0.8730 0.7822 0.8094 0.0476  0.0834  0.1116  361  ASN B C   
5833 O O   . ASN B 266 ? 0.8786 0.7829 0.8218 0.0444  0.0881  0.1061  361  ASN B O   
5834 C CB  . ASN B 266 ? 0.8918 0.7746 0.8241 0.0556  0.0808  0.1278  361  ASN B CB  
5835 C CG  . ASN B 266 ? 1.0373 0.9147 0.9564 0.0474  0.0856  0.1323  361  ASN B CG  
5836 O OD1 . ASN B 266 ? 1.0817 0.9481 1.0009 0.0416  0.0921  0.1316  361  ASN B OD1 
5837 N ND2 . ASN B 266 ? 0.9952 0.8804 0.9026 0.0465  0.0826  0.1363  361  ASN B ND2 
5838 N N   . TYR B 267 ? 0.8389 0.7596 0.7681 0.0442  0.0828  0.1104  362  TYR B N   
5839 C CA  . TYR B 267 ? 0.8436 0.7720 0.7733 0.0368  0.0878  0.1033  362  TYR B CA  
5840 C C   . TYR B 267 ? 0.8512 0.7749 0.7685 0.0304  0.0923  0.1086  362  TYR B C   
5841 O O   . TYR B 267 ? 0.8421 0.7732 0.7500 0.0293  0.0911  0.1104  362  TYR B O   
5842 C CB  . TYR B 267 ? 0.7139 0.6595 0.6465 0.0381  0.0845  0.0967  362  TYR B CB  
5843 C CG  . TYR B 267 ? 0.7144 0.6689 0.6510 0.0321  0.0890  0.0885  362  TYR B CG  
5844 C CD1 . TYR B 267 ? 0.6578 0.6147 0.6055 0.0318  0.0900  0.0811  362  TYR B CD1 
5845 C CD2 . TYR B 267 ? 0.6975 0.6581 0.6267 0.0268  0.0920  0.0881  362  TYR B CD2 
5846 C CE1 . TYR B 267 ? 0.6208 0.5862 0.5728 0.0268  0.0931  0.0741  362  TYR B CE1 
5847 C CE2 . TYR B 267 ? 0.6674 0.6370 0.6022 0.0220  0.0959  0.0805  362  TYR B CE2 
5848 C CZ  . TYR B 267 ? 0.6271 0.5992 0.5736 0.0222  0.0959  0.0738  362  TYR B CZ  
5849 O OH  . TYR B 267 ? 0.5843 0.5655 0.5371 0.0180  0.0986  0.0668  362  TYR B OH  
5850 N N   . PHE B 268 ? 0.8372 0.7483 0.7544 0.0256  0.0980  0.1107  363  PHE B N   
5851 C CA  . PHE B 268 ? 0.9017 0.8069 0.8082 0.0185  0.1037  0.1157  363  PHE B CA  
5852 C C   . PHE B 268 ? 0.9746 0.8790 0.8658 0.0205  0.1005  0.1246  363  PHE B C   
5853 O O   . PHE B 268 ? 1.0238 0.9375 0.9067 0.0169  0.1021  0.1237  363  PHE B O   
5854 C CB  . PHE B 268 ? 0.8232 0.7400 0.7327 0.0109  0.1091  0.1079  363  PHE B CB  
5855 C CG  . PHE B 268 ? 0.8050 0.7245 0.7287 0.0085  0.1113  0.0989  363  PHE B CG  
5856 C CD1 . PHE B 268 ? 0.7110 0.6431 0.6438 0.0120  0.1075  0.0908  363  PHE B CD1 
5857 C CD2 . PHE B 268 ? 0.7430 0.6523 0.6701 0.0023  0.1170  0.0985  363  PHE B CD2 
5858 C CE1 . PHE B 268 ? 0.7265 0.6610 0.6706 0.0096  0.1090  0.0829  363  PHE B CE1 
5859 C CE2 . PHE B 268 ? 0.7718 0.6840 0.7110 -0.0003 0.1184  0.0899  363  PHE B CE2 
5860 C CZ  . PHE B 268 ? 0.7287 0.6536 0.6759 0.0035  0.1141  0.0823  363  PHE B CZ  
5861 N N   . ASN B 269 ? 0.9582 0.8518 0.8458 0.0267  0.0958  0.1331  364  ASN B N   
5862 C CA  . ASN B 269 ? 1.0449 0.9359 0.9173 0.0293  0.0915  0.1429  364  ASN B CA  
5863 C C   . ASN B 269 ? 1.0113 0.9183 0.8813 0.0334  0.0846  0.1400  364  ASN B C   
5864 O O   . ASN B 269 ? 1.0449 0.9527 0.9008 0.0343  0.0809  0.1466  364  ASN B O   
5865 C CB  . ASN B 269 ? 1.0933 0.9782 0.9504 0.0213  0.0980  0.1485  364  ASN B CB  
5866 C CG  . ASN B 269 ? 1.1691 1.0335 1.0227 0.0192  0.1022  0.1571  364  ASN B CG  
5867 O OD1 . ASN B 269 ? 1.1572 1.0118 1.0215 0.0230  0.1012  0.1573  364  ASN B OD1 
5868 N ND2 . ASN B 269 ? 1.2299 1.0873 1.0685 0.0128  0.1074  0.1641  364  ASN B ND2 
5869 N N   . GLN B 270 ? 0.9638 0.8833 0.8466 0.0356  0.0826  0.1303  365  GLN B N   
5870 C CA  . GLN B 270 ? 0.9094 0.8428 0.7927 0.0402  0.0756  0.1273  365  GLN B CA  
5871 C C   . GLN B 270 ? 0.8891 0.8227 0.7853 0.0483  0.0695  0.1268  365  GLN B C   
5872 O O   . GLN B 270 ? 0.8973 0.8234 0.8042 0.0497  0.0720  0.1250  365  GLN B O   
5873 C CB  . GLN B 270 ? 0.8473 0.7955 0.7350 0.0363  0.0783  0.1167  365  GLN B CB  
5874 C CG  . GLN B 270 ? 0.9087 0.8591 0.7856 0.0285  0.0848  0.1159  365  GLN B CG  
5875 C CD  . GLN B 270 ? 0.8826 0.8484 0.7638 0.0263  0.0862  0.1060  365  GLN B CD  
5876 O OE1 . GLN B 270 ? 0.8861 0.8553 0.7721 0.0210  0.0927  0.1004  365  GLN B OE1 
5877 N NE2 . GLN B 270 ? 0.8327 0.8078 0.7128 0.0304  0.0798  0.1038  365  GLN B NE2 
5878 N N   . LYS B 271 ? 0.8769 0.8193 0.7721 0.0535  0.0618  0.1279  366  LYS B N   
5879 C CA  . LYS B 271 ? 0.8556 0.8017 0.7645 0.0611  0.0560  0.1263  366  LYS B CA  
5880 C C   . LYS B 271 ? 0.8136 0.7732 0.7332 0.0602  0.0568  0.1152  366  LYS B C   
5881 O O   . LYS B 271 ? 0.8137 0.7846 0.7287 0.0580  0.0551  0.1114  366  LYS B O   
5882 C CB  . LYS B 271 ? 0.8233 0.7733 0.7271 0.0668  0.0467  0.1330  366  LYS B CB  
5883 N N   . GLY B 272 ? 0.7854 0.7430 0.7184 0.0616  0.0596  0.1100  367  GLY B N   
5884 C CA  . GLY B 272 ? 0.7336 0.7024 0.6764 0.0610  0.0605  0.1003  367  GLY B CA  
5885 C C   . GLY B 272 ? 0.7345 0.7060 0.6908 0.0677  0.0570  0.0983  367  GLY B C   
5886 O O   . GLY B 272 ? 0.7404 0.7048 0.7004 0.0731  0.0545  0.1039  367  GLY B O   
5887 N N   . PHE B 273 ? 0.6767 0.6584 0.6408 0.0671  0.0575  0.0902  368  PHE B N   
5888 C CA  . PHE B 273 ? 0.6515 0.6380 0.6284 0.0725  0.0551  0.0872  368  PHE B CA  
5889 C C   . PHE B 273 ? 0.6512 0.6412 0.6347 0.0696  0.0596  0.0785  368  PHE B C   
5890 O O   . PHE B 273 ? 0.6096 0.6031 0.5885 0.0642  0.0623  0.0745  368  PHE B O   
5891 C CB  . PHE B 273 ? 0.6860 0.6845 0.6646 0.0757  0.0482  0.0876  368  PHE B CB  
5892 C CG  . PHE B 273 ? 0.7577 0.7547 0.7278 0.0779  0.0425  0.0961  368  PHE B CG  
5893 C CD1 . PHE B 273 ? 0.7561 0.7508 0.7324 0.0847  0.0376  0.1019  368  PHE B CD1 
5894 C CD2 . PHE B 273 ? 0.7733 0.7715 0.7291 0.0734  0.0418  0.0981  368  PHE B CD2 
5895 C CE1 . PHE B 273 ? 0.7426 0.7359 0.7104 0.0871  0.0313  0.1104  368  PHE B CE1 
5896 C CE2 . PHE B 273 ? 0.7810 0.7773 0.7268 0.0752  0.0363  0.1062  368  PHE B CE2 
5897 C CZ  . PHE B 273 ? 0.7439 0.7378 0.6954 0.0820  0.0306  0.1126  368  PHE B CZ  
5898 N N   . LEU B 274 ? 0.5792 0.5685 0.5734 0.0733  0.0605  0.0757  369  LEU B N   
5899 C CA  . LEU B 274 ? 0.5611 0.5545 0.5610 0.0713  0.0639  0.0678  369  LEU B CA  
5900 C C   . LEU B 274 ? 0.5654 0.5720 0.5699 0.0725  0.0605  0.0644  369  LEU B C   
5901 O O   . LEU B 274 ? 0.5382 0.5497 0.5472 0.0769  0.0560  0.0671  369  LEU B O   
5902 C CB  . LEU B 274 ? 0.5788 0.5646 0.5868 0.0743  0.0672  0.0658  369  LEU B CB  
5903 C CG  . LEU B 274 ? 0.6160 0.5876 0.6205 0.0723  0.0715  0.0676  369  LEU B CG  
5904 C CD1 . LEU B 274 ? 0.5754 0.5397 0.5877 0.0752  0.0752  0.0642  369  LEU B CD1 
5905 C CD2 . LEU B 274 ? 0.6341 0.6054 0.6317 0.0649  0.0747  0.0643  369  LEU B CD2 
5906 N N   . ALA B 275 ? 0.5091 0.5212 0.5128 0.0685  0.0625  0.0586  370  ALA B N   
5907 C CA  . ALA B 275 ? 0.5426 0.5658 0.5499 0.0688  0.0598  0.0552  370  ALA B CA  
5908 C C   . ALA B 275 ? 0.5458 0.5720 0.5640 0.0730  0.0597  0.0534  370  ALA B C   
5909 O O   . ALA B 275 ? 0.5245 0.5455 0.5467 0.0737  0.0636  0.0510  370  ALA B O   
5910 C CB  . ALA B 275 ? 0.4958 0.5226 0.5006 0.0640  0.0624  0.0498  370  ALA B CB  
5911 N N   . GLN B 276 ? 0.5640 0.5987 0.5868 0.0754  0.0553  0.0542  371  GLN B N   
5912 C CA  . GLN B 276 ? 0.6042 0.6443 0.6382 0.0785  0.0555  0.0517  371  GLN B CA  
5913 C C   . GLN B 276 ? 0.5898 0.6364 0.6251 0.0752  0.0569  0.0462  371  GLN B C   
5914 O O   . GLN B 276 ? 0.5662 0.6163 0.6098 0.0766  0.0587  0.0434  371  GLN B O   
5915 C CB  . GLN B 276 ? 0.6054 0.6521 0.6456 0.0827  0.0497  0.0555  371  GLN B CB  
5916 C CG  . GLN B 276 ? 0.6771 0.7169 0.7167 0.0868  0.0477  0.0619  371  GLN B CG  
5917 C CD  . GLN B 276 ? 0.8050 0.8523 0.8487 0.0906  0.0403  0.0664  371  GLN B CD  
5918 O OE1 . GLN B 276 ? 0.8317 0.8780 0.8664 0.0901  0.0360  0.0710  371  GLN B OE1 
5919 N NE2 . GLN B 276 ? 0.8170 0.8724 0.8742 0.0941  0.0389  0.0649  371  GLN B NE2 
5920 N N   . SER B 277 ? 0.5235 0.5712 0.5510 0.0710  0.0568  0.0445  372  SER B N   
5921 C CA  . SER B 277 ? 0.5461 0.5995 0.5742 0.0682  0.0573  0.0401  372  SER B CA  
5922 C C   . SER B 277 ? 0.5484 0.6008 0.5676 0.0643  0.0576  0.0391  372  SER B C   
5923 O O   . SER B 277 ? 0.5253 0.5763 0.5383 0.0638  0.0558  0.0421  372  SER B O   
5924 C CB  . SER B 277 ? 0.5478 0.6102 0.5815 0.0692  0.0532  0.0398  372  SER B CB  
5925 O OG  . SER B 277 ? 0.5622 0.6286 0.5948 0.0660  0.0534  0.0359  372  SER B OG  
5926 N N   . PRO B 278 ? 0.5029 0.5563 0.5213 0.0616  0.0598  0.0352  373  PRO B N   
5927 C CA  . PRO B 278 ? 0.4989 0.5529 0.5108 0.0584  0.0601  0.0339  373  PRO B CA  
5928 C C   . PRO B 278 ? 0.5098 0.5703 0.5214 0.0576  0.0573  0.0322  373  PRO B C   
5929 O O   . PRO B 278 ? 0.5120 0.5739 0.5201 0.0552  0.0581  0.0299  373  PRO B O   
5930 C CB  . PRO B 278 ? 0.4645 0.5167 0.4772 0.0566  0.0632  0.0307  373  PRO B CB  
5931 C CG  . PRO B 278 ? 0.4808 0.5345 0.4996 0.0582  0.0635  0.0293  373  PRO B CG  
5932 C CD  . PRO B 278 ? 0.4698 0.5226 0.4925 0.0614  0.0627  0.0321  373  PRO B CD  
5933 N N   . GLN B 279 ? 0.4654 0.5300 0.4812 0.0595  0.0541  0.0331  374  GLN B N   
5934 C CA  . GLN B 279 ? 0.5225 0.5934 0.5391 0.0584  0.0511  0.0308  374  GLN B CA  
5935 C C   . GLN B 279 ? 0.4776 0.5492 0.4858 0.0558  0.0506  0.0295  374  GLN B C   
5936 O O   . GLN B 279 ? 0.4982 0.5715 0.5061 0.0539  0.0515  0.0256  374  GLN B O   
5937 C CB  . GLN B 279 ? 0.4812 0.5565 0.5021 0.0607  0.0467  0.0332  374  GLN B CB  
5938 C CG  . GLN B 279 ? 0.4665 0.5485 0.4882 0.0591  0.0429  0.0306  374  GLN B CG  
5939 C CD  . GLN B 279 ? 0.5217 0.6060 0.5506 0.0577  0.0447  0.0266  374  GLN B CD  
5940 O OE1 . GLN B 279 ? 0.5229 0.6067 0.5590 0.0591  0.0469  0.0268  374  GLN B OE1 
5941 N NE2 . GLN B 279 ? 0.4872 0.5731 0.5136 0.0549  0.0443  0.0228  374  GLN B NE2 
5942 N N   . LEU B 280 ? 0.4501 0.5197 0.4511 0.0559  0.0495  0.0329  375  LEU B N   
5943 C CA  . LEU B 280 ? 0.5318 0.6024 0.5238 0.0534  0.0494  0.0318  375  LEU B CA  
5944 C C   . LEU B 280 ? 0.4693 0.5382 0.4601 0.0512  0.0541  0.0286  375  LEU B C   
5945 O O   . LEU B 280 ? 0.5003 0.5718 0.4888 0.0493  0.0549  0.0247  375  LEU B O   
5946 C CB  . LEU B 280 ? 0.5302 0.5979 0.5137 0.0537  0.0480  0.0370  375  LEU B CB  
5947 C CG  . LEU B 280 ? 0.5632 0.6327 0.5482 0.0567  0.0424  0.0412  375  LEU B CG  
5948 C CD1 . LEU B 280 ? 0.5787 0.6447 0.5532 0.0568  0.0406  0.0469  375  LEU B CD1 
5949 C CD2 . LEU B 280 ? 0.5100 0.5872 0.4984 0.0564  0.0379  0.0380  375  LEU B CD2 
5950 N N   . TYR B 281 ? 0.4690 0.5338 0.4623 0.0514  0.0572  0.0296  376  TYR B N   
5951 C CA  . TYR B 281 ? 0.4656 0.5296 0.4584 0.0493  0.0611  0.0271  376  TYR B CA  
5952 C C   . TYR B 281 ? 0.4674 0.5339 0.4663 0.0494  0.0615  0.0229  376  TYR B C   
5953 O O   . TYR B 281 ? 0.4690 0.5373 0.4679 0.0481  0.0634  0.0198  376  TYR B O   
5954 C CB  . TYR B 281 ? 0.4754 0.5345 0.4688 0.0490  0.0636  0.0294  376  TYR B CB  
5955 C CG  . TYR B 281 ? 0.5431 0.5983 0.5296 0.0483  0.0640  0.0338  376  TYR B CG  
5956 C CD1 . TYR B 281 ? 0.5203 0.5760 0.5002 0.0455  0.0664  0.0338  376  TYR B CD1 
5957 C CD2 . TYR B 281 ? 0.5481 0.5991 0.5347 0.0506  0.0623  0.0381  376  TYR B CD2 
5958 C CE1 . TYR B 281 ? 0.5939 0.6453 0.5663 0.0445  0.0670  0.0385  376  TYR B CE1 
5959 C CE2 . TYR B 281 ? 0.5864 0.6328 0.5663 0.0502  0.0624  0.0430  376  TYR B CE2 
5960 C CZ  . TYR B 281 ? 0.6356 0.6819 0.6077 0.0470  0.0647  0.0434  376  TYR B CZ  
5961 O OH  . TYR B 281 ? 0.6618 0.7026 0.6260 0.0463  0.0651  0.0489  376  TYR B OH  
5962 N N   . LYS B 282 ? 0.4348 0.5014 0.4395 0.0511  0.0602  0.0228  377  LYS B N   
5963 C CA  . LYS B 282 ? 0.4695 0.5373 0.4788 0.0510  0.0606  0.0196  377  LYS B CA  
5964 C C   . LYS B 282 ? 0.4514 0.5224 0.4603 0.0503  0.0593  0.0165  377  LYS B C   
5965 O O   . LYS B 282 ? 0.4419 0.5133 0.4527 0.0498  0.0605  0.0135  377  LYS B O   
5966 C CB  . LYS B 282 ? 0.4396 0.5063 0.4543 0.0524  0.0603  0.0203  377  LYS B CB  
5967 C CG  . LYS B 282 ? 0.4563 0.5251 0.4740 0.0536  0.0580  0.0215  377  LYS B CG  
5968 C CD  . LYS B 282 ? 0.4833 0.5508 0.5065 0.0548  0.0592  0.0222  377  LYS B CD  
5969 C CE  . LYS B 282 ? 0.4807 0.5518 0.5093 0.0562  0.0572  0.0231  377  LYS B CE  
5970 N NZ  . LYS B 282 ? 0.4641 0.5355 0.4988 0.0564  0.0591  0.0223  377  LYS B NZ  
5971 N N   . GLN B 283 ? 0.4420 0.5152 0.4482 0.0502  0.0566  0.0172  378  GLN B N   
5972 C CA  . GLN B 283 ? 0.4337 0.5096 0.4380 0.0488  0.0555  0.0135  378  GLN B CA  
5973 C C   . GLN B 283 ? 0.4773 0.5531 0.4756 0.0474  0.0581  0.0115  378  GLN B C   
5974 O O   . GLN B 283 ? 0.4841 0.5606 0.4829 0.0466  0.0593  0.0071  378  GLN B O   
5975 C CB  . GLN B 283 ? 0.4255 0.5044 0.4276 0.0486  0.0513  0.0144  378  GLN B CB  
5976 C CG  . GLN B 283 ? 0.4061 0.4871 0.4163 0.0497  0.0488  0.0151  378  GLN B CG  
5977 C CD  . GLN B 283 ? 0.4701 0.5557 0.4790 0.0491  0.0439  0.0152  378  GLN B CD  
5978 O OE1 . GLN B 283 ? 0.4462 0.5332 0.4544 0.0508  0.0411  0.0193  378  GLN B OE1 
5979 N NE2 . GLN B 283 ? 0.4521 0.5399 0.4603 0.0468  0.0425  0.0106  378  GLN B NE2 
5980 N N   . MET B 284 ? 0.4630 0.5376 0.4559 0.0470  0.0595  0.0144  379  MET B N   
5981 C CA  . MET B 284 ? 0.4921 0.5672 0.4803 0.0453  0.0631  0.0123  379  MET B CA  
5982 C C   . MET B 284 ? 0.4860 0.5614 0.4810 0.0457  0.0661  0.0093  379  MET B C   
5983 O O   . MET B 284 ? 0.5132 0.5903 0.5079 0.0450  0.0686  0.0053  379  MET B O   
5984 C CB  . MET B 284 ? 0.4610 0.5342 0.4427 0.0442  0.0647  0.0164  379  MET B CB  
5985 C CG  . MET B 284 ? 0.5546 0.6276 0.5270 0.0437  0.0619  0.0192  379  MET B CG  
5986 S SD  . MET B 284 ? 0.6920 0.7602 0.6582 0.0433  0.0628  0.0263  379  MET B SD  
5987 C CE  . MET B 284 ? 0.5713 0.6397 0.5328 0.0400  0.0692  0.0244  379  MET B CE  
5988 N N   . CYS B 285 ? 0.4465 0.5203 0.4476 0.0469  0.0657  0.0110  380  CYS B N   
5989 C CA  . CYS B 285 ? 0.4596 0.5340 0.4671 0.0476  0.0674  0.0087  380  CYS B CA  
5990 C C   . CYS B 285 ? 0.4721 0.5468 0.4834 0.0485  0.0666  0.0052  380  CYS B C   
5991 O O   . CYS B 285 ? 0.4558 0.5316 0.4708 0.0491  0.0684  0.0022  380  CYS B O   
5992 C CB  . CYS B 285 ? 0.4627 0.5349 0.4740 0.0484  0.0667  0.0113  380  CYS B CB  
5993 S SG  . CYS B 285 ? 0.4852 0.5560 0.4933 0.0467  0.0685  0.0145  380  CYS B SG  
5994 N N   . ILE B 286 ? 0.4796 0.5533 0.4910 0.0487  0.0640  0.0053  381  ILE B N   
5995 C CA  . ILE B 286 ? 0.4418 0.5148 0.4565 0.0490  0.0635  0.0017  381  ILE B CA  
5996 C C   . ILE B 286 ? 0.4468 0.5213 0.4577 0.0479  0.0650  -0.0027 381  ILE B C   
5997 O O   . ILE B 286 ? 0.4258 0.4995 0.4401 0.0485  0.0668  -0.0065 381  ILE B O   
5998 C CB  . ILE B 286 ? 0.4730 0.5454 0.4895 0.0487  0.0607  0.0026  381  ILE B CB  
5999 C CG1 . ILE B 286 ? 0.4079 0.4786 0.4282 0.0497  0.0604  0.0062  381  ILE B CG1 
6000 C CG2 . ILE B 286 ? 0.4310 0.5021 0.4504 0.0480  0.0604  -0.0016 381  ILE B CG2 
6001 C CD1 . ILE B 286 ? 0.4219 0.4898 0.4463 0.0509  0.0616  0.0061  381  ILE B CD1 
6002 N N   . ASN B 287 ? 0.4384 0.5147 0.4417 0.0463  0.0645  -0.0022 382  ASN B N   
6003 C CA  . ASN B 287 ? 0.4782 0.5558 0.4757 0.0448  0.0665  -0.0065 382  ASN B CA  
6004 C C   . ASN B 287 ? 0.4940 0.5727 0.4930 0.0453  0.0713  -0.0082 382  ASN B C   
6005 O O   . ASN B 287 ? 0.4826 0.5621 0.4797 0.0447  0.0743  -0.0132 382  ASN B O   
6006 C CB  . ASN B 287 ? 0.4544 0.5334 0.4417 0.0430  0.0646  -0.0044 382  ASN B CB  
6007 C CG  . ASN B 287 ? 0.4536 0.5333 0.4400 0.0424  0.0596  -0.0044 382  ASN B CG  
6008 O OD1 . ASN B 287 ? 0.4492 0.5282 0.4412 0.0423  0.0585  -0.0077 382  ASN B OD1 
6009 N ND2 . ASN B 287 ? 0.4431 0.5242 0.4233 0.0419  0.0564  -0.0006 382  ASN B ND2 
6010 N N   . SER B 288 ? 0.4616 0.5408 0.4649 0.0462  0.0723  -0.0049 383  SER B N   
6011 C CA  . SER B 288 ? 0.5042 0.5858 0.5117 0.0466  0.0764  -0.0068 383  SER B CA  
6012 C C   . SER B 288 ? 0.5104 0.5917 0.5280 0.0492  0.0765  -0.0090 383  SER B C   
6013 O O   . SER B 288 ? 0.5335 0.6178 0.5569 0.0501  0.0793  -0.0106 383  SER B O   
6014 C CB  . SER B 288 ? 0.4837 0.5664 0.4913 0.0457  0.0774  -0.0026 383  SER B CB  
6015 O OG  . SER B 288 ? 0.5207 0.6027 0.5189 0.0435  0.0776  0.0002  383  SER B OG  
6016 N N   . GLY B 289 ? 0.4948 0.5728 0.5153 0.0504  0.0734  -0.0087 384  GLY B N   
6017 C CA  . GLY B 289 ? 0.4780 0.5543 0.5070 0.0531  0.0733  -0.0102 384  GLY B CA  
6018 C C   . GLY B 289 ? 0.5034 0.5787 0.5372 0.0546  0.0709  -0.0060 384  GLY B C   
6019 O O   . GLY B 289 ? 0.4509 0.5250 0.4914 0.0570  0.0704  -0.0064 384  GLY B O   
6020 N N   . PHE B 290 ? 0.4456 0.5209 0.4759 0.0533  0.0693  -0.0019 385  PHE B N   
6021 C CA  . PHE B 290 ? 0.4456 0.5196 0.4789 0.0543  0.0673  0.0015  385  PHE B CA  
6022 C C   . PHE B 290 ? 0.4265 0.4959 0.4611 0.0553  0.0651  0.0028  385  PHE B C   
6023 O O   . PHE B 290 ? 0.4649 0.5326 0.5015 0.0564  0.0636  0.0053  385  PHE B O   
6024 C CB  . PHE B 290 ? 0.4264 0.5007 0.4554 0.0527  0.0668  0.0048  385  PHE B CB  
6025 C CG  . PHE B 290 ? 0.5137 0.5918 0.5423 0.0512  0.0690  0.0046  385  PHE B CG  
6026 C CD1 . PHE B 290 ? 0.5558 0.6378 0.5878 0.0515  0.0715  0.0014  385  PHE B CD1 
6027 C CD2 . PHE B 290 ? 0.5733 0.6506 0.5983 0.0495  0.0690  0.0073  385  PHE B CD2 
6028 C CE1 . PHE B 290 ? 0.5488 0.6346 0.5808 0.0495  0.0743  0.0012  385  PHE B CE1 
6029 C CE2 . PHE B 290 ? 0.5842 0.6643 0.6088 0.0475  0.0715  0.0072  385  PHE B CE2 
6030 C CZ  . PHE B 290 ? 0.5102 0.5949 0.5384 0.0473  0.0742  0.0042  385  PHE B CZ  
6031 N N   . ASP B 291 ? 0.4344 0.5017 0.4673 0.0545  0.0650  0.0012  386  ASP B N   
6032 C CA  . ASP B 291 ? 0.4654 0.5282 0.5007 0.0549  0.0639  0.0013  386  ASP B CA  
6033 C C   . ASP B 291 ? 0.4332 0.4939 0.4671 0.0542  0.0626  0.0052  386  ASP B C   
6034 O O   . ASP B 291 ? 0.4393 0.4984 0.4734 0.0529  0.0622  0.0050  386  ASP B O   
6035 C CB  . ASP B 291 ? 0.4230 0.4831 0.4638 0.0575  0.0640  0.0008  386  ASP B CB  
6036 C CG  . ASP B 291 ? 0.4793 0.5334 0.5223 0.0575  0.0637  0.0004  386  ASP B CG  
6037 O OD1 . ASP B 291 ? 0.4792 0.5322 0.5223 0.0563  0.0646  -0.0034 386  ASP B OD1 
6038 O OD2 . ASP B 291 ? 0.5055 0.5557 0.5495 0.0583  0.0626  0.0039  386  ASP B OD2 
6039 N N   . ARG B 292 ? 0.4088 0.4698 0.4418 0.0547  0.0622  0.0082  387  ARG B N   
6040 C CA  . ARG B 292 ? 0.4154 0.4743 0.4464 0.0541  0.0618  0.0113  387  ARG B CA  
6041 C C   . ARG B 292 ? 0.4097 0.4703 0.4378 0.0538  0.0618  0.0130  387  ARG B C   
6042 O O   . ARG B 292 ? 0.4250 0.4862 0.4535 0.0545  0.0612  0.0134  387  ARG B O   
6043 C CB  . ARG B 292 ? 0.4504 0.5047 0.4826 0.0550  0.0612  0.0133  387  ARG B CB  
6044 C CG  . ARG B 292 ? 0.4645 0.5150 0.4994 0.0545  0.0617  0.0123  387  ARG B CG  
6045 C CD  . ARG B 292 ? 0.4630 0.5078 0.4982 0.0554  0.0613  0.0151  387  ARG B CD  
6046 N NE  . ARG B 292 ? 0.4863 0.5266 0.5244 0.0544  0.0622  0.0142  387  ARG B NE  
6047 C CZ  . ARG B 292 ? 0.5426 0.5767 0.5801 0.0539  0.0628  0.0172  387  ARG B CZ  
6048 N NH1 . ARG B 292 ? 0.5306 0.5624 0.5639 0.0546  0.0623  0.0213  387  ARG B NH1 
6049 N NH2 . ARG B 292 ? 0.5300 0.5600 0.5707 0.0523  0.0640  0.0159  387  ARG B NH2 
6050 N N   . VAL B 293 ? 0.3795 0.4409 0.4053 0.0529  0.0623  0.0138  388  VAL B N   
6051 C CA  . VAL B 293 ? 0.4203 0.4821 0.4434 0.0524  0.0627  0.0151  388  VAL B CA  
6052 C C   . VAL B 293 ? 0.4310 0.4907 0.4527 0.0522  0.0634  0.0169  388  VAL B C   
6053 O O   . VAL B 293 ? 0.4146 0.4744 0.4380 0.0523  0.0636  0.0171  388  VAL B O   
6054 C CB  . VAL B 293 ? 0.4479 0.5125 0.4696 0.0518  0.0632  0.0143  388  VAL B CB  
6055 C CG1 . VAL B 293 ? 0.3478 0.4150 0.3714 0.0519  0.0636  0.0120  388  VAL B CG1 
6056 C CG2 . VAL B 293 ? 0.3910 0.4563 0.4116 0.0516  0.0628  0.0147  388  VAL B CG2 
6057 N N   . PHE B 294 ? 0.4303 0.4883 0.4494 0.0519  0.0640  0.0177  389  PHE B N   
6058 C CA  . PHE B 294 ? 0.4137 0.4695 0.4315 0.0519  0.0654  0.0188  389  PHE B CA  
6059 C C   . PHE B 294 ? 0.4496 0.5040 0.4650 0.0512  0.0661  0.0189  389  PHE B C   
6060 O O   . PHE B 294 ? 0.4324 0.4877 0.4469 0.0502  0.0654  0.0182  389  PHE B O   
6061 C CB  . PHE B 294 ? 0.3737 0.4265 0.3897 0.0517  0.0665  0.0193  389  PHE B CB  
6062 C CG  . PHE B 294 ? 0.4282 0.4792 0.4402 0.0509  0.0657  0.0191  389  PHE B CG  
6063 C CD1 . PHE B 294 ? 0.4338 0.4824 0.4422 0.0499  0.0667  0.0186  389  PHE B CD1 
6064 C CD2 . PHE B 294 ? 0.4546 0.5060 0.4666 0.0511  0.0637  0.0195  389  PHE B CD2 
6065 C CE1 . PHE B 294 ? 0.4787 0.5262 0.4832 0.0487  0.0653  0.0181  389  PHE B CE1 
6066 C CE2 . PHE B 294 ? 0.4701 0.5208 0.4788 0.0504  0.0619  0.0196  389  PHE B CE2 
6067 C CZ  . PHE B 294 ? 0.4516 0.5008 0.4562 0.0489  0.0626  0.0187  389  PHE B CZ  
6068 N N   . GLU B 295 ? 0.4714 0.5237 0.4866 0.0519  0.0675  0.0198  390  GLU B N   
6069 C CA  . GLU B 295 ? 0.4475 0.4966 0.4605 0.0513  0.0686  0.0200  390  GLU B CA  
6070 C C   . GLU B 295 ? 0.4667 0.5119 0.4792 0.0520  0.0709  0.0199  390  GLU B C   
6071 O O   . GLU B 295 ? 0.4777 0.5239 0.4932 0.0536  0.0718  0.0204  390  GLU B O   
6072 C CB  . GLU B 295 ? 0.4161 0.4658 0.4294 0.0517  0.0682  0.0216  390  GLU B CB  
6073 C CG  . GLU B 295 ? 0.4719 0.5171 0.4828 0.0505  0.0696  0.0222  390  GLU B CG  
6074 C CD  . GLU B 295 ? 0.4966 0.5420 0.5063 0.0503  0.0693  0.0243  390  GLU B CD  
6075 O OE1 . GLU B 295 ? 0.5047 0.5456 0.5124 0.0492  0.0707  0.0254  390  GLU B OE1 
6076 O OE2 . GLU B 295 ? 0.5040 0.5536 0.5140 0.0510  0.0677  0.0249  390  GLU B OE2 
6077 N N   . VAL B 296 ? 0.4537 0.4947 0.4628 0.0507  0.0722  0.0187  391  VAL B N   
6078 C CA  . VAL B 296 ? 0.4916 0.5277 0.4996 0.0513  0.0752  0.0178  391  VAL B CA  
6079 C C   . VAL B 296 ? 0.4820 0.5135 0.4894 0.0510  0.0762  0.0180  391  VAL B C   
6080 O O   . VAL B 296 ? 0.4603 0.4897 0.4644 0.0483  0.0758  0.0166  391  VAL B O   
6081 C CB  . VAL B 296 ? 0.5357 0.5695 0.5384 0.0495  0.0762  0.0157  391  VAL B CB  
6082 C CG1 . VAL B 296 ? 0.4797 0.5080 0.4806 0.0500  0.0801  0.0139  391  VAL B CG1 
6083 C CG2 . VAL B 296 ? 0.4271 0.4642 0.4298 0.0498  0.0754  0.0164  391  VAL B CG2 
6084 N N   . ALA B 297 ? 0.4214 0.4512 0.4323 0.0536  0.0772  0.0198  392  ALA B N   
6085 C CA  . ALA B 297 ? 0.4246 0.4494 0.4347 0.0532  0.0777  0.0210  392  ALA B CA  
6086 C C   . ALA B 297 ? 0.4799 0.5015 0.4942 0.0569  0.0792  0.0229  392  ALA B C   
6087 O O   . ALA B 297 ? 0.4832 0.5089 0.5022 0.0597  0.0789  0.0236  392  ALA B O   
6088 C CB  . ALA B 297 ? 0.4624 0.4907 0.4718 0.0519  0.0752  0.0232  392  ALA B CB  
6089 N N   . PRO B 298 ? 0.4872 0.5013 0.5007 0.0571  0.0808  0.0237  393  PRO B N   
6090 C CA  . PRO B 298 ? 0.5148 0.5255 0.5332 0.0615  0.0817  0.0262  393  PRO B CA  
6091 C C   . PRO B 298 ? 0.5190 0.5349 0.5403 0.0639  0.0780  0.0308  393  PRO B C   
6092 O O   . PRO B 298 ? 0.4926 0.5117 0.5102 0.0618  0.0754  0.0324  393  PRO B O   
6093 C CB  . PRO B 298 ? 0.5329 0.5331 0.5487 0.0603  0.0839  0.0265  393  PRO B CB  
6094 C CG  . PRO B 298 ? 0.5133 0.5123 0.5233 0.0549  0.0844  0.0232  393  PRO B CG  
6095 C CD  . PRO B 298 ? 0.5049 0.5133 0.5137 0.0532  0.0818  0.0223  393  PRO B CD  
6096 N N   . VAL B 299 ? 0.4412 0.4583 0.4693 0.0685  0.0778  0.0326  394  VAL B N   
6097 C CA  . VAL B 299 ? 0.4881 0.5084 0.5193 0.0717  0.0739  0.0374  394  VAL B CA  
6098 C C   . VAL B 299 ? 0.5281 0.5418 0.5647 0.0764  0.0753  0.0398  394  VAL B C   
6099 O O   . VAL B 299 ? 0.4748 0.4839 0.5148 0.0777  0.0796  0.0367  394  VAL B O   
6100 C CB  . VAL B 299 ? 0.5162 0.5474 0.5526 0.0729  0.0709  0.0373  394  VAL B CB  
6101 C CG1 . VAL B 299 ? 0.4416 0.4779 0.4730 0.0687  0.0698  0.0349  394  VAL B CG1 
6102 C CG2 . VAL B 299 ? 0.4969 0.5304 0.5416 0.0755  0.0738  0.0347  394  VAL B CG2 
6103 N N   . PHE B 300 ? 0.5031 0.5162 0.5401 0.0791  0.0715  0.0454  395  PHE B N   
6104 C CA  . PHE B 300 ? 0.5228 0.5284 0.5643 0.0839  0.0719  0.0491  395  PHE B CA  
6105 C C   . PHE B 300 ? 0.5795 0.5924 0.6275 0.0888  0.0665  0.0538  395  PHE B C   
6106 O O   . PHE B 300 ? 0.5747 0.5934 0.6180 0.0873  0.0616  0.0567  395  PHE B O   
6107 C CB  . PHE B 300 ? 0.4961 0.4906 0.5294 0.0818  0.0726  0.0525  395  PHE B CB  
6108 C CG  . PHE B 300 ? 0.5111 0.5009 0.5373 0.0757  0.0765  0.0480  395  PHE B CG  
6109 C CD1 . PHE B 300 ? 0.5364 0.5168 0.5632 0.0750  0.0814  0.0444  395  PHE B CD1 
6110 C CD2 . PHE B 300 ? 0.4770 0.4722 0.4964 0.0707  0.0751  0.0471  395  PHE B CD2 
6111 C CE1 . PHE B 300 ? 0.5444 0.5214 0.5650 0.0691  0.0841  0.0401  395  PHE B CE1 
6112 C CE2 . PHE B 300 ? 0.4880 0.4803 0.5026 0.0654  0.0780  0.0431  395  PHE B CE2 
6113 C CZ  . PHE B 300 ? 0.5187 0.5022 0.5338 0.0644  0.0822  0.0397  395  PHE B CZ  
6114 N N   . ARG B 301 ? 0.5091 0.5225 0.5684 0.0945  0.0671  0.0544  396  ARG B N   
6115 C CA  . ARG B 301 ? 0.6220 0.6433 0.6891 0.0995  0.0612  0.0590  396  ARG B CA  
6116 C C   . ARG B 301 ? 0.6359 0.6502 0.7117 0.1064  0.0617  0.0627  396  ARG B C   
6117 O O   . ARG B 301 ? 0.5783 0.5861 0.6593 0.1082  0.0678  0.0592  396  ARG B O   
6118 C CB  . ARG B 301 ? 0.6425 0.6775 0.7188 0.0997  0.0602  0.0554  396  ARG B CB  
6119 C CG  . ARG B 301 ? 0.6777 0.7137 0.7644 0.1017  0.0662  0.0504  396  ARG B CG  
6120 C CD  . ARG B 301 ? 0.7656 0.8149 0.8594 0.1002  0.0656  0.0469  396  ARG B CD  
6121 N NE  . ARG B 301 ? 0.7802 0.8405 0.8823 0.1031  0.0585  0.0505  396  ARG B NE  
6122 N N   . ALA B 302 ? 0.6715 0.6870 0.7483 0.1103  0.0553  0.0698  397  ALA B N   
6123 C CA  . ALA B 302 ? 0.6849 0.6910 0.7669 0.1168  0.0547  0.0753  397  ALA B CA  
6124 C C   . ALA B 302 ? 0.7057 0.7215 0.8043 0.1244  0.0505  0.0777  397  ALA B C   
6125 O O   . ALA B 302 ? 0.7611 0.7726 0.8634 0.1304  0.0463  0.0847  397  ALA B O   
6126 C CB  . ALA B 302 ? 0.6766 0.6745 0.7458 0.1156  0.0506  0.0829  397  ALA B CB  
6127 N N   . GLU B 303 ? 0.7260 0.7548 0.8351 0.1244  0.0514  0.0725  398  GLU B N   
6128 C CA  . GLU B 303 ? 0.7327 0.7713 0.8604 0.1316  0.0486  0.0738  398  GLU B CA  
6129 C C   . GLU B 303 ? 0.7146 0.7437 0.8528 0.1377  0.0550  0.0727  398  GLU B C   
6130 O O   . GLU B 303 ? 0.7362 0.7577 0.8718 0.1351  0.0635  0.0666  398  GLU B O   
6131 C CB  . GLU B 303 ? 0.7750 0.8293 0.9120 0.1293  0.0494  0.0678  398  GLU B CB  
6132 C CG  . GLU B 303 ? 0.8822 0.9481 1.0131 0.1243  0.0425  0.0683  398  GLU B CG  
6133 C CD  . GLU B 303 ? 0.8225 0.8861 0.9400 0.1160  0.0468  0.0629  398  GLU B CD  
6134 O OE1 . GLU B 303 ? 0.8011 0.8522 0.9063 0.1133  0.0506  0.0628  398  GLU B OE1 
6135 O OE2 . GLU B 303 ? 0.8307 0.9048 0.9506 0.1121  0.0465  0.0588  398  GLU B OE2 
6136 N N   . ASN B 304 ? 0.7302 0.7597 0.8805 0.1461  0.0508  0.0785  399  ASN B N   
6137 C CA  . ASN B 304 ? 0.7323 0.7537 0.8954 0.1531  0.0568  0.0773  399  ASN B CA  
6138 C C   . ASN B 304 ? 0.7411 0.7766 0.9239 0.1564  0.0603  0.0715  399  ASN B C   
6139 O O   . ASN B 304 ? 0.7774 0.8215 0.9780 0.1640  0.0566  0.0746  399  ASN B O   
6140 C CB  . ASN B 304 ? 0.7367 0.7510 0.9043 0.1611  0.0508  0.0867  399  ASN B CB  
6141 C CG  . ASN B 304 ? 0.7572 0.7575 0.9341 0.1676  0.0579  0.0856  399  ASN B CG  
6142 O OD1 . ASN B 304 ? 0.7412 0.7392 0.9229 0.1666  0.0673  0.0773  399  ASN B OD1 
6143 N ND2 . ASN B 304 ? 0.7565 0.7469 0.9354 0.1743  0.0536  0.0941  399  ASN B ND2 
6144 N N   . SER B 305 ? 0.7110 0.7489 0.8905 0.1503  0.0679  0.0632  400  SER B N   
6145 C CA  . SER B 305 ? 0.6972 0.7465 0.8932 0.1521  0.0736  0.0569  400  SER B CA  
6146 C C   . SER B 305 ? 0.6945 0.7325 0.8874 0.1506  0.0854  0.0494  400  SER B C   
6147 O O   . SER B 305 ? 0.6638 0.6924 0.8393 0.1436  0.0888  0.0463  400  SER B O   
6148 C CB  . SER B 305 ? 0.7433 0.8082 0.9386 0.1458  0.0714  0.0538  400  SER B CB  
6149 O OG  . SER B 305 ? 0.8165 0.8881 1.0056 0.1438  0.0609  0.0594  400  SER B OG  
6150 N N   . ASN B 306 ? 0.6613 0.7007 0.8711 0.1569  0.0916  0.0461  401  ASN B N   
6151 C CA  . ASN B 306 ? 0.6760 0.7065 0.8843 0.1557  0.1035  0.0379  401  ASN B CA  
6152 C C   . ASN B 306 ? 0.6634 0.7091 0.8842 0.1549  0.1090  0.0320  401  ASN B C   
6153 O O   . ASN B 306 ? 0.7000 0.7533 0.9413 0.1619  0.1118  0.0310  401  ASN B O   
6154 C CB  . ASN B 306 ? 0.7068 0.7240 0.9235 0.1637  0.1079  0.0382  401  ASN B CB  
6155 C CG  . ASN B 306 ? 0.7331 0.7337 0.9366 0.1637  0.1034  0.0441  401  ASN B CG  
6156 O OD1 . ASN B 306 ? 0.7325 0.7201 0.9188 0.1574  0.1072  0.0410  401  ASN B OD1 
6157 N ND2 . ASN B 306 ? 0.7302 0.7316 0.9414 0.1703  0.0951  0.0528  401  ASN B ND2 
6158 N N   . THR B 307 ? 0.6350 0.6853 0.8441 0.1463  0.1106  0.0283  402  THR B N   
6159 C CA  . THR B 307 ? 0.5946 0.6580 0.8124 0.1438  0.1163  0.0230  402  THR B CA  
6160 C C   . THR B 307 ? 0.6223 0.6773 0.8242 0.1368  0.1254  0.0159  402  THR B C   
6161 O O   . THR B 307 ? 0.6223 0.6630 0.8067 0.1333  0.1260  0.0152  402  THR B O   
6162 C CB  . THR B 307 ? 0.6299 0.7092 0.8502 0.1400  0.1083  0.0260  402  THR B CB  
6163 O OG1 . THR B 307 ? 0.6293 0.7036 0.8285 0.1318  0.1053  0.0264  402  THR B OG1 
6164 C CG2 . THR B 307 ? 0.6190 0.7062 0.8511 0.1460  0.0974  0.0335  402  THR B CG2 
6165 N N   . TYR B 308 ? 0.6179 0.6824 0.8260 0.1344  0.1321  0.0109  403  TYR B N   
6166 C CA  . TYR B 308 ? 0.6258 0.6841 0.8186 0.1275  0.1405  0.0047  403  TYR B CA  
6167 C C   . TYR B 308 ? 0.5672 0.6231 0.7402 0.1193  0.1350  0.0064  403  TYR B C   
6168 O O   . TYR B 308 ? 0.5790 0.6268 0.7359 0.1137  0.1399  0.0023  403  TYR B O   
6169 C CB  . TYR B 308 ? 0.6178 0.6879 0.8222 0.1266  0.1489  0.0000  403  TYR B CB  
6170 C CG  . TYR B 308 ? 0.6571 0.7418 0.8646 0.1217  0.1440  0.0024  403  TYR B CG  
6171 C CD1 . TYR B 308 ? 0.6668 0.7502 0.8582 0.1133  0.1458  0.0006  403  TYR B CD1 
6172 C CD2 . TYR B 308 ? 0.6340 0.7331 0.8603 0.1256  0.1370  0.0066  403  TYR B CD2 
6173 C CE1 . TYR B 308 ? 0.6765 0.7716 0.8706 0.1088  0.1416  0.0028  403  TYR B CE1 
6174 C CE2 . TYR B 308 ? 0.6674 0.7791 0.8964 0.1206  0.1326  0.0082  403  TYR B CE2 
6175 C CZ  . TYR B 308 ? 0.7263 0.8353 0.9393 0.1123  0.1351  0.0062  403  TYR B CZ  
6176 O OH  . TYR B 308 ? 0.6982 0.8183 0.9142 0.1074  0.1309  0.0077  403  TYR B OH  
6177 N N   . ARG B 309 ? 0.5678 0.6305 0.7414 0.1186  0.1249  0.0122  404  ARG B N   
6178 C CA  . ARG B 309 ? 0.6263 0.6886 0.7837 0.1111  0.1204  0.0134  404  ARG B CA  
6179 C C   . ARG B 309 ? 0.6124 0.6692 0.7600 0.1105  0.1113  0.0186  404  ARG B C   
6180 O O   . ARG B 309 ? 0.6206 0.6766 0.7550 0.1047  0.1080  0.0192  404  ARG B O   
6181 C CB  . ARG B 309 ? 0.6691 0.7463 0.8341 0.1081  0.1182  0.0140  404  ARG B CB  
6182 C CG  . ARG B 309 ? 0.7298 0.8184 0.9086 0.1118  0.1093  0.0190  404  ARG B CG  
6183 C CD  . ARG B 309 ? 0.8059 0.9087 0.9929 0.1080  0.1087  0.0181  404  ARG B CD  
6184 N NE  . ARG B 309 ? 0.8535 0.9628 1.0386 0.1057  0.0985  0.0221  404  ARG B NE  
6185 C CZ  . ARG B 309 ? 0.8396 0.9557 1.0227 0.0999  0.0969  0.0213  404  ARG B CZ  
6186 N NH1 . ARG B 309 ? 0.7681 0.8848 0.9493 0.0953  0.1046  0.0174  404  ARG B NH1 
6187 N NH2 . ARG B 309 ? 0.8347 0.9568 1.0173 0.0984  0.0876  0.0244  404  ARG B NH2 
6188 N N   . HIS B 310 ? 0.6314 0.6841 0.7846 0.1163  0.1075  0.0226  405  HIS B N   
6189 C CA  . HIS B 310 ? 0.6503 0.6984 0.7940 0.1155  0.0992  0.0281  405  HIS B CA  
6190 C C   . HIS B 310 ? 0.5979 0.6293 0.7282 0.1141  0.1020  0.0271  405  HIS B C   
6191 O O   . HIS B 310 ? 0.5837 0.6066 0.7182 0.1180  0.1076  0.0249  405  HIS B O   
6192 C CB  . HIS B 310 ? 0.6065 0.6604 0.7628 0.1220  0.0919  0.0343  405  HIS B CB  
6193 C CG  . HIS B 310 ? 0.7028 0.7528 0.8482 0.1207  0.0835  0.0403  405  HIS B CG  
6194 N ND1 . HIS B 310 ? 0.7301 0.7674 0.8700 0.1234  0.0822  0.0441  405  HIS B ND1 
6195 C CD2 . HIS B 310 ? 0.7168 0.7734 0.8550 0.1164  0.0766  0.0428  405  HIS B CD2 
6196 C CE1 . HIS B 310 ? 0.7389 0.7756 0.8685 0.1208  0.0751  0.0490  405  HIS B CE1 
6197 N NE2 . HIS B 310 ? 0.7301 0.7785 0.8584 0.1167  0.0717  0.0480  405  HIS B NE2 
6198 N N   . LEU B 311 ? 0.6184 0.6457 0.7335 0.1085  0.0984  0.0284  406  LEU B N   
6199 C CA  . LEU B 311 ? 0.5928 0.6057 0.6955 0.1063  0.0996  0.0283  406  LEU B CA  
6200 C C   . LEU B 311 ? 0.6283 0.6401 0.7247 0.1054  0.0918  0.0347  406  LEU B C   
6201 O O   . LEU B 311 ? 0.5874 0.6089 0.6828 0.1035  0.0862  0.0372  406  LEU B O   
6202 C CB  . LEU B 311 ? 0.5536 0.5624 0.6430 0.0993  0.1038  0.0227  406  LEU B CB  
6203 C CG  . LEU B 311 ? 0.5915 0.5990 0.6819 0.0986  0.1122  0.0159  406  LEU B CG  
6204 C CD1 . LEU B 311 ? 0.5285 0.5347 0.6044 0.0913  0.1137  0.0121  406  LEU B CD1 
6205 C CD2 . LEU B 311 ? 0.5797 0.5751 0.6726 0.1022  0.1181  0.0130  406  LEU B CD2 
6206 N N   . CYS B 312 ? 0.5800 0.5792 0.6718 0.1066  0.0918  0.0372  407  CYS B N   
6207 C CA  . CYS B 312 ? 0.5720 0.5686 0.6561 0.1052  0.0855  0.0434  407  CYS B CA  
6208 C C   . CYS B 312 ? 0.5556 0.5508 0.6255 0.0974  0.0852  0.0414  407  CYS B C   
6209 O O   . CYS B 312 ? 0.5489 0.5462 0.6123 0.0952  0.0801  0.0456  407  CYS B O   
6210 C CB  . CYS B 312 ? 0.5597 0.5424 0.6438 0.1088  0.0862  0.0473  407  CYS B CB  
6211 S SG  . CYS B 312 ? 0.6079 0.5922 0.7100 0.1192  0.0854  0.0508  407  CYS B SG  
6212 N N   . GLU B 313 ? 0.5400 0.5322 0.6051 0.0933  0.0905  0.0351  408  GLU B N   
6213 C CA  . GLU B 313 ? 0.5420 0.5344 0.5954 0.0864  0.0900  0.0328  408  GLU B CA  
6214 C C   . GLU B 313 ? 0.5193 0.5172 0.5720 0.0837  0.0934  0.0270  408  GLU B C   
6215 O O   . GLU B 313 ? 0.5022 0.4969 0.5585 0.0854  0.0988  0.0229  408  GLU B O   
6216 C CB  . GLU B 313 ? 0.5093 0.4887 0.5546 0.0830  0.0925  0.0318  408  GLU B CB  
6217 C CG  . GLU B 313 ? 0.5820 0.5627 0.6170 0.0760  0.0916  0.0295  408  GLU B CG  
6218 C CD  . GLU B 313 ? 0.6290 0.5978 0.6576 0.0721  0.0945  0.0273  408  GLU B CD  
6219 O OE1 . GLU B 313 ? 0.6025 0.5726 0.6240 0.0664  0.0942  0.0244  408  GLU B OE1 
6220 O OE2 . GLU B 313 ? 0.6126 0.5708 0.6438 0.0748  0.0969  0.0284  408  GLU B OE2 
6221 N N   . TYR B 314 ? 0.4892 0.4949 0.5372 0.0798  0.0905  0.0267  409  TYR B N   
6222 C CA  . TYR B 314 ? 0.5115 0.5209 0.5571 0.0769  0.0936  0.0219  409  TYR B CA  
6223 C C   . TYR B 314 ? 0.4945 0.5078 0.5318 0.0719  0.0902  0.0219  409  TYR B C   
6224 O O   . TYR B 314 ? 0.5262 0.5392 0.5601 0.0705  0.0865  0.0248  409  TYR B O   
6225 C CB  . TYR B 314 ? 0.5001 0.5182 0.5558 0.0802  0.0948  0.0215  409  TYR B CB  
6226 C CG  . TYR B 314 ? 0.4931 0.5212 0.5542 0.0814  0.0891  0.0255  409  TYR B CG  
6227 C CD1 . TYR B 314 ? 0.5264 0.5620 0.5851 0.0780  0.0870  0.0249  409  TYR B CD1 
6228 C CD2 . TYR B 314 ? 0.5351 0.5645 0.6032 0.0858  0.0854  0.0300  409  TYR B CD2 
6229 C CE1 . TYR B 314 ? 0.5084 0.5526 0.5715 0.0785  0.0818  0.0278  409  TYR B CE1 
6230 C CE2 . TYR B 314 ? 0.5775 0.6162 0.6493 0.0865  0.0795  0.0333  409  TYR B CE2 
6231 C CZ  . TYR B 314 ? 0.5861 0.6321 0.6553 0.0826  0.0779  0.0318  409  TYR B CZ  
6232 O OH  . TYR B 314 ? 0.6826 0.7373 0.7550 0.0827  0.0722  0.0342  409  TYR B OH  
6233 N N   . VAL B 315 ? 0.4991 0.5154 0.5330 0.0691  0.0920  0.0185  410  VAL B N   
6234 C CA  . VAL B 315 ? 0.4934 0.5130 0.5203 0.0648  0.0891  0.0183  410  VAL B CA  
6235 C C   . VAL B 315 ? 0.4672 0.4963 0.4986 0.0653  0.0866  0.0198  410  VAL B C   
6236 O O   . VAL B 315 ? 0.4645 0.4969 0.5001 0.0663  0.0893  0.0185  410  VAL B O   
6237 C CB  . VAL B 315 ? 0.5083 0.5241 0.5271 0.0612  0.0918  0.0141  410  VAL B CB  
6238 C CG1 . VAL B 315 ? 0.4780 0.4981 0.4914 0.0577  0.0882  0.0144  410  VAL B CG1 
6239 C CG2 . VAL B 315 ? 0.4932 0.4996 0.5075 0.0598  0.0937  0.0120  410  VAL B CG2 
6240 N N   . SER B 316 ? 0.4512 0.4843 0.4817 0.0644  0.0820  0.0222  411  SER B N   
6241 C CA  . SER B 316 ? 0.4879 0.5289 0.5216 0.0641  0.0794  0.0231  411  SER B CA  
6242 C C   . SER B 316 ? 0.4579 0.4998 0.4854 0.0606  0.0786  0.0216  411  SER B C   
6243 O O   . SER B 316 ? 0.4493 0.4884 0.4710 0.0585  0.0775  0.0213  411  SER B O   
6244 C CB  . SER B 316 ? 0.4871 0.5319 0.5231 0.0654  0.0749  0.0263  411  SER B CB  
6245 O OG  . SER B 316 ? 0.4908 0.5432 0.5311 0.0653  0.0725  0.0265  411  SER B OG  
6246 N N   . LEU B 317 ? 0.4545 0.5001 0.4840 0.0599  0.0794  0.0208  412  LEU B N   
6247 C CA  . LEU B 317 ? 0.4344 0.4814 0.4598 0.0573  0.0780  0.0202  412  LEU B CA  
6248 C C   . LEU B 317 ? 0.4725 0.5253 0.5023 0.0575  0.0746  0.0214  412  LEU B C   
6249 O O   . LEU B 317 ? 0.4921 0.5491 0.5285 0.0584  0.0748  0.0217  412  LEU B O   
6250 C CB  . LEU B 317 ? 0.4112 0.4570 0.4348 0.0561  0.0814  0.0190  412  LEU B CB  
6251 C CG  . LEU B 317 ? 0.4910 0.5319 0.5116 0.0563  0.0860  0.0171  412  LEU B CG  
6252 C CD1 . LEU B 317 ? 0.4448 0.4851 0.4627 0.0549  0.0897  0.0162  412  LEU B CD1 
6253 C CD2 . LEU B 317 ? 0.4497 0.4851 0.4625 0.0549  0.0853  0.0159  412  LEU B CD2 
6254 N N   . ASP B 318 ? 0.4349 0.4882 0.4614 0.0564  0.0717  0.0216  413  ASP B N   
6255 C CA  . ASP B 318 ? 0.4324 0.4904 0.4615 0.0564  0.0686  0.0221  413  ASP B CA  
6256 C C   . ASP B 318 ? 0.4350 0.4936 0.4621 0.0546  0.0676  0.0209  413  ASP B C   
6257 O O   . ASP B 318 ? 0.4506 0.5065 0.4733 0.0537  0.0679  0.0204  413  ASP B O   
6258 C CB  . ASP B 318 ? 0.4257 0.4837 0.4527 0.0570  0.0665  0.0234  413  ASP B CB  
6259 C CG  . ASP B 318 ? 0.4926 0.5516 0.5236 0.0594  0.0660  0.0253  413  ASP B CG  
6260 O OD1 . ASP B 318 ? 0.4871 0.5418 0.5179 0.0607  0.0680  0.0261  413  ASP B OD1 
6261 O OD2 . ASP B 318 ? 0.5072 0.5711 0.5419 0.0601  0.0633  0.0259  413  ASP B OD2 
6262 N N   . VAL B 319 ? 0.4260 0.4879 0.4568 0.0542  0.0664  0.0203  414  VAL B N   
6263 C CA  . VAL B 319 ? 0.4144 0.4760 0.4443 0.0528  0.0656  0.0191  414  VAL B CA  
6264 C C   . VAL B 319 ? 0.4596 0.5248 0.4914 0.0525  0.0630  0.0178  414  VAL B C   
6265 O O   . VAL B 319 ? 0.4324 0.5013 0.4678 0.0528  0.0618  0.0180  414  VAL B O   
6266 C CB  . VAL B 319 ? 0.4627 0.5228 0.4947 0.0519  0.0675  0.0191  414  VAL B CB  
6267 C CG1 . VAL B 319 ? 0.4117 0.4696 0.4426 0.0510  0.0666  0.0185  414  VAL B CG1 
6268 C CG2 . VAL B 319 ? 0.4743 0.5309 0.5032 0.0521  0.0704  0.0201  414  VAL B CG2 
6269 N N   . GLU B 320 ? 0.3661 0.4309 0.3957 0.0519  0.0622  0.0163  415  GLU B N   
6270 C CA  . GLU B 320 ? 0.3990 0.4664 0.4292 0.0511  0.0603  0.0142  415  GLU B CA  
6271 C C   . GLU B 320 ? 0.4304 0.4955 0.4607 0.0507  0.0608  0.0122  415  GLU B C   
6272 O O   . GLU B 320 ? 0.3994 0.4624 0.4281 0.0515  0.0617  0.0127  415  GLU B O   
6273 C CB  . GLU B 320 ? 0.4237 0.4932 0.4498 0.0514  0.0591  0.0144  415  GLU B CB  
6274 C CG  . GLU B 320 ? 0.4230 0.4959 0.4482 0.0504  0.0567  0.0124  415  GLU B CG  
6275 C CD  . GLU B 320 ? 0.4597 0.5361 0.4880 0.0506  0.0543  0.0138  415  GLU B CD  
6276 O OE1 . GLU B 320 ? 0.4494 0.5258 0.4803 0.0521  0.0548  0.0166  415  GLU B OE1 
6277 O OE2 . GLU B 320 ? 0.4500 0.5297 0.4787 0.0494  0.0517  0.0118  415  GLU B OE2 
6278 N N   . MET B 321 ? 0.4235 0.4888 0.4564 0.0496  0.0601  0.0098  416  MET B N   
6279 C CA  . MET B 321 ? 0.4068 0.4685 0.4409 0.0496  0.0609  0.0081  416  MET B CA  
6280 C C   . MET B 321 ? 0.4201 0.4821 0.4562 0.0481  0.0601  0.0044  416  MET B C   
6281 O O   . MET B 321 ? 0.4456 0.5106 0.4832 0.0464  0.0587  0.0036  416  MET B O   
6282 C CB  . MET B 321 ? 0.3867 0.4441 0.4226 0.0497  0.0621  0.0105  416  MET B CB  
6283 C CG  . MET B 321 ? 0.4072 0.4644 0.4471 0.0477  0.0627  0.0107  416  MET B CG  
6284 S SD  . MET B 321 ? 0.4367 0.4892 0.4769 0.0471  0.0653  0.0143  416  MET B SD  
6285 C CE  . MET B 321 ? 0.3927 0.4380 0.4316 0.0481  0.0653  0.0147  416  MET B CE  
6286 N N   . THR B 322 ? 0.4045 0.4633 0.4411 0.0486  0.0608  0.0019  417  THR B N   
6287 C CA  . THR B 322 ? 0.4475 0.5050 0.4858 0.0469  0.0606  -0.0025 417  THR B CA  
6288 C C   . THR B 322 ? 0.4387 0.4917 0.4818 0.0454  0.0611  -0.0021 417  THR B C   
6289 O O   . THR B 322 ? 0.4062 0.4562 0.4506 0.0461  0.0621  0.0017  417  THR B O   
6290 C CB  . THR B 322 ? 0.4579 0.5133 0.4958 0.0484  0.0619  -0.0059 417  THR B CB  
6291 O OG1 . THR B 322 ? 0.4250 0.4757 0.4660 0.0507  0.0630  -0.0039 417  THR B OG1 
6292 C CG2 . THR B 322 ? 0.4272 0.4872 0.4606 0.0493  0.0623  -0.0062 417  THR B CG2 
6293 N N   . TYR B 323 ? 0.4648 0.5169 0.5101 0.0429  0.0606  -0.0062 418  TYR B N   
6294 C CA  . TYR B 323 ? 0.4739 0.5201 0.5241 0.0409  0.0617  -0.0065 418  TYR B CA  
6295 C C   . TYR B 323 ? 0.4661 0.5076 0.5172 0.0401  0.0622  -0.0120 418  TYR B C   
6296 O O   . TYR B 323 ? 0.4843 0.5282 0.5320 0.0408  0.0618  -0.0160 418  TYR B O   
6297 C CB  . TYR B 323 ? 0.4159 0.4659 0.4700 0.0375  0.0608  -0.0059 418  TYR B CB  
6298 C CG  . TYR B 323 ? 0.4477 0.5046 0.5016 0.0352  0.0578  -0.0099 418  TYR B CG  
6299 C CD1 . TYR B 323 ? 0.4525 0.5079 0.5085 0.0317  0.0569  -0.0154 418  TYR B CD1 
6300 C CD2 . TYR B 323 ? 0.4101 0.4744 0.4613 0.0362  0.0556  -0.0081 418  TYR B CD2 
6301 C CE1 . TYR B 323 ? 0.4386 0.5007 0.4933 0.0293  0.0533  -0.0191 418  TYR B CE1 
6302 C CE2 . TYR B 323 ? 0.4637 0.5343 0.5139 0.0344  0.0521  -0.0110 418  TYR B CE2 
6303 C CZ  . TYR B 323 ? 0.4492 0.5191 0.5007 0.0308  0.0507  -0.0166 418  TYR B CZ  
6304 O OH  . TYR B 323 ? 0.4612 0.5378 0.5106 0.0287  0.0464  -0.0195 418  TYR B OH  
6305 N N   . LYS B 324 ? 0.4506 0.4847 0.5060 0.0387  0.0636  -0.0125 419  LYS B N   
6306 C CA  . LYS B 324 ? 0.4879 0.5154 0.5450 0.0382  0.0647  -0.0179 419  LYS B CA  
6307 C C   . LYS B 324 ? 0.5153 0.5448 0.5734 0.0333  0.0634  -0.0239 419  LYS B C   
6308 O O   . LYS B 324 ? 0.4939 0.5255 0.5485 0.0329  0.0627  -0.0295 419  LYS B O   
6309 C CB  . LYS B 324 ? 0.5116 0.5285 0.5726 0.0390  0.0668  -0.0151 419  LYS B CB  
6310 C CG  . LYS B 324 ? 0.5245 0.5393 0.5841 0.0440  0.0672  -0.0096 419  LYS B CG  
6311 C CD  . LYS B 324 ? 0.6062 0.6107 0.6685 0.0445  0.0686  -0.0052 419  LYS B CD  
6312 C CE  . LYS B 324 ? 0.6960 0.6989 0.7567 0.0496  0.0680  -0.0001 419  LYS B CE  
6313 N NZ  . LYS B 324 ? 0.8312 0.8241 0.8924 0.0502  0.0687  0.0057  419  LYS B NZ  
6314 N N   . TYR B 325 ? 0.4637 0.4931 0.5264 0.0293  0.0630  -0.0229 420  TYR B N   
6315 C CA  . TYR B 325 ? 0.5035 0.5351 0.5687 0.0241  0.0613  -0.0288 420  TYR B CA  
6316 C C   . TYR B 325 ? 0.5157 0.5567 0.5844 0.0210  0.0588  -0.0267 420  TYR B C   
6317 O O   . TYR B 325 ? 0.5589 0.6061 0.6281 0.0175  0.0555  -0.0312 420  TYR B O   
6318 C CB  . TYR B 325 ? 0.5135 0.5338 0.5837 0.0213  0.0637  -0.0316 420  TYR B CB  
6319 C CG  . TYR B 325 ? 0.5476 0.5594 0.6156 0.0246  0.0658  -0.0352 420  TYR B CG  
6320 C CD1 . TYR B 325 ? 0.5860 0.5995 0.6498 0.0240  0.0651  -0.0427 420  TYR B CD1 
6321 C CD2 . TYR B 325 ? 0.5747 0.5771 0.6443 0.0286  0.0686  -0.0308 420  TYR B CD2 
6322 C CE1 . TYR B 325 ? 0.5706 0.5769 0.6331 0.0273  0.0677  -0.0465 420  TYR B CE1 
6323 C CE2 . TYR B 325 ? 0.6071 0.6024 0.6764 0.0323  0.0704  -0.0342 420  TYR B CE2 
6324 C CZ  . TYR B 325 ? 0.5842 0.5817 0.6505 0.0316  0.0704  -0.0423 420  TYR B CZ  
6325 O OH  . TYR B 325 ? 0.6860 0.6773 0.7528 0.0354  0.0730  -0.0465 420  TYR B OH  
6326 N N   . ASP B 326 ? 0.5003 0.5428 0.5714 0.0223  0.0601  -0.0203 421  ASP B N   
6327 C CA  . ASP B 326 ? 0.4957 0.5464 0.5726 0.0195  0.0589  -0.0184 421  ASP B CA  
6328 C C   . ASP B 326 ? 0.4639 0.5198 0.5383 0.0235  0.0592  -0.0125 421  ASP B C   
6329 O O   . ASP B 326 ? 0.4524 0.5028 0.5243 0.0263  0.0620  -0.0081 421  ASP B O   
6330 C CB  . ASP B 326 ? 0.5121 0.5572 0.5965 0.0155  0.0622  -0.0172 421  ASP B CB  
6331 C CG  . ASP B 326 ? 0.5801 0.6346 0.6731 0.0116  0.0613  -0.0170 421  ASP B CG  
6332 O OD1 . ASP B 326 ? 0.5366 0.6011 0.6302 0.0135  0.0591  -0.0149 421  ASP B OD1 
6333 O OD2 . ASP B 326 ? 0.6641 0.7158 0.7643 0.0065  0.0630  -0.0187 421  ASP B OD2 
6334 N N   . TYR B 327 ? 0.4565 0.5225 0.5314 0.0239  0.0559  -0.0124 422  TYR B N   
6335 C CA  . TYR B 327 ? 0.4914 0.5615 0.5643 0.0277  0.0563  -0.0073 422  TYR B CA  
6336 C C   . TYR B 327 ? 0.4655 0.5341 0.5433 0.0273  0.0603  -0.0030 422  TYR B C   
6337 O O   . TYR B 327 ? 0.4559 0.5239 0.5302 0.0306  0.0620  0.0011  422  TYR B O   
6338 C CB  . TYR B 327 ? 0.4557 0.5363 0.5295 0.0282  0.0519  -0.0076 422  TYR B CB  
6339 C CG  . TYR B 327 ? 0.4594 0.5479 0.5439 0.0257  0.0511  -0.0071 422  TYR B CG  
6340 C CD1 . TYR B 327 ? 0.4353 0.5289 0.5235 0.0283  0.0521  -0.0029 422  TYR B CD1 
6341 C CD2 . TYR B 327 ? 0.5181 0.6090 0.6099 0.0207  0.0496  -0.0112 422  TYR B CD2 
6342 C CE1 . TYR B 327 ? 0.4863 0.5880 0.5860 0.0264  0.0518  -0.0027 422  TYR B CE1 
6343 C CE2 . TYR B 327 ? 0.4944 0.5938 0.5979 0.0182  0.0490  -0.0110 422  TYR B CE2 
6344 C CZ  . TYR B 327 ? 0.5017 0.6069 0.6095 0.0213  0.0502  -0.0066 422  TYR B CZ  
6345 O OH  . TYR B 327 ? 0.5022 0.6168 0.6231 0.0192  0.0501  -0.0066 422  TYR B OH  
6346 N N   . LEU B 328 ? 0.4496 0.5168 0.5347 0.0231  0.0621  -0.0041 423  LEU B N   
6347 C CA  . LEU B 328 ? 0.4748 0.5399 0.5635 0.0222  0.0668  0.0000  423  LEU B CA  
6348 C C   . LEU B 328 ? 0.4773 0.5320 0.5581 0.0247  0.0701  0.0037  423  LEU B C   
6349 O O   . LEU B 328 ? 0.4604 0.5138 0.5399 0.0255  0.0735  0.0079  423  LEU B O   
6350 C CB  . LEU B 328 ? 0.4571 0.5221 0.5552 0.0163  0.0687  -0.0020 423  LEU B CB  
6351 C CG  . LEU B 328 ? 0.5371 0.6147 0.6453 0.0137  0.0655  -0.0049 423  LEU B CG  
6352 C CD1 . LEU B 328 ? 0.5242 0.6021 0.6427 0.0071  0.0669  -0.0079 423  LEU B CD1 
6353 C CD2 . LEU B 328 ? 0.4767 0.5626 0.5887 0.0164  0.0668  -0.0014 423  LEU B CD2 
6354 N N   . GLU B 329 ? 0.4568 0.5044 0.5324 0.0261  0.0689  0.0023  424  GLU B N   
6355 C CA  . GLU B 329 ? 0.4764 0.5160 0.5449 0.0295  0.0706  0.0061  424  GLU B CA  
6356 C C   . GLU B 329 ? 0.4949 0.5388 0.5586 0.0330  0.0706  0.0094  424  GLU B C   
6357 O O   . GLU B 329 ? 0.4471 0.4870 0.5069 0.0340  0.0731  0.0136  424  GLU B O   
6358 C CB  . GLU B 329 ? 0.4839 0.5185 0.5488 0.0318  0.0687  0.0034  424  GLU B CB  
6359 C CG  . GLU B 329 ? 0.5193 0.5475 0.5878 0.0290  0.0689  -0.0006 424  GLU B CG  
6360 C CD  . GLU B 329 ? 0.5315 0.5585 0.5973 0.0314  0.0669  -0.0052 424  GLU B CD  
6361 O OE1 . GLU B 329 ? 0.4783 0.5060 0.5393 0.0357  0.0663  -0.0036 424  GLU B OE1 
6362 O OE2 . GLU B 329 ? 0.5080 0.5336 0.5764 0.0286  0.0662  -0.0107 424  GLU B OE2 
6363 N N   . ASN B 330 ? 0.4487 0.5003 0.5120 0.0346  0.0677  0.0075  425  ASN B N   
6364 C CA  . ASN B 330 ? 0.4325 0.4873 0.4916 0.0377  0.0678  0.0103  425  ASN B CA  
6365 C C   . ASN B 330 ? 0.4573 0.5158 0.5203 0.0367  0.0705  0.0125  425  ASN B C   
6366 O O   . ASN B 330 ? 0.4298 0.4869 0.4886 0.0385  0.0726  0.0154  425  ASN B O   
6367 C CB  . ASN B 330 ? 0.3977 0.4585 0.4551 0.0395  0.0643  0.0082  425  ASN B CB  
6368 C CG  . ASN B 330 ? 0.4343 0.4920 0.4873 0.0408  0.0627  0.0058  425  ASN B CG  
6369 O OD1 . ASN B 330 ? 0.4596 0.5108 0.5113 0.0412  0.0639  0.0060  425  ASN B OD1 
6370 N ND2 . ASN B 330 ? 0.4287 0.4910 0.4792 0.0416  0.0602  0.0041  425  ASN B ND2 
6371 N N   . VAL B 331 ? 0.4492 0.5130 0.5207 0.0338  0.0706  0.0107  426  VAL B N   
6372 C CA  . VAL B 331 ? 0.4277 0.4965 0.5047 0.0331  0.0736  0.0123  426  VAL B CA  
6373 C C   . VAL B 331 ? 0.4536 0.5155 0.5274 0.0319  0.0789  0.0155  426  VAL B C   
6374 O O   . VAL B 331 ? 0.4257 0.4875 0.4964 0.0335  0.0819  0.0178  426  VAL B O   
6375 C CB  . VAL B 331 ? 0.4164 0.4932 0.5049 0.0299  0.0725  0.0097  426  VAL B CB  
6376 C CG1 . VAL B 331 ? 0.4096 0.4919 0.5058 0.0293  0.0766  0.0112  426  VAL B CG1 
6377 C CG2 . VAL B 331 ? 0.4173 0.5013 0.5072 0.0314  0.0665  0.0072  426  VAL B CG2 
6378 N N   . HIS B 332 ? 0.4402 0.4951 0.5135 0.0292  0.0802  0.0157  427  HIS B N   
6379 C CA  . HIS B 332 ? 0.4935 0.5404 0.5616 0.0280  0.0848  0.0196  427  HIS B CA  
6380 C C   . HIS B 332 ? 0.4745 0.5167 0.5314 0.0318  0.0843  0.0223  427  HIS B C   
6381 O O   . HIS B 332 ? 0.4612 0.5010 0.5129 0.0319  0.0879  0.0252  427  HIS B O   
6382 C CB  . HIS B 332 ? 0.5188 0.5575 0.5878 0.0249  0.0855  0.0197  427  HIS B CB  
6383 C CG  . HIS B 332 ? 0.5847 0.6278 0.6649 0.0201  0.0865  0.0167  427  HIS B CG  
6384 N ND1 . HIS B 332 ? 0.5842 0.6342 0.6721 0.0174  0.0903  0.0169  427  HIS B ND1 
6385 C CD2 . HIS B 332 ? 0.5727 0.6147 0.6585 0.0173  0.0843  0.0131  427  HIS B CD2 
6386 C CE1 . HIS B 332 ? 0.5710 0.6247 0.6693 0.0129  0.0899  0.0137  427  HIS B CE1 
6387 N NE2 . HIS B 332 ? 0.5789 0.6273 0.6755 0.0126  0.0862  0.0112  427  HIS B NE2 
6388 N N   . PHE B 333 ? 0.4585 0.5005 0.5120 0.0349  0.0799  0.0210  428  PHE B N   
6389 C CA  . PHE B 333 ? 0.4753 0.5144 0.5198 0.0381  0.0790  0.0232  428  PHE B CA  
6390 C C   . PHE B 333 ? 0.4273 0.4714 0.4704 0.0394  0.0805  0.0234  428  PHE B C   
6391 O O   . PHE B 333 ? 0.4403 0.4812 0.4766 0.0398  0.0828  0.0258  428  PHE B O   
6392 C CB  . PHE B 333 ? 0.4259 0.4649 0.4687 0.0408  0.0746  0.0214  428  PHE B CB  
6393 C CG  . PHE B 333 ? 0.4663 0.5038 0.5015 0.0437  0.0732  0.0232  428  PHE B CG  
6394 C CD1 . PHE B 333 ? 0.4702 0.5009 0.4996 0.0445  0.0730  0.0263  428  PHE B CD1 
6395 C CD2 . PHE B 333 ? 0.4327 0.4755 0.4668 0.0454  0.0720  0.0221  428  PHE B CD2 
6396 C CE1 . PHE B 333 ? 0.5326 0.5630 0.5558 0.0468  0.0711  0.0277  428  PHE B CE1 
6397 C CE2 . PHE B 333 ? 0.4449 0.4865 0.4728 0.0473  0.0708  0.0233  428  PHE B CE2 
6398 C CZ  . PHE B 333 ? 0.4363 0.4723 0.4590 0.0479  0.0702  0.0258  428  PHE B CZ  
6399 N N   . TYR B 334 ? 0.4320 0.4839 0.4817 0.0399  0.0793  0.0210  429  TYR B N   
6400 C CA  . TYR B 334 ? 0.4135 0.4691 0.4629 0.0415  0.0811  0.0213  429  TYR B CA  
6401 C C   . TYR B 334 ? 0.4392 0.4940 0.4897 0.0395  0.0869  0.0227  429  TYR B C   
6402 O O   . TYR B 334 ? 0.4299 0.4829 0.4748 0.0405  0.0898  0.0236  429  TYR B O   
6403 C CB  . TYR B 334 ? 0.4387 0.5025 0.4959 0.0427  0.0786  0.0192  429  TYR B CB  
6404 C CG  . TYR B 334 ? 0.4328 0.4977 0.4882 0.0440  0.0736  0.0178  429  TYR B CG  
6405 C CD1 . TYR B 334 ? 0.4264 0.4869 0.4739 0.0456  0.0721  0.0183  429  TYR B CD1 
6406 C CD2 . TYR B 334 ? 0.4367 0.5078 0.4985 0.0435  0.0703  0.0157  429  TYR B CD2 
6407 C CE1 . TYR B 334 ? 0.4725 0.5342 0.5185 0.0465  0.0685  0.0168  429  TYR B CE1 
6408 C CE2 . TYR B 334 ? 0.4134 0.4851 0.4719 0.0444  0.0663  0.0142  429  TYR B CE2 
6409 C CZ  . TYR B 334 ? 0.4358 0.5027 0.4866 0.0459  0.0659  0.0147  429  TYR B CZ  
6410 O OH  . TYR B 334 ? 0.4347 0.5024 0.4824 0.0465  0.0630  0.0131  429  TYR B OH  
6411 N N   . ASP B 335 ? 0.4416 0.4970 0.4984 0.0362  0.0891  0.0226  430  ASP B N   
6412 C CA  . ASP B 335 ? 0.4258 0.4806 0.4839 0.0338  0.0955  0.0239  430  ASP B CA  
6413 C C   . ASP B 335 ? 0.4795 0.5251 0.5245 0.0335  0.0980  0.0271  430  ASP B C   
6414 O O   . ASP B 335 ? 0.4408 0.4855 0.4808 0.0336  0.1024  0.0278  430  ASP B O   
6415 C CB  . ASP B 335 ? 0.4457 0.5024 0.5134 0.0296  0.0971  0.0232  430  ASP B CB  
6416 C CG  . ASP B 335 ? 0.4470 0.5023 0.5157 0.0261  0.1046  0.0250  430  ASP B CG  
6417 O OD1 . ASP B 335 ? 0.4464 0.5051 0.5154 0.0271  0.1090  0.0248  430  ASP B OD1 
6418 O OD2 . ASP B 335 ? 0.4785 0.5292 0.5483 0.0222  0.1066  0.0263  430  ASP B OD2 
6419 N N   . SER B 336 ? 0.4322 0.4710 0.4712 0.0335  0.0948  0.0288  431  SER B N   
6420 C CA  . SER B 336 ? 0.4731 0.5034 0.4996 0.0334  0.0960  0.0325  431  SER B CA  
6421 C C   . SER B 336 ? 0.4552 0.4860 0.4736 0.0362  0.0948  0.0321  431  SER B C   
6422 O O   . SER B 336 ? 0.4979 0.5248 0.5069 0.0355  0.0981  0.0338  431  SER B O   
6423 C CB  . SER B 336 ? 0.4602 0.4835 0.4836 0.0337  0.0922  0.0345  431  SER B CB  
6424 O OG  . SER B 336 ? 0.5948 0.6203 0.6183 0.0371  0.0865  0.0326  431  SER B OG  
6425 N N   . MET B 337 ? 0.4225 0.4583 0.4445 0.0390  0.0907  0.0294  432  MET B N   
6426 C CA  . MET B 337 ? 0.4545 0.4907 0.4702 0.0411  0.0899  0.0286  432  MET B CA  
6427 C C   . MET B 337 ? 0.4301 0.4677 0.4451 0.0405  0.0956  0.0277  432  MET B C   
6428 O O   . MET B 337 ? 0.4487 0.4821 0.4535 0.0401  0.0977  0.0283  432  MET B O   
6429 C CB  . MET B 337 ? 0.4234 0.4645 0.4443 0.0436  0.0854  0.0262  432  MET B CB  
6430 C CG  . MET B 337 ? 0.4495 0.4909 0.4653 0.0455  0.0847  0.0251  432  MET B CG  
6431 S SD  . MET B 337 ? 0.5353 0.5815 0.5564 0.0478  0.0800  0.0232  432  MET B SD  
6432 C CE  . MET B 337 ? 0.4684 0.5211 0.5004 0.0483  0.0816  0.0218  432  MET B CE  
6433 N N   . PHE B 338 ? 0.4317 0.4752 0.4575 0.0400  0.0985  0.0261  433  PHE B N   
6434 C CA  . PHE B 338 ? 0.4385 0.4837 0.4651 0.0400  0.1046  0.0248  433  PHE B CA  
6435 C C   . PHE B 338 ? 0.4653 0.5054 0.4843 0.0368  0.1106  0.0267  433  PHE B C   
6436 O O   . PHE B 338 ? 0.4409 0.4783 0.4519 0.0367  0.1148  0.0260  433  PHE B O   
6437 C CB  . PHE B 338 ? 0.4577 0.5117 0.4994 0.0407  0.1060  0.0227  433  PHE B CB  
6438 C CG  . PHE B 338 ? 0.4725 0.5302 0.5180 0.0445  0.1030  0.0209  433  PHE B CG  
6439 C CD1 . PHE B 338 ? 0.5047 0.5620 0.5491 0.0463  0.1070  0.0193  433  PHE B CD1 
6440 C CD2 . PHE B 338 ? 0.4585 0.5187 0.5071 0.0460  0.0965  0.0208  433  PHE B CD2 
6441 C CE1 . PHE B 338 ? 0.5315 0.5906 0.5790 0.0499  0.1043  0.0181  433  PHE B CE1 
6442 C CE2 . PHE B 338 ? 0.4687 0.5311 0.5194 0.0493  0.0939  0.0199  433  PHE B CE2 
6443 C CZ  . PHE B 338 ? 0.4616 0.5232 0.5121 0.0512  0.0977  0.0188  433  PHE B CZ  
6444 N N   . LYS B 339 ? 0.4448 0.4824 0.4645 0.0339  0.1110  0.0292  434  LYS B N   
6445 C CA  . LYS B 339 ? 0.4719 0.5037 0.4831 0.0306  0.1171  0.0317  434  LYS B CA  
6446 C C   . LYS B 339 ? 0.5123 0.5367 0.5065 0.0312  0.1156  0.0336  434  LYS B C   
6447 O O   . LYS B 339 ? 0.5079 0.5290 0.4925 0.0297  0.1210  0.0337  434  LYS B O   
6448 C CB  . LYS B 339 ? 0.4663 0.4950 0.4806 0.0273  0.1174  0.0347  434  LYS B CB  
6449 C CG  . LYS B 339 ? 0.4886 0.5251 0.5201 0.0260  0.1181  0.0324  434  LYS B CG  
6450 C CD  . LYS B 339 ? 0.5137 0.5473 0.5489 0.0211  0.1222  0.0347  434  LYS B CD  
6451 C CE  . LYS B 339 ? 0.5511 0.5739 0.5767 0.0201  0.1194  0.0389  434  LYS B CE  
6452 N NZ  . LYS B 339 ? 0.5167 0.5369 0.5498 0.0157  0.1212  0.0401  434  LYS B NZ  
6453 N N   . HIS B 340 ? 0.4902 0.5127 0.4811 0.0335  0.1081  0.0342  435  HIS B N   
6454 C CA  . HIS B 340 ? 0.5096 0.5264 0.4858 0.0342  0.1051  0.0359  435  HIS B CA  
6455 C C   . HIS B 340 ? 0.4841 0.5022 0.4554 0.0351  0.1071  0.0324  435  HIS B C   
6456 O O   . HIS B 340 ? 0.5071 0.5204 0.4650 0.0336  0.1096  0.0330  435  HIS B O   
6457 C CB  . HIS B 340 ? 0.4923 0.5088 0.4699 0.0366  0.0969  0.0368  435  HIS B CB  
6458 C CG  . HIS B 340 ? 0.5503 0.5632 0.5158 0.0376  0.0925  0.0380  435  HIS B CG  
6459 N ND1 . HIS B 340 ? 0.5883 0.5942 0.5416 0.0364  0.0916  0.0423  435  HIS B ND1 
6460 C CD2 . HIS B 340 ? 0.5247 0.5400 0.4884 0.0395  0.0885  0.0355  435  HIS B CD2 
6461 C CE1 . HIS B 340 ? 0.5498 0.5550 0.4948 0.0376  0.0867  0.0422  435  HIS B CE1 
6462 N NE2 . HIS B 340 ? 0.5388 0.5497 0.4903 0.0392  0.0850  0.0379  435  HIS B NE2 
6463 N N   . ILE B 341 ? 0.4839 0.5082 0.4655 0.0373  0.1067  0.0287  436  ILE B N   
6464 C CA  . ILE B 341 ? 0.4917 0.5164 0.4702 0.0383  0.1095  0.0251  436  ILE B CA  
6465 C C   . ILE B 341 ? 0.5113 0.5343 0.4856 0.0361  0.1182  0.0243  436  ILE B C   
6466 O O   . ILE B 341 ? 0.4864 0.5046 0.4479 0.0349  0.1208  0.0231  436  ILE B O   
6467 C CB  . ILE B 341 ? 0.4796 0.5105 0.4711 0.0413  0.1080  0.0222  436  ILE B CB  
6468 C CG1 . ILE B 341 ? 0.4404 0.4721 0.4328 0.0430  0.1002  0.0227  436  ILE B CG1 
6469 C CG2 . ILE B 341 ? 0.4821 0.5126 0.4725 0.0424  0.1124  0.0185  436  ILE B CG2 
6470 C CD1 . ILE B 341 ? 0.4588 0.4966 0.4640 0.0456  0.0979  0.0212  436  ILE B CD1 
6471 N N   . PHE B 342 ? 0.4680 0.4948 0.4524 0.0349  0.1230  0.0248  437  PHE B N   
6472 C CA  . PHE B 342 ? 0.5309 0.5570 0.5127 0.0327  0.1323  0.0237  437  PHE B CA  
6473 C C   . PHE B 342 ? 0.5352 0.5529 0.4984 0.0293  0.1342  0.0267  437  PHE B C   
6474 O O   . PHE B 342 ? 0.4959 0.5098 0.4475 0.0282  0.1392  0.0248  437  PHE B O   
6475 C CB  . PHE B 342 ? 0.4951 0.5276 0.4921 0.0314  0.1370  0.0239  437  PHE B CB  
6476 C CG  . PHE B 342 ? 0.4986 0.5401 0.5138 0.0347  0.1342  0.0214  437  PHE B CG  
6477 C CD1 . PHE B 342 ? 0.4431 0.4865 0.4610 0.0386  0.1326  0.0182  437  PHE B CD1 
6478 C CD2 . PHE B 342 ? 0.4776 0.5252 0.5068 0.0338  0.1328  0.0224  437  PHE B CD2 
6479 C CE1 . PHE B 342 ? 0.4452 0.4963 0.4787 0.0418  0.1295  0.0168  437  PHE B CE1 
6480 C CE2 . PHE B 342 ? 0.4661 0.5223 0.5109 0.0367  0.1294  0.0204  437  PHE B CE2 
6481 C CZ  . PHE B 342 ? 0.4320 0.4900 0.4787 0.0409  0.1276  0.0179  437  PHE B CZ  
6482 N N   . THR B 343 ? 0.5284 0.5423 0.4875 0.0281  0.1294  0.0315  438  THR B N   
6483 C CA  . THR B 343 ? 0.5187 0.5242 0.4601 0.0251  0.1305  0.0356  438  THR B CA  
6484 C C   . THR B 343 ? 0.5602 0.5616 0.4862 0.0258  0.1275  0.0341  438  THR B C   
6485 O O   . THR B 343 ? 0.5618 0.5582 0.4726 0.0232  0.1322  0.0343  438  THR B O   
6486 C CB  . THR B 343 ? 0.5262 0.5278 0.4673 0.0248  0.1246  0.0411  438  THR B CB  
6487 O OG1 . THR B 343 ? 0.5177 0.5222 0.4722 0.0232  0.1281  0.0420  438  THR B OG1 
6488 C CG2 . THR B 343 ? 0.5226 0.5147 0.4442 0.0223  0.1245  0.0464  438  THR B CG2 
6489 N N   . GLU B 344 ? 0.5486 0.5527 0.4786 0.0289  0.1201  0.0321  439  GLU B N   
6490 C CA  . GLU B 344 ? 0.5696 0.5703 0.4859 0.0290  0.1160  0.0307  439  GLU B CA  
6491 C C   . GLU B 344 ? 0.6162 0.6169 0.5289 0.0286  0.1222  0.0250  439  GLU B C   
6492 O O   . GLU B 344 ? 0.6269 0.6226 0.5234 0.0266  0.1229  0.0237  439  GLU B O   
6493 C CB  . GLU B 344 ? 0.5796 0.5833 0.5022 0.0320  0.1067  0.0304  439  GLU B CB  
6494 C CG  . GLU B 344 ? 0.5432 0.5455 0.4665 0.0326  0.1003  0.0358  439  GLU B CG  
6495 C CD  . GLU B 344 ? 0.6889 0.6844 0.5946 0.0308  0.0979  0.0400  439  GLU B CD  
6496 O OE1 . GLU B 344 ? 0.7060 0.7004 0.6011 0.0304  0.0947  0.0383  439  GLU B OE1 
6497 O OE2 . GLU B 344 ? 0.7123 0.7034 0.6145 0.0295  0.0992  0.0452  439  GLU B OE2 
6498 N N   . LEU B 345 ? 0.5505 0.5564 0.4779 0.0304  0.1270  0.0214  440  LEU B N   
6499 C CA  . LEU B 345 ? 0.6101 0.6154 0.5354 0.0305  0.1336  0.0158  440  LEU B CA  
6500 C C   . LEU B 345 ? 0.5967 0.5982 0.5108 0.0271  0.1429  0.0155  440  LEU B C   
6501 O O   . LEU B 345 ? 0.6627 0.6599 0.5646 0.0258  0.1470  0.0115  440  LEU B O   
6502 C CB  . LEU B 345 ? 0.5574 0.5695 0.5022 0.0338  0.1362  0.0127  440  LEU B CB  
6503 C CG  . LEU B 345 ? 0.5628 0.5775 0.5163 0.0372  0.1292  0.0113  440  LEU B CG  
6504 C CD1 . LEU B 345 ? 0.5685 0.5898 0.5408 0.0405  0.1320  0.0096  440  LEU B CD1 
6505 C CD2 . LEU B 345 ? 0.5543 0.5638 0.4971 0.0370  0.1279  0.0074  440  LEU B CD2 
6506 N N   . SER B 346 ? 0.6218 0.6242 0.5389 0.0252  0.1466  0.0196  441  SER B N   
6507 C CA  . SER B 346 ? 0.6210 0.6211 0.5311 0.0217  0.1572  0.0194  441  SER B CA  
6508 C C   . SER B 346 ? 0.7072 0.6987 0.5938 0.0178  0.1571  0.0232  441  SER B C   
6509 O O   . SER B 346 ? 0.7422 0.7309 0.6208 0.0143  0.1660  0.0241  441  SER B O   
6510 C CB  . SER B 346 ? 0.5493 0.5548 0.4750 0.0209  0.1617  0.0220  441  SER B CB  
6511 O OG  . SER B 346 ? 0.6259 0.6400 0.5732 0.0246  0.1599  0.0193  441  SER B OG  
6512 N N   . LYS B 347 ? 0.6954 0.6829 0.5709 0.0182  0.1475  0.0256  442  LYS B N   
6513 C CA  . LYS B 347 ? 0.7892 0.7689 0.6435 0.0148  0.1461  0.0307  442  LYS B CA  
6514 C C   . LYS B 347 ? 0.8782 0.8530 0.7124 0.0130  0.1464  0.0268  442  LYS B C   
6515 O O   . LYS B 347 ? 0.8259 0.8022 0.6621 0.0135  0.1517  0.0197  442  LYS B O   
6516 C CB  . LYS B 347 ? 0.7551 0.7338 0.6106 0.0164  0.1350  0.0370  442  LYS B CB  
6517 C CG  . LYS B 347 ? 0.7819 0.7620 0.6361 0.0190  0.1250  0.0347  442  LYS B CG  
6518 C CD  . LYS B 347 ? 0.8358 0.8162 0.6947 0.0211  0.1150  0.0404  442  LYS B CD  
6519 C CE  . LYS B 347 ? 0.8753 0.8567 0.7291 0.0227  0.1052  0.0390  442  LYS B CE  
6520 N NZ  . LYS B 347 ? 0.7762 0.7620 0.6372 0.0238  0.1062  0.0314  442  LYS B NZ  
6521 N N   . GLY B 348 ? 1.0997 1.0681 0.9141 0.0108  0.1411  0.0316  443  GLY B N   
6522 C CA  . GLY B 348 ? 1.0699 1.0360 0.8703 0.0106  0.1334  0.0292  443  GLY B CA  
6523 C C   . GLY B 348 ? 1.0897 1.0524 0.8752 0.0077  0.1403  0.0222  443  GLY B C   
6524 O O   . GLY B 348 ? 1.1399 1.1018 0.9250 0.0061  0.1520  0.0189  443  GLY B O   
6525 N N   . GLY B 349 ? 0.9702 0.9310 0.7433 0.0070  0.1329  0.0195  444  GLY B N   
6526 C CA  . GLY B 349 ? 0.9121 0.8690 0.6701 0.0041  0.1382  0.0119  444  GLY B CA  
6527 C C   . GLY B 349 ? 0.8362 0.7966 0.6091 0.0066  0.1394  0.0035  444  GLY B C   
6528 O O   . GLY B 349 ? 0.8423 0.8019 0.6187 0.0065  0.1500  -0.0027 444  GLY B O   
6529 N N   . LYS B 350 ? 0.7975 0.7615 0.5797 0.0089  0.1291  0.0033  445  LYS B N   
6530 C CA  . LYS B 350 ? 0.8004 0.7663 0.5945 0.0107  0.1296  -0.0042 445  LYS B CA  
6531 C C   . LYS B 350 ? 0.7405 0.7102 0.5559 0.0143  0.1379  -0.0059 445  LYS B C   
6532 O O   . LYS B 350 ? 0.7116 0.6796 0.5302 0.0148  0.1456  -0.0129 445  LYS B O   
6533 C CB  . LYS B 350 ? 0.7582 0.7280 0.5598 0.0123  0.1173  -0.0029 445  LYS B CB  
6534 C CG  . LYS B 350 ? 0.8246 0.7949 0.6364 0.0134  0.1173  -0.0103 445  LYS B CG  
6535 C CD  . LYS B 350 ? 0.7917 0.7671 0.6142 0.0150  0.1064  -0.0084 445  LYS B CD  
6536 N N   . ASN B 351 ? 0.6924 0.6672 0.5225 0.0169  0.1362  0.0002  446  ASN B N   
6537 C CA  . ASN B 351 ? 0.6632 0.6431 0.5149 0.0205  0.1420  -0.0012 446  ASN B CA  
6538 C C   . ASN B 351 ? 0.7162 0.6949 0.5669 0.0194  0.1549  -0.0041 446  ASN B C   
6539 O O   . ASN B 351 ? 0.6406 0.6218 0.5049 0.0221  0.1612  -0.0088 446  ASN B O   
6540 C CB  . ASN B 351 ? 0.6491 0.6347 0.5156 0.0228  0.1369  0.0055  446  ASN B CB  
6541 C CG  . ASN B 351 ? 0.6770 0.6656 0.5511 0.0250  0.1262  0.0067  446  ASN B CG  
6542 O OD1 . ASN B 351 ? 0.6394 0.6267 0.5118 0.0252  0.1235  0.0021  446  ASN B OD1 
6543 N ND2 . ASN B 351 ? 0.6040 0.5961 0.4865 0.0265  0.1206  0.0124  446  ASN B ND2 
6544 N N   . GLU B 352 ? 0.6950 0.6701 0.5301 0.0157  0.1592  -0.0010 447  GLU B N   
6545 C CA  . GLU B 352 ? 0.7568 0.7311 0.5906 0.0142  0.1725  -0.0041 447  GLU B CA  
6546 C C   . GLU B 352 ? 0.7255 0.6951 0.5499 0.0134  0.1789  -0.0131 447  GLU B C   
6547 O O   . GLU B 352 ? 0.7127 0.6840 0.5466 0.0149  0.1894  -0.0181 447  GLU B O   
6548 C CB  . GLU B 352 ? 0.8162 0.7868 0.6341 0.0099  0.1763  0.0016  447  GLU B CB  
6549 C CG  . GLU B 352 ? 0.9183 0.8806 0.7074 0.0054  0.1761  0.0006  447  GLU B CG  
6550 C CD  . GLU B 352 ? 1.0313 0.9891 0.8039 0.0009  0.1823  0.0062  447  GLU B CD  
6551 O OE1 . GLU B 352 ? 1.0451 1.0051 0.8252 0.0000  0.1939  0.0056  447  GLU B OE1 
6552 O OE2 . GLU B 352 ? 1.0918 1.0441 0.8444 -0.0018 0.1754  0.0113  447  GLU B OE2 
6553 N N   . MET B 353 ? 0.7044 0.6684 0.5119 0.0113  0.1726  -0.0157 448  MET B N   
6554 C CA  . MET B 353 ? 0.7420 0.7009 0.5419 0.0105  0.1779  -0.0251 448  MET B CA  
6555 C C   . MET B 353 ? 0.7387 0.7008 0.5609 0.0155  0.1787  -0.0299 448  MET B C   
6556 O O   . MET B 353 ? 0.7087 0.6690 0.5355 0.0168  0.1886  -0.0368 448  MET B O   
6557 C CB  . MET B 353 ? 0.8085 0.7617 0.5870 0.0068  0.1694  -0.0268 448  MET B CB  
6558 C CG  . MET B 353 ? 0.9186 0.8663 0.6919 0.0061  0.1728  -0.0372 448  MET B CG  
6559 S SD  . MET B 353 ? 1.1442 1.0836 0.8844 -0.0006 0.1686  -0.0413 448  MET B SD  
6560 C CE  . MET B 353 ? 0.9789 0.9229 0.7186 -0.0008 0.1508  -0.0326 448  MET B CE  
6561 N N   . LEU B 354 ? 0.6717 0.6381 0.5076 0.0184  0.1685  -0.0261 449  LEU B N   
6562 C CA  . LEU B 354 ? 0.6853 0.6544 0.5419 0.0232  0.1684  -0.0292 449  LEU B CA  
6563 C C   . LEU B 354 ? 0.6389 0.6134 0.5141 0.0269  0.1777  -0.0294 449  LEU B C   
6564 O O   . LEU B 354 ? 0.6520 0.6254 0.5369 0.0299  0.1842  -0.0352 449  LEU B O   
6565 C CB  . LEU B 354 ? 0.6098 0.5835 0.4770 0.0252  0.1563  -0.0238 449  LEU B CB  
6566 C CG  . LEU B 354 ? 0.6443 0.6147 0.4995 0.0225  0.1463  -0.0244 449  LEU B CG  
6567 C CD1 . LEU B 354 ? 0.6549 0.6312 0.5221 0.0246  0.1357  -0.0186 449  LEU B CD1 
6568 C CD2 . LEU B 354 ? 0.6598 0.6240 0.5122 0.0219  0.1483  -0.0327 449  LEU B CD2 
6569 N N   . ILE B 355 ? 0.6393 0.6197 0.5205 0.0267  0.1783  -0.0231 450  ILE B N   
6570 C CA  . ILE B 355 ? 0.6246 0.6117 0.5248 0.0297  0.1863  -0.0229 450  ILE B CA  
6571 C C   . ILE B 355 ? 0.6616 0.6459 0.5562 0.0286  0.1999  -0.0292 450  ILE B C   
6572 O O   . ILE B 355 ? 0.6341 0.6219 0.5453 0.0324  0.2072  -0.0331 450  ILE B O   
6573 C CB  . ILE B 355 ? 0.6485 0.6416 0.5542 0.0286  0.1840  -0.0152 450  ILE B CB  
6574 C CG1 . ILE B 355 ? 0.5906 0.5872 0.5054 0.0307  0.1716  -0.0101 450  ILE B CG1 
6575 C CG2 . ILE B 355 ? 0.6276 0.6281 0.5510 0.0302  0.1935  -0.0156 450  ILE B CG2 
6576 C CD1 . ILE B 355 ? 0.6514 0.6511 0.5667 0.0287  0.1680  -0.0028 450  ILE B CD1 
6577 N N   . LYS B 356 ? 0.6475 0.6254 0.5187 0.0234  0.2035  -0.0301 451  LYS B N   
6578 C CA  . LYS B 356 ? 0.6969 0.6714 0.5604 0.0217  0.2172  -0.0366 451  LYS B CA  
6579 C C   . LYS B 356 ? 0.7119 0.6814 0.5775 0.0244  0.2210  -0.0458 451  LYS B C   
6580 O O   . LYS B 356 ? 0.6696 0.6401 0.5443 0.0267  0.2325  -0.0516 451  LYS B O   
6581 C CB  . LYS B 356 ? 0.6877 0.6554 0.5224 0.0152  0.2189  -0.0352 451  LYS B CB  
6582 C CG  . LYS B 356 ? 0.7791 0.7428 0.6021 0.0125  0.2336  -0.0418 451  LYS B CG  
6583 N N   . THR B 357 ? 0.6620 0.6263 0.5205 0.0242  0.2115  -0.0473 452  THR B N   
6584 C CA  . THR B 357 ? 0.6716 0.6299 0.5328 0.0266  0.2145  -0.0558 452  THR B CA  
6585 C C   . THR B 357 ? 0.6698 0.6338 0.5595 0.0336  0.2162  -0.0561 452  THR B C   
6586 O O   . THR B 357 ? 0.6687 0.6295 0.5658 0.0368  0.2248  -0.0631 452  THR B O   
6587 C CB  . THR B 357 ? 0.7011 0.6533 0.5500 0.0242  0.2033  -0.0567 452  THR B CB  
6588 O OG1 . THR B 357 ? 0.6821 0.6305 0.5055 0.0180  0.2000  -0.0552 452  THR B OG1 
6589 C CG2 . THR B 357 ? 0.6895 0.6333 0.5378 0.0253  0.2071  -0.0661 452  THR B CG2 
6590 N N   . VAL B 358 ? 0.6522 0.6243 0.5579 0.0364  0.2081  -0.0485 453  VAL B N   
6591 C CA  . VAL B 358 ? 0.6351 0.6136 0.5673 0.0430  0.2092  -0.0480 453  VAL B CA  
6592 C C   . VAL B 358 ? 0.6276 0.6120 0.5718 0.0450  0.2216  -0.0501 453  VAL B C   
6593 O O   . VAL B 358 ? 0.6517 0.6370 0.6117 0.0502  0.2279  -0.0546 453  VAL B O   
6594 C CB  . VAL B 358 ? 0.6105 0.5967 0.5553 0.0448  0.1979  -0.0396 453  VAL B CB  
6595 C CG1 . VAL B 358 ? 0.5672 0.5610 0.5387 0.0515  0.1990  -0.0386 453  VAL B CG1 
6596 C CG2 . VAL B 358 ? 0.5926 0.5736 0.5284 0.0434  0.1867  -0.0382 453  VAL B CG2 
6597 N N   . LYS B 359 ? 0.5976 0.5862 0.5353 0.0410  0.2256  -0.0468 454  LYS B N   
6598 C CA  . LYS B 359 ? 0.6415 0.6372 0.5917 0.0422  0.2376  -0.0484 454  LYS B CA  
6599 C C   . LYS B 359 ? 0.6577 0.6472 0.6007 0.0421  0.2510  -0.0577 454  LYS B C   
6600 O O   . LYS B 359 ? 0.6532 0.6489 0.6128 0.0453  0.2614  -0.0609 454  LYS B O   
6601 C CB  . LYS B 359 ? 0.6394 0.6394 0.5822 0.0369  0.2392  -0.0425 454  LYS B CB  
6602 C CG  . LYS B 359 ? 0.6960 0.7012 0.6446 0.0365  0.2268  -0.0338 454  LYS B CG  
6603 C CD  . LYS B 359 ? 0.6759 0.6935 0.6516 0.0400  0.2272  -0.0306 454  LYS B CD  
6604 C CE  . LYS B 359 ? 0.6994 0.7208 0.6837 0.0417  0.2135  -0.0243 454  LYS B CE  
6605 N NZ  . LYS B 359 ? 0.6632 0.6943 0.6611 0.0404  0.2132  -0.0190 454  LYS B NZ  
6606 N N   . GLY B 360 ? 0.6558 0.6338 0.5749 0.0384  0.2511  -0.0626 455  GLY B N   
6607 C CA  . GLY B 360 ? 0.6657 0.6370 0.5773 0.0383  0.2640  -0.0724 455  GLY B CA  
6608 C C   . GLY B 360 ? 0.6815 0.6533 0.6159 0.0459  0.2686  -0.0780 455  GLY B C   
6609 O O   . GLY B 360 ? 0.6925 0.6647 0.6334 0.0480  0.2818  -0.0847 455  GLY B O   
6610 N N   . GLN B 361 ? 0.6197 0.5916 0.5668 0.0502  0.2580  -0.0752 456  GLN B N   
6611 C CA  . GLN B 361 ? 0.6602 0.6322 0.6297 0.0580  0.2611  -0.0790 456  GLN B CA  
6612 C C   . GLN B 361 ? 0.6648 0.6508 0.6634 0.0639  0.2590  -0.0729 456  GLN B C   
6613 O O   . GLN B 361 ? 0.6501 0.6402 0.6691 0.0700  0.2669  -0.0763 456  GLN B O   
6614 C CB  . GLN B 361 ? 0.6265 0.5888 0.5924 0.0594  0.2516  -0.0799 456  GLN B CB  
6615 C CG  . GLN B 361 ? 0.6692 0.6289 0.6561 0.0674  0.2546  -0.0836 456  GLN B CG  
6616 C CD  . GLN B 361 ? 0.7073 0.6540 0.6864 0.0674  0.2485  -0.0866 456  GLN B CD  
6617 O OE1 . GLN B 361 ? 0.6837 0.6267 0.6475 0.0623  0.2387  -0.0837 456  GLN B OE1 
6618 N NE2 . GLN B 361 ? 0.7013 0.6409 0.6918 0.0731  0.2546  -0.0926 456  GLN B NE2 
6619 N N   . TYR B 362 ? 0.6260 0.6194 0.6273 0.0622  0.2486  -0.0640 457  TYR B N   
6620 C CA  . TYR B 362 ? 0.6260 0.6329 0.6532 0.0669  0.2448  -0.0580 457  TYR B CA  
6621 C C   . TYR B 362 ? 0.6430 0.6591 0.6687 0.0620  0.2462  -0.0531 457  TYR B C   
6622 O O   . TYR B 362 ? 0.5864 0.6048 0.6071 0.0590  0.2361  -0.0463 457  TYR B O   
6623 C CB  . TYR B 362 ? 0.6124 0.6192 0.6455 0.0695  0.2305  -0.0521 457  TYR B CB  
6624 C CG  . TYR B 362 ? 0.6433 0.6390 0.6746 0.0730  0.2282  -0.0561 457  TYR B CG  
6625 C CD1 . TYR B 362 ? 0.6065 0.5927 0.6199 0.0692  0.2199  -0.0555 457  TYR B CD1 
6626 C CD2 . TYR B 362 ? 0.5984 0.5930 0.6469 0.0799  0.2346  -0.0605 457  TYR B CD2 
6627 C CE1 . TYR B 362 ? 0.6339 0.6094 0.6461 0.0717  0.2181  -0.0591 457  TYR B CE1 
6628 C CE2 . TYR B 362 ? 0.6379 0.6208 0.6848 0.0830  0.2328  -0.0639 457  TYR B CE2 
6629 C CZ  . TYR B 362 ? 0.6289 0.6022 0.6573 0.0784  0.2246  -0.0632 457  TYR B CZ  
6630 O OH  . TYR B 362 ? 0.6952 0.6565 0.7219 0.0805  0.2230  -0.0666 457  TYR B OH  
6631 N N   . PRO B 363 ? 0.6420 0.6632 0.6724 0.0610  0.2589  -0.0565 458  PRO B N   
6632 C CA  . PRO B 363 ? 0.6494 0.6777 0.6764 0.0554  0.2613  -0.0519 458  PRO B CA  
6633 C C   . PRO B 363 ? 0.6278 0.6693 0.6774 0.0575  0.2538  -0.0449 458  PRO B C   
6634 O O   . PRO B 363 ? 0.6070 0.6561 0.6805 0.0640  0.2518  -0.0450 458  PRO B O   
6635 C CB  . PRO B 363 ? 0.6491 0.6799 0.6787 0.0545  0.2782  -0.0581 458  PRO B CB  
6636 C CG  . PRO B 363 ? 0.6649 0.6954 0.7112 0.0621  0.2828  -0.0647 458  PRO B CG  
6637 C CD  . PRO B 363 ? 0.6683 0.6882 0.7065 0.0647  0.2725  -0.0649 458  PRO B CD  
6638 N N   . CYS B 364 ? 0.5745 0.6181 0.6155 0.0518  0.2495  -0.0389 459  CYS B N   
6639 C CA  . CYS B 364 ? 0.5840 0.6392 0.6434 0.0523  0.2427  -0.0327 459  CYS B CA  
6640 C C   . CYS B 364 ? 0.6232 0.6773 0.6683 0.0447  0.2420  -0.0275 459  CYS B C   
6641 O O   . CYS B 364 ? 0.6157 0.6591 0.6359 0.0406  0.2392  -0.0262 459  CYS B O   
6642 C CB  . CYS B 364 ? 0.6203 0.6757 0.6864 0.0565  0.2283  -0.0290 459  CYS B CB  
6643 S SG  . CYS B 364 ? 0.6541 0.7247 0.7450 0.0577  0.2200  -0.0227 459  CYS B SG  
6644 N N   . GLU B 365 ? 0.5830 0.6483 0.6445 0.0430  0.2446  -0.0247 460  GLU B N   
6645 C CA  . GLU B 365 ? 0.6210 0.6860 0.6735 0.0362  0.2434  -0.0190 460  GLU B CA  
6646 C C   . GLU B 365 ? 0.6184 0.6760 0.6566 0.0350  0.2296  -0.0136 460  GLU B C   
6647 O O   . GLU B 365 ? 0.5656 0.6247 0.6118 0.0395  0.2193  -0.0128 460  GLU B O   
6648 C CB  . GLU B 365 ? 0.6563 0.7359 0.7350 0.0360  0.2448  -0.0170 460  GLU B CB  
6649 C CG  . GLU B 365 ? 0.8062 0.8870 0.8812 0.0287  0.2468  -0.0120 460  GLU B CG  
6650 C CD  . GLU B 365 ? 0.8501 0.9458 0.9531 0.0290  0.2440  -0.0102 460  GLU B CD  
6651 O OE1 . GLU B 365 ? 0.8732 0.9773 0.9956 0.0352  0.2377  -0.0117 460  GLU B OE1 
6652 O OE2 . GLU B 365 ? 0.8326 0.9311 0.9376 0.0229  0.2478  -0.0071 460  GLU B OE2 
6653 N N   . ASP B 366 ? 0.6470 0.6966 0.6639 0.0290  0.2296  -0.0099 461  ASP B N   
6654 C CA  . ASP B 366 ? 0.6329 0.6763 0.6375 0.0277  0.2172  -0.0045 461  ASP B CA  
6655 C C   . ASP B 366 ? 0.5913 0.6433 0.6155 0.0295  0.2083  -0.0008 461  ASP B C   
6656 O O   . ASP B 366 ? 0.5172 0.5785 0.5587 0.0283  0.2123  -0.0001 461  ASP B O   
6657 C CB  . ASP B 366 ? 0.6746 0.7099 0.6579 0.0211  0.2194  0.0001  461  ASP B CB  
6658 C CG  . ASP B 366 ? 0.7799 0.8048 0.7381 0.0188  0.2249  -0.0026 461  ASP B CG  
6659 O OD1 . ASP B 366 ? 0.8254 0.8485 0.7821 0.0222  0.2267  -0.0086 461  ASP B OD1 
6660 O OD2 . ASP B 366 ? 0.7645 0.7825 0.7039 0.0134  0.2272  0.0013  461  ASP B OD2 
6661 N N   . PHE B 367 ? 0.5524 0.6015 0.5735 0.0320  0.1964  0.0012  462  PHE B N   
6662 C CA  . PHE B 367 ? 0.5299 0.5855 0.5655 0.0332  0.1874  0.0046  462  PHE B CA  
6663 C C   . PHE B 367 ? 0.5142 0.5680 0.5448 0.0276  0.1870  0.0097  462  PHE B C   
6664 O O   . PHE B 367 ? 0.4875 0.5316 0.4979 0.0243  0.1865  0.0125  462  PHE B O   
6665 C CB  . PHE B 367 ? 0.4935 0.5451 0.5241 0.0365  0.1758  0.0055  462  PHE B CB  
6666 C CG  . PHE B 367 ? 0.4978 0.5565 0.5434 0.0383  0.1670  0.0081  462  PHE B CG  
6667 C CD1 . PHE B 367 ? 0.4915 0.5596 0.5570 0.0427  0.1655  0.0061  462  PHE B CD1 
6668 C CD2 . PHE B 367 ? 0.4742 0.5301 0.5140 0.0356  0.1601  0.0123  462  PHE B CD2 
6669 C CE1 . PHE B 367 ? 0.4591 0.5338 0.5369 0.0439  0.1572  0.0082  462  PHE B CE1 
6670 C CE2 . PHE B 367 ? 0.4807 0.5427 0.5333 0.0369  0.1525  0.0139  462  PHE B CE2 
6671 C CZ  . PHE B 367 ? 0.4672 0.5388 0.5382 0.0408  0.1509  0.0118  462  PHE B CZ  
6672 N N   . GLN B 368 ? 0.4787 0.5417 0.5279 0.0266  0.1868  0.0109  463  GLN B N   
6673 C CA  . GLN B 368 ? 0.4934 0.5552 0.5414 0.0209  0.1877  0.0152  463  GLN B CA  
6674 C C   . GLN B 368 ? 0.5012 0.5668 0.5599 0.0216  0.1773  0.0174  463  GLN B C   
6675 O O   . GLN B 368 ? 0.4301 0.5047 0.5052 0.0255  0.1725  0.0152  463  GLN B O   
6676 C CB  . GLN B 368 ? 0.4962 0.5656 0.5570 0.0174  0.1991  0.0138  463  GLN B CB  
6677 C CG  . GLN B 368 ? 0.5395 0.6034 0.5863 0.0150  0.2107  0.0122  463  GLN B CG  
6678 C CD  . GLN B 368 ? 0.5897 0.6633 0.6526 0.0124  0.2226  0.0099  463  GLN B CD  
6679 O OE1 . GLN B 368 ? 0.5746 0.6508 0.6440 0.0072  0.2256  0.0127  463  GLN B OE1 
6680 N NE2 . GLN B 368 ? 0.5911 0.6702 0.6621 0.0161  0.2295  0.0044  463  GLN B NE2 
6681 N N   . TRP B 369 ? 0.4558 0.5139 0.5043 0.0179  0.1738  0.0219  464  TRP B N   
6682 C CA  . TRP B 369 ? 0.4815 0.5414 0.5381 0.0176  0.1650  0.0239  464  TRP B CA  
6683 C C   . TRP B 369 ? 0.4951 0.5479 0.5450 0.0117  0.1674  0.0284  464  TRP B C   
6684 O O   . TRP B 369 ? 0.4607 0.5043 0.4938 0.0089  0.1724  0.0312  464  TRP B O   
6685 C CB  . TRP B 369 ? 0.4947 0.5505 0.5437 0.0220  0.1543  0.0243  464  TRP B CB  
6686 C CG  . TRP B 369 ? 0.5149 0.5584 0.5425 0.0211  0.1515  0.0278  464  TRP B CG  
6687 C CD1 . TRP B 369 ? 0.4981 0.5354 0.5198 0.0201  0.1451  0.0314  464  TRP B CD1 
6688 C CD2 . TRP B 369 ? 0.5134 0.5497 0.5232 0.0214  0.1548  0.0278  464  TRP B CD2 
6689 N NE1 . TRP B 369 ? 0.4823 0.5098 0.4847 0.0201  0.1437  0.0342  464  TRP B NE1 
6690 C CE2 . TRP B 369 ? 0.5443 0.5710 0.5384 0.0205  0.1493  0.0320  464  TRP B CE2 
6691 C CE3 . TRP B 369 ? 0.4997 0.5367 0.5055 0.0224  0.1616  0.0243  464  TRP B CE3 
6692 C CZ2 . TRP B 369 ? 0.4952 0.5139 0.4696 0.0203  0.1498  0.0331  464  TRP B CZ2 
6693 C CZ3 . TRP B 369 ? 0.5201 0.5481 0.5052 0.0218  0.1626  0.0248  464  TRP B CZ3 
6694 C CH2 . TRP B 369 ? 0.5016 0.5210 0.4712 0.0206  0.1563  0.0293  464  TRP B CH2 
6695 N N   . LEU B 370 ? 0.4514 0.5084 0.5145 0.0096  0.1638  0.0289  465  LEU B N   
6696 C CA  . LEU B 370 ? 0.5283 0.5787 0.5884 0.0037  0.1663  0.0329  465  LEU B CA  
6697 C C   . LEU B 370 ? 0.5322 0.5714 0.5791 0.0046  0.1581  0.0367  465  LEU B C   
6698 O O   . LEU B 370 ? 0.5036 0.5431 0.5488 0.0093  0.1496  0.0355  465  LEU B O   
6699 C CB  . LEU B 370 ? 0.5198 0.5798 0.6014 0.0003  0.1667  0.0310  465  LEU B CB  
6700 C CG  . LEU B 370 ? 0.5117 0.5859 0.6122 -0.0001 0.1733  0.0268  465  LEU B CG  
6701 C CD1 . LEU B 370 ? 0.4569 0.5404 0.5782 -0.0040 0.1714  0.0252  465  LEU B CD1 
6702 C CD2 . LEU B 370 ? 0.4713 0.5428 0.5650 -0.0036 0.1856  0.0279  465  LEU B CD2 
6703 N N   . GLU B 371 ? 0.5705 0.5999 0.6092 -0.0001 0.1610  0.0414  466  GLU B N   
6704 C CA  . GLU B 371 ? 0.5596 0.5781 0.5881 0.0006  0.1538  0.0454  466  GLU B CA  
6705 C C   . GLU B 371 ? 0.5849 0.6079 0.6272 0.0020  0.1459  0.0427  466  GLU B C   
6706 O O   . GLU B 371 ? 0.5204 0.5385 0.5570 0.0055  0.1380  0.0435  466  GLU B O   
6707 C CB  . GLU B 371 ? 0.5587 0.5657 0.5778 -0.0049 0.1593  0.0513  466  GLU B CB  
6708 C CG  . GLU B 371 ? 0.5981 0.5916 0.6017 -0.0032 0.1529  0.0567  466  GLU B CG  
6709 C CD  . GLU B 371 ? 0.6767 0.6680 0.6899 -0.0027 0.1460  0.0564  466  GLU B CD  
6710 O OE1 . GLU B 371 ? 0.6780 0.6743 0.7068 -0.0065 0.1484  0.0539  466  GLU B OE1 
6711 O OE2 . GLU B 371 ? 0.7136 0.6986 0.7192 0.0014  0.1383  0.0583  466  GLU B OE2 
6712 N N   . GLU B 372 ? 0.5353 0.5682 0.5960 -0.0006 0.1478  0.0391  467  GLU B N   
6713 C CA  . GLU B 372 ? 0.5437 0.5824 0.6176 0.0003  0.1404  0.0357  467  GLU B CA  
6714 C C   . GLU B 372 ? 0.5191 0.5731 0.6079 0.0027  0.1396  0.0306  467  GLU B C   
6715 O O   . GLU B 372 ? 0.4824 0.5446 0.5828 -0.0002 0.1461  0.0290  467  GLU B O   
6716 C CB  . GLU B 372 ? 0.5758 0.6115 0.6583 -0.0059 0.1424  0.0363  467  GLU B CB  
6717 C CG  . GLU B 372 ? 0.6294 0.6687 0.7226 -0.0056 0.1346  0.0326  467  GLU B CG  
6718 C CD  . GLU B 372 ? 0.8202 0.8472 0.9023 -0.0034 0.1285  0.0348  467  GLU B CD  
6719 O OE1 . GLU B 372 ? 0.8127 0.8398 0.8878 0.0024  0.1226  0.0342  467  GLU B OE1 
6720 O OE2 . GLU B 372 ? 0.9482 0.9653 1.0293 -0.0075 0.1301  0.0371  467  GLU B OE2 
6721 N N   . THR B 373 ? 0.4636 0.5214 0.5527 0.0080  0.1318  0.0283  468  THR B N   
6722 C CA  . THR B 373 ? 0.4711 0.5417 0.5720 0.0114  0.1304  0.0244  468  THR B CA  
6723 C C   . THR B 373 ? 0.4852 0.5668 0.6055 0.0083  0.1289  0.0212  468  THR B C   
6724 O O   . THR B 373 ? 0.4738 0.5536 0.5966 0.0064  0.1236  0.0204  468  THR B O   
6725 C CB  . THR B 373 ? 0.4468 0.5172 0.5417 0.0173  0.1223  0.0235  468  THR B CB  
6726 O OG1 . THR B 373 ? 0.4325 0.4929 0.5099 0.0196  0.1228  0.0262  468  THR B OG1 
6727 C CG2 . THR B 373 ? 0.4147 0.4967 0.5203 0.0213  0.1212  0.0205  468  THR B CG2 
6728 N N   . PRO B 374 ? 0.4537 0.5472 0.5885 0.0079  0.1332  0.0191  469  PRO B N   
6729 C CA  . PRO B 374 ? 0.4474 0.5533 0.6017 0.0055  0.1300  0.0157  469  PRO B CA  
6730 C C   . PRO B 374 ? 0.4743 0.5857 0.6315 0.0100  0.1196  0.0135  469  PRO B C   
6731 O O   . PRO B 374 ? 0.4210 0.5327 0.5724 0.0160  0.1167  0.0137  469  PRO B O   
6732 C CB  . PRO B 374 ? 0.4798 0.5974 0.6484 0.0054  0.1373  0.0142  469  PRO B CB  
6733 C CG  . PRO B 374 ? 0.4446 0.5531 0.5996 0.0050  0.1467  0.0170  469  PRO B CG  
6734 C CD  . PRO B 374 ? 0.4145 0.5106 0.5491 0.0092  0.1416  0.0193  469  PRO B CD  
6735 N N   . ILE B 375 ? 0.4769 0.5922 0.6424 0.0067  0.1141  0.0112  470  ILE B N   
6736 C CA  . ILE B 375 ? 0.4336 0.5547 0.6019 0.0098  0.1041  0.0088  470  ILE B CA  
6737 C C   . ILE B 375 ? 0.4529 0.5890 0.6414 0.0068  0.1015  0.0054  470  ILE B C   
6738 O O   . ILE B 375 ? 0.4769 0.6140 0.6735 0.0002  0.1037  0.0038  470  ILE B O   
6739 C CB  . ILE B 375 ? 0.4649 0.5754 0.6215 0.0087  0.0988  0.0085  470  ILE B CB  
6740 C CG1 . ILE B 375 ? 0.4723 0.5694 0.6103 0.0120  0.1006  0.0120  470  ILE B CG1 
6741 C CG2 . ILE B 375 ? 0.4476 0.5644 0.6063 0.0112  0.0893  0.0057  470  ILE B CG2 
6742 C CD1 . ILE B 375 ? 0.5094 0.5961 0.6368 0.0118  0.0959  0.0118  470  ILE B CD1 
6743 N N   . PHE B 376 ? 0.4096 0.5573 0.6067 0.0116  0.0967  0.0043  471  PHE B N   
6744 C CA  . PHE B 376 ? 0.4505 0.6142 0.6672 0.0098  0.0922  0.0013  471  PHE B CA  
6745 C C   . PHE B 376 ? 0.4518 0.6190 0.6657 0.0125  0.0810  -0.0002 471  PHE B C   
6746 O O   . PHE B 376 ? 0.4472 0.6087 0.6484 0.0181  0.0777  0.0017  471  PHE B O   
6747 C CB  . PHE B 376 ? 0.4179 0.5940 0.6496 0.0134  0.0962  0.0017  471  PHE B CB  
6748 C CG  . PHE B 376 ? 0.4448 0.6171 0.6768 0.0116  0.1082  0.0031  471  PHE B CG  
6749 C CD1 . PHE B 376 ? 0.4339 0.6094 0.6766 0.0042  0.1147  0.0019  471  PHE B CD1 
6750 C CD2 . PHE B 376 ? 0.4071 0.5722 0.6280 0.0167  0.1134  0.0054  471  PHE B CD2 
6751 C CE1 . PHE B 376 ? 0.4623 0.6338 0.7037 0.0021  0.1264  0.0034  471  PHE B CE1 
6752 C CE2 . PHE B 376 ? 0.4252 0.5865 0.6445 0.0147  0.1246  0.0064  471  PHE B CE2 
6753 C CZ  . PHE B 376 ? 0.4215 0.5860 0.6506 0.0075  0.1313  0.0056  471  PHE B CZ  
6754 N N   . THR B 377 ? 0.4147 0.5911 0.6398 0.0082  0.0750  -0.0036 472  THR B N   
6755 C CA  . THR B 377 ? 0.4282 0.6109 0.6523 0.0114  0.0643  -0.0048 472  THR B CA  
6756 C C   . THR B 377 ? 0.4290 0.6252 0.6656 0.0173  0.0619  -0.0032 472  THR B C   
6757 O O   . THR B 377 ? 0.4402 0.6441 0.6912 0.0175  0.0679  -0.0028 472  THR B O   
6758 C CB  . THR B 377 ? 0.4475 0.6363 0.6786 0.0049  0.0577  -0.0095 472  THR B CB  
6759 O OG1 . THR B 377 ? 0.4524 0.6561 0.7056 0.0012  0.0587  -0.0114 472  THR B OG1 
6760 C CG2 . THR B 377 ? 0.4670 0.6415 0.6872 -0.0010 0.0607  -0.0114 472  THR B CG2 
6761 N N   . TYR B 378 ? 0.4403 0.6388 0.6713 0.0224  0.0534  -0.0021 473  TYR B N   
6762 C CA  . TYR B 378 ? 0.4153 0.6261 0.6584 0.0286  0.0498  -0.0001 473  TYR B CA  
6763 C C   . TYR B 378 ? 0.4432 0.6717 0.7100 0.0253  0.0474  -0.0027 473  TYR B C   
6764 O O   . TYR B 378 ? 0.4062 0.6450 0.6894 0.0288  0.0506  -0.0017 473  TYR B O   
6765 C CB  . TYR B 378 ? 0.4109 0.6208 0.6432 0.0333  0.0400  0.0016  473  TYR B CB  
6766 C CG  . TYR B 378 ? 0.4582 0.6777 0.7000 0.0407  0.0360  0.0048  473  TYR B CG  
6767 C CD1 . TYR B 378 ? 0.4525 0.6652 0.6896 0.0472  0.0412  0.0084  473  TYR B CD1 
6768 C CD2 . TYR B 378 ? 0.4275 0.6623 0.6829 0.0413  0.0264  0.0043  473  TYR B CD2 
6769 C CE1 . TYR B 378 ? 0.4671 0.6870 0.7130 0.0544  0.0377  0.0115  473  TYR B CE1 
6770 C CE2 . TYR B 378 ? 0.4591 0.7020 0.7233 0.0488  0.0222  0.0080  473  TYR B CE2 
6771 C CZ  . TYR B 378 ? 0.4546 0.6894 0.7143 0.0555  0.0282  0.0116  473  TYR B CZ  
6772 O OH  . TYR B 378 ? 0.4635 0.7050 0.7324 0.0633  0.0243  0.0154  473  TYR B OH  
6773 N N   . GLU B 379 ? 0.4129 0.6453 0.6826 0.0185  0.0422  -0.0066 474  GLU B N   
6774 C CA  . GLU B 379 ? 0.4624 0.7125 0.7554 0.0144  0.0392  -0.0097 474  GLU B CA  
6775 C C   . GLU B 379 ? 0.4311 0.6845 0.7390 0.0111  0.0507  -0.0103 474  GLU B C   
6776 O O   . GLU B 379 ? 0.4267 0.6961 0.7565 0.0123  0.0513  -0.0107 474  GLU B O   
6777 C CB  . GLU B 379 ? 0.4366 0.6883 0.7280 0.0067  0.0320  -0.0145 474  GLU B CB  
6778 C CG  . GLU B 379 ? 0.5404 0.8104 0.8565 0.0008  0.0290  -0.0185 474  GLU B CG  
6779 C CD  . GLU B 379 ? 0.6318 0.9007 0.9456 -0.0083 0.0239  -0.0242 474  GLU B CD  
6780 O OE1 . GLU B 379 ? 0.6316 0.8847 0.9248 -0.0099 0.0237  -0.0252 474  GLU B OE1 
6781 O OE2 . GLU B 379 ? 0.6566 0.9405 0.9898 -0.0139 0.0201  -0.0281 474  GLU B OE2 
6782 N N   . GLU B 380 ? 0.4133 0.6518 0.7095 0.0071  0.0600  -0.0101 475  GLU B N   
6783 C CA  . GLU B 380 ? 0.4171 0.6566 0.7238 0.0039  0.0720  -0.0100 475  GLU B CA  
6784 C C   . GLU B 380 ? 0.4101 0.6533 0.7222 0.0115  0.0777  -0.0070 475  GLU B C   
6785 O O   . GLU B 380 ? 0.4159 0.6706 0.7472 0.0107  0.0840  -0.0078 475  GLU B O   
6786 C CB  . GLU B 380 ? 0.4432 0.6639 0.7327 -0.0008 0.0801  -0.0092 475  GLU B CB  
6787 C CG  . GLU B 380 ? 0.4920 0.7089 0.7820 -0.0101 0.0790  -0.0127 475  GLU B CG  
6788 C CD  . GLU B 380 ? 0.5230 0.7187 0.7907 -0.0119 0.0828  -0.0111 475  GLU B CD  
6789 O OE1 . GLU B 380 ? 0.5470 0.7320 0.7994 -0.0064 0.0864  -0.0074 475  GLU B OE1 
6790 O OE2 . GLU B 380 ? 0.6123 0.8019 0.8782 -0.0189 0.0820  -0.0138 475  GLU B OE2 
6791 N N   . ALA B 381 ? 0.4107 0.6439 0.7061 0.0187  0.0765  -0.0038 476  ALA B N   
6792 C CA  . ALA B 381 ? 0.4601 0.6947 0.7591 0.0260  0.0821  -0.0014 476  ALA B CA  
6793 C C   . ALA B 381 ? 0.4203 0.6743 0.7430 0.0304  0.0773  -0.0019 476  ALA B C   
6794 O O   . ALA B 381 ? 0.4476 0.7100 0.7863 0.0324  0.0849  -0.0023 476  ALA B O   
6795 C CB  . ALA B 381 ? 0.3867 0.6072 0.6638 0.0323  0.0799  0.0017  476  ALA B CB  
6796 N N   . ILE B 382 ? 0.4317 0.6935 0.7573 0.0318  0.0647  -0.0021 477  ILE B N   
6797 C CA  . ILE B 382 ? 0.4292 0.7102 0.7776 0.0362  0.0582  -0.0020 477  ILE B CA  
6798 C C   . ILE B 382 ? 0.4407 0.7378 0.8143 0.0301  0.0623  -0.0056 477  ILE B C   
6799 O O   . ILE B 382 ? 0.3950 0.7062 0.7905 0.0340  0.0650  -0.0057 477  ILE B O   
6800 C CB  . ILE B 382 ? 0.4245 0.7100 0.7683 0.0378  0.0432  -0.0013 477  ILE B CB  
6801 C CG1 . ILE B 382 ? 0.4261 0.6963 0.7462 0.0441  0.0402  0.0026  477  ILE B CG1 
6802 C CG2 . ILE B 382 ? 0.4044 0.7105 0.7724 0.0422  0.0355  -0.0009 477  ILE B CG2 
6803 C CD1 . ILE B 382 ? 0.4483 0.7153 0.7702 0.0526  0.0462  0.0060  477  ILE B CD1 
6804 N N   . LYS B 383 ? 0.4267 0.7218 0.7987 0.0204  0.0630  -0.0089 478  LYS B N   
6805 C CA  . LYS B 383 ? 0.4299 0.7402 0.8263 0.0137  0.0670  -0.0124 478  LYS B CA  
6806 C C   . LYS B 383 ? 0.4497 0.7584 0.8532 0.0133  0.0826  -0.0121 478  LYS B C   
6807 O O   . LYS B 383 ? 0.4424 0.7674 0.8710 0.0114  0.0871  -0.0142 478  LYS B O   
6808 C CB  . LYS B 383 ? 0.4554 0.7621 0.8475 0.0031  0.0644  -0.0160 478  LYS B CB  
6809 C CG  . LYS B 383 ? 0.4738 0.7864 0.8638 0.0023  0.0491  -0.0178 478  LYS B CG  
6810 C CD  . LYS B 383 ? 0.5695 0.8802 0.9592 -0.0089 0.0473  -0.0226 478  LYS B CD  
6811 C CE  . LYS B 383 ? 0.6180 0.9365 1.0068 -0.0102 0.0319  -0.0254 478  LYS B CE  
6812 N NZ  . LYS B 383 ? 0.6506 0.9687 1.0418 -0.0216 0.0300  -0.0312 478  LYS B NZ  
6813 N N   . MET B 384 ? 0.4406 0.7304 0.8222 0.0149  0.0909  -0.0097 479  MET B N   
6814 C CA  . MET B 384 ? 0.4785 0.7660 0.8637 0.0159  0.1053  -0.0091 479  MET B CA  
6815 C C   . MET B 384 ? 0.4286 0.7288 0.8309 0.0251  0.1059  -0.0085 479  MET B C   
6816 O O   . MET B 384 ? 0.4558 0.7674 0.8781 0.0246  0.1149  -0.0102 479  MET B O   
6817 C CB  . MET B 384 ? 0.4471 0.7120 0.8036 0.0169  0.1118  -0.0064 479  MET B CB  
6818 C CG  . MET B 384 ? 0.5076 0.7594 0.8496 0.0079  0.1146  -0.0067 479  MET B CG  
6819 S SD  . MET B 384 ? 0.6105 0.8369 0.9183 0.0104  0.1176  -0.0031 479  MET B SD  
6820 C CE  . MET B 384 ? 0.4459 0.6700 0.7538 0.0135  0.1322  -0.0020 479  MET B CE  
6821 N N   . LEU B 385 ? 0.4278 0.7253 0.8222 0.0336  0.0971  -0.0060 480  LEU B N   
6822 C CA  . LEU B 385 ? 0.4573 0.7654 0.8679 0.0431  0.0971  -0.0050 480  LEU B CA  
6823 C C   . LEU B 385 ? 0.4588 0.7915 0.9016 0.0429  0.0921  -0.0071 480  LEU B C   
6824 O O   . LEU B 385 ? 0.4692 0.8140 0.9333 0.0478  0.0977  -0.0079 480  LEU B O   
6825 C CB  . LEU B 385 ? 0.4429 0.7429 0.8389 0.0516  0.0874  -0.0014 480  LEU B CB  
6826 C CG  . LEU B 385 ? 0.4612 0.7398 0.8308 0.0545  0.0934  0.0007  480  LEU B CG  
6827 C CD1 . LEU B 385 ? 0.4678 0.7380 0.8206 0.0594  0.0820  0.0041  480  LEU B CD1 
6828 C CD2 . LEU B 385 ? 0.4703 0.7486 0.8472 0.0608  0.1042  0.0005  480  LEU B CD2 
6829 N N   . ILE B 386 ? 0.4497 0.7904 0.8970 0.0373  0.0814  -0.0085 481  ILE B N   
6830 C CA  . ILE B 386 ? 0.4598 0.8249 0.9381 0.0358  0.0758  -0.0109 481  ILE B CA  
6831 C C   . ILE B 386 ? 0.4694 0.8435 0.9669 0.0288  0.0890  -0.0145 481  ILE B C   
6832 O O   . ILE B 386 ? 0.4215 0.8147 0.9475 0.0315  0.0917  -0.0160 481  ILE B O   
6833 C CB  . ILE B 386 ? 0.4424 0.8127 0.9186 0.0302  0.0613  -0.0123 481  ILE B CB  
6834 C CG1 . ILE B 386 ? 0.4365 0.8001 0.8956 0.0376  0.0483  -0.0085 481  ILE B CG1 
6835 C CG2 . ILE B 386 ? 0.4018 0.7983 0.9110 0.0270  0.0558  -0.0155 481  ILE B CG2 
6836 C CD1 . ILE B 386 ? 0.4960 0.8606 0.9463 0.0317  0.0351  -0.0101 481  ILE B CD1 
6837 N N   . GLN B 387 ? 0.4380 0.7986 0.9205 0.0198  0.0976  -0.0158 482  GLN B N   
6838 C CA  . GLN B 387 ? 0.4682 0.8357 0.9666 0.0119  0.1105  -0.0187 482  GLN B CA  
6839 C C   . GLN B 387 ? 0.4849 0.8551 0.9928 0.0175  0.1241  -0.0185 482  GLN B C   
6840 O O   . GLN B 387 ? 0.4805 0.8658 1.0129 0.0142  0.1328  -0.0213 482  GLN B O   
6841 C CB  . GLN B 387 ? 0.5151 0.8637 0.9913 0.0022  0.1169  -0.0188 482  GLN B CB  
6842 C CG  . GLN B 387 ? 0.6125 0.9656 1.1020 -0.0072 0.1307  -0.0212 482  GLN B CG  
6843 C CD  . GLN B 387 ? 0.7404 1.0710 1.2042 -0.0147 0.1386  -0.0197 482  GLN B CD  
6844 O OE1 . GLN B 387 ? 0.8370 1.1520 1.2778 -0.0152 0.1313  -0.0182 482  GLN B OE1 
6845 N NE2 . GLN B 387 ? 0.7619 1.0907 1.2295 -0.0203 0.1538  -0.0200 482  GLN B NE2 
6846 N N   . HIS B 388 ? 0.5033 0.8591 0.9925 0.0258  0.1266  -0.0156 483  HIS B N   
6847 C CA  . HIS B 388 ? 0.4862 0.8427 0.9819 0.0317  0.1395  -0.0160 483  HIS B CA  
6848 C C   . HIS B 388 ? 0.4506 0.8233 0.9694 0.0425  0.1342  -0.0159 483  HIS B C   
6849 O O   . HIS B 388 ? 0.4557 0.8269 0.9780 0.0494  0.1435  -0.0161 483  HIS B O   
6850 C CB  . HIS B 388 ? 0.4907 0.8225 0.9539 0.0344  0.1456  -0.0135 483  HIS B CB  
6851 C CG  . HIS B 388 ? 0.4964 0.8138 0.9414 0.0247  0.1559  -0.0137 483  HIS B CG  
6852 N ND1 . HIS B 388 ? 0.4852 0.8000 0.9307 0.0220  0.1723  -0.0150 483  HIS B ND1 
6853 C CD2 . HIS B 388 ? 0.5212 0.8262 0.9476 0.0171  0.1522  -0.0125 483  HIS B CD2 
6854 C CE1 . HIS B 388 ? 0.5148 0.8158 0.9418 0.0132  0.1777  -0.0140 483  HIS B CE1 
6855 N NE2 . HIS B 388 ? 0.5418 0.8365 0.9576 0.0104  0.1657  -0.0125 483  HIS B NE2 
6856 N N   . GLY B 389 ? 0.4591 0.8469 0.9935 0.0444  0.1194  -0.0155 484  GLY B N   
6857 C CA  . GLY B 389 ? 0.4359 0.8404 0.9942 0.0548  0.1130  -0.0147 484  GLY B CA  
6858 C C   . GLY B 389 ? 0.4933 0.8854 1.0360 0.0661  0.1075  -0.0106 484  GLY B C   
6859 O O   . GLY B 389 ? 0.4405 0.8436 1.0022 0.0759  0.1046  -0.0096 484  GLY B O   
6860 N N   . LYS B 390 ? 0.4705 0.8401 0.9801 0.0652  0.1060  -0.0082 485  LYS B N   
6861 C CA  . LYS B 390 ? 0.4777 0.8341 0.9712 0.0750  0.1016  -0.0044 485  LYS B CA  
6862 C C   . LYS B 390 ? 0.5272 0.8875 1.0187 0.0790  0.0835  -0.0007 485  LYS B C   
6863 O O   . LYS B 390 ? 0.5149 0.8684 0.9995 0.0882  0.0784  0.0030  485  LYS B O   
6864 C CB  . LYS B 390 ? 0.4653 0.7963 0.9246 0.0721  0.1083  -0.0035 485  LYS B CB  
6865 C CG  . LYS B 390 ? 0.4804 0.8052 0.9370 0.0678  0.1260  -0.0066 485  LYS B CG  
6866 C CD  . LYS B 390 ? 0.5172 0.8483 0.9913 0.0761  0.1355  -0.0082 485  LYS B CD  
6867 C CE  . LYS B 390 ? 0.5344 0.8626 1.0087 0.0711  0.1536  -0.0119 485  LYS B CE  
6868 N NZ  . LYS B 390 ? 0.5461 0.8796 1.0367 0.0796  0.1635  -0.0142 485  LYS B NZ  
6869 N N   . LEU B 391 ? 0.5178 0.8885 1.0147 0.0721  0.0739  -0.0018 486  LEU B N   
6870 C CA  . LEU B 391 ? 0.5020 0.8746 0.9918 0.0738  0.0568  0.0012  486  LEU B CA  
6871 C C   . LEU B 391 ? 0.5209 0.9161 1.0346 0.0683  0.0482  -0.0015 486  LEU B C   
6872 O O   . LEU B 391 ? 0.5145 0.9161 1.0381 0.0593  0.0551  -0.0058 486  LEU B O   
6873 C CB  . LEU B 391 ? 0.5101 0.8620 0.9659 0.0686  0.0541  0.0022  486  LEU B CB  
6874 C CG  . LEU B 391 ? 0.5273 0.8656 0.9604 0.0748  0.0447  0.0071  486  LEU B CG  
6875 C CD1 . LEU B 391 ? 0.5310 0.8623 0.9635 0.0854  0.0494  0.0104  486  LEU B CD1 
6876 C CD2 . LEU B 391 ? 0.5115 0.8299 0.9138 0.0683  0.0465  0.0067  486  LEU B CD2 
6877 N N   . HIS B 392 ? 0.5285 0.9357 1.0515 0.0737  0.0331  0.0013  487  HIS B N   
6878 C CA  . HIS B 392 ? 0.5410 0.9697 1.0843 0.0685  0.0221  -0.0012 487  HIS B CA  
6879 C C   . HIS B 392 ? 0.5619 0.9853 1.0848 0.0675  0.0061  0.0013  487  HIS B C   
6880 O O   . HIS B 392 ? 0.5762 0.9978 1.0932 0.0764  -0.0035 0.0065  487  HIS B O   
6881 C CB  . HIS B 392 ? 0.5647 1.0174 1.1438 0.0761  0.0189  -0.0006 487  HIS B CB  
6882 C CG  . HIS B 392 ? 0.5929 1.0501 1.1911 0.0776  0.0358  -0.0033 487  HIS B CG  
6883 N ND1 . HIS B 392 ? 0.6071 1.0515 1.1987 0.0862  0.0460  -0.0010 487  HIS B ND1 
6884 C CD2 . HIS B 392 ? 0.5915 1.0632 1.2133 0.0708  0.0453  -0.0084 487  HIS B CD2 
6885 C CE1 . HIS B 392 ? 0.5729 1.0241 1.1831 0.0850  0.0609  -0.0048 487  HIS B CE1 
6886 N NE2 . HIS B 392 ? 0.6026 1.0706 1.2314 0.0757  0.0610  -0.0091 487  HIS B NE2 
6887 N N   . LEU B 393 ? 0.5236 0.9427 1.0342 0.0566  0.0041  -0.0025 488  LEU B N   
6888 C CA  . LEU B 393 ? 0.5199 0.9312 1.0074 0.0541  -0.0088 -0.0014 488  LEU B CA  
6889 C C   . LEU B 393 ? 0.5163 0.9379 1.0107 0.0424  -0.0140 -0.0073 488  LEU B C   
6890 O O   . LEU B 393 ? 0.5477 0.9672 1.0463 0.0338  -0.0035 -0.0118 488  LEU B O   
6891 C CB  . LEU B 393 ? 0.5115 0.8959 0.9646 0.0536  -0.0026 0.0002  488  LEU B CB  
6892 C CG  . LEU B 393 ? 0.5391 0.9100 0.9797 0.0642  0.0011  0.0059  488  LEU B CG  
6893 C CD1 . LEU B 393 ? 0.4575 0.8039 0.8686 0.0614  0.0101  0.0060  488  LEU B CD1 
6894 C CD2 . LEU B 393 ? 0.5047 0.8786 0.9401 0.0716  -0.0136 0.0112  488  LEU B CD2 
6895 N N   . LYS B 394 ? 0.4900 0.9221 0.9849 0.0417  -0.0301 -0.0072 489  LYS B N   
6896 C CA  . LYS B 394 ? 0.4769 0.9151 0.9722 0.0302  -0.0365 -0.0133 489  LYS B CA  
6897 C C   . LYS B 394 ? 0.4992 0.9140 0.9606 0.0245  -0.0347 -0.0147 489  LYS B C   
6898 O O   . LYS B 394 ? 0.5077 0.9048 0.9451 0.0303  -0.0330 -0.0104 489  LYS B O   
6899 C CB  . LYS B 394 ? 0.4520 0.9099 0.9587 0.0314  -0.0550 -0.0130 489  LYS B CB  
6900 C CG  . LYS B 394 ? 0.4598 0.9452 1.0053 0.0304  -0.0572 -0.0156 489  LYS B CG  
6901 C CD  . LYS B 394 ? 0.5179 1.0215 1.0787 0.0402  -0.0719 -0.0106 489  LYS B CD  
6902 N N   . GLU B 395 ? 0.5004 0.9155 0.9613 0.0129  -0.0347 -0.0212 490  GLU B N   
6903 C CA  . GLU B 395 ? 0.5024 0.8958 0.9344 0.0069  -0.0316 -0.0235 490  GLU B CA  
6904 C C   . GLU B 395 ? 0.5151 0.8979 0.9205 0.0123  -0.0413 -0.0199 490  GLU B C   
6905 O O   . GLU B 395 ? 0.5001 0.8622 0.8809 0.0142  -0.0353 -0.0178 490  GLU B O   
6906 C CB  . GLU B 395 ? 0.6039 1.0023 1.0414 -0.0058 -0.0343 -0.0312 490  GLU B CB  
6907 C CG  . GLU B 395 ? 0.6758 1.0513 1.0892 -0.0127 -0.0268 -0.0342 490  GLU B CG  
6908 C CD  . GLU B 395 ? 0.7263 1.0927 1.1446 -0.0153 -0.0100 -0.0341 490  GLU B CD  
6909 O OE1 . GLU B 395 ? 0.7312 1.1122 1.1757 -0.0181 -0.0050 -0.0355 490  GLU B OE1 
6910 O OE2 . GLU B 395 ? 0.6999 1.0449 1.0959 -0.0145 -0.0019 -0.0323 490  GLU B OE2 
6911 N N   . GLU B 396 ? 0.4964 0.8935 0.9065 0.0147  -0.0564 -0.0189 491  GLU B N   
6912 C CA  . GLU B 396 ? 0.5128 0.9010 0.8973 0.0186  -0.0665 -0.0158 491  GLU B CA  
6913 C C   . GLU B 396 ? 0.5039 0.8840 0.8794 0.0306  -0.0648 -0.0074 491  GLU B C   
6914 O O   . GLU B 396 ? 0.4778 0.8504 0.8324 0.0345  -0.0726 -0.0036 491  GLU B O   
6915 C CB  . GLU B 396 ? 0.4897 0.8963 0.8815 0.0164  -0.0838 -0.0176 491  GLU B CB  
6916 C CG  . GLU B 396 ? 0.4794 0.9076 0.8977 0.0241  -0.0913 -0.0130 491  GLU B CG  
6917 C CD  . GLU B 396 ? 0.4759 0.9236 0.9287 0.0194  -0.0876 -0.0176 491  GLU B CD  
6918 O OE1 . GLU B 396 ? 0.4886 0.9567 0.9660 0.0250  -0.0949 -0.0149 491  GLU B OE1 
6919 O OE2 . GLU B 396 ? 0.5333 0.9761 0.9892 0.0104  -0.0775 -0.0235 491  GLU B OE2 
6920 N N   . GLU B 397 ? 0.4826 0.8633 0.8728 0.0361  -0.0542 -0.0045 492  GLU B N   
6921 C CA  . GLU B 397 ? 0.4728 0.8446 0.8559 0.0471  -0.0511 0.0028  492  GLU B CA  
6922 C C   . GLU B 397 ? 0.4670 0.8178 0.8344 0.0475  -0.0361 0.0033  492  GLU B C   
6923 O O   . GLU B 397 ? 0.4760 0.8161 0.8329 0.0556  -0.0332 0.0087  492  GLU B O   
6924 C CB  . GLU B 397 ? 0.4869 0.8764 0.8998 0.0548  -0.0517 0.0059  492  GLU B CB  
6925 C CG  . GLU B 397 ? 0.4718 0.8844 0.9033 0.0553  -0.0675 0.0059  492  GLU B CG  
6926 C CD  . GLU B 397 ? 0.4720 0.9043 0.9375 0.0620  -0.0672 0.0078  492  GLU B CD  
6927 O OE1 . GLU B 397 ? 0.4440 0.8934 0.9233 0.0663  -0.0810 0.0105  492  GLU B OE1 
6928 O OE2 . GLU B 397 ? 0.4908 0.9219 0.9696 0.0630  -0.0532 0.0065  492  GLU B OE2 
6929 N N   . ILE B 398 ? 0.4783 0.8223 0.8428 0.0388  -0.0270 -0.0021 493  ILE B N   
6930 C CA  . ILE B 398 ? 0.4828 0.8093 0.8362 0.0392  -0.0126 -0.0014 493  ILE B CA  
6931 C C   . ILE B 398 ? 0.4810 0.7876 0.8040 0.0418  -0.0129 0.0015  493  ILE B C   
6932 O O   . ILE B 398 ? 0.4813 0.7770 0.7960 0.0482  -0.0065 0.0056  493  ILE B O   
6933 C CB  . ILE B 398 ? 0.5159 0.8401 0.8739 0.0292  -0.0036 -0.0072 493  ILE B CB  
6934 C CG1 . ILE B 398 ? 0.4416 0.7836 0.8304 0.0277  0.0012  -0.0092 493  ILE B CG1 
6935 C CG2 . ILE B 398 ? 0.4994 0.8021 0.8377 0.0287  0.0087  -0.0063 493  ILE B CG2 
6936 C CD1 . ILE B 398 ? 0.5298 0.8735 0.9267 0.0167  0.0071  -0.0149 493  ILE B CD1 
6937 N N   . LEU B 399 ? 0.4820 0.7839 0.7886 0.0368  -0.0202 -0.0009 494  LEU B N   
6938 C CA  . LEU B 399 ? 0.4943 0.7785 0.7731 0.0388  -0.0203 0.0014  494  LEU B CA  
6939 C C   . LEU B 399 ? 0.5084 0.7922 0.7808 0.0481  -0.0267 0.0081  494  LEU B C   
6940 O O   . LEU B 399 ? 0.5040 0.7726 0.7561 0.0512  -0.0241 0.0112  494  LEU B O   
6941 C CB  . LEU B 399 ? 0.5495 0.8301 0.8135 0.0314  -0.0267 -0.0033 494  LEU B CB  
6942 C CG  . LEU B 399 ? 0.5645 0.8414 0.8313 0.0221  -0.0200 -0.0098 494  LEU B CG  
6943 C CD1 . LEU B 399 ? 0.5096 0.7805 0.7596 0.0156  -0.0259 -0.0147 494  LEU B CD1 
6944 C CD2 . LEU B 399 ? 0.5172 0.7790 0.7777 0.0230  -0.0063 -0.0084 494  LEU B CD2 
6945 N N   . ALA B 400 ? 0.4861 0.7860 0.7758 0.0525  -0.0351 0.0107  495  ALA B N   
6946 C CA  . ALA B 400 ? 0.5268 0.8256 0.8116 0.0617  -0.0409 0.0178  495  ALA B CA  
6947 C C   . ALA B 400 ? 0.5247 0.8190 0.8183 0.0694  -0.0314 0.0217  495  ALA B C   
6948 O O   . ALA B 400 ? 0.5232 0.8115 0.8098 0.0771  -0.0337 0.0278  495  ALA B O   
6949 C CB  . ALA B 400 ? 0.4877 0.8054 0.7869 0.0641  -0.0550 0.0197  495  ALA B CB  
6950 N N   . TYR B 401 ? 0.4858 0.7822 0.7939 0.0671  -0.0207 0.0183  496  TYR B N   
6951 C CA  . TYR B 401 ? 0.4775 0.7712 0.7955 0.0740  -0.0113 0.0209  496  TYR B CA  
6952 C C   . TYR B 401 ? 0.4963 0.7687 0.7920 0.0747  -0.0019 0.0221  496  TYR B C   
6953 O O   . TYR B 401 ? 0.5127 0.7757 0.7962 0.0680  0.0039  0.0185  496  TYR B O   
6954 C CB  . TYR B 401 ? 0.4988 0.8041 0.8413 0.0710  -0.0031 0.0166  496  TYR B CB  
6955 C CG  . TYR B 401 ? 0.5058 0.8055 0.8545 0.0772  0.0085  0.0183  496  TYR B CG  
6956 C CD1 . TYR B 401 ? 0.5157 0.8218 0.8781 0.0870  0.0061  0.0225  496  TYR B CD1 
6957 C CD2 . TYR B 401 ? 0.5021 0.7892 0.8417 0.0736  0.0216  0.0158  496  TYR B CD2 
6958 C CE1 . TYR B 401 ? 0.5392 0.8388 0.9063 0.0926  0.0172  0.0233  496  TYR B CE1 
6959 C CE2 . TYR B 401 ? 0.4993 0.7806 0.8425 0.0788  0.0321  0.0168  496  TYR B CE2 
6960 C CZ  . TYR B 401 ? 0.5148 0.8020 0.8714 0.0881  0.0302  0.0201  496  TYR B CZ  
6961 O OH  . TYR B 401 ? 0.5481 0.8283 0.9074 0.0931  0.0413  0.0203  496  TYR B OH  
6962 N N   . ASP B 402 ? 0.4669 0.7317 0.7580 0.0829  -0.0008 0.0272  497  ASP B N   
6963 C CA  . ASP B 402 ? 0.5257 0.7712 0.7971 0.0843  0.0074  0.0286  497  ASP B CA  
6964 C C   . ASP B 402 ? 0.5482 0.7919 0.8314 0.0873  0.0195  0.0275  497  ASP B C   
6965 O O   . ASP B 402 ? 0.5422 0.7911 0.8398 0.0948  0.0198  0.0301  497  ASP B O   
6966 C CB  . ASP B 402 ? 0.4722 0.7095 0.7298 0.0905  0.0008  0.0347  497  ASP B CB  
6967 C CG  . ASP B 402 ? 0.5856 0.8031 0.8194 0.0898  0.0070  0.0356  497  ASP B CG  
6968 O OD1 . ASP B 402 ? 0.5022 0.7121 0.7282 0.0845  0.0152  0.0317  497  ASP B OD1 
6969 O OD2 . ASP B 402 ? 0.5925 0.8021 0.8156 0.0947  0.0035  0.0407  497  ASP B OD2 
6970 N N   . MET B 403 ? 0.5439 0.7804 0.8212 0.0817  0.0295  0.0236  498  MET B N   
6971 C CA  . MET B 403 ? 0.5205 0.7561 0.8082 0.0833  0.0414  0.0218  498  MET B CA  
6972 C C   . MET B 403 ? 0.4880 0.7120 0.7686 0.0908  0.0456  0.0249  498  MET B C   
6973 O O   . MET B 403 ? 0.5267 0.7359 0.7863 0.0906  0.0458  0.0266  498  MET B O   
6974 C CB  . MET B 403 ? 0.5156 0.7435 0.7939 0.0755  0.0505  0.0178  498  MET B CB  
6975 C CG  . MET B 403 ? 0.5387 0.7686 0.8291 0.0755  0.0627  0.0154  498  MET B CG  
6976 S SD  . MET B 403 ? 0.5557 0.7791 0.8379 0.0656  0.0721  0.0116  498  MET B SD  
6977 C CE  . MET B 403 ? 0.5524 0.7567 0.8040 0.0635  0.0693  0.0131  498  MET B CE  
6978 N N   . SER B 404 ? 0.5476 0.7784 0.8467 0.0971  0.0494  0.0254  499  SER B N   
6979 C CA  . SER B 404 ? 0.5498 0.7694 0.8445 0.1042  0.0545  0.0275  499  SER B CA  
6980 C C   . SER B 404 ? 0.5882 0.7965 0.8741 0.1013  0.0679  0.0238  499  SER B C   
6981 O O   . SER B 404 ? 0.5453 0.7564 0.8324 0.0947  0.0740  0.0200  499  SER B O   
6982 C CB  . SER B 404 ? 0.5526 0.7835 0.8714 0.1127  0.0536  0.0291  499  SER B CB  
6983 O OG  . SER B 404 ? 0.5891 0.8325 0.9285 0.1110  0.0612  0.0247  499  SER B OG  
6984 N N   . THR B 405 ? 0.5678 0.7628 0.8442 0.1061  0.0724  0.0250  500  THR B N   
6985 C CA  . THR B 405 ? 0.6158 0.7993 0.8820 0.1037  0.0844  0.0216  500  THR B CA  
6986 C C   . THR B 405 ? 0.6255 0.8182 0.9100 0.1037  0.0946  0.0174  500  THR B C   
6987 O O   . THR B 405 ? 0.6005 0.7895 0.8784 0.0979  0.1034  0.0140  500  THR B O   
6988 C CB  . THR B 405 ? 0.6467 0.8152 0.9015 0.1092  0.0864  0.0234  500  THR B CB  
6989 O OG1 . THR B 405 ? 0.7907 0.9648 1.0628 0.1178  0.0839  0.0257  500  THR B OG1 
6990 C CG2 . THR B 405 ? 0.6340 0.7924 0.8686 0.1075  0.0785  0.0269  500  THR B CG2 
6991 N N   . ASP B 406 ? 0.5851 0.7902 0.8931 0.1102  0.0935  0.0179  501  ASP B N   
6992 C CA  . ASP B 406 ? 0.5822 0.7989 0.9105 0.1100  0.1030  0.0138  501  ASP B CA  
6993 C C   . ASP B 406 ? 0.5359 0.7633 0.8694 0.1014  0.1031  0.0116  501  ASP B C   
6994 O O   . ASP B 406 ? 0.5488 0.7772 0.8845 0.0967  0.1139  0.0078  501  ASP B O   
6995 C CB  . ASP B 406 ? 0.6380 0.8682 0.9930 0.1189  0.1001  0.0150  501  ASP B CB  
6996 C CG  . ASP B 406 ? 0.7247 0.9436 1.0779 0.1276  0.1032  0.0162  501  ASP B CG  
6997 O OD1 . ASP B 406 ? 0.7700 0.9709 1.1009 0.1263  0.1074  0.0158  501  ASP B OD1 
6998 O OD2 . ASP B 406 ? 0.7859 1.0139 1.1607 0.1359  0.1013  0.0176  501  ASP B OD2 
6999 N N   . MET B 407 ? 0.5496 0.7849 0.8850 0.0990  0.0914  0.0139  502  MET B N   
7000 C CA  . MET B 407 ? 0.5422 0.7866 0.8822 0.0903  0.0911  0.0115  502  MET B CA  
7001 C C   . MET B 407 ? 0.5205 0.7503 0.8372 0.0826  0.0970  0.0100  502  MET B C   
7002 O O   . MET B 407 ? 0.4989 0.7323 0.8194 0.0759  0.1038  0.0072  502  MET B O   
7003 C CB  . MET B 407 ? 0.5301 0.7848 0.8752 0.0894  0.0767  0.0137  502  MET B CB  
7004 C CG  . MET B 407 ? 0.5459 0.8199 0.9135 0.0846  0.0750  0.0110  502  MET B CG  
7005 S SD  . MET B 407 ? 0.5729 0.8638 0.9730 0.0883  0.0848  0.0081  502  MET B SD  
7006 C CE  . MET B 407 ? 0.5976 0.8972 1.0141 0.1009  0.0753  0.0122  502  MET B CE  
7007 N N   . GLU B 408 ? 0.5024 0.7160 0.7956 0.0835  0.0947  0.0122  503  GLU B N   
7008 C CA  . GLU B 408 ? 0.5168 0.7163 0.7885 0.0773  0.1005  0.0110  503  GLU B CA  
7009 C C   . GLU B 408 ? 0.5180 0.7144 0.7911 0.0760  0.1143  0.0080  503  GLU B C   
7010 O O   . GLU B 408 ? 0.4911 0.6849 0.7582 0.0691  0.1202  0.0064  503  GLU B O   
7011 C CB  . GLU B 408 ? 0.5091 0.6928 0.7580 0.0795  0.0965  0.0136  503  GLU B CB  
7012 C CG  . GLU B 408 ? 0.5701 0.7538 0.8112 0.0787  0.0842  0.0163  503  GLU B CG  
7013 C CD  . GLU B 408 ? 0.6674 0.8359 0.8869 0.0806  0.0815  0.0187  503  GLU B CD  
7014 O OE1 . GLU B 408 ? 0.6556 0.8221 0.8651 0.0787  0.0733  0.0203  503  GLU B OE1 
7015 O OE2 . GLU B 408 ? 0.7157 0.8742 0.9279 0.0834  0.0878  0.0185  503  GLU B OE2 
7016 N N   . LYS B 409 ? 0.5126 0.7090 0.7935 0.0826  0.1199  0.0072  504  LYS B N   
7017 C CA  . LYS B 409 ? 0.5468 0.7397 0.8274 0.0813  0.1337  0.0038  504  LYS B CA  
7018 C C   . LYS B 409 ? 0.4784 0.6859 0.7788 0.0771  0.1401  0.0012  504  LYS B C   
7019 O O   . LYS B 409 ? 0.4891 0.6927 0.7831 0.0715  0.1503  -0.0010 504  LYS B O   
7020 C CB  . LYS B 409 ? 0.5604 0.7493 0.8452 0.0895  0.1385  0.0027  504  LYS B CB  
7021 C CG  . LYS B 409 ? 0.6162 0.7857 0.8756 0.0899  0.1407  0.0029  504  LYS B CG  
7022 C CD  . LYS B 409 ? 0.6497 0.8131 0.9062 0.0970  0.1328  0.0057  504  LYS B CD  
7023 C CE  . LYS B 409 ? 0.7324 0.8975 1.0039 0.1051  0.1383  0.0039  504  LYS B CE  
7024 N NZ  . LYS B 409 ? 0.7365 0.8942 1.0049 0.1120  0.1308  0.0074  504  LYS B NZ  
7025 N N   . GLU B 410 ? 0.4702 0.6948 0.7944 0.0794  0.1341  0.0015  505  GLU B N   
7026 C CA  . GLU B 410 ? 0.4861 0.7259 0.8305 0.0745  0.1394  -0.0011 505  GLU B CA  
7027 C C   . GLU B 410 ? 0.4726 0.7089 0.8057 0.0644  0.1388  -0.0010 505  GLU B C   
7028 O O   . GLU B 410 ? 0.4419 0.6810 0.7792 0.0581  0.1485  -0.0031 505  GLU B O   
7029 C CB  . GLU B 410 ? 0.4714 0.7308 0.8433 0.0787  0.1308  -0.0005 505  GLU B CB  
7030 C CG  . GLU B 410 ? 0.5031 0.7664 0.8885 0.0893  0.1310  -0.0001 505  GLU B CG  
7031 C CD  . GLU B 410 ? 0.5578 0.8280 0.9603 0.0909  0.1453  -0.0043 505  GLU B CD  
7032 O OE1 . GLU B 410 ? 0.5217 0.8001 0.9329 0.0838  0.1529  -0.0070 505  GLU B OE1 
7033 O OE2 . GLU B 410 ? 0.6484 0.9153 1.0553 0.0991  0.1494  -0.0049 505  GLU B OE2 
7034 N N   . LEU B 411 ? 0.4363 0.6665 0.7555 0.0627  0.1278  0.0015  506  LEU B N   
7035 C CA  . LEU B 411 ? 0.4587 0.6835 0.7662 0.0537  0.1273  0.0016  506  LEU B CA  
7036 C C   . LEU B 411 ? 0.4486 0.6574 0.7351 0.0502  0.1376  0.0015  506  LEU B C   
7037 O O   . LEU B 411 ? 0.4376 0.6446 0.7215 0.0427  0.1436  0.0008  506  LEU B O   
7038 C CB  . LEU B 411 ? 0.4194 0.6399 0.7153 0.0534  0.1141  0.0038  506  LEU B CB  
7039 C CG  . LEU B 411 ? 0.4290 0.6420 0.7117 0.0449  0.1129  0.0037  506  LEU B CG  
7040 C CD1 . LEU B 411 ? 0.4624 0.6888 0.7640 0.0381  0.1139  0.0013  506  LEU B CD1 
7041 C CD2 . LEU B 411 ? 0.4585 0.6650 0.7268 0.0458  0.1012  0.0055  506  LEU B CD2 
7042 N N   . GLY B 412 ? 0.4345 0.6314 0.7060 0.0553  0.1395  0.0023  507  GLY B N   
7043 C CA  . GLY B 412 ? 0.4521 0.6344 0.7033 0.0523  0.1487  0.0021  507  GLY B CA  
7044 C C   . GLY B 412 ? 0.4882 0.6750 0.7480 0.0491  0.1622  -0.0005 507  GLY B C   
7045 O O   . GLY B 412 ? 0.4367 0.6154 0.6835 0.0428  0.1691  -0.0002 507  GLY B O   
7046 N N   . LYS B 413 ? 0.4273 0.6273 0.7096 0.0534  0.1664  -0.0029 508  LYS B N   
7047 C CA  . LYS B 413 ? 0.4847 0.6903 0.7769 0.0502  0.1802  -0.0058 508  LYS B CA  
7048 C C   . LYS B 413 ? 0.4584 0.6721 0.7601 0.0415  0.1820  -0.0056 508  LYS B C   
7049 O O   . LYS B 413 ? 0.4331 0.6429 0.7289 0.0352  0.1930  -0.0062 508  LYS B O   
7050 C CB  . LYS B 413 ? 0.4855 0.7046 0.8022 0.0574  0.1842  -0.0086 508  LYS B CB  
7051 C CG  . LYS B 413 ? 0.5226 0.7331 0.8320 0.0662  0.1836  -0.0091 508  LYS B CG  
7052 C CD  . LYS B 413 ? 0.6276 0.8518 0.9637 0.0733  0.1887  -0.0121 508  LYS B CD  
7053 C CE  . LYS B 413 ? 0.7194 0.9351 1.0509 0.0826  0.1873  -0.0124 508  LYS B CE  
7054 N NZ  . LYS B 413 ? 0.7556 0.9834 1.1133 0.0898  0.1940  -0.0157 508  LYS B NZ  
7055 N N   . ILE B 414 ? 0.4575 0.6824 0.7739 0.0407  0.1713  -0.0049 509  ILE B N   
7056 C CA  . ILE B 414 ? 0.4458 0.6773 0.7708 0.0318  0.1720  -0.0051 509  ILE B CA  
7057 C C   . ILE B 414 ? 0.4254 0.6396 0.7248 0.0249  0.1737  -0.0027 509  ILE B C   
7058 O O   . ILE B 414 ? 0.4504 0.6631 0.7492 0.0173  0.1824  -0.0028 509  ILE B O   
7059 C CB  . ILE B 414 ? 0.4261 0.6710 0.7680 0.0322  0.1586  -0.0051 509  ILE B CB  
7060 C CG1 . ILE B 414 ? 0.4586 0.7235 0.8302 0.0379  0.1581  -0.0073 509  ILE B CG1 
7061 C CG2 . ILE B 414 ? 0.4315 0.6785 0.7763 0.0221  0.1577  -0.0054 509  ILE B CG2 
7062 C CD1 . ILE B 414 ? 0.4538 0.7305 0.8384 0.0408  0.1428  -0.0066 509  ILE B CD1 
7063 N N   . VAL B 415 ? 0.4234 0.6243 0.7019 0.0275  0.1655  -0.0004 510  VAL B N   
7064 C CA  . VAL B 415 ? 0.4563 0.6415 0.7121 0.0217  0.1654  0.0022  510  VAL B CA  
7065 C C   . VAL B 415 ? 0.4476 0.6209 0.6864 0.0199  0.1773  0.0029  510  VAL B C   
7066 O O   . VAL B 415 ? 0.4423 0.6068 0.6697 0.0132  0.1820  0.0048  510  VAL B O   
7067 C CB  . VAL B 415 ? 0.4236 0.5994 0.6636 0.0253  0.1534  0.0041  510  VAL B CB  
7068 C CG1 . VAL B 415 ? 0.4235 0.5830 0.6407 0.0205  0.1539  0.0068  510  VAL B CG1 
7069 C CG2 . VAL B 415 ? 0.4335 0.6205 0.6880 0.0255  0.1419  0.0034  510  VAL B CG2 
7070 N N   . LYS B 416 ? 0.4431 0.6149 0.6790 0.0258  0.1823  0.0015  511  LYS B N   
7071 C CA  . LYS B 416 ? 0.4649 0.6268 0.6854 0.0238  0.1944  0.0013  511  LYS B CA  
7072 C C   . LYS B 416 ? 0.4925 0.6615 0.7245 0.0171  0.2063  0.0003  511  LYS B C   
7073 O O   . LYS B 416 ? 0.4949 0.6535 0.7107 0.0112  0.2140  0.0022  511  LYS B O   
7074 C CB  . LYS B 416 ? 0.4935 0.6547 0.7131 0.0313  0.1979  -0.0013 511  LYS B CB  
7075 C CG  . LYS B 416 ? 0.5191 0.6721 0.7250 0.0296  0.2112  -0.0028 511  LYS B CG  
7076 C CD  . LYS B 416 ? 0.5554 0.6901 0.7306 0.0280  0.2093  -0.0002 511  LYS B CD  
7077 C CE  . LYS B 416 ? 0.6034 0.7309 0.7661 0.0306  0.2188  -0.0033 511  LYS B CE  
7078 N NZ  . LYS B 416 ? 0.6136 0.7242 0.7464 0.0283  0.2176  -0.0010 511  LYS B NZ  
7079 N N   . ALA B 417 ? 0.4455 0.6323 0.7055 0.0175  0.2078  -0.0024 512  ALA B N   
7080 C CA  . ALA B 417 ? 0.4665 0.6613 0.7394 0.0109  0.2202  -0.0037 512  ALA B CA  
7081 C C   . ALA B 417 ? 0.4875 0.6796 0.7588 0.0016  0.2185  -0.0010 512  ALA B C   
7082 O O   . ALA B 417 ? 0.5138 0.7024 0.7811 -0.0057 0.2294  -0.0001 512  ALA B O   
7083 C CB  . ALA B 417 ? 0.4112 0.6272 0.7168 0.0143  0.2224  -0.0077 512  ALA B CB  
7084 N N   . SER B 418 ? 0.4511 0.6443 0.7251 0.0015  0.2053  0.0001  513  SER B N   
7085 C CA  . SER B 418 ? 0.4679 0.6587 0.7426 -0.0072 0.2035  0.0019  513  SER B CA  
7086 C C   . SER B 418 ? 0.4876 0.6574 0.7334 -0.0101 0.2013  0.0063  513  SER B C   
7087 O O   . SER B 418 ? 0.5291 0.6924 0.7705 -0.0181 0.2055  0.0085  513  SER B O   
7088 C CB  . SER B 418 ? 0.4558 0.6583 0.7481 -0.0065 0.1905  0.0003  513  SER B CB  
7089 O OG  . SER B 418 ? 0.4341 0.6286 0.7120 -0.0004 0.1785  0.0016  513  SER B OG  
7090 N N   . HIS B 419 ? 0.4444 0.6037 0.6716 -0.0040 0.1945  0.0077  514  HIS B N   
7091 C CA  . HIS B 419 ? 0.4625 0.6036 0.6645 -0.0056 0.1905  0.0117  514  HIS B CA  
7092 C C   . HIS B 419 ? 0.4673 0.5952 0.6458 -0.0034 0.1966  0.0137  514  HIS B C   
7093 O O   . HIS B 419 ? 0.4830 0.5959 0.6404 -0.0050 0.1942  0.0175  514  HIS B O   
7094 C CB  . HIS B 419 ? 0.4478 0.5876 0.6471 -0.0009 0.1760  0.0116  514  HIS B CB  
7095 C CG  . HIS B 419 ? 0.4775 0.6258 0.6930 -0.0045 0.1689  0.0101  514  HIS B CG  
7096 N ND1 . HIS B 419 ? 0.4692 0.6354 0.7104 -0.0054 0.1690  0.0067  514  HIS B ND1 
7097 C CD2 . HIS B 419 ? 0.4908 0.6321 0.7006 -0.0077 0.1615  0.0112  514  HIS B CD2 
7098 C CE1 . HIS B 419 ? 0.4665 0.6364 0.7163 -0.0094 0.1615  0.0057  514  HIS B CE1 
7099 N NE2 . HIS B 419 ? 0.4902 0.6447 0.7210 -0.0109 0.1573  0.0081  514  HIS B NE2 
7100 N N   . HIS B 420 ? 0.4391 0.5722 0.6209 0.0004  0.2038  0.0111  515  HIS B N   
7101 C CA  . HIS B 420 ? 0.4588 0.5804 0.6190 0.0015  0.2113  0.0120  515  HIS B CA  
7102 C C   . HIS B 420 ? 0.4634 0.5727 0.6027 0.0062  0.2021  0.0138  515  HIS B C   
7103 O O   . HIS B 420 ? 0.4983 0.5938 0.6146 0.0042  0.2039  0.0168  515  HIS B O   
7104 C CB  . HIS B 420 ? 0.4657 0.5784 0.6135 -0.0066 0.2215  0.0153  515  HIS B CB  
7105 C CG  . HIS B 420 ? 0.5006 0.6250 0.6691 -0.0124 0.2311  0.0138  515  HIS B CG  
7106 N ND1 . HIS B 420 ? 0.5058 0.6469 0.6980 -0.0096 0.2358  0.0089  515  HIS B ND1 
7107 C CD2 . HIS B 420 ? 0.5615 0.6836 0.7315 -0.0209 0.2368  0.0166  515  HIS B CD2 
7108 C CE1 . HIS B 420 ? 0.5453 0.6950 0.7535 -0.0164 0.2441  0.0084  515  HIS B CE1 
7109 N NE2 . HIS B 420 ? 0.5575 0.6956 0.7524 -0.0236 0.2450  0.0130  515  HIS B NE2 
7110 N N   . THR B 421 ? 0.4644 0.5790 0.6116 0.0122  0.1921  0.0120  516  THR B N   
7111 C CA  . THR B 421 ? 0.4438 0.5482 0.5738 0.0164  0.1832  0.0135  516  THR B CA  
7112 C C   . THR B 421 ? 0.4837 0.5949 0.6228 0.0240  0.1783  0.0104  516  THR B C   
7113 O O   . THR B 421 ? 0.4696 0.5941 0.6303 0.0261  0.1777  0.0080  516  THR B O   
7114 C CB  . THR B 421 ? 0.4211 0.5209 0.5473 0.0144  0.1732  0.0164  516  THR B CB  
7115 O OG1 . THR B 421 ? 0.4358 0.5267 0.5460 0.0185  0.1654  0.0176  516  THR B OG1 
7116 C CG2 . THR B 421 ? 0.4221 0.5351 0.5705 0.0150  0.1664  0.0145  516  THR B CG2 
7117 N N   . ASP B 422 ? 0.4257 0.5276 0.5484 0.0279  0.1745  0.0106  517  ASP B N   
7118 C CA  . ASP B 422 ? 0.4247 0.5296 0.5525 0.0348  0.1690  0.0086  517  ASP B CA  
7119 C C   . ASP B 422 ? 0.4626 0.5658 0.5878 0.0369  0.1564  0.0105  517  ASP B C   
7120 O O   . ASP B 422 ? 0.4402 0.5443 0.5673 0.0423  0.1511  0.0096  517  ASP B O   
7121 C CB  . ASP B 422 ? 0.4452 0.5409 0.5572 0.0375  0.1735  0.0069  517  ASP B CB  
7122 C CG  . ASP B 422 ? 0.5144 0.6124 0.6297 0.0365  0.1865  0.0038  517  ASP B CG  
7123 O OD1 . ASP B 422 ? 0.5065 0.6167 0.6432 0.0379  0.1906  0.0016  517  ASP B OD1 
7124 O OD2 . ASP B 422 ? 0.5101 0.5982 0.6066 0.0341  0.1927  0.0035  517  ASP B OD2 
7125 N N   . TYR B 423 ? 0.4028 0.5033 0.5241 0.0326  0.1521  0.0131  518  TYR B N   
7126 C CA  . TYR B 423 ? 0.4199 0.5168 0.5354 0.0342  0.1414  0.0146  518  TYR B CA  
7127 C C   . TYR B 423 ? 0.4091 0.5118 0.5354 0.0307  0.1368  0.0152  518  TYR B C   
7128 O O   . TYR B 423 ? 0.3889 0.4894 0.5147 0.0252  0.1409  0.0163  518  TYR B O   
7129 C CB  . TYR B 423 ? 0.4172 0.5005 0.5105 0.0330  0.1403  0.0169  518  TYR B CB  
7130 C CG  . TYR B 423 ? 0.4390 0.5180 0.5261 0.0334  0.1307  0.0187  518  TYR B CG  
7131 C CD1 . TYR B 423 ? 0.4398 0.5217 0.5298 0.0378  0.1232  0.0178  518  TYR B CD1 
7132 C CD2 . TYR B 423 ? 0.4224 0.4937 0.5001 0.0296  0.1297  0.0214  518  TYR B CD2 
7133 C CE1 . TYR B 423 ? 0.4345 0.5128 0.5186 0.0380  0.1154  0.0190  518  TYR B CE1 
7134 C CE2 . TYR B 423 ? 0.4119 0.4795 0.4848 0.0303  0.1217  0.0225  518  TYR B CE2 
7135 C CZ  . TYR B 423 ? 0.4489 0.5204 0.5251 0.0344  0.1148  0.0210  518  TYR B CZ  
7136 O OH  . TYR B 423 ? 0.4335 0.5015 0.5049 0.0350  0.1078  0.0217  518  TYR B OH  
7137 N N   . TYR B 424 ? 0.4057 0.5152 0.5412 0.0335  0.1284  0.0143  519  TYR B N   
7138 C CA  . TYR B 424 ? 0.4094 0.5236 0.5536 0.0298  0.1234  0.0141  519  TYR B CA  
7139 C C   . TYR B 424 ? 0.3922 0.5090 0.5372 0.0331  0.1130  0.0137  519  TYR B C   
7140 O O   . TYR B 424 ? 0.3907 0.5063 0.5311 0.0383  0.1100  0.0140  519  TYR B O   
7141 C CB  . TYR B 424 ? 0.3859 0.5129 0.5507 0.0269  0.1275  0.0122  519  TYR B CB  
7142 C CG  . TYR B 424 ? 0.4147 0.5536 0.5947 0.0321  0.1271  0.0104  519  TYR B CG  
7143 C CD1 . TYR B 424 ? 0.4276 0.5679 0.6105 0.0343  0.1358  0.0096  519  TYR B CD1 
7144 C CD2 . TYR B 424 ? 0.4253 0.5735 0.6162 0.0350  0.1180  0.0096  519  TYR B CD2 
7145 C CE1 . TYR B 424 ? 0.4472 0.5975 0.6447 0.0399  0.1356  0.0080  519  TYR B CE1 
7146 C CE2 . TYR B 424 ? 0.4092 0.5678 0.6142 0.0406  0.1170  0.0087  519  TYR B CE2 
7147 C CZ  . TYR B 424 ? 0.4445 0.6038 0.6532 0.0432  0.1259  0.0079  519  TYR B CZ  
7148 O OH  . TYR B 424 ? 0.4959 0.6648 0.7195 0.0492  0.1254  0.0070  519  TYR B OH  
7149 N N   . ILE B 425 ? 0.3674 0.4871 0.5174 0.0298  0.1077  0.0130  520  ILE B N   
7150 C CA  . ILE B 425 ? 0.3903 0.5107 0.5378 0.0316  0.0982  0.0125  520  ILE B CA  
7151 C C   . ILE B 425 ? 0.4043 0.5377 0.5686 0.0302  0.0933  0.0102  520  ILE B C   
7152 O O   . ILE B 425 ? 0.3709 0.5092 0.5459 0.0251  0.0963  0.0088  520  ILE B O   
7153 C CB  . ILE B 425 ? 0.4119 0.5212 0.5460 0.0288  0.0959  0.0132  520  ILE B CB  
7154 C CG1 . ILE B 425 ? 0.4011 0.4986 0.5185 0.0308  0.0990  0.0156  520  ILE B CG1 
7155 C CG2 . ILE B 425 ? 0.3721 0.4831 0.5049 0.0297  0.0870  0.0117  520  ILE B CG2 
7156 C CD1 . ILE B 425 ? 0.3884 0.4751 0.4947 0.0279  0.0984  0.0169  520  ILE B CD1 
7157 N N   . ILE B 426 ? 0.3937 0.5328 0.5604 0.0342  0.0857  0.0099  521  ILE B N   
7158 C CA  . ILE B 426 ? 0.3861 0.5368 0.5657 0.0327  0.0787  0.0079  521  ILE B CA  
7159 C C   . ILE B 426 ? 0.4249 0.5710 0.5933 0.0325  0.0708  0.0072  521  ILE B C   
7160 O O   . ILE B 426 ? 0.4424 0.5818 0.5983 0.0365  0.0686  0.0090  521  ILE B O   
7161 C CB  . ILE B 426 ? 0.3628 0.5258 0.5563 0.0378  0.0763  0.0083  521  ILE B CB  
7162 C CG1 . ILE B 426 ? 0.4090 0.5772 0.6150 0.0377  0.0853  0.0081  521  ILE B CG1 
7163 C CG2 . ILE B 426 ? 0.3750 0.5511 0.5815 0.0362  0.0678  0.0064  521  ILE B CG2 
7164 C CD1 . ILE B 426 ? 0.3767 0.5567 0.5981 0.0435  0.0840  0.0085  521  ILE B CD1 
7165 N N   . ILE B 427 ? 0.4047 0.5540 0.5774 0.0274  0.0670  0.0044  522  ILE B N   
7166 C CA  . ILE B 427 ? 0.4078 0.5537 0.5710 0.0266  0.0598  0.0027  522  ILE B CA  
7167 C C   . ILE B 427 ? 0.4339 0.5930 0.6082 0.0254  0.0517  0.0002  522  ILE B C   
7168 O O   . ILE B 427 ? 0.4008 0.5715 0.5916 0.0243  0.0518  -0.0005 522  ILE B O   
7169 C CB  . ILE B 427 ? 0.4324 0.5679 0.5879 0.0215  0.0620  0.0008  522  ILE B CB  
7170 C CG1 . ILE B 427 ? 0.4254 0.5659 0.5944 0.0148  0.0643  -0.0020 522  ILE B CG1 
7171 C CG2 . ILE B 427 ? 0.4226 0.5450 0.5655 0.0231  0.0682  0.0036  522  ILE B CG2 
7172 C CD1 . ILE B 427 ? 0.4473 0.5765 0.6097 0.0096  0.0661  -0.0040 522  ILE B CD1 
7173 N N   . ASN B 428 ? 0.4089 0.5662 0.5737 0.0253  0.0447  -0.0013 523  ASN B N   
7174 C CA  . ASN B 428 ? 0.4047 0.5725 0.5763 0.0226  0.0363  -0.0046 523  ASN B CA  
7175 C C   . ASN B 428 ? 0.4291 0.6096 0.6104 0.0274  0.0310  -0.0021 523  ASN B C   
7176 O O   . ASN B 428 ? 0.4441 0.6378 0.6410 0.0253  0.0270  -0.0038 523  ASN B O   
7177 C CB  . ASN B 428 ? 0.4308 0.6029 0.6146 0.0152  0.0378  -0.0088 523  ASN B CB  
7178 C CG  . ASN B 428 ? 0.4675 0.6267 0.6412 0.0104  0.0408  -0.0117 523  ASN B CG  
7179 O OD1 . ASN B 428 ? 0.4700 0.6176 0.6282 0.0128  0.0420  -0.0106 523  ASN B OD1 
7180 N ND2 . ASN B 428 ? 0.4805 0.6417 0.6637 0.0035  0.0419  -0.0156 523  ASN B ND2 
7181 N N   . PHE B 429 ? 0.3970 0.5734 0.5701 0.0338  0.0311  0.0021  524  PHE B N   
7182 C CA  . PHE B 429 ? 0.4321 0.6183 0.6124 0.0392  0.0255  0.0052  524  PHE B CA  
7183 C C   . PHE B 429 ? 0.4390 0.6320 0.6162 0.0380  0.0147  0.0039  524  PHE B C   
7184 O O   . PHE B 429 ? 0.4409 0.6275 0.6048 0.0346  0.0125  0.0012  524  PHE B O   
7185 C CB  . PHE B 429 ? 0.4206 0.5984 0.5906 0.0457  0.0280  0.0099  524  PHE B CB  
7186 C CG  . PHE B 429 ? 0.4563 0.6307 0.6318 0.0482  0.0373  0.0115  524  PHE B CG  
7187 C CD1 . PHE B 429 ? 0.4634 0.6268 0.6306 0.0456  0.0451  0.0106  524  PHE B CD1 
7188 C CD2 . PHE B 429 ? 0.4682 0.6501 0.6568 0.0533  0.0380  0.0139  524  PHE B CD2 
7189 C CE1 . PHE B 429 ? 0.4390 0.5991 0.6094 0.0474  0.0535  0.0118  524  PHE B CE1 
7190 C CE2 . PHE B 429 ? 0.4571 0.6355 0.6498 0.0554  0.0470  0.0146  524  PHE B CE2 
7191 C CZ  . PHE B 429 ? 0.4514 0.6188 0.6341 0.0522  0.0548  0.0135  524  PHE B CZ  
7192 N N   . PRO B 430 ? 0.4441 0.6500 0.6331 0.0410  0.0079  0.0057  525  PRO B N   
7193 C CA  . PRO B 430 ? 0.4466 0.6590 0.6308 0.0400  -0.0032 0.0049  525  PRO B CA  
7194 C C   . PRO B 430 ? 0.4864 0.6889 0.6498 0.0435  -0.0058 0.0082  525  PRO B C   
7195 O O   . PRO B 430 ? 0.4755 0.6715 0.6343 0.0492  -0.0023 0.0130  525  PRO B O   
7196 C CB  . PRO B 430 ? 0.4450 0.6736 0.6480 0.0437  -0.0095 0.0074  525  PRO B CB  
7197 C CG  . PRO B 430 ? 0.4744 0.7045 0.6921 0.0470  -0.0009 0.0091  525  PRO B CG  
7198 C CD  . PRO B 430 ? 0.4740 0.6907 0.6835 0.0440  0.0101  0.0073  525  PRO B CD  
7199 N N   . SER B 431 ? 0.4644 0.6654 0.6151 0.0395  -0.0115 0.0052  526  SER B N   
7200 C CA  . SER B 431 ? 0.5121 0.7029 0.6417 0.0414  -0.0127 0.0073  526  SER B CA  
7201 C C   . SER B 431 ? 0.5005 0.6935 0.6276 0.0482  -0.0177 0.0142  526  SER B C   
7202 O O   . SER B 431 ? 0.4882 0.6710 0.6029 0.0517  -0.0143 0.0180  526  SER B O   
7203 C CB  . SER B 431 ? 0.4816 0.6726 0.5996 0.0357  -0.0184 0.0021  526  SER B CB  
7204 O OG  . SER B 431 ? 0.5147 0.7012 0.6343 0.0298  -0.0131 -0.0042 526  SER B OG  
7205 N N   . ALA B 432 ? 0.4478 0.6542 0.5871 0.0501  -0.0259 0.0161  527  ALA B N   
7206 C CA  . ALA B 432 ? 0.5243 0.7328 0.6617 0.0569  -0.0318 0.0233  527  ALA B CA  
7207 C C   . ALA B 432 ? 0.5300 0.7331 0.6741 0.0634  -0.0247 0.0282  527  ALA B C   
7208 O O   . ALA B 432 ? 0.5384 0.7386 0.6779 0.0693  -0.0276 0.0345  527  ALA B O   
7209 C CB  . ALA B 432 ? 0.4794 0.7047 0.6309 0.0577  -0.0428 0.0241  527  ALA B CB  
7210 N N   . LEU B 433 ? 0.5190 0.7199 0.6731 0.0624  -0.0154 0.0254  528  LEU B N   
7211 C CA  . LEU B 433 ? 0.4881 0.6842 0.6489 0.0680  -0.0082 0.0289  528  LEU B CA  
7212 C C   . LEU B 433 ? 0.4949 0.6752 0.6405 0.0676  0.0005  0.0289  528  LEU B C   
7213 O O   . LEU B 433 ? 0.5293 0.7043 0.6789 0.0710  0.0076  0.0306  528  LEU B O   
7214 C CB  . LEU B 433 ? 0.4725 0.6778 0.6550 0.0675  -0.0035 0.0262  528  LEU B CB  
7215 C CG  . LEU B 433 ? 0.4989 0.7220 0.7005 0.0683  -0.0118 0.0261  528  LEU B CG  
7216 C CD1 . LEU B 433 ? 0.5150 0.7469 0.7390 0.0680  -0.0055 0.0236  528  LEU B CD1 
7217 C CD2 . LEU B 433 ? 0.4902 0.7167 0.6930 0.0759  -0.0197 0.0328  528  LEU B CD2 
7218 N N   . ARG B 434 ? 0.4511 0.6241 0.5799 0.0633  0.0002  0.0267  529  ARG B N   
7219 C CA  . ARG B 434 ? 0.4959 0.6555 0.6114 0.0623  0.0078  0.0261  529  ARG B CA  
7220 C C   . ARG B 434 ? 0.4738 0.6261 0.5711 0.0631  0.0047  0.0289  529  ARG B C   
7221 O O   . ARG B 434 ? 0.4836 0.6410 0.5762 0.0630  -0.0034 0.0302  529  ARG B O   
7222 C CB  . ARG B 434 ? 0.4635 0.6208 0.5777 0.0560  0.0120  0.0201  529  ARG B CB  
7223 C CG  . ARG B 434 ? 0.4515 0.6155 0.5831 0.0542  0.0158  0.0175  529  ARG B CG  
7224 C CD  . ARG B 434 ? 0.4511 0.6113 0.5890 0.0581  0.0234  0.0199  529  ARG B CD  
7225 N NE  . ARG B 434 ? 0.4644 0.6127 0.5918 0.0566  0.0310  0.0189  529  ARG B NE  
7226 C CZ  . ARG B 434 ? 0.4843 0.6287 0.6158 0.0573  0.0387  0.0189  529  ARG B CZ  
7227 N NH1 . ARG B 434 ? 0.4792 0.6304 0.6254 0.0595  0.0411  0.0195  529  ARG B NH1 
7228 N NH2 . ARG B 434 ? 0.4475 0.5814 0.5683 0.0556  0.0441  0.0181  529  ARG B NH2 
7229 N N   . PRO B 435 ? 0.4783 0.6192 0.5647 0.0637  0.0107  0.0299  530  PRO B N   
7230 C CA  . PRO B 435 ? 0.4937 0.6278 0.5636 0.0644  0.0087  0.0330  530  PRO B CA  
7231 C C   . PRO B 435 ? 0.4777 0.6127 0.5360 0.0596  0.0050  0.0294  530  PRO B C   
7232 O O   . PRO B 435 ? 0.4692 0.6076 0.5309 0.0553  0.0052  0.0239  530  PRO B O   
7233 C CB  . PRO B 435 ? 0.4754 0.5982 0.5391 0.0649  0.0170  0.0334  530  PRO B CB  
7234 C CG  . PRO B 435 ? 0.4972 0.6210 0.5747 0.0666  0.0222  0.0325  530  PRO B CG  
7235 C CD  . PRO B 435 ? 0.4518 0.5859 0.5414 0.0642  0.0196  0.0290  530  PRO B CD  
7236 N N   . PHE B 436 ? 0.4757 0.6066 0.5194 0.0601  0.0023  0.0326  531  PHE B N   
7237 C CA  . PHE B 436 ? 0.5431 0.6751 0.5741 0.0559  -0.0016 0.0294  531  PHE B CA  
7238 C C   . PHE B 436 ? 0.5279 0.6545 0.5532 0.0515  0.0045  0.0231  531  PHE B C   
7239 O O   . PHE B 436 ? 0.5107 0.6393 0.5296 0.0474  0.0021  0.0183  531  PHE B O   
7240 C CB  . PHE B 436 ? 0.4977 0.6254 0.5132 0.0574  -0.0044 0.0347  531  PHE B CB  
7241 C CG  . PHE B 436 ? 0.5188 0.6356 0.5247 0.0576  0.0031  0.0362  531  PHE B CG  
7242 C CD1 . PHE B 436 ? 0.5110 0.6222 0.5212 0.0616  0.0069  0.0410  531  PHE B CD1 
7243 C CD2 . PHE B 436 ? 0.5334 0.6457 0.5265 0.0536  0.0066  0.0322  531  PHE B CD2 
7244 C CE1 . PHE B 436 ? 0.5467 0.6486 0.5489 0.0612  0.0134  0.0420  531  PHE B CE1 
7245 C CE2 . PHE B 436 ? 0.5607 0.6645 0.5469 0.0536  0.0134  0.0333  531  PHE B CE2 
7246 C CZ  . PHE B 436 ? 0.5327 0.6314 0.5234 0.0572  0.0166  0.0383  531  PHE B CZ  
7247 N N   . TYR B 437 ? 0.4877 0.6073 0.5148 0.0523  0.0121  0.0230  532  TYR B N   
7248 C CA  . TYR B 437 ? 0.4803 0.5946 0.5026 0.0490  0.0175  0.0178  532  TYR B CA  
7249 C C   . TYR B 437 ? 0.4946 0.6115 0.5281 0.0465  0.0192  0.0129  532  TYR B C   
7250 O O   . TYR B 437 ? 0.4850 0.5970 0.5161 0.0442  0.0236  0.0088  532  TYR B O   
7251 C CB  . TYR B 437 ? 0.5021 0.6080 0.5205 0.0508  0.0242  0.0201  532  TYR B CB  
7252 C CG  . TYR B 437 ? 0.4758 0.5807 0.5042 0.0543  0.0266  0.0237  532  TYR B CG  
7253 C CD1 . TYR B 437 ? 0.4863 0.5881 0.5125 0.0578  0.0265  0.0293  532  TYR B CD1 
7254 C CD2 . TYR B 437 ? 0.4750 0.5813 0.5146 0.0539  0.0294  0.0214  532  TYR B CD2 
7255 C CE1 . TYR B 437 ? 0.4976 0.5979 0.5330 0.0610  0.0293  0.0318  532  TYR B CE1 
7256 C CE2 . TYR B 437 ? 0.5128 0.6182 0.5607 0.0569  0.0323  0.0240  532  TYR B CE2 
7257 C CZ  . TYR B 437 ? 0.4896 0.5919 0.5354 0.0605  0.0323  0.0288  532  TYR B CZ  
7258 O OH  . TYR B 437 ? 0.5511 0.6519 0.6051 0.0634  0.0357  0.0306  532  TYR B OH  
7259 N N   . THR B 438 ? 0.4730 0.5972 0.5191 0.0471  0.0161  0.0134  533  THR B N   
7260 C CA  . THR B 438 ? 0.4470 0.5739 0.5046 0.0443  0.0179  0.0093  533  THR B CA  
7261 C C   . THR B 438 ? 0.4635 0.5935 0.5186 0.0394  0.0143  0.0034  533  THR B C   
7262 O O   . THR B 438 ? 0.4598 0.5965 0.5129 0.0385  0.0073  0.0031  533  THR B O   
7263 C CB  . THR B 438 ? 0.4478 0.5829 0.5208 0.0463  0.0160  0.0117  533  THR B CB  
7264 O OG1 . THR B 438 ? 0.4427 0.5744 0.5178 0.0510  0.0197  0.0165  533  THR B OG1 
7265 C CG2 . THR B 438 ? 0.4130 0.5507 0.4981 0.0429  0.0190  0.0077  533  THR B CG2 
7266 N N   . MET B 439 ? 0.4688 0.5937 0.5243 0.0362  0.0186  -0.0013 534  MET B N   
7267 C CA  . MET B 439 ? 0.4773 0.6039 0.5314 0.0311  0.0158  -0.0077 534  MET B CA  
7268 C C   . MET B 439 ? 0.5205 0.6559 0.5892 0.0285  0.0124  -0.0094 534  MET B C   
7269 O O   . MET B 439 ? 0.4612 0.5969 0.5415 0.0287  0.0164  -0.0083 534  MET B O   
7270 C CB  . MET B 439 ? 0.4891 0.6063 0.5393 0.0289  0.0217  -0.0121 534  MET B CB  
7271 C CG  . MET B 439 ? 0.4533 0.5702 0.5008 0.0237  0.0195  -0.0196 534  MET B CG  
7272 S SD  . MET B 439 ? 0.5617 0.6831 0.5949 0.0224  0.0125  -0.0218 534  MET B SD  
7273 C CE  . MET B 439 ? 0.6107 0.7333 0.6460 0.0154  0.0097  -0.0313 534  MET B CE  
7274 N N   . TYR B 440 ? 0.5048 0.6479 0.5728 0.0257  0.0050  -0.0122 535  TYR B N   
7275 C CA  . TYR B 440 ? 0.5309 0.6837 0.6132 0.0223  0.0009  -0.0148 535  TYR B CA  
7276 C C   . TYR B 440 ? 0.5487 0.6970 0.6333 0.0161  0.0037  -0.0220 535  TYR B C   
7277 O O   . TYR B 440 ? 0.5180 0.6569 0.5916 0.0148  0.0070  -0.0255 535  TYR B O   
7278 C CB  . TYR B 440 ? 0.5178 0.6812 0.5980 0.0218  -0.0092 -0.0147 535  TYR B CB  
7279 C CG  . TYR B 440 ? 0.5907 0.7498 0.6524 0.0196  -0.0122 -0.0182 535  TYR B CG  
7280 C CD1 . TYR B 440 ? 0.5805 0.7391 0.6392 0.0133  -0.0139 -0.0263 535  TYR B CD1 
7281 C CD2 . TYR B 440 ? 0.5754 0.7303 0.6222 0.0236  -0.0125 -0.0138 535  TYR B CD2 
7282 C CE1 . TYR B 440 ? 0.6297 0.7842 0.6708 0.0112  -0.0158 -0.0303 535  TYR B CE1 
7283 C CE2 . TYR B 440 ? 0.5884 0.7395 0.6177 0.0212  -0.0142 -0.0171 535  TYR B CE2 
7284 C CZ  . TYR B 440 ? 0.6302 0.7812 0.6565 0.0152  -0.0158 -0.0256 535  TYR B CZ  
7285 O OH  . TYR B 440 ? 0.7068 0.8538 0.7152 0.0128  -0.0168 -0.0297 535  TYR B OH  
7286 N N   . LYS B 441 ? 0.5497 0.7047 0.6496 0.0124  0.0029  -0.0243 536  LYS B N   
7287 C CA  . LYS B 441 ? 0.5820 0.7330 0.6850 0.0058  0.0047  -0.0313 536  LYS B CA  
7288 C C   . LYS B 441 ? 0.6303 0.7855 0.7260 0.0014  -0.0029 -0.0375 536  LYS B C   
7289 O O   . LYS B 441 ? 0.6048 0.7721 0.7048 0.0007  -0.0110 -0.0372 536  LYS B O   
7290 C CB  . LYS B 441 ? 0.5799 0.7370 0.7019 0.0025  0.0066  -0.0317 536  LYS B CB  
7291 C CG  . LYS B 441 ? 0.5637 0.7144 0.6915 0.0052  0.0155  -0.0271 536  LYS B CG  
7292 C CD  . LYS B 441 ? 0.5706 0.7266 0.7161 0.0005  0.0181  -0.0285 536  LYS B CD  
7293 C CE  . LYS B 441 ? 0.5388 0.6876 0.6878 0.0026  0.0274  -0.0239 536  LYS B CE  
7294 N NZ  . LYS B 441 ? 0.5515 0.6845 0.6872 0.0037  0.0328  -0.0237 536  LYS B NZ  
7295 N N   . GLU B 442 ? 0.6517 0.7969 0.7361 -0.0014 -0.0005 -0.0433 537  GLU B N   
7296 C CA  . GLU B 442 ? 0.7174 0.8655 0.7912 -0.0052 -0.0073 -0.0492 537  GLU B CA  
7297 C C   . GLU B 442 ? 0.7172 0.8743 0.8021 -0.0121 -0.0132 -0.0552 537  GLU B C   
7298 O O   . GLU B 442 ? 0.7115 0.8768 0.7910 -0.0146 -0.0218 -0.0581 537  GLU B O   
7299 C CB  . GLU B 442 ? 0.7772 0.9122 0.8365 -0.0062 -0.0024 -0.0546 537  GLU B CB  
7300 C CG  . GLU B 442 ? 0.8282 0.9615 0.8700 -0.0019 -0.0033 -0.0518 537  GLU B CG  
7301 C CD  . GLU B 442 ? 0.8954 1.0159 0.9254 -0.0011 0.0037  -0.0553 537  GLU B CD  
7302 O OE1 . GLU B 442 ? 0.9057 1.0174 0.9421 -0.0011 0.0106  -0.0565 537  GLU B OE1 
7303 O OE2 . GLU B 442 ? 0.9015 1.0210 0.9159 -0.0005 0.0025  -0.0567 537  GLU B OE2 
7304 N N   . ASP B 443 ? 0.7180 0.8740 0.8182 -0.0156 -0.0090 -0.0567 538  ASP B N   
7305 C CA  . ASP B 443 ? 0.7175 0.8829 0.8310 -0.0227 -0.0141 -0.0621 538  ASP B CA  
7306 C C   . ASP B 443 ? 0.6825 0.8643 0.8118 -0.0211 -0.0194 -0.0571 538  ASP B C   
7307 O O   . ASP B 443 ? 0.6902 0.8835 0.8303 -0.0266 -0.0260 -0.0613 538  ASP B O   
7308 C CB  . ASP B 443 ? 0.8015 0.9579 0.9250 -0.0279 -0.0066 -0.0660 538  ASP B CB  
7309 C CG  . ASP B 443 ? 0.9354 1.0761 1.0459 -0.0304 -0.0023 -0.0725 538  ASP B CG  
7310 O OD1 . ASP B 443 ? 1.0067 1.1475 1.1051 -0.0328 -0.0074 -0.0786 538  ASP B OD1 
7311 O OD2 . ASP B 443 ? 1.0410 1.1691 1.1531 -0.0297 0.0063  -0.0715 538  ASP B OD2 
7312 N N   . GLU B 444 ? 0.6446 0.8281 0.7764 -0.0138 -0.0167 -0.0487 539  GLU B N   
7313 C CA  . GLU B 444 ? 0.6209 0.8195 0.7683 -0.0110 -0.0210 -0.0436 539  GLU B CA  
7314 C C   . GLU B 444 ? 0.5671 0.7654 0.7056 -0.0022 -0.0218 -0.0356 539  GLU B C   
7315 O O   . GLU B 444 ? 0.5473 0.7423 0.6904 0.0028  -0.0153 -0.0299 539  GLU B O   
7316 C CB  . GLU B 444 ? 0.6130 0.8130 0.7793 -0.0124 -0.0137 -0.0422 539  GLU B CB  
7317 C CG  . GLU B 444 ? 0.6561 0.8744 0.8437 -0.0130 -0.0187 -0.0408 539  GLU B CG  
7318 C CD  . GLU B 444 ? 0.6865 0.9056 0.8916 -0.0140 -0.0097 -0.0388 539  GLU B CD  
7319 O OE1 . GLU B 444 ? 0.7256 0.9593 0.9490 -0.0127 -0.0117 -0.0365 539  GLU B OE1 
7320 O OE2 . GLU B 444 ? 0.6875 0.8926 0.8877 -0.0157 -0.0006 -0.0394 539  GLU B OE2 
7321 N N   . PRO B 445 ? 0.5518 0.7531 0.6769 -0.0005 -0.0297 -0.0351 540  PRO B N   
7322 C CA  . PRO B 445 ? 0.5653 0.7629 0.6787 0.0072  -0.0295 -0.0277 540  PRO B CA  
7323 C C   . PRO B 445 ? 0.5554 0.7618 0.6821 0.0135  -0.0308 -0.0201 540  PRO B C   
7324 O O   . PRO B 445 ? 0.5378 0.7389 0.6567 0.0198  -0.0284 -0.0138 540  PRO B O   
7325 C CB  . PRO B 445 ? 0.5896 0.7897 0.6865 0.0061  -0.0386 -0.0294 540  PRO B CB  
7326 C CG  . PRO B 445 ? 0.6060 0.8073 0.7026 -0.0024 -0.0415 -0.0390 540  PRO B CG  
7327 C CD  . PRO B 445 ? 0.5827 0.7901 0.7015 -0.0060 -0.0390 -0.0413 540  PRO B CD  
7328 N N   . ALA B 446 ? 0.5101 0.7301 0.6571 0.0120  -0.0343 -0.0206 541  ALA B N   
7329 C CA  . ALA B 446 ? 0.5195 0.7473 0.6807 0.0185  -0.0340 -0.0138 541  ALA B CA  
7330 C C   . ALA B 446 ? 0.5114 0.7298 0.6765 0.0213  -0.0220 -0.0111 541  ALA B C   
7331 O O   . ALA B 446 ? 0.5110 0.7316 0.6830 0.0277  -0.0200 -0.0053 541  ALA B O   
7332 C CB  . ALA B 446 ? 0.5334 0.7791 0.7175 0.0160  -0.0400 -0.0156 541  ALA B CB  
7333 N N   . ILE B 447 ? 0.4688 0.6762 0.6290 0.0168  -0.0144 -0.0153 542  ILE B N   
7334 C CA  . ILE B 447 ? 0.5127 0.7109 0.6757 0.0180  -0.0034 -0.0135 542  ILE B CA  
7335 C C   . ILE B 447 ? 0.4920 0.6745 0.6349 0.0199  0.0011  -0.0126 542  ILE B C   
7336 O O   . ILE B 447 ? 0.5094 0.6873 0.6392 0.0172  -0.0021 -0.0162 542  ILE B O   
7337 C CB  . ILE B 447 ? 0.5385 0.7370 0.7133 0.0109  0.0013  -0.0186 542  ILE B CB  
7338 C CG1 . ILE B 447 ? 0.5870 0.8024 0.7841 0.0089  -0.0023 -0.0194 542  ILE B CG1 
7339 C CG2 . ILE B 447 ? 0.5350 0.7216 0.7085 0.0113  0.0125  -0.0169 542  ILE B CG2 
7340 C CD1 . ILE B 447 ? 0.5271 0.7486 0.7365 0.0151  0.0013  -0.0138 542  ILE B CD1 
7341 N N   . SER B 448 ? 0.4699 0.6447 0.6105 0.0244  0.0084  -0.0082 543  SER B N   
7342 C CA  . SER B 448 ? 0.4845 0.6460 0.6079 0.0264  0.0124  -0.0071 543  SER B CA  
7343 C C   . SER B 448 ? 0.4677 0.6191 0.5915 0.0257  0.0218  -0.0070 543  SER B C   
7344 O O   . SER B 448 ? 0.4380 0.5921 0.5742 0.0246  0.0261  -0.0065 543  SER B O   
7345 C CB  . SER B 448 ? 0.4692 0.6299 0.5852 0.0330  0.0108  -0.0012 543  SER B CB  
7346 O OG  . SER B 448 ? 0.4178 0.5811 0.5446 0.0371  0.0146  0.0029  543  SER B OG  
7347 N N   . ASN B 449 ? 0.4578 0.5978 0.5677 0.0262  0.0250  -0.0074 544  ASN B N   
7348 C CA  . ASN B 449 ? 0.4679 0.5975 0.5758 0.0260  0.0329  -0.0068 544  ASN B CA  
7349 C C   . ASN B 449 ? 0.4853 0.6116 0.5897 0.0316  0.0366  -0.0014 544  ASN B C   
7350 O O   . ASN B 449 ? 0.4383 0.5569 0.5312 0.0340  0.0382  0.0001  544  ASN B O   
7351 C CB  . ASN B 449 ? 0.4542 0.5740 0.5509 0.0239  0.0340  -0.0104 544  ASN B CB  
7352 C CG  . ASN B 449 ? 0.5183 0.6390 0.6198 0.0178  0.0323  -0.0163 544  ASN B CG  
7353 O OD1 . ASN B 449 ? 0.4827 0.6097 0.5967 0.0145  0.0320  -0.0173 544  ASN B OD1 
7354 N ND2 . ASN B 449 ? 0.5047 0.6188 0.5967 0.0160  0.0316  -0.0206 544  ASN B ND2 
7355 N N   . SER B 450 ? 0.4436 0.5758 0.5590 0.0332  0.0383  0.0012  545  SER B N   
7356 C CA  . SER B 450 ? 0.4591 0.5902 0.5735 0.0385  0.0409  0.0058  545  SER B CA  
7357 C C   . SER B 450 ? 0.4459 0.5772 0.5698 0.0381  0.0476  0.0068  545  SER B C   
7358 O O   . SER B 450 ? 0.4337 0.5690 0.5675 0.0340  0.0491  0.0046  545  SER B O   
7359 C CB  . SER B 450 ? 0.4536 0.5936 0.5720 0.0421  0.0348  0.0081  545  SER B CB  
7360 O OG  . SER B 450 ? 0.4436 0.5952 0.5766 0.0400  0.0315  0.0063  545  SER B OG  
7361 N N   . TYR B 451 ? 0.4128 0.5396 0.5332 0.0420  0.0520  0.0100  546  TYR B N   
7362 C CA  . TYR B 451 ? 0.4291 0.5541 0.5549 0.0415  0.0594  0.0108  546  TYR B CA  
7363 C C   . TYR B 451 ? 0.4417 0.5653 0.5663 0.0466  0.0623  0.0137  546  TYR B C   
7364 O O   . TYR B 451 ? 0.4363 0.5545 0.5508 0.0497  0.0606  0.0153  546  TYR B O   
7365 C CB  . TYR B 451 ? 0.3545 0.4688 0.4714 0.0384  0.0641  0.0103  546  TYR B CB  
7366 C CG  . TYR B 451 ? 0.4356 0.5417 0.5383 0.0399  0.0619  0.0107  546  TYR B CG  
7367 C CD1 . TYR B 451 ? 0.4325 0.5375 0.5310 0.0378  0.0576  0.0081  546  TYR B CD1 
7368 C CD2 . TYR B 451 ? 0.4029 0.5029 0.4970 0.0433  0.0643  0.0131  546  TYR B CD2 
7369 C CE1 . TYR B 451 ? 0.3995 0.4980 0.4863 0.0393  0.0562  0.0082  546  TYR B CE1 
7370 C CE2 . TYR B 451 ? 0.4329 0.5268 0.5157 0.0445  0.0624  0.0133  546  TYR B CE2 
7371 C CZ  . TYR B 451 ? 0.4312 0.5247 0.5108 0.0426  0.0586  0.0109  546  TYR B CZ  
7372 O OH  . TYR B 451 ? 0.4290 0.5173 0.4986 0.0438  0.0574  0.0109  546  TYR B OH  
7373 N N   . ASP B 452 ? 0.4311 0.5593 0.5665 0.0472  0.0671  0.0139  547  ASP B N   
7374 C CA  . ASP B 452 ? 0.4251 0.5503 0.5598 0.0513  0.0723  0.0157  547  ASP B CA  
7375 C C   . ASP B 452 ? 0.4190 0.5397 0.5529 0.0484  0.0808  0.0151  547  ASP B C   
7376 O O   . ASP B 452 ? 0.4266 0.5514 0.5684 0.0443  0.0832  0.0137  547  ASP B O   
7377 C CB  . ASP B 452 ? 0.4286 0.5641 0.5780 0.0554  0.0711  0.0163  547  ASP B CB  
7378 C CG  . ASP B 452 ? 0.5087 0.6465 0.6564 0.0595  0.0631  0.0184  547  ASP B CG  
7379 O OD1 . ASP B 452 ? 0.5001 0.6317 0.6348 0.0590  0.0593  0.0190  547  ASP B OD1 
7380 O OD2 . ASP B 452 ? 0.5419 0.6878 0.7015 0.0635  0.0609  0.0195  547  ASP B OD2 
7381 N N   . PHE B 453 ? 0.4055 0.5174 0.5289 0.0502  0.0854  0.0161  548  PHE B N   
7382 C CA  . PHE B 453 ? 0.4095 0.5172 0.5309 0.0480  0.0937  0.0159  548  PHE B CA  
7383 C C   . PHE B 453 ? 0.4266 0.5375 0.5549 0.0518  0.0987  0.0155  548  PHE B C   
7384 O O   . PHE B 453 ? 0.4397 0.5508 0.5683 0.0565  0.0959  0.0161  548  PHE B O   
7385 C CB  . PHE B 453 ? 0.3777 0.4732 0.4817 0.0470  0.0955  0.0169  548  PHE B CB  
7386 C CG  . PHE B 453 ? 0.4011 0.4921 0.4981 0.0439  0.0917  0.0173  548  PHE B CG  
7387 C CD1 . PHE B 453 ? 0.4092 0.5055 0.5130 0.0421  0.0866  0.0162  548  PHE B CD1 
7388 C CD2 . PHE B 453 ? 0.3855 0.4666 0.4688 0.0429  0.0930  0.0185  548  PHE B CD2 
7389 C CE1 . PHE B 453 ? 0.4350 0.5259 0.5322 0.0394  0.0838  0.0159  548  PHE B CE1 
7390 C CE2 . PHE B 453 ? 0.4206 0.4971 0.4984 0.0408  0.0898  0.0189  548  PHE B CE2 
7391 C CZ  . PHE B 453 ? 0.4102 0.4912 0.4950 0.0391  0.0856  0.0174  548  PHE B CZ  
7392 N N   . PHE B 454 ? 0.4008 0.5133 0.5342 0.0497  0.1066  0.0145  549  PHE B N   
7393 C CA  . PHE B 454 ? 0.4510 0.5676 0.5933 0.0529  0.1128  0.0133  549  PHE B CA  
7394 C C   . PHE B 454 ? 0.4533 0.5620 0.5856 0.0509  0.1221  0.0126  549  PHE B C   
7395 O O   . PHE B 454 ? 0.4356 0.5406 0.5618 0.0459  0.1254  0.0132  549  PHE B O   
7396 C CB  . PHE B 454 ? 0.4145 0.5451 0.5782 0.0525  0.1138  0.0120  549  PHE B CB  
7397 C CG  . PHE B 454 ? 0.4385 0.5780 0.6124 0.0548  0.1041  0.0127  549  PHE B CG  
7398 C CD1 . PHE B 454 ? 0.4315 0.5769 0.6153 0.0609  0.1013  0.0131  549  PHE B CD1 
7399 C CD2 . PHE B 454 ? 0.4096 0.5505 0.5818 0.0509  0.0976  0.0129  549  PHE B CD2 
7400 C CE1 . PHE B 454 ? 0.4637 0.6168 0.6548 0.0631  0.0918  0.0143  549  PHE B CE1 
7401 C CE2 . PHE B 454 ? 0.3936 0.5424 0.5730 0.0526  0.0885  0.0132  549  PHE B CE2 
7402 C CZ  . PHE B 454 ? 0.4383 0.5933 0.6266 0.0587  0.0853  0.0142  549  PHE B CZ  
7403 N N   . MET B 455 ? 0.4037 0.5096 0.5343 0.0549  0.1263  0.0113  550  MET B N   
7404 C CA  . MET B 455 ? 0.4466 0.5459 0.5684 0.0538  0.1357  0.0097  550  MET B CA  
7405 C C   . MET B 455 ? 0.4614 0.5677 0.5982 0.0575  0.1423  0.0070  550  MET B C   
7406 O O   . MET B 455 ? 0.4462 0.5549 0.5905 0.0631  0.1392  0.0066  550  MET B O   
7407 C CB  . MET B 455 ? 0.4136 0.5007 0.5167 0.0550  0.1344  0.0098  550  MET B CB  
7408 C CG  . MET B 455 ? 0.4365 0.5166 0.5249 0.0517  0.1285  0.0123  550  MET B CG  
7409 S SD  . MET B 455 ? 0.4459 0.5140 0.5151 0.0530  0.1264  0.0120  550  MET B SD  
7410 C CE  . MET B 455 ? 0.4305 0.4938 0.4928 0.0522  0.1372  0.0090  550  MET B CE  
7411 N N   . ARG B 456 ? 0.4303 0.5397 0.5715 0.0545  0.1517  0.0054  551  ARG B N   
7412 C CA  . ARG B 456 ? 0.4932 0.6108 0.6509 0.0578  0.1592  0.0024  551  ARG B CA  
7413 C C   . ARG B 456 ? 0.4847 0.6150 0.6642 0.0624  0.1526  0.0029  551  ARG B C   
7414 O O   . ARG B 456 ? 0.5031 0.6370 0.6936 0.0685  0.1538  0.0014  551  ARG B O   
7415 C CB  . ARG B 456 ? 0.4810 0.5901 0.6298 0.0615  0.1651  -0.0004 551  ARG B CB  
7416 C CG  . ARG B 456 ? 0.5115 0.6086 0.6381 0.0568  0.1716  -0.0013 551  ARG B CG  
7417 C CD  . ARG B 456 ? 0.5127 0.6034 0.6334 0.0597  0.1797  -0.0056 551  ARG B CD  
7418 N NE  . ARG B 456 ? 0.4904 0.5689 0.5870 0.0553  0.1835  -0.0062 551  ARG B NE  
7419 C CZ  . ARG B 456 ? 0.5250 0.6016 0.6139 0.0508  0.1932  -0.0075 551  ARG B CZ  
7420 N NH1 . ARG B 456 ? 0.5024 0.5886 0.6066 0.0498  0.2014  -0.0088 551  ARG B NH1 
7421 N NH2 . ARG B 456 ? 0.5217 0.5869 0.5869 0.0470  0.1947  -0.0074 551  ARG B NH2 
7422 N N   . GLY B 457 ? 0.4459 0.5825 0.6310 0.0596  0.1451  0.0051  552  GLY B N   
7423 C CA  . GLY B 457 ? 0.4289 0.5785 0.6338 0.0629  0.1379  0.0057  552  GLY B CA  
7424 C C   . GLY B 457 ? 0.5169 0.6640 0.7189 0.0684  0.1280  0.0078  552  GLY B C   
7425 O O   . GLY B 457 ? 0.5212 0.6789 0.7387 0.0718  0.1214  0.0088  552  GLY B O   
7426 N N   . GLU B 458 ? 0.4466 0.5804 0.6294 0.0693  0.1264  0.0087  553  GLU B N   
7427 C CA  . GLU B 458 ? 0.4791 0.6096 0.6586 0.0742  0.1182  0.0109  553  GLU B CA  
7428 C C   . GLU B 458 ? 0.4489 0.5718 0.6115 0.0708  0.1113  0.0130  553  GLU B C   
7429 O O   . GLU B 458 ? 0.4139 0.5290 0.5625 0.0663  0.1144  0.0125  553  GLU B O   
7430 C CB  . GLU B 458 ? 0.4770 0.5986 0.6515 0.0792  0.1229  0.0098  553  GLU B CB  
7431 C CG  . GLU B 458 ? 0.5540 0.6827 0.7459 0.0830  0.1310  0.0070  553  GLU B CG  
7432 C CD  . GLU B 458 ? 0.6234 0.7437 0.8133 0.0888  0.1355  0.0054  553  GLU B CD  
7433 O OE1 . GLU B 458 ? 0.6301 0.7447 0.8158 0.0926  0.1290  0.0078  553  GLU B OE1 
7434 O OE2 . GLU B 458 ? 0.5851 0.7039 0.7772 0.0891  0.1459  0.0015  553  GLU B OE2 
7435 N N   . GLU B 459 ? 0.4673 0.5928 0.6314 0.0731  0.1020  0.0154  554  GLU B N   
7436 C CA  . GLU B 459 ? 0.4996 0.6197 0.6498 0.0701  0.0954  0.0169  554  GLU B CA  
7437 C C   . GLU B 459 ? 0.4536 0.5603 0.5859 0.0704  0.0968  0.0173  554  GLU B C   
7438 O O   . GLU B 459 ? 0.4764 0.5786 0.6075 0.0747  0.0974  0.0178  554  GLU B O   
7439 C CB  . GLU B 459 ? 0.4740 0.6005 0.6300 0.0726  0.0858  0.0192  554  GLU B CB  
7440 C CG  . GLU B 459 ? 0.5467 0.6685 0.6893 0.0694  0.0795  0.0203  554  GLU B CG  
7441 C CD  . GLU B 459 ? 0.6066 0.7211 0.7390 0.0728  0.0756  0.0227  554  GLU B CD  
7442 O OE1 . GLU B 459 ? 0.6448 0.7491 0.7630 0.0713  0.0776  0.0225  554  GLU B OE1 
7443 O OE2 . GLU B 459 ? 0.6436 0.7626 0.7828 0.0770  0.0707  0.0249  554  GLU B OE2 
7444 N N   . ILE B 460 ? 0.4330 0.5333 0.5521 0.0658  0.0970  0.0171  555  ILE B N   
7445 C CA  . ILE B 460 ? 0.5011 0.5899 0.6038 0.0655  0.0978  0.0172  555  ILE B CA  
7446 C C   . ILE B 460 ? 0.4668 0.5526 0.5600 0.0638  0.0909  0.0188  555  ILE B C   
7447 O O   . ILE B 460 ? 0.4917 0.5703 0.5746 0.0646  0.0893  0.0194  555  ILE B O   
7448 C CB  . ILE B 460 ? 0.4646 0.5476 0.5587 0.0620  0.1048  0.0156  555  ILE B CB  
7449 C CG1 . ILE B 460 ? 0.4286 0.5162 0.5265 0.0577  0.1059  0.0157  555  ILE B CG1 
7450 C CG2 . ILE B 460 ? 0.5276 0.6098 0.6256 0.0642  0.1123  0.0135  555  ILE B CG2 
7451 C CD1 . ILE B 460 ? 0.5021 0.5822 0.5861 0.0537  0.1061  0.0164  555  ILE B CD1 
7452 N N   . LEU B 461 ? 0.4740 0.5654 0.5712 0.0612  0.0873  0.0190  556  LEU B N   
7453 C CA  . LEU B 461 ? 0.4565 0.5459 0.5461 0.0592  0.0816  0.0197  556  LEU B CA  
7454 C C   . LEU B 461 ? 0.4748 0.5730 0.5733 0.0594  0.0756  0.0200  556  LEU B C   
7455 O O   . LEU B 461 ? 0.4652 0.5711 0.5751 0.0582  0.0762  0.0190  556  LEU B O   
7456 C CB  . LEU B 461 ? 0.3903 0.4756 0.4732 0.0549  0.0836  0.0190  556  LEU B CB  
7457 C CG  . LEU B 461 ? 0.4531 0.5361 0.5293 0.0529  0.0786  0.0191  556  LEU B CG  
7458 C CD1 . LEU B 461 ? 0.3786 0.4541 0.4452 0.0504  0.0811  0.0193  556  LEU B CD1 
7459 C CD2 . LEU B 461 ? 0.4393 0.5292 0.5235 0.0510  0.0748  0.0181  556  LEU B CD2 
7460 N N   . SER B 462 ? 0.4281 0.5252 0.5210 0.0604  0.0699  0.0211  557  SER B N   
7461 C CA  . SER B 462 ? 0.4687 0.5733 0.5668 0.0601  0.0636  0.0212  557  SER B CA  
7462 C C   . SER B 462 ? 0.4414 0.5421 0.5287 0.0578  0.0600  0.0206  557  SER B C   
7463 O O   . SER B 462 ? 0.4380 0.5317 0.5152 0.0586  0.0606  0.0216  557  SER B O   
7464 C CB  . SER B 462 ? 0.4869 0.5954 0.5898 0.0647  0.0598  0.0236  557  SER B CB  
7465 O OG  . SER B 462 ? 0.5591 0.6765 0.6687 0.0642  0.0535  0.0237  557  SER B OG  
7466 N N   . GLY B 463 ? 0.4087 0.5138 0.4984 0.0548  0.0566  0.0188  558  GLY B N   
7467 C CA  . GLY B 463 ? 0.4293 0.5307 0.5091 0.0530  0.0538  0.0176  558  GLY B CA  
7468 C C   . GLY B 463 ? 0.4537 0.5605 0.5372 0.0497  0.0498  0.0149  558  GLY B C   
7469 O O   . GLY B 463 ? 0.4383 0.5528 0.5326 0.0488  0.0482  0.0141  558  GLY B O   
7470 N N   . SER B 464 ? 0.4279 0.5307 0.5027 0.0477  0.0483  0.0129  559  SER B N   
7471 C CA  . SER B 464 ? 0.4426 0.5494 0.5193 0.0443  0.0445  0.0094  559  SER B CA  
7472 C C   . SER B 464 ? 0.4446 0.5449 0.5117 0.0425  0.0449  0.0067  559  SER B C   
7473 O O   . SER B 464 ? 0.4445 0.5391 0.5035 0.0443  0.0469  0.0080  559  SER B O   
7474 C CB  . SER B 464 ? 0.4276 0.5425 0.5059 0.0451  0.0379  0.0098  559  SER B CB  
7475 O OG  . SER B 464 ? 0.4438 0.5558 0.5104 0.0465  0.0354  0.0109  559  SER B OG  
7476 N N   . GLN B 465 ? 0.4471 0.5486 0.5165 0.0387  0.0433  0.0027  560  GLN B N   
7477 C CA  . GLN B 465 ? 0.4495 0.5475 0.5105 0.0371  0.0419  -0.0009 560  GLN B CA  
7478 C C   . GLN B 465 ? 0.4671 0.5688 0.5205 0.0387  0.0375  -0.0001 560  GLN B C   
7479 O O   . GLN B 465 ? 0.4539 0.5629 0.5109 0.0391  0.0331  0.0013  560  GLN B O   
7480 C CB  . GLN B 465 ? 0.4536 0.5529 0.5194 0.0325  0.0404  -0.0060 560  GLN B CB  
7481 C CG  . GLN B 465 ? 0.4565 0.5516 0.5139 0.0306  0.0395  -0.0109 560  GLN B CG  
7482 C CD  . GLN B 465 ? 0.5207 0.6166 0.5827 0.0256  0.0377  -0.0167 560  GLN B CD  
7483 O OE1 . GLN B 465 ? 0.5627 0.6596 0.6345 0.0232  0.0388  -0.0169 560  GLN B OE1 
7484 N NE2 . GLN B 465 ? 0.5456 0.6407 0.6002 0.0238  0.0355  -0.0216 560  GLN B NE2 
7485 N N   . ARG B 466 ? 0.4454 0.5422 0.4887 0.0395  0.0389  -0.0006 561  ARG B N   
7486 C CA  . ARG B 466 ? 0.4232 0.5220 0.4574 0.0407  0.0358  0.0007  561  ARG B CA  
7487 C C   . ARG B 466 ? 0.4760 0.5761 0.5041 0.0374  0.0330  -0.0044 561  ARG B C   
7488 O O   . ARG B 466 ? 0.4584 0.5548 0.4869 0.0351  0.0352  -0.0093 561  ARG B O   
7489 C CB  . ARG B 466 ? 0.4465 0.5398 0.4733 0.0430  0.0396  0.0031  561  ARG B CB  
7490 C CG  . ARG B 466 ? 0.4610 0.5509 0.4926 0.0453  0.0435  0.0066  561  ARG B CG  
7491 C CD  . ARG B 466 ? 0.4337 0.5273 0.4714 0.0475  0.0419  0.0107  561  ARG B CD  
7492 N NE  . ARG B 466 ? 0.4591 0.5484 0.4981 0.0497  0.0460  0.0135  561  ARG B NE  
7493 C CZ  . ARG B 466 ? 0.4536 0.5443 0.4987 0.0517  0.0467  0.0164  561  ARG B CZ  
7494 N NH1 . ARG B 466 ? 0.4401 0.5371 0.4924 0.0523  0.0436  0.0171  561  ARG B NH1 
7495 N NH2 . ARG B 466 ? 0.4606 0.5465 0.5048 0.0532  0.0505  0.0182  561  ARG B NH2 
7496 N N   . ILE B 467 ? 0.4671 0.5719 0.4890 0.0373  0.0280  -0.0034 562  ILE B N   
7497 C CA  . ILE B 467 ? 0.4836 0.5889 0.4954 0.0344  0.0256  -0.0080 562  ILE B CA  
7498 C C   . ILE B 467 ? 0.5082 0.6068 0.5109 0.0349  0.0310  -0.0095 562  ILE B C   
7499 O O   . ILE B 467 ? 0.4693 0.5661 0.4666 0.0373  0.0329  -0.0052 562  ILE B O   
7500 C CB  . ILE B 467 ? 0.4781 0.5894 0.4833 0.0347  0.0190  -0.0051 562  ILE B CB  
7501 C CG1 . ILE B 467 ? 0.4901 0.6097 0.5069 0.0345  0.0132  -0.0040 562  ILE B CG1 
7502 C CG2 . ILE B 467 ? 0.4957 0.6070 0.4877 0.0314  0.0170  -0.0100 562  ILE B CG2 
7503 C CD1 . ILE B 467 ? 0.5105 0.6367 0.5225 0.0356  0.0056  -0.0001 562  ILE B CD1 
7504 N N   . SER B 468 ? 0.5102 0.6051 0.5120 0.0326  0.0338  -0.0158 563  SER B N   
7505 C CA  . SER B 468 ? 0.4956 0.5850 0.4913 0.0333  0.0394  -0.0179 563  SER B CA  
7506 C C   . SER B 468 ? 0.5468 0.6359 0.5317 0.0304  0.0392  -0.0240 563  SER B C   
7507 O O   . SER B 468 ? 0.5884 0.6730 0.5709 0.0303  0.0441  -0.0285 563  SER B O   
7508 C CB  . SER B 468 ? 0.5168 0.6008 0.5215 0.0342  0.0439  -0.0196 563  SER B CB  
7509 O OG  . SER B 468 ? 0.5426 0.6259 0.5529 0.0313  0.0425  -0.0244 563  SER B OG  
7510 N N   . ASP B 469 ? 0.5725 0.6665 0.5507 0.0283  0.0335  -0.0244 564  ASP B N   
7511 C CA  . ASP B 469 ? 0.5272 0.6213 0.4922 0.0252  0.0328  -0.0299 564  ASP B CA  
7512 C C   . ASP B 469 ? 0.5809 0.6786 0.5340 0.0257  0.0293  -0.0245 564  ASP B C   
7513 O O   . ASP B 469 ? 0.5749 0.6776 0.5305 0.0265  0.0231  -0.0196 564  ASP B O   
7514 C CB  . ASP B 469 ? 0.5372 0.6337 0.5040 0.0210  0.0281  -0.0363 564  ASP B CB  
7515 C CG  . ASP B 469 ? 0.6111 0.7077 0.5627 0.0174  0.0270  -0.0426 564  ASP B CG  
7516 O OD1 . ASP B 469 ? 0.6801 0.7715 0.6298 0.0156  0.0317  -0.0502 564  ASP B OD1 
7517 O OD2 . ASP B 469 ? 0.6249 0.7264 0.5660 0.0164  0.0216  -0.0399 564  ASP B OD2 
7518 N N   . VAL B 470 ? 0.5268 0.6217 0.4676 0.0255  0.0336  -0.0251 565  VAL B N   
7519 C CA  . VAL B 470 ? 0.5477 0.6440 0.4773 0.0264  0.0317  -0.0184 565  VAL B CA  
7520 C C   . VAL B 470 ? 0.5861 0.6876 0.5065 0.0241  0.0232  -0.0179 565  VAL B C   
7521 O O   . VAL B 470 ? 0.5682 0.6722 0.4857 0.0259  0.0183  -0.0103 565  VAL B O   
7522 C CB  . VAL B 470 ? 0.5478 0.6402 0.4663 0.0258  0.0390  -0.0196 565  VAL B CB  
7523 C CG1 . VAL B 470 ? 0.5623 0.6541 0.4687 0.0219  0.0406  -0.0281 565  VAL B CG1 
7524 C CG2 . VAL B 470 ? 0.5593 0.6517 0.4685 0.0270  0.0382  -0.0113 565  VAL B CG2 
7525 N N   . ASN B 471 ? 0.5747 0.6776 0.4913 0.0202  0.0209  -0.0258 566  ASN B N   
7526 C CA  . ASN B 471 ? 0.6161 0.7247 0.5238 0.0175  0.0120  -0.0260 566  ASN B CA  
7527 C C   . ASN B 471 ? 0.6208 0.7359 0.5427 0.0189  0.0042  -0.0223 566  ASN B C   
7528 O O   . ASN B 471 ? 0.6297 0.7501 0.5478 0.0199  -0.0033 -0.0164 566  ASN B O   
7529 C CB  . ASN B 471 ? 0.5799 0.6877 0.4793 0.0124  0.0121  -0.0367 566  ASN B CB  
7530 C CG  . ASN B 471 ? 0.6777 0.7801 0.5615 0.0110  0.0197  -0.0406 566  ASN B CG  
7531 O OD1 . ASN B 471 ? 0.7589 0.8567 0.6452 0.0099  0.0265  -0.0483 566  ASN B OD1 
7532 N ND2 . ASN B 471 ? 0.6451 0.7478 0.5134 0.0112  0.0189  -0.0350 566  ASN B ND2 
7533 N N   . LEU B 472 ? 0.5895 0.7045 0.5283 0.0191  0.0061  -0.0252 567  LEU B N   
7534 C CA  . LEU B 472 ? 0.6114 0.7328 0.5654 0.0206  0.0004  -0.0214 567  LEU B CA  
7535 C C   . LEU B 472 ? 0.5587 0.6807 0.5163 0.0259  0.0002  -0.0114 567  LEU B C   
7536 O O   . LEU B 472 ? 0.5627 0.6913 0.5259 0.0277  -0.0066 -0.0064 567  LEU B O   
7537 C CB  . LEU B 472 ? 0.5574 0.6770 0.5276 0.0197  0.0041  -0.0258 567  LEU B CB  
7538 C CG  . LEU B 472 ? 0.6395 0.7577 0.6083 0.0144  0.0042  -0.0359 567  LEU B CG  
7539 C CD1 . LEU B 472 ? 0.6157 0.7317 0.6013 0.0136  0.0075  -0.0387 567  LEU B CD1 
7540 C CD2 . LEU B 472 ? 0.6031 0.7293 0.5660 0.0104  -0.0052 -0.0387 567  LEU B CD2 
7541 N N   . LEU B 473 ? 0.5404 0.6555 0.4953 0.0284  0.0077  -0.0086 568  LEU B N   
7542 C CA  . LEU B 473 ? 0.5529 0.6669 0.5105 0.0330  0.0082  0.0002  568  LEU B CA  
7543 C C   . LEU B 473 ? 0.5775 0.6940 0.5230 0.0339  0.0021  0.0061  568  LEU B C   
7544 O O   . LEU B 473 ? 0.5502 0.6700 0.5018 0.0373  -0.0026 0.0128  568  LEU B O   
7545 C CB  . LEU B 473 ? 0.5557 0.6621 0.5113 0.0345  0.0171  0.0011  568  LEU B CB  
7546 C CG  . LEU B 473 ? 0.5275 0.6312 0.4860 0.0386  0.0189  0.0093  568  LEU B CG  
7547 C CD1 . LEU B 473 ? 0.4800 0.5863 0.4549 0.0414  0.0175  0.0118  568  LEU B CD1 
7548 C CD2 . LEU B 473 ? 0.5174 0.6146 0.4729 0.0390  0.0271  0.0092  568  LEU B CD2 
7549 N N   . LEU B 474 ? 0.6016 0.7163 0.5295 0.0309  0.0022  0.0039  569  LEU B N   
7550 C CA  . LEU B 474 ? 0.6155 0.7318 0.5293 0.0313  -0.0040 0.0098  569  LEU B CA  
7551 C C   . LEU B 474 ? 0.6012 0.7266 0.5197 0.0312  -0.0149 0.0107  569  LEU B C   
7552 O O   . LEU B 474 ? 0.6370 0.7651 0.5547 0.0345  -0.0212 0.0187  569  LEU B O   
7553 C CB  . LEU B 474 ? 0.6351 0.7478 0.5281 0.0274  -0.0013 0.0062  569  LEU B CB  
7554 C CG  . LEU B 474 ? 0.6698 0.7748 0.5555 0.0280  0.0082  0.0085  569  LEU B CG  
7555 C CD1 . LEU B 474 ? 0.6530 0.7554 0.5221 0.0235  0.0129  0.0016  569  LEU B CD1 
7556 C CD2 . LEU B 474 ? 0.6563 0.7587 0.5349 0.0309  0.0061  0.0192  569  LEU B CD2 
7557 N N   . GLU B 475 ? 0.6280 0.7583 0.5520 0.0275  -0.0175 0.0025  570  GLU B N   
7558 C CA  . GLU B 475 ? 0.5973 0.7377 0.5284 0.0268  -0.0280 0.0025  570  GLU B CA  
7559 C C   . GLU B 475 ? 0.6182 0.7630 0.5684 0.0319  -0.0304 0.0091  570  GLU B C   
7560 O O   . GLU B 475 ? 0.6047 0.7567 0.5577 0.0343  -0.0391 0.0145  570  GLU B O   
7561 C CB  . GLU B 475 ? 0.6130 0.7568 0.5500 0.0215  -0.0288 -0.0079 570  GLU B CB  
7562 C CG  . GLU B 475 ? 0.7670 0.9114 0.6860 0.0159  -0.0324 -0.0148 570  GLU B CG  
7563 C CD  . GLU B 475 ? 0.8558 0.9980 0.7790 0.0108  -0.0282 -0.0262 570  GLU B CD  
7564 O OE1 . GLU B 475 ? 0.8199 0.9662 0.7611 0.0098  -0.0296 -0.0292 570  GLU B OE1 
7565 O OE2 . GLU B 475 ? 0.8857 1.0213 0.7944 0.0078  -0.0230 -0.0323 570  GLU B OE2 
7566 N N   . ASN B 476 ? 0.5975 0.7383 0.5611 0.0338  -0.0226 0.0086  571  ASN B N   
7567 C CA  . ASN B 476 ? 0.6037 0.7487 0.5857 0.0383  -0.0238 0.0137  571  ASN B CA  
7568 C C   . ASN B 476 ? 0.6003 0.7420 0.5785 0.0438  -0.0243 0.0234  571  ASN B C   
7569 O O   . ASN B 476 ? 0.6096 0.7569 0.5987 0.0479  -0.0294 0.0287  571  ASN B O   
7570 C CB  . ASN B 476 ? 0.5920 0.7330 0.5873 0.0384  -0.0153 0.0104  571  ASN B CB  
7571 C CG  . ASN B 476 ? 0.5785 0.7278 0.5938 0.0389  -0.0178 0.0095  571  ASN B CG  
7572 O OD1 . ASN B 476 ? 0.6109 0.7690 0.6307 0.0362  -0.0249 0.0065  571  ASN B OD1 
7573 N ND2 . ASN B 476 ? 0.5769 0.7236 0.6043 0.0420  -0.0120 0.0119  571  ASN B ND2 
7574 N N   . ILE B 477 ? 0.6063 0.7387 0.5699 0.0439  -0.0188 0.0255  572  ILE B N   
7575 C CA  . ILE B 477 ? 0.6168 0.7445 0.5743 0.0483  -0.0191 0.0347  572  ILE B CA  
7576 C C   . ILE B 477 ? 0.6829 0.8162 0.6330 0.0495  -0.0297 0.0401  572  ILE B C   
7577 O O   . ILE B 477 ? 0.6839 0.8177 0.6393 0.0547  -0.0336 0.0481  572  ILE B O   
7578 C CB  . ILE B 477 ? 0.6267 0.7442 0.5688 0.0466  -0.0112 0.0350  572  ILE B CB  
7579 C CG1 . ILE B 477 ? 0.5665 0.6789 0.5185 0.0470  -0.0017 0.0318  572  ILE B CG1 
7580 C CG2 . ILE B 477 ? 0.6416 0.7536 0.5729 0.0496  -0.0124 0.0444  572  ILE B CG2 
7581 C CD1 . ILE B 477 ? 0.5821 0.6864 0.5215 0.0447  0.0063  0.0304  572  ILE B CD1 
7582 N N   . LYS B 478 ? 0.6611 0.7984 0.5987 0.0450  -0.0349 0.0358  573  LYS B N   
7583 C CA  . LYS B 478 ? 0.6477 0.7916 0.5780 0.0458  -0.0464 0.0405  573  LYS B CA  
7584 C C   . LYS B 478 ? 0.6952 0.8510 0.6460 0.0483  -0.0544 0.0409  573  LYS B C   
7585 O O   . LYS B 478 ? 0.6932 0.8539 0.6467 0.0525  -0.0630 0.0483  573  LYS B O   
7586 C CB  . LYS B 478 ? 0.6679 0.8130 0.5789 0.0396  -0.0495 0.0345  573  LYS B CB  
7587 C CG  . LYS B 478 ? 0.7590 0.9112 0.6594 0.0396  -0.0621 0.0389  573  LYS B CG  
7588 C CD  . LYS B 478 ? 0.8294 0.9834 0.7113 0.0326  -0.0650 0.0311  573  LYS B CD  
7589 N N   . ARG B 479 ? 0.6701 0.8306 0.6361 0.0457  -0.0517 0.0330  574  ARG B N   
7590 C CA  . ARG B 479 ? 0.6567 0.8293 0.6439 0.0471  -0.0581 0.0323  574  ARG B CA  
7591 C C   . ARG B 479 ? 0.6656 0.8385 0.6682 0.0545  -0.0573 0.0403  574  ARG B C   
7592 O O   . ARG B 479 ? 0.6494 0.8327 0.6656 0.0578  -0.0653 0.0436  574  ARG B O   
7593 C CB  . ARG B 479 ? 0.6584 0.8332 0.6577 0.0424  -0.0529 0.0226  574  ARG B CB  
7594 C CG  . ARG B 479 ? 0.7574 0.9460 0.7707 0.0394  -0.0612 0.0180  574  ARG B CG  
7595 C CD  . ARG B 479 ? 0.7645 0.9529 0.7871 0.0337  -0.0553 0.0082  574  ARG B CD  
7596 N NE  . ARG B 479 ? 0.8225 1.0110 0.8320 0.0268  -0.0582 0.0001  574  ARG B NE  
7597 C CZ  . ARG B 479 ? 0.8294 1.0077 0.8266 0.0230  -0.0507 -0.0058 574  ARG B CZ  
7598 N NH1 . ARG B 479 ? 0.6762 0.8440 0.6729 0.0254  -0.0402 -0.0046 574  ARG B NH1 
7599 N NH2 . ARG B 479 ? 0.8654 1.0443 0.8509 0.0169  -0.0540 -0.0135 574  ARG B NH2 
7600 N N   . PHE B 480 ? 0.6823 0.8442 0.6834 0.0572  -0.0478 0.0431  575  PHE B N   
7601 C CA  . PHE B 480 ? 0.6623 0.8221 0.6759 0.0640  -0.0457 0.0501  575  PHE B CA  
7602 C C   . PHE B 480 ? 0.7028 0.8563 0.7039 0.0684  -0.0491 0.0597  575  PHE B C   
7603 O O   . PHE B 480 ? 0.6945 0.8435 0.7037 0.0741  -0.0464 0.0656  575  PHE B O   
7604 C CB  . PHE B 480 ? 0.6358 0.7870 0.6550 0.0641  -0.0337 0.0474  575  PHE B CB  
7605 C CG  . PHE B 480 ? 0.6041 0.7615 0.6413 0.0622  -0.0305 0.0408  575  PHE B CG  
7606 C CD1 . PHE B 480 ? 0.6586 0.8209 0.7156 0.0665  -0.0296 0.0429  575  PHE B CD1 
7607 C CD2 . PHE B 480 ? 0.5703 0.7285 0.6049 0.0559  -0.0282 0.0327  575  PHE B CD2 
7608 C CE1 . PHE B 480 ? 0.6315 0.7996 0.7045 0.0642  -0.0261 0.0371  575  PHE B CE1 
7609 C CE2 . PHE B 480 ? 0.5806 0.7436 0.6312 0.0538  -0.0251 0.0273  575  PHE B CE2 
7610 C CZ  . PHE B 480 ? 0.5866 0.7547 0.6560 0.0577  -0.0239 0.0297  575  PHE B CZ  
7611 N N   . ASN B 481 ? 0.6947 0.8473 0.6760 0.0658  -0.0546 0.0614  576  ASN B N   
7612 C CA  . ASN B 481 ? 0.7240 0.8703 0.6913 0.0694  -0.0586 0.0713  576  ASN B CA  
7613 C C   . ASN B 481 ? 0.7356 0.8674 0.6965 0.0711  -0.0484 0.0752  576  ASN B C   
7614 O O   . ASN B 481 ? 0.7365 0.8620 0.6959 0.0761  -0.0494 0.0840  576  ASN B O   
7615 C CB  . ASN B 481 ? 0.7592 0.9132 0.7396 0.0762  -0.0684 0.0789  576  ASN B CB  
7616 C CG  . ASN B 481 ? 0.8174 0.9875 0.8073 0.0745  -0.0790 0.0749  576  ASN B CG  
7617 O OD1 . ASN B 481 ? 0.8967 1.0707 0.8717 0.0696  -0.0853 0.0721  576  ASN B OD1 
7618 N ND2 . ASN B 481 ? 0.8345 1.0142 0.8494 0.0783  -0.0808 0.0742  576  ASN B ND2 
7619 N N   . LEU B 482 ? 0.7343 0.8606 0.6920 0.0668  -0.0386 0.0685  577  LEU B N   
7620 C CA  . LEU B 482 ? 0.7393 0.8529 0.6912 0.0675  -0.0292 0.0713  577  LEU B CA  
7621 C C   . LEU B 482 ? 0.7434 0.8497 0.6712 0.0637  -0.0276 0.0734  577  LEU B C   
7622 O O   . LEU B 482 ? 0.7338 0.8443 0.6489 0.0596  -0.0317 0.0702  577  LEU B O   
7623 C CB  . LEU B 482 ? 0.6881 0.7999 0.6502 0.0654  -0.0196 0.0638  577  LEU B CB  
7624 C CG  . LEU B 482 ? 0.7192 0.8364 0.7040 0.0692  -0.0195 0.0627  577  LEU B CG  
7625 C CD1 . LEU B 482 ? 0.6541 0.7680 0.6466 0.0671  -0.0100 0.0563  577  LEU B CD1 
7626 C CD2 . LEU B 482 ? 0.7203 0.8335 0.7115 0.0758  -0.0209 0.0711  577  LEU B CD2 
7627 N N   . ASP B 483 ? 0.7604 0.8555 0.6820 0.0648  -0.0211 0.0785  578  ASP B N   
7628 C CA  . ASP B 483 ? 0.8155 0.9026 0.7149 0.0613  -0.0180 0.0815  578  ASP B CA  
7629 C C   . ASP B 483 ? 0.7650 0.8495 0.6609 0.0561  -0.0080 0.0732  578  ASP B C   
7630 O O   . ASP B 483 ? 0.7598 0.8379 0.6616 0.0564  0.0001  0.0728  578  ASP B O   
7631 C CB  . ASP B 483 ? 0.8382 0.9144 0.7336 0.0649  -0.0161 0.0916  578  ASP B CB  
7632 C CG  . ASP B 483 ? 0.8883 0.9564 0.7602 0.0611  -0.0134 0.0960  578  ASP B CG  
7633 O OD1 . ASP B 483 ? 0.8669 0.9365 0.7268 0.0554  -0.0098 0.0899  578  ASP B OD1 
7634 O OD2 . ASP B 483 ? 0.9662 1.0257 0.8318 0.0638  -0.0144 0.1058  578  ASP B OD2 
7635 N N   . ALA B 484 ? 0.7560 0.8453 0.6422 0.0513  -0.0089 0.0664  579  ALA B N   
7636 C CA  . ALA B 484 ? 0.7534 0.8410 0.6374 0.0468  0.0002  0.0581  579  ALA B CA  
7637 C C   . ALA B 484 ? 0.7962 0.8742 0.6700 0.0451  0.0089  0.0613  579  ALA B C   
7638 O O   . ALA B 484 ? 0.7579 0.8337 0.6369 0.0434  0.0172  0.0562  579  ALA B O   
7639 C CB  . ALA B 484 ? 0.7322 0.8251 0.6049 0.0420  -0.0023 0.0509  579  ALA B CB  
7640 N N   . ASN B 485 ? 0.7823 0.8546 0.6419 0.0456  0.0070  0.0700  580  ASN B N   
7641 C CA  . ASN B 485 ? 0.8023 0.8654 0.6526 0.0433  0.0158  0.0731  580  ASN B CA  
7642 C C   . ASN B 485 ? 0.7933 0.8512 0.6590 0.0460  0.0213  0.0748  580  ASN B C   
7643 O O   . ASN B 485 ? 0.8027 0.8559 0.6673 0.0432  0.0300  0.0732  580  ASN B O   
7644 C CB  . ASN B 485 ? 0.8603 0.9175 0.6917 0.0430  0.0126  0.0828  580  ASN B CB  
7645 C CG  . ASN B 485 ? 0.9073 0.9664 0.7177 0.0379  0.0126  0.0799  580  ASN B CG  
7646 O OD1 . ASN B 485 ? 0.9428 1.0059 0.7430 0.0381  0.0037  0.0820  580  ASN B OD1 
7647 N ND2 . ASN B 485 ? 1.0063 1.0632 0.8104 0.0332  0.0226  0.0745  580  ASN B ND2 
7648 N N   . LYS B 486 ? 0.7844 0.8437 0.6648 0.0511  0.0164  0.0776  581  LYS B N   
7649 C CA  . LYS B 486 ? 0.7984 0.8531 0.6936 0.0536  0.0213  0.0781  581  LYS B CA  
7650 C C   . LYS B 486 ? 0.7666 0.8261 0.6747 0.0522  0.0260  0.0687  581  LYS B C   
7651 O O   . LYS B 486 ? 0.7691 0.8251 0.6883 0.0536  0.0304  0.0681  581  LYS B O   
7652 C CB  . LYS B 486 ? 0.8245 0.8791 0.7309 0.0598  0.0148  0.0840  581  LYS B CB  
7653 C CG  . LYS B 486 ? 0.8932 0.9410 0.7884 0.0621  0.0104  0.0946  581  LYS B CG  
7654 C CD  . LYS B 486 ? 0.9524 1.0001 0.8608 0.0690  0.0044  0.1002  581  LYS B CD  
7655 C CE  . LYS B 486 ? 1.0164 1.0554 0.9140 0.0718  0.0003  0.1117  581  LYS B CE  
7656 N NZ  . LYS B 486 ? 1.0355 1.0748 0.9475 0.0794  -0.0057 0.1170  581  LYS B NZ  
7657 N N   . LEU B 487 ? 0.7036 0.7703 0.6100 0.0496  0.0250  0.0615  582  LEU B N   
7658 C CA  . LEU B 487 ? 0.6738 0.7443 0.5918 0.0485  0.0290  0.0532  582  LEU B CA  
7659 C C   . LEU B 487 ? 0.6544 0.7255 0.5640 0.0438  0.0347  0.0469  582  LEU B C   
7660 O O   . LEU B 487 ? 0.6199 0.6944 0.5376 0.0429  0.0373  0.0397  582  LEU B O   
7661 C CB  . LEU B 487 ? 0.6522 0.7308 0.5805 0.0502  0.0227  0.0496  582  LEU B CB  
7662 C CG  . LEU B 487 ? 0.6651 0.7449 0.6070 0.0551  0.0185  0.0539  582  LEU B CG  
7663 C CD1 . LEU B 487 ? 0.6054 0.6943 0.5535 0.0563  0.0104  0.0523  582  LEU B CD1 
7664 C CD2 . LEU B 487 ? 0.5995 0.6771 0.5549 0.0563  0.0243  0.0512  582  LEU B CD2 
7665 N N   . ASN B 488 ? 0.6332 0.7007 0.5273 0.0410  0.0374  0.0496  583  ASN B N   
7666 C CA  . ASN B 488 ? 0.6393 0.7087 0.5240 0.0368  0.0419  0.0431  583  ASN B CA  
7667 C C   . ASN B 488 ? 0.6341 0.7037 0.5288 0.0357  0.0497  0.0370  583  ASN B C   
7668 O O   . ASN B 488 ? 0.6281 0.7017 0.5254 0.0343  0.0514  0.0293  583  ASN B O   
7669 C CB  . ASN B 488 ? 0.7456 0.8108 0.6110 0.0338  0.0440  0.0477  583  ASN B CB  
7670 C CG  . ASN B 488 ? 0.8083 0.8663 0.6734 0.0334  0.0502  0.0534  583  ASN B CG  
7671 O OD1 . ASN B 488 ? 0.8296 0.8834 0.7017 0.0365  0.0481  0.0594  583  ASN B OD1 
7672 N ND2 . ASN B 488 ? 0.8322 0.8888 0.6902 0.0293  0.0584  0.0508  583  ASN B ND2 
7673 N N   . PHE B 489 ? 0.6175 0.6827 0.5190 0.0365  0.0540  0.0403  584  PHE B N   
7674 C CA  . PHE B 489 ? 0.6788 0.7450 0.5907 0.0358  0.0603  0.0349  584  PHE B CA  
7675 C C   . PHE B 489 ? 0.6184 0.6889 0.5433 0.0380  0.0576  0.0296  584  PHE B C   
7676 O O   . PHE B 489 ? 0.6092 0.6827 0.5376 0.0369  0.0605  0.0228  584  PHE B O   
7677 C CB  . PHE B 489 ? 0.6211 0.6821 0.5382 0.0361  0.0641  0.0394  584  PHE B CB  
7678 C CG  . PHE B 489 ? 0.8024 0.8589 0.7076 0.0328  0.0688  0.0435  584  PHE B CG  
7679 C CD1 . PHE B 489 ? 0.7706 0.8292 0.6730 0.0291  0.0760  0.0393  584  PHE B CD1 
7680 C CD2 . PHE B 489 ? 0.8192 0.8695 0.7160 0.0334  0.0661  0.0519  584  PHE B CD2 
7681 C CE1 . PHE B 489 ? 0.8336 0.8882 0.7247 0.0255  0.0811  0.0431  584  PHE B CE1 
7682 C CE2 . PHE B 489 ? 0.8242 0.8695 0.7089 0.0299  0.0708  0.0563  584  PHE B CE2 
7683 C CZ  . PHE B 489 ? 0.8277 0.8753 0.7094 0.0257  0.0785  0.0519  584  PHE B CZ  
7684 N N   . TYR B 490 ? 0.5785 0.6492 0.5104 0.0411  0.0521  0.0326  585  TYR B N   
7685 C CA  . TYR B 490 ? 0.5733 0.6479 0.5167 0.0426  0.0496  0.0281  585  TYR B CA  
7686 C C   . TYR B 490 ? 0.5369 0.6160 0.4760 0.0407  0.0475  0.0223  585  TYR B C   
7687 O O   . TYR B 490 ? 0.5157 0.5963 0.4608 0.0401  0.0498  0.0161  585  TYR B O   
7688 C CB  . TYR B 490 ? 0.5409 0.6158 0.4916 0.0460  0.0443  0.0325  585  TYR B CB  
7689 C CG  . TYR B 490 ? 0.5010 0.5806 0.4623 0.0472  0.0410  0.0288  585  TYR B CG  
7690 C CD1 . TYR B 490 ? 0.4806 0.5598 0.4530 0.0480  0.0439  0.0259  585  TYR B CD1 
7691 C CD2 . TYR B 490 ? 0.5150 0.5995 0.4753 0.0474  0.0346  0.0286  585  TYR B CD2 
7692 C CE1 . TYR B 490 ? 0.4664 0.5494 0.4483 0.0487  0.0414  0.0231  585  TYR B CE1 
7693 C CE2 . TYR B 490 ? 0.4712 0.5603 0.4423 0.0479  0.0318  0.0253  585  TYR B CE2 
7694 C CZ  . TYR B 490 ? 0.4801 0.5680 0.4618 0.0485  0.0357  0.0227  585  TYR B CZ  
7695 O OH  . TYR B 490 ? 0.4672 0.5591 0.4590 0.0486  0.0336  0.0198  585  TYR B OH  
7696 N N   . ILE B 491 ? 0.5405 0.6208 0.4681 0.0397  0.0431  0.0242  586  ILE B N   
7697 C CA  . ILE B 491 ? 0.5834 0.6678 0.5057 0.0373  0.0405  0.0181  586  ILE B CA  
7698 C C   . ILE B 491 ? 0.5805 0.6638 0.4984 0.0346  0.0476  0.0117  586  ILE B C   
7699 O O   . ILE B 491 ? 0.5254 0.6106 0.4474 0.0336  0.0484  0.0045  586  ILE B O   
7700 C CB  . ILE B 491 ? 0.6002 0.6860 0.5087 0.0363  0.0344  0.0217  586  ILE B CB  
7701 C CG1 . ILE B 491 ? 0.5797 0.6687 0.4956 0.0394  0.0263  0.0265  586  ILE B CG1 
7702 C CG2 . ILE B 491 ? 0.5405 0.6293 0.4390 0.0327  0.0334  0.0145  586  ILE B CG2 
7703 C CD1 . ILE B 491 ? 0.5814 0.6704 0.4842 0.0397  0.0202  0.0331  586  ILE B CD1 
7704 N N   . ASP B 492 ? 0.5612 0.6415 0.4722 0.0335  0.0532  0.0142  587  ASP B N   
7705 C CA  . ASP B 492 ? 0.5814 0.6617 0.4883 0.0310  0.0603  0.0081  587  ASP B CA  
7706 C C   . ASP B 492 ? 0.5839 0.6649 0.5060 0.0325  0.0641  0.0032  587  ASP B C   
7707 O O   . ASP B 492 ? 0.5294 0.6114 0.4519 0.0314  0.0685  -0.0036 587  ASP B O   
7708 C CB  . ASP B 492 ? 0.6270 0.7044 0.5240 0.0292  0.0656  0.0124  587  ASP B CB  
7709 C CG  . ASP B 492 ? 0.7298 0.8082 0.6195 0.0261  0.0728  0.0063  587  ASP B CG  
7710 O OD1 . ASP B 492 ? 0.7397 0.8183 0.6368 0.0260  0.0796  0.0046  587  ASP B OD1 
7711 O OD2 . ASP B 492 ? 0.7662 0.8455 0.6431 0.0238  0.0716  0.0029  587  ASP B OD2 
7712 N N   . SER B 493 ? 0.4734 0.5536 0.4076 0.0353  0.0623  0.0065  588  SER B N   
7713 C CA  . SER B 493 ? 0.5258 0.6064 0.4733 0.0368  0.0651  0.0025  588  SER B CA  
7714 C C   . SER B 493 ? 0.4827 0.5648 0.4347 0.0368  0.0628  -0.0036 588  SER B C   
7715 O O   . SER B 493 ? 0.4642 0.5458 0.4255 0.0379  0.0654  -0.0073 588  SER B O   
7716 C CB  . SER B 493 ? 0.5271 0.6062 0.4846 0.0392  0.0636  0.0073  588  SER B CB  
7717 O OG  . SER B 493 ? 0.4636 0.5435 0.4257 0.0407  0.0579  0.0085  588  SER B OG  
7718 N N   . PHE B 494 ? 0.4866 0.5701 0.4323 0.0356  0.0578  -0.0045 589  PHE B N   
7719 C CA  . PHE B 494 ? 0.5072 0.5915 0.4564 0.0347  0.0558  -0.0109 589  PHE B CA  
7720 C C   . PHE B 494 ? 0.5280 0.6124 0.4673 0.0319  0.0587  -0.0178 589  PHE B C   
7721 O O   . PHE B 494 ? 0.5549 0.6389 0.4968 0.0308  0.0579  -0.0242 589  PHE B O   
7722 C CB  . PHE B 494 ? 0.4730 0.5601 0.4232 0.0345  0.0482  -0.0089 589  PHE B CB  
7723 C CG  . PHE B 494 ? 0.4864 0.5738 0.4476 0.0373  0.0458  -0.0033 589  PHE B CG  
7724 C CD1 . PHE B 494 ? 0.4732 0.5608 0.4464 0.0380  0.0448  -0.0052 589  PHE B CD1 
7725 C CD2 . PHE B 494 ? 0.4633 0.5500 0.4224 0.0391  0.0450  0.0039  589  PHE B CD2 
7726 C CE1 . PHE B 494 ? 0.4899 0.5778 0.4724 0.0404  0.0434  -0.0004 589  PHE B CE1 
7727 C CE2 . PHE B 494 ? 0.4881 0.5746 0.4571 0.0418  0.0434  0.0084  589  PHE B CE2 
7728 C CZ  . PHE B 494 ? 0.4593 0.5468 0.4398 0.0424  0.0428  0.0061  589  PHE B CZ  
7729 N N   . ALA B 495 ? 0.4906 0.5748 0.4183 0.0305  0.0624  -0.0170 590  ALA B N   
7730 C CA  . ALA B 495 ? 0.5763 0.6606 0.4917 0.0274  0.0649  -0.0234 590  ALA B CA  
7731 C C   . ALA B 495 ? 0.5508 0.6338 0.4717 0.0277  0.0724  -0.0309 590  ALA B C   
7732 O O   . ALA B 495 ? 0.5759 0.6586 0.4876 0.0252  0.0755  -0.0376 590  ALA B O   
7733 C CB  . ALA B 495 ? 0.5566 0.6410 0.4559 0.0253  0.0664  -0.0193 590  ALA B CB  
7734 N N   . TYR B 496 ? 0.4838 0.5662 0.4191 0.0306  0.0754  -0.0301 591  TYR B N   
7735 C CA  . TYR B 496 ? 0.5025 0.5841 0.4453 0.0318  0.0819  -0.0365 591  TYR B CA  
7736 C C   . TYR B 496 ? 0.5029 0.5823 0.4602 0.0345  0.0797  -0.0381 591  TYR B C   
7737 O O   . TYR B 496 ? 0.4732 0.5522 0.4421 0.0373  0.0828  -0.0378 591  TYR B O   
7738 C CB  . TYR B 496 ? 0.5176 0.6011 0.4637 0.0329  0.0880  -0.0338 591  TYR B CB  
7739 C CG  . TYR B 496 ? 0.5567 0.6414 0.4892 0.0302  0.0890  -0.0289 591  TYR B CG  
7740 C CD1 . TYR B 496 ? 0.6086 0.6938 0.5272 0.0271  0.0934  -0.0327 591  TYR B CD1 
7741 C CD2 . TYR B 496 ? 0.5290 0.6134 0.4619 0.0307  0.0857  -0.0204 591  TYR B CD2 
7742 C CE1 . TYR B 496 ? 0.6371 0.7224 0.5420 0.0244  0.0944  -0.0275 591  TYR B CE1 
7743 C CE2 . TYR B 496 ? 0.6010 0.6850 0.5214 0.0283  0.0865  -0.0153 591  TYR B CE2 
7744 C CZ  . TYR B 496 ? 0.6569 0.7413 0.5632 0.0251  0.0908  -0.0185 591  TYR B CZ  
7745 O OH  . TYR B 496 ? 0.6565 0.7397 0.5494 0.0226  0.0917  -0.0125 591  TYR B OH  
7746 N N   . SER B 497 ? 0.4658 0.5439 0.4223 0.0332  0.0740  -0.0393 592  SER B N   
7747 C CA  . SER B 497 ? 0.4802 0.5557 0.4485 0.0346  0.0713  -0.0403 592  SER B CA  
7748 C C   . SER B 497 ? 0.4914 0.5679 0.4672 0.0366  0.0676  -0.0323 592  SER B C   
7749 O O   . SER B 497 ? 0.4423 0.5205 0.4171 0.0377  0.0685  -0.0268 592  SER B O   
7750 C CB  . SER B 497 ? 0.5069 0.5789 0.4851 0.0370  0.0763  -0.0452 592  SER B CB  
7751 O OG  . SER B 497 ? 0.5196 0.5926 0.5069 0.0404  0.0782  -0.0403 592  SER B OG  
7752 N N   . SER B 498 ? 0.4897 0.5646 0.4728 0.0367  0.0638  -0.0322 593  SER B N   
7753 C CA  . SER B 498 ? 0.4899 0.5655 0.4801 0.0382  0.0607  -0.0256 593  SER B CA  
7754 C C   . SER B 498 ? 0.5101 0.5821 0.5106 0.0387  0.0602  -0.0272 593  SER B C   
7755 O O   . SER B 498 ? 0.4813 0.5520 0.4820 0.0363  0.0584  -0.0318 593  SER B O   
7756 C CB  . SER B 498 ? 0.4714 0.5509 0.4562 0.0367  0.0553  -0.0219 593  SER B CB  
7757 O OG  . SER B 498 ? 0.4639 0.5440 0.4559 0.0385  0.0532  -0.0161 593  SER B OG  
7758 N N   . TYR B 499 ? 0.4529 0.5227 0.4611 0.0414  0.0617  -0.0236 594  TYR B N   
7759 C CA  . TYR B 499 ? 0.4657 0.5315 0.4827 0.0419  0.0612  -0.0236 594  TYR B CA  
7760 C C   . TYR B 499 ? 0.4734 0.5415 0.4923 0.0400  0.0571  -0.0210 594  TYR B C   
7761 O O   . TYR B 499 ? 0.4680 0.5405 0.4839 0.0400  0.0548  -0.0171 594  TYR B O   
7762 C CB  . TYR B 499 ? 0.4847 0.5483 0.5076 0.0451  0.0631  -0.0194 594  TYR B CB  
7763 C CG  . TYR B 499 ? 0.5180 0.5808 0.5420 0.0474  0.0668  -0.0214 594  TYR B CG  
7764 C CD1 . TYR B 499 ? 0.4917 0.5497 0.5213 0.0489  0.0689  -0.0251 594  TYR B CD1 
7765 C CD2 . TYR B 499 ? 0.4944 0.5613 0.5151 0.0483  0.0683  -0.0194 594  TYR B CD2 
7766 C CE1 . TYR B 499 ? 0.5243 0.5826 0.5568 0.0516  0.0723  -0.0271 594  TYR B CE1 
7767 C CE2 . TYR B 499 ? 0.5358 0.6034 0.5592 0.0503  0.0719  -0.0215 594  TYR B CE2 
7768 C CZ  . TYR B 499 ? 0.5378 0.6016 0.5676 0.0522  0.0738  -0.0253 594  TYR B CZ  
7769 O OH  . TYR B 499 ? 0.6222 0.6877 0.6565 0.0547  0.0773  -0.0274 594  TYR B OH  
7770 N N   . PRO B 500 ? 0.5074 0.5724 0.5321 0.0383  0.0564  -0.0232 595  PRO B N   
7771 C CA  . PRO B 500 ? 0.4713 0.5390 0.5006 0.0368  0.0534  -0.0202 595  PRO B CA  
7772 C C   . PRO B 500 ? 0.4786 0.5461 0.5113 0.0395  0.0545  -0.0138 595  PRO B C   
7773 O O   . PRO B 500 ? 0.4493 0.5121 0.4843 0.0415  0.0572  -0.0123 595  PRO B O   
7774 C CB  . PRO B 500 ? 0.4784 0.5413 0.5138 0.0342  0.0539  -0.0241 595  PRO B CB  
7775 C CG  . PRO B 500 ? 0.5009 0.5573 0.5352 0.0353  0.0572  -0.0286 595  PRO B CG  
7776 C CD  . PRO B 500 ? 0.4761 0.5347 0.5039 0.0379  0.0588  -0.0284 595  PRO B CD  
7777 N N   . HIS B 501 ? 0.4525 0.5250 0.4850 0.0397  0.0522  -0.0100 596  HIS B N   
7778 C CA  . HIS B 501 ? 0.4548 0.5269 0.4893 0.0421  0.0536  -0.0046 596  HIS B CA  
7779 C C   . HIS B 501 ? 0.4537 0.5305 0.4924 0.0417  0.0515  -0.0018 596  HIS B C   
7780 O O   . HIS B 501 ? 0.4348 0.5165 0.4746 0.0399  0.0482  -0.0034 596  HIS B O   
7781 C CB  . HIS B 501 ? 0.4787 0.5512 0.5072 0.0444  0.0548  -0.0026 596  HIS B CB  
7782 C CG  . HIS B 501 ? 0.4673 0.5441 0.4896 0.0441  0.0525  -0.0021 596  HIS B CG  
7783 N ND1 . HIS B 501 ? 0.4460 0.5240 0.4624 0.0425  0.0517  -0.0061 596  HIS B ND1 
7784 C CD2 . HIS B 501 ? 0.4159 0.4952 0.4361 0.0453  0.0511  0.0020  596  HIS B CD2 
7785 C CE1 . HIS B 501 ? 0.4460 0.5273 0.4562 0.0425  0.0495  -0.0038 596  HIS B CE1 
7786 N NE2 . HIS B 501 ? 0.4068 0.4887 0.4196 0.0444  0.0491  0.0013  596  HIS B NE2 
7787 N N   . SER B 502 ? 0.4272 0.5028 0.4687 0.0433  0.0534  0.0021  597  SER B N   
7788 C CA  . SER B 502 ? 0.4433 0.5230 0.4895 0.0437  0.0526  0.0050  597  SER B CA  
7789 C C   . SER B 502 ? 0.4382 0.5158 0.4819 0.0464  0.0547  0.0088  597  SER B C   
7790 O O   . SER B 502 ? 0.4243 0.4978 0.4635 0.0474  0.0565  0.0091  597  SER B O   
7791 C CB  . SER B 502 ? 0.4341 0.5136 0.4883 0.0416  0.0540  0.0045  597  SER B CB  
7792 O OG  . SER B 502 ? 0.4275 0.5011 0.4811 0.0424  0.0578  0.0066  597  SER B OG  
7793 N N   . GLY B 503 ? 0.4228 0.5036 0.4705 0.0476  0.0546  0.0113  598  GLY B N   
7794 C CA  . GLY B 503 ? 0.4164 0.4943 0.4620 0.0498  0.0571  0.0143  598  GLY B CA  
7795 C C   . GLY B 503 ? 0.4536 0.5345 0.5057 0.0509  0.0580  0.0162  598  GLY B C   
7796 O O   . GLY B 503 ? 0.4196 0.5059 0.4791 0.0500  0.0567  0.0154  598  GLY B O   
7797 N N   . CYS B 504 ? 0.4386 0.5164 0.4885 0.0528  0.0605  0.0182  599  CYS B N   
7798 C CA  . CYS B 504 ? 0.4486 0.5284 0.5046 0.0544  0.0626  0.0196  599  CYS B CA  
7799 C C   . CYS B 504 ? 0.4741 0.5496 0.5258 0.0567  0.0644  0.0214  599  CYS B C   
7800 O O   . CYS B 504 ? 0.4558 0.5265 0.5001 0.0564  0.0650  0.0214  599  CYS B O   
7801 C CB  . CYS B 504 ? 0.4303 0.5093 0.4903 0.0527  0.0665  0.0189  599  CYS B CB  
7802 S SG  . CYS B 504 ? 0.4982 0.5690 0.5495 0.0516  0.0699  0.0191  599  CYS B SG  
7803 N N   . GLY B 505 ? 0.4240 0.5017 0.4815 0.0591  0.0652  0.0225  600  GLY B N   
7804 C CA  . GLY B 505 ? 0.4495 0.5225 0.5045 0.0614  0.0675  0.0238  600  GLY B CA  
7805 C C   . GLY B 505 ? 0.4702 0.5434 0.5311 0.0624  0.0722  0.0231  600  GLY B C   
7806 O O   . GLY B 505 ? 0.4041 0.4834 0.4744 0.0626  0.0726  0.0227  600  GLY B O   
7807 N N   . ILE B 506 ? 0.4435 0.5101 0.4989 0.0626  0.0760  0.0226  601  ILE B N   
7808 C CA  . ILE B 506 ? 0.4456 0.5106 0.5031 0.0628  0.0817  0.0212  601  ILE B CA  
7809 C C   . ILE B 506 ? 0.4644 0.5236 0.5196 0.0651  0.0843  0.0209  601  ILE B C   
7810 O O   . ILE B 506 ? 0.4457 0.4991 0.4926 0.0643  0.0834  0.0209  601  ILE B O   
7811 C CB  . ILE B 506 ? 0.4225 0.4839 0.4725 0.0594  0.0842  0.0200  601  ILE B CB  
7812 C CG1 . ILE B 506 ? 0.4432 0.5088 0.4960 0.0570  0.0824  0.0201  601  ILE B CG1 
7813 C CG2 . ILE B 506 ? 0.4970 0.5555 0.5463 0.0593  0.0906  0.0184  601  ILE B CG2 
7814 C CD1 . ILE B 506 ? 0.4387 0.4994 0.4820 0.0545  0.0816  0.0202  601  ILE B CD1 
7815 N N   . GLY B 507 ? 0.4469 0.5075 0.5100 0.0677  0.0879  0.0202  602  GLY B N   
7816 C CA  . GLY B 507 ? 0.4503 0.5036 0.5103 0.0696  0.0912  0.0193  602  GLY B CA  
7817 C C   . GLY B 507 ? 0.4846 0.5319 0.5366 0.0673  0.0969  0.0161  602  GLY B C   
7818 O O   . GLY B 507 ? 0.4534 0.5032 0.5084 0.0667  0.1015  0.0145  602  GLY B O   
7819 N N   . LEU B 508 ? 0.4790 0.5187 0.5207 0.0656  0.0969  0.0150  603  LEU B N   
7820 C CA  . LEU B 508 ? 0.4965 0.5310 0.5287 0.0628  0.1012  0.0120  603  LEU B CA  
7821 C C   . LEU B 508 ? 0.5076 0.5394 0.5428 0.0646  0.1082  0.0090  603  LEU B C   
7822 O O   . LEU B 508 ? 0.4989 0.5315 0.5321 0.0631  0.1130  0.0072  603  LEU B O   
7823 C CB  . LEU B 508 ? 0.4753 0.5032 0.4971 0.0605  0.0988  0.0112  603  LEU B CB  
7824 C CG  . LEU B 508 ? 0.5249 0.5462 0.5361 0.0578  0.1026  0.0075  603  LEU B CG  
7825 C CD1 . LEU B 508 ? 0.4995 0.5228 0.5040 0.0548  0.1031  0.0076  603  LEU B CD1 
7826 C CD2 . LEU B 508 ? 0.4541 0.4698 0.4579 0.0556  0.0997  0.0065  603  LEU B CD2 
7827 N N   . GLU B 509 ? 0.4775 0.5054 0.5172 0.0680  0.1094  0.0083  604  GLU B N   
7828 C CA  . GLU B 509 ? 0.4873 0.5119 0.5305 0.0702  0.1165  0.0048  604  GLU B CA  
7829 C C   . GLU B 509 ? 0.4950 0.5281 0.5499 0.0722  0.1202  0.0049  604  GLU B C   
7830 O O   . GLU B 509 ? 0.4524 0.4844 0.5072 0.0720  0.1275  0.0014  604  GLU B O   
7831 C CB  . GLU B 509 ? 0.4814 0.5003 0.5297 0.0743  0.1164  0.0050  604  GLU B CB  
7832 C CG  . GLU B 509 ? 0.5013 0.5112 0.5390 0.0717  0.1137  0.0046  604  GLU B CG  
7833 C CD  . GLU B 509 ? 0.5285 0.5414 0.5667 0.0714  0.1062  0.0095  604  GLU B CD  
7834 O OE1 . GLU B 509 ? 0.5180 0.5241 0.5516 0.0705  0.1042  0.0100  604  GLU B OE1 
7835 O OE2 . GLU B 509 ? 0.5065 0.5282 0.5497 0.0719  0.1026  0.0125  604  GLU B OE2 
7836 N N   . ARG B 510 ? 0.4893 0.5311 0.5540 0.0736  0.1155  0.0085  605  ARG B N   
7837 C CA  . ARG B 510 ? 0.4772 0.5283 0.5549 0.0751  0.1183  0.0085  605  ARG B CA  
7838 C C   . ARG B 510 ? 0.4865 0.5403 0.5592 0.0704  0.1215  0.0076  605  ARG B C   
7839 O O   . ARG B 510 ? 0.4982 0.5562 0.5778 0.0705  0.1279  0.0057  605  ARG B O   
7840 C CB  . ARG B 510 ? 0.5337 0.5934 0.6231 0.0777  0.1114  0.0124  605  ARG B CB  
7841 C CG  . ARG B 510 ? 0.6358 0.7062 0.7421 0.0800  0.1141  0.0121  605  ARG B CG  
7842 C CD  . ARG B 510 ? 0.7129 0.7923 0.8305 0.0825  0.1063  0.0157  605  ARG B CD  
7843 N NE  . ARG B 510 ? 0.8143 0.8908 0.9366 0.0880  0.1036  0.0177  605  ARG B NE  
7844 C CZ  . ARG B 510 ? 0.8263 0.9086 0.9563 0.0910  0.0963  0.0215  605  ARG B CZ  
7845 N NH1 . ARG B 510 ? 0.8488 0.9266 0.9810 0.0960  0.0937  0.0240  605  ARG B NH1 
7846 N NH2 . ARG B 510 ? 0.7975 0.8897 0.9324 0.0889  0.0913  0.0228  605  ARG B NH2 
7847 N N   . VAL B 511 ? 0.4938 0.5453 0.5553 0.0664  0.1173  0.0091  606  VAL B N   
7848 C CA  . VAL B 511 ? 0.4971 0.5487 0.5516 0.0620  0.1203  0.0087  606  VAL B CA  
7849 C C   . VAL B 511 ? 0.4902 0.5355 0.5360 0.0607  0.1282  0.0052  606  VAL B C   
7850 O O   . VAL B 511 ? 0.4937 0.5412 0.5405 0.0589  0.1344  0.0042  606  VAL B O   
7851 C CB  . VAL B 511 ? 0.4836 0.5323 0.5271 0.0588  0.1143  0.0109  606  VAL B CB  
7852 C CG1 . VAL B 511 ? 0.4477 0.4940 0.4818 0.0546  0.1177  0.0110  606  VAL B CG1 
7853 C CG2 . VAL B 511 ? 0.5184 0.5738 0.5701 0.0593  0.1079  0.0137  606  VAL B CG2 
7854 N N   . LEU B 512 ? 0.5035 0.5407 0.5401 0.0612  0.1282  0.0031  607  LEU B N   
7855 C CA  . LEU B 512 ? 0.4803 0.5109 0.5069 0.0595  0.1356  -0.0010 607  LEU B CA  
7856 C C   . LEU B 512 ? 0.5015 0.5349 0.5393 0.0625  0.1439  -0.0040 607  LEU B C   
7857 O O   . LEU B 512 ? 0.5115 0.5444 0.5452 0.0604  0.1516  -0.0064 607  LEU B O   
7858 C CB  . LEU B 512 ? 0.4996 0.5211 0.5154 0.0592  0.1335  -0.0033 607  LEU B CB  
7859 C CG  . LEU B 512 ? 0.5371 0.5507 0.5399 0.0568  0.1401  -0.0083 607  LEU B CG  
7860 C CD1 . LEU B 512 ? 0.4562 0.4699 0.4468 0.0521  0.1419  -0.0075 607  LEU B CD1 
7861 C CD2 . LEU B 512 ? 0.4806 0.4858 0.4741 0.0558  0.1368  -0.0106 607  LEU B CD2 
7862 N N   . MET B 513 ? 0.4740 0.5106 0.5263 0.0677  0.1426  -0.0037 608  MET B N   
7863 C CA  . MET B 513 ? 0.4986 0.5389 0.5646 0.0716  0.1500  -0.0064 608  MET B CA  
7864 C C   . MET B 513 ? 0.4964 0.5466 0.5715 0.0700  0.1542  -0.0057 608  MET B C   
7865 O O   . MET B 513 ? 0.5299 0.5810 0.6073 0.0698  0.1636  -0.0092 608  MET B O   
7866 C CB  . MET B 513 ? 0.4656 0.5086 0.5465 0.0776  0.1457  -0.0046 608  MET B CB  
7867 C CG  . MET B 513 ? 0.5258 0.5753 0.6251 0.0827  0.1515  -0.0062 608  MET B CG  
7868 S SD  . MET B 513 ? 0.5766 0.6313 0.6930 0.0896  0.1432  -0.0017 608  MET B SD  
7869 C CE  . MET B 513 ? 0.5990 0.6636 0.7387 0.0954  0.1503  -0.0038 608  MET B CE  
7870 N N   . LEU B 514 ? 0.4833 0.5411 0.5641 0.0687  0.1479  -0.0015 609  LEU B N   
7871 C CA  . LEU B 514 ? 0.4857 0.5528 0.5762 0.0666  0.1517  -0.0009 609  LEU B CA  
7872 C C   . LEU B 514 ? 0.5228 0.5853 0.5984 0.0606  0.1571  -0.0015 609  LEU B C   
7873 O O   . LEU B 514 ? 0.4866 0.5536 0.5675 0.0589  0.1651  -0.0029 609  LEU B O   
7874 C CB  . LEU B 514 ? 0.4794 0.5549 0.5798 0.0665  0.1430  0.0032  609  LEU B CB  
7875 C CG  . LEU B 514 ? 0.5049 0.5864 0.6211 0.0726  0.1381  0.0042  609  LEU B CG  
7876 C CD1 . LEU B 514 ? 0.4644 0.5511 0.5842 0.0722  0.1281  0.0080  609  LEU B CD1 
7877 C CD2 . LEU B 514 ? 0.4772 0.5685 0.6133 0.0759  0.1443  0.0022  609  LEU B CD2 
7878 N N   . PHE B 515 ? 0.4921 0.5460 0.5493 0.0575  0.1530  -0.0002 610  PHE B N   
7879 C CA  . PHE B 515 ? 0.5348 0.5835 0.5764 0.0522  0.1575  -0.0002 610  PHE B CA  
7880 C C   . PHE B 515 ? 0.5146 0.5597 0.5513 0.0520  0.1683  -0.0049 610  PHE B C   
7881 O O   . PHE B 515 ? 0.5110 0.5576 0.5459 0.0487  0.1760  -0.0053 610  PHE B O   
7882 C CB  . PHE B 515 ? 0.4732 0.5135 0.4964 0.0498  0.1509  0.0015  610  PHE B CB  
7883 C CG  . PHE B 515 ? 0.5219 0.5571 0.5289 0.0446  0.1540  0.0028  610  PHE B CG  
7884 C CD1 . PHE B 515 ? 0.5363 0.5737 0.5434 0.0417  0.1515  0.0072  610  PHE B CD1 
7885 C CD2 . PHE B 515 ? 0.5412 0.5687 0.5322 0.0426  0.1593  -0.0002 610  PHE B CD2 
7886 C CE1 . PHE B 515 ? 0.5072 0.5391 0.4993 0.0372  0.1542  0.0093  610  PHE B CE1 
7887 C CE2 . PHE B 515 ? 0.5525 0.5751 0.5272 0.0379  0.1617  0.0017  610  PHE B CE2 
7888 C CZ  . PHE B 515 ? 0.5173 0.5419 0.4928 0.0354  0.1591  0.0069  610  PHE B CZ  
7889 N N   . LEU B 516 ? 0.5161 0.5558 0.5505 0.0551  0.1696  -0.0088 611  LEU B N   
7890 C CA  . LEU B 516 ? 0.5394 0.5745 0.5684 0.0550  0.1802  -0.0143 611  LEU B CA  
7891 C C   . LEU B 516 ? 0.5642 0.6075 0.6138 0.0592  0.1879  -0.0170 611  LEU B C   
7892 O O   . LEU B 516 ? 0.5376 0.5785 0.5850 0.0592  0.1984  -0.0220 611  LEU B O   
7893 C CB  . LEU B 516 ? 0.5306 0.5554 0.5478 0.0561  0.1787  -0.0181 611  LEU B CB  
7894 C CG  . LEU B 516 ? 0.5558 0.5731 0.5528 0.0519  0.1715  -0.0162 611  LEU B CG  
7895 C CD1 . LEU B 516 ? 0.5131 0.5221 0.5034 0.0532  0.1683  -0.0196 611  LEU B CD1 
7896 C CD2 . LEU B 516 ? 0.5577 0.5706 0.5365 0.0465  0.1773  -0.0172 611  LEU B CD2 
7897 N N   . GLY B 517 ? 0.5364 0.5895 0.6060 0.0628  0.1831  -0.0141 612  GLY B N   
7898 C CA  . GLY B 517 ? 0.5316 0.5935 0.6228 0.0674  0.1894  -0.0166 612  GLY B CA  
7899 C C   . GLY B 517 ? 0.5665 0.6236 0.6630 0.0734  0.1920  -0.0207 612  GLY B C   
7900 O O   . GLY B 517 ? 0.5327 0.5944 0.6432 0.0770  0.2005  -0.0244 612  GLY B O   
7901 N N   . LEU B 518 ? 0.4988 0.5465 0.5851 0.0746  0.1854  -0.0203 613  LEU B N   
7902 C CA  . LEU B 518 ? 0.5735 0.6147 0.6642 0.0800  0.1880  -0.0241 613  LEU B CA  
7903 C C   . LEU B 518 ? 0.5631 0.6129 0.6780 0.0873  0.1845  -0.0217 613  LEU B C   
7904 O O   . LEU B 518 ? 0.5246 0.5837 0.6493 0.0877  0.1766  -0.0165 613  LEU B O   
7905 C CB  . LEU B 518 ? 0.5435 0.5722 0.6169 0.0785  0.1817  -0.0241 613  LEU B CB  
7906 C CG  . LEU B 518 ? 0.5475 0.5674 0.5968 0.0718  0.1844  -0.0269 613  LEU B CG  
7907 C CD1 . LEU B 518 ? 0.5347 0.5462 0.5694 0.0693  0.1757  -0.0254 613  LEU B CD1 
7908 C CD2 . LEU B 518 ? 0.5564 0.5696 0.5997 0.0717  0.1962  -0.0345 613  LEU B CD2 
7909 N N   . ASN B 519 ? 0.5173 0.5637 0.6418 0.0931  0.1901  -0.0256 614  ASN B N   
7910 C CA  . ASN B 519 ? 0.5614 0.6167 0.7106 0.1007  0.1884  -0.0236 614  ASN B CA  
7911 C C   . ASN B 519 ? 0.5616 0.6129 0.7138 0.1051  0.1778  -0.0189 614  ASN B C   
7912 O O   . ASN B 519 ? 0.6139 0.6729 0.7858 0.1115  0.1745  -0.0160 614  ASN B O   
7913 C CB  . ASN B 519 ? 0.5237 0.5779 0.6844 0.1058  0.2003  -0.0300 614  ASN B CB  
7914 C CG  . ASN B 519 ? 0.6057 0.6437 0.7579 0.1089  0.2024  -0.0338 614  ASN B CG  
7915 O OD1 . ASN B 519 ? 0.5888 0.6159 0.7233 0.1055  0.1967  -0.0328 614  ASN B OD1 
7916 N ND2 . ASN B 519 ? 0.6193 0.6560 0.7853 0.1152  0.2110  -0.0386 614  ASN B ND2 
7917 N N   . ASN B 520 ? 0.5531 0.5929 0.6867 0.1017  0.1726  -0.0179 615  ASN B N   
7918 C CA  . ASN B 520 ? 0.5496 0.5836 0.6850 0.1057  0.1644  -0.0139 615  ASN B CA  
7919 C C   . ASN B 520 ? 0.5526 0.5793 0.6682 0.0998  0.1573  -0.0116 615  ASN B C   
7920 O O   . ASN B 520 ? 0.5307 0.5493 0.6291 0.0945  0.1608  -0.0155 615  ASN B O   
7921 C CB  . ASN B 520 ? 0.5507 0.5735 0.6898 0.1111  0.1703  -0.0180 615  ASN B CB  
7922 C CG  . ASN B 520 ? 0.5888 0.6067 0.7345 0.1167  0.1625  -0.0128 615  ASN B CG  
7923 O OD1 . ASN B 520 ? 0.5782 0.5897 0.7117 0.1136  0.1554  -0.0095 615  ASN B OD1 
7924 N ND2 . ASN B 520 ? 0.5923 0.6134 0.7578 0.1249  0.1641  -0.0120 615  ASN B ND2 
7925 N N   . ILE B 521 ? 0.5237 0.5536 0.6419 0.1008  0.1473  -0.0054 616  ILE B N   
7926 C CA  . ILE B 521 ? 0.5565 0.5813 0.6586 0.0957  0.1404  -0.0029 616  ILE B CA  
7927 C C   . ILE B 521 ? 0.5589 0.5687 0.6485 0.0944  0.1420  -0.0058 616  ILE B C   
7928 O O   . ILE B 521 ? 0.5364 0.5414 0.6107 0.0889  0.1389  -0.0059 616  ILE B O   
7929 C CB  . ILE B 521 ? 0.5816 0.6127 0.6902 0.0976  0.1303  0.0040  616  ILE B CB  
7930 C CG1 . ILE B 521 ? 0.5761 0.6044 0.6695 0.0920  0.1238  0.0064  616  ILE B CG1 
7931 C CG2 . ILE B 521 ? 0.5248 0.5509 0.6422 0.1041  0.1280  0.0067  616  ILE B CG2 
7932 C CD1 . ILE B 521 ? 0.5539 0.5890 0.6419 0.0869  0.1234  0.0060  616  ILE B CD1 
7933 N N   . ARG B 522 ? 0.5220 0.5243 0.6184 0.0994  0.1468  -0.0083 617  ARG B N   
7934 C CA  . ARG B 522 ? 0.5648 0.5521 0.6495 0.0977  0.1491  -0.0119 617  ARG B CA  
7935 C C   . ARG B 522 ? 0.5246 0.5067 0.5940 0.0917  0.1554  -0.0188 617  ARG B C   
7936 O O   . ARG B 522 ? 0.5057 0.4763 0.5628 0.0884  0.1561  -0.0222 617  ARG B O   
7937 C CB  . ARG B 522 ? 0.5599 0.5396 0.6564 0.1048  0.1533  -0.0133 617  ARG B CB  
7938 C CG  . ARG B 522 ? 0.5781 0.5602 0.6864 0.1103  0.1457  -0.0056 617  ARG B CG  
7939 C CD  . ARG B 522 ? 0.6039 0.5838 0.7297 0.1192  0.1496  -0.0057 617  ARG B CD  
7940 N NE  . ARG B 522 ? 0.5617 0.5458 0.6982 0.1244  0.1412  0.0026  617  ARG B NE  
7941 C CZ  . ARG B 522 ? 0.6037 0.6030 0.7516 0.1268  0.1361  0.0072  617  ARG B CZ  
7942 N NH1 . ARG B 522 ? 0.5835 0.5953 0.7349 0.1243  0.1388  0.0045  617  ARG B NH1 
7943 N NH2 . ARG B 522 ? 0.5769 0.5789 0.7328 0.1316  0.1280  0.0147  617  ARG B NH2 
7944 N N   . LYS B 523 ? 0.5307 0.5209 0.5999 0.0898  0.1599  -0.0208 618  LYS B N   
7945 C CA  . LYS B 523 ? 0.5397 0.5251 0.5920 0.0837  0.1650  -0.0265 618  LYS B CA  
7946 C C   . LYS B 523 ? 0.5420 0.5283 0.5792 0.0772  0.1578  -0.0237 618  LYS B C   
7947 O O   . LYS B 523 ? 0.5420 0.5222 0.5629 0.0719  0.1598  -0.0278 618  LYS B O   
7948 C CB  . LYS B 523 ? 0.5197 0.5123 0.5766 0.0840  0.1735  -0.0295 618  LYS B CB  
7949 C CG  . LYS B 523 ? 0.5020 0.4906 0.5696 0.0895  0.1836  -0.0352 618  LYS B CG  
7950 C CD  . LYS B 523 ? 0.5805 0.5770 0.6529 0.0892  0.1931  -0.0386 618  LYS B CD  
7951 C CE  . LYS B 523 ? 0.5702 0.5617 0.6516 0.0943  0.2045  -0.0457 618  LYS B CE  
7952 N NZ  . LYS B 523 ? 0.5126 0.5058 0.6157 0.1029  0.2020  -0.0428 618  LYS B NZ  
7953 N N   . THR B 524 ? 0.4936 0.4873 0.5356 0.0774  0.1494  -0.0172 619  THR B N   
7954 C CA  . THR B 524 ? 0.5205 0.5163 0.5505 0.0719  0.1429  -0.0145 619  THR B CA  
7955 C C   . THR B 524 ? 0.4980 0.4907 0.5261 0.0714  0.1348  -0.0109 619  THR B C   
7956 O O   . THR B 524 ? 0.4684 0.4646 0.4903 0.0679  0.1288  -0.0079 619  THR B O   
7957 C CB  . THR B 524 ? 0.5010 0.5086 0.5368 0.0714  0.1410  -0.0106 619  THR B CB  
7958 O OG1 . THR B 524 ? 0.4665 0.4813 0.5188 0.0764  0.1377  -0.0064 619  THR B OG1 
7959 C CG2 . THR B 524 ? 0.5107 0.5208 0.5459 0.0704  0.1498  -0.0142 619  THR B CG2 
7960 N N   . SER B 525 ? 0.5380 0.5236 0.5713 0.0747  0.1351  -0.0111 620  SER B N   
7961 C CA  . SER B 525 ? 0.5238 0.5041 0.5538 0.0736  0.1292  -0.0085 620  SER B CA  
7962 C C   . SER B 525 ? 0.5250 0.4922 0.5472 0.0717  0.1332  -0.0140 620  SER B C   
7963 O O   . SER B 525 ? 0.5311 0.4924 0.5582 0.0751  0.1397  -0.0178 620  SER B O   
7964 C CB  . SER B 525 ? 0.4995 0.4823 0.5428 0.0792  0.1255  -0.0028 620  SER B CB  
7965 O OG  . SER B 525 ? 0.5468 0.5240 0.5863 0.0778  0.1205  0.0003  620  SER B OG  
7966 N N   . LEU B 526 ? 0.5162 0.4790 0.5270 0.0661  0.1295  -0.0150 621  LEU B N   
7967 C CA  . LEU B 526 ? 0.5815 0.5322 0.5833 0.0628  0.1331  -0.0214 621  LEU B CA  
7968 C C   . LEU B 526 ? 0.5554 0.4957 0.5649 0.0668  0.1361  -0.0218 621  LEU B C   
7969 O O   . LEU B 526 ? 0.6188 0.5503 0.6278 0.0680  0.1429  -0.0278 621  LEU B O   
7970 C CB  . LEU B 526 ? 0.5658 0.5154 0.5566 0.0561  0.1276  -0.0217 621  LEU B CB  
7971 C CG  . LEU B 526 ? 0.5739 0.5268 0.5515 0.0505  0.1264  -0.0249 621  LEU B CG  
7972 C CD1 . LEU B 526 ? 0.5642 0.5167 0.5352 0.0450  0.1200  -0.0245 621  LEU B CD1 
7973 C CD2 . LEU B 526 ? 0.5443 0.4900 0.5134 0.0489  0.1333  -0.0326 621  LEU B CD2 
7974 N N   . PHE B 527 ? 0.5422 0.4824 0.5582 0.0689  0.1312  -0.0157 622  PHE B N   
7975 C CA  . PHE B 527 ? 0.6024 0.5319 0.6258 0.0730  0.1332  -0.0145 622  PHE B CA  
7976 C C   . PHE B 527 ? 0.5841 0.5208 0.6203 0.0796  0.1297  -0.0068 622  PHE B C   
7977 O O   . PHE B 527 ? 0.5831 0.5220 0.6197 0.0791  0.1237  -0.0006 622  PHE B O   
7978 C CB  . PHE B 527 ? 0.5717 0.4915 0.5880 0.0679  0.1307  -0.0147 622  PHE B CB  
7979 C CG  . PHE B 527 ? 0.5775 0.4914 0.5813 0.0610  0.1331  -0.0227 622  PHE B CG  
7980 C CD1 . PHE B 527 ? 0.6288 0.5309 0.6305 0.0611  0.1401  -0.0302 622  PHE B CD1 
7981 C CD2 . PHE B 527 ? 0.5706 0.4912 0.5651 0.0544  0.1283  -0.0231 622  PHE B CD2 
7982 C CE1 . PHE B 527 ? 0.5897 0.4866 0.5787 0.0543  0.1419  -0.0381 622  PHE B CE1 
7983 C CE2 . PHE B 527 ? 0.5625 0.4785 0.5453 0.0480  0.1295  -0.0304 622  PHE B CE2 
7984 C CZ  . PHE B 527 ? 0.6242 0.5284 0.6037 0.0477  0.1362  -0.0379 622  PHE B CZ  
7985 N N   . PRO B 528 ? 0.5393 0.4809 0.5861 0.0855  0.1333  -0.0071 623  PRO B N   
7986 C CA  . PRO B 528 ? 0.5372 0.4894 0.5958 0.0909  0.1289  -0.0001 623  PRO B CA  
7987 C C   . PRO B 528 ? 0.6061 0.5523 0.6704 0.0949  0.1249  0.0063  623  PRO B C   
7988 O O   . PRO B 528 ? 0.5749 0.5077 0.6398 0.0965  0.1281  0.0050  623  PRO B O   
7989 C CB  . PRO B 528 ? 0.5696 0.5264 0.6394 0.0963  0.1350  -0.0033 623  PRO B CB  
7990 C CG  . PRO B 528 ? 0.5502 0.5033 0.6095 0.0915  0.1419  -0.0117 623  PRO B CG  
7991 C CD  . PRO B 528 ? 0.5755 0.5156 0.6224 0.0864  0.1414  -0.0144 623  PRO B CD  
7992 N N   . ARG B 529 ? 0.5575 0.5132 0.6255 0.0963  0.1180  0.0133  624  ARG B N   
7993 C CA  . ARG B 529 ? 0.5665 0.5187 0.6394 0.1005  0.1132  0.0208  624  ARG B CA  
7994 C C   . ARG B 529 ? 0.5909 0.5542 0.6781 0.1075  0.1104  0.0250  624  ARG B C   
7995 O O   . ARG B 529 ? 0.5915 0.5682 0.6801 0.1063  0.1068  0.0262  624  ARG B O   
7996 C CB  . ARG B 529 ? 0.5945 0.5486 0.6578 0.0954  0.1068  0.0255  624  ARG B CB  
7997 C CG  . ARG B 529 ? 0.6365 0.5797 0.6883 0.0890  0.1085  0.0229  624  ARG B CG  
7998 C CD  . ARG B 529 ? 0.5852 0.5127 0.6384 0.0914  0.1106  0.0249  624  ARG B CD  
7999 N NE  . ARG B 529 ? 0.5981 0.5152 0.6412 0.0844  0.1130  0.0210  624  ARG B NE  
8000 C CZ  . ARG B 529 ? 0.6450 0.5535 0.6853 0.0822  0.1189  0.0133  624  ARG B CZ  
8001 N NH1 . ARG B 529 ? 0.6487 0.5565 0.6953 0.0866  0.1239  0.0086  624  ARG B NH1 
8002 N NH2 . ARG B 529 ? 0.6171 0.5176 0.6483 0.0750  0.1199  0.0099  624  ARG B NH2 
8003 N N   . ASP B 530 ? 0.6248 0.5825 0.7232 0.1149  0.1119  0.0273  625  ASP B N   
8004 C CA  . ASP B 530 ? 0.5919 0.5607 0.7050 0.1219  0.1078  0.0322  625  ASP B CA  
8005 C C   . ASP B 530 ? 0.5886 0.5481 0.7072 0.1282  0.1046  0.0392  625  ASP B C   
8006 O O   . ASP B 530 ? 0.5851 0.5289 0.6962 0.1267  0.1069  0.0392  625  ASP B O   
8007 C CB  . ASP B 530 ? 0.6156 0.5917 0.7415 0.1257  0.1141  0.0265  625  ASP B CB  
8008 C CG  . ASP B 530 ? 0.6762 0.6391 0.8067 0.1295  0.1225  0.0215  625  ASP B CG  
8009 O OD1 . ASP B 530 ? 0.6209 0.5746 0.7579 0.1355  0.1215  0.0256  625  ASP B OD1 
8010 O OD2 . ASP B 530 ? 0.6911 0.6524 0.8182 0.1266  0.1303  0.0135  625  ASP B OD2 
8011 N N   . PRO B 531 ? 0.5901 0.5581 0.7212 0.1351  0.0989  0.0454  626  PRO B N   
8012 C CA  . PRO B 531 ? 0.6441 0.6027 0.7781 0.1409  0.0946  0.0536  626  PRO B CA  
8013 C C   . PRO B 531 ? 0.6712 0.6123 0.8093 0.1452  0.1013  0.0516  626  PRO B C   
8014 O O   . PRO B 531 ? 0.6883 0.6171 0.8244 0.1480  0.0987  0.0581  626  PRO B O   
8015 C CB  . PRO B 531 ? 0.6642 0.6375 0.8138 0.1481  0.0881  0.0588  626  PRO B CB  
8016 C CG  . PRO B 531 ? 0.6717 0.6619 0.8199 0.1429  0.0862  0.0555  626  PRO B CG  
8017 C CD  . PRO B 531 ? 0.6329 0.6199 0.7750 0.1372  0.0951  0.0462  626  PRO B CD  
8018 N N   . LYS B 532 ? 0.6383 0.5770 0.7812 0.1455  0.1102  0.0427  627  LYS B N   
8019 C CA  . LYS B 532 ? 0.7071 0.6288 0.8543 0.1496  0.1173  0.0395  627  LYS B CA  
8020 C C   . LYS B 532 ? 0.6711 0.5803 0.8040 0.1416  0.1245  0.0312  627  LYS B C   
8021 O O   . LYS B 532 ? 0.7101 0.6054 0.8456 0.1438  0.1318  0.0262  627  LYS B O   
8022 C CB  . LYS B 532 ? 0.6535 0.5816 0.8203 0.1580  0.1225  0.0356  627  LYS B CB  
8023 C CG  . LYS B 532 ? 0.7026 0.6372 0.8865 0.1680  0.1159  0.0442  627  LYS B CG  
8024 C CD  . LYS B 532 ? 0.7930 0.7089 0.9832 0.1754  0.1181  0.0474  627  LYS B CD  
8025 C CE  . LYS B 532 ? 0.7557 0.6745 0.9566 0.1841  0.1086  0.0591  627  LYS B CE  
8026 N NZ  . LYS B 532 ? 0.7979 0.6977 1.0061 0.1921  0.1112  0.0623  627  LYS B NZ  
8027 N N   . ARG B 533 ? 0.6390 0.5528 0.7572 0.1325  0.1226  0.0294  628  ARG B N   
8028 C CA  . ARG B 533 ? 0.6607 0.5649 0.7657 0.1246  0.1285  0.0213  628  ARG B CA  
8029 C C   . ARG B 533 ? 0.6867 0.5900 0.7765 0.1162  0.1233  0.0244  628  ARG B C   
8030 O O   . ARG B 533 ? 0.6374 0.5542 0.7226 0.1124  0.1187  0.0258  628  ARG B O   
8031 C CB  . ARG B 533 ? 0.6450 0.5585 0.7494 0.1219  0.1340  0.0126  628  ARG B CB  
8032 C CG  . ARG B 533 ? 0.6430 0.5474 0.7327 0.1136  0.1391  0.0043  628  ARG B CG  
8033 C CD  . ARG B 533 ? 0.7096 0.6210 0.7985 0.1120  0.1456  -0.0042 628  ARG B CD  
8034 N NE  . ARG B 533 ? 0.6845 0.5913 0.7854 0.1189  0.1534  -0.0088 628  ARG B NE  
8035 C CZ  . ARG B 533 ? 0.6966 0.5874 0.7953 0.1192  0.1605  -0.0152 628  ARG B CZ  
8036 N NH1 . ARG B 533 ? 0.6925 0.5702 0.7775 0.1125  0.1605  -0.0179 628  ARG B NH1 
8037 N NH2 . ARG B 533 ? 0.7192 0.6071 0.8302 0.1261  0.1681  -0.0196 628  ARG B NH2 
8038 N N   . LEU B 534 ? 0.6673 0.5544 0.7499 0.1132  0.1246  0.0248  629  LEU B N   
8039 C CA  . LEU B 534 ? 0.6972 0.5816 0.7661 0.1047  0.1214  0.0264  629  LEU B CA  
8040 C C   . LEU B 534 ? 0.7172 0.5913 0.7765 0.0973  0.1271  0.0176  629  LEU B C   
8041 O O   . LEU B 534 ? 0.6634 0.5370 0.7122 0.0894  0.1249  0.0174  629  LEU B O   
8042 C CB  . LEU B 534 ? 0.6701 0.5447 0.7383 0.1065  0.1175  0.0359  629  LEU B CB  
8043 C CG  . LEU B 534 ? 0.7126 0.5858 0.7686 0.0988  0.1136  0.0399  629  LEU B CG  
8044 C CD1 . LEU B 534 ? 0.6554 0.5471 0.7071 0.0952  0.1084  0.0409  629  LEU B CD1 
8045 C CD2 . LEU B 534 ? 0.7633 0.6263 0.8199 0.1023  0.1104  0.0501  629  LEU B CD2 
8046 N N   . ILE B 535 ? 0.7097 0.5763 0.7726 0.0994  0.1342  0.0099  630  ILE B N   
8047 C CA  . ILE B 535 ? 0.7337 0.5884 0.7879 0.0930  0.1399  0.0008  630  ILE B CA  
8048 C C   . ILE B 535 ? 0.7432 0.6041 0.7973 0.0932  0.1453  -0.0082 630  ILE B C   
8049 O O   . ILE B 535 ? 0.7617 0.6282 0.8269 0.1006  0.1478  -0.0081 630  ILE B O   
8050 C CB  . ILE B 535 ? 0.7627 0.5966 0.8203 0.0957  0.1444  0.0004  630  ILE B CB  
8051 C CG1 . ILE B 535 ? 0.8216 0.6484 0.8785 0.0954  0.1394  0.0102  630  ILE B CG1 
8052 C CG2 . ILE B 535 ? 0.8359 0.6571 0.8841 0.0883  0.1503  -0.0101 630  ILE B CG2 
8053 C CD1 . ILE B 535 ? 0.8900 0.7126 0.9343 0.0847  0.1379  0.0090  630  ILE B CD1 
8054 N N   . PRO B 536 ? 0.7363 0.5972 0.7784 0.0852  0.1473  -0.0160 631  PRO B N   
8055 C CA  . PRO B 536 ? 0.7244 0.5833 0.7543 0.0758  0.1438  -0.0171 631  PRO B CA  
8056 C C   . PRO B 536 ? 0.7501 0.6231 0.7786 0.0739  0.1359  -0.0093 631  PRO B C   
8057 O O   . PRO B 536 ? 0.7178 0.6041 0.7515 0.0781  0.1336  -0.0059 631  PRO B O   
8058 C CB  . PRO B 536 ? 0.7549 0.6154 0.7746 0.0699  0.1474  -0.0272 631  PRO B CB  
8059 C CG  . PRO B 536 ? 0.7324 0.5997 0.7583 0.0760  0.1520  -0.0299 631  PRO B CG  
8060 C CD  . PRO B 536 ? 0.7341 0.5964 0.7745 0.0853  0.1540  -0.0252 631  PRO B CD  
8061 O OXT . PRO B 536 ? 0.7645 0.6358 0.7872 0.0682  0.1322  -0.0067 631  PRO B OXT 
8062 S S   . SO4 C .   ? 1.0375 1.0809 0.9813 -0.0081 0.1316  0.0471  701  SO4 A S   
8063 O O1  . SO4 C .   ? 1.0116 1.0633 0.9683 -0.0133 0.1380  0.0423  701  SO4 A O1  
8064 O O2  . SO4 C .   ? 0.9125 0.9611 0.8466 -0.0064 0.1325  0.0455  701  SO4 A O2  
8065 O O3  . SO4 C .   ? 0.8187 0.8624 0.7713 -0.0025 0.1237  0.0448  701  SO4 A O3  
8066 O O4  . SO4 C .   ? 1.0071 1.0368 0.9392 -0.0106 0.1328  0.0557  701  SO4 A O4  
8067 C C1  . EDO D .   ? 0.7245 0.8614 0.8910 0.0909  0.0915  -0.0337 702  EDO A C1  
8068 O O1  . EDO D .   ? 0.6955 0.8314 0.8481 0.0844  0.0898  -0.0301 702  EDO A O1  
8069 C C2  . EDO D .   ? 0.7698 0.8966 0.9285 0.0914  0.0963  -0.0384 702  EDO A C2  
8070 O O2  . EDO D .   ? 0.7538 0.8684 0.9041 0.0923  0.0911  -0.0348 702  EDO A O2  
8071 S S   . SO4 E .   ? 0.9722 0.9764 1.0529 -0.1031 0.1438  0.0033  703  SO4 A S   
8072 O O1  . SO4 E .   ? 0.9831 0.9678 1.0560 -0.1083 0.1521  0.0099  703  SO4 A O1  
8073 O O2  . SO4 E .   ? 0.9603 0.9658 1.0309 -0.0911 0.1404  0.0076  703  SO4 A O2  
8074 O O3  . SO4 E .   ? 0.8841 0.9104 0.9804 -0.1083 0.1456  -0.0003 703  SO4 A O3  
8075 O O4  . SO4 E .   ? 0.8905 0.8911 0.9739 -0.1048 0.1373  -0.0040 703  SO4 A O4  
8076 S S   . SO4 F .   ? 1.0267 0.9548 0.9331 -0.1523 0.0347  -0.1737 704  SO4 A S   
8077 O O1  . SO4 F .   ? 1.0135 0.9625 0.9339 -0.1605 0.0238  -0.1744 704  SO4 A O1  
8078 O O2  . SO4 F .   ? 0.9077 0.8411 0.8197 -0.1394 0.0382  -0.1605 704  SO4 A O2  
8079 O O3  . SO4 F .   ? 1.1379 1.0619 1.0208 -0.1527 0.0314  -0.1813 704  SO4 A O3  
8080 O O4  . SO4 F .   ? 1.0392 0.9450 0.9493 -0.1570 0.0454  -0.1792 704  SO4 A O4  
8081 S S   . SO4 G .   ? 1.0230 0.9604 1.1754 0.1418  0.1533  -0.0006 701  SO4 B S   
8082 O O1  . SO4 G .   ? 0.8170 0.7560 0.9498 0.1316  0.1490  -0.0006 701  SO4 B O1  
8083 O O2  . SO4 G .   ? 0.9688 0.8910 1.1239 0.1466  0.1509  0.0043  701  SO4 B O2  
8084 O O3  . SO4 G .   ? 1.0089 0.9650 1.1777 0.1471  0.1482  0.0050  701  SO4 B O3  
8085 O O4  . SO4 G .   ? 0.8984 0.8309 1.0525 0.1423  0.1653  -0.0110 701  SO4 B O4  
8086 C C1  . EDO H .   ? 1.0578 0.9673 0.8125 0.0053  0.2314  -0.0973 702  EDO B C1  
8087 O O1  . EDO H .   ? 1.0091 0.9249 0.7853 0.0096  0.2208  -0.0903 702  EDO B O1  
8088 C C2  . EDO H .   ? 1.0985 0.9973 0.8338 0.0005  0.2292  -0.1068 702  EDO B C2  
8089 O O2  . EDO H .   ? 1.1481 1.0472 0.8660 -0.0048 0.2157  -0.1024 702  EDO B O2  
8090 O O   . HOH I .   ? 0.5342 0.6834 0.6932 -0.0905 0.0640  -0.0483 801  HOH A O   
8091 O O   . HOH I .   ? 0.6786 0.7347 0.8448 -0.1635 0.1413  -0.0363 802  HOH A O   
8092 O O   . HOH I .   ? 0.6723 0.7047 0.6620 0.0409  0.0703  0.0103  803  HOH A O   
8093 O O   . HOH I .   ? 0.7308 0.7947 0.8534 -0.1139 0.1479  -0.0061 804  HOH A O   
8094 O O   . HOH I .   ? 0.5276 0.8400 0.9415 -0.2192 0.1481  -0.0805 805  HOH A O   
8095 O O   . HOH I .   ? 0.7888 0.6956 0.8139 0.0186  0.1279  -0.2030 806  HOH A O   
8096 O O   . HOH I .   ? 0.7898 0.7467 0.6827 0.0078  0.1828  -0.2722 807  HOH A O   
8097 O O   . HOH I .   ? 0.9103 0.8892 0.8900 -0.0390 0.0612  -0.1895 808  HOH A O   
8098 O O   . HOH I .   ? 0.6140 0.5795 0.6054 -0.0048 0.0884  -0.0151 809  HOH A O   
8099 O O   . HOH I .   ? 0.7494 0.7435 0.6264 0.0192  0.0783  -0.0112 810  HOH A O   
8100 O O   . HOH I .   ? 0.6695 0.7517 0.8698 0.1214  0.1909  -0.1477 811  HOH A O   
8101 O O   . HOH I .   ? 0.7714 0.7875 0.7290 -0.0192 0.1349  0.0556  812  HOH A O   
8102 O O   . HOH I .   ? 0.5674 0.6046 0.6394 0.0698  0.0753  -0.0250 813  HOH A O   
8103 O O   . HOH I .   ? 0.4701 0.4759 0.4504 0.0373  0.0826  0.0008  814  HOH A O   
8104 O O   . HOH I .   ? 1.0739 0.9201 1.0946 0.0146  0.1603  -0.2691 815  HOH A O   
8105 O O   . HOH I .   ? 0.5833 0.9065 0.8936 -0.1275 -0.0086 -0.0893 816  HOH A O   
8106 O O   . HOH I .   ? 0.4901 0.6804 0.6562 -0.0518 0.0407  -0.0389 817  HOH A O   
8107 O O   . HOH I .   ? 0.5975 0.7722 0.6404 -0.0408 -0.0514 -0.0459 818  HOH A O   
8108 O O   . HOH I .   ? 0.6683 0.6874 0.6672 0.0359  0.0800  0.0292  819  HOH A O   
8109 O O   . HOH I .   ? 0.6449 0.7274 0.7471 -0.0688 0.0942  -0.0215 820  HOH A O   
8110 O O   . HOH I .   ? 0.5393 0.7647 0.6889 -0.0343 -0.0258 -0.0404 821  HOH A O   
8111 O O   . HOH I .   ? 0.5392 0.8793 0.8836 -0.0724 0.0524  -0.0580 822  HOH A O   
8112 O O   . HOH I .   ? 0.8134 0.8065 0.6312 -0.0543 0.0188  -0.0867 823  HOH A O   
8113 O O   . HOH I .   ? 0.5679 0.5606 0.5655 0.0468  0.0898  0.0080  824  HOH A O   
8114 O O   . HOH I .   ? 0.6690 0.6746 0.7333 0.0617  0.0662  -0.0001 825  HOH A O   
8115 O O   . HOH I .   ? 0.6494 0.5747 0.7482 0.0643  0.0809  -0.0232 826  HOH A O   
8116 O O   A HOH I .   ? 0.6439 0.7183 0.5146 0.0126  0.0919  -0.0838 827  HOH A O   
8117 O O   B HOH I .   ? 0.6766 0.7535 0.5410 0.0132  0.1059  -0.0832 827  HOH A O   
8118 O O   . HOH I .   ? 0.6088 0.6899 0.6754 0.0675  0.0547  0.0082  828  HOH A O   
8119 O O   . HOH I .   ? 0.7197 0.9085 0.8877 0.0592  0.1291  -0.0450 829  HOH A O   
8120 O O   . HOH I .   ? 0.5763 0.7405 0.7123 -0.0162 0.0931  -0.0129 830  HOH A O   
8121 O O   . HOH I .   ? 0.7828 0.5852 0.6753 0.0058  0.1748  -0.1267 831  HOH A O   
8122 O O   . HOH I .   ? 0.5845 0.7851 0.6916 -0.0259 -0.0325 -0.0349 832  HOH A O   
8123 O O   . HOH I .   ? 0.7330 0.8148 0.6262 0.0204  0.1127  -0.0707 833  HOH A O   
8124 O O   . HOH I .   ? 0.7786 0.6827 0.9359 0.1134  0.0881  -0.0323 834  HOH A O   
8125 O O   . HOH I .   ? 0.5158 0.6456 0.5743 0.0251  0.1138  -0.0080 835  HOH A O   
8126 O O   . HOH I .   ? 0.4517 0.5189 0.4709 0.0401  0.0699  0.0148  836  HOH A O   
8127 O O   . HOH I .   ? 0.7587 0.7745 0.7860 -0.0290 0.0812  -0.0156 837  HOH A O   
8128 O O   . HOH I .   ? 0.5983 0.5984 0.7455 0.1128  0.2304  -0.2226 838  HOH A O   
8129 O O   . HOH I .   ? 0.4992 0.5481 0.5081 0.0283  0.0801  0.0213  839  HOH A O   
8130 O O   . HOH I .   ? 0.7630 0.5870 0.7399 -0.1055 0.1128  -0.1071 840  HOH A O   
8131 O O   . HOH I .   ? 0.6772 0.8062 0.6436 0.0182  0.1749  -0.0538 841  HOH A O   
8132 O O   . HOH I .   ? 0.5319 0.7136 0.7002 -0.0429 0.0908  -0.0226 842  HOH A O   
8133 O O   . HOH I .   ? 0.9656 0.7264 0.8363 -0.0361 0.1623  -0.1572 843  HOH A O   
8134 O O   . HOH I .   ? 0.7771 0.6456 0.6453 -0.0217 0.1232  -0.1076 844  HOH A O   
8135 O O   . HOH I .   ? 0.6395 0.6538 0.6304 -0.0224 0.1277  0.0438  845  HOH A O   
8136 O O   . HOH I .   ? 0.6098 0.8361 0.8122 -0.0068 0.1014  -0.0244 846  HOH A O   
8137 O O   . HOH I .   ? 0.5783 0.6491 0.5473 0.0314  0.0149  0.0126  847  HOH A O   
8138 O O   . HOH I .   ? 0.4564 0.6084 0.5705 0.0533  0.1107  -0.0294 848  HOH A O   
8139 O O   . HOH I .   ? 0.8213 0.6061 0.8040 -0.1174 0.1251  -0.1125 849  HOH A O   
8140 O O   . HOH I .   ? 0.5703 0.6153 0.6286 0.0675  0.0611  0.0046  850  HOH A O   
8141 O O   . HOH I .   ? 0.5717 0.5135 0.5672 0.0394  0.1021  0.0021  851  HOH A O   
8142 O O   . HOH I .   ? 0.9236 0.9453 0.9292 -0.0681 0.1714  0.0476  852  HOH A O   
8143 O O   . HOH I .   ? 0.6013 0.8460 0.9701 -0.2455 0.1163  -0.0984 853  HOH A O   
8144 O O   . HOH I .   ? 0.5159 0.7592 0.7400 -0.0442 0.0458  -0.0387 854  HOH A O   
8145 O O   A HOH I .   ? 0.6337 0.5904 0.6345 -0.0006 0.0999  0.0165  855  HOH A O   
8146 O O   B HOH I .   ? 0.6292 0.5659 0.6312 -0.0123 0.1069  0.0154  855  HOH A O   
8147 O O   . HOH I .   ? 0.6514 0.6195 0.6474 -0.0284 0.0839  -0.0310 856  HOH A O   
8148 O O   . HOH I .   ? 0.7831 0.6618 0.7803 0.0289  0.1113  0.0306  857  HOH A O   
8149 O O   . HOH I .   ? 0.7725 0.6961 0.7399 -0.0073 0.1209  -0.2325 858  HOH A O   
8150 O O   . HOH I .   ? 0.6135 0.5689 0.5924 -0.0197 0.0854  -0.0358 859  HOH A O   
8151 O O   . HOH I .   ? 0.6364 0.6541 0.5402 0.0190  0.1622  -0.1977 860  HOH A O   
8152 O O   . HOH I .   ? 0.5715 0.9180 0.8381 -0.0491 -0.0760 -0.0556 861  HOH A O   
8153 O O   . HOH I .   ? 0.4755 0.6149 0.5481 0.0358  0.1169  -0.0195 862  HOH A O   
8154 O O   . HOH I .   ? 0.5437 0.5332 0.5334 0.0225  0.0838  -0.0007 863  HOH A O   
8155 O O   . HOH I .   ? 0.5033 0.6139 0.5370 0.0033  0.1249  0.0074  864  HOH A O   
8156 O O   . HOH I .   ? 0.6895 0.8017 0.7696 0.0731  0.0088  0.0264  865  HOH A O   
8157 O O   . HOH I .   ? 0.6755 0.5860 0.6644 0.0284  0.1029  0.0489  866  HOH A O   
8158 O O   . HOH I .   ? 0.6219 0.6491 0.5520 0.0361  0.0508  0.0200  867  HOH A O   
8159 O O   . HOH I .   ? 0.7854 0.8053 0.8217 -0.0480 0.1286  0.0227  868  HOH A O   
8160 O O   . HOH I .   ? 0.5581 0.6133 0.7479 0.1230  0.1066  -0.0614 869  HOH A O   
8161 O O   . HOH I .   ? 0.7203 0.5679 0.7157 -0.0968 0.1124  -0.0823 870  HOH A O   
8162 O O   . HOH I .   ? 0.4889 0.5222 0.4834 0.0208  0.0901  0.0323  871  HOH A O   
8163 O O   . HOH I .   ? 0.6455 0.5422 0.6345 0.0219  0.1123  -0.0107 872  HOH A O   
8164 O O   . HOH I .   ? 0.6547 0.7728 0.8775 0.1298  0.0595  -0.0138 873  HOH A O   
8165 O O   . HOH I .   ? 1.0475 0.8319 1.0530 0.0393  0.1296  0.0411  874  HOH A O   
8166 O O   . HOH I .   ? 0.6802 0.7410 0.6870 0.0161  0.0483  -0.0642 875  HOH A O   
8167 O O   . HOH I .   ? 0.8946 0.7235 0.7187 -0.0659 0.1171  -0.1588 876  HOH A O   
8168 O O   . HOH I .   ? 0.6530 0.5778 0.7775 0.0898  0.1461  -0.1511 877  HOH A O   
8169 O O   . HOH I .   ? 0.5551 0.6505 0.6179 0.0611  0.0880  -0.0232 878  HOH A O   
8170 O O   . HOH I .   ? 0.5287 0.5778 0.5571 0.0029  0.0824  0.0076  879  HOH A O   
8171 O O   . HOH I .   ? 0.6404 0.6683 0.5803 0.0439  0.0654  0.0633  880  HOH A O   
8172 O O   . HOH I .   ? 0.7294 0.6397 0.6075 0.0228  0.1577  -0.0775 881  HOH A O   
8173 O O   . HOH I .   ? 0.5824 0.5662 0.5897 0.0551  0.0949  0.0109  882  HOH A O   
8174 O O   . HOH I .   ? 0.4604 0.5736 0.4885 0.0197  0.1164  -0.0002 883  HOH A O   
8175 O O   . HOH I .   ? 0.6872 0.5948 0.5363 -0.0100 0.1158  -0.0884 884  HOH A O   
8176 O O   . HOH I .   ? 0.4884 0.5842 0.5033 0.0488  0.1252  -0.0639 885  HOH A O   
8177 O O   . HOH I .   ? 0.5761 0.7669 0.8443 -0.1700 0.1476  -0.0474 886  HOH A O   
8178 O O   . HOH I .   ? 0.7282 0.6093 0.6076 -0.0668 0.0892  -0.1238 887  HOH A O   
8179 O O   . HOH I .   ? 0.7446 0.7405 0.7922 -0.0716 0.0903  -0.0340 888  HOH A O   
8180 O O   . HOH I .   ? 0.7878 0.7335 0.5815 -0.0460 0.0596  -0.0980 889  HOH A O   
8181 O O   . HOH I .   ? 0.5051 0.4838 0.4559 0.0401  0.1133  -0.0190 890  HOH A O   
8182 O O   . HOH I .   ? 0.4996 0.6091 0.5429 0.0272  0.0984  0.0016  891  HOH A O   
8183 O O   . HOH I .   ? 0.6958 0.8467 0.7652 0.0142  0.1400  -0.0159 892  HOH A O   
8184 O O   . HOH I .   ? 0.6152 0.6706 0.5884 0.0136  0.0571  -0.0848 893  HOH A O   
8185 O O   . HOH I .   ? 0.7353 0.7329 0.7423 -0.0050 0.0839  -0.0044 894  HOH A O   
8186 O O   . HOH I .   ? 0.6806 0.6811 0.6573 0.0450  0.1890  -0.2137 895  HOH A O   
8187 O O   . HOH I .   ? 0.7440 0.6668 0.7603 0.0017  0.1068  -0.1899 896  HOH A O   
8188 O O   . HOH I .   ? 0.5356 0.6074 0.5797 0.0591  0.0612  0.0074  897  HOH A O   
8189 O O   . HOH I .   ? 0.7978 0.8621 1.0275 0.1389  0.1173  -0.0728 898  HOH A O   
8190 O O   . HOH I .   ? 0.7850 0.8071 0.6219 -0.0178 0.0127  -0.0369 899  HOH A O   
8191 O O   . HOH I .   ? 0.5310 0.7751 0.7529 -0.0579 0.0308  -0.0463 900  HOH A O   
8192 O O   . HOH I .   ? 0.7873 0.7418 0.6487 0.0115  0.1097  -0.0476 901  HOH A O   
8193 O O   . HOH I .   ? 0.6272 0.5603 0.6245 -0.0717 0.0871  -0.0647 902  HOH A O   
8194 O O   . HOH I .   ? 0.8575 0.6006 0.7147 -0.0238 0.1848  -0.1723 903  HOH A O   
8195 O O   . HOH I .   ? 0.6734 0.5115 0.6123 -0.0364 0.1205  -0.0891 904  HOH A O   
8196 O O   . HOH I .   ? 0.7733 0.6272 0.8150 -0.1662 0.1123  -0.1086 905  HOH A O   
8197 O O   . HOH I .   ? 0.7722 0.7552 0.8445 0.0361  0.0726  -0.0113 906  HOH A O   
8198 O O   . HOH I .   ? 0.5566 0.6044 0.5176 0.0253  0.0911  0.0389  907  HOH A O   
8199 O O   . HOH I .   ? 0.5768 0.6106 0.5675 0.0307  0.0832  0.0341  908  HOH A O   
8200 O O   . HOH I .   ? 0.8476 0.8728 0.8420 0.0423  0.0754  0.0107  909  HOH A O   
8201 O O   . HOH I .   ? 0.7187 0.6852 0.5532 -0.0293 0.0576  -0.0731 910  HOH A O   
8202 O O   . HOH I .   ? 0.7225 0.7567 0.8102 -0.1713 0.0432  -0.1227 911  HOH A O   
8203 O O   . HOH I .   ? 0.4860 0.5524 0.5065 0.0407  0.0626  0.0126  912  HOH A O   
8204 O O   . HOH I .   ? 0.8063 0.7428 0.7143 -0.0219 0.1379  0.0979  913  HOH A O   
8205 O O   . HOH I .   ? 0.7685 0.8625 0.8792 -0.1936 0.0064  -0.1453 914  HOH A O   
8206 O O   . HOH I .   ? 0.7869 0.7540 0.7583 -0.0567 0.1602  0.0664  915  HOH A O   
8207 O O   . HOH I .   ? 0.7246 0.6762 0.7198 -0.0049 0.0950  -0.1823 916  HOH A O   
8208 O O   . HOH I .   ? 0.5337 0.5109 0.5279 0.0295  0.0891  0.0071  917  HOH A O   
8209 O O   . HOH I .   ? 0.8754 0.8534 0.9419 -0.0174 0.0633  -0.1114 918  HOH A O   
8210 O O   . HOH I .   ? 0.7597 0.7601 0.6515 0.0198  0.0926  0.0819  919  HOH A O   
8211 O O   . HOH I .   ? 0.7207 0.5369 0.7164 -0.0503 0.1299  -0.0345 920  HOH A O   
8212 O O   . HOH I .   ? 0.4462 0.5219 0.4743 0.0444  0.0659  0.0118  921  HOH A O   
8213 O O   . HOH I .   ? 0.6494 0.6862 0.6134 0.0400  0.0553  0.0166  922  HOH A O   
8214 O O   . HOH I .   ? 0.7356 0.6420 0.5452 -0.0209 0.1119  -0.0995 923  HOH A O   
8215 O O   . HOH I .   ? 0.6344 0.7089 0.6406 -0.0242 0.1441  0.0283  924  HOH A O   
8216 O O   . HOH I .   ? 0.4653 0.5807 0.5400 0.0596  0.1074  -0.0361 925  HOH A O   
8217 O O   . HOH I .   ? 0.9191 1.0094 0.9990 -0.0323 0.0973  -0.0033 926  HOH A O   
8218 O O   . HOH I .   ? 0.6491 0.7765 0.6384 0.0005  -0.0333 -0.0121 927  HOH A O   
8219 O O   . HOH I .   ? 0.7990 0.9569 0.8826 -0.0014 0.1467  -0.0109 928  HOH A O   
8220 O O   . HOH I .   ? 0.6561 0.7829 0.6358 -0.0388 -0.0389 -0.0464 929  HOH A O   
8221 O O   . HOH I .   ? 0.7440 0.8695 0.7487 0.0301  -0.0314 0.0131  930  HOH A O   
8222 O O   . HOH I .   ? 0.5165 0.6914 0.6448 0.0043  0.1196  -0.0141 931  HOH A O   
8223 O O   . HOH I .   ? 0.5284 0.7339 0.7042 0.0297  0.0424  -0.0128 932  HOH A O   
8224 O O   . HOH I .   ? 0.5338 0.9096 0.9149 -0.1167 0.0132  -0.0826 933  HOH A O   
8225 O O   . HOH I .   ? 0.8201 0.9840 1.0940 0.1332  0.0854  -0.0390 934  HOH A O   
8226 O O   . HOH I .   ? 0.9108 0.5537 0.8947 -0.0258 0.1790  -0.0849 935  HOH A O   
8227 O O   . HOH I .   ? 0.6435 0.6742 0.5610 0.0125  0.1081  -0.1483 936  HOH A O   
8228 O O   . HOH I .   ? 0.8395 0.9321 0.9179 0.0847  0.0075  0.0359  937  HOH A O   
8229 O O   . HOH I .   ? 0.7520 0.8013 0.6282 -0.0001 0.0861  -0.1356 938  HOH A O   
8230 O O   . HOH I .   ? 0.5757 0.6447 0.5309 0.0165  0.0542  -0.0722 939  HOH A O   
8231 O O   . HOH I .   ? 0.7177 0.6914 0.7885 0.0462  0.0724  -0.0027 940  HOH A O   
8232 O O   . HOH I .   ? 0.4623 0.5251 0.4773 0.0336  0.0760  0.0173  941  HOH A O   
8233 O O   . HOH I .   ? 0.7033 0.8637 0.7617 0.0141  0.1645  -0.0299 942  HOH A O   
8234 O O   . HOH I .   ? 0.6949 0.7855 0.6491 -0.0187 0.1647  0.0227  943  HOH A O   
8235 O O   . HOH I .   ? 0.7715 0.8177 0.8249 0.0602  0.0736  -0.0251 944  HOH A O   
8236 O O   . HOH I .   ? 0.7349 0.7481 0.5966 -0.0438 0.0163  -0.0703 945  HOH A O   
8237 O O   . HOH I .   ? 0.7506 0.7832 0.6586 -0.0344 0.0459  -0.1733 946  HOH A O   
8238 O O   . HOH I .   ? 0.6884 0.9828 0.8690 -0.0105 -0.0937 -0.0274 947  HOH A O   
8239 O O   . HOH I .   ? 0.6207 0.8355 0.7950 0.0368  0.0055  -0.0066 948  HOH A O   
8240 O O   . HOH I .   ? 0.5996 0.8899 0.8822 0.0029  0.0838  -0.0352 949  HOH A O   
8241 O O   . HOH I .   ? 0.6485 0.6521 0.6729 0.0623  0.1933  -0.2040 950  HOH A O   
8242 O O   . HOH I .   ? 0.5350 0.6176 0.5804 0.0566  0.0471  0.0147  951  HOH A O   
8243 O O   . HOH I .   ? 0.6300 0.7354 0.6325 0.0429  0.1371  -0.0648 952  HOH A O   
8244 O O   . HOH I .   ? 0.5040 0.5855 0.5372 0.0544  0.0842  -0.0240 953  HOH A O   
8245 O O   . HOH I .   ? 0.6576 0.7367 0.5867 0.0290  0.1363  -0.0976 954  HOH A O   
8246 O O   . HOH I .   ? 0.5265 0.4842 0.5399 0.0643  0.1163  -0.0041 955  HOH A O   
8247 O O   . HOH I .   ? 0.7336 0.8237 0.6376 0.0219  0.1345  -0.0721 956  HOH A O   
8248 O O   . HOH I .   ? 0.5650 0.8275 0.8277 0.0468  0.0756  -0.0290 957  HOH A O   
8249 O O   . HOH I .   ? 0.7678 0.8436 0.8114 0.0048  0.0345  -0.0571 958  HOH A O   
8250 O O   . HOH I .   ? 0.9499 0.7902 0.9668 -0.2152 0.0885  -0.1792 959  HOH A O   
8251 O O   . HOH I .   ? 0.6607 0.8478 0.7316 0.0108  -0.0511 -0.0072 960  HOH A O   
8252 O O   . HOH I .   ? 0.6754 0.8137 0.7860 0.0670  0.1367  -0.0618 961  HOH A O   
8253 O O   . HOH I .   ? 0.7046 0.8214 0.6447 -0.0060 0.1767  -0.0098 962  HOH A O   
8254 O O   . HOH I .   ? 0.8568 0.8804 0.7551 0.0052  0.1135  0.0641  963  HOH A O   
8255 O O   . HOH I .   ? 0.6747 0.6182 0.6621 -0.0376 0.0882  -0.0433 964  HOH A O   
8256 O O   A HOH I .   ? 0.6391 0.7131 0.6910 -0.0571 0.1552  0.0227  965  HOH A O   
8257 O O   B HOH I .   ? 0.6254 0.7124 0.6818 -0.0579 0.1613  0.0209  965  HOH A O   
8258 O O   . HOH I .   ? 0.6525 0.7775 0.7152 -0.0267 0.1498  0.0073  966  HOH A O   
8259 O O   . HOH I .   ? 0.8852 0.8342 0.9010 -0.0575 0.0947  -0.0360 967  HOH A O   
8260 O O   . HOH I .   ? 0.7733 0.9647 0.9467 0.0822  -0.0161 0.0182  968  HOH A O   
8261 O O   . HOH I .   ? 0.6357 0.7163 0.5767 0.0311  0.0869  0.0046  969  HOH A O   
8262 O O   . HOH I .   ? 0.8070 0.6267 0.6937 -0.0851 0.1093  -0.1493 970  HOH A O   
8263 O O   . HOH I .   ? 0.5618 0.7705 0.7397 0.0385  0.0261  -0.0089 971  HOH A O   
8264 O O   . HOH I .   ? 0.5442 0.5545 0.5443 0.0467  0.0827  0.0128  972  HOH A O   
8265 O O   . HOH I .   ? 0.9810 1.1038 1.0149 0.0708  -0.0488 0.0483  973  HOH A O   
8266 O O   . HOH I .   ? 0.5185 0.5823 0.4851 0.0248  0.0946  0.0283  974  HOH A O   
8267 O O   . HOH I .   ? 0.9833 0.9621 0.8477 -0.0004 0.1165  0.0963  975  HOH A O   
8268 O O   . HOH I .   ? 0.7258 0.6955 0.7814 -0.1005 0.0970  -0.0493 976  HOH A O   
8269 O O   . HOH I .   ? 0.8893 0.8163 1.0566 0.1200  0.2130  -0.2243 977  HOH A O   
8270 O O   . HOH I .   ? 0.6019 0.9032 0.9050 0.0466  0.0307  -0.0243 978  HOH A O   
8271 O O   . HOH I .   ? 0.8689 0.8446 0.6624 -0.0166 0.0560  -0.0510 979  HOH A O   
8272 O O   . HOH I .   ? 0.6274 0.7100 0.5565 0.0286  0.1221  -0.0770 980  HOH A O   
8273 O O   . HOH I .   ? 0.7030 0.5930 0.6983 0.0179  0.1112  0.0100  981  HOH A O   
8274 O O   . HOH I .   ? 0.7319 0.7515 0.7512 -0.0113 0.1010  0.0190  982  HOH A O   
8275 O O   . HOH I .   ? 0.9072 0.9628 0.8520 0.0447  0.0576  0.0454  983  HOH A O   
8276 O O   . HOH I .   ? 0.7874 0.9370 1.0562 0.1320  0.1543  -0.0977 984  HOH A O   
8277 O O   A HOH I .   ? 0.5289 0.5987 0.5509 0.0514  0.0457  0.0180  985  HOH A O   
8278 O O   B HOH I .   ? 0.4731 0.5445 0.5018 0.0535  0.0484  0.0172  985  HOH A O   
8279 O O   . HOH I .   ? 0.5805 0.6955 0.6035 0.0468  0.1510  -0.0748 986  HOH A O   
8280 O O   . HOH I .   ? 0.8726 0.7359 0.8304 0.0406  0.1003  0.1021  987  HOH A O   
8281 O O   . HOH I .   ? 0.5510 0.6541 0.5747 0.0128  0.1149  0.0082  988  HOH A O   
8282 O O   . HOH I .   ? 0.8068 0.8887 0.6102 0.0046  0.0972  -0.0443 989  HOH A O   
8283 O O   . HOH I .   ? 0.9015 0.9763 0.9226 0.0124  0.0375  -0.0550 990  HOH A O   
8284 O O   . HOH I .   ? 0.7363 0.8010 0.6328 0.0059  -0.0113 -0.0037 991  HOH A O   
8285 O O   . HOH I .   ? 0.7597 0.9435 0.8948 -0.0316 0.1577  -0.0122 992  HOH A O   
8286 O O   . HOH I .   ? 0.6425 0.9041 0.8440 0.0200  -0.0338 -0.0142 993  HOH A O   
8287 O O   . HOH I .   ? 1.0544 0.9466 0.9351 -0.1246 0.0590  -0.1640 994  HOH A O   
8288 O O   . HOH I .   ? 0.7923 0.7721 0.6422 0.0140  0.0903  -0.0216 995  HOH A O   
8289 O O   . HOH I .   ? 0.5466 0.7492 0.7137 0.0063  0.1136  -0.0207 996  HOH A O   
8290 O O   . HOH I .   ? 0.9061 0.9425 0.9416 -0.0207 0.0814  -0.0072 997  HOH A O   
8291 O O   A HOH I .   ? 0.6441 0.7156 0.5029 0.0061  0.1214  0.0192  998  HOH A O   
8292 O O   B HOH I .   ? 0.6660 0.7350 0.5339 0.0019  0.1300  0.0258  998  HOH A O   
8293 O O   . HOH I .   ? 0.7273 0.7944 0.7073 0.0425  0.0201  0.0220  999  HOH A O   
8294 O O   . HOH I .   ? 0.7026 0.8486 0.9424 0.1248  0.0763  -0.0294 1000 HOH A O   
8295 O O   . HOH I .   ? 0.6736 0.6218 0.6748 -0.0559 0.0871  -0.0487 1001 HOH A O   
8296 O O   . HOH I .   ? 0.6732 0.9689 0.9715 0.0330  0.0817  -0.0356 1002 HOH A O   
8297 O O   . HOH I .   ? 0.7847 0.7316 0.8522 0.1278  0.0553  0.1006  1003 HOH A O   
8298 O O   . HOH I .   ? 0.8114 0.9378 0.8584 -0.0147 0.1491  0.0051  1004 HOH A O   
8299 O O   . HOH I .   ? 0.6824 0.9874 0.9231 0.0092  -0.0543 -0.0224 1005 HOH A O   
8300 O O   . HOH I .   ? 0.8371 0.9909 1.0646 0.1121  0.1516  -0.0898 1006 HOH A O   
8301 O O   . HOH I .   ? 0.8965 0.9900 0.9794 0.0945  -0.0102 0.0477  1007 HOH A O   
8302 O O   . HOH I .   ? 0.6211 0.8036 0.7475 0.0005  0.1396  -0.0177 1008 HOH A O   
8303 O O   . HOH I .   ? 0.8716 0.8327 0.9436 0.0641  0.0680  0.0128  1009 HOH A O   
8304 O O   . HOH I .   ? 0.6438 0.6024 0.6837 0.0734  0.2404  -0.2719 1010 HOH A O   
8305 O O   . HOH I .   ? 0.6931 0.9406 0.8632 0.0246  -0.0502 -0.0073 1011 HOH A O   
8306 O O   . HOH I .   ? 0.6680 0.8179 0.6885 0.0123  -0.0427 -0.0029 1012 HOH A O   
8307 O O   A HOH I .   ? 0.7456 0.7706 0.5803 -0.0310 0.0042  -0.0513 1013 HOH A O   
8308 O O   B HOH I .   ? 0.6978 0.7277 0.5511 -0.0353 0.0030  -0.0561 1013 HOH A O   
8309 O O   . HOH I .   ? 0.5483 0.9195 0.9195 -0.0537 0.0341  -0.0573 1014 HOH A O   
8310 O O   . HOH I .   ? 0.7825 0.7974 0.8177 -0.0385 0.1149  0.0156  1015 HOH A O   
8311 O O   A HOH I .   ? 0.6237 0.7421 0.6214 -0.0212 0.1740  0.0088  1016 HOH A O   
8312 O O   B HOH I .   ? 0.5969 0.7236 0.6110 -0.0155 0.1683  0.0032  1016 HOH A O   
8313 O O   . HOH I .   ? 0.5532 0.8088 0.8015 -0.0567 0.0656  -0.0414 1017 HOH A O   
8314 O O   . HOH I .   ? 0.9335 0.9810 0.9189 -0.0321 0.1493  0.0416  1018 HOH A O   
8315 O O   . HOH I .   ? 0.9100 0.9758 0.8831 0.0028  0.0408  -0.0875 1019 HOH A O   
8316 O O   . HOH I .   ? 0.6648 0.9252 0.9391 0.0640  0.0833  -0.0330 1020 HOH A O   
8317 O O   . HOH I .   ? 0.7714 0.8322 0.6505 -0.0032 0.0644  -0.1192 1021 HOH A O   
8318 O O   . HOH I .   ? 0.7367 0.8053 0.6392 0.0010  0.0530  -0.1007 1022 HOH A O   
8319 O O   . HOH I .   ? 0.9072 0.9685 0.7672 0.0131  0.1014  0.0331  1023 HOH A O   
8320 O O   . HOH I .   ? 0.5904 0.8871 1.0389 -0.2832 0.1464  -0.1045 1024 HOH A O   
8321 O O   . HOH I .   ? 0.5587 0.5367 0.5799 0.0664  0.1036  0.0094  1025 HOH A O   
8322 O O   . HOH I .   ? 0.5773 0.6924 0.6029 0.0091  0.1281  0.0027  1026 HOH A O   
8323 O O   . HOH I .   ? 0.6644 0.6964 0.6910 -0.0081 0.0909  0.0093  1027 HOH A O   
8324 O O   . HOH I .   ? 0.8612 0.6421 0.8636 -0.1290 0.1304  -0.1015 1028 HOH A O   
8325 O O   A HOH I .   ? 0.7389 0.8054 0.6090 0.0187  0.0912  0.0264  1029 HOH A O   
8326 O O   B HOH I .   ? 0.7366 0.8046 0.6142 0.0240  0.0784  0.0263  1029 HOH A O   
8327 O O   . HOH I .   ? 0.7460 0.8745 0.6955 0.0071  0.1812  -0.0398 1030 HOH A O   
8328 O O   . HOH I .   ? 0.9118 0.9693 0.8061 -0.0344 0.0298  -0.1558 1031 HOH A O   
8329 O O   . HOH I .   ? 0.8810 0.9453 0.7502 0.0096  0.1022  -0.1111 1032 HOH A O   
8330 O O   . HOH I .   ? 0.6914 0.9380 0.9238 -0.0346 0.0712  -0.0333 1033 HOH A O   
8331 O O   . HOH I .   ? 0.8441 0.9871 0.8941 -0.0097 0.1598  -0.0045 1034 HOH A O   
8332 O O   . HOH I .   ? 0.9684 0.7205 0.9845 -0.1167 0.1491  -0.0596 1035 HOH A O   
8333 O O   . HOH I .   ? 0.7986 0.6993 0.9033 0.0735  0.0786  -0.0047 1036 HOH A O   
8334 O O   . HOH I .   ? 0.8574 0.9438 0.7263 0.0144  0.1435  -0.0883 1037 HOH A O   
8335 O O   . HOH I .   ? 0.9702 0.7236 0.9812 -0.1248 0.1438  -0.0814 1038 HOH A O   
8336 O O   A HOH I .   ? 0.5286 0.6091 0.5843 0.0635  0.0490  0.0138  1039 HOH A O   
8337 O O   B HOH I .   ? 0.4912 0.5578 0.5339 0.0631  0.0486  0.0185  1039 HOH A O   
8338 O O   . HOH I .   ? 0.6827 0.6467 0.8574 0.1250  0.2241  -0.2243 1040 HOH A O   
8339 O O   . HOH I .   ? 0.8387 0.9054 0.7604 -0.0031 0.0449  -0.1051 1041 HOH A O   
8340 O O   . HOH J .   ? 0.5508 0.6098 0.6004 0.0604  0.0787  -0.0295 801  HOH B O   
8341 O O   . HOH J .   ? 0.6207 0.7865 0.8154 0.0700  0.0633  0.0198  802  HOH B O   
8342 O O   . HOH J .   ? 0.4736 0.6503 0.7050 0.0581  0.1081  0.0092  803  HOH B O   
8343 O O   . HOH J .   ? 1.2120 1.0621 0.7217 -0.0535 0.2178  -0.1472 804  HOH B O   
8344 O O   . HOH J .   ? 0.6651 0.7454 0.5767 0.0253  0.0918  0.0028  805  HOH B O   
8345 O O   . HOH J .   ? 0.5916 0.7912 0.8026 0.0721  0.0252  0.0241  806  HOH B O   
8346 O O   . HOH J .   ? 0.5989 0.5760 0.7002 0.1067  0.1851  -0.0348 807  HOH B O   
8347 O O   . HOH J .   ? 0.5170 0.6377 0.6549 0.0085  0.0486  -0.0136 808  HOH B O   
8348 O O   . HOH J .   ? 0.9251 0.8219 0.6229 -0.0390 0.1165  -0.1185 809  HOH B O   
8349 O O   . HOH J .   ? 0.8195 0.7492 0.8892 0.1052  0.2687  -0.0995 810  HOH B O   
8350 O O   . HOH J .   ? 0.7492 0.8891 0.7566 0.0019  -0.0136 -0.0476 811  HOH B O   
8351 O O   . HOH J .   ? 0.7924 0.7514 0.6197 0.0114  0.1184  -0.0387 812  HOH B O   
8352 O O   . HOH J .   ? 0.6023 0.6876 0.6929 0.0354  0.2125  -0.0038 813  HOH B O   
8353 O O   . HOH J .   ? 1.0156 0.9835 1.1465 0.1181  0.2999  -0.1119 814  HOH B O   
8354 O O   . HOH J .   ? 0.5277 0.5843 0.6153 0.0179  0.1009  0.0215  815  HOH B O   
8355 O O   . HOH J .   ? 0.6629 0.6750 0.7406 0.0214  0.0699  -0.0124 816  HOH B O   
8356 O O   . HOH J .   ? 0.8134 0.7334 0.8416 0.0916  0.2842  -0.1150 817  HOH B O   
8357 O O   . HOH J .   ? 0.7027 0.6758 0.8951 0.1739  0.0830  0.0704  818  HOH B O   
8358 O O   . HOH J .   ? 0.6754 0.6577 0.8494 0.1478  0.1238  0.0244  819  HOH B O   
8359 O O   . HOH J .   ? 0.5478 0.6155 0.5913 0.0652  0.0602  0.0301  820  HOH B O   
8360 O O   . HOH J .   ? 0.7502 0.7515 0.6521 0.0329  0.0861  0.0310  821  HOH B O   
8361 O O   . HOH J .   ? 0.9879 0.9372 0.8766 0.0132  0.1031  0.1057  822  HOH B O   
8362 O O   . HOH J .   ? 0.6203 0.7085 0.7138 0.0710  0.0747  0.0245  823  HOH B O   
8363 O O   . HOH J .   ? 0.4853 0.9541 1.0254 0.0736  -0.0540 0.0080  824  HOH B O   
8364 O O   . HOH J .   ? 0.6209 0.7001 0.5865 0.0184  0.0436  -0.0561 825  HOH B O   
8365 O O   . HOH J .   ? 0.5713 0.6931 0.7595 0.0797  0.1631  -0.0035 826  HOH B O   
8366 O O   . HOH J .   ? 0.8050 0.6992 0.6298 0.0122  0.1780  -0.1001 827  HOH B O   
8367 O O   . HOH J .   ? 0.7723 0.7598 0.6441 0.0189  0.1626  0.0091  828  HOH B O   
8368 O O   . HOH J .   ? 0.5750 0.6502 0.6507 -0.0014 0.2222  0.0198  829  HOH B O   
8369 O O   . HOH J .   ? 0.7818 0.9241 0.9514 0.0804  0.0634  0.0258  830  HOH B O   
8370 O O   . HOH J .   ? 0.6529 0.6390 0.6735 0.0646  0.0940  0.0186  831  HOH B O   
8371 O O   . HOH J .   ? 0.8276 0.6263 0.6916 0.0363  0.2644  -0.1732 832  HOH B O   
8372 O O   . HOH J .   ? 0.8216 1.0478 1.1781 0.0842  0.2228  -0.0239 833  HOH B O   
8373 O O   . HOH J .   ? 0.6445 0.9337 1.0326 0.1113  0.0410  0.0254  834  HOH B O   
8374 O O   . HOH J .   ? 0.4565 0.8140 0.9236 0.0003  0.0732  -0.0209 835  HOH B O   
8375 O O   . HOH J .   ? 0.7963 0.8807 0.9666 0.1299  0.0548  0.0567  836  HOH B O   
8376 O O   . HOH J .   ? 0.5858 0.6272 0.5525 0.0454  0.0437  0.0264  837  HOH B O   
8377 O O   . HOH J .   ? 0.4772 0.7483 0.8688 0.0645  0.1631  -0.0088 838  HOH B O   
8378 O O   . HOH J .   ? 0.4691 0.5125 0.4757 0.0460  0.0694  0.0171  839  HOH B O   
8379 O O   . HOH J .   ? 0.6582 0.6114 0.6801 0.0793  0.2026  -0.0582 840  HOH B O   
8380 O O   . HOH J .   ? 0.4447 0.6043 0.5291 0.0493  -0.0043 0.0164  841  HOH B O   
8381 O O   . HOH J .   ? 0.8398 0.6587 0.8480 0.0951  0.2949  -0.1555 842  HOH B O   
8382 O O   . HOH J .   ? 0.7355 0.6991 0.5588 -0.0074 0.0790  -0.0531 843  HOH B O   
8383 O O   . HOH J .   ? 0.4458 0.5274 0.4065 0.0365  0.0733  -0.0208 844  HOH B O   
8384 O O   . HOH J .   ? 0.8701 0.6460 0.7071 -0.0559 0.1484  -0.1722 845  HOH B O   
8385 O O   . HOH J .   ? 0.7445 0.6024 0.7752 0.0735  0.1270  0.0109  846  HOH B O   
8386 O O   . HOH J .   ? 0.5365 0.7908 0.7479 0.0531  -0.0366 0.0155  847  HOH B O   
8387 O O   . HOH J .   ? 0.5156 0.5782 0.6218 0.0076  0.1128  0.0216  848  HOH B O   
8388 O O   . HOH J .   ? 0.5254 0.5114 0.5496 0.0685  0.1105  0.0035  849  HOH B O   
8389 O O   . HOH J .   ? 0.7924 0.8841 0.9436 0.0903  0.1214  0.0105  850  HOH B O   
8390 O O   . HOH J .   ? 0.6837 0.6140 0.5970 0.0475  0.2348  -0.0891 851  HOH B O   
8391 O O   . HOH J .   ? 0.6347 0.9064 1.0263 0.1236  0.0612  0.0249  852  HOH B O   
8392 O O   . HOH J .   ? 0.8835 0.6890 0.6984 0.0158  0.2462  -0.1737 853  HOH B O   
8393 O O   . HOH J .   ? 0.5421 0.7305 0.8045 -0.0063 0.2572  -0.0036 854  HOH B O   
8394 O O   . HOH J .   ? 0.7956 0.7577 0.9812 0.1473  0.2217  -0.0520 855  HOH B O   
8395 O O   . HOH J .   ? 0.6178 0.6408 0.7819 0.1339  0.1068  0.0302  856  HOH B O   
8396 O O   . HOH J .   ? 0.9325 0.8968 0.9376 0.0711  0.3221  -0.1229 857  HOH B O   
8397 O O   . HOH J .   ? 0.4947 0.9259 1.0684 0.0465  0.0751  -0.0148 858  HOH B O   
8398 O O   . HOH J .   ? 0.5381 0.5901 0.5815 0.0611  0.0596  0.0105  859  HOH B O   
8399 O O   . HOH J .   ? 0.4765 0.6054 0.6430 0.0482  0.1396  0.0085  860  HOH B O   
8400 O O   . HOH J .   ? 0.4815 0.5390 0.5487 0.0174  0.1391  0.0279  861  HOH B O   
8401 O O   A HOH J .   ? 0.4792 0.5335 0.4980 0.0595  0.0442  0.0270  862  HOH B O   
8402 O O   B HOH J .   ? 0.4756 0.5375 0.5021 0.0579  0.0483  0.0212  862  HOH B O   
8403 O O   . HOH J .   ? 0.5827 0.6076 0.6365 0.0422  0.0672  0.0062  863  HOH B O   
8404 O O   . HOH J .   ? 0.4937 0.7384 0.8420 0.0097  0.1939  -0.0076 864  HOH B O   
8405 O O   . HOH J .   ? 0.6670 0.6635 0.5698 0.0274  0.0892  -0.0065 865  HOH B O   
8406 O O   . HOH J .   ? 0.6555 0.6517 0.6618 0.0121  0.1250  0.0516  866  HOH B O   
8407 O O   . HOH J .   ? 0.5662 0.5430 0.6190 0.0850  0.1111  0.0127  867  HOH B O   
8408 O O   . HOH J .   ? 0.4800 0.5636 0.5112 0.0337  0.0433  -0.0156 868  HOH B O   
8409 O O   . HOH J .   ? 0.4663 0.5048 0.5305 0.0137  0.1189  0.0321  869  HOH B O   
8410 O O   . HOH J .   ? 0.5708 0.6407 0.5790 0.0310  0.0521  -0.0367 870  HOH B O   
8411 O O   . HOH J .   ? 0.4715 0.5119 0.4731 0.0540  0.0660  0.0368  871  HOH B O   
8412 O O   . HOH J .   ? 0.5348 0.5127 0.5110 0.0477  0.1123  -0.0134 872  HOH B O   
8413 O O   . HOH J .   ? 0.5362 0.6151 0.5066 0.0263  0.0498  -0.0432 873  HOH B O   
8414 O O   . HOH J .   ? 0.6041 0.6090 0.6320 0.0878  0.0565  0.0696  874  HOH B O   
8415 O O   . HOH J .   ? 0.5547 0.6521 0.7015 -0.0199 0.2033  0.0245  875  HOH B O   
8416 O O   . HOH J .   ? 0.5100 0.7247 0.7738 -0.0107 0.0450  -0.0210 876  HOH B O   
8417 O O   . HOH J .   ? 0.4936 0.5845 0.5331 0.0525  0.0804  -0.0091 877  HOH B O   
8418 O O   . HOH J .   ? 0.5327 0.5656 0.5381 0.0445  0.0737  0.0221  878  HOH B O   
8419 O O   . HOH J .   ? 0.6168 0.6343 0.6437 0.0527  0.0643  0.0298  879  HOH B O   
8420 O O   . HOH J .   ? 0.5805 0.6060 0.5501 0.0243  0.1823  0.0114  880  HOH B O   
8421 O O   . HOH J .   ? 0.6153 0.8867 0.8653 0.0854  -0.0466 0.0390  881  HOH B O   
8422 O O   . HOH J .   ? 0.6665 0.5995 0.6443 0.0675  0.2225  -0.0793 882  HOH B O   
8423 O O   . HOH J .   ? 0.4611 0.5049 0.4817 0.0580  0.0712  0.0252  883  HOH B O   
8424 O O   . HOH J .   ? 0.5663 0.6014 0.5690 0.0397  0.1911  -0.0075 884  HOH B O   
8425 O O   . HOH J .   ? 0.4273 0.5056 0.5241 0.0164  0.1495  0.0224  885  HOH B O   
8426 O O   . HOH J .   ? 0.5257 0.5699 0.5680 0.0514  0.0629  0.0062  886  HOH B O   
8427 O O   . HOH J .   ? 0.6259 0.6555 0.6282 0.0409  0.0758  0.0264  887  HOH B O   
8428 O O   . HOH J .   ? 0.6190 0.5279 0.6693 0.0896  0.1401  -0.0101 888  HOH B O   
8429 O O   . HOH J .   ? 0.5044 0.5865 0.5520 0.0587  0.0541  0.0239  889  HOH B O   
8430 O O   . HOH J .   ? 0.4095 0.5531 0.6005 0.0382  0.1651  0.0047  890  HOH B O   
8431 O O   . HOH J .   ? 0.4165 0.4848 0.4448 0.0522  0.0668  -0.0067 891  HOH B O   
8432 O O   . HOH J .   ? 0.4966 0.8257 0.8216 0.0214  -0.0392 -0.0119 892  HOH B O   
8433 O O   . HOH J .   ? 0.6406 0.6746 0.6969 0.0667  0.2168  -0.0354 893  HOH B O   
8434 O O   . HOH J .   ? 0.6085 0.6162 0.6617 -0.0183 0.1644  0.0511  894  HOH B O   
8435 O O   . HOH J .   ? 0.5889 0.5496 0.6221 0.0751  0.1116  0.0083  895  HOH B O   
8436 O O   . HOH J .   ? 0.5713 0.6298 0.5716 0.0597  0.0513  0.0417  896  HOH B O   
8437 O O   . HOH J .   ? 0.5544 0.5118 0.5661 0.0726  0.1731  -0.0418 897  HOH B O   
8438 O O   . HOH J .   ? 0.5358 0.5523 0.4862 0.0417  0.0759  0.0330  898  HOH B O   
8439 O O   . HOH J .   ? 0.5482 0.5798 0.6016 0.0230  0.1006  0.0304  899  HOH B O   
8440 O O   . HOH J .   ? 0.5534 0.6170 0.6129 0.0707  0.0710  0.0282  900  HOH B O   
8441 O O   . HOH J .   ? 0.8902 0.9722 0.9679 0.1010  0.0225  0.0692  901  HOH B O   
8442 O O   . HOH J .   ? 0.7415 0.7728 0.7498 0.0785  0.0449  0.0688  902  HOH B O   
8443 O O   . HOH J .   ? 0.5375 0.5364 0.5049 0.0435  0.1004  -0.0048 903  HOH B O   
8444 O O   . HOH J .   ? 0.4753 0.6336 0.5423 0.0388  -0.0085 0.0053  904  HOH B O   
8445 O O   . HOH J .   ? 0.7574 0.6405 0.5985 0.0255  0.2198  -0.1159 905  HOH B O   
8446 O O   . HOH J .   ? 0.5050 0.5948 0.5711 0.0631  0.0546  0.0261  906  HOH B O   
8447 O O   . HOH J .   ? 0.4838 0.5190 0.5005 0.0592  0.0706  0.0307  907  HOH B O   
8448 O O   . HOH J .   ? 0.4814 0.5212 0.5473 0.0770  0.1018  0.0156  908  HOH B O   
8449 O O   . HOH J .   ? 0.4654 0.5995 0.6449 0.0468  0.1779  0.0004  909  HOH B O   
8450 O O   . HOH J .   ? 0.8855 0.7515 0.7000 0.0262  0.2747  -0.1485 910  HOH B O   
8451 O O   . HOH J .   ? 0.7672 0.6406 0.5948 0.0033  0.1661  -0.1124 911  HOH B O   
8452 O O   . HOH J .   ? 0.6851 0.7052 0.7407 0.0323  0.0773  0.0192  912  HOH B O   
8453 O O   . HOH J .   ? 0.6934 0.8340 0.8428 0.0730  0.0514  0.0260  913  HOH B O   
8454 O O   . HOH J .   ? 0.5332 0.5441 0.5272 0.0308  0.1020  0.0423  914  HOH B O   
8455 O O   . HOH J .   ? 0.5380 0.5753 0.5867 0.0494  0.0642  -0.0054 915  HOH B O   
8456 O O   . HOH J .   ? 0.4462 0.5440 0.4480 0.0436  0.0317  0.0080  916  HOH B O   
8457 O O   . HOH J .   ? 0.4728 0.6020 0.5665 0.0536  0.0315  0.0178  917  HOH B O   
8458 O O   . HOH J .   ? 0.6434 0.7126 0.6910 0.0600  0.0734  -0.0149 918  HOH B O   
8459 O O   . HOH J .   ? 0.7526 0.8374 0.8630 0.0054  0.0519  -0.0216 919  HOH B O   
8460 O O   . HOH J .   ? 1.0240 0.9465 0.8772 0.0122  0.1031  0.1307  920  HOH B O   
8461 O O   . HOH J .   ? 0.7228 0.7901 0.7991 0.0913  0.0486  0.0513  921  HOH B O   
8462 O O   . HOH J .   ? 0.6408 0.6309 0.5416 0.0154  0.1493  0.0395  922  HOH B O   
8463 O O   . HOH J .   ? 0.4378 0.6510 0.6708 0.0141  0.0301  -0.0102 923  HOH B O   
8464 O O   . HOH J .   ? 0.4487 0.5091 0.4868 0.0548  0.0679  -0.0120 924  HOH B O   
8465 O O   . HOH J .   ? 0.7239 0.7738 0.7877 0.0860  0.0611  0.0451  925  HOH B O   
8466 O O   . HOH J .   ? 0.6745 0.7901 0.5619 0.0375  -0.0183 0.0337  926  HOH B O   
8467 O O   . HOH J .   ? 0.5199 0.6903 0.7676 0.0693  0.1638  -0.0024 927  HOH B O   
8468 O O   A HOH J .   ? 0.5085 0.5878 0.6423 0.0806  0.1682  -0.0088 928  HOH B O   
8469 O O   B HOH J .   ? 0.5126 0.6076 0.6642 0.0778  0.1765  -0.0097 928  HOH B O   
8470 O O   . HOH J .   ? 0.7704 0.7073 0.7927 0.1064  0.0561  0.1056  929  HOH B O   
8471 O O   . HOH J .   ? 0.4584 0.8067 0.8294 0.0771  -0.0423 0.0219  930  HOH B O   
8472 O O   . HOH J .   ? 0.6283 0.9452 1.0956 0.0649  0.1945  -0.0194 931  HOH B O   
8473 O O   . HOH J .   ? 0.7288 0.8000 0.8560 -0.0135 0.1582  0.0278  932  HOH B O   
8474 O O   . HOH J .   ? 1.0101 0.7443 0.7965 -0.0770 0.1623  -0.2189 933  HOH B O   
8475 O O   . HOH J .   ? 0.5362 0.5289 0.4811 0.0147  0.1388  0.0513  934  HOH B O   
8476 O O   . HOH J .   ? 0.6462 0.8837 0.8167 -0.0033 -0.0422 -0.0343 935  HOH B O   
8477 O O   . HOH J .   ? 0.5240 0.6048 0.4567 0.0265  0.0646  -0.0426 936  HOH B O   
8478 O O   . HOH J .   ? 0.7450 0.8713 0.8893 -0.0105 0.0331  -0.0357 937  HOH B O   
8479 O O   . HOH J .   ? 0.5365 0.6142 0.6124 0.0178  0.0470  -0.0230 938  HOH B O   
8480 O O   . HOH J .   ? 0.7609 0.7385 0.5908 0.0177  0.1202  0.0161  939  HOH B O   
8481 O O   . HOH J .   ? 0.5067 0.7310 0.8261 -0.0019 0.1594  -0.0031 940  HOH B O   
8482 O O   . HOH J .   ? 0.5480 0.6752 0.5942 0.0710  -0.0018 0.0467  941  HOH B O   
8483 O O   . HOH J .   ? 0.7304 0.7095 0.6114 0.0241  0.2587  -0.0533 942  HOH B O   
8484 O O   . HOH J .   ? 0.9136 0.7904 1.0059 0.1220  0.3076  -0.1422 943  HOH B O   
8485 O O   . HOH J .   ? 0.8546 0.8016 0.6256 -0.0181 0.0856  -0.0683 944  HOH B O   
8486 O O   . HOH J .   ? 0.4742 0.7074 0.6458 0.0406  -0.0346 0.0065  945  HOH B O   
8487 O O   . HOH J .   ? 0.6960 0.7806 0.6441 0.0271  0.0499  -0.0347 946  HOH B O   
8488 O O   . HOH J .   ? 0.7944 0.7008 0.5825 -0.0510 0.0847  -0.1217 947  HOH B O   
8489 O O   . HOH J .   ? 0.7264 0.7618 0.7756 0.0593  0.0626  0.0058  948  HOH B O   
8490 O O   . HOH J .   ? 0.6056 0.5476 0.6488 0.0888  0.1942  -0.0533 949  HOH B O   
8491 O O   . HOH J .   ? 0.6499 0.5521 0.6907 0.0862  0.1545  -0.0277 950  HOH B O   
8492 O O   . HOH J .   ? 1.0069 0.9564 1.0671 0.0955  0.3134  -0.1264 951  HOH B O   
8493 O O   A HOH J .   ? 0.5399 0.6895 0.7589 -0.0121 0.0904  -0.0058 952  HOH B O   
8494 O O   B HOH J .   ? 0.6946 0.8310 0.8987 -0.0154 0.0793  -0.0109 952  HOH B O   
8495 O O   . HOH J .   ? 0.5807 0.6092 0.6814 0.0892  0.2127  -0.0403 953  HOH B O   
8496 O O   . HOH J .   ? 0.9049 0.8889 0.7961 0.0473  0.0588  0.1069  954  HOH B O   
8497 O O   . HOH J .   ? 0.7610 0.8596 0.8226 0.0129  0.0297  -0.0343 955  HOH B O   
8498 O O   . HOH J .   ? 1.2448 1.0109 0.9510 -0.1650 0.0936  -0.2790 956  HOH B O   
8499 O O   . HOH J .   ? 0.9230 0.8896 0.6972 0.0098  0.1041  0.0178  957  HOH B O   
8500 O O   . HOH J .   ? 0.7492 1.0062 1.1167 -0.0044 0.1723  -0.0082 958  HOH B O   
8501 O O   . HOH J .   ? 0.5827 0.7591 0.6447 0.0361  -0.0283 0.0046  959  HOH B O   
8502 O O   . HOH J .   ? 0.5026 0.5534 0.5018 0.0350  0.0786  0.0263  960  HOH B O   
8503 O O   . HOH J .   ? 0.6980 0.7263 0.6883 0.0376  0.2636  -0.0404 961  HOH B O   
8504 O O   . HOH J .   ? 1.2347 1.1028 0.9062 -0.0105 0.3060  -0.1604 962  HOH B O   
8505 O O   . HOH J .   ? 0.7220 0.7577 0.9197 0.1329  0.1843  -0.0220 963  HOH B O   
8506 O O   . HOH J .   ? 0.6943 0.8139 0.7940 0.0684  0.0399  0.0291  964  HOH B O   
8507 O O   . HOH J .   ? 0.5360 0.5808 0.5783 0.0465  0.0648  -0.0203 965  HOH B O   
8508 O O   . HOH J .   ? 0.4815 0.6779 0.7596 0.0388  0.2190  -0.0110 966  HOH B O   
8509 O O   . HOH J .   ? 0.5108 0.5213 0.4956 0.0190  0.1319  0.0436  967  HOH B O   
8510 O O   . HOH J .   ? 0.8209 0.8623 0.9166 0.0792  0.2509  -0.0529 968  HOH B O   
8511 O O   . HOH J .   ? 1.0703 0.9369 0.7948 -0.0008 0.2529  -0.1438 969  HOH B O   
8512 O O   . HOH J .   ? 0.7558 0.8433 0.9165 0.1097  0.0856  0.0312  970  HOH B O   
8513 O O   . HOH J .   ? 0.5445 1.0033 1.0708 -0.0003 -0.0333 -0.0309 971  HOH B O   
8514 O O   . HOH J .   ? 0.5096 0.6103 0.5764 0.0589  0.0453  0.0233  972  HOH B O   
8515 O O   . HOH J .   ? 0.8252 0.6499 0.8055 0.0568  0.1824  -0.0812 973  HOH B O   
8516 O O   . HOH J .   ? 0.6694 0.6755 0.6567 0.0466  0.0705  0.0452  974  HOH B O   
8517 O O   . HOH J .   ? 0.5197 0.4994 0.5235 0.0600  0.1156  -0.0065 975  HOH B O   
8518 O O   . HOH J .   ? 0.9452 0.6562 0.7506 0.0093  0.2827  -0.2365 976  HOH B O   
8519 O O   . HOH J .   ? 0.6191 0.7366 0.7801 0.0557  0.2003  -0.0092 977  HOH B O   
8520 O O   . HOH J .   ? 0.8340 0.9298 0.8856 -0.0046 0.0209  -0.0615 978  HOH B O   
8521 O O   . HOH J .   ? 0.7082 0.6947 0.5918 0.0081  0.1733  0.0359  979  HOH B O   
8522 O O   . HOH J .   ? 0.6979 0.8441 0.9307 -0.0222 0.1446  0.0065  980  HOH B O   
8523 O O   . HOH J .   ? 0.5438 0.7174 0.7177 0.0688  0.0301  0.0244  981  HOH B O   
8524 O O   . HOH J .   ? 0.7803 0.8641 0.8300 0.0665  0.0475  0.0330  982  HOH B O   
8525 O O   . HOH J .   ? 0.5852 0.8682 0.9025 0.1013  -0.0176 0.0384  983  HOH B O   
8526 O O   . HOH J .   ? 0.8234 0.7198 1.0532 0.1789  0.2541  -0.0797 984  HOH B O   
8527 O O   . HOH J .   ? 0.8580 0.7292 0.9771 0.1339  0.1512  0.0036  985  HOH B O   
8528 O O   . HOH J .   ? 0.5590 0.6602 0.5683 0.0240  0.0256  -0.0272 986  HOH B O   
8529 O O   . HOH J .   ? 0.7308 0.7773 0.7287 0.0169  0.2569  -0.0104 987  HOH B O   
8530 O O   A HOH J .   ? 0.5216 0.6308 0.6993 -0.0097 0.1237  0.0109  988  HOH B O   
8531 O O   B HOH J .   ? 0.5079 0.6038 0.6687 -0.0071 0.1194  0.0127  988  HOH B O   
8532 O O   . HOH J .   ? 0.8432 0.6463 0.6880 0.0358  0.2868  -0.1854 989  HOH B O   
8533 O O   . HOH J .   ? 0.5389 0.5639 0.5415 0.0428  0.0757  0.0169  990  HOH B O   
8534 O O   . HOH J .   ? 0.7602 0.9058 0.9846 -0.0152 0.1194  0.0023  991  HOH B O   
8535 O O   . HOH J .   ? 0.5690 0.6031 0.6391 -0.0142 0.1700  0.0421  992  HOH B O   
8536 O O   . HOH J .   ? 0.6535 1.0959 1.0959 -0.0159 -0.0884 -0.0410 993  HOH B O   
8537 O O   . HOH J .   ? 0.8379 0.7981 1.1586 0.1989  0.3382  -0.1430 994  HOH B O   
8538 O O   . HOH J .   ? 0.7611 0.8009 0.8118 0.0563  0.0664  -0.0103 995  HOH B O   
8539 O O   . HOH J .   ? 0.5457 0.5803 0.5944 0.0421  0.0683  0.0132  996  HOH B O   
8540 O O   A HOH J .   ? 0.5884 0.5996 0.7823 0.1432  0.1567  -0.0034 997  HOH B O   
8541 O O   B HOH J .   ? 0.5891 0.6000 0.7971 0.1530  0.1418  0.0098  997  HOH B O   
8542 O O   . HOH J .   ? 0.6175 0.6510 0.6631 0.0634  0.0583  0.0165  998  HOH B O   
8543 O O   . HOH J .   ? 0.6700 0.7353 0.7155 0.0627  0.0547  0.0137  999  HOH B O   
8544 O O   . HOH J .   ? 0.7702 0.7598 0.6490 0.0069  0.1920  0.0239  1000 HOH B O   
8545 O O   . HOH J .   ? 0.7264 0.8439 0.7971 0.0068  0.0178  -0.0379 1001 HOH B O   
8546 O O   . HOH J .   ? 0.6780 0.7258 0.7834 0.0981  0.0884  0.0300  1002 HOH B O   
8547 O O   . HOH J .   ? 0.8512 0.7357 0.7889 0.0264  0.1032  0.1056  1003 HOH B O   
8548 O O   . HOH J .   ? 0.9322 0.9430 0.9727 0.0164  0.1093  0.0397  1004 HOH B O   
8549 O O   A HOH J .   ? 0.5391 0.5354 0.4866 0.0291  0.1057  0.0489  1005 HOH B O   
8550 O O   B HOH J .   ? 0.5687 0.5607 0.4946 0.0300  0.1011  0.0498  1005 HOH B O   
8551 O O   . HOH J .   ? 0.8438 0.9173 0.7727 0.0320  0.0770  0.0176  1006 HOH B O   
8552 O O   . HOH J .   ? 0.7950 0.8564 0.8480 0.0729  0.0632  0.0344  1007 HOH B O   
8553 O O   . HOH J .   ? 0.6604 0.7753 0.7597 0.0021  0.0263  -0.0359 1008 HOH B O   
8554 O O   . HOH J .   ? 0.8069 0.7620 1.0024 0.1566  0.1817  -0.0198 1009 HOH B O   
8555 O O   . HOH J .   ? 0.6170 0.7557 0.7957 0.0068  0.2422  0.0013  1010 HOH B O   
8556 O O   . HOH J .   ? 0.5159 0.5196 0.4891 0.0256  0.1146  0.0462  1011 HOH B O   
8557 O O   . HOH J .   ? 0.7021 0.7991 0.9264 0.1183  0.1761  -0.0134 1012 HOH B O   
8558 O O   . HOH J .   ? 0.6202 0.6622 0.7176 0.0808  0.2230  -0.0402 1013 HOH B O   
8559 O O   . HOH J .   ? 0.7302 0.7384 0.7438 0.0245  0.1059  0.0434  1014 HOH B O   
8560 O O   . HOH J .   ? 0.8115 0.8153 0.9690 0.1240  0.1987  -0.0358 1015 HOH B O   
8561 O O   . HOH J .   ? 0.8672 0.8772 0.9072 0.0518  0.0657  0.0239  1016 HOH B O   
8562 O O   . HOH J .   ? 0.7562 0.9347 1.0284 -0.0365 0.2327  0.0073  1017 HOH B O   
8563 O O   . HOH J .   ? 0.6181 0.8077 0.8350 0.0755  0.0440  0.0232  1018 HOH B O   
8564 O O   . HOH J .   ? 0.5546 0.7549 0.7813 -0.0025 0.0317  -0.0202 1019 HOH B O   
8565 O O   . HOH J .   ? 0.6004 0.7785 0.8541 -0.0281 0.2695  0.0034  1020 HOH B O   
8566 O O   A HOH J .   ? 0.6784 0.8662 0.7164 0.0151  -0.0468 -0.0190 1021 HOH B O   
8567 O O   B HOH J .   ? 0.6610 0.8544 0.7174 0.0191  -0.0460 -0.0140 1021 HOH B O   
8568 O O   . HOH J .   ? 0.6189 0.6426 0.5869 0.0300  0.1888  -0.0001 1022 HOH B O   
8569 O O   . HOH J .   ? 0.8036 0.8232 0.8420 0.0461  0.0691  0.0231  1023 HOH B O   
8570 O O   . HOH J .   ? 0.7749 0.9041 0.8826 -0.0100 0.0142  -0.0487 1024 HOH B O   
8571 O O   . HOH J .   ? 0.5246 0.6420 0.6123 0.0597  0.0392  0.0230  1025 HOH B O   
8572 O O   . HOH J .   ? 0.9794 0.7024 0.8299 0.0183  0.2602  -0.2066 1026 HOH B O   
8573 O O   . HOH J .   ? 0.6982 0.9513 0.8546 0.0022  -0.0630 -0.0293 1027 HOH B O   
8574 O O   . HOH J .   ? 0.6224 0.6366 0.5753 0.0446  0.0664  0.0404  1028 HOH B O   
8575 O O   . HOH J .   ? 0.5951 0.7788 0.8489 0.0234  0.2406  -0.0100 1029 HOH B O   
8576 O O   . HOH J .   ? 0.6426 0.6951 0.7317 0.0859  0.0922  0.0234  1030 HOH B O   
8577 O O   . HOH J .   ? 0.7799 0.8889 0.9600 -0.0161 0.1513  0.0164  1031 HOH B O   
8578 O O   . HOH J .   ? 0.6816 0.6328 0.7670 0.1053  0.2010  -0.0505 1032 HOH B O   
8579 O O   . HOH J .   ? 0.8575 0.8728 0.9052 0.0258  0.0909  0.0310  1033 HOH B O   
8580 O O   . HOH J .   ? 0.8815 0.8874 0.9336 0.0436  0.0699  0.0151  1034 HOH B O   
8581 O O   . HOH J .   ? 0.7447 0.8215 0.7679 0.0214  0.0410  -0.0404 1035 HOH B O   
8582 O O   . HOH J .   ? 0.5641 0.5995 0.5641 0.0333  0.0795  0.0277  1036 HOH B O   
8583 O O   . HOH J .   ? 0.7016 0.7004 0.6740 0.0351  0.0911  0.0491  1037 HOH B O   
8584 O O   . HOH J .   ? 0.5491 0.8760 0.9091 0.0956  -0.0348 0.0334  1038 HOH B O   
8585 O O   . HOH J .   ? 0.5708 0.7294 0.7958 0.0572  0.1850  -0.0053 1039 HOH B O   
8586 O O   . HOH J .   ? 0.6600 0.9153 0.8087 0.0170  -0.0682 -0.0140 1040 HOH B O   
8587 O O   . HOH J .   ? 0.5339 0.8037 0.9201 0.0236  0.2061  -0.0135 1041 HOH B O   
8588 O O   . HOH J .   ? 0.6896 0.7005 0.6137 0.0380  0.0740  0.0313  1042 HOH B O   
8589 O O   A HOH J .   ? 0.5815 0.7297 0.7639 -0.0161 0.0379  -0.0317 1043 HOH B O   
8590 O O   B HOH J .   ? 0.5418 0.6828 0.7181 -0.0095 0.0455  -0.0243 1043 HOH B O   
8591 O O   . HOH J .   ? 0.8283 0.9297 1.0280 0.1026  0.1716  -0.0106 1044 HOH B O   
8592 O O   . HOH J .   ? 0.9530 1.0371 1.0477 0.0052  0.0434  -0.0318 1045 HOH B O   
8593 O O   . HOH J .   ? 0.6995 0.8955 0.7809 0.0424  -0.0419 0.0128  1046 HOH B O   
8594 O O   . HOH J .   ? 0.7174 0.9241 0.8033 0.0570  -0.0574 0.0313  1047 HOH B O   
8595 O O   . HOH J .   ? 0.9034 1.0125 1.0698 0.0710  0.2031  -0.0165 1048 HOH B O   
8596 O O   . HOH J .   ? 0.7742 0.7916 0.6762 0.0308  0.0536  0.0178  1049 HOH B O   
8597 O O   . HOH J .   ? 0.6047 0.6640 0.6151 0.0562  0.0381  0.0270  1050 HOH B O   
8598 O O   . HOH J .   ? 0.6185 0.7924 0.8657 0.0495  0.2137  -0.0114 1051 HOH B O   
# 
