data_8ZK8
# 
_entry.id   8ZK8 
# 
_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   8ZK8         pdb_00008zk8 10.2210/pdb8zk8/pdb 
WWPDB D_1300047936 ?            ?                   
# 
_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       2025-05-21 
_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                        8ZK8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-15 
_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              zhanghb@qibebt.ac.cn 
_pdbx_contact_author.name_first         Haibo 
_pdbx_contact_author.name_last          Zhang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3728-9840 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Dong, S.'  1 0000-0002-0452-5221 
'Liu, L.'   2 0000-0002-9684-4325 
'Zhang, H.' 3 0000-0003-3728-9840 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of the Decarboxylase KDC4427 mutant E468L in complex with  indole-3-pyruvic acid' 
_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 'Dong, S.'  1 0000-0002-0452-5221 
primary 'Liu, L.'   2 0000-0002-9684-4325 
primary 'Zhang, H.' 3 0000-0003-3728-9840 
# 
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 'Indolepyruvate decarboxylase'          61941.367 2   ? E468L ? ? 
2 non-polymer syn 'THIAMINE DIPHOSPHATE'                  425.314   2   ? ?     ? ? 
3 non-polymer syn 'MAGNESIUM ION'                         24.305    2   ? ?     ? ? 
4 non-polymer syn '3-(1H-INDOL-3-YL)-2-OXOPROPANOIC ACID' 203.194   2   ? ?     ? ? 
5 water       nat water                                   18.015    451 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        KDC4427 
# 
_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       
;MGSSHHHHHHSQDPMRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCK
GFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNAC
YEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLK
HALQKWVKDVPMAHATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIE
VQPHASRVGDVWFTGIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTS
AFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYT
VLRAIHGPEQRYNDIALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKAL
EARNSA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPMRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCK
GFAALLTTFGVGELSAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNAC
YEIDRVLTTMLRERRPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLK
HALQKWVKDVPMAHATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIE
VQPHASRVGDVWFTGIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTS
AFGAIDLRLPADVNFIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYT
VLRAIHGPEQRYNDIALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKAL
EARNSA
;
_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 'THIAMINE DIPHOSPHATE'                  TPP 
3 'MAGNESIUM ION'                         MG  
4 '3-(1H-INDOL-3-YL)-2-OXOPROPANOIC ACID' 3IO 
5 water                                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  MET n 
1 16  ARG n 
1 17  THR n 
1 18  PRO n 
1 19  TYR n 
1 20  CYS n 
1 21  VAL n 
1 22  ALA n 
1 23  ASP n 
1 24  TYR n 
1 25  LEU n 
1 26  LEU n 
1 27  ASP n 
1 28  ARG n 
1 29  LEU n 
1 30  THR n 
1 31  ASP n 
1 32  CYS n 
1 33  GLY n 
1 34  ALA n 
1 35  ASP n 
1 36  HIS n 
1 37  LEU n 
1 38  PHE n 
1 39  GLY n 
1 40  VAL n 
1 41  PRO n 
1 42  GLY n 
1 43  ASP n 
1 44  TYR n 
1 45  ASN n 
1 46  LEU n 
1 47  GLN n 
1 48  PHE n 
1 49  LEU n 
1 50  ASP n 
1 51  HIS n 
1 52  VAL n 
1 53  ILE n 
1 54  ASP n 
1 55  SER n 
1 56  PRO n 
1 57  ASP n 
1 58  ILE n 
1 59  CYS n 
1 60  TRP n 
1 61  VAL n 
1 62  GLY n 
1 63  CYS n 
1 64  ALA n 
1 65  ASN n 
1 66  GLU n 
1 67  LEU n 
1 68  ASN n 
1 69  ALA n 
1 70  SER n 
1 71  TYR n 
1 72  ALA n 
1 73  ALA n 
1 74  ASP n 
1 75  GLY n 
1 76  TYR n 
1 77  ALA n 
1 78  ARG n 
1 79  CYS n 
1 80  LYS n 
1 81  GLY n 
1 82  PHE n 
1 83  ALA n 
1 84  ALA n 
1 85  LEU n 
1 86  LEU n 
1 87  THR n 
1 88  THR n 
1 89  PHE n 
1 90  GLY n 
1 91  VAL n 
1 92  GLY n 
1 93  GLU n 
1 94  LEU n 
1 95  SER n 
1 96  ALA n 
1 97  MET n 
1 98  ASN n 
1 99  GLY n 
1 100 ILE n 
1 101 ALA n 
1 102 GLY n 
1 103 SER n 
1 104 TYR n 
1 105 ALA n 
1 106 GLU n 
1 107 HIS n 
1 108 VAL n 
1 109 PRO n 
1 110 VAL n 
1 111 LEU n 
1 112 HIS n 
1 113 ILE n 
1 114 VAL n 
1 115 GLY n 
1 116 ALA n 
1 117 PRO n 
1 118 GLY n 
1 119 THR n 
1 120 ALA n 
1 121 SER n 
1 122 GLN n 
1 123 GLN n 
1 124 ARG n 
1 125 GLY n 
1 126 GLU n 
1 127 LEU n 
1 128 LEU n 
1 129 HIS n 
1 130 HIS n 
1 131 THR n 
1 132 LEU n 
1 133 GLY n 
1 134 ASP n 
1 135 GLY n 
1 136 GLU n 
1 137 PHE n 
1 138 ARG n 
1 139 HIS n 
1 140 PHE n 
1 141 TYR n 
1 142 HIS n 
1 143 MET n 
1 144 SER n 
1 145 GLU n 
1 146 PRO n 
1 147 ILE n 
1 148 THR n 
1 149 VAL n 
1 150 ALA n 
1 151 GLN n 
1 152 ALA n 
1 153 ILE n 
1 154 LEU n 
1 155 THR n 
1 156 GLU n 
1 157 GLN n 
1 158 ASN n 
1 159 ALA n 
1 160 CYS n 
1 161 TYR n 
1 162 GLU n 
1 163 ILE n 
1 164 ASP n 
1 165 ARG n 
1 166 VAL n 
1 167 LEU n 
1 168 THR n 
1 169 THR n 
1 170 MET n 
1 171 LEU n 
1 172 ARG n 
1 173 GLU n 
1 174 ARG n 
1 175 ARG n 
1 176 PRO n 
1 177 GLY n 
1 178 TYR n 
1 179 LEU n 
1 180 MET n 
1 181 LEU n 
1 182 PRO n 
1 183 ALA n 
1 184 ASP n 
1 185 VAL n 
1 186 ALA n 
1 187 LYS n 
1 188 LYS n 
1 189 ALA n 
1 190 ALA n 
1 191 THR n 
1 192 PRO n 
1 193 PRO n 
1 194 VAL n 
1 195 ASN n 
1 196 ALA n 
1 197 LEU n 
1 198 THR n 
1 199 LEU n 
1 200 ARG n 
1 201 HIS n 
1 202 ALA n 
1 203 HIS n 
1 204 ALA n 
1 205 ASP n 
1 206 SER n 
1 207 ALA n 
1 208 CYS n 
1 209 LEU n 
1 210 LYS n 
1 211 ALA n 
1 212 PHE n 
1 213 ARG n 
1 214 ASP n 
1 215 ALA n 
1 216 ALA n 
1 217 GLU n 
1 218 ASN n 
1 219 ARG n 
1 220 LEU n 
1 221 ALA n 
1 222 MET n 
1 223 SER n 
1 224 LYS n 
1 225 ARG n 
1 226 THR n 
1 227 ALA n 
1 228 LEU n 
1 229 LEU n 
1 230 ALA n 
1 231 ASP n 
1 232 PHE n 
1 233 LEU n 
1 234 VAL n 
1 235 LEU n 
1 236 ARG n 
1 237 HIS n 
1 238 GLY n 
1 239 LEU n 
1 240 LYS n 
1 241 HIS n 
1 242 ALA n 
1 243 LEU n 
1 244 GLN n 
1 245 LYS n 
1 246 TRP n 
1 247 VAL n 
1 248 LYS n 
1 249 ASP n 
1 250 VAL n 
1 251 PRO n 
1 252 MET n 
1 253 ALA n 
1 254 HIS n 
1 255 ALA n 
1 256 THR n 
1 257 MET n 
1 258 LEU n 
1 259 MET n 
1 260 GLY n 
1 261 LYS n 
1 262 GLY n 
1 263 ILE n 
1 264 PHE n 
1 265 ASP n 
1 266 GLU n 
1 267 ARG n 
1 268 HIS n 
1 269 VAL n 
1 270 GLY n 
1 271 PHE n 
1 272 TYR n 
1 273 GLY n 
1 274 THR n 
1 275 TYR n 
1 276 SER n 
1 277 GLY n 
1 278 SER n 
1 279 ALA n 
1 280 SER n 
1 281 ALA n 
1 282 GLY n 
1 283 ALA n 
1 284 VAL n 
1 285 LYS n 
1 286 GLU n 
1 287 ALA n 
1 288 ILE n 
1 289 GLU n 
1 290 GLY n 
1 291 ALA n 
1 292 ASP n 
1 293 THR n 
1 294 VAL n 
1 295 LEU n 
1 296 CYS n 
1 297 ILE n 
1 298 GLY n 
1 299 THR n 
1 300 ARG n 
1 301 PHE n 
1 302 THR n 
1 303 ASP n 
1 304 THR n 
1 305 LEU n 
1 306 THR n 
1 307 ALA n 
1 308 GLY n 
1 309 PHE n 
1 310 THR n 
1 311 HIS n 
1 312 GLN n 
1 313 LEU n 
1 314 THR n 
1 315 PRO n 
1 316 SER n 
1 317 GLN n 
1 318 THR n 
1 319 ILE n 
1 320 GLU n 
1 321 VAL n 
1 322 GLN n 
1 323 PRO n 
1 324 HIS n 
1 325 ALA n 
1 326 SER n 
1 327 ARG n 
1 328 VAL n 
1 329 GLY n 
1 330 ASP n 
1 331 VAL n 
1 332 TRP n 
1 333 PHE n 
1 334 THR n 
1 335 GLY n 
1 336 ILE n 
1 337 PRO n 
1 338 MET n 
1 339 LEU n 
1 340 GLN n 
1 341 ALA n 
1 342 ILE n 
1 343 GLU n 
1 344 THR n 
1 345 LEU n 
1 346 VAL n 
1 347 GLU n 
1 348 LEU n 
1 349 CYS n 
1 350 LYS n 
1 351 GLN n 
1 352 HIS n 
1 353 VAL n 
1 354 HIS n 
1 355 ASP n 
1 356 THR n 
1 357 PRO n 
1 358 VAL n 
1 359 PRO n 
1 360 SER n 
1 361 SER n 
1 362 GLN n 
1 363 SER n 
1 364 ALA n 
1 365 MET n 
1 366 VAL n 
1 367 TYR n 
1 368 PRO n 
1 369 GLN n 
1 370 PRO n 
1 371 ASP n 
1 372 GLY n 
1 373 SER n 
1 374 LEU n 
1 375 THR n 
1 376 GLN n 
1 377 ASP n 
1 378 ASN n 
1 379 PHE n 
1 380 TRP n 
1 381 LYS n 
1 382 THR n 
1 383 LEU n 
1 384 GLN n 
1 385 THR n 
1 386 PHE n 
1 387 ILE n 
1 388 ARG n 
1 389 PRO n 
1 390 GLY n 
1 391 ASP n 
1 392 ILE n 
1 393 ILE n 
1 394 LEU n 
1 395 ALA n 
1 396 ASP n 
1 397 GLN n 
1 398 GLY n 
1 399 THR n 
1 400 SER n 
1 401 ALA n 
1 402 PHE n 
1 403 GLY n 
1 404 ALA n 
1 405 ILE n 
1 406 ASP n 
1 407 LEU n 
1 408 ARG n 
1 409 LEU n 
1 410 PRO n 
1 411 ALA n 
1 412 ASP n 
1 413 VAL n 
1 414 ASN n 
1 415 PHE n 
1 416 ILE n 
1 417 VAL n 
1 418 GLN n 
1 419 PRO n 
1 420 LEU n 
1 421 TRP n 
1 422 GLY n 
1 423 SER n 
1 424 ILE n 
1 425 GLY n 
1 426 TYR n 
1 427 THR n 
1 428 LEU n 
1 429 ALA n 
1 430 ALA n 
1 431 ALA n 
1 432 PHE n 
1 433 GLY n 
1 434 ALA n 
1 435 GLN n 
1 436 THR n 
1 437 ALA n 
1 438 CYS n 
1 439 PRO n 
1 440 ASN n 
1 441 ARG n 
1 442 ARG n 
1 443 VAL n 
1 444 ILE n 
1 445 VAL n 
1 446 LEU n 
1 447 THR n 
1 448 GLY n 
1 449 ASP n 
1 450 GLY n 
1 451 ALA n 
1 452 ALA n 
1 453 GLN n 
1 454 LEU n 
1 455 THR n 
1 456 ILE n 
1 457 GLN n 
1 458 GLU n 
1 459 LEU n 
1 460 GLY n 
1 461 SER n 
1 462 MET n 
1 463 LEU n 
1 464 ARG n 
1 465 ASP n 
1 466 LYS n 
1 467 GLN n 
1 468 HIS n 
1 469 PRO n 
1 470 ILE n 
1 471 ILE n 
1 472 LEU n 
1 473 VAL n 
1 474 LEU n 
1 475 ASN n 
1 476 ASN n 
1 477 GLU n 
1 478 GLY n 
1 479 TYR n 
1 480 THR n 
1 481 VAL n 
1 482 LEU n 
1 483 ARG n 
1 484 ALA n 
1 485 ILE n 
1 486 HIS n 
1 487 GLY n 
1 488 PRO n 
1 489 GLU n 
1 490 GLN n 
1 491 ARG n 
1 492 TYR n 
1 493 ASN n 
1 494 ASP n 
1 495 ILE n 
1 496 ALA n 
1 497 LEU n 
1 498 TRP n 
1 499 ASN n 
1 500 TRP n 
1 501 THR n 
1 502 GLN n 
1 503 ILE n 
1 504 PRO n 
1 505 GLN n 
1 506 ALA n 
1 507 LEU n 
1 508 SER n 
1 509 LEU n 
1 510 ASP n 
1 511 PRO n 
1 512 GLN n 
1 513 ALA n 
1 514 GLN n 
1 515 CYS n 
1 516 TRP n 
1 517 ARG n 
1 518 VAL n 
1 519 SER n 
1 520 GLU n 
1 521 ALA n 
1 522 GLU n 
1 523 GLN n 
1 524 LEU n 
1 525 ALA n 
1 526 ASP n 
1 527 VAL n 
1 528 LEU n 
1 529 GLU n 
1 530 LYS n 
1 531 VAL n 
1 532 ALA n 
1 533 HIS n 
1 534 HIS n 
1 535 GLU n 
1 536 ARG n 
1 537 LEU n 
1 538 SER n 
1 539 LEU n 
1 540 ILE n 
1 541 GLU n 
1 542 VAL n 
1 543 MET n 
1 544 LEU n 
1 545 PRO n 
1 546 LYS n 
1 547 ALA n 
1 548 ASP n 
1 549 ILE n 
1 550 PRO n 
1 551 PRO n 
1 552 LEU n 
1 553 LEU n 
1 554 GLY n 
1 555 ALA n 
1 556 ILE n 
1 557 THR n 
1 558 LYS n 
1 559 ALA n 
1 560 LEU n 
1 561 GLU n 
1 562 ALA n 
1 563 ARG n 
1 564 ASN n 
1 565 SER n 
1 566 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   566 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ipdC, DEO48_12930' 
_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      'Enterobacter sp. CGMCC 5087' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2183878 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
3IO non-polymer         . '3-(1H-INDOL-3-YL)-2-OXOPROPANOIC ACID' ? 'C11 H9 N O3'          203.194 
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 
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 
MG  non-polymer         . 'MAGNESIUM ION'                         ? 'Mg 2'                 24.305  
PHE 'L-peptide linking' y PHENYLALANINE                           ? 'C9 H11 N O2'          165.189 
PRO 'L-peptide linking' y PROLINE                                 ? 'C5 H9 N O2'           115.130 
SER 'L-peptide linking' y SERINE                                  ? 'C3 H7 N O3'           105.093 
THR 'L-peptide linking' y THREONINE                               ? 'C4 H9 N O3'           119.119 
TPP non-polymer         . 'THIAMINE DIPHOSPHATE'                  ? 'C12 H19 N4 O7 P2 S 1' 425.314 
TRP 'L-peptide linking' y TRYPTOPHAN                              ? 'C11 H12 N2 O2'        204.225 
TYR 'L-peptide linking' y TYROSINE                                ? 'C9 H11 N O3'          181.189 
VAL 'L-peptide linking' y VALINE                                  ? 'C5 H11 N O2'          117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -13 ?   ?   ?   A . n 
A 1 2   GLY 2   -12 ?   ?   ?   A . n 
A 1 3   SER 3   -11 ?   ?   ?   A . n 
A 1 4   SER 4   -10 ?   ?   ?   A . n 
A 1 5   HIS 5   -9  ?   ?   ?   A . n 
A 1 6   HIS 6   -8  ?   ?   ?   A . n 
A 1 7   HIS 7   -7  ?   ?   ?   A . n 
A 1 8   HIS 8   -6  ?   ?   ?   A . n 
A 1 9   HIS 9   -5  ?   ?   ?   A . n 
A 1 10  HIS 10  -4  ?   ?   ?   A . n 
A 1 11  SER 11  -3  ?   ?   ?   A . n 
A 1 12  GLN 12  -2  ?   ?   ?   A . n 
A 1 13  ASP 13  -1  ?   ?   ?   A . n 
A 1 14  PRO 14  0   ?   ?   ?   A . n 
A 1 15  MET 15  1   ?   ?   ?   A . n 
A 1 16  ARG 16  2   ?   ?   ?   A . n 
A 1 17  THR 17  3   3   THR THR A . n 
A 1 18  PRO 18  4   4   PRO PRO A . n 
A 1 19  TYR 19  5   5   TYR TYR A . n 
A 1 20  CYS 20  6   6   CYS CYS A . n 
A 1 21  VAL 21  7   7   VAL VAL A . n 
A 1 22  ALA 22  8   8   ALA ALA A . n 
A 1 23  ASP 23  9   9   ASP ASP A . n 
A 1 24  TYR 24  10  10  TYR TYR A . n 
A 1 25  LEU 25  11  11  LEU LEU A . n 
A 1 26  LEU 26  12  12  LEU LEU A . n 
A 1 27  ASP 27  13  13  ASP ASP A . n 
A 1 28  ARG 28  14  14  ARG ARG A . n 
A 1 29  LEU 29  15  15  LEU LEU A . n 
A 1 30  THR 30  16  16  THR THR A . n 
A 1 31  ASP 31  17  17  ASP ASP A . n 
A 1 32  CYS 32  18  18  CYS CYS A . n 
A 1 33  GLY 33  19  19  GLY GLY A . n 
A 1 34  ALA 34  20  20  ALA ALA A . n 
A 1 35  ASP 35  21  21  ASP ASP A . n 
A 1 36  HIS 36  22  22  HIS HIS A . n 
A 1 37  LEU 37  23  23  LEU LEU A . n 
A 1 38  PHE 38  24  24  PHE PHE A . n 
A 1 39  GLY 39  25  25  GLY GLY A . n 
A 1 40  VAL 40  26  26  VAL VAL A . n 
A 1 41  PRO 41  27  27  PRO PRO A . n 
A 1 42  GLY 42  28  28  GLY GLY A . n 
A 1 43  ASP 43  29  29  ASP ASP A . n 
A 1 44  TYR 44  30  30  TYR TYR A . n 
A 1 45  ASN 45  31  31  ASN ASN A . n 
A 1 46  LEU 46  32  32  LEU LEU A . n 
A 1 47  GLN 47  33  33  GLN GLN A . n 
A 1 48  PHE 48  34  34  PHE PHE A . n 
A 1 49  LEU 49  35  35  LEU LEU A . n 
A 1 50  ASP 50  36  36  ASP ASP A . n 
A 1 51  HIS 51  37  37  HIS HIS A . n 
A 1 52  VAL 52  38  38  VAL VAL A . n 
A 1 53  ILE 53  39  39  ILE ILE A . n 
A 1 54  ASP 54  40  40  ASP ASP A . n 
A 1 55  SER 55  41  41  SER SER A . n 
A 1 56  PRO 56  42  42  PRO PRO A . n 
A 1 57  ASP 57  43  43  ASP ASP A . n 
A 1 58  ILE 58  44  44  ILE ILE A . n 
A 1 59  CYS 59  45  45  CYS CYS A . n 
A 1 60  TRP 60  46  46  TRP TRP A . n 
A 1 61  VAL 61  47  47  VAL VAL A . n 
A 1 62  GLY 62  48  48  GLY GLY A . n 
A 1 63  CYS 63  49  49  CYS CYS A . n 
A 1 64  ALA 64  50  50  ALA ALA A . n 
A 1 65  ASN 65  51  51  ASN ASN A . n 
A 1 66  GLU 66  52  52  GLU GLU A . n 
A 1 67  LEU 67  53  53  LEU LEU A . n 
A 1 68  ASN 68  54  54  ASN ASN A . n 
A 1 69  ALA 69  55  55  ALA ALA A . n 
A 1 70  SER 70  56  56  SER SER A . n 
A 1 71  TYR 71  57  57  TYR TYR A . n 
A 1 72  ALA 72  58  58  ALA ALA A . n 
A 1 73  ALA 73  59  59  ALA ALA A . n 
A 1 74  ASP 74  60  60  ASP ASP A . n 
A 1 75  GLY 75  61  61  GLY GLY A . n 
A 1 76  TYR 76  62  62  TYR TYR A . n 
A 1 77  ALA 77  63  63  ALA ALA A . n 
A 1 78  ARG 78  64  64  ARG ARG A . n 
A 1 79  CYS 79  65  65  CYS CYS A . n 
A 1 80  LYS 80  66  66  LYS LYS A . n 
A 1 81  GLY 81  67  67  GLY GLY A . n 
A 1 82  PHE 82  68  68  PHE PHE A . n 
A 1 83  ALA 83  69  69  ALA ALA A . n 
A 1 84  ALA 84  70  70  ALA ALA A . n 
A 1 85  LEU 85  71  71  LEU LEU A . n 
A 1 86  LEU 86  72  72  LEU LEU A . n 
A 1 87  THR 87  73  73  THR THR A . n 
A 1 88  THR 88  74  74  THR THR A . n 
A 1 89  PHE 89  75  75  PHE PHE A . n 
A 1 90  GLY 90  76  76  GLY GLY A . n 
A 1 91  VAL 91  77  77  VAL VAL A . n 
A 1 92  GLY 92  78  78  GLY GLY A . n 
A 1 93  GLU 93  79  79  GLU GLU A . n 
A 1 94  LEU 94  80  80  LEU LEU A . n 
A 1 95  SER 95  81  81  SER SER A . n 
A 1 96  ALA 96  82  82  ALA ALA A . n 
A 1 97  MET 97  83  83  MET MET A . n 
A 1 98  ASN 98  84  84  ASN ASN A . n 
A 1 99  GLY 99  85  85  GLY GLY A . n 
A 1 100 ILE 100 86  86  ILE ILE A . n 
A 1 101 ALA 101 87  87  ALA ALA A . n 
A 1 102 GLY 102 88  88  GLY GLY A . n 
A 1 103 SER 103 89  89  SER SER A . n 
A 1 104 TYR 104 90  90  TYR TYR A . n 
A 1 105 ALA 105 91  91  ALA ALA A . n 
A 1 106 GLU 106 92  92  GLU GLU A . n 
A 1 107 HIS 107 93  93  HIS HIS A . n 
A 1 108 VAL 108 94  94  VAL VAL A . n 
A 1 109 PRO 109 95  95  PRO PRO A . n 
A 1 110 VAL 110 96  96  VAL VAL A . n 
A 1 111 LEU 111 97  97  LEU LEU A . n 
A 1 112 HIS 112 98  98  HIS HIS A . n 
A 1 113 ILE 113 99  99  ILE ILE A . n 
A 1 114 VAL 114 100 100 VAL VAL A . n 
A 1 115 GLY 115 101 101 GLY GLY A . n 
A 1 116 ALA 116 102 102 ALA ALA A . n 
A 1 117 PRO 117 103 103 PRO PRO A . n 
A 1 118 GLY 118 104 104 GLY GLY A . n 
A 1 119 THR 119 105 105 THR THR A . n 
A 1 120 ALA 120 106 106 ALA ALA A . n 
A 1 121 SER 121 107 107 SER SER A . n 
A 1 122 GLN 122 108 108 GLN GLN A . n 
A 1 123 GLN 123 109 109 GLN GLN A . n 
A 1 124 ARG 124 110 110 ARG ARG A . n 
A 1 125 GLY 125 111 111 GLY GLY A . n 
A 1 126 GLU 126 112 112 GLU GLU A . n 
A 1 127 LEU 127 113 113 LEU LEU A . n 
A 1 128 LEU 128 114 114 LEU LEU A . n 
A 1 129 HIS 129 115 115 HIS HIS A . n 
A 1 130 HIS 130 116 116 HIS HIS A . n 
A 1 131 THR 131 117 117 THR THR A . n 
A 1 132 LEU 132 118 118 LEU LEU A . n 
A 1 133 GLY 133 119 119 GLY GLY A . n 
A 1 134 ASP 134 120 120 ASP ASP A . n 
A 1 135 GLY 135 121 121 GLY GLY A . n 
A 1 136 GLU 136 122 122 GLU GLU A . n 
A 1 137 PHE 137 123 123 PHE PHE A . n 
A 1 138 ARG 138 124 124 ARG ARG A . n 
A 1 139 HIS 139 125 125 HIS HIS A . n 
A 1 140 PHE 140 126 126 PHE PHE A . n 
A 1 141 TYR 141 127 127 TYR TYR A . n 
A 1 142 HIS 142 128 128 HIS HIS A . n 
A 1 143 MET 143 129 129 MET MET A . n 
A 1 144 SER 144 130 130 SER SER A . n 
A 1 145 GLU 145 131 131 GLU GLU A . n 
A 1 146 PRO 146 132 132 PRO PRO A . n 
A 1 147 ILE 147 133 133 ILE ILE A . n 
A 1 148 THR 148 134 134 THR THR A . n 
A 1 149 VAL 149 135 135 VAL VAL A . n 
A 1 150 ALA 150 136 136 ALA ALA A . n 
A 1 151 GLN 151 137 137 GLN GLN A . n 
A 1 152 ALA 152 138 138 ALA ALA A . n 
A 1 153 ILE 153 139 139 ILE ILE A . n 
A 1 154 LEU 154 140 140 LEU LEU A . n 
A 1 155 THR 155 141 141 THR THR A . n 
A 1 156 GLU 156 142 142 GLU GLU A . n 
A 1 157 GLN 157 143 143 GLN GLN A . n 
A 1 158 ASN 158 144 144 ASN ASN A . n 
A 1 159 ALA 159 145 145 ALA ALA A . n 
A 1 160 CYS 160 146 146 CYS CYS A . n 
A 1 161 TYR 161 147 147 TYR TYR A . n 
A 1 162 GLU 162 148 148 GLU GLU A . n 
A 1 163 ILE 163 149 149 ILE ILE A . n 
A 1 164 ASP 164 150 150 ASP ASP A . n 
A 1 165 ARG 165 151 151 ARG ARG A . n 
A 1 166 VAL 166 152 152 VAL VAL A . n 
A 1 167 LEU 167 153 153 LEU LEU A . n 
A 1 168 THR 168 154 154 THR THR A . n 
A 1 169 THR 169 155 155 THR THR A . n 
A 1 170 MET 170 156 156 MET MET A . n 
A 1 171 LEU 171 157 157 LEU LEU A . n 
A 1 172 ARG 172 158 158 ARG ARG A . n 
A 1 173 GLU 173 159 159 GLU GLU A . n 
A 1 174 ARG 174 160 160 ARG ARG A . n 
A 1 175 ARG 175 161 161 ARG ARG A . n 
A 1 176 PRO 176 162 162 PRO PRO A . n 
A 1 177 GLY 177 163 163 GLY GLY A . n 
A 1 178 TYR 178 164 164 TYR TYR A . n 
A 1 179 LEU 179 165 165 LEU LEU A . n 
A 1 180 MET 180 166 166 MET MET A . n 
A 1 181 LEU 181 167 167 LEU LEU A . n 
A 1 182 PRO 182 168 168 PRO PRO A . n 
A 1 183 ALA 183 169 169 ALA ALA A . n 
A 1 184 ASP 184 170 170 ASP ASP A . n 
A 1 185 VAL 185 171 171 VAL VAL A . n 
A 1 186 ALA 186 172 172 ALA ALA A . n 
A 1 187 LYS 187 173 173 LYS LYS A . n 
A 1 188 LYS 188 174 174 LYS LYS A . n 
A 1 189 ALA 189 175 175 ALA ALA A . n 
A 1 190 ALA 190 176 176 ALA ALA A . n 
A 1 191 THR 191 177 177 THR THR A . n 
A 1 192 PRO 192 178 178 PRO PRO A . n 
A 1 193 PRO 193 179 179 PRO PRO A . n 
A 1 194 VAL 194 180 180 VAL VAL A . n 
A 1 195 ASN 195 181 181 ASN ASN A . n 
A 1 196 ALA 196 182 182 ALA ALA A . n 
A 1 197 LEU 197 183 183 LEU LEU A . n 
A 1 198 THR 198 184 184 THR THR A . n 
A 1 199 LEU 199 185 185 LEU LEU A . n 
A 1 200 ARG 200 186 186 ARG ARG A . n 
A 1 201 HIS 201 187 187 HIS HIS A . n 
A 1 202 ALA 202 188 188 ALA ALA A . n 
A 1 203 HIS 203 189 189 HIS HIS A . n 
A 1 204 ALA 204 190 190 ALA ALA A . n 
A 1 205 ASP 205 191 191 ASP ASP A . n 
A 1 206 SER 206 192 192 SER SER A . n 
A 1 207 ALA 207 193 193 ALA ALA A . n 
A 1 208 CYS 208 194 194 CYS CYS A . n 
A 1 209 LEU 209 195 195 LEU LEU A . n 
A 1 210 LYS 210 196 196 LYS LYS A . n 
A 1 211 ALA 211 197 197 ALA ALA A . n 
A 1 212 PHE 212 198 198 PHE PHE A . n 
A 1 213 ARG 213 199 199 ARG ARG A . n 
A 1 214 ASP 214 200 200 ASP ASP A . n 
A 1 215 ALA 215 201 201 ALA ALA A . n 
A 1 216 ALA 216 202 202 ALA ALA A . n 
A 1 217 GLU 217 203 203 GLU GLU A . n 
A 1 218 ASN 218 204 204 ASN ASN A . n 
A 1 219 ARG 219 205 205 ARG ARG A . n 
A 1 220 LEU 220 206 206 LEU LEU A . n 
A 1 221 ALA 221 207 207 ALA ALA A . n 
A 1 222 MET 222 208 208 MET MET A . n 
A 1 223 SER 223 209 209 SER SER A . n 
A 1 224 LYS 224 210 210 LYS LYS A . n 
A 1 225 ARG 225 211 211 ARG ARG A . n 
A 1 226 THR 226 212 212 THR THR A . n 
A 1 227 ALA 227 213 213 ALA ALA A . n 
A 1 228 LEU 228 214 214 LEU LEU A . n 
A 1 229 LEU 229 215 215 LEU LEU A . n 
A 1 230 ALA 230 216 216 ALA ALA A . n 
A 1 231 ASP 231 217 217 ASP ASP A . n 
A 1 232 PHE 232 218 218 PHE PHE A . n 
A 1 233 LEU 233 219 219 LEU LEU A . n 
A 1 234 VAL 234 220 220 VAL VAL A . n 
A 1 235 LEU 235 221 221 LEU LEU A . n 
A 1 236 ARG 236 222 222 ARG ARG A . n 
A 1 237 HIS 237 223 223 HIS HIS A . n 
A 1 238 GLY 238 224 224 GLY GLY A . n 
A 1 239 LEU 239 225 225 LEU LEU A . n 
A 1 240 LYS 240 226 226 LYS LYS A . n 
A 1 241 HIS 241 227 227 HIS HIS A . n 
A 1 242 ALA 242 228 228 ALA ALA A . n 
A 1 243 LEU 243 229 229 LEU LEU A . n 
A 1 244 GLN 244 230 230 GLN GLN A . n 
A 1 245 LYS 245 231 231 LYS LYS A . n 
A 1 246 TRP 246 232 232 TRP TRP A . n 
A 1 247 VAL 247 233 233 VAL VAL A . n 
A 1 248 LYS 248 234 234 LYS LYS A . n 
A 1 249 ASP 249 235 235 ASP ASP A . n 
A 1 250 VAL 250 236 236 VAL VAL A . n 
A 1 251 PRO 251 237 237 PRO PRO A . n 
A 1 252 MET 252 238 238 MET MET A . n 
A 1 253 ALA 253 239 239 ALA ALA A . n 
A 1 254 HIS 254 240 240 HIS HIS A . n 
A 1 255 ALA 255 241 241 ALA ALA A . n 
A 1 256 THR 256 242 242 THR THR A . n 
A 1 257 MET 257 243 243 MET MET A . n 
A 1 258 LEU 258 244 244 LEU LEU A . n 
A 1 259 MET 259 245 245 MET MET A . n 
A 1 260 GLY 260 246 246 GLY GLY A . n 
A 1 261 LYS 261 247 247 LYS LYS A . n 
A 1 262 GLY 262 248 248 GLY GLY A . n 
A 1 263 ILE 263 249 249 ILE ILE A . n 
A 1 264 PHE 264 250 250 PHE PHE A . n 
A 1 265 ASP 265 251 251 ASP ASP A . n 
A 1 266 GLU 266 252 252 GLU GLU A . n 
A 1 267 ARG 267 253 253 ARG ARG A . n 
A 1 268 HIS 268 254 254 HIS HIS A . n 
A 1 269 VAL 269 255 255 VAL VAL A . n 
A 1 270 GLY 270 256 256 GLY GLY A . n 
A 1 271 PHE 271 257 257 PHE PHE A . n 
A 1 272 TYR 272 258 258 TYR TYR A . n 
A 1 273 GLY 273 259 259 GLY GLY A . n 
A 1 274 THR 274 260 260 THR THR A . n 
A 1 275 TYR 275 261 261 TYR TYR A . n 
A 1 276 SER 276 262 262 SER SER A . n 
A 1 277 GLY 277 263 263 GLY GLY A . n 
A 1 278 SER 278 264 264 SER SER A . n 
A 1 279 ALA 279 265 265 ALA ALA A . n 
A 1 280 SER 280 266 266 SER SER A . n 
A 1 281 ALA 281 267 267 ALA ALA A . n 
A 1 282 GLY 282 268 268 GLY GLY A . n 
A 1 283 ALA 283 269 269 ALA ALA A . n 
A 1 284 VAL 284 270 270 VAL VAL A . n 
A 1 285 LYS 285 271 271 LYS LYS A . n 
A 1 286 GLU 286 272 272 GLU GLU A . n 
A 1 287 ALA 287 273 273 ALA ALA A . n 
A 1 288 ILE 288 274 274 ILE ILE A . n 
A 1 289 GLU 289 275 275 GLU GLU A . n 
A 1 290 GLY 290 276 276 GLY GLY A . n 
A 1 291 ALA 291 277 277 ALA ALA A . n 
A 1 292 ASP 292 278 278 ASP ASP A . n 
A 1 293 THR 293 279 279 THR THR A . n 
A 1 294 VAL 294 280 280 VAL VAL A . n 
A 1 295 LEU 295 281 281 LEU LEU A . n 
A 1 296 CYS 296 282 282 CYS CYS A . n 
A 1 297 ILE 297 283 283 ILE ILE A . n 
A 1 298 GLY 298 284 284 GLY GLY A . n 
A 1 299 THR 299 285 285 THR THR A . n 
A 1 300 ARG 300 286 286 ARG ARG A . n 
A 1 301 PHE 301 287 287 PHE PHE A . n 
A 1 302 THR 302 288 288 THR THR A . n 
A 1 303 ASP 303 289 289 ASP ASP A . n 
A 1 304 THR 304 290 290 THR THR A . n 
A 1 305 LEU 305 291 291 LEU LEU A . n 
A 1 306 THR 306 292 292 THR THR A . n 
A 1 307 ALA 307 293 293 ALA ALA A . n 
A 1 308 GLY 308 294 294 GLY GLY A . n 
A 1 309 PHE 309 295 295 PHE PHE A . n 
A 1 310 THR 310 296 296 THR THR A . n 
A 1 311 HIS 311 297 297 HIS HIS A . n 
A 1 312 GLN 312 298 298 GLN GLN A . n 
A 1 313 LEU 313 299 299 LEU LEU A . n 
A 1 314 THR 314 300 300 THR THR A . n 
A 1 315 PRO 315 301 301 PRO PRO A . n 
A 1 316 SER 316 302 302 SER SER A . n 
A 1 317 GLN 317 303 303 GLN GLN A . n 
A 1 318 THR 318 304 304 THR THR A . n 
A 1 319 ILE 319 305 305 ILE ILE A . n 
A 1 320 GLU 320 306 306 GLU GLU A . n 
A 1 321 VAL 321 307 307 VAL VAL A . n 
A 1 322 GLN 322 308 308 GLN GLN A . n 
A 1 323 PRO 323 309 309 PRO PRO A . n 
A 1 324 HIS 324 310 310 HIS HIS A . n 
A 1 325 ALA 325 311 311 ALA ALA A . n 
A 1 326 SER 326 312 312 SER SER A . n 
A 1 327 ARG 327 313 313 ARG ARG A . n 
A 1 328 VAL 328 314 314 VAL VAL A . n 
A 1 329 GLY 329 315 315 GLY GLY A . n 
A 1 330 ASP 330 316 316 ASP ASP A . n 
A 1 331 VAL 331 317 317 VAL VAL A . n 
A 1 332 TRP 332 318 318 TRP TRP A . n 
A 1 333 PHE 333 319 319 PHE PHE A . n 
A 1 334 THR 334 320 320 THR THR A . n 
A 1 335 GLY 335 321 321 GLY GLY A . n 
A 1 336 ILE 336 322 322 ILE ILE A . n 
A 1 337 PRO 337 323 323 PRO PRO A . n 
A 1 338 MET 338 324 324 MET MET A . n 
A 1 339 LEU 339 325 325 LEU LEU A . n 
A 1 340 GLN 340 326 326 GLN GLN A . n 
A 1 341 ALA 341 327 327 ALA ALA A . n 
A 1 342 ILE 342 328 328 ILE ILE A . n 
A 1 343 GLU 343 329 329 GLU GLU A . n 
A 1 344 THR 344 330 330 THR THR A . n 
A 1 345 LEU 345 331 331 LEU LEU A . n 
A 1 346 VAL 346 332 332 VAL VAL A . n 
A 1 347 GLU 347 333 333 GLU GLU A . n 
A 1 348 LEU 348 334 334 LEU LEU A . n 
A 1 349 CYS 349 335 335 CYS CYS A . n 
A 1 350 LYS 350 336 336 LYS LYS A . n 
A 1 351 GLN 351 337 337 GLN GLN A . n 
A 1 352 HIS 352 338 338 HIS HIS A . n 
A 1 353 VAL 353 339 339 VAL VAL A . n 
A 1 354 HIS 354 340 340 HIS HIS A . n 
A 1 355 ASP 355 341 341 ASP ASP A . n 
A 1 356 THR 356 342 342 THR THR A . n 
A 1 357 PRO 357 343 343 PRO PRO A . n 
A 1 358 VAL 358 344 344 VAL VAL A . n 
A 1 359 PRO 359 345 345 PRO PRO A . n 
A 1 360 SER 360 346 ?   ?   ?   A . n 
A 1 361 SER 361 347 ?   ?   ?   A . n 
A 1 362 GLN 362 348 ?   ?   ?   A . n 
A 1 363 SER 363 349 ?   ?   ?   A . n 
A 1 364 ALA 364 350 ?   ?   ?   A . n 
A 1 365 MET 365 351 ?   ?   ?   A . n 
A 1 366 VAL 366 352 ?   ?   ?   A . n 
A 1 367 TYR 367 353 ?   ?   ?   A . n 
A 1 368 PRO 368 354 ?   ?   ?   A . n 
A 1 369 GLN 369 355 ?   ?   ?   A . n 
A 1 370 PRO 370 356 356 PRO PRO A . n 
A 1 371 ASP 371 357 357 ASP ASP A . n 
A 1 372 GLY 372 358 358 GLY GLY A . n 
A 1 373 SER 373 359 359 SER SER A . n 
A 1 374 LEU 374 360 360 LEU LEU A . n 
A 1 375 THR 375 361 361 THR THR A . n 
A 1 376 GLN 376 362 362 GLN GLN A . n 
A 1 377 ASP 377 363 363 ASP ASP A . n 
A 1 378 ASN 378 364 364 ASN ASN A . n 
A 1 379 PHE 379 365 365 PHE PHE A . n 
A 1 380 TRP 380 366 366 TRP TRP A . n 
A 1 381 LYS 381 367 367 LYS LYS A . n 
A 1 382 THR 382 368 368 THR THR A . n 
A 1 383 LEU 383 369 369 LEU LEU A . n 
A 1 384 GLN 384 370 370 GLN GLN A . n 
A 1 385 THR 385 371 371 THR THR A . n 
A 1 386 PHE 386 372 372 PHE PHE A . n 
A 1 387 ILE 387 373 373 ILE ILE A . n 
A 1 388 ARG 388 374 374 ARG ARG A . n 
A 1 389 PRO 389 375 375 PRO PRO A . n 
A 1 390 GLY 390 376 376 GLY GLY A . n 
A 1 391 ASP 391 377 377 ASP ASP A . n 
A 1 392 ILE 392 378 378 ILE ILE A . n 
A 1 393 ILE 393 379 379 ILE ILE A . n 
A 1 394 LEU 394 380 380 LEU LEU A . n 
A 1 395 ALA 395 381 381 ALA ALA A . n 
A 1 396 ASP 396 382 382 ASP ASP A . n 
A 1 397 GLN 397 383 383 GLN GLN A . n 
A 1 398 GLY 398 384 384 GLY GLY A . n 
A 1 399 THR 399 385 385 THR THR A . n 
A 1 400 SER 400 386 386 SER SER A . n 
A 1 401 ALA 401 387 387 ALA ALA A . n 
A 1 402 PHE 402 388 388 PHE PHE A . n 
A 1 403 GLY 403 389 389 GLY GLY A . n 
A 1 404 ALA 404 390 390 ALA ALA A . n 
A 1 405 ILE 405 391 391 ILE ILE A . n 
A 1 406 ASP 406 392 392 ASP ASP A . n 
A 1 407 LEU 407 393 393 LEU LEU A . n 
A 1 408 ARG 408 394 394 ARG ARG A . n 
A 1 409 LEU 409 395 395 LEU LEU A . n 
A 1 410 PRO 410 396 396 PRO PRO A . n 
A 1 411 ALA 411 397 397 ALA ALA A . n 
A 1 412 ASP 412 398 398 ASP ASP A . n 
A 1 413 VAL 413 399 399 VAL VAL A . n 
A 1 414 ASN 414 400 400 ASN ASN A . n 
A 1 415 PHE 415 401 401 PHE PHE A . n 
A 1 416 ILE 416 402 402 ILE ILE A . n 
A 1 417 VAL 417 403 403 VAL VAL A . n 
A 1 418 GLN 418 404 404 GLN GLN A . n 
A 1 419 PRO 419 405 405 PRO PRO A . n 
A 1 420 LEU 420 406 406 LEU LEU A . n 
A 1 421 TRP 421 407 407 TRP TRP A . n 
A 1 422 GLY 422 408 408 GLY GLY A . n 
A 1 423 SER 423 409 409 SER SER A . n 
A 1 424 ILE 424 410 410 ILE ILE A . n 
A 1 425 GLY 425 411 411 GLY GLY A . n 
A 1 426 TYR 426 412 412 TYR TYR A . n 
A 1 427 THR 427 413 413 THR THR A . n 
A 1 428 LEU 428 414 414 LEU LEU A . n 
A 1 429 ALA 429 415 415 ALA ALA A . n 
A 1 430 ALA 430 416 416 ALA ALA A . n 
A 1 431 ALA 431 417 417 ALA ALA A . n 
A 1 432 PHE 432 418 418 PHE PHE A . n 
A 1 433 GLY 433 419 419 GLY GLY A . n 
A 1 434 ALA 434 420 420 ALA ALA A . n 
A 1 435 GLN 435 421 421 GLN GLN A . n 
A 1 436 THR 436 422 422 THR THR A . n 
A 1 437 ALA 437 423 423 ALA ALA A . n 
A 1 438 CYS 438 424 424 CYS CYS A . n 
A 1 439 PRO 439 425 425 PRO PRO A . n 
A 1 440 ASN 440 426 426 ASN ASN A . n 
A 1 441 ARG 441 427 427 ARG ARG A . n 
A 1 442 ARG 442 428 428 ARG ARG A . n 
A 1 443 VAL 443 429 429 VAL VAL A . n 
A 1 444 ILE 444 430 430 ILE ILE A . n 
A 1 445 VAL 445 431 431 VAL VAL A . n 
A 1 446 LEU 446 432 432 LEU LEU A . n 
A 1 447 THR 447 433 433 THR THR A . n 
A 1 448 GLY 448 434 434 GLY GLY A . n 
A 1 449 ASP 449 435 435 ASP ASP A . n 
A 1 450 GLY 450 436 436 GLY GLY A . n 
A 1 451 ALA 451 437 437 ALA ALA A . n 
A 1 452 ALA 452 438 438 ALA ALA A . n 
A 1 453 GLN 453 439 439 GLN GLN A . n 
A 1 454 LEU 454 440 440 LEU LEU A . n 
A 1 455 THR 455 441 441 THR THR A . n 
A 1 456 ILE 456 442 442 ILE ILE A . n 
A 1 457 GLN 457 443 443 GLN GLN A . n 
A 1 458 GLU 458 444 444 GLU GLU A . n 
A 1 459 LEU 459 445 445 LEU LEU A . n 
A 1 460 GLY 460 446 446 GLY GLY A . n 
A 1 461 SER 461 447 447 SER SER A . n 
A 1 462 MET 462 448 448 MET MET A . n 
A 1 463 LEU 463 449 449 LEU LEU A . n 
A 1 464 ARG 464 450 450 ARG ARG A . n 
A 1 465 ASP 465 451 451 ASP ASP A . n 
A 1 466 LYS 466 452 452 LYS LYS A . n 
A 1 467 GLN 467 453 453 GLN GLN A . n 
A 1 468 HIS 468 454 454 HIS HIS A . n 
A 1 469 PRO 469 455 455 PRO PRO A . n 
A 1 470 ILE 470 456 456 ILE ILE A . n 
A 1 471 ILE 471 457 457 ILE ILE A . n 
A 1 472 LEU 472 458 458 LEU LEU A . n 
A 1 473 VAL 473 459 459 VAL VAL A . n 
A 1 474 LEU 474 460 460 LEU LEU A . n 
A 1 475 ASN 475 461 461 ASN ASN A . n 
A 1 476 ASN 476 462 462 ASN ASN A . n 
A 1 477 GLU 477 463 463 GLU GLU A . n 
A 1 478 GLY 478 464 464 GLY GLY A . n 
A 1 479 TYR 479 465 465 TYR TYR A . n 
A 1 480 THR 480 466 466 THR THR A . n 
A 1 481 VAL 481 467 467 VAL VAL A . n 
A 1 482 LEU 482 468 468 LEU LEU A . n 
A 1 483 ARG 483 469 469 ARG ARG A . n 
A 1 484 ALA 484 470 470 ALA ALA A . n 
A 1 485 ILE 485 471 471 ILE ILE A . n 
A 1 486 HIS 486 472 472 HIS HIS A . n 
A 1 487 GLY 487 473 473 GLY GLY A . n 
A 1 488 PRO 488 474 474 PRO PRO A . n 
A 1 489 GLU 489 475 475 GLU GLU A . n 
A 1 490 GLN 490 476 476 GLN GLN A . n 
A 1 491 ARG 491 477 477 ARG ARG A . n 
A 1 492 TYR 492 478 478 TYR TYR A . n 
A 1 493 ASN 493 479 479 ASN ASN A . n 
A 1 494 ASP 494 480 480 ASP ASP A . n 
A 1 495 ILE 495 481 481 ILE ILE A . n 
A 1 496 ALA 496 482 482 ALA ALA A . n 
A 1 497 LEU 497 483 483 LEU LEU A . n 
A 1 498 TRP 498 484 484 TRP TRP A . n 
A 1 499 ASN 499 485 485 ASN ASN A . n 
A 1 500 TRP 500 486 486 TRP TRP A . n 
A 1 501 THR 501 487 487 THR THR A . n 
A 1 502 GLN 502 488 488 GLN GLN A . n 
A 1 503 ILE 503 489 489 ILE ILE A . n 
A 1 504 PRO 504 490 490 PRO PRO A . n 
A 1 505 GLN 505 491 491 GLN GLN A . n 
A 1 506 ALA 506 492 492 ALA ALA A . n 
A 1 507 LEU 507 493 493 LEU LEU A . n 
A 1 508 SER 508 494 494 SER SER A . n 
A 1 509 LEU 509 495 495 LEU LEU A . n 
A 1 510 ASP 510 496 496 ASP ASP A . n 
A 1 511 PRO 511 497 497 PRO PRO A . n 
A 1 512 GLN 512 498 498 GLN GLN A . n 
A 1 513 ALA 513 499 499 ALA ALA A . n 
A 1 514 GLN 514 500 500 GLN GLN A . n 
A 1 515 CYS 515 501 501 CYS CYS A . n 
A 1 516 TRP 516 502 502 TRP TRP A . n 
A 1 517 ARG 517 503 503 ARG ARG A . n 
A 1 518 VAL 518 504 504 VAL VAL A . n 
A 1 519 SER 519 505 505 SER SER A . n 
A 1 520 GLU 520 506 506 GLU GLU A . n 
A 1 521 ALA 521 507 507 ALA ALA A . n 
A 1 522 GLU 522 508 508 GLU GLU A . n 
A 1 523 GLN 523 509 509 GLN GLN A . n 
A 1 524 LEU 524 510 510 LEU LEU A . n 
A 1 525 ALA 525 511 511 ALA ALA A . n 
A 1 526 ASP 526 512 512 ASP ASP A . n 
A 1 527 VAL 527 513 513 VAL VAL A . n 
A 1 528 LEU 528 514 514 LEU LEU A . n 
A 1 529 GLU 529 515 515 GLU GLU A . n 
A 1 530 LYS 530 516 516 LYS LYS A . n 
A 1 531 VAL 531 517 517 VAL VAL A . n 
A 1 532 ALA 532 518 518 ALA ALA A . n 
A 1 533 HIS 533 519 519 HIS HIS A . n 
A 1 534 HIS 534 520 520 HIS HIS A . n 
A 1 535 GLU 535 521 521 GLU GLU A . n 
A 1 536 ARG 536 522 522 ARG ARG A . n 
A 1 537 LEU 537 523 523 LEU LEU A . n 
A 1 538 SER 538 524 524 SER SER A . n 
A 1 539 LEU 539 525 525 LEU LEU A . n 
A 1 540 ILE 540 526 526 ILE ILE A . n 
A 1 541 GLU 541 527 527 GLU GLU A . n 
A 1 542 VAL 542 528 528 VAL VAL A . n 
A 1 543 MET 543 529 529 MET MET A . n 
A 1 544 LEU 544 530 530 LEU LEU A . n 
A 1 545 PRO 545 531 531 PRO PRO A . n 
A 1 546 LYS 546 532 532 LYS LYS A . n 
A 1 547 ALA 547 533 533 ALA ALA A . n 
A 1 548 ASP 548 534 534 ASP ASP A . n 
A 1 549 ILE 549 535 535 ILE ILE A . n 
A 1 550 PRO 550 536 536 PRO PRO A . n 
A 1 551 PRO 551 537 537 PRO PRO A . n 
A 1 552 LEU 552 538 538 LEU LEU A . n 
A 1 553 LEU 553 539 539 LEU LEU A . n 
A 1 554 GLY 554 540 540 GLY GLY A . n 
A 1 555 ALA 555 541 541 ALA ALA A . n 
A 1 556 ILE 556 542 542 ILE ILE A . n 
A 1 557 THR 557 543 543 THR THR A . n 
A 1 558 LYS 558 544 544 LYS LYS A . n 
A 1 559 ALA 559 545 545 ALA ALA A . n 
A 1 560 LEU 560 546 546 LEU LEU A . n 
A 1 561 GLU 561 547 547 GLU GLU A . n 
A 1 562 ALA 562 548 548 ALA ALA A . n 
A 1 563 ARG 563 549 ?   ?   ?   A . n 
A 1 564 ASN 564 550 ?   ?   ?   A . n 
A 1 565 SER 565 551 ?   ?   ?   A . n 
A 1 566 ALA 566 552 ?   ?   ?   A . n 
B 1 1   MET 1   -13 ?   ?   ?   B . n 
B 1 2   GLY 2   -12 ?   ?   ?   B . n 
B 1 3   SER 3   -11 ?   ?   ?   B . n 
B 1 4   SER 4   -10 ?   ?   ?   B . n 
B 1 5   HIS 5   -9  ?   ?   ?   B . n 
B 1 6   HIS 6   -8  ?   ?   ?   B . n 
B 1 7   HIS 7   -7  ?   ?   ?   B . n 
B 1 8   HIS 8   -6  ?   ?   ?   B . n 
B 1 9   HIS 9   -5  ?   ?   ?   B . n 
B 1 10  HIS 10  -4  ?   ?   ?   B . n 
B 1 11  SER 11  -3  ?   ?   ?   B . n 
B 1 12  GLN 12  -2  ?   ?   ?   B . n 
B 1 13  ASP 13  -1  ?   ?   ?   B . n 
B 1 14  PRO 14  0   ?   ?   ?   B . n 
B 1 15  MET 15  1   ?   ?   ?   B . n 
B 1 16  ARG 16  2   ?   ?   ?   B . n 
B 1 17  THR 17  3   3   THR THR B . n 
B 1 18  PRO 18  4   4   PRO PRO B . n 
B 1 19  TYR 19  5   5   TYR TYR B . n 
B 1 20  CYS 20  6   6   CYS CYS B . n 
B 1 21  VAL 21  7   7   VAL VAL B . n 
B 1 22  ALA 22  8   8   ALA ALA B . n 
B 1 23  ASP 23  9   9   ASP ASP B . n 
B 1 24  TYR 24  10  10  TYR TYR B . n 
B 1 25  LEU 25  11  11  LEU LEU B . n 
B 1 26  LEU 26  12  12  LEU LEU B . n 
B 1 27  ASP 27  13  13  ASP ASP B . n 
B 1 28  ARG 28  14  14  ARG ARG B . n 
B 1 29  LEU 29  15  15  LEU LEU B . n 
B 1 30  THR 30  16  16  THR THR B . n 
B 1 31  ASP 31  17  17  ASP ASP B . n 
B 1 32  CYS 32  18  18  CYS CYS B . n 
B 1 33  GLY 33  19  19  GLY GLY B . n 
B 1 34  ALA 34  20  20  ALA ALA B . n 
B 1 35  ASP 35  21  21  ASP ASP B . n 
B 1 36  HIS 36  22  22  HIS HIS B . n 
B 1 37  LEU 37  23  23  LEU LEU B . n 
B 1 38  PHE 38  24  24  PHE PHE B . n 
B 1 39  GLY 39  25  25  GLY GLY B . n 
B 1 40  VAL 40  26  26  VAL VAL B . n 
B 1 41  PRO 41  27  27  PRO PRO B . n 
B 1 42  GLY 42  28  28  GLY GLY B . n 
B 1 43  ASP 43  29  29  ASP ASP B . n 
B 1 44  TYR 44  30  30  TYR TYR B . n 
B 1 45  ASN 45  31  31  ASN ASN B . n 
B 1 46  LEU 46  32  32  LEU LEU B . n 
B 1 47  GLN 47  33  33  GLN GLN B . n 
B 1 48  PHE 48  34  34  PHE PHE B . n 
B 1 49  LEU 49  35  35  LEU LEU B . n 
B 1 50  ASP 50  36  36  ASP ASP B . n 
B 1 51  HIS 51  37  37  HIS HIS B . n 
B 1 52  VAL 52  38  38  VAL VAL B . n 
B 1 53  ILE 53  39  39  ILE ILE B . n 
B 1 54  ASP 54  40  40  ASP ASP B . n 
B 1 55  SER 55  41  41  SER SER B . n 
B 1 56  PRO 56  42  42  PRO PRO B . n 
B 1 57  ASP 57  43  43  ASP ASP B . n 
B 1 58  ILE 58  44  44  ILE ILE B . n 
B 1 59  CYS 59  45  45  CYS CYS B . n 
B 1 60  TRP 60  46  46  TRP TRP B . n 
B 1 61  VAL 61  47  47  VAL VAL B . n 
B 1 62  GLY 62  48  48  GLY GLY B . n 
B 1 63  CYS 63  49  49  CYS CYS B . n 
B 1 64  ALA 64  50  50  ALA ALA B . n 
B 1 65  ASN 65  51  51  ASN ASN B . n 
B 1 66  GLU 66  52  52  GLU GLU B . n 
B 1 67  LEU 67  53  53  LEU LEU B . n 
B 1 68  ASN 68  54  54  ASN ASN B . n 
B 1 69  ALA 69  55  55  ALA ALA B . n 
B 1 70  SER 70  56  56  SER SER B . n 
B 1 71  TYR 71  57  57  TYR TYR B . n 
B 1 72  ALA 72  58  58  ALA ALA B . n 
B 1 73  ALA 73  59  59  ALA ALA B . n 
B 1 74  ASP 74  60  60  ASP ASP B . n 
B 1 75  GLY 75  61  61  GLY GLY B . n 
B 1 76  TYR 76  62  62  TYR TYR B . n 
B 1 77  ALA 77  63  63  ALA ALA B . n 
B 1 78  ARG 78  64  64  ARG ARG B . n 
B 1 79  CYS 79  65  65  CYS CYS B . n 
B 1 80  LYS 80  66  66  LYS LYS B . n 
B 1 81  GLY 81  67  67  GLY GLY B . n 
B 1 82  PHE 82  68  68  PHE PHE B . n 
B 1 83  ALA 83  69  69  ALA ALA B . n 
B 1 84  ALA 84  70  70  ALA ALA B . n 
B 1 85  LEU 85  71  71  LEU LEU B . n 
B 1 86  LEU 86  72  72  LEU LEU B . n 
B 1 87  THR 87  73  73  THR THR B . n 
B 1 88  THR 88  74  74  THR THR B . n 
B 1 89  PHE 89  75  75  PHE PHE B . n 
B 1 90  GLY 90  76  76  GLY GLY B . n 
B 1 91  VAL 91  77  77  VAL VAL B . n 
B 1 92  GLY 92  78  78  GLY GLY B . n 
B 1 93  GLU 93  79  79  GLU GLU B . n 
B 1 94  LEU 94  80  80  LEU LEU B . n 
B 1 95  SER 95  81  81  SER SER B . n 
B 1 96  ALA 96  82  82  ALA ALA B . n 
B 1 97  MET 97  83  83  MET MET B . n 
B 1 98  ASN 98  84  84  ASN ASN B . n 
B 1 99  GLY 99  85  85  GLY GLY B . n 
B 1 100 ILE 100 86  86  ILE ILE B . n 
B 1 101 ALA 101 87  87  ALA ALA B . n 
B 1 102 GLY 102 88  88  GLY GLY B . n 
B 1 103 SER 103 89  89  SER SER B . n 
B 1 104 TYR 104 90  90  TYR TYR B . n 
B 1 105 ALA 105 91  91  ALA ALA B . n 
B 1 106 GLU 106 92  92  GLU GLU B . n 
B 1 107 HIS 107 93  93  HIS HIS B . n 
B 1 108 VAL 108 94  94  VAL VAL B . n 
B 1 109 PRO 109 95  95  PRO PRO B . n 
B 1 110 VAL 110 96  96  VAL VAL B . n 
B 1 111 LEU 111 97  97  LEU LEU B . n 
B 1 112 HIS 112 98  98  HIS HIS B . n 
B 1 113 ILE 113 99  99  ILE ILE B . n 
B 1 114 VAL 114 100 100 VAL VAL B . n 
B 1 115 GLY 115 101 101 GLY GLY B . n 
B 1 116 ALA 116 102 102 ALA ALA B . n 
B 1 117 PRO 117 103 103 PRO PRO B . n 
B 1 118 GLY 118 104 104 GLY GLY B . n 
B 1 119 THR 119 105 105 THR THR B . n 
B 1 120 ALA 120 106 106 ALA ALA B . n 
B 1 121 SER 121 107 107 SER SER B . n 
B 1 122 GLN 122 108 108 GLN GLN B . n 
B 1 123 GLN 123 109 109 GLN GLN B . n 
B 1 124 ARG 124 110 110 ARG ARG B . n 
B 1 125 GLY 125 111 111 GLY GLY B . n 
B 1 126 GLU 126 112 112 GLU GLU B . n 
B 1 127 LEU 127 113 113 LEU LEU B . n 
B 1 128 LEU 128 114 114 LEU LEU B . n 
B 1 129 HIS 129 115 115 HIS HIS B . n 
B 1 130 HIS 130 116 116 HIS HIS B . n 
B 1 131 THR 131 117 117 THR THR B . n 
B 1 132 LEU 132 118 118 LEU LEU B . n 
B 1 133 GLY 133 119 119 GLY GLY B . n 
B 1 134 ASP 134 120 120 ASP ASP B . n 
B 1 135 GLY 135 121 121 GLY GLY B . n 
B 1 136 GLU 136 122 122 GLU GLU B . n 
B 1 137 PHE 137 123 123 PHE PHE B . n 
B 1 138 ARG 138 124 124 ARG ARG B . n 
B 1 139 HIS 139 125 125 HIS HIS B . n 
B 1 140 PHE 140 126 126 PHE PHE B . n 
B 1 141 TYR 141 127 127 TYR TYR B . n 
B 1 142 HIS 142 128 128 HIS HIS B . n 
B 1 143 MET 143 129 129 MET MET B . n 
B 1 144 SER 144 130 130 SER SER B . n 
B 1 145 GLU 145 131 131 GLU GLU B . n 
B 1 146 PRO 146 132 132 PRO PRO B . n 
B 1 147 ILE 147 133 133 ILE ILE B . n 
B 1 148 THR 148 134 134 THR THR B . n 
B 1 149 VAL 149 135 135 VAL VAL B . n 
B 1 150 ALA 150 136 136 ALA ALA B . n 
B 1 151 GLN 151 137 137 GLN GLN B . n 
B 1 152 ALA 152 138 138 ALA ALA B . n 
B 1 153 ILE 153 139 139 ILE ILE B . n 
B 1 154 LEU 154 140 140 LEU LEU B . n 
B 1 155 THR 155 141 141 THR THR B . n 
B 1 156 GLU 156 142 142 GLU GLU B . n 
B 1 157 GLN 157 143 143 GLN GLN B . n 
B 1 158 ASN 158 144 144 ASN ASN B . n 
B 1 159 ALA 159 145 145 ALA ALA B . n 
B 1 160 CYS 160 146 146 CYS CYS B . n 
B 1 161 TYR 161 147 147 TYR TYR B . n 
B 1 162 GLU 162 148 148 GLU GLU B . n 
B 1 163 ILE 163 149 149 ILE ILE B . n 
B 1 164 ASP 164 150 150 ASP ASP B . n 
B 1 165 ARG 165 151 151 ARG ARG B . n 
B 1 166 VAL 166 152 152 VAL VAL B . n 
B 1 167 LEU 167 153 153 LEU LEU B . n 
B 1 168 THR 168 154 154 THR THR B . n 
B 1 169 THR 169 155 155 THR THR B . n 
B 1 170 MET 170 156 156 MET MET B . n 
B 1 171 LEU 171 157 157 LEU LEU B . n 
B 1 172 ARG 172 158 158 ARG ARG B . n 
B 1 173 GLU 173 159 159 GLU GLU B . n 
B 1 174 ARG 174 160 160 ARG ARG B . n 
B 1 175 ARG 175 161 161 ARG ARG B . n 
B 1 176 PRO 176 162 162 PRO PRO B . n 
B 1 177 GLY 177 163 163 GLY GLY B . n 
B 1 178 TYR 178 164 164 TYR TYR B . n 
B 1 179 LEU 179 165 165 LEU LEU B . n 
B 1 180 MET 180 166 166 MET MET B . n 
B 1 181 LEU 181 167 167 LEU LEU B . n 
B 1 182 PRO 182 168 168 PRO PRO B . n 
B 1 183 ALA 183 169 169 ALA ALA B . n 
B 1 184 ASP 184 170 170 ASP ASP B . n 
B 1 185 VAL 185 171 171 VAL VAL B . n 
B 1 186 ALA 186 172 172 ALA ALA B . n 
B 1 187 LYS 187 173 173 LYS LYS B . n 
B 1 188 LYS 188 174 174 LYS LYS B . n 
B 1 189 ALA 189 175 175 ALA ALA B . n 
B 1 190 ALA 190 176 176 ALA ALA B . n 
B 1 191 THR 191 177 177 THR THR B . n 
B 1 192 PRO 192 178 178 PRO PRO B . n 
B 1 193 PRO 193 179 179 PRO PRO B . n 
B 1 194 VAL 194 180 180 VAL VAL B . n 
B 1 195 ASN 195 181 181 ASN ASN B . n 
B 1 196 ALA 196 182 182 ALA ALA B . n 
B 1 197 LEU 197 183 183 LEU LEU B . n 
B 1 198 THR 198 184 184 THR THR B . n 
B 1 199 LEU 199 185 185 LEU LEU B . n 
B 1 200 ARG 200 186 186 ARG ARG B . n 
B 1 201 HIS 201 187 187 HIS HIS B . n 
B 1 202 ALA 202 188 188 ALA ALA B . n 
B 1 203 HIS 203 189 189 HIS HIS B . n 
B 1 204 ALA 204 190 190 ALA ALA B . n 
B 1 205 ASP 205 191 191 ASP ASP B . n 
B 1 206 SER 206 192 192 SER SER B . n 
B 1 207 ALA 207 193 193 ALA ALA B . n 
B 1 208 CYS 208 194 194 CYS CYS B . n 
B 1 209 LEU 209 195 195 LEU LEU B . n 
B 1 210 LYS 210 196 196 LYS LYS B . n 
B 1 211 ALA 211 197 197 ALA ALA B . n 
B 1 212 PHE 212 198 198 PHE PHE B . n 
B 1 213 ARG 213 199 199 ARG ARG B . n 
B 1 214 ASP 214 200 200 ASP ASP B . n 
B 1 215 ALA 215 201 201 ALA ALA B . n 
B 1 216 ALA 216 202 202 ALA ALA B . n 
B 1 217 GLU 217 203 203 GLU GLU B . n 
B 1 218 ASN 218 204 204 ASN ASN B . n 
B 1 219 ARG 219 205 205 ARG ARG B . n 
B 1 220 LEU 220 206 206 LEU LEU B . n 
B 1 221 ALA 221 207 207 ALA ALA B . n 
B 1 222 MET 222 208 208 MET MET B . n 
B 1 223 SER 223 209 209 SER SER B . n 
B 1 224 LYS 224 210 210 LYS LYS B . n 
B 1 225 ARG 225 211 211 ARG ARG B . n 
B 1 226 THR 226 212 212 THR THR B . n 
B 1 227 ALA 227 213 213 ALA ALA B . n 
B 1 228 LEU 228 214 214 LEU LEU B . n 
B 1 229 LEU 229 215 215 LEU LEU B . n 
B 1 230 ALA 230 216 216 ALA ALA B . n 
B 1 231 ASP 231 217 217 ASP ASP B . n 
B 1 232 PHE 232 218 218 PHE PHE B . n 
B 1 233 LEU 233 219 219 LEU LEU B . n 
B 1 234 VAL 234 220 220 VAL VAL B . n 
B 1 235 LEU 235 221 221 LEU LEU B . n 
B 1 236 ARG 236 222 222 ARG ARG B . n 
B 1 237 HIS 237 223 223 HIS HIS B . n 
B 1 238 GLY 238 224 224 GLY GLY B . n 
B 1 239 LEU 239 225 225 LEU LEU B . n 
B 1 240 LYS 240 226 226 LYS LYS B . n 
B 1 241 HIS 241 227 227 HIS HIS B . n 
B 1 242 ALA 242 228 228 ALA ALA B . n 
B 1 243 LEU 243 229 229 LEU LEU B . n 
B 1 244 GLN 244 230 230 GLN GLN B . n 
B 1 245 LYS 245 231 231 LYS LYS B . n 
B 1 246 TRP 246 232 232 TRP TRP B . n 
B 1 247 VAL 247 233 233 VAL VAL B . n 
B 1 248 LYS 248 234 234 LYS LYS B . n 
B 1 249 ASP 249 235 235 ASP ASP B . n 
B 1 250 VAL 250 236 236 VAL VAL B . n 
B 1 251 PRO 251 237 237 PRO PRO B . n 
B 1 252 MET 252 238 238 MET MET B . n 
B 1 253 ALA 253 239 239 ALA ALA B . n 
B 1 254 HIS 254 240 240 HIS HIS B . n 
B 1 255 ALA 255 241 241 ALA ALA B . n 
B 1 256 THR 256 242 242 THR THR B . n 
B 1 257 MET 257 243 243 MET MET B . n 
B 1 258 LEU 258 244 244 LEU LEU B . n 
B 1 259 MET 259 245 245 MET MET B . n 
B 1 260 GLY 260 246 246 GLY GLY B . n 
B 1 261 LYS 261 247 247 LYS LYS B . n 
B 1 262 GLY 262 248 248 GLY GLY B . n 
B 1 263 ILE 263 249 249 ILE ILE B . n 
B 1 264 PHE 264 250 250 PHE PHE B . n 
B 1 265 ASP 265 251 251 ASP ASP B . n 
B 1 266 GLU 266 252 252 GLU GLU B . n 
B 1 267 ARG 267 253 253 ARG ARG B . n 
B 1 268 HIS 268 254 254 HIS HIS B . n 
B 1 269 VAL 269 255 255 VAL VAL B . n 
B 1 270 GLY 270 256 256 GLY GLY B . n 
B 1 271 PHE 271 257 257 PHE PHE B . n 
B 1 272 TYR 272 258 258 TYR TYR B . n 
B 1 273 GLY 273 259 259 GLY GLY B . n 
B 1 274 THR 274 260 260 THR THR B . n 
B 1 275 TYR 275 261 261 TYR TYR B . n 
B 1 276 SER 276 262 262 SER SER B . n 
B 1 277 GLY 277 263 263 GLY GLY B . n 
B 1 278 SER 278 264 264 SER SER B . n 
B 1 279 ALA 279 265 265 ALA ALA B . n 
B 1 280 SER 280 266 266 SER SER B . n 
B 1 281 ALA 281 267 267 ALA ALA B . n 
B 1 282 GLY 282 268 268 GLY GLY B . n 
B 1 283 ALA 283 269 269 ALA ALA B . n 
B 1 284 VAL 284 270 270 VAL VAL B . n 
B 1 285 LYS 285 271 271 LYS LYS B . n 
B 1 286 GLU 286 272 272 GLU GLU B . n 
B 1 287 ALA 287 273 273 ALA ALA B . n 
B 1 288 ILE 288 274 274 ILE ILE B . n 
B 1 289 GLU 289 275 275 GLU GLU B . n 
B 1 290 GLY 290 276 276 GLY GLY B . n 
B 1 291 ALA 291 277 277 ALA ALA B . n 
B 1 292 ASP 292 278 278 ASP ASP B . n 
B 1 293 THR 293 279 279 THR THR B . n 
B 1 294 VAL 294 280 280 VAL VAL B . n 
B 1 295 LEU 295 281 281 LEU LEU B . n 
B 1 296 CYS 296 282 282 CYS CYS B . n 
B 1 297 ILE 297 283 283 ILE ILE B . n 
B 1 298 GLY 298 284 284 GLY GLY B . n 
B 1 299 THR 299 285 285 THR THR B . n 
B 1 300 ARG 300 286 286 ARG ARG B . n 
B 1 301 PHE 301 287 287 PHE PHE B . n 
B 1 302 THR 302 288 288 THR THR B . n 
B 1 303 ASP 303 289 289 ASP ASP B . n 
B 1 304 THR 304 290 290 THR THR B . n 
B 1 305 LEU 305 291 291 LEU LEU B . n 
B 1 306 THR 306 292 292 THR THR B . n 
B 1 307 ALA 307 293 293 ALA ALA B . n 
B 1 308 GLY 308 294 294 GLY GLY B . n 
B 1 309 PHE 309 295 295 PHE PHE B . n 
B 1 310 THR 310 296 296 THR THR B . n 
B 1 311 HIS 311 297 297 HIS HIS B . n 
B 1 312 GLN 312 298 298 GLN GLN B . n 
B 1 313 LEU 313 299 299 LEU LEU B . n 
B 1 314 THR 314 300 300 THR THR B . n 
B 1 315 PRO 315 301 301 PRO PRO B . n 
B 1 316 SER 316 302 302 SER SER B . n 
B 1 317 GLN 317 303 303 GLN GLN B . n 
B 1 318 THR 318 304 304 THR THR B . n 
B 1 319 ILE 319 305 305 ILE ILE B . n 
B 1 320 GLU 320 306 306 GLU GLU B . n 
B 1 321 VAL 321 307 307 VAL VAL B . n 
B 1 322 GLN 322 308 308 GLN GLN B . n 
B 1 323 PRO 323 309 309 PRO PRO B . n 
B 1 324 HIS 324 310 310 HIS HIS B . n 
B 1 325 ALA 325 311 311 ALA ALA B . n 
B 1 326 SER 326 312 312 SER SER B . n 
B 1 327 ARG 327 313 313 ARG ARG B . n 
B 1 328 VAL 328 314 314 VAL VAL B . n 
B 1 329 GLY 329 315 315 GLY GLY B . n 
B 1 330 ASP 330 316 316 ASP ASP B . n 
B 1 331 VAL 331 317 317 VAL VAL B . n 
B 1 332 TRP 332 318 318 TRP TRP B . n 
B 1 333 PHE 333 319 319 PHE PHE B . n 
B 1 334 THR 334 320 320 THR THR B . n 
B 1 335 GLY 335 321 321 GLY GLY B . n 
B 1 336 ILE 336 322 322 ILE ILE B . n 
B 1 337 PRO 337 323 323 PRO PRO B . n 
B 1 338 MET 338 324 324 MET MET B . n 
B 1 339 LEU 339 325 325 LEU LEU B . n 
B 1 340 GLN 340 326 326 GLN GLN B . n 
B 1 341 ALA 341 327 327 ALA ALA B . n 
B 1 342 ILE 342 328 328 ILE ILE B . n 
B 1 343 GLU 343 329 329 GLU GLU B . n 
B 1 344 THR 344 330 330 THR THR B . n 
B 1 345 LEU 345 331 331 LEU LEU B . n 
B 1 346 VAL 346 332 332 VAL VAL B . n 
B 1 347 GLU 347 333 333 GLU GLU B . n 
B 1 348 LEU 348 334 334 LEU LEU B . n 
B 1 349 CYS 349 335 335 CYS CYS B . n 
B 1 350 LYS 350 336 336 LYS LYS B . n 
B 1 351 GLN 351 337 337 GLN GLN B . n 
B 1 352 HIS 352 338 338 HIS HIS B . n 
B 1 353 VAL 353 339 339 VAL VAL B . n 
B 1 354 HIS 354 340 340 HIS HIS B . n 
B 1 355 ASP 355 341 341 ASP ASP B . n 
B 1 356 THR 356 342 342 THR THR B . n 
B 1 357 PRO 357 343 343 PRO PRO B . n 
B 1 358 VAL 358 344 344 VAL VAL B . n 
B 1 359 PRO 359 345 345 PRO PRO B . n 
B 1 360 SER 360 346 ?   ?   ?   B . n 
B 1 361 SER 361 347 ?   ?   ?   B . n 
B 1 362 GLN 362 348 ?   ?   ?   B . n 
B 1 363 SER 363 349 ?   ?   ?   B . n 
B 1 364 ALA 364 350 ?   ?   ?   B . n 
B 1 365 MET 365 351 ?   ?   ?   B . n 
B 1 366 VAL 366 352 ?   ?   ?   B . n 
B 1 367 TYR 367 353 ?   ?   ?   B . n 
B 1 368 PRO 368 354 ?   ?   ?   B . n 
B 1 369 GLN 369 355 ?   ?   ?   B . n 
B 1 370 PRO 370 356 356 PRO PRO B . n 
B 1 371 ASP 371 357 357 ASP ASP B . n 
B 1 372 GLY 372 358 358 GLY GLY B . n 
B 1 373 SER 373 359 359 SER SER B . n 
B 1 374 LEU 374 360 360 LEU LEU B . n 
B 1 375 THR 375 361 361 THR THR B . n 
B 1 376 GLN 376 362 362 GLN GLN B . n 
B 1 377 ASP 377 363 363 ASP ASP B . n 
B 1 378 ASN 378 364 364 ASN ASN B . n 
B 1 379 PHE 379 365 365 PHE PHE B . n 
B 1 380 TRP 380 366 366 TRP TRP B . n 
B 1 381 LYS 381 367 367 LYS LYS B . n 
B 1 382 THR 382 368 368 THR THR B . n 
B 1 383 LEU 383 369 369 LEU LEU B . n 
B 1 384 GLN 384 370 370 GLN GLN B . n 
B 1 385 THR 385 371 371 THR THR B . n 
B 1 386 PHE 386 372 372 PHE PHE B . n 
B 1 387 ILE 387 373 373 ILE ILE B . n 
B 1 388 ARG 388 374 374 ARG ARG B . n 
B 1 389 PRO 389 375 375 PRO PRO B . n 
B 1 390 GLY 390 376 376 GLY GLY B . n 
B 1 391 ASP 391 377 377 ASP ASP B . n 
B 1 392 ILE 392 378 378 ILE ILE B . n 
B 1 393 ILE 393 379 379 ILE ILE B . n 
B 1 394 LEU 394 380 380 LEU LEU B . n 
B 1 395 ALA 395 381 381 ALA ALA B . n 
B 1 396 ASP 396 382 382 ASP ASP B . n 
B 1 397 GLN 397 383 383 GLN GLN B . n 
B 1 398 GLY 398 384 384 GLY GLY B . n 
B 1 399 THR 399 385 385 THR THR B . n 
B 1 400 SER 400 386 386 SER SER B . n 
B 1 401 ALA 401 387 387 ALA ALA B . n 
B 1 402 PHE 402 388 388 PHE PHE B . n 
B 1 403 GLY 403 389 389 GLY GLY B . n 
B 1 404 ALA 404 390 390 ALA ALA B . n 
B 1 405 ILE 405 391 391 ILE ILE B . n 
B 1 406 ASP 406 392 392 ASP ASP B . n 
B 1 407 LEU 407 393 393 LEU LEU B . n 
B 1 408 ARG 408 394 394 ARG ARG B . n 
B 1 409 LEU 409 395 395 LEU LEU B . n 
B 1 410 PRO 410 396 396 PRO PRO B . n 
B 1 411 ALA 411 397 397 ALA ALA B . n 
B 1 412 ASP 412 398 398 ASP ASP B . n 
B 1 413 VAL 413 399 399 VAL VAL B . n 
B 1 414 ASN 414 400 400 ASN ASN B . n 
B 1 415 PHE 415 401 401 PHE PHE B . n 
B 1 416 ILE 416 402 402 ILE ILE B . n 
B 1 417 VAL 417 403 403 VAL VAL B . n 
B 1 418 GLN 418 404 404 GLN GLN B . n 
B 1 419 PRO 419 405 405 PRO PRO B . n 
B 1 420 LEU 420 406 406 LEU LEU B . n 
B 1 421 TRP 421 407 407 TRP TRP B . n 
B 1 422 GLY 422 408 408 GLY GLY B . n 
B 1 423 SER 423 409 409 SER SER B . n 
B 1 424 ILE 424 410 410 ILE ILE B . n 
B 1 425 GLY 425 411 411 GLY GLY B . n 
B 1 426 TYR 426 412 412 TYR TYR B . n 
B 1 427 THR 427 413 413 THR THR B . n 
B 1 428 LEU 428 414 414 LEU LEU B . n 
B 1 429 ALA 429 415 415 ALA ALA B . n 
B 1 430 ALA 430 416 416 ALA ALA B . n 
B 1 431 ALA 431 417 417 ALA ALA B . n 
B 1 432 PHE 432 418 418 PHE PHE B . n 
B 1 433 GLY 433 419 419 GLY GLY B . n 
B 1 434 ALA 434 420 420 ALA ALA B . n 
B 1 435 GLN 435 421 421 GLN GLN B . n 
B 1 436 THR 436 422 422 THR THR B . n 
B 1 437 ALA 437 423 423 ALA ALA B . n 
B 1 438 CYS 438 424 424 CYS CYS B . n 
B 1 439 PRO 439 425 425 PRO PRO B . n 
B 1 440 ASN 440 426 426 ASN ASN B . n 
B 1 441 ARG 441 427 427 ARG ARG B . n 
B 1 442 ARG 442 428 428 ARG ARG B . n 
B 1 443 VAL 443 429 429 VAL VAL B . n 
B 1 444 ILE 444 430 430 ILE ILE B . n 
B 1 445 VAL 445 431 431 VAL VAL B . n 
B 1 446 LEU 446 432 432 LEU LEU B . n 
B 1 447 THR 447 433 433 THR THR B . n 
B 1 448 GLY 448 434 434 GLY GLY B . n 
B 1 449 ASP 449 435 435 ASP ASP B . n 
B 1 450 GLY 450 436 436 GLY GLY B . n 
B 1 451 ALA 451 437 437 ALA ALA B . n 
B 1 452 ALA 452 438 438 ALA ALA B . n 
B 1 453 GLN 453 439 439 GLN GLN B . n 
B 1 454 LEU 454 440 440 LEU LEU B . n 
B 1 455 THR 455 441 441 THR THR B . n 
B 1 456 ILE 456 442 442 ILE ILE B . n 
B 1 457 GLN 457 443 443 GLN GLN B . n 
B 1 458 GLU 458 444 444 GLU GLU B . n 
B 1 459 LEU 459 445 445 LEU LEU B . n 
B 1 460 GLY 460 446 446 GLY GLY B . n 
B 1 461 SER 461 447 447 SER SER B . n 
B 1 462 MET 462 448 448 MET MET B . n 
B 1 463 LEU 463 449 449 LEU LEU B . n 
B 1 464 ARG 464 450 450 ARG ARG B . n 
B 1 465 ASP 465 451 451 ASP ASP B . n 
B 1 466 LYS 466 452 452 LYS LYS B . n 
B 1 467 GLN 467 453 453 GLN GLN B . n 
B 1 468 HIS 468 454 454 HIS HIS B . n 
B 1 469 PRO 469 455 455 PRO PRO B . n 
B 1 470 ILE 470 456 456 ILE ILE B . n 
B 1 471 ILE 471 457 457 ILE ILE B . n 
B 1 472 LEU 472 458 458 LEU LEU B . n 
B 1 473 VAL 473 459 459 VAL VAL B . n 
B 1 474 LEU 474 460 460 LEU LEU B . n 
B 1 475 ASN 475 461 461 ASN ASN B . n 
B 1 476 ASN 476 462 462 ASN ASN B . n 
B 1 477 GLU 477 463 463 GLU GLU B . n 
B 1 478 GLY 478 464 464 GLY GLY B . n 
B 1 479 TYR 479 465 465 TYR TYR B . n 
B 1 480 THR 480 466 466 THR THR B . n 
B 1 481 VAL 481 467 467 VAL VAL B . n 
B 1 482 LEU 482 468 468 LEU LEU B . n 
B 1 483 ARG 483 469 469 ARG ARG B . n 
B 1 484 ALA 484 470 470 ALA ALA B . n 
B 1 485 ILE 485 471 471 ILE ILE B . n 
B 1 486 HIS 486 472 472 HIS HIS B . n 
B 1 487 GLY 487 473 473 GLY GLY B . n 
B 1 488 PRO 488 474 474 PRO PRO B . n 
B 1 489 GLU 489 475 475 GLU GLU B . n 
B 1 490 GLN 490 476 476 GLN GLN B . n 
B 1 491 ARG 491 477 477 ARG ARG B . n 
B 1 492 TYR 492 478 478 TYR TYR B . n 
B 1 493 ASN 493 479 479 ASN ASN B . n 
B 1 494 ASP 494 480 480 ASP ASP B . n 
B 1 495 ILE 495 481 481 ILE ILE B . n 
B 1 496 ALA 496 482 482 ALA ALA B . n 
B 1 497 LEU 497 483 483 LEU LEU B . n 
B 1 498 TRP 498 484 484 TRP TRP B . n 
B 1 499 ASN 499 485 485 ASN ASN B . n 
B 1 500 TRP 500 486 486 TRP TRP B . n 
B 1 501 THR 501 487 487 THR THR B . n 
B 1 502 GLN 502 488 488 GLN GLN B . n 
B 1 503 ILE 503 489 489 ILE ILE B . n 
B 1 504 PRO 504 490 490 PRO PRO B . n 
B 1 505 GLN 505 491 491 GLN GLN B . n 
B 1 506 ALA 506 492 492 ALA ALA B . n 
B 1 507 LEU 507 493 493 LEU LEU B . n 
B 1 508 SER 508 494 494 SER SER B . n 
B 1 509 LEU 509 495 495 LEU LEU B . n 
B 1 510 ASP 510 496 496 ASP ASP B . n 
B 1 511 PRO 511 497 497 PRO PRO B . n 
B 1 512 GLN 512 498 498 GLN GLN B . n 
B 1 513 ALA 513 499 499 ALA ALA B . n 
B 1 514 GLN 514 500 500 GLN GLN B . n 
B 1 515 CYS 515 501 501 CYS CYS B . n 
B 1 516 TRP 516 502 502 TRP TRP B . n 
B 1 517 ARG 517 503 503 ARG ARG B . n 
B 1 518 VAL 518 504 504 VAL VAL B . n 
B 1 519 SER 519 505 505 SER SER B . n 
B 1 520 GLU 520 506 506 GLU GLU B . n 
B 1 521 ALA 521 507 507 ALA ALA B . n 
B 1 522 GLU 522 508 508 GLU GLU B . n 
B 1 523 GLN 523 509 509 GLN GLN B . n 
B 1 524 LEU 524 510 510 LEU LEU B . n 
B 1 525 ALA 525 511 511 ALA ALA B . n 
B 1 526 ASP 526 512 512 ASP ASP B . n 
B 1 527 VAL 527 513 513 VAL VAL B . n 
B 1 528 LEU 528 514 514 LEU LEU B . n 
B 1 529 GLU 529 515 515 GLU GLU B . n 
B 1 530 LYS 530 516 516 LYS LYS B . n 
B 1 531 VAL 531 517 517 VAL VAL B . n 
B 1 532 ALA 532 518 518 ALA ALA B . n 
B 1 533 HIS 533 519 519 HIS HIS B . n 
B 1 534 HIS 534 520 520 HIS HIS B . n 
B 1 535 GLU 535 521 521 GLU GLU B . n 
B 1 536 ARG 536 522 522 ARG ARG B . n 
B 1 537 LEU 537 523 523 LEU LEU B . n 
B 1 538 SER 538 524 524 SER SER B . n 
B 1 539 LEU 539 525 525 LEU LEU B . n 
B 1 540 ILE 540 526 526 ILE ILE B . n 
B 1 541 GLU 541 527 527 GLU GLU B . n 
B 1 542 VAL 542 528 528 VAL VAL B . n 
B 1 543 MET 543 529 529 MET MET B . n 
B 1 544 LEU 544 530 530 LEU LEU B . n 
B 1 545 PRO 545 531 531 PRO PRO B . n 
B 1 546 LYS 546 532 532 LYS LYS B . n 
B 1 547 ALA 547 533 533 ALA ALA B . n 
B 1 548 ASP 548 534 534 ASP ASP B . n 
B 1 549 ILE 549 535 535 ILE ILE B . n 
B 1 550 PRO 550 536 536 PRO PRO B . n 
B 1 551 PRO 551 537 537 PRO PRO B . n 
B 1 552 LEU 552 538 538 LEU LEU B . n 
B 1 553 LEU 553 539 539 LEU LEU B . n 
B 1 554 GLY 554 540 540 GLY GLY B . n 
B 1 555 ALA 555 541 541 ALA ALA B . n 
B 1 556 ILE 556 542 542 ILE ILE B . n 
B 1 557 THR 557 543 543 THR THR B . n 
B 1 558 LYS 558 544 544 LYS LYS B . n 
B 1 559 ALA 559 545 545 ALA ALA B . n 
B 1 560 LEU 560 546 546 LEU LEU B . n 
B 1 561 GLU 561 547 547 GLU GLU B . n 
B 1 562 ALA 562 548 548 ALA ALA B . n 
B 1 563 ARG 563 549 ?   ?   ?   B . n 
B 1 564 ASN 564 550 ?   ?   ?   B . n 
B 1 565 SER 565 551 ?   ?   ?   B . n 
B 1 566 ALA 566 552 ?   ?   ?   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 3IO ? ? 3IO ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 TPP ? ? TPP ? ? '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 TPP 1   601 1   TPP TPP A . 
D 3 MG  1   602 1   MG  MG  A . 
E 4 3IO 1   603 2   3IO IPY A . 
F 2 TPP 1   601 2   TPP TPP B . 
G 3 MG  1   602 2   MG  MG  B . 
H 4 3IO 1   603 1   3IO IPY B . 
I 5 HOH 1   701 12  HOH HOH A . 
I 5 HOH 2   702 253 HOH HOH A . 
I 5 HOH 3   703 333 HOH HOH A . 
I 5 HOH 4   704 102 HOH HOH A . 
I 5 HOH 5   705 448 HOH HOH A . 
I 5 HOH 6   706 55  HOH HOH A . 
I 5 HOH 7   707 277 HOH HOH A . 
I 5 HOH 8   708 257 HOH HOH A . 
I 5 HOH 9   709 33  HOH HOH A . 
I 5 HOH 10  710 357 HOH HOH A . 
I 5 HOH 11  711 129 HOH HOH A . 
I 5 HOH 12  712 169 HOH HOH A . 
I 5 HOH 13  713 178 HOH HOH A . 
I 5 HOH 14  714 18  HOH HOH A . 
I 5 HOH 15  715 391 HOH HOH A . 
I 5 HOH 16  716 146 HOH HOH A . 
I 5 HOH 17  717 451 HOH HOH A . 
I 5 HOH 18  718 38  HOH HOH A . 
I 5 HOH 19  719 101 HOH HOH A . 
I 5 HOH 20  720 222 HOH HOH A . 
I 5 HOH 21  721 225 HOH HOH A . 
I 5 HOH 22  722 67  HOH HOH A . 
I 5 HOH 23  723 154 HOH HOH A . 
I 5 HOH 24  724 419 HOH HOH A . 
I 5 HOH 25  725 176 HOH HOH A . 
I 5 HOH 26  726 162 HOH HOH A . 
I 5 HOH 27  727 26  HOH HOH A . 
I 5 HOH 28  728 72  HOH HOH A . 
I 5 HOH 29  729 193 HOH HOH A . 
I 5 HOH 30  730 138 HOH HOH A . 
I 5 HOH 31  731 161 HOH HOH A . 
I 5 HOH 32  732 28  HOH HOH A . 
I 5 HOH 33  733 287 HOH HOH A . 
I 5 HOH 34  734 3   HOH HOH A . 
I 5 HOH 35  735 415 HOH HOH A . 
I 5 HOH 36  736 7   HOH HOH A . 
I 5 HOH 37  737 211 HOH HOH A . 
I 5 HOH 38  738 125 HOH HOH A . 
I 5 HOH 39  739 195 HOH HOH A . 
I 5 HOH 40  740 239 HOH HOH A . 
I 5 HOH 41  741 95  HOH HOH A . 
I 5 HOH 42  742 64  HOH HOH A . 
I 5 HOH 43  743 220 HOH HOH A . 
I 5 HOH 44  744 370 HOH HOH A . 
I 5 HOH 45  745 66  HOH HOH A . 
I 5 HOH 46  746 156 HOH HOH A . 
I 5 HOH 47  747 2   HOH HOH A . 
I 5 HOH 48  748 65  HOH HOH A . 
I 5 HOH 49  749 16  HOH HOH A . 
I 5 HOH 50  750 70  HOH HOH A . 
I 5 HOH 51  751 397 HOH HOH A . 
I 5 HOH 52  752 9   HOH HOH A . 
I 5 HOH 53  753 218 HOH HOH A . 
I 5 HOH 54  754 41  HOH HOH A . 
I 5 HOH 55  755 10  HOH HOH A . 
I 5 HOH 56  756 40  HOH HOH A . 
I 5 HOH 57  757 39  HOH HOH A . 
I 5 HOH 58  758 191 HOH HOH A . 
I 5 HOH 59  759 442 HOH HOH A . 
I 5 HOH 60  760 54  HOH HOH A . 
I 5 HOH 61  761 348 HOH HOH A . 
I 5 HOH 62  762 22  HOH HOH A . 
I 5 HOH 63  763 201 HOH HOH A . 
I 5 HOH 64  764 122 HOH HOH A . 
I 5 HOH 65  765 345 HOH HOH A . 
I 5 HOH 66  766 127 HOH HOH A . 
I 5 HOH 67  767 346 HOH HOH A . 
I 5 HOH 68  768 42  HOH HOH A . 
I 5 HOH 69  769 96  HOH HOH A . 
I 5 HOH 70  770 23  HOH HOH A . 
I 5 HOH 71  771 283 HOH HOH A . 
I 5 HOH 72  772 57  HOH HOH A . 
I 5 HOH 73  773 153 HOH HOH A . 
I 5 HOH 74  774 49  HOH HOH A . 
I 5 HOH 75  775 362 HOH HOH A . 
I 5 HOH 76  776 292 HOH HOH A . 
I 5 HOH 77  777 15  HOH HOH A . 
I 5 HOH 78  778 136 HOH HOH A . 
I 5 HOH 79  779 296 HOH HOH A . 
I 5 HOH 80  780 19  HOH HOH A . 
I 5 HOH 81  781 128 HOH HOH A . 
I 5 HOH 82  782 119 HOH HOH A . 
I 5 HOH 83  783 279 HOH HOH A . 
I 5 HOH 84  784 114 HOH HOH A . 
I 5 HOH 85  785 213 HOH HOH A . 
I 5 HOH 86  786 332 HOH HOH A . 
I 5 HOH 87  787 363 HOH HOH A . 
I 5 HOH 88  788 61  HOH HOH A . 
I 5 HOH 89  789 226 HOH HOH A . 
I 5 HOH 90  790 259 HOH HOH A . 
I 5 HOH 91  791 150 HOH HOH A . 
I 5 HOH 92  792 185 HOH HOH A . 
I 5 HOH 93  793 34  HOH HOH A . 
I 5 HOH 94  794 275 HOH HOH A . 
I 5 HOH 95  795 354 HOH HOH A . 
I 5 HOH 96  796 246 HOH HOH A . 
I 5 HOH 97  797 270 HOH HOH A . 
I 5 HOH 98  798 355 HOH HOH A . 
I 5 HOH 99  799 82  HOH HOH A . 
I 5 HOH 100 800 267 HOH HOH A . 
I 5 HOH 101 801 73  HOH HOH A . 
I 5 HOH 102 802 143 HOH HOH A . 
I 5 HOH 103 803 149 HOH HOH A . 
I 5 HOH 104 804 166 HOH HOH A . 
I 5 HOH 105 805 157 HOH HOH A . 
I 5 HOH 106 806 416 HOH HOH A . 
I 5 HOH 107 807 111 HOH HOH A . 
I 5 HOH 108 808 347 HOH HOH A . 
I 5 HOH 109 809 62  HOH HOH A . 
I 5 HOH 110 810 130 HOH HOH A . 
I 5 HOH 111 811 280 HOH HOH A . 
I 5 HOH 112 812 106 HOH HOH A . 
I 5 HOH 113 813 68  HOH HOH A . 
I 5 HOH 114 814 256 HOH HOH A . 
I 5 HOH 115 815 324 HOH HOH A . 
I 5 HOH 116 816 202 HOH HOH A . 
I 5 HOH 117 817 216 HOH HOH A . 
I 5 HOH 118 818 217 HOH HOH A . 
I 5 HOH 119 819 446 HOH HOH A . 
I 5 HOH 120 820 139 HOH HOH A . 
I 5 HOH 121 821 301 HOH HOH A . 
I 5 HOH 122 822 339 HOH HOH A . 
I 5 HOH 123 823 80  HOH HOH A . 
I 5 HOH 124 824 206 HOH HOH A . 
I 5 HOH 125 825 159 HOH HOH A . 
I 5 HOH 126 826 431 HOH HOH A . 
I 5 HOH 127 827 205 HOH HOH A . 
I 5 HOH 128 828 234 HOH HOH A . 
I 5 HOH 129 829 29  HOH HOH A . 
I 5 HOH 130 830 53  HOH HOH A . 
I 5 HOH 131 831 121 HOH HOH A . 
I 5 HOH 132 832 107 HOH HOH A . 
I 5 HOH 133 833 407 HOH HOH A . 
I 5 HOH 134 834 112 HOH HOH A . 
I 5 HOH 135 835 113 HOH HOH A . 
I 5 HOH 136 836 214 HOH HOH A . 
I 5 HOH 137 837 310 HOH HOH A . 
I 5 HOH 138 838 307 HOH HOH A . 
I 5 HOH 139 839 251 HOH HOH A . 
I 5 HOH 140 840 300 HOH HOH A . 
I 5 HOH 141 841 411 HOH HOH A . 
I 5 HOH 142 842 401 HOH HOH A . 
I 5 HOH 143 843 155 HOH HOH A . 
I 5 HOH 144 844 152 HOH HOH A . 
I 5 HOH 145 845 394 HOH HOH A . 
I 5 HOH 146 846 281 HOH HOH A . 
I 5 HOH 147 847 208 HOH HOH A . 
I 5 HOH 148 848 47  HOH HOH A . 
I 5 HOH 149 849 203 HOH HOH A . 
I 5 HOH 150 850 50  HOH HOH A . 
I 5 HOH 151 851 228 HOH HOH A . 
I 5 HOH 152 852 435 HOH HOH A . 
I 5 HOH 153 853 235 HOH HOH A . 
I 5 HOH 154 854 98  HOH HOH A . 
I 5 HOH 155 855 242 HOH HOH A . 
I 5 HOH 156 856 298 HOH HOH A . 
I 5 HOH 157 857 196 HOH HOH A . 
I 5 HOH 158 858 293 HOH HOH A . 
I 5 HOH 159 859 77  HOH HOH A . 
I 5 HOH 160 860 240 HOH HOH A . 
I 5 HOH 161 861 212 HOH HOH A . 
I 5 HOH 162 862 123 HOH HOH A . 
I 5 HOH 163 863 237 HOH HOH A . 
I 5 HOH 164 864 241 HOH HOH A . 
I 5 HOH 165 865 325 HOH HOH A . 
I 5 HOH 166 866 337 HOH HOH A . 
I 5 HOH 167 867 124 HOH HOH A . 
I 5 HOH 168 868 32  HOH HOH A . 
I 5 HOH 169 869 200 HOH HOH A . 
I 5 HOH 170 870 371 HOH HOH A . 
I 5 HOH 171 871 413 HOH HOH A . 
I 5 HOH 172 872 263 HOH HOH A . 
I 5 HOH 173 873 174 HOH HOH A . 
I 5 HOH 174 874 465 HOH HOH A . 
I 5 HOH 175 875 457 HOH HOH A . 
I 5 HOH 176 876 63  HOH HOH A . 
I 5 HOH 177 877 320 HOH HOH A . 
I 5 HOH 178 878 85  HOH HOH A . 
I 5 HOH 179 879 278 HOH HOH A . 
I 5 HOH 180 880 338 HOH HOH A . 
I 5 HOH 181 881 302 HOH HOH A . 
I 5 HOH 182 882 197 HOH HOH A . 
I 5 HOH 183 883 120 HOH HOH A . 
I 5 HOH 184 884 314 HOH HOH A . 
I 5 HOH 185 885 116 HOH HOH A . 
I 5 HOH 186 886 430 HOH HOH A . 
I 5 HOH 187 887 282 HOH HOH A . 
I 5 HOH 188 888 364 HOH HOH A . 
I 5 HOH 189 889 366 HOH HOH A . 
I 5 HOH 190 890 158 HOH HOH A . 
I 5 HOH 191 891 468 HOH HOH A . 
I 5 HOH 192 892 387 HOH HOH A . 
I 5 HOH 193 893 459 HOH HOH A . 
I 5 HOH 194 894 341 HOH HOH A . 
I 5 HOH 195 895 321 HOH HOH A . 
I 5 HOH 196 896 369 HOH HOH A . 
I 5 HOH 197 897 273 HOH HOH A . 
I 5 HOH 198 898 97  HOH HOH A . 
I 5 HOH 199 899 342 HOH HOH A . 
I 5 HOH 200 900 344 HOH HOH A . 
I 5 HOH 201 901 372 HOH HOH A . 
I 5 HOH 202 902 323 HOH HOH A . 
I 5 HOH 203 903 272 HOH HOH A . 
I 5 HOH 204 904 358 HOH HOH A . 
I 5 HOH 205 905 94  HOH HOH A . 
I 5 HOH 206 906 395 HOH HOH A . 
I 5 HOH 207 907 461 HOH HOH A . 
I 5 HOH 208 908 377 HOH HOH A . 
I 5 HOH 209 909 439 HOH HOH A . 
I 5 HOH 210 910 434 HOH HOH A . 
I 5 HOH 211 911 186 HOH HOH A . 
I 5 HOH 212 912 453 HOH HOH A . 
I 5 HOH 213 913 249 HOH HOH A . 
I 5 HOH 214 914 336 HOH HOH A . 
I 5 HOH 215 915 351 HOH HOH A . 
I 5 HOH 216 916 376 HOH HOH A . 
I 5 HOH 217 917 340 HOH HOH A . 
I 5 HOH 218 918 432 HOH HOH A . 
I 5 HOH 219 919 458 HOH HOH A . 
I 5 HOH 220 920 334 HOH HOH A . 
I 5 HOH 221 921 289 HOH HOH A . 
I 5 HOH 222 922 470 HOH HOH A . 
I 5 HOH 223 923 306 HOH HOH A . 
I 5 HOH 224 924 447 HOH HOH A . 
I 5 HOH 225 925 456 HOH HOH A . 
I 5 HOH 226 926 255 HOH HOH A . 
I 5 HOH 227 927 318 HOH HOH A . 
I 5 HOH 228 928 380 HOH HOH A . 
I 5 HOH 229 929 227 HOH HOH A . 
I 5 HOH 230 930 353 HOH HOH A . 
I 5 HOH 231 931 231 HOH HOH A . 
I 5 HOH 232 932 440 HOH HOH A . 
I 5 HOH 233 933 245 HOH HOH A . 
I 5 HOH 234 934 420 HOH HOH A . 
I 5 HOH 235 935 182 HOH HOH A . 
I 5 HOH 236 936 388 HOH HOH A . 
I 5 HOH 237 937 305 HOH HOH A . 
I 5 HOH 238 938 449 HOH HOH A . 
I 5 HOH 239 939 429 HOH HOH A . 
I 5 HOH 240 940 381 HOH HOH A . 
I 5 HOH 241 941 52  HOH HOH A . 
I 5 HOH 242 942 350 HOH HOH A . 
I 5 HOH 243 943 462 HOH HOH A . 
I 5 HOH 244 944 421 HOH HOH A . 
I 5 HOH 245 945 427 HOH HOH A . 
I 5 HOH 246 946 463 HOH HOH A . 
J 5 HOH 1   701 443 HOH HOH B . 
J 5 HOH 2   702 438 HOH HOH B . 
J 5 HOH 3   703 137 HOH HOH B . 
J 5 HOH 4   704 131 HOH HOH B . 
J 5 HOH 5   705 418 HOH HOH B . 
J 5 HOH 6   706 184 HOH HOH B . 
J 5 HOH 7   707 384 HOH HOH B . 
J 5 HOH 8   708 165 HOH HOH B . 
J 5 HOH 9   709 11  HOH HOH B . 
J 5 HOH 10  710 229 HOH HOH B . 
J 5 HOH 11  711 44  HOH HOH B . 
J 5 HOH 12  712 79  HOH HOH B . 
J 5 HOH 13  713 224 HOH HOH B . 
J 5 HOH 14  714 328 HOH HOH B . 
J 5 HOH 15  715 51  HOH HOH B . 
J 5 HOH 16  716 117 HOH HOH B . 
J 5 HOH 17  717 204 HOH HOH B . 
J 5 HOH 18  718 399 HOH HOH B . 
J 5 HOH 19  719 89  HOH HOH B . 
J 5 HOH 20  720 4   HOH HOH B . 
J 5 HOH 21  721 145 HOH HOH B . 
J 5 HOH 22  722 199 HOH HOH B . 
J 5 HOH 23  723 232 HOH HOH B . 
J 5 HOH 24  724 151 HOH HOH B . 
J 5 HOH 25  725 17  HOH HOH B . 
J 5 HOH 26  726 1   HOH HOH B . 
J 5 HOH 27  727 295 HOH HOH B . 
J 5 HOH 28  728 78  HOH HOH B . 
J 5 HOH 29  729 389 HOH HOH B . 
J 5 HOH 30  730 86  HOH HOH B . 
J 5 HOH 31  731 285 HOH HOH B . 
J 5 HOH 32  732 60  HOH HOH B . 
J 5 HOH 33  733 349 HOH HOH B . 
J 5 HOH 34  734 170 HOH HOH B . 
J 5 HOH 35  735 6   HOH HOH B . 
J 5 HOH 36  736 69  HOH HOH B . 
J 5 HOH 37  737 45  HOH HOH B . 
J 5 HOH 38  738 175 HOH HOH B . 
J 5 HOH 39  739 433 HOH HOH B . 
J 5 HOH 40  740 30  HOH HOH B . 
J 5 HOH 41  741 31  HOH HOH B . 
J 5 HOH 42  742 5   HOH HOH B . 
J 5 HOH 43  743 160 HOH HOH B . 
J 5 HOH 44  744 148 HOH HOH B . 
J 5 HOH 45  745 141 HOH HOH B . 
J 5 HOH 46  746 88  HOH HOH B . 
J 5 HOH 47  747 27  HOH HOH B . 
J 5 HOH 48  748 48  HOH HOH B . 
J 5 HOH 49  749 76  HOH HOH B . 
J 5 HOH 50  750 110 HOH HOH B . 
J 5 HOH 51  751 291 HOH HOH B . 
J 5 HOH 52  752 173 HOH HOH B . 
J 5 HOH 53  753 288 HOH HOH B . 
J 5 HOH 54  754 84  HOH HOH B . 
J 5 HOH 55  755 14  HOH HOH B . 
J 5 HOH 56  756 210 HOH HOH B . 
J 5 HOH 57  757 104 HOH HOH B . 
J 5 HOH 58  758 356 HOH HOH B . 
J 5 HOH 59  759 221 HOH HOH B . 
J 5 HOH 60  760 147 HOH HOH B . 
J 5 HOH 61  761 265 HOH HOH B . 
J 5 HOH 62  762 180 HOH HOH B . 
J 5 HOH 63  763 8   HOH HOH B . 
J 5 HOH 64  764 192 HOH HOH B . 
J 5 HOH 65  765 90  HOH HOH B . 
J 5 HOH 66  766 383 HOH HOH B . 
J 5 HOH 67  767 133 HOH HOH B . 
J 5 HOH 68  768 56  HOH HOH B . 
J 5 HOH 69  769 118 HOH HOH B . 
J 5 HOH 70  770 455 HOH HOH B . 
J 5 HOH 71  771 409 HOH HOH B . 
J 5 HOH 72  772 368 HOH HOH B . 
J 5 HOH 73  773 83  HOH HOH B . 
J 5 HOH 74  774 194 HOH HOH B . 
J 5 HOH 75  775 359 HOH HOH B . 
J 5 HOH 76  776 223 HOH HOH B . 
J 5 HOH 77  777 167 HOH HOH B . 
J 5 HOH 78  778 37  HOH HOH B . 
J 5 HOH 79  779 132 HOH HOH B . 
J 5 HOH 80  780 92  HOH HOH B . 
J 5 HOH 81  781 452 HOH HOH B . 
J 5 HOH 82  782 271 HOH HOH B . 
J 5 HOH 83  783 360 HOH HOH B . 
J 5 HOH 84  784 24  HOH HOH B . 
J 5 HOH 85  785 21  HOH HOH B . 
J 5 HOH 86  786 126 HOH HOH B . 
J 5 HOH 87  787 87  HOH HOH B . 
J 5 HOH 88  788 59  HOH HOH B . 
J 5 HOH 89  789 103 HOH HOH B . 
J 5 HOH 90  790 25  HOH HOH B . 
J 5 HOH 91  791 406 HOH HOH B . 
J 5 HOH 92  792 13  HOH HOH B . 
J 5 HOH 93  793 43  HOH HOH B . 
J 5 HOH 94  794 58  HOH HOH B . 
J 5 HOH 95  795 93  HOH HOH B . 
J 5 HOH 96  796 378 HOH HOH B . 
J 5 HOH 97  797 115 HOH HOH B . 
J 5 HOH 98  798 250 HOH HOH B . 
J 5 HOH 99  799 108 HOH HOH B . 
J 5 HOH 100 800 290 HOH HOH B . 
J 5 HOH 101 801 382 HOH HOH B . 
J 5 HOH 102 802 135 HOH HOH B . 
J 5 HOH 103 803 71  HOH HOH B . 
J 5 HOH 104 804 233 HOH HOH B . 
J 5 HOH 105 805 163 HOH HOH B . 
J 5 HOH 106 806 134 HOH HOH B . 
J 5 HOH 107 807 164 HOH HOH B . 
J 5 HOH 108 808 91  HOH HOH B . 
J 5 HOH 109 809 424 HOH HOH B . 
J 5 HOH 110 810 311 HOH HOH B . 
J 5 HOH 111 811 209 HOH HOH B . 
J 5 HOH 112 812 172 HOH HOH B . 
J 5 HOH 113 813 74  HOH HOH B . 
J 5 HOH 114 814 361 HOH HOH B . 
J 5 HOH 115 815 248 HOH HOH B . 
J 5 HOH 116 816 238 HOH HOH B . 
J 5 HOH 117 817 189 HOH HOH B . 
J 5 HOH 118 818 46  HOH HOH B . 
J 5 HOH 119 819 258 HOH HOH B . 
J 5 HOH 120 820 215 HOH HOH B . 
J 5 HOH 121 821 140 HOH HOH B . 
J 5 HOH 122 822 317 HOH HOH B . 
J 5 HOH 123 823 467 HOH HOH B . 
J 5 HOH 124 824 230 HOH HOH B . 
J 5 HOH 125 825 274 HOH HOH B . 
J 5 HOH 126 826 266 HOH HOH B . 
J 5 HOH 127 827 261 HOH HOH B . 
J 5 HOH 128 828 190 HOH HOH B . 
J 5 HOH 129 829 81  HOH HOH B . 
J 5 HOH 130 830 109 HOH HOH B . 
J 5 HOH 131 831 441 HOH HOH B . 
J 5 HOH 132 832 312 HOH HOH B . 
J 5 HOH 133 833 445 HOH HOH B . 
J 5 HOH 134 834 198 HOH HOH B . 
J 5 HOH 135 835 171 HOH HOH B . 
J 5 HOH 136 836 297 HOH HOH B . 
J 5 HOH 137 837 20  HOH HOH B . 
J 5 HOH 138 838 422 HOH HOH B . 
J 5 HOH 139 839 100 HOH HOH B . 
J 5 HOH 140 840 408 HOH HOH B . 
J 5 HOH 141 841 142 HOH HOH B . 
J 5 HOH 142 842 414 HOH HOH B . 
J 5 HOH 143 843 315 HOH HOH B . 
J 5 HOH 144 844 331 HOH HOH B . 
J 5 HOH 145 845 252 HOH HOH B . 
J 5 HOH 146 846 187 HOH HOH B . 
J 5 HOH 147 847 268 HOH HOH B . 
J 5 HOH 148 848 343 HOH HOH B . 
J 5 HOH 149 849 316 HOH HOH B . 
J 5 HOH 150 850 269 HOH HOH B . 
J 5 HOH 151 851 75  HOH HOH B . 
J 5 HOH 152 852 183 HOH HOH B . 
J 5 HOH 153 853 417 HOH HOH B . 
J 5 HOH 154 854 436 HOH HOH B . 
J 5 HOH 155 855 99  HOH HOH B . 
J 5 HOH 156 856 367 HOH HOH B . 
J 5 HOH 157 857 327 HOH HOH B . 
J 5 HOH 158 858 177 HOH HOH B . 
J 5 HOH 159 859 426 HOH HOH B . 
J 5 HOH 160 860 437 HOH HOH B . 
J 5 HOH 161 861 375 HOH HOH B . 
J 5 HOH 162 862 304 HOH HOH B . 
J 5 HOH 163 863 313 HOH HOH B . 
J 5 HOH 164 864 303 HOH HOH B . 
J 5 HOH 165 865 326 HOH HOH B . 
J 5 HOH 166 866 181 HOH HOH B . 
J 5 HOH 167 867 35  HOH HOH B . 
J 5 HOH 168 868 284 HOH HOH B . 
J 5 HOH 169 869 319 HOH HOH B . 
J 5 HOH 170 870 219 HOH HOH B . 
J 5 HOH 171 871 286 HOH HOH B . 
J 5 HOH 172 872 308 HOH HOH B . 
J 5 HOH 173 873 179 HOH HOH B . 
J 5 HOH 174 874 405 HOH HOH B . 
J 5 HOH 175 875 299 HOH HOH B . 
J 5 HOH 176 876 236 HOH HOH B . 
J 5 HOH 177 877 276 HOH HOH B . 
J 5 HOH 178 878 412 HOH HOH B . 
J 5 HOH 179 879 335 HOH HOH B . 
J 5 HOH 180 880 188 HOH HOH B . 
J 5 HOH 181 881 464 HOH HOH B . 
J 5 HOH 182 882 294 HOH HOH B . 
J 5 HOH 183 883 423 HOH HOH B . 
J 5 HOH 184 884 309 HOH HOH B . 
J 5 HOH 185 885 410 HOH HOH B . 
J 5 HOH 186 886 466 HOH HOH B . 
J 5 HOH 187 887 244 HOH HOH B . 
J 5 HOH 188 888 105 HOH HOH B . 
J 5 HOH 189 889 385 HOH HOH B . 
J 5 HOH 190 890 402 HOH HOH B . 
J 5 HOH 191 891 330 HOH HOH B . 
J 5 HOH 192 892 428 HOH HOH B . 
J 5 HOH 193 893 329 HOH HOH B . 
J 5 HOH 194 894 322 HOH HOH B . 
J 5 HOH 195 895 379 HOH HOH B . 
J 5 HOH 196 896 264 HOH HOH B . 
J 5 HOH 197 897 254 HOH HOH B . 
J 5 HOH 198 898 373 HOH HOH B . 
J 5 HOH 199 899 247 HOH HOH B . 
J 5 HOH 200 900 144 HOH HOH B . 
J 5 HOH 201 901 450 HOH HOH B . 
J 5 HOH 202 902 352 HOH HOH B . 
J 5 HOH 203 903 374 HOH HOH B . 
J 5 HOH 204 904 469 HOH HOH B . 
J 5 HOH 205 905 207 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZK8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     116.871 
_cell.length_a_esd                 ? 
_cell.length_b                     136.857 
_cell.length_b_esd                 ? 
_cell.length_c                     77.265 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZK8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 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                   8ZK8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.49 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.68 
_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    '0.1M calcium acetate, 0.1M sodium MES, pH 6.0, 13% PEG 400' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 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         2024-03-24 
_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   0.979 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL10U2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL10U2 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZK8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.16 
_reflns.d_resolution_low                               136.86 
_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                                     67251 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.74 
_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                                0.190 
_reflns.pdbx_Rpim_I_all                                0.075 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       429270 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.993 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.174 
_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                                    2.16 
_reflns_shell.d_res_low                                     2.22 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           30991 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4918 
_reflns_shell.percent_possible_obs                          100.0 
_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                               6.3 
_reflns_shell.pdbx_chi_squared                              0.75 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.8 
_reflns_shell.pdbx_Rrim_I_all                               1.097 
_reflns_shell.pdbx_Rpim_I_all                               0.435 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.874 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.005 
_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                                 8ZK8 
_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                            2.16 
_refine.ls_d_res_low                             19.98 
_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                     66964 
_refine.ls_number_reflns_R_free                  3271 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.82 
_refine.ls_percent_reflns_R_free                 4.88 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1838 
_refine.ls_R_factor_R_free                       0.2201 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1819 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_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             1.10 
_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                 26.06 
_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                            0.25 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.16 
_refine_hist.d_res_low                        19.98 
_refine_hist.number_atoms_solvent             451 
_refine_hist.number_atoms_total               8763 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8228 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005  ? 8506  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.863  ? 11598 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 10.153 ? 1164  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.049  ? 1312  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 1500  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.16 2.19  . . 156 2714 100.00 . . . . 0.2971 . . . . . . . . . . . 0.3655 
'X-RAY DIFFRACTION' 2.19 2.23  . . 141 2732 100.00 . . . . 0.2788 . . . . . . . . . . . 0.3730 
'X-RAY DIFFRACTION' 2.23 2.26  . . 116 2739 100.00 . . . . 0.2702 . . . . . . . . . . . 0.3406 
'X-RAY DIFFRACTION' 2.26 2.30  . . 124 2766 100.00 . . . . 0.2475 . . . . . . . . . . . 0.3019 
'X-RAY DIFFRACTION' 2.30 2.34  . . 140 2759 100.00 . . . . 0.2385 . . . . . . . . . . . 0.2878 
'X-RAY DIFFRACTION' 2.34 2.39  . . 143 2709 100.00 . . . . 0.2317 . . . . . . . . . . . 0.3078 
'X-RAY DIFFRACTION' 2.39 2.44  . . 158 2707 100.00 . . . . 0.2274 . . . . . . . . . . . 0.2703 
'X-RAY DIFFRACTION' 2.44 2.49  . . 142 2776 100.00 . . . . 0.2218 . . . . . . . . . . . 0.2758 
'X-RAY DIFFRACTION' 2.49 2.55  . . 130 2736 100.00 . . . . 0.2075 . . . . . . . . . . . 0.2525 
'X-RAY DIFFRACTION' 2.55 2.61  . . 134 2749 100.00 . . . . 0.1986 . . . . . . . . . . . 0.2495 
'X-RAY DIFFRACTION' 2.61 2.68  . . 142 2754 100.00 . . . . 0.1891 . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 2.68 2.76  . . 139 2738 100.00 . . . . 0.1971 . . . . . . . . . . . 0.2548 
'X-RAY DIFFRACTION' 2.76 2.85  . . 145 2765 100.00 . . . . 0.1811 . . . . . . . . . . . 0.2352 
'X-RAY DIFFRACTION' 2.85 2.95  . . 137 2728 100.00 . . . . 0.1849 . . . . . . . . . . . 0.2341 
'X-RAY DIFFRACTION' 2.95 3.07  . . 147 2772 100.00 . . . . 0.1737 . . . . . . . . . . . 0.2040 
'X-RAY DIFFRACTION' 3.07 3.21  . . 130 2782 100.00 . . . . 0.1728 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 3.21 3.38  . . 146 2763 100.00 . . . . 0.1581 . . . . . . . . . . . 0.2015 
'X-RAY DIFFRACTION' 3.38 3.59  . . 169 2764 100.00 . . . . 0.1575 . . . . . . . . . . . 0.2029 
'X-RAY DIFFRACTION' 3.59 3.86  . . 142 2789 100.00 . . . . 0.1498 . . . . . . . . . . . 0.1867 
'X-RAY DIFFRACTION' 3.86 4.25  . . 150 2812 100.00 . . . . 0.1476 . . . . . . . . . . . 0.1602 
'X-RAY DIFFRACTION' 4.25 4.85  . . 139 2819 100.00 . . . . 0.1401 . . . . . . . . . . . 0.1634 
'X-RAY DIFFRACTION' 4.85 6.09  . . 154 2854 100.00 . . . . 0.1738 . . . . . . . . . . . 0.1995 
'X-RAY DIFFRACTION' 6.09 19.98 . . 147 2966 100.00 . . . . 0.1774 . . . . . . . . . . . 0.1798 
# 
_struct.entry_id                     8ZK8 
_struct.title                        
'Crystal structure of the Decarboxylase KDC4427 mutant E468L in complex with indole-3-pyruvic acid' 
_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        8ZK8 
_struct_keywords.text            'Decarboxylase, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A2U3EYQ2_9ENTR 
_struct_ref.pdbx_db_accession          A0A2U3EYQ2 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MRTPYCVADYLLDRLTDCGADHLFGVPGDYNLQFLDHVIDSPDICWVGCANELNASYAADGYARCKGFAALLTTFGVGEL
SAMNGIAGSYAEHVPVLHIVGAPGTASQQRGELLHHTLGDGEFRHFYHMSEPITVAQAILTEQNACYEIDRVLTTMLRER
RPGYLMLPADVAKKAATPPVNALTLRHAHADSACLKAFRDAAENRLAMSKRTALLADFLVLRHGLKHALQKWVKDVPMAH
ATMLMGKGIFDERHVGFYGTYSGSASAGAVKEAIEGADTVLCIGTRFTDTLTAGFTHQLTPSQTIEVQPHASRVGDVWFT
GIPMLQAIETLVELCKQHVHDTPVPSSQSAMVYPQPDGSLTQDNFWKTLQTFIRPGDIILADQGTSAFGAIDLRLPADVN
FIVQPLWGSIGYTLAAAFGAQTACPNRRVIVLTGDGAAQLTIQELGSMLRDKQHPIILVLNNEGYTVERAIHGPEQRYND
IALWNWTQIPQALSLDPQAQCWRVSEAEQLADVLEKVAHHERLSLIEVMLPKADIPPLLGAITKALEARNSA
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZK8 A 15 ? 566 ? A0A2U3EYQ2 1 ? 552 ? 1 552 
2 1 8ZK8 B 15 ? 566 ? A0A2U3EYQ2 1 ? 552 ? 1 552 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZK8 MET A 1   ? UNP A0A2U3EYQ2 ?   ?   'initiating methionine' -13 1  
1 8ZK8 GLY A 2   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -12 2  
1 8ZK8 SER A 3   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -11 3  
1 8ZK8 SER A 4   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -10 4  
1 8ZK8 HIS A 5   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -9  5  
1 8ZK8 HIS A 6   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -8  6  
1 8ZK8 HIS A 7   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -7  7  
1 8ZK8 HIS A 8   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -6  8  
1 8ZK8 HIS A 9   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -5  9  
1 8ZK8 HIS A 10  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -4  10 
1 8ZK8 SER A 11  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -3  11 
1 8ZK8 GLN A 12  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -2  12 
1 8ZK8 ASP A 13  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -1  13 
1 8ZK8 PRO A 14  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        0   14 
1 8ZK8 LEU A 482 ? UNP A0A2U3EYQ2 GLU 468 'engineered mutation'   468 15 
2 8ZK8 MET B 1   ? UNP A0A2U3EYQ2 ?   ?   'initiating methionine' -13 16 
2 8ZK8 GLY B 2   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -12 17 
2 8ZK8 SER B 3   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -11 18 
2 8ZK8 SER B 4   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -10 19 
2 8ZK8 HIS B 5   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -9  20 
2 8ZK8 HIS B 6   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -8  21 
2 8ZK8 HIS B 7   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -7  22 
2 8ZK8 HIS B 8   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -6  23 
2 8ZK8 HIS B 9   ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -5  24 
2 8ZK8 HIS B 10  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -4  25 
2 8ZK8 SER B 11  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -3  26 
2 8ZK8 GLN B 12  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -2  27 
2 8ZK8 ASP B 13  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        -1  28 
2 8ZK8 PRO B 14  ? UNP A0A2U3EYQ2 ?   ?   'expression tag'        0   29 
2 8ZK8 LEU B 482 ? UNP A0A2U3EYQ2 GLU 468 'engineered mutation'   468 30 
# 
_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)' 9600  ? 
1 MORE         -84   ? 
1 'SSA (A^2)'  35210 ? 
# 
_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 CYS A 20  ? CYS A 32  ? CYS A 6   CYS A 18  1 ? 13 
HELX_P HELX_P2  AA2 GLY A 42  ? TYR A 44  ? GLY A 28  TYR A 30  5 ? 3  
HELX_P HELX_P3  AA3 ASN A 45  ? SER A 55  ? ASN A 31  SER A 41  1 ? 11 
HELX_P HELX_P4  AA4 ASN A 65  ? GLY A 81  ? ASN A 51  GLY A 67  1 ? 17 
HELX_P HELX_P5  AA5 GLY A 90  ? ALA A 96  ? GLY A 76  ALA A 82  1 ? 7  
HELX_P HELX_P6  AA6 ALA A 96  ? GLU A 106 ? ALA A 82  GLU A 92  1 ? 11 
HELX_P HELX_P7  AA7 GLY A 118 ? ARG A 124 ? GLY A 104 ARG A 110 1 ? 7  
HELX_P HELX_P8  AA8 ARG A 138 ? SER A 144 ? ARG A 124 SER A 130 1 ? 7  
HELX_P HELX_P9  AA9 GLU A 145 ? THR A 148 ? GLU A 131 THR A 134 5 ? 4  
HELX_P HELX_P10 AB1 ASN A 158 ? ARG A 174 ? ASN A 144 ARG A 160 1 ? 17 
HELX_P HELX_P11 AB2 ALA A 183 ? LYS A 187 ? ALA A 169 LYS A 173 1 ? 5  
HELX_P HELX_P12 AB3 ASP A 205 ? MET A 222 ? ASP A 191 MET A 208 1 ? 18 
HELX_P HELX_P13 AB4 ASP A 231 ? HIS A 237 ? ASP A 217 HIS A 223 1 ? 7  
HELX_P HELX_P14 AB5 LEU A 239 ? VAL A 250 ? LEU A 225 VAL A 236 1 ? 12 
HELX_P HELX_P15 AB6 SER A 276 ? SER A 280 ? SER A 262 SER A 266 5 ? 5  
HELX_P HELX_P16 AB7 ALA A 281 ? GLU A 289 ? ALA A 267 GLU A 275 1 ? 9  
HELX_P HELX_P17 AB8 PRO A 337 ? VAL A 353 ? PRO A 323 VAL A 339 1 ? 17 
HELX_P HELX_P18 AB9 THR A 375 ? ILE A 387 ? THR A 361 ILE A 373 1 ? 13 
HELX_P HELX_P19 AC1 GLY A 398 ? ILE A 405 ? GLY A 384 ILE A 391 1 ? 8  
HELX_P HELX_P20 AC2 GLY A 425 ? CYS A 438 ? GLY A 411 CYS A 424 1 ? 14 
HELX_P HELX_P21 AC3 ASP A 449 ? THR A 455 ? ASP A 435 THR A 441 1 ? 7  
HELX_P HELX_P22 AC4 GLN A 457 ? ASP A 465 ? GLN A 443 ASP A 451 1 ? 9  
HELX_P HELX_P23 AC5 TYR A 479 ? HIS A 486 ? TYR A 465 HIS A 472 1 ? 8  
HELX_P HELX_P24 AC6 GLN A 490 ? ASP A 494 ? GLN A 476 ASP A 480 5 ? 5  
HELX_P HELX_P25 AC7 ASN A 499 ? THR A 501 ? ASN A 485 THR A 487 5 ? 3  
HELX_P HELX_P26 AC8 GLN A 502 ? LEU A 507 ? GLN A 488 LEU A 493 1 ? 6  
HELX_P HELX_P27 AC9 GLU A 520 ? VAL A 531 ? GLU A 506 VAL A 517 1 ? 12 
HELX_P HELX_P28 AD1 PRO A 550 ? GLU A 561 ? PRO A 536 GLU A 547 1 ? 12 
HELX_P HELX_P29 AD2 CYS B 20  ? CYS B 32  ? CYS B 6   CYS B 18  1 ? 13 
HELX_P HELX_P30 AD3 ASN B 45  ? SER B 55  ? ASN B 31  SER B 41  1 ? 11 
HELX_P HELX_P31 AD4 ASN B 65  ? GLY B 81  ? ASN B 51  GLY B 67  1 ? 17 
HELX_P HELX_P32 AD5 GLY B 90  ? ALA B 96  ? GLY B 76  ALA B 82  1 ? 7  
HELX_P HELX_P33 AD6 ALA B 96  ? GLU B 106 ? ALA B 82  GLU B 92  1 ? 11 
HELX_P HELX_P34 AD7 GLY B 118 ? ARG B 124 ? GLY B 104 ARG B 110 1 ? 7  
HELX_P HELX_P35 AD8 ARG B 138 ? GLU B 145 ? ARG B 124 GLU B 131 1 ? 8  
HELX_P HELX_P36 AD9 PRO B 146 ? THR B 148 ? PRO B 132 THR B 134 5 ? 3  
HELX_P HELX_P37 AE1 ASN B 158 ? ARG B 174 ? ASN B 144 ARG B 160 1 ? 17 
HELX_P HELX_P38 AE2 ALA B 183 ? LYS B 187 ? ALA B 169 LYS B 173 1 ? 5  
HELX_P HELX_P39 AE3 ASP B 205 ? MET B 222 ? ASP B 191 MET B 208 1 ? 18 
HELX_P HELX_P40 AE4 ASP B 231 ? HIS B 237 ? ASP B 217 HIS B 223 1 ? 7  
HELX_P HELX_P41 AE5 LEU B 239 ? VAL B 250 ? LEU B 225 VAL B 236 1 ? 12 
HELX_P HELX_P42 AE6 SER B 276 ? SER B 280 ? SER B 262 SER B 266 5 ? 5  
HELX_P HELX_P43 AE7 ALA B 281 ? GLU B 289 ? ALA B 267 GLU B 275 1 ? 9  
HELX_P HELX_P44 AE8 PRO B 337 ? VAL B 353 ? PRO B 323 VAL B 339 1 ? 17 
HELX_P HELX_P45 AE9 THR B 375 ? ILE B 387 ? THR B 361 ILE B 373 1 ? 13 
HELX_P HELX_P46 AF1 GLY B 398 ? ILE B 405 ? GLY B 384 ILE B 391 1 ? 8  
HELX_P HELX_P47 AF2 GLY B 425 ? CYS B 438 ? GLY B 411 CYS B 424 1 ? 14 
HELX_P HELX_P48 AF3 ASP B 449 ? THR B 455 ? ASP B 435 THR B 441 1 ? 7  
HELX_P HELX_P49 AF4 GLN B 457 ? ASP B 465 ? GLN B 443 ASP B 451 1 ? 9  
HELX_P HELX_P50 AF5 TYR B 479 ? HIS B 486 ? TYR B 465 HIS B 472 1 ? 8  
HELX_P HELX_P51 AF6 GLN B 490 ? ASP B 494 ? GLN B 476 ASP B 480 5 ? 5  
HELX_P HELX_P52 AF7 ASN B 499 ? THR B 501 ? ASN B 485 THR B 487 5 ? 3  
HELX_P HELX_P53 AF8 GLN B 502 ? LEU B 507 ? GLN B 488 LEU B 493 1 ? 6  
HELX_P HELX_P54 AF9 GLU B 520 ? VAL B 531 ? GLU B 506 VAL B 517 1 ? 12 
HELX_P HELX_P55 AG1 PRO B 550 ? LEU B 560 ? PRO B 536 LEU B 546 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASP 449 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASP 435 A MG  602 1_555 ? ? ? ? ? ? ? 2.142 ? ? 
metalc2  metalc ? ? A ASN 476 OD1 ? ? ? 1_555 D MG  . MG ? ? A ASN 462 A MG  602 1_555 ? ? ? ? ? ? ? 1.942 ? ? 
metalc3  metalc ? ? A GLY 478 O   ? ? ? 1_555 D MG  . MG ? ? A GLY 464 A MG  602 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc4  metalc ? ? C TPP .   O2A ? ? ? 1_555 D MG  . MG ? ? A TPP 601 A MG  602 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc5  metalc ? ? C TPP .   O2B ? ? ? 1_555 D MG  . MG ? ? A TPP 601 A MG  602 1_555 ? ? ? ? ? ? ? 2.091 ? ? 
metalc6  metalc ? ? D MG  .   MG  ? ? ? 1_555 I HOH . O  ? ? A MG  602 A HOH 747 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc7  metalc ? ? B ASP 449 OD1 ? ? ? 1_555 G MG  . MG ? ? B ASP 435 B MG  602 1_555 ? ? ? ? ? ? ? 2.170 ? ? 
metalc8  metalc ? ? B ASN 476 OD1 ? ? ? 1_555 G MG  . MG ? ? B ASN 462 B MG  602 1_555 ? ? ? ? ? ? ? 2.058 ? ? 
metalc9  metalc ? ? B GLY 478 O   ? ? ? 1_555 G MG  . MG ? ? B GLY 464 B MG  602 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc10 metalc ? ? F TPP .   O2A ? ? ? 1_555 G MG  . MG ? ? B TPP 601 B MG  602 1_555 ? ? ? ? ? ? ? 1.973 ? ? 
metalc11 metalc ? ? F TPP .   O3B ? ? ? 1_555 G MG  . MG ? ? B TPP 601 B MG  602 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc12 metalc ? ? G MG  .   MG  ? ? ? 1_555 J HOH . O  ? ? B MG  602 B HOH 735 1_555 ? ? ? ? ? ? ? 1.920 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 OD1 ? A ASN 476 ? A ASN 462 ? 1_555 96.2  ? 
2  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? A GLY 478 ? A GLY 464 ? 1_555 102.1 ? 
3  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? A GLY 478 ? A GLY 464 ? 1_555 96.5  ? 
4  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 79.5  ? 
5  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 167.7 ? 
6  O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2A ? C TPP .   ? A TPP 601 ? 1_555 95.7  ? 
7  OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 159.5 ? 
8  OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 94.0  ? 
9  O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 94.4  ? 
10 O2A ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O2B ? C TPP .   ? A TPP 601 ? 1_555 86.8  ? 
11 OD1 ? A ASP 449 ? A ASP 435 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? I HOH .   ? A HOH 747 ? 1_555 82.8  ? 
12 OD1 ? A ASN 476 ? A ASN 462 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? I HOH .   ? A HOH 747 ? 1_555 84.6  ? 
13 O   ? A GLY 478 ? A GLY 464 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? I HOH .   ? A HOH 747 ? 1_555 174.9 ? 
14 O2A ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? I HOH .   ? A HOH 747 ? 1_555 83.4  ? 
15 O2B ? C TPP .   ? A TPP 601 ? 1_555 MG ? D MG . ? A MG 602 ? 1_555 O   ? I HOH .   ? A HOH 747 ? 1_555 80.5  ? 
16 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 98.1  ? 
17 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? B GLY 478 ? B GLY 464 ? 1_555 100.0 ? 
18 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? B GLY 478 ? B GLY 464 ? 1_555 89.8  ? 
19 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O2A ? F TPP .   ? B TPP 601 ? 1_555 81.2  ? 
20 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O2A ? F TPP .   ? B TPP 601 ? 1_555 176.5 ? 
21 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O2A ? F TPP .   ? B TPP 601 ? 1_555 93.6  ? 
22 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O3B ? F TPP .   ? B TPP 601 ? 1_555 160.1 ? 
23 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O3B ? F TPP .   ? B TPP 601 ? 1_555 89.6  ? 
24 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O3B ? F TPP .   ? B TPP 601 ? 1_555 98.3  ? 
25 O2A ? F TPP .   ? B TPP 601 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O3B ? F TPP .   ? B TPP 601 ? 1_555 89.9  ? 
26 OD1 ? B ASP 449 ? B ASP 435 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? J HOH .   ? B HOH 735 ? 1_555 79.2  ? 
27 OD1 ? B ASN 476 ? B ASN 462 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? J HOH .   ? B HOH 735 ? 1_555 91.8  ? 
28 O   ? B GLY 478 ? B GLY 464 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? J HOH .   ? B HOH 735 ? 1_555 178.3 ? 
29 O2A ? F TPP .   ? B TPP 601 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? J HOH .   ? B HOH 735 ? 1_555 84.8  ? 
30 O3B ? F TPP .   ? B TPP 601 ? 1_555 MG ? G MG . ? B MG 602 ? 1_555 O   ? J HOH .   ? B HOH 735 ? 1_555 82.3  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 6 ? 
AA3 ? 6 ? 
AA4 ? 6 ? 
AA5 ? 6 ? 
AA6 ? 6 ? 
# 
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 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? parallel      
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? anti-parallel 
AA5 5 6 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? 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 CYS A 59  ? GLY A 62  ? CYS A 45  GLY A 48  
AA1 2 HIS A 36  ? GLY A 39  ? HIS A 22  GLY A 25  
AA1 3 ALA A 83  ? THR A 88  ? ALA A 69  THR A 74  
AA1 4 VAL A 110 ? ALA A 116 ? VAL A 96  ALA A 102 
AA1 5 GLY A 177 ? PRO A 182 ? GLY A 163 PRO A 168 
AA1 6 ALA A 150 ? ILE A 153 ? ALA A 136 ILE A 139 
AA2 1 ALA A 253 ? THR A 256 ? ALA A 239 THR A 242 
AA2 2 THR A 226 ? ALA A 230 ? THR A 212 ALA A 216 
AA2 3 THR A 293 ? ILE A 297 ? THR A 279 ILE A 283 
AA2 4 THR A 318 ? VAL A 321 ? THR A 304 VAL A 307 
AA2 5 ALA A 325 ? VAL A 328 ? ALA A 311 VAL A 314 
AA2 6 VAL A 331 ? THR A 334 ? VAL A 317 THR A 320 
AA3 1 ASN A 414 ? ILE A 416 ? ASN A 400 ILE A 402 
AA3 2 ILE A 392 ? ALA A 395 ? ILE A 378 ALA A 381 
AA3 3 VAL A 443 ? GLY A 448 ? VAL A 429 GLY A 434 
AA3 4 ILE A 470 ? ASN A 475 ? ILE A 456 ASN A 461 
AA3 5 LEU A 537 ? MET A 543 ? LEU A 523 MET A 529 
AA3 6 ALA A 513 ? VAL A 518 ? ALA A 499 VAL A 504 
AA4 1 CYS B 59  ? GLY B 62  ? CYS B 45  GLY B 48  
AA4 2 HIS B 36  ? GLY B 39  ? HIS B 22  GLY B 25  
AA4 3 ALA B 83  ? THR B 88  ? ALA B 69  THR B 74  
AA4 4 VAL B 110 ? ALA B 116 ? VAL B 96  ALA B 102 
AA4 5 GLY B 177 ? PRO B 182 ? GLY B 163 PRO B 168 
AA4 6 ALA B 150 ? ILE B 153 ? ALA B 136 ILE B 139 
AA5 1 HIS B 254 ? THR B 256 ? HIS B 240 THR B 242 
AA5 2 THR B 226 ? ALA B 230 ? THR B 212 ALA B 216 
AA5 3 THR B 293 ? ILE B 297 ? THR B 279 ILE B 283 
AA5 4 THR B 318 ? VAL B 321 ? THR B 304 VAL B 307 
AA5 5 ALA B 325 ? VAL B 328 ? ALA B 311 VAL B 314 
AA5 6 VAL B 331 ? THR B 334 ? VAL B 317 THR B 320 
AA6 1 ASN B 414 ? ILE B 416 ? ASN B 400 ILE B 402 
AA6 2 ILE B 392 ? ALA B 395 ? ILE B 378 ALA B 381 
AA6 3 VAL B 443 ? GLY B 448 ? VAL B 429 GLY B 434 
AA6 4 ILE B 470 ? ASN B 475 ? ILE B 456 ASN B 461 
AA6 5 LEU B 537 ? MET B 543 ? LEU B 523 MET B 529 
AA6 6 ALA B 513 ? VAL B 518 ? ALA B 499 VAL B 504 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 61  ? O VAL A 47  N LEU A 37  ? N LEU A 23  
AA1 2 3 N PHE A 38  ? N PHE A 24  O LEU A 86  ? O LEU A 72  
AA1 3 4 N LEU A 85  ? N LEU A 71  O ILE A 113 ? O ILE A 99  
AA1 4 5 N VAL A 114 ? N VAL A 100 O LEU A 181 ? O LEU A 167 
AA1 5 6 O MET A 180 ? O MET A 166 N ALA A 152 ? N ALA A 138 
AA2 1 2 O ALA A 253 ? O ALA A 239 N LEU A 228 ? N LEU A 214 
AA2 2 3 N LEU A 229 ? N LEU A 215 O LEU A 295 ? O LEU A 281 
AA2 3 4 N CYS A 296 ? N CYS A 282 O ILE A 319 ? O ILE A 305 
AA2 4 5 N GLU A 320 ? N GLU A 306 O ARG A 327 ? O ARG A 313 
AA2 5 6 N SER A 326 ? N SER A 312 O PHE A 333 ? O PHE A 319 
AA3 1 2 O ILE A 416 ? O ILE A 402 N ILE A 393 ? N ILE A 379 
AA3 2 3 N LEU A 394 ? N LEU A 380 O LEU A 446 ? O LEU A 432 
AA3 3 4 N VAL A 445 ? N VAL A 431 O LEU A 472 ? O LEU A 458 
AA3 4 5 N ILE A 471 ? N ILE A 457 O SER A 538 ? O SER A 524 
AA3 5 6 O GLU A 541 ? O GLU A 527 N TRP A 516 ? N TRP A 502 
AA4 1 2 O VAL B 61  ? O VAL B 47  N LEU B 37  ? N LEU B 23  
AA4 2 3 N PHE B 38  ? N PHE B 24  O LEU B 86  ? O LEU B 72  
AA4 3 4 N LEU B 85  ? N LEU B 71  O LEU B 111 ? O LEU B 97  
AA4 4 5 N HIS B 112 ? N HIS B 98  O LEU B 179 ? O LEU B 165 
AA4 5 6 O MET B 180 ? O MET B 166 N ALA B 152 ? N ALA B 138 
AA5 1 2 O ALA B 255 ? O ALA B 241 N LEU B 228 ? N LEU B 214 
AA5 2 3 N LEU B 229 ? N LEU B 215 O LEU B 295 ? O LEU B 281 
AA5 3 4 N CYS B 296 ? N CYS B 282 O ILE B 319 ? O ILE B 305 
AA5 4 5 N GLU B 320 ? N GLU B 306 O ARG B 327 ? O ARG B 313 
AA5 5 6 N SER B 326 ? N SER B 312 O PHE B 333 ? O PHE B 319 
AA6 1 2 O ILE B 416 ? O ILE B 402 N ILE B 393 ? N ILE B 379 
AA6 2 3 N LEU B 394 ? N LEU B 380 O LEU B 446 ? O LEU B 432 
AA6 3 4 N VAL B 445 ? N VAL B 431 O LEU B 472 ? O LEU B 458 
AA6 4 5 N ILE B 471 ? N ILE B 457 O SER B 538 ? O SER B 524 
AA6 5 6 O GLU B 541 ? O GLU B 527 N TRP B 516 ? N TRP B 502 
# 
_pdbx_entry_details.entry_id                   8ZK8 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 PHE A 68  ? ? -170.50 149.38 
2  1 HIS A 93  ? ? 60.17   60.70  
3  1 ARG A 186 ? ? 60.00   76.69  
4  1 HIS A 187 ? ? -34.23  134.92 
5  1 ILE A 274 ? ? -93.81  -63.08 
6  1 HIS A 340 ? ? -102.37 57.84  
7  1 VAL A 344 ? ? 47.28   97.39  
8  1 ASP A 496 ? ? -155.72 75.71  
9  1 GLU A 547 ? ? -68.30  91.28  
10 1 ARG B 186 ? ? 60.42   74.48  
11 1 HIS B 187 ? ? -36.51  136.97 
12 1 ILE B 274 ? ? -94.45  -63.22 
13 1 ASP B 341 ? ? -43.63  153.00 
14 1 VAL B 344 ? ? 41.98   87.42  
15 1 ASP B 496 ? ? -156.38 72.55  
16 1 GLN B 498 ? ? -91.88  52.89  
17 1 HIS B 520 ? ? 37.52   51.80  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 18.8034  6.7301  20.3929  0.2142 ? -0.0120 ? -0.0258 ? 0.2255 ? 0.0351  ? 0.3597 ? 1.1443 ? 
0.1848  ? -0.1728 ? 1.4075 ? -0.0660 ? 1.0012 ? 0.0187  ? -0.1644 ? -0.1535 ? 0.1941  ? -0.0786 ? -0.1366 ? 0.0672  ? 0.1460  ? 
0.0762  ? 
2  'X-RAY DIFFRACTION' ? refined 22.7606  -5.9031 17.8692  0.2899 ? 0.0135  ? -0.0681 ? 0.2464 ? 0.0762  ? 0.5242 ? 0.9071 ? 
0.9563  ? 1.1192  ? 1.0512 ? 1.4574  ? 2.7905 ? -0.0110 ? -0.0525 ? -0.2237 ? 0.2718  ? -0.0254 ? -0.3088 ? 0.3956  ? 0.1961  ? 
0.0205  ? 
3  'X-RAY DIFFRACTION' ? refined 27.5198  -3.7809 -13.5526 0.2615 ? 0.0137  ? 0.0923  ? 0.2473 ? -0.0280 ? 0.4843 ? 1.0229 ? 
-0.0758 ? -0.2056 ? 2.4092 ? -0.0385 ? 0.9222 ? -0.0322 ? 0.0705  ? -0.1522 ? -0.3112 ? -0.0218 ? -0.3469 ? 0.0112  ? 0.0732  ? 
0.0662  ? 
4  'X-RAY DIFFRACTION' ? refined 33.7461  16.9337 -10.6117 0.2499 ? -0.0411 ? 0.0781  ? 0.2645 ? -0.0007 ? 0.4300 ? 2.6202 ? 
-0.4004 ? 0.8420  ? 5.9949 ? 0.0799  ? 1.2646 ? -0.0259 ? 0.2057  ? -0.0770 ? -0.6669 ? 0.0516  ? -0.3186 ? 0.1019  ? 0.1939  ? 
0.0088  ? 
5  'X-RAY DIFFRACTION' ? refined 24.3929  23.0152 2.1888   0.2490 ? -0.0221 ? 0.0234  ? 0.2168 ? 0.0196  ? 0.4173 ? 1.7350 ? 
0.0162  ? 0.4462  ? 1.0116 ? -0.2935 ? 1.1993 ? -0.0146 ? 0.1015  ? 0.1068  ? -0.0278 ? -0.0201 ? -0.2045 ? -0.1586 ? 0.1202  ? 
0.0340  ? 
6  'X-RAY DIFFRACTION' ? refined 29.8137  30.1801 -2.1387  0.2703 ? -0.0366 ? 0.0621  ? 0.2234 ? 0.0378  ? 0.5432 ? 1.2238 ? 
0.1718  ? 0.0871  ? 1.8837 ? 0.9336  ? 3.8992 ? -0.0318 ? 0.0897  ? 0.2148  ? -0.1772 ? 0.0560  ? -0.3486 ? -0.1793 ? 0.4145  ? 
-0.0624 ? 
7  'X-RAY DIFFRACTION' ? refined 0.3993   19.8797 3.2920   0.2106 ? 0.0106  ? -0.0033 ? 0.2224 ? 0.0127  ? 0.4277 ? 0.7024 ? 
0.1199  ? -0.0771 ? 1.3497 ? 0.0758  ? 0.7328 ? 0.0064  ? 0.0530  ? 0.0735  ? -0.0576 ? -0.0122 ? 0.1549  ? -0.0504 ? -0.1059 ? 
0.0060  ? 
8  'X-RAY DIFFRACTION' ? refined -12.9234 19.5891 5.8501   0.1920 ? 0.0231  ? -0.0208 ? 0.2340 ? 0.0128  ? 0.4990 ? 0.7557 ? 
0.7348  ? 0.2535  ? 1.6622 ? -0.9290 ? 2.8497 ? 0.0404  ? 0.0028  ? 0.1771  ? 0.0549  ? 0.0362  ? 0.4316  ? -0.0651 ? -0.4214 ? 
-0.1183 ? 
9  'X-RAY DIFFRACTION' ? refined -11.1278 24.4251 37.5336  0.4132 ? -0.0522 ? 0.1681  ? 0.3797 ? -0.1313 ? 0.5153 ? 2.1193 ? 
0.7548  ? -0.3693 ? 1.2686 ? 0.0863  ? 1.1358 ? 0.1622  ? -0.5240 ? 0.4248  ? 0.4279  ? -0.2116 ? 0.4478  ? -0.1512 ? -0.0431 ? 
0.0342  ? 
10 'X-RAY DIFFRACTION' ? refined -5.7574  34.0036 38.2773  0.5781 ? -0.0852 ? 0.1575  ? 0.5054 ? -0.2083 ? 0.8145 ? 5.9715 ? 
2.0323  ? -0.6009 ? 1.1887 ? 0.0829  ? 0.1924 ? 0.2578  ? -1.2280 ? 0.7537  ? 0.4953  ? -0.3712 ? 0.6678  ? -0.2376 ? -0.1027 ? 
0.0029  ? 
11 'X-RAY DIFFRACTION' ? refined 11.2553  32.1384 23.9658  0.2404 ? -0.0464 ? 0.0199  ? 0.2052 ? -0.0585 ? 0.3423 ? 1.1015 ? 
0.3931  ? 0.2546  ? 1.2186 ? 0.0690  ? 1.2615 ? 0.0885  ? -0.1461 ? 0.2122  ? 0.2056  ? -0.0902 ? 0.0557  ? -0.1304 ? -0.0112 ? 
0.0169  ? 
12 'X-RAY DIFFRACTION' ? refined 23.3453  39.1769 18.0223  0.2790 ? -0.0739 ? -0.0290 ? 0.2247 ? -0.0098 ? 0.5574 ? 2.0833 ? 
0.3802  ? -0.9855 ? 0.8967 ? 1.1917  ? 3.2533 ? 0.0800  ? -0.1975 ? 0.3877  ? -0.0293 ? -0.0305 ? -0.2391 ? -0.4579 ? 0.0127  ? 
-0.1308 ? 
13 'X-RAY DIFFRACTION' ? refined 16.0034  37.1622 31.2272  0.3499 ? -0.0751 ? 0.0132  ? 0.3192 ? -0.1231 ? 0.4009 ? 3.2245 ? 
-0.7203 ? 0.3737  ? 1.3791 ? 0.1343  ? 3.7265 ? 0.0717  ? -0.5610 ? 0.3322  ? 0.2893  ? 0.0102  ? -0.1073 ? -0.1014 ? 0.0537  ? 
-0.0125 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 3 through 144 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 145 through 191 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 192 through 338 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 339 through 403 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 404 through 479 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 480 through 548 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 144 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 145 through 191 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 192 through 323 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 324 through 370 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 371 through 479 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 480 through 506 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 507 through 548 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -13 ? A MET 1   
2  1 Y 1 A GLY -12 ? A GLY 2   
3  1 Y 1 A SER -11 ? A SER 3   
4  1 Y 1 A SER -10 ? A SER 4   
5  1 Y 1 A HIS -9  ? A HIS 5   
6  1 Y 1 A HIS -8  ? A HIS 6   
7  1 Y 1 A HIS -7  ? A HIS 7   
8  1 Y 1 A HIS -6  ? A HIS 8   
9  1 Y 1 A HIS -5  ? A HIS 9   
10 1 Y 1 A HIS -4  ? A HIS 10  
11 1 Y 1 A SER -3  ? A SER 11  
12 1 Y 1 A GLN -2  ? A GLN 12  
13 1 Y 1 A ASP -1  ? A ASP 13  
14 1 Y 1 A PRO 0   ? A PRO 14  
15 1 Y 1 A MET 1   ? A MET 15  
16 1 Y 1 A ARG 2   ? A ARG 16  
17 1 Y 1 A SER 346 ? A SER 360 
18 1 Y 1 A SER 347 ? A SER 361 
19 1 Y 1 A GLN 348 ? A GLN 362 
20 1 Y 1 A SER 349 ? A SER 363 
21 1 Y 1 A ALA 350 ? A ALA 364 
22 1 Y 1 A MET 351 ? A MET 365 
23 1 Y 1 A VAL 352 ? A VAL 366 
24 1 Y 1 A TYR 353 ? A TYR 367 
25 1 Y 1 A PRO 354 ? A PRO 368 
26 1 Y 1 A GLN 355 ? A GLN 369 
27 1 Y 1 A ARG 549 ? A ARG 563 
28 1 Y 1 A ASN 550 ? A ASN 564 
29 1 Y 1 A SER 551 ? A SER 565 
30 1 Y 1 A ALA 552 ? A ALA 566 
31 1 Y 1 B MET -13 ? B MET 1   
32 1 Y 1 B GLY -12 ? B GLY 2   
33 1 Y 1 B SER -11 ? B SER 3   
34 1 Y 1 B SER -10 ? B SER 4   
35 1 Y 1 B HIS -9  ? B HIS 5   
36 1 Y 1 B HIS -8  ? B HIS 6   
37 1 Y 1 B HIS -7  ? B HIS 7   
38 1 Y 1 B HIS -6  ? B HIS 8   
39 1 Y 1 B HIS -5  ? B HIS 9   
40 1 Y 1 B HIS -4  ? B HIS 10  
41 1 Y 1 B SER -3  ? B SER 11  
42 1 Y 1 B GLN -2  ? B GLN 12  
43 1 Y 1 B ASP -1  ? B ASP 13  
44 1 Y 1 B PRO 0   ? B PRO 14  
45 1 Y 1 B MET 1   ? B MET 15  
46 1 Y 1 B ARG 2   ? B ARG 16  
47 1 Y 1 B SER 346 ? B SER 360 
48 1 Y 1 B SER 347 ? B SER 361 
49 1 Y 1 B GLN 348 ? B GLN 362 
50 1 Y 1 B SER 349 ? B SER 363 
51 1 Y 1 B ALA 350 ? B ALA 364 
52 1 Y 1 B MET 351 ? B MET 365 
53 1 Y 1 B VAL 352 ? B VAL 366 
54 1 Y 1 B TYR 353 ? B TYR 367 
55 1 Y 1 B PRO 354 ? B PRO 368 
56 1 Y 1 B GLN 355 ? B GLN 369 
57 1 Y 1 B ARG 549 ? B ARG 563 
58 1 Y 1 B ASN 550 ? B ASN 564 
59 1 Y 1 B SER 551 ? B SER 565 
60 1 Y 1 B ALA 552 ? B ALA 566 
# 
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 
3IO CAO    C  Y N 1   
3IO CAG    C  Y N 2   
3IO CAE    C  Y N 3   
3IO CAD    C  Y N 4   
3IO CAF    C  Y N 5   
3IO CAN    C  Y N 6   
3IO NAJ    N  Y N 7   
3IO CAH    C  Y N 8   
3IO CAM    C  Y N 9   
3IO CAI    C  N N 10  
3IO CAL    C  N N 11  
3IO OAB    O  N N 12  
3IO CAK    C  N N 13  
3IO OAC    O  N N 14  
3IO OAA    O  N N 15  
3IO HAG    H  N N 16  
3IO HAE    H  N N 17  
3IO HAD    H  N N 18  
3IO HAF    H  N N 19  
3IO HNAJ   H  N N 20  
3IO HAH    H  N N 21  
3IO HAI1   H  N N 22  
3IO HAI2   H  N N 23  
3IO HOAC   H  N N 24  
ALA N      N  N N 25  
ALA CA     C  N S 26  
ALA C      C  N N 27  
ALA O      O  N N 28  
ALA CB     C  N N 29  
ALA OXT    O  N N 30  
ALA H      H  N N 31  
ALA H2     H  N N 32  
ALA HA     H  N N 33  
ALA HB1    H  N N 34  
ALA HB2    H  N N 35  
ALA HB3    H  N N 36  
ALA HXT    H  N N 37  
ARG N      N  N N 38  
ARG CA     C  N S 39  
ARG C      C  N N 40  
ARG O      O  N N 41  
ARG CB     C  N N 42  
ARG CG     C  N N 43  
ARG CD     C  N N 44  
ARG NE     N  N N 45  
ARG CZ     C  N N 46  
ARG NH1    N  N N 47  
ARG NH2    N  N N 48  
ARG OXT    O  N N 49  
ARG H      H  N N 50  
ARG H2     H  N N 51  
ARG HA     H  N N 52  
ARG HB2    H  N N 53  
ARG HB3    H  N N 54  
ARG HG2    H  N N 55  
ARG HG3    H  N N 56  
ARG HD2    H  N N 57  
ARG HD3    H  N N 58  
ARG HE     H  N N 59  
ARG HH11   H  N N 60  
ARG HH12   H  N N 61  
ARG HH21   H  N N 62  
ARG HH22   H  N N 63  
ARG HXT    H  N N 64  
ASN N      N  N N 65  
ASN CA     C  N S 66  
ASN C      C  N N 67  
ASN O      O  N N 68  
ASN CB     C  N N 69  
ASN CG     C  N N 70  
ASN OD1    O  N N 71  
ASN ND2    N  N N 72  
ASN OXT    O  N N 73  
ASN H      H  N N 74  
ASN H2     H  N N 75  
ASN HA     H  N N 76  
ASN HB2    H  N N 77  
ASN HB3    H  N N 78  
ASN HD21   H  N N 79  
ASN HD22   H  N N 80  
ASN HXT    H  N N 81  
ASP N      N  N N 82  
ASP CA     C  N S 83  
ASP C      C  N N 84  
ASP O      O  N N 85  
ASP CB     C  N N 86  
ASP CG     C  N N 87  
ASP OD1    O  N N 88  
ASP OD2    O  N N 89  
ASP OXT    O  N N 90  
ASP H      H  N N 91  
ASP H2     H  N N 92  
ASP HA     H  N N 93  
ASP HB2    H  N N 94  
ASP HB3    H  N N 95  
ASP HD2    H  N N 96  
ASP HXT    H  N N 97  
CYS N      N  N N 98  
CYS CA     C  N R 99  
CYS C      C  N N 100 
CYS O      O  N N 101 
CYS CB     C  N N 102 
CYS SG     S  N N 103 
CYS OXT    O  N N 104 
CYS H      H  N N 105 
CYS H2     H  N N 106 
CYS HA     H  N N 107 
CYS HB2    H  N N 108 
CYS HB3    H  N N 109 
CYS HG     H  N N 110 
CYS HXT    H  N N 111 
GLN N      N  N N 112 
GLN CA     C  N S 113 
GLN C      C  N N 114 
GLN O      O  N N 115 
GLN CB     C  N N 116 
GLN CG     C  N N 117 
GLN CD     C  N N 118 
GLN OE1    O  N N 119 
GLN NE2    N  N N 120 
GLN OXT    O  N N 121 
GLN H      H  N N 122 
GLN H2     H  N N 123 
GLN HA     H  N N 124 
GLN HB2    H  N N 125 
GLN HB3    H  N N 126 
GLN HG2    H  N N 127 
GLN HG3    H  N N 128 
GLN HE21   H  N N 129 
GLN HE22   H  N N 130 
GLN HXT    H  N N 131 
GLU N      N  N N 132 
GLU CA     C  N S 133 
GLU C      C  N N 134 
GLU O      O  N N 135 
GLU CB     C  N N 136 
GLU CG     C  N N 137 
GLU CD     C  N N 138 
GLU OE1    O  N N 139 
GLU OE2    O  N N 140 
GLU OXT    O  N N 141 
GLU H      H  N N 142 
GLU H2     H  N N 143 
GLU HA     H  N N 144 
GLU HB2    H  N N 145 
GLU HB3    H  N N 146 
GLU HG2    H  N N 147 
GLU HG3    H  N N 148 
GLU HE2    H  N N 149 
GLU HXT    H  N N 150 
GLY N      N  N N 151 
GLY CA     C  N N 152 
GLY C      C  N N 153 
GLY O      O  N N 154 
GLY OXT    O  N N 155 
GLY H      H  N N 156 
GLY H2     H  N N 157 
GLY HA2    H  N N 158 
GLY HA3    H  N N 159 
GLY HXT    H  N N 160 
HIS N      N  N N 161 
HIS CA     C  N S 162 
HIS C      C  N N 163 
HIS O      O  N N 164 
HIS CB     C  N N 165 
HIS CG     C  Y N 166 
HIS ND1    N  Y N 167 
HIS CD2    C  Y N 168 
HIS CE1    C  Y N 169 
HIS NE2    N  Y N 170 
HIS OXT    O  N N 171 
HIS H      H  N N 172 
HIS H2     H  N N 173 
HIS HA     H  N N 174 
HIS HB2    H  N N 175 
HIS HB3    H  N N 176 
HIS HD1    H  N N 177 
HIS HD2    H  N N 178 
HIS HE1    H  N N 179 
HIS HE2    H  N N 180 
HIS HXT    H  N N 181 
HOH O      O  N N 182 
HOH H1     H  N N 183 
HOH H2     H  N N 184 
ILE N      N  N N 185 
ILE CA     C  N S 186 
ILE C      C  N N 187 
ILE O      O  N N 188 
ILE CB     C  N S 189 
ILE CG1    C  N N 190 
ILE CG2    C  N N 191 
ILE CD1    C  N N 192 
ILE OXT    O  N N 193 
ILE H      H  N N 194 
ILE H2     H  N N 195 
ILE HA     H  N N 196 
ILE HB     H  N N 197 
ILE HG12   H  N N 198 
ILE HG13   H  N N 199 
ILE HG21   H  N N 200 
ILE HG22   H  N N 201 
ILE HG23   H  N N 202 
ILE HD11   H  N N 203 
ILE HD12   H  N N 204 
ILE HD13   H  N N 205 
ILE HXT    H  N N 206 
LEU N      N  N N 207 
LEU CA     C  N S 208 
LEU C      C  N N 209 
LEU O      O  N N 210 
LEU CB     C  N N 211 
LEU CG     C  N N 212 
LEU CD1    C  N N 213 
LEU CD2    C  N N 214 
LEU OXT    O  N N 215 
LEU H      H  N N 216 
LEU H2     H  N N 217 
LEU HA     H  N N 218 
LEU HB2    H  N N 219 
LEU HB3    H  N N 220 
LEU HG     H  N N 221 
LEU HD11   H  N N 222 
LEU HD12   H  N N 223 
LEU HD13   H  N N 224 
LEU HD21   H  N N 225 
LEU HD22   H  N N 226 
LEU HD23   H  N N 227 
LEU HXT    H  N N 228 
LYS N      N  N N 229 
LYS CA     C  N S 230 
LYS C      C  N N 231 
LYS O      O  N N 232 
LYS CB     C  N N 233 
LYS CG     C  N N 234 
LYS CD     C  N N 235 
LYS CE     C  N N 236 
LYS NZ     N  N N 237 
LYS OXT    O  N N 238 
LYS H      H  N N 239 
LYS H2     H  N N 240 
LYS HA     H  N N 241 
LYS HB2    H  N N 242 
LYS HB3    H  N N 243 
LYS HG2    H  N N 244 
LYS HG3    H  N N 245 
LYS HD2    H  N N 246 
LYS HD3    H  N N 247 
LYS HE2    H  N N 248 
LYS HE3    H  N N 249 
LYS HZ1    H  N N 250 
LYS HZ2    H  N N 251 
LYS HZ3    H  N N 252 
LYS HXT    H  N N 253 
MET N      N  N N 254 
MET CA     C  N S 255 
MET C      C  N N 256 
MET O      O  N N 257 
MET CB     C  N N 258 
MET CG     C  N N 259 
MET SD     S  N N 260 
MET CE     C  N N 261 
MET OXT    O  N N 262 
MET H      H  N N 263 
MET H2     H  N N 264 
MET HA     H  N N 265 
MET HB2    H  N N 266 
MET HB3    H  N N 267 
MET HG2    H  N N 268 
MET HG3    H  N N 269 
MET HE1    H  N N 270 
MET HE2    H  N N 271 
MET HE3    H  N N 272 
MET HXT    H  N N 273 
MG  MG     MG N N 274 
PHE N      N  N N 275 
PHE CA     C  N S 276 
PHE C      C  N N 277 
PHE O      O  N N 278 
PHE CB     C  N N 279 
PHE CG     C  Y N 280 
PHE CD1    C  Y N 281 
PHE CD2    C  Y N 282 
PHE CE1    C  Y N 283 
PHE CE2    C  Y N 284 
PHE CZ     C  Y N 285 
PHE OXT    O  N N 286 
PHE H      H  N N 287 
PHE H2     H  N N 288 
PHE HA     H  N N 289 
PHE HB2    H  N N 290 
PHE HB3    H  N N 291 
PHE HD1    H  N N 292 
PHE HD2    H  N N 293 
PHE HE1    H  N N 294 
PHE HE2    H  N N 295 
PHE HZ     H  N N 296 
PHE HXT    H  N N 297 
PRO N      N  N N 298 
PRO CA     C  N S 299 
PRO C      C  N N 300 
PRO O      O  N N 301 
PRO CB     C  N N 302 
PRO CG     C  N N 303 
PRO CD     C  N N 304 
PRO OXT    O  N N 305 
PRO H      H  N N 306 
PRO HA     H  N N 307 
PRO HB2    H  N N 308 
PRO HB3    H  N N 309 
PRO HG2    H  N N 310 
PRO HG3    H  N N 311 
PRO HD2    H  N N 312 
PRO HD3    H  N N 313 
PRO HXT    H  N N 314 
SER N      N  N N 315 
SER CA     C  N S 316 
SER C      C  N N 317 
SER O      O  N N 318 
SER CB     C  N N 319 
SER OG     O  N N 320 
SER OXT    O  N N 321 
SER H      H  N N 322 
SER H2     H  N N 323 
SER HA     H  N N 324 
SER HB2    H  N N 325 
SER HB3    H  N N 326 
SER HG     H  N N 327 
SER HXT    H  N N 328 
THR N      N  N N 329 
THR CA     C  N S 330 
THR C      C  N N 331 
THR O      O  N N 332 
THR CB     C  N R 333 
THR OG1    O  N N 334 
THR CG2    C  N N 335 
THR OXT    O  N N 336 
THR H      H  N N 337 
THR H2     H  N N 338 
THR HA     H  N N 339 
THR HB     H  N N 340 
THR HG1    H  N N 341 
THR HG21   H  N N 342 
THR HG22   H  N N 343 
THR HG23   H  N N 344 
THR HXT    H  N N 345 
TPP "N1'"  N  Y N 346 
TPP "C2'"  C  Y N 347 
TPP CM2    C  N N 348 
TPP "N3'"  N  Y N 349 
TPP "C4'"  C  Y N 350 
TPP "N4'"  N  N N 351 
TPP "C5'"  C  Y N 352 
TPP "C6'"  C  Y N 353 
TPP "C7'"  C  N N 354 
TPP N3     N  Y N 355 
TPP C2     C  Y N 356 
TPP S1     S  Y N 357 
TPP C5     C  Y N 358 
TPP C4     C  Y N 359 
TPP CM4    C  N N 360 
TPP C6     C  N N 361 
TPP C7     C  N N 362 
TPP O7     O  N N 363 
TPP PA     P  N S 364 
TPP O1A    O  N N 365 
TPP O2A    O  N N 366 
TPP O3A    O  N N 367 
TPP PB     P  N N 368 
TPP O1B    O  N N 369 
TPP O2B    O  N N 370 
TPP O3B    O  N N 371 
TPP HM21   H  N N 372 
TPP HM22   H  N N 373 
TPP HM23   H  N N 374 
TPP HN41   H  N N 375 
TPP HN42   H  N N 376 
TPP "H6'"  H  N N 377 
TPP "H7'1" H  N N 378 
TPP "H7'2" H  N N 379 
TPP H2     H  N N 380 
TPP HM41   H  N N 381 
TPP HM42   H  N N 382 
TPP HM43   H  N N 383 
TPP H61    H  N N 384 
TPP H62    H  N N 385 
TPP H71    H  N N 386 
TPP H72    H  N N 387 
TPP HOA2   H  N N 388 
TPP HOB2   H  N N 389 
TPP HOB3   H  N N 390 
TRP N      N  N N 391 
TRP CA     C  N S 392 
TRP C      C  N N 393 
TRP O      O  N N 394 
TRP CB     C  N N 395 
TRP CG     C  Y N 396 
TRP CD1    C  Y N 397 
TRP CD2    C  Y N 398 
TRP NE1    N  Y N 399 
TRP CE2    C  Y N 400 
TRP CE3    C  Y N 401 
TRP CZ2    C  Y N 402 
TRP CZ3    C  Y N 403 
TRP CH2    C  Y N 404 
TRP OXT    O  N N 405 
TRP H      H  N N 406 
TRP H2     H  N N 407 
TRP HA     H  N N 408 
TRP HB2    H  N N 409 
TRP HB3    H  N N 410 
TRP HD1    H  N N 411 
TRP HE1    H  N N 412 
TRP HE3    H  N N 413 
TRP HZ2    H  N N 414 
TRP HZ3    H  N N 415 
TRP HH2    H  N N 416 
TRP HXT    H  N N 417 
TYR N      N  N N 418 
TYR CA     C  N S 419 
TYR C      C  N N 420 
TYR O      O  N N 421 
TYR CB     C  N N 422 
TYR CG     C  Y N 423 
TYR CD1    C  Y N 424 
TYR CD2    C  Y N 425 
TYR CE1    C  Y N 426 
TYR CE2    C  Y N 427 
TYR CZ     C  Y N 428 
TYR OH     O  N N 429 
TYR OXT    O  N N 430 
TYR H      H  N N 431 
TYR H2     H  N N 432 
TYR HA     H  N N 433 
TYR HB2    H  N N 434 
TYR HB3    H  N N 435 
TYR HD1    H  N N 436 
TYR HD2    H  N N 437 
TYR HE1    H  N N 438 
TYR HE2    H  N N 439 
TYR HH     H  N N 440 
TYR HXT    H  N N 441 
VAL N      N  N N 442 
VAL CA     C  N S 443 
VAL C      C  N N 444 
VAL O      O  N N 445 
VAL CB     C  N N 446 
VAL CG1    C  N N 447 
VAL CG2    C  N N 448 
VAL OXT    O  N N 449 
VAL H      H  N N 450 
VAL H2     H  N N 451 
VAL HA     H  N N 452 
VAL HB     H  N N 453 
VAL HG11   H  N N 454 
VAL HG12   H  N N 455 
VAL HG13   H  N N 456 
VAL HG21   H  N N 457 
VAL HG22   H  N N 458 
VAL HG23   H  N N 459 
VAL HXT    H  N N 460 
# 
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 
3IO CAO   CAG    sing Y N 1   
3IO CAO   CAN    doub Y N 2   
3IO CAO   CAM    sing Y N 3   
3IO CAG   CAE    doub Y N 4   
3IO CAG   HAG    sing N N 5   
3IO CAE   CAD    sing Y N 6   
3IO CAE   HAE    sing N N 7   
3IO CAD   CAF    doub Y N 8   
3IO CAD   HAD    sing N N 9   
3IO CAF   CAN    sing Y N 10  
3IO CAF   HAF    sing N N 11  
3IO CAN   NAJ    sing Y N 12  
3IO NAJ   CAH    sing Y N 13  
3IO NAJ   HNAJ   sing N N 14  
3IO CAH   CAM    doub Y N 15  
3IO CAH   HAH    sing N N 16  
3IO CAM   CAI    sing N N 17  
3IO CAI   CAL    sing N N 18  
3IO CAI   HAI1   sing N N 19  
3IO CAI   HAI2   sing N N 20  
3IO CAL   OAB    doub N N 21  
3IO CAL   CAK    sing N N 22  
3IO CAK   OAC    sing N N 23  
3IO CAK   OAA    doub N N 24  
3IO OAC   HOAC   sing N N 25  
ALA N     CA     sing N N 26  
ALA N     H      sing N N 27  
ALA N     H2     sing N N 28  
ALA CA    C      sing N N 29  
ALA CA    CB     sing N N 30  
ALA CA    HA     sing N N 31  
ALA C     O      doub N N 32  
ALA C     OXT    sing N N 33  
ALA CB    HB1    sing N N 34  
ALA CB    HB2    sing N N 35  
ALA CB    HB3    sing N N 36  
ALA OXT   HXT    sing N N 37  
ARG N     CA     sing N N 38  
ARG N     H      sing N N 39  
ARG N     H2     sing N N 40  
ARG CA    C      sing N N 41  
ARG CA    CB     sing N N 42  
ARG CA    HA     sing N N 43  
ARG C     O      doub N N 44  
ARG C     OXT    sing N N 45  
ARG CB    CG     sing N N 46  
ARG CB    HB2    sing N N 47  
ARG CB    HB3    sing N N 48  
ARG CG    CD     sing N N 49  
ARG CG    HG2    sing N N 50  
ARG CG    HG3    sing N N 51  
ARG CD    NE     sing N N 52  
ARG CD    HD2    sing N N 53  
ARG CD    HD3    sing N N 54  
ARG NE    CZ     sing N N 55  
ARG NE    HE     sing N N 56  
ARG CZ    NH1    sing N N 57  
ARG CZ    NH2    doub N N 58  
ARG NH1   HH11   sing N N 59  
ARG NH1   HH12   sing N N 60  
ARG NH2   HH21   sing N N 61  
ARG NH2   HH22   sing N N 62  
ARG OXT   HXT    sing N N 63  
ASN N     CA     sing N N 64  
ASN N     H      sing N N 65  
ASN N     H2     sing N N 66  
ASN CA    C      sing N N 67  
ASN CA    CB     sing N N 68  
ASN CA    HA     sing N N 69  
ASN C     O      doub N N 70  
ASN C     OXT    sing N N 71  
ASN CB    CG     sing N N 72  
ASN CB    HB2    sing N N 73  
ASN CB    HB3    sing N N 74  
ASN CG    OD1    doub N N 75  
ASN CG    ND2    sing N N 76  
ASN ND2   HD21   sing N N 77  
ASN ND2   HD22   sing N N 78  
ASN OXT   HXT    sing N N 79  
ASP N     CA     sing N N 80  
ASP N     H      sing N N 81  
ASP N     H2     sing N N 82  
ASP CA    C      sing N N 83  
ASP CA    CB     sing N N 84  
ASP CA    HA     sing N N 85  
ASP C     O      doub N N 86  
ASP C     OXT    sing N N 87  
ASP CB    CG     sing N N 88  
ASP CB    HB2    sing N N 89  
ASP CB    HB3    sing N N 90  
ASP CG    OD1    doub N N 91  
ASP CG    OD2    sing N N 92  
ASP OD2   HD2    sing N N 93  
ASP OXT   HXT    sing N N 94  
CYS N     CA     sing N N 95  
CYS N     H      sing N N 96  
CYS N     H2     sing N N 97  
CYS CA    C      sing N N 98  
CYS CA    CB     sing N N 99  
CYS CA    HA     sing N N 100 
CYS C     O      doub N N 101 
CYS C     OXT    sing N N 102 
CYS CB    SG     sing N N 103 
CYS CB    HB2    sing N N 104 
CYS CB    HB3    sing N N 105 
CYS SG    HG     sing N N 106 
CYS OXT   HXT    sing N N 107 
GLN N     CA     sing N N 108 
GLN N     H      sing N N 109 
GLN N     H2     sing N N 110 
GLN CA    C      sing N N 111 
GLN CA    CB     sing N N 112 
GLN CA    HA     sing N N 113 
GLN C     O      doub N N 114 
GLN C     OXT    sing N N 115 
GLN CB    CG     sing N N 116 
GLN CB    HB2    sing N N 117 
GLN CB    HB3    sing N N 118 
GLN CG    CD     sing N N 119 
GLN CG    HG2    sing N N 120 
GLN CG    HG3    sing N N 121 
GLN CD    OE1    doub N N 122 
GLN CD    NE2    sing N N 123 
GLN NE2   HE21   sing N N 124 
GLN NE2   HE22   sing N N 125 
GLN OXT   HXT    sing N N 126 
GLU N     CA     sing N N 127 
GLU N     H      sing N N 128 
GLU N     H2     sing N N 129 
GLU CA    C      sing N N 130 
GLU CA    CB     sing N N 131 
GLU CA    HA     sing N N 132 
GLU C     O      doub N N 133 
GLU C     OXT    sing N N 134 
GLU CB    CG     sing N N 135 
GLU CB    HB2    sing N N 136 
GLU CB    HB3    sing N N 137 
GLU CG    CD     sing N N 138 
GLU CG    HG2    sing N N 139 
GLU CG    HG3    sing N N 140 
GLU CD    OE1    doub N N 141 
GLU CD    OE2    sing N N 142 
GLU OE2   HE2    sing N N 143 
GLU OXT   HXT    sing N N 144 
GLY N     CA     sing N N 145 
GLY N     H      sing N N 146 
GLY N     H2     sing N N 147 
GLY CA    C      sing N N 148 
GLY CA    HA2    sing N N 149 
GLY CA    HA3    sing N N 150 
GLY C     O      doub N N 151 
GLY C     OXT    sing N N 152 
GLY OXT   HXT    sing N N 153 
HIS N     CA     sing N N 154 
HIS N     H      sing N N 155 
HIS N     H2     sing N N 156 
HIS CA    C      sing N N 157 
HIS CA    CB     sing N N 158 
HIS CA    HA     sing N N 159 
HIS C     O      doub N N 160 
HIS C     OXT    sing N N 161 
HIS CB    CG     sing N N 162 
HIS CB    HB2    sing N N 163 
HIS CB    HB3    sing N N 164 
HIS CG    ND1    sing Y N 165 
HIS CG    CD2    doub Y N 166 
HIS ND1   CE1    doub Y N 167 
HIS ND1   HD1    sing N N 168 
HIS CD2   NE2    sing Y N 169 
HIS CD2   HD2    sing N N 170 
HIS CE1   NE2    sing Y N 171 
HIS CE1   HE1    sing N N 172 
HIS NE2   HE2    sing N N 173 
HIS OXT   HXT    sing N N 174 
HOH O     H1     sing N N 175 
HOH O     H2     sing N N 176 
ILE N     CA     sing N N 177 
ILE N     H      sing N N 178 
ILE N     H2     sing N N 179 
ILE CA    C      sing N N 180 
ILE CA    CB     sing N N 181 
ILE CA    HA     sing N N 182 
ILE C     O      doub N N 183 
ILE C     OXT    sing N N 184 
ILE CB    CG1    sing N N 185 
ILE CB    CG2    sing N N 186 
ILE CB    HB     sing N N 187 
ILE CG1   CD1    sing N N 188 
ILE CG1   HG12   sing N N 189 
ILE CG1   HG13   sing N N 190 
ILE CG2   HG21   sing N N 191 
ILE CG2   HG22   sing N N 192 
ILE CG2   HG23   sing N N 193 
ILE CD1   HD11   sing N N 194 
ILE CD1   HD12   sing N N 195 
ILE CD1   HD13   sing N N 196 
ILE OXT   HXT    sing N N 197 
LEU N     CA     sing N N 198 
LEU N     H      sing N N 199 
LEU N     H2     sing N N 200 
LEU CA    C      sing N N 201 
LEU CA    CB     sing N N 202 
LEU CA    HA     sing N N 203 
LEU C     O      doub N N 204 
LEU C     OXT    sing N N 205 
LEU CB    CG     sing N N 206 
LEU CB    HB2    sing N N 207 
LEU CB    HB3    sing N N 208 
LEU CG    CD1    sing N N 209 
LEU CG    CD2    sing N N 210 
LEU CG    HG     sing N N 211 
LEU CD1   HD11   sing N N 212 
LEU CD1   HD12   sing N N 213 
LEU CD1   HD13   sing N N 214 
LEU CD2   HD21   sing N N 215 
LEU CD2   HD22   sing N N 216 
LEU CD2   HD23   sing N N 217 
LEU OXT   HXT    sing N N 218 
LYS N     CA     sing N N 219 
LYS N     H      sing N N 220 
LYS N     H2     sing N N 221 
LYS CA    C      sing N N 222 
LYS CA    CB     sing N N 223 
LYS CA    HA     sing N N 224 
LYS C     O      doub N N 225 
LYS C     OXT    sing N N 226 
LYS CB    CG     sing N N 227 
LYS CB    HB2    sing N N 228 
LYS CB    HB3    sing N N 229 
LYS CG    CD     sing N N 230 
LYS CG    HG2    sing N N 231 
LYS CG    HG3    sing N N 232 
LYS CD    CE     sing N N 233 
LYS CD    HD2    sing N N 234 
LYS CD    HD3    sing N N 235 
LYS CE    NZ     sing N N 236 
LYS CE    HE2    sing N N 237 
LYS CE    HE3    sing N N 238 
LYS NZ    HZ1    sing N N 239 
LYS NZ    HZ2    sing N N 240 
LYS NZ    HZ3    sing N N 241 
LYS OXT   HXT    sing N N 242 
MET N     CA     sing N N 243 
MET N     H      sing N N 244 
MET N     H2     sing N N 245 
MET CA    C      sing N N 246 
MET CA    CB     sing N N 247 
MET CA    HA     sing N N 248 
MET C     O      doub N N 249 
MET C     OXT    sing N N 250 
MET CB    CG     sing N N 251 
MET CB    HB2    sing N N 252 
MET CB    HB3    sing N N 253 
MET CG    SD     sing N N 254 
MET CG    HG2    sing N N 255 
MET CG    HG3    sing N N 256 
MET SD    CE     sing N N 257 
MET CE    HE1    sing N N 258 
MET CE    HE2    sing N N 259 
MET CE    HE3    sing N N 260 
MET OXT   HXT    sing N N 261 
PHE N     CA     sing N N 262 
PHE N     H      sing N N 263 
PHE N     H2     sing N N 264 
PHE CA    C      sing N N 265 
PHE CA    CB     sing N N 266 
PHE CA    HA     sing N N 267 
PHE C     O      doub N N 268 
PHE C     OXT    sing N N 269 
PHE CB    CG     sing N N 270 
PHE CB    HB2    sing N N 271 
PHE CB    HB3    sing N N 272 
PHE CG    CD1    doub Y N 273 
PHE CG    CD2    sing Y N 274 
PHE CD1   CE1    sing Y N 275 
PHE CD1   HD1    sing N N 276 
PHE CD2   CE2    doub Y N 277 
PHE CD2   HD2    sing N N 278 
PHE CE1   CZ     doub Y N 279 
PHE CE1   HE1    sing N N 280 
PHE CE2   CZ     sing Y N 281 
PHE CE2   HE2    sing N N 282 
PHE CZ    HZ     sing N N 283 
PHE OXT   HXT    sing N N 284 
PRO N     CA     sing N N 285 
PRO N     CD     sing N N 286 
PRO N     H      sing N N 287 
PRO CA    C      sing N N 288 
PRO CA    CB     sing N N 289 
PRO CA    HA     sing N N 290 
PRO C     O      doub N N 291 
PRO C     OXT    sing N N 292 
PRO CB    CG     sing N N 293 
PRO CB    HB2    sing N N 294 
PRO CB    HB3    sing N N 295 
PRO CG    CD     sing N N 296 
PRO CG    HG2    sing N N 297 
PRO CG    HG3    sing N N 298 
PRO CD    HD2    sing N N 299 
PRO CD    HD3    sing N N 300 
PRO OXT   HXT    sing N N 301 
SER N     CA     sing N N 302 
SER N     H      sing N N 303 
SER N     H2     sing N N 304 
SER CA    C      sing N N 305 
SER CA    CB     sing N N 306 
SER CA    HA     sing N N 307 
SER C     O      doub N N 308 
SER C     OXT    sing N N 309 
SER CB    OG     sing N N 310 
SER CB    HB2    sing N N 311 
SER CB    HB3    sing N N 312 
SER OG    HG     sing N N 313 
SER OXT   HXT    sing N N 314 
THR N     CA     sing N N 315 
THR N     H      sing N N 316 
THR N     H2     sing N N 317 
THR CA    C      sing N N 318 
THR CA    CB     sing N N 319 
THR CA    HA     sing N N 320 
THR C     O      doub N N 321 
THR C     OXT    sing N N 322 
THR CB    OG1    sing N N 323 
THR CB    CG2    sing N N 324 
THR CB    HB     sing N N 325 
THR OG1   HG1    sing N N 326 
THR CG2   HG21   sing N N 327 
THR CG2   HG22   sing N N 328 
THR CG2   HG23   sing N N 329 
THR OXT   HXT    sing N N 330 
TPP "N1'" "C2'"  doub Y N 331 
TPP "N1'" "C6'"  sing Y N 332 
TPP "C2'" CM2    sing N N 333 
TPP "C2'" "N3'"  sing Y N 334 
TPP CM2   HM21   sing N N 335 
TPP CM2   HM22   sing N N 336 
TPP CM2   HM23   sing N N 337 
TPP "N3'" "C4'"  doub Y N 338 
TPP "C4'" "N4'"  sing N N 339 
TPP "C4'" "C5'"  sing Y N 340 
TPP "N4'" HN41   sing N N 341 
TPP "N4'" HN42   sing N N 342 
TPP "C5'" "C6'"  doub Y N 343 
TPP "C5'" "C7'"  sing N N 344 
TPP "C6'" "H6'"  sing N N 345 
TPP "C7'" N3     sing N N 346 
TPP "C7'" "H7'1" sing N N 347 
TPP "C7'" "H7'2" sing N N 348 
TPP N3    C2     doub Y N 349 
TPP N3    C4     sing Y N 350 
TPP C2    S1     sing Y N 351 
TPP C2    H2     sing N N 352 
TPP S1    C5     sing Y N 353 
TPP C5    C4     doub Y N 354 
TPP C5    C6     sing N N 355 
TPP C4    CM4    sing N N 356 
TPP CM4   HM41   sing N N 357 
TPP CM4   HM42   sing N N 358 
TPP CM4   HM43   sing N N 359 
TPP C6    C7     sing N N 360 
TPP C6    H61    sing N N 361 
TPP C6    H62    sing N N 362 
TPP C7    O7     sing N N 363 
TPP C7    H71    sing N N 364 
TPP C7    H72    sing N N 365 
TPP O7    PA     sing N N 366 
TPP PA    O1A    doub N N 367 
TPP PA    O2A    sing N N 368 
TPP PA    O3A    sing N N 369 
TPP O2A   HOA2   sing N N 370 
TPP O3A   PB     sing N N 371 
TPP PB    O1B    doub N N 372 
TPP PB    O2B    sing N N 373 
TPP PB    O3B    sing N N 374 
TPP O2B   HOB2   sing N N 375 
TPP O3B   HOB3   sing N N 376 
TRP N     CA     sing N N 377 
TRP N     H      sing N N 378 
TRP N     H2     sing N N 379 
TRP CA    C      sing N N 380 
TRP CA    CB     sing N N 381 
TRP CA    HA     sing N N 382 
TRP C     O      doub N N 383 
TRP C     OXT    sing N N 384 
TRP CB    CG     sing N N 385 
TRP CB    HB2    sing N N 386 
TRP CB    HB3    sing N N 387 
TRP CG    CD1    doub Y N 388 
TRP CG    CD2    sing Y N 389 
TRP CD1   NE1    sing Y N 390 
TRP CD1   HD1    sing N N 391 
TRP CD2   CE2    doub Y N 392 
TRP CD2   CE3    sing Y N 393 
TRP NE1   CE2    sing Y N 394 
TRP NE1   HE1    sing N N 395 
TRP CE2   CZ2    sing Y N 396 
TRP CE3   CZ3    doub Y N 397 
TRP CE3   HE3    sing N N 398 
TRP CZ2   CH2    doub Y N 399 
TRP CZ2   HZ2    sing N N 400 
TRP CZ3   CH2    sing Y N 401 
TRP CZ3   HZ3    sing N N 402 
TRP CH2   HH2    sing N N 403 
TRP OXT   HXT    sing N N 404 
TYR N     CA     sing N N 405 
TYR N     H      sing N N 406 
TYR N     H2     sing N N 407 
TYR CA    C      sing N N 408 
TYR CA    CB     sing N N 409 
TYR CA    HA     sing N N 410 
TYR C     O      doub N N 411 
TYR C     OXT    sing N N 412 
TYR CB    CG     sing N N 413 
TYR CB    HB2    sing N N 414 
TYR CB    HB3    sing N N 415 
TYR CG    CD1    doub Y N 416 
TYR CG    CD2    sing Y N 417 
TYR CD1   CE1    sing Y N 418 
TYR CD1   HD1    sing N N 419 
TYR CD2   CE2    doub Y N 420 
TYR CD2   HD2    sing N N 421 
TYR CE1   CZ     doub Y N 422 
TYR CE1   HE1    sing N N 423 
TYR CE2   CZ     sing Y N 424 
TYR CE2   HE2    sing N N 425 
TYR CZ    OH     sing N N 426 
TYR OH    HH     sing N N 427 
TYR OXT   HXT    sing N N 428 
VAL N     CA     sing N N 429 
VAL N     H      sing N N 430 
VAL N     H2     sing N N 431 
VAL CA    C      sing N N 432 
VAL CA    CB     sing N N 433 
VAL CA    HA     sing N N 434 
VAL C     O      doub N N 435 
VAL C     OXT    sing N N 436 
VAL CB    CG1    sing N N 437 
VAL CB    CG2    sing N N 438 
VAL CB    HB     sing N N 439 
VAL CG1   HG11   sing N N 440 
VAL CG1   HG12   sing N N 441 
VAL CG1   HG13   sing N N 442 
VAL CG2   HG21   sing N N 443 
VAL CG2   HG22   sing N N 444 
VAL CG2   HG23   sing N N 445 
VAL OXT   HXT    sing N N 446 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32171203 
_pdbx_audit_support.ordinal                1 
# 
_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   1ovm 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZK8 
_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]   0.008556 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007307 
_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]   0.012942 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . THR A 1 17  ? 30.535  2.524   39.577  1.00 88.95  ?  3   THR A N     1 
ATOM   2    C  CA    . THR A 1 17  ? 30.364  2.452   38.129  1.00 83.63  ?  3   THR A CA    1 
ATOM   3    C  C     . THR A 1 17  ? 30.377  1.014   37.600  1.00 78.40  ?  3   THR A C     1 
ATOM   4    O  O     . THR A 1 17  ? 31.226  0.668   36.775  1.00 84.75  ?  3   THR A O     1 
ATOM   5    C  CB    . THR A 1 17  ? 31.468  3.248   37.404  1.00 85.55  ?  3   THR A CB    1 
ATOM   6    O  OG1   . THR A 1 17  ? 32.752  2.727   37.773  1.00 80.55  ?  3   THR A OG1   1 
ATOM   7    C  CG2   . THR A 1 17  ? 31.399  4.721   37.777  1.00 91.45  ?  3   THR A CG2   1 
ATOM   8    N  N     . PRO A 1 18  ? 29.458  0.171   38.072  1.00 64.36  ?  4   PRO A N     1 
ATOM   9    C  CA    . PRO A 1 18  ? 29.412  -1.206  37.571  1.00 63.42  ?  4   PRO A CA    1 
ATOM   10   C  C     . PRO A 1 18  ? 29.019  -1.258  36.102  1.00 53.79  ?  4   PRO A C     1 
ATOM   11   O  O     . PRO A 1 18  ? 28.225  -0.449  35.617  1.00 62.02  ?  4   PRO A O     1 
ATOM   12   C  CB    . PRO A 1 18  ? 28.349  -1.876  38.454  1.00 57.62  ?  4   PRO A CB    1 
ATOM   13   C  CG    . PRO A 1 18  ? 28.086  -0.909  39.578  1.00 61.05  ?  4   PRO A CG    1 
ATOM   14   C  CD    . PRO A 1 18  ? 28.355  0.440   39.008  1.00 64.93  ?  4   PRO A CD    1 
ATOM   15   N  N     . TYR A 1 19  ? 29.587  -2.236  35.396  1.00 49.80  ?  5   TYR A N     1 
ATOM   16   C  CA    . TYR A 1 19  ? 29.251  -2.448  33.994  1.00 46.41  ?  5   TYR A CA    1 
ATOM   17   C  C     . TYR A 1 19  ? 27.760  -2.718  33.848  1.00 49.85  ?  5   TYR A C     1 
ATOM   18   O  O     . TYR A 1 19  ? 27.195  -3.546  34.569  1.00 42.27  ?  5   TYR A O     1 
ATOM   19   C  CB    . TYR A 1 19  ? 30.060  -3.613  33.429  1.00 41.14  ?  5   TYR A CB    1 
ATOM   20   C  CG    . TYR A 1 19  ? 30.100  -3.668  31.919  1.00 44.03  ?  5   TYR A CG    1 
ATOM   21   C  CD1   . TYR A 1 19  ? 29.114  -4.340  31.202  1.00 41.82  ?  5   TYR A CD1   1 
ATOM   22   C  CD2   . TYR A 1 19  ? 31.132  -3.063  31.209  1.00 40.65  ?  5   TYR A CD2   1 
ATOM   23   C  CE1   . TYR A 1 19  ? 29.151  -4.402  29.822  1.00 39.30  ?  5   TYR A CE1   1 
ATOM   24   C  CE2   . TYR A 1 19  ? 31.177  -3.119  29.828  1.00 36.39  ?  5   TYR A CE2   1 
ATOM   25   C  CZ    . TYR A 1 19  ? 30.184  -3.790  29.141  1.00 35.91  ?  5   TYR A CZ    1 
ATOM   26   O  OH    . TYR A 1 19  ? 30.223  -3.854  27.770  1.00 41.21  ?  5   TYR A OH    1 
ATOM   27   N  N     . CYS A 1 20  ? 27.123  -2.018  32.912  1.00 40.37  ?  6   CYS A N     1 
ATOM   28   C  CA    . CYS A 1 20  ? 25.676  -2.053  32.782  1.00 44.68  ?  6   CYS A CA    1 
ATOM   29   C  C     . CYS A 1 20  ? 25.290  -2.035  31.306  1.00 40.19  ?  6   CYS A C     1 
ATOM   30   O  O     . CYS A 1 20  ? 26.144  -2.028  30.415  1.00 40.05  ?  6   CYS A O     1 
ATOM   31   C  CB    . CYS A 1 20  ? 25.039  -0.883  33.536  1.00 43.06  ?  6   CYS A CB    1 
ATOM   32   S  SG    . CYS A 1 20  ? 25.522  0.713   32.896  1.00 46.11  ?  6   CYS A SG    1 
ATOM   33   N  N     . VAL A 1 21  ? 23.976  -2.019  31.059  1.00 33.99  ?  7   VAL A N     1 
ATOM   34   C  CA    . VAL A 1 21  ? 23.450  -2.069  29.696  1.00 36.72  ?  7   VAL A CA    1 
ATOM   35   C  C     . VAL A 1 21  ? 23.956  -0.885  28.876  1.00 40.28  ?  7   VAL A C     1 
ATOM   36   O  O     . VAL A 1 21  ? 24.276  -1.023  27.689  1.00 34.67  ?  7   VAL A O     1 
ATOM   37   C  CB    . VAL A 1 21  ? 21.909  -2.131  29.734  1.00 33.94  ?  7   VAL A CB    1 
ATOM   38   C  CG1   . VAL A 1 21  ? 21.301  -1.727  28.397  1.00 28.75  ?  7   VAL A CG1   1 
ATOM   39   C  CG2   . VAL A 1 21  ? 21.455  -3.530  30.134  1.00 30.95  ?  7   VAL A CG2   1 
ATOM   40   N  N     . ALA A 1 22  ? 24.033  0.297   29.494  1.00 35.58  ?  8   ALA A N     1 
ATOM   41   C  CA    . ALA A 1 22  ? 24.583  1.460   28.806  1.00 39.39  ?  8   ALA A CA    1 
ATOM   42   C  C     . ALA A 1 22  ? 25.995  1.183   28.297  1.00 41.34  ?  8   ALA A C     1 
ATOM   43   O  O     . ALA A 1 22  ? 26.326  1.491   27.146  1.00 36.21  ?  8   ALA A O     1 
ATOM   44   C  CB    . ALA A 1 22  ? 24.574  2.664   29.746  1.00 31.74  ?  8   ALA A CB    1 
ATOM   45   N  N     . ASP A 1 23  ? 26.840  0.580   29.139  1.00 37.82  ?  9   ASP A N     1 
ATOM   46   C  CA    . ASP A 1 23  ? 28.200  0.254   28.719  1.00 36.50  ?  9   ASP A CA    1 
ATOM   47   C  C     . ASP A 1 23  ? 28.208  -0.827  27.646  1.00 40.99  ?  9   ASP A C     1 
ATOM   48   O  O     . ASP A 1 23  ? 29.041  -0.796  26.731  1.00 33.39  ?  9   ASP A O     1 
ATOM   49   C  CB    . ASP A 1 23  ? 29.031  -0.191  29.921  1.00 35.94  ?  9   ASP A CB    1 
ATOM   50   C  CG    . ASP A 1 23  ? 29.104  0.865   30.994  1.00 46.14  ?  9   ASP A CG    1 
ATOM   51   O  OD1   . ASP A 1 23  ? 29.479  2.015   30.669  1.00 42.42  ?  9   ASP A OD1   1 
ATOM   52   O  OD2   . ASP A 1 23  ? 28.789  0.546   32.160  1.00 44.69  ?  9   ASP A OD2   1 
ATOM   53   N  N     . TYR A 1 24  ? 27.299  -1.802  27.754  1.00 31.48  ?  10  TYR A N     1 
ATOM   54   C  CA    . TYR A 1 24  ? 27.225  -2.865  26.758  1.00 36.07  ?  10  TYR A CA    1 
ATOM   55   C  C     . TYR A 1 24  ? 26.900  -2.304  25.382  1.00 34.45  ?  10  TYR A C     1 
ATOM   56   O  O     . TYR A 1 24  ? 27.523  -2.685  24.384  1.00 35.33  ?  10  TYR A O     1 
ATOM   57   C  CB    . TYR A 1 24  ? 26.177  -3.900  27.176  1.00 35.28  ?  10  TYR A CB    1 
ATOM   58   C  CG    . TYR A 1 24  ? 26.128  -5.126  26.297  1.00 39.28  ?  10  TYR A CG    1 
ATOM   59   C  CD1   . TYR A 1 24  ? 25.361  -5.150  25.138  1.00 40.02  ?  10  TYR A CD1   1 
ATOM   60   C  CD2   . TYR A 1 24  ? 26.841  -6.269  26.632  1.00 40.83  ?  10  TYR A CD2   1 
ATOM   61   C  CE1   . TYR A 1 24  ? 25.312  -6.279  24.334  1.00 34.97  ?  10  TYR A CE1   1 
ATOM   62   C  CE2   . TYR A 1 24  ? 26.797  -7.399  25.836  1.00 42.61  ?  10  TYR A CE2   1 
ATOM   63   C  CZ    . TYR A 1 24  ? 26.033  -7.398  24.690  1.00 40.62  ?  10  TYR A CZ    1 
ATOM   64   O  OH    . TYR A 1 24  ? 25.994  -8.523  23.898  1.00 38.50  ?  10  TYR A OH    1 
ATOM   65   N  N     . LEU A 1 25  ? 25.928  -1.392  25.314  1.00 28.99  ?  11  LEU A N     1 
ATOM   66   C  CA    . LEU A 1 25  ? 25.571  -0.777  24.041  1.00 34.44  ?  11  LEU A CA    1 
ATOM   67   C  C     . LEU A 1 25  ? 26.749  -0.011  23.457  1.00 34.62  ?  11  LEU A C     1 
ATOM   68   O  O     . LEU A 1 25  ? 27.015  -0.086  22.252  1.00 33.62  ?  11  LEU A O     1 
ATOM   69   C  CB    . LEU A 1 25  ? 24.363  0.144   24.231  1.00 31.51  ?  11  LEU A CB    1 
ATOM   70   C  CG    . LEU A 1 25  ? 23.896  1.000   23.051  1.00 40.45  ?  11  LEU A CG    1 
ATOM   71   C  CD1   . LEU A 1 25  ? 23.713  0.162   21.795  1.00 28.83  ?  11  LEU A CD1   1 
ATOM   72   C  CD2   . LEU A 1 25  ? 22.597  1.724   23.398  1.00 30.60  ?  11  LEU A CD2   1 
ATOM   73   N  N     . LEU A 1 26  ? 27.471  0.731   24.298  1.00 34.11  ?  12  LEU A N     1 
ATOM   74   C  CA    . LEU A 1 26  ? 28.625  1.473   23.804  1.00 36.72  ?  12  LEU A CA    1 
ATOM   75   C  C     . LEU A 1 26  ? 29.711  0.527   23.308  1.00 37.89  ?  12  LEU A C     1 
ATOM   76   O  O     . LEU A 1 26  ? 30.319  0.771   22.260  1.00 36.46  ?  12  LEU A O     1 
ATOM   77   C  CB    . LEU A 1 26  ? 29.159  2.397   24.896  1.00 33.12  ?  12  LEU A CB    1 
ATOM   78   C  CG    . LEU A 1 26  ? 28.189  3.534   25.224  1.00 37.06  ?  12  LEU A CG    1 
ATOM   79   C  CD1   . LEU A 1 26  ? 28.689  4.333   26.413  1.00 34.02  ?  12  LEU A CD1   1 
ATOM   80   C  CD2   . LEU A 1 26  ? 27.964  4.428   24.009  1.00 28.22  ?  12  LEU A CD2   1 
ATOM   81   N  N     . ASP A 1 27  ? 29.945  -0.576  24.028  1.00 31.75  ?  13  ASP A N     1 
ATOM   82   C  CA    . ASP A 1 27  ? 30.924  -1.558  23.567  1.00 39.92  ?  13  ASP A CA    1 
ATOM   83   C  C     . ASP A 1 27  ? 30.534  -2.119  22.206  1.00 36.38  ?  13  ASP A C     1 
ATOM   84   O  O     . ASP A 1 27  ? 31.374  -2.228  21.305  1.00 37.63  ?  13  ASP A O     1 
ATOM   85   C  CB    . ASP A 1 27  ? 31.063  -2.687  24.588  1.00 40.72  ?  13  ASP A CB    1 
ATOM   86   C  CG    . ASP A 1 27  ? 32.136  -2.411  25.621  1.00 43.85  ?  13  ASP A CG    1 
ATOM   87   O  OD1   . ASP A 1 27  ? 33.017  -1.565  25.357  1.00 53.07  ?  13  ASP A OD1   1 
ATOM   88   O  OD2   . ASP A 1 27  ? 32.095  -3.042  26.701  1.00 41.40  ?  13  ASP A OD2   1 
ATOM   89   N  N     . ARG A 1 28  ? 29.255  -2.458  22.030  1.00 33.50  ?  14  ARG A N     1 
ATOM   90   C  CA    . ARG A 1 28  ? 28.788  -2.947  20.739  1.00 37.54  ?  14  ARG A CA    1 
ATOM   91   C  C     . ARG A 1 28  ? 28.900  -1.873  19.668  1.00 34.13  ?  14  ARG A C     1 
ATOM   92   O  O     . ARG A 1 28  ? 29.156  -2.183  18.499  1.00 37.17  ?  14  ARG A O     1 
ATOM   93   C  CB    . ARG A 1 28  ? 27.345  -3.442  20.864  1.00 33.57  ?  14  ARG A CB    1 
ATOM   94   C  CG    . ARG A 1 28  ? 27.199  -4.700  21.705  1.00 30.20  ?  14  ARG A CG    1 
ATOM   95   C  CD    . ARG A 1 28  ? 28.271  -5.709  21.337  1.00 37.68  ?  14  ARG A CD    1 
ATOM   96   N  NE    . ARG A 1 28  ? 27.818  -7.084  21.500  1.00 42.59  ?  14  ARG A NE    1 
ATOM   97   C  CZ    . ARG A 1 28  ? 28.621  -8.136  21.556  1.00 43.03  ?  14  ARG A CZ    1 
ATOM   98   N  NH1   . ARG A 1 28  ? 29.934  -8.008  21.457  1.00 54.17  ?  14  ARG A NH1   1 
ATOM   99   N  NH2   . ARG A 1 28  ? 28.095  -9.346  21.715  1.00 44.75  ?  14  ARG A NH2   1 
ATOM   100  N  N     . LEU A 1 29  ? 28.713  -0.608  20.055  1.00 36.69  ?  15  LEU A N     1 
ATOM   101  C  CA    . LEU A 1 29  ? 28.823  0.505   19.118  1.00 33.18  ?  15  LEU A CA    1 
ATOM   102  C  C     . LEU A 1 29  ? 30.216  0.585   18.497  1.00 43.21  ?  15  LEU A C     1 
ATOM   103  O  O     . LEU A 1 29  ? 30.357  0.772   17.282  1.00 38.63  ?  15  LEU A O     1 
ATOM   104  C  CB    . LEU A 1 29  ? 28.496  1.807   19.847  1.00 43.26  ?  15  LEU A CB    1 
ATOM   105  C  CG    . LEU A 1 29  ? 28.044  3.006   19.026  1.00 51.43  ?  15  LEU A CG    1 
ATOM   106  C  CD1   . LEU A 1 29  ? 27.292  2.528   17.797  1.00 61.45  ?  15  LEU A CD1   1 
ATOM   107  C  CD2   . LEU A 1 29  ? 27.189  3.936   19.884  1.00 45.64  ?  15  LEU A CD2   1 
ATOM   108  N  N     . THR A 1 30  ? 31.262  0.473   19.320  1.00 38.32  ?  16  THR A N     1 
ATOM   109  C  CA    . THR A 1 30  ? 32.616  0.518   18.776  1.00 39.44  ?  16  THR A CA    1 
ATOM   110  C  C     . THR A 1 30  ? 32.918  -0.705  17.917  1.00 43.70  ?  16  THR A C     1 
ATOM   111  O  O     . THR A 1 30  ? 33.628  -0.586  16.911  1.00 39.51  ?  16  THR A O     1 
ATOM   112  C  CB    . THR A 1 30  ? 33.646  0.635   19.898  1.00 37.56  ?  16  THR A CB    1 
ATOM   113  O  OG1   . THR A 1 30  ? 34.020  -0.672  20.334  1.00 73.02  ?  16  THR A OG1   1 
ATOM   114  C  CG2   . THR A 1 30  ? 33.080  1.392   21.071  1.00 38.22  ?  16  THR A CG2   1 
ATOM   115  N  N     . ASP A 1 31  ? 32.378  -1.875  18.285  1.00 39.67  ?  17  ASP A N     1 
ATOM   116  C  CA    . ASP A 1 31  ? 32.557  -3.073  17.468  1.00 37.43  ?  17  ASP A CA    1 
ATOM   117  C  C     . ASP A 1 31  ? 32.090  -2.832  16.038  1.00 35.94  ?  17  ASP A C     1 
ATOM   118  O  O     . ASP A 1 31  ? 32.717  -3.301  15.082  1.00 42.10  ?  17  ASP A O     1 
ATOM   119  C  CB    . ASP A 1 31  ? 31.782  -4.252  18.068  1.00 44.52  ?  17  ASP A CB    1 
ATOM   120  C  CG    . ASP A 1 31  ? 32.389  -4.773  19.363  1.00 47.88  ?  17  ASP A CG    1 
ATOM   121  O  OD1   . ASP A 1 31  ? 33.536  -4.412  19.693  1.00 50.78  ?  17  ASP A OD1   1 
ATOM   122  O  OD2   . ASP A 1 31  ? 31.702  -5.552  20.059  1.00 46.10  ?  17  ASP A OD2   1 
ATOM   123  N  N     . CYS A 1 32  ? 30.985  -2.108  15.873  1.00 34.27  ?  18  CYS A N     1 
ATOM   124  C  CA    . CYS A 1 32  ? 30.427  -1.859  14.551  1.00 33.99  ?  18  CYS A CA    1 
ATOM   125  C  C     . CYS A 1 32  ? 31.185  -0.789  13.774  1.00 33.84  ?  18  CYS A C     1 
ATOM   126  O  O     . CYS A 1 32  ? 30.912  -0.607  12.583  1.00 40.84  ?  18  CYS A O     1 
ATOM   127  C  CB    . CYS A 1 32  ? 28.949  -1.481  14.678  1.00 36.37  ?  18  CYS A CB    1 
ATOM   128  S  SG    . CYS A 1 32  ? 27.929  -2.850  15.315  1.00 37.12  ?  18  CYS A SG    1 
ATOM   129  N  N     . GLY A 1 33  ? 32.115  -0.081  14.410  1.00 32.19  ?  19  GLY A N     1 
ATOM   130  C  CA    . GLY A 1 33  ? 32.982  0.849   13.717  1.00 44.90  ?  19  GLY A CA    1 
ATOM   131  C  C     . GLY A 1 33  ? 32.796  2.321   14.042  1.00 47.93  ?  19  GLY A C     1 
ATOM   132  O  O     . GLY A 1 33  ? 33.432  3.160   13.393  1.00 48.50  ?  19  GLY A O     1 
ATOM   133  N  N     . ALA A 1 34  ? 31.970  2.665   15.024  1.00 35.39  ?  20  ALA A N     1 
ATOM   134  C  CA    . ALA A 1 34  ? 31.727  4.053   15.389  1.00 41.80  ?  20  ALA A CA    1 
ATOM   135  C  C     . ALA A 1 34  ? 32.601  4.456   16.570  1.00 44.85  ?  20  ALA A C     1 
ATOM   136  O  O     . ALA A 1 34  ? 32.650  3.753   17.584  1.00 49.54  ?  20  ALA A O     1 
ATOM   137  C  CB    . ALA A 1 34  ? 30.255  4.279   15.732  1.00 33.99  ?  20  ALA A CB    1 
ATOM   138  N  N     . ASP A 1 35  ? 33.296  5.583   16.430  1.00 46.78  ?  21  ASP A N     1 
ATOM   139  C  CA    . ASP A 1 35  ? 34.068  6.163   17.519  1.00 38.40  ?  21  ASP A CA    1 
ATOM   140  C  C     . ASP A 1 35  ? 33.413  7.411   18.095  1.00 43.69  ?  21  ASP A C     1 
ATOM   141  O  O     . ASP A 1 35  ? 33.938  7.985   19.056  1.00 39.62  ?  21  ASP A O     1 
ATOM   142  C  CB    . ASP A 1 35  ? 35.490  6.492   17.047  1.00 34.55  ?  21  ASP A CB    1 
ATOM   143  C  CG    . ASP A 1 35  ? 36.192  5.293   16.427  1.00 52.35  ?  21  ASP A CG    1 
ATOM   144  O  OD1   . ASP A 1 35  ? 36.114  4.187   17.003  1.00 51.15  ?  21  ASP A OD1   1 
ATOM   145  O  OD2   . ASP A 1 35  ? 36.820  5.454   15.361  1.00 48.70  ?  21  ASP A OD2   1 
ATOM   146  N  N     . HIS A 1 36  ? 32.283  7.844   17.538  1.00 35.09  ?  22  HIS A N     1 
ATOM   147  C  CA    . HIS A 1 36  ? 31.586  9.031   18.008  1.00 34.15  ?  22  HIS A CA    1 
ATOM   148  C  C     . HIS A 1 36  ? 30.093  8.755   18.111  1.00 36.60  ?  22  HIS A C     1 
ATOM   149  O  O     . HIS A 1 36  ? 29.549  7.876   17.436  1.00 33.23  ?  22  HIS A O     1 
ATOM   150  C  CB    . HIS A 1 36  ? 31.813  10.234  17.082  1.00 34.99  ?  22  HIS A CB    1 
ATOM   151  C  CG    . HIS A 1 36  ? 33.254  10.607  16.921  1.00 38.33  ?  22  HIS A CG    1 
ATOM   152  N  ND1   . HIS A 1 36  ? 34.131  9.866   16.159  1.00 35.43  ?  22  HIS A ND1   1 
ATOM   153  C  CD2   . HIS A 1 36  ? 33.972  11.637  17.428  1.00 27.68  ?  22  HIS A CD2   1 
ATOM   154  C  CE1   . HIS A 1 36  ? 35.326  10.426  16.200  1.00 35.69  ?  22  HIS A CE1   1 
ATOM   155  N  NE2   . HIS A 1 36  ? 35.256  11.503  16.962  1.00 35.98  ?  22  HIS A NE2   1 
ATOM   156  N  N     . LEU A 1 37  ? 29.441  9.532   18.971  1.00 31.66  ?  23  LEU A N     1 
ATOM   157  C  CA    . LEU A 1 37  ? 27.994  9.504   19.135  1.00 33.51  ?  23  LEU A CA    1 
ATOM   158  C  C     . LEU A 1 37  ? 27.477  10.927  18.975  1.00 32.14  ?  23  LEU A C     1 
ATOM   159  O  O     . LEU A 1 37  ? 27.856  11.816  19.745  1.00 29.52  ?  23  LEU A O     1 
ATOM   160  C  CB    . LEU A 1 37  ? 27.603  8.929   20.499  1.00 26.65  ?  23  LEU A CB    1 
ATOM   161  C  CG    . LEU A 1 37  ? 26.100  8.911   20.804  1.00 27.46  ?  23  LEU A CG    1 
ATOM   162  C  CD1   . LEU A 1 37  ? 25.360  8.057   19.796  1.00 27.85  ?  23  LEU A CD1   1 
ATOM   163  C  CD2   . LEU A 1 37  ? 25.840  8.410   22.213  1.00 31.70  ?  23  LEU A CD2   1 
ATOM   164  N  N     . PHE A 1 38  ? 26.648  11.149  17.958  1.00 29.19  ?  24  PHE A N     1 
ATOM   165  C  CA    . PHE A 1 38  ? 26.035  12.448  17.709  1.00 29.46  ?  24  PHE A CA    1 
ATOM   166  C  C     . PHE A 1 38  ? 24.676  12.536  18.386  1.00 30.63  ?  24  PHE A C     1 
ATOM   167  O  O     . PHE A 1 38  ? 23.995  11.526  18.585  1.00 31.49  ?  24  PHE A O     1 
ATOM   168  C  CB    . PHE A 1 38  ? 25.868  12.691  16.207  1.00 24.31  ?  24  PHE A CB    1 
ATOM   169  C  CG    . PHE A 1 38  ? 27.154  12.597  15.431  1.00 29.31  ?  24  PHE A CG    1 
ATOM   170  C  CD1   . PHE A 1 38  ? 27.621  11.371  14.976  1.00 27.42  ?  24  PHE A CD1   1 
ATOM   171  C  CD2   . PHE A 1 38  ? 27.895  13.741  15.155  1.00 26.37  ?  24  PHE A CD2   1 
ATOM   172  C  CE1   . PHE A 1 38  ? 28.810  11.283  14.261  1.00 27.84  ?  24  PHE A CE1   1 
ATOM   173  C  CE2   . PHE A 1 38  ? 29.080  13.665  14.438  1.00 30.21  ?  24  PHE A CE2   1 
ATOM   174  C  CZ    . PHE A 1 38  ? 29.542  12.432  13.991  1.00 31.99  ?  24  PHE A CZ    1 
ATOM   175  N  N     . GLY A 1 39  ? 24.274  13.751  18.736  1.00 28.35  ?  25  GLY A N     1 
ATOM   176  C  CA    . GLY A 1 39  ? 22.906  13.932  19.187  1.00 29.74  ?  25  GLY A CA    1 
ATOM   177  C  C     . GLY A 1 39  ? 22.728  15.208  19.994  1.00 33.50  ?  25  GLY A C     1 
ATOM   178  O  O     . GLY A 1 39  ? 23.549  16.122  19.937  1.00 28.07  ?  25  GLY A O     1 
ATOM   179  N  N     . VAL A 1 40  ? 21.607  15.247  20.708  1.00 27.20  ?  26  VAL A N     1 
ATOM   180  C  CA    . VAL A 1 40  ? 21.234  16.372  21.562  1.00 29.89  ?  26  VAL A CA    1 
ATOM   181  C  C     . VAL A 1 40  ? 20.765  15.789  22.890  1.00 32.57  ?  26  VAL A C     1 
ATOM   182  O  O     . VAL A 1 40  ? 19.948  14.858  22.895  1.00 30.26  ?  26  VAL A O     1 
ATOM   183  C  CB    . VAL A 1 40  ? 20.140  17.234  20.905  1.00 29.84  ?  26  VAL A CB    1 
ATOM   184  C  CG1   . VAL A 1 40  ? 19.672  18.348  21.847  1.00 22.35  ?  26  VAL A CG1   1 
ATOM   185  C  CG2   . VAL A 1 40  ? 20.630  17.810  19.581  1.00 26.87  ?  26  VAL A CG2   1 
ATOM   186  N  N     . PRO A 1 41  ? 21.228  16.295  24.028  1.00 29.13  ?  27  PRO A N     1 
ATOM   187  C  CA    . PRO A 1 41  ? 20.825  15.706  25.309  1.00 23.61  ?  27  PRO A CA    1 
ATOM   188  C  C     . PRO A 1 41  ? 19.391  16.061  25.684  1.00 32.49  ?  27  PRO A C     1 
ATOM   189  O  O     . PRO A 1 41  ? 18.789  17.018  25.188  1.00 26.67  ?  27  PRO A O     1 
ATOM   190  C  CB    . PRO A 1 41  ? 21.818  16.314  26.304  1.00 27.58  ?  27  PRO A CB    1 
ATOM   191  C  CG    . PRO A 1 41  ? 22.187  17.626  25.692  1.00 27.13  ?  27  PRO A CG    1 
ATOM   192  C  CD    . PRO A 1 41  ? 22.191  17.398  24.203  1.00 27.45  ?  27  PRO A CD    1 
ATOM   193  N  N     . GLY A 1 42  ? 18.848  15.253  26.586  1.00 32.25  ?  28  GLY A N     1 
ATOM   194  C  CA    . GLY A 1 42  ? 17.553  15.511  27.186  1.00 35.44  ?  28  GLY A CA    1 
ATOM   195  C  C     . GLY A 1 42  ? 17.537  14.835  28.537  1.00 31.87  ?  28  GLY A C     1 
ATOM   196  O  O     . GLY A 1 42  ? 18.403  14.010  28.839  1.00 36.41  ?  28  GLY A O     1 
ATOM   197  N  N     . ASP A 1 43  ? 16.550  15.195  29.361  1.00 35.24  ?  29  ASP A N     1 
ATOM   198  C  CA    . ASP A 1 43  ? 16.527  14.648  30.716  1.00 32.59  ?  29  ASP A CA    1 
ATOM   199  C  C     . ASP A 1 43  ? 16.411  13.125  30.711  1.00 40.20  ?  29  ASP A C     1 
ATOM   200  O  O     . ASP A 1 43  ? 16.948  12.461  31.605  1.00 37.91  ?  29  ASP A O     1 
ATOM   201  C  CB    . ASP A 1 43  ? 15.401  15.292  31.546  1.00 41.33  ?  29  ASP A CB    1 
ATOM   202  C  CG    . ASP A 1 43  ? 14.042  14.656  31.318  1.00 41.51  ?  29  ASP A CG    1 
ATOM   203  O  OD1   . ASP A 1 43  ? 13.694  14.356  30.163  1.00 48.64  ?  29  ASP A OD1   1 
ATOM   204  O  OD2   . ASP A 1 43  ? 13.307  14.461  32.312  1.00 50.77  ?  29  ASP A OD2   1 
ATOM   205  N  N     . TYR A 1 44  ? 15.781  12.549  29.684  1.00 35.08  ?  30  TYR A N     1 
ATOM   206  C  CA    . TYR A 1 44  ? 15.616  11.099  29.623  1.00 40.32  ?  30  TYR A CA    1 
ATOM   207  C  C     . TYR A 1 44  ? 16.893  10.354  29.244  1.00 40.97  ?  30  TYR A C     1 
ATOM   208  O  O     . TYR A 1 44  ? 16.909  9.123   29.345  1.00 34.69  ?  30  TYR A O     1 
ATOM   209  C  CB    . TYR A 1 44  ? 14.497  10.733  28.646  1.00 33.23  ?  30  TYR A CB    1 
ATOM   210  C  CG    . TYR A 1 44  ? 13.136  11.259  29.055  1.00 35.25  ?  30  TYR A CG    1 
ATOM   211  C  CD1   . TYR A 1 44  ? 12.671  11.107  30.355  1.00 36.52  ?  30  TYR A CD1   1 
ATOM   212  C  CD2   . TYR A 1 44  ? 12.326  11.925  28.145  1.00 37.72  ?  30  TYR A CD2   1 
ATOM   213  C  CE1   . TYR A 1 44  ? 11.431  11.593  30.730  1.00 32.33  ?  30  TYR A CE1   1 
ATOM   214  C  CE2   . TYR A 1 44  ? 11.086  12.411  28.511  1.00 31.03  ?  30  TYR A CE2   1 
ATOM   215  C  CZ    . TYR A 1 44  ? 10.646  12.247  29.801  1.00 32.62  ?  30  TYR A CZ    1 
ATOM   216  O  OH    . TYR A 1 44  ? 9.410   12.735  30.158  1.00 36.54  ?  30  TYR A OH    1 
ATOM   217  N  N     . ASN A 1 45  ? 17.956  11.047  28.804  1.00 35.66  ?  31  ASN A N     1 
ATOM   218  C  CA    . ASN A 1 45  ? 19.182  10.362  28.400  1.00 36.70  ?  31  ASN A CA    1 
ATOM   219  C  C     . ASN A 1 45  ? 20.441  10.890  29.083  1.00 34.00  ?  31  ASN A C     1 
ATOM   220  O  O     . ASN A 1 45  ? 21.548  10.546  28.654  1.00 36.73  ?  31  ASN A O     1 
ATOM   221  C  CB    . ASN A 1 45  ? 19.364  10.414  26.870  1.00 33.44  ?  31  ASN A CB    1 
ATOM   222  C  CG    . ASN A 1 45  ? 19.581  11.828  26.328  1.00 36.77  ?  31  ASN A CG    1 
ATOM   223  O  OD1   . ASN A 1 45  ? 20.140  12.696  26.996  1.00 36.81  ?  31  ASN A OD1   1 
ATOM   224  N  ND2   . ASN A 1 45  ? 19.158  12.048  25.087  1.00 30.15  ?  31  ASN A ND2   1 
ATOM   225  N  N     . LEU A 1 46  ? 20.310  11.717  30.122  1.00 28.81  ?  32  LEU A N     1 
ATOM   226  C  CA    . LEU A 1 46  ? 21.493  12.286  30.763  1.00 37.41  ?  32  LEU A CA    1 
ATOM   227  C  C     . LEU A 1 46  ? 22.350  11.207  31.424  1.00 39.64  ?  32  LEU A C     1 
ATOM   228  O  O     . LEU A 1 46  ? 23.583  11.245  31.333  1.00 30.82  ?  32  LEU A O     1 
ATOM   229  C  CB    . LEU A 1 46  ? 21.075  13.351  31.778  1.00 33.50  ?  32  LEU A CB    1 
ATOM   230  C  CG    . LEU A 1 46  ? 20.448  14.622  31.188  1.00 32.84  ?  32  LEU A CG    1 
ATOM   231  C  CD1   . LEU A 1 46  ? 20.475  15.749  32.179  1.00 27.94  ?  32  LEU A CD1   1 
ATOM   232  C  CD2   . LEU A 1 46  ? 21.153  15.056  29.913  1.00 31.15  ?  32  LEU A CD2   1 
ATOM   233  N  N     . GLN A 1 47  ? 21.717  10.240  32.097  1.00 34.18  ?  33  GLN A N     1 
ATOM   234  C  CA    . GLN A 1 47  ? 22.477  9.198   32.785  1.00 37.24  ?  33  GLN A CA    1 
ATOM   235  C  C     . GLN A 1 47  ? 23.213  8.304   31.796  1.00 37.62  ?  33  GLN A C     1 
ATOM   236  O  O     . GLN A 1 47  ? 24.336  7.862   32.064  1.00 35.22  ?  33  GLN A O     1 
ATOM   237  C  CB    . GLN A 1 47  ? 21.553  8.366   33.668  1.00 40.42  ?  33  GLN A CB    1 
ATOM   238  C  CG    . GLN A 1 47  ? 20.534  9.175   34.443  1.00 55.89  ?  33  GLN A CG    1 
ATOM   239  C  CD    . GLN A 1 47  ? 20.511  8.817   35.911  1.00 58.20  ?  33  GLN A CD    1 
ATOM   240  O  OE1   . GLN A 1 47  ? 21.520  8.396   36.472  1.00 64.42  ?  33  GLN A OE1   1 
ATOM   241  N  NE2   . GLN A 1 47  ? 19.351  8.965   36.539  1.00 67.76  ?  33  GLN A NE2   1 
ATOM   242  N  N     . PHE A 1 48  ? 22.596  8.027   30.645  1.00 35.40  ?  34  PHE A N     1 
ATOM   243  C  CA    . PHE A 1 48  ? 23.302  7.307   29.592  1.00 38.22  ?  34  PHE A CA    1 
ATOM   244  C  C     . PHE A 1 48  ? 24.524  8.087   29.121  1.00 38.17  ?  34  PHE A C     1 
ATOM   245  O  O     . PHE A 1 48  ? 25.590  7.506   28.883  1.00 40.75  ?  34  PHE A O     1 
ATOM   246  C  CB    . PHE A 1 48  ? 22.356  7.037   28.424  1.00 26.19  ?  34  PHE A CB    1 
ATOM   247  C  CG    . PHE A 1 48  ? 23.011  6.362   27.254  1.00 41.37  ?  34  PHE A CG    1 
ATOM   248  C  CD1   . PHE A 1 48  ? 23.438  5.044   27.345  1.00 37.55  ?  34  PHE A CD1   1 
ATOM   249  C  CD2   . PHE A 1 48  ? 23.190  7.040   26.057  1.00 36.38  ?  34  PHE A CD2   1 
ATOM   250  C  CE1   . PHE A 1 48  ? 24.034  4.417   26.268  1.00 32.62  ?  34  PHE A CE1   1 
ATOM   251  C  CE2   . PHE A 1 48  ? 23.792  6.415   24.976  1.00 34.27  ?  34  PHE A CE2   1 
ATOM   252  C  CZ    . PHE A 1 48  ? 24.212  5.102   25.084  1.00 35.89  ?  34  PHE A CZ    1 
ATOM   253  N  N     . LEU A 1 49  ? 24.390  9.409   28.996  1.00 37.95  ?  35  LEU A N     1 
ATOM   254  C  CA    . LEU A 1 49  ? 25.488  10.233  28.501  1.00 38.98  ?  35  LEU A CA    1 
ATOM   255  C  C     . LEU A 1 49  ? 26.696  10.197  29.428  1.00 31.31  ?  35  LEU A C     1 
ATOM   256  O  O     . LEU A 1 49  ? 27.832  10.355  28.969  1.00 37.43  ?  35  LEU A O     1 
ATOM   257  C  CB    . LEU A 1 49  ? 25.008  11.668  28.307  1.00 34.00  ?  35  LEU A CB    1 
ATOM   258  C  CG    . LEU A 1 49  ? 24.330  11.927  26.965  1.00 35.28  ?  35  LEU A CG    1 
ATOM   259  C  CD1   . LEU A 1 49  ? 23.695  13.311  26.941  1.00 25.88  ?  35  LEU A CD1   1 
ATOM   260  C  CD2   . LEU A 1 49  ? 25.342  11.768  25.846  1.00 33.88  ?  35  LEU A CD2   1 
ATOM   261  N  N     . ASP A 1 50  ? 26.477  9.997   30.729  1.00 31.19  ?  36  ASP A N     1 
ATOM   262  C  CA    . ASP A 1 50  ? 27.601  9.820   31.644  1.00 34.68  ?  36  ASP A CA    1 
ATOM   263  C  C     . ASP A 1 50  ? 28.510  8.689   31.182  1.00 38.66  ?  36  ASP A C     1 
ATOM   264  O  O     . ASP A 1 50  ? 29.737  8.790   31.278  1.00 38.60  ?  36  ASP A O     1 
ATOM   265  C  CB    . ASP A 1 50  ? 27.092  9.542   33.056  1.00 45.18  ?  36  ASP A CB    1 
ATOM   266  C  CG    . ASP A 1 50  ? 26.499  10.766  33.715  1.00 48.01  ?  36  ASP A CG    1 
ATOM   267  O  OD1   . ASP A 1 50  ? 26.582  11.862  33.122  1.00 46.52  ?  36  ASP A OD1   1 
ATOM   268  O  OD2   . ASP A 1 50  ? 25.950  10.628  34.829  1.00 39.95  ?  36  ASP A OD2   1 
ATOM   269  N  N     . HIS A 1 51  ? 27.922  7.594   30.694  1.00 37.71  ?  37  HIS A N     1 
ATOM   270  C  CA    . HIS A 1 51  ? 28.731  6.481   30.207  1.00 38.31  ?  37  HIS A CA    1 
ATOM   271  C  C     . HIS A 1 51  ? 29.407  6.812   28.882  1.00 37.52  ?  37  HIS A C     1 
ATOM   272  O  O     . HIS A 1 51  ? 30.508  6.318   28.614  1.00 35.46  ?  37  HIS A O     1 
ATOM   273  C  CB    . HIS A 1 51  ? 27.863  5.227   30.089  1.00 32.54  ?  37  HIS A CB    1 
ATOM   274  C  CG    . HIS A 1 51  ? 27.294  4.782   31.397  1.00 32.35  ?  37  HIS A CG    1 
ATOM   275  N  ND1   . HIS A 1 51  ? 27.886  3.808   32.174  1.00 34.10  ?  37  HIS A ND1   1 
ATOM   276  C  CD2   . HIS A 1 51  ? 26.207  5.204   32.086  1.00 32.02  ?  37  HIS A CD2   1 
ATOM   277  C  CE1   . HIS A 1 51  ? 27.182  3.643   33.280  1.00 38.16  ?  37  HIS A CE1   1 
ATOM   278  N  NE2   . HIS A 1 51  ? 26.156  4.475   33.249  1.00 32.43  ?  37  HIS A NE2   1 
ATOM   279  N  N     . VAL A 1 52  ? 28.772  7.637   28.046  1.00 37.29  ?  38  VAL A N     1 
ATOM   280  C  CA    . VAL A 1 52  ? 29.418  8.085   26.816  1.00 31.87  ?  38  VAL A CA    1 
ATOM   281  C  C     . VAL A 1 52  ? 30.635  8.949   27.133  1.00 39.83  ?  38  VAL A C     1 
ATOM   282  O  O     . VAL A 1 52  ? 31.704  8.779   26.535  1.00 39.98  ?  38  VAL A O     1 
ATOM   283  C  CB    . VAL A 1 52  ? 28.410  8.834   25.925  1.00 33.99  ?  38  VAL A CB    1 
ATOM   284  C  CG1   . VAL A 1 52  ? 29.080  9.295   24.636  1.00 33.67  ?  38  VAL A CG1   1 
ATOM   285  C  CG2   . VAL A 1 52  ? 27.206  7.959   25.628  1.00 31.12  ?  38  VAL A CG2   1 
ATOM   286  N  N     . ILE A 1 53  ? 30.495  9.886   28.076  1.00 41.10  ?  39  ILE A N     1 
ATOM   287  C  CA    . ILE A 1 53  ? 31.624  10.723  28.477  1.00 39.61  ?  39  ILE A CA    1 
ATOM   288  C  C     . ILE A 1 53  ? 32.741  9.865   29.056  1.00 48.70  ?  39  ILE A C     1 
ATOM   289  O  O     . ILE A 1 53  ? 33.922  10.055  28.741  1.00 43.90  ?  39  ILE A O     1 
ATOM   290  C  CB    . ILE A 1 53  ? 31.163  11.797  29.481  1.00 39.01  ?  39  ILE A CB    1 
ATOM   291  C  CG1   . ILE A 1 53  ? 30.185  12.763  28.817  1.00 32.01  ?  39  ILE A CG1   1 
ATOM   292  C  CG2   . ILE A 1 53  ? 32.365  12.555  30.047  1.00 38.77  ?  39  ILE A CG2   1 
ATOM   293  C  CD1   . ILE A 1 53  ? 30.791  13.527  27.663  1.00 40.82  ?  39  ILE A CD1   1 
ATOM   294  N  N     . ASP A 1 54  ? 32.386  8.909   29.912  1.00 42.66  ?  40  ASP A N     1 
ATOM   295  C  CA    . ASP A 1 54  ? 33.383  8.093   30.587  1.00 48.93  ?  40  ASP A CA    1 
ATOM   296  C  C     . ASP A 1 54  ? 34.017  7.061   29.662  1.00 48.30  ?  40  ASP A C     1 
ATOM   297  O  O     . ASP A 1 54  ? 35.094  6.549   29.978  1.00 49.84  ?  40  ASP A O     1 
ATOM   298  C  CB    . ASP A 1 54  ? 32.747  7.397   31.792  1.00 51.21  ?  40  ASP A CB    1 
ATOM   299  C  CG    . ASP A 1 54  ? 32.702  8.285   33.021  1.00 60.63  ?  40  ASP A CG    1 
ATOM   300  O  OD1   . ASP A 1 54  ? 33.229  9.416   32.960  1.00 63.46  ?  40  ASP A OD1   1 
ATOM   301  O  OD2   . ASP A 1 54  ? 32.142  7.851   34.051  1.00 66.01  ?  40  ASP A OD2   1 
ATOM   302  N  N     . SER A 1 55  ? 33.380  6.737   28.543  1.00 49.10  ?  41  SER A N     1 
ATOM   303  C  CA    . SER A 1 55  ? 33.911  5.703   27.660  1.00 45.09  ?  41  SER A CA    1 
ATOM   304  C  C     . SER A 1 55  ? 35.207  6.176   27.012  1.00 47.62  ?  41  SER A C     1 
ATOM   305  O  O     . SER A 1 55  ? 35.275  7.315   26.539  1.00 51.09  ?  41  SER A O     1 
ATOM   306  C  CB    . SER A 1 55  ? 32.899  5.349   26.578  1.00 47.96  ?  41  SER A CB    1 
ATOM   307  O  OG    . SER A 1 55  ? 33.562  4.897   25.409  1.00 48.71  ?  41  SER A OG    1 
ATOM   308  N  N     . PRO A 1 56  ? 36.249  5.340   26.965  1.00 56.82  ?  42  PRO A N     1 
ATOM   309  C  CA    . PRO A 1 56  ? 37.470  5.725   26.245  1.00 53.46  ?  42  PRO A CA    1 
ATOM   310  C  C     . PRO A 1 56  ? 37.395  5.506   24.744  1.00 52.14  ?  42  PRO A C     1 
ATOM   311  O  O     . PRO A 1 56  ? 38.318  5.925   24.032  1.00 51.03  ?  42  PRO A O     1 
ATOM   312  C  CB    . PRO A 1 56  ? 38.535  4.821   26.873  1.00 54.32  ?  42  PRO A CB    1 
ATOM   313  C  CG    . PRO A 1 56  ? 37.779  3.592   27.253  1.00 49.87  ?  42  PRO A CG    1 
ATOM   314  C  CD    . PRO A 1 56  ? 36.393  4.042   27.648  1.00 49.66  ?  42  PRO A CD    1 
ATOM   315  N  N     . ASP A 1 57  ? 36.332  4.869   24.245  1.00 51.19  ?  43  ASP A N     1 
ATOM   316  C  CA    . ASP A 1 57  ? 36.216  4.516   22.838  1.00 36.64  ?  43  ASP A CA    1 
ATOM   317  C  C     . ASP A 1 57  ? 35.196  5.344   22.071  1.00 45.25  ?  43  ASP A C     1 
ATOM   318  O  O     . ASP A 1 57  ? 35.269  5.388   20.839  1.00 46.12  ?  43  ASP A O     1 
ATOM   319  C  CB    . ASP A 1 57  ? 35.847  3.034   22.691  1.00 54.20  ?  43  ASP A CB    1 
ATOM   320  C  CG    . ASP A 1 57  ? 36.775  2.120   23.473  1.00 60.46  ?  43  ASP A CG    1 
ATOM   321  O  OD1   . ASP A 1 57  ? 37.926  1.938   23.029  1.00 50.00  ?  43  ASP A OD1   1 
ATOM   322  O  OD2   . ASP A 1 57  ? 36.353  1.583   24.522  1.00 58.50  ?  43  ASP A OD2   1 
ATOM   323  N  N     . ILE A 1 58  ? 34.263  6.000   22.756  1.00 36.89  ?  44  ILE A N     1 
ATOM   324  C  CA    . ILE A 1 58  ? 33.192  6.754   22.115  1.00 36.67  ?  44  ILE A CA    1 
ATOM   325  C  C     . ILE A 1 58  ? 33.291  8.201   22.570  1.00 40.32  ?  44  ILE A C     1 
ATOM   326  O  O     . ILE A 1 58  ? 33.390  8.478   23.772  1.00 37.71  ?  44  ILE A O     1 
ATOM   327  C  CB    . ILE A 1 58  ? 31.807  6.171   22.452  1.00 33.96  ?  44  ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 58  ? 31.723  4.704   22.025  1.00 47.54  ?  44  ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 58  ? 30.703  6.983   21.787  1.00 32.27  ?  44  ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 58  ? 31.401  4.511   20.553  1.00 50.38  ?  44  ILE A CD1   1 
ATOM   331  N  N     . CYS A 1 59  ? 33.250  9.119   21.613  1.00 38.13  ?  45  CYS A N     1 
ATOM   332  C  CA    . CYS A 1 59  ? 33.335  10.547  21.878  1.00 36.15  ?  45  CYS A CA    1 
ATOM   333  C  C     . CYS A 1 59  ? 31.968  11.168  21.627  1.00 32.44  ?  45  CYS A C     1 
ATOM   334  O  O     . CYS A 1 59  ? 31.410  11.026  20.533  1.00 31.04  ?  45  CYS A O     1 
ATOM   335  C  CB    . CYS A 1 59  ? 34.402  11.192  20.993  1.00 38.06  ?  45  CYS A CB    1 
ATOM   336  S  SG    . CYS A 1 59  ? 34.511  12.984  21.115  1.00 48.04  ?  45  CYS A SG    1 
ATOM   337  N  N     . TRP A 1 60  ? 31.431  11.850  22.635  1.00 34.14  ?  46  TRP A N     1 
ATOM   338  C  CA    . TRP A 1 60  ? 30.162  12.545  22.462  1.00 40.03  ?  46  TRP A CA    1 
ATOM   339  C  C     . TRP A 1 60  ? 30.347  13.768  21.574  1.00 34.28  ?  46  TRP A C     1 
ATOM   340  O  O     . TRP A 1 60  ? 31.298  14.537  21.737  1.00 36.24  ?  46  TRP A O     1 
ATOM   341  C  CB    . TRP A 1 60  ? 29.591  12.968  23.816  1.00 31.70  ?  46  TRP A CB    1 
ATOM   342  C  CG    . TRP A 1 60  ? 28.385  13.853  23.696  1.00 32.39  ?  46  TRP A CG    1 
ATOM   343  C  CD1   . TRP A 1 60  ? 28.287  15.166  24.068  1.00 33.28  ?  46  TRP A CD1   1 
ATOM   344  C  CD2   . TRP A 1 60  ? 27.104  13.489  23.166  1.00 29.59  ?  46  TRP A CD2   1 
ATOM   345  N  NE1   . TRP A 1 60  ? 27.022  15.639  23.804  1.00 36.26  ?  46  TRP A NE1   1 
ATOM   346  C  CE2   . TRP A 1 60  ? 26.277  14.630  23.251  1.00 36.89  ?  46  TRP A CE2   1 
ATOM   347  C  CE3   . TRP A 1 60  ? 26.575  12.309  22.634  1.00 28.55  ?  46  TRP A CE3   1 
ATOM   348  C  CZ2   . TRP A 1 60  ? 24.950  14.627  22.815  1.00 29.33  ?  46  TRP A CZ2   1 
ATOM   349  C  CZ3   . TRP A 1 60  ? 25.258  12.306  22.203  1.00 32.23  ?  46  TRP A CZ3   1 
ATOM   350  C  CH2   . TRP A 1 60  ? 24.462  13.462  22.296  1.00 28.48  ?  46  TRP A CH2   1 
ATOM   351  N  N     . VAL A 1 61  ? 29.430  13.948  20.627  1.00 34.56  ?  47  VAL A N     1 
ATOM   352  C  CA    . VAL A 1 61  ? 29.442  15.098  19.722  1.00 36.02  ?  47  VAL A CA    1 
ATOM   353  C  C     . VAL A 1 61  ? 28.062  15.746  19.806  1.00 29.46  ?  47  VAL A C     1 
ATOM   354  O  O     . VAL A 1 61  ? 27.140  15.384  19.067  1.00 27.55  ?  47  VAL A O     1 
ATOM   355  C  CB    . VAL A 1 61  ? 29.788  14.713  18.281  1.00 31.07  ?  47  VAL A CB    1 
ATOM   356  C  CG1   . VAL A 1 61  ? 29.858  15.963  17.409  1.00 26.98  ?  47  VAL A CG1   1 
ATOM   357  C  CG2   . VAL A 1 61  ? 31.107  13.949  18.236  1.00 31.20  ?  47  VAL A CG2   1 
ATOM   358  N  N     . GLY A 1 62  ? 27.920  16.732  20.687  1.00 32.97  ?  48  GLY A N     1 
ATOM   359  C  CA    . GLY A 1 62  ? 26.673  17.469  20.766  1.00 27.73  ?  48  GLY A CA    1 
ATOM   360  C  C     . GLY A 1 62  ? 26.456  18.300  19.513  1.00 36.89  ?  48  GLY A C     1 
ATOM   361  O  O     . GLY A 1 62  ? 27.380  18.922  18.985  1.00 28.63  ?  48  GLY A O     1 
ATOM   362  N  N     . CYS A 1 63  ? 25.222  18.283  19.018  1.00 29.23  ?  49  CYS A N     1 
ATOM   363  C  CA    . CYS A 1 63  ? 24.851  18.984  17.798  1.00 34.71  ?  49  CYS A CA    1 
ATOM   364  C  C     . CYS A 1 63  ? 23.853  20.097  18.100  1.00 36.34  ?  49  CYS A C     1 
ATOM   365  O  O     . CYS A 1 63  ? 23.295  20.190  19.196  1.00 31.55  ?  49  CYS A O     1 
ATOM   366  C  CB    . CYS A 1 63  ? 24.279  18.001  16.773  1.00 33.46  ?  49  CYS A CB    1 
ATOM   367  S  SG    . CYS A 1 63  ? 25.490  16.761  16.253  1.00 30.42  ?  49  CYS A SG    1 
ATOM   368  N  N     . ALA A 1 64  ? 23.626  20.948  17.097  1.00 35.55  ?  50  ALA A N     1 
ATOM   369  C  CA    . ALA A 1 64  ? 22.783  22.120  17.313  1.00 41.03  ?  50  ALA A CA    1 
ATOM   370  C  C     . ALA A 1 64  ? 21.292  21.793  17.247  1.00 37.80  ?  50  ALA A C     1 
ATOM   371  O  O     . ALA A 1 64  ? 20.489  22.506  17.857  1.00 41.01  ?  50  ALA A O     1 
ATOM   372  C  CB    . ALA A 1 64  ? 23.143  23.218  16.313  1.00 28.99  ?  50  ALA A CB    1 
ATOM   373  N  N     . ASN A 1 65  ? 20.898  20.754  16.511  1.00 30.46  ?  51  ASN A N     1 
ATOM   374  C  CA    . ASN A 1 65  ? 19.552  20.201  16.631  1.00 34.69  ?  51  ASN A CA    1 
ATOM   375  C  C     . ASN A 1 65  ? 19.575  18.760  16.133  1.00 32.96  ?  51  ASN A C     1 
ATOM   376  O  O     . ASN A 1 65  ? 20.547  18.308  15.521  1.00 25.60  ?  51  ASN A O     1 
ATOM   377  C  CB    . ASN A 1 65  ? 18.487  21.055  15.908  1.00 23.96  ?  51  ASN A CB    1 
ATOM   378  C  CG    . ASN A 1 65  ? 18.683  21.142  14.397  1.00 27.85  ?  51  ASN A CG    1 
ATOM   379  O  OD1   . ASN A 1 65  ? 19.076  20.179  13.742  1.00 28.16  ?  51  ASN A OD1   1 
ATOM   380  N  ND2   . ASN A 1 65  ? 18.356  22.303  13.833  1.00 21.75  ?  51  ASN A ND2   1 
ATOM   381  N  N     . GLU A 1 66  ? 18.488  18.037  16.423  1.00 29.81  ?  52  GLU A N     1 
ATOM   382  C  CA    . GLU A 1 66  ? 18.465  16.597  16.167  1.00 31.30  ?  52  GLU A CA    1 
ATOM   383  C  C     . GLU A 1 66  ? 18.463  16.290  14.676  1.00 31.00  ?  52  GLU A C     1 
ATOM   384  O  O     . GLU A 1 66  ? 19.078  15.309  14.244  1.00 30.22  ?  52  GLU A O     1 
ATOM   385  C  CB    . GLU A 1 66  ? 17.256  15.952  16.843  1.00 25.45  ?  52  GLU A CB    1 
ATOM   386  C  CG    . GLU A 1 66  ? 17.366  15.876  18.344  1.00 26.71  ?  52  GLU A CG    1 
ATOM   387  C  CD    . GLU A 1 66  ? 16.842  17.130  19.019  1.00 32.51  ?  52  GLU A CD    1 
ATOM   388  O  OE1   . GLU A 1 66  ? 16.531  18.116  18.313  1.00 22.55  ?  52  GLU A OE1   1 
ATOM   389  O  OE2   . GLU A 1 66  ? 16.743  17.122  20.259  1.00 29.03  ?  52  GLU A OE2   1 
ATOM   390  N  N     . LEU A 1 67  ? 17.769  17.101  13.872  1.00 26.47  ?  53  LEU A N     1 
ATOM   391  C  CA    . LEU A 1 67  ? 17.780  16.856  12.435  1.00 24.23  ?  53  LEU A CA    1 
ATOM   392  C  C     . LEU A 1 67  ? 19.203  16.904  11.904  1.00 29.50  ?  53  LEU A C     1 
ATOM   393  O  O     . LEU A 1 67  ? 19.641  15.995  11.190  1.00 26.66  ?  53  LEU A O     1 
ATOM   394  C  CB    . LEU A 1 67  ? 16.908  17.879  11.707  1.00 25.97  ?  53  LEU A CB    1 
ATOM   395  C  CG    . LEU A 1 67  ? 16.860  17.715  10.184  1.00 26.31  ?  53  LEU A CG    1 
ATOM   396  C  CD1   . LEU A 1 67  ? 16.480  16.290  9.822   1.00 23.81  ?  53  LEU A CD1   1 
ATOM   397  C  CD2   . LEU A 1 67  ? 15.889  18.700  9.546   1.00 27.21  ?  53  LEU A CD2   1 
ATOM   398  N  N     . ASN A 1 68  ? 19.958  17.935  12.305  1.00 23.26  ?  54  ASN A N     1 
ATOM   399  C  CA    . ASN A 1 68  ? 21.354  18.055  11.900  1.00 24.02  ?  54  ASN A CA    1 
ATOM   400  C  C     . ASN A 1 68  ? 22.193  16.895  12.426  1.00 29.07  ?  54  ASN A C     1 
ATOM   401  O  O     . ASN A 1 68  ? 23.062  16.376  11.716  1.00 24.96  ?  54  ASN A O     1 
ATOM   402  C  CB    . ASN A 1 68  ? 21.924  19.376  12.404  1.00 21.59  ?  54  ASN A CB    1 
ATOM   403  C  CG    . ASN A 1 68  ? 21.263  20.592  11.770  1.00 31.17  ?  54  ASN A CG    1 
ATOM   404  O  OD1   . ASN A 1 68  ? 20.335  20.472  10.968  1.00 33.17  ?  54  ASN A OD1   1 
ATOM   405  N  ND2   . ASN A 1 68  ? 21.736  21.771  12.138  1.00 28.49  ?  54  ASN A ND2   1 
ATOM   406  N  N     . ALA A 1 69  ? 21.951  16.479  13.671  1.00 26.94  ?  55  ALA A N     1 
ATOM   407  C  CA    . ALA A 1 69  ? 22.694  15.353  14.225  1.00 28.35  ?  55  ALA A CA    1 
ATOM   408  C  C     . ALA A 1 69  ? 22.472  14.092  13.400  1.00 29.37  ?  55  ALA A C     1 
ATOM   409  O  O     . ALA A 1 69  ? 23.406  13.311  13.186  1.00 24.12  ?  55  ALA A O     1 
ATOM   410  C  CB    . ALA A 1 69  ? 22.297  15.121  15.683  1.00 23.80  ?  55  ALA A CB    1 
ATOM   411  N  N     . SER A 1 70  ? 21.243  13.875  12.922  1.00 25.91  ?  56  SER A N     1 
ATOM   412  C  CA    . SER A 1 70  ? 20.983  12.687  12.111  1.00 26.52  ?  56  SER A CA    1 
ATOM   413  C  C     . SER A 1 70  ? 21.658  12.794  10.746  1.00 25.97  ?  56  SER A C     1 
ATOM   414  O  O     . SER A 1 70  ? 22.194  11.802  10.236  1.00 25.95  ?  56  SER A O     1 
ATOM   415  C  CB    . SER A 1 70  ? 19.471  12.451  11.980  1.00 27.03  ?  56  SER A CB    1 
ATOM   416  O  OG    . SER A 1 70  ? 18.852  13.340  11.067  1.00 24.70  ?  56  SER A OG    1 
ATOM   417  N  N     . TYR A 1 71  ? 21.672  13.996  10.157  1.00 23.13  ?  57  TYR A N     1 
ATOM   418  C  CA    . TYR A 1 71  ? 22.437  14.218  8.931   1.00 28.50  ?  57  TYR A CA    1 
ATOM   419  C  C     . TYR A 1 71  ? 23.929  13.990  9.158   1.00 30.82  ?  57  TYR A C     1 
ATOM   420  O  O     . TYR A 1 71  ? 24.611  13.391  8.317   1.00 27.20  ?  57  TYR A O     1 
ATOM   421  C  CB    . TYR A 1 71  ? 22.219  15.636  8.410   1.00 24.17  ?  57  TYR A CB    1 
ATOM   422  C  CG    . TYR A 1 71  ? 20.846  15.966  7.855   1.00 28.20  ?  57  TYR A CG    1 
ATOM   423  C  CD1   . TYR A 1 71  ? 19.990  14.974  7.381   1.00 23.26  ?  57  TYR A CD1   1 
ATOM   424  C  CD2   . TYR A 1 71  ? 20.417  17.290  7.787   1.00 23.73  ?  57  TYR A CD2   1 
ATOM   425  C  CE1   . TYR A 1 71  ? 18.734  15.296  6.865   1.00 23.34  ?  57  TYR A CE1   1 
ATOM   426  C  CE2   . TYR A 1 71  ? 19.172  17.620  7.281   1.00 25.76  ?  57  TYR A CE2   1 
ATOM   427  C  CZ    . TYR A 1 71  ? 18.334  16.621  6.820   1.00 29.91  ?  57  TYR A CZ    1 
ATOM   428  O  OH    . TYR A 1 71  ? 17.101  16.963  6.312   1.00 26.93  ?  57  TYR A OH    1 
ATOM   429  N  N     . ALA A 1 72  ? 24.463  14.491  10.276  1.00 27.33  ?  58  ALA A N     1 
ATOM   430  C  CA    . ALA A 1 72  ? 25.885  14.306  10.555  1.00 30.96  ?  58  ALA A CA    1 
ATOM   431  C  C     . ALA A 1 72  ? 26.221  12.829  10.723  1.00 27.43  ?  58  ALA A C     1 
ATOM   432  O  O     . ALA A 1 72  ? 27.229  12.351  10.188  1.00 22.78  ?  58  ALA A O     1 
ATOM   433  C  CB    . ALA A 1 72  ? 26.289  15.095  11.800  1.00 21.81  ?  58  ALA A CB    1 
ATOM   434  N  N     . ALA A 1 73  ? 25.371  12.086  11.438  1.00 24.58  ?  59  ALA A N     1 
ATOM   435  C  CA    . ALA A 1 73  ? 25.588  10.648  11.589  1.00 31.08  ?  59  ALA A CA    1 
ATOM   436  C  C     . ALA A 1 73  ? 25.597  9.956   10.234  1.00 29.08  ?  59  ALA A C     1 
ATOM   437  O  O     . ALA A 1 73  ? 26.460  9.112   9.963   1.00 32.22  ?  59  ALA A O     1 
ATOM   438  C  CB    . ALA A 1 73  ? 24.510  10.043  12.491  1.00 21.13  ?  59  ALA A CB    1 
ATOM   439  N  N     . ASP A 1 74  ? 24.668  10.334  9.354   1.00 27.05  ?  60  ASP A N     1 
ATOM   440  C  CA    . ASP A 1 74  ? 24.642  9.775   8.007   1.00 29.33  ?  60  ASP A CA    1 
ATOM   441  C  C     . ASP A 1 74  ? 25.970  10.019  7.295   1.00 30.60  ?  60  ASP A C     1 
ATOM   442  O  O     . ASP A 1 74  ? 26.602  9.078   6.797   1.00 26.67  ?  60  ASP A O     1 
ATOM   443  C  CB    . ASP A 1 74  ? 23.469  10.382  7.227   1.00 21.10  ?  60  ASP A CB    1 
ATOM   444  C  CG    . ASP A 1 74  ? 23.197  9.677   5.910   1.00 29.06  ?  60  ASP A CG    1 
ATOM   445  O  OD1   . ASP A 1 74  ? 24.103  9.649   5.041   1.00 27.28  ?  60  ASP A OD1   1 
ATOM   446  O  OD2   . ASP A 1 74  ? 22.058  9.179   5.727   1.00 26.66  ?  60  ASP A OD2   1 
ATOM   447  N  N     . GLY A 1 75  ? 26.439  11.271  7.289   1.00 27.18  ?  61  GLY A N     1 
ATOM   448  C  CA    . GLY A 1 75  ? 27.705  11.567  6.638   1.00 25.88  ?  61  GLY A CA    1 
ATOM   449  C  C     . GLY A 1 75  ? 28.869  10.837  7.281   1.00 26.01  ?  61  GLY A C     1 
ATOM   450  O  O     . GLY A 1 75  ? 29.759  10.339  6.590   1.00 24.46  ?  61  GLY A O     1 
ATOM   451  N  N     . TYR A 1 76  ? 28.858  10.747  8.612   1.00 27.27  ?  62  TYR A N     1 
ATOM   452  C  CA    . TYR A 1 76  ? 29.836  9.944   9.338   1.00 28.01  ?  62  TYR A CA    1 
ATOM   453  C  C     . TYR A 1 76  ? 29.809  8.487   8.879   1.00 30.85  ?  62  TYR A C     1 
ATOM   454  O  O     . TYR A 1 76  ? 30.854  7.898   8.578   1.00 25.72  ?  62  TYR A O     1 
ATOM   455  C  CB    . TYR A 1 76  ? 29.550  10.054  10.836  1.00 23.87  ?  62  TYR A CB    1 
ATOM   456  C  CG    . TYR A 1 76  ? 30.552  9.392   11.763  1.00 31.21  ?  62  TYR A CG    1 
ATOM   457  C  CD1   . TYR A 1 76  ? 30.449  8.040   12.093  1.00 29.08  ?  62  TYR A CD1   1 
ATOM   458  C  CD2   . TYR A 1 76  ? 31.574  10.131  12.344  1.00 27.31  ?  62  TYR A CD2   1 
ATOM   459  C  CE1   . TYR A 1 76  ? 31.352  7.446   12.964  1.00 25.59  ?  62  TYR A CE1   1 
ATOM   460  C  CE2   . TYR A 1 76  ? 32.476  9.552   13.210  1.00 33.01  ?  62  TYR A CE2   1 
ATOM   461  C  CZ    . TYR A 1 76  ? 32.363  8.214   13.517  1.00 31.14  ?  62  TYR A CZ    1 
ATOM   462  O  OH    . TYR A 1 76  ? 33.266  7.660   14.387  1.00 35.57  ?  62  TYR A OH    1 
ATOM   463  N  N     . ALA A 1 77  ? 28.614  7.892   8.806   1.00 29.66  ?  63  ALA A N     1 
ATOM   464  C  CA    . ALA A 1 77  ? 28.520  6.487   8.418   1.00 26.89  ?  63  ALA A CA    1 
ATOM   465  C  C     . ALA A 1 77  ? 28.971  6.268   6.980   1.00 32.00  ?  63  ALA A C     1 
ATOM   466  O  O     . ALA A 1 77  ? 29.485  5.193   6.647   1.00 27.95  ?  63  ALA A O     1 
ATOM   467  C  CB    . ALA A 1 77  ? 27.093  5.976   8.610   1.00 24.67  ?  63  ALA A CB    1 
ATOM   468  N  N     . ARG A 1 78  ? 28.809  7.270   6.116   1.00 26.38  ?  64  ARG A N     1 
ATOM   469  C  CA    . ARG A 1 78  ? 29.327  7.139   4.762   1.00 25.21  ?  64  ARG A CA    1 
ATOM   470  C  C     . ARG A 1 78  ? 30.848  7.196   4.713   1.00 28.42  ?  64  ARG A C     1 
ATOM   471  O  O     . ARG A 1 78  ? 31.429  6.941   3.653   1.00 27.86  ?  64  ARG A O     1 
ATOM   472  C  CB    . ARG A 1 78  ? 28.737  8.225   3.867   1.00 24.88  ?  64  ARG A CB    1 
ATOM   473  C  CG    . ARG A 1 78  ? 27.229  8.127   3.690   1.00 24.29  ?  64  ARG A CG    1 
ATOM   474  C  CD    . ARG A 1 78  ? 26.756  9.214   2.743   1.00 28.28  ?  64  ARG A CD    1 
ATOM   475  N  NE    . ARG A 1 78  ? 25.311  9.228   2.564   1.00 23.36  ?  64  ARG A NE    1 
ATOM   476  C  CZ    . ARG A 1 78  ? 24.716  9.296   1.381   1.00 31.34  ?  64  ARG A CZ    1 
ATOM   477  N  NH1   . ARG A 1 78  ? 25.417  9.313   0.257   1.00 27.75  ?  64  ARG A NH1   1 
ATOM   478  N  NH2   . ARG A 1 78  ? 23.386  9.358   1.325   1.00 24.82  ?  64  ARG A NH2   1 
ATOM   479  N  N     . CYS A 1 79  ? 31.502  7.533   5.822   1.00 26.29  ?  65  CYS A N     1 
ATOM   480  C  CA    . CYS A 1 79  ? 32.955  7.540   5.888   1.00 29.71  ?  65  CYS A CA    1 
ATOM   481  C  C     . CYS A 1 79  ? 33.527  6.391   6.700   1.00 34.95  ?  65  CYS A C     1 
ATOM   482  O  O     . CYS A 1 79  ? 34.589  5.875   6.350   1.00 35.13  ?  65  CYS A O     1 
ATOM   483  C  CB    . CYS A 1 79  ? 33.448  8.862   6.485   1.00 28.12  ?  65  CYS A CB    1 
ATOM   484  S  SG    . CYS A 1 79  ? 33.130  10.285  5.415   1.00 37.88  ?  65  CYS A SG    1 
ATOM   485  N  N     . LYS A 1 80  ? 32.842  5.960   7.758   1.00 27.86  ?  66  LYS A N     1 
ATOM   486  C  CA    . LYS A 1 80  ? 33.357  4.902   8.611   1.00 36.89  ?  66  LYS A CA    1 
ATOM   487  C  C     . LYS A 1 80  ? 32.581  3.598   8.503   1.00 44.22  ?  66  LYS A C     1 
ATOM   488  O  O     . LYS A 1 80  ? 33.023  2.593   9.067   1.00 39.09  ?  66  LYS A O     1 
ATOM   489  C  CB    . LYS A 1 80  ? 33.377  5.367   10.075  1.00 42.33  ?  66  LYS A CB    1 
ATOM   490  C  CG    . LYS A 1 80  ? 34.626  6.183   10.428  1.00 47.38  ?  66  LYS A CG    1 
ATOM   491  C  CD    . LYS A 1 80  ? 34.768  6.348   11.928  1.00 39.51  ?  66  LYS A CD    1 
ATOM   492  C  CE    . LYS A 1 80  ? 36.210  6.280   12.360  1.00 43.00  ?  66  LYS A CE    1 
ATOM   493  N  NZ    . LYS A 1 80  ? 36.901  5.099   11.782  1.00 81.10  ?  66  LYS A NZ    1 
ATOM   494  N  N     . GLY A 1 81  ? 31.461  3.578   7.774   1.00 34.21  ?  67  GLY A N     1 
ATOM   495  C  CA    . GLY A 1 81  ? 30.659  2.385   7.601   1.00 34.00  ?  67  GLY A CA    1 
ATOM   496  C  C     . GLY A 1 81  ? 29.580  2.172   8.640   1.00 36.73  ?  67  GLY A C     1 
ATOM   497  O  O     . GLY A 1 81  ? 28.840  1.184   8.544   1.00 37.78  ?  67  GLY A O     1 
ATOM   498  N  N     . PHE A 1 82  ? 29.472  3.056   9.629   1.00 35.46  ?  68  PHE A N     1 
ATOM   499  C  CA    . PHE A 1 82  ? 28.523  2.908   10.724  1.00 27.60  ?  68  PHE A CA    1 
ATOM   500  C  C     . PHE A 1 82  ? 28.508  4.197   11.528  1.00 32.56  ?  68  PHE A C     1 
ATOM   501  O  O     . PHE A 1 82  ? 29.530  4.887   11.626  1.00 25.65  ?  68  PHE A O     1 
ATOM   502  C  CB    . PHE A 1 82  ? 28.895  1.730   11.631  1.00 27.08  ?  68  PHE A CB    1 
ATOM   503  C  CG    . PHE A 1 82  ? 27.782  1.283   12.519  1.00 32.90  ?  68  PHE A CG    1 
ATOM   504  C  CD1   . PHE A 1 82  ? 26.870  0.340   12.080  1.00 39.62  ?  68  PHE A CD1   1 
ATOM   505  C  CD2   . PHE A 1 82  ? 27.646  1.800   13.795  1.00 34.09  ?  68  PHE A CD2   1 
ATOM   506  C  CE1   . PHE A 1 82  ? 25.841  -0.086  12.899  1.00 37.73  ?  68  PHE A CE1   1 
ATOM   507  C  CE2   . PHE A 1 82  ? 26.606  1.385   14.614  1.00 33.34  ?  68  PHE A CE2   1 
ATOM   508  C  CZ    . PHE A 1 82  ? 25.708  0.445   14.165  1.00 30.26  ?  68  PHE A CZ    1 
ATOM   509  N  N     . ALA A 1 83  ? 27.353  4.506   12.115  1.00 23.90  ?  69  ALA A N     1 
ATOM   510  C  CA    . ALA A 1 83  ? 27.237  5.702   12.941  1.00 34.86  ?  69  ALA A CA    1 
ATOM   511  C  C     . ALA A 1 83  ? 26.098  5.515   13.929  1.00 37.31  ?  69  ALA A C     1 
ATOM   512  O  O     . ALA A 1 83  ? 25.274  4.607   13.793  1.00 31.30  ?  69  ALA A O     1 
ATOM   513  C  CB    . ALA A 1 83  ? 27.020  6.955   12.092  1.00 28.82  ?  69  ALA A CB    1 
ATOM   514  N  N     . ALA A 1 84  ? 26.071  6.382   14.940  1.00 23.62  ?  70  ALA A N     1 
ATOM   515  C  CA    . ALA A 1 84  ? 25.044  6.305   15.967  1.00 25.48  ?  70  ALA A CA    1 
ATOM   516  C  C     . ALA A 1 84  ? 24.563  7.698   16.325  1.00 31.93  ?  70  ALA A C     1 
ATOM   517  O  O     . ALA A 1 84  ? 25.355  8.646   16.388  1.00 23.83  ?  70  ALA A O     1 
ATOM   518  C  CB    . ALA A 1 84  ? 25.546  5.598   17.223  1.00 34.41  ?  70  ALA A CB    1 
ATOM   519  N  N     . LEU A 1 85  ? 23.260  7.798   16.576  1.00 28.94  ?  71  LEU A N     1 
ATOM   520  C  CA    . LEU A 1 85  ? 22.593  9.037   16.934  1.00 27.63  ?  71  LEU A CA    1 
ATOM   521  C  C     . LEU A 1 85  ? 21.846  8.842   18.244  1.00 28.38  ?  71  LEU A C     1 
ATOM   522  O  O     . LEU A 1 85  ? 21.193  7.816   18.444  1.00 30.25  ?  71  LEU A O     1 
ATOM   523  C  CB    . LEU A 1 85  ? 21.628  9.457   15.825  1.00 25.28  ?  71  LEU A CB    1 
ATOM   524  C  CG    . LEU A 1 85  ? 20.516  10.427  16.200  1.00 29.30  ?  71  LEU A CG    1 
ATOM   525  C  CD1   . LEU A 1 85  ? 21.085  11.825  16.218  1.00 31.12  ?  71  LEU A CD1   1 
ATOM   526  C  CD2   . LEU A 1 85  ? 19.384  10.324  15.203  1.00 29.79  ?  71  LEU A CD2   1 
ATOM   527  N  N     . LEU A 1 86  ? 21.938  9.825   19.134  1.00 26.21  ?  72  LEU A N     1 
ATOM   528  C  CA    . LEU A 1 86  ? 21.232  9.796   20.409  1.00 23.47  ?  72  LEU A CA    1 
ATOM   529  C  C     . LEU A 1 86  ? 20.283  10.986  20.484  1.00 29.84  ?  72  LEU A C     1 
ATOM   530  O  O     . LEU A 1 86  ? 20.711  12.133  20.335  1.00 26.87  ?  72  LEU A O     1 
ATOM   531  C  CB    . LEU A 1 86  ? 22.212  9.820   21.579  1.00 22.09  ?  72  LEU A CB    1 
ATOM   532  C  CG    . LEU A 1 86  ? 21.524  10.002  22.935  1.00 27.90  ?  72  LEU A CG    1 
ATOM   533  C  CD1   . LEU A 1 86  ? 20.800  8.730   23.349  1.00 28.16  ?  72  LEU A CD1   1 
ATOM   534  C  CD2   . LEU A 1 86  ? 22.524  10.430  24.000  1.00 27.66  ?  72  LEU A CD2   1 
ATOM   535  N  N     . THR A 1 87  ? 18.999  10.715  20.710  1.00 26.55  ?  73  THR A N     1 
ATOM   536  C  CA    . THR A 1 87  ? 17.998  11.759  20.887  1.00 29.97  ?  73  THR A CA    1 
ATOM   537  C  C     . THR A 1 87  ? 17.196  11.483  22.153  1.00 28.29  ?  73  THR A C     1 
ATOM   538  O  O     . THR A 1 87  ? 17.308  10.417  22.766  1.00 28.36  ?  73  THR A O     1 
ATOM   539  C  CB    . THR A 1 87  ? 17.049  11.844  19.684  1.00 33.08  ?  73  THR A CB    1 
ATOM   540  O  OG1   . THR A 1 87  ? 16.394  10.578  19.506  1.00 27.89  ?  73  THR A OG1   1 
ATOM   541  C  CG2   . THR A 1 87  ? 17.820  12.212  18.415  1.00 23.01  ?  73  THR A CG2   1 
ATOM   542  N  N     . THR A 1 88  ? 16.378  12.456  22.545  1.00 24.90  ?  74  THR A N     1 
ATOM   543  C  CA    . THR A 1 88  ? 15.483  12.279  23.679  1.00 25.89  ?  74  THR A CA    1 
ATOM   544  C  C     . THR A 1 88  ? 14.092  11.880  23.190  1.00 26.72  ?  74  THR A C     1 
ATOM   545  O  O     . THR A 1 88  ? 13.700  12.181  22.059  1.00 27.00  ?  74  THR A O     1 
ATOM   546  C  CB    . THR A 1 88  ? 15.419  13.543  24.541  1.00 34.87  ?  74  THR A CB    1 
ATOM   547  O  OG1   . THR A 1 88  ? 14.737  13.250  25.766  1.00 37.99  ?  74  THR A OG1   1 
ATOM   548  C  CG2   . THR A 1 88  ? 14.699  14.673  23.820  1.00 32.90  ?  74  THR A CG2   1 
ATOM   549  N  N     . PHE A 1 89  ? 13.359  11.180  24.058  1.00 32.31  ?  75  PHE A N     1 
ATOM   550  C  CA    . PHE A 1 89  ? 12.044  10.636  23.726  1.00 27.79  ?  75  PHE A CA    1 
ATOM   551  C  C     . PHE A 1 89  ? 11.118  11.707  23.160  1.00 29.67  ?  75  PHE A C     1 
ATOM   552  O  O     . PHE A 1 89  ? 10.982  12.796  23.724  1.00 28.99  ?  75  PHE A O     1 
ATOM   553  C  CB    . PHE A 1 89  ? 11.433  10.014  24.987  1.00 34.68  ?  75  PHE A CB    1 
ATOM   554  C  CG    . PHE A 1 89  ? 10.072  9.397   24.786  1.00 37.99  ?  75  PHE A CG    1 
ATOM   555  C  CD1   . PHE A 1 89  ? 9.945   8.065   24.410  1.00 31.88  ?  75  PHE A CD1   1 
ATOM   556  C  CD2   . PHE A 1 89  ? 8.919   10.140  25.005  1.00 32.05  ?  75  PHE A CD2   1 
ATOM   557  C  CE1   . PHE A 1 89  ? 8.695   7.489   24.239  1.00 32.26  ?  75  PHE A CE1   1 
ATOM   558  C  CE2   . PHE A 1 89  ? 7.667   9.572   24.836  1.00 28.71  ?  75  PHE A CE2   1 
ATOM   559  C  CZ    . PHE A 1 89  ? 7.555   8.245   24.453  1.00 37.81  ?  75  PHE A CZ    1 
ATOM   560  N  N     . GLY A 1 90  ? 10.513  11.406  22.015  1.00 26.04  ?  76  GLY A N     1 
ATOM   561  C  CA    . GLY A 1 90  ? 9.491   12.267  21.456  1.00 25.71  ?  76  GLY A CA    1 
ATOM   562  C  C     . GLY A 1 90  ? 10.030  13.453  20.681  1.00 25.86  ?  76  GLY A C     1 
ATOM   563  O  O     . GLY A 1 90  ? 10.145  13.399  19.453  1.00 30.09  ?  76  GLY A O     1 
ATOM   564  N  N     . VAL A 1 91  ? 10.384  14.527  21.391  1.00 30.00  ?  77  VAL A N     1 
ATOM   565  C  CA    . VAL A 1 91  ? 10.802  15.761  20.723  1.00 27.43  ?  77  VAL A CA    1 
ATOM   566  C  C     . VAL A 1 91  ? 12.113  15.555  19.977  1.00 29.93  ?  77  VAL A C     1 
ATOM   567  O  O     . VAL A 1 91  ? 12.334  16.141  18.909  1.00 26.71  ?  77  VAL A O     1 
ATOM   568  C  CB    . VAL A 1 91  ? 10.907  16.918  21.733  1.00 31.21  ?  77  VAL A CB    1 
ATOM   569  C  CG1   . VAL A 1 91  ? 9.543   17.249  22.315  1.00 28.22  ?  77  VAL A CG1   1 
ATOM   570  C  CG2   . VAL A 1 91  ? 11.899  16.586  22.840  1.00 25.51  ?  77  VAL A CG2   1 
ATOM   571  N  N     . GLY A 1 92  ? 13.010  14.735  20.527  1.00 29.98  ?  78  GLY A N     1 
ATOM   572  C  CA    . GLY A 1 92  ? 14.282  14.508  19.863  1.00 26.27  ?  78  GLY A CA    1 
ATOM   573  C  C     . GLY A 1 92  ? 14.146  13.601  18.657  1.00 31.45  ?  78  GLY A C     1 
ATOM   574  O  O     . GLY A 1 92  ? 14.559  13.955  17.548  1.00 24.01  ?  78  GLY A O     1 
ATOM   575  N  N     . GLU A 1 93  ? 13.551  12.419  18.856  1.00 24.61  ?  79  GLU A N     1 
ATOM   576  C  CA    . GLU A 1 93  ? 13.496  11.422  17.791  1.00 26.39  ?  79  GLU A CA    1 
ATOM   577  C  C     . GLU A 1 93  ? 12.647  11.896  16.615  1.00 27.31  ?  79  GLU A C     1 
ATOM   578  O  O     . GLU A 1 93  ? 12.997  11.651  15.456  1.00 32.06  ?  79  GLU A O     1 
ATOM   579  C  CB    . GLU A 1 93  ? 12.975  10.091  18.340  1.00 24.87  ?  79  GLU A CB    1 
ATOM   580  C  CG    . GLU A 1 93  ? 11.526  10.106  18.828  1.00 25.37  ?  79  GLU A CG    1 
ATOM   581  C  CD    . GLU A 1 93  ? 11.139  8.820   19.528  1.00 29.67  ?  79  GLU A CD    1 
ATOM   582  O  OE1   . GLU A 1 93  ? 11.217  7.750   18.887  1.00 28.71  ?  79  GLU A OE1   1 
ATOM   583  O  OE2   . GLU A 1 93  ? 10.756  8.878   20.717  1.00 26.62  ?  79  GLU A OE2   1 
ATOM   584  N  N     . LEU A 1 94  ? 11.535  12.584  16.882  1.00 25.54  ?  80  LEU A N     1 
ATOM   585  C  CA    . LEU A 1 94  ? 10.707  13.052  15.772  1.00 22.74  ?  80  LEU A CA    1 
ATOM   586  C  C     . LEU A 1 94  ? 11.416  14.131  14.960  1.00 26.04  ?  80  LEU A C     1 
ATOM   587  O  O     . LEU A 1 94  ? 11.195  14.239  13.748  1.00 21.10  ?  80  LEU A O     1 
ATOM   588  C  CB    . LEU A 1 94  ? 9.361   13.545  16.294  1.00 21.34  ?  80  LEU A CB    1 
ATOM   589  C  CG    . LEU A 1 94  ? 8.421   12.434  16.784  1.00 24.52  ?  80  LEU A CG    1 
ATOM   590  C  CD1   . LEU A 1 94  ? 7.009   12.962  16.916  1.00 22.40  ?  80  LEU A CD1   1 
ATOM   591  C  CD2   . LEU A 1 94  ? 8.445   11.211  15.869  1.00 24.29  ?  80  LEU A CD2   1 
ATOM   592  N  N     . SER A 1 95  ? 12.270  14.933  15.602  1.00 25.85  ?  81  SER A N     1 
ATOM   593  C  CA    . SER A 1 95  ? 13.071  15.904  14.863  1.00 26.07  ?  81  SER A CA    1 
ATOM   594  C  C     . SER A 1 95  ? 14.062  15.225  13.925  1.00 30.33  ?  81  SER A C     1 
ATOM   595  O  O     . SER A 1 95  ? 14.399  15.782  12.873  1.00 24.90  ?  81  SER A O     1 
ATOM   596  C  CB    . SER A 1 95  ? 13.809  16.819  15.835  1.00 26.41  ?  81  SER A CB    1 
ATOM   597  O  OG    . SER A 1 95  ? 12.889  17.605  16.576  1.00 30.09  ?  81  SER A OG    1 
ATOM   598  N  N     . ALA A 1 96  ? 14.539  14.031  14.286  1.00 25.62  ?  82  ALA A N     1 
ATOM   599  C  CA    . ALA A 1 96  ? 15.523  13.304  13.492  1.00 27.27  ?  82  ALA A CA    1 
ATOM   600  C  C     . ALA A 1 96  ? 14.896  12.399  12.441  1.00 31.77  ?  82  ALA A C     1 
ATOM   601  O  O     . ALA A 1 96  ? 15.631  11.760  11.679  1.00 28.60  ?  82  ALA A O     1 
ATOM   602  C  CB    . ALA A 1 96  ? 16.414  12.459  14.409  1.00 25.27  ?  82  ALA A CB    1 
ATOM   603  N  N     . MET A 1 97  ? 13.563  12.358  12.366  1.00 24.28  ?  83  MET A N     1 
ATOM   604  C  CA    . MET A 1 97  ? 12.881  11.377  11.526  1.00 27.11  ?  83  MET A CA    1 
ATOM   605  C  C     . MET A 1 97  ? 13.278  11.511  10.061  1.00 26.09  ?  83  MET A C     1 
ATOM   606  O  O     . MET A 1 97  ? 13.481  10.507  9.375   1.00 26.42  ?  83  MET A O     1 
ATOM   607  C  CB    . MET A 1 97  ? 11.365  11.517  11.697  1.00 28.49  ?  83  MET A CB    1 
ATOM   608  C  CG    . MET A 1 97  ? 10.565  10.434  11.009  1.00 38.55  ?  83  MET A CG    1 
ATOM   609  S  SD    . MET A 1 97  ? 8.990   10.131  11.833  1.00 64.73  ?  83  MET A SD    1 
ATOM   610  C  CE    . MET A 1 97  ? 9.492   8.952   13.090  1.00 36.76  ?  83  MET A CE    1 
ATOM   611  N  N     . ASN A 1 98  ? 13.361  12.743  9.553   1.00 27.91  ?  84  ASN A N     1 
ATOM   612  C  CA    . ASN A 1 98  ? 13.720  12.933  8.151   1.00 24.71  ?  84  ASN A CA    1 
ATOM   613  C  C     . ASN A 1 98  ? 15.152  12.477  7.863   1.00 26.21  ?  84  ASN A C     1 
ATOM   614  O  O     . ASN A 1 98  ? 15.442  12.013  6.753   1.00 25.62  ?  84  ASN A O     1 
ATOM   615  C  CB    . ASN A 1 98  ? 13.535  14.400  7.755   1.00 23.55  ?  84  ASN A CB    1 
ATOM   616  C  CG    . ASN A 1 98  ? 13.865  14.647  6.300   1.00 29.98  ?  84  ASN A CG    1 
ATOM   617  O  OD1   . ASN A 1 98  ? 13.332  13.984  5.411   1.00 28.13  ?  84  ASN A OD1   1 
ATOM   618  N  ND2   . ASN A 1 98  ? 14.772  15.578  6.049   1.00 20.39  ?  84  ASN A ND2   1 
ATOM   619  N  N     . GLY A 1 99  ? 16.064  12.631  8.826   1.00 20.37  ?  85  GLY A N     1 
ATOM   620  C  CA    . GLY A 1 99  ? 17.419  12.128  8.628   1.00 22.70  ?  85  GLY A CA    1 
ATOM   621  C  C     . GLY A 1 99  ? 17.476  10.610  8.589   1.00 25.98  ?  85  GLY A C     1 
ATOM   622  O  O     . GLY A 1 99  ? 18.114  10.021  7.709   1.00 29.72  ?  85  GLY A O     1 
ATOM   623  N  N     . ILE A 1 100 ? 16.793  9.951   9.532   1.00 27.02  ?  86  ILE A N     1 
ATOM   624  C  CA    . ILE A 1 100 ? 16.763  8.489   9.540   1.00 29.90  ?  86  ILE A CA    1 
ATOM   625  C  C     . ILE A 1 100 ? 16.106  7.965   8.267   1.00 27.54  ?  86  ILE A C     1 
ATOM   626  O  O     . ILE A 1 100 ? 16.528  6.947   7.703   1.00 25.97  ?  86  ILE A O     1 
ATOM   627  C  CB    . ILE A 1 100 ? 16.049  7.963   10.801  1.00 23.71  ?  86  ILE A CB    1 
ATOM   628  C  CG1   . ILE A 1 100 ? 16.813  8.360   12.066  1.00 24.72  ?  86  ILE A CG1   1 
ATOM   629  C  CG2   . ILE A 1 100 ? 15.890  6.448   10.731  1.00 25.02  ?  86  ILE A CG2   1 
ATOM   630  C  CD1   . ILE A 1 100 ? 18.240  7.838   12.107  1.00 26.21  ?  86  ILE A CD1   1 
ATOM   631  N  N     . ALA A 1 101 ? 15.055  8.644   7.799   1.00 19.24  ?  87  ALA A N     1 
ATOM   632  C  CA    . ALA A 1 101 ? 14.404  8.218   6.564   1.00 25.44  ?  87  ALA A CA    1 
ATOM   633  C  C     . ALA A 1 101 ? 15.358  8.297   5.379   1.00 19.90  ?  87  ALA A C     1 
ATOM   634  O  O     . ALA A 1 101 ? 15.366  7.410   4.517   1.00 27.21  ?  87  ALA A O     1 
ATOM   635  C  CB    . ALA A 1 101 ? 13.152  9.057   6.310   1.00 20.83  ?  87  ALA A CB    1 
ATOM   636  N  N     . GLY A 1 102 ? 16.154  9.363   5.304   1.00 20.87  ?  88  GLY A N     1 
ATOM   637  C  CA    . GLY A 1 102 ? 17.155  9.444   4.255   1.00 20.76  ?  88  GLY A CA    1 
ATOM   638  C  C     . GLY A 1 102 ? 18.187  8.340   4.359   1.00 23.49  ?  88  GLY A C     1 
ATOM   639  O  O     . GLY A 1 102 ? 18.627  7.789   3.347   1.00 24.52  ?  88  GLY A O     1 
ATOM   640  N  N     . SER A 1 103 ? 18.582  7.996   5.585   1.00 22.36  ?  89  SER A N     1 
ATOM   641  C  CA    . SER A 1 103 ? 19.518  6.891   5.770   1.00 23.08  ?  89  SER A CA    1 
ATOM   642  C  C     . SER A 1 103 ? 18.913  5.577   5.300   1.00 28.06  ?  89  SER A C     1 
ATOM   643  O  O     . SER A 1 103 ? 19.600  4.756   4.679   1.00 24.42  ?  89  SER A O     1 
ATOM   644  C  CB    . SER A 1 103 ? 19.938  6.802   7.234   1.00 23.64  ?  89  SER A CB    1 
ATOM   645  O  OG    . SER A 1 103 ? 20.604  7.999   7.625   1.00 27.52  ?  89  SER A OG    1 
ATOM   646  N  N     . TYR A 1 104 ? 17.625  5.358   5.582   1.00 27.29  ?  90  TYR A N     1 
ATOM   647  C  CA    . TYR A 1 104 ? 16.964  4.156   5.083   1.00 29.68  ?  90  TYR A CA    1 
ATOM   648  C  C     . TYR A 1 104 ? 16.887  4.164   3.562   1.00 28.91  ?  90  TYR A C     1 
ATOM   649  O  O     . TYR A 1 104 ? 17.210  3.161   2.910   1.00 28.41  ?  90  TYR A O     1 
ATOM   650  C  CB    . TYR A 1 104 ? 15.568  4.027   5.700   1.00 24.77  ?  90  TYR A CB    1 
ATOM   651  C  CG    . TYR A 1 104 ? 14.850  2.746   5.321   1.00 23.03  ?  90  TYR A CG    1 
ATOM   652  C  CD1   . TYR A 1 104 ? 14.076  2.678   4.170   1.00 26.10  ?  90  TYR A CD1   1 
ATOM   653  C  CD2   . TYR A 1 104 ? 14.943  1.606   6.116   1.00 28.90  ?  90  TYR A CD2   1 
ATOM   654  C  CE1   . TYR A 1 104 ? 13.413  1.514   3.814   1.00 26.36  ?  90  TYR A CE1   1 
ATOM   655  C  CE2   . TYR A 1 104 ? 14.286  0.427   5.764   1.00 28.70  ?  90  TYR A CE2   1 
ATOM   656  C  CZ    . TYR A 1 104 ? 13.521  0.393   4.613   1.00 30.82  ?  90  TYR A CZ    1 
ATOM   657  O  OH    . TYR A 1 104 ? 12.858  -0.757  4.248   1.00 35.30  ?  90  TYR A OH    1 
ATOM   658  N  N     . ALA A 1 105 ? 16.507  5.304   2.979   1.00 25.97  ?  91  ALA A N     1 
ATOM   659  C  CA    . ALA A 1 105 ? 16.328  5.392   1.532   1.00 25.30  ?  91  ALA A CA    1 
ATOM   660  C  C     . ALA A 1 105 ? 17.626  5.104   0.791   1.00 29.56  ?  91  ALA A C     1 
ATOM   661  O  O     . ALA A 1 105 ? 17.616  4.483   -0.278  1.00 25.91  ?  91  ALA A O     1 
ATOM   662  C  CB    . ALA A 1 105 ? 15.801  6.781   1.155   1.00 25.21  ?  91  ALA A CB    1 
ATOM   663  N  N     . GLU A 1 106 ? 18.749  5.579   1.321   1.00 26.51  ?  92  GLU A N     1 
ATOM   664  C  CA    . GLU A 1 106 ? 20.033  5.456   0.647   1.00 35.65  ?  92  GLU A CA    1 
ATOM   665  C  C     . GLU A 1 106 ? 20.930  4.401   1.284   1.00 29.71  ?  92  GLU A C     1 
ATOM   666  O  O     . GLU A 1 106 ? 22.127  4.355   0.984   1.00 28.10  ?  92  GLU A O     1 
ATOM   667  C  CB    . GLU A 1 106 ? 20.728  6.820   0.606   1.00 29.54  ?  92  GLU A CB    1 
ATOM   668  C  CG    . GLU A 1 106 ? 19.799  7.960   0.165   1.00 28.08  ?  92  GLU A CG    1 
ATOM   669  C  CD    . GLU A 1 106 ? 20.421  8.869   -0.896  1.00 32.52  ?  92  GLU A CD    1 
ATOM   670  O  OE1   . GLU A 1 106 ? 21.669  8.940   -0.977  1.00 35.47  ?  92  GLU A OE1   1 
ATOM   671  O  OE2   . GLU A 1 106 ? 19.660  9.527   -1.643  1.00 30.12  ?  92  GLU A OE2   1 
ATOM   672  N  N     . HIS A 1 107 ? 20.378  3.558   2.157   1.00 30.00  ?  93  HIS A N     1 
ATOM   673  C  CA    . HIS A 1 107 ? 21.079  2.403   2.717   1.00 30.79  ?  93  HIS A CA    1 
ATOM   674  C  C     . HIS A 1 107 ? 22.330  2.829   3.487   1.00 34.54  ?  93  HIS A C     1 
ATOM   675  O  O     . HIS A 1 107 ? 23.452  2.428   3.172   1.00 29.81  ?  93  HIS A O     1 
ATOM   676  C  CB    . HIS A 1 107 ? 21.440  1.394   1.618   1.00 27.45  ?  93  HIS A CB    1 
ATOM   677  C  CG    . HIS A 1 107 ? 20.255  0.787   0.933   1.00 40.53  ?  93  HIS A CG    1 
ATOM   678  N  ND1   . HIS A 1 107 ? 19.979  -0.565  0.977   1.00 33.52  ?  93  HIS A ND1   1 
ATOM   679  C  CD2   . HIS A 1 107 ? 19.271  1.348   0.191   1.00 32.14  ?  93  HIS A CD2   1 
ATOM   680  C  CE1   . HIS A 1 107 ? 18.882  -0.810  0.282   1.00 39.65  ?  93  HIS A CE1   1 
ATOM   681  N  NE2   . HIS A 1 107 ? 18.431  0.335   -0.202  1.00 37.70  ?  93  HIS A NE2   1 
ATOM   682  N  N     . VAL A 1 108 ? 22.119  3.630   4.524   1.00 27.53  ?  94  VAL A N     1 
ATOM   683  C  CA    . VAL A 1 108 ? 23.196  4.094   5.387   1.00 29.87  ?  94  VAL A CA    1 
ATOM   684  C  C     . VAL A 1 108 ? 22.933  3.562   6.790   1.00 26.28  ?  94  VAL A C     1 
ATOM   685  O  O     . VAL A 1 108 ? 21.872  3.823   7.363   1.00 23.56  ?  94  VAL A O     1 
ATOM   686  C  CB    . VAL A 1 108 ? 23.330  5.627   5.398   1.00 31.07  ?  94  VAL A CB    1 
ATOM   687  C  CG1   . VAL A 1 108 ? 24.575  6.033   6.164   1.00 22.58  ?  94  VAL A CG1   1 
ATOM   688  C  CG2   . VAL A 1 108 ? 23.401  6.155   3.979   1.00 28.29  ?  94  VAL A CG2   1 
ATOM   689  N  N     . PRO A 1 109 ? 23.848  2.800   7.372   1.00 31.14  ?  95  PRO A N     1 
ATOM   690  C  CA    . PRO A 1 109 ? 23.593  2.209   8.692   1.00 28.11  ?  95  PRO A CA    1 
ATOM   691  C  C     . PRO A 1 109 ? 23.782  3.186   9.843   1.00 26.85  ?  95  PRO A C     1 
ATOM   692  O  O     . PRO A 1 109 ? 24.859  3.244   10.442  1.00 28.05  ?  95  PRO A O     1 
ATOM   693  C  CB    . PRO A 1 109 ? 24.608  1.060   8.758   1.00 28.82  ?  95  PRO A CB    1 
ATOM   694  C  CG    . PRO A 1 109 ? 25.728  1.495   7.863   1.00 32.26  ?  95  PRO A CG    1 
ATOM   695  C  CD    . PRO A 1 109 ? 25.132  2.368   6.793   1.00 28.38  ?  95  PRO A CD    1 
ATOM   696  N  N     . VAL A 1 110 ? 22.748  3.951   10.173  1.00 26.71  ?  96  VAL A N     1 
ATOM   697  C  CA    . VAL A 1 110 ? 22.782  4.871   11.305  1.00 29.13  ?  96  VAL A CA    1 
ATOM   698  C  C     . VAL A 1 110 ? 21.918  4.284   12.412  1.00 30.53  ?  96  VAL A C     1 
ATOM   699  O  O     . VAL A 1 110 ? 20.761  3.923   12.176  1.00 29.74  ?  96  VAL A O     1 
ATOM   700  C  CB    . VAL A 1 110 ? 22.298  6.279   10.911  1.00 29.86  ?  96  VAL A CB    1 
ATOM   701  C  CG1   . VAL A 1 110 ? 22.188  7.158   12.144  1.00 27.30  ?  96  VAL A CG1   1 
ATOM   702  C  CG2   . VAL A 1 110 ? 23.250  6.911   9.896   1.00 25.79  ?  96  VAL A CG2   1 
ATOM   703  N  N     . LEU A 1 111 ? 22.489  4.140   13.603  1.00 31.42  ?  97  LEU A N     1 
ATOM   704  C  CA    . LEU A 1 111 ? 21.749  3.620   14.746  1.00 27.68  ?  97  LEU A CA    1 
ATOM   705  C  C     . LEU A 1 111 ? 21.116  4.778   15.509  1.00 35.61  ?  97  LEU A C     1 
ATOM   706  O  O     . LEU A 1 111 ? 21.815  5.697   15.949  1.00 29.67  ?  97  LEU A O     1 
ATOM   707  C  CB    . LEU A 1 111 ? 22.655  2.807   15.667  1.00 29.53  ?  97  LEU A CB    1 
ATOM   708  C  CG    . LEU A 1 111 ? 22.038  2.455   17.025  1.00 32.11  ?  97  LEU A CG    1 
ATOM   709  C  CD1   . LEU A 1 111 ? 21.002  1.331   16.891  1.00 26.95  ?  97  LEU A CD1   1 
ATOM   710  C  CD2   . LEU A 1 111 ? 23.120  2.069   18.024  1.00 39.33  ?  97  LEU A CD2   1 
ATOM   711  N  N     . HIS A 1 112 ? 19.799  4.726   15.678  1.00 33.29  ?  98  HIS A N     1 
ATOM   712  C  CA    . HIS A 1 112 ? 19.064  5.747   16.412  1.00 25.67  ?  98  HIS A CA    1 
ATOM   713  C  C     . HIS A 1 112 ? 18.814  5.230   17.822  1.00 27.60  ?  98  HIS A C     1 
ATOM   714  O  O     . HIS A 1 112 ? 18.033  4.294   18.015  1.00 24.53  ?  98  HIS A O     1 
ATOM   715  C  CB    . HIS A 1 112 ? 17.750  6.087   15.713  1.00 28.54  ?  98  HIS A CB    1 
ATOM   716  C  CG    . HIS A 1 112 ? 17.097  7.332   16.227  1.00 22.54  ?  98  HIS A CG    1 
ATOM   717  N  ND1   . HIS A 1 112 ? 15.911  7.819   15.716  1.00 25.44  ?  98  HIS A ND1   1 
ATOM   718  C  CD2   . HIS A 1 112 ? 17.470  8.196   17.201  1.00 27.66  ?  98  HIS A CD2   1 
ATOM   719  C  CE1   . HIS A 1 112 ? 15.580  8.927   16.356  1.00 25.07  ?  98  HIS A CE1   1 
ATOM   720  N  NE2   . HIS A 1 112 ? 16.512  9.181   17.259  1.00 26.77  ?  98  HIS A NE2   1 
ATOM   721  N  N     . ILE A 1 113 ? 19.494  5.816   18.803  1.00 24.02  ?  99  ILE A N     1 
ATOM   722  C  CA    . ILE A 1 113 ? 19.251  5.511   20.208  1.00 24.68  ?  99  ILE A CA    1 
ATOM   723  C  C     . ILE A 1 113 ? 18.333  6.589   20.766  1.00 31.23  ?  99  ILE A C     1 
ATOM   724  O  O     . ILE A 1 113 ? 18.623  7.787   20.654  1.00 29.63  ?  99  ILE A O     1 
ATOM   725  C  CB    . ILE A 1 113 ? 20.558  5.431   21.012  1.00 27.89  ?  99  ILE A CB    1 
ATOM   726  C  CG1   . ILE A 1 113 ? 21.582  4.544   20.302  1.00 30.87  ?  99  ILE A CG1   1 
ATOM   727  C  CG2   . ILE A 1 113 ? 20.277  4.913   22.419  1.00 23.71  ?  99  ILE A CG2   1 
ATOM   728  C  CD1   . ILE A 1 113 ? 22.993  4.733   20.809  1.00 29.59  ?  99  ILE A CD1   1 
ATOM   729  N  N     . VAL A 1 114 ? 17.213  6.174   21.347  1.00 28.44  ?  100 VAL A N     1 
ATOM   730  C  CA    . VAL A 1 114 ? 16.246  7.099   21.924  1.00 25.36  ?  100 VAL A CA    1 
ATOM   731  C  C     . VAL A 1 114 ? 16.220  6.876   23.429  1.00 30.45  ?  100 VAL A C     1 
ATOM   732  O  O     . VAL A 1 114 ? 15.817  5.806   23.897  1.00 30.15  ?  100 VAL A O     1 
ATOM   733  C  CB    . VAL A 1 114 ? 14.853  6.910   21.307  1.00 31.82  ?  100 VAL A CB    1 
ATOM   734  C  CG1   . VAL A 1 114 ? 13.828  7.832   21.982  1.00 27.88  ?  100 VAL A CG1   1 
ATOM   735  C  CG2   . VAL A 1 114 ? 14.909  7.152   19.796  1.00 22.41  ?  100 VAL A CG2   1 
ATOM   736  N  N     . GLY A 1 115 ? 16.654  7.882   24.187  1.00 26.07  ?  101 GLY A N     1 
ATOM   737  C  CA    . GLY A 1 115 ? 16.520  7.835   25.634  1.00 32.83  ?  101 GLY A CA    1 
ATOM   738  C  C     . GLY A 1 115 ? 15.088  8.146   26.032  1.00 35.12  ?  101 GLY A C     1 
ATOM   739  O  O     . GLY A 1 115 ? 14.522  9.162   25.615  1.00 29.47  ?  101 GLY A O     1 
ATOM   740  N  N     . ALA A 1 116 ? 14.507  7.282   26.852  1.00 26.48  ?  102 ALA A N     1 
ATOM   741  C  CA    . ALA A 1 116 ? 13.083  7.283   27.146  1.00 30.93  ?  102 ALA A CA    1 
ATOM   742  C  C     . ALA A 1 116 ? 12.850  7.302   28.648  1.00 32.98  ?  102 ALA A C     1 
ATOM   743  O  O     . ALA A 1 116 ? 13.744  6.954   29.426  1.00 30.82  ?  102 ALA A O     1 
ATOM   744  C  CB    . ALA A 1 116 ? 12.403  6.051   26.528  1.00 28.97  ?  102 ALA A CB    1 
ATOM   745  N  N     . PRO A 1 117 ? 11.661  7.721   29.091  1.00 33.79  ?  103 PRO A N     1 
ATOM   746  C  CA    . PRO A 1 117 ? 11.345  7.655   30.523  1.00 34.20  ?  103 PRO A CA    1 
ATOM   747  C  C     . PRO A 1 117 ? 11.431  6.230   31.048  1.00 31.84  ?  103 PRO A C     1 
ATOM   748  O  O     . PRO A 1 117 ? 11.341  5.255   30.299  1.00 32.37  ?  103 PRO A O     1 
ATOM   749  C  CB    . PRO A 1 117 ? 9.902   8.174   30.607  1.00 31.67  ?  103 PRO A CB    1 
ATOM   750  C  CG    . PRO A 1 117 ? 9.626   8.848   29.328  1.00 38.51  ?  103 PRO A CG    1 
ATOM   751  C  CD    . PRO A 1 117 ? 10.596  8.366   28.301  1.00 40.80  ?  103 PRO A CD    1 
ATOM   752  N  N     . GLY A 1 118 ? 11.603  6.125   32.364  1.00 34.32  ?  104 GLY A N     1 
ATOM   753  C  CA    . GLY A 1 118 ? 11.726  4.820   32.986  1.00 35.51  ?  104 GLY A CA    1 
ATOM   754  C  C     . GLY A 1 118 ? 10.500  3.957   32.754  1.00 40.09  ?  104 GLY A C     1 
ATOM   755  O  O     . GLY A 1 118 ? 9.385   4.454   32.580  1.00 31.23  ?  104 GLY A O     1 
ATOM   756  N  N     . THR A 1 119 ? 10.724  2.636   32.742  1.00 36.61  ?  105 THR A N     1 
ATOM   757  C  CA    . THR A 1 119 ? 9.641   1.702   32.444  1.00 43.79  ?  105 THR A CA    1 
ATOM   758  C  C     . THR A 1 119 ? 8.484   1.867   33.424  1.00 36.61  ?  105 THR A C     1 
ATOM   759  O  O     . THR A 1 119 ? 7.317   1.783   33.030  1.00 37.34  ?  105 THR A O     1 
ATOM   760  C  CB    . THR A 1 119 ? 10.152  0.256   32.455  1.00 47.91  ?  105 THR A CB    1 
ATOM   761  O  OG1   . THR A 1 119 ? 10.420  -0.155  33.801  1.00 58.09  ?  105 THR A OG1   1 
ATOM   762  C  CG2   . THR A 1 119 ? 11.425  0.118   31.626  1.00 37.50  ?  105 THR A CG2   1 
ATOM   763  N  N     . ALA A 1 120 ? 8.787   2.109   34.702  1.00 43.23  ?  106 ALA A N     1 
ATOM   764  C  CA    . ALA A 1 120 ? 7.731   2.307   35.692  1.00 40.90  ?  106 ALA A CA    1 
ATOM   765  C  C     . ALA A 1 120 ? 6.842   3.483   35.311  1.00 53.04  ?  106 ALA A C     1 
ATOM   766  O  O     . ALA A 1 120 ? 5.611   3.387   35.365  1.00 50.74  ?  106 ALA A O     1 
ATOM   767  C  CB    . ALA A 1 120 ? 8.336   2.525   37.079  1.00 38.17  ?  106 ALA A CB    1 
ATOM   768  N  N     . SER A 1 121 ? 7.453   4.598   34.897  1.00 43.24  ?  107 SER A N     1 
ATOM   769  C  CA    . SER A 1 121 ? 6.678   5.760   34.470  1.00 43.64  ?  107 SER A CA    1 
ATOM   770  C  C     . SER A 1 121 ? 5.797   5.425   33.276  1.00 40.43  ?  107 SER A C     1 
ATOM   771  O  O     . SER A 1 121 ? 4.648   5.874   33.194  1.00 36.95  ?  107 SER A O     1 
ATOM   772  C  CB    . SER A 1 121 ? 7.613   6.921   34.124  1.00 34.07  ?  107 SER A CB    1 
ATOM   773  O  OG    . SER A 1 121 ? 7.822   7.757   35.245  1.00 54.11  ?  107 SER A OG    1 
ATOM   774  N  N     . GLN A 1 122 ? 6.329   4.649   32.330  1.00 35.50  ?  108 GLN A N     1 
ATOM   775  C  CA    . GLN A 1 122 ? 5.559   4.291   31.144  1.00 39.64  ?  108 GLN A CA    1 
ATOM   776  C  C     . GLN A 1 122 ? 4.352   3.423   31.494  1.00 48.18  ?  108 GLN A C     1 
ATOM   777  O  O     . GLN A 1 122 ? 3.243   3.670   31.003  1.00 40.36  ?  108 GLN A O     1 
ATOM   778  C  CB    . GLN A 1 122 ? 6.467   3.585   30.133  1.00 33.86  ?  108 GLN A CB    1 
ATOM   779  C  CG    . GLN A 1 122 ? 7.651   4.431   29.653  1.00 36.87  ?  108 GLN A CG    1 
ATOM   780  C  CD    . GLN A 1 122 ? 8.272   3.891   28.378  1.00 34.02  ?  108 GLN A CD    1 
ATOM   781  O  OE1   . GLN A 1 122 ? 7.595   3.278   27.554  1.00 38.80  ?  108 GLN A OE1   1 
ATOM   782  N  NE2   . GLN A 1 122 ? 9.568   4.107   28.216  1.00 35.65  ?  108 GLN A NE2   1 
ATOM   783  N  N     . GLN A 1 123 ? 4.537   2.422   32.361  1.00 38.79  ?  109 GLN A N     1 
ATOM   784  C  CA    . GLN A 1 123 ? 3.458   1.479   32.645  1.00 44.11  ?  109 GLN A CA    1 
ATOM   785  C  C     . GLN A 1 123 ? 2.286   2.146   33.355  1.00 38.52  ?  109 GLN A C     1 
ATOM   786  O  O     . GLN A 1 123 ? 1.142   1.713   33.191  1.00 48.99  ?  109 GLN A O     1 
ATOM   787  C  CB    . GLN A 1 123 ? 3.994   0.304   33.465  1.00 39.41  ?  109 GLN A CB    1 
ATOM   788  C  CG    . GLN A 1 123 ? 5.146   -0.409  32.781  1.00 41.87  ?  109 GLN A CG    1 
ATOM   789  C  CD    . GLN A 1 123 ? 5.699   -1.567  33.584  1.00 59.94  ?  109 GLN A CD    1 
ATOM   790  O  OE1   . GLN A 1 123 ? 5.851   -1.477  34.803  1.00 58.12  ?  109 GLN A OE1   1 
ATOM   791  N  NE2   . GLN A 1 123 ? 6.026   -2.658  32.898  1.00 54.60  ?  109 GLN A NE2   1 
ATOM   792  N  N     . ARG A 1 124 ? 2.541   3.198   34.135  1.00 42.31  ?  110 ARG A N     1 
ATOM   793  C  CA    . ARG A 1 124 ? 1.460   3.940   34.771  1.00 39.45  ?  110 ARG A CA    1 
ATOM   794  C  C     . ARG A 1 124 ? 0.798   4.943   33.838  1.00 37.17  ?  110 ARG A C     1 
ATOM   795  O  O     . ARG A 1 124 ? -0.174  5.585   34.245  1.00 41.65  ?  110 ARG A O     1 
ATOM   796  C  CB    . ARG A 1 124 ? 1.959   4.667   36.025  1.00 46.30  ?  110 ARG A CB    1 
ATOM   797  C  CG    . ARG A 1 124 ? 2.999   3.898   36.808  1.00 48.07  ?  110 ARG A CG    1 
ATOM   798  C  CD    . ARG A 1 124 ? 3.257   4.497   38.183  1.00 48.99  ?  110 ARG A CD    1 
ATOM   799  N  NE    . ARG A 1 124 ? 4.125   5.666   38.093  1.00 73.76  ?  110 ARG A NE    1 
ATOM   800  C  CZ    . ARG A 1 124 ? 5.331   5.755   38.644  1.00 72.80  ?  110 ARG A CZ    1 
ATOM   801  N  NH1   . ARG A 1 124 ? 5.925   4.702   39.187  1.00 71.39  ?  110 ARG A NH1   1 
ATOM   802  N  NH2   . ARG A 1 124 ? 5.985   6.914   38.594  1.00 59.88  ?  110 ARG A NH2   1 
ATOM   803  N  N     . GLY A 1 125 ? 1.304   5.113   32.621  1.00 34.76  ?  111 GLY A N     1 
ATOM   804  C  CA    . GLY A 1 125 ? 0.695   6.058   31.701  1.00 39.09  ?  111 GLY A CA    1 
ATOM   805  C  C     . GLY A 1 125 ? 0.703   7.479   32.219  1.00 41.28  ?  111 GLY A C     1 
ATOM   806  O  O     . GLY A 1 125 ? -0.308  8.183   32.107  1.00 34.25  ?  111 GLY A O     1 
ATOM   807  N  N     . GLU A 1 126 ? 1.815   7.909   32.809  1.00 38.87  ?  112 GLU A N     1 
ATOM   808  C  CA    . GLU A 1 126 ? 1.886   9.247   33.380  1.00 36.61  ?  112 GLU A CA    1 
ATOM   809  C  C     . GLU A 1 126 ? 1.869   10.306  32.281  1.00 37.88  ?  112 GLU A C     1 
ATOM   810  O  O     . GLU A 1 126 ? 2.292   10.066  31.145  1.00 33.43  ?  112 GLU A O     1 
ATOM   811  C  CB    . GLU A 1 126 ? 3.149   9.396   34.233  1.00 33.41  ?  112 GLU A CB    1 
ATOM   812  C  CG    . GLU A 1 126 ? 3.277   8.360   35.337  1.00 42.41  ?  112 GLU A CG    1 
ATOM   813  C  CD    . GLU A 1 126 ? 4.384   8.687   36.325  1.00 51.90  ?  112 GLU A CD    1 
ATOM   814  O  OE1   . GLU A 1 126 ? 5.488   9.073   35.884  1.00 54.29  ?  112 GLU A OE1   1 
ATOM   815  O  OE2   . GLU A 1 126 ? 4.152   8.545   37.543  1.00 58.30  ?  112 GLU A OE2   1 
ATOM   816  N  N     . LEU A 1 127 ? 1.362   11.490  32.631  1.00 35.47  ?  113 LEU A N     1 
ATOM   817  C  CA    . LEU A 1 127 ? 1.325   12.632  31.715  1.00 36.50  ?  113 LEU A CA    1 
ATOM   818  C  C     . LEU A 1 127 ? 2.672   13.351  31.780  1.00 40.27  ?  113 LEU A C     1 
ATOM   819  O  O     . LEU A 1 127 ? 2.822   14.414  32.389  1.00 41.58  ?  113 LEU A O     1 
ATOM   820  C  CB    . LEU A 1 127 ? 0.174   13.568  32.067  1.00 35.70  ?  113 LEU A CB    1 
ATOM   821  C  CG    . LEU A 1 127 ? -1.219  12.946  32.194  1.00 33.08  ?  113 LEU A CG    1 
ATOM   822  C  CD1   . LEU A 1 127 ? -2.265  14.014  32.460  1.00 43.30  ?  113 LEU A CD1   1 
ATOM   823  C  CD2   . LEU A 1 127 ? -1.563  12.160  30.943  1.00 42.60  ?  113 LEU A CD2   1 
ATOM   824  N  N     . LEU A 1 128 ? 3.667   12.756  31.124  1.00 32.24  ?  114 LEU A N     1 
ATOM   825  C  CA    . LEU A 1 128 ? 5.034   13.256  31.146  1.00 36.29  ?  114 LEU A CA    1 
ATOM   826  C  C     . LEU A 1 128 ? 5.289   14.201  29.974  1.00 33.49  ?  114 LEU A C     1 
ATOM   827  O  O     . LEU A 1 128 ? 4.643   14.121  28.926  1.00 33.88  ?  114 LEU A O     1 
ATOM   828  C  CB    . LEU A 1 128 ? 6.034   12.095  31.096  1.00 26.12  ?  114 LEU A CB    1 
ATOM   829  C  CG    . LEU A 1 128 ? 6.022   11.069  32.234  1.00 36.25  ?  114 LEU A CG    1 
ATOM   830  C  CD1   . LEU A 1 128 ? 7.154   10.049  32.060  1.00 28.88  ?  114 LEU A CD1   1 
ATOM   831  C  CD2   . LEU A 1 128 ? 6.106   11.744  33.596  1.00 30.81  ?  114 LEU A CD2   1 
ATOM   832  N  N     . HIS A 1 129 ? 6.268   15.087  30.153  1.00 30.60  ?  115 HIS A N     1 
ATOM   833  C  CA    . HIS A 1 129 ? 6.680   15.940  29.047  1.00 30.81  ?  115 HIS A CA    1 
ATOM   834  C  C     . HIS A 1 129 ? 7.244   15.083  27.917  1.00 30.56  ?  115 HIS A C     1 
ATOM   835  O  O     . HIS A 1 129 ? 7.758   13.983  28.141  1.00 32.22  ?  115 HIS A O     1 
ATOM   836  C  CB    . HIS A 1 129 ? 7.715   16.974  29.511  1.00 29.37  ?  115 HIS A CB    1 
ATOM   837  C  CG    . HIS A 1 129 ? 8.981   16.370  30.036  1.00 42.43  ?  115 HIS A CG    1 
ATOM   838  N  ND1   . HIS A 1 129 ? 9.091   15.864  31.314  1.00 33.48  ?  115 HIS A ND1   1 
ATOM   839  C  CD2   . HIS A 1 129 ? 10.190  16.185  29.454  1.00 38.15  ?  115 HIS A CD2   1 
ATOM   840  C  CE1   . HIS A 1 129 ? 10.312  15.394  31.496  1.00 39.65  ?  115 HIS A CE1   1 
ATOM   841  N  NE2   . HIS A 1 129 ? 10.999  15.577  30.383  1.00 38.11  ?  115 HIS A NE2   1 
ATOM   842  N  N     . HIS A 1 130 ? 7.114   15.592  26.689  1.00 26.47  ?  116 HIS A N     1 
ATOM   843  C  CA    . HIS A 1 130 ? 7.481   14.901  25.455  1.00 27.21  ?  116 HIS A CA    1 
ATOM   844  C  C     . HIS A 1 130 ? 6.542   13.746  25.117  1.00 34.15  ?  116 HIS A C     1 
ATOM   845  O  O     . HIS A 1 130 ? 6.934   12.829  24.388  1.00 31.52  ?  116 HIS A O     1 
ATOM   846  C  CB    . HIS A 1 130 ? 8.931   14.390  25.486  1.00 25.37  ?  116 HIS A CB    1 
ATOM   847  C  CG    . HIS A 1 130 ? 9.943   15.444  25.815  1.00 32.62  ?  116 HIS A CG    1 
ATOM   848  N  ND1   . HIS A 1 130 ? 9.666   16.793  25.742  1.00 30.57  ?  116 HIS A ND1   1 
ATOM   849  C  CD2   . HIS A 1 130 ? 11.234  15.345  26.213  1.00 31.54  ?  116 HIS A CD2   1 
ATOM   850  C  CE1   . HIS A 1 130 ? 10.742  17.480  26.083  1.00 37.20  ?  116 HIS A CE1   1 
ATOM   851  N  NE2   . HIS A 1 130 ? 11.709  16.625  26.371  1.00 37.30  ?  116 HIS A NE2   1 
ATOM   852  N  N     . THR A 1 131 ? 5.314   13.756  25.635  1.00 33.63  ?  117 THR A N     1 
ATOM   853  C  CA    . THR A 1 131 ? 4.276   12.823  25.217  1.00 30.86  ?  117 THR A CA    1 
ATOM   854  C  C     . THR A 1 131 ? 3.099   13.600  24.645  1.00 35.64  ?  117 THR A C     1 
ATOM   855  O  O     . THR A 1 131 ? 3.017   14.825  24.755  1.00 29.93  ?  117 THR A O     1 
ATOM   856  C  CB    . THR A 1 131 ? 3.786   11.935  26.373  1.00 31.90  ?  117 THR A CB    1 
ATOM   857  O  OG1   . THR A 1 131 ? 2.971   12.711  27.260  1.00 29.25  ?  117 THR A OG1   1 
ATOM   858  C  CG2   . THR A 1 131 ? 4.953   11.332  27.136  1.00 33.52  ?  117 THR A CG2   1 
ATOM   859  N  N     . LEU A 1 132 ? 2.161   12.863  24.052  1.00 31.07  ?  118 LEU A N     1 
ATOM   860  C  CA    . LEU A 1 132 ? 0.957   13.464  23.501  1.00 32.10  ?  118 LEU A CA    1 
ATOM   861  C  C     . LEU A 1 132 ? -0.117  13.705  24.558  1.00 33.94  ?  118 LEU A C     1 
ATOM   862  O  O     . LEU A 1 132 ? -1.242  14.075  24.203  1.00 30.60  ?  118 LEU A O     1 
ATOM   863  C  CB    . LEU A 1 132 ? 0.404   12.586  22.376  1.00 35.18  ?  118 LEU A CB    1 
ATOM   864  C  CG    . LEU A 1 132 ? 1.389   12.231  21.262  1.00 28.96  ?  118 LEU A CG    1 
ATOM   865  C  CD1   . LEU A 1 132 ? 0.703   11.371  20.218  1.00 26.33  ?  118 LEU A CD1   1 
ATOM   866  C  CD2   . LEU A 1 132 ? 1.966   13.482  20.626  1.00 33.62  ?  118 LEU A CD2   1 
ATOM   867  N  N     . GLY A 1 133 ? 0.199   13.506  25.836  1.00 29.54  ?  119 GLY A N     1 
ATOM   868  C  CA    . GLY A 1 133 ? -0.760  13.730  26.898  1.00 29.18  ?  119 GLY A CA    1 
ATOM   869  C  C     . GLY A 1 133 ? -1.791  12.641  27.077  1.00 34.23  ?  119 GLY A C     1 
ATOM   870  O  O     . GLY A 1 133 ? -2.792  12.868  27.768  1.00 30.86  ?  119 GLY A O     1 
ATOM   871  N  N     . ASP A 1 134 ? -1.589  11.471  26.466  1.00 31.35  ?  120 ASP A N     1 
ATOM   872  C  CA    . ASP A 1 134 ? -2.526  10.357  26.533  1.00 29.80  ?  120 ASP A CA    1 
ATOM   873  C  C     . ASP A 1 134 ? -1.991  9.163   27.318  1.00 40.47  ?  120 ASP A C     1 
ATOM   874  O  O     . ASP A 1 134 ? -2.677  8.143   27.406  1.00 30.77  ?  120 ASP A O     1 
ATOM   875  C  CB    . ASP A 1 134 ? -2.899  9.902   25.118  1.00 27.80  ?  120 ASP A CB    1 
ATOM   876  C  CG    . ASP A 1 134 ? -1.675  9.577   24.263  1.00 39.38  ?  120 ASP A CG    1 
ATOM   877  O  OD1   . ASP A 1 134 ? -0.536  9.562   24.792  1.00 30.18  ?  120 ASP A OD1   1 
ATOM   878  O  OD2   . ASP A 1 134 ? -1.853  9.344   23.050  1.00 38.24  ?  120 ASP A OD2   1 
ATOM   879  N  N     . GLY A 1 135 ? -0.781  9.244   27.866  1.00 31.50  ?  121 GLY A N     1 
ATOM   880  C  CA    . GLY A 1 135 ? -0.235  8.115   28.585  1.00 33.07  ?  121 GLY A CA    1 
ATOM   881  C  C     . GLY A 1 135 ? 0.321   7.015   27.710  1.00 37.89  ?  121 GLY A C     1 
ATOM   882  O  O     . GLY A 1 135 ? 0.669   5.949   28.228  1.00 34.64  ?  121 GLY A O     1 
ATOM   883  N  N     . GLU A 1 136 ? 0.401   7.232   26.403  1.00 34.53  ?  122 GLU A N     1 
ATOM   884  C  CA    . GLU A 1 136 ? 0.927   6.250   25.468  1.00 32.63  ?  122 GLU A CA    1 
ATOM   885  C  C     . GLU A 1 136 ? 2.395   6.545   25.208  1.00 34.21  ?  122 GLU A C     1 
ATOM   886  O  O     . GLU A 1 136 ? 2.756   7.684   24.893  1.00 31.19  ?  122 GLU A O     1 
ATOM   887  C  CB    . GLU A 1 136 ? 0.148   6.274   24.154  1.00 34.54  ?  122 GLU A CB    1 
ATOM   888  C  CG    . GLU A 1 136 ? 0.557   5.185   23.185  1.00 47.36  ?  122 GLU A CG    1 
ATOM   889  C  CD    . GLU A 1 136 ? 0.568   3.815   23.830  1.00 50.98  ?  122 GLU A CD    1 
ATOM   890  O  OE1   . GLU A 1 136 ? -0.411  3.485   24.538  1.00 55.19  ?  122 GLU A OE1   1 
ATOM   891  O  OE2   . GLU A 1 136 ? 1.561   3.079   23.637  1.00 39.64  ?  122 GLU A OE2   1 
ATOM   892  N  N     . PHE A 1 137 ? 3.238   5.520   25.331  1.00 32.17  ?  123 PHE A N     1 
ATOM   893  C  CA    . PHE A 1 137 ? 4.677   5.706   25.192  1.00 39.01  ?  123 PHE A CA    1 
ATOM   894  C  C     . PHE A 1 137 ? 5.270   4.919   24.031  1.00 36.26  ?  123 PHE A C     1 
ATOM   895  O  O     . PHE A 1 137 ? 6.498   4.828   23.924  1.00 33.04  ?  123 PHE A O     1 
ATOM   896  C  CB    . PHE A 1 137 ? 5.376   5.350   26.508  1.00 26.46  ?  123 PHE A CB    1 
ATOM   897  C  CG    . PHE A 1 137 ? 5.098   6.336   27.618  1.00 38.08  ?  123 PHE A CG    1 
ATOM   898  C  CD1   . PHE A 1 137 ? 5.907   7.448   27.797  1.00 32.90  ?  123 PHE A CD1   1 
ATOM   899  C  CD2   . PHE A 1 137 ? 4.014   6.161   28.467  1.00 37.50  ?  123 PHE A CD2   1 
ATOM   900  C  CE1   . PHE A 1 137 ? 5.652   8.360   28.810  1.00 29.68  ?  123 PHE A CE1   1 
ATOM   901  C  CE2   . PHE A 1 137 ? 3.753   7.072   29.483  1.00 36.60  ?  123 PHE A CE2   1 
ATOM   902  C  CZ    . PHE A 1 137 ? 4.573   8.175   29.652  1.00 28.96  ?  123 PHE A CZ    1 
ATOM   903  N  N     . ARG A 1 138 ? 4.438   4.384   23.134  1.00 29.37  ?  124 ARG A N     1 
ATOM   904  C  CA    . ARG A 1 138 ? 4.928   3.596   22.010  1.00 24.24  ?  124 ARG A CA    1 
ATOM   905  C  C     . ARG A 1 138 ? 4.532   4.179   20.661  1.00 28.57  ?  124 ARG A C     1 
ATOM   906  O  O     . ARG A 1 138 ? 4.827   3.566   19.627  1.00 33.26  ?  124 ARG A O     1 
ATOM   907  C  CB    . ARG A 1 138 ? 4.427   2.153   22.124  1.00 26.61  ?  124 ARG A CB    1 
ATOM   908  C  CG    . ARG A 1 138 ? 5.258   1.309   23.072  1.00 34.85  ?  124 ARG A CG    1 
ATOM   909  C  CD    . ARG A 1 138 ? 4.639   -0.044  23.317  1.00 44.54  ?  124 ARG A CD    1 
ATOM   910  N  NE    . ARG A 1 138 ? 5.399   -0.790  24.312  1.00 68.75  ?  124 ARG A NE    1 
ATOM   911  C  CZ    . ARG A 1 138 ? 4.864   -1.583  25.229  1.00 57.06  ?  124 ARG A CZ    1 
ATOM   912  N  NH1   . ARG A 1 138 ? 3.555   -1.763  25.308  1.00 63.47  ?  124 ARG A NH1   1 
ATOM   913  N  NH2   . ARG A 1 138 ? 5.661   -2.208  26.090  1.00 63.37  ?  124 ARG A NH2   1 
ATOM   914  N  N     . HIS A 1 139 ? 3.902   5.356   20.643  1.00 24.40  ?  125 HIS A N     1 
ATOM   915  C  CA    . HIS A 1 139 ? 3.535   6.003   19.386  1.00 34.45  ?  125 HIS A CA    1 
ATOM   916  C  C     . HIS A 1 139 ? 4.748   6.180   18.479  1.00 27.04  ?  125 HIS A C     1 
ATOM   917  O  O     . HIS A 1 139 ? 4.717   5.814   17.299  1.00 28.26  ?  125 HIS A O     1 
ATOM   918  C  CB    . HIS A 1 139 ? 2.905   7.375   19.663  1.00 31.68  ?  125 HIS A CB    1 
ATOM   919  C  CG    . HIS A 1 139 ? 1.493   7.325   20.153  1.00 31.38  ?  125 HIS A CG    1 
ATOM   920  N  ND1   . HIS A 1 139 ? 0.534   6.506   19.596  1.00 34.44  ?  125 HIS A ND1   1 
ATOM   921  C  CD2   . HIS A 1 139 ? 0.869   8.023   21.131  1.00 35.16  ?  125 HIS A CD2   1 
ATOM   922  C  CE1   . HIS A 1 139 ? -0.615  6.690   20.222  1.00 39.45  ?  125 HIS A CE1   1 
ATOM   923  N  NE2   . HIS A 1 139 ? -0.440  7.609   21.155  1.00 35.23  ?  125 HIS A NE2   1 
ATOM   924  N  N     . PHE A 1 140 ? 5.822   6.758   19.014  1.00 23.34  ?  126 PHE A N     1 
ATOM   925  C  CA    . PHE A 1 140 ? 6.963   7.139   18.187  1.00 31.56  ?  126 PHE A CA    1 
ATOM   926  C  C     . PHE A 1 140 ? 7.799   5.936   17.781  1.00 30.36  ?  126 PHE A C     1 
ATOM   927  O  O     . PHE A 1 140 ? 8.401   5.942   16.700  1.00 28.07  ?  126 PHE A O     1 
ATOM   928  C  CB    . PHE A 1 140 ? 7.806   8.173   18.931  1.00 24.28  ?  126 PHE A CB    1 
ATOM   929  C  CG    . PHE A 1 140 ? 6.976   9.175   19.693  1.00 30.63  ?  126 PHE A CG    1 
ATOM   930  C  CD1   . PHE A 1 140 ? 5.933   9.845   19.062  1.00 25.94  ?  126 PHE A CD1   1 
ATOM   931  C  CD2   . PHE A 1 140 ? 7.208   9.419   21.039  1.00 25.56  ?  126 PHE A CD2   1 
ATOM   932  C  CE1   . PHE A 1 140 ? 5.144   10.748  19.754  1.00 26.92  ?  126 PHE A CE1   1 
ATOM   933  C  CE2   . PHE A 1 140 ? 6.430   10.325  21.736  1.00 27.16  ?  126 PHE A CE2   1 
ATOM   934  C  CZ    . PHE A 1 140 ? 5.395   10.994  21.091  1.00 27.52  ?  126 PHE A CZ    1 
ATOM   935  N  N     . TYR A 1 141 ? 7.823   4.894   18.614  1.00 30.50  ?  127 TYR A N     1 
ATOM   936  C  CA    . TYR A 1 141 ? 8.456   3.639   18.224  1.00 26.71  ?  127 TYR A CA    1 
ATOM   937  C  C     . TYR A 1 141 ? 7.821   3.089   16.952  1.00 30.66  ?  127 TYR A C     1 
ATOM   938  O  O     . TYR A 1 141 ? 8.517   2.779   15.978  1.00 25.24  ?  127 TYR A O     1 
ATOM   939  C  CB    . TYR A 1 141 ? 8.344   2.637   19.377  1.00 32.85  ?  127 TYR A CB    1 
ATOM   940  C  CG    . TYR A 1 141 ? 8.821   1.233   19.079  1.00 30.92  ?  127 TYR A CG    1 
ATOM   941  C  CD1   . TYR A 1 141 ? 10.172  0.902   19.163  1.00 30.96  ?  127 TYR A CD1   1 
ATOM   942  C  CD2   . TYR A 1 141 ? 7.922   0.230   18.741  1.00 37.54  ?  127 TYR A CD2   1 
ATOM   943  C  CE1   . TYR A 1 141 ? 10.615  -0.384  18.906  1.00 32.53  ?  127 TYR A CE1   1 
ATOM   944  C  CE2   . TYR A 1 141 ? 8.356   -1.065  18.480  1.00 38.77  ?  127 TYR A CE2   1 
ATOM   945  C  CZ    . TYR A 1 141 ? 9.703   -1.361  18.563  1.00 37.38  ?  127 TYR A CZ    1 
ATOM   946  O  OH    . TYR A 1 141 ? 10.137  -2.637  18.306  1.00 47.45  ?  127 TYR A OH    1 
ATOM   947  N  N     . HIS A 1 142 ? 6.489   3.013   16.923  1.00 25.50  ?  128 HIS A N     1 
ATOM   948  C  CA    . HIS A 1 142 ? 5.811   2.469   15.751  1.00 26.26  ?  128 HIS A CA    1 
ATOM   949  C  C     . HIS A 1 142 ? 5.993   3.364   14.535  1.00 31.98  ?  128 HIS A C     1 
ATOM   950  O  O     . HIS A 1 142 ? 6.154   2.866   13.414  1.00 32.55  ?  128 HIS A O     1 
ATOM   951  C  CB    . HIS A 1 142 ? 4.328   2.263   16.054  1.00 27.05  ?  128 HIS A CB    1 
ATOM   952  C  CG    . HIS A 1 142 ? 4.080   1.208   17.082  1.00 39.07  ?  128 HIS A CG    1 
ATOM   953  N  ND1   . HIS A 1 142 ? 3.266   1.405   18.176  1.00 37.43  ?  128 HIS A ND1   1 
ATOM   954  C  CD2   . HIS A 1 142 ? 4.565   -0.052  17.193  1.00 35.34  ?  128 HIS A CD2   1 
ATOM   955  C  CE1   . HIS A 1 142 ? 3.248   0.306   18.910  1.00 48.25  ?  128 HIS A CE1   1 
ATOM   956  N  NE2   . HIS A 1 142 ? 4.029   -0.592  18.336  1.00 42.28  ?  128 HIS A NE2   1 
ATOM   957  N  N     . MET A 1 143 ? 5.987   4.687   14.739  1.00 28.07  ?  129 MET A N     1 
ATOM   958  C  CA    . MET A 1 143 ? 6.177   5.622   13.632  1.00 27.23  ?  129 MET A CA    1 
ATOM   959  C  C     . MET A 1 143 ? 7.539   5.454   12.969  1.00 30.67  ?  129 MET A C     1 
ATOM   960  O  O     . MET A 1 143 ? 7.696   5.775   11.785  1.00 33.67  ?  129 MET A O     1 
ATOM   961  C  CB    . MET A 1 143 ? 5.999   7.061   14.125  1.00 28.04  ?  129 MET A CB    1 
ATOM   962  C  CG    . MET A 1 143 ? 4.540   7.492   14.333  1.00 26.13  ?  129 MET A CG    1 
ATOM   963  S  SD    . MET A 1 143 ? 4.402   8.847   15.521  1.00 32.13  ?  129 MET A SD    1 
ATOM   964  C  CE    . MET A 1 143 ? 4.798   10.251  14.479  1.00 19.81  ?  129 MET A CE    1 
ATOM   965  N  N     . SER A 1 144 ? 8.532   4.958   13.705  1.00 26.34  ?  130 SER A N     1 
ATOM   966  C  CA    . SER A 1 144 ? 9.856   4.728   13.145  1.00 26.37  ?  130 SER A CA    1 
ATOM   967  C  C     . SER A 1 144 ? 9.976   3.406   12.390  1.00 32.81  ?  130 SER A C     1 
ATOM   968  O  O     . SER A 1 144 ? 10.982  3.201   11.698  1.00 25.90  ?  130 SER A O     1 
ATOM   969  C  CB    . SER A 1 144 ? 10.904  4.778   14.257  1.00 32.57  ?  130 SER A CB    1 
ATOM   970  O  OG    . SER A 1 144 ? 12.201  4.953   13.715  1.00 40.23  ?  130 SER A OG    1 
ATOM   971  N  N     . GLU A 1 145 ? 8.993   2.505   12.516  1.00 28.46  ?  131 GLU A N     1 
ATOM   972  C  CA    . GLU A 1 145 ? 9.096   1.195   11.868  1.00 32.22  ?  131 GLU A CA    1 
ATOM   973  C  C     . GLU A 1 145 ? 9.341   1.271   10.364  1.00 31.38  ?  131 GLU A C     1 
ATOM   974  O  O     . GLU A 1 145 ? 10.218  0.541   9.871   1.00 31.02  ?  131 GLU A O     1 
ATOM   975  C  CB    . GLU A 1 145 ? 7.842   0.361   12.165  1.00 29.62  ?  131 GLU A CB    1 
ATOM   976  C  CG    . GLU A 1 145 ? 7.974   -1.099  11.741  1.00 52.34  ?  131 GLU A CG    1 
ATOM   977  C  CD    . GLU A 1 145 ? 7.483   -1.364  10.323  1.00 59.10  ?  131 GLU A CD    1 
ATOM   978  O  OE1   . GLU A 1 145 ? 7.856   -2.414  9.749   1.00 64.34  ?  131 GLU A OE1   1 
ATOM   979  O  OE2   . GLU A 1 145 ? 6.714   -0.535  9.789   1.00 58.05  ?  131 GLU A OE2   1 
ATOM   980  N  N     . PRO A 1 146 ? 8.629   2.090   9.580   1.00 30.45  ?  132 PRO A N     1 
ATOM   981  C  CA    . PRO A 1 146 ? 8.835   2.054   8.123   1.00 29.75  ?  132 PRO A CA    1 
ATOM   982  C  C     . PRO A 1 146 ? 10.207  2.530   7.665   1.00 32.43  ?  132 PRO A C     1 
ATOM   983  O  O     . PRO A 1 146 ? 10.548  2.306   6.496   1.00 29.77  ?  132 PRO A O     1 
ATOM   984  C  CB    . PRO A 1 146 ? 7.728   2.971   7.585   1.00 34.21  ?  132 PRO A CB    1 
ATOM   985  C  CG    . PRO A 1 146 ? 6.708   3.013   8.665   1.00 30.72  ?  132 PRO A CG    1 
ATOM   986  C  CD    . PRO A 1 146 ? 7.486   2.952   9.935   1.00 29.06  ?  132 PRO A CD    1 
ATOM   987  N  N     . ILE A 1 147 ? 10.999  3.176   8.522   1.00 30.00  ?  133 ILE A N     1 
ATOM   988  C  CA    . ILE A 1 147 ? 12.278  3.733   8.097   1.00 28.13  ?  133 ILE A CA    1 
ATOM   989  C  C     . ILE A 1 147 ? 13.458  3.075   8.816   1.00 30.72  ?  133 ILE A C     1 
ATOM   990  O  O     . ILE A 1 147 ? 14.536  3.649   8.885   1.00 31.60  ?  133 ILE A O     1 
ATOM   991  C  CB    . ILE A 1 147 ? 12.299  5.264   8.271   1.00 27.08  ?  133 ILE A CB    1 
ATOM   992  C  CG1   . ILE A 1 147 ? 11.996  5.654   9.718   1.00 22.98  ?  133 ILE A CG1   1 
ATOM   993  C  CG2   . ILE A 1 147 ? 11.287  5.921   7.339   1.00 23.49  ?  133 ILE A CG2   1 
ATOM   994  C  CD1   . ILE A 1 147 ? 12.184  7.135   9.992   1.00 28.13  ?  133 ILE A CD1   1 
ATOM   995  N  N     . THR A 1 148 ? 13.272  1.864   9.341   1.00 31.72  ?  134 THR A N     1 
ATOM   996  C  CA    . THR A 1 148 ? 14.355  1.098   9.945   1.00 28.74  ?  134 THR A CA    1 
ATOM   997  C  C     . THR A 1 148 ? 14.211  -0.367  9.548   1.00 34.71  ?  134 THR A C     1 
ATOM   998  O  O     . THR A 1 148 ? 13.100  -0.846  9.309   1.00 35.92  ?  134 THR A O     1 
ATOM   999  C  CB    . THR A 1 148 ? 14.355  1.224   11.476  1.00 29.61  ?  134 THR A CB    1 
ATOM   1000 O  OG1   . THR A 1 148 ? 13.053  0.911   11.981  1.00 33.61  ?  134 THR A OG1   1 
ATOM   1001 C  CG2   . THR A 1 148 ? 14.735  2.642   11.914  1.00 20.18  ?  134 THR A CG2   1 
ATOM   1002 N  N     . VAL A 1 149 ? 15.344  -1.078  9.466   1.00 28.70  ?  135 VAL A N     1 
ATOM   1003 C  CA    . VAL A 1 149 ? 15.296  -2.515  9.193   1.00 32.93  ?  135 VAL A CA    1 
ATOM   1004 C  C     . VAL A 1 149 ? 15.104  -3.348  10.453  1.00 24.09  ?  135 VAL A C     1 
ATOM   1005 O  O     . VAL A 1 149 ? 14.800  -4.544  10.353  1.00 31.32  ?  135 VAL A O     1 
ATOM   1006 C  CB    . VAL A 1 149 ? 16.553  -3.027  8.467   1.00 29.63  ?  135 VAL A CB    1 
ATOM   1007 C  CG1   . VAL A 1 149 ? 16.524  -2.609  7.014   1.00 38.15  ?  135 VAL A CG1   1 
ATOM   1008 C  CG2   . VAL A 1 149 ? 17.834  -2.570  9.172   1.00 25.27  ?  135 VAL A CG2   1 
ATOM   1009 N  N     . ALA A 1 150 ? 15.301  -2.763  11.628  1.00 25.96  ?  136 ALA A N     1 
ATOM   1010 C  CA    . ALA A 1 150 ? 15.155  -3.486  12.880  1.00 31.83  ?  136 ALA A CA    1 
ATOM   1011 C  C     . ALA A 1 150 ? 15.009  -2.464  13.992  1.00 27.07  ?  136 ALA A C     1 
ATOM   1012 O  O     . ALA A 1 150 ? 15.599  -1.383  13.936  1.00 23.01  ?  136 ALA A O     1 
ATOM   1013 C  CB    . ALA A 1 150 ? 16.351  -4.408  13.150  1.00 29.08  ?  136 ALA A CB    1 
ATOM   1014 N  N     . GLN A 1 151 ? 14.209  -2.808  14.994  1.00 25.89  ?  137 GLN A N     1 
ATOM   1015 C  CA    . GLN A 1 151 ? 14.042  -1.926  16.136  1.00 28.52  ?  137 GLN A CA    1 
ATOM   1016 C  C     . GLN A 1 151 ? 13.687  -2.764  17.352  1.00 34.56  ?  137 GLN A C     1 
ATOM   1017 O  O     . GLN A 1 151 ? 13.272  -3.919  17.233  1.00 28.16  ?  137 GLN A O     1 
ATOM   1018 C  CB    . GLN A 1 151 ? 12.969  -0.855  15.883  1.00 27.16  ?  137 GLN A CB    1 
ATOM   1019 C  CG    . GLN A 1 151 ? 11.602  -1.402  15.568  1.00 34.07  ?  137 GLN A CG    1 
ATOM   1020 C  CD    . GLN A 1 151 ? 10.645  -0.331  15.064  1.00 60.89  ?  137 GLN A CD    1 
ATOM   1021 O  OE1   . GLN A 1 151 ? 10.960  0.868   15.070  1.00 47.19  ?  137 GLN A OE1   1 
ATOM   1022 N  NE2   . GLN A 1 151 ? 9.457   -0.757  14.649  1.00 50.21  ?  137 GLN A NE2   1 
ATOM   1023 N  N     . ALA A 1 152 ? 13.875  -2.175  18.528  1.00 27.30  ?  138 ALA A N     1 
ATOM   1024 C  CA    . ALA A 1 152 ? 13.538  -2.874  19.758  1.00 31.45  ?  138 ALA A CA    1 
ATOM   1025 C  C     . ALA A 1 152 ? 13.256  -1.858  20.852  1.00 26.45  ?  138 ALA A C     1 
ATOM   1026 O  O     . ALA A 1 152 ? 13.765  -0.736  20.822  1.00 26.28  ?  138 ALA A O     1 
ATOM   1027 C  CB    . ALA A 1 152 ? 14.653  -3.833  20.192  1.00 25.70  ?  138 ALA A CB    1 
ATOM   1028 N  N     . ILE A 1 153 ? 12.403  -2.252  21.789  1.00 30.76  ?  139 ILE A N     1 
ATOM   1029 C  CA    . ILE A 1 153 ? 12.259  -1.568  23.066  1.00 30.14  ?  139 ILE A CA    1 
ATOM   1030 C  C     . ILE A 1 153 ? 13.056  -2.376  24.078  1.00 34.19  ?  139 ILE A C     1 
ATOM   1031 O  O     . ILE A 1 153 ? 12.718  -3.528  24.370  1.00 34.95  ?  139 ILE A O     1 
ATOM   1032 C  CB    . ILE A 1 153 ? 10.792  -1.435  23.489  1.00 31.32  ?  139 ILE A CB    1 
ATOM   1033 C  CG1   . ILE A 1 153 ? 10.030  -0.505  22.541  1.00 35.65  ?  139 ILE A CG1   1 
ATOM   1034 C  CG2   . ILE A 1 153 ? 10.709  -0.927  24.919  1.00 31.42  ?  139 ILE A CG2   1 
ATOM   1035 C  CD1   . ILE A 1 153 ? 8.517   -0.589  22.699  1.00 31.82  ?  139 ILE A CD1   1 
ATOM   1036 N  N     . LEU A 1 154 ? 14.131  -1.796  24.600  1.00 30.95  ?  140 LEU A N     1 
ATOM   1037 C  CA    . LEU A 1 154 ? 15.008  -2.530  25.500  1.00 35.29  ?  140 LEU A CA    1 
ATOM   1038 C  C     . LEU A 1 154 ? 14.361  -2.651  26.872  1.00 39.63  ?  140 LEU A C     1 
ATOM   1039 O  O     . LEU A 1 154 ? 13.849  -1.667  27.417  1.00 28.81  ?  140 LEU A O     1 
ATOM   1040 C  CB    . LEU A 1 154 ? 16.370  -1.845  25.606  1.00 27.88  ?  140 LEU A CB    1 
ATOM   1041 C  CG    . LEU A 1 154 ? 17.138  -1.747  24.288  1.00 32.75  ?  140 LEU A CG    1 
ATOM   1042 C  CD1   . LEU A 1 154 ? 18.518  -1.135  24.501  1.00 33.39  ?  140 LEU A CD1   1 
ATOM   1043 C  CD2   . LEU A 1 154 ? 17.251  -3.119  23.630  1.00 30.18  ?  140 LEU A CD2   1 
ATOM   1044 N  N     . THR A 1 155 ? 14.361  -3.865  27.415  1.00 35.39  ?  141 THR A N     1 
ATOM   1045 C  CA    . THR A 1 155 ? 13.863  -4.140  28.753  1.00 36.19  ?  141 THR A CA    1 
ATOM   1046 C  C     . THR A 1 155 ? 14.965  -4.804  29.565  1.00 40.54  ?  141 THR A C     1 
ATOM   1047 O  O     . THR A 1 155 ? 16.014  -5.186  29.040  1.00 37.45  ?  141 THR A O     1 
ATOM   1048 C  CB    . THR A 1 155 ? 12.621  -5.042  28.732  1.00 34.23  ?  141 THR A CB    1 
ATOM   1049 O  OG1   . THR A 1 155 ? 13.006  -6.375  28.371  1.00 35.56  ?  141 THR A OG1   1 
ATOM   1050 C  CG2   . THR A 1 155 ? 11.575  -4.524  27.744  1.00 30.87  ?  141 THR A CG2   1 
ATOM   1051 N  N     . GLU A 1 156 ? 14.713  -4.930  30.868  1.00 40.03  ?  142 GLU A N     1 
ATOM   1052 C  CA    . GLU A 1 156 ? 15.634  -5.653  31.735  1.00 34.54  ?  142 GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 156 ? 15.780  -7.107  31.297  1.00 44.63  ?  142 GLU A C     1 
ATOM   1054 O  O     . GLU A 1 156 ? 16.829  -7.724  31.520  1.00 38.85  ?  142 GLU A O     1 
ATOM   1055 C  CB    . GLU A 1 156 ? 15.142  -5.563  33.183  1.00 42.13  ?  142 GLU A CB    1 
ATOM   1056 C  CG    . GLU A 1 156 ? 15.930  -6.386  34.185  1.00 51.99  ?  142 GLU A CG    1 
ATOM   1057 C  CD    . GLU A 1 156 ? 15.374  -6.284  35.593  1.00 59.12  ?  142 GLU A CD    1 
ATOM   1058 O  OE1   . GLU A 1 156 ? 14.169  -5.980  35.735  1.00 57.16  ?  142 GLU A OE1   1 
ATOM   1059 O  OE2   . GLU A 1 156 ? 16.140  -6.511  36.556  1.00 57.36  ?  142 GLU A OE2   1 
ATOM   1060 N  N     . GLN A 1 157 ? 14.754  -7.662  30.650  1.00 38.02  ?  143 GLN A N     1 
ATOM   1061 C  CA    . GLN A 1 157 ? 14.730  -9.070  30.279  1.00 37.63  ?  143 GLN A CA    1 
ATOM   1062 C  C     . GLN A 1 157 ? 15.262  -9.348  28.877  1.00 39.12  ?  143 GLN A C     1 
ATOM   1063 O  O     . GLN A 1 157 ? 15.448  -10.524 28.534  1.00 36.40  ?  143 GLN A O     1 
ATOM   1064 C  CB    . GLN A 1 157 ? 13.298  -9.618  30.397  1.00 34.59  ?  143 GLN A CB    1 
ATOM   1065 C  CG    . GLN A 1 157 ? 12.680  -9.402  31.770  1.00 43.48  ?  143 GLN A CG    1 
ATOM   1066 C  CD    . GLN A 1 157 ? 11.365  -10.136 31.966  1.00 58.37  ?  143 GLN A CD    1 
ATOM   1067 O  OE1   . GLN A 1 157 ? 11.110  -11.170 31.343  1.00 64.43  ?  143 GLN A OE1   1 
ATOM   1068 N  NE2   . GLN A 1 157 ? 10.523  -9.605  32.845  1.00 56.35  ?  143 GLN A NE2   1 
ATOM   1069 N  N     . ASN A 1 158 ? 15.510  -8.315  28.057  1.00 30.73  ?  144 ASN A N     1 
ATOM   1070 C  CA    . ASN A 1 158 ? 15.915  -8.538  26.674  1.00 35.63  ?  144 ASN A CA    1 
ATOM   1071 C  C     . ASN A 1 158 ? 17.117  -7.721  26.210  1.00 41.07  ?  144 ASN A C     1 
ATOM   1072 O  O     . ASN A 1 158 ? 17.539  -7.889  25.061  1.00 35.46  ?  144 ASN A O     1 
ATOM   1073 C  CB    . ASN A 1 158 ? 14.730  -8.262  25.722  1.00 37.10  ?  144 ASN A CB    1 
ATOM   1074 C  CG    . ASN A 1 158 ? 14.396  -6.769  25.581  1.00 40.70  ?  144 ASN A CG    1 
ATOM   1075 O  OD1   . ASN A 1 158 ? 15.129  -5.889  26.041  1.00 34.79  ?  144 ASN A OD1   1 
ATOM   1076 N  ND2   . ASN A 1 158 ? 13.266  -6.488  24.940  1.00 38.45  ?  144 ASN A ND2   1 
ATOM   1077 N  N     . ALA A 1 159 ? 17.682  -6.859  27.062  1.00 31.96  ?  145 ALA A N     1 
ATOM   1078 C  CA    . ALA A 1 159 ? 18.453  -5.717  26.575  1.00 30.81  ?  145 ALA A CA    1 
ATOM   1079 C  C     . ALA A 1 159 ? 19.612  -6.142  25.682  1.00 35.62  ?  145 ALA A C     1 
ATOM   1080 O  O     . ALA A 1 159 ? 19.739  -5.673  24.544  1.00 35.20  ?  145 ALA A O     1 
ATOM   1081 C  CB    . ALA A 1 159 ? 18.964  -4.893  27.757  1.00 32.10  ?  145 ALA A CB    1 
ATOM   1082 N  N     . CYS A 1 160 ? 20.455  -7.054  26.165  1.00 39.67  ?  146 CYS A N     1 
ATOM   1083 C  CA    . CYS A 1 160 ? 21.724  -7.293  25.489  1.00 40.54  ?  146 CYS A CA    1 
ATOM   1084 C  C     . CYS A 1 160 ? 21.542  -8.045  24.175  1.00 41.89  ?  146 CYS A C     1 
ATOM   1085 O  O     . CYS A 1 160 ? 22.246  -7.761  23.198  1.00 37.89  ?  146 CYS A O     1 
ATOM   1086 C  CB    . CYS A 1 160 ? 22.681  -8.026  26.421  1.00 42.72  ?  146 CYS A CB    1 
ATOM   1087 S  SG    . CYS A 1 160 ? 23.264  -6.936  27.731  1.00 47.33  ?  146 CYS A SG    1 
ATOM   1088 N  N     . TYR A 1 161 ? 20.618  -9.010  24.117  1.00 41.48  ?  147 TYR A N     1 
ATOM   1089 C  CA    . TYR A 1 161 ? 20.451  -9.709  22.847  1.00 36.02  ?  147 TYR A CA    1 
ATOM   1090 C  C     . TYR A 1 161 ? 19.620  -8.903  21.853  1.00 35.66  ?  147 TYR A C     1 
ATOM   1091 O  O     . TYR A 1 161 ? 19.810  -9.047  20.640  1.00 40.53  ?  147 TYR A O     1 
ATOM   1092 C  CB    . TYR A 1 161 ? 19.871  -11.114 23.057  1.00 41.87  ?  147 TYR A CB    1 
ATOM   1093 C  CG    . TYR A 1 161 ? 18.419  -11.234 23.472  1.00 45.30  ?  147 TYR A CG    1 
ATOM   1094 C  CD1   . TYR A 1 161 ? 17.397  -11.203 22.529  1.00 41.41  ?  147 TYR A CD1   1 
ATOM   1095 C  CD2   . TYR A 1 161 ? 18.077  -11.463 24.802  1.00 47.17  ?  147 TYR A CD2   1 
ATOM   1096 C  CE1   . TYR A 1 161 ? 16.066  -11.348 22.907  1.00 52.71  ?  147 TYR A CE1   1 
ATOM   1097 C  CE2   . TYR A 1 161 ? 16.752  -11.611 25.191  1.00 47.04  ?  147 TYR A CE2   1 
ATOM   1098 C  CZ    . TYR A 1 161 ? 15.748  -11.553 24.241  1.00 52.14  ?  147 TYR A CZ    1 
ATOM   1099 O  OH    . TYR A 1 161 ? 14.428  -11.699 24.626  1.00 41.48  ?  147 TYR A OH    1 
ATOM   1100 N  N     . GLU A 1 162 ? 18.727  -8.034  22.329  1.00 29.94  ?  148 GLU A N     1 
ATOM   1101 C  CA    . GLU A 1 162 ? 18.040  -7.131  21.411  1.00 32.95  ?  148 GLU A CA    1 
ATOM   1102 C  C     . GLU A 1 162 ? 19.004  -6.100  20.828  1.00 36.71  ?  148 GLU A C     1 
ATOM   1103 O  O     . GLU A 1 162 ? 18.887  -5.729  19.653  1.00 32.13  ?  148 GLU A O     1 
ATOM   1104 C  CB    . GLU A 1 162 ? 16.862  -6.455  22.113  1.00 31.85  ?  148 GLU A CB    1 
ATOM   1105 C  CG    . GLU A 1 162 ? 15.590  -7.309  22.202  1.00 38.68  ?  148 GLU A CG    1 
ATOM   1106 C  CD    . GLU A 1 162 ? 15.116  -7.839  20.851  1.00 28.72  ?  148 GLU A CD    1 
ATOM   1107 O  OE1   . GLU A 1 162 ? 14.115  -7.318  20.331  1.00 55.46  ?  148 GLU A OE1   1 
ATOM   1108 O  OE2   . GLU A 1 162 ? 15.714  -8.785  20.311  1.00 48.91  ?  148 GLU A OE2   1 
ATOM   1109 N  N     . ILE A 1 163 ? 19.966  -5.628  21.628  1.00 33.08  ?  149 ILE A N     1 
ATOM   1110 C  CA    . ILE A 1 163 ? 21.002  -4.741  21.099  1.00 35.99  ?  149 ILE A CA    1 
ATOM   1111 C  C     . ILE A 1 163 ? 21.778  -5.442  19.990  1.00 30.94  ?  149 ILE A C     1 
ATOM   1112 O  O     . ILE A 1 163 ? 21.978  -4.893  18.899  1.00 28.56  ?  149 ILE A O     1 
ATOM   1113 C  CB    . ILE A 1 163 ? 21.946  -4.278  22.223  1.00 31.37  ?  149 ILE A CB    1 
ATOM   1114 C  CG1   . ILE A 1 163 ? 21.281  -3.218  23.099  1.00 34.36  ?  149 ILE A CG1   1 
ATOM   1115 C  CG2   . ILE A 1 163 ? 23.253  -3.746  21.639  1.00 30.09  ?  149 ILE A CG2   1 
ATOM   1116 C  CD1   . ILE A 1 163 ? 21.986  -3.017  24.429  1.00 30.92  ?  149 ILE A CD1   1 
ATOM   1117 N  N     . ASP A 1 164 ? 22.211  -6.679  20.251  1.00 28.98  ?  150 ASP A N     1 
ATOM   1118 C  CA    . ASP A 1 164 ? 23.005  -7.406  19.266  1.00 29.79  ?  150 ASP A CA    1 
ATOM   1119 C  C     . ASP A 1 164 ? 22.190  -7.729  18.019  1.00 30.29  ?  150 ASP A C     1 
ATOM   1120 O  O     . ASP A 1 164 ? 22.716  -7.684  16.901  1.00 33.06  ?  150 ASP A O     1 
ATOM   1121 C  CB    . ASP A 1 164 ? 23.585  -8.674  19.894  1.00 30.92  ?  150 ASP A CB    1 
ATOM   1122 C  CG    . ASP A 1 164 ? 24.686  -8.372  20.905  1.00 40.12  ?  150 ASP A CG    1 
ATOM   1123 O  OD1   . ASP A 1 164 ? 25.077  -7.189  21.047  1.00 38.58  ?  150 ASP A OD1   1 
ATOM   1124 O  OD2   . ASP A 1 164 ? 25.172  -9.319  21.553  1.00 37.59  ?  150 ASP A OD2   1 
ATOM   1125 N  N     . ARG A 1 165 ? 20.906  -8.059  18.186  1.00 28.64  ?  151 ARG A N     1 
ATOM   1126 C  CA    . ARG A 1 165 ? 20.068  -8.379  17.032  1.00 29.13  ?  151 ARG A CA    1 
ATOM   1127 C  C     . ARG A 1 165 ? 19.901  -7.171  16.115  1.00 31.48  ?  151 ARG A C     1 
ATOM   1128 O  O     . ARG A 1 165 ? 20.023  -7.287  14.889  1.00 34.42  ?  151 ARG A O     1 
ATOM   1129 C  CB    . ARG A 1 165 ? 18.701  -8.894  17.491  1.00 40.71  ?  151 ARG A CB    1 
ATOM   1130 C  CG    . ARG A 1 165 ? 17.648  -8.927  16.379  1.00 32.48  ?  151 ARG A CG    1 
ATOM   1131 C  CD    . ARG A 1 165 ? 16.278  -9.390  16.884  1.00 31.65  ?  151 ARG A CD    1 
ATOM   1132 N  NE    . ARG A 1 165 ? 15.554  -8.353  17.615  1.00 31.34  ?  151 ARG A NE    1 
ATOM   1133 C  CZ    . ARG A 1 165 ? 14.936  -7.325  17.047  1.00 35.14  ?  151 ARG A CZ    1 
ATOM   1134 N  NH1   . ARG A 1 165 ? 14.955  -7.140  15.736  1.00 31.06  ?  151 ARG A NH1   1 
ATOM   1135 N  NH2   . ARG A 1 165 ? 14.270  -6.467  17.813  1.00 32.40  ?  151 ARG A NH2   1 
ATOM   1136 N  N     . VAL A 1 166 ? 19.609  -6.002  16.694  1.00 29.94  ?  152 VAL A N     1 
ATOM   1137 C  CA    . VAL A 1 166 ? 19.377  -4.804  15.886  1.00 25.70  ?  152 VAL A CA    1 
ATOM   1138 C  C     . VAL A 1 166 ? 20.640  -4.416  15.127  1.00 29.21  ?  152 VAL A C     1 
ATOM   1139 O  O     . VAL A 1 166 ? 20.599  -4.106  13.929  1.00 25.27  ?  152 VAL A O     1 
ATOM   1140 C  CB    . VAL A 1 166 ? 18.883  -3.644  16.771  1.00 27.98  ?  152 VAL A CB    1 
ATOM   1141 C  CG1   . VAL A 1 166 ? 18.928  -2.315  15.996  1.00 24.66  ?  152 VAL A CG1   1 
ATOM   1142 C  CG2   . VAL A 1 166 ? 17.478  -3.927  17.291  1.00 32.46  ?  152 VAL A CG2   1 
ATOM   1143 N  N     . LEU A 1 167 ? 21.782  -4.419  15.821  1.00 27.59  ?  153 LEU A N     1 
ATOM   1144 C  CA    . LEU A 1 167 ? 23.036  -4.035  15.181  1.00 29.66  ?  153 LEU A CA    1 
ATOM   1145 C  C     . LEU A 1 167 ? 23.413  -5.015  14.079  1.00 32.81  ?  153 LEU A C     1 
ATOM   1146 O  O     . LEU A 1 167 ? 23.898  -4.610  13.014  1.00 34.07  ?  153 LEU A O     1 
ATOM   1147 C  CB    . LEU A 1 167 ? 24.151  -3.938  16.225  1.00 31.11  ?  153 LEU A CB    1 
ATOM   1148 C  CG    . LEU A 1 167 ? 24.004  -2.765  17.195  1.00 35.55  ?  153 LEU A CG    1 
ATOM   1149 C  CD1   . LEU A 1 167 ? 25.165  -2.694  18.176  1.00 37.31  ?  153 LEU A CD1   1 
ATOM   1150 C  CD2   . LEU A 1 167 ? 23.900  -1.481  16.410  1.00 34.83  ?  153 LEU A CD2   1 
ATOM   1151 N  N     . THR A 1 168 ? 23.200  -6.312  14.318  1.00 30.49  ?  154 THR A N     1 
ATOM   1152 C  CA    . THR A 1 168 ? 23.536  -7.315  13.314  1.00 31.71  ?  154 THR A CA    1 
ATOM   1153 C  C     . THR A 1 168 ? 22.709  -7.131  12.049  1.00 33.12  ?  154 THR A C     1 
ATOM   1154 O  O     . THR A 1 168 ? 23.243  -7.204  10.937  1.00 33.42  ?  154 THR A O     1 
ATOM   1155 C  CB    . THR A 1 168 ? 23.330  -8.715  13.894  1.00 33.22  ?  154 THR A CB    1 
ATOM   1156 O  OG1   . THR A 1 168 ? 24.202  -8.889  15.017  1.00 36.86  ?  154 THR A OG1   1 
ATOM   1157 C  CG2   . THR A 1 168 ? 23.629  -9.782  12.850  1.00 44.83  ?  154 THR A CG2   1 
ATOM   1158 N  N     . THR A 1 169 ? 21.404  -6.878  12.203  1.00 29.44  ?  155 THR A N     1 
ATOM   1159 C  CA    . THR A 1 169 ? 20.554  -6.602  11.048  1.00 28.80  ?  155 THR A CA    1 
ATOM   1160 C  C     . THR A 1 169 ? 21.001  -5.334  10.326  1.00 32.17  ?  155 THR A C     1 
ATOM   1161 O  O     . THR A 1 169 ? 21.068  -5.307  9.090   1.00 30.75  ?  155 THR A O     1 
ATOM   1162 C  CB    . THR A 1 169 ? 19.090  -6.494  11.494  1.00 31.29  ?  155 THR A CB    1 
ATOM   1163 O  OG1   . THR A 1 169 ? 18.710  -7.698  12.173  1.00 31.43  ?  155 THR A OG1   1 
ATOM   1164 C  CG2   . THR A 1 169 ? 18.168  -6.283  10.302  1.00 24.58  ?  155 THR A CG2   1 
ATOM   1165 N  N     . MET A 1 170 ? 21.336  -4.281  11.083  1.00 33.61  ?  156 MET A N     1 
ATOM   1166 C  CA    . MET A 1 170 ? 21.871  -3.060  10.480  1.00 33.95  ?  156 MET A CA    1 
ATOM   1167 C  C     . MET A 1 170 ? 23.110  -3.360  9.647   1.00 40.19  ?  156 MET A C     1 
ATOM   1168 O  O     . MET A 1 170 ? 23.250  -2.870  8.522   1.00 38.74  ?  156 MET A O     1 
ATOM   1169 C  CB    . MET A 1 170 ? 22.212  -2.038  11.566  1.00 27.73  ?  156 MET A CB    1 
ATOM   1170 C  CG    . MET A 1 170 ? 21.027  -1.333  12.201  1.00 25.53  ?  156 MET A CG    1 
ATOM   1171 S  SD    . MET A 1 170 ? 21.640  -0.155  13.417  1.00 32.24  ?  156 MET A SD    1 
ATOM   1172 C  CE    . MET A 1 170 ? 22.549  0.959   12.346  1.00 25.03  ?  156 MET A CE    1 
ATOM   1173 N  N     . LEU A 1 171 ? 24.029  -4.159  10.194  1.00 31.06  ?  157 LEU A N     1 
ATOM   1174 C  CA    . LEU A 1 171 ? 25.220  -4.533  9.441   1.00 33.95  ?  157 LEU A CA    1 
ATOM   1175 C  C     . LEU A 1 171 ? 24.859  -5.358  8.213   1.00 40.70  ?  157 LEU A C     1 
ATOM   1176 O  O     . LEU A 1 171 ? 25.408  -5.138  7.128   1.00 38.59  ?  157 LEU A O     1 
ATOM   1177 C  CB    . LEU A 1 171 ? 26.184  -5.311  10.338  1.00 35.46  ?  157 LEU A CB    1 
ATOM   1178 C  CG    . LEU A 1 171 ? 26.870  -4.513  11.449  1.00 42.33  ?  157 LEU A CG    1 
ATOM   1179 C  CD1   . LEU A 1 171 ? 27.627  -5.435  12.404  1.00 36.51  ?  157 LEU A CD1   1 
ATOM   1180 C  CD2   . LEU A 1 171 ? 27.799  -3.468  10.852  1.00 38.03  ?  157 LEU A CD2   1 
ATOM   1181 N  N     . ARG A 1 172 ? 23.906  -6.286  8.357   1.00 33.10  ?  158 ARG A N     1 
ATOM   1182 C  CA    . ARG A 1 172 ? 23.524  -7.144  7.241   1.00 37.53  ?  158 ARG A CA    1 
ATOM   1183 C  C     . ARG A 1 172 ? 22.887  -6.336  6.117   1.00 45.19  ?  158 ARG A C     1 
ATOM   1184 O  O     . ARG A 1 172 ? 23.251  -6.494  4.946   1.00 41.66  ?  158 ARG A O     1 
ATOM   1185 C  CB    . ARG A 1 172 ? 22.563  -8.236  7.724   1.00 40.10  ?  158 ARG A CB    1 
ATOM   1186 C  CG    . ARG A 1 172 ? 22.256  -9.299  6.675   1.00 56.81  ?  158 ARG A CG    1 
ATOM   1187 C  CD    . ARG A 1 172 ? 21.674  -10.602 7.265   1.00 75.12  ?  158 ARG A CD    1 
ATOM   1188 N  NE    . ARG A 1 172 ? 20.780  -10.402 8.402   1.00 71.38  ?  158 ARG A NE    1 
ATOM   1189 C  CZ    . ARG A 1 172 ? 21.054  -10.764 9.650   1.00 68.88  ?  158 ARG A CZ    1 
ATOM   1190 N  NH1   . ARG A 1 172 ? 20.210  -10.526 10.640  1.00 63.00  ?  158 ARG A NH1   1 
ATOM   1191 N  NH2   . ARG A 1 172 ? 22.198  -11.391 9.909   1.00 59.77  ?  158 ARG A NH2   1 
ATOM   1192 N  N     . GLU A 1 173 ? 21.944  -5.454  6.456   1.00 32.27  ?  159 GLU A N     1 
ATOM   1193 C  CA    . GLU A 1 173 ? 21.185  -4.720  5.452   1.00 29.74  ?  159 GLU A CA    1 
ATOM   1194 C  C     . GLU A 1 173 ? 21.782  -3.366  5.118   1.00 31.52  ?  159 GLU A C     1 
ATOM   1195 O  O     . GLU A 1 173 ? 21.385  -2.770  4.110   1.00 38.72  ?  159 GLU A O     1 
ATOM   1196 C  CB    . GLU A 1 173 ? 19.739  -4.513  5.919   1.00 39.58  ?  159 GLU A CB    1 
ATOM   1197 C  CG    . GLU A 1 173 ? 18.968  -5.799  6.130   1.00 45.90  ?  159 GLU A CG    1 
ATOM   1198 C  CD    . GLU A 1 173 ? 18.992  -6.683  4.902   1.00 50.16  ?  159 GLU A CD    1 
ATOM   1199 O  OE1   . GLU A 1 173 ? 18.784  -6.158  3.786   1.00 52.48  ?  159 GLU A OE1   1 
ATOM   1200 O  OE2   . GLU A 1 173 ? 19.232  -7.899  5.053   1.00 53.87  ?  159 GLU A OE2   1 
ATOM   1201 N  N     . ARG A 1 174 ? 22.732  -2.880  5.920   1.00 33.67  ?  160 ARG A N     1 
ATOM   1202 C  CA    . ARG A 1 174 ? 23.311  -1.548  5.745   1.00 32.52  ?  160 ARG A CA    1 
ATOM   1203 C  C     . ARG A 1 174 ? 22.217  -0.481  5.773   1.00 32.20  ?  160 ARG A C     1 
ATOM   1204 O  O     . ARG A 1 174 ? 22.097  0.341   4.866   1.00 37.83  ?  160 ARG A O     1 
ATOM   1205 C  CB    . ARG A 1 174 ? 24.134  -1.466  4.455   1.00 37.98  ?  160 ARG A CB    1 
ATOM   1206 C  CG    . ARG A 1 174 ? 25.332  -2.405  4.429   1.00 45.57  ?  160 ARG A CG    1 
ATOM   1207 C  CD    . ARG A 1 174 ? 26.209  -2.180  5.643   1.00 36.92  ?  160 ARG A CD    1 
ATOM   1208 N  NE    . ARG A 1 174 ? 27.355  -3.082  5.688   1.00 57.77  ?  160 ARG A NE    1 
ATOM   1209 C  CZ    . ARG A 1 174 ? 28.471  -2.829  6.359   1.00 68.55  ?  160 ARG A CZ    1 
ATOM   1210 N  NH1   . ARG A 1 174 ? 28.637  -1.692  7.023   1.00 54.99  ?  160 ARG A NH1   1 
ATOM   1211 N  NH2   . ARG A 1 174 ? 29.445  -3.735  6.362   1.00 71.84  ?  160 ARG A NH2   1 
ATOM   1212 N  N     . ARG A 1 175 ? 21.411  -0.506  6.827   1.00 30.54  ?  161 ARG A N     1 
ATOM   1213 C  CA    . ARG A 1 175 ? 20.271  0.394   6.944   1.00 31.30  ?  161 ARG A CA    1 
ATOM   1214 C  C     . ARG A 1 175 ? 20.080  0.733   8.418   1.00 33.11  ?  161 ARG A C     1 
ATOM   1215 O  O     . ARG A 1 175 ? 20.620  0.048   9.288   1.00 27.41  ?  161 ARG A O     1 
ATOM   1216 C  CB    . ARG A 1 175 ? 19.008  -0.239  6.344   1.00 33.75  ?  161 ARG A CB    1 
ATOM   1217 C  CG    . ARG A 1 175 ? 18.875  0.021   4.852   1.00 28.78  ?  161 ARG A CG    1 
ATOM   1218 C  CD    . ARG A 1 175 ? 17.571  -0.493  4.300   1.00 29.94  ?  161 ARG A CD    1 
ATOM   1219 N  NE    . ARG A 1 175 ? 17.040  0.393   3.271   1.00 28.30  ?  161 ARG A NE    1 
ATOM   1220 C  CZ    . ARG A 1 175 ? 16.210  0.009   2.312   1.00 27.97  ?  161 ARG A CZ    1 
ATOM   1221 N  NH1   . ARG A 1 175 ? 15.788  -1.243  2.222   1.00 26.17  ?  161 ARG A NH1   1 
ATOM   1222 N  NH2   . ARG A 1 175 ? 15.791  0.904   1.421   1.00 25.13  ?  161 ARG A NH2   1 
ATOM   1223 N  N     . PRO A 1 176 ? 19.331  1.802   8.718   1.00 29.95  ?  162 PRO A N     1 
ATOM   1224 C  CA    . PRO A 1 176 ? 19.236  2.255   10.113  1.00 24.52  ?  162 PRO A CA    1 
ATOM   1225 C  C     . PRO A 1 176 ? 18.504  1.278   11.015  1.00 25.52  ?  162 PRO A C     1 
ATOM   1226 O  O     . PRO A 1 176 ? 17.667  0.482   10.578  1.00 27.23  ?  162 PRO A O     1 
ATOM   1227 C  CB    . PRO A 1 176 ? 18.467  3.583   10.016  1.00 29.58  ?  162 PRO A CB    1 
ATOM   1228 C  CG    . PRO A 1 176 ? 18.372  3.915   8.591   1.00 32.98  ?  162 PRO A CG    1 
ATOM   1229 C  CD    . PRO A 1 176 ? 18.603  2.685   7.796   1.00 27.66  ?  162 PRO A CD    1 
ATOM   1230 N  N     . GLY A 1 177 ? 18.850  1.349   12.305  1.00 27.76  ?  163 GLY A N     1 
ATOM   1231 C  CA    . GLY A 1 177 ? 18.114  0.655   13.337  1.00 27.84  ?  163 GLY A CA    1 
ATOM   1232 C  C     . GLY A 1 177 ? 17.703  1.631   14.426  1.00 31.67  ?  163 GLY A C     1 
ATOM   1233 O  O     . GLY A 1 177 ? 18.114  2.791   14.434  1.00 24.20  ?  163 GLY A O     1 
ATOM   1234 N  N     . TYR A 1 178 ? 16.879  1.139   15.346  1.00 28.20  ?  164 TYR A N     1 
ATOM   1235 C  CA    . TYR A 1 178 ? 16.251  1.982   16.355  1.00 27.04  ?  164 TYR A CA    1 
ATOM   1236 C  C     . TYR A 1 178 ? 16.241  1.241   17.680  1.00 31.75  ?  164 TYR A C     1 
ATOM   1237 O  O     . TYR A 1 178 ? 15.787  0.094   17.749  1.00 30.21  ?  164 TYR A O     1 
ATOM   1238 C  CB    . TYR A 1 178 ? 14.819  2.346   15.926  1.00 28.11  ?  164 TYR A CB    1 
ATOM   1239 C  CG    . TYR A 1 178 ? 13.983  3.150   16.915  1.00 33.21  ?  164 TYR A CG    1 
ATOM   1240 C  CD1   . TYR A 1 178 ? 13.491  2.570   18.084  1.00 31.73  ?  164 TYR A CD1   1 
ATOM   1241 C  CD2   . TYR A 1 178 ? 13.638  4.469   16.648  1.00 27.51  ?  164 TYR A CD2   1 
ATOM   1242 C  CE1   . TYR A 1 178 ? 12.712  3.288   18.974  1.00 32.00  ?  164 TYR A CE1   1 
ATOM   1243 C  CE2   . TYR A 1 178 ? 12.861  5.202   17.536  1.00 29.79  ?  164 TYR A CE2   1 
ATOM   1244 C  CZ    . TYR A 1 178 ? 12.398  4.607   18.695  1.00 36.80  ?  164 TYR A CZ    1 
ATOM   1245 O  OH    . TYR A 1 178 ? 11.619  5.324   19.578  1.00 30.38  ?  164 TYR A OH    1 
ATOM   1246 N  N     . LEU A 1 179 ? 16.699  1.905   18.734  1.00 24.53  ?  165 LEU A N     1 
ATOM   1247 C  CA    . LEU A 1 179 ? 16.658  1.339   20.076  1.00 30.46  ?  165 LEU A CA    1 
ATOM   1248 C  C     . LEU A 1 179 ? 16.005  2.341   21.010  1.00 34.31  ?  165 LEU A C     1 
ATOM   1249 O  O     . LEU A 1 179 ? 16.479  3.474   21.134  1.00 34.35  ?  165 LEU A O     1 
ATOM   1250 C  CB    . LEU A 1 179 ? 18.062  0.997   20.583  1.00 25.11  ?  165 LEU A CB    1 
ATOM   1251 C  CG    . LEU A 1 179 ? 18.846  -0.110  19.885  1.00 28.48  ?  165 LEU A CG    1 
ATOM   1252 C  CD1   . LEU A 1 179 ? 20.229  -0.244  20.517  1.00 25.55  ?  165 LEU A CD1   1 
ATOM   1253 C  CD2   . LEU A 1 179 ? 18.087  -1.415  19.965  1.00 28.11  ?  165 LEU A CD2   1 
ATOM   1254 N  N     . MET A 1 180 ? 14.944  1.920   21.689  1.00 32.93  ?  166 MET A N     1 
ATOM   1255 C  CA    . MET A 1 180 ? 14.385  2.700   22.785  1.00 32.52  ?  166 MET A CA    1 
ATOM   1256 C  C     . MET A 1 180 ? 15.033  2.217   24.072  1.00 30.94  ?  166 MET A C     1 
ATOM   1257 O  O     . MET A 1 180 ? 15.011  1.018   24.372  1.00 32.28  ?  166 MET A O     1 
ATOM   1258 C  CB    . MET A 1 180 ? 12.862  2.569   22.856  1.00 31.41  ?  166 MET A CB    1 
ATOM   1259 C  CG    . MET A 1 180 ? 12.212  3.658   23.707  1.00 38.57  ?  166 MET A CG    1 
ATOM   1260 S  SD    . MET A 1 180 ? 10.757  3.141   24.655  1.00 40.04  ?  166 MET A SD    1 
ATOM   1261 C  CE    . MET A 1 180 ? 9.494   3.349   23.407  1.00 28.59  ?  166 MET A CE    1 
ATOM   1262 N  N     . LEU A 1 181 ? 15.647  3.138   24.811  1.00 30.07  ?  167 LEU A N     1 
ATOM   1263 C  CA    . LEU A 1 181 ? 16.412  2.799   26.007  1.00 33.58  ?  167 LEU A CA    1 
ATOM   1264 C  C     . LEU A 1 181 ? 15.836  3.549   27.200  1.00 28.63  ?  167 LEU A C     1 
ATOM   1265 O  O     . LEU A 1 181 ? 16.238  4.689   27.481  1.00 32.28  ?  167 LEU A O     1 
ATOM   1266 C  CB    . LEU A 1 181 ? 17.893  3.118   25.812  1.00 35.34  ?  167 LEU A CB    1 
ATOM   1267 C  CG    . LEU A 1 181 ? 18.810  2.802   26.995  1.00 39.78  ?  167 LEU A CG    1 
ATOM   1268 C  CD1   . LEU A 1 181 ? 18.830  1.314   27.294  1.00 29.27  ?  167 LEU A CD1   1 
ATOM   1269 C  CD2   . LEU A 1 181 ? 20.208  3.325   26.735  1.00 35.22  ?  167 LEU A CD2   1 
ATOM   1270 N  N     . PRO A 1 182 ? 14.905  2.946   27.939  1.00 37.91  ?  168 PRO A N     1 
ATOM   1271 C  CA    . PRO A 1 182 ? 14.440  3.572   29.182  1.00 34.03  ?  168 PRO A CA    1 
ATOM   1272 C  C     . PRO A 1 182 ? 15.599  3.771   30.145  1.00 36.56  ?  168 PRO A C     1 
ATOM   1273 O  O     . PRO A 1 182 ? 16.521  2.953   30.213  1.00 39.68  ?  168 PRO A O     1 
ATOM   1274 C  CB    . PRO A 1 182 ? 13.416  2.567   29.725  1.00 36.29  ?  168 PRO A CB    1 
ATOM   1275 C  CG    . PRO A 1 182 ? 12.986  1.770   28.527  1.00 31.42  ?  168 PRO A CG    1 
ATOM   1276 C  CD    . PRO A 1 182 ? 14.205  1.679   27.658  1.00 34.86  ?  168 PRO A CD    1 
ATOM   1277 N  N     . ALA A 1 183 ? 15.546  4.877   30.893  1.00 36.40  ?  169 ALA A N     1 
ATOM   1278 C  CA    . ALA A 1 183 ? 16.669  5.247   31.749  1.00 37.78  ?  169 ALA A CA    1 
ATOM   1279 C  C     . ALA A 1 183 ? 16.955  4.173   32.791  1.00 36.04  ?  169 ALA A C     1 
ATOM   1280 O  O     . ALA A 1 183 ? 18.118  3.910   33.116  1.00 38.86  ?  169 ALA A O     1 
ATOM   1281 C  CB    . ALA A 1 183 ? 16.400  6.596   32.420  1.00 42.74  ?  169 ALA A CB    1 
ATOM   1282 N  N     . ASP A 1 184 ? 15.912  3.541   33.331  1.00 37.03  ?  170 ASP A N     1 
ATOM   1283 C  CA    . ASP A 1 184 ? 16.140  2.499   34.328  1.00 42.08  ?  170 ASP A CA    1 
ATOM   1284 C  C     . ASP A 1 184 ? 16.783  1.267   33.698  1.00 39.53  ?  170 ASP A C     1 
ATOM   1285 O  O     . ASP A 1 184 ? 17.614  0.605   34.329  1.00 48.74  ?  170 ASP A O     1 
ATOM   1286 C  CB    . ASP A 1 184 ? 14.828  2.134   35.023  1.00 33.44  ?  170 ASP A CB    1 
ATOM   1287 C  CG    . ASP A 1 184 ? 13.814  1.549   34.070  1.00 42.86  ?  170 ASP A CG    1 
ATOM   1288 O  OD1   . ASP A 1 184 ? 13.743  2.031   32.920  1.00 44.94  ?  170 ASP A OD1   1 
ATOM   1289 O  OD2   . ASP A 1 184 ? 13.085  0.611   34.465  1.00 46.75  ?  170 ASP A OD2   1 
ATOM   1290 N  N     . VAL A 1 185 ? 16.417  0.950   32.453  1.00 36.13  ?  171 VAL A N     1 
ATOM   1291 C  CA    . VAL A 1 185 ? 17.005  -0.195  31.763  1.00 41.68  ?  171 VAL A CA    1 
ATOM   1292 C  C     . VAL A 1 185 ? 18.491  0.033   31.515  1.00 51.05  ?  171 VAL A C     1 
ATOM   1293 O  O     . VAL A 1 185 ? 19.303  -0.898  31.613  1.00 40.90  ?  171 VAL A O     1 
ATOM   1294 C  CB    . VAL A 1 185 ? 16.246  -0.469  30.452  1.00 38.90  ?  171 VAL A CB    1 
ATOM   1295 C  CG1   . VAL A 1 185 ? 16.937  -1.559  29.645  1.00 35.48  ?  171 VAL A CG1   1 
ATOM   1296 C  CG2   . VAL A 1 185 ? 14.802  -0.855  30.745  1.00 38.47  ?  171 VAL A CG2   1 
ATOM   1297 N  N     . ALA A 1 186 ? 18.871  1.276   31.198  1.00 40.38  ?  172 ALA A N     1 
ATOM   1298 C  CA    . ALA A 1 186 ? 20.265  1.584   30.896  1.00 36.59  ?  172 ALA A CA    1 
ATOM   1299 C  C     . ALA A 1 186 ? 21.183  1.287   32.073  1.00 37.92  ?  172 ALA A C     1 
ATOM   1300 O  O     . ALA A 1 186 ? 22.371  1.001   31.875  1.00 42.74  ?  172 ALA A O     1 
ATOM   1301 C  CB    . ALA A 1 186 ? 20.396  3.050   30.482  1.00 28.75  ?  172 ALA A CB    1 
ATOM   1302 N  N     . LYS A 1 187 ? 20.665  1.360   33.296  1.00 40.90  ?  173 LYS A N     1 
ATOM   1303 C  CA    . LYS A 1 187 ? 21.471  1.123   34.487  1.00 44.21  ?  173 LYS A CA    1 
ATOM   1304 C  C     . LYS A 1 187 ? 21.515  -0.342  34.908  1.00 46.65  ?  173 LYS A C     1 
ATOM   1305 O  O     . LYS A 1 187 ? 22.246  -0.674  35.847  1.00 40.94  ?  173 LYS A O     1 
ATOM   1306 C  CB    . LYS A 1 187 ? 20.943  1.967   35.653  1.00 37.25  ?  173 LYS A CB    1 
ATOM   1307 C  CG    . LYS A 1 187 ? 21.258  3.446   35.531  1.00 41.24  ?  173 LYS A CG    1 
ATOM   1308 C  CD    . LYS A 1 187 ? 20.062  4.309   35.897  1.00 59.99  ?  173 LYS A CD    1 
ATOM   1309 C  CE    . LYS A 1 187 ? 20.063  4.659   37.378  1.00 68.72  ?  173 LYS A CE    1 
ATOM   1310 N  NZ    . LYS A 1 187 ? 19.020  5.675   37.708  1.00 74.52  ?  173 LYS A NZ    1 
ATOM   1311 N  N     . LYS A 1 188 ? 20.758  -1.218  34.252  1.00 42.83  ?  174 LYS A N     1 
ATOM   1312 C  CA    . LYS A 1 188 ? 20.711  -2.616  34.660  1.00 37.37  ?  174 LYS A CA    1 
ATOM   1313 C  C     . LYS A 1 188 ? 22.061  -3.295  34.443  1.00 46.81  ?  174 LYS A C     1 
ATOM   1314 O  O     . LYS A 1 188 ? 22.789  -2.978  33.500  1.00 39.54  ?  174 LYS A O     1 
ATOM   1315 C  CB    . LYS A 1 188 ? 19.613  -3.353  33.897  1.00 43.11  ?  174 LYS A CB    1 
ATOM   1316 C  CG    . LYS A 1 188 ? 18.207  -3.061  34.418  1.00 55.90  ?  174 LYS A CG    1 
ATOM   1317 C  CD    . LYS A 1 188 ? 18.161  -3.125  35.941  1.00 53.03  ?  174 LYS A CD    1 
ATOM   1318 C  CE    . LYS A 1 188 ? 16.738  -3.253  36.451  1.00 55.56  ?  174 LYS A CE    1 
ATOM   1319 N  NZ    . LYS A 1 188 ? 15.872  -2.174  35.913  1.00 47.61  ?  174 LYS A NZ    1 
ATOM   1320 N  N     . ALA A 1 189 ? 22.396  -4.222  35.338  1.00 45.06  ?  175 ALA A N     1 
ATOM   1321 C  CA    . ALA A 1 189 ? 23.684  -4.901  35.277  1.00 54.19  ?  175 ALA A CA    1 
ATOM   1322 C  C     . ALA A 1 189 ? 23.833  -5.696  33.985  1.00 44.61  ?  175 ALA A C     1 
ATOM   1323 O  O     . ALA A 1 189 ? 22.876  -6.285  33.479  1.00 45.43  ?  175 ALA A O     1 
ATOM   1324 C  CB    . ALA A 1 189 ? 23.849  -5.835  36.477  1.00 49.92  ?  175 ALA A CB    1 
ATOM   1325 N  N     . ALA A 1 190 ? 25.047  -5.691  33.443  1.00 49.77  ?  176 ALA A N     1 
ATOM   1326 C  CA    . ALA A 1 190 ? 25.393  -6.483  32.274  1.00 41.51  ?  176 ALA A CA    1 
ATOM   1327 C  C     . ALA A 1 190 ? 26.820  -6.985  32.443  1.00 40.89  ?  176 ALA A C     1 
ATOM   1328 O  O     . ALA A 1 190 ? 27.506  -6.658  33.416  1.00 49.00  ?  176 ALA A O     1 
ATOM   1329 C  CB    . ALA A 1 190 ? 25.231  -5.682  30.976  1.00 36.89  ?  176 ALA A CB    1 
ATOM   1330 N  N     . THR A 1 191 ? 27.258  -7.810  31.496  1.00 38.43  ?  177 THR A N     1 
ATOM   1331 C  CA    . THR A 1 191 ? 28.601  -8.358  31.494  1.00 41.29  ?  177 THR A CA    1 
ATOM   1332 C  C     . THR A 1 191 ? 29.293  -8.028  30.179  1.00 43.74  ?  177 THR A C     1 
ATOM   1333 O  O     . THR A 1 191 ? 28.677  -8.159  29.111  1.00 38.48  ?  177 THR A O     1 
ATOM   1334 C  CB    . THR A 1 191 ? 28.581  -9.874  31.704  1.00 52.69  ?  177 THR A CB    1 
ATOM   1335 O  OG1   . THR A 1 191 ? 28.321  -10.524 30.454  1.00 63.41  ?  177 THR A OG1   1 
ATOM   1336 C  CG2   . THR A 1 191 ? 27.506  -10.252 32.705  1.00 48.76  ?  177 THR A CG2   1 
ATOM   1337 N  N     . PRO A 1 192 ? 30.546  -7.586  30.208  1.00 47.60  ?  178 PRO A N     1 
ATOM   1338 C  CA    . PRO A 1 192 ? 31.263  -7.288  28.963  1.00 44.98  ?  178 PRO A CA    1 
ATOM   1339 C  C     . PRO A 1 192 ? 31.398  -8.532  28.106  1.00 48.06  ?  178 PRO A C     1 
ATOM   1340 O  O     . PRO A 1 192 ? 31.742  -9.612  28.609  1.00 47.08  ?  178 PRO A O     1 
ATOM   1341 C  CB    . PRO A 1 192 ? 32.639  -6.797  29.448  1.00 47.80  ?  178 PRO A CB    1 
ATOM   1342 C  CG    . PRO A 1 192 ? 32.457  -6.470  30.901  1.00 51.91  ?  178 PRO A CG    1 
ATOM   1343 C  CD    . PRO A 1 192 ? 31.395  -7.404  31.396  1.00 42.37  ?  178 PRO A CD    1 
ATOM   1344 N  N     . PRO A 1 193 ? 31.116  -8.432  26.810  1.00 47.72  ?  179 PRO A N     1 
ATOM   1345 C  CA    . PRO A 1 193 ? 31.237  -9.612  25.946  1.00 47.87  ?  179 PRO A CA    1 
ATOM   1346 C  C     . PRO A 1 193 ? 32.700  -9.947  25.688  1.00 57.08  ?  179 PRO A C     1 
ATOM   1347 O  O     . PRO A 1 193 ? 33.545  -9.060  25.541  1.00 48.66  ?  179 PRO A O     1 
ATOM   1348 C  CB    . PRO A 1 193 ? 30.514  -9.199  24.658  1.00 42.26  ?  179 PRO A CB    1 
ATOM   1349 C  CG    . PRO A 1 193 ? 30.186  -7.728  24.801  1.00 43.27  ?  179 PRO A CG    1 
ATOM   1350 C  CD    . PRO A 1 193 ? 30.799  -7.208  26.059  1.00 43.10  ?  179 PRO A CD    1 
ATOM   1351 N  N     . VAL A 1 194 ? 32.995  -11.248 25.648  1.00 52.61  ?  180 VAL A N     1 
ATOM   1352 C  CA    . VAL A 1 194 ? 34.356  -11.686 25.353  1.00 52.73  ?  180 VAL A CA    1 
ATOM   1353 C  C     . VAL A 1 194 ? 34.705  -11.406 23.899  1.00 56.28  ?  180 VAL A C     1 
ATOM   1354 O  O     . VAL A 1 194 ? 35.831  -11.007 23.581  1.00 71.91  ?  180 VAL A O     1 
ATOM   1355 C  CB    . VAL A 1 194 ? 34.522  -13.183 25.683  1.00 57.71  ?  180 VAL A CB    1 
ATOM   1356 C  CG1   . VAL A 1 194 ? 35.866  -13.687 25.196  1.00 58.02  ?  180 VAL A CG1   1 
ATOM   1357 C  CG2   . VAL A 1 194 ? 34.388  -13.427 27.169  1.00 49.98  ?  180 VAL A CG2   1 
ATOM   1358 N  N     . ASN A 1 195 ? 33.754  -11.613 22.995  1.00 53.21  ?  181 ASN A N     1 
ATOM   1359 C  CA    . ASN A 1 195 ? 33.982  -11.487 21.564  1.00 54.28  ?  181 ASN A CA    1 
ATOM   1360 C  C     . ASN A 1 195 ? 33.224  -10.291 21.010  1.00 60.23  ?  181 ASN A C     1 
ATOM   1361 O  O     . ASN A 1 195 ? 32.046  -10.089 21.326  1.00 55.06  ?  181 ASN A O     1 
ATOM   1362 C  CB    . ASN A 1 195 ? 33.581  -12.768 20.833  1.00 60.91  ?  181 ASN A CB    1 
ATOM   1363 C  CG    . ASN A 1 195 ? 34.666  -13.826 20.893  1.00 65.13  ?  181 ASN A CG    1 
ATOM   1364 O  OD1   . ASN A 1 195 ? 34.799  -14.532 21.891  1.00 68.96  ?  181 ASN A OD1   1 
ATOM   1365 N  ND2   . ASN A 1 195 ? 35.459  -13.929 19.831  1.00 67.42  ?  181 ASN A ND2   1 
ATOM   1366 N  N     . ALA A 1 196 ? 33.905  -9.504  20.187  1.00 47.95  ?  182 ALA A N     1 
ATOM   1367 C  CA    . ALA A 1 196 ? 33.284  -8.355  19.557  1.00 51.03  ?  182 ALA A CA    1 
ATOM   1368 C  C     . ALA A 1 196 ? 32.217  -8.796  18.561  1.00 66.22  ?  182 ALA A C     1 
ATOM   1369 O  O     . ALA A 1 196 ? 32.323  -9.850  17.924  1.00 50.95  ?  182 ALA A O     1 
ATOM   1370 C  CB    . ALA A 1 196 ? 34.339  -7.504  18.853  1.00 56.91  ?  182 ALA A CB    1 
ATOM   1371 N  N     . LEU A 1 197 ? 31.160  -7.990  18.466  1.00 55.83  ?  183 LEU A N     1 
ATOM   1372 C  CA    . LEU A 1 197 ? 30.095  -8.248  17.508  1.00 44.99  ?  183 LEU A CA    1 
ATOM   1373 C  C     . LEU A 1 197 ? 30.660  -8.261  16.096  1.00 55.67  ?  183 LEU A C     1 
ATOM   1374 O  O     . LEU A 1 197 ? 31.329  -7.312  15.674  1.00 60.37  ?  183 LEU A O     1 
ATOM   1375 C  CB    . LEU A 1 197 ? 29.010  -7.179  17.627  1.00 44.10  ?  183 LEU A CB    1 
ATOM   1376 C  CG    . LEU A 1 197 ? 27.579  -7.552  17.245  1.00 47.71  ?  183 LEU A CG    1 
ATOM   1377 C  CD1   . LEU A 1 197 ? 27.015  -8.605  18.183  1.00 42.17  ?  183 LEU A CD1   1 
ATOM   1378 C  CD2   . LEU A 1 197 ? 26.704  -6.303  17.218  1.00 39.38  ?  183 LEU A CD2   1 
ATOM   1379 N  N     . THR A 1 198 ? 30.383  -9.336  15.362  1.00 61.38  ?  184 THR A N     1 
ATOM   1380 C  CA    . THR A 1 198 ? 30.858  -9.475  13.994  1.00 67.24  ?  184 THR A CA    1 
ATOM   1381 C  C     . THR A 1 198 ? 29.760  -10.068 13.127  1.00 68.83  ?  184 THR A C     1 
ATOM   1382 O  O     . THR A 1 198 ? 28.888  -10.794 13.611  1.00 71.80  ?  184 THR A O     1 
ATOM   1383 C  CB    . THR A 1 198 ? 32.114  -10.353 13.928  1.00 67.40  ?  184 THR A CB    1 
ATOM   1384 O  OG1   . THR A 1 198 ? 32.355  -10.747 12.572  1.00 86.48  ?  184 THR A OG1   1 
ATOM   1385 C  CG2   . THR A 1 198 ? 31.941  -11.591 14.795  1.00 70.56  ?  184 THR A CG2   1 
ATOM   1386 N  N     . LEU A 1 199 ? 29.822  -9.759  11.829  1.00 70.94  ?  185 LEU A N     1 
ATOM   1387 C  CA    . LEU A 1 199 ? 28.788  -10.162 10.882  1.00 77.13  ?  185 LEU A CA    1 
ATOM   1388 C  C     . LEU A 1 199 ? 29.068  -11.530 10.269  1.00 76.26  ?  185 LEU A C     1 
ATOM   1389 O  O     . LEU A 1 199 ? 28.144  -12.343 10.150  1.00 85.24  ?  185 LEU A O     1 
ATOM   1390 C  CB    . LEU A 1 199 ? 28.630  -9.102  9.785   1.00 83.84  ?  185 LEU A CB    1 
ATOM   1391 C  CG    . LEU A 1 199 ? 27.491  -9.303  8.777   1.00 72.45  ?  185 LEU A CG    1 
ATOM   1392 C  CD1   . LEU A 1 199 ? 26.151  -9.367  9.489   1.00 59.48  ?  185 LEU A CD1   1 
ATOM   1393 C  CD2   . LEU A 1 199 ? 27.484  -8.191  7.728   1.00 54.87  ?  185 LEU A CD2   1 
ATOM   1394 N  N     . ARG A 1 200 ? 30.316  -11.799 9.869   1.00 83.13  ?  186 ARG A N     1 
ATOM   1395 C  CA    . ARG A 1 200 ? 30.675  -13.116 9.343   1.00 96.88  ?  186 ARG A CA    1 
ATOM   1396 C  C     . ARG A 1 200 ? 29.873  -13.484 8.099   1.00 91.49  ?  186 ARG A C     1 
ATOM   1397 O  O     . ARG A 1 200 ? 28.910  -14.254 8.190   1.00 96.90  ?  186 ARG A O     1 
ATOM   1398 C  CB    . ARG A 1 200 ? 30.526  -14.187 10.428  1.00 101.11 ?  186 ARG A CB    1 
ATOM   1399 C  CG    . ARG A 1 200 ? 31.691  -14.204 11.412  1.00 89.93  ?  186 ARG A CG    1 
ATOM   1400 C  CD    . ARG A 1 200 ? 31.237  -14.557 12.817  1.00 94.92  ?  186 ARG A CD    1 
ATOM   1401 N  NE    . ARG A 1 200 ? 31.735  -15.861 13.236  1.00 102.89 ?  186 ARG A NE    1 
ATOM   1402 C  CZ    . ARG A 1 200 ? 31.280  -16.536 14.282  1.00 101.65 ?  186 ARG A CZ    1 
ATOM   1403 N  NH1   . ARG A 1 200 ? 30.305  -16.061 15.041  1.00 92.84  ?  186 ARG A NH1   1 
ATOM   1404 N  NH2   . ARG A 1 200 ? 31.818  -17.717 14.576  1.00 93.59  ?  186 ARG A NH2   1 
ATOM   1405 N  N     . HIS A 1 201 ? 30.241  -12.897 6.953   1.00 77.66  ?  187 HIS A N     1 
ATOM   1406 C  CA    . HIS A 1 201 ? 29.513  -12.992 5.687   1.00 81.95  ?  187 HIS A CA    1 
ATOM   1407 C  C     . HIS A 1 201 ? 28.826  -14.330 5.448   1.00 82.18  ?  187 HIS A C     1 
ATOM   1408 O  O     . HIS A 1 201 ? 29.417  -15.394 5.660   1.00 70.50  ?  187 HIS A O     1 
ATOM   1409 C  CB    . HIS A 1 201 ? 30.465  -12.786 4.500   1.00 75.24  ?  187 HIS A CB    1 
ATOM   1410 C  CG    . HIS A 1 201 ? 31.226  -11.499 4.524   1.00 91.08  ?  187 HIS A CG    1 
ATOM   1411 N  ND1   . HIS A 1 201 ? 30.666  -10.295 4.154   1.00 84.25  ?  187 HIS A ND1   1 
ATOM   1412 C  CD2   . HIS A 1 201 ? 32.518  -11.236 4.832   1.00 78.84  ?  187 HIS A CD2   1 
ATOM   1413 C  CE1   . HIS A 1 201 ? 31.575  -9.341  4.255   1.00 90.38  ?  187 HIS A CE1   1 
ATOM   1414 N  NE2   . HIS A 1 201 ? 32.707  -9.886  4.664   1.00 91.99  ?  187 HIS A NE2   1 
ATOM   1415 N  N     . ALA A 1 202 ? 27.578  -14.277 4.994   1.00 68.93  ?  188 ALA A N     1 
ATOM   1416 C  CA    . ALA A 1 202 ? 26.848  -15.487 4.675   1.00 69.65  ?  188 ALA A CA    1 
ATOM   1417 C  C     . ALA A 1 202 ? 27.307  -16.015 3.320   1.00 61.37  ?  188 ALA A C     1 
ATOM   1418 O  O     . ALA A 1 202 ? 28.042  -15.354 2.578   1.00 58.11  ?  188 ALA A O     1 
ATOM   1419 C  CB    . ALA A 1 202 ? 25.342  -15.231 4.674   1.00 65.68  ?  188 ALA A CB    1 
ATOM   1420 N  N     . HIS A 1 203 ? 26.882  -17.228 3.003   1.00 53.32  ?  189 HIS A N     1 
ATOM   1421 C  CA    . HIS A 1 203 ? 27.248  -17.863 1.750   1.00 44.99  ?  189 HIS A CA    1 
ATOM   1422 C  C     . HIS A 1 203 ? 25.997  -18.361 1.050   1.00 41.71  ?  189 HIS A C     1 
ATOM   1423 O  O     . HIS A 1 203 ? 25.076  -18.872 1.693   1.00 42.32  ?  189 HIS A O     1 
ATOM   1424 C  CB    . HIS A 1 203 ? 28.230  -19.016 1.982   1.00 41.69  ?  189 HIS A CB    1 
ATOM   1425 C  CG    . HIS A 1 203 ? 29.422  -18.633 2.803   1.00 72.08  ?  189 HIS A CG    1 
ATOM   1426 N  ND1   . HIS A 1 203 ? 30.609  -18.209 2.243   1.00 75.54  ?  189 HIS A ND1   1 
ATOM   1427 C  CD2   . HIS A 1 203 ? 29.604  -18.592 4.144   1.00 76.83  ?  189 HIS A CD2   1 
ATOM   1428 C  CE1   . HIS A 1 203 ? 31.474  -17.936 3.203   1.00 70.62  ?  189 HIS A CE1   1 
ATOM   1429 N  NE2   . HIS A 1 203 ? 30.889  -18.159 4.367   1.00 80.66  ?  189 HIS A NE2   1 
ATOM   1430 N  N     . ALA A 1 204 ? 25.953  -18.175 -0.264  1.00 40.29  ?  190 ALA A N     1 
ATOM   1431 C  CA    . ALA A 1 204 ? 24.872  -18.737 -1.052  1.00 40.36  ?  190 ALA A CA    1 
ATOM   1432 C  C     . ALA A 1 204 ? 24.942  -20.257 -1.016  1.00 38.20  ?  190 ALA A C     1 
ATOM   1433 O  O     . ALA A 1 204 ? 26.017  -20.845 -0.880  1.00 40.09  ?  190 ALA A O     1 
ATOM   1434 C  CB    . ALA A 1 204 ? 24.950  -18.249 -2.498  1.00 41.28  ?  190 ALA A CB    1 
ATOM   1435 N  N     . ASP A 1 205 ? 23.778  -20.893 -1.106  1.00 38.48  ?  191 ASP A N     1 
ATOM   1436 C  CA    . ASP A 1 205 ? 23.733  -22.324 -1.373  1.00 39.00  ?  191 ASP A CA    1 
ATOM   1437 C  C     . ASP A 1 205 ? 24.538  -22.607 -2.633  1.00 40.20  ?  191 ASP A C     1 
ATOM   1438 O  O     . ASP A 1 205 ? 24.413  -21.888 -3.625  1.00 39.93  ?  191 ASP A O     1 
ATOM   1439 C  CB    . ASP A 1 205 ? 22.277  -22.773 -1.538  1.00 37.92  ?  191 ASP A CB    1 
ATOM   1440 C  CG    . ASP A 1 205 ? 22.121  -24.282 -1.555  1.00 39.54  ?  191 ASP A CG    1 
ATOM   1441 O  OD1   . ASP A 1 205 ? 22.346  -24.895 -2.622  1.00 40.34  ?  191 ASP A OD1   1 
ATOM   1442 O  OD2   . ASP A 1 205 ? 21.771  -24.855 -0.499  1.00 40.11  ?  191 ASP A OD2   1 
ATOM   1443 N  N     . SER A 1 206 ? 25.401  -23.629 -2.582  1.00 37.09  ?  192 SER A N     1 
ATOM   1444 C  CA    . SER A 1 206 ? 26.359  -23.803 -3.671  1.00 38.26  ?  192 SER A CA    1 
ATOM   1445 C  C     . SER A 1 206 ? 25.665  -24.138 -4.987  1.00 38.13  ?  192 SER A C     1 
ATOM   1446 O  O     . SER A 1 206 ? 26.133  -23.725 -6.055  1.00 39.42  ?  192 SER A O     1 
ATOM   1447 C  CB    . SER A 1 206 ? 27.403  -24.863 -3.311  1.00 35.35  ?  192 SER A CB    1 
ATOM   1448 O  OG    . SER A 1 206 ? 26.823  -26.035 -2.775  1.00 39.54  ?  192 SER A OG    1 
ATOM   1449 N  N     . ALA A 1 207 ? 24.543  -24.861 -4.936  1.00 40.67  ?  193 ALA A N     1 
ATOM   1450 C  CA    . ALA A 1 207 ? 23.767  -25.103 -6.151  1.00 35.86  ?  193 ALA A CA    1 
ATOM   1451 C  C     . ALA A 1 207 ? 23.140  -23.810 -6.668  1.00 33.03  ?  193 ALA A C     1 
ATOM   1452 O  O     . ALA A 1 207 ? 23.096  -23.575 -7.882  1.00 32.88  ?  193 ALA A O     1 
ATOM   1453 C  CB    . ALA A 1 207 ? 22.692  -26.158 -5.886  1.00 34.89  ?  193 ALA A CB    1 
ATOM   1454 N  N     . CYS A 1 208 ? 22.649  -22.960 -5.763  1.00 32.34  ?  194 CYS A N     1 
ATOM   1455 C  CA    . CYS A 1 208 ? 22.092  -21.675 -6.174  1.00 35.48  ?  194 CYS A CA    1 
ATOM   1456 C  C     . CYS A 1 208 ? 23.154  -20.794 -6.824  1.00 36.12  ?  194 CYS A C     1 
ATOM   1457 O  O     . CYS A 1 208 ? 22.915  -20.179 -7.871  1.00 37.96  ?  194 CYS A O     1 
ATOM   1458 C  CB    . CYS A 1 208 ? 21.477  -20.964 -4.969  1.00 36.56  ?  194 CYS A CB    1 
ATOM   1459 S  SG    . CYS A 1 208 ? 20.823  -19.317 -5.342  1.00 53.69  ?  194 CYS A SG    1 
ATOM   1460 N  N     . LEU A 1 209 ? 24.339  -20.720 -6.216  1.00 44.92  ?  195 LEU A N     1 
ATOM   1461 C  CA    . LEU A 1 209 ? 25.419  -19.938 -6.812  1.00 34.37  ?  195 LEU A CA    1 
ATOM   1462 C  C     . LEU A 1 209 ? 25.831  -20.512 -8.160  1.00 34.45  ?  195 LEU A C     1 
ATOM   1463 O  O     . LEU A 1 209 ? 26.041  -19.765 -9.122  1.00 39.72  ?  195 LEU A O     1 
ATOM   1464 C  CB    . LEU A 1 209 ? 26.620  -19.882 -5.868  1.00 42.38  ?  195 LEU A CB    1 
ATOM   1465 C  CG    . LEU A 1 209 ? 27.750  -18.928 -6.280  1.00 33.72  ?  195 LEU A CG    1 
ATOM   1466 C  CD1   . LEU A 1 209 ? 27.266  -17.488 -6.297  1.00 29.87  ?  195 LEU A CD1   1 
ATOM   1467 C  CD2   . LEU A 1 209 ? 28.952  -19.081 -5.356  1.00 42.52  ?  195 LEU A CD2   1 
ATOM   1468 N  N     . LYS A 1 210 ? 25.925  -21.842 -8.255  1.00 36.29  ?  196 LYS A N     1 
ATOM   1469 C  CA    . LYS A 1 210 ? 26.298  -22.473 -9.516  1.00 32.95  ?  196 LYS A CA    1 
ATOM   1470 C  C     . LYS A 1 210 ? 25.291  -22.162 -10.616 1.00 32.64  ?  196 LYS A C     1 
ATOM   1471 O  O     . LYS A 1 210 ? 25.676  -21.918 -11.767 1.00 37.44  ?  196 LYS A O     1 
ATOM   1472 C  CB    . LYS A 1 210 ? 26.434  -23.985 -9.328  1.00 37.97  ?  196 LYS A CB    1 
ATOM   1473 C  CG    . LYS A 1 210 ? 26.736  -24.740 -10.612 1.00 43.57  ?  196 LYS A CG    1 
ATOM   1474 C  CD    . LYS A 1 210 ? 28.214  -25.060 -10.731 1.00 62.89  ?  196 LYS A CD    1 
ATOM   1475 C  CE    . LYS A 1 210 ? 28.558  -25.614 -12.107 1.00 56.00  ?  196 LYS A CE    1 
ATOM   1476 N  NZ    . LYS A 1 210 ? 29.269  -24.610 -12.943 1.00 56.09  ?  196 LYS A NZ    1 
ATOM   1477 N  N     . ALA A 1 211 ? 23.996  -22.163 -10.286 1.00 33.55  ?  197 ALA A N     1 
ATOM   1478 C  CA    . ALA A 1 211 ? 22.985  -21.832 -11.286 1.00 35.18  ?  197 ALA A CA    1 
ATOM   1479 C  C     . ALA A 1 211 ? 23.181  -20.417 -11.817 1.00 32.68  ?  197 ALA A C     1 
ATOM   1480 O  O     . ALA A 1 211 ? 23.128  -20.187 -13.029 1.00 36.77  ?  197 ALA A O     1 
ATOM   1481 C  CB    . ALA A 1 211 ? 21.582  -21.996 -10.694 1.00 31.96  ?  197 ALA A CB    1 
ATOM   1482 N  N     . PHE A 1 212 ? 23.420  -19.453 -10.923 1.00 30.47  ?  198 PHE A N     1 
ATOM   1483 C  CA    . PHE A 1 212 ? 23.703  -18.092 -11.374 1.00 30.25  ?  198 PHE A CA    1 
ATOM   1484 C  C     . PHE A 1 212 ? 24.980  -18.043 -12.202 1.00 30.24  ?  198 PHE A C     1 
ATOM   1485 O  O     . PHE A 1 212 ? 25.017  -17.407 -13.262 1.00 30.21  ?  198 PHE A O     1 
ATOM   1486 C  CB    . PHE A 1 212 ? 23.811  -17.145 -10.178 1.00 30.46  ?  198 PHE A CB    1 
ATOM   1487 C  CG    . PHE A 1 212 ? 24.470  -15.820 -10.501 1.00 38.38  ?  198 PHE A CG    1 
ATOM   1488 C  CD1   . PHE A 1 212 ? 23.841  -14.897 -11.320 1.00 32.46  ?  198 PHE A CD1   1 
ATOM   1489 C  CD2   . PHE A 1 212 ? 25.718  -15.502 -9.980  1.00 29.52  ?  198 PHE A CD2   1 
ATOM   1490 C  CE1   . PHE A 1 212 ? 24.446  -13.686 -11.615 1.00 31.26  ?  198 PHE A CE1   1 
ATOM   1491 C  CE2   . PHE A 1 212 ? 26.329  -14.291 -10.270 1.00 33.27  ?  198 PHE A CE2   1 
ATOM   1492 C  CZ    . PHE A 1 212 ? 25.690  -13.381 -11.089 1.00 30.38  ?  198 PHE A CZ    1 
ATOM   1493 N  N     . ARG A 1 213 ? 26.026  -18.738 -11.748 1.00 32.62  ?  199 ARG A N     1 
ATOM   1494 C  CA    . ARG A 1 213 ? 27.295  -18.737 -12.471 1.00 33.62  ?  199 ARG A CA    1 
ATOM   1495 C  C     . ARG A 1 213 ? 27.128  -19.284 -13.880 1.00 37.75  ?  199 ARG A C     1 
ATOM   1496 O  O     . ARG A 1 213 ? 27.661  -18.716 -14.841 1.00 41.69  ?  199 ARG A O     1 
ATOM   1497 C  CB    . ARG A 1 213 ? 28.335  -19.554 -11.702 1.00 33.40  ?  199 ARG A CB    1 
ATOM   1498 C  CG    . ARG A 1 213 ? 29.716  -19.548 -12.332 1.00 36.88  ?  199 ARG A CG    1 
ATOM   1499 C  CD    . ARG A 1 213 ? 30.662  -20.502 -11.619 1.00 41.39  ?  199 ARG A CD    1 
ATOM   1500 N  NE    . ARG A 1 213 ? 32.049  -20.059 -11.725 1.00 55.80  ?  199 ARG A NE    1 
ATOM   1501 C  CZ    . ARG A 1 213 ? 32.829  -20.289 -12.771 1.00 61.84  ?  199 ARG A CZ    1 
ATOM   1502 N  NH1   . ARG A 1 213 ? 32.396  -20.969 -13.820 1.00 72.64  ?  199 ARG A NH1   1 
ATOM   1503 N  NH2   . ARG A 1 213 ? 34.075  -19.824 -12.767 1.00 62.57  ?  199 ARG A NH2   1 
ATOM   1504 N  N     . ASP A 1 214 ? 26.391  -20.390 -14.024 1.00 34.36  ?  200 ASP A N     1 
ATOM   1505 C  CA    . ASP A 1 214 ? 26.185  -20.981 -15.342 1.00 34.66  ?  200 ASP A CA    1 
ATOM   1506 C  C     . ASP A 1 214 ? 25.424  -20.033 -16.266 1.00 33.64  ?  200 ASP A C     1 
ATOM   1507 O  O     . ASP A 1 214 ? 25.753  -19.910 -17.451 1.00 36.75  ?  200 ASP A O     1 
ATOM   1508 C  CB    . ASP A 1 214 ? 25.437  -22.311 -15.208 1.00 42.45  ?  200 ASP A CB    1 
ATOM   1509 C  CG    . ASP A 1 214 ? 26.260  -23.382 -14.496 1.00 47.63  ?  200 ASP A CG    1 
ATOM   1510 O  OD1   . ASP A 1 214 ? 27.505  -23.270 -14.478 1.00 48.67  ?  200 ASP A OD1   1 
ATOM   1511 O  OD2   . ASP A 1 214 ? 25.661  -24.339 -13.959 1.00 44.81  ?  200 ASP A OD2   1 
ATOM   1512 N  N     . ALA A 1 215 ? 24.395  -19.361 -15.746 1.00 32.32  ?  201 ALA A N     1 
ATOM   1513 C  CA    . ALA A 1 215 ? 23.637  -18.426 -16.571 1.00 37.15  ?  201 ALA A CA    1 
ATOM   1514 C  C     . ALA A 1 215 ? 24.469  -17.201 -16.938 1.00 38.01  ?  201 ALA A C     1 
ATOM   1515 O  O     . ALA A 1 215 ? 24.447  -16.751 -18.090 1.00 46.37  ?  201 ALA A O     1 
ATOM   1516 C  CB    . ALA A 1 215 ? 22.356  -18.009 -15.850 1.00 31.25  ?  201 ALA A CB    1 
ATOM   1517 N  N     . ALA A 1 216 ? 25.223  -16.659 -15.981 1.00 32.16  ?  202 ALA A N     1 
ATOM   1518 C  CA    . ALA A 1 216 ? 26.063  -15.504 -16.282 1.00 36.93  ?  202 ALA A CA    1 
ATOM   1519 C  C     . ALA A 1 216 ? 27.180  -15.860 -17.257 1.00 36.72  ?  202 ALA A C     1 
ATOM   1520 O  O     . ALA A 1 216 ? 27.498  -15.072 -18.155 1.00 41.28  ?  202 ALA A O     1 
ATOM   1521 C  CB    . ALA A 1 216 ? 26.644  -14.932 -14.991 1.00 39.47  ?  202 ALA A CB    1 
ATOM   1522 N  N     . GLU A 1 217 ? 27.780  -17.044 -17.104 1.00 34.23  ?  203 GLU A N     1 
ATOM   1523 C  CA    . GLU A 1 217 ? 28.839  -17.459 -18.021 1.00 43.34  ?  203 GLU A CA    1 
ATOM   1524 C  C     . GLU A 1 217 ? 28.326  -17.589 -19.449 1.00 40.69  ?  203 GLU A C     1 
ATOM   1525 O  O     . GLU A 1 217 ? 28.984  -17.142 -20.394 1.00 44.80  ?  203 GLU A O     1 
ATOM   1526 C  CB    . GLU A 1 217 ? 29.456  -18.777 -17.566 1.00 38.08  ?  203 GLU A CB    1 
ATOM   1527 C  CG    . GLU A 1 217 ? 30.283  -19.449 -18.645 1.00 47.02  ?  203 GLU A CG    1 
ATOM   1528 C  CD    . GLU A 1 217 ? 31.310  -20.396 -18.075 1.00 54.91  ?  203 GLU A CD    1 
ATOM   1529 O  OE1   . GLU A 1 217 ? 30.917  -21.263 -17.264 1.00 58.99  ?  203 GLU A OE1   1 
ATOM   1530 O  OE2   . GLU A 1 217 ? 32.503  -20.278 -18.439 1.00 58.30  ?  203 GLU A OE2   1 
ATOM   1531 N  N     . ASN A 1 218 ? 27.152  -18.201 -19.627 1.00 45.86  ?  204 ASN A N     1 
ATOM   1532 C  CA    . ASN A 1 218 ? 26.586  -18.328 -20.966 1.00 47.85  ?  204 ASN A CA    1 
ATOM   1533 C  C     . ASN A 1 218 ? 26.370  -16.956 -21.588 1.00 46.71  ?  204 ASN A C     1 
ATOM   1534 O  O     . ASN A 1 218 ? 26.700  -16.731 -22.757 1.00 58.25  ?  204 ASN A O     1 
ATOM   1535 C  CB    . ASN A 1 218 ? 25.277  -19.113 -20.915 1.00 41.92  ?  204 ASN A CB    1 
ATOM   1536 C  CG    . ASN A 1 218 ? 25.506  -20.604 -20.895 1.00 63.88  ?  204 ASN A CG    1 
ATOM   1537 O  OD1   . ASN A 1 218 ? 24.680  -21.365 -20.393 1.00 82.33  ?  204 ASN A OD1   1 
ATOM   1538 N  ND2   . ASN A 1 218 ? 26.642  -21.035 -21.437 1.00 69.71  ?  204 ASN A ND2   1 
ATOM   1539 N  N     . ARG A 1 219 ? 25.785  -16.034 -20.824 1.00 46.60  ?  205 ARG A N     1 
ATOM   1540 C  CA    . ARG A 1 219 ? 25.517  -14.699 -21.343 1.00 41.99  ?  205 ARG A CA    1 
ATOM   1541 C  C     . ARG A 1 219 ? 26.814  -13.973 -21.688 1.00 46.37  ?  205 ARG A C     1 
ATOM   1542 O  O     . ARG A 1 219 ? 26.933  -13.360 -22.755 1.00 57.31  ?  205 ARG A O     1 
ATOM   1543 C  CB    . ARG A 1 219 ? 24.708  -13.903 -20.323 1.00 39.13  ?  205 ARG A CB    1 
ATOM   1544 C  CG    . ARG A 1 219 ? 24.285  -12.534 -20.814 1.00 43.99  ?  205 ARG A CG    1 
ATOM   1545 C  CD    . ARG A 1 219 ? 23.479  -12.647 -22.092 1.00 47.99  ?  205 ARG A CD    1 
ATOM   1546 N  NE    . ARG A 1 219 ? 23.135  -11.339 -22.638 1.00 46.58  ?  205 ARG A NE    1 
ATOM   1547 C  CZ    . ARG A 1 219 ? 23.971  -10.575 -23.324 1.00 48.38  ?  205 ARG A CZ    1 
ATOM   1548 N  NH1   . ARG A 1 219 ? 25.209  -10.966 -23.586 1.00 50.78  ?  205 ARG A NH1   1 
ATOM   1549 N  NH2   . ARG A 1 219 ? 23.553  -9.394  -23.768 1.00 50.66  ?  205 ARG A NH2   1 
ATOM   1550 N  N     . LEU A 1 220 ? 27.804  -14.035 -20.794 1.00 42.14  ?  206 LEU A N     1 
ATOM   1551 C  CA    . LEU A 1 220 ? 29.071  -13.355 -21.042 1.00 41.18  ?  206 LEU A CA    1 
ATOM   1552 C  C     . LEU A 1 220 ? 29.876  -14.017 -22.153 1.00 40.78  ?  206 LEU A C     1 
ATOM   1553 O  O     . LEU A 1 220 ? 30.651  -13.340 -22.835 1.00 46.65  ?  206 LEU A O     1 
ATOM   1554 C  CB    . LEU A 1 220 ? 29.899  -13.302 -19.759 1.00 37.04  ?  206 LEU A CB    1 
ATOM   1555 C  CG    . LEU A 1 220 ? 29.474  -12.250 -18.727 1.00 43.18  ?  206 LEU A CG    1 
ATOM   1556 C  CD1   . LEU A 1 220 ? 30.106  -12.540 -17.377 1.00 41.08  ?  206 LEU A CD1   1 
ATOM   1557 C  CD2   . LEU A 1 220 ? 29.824  -10.839 -19.195 1.00 34.78  ?  206 LEU A CD2   1 
ATOM   1558 N  N     . ALA A 1 221 ? 29.708  -15.326 -22.356 1.00 37.91  ?  207 ALA A N     1 
ATOM   1559 C  CA    . ALA A 1 221 ? 30.514  -16.025 -23.353 1.00 46.26  ?  207 ALA A CA    1 
ATOM   1560 C  C     . ALA A 1 221 ? 30.240  -15.519 -24.763 1.00 41.25  ?  207 ALA A C     1 
ATOM   1561 O  O     . ALA A 1 221 ? 31.147  -15.512 -25.604 1.00 58.00  ?  207 ALA A O     1 
ATOM   1562 C  CB    . ALA A 1 221 ? 30.272  -17.534 -23.272 1.00 42.57  ?  207 ALA A CB    1 
ATOM   1563 N  N     . MET A 1 222 ? 29.002  -15.115 -25.051 1.00 53.62  ?  208 MET A N     1 
ATOM   1564 C  CA    . MET A 1 222 ? 28.641  -14.549 -26.345 1.00 63.38  ?  208 MET A CA    1 
ATOM   1565 C  C     . MET A 1 222 ? 28.531  -13.029 -26.325 1.00 55.44  ?  208 MET A C     1 
ATOM   1566 O  O     . MET A 1 222 ? 27.958  -12.441 -27.249 1.00 52.58  ?  208 MET A O     1 
ATOM   1567 C  CB    . MET A 1 222 ? 27.346  -15.180 -26.849 1.00 65.46  ?  208 MET A CB    1 
ATOM   1568 C  CG    . MET A 1 222 ? 26.094  -14.738 -26.139 1.00 64.09  ?  208 MET A CG    1 
ATOM   1569 S  SD    . MET A 1 222 ? 24.926  -16.120 -26.274 1.00 96.85  ?  208 MET A SD    1 
ATOM   1570 C  CE    . MET A 1 222 ? 23.412  -15.363 -25.672 1.00 64.52  ?  208 MET A CE    1 
ATOM   1571 N  N     . SER A 1 223 ? 29.082  -12.385 -25.305 1.00 51.55  ?  209 SER A N     1 
ATOM   1572 C  CA    . SER A 1 223 ? 29.109  -10.933 -25.251 1.00 49.75  ?  209 SER A CA    1 
ATOM   1573 C  C     . SER A 1 223 ? 30.254  -10.439 -26.125 1.00 56.20  ?  209 SER A C     1 
ATOM   1574 O  O     . SER A 1 223 ? 31.404  -10.856 -25.948 1.00 63.10  ?  209 SER A O     1 
ATOM   1575 C  CB    . SER A 1 223 ? 29.282  -10.455 -23.814 1.00 53.57  ?  209 SER A CB    1 
ATOM   1576 O  OG    . SER A 1 223 ? 29.558  -9.066  -23.765 1.00 63.03  ?  209 SER A OG    1 
ATOM   1577 N  N     . LYS A 1 224 ? 29.943  -9.567  -27.085 1.00 54.14  ?  210 LYS A N     1 
ATOM   1578 C  CA    . LYS A 1 224 ? 30.986  -9.001  -27.934 1.00 52.07  ?  210 LYS A CA    1 
ATOM   1579 C  C     . LYS A 1 224 ? 31.713  -7.871  -27.213 1.00 62.18  ?  210 LYS A C     1 
ATOM   1580 O  O     . LYS A 1 224 ? 32.942  -7.887  -27.089 1.00 64.51  ?  210 LYS A O     1 
ATOM   1581 C  CB    . LYS A 1 224 ? 30.375  -8.524  -29.253 1.00 54.31  ?  210 LYS A CB    1 
ATOM   1582 C  CG    . LYS A 1 224 ? 31.343  -8.488  -30.425 1.00 73.48  ?  210 LYS A CG    1 
ATOM   1583 C  CD    . LYS A 1 224 ? 30.598  -8.329  -31.746 1.00 72.58  ?  210 LYS A CD    1 
ATOM   1584 C  CE    . LYS A 1 224 ? 30.804  -6.926  -32.318 1.00 79.94  ?  210 LYS A CE    1 
ATOM   1585 N  NZ    . LYS A 1 224 ? 31.161  -6.929  -33.771 1.00 73.79  ?  210 LYS A NZ    1 
ATOM   1586 N  N     . ARG A 1 225 ? 30.968  -6.873  -26.741 1.00 54.38  ?  211 ARG A N     1 
ATOM   1587 C  CA    . ARG A 1 225 ? 31.505  -5.780  -25.942 1.00 45.91  ?  211 ARG A CA    1 
ATOM   1588 C  C     . ARG A 1 225 ? 30.771  -5.733  -24.607 1.00 52.33  ?  211 ARG A C     1 
ATOM   1589 O  O     . ARG A 1 225 ? 29.538  -5.675  -24.577 1.00 46.26  ?  211 ARG A O     1 
ATOM   1590 C  CB    . ARG A 1 225 ? 31.357  -4.447  -26.677 1.00 52.82  ?  211 ARG A CB    1 
ATOM   1591 C  CG    . ARG A 1 225 ? 32.651  -3.874  -27.214 1.00 58.15  ?  211 ARG A CG    1 
ATOM   1592 C  CD    . ARG A 1 225 ? 32.602  -2.353  -27.213 1.00 68.17  ?  211 ARG A CD    1 
ATOM   1593 N  NE    . ARG A 1 225 ? 32.569  -1.823  -25.855 1.00 64.45  ?  211 ARG A NE    1 
ATOM   1594 C  CZ    . ARG A 1 225 ? 31.700  -0.922  -25.417 1.00 68.98  ?  211 ARG A CZ    1 
ATOM   1595 N  NH1   . ARG A 1 225 ? 30.773  -0.408  -26.211 1.00 61.23  ?  211 ARG A NH1   1 
ATOM   1596 N  NH2   . ARG A 1 225 ? 31.759  -0.530  -24.147 1.00 55.81  ?  211 ARG A NH2   1 
ATOM   1597 N  N     . THR A 1 226 ? 31.525  -5.733  -23.510 1.00 47.25  ?  212 THR A N     1 
ATOM   1598 C  CA    . THR A 1 226 ? 30.960  -5.732  -22.167 1.00 38.50  ?  212 THR A CA    1 
ATOM   1599 C  C     . THR A 1 226 ? 31.335  -4.447  -21.441 1.00 38.87  ?  212 THR A C     1 
ATOM   1600 O  O     . THR A 1 226 ? 32.452  -3.939  -21.591 1.00 37.98  ?  212 THR A O     1 
ATOM   1601 C  CB    . THR A 1 226 ? 31.442  -6.949  -21.368 1.00 40.31  ?  212 THR A CB    1 
ATOM   1602 O  OG1   . THR A 1 226 ? 31.112  -8.143  -22.085 1.00 45.53  ?  212 THR A OG1   1 
ATOM   1603 C  CG2   . THR A 1 226 ? 30.779  -7.000  -19.995 1.00 37.12  ?  212 THR A CG2   1 
ATOM   1604 N  N     . ALA A 1 227 ? 30.386  -3.910  -20.675 1.00 39.59  ?  213 ALA A N     1 
ATOM   1605 C  CA    . ALA A 1 227 ? 30.592  -2.705  -19.890 1.00 41.51  ?  213 ALA A CA    1 
ATOM   1606 C  C     . ALA A 1 227 ? 30.104  -2.932  -18.465 1.00 40.41  ?  213 ALA A C     1 
ATOM   1607 O  O     . ALA A 1 227 ? 29.264  -3.797  -18.204 1.00 39.60  ?  213 ALA A O     1 
ATOM   1608 C  CB    . ALA A 1 227 ? 29.877  -1.498  -20.511 1.00 38.59  ?  213 ALA A CB    1 
ATOM   1609 N  N     . LEU A 1 228 ? 30.642  -2.137  -17.544 1.00 33.94  ?  214 LEU A N     1 
ATOM   1610 C  CA    . LEU A 1 228 ? 30.350  -2.246  -16.120 1.00 37.18  ?  214 LEU A CA    1 
ATOM   1611 C  C     . LEU A 1 228 ? 29.708  -0.952  -15.634 1.00 39.13  ?  214 LEU A C     1 
ATOM   1612 O  O     . LEU A 1 228 ? 30.247  0.135   -15.859 1.00 38.62  ?  214 LEU A O     1 
ATOM   1613 C  CB    . LEU A 1 228 ? 31.626  -2.537  -15.317 1.00 32.70  ?  214 LEU A CB    1 
ATOM   1614 C  CG    . LEU A 1 228 ? 31.488  -3.194  -13.937 1.00 43.24  ?  214 LEU A CG    1 
ATOM   1615 C  CD1   . LEU A 1 228 ? 32.825  -3.710  -13.460 1.00 55.24  ?  214 LEU A CD1   1 
ATOM   1616 C  CD2   . LEU A 1 228 ? 30.930  -2.227  -12.911 1.00 57.40  ?  214 LEU A CD2   1 
ATOM   1617 N  N     . LEU A 1 229 ? 28.559  -1.070  -14.968 1.00 32.59  ?  215 LEU A N     1 
ATOM   1618 C  CA    . LEU A 1 229 ? 27.886  0.065   -14.342 1.00 33.58  ?  215 LEU A CA    1 
ATOM   1619 C  C     . LEU A 1 229 ? 27.675  -0.261  -12.868 1.00 40.12  ?  215 LEU A C     1 
ATOM   1620 O  O     . LEU A 1 229 ? 26.913  -1.175  -12.533 1.00 35.92  ?  215 LEU A O     1 
ATOM   1621 C  CB    . LEU A 1 229 ? 26.559  0.372   -15.036 1.00 32.92  ?  215 LEU A CB    1 
ATOM   1622 C  CG    . LEU A 1 229 ? 25.795  1.593   -14.513 1.00 33.66  ?  215 LEU A CG    1 
ATOM   1623 C  CD1   . LEU A 1 229 ? 26.569  2.878   -14.779 1.00 30.42  ?  215 LEU A CD1   1 
ATOM   1624 C  CD2   . LEU A 1 229 ? 24.419  1.659   -15.139 1.00 32.79  ?  215 LEU A CD2   1 
ATOM   1625 N  N     . ALA A 1 230 ? 28.335  0.496   -11.991 1.00 36.21  ?  216 ALA A N     1 
ATOM   1626 C  CA    . ALA A 1 230 ? 28.282  0.278   -10.553 1.00 34.71  ?  216 ALA A CA    1 
ATOM   1627 C  C     . ALA A 1 230 ? 27.705  1.500   -9.854  1.00 41.21  ?  216 ALA A C     1 
ATOM   1628 O  O     . ALA A 1 230 ? 27.853  2.626   -10.333 1.00 34.55  ?  216 ALA A O     1 
ATOM   1629 C  CB    . ALA A 1 230 ? 29.677  -0.015  -9.994  1.00 29.84  ?  216 ALA A CB    1 
ATOM   1630 N  N     . ASP A 1 231 ? 27.054  1.288   -8.716  1.00 30.34  ?  217 ASP A N     1 
ATOM   1631 C  CA    . ASP A 1 231 ? 26.521  2.440   -8.004  1.00 25.46  ?  217 ASP A CA    1 
ATOM   1632 C  C     . ASP A 1 231 ? 26.499  2.169   -6.503  1.00 28.72  ?  217 ASP A C     1 
ATOM   1633 O  O     . ASP A 1 231 ? 27.190  1.275   -6.007  1.00 28.89  ?  217 ASP A O     1 
ATOM   1634 C  CB    . ASP A 1 231 ? 25.151  2.854   -8.554  1.00 32.56  ?  217 ASP A CB    1 
ATOM   1635 C  CG    . ASP A 1 231 ? 24.922  4.345   -8.405  1.00 39.09  ?  217 ASP A CG    1 
ATOM   1636 O  OD1   . ASP A 1 231 ? 25.594  5.116   -9.123  1.00 35.26  ?  217 ASP A OD1   1 
ATOM   1637 O  OD2   . ASP A 1 231 ? 24.100  4.744   -7.557  1.00 38.09  ?  217 ASP A OD2   1 
ATOM   1638 N  N     . PHE A 1 232 ? 25.698  2.964   -5.783  1.00 29.43  ?  218 PHE A N     1 
ATOM   1639 C  CA    . PHE A 1 232 ? 25.943  3.244   -4.372  1.00 28.79  ?  218 PHE A CA    1 
ATOM   1640 C  C     . PHE A 1 232 ? 25.901  2.012   -3.489  1.00 26.44  ?  218 PHE A C     1 
ATOM   1641 O  O     . PHE A 1 232 ? 26.514  2.021   -2.415  1.00 28.06  ?  218 PHE A O     1 
ATOM   1642 C  CB    . PHE A 1 232 ? 24.938  4.277   -3.856  1.00 27.70  ?  218 PHE A CB    1 
ATOM   1643 C  CG    . PHE A 1 232 ? 23.553  3.733   -3.636  1.00 24.66  ?  218 PHE A CG    1 
ATOM   1644 C  CD1   . PHE A 1 232 ? 22.697  3.535   -4.703  1.00 25.97  ?  218 PHE A CD1   1 
ATOM   1645 C  CD2   . PHE A 1 232 ? 23.100  3.445   -2.360  1.00 26.41  ?  218 PHE A CD2   1 
ATOM   1646 C  CE1   . PHE A 1 232 ? 21.417  3.046   -4.507  1.00 30.09  ?  218 PHE A CE1   1 
ATOM   1647 C  CE2   . PHE A 1 232 ? 21.820  2.956   -2.156  1.00 32.06  ?  218 PHE A CE2   1 
ATOM   1648 C  CZ    . PHE A 1 232 ? 20.977  2.761   -3.232  1.00 24.45  ?  218 PHE A CZ    1 
ATOM   1649 N  N     . LEU A 1 233 ? 25.204  0.952   -3.901  1.00 29.77  ?  219 LEU A N     1 
ATOM   1650 C  CA    . LEU A 1 233 ? 25.158  -0.224  -3.042  1.00 26.09  ?  219 LEU A CA    1 
ATOM   1651 C  C     . LEU A 1 233 ? 26.538  -0.867  -2.927  1.00 29.77  ?  219 LEU A C     1 
ATOM   1652 O  O     . LEU A 1 233 ? 26.843  -1.501  -1.909  1.00 34.44  ?  219 LEU A O     1 
ATOM   1653 C  CB    . LEU A 1 233 ? 24.105  -1.203  -3.554  1.00 28.48  ?  219 LEU A CB    1 
ATOM   1654 C  CG    . LEU A 1 233 ? 22.678  -0.672  -3.322  1.00 38.03  ?  219 LEU A CG    1 
ATOM   1655 C  CD1   . LEU A 1 233 ? 21.647  -1.504  -4.055  1.00 32.68  ?  219 LEU A CD1   1 
ATOM   1656 C  CD2   . LEU A 1 233 ? 22.333  -0.577  -1.836  1.00 27.76  ?  219 LEU A CD2   1 
ATOM   1657 N  N     . VAL A 1 234 ? 27.399  -0.664  -3.929  1.00 24.96  ?  220 VAL A N     1 
ATOM   1658 C  CA    . VAL A 1 234 ? 28.789  -1.108  -3.828  1.00 25.63  ?  220 VAL A CA    1 
ATOM   1659 C  C     . VAL A 1 234 ? 29.511  -0.363  -2.710  1.00 29.52  ?  220 VAL A C     1 
ATOM   1660 O  O     . VAL A 1 234 ? 30.305  -0.949  -1.964  1.00 29.76  ?  220 VAL A O     1 
ATOM   1661 C  CB    . VAL A 1 234 ? 29.502  -0.912  -5.179  1.00 29.78  ?  220 VAL A CB    1 
ATOM   1662 C  CG1   . VAL A 1 234 ? 31.029  -1.035  -5.027  1.00 26.66  ?  220 VAL A CG1   1 
ATOM   1663 C  CG2   . VAL A 1 234 ? 28.980  -1.898  -6.202  1.00 30.74  ?  220 VAL A CG2   1 
ATOM   1664 N  N     . LEU A 1 235 ? 29.240  0.939   -2.566  1.00 32.30  ?  221 LEU A N     1 
ATOM   1665 C  CA    . LEU A 1 235 ? 29.858  1.703   -1.486  1.00 30.64  ?  221 LEU A CA    1 
ATOM   1666 C  C     . LEU A 1 235 ? 29.388  1.211   -0.121  1.00 27.01  ?  221 LEU A C     1 
ATOM   1667 O  O     . LEU A 1 235 ? 30.202  0.954   0.774   1.00 29.57  ?  221 LEU A O     1 
ATOM   1668 C  CB    . LEU A 1 235 ? 29.549  3.192   -1.653  1.00 26.61  ?  221 LEU A CB    1 
ATOM   1669 C  CG    . LEU A 1 235 ? 30.097  3.888   -2.900  1.00 28.02  ?  221 LEU A CG    1 
ATOM   1670 C  CD1   . LEU A 1 235 ? 29.425  5.242   -3.082  1.00 26.63  ?  221 LEU A CD1   1 
ATOM   1671 C  CD2   . LEU A 1 235 ? 31.606  4.053   -2.806  1.00 34.77  ?  221 LEU A CD2   1 
ATOM   1672 N  N     . ARG A 1 236 ? 28.074  1.035   0.042   1.00 26.38  ?  222 ARG A N     1 
ATOM   1673 C  CA    . ARG A 1 236 ? 27.528  0.707   1.355   1.00 26.72  ?  222 ARG A CA    1 
ATOM   1674 C  C     . ARG A 1 236 ? 27.985  -0.661  1.840   1.00 27.65  ?  222 ARG A C     1 
ATOM   1675 O  O     . ARG A 1 236 ? 28.178  -0.855  3.047   1.00 32.02  ?  222 ARG A O     1 
ATOM   1676 C  CB    . ARG A 1 236 ? 26.000  0.767   1.321   1.00 30.21  ?  222 ARG A CB    1 
ATOM   1677 C  CG    . ARG A 1 236 ? 25.462  2.000   0.638   1.00 26.52  ?  222 ARG A CG    1 
ATOM   1678 C  CD    . ARG A 1 236 ? 25.843  3.253   1.409   1.00 28.25  ?  222 ARG A CD    1 
ATOM   1679 N  NE    . ARG A 1 236 ? 24.980  4.365   1.040   1.00 29.55  ?  222 ARG A NE    1 
ATOM   1680 C  CZ    . ARG A 1 236 ? 25.383  5.444   0.385   1.00 39.33  ?  222 ARG A CZ    1 
ATOM   1681 N  NH1   . ARG A 1 236 ? 26.656  5.621   0.060   1.00 29.75  ?  222 ARG A NH1   1 
ATOM   1682 N  NH2   . ARG A 1 236 ? 24.485  6.365   0.043   1.00 25.98  ?  222 ARG A NH2   1 
ATOM   1683 N  N     . HIS A 1 237 ? 28.153  -1.620  0.932   1.00 27.45  ?  223 HIS A N     1 
ATOM   1684 C  CA    . HIS A 1 237 ? 28.550  -2.972  1.299   1.00 36.66  ?  223 HIS A CA    1 
ATOM   1685 C  C     . HIS A 1 237 ? 30.058  -3.188  1.216   1.00 36.38  ?  223 HIS A C     1 
ATOM   1686 O  O     . HIS A 1 237 ? 30.503  -4.335  1.148   1.00 36.22  ?  223 HIS A O     1 
ATOM   1687 C  CB    . HIS A 1 237 ? 27.818  -3.989  0.421   1.00 32.75  ?  223 HIS A CB    1 
ATOM   1688 C  CG    . HIS A 1 237 ? 26.347  -4.056  0.688   1.00 39.71  ?  223 HIS A CG    1 
ATOM   1689 N  ND1   . HIS A 1 237 ? 25.794  -4.941  1.588   1.00 39.18  ?  223 HIS A ND1   1 
ATOM   1690 C  CD2   . HIS A 1 237 ? 25.318  -3.325  0.195   1.00 40.87  ?  223 HIS A CD2   1 
ATOM   1691 C  CE1   . HIS A 1 237 ? 24.485  -4.761  1.630   1.00 48.27  ?  223 HIS A CE1   1 
ATOM   1692 N  NE2   . HIS A 1 237 ? 24.171  -3.785  0.796   1.00 37.69  ?  223 HIS A NE2   1 
ATOM   1693 N  N     . GLY A 1 238 ? 30.845  -2.113  1.218   1.00 44.80  ?  224 GLY A N     1 
ATOM   1694 C  CA    . GLY A 1 238 ? 32.292  -2.223  1.316   1.00 41.56  ?  224 GLY A CA    1 
ATOM   1695 C  C     . GLY A 1 238 ? 32.981  -2.873  0.135   1.00 35.60  ?  224 GLY A C     1 
ATOM   1696 O  O     . GLY A 1 238 ? 34.039  -3.485  0.306   1.00 41.05  ?  224 GLY A O     1 
ATOM   1697 N  N     . LEU A 1 239 ? 32.421  -2.742  -1.068  1.00 35.59  ?  225 LEU A N     1 
ATOM   1698 C  CA    . LEU A 1 239 ? 32.955  -3.404  -2.250  1.00 37.98  ?  225 LEU A CA    1 
ATOM   1699 C  C     . LEU A 1 239 ? 33.636  -2.441  -3.220  1.00 38.44  ?  225 LEU A C     1 
ATOM   1700 O  O     . LEU A 1 239 ? 33.878  -2.804  -4.377  1.00 33.68  ?  225 LEU A O     1 
ATOM   1701 C  CB    . LEU A 1 239 ? 31.836  -4.173  -2.952  1.00 37.34  ?  225 LEU A CB    1 
ATOM   1702 C  CG    . LEU A 1 239 ? 31.296  -5.313  -2.088  1.00 32.12  ?  225 LEU A CG    1 
ATOM   1703 C  CD1   . LEU A 1 239 ? 29.922  -5.751  -2.550  1.00 33.77  ?  225 LEU A CD1   1 
ATOM   1704 C  CD2   . LEU A 1 239 ? 32.266  -6.474  -2.106  1.00 34.46  ?  225 LEU A CD2   1 
ATOM   1705 N  N     . LYS A 1 240 ? 33.963  -1.225  -2.773  1.00 33.01  ?  226 LYS A N     1 
ATOM   1706 C  CA    . LYS A 1 240 ? 34.620  -0.263  -3.656  1.00 31.55  ?  226 LYS A CA    1 
ATOM   1707 C  C     . LYS A 1 240 ? 35.975  -0.786  -4.139  1.00 35.30  ?  226 LYS A C     1 
ATOM   1708 O  O     . LYS A 1 240 ? 36.298  -0.688  -5.329  1.00 36.48  ?  226 LYS A O     1 
ATOM   1709 C  CB    . LYS A 1 240 ? 34.765  1.078   -2.931  1.00 29.89  ?  226 LYS A CB    1 
ATOM   1710 C  CG    . LYS A 1 240 ? 35.754  2.057   -3.546  1.00 35.74  ?  226 LYS A CG    1 
ATOM   1711 C  CD    . LYS A 1 240 ? 35.691  3.414   -2.844  1.00 31.74  ?  226 LYS A CD    1 
ATOM   1712 C  CE    . LYS A 1 240 ? 36.635  4.413   -3.491  1.00 51.71  ?  226 LYS A CE    1 
ATOM   1713 N  NZ    . LYS A 1 240 ? 36.806  5.678   -2.708  1.00 53.40  ?  226 LYS A NZ    1 
ATOM   1714 N  N     . HIS A 1 241 ? 36.771  -1.370  -3.240  1.00 31.39  ?  227 HIS A N     1 
ATOM   1715 C  CA    . HIS A 1 241 ? 38.062  -1.921  -3.658  1.00 41.05  ?  227 HIS A CA    1 
ATOM   1716 C  C     . HIS A 1 241 ? 37.884  -3.052  -4.666  1.00 49.62  ?  227 HIS A C     1 
ATOM   1717 O  O     . HIS A 1 241 ? 38.640  -3.147  -5.639  1.00 42.57  ?  227 HIS A O     1 
ATOM   1718 C  CB    . HIS A 1 241 ? 38.848  -2.415  -2.443  1.00 36.63  ?  227 HIS A CB    1 
ATOM   1719 C  CG    . HIS A 1 241 ? 40.172  -3.034  -2.780  1.00 61.83  ?  227 HIS A CG    1 
ATOM   1720 N  ND1   . HIS A 1 241 ? 41.054  -2.475  -3.682  1.00 69.31  ?  227 HIS A ND1   1 
ATOM   1721 C  CD2   . HIS A 1 241 ? 40.752  -4.179  -2.347  1.00 60.38  ?  227 HIS A CD2   1 
ATOM   1722 C  CE1   . HIS A 1 241 ? 42.127  -3.241  -3.776  1.00 68.06  ?  227 HIS A CE1   1 
ATOM   1723 N  NE2   . HIS A 1 241 ? 41.968  -4.282  -2.977  1.00 81.12  ?  227 HIS A NE2   1 
ATOM   1724 N  N     . ALA A 1 242 ? 36.895  -3.925  -4.443  1.00 49.15  ?  228 ALA A N     1 
ATOM   1725 C  CA    . ALA A 1 242 ? 36.673  -5.043  -5.357  1.00 42.11  ?  228 ALA A CA    1 
ATOM   1726 C  C     . ALA A 1 242 ? 36.300  -4.547  -6.750  1.00 44.62  ?  228 ALA A C     1 
ATOM   1727 O  O     . ALA A 1 242 ? 36.751  -5.107  -7.756  1.00 31.98  ?  228 ALA A O     1 
ATOM   1728 C  CB    . ALA A 1 242 ? 35.593  -5.973  -4.805  1.00 34.32  ?  228 ALA A CB    1 
ATOM   1729 N  N     . LEU A 1 243 ? 35.470  -3.501  -6.828  1.00 35.63  ?  229 LEU A N     1 
ATOM   1730 C  CA    . LEU A 1 243 ? 35.092  -2.948  -8.125  1.00 29.53  ?  229 LEU A CA    1 
ATOM   1731 C  C     . LEU A 1 243 ? 36.276  -2.270  -8.804  1.00 37.70  ?  229 LEU A C     1 
ATOM   1732 O  O     . LEU A 1 243 ? 36.416  -2.338  -10.031 1.00 35.78  ?  229 LEU A O     1 
ATOM   1733 C  CB    . LEU A 1 243 ? 33.933  -1.960  -7.958  1.00 36.96  ?  229 LEU A CB    1 
ATOM   1734 C  CG    . LEU A 1 243 ? 32.515  -2.506  -8.151  1.00 37.09  ?  229 LEU A CG    1 
ATOM   1735 C  CD1   . LEU A 1 243 ? 32.223  -2.738  -9.629  1.00 30.63  ?  229 LEU A CD1   1 
ATOM   1736 C  CD2   . LEU A 1 243 ? 32.297  -3.788  -7.352  1.00 33.18  ?  229 LEU A CD2   1 
ATOM   1737 N  N     . GLN A 1 244 ? 37.129  -1.600  -8.022  1.00 36.66  ?  230 GLN A N     1 
ATOM   1738 C  CA    . GLN A 1 244 ? 38.319  -0.964  -8.580  1.00 40.66  ?  230 GLN A CA    1 
ATOM   1739 C  C     . GLN A 1 244 ? 39.293  -2.002  -9.133  1.00 44.44  ?  230 GLN A C     1 
ATOM   1740 O  O     . GLN A 1 244 ? 39.787  -1.869  -10.260 1.00 38.66  ?  230 GLN A O     1 
ATOM   1741 C  CB    . GLN A 1 244 ? 39.000  -0.106  -7.510  1.00 44.00  ?  230 GLN A CB    1 
ATOM   1742 C  CG    . GLN A 1 244 ? 38.438  1.303   -7.372  1.00 65.13  ?  230 GLN A CG    1 
ATOM   1743 C  CD    . GLN A 1 244 ? 38.969  2.038   -6.147  1.00 56.66  ?  230 GLN A CD    1 
ATOM   1744 O  OE1   . GLN A 1 244 ? 38.352  2.988   -5.665  1.00 50.44  ?  230 GLN A OE1   1 
ATOM   1745 N  NE2   . GLN A 1 244 ? 40.112  1.595   -5.635  1.00 45.39  ?  230 GLN A NE2   1 
ATOM   1746 N  N     . LYS A 1 245 ? 39.582  -3.046  -8.351  1.00 41.10  ?  231 LYS A N     1 
ATOM   1747 C  CA    . LYS A 1 245 ? 40.461  -4.110  -8.829  1.00 42.75  ?  231 LYS A CA    1 
ATOM   1748 C  C     . LYS A 1 245 ? 39.852  -4.834  -10.021 1.00 39.04  ?  231 LYS A C     1 
ATOM   1749 O  O     . LYS A 1 245 ? 40.578  -5.295  -10.911 1.00 42.27  ?  231 LYS A O     1 
ATOM   1750 C  CB    . LYS A 1 245 ? 40.755  -5.095  -7.696  1.00 39.76  ?  231 LYS A CB    1 
ATOM   1751 C  CG    . LYS A 1 245 ? 41.868  -6.085  -8.008  1.00 61.15  ?  231 LYS A CG    1 
ATOM   1752 C  CD    . LYS A 1 245 ? 42.842  -6.212  -6.844  1.00 72.79  ?  231 LYS A CD    1 
ATOM   1753 C  CE    . LYS A 1 245 ? 43.669  -7.491  -6.938  1.00 64.99  ?  231 LYS A CE    1 
ATOM   1754 N  NZ    . LYS A 1 245 ? 43.755  -8.014  -8.330  1.00 66.82  ?  231 LYS A NZ    1 
ATOM   1755 N  N     . TRP A 1 246 ? 38.523  -4.934  -10.053 1.00 40.07  ?  232 TRP A N     1 
ATOM   1756 C  CA    . TRP A 1 246 ? 37.833  -5.574  -11.167 1.00 44.54  ?  232 TRP A CA    1 
ATOM   1757 C  C     . TRP A 1 246 ? 38.168  -4.890  -12.489 1.00 40.59  ?  232 TRP A C     1 
ATOM   1758 O  O     . TRP A 1 246 ? 38.602  -5.541  -13.445 1.00 37.20  ?  232 TRP A O     1 
ATOM   1759 C  CB    . TRP A 1 246 ? 36.325  -5.543  -10.898 1.00 37.44  ?  232 TRP A CB    1 
ATOM   1760 C  CG    . TRP A 1 246 ? 35.463  -6.326  -11.842 1.00 41.97  ?  232 TRP A CG    1 
ATOM   1761 C  CD1   . TRP A 1 246 ? 35.844  -6.943  -13.000 1.00 41.72  ?  232 TRP A CD1   1 
ATOM   1762 C  CD2   . TRP A 1 246 ? 34.059  -6.576  -11.698 1.00 35.95  ?  232 TRP A CD2   1 
ATOM   1763 N  NE1   . TRP A 1 246 ? 34.759  -7.558  -13.586 1.00 38.47  ?  232 TRP A NE1   1 
ATOM   1764 C  CE2   . TRP A 1 246 ? 33.654  -7.347  -12.803 1.00 34.79  ?  232 TRP A CE2   1 
ATOM   1765 C  CE3   . TRP A 1 246 ? 33.106  -6.221  -10.738 1.00 29.94  ?  232 TRP A CE3   1 
ATOM   1766 C  CZ2   . TRP A 1 246 ? 32.339  -7.766  -12.975 1.00 36.25  ?  232 TRP A CZ2   1 
ATOM   1767 C  CZ3   . TRP A 1 246 ? 31.801  -6.638  -10.912 1.00 33.57  ?  232 TRP A CZ3   1 
ATOM   1768 C  CH2   . TRP A 1 246 ? 31.430  -7.400  -12.021 1.00 30.44  ?  232 TRP A CH2   1 
ATOM   1769 N  N     . VAL A 1 247 ? 38.014  -3.566  -12.554 1.00 37.35  ?  233 VAL A N     1 
ATOM   1770 C  CA    . VAL A 1 247 ? 38.240  -2.894  -13.829 1.00 40.16  ?  233 VAL A CA    1 
ATOM   1771 C  C     . VAL A 1 247 ? 39.722  -2.739  -14.142 1.00 37.61  ?  233 VAL A C     1 
ATOM   1772 O  O     . VAL A 1 247 ? 40.082  -2.623  -15.320 1.00 48.91  ?  233 VAL A O     1 
ATOM   1773 C  CB    . VAL A 1 247 ? 37.526  -1.529  -13.874 1.00 36.65  ?  233 VAL A CB    1 
ATOM   1774 C  CG1   . VAL A 1 247 ? 36.062  -1.690  -13.496 1.00 41.19  ?  233 VAL A CG1   1 
ATOM   1775 C  CG2   . VAL A 1 247 ? 38.193  -0.542  -12.946 1.00 38.73  ?  233 VAL A CG2   1 
ATOM   1776 N  N     . LYS A 1 248 ? 40.597  -2.783  -13.131 1.00 43.64  ?  234 LYS A N     1 
ATOM   1777 C  CA    . LYS A 1 248 ? 42.034  -2.816  -13.389 1.00 41.00  ?  234 LYS A CA    1 
ATOM   1778 C  C     . LYS A 1 248 ? 42.460  -4.148  -13.995 1.00 50.63  ?  234 LYS A C     1 
ATOM   1779 O  O     . LYS A 1 248 ? 43.167  -4.182  -15.009 1.00 52.77  ?  234 LYS A O     1 
ATOM   1780 C  CB    . LYS A 1 248 ? 42.803  -2.552  -12.094 1.00 54.81  ?  234 LYS A CB    1 
ATOM   1781 C  CG    . LYS A 1 248 ? 44.256  -2.996  -12.149 1.00 66.25  ?  234 LYS A CG    1 
ATOM   1782 C  CD    . LYS A 1 248 ? 44.846  -3.166  -10.759 1.00 72.73  ?  234 LYS A CD    1 
ATOM   1783 C  CE    . LYS A 1 248 ? 45.837  -4.318  -10.730 1.00 59.54  ?  234 LYS A CE    1 
ATOM   1784 N  NZ    . LYS A 1 248 ? 47.237  -3.813  -10.753 1.00 66.19  ?  234 LYS A NZ    1 
ATOM   1785 N  N     . ASP A 1 249 ? 42.042  -5.260  -13.383 1.00 55.08  ?  235 ASP A N     1 
ATOM   1786 C  CA    . ASP A 1 249 ? 42.410  -6.577  -13.890 1.00 47.71  ?  235 ASP A CA    1 
ATOM   1787 C  C     . ASP A 1 249 ? 41.678  -6.907  -15.177 1.00 43.90  ?  235 ASP A C     1 
ATOM   1788 O  O     . ASP A 1 249 ? 42.127  -7.773  -15.934 1.00 53.41  ?  235 ASP A O     1 
ATOM   1789 C  CB    . ASP A 1 249 ? 42.094  -7.666  -12.859 1.00 45.40  ?  235 ASP A CB    1 
ATOM   1790 C  CG    . ASP A 1 249 ? 42.970  -7.586  -11.629 1.00 52.66  ?  235 ASP A CG    1 
ATOM   1791 O  OD1   . ASP A 1 249 ? 44.081  -7.016  -11.710 1.00 60.65  ?  235 ASP A OD1   1 
ATOM   1792 O  OD2   . ASP A 1 249 ? 42.541  -8.097  -10.576 1.00 52.45  ?  235 ASP A OD2   1 
ATOM   1793 N  N     . VAL A 1 250 ? 40.548  -6.255  -15.422 1.00 43.67  ?  236 VAL A N     1 
ATOM   1794 C  CA    . VAL A 1 250 ? 39.718  -6.525  -16.589 1.00 40.85  ?  236 VAL A CA    1 
ATOM   1795 C  C     . VAL A 1 250 ? 39.305  -5.198  -17.215 1.00 42.40  ?  236 VAL A C     1 
ATOM   1796 O  O     . VAL A 1 250 ? 38.213  -4.689  -16.923 1.00 49.67  ?  236 VAL A O     1 
ATOM   1797 C  CB    . VAL A 1 250 ? 38.492  -7.366  -16.201 1.00 48.88  ?  236 VAL A CB    1 
ATOM   1798 C  CG1   . VAL A 1 250 ? 37.735  -7.709  -17.405 1.00 35.28  ?  236 VAL A CG1   1 
ATOM   1799 C  CG2   . VAL A 1 250 ? 38.904  -8.641  -15.479 1.00 39.94  ?  236 VAL A CG2   1 
ATOM   1800 N  N     . PRO A 1 251 ? 40.141  -4.593  -18.056 1.00 52.46  ?  237 PRO A N     1 
ATOM   1801 C  CA    . PRO A 1 251 ? 39.787  -3.287  -18.629 1.00 41.01  ?  237 PRO A CA    1 
ATOM   1802 C  C     . PRO A 1 251 ? 38.551  -3.373  -19.516 1.00 53.21  ?  237 PRO A C     1 
ATOM   1803 O  O     . PRO A 1 251 ? 38.480  -4.187  -20.440 1.00 52.36  ?  237 PRO A O     1 
ATOM   1804 C  CB    . PRO A 1 251 ? 41.038  -2.900  -19.430 1.00 46.08  ?  237 PRO A CB    1 
ATOM   1805 C  CG    . PRO A 1 251 ? 42.145  -3.753  -18.865 1.00 49.10  ?  237 PRO A CG    1 
ATOM   1806 C  CD    . PRO A 1 251 ? 41.478  -5.041  -18.483 1.00 51.96  ?  237 PRO A CD    1 
ATOM   1807 N  N     . MET A 1 252 ? 37.574  -2.516  -19.219 1.00 48.59  ?  238 MET A N     1 
ATOM   1808 C  CA    . MET A 1 252 ? 36.371  -2.365  -20.027 1.00 43.24  ?  238 MET A CA    1 
ATOM   1809 C  C     . MET A 1 252 ? 35.791  -0.989  -19.756 1.00 43.90  ?  238 MET A C     1 
ATOM   1810 O  O     . MET A 1 252 ? 36.135  -0.336  -18.767 1.00 41.73  ?  238 MET A O     1 
ATOM   1811 C  CB    . MET A 1 252 ? 35.317  -3.442  -19.730 1.00 50.08  ?  238 MET A CB    1 
ATOM   1812 C  CG    . MET A 1 252 ? 35.051  -3.704  -18.250 1.00 53.71  ?  238 MET A CG    1 
ATOM   1813 S  SD    . MET A 1 252 ? 34.128  -5.242  -17.965 1.00 57.37  ?  238 MET A SD    1 
ATOM   1814 C  CE    . MET A 1 252 ? 34.233  -5.381  -16.187 1.00 45.92  ?  238 MET A CE    1 
ATOM   1815 N  N     . ALA A 1 253 ? 34.910  -0.551  -20.652 1.00 43.90  ?  239 ALA A N     1 
ATOM   1816 C  CA    . ALA A 1 253 ? 34.177  0.683   -20.408 1.00 45.32  ?  239 ALA A CA    1 
ATOM   1817 C  C     . ALA A 1 253 ? 33.385  0.543   -19.117 1.00 45.77  ?  239 ALA A C     1 
ATOM   1818 O  O     . ALA A 1 253 ? 32.707  -0.465  -18.900 1.00 39.40  ?  239 ALA A O     1 
ATOM   1819 C  CB    . ALA A 1 253 ? 33.247  1.001   -21.576 1.00 35.43  ?  239 ALA A CB    1 
ATOM   1820 N  N     . HIS A 1 254 ? 33.509  1.533   -18.237 1.00 38.64  ?  240 HIS A N     1 
ATOM   1821 C  CA    . HIS A 1 254 ? 32.856  1.465   -16.940 1.00 34.54  ?  240 HIS A CA    1 
ATOM   1822 C  C     . HIS A 1 254 ? 32.418  2.859   -16.521 1.00 42.05  ?  240 HIS A C     1 
ATOM   1823 O  O     . HIS A 1 254 ? 33.018  3.865   -16.916 1.00 41.41  ?  240 HIS A O     1 
ATOM   1824 C  CB    . HIS A 1 254 ? 33.763  0.840   -15.871 1.00 36.01  ?  240 HIS A CB    1 
ATOM   1825 C  CG    . HIS A 1 254 ? 35.052  1.574   -15.659 1.00 40.36  ?  240 HIS A CG    1 
ATOM   1826 N  ND1   . HIS A 1 254 ? 36.000  1.717   -16.649 1.00 40.80  ?  240 HIS A ND1   1 
ATOM   1827 C  CD2   . HIS A 1 254 ? 35.560  2.185   -14.562 1.00 38.43  ?  240 HIS A CD2   1 
ATOM   1828 C  CE1   . HIS A 1 254 ? 37.031  2.395   -16.176 1.00 39.86  ?  240 HIS A CE1   1 
ATOM   1829 N  NE2   . HIS A 1 254 ? 36.790  2.689   -14.911 1.00 46.24  ?  240 HIS A NE2   1 
ATOM   1830 N  N     . ALA A 1 255 ? 31.359  2.903   -15.717 1.00 36.30  ?  241 ALA A N     1 
ATOM   1831 C  CA    . ALA A 1 255 ? 30.824  4.156   -15.214 1.00 34.22  ?  241 ALA A CA    1 
ATOM   1832 C  C     . ALA A 1 255 ? 30.106  3.890   -13.905 1.00 34.07  ?  241 ALA A C     1 
ATOM   1833 O  O     . ALA A 1 255 ? 30.002  2.751   -13.444 1.00 33.96  ?  241 ALA A O     1 
ATOM   1834 C  CB    . ALA A 1 255 ? 29.869  4.810   -16.219 1.00 34.31  ?  241 ALA A CB    1 
ATOM   1835 N  N     . THR A 1 256 ? 29.668  4.976   -13.280 1.00 37.29  ?  242 THR A N     1 
ATOM   1836 C  CA    . THR A 1 256 ? 28.704  4.951   -12.193 1.00 33.85  ?  242 THR A CA    1 
ATOM   1837 C  C     . THR A 1 256 ? 27.569  5.895   -12.552 1.00 32.79  ?  242 THR A C     1 
ATOM   1838 O  O     . THR A 1 256 ? 27.608  6.590   -13.572 1.00 37.54  ?  242 THR A O     1 
ATOM   1839 C  CB    . THR A 1 256 ? 29.324  5.365   -10.847 1.00 36.00  ?  242 THR A CB    1 
ATOM   1840 O  OG1   . THR A 1 256 ? 29.454  6.793   -10.791 1.00 37.16  ?  242 THR A OG1   1 
ATOM   1841 C  CG2   . THR A 1 256 ? 30.688  4.711   -10.651 1.00 33.62  ?  242 THR A CG2   1 
ATOM   1842 N  N     . MET A 1 257 ? 26.549  5.917   -11.708 1.00 30.62  ?  243 MET A N     1 
ATOM   1843 C  CA    . MET A 1 257 ? 25.562  6.983   -11.752 1.00 36.39  ?  243 MET A CA    1 
ATOM   1844 C  C     . MET A 1 257 ? 25.911  7.998   -10.663 1.00 28.90  ?  243 MET A C     1 
ATOM   1845 O  O     . MET A 1 257 ? 26.974  7.922   -10.036 1.00 36.17  ?  243 MET A O     1 
ATOM   1846 C  CB    . MET A 1 257 ? 24.147  6.408   -11.631 1.00 36.18  ?  243 MET A CB    1 
ATOM   1847 C  CG    . MET A 1 257 ? 23.708  5.626   -12.871 1.00 35.77  ?  243 MET A CG    1 
ATOM   1848 S  SD    . MET A 1 257 ? 22.064  4.884   -12.765 1.00 34.77  ?  243 MET A SD    1 
ATOM   1849 C  CE    . MET A 1 257 ? 22.290  3.712   -11.417 1.00 31.82  ?  243 MET A CE    1 
ATOM   1850 N  N     . LEU A 1 258 ? 25.028  8.972   -10.444 1.00 25.62  ?  244 LEU A N     1 
ATOM   1851 C  CA    . LEU A 1 258 ? 25.355  10.066  -9.532  1.00 32.56  ?  244 LEU A CA    1 
ATOM   1852 C  C     . LEU A 1 258 ? 25.566  9.574   -8.102  1.00 36.81  ?  244 LEU A C     1 
ATOM   1853 O  O     . LEU A 1 258 ? 26.513  10.005  -7.431  1.00 35.25  ?  244 LEU A O     1 
ATOM   1854 C  CB    . LEU A 1 258 ? 24.259  11.133  -9.576  1.00 27.44  ?  244 LEU A CB    1 
ATOM   1855 C  CG    . LEU A 1 258 ? 24.421  12.330  -8.637  1.00 28.41  ?  244 LEU A CG    1 
ATOM   1856 C  CD1   . LEU A 1 258 ? 25.760  13.024  -8.849  1.00 26.88  ?  244 LEU A CD1   1 
ATOM   1857 C  CD2   . LEU A 1 258 ? 23.267  13.321  -8.817  1.00 32.48  ?  244 LEU A CD2   1 
ATOM   1858 N  N     . MET A 1 259 ? 24.703  8.666   -7.622  1.00 32.53  ?  245 MET A N     1 
ATOM   1859 C  CA    . MET A 1 259 ? 24.769  8.236   -6.224  1.00 31.56  ?  245 MET A CA    1 
ATOM   1860 C  C     . MET A 1 259 ? 26.081  7.535   -5.913  1.00 28.94  ?  245 MET A C     1 
ATOM   1861 O  O     . MET A 1 259 ? 26.641  7.708   -4.824  1.00 37.07  ?  245 MET A O     1 
ATOM   1862 C  CB    . MET A 1 259 ? 23.606  7.299   -5.874  1.00 35.42  ?  245 MET A CB    1 
ATOM   1863 C  CG    . MET A 1 259 ? 22.222  7.876   -6.001  1.00 33.06  ?  245 MET A CG    1 
ATOM   1864 S  SD    . MET A 1 259 ? 20.942  6.812   -5.301  1.00 38.35  ?  245 MET A SD    1 
ATOM   1865 C  CE    . MET A 1 259 ? 21.305  6.915   -3.552  1.00 35.64  ?  245 MET A CE    1 
ATOM   1866 N  N     . GLY A 1 260 ? 26.560  6.707   -6.834  1.00 31.34  ?  246 GLY A N     1 
ATOM   1867 C  CA    . GLY A 1 260 ? 27.763  5.929   -6.651  1.00 32.27  ?  246 GLY A CA    1 
ATOM   1868 C  C     . GLY A 1 260 ? 29.026  6.575   -7.171  1.00 36.06  ?  246 GLY A C     1 
ATOM   1869 O  O     . GLY A 1 260 ? 30.057  5.904   -7.259  1.00 30.83  ?  246 GLY A O     1 
ATOM   1870 N  N     . LYS A 1 261 ? 28.981  7.853   -7.536  1.00 37.03  ?  247 LYS A N     1 
ATOM   1871 C  CA    . LYS A 1 261 ? 30.187  8.535   -7.978  1.00 36.50  ?  247 LYS A CA    1 
ATOM   1872 C  C     . LYS A 1 261 ? 31.244  8.487   -6.881  1.00 39.57  ?  247 LYS A C     1 
ATOM   1873 O  O     . LYS A 1 261 ? 30.949  8.718   -5.704  1.00 32.37  ?  247 LYS A O     1 
ATOM   1874 C  CB    . LYS A 1 261 ? 29.867  9.978   -8.361  1.00 33.79  ?  247 LYS A CB    1 
ATOM   1875 C  CG    . LYS A 1 261 ? 30.981  10.658  -9.101  1.00 43.78  ?  247 LYS A CG    1 
ATOM   1876 C  CD    . LYS A 1 261 ? 30.726  12.150  -9.243  1.00 55.06  ?  247 LYS A CD    1 
ATOM   1877 C  CE    . LYS A 1 261 ? 30.476  12.523  -10.691 1.00 44.54  ?  247 LYS A CE    1 
ATOM   1878 N  NZ    . LYS A 1 261 ? 31.693  12.320  -11.536 1.00 29.37  ?  247 LYS A NZ    1 
ATOM   1879 N  N     . GLY A 1 262 ? 32.474  8.156   -7.268  1.00 32.84  ?  248 GLY A N     1 
ATOM   1880 C  CA    . GLY A 1 262 ? 33.562  7.967   -6.331  1.00 32.41  ?  248 GLY A CA    1 
ATOM   1881 C  C     . GLY A 1 262 ? 34.029  6.532   -6.213  1.00 41.72  ?  248 GLY A C     1 
ATOM   1882 O  O     . GLY A 1 262 ? 35.068  6.284   -5.586  1.00 37.51  ?  248 GLY A O     1 
ATOM   1883 N  N     . ILE A 1 263 ? 33.296  5.581   -6.794  1.00 37.17  ?  249 ILE A N     1 
ATOM   1884 C  CA    . ILE A 1 263 ? 33.741  4.192   -6.787  1.00 33.35  ?  249 ILE A CA    1 
ATOM   1885 C  C     . ILE A 1 263 ? 35.014  4.037   -7.610  1.00 36.95  ?  249 ILE A C     1 
ATOM   1886 O  O     . ILE A 1 263 ? 35.946  3.331   -7.209  1.00 37.51  ?  249 ILE A O     1 
ATOM   1887 C  CB    . ILE A 1 263 ? 32.618  3.274   -7.305  1.00 29.93  ?  249 ILE A CB    1 
ATOM   1888 C  CG1   . ILE A 1 263 ? 31.484  3.190   -6.278  1.00 30.61  ?  249 ILE A CG1   1 
ATOM   1889 C  CG2   . ILE A 1 263 ? 33.169  1.885   -7.652  1.00 29.24  ?  249 ILE A CG2   1 
ATOM   1890 C  CD1   . ILE A 1 263 ? 30.145  2.769   -6.864  1.00 26.13  ?  249 ILE A CD1   1 
ATOM   1891 N  N     . PHE A 1 264 ? 35.079  4.697   -8.764  1.00 39.59  ?  250 PHE A N     1 
ATOM   1892 C  CA    . PHE A 1 264 ? 36.181  4.543   -9.703  1.00 35.02  ?  250 PHE A CA    1 
ATOM   1893 C  C     . PHE A 1 264 ? 37.021  5.811   -9.772  1.00 33.80  ?  250 PHE A C     1 
ATOM   1894 O  O     . PHE A 1 264 ? 36.494  6.924   -9.676  1.00 36.71  ?  250 PHE A O     1 
ATOM   1895 C  CB    . PHE A 1 264 ? 35.659  4.217   -11.106 1.00 39.09  ?  250 PHE A CB    1 
ATOM   1896 C  CG    . PHE A 1 264 ? 34.900  2.927   -11.188 1.00 38.44  ?  250 PHE A CG    1 
ATOM   1897 C  CD1   . PHE A 1 264 ? 35.523  1.719   -10.917 1.00 36.28  ?  250 PHE A CD1   1 
ATOM   1898 C  CD2   . PHE A 1 264 ? 33.560  2.921   -11.545 1.00 37.82  ?  250 PHE A CD2   1 
ATOM   1899 C  CE1   . PHE A 1 264 ? 34.818  0.525   -10.994 1.00 36.51  ?  250 PHE A CE1   1 
ATOM   1900 C  CE2   . PHE A 1 264 ? 32.851  1.734   -11.624 1.00 36.02  ?  250 PHE A CE2   1 
ATOM   1901 C  CZ    . PHE A 1 264 ? 33.483  0.533   -11.350 1.00 34.32  ?  250 PHE A CZ    1 
ATOM   1902 N  N     . ASP A 1 265 ? 38.333  5.634   -9.938  1.00 39.50  ?  251 ASP A N     1 
ATOM   1903 C  CA    . ASP A 1 265 ? 39.207  6.723   -10.363 1.00 40.56  ?  251 ASP A CA    1 
ATOM   1904 C  C     . ASP A 1 265 ? 38.811  7.117   -11.779 1.00 38.66  ?  251 ASP A C     1 
ATOM   1905 O  O     . ASP A 1 265 ? 39.001  6.343   -12.721 1.00 45.17  ?  251 ASP A O     1 
ATOM   1906 C  CB    . ASP A 1 265 ? 40.671  6.288   -10.297 1.00 40.79  ?  251 ASP A CB    1 
ATOM   1907 C  CG    . ASP A 1 265 ? 41.651  7.440   -10.544 1.00 55.06  ?  251 ASP A CG    1 
ATOM   1908 O  OD1   . ASP A 1 265 ? 41.257  8.468   -11.136 1.00 50.64  ?  251 ASP A OD1   1 
ATOM   1909 O  OD2   . ASP A 1 265 ? 42.832  7.310   -10.154 1.00 55.86  ?  251 ASP A OD2   1 
ATOM   1910 N  N     . GLU A 1 266 ? 38.272  8.323   -11.936 1.00 40.75  ?  252 GLU A N     1 
ATOM   1911 C  CA    . GLU A 1 266 ? 37.681  8.748   -13.199 1.00 40.18  ?  252 GLU A CA    1 
ATOM   1912 C  C     . GLU A 1 266 ? 38.712  9.175   -14.239 1.00 43.93  ?  252 GLU A C     1 
ATOM   1913 O  O     . GLU A 1 266 ? 38.331  9.464   -15.378 1.00 51.22  ?  252 GLU A O     1 
ATOM   1914 C  CB    . GLU A 1 266 ? 36.682  9.881   -12.941 1.00 36.15  ?  252 GLU A CB    1 
ATOM   1915 C  CG    . GLU A 1 266 ? 35.793  9.659   -11.706 1.00 46.17  ?  252 GLU A CG    1 
ATOM   1916 C  CD    . GLU A 1 266 ? 34.424  10.323  -11.830 1.00 48.31  ?  252 GLU A CD    1 
ATOM   1917 O  OE1   . GLU A 1 266 ? 34.362  11.435  -12.404 1.00 43.51  ?  252 GLU A OE1   1 
ATOM   1918 O  OE2   . GLU A 1 266 ? 33.419  9.751   -11.335 1.00 36.70  ?  252 GLU A OE2   1 
ATOM   1919 N  N     . ARG A 1 267 ? 39.997  9.223   -13.886 1.00 53.33  ?  253 ARG A N     1 
ATOM   1920 C  CA    . ARG A 1 267 ? 41.049  9.457   -14.870 1.00 55.05  ?  253 ARG A CA    1 
ATOM   1921 C  C     . ARG A 1 267 ? 41.491  8.186   -15.583 1.00 50.90  ?  253 ARG A C     1 
ATOM   1922 O  O     . ARG A 1 267 ? 42.196  8.278   -16.593 1.00 49.41  ?  253 ARG A O     1 
ATOM   1923 C  CB    . ARG A 1 267 ? 42.263  10.099  -14.202 1.00 45.68  ?  253 ARG A CB    1 
ATOM   1924 C  CG    . ARG A 1 267 ? 41.938  11.301  -13.341 1.00 52.86  ?  253 ARG A CG    1 
ATOM   1925 C  CD    . ARG A 1 267 ? 43.099  11.619  -12.417 1.00 60.72  ?  253 ARG A CD    1 
ATOM   1926 N  NE    . ARG A 1 267 ? 43.306  10.577  -11.417 1.00 50.70  ?  253 ARG A NE    1 
ATOM   1927 C  CZ    . ARG A 1 267 ? 44.161  10.671  -10.407 1.00 47.22  ?  253 ARG A CZ    1 
ATOM   1928 N  NH1   . ARG A 1 267 ? 44.931  11.737  -10.249 1.00 48.11  ?  253 ARG A NH1   1 
ATOM   1929 N  NH2   . ARG A 1 267 ? 44.242  9.674   -9.532  1.00 45.13  ?  253 ARG A NH2   1 
ATOM   1930 N  N     . HIS A 1 268 ? 41.102  7.018   -15.079 1.00 54.47  ?  254 HIS A N     1 
ATOM   1931 C  CA    . HIS A 1 268 ? 41.575  5.745   -15.600 1.00 62.59  ?  254 HIS A CA    1 
ATOM   1932 C  C     . HIS A 1 268 ? 40.987  5.443   -16.976 1.00 64.42  ?  254 HIS A C     1 
ATOM   1933 O  O     . HIS A 1 268 ? 39.915  5.928   -17.352 1.00 56.33  ?  254 HIS A O     1 
ATOM   1934 C  CB    . HIS A 1 268 ? 41.251  4.618   -14.618 1.00 47.52  ?  254 HIS A CB    1 
ATOM   1935 C  CG    . HIS A 1 268 ? 42.238  4.504   -13.498 1.00 77.66  ?  254 HIS A CG    1 
ATOM   1936 N  ND1   . HIS A 1 268 ? 42.998  5.572   -13.069 1.00 80.30  ?  254 HIS A ND1   1 
ATOM   1937 C  CD2   . HIS A 1 268 ? 42.592  3.453   -12.720 1.00 65.09  ?  254 HIS A CD2   1 
ATOM   1938 C  CE1   . HIS A 1 268 ? 43.782  5.183   -12.080 1.00 67.60  ?  254 HIS A CE1   1 
ATOM   1939 N  NE2   . HIS A 1 268 ? 43.551  3.903   -11.845 1.00 76.70  ?  254 HIS A NE2   1 
ATOM   1940 N  N     . VAL A 1 269 ? 41.719  4.616   -17.728 1.00 57.64  ?  255 VAL A N     1 
ATOM   1941 C  CA    . VAL A 1 269 ? 41.269  4.196   -19.048 1.00 60.56  ?  255 VAL A CA    1 
ATOM   1942 C  C     . VAL A 1 269 ? 39.974  3.405   -18.919 1.00 55.39  ?  255 VAL A C     1 
ATOM   1943 O  O     . VAL A 1 269 ? 39.790  2.609   -17.987 1.00 48.87  ?  255 VAL A O     1 
ATOM   1944 C  CB    . VAL A 1 269 ? 42.372  3.377   -19.745 1.00 66.73  ?  255 VAL A CB    1 
ATOM   1945 C  CG1   . VAL A 1 269 ? 42.743  2.153   -18.920 1.00 56.36  ?  255 VAL A CG1   1 
ATOM   1946 C  CG2   . VAL A 1 269 ? 41.944  2.965   -21.145 1.00 65.88  ?  255 VAL A CG2   1 
ATOM   1947 N  N     . GLY A 1 270 ? 39.057  3.636   -19.857 1.00 46.20  ?  256 GLY A N     1 
ATOM   1948 C  CA    . GLY A 1 270 ? 37.756  3.009   -19.833 1.00 46.54  ?  256 GLY A CA    1 
ATOM   1949 C  C     . GLY A 1 270 ? 36.664  3.830   -19.182 1.00 51.13  ?  256 GLY A C     1 
ATOM   1950 O  O     . GLY A 1 270 ? 35.487  3.454   -19.278 1.00 48.43  ?  256 GLY A O     1 
ATOM   1951 N  N     . PHE A 1 271 ? 37.003  4.944   -18.537 1.00 44.77  ?  257 PHE A N     1 
ATOM   1952 C  CA    . PHE A 1 271 ? 36.008  5.828   -17.945 1.00 43.65  ?  257 PHE A CA    1 
ATOM   1953 C  C     . PHE A 1 271 ? 35.805  7.032   -18.850 1.00 49.92  ?  257 PHE A C     1 
ATOM   1954 O  O     . PHE A 1 271 ? 36.775  7.685   -19.246 1.00 47.24  ?  257 PHE A O     1 
ATOM   1955 C  CB    . PHE A 1 271 ? 36.423  6.290   -16.548 1.00 36.71  ?  257 PHE A CB    1 
ATOM   1956 C  CG    . PHE A 1 271 ? 35.320  6.983   -15.793 1.00 46.01  ?  257 PHE A CG    1 
ATOM   1957 C  CD1   . PHE A 1 271 ? 34.392  6.251   -15.068 1.00 44.34  ?  257 PHE A CD1   1 
ATOM   1958 C  CD2   . PHE A 1 271 ? 35.202  8.364   -15.820 1.00 47.01  ?  257 PHE A CD2   1 
ATOM   1959 C  CE1   . PHE A 1 271 ? 33.371  6.885   -14.379 1.00 40.73  ?  257 PHE A CE1   1 
ATOM   1960 C  CE2   . PHE A 1 271 ? 34.182  9.001   -15.134 1.00 48.13  ?  257 PHE A CE2   1 
ATOM   1961 C  CZ    . PHE A 1 271 ? 33.266  8.261   -14.415 1.00 40.97  ?  257 PHE A CZ    1 
ATOM   1962 N  N     . TYR A 1 272 ? 34.544  7.314   -19.185 1.00 45.73  ?  258 TYR A N     1 
ATOM   1963 C  CA    . TYR A 1 272 ? 34.213  8.423   -20.066 1.00 45.69  ?  258 TYR A CA    1 
ATOM   1964 C  C     . TYR A 1 272 ? 33.313  9.460   -19.409 1.00 47.29  ?  258 TYR A C     1 
ATOM   1965 O  O     . TYR A 1 272 ? 32.996  10.474  -20.043 1.00 36.23  ?  258 TYR A O     1 
ATOM   1966 C  CB    . TYR A 1 272 ? 33.550  7.907   -21.350 1.00 43.76  ?  258 TYR A CB    1 
ATOM   1967 C  CG    . TYR A 1 272 ? 34.356  6.851   -22.077 1.00 52.39  ?  258 TYR A CG    1 
ATOM   1968 C  CD1   . TYR A 1 272 ? 34.252  5.506   -21.731 1.00 51.74  ?  258 TYR A CD1   1 
ATOM   1969 C  CD2   . TYR A 1 272 ? 35.211  7.195   -23.120 1.00 52.16  ?  258 TYR A CD2   1 
ATOM   1970 C  CE1   . TYR A 1 272 ? 34.983  4.536   -22.395 1.00 43.54  ?  258 TYR A CE1   1 
ATOM   1971 C  CE2   . TYR A 1 272 ? 35.946  6.233   -23.789 1.00 55.23  ?  258 TYR A CE2   1 
ATOM   1972 C  CZ    . TYR A 1 272 ? 35.827  4.904   -23.423 1.00 54.67  ?  258 TYR A CZ    1 
ATOM   1973 O  OH    . TYR A 1 272 ? 36.555  3.942   -24.085 1.00 64.46  ?  258 TYR A OH    1 
ATOM   1974 N  N     . GLY A 1 273 ? 32.914  9.255   -18.160 1.00 41.41  ?  259 GLY A N     1 
ATOM   1975 C  CA    . GLY A 1 273 ? 32.012  10.159  -17.480 1.00 40.11  ?  259 GLY A CA    1 
ATOM   1976 C  C     . GLY A 1 273 ? 30.876  9.416   -16.802 1.00 41.77  ?  259 GLY A C     1 
ATOM   1977 O  O     . GLY A 1 273 ? 30.629  8.237   -17.036 1.00 38.66  ?  259 GLY A O     1 
ATOM   1978 N  N     . THR A 1 274 ? 30.187  10.153  -15.936 1.00 36.58  ?  260 THR A N     1 
ATOM   1979 C  CA    . THR A 1 274 ? 29.071  9.587   -15.195 1.00 35.95  ?  260 THR A CA    1 
ATOM   1980 C  C     . THR A 1 274 ? 27.897  9.311   -16.129 1.00 37.39  ?  260 THR A C     1 
ATOM   1981 O  O     . THR A 1 274 ? 27.663  10.040  -17.096 1.00 38.68  ?  260 THR A O     1 
ATOM   1982 C  CB    . THR A 1 274 ? 28.670  10.534  -14.066 1.00 34.39  ?  260 THR A CB    1 
ATOM   1983 O  OG1   . THR A 1 274 ? 29.825  10.801  -13.261 1.00 35.71  ?  260 THR A OG1   1 
ATOM   1984 C  CG2   . THR A 1 274 ? 27.588  9.919   -13.184 1.00 30.48  ?  260 THR A CG2   1 
ATOM   1985 N  N     . TYR A 1 275 ? 27.188  8.218   -15.860 1.00 36.94  ?  261 TYR A N     1 
ATOM   1986 C  CA    . TYR A 1 275 ? 26.039  7.811   -16.657 1.00 41.02  ?  261 TYR A CA    1 
ATOM   1987 C  C     . TYR A 1 275 ? 24.775  8.419   -16.065 1.00 35.74  ?  261 TYR A C     1 
ATOM   1988 O  O     . TYR A 1 275 ? 24.520  8.285   -14.864 1.00 40.85  ?  261 TYR A O     1 
ATOM   1989 C  CB    . TYR A 1 275 ? 25.934  6.284   -16.700 1.00 36.17  ?  261 TYR A CB    1 
ATOM   1990 C  CG    . TYR A 1 275 ? 24.725  5.751   -17.436 1.00 34.77  ?  261 TYR A CG    1 
ATOM   1991 C  CD1   . TYR A 1 275 ? 24.588  5.930   -18.807 1.00 38.73  ?  261 TYR A CD1   1 
ATOM   1992 C  CD2   . TYR A 1 275 ? 23.730  5.053   -16.764 1.00 34.03  ?  261 TYR A CD2   1 
ATOM   1993 C  CE1   . TYR A 1 275 ? 23.489  5.443   -19.487 1.00 36.02  ?  261 TYR A CE1   1 
ATOM   1994 C  CE2   . TYR A 1 275 ? 22.624  4.560   -17.435 1.00 35.04  ?  261 TYR A CE2   1 
ATOM   1995 C  CZ    . TYR A 1 275 ? 22.509  4.756   -18.798 1.00 45.97  ?  261 TYR A CZ    1 
ATOM   1996 O  OH    . TYR A 1 275 ? 21.411  4.270   -19.477 1.00 33.16  ?  261 TYR A OH    1 
ATOM   1997 N  N     . SER A 1 276 ? 24.002  9.110   -16.899 1.00 32.90  ?  262 SER A N     1 
ATOM   1998 C  CA    . SER A 1 276 ? 22.761  9.728   -16.446 1.00 31.50  ?  262 SER A CA    1 
ATOM   1999 C  C     . SER A 1 276 ? 21.657  9.552   -17.487 1.00 38.98  ?  262 SER A C     1 
ATOM   2000 O  O     . SER A 1 276 ? 20.874  10.472  -17.750 1.00 37.31  ?  262 SER A O     1 
ATOM   2001 C  CB    . SER A 1 276 ? 22.975  11.207  -16.119 1.00 28.77  ?  262 SER A CB    1 
ATOM   2002 O  OG    . SER A 1 276 ? 23.626  11.869  -17.187 1.00 40.72  ?  262 SER A OG    1 
ATOM   2003 N  N     . GLY A 1 277 ? 21.555  8.356   -18.068 1.00 41.12  ?  263 GLY A N     1 
ATOM   2004 C  CA    . GLY A 1 277 ? 20.535  8.121   -19.082 1.00 33.12  ?  263 GLY A CA    1 
ATOM   2005 C  C     . GLY A 1 277 ? 20.774  8.956   -20.329 1.00 38.25  ?  263 GLY A C     1 
ATOM   2006 O  O     . GLY A 1 277 ? 21.905  9.103   -20.805 1.00 36.30  ?  263 GLY A O     1 
ATOM   2007 N  N     . SER A 1 278 ? 19.689  9.514   -20.871 1.00 41.19  ?  264 SER A N     1 
ATOM   2008 C  CA    . SER A 1 278 ? 19.792  10.343  -22.067 1.00 43.00  ?  264 SER A CA    1 
ATOM   2009 C  C     . SER A 1 278 ? 20.551  11.642  -21.825 1.00 49.58  ?  264 SER A C     1 
ATOM   2010 O  O     . SER A 1 278 ? 20.949  12.297  -22.795 1.00 50.95  ?  264 SER A O     1 
ATOM   2011 C  CB    . SER A 1 278 ? 18.397  10.654  -22.611 1.00 46.11  ?  264 SER A CB    1 
ATOM   2012 O  OG    . SER A 1 278 ? 17.759  11.653  -21.833 1.00 46.14  ?  264 SER A OG    1 
ATOM   2013 N  N     . ALA A 1 279 ? 20.772  12.022  -20.569 1.00 40.68  ?  265 ALA A N     1 
ATOM   2014 C  CA    . ALA A 1 279 ? 21.564  13.204  -20.257 1.00 32.61  ?  265 ALA A CA    1 
ATOM   2015 C  C     . ALA A 1 279 ? 23.061  12.931  -20.253 1.00 37.43  ?  265 ALA A C     1 
ATOM   2016 O  O     . ALA A 1 279 ? 23.838  13.863  -20.027 1.00 54.46  ?  265 ALA A O     1 
ATOM   2017 C  CB    . ALA A 1 279 ? 21.149  13.769  -18.900 1.00 35.62  ?  265 ALA A CB    1 
ATOM   2018 N  N     . SER A 1 280 ? 23.484  11.692  -20.494 1.00 36.97  ?  266 SER A N     1 
ATOM   2019 C  CA    . SER A 1 280 ? 24.900  11.362  -20.482 1.00 40.73  ?  266 SER A CA    1 
ATOM   2020 C  C     . SER A 1 280 ? 25.614  12.014  -21.662 1.00 42.59  ?  266 SER A C     1 
ATOM   2021 O  O     . SER A 1 280 ? 25.017  12.317  -22.698 1.00 44.51  ?  266 SER A O     1 
ATOM   2022 C  CB    . SER A 1 280 ? 25.112  9.844   -20.550 1.00 40.93  ?  266 SER A CB    1 
ATOM   2023 O  OG    . SER A 1 280 ? 24.312  9.141   -19.613 1.00 39.00  ?  266 SER A OG    1 
ATOM   2024 N  N     . ALA A 1 281 ? 26.918  12.218  -21.497 1.00 42.26  ?  267 ALA A N     1 
ATOM   2025 C  CA    . ALA A 1 281 ? 27.745  12.614  -22.624 1.00 48.23  ?  267 ALA A CA    1 
ATOM   2026 C  C     . ALA A 1 281 ? 27.672  11.545  -23.708 1.00 53.72  ?  267 ALA A C     1 
ATOM   2027 O  O     . ALA A 1 281 ? 27.430  10.366  -23.431 1.00 60.34  ?  267 ALA A O     1 
ATOM   2028 C  CB    . ALA A 1 281 ? 29.193  12.830  -22.183 1.00 38.99  ?  267 ALA A CB    1 
ATOM   2029 N  N     . GLY A 1 282 ? 27.858  11.972  -24.957 1.00 49.48  ?  268 GLY A N     1 
ATOM   2030 C  CA    . GLY A 1 282 ? 27.741  11.042  -26.068 1.00 47.84  ?  268 GLY A CA    1 
ATOM   2031 C  C     . GLY A 1 282 ? 28.655  9.839   -25.929 1.00 51.12  ?  268 GLY A C     1 
ATOM   2032 O  O     . GLY A 1 282 ? 28.251  8.708   -26.207 1.00 54.98  ?  268 GLY A O     1 
ATOM   2033 N  N     . ALA A 1 283 ? 29.894  10.064  -25.482 1.00 48.86  ?  269 ALA A N     1 
ATOM   2034 C  CA    . ALA A 1 283 ? 30.821  8.954   -25.281 1.00 51.85  ?  269 ALA A CA    1 
ATOM   2035 C  C     . ALA A 1 283 ? 30.334  8.013   -24.186 1.00 46.23  ?  269 ALA A C     1 
ATOM   2036 O  O     . ALA A 1 283 ? 30.499  6.792   -24.290 1.00 47.10  ?  269 ALA A O     1 
ATOM   2037 C  CB    . ALA A 1 283 ? 32.219  9.481   -24.955 1.00 37.24  ?  269 ALA A CB    1 
ATOM   2038 N  N     . VAL A 1 284 ? 29.744  8.562   -23.121 1.00 51.12  ?  270 VAL A N     1 
ATOM   2039 C  CA    . VAL A 1 284 ? 29.236  7.725   -22.035 1.00 41.97  ?  270 VAL A CA    1 
ATOM   2040 C  C     . VAL A 1 284 ? 28.072  6.868   -22.517 1.00 47.30  ?  270 VAL A C     1 
ATOM   2041 O  O     . VAL A 1 284 ? 27.993  5.672   -22.214 1.00 47.63  ?  270 VAL A O     1 
ATOM   2042 C  CB    . VAL A 1 284 ? 28.834  8.596   -20.834 1.00 40.12  ?  270 VAL A CB    1 
ATOM   2043 C  CG1   . VAL A 1 284 ? 28.231  7.739   -19.728 1.00 39.43  ?  270 VAL A CG1   1 
ATOM   2044 C  CG2   . VAL A 1 284 ? 30.035  9.360   -20.330 1.00 43.38  ?  270 VAL A CG2   1 
ATOM   2045 N  N     . LYS A 1 285 ? 27.143  7.474   -23.263 1.00 50.51  ?  271 LYS A N     1 
ATOM   2046 C  CA    . LYS A 1 285 ? 26.019  6.723   -23.810 1.00 43.86  ?  271 LYS A CA    1 
ATOM   2047 C  C     . LYS A 1 285 ? 26.503  5.560   -24.667 1.00 46.79  ?  271 LYS A C     1 
ATOM   2048 O  O     . LYS A 1 285 ? 25.977  4.445   -24.572 1.00 46.52  ?  271 LYS A O     1 
ATOM   2049 C  CB    . LYS A 1 285 ? 25.119  7.654   -24.622 1.00 40.92  ?  271 LYS A CB    1 
ATOM   2050 C  CG    . LYS A 1 285 ? 23.632  7.464   -24.379 1.00 53.35  ?  271 LYS A CG    1 
ATOM   2051 C  CD    . LYS A 1 285 ? 22.811  8.516   -25.118 1.00 54.61  ?  271 LYS A CD    1 
ATOM   2052 C  CE    . LYS A 1 285 ? 23.098  9.921   -24.598 1.00 58.13  ?  271 LYS A CE    1 
ATOM   2053 N  NZ    . LYS A 1 285 ? 21.989  10.872  -24.915 1.00 58.71  ?  271 LYS A NZ    1 
ATOM   2054 N  N     . GLU A 1 286 ? 27.512  5.799   -25.506 1.00 40.81  ?  272 GLU A N     1 
ATOM   2055 C  CA    . GLU A 1 286 ? 28.039  4.731   -26.349 1.00 53.22  ?  272 GLU A CA    1 
ATOM   2056 C  C     . GLU A 1 286 ? 28.807  3.699   -25.528 1.00 54.76  ?  272 GLU A C     1 
ATOM   2057 O  O     . GLU A 1 286 ? 28.735  2.497   -25.808 1.00 48.24  ?  272 GLU A O     1 
ATOM   2058 C  CB    . GLU A 1 286 ? 28.931  5.326   -27.438 1.00 51.38  ?  272 GLU A CB    1 
ATOM   2059 C  CG    . GLU A 1 286 ? 29.457  4.324   -28.456 1.00 60.80  ?  272 GLU A CG    1 
ATOM   2060 C  CD    . GLU A 1 286 ? 28.419  3.295   -28.864 1.00 66.44  ?  272 GLU A CD    1 
ATOM   2061 O  OE1   . GLU A 1 286 ? 28.606  2.100   -28.545 1.00 67.38  ?  272 GLU A OE1   1 
ATOM   2062 O  OE2   . GLU A 1 286 ? 27.412  3.684   -29.495 1.00 71.03  ?  272 GLU A OE2   1 
ATOM   2063 N  N     . ALA A 1 287 ? 29.545  4.148   -24.509 1.00 48.13  ?  273 ALA A N     1 
ATOM   2064 C  CA    . ALA A 1 287 ? 30.333  3.222   -23.701 1.00 45.56  ?  273 ALA A CA    1 
ATOM   2065 C  C     . ALA A 1 287 ? 29.443  2.236   -22.953 1.00 56.25  ?  273 ALA A C     1 
ATOM   2066 O  O     . ALA A 1 287 ? 29.708  1.027   -22.940 1.00 45.29  ?  273 ALA A O     1 
ATOM   2067 C  CB    . ALA A 1 287 ? 31.212  4.000   -22.723 1.00 40.57  ?  273 ALA A CB    1 
ATOM   2068 N  N     . ILE A 1 288 ? 28.372  2.732   -22.333 1.00 48.68  ?  274 ILE A N     1 
ATOM   2069 C  CA    . ILE A 1 288 ? 27.538  1.891   -21.482 1.00 49.74  ?  274 ILE A CA    1 
ATOM   2070 C  C     . ILE A 1 288 ? 26.373  1.324   -22.281 1.00 40.08  ?  274 ILE A C     1 
ATOM   2071 O  O     . ILE A 1 288 ? 26.270  0.107   -22.462 1.00 44.41  ?  274 ILE A O     1 
ATOM   2072 C  CB    . ILE A 1 288 ? 27.028  2.673   -20.257 1.00 50.60  ?  274 ILE A CB    1 
ATOM   2073 C  CG1   . ILE A 1 288 ? 28.203  3.274   -19.487 1.00 46.91  ?  274 ILE A CG1   1 
ATOM   2074 C  CG2   . ILE A 1 288 ? 26.203  1.765   -19.358 1.00 38.58  ?  274 ILE A CG2   1 
ATOM   2075 C  CD1   . ILE A 1 288 ? 29.243  2.250   -19.082 1.00 42.45  ?  274 ILE A CD1   1 
ATOM   2076 N  N     . GLU A 1 289 ? 25.498  2.198   -22.780 1.00 44.40  ?  275 GLU A N     1 
ATOM   2077 C  CA    . GLU A 1 289 ? 24.309  1.734   -23.485 1.00 37.20  ?  275 GLU A CA    1 
ATOM   2078 C  C     . GLU A 1 289 ? 24.643  1.084   -24.819 1.00 42.73  ?  275 GLU A C     1 
ATOM   2079 O  O     . GLU A 1 289 ? 23.826  0.319   -25.343 1.00 46.58  ?  275 GLU A O     1 
ATOM   2080 C  CB    . GLU A 1 289 ? 23.331  2.890   -23.698 1.00 36.32  ?  275 GLU A CB    1 
ATOM   2081 C  CG    . GLU A 1 289 ? 22.656  3.355   -22.424 1.00 38.85  ?  275 GLU A CG    1 
ATOM   2082 C  CD    . GLU A 1 289 ? 21.635  4.450   -22.664 1.00 49.56  ?  275 GLU A CD    1 
ATOM   2083 O  OE1   . GLU A 1 289 ? 21.472  4.873   -23.831 1.00 45.52  ?  275 GLU A OE1   1 
ATOM   2084 O  OE2   . GLU A 1 289 ? 20.987  4.876   -21.684 1.00 41.31  ?  275 GLU A OE2   1 
ATOM   2085 N  N     . GLY A 1 290 ? 25.819  1.363   -25.377 1.00 39.12  ?  276 GLY A N     1 
ATOM   2086 C  CA    . GLY A 1 290 ? 26.210  0.750   -26.632 1.00 45.09  ?  276 GLY A CA    1 
ATOM   2087 C  C     . GLY A 1 290 ? 26.760  -0.654  -26.518 1.00 39.70  ?  276 GLY A C     1 
ATOM   2088 O  O     . GLY A 1 290 ? 26.876  -1.343  -27.535 1.00 44.53  ?  276 GLY A O     1 
ATOM   2089 N  N     . ALA A 1 291 ? 27.112  -1.086  -25.310 1.00 39.19  ?  277 ALA A N     1 
ATOM   2090 C  CA    . ALA A 1 291 ? 27.577  -2.447  -25.101 1.00 41.16  ?  277 ALA A CA    1 
ATOM   2091 C  C     . ALA A 1 291 ? 26.421  -3.434  -25.219 1.00 44.35  ?  277 ALA A C     1 
ATOM   2092 O  O     . ALA A 1 291 ? 25.270  -3.120  -24.901 1.00 40.84  ?  277 ALA A O     1 
ATOM   2093 C  CB    . ALA A 1 291 ? 28.240  -2.578  -23.730 1.00 37.08  ?  277 ALA A CB    1 
ATOM   2094 N  N     . ASP A 1 292 ? 26.731  -4.640  -25.696 1.00 36.40  ?  278 ASP A N     1 
ATOM   2095 C  CA    . ASP A 1 292 ? 25.703  -5.669  -25.781 1.00 44.95  ?  278 ASP A CA    1 
ATOM   2096 C  C     . ASP A 1 292 ? 25.454  -6.351  -24.444 1.00 44.17  ?  278 ASP A C     1 
ATOM   2097 O  O     . ASP A 1 292 ? 24.414  -6.997  -24.276 1.00 42.79  ?  278 ASP A O     1 
ATOM   2098 C  CB    . ASP A 1 292 ? 26.079  -6.712  -26.830 1.00 47.49  ?  278 ASP A CB    1 
ATOM   2099 C  CG    . ASP A 1 292 ? 27.466  -7.264  -26.617 1.00 58.93  ?  278 ASP A CG    1 
ATOM   2100 O  OD1   . ASP A 1 292 ? 27.666  -7.997  -25.624 1.00 64.68  ?  278 ASP A OD1   1 
ATOM   2101 O  OD2   . ASP A 1 292 ? 28.356  -6.960  -27.438 1.00 56.19  ?  278 ASP A OD2   1 
ATOM   2102 N  N     . THR A 1 293 ? 26.375  -6.215  -23.494 1.00 37.88  ?  279 THR A N     1 
ATOM   2103 C  CA    . THR A 1 293 ? 26.196  -6.747  -22.149 1.00 39.61  ?  279 THR A CA    1 
ATOM   2104 C  C     . THR A 1 293 ? 26.665  -5.702  -21.155 1.00 42.14  ?  279 THR A C     1 
ATOM   2105 O  O     . THR A 1 293 ? 27.819  -5.264  -21.214 1.00 40.64  ?  279 THR A O     1 
ATOM   2106 C  CB    . THR A 1 293 ? 26.975  -8.050  -21.950 1.00 47.16  ?  279 THR A CB    1 
ATOM   2107 O  OG1   . THR A 1 293 ? 26.574  -9.006  -22.938 1.00 48.81  ?  279 THR A OG1   1 
ATOM   2108 C  CG2   . THR A 1 293 ? 26.708  -8.613  -20.564 1.00 51.60  ?  279 THR A CG2   1 
ATOM   2109 N  N     . VAL A 1 294 ? 25.782  -5.309  -20.242 1.00 37.29  ?  280 VAL A N     1 
ATOM   2110 C  CA    . VAL A 1 294 ? 26.104  -4.333  -19.210 1.00 34.33  ?  280 VAL A CA    1 
ATOM   2111 C  C     . VAL A 1 294 ? 25.921  -4.997  -17.854 1.00 32.25  ?  280 VAL A C     1 
ATOM   2112 O  O     . VAL A 1 294 ? 24.846  -5.531  -17.555 1.00 31.10  ?  280 VAL A O     1 
ATOM   2113 C  CB    . VAL A 1 294 ? 25.247  -3.063  -19.329 1.00 36.80  ?  280 VAL A CB    1 
ATOM   2114 C  CG1   . VAL A 1 294 ? 25.550  -2.114  -18.177 1.00 35.45  ?  280 VAL A CG1   1 
ATOM   2115 C  CG2   . VAL A 1 294 ? 25.515  -2.376  -20.661 1.00 32.12  ?  280 VAL A CG2   1 
ATOM   2116 N  N     . LEU A 1 295 ? 26.974  -4.978  -17.046 1.00 33.72  ?  281 LEU A N     1 
ATOM   2117 C  CA    . LEU A 1 295 ? 26.922  -5.494  -15.684 1.00 32.20  ?  281 LEU A CA    1 
ATOM   2118 C  C     . LEU A 1 295 ? 26.507  -4.350  -14.764 1.00 37.50  ?  281 LEU A C     1 
ATOM   2119 O  O     . LEU A 1 295 ? 27.259  -3.384  -14.587 1.00 38.53  ?  281 LEU A O     1 
ATOM   2120 C  CB    . LEU A 1 295 ? 28.277  -6.077  -15.282 1.00 28.23  ?  281 LEU A CB    1 
ATOM   2121 C  CG    . LEU A 1 295 ? 28.962  -6.940  -16.345 1.00 39.32  ?  281 LEU A CG    1 
ATOM   2122 C  CD1   . LEU A 1 295 ? 30.281  -7.512  -15.837 1.00 46.76  ?  281 LEU A CD1   1 
ATOM   2123 C  CD2   . LEU A 1 295 ? 28.043  -8.066  -16.803 1.00 32.19  ?  281 LEU A CD2   1 
ATOM   2124 N  N     . CYS A 1 296 ? 25.302  -4.445  -14.198 1.00 32.32  ?  282 CYS A N     1 
ATOM   2125 C  CA    . CYS A 1 296 ? 24.770  -3.426  -13.297 1.00 26.27  ?  282 CYS A CA    1 
ATOM   2126 C  C     . CYS A 1 296 ? 24.954  -3.916  -11.867 1.00 32.31  ?  282 CYS A C     1 
ATOM   2127 O  O     . CYS A 1 296 ? 24.236  -4.813  -11.414 1.00 35.97  ?  282 CYS A O     1 
ATOM   2128 C  CB    . CYS A 1 296 ? 23.299  -3.148  -13.590 1.00 27.97  ?  282 CYS A CB    1 
ATOM   2129 S  SG    . CYS A 1 296 ? 22.976  -2.661  -15.286 1.00 38.21  ?  282 CYS A SG    1 
ATOM   2130 N  N     . ILE A 1 297 ? 25.888  -3.306  -11.149 1.00 28.52  ?  283 ILE A N     1 
ATOM   2131 C  CA    . ILE A 1 297 ? 26.290  -3.769  -9.828  1.00 33.65  ?  283 ILE A CA    1 
ATOM   2132 C  C     . ILE A 1 297 ? 25.805  -2.755  -8.803  1.00 30.13  ?  283 ILE A C     1 
ATOM   2133 O  O     . ILE A 1 297 ? 26.353  -1.650  -8.707  1.00 31.26  ?  283 ILE A O     1 
ATOM   2134 C  CB    . ILE A 1 297 ? 27.810  -3.961  -9.737  1.00 26.00  ?  283 ILE A CB    1 
ATOM   2135 C  CG1   . ILE A 1 297 ? 28.326  -4.782  -10.925 1.00 34.94  ?  283 ILE A CG1   1 
ATOM   2136 C  CG2   . ILE A 1 297 ? 28.181  -4.583  -8.409  1.00 26.07  ?  283 ILE A CG2   1 
ATOM   2137 C  CD1   . ILE A 1 297 ? 27.721  -6.184  -11.036 1.00 25.95  ?  283 ILE A CD1   1 
ATOM   2138 N  N     . GLY A 1 298 ? 24.817  -3.148  -8.003  1.00 24.05  ?  284 GLY A N     1 
ATOM   2139 C  CA    . GLY A 1 298 ? 24.293  -2.280  -6.960  1.00 30.32  ?  284 GLY A CA    1 
ATOM   2140 C  C     . GLY A 1 298 ? 23.636  -1.020  -7.484  1.00 36.27  ?  284 GLY A C     1 
ATOM   2141 O  O     . GLY A 1 298 ? 23.834  0.063   -6.920  1.00 35.96  ?  284 GLY A O     1 
ATOM   2142 N  N     . THR A 1 299 ? 22.859  -1.139  -8.556  1.00 31.24  ?  285 THR A N     1 
ATOM   2143 C  CA    . THR A 1 299 ? 22.274  -0.000  -9.250  1.00 30.27  ?  285 THR A CA    1 
ATOM   2144 C  C     . THR A 1 299 ? 20.800  0.148   -8.891  1.00 39.29  ?  285 THR A C     1 
ATOM   2145 O  O     . THR A 1 299 ? 20.087  -0.848  -8.721  1.00 29.31  ?  285 THR A O     1 
ATOM   2146 C  CB    . THR A 1 299 ? 22.408  -0.167  -10.764 1.00 31.52  ?  285 THR A CB    1 
ATOM   2147 O  OG1   . THR A 1 299 ? 22.016  -1.498  -11.125 1.00 41.18  ?  285 THR A OG1   1 
ATOM   2148 C  CG2   . THR A 1 299 ? 23.844  0.066   -11.211 1.00 24.57  ?  285 THR A CG2   1 
ATOM   2149 N  N     . ARG A 1 300 ? 20.353  1.399   -8.765  1.00 33.21  ?  286 ARG A N     1 
ATOM   2150 C  CA    . ARG A 1 300 ? 18.939  1.732   -8.619  1.00 33.36  ?  286 ARG A CA    1 
ATOM   2151 C  C     . ARG A 1 300 ? 18.643  2.873   -9.577  1.00 36.38  ?  286 ARG A C     1 
ATOM   2152 O  O     . ARG A 1 300 ? 19.199  3.965   -9.429  1.00 33.84  ?  286 ARG A O     1 
ATOM   2153 C  CB    . ARG A 1 300 ? 18.586  2.126   -7.181  1.00 32.84  ?  286 ARG A CB    1 
ATOM   2154 C  CG    . ARG A 1 300 ? 18.800  1.028   -6.147  1.00 34.35  ?  286 ARG A CG    1 
ATOM   2155 C  CD    . ARG A 1 300 ? 17.883  -0.170  -6.393  1.00 34.68  ?  286 ARG A CD    1 
ATOM   2156 N  NE    . ARG A 1 300 ? 18.359  -1.378  -5.726  1.00 30.26  ?  286 ARG A NE    1 
ATOM   2157 C  CZ    . ARG A 1 300 ? 18.049  -1.721  -4.482  1.00 33.43  ?  286 ARG A CZ    1 
ATOM   2158 N  NH1   . ARG A 1 300 ? 17.272  -0.959  -3.729  1.00 29.93  ?  286 ARG A NH1   1 
ATOM   2159 N  NH2   . ARG A 1 300 ? 18.521  -2.866  -3.986  1.00 23.82  ?  286 ARG A NH2   1 
ATOM   2160 N  N     . PHE A 1 301 ? 17.775  2.623   -10.559 1.00 32.25  ?  287 PHE A N     1 
ATOM   2161 C  CA    . PHE A 1 301 ? 17.529  3.590   -11.629 1.00 37.50  ?  287 PHE A CA    1 
ATOM   2162 C  C     . PHE A 1 301 ? 16.441  4.566   -11.184 1.00 37.73  ?  287 PHE A C     1 
ATOM   2163 O  O     . PHE A 1 301 ? 15.272  4.468   -11.567 1.00 32.49  ?  287 PHE A O     1 
ATOM   2164 C  CB    . PHE A 1 301 ? 17.158  2.866   -12.918 1.00 32.57  ?  287 PHE A CB    1 
ATOM   2165 C  CG    . PHE A 1 301 ? 18.285  2.054   -13.501 1.00 37.05  ?  287 PHE A CG    1 
ATOM   2166 C  CD1   . PHE A 1 301 ? 19.347  2.677   -14.143 1.00 32.53  ?  287 PHE A CD1   1 
ATOM   2167 C  CD2   . PHE A 1 301 ? 18.287  0.670   -13.398 1.00 37.39  ?  287 PHE A CD2   1 
ATOM   2168 C  CE1   . PHE A 1 301 ? 20.390  1.936   -14.680 1.00 37.46  ?  287 PHE A CE1   1 
ATOM   2169 C  CE2   . PHE A 1 301 ? 19.322  -0.079  -13.931 1.00 35.28  ?  287 PHE A CE2   1 
ATOM   2170 C  CZ    . PHE A 1 301 ? 20.376  0.551   -14.572 1.00 40.56  ?  287 PHE A CZ    1 
ATOM   2171 N  N     . THR A 1 302 ? 16.848  5.547   -10.378 1.00 29.79  ?  288 THR A N     1 
ATOM   2172 C  CA    . THR A 1 302 ? 15.910  6.553   -9.895  1.00 29.99  ?  288 THR A CA    1 
ATOM   2173 C  C     . THR A 1 302 ? 15.666  7.618   -10.961 1.00 24.87  ?  288 THR A C     1 
ATOM   2174 O  O     . THR A 1 302 ? 16.369  7.697   -11.972 1.00 31.70  ?  288 THR A O     1 
ATOM   2175 C  CB    . THR A 1 302 ? 16.417  7.201   -8.609  1.00 28.82  ?  288 THR A CB    1 
ATOM   2176 O  OG1   . THR A 1 302 ? 17.418  8.178   -8.931  1.00 36.07  ?  288 THR A OG1   1 
ATOM   2177 C  CG2   . THR A 1 302 ? 17.003  6.152   -7.675  1.00 31.23  ?  288 THR A CG2   1 
ATOM   2178 N  N     . ASP A 1 303 ? 14.647  8.453   -10.720 1.00 26.99  ?  289 ASP A N     1 
ATOM   2179 C  CA    . ASP A 1 303 ? 14.270  9.459   -11.712 1.00 29.18  ?  289 ASP A CA    1 
ATOM   2180 C  C     . ASP A 1 303 ? 15.395  10.466  -11.957 1.00 36.71  ?  289 ASP A C     1 
ATOM   2181 O  O     . ASP A 1 303 ? 15.687  10.811  -13.108 1.00 32.61  ?  289 ASP A O     1 
ATOM   2182 C  CB    . ASP A 1 303 ? 12.981  10.170  -11.283 1.00 31.54  ?  289 ASP A CB    1 
ATOM   2183 C  CG    . ASP A 1 303 ? 13.075  10.804  -9.899  1.00 35.87  ?  289 ASP A CG    1 
ATOM   2184 O  OD1   . ASP A 1 303 ? 14.076  10.575  -9.182  1.00 41.93  ?  289 ASP A OD1   1 
ATOM   2185 O  OD2   . ASP A 1 303 ? 12.132  11.532  -9.523  1.00 36.11  ?  289 ASP A OD2   1 
ATOM   2186 N  N     . THR A 1 304 ? 16.044  10.941  -10.890 1.00 32.17  ?  290 THR A N     1 
ATOM   2187 C  CA    . THR A 1 304 ? 17.126  11.911  -11.059 1.00 34.29  ?  290 THR A CA    1 
ATOM   2188 C  C     . THR A 1 304 ? 18.343  11.285  -11.734 1.00 40.63  ?  290 THR A C     1 
ATOM   2189 O  O     . THR A 1 304 ? 18.933  11.882  -12.644 1.00 34.52  ?  290 THR A O     1 
ATOM   2190 C  CB    . THR A 1 304 ? 17.522  12.499  -9.705  1.00 34.88  ?  290 THR A CB    1 
ATOM   2191 O  OG1   . THR A 1 304 ? 16.413  13.214  -9.145  1.00 46.58  ?  290 THR A OG1   1 
ATOM   2192 C  CG2   . THR A 1 304 ? 18.707  13.449  -9.859  1.00 45.48  ?  290 THR A CG2   1 
ATOM   2193 N  N     . LEU A 1 305 ? 18.716  10.072  -11.317 1.00 33.04  ?  291 LEU A N     1 
ATOM   2194 C  CA    . LEU A 1 305 ? 19.918  9.435   -11.845 1.00 37.21  ?  291 LEU A CA    1 
ATOM   2195 C  C     . LEU A 1 305 ? 19.797  9.141   -13.329 1.00 35.29  ?  291 LEU A C     1 
ATOM   2196 O  O     . LEU A 1 305 ? 20.812  9.073   -14.030 1.00 42.36  ?  291 LEU A O     1 
ATOM   2197 C  CB    . LEU A 1 305 ? 20.204  8.139   -11.089 1.00 28.47  ?  291 LEU A CB    1 
ATOM   2198 C  CG    . LEU A 1 305 ? 21.171  8.235   -9.914  1.00 33.74  ?  291 LEU A CG    1 
ATOM   2199 C  CD1   . LEU A 1 305 ? 20.665  9.251   -8.903  1.00 30.34  ?  291 LEU A CD1   1 
ATOM   2200 C  CD2   . LEU A 1 305 ? 21.337  6.854   -9.272  1.00 34.58  ?  291 LEU A CD2   1 
ATOM   2201 N  N     . THR A 1 306 ? 18.576  8.951   -13.824 1.00 35.26  ?  292 THR A N     1 
ATOM   2202 C  CA    . THR A 1 306 ? 18.349  8.579   -15.213 1.00 39.97  ?  292 THR A CA    1 
ATOM   2203 C  C     . THR A 1 306 ? 17.732  9.706   -16.029 1.00 42.83  ?  292 THR A C     1 
ATOM   2204 O  O     . THR A 1 306 ? 17.246  9.456   -17.138 1.00 42.71  ?  292 THR A O     1 
ATOM   2205 C  CB    . THR A 1 306 ? 17.468  7.333   -15.284 1.00 43.53  ?  292 THR A CB    1 
ATOM   2206 O  OG1   . THR A 1 306 ? 16.248  7.579   -14.577 1.00 36.47  ?  292 THR A OG1   1 
ATOM   2207 C  CG2   . THR A 1 306 ? 18.187  6.153   -14.641 1.00 31.64  ?  292 THR A CG2   1 
ATOM   2208 N  N     . ALA A 1 307 ? 17.725  10.931  -15.500 1.00 43.41  ?  293 ALA A N     1 
ATOM   2209 C  CA    . ALA A 1 307 ? 17.158  12.095  -16.179 1.00 46.36  ?  293 ALA A CA    1 
ATOM   2210 C  C     . ALA A 1 307 ? 15.746  11.809  -16.683 1.00 41.25  ?  293 ALA A C     1 
ATOM   2211 O  O     . ALA A 1 307 ? 15.427  11.994  -17.859 1.00 53.43  ?  293 ALA A O     1 
ATOM   2212 C  CB    . ALA A 1 307 ? 18.063  12.560  -17.322 1.00 37.96  ?  293 ALA A CB    1 
ATOM   2213 N  N     . GLY A 1 308 ? 14.897  11.329  -15.779 1.00 42.61  ?  294 GLY A N     1 
ATOM   2214 C  CA    . GLY A 1 308 ? 13.513  11.066  -16.126 1.00 38.98  ?  294 GLY A CA    1 
ATOM   2215 C  C     . GLY A 1 308 ? 13.269  9.685   -16.699 1.00 39.61  ?  294 GLY A C     1 
ATOM   2216 O  O     . GLY A 1 308 ? 12.443  9.523   -17.602 1.00 42.01  ?  294 GLY A O     1 
ATOM   2217 N  N     . PHE A 1 309 ? 13.991  8.683   -16.187 1.00 41.03  ?  295 PHE A N     1 
ATOM   2218 C  CA    . PHE A 1 309 ? 13.851  7.290   -16.628 1.00 38.66  ?  295 PHE A CA    1 
ATOM   2219 C  C     . PHE A 1 309 ? 14.079  7.149   -18.131 1.00 34.78  ?  295 PHE A C     1 
ATOM   2220 O  O     . PHE A 1 309 ? 13.397  6.376   -18.810 1.00 41.15  ?  295 PHE A O     1 
ATOM   2221 C  CB    . PHE A 1 309 ? 12.488  6.717   -16.233 1.00 35.93  ?  295 PHE A CB    1 
ATOM   2222 C  CG    . PHE A 1 309 ? 12.214  6.774   -14.761 1.00 38.27  ?  295 PHE A CG    1 
ATOM   2223 C  CD1   . PHE A 1 309 ? 13.034  6.114   -13.866 1.00 29.65  ?  295 PHE A CD1   1 
ATOM   2224 C  CD2   . PHE A 1 309 ? 11.134  7.491   -14.271 1.00 38.32  ?  295 PHE A CD2   1 
ATOM   2225 C  CE1   . PHE A 1 309 ? 12.786  6.165   -12.510 1.00 35.33  ?  295 PHE A CE1   1 
ATOM   2226 C  CE2   . PHE A 1 309 ? 10.879  7.544   -12.915 1.00 40.06  ?  295 PHE A CE2   1 
ATOM   2227 C  CZ    . PHE A 1 309 ? 11.709  6.880   -12.032 1.00 34.73  ?  295 PHE A CZ    1 
ATOM   2228 N  N     . THR A 1 310 ? 15.052  7.892   -18.656 1.00 34.94  ?  296 THR A N     1 
ATOM   2229 C  CA    . THR A 1 310 ? 15.394  7.843   -20.071 1.00 39.18  ?  296 THR A CA    1 
ATOM   2230 C  C     . THR A 1 310 ? 16.576  6.924   -20.361 1.00 42.27  ?  296 THR A C     1 
ATOM   2231 O  O     . THR A 1 310 ? 17.128  6.967   -21.465 1.00 37.91  ?  296 THR A O     1 
ATOM   2232 C  CB    . THR A 1 310 ? 15.680  9.250   -20.599 1.00 43.93  ?  296 THR A CB    1 
ATOM   2233 O  OG1   . THR A 1 310 ? 16.813  9.796   -19.914 1.00 49.14  ?  296 THR A OG1   1 
ATOM   2234 C  CG2   . THR A 1 310 ? 14.471  10.159  -20.389 1.00 40.76  ?  296 THR A CG2   1 
ATOM   2235 N  N     . HIS A 1 311 ? 16.980  6.101   -19.397 1.00 36.02  ?  297 HIS A N     1 
ATOM   2236 C  CA    . HIS A 1 311 ? 18.007  5.102   -19.652 1.00 36.70  ?  297 HIS A CA    1 
ATOM   2237 C  C     . HIS A 1 311 ? 17.488  4.045   -20.617 1.00 37.22  ?  297 HIS A C     1 
ATOM   2238 O  O     . HIS A 1 311 ? 16.307  3.691   -20.596 1.00 46.51  ?  297 HIS A O     1 
ATOM   2239 C  CB    . HIS A 1 311 ? 18.450  4.443   -18.345 1.00 32.61  ?  297 HIS A CB    1 
ATOM   2240 C  CG    . HIS A 1 311 ? 17.331  3.832   -17.563 1.00 37.87  ?  297 HIS A CG    1 
ATOM   2241 N  ND1   . HIS A 1 311 ? 16.249  4.560   -17.115 1.00 34.24  ?  297 HIS A ND1   1 
ATOM   2242 C  CD2   . HIS A 1 311 ? 17.130  2.561   -17.138 1.00 32.66  ?  297 HIS A CD2   1 
ATOM   2243 C  CE1   . HIS A 1 311 ? 15.427  3.764   -16.454 1.00 38.94  ?  297 HIS A CE1   1 
ATOM   2244 N  NE2   . HIS A 1 311 ? 15.940  2.547   -16.451 1.00 39.74  ?  297 HIS A NE2   1 
ATOM   2245 N  N     . GLN A 1 312 ? 18.374  3.551   -21.477 1.00 38.47  ?  298 GLN A N     1 
ATOM   2246 C  CA    . GLN A 1 312 ? 18.034  2.532   -22.469 1.00 42.93  ?  298 GLN A CA    1 
ATOM   2247 C  C     . GLN A 1 312 ? 18.881  1.290   -22.195 1.00 46.72  ?  298 GLN A C     1 
ATOM   2248 O  O     . GLN A 1 312 ? 19.949  1.102   -22.785 1.00 44.72  ?  298 GLN A O     1 
ATOM   2249 C  CB    . GLN A 1 312 ? 18.245  3.055   -23.882 1.00 39.89  ?  298 GLN A CB    1 
ATOM   2250 C  CG    . GLN A 1 312 ? 17.575  4.391   -24.147 1.00 55.40  ?  298 GLN A CG    1 
ATOM   2251 C  CD    . GLN A 1 312 ? 17.241  4.595   -25.610 1.00 65.82  ?  298 GLN A CD    1 
ATOM   2252 O  OE1   . GLN A 1 312 ? 16.626  3.736   -26.243 1.00 81.77  ?  298 GLN A OE1   1 
ATOM   2253 N  NE2   . GLN A 1 312 ? 17.649  5.736   -26.157 1.00 65.19  ?  298 GLN A NE2   1 
ATOM   2254 N  N     . LEU A 1 313 ? 18.391  0.436   -21.300 1.00 36.44  ?  299 LEU A N     1 
ATOM   2255 C  CA    . LEU A 1 313 ? 19.039  -0.831  -20.983 1.00 46.55  ?  299 LEU A CA    1 
ATOM   2256 C  C     . LEU A 1 313 ? 17.957  -1.894  -20.868 1.00 43.37  ?  299 LEU A C     1 
ATOM   2257 O  O     . LEU A 1 313 ? 17.062  -1.773  -20.026 1.00 43.23  ?  299 LEU A O     1 
ATOM   2258 C  CB    . LEU A 1 313 ? 19.850  -0.734  -19.686 1.00 34.57  ?  299 LEU A CB    1 
ATOM   2259 C  CG    . LEU A 1 313 ? 21.080  0.175   -19.696 1.00 38.05  ?  299 LEU A CG    1 
ATOM   2260 C  CD1   . LEU A 1 313 ? 21.528  0.476   -18.276 1.00 36.76  ?  299 LEU A CD1   1 
ATOM   2261 C  CD2   . LEU A 1 313 ? 22.221  -0.439  -20.505 1.00 37.72  ?  299 LEU A CD2   1 
ATOM   2262 N  N     . THR A 1 314 ? 18.017  -2.915  -21.729 1.00 40.20  ?  300 THR A N     1 
ATOM   2263 C  CA    . THR A 1 314 ? 17.000  -3.955  -21.728 1.00 41.00  ?  300 THR A CA    1 
ATOM   2264 C  C     . THR A 1 314 ? 17.387  -5.081  -20.781 1.00 48.45  ?  300 THR A C     1 
ATOM   2265 O  O     . THR A 1 314 ? 18.563  -5.244  -20.435 1.00 40.61  ?  300 THR A O     1 
ATOM   2266 C  CB    . THR A 1 314 ? 16.799  -4.513  -23.139 1.00 39.06  ?  300 THR A CB    1 
ATOM   2267 O  OG1   . THR A 1 314 ? 17.912  -5.345  -23.495 1.00 48.98  ?  300 THR A OG1   1 
ATOM   2268 C  CG2   . THR A 1 314 ? 16.644  -3.392  -24.158 1.00 37.88  ?  300 THR A CG2   1 
ATOM   2269 N  N     . PRO A 1 315 ? 16.407  -5.867  -20.322 1.00 46.66  ?  301 PRO A N     1 
ATOM   2270 C  CA    . PRO A 1 315 ? 16.744  -7.012  -19.455 1.00 35.82  ?  301 PRO A CA    1 
ATOM   2271 C  C     . PRO A 1 315 ? 17.718  -7.995  -20.084 1.00 39.57  ?  301 PRO A C     1 
ATOM   2272 O  O     . PRO A 1 315 ? 18.618  -8.490  -19.393 1.00 39.21  ?  301 PRO A O     1 
ATOM   2273 C  CB    . PRO A 1 315 ? 15.375  -7.658  -19.194 1.00 33.45  ?  301 PRO A CB    1 
ATOM   2274 C  CG    . PRO A 1 315 ? 14.396  -6.525  -19.331 1.00 39.91  ?  301 PRO A CG    1 
ATOM   2275 C  CD    . PRO A 1 315 ? 14.954  -5.624  -20.395 1.00 37.93  ?  301 PRO A CD    1 
ATOM   2276 N  N     . SER A 1 316 ? 17.578  -8.284  -21.380 1.00 41.59  ?  302 SER A N     1 
ATOM   2277 C  CA    . SER A 1 316 ? 18.495  -9.216  -22.030 1.00 37.34  ?  302 SER A CA    1 
ATOM   2278 C  C     . SER A 1 316 ? 19.891  -8.628  -22.153 1.00 44.81  ?  302 SER A C     1 
ATOM   2279 O  O     . SER A 1 316 ? 20.875  -9.374  -22.210 1.00 44.96  ?  302 SER A O     1 
ATOM   2280 C  CB    . SER A 1 316 ? 17.964  -9.616  -23.406 1.00 46.37  ?  302 SER A CB    1 
ATOM   2281 O  OG    . SER A 1 316 ? 17.781  -8.480  -24.230 1.00 65.54  ?  302 SER A OG    1 
ATOM   2282 N  N     . GLN A 1 317 ? 19.995  -7.300  -22.192 1.00 42.58  ?  303 GLN A N     1 
ATOM   2283 C  CA    . GLN A 1 317 ? 21.279  -6.631  -22.308 1.00 39.69  ?  303 GLN A CA    1 
ATOM   2284 C  C     . GLN A 1 317 ? 22.053  -6.620  -20.996 1.00 41.54  ?  303 GLN A C     1 
ATOM   2285 O  O     . GLN A 1 317 ? 23.265  -6.400  -21.012 1.00 40.88  ?  303 GLN A O     1 
ATOM   2286 C  CB    . GLN A 1 317 ? 21.055  -5.192  -22.801 1.00 36.25  ?  303 GLN A CB    1 
ATOM   2287 C  CG    . GLN A 1 317 ? 22.306  -4.366  -23.100 1.00 37.95  ?  303 GLN A CG    1 
ATOM   2288 C  CD    . GLN A 1 317 ? 21.983  -2.908  -23.425 1.00 48.60  ?  303 GLN A CD    1 
ATOM   2289 O  OE1   . GLN A 1 317 ? 20.843  -2.462  -23.269 1.00 49.25  ?  303 GLN A OE1   1 
ATOM   2290 N  NE2   . GLN A 1 317 ? 22.987  -2.162  -23.874 1.00 39.33  ?  303 GLN A NE2   1 
ATOM   2291 N  N     . THR A 1 318 ? 21.403  -6.890  -19.868 1.00 35.46  ?  304 THR A N     1 
ATOM   2292 C  CA    . THR A 1 318 ? 21.991  -6.594  -18.571 1.00 33.66  ?  304 THR A CA    1 
ATOM   2293 C  C     . THR A 1 318 ? 22.103  -7.833  -17.690 1.00 38.60  ?  304 THR A C     1 
ATOM   2294 O  O     . THR A 1 318 ? 21.314  -8.775  -17.793 1.00 41.25  ?  304 THR A O     1 
ATOM   2295 C  CB    . THR A 1 318 ? 21.186  -5.518  -17.825 1.00 30.27  ?  304 THR A CB    1 
ATOM   2296 O  OG1   . THR A 1 318 ? 19.794  -5.863  -17.834 1.00 36.01  ?  304 THR A OG1   1 
ATOM   2297 C  CG2   . THR A 1 318 ? 21.373  -4.163  -18.487 1.00 32.17  ?  304 THR A CG2   1 
ATOM   2298 N  N     . ILE A 1 319 ? 23.127  -7.817  -16.842 1.00 36.61  ?  305 ILE A N     1 
ATOM   2299 C  CA    . ILE A 1 319 ? 23.246  -8.691  -15.682 1.00 33.33  ?  305 ILE A CA    1 
ATOM   2300 C  C     . ILE A 1 319 ? 23.279  -7.784  -14.462 1.00 37.47  ?  305 ILE A C     1 
ATOM   2301 O  O     . ILE A 1 319 ? 24.039  -6.806  -14.431 1.00 31.15  ?  305 ILE A O     1 
ATOM   2302 C  CB    . ILE A 1 319 ? 24.504  -9.576  -15.747 1.00 27.56  ?  305 ILE A CB    1 
ATOM   2303 C  CG1   . ILE A 1 319 ? 24.415  -10.550 -16.921 1.00 28.66  ?  305 ILE A CG1   1 
ATOM   2304 C  CG2   . ILE A 1 319 ? 24.702  -10.331 -14.436 1.00 27.28  ?  305 ILE A CG2   1 
ATOM   2305 C  CD1   . ILE A 1 319 ? 25.728  -11.242 -17.221 1.00 29.23  ?  305 ILE A CD1   1 
ATOM   2306 N  N     . GLU A 1 320 ? 22.424  -8.068  -13.485 1.00 30.20  ?  306 GLU A N     1 
ATOM   2307 C  CA    . GLU A 1 320 ? 22.182  -7.153  -12.377 1.00 37.72  ?  306 GLU A CA    1 
ATOM   2308 C  C     . GLU A 1 320 ? 22.524  -7.835  -11.059 1.00 36.19  ?  306 GLU A C     1 
ATOM   2309 O  O     . GLU A 1 320 ? 22.143  -8.987  -10.837 1.00 32.72  ?  306 GLU A O     1 
ATOM   2310 C  CB    . GLU A 1 320 ? 20.719  -6.687  -12.390 1.00 32.17  ?  306 GLU A CB    1 
ATOM   2311 C  CG    . GLU A 1 320 ? 20.278  -5.904  -11.170 1.00 38.37  ?  306 GLU A CG    1 
ATOM   2312 C  CD    . GLU A 1 320 ? 18.820  -5.467  -11.254 1.00 50.87  ?  306 GLU A CD    1 
ATOM   2313 O  OE1   . GLU A 1 320 ? 18.159  -5.732  -12.289 1.00 37.39  ?  306 GLU A OE1   1 
ATOM   2314 O  OE2   . GLU A 1 320 ? 18.332  -4.871  -10.272 1.00 46.69  ?  306 GLU A OE2   1 
ATOM   2315 N  N     . VAL A 1 321 ? 23.244  -7.130  -10.189 1.00 27.19  ?  307 VAL A N     1 
ATOM   2316 C  CA    . VAL A 1 321 ? 23.624  -7.659  -8.885  1.00 29.01  ?  307 VAL A CA    1 
ATOM   2317 C  C     . VAL A 1 321 ? 23.058  -6.742  -7.808  1.00 32.56  ?  307 VAL A C     1 
ATOM   2318 O  O     . VAL A 1 321 ? 23.379  -5.544  -7.769  1.00 27.71  ?  307 VAL A O     1 
ATOM   2319 C  CB    . VAL A 1 321 ? 25.147  -7.802  -8.742  1.00 25.14  ?  307 VAL A CB    1 
ATOM   2320 C  CG1   . VAL A 1 321 ? 25.510  -8.134  -7.301  1.00 25.81  ?  307 VAL A CG1   1 
ATOM   2321 C  CG2   . VAL A 1 321 ? 25.664  -8.874  -9.684  1.00 25.71  ?  307 VAL A CG2   1 
ATOM   2322 N  N     . GLN A 1 322 ? 22.234  -7.315  -6.920  1.00 25.76  ?  308 GLN A N     1 
ATOM   2323 C  CA    . GLN A 1 322 ? 21.609  -6.602  -5.813  1.00 31.99  ?  308 GLN A CA    1 
ATOM   2324 C  C     . GLN A 1 322 ? 22.042  -7.268  -4.508  1.00 27.63  ?  308 GLN A C     1 
ATOM   2325 O  O     . GLN A 1 322 ? 22.628  -8.353  -4.552  1.00 31.83  ?  308 GLN A O     1 
ATOM   2326 C  CB    . GLN A 1 322 ? 20.084  -6.591  -5.986  1.00 30.36  ?  308 GLN A CB    1 
ATOM   2327 C  CG    . GLN A 1 322 ? 19.626  -5.824  -7.217  1.00 26.65  ?  308 GLN A CG    1 
ATOM   2328 C  CD    . GLN A 1 322 ? 19.948  -4.333  -7.140  1.00 41.64  ?  308 GLN A CD    1 
ATOM   2329 O  OE1   . GLN A 1 322 ? 20.110  -3.769  -6.055  1.00 29.38  ?  308 GLN A OE1   1 
ATOM   2330 N  NE2   . GLN A 1 322 ? 20.040  -3.692  -8.300  1.00 30.87  ?  308 GLN A NE2   1 
ATOM   2331 N  N     . PRO A 1 323 ? 21.782  -6.663  -3.338  1.00 33.45  ?  309 PRO A N     1 
ATOM   2332 C  CA    . PRO A 1 323 ? 22.397  -7.173  -2.097  1.00 33.07  ?  309 PRO A CA    1 
ATOM   2333 C  C     . PRO A 1 323 ? 22.161  -8.647  -1.801  1.00 40.16  ?  309 PRO A C     1 
ATOM   2334 O  O     . PRO A 1 323 ? 23.085  -9.327  -1.332  1.00 35.73  ?  309 PRO A O     1 
ATOM   2335 C  CB    . PRO A 1 323 ? 21.766  -6.279  -1.022  1.00 36.34  ?  309 PRO A CB    1 
ATOM   2336 C  CG    . PRO A 1 323 ? 21.544  -4.988  -1.717  1.00 36.67  ?  309 PRO A CG    1 
ATOM   2337 C  CD    . PRO A 1 323 ? 21.183  -5.328  -3.135  1.00 32.93  ?  309 PRO A CD    1 
ATOM   2338 N  N     . HIS A 1 324 ? 20.967  -9.172  -2.062  1.00 33.94  ?  310 HIS A N     1 
ATOM   2339 C  CA    . HIS A 1 324 ? 20.678  -10.567 -1.750  1.00 41.36  ?  310 HIS A CA    1 
ATOM   2340 C  C     . HIS A 1 324 ? 20.264  -11.374 -2.972  1.00 30.06  ?  310 HIS A C     1 
ATOM   2341 O  O     . HIS A 1 324 ? 19.893  -12.540 -2.827  1.00 30.64  ?  310 HIS A O     1 
ATOM   2342 C  CB    . HIS A 1 324 ? 19.594  -10.656 -0.673  1.00 36.16  ?  310 HIS A CB    1 
ATOM   2343 C  CG    . HIS A 1 324 ? 19.917  -9.888  0.571   1.00 46.15  ?  310 HIS A CG    1 
ATOM   2344 N  ND1   . HIS A 1 324 ? 20.817  -10.340 1.512   1.00 39.95  ?  310 HIS A ND1   1 
ATOM   2345 C  CD2   . HIS A 1 324 ? 19.464  -8.695  1.026   1.00 39.47  ?  310 HIS A CD2   1 
ATOM   2346 C  CE1   . HIS A 1 324 ? 20.902  -9.460  2.494   1.00 52.21  ?  310 HIS A CE1   1 
ATOM   2347 N  NE2   . HIS A 1 324 ? 20.090  -8.454  2.225   1.00 46.27  ?  310 HIS A NE2   1 
ATOM   2348 N  N     . ALA A 1 325 ? 20.307  -10.789 -4.167  1.00 27.75  ?  311 ALA A N     1 
ATOM   2349 C  CA    . ALA A 1 325 ? 19.848  -11.499 -5.349  1.00 28.87  ?  311 ALA A CA    1 
ATOM   2350 C  C     . ALA A 1 325 ? 20.483  -10.884 -6.585  1.00 32.01  ?  311 ALA A C     1 
ATOM   2351 O  O     . ALA A 1 325 ? 20.824  -9.698  -6.603  1.00 32.25  ?  311 ALA A O     1 
ATOM   2352 C  CB    . ALA A 1 325 ? 18.318  -11.470 -5.461  1.00 30.22  ?  311 ALA A CB    1 
ATOM   2353 N  N     . SER A 1 326 ? 20.629  -11.705 -7.619  1.00 30.15  ?  312 SER A N     1 
ATOM   2354 C  CA    . SER A 1 326 ? 21.192  -11.264 -8.883  1.00 28.97  ?  312 SER A CA    1 
ATOM   2355 C  C     . SER A 1 326 ? 20.330  -11.776 -10.026 1.00 31.45  ?  312 SER A C     1 
ATOM   2356 O  O     . SER A 1 326 ? 19.618  -12.778 -9.900  1.00 27.97  ?  312 SER A O     1 
ATOM   2357 C  CB    . SER A 1 326 ? 22.643  -11.737 -9.052  1.00 29.39  ?  312 SER A CB    1 
ATOM   2358 O  OG    . SER A 1 326 ? 23.496  -11.066 -8.142  1.00 29.14  ?  312 SER A OG    1 
ATOM   2359 N  N     . ARG A 1 327 ? 20.405  -11.074 -11.152 1.00 29.96  ?  313 ARG A N     1 
ATOM   2360 C  CA    . ARG A 1 327 ? 19.569  -11.370 -12.304 1.00 36.75  ?  313 ARG A CA    1 
ATOM   2361 C  C     . ARG A 1 327 ? 20.429  -11.527 -13.547 1.00 36.52  ?  313 ARG A C     1 
ATOM   2362 O  O     . ARG A 1 327 ? 21.381  -10.767 -13.759 1.00 36.87  ?  313 ARG A O     1 
ATOM   2363 C  CB    . ARG A 1 327 ? 18.523  -10.269 -12.525 1.00 29.15  ?  313 ARG A CB    1 
ATOM   2364 C  CG    . ARG A 1 327 ? 17.764  -10.394 -13.834 1.00 36.67  ?  313 ARG A CG    1 
ATOM   2365 C  CD    . ARG A 1 327 ? 16.786  -9.241  -14.029 1.00 39.01  ?  313 ARG A CD    1 
ATOM   2366 N  NE    . ARG A 1 327 ? 17.453  -7.945  -14.095 1.00 41.58  ?  313 ARG A NE    1 
ATOM   2367 C  CZ    . ARG A 1 327 ? 18.103  -7.483  -15.155 1.00 37.63  ?  313 ARG A CZ    1 
ATOM   2368 N  NH1   . ARG A 1 327 ? 18.209  -8.194  -16.268 1.00 30.68  ?  313 ARG A NH1   1 
ATOM   2369 N  NH2   . ARG A 1 327 ? 18.652  -6.273  -15.101 1.00 30.77  ?  313 ARG A NH2   1 
ATOM   2370 N  N     . VAL A 1 328 ? 20.110  -12.537 -14.349 1.00 30.36  ?  314 VAL A N     1 
ATOM   2371 C  CA    . VAL A 1 328 ? 20.676  -12.697 -15.682 1.00 32.06  ?  314 VAL A CA    1 
ATOM   2372 C  C     . VAL A 1 328 ? 19.499  -12.714 -16.644 1.00 33.45  ?  314 VAL A C     1 
ATOM   2373 O  O     . VAL A 1 328 ? 18.653  -13.616 -16.582 1.00 30.37  ?  314 VAL A O     1 
ATOM   2374 C  CB    . VAL A 1 328 ? 21.524  -13.968 -15.809 1.00 34.20  ?  314 VAL A CB    1 
ATOM   2375 C  CG1   . VAL A 1 328 ? 22.109  -14.071 -17.203 1.00 29.83  ?  314 VAL A CG1   1 
ATOM   2376 C  CG2   . VAL A 1 328 ? 22.627  -13.981 -14.753 1.00 28.59  ?  314 VAL A CG2   1 
ATOM   2377 N  N     . GLY A 1 329 ? 19.420  -11.706 -17.503 1.00 35.20  ?  315 GLY A N     1 
ATOM   2378 C  CA    . GLY A 1 329 ? 18.295  -11.628 -18.421 1.00 41.88  ?  315 GLY A CA    1 
ATOM   2379 C  C     . GLY A 1 329 ? 16.986  -11.472 -17.668 1.00 41.91  ?  315 GLY A C     1 
ATOM   2380 O  O     . GLY A 1 329 ? 16.810  -10.550 -16.862 1.00 35.25  ?  315 GLY A O     1 
ATOM   2381 N  N     . ASP A 1 330 ? 16.046  -12.381 -17.926 1.00 39.37  ?  316 ASP A N     1 
ATOM   2382 C  CA    . ASP A 1 330 ? 14.737  -12.351 -17.287 1.00 44.26  ?  316 ASP A CA    1 
ATOM   2383 C  C     . ASP A 1 330 ? 14.652  -13.229 -16.045 1.00 45.48  ?  316 ASP A C     1 
ATOM   2384 O  O     . ASP A 1 330 ? 13.606  -13.238 -15.388 1.00 46.20  ?  316 ASP A O     1 
ATOM   2385 C  CB    . ASP A 1 330 ? 13.657  -12.788 -18.281 1.00 47.27  ?  316 ASP A CB    1 
ATOM   2386 C  CG    . ASP A 1 330 ? 13.497  -11.819 -19.434 1.00 59.25  ?  316 ASP A CG    1 
ATOM   2387 O  OD1   . ASP A 1 330 ? 13.378  -10.601 -19.182 1.00 53.84  ?  316 ASP A OD1   1 
ATOM   2388 O  OD2   . ASP A 1 330 ? 13.492  -12.280 -20.595 1.00 79.55  ?  316 ASP A OD2   1 
ATOM   2389 N  N     . VAL A 1 331 ? 15.721  -13.941 -15.691 1.00 41.53  ?  317 VAL A N     1 
ATOM   2390 C  CA    . VAL A 1 331 ? 15.708  -14.912 -14.601 1.00 38.22  ?  317 VAL A CA    1 
ATOM   2391 C  C     . VAL A 1 331 ? 16.446  -14.322 -13.407 1.00 43.17  ?  317 VAL A C     1 
ATOM   2392 O  O     . VAL A 1 331 ? 17.578  -13.836 -13.543 1.00 35.80  ?  317 VAL A O     1 
ATOM   2393 C  CB    . VAL A 1 331 ? 16.339  -16.252 -15.021 1.00 41.23  ?  317 VAL A CB    1 
ATOM   2394 C  CG1   . VAL A 1 331 ? 16.385  -17.207 -13.841 1.00 33.28  ?  317 VAL A CG1   1 
ATOM   2395 C  CG2   . VAL A 1 331 ? 15.572  -16.870 -16.184 1.00 36.54  ?  317 VAL A CG2   1 
ATOM   2396 N  N     . TRP A 1 332 ? 15.814  -14.390 -12.239 1.00 31.21  ?  318 TRP A N     1 
ATOM   2397 C  CA    . TRP A 1 332 ? 16.385  -13.922 -10.984 1.00 29.44  ?  318 TRP A CA    1 
ATOM   2398 C  C     . TRP A 1 332 ? 16.951  -15.089 -10.182 1.00 34.38  ?  318 TRP A C     1 
ATOM   2399 O  O     . TRP A 1 332 ? 16.385  -16.186 -10.173 1.00 33.32  ?  318 TRP A O     1 
ATOM   2400 C  CB    . TRP A 1 332 ? 15.328  -13.191 -10.156 1.00 37.60  ?  318 TRP A CB    1 
ATOM   2401 C  CG    . TRP A 1 332 ? 15.205  -11.732 -10.491 1.00 38.72  ?  318 TRP A CG    1 
ATOM   2402 C  CD1   . TRP A 1 332 ? 14.282  -11.150 -11.317 1.00 34.26  ?  318 TRP A CD1   1 
ATOM   2403 C  CD2   . TRP A 1 332 ? 16.035  -10.674 -10.008 1.00 36.98  ?  318 TRP A CD2   1 
ATOM   2404 N  NE1   . TRP A 1 332 ? 14.487  -9.794  -11.373 1.00 45.69  ?  318 TRP A NE1   1 
ATOM   2405 C  CE2   . TRP A 1 332 ? 15.559  -9.474  -10.581 1.00 43.39  ?  318 TRP A CE2   1 
ATOM   2406 C  CE3   . TRP A 1 332 ? 17.136  -10.620 -9.147  1.00 38.46  ?  318 TRP A CE3   1 
ATOM   2407 C  CZ2   . TRP A 1 332 ? 16.147  -8.235  -10.319 1.00 39.80  ?  318 TRP A CZ2   1 
ATOM   2408 C  CZ3   . TRP A 1 332 ? 17.721  -9.385  -8.889  1.00 34.82  ?  318 TRP A CZ3   1 
ATOM   2409 C  CH2   . TRP A 1 332 ? 17.224  -8.213  -9.473  1.00 35.10  ?  318 TRP A CH2   1 
ATOM   2410 N  N     . PHE A 1 333 ? 18.067  -14.843 -9.501  1.00 37.00  ?  319 PHE A N     1 
ATOM   2411 C  CA    . PHE A 1 333 ? 18.733  -15.838 -8.662  1.00 32.78  ?  319 PHE A CA    1 
ATOM   2412 C  C     . PHE A 1 333 ? 18.805  -15.260 -7.251  1.00 30.45  ?  319 PHE A C     1 
ATOM   2413 O  O     . PHE A 1 333 ? 19.654  -14.409 -6.968  1.00 32.00  ?  319 PHE A O     1 
ATOM   2414 C  CB    . PHE A 1 333 ? 20.119  -16.178 -9.213  1.00 27.97  ?  319 PHE A CB    1 
ATOM   2415 C  CG    . PHE A 1 333 ? 20.089  -16.739 -10.605 1.00 32.95  ?  319 PHE A CG    1 
ATOM   2416 C  CD1   . PHE A 1 333 ? 19.946  -18.105 -10.812 1.00 35.49  ?  319 PHE A CD1   1 
ATOM   2417 C  CD2   . PHE A 1 333 ? 20.183  -15.904 -11.709 1.00 30.13  ?  319 PHE A CD2   1 
ATOM   2418 C  CE1   . PHE A 1 333 ? 19.907  -18.630 -12.090 1.00 32.06  ?  319 PHE A CE1   1 
ATOM   2419 C  CE2   . PHE A 1 333 ? 20.144  -16.422 -12.992 1.00 29.04  ?  319 PHE A CE2   1 
ATOM   2420 C  CZ    . PHE A 1 333 ? 20.007  -17.787 -13.183 1.00 29.89  ?  319 PHE A CZ    1 
ATOM   2421 N  N     . THR A 1 334 ? 17.911  -15.707 -6.372  1.00 27.66  ?  320 THR A N     1 
ATOM   2422 C  CA    . THR A 1 334 ? 17.770  -15.110 -5.051  1.00 39.95  ?  320 THR A CA    1 
ATOM   2423 C  C     . THR A 1 334 ? 18.531  -15.912 -4.002  1.00 32.64  ?  320 THR A C     1 
ATOM   2424 O  O     . THR A 1 334 ? 18.785  -17.105 -4.160  1.00 36.74  ?  320 THR A O     1 
ATOM   2425 C  CB    . THR A 1 334 ? 16.289  -14.991 -4.658  1.00 37.01  ?  320 THR A CB    1 
ATOM   2426 O  OG1   . THR A 1 334 ? 15.779  -16.271 -4.264  1.00 39.17  ?  320 THR A OG1   1 
ATOM   2427 C  CG2   . THR A 1 334 ? 15.474  -14.476 -5.831  1.00 30.02  ?  320 THR A CG2   1 
ATOM   2428 N  N     . GLY A 1 335 ? 18.875  -15.235 -2.907  1.00 33.38  ?  321 GLY A N     1 
ATOM   2429 C  CA    . GLY A 1 335 ? 19.679  -15.847 -1.868  1.00 33.14  ?  321 GLY A CA    1 
ATOM   2430 C  C     . GLY A 1 335 ? 21.167  -15.888 -2.151  1.00 40.16  ?  321 GLY A C     1 
ATOM   2431 O  O     . GLY A 1 335 ? 21.869  -16.748 -1.612  1.00 36.82  ?  321 GLY A O     1 
ATOM   2432 N  N     . ILE A 1 336 ? 21.676  -14.980 -2.976  1.00 36.51  ?  322 ILE A N     1 
ATOM   2433 C  CA    . ILE A 1 336 ? 23.094  -14.924 -3.307  1.00 41.70  ?  322 ILE A CA    1 
ATOM   2434 C  C     . ILE A 1 336 ? 23.665  -13.618 -2.766  1.00 43.89  ?  322 ILE A C     1 
ATOM   2435 O  O     . ILE A 1 336 ? 23.239  -12.535 -3.184  1.00 30.60  ?  322 ILE A O     1 
ATOM   2436 C  CB    . ILE A 1 336 ? 23.350  -15.036 -4.818  1.00 30.25  ?  322 ILE A CB    1 
ATOM   2437 C  CG1   . ILE A 1 336 ? 23.103  -16.468 -5.288  1.00 36.11  ?  322 ILE A CG1   1 
ATOM   2438 C  CG2   . ILE A 1 336 ? 24.785  -14.603 -5.148  1.00 32.78  ?  322 ILE A CG2   1 
ATOM   2439 C  CD1   . ILE A 1 336 ? 22.863  -16.579 -6.767  1.00 45.45  ?  322 ILE A CD1   1 
ATOM   2440 N  N     . PRO A 1 337 ? 24.615  -13.663 -1.833  1.00 36.48  ?  323 PRO A N     1 
ATOM   2441 C  CA    . PRO A 1 337 ? 25.241  -12.424 -1.368  1.00 29.17  ?  323 PRO A CA    1 
ATOM   2442 C  C     . PRO A 1 337 ? 25.916  -11.697 -2.519  1.00 32.37  ?  323 PRO A C     1 
ATOM   2443 O  O     . PRO A 1 337 ? 26.547  -12.306 -3.386  1.00 31.38  ?  323 PRO A O     1 
ATOM   2444 C  CB    . PRO A 1 337 ? 26.261  -12.904 -0.327  1.00 35.05  ?  323 PRO A CB    1 
ATOM   2445 C  CG    . PRO A 1 337 ? 25.789  -14.258 0.074   1.00 34.60  ?  323 PRO A CG    1 
ATOM   2446 C  CD    . PRO A 1 337 ? 25.152  -14.848 -1.144  1.00 35.62  ?  323 PRO A CD    1 
ATOM   2447 N  N     . MET A 1 338 ? 25.795  -10.375 -2.499  1.00 30.97  ?  324 MET A N     1 
ATOM   2448 C  CA    . MET A 1 338 ? 26.311  -9.559  -3.587  1.00 35.49  ?  324 MET A CA    1 
ATOM   2449 C  C     . MET A 1 338 ? 27.821  -9.723  -3.746  1.00 35.23  ?  324 MET A C     1 
ATOM   2450 O  O     . MET A 1 338 ? 28.329  -9.728  -4.875  1.00 30.07  ?  324 MET A O     1 
ATOM   2451 C  CB    . MET A 1 338 ? 25.889  -8.108  -3.340  1.00 31.18  ?  324 MET A CB    1 
ATOM   2452 C  CG    . MET A 1 338 ? 26.868  -7.032  -3.685  1.00 30.85  ?  324 MET A CG    1 
ATOM   2453 S  SD    . MET A 1 338 ? 26.147  -5.422  -3.237  1.00 39.87  ?  324 MET A SD    1 
ATOM   2454 C  CE    . MET A 1 338 ? 25.398  -4.969  -4.793  1.00 32.92  ?  324 MET A CE    1 
ATOM   2455 N  N     . LEU A 1 339 ? 28.548  -9.909  -2.640  1.00 30.30  ?  325 LEU A N     1 
ATOM   2456 C  CA    . LEU A 1 339 ? 29.986  -10.148 -2.740  1.00 35.13  ?  325 LEU A CA    1 
ATOM   2457 C  C     . LEU A 1 339 ? 30.278  -11.421 -3.528  1.00 43.08  ?  325 LEU A C     1 
ATOM   2458 O  O     . LEU A 1 339 ? 31.193  -11.449 -4.361  1.00 39.35  ?  325 LEU A O     1 
ATOM   2459 C  CB    . LEU A 1 339 ? 30.608  -10.231 -1.343  1.00 36.12  ?  325 LEU A CB    1 
ATOM   2460 C  CG    . LEU A 1 339 ? 32.018  -10.836 -1.262  1.00 48.89  ?  325 LEU A CG    1 
ATOM   2461 C  CD1   . LEU A 1 339 ? 33.023  -9.923  -1.944  1.00 40.23  ?  325 LEU A CD1   1 
ATOM   2462 C  CD2   . LEU A 1 339 ? 32.443  -11.112 0.174   1.00 36.38  ?  325 LEU A CD2   1 
ATOM   2463 N  N     . GLN A 1 340 ? 29.521  -12.491 -3.269  1.00 34.75  ?  326 GLN A N     1 
ATOM   2464 C  CA    . GLN A 1 340 ? 29.736  -13.741 -3.996  1.00 31.39  ?  326 GLN A CA    1 
ATOM   2465 C  C     . GLN A 1 340 ? 29.383  -13.600 -5.473  1.00 37.20  ?  326 GLN A C     1 
ATOM   2466 O  O     . GLN A 1 340 ? 30.084  -14.142 -6.336  1.00 29.70  ?  326 GLN A O     1 
ATOM   2467 C  CB    . GLN A 1 340 ? 28.931  -14.867 -3.356  1.00 32.09  ?  326 GLN A CB    1 
ATOM   2468 C  CG    . GLN A 1 340 ? 29.615  -15.512 -2.166  1.00 34.29  ?  326 GLN A CG    1 
ATOM   2469 C  CD    . GLN A 1 340 ? 28.930  -16.792 -1.732  1.00 40.75  ?  326 GLN A CD    1 
ATOM   2470 O  OE1   . GLN A 1 340 ? 27.754  -16.783 -1.365  1.00 35.41  ?  326 GLN A OE1   1 
ATOM   2471 N  NE2   . GLN A 1 340 ? 29.665  -17.902 -1.764  1.00 39.15  ?  326 GLN A NE2   1 
ATOM   2472 N  N     . ALA A 1 341 ? 28.297  -12.881 -5.782  1.00 32.44  ?  327 ALA A N     1 
ATOM   2473 C  CA    . ALA A 1 341 ? 27.940  -12.636 -7.178  1.00 29.24  ?  327 ALA A CA    1 
ATOM   2474 C  C     . ALA A 1 341 ? 29.036  -11.857 -7.897  1.00 38.51  ?  327 ALA A C     1 
ATOM   2475 O  O     . ALA A 1 341 ? 29.372  -12.157 -9.050  1.00 36.73  ?  327 ALA A O     1 
ATOM   2476 C  CB    . ALA A 1 341 ? 26.614  -11.886 -7.259  1.00 26.89  ?  327 ALA A CB    1 
ATOM   2477 N  N     . ILE A 1 342 ? 29.581  -10.829 -7.244  1.00 33.53  ?  328 ILE A N     1 
ATOM   2478 C  CA    . ILE A 1 342 ? 30.645  -10.041 -7.859  1.00 31.69  ?  328 ILE A CA    1 
ATOM   2479 C  C     . ILE A 1 342 ? 31.883  -10.906 -8.077  1.00 35.97  ?  328 ILE A C     1 
ATOM   2480 O  O     . ILE A 1 342 ? 32.486  -10.900 -9.158  1.00 39.47  ?  328 ILE A O     1 
ATOM   2481 C  CB    . ILE A 1 342 ? 30.954  -8.799  -7.003  1.00 30.46  ?  328 ILE A CB    1 
ATOM   2482 C  CG1   . ILE A 1 342 ? 29.824  -7.771  -7.129  1.00 31.14  ?  328 ILE A CG1   1 
ATOM   2483 C  CG2   . ILE A 1 342 ? 32.278  -8.174  -7.415  1.00 29.52  ?  328 ILE A CG2   1 
ATOM   2484 C  CD1   . ILE A 1 342 ? 29.864  -6.683  -6.074  1.00 33.81  ?  328 ILE A CD1   1 
ATOM   2485 N  N     . GLU A 1 343 ? 32.264  -11.690 -7.065  1.00 32.28  ?  329 GLU A N     1 
ATOM   2486 C  CA    . GLU A 1 343 ? 33.430  -12.560 -7.215  1.00 37.84  ?  329 GLU A CA    1 
ATOM   2487 C  C     . GLU A 1 343 ? 33.237  -13.549 -8.356  1.00 34.35  ?  329 GLU A C     1 
ATOM   2488 O  O     . GLU A 1 343 ? 34.180  -13.845 -9.101  1.00 33.39  ?  329 GLU A O     1 
ATOM   2489 C  CB    . GLU A 1 343 ? 33.706  -13.303 -5.912  1.00 41.43  ?  329 GLU A CB    1 
ATOM   2490 C  CG    . GLU A 1 343 ? 34.287  -12.433 -4.821  1.00 46.96  ?  329 GLU A CG    1 
ATOM   2491 C  CD    . GLU A 1 343 ? 34.456  -13.193 -3.523  1.00 62.01  ?  329 GLU A CD    1 
ATOM   2492 O  OE1   . GLU A 1 343 ? 33.751  -14.210 -3.334  1.00 56.32  ?  329 GLU A OE1   1 
ATOM   2493 O  OE2   . GLU A 1 343 ? 35.290  -12.773 -2.693  1.00 71.96  ?  329 GLU A OE2   1 
ATOM   2494 N  N     . THR A 1 344 ? 32.018  -14.065 -8.510  1.00 32.23  ?  330 THR A N     1 
ATOM   2495 C  CA    . THR A 1 344 ? 31.713  -14.940 -9.635  1.00 36.29  ?  330 THR A CA    1 
ATOM   2496 C  C     . THR A 1 344 ? 31.882  -14.203 -10.959 1.00 30.83  ?  330 THR A C     1 
ATOM   2497 O  O     . THR A 1 344 ? 32.517  -14.711 -11.890 1.00 37.88  ?  330 THR A O     1 
ATOM   2498 C  CB    . THR A 1 344 ? 30.284  -15.471 -9.491  1.00 39.45  ?  330 THR A CB    1 
ATOM   2499 O  OG1   . THR A 1 344 ? 30.197  -16.286 -8.318  1.00 39.34  ?  330 THR A OG1   1 
ATOM   2500 C  CG2   . THR A 1 344 ? 29.872  -16.283 -10.711 1.00 33.82  ?  330 THR A CG2   1 
ATOM   2501 N  N     . LEU A 1 345 ? 31.322  -12.994 -11.055 1.00 32.05  ?  331 LEU A N     1 
ATOM   2502 C  CA    . LEU A 1 345 ? 31.408  -12.236 -12.301 1.00 36.45  ?  331 LEU A CA    1 
ATOM   2503 C  C     . LEU A 1 345 ? 32.845  -11.861 -12.629 1.00 34.04  ?  331 LEU A C     1 
ATOM   2504 O  O     . LEU A 1 345 ? 33.244  -11.884 -13.798 1.00 37.85  ?  331 LEU A O     1 
ATOM   2505 C  CB    . LEU A 1 345 ? 30.540  -10.980 -12.221 1.00 29.41  ?  331 LEU A CB    1 
ATOM   2506 C  CG    . LEU A 1 345 ? 29.036  -11.231 -12.239 1.00 41.98  ?  331 LEU A CG    1 
ATOM   2507 C  CD1   . LEU A 1 345 ? 28.265  -9.918  -12.096 1.00 36.74  ?  331 LEU A CD1   1 
ATOM   2508 C  CD2   . LEU A 1 345 ? 28.651  -11.970 -13.513 1.00 37.81  ?  331 LEU A CD2   1 
ATOM   2509 N  N     . VAL A 1 346 ? 33.652  -11.562 -11.610 1.00 34.77  ?  332 VAL A N     1 
ATOM   2510 C  CA    . VAL A 1 346 ? 35.038  -11.170 -11.854 1.00 39.05  ?  332 VAL A CA    1 
ATOM   2511 C  C     . VAL A 1 346 ? 35.799  -12.318 -12.492 1.00 37.06  ?  332 VAL A C     1 
ATOM   2512 O  O     . VAL A 1 346 ? 36.506  -12.139 -13.491 1.00 34.98  ?  332 VAL A O     1 
ATOM   2513 C  CB    . VAL A 1 346 ? 35.713  -10.719 -10.547 1.00 34.41  ?  332 VAL A CB    1 
ATOM   2514 C  CG1   . VAL A 1 346 ? 37.215  -10.577 -10.758 1.00 33.36  ?  332 VAL A CG1   1 
ATOM   2515 C  CG2   . VAL A 1 346 ? 35.110  -9.407  -10.061 1.00 38.50  ?  332 VAL A CG2   1 
ATOM   2516 N  N     . GLU A 1 347 ? 35.654  -13.521 -11.927 1.00 37.29  ?  333 GLU A N     1 
ATOM   2517 C  CA    . GLU A 1 347 ? 36.255  -14.708 -12.527 1.00 35.27  ?  333 GLU A CA    1 
ATOM   2518 C  C     . GLU A 1 347 ? 35.777  -14.907 -13.958 1.00 35.28  ?  333 GLU A C     1 
ATOM   2519 O  O     . GLU A 1 347 ? 36.577  -15.161 -14.865 1.00 42.66  ?  333 GLU A O     1 
ATOM   2520 C  CB    . GLU A 1 347 ? 35.939  -15.933 -11.671 1.00 34.75  ?  333 GLU A CB    1 
ATOM   2521 C  CG    . GLU A 1 347 ? 36.565  -17.217 -12.175 1.00 40.81  ?  333 GLU A CG    1 
ATOM   2522 C  CD    . GLU A 1 347 ? 36.779  -18.235 -11.066 1.00 69.83  ?  333 GLU A CD    1 
ATOM   2523 O  OE1   . GLU A 1 347 ? 35.784  -18.869 -10.655 1.00 60.71  ?  333 GLU A OE1   1 
ATOM   2524 O  OE2   . GLU A 1 347 ? 37.934  -18.423 -10.625 1.00 74.43  ?  333 GLU A OE2   1 
ATOM   2525 N  N     . LEU A 1 348 ? 34.464  -14.813 -14.173 1.00 34.33  ?  334 LEU A N     1 
ATOM   2526 C  CA    . LEU A 1 348 ? 33.924  -15.051 -15.507 1.00 34.05  ?  334 LEU A CA    1 
ATOM   2527 C  C     . LEU A 1 348 ? 34.412  -13.994 -16.491 1.00 43.70  ?  334 LEU A C     1 
ATOM   2528 O  O     . LEU A 1 348 ? 34.745  -14.308 -17.642 1.00 35.36  ?  334 LEU A O     1 
ATOM   2529 C  CB    . LEU A 1 348 ? 32.397  -15.066 -15.465 1.00 33.71  ?  334 LEU A CB    1 
ATOM   2530 C  CG    . LEU A 1 348 ? 31.746  -16.253 -14.757 1.00 46.40  ?  334 LEU A CG    1 
ATOM   2531 C  CD1   . LEU A 1 348 ? 30.232  -16.097 -14.771 1.00 32.02  ?  334 LEU A CD1   1 
ATOM   2532 C  CD2   . LEU A 1 348 ? 32.162  -17.564 -15.406 1.00 41.24  ?  334 LEU A CD2   1 
ATOM   2533 N  N     . CYS A 1 349 ? 34.495  -12.738 -16.038 1.00 34.92  ?  335 CYS A N     1 
ATOM   2534 C  CA    . CYS A 1 349 ? 34.979  -11.666 -16.902 1.00 34.00  ?  335 CYS A CA    1 
ATOM   2535 C  C     . CYS A 1 349 ? 36.444  -11.870 -17.275 1.00 38.78  ?  335 CYS A C     1 
ATOM   2536 O  O     . CYS A 1 349 ? 36.823  -11.666 -18.433 1.00 40.78  ?  335 CYS A O     1 
ATOM   2537 C  CB    . CYS A 1 349 ? 34.779  -10.308 -16.226 1.00 33.01  ?  335 CYS A CB    1 
ATOM   2538 S  SG    . CYS A 1 349 ? 33.107  -9.624  -16.409 1.00 41.36  ?  335 CYS A SG    1 
ATOM   2539 N  N     . LYS A 1 350 ? 37.281  -12.305 -16.322 1.00 40.13  ?  336 LYS A N     1 
ATOM   2540 C  CA    . LYS A 1 350 ? 38.680  -12.577 -16.651 1.00 45.70  ?  336 LYS A CA    1 
ATOM   2541 C  C     . LYS A 1 350 ? 38.802  -13.626 -17.744 1.00 43.01  ?  336 LYS A C     1 
ATOM   2542 O  O     . LYS A 1 350 ? 39.778  -13.623 -18.501 1.00 39.99  ?  336 LYS A O     1 
ATOM   2543 C  CB    . LYS A 1 350 ? 39.452  -13.039 -15.414 1.00 40.96  ?  336 LYS A CB    1 
ATOM   2544 C  CG    . LYS A 1 350 ? 39.606  -11.986 -14.341 1.00 45.65  ?  336 LYS A CG    1 
ATOM   2545 C  CD    . LYS A 1 350 ? 40.461  -12.484 -13.192 1.00 53.13  ?  336 LYS A CD    1 
ATOM   2546 C  CE    . LYS A 1 350 ? 40.807  -11.345 -12.243 1.00 40.86  ?  336 LYS A CE    1 
ATOM   2547 N  NZ    . LYS A 1 350 ? 40.646  -11.752 -10.819 1.00 62.67  ?  336 LYS A NZ    1 
ATOM   2548 N  N     . GLN A 1 351 ? 37.813  -14.508 -17.861 1.00 42.43  ?  337 GLN A N     1 
ATOM   2549 C  CA    . GLN A 1 351 ? 37.835  -15.551 -18.875 1.00 44.67  ?  337 GLN A CA    1 
ATOM   2550 C  C     . GLN A 1 351 ? 37.209  -15.111 -20.192 1.00 44.08  ?  337 GLN A C     1 
ATOM   2551 O  O     . GLN A 1 351 ? 37.725  -15.452 -21.262 1.00 41.99  ?  337 GLN A O     1 
ATOM   2552 C  CB    . GLN A 1 351 ? 37.105  -16.801 -18.364 1.00 38.94  ?  337 GLN A CB    1 
ATOM   2553 C  CG    . GLN A 1 351 ? 37.362  -18.037 -19.218 1.00 51.00  ?  337 GLN A CG    1 
ATOM   2554 C  CD    . GLN A 1 351 ? 36.502  -19.234 -18.851 1.00 42.81  ?  337 GLN A CD    1 
ATOM   2555 O  OE1   . GLN A 1 351 ? 35.982  -19.329 -17.739 1.00 47.10  ?  337 GLN A OE1   1 
ATOM   2556 N  NE2   . GLN A 1 351 ? 36.352  -20.159 -19.792 1.00 41.23  ?  337 GLN A NE2   1 
ATOM   2557 N  N     . HIS A 1 352 ? 36.128  -14.326 -20.147 1.00 44.09  ?  338 HIS A N     1 
ATOM   2558 C  CA    . HIS A 1 352 ? 35.279  -14.166 -21.318 1.00 54.31  ?  338 HIS A CA    1 
ATOM   2559 C  C     . HIS A 1 352 ? 35.180  -12.767 -21.903 1.00 49.26  ?  338 HIS A C     1 
ATOM   2560 O  O     . HIS A 1 352 ? 34.706  -12.640 -23.037 1.00 55.78  ?  338 HIS A O     1 
ATOM   2561 C  CB    . HIS A 1 352 ? 33.851  -14.638 -21.011 1.00 44.82  ?  338 HIS A CB    1 
ATOM   2562 C  CG    . HIS A 1 352 ? 33.741  -16.112 -20.776 1.00 43.16  ?  338 HIS A CG    1 
ATOM   2563 N  ND1   . HIS A 1 352 ? 33.786  -17.030 -21.803 1.00 41.97  ?  338 HIS A ND1   1 
ATOM   2564 C  CD2   . HIS A 1 352 ? 33.552  -16.825 -19.641 1.00 42.78  ?  338 HIS A CD2   1 
ATOM   2565 C  CE1   . HIS A 1 352 ? 33.651  -18.248 -21.308 1.00 41.34  ?  338 HIS A CE1   1 
ATOM   2566 N  NE2   . HIS A 1 352 ? 33.508  -18.152 -19.999 1.00 48.07  ?  338 HIS A NE2   1 
ATOM   2567 N  N     . VAL A 1 353 ? 35.611  -11.719 -21.218 1.00 72.02  ?  339 VAL A N     1 
ATOM   2568 C  CA    . VAL A 1 353 ? 35.560  -10.406 -21.844 1.00 70.95  ?  339 VAL A CA    1 
ATOM   2569 C  C     . VAL A 1 353 ? 36.898  -10.162 -22.524 1.00 73.13  ?  339 VAL A C     1 
ATOM   2570 O  O     . VAL A 1 353 ? 37.964  -10.161 -21.892 1.00 80.37  ?  339 VAL A O     1 
ATOM   2571 C  CB    . VAL A 1 353 ? 35.196  -9.292  -20.853 1.00 66.46  ?  339 VAL A CB    1 
ATOM   2572 C  CG1   . VAL A 1 353 ? 33.872  -9.591  -20.166 1.00 64.82  ?  339 VAL A CG1   1 
ATOM   2573 C  CG2   . VAL A 1 353 ? 36.235  -9.126  -19.838 1.00 67.59  ?  339 VAL A CG2   1 
ATOM   2574 N  N     . HIS A 1 354 ? 36.819  -10.033 -23.842 1.00 86.52  ?  340 HIS A N     1 
ATOM   2575 C  CA    . HIS A 1 354 ? 37.936  -9.923  -24.768 1.00 102.53 ?  340 HIS A CA    1 
ATOM   2576 C  C     . HIS A 1 354 ? 38.090  -8.457  -25.178 1.00 102.95 ?  340 HIS A C     1 
ATOM   2577 O  O     . HIS A 1 354 ? 38.039  -8.090  -26.357 1.00 106.56 ?  340 HIS A O     1 
ATOM   2578 C  CB    . HIS A 1 354 ? 37.693  -11.003 -25.850 1.00 103.87 ?  340 HIS A CB    1 
ATOM   2579 C  CG    . HIS A 1 354 ? 37.030  -10.546 -27.115 1.00 117.99 ?  340 HIS A CG    1 
ATOM   2580 N  ND1   . HIS A 1 354 ? 37.296  -9.354  -27.749 1.00 119.95 ?  340 HIS A ND1   1 
ATOM   2581 C  CD2   . HIS A 1 354 ? 36.012  -11.114 -27.806 1.00 119.03 ?  340 HIS A CD2   1 
ATOM   2582 C  CE1   . HIS A 1 354 ? 36.516  -9.233  -28.809 1.00 115.39 ?  340 HIS A CE1   1 
ATOM   2583 N  NE2   . HIS A 1 354 ? 35.721  -10.285 -28.861 1.00 116.74 ?  340 HIS A NE2   1 
ATOM   2584 N  N     . ASP A 1 355 ? 38.285  -7.594  -24.177 1.00 87.20  ?  341 ASP A N     1 
ATOM   2585 C  CA    . ASP A 1 355 ? 38.129  -6.155  -24.338 1.00 94.06  ?  341 ASP A CA    1 
ATOM   2586 C  C     . ASP A 1 355 ? 39.380  -5.411  -23.887 1.00 101.14 ?  341 ASP A C     1 
ATOM   2587 O  O     . ASP A 1 355 ? 40.082  -5.836  -22.962 1.00 98.61  ?  341 ASP A O     1 
ATOM   2588 C  CB    . ASP A 1 355 ? 36.917  -5.662  -23.526 1.00 97.19  ?  341 ASP A CB    1 
ATOM   2589 C  CG    . ASP A 1 355 ? 35.855  -5.008  -24.388 1.00 93.28  ?  341 ASP A CG    1 
ATOM   2590 O  OD1   . ASP A 1 355 ? 35.934  -3.777  -24.590 1.00 81.36  ?  341 ASP A OD1   1 
ATOM   2591 O  OD2   . ASP A 1 355 ? 34.941  -5.717  -24.863 1.00 83.43  ?  341 ASP A OD2   1 
ATOM   2592 N  N     . THR A 1 356 ? 39.538  -4.236  -24.486 1.00 105.61 ?  342 THR A N     1 
ATOM   2593 C  CA    . THR A 1 356 ? 40.553  -3.254  -24.139 1.00 95.97  ?  342 THR A CA    1 
ATOM   2594 C  C     . THR A 1 356 ? 40.006  -1.898  -24.568 1.00 97.32  ?  342 THR A C     1 
ATOM   2595 O  O     . THR A 1 356 ? 39.709  -1.673  -25.729 1.00 98.92  ?  342 THR A O     1 
ATOM   2596 C  CB    . THR A 1 356 ? 41.931  -3.528  -24.704 1.00 101.76 ?  342 THR A CB    1 
ATOM   2597 O  OG1   . THR A 1 356 ? 42.898  -2.987  -23.797 1.00 95.03  ?  342 THR A OG1   1 
ATOM   2598 C  CG2   . THR A 1 356 ? 42.094  -2.882  -26.058 1.00 96.15  ?  342 THR A CG2   1 
ATOM   2599 N  N     . PRO A 1 357 ? 39.826  -1.003  -23.602 1.00 94.82  ?  343 PRO A N     1 
ATOM   2600 C  CA    . PRO A 1 357 ? 39.261  0.318   -23.827 1.00 95.43  ?  343 PRO A CA    1 
ATOM   2601 C  C     . PRO A 1 357 ? 40.110  1.234   -24.695 1.00 104.63 ?  343 PRO A C     1 
ATOM   2602 O  O     . PRO A 1 357 ? 39.538  1.720   -25.653 1.00 107.28 ?  343 PRO A O     1 
ATOM   2603 C  CB    . PRO A 1 357 ? 39.139  0.881   -22.420 1.00 79.16  ?  343 PRO A CB    1 
ATOM   2604 C  CG    . PRO A 1 357 ? 39.149  -0.284  -21.540 1.00 62.74  ?  343 PRO A CG    1 
ATOM   2605 C  CD    . PRO A 1 357 ? 40.116  -1.211  -22.184 1.00 86.28  ?  343 PRO A CD    1 
ATOM   2606 N  N     . VAL A 1 358 ? 41.382  1.448   -24.373 1.00 107.27 ?  344 VAL A N     1 
ATOM   2607 C  CA    . VAL A 1 358 ? 42.236  2.319   -25.172 1.00 109.86 ?  344 VAL A CA    1 
ATOM   2608 C  C     . VAL A 1 358 ? 41.534  3.636   -25.486 1.00 118.09 ?  344 VAL A C     1 
ATOM   2609 O  O     . VAL A 1 358 ? 40.742  3.714   -26.424 1.00 121.12 ?  344 VAL A O     1 
ATOM   2610 C  CB    . VAL A 1 358 ? 42.655  1.643   -26.490 1.00 102.65 ?  344 VAL A CB    1 
ATOM   2611 C  CG1   . VAL A 1 358 ? 41.434  1.113   -27.226 1.00 106.83 ?  344 VAL A CG1   1 
ATOM   2612 C  CG2   . VAL A 1 358 ? 43.430  2.619   -27.363 1.00 101.99 ?  344 VAL A CG2   1 
ATOM   2613 N  N     . PRO A 1 359 ? 41.827  4.678   -24.694 1.00 115.81 ?  345 PRO A N     1 
ATOM   2614 C  CA    . PRO A 1 359 ? 41.230  6.005   -24.875 1.00 108.45 ?  345 PRO A CA    1 
ATOM   2615 C  C     . PRO A 1 359 ? 41.351  6.489   -26.316 1.00 100.30 ?  345 PRO A C     1 
ATOM   2616 O  O     . PRO A 1 359 ? 40.377  7.015   -26.854 1.00 84.49  ?  345 PRO A O     1 
ATOM   2617 C  CB    . PRO A 1 359 ? 42.067  6.890   -23.951 1.00 99.96  ?  345 PRO A CB    1 
ATOM   2618 C  CG    . PRO A 1 359 ? 42.547  5.965   -22.886 1.00 106.49 ?  345 PRO A CG    1 
ATOM   2619 C  CD    . PRO A 1 359 ? 42.770  4.643   -23.563 1.00 113.70 ?  345 PRO A CD    1 
ATOM   2620 N  N     . PRO A 1 370 ? 39.605  29.464  -17.635 1.00 95.33  ?  356 PRO A N     1 
ATOM   2621 C  CA    . PRO A 1 370 ? 39.168  30.653  -16.894 1.00 89.96  ?  356 PRO A CA    1 
ATOM   2622 C  C     . PRO A 1 370 ? 38.300  31.586  -17.742 1.00 91.55  ?  356 PRO A C     1 
ATOM   2623 O  O     . PRO A 1 370 ? 38.321  31.503  -18.971 1.00 94.15  ?  356 PRO A O     1 
ATOM   2624 C  CB    . PRO A 1 370 ? 40.487  31.338  -16.502 1.00 86.33  ?  356 PRO A CB    1 
ATOM   2625 C  CG    . PRO A 1 370 ? 41.589  30.549  -17.181 1.00 82.68  ?  356 PRO A CG    1 
ATOM   2626 C  CD    . PRO A 1 370 ? 41.039  29.194  -17.447 1.00 79.06  ?  356 PRO A CD    1 
ATOM   2627 N  N     . ASP A 1 371 ? 37.560  32.471  -17.083 1.00 89.43  ?  357 ASP A N     1 
ATOM   2628 C  CA    . ASP A 1 371 ? 36.517  33.274  -17.719 1.00 85.81  ?  357 ASP A CA    1 
ATOM   2629 C  C     . ASP A 1 371 ? 36.481  34.633  -17.027 1.00 83.79  ?  357 ASP A C     1 
ATOM   2630 O  O     . ASP A 1 371 ? 37.441  35.030  -16.359 1.00 87.46  ?  357 ASP A O     1 
ATOM   2631 C  CB    . ASP A 1 371 ? 35.148  32.565  -17.645 1.00 90.63  ?  357 ASP A CB    1 
ATOM   2632 C  CG    . ASP A 1 371 ? 35.026  31.385  -18.602 1.00 91.89  ?  357 ASP A CG    1 
ATOM   2633 O  OD1   . ASP A 1 371 ? 35.729  30.369  -18.410 1.00 97.17  ?  357 ASP A OD1   1 
ATOM   2634 O  OD2   . ASP A 1 371 ? 34.205  31.471  -19.541 1.00 88.45  ?  357 ASP A OD2   1 
ATOM   2635 N  N     . GLY A 1 372 ? 35.380  35.361  -17.210 1.00 73.02  ?  358 GLY A N     1 
ATOM   2636 C  CA    . GLY A 1 372 ? 35.127  36.582  -16.469 1.00 62.57  ?  358 GLY A CA    1 
ATOM   2637 C  C     . GLY A 1 372 ? 34.028  36.387  -15.439 1.00 71.83  ?  358 GLY A C     1 
ATOM   2638 O  O     . GLY A 1 372 ? 34.262  35.789  -14.384 1.00 59.84  ?  358 GLY A O     1 
ATOM   2639 N  N     . SER A 1 373 ? 32.819  36.859  -15.745 1.00 55.06  ?  359 SER A N     1 
ATOM   2640 C  CA    . SER A 1 373 ? 31.699  36.728  -14.820 1.00 43.96  ?  359 SER A CA    1 
ATOM   2641 C  C     . SER A 1 373 ? 31.369  35.260  -14.562 1.00 51.89  ?  359 SER A C     1 
ATOM   2642 O  O     . SER A 1 373 ? 31.354  34.435  -15.479 1.00 44.11  ?  359 SER A O     1 
ATOM   2643 C  CB    . SER A 1 373 ? 30.471  37.451  -15.374 1.00 54.87  ?  359 SER A CB    1 
ATOM   2644 O  OG    . SER A 1 373 ? 29.659  37.953  -14.328 1.00 73.29  ?  359 SER A OG    1 
ATOM   2645 N  N     . LEU A 1 374 ? 31.095  34.940  -13.299 1.00 38.91  ?  360 LEU A N     1 
ATOM   2646 C  CA    . LEU A 1 374 ? 30.872  33.558  -12.902 1.00 43.05  ?  360 LEU A CA    1 
ATOM   2647 C  C     . LEU A 1 374 ? 29.594  33.005  -13.524 1.00 46.20  ?  360 LEU A C     1 
ATOM   2648 O  O     . LEU A 1 374 ? 28.545  33.659  -13.524 1.00 44.66  ?  360 LEU A O     1 
ATOM   2649 C  CB    . LEU A 1 374 ? 30.797  33.452  -11.380 1.00 34.56  ?  360 LEU A CB    1 
ATOM   2650 C  CG    . LEU A 1 374 ? 32.108  33.142  -10.662 1.00 44.02  ?  360 LEU A CG    1 
ATOM   2651 C  CD1   . LEU A 1 374 ? 31.984  33.440  -9.177  1.00 35.54  ?  360 LEU A CD1   1 
ATOM   2652 C  CD2   . LEU A 1 374 ? 32.513  31.697  -10.894 1.00 43.62  ?  360 LEU A CD2   1 
ATOM   2653 N  N     . THR A 1 375 ? 29.693  31.797  -14.064 1.00 39.47  ?  361 THR A N     1 
ATOM   2654 C  CA    . THR A 1 375 ? 28.554  31.032  -14.540 1.00 40.35  ?  361 THR A CA    1 
ATOM   2655 C  C     . THR A 1 375 ? 28.653  29.633  -13.959 1.00 37.38  ?  361 THR A C     1 
ATOM   2656 O  O     . THR A 1 375 ? 29.678  29.253  -13.385 1.00 44.22  ?  361 THR A O     1 
ATOM   2657 C  CB    . THR A 1 375 ? 28.511  30.960  -16.072 1.00 41.39  ?  361 THR A CB    1 
ATOM   2658 O  OG1   . THR A 1 375 ? 29.713  30.338  -16.549 1.00 47.89  ?  361 THR A OG1   1 
ATOM   2659 C  CG2   . THR A 1 375 ? 28.379  32.347  -16.676 1.00 35.57  ?  361 THR A CG2   1 
ATOM   2660 N  N     . GLN A 1 376 ? 27.574  28.857  -14.104 1.00 35.76  ?  362 GLN A N     1 
ATOM   2661 C  CA    . GLN A 1 376 ? 27.659  27.441  -13.759 1.00 38.95  ?  362 GLN A CA    1 
ATOM   2662 C  C     . GLN A 1 376 ? 28.792  26.772  -14.527 1.00 35.05  ?  362 GLN A C     1 
ATOM   2663 O  O     . GLN A 1 376 ? 29.562  25.991  -13.960 1.00 32.32  ?  362 GLN A O     1 
ATOM   2664 C  CB    . GLN A 1 376 ? 26.329  26.739  -14.044 1.00 35.03  ?  362 GLN A CB    1 
ATOM   2665 C  CG    . GLN A 1 376 ? 25.189  27.135  -13.114 1.00 35.52  ?  362 GLN A CG    1 
ATOM   2666 C  CD    . GLN A 1 376 ? 25.264  26.454  -11.761 1.00 41.29  ?  362 GLN A CD    1 
ATOM   2667 O  OE1   . GLN A 1 376 ? 25.853  25.379  -11.620 1.00 31.69  ?  362 GLN A OE1   1 
ATOM   2668 N  NE2   . GLN A 1 376 ? 24.653  27.074  -10.754 1.00 33.26  ?  362 GLN A NE2   1 
ATOM   2669 N  N     . ASP A 1 377 ? 28.930  27.104  -15.811 1.00 34.57  ?  363 ASP A N     1 
ATOM   2670 C  CA    . ASP A 1 377 ? 29.930  26.462  -16.657 1.00 46.26  ?  363 ASP A CA    1 
ATOM   2671 C  C     . ASP A 1 377 ? 31.352  26.719  -16.152 1.00 45.67  ?  363 ASP A C     1 
ATOM   2672 O  O     . ASP A 1 377 ? 32.122  25.775  -15.946 1.00 47.35  ?  363 ASP A O     1 
ATOM   2673 C  CB    . ASP A 1 377 ? 29.764  26.945  -18.099 1.00 47.16  ?  363 ASP A CB    1 
ATOM   2674 C  CG    . ASP A 1 377 ? 30.424  26.020  -19.105 1.00 62.27  ?  363 ASP A CG    1 
ATOM   2675 O  OD1   . ASP A 1 377 ? 31.638  26.177  -19.344 1.00 66.67  ?  363 ASP A OD1   1 
ATOM   2676 O  OD2   . ASP A 1 377 ? 29.730  25.139  -19.655 1.00 77.91  ?  363 ASP A OD2   1 
ATOM   2677 N  N     . ASN A 1 378 ? 31.726  27.985  -15.935 1.00 36.29  ?  364 ASN A N     1 
ATOM   2678 C  CA    . ASN A 1 378 ? 33.105  28.209  -15.514 1.00 36.72  ?  364 ASN A CA    1 
ATOM   2679 C  C     . ASN A 1 378 ? 33.321  27.935  -14.030 1.00 35.41  ?  364 ASN A C     1 
ATOM   2680 O  O     . ASN A 1 378 ? 34.460  27.681  -13.628 1.00 36.23  ?  364 ASN A O     1 
ATOM   2681 C  CB    . ASN A 1 378 ? 33.596  29.627  -15.878 1.00 46.44  ?  364 ASN A CB    1 
ATOM   2682 C  CG    . ASN A 1 378 ? 32.714  30.744  -15.336 1.00 39.94  ?  364 ASN A CG    1 
ATOM   2683 O  OD1   . ASN A 1 378 ? 32.347  30.764  -14.162 1.00 38.08  ?  364 ASN A OD1   1 
ATOM   2684 N  ND2   . ASN A 1 378 ? 32.403  31.706  -16.196 1.00 41.34  ?  364 ASN A ND2   1 
ATOM   2685 N  N     . PHE A 1 379 ? 32.264  27.930  -13.213 1.00 30.82  ?  365 PHE A N     1 
ATOM   2686 C  CA    . PHE A 1 379 ? 32.433  27.536  -11.816 1.00 33.31  ?  365 PHE A CA    1 
ATOM   2687 C  C     . PHE A 1 379 ? 32.866  26.077  -11.706 1.00 35.76  ?  365 PHE A C     1 
ATOM   2688 O  O     . PHE A 1 379 ? 33.813  25.751  -10.982 1.00 33.20  ?  365 PHE A O     1 
ATOM   2689 C  CB    . PHE A 1 379 ? 31.140  27.767  -11.023 1.00 34.04  ?  365 PHE A CB    1 
ATOM   2690 C  CG    . PHE A 1 379 ? 31.157  27.130  -9.658  1.00 34.46  ?  365 PHE A CG    1 
ATOM   2691 C  CD1   . PHE A 1 379 ? 31.794  27.755  -8.594  1.00 36.49  ?  365 PHE A CD1   1 
ATOM   2692 C  CD2   . PHE A 1 379 ? 30.571  25.891  -9.446  1.00 34.25  ?  365 PHE A CD2   1 
ATOM   2693 C  CE1   . PHE A 1 379 ? 31.836  27.164  -7.341  1.00 36.64  ?  365 PHE A CE1   1 
ATOM   2694 C  CE2   . PHE A 1 379 ? 30.611  25.293  -8.195  1.00 31.10  ?  365 PHE A CE2   1 
ATOM   2695 C  CZ    . PHE A 1 379 ? 31.244  25.928  -7.143  1.00 34.81  ?  365 PHE A CZ    1 
ATOM   2696 N  N     . TRP A 1 380 ? 32.167  25.177  -12.406 1.00 36.21  ?  366 TRP A N     1 
ATOM   2697 C  CA    . TRP A 1 380 ? 32.494  23.757  -12.309 1.00 35.16  ?  366 TRP A CA    1 
ATOM   2698 C  C     . TRP A 1 380 ? 33.819  23.442  -12.984 1.00 36.94  ?  366 TRP A C     1 
ATOM   2699 O  O     . TRP A 1 380 ? 34.553  22.559  -12.522 1.00 37.97  ?  366 TRP A O     1 
ATOM   2700 C  CB    . TRP A 1 380 ? 31.355  22.919  -12.898 1.00 33.12  ?  366 TRP A CB    1 
ATOM   2701 C  CG    . TRP A 1 380 ? 30.139  23.014  -12.040 1.00 31.47  ?  366 TRP A CG    1 
ATOM   2702 C  CD1   . TRP A 1 380 ? 28.967  23.642  -12.340 1.00 31.41  ?  366 TRP A CD1   1 
ATOM   2703 C  CD2   . TRP A 1 380 ? 29.993  22.501  -10.713 1.00 30.11  ?  366 TRP A CD2   1 
ATOM   2704 N  NE1   . TRP A 1 380 ? 28.093  23.544  -11.284 1.00 32.60  ?  366 TRP A NE1   1 
ATOM   2705 C  CE2   . TRP A 1 380 ? 28.702  22.850  -10.271 1.00 35.89  ?  366 TRP A CE2   1 
ATOM   2706 C  CE3   . TRP A 1 380 ? 30.830  21.781  -9.853  1.00 30.18  ?  366 TRP A CE3   1 
ATOM   2707 C  CZ2   . TRP A 1 380 ? 28.225  22.496  -9.011  1.00 29.65  ?  366 TRP A CZ2   1 
ATOM   2708 C  CZ3   . TRP A 1 380 ? 30.358  21.434  -8.606  1.00 28.70  ?  366 TRP A CZ3   1 
ATOM   2709 C  CH2   . TRP A 1 380 ? 29.067  21.789  -8.196  1.00 36.45  ?  366 TRP A CH2   1 
ATOM   2710 N  N     . LYS A 1 381 ? 34.149  24.153  -14.065 1.00 33.11  ?  367 LYS A N     1 
ATOM   2711 C  CA    . LYS A 1 381 ? 35.469  24.002  -14.671 1.00 42.99  ?  367 LYS A CA    1 
ATOM   2712 C  C     . LYS A 1 381 ? 36.570  24.491  -13.736 1.00 36.23  ?  367 LYS A C     1 
ATOM   2713 O  O     . LYS A 1 381 ? 37.655  23.898  -13.679 1.00 37.94  ?  367 LYS A O     1 
ATOM   2714 C  CB    . LYS A 1 381 ? 35.515  24.737  -16.009 1.00 38.64  ?  367 LYS A CB    1 
ATOM   2715 C  CG    . LYS A 1 381 ? 34.828  23.968  -17.121 1.00 41.07  ?  367 LYS A CG    1 
ATOM   2716 C  CD    . LYS A 1 381 ? 34.781  24.751  -18.418 1.00 51.62  ?  367 LYS A CD    1 
ATOM   2717 C  CE    . LYS A 1 381 ? 33.914  24.029  -19.445 1.00 58.07  ?  367 LYS A CE    1 
ATOM   2718 N  NZ    . LYS A 1 381 ? 33.764  24.823  -20.698 1.00 52.93  ?  367 LYS A NZ    1 
ATOM   2719 N  N     . THR A 1 382 ? 36.328  25.593  -13.024 1.00 37.14  ?  368 THR A N     1 
ATOM   2720 C  CA    . THR A 1 382 ? 37.304  26.073  -12.050 1.00 40.45  ?  368 THR A CA    1 
ATOM   2721 C  C     . THR A 1 382 ? 37.465  25.089  -10.894 1.00 43.35  ?  368 THR A C     1 
ATOM   2722 O  O     . THR A 1 382 ? 38.590  24.788  -10.478 1.00 41.89  ?  368 THR A O     1 
ATOM   2723 C  CB    . THR A 1 382 ? 36.886  27.455  -11.546 1.00 35.12  ?  368 THR A CB    1 
ATOM   2724 O  OG1   . THR A 1 382 ? 36.886  28.366  -12.648 1.00 33.43  ?  368 THR A OG1   1 
ATOM   2725 C  CG2   . THR A 1 382 ? 37.841  27.964  -10.480 1.00 35.59  ?  368 THR A CG2   1 
ATOM   2726 N  N     . LEU A 1 383 ? 36.354  24.548  -10.391 1.00 38.88  ?  369 LEU A N     1 
ATOM   2727 C  CA    . LEU A 1 383 ? 36.428  23.578  -9.304  1.00 38.40  ?  369 LEU A CA    1 
ATOM   2728 C  C     . LEU A 1 383 ? 37.151  22.307  -9.734  1.00 38.88  ?  369 LEU A C     1 
ATOM   2729 O  O     . LEU A 1 383 ? 37.817  21.662  -8.915  1.00 37.79  ?  369 LEU A O     1 
ATOM   2730 C  CB    . LEU A 1 383 ? 35.021  23.250  -8.807  1.00 38.97  ?  369 LEU A CB    1 
ATOM   2731 C  CG    . LEU A 1 383 ? 34.908  22.495  -7.484  1.00 42.48  ?  369 LEU A CG    1 
ATOM   2732 C  CD1   . LEU A 1 383 ? 35.690  23.187  -6.379  1.00 39.98  ?  369 LEU A CD1   1 
ATOM   2733 C  CD2   . LEU A 1 383 ? 33.450  22.365  -7.107  1.00 54.68  ?  369 LEU A CD2   1 
ATOM   2734 N  N     . GLN A 1 384 ? 37.044  21.940  -11.014 1.00 38.05  ?  370 GLN A N     1 
ATOM   2735 C  CA    . GLN A 1 384 ? 37.715  20.740  -11.503 1.00 37.84  ?  370 GLN A CA    1 
ATOM   2736 C  C     . GLN A 1 384 ? 39.224  20.821  -11.290 1.00 40.88  ?  370 GLN A C     1 
ATOM   2737 O  O     . GLN A 1 384 ? 39.857  19.832  -10.904 1.00 40.72  ?  370 GLN A O     1 
ATOM   2738 C  CB    . GLN A 1 384 ? 37.398  20.531  -12.983 1.00 32.32  ?  370 GLN A CB    1 
ATOM   2739 C  CG    . GLN A 1 384 ? 38.133  19.357  -13.605 1.00 31.92  ?  370 GLN A CG    1 
ATOM   2740 C  CD    . GLN A 1 384 ? 37.707  18.032  -12.996 1.00 36.58  ?  370 GLN A CD    1 
ATOM   2741 O  OE1   . GLN A 1 384 ? 36.515  17.743  -12.882 1.00 39.04  ?  370 GLN A OE1   1 
ATOM   2742 N  NE2   . GLN A 1 384 ? 38.679  17.225  -12.594 1.00 41.36  ?  370 GLN A NE2   1 
ATOM   2743 N  N     . THR A 1 385 ? 39.820  21.990  -11.531 1.00 42.61  ?  371 THR A N     1 
ATOM   2744 C  CA    . THR A 1 385 ? 41.259  22.135  -11.334 1.00 42.62  ?  371 THR A CA    1 
ATOM   2745 C  C     . THR A 1 385 ? 41.659  22.123  -9.863  1.00 34.81  ?  371 THR A C     1 
ATOM   2746 O  O     . THR A 1 385 ? 42.848  21.971  -9.565  1.00 42.66  ?  371 THR A O     1 
ATOM   2747 C  CB    . THR A 1 385 ? 41.763  23.426  -11.992 1.00 38.07  ?  371 THR A CB    1 
ATOM   2748 O  OG1   . THR A 1 385 ? 41.285  24.561  -11.260 1.00 46.02  ?  371 THR A OG1   1 
ATOM   2749 C  CG2   . THR A 1 385 ? 41.271  23.522  -13.426 1.00 39.96  ?  371 THR A CG2   1 
ATOM   2750 N  N     . PHE A 1 386 ? 40.704  22.259  -8.945  1.00 33.66  ?  372 PHE A N     1 
ATOM   2751 C  CA    . PHE A 1 386 ? 40.990  22.387  -7.520  1.00 39.85  ?  372 PHE A CA    1 
ATOM   2752 C  C     . PHE A 1 386 ? 40.952  21.052  -6.771  1.00 40.27  ?  372 PHE A C     1 
ATOM   2753 O  O     . PHE A 1 386 ? 41.688  20.880  -5.793  1.00 41.79  ?  372 PHE A O     1 
ATOM   2754 C  CB    . PHE A 1 386 ? 39.997  23.375  -6.893  1.00 35.80  ?  372 PHE A CB    1 
ATOM   2755 C  CG    . PHE A 1 386 ? 40.140  23.538  -5.403  1.00 41.66  ?  372 PHE A CG    1 
ATOM   2756 C  CD1   . PHE A 1 386 ? 41.195  24.258  -4.865  1.00 42.19  ?  372 PHE A CD1   1 
ATOM   2757 C  CD2   . PHE A 1 386 ? 39.200  22.987  -4.541  1.00 46.12  ?  372 PHE A CD2   1 
ATOM   2758 C  CE1   . PHE A 1 386 ? 41.318  24.416  -3.495  1.00 41.31  ?  372 PHE A CE1   1 
ATOM   2759 C  CE2   . PHE A 1 386 ? 39.319  23.141  -3.169  1.00 40.66  ?  372 PHE A CE2   1 
ATOM   2760 C  CZ    . PHE A 1 386 ? 40.380  23.854  -2.646  1.00 43.44  ?  372 PHE A CZ    1 
ATOM   2761 N  N     . ILE A 1 387 ? 40.115  20.102  -7.191  1.00 39.99  ?  373 ILE A N     1 
ATOM   2762 C  CA    . ILE A 1 387 ? 39.973  18.856  -6.440  1.00 39.74  ?  373 ILE A CA    1 
ATOM   2763 C  C     . ILE A 1 387 ? 41.248  18.020  -6.542  1.00 39.96  ?  373 ILE A C     1 
ATOM   2764 O  O     . ILE A 1 387 ? 41.991  18.085  -7.533  1.00 44.71  ?  373 ILE A O     1 
ATOM   2765 C  CB    . ILE A 1 387 ? 38.742  18.072  -6.931  1.00 36.63  ?  373 ILE A CB    1 
ATOM   2766 C  CG1   . ILE A 1 387 ? 38.920  17.650  -8.388  1.00 38.26  ?  373 ILE A CG1   1 
ATOM   2767 C  CG2   . ILE A 1 387 ? 37.487  18.919  -6.781  1.00 29.57  ?  373 ILE A CG2   1 
ATOM   2768 C  CD1   . ILE A 1 387 ? 37.649  17.118  -9.019  1.00 42.31  ?  373 ILE A CD1   1 
ATOM   2769 N  N     . ARG A 1 388 ? 41.518  17.243  -5.497  1.00 34.15  ?  374 ARG A N     1 
ATOM   2770 C  CA    . ARG A 1 388 ? 42.738  16.462  -5.373  1.00 37.96  ?  374 ARG A CA    1 
ATOM   2771 C  C     . ARG A 1 388 ? 42.413  15.069  -4.849  1.00 42.78  ?  374 ARG A C     1 
ATOM   2772 O  O     . ARG A 1 388 ? 41.337  14.852  -4.279  1.00 38.57  ?  374 ARG A O     1 
ATOM   2773 C  CB    . ARG A 1 388 ? 43.748  17.137  -4.432  1.00 37.56  ?  374 ARG A CB    1 
ATOM   2774 C  CG    . ARG A 1 388 ? 44.309  18.448  -4.948  1.00 42.14  ?  374 ARG A CG    1 
ATOM   2775 C  CD    . ARG A 1 388 ? 45.484  18.232  -5.897  1.00 42.80  ?  374 ARG A CD    1 
ATOM   2776 N  NE    . ARG A 1 388 ? 46.026  19.497  -6.384  1.00 52.51  ?  374 ARG A NE    1 
ATOM   2777 C  CZ    . ARG A 1 388 ? 45.411  20.298  -7.245  1.00 56.01  ?  374 ARG A CZ    1 
ATOM   2778 N  NH1   . ARG A 1 388 ? 44.228  19.990  -7.755  1.00 51.57  ?  374 ARG A NH1   1 
ATOM   2779 N  NH2   . ARG A 1 388 ? 45.998  21.436  -7.606  1.00 53.08  ?  374 ARG A NH2   1 
ATOM   2780 N  N     . PRO A 1 389 ? 43.325  14.111  -5.017  1.00 37.44  ?  375 PRO A N     1 
ATOM   2781 C  CA    . PRO A 1 389 ? 43.140  12.803  -4.374  1.00 33.71  ?  375 PRO A CA    1 
ATOM   2782 C  C     . PRO A 1 389 ? 43.000  12.947  -2.865  1.00 35.06  ?  375 PRO A C     1 
ATOM   2783 O  O     . PRO A 1 389 ? 43.621  13.813  -2.244  1.00 38.53  ?  375 PRO A O     1 
ATOM   2784 C  CB    . PRO A 1 389 ? 44.418  12.039  -4.747  1.00 40.23  ?  375 PRO A CB    1 
ATOM   2785 C  CG    . PRO A 1 389 ? 44.885  12.665  -6.010  1.00 36.56  ?  375 PRO A CG    1 
ATOM   2786 C  CD    . PRO A 1 389 ? 44.444  14.104  -5.979  1.00 38.73  ?  375 PRO A CD    1 
ATOM   2787 N  N     . GLY A 1 390 ? 42.155  12.101  -2.280  1.00 36.51  ?  376 GLY A N     1 
ATOM   2788 C  CA    . GLY A 1 390 ? 41.887  12.144  -0.857  1.00 38.07  ?  376 GLY A CA    1 
ATOM   2789 C  C     . GLY A 1 390 ? 40.770  13.075  -0.432  1.00 38.99  ?  376 GLY A C     1 
ATOM   2790 O  O     . GLY A 1 390 ? 40.428  13.100  0.758   1.00 37.50  ?  376 GLY A O     1 
ATOM   2791 N  N     . ASP A 1 391 ? 40.193  13.840  -1.356  1.00 32.86  ?  377 ASP A N     1 
ATOM   2792 C  CA    . ASP A 1 391 ? 39.140  14.781  -1.002  1.00 39.03  ?  377 ASP A CA    1 
ATOM   2793 C  C     . ASP A 1 391 ? 37.851  14.065  -0.610  1.00 38.86  ?  377 ASP A C     1 
ATOM   2794 O  O     . ASP A 1 391 ? 37.504  13.005  -1.143  1.00 33.04  ?  377 ASP A O     1 
ATOM   2795 C  CB    . ASP A 1 391 ? 38.845  15.727  -2.170  1.00 31.71  ?  377 ASP A CB    1 
ATOM   2796 C  CG    . ASP A 1 391 ? 39.784  16.927  -2.210  1.00 42.88  ?  377 ASP A CG    1 
ATOM   2797 O  OD1   . ASP A 1 391 ? 40.478  17.185  -1.203  1.00 36.38  ?  377 ASP A OD1   1 
ATOM   2798 O  OD2   . ASP A 1 391 ? 39.823  17.612  -3.257  1.00 32.39  ?  377 ASP A OD2   1 
ATOM   2799 N  N     . ILE A 1 392 ? 37.135  14.661  0.336   1.00 37.50  ?  378 ILE A N     1 
ATOM   2800 C  CA    . ILE A 1 392 ? 35.743  14.318  0.599   1.00 35.39  ?  378 ILE A CA    1 
ATOM   2801 C  C     . ILE A 1 392 ? 34.908  15.465  0.056   1.00 32.62  ?  378 ILE A C     1 
ATOM   2802 O  O     . ILE A 1 392 ? 35.047  16.610  0.505   1.00 33.95  ?  378 ILE A O     1 
ATOM   2803 C  CB    . ILE A 1 392 ? 35.472  14.085  2.092   1.00 32.60  ?  378 ILE A CB    1 
ATOM   2804 C  CG1   . ILE A 1 392 ? 36.343  12.939  2.608   1.00 28.63  ?  378 ILE A CG1   1 
ATOM   2805 C  CG2   . ILE A 1 392 ? 33.979  13.786  2.322   1.00 27.18  ?  378 ILE A CG2   1 
ATOM   2806 C  CD1   . ILE A 1 392 ? 36.255  12.729  4.091   1.00 30.30  ?  378 ILE A CD1   1 
ATOM   2807 N  N     . ILE A 1 393 ? 34.063  15.165  -0.923  1.00 32.12  ?  379 ILE A N     1 
ATOM   2808 C  CA    . ILE A 1 393 ? 33.266  16.162  -1.626  1.00 25.80  ?  379 ILE A CA    1 
ATOM   2809 C  C     . ILE A 1 393 ? 31.798  15.853  -1.367  1.00 27.38  ?  379 ILE A C     1 
ATOM   2810 O  O     . ILE A 1 393 ? 31.338  14.734  -1.629  1.00 29.69  ?  379 ILE A O     1 
ATOM   2811 C  CB    . ILE A 1 393 ? 33.563  16.160  -3.133  1.00 22.81  ?  379 ILE A CB    1 
ATOM   2812 C  CG1   . ILE A 1 393 ? 35.015  16.565  -3.398  1.00 31.54  ?  379 ILE A CG1   1 
ATOM   2813 C  CG2   . ILE A 1 393 ? 32.569  17.056  -3.867  1.00 26.99  ?  379 ILE A CG2   1 
ATOM   2814 C  CD1   . ILE A 1 393 ? 35.477  16.306  -4.816  1.00 25.85  ?  379 ILE A CD1   1 
ATOM   2815 N  N     . LEU A 1 394 ? 31.064  16.838  -0.857  1.00 25.64  ?  380 LEU A N     1 
ATOM   2816 C  CA    . LEU A 1 394 ? 29.636  16.706  -0.600  1.00 29.99  ?  380 LEU A CA    1 
ATOM   2817 C  C     . LEU A 1 394 ? 28.898  17.783  -1.376  1.00 32.23  ?  380 LEU A C     1 
ATOM   2818 O  O     . LEU A 1 394 ? 29.294  18.952  -1.343  1.00 25.65  ?  380 LEU A O     1 
ATOM   2819 C  CB    . LEU A 1 394 ? 29.321  16.822  0.893   1.00 25.22  ?  380 LEU A CB    1 
ATOM   2820 C  CG    . LEU A 1 394 ? 30.094  15.923  1.860   1.00 30.21  ?  380 LEU A CG    1 
ATOM   2821 C  CD1   . LEU A 1 394 ? 31.345  16.611  2.339   1.00 28.03  ?  380 LEU A CD1   1 
ATOM   2822 C  CD2   . LEU A 1 394 ? 29.220  15.546  3.044   1.00 27.03  ?  380 LEU A CD2   1 
ATOM   2823 N  N     . ALA A 1 395 ? 27.829  17.388  -2.070  1.00 31.33  ?  381 ALA A N     1 
ATOM   2824 C  CA    . ALA A 1 395 ? 27.045  18.299  -2.897  1.00 32.90  ?  381 ALA A CA    1 
ATOM   2825 C  C     . ALA A 1 395 ? 25.560  18.101  -2.617  1.00 36.92  ?  381 ALA A C     1 
ATOM   2826 O  O     . ALA A 1 395 ? 25.075  16.964  -2.613  1.00 30.12  ?  381 ALA A O     1 
ATOM   2827 C  CB    . ALA A 1 395 ? 27.341  18.077  -4.383  1.00 29.06  ?  381 ALA A CB    1 
ATOM   2828 N  N     . ASP A 1 396 ? 24.840  19.202  -2.397  1.00 30.56  ?  382 ASP A N     1 
ATOM   2829 C  CA    . ASP A 1 396 ? 23.425  19.130  -2.060  1.00 34.81  ?  382 ASP A CA    1 
ATOM   2830 C  C     . ASP A 1 396 ? 22.553  19.178  -3.306  1.00 31.38  ?  382 ASP A C     1 
ATOM   2831 O  O     . ASP A 1 396 ? 22.977  19.623  -4.375  1.00 35.38  ?  382 ASP A O     1 
ATOM   2832 C  CB    . ASP A 1 396 ? 23.015  20.258  -1.111  1.00 29.10  ?  382 ASP A CB    1 
ATOM   2833 C  CG    . ASP A 1 396 ? 21.981  19.802  -0.091  1.00 39.70  ?  382 ASP A CG    1 
ATOM   2834 O  OD1   . ASP A 1 396 ? 21.144  18.923  -0.426  1.00 32.59  ?  382 ASP A OD1   1 
ATOM   2835 O  OD2   . ASP A 1 396 ? 22.004  20.319  1.049   1.00 35.13  ?  382 ASP A OD2   1 
ATOM   2836 N  N     . GLN A 1 397 ? 21.314  18.708  -3.143  1.00 28.70  ?  383 GLN A N     1 
ATOM   2837 C  CA    . GLN A 1 397 ? 20.330  18.772  -4.213  1.00 27.50  ?  383 GLN A CA    1 
ATOM   2838 C  C     . GLN A 1 397 ? 20.131  20.212  -4.657  1.00 34.12  ?  383 GLN A C     1 
ATOM   2839 O  O     . GLN A 1 397 ? 20.052  21.130  -3.838  1.00 44.01  ?  383 GLN A O     1 
ATOM   2840 C  CB    . GLN A 1 397 ? 19.004  18.173  -3.749  1.00 29.39  ?  383 GLN A CB    1 
ATOM   2841 C  CG    . GLN A 1 397 ? 19.089  16.692  -3.454  1.00 35.89  ?  383 GLN A CG    1 
ATOM   2842 C  CD    . GLN A 1 397 ? 19.746  15.926  -4.579  1.00 40.06  ?  383 GLN A CD    1 
ATOM   2843 O  OE1   . GLN A 1 397 ? 19.177  15.791  -5.661  1.00 49.52  ?  383 GLN A OE1   1 
ATOM   2844 N  NE2   . GLN A 1 397 ? 20.953  15.422  -4.333  1.00 35.47  ?  383 GLN A NE2   1 
ATOM   2845 N  N     . GLY A 1 398 ? 20.064  20.406  -5.961  1.00 38.62  ?  384 GLY A N     1 
ATOM   2846 C  CA    . GLY A 1 398 ? 20.136  21.718  -6.553  1.00 34.68  ?  384 GLY A CA    1 
ATOM   2847 C  C     . GLY A 1 398 ? 21.174  21.722  -7.644  1.00 40.36  ?  384 GLY A C     1 
ATOM   2848 O  O     . GLY A 1 398 ? 21.636  20.670  -8.101  1.00 35.16  ?  384 GLY A O     1 
ATOM   2849 N  N     . THR A 1 399 ? 21.570  22.924  -8.069  1.00 29.76  ?  385 THR A N     1 
ATOM   2850 C  CA    . THR A 1 399 ? 22.624  23.021  -9.068  1.00 31.23  ?  385 THR A CA    1 
ATOM   2851 C  C     . THR A 1 399 ? 23.939  22.446  -8.560  1.00 31.41  ?  385 THR A C     1 
ATOM   2852 O  O     . THR A 1 399 ? 24.788  22.065  -9.373  1.00 35.18  ?  385 THR A O     1 
ATOM   2853 C  CB    . THR A 1 399 ? 22.827  24.480  -9.502  1.00 31.29  ?  385 THR A CB    1 
ATOM   2854 O  OG1   . THR A 1 399 ? 23.307  25.255  -8.397  1.00 35.30  ?  385 THR A OG1   1 
ATOM   2855 C  CG2   . THR A 1 399 ? 21.527  25.081  -10.002 1.00 29.39  ?  385 THR A CG2   1 
ATOM   2856 N  N     . SER A 1 400 ? 24.119  22.373  -7.237  1.00 30.12  ?  386 SER A N     1 
ATOM   2857 C  CA    . SER A 1 400 ? 25.340  21.814  -6.662  1.00 29.00  ?  386 SER A CA    1 
ATOM   2858 C  C     . SER A 1 400 ? 25.517  20.349  -7.051  1.00 35.04  ?  386 SER A C     1 
ATOM   2859 O  O     . SER A 1 400 ? 26.514  19.976  -7.679  1.00 31.24  ?  386 SER A O     1 
ATOM   2860 C  CB    . SER A 1 400 ? 25.318  21.973  -5.141  1.00 26.48  ?  386 SER A CB    1 
ATOM   2861 O  OG    . SER A 1 400 ? 25.556  23.318  -4.766  1.00 32.12  ?  386 SER A OG    1 
ATOM   2862 N  N     . ALA A 1 401 ? 24.566  19.491  -6.664  1.00 32.12  ?  387 ALA A N     1 
ATOM   2863 C  CA    . ALA A 1 401 ? 24.680  18.077  -7.018  1.00 31.98  ?  387 ALA A CA    1 
ATOM   2864 C  C     . ALA A 1 401 ? 24.588  17.881  -8.525  1.00 36.12  ?  387 ALA A C     1 
ATOM   2865 O  O     . ALA A 1 401 ? 25.299  17.045  -9.094  1.00 30.05  ?  387 ALA A O     1 
ATOM   2866 C  CB    . ALA A 1 401 ? 23.604  17.255  -6.307  1.00 26.66  ?  387 ALA A CB    1 
ATOM   2867 N  N     . PHE A 1 402 ? 23.717  18.645  -9.187  1.00 34.08  ?  388 PHE A N     1 
ATOM   2868 C  CA    . PHE A 1 402 ? 23.499  18.455  -10.616 1.00 42.78  ?  388 PHE A CA    1 
ATOM   2869 C  C     . PHE A 1 402 ? 24.646  19.002  -11.459 1.00 41.47  ?  388 PHE A C     1 
ATOM   2870 O  O     . PHE A 1 402 ? 24.764  18.641  -12.636 1.00 31.85  ?  388 PHE A O     1 
ATOM   2871 C  CB    . PHE A 1 402 ? 22.172  19.098  -11.025 1.00 33.56  ?  388 PHE A CB    1 
ATOM   2872 C  CG    . PHE A 1 402 ? 20.969  18.513  -10.321 1.00 40.37  ?  388 PHE A CG    1 
ATOM   2873 C  CD1   . PHE A 1 402 ? 21.038  17.270  -9.706  1.00 48.60  ?  388 PHE A CD1   1 
ATOM   2874 C  CD2   . PHE A 1 402 ? 19.774  19.206  -10.274 1.00 44.72  ?  388 PHE A CD2   1 
ATOM   2875 C  CE1   . PHE A 1 402 ? 19.935  16.733  -9.061  1.00 53.13  ?  388 PHE A CE1   1 
ATOM   2876 C  CE2   . PHE A 1 402 ? 18.667  18.674  -9.630  1.00 48.34  ?  388 PHE A CE2   1 
ATOM   2877 C  CZ    . PHE A 1 402 ? 18.748  17.439  -9.024  1.00 49.84  ?  388 PHE A CZ    1 
ATOM   2878 N  N     . GLY A 1 403 ? 25.498  19.848  -10.887 1.00 30.92  ?  389 GLY A N     1 
ATOM   2879 C  CA    . GLY A 1 403 ? 26.672  20.307  -11.600 1.00 31.79  ?  389 GLY A CA    1 
ATOM   2880 C  C     . GLY A 1 403 ? 27.899  19.495  -11.244 1.00 32.61  ?  389 GLY A C     1 
ATOM   2881 O  O     . GLY A 1 403 ? 28.772  19.263  -12.089 1.00 29.84  ?  389 GLY A O     1 
ATOM   2882 N  N     . ALA A 1 404 ? 27.966  19.046  -9.988  1.00 28.30  ?  390 ALA A N     1 
ATOM   2883 C  CA    . ALA A 1 404 ? 29.109  18.259  -9.541  1.00 32.66  ?  390 ALA A CA    1 
ATOM   2884 C  C     . ALA A 1 404 ? 29.218  16.931  -10.276 1.00 31.20  ?  390 ALA A C     1 
ATOM   2885 O  O     . ALA A 1 404 ? 30.304  16.342  -10.300 1.00 32.24  ?  390 ALA A O     1 
ATOM   2886 C  CB    . ALA A 1 404 ? 29.030  18.017  -8.034  1.00 27.43  ?  390 ALA A CB    1 
ATOM   2887 N  N     . ILE A 1 405 ? 28.131  16.461  -10.897 1.00 34.20  ?  391 ILE A N     1 
ATOM   2888 C  CA    . ILE A 1 405 ? 28.159  15.195  -11.619 1.00 34.47  ?  391 ILE A CA    1 
ATOM   2889 C  C     . ILE A 1 405 ? 29.171  15.220  -12.760 1.00 44.59  ?  391 ILE A C     1 
ATOM   2890 O  O     . ILE A 1 405 ? 29.637  14.159  -13.199 1.00 30.01  ?  391 ILE A O     1 
ATOM   2891 C  CB    . ILE A 1 405 ? 26.745  14.840  -12.132 1.00 29.63  ?  391 ILE A CB    1 
ATOM   2892 C  CG1   . ILE A 1 405 ? 26.642  13.342  -12.442 1.00 27.62  ?  391 ILE A CG1   1 
ATOM   2893 C  CG2   . ILE A 1 405 ? 26.383  15.662  -13.361 1.00 33.62  ?  391 ILE A CG2   1 
ATOM   2894 C  CD1   . ILE A 1 405 ? 25.271  12.906  -12.914 1.00 30.18  ?  391 ILE A CD1   1 
ATOM   2895 N  N     . ASP A 1 406 ? 29.520  16.408  -13.256 1.00 33.95  ?  392 ASP A N     1 
ATOM   2896 C  CA    . ASP A 1 406 ? 30.460  16.567  -14.359 1.00 29.53  ?  392 ASP A CA    1 
ATOM   2897 C  C     . ASP A 1 406 ? 31.916  16.622  -13.907 1.00 31.95  ?  392 ASP A C     1 
ATOM   2898 O  O     . ASP A 1 406 ? 32.809  16.699  -14.756 1.00 32.58  ?  392 ASP A O     1 
ATOM   2899 C  CB    . ASP A 1 406 ? 30.120  17.829  -15.158 1.00 41.83  ?  392 ASP A CB    1 
ATOM   2900 C  CG    . ASP A 1 406 ? 28.771  17.735  -15.856 1.00 38.43  ?  392 ASP A CG    1 
ATOM   2901 O  OD1   . ASP A 1 406 ? 28.418  16.630  -16.312 1.00 40.19  ?  392 ASP A OD1   1 
ATOM   2902 O  OD2   . ASP A 1 406 ? 28.069  18.764  -15.957 1.00 50.66  ?  392 ASP A OD2   1 
ATOM   2903 N  N     . LEU A 1 407 ? 32.180  16.619  -12.604 1.00 32.31  ?  393 LEU A N     1 
ATOM   2904 C  CA    . LEU A 1 407 ? 33.556  16.586  -12.130 1.00 30.81  ?  393 LEU A CA    1 
ATOM   2905 C  C     . LEU A 1 407 ? 34.206  15.245  -12.454 1.00 37.46  ?  393 LEU A C     1 
ATOM   2906 O  O     . LEU A 1 407 ? 33.580  14.187  -12.342 1.00 31.72  ?  393 LEU A O     1 
ATOM   2907 C  CB    . LEU A 1 407 ? 33.610  16.836  -10.625 1.00 26.92  ?  393 LEU A CB    1 
ATOM   2908 C  CG    . LEU A 1 407 ? 33.196  18.226  -10.148 1.00 37.05  ?  393 LEU A CG    1 
ATOM   2909 C  CD1   . LEU A 1 407 ? 32.963  18.211  -8.645  1.00 27.95  ?  393 LEU A CD1   1 
ATOM   2910 C  CD2   . LEU A 1 407 ? 34.233  19.288  -10.542 1.00 34.17  ?  393 LEU A CD2   1 
ATOM   2911 N  N     . ARG A 1 408 ? 35.471  15.296  -12.866 1.00 36.60  ?  394 ARG A N     1 
ATOM   2912 C  CA    . ARG A 1 408 ? 36.275  14.101  -13.110 1.00 36.26  ?  394 ARG A CA    1 
ATOM   2913 C  C     . ARG A 1 408 ? 37.093  13.858  -11.845 1.00 38.14  ?  394 ARG A C     1 
ATOM   2914 O  O     . ARG A 1 408 ? 38.099  14.531  -11.603 1.00 35.88  ?  394 ARG A O     1 
ATOM   2915 C  CB    . ARG A 1 408 ? 37.154  14.280  -14.342 1.00 41.11  ?  394 ARG A CB    1 
ATOM   2916 C  CG    . ARG A 1 408 ? 37.973  13.058  -14.703 1.00 48.01  ?  394 ARG A CG    1 
ATOM   2917 C  CD    . ARG A 1 408 ? 38.059  12.870  -16.208 1.00 49.86  ?  394 ARG A CD    1 
ATOM   2918 N  NE    . ARG A 1 408 ? 39.330  13.336  -16.749 1.00 61.40  ?  394 ARG A NE    1 
ATOM   2919 C  CZ    . ARG A 1 408 ? 39.990  12.737  -17.732 1.00 82.39  ?  394 ARG A CZ    1 
ATOM   2920 N  NH1   . ARG A 1 408 ? 39.532  11.633  -18.301 1.00 68.41  ?  394 ARG A NH1   1 
ATOM   2921 N  NH2   . ARG A 1 408 ? 41.142  13.256  -18.151 1.00 82.78  ?  394 ARG A NH2   1 
ATOM   2922 N  N     . LEU A 1 409 ? 36.639  12.916  -11.024 1.00 37.10  ?  395 LEU A N     1 
ATOM   2923 C  CA    . LEU A 1 409 ? 37.213  12.724  -9.696  1.00 33.92  ?  395 LEU A CA    1 
ATOM   2924 C  C     . LEU A 1 409 ? 38.523  11.948  -9.782  1.00 41.66  ?  395 LEU A C     1 
ATOM   2925 O  O     . LEU A 1 409 ? 38.583  10.914  -10.456 1.00 38.83  ?  395 LEU A O     1 
ATOM   2926 C  CB    . LEU A 1 409 ? 36.240  11.982  -8.788  1.00 35.11  ?  395 LEU A CB    1 
ATOM   2927 C  CG    . LEU A 1 409 ? 34.854  12.579  -8.549  1.00 42.64  ?  395 LEU A CG    1 
ATOM   2928 C  CD1   . LEU A 1 409 ? 34.088  11.711  -7.554  1.00 31.41  ?  395 LEU A CD1   1 
ATOM   2929 C  CD2   . LEU A 1 409 ? 34.951  14.023  -8.062  1.00 29.84  ?  395 LEU A CD2   1 
ATOM   2930 N  N     . PRO A 1 410 ? 39.582  12.402  -9.105  1.00 44.37  ?  396 PRO A N     1 
ATOM   2931 C  CA    . PRO A 1 410 ? 40.807  11.596  -9.018  1.00 47.74  ?  396 PRO A CA    1 
ATOM   2932 C  C     . PRO A 1 410 ? 40.643  10.431  -8.054  1.00 43.70  ?  396 PRO A C     1 
ATOM   2933 O  O     . PRO A 1 410 ? 39.532  10.154  -7.588  1.00 44.93  ?  396 PRO A O     1 
ATOM   2934 C  CB    . PRO A 1 410 ? 41.860  12.596  -8.525  1.00 40.81  ?  396 PRO A CB    1 
ATOM   2935 C  CG    . PRO A 1 410 ? 41.092  13.721  -7.898  1.00 36.60  ?  396 PRO A CG    1 
ATOM   2936 C  CD    . PRO A 1 410 ? 39.637  13.604  -8.258  1.00 31.61  ?  396 PRO A CD    1 
ATOM   2937 N  N     . ALA A 1 411 ? 41.735  9.731   -7.767  1.00 40.68  ?  397 ALA A N     1 
ATOM   2938 C  CA    . ALA A 1 411 ? 41.674  8.555   -6.912  1.00 50.69  ?  397 ALA A CA    1 
ATOM   2939 C  C     . ALA A 1 411 ? 41.376  8.927   -5.462  1.00 39.63  ?  397 ALA A C     1 
ATOM   2940 O  O     . ALA A 1 411 ? 41.677  10.034  -5.003  1.00 43.33  ?  397 ALA A O     1 
ATOM   2941 C  CB    . ALA A 1 411 ? 42.993  7.782   -6.983  1.00 41.70  ?  397 ALA A CB    1 
ATOM   2942 N  N     . ASP A 1 412 ? 40.778  7.973   -4.741  1.00 38.69  ?  398 ASP A N     1 
ATOM   2943 C  CA    . ASP A 1 412 ? 40.575  8.059   -3.292  1.00 38.78  ?  398 ASP A CA    1 
ATOM   2944 C  C     . ASP A 1 412 ? 39.710  9.257   -2.891  1.00 41.28  ?  398 ASP A C     1 
ATOM   2945 O  O     . ASP A 1 412 ? 39.970  9.928   -1.891  1.00 41.36  ?  398 ASP A O     1 
ATOM   2946 C  CB    . ASP A 1 412 ? 41.916  8.086   -2.555  1.00 34.93  ?  398 ASP A CB    1 
ATOM   2947 C  CG    . ASP A 1 412 ? 42.737  6.833   -2.797  1.00 68.55  ?  398 ASP A CG    1 
ATOM   2948 O  OD1   . ASP A 1 412 ? 42.203  5.723   -2.581  1.00 75.32  ?  398 ASP A OD1   1 
ATOM   2949 O  OD2   . ASP A 1 412 ? 43.914  6.953   -3.206  1.00 70.28  ?  398 ASP A OD2   1 
ATOM   2950 N  N     . VAL A 1 413 ? 38.663  9.525   -3.662  1.00 40.79  ?  399 VAL A N     1 
ATOM   2951 C  CA    . VAL A 1 413 ? 37.718  10.593  -3.351  1.00 38.86  ?  399 VAL A CA    1 
ATOM   2952 C  C     . VAL A 1 413 ? 36.439  9.972   -2.807  1.00 38.70  ?  399 VAL A C     1 
ATOM   2953 O  O     . VAL A 1 413 ? 35.889  9.038   -3.404  1.00 37.11  ?  399 VAL A O     1 
ATOM   2954 C  CB    . VAL A 1 413 ? 37.422  11.463  -4.585  1.00 34.16  ?  399 VAL A CB    1 
ATOM   2955 C  CG1   . VAL A 1 413 ? 36.254  12.400  -4.307  1.00 29.87  ?  399 VAL A CG1   1 
ATOM   2956 C  CG2   . VAL A 1 413 ? 38.656  12.260  -4.972  1.00 33.92  ?  399 VAL A CG2   1 
ATOM   2957 N  N     . ASN A 1 414 ? 35.989  10.460  -1.656  1.00 31.42  ?  400 ASN A N     1 
ATOM   2958 C  CA    . ASN A 1 414 ? 34.682  10.107  -1.115  1.00 29.37  ?  400 ASN A CA    1 
ATOM   2959 C  C     . ASN A 1 414 ? 33.709  11.206  -1.529  1.00 35.80  ?  400 ASN A C     1 
ATOM   2960 O  O     . ASN A 1 414 ? 33.793  12.338  -1.041  1.00 30.19  ?  400 ASN A O     1 
ATOM   2961 C  CB    . ASN A 1 414 ? 34.732  9.944   0.403   1.00 27.50  ?  400 ASN A CB    1 
ATOM   2962 C  CG    . ASN A 1 414 ? 33.417  9.436   0.981   1.00 34.71  ?  400 ASN A CG    1 
ATOM   2963 O  OD1   . ASN A 1 414 ? 32.369  9.534   0.344   1.00 33.75  ?  400 ASN A OD1   1 
ATOM   2964 N  ND2   . ASN A 1 414 ? 33.470  8.886   2.190   1.00 33.19  ?  400 ASN A ND2   1 
ATOM   2965 N  N     . PHE A 1 415 ? 32.788  10.865  -2.425  1.00 31.59  ?  401 PHE A N     1 
ATOM   2966 C  CA    . PHE A 1 415 ? 31.836  11.804  -3.010  1.00 34.46  ?  401 PHE A CA    1 
ATOM   2967 C  C     . PHE A 1 415 ? 30.461  11.499  -2.423  1.00 38.19  ?  401 PHE A C     1 
ATOM   2968 O  O     . PHE A 1 415 ? 29.891  10.434  -2.690  1.00 30.78  ?  401 PHE A O     1 
ATOM   2969 C  CB    . PHE A 1 415 ? 31.861  11.676  -4.534  1.00 29.91  ?  401 PHE A CB    1 
ATOM   2970 C  CG    . PHE A 1 415 ? 30.860  12.539  -5.248  1.00 40.13  ?  401 PHE A CG    1 
ATOM   2971 C  CD1   . PHE A 1 415 ? 29.561  12.106  -5.442  1.00 30.28  ?  401 PHE A CD1   1 
ATOM   2972 C  CD2   . PHE A 1 415 ? 31.225  13.783  -5.744  1.00 38.51  ?  401 PHE A CD2   1 
ATOM   2973 C  CE1   . PHE A 1 415 ? 28.640  12.893  -6.108  1.00 30.53  ?  401 PHE A CE1   1 
ATOM   2974 C  CE2   . PHE A 1 415 ? 30.298  14.579  -6.410  1.00 42.02  ?  401 PHE A CE2   1 
ATOM   2975 C  CZ    . PHE A 1 415 ? 29.004  14.126  -6.591  1.00 30.65  ?  401 PHE A CZ    1 
ATOM   2976 N  N     . ILE A 1 416 ? 29.930  12.418  -1.619  1.00 29.30  ?  402 ILE A N     1 
ATOM   2977 C  CA    . ILE A 1 416 ? 28.707  12.173  -0.859  1.00 27.60  ?  402 ILE A CA    1 
ATOM   2978 C  C     . ILE A 1 416 ? 27.579  13.010  -1.444  1.00 36.65  ?  402 ILE A C     1 
ATOM   2979 O  O     . ILE A 1 416 ? 27.589  14.247  -1.360  1.00 28.96  ?  402 ILE A O     1 
ATOM   2980 C  CB    . ILE A 1 416 ? 28.888  12.475  0.634   1.00 33.88  ?  402 ILE A CB    1 
ATOM   2981 C  CG1   . ILE A 1 416 ? 29.769  11.416  1.290   1.00 26.86  ?  402 ILE A CG1   1 
ATOM   2982 C  CG2   . ILE A 1 416 ? 27.528  12.534  1.330   1.00 27.13  ?  402 ILE A CG2   1 
ATOM   2983 C  CD1   . ILE A 1 416 ? 30.262  11.815  2.661   1.00 27.93  ?  402 ILE A CD1   1 
ATOM   2984 N  N     . VAL A 1 417 ? 26.579  12.328  -1.987  1.00 36.34  ?  403 VAL A N     1 
ATOM   2985 C  CA    . VAL A 1 417 ? 25.413  12.972  -2.568  1.00 37.91  ?  403 VAL A CA    1 
ATOM   2986 C  C     . VAL A 1 417 ? 24.203  12.114  -2.223  1.00 44.73  ?  403 VAL A C     1 
ATOM   2987 O  O     . VAL A 1 417 ? 24.321  10.900  -2.025  1.00 31.24  ?  403 VAL A O     1 
ATOM   2988 C  CB    . VAL A 1 417 ? 25.599  13.161  -4.093  1.00 40.17  ?  403 VAL A CB    1 
ATOM   2989 C  CG1   . VAL A 1 417 ? 25.487  11.825  -4.828  1.00 29.22  ?  403 VAL A CG1   1 
ATOM   2990 C  CG2   . VAL A 1 417 ? 24.621  14.181  -4.635  1.00 41.31  ?  403 VAL A CG2   1 
ATOM   2991 N  N     . GLN A 1 418 ? 23.039  12.762  -2.112  1.00 34.20  ?  404 GLN A N     1 
ATOM   2992 C  CA    . GLN A 1 418 ? 21.809  12.122  -1.640  1.00 29.15  ?  404 GLN A CA    1 
ATOM   2993 C  C     . GLN A 1 418 ? 20.673  12.397  -2.624  1.00 29.53  ?  404 GLN A C     1 
ATOM   2994 O  O     . GLN A 1 418 ? 19.687  13.053  -2.284  1.00 25.35  ?  404 GLN A O     1 
ATOM   2995 C  CB    . GLN A 1 418 ? 21.454  12.624  -0.237  1.00 30.34  ?  404 GLN A CB    1 
ATOM   2996 C  CG    . GLN A 1 418 ? 20.340  11.852  0.484   1.00 29.64  ?  404 GLN A CG    1 
ATOM   2997 C  CD    . GLN A 1 418 ? 19.736  12.625  1.649   1.00 27.71  ?  404 GLN A CD    1 
ATOM   2998 O  OE1   . GLN A 1 418 ? 19.242  13.741  1.479   1.00 30.04  ?  404 GLN A OE1   1 
ATOM   2999 N  NE2   . GLN A 1 418 ? 19.757  12.026  2.835   1.00 26.15  ?  404 GLN A NE2   1 
ATOM   3000 N  N     . PRO A 1 419 ? 20.768  11.885  -3.854  1.00 31.91  ?  405 PRO A N     1 
ATOM   3001 C  CA    . PRO A 1 419 ? 19.755  12.219  -4.867  1.00 24.40  ?  405 PRO A CA    1 
ATOM   3002 C  C     . PRO A 1 419 ? 18.484  11.380  -4.803  1.00 38.56  ?  405 PRO A C     1 
ATOM   3003 O  O     . PRO A 1 419 ? 17.499  11.751  -5.459  1.00 29.98  ?  405 PRO A O     1 
ATOM   3004 C  CB    . PRO A 1 419 ? 20.493  11.979  -6.195  1.00 32.57  ?  405 PRO A CB    1 
ATOM   3005 C  CG    . PRO A 1 419 ? 21.771  11.273  -5.843  1.00 30.59  ?  405 PRO A CG    1 
ATOM   3006 C  CD    . PRO A 1 419 ? 21.779  10.961  -4.384  1.00 25.84  ?  405 PRO A CD    1 
ATOM   3007 N  N     . LEU A 1 420 ? 18.469  10.257  -4.077  1.00 27.01  ?  406 LEU A N     1 
ATOM   3008 C  CA    . LEU A 1 420 ? 17.226  9.498   -3.969  1.00 30.71  ?  406 LEU A CA    1 
ATOM   3009 C  C     . LEU A 1 420 ? 16.304  10.122  -2.929  1.00 24.92  ?  406 LEU A C     1 
ATOM   3010 O  O     . LEU A 1 420 ? 15.160  10.477  -3.232  1.00 28.62  ?  406 LEU A O     1 
ATOM   3011 C  CB    . LEU A 1 420 ? 17.505  8.027   -3.633  1.00 25.19  ?  406 LEU A CB    1 
ATOM   3012 C  CG    . LEU A 1 420 ? 16.244  7.211   -3.296  1.00 25.63  ?  406 LEU A CG    1 
ATOM   3013 C  CD1   . LEU A 1 420 ? 15.194  7.289   -4.401  1.00 25.74  ?  406 LEU A CD1   1 
ATOM   3014 C  CD2   . LEU A 1 420 ? 16.583  5.758   -2.993  1.00 26.09  ?  406 LEU A CD2   1 
ATOM   3015 N  N     . TRP A 1 421 ? 16.775  10.255  -1.688  1.00 23.51  ?  407 TRP A N     1 
ATOM   3016 C  CA    . TRP A 1 421 ? 15.970  10.970  -0.701  1.00 26.57  ?  407 TRP A CA    1 
ATOM   3017 C  C     . TRP A 1 421 ? 15.902  12.461  -1.035  1.00 28.25  ?  407 TRP A C     1 
ATOM   3018 O  O     . TRP A 1 421 ? 14.815  13.049  -1.074  1.00 31.42  ?  407 TRP A O     1 
ATOM   3019 C  CB    . TRP A 1 421 ? 16.527  10.739  0.703   1.00 24.01  ?  407 TRP A CB    1 
ATOM   3020 C  CG    . TRP A 1 421 ? 15.622  11.224  1.807   1.00 27.68  ?  407 TRP A CG    1 
ATOM   3021 C  CD1   . TRP A 1 421 ? 15.944  12.107  2.803   1.00 23.73  ?  407 TRP A CD1   1 
ATOM   3022 C  CD2   . TRP A 1 421 ? 14.256  10.848  2.031   1.00 24.68  ?  407 TRP A CD2   1 
ATOM   3023 N  NE1   . TRP A 1 421 ? 14.868  12.293  3.635   1.00 30.61  ?  407 TRP A NE1   1 
ATOM   3024 C  CE2   . TRP A 1 421 ? 13.817  11.539  3.179   1.00 31.92  ?  407 TRP A CE2   1 
ATOM   3025 C  CE3   . TRP A 1 421 ? 13.359  10.001  1.370   1.00 29.26  ?  407 TRP A CE3   1 
ATOM   3026 C  CZ2   . TRP A 1 421 ? 12.516  11.412  3.679   1.00 25.63  ?  407 TRP A CZ2   1 
ATOM   3027 C  CZ3   . TRP A 1 421 ? 12.071  9.870   1.873   1.00 31.34  ?  407 TRP A CZ3   1 
ATOM   3028 C  CH2   . TRP A 1 421 ? 11.665  10.571  3.015   1.00 27.71  ?  407 TRP A CH2   1 
ATOM   3029 N  N     . GLY A 1 422 ? 17.047  13.079  -1.312  1.00 24.98  ?  408 GLY A N     1 
ATOM   3030 C  CA    . GLY A 1 422 ? 17.070  14.449  -1.809  1.00 22.41  ?  408 GLY A CA    1 
ATOM   3031 C  C     . GLY A 1 422 ? 16.614  15.531  -0.855  1.00 24.28  ?  408 GLY A C     1 
ATOM   3032 O  O     . GLY A 1 422 ? 15.872  16.434  -1.261  1.00 25.39  ?  408 GLY A O     1 
ATOM   3033 N  N     . SER A 1 423 ? 17.046  15.475  0.400   1.00 26.47  ?  409 SER A N     1 
ATOM   3034 C  CA    . SER A 1 423 ? 16.652  16.458  1.407   1.00 23.59  ?  409 SER A CA    1 
ATOM   3035 C  C     . SER A 1 423 ? 17.692  17.572  1.438   1.00 27.75  ?  409 SER A C     1 
ATOM   3036 O  O     . SER A 1 423 ? 18.838  17.340  1.829   1.00 32.29  ?  409 SER A O     1 
ATOM   3037 C  CB    . SER A 1 423 ? 16.529  15.791  2.773   1.00 23.32  ?  409 SER A CB    1 
ATOM   3038 O  OG    . SER A 1 423 ? 16.161  16.717  3.772   1.00 28.90  ?  409 SER A OG    1 
ATOM   3039 N  N     . ILE A 1 424 ? 17.302  18.782  1.028   1.00 27.16  ?  410 ILE A N     1 
ATOM   3040 C  CA    . ILE A 1 424 ? 18.250  19.890  1.063   1.00 30.61  ?  410 ILE A CA    1 
ATOM   3041 C  C     . ILE A 1 424 ? 18.524  20.283  2.511   1.00 29.30  ?  410 ILE A C     1 
ATOM   3042 O  O     . ILE A 1 424 ? 17.675  20.125  3.402   1.00 27.59  ?  410 ILE A O     1 
ATOM   3043 C  CB    . ILE A 1 424 ? 17.770  21.095  0.235   1.00 23.23  ?  410 ILE A CB    1 
ATOM   3044 C  CG1   . ILE A 1 424 ? 16.512  21.727  0.841   1.00 27.82  ?  410 ILE A CG1   1 
ATOM   3045 C  CG2   . ILE A 1 424 ? 17.564  20.694  -1.226  1.00 28.71  ?  410 ILE A CG2   1 
ATOM   3046 C  CD1   . ILE A 1 424 ? 16.240  23.114  0.290   1.00 25.47  ?  410 ILE A CD1   1 
ATOM   3047 N  N     . GLY A 1 425 ? 19.739  20.766  2.752   1.00 25.11  ?  411 GLY A N     1 
ATOM   3048 C  CA    . GLY A 1 425 ? 20.263  20.962  4.082   1.00 27.63  ?  411 GLY A CA    1 
ATOM   3049 C  C     . GLY A 1 425 ? 21.097  19.800  4.581   1.00 32.13  ?  411 GLY A C     1 
ATOM   3050 O  O     . GLY A 1 425 ? 21.908  19.980  5.498   1.00 23.54  ?  411 GLY A O     1 
ATOM   3051 N  N     . TYR A 1 426 ? 20.956  18.628  3.954   1.00 29.45  ?  412 TYR A N     1 
ATOM   3052 C  CA    . TYR A 1 426 ? 21.702  17.449  4.381   1.00 29.69  ?  412 TYR A CA    1 
ATOM   3053 C  C     . TYR A 1 426 ? 23.207  17.695  4.284   1.00 27.52  ?  412 TYR A C     1 
ATOM   3054 O  O     . TYR A 1 426 ? 23.966  17.341  5.194   1.00 23.36  ?  412 TYR A O     1 
ATOM   3055 C  CB    . TYR A 1 426 ? 21.281  16.238  3.536   1.00 24.49  ?  412 TYR A CB    1 
ATOM   3056 C  CG    . TYR A 1 426 ? 22.248  15.071  3.582   1.00 27.58  ?  412 TYR A CG    1 
ATOM   3057 C  CD1   . TYR A 1 426 ? 22.169  14.118  4.590   1.00 24.64  ?  412 TYR A CD1   1 
ATOM   3058 C  CD2   . TYR A 1 426 ? 23.250  14.933  2.625   1.00 30.35  ?  412 TYR A CD2   1 
ATOM   3059 C  CE1   . TYR A 1 426 ? 23.055  13.053  4.641   1.00 26.76  ?  412 TYR A CE1   1 
ATOM   3060 C  CE2   . TYR A 1 426 ? 24.148  13.867  2.673   1.00 28.35  ?  412 TYR A CE2   1 
ATOM   3061 C  CZ    . TYR A 1 426 ? 24.044  12.939  3.682   1.00 26.98  ?  412 TYR A CZ    1 
ATOM   3062 O  OH    . TYR A 1 426 ? 24.928  11.888  3.738   1.00 24.13  ?  412 TYR A OH    1 
ATOM   3063 N  N     . THR A 1 427 ? 23.650  18.328  3.198   1.00 24.56  ?  413 THR A N     1 
ATOM   3064 C  CA    . THR A 1 427 ? 25.074  18.371  2.882   1.00 28.81  ?  413 THR A CA    1 
ATOM   3065 C  C     . THR A 1 427 ? 25.874  19.106  3.951   1.00 27.92  ?  413 THR A C     1 
ATOM   3066 O  O     . THR A 1 427 ? 26.909  18.611  4.411   1.00 28.36  ?  413 THR A O     1 
ATOM   3067 C  CB    . THR A 1 427 ? 25.262  19.044  1.527   1.00 31.06  ?  413 THR A CB    1 
ATOM   3068 O  OG1   . THR A 1 427 ? 24.677  18.220  0.514   1.00 33.58  ?  413 THR A OG1   1 
ATOM   3069 C  CG2   . THR A 1 427 ? 26.743  19.263  1.229   1.00 23.63  ?  413 THR A CG2   1 
ATOM   3070 N  N     . LEU A 1 428 ? 25.395  20.279  4.379   1.00 30.77  ?  414 LEU A N     1 
ATOM   3071 C  CA    . LEU A 1 428 ? 26.127  21.071  5.365   1.00 24.06  ?  414 LEU A CA    1 
ATOM   3072 C  C     . LEU A 1 428 ? 26.318  20.303  6.665   1.00 28.73  ?  414 LEU A C     1 
ATOM   3073 O  O     . LEU A 1 428 ? 27.420  20.269  7.221   1.00 27.78  ?  414 LEU A O     1 
ATOM   3074 C  CB    . LEU A 1 428 ? 25.397  22.385  5.628   1.00 30.40  ?  414 LEU A CB    1 
ATOM   3075 C  CG    . LEU A 1 428 ? 26.092  23.372  6.570   1.00 36.15  ?  414 LEU A CG    1 
ATOM   3076 C  CD1   . LEU A 1 428 ? 27.491  23.720  6.071   1.00 24.32  ?  414 LEU A CD1   1 
ATOM   3077 C  CD2   . LEU A 1 428 ? 25.241  24.636  6.749   1.00 28.62  ?  414 LEU A CD2   1 
ATOM   3078 N  N     . ALA A 1 429 ? 25.251  19.670  7.160   1.00 28.70  ?  415 ALA A N     1 
ATOM   3079 C  CA    . ALA A 1 429 ? 25.345  18.920  8.409   1.00 23.83  ?  415 ALA A CA    1 
ATOM   3080 C  C     . ALA A 1 429 ? 26.110  17.613  8.230   1.00 30.21  ?  415 ALA A C     1 
ATOM   3081 O  O     . ALA A 1 429 ? 26.869  17.211  9.121   1.00 29.12  ?  415 ALA A O     1 
ATOM   3082 C  CB    . ALA A 1 429 ? 23.943  18.650  8.962   1.00 24.21  ?  415 ALA A CB    1 
ATOM   3083 N  N     . ALA A 1 430 ? 25.910  16.922  7.101   1.00 26.92  ?  416 ALA A N     1 
ATOM   3084 C  CA    . ALA A 1 430 ? 26.667  15.697  6.846   1.00 25.93  ?  416 ALA A CA    1 
ATOM   3085 C  C     . ALA A 1 430 ? 28.156  15.980  6.730   1.00 34.42  ?  416 ALA A C     1 
ATOM   3086 O  O     . ALA A 1 430 ? 28.980  15.119  7.065   1.00 29.55  ?  416 ALA A O     1 
ATOM   3087 C  CB    . ALA A 1 430 ? 26.169  15.005  5.579   1.00 23.07  ?  416 ALA A CB    1 
ATOM   3088 N  N     . ALA A 1 431 ? 28.520  17.170  6.239   1.00 26.22  ?  417 ALA A N     1 
ATOM   3089 C  CA    . ALA A 1 431 ? 29.930  17.528  6.163   1.00 29.59  ?  417 ALA A CA    1 
ATOM   3090 C  C     . ALA A 1 431 ? 30.547  17.585  7.553   1.00 25.08  ?  417 ALA A C     1 
ATOM   3091 O  O     . ALA A 1 431 ? 31.669  17.112  7.763   1.00 27.58  ?  417 ALA A O     1 
ATOM   3092 C  CB    . ALA A 1 431 ? 30.093  18.866  5.446   1.00 24.57  ?  417 ALA A CB    1 
ATOM   3093 N  N     . PHE A 1 432 ? 29.812  18.137  8.519   1.00 26.22  ?  418 PHE A N     1 
ATOM   3094 C  CA    . PHE A 1 432 ? 30.271  18.125  9.903   1.00 27.23  ?  418 PHE A CA    1 
ATOM   3095 C  C     . PHE A 1 432 ? 30.521  16.696  10.380  1.00 29.97  ?  418 PHE A C     1 
ATOM   3096 O  O     . PHE A 1 432 ? 31.515  16.426  11.067  1.00 28.66  ?  418 PHE A O     1 
ATOM   3097 C  CB    . PHE A 1 432 ? 29.238  18.833  10.787  1.00 24.64  ?  418 PHE A CB    1 
ATOM   3098 C  CG    . PHE A 1 432 ? 29.519  18.727  12.258  1.00 30.00  ?  418 PHE A CG    1 
ATOM   3099 C  CD1   . PHE A 1 432 ? 30.677  19.265  12.795  1.00 25.79  ?  418 PHE A CD1   1 
ATOM   3100 C  CD2   . PHE A 1 432 ? 28.625  18.078  13.104  1.00 29.33  ?  418 PHE A CD2   1 
ATOM   3101 C  CE1   . PHE A 1 432 ? 30.943  19.168  14.147  1.00 26.32  ?  418 PHE A CE1   1 
ATOM   3102 C  CE2   . PHE A 1 432 ? 28.882  17.975  14.460  1.00 26.93  ?  418 PHE A CE2   1 
ATOM   3103 C  CZ    . PHE A 1 432 ? 30.053  18.524  14.983  1.00 26.91  ?  418 PHE A CZ    1 
ATOM   3104 N  N     . GLY A 1 433 ? 29.631  15.767  10.022  1.00 25.54  ?  419 GLY A N     1 
ATOM   3105 C  CA    . GLY A 1 433 ? 29.849  14.369  10.369  1.00 24.91  ?  419 GLY A CA    1 
ATOM   3106 C  C     . GLY A 1 433 ? 31.028  13.740  9.647   1.00 27.83  ?  419 GLY A C     1 
ATOM   3107 O  O     . GLY A 1 433 ? 31.793  12.972  10.239  1.00 26.16  ?  419 GLY A O     1 
ATOM   3108 N  N     . ALA A 1 434 ? 31.166  14.014  8.347   1.00 28.56  ?  420 ALA A N     1 
ATOM   3109 C  CA    . ALA A 1 434 ? 32.276  13.445  7.586   1.00 30.47  ?  420 ALA A CA    1 
ATOM   3110 C  C     . ALA A 1 434 ? 33.620  13.966  8.085   1.00 31.67  ?  420 ALA A C     1 
ATOM   3111 O  O     . ALA A 1 434 ? 34.580  13.198  8.220   1.00 33.78  ?  420 ALA A O     1 
ATOM   3112 C  CB    . ALA A 1 434 ? 32.106  13.744  6.097   1.00 25.86  ?  420 ALA A CB    1 
ATOM   3113 N  N     . GLN A 1 435 ? 33.711  15.272  8.355   1.00 30.84  ?  421 GLN A N     1 
ATOM   3114 C  CA    . GLN A 1 435 ? 34.952  15.835  8.883   1.00 32.91  ?  421 GLN A CA    1 
ATOM   3115 C  C     . GLN A 1 435 ? 35.274  15.260  10.257  1.00 36.24  ?  421 GLN A C     1 
ATOM   3116 O  O     . GLN A 1 435 ? 36.444  15.014  10.581  1.00 42.57  ?  421 GLN A O     1 
ATOM   3117 C  CB    . GLN A 1 435 ? 34.858  17.361  8.945   1.00 30.50  ?  421 GLN A CB    1 
ATOM   3118 C  CG    . GLN A 1 435 ? 36.163  18.059  9.332   1.00 29.05  ?  421 GLN A CG    1 
ATOM   3119 C  CD    . GLN A 1 435 ? 37.157  18.100  8.194   1.00 34.50  ?  421 GLN A CD    1 
ATOM   3120 O  OE1   . GLN A 1 435 ? 37.222  19.077  7.447   1.00 29.97  ?  421 GLN A OE1   1 
ATOM   3121 N  NE2   . GLN A 1 435 ? 37.933  17.026  8.045   1.00 29.26  ?  421 GLN A NE2   1 
ATOM   3122 N  N     . THR A 1 436 ? 34.244  15.036  11.075  1.00 30.01  ?  422 THR A N     1 
ATOM   3123 C  CA    . THR A 1 436 ? 34.426  14.361  12.356  1.00 32.36  ?  422 THR A CA    1 
ATOM   3124 C  C     . THR A 1 436 ? 34.988  12.957  12.157  1.00 36.16  ?  422 THR A C     1 
ATOM   3125 O  O     . THR A 1 436 ? 35.879  12.525  12.896  1.00 36.57  ?  422 THR A O     1 
ATOM   3126 C  CB    . THR A 1 436 ? 33.086  14.303  13.101  1.00 31.24  ?  422 THR A CB    1 
ATOM   3127 O  OG1   . THR A 1 436 ? 32.670  15.629  13.451  1.00 31.22  ?  422 THR A OG1   1 
ATOM   3128 C  CG2   . THR A 1 436 ? 33.181  13.451  14.363  1.00 27.58  ?  422 THR A CG2   1 
ATOM   3129 N  N     . ALA A 1 437 ? 34.474  12.229  11.162  1.00 30.55  ?  423 ALA A N     1 
ATOM   3130 C  CA    . ALA A 1 437 ? 34.982  10.890  10.890  1.00 38.08  ?  423 ALA A CA    1 
ATOM   3131 C  C     . ALA A 1 437 ? 36.417  10.932  10.376  1.00 39.76  ?  423 ALA A C     1 
ATOM   3132 O  O     . ALA A 1 437 ? 37.236  10.086  10.744  1.00 33.92  ?  423 ALA A O     1 
ATOM   3133 C  CB    . ALA A 1 437 ? 34.076  10.174  9.889   1.00 27.96  ?  423 ALA A CB    1 
ATOM   3134 N  N     . CYS A 1 438 ? 36.747  11.912  9.539   1.00 34.10  ?  424 CYS A N     1 
ATOM   3135 C  CA    . CYS A 1 438 ? 38.052  11.978  8.879   1.00 34.36  ?  424 CYS A CA    1 
ATOM   3136 C  C     . CYS A 1 438 ? 38.679  13.343  9.132   1.00 35.63  ?  424 CYS A C     1 
ATOM   3137 O  O     . CYS A 1 438 ? 38.731  14.197  8.240   1.00 39.77  ?  424 CYS A O     1 
ATOM   3138 C  CB    . CYS A 1 438 ? 37.910  11.701  7.383   1.00 37.28  ?  424 CYS A CB    1 
ATOM   3139 S  SG    . CYS A 1 438 ? 37.048  10.158  7.038   1.00 41.92  ?  424 CYS A SG    1 
ATOM   3140 N  N     . PRO A 1 439 ? 39.181  13.574  10.349  1.00 31.58  ?  425 PRO A N     1 
ATOM   3141 C  CA    . PRO A 1 439 ? 39.754  14.890  10.669  1.00 34.50  ?  425 PRO A CA    1 
ATOM   3142 C  C     . PRO A 1 439 ? 40.995  15.228  9.864   1.00 38.66  ?  425 PRO A C     1 
ATOM   3143 O  O     . PRO A 1 439 ? 41.363  16.404  9.792   1.00 40.06  ?  425 PRO A O     1 
ATOM   3144 C  CB    . PRO A 1 439 ? 40.075  14.777  12.165  1.00 40.63  ?  425 PRO A CB    1 
ATOM   3145 C  CG    . PRO A 1 439 ? 40.290  13.319  12.382  1.00 40.42  ?  425 PRO A CG    1 
ATOM   3146 C  CD    . PRO A 1 439 ? 39.310  12.628  11.470  1.00 33.04  ?  425 PRO A CD    1 
ATOM   3147 N  N     . ASN A 1 440 ? 41.655  14.245  9.264   1.00 38.07  ?  426 ASN A N     1 
ATOM   3148 C  CA    . ASN A 1 440 ? 42.881  14.482  8.517   1.00 44.32  ?  426 ASN A CA    1 
ATOM   3149 C  C     . ASN A 1 440 ? 42.653  14.557  7.013   1.00 43.83  ?  426 ASN A C     1 
ATOM   3150 O  O     . ASN A 1 440 ? 43.623  14.587  6.254   1.00 44.14  ?  426 ASN A O     1 
ATOM   3151 C  CB    . ASN A 1 440 ? 43.910  13.401  8.846   1.00 38.47  ?  426 ASN A CB    1 
ATOM   3152 C  CG    . ASN A 1 440 ? 44.262  13.375  10.318  1.00 53.57  ?  426 ASN A CG    1 
ATOM   3153 O  OD1   . ASN A 1 440 ? 44.534  14.416  10.919  1.00 53.65  ?  426 ASN A OD1   1 
ATOM   3154 N  ND2   . ASN A 1 440 ? 44.265  12.186  10.908  1.00 50.42  ?  426 ASN A ND2   1 
ATOM   3155 N  N     . ARG A 1 441 ? 41.403  14.585  6.563   1.00 40.61  ?  427 ARG A N     1 
ATOM   3156 C  CA    . ARG A 1 441 ? 41.097  14.682  5.146   1.00 43.81  ?  427 ARG A CA    1 
ATOM   3157 C  C     . ARG A 1 441 ? 40.466  16.035  4.839   1.00 35.57  ?  427 ARG A C     1 
ATOM   3158 O  O     . ARG A 1 441 ? 39.853  16.665  5.705   1.00 31.76  ?  427 ARG A O     1 
ATOM   3159 C  CB    . ARG A 1 441 ? 40.175  13.538  4.700   1.00 35.30  ?  427 ARG A CB    1 
ATOM   3160 C  CG    . ARG A 1 441 ? 40.881  12.177  4.644   1.00 38.29  ?  427 ARG A CG    1 
ATOM   3161 C  CD    . ARG A 1 441 ? 39.954  11.070  4.147   1.00 46.65  ?  427 ARG A CD    1 
ATOM   3162 N  NE    . ARG A 1 441 ? 39.645  11.209  2.729   1.00 47.06  ?  427 ARG A NE    1 
ATOM   3163 C  CZ    . ARG A 1 441 ? 39.030  10.289  1.999   1.00 50.43  ?  427 ARG A CZ    1 
ATOM   3164 N  NH1   . ARG A 1 441 ? 38.649  9.133   2.521   1.00 41.64  ?  427 ARG A NH1   1 
ATOM   3165 N  NH2   . ARG A 1 441 ? 38.790  10.535  0.714   1.00 45.59  ?  427 ARG A NH2   1 
ATOM   3166 N  N     . ARG A 1 442 ? 40.664  16.498  3.607   1.00 31.89  ?  428 ARG A N     1 
ATOM   3167 C  CA    . ARG A 1 442 ? 40.109  17.775  3.180   1.00 42.94  ?  428 ARG A CA    1 
ATOM   3168 C  C     . ARG A 1 442 ? 38.660  17.599  2.742   1.00 38.64  ?  428 ARG A C     1 
ATOM   3169 O  O     . ARG A 1 442 ? 38.355  16.757  1.891   1.00 31.73  ?  428 ARG A O     1 
ATOM   3170 C  CB    . ARG A 1 442 ? 40.939  18.369  2.042   1.00 39.57  ?  428 ARG A CB    1 
ATOM   3171 C  CG    . ARG A 1 442 ? 40.559  19.799  1.694   1.00 33.06  ?  428 ARG A CG    1 
ATOM   3172 C  CD    . ARG A 1 442 ? 41.504  20.376  0.665   1.00 41.23  ?  428 ARG A CD    1 
ATOM   3173 N  NE    . ARG A 1 442 ? 41.282  19.818  -0.663  1.00 35.83  ?  428 ARG A NE    1 
ATOM   3174 C  CZ    . ARG A 1 442 ? 41.803  20.318  -1.775  1.00 41.33  ?  428 ARG A CZ    1 
ATOM   3175 N  NH1   . ARG A 1 442 ? 42.587  21.385  -1.754  1.00 45.28  ?  428 ARG A NH1   1 
ATOM   3176 N  NH2   . ARG A 1 442 ? 41.529  19.734  -2.939  1.00 34.92  ?  428 ARG A NH2   1 
ATOM   3177 N  N     . VAL A 1 443 ? 37.774  18.420  3.295   1.00 30.55  ?  429 VAL A N     1 
ATOM   3178 C  CA    . VAL A 1 443 ? 36.340  18.298  3.064   1.00 30.42  ?  429 VAL A CA    1 
ATOM   3179 C  C     . VAL A 1 443 ? 35.879  19.527  2.297   1.00 34.16  ?  429 VAL A C     1 
ATOM   3180 O  O     . VAL A 1 443 ? 36.111  20.666  2.727   1.00 31.30  ?  429 VAL A O     1 
ATOM   3181 C  CB    . VAL A 1 443 ? 35.567  18.132  4.380   1.00 35.63  ?  429 VAL A CB    1 
ATOM   3182 C  CG1   . VAL A 1 443 ? 34.065  18.161  4.131   1.00 34.17  ?  429 VAL A CG1   1 
ATOM   3183 C  CG2   . VAL A 1 443 ? 35.965  16.828  5.058   1.00 29.53  ?  429 VAL A CG2   1 
ATOM   3184 N  N     . ILE A 1 444 ? 35.256  19.294  1.145   1.00 30.44  ?  430 ILE A N     1 
ATOM   3185 C  CA    . ILE A 1 444 ? 34.736  20.349  0.285   1.00 29.56  ?  430 ILE A CA    1 
ATOM   3186 C  C     . ILE A 1 444 ? 33.220  20.233  0.280   1.00 36.22  ?  430 ILE A C     1 
ATOM   3187 O  O     . ILE A 1 444 ? 32.669  19.175  -0.059  1.00 30.32  ?  430 ILE A O     1 
ATOM   3188 C  CB    . ILE A 1 444 ? 35.307  20.257  -1.138  1.00 31.41  ?  430 ILE A CB    1 
ATOM   3189 C  CG1   . ILE A 1 444 ? 36.824  20.480  -1.118  1.00 31.21  ?  430 ILE A CG1   1 
ATOM   3190 C  CG2   . ILE A 1 444 ? 34.630  21.267  -2.051  1.00 31.18  ?  430 ILE A CG2   1 
ATOM   3191 C  CD1   . ILE A 1 444 ? 37.577  19.657  -2.134  1.00 31.12  ?  430 ILE A CD1   1 
ATOM   3192 N  N     . VAL A 1 445 ? 32.548  21.313  0.665   1.00 27.54  ?  431 VAL A N     1 
ATOM   3193 C  CA    . VAL A 1 445 ? 31.097  21.339  0.811   1.00 26.52  ?  431 VAL A CA    1 
ATOM   3194 C  C     . VAL A 1 445 ? 30.530  22.210  -0.299  1.00 31.56  ?  431 VAL A C     1 
ATOM   3195 O  O     . VAL A 1 445 ? 30.824  23.410  -0.368  1.00 34.06  ?  431 VAL A O     1 
ATOM   3196 C  CB    . VAL A 1 445 ? 30.678  21.868  2.190   1.00 32.02  ?  431 VAL A CB    1 
ATOM   3197 C  CG1   . VAL A 1 445 ? 29.216  21.584  2.445   1.00 31.71  ?  431 VAL A CG1   1 
ATOM   3198 C  CG2   . VAL A 1 445 ? 31.548  21.269  3.284   1.00 25.76  ?  431 VAL A CG2   1 
ATOM   3199 N  N     . LEU A 1 446 ? 29.720  21.612  -1.162  1.00 28.38  ?  432 LEU A N     1 
ATOM   3200 C  CA    . LEU A 1 446 ? 29.028  22.325  -2.233  1.00 31.32  ?  432 LEU A CA    1 
ATOM   3201 C  C     . LEU A 1 446 ? 27.553  22.379  -1.862  1.00 36.49  ?  432 LEU A C     1 
ATOM   3202 O  O     . LEU A 1 446 ? 26.842  21.379  -1.985  1.00 31.33  ?  432 LEU A O     1 
ATOM   3203 C  CB    . LEU A 1 446 ? 29.237  21.634  -3.575  1.00 28.27  ?  432 LEU A CB    1 
ATOM   3204 C  CG    . LEU A 1 446 ? 30.692  21.548  -4.030  1.00 38.72  ?  432 LEU A CG    1 
ATOM   3205 C  CD1   . LEU A 1 446 ? 30.859  20.572  -5.182  1.00 28.29  ?  432 LEU A CD1   1 
ATOM   3206 C  CD2   . LEU A 1 446 ? 31.183  22.932  -4.418  1.00 33.67  ?  432 LEU A CD2   1 
ATOM   3207 N  N     . THR A 1 447 ? 27.094  23.543  -1.394  1.00 37.00  ?  433 THR A N     1 
ATOM   3208 C  CA    . THR A 1 447 ? 25.706  23.720  -0.986  1.00 26.46  ?  433 THR A CA    1 
ATOM   3209 C  C     . THR A 1 447 ? 25.132  24.981  -1.611  1.00 35.88  ?  433 THR A C     1 
ATOM   3210 O  O     . THR A 1 447 ? 25.828  25.990  -1.760  1.00 30.90  ?  433 THR A O     1 
ATOM   3211 C  CB    . THR A 1 447 ? 25.555  23.793  0.546   1.00 26.64  ?  433 THR A CB    1 
ATOM   3212 O  OG1   . THR A 1 447 ? 24.166  23.872  0.883   1.00 26.51  ?  433 THR A OG1   1 
ATOM   3213 C  CG2   . THR A 1 447 ? 26.278  25.016  1.121   1.00 24.60  ?  433 THR A CG2   1 
ATOM   3214 N  N     . GLY A 1 448 ? 23.860  24.911  -1.991  1.00 32.35  ?  434 GLY A N     1 
ATOM   3215 C  CA    . GLY A 1 448 ? 23.165  26.099  -2.423  1.00 29.72  ?  434 GLY A CA    1 
ATOM   3216 C  C     . GLY A 1 448 ? 22.852  27.017  -1.259  1.00 32.90  ?  434 GLY A C     1 
ATOM   3217 O  O     . GLY A 1 448 ? 22.952  26.640  -0.086  1.00 24.37  ?  434 GLY A O     1 
ATOM   3218 N  N     . ASP A 1 449 ? 22.497  28.264  -1.593  1.00 26.17  ?  435 ASP A N     1 
ATOM   3219 C  CA    . ASP A 1 449 ? 22.074  29.198  -0.553  1.00 25.46  ?  435 ASP A CA    1 
ATOM   3220 C  C     . ASP A 1 449 ? 20.766  28.745  0.091   1.00 24.80  ?  435 ASP A C     1 
ATOM   3221 O  O     . ASP A 1 449 ? 20.600  28.840  1.313   1.00 26.42  ?  435 ASP A O     1 
ATOM   3222 C  CB    . ASP A 1 449 ? 21.946  30.617  -1.121  1.00 26.29  ?  435 ASP A CB    1 
ATOM   3223 C  CG    . ASP A 1 449 ? 21.143  30.673  -2.411  1.00 30.00  ?  435 ASP A CG    1 
ATOM   3224 O  OD1   . ASP A 1 449 ? 20.730  29.609  -2.927  1.00 27.44  ?  435 ASP A OD1   1 
ATOM   3225 O  OD2   . ASP A 1 449 ? 20.920  31.793  -2.916  1.00 32.37  ?  435 ASP A OD2   1 
ATOM   3226 N  N     . GLY A 1 450 ? 19.826  28.239  -0.708  1.00 26.28  ?  436 GLY A N     1 
ATOM   3227 C  CA    . GLY A 1 450 ? 18.597  27.712  -0.131  1.00 26.47  ?  436 GLY A CA    1 
ATOM   3228 C  C     . GLY A 1 450 ? 18.846  26.545  0.808   1.00 25.68  ?  436 GLY A C     1 
ATOM   3229 O  O     . GLY A 1 450 ? 18.333  26.514  1.930   1.00 26.38  ?  436 GLY A O     1 
ATOM   3230 N  N     . ALA A 1 451 ? 19.668  25.583  0.374   1.00 24.48  ?  437 ALA A N     1 
ATOM   3231 C  CA    . ALA A 1 451 ? 19.905  24.383  1.176   1.00 22.74  ?  437 ALA A CA    1 
ATOM   3232 C  C     . ALA A 1 451 ? 20.585  24.707  2.503   1.00 24.26  ?  437 ALA A C     1 
ATOM   3233 O  O     . ALA A 1 451 ? 20.219  24.153  3.546   1.00 24.02  ?  437 ALA A O     1 
ATOM   3234 C  CB    . ALA A 1 451 ? 20.740  23.380  0.381   1.00 22.72  ?  437 ALA A CB    1 
ATOM   3235 N  N     . ALA A 1 452 ? 21.580  25.599  2.488   1.00 23.31  ?  438 ALA A N     1 
ATOM   3236 C  CA    . ALA A 1 452 ? 22.339  25.881  3.705   1.00 25.73  ?  438 ALA A CA    1 
ATOM   3237 C  C     . ALA A 1 452 ? 21.478  26.520  4.794   1.00 25.66  ?  438 ALA A C     1 
ATOM   3238 O  O     . ALA A 1 452 ? 21.783  26.379  5.984   1.00 27.85  ?  438 ALA A O     1 
ATOM   3239 C  CB    . ALA A 1 452 ? 23.541  26.771  3.380   1.00 24.17  ?  438 ALA A CB    1 
ATOM   3240 N  N     . GLN A 1 453 ? 20.410  27.232  4.414   1.00 25.54  ?  439 GLN A N     1 
ATOM   3241 C  CA    . GLN A 1 453 ? 19.545  27.852  5.415   1.00 24.18  ?  439 GLN A CA    1 
ATOM   3242 C  C     . GLN A 1 453 ? 18.898  26.816  6.323   1.00 27.85  ?  439 GLN A C     1 
ATOM   3243 O  O     . GLN A 1 453 ? 18.666  27.085  7.507   1.00 25.65  ?  439 GLN A O     1 
ATOM   3244 C  CB    . GLN A 1 453 ? 18.458  28.689  4.735   1.00 26.21  ?  439 GLN A CB    1 
ATOM   3245 C  CG    . GLN A 1 453 ? 18.987  29.859  3.938   1.00 26.43  ?  439 GLN A CG    1 
ATOM   3246 C  CD    . GLN A 1 453 ? 17.888  30.812  3.503   1.00 31.41  ?  439 GLN A CD    1 
ATOM   3247 O  OE1   . GLN A 1 453 ? 16.732  30.416  3.322   1.00 30.88  ?  439 GLN A OE1   1 
ATOM   3248 N  NE2   . GLN A 1 453 ? 18.250  32.072  3.311   1.00 26.22  ?  439 GLN A NE2   1 
ATOM   3249 N  N     . LEU A 1 454 ? 18.625  25.621  5.799   1.00 23.99  ?  440 LEU A N     1 
ATOM   3250 C  CA    . LEU A 1 454 ? 17.874  24.638  6.571   1.00 29.34  ?  440 LEU A CA    1 
ATOM   3251 C  C     . LEU A 1 454 ? 18.679  24.092  7.744   1.00 30.28  ?  440 LEU A C     1 
ATOM   3252 O  O     . LEU A 1 454 ? 18.091  23.689  8.756   1.00 26.62  ?  440 LEU A O     1 
ATOM   3253 C  CB    . LEU A 1 454 ? 17.414  23.501  5.657   1.00 23.90  ?  440 LEU A CB    1 
ATOM   3254 C  CG    . LEU A 1 454 ? 16.118  23.776  4.881   1.00 29.65  ?  440 LEU A CG    1 
ATOM   3255 C  CD1   . LEU A 1 454 ? 16.375  24.644  3.661   1.00 22.42  ?  440 LEU A CD1   1 
ATOM   3256 C  CD2   . LEU A 1 454 ? 15.442  22.468  4.476   1.00 26.21  ?  440 LEU A CD2   1 
ATOM   3257 N  N     . THR A 1 455 ? 20.015  24.084  7.646   1.00 26.17  ?  441 THR A N     1 
ATOM   3258 C  CA    . THR A 1 455 ? 20.851  23.450  8.661   1.00 24.12  ?  441 THR A CA    1 
ATOM   3259 C  C     . THR A 1 455 ? 22.021  24.335  9.080   1.00 34.63  ?  441 THR A C     1 
ATOM   3260 O  O     . THR A 1 455 ? 23.047  23.828  9.545   1.00 30.84  ?  441 THR A O     1 
ATOM   3261 C  CB    . THR A 1 455 ? 21.371  22.098  8.166   1.00 25.91  ?  441 THR A CB    1 
ATOM   3262 O  OG1   . THR A 1 455 ? 22.066  22.282  6.929   1.00 25.11  ?  441 THR A OG1   1 
ATOM   3263 C  CG2   . THR A 1 455 ? 20.227  21.116  7.947   1.00 24.17  ?  441 THR A CG2   1 
ATOM   3264 N  N     . ILE A 1 456 ? 21.867  25.660  8.969   1.00 30.28  ?  442 ILE A N     1 
ATOM   3265 C  CA    . ILE A 1 456 ? 23.004  26.565  9.117   1.00 28.16  ?  442 ILE A CA    1 
ATOM   3266 C  C     . ILE A 1 456 ? 23.643  26.462  10.497  1.00 30.03  ?  442 ILE A C     1 
ATOM   3267 O  O     . ILE A 1 456 ? 24.844  26.719  10.650  1.00 28.94  ?  442 ILE A O     1 
ATOM   3268 C  CB    . ILE A 1 456 ? 22.575  28.017  8.811   1.00 27.99  ?  442 ILE A CB    1 
ATOM   3269 C  CG1   . ILE A 1 456 ? 23.801  28.932  8.722   1.00 31.98  ?  442 ILE A CG1   1 
ATOM   3270 C  CG2   . ILE A 1 456 ? 21.623  28.533  9.872   1.00 25.36  ?  442 ILE A CG2   1 
ATOM   3271 C  CD1   . ILE A 1 456 ? 24.761  28.563  7.625   1.00 28.30  ?  442 ILE A CD1   1 
ATOM   3272 N  N     . GLN A 1 457 ? 22.875  26.081  11.522  1.00 25.78  ?  443 GLN A N     1 
ATOM   3273 C  CA    . GLN A 1 457 ? 23.428  26.112  12.872  1.00 25.42  ?  443 GLN A CA    1 
ATOM   3274 C  C     . GLN A 1 457 ? 24.555  25.094  13.064  1.00 29.52  ?  443 GLN A C     1 
ATOM   3275 O  O     . GLN A 1 457 ? 25.364  25.250  13.986  1.00 25.92  ?  443 GLN A O     1 
ATOM   3276 C  CB    . GLN A 1 457 ? 22.318  25.901  13.910  1.00 25.57  ?  443 GLN A CB    1 
ATOM   3277 C  CG    . GLN A 1 457 ? 21.421  24.685  13.662  1.00 26.54  ?  443 GLN A CG    1 
ATOM   3278 C  CD    . GLN A 1 457 ? 20.210  25.017  12.824  1.00 28.96  ?  443 GLN A CD    1 
ATOM   3279 O  OE1   . GLN A 1 457 ? 20.183  24.728  11.629  1.00 32.94  ?  443 GLN A OE1   1 
ATOM   3280 N  NE2   . GLN A 1 457 ? 19.202  25.637  13.439  1.00 24.98  ?  443 GLN A NE2   1 
ATOM   3281 N  N     . GLU A 1 458 ? 24.655  24.079  12.203  1.00 26.64  ?  444 GLU A N     1 
ATOM   3282 C  CA    . GLU A 1 458 ? 25.737  23.114  12.372  1.00 34.30  ?  444 GLU A CA    1 
ATOM   3283 C  C     . GLU A 1 458 ? 27.086  23.688  11.973  1.00 31.64  ?  444 GLU A C     1 
ATOM   3284 O  O     . GLU A 1 458 ? 28.117  23.139  12.372  1.00 34.05  ?  444 GLU A O     1 
ATOM   3285 C  CB    . GLU A 1 458 ? 25.460  21.834  11.584  1.00 32.37  ?  444 GLU A CB    1 
ATOM   3286 C  CG    . GLU A 1 458 ? 25.644  20.584  12.431  1.00 33.62  ?  444 GLU A CG    1 
ATOM   3287 C  CD    . GLU A 1 458 ? 24.963  20.703  13.790  1.00 34.64  ?  444 GLU A CD    1 
ATOM   3288 O  OE1   . GLU A 1 458 ? 23.835  21.240  13.857  1.00 27.11  ?  444 GLU A OE1   1 
ATOM   3289 O  OE2   . GLU A 1 458 ? 25.552  20.259  14.796  1.00 42.53  ?  444 GLU A OE2   1 
ATOM   3290 N  N     . LEU A 1 459 ? 27.101  24.787  11.218  1.00 28.25  ?  445 LEU A N     1 
ATOM   3291 C  CA    . LEU A 1 459 ? 28.344  25.519  11.010  1.00 27.64  ?  445 LEU A CA    1 
ATOM   3292 C  C     . LEU A 1 459 ? 28.943  25.949  12.343  1.00 29.39  ?  445 LEU A C     1 
ATOM   3293 O  O     . LEU A 1 459 ? 30.170  25.955  12.511  1.00 28.90  ?  445 LEU A O     1 
ATOM   3294 C  CB    . LEU A 1 459 ? 28.088  26.724  10.108  1.00 30.35  ?  445 LEU A CB    1 
ATOM   3295 C  CG    . LEU A 1 459 ? 29.211  27.740  9.882   1.00 47.97  ?  445 LEU A CG    1 
ATOM   3296 C  CD1   . LEU A 1 459 ? 30.482  27.061  9.391   1.00 27.19  ?  445 LEU A CD1   1 
ATOM   3297 C  CD2   . LEU A 1 459 ? 28.746  28.810  8.902   1.00 32.22  ?  445 LEU A CD2   1 
ATOM   3298 N  N     . GLY A 1 460 ? 28.090  26.295  13.309  1.00 27.40  ?  446 GLY A N     1 
ATOM   3299 C  CA    . GLY A 1 460 ? 28.577  26.575  14.650  1.00 27.74  ?  446 GLY A CA    1 
ATOM   3300 C  C     . GLY A 1 460 ? 29.266  25.380  15.283  1.00 32.51  ?  446 GLY A C     1 
ATOM   3301 O  O     . GLY A 1 460 ? 30.279  25.531  15.974  1.00 34.71  ?  446 GLY A O     1 
ATOM   3302 N  N     . SER A 1 461 ? 28.721  24.177  15.064  1.00 31.20  ?  447 SER A N     1 
ATOM   3303 C  CA    . SER A 1 461 ? 29.383  22.963  15.538  1.00 27.02  ?  447 SER A CA    1 
ATOM   3304 C  C     . SER A 1 461 ? 30.736  22.783  14.862  1.00 28.81  ?  447 SER A C     1 
ATOM   3305 O  O     . SER A 1 461 ? 31.715  22.379  15.501  1.00 28.06  ?  447 SER A O     1 
ATOM   3306 C  CB    . SER A 1 461 ? 28.494  21.741  15.286  1.00 29.74  ?  447 SER A CB    1 
ATOM   3307 O  OG    . SER A 1 461 ? 27.218  21.915  15.873  1.00 38.30  ?  447 SER A OG    1 
ATOM   3308 N  N     . MET A 1 462 ? 30.794  23.053  13.557  1.00 29.32  ?  448 MET A N     1 
ATOM   3309 C  CA    . MET A 1 462 ? 32.054  23.031  12.824  1.00 27.22  ?  448 MET A CA    1 
ATOM   3310 C  C     . MET A 1 462 ? 33.077  23.948  13.483  1.00 30.82  ?  448 MET A C     1 
ATOM   3311 O  O     . MET A 1 462 ? 34.210  23.541  13.768  1.00 29.91  ?  448 MET A O     1 
ATOM   3312 C  CB    . MET A 1 462 ? 31.796  23.471  11.384  1.00 29.21  ?  448 MET A CB    1 
ATOM   3313 C  CG    . MET A 1 462 ? 31.119  22.433  10.513  1.00 26.03  ?  448 MET A CG    1 
ATOM   3314 S  SD    . MET A 1 462 ? 30.940  23.057  8.835   1.00 28.74  ?  448 MET A SD    1 
ATOM   3315 C  CE    . MET A 1 462 ? 30.043  21.715  8.064   1.00 28.17  ?  448 MET A CE    1 
ATOM   3316 N  N     . LEU A 1 463 ? 32.672  25.187  13.771  1.00 31.50  ?  449 LEU A N     1 
ATOM   3317 C  CA    . LEU A 1 463 ? 33.593  26.159  14.355  1.00 32.45  ?  449 LEU A CA    1 
ATOM   3318 C  C     . LEU A 1 463 ? 33.990  25.765  15.772  1.00 35.18  ?  449 LEU A C     1 
ATOM   3319 O  O     . LEU A 1 463 ? 35.155  25.918  16.160  1.00 36.52  ?  449 LEU A O     1 
ATOM   3320 C  CB    . LEU A 1 463 ? 32.959  27.550  14.337  1.00 30.00  ?  449 LEU A CB    1 
ATOM   3321 C  CG    . LEU A 1 463 ? 32.659  28.111  12.944  1.00 34.33  ?  449 LEU A CG    1 
ATOM   3322 C  CD1   . LEU A 1 463 ? 31.686  29.286  13.012  1.00 33.93  ?  449 LEU A CD1   1 
ATOM   3323 C  CD2   . LEU A 1 463 ? 33.956  28.525  12.261  1.00 40.59  ?  449 LEU A CD2   1 
ATOM   3324 N  N     . ARG A 1 464 ? 33.042  25.237  16.550  1.00 31.81  ?  450 ARG A N     1 
ATOM   3325 C  CA    . ARG A 1 464 ? 33.352  24.828  17.915  1.00 37.91  ?  450 ARG A CA    1 
ATOM   3326 C  C     . ARG A 1 464 ? 34.432  23.754  17.937  1.00 39.53  ?  450 ARG A C     1 
ATOM   3327 O  O     . ARG A 1 464 ? 35.326  23.778  18.791  1.00 35.55  ?  450 ARG A O     1 
ATOM   3328 C  CB    . ARG A 1 464 ? 32.086  24.329  18.614  1.00 34.65  ?  450 ARG A CB    1 
ATOM   3329 C  CG    . ARG A 1 464 ? 32.301  23.908  20.062  1.00 38.44  ?  450 ARG A CG    1 
ATOM   3330 C  CD    . ARG A 1 464 ? 31.194  22.978  20.531  1.00 37.45  ?  450 ARG A CD    1 
ATOM   3331 N  NE    . ARG A 1 464 ? 31.081  21.813  19.665  1.00 33.98  ?  450 ARG A NE    1 
ATOM   3332 C  CZ    . ARG A 1 464 ? 30.021  21.019  19.610  1.00 39.10  ?  450 ARG A CZ    1 
ATOM   3333 N  NH1   . ARG A 1 464 ? 28.960  21.230  20.373  1.00 38.74  ?  450 ARG A NH1   1 
ATOM   3334 N  NH2   . ARG A 1 464 ? 30.026  19.987  18.767  1.00 36.40  ?  450 ARG A NH2   1 
ATOM   3335 N  N     . ASP A 1 465 ? 34.382  22.822  16.991  1.00 31.67  ?  451 ASP A N     1 
ATOM   3336 C  CA    . ASP A 1 465 ? 35.315  21.708  16.935  1.00 35.91  ?  451 ASP A CA    1 
ATOM   3337 C  C     . ASP A 1 465 ? 36.545  22.006  16.081  1.00 35.65  ?  451 ASP A C     1 
ATOM   3338 O  O     . ASP A 1 465 ? 37.335  21.094  15.819  1.00 38.54  ?  451 ASP A O     1 
ATOM   3339 C  CB    . ASP A 1 465 ? 34.594  20.457  16.428  1.00 30.11  ?  451 ASP A CB    1 
ATOM   3340 C  CG    . ASP A 1 465 ? 33.534  19.962  17.400  1.00 36.51  ?  451 ASP A CG    1 
ATOM   3341 O  OD1   . ASP A 1 465 ? 33.535  20.415  18.566  1.00 34.11  ?  451 ASP A OD1   1 
ATOM   3342 O  OD2   . ASP A 1 465 ? 32.701  19.119  17.005  1.00 32.28  ?  451 ASP A OD2   1 
ATOM   3343 N  N     . LYS A 1 466 ? 36.712  23.254  15.638  1.00 37.82  ?  452 LYS A N     1 
ATOM   3344 C  CA    . LYS A 1 466 ? 37.910  23.706  14.923  1.00 43.16  ?  452 LYS A CA    1 
ATOM   3345 C  C     . LYS A 1 466 ? 38.130  22.928  13.628  1.00 38.83  ?  452 LYS A C     1 
ATOM   3346 O  O     . LYS A 1 466 ? 39.265  22.674  13.222  1.00 39.83  ?  452 LYS A O     1 
ATOM   3347 C  CB    . LYS A 1 466 ? 39.152  23.631  15.816  1.00 41.84  ?  452 LYS A CB    1 
ATOM   3348 C  CG    . LYS A 1 466 ? 38.948  24.197  17.211  1.00 46.55  ?  452 LYS A CG    1 
ATOM   3349 C  CD    . LYS A 1 466 ? 38.863  25.710  17.182  1.00 48.42  ?  452 LYS A CD    1 
ATOM   3350 C  CE    . LYS A 1 466 ? 39.212  26.299  18.536  1.00 60.05  ?  452 LYS A CE    1 
ATOM   3351 N  NZ    . LYS A 1 466 ? 40.277  25.511  19.209  1.00 57.15  ?  452 LYS A NZ    1 
ATOM   3352 N  N     . GLN A 1 467 ? 37.038  22.564  12.963  1.00 34.22  ?  453 GLN A N     1 
ATOM   3353 C  CA    . GLN A 1 467 ? 37.144  21.928  11.661  1.00 30.22  ?  453 GLN A CA    1 
ATOM   3354 C  C     . GLN A 1 467 ? 37.518  22.954  10.597  1.00 35.29  ?  453 GLN A C     1 
ATOM   3355 O  O     . GLN A 1 467 ? 37.246  24.151  10.728  1.00 35.92  ?  453 GLN A O     1 
ATOM   3356 C  CB    . GLN A 1 467 ? 35.830  21.249  11.288  1.00 33.17  ?  453 GLN A CB    1 
ATOM   3357 C  CG    . GLN A 1 467 ? 35.374  20.184  12.271  1.00 35.56  ?  453 GLN A CG    1 
ATOM   3358 C  CD    . GLN A 1 467 ? 34.143  19.463  11.778  1.00 32.15  ?  453 GLN A CD    1 
ATOM   3359 O  OE1   . GLN A 1 467 ? 33.418  19.978  10.925  1.00 30.09  ?  453 GLN A OE1   1 
ATOM   3360 N  NE2   . GLN A 1 467 ? 33.901  18.264  12.298  1.00 27.20  ?  453 GLN A NE2   1 
ATOM   3361 N  N     . HIS A 1 468 ? 38.129  22.470  9.515   1.00 31.21  ?  454 HIS A N     1 
ATOM   3362 C  CA    . HIS A 1 468 ? 38.561  23.333  8.415   1.00 31.88  ?  454 HIS A CA    1 
ATOM   3363 C  C     . HIS A 1 468 ? 38.033  22.835  7.071   1.00 37.67  ?  454 HIS A C     1 
ATOM   3364 O  O     . HIS A 1 468 ? 38.810  22.578  6.146   1.00 33.31  ?  454 HIS A O     1 
ATOM   3365 C  CB    . HIS A 1 468 ? 40.086  23.432  8.382   1.00 40.43  ?  454 HIS A CB    1 
ATOM   3366 C  CG    . HIS A 1 468 ? 40.707  23.810  9.693   1.00 49.28  ?  454 HIS A CG    1 
ATOM   3367 N  ND1   . HIS A 1 468 ? 41.939  23.339  10.092  1.00 53.24  ?  454 HIS A ND1   1 
ATOM   3368 C  CD2   . HIS A 1 468 ? 40.274  24.618  10.690  1.00 46.76  ?  454 HIS A CD2   1 
ATOM   3369 C  CE1   . HIS A 1 468 ? 42.238  23.838  11.278  1.00 41.65  ?  454 HIS A CE1   1 
ATOM   3370 N  NE2   . HIS A 1 468 ? 41.245  24.619  11.663  1.00 45.50  ?  454 HIS A NE2   1 
ATOM   3371 N  N     . PRO A 1 469 ? 36.711  22.752  6.902   1.00 33.03  ?  455 PRO A N     1 
ATOM   3372 C  CA    . PRO A 1 469 ? 36.162  22.436  5.582   1.00 28.63  ?  455 PRO A CA    1 
ATOM   3373 C  C     . PRO A 1 469 ? 36.229  23.644  4.660   1.00 33.01  ?  455 PRO A C     1 
ATOM   3374 O  O     . PRO A 1 469 ? 36.438  24.781  5.085   1.00 37.24  ?  455 PRO A O     1 
ATOM   3375 C  CB    . PRO A 1 469 ? 34.710  22.055  5.884   1.00 28.44  ?  455 PRO A CB    1 
ATOM   3376 C  CG    . PRO A 1 469 ? 34.363  22.864  7.060   1.00 27.54  ?  455 PRO A CG    1 
ATOM   3377 C  CD    . PRO A 1 469 ? 35.633  22.985  7.882   1.00 29.25  ?  455 PRO A CD    1 
ATOM   3378 N  N     . ILE A 1 470 ? 36.091  23.371  3.371   1.00 34.59  ?  456 ILE A N     1 
ATOM   3379 C  CA    . ILE A 1 470 ? 35.980  24.411  2.358   1.00 32.84  ?  456 ILE A CA    1 
ATOM   3380 C  C     . ILE A 1 470 ? 34.517  24.443  1.926   1.00 41.01  ?  456 ILE A C     1 
ATOM   3381 O  O     . ILE A 1 470 ? 34.040  23.539  1.229   1.00 32.40  ?  456 ILE A O     1 
ATOM   3382 C  CB    . ILE A 1 470 ? 36.926  24.170  1.179   1.00 33.63  ?  456 ILE A CB    1 
ATOM   3383 C  CG1   . ILE A 1 470 ? 38.380  24.248  1.657   1.00 36.78  ?  456 ILE A CG1   1 
ATOM   3384 C  CG2   . ILE A 1 470 ? 36.664  25.193  0.075   1.00 30.72  ?  456 ILE A CG2   1 
ATOM   3385 C  CD1   . ILE A 1 470 ? 39.331  23.309  0.941   1.00 42.08  ?  456 ILE A CD1   1 
ATOM   3386 N  N     . ILE A 1 471 ? 33.786  25.465  2.370   1.00 30.70  ?  457 ILE A N     1 
ATOM   3387 C  CA    . ILE A 1 471 ? 32.349  25.574  2.134   1.00 27.52  ?  457 ILE A CA    1 
ATOM   3388 C  C     . ILE A 1 471 ? 32.114  26.561  1.001   1.00 27.97  ?  457 ILE A C     1 
ATOM   3389 O  O     . ILE A 1 471 ? 32.418  27.752  1.132   1.00 36.93  ?  457 ILE A O     1 
ATOM   3390 C  CB    . ILE A 1 471 ? 31.598  26.006  3.402   1.00 27.09  ?  457 ILE A CB    1 
ATOM   3391 C  CG1   . ILE A 1 471 ? 31.857  25.015  4.537   1.00 28.89  ?  457 ILE A CG1   1 
ATOM   3392 C  CG2   . ILE A 1 471 ? 30.095  26.111  3.122   1.00 26.38  ?  457 ILE A CG2   1 
ATOM   3393 C  CD1   . ILE A 1 471 ? 31.451  25.528  5.897   1.00 32.27  ?  457 ILE A CD1   1 
ATOM   3394 N  N     . LEU A 1 472 ? 31.566  26.074  -0.109  1.00 29.10  ?  458 LEU A N     1 
ATOM   3395 C  CA    . LEU A 1 472 ? 31.208  26.917  -1.245  1.00 33.91  ?  458 LEU A CA    1 
ATOM   3396 C  C     . LEU A 1 472 ? 29.692  27.059  -1.271  1.00 39.57  ?  458 LEU A C     1 
ATOM   3397 O  O     . LEU A 1 472 ? 28.970  26.079  -1.496  1.00 27.15  ?  458 LEU A O     1 
ATOM   3398 C  CB    . LEU A 1 472 ? 31.734  26.334  -2.552  1.00 28.68  ?  458 LEU A CB    1 
ATOM   3399 C  CG    . LEU A 1 472 ? 33.261  26.280  -2.628  1.00 29.64  ?  458 LEU A CG    1 
ATOM   3400 C  CD1   . LEU A 1 472 ? 33.731  24.842  -2.730  1.00 38.50  ?  458 LEU A CD1   1 
ATOM   3401 C  CD2   . LEU A 1 472 ? 33.780  27.106  -3.797  1.00 30.77  ?  458 LEU A CD2   1 
ATOM   3402 N  N     . VAL A 1 473 ? 29.209  28.274  -1.041  1.00 30.06  ?  459 VAL A N     1 
ATOM   3403 C  CA    . VAL A 1 473 ? 27.782  28.558  -1.065  1.00 27.14  ?  459 VAL A CA    1 
ATOM   3404 C  C     . VAL A 1 473 ? 27.446  29.151  -2.423  1.00 32.39  ?  459 VAL A C     1 
ATOM   3405 O  O     . VAL A 1 473 ? 27.909  30.247  -2.766  1.00 30.99  ?  459 VAL A O     1 
ATOM   3406 C  CB    . VAL A 1 473 ? 27.376  29.509  0.069   1.00 31.67  ?  459 VAL A CB    1 
ATOM   3407 C  CG1   . VAL A 1 473 ? 25.897  29.833  -0.025  1.00 28.16  ?  459 VAL A CG1   1 
ATOM   3408 C  CG2   . VAL A 1 473 ? 27.704  28.881  1.413   1.00 28.23  ?  459 VAL A CG2   1 
ATOM   3409 N  N     . LEU A 1 474 ? 26.635  28.433  -3.191  1.00 27.23  ?  460 LEU A N     1 
ATOM   3410 C  CA    . LEU A 1 474 ? 26.215  28.883  -4.516  1.00 33.33  ?  460 LEU A CA    1 
ATOM   3411 C  C     . LEU A 1 474 ? 25.075  29.872  -4.320  1.00 34.07  ?  460 LEU A C     1 
ATOM   3412 O  O     . LEU A 1 474 ? 23.903  29.500  -4.217  1.00 33.48  ?  460 LEU A O     1 
ATOM   3413 C  CB    . LEU A 1 474 ? 25.796  27.702  -5.386  1.00 37.94  ?  460 LEU A CB    1 
ATOM   3414 C  CG    . LEU A 1 474 ? 26.882  26.766  -5.936  1.00 44.69  ?  460 LEU A CG    1 
ATOM   3415 C  CD1   . LEU A 1 474 ? 27.581  25.978  -4.838  1.00 44.36  ?  460 LEU A CD1   1 
ATOM   3416 C  CD2   . LEU A 1 474 ? 26.278  25.815  -6.962  1.00 33.75  ?  460 LEU A CD2   1 
ATOM   3417 N  N     . ASN A 1 475 ? 25.428  31.155  -4.273  1.00 29.41  ?  461 ASN A N     1 
ATOM   3418 C  CA    . ASN A 1 475 ? 24.463  32.219  -4.011  1.00 28.82  ?  461 ASN A CA    1 
ATOM   3419 C  C     . ASN A 1 475 ? 23.868  32.641  -5.343  1.00 33.96  ?  461 ASN A C     1 
ATOM   3420 O  O     . ASN A 1 475 ? 24.386  33.521  -6.031  1.00 33.32  ?  461 ASN A O     1 
ATOM   3421 C  CB    . ASN A 1 475 ? 25.122  33.391  -3.293  1.00 30.09  ?  461 ASN A CB    1 
ATOM   3422 C  CG    . ASN A 1 475 ? 24.126  34.482  -2.922  1.00 40.70  ?  461 ASN A CG    1 
ATOM   3423 O  OD1   . ASN A 1 475 ? 22.930  34.363  -3.193  1.00 37.32  ?  461 ASN A OD1   1 
ATOM   3424 N  ND2   . ASN A 1 475 ? 24.615  35.549  -2.298  1.00 32.04  ?  461 ASN A ND2   1 
ATOM   3425 N  N     . ASN A 1 476 ? 22.754  32.012  -5.707  1.00 31.71  ?  462 ASN A N     1 
ATOM   3426 C  CA    . ASN A 1 476 ? 21.977  32.445  -6.858  1.00 33.85  ?  462 ASN A CA    1 
ATOM   3427 C  C     . ASN A 1 476 ? 20.679  33.130  -6.449  1.00 34.40  ?  462 ASN A C     1 
ATOM   3428 O  O     . ASN A 1 476 ? 19.796  33.319  -7.292  1.00 29.60  ?  462 ASN A O     1 
ATOM   3429 C  CB    . ASN A 1 476 ? 21.699  31.255  -7.774  1.00 32.83  ?  462 ASN A CB    1 
ATOM   3430 C  CG    . ASN A 1 476 ? 21.414  29.984  -7.004  1.00 32.94  ?  462 ASN A CG    1 
ATOM   3431 O  OD1   . ASN A 1 476 ? 20.791  30.013  -5.943  1.00 29.41  ?  462 ASN A OD1   1 
ATOM   3432 N  ND2   . ASN A 1 476 ? 21.835  28.852  -7.555  1.00 34.51  ?  462 ASN A ND2   1 
ATOM   3433 N  N     . GLU A 1 477 ? 20.559  33.514  -5.175  1.00 29.03  ?  463 GLU A N     1 
ATOM   3434 C  CA    . GLU A 1 477 ? 19.416  34.249  -4.631  1.00 29.15  ?  463 GLU A CA    1 
ATOM   3435 C  C     . GLU A 1 477 ? 18.092  33.522  -4.884  1.00 36.41  ?  463 GLU A C     1 
ATOM   3436 O  O     . GLU A 1 477 ? 17.158  34.062  -5.485  1.00 33.82  ?  463 GLU A O     1 
ATOM   3437 C  CB    . GLU A 1 477 ? 19.377  35.677  -5.183  1.00 30.44  ?  463 GLU A CB    1 
ATOM   3438 C  CG    . GLU A 1 477 ? 20.638  36.462  -4.865  1.00 40.84  ?  463 GLU A CG    1 
ATOM   3439 C  CD    . GLU A 1 477 ? 20.470  37.953  -5.067  1.00 52.68  ?  463 GLU A CD    1 
ATOM   3440 O  OE1   . GLU A 1 477 ? 19.720  38.352  -5.985  1.00 50.11  ?  463 GLU A OE1   1 
ATOM   3441 O  OE2   . GLU A 1 477 ? 21.097  38.724  -4.308  1.00 56.30  ?  463 GLU A OE2   1 
ATOM   3442 N  N     . GLY A 1 478 ? 18.008  32.290  -4.373  1.00 29.75  ?  464 GLY A N     1 
ATOM   3443 C  CA    . GLY A 1 478 ? 16.758  31.569  -4.353  1.00 27.78  ?  464 GLY A CA    1 
ATOM   3444 C  C     . GLY A 1 478 ? 16.946  30.129  -4.778  1.00 39.31  ?  464 GLY A C     1 
ATOM   3445 O  O     . GLY A 1 478 ? 18.058  29.603  -4.808  1.00 30.15  ?  464 GLY A O     1 
ATOM   3446 N  N     . TYR A 1 479 ? 15.817  29.482  -5.079  1.00 30.97  ?  465 TYR A N     1 
ATOM   3447 C  CA    . TYR A 1 479 ? 15.776  28.077  -5.485  1.00 26.25  ?  465 TYR A CA    1 
ATOM   3448 C  C     . TYR A 1 479 ? 15.758  27.985  -7.011  1.00 31.23  ?  465 TYR A C     1 
ATOM   3449 O  O     . TYR A 1 479 ? 14.706  27.819  -7.633  1.00 28.56  ?  465 TYR A O     1 
ATOM   3450 C  CB    . TYR A 1 479 ? 14.537  27.397  -4.898  1.00 29.06  ?  465 TYR A CB    1 
ATOM   3451 C  CG    . TYR A 1 479 ? 14.294  27.543  -3.405  1.00 29.31  ?  465 TYR A CG    1 
ATOM   3452 C  CD1   . TYR A 1 479 ? 15.247  27.135  -2.479  1.00 25.55  ?  465 TYR A CD1   1 
ATOM   3453 C  CD2   . TYR A 1 479 ? 13.080  28.029  -2.922  1.00 26.93  ?  465 TYR A CD2   1 
ATOM   3454 C  CE1   . TYR A 1 479 ? 15.014  27.233  -1.114  1.00 23.81  ?  465 TYR A CE1   1 
ATOM   3455 C  CE2   . TYR A 1 479 ? 12.838  28.130  -1.555  1.00 24.39  ?  465 TYR A CE2   1 
ATOM   3456 C  CZ    . TYR A 1 479 ? 13.808  27.723  -0.658  1.00 23.99  ?  465 TYR A CZ    1 
ATOM   3457 O  OH    . TYR A 1 479 ? 13.581  27.819  0.696   1.00 26.36  ?  465 TYR A OH    1 
ATOM   3458 N  N     . THR A 1 480 ? 16.941  28.052  -7.631  1.00 26.49  ?  466 THR A N     1 
ATOM   3459 C  CA    . THR A 1 480 ? 16.946  28.075  -9.095  1.00 34.76  ?  466 THR A CA    1 
ATOM   3460 C  C     . THR A 1 480 ? 16.535  26.737  -9.698  1.00 30.40  ?  466 THR A C     1 
ATOM   3461 O  O     . THR A 1 480 ? 15.999  26.711  -10.812 1.00 37.68  ?  466 THR A O     1 
ATOM   3462 C  CB    . THR A 1 480 ? 18.297  28.522  -9.649  1.00 27.82  ?  466 THR A CB    1 
ATOM   3463 O  OG1   . THR A 1 480 ? 19.168  27.403  -9.789  1.00 40.05  ?  466 THR A OG1   1 
ATOM   3464 C  CG2   . THR A 1 480 ? 18.889  29.532  -8.758  1.00 30.00  ?  466 THR A CG2   1 
ATOM   3465 N  N     . VAL A 1 481 ? 16.791  25.622  -9.010  1.00 28.11  ?  467 VAL A N     1 
ATOM   3466 C  CA    . VAL A 1 481 ? 16.298  24.340  -9.510  1.00 26.01  ?  467 VAL A CA    1 
ATOM   3467 C  C     . VAL A 1 481 ? 14.777  24.370  -9.605  1.00 26.08  ?  467 VAL A C     1 
ATOM   3468 O  O     . VAL A 1 481 ? 14.192  23.958  -10.613 1.00 33.56  ?  467 VAL A O     1 
ATOM   3469 C  CB    . VAL A 1 481 ? 16.790  23.182  -8.624  1.00 28.94  ?  467 VAL A CB    1 
ATOM   3470 C  CG1   . VAL A 1 481 ? 15.834  22.003  -8.698  1.00 37.89  ?  467 VAL A CG1   1 
ATOM   3471 C  CG2   . VAL A 1 481 ? 18.150  22.742  -9.077  1.00 42.19  ?  467 VAL A CG2   1 
ATOM   3472 N  N     . LEU A 1 482 ? 14.115  24.884  -8.563  1.00 30.27  ?  468 LEU A N     1 
ATOM   3473 C  CA    . LEU A 1 482 ? 12.665  25.054  -8.623  1.00 29.60  ?  468 LEU A CA    1 
ATOM   3474 C  C     . LEU A 1 482 ? 12.273  26.063  -9.696  1.00 35.14  ?  468 LEU A C     1 
ATOM   3475 O  O     . LEU A 1 482 ? 11.267  25.878  -10.393 1.00 33.02  ?  468 LEU A O     1 
ATOM   3476 C  CB    . LEU A 1 482 ? 12.135  25.488  -7.258  1.00 25.15  ?  468 LEU A CB    1 
ATOM   3477 C  CG    . LEU A 1 482 ? 12.341  24.512  -6.100  1.00 27.08  ?  468 LEU A CG    1 
ATOM   3478 C  CD1   . LEU A 1 482 ? 11.579  24.979  -4.882  1.00 28.71  ?  468 LEU A CD1   1 
ATOM   3479 C  CD2   . LEU A 1 482 ? 11.911  23.106  -6.499  1.00 31.56  ?  468 LEU A CD2   1 
ATOM   3480 N  N     . ARG A 1 483 ? 13.079  27.118  -9.867  1.00 33.27  ?  469 ARG A N     1 
ATOM   3481 C  CA    . ARG A 1 483 ? 12.803  28.110  -10.905 1.00 32.94  ?  469 ARG A CA    1 
ATOM   3482 C  C     . ARG A 1 483 ? 12.864  27.481  -12.289 1.00 40.10  ?  469 ARG A C     1 
ATOM   3483 O  O     . ARG A 1 483 ? 12.019  27.762  -13.147 1.00 35.85  ?  469 ARG A O     1 
ATOM   3484 C  CB    . ARG A 1 483 ? 13.807  29.263  -10.824 1.00 31.31  ?  469 ARG A CB    1 
ATOM   3485 C  CG    . ARG A 1 483 ? 13.659  30.225  -9.651  1.00 32.60  ?  469 ARG A CG    1 
ATOM   3486 C  CD    . ARG A 1 483 ? 14.641  31.389  -9.823  1.00 29.02  ?  469 ARG A CD    1 
ATOM   3487 N  NE    . ARG A 1 483 ? 14.930  32.100  -8.584  1.00 28.83  ?  469 ARG A NE    1 
ATOM   3488 C  CZ    . ARG A 1 483 ? 14.118  32.986  -8.022  1.00 37.28  ?  469 ARG A CZ    1 
ATOM   3489 N  NH1   . ARG A 1 483 ? 12.941  33.278  -8.552  1.00 29.58  ?  469 ARG A NH1   1 
ATOM   3490 N  NH2   . ARG A 1 483 ? 14.502  33.603  -6.907  1.00 29.08  ?  469 ARG A NH2   1 
ATOM   3491 N  N     . ALA A 1 484 ? 13.885  26.653  -12.533 1.00 33.63  ?  470 ALA A N     1 
ATOM   3492 C  CA    . ALA A 1 484 ? 13.964  25.903  -13.783 1.00 39.99  ?  470 ALA A CA    1 
ATOM   3493 C  C     . ALA A 1 484 ? 12.758  24.990  -13.969 1.00 28.97  ?  470 ALA A C     1 
ATOM   3494 O  O     . ALA A 1 484 ? 12.288  24.799  -15.096 1.00 37.22  ?  470 ALA A O     1 
ATOM   3495 C  CB    . ALA A 1 484 ? 15.264  25.099  -13.831 1.00 40.33  ?  470 ALA A CB    1 
ATOM   3496 N  N     . ILE A 1 485 ? 12.296  24.354  -12.892 1.00 29.69  ?  471 ILE A N     1 
ATOM   3497 C  CA    . ILE A 1 485 ? 11.144  23.456  -12.983 1.00 33.77  ?  471 ILE A CA    1 
ATOM   3498 C  C     . ILE A 1 485 ? 9.872   24.242  -13.303 1.00 40.89  ?  471 ILE A C     1 
ATOM   3499 O  O     . ILE A 1 485 ? 9.188   23.965  -14.296 1.00 38.46  ?  471 ILE A O     1 
ATOM   3500 C  CB    . ILE A 1 485 ? 11.006  22.611  -11.706 1.00 33.32  ?  471 ILE A CB    1 
ATOM   3501 C  CG1   . ILE A 1 485 ? 12.109  21.542  -11.677 1.00 33.81  ?  471 ILE A CG1   1 
ATOM   3502 C  CG2   . ILE A 1 485 ? 9.640   21.940  -11.657 1.00 37.61  ?  471 ILE A CG2   1 
ATOM   3503 C  CD1   . ILE A 1 485 ? 12.504  21.075  -10.286 1.00 33.80  ?  471 ILE A CD1   1 
ATOM   3504 N  N     . HIS A 1 486 ? 9.517   25.207  -12.451 1.00 38.62  ?  472 HIS A N     1 
ATOM   3505 C  CA    . HIS A 1 486 ? 8.229   25.882  -12.584 1.00 42.24  ?  472 HIS A CA    1 
ATOM   3506 C  C     . HIS A 1 486 ? 8.232   27.199  -11.812 1.00 36.57  ?  472 HIS A C     1 
ATOM   3507 O  O     . HIS A 1 486 ? 8.683   27.254  -10.664 1.00 33.87  ?  472 HIS A O     1 
ATOM   3508 C  CB    . HIS A 1 486 ? 7.089   24.982  -12.094 1.00 36.82  ?  472 HIS A CB    1 
ATOM   3509 C  CG    . HIS A 1 486 ? 5.738   25.616  -12.181 1.00 31.33  ?  472 HIS A CG    1 
ATOM   3510 N  ND1   . HIS A 1 486 ? 4.939   25.507  -13.299 1.00 36.23  ?  472 HIS A ND1   1 
ATOM   3511 C  CD2   . HIS A 1 486 ? 5.036   26.350  -11.286 1.00 33.43  ?  472 HIS A CD2   1 
ATOM   3512 C  CE1   . HIS A 1 486 ? 3.809   26.161  -13.095 1.00 33.60  ?  472 HIS A CE1   1 
ATOM   3513 N  NE2   . HIS A 1 486 ? 3.841   26.677  -11.880 1.00 36.85  ?  472 HIS A NE2   1 
ATOM   3514 N  N     . GLY A 1 487 ? 7.708   28.249  -12.451 1.00 38.22  ?  473 GLY A N     1 
ATOM   3515 C  CA    . GLY A 1 487 ? 7.537   29.550  -11.838 1.00 32.60  ?  473 GLY A CA    1 
ATOM   3516 C  C     . GLY A 1 487 ? 8.833   30.290  -11.554 1.00 37.06  ?  473 GLY A C     1 
ATOM   3517 O  O     . GLY A 1 487 ? 9.122   30.645  -10.407 1.00 36.84  ?  473 GLY A O     1 
ATOM   3518 N  N     . PRO A 1 488 ? 9.620   30.584  -12.601 1.00 35.28  ?  474 PRO A N     1 
ATOM   3519 C  CA    . PRO A 1 488 ? 10.910  31.269  -12.373 1.00 34.66  ?  474 PRO A CA    1 
ATOM   3520 C  C     . PRO A 1 488 ? 10.775  32.609  -11.674 1.00 39.13  ?  474 PRO A C     1 
ATOM   3521 O  O     . PRO A 1 488 ? 11.651  32.982  -10.881 1.00 33.86  ?  474 PRO A O     1 
ATOM   3522 C  CB    . PRO A 1 488 ? 11.485  31.433  -13.789 1.00 32.85  ?  474 PRO A CB    1 
ATOM   3523 C  CG    . PRO A 1 488 ? 10.331  31.230  -14.718 1.00 35.37  ?  474 PRO A CG    1 
ATOM   3524 C  CD    . PRO A 1 488 ? 9.358   30.340  -14.030 1.00 31.26  ?  474 PRO A CD    1 
ATOM   3525 N  N     . GLU A 1 489 ? 9.714   33.357  -11.967 1.00 37.43  ?  475 GLU A N     1 
ATOM   3526 C  CA    . GLU A 1 489 ? 9.491   34.667  -11.370 1.00 44.85  ?  475 GLU A CA    1 
ATOM   3527 C  C     . GLU A 1 489 ? 8.530   34.621  -10.185 1.00 43.89  ?  475 GLU A C     1 
ATOM   3528 O  O     . GLU A 1 489 ? 8.126   35.674  -9.688  1.00 32.49  ?  475 GLU A O     1 
ATOM   3529 C  CB    . GLU A 1 489 ? 8.990   35.651  -12.427 1.00 41.03  ?  475 GLU A CB    1 
ATOM   3530 C  CG    . GLU A 1 489 ? 9.962   35.826  -13.584 1.00 54.74  ?  475 GLU A CG    1 
ATOM   3531 C  CD    . GLU A 1 489 ? 9.610   36.994  -14.478 1.00 65.34  ?  475 GLU A CD    1 
ATOM   3532 O  OE1   . GLU A 1 489 ? 9.115   38.016  -13.955 1.00 87.21  ?  475 GLU A OE1   1 
ATOM   3533 O  OE2   . GLU A 1 489 ? 9.828   36.896  -15.704 1.00 67.35  ?  475 GLU A OE2   1 
ATOM   3534 N  N     . GLN A 1 490 ? 8.143   33.433  -9.732  1.00 39.34  ?  476 GLN A N     1 
ATOM   3535 C  CA    . GLN A 1 490 ? 7.230   33.327  -8.603  1.00 38.78  ?  476 GLN A CA    1 
ATOM   3536 C  C     . GLN A 1 490 ? 7.963   33.534  -7.282  1.00 42.14  ?  476 GLN A C     1 
ATOM   3537 O  O     . GLN A 1 490 ? 9.099   33.088  -7.098  1.00 32.01  ?  476 GLN A O     1 
ATOM   3538 C  CB    . GLN A 1 490 ? 6.515   31.973  -8.606  1.00 30.76  ?  476 GLN A CB    1 
ATOM   3539 C  CG    . GLN A 1 490 ? 5.461   31.840  -9.702  1.00 30.40  ?  476 GLN A CG    1 
ATOM   3540 C  CD    . GLN A 1 490 ? 4.185   32.626  -9.401  1.00 40.73  ?  476 GLN A CD    1 
ATOM   3541 O  OE1   . GLN A 1 490 ? 4.218   33.840  -9.187  1.00 38.95  ?  476 GLN A OE1   1 
ATOM   3542 N  NE2   . GLN A 1 490 ? 3.052   31.932  -9.392  1.00 35.24  ?  476 GLN A NE2   1 
ATOM   3543 N  N     . ARG A 1 491 ? 7.287   34.216  -6.359  1.00 36.31  ?  477 ARG A N     1 
ATOM   3544 C  CA    . ARG A 1 491 ? 7.878   34.613  -5.088  1.00 36.33  ?  477 ARG A CA    1 
ATOM   3545 C  C     . ARG A 1 491 ? 8.180   33.428  -4.170  1.00 37.30  ?  477 ARG A C     1 
ATOM   3546 O  O     . ARG A 1 491 ? 9.057   33.542  -3.307  1.00 35.68  ?  477 ARG A O     1 
ATOM   3547 C  CB    . ARG A 1 491 ? 6.928   35.617  -4.414  1.00 45.96  ?  477 ARG A CB    1 
ATOM   3548 C  CG    . ARG A 1 491 ? 7.090   35.815  -2.921  1.00 50.57  ?  477 ARG A CG    1 
ATOM   3549 C  CD    . ARG A 1 491 ? 6.168   36.925  -2.410  1.00 53.20  ?  477 ARG A CD    1 
ATOM   3550 N  NE    . ARG A 1 491 ? 4.916   36.428  -1.847  1.00 48.56  ?  477 ARG A NE    1 
ATOM   3551 C  CZ    . ARG A 1 491 ? 4.812   35.767  -0.700  1.00 59.07  ?  477 ARG A CZ    1 
ATOM   3552 N  NH1   . ARG A 1 491 ? 5.876   35.471  0.030   1.00 43.09  ?  477 ARG A NH1   1 
ATOM   3553 N  NH2   . ARG A 1 491 ? 3.606   35.400  -0.271  1.00 59.88  ?  477 ARG A NH2   1 
ATOM   3554 N  N     . TYR A 1 492 ? 7.503   32.287  -4.342  1.00 28.22  ?  478 TYR A N     1 
ATOM   3555 C  CA    . TYR A 1 492 ? 7.815   31.142  -3.492  1.00 31.89  ?  478 TYR A CA    1 
ATOM   3556 C  C     . TYR A 1 492 ? 9.176   30.533  -3.812  1.00 33.74  ?  478 TYR A C     1 
ATOM   3557 O  O     . TYR A 1 492 ? 9.701   29.759  -3.002  1.00 25.92  ?  478 TYR A O     1 
ATOM   3558 C  CB    . TYR A 1 492 ? 6.727   30.072  -3.595  1.00 29.75  ?  478 TYR A CB    1 
ATOM   3559 C  CG    . TYR A 1 492 ? 6.363   29.642  -4.998  1.00 35.07  ?  478 TYR A CG    1 
ATOM   3560 C  CD1   . TYR A 1 492 ? 7.239   28.876  -5.767  1.00 29.30  ?  478 TYR A CD1   1 
ATOM   3561 C  CD2   . TYR A 1 492 ? 5.124   29.967  -5.542  1.00 29.58  ?  478 TYR A CD2   1 
ATOM   3562 C  CE1   . TYR A 1 492 ? 6.899   28.468  -7.046  1.00 27.11  ?  478 TYR A CE1   1 
ATOM   3563 C  CE2   . TYR A 1 492 ? 4.770   29.557  -6.818  1.00 35.32  ?  478 TYR A CE2   1 
ATOM   3564 C  CZ    . TYR A 1 492 ? 5.663   28.808  -7.565  1.00 33.09  ?  478 TYR A CZ    1 
ATOM   3565 O  OH    . TYR A 1 492 ? 5.321   28.401  -8.833  1.00 32.46  ?  478 TYR A OH    1 
ATOM   3566 N  N     . ASN A 1 493 ? 9.758   30.866  -4.963  1.00 29.97  ?  479 ASN A N     1 
ATOM   3567 C  CA    . ASN A 1 493 ? 11.108  30.441  -5.300  1.00 32.55  ?  479 ASN A CA    1 
ATOM   3568 C  C     . ASN A 1 493 ? 12.177  31.402  -4.789  1.00 35.18  ?  479 ASN A C     1 
ATOM   3569 O  O     . ASN A 1 493 ? 13.370  31.139  -4.989  1.00 33.17  ?  479 ASN A O     1 
ATOM   3570 C  CB    . ASN A 1 493 ? 11.228  30.259  -6.817  1.00 33.90  ?  479 ASN A CB    1 
ATOM   3571 C  CG    . ASN A 1 493 ? 10.527  29.000  -7.304  1.00 28.00  ?  479 ASN A CG    1 
ATOM   3572 O  OD1   . ASN A 1 493 ? 10.280  28.082  -6.527  1.00 28.17  ?  479 ASN A OD1   1 
ATOM   3573 N  ND2   . ASN A 1 493 ? 10.195  28.957  -8.590  1.00 30.93  ?  479 ASN A ND2   1 
ATOM   3574 N  N     . ASP A 1 494 ? 11.782  32.498  -4.140  1.00 31.51  ?  480 ASP A N     1 
ATOM   3575 C  CA    . ASP A 1 494 ? 12.708  33.404  -3.474  1.00 32.65  ?  480 ASP A CA    1 
ATOM   3576 C  C     . ASP A 1 494 ? 12.998  32.916  -2.055  1.00 41.78  ?  480 ASP A C     1 
ATOM   3577 O  O     . ASP A 1 494 ? 12.219  32.167  -1.456  1.00 36.78  ?  480 ASP A O     1 
ATOM   3578 C  CB    . ASP A 1 494 ? 12.143  34.829  -3.406  1.00 32.58  ?  480 ASP A CB    1 
ATOM   3579 C  CG    . ASP A 1 494 ? 11.937  35.461  -4.777  1.00 35.78  ?  480 ASP A CG    1 
ATOM   3580 O  OD1   . ASP A 1 494 ? 12.732  35.192  -5.702  1.00 40.45  ?  480 ASP A OD1   1 
ATOM   3581 O  OD2   . ASP A 1 494 ? 10.981  36.257  -4.918  1.00 43.32  ?  480 ASP A OD2   1 
ATOM   3582 N  N     . ILE A 1 495 ? 14.122  33.383  -1.507  1.00 31.17  ?  481 ILE A N     1 
ATOM   3583 C  CA    . ILE A 1 495 ? 14.515  33.108  -0.132  1.00 28.52  ?  481 ILE A CA    1 
ATOM   3584 C  C     . ILE A 1 495 ? 14.925  34.422  0.521   1.00 38.02  ?  481 ILE A C     1 
ATOM   3585 O  O     . ILE A 1 495 ? 15.215  35.413  -0.152  1.00 33.66  ?  481 ILE A O     1 
ATOM   3586 C  CB    . ILE A 1 495 ? 15.672  32.089  -0.040  1.00 30.22  ?  481 ILE A CB    1 
ATOM   3587 C  CG1   . ILE A 1 495 ? 16.900  32.613  -0.782  1.00 29.08  ?  481 ILE A CG1   1 
ATOM   3588 C  CG2   . ILE A 1 495 ? 15.258  30.727  -0.605  1.00 26.84  ?  481 ILE A CG2   1 
ATOM   3589 C  CD1   . ILE A 1 495 ? 18.145  31.770  -0.576  1.00 29.87  ?  481 ILE A CD1   1 
ATOM   3590 N  N     . ALA A 1 496 ? 14.934  34.427  1.853   1.00 29.75  ?  482 ALA A N     1 
ATOM   3591 C  CA    . ALA A 1 496 ? 15.557  35.527  2.577   1.00 29.15  ?  482 ALA A CA    1 
ATOM   3592 C  C     . ALA A 1 496 ? 17.032  35.616  2.199   1.00 28.41  ?  482 ALA A C     1 
ATOM   3593 O  O     . ALA A 1 496 ? 17.722  34.598  2.106   1.00 31.00  ?  482 ALA A O     1 
ATOM   3594 C  CB    . ALA A 1 496 ? 15.403  35.330  4.084   1.00 34.30  ?  482 ALA A CB    1 
ATOM   3595 N  N     . LEU A 1 497 ? 17.509  36.833  1.949   1.00 32.81  ?  483 LEU A N     1 
ATOM   3596 C  CA    . LEU A 1 497 ? 18.875  37.048  1.481   1.00 31.00  ?  483 LEU A CA    1 
ATOM   3597 C  C     . LEU A 1 497 ? 19.796  37.235  2.686   1.00 34.65  ?  483 LEU A C     1 
ATOM   3598 O  O     . LEU A 1 497 ? 19.732  38.262  3.373   1.00 29.58  ?  483 LEU A O     1 
ATOM   3599 C  CB    . LEU A 1 497 ? 18.926  38.251  0.542   1.00 35.89  ?  483 LEU A CB    1 
ATOM   3600 C  CG    . LEU A 1 497 ? 18.160  38.036  -0.770  1.00 36.21  ?  483 LEU A CG    1 
ATOM   3601 C  CD1   . LEU A 1 497 ? 18.305  39.221  -1.710  1.00 32.13  ?  483 LEU A CD1   1 
ATOM   3602 C  CD2   . LEU A 1 497 ? 18.625  36.750  -1.447  1.00 32.42  ?  483 LEU A CD2   1 
ATOM   3603 N  N     . TRP A 1 498 ? 20.676  36.264  2.915   1.00 28.80  ?  484 TRP A N     1 
ATOM   3604 C  CA    . TRP A 1 498 ? 21.567  36.276  4.065   1.00 31.80  ?  484 TRP A CA    1 
ATOM   3605 C  C     . TRP A 1 498 ? 22.897  36.933  3.712   1.00 32.15  ?  484 TRP A C     1 
ATOM   3606 O  O     . TRP A 1 498 ? 23.237  37.119  2.542   1.00 32.36  ?  484 TRP A O     1 
ATOM   3607 C  CB    . TRP A 1 498 ? 21.822  34.859  4.580   1.00 29.80  ?  484 TRP A CB    1 
ATOM   3608 C  CG    . TRP A 1 498 ? 20.647  34.238  5.281   1.00 35.46  ?  484 TRP A CG    1 
ATOM   3609 C  CD1   . TRP A 1 498 ? 19.388  34.762  5.399   1.00 33.33  ?  484 TRP A CD1   1 
ATOM   3610 C  CD2   . TRP A 1 498 ? 20.618  32.972  5.954   1.00 29.22  ?  484 TRP A CD2   1 
ATOM   3611 N  NE1   . TRP A 1 498 ? 18.583  33.901  6.105   1.00 29.51  ?  484 TRP A NE1   1 
ATOM   3612 C  CE2   . TRP A 1 498 ? 19.311  32.795  6.456   1.00 32.79  ?  484 TRP A CE2   1 
ATOM   3613 C  CE3   . TRP A 1 498 ? 21.570  31.972  6.181   1.00 30.09  ?  484 TRP A CE3   1 
ATOM   3614 C  CZ2   . TRP A 1 498 ? 18.931  31.659  7.170   1.00 30.35  ?  484 TRP A CZ2   1 
ATOM   3615 C  CZ3   . TRP A 1 498 ? 21.191  30.842  6.894   1.00 33.48  ?  484 TRP A CZ3   1 
ATOM   3616 C  CH2   . TRP A 1 498 ? 19.882  30.697  7.379   1.00 31.44  ?  484 TRP A CH2   1 
ATOM   3617 N  N     . ASN A 1 499 ? 23.644  37.298  4.754   1.00 33.71  ?  485 ASN A N     1 
ATOM   3618 C  CA    . ASN A 1 499 ? 24.986  37.866  4.607   1.00 36.38  ?  485 ASN A CA    1 
ATOM   3619 C  C     . ASN A 1 499 ? 25.996  36.769  4.932   1.00 33.59  ?  485 ASN A C     1 
ATOM   3620 O  O     . ASN A 1 499 ? 26.534  36.688  6.037   1.00 31.77  ?  485 ASN A O     1 
ATOM   3621 C  CB    . ASN A 1 499 ? 25.147  39.074  5.516   1.00 32.91  ?  485 ASN A CB    1 
ATOM   3622 C  CG    . ASN A 1 499 ? 26.345  39.925  5.147   1.00 40.34  ?  485 ASN A CG    1 
ATOM   3623 O  OD1   . ASN A 1 499 ? 27.007  39.682  4.138   1.00 39.97  ?  485 ASN A OD1   1 
ATOM   3624 N  ND2   . ASN A 1 499 ? 26.627  40.930  5.963   1.00 37.30  ?  485 ASN A ND2   1 
ATOM   3625 N  N     . TRP A 1 500 ? 26.282  35.938  3.922   1.00 33.04  ?  486 TRP A N     1 
ATOM   3626 C  CA    . TRP A 1 500 ? 26.931  34.649  4.162   1.00 34.83  ?  486 TRP A CA    1 
ATOM   3627 C  C     . TRP A 1 500 ? 28.320  34.805  4.769   1.00 37.71  ?  486 TRP A C     1 
ATOM   3628 O  O     . TRP A 1 500 ? 28.692  34.049  5.675   1.00 35.58  ?  486 TRP A O     1 
ATOM   3629 C  CB    . TRP A 1 500 ? 27.004  33.850  2.859   1.00 32.27  ?  486 TRP A CB    1 
ATOM   3630 C  CG    . TRP A 1 500 ? 25.652  33.435  2.374   1.00 31.20  ?  486 TRP A CG    1 
ATOM   3631 C  CD1   . TRP A 1 500 ? 24.875  34.083  1.460   1.00 31.37  ?  486 TRP A CD1   1 
ATOM   3632 C  CD2   . TRP A 1 500 ? 24.910  32.282  2.789   1.00 30.97  ?  486 TRP A CD2   1 
ATOM   3633 N  NE1   . TRP A 1 500 ? 23.691  33.406  1.280   1.00 33.97  ?  486 TRP A NE1   1 
ATOM   3634 C  CE2   . TRP A 1 500 ? 23.690  32.294  2.083   1.00 38.77  ?  486 TRP A CE2   1 
ATOM   3635 C  CE3   . TRP A 1 500 ? 25.159  31.240  3.689   1.00 31.99  ?  486 TRP A CE3   1 
ATOM   3636 C  CZ2   . TRP A 1 500 ? 22.716  31.304  2.250   1.00 31.62  ?  486 TRP A CZ2   1 
ATOM   3637 C  CZ3   . TRP A 1 500 ? 24.198  30.258  3.855   1.00 27.10  ?  486 TRP A CZ3   1 
ATOM   3638 C  CH2   . TRP A 1 500 ? 22.989  30.296  3.137   1.00 35.77  ?  486 TRP A CH2   1 
ATOM   3639 N  N     . THR A 1 501 ? 29.103  35.777  4.294   1.00 29.25  ?  487 THR A N     1 
ATOM   3640 C  CA    . THR A 1 501 ? 30.468  35.926  4.789   1.00 35.87  ?  487 THR A CA    1 
ATOM   3641 C  C     . THR A 1 501 ? 30.524  36.370  6.244   1.00 37.72  ?  487 THR A C     1 
ATOM   3642 O  O     . THR A 1 501 ? 31.615  36.391  6.824   1.00 38.18  ?  487 THR A O     1 
ATOM   3643 C  CB    . THR A 1 501 ? 31.261  36.911  3.925   1.00 37.93  ?  487 THR A CB    1 
ATOM   3644 O  OG1   . THR A 1 501 ? 30.645  38.203  3.974   1.00 41.90  ?  487 THR A OG1   1 
ATOM   3645 C  CG2   . THR A 1 501 ? 31.317  36.427  2.481   1.00 31.26  ?  487 THR A CG2   1 
ATOM   3646 N  N     . GLN A 1 502 ? 29.397  36.763  6.832   1.00 32.66  ?  488 GLN A N     1 
ATOM   3647 C  CA    . GLN A 1 502 ? 29.354  37.196  8.220   1.00 31.80  ?  488 GLN A CA    1 
ATOM   3648 C  C     . GLN A 1 502 ? 28.801  36.138  9.165   1.00 32.23  ?  488 GLN A C     1 
ATOM   3649 O  O     . GLN A 1 502 ? 28.735  36.378  10.373  1.00 38.66  ?  488 GLN A O     1 
ATOM   3650 C  CB    . GLN A 1 502 ? 28.520  38.476  8.332   1.00 33.28  ?  488 GLN A CB    1 
ATOM   3651 C  CG    . GLN A 1 502 ? 29.210  39.709  7.768   1.00 36.57  ?  488 GLN A CG    1 
ATOM   3652 C  CD    . GLN A 1 502 ? 30.415  40.125  8.588   1.00 62.67  ?  488 GLN A CD    1 
ATOM   3653 O  OE1   . GLN A 1 502 ? 31.476  40.454  8.045   1.00 66.38  ?  488 GLN A OE1   1 
ATOM   3654 N  NE2   . GLN A 1 502 ? 30.260  40.112  9.908   1.00 58.24  ?  488 GLN A NE2   1 
ATOM   3655 N  N     . ILE A 1 503 ? 28.413  34.974  8.657   1.00 28.60  ?  489 ILE A N     1 
ATOM   3656 C  CA    . ILE A 1 503 ? 27.801  33.946  9.496   1.00 35.30  ?  489 ILE A CA    1 
ATOM   3657 C  C     . ILE A 1 503 ? 28.811  33.313  10.451  1.00 34.86  ?  489 ILE A C     1 
ATOM   3658 O  O     . ILE A 1 503 ? 28.474  33.110  11.628  1.00 29.84  ?  489 ILE A O     1 
ATOM   3659 C  CB    . ILE A 1 503 ? 27.094  32.887  8.636   1.00 36.43  ?  489 ILE A CB    1 
ATOM   3660 C  CG1   . ILE A 1 503 ? 25.863  33.515  7.979   1.00 36.67  ?  489 ILE A CG1   1 
ATOM   3661 C  CG2   . ILE A 1 503 ? 26.679  31.698  9.487   1.00 34.14  ?  489 ILE A CG2   1 
ATOM   3662 C  CD1   . ILE A 1 503 ? 25.253  32.668  6.904   1.00 35.58  ?  489 ILE A CD1   1 
ATOM   3663 N  N     . PRO A 1 504 ? 30.041  32.979  10.024  1.00 38.39  ?  490 PRO A N     1 
ATOM   3664 C  CA    . PRO A 1 504 ? 30.987  32.399  10.996  1.00 36.88  ?  490 PRO A CA    1 
ATOM   3665 C  C     . PRO A 1 504 ? 31.244  33.277  12.209  1.00 30.84  ?  490 PRO A C     1 
ATOM   3666 O  O     . PRO A 1 504 ? 31.331  32.756  13.327  1.00 39.02  ?  490 PRO A O     1 
ATOM   3667 C  CB    . PRO A 1 504 ? 32.256  32.194  10.157  1.00 32.22  ?  490 PRO A CB    1 
ATOM   3668 C  CG    . PRO A 1 504 ? 31.732  31.928  8.798   1.00 39.88  ?  490 PRO A CG    1 
ATOM   3669 C  CD    . PRO A 1 504 ? 30.571  32.878  8.650   1.00 34.64  ?  490 PRO A CD    1 
ATOM   3670 N  N     . GLN A 1 505 ? 31.340  34.597  12.036  1.00 37.02  ?  491 GLN A N     1 
ATOM   3671 C  CA    . GLN A 1 505 ? 31.618  35.459  13.181  1.00 45.33  ?  491 GLN A CA    1 
ATOM   3672 C  C     . GLN A 1 505 ? 30.399  35.643  14.079  1.00 39.04  ?  491 GLN A C     1 
ATOM   3673 O  O     . GLN A 1 505 ? 30.541  36.138  15.202  1.00 43.30  ?  491 GLN A O     1 
ATOM   3674 C  CB    . GLN A 1 505 ? 32.165  36.811  12.711  1.00 49.70  ?  491 GLN A CB    1 
ATOM   3675 C  CG    . GLN A 1 505 ? 31.148  37.681  12.019  1.00 57.71  ?  491 GLN A CG    1 
ATOM   3676 C  CD    . GLN A 1 505 ? 30.332  38.512  12.991  1.00 70.67  ?  491 GLN A CD    1 
ATOM   3677 O  OE1   . GLN A 1 505 ? 30.872  39.167  13.886  1.00 71.87  ?  491 GLN A OE1   1 
ATOM   3678 N  NE2   . GLN A 1 505 ? 29.017  38.432  12.860  1.00 58.07  ?  491 GLN A NE2   1 
ATOM   3679 N  N     . ALA A 1 506 ? 29.206  35.294  13.599  1.00 33.76  ?  492 ALA A N     1 
ATOM   3680 C  CA    . ALA A 1 506 ? 28.018  35.321  14.441  1.00 36.21  ?  492 ALA A CA    1 
ATOM   3681 C  C     . ALA A 1 506 ? 27.809  34.021  15.204  1.00 36.03  ?  492 ALA A C     1 
ATOM   3682 O  O     . ALA A 1 506 ? 27.227  34.037  16.297  1.00 34.46  ?  492 ALA A O     1 
ATOM   3683 C  CB    . ALA A 1 506 ? 26.776  35.617  13.596  1.00 32.60  ?  492 ALA A CB    1 
ATOM   3684 N  N     . LEU A 1 507 ? 28.267  32.897  14.655  1.00 31.67  ?  493 LEU A N     1 
ATOM   3685 C  CA    . LEU A 1 507 ? 28.046  31.584  15.247  1.00 32.06  ?  493 LEU A CA    1 
ATOM   3686 C  C     . LEU A 1 507 ? 29.233  31.092  16.068  1.00 30.83  ?  493 LEU A C     1 
ATOM   3687 O  O     . LEU A 1 507 ? 29.250  29.930  16.479  1.00 35.47  ?  493 LEU A O     1 
ATOM   3688 C  CB    . LEU A 1 507 ? 27.714  30.568  14.152  1.00 28.74  ?  493 LEU A CB    1 
ATOM   3689 C  CG    . LEU A 1 507 ? 26.404  30.769  13.384  1.00 35.31  ?  493 LEU A CG    1 
ATOM   3690 C  CD1   . LEU A 1 507 ? 26.021  29.491  12.658  1.00 27.12  ?  493 LEU A CD1   1 
ATOM   3691 C  CD2   . LEU A 1 507 ? 25.271  31.230  14.307  1.00 31.94  ?  493 LEU A CD2   1 
ATOM   3692 N  N     . SER A 1 508 ? 30.222  31.945  16.319  1.00 31.81  ?  494 SER A N     1 
ATOM   3693 C  CA    . SER A 1 508 ? 31.361  31.578  17.148  1.00 37.55  ?  494 SER A CA    1 
ATOM   3694 C  C     . SER A 1 508 ? 31.947  32.847  17.748  1.00 38.55  ?  494 SER A C     1 
ATOM   3695 O  O     . SER A 1 508 ? 31.954  33.896  17.102  1.00 40.03  ?  494 SER A O     1 
ATOM   3696 C  CB    . SER A 1 508 ? 32.421  30.819  16.339  1.00 34.60  ?  494 SER A CB    1 
ATOM   3697 O  OG    . SER A 1 508 ? 33.715  31.032  16.866  1.00 42.35  ?  494 SER A OG    1 
ATOM   3698 N  N     . LEU A 1 509 ? 32.431  32.747  18.988  1.00 36.16  ?  495 LEU A N     1 
ATOM   3699 C  CA    . LEU A 1 509 ? 33.027  33.893  19.661  1.00 40.61  ?  495 LEU A CA    1 
ATOM   3700 C  C     . LEU A 1 509 ? 34.421  34.216  19.149  1.00 53.66  ?  495 LEU A C     1 
ATOM   3701 O  O     . LEU A 1 509 ? 34.904  35.332  19.365  1.00 59.81  ?  495 LEU A O     1 
ATOM   3702 C  CB    . LEU A 1 509 ? 33.086  33.648  21.170  1.00 39.59  ?  495 LEU A CB    1 
ATOM   3703 C  CG    . LEU A 1 509 ? 31.748  33.678  21.909  1.00 41.00  ?  495 LEU A CG    1 
ATOM   3704 C  CD1   . LEU A 1 509 ? 31.959  33.475  23.404  1.00 39.28  ?  495 LEU A CD1   1 
ATOM   3705 C  CD2   . LEU A 1 509 ? 31.030  34.988  21.636  1.00 37.39  ?  495 LEU A CD2   1 
ATOM   3706 N  N     . ASP A 1 510 ? 35.064  33.277  18.472  1.00 49.23  ?  496 ASP A N     1 
ATOM   3707 C  CA    . ASP A 1 510 ? 36.401  33.450  17.923  1.00 51.66  ?  496 ASP A CA    1 
ATOM   3708 C  C     . ASP A 1 510 ? 36.531  32.473  16.766  1.00 45.40  ?  496 ASP A C     1 
ATOM   3709 O  O     . ASP A 1 510 ? 37.195  31.437  16.892  1.00 44.29  ?  496 ASP A O     1 
ATOM   3710 C  CB    . ASP A 1 510 ? 37.477  33.211  18.984  1.00 54.08  ?  496 ASP A CB    1 
ATOM   3711 C  CG    . ASP A 1 510 ? 38.883  33.400  18.444  1.00 69.02  ?  496 ASP A CG    1 
ATOM   3712 O  OD1   . ASP A 1 510 ? 39.074  34.282  17.580  1.00 58.91  ?  496 ASP A OD1   1 
ATOM   3713 O  OD2   . ASP A 1 510 ? 39.800  32.672  18.888  1.00 72.90  ?  496 ASP A OD2   1 
ATOM   3714 N  N     . PRO A 1 511 ? 35.935  32.756  15.644  1.00 44.22  ?  497 PRO A N     1 
ATOM   3715 C  CA    . PRO A 1 511 ? 36.026  31.742  14.609  1.00 38.93  ?  497 PRO A CA    1 
ATOM   3716 C  C     . PRO A 1 511 ? 37.381  31.530  13.970  1.00 50.38  ?  497 PRO A C     1 
ATOM   3717 O  O     . PRO A 1 511 ? 38.077  32.466  13.673  1.00 52.17  ?  497 PRO A O     1 
ATOM   3718 C  CB    . PRO A 1 511 ? 35.067  32.255  13.571  1.00 48.10  ?  497 PRO A CB    1 
ATOM   3719 C  CG    . PRO A 1 511 ? 34.973  33.691  13.812  1.00 48.83  ?  497 PRO A CG    1 
ATOM   3720 C  CD    . PRO A 1 511 ? 35.075  33.865  15.266  1.00 41.81  ?  497 PRO A CD    1 
ATOM   3721 N  N     . GLN A 1 512 ? 37.743  30.294  13.680  1.00 50.24  ?  498 GLN A N     1 
ATOM   3722 C  CA    . GLN A 1 512 ? 39.003  30.024  13.002  1.00 63.95  ?  498 GLN A CA    1 
ATOM   3723 C  C     . GLN A 1 512 ? 38.572  29.954  11.559  1.00 65.69  ?  498 GLN A C     1 
ATOM   3724 O  O     . GLN A 1 512 ? 38.499  28.874  11.014  1.00 61.99  ?  498 GLN A O     1 
ATOM   3725 C  CB    . GLN A 1 512 ? 39.583  28.646  13.404  1.00 70.04  ?  498 GLN A CB    1 
ATOM   3726 C  CG    . GLN A 1 512 ? 40.392  28.570  14.693  1.00 59.42  ?  498 GLN A CG    1 
ATOM   3727 C  CD    . GLN A 1 512 ? 41.422  27.435  14.733  1.00 80.62  ?  498 GLN A CD    1 
ATOM   3728 O  OE1   . GLN A 1 512 ? 41.639  26.710  13.757  1.00 65.90  ?  498 GLN A OE1   1 
ATOM   3729 N  NE2   . GLN A 1 512 ? 42.065  27.286  15.879  1.00 82.41  ?  498 GLN A NE2   1 
ATOM   3730 N  N     . ALA A 1 513 ? 38.312  31.082  10.922  1.00 57.71  ?  499 ALA A N     1 
ATOM   3731 C  CA    . ALA A 1 513 ? 37.771  31.027  9.598   1.00 47.73  ?  499 ALA A CA    1 
ATOM   3732 C  C     . ALA A 1 513 ? 38.003  32.233  8.773   1.00 41.84  ?  499 ALA A C     1 
ATOM   3733 O  O     . ALA A 1 513 ? 38.185  33.279  9.280   1.00 47.36  ?  499 ALA A O     1 
ATOM   3734 C  CB    . ALA A 1 513 ? 36.279  30.803  9.707   1.00 33.90  ?  499 ALA A CB    1 
ATOM   3735 N  N     . GLN A 1 514 ? 37.959  32.055  7.478   1.00 45.65  ?  500 GLN A N     1 
ATOM   3736 C  CA    . GLN A 1 514 ? 38.088  33.124  6.551   1.00 43.44  ?  500 GLN A CA    1 
ATOM   3737 C  C     . GLN A 1 514 ? 36.998  32.990  5.539   1.00 39.70  ?  500 GLN A C     1 
ATOM   3738 O  O     . GLN A 1 514 ? 36.788  31.939  5.015   1.00 35.22  ?  500 GLN A O     1 
ATOM   3739 C  CB    . GLN A 1 514 ? 39.405  33.093  5.779   1.00 41.61  ?  500 GLN A CB    1 
ATOM   3740 C  CG    . GLN A 1 514 ? 40.572  32.414  6.431   1.00 69.12  ?  500 GLN A CG    1 
ATOM   3741 C  CD    . GLN A 1 514 ? 41.867  32.699  5.696   1.00 77.77  ?  500 GLN A CD    1 
ATOM   3742 O  OE1   . GLN A 1 514 ? 42.630  31.797  5.393   1.00 77.19  ?  500 GLN A OE1   1 
ATOM   3743 N  NE2   . GLN A 1 514 ? 42.091  33.981  5.372   1.00 68.29  ?  500 GLN A NE2   1 
ATOM   3744 N  N     . CYS A 1 515 ? 36.369  34.101  5.211   1.00 42.52  ?  501 CYS A N     1 
ATOM   3745 C  CA    . CYS A 1 515 ? 35.319  34.120  4.226   1.00 41.21  ?  501 CYS A CA    1 
ATOM   3746 C  C     . CYS A 1 515 ? 35.615  35.078  3.111   1.00 40.87  ?  501 CYS A C     1 
ATOM   3747 O  O     . CYS A 1 515 ? 36.233  36.083  3.315   1.00 40.60  ?  501 CYS A O     1 
ATOM   3748 C  CB    . CYS A 1 515 ? 34.009  34.509  4.876   1.00 39.90  ?  501 CYS A CB    1 
ATOM   3749 S  SG    . CYS A 1 515 ? 33.687  33.700  6.427   1.00 50.49  ?  501 CYS A SG    1 
ATOM   3750 N  N     . TRP A 1 516 ? 35.133  34.755  1.945   1.00 38.61  ?  502 TRP A N     1 
ATOM   3751 C  CA    . TRP A 1 516 ? 35.289  35.549  0.770   1.00 36.03  ?  502 TRP A CA    1 
ATOM   3752 C  C     . TRP A 1 516 ? 33.995  35.536  -0.006  1.00 37.28  ?  502 TRP A C     1 
ATOM   3753 O  O     . TRP A 1 516 ? 33.219  34.647  0.130   1.00 39.47  ?  502 TRP A O     1 
ATOM   3754 C  CB    . TRP A 1 516 ? 36.305  34.919  -0.158  1.00 37.57  ?  502 TRP A CB    1 
ATOM   3755 C  CG    . TRP A 1 516 ? 37.694  34.952  0.263   1.00 40.69  ?  502 TRP A CG    1 
ATOM   3756 C  CD1   . TRP A 1 516 ? 38.609  35.889  -0.042  1.00 45.30  ?  502 TRP A CD1   1 
ATOM   3757 C  CD2   . TRP A 1 516 ? 38.360  33.987  1.047   1.00 45.98  ?  502 TRP A CD2   1 
ATOM   3758 N  NE1   . TRP A 1 516 ? 39.802  35.580  0.497   1.00 42.55  ?  502 TRP A NE1   1 
ATOM   3759 C  CE2   . TRP A 1 516 ? 39.678  34.417  1.191   1.00 47.66  ?  502 TRP A CE2   1 
ATOM   3760 C  CE3   . TRP A 1 516 ? 37.975  32.802  1.650   1.00 42.93  ?  502 TRP A CE3   1 
ATOM   3761 C  CZ2   . TRP A 1 516 ? 40.596  33.714  1.904   1.00 43.25  ?  502 TRP A CZ2   1 
ATOM   3762 C  CZ3   . TRP A 1 516 ? 38.876  32.120  2.350   1.00 46.01  ?  502 TRP A CZ3   1 
ATOM   3763 C  CH2   . TRP A 1 516 ? 40.182  32.571  2.483   1.00 39.80  ?  502 TRP A CH2   1 
ATOM   3764 N  N     . ARG A 1 517 ? 33.764  36.581  -0.768  1.00 37.93  ?  503 ARG A N     1 
ATOM   3765 C  CA    . ARG A 1 517 ? 32.678  36.686  -1.733  1.00 36.44  ?  503 ARG A CA    1 
ATOM   3766 C  C     . ARG A 1 517 ? 33.275  36.886  -3.116  1.00 34.85  ?  503 ARG A C     1 
ATOM   3767 O  O     . ARG A 1 517 ? 34.097  37.784  -3.310  1.00 41.77  ?  503 ARG A O     1 
ATOM   3768 C  CB    . ARG A 1 517 ? 31.734  37.844  -1.387  1.00 47.39  ?  503 ARG A CB    1 
ATOM   3769 C  CG    . ARG A 1 517 ? 30.529  37.972  -2.316  1.00 44.63  ?  503 ARG A CG    1 
ATOM   3770 C  CD    . ARG A 1 517 ? 29.779  39.282  -2.078  1.00 51.19  ?  503 ARG A CD    1 
ATOM   3771 N  NE    . ARG A 1 517 ? 29.600  39.564  -0.659  1.00 47.91  ?  503 ARG A NE    1 
ATOM   3772 C  CZ    . ARG A 1 517 ? 30.192  40.552  -0.002  1.00 46.80  ?  503 ARG A CZ    1 
ATOM   3773 N  NH1   . ARG A 1 517 ? 31.020  41.389  -0.609  1.00 43.06  ?  503 ARG A NH1   1 
ATOM   3774 N  NH2   . ARG A 1 517 ? 29.949  40.703  1.298   1.00 47.69  ?  503 ARG A NH2   1 
ATOM   3775 N  N     . VAL A 1 518 ? 32.888  36.046  -4.071  1.00 37.22  ?  504 VAL A N     1 
ATOM   3776 C  CA    . VAL A 1 518 ? 33.463  36.082  -5.411  1.00 36.99  ?  504 VAL A CA    1 
ATOM   3777 C  C     . VAL A 1 518 ? 32.342  36.181  -6.437  1.00 43.32  ?  504 VAL A C     1 
ATOM   3778 O  O     . VAL A 1 518 ? 31.279  35.568  -6.277  1.00 41.02  ?  504 VAL A O     1 
ATOM   3779 C  CB    . VAL A 1 518 ? 34.361  34.858  -5.689  1.00 35.43  ?  504 VAL A CB    1 
ATOM   3780 C  CG1   . VAL A 1 518 ? 35.481  34.791  -4.668  1.00 40.92  ?  504 VAL A CG1   1 
ATOM   3781 C  CG2   . VAL A 1 518 ? 33.552  33.566  -5.667  1.00 33.59  ?  504 VAL A CG2   1 
ATOM   3782 N  N     . SER A 1 519 ? 32.574  36.982  -7.481  1.00 36.47  ?  505 SER A N     1 
ATOM   3783 C  CA    . SER A 1 519 ? 31.642  37.093  -8.595  1.00 38.44  ?  505 SER A CA    1 
ATOM   3784 C  C     . SER A 1 519 ? 32.277  36.828  -9.953  1.00 49.12  ?  505 SER A C     1 
ATOM   3785 O  O     . SER A 1 519 ? 31.550  36.763  -10.951 1.00 45.15  ?  505 SER A O     1 
ATOM   3786 C  CB    . SER A 1 519 ? 31.000  38.490  -8.623  1.00 40.84  ?  505 SER A CB    1 
ATOM   3787 O  OG    . SER A 1 519 ? 31.978  39.490  -8.870  1.00 50.68  ?  505 SER A OG    1 
ATOM   3788 N  N     . GLU A 1 520 ? 33.590  36.646  -10.023 1.00 38.88  ?  506 GLU A N     1 
ATOM   3789 C  CA    . GLU A 1 520 ? 34.299  36.427  -11.272 1.00 46.00  ?  506 GLU A CA    1 
ATOM   3790 C  C     . GLU A 1 520 ? 35.092  35.131  -11.182 1.00 44.86  ?  506 GLU A C     1 
ATOM   3791 O  O     . GLU A 1 520 ? 35.525  34.724  -10.099 1.00 39.36  ?  506 GLU A O     1 
ATOM   3792 C  CB    . GLU A 1 520 ? 35.236  37.601  -11.612 1.00 47.57  ?  506 GLU A CB    1 
ATOM   3793 C  CG    . GLU A 1 520 ? 34.653  38.982  -11.321 1.00 57.13  ?  506 GLU A CG    1 
ATOM   3794 C  CD    . GLU A 1 520 ? 33.540  39.379  -12.280 1.00 56.34  ?  506 GLU A CD    1 
ATOM   3795 O  OE1   . GLU A 1 520 ? 33.774  39.358  -13.508 1.00 54.04  ?  506 GLU A OE1   1 
ATOM   3796 O  OE2   . GLU A 1 520 ? 32.431  39.714  -11.805 1.00 59.10  ?  506 GLU A OE2   1 
ATOM   3797 N  N     . ALA A 1 521 ? 35.261  34.475  -12.332 1.00 43.22  ?  507 ALA A N     1 
ATOM   3798 C  CA    . ALA A 1 521 ? 35.951  33.188  -12.355 1.00 51.67  ?  507 ALA A CA    1 
ATOM   3799 C  C     . ALA A 1 521 ? 37.389  33.325  -11.869 1.00 50.29  ?  507 ALA A C     1 
ATOM   3800 O  O     . ALA A 1 521 ? 37.887  32.462  -11.136 1.00 41.59  ?  507 ALA A O     1 
ATOM   3801 C  CB    . ALA A 1 521 ? 35.914  32.594  -13.763 1.00 49.50  ?  507 ALA A CB    1 
ATOM   3802 N  N     . GLU A 1 522 ? 38.074  34.400  -12.276 1.00 45.55  ?  508 GLU A N     1 
ATOM   3803 C  CA    . GLU A 1 522 ? 39.446  34.619  -11.829 1.00 48.97  ?  508 GLU A CA    1 
ATOM   3804 C  C     . GLU A 1 522 ? 39.521  34.803  -10.314 1.00 48.38  ?  508 GLU A C     1 
ATOM   3805 O  O     . GLU A 1 522 ? 40.445  34.291  -9.671  1.00 46.59  ?  508 GLU A O     1 
ATOM   3806 C  CB    . GLU A 1 522 ? 40.063  35.815  -12.566 1.00 48.83  ?  508 GLU A CB    1 
ATOM   3807 C  CG    . GLU A 1 522 ? 39.385  37.169  -12.338 1.00 67.02  ?  508 GLU A CG    1 
ATOM   3808 C  CD    . GLU A 1 522 ? 38.385  37.532  -13.429 1.00 79.72  ?  508 GLU A CD    1 
ATOM   3809 O  OE1   . GLU A 1 522 ? 38.028  36.648  -14.241 1.00 76.91  ?  508 GLU A OE1   1 
ATOM   3810 O  OE2   . GLU A 1 522 ? 37.966  38.710  -13.481 1.00 80.08  ?  508 GLU A OE2   1 
ATOM   3811 N  N     . GLN A 1 523 ? 38.566  35.530  -9.724  1.00 44.94  ?  509 GLN A N     1 
ATOM   3812 C  CA    . GLN A 1 523 ? 38.558  35.677  -8.269  1.00 55.00  ?  509 GLN A CA    1 
ATOM   3813 C  C     . GLN A 1 523 ? 38.401  34.333  -7.575  1.00 41.32  ?  509 GLN A C     1 
ATOM   3814 O  O     . GLN A 1 523 ? 39.047  34.076  -6.552  1.00 45.94  ?  509 GLN A O     1 
ATOM   3815 C  CB    . GLN A 1 523 ? 37.432  36.600  -7.804  1.00 50.97  ?  509 GLN A CB    1 
ATOM   3816 C  CG    . GLN A 1 523 ? 37.195  37.837  -8.605  1.00 57.39  ?  509 GLN A CG    1 
ATOM   3817 C  CD    . GLN A 1 523 ? 36.115  38.678  -7.966  1.00 61.39  ?  509 GLN A CD    1 
ATOM   3818 O  OE1   . GLN A 1 523 ? 34.928  38.424  -8.162  1.00 54.37  ?  509 GLN A OE1   1 
ATOM   3819 N  NE2   . GLN A 1 523 ? 36.518  39.677  -7.189  1.00 54.83  ?  509 GLN A NE2   1 
ATOM   3820 N  N     . LEU A 1 524 ? 37.511  33.481  -8.088  1.00 47.54  ?  510 LEU A N     1 
ATOM   3821 C  CA    . LEU A 1 524 ? 37.315  32.164  -7.493  1.00 43.61  ?  510 LEU A CA    1 
ATOM   3822 C  C     . LEU A 1 524 ? 38.597  31.343  -7.537  1.00 39.68  ?  510 LEU A C     1 
ATOM   3823 O  O     . LEU A 1 524 ? 39.027  30.792  -6.517  1.00 41.20  ?  510 LEU A O     1 
ATOM   3824 C  CB    . LEU A 1 524 ? 36.184  31.436  -8.217  1.00 40.54  ?  510 LEU A CB    1 
ATOM   3825 C  CG    . LEU A 1 524 ? 35.878  30.012  -7.769  1.00 37.42  ?  510 LEU A CG    1 
ATOM   3826 C  CD1   . LEU A 1 524 ? 35.596  29.951  -6.274  1.00 34.28  ?  510 LEU A CD1   1 
ATOM   3827 C  CD2   . LEU A 1 524 ? 34.705  29.490  -8.556  1.00 35.97  ?  510 LEU A CD2   1 
ATOM   3828 N  N     . ALA A 1 525 ? 39.245  31.287  -8.703  1.00 41.33  ?  511 ALA A N     1 
ATOM   3829 C  CA    . ALA A 1 525 ? 40.487  30.530  -8.826  1.00 46.11  ?  511 ALA A CA    1 
ATOM   3830 C  C     . ALA A 1 525 ? 41.548  31.076  -7.882  1.00 54.45  ?  511 ALA A C     1 
ATOM   3831 O  O     . ALA A 1 525 ? 42.303  30.312  -7.269  1.00 49.43  ?  511 ALA A O     1 
ATOM   3832 C  CB    . ALA A 1 525 ? 40.985  30.563  -10.270 1.00 44.85  ?  511 ALA A CB    1 
ATOM   3833 N  N     . ASP A 1 526 ? 41.617  32.402  -7.764  1.00 55.87  ?  512 ASP A N     1 
ATOM   3834 C  CA    . ASP A 1 526 ? 42.526  33.043  -6.822  1.00 56.71  ?  512 ASP A CA    1 
ATOM   3835 C  C     . ASP A 1 526 ? 42.191  32.671  -5.379  1.00 52.49  ?  512 ASP A C     1 
ATOM   3836 O  O     . ASP A 1 526 ? 43.090  32.376  -4.582  1.00 46.56  ?  512 ASP A O     1 
ATOM   3837 C  CB    . ASP A 1 526 ? 42.438  34.554  -7.021  1.00 60.88  ?  512 ASP A CB    1 
ATOM   3838 C  CG    . ASP A 1 526 ? 43.297  35.329  -6.064  1.00 68.95  ?  512 ASP A CG    1 
ATOM   3839 O  OD1   . ASP A 1 526 ? 44.201  34.750  -5.419  1.00 75.06  ?  512 ASP A OD1   1 
ATOM   3840 O  OD2   . ASP A 1 526 ? 43.027  36.539  -5.938  1.00 83.23  ?  512 ASP A OD2   1 
ATOM   3841 N  N     . VAL A 1 527 ? 40.904  32.686  -5.021  1.00 42.92  ?  513 VAL A N     1 
ATOM   3842 C  CA    . VAL A 1 527 ? 40.510  32.359  -3.652  1.00 42.46  ?  513 VAL A CA    1 
ATOM   3843 C  C     . VAL A 1 527 ? 40.745  30.877  -3.365  1.00 51.78  ?  513 VAL A C     1 
ATOM   3844 O  O     . VAL A 1 527 ? 41.204  30.504  -2.277  1.00 46.77  ?  513 VAL A O     1 
ATOM   3845 C  CB    . VAL A 1 527 ? 39.049  32.779  -3.407  1.00 44.74  ?  513 VAL A CB    1 
ATOM   3846 C  CG1   . VAL A 1 527 ? 38.519  32.175  -2.119  1.00 40.20  ?  513 VAL A CG1   1 
ATOM   3847 C  CG2   . VAL A 1 527 ? 38.947  34.301  -3.363  1.00 41.54  ?  513 VAL A CG2   1 
ATOM   3848 N  N     . LEU A 1 528 ? 40.450  30.010  -4.337  1.00 46.16  ?  514 LEU A N     1 
ATOM   3849 C  CA    . LEU A 1 528 ? 40.728  28.587  -4.161  1.00 43.46  ?  514 LEU A CA    1 
ATOM   3850 C  C     . LEU A 1 528 ? 42.220  28.336  -3.991  1.00 47.27  ?  514 LEU A C     1 
ATOM   3851 O  O     . LEU A 1 528 ? 42.617  27.438  -3.238  1.00 52.17  ?  514 LEU A O     1 
ATOM   3852 C  CB    . LEU A 1 528 ? 40.174  27.795  -5.345  1.00 39.94  ?  514 LEU A CB    1 
ATOM   3853 C  CG    . LEU A 1 528 ? 38.645  27.749  -5.424  1.00 37.98  ?  514 LEU A CG    1 
ATOM   3854 C  CD1   . LEU A 1 528 ? 38.183  27.141  -6.742  1.00 37.25  ?  514 LEU A CD1   1 
ATOM   3855 C  CD2   . LEU A 1 528 ? 38.072  26.983  -4.240  1.00 40.35  ?  514 LEU A CD2   1 
ATOM   3856 N  N     . GLU A 1 529 ? 43.053  29.128  -4.673  1.00 49.56  ?  515 GLU A N     1 
ATOM   3857 C  CA    . GLU A 1 529 ? 44.500  29.073  -4.481  1.00 49.25  ?  515 GLU A CA    1 
ATOM   3858 C  C     . GLU A 1 529 ? 44.867  29.306  -3.018  1.00 48.34  ?  515 GLU A C     1 
ATOM   3859 O  O     . GLU A 1 529 ? 45.671  28.567  -2.438  1.00 49.73  ?  515 GLU A O     1 
ATOM   3860 C  CB    . GLU A 1 529 ? 45.164  30.142  -5.358  1.00 55.31  ?  515 GLU A CB    1 
ATOM   3861 C  CG    . GLU A 1 529 ? 46.009  29.661  -6.525  1.00 72.94  ?  515 GLU A CG    1 
ATOM   3862 C  CD    . GLU A 1 529 ? 46.349  30.791  -7.511  1.00 98.20  ?  515 GLU A CD    1 
ATOM   3863 O  OE1   . GLU A 1 529 ? 46.547  31.953  -7.072  1.00 95.81  ?  515 GLU A OE1   1 
ATOM   3864 O  OE2   . GLU A 1 529 ? 46.416  30.516  -8.731  1.00 94.83  ?  515 GLU A OE2   1 
ATOM   3865 N  N     . LYS A 1 530 ? 44.263  30.326  -2.402  1.00 47.22  ?  516 LYS A N     1 
ATOM   3866 C  CA    . LYS A 1 530 ? 44.606  30.714  -1.036  1.00 53.85  ?  516 LYS A CA    1 
ATOM   3867 C  C     . LYS A 1 530 ? 44.223  29.643  -0.016  1.00 54.42  ?  516 LYS A C     1 
ATOM   3868 O  O     . LYS A 1 530 ? 44.948  29.433  0.964   1.00 54.77  ?  516 LYS A O     1 
ATOM   3869 C  CB    . LYS A 1 530 ? 43.938  32.051  -0.690  1.00 46.82  ?  516 LYS A CB    1 
ATOM   3870 C  CG    . LYS A 1 530 ? 44.872  33.252  -0.801  1.00 62.45  ?  516 LYS A CG    1 
ATOM   3871 C  CD    . LYS A 1 530 ? 44.177  34.497  -1.347  1.00 53.25  ?  516 LYS A CD    1 
ATOM   3872 C  CE    . LYS A 1 530 ? 45.217  35.556  -1.731  1.00 64.87  ?  516 LYS A CE    1 
ATOM   3873 N  NZ    . LYS A 1 530 ? 44.978  36.907  -1.135  1.00 61.23  ?  516 LYS A NZ    1 
ATOM   3874 N  N     . VAL A 1 531 ? 43.088  28.963  -0.218  1.00 48.93  ?  517 VAL A N     1 
ATOM   3875 C  CA    . VAL A 1 531 ? 42.544  28.039  0.778   1.00 42.75  ?  517 VAL A CA    1 
ATOM   3876 C  C     . VAL A 1 531 ? 42.985  26.598  0.536   1.00 49.98  ?  517 VAL A C     1 
ATOM   3877 O  O     . VAL A 1 531 ? 42.404  25.666  1.107   1.00 77.28  ?  517 VAL A O     1 
ATOM   3878 C  CB    . VAL A 1 531 ? 41.000  28.107  0.811   1.00 60.23  ?  517 VAL A CB    1 
ATOM   3879 C  CG1   . VAL A 1 531 ? 40.527  29.529  0.928   1.00 49.85  ?  517 VAL A CG1   1 
ATOM   3880 C  CG2   . VAL A 1 531 ? 40.388  27.448  -0.423  1.00 43.19  ?  517 VAL A CG2   1 
ATOM   3881 N  N     . ALA A 1 532 ? 44.015  26.398  -0.292  1.00 48.83  ?  518 ALA A N     1 
ATOM   3882 C  CA    . ALA A 1 532 ? 44.305  25.066  -0.827  1.00 56.38  ?  518 ALA A CA    1 
ATOM   3883 C  C     . ALA A 1 532 ? 44.492  24.013  0.265   1.00 85.29  ?  518 ALA A C     1 
ATOM   3884 O  O     . ALA A 1 532 ? 43.966  22.897  0.155   1.00 71.07  ?  518 ALA A O     1 
ATOM   3885 C  CB    . ALA A 1 532 ? 45.544  25.121  -1.718  1.00 62.50  ?  518 ALA A CB    1 
ATOM   3886 N  N     . HIS A 1 533 ? 45.236  24.335  1.322   1.00 80.99  ?  519 HIS A N     1 
ATOM   3887 C  CA    . HIS A 1 533 ? 45.607  23.342  2.322   1.00 86.77  ?  519 HIS A CA    1 
ATOM   3888 C  C     . HIS A 1 533 ? 44.741  23.397  3.578   1.00 79.99  ?  519 HIS A C     1 
ATOM   3889 O  O     . HIS A 1 533 ? 45.187  22.948  4.641   1.00 80.41  ?  519 HIS A O     1 
ATOM   3890 C  CB    . HIS A 1 533 ? 47.089  23.474  2.669   1.00 76.60  ?  519 HIS A CB    1 
ATOM   3891 C  CG    . HIS A 1 533 ? 47.989  22.911  1.615   1.00 90.90  ?  519 HIS A CG    1 
ATOM   3892 N  ND1   . HIS A 1 533 ? 48.477  23.666  0.570   1.00 95.16  ?  519 HIS A ND1   1 
ATOM   3893 C  CD2   . HIS A 1 533 ? 48.463  21.657  1.427   1.00 93.62  ?  519 HIS A CD2   1 
ATOM   3894 C  CE1   . HIS A 1 533 ? 49.227  22.905  -0.207  1.00 93.11  ?  519 HIS A CE1   1 
ATOM   3895 N  NE2   . HIS A 1 533 ? 49.236  21.682  0.291   1.00 101.00 ?  519 HIS A NE2   1 
ATOM   3896 N  N     . HIS A 1 534 ? 43.519  23.922  3.467   1.00 75.03  ?  520 HIS A N     1 
ATOM   3897 C  CA    . HIS A 1 534 ? 42.513  23.931  4.535   1.00 70.36  ?  520 HIS A CA    1 
ATOM   3898 C  C     . HIS A 1 534 ? 43.158  24.236  5.882   1.00 76.92  ?  520 HIS A C     1 
ATOM   3899 O  O     . HIS A 1 534 ? 43.023  23.506  6.866   1.00 70.68  ?  520 HIS A O     1 
ATOM   3900 C  CB    . HIS A 1 534 ? 41.717  22.625  4.589   1.00 59.14  ?  520 HIS A CB    1 
ATOM   3901 C  CG    . HIS A 1 534 ? 42.561  21.392  4.668   1.00 55.22  ?  520 HIS A CG    1 
ATOM   3902 N  ND1   . HIS A 1 534 ? 43.148  20.824  3.558   1.00 75.60  ?  520 HIS A ND1   1 
ATOM   3903 C  CD2   . HIS A 1 534 ? 42.914  20.615  5.720   1.00 66.01  ?  520 HIS A CD2   1 
ATOM   3904 C  CE1   . HIS A 1 534 ? 43.834  19.755  3.923   1.00 67.24  ?  520 HIS A CE1   1 
ATOM   3905 N  NE2   . HIS A 1 534 ? 43.708  19.605  5.229   1.00 74.36  ?  520 HIS A NE2   1 
ATOM   3906 N  N     . GLU A 1 535 ? 43.770  25.389  5.928   1.00 78.34  ?  521 GLU A N     1 
ATOM   3907 C  CA    . GLU A 1 535 ? 44.433  25.942  7.069   1.00 55.55  ?  521 GLU A CA    1 
ATOM   3908 C  C     . GLU A 1 535 ? 43.397  26.328  8.118   1.00 55.52  ?  521 GLU A C     1 
ATOM   3909 O  O     . GLU A 1 535 ? 43.641  26.224  9.300   1.00 57.71  ?  521 GLU A O     1 
ATOM   3910 C  CB    . GLU A 1 535 ? 45.198  27.163  6.577   1.00 63.12  ?  521 GLU A CB    1 
ATOM   3911 C  CG    . GLU A 1 535 ? 44.883  27.597  5.140   1.00 62.40  ?  521 GLU A CG    1 
ATOM   3912 C  CD    . GLU A 1 535 ? 45.826  28.600  4.570   1.00 87.09  ?  521 GLU A CD    1 
ATOM   3913 O  OE1   . GLU A 1 535 ? 45.557  29.815  4.721   1.00 77.41  ?  521 GLU A OE1   1 
ATOM   3914 O  OE2   . GLU A 1 535 ? 46.810  28.157  3.936   1.00 87.53  ?  521 GLU A OE2   1 
ATOM   3915 N  N     . ARG A 1 536 ? 42.249  26.801  7.641   1.00 49.37  ?  522 ARG A N     1 
ATOM   3916 C  CA    . ARG A 1 536 ? 41.120  27.203  8.461   1.00 41.85  ?  522 ARG A CA    1 
ATOM   3917 C  C     . ARG A 1 536 ? 39.791  26.964  7.737   1.00 38.61  ?  522 ARG A C     1 
ATOM   3918 O  O     . ARG A 1 536 ? 39.775  26.679  6.569   1.00 41.26  ?  522 ARG A O     1 
ATOM   3919 C  CB    . ARG A 1 536 ? 41.278  28.653  8.949   1.00 52.15  ?  522 ARG A CB    1 
ATOM   3920 C  CG    . ARG A 1 536 ? 41.359  29.741  7.890   1.00 76.63  ?  522 ARG A CG    1 
ATOM   3921 C  CD    . ARG A 1 536 ? 41.602  31.163  8.463   1.00 85.14  ?  522 ARG A CD    1 
ATOM   3922 N  NE    . ARG A 1 536 ? 42.854  31.283  9.175   1.00 100.55 ?  522 ARG A NE    1 
ATOM   3923 C  CZ    . ARG A 1 536 ? 43.021  31.874  10.356  1.00 91.75  ?  522 ARG A CZ    1 
ATOM   3924 N  NH1   . ARG A 1 536 ? 42.016  32.461  10.975  1.00 98.89  ?  522 ARG A NH1   1 
ATOM   3925 N  NH2   . ARG A 1 536 ? 44.217  31.884  10.923  1.00 88.88  ?  522 ARG A NH2   1 
ATOM   3926 N  N     . LEU A 1 537 ? 38.672  27.033  8.437   1.00 37.06  ?  523 LEU A N     1 
ATOM   3927 C  CA    . LEU A 1 537 ? 37.382  26.868  7.770   1.00 34.98  ?  523 LEU A CA    1 
ATOM   3928 C  C     . LEU A 1 537 ? 37.235  27.972  6.741   1.00 40.01  ?  523 LEU A C     1 
ATOM   3929 O  O     . LEU A 1 537 ? 37.484  29.094  7.048   1.00 35.74  ?  523 LEU A O     1 
ATOM   3930 C  CB    . LEU A 1 537 ? 36.245  26.921  8.779   1.00 33.77  ?  523 LEU A CB    1 
ATOM   3931 C  CG    . LEU A 1 537 ? 34.821  26.794  8.262   1.00 31.85  ?  523 LEU A CG    1 
ATOM   3932 C  CD1   . LEU A 1 537 ? 33.980  26.018  9.226   1.00 31.38  ?  523 LEU A CD1   1 
ATOM   3933 C  CD2   . LEU A 1 537 ? 34.193  28.129  7.976   1.00 31.62  ?  523 LEU A CD2   1 
ATOM   3934 N  N     . SER A 1 538 ? 36.813  27.645  5.535   1.00 39.52  ?  524 SER A N     1 
ATOM   3935 C  CA    . SER A 1 538 ? 36.693  28.597  4.443   1.00 33.42  ?  524 SER A CA    1 
ATOM   3936 C  C     . SER A 1 538 ? 35.255  28.611  3.964   1.00 34.52  ?  524 SER A C     1 
ATOM   3937 O  O     . SER A 1 538 ? 34.687  27.557  3.656   1.00 36.58  ?  524 SER A O     1 
ATOM   3938 C  CB    . SER A 1 538 ? 37.628  28.236  3.289   1.00 34.59  ?  524 SER A CB    1 
ATOM   3939 O  OG    . SER A 1 538 ? 38.968  28.158  3.726   1.00 36.60  ?  524 SER A OG    1 
ATOM   3940 N  N     . LEU A 1 539 ? 34.684  29.803  3.872   1.00 39.47  ?  525 LEU A N     1 
ATOM   3941 C  CA    . LEU A 1 539 ? 33.329  29.998  3.379   1.00 31.98  ?  525 LEU A CA    1 
ATOM   3942 C  C     . LEU A 1 539 ? 33.437  30.914  2.171   1.00 38.39  ?  525 LEU A C     1 
ATOM   3943 O  O     . LEU A 1 539 ? 33.796  32.089  2.306   1.00 34.38  ?  525 LEU A O     1 
ATOM   3944 C  CB    . LEU A 1 539 ? 32.427  30.587  4.464   1.00 38.95  ?  525 LEU A CB    1 
ATOM   3945 C  CG    . LEU A 1 539 ? 30.912  30.428  4.302   1.00 46.85  ?  525 LEU A CG    1 
ATOM   3946 C  CD1   . LEU A 1 539 ? 30.227  30.318  5.655   1.00 43.57  ?  525 LEU A CD1   1 
ATOM   3947 C  CD2   . LEU A 1 539 ? 30.333  31.594  3.516   1.00 42.64  ?  525 LEU A CD2   1 
ATOM   3948 N  N     . ILE A 1 540 ? 33.167  30.367  0.992   1.00 37.72  ?  526 ILE A N     1 
ATOM   3949 C  CA    . ILE A 1 540 ? 33.246  31.110  -0.257  1.00 33.37  ?  526 ILE A CA    1 
ATOM   3950 C  C     . ILE A 1 540 ? 31.825  31.309  -0.765  1.00 38.34  ?  526 ILE A C     1 
ATOM   3951 O  O     . ILE A 1 540 ? 31.146  30.346  -1.141  1.00 32.63  ?  526 ILE A O     1 
ATOM   3952 C  CB    . ILE A 1 540 ? 34.120  30.392  -1.290  1.00 31.18  ?  526 ILE A CB    1 
ATOM   3953 C  CG1   . ILE A 1 540 ? 35.484  30.057  -0.672  1.00 32.40  ?  526 ILE A CG1   1 
ATOM   3954 C  CG2   . ILE A 1 540 ? 34.275  31.253  -2.532  1.00 33.68  ?  526 ILE A CG2   1 
ATOM   3955 C  CD1   . ILE A 1 540 ? 36.390  29.209  -1.560  1.00 33.48  ?  526 ILE A CD1   1 
ATOM   3956 N  N     . GLU A 1 541 ? 31.369  32.557  -0.771  1.00 32.90  ?  527 GLU A N     1 
ATOM   3957 C  CA    . GLU A 1 541 ? 30.050  32.892  -1.295  1.00 33.68  ?  527 GLU A CA    1 
ATOM   3958 C  C     . GLU A 1 541 ? 30.187  33.126  -2.795  1.00 35.15  ?  527 GLU A C     1 
ATOM   3959 O  O     . GLU A 1 541 ? 30.767  34.130  -3.224  1.00 40.32  ?  527 GLU A O     1 
ATOM   3960 C  CB    . GLU A 1 541 ? 29.485  34.118  -0.587  1.00 35.19  ?  527 GLU A CB    1 
ATOM   3961 C  CG    . GLU A 1 541 ? 28.235  34.661  -1.225  1.00 36.85  ?  527 GLU A CG    1 
ATOM   3962 C  CD    . GLU A 1 541 ? 27.709  35.895  -0.523  1.00 39.08  ?  527 GLU A CD    1 
ATOM   3963 O  OE1   . GLU A 1 541 ? 28.457  36.509  0.270   1.00 36.94  ?  527 GLU A OE1   1 
ATOM   3964 O  OE2   . GLU A 1 541 ? 26.539  36.252  -0.771  1.00 43.79  ?  527 GLU A OE2   1 
ATOM   3965 N  N     . VAL A 1 542 ? 29.683  32.187  -3.590  1.00 36.47  ?  528 VAL A N     1 
ATOM   3966 C  CA    . VAL A 1 542 ? 29.821  32.216  -5.043  1.00 33.39  ?  528 VAL A CA    1 
ATOM   3967 C  C     . VAL A 1 542 ? 28.562  32.839  -5.632  1.00 34.94  ?  528 VAL A C     1 
ATOM   3968 O  O     . VAL A 1 542 ? 27.461  32.296  -5.482  1.00 33.37  ?  528 VAL A O     1 
ATOM   3969 C  CB    . VAL A 1 542 ? 30.052  30.804  -5.606  1.00 32.97  ?  528 VAL A CB    1 
ATOM   3970 C  CG1   . VAL A 1 542 ? 30.360  30.869  -7.095  1.00 33.96  ?  528 VAL A CG1   1 
ATOM   3971 C  CG2   . VAL A 1 542 ? 31.173  30.103  -4.843  1.00 29.15  ?  528 VAL A CG2   1 
ATOM   3972 N  N     . MET A 1 543 ? 28.716  33.968  -6.319  1.00 34.21  ?  529 MET A N     1 
ATOM   3973 C  CA    . MET A 1 543 ? 27.580  34.672  -6.905  1.00 38.43  ?  529 MET A CA    1 
ATOM   3974 C  C     . MET A 1 543 ? 27.338  34.173  -8.325  1.00 37.27  ?  529 MET A C     1 
ATOM   3975 O  O     . MET A 1 543 ? 28.201  34.324  -9.198  1.00 42.67  ?  529 MET A O     1 
ATOM   3976 C  CB    . MET A 1 543 ? 27.811  36.185  -6.888  1.00 31.90  ?  529 MET A CB    1 
ATOM   3977 C  CG    . MET A 1 543 ? 28.292  36.695  -5.543  1.00 43.17  ?  529 MET A CG    1 
ATOM   3978 S  SD    . MET A 1 543 ? 27.019  36.830  -4.269  1.00 59.81  ?  529 MET A SD    1 
ATOM   3979 C  CE    . MET A 1 543 ? 25.513  37.000  -5.238  1.00 63.52  ?  529 MET A CE    1 
ATOM   3980 N  N     . LEU A 1 544 ? 26.161  33.599  -8.556  1.00 34.79  ?  530 LEU A N     1 
ATOM   3981 C  CA    . LEU A 1 544 ? 25.797  33.007  -9.833  1.00 36.53  ?  530 LEU A CA    1 
ATOM   3982 C  C     . LEU A 1 544 ? 24.445  33.538  -10.290 1.00 43.53  ?  530 LEU A C     1 
ATOM   3983 O  O     . LEU A 1 544 ? 23.632  33.971  -9.465  1.00 35.07  ?  530 LEU A O     1 
ATOM   3984 C  CB    . LEU A 1 544 ? 25.750  31.476  -9.728  1.00 29.28  ?  530 LEU A CB    1 
ATOM   3985 C  CG    . LEU A 1 544 ? 27.105  30.796  -9.490  1.00 32.89  ?  530 LEU A CG    1 
ATOM   3986 C  CD1   . LEU A 1 544 ? 26.935  29.434  -8.836  1.00 28.06  ?  530 LEU A CD1   1 
ATOM   3987 C  CD2   . LEU A 1 544 ? 27.890  30.671  -10.790 1.00 35.06  ?  530 LEU A CD2   1 
ATOM   3988 N  N     . PRO A 1 545 ? 24.189  33.547  -11.600 1.00 38.69  ?  531 PRO A N     1 
ATOM   3989 C  CA    . PRO A 1 545 ? 22.921  34.100  -12.094 1.00 32.18  ?  531 PRO A CA    1 
ATOM   3990 C  C     . PRO A 1 545 ? 21.724  33.272  -11.647 1.00 38.63  ?  531 PRO A C     1 
ATOM   3991 O  O     . PRO A 1 545 ? 21.810  32.054  -11.460 1.00 34.60  ?  531 PRO A O     1 
ATOM   3992 C  CB    . PRO A 1 545 ? 23.085  34.073  -13.619 1.00 39.22  ?  531 PRO A CB    1 
ATOM   3993 C  CG    . PRO A 1 545 ? 24.575  33.998  -13.847 1.00 42.65  ?  531 PRO A CG    1 
ATOM   3994 C  CD    . PRO A 1 545 ? 25.096  33.177  -12.701 1.00 39.62  ?  531 PRO A CD    1 
ATOM   3995 N  N     . LYS A 1 546 ? 20.587  33.960  -11.513 1.00 37.60  ?  532 LYS A N     1 
ATOM   3996 C  CA    . LYS A 1 546 ? 19.367  33.342  -11.006 1.00 40.99  ?  532 LYS A CA    1 
ATOM   3997 C  C     . LYS A 1 546 ? 18.897  32.204  -11.904 1.00 33.51  ?  532 LYS A C     1 
ATOM   3998 O  O     . LYS A 1 546 ? 18.394  31.190  -11.414 1.00 34.41  ?  532 LYS A O     1 
ATOM   3999 C  CB    . LYS A 1 546 ? 18.272  34.406  -10.885 1.00 46.28  ?  532 LYS A CB    1 
ATOM   4000 C  CG    . LYS A 1 546 ? 17.768  34.675  -9.474  1.00 45.81  ?  532 LYS A CG    1 
ATOM   4001 C  CD    . LYS A 1 546 ? 16.659  35.735  -9.486  1.00 42.07  ?  532 LYS A CD    1 
ATOM   4002 C  CE    . LYS A 1 546 ? 16.680  36.580  -8.223  1.00 40.66  ?  532 LYS A CE    1 
ATOM   4003 N  NZ    . LYS A 1 546 ? 15.489  37.475  -8.113  1.00 54.53  ?  532 LYS A NZ    1 
ATOM   4004 N  N     . ALA A 1 547 ? 19.055  32.348  -13.217 1.00 32.38  ?  533 ALA A N     1 
ATOM   4005 C  CA    . ALA A 1 547 ? 18.539  31.372  -14.163 1.00 38.98  ?  533 ALA A CA    1 
ATOM   4006 C  C     . ALA A 1 547 ? 19.593  30.397  -14.673 1.00 41.39  ?  533 ALA A C     1 
ATOM   4007 O  O     . ALA A 1 547 ? 19.273  29.550  -15.512 1.00 43.95  ?  533 ALA A O     1 
ATOM   4008 C  CB    . ALA A 1 547 ? 17.898  32.089  -15.354 1.00 34.17  ?  533 ALA A CB    1 
ATOM   4009 N  N     . ASP A 1 548 ? 20.831  30.482  -14.192 1.00 39.30  ?  534 ASP A N     1 
ATOM   4010 C  CA    . ASP A 1 548 ? 21.904  29.655  -14.731 1.00 39.06  ?  534 ASP A CA    1 
ATOM   4011 C  C     . ASP A 1 548 ? 21.796  28.217  -14.236 1.00 36.42  ?  534 ASP A C     1 
ATOM   4012 O  O     . ASP A 1 548 ? 21.696  27.973  -13.029 1.00 33.28  ?  534 ASP A O     1 
ATOM   4013 C  CB    . ASP A 1 548 ? 23.260  30.244  -14.353 1.00 45.75  ?  534 ASP A CB    1 
ATOM   4014 C  CG    . ASP A 1 548 ? 24.373  29.722  -15.220 1.00 42.06  ?  534 ASP A CG    1 
ATOM   4015 O  OD1   . ASP A 1 548 ? 24.098  28.886  -16.108 1.00 49.35  ?  534 ASP A OD1   1 
ATOM   4016 O  OD2   . ASP A 1 548 ? 25.524  30.152  -15.018 1.00 52.15  ?  534 ASP A OD2   1 
ATOM   4017 N  N     . ILE A 1 549 ? 21.895  27.268  -15.164 1.00 35.40  ?  535 ILE A N     1 
ATOM   4018 C  CA    . ILE A 1 549 ? 21.574  25.866  -14.900 1.00 40.07  ?  535 ILE A CA    1 
ATOM   4019 C  C     . ILE A 1 549 ? 22.710  24.971  -15.390 1.00 34.80  ?  535 ILE A C     1 
ATOM   4020 O  O     . ILE A 1 549 ? 23.239  25.200  -16.486 1.00 41.09  ?  535 ILE A O     1 
ATOM   4021 C  CB    . ILE A 1 549 ? 20.239  25.493  -15.567 1.00 37.79  ?  535 ILE A CB    1 
ATOM   4022 C  CG1   . ILE A 1 549 ? 19.083  26.060  -14.752 1.00 47.73  ?  535 ILE A CG1   1 
ATOM   4023 C  CG2   . ILE A 1 549 ? 20.095  24.003  -15.756 1.00 54.03  ?  535 ILE A CG2   1 
ATOM   4024 C  CD1   . ILE A 1 549 ? 19.225  25.847  -13.277 1.00 41.08  ?  535 ILE A CD1   1 
ATOM   4025 N  N     . PRO A 1 550 ? 23.103  23.941  -14.640 1.00 33.25  ?  536 PRO A N     1 
ATOM   4026 C  CA    . PRO A 1 550 ? 24.096  22.966  -15.152 1.00 35.92  ?  536 PRO A CA    1 
ATOM   4027 C  C     . PRO A 1 550 ? 23.485  22.052  -16.201 1.00 51.26  ?  536 PRO A C     1 
ATOM   4028 O  O     . PRO A 1 550 ? 22.260  21.854  -16.226 1.00 46.40  ?  536 PRO A O     1 
ATOM   4029 C  CB    . PRO A 1 550 ? 24.508  22.166  -13.903 1.00 37.24  ?  536 PRO A CB    1 
ATOM   4030 C  CG    . PRO A 1 550 ? 23.666  22.650  -12.772 1.00 38.00  ?  536 PRO A CG    1 
ATOM   4031 C  CD    . PRO A 1 550 ? 22.647  23.629  -13.275 1.00 35.50  ?  536 PRO A CD    1 
ATOM   4032 N  N     . PRO A 1 551 ? 24.313  21.441  -17.059 1.00 53.90  ?  537 PRO A N     1 
ATOM   4033 C  CA    . PRO A 1 551 ? 23.764  20.666  -18.193 1.00 36.61  ?  537 PRO A CA    1 
ATOM   4034 C  C     . PRO A 1 551 ? 22.823  19.535  -17.809 1.00 42.74  ?  537 PRO A C     1 
ATOM   4035 O  O     . PRO A 1 551 ? 21.838  19.305  -18.522 1.00 48.85  ?  537 PRO A O     1 
ATOM   4036 C  CB    . PRO A 1 551 ? 25.025  20.126  -18.883 1.00 46.69  ?  537 PRO A CB    1 
ATOM   4037 C  CG    . PRO A 1 551 ? 26.115  21.068  -18.492 1.00 48.87  ?  537 PRO A CG    1 
ATOM   4038 C  CD    . PRO A 1 551 ? 25.780  21.564  -17.118 1.00 49.52  ?  537 PRO A CD    1 
ATOM   4039 N  N     . LEU A 1 552 ? 23.085  18.821  -16.710 1.00 38.42  ?  538 LEU A N     1 
ATOM   4040 C  CA    . LEU A 1 552 ? 22.229  17.692  -16.354 1.00 45.94  ?  538 LEU A CA    1 
ATOM   4041 C  C     . LEU A 1 552 ? 20.817  18.162  -16.041 1.00 51.70  ?  538 LEU A C     1 
ATOM   4042 O  O     . LEU A 1 552 ? 19.836  17.516  -16.427 1.00 47.82  ?  538 LEU A O     1 
ATOM   4043 C  CB    . LEU A 1 552 ? 22.809  16.924  -15.160 1.00 34.17  ?  538 LEU A CB    1 
ATOM   4044 C  CG    . LEU A 1 552 ? 21.859  15.915  -14.492 1.00 38.92  ?  538 LEU A CG    1 
ATOM   4045 C  CD1   . LEU A 1 552 ? 21.498  14.805  -15.457 1.00 33.64  ?  538 LEU A CD1   1 
ATOM   4046 C  CD2   . LEU A 1 552 ? 22.424  15.326  -13.200 1.00 36.95  ?  538 LEU A CD2   1 
ATOM   4047 N  N     . LEU A 1 553 ? 20.695  19.294  -15.348 1.00 50.15  ?  539 LEU A N     1 
ATOM   4048 C  CA    . LEU A 1 553 ? 19.376  19.770  -14.959 1.00 50.65  ?  539 LEU A CA    1 
ATOM   4049 C  C     . LEU A 1 553 ? 18.588  20.284  -16.157 1.00 46.41  ?  539 LEU A C     1 
ATOM   4050 O  O     . LEU A 1 553 ? 17.358  20.184  -16.175 1.00 48.95  ?  539 LEU A O     1 
ATOM   4051 C  CB    . LEU A 1 553 ? 19.514  20.837  -13.880 1.00 38.46  ?  539 LEU A CB    1 
ATOM   4052 C  CG    . LEU A 1 553 ? 18.286  21.662  -13.529 1.00 55.85  ?  539 LEU A CG    1 
ATOM   4053 C  CD1   . LEU A 1 553 ? 17.148  20.762  -13.047 1.00 44.57  ?  539 LEU A CD1   1 
ATOM   4054 C  CD2   . LEU A 1 553 ? 18.694  22.618  -12.446 1.00 42.76  ?  539 LEU A CD2   1 
ATOM   4055 N  N     . GLY A 1 554 ? 19.273  20.667  -17.203 1.00 45.10  ?  540 GLY A N     1 
ATOM   4056 C  CA    . GLY A 1 554 ? 18.584  21.089  -18.382 1.00 42.11  ?  540 GLY A CA    1 
ATOM   4057 C  C     . GLY A 1 554 ? 17.913  19.891  -19.006 1.00 56.70  ?  540 GLY A C     1 
ATOM   4058 O  O     . GLY A 1 554 ? 16.815  19.978  -19.476 1.00 67.40  ?  540 GLY A O     1 
ATOM   4059 N  N     . ALA A 1 555 ? 18.585  18.759  -19.023 1.00 50.77  ?  541 ALA A N     1 
ATOM   4060 C  CA    . ALA A 1 555 ? 18.002  17.562  -19.593 1.00 56.74  ?  541 ALA A CA    1 
ATOM   4061 C  C     . ALA A 1 555 ? 16.851  17.067  -18.736 1.00 54.76  ?  541 ALA A C     1 
ATOM   4062 O  O     . ALA A 1 555 ? 15.854  16.595  -19.223 1.00 62.39  ?  541 ALA A O     1 
ATOM   4063 C  CB    . ALA A 1 555 ? 19.047  16.497  -19.727 1.00 43.32  ?  541 ALA A CB    1 
ATOM   4064 N  N     . ILE A 1 556 ? 16.999  17.164  -17.443 1.00 50.29  ?  542 ILE A N     1 
ATOM   4065 C  CA    . ILE A 1 556 ? 15.942  16.732  -16.586 1.00 54.58  ?  542 ILE A CA    1 
ATOM   4066 C  C     . ILE A 1 556 ? 14.675  17.530  -16.815 1.00 65.66  ?  542 ILE A C     1 
ATOM   4067 O  O     . ILE A 1 556 ? 13.618  16.965  -16.917 1.00 67.61  ?  542 ILE A O     1 
ATOM   4068 C  CB    . ILE A 1 556 ? 16.343  16.824  -15.133 1.00 57.57  ?  542 ILE A CB    1 
ATOM   4069 C  CG1   . ILE A 1 556 ? 17.375  15.762  -14.816 1.00 41.91  ?  542 ILE A CG1   1 
ATOM   4070 C  CG2   . ILE A 1 556 ? 15.121  16.720  -14.252 1.00 53.27  ?  542 ILE A CG2   1 
ATOM   4071 C  CD1   . ILE A 1 556 ? 17.585  15.594  -13.357 1.00 44.71  ?  542 ILE A CD1   1 
ATOM   4072 N  N     . THR A 1 557 ? 14.780  18.844  -16.932 1.00 54.22  ?  543 THR A N     1 
ATOM   4073 C  CA    . THR A 1 557 ? 13.607  19.662  -17.157 1.00 63.31  ?  543 THR A CA    1 
ATOM   4074 C  C     . THR A 1 557 ? 12.997  19.355  -18.507 1.00 63.11  ?  543 THR A C     1 
ATOM   4075 O  O     . THR A 1 557 ? 11.798  19.337  -18.642 1.00 65.89  ?  543 THR A O     1 
ATOM   4076 C  CB    . THR A 1 557 ? 13.859  21.174  -16.961 1.00 52.36  ?  543 THR A CB    1 
ATOM   4077 O  OG1   . THR A 1 557 ? 14.846  21.643  -17.865 1.00 57.66  ?  543 THR A OG1   1 
ATOM   4078 C  CG2   . THR A 1 557 ? 14.311  21.450  -15.575 1.00 48.33  ?  543 THR A CG2   1 
ATOM   4079 N  N     . LYS A 1 558 ? 13.817  19.099  -19.511 1.00 62.84  ?  544 LYS A N     1 
ATOM   4080 C  CA    . LYS A 1 558 ? 13.291  18.712  -20.817 1.00 76.37  ?  544 LYS A CA    1 
ATOM   4081 C  C     . LYS A 1 558 ? 12.490  17.417  -20.731 1.00 69.46  ?  544 LYS A C     1 
ATOM   4082 O  O     . LYS A 1 558 ? 11.459  17.309  -21.325 1.00 65.39  ?  544 LYS A O     1 
ATOM   4083 C  CB    . LYS A 1 558 ? 14.400  18.601  -21.848 1.00 69.58  ?  544 LYS A CB    1 
ATOM   4084 C  CG    . LYS A 1 558 ? 14.860  19.960  -22.347 1.00 78.31  ?  544 LYS A CG    1 
ATOM   4085 C  CD    . LYS A 1 558 ? 15.022  20.024  -23.861 1.00 83.96  ?  544 LYS A CD    1 
ATOM   4086 C  CE    . LYS A 1 558 ? 14.799  21.448  -24.368 1.00 84.97  ?  544 LYS A CE    1 
ATOM   4087 N  NZ    . LYS A 1 558 ? 14.083  21.553  -25.676 1.00 91.44  ?  544 LYS A NZ    1 
ATOM   4088 N  N     . ALA A 1 559 ? 12.960  16.454  -19.944 1.00 70.43  ?  545 ALA A N     1 
ATOM   4089 C  CA    . ALA A 1 559 ? 12.270  15.184  -19.759 1.00 72.00  ?  545 ALA A CA    1 
ATOM   4090 C  C     . ALA A 1 559 ? 10.947  15.382  -19.054 1.00 69.14  ?  545 ALA A C     1 
ATOM   4091 O  O     . ALA A 1 559 ? 9.979   14.748  -19.382 1.00 71.86  ?  545 ALA A O     1 
ATOM   4092 C  CB    . ALA A 1 559 ? 13.133  14.192  -19.011 1.00 58.12  ?  545 ALA A CB    1 
ATOM   4093 N  N     . LEU A 1 560 ? 10.892  16.332  -18.131 1.00 78.15  ?  546 LEU A N     1 
ATOM   4094 C  CA    . LEU A 1 560 ? 9.677   16.682  -17.401 1.00 78.96  ?  546 LEU A CA    1 
ATOM   4095 C  C     . LEU A 1 560 ? 8.527   17.101  -18.328 1.00 82.07  ?  546 LEU A C     1 
ATOM   4096 O  O     . LEU A 1 560 ? 7.384   16.866  -18.025 1.00 80.03  ?  546 LEU A O     1 
ATOM   4097 C  CB    . LEU A 1 560 ? 9.953   17.752  -16.350 1.00 68.89  ?  546 LEU A CB    1 
ATOM   4098 C  CG    . LEU A 1 560 ? 9.591   17.369  -14.909 1.00 75.29  ?  546 LEU A CG    1 
ATOM   4099 C  CD1   . LEU A 1 560 ? 9.321   15.883  -14.780 1.00 74.96  ?  546 LEU A CD1   1 
ATOM   4100 C  CD2   . LEU A 1 560 ? 10.638  17.782  -13.904 1.00 78.99  ?  546 LEU A CD2   1 
ATOM   4101 N  N     . GLU A 1 561 ? 8.816   17.752  -19.444 1.00 85.44  ?  547 GLU A N     1 
ATOM   4102 C  CA    . GLU A 1 561 ? 7.802   18.079  -20.409 1.00 91.97  ?  547 GLU A CA    1 
ATOM   4103 C  C     . GLU A 1 561 ? 7.321   16.759  -21.043 1.00 91.80  ?  547 GLU A C     1 
ATOM   4104 O  O     . GLU A 1 561 ? 7.888   16.287  -22.013 1.00 88.09  ?  547 GLU A O     1 
ATOM   4105 C  CB    . GLU A 1 561 ? 8.395   19.002  -21.458 1.00 91.12  ?  547 GLU A CB    1 
ATOM   4106 C  CG    . GLU A 1 561 ? 7.429   19.314  -22.568 1.00 100.18 ?  547 GLU A CG    1 
ATOM   4107 C  CD    . GLU A 1 561 ? 6.897   20.732  -22.515 1.00 107.27 ?  547 GLU A CD    1 
ATOM   4108 O  OE1   . GLU A 1 561 ? 7.179   21.442  -21.535 1.00 102.38 ?  547 GLU A OE1   1 
ATOM   4109 O  OE2   . GLU A 1 561 ? 6.179   21.129  -23.465 1.00 105.95 ?  547 GLU A OE2   1 
ATOM   4110 N  N     . ALA A 1 562 ? 6.283   16.164  -20.458 1.00 90.20  ?  548 ALA A N     1 
ATOM   4111 C  CA    . ALA A 1 562 ? 5.741   14.896  -20.892 1.00 88.77  ?  548 ALA A CA    1 
ATOM   4112 C  C     . ALA A 1 562 ? 4.270   14.757  -20.478 1.00 91.09  ?  548 ALA A C     1 
ATOM   4113 O  O     . ALA A 1 562 ? 3.925   13.943  -19.616 1.00 88.63  ?  548 ALA A O     1 
ATOM   4114 C  CB    . ALA A 1 562 ? 6.557   13.767  -20.304 1.00 72.33  ?  548 ALA A CB    1 
ATOM   4115 N  N     . THR B 1 17  ? -7.177  29.202  -15.985 1.00 87.92  ?  3   THR B N     1 
ATOM   4116 C  CA    . THR B 1 17  ? -7.202  28.998  -14.539 1.00 79.59  ?  3   THR B CA    1 
ATOM   4117 C  C     . THR B 1 17  ? -8.609  28.703  -13.996 1.00 76.71  ?  3   THR B C     1 
ATOM   4118 O  O     . THR B 1 17  ? -9.115  29.449  -13.154 1.00 76.21  ?  3   THR B O     1 
ATOM   4119 C  CB    . THR B 1 17  ? -6.635  30.232  -13.801 1.00 94.70  ?  3   THR B CB    1 
ATOM   4120 O  OG1   . THR B 1 17  ? -7.595  31.297  -13.831 1.00 83.41  ?  3   THR B OG1   1 
ATOM   4121 C  CG2   . THR B 1 17  ? -5.339  30.703  -14.456 1.00 78.04  ?  3   THR B CG2   1 
ATOM   4122 N  N     . PRO B 1 18  ? -9.244  27.633  -14.476 1.00 72.37  ?  4   PRO B N     1 
ATOM   4123 C  CA    . PRO B 1 18  ? -10.570 27.276  -13.958 1.00 60.17  ?  4   PRO B CA    1 
ATOM   4124 C  C     . PRO B 1 18  ? -10.500 26.868  -12.495 1.00 59.62  ?  4   PRO B C     1 
ATOM   4125 O  O     . PRO B 1 18  ? -9.507  26.303  -12.029 1.00 55.04  ?  4   PRO B O     1 
ATOM   4126 C  CB    . PRO B 1 18  ? -10.997 26.096  -14.842 1.00 62.40  ?  4   PRO B CB    1 
ATOM   4127 C  CG    . PRO B 1 18  ? -10.049 26.108  -16.009 1.00 71.48  ?  4   PRO B CG    1 
ATOM   4128 C  CD    . PRO B 1 18  ? -8.773  26.646  -15.460 1.00 67.67  ?  4   PRO B CD    1 
ATOM   4129 N  N     . TYR B 1 19  ? -11.582 27.154  -11.773 1.00 43.32  ?  5   TYR B N     1 
ATOM   4130 C  CA    . TYR B 1 19  ? -11.661 26.788  -10.364 1.00 39.51  ?  5   TYR B CA    1 
ATOM   4131 C  C     . TYR B 1 19  ? -11.452 25.289  -10.193 1.00 40.24  ?  5   TYR B C     1 
ATOM   4132 O  O     . TYR B 1 19  ? -12.067 24.477  -10.891 1.00 36.53  ?  5   TYR B O     1 
ATOM   4133 C  CB    . TYR B 1 19  ? -13.016 27.208  -9.795  1.00 36.69  ?  5   TYR B CB    1 
ATOM   4134 C  CG    . TYR B 1 19  ? -13.104 27.173  -8.288  1.00 40.13  ?  5   TYR B CG    1 
ATOM   4135 C  CD1   . TYR B 1 19  ? -12.777 28.291  -7.526  1.00 34.00  ?  5   TYR B CD1   1 
ATOM   4136 C  CD2   . TYR B 1 19  ? -13.528 26.027  -7.625  1.00 35.12  ?  5   TYR B CD2   1 
ATOM   4137 C  CE1   . TYR B 1 19  ? -12.863 28.264  -6.148  1.00 33.42  ?  5   TYR B CE1   1 
ATOM   4138 C  CE2   . TYR B 1 19  ? -13.618 25.992  -6.247  1.00 33.28  ?  5   TYR B CE2   1 
ATOM   4139 C  CZ    . TYR B 1 19  ? -13.281 27.110  -5.515  1.00 33.07  ?  5   TYR B CZ    1 
ATOM   4140 O  OH    . TYR B 1 19  ? -13.371 27.072  -4.145  1.00 32.58  ?  5   TYR B OH    1 
ATOM   4141 N  N     . CYS B 1 20  ? -10.573 24.920  -9.265  1.00 32.38  ?  6   CYS B N     1 
ATOM   4142 C  CA    . CYS B 1 20  ? -10.167 23.535  -9.129  1.00 31.71  ?  6   CYS B CA    1 
ATOM   4143 C  C     . CYS B 1 20  ? -10.018 23.188  -7.654  1.00 31.37  ?  6   CYS B C     1 
ATOM   4144 O  O     . CYS B 1 20  ? -10.209 24.030  -6.769  1.00 32.86  ?  6   CYS B O     1 
ATOM   4145 C  CB    . CYS B 1 20  ? -8.870  23.276  -9.899  1.00 34.62  ?  6   CYS B CB    1 
ATOM   4146 S  SG    . CYS B 1 20  ? -7.492  24.214  -9.273  1.00 37.57  ?  6   CYS B SG    1 
ATOM   4147 N  N     . VAL B 1 21  ? -9.618  21.936  -7.408  1.00 30.18  ?  7   VAL B N     1 
ATOM   4148 C  CA    . VAL B 1 21  ? -9.521  21.406  -6.050  1.00 29.95  ?  7   VAL B CA    1 
ATOM   4149 C  C     . VAL B 1 21  ? -8.571  22.247  -5.208  1.00 31.03  ?  7   VAL B C     1 
ATOM   4150 O  O     . VAL B 1 21  ? -8.828  22.498  -4.024  1.00 28.44  ?  7   VAL B O     1 
ATOM   4151 C  CB    . VAL B 1 21  ? -9.086  19.925  -6.098  1.00 29.59  ?  7   VAL B CB    1 
ATOM   4152 C  CG1   . VAL B 1 21  ? -8.639  19.431  -4.725  1.00 28.08  ?  7   VAL B CG1   1 
ATOM   4153 C  CG2   . VAL B 1 21  ? -10.220 19.054  -6.643  1.00 30.10  ?  7   VAL B CG2   1 
ATOM   4154 N  N     . ALA B 1 22  ? -7.460  22.698  -5.805  1.00 28.43  ?  8   ALA B N     1 
ATOM   4155 C  CA    . ALA B 1 22  ? -6.531  23.578  -5.099  1.00 32.91  ?  8   ALA B CA    1 
ATOM   4156 C  C     . ALA B 1 22  ? -7.233  24.827  -4.576  1.00 31.62  ?  8   ALA B C     1 
ATOM   4157 O  O     . ALA B 1 22  ? -7.004  25.245  -3.434  1.00 28.87  ?  8   ALA B O     1 
ATOM   4158 C  CB    . ALA B 1 22  ? -5.373  23.969  -6.020  1.00 27.78  ?  8   ALA B CB    1 
ATOM   4159 N  N     . ASP B 1 23  ? -8.078  25.448  -5.403  1.00 30.12  ?  9   ASP B N     1 
ATOM   4160 C  CA    . ASP B 1 23  ? -8.809  26.632  -4.961  1.00 29.81  ?  9   ASP B CA    1 
ATOM   4161 C  C     . ASP B 1 23  ? -9.836  26.286  -3.894  1.00 35.36  ?  9   ASP B C     1 
ATOM   4162 O  O     . ASP B 1 23  ? -10.047 27.061  -2.951  1.00 34.94  ?  9   ASP B O     1 
ATOM   4163 C  CB    . ASP B 1 23  ? -9.482  27.305  -6.153  1.00 32.41  ?  9   ASP B CB    1 
ATOM   4164 C  CG    . ASP B 1 23  ? -8.511  27.596  -7.267  1.00 40.83  ?  9   ASP B CG    1 
ATOM   4165 O  OD1   . ASP B 1 23  ? -7.435  28.160  -6.972  1.00 35.42  ?  9   ASP B OD1   1 
ATOM   4166 O  OD2   . ASP B 1 23  ? -8.816  27.247  -8.429  1.00 39.49  ?  9   ASP B OD2   1 
ATOM   4167 N  N     . TYR B 1 24  ? -10.489 25.126  -4.024  1.00 32.73  ?  10  TYR B N     1 
ATOM   4168 C  CA    . TYR B 1 24  ? -11.475 24.726  -3.027  1.00 30.21  ?  10  TYR B CA    1 
ATOM   4169 C  C     . TYR B 1 24  ? -10.832 24.589  -1.655  1.00 29.34  ?  10  TYR B C     1 
ATOM   4170 O  O     . TYR B 1 24  ? -11.374 25.073  -0.654  1.00 30.94  ?  10  TYR B O     1 
ATOM   4171 C  CB    . TYR B 1 24  ? -12.142 23.417  -3.453  1.00 30.48  ?  10  TYR B CB    1 
ATOM   4172 C  CG    . TYR B 1 24  ? -13.279 22.961  -2.566  1.00 31.21  ?  10  TYR B CG    1 
ATOM   4173 C  CD1   . TYR B 1 24  ? -13.045 22.148  -1.458  1.00 35.58  ?  10  TYR B CD1   1 
ATOM   4174 C  CD2   . TYR B 1 24  ? -14.591 23.319  -2.850  1.00 32.01  ?  10  TYR B CD2   1 
ATOM   4175 C  CE1   . TYR B 1 24  ? -14.092 21.717  -0.649  1.00 30.79  ?  10  TYR B CE1   1 
ATOM   4176 C  CE2   . TYR B 1 24  ? -15.641 22.894  -2.052  1.00 34.34  ?  10  TYR B CE2   1 
ATOM   4177 C  CZ    . TYR B 1 24  ? -15.385 22.096  -0.953  1.00 38.15  ?  10  TYR B CZ    1 
ATOM   4178 O  OH    . TYR B 1 24  ? -16.431 21.678  -0.162  1.00 34.74  ?  10  TYR B OH    1 
ATOM   4179 N  N     . LEU B 1 25  ? -9.657  23.958  -1.595  1.00 28.46  ?  11  LEU B N     1 
ATOM   4180 C  CA    . LEU B 1 25  ? -8.957  23.807  -0.324  1.00 27.69  ?  11  LEU B CA    1 
ATOM   4181 C  C     . LEU B 1 25  ? -8.602  25.161  0.277   1.00 29.15  ?  11  LEU B C     1 
ATOM   4182 O  O     . LEU B 1 25  ? -8.773  25.377  1.482   1.00 37.23  ?  11  LEU B O     1 
ATOM   4183 C  CB    . LEU B 1 25  ? -7.699  22.956  -0.523  1.00 26.87  ?  11  LEU B CB    1 
ATOM   4184 C  CG    . LEU B 1 25  ? -6.688  22.888  0.627   1.00 26.10  ?  11  LEU B CG    1 
ATOM   4185 C  CD1   . LEU B 1 25  ? -7.360  22.506  1.939   1.00 26.12  ?  11  LEU B CD1   1 
ATOM   4186 C  CD2   . LEU B 1 25  ? -5.555  21.906  0.293   1.00 27.28  ?  11  LEU B CD2   1 
ATOM   4187 N  N     . LEU B 1 26  ? -8.111  26.089  -0.548  1.00 29.68  ?  12  LEU B N     1 
ATOM   4188 C  CA    . LEU B 1 26  ? -7.778  27.420  -0.045  1.00 32.29  ?  12  LEU B CA    1 
ATOM   4189 C  C     . LEU B 1 26  ? -9.024  28.149  0.441   1.00 33.90  ?  12  LEU B C     1 
ATOM   4190 O  O     . LEU B 1 26  ? -8.992  28.835  1.470   1.00 28.76  ?  12  LEU B O     1 
ATOM   4191 C  CB    . LEU B 1 26  ? -7.063  28.226  -1.130  1.00 35.28  ?  12  LEU B CB    1 
ATOM   4192 C  CG    . LEU B 1 26  ? -5.712  27.664  -1.590  1.00 33.44  ?  12  LEU B CG    1 
ATOM   4193 C  CD1   . LEU B 1 26  ? -5.131  28.485  -2.733  1.00 33.72  ?  12  LEU B CD1   1 
ATOM   4194 C  CD2   . LEU B 1 26  ? -4.724  27.574  -0.432  1.00 27.78  ?  12  LEU B CD2   1 
ATOM   4195 N  N     . ASP B 1 27  ? -10.137 28.006  -0.282  1.00 31.95  ?  13  ASP B N     1 
ATOM   4196 C  CA    . ASP B 1 27  ? -11.386 28.619  0.154   1.00 31.46  ?  13  ASP B CA    1 
ATOM   4197 C  C     . ASP B 1 27  ? -11.818 28.078  1.511   1.00 38.23  ?  13  ASP B C     1 
ATOM   4198 O  O     . ASP B 1 27  ? -12.210 28.842  2.402   1.00 33.72  ?  13  ASP B O     1 
ATOM   4199 C  CB    . ASP B 1 27  ? -12.481 28.375  -0.886  1.00 40.84  ?  13  ASP B CB    1 
ATOM   4200 C  CG    . ASP B 1 27  ? -12.607 29.512  -1.882  1.00 50.93  ?  13  ASP B CG    1 
ATOM   4201 O  OD1   . ASP B 1 27  ? -12.225 30.654  -1.539  1.00 61.74  ?  13  ASP B OD1   1 
ATOM   4202 O  OD2   . ASP B 1 27  ? -13.095 29.259  -3.007  1.00 38.87  ?  13  ASP B OD2   1 
ATOM   4203 N  N     . ARG B 1 28  ? -11.762 26.752  1.684   1.00 36.67  ?  14  ARG B N     1 
ATOM   4204 C  CA    . ARG B 1 28  ? -12.133 26.165  2.967   1.00 30.89  ?  14  ARG B CA    1 
ATOM   4205 C  C     . ARG B 1 28  ? -11.141 26.553  4.057   1.00 34.32  ?  14  ARG B C     1 
ATOM   4206 O  O     . ARG B 1 28  ? -11.531 26.785  5.208   1.00 30.52  ?  14  ARG B O     1 
ATOM   4207 C  CB    . ARG B 1 28  ? -12.229 24.646  2.837   1.00 34.31  ?  14  ARG B CB    1 
ATOM   4208 C  CG    . ARG B 1 28  ? -13.246 24.168  1.819   1.00 30.06  ?  14  ARG B CG    1 
ATOM   4209 C  CD    . ARG B 1 28  ? -14.566 24.897  1.978   1.00 31.18  ?  14  ARG B CD    1 
ATOM   4210 N  NE    . ARG B 1 28  ? -15.683 23.975  2.140   1.00 32.07  ?  14  ARG B NE    1 
ATOM   4211 C  CZ    . ARG B 1 28  ? -16.958 24.337  2.199   1.00 39.42  ?  14  ARG B CZ    1 
ATOM   4212 N  NH1   . ARG B 1 28  ? -17.324 25.609  2.116   1.00 36.21  ?  14  ARG B NH1   1 
ATOM   4213 N  NH2   . ARG B 1 28  ? -17.887 23.403  2.364   1.00 35.54  ?  14  ARG B NH2   1 
ATOM   4214 N  N     . LEU B 1 29  ? -9.857  26.644  3.703   1.00 29.05  ?  15  LEU B N     1 
ATOM   4215 C  CA    . LEU B 1 29  ? -8.830  27.029  4.665   1.00 36.59  ?  15  LEU B CA    1 
ATOM   4216 C  C     . LEU B 1 29  ? -9.085  28.427  5.221   1.00 38.93  ?  15  LEU B C     1 
ATOM   4217 O  O     . LEU B 1 29  ? -8.972  28.662  6.431   1.00 33.61  ?  15  LEU B O     1 
ATOM   4218 C  CB    . LEU B 1 29  ? -7.458  26.967  3.998   1.00 38.30  ?  15  LEU B CB    1 
ATOM   4219 C  CG    . LEU B 1 29  ? -6.282  27.153  4.944   1.00 42.30  ?  15  LEU B CG    1 
ATOM   4220 C  CD1   . LEU B 1 29  ? -6.315  26.035  5.972   1.00 43.90  ?  15  LEU B CD1   1 
ATOM   4221 C  CD2   . LEU B 1 29  ? -4.974  27.152  4.161   1.00 39.40  ?  15  LEU B CD2   1 
ATOM   4222 N  N     . THR B 1 30  ? -9.412  29.377  4.348   1.00 34.51  ?  16  THR B N     1 
ATOM   4223 C  CA    . THR B 1 30  ? -9.688  30.726  4.826   1.00 38.97  ?  16  THR B CA    1 
ATOM   4224 C  C     . THR B 1 30  ? -10.960 30.770  5.663   1.00 35.65  ?  16  THR B C     1 
ATOM   4225 O  O     . THR B 1 30  ? -11.043 31.556  6.613   1.00 44.76  ?  16  THR B O     1 
ATOM   4226 C  CB    . THR B 1 30  ? -9.762  31.696  3.648   1.00 35.49  ?  16  THR B CB    1 
ATOM   4227 O  OG1   . THR B 1 30  ? -10.675 31.195  2.668   1.00 51.43  ?  16  THR B OG1   1 
ATOM   4228 C  CG2   . THR B 1 30  ? -8.395  31.829  3.010   1.00 46.20  ?  16  THR B CG2   1 
ATOM   4229 N  N     . ASP B 1 31  ? -11.956 29.942  5.326   1.00 43.81  ?  17  ASP B N     1 
ATOM   4230 C  CA    . ASP B 1 31  ? -13.162 29.846  6.147   1.00 40.94  ?  17  ASP B CA    1 
ATOM   4231 C  C     . ASP B 1 31  ? -12.826 29.466  7.583   1.00 37.92  ?  17  ASP B C     1 
ATOM   4232 O  O     . ASP B 1 31  ? -13.439 29.977  8.527   1.00 37.06  ?  17  ASP B O     1 
ATOM   4233 C  CB    . ASP B 1 31  ? -14.133 28.819  5.558   1.00 44.99  ?  17  ASP B CB    1 
ATOM   4234 C  CG    . ASP B 1 31  ? -14.758 29.272  4.253   1.00 50.80  ?  17  ASP B CG    1 
ATOM   4235 O  OD1   . ASP B 1 31  ? -14.536 30.431  3.847   1.00 45.08  ?  17  ASP B OD1   1 
ATOM   4236 O  OD2   . ASP B 1 31  ? -15.462 28.451  3.623   1.00 41.76  ?  17  ASP B OD2   1 
ATOM   4237 N  N     . CYS B 1 32  ? -11.858 28.563  7.768   1.00 39.69  ?  18  CYS B N     1 
ATOM   4238 C  CA    . CYS B 1 32  ? -11.504 28.076  9.094   1.00 30.01  ?  18  CYS B CA    1 
ATOM   4239 C  C     . CYS B 1 32  ? -10.697 29.083  9.904   1.00 40.29  ?  18  CYS B C     1 
ATOM   4240 O  O     . CYS B 1 32  ? -10.506 28.869  11.108  1.00 33.30  ?  18  CYS B O     1 
ATOM   4241 C  CB    . CYS B 1 32  ? -10.736 26.755  8.973   1.00 36.02  ?  18  CYS B CB    1 
ATOM   4242 S  SG    . CYS B 1 32  ? -11.713 25.417  8.208   1.00 37.93  ?  18  CYS B SG    1 
ATOM   4243 N  N     . GLY B 1 33  ? -10.246 30.175  9.290   1.00 32.62  ?  19  GLY B N     1 
ATOM   4244 C  CA    . GLY B 1 33  ? -9.603  31.256  10.006  1.00 34.77  ?  19  GLY B CA    1 
ATOM   4245 C  C     . GLY B 1 33  ? -8.137  31.496  9.692   1.00 39.51  ?  19  GLY B C     1 
ATOM   4246 O  O     . GLY B 1 33  ? -7.508  32.313  10.373  1.00 39.46  ?  19  GLY B O     1 
ATOM   4247 N  N     . ALA B 1 34  ? -7.571  30.821  8.699   1.00 37.49  ?  20  ALA B N     1 
ATOM   4248 C  CA    . ALA B 1 34  ? -6.173  31.007  8.333   1.00 33.48  ?  20  ALA B CA    1 
ATOM   4249 C  C     . ALA B 1 34  ? -6.083  31.961  7.151   1.00 42.05  ?  20  ALA B C     1 
ATOM   4250 O  O     . ALA B 1 34  ? -6.755  31.761  6.133   1.00 43.78  ?  20  ALA B O     1 
ATOM   4251 C  CB    . ALA B 1 34  ? -5.510  29.673  7.991   1.00 32.81  ?  20  ALA B CB    1 
ATOM   4252 N  N     . ASP B 1 35  ? -5.258  32.998  7.292   1.00 38.65  ?  21  ASP B N     1 
ATOM   4253 C  CA    . ASP B 1 35  ? -4.997  33.941  6.214   1.00 36.08  ?  21  ASP B CA    1 
ATOM   4254 C  C     . ASP B 1 35  ? -3.604  33.790  5.628   1.00 38.40  ?  21  ASP B C     1 
ATOM   4255 O  O     . ASP B 1 35  ? -3.264  34.503  4.674   1.00 29.24  ?  21  ASP B O     1 
ATOM   4256 C  CB    . ASP B 1 35  ? -5.195  35.375  6.712   1.00 34.44  ?  21  ASP B CB    1 
ATOM   4257 C  CG    . ASP B 1 35  ? -6.535  35.568  7.382   1.00 46.07  ?  21  ASP B CG    1 
ATOM   4258 O  OD1   . ASP B 1 35  ? -7.548  35.109  6.815   1.00 48.80  ?  21  ASP B OD1   1 
ATOM   4259 O  OD2   . ASP B 1 35  ? -6.572  36.167  8.477   1.00 45.96  ?  21  ASP B OD2   1 
ATOM   4260 N  N     . HIS B 1 36  ? -2.796  32.886  6.177   1.00 31.20  ?  22  HIS B N     1 
ATOM   4261 C  CA    . HIS B 1 36  ? -1.438  32.647  5.722   1.00 34.56  ?  22  HIS B CA    1 
ATOM   4262 C  C     . HIS B 1 36  ? -1.200  31.148  5.625   1.00 33.55  ?  22  HIS B C     1 
ATOM   4263 O  O     . HIS B 1 36  ? -1.862  30.352  6.298   1.00 30.97  ?  22  HIS B O     1 
ATOM   4264 C  CB    . HIS B 1 36  ? -0.401  33.280  6.671   1.00 31.98  ?  22  HIS B CB    1 
ATOM   4265 C  CG    . HIS B 1 36  ? -0.537  34.765  6.812   1.00 32.44  ?  22  HIS B CG    1 
ATOM   4266 N  ND1   . HIS B 1 36  ? -1.558  35.354  7.528   1.00 31.98  ?  22  HIS B ND1   1 
ATOM   4267 C  CD2   . HIS B 1 36  ? 0.211   35.779  6.318   1.00 27.21  ?  22  HIS B CD2   1 
ATOM   4268 C  CE1   . HIS B 1 36  ? -1.428  36.668  7.474   1.00 32.34  ?  22  HIS B CE1   1 
ATOM   4269 N  NE2   . HIS B 1 36  ? -0.363  36.952  6.746   1.00 35.08  ?  22  HIS B NE2   1 
ATOM   4270 N  N     . LEU B 1 37  ? -0.256  30.774  4.763   1.00 30.85  ?  23  LEU B N     1 
ATOM   4271 C  CA    . LEU B 1 37  ? 0.181   29.391  4.615   1.00 29.78  ?  23  LEU B CA    1 
ATOM   4272 C  C     . LEU B 1 37  ? 1.696   29.360  4.746   1.00 30.07  ?  23  LEU B C     1 
ATOM   4273 O  O     . LEU B 1 37  ? 2.405   29.963  3.933   1.00 27.55  ?  23  LEU B O     1 
ATOM   4274 C  CB    . LEU B 1 37  ? -0.267  28.809  3.270   1.00 29.59  ?  23  LEU B CB    1 
ATOM   4275 C  CG    . LEU B 1 37  ? 0.198   27.398  2.903   1.00 28.86  ?  23  LEU B CG    1 
ATOM   4276 C  CD1   . LEU B 1 37  ? -0.340  26.367  3.885   1.00 29.07  ?  23  LEU B CD1   1 
ATOM   4277 C  CD2   . LEU B 1 37  ? -0.220  27.048  1.484   1.00 28.31  ?  23  LEU B CD2   1 
ATOM   4278 N  N     . PHE B 1 38  ? 2.186   28.677  5.774   1.00 29.46  ?  24  PHE B N     1 
ATOM   4279 C  CA    . PHE B 1 38  ? 3.615   28.534  6.011   1.00 31.88  ?  24  PHE B CA    1 
ATOM   4280 C  C     . PHE B 1 38  ? 4.135   27.267  5.349   1.00 29.31  ?  24  PHE B C     1 
ATOM   4281 O  O     . PHE B 1 38  ? 3.403   26.287  5.189   1.00 28.66  ?  24  PHE B O     1 
ATOM   4282 C  CB    . PHE B 1 38  ? 3.908   28.484  7.511   1.00 31.37  ?  24  PHE B CB    1 
ATOM   4283 C  CG    . PHE B 1 38  ? 3.400   29.676  8.267   1.00 27.95  ?  24  PHE B CG    1 
ATOM   4284 C  CD1   . PHE B 1 38  ? 2.109   29.698  8.773   1.00 26.56  ?  24  PHE B CD1   1 
ATOM   4285 C  CD2   . PHE B 1 38  ? 4.219   30.777  8.475   1.00 25.81  ?  24  PHE B CD2   1 
ATOM   4286 C  CE1   . PHE B 1 38  ? 1.636   30.807  9.468   1.00 31.82  ?  24  PHE B CE1   1 
ATOM   4287 C  CE2   . PHE B 1 38  ? 3.757   31.884  9.169   1.00 27.27  ?  24  PHE B CE2   1 
ATOM   4288 C  CZ    . PHE B 1 38  ? 2.460   31.900  9.667   1.00 27.51  ?  24  PHE B CZ    1 
ATOM   4289 N  N     . GLY B 1 39  ? 5.408   27.282  4.970   1.00 30.71  ?  25  GLY B N     1 
ATOM   4290 C  CA    . GLY B 1 39  ? 6.010   26.044  4.513   1.00 32.96  ?  25  GLY B CA    1 
ATOM   4291 C  C     . GLY B 1 39  ? 7.253   26.280  3.673   1.00 36.92  ?  25  GLY B C     1 
ATOM   4292 O  O     . GLY B 1 39  ? 7.845   27.359  3.693   1.00 26.75  ?  25  GLY B O     1 
ATOM   4293 N  N     . VAL B 1 40  ? 7.632   25.225  2.958   1.00 28.59  ?  26  VAL B N     1 
ATOM   4294 C  CA    . VAL B 1 40  ? 8.803   25.214  2.088   1.00 28.77  ?  26  VAL B CA    1 
ATOM   4295 C  C     . VAL B 1 40  ? 8.372   24.599  0.761   1.00 28.18  ?  26  VAL B C     1 
ATOM   4296 O  O     . VAL B 1 40  ? 7.729   23.537  0.748   1.00 25.61  ?  26  VAL B O     1 
ATOM   4297 C  CB    . VAL B 1 40  ? 9.962   24.431  2.732   1.00 28.32  ?  26  VAL B CB    1 
ATOM   4298 C  CG1   . VAL B 1 40  ? 11.154  24.334  1.791   1.00 26.52  ?  26  VAL B CG1   1 
ATOM   4299 C  CG2   . VAL B 1 40  ? 10.372  25.069  4.053   1.00 26.55  ?  26  VAL B CG2   1 
ATOM   4300 N  N     . PRO B 1 41  ? 8.703   25.215  -0.368  1.00 27.38  ?  27  PRO B N     1 
ATOM   4301 C  CA    . PRO B 1 41  ? 8.255   24.691  -1.659  1.00 23.64  ?  27  PRO B CA    1 
ATOM   4302 C  C     . PRO B 1 41  ? 9.040   23.462  -2.087  1.00 28.81  ?  27  PRO B C     1 
ATOM   4303 O  O     . PRO B 1 41  ? 10.146  23.181  -1.614  1.00 30.05  ?  27  PRO B O     1 
ATOM   4304 C  CB    . PRO B 1 41  ? 8.513   25.859  -2.620  1.00 28.68  ?  27  PRO B CB    1 
ATOM   4305 C  CG    . PRO B 1 41  ? 9.664   26.576  -2.010  1.00 31.24  ?  27  PRO B CG    1 
ATOM   4306 C  CD    . PRO B 1 41  ? 9.508   26.440  -0.515  1.00 24.20  ?  27  PRO B CD    1 
ATOM   4307 N  N     . GLY B 1 42  ? 8.432   22.724  -3.007  1.00 35.08  ?  28  GLY B N     1 
ATOM   4308 C  CA    . GLY B 1 42  ? 9.083   21.604  -3.656  1.00 25.41  ?  28  GLY B CA    1 
ATOM   4309 C  C     . GLY B 1 42  ? 8.429   21.377  -4.998  1.00 34.53  ?  28  GLY B C     1 
ATOM   4310 O  O     . GLY B 1 42  ? 7.337   21.883  -5.265  1.00 34.97  ?  28  GLY B O     1 
ATOM   4311 N  N     . ASP B 1 43  ? 9.106   20.603  -5.853  1.00 26.18  ?  29  ASP B N     1 
ATOM   4312 C  CA    . ASP B 1 43  ? 8.579   20.380  -7.196  1.00 30.81  ?  29  ASP B CA    1 
ATOM   4313 C  C     . ASP B 1 43  ? 7.213   19.705  -7.151  1.00 37.67  ?  29  ASP B C     1 
ATOM   4314 O  O     . ASP B 1 43  ? 6.380   19.930  -8.040  1.00 40.34  ?  29  ASP B O     1 
ATOM   4315 C  CB    . ASP B 1 43  ? 9.585   19.595  -8.055  1.00 34.15  ?  29  ASP B CB    1 
ATOM   4316 C  CG    . ASP B 1 43  ? 9.561   18.078  -7.815  1.00 49.81  ?  29  ASP B CG    1 
ATOM   4317 O  OD1   . ASP B 1 43  ? 9.387   17.628  -6.667  1.00 37.47  ?  29  ASP B OD1   1 
ATOM   4318 O  OD2   . ASP B 1 43  ? 9.747   17.322  -8.796  1.00 39.92  ?  29  ASP B OD2   1 
ATOM   4319 N  N     . TYR B 1 44  ? 6.936   18.930  -6.097  1.00 30.50  ?  30  TYR B N     1 
ATOM   4320 C  CA    . TYR B 1 44  ? 5.637   18.277  -5.983  1.00 33.01  ?  30  TYR B CA    1 
ATOM   4321 C  C     . TYR B 1 44  ? 4.514   19.237  -5.592  1.00 37.56  ?  30  TYR B C     1 
ATOM   4322 O  O     . TYR B 1 44  ? 3.348   18.853  -5.698  1.00 31.04  ?  30  TYR B O     1 
ATOM   4323 C  CB    . TYR B 1 44  ? 5.705   17.133  -4.967  1.00 31.55  ?  30  TYR B CB    1 
ATOM   4324 C  CG    . TYR B 1 44  ? 6.619   15.985  -5.360  1.00 31.66  ?  30  TYR B CG    1 
ATOM   4325 C  CD1   . TYR B 1 44  ? 6.601   15.454  -6.646  1.00 38.43  ?  30  TYR B CD1   1 
ATOM   4326 C  CD2   . TYR B 1 44  ? 7.502   15.429  -4.436  1.00 39.17  ?  30  TYR B CD2   1 
ATOM   4327 C  CE1   . TYR B 1 44  ? 7.440   14.395  -7.002  1.00 30.55  ?  30  TYR B CE1   1 
ATOM   4328 C  CE2   . TYR B 1 44  ? 8.339   14.376  -4.780  1.00 27.29  ?  30  TYR B CE2   1 
ATOM   4329 C  CZ    . TYR B 1 44  ? 8.304   13.864  -6.061  1.00 30.54  ?  30  TYR B CZ    1 
ATOM   4330 O  OH    . TYR B 1 44  ? 9.141   12.819  -6.395  1.00 28.67  ?  30  TYR B OH    1 
ATOM   4331 N  N     . ASN B 1 45  ? 4.818   20.471  -5.151  1.00 37.04  ?  31  ASN B N     1 
ATOM   4332 C  CA    . ASN B 1 45  ? 3.760   21.398  -4.748  1.00 31.43  ?  31  ASN B CA    1 
ATOM   4333 C  C     . ASN B 1 45  ? 3.849   22.771  -5.406  1.00 29.49  ?  31  ASN B C     1 
ATOM   4334 O  O     . ASN B 1 45  ? 3.122   23.682  -4.994  1.00 34.26  ?  31  ASN B O     1 
ATOM   4335 C  CB    . ASN B 1 45  ? 3.710   21.566  -3.216  1.00 25.50  ?  31  ASN B CB    1 
ATOM   4336 C  CG    . ASN B 1 45  ? 4.961   22.229  -2.628  1.00 37.00  ?  31  ASN B CG    1 
ATOM   4337 O  OD1   . ASN B 1 45  ? 5.593   23.098  -3.243  1.00 28.75  ?  31  ASN B OD1   1 
ATOM   4338 N  ND2   . ASN B 1 45  ? 5.307   21.826  -1.406  1.00 24.25  ?  31  ASN B ND2   1 
ATOM   4339 N  N     . LEU B 1 46  ? 4.696   22.948  -6.422  1.00 31.93  ?  32  LEU B N     1 
ATOM   4340 C  CA    . LEU B 1 46  ? 4.841   24.267  -7.032  1.00 28.96  ?  32  LEU B CA    1 
ATOM   4341 C  C     . LEU B 1 46  ? 3.543   24.722  -7.691  1.00 34.45  ?  32  LEU B C     1 
ATOM   4342 O  O     . LEU B 1 46  ? 3.145   25.886  -7.554  1.00 32.56  ?  32  LEU B O     1 
ATOM   4343 C  CB    . LEU B 1 46  ? 5.976   24.253  -8.055  1.00 31.42  ?  32  LEU B CB    1 
ATOM   4344 C  CG    . LEU B 1 46  ? 7.401   24.032  -7.542  1.00 28.88  ?  32  LEU B CG    1 
ATOM   4345 C  CD1   . LEU B 1 46  ? 8.414   24.234  -8.667  1.00 28.04  ?  32  LEU B CD1   1 
ATOM   4346 C  CD2   . LEU B 1 46  ? 7.707   24.939  -6.358  1.00 25.08  ?  32  LEU B CD2   1 
ATOM   4347 N  N     . GLN B 1 47  ? 2.861   23.818  -8.399  1.00 30.61  ?  33  GLN B N     1 
ATOM   4348 C  CA    . GLN B 1 47  ? 1.636   24.199  -9.099  1.00 38.96  ?  33  GLN B CA    1 
ATOM   4349 C  C     . GLN B 1 47  ? 0.525   24.558  -8.121  1.00 34.61  ?  33  GLN B C     1 
ATOM   4350 O  O     . GLN B 1 47  ? -0.273  25.464  -8.386  1.00 31.36  ?  33  GLN B O     1 
ATOM   4351 C  CB    . GLN B 1 47  ? 1.206   23.080  -10.046 1.00 38.53  ?  33  GLN B CB    1 
ATOM   4352 C  CG    . GLN B 1 47  ? 2.371   22.558  -10.878 1.00 55.81  ?  33  GLN B CG    1 
ATOM   4353 C  CD    . GLN B 1 47  ? 1.964   22.096  -12.258 1.00 51.29  ?  33  GLN B CD    1 
ATOM   4354 O  OE1   . GLN B 1 47  ? 1.662   20.925  -12.468 1.00 68.20  ?  33  GLN B OE1   1 
ATOM   4355 N  NE2   . GLN B 1 47  ? 1.969   23.015  -13.213 1.00 71.25  ?  33  GLN B NE2   1 
ATOM   4356 N  N     . PHE B 1 48  ? 0.456   23.863  -6.985  1.00 34.00  ?  34  PHE B N     1 
ATOM   4357 C  CA    . PHE B 1 48  ? -0.471  24.274  -5.936  1.00 29.96  ?  34  PHE B CA    1 
ATOM   4358 C  C     . PHE B 1 48  ? -0.137  25.674  -5.431  1.00 35.41  ?  34  PHE B C     1 
ATOM   4359 O  O     . PHE B 1 48  ? -1.038  26.477  -5.157  1.00 32.48  ?  34  PHE B O     1 
ATOM   4360 C  CB    . PHE B 1 48  ? -0.443  23.272  -4.783  1.00 25.62  ?  34  PHE B CB    1 
ATOM   4361 C  CG    . PHE B 1 48  ? -1.249  23.698  -3.591  1.00 30.99  ?  34  PHE B CG    1 
ATOM   4362 C  CD1   . PHE B 1 48  ? -2.631  23.755  -3.659  1.00 34.75  ?  34  PHE B CD1   1 
ATOM   4363 C  CD2   . PHE B 1 48  ? -0.627  24.039  -2.402  1.00 26.27  ?  34  PHE B CD2   1 
ATOM   4364 C  CE1   . PHE B 1 48  ? -3.379  24.145  -2.565  1.00 26.66  ?  34  PHE B CE1   1 
ATOM   4365 C  CE2   . PHE B 1 48  ? -1.367  24.430  -1.304  1.00 27.29  ?  34  PHE B CE2   1 
ATOM   4366 C  CZ    . PHE B 1 48  ? -2.747  24.485  -1.387  1.00 27.90  ?  34  PHE B CZ    1 
ATOM   4367 N  N     . LEU B 1 49  ? 1.160   25.980  -5.297  1.00 28.38  ?  35  LEU B N     1 
ATOM   4368 C  CA    . LEU B 1 49  ? 1.575   27.276  -4.767  1.00 28.91  ?  35  LEU B CA    1 
ATOM   4369 C  C     . LEU B 1 49  ? 1.145   28.428  -5.667  1.00 26.65  ?  35  LEU B C     1 
ATOM   4370 O  O     . LEU B 1 49  ? 0.931   29.542  -5.179  1.00 28.78  ?  35  LEU B O     1 
ATOM   4371 C  CB    . LEU B 1 49  ? 3.088   27.302  -4.558  1.00 27.82  ?  35  LEU B CB    1 
ATOM   4372 C  CG    . LEU B 1 49  ? 3.567   26.714  -3.231  1.00 30.93  ?  35  LEU B CG    1 
ATOM   4373 C  CD1   . LEU B 1 49  ? 5.061   26.436  -3.269  1.00 26.69  ?  35  LEU B CD1   1 
ATOM   4374 C  CD2   . LEU B 1 49  ? 3.226   27.640  -2.085  1.00 27.82  ?  35  LEU B CD2   1 
ATOM   4375 N  N     . ASP B 1 50  ? 1.026   28.188  -6.977  1.00 29.09  ?  36  ASP B N     1 
ATOM   4376 C  CA    . ASP B 1 50  ? 0.495   29.208  -7.876  1.00 33.05  ?  36  ASP B CA    1 
ATOM   4377 C  C     . ASP B 1 50  ? -0.881  29.679  -7.425  1.00 36.80  ?  36  ASP B C     1 
ATOM   4378 O  O     . ASP B 1 50  ? -1.190  30.874  -7.491  1.00 40.13  ?  36  ASP B O     1 
ATOM   4379 C  CB    . ASP B 1 50  ? 0.412   28.669  -9.302  1.00 30.42  ?  36  ASP B CB    1 
ATOM   4380 C  CG    . ASP B 1 50  ? 1.765   28.469  -9.925  1.00 40.84  ?  36  ASP B CG    1 
ATOM   4381 O  OD1   . ASP B 1 50  ? 2.766   28.957  -9.351  1.00 39.61  ?  36  ASP B OD1   1 
ATOM   4382 O  OD2   . ASP B 1 50  ? 1.825   27.816  -10.991 1.00 42.68  ?  36  ASP B OD2   1 
ATOM   4383 N  N     . HIS B 1 51  ? -1.728  28.750  -6.981  1.00 33.81  ?  37  HIS B N     1 
ATOM   4384 C  CA    . HIS B 1 51  ? -3.050  29.140  -6.508  1.00 33.54  ?  37  HIS B CA    1 
ATOM   4385 C  C     . HIS B 1 51  ? -2.960  29.868  -5.179  1.00 32.41  ?  37  HIS B C     1 
ATOM   4386 O  O     . HIS B 1 51  ? -3.771  30.758  -4.908  1.00 35.82  ?  37  HIS B O     1 
ATOM   4387 C  CB    . HIS B 1 51  ? -3.950  27.909  -6.394  1.00 30.97  ?  37  HIS B CB    1 
ATOM   4388 C  CG    . HIS B 1 51  ? -4.210  27.238  -7.706  1.00 32.84  ?  37  HIS B CG    1 
ATOM   4389 N  ND1   . HIS B 1 51  ? -5.355  27.457  -8.441  1.00 29.84  ?  37  HIS B ND1   1 
ATOM   4390 C  CD2   . HIS B 1 51  ? -3.457  26.377  -8.429  1.00 35.53  ?  37  HIS B CD2   1 
ATOM   4391 C  CE1   . HIS B 1 51  ? -5.303  26.747  -9.554  1.00 34.37  ?  37  HIS B CE1   1 
ATOM   4392 N  NE2   . HIS B 1 51  ? -4.162  26.083  -9.571  1.00 37.82  ?  37  HIS B NE2   1 
ATOM   4393 N  N     . VAL B 1 52  ? -1.976  29.517  -4.347  1.00 31.56  ?  38  VAL B N     1 
ATOM   4394 C  CA    . VAL B 1 52  ? -1.760  30.260  -3.111  1.00 31.75  ?  38  VAL B CA    1 
ATOM   4395 C  C     . VAL B 1 52  ? -1.334  31.688  -3.422  1.00 33.04  ?  38  VAL B C     1 
ATOM   4396 O  O     . VAL B 1 52  ? -1.852  32.647  -2.838  1.00 34.97  ?  38  VAL B O     1 
ATOM   4397 C  CB    . VAL B 1 52  ? -0.723  29.537  -2.230  1.00 31.55  ?  38  VAL B CB    1 
ATOM   4398 C  CG1   . VAL B 1 52  ? -0.441  30.342  -0.962  1.00 26.12  ?  38  VAL B CG1   1 
ATOM   4399 C  CG2   . VAL B 1 52  ? -1.217  28.134  -1.881  1.00 25.86  ?  38  VAL B CG2   1 
ATOM   4400 N  N     . ILE B 1 53  ? -0.401  31.848  -4.364  1.00 30.68  ?  39  ILE B N     1 
ATOM   4401 C  CA    . ILE B 1 53  ? 0.052   33.175  -4.768  1.00 38.75  ?  39  ILE B CA    1 
ATOM   4402 C  C     . ILE B 1 53  ? -1.108  33.975  -5.352  1.00 47.06  ?  39  ILE B C     1 
ATOM   4403 O  O     . ILE B 1 53  ? -1.308  35.148  -5.019  1.00 39.76  ?  39  ILE B O     1 
ATOM   4404 C  CB    . ILE B 1 53  ? 1.218   33.055  -5.770  1.00 39.06  ?  39  ILE B CB    1 
ATOM   4405 C  CG1   . ILE B 1 53  ? 2.520   32.609  -5.084  1.00 35.83  ?  39  ILE B CG1   1 
ATOM   4406 C  CG2   . ILE B 1 53  ? 1.433   34.368  -6.500  1.00 43.65  ?  39  ILE B CG2   1 
ATOM   4407 C  CD1   . ILE B 1 53  ? 2.747   33.180  -3.700  1.00 35.45  ?  39  ILE B CD1   1 
ATOM   4408 N  N     . ASP B 1 54  ? -1.903  33.341  -6.218  1.00 42.64  ?  40  ASP B N     1 
ATOM   4409 C  CA    . ASP B 1 54  ? -2.967  34.051  -6.917  1.00 46.95  ?  40  ASP B CA    1 
ATOM   4410 C  C     . ASP B 1 54  ? -4.160  34.364  -6.028  1.00 41.86  ?  40  ASP B C     1 
ATOM   4411 O  O     . ASP B 1 54  ? -4.941  35.259  -6.362  1.00 42.93  ?  40  ASP B O     1 
ATOM   4412 C  CB    . ASP B 1 54  ? -3.443  33.237  -8.121  1.00 51.66  ?  40  ASP B CB    1 
ATOM   4413 C  CG    . ASP B 1 54  ? -2.489  33.319  -9.289  1.00 63.62  ?  40  ASP B CG    1 
ATOM   4414 O  OD1   . ASP B 1 54  ? -1.571  34.167  -9.252  1.00 66.86  ?  40  ASP B OD1   1 
ATOM   4415 O  OD2   . ASP B 1 54  ? -2.651  32.530  -10.245 1.00 70.54  ?  40  ASP B OD2   1 
ATOM   4416 N  N     . SER B 1 55  ? -4.330  33.652  -4.924  1.00 34.90  ?  41  SER B N     1 
ATOM   4417 C  CA    . SER B 1 55  ? -5.501  33.870  -4.091  1.00 39.83  ?  41  SER B CA    1 
ATOM   4418 C  C     . SER B 1 55  ? -5.422  35.230  -3.398  1.00 51.08  ?  41  SER B C     1 
ATOM   4419 O  O     . SER B 1 55  ? -4.362  35.613  -2.894  1.00 43.56  ?  41  SER B O     1 
ATOM   4420 C  CB    . SER B 1 55  ? -5.635  32.763  -3.052  1.00 43.68  ?  41  SER B CB    1 
ATOM   4421 O  OG    . SER B 1 55  ? -6.418  33.202  -1.957  1.00 47.67  ?  41  SER B OG    1 
ATOM   4422 N  N     . PRO B 1 56  ? -6.523  35.986  -3.357  1.00 44.30  ?  42  PRO B N     1 
ATOM   4423 C  CA    . PRO B 1 56  ? -6.524  37.232  -2.584  1.00 44.10  ?  42  PRO B CA    1 
ATOM   4424 C  C     . PRO B 1 56  ? -6.744  37.023  -1.096  1.00 38.45  ?  42  PRO B C     1 
ATOM   4425 O  O     . PRO B 1 56  ? -6.653  37.994  -0.334  1.00 45.81  ?  42  PRO B O     1 
ATOM   4426 C  CB    . PRO B 1 56  ? -7.687  38.030  -3.199  1.00 44.23  ?  42  PRO B CB    1 
ATOM   4427 C  CG    . PRO B 1 56  ? -8.511  37.032  -3.984  1.00 40.26  ?  42  PRO B CG    1 
ATOM   4428 C  CD    . PRO B 1 56  ? -7.849  35.687  -3.924  1.00 42.03  ?  42  PRO B CD    1 
ATOM   4429 N  N     . ASP B 1 57  ? -7.022  35.795  -0.654  1.00 34.08  ?  43  ASP B N     1 
ATOM   4430 C  CA    . ASP B 1 57  ? -7.377  35.550  0.736   1.00 33.68  ?  43  ASP B CA    1 
ATOM   4431 C  C     . ASP B 1 57  ? -6.286  34.885  1.556   1.00 35.43  ?  43  ASP B C     1 
ATOM   4432 O  O     . ASP B 1 57  ? -6.337  34.958  2.787   1.00 38.78  ?  43  ASP B O     1 
ATOM   4433 C  CB    . ASP B 1 57  ? -8.636  34.675  0.808   1.00 35.61  ?  43  ASP B CB    1 
ATOM   4434 C  CG    . ASP B 1 57  ? -9.790  35.256  0.016   1.00 45.42  ?  43  ASP B CG    1 
ATOM   4435 O  OD1   . ASP B 1 57  ? -10.121 36.440  0.237   1.00 45.13  ?  43  ASP B OD1   1 
ATOM   4436 O  OD2   . ASP B 1 57  ? -10.356 34.535  -0.829  1.00 45.43  ?  43  ASP B OD2   1 
ATOM   4437 N  N     . ILE B 1 58  ? -5.315  34.239  0.922   1.00 32.73  ?  44  ILE B N     1 
ATOM   4438 C  CA    . ILE B 1 58  ? -4.265  33.512  1.622   1.00 33.62  ?  44  ILE B CA    1 
ATOM   4439 C  C     . ILE B 1 58  ? -2.911  34.047  1.168   1.00 36.40  ?  44  ILE B C     1 
ATOM   4440 O  O     . ILE B 1 58  ? -2.684  34.257  -0.030  1.00 29.29  ?  44  ILE B O     1 
ATOM   4441 C  CB    . ILE B 1 58  ? -4.385  31.991  1.398   1.00 35.37  ?  44  ILE B CB    1 
ATOM   4442 C  CG1   . ILE B 1 58  ? -3.325  31.231  2.205   1.00 34.26  ?  44  ILE B CG1   1 
ATOM   4443 C  CG2   . ILE B 1 58  ? -4.315  31.645  -0.069  1.00 49.28  ?  44  ILE B CG2   1 
ATOM   4444 C  CD1   . ILE B 1 58  ? -3.836  30.717  3.535   1.00 44.47  ?  44  ILE B CD1   1 
ATOM   4445 N  N     . CYS B 1 59  ? -2.026  34.294  2.125   1.00 27.59  ?  45  CYS B N     1 
ATOM   4446 C  CA    . CYS B 1 59  ? -0.694  34.817  1.849   1.00 36.35  ?  45  CYS B CA    1 
ATOM   4447 C  C     . CYS B 1 59  ? 0.339   33.720  2.089   1.00 38.59  ?  45  CYS B C     1 
ATOM   4448 O  O     . CYS B 1 59  ? 0.377   33.124  3.170   1.00 31.04  ?  45  CYS B O     1 
ATOM   4449 C  CB    . CYS B 1 59  ? -0.414  36.035  2.728   1.00 33.80  ?  45  CYS B CB    1 
ATOM   4450 S  SG    . CYS B 1 59  ? 1.252   36.688  2.589   1.00 49.67  ?  45  CYS B SG    1 
ATOM   4451 N  N     . TRP B 1 60  ? 1.161   33.440  1.079   1.00 32.77  ?  46  TRP B N     1 
ATOM   4452 C  CA    . TRP B 1 60  ? 2.240   32.473  1.255   1.00 35.44  ?  46  TRP B CA    1 
ATOM   4453 C  C     . TRP B 1 60  ? 3.335   33.058  2.138   1.00 31.47  ?  46  TRP B C     1 
ATOM   4454 O  O     . TRP B 1 60  ? 3.725   34.217  1.983   1.00 36.84  ?  46  TRP B O     1 
ATOM   4455 C  CB    . TRP B 1 60  ? 2.834   32.063  -0.094  1.00 28.27  ?  46  TRP B CB    1 
ATOM   4456 C  CG    . TRP B 1 60  ? 4.073   31.202  0.017   1.00 33.94  ?  46  TRP B CG    1 
ATOM   4457 C  CD1   . TRP B 1 60  ? 5.347   31.536  -0.365  1.00 30.33  ?  46  TRP B CD1   1 
ATOM   4458 C  CD2   . TRP B 1 60  ? 4.150   29.866  0.535   1.00 28.20  ?  46  TRP B CD2   1 
ATOM   4459 N  NE1   . TRP B 1 60  ? 6.205   30.493  -0.117  1.00 32.03  ?  46  TRP B NE1   1 
ATOM   4460 C  CE2   . TRP B 1 60  ? 5.498   29.455  0.433   1.00 29.62  ?  46  TRP B CE2   1 
ATOM   4461 C  CE3   . TRP B 1 60  ? 3.210   28.975  1.071   1.00 29.63  ?  46  TRP B CE3   1 
ATOM   4462 C  CZ2   . TRP B 1 60  ? 5.930   28.193  0.853   1.00 25.60  ?  46  TRP B CZ2   1 
ATOM   4463 C  CZ3   . TRP B 1 60  ? 3.637   27.719  1.481   1.00 26.92  ?  46  TRP B CZ3   1 
ATOM   4464 C  CH2   . TRP B 1 60  ? 4.990   27.342  1.372   1.00 27.46  ?  46  TRP B CH2   1 
ATOM   4465 N  N     . VAL B 1 61  ? 3.819   32.254  3.080   1.00 30.53  ?  47  VAL B N     1 
ATOM   4466 C  CA    . VAL B 1 61  ? 4.915   32.639  3.969   1.00 31.53  ?  47  VAL B CA    1 
ATOM   4467 C  C     . VAL B 1 61  ? 5.963   31.532  3.873   1.00 28.88  ?  47  VAL B C     1 
ATOM   4468 O  O     . VAL B 1 61  ? 5.871   30.506  4.553   1.00 29.81  ?  47  VAL B O     1 
ATOM   4469 C  CB    . VAL B 1 61  ? 4.460   32.850  5.416   1.00 31.42  ?  47  VAL B CB    1 
ATOM   4470 C  CG1   . VAL B 1 61  ? 5.658   33.182  6.294   1.00 25.80  ?  47  VAL B CG1   1 
ATOM   4471 C  CG2   . VAL B 1 61  ? 3.426   33.962  5.490   1.00 28.11  ?  47  VAL B CG2   1 
ATOM   4472 N  N     . GLY B 1 62  ? 6.950   31.719  3.000   1.00 25.13  ?  48  GLY B N     1 
ATOM   4473 C  CA    . GLY B 1 62  ? 8.042   30.764  2.916   1.00 31.33  ?  48  GLY B CA    1 
ATOM   4474 C  C     . GLY B 1 62  ? 8.914   30.818  4.159   1.00 32.37  ?  48  GLY B C     1 
ATOM   4475 O  O     . GLY B 1 62  ? 9.261   31.891  4.656   1.00 30.10  ?  48  GLY B O     1 
ATOM   4476 N  N     . CYS B 1 63  ? 9.286   29.644  4.657   1.00 28.99  ?  49  CYS B N     1 
ATOM   4477 C  CA    . CYS B 1 63  ? 10.077  29.538  5.874   1.00 29.81  ?  49  CYS B CA    1 
ATOM   4478 C  C     . CYS B 1 63  ? 11.464  28.988  5.561   1.00 31.15  ?  49  CYS B C     1 
ATOM   4479 O  O     . CYS B 1 63  ? 11.751  28.555  4.442   1.00 28.63  ?  49  CYS B O     1 
ATOM   4480 C  CB    . CYS B 1 63  ? 9.358   28.667  6.907   1.00 27.01  ?  49  CYS B CB    1 
ATOM   4481 S  SG    . CYS B 1 63  ? 7.796   29.401  7.478   1.00 32.19  ?  49  CYS B SG    1 
ATOM   4482 N  N     . ALA B 1 64  ? 12.345  29.048  6.563   1.00 27.15  ?  50  ALA B N     1 
ATOM   4483 C  CA    . ALA B 1 64  ? 13.728  28.638  6.342   1.00 33.28  ?  50  ALA B CA    1 
ATOM   4484 C  C     . ALA B 1 64  ? 13.905  27.120  6.412   1.00 29.36  ?  50  ALA B C     1 
ATOM   4485 O  O     . ALA B 1 64  ? 14.846  26.596  5.809   1.00 31.52  ?  50  ALA B O     1 
ATOM   4486 C  CB    . ALA B 1 64  ? 14.658  29.353  7.329   1.00 24.36  ?  50  ALA B CB    1 
ATOM   4487 N  N     . ASN B 1 65  ? 13.047  26.406  7.148   1.00 27.63  ?  51  ASN B N     1 
ATOM   4488 C  CA    . ASN B 1 65  ? 12.949  24.952  7.032   1.00 25.64  ?  51  ASN B CA    1 
ATOM   4489 C  C     . ASN B 1 65  ? 11.573  24.509  7.526   1.00 27.53  ?  51  ASN B C     1 
ATOM   4490 O  O     . ASN B 1 65  ? 10.819  25.288  8.116   1.00 26.32  ?  51  ASN B O     1 
ATOM   4491 C  CB    . ASN B 1 65  ? 14.099  24.215  7.756   1.00 23.03  ?  51  ASN B CB    1 
ATOM   4492 C  CG    . ASN B 1 65  ? 14.093  24.383  9.274   1.00 30.13  ?  51  ASN B CG    1 
ATOM   4493 O  OD1   . ASN B 1 65  ? 13.046  24.495  9.912   1.00 26.44  ?  51  ASN B OD1   1 
ATOM   4494 N  ND2   . ASN B 1 65  ? 15.292  24.347  9.866   1.00 23.53  ?  51  ASN B ND2   1 
ATOM   4495 N  N     . GLU B 1 66  ? 11.243  23.243  7.251   1.00 22.35  ?  52  GLU B N     1 
ATOM   4496 C  CA    . GLU B 1 66  ? 9.883   22.765  7.506   1.00 23.50  ?  52  GLU B CA    1 
ATOM   4497 C  C     . GLU B 1 66  ? 9.575   22.684  8.996   1.00 25.55  ?  52  GLU B C     1 
ATOM   4498 O  O     . GLU B 1 66  ? 8.435   22.933  9.409   1.00 25.06  ?  52  GLU B O     1 
ATOM   4499 C  CB    . GLU B 1 66  ? 9.658   21.407  6.848   1.00 22.12  ?  52  GLU B CB    1 
ATOM   4500 C  CG    . GLU B 1 66  ? 9.537   21.468  5.344   1.00 21.92  ?  52  GLU B CG    1 
ATOM   4501 C  CD    . GLU B 1 66  ? 10.895  21.403  4.665   1.00 31.97  ?  52  GLU B CD    1 
ATOM   4502 O  OE1   . GLU B 1 66  ? 11.929  21.402  5.375   1.00 24.60  ?  52  GLU B OE1   1 
ATOM   4503 O  OE2   . GLU B 1 66  ? 10.924  21.350  3.420   1.00 27.35  ?  52  GLU B OE2   1 
ATOM   4504 N  N     . LEU B 1 67  ? 10.556  22.296  9.818   1.00 26.32  ?  53  LEU B N     1 
ATOM   4505 C  CA    . LEU B 1 67  ? 10.308  22.234  11.256  1.00 22.51  ?  53  LEU B CA    1 
ATOM   4506 C  C     . LEU B 1 67  ? 9.923   23.604  11.799  1.00 25.85  ?  53  LEU B C     1 
ATOM   4507 O  O     . LEU B 1 67  ? 8.934   23.739  12.530  1.00 30.01  ?  53  LEU B O     1 
ATOM   4508 C  CB    . LEU B 1 67  ? 11.532  21.688  11.990  1.00 23.63  ?  53  LEU B CB    1 
ATOM   4509 C  CG    . LEU B 1 67  ? 11.311  21.501  13.495  1.00 29.69  ?  53  LEU B CG    1 
ATOM   4510 C  CD1   . LEU B 1 67  ? 10.063  20.645  13.763  1.00 23.37  ?  53  LEU B CD1   1 
ATOM   4511 C  CD2   . LEU B 1 67  ? 12.535  20.901  14.171  1.00 24.59  ?  53  LEU B CD2   1 
ATOM   4512 N  N     . ASN B 1 68  ? 10.674  24.642  11.415  1.00 27.80  ?  54  ASN B N     1 
ATOM   4513 C  CA    . ASN B 1 68  ? 10.338  25.999  11.836  1.00 23.94  ?  54  ASN B CA    1 
ATOM   4514 C  C     . ASN B 1 68  ? 8.980   26.408  11.290  1.00 23.21  ?  54  ASN B C     1 
ATOM   4515 O  O     . ASN B 1 68  ? 8.206   27.088  11.973  1.00 26.43  ?  54  ASN B O     1 
ATOM   4516 C  CB    . ASN B 1 68  ? 11.413  26.987  11.377  1.00 23.57  ?  54  ASN B CB    1 
ATOM   4517 C  CG    . ASN B 1 68  ? 12.768  26.723  12.010  1.00 30.99  ?  54  ASN B CG    1 
ATOM   4518 O  OD1   . ASN B 1 68  ? 12.942  25.763  12.762  1.00 31.24  ?  54  ASN B OD1   1 
ATOM   4519 N  ND2   . ASN B 1 68  ? 13.742  27.579  11.701  1.00 31.43  ?  54  ASN B ND2   1 
ATOM   4520 N  N     . ALA B 1 69  ? 8.681   26.008  10.053  1.00 26.23  ?  55  ALA B N     1 
ATOM   4521 C  CA    . ALA B 1 69  ? 7.380   26.308  9.468   1.00 23.84  ?  55  ALA B CA    1 
ATOM   4522 C  C     . ALA B 1 69  ? 6.254   25.703  10.291  1.00 26.06  ?  55  ALA B C     1 
ATOM   4523 O  O     . ALA B 1 69  ? 5.219   26.346  10.503  1.00 25.16  ?  55  ALA B O     1 
ATOM   4524 C  CB    . ALA B 1 69  ? 7.320   25.792  8.031   1.00 23.49  ?  55  ALA B CB    1 
ATOM   4525 N  N     . SER B 1 70  ? 6.438   24.470  10.779  1.00 26.72  ?  56  SER B N     1 
ATOM   4526 C  CA    . SER B 1 70  ? 5.393   23.847  11.587  1.00 28.62  ?  56  SER B CA    1 
ATOM   4527 C  C     . SER B 1 70  ? 5.270   24.521  12.951  1.00 26.66  ?  56  SER B C     1 
ATOM   4528 O  O     . SER B 1 70  ? 4.157   24.695  13.466  1.00 28.91  ?  56  SER B O     1 
ATOM   4529 C  CB    . SER B 1 70  ? 5.655   22.340  11.725  1.00 26.14  ?  56  SER B CB    1 
ATOM   4530 O  OG    . SER B 1 70  ? 6.773   22.057  12.539  1.00 24.32  ?  56  SER B OG    1 
ATOM   4531 N  N     . TYR B 1 71  ? 6.399   24.922  13.545  1.00 26.53  ?  57  TYR B N     1 
ATOM   4532 C  CA    . TYR B 1 71  ? 6.351   25.708  14.776  1.00 26.88  ?  57  TYR B CA    1 
ATOM   4533 C  C     . TYR B 1 71  ? 5.638   27.036  14.553  1.00 28.47  ?  57  TYR B C     1 
ATOM   4534 O  O     . TYR B 1 71  ? 4.831   27.470  15.385  1.00 30.49  ?  57  TYR B O     1 
ATOM   4535 C  CB    . TYR B 1 71  ? 7.766   25.982  15.292  1.00 33.58  ?  57  TYR B CB    1 
ATOM   4536 C  CG    . TYR B 1 71  ? 8.539   24.806  15.853  1.00 24.87  ?  57  TYR B CG    1 
ATOM   4537 C  CD1   . TYR B 1 71  ? 7.897   23.686  16.358  1.00 24.69  ?  57  TYR B CD1   1 
ATOM   4538 C  CD2   . TYR B 1 71  ? 9.927   24.846  15.910  1.00 29.63  ?  57  TYR B CD2   1 
ATOM   4539 C  CE1   . TYR B 1 71  ? 8.623   22.623  16.887  1.00 23.92  ?  57  TYR B CE1   1 
ATOM   4540 C  CE2   . TYR B 1 71  ? 10.657  23.796  16.429  1.00 26.26  ?  57  TYR B CE2   1 
ATOM   4541 C  CZ    . TYR B 1 71  ? 10.006  22.688  16.914  1.00 27.83  ?  57  TYR B CZ    1 
ATOM   4542 O  OH    . TYR B 1 71  ? 10.750  21.654  17.432  1.00 30.29  ?  57  TYR B OH    1 
ATOM   4543 N  N     . ALA B 1 72  ? 5.952   27.714  13.446  1.00 24.72  ?  58  ALA B N     1 
ATOM   4544 C  CA    . ALA B 1 72  ? 5.330   29.002  13.160  1.00 29.66  ?  58  ALA B CA    1 
ATOM   4545 C  C     . ALA B 1 72  ? 3.826   28.847  12.972  1.00 27.88  ?  58  ALA B C     1 
ATOM   4546 O  O     . ALA B 1 72  ? 3.042   29.671  13.458  1.00 27.53  ?  58  ALA B O     1 
ATOM   4547 C  CB    . ALA B 1 72  ? 5.971   29.637  11.925  1.00 24.24  ?  58  ALA B CB    1 
ATOM   4548 N  N     . ALA B 1 73  ? 3.407   27.791  12.272  1.00 24.62  ?  59  ALA B N     1 
ATOM   4549 C  CA    . ALA B 1 73  ? 1.980   27.528  12.109  1.00 30.98  ?  59  ALA B CA    1 
ATOM   4550 C  C     . ALA B 1 73  ? 1.304   27.325  13.459  1.00 25.03  ?  59  ALA B C     1 
ATOM   4551 O  O     . ALA B 1 73  ? 0.206   27.841  13.698  1.00 33.92  ?  59  ALA B O     1 
ATOM   4552 C  CB    . ALA B 1 73  ? 1.774   26.311  11.208  1.00 23.72  ?  59  ALA B CB    1 
ATOM   4553 N  N     . ASP B 1 74  ? 1.958   26.589  14.359  1.00 25.94  ?  60  ASP B N     1 
ATOM   4554 C  CA    . ASP B 1 74  ? 1.425   26.392  15.703  1.00 25.46  ?  60  ASP B CA    1 
ATOM   4555 C  C     . ASP B 1 74  ? 1.204   27.726  16.413  1.00 32.24  ?  60  ASP B C     1 
ATOM   4556 O  O     . ASP B 1 74  ? 0.113   27.992  16.931  1.00 28.52  ?  60  ASP B O     1 
ATOM   4557 C  CB    . ASP B 1 74  ? 2.377   25.495  16.501  1.00 24.70  ?  60  ASP B CB    1 
ATOM   4558 C  CG    . ASP B 1 74  ? 1.774   25.004  17.801  1.00 33.46  ?  60  ASP B CG    1 
ATOM   4559 O  OD1   . ASP B 1 74  ? 1.479   25.851  18.671  1.00 30.83  ?  60  ASP B OD1   1 
ATOM   4560 O  OD2   . ASP B 1 74  ? 1.617   23.771  17.963  1.00 25.00  ?  60  ASP B OD2   1 
ATOM   4561 N  N     . GLY B 1 75  ? 2.231   28.584  16.438  1.00 30.60  ?  61  GLY B N     1 
ATOM   4562 C  CA    . GLY B 1 75  ? 2.086   29.880  17.083  1.00 26.14  ?  61  GLY B CA    1 
ATOM   4563 C  C     . GLY B 1 75  ? 1.047   30.750  16.405  1.00 27.78  ?  61  GLY B C     1 
ATOM   4564 O  O     . GLY B 1 75  ? 0.302   31.478  17.064  1.00 27.07  ?  61  GLY B O     1 
ATOM   4565 N  N     . TYR B 1 76  ? 0.992   30.690  15.076  1.00 26.96  ?  62  TYR B N     1 
ATOM   4566 C  CA    . TYR B 1 76  ? -0.068  31.365  14.339  1.00 26.80  ?  62  TYR B CA    1 
ATOM   4567 C  C     . TYR B 1 76  ? -1.438  30.901  14.818  1.00 31.46  ?  62  TYR B C     1 
ATOM   4568 O  O     . TYR B 1 76  ? -2.306  31.723  15.134  1.00 27.39  ?  62  TYR B O     1 
ATOM   4569 C  CB    . TYR B 1 76  ? 0.109   31.092  12.847  1.00 25.85  ?  62  TYR B CB    1 
ATOM   4570 C  CG    . TYR B 1 76  ? -0.777  31.887  11.914  1.00 32.84  ?  62  TYR B CG    1 
ATOM   4571 C  CD1   . TYR B 1 76  ? -2.044  31.429  11.569  1.00 29.80  ?  62  TYR B CD1   1 
ATOM   4572 C  CD2   . TYR B 1 76  ? -0.332  33.078  11.346  1.00 28.98  ?  62  TYR B CD2   1 
ATOM   4573 C  CE1   . TYR B 1 76  ? -2.845  32.137  10.700  1.00 26.82  ?  62  TYR B CE1   1 
ATOM   4574 C  CE2   . TYR B 1 76  ? -1.125  33.794  10.477  1.00 28.12  ?  62  TYR B CE2   1 
ATOM   4575 C  CZ    . TYR B 1 76  ? -2.381  33.317  10.159  1.00 35.09  ?  62  TYR B CZ    1 
ATOM   4576 O  OH    . TYR B 1 76  ? -3.173  34.017  9.289   1.00 37.89  ?  62  TYR B OH    1 
ATOM   4577 N  N     . ALA B 1 77  ? -1.631  29.580  14.922  1.00 27.93  ?  63  ALA B N     1 
ATOM   4578 C  CA    . ALA B 1 77  ? -2.927  29.040  15.322  1.00 30.81  ?  63  ALA B CA    1 
ATOM   4579 C  C     . ALA B 1 77  ? -3.286  29.409  16.755  1.00 31.00  ?  63  ALA B C     1 
ATOM   4580 O  O     . ALA B 1 77  ? -4.473  29.548  17.077  1.00 30.77  ?  63  ALA B O     1 
ATOM   4581 C  CB    . ALA B 1 77  ? -2.939  27.521  15.146  1.00 26.18  ?  63  ALA B CB    1 
ATOM   4582 N  N     . ARG B 1 78  ? -2.291  29.581  17.626  1.00 27.36  ?  64  ARG B N     1 
ATOM   4583 C  CA    . ARG B 1 78  ? -2.573  30.058  18.975  1.00 28.12  ?  64  ARG B CA    1 
ATOM   4584 C  C     . ARG B 1 78  ? -2.980  31.527  19.000  1.00 29.95  ?  64  ARG B C     1 
ATOM   4585 O  O     . ARG B 1 78  ? -3.375  32.029  20.058  1.00 32.92  ?  64  ARG B O     1 
ATOM   4586 C  CB    . ARG B 1 78  ? -1.359  29.837  19.875  1.00 31.01  ?  64  ARG B CB    1 
ATOM   4587 C  CG    . ARG B 1 78  ? -0.971  28.372  20.040  1.00 30.20  ?  64  ARG B CG    1 
ATOM   4588 C  CD    . ARG B 1 78  ? 0.171   28.228  21.031  1.00 32.37  ?  64  ARG B CD    1 
ATOM   4589 N  NE    . ARG B 1 78  ? 0.576   26.842  21.217  1.00 27.67  ?  64  ARG B NE    1 
ATOM   4590 C  CZ    . ARG B 1 78  ? 0.957   26.328  22.379  1.00 36.83  ?  64  ARG B CZ    1 
ATOM   4591 N  NH1   . ARG B 1 78  ? 0.956   27.053  23.488  1.00 28.42  ?  64  ARG B NH1   1 
ATOM   4592 N  NH2   . ARG B 1 78  ? 1.362   25.059  22.426  1.00 35.02  ?  64  ARG B NH2   1 
ATOM   4593 N  N     . CYS B 1 79  ? -2.871  32.232  17.874  1.00 30.11  ?  65  CYS B N     1 
ATOM   4594 C  CA    . CYS B 1 79  ? -3.335  33.608  17.775  1.00 30.24  ?  65  CYS B CA    1 
ATOM   4595 C  C     . CYS B 1 79  ? -4.609  33.760  16.963  1.00 31.76  ?  65  CYS B C     1 
ATOM   4596 O  O     . CYS B 1 79  ? -5.436  34.607  17.299  1.00 32.38  ?  65  CYS B O     1 
ATOM   4597 C  CB    . CYS B 1 79  ? -2.246  34.494  17.158  1.00 35.84  ?  65  CYS B CB    1 
ATOM   4598 S  SG    . CYS B 1 79  ? -0.726  34.553  18.130  1.00 34.13  ?  65  CYS B SG    1 
ATOM   4599 N  N     . LYS B 1 80  ? -4.806  32.949  15.922  1.00 33.44  ?  66  LYS B N     1 
ATOM   4600 C  CA    . LYS B 1 80  ? -5.981  33.068  15.067  1.00 37.87  ?  66  LYS B CA    1 
ATOM   4601 C  C     . LYS B 1 80  ? -6.962  31.913  15.196  1.00 37.98  ?  66  LYS B C     1 
ATOM   4602 O  O     . LYS B 1 80  ? -8.047  31.982  14.609  1.00 40.96  ?  66  LYS B O     1 
ATOM   4603 C  CB    . LYS B 1 80  ? -5.558  33.190  13.597  1.00 37.86  ?  66  LYS B CB    1 
ATOM   4604 C  CG    . LYS B 1 80  ? -4.433  34.168  13.375  1.00 42.21  ?  66  LYS B CG    1 
ATOM   4605 C  CD    . LYS B 1 80  ? -4.942  35.473  12.799  1.00 43.93  ?  66  LYS B CD    1 
ATOM   4606 C  CE    . LYS B 1 80  ? -5.187  35.344  11.308  1.00 44.30  ?  66  LYS B CE    1 
ATOM   4607 N  NZ    . LYS B 1 80  ? -5.336  36.672  10.650  1.00 61.66  ?  66  LYS B NZ    1 
ATOM   4608 N  N     . GLY B 1 81  ? -6.625  30.867  15.942  1.00 34.73  ?  67  GLY B N     1 
ATOM   4609 C  CA    . GLY B 1 81  ? -7.512  29.734  16.110  1.00 38.39  ?  67  GLY B CA    1 
ATOM   4610 C  C     . GLY B 1 81  ? -7.365  28.641  15.072  1.00 35.47  ?  67  GLY B C     1 
ATOM   4611 O  O     . GLY B 1 81  ? -8.048  27.618  15.178  1.00 35.22  ?  67  GLY B O     1 
ATOM   4612 N  N     . PHE B 1 82  ? -6.488  28.814  14.086  1.00 32.33  ?  68  PHE B N     1 
ATOM   4613 C  CA    . PHE B 1 82  ? -6.327  27.867  12.990  1.00 29.89  ?  68  PHE B CA    1 
ATOM   4614 C  C     . PHE B 1 82  ? -5.083  28.259  12.209  1.00 31.59  ?  68  PHE B C     1 
ATOM   4615 O  O     . PHE B 1 82  ? -4.718  29.437  12.158  1.00 30.33  ?  68  PHE B O     1 
ATOM   4616 C  CB    . PHE B 1 82  ? -7.556  27.864  12.074  1.00 31.10  ?  68  PHE B CB    1 
ATOM   4617 C  CG    . PHE B 1 82  ? -7.759  26.583  11.310  1.00 34.97  ?  68  PHE B CG    1 
ATOM   4618 C  CD1   . PHE B 1 82  ? -7.162  26.395  10.074  1.00 29.12  ?  68  PHE B CD1   1 
ATOM   4619 C  CD2   . PHE B 1 82  ? -8.578  25.578  11.817  1.00 44.45  ?  68  PHE B CD2   1 
ATOM   4620 C  CE1   . PHE B 1 82  ? -7.355  25.218  9.366   1.00 31.24  ?  68  PHE B CE1   1 
ATOM   4621 C  CE2   . PHE B 1 82  ? -8.782  24.396  11.114  1.00 31.26  ?  68  PHE B CE2   1 
ATOM   4622 C  CZ    . PHE B 1 82  ? -8.174  24.221  9.884   1.00 37.77  ?  68  PHE B CZ    1 
ATOM   4623 N  N     . ALA B 1 83  ? -4.430  27.263  11.617  1.00 26.58  ?  69  ALA B N     1 
ATOM   4624 C  CA    . ALA B 1 83  ? -3.250  27.522  10.803  1.00 29.68  ?  69  ALA B CA    1 
ATOM   4625 C  C     . ALA B 1 83  ? -3.075  26.388  9.808   1.00 34.38  ?  69  ALA B C     1 
ATOM   4626 O  O     . ALA B 1 83  ? -3.694  25.328  9.923   1.00 33.38  ?  69  ALA B O     1 
ATOM   4627 C  CB    . ALA B 1 83  ? -1.994  27.680  11.659  1.00 27.85  ?  69  ALA B CB    1 
ATOM   4628 N  N     . ALA B 1 84  ? -2.230  26.637  8.812   1.00 27.99  ?  70  ALA B N     1 
ATOM   4629 C  CA    . ALA B 1 84  ? -1.960  25.649  7.782   1.00 29.15  ?  70  ALA B CA    1 
ATOM   4630 C  C     . ALA B 1 84  ? -0.475  25.641  7.446   1.00 35.96  ?  70  ALA B C     1 
ATOM   4631 O  O     . ALA B 1 84  ? 0.184   26.688  7.437   1.00 28.22  ?  70  ALA B O     1 
ATOM   4632 C  CB    . ALA B 1 84  ? -2.782  25.914  6.527   1.00 31.10  ?  70  ALA B CB    1 
ATOM   4633 N  N     . LEU B 1 85  ? 0.036   24.444  7.180   1.00 28.12  ?  71  LEU B N     1 
ATOM   4634 C  CA    . LEU B 1 85  ? 1.421   24.208  6.818   1.00 34.25  ?  71  LEU B CA    1 
ATOM   4635 C  C     . LEU B 1 85  ? 1.447   23.447  5.502   1.00 30.28  ?  71  LEU B C     1 
ATOM   4636 O  O     . LEU B 1 85  ? 0.638   22.542  5.289   1.00 29.57  ?  71  LEU B O     1 
ATOM   4637 C  CB    . LEU B 1 85  ? 2.144   23.410  7.920   1.00 35.95  ?  71  LEU B CB    1 
ATOM   4638 C  CG    . LEU B 1 85  ? 3.385   22.614  7.529   1.00 35.09  ?  71  LEU B CG    1 
ATOM   4639 C  CD1   . LEU B 1 85  ? 4.546   23.562  7.295   1.00 30.73  ?  71  LEU B CD1   1 
ATOM   4640 C  CD2   . LEU B 1 85  ? 3.731   21.578  8.600   1.00 34.76  ?  71  LEU B CD2   1 
ATOM   4641 N  N     . LEU B 1 86  ? 2.348   23.835  4.604   1.00 25.80  ?  72  LEU B N     1 
ATOM   4642 C  CA    . LEU B 1 86  ? 2.521   23.144  3.332   1.00 28.24  ?  72  LEU B CA    1 
ATOM   4643 C  C     . LEU B 1 86  ? 3.951   22.625  3.240   1.00 31.90  ?  72  LEU B C     1 
ATOM   4644 O  O     . LEU B 1 86  ? 4.903   23.401  3.362   1.00 27.19  ?  72  LEU B O     1 
ATOM   4645 C  CB    . LEU B 1 86  ? 2.213   24.067  2.155   1.00 25.41  ?  72  LEU B CB    1 
ATOM   4646 C  CG    . LEU B 1 86  ? 2.627   23.492  0.800   1.00 29.34  ?  72  LEU B CG    1 
ATOM   4647 C  CD1   . LEU B 1 86  ? 1.673   22.393  0.352   1.00 23.17  ?  72  LEU B CD1   1 
ATOM   4648 C  CD2   . LEU B 1 86  ? 2.729   24.584  -0.244  1.00 30.03  ?  72  LEU B CD2   1 
ATOM   4649 N  N     . THR B 1 87  ? 4.107   21.322  3.027   1.00 27.57  ?  73  THR B N     1 
ATOM   4650 C  CA    . THR B 1 87  ? 5.424   20.738  2.820   1.00 25.43  ?  73  THR B CA    1 
ATOM   4651 C  C     . THR B 1 87  ? 5.399   19.894  1.556   1.00 27.83  ?  73  THR B C     1 
ATOM   4652 O  O     . THR B 1 87  ? 4.347   19.662  0.952   1.00 28.04  ?  73  THR B O     1 
ATOM   4653 C  CB    . THR B 1 87  ? 5.880   19.877  4.006   1.00 27.39  ?  73  THR B CB    1 
ATOM   4654 O  OG1   . THR B 1 87  ? 5.026   18.731  4.124   1.00 28.35  ?  73  THR B OG1   1 
ATOM   4655 C  CG2   . THR B 1 87  ? 5.852   20.671  5.301   1.00 21.80  ?  73  THR B CG2   1 
ATOM   4656 N  N     . THR B 1 88  ? 6.575   19.443  1.146   1.00 26.25  ?  74  THR B N     1 
ATOM   4657 C  CA    . THR B 1 88  ? 6.675   18.546  0.011   1.00 28.77  ?  74  THR B CA    1 
ATOM   4658 C  C     . THR B 1 88  ? 6.745   17.104  0.499   1.00 29.37  ?  74  THR B C     1 
ATOM   4659 O  O     . THR B 1 88  ? 7.181   16.827  1.623   1.00 27.35  ?  74  THR B O     1 
ATOM   4660 C  CB    . THR B 1 88  ? 7.892   18.881  -0.858  1.00 32.92  ?  74  THR B CB    1 
ATOM   4661 O  OG1   . THR B 1 88  ? 7.765   18.220  -2.123  1.00 40.97  ?  74  THR B OG1   1 
ATOM   4662 C  CG2   . THR B 1 88  ? 9.180   18.431  -0.190  1.00 29.21  ?  74  THR B CG2   1 
ATOM   4663 N  N     . PHE B 1 89  ? 6.288   16.193  -0.363  1.00 28.52  ?  75  PHE B N     1 
ATOM   4664 C  CA    . PHE B 1 89  ? 6.220   14.769  -0.051  1.00 22.08  ?  75  PHE B CA    1 
ATOM   4665 C  C     . PHE B 1 89  ? 7.564   14.257  0.445   1.00 25.60  ?  75  PHE B C     1 
ATOM   4666 O  O     . PHE B 1 89  ? 8.605   14.547  -0.146  1.00 24.07  ?  75  PHE B O     1 
ATOM   4667 C  CB    . PHE B 1 89  ? 5.797   13.993  -1.301  1.00 26.57  ?  75  PHE B CB    1 
ATOM   4668 C  CG    . PHE B 1 89  ? 5.737   12.503  -1.106  1.00 31.36  ?  75  PHE B CG    1 
ATOM   4669 C  CD1   . PHE B 1 89  ? 4.569   11.896  -0.667  1.00 31.25  ?  75  PHE B CD1   1 
ATOM   4670 C  CD2   . PHE B 1 89  ? 6.848   11.705  -1.371  1.00 24.91  ?  75  PHE B CD2   1 
ATOM   4671 C  CE1   . PHE B 1 89  ? 4.509   10.525  -0.486  1.00 29.09  ?  75  PHE B CE1   1 
ATOM   4672 C  CE2   . PHE B 1 89  ? 6.793   10.338  -1.190  1.00 28.65  ?  75  PHE B CE2   1 
ATOM   4673 C  CZ    . PHE B 1 89  ? 5.620   9.746   -0.747  1.00 27.09  ?  75  PHE B CZ    1 
ATOM   4674 N  N     . GLY B 1 90  ? 7.542   13.527  1.558   1.00 25.76  ?  76  GLY B N     1 
ATOM   4675 C  CA    . GLY B 1 90  ? 8.742   12.863  2.028   1.00 26.46  ?  76  GLY B CA    1 
ATOM   4676 C  C     . GLY B 1 90  ? 9.634   13.743  2.881   1.00 25.13  ?  76  GLY B C     1 
ATOM   4677 O  O     . GLY B 1 90  ? 9.473   13.806  4.105   1.00 26.17  ?  76  GLY B O     1 
ATOM   4678 N  N     . VAL B 1 91  ? 10.590  14.420  2.238   1.00 23.65  ?  77  VAL B N     1 
ATOM   4679 C  CA    . VAL B 1 91  ? 11.590  15.210  2.962   1.00 29.43  ?  77  VAL B CA    1 
ATOM   4680 C  C     . VAL B 1 91  ? 10.956  16.384  3.697   1.00 26.01  ?  77  VAL B C     1 
ATOM   4681 O  O     . VAL B 1 91  ? 11.418  16.772  4.778   1.00 28.77  ?  77  VAL B O     1 
ATOM   4682 C  CB    . VAL B 1 91  ? 12.692  15.697  2.002   1.00 27.19  ?  77  VAL B CB    1 
ATOM   4683 C  CG1   . VAL B 1 91  ? 13.456  14.516  1.427   1.00 23.28  ?  77  VAL B CG1   1 
ATOM   4684 C  CG2   . VAL B 1 91  ? 12.096  16.544  0.888   1.00 25.54  ?  77  VAL B CG2   1 
ATOM   4685 N  N     . GLY B 1 92  ? 9.912   16.984  3.125   1.00 27.62  ?  78  GLY B N     1 
ATOM   4686 C  CA    . GLY B 1 92  ? 9.283   18.116  3.782   1.00 25.58  ?  78  GLY B CA    1 
ATOM   4687 C  C     . GLY B 1 92  ? 8.438   17.688  4.965   1.00 31.09  ?  78  GLY B C     1 
ATOM   4688 O  O     . GLY B 1 92  ? 8.632   18.169  6.085   1.00 26.55  ?  78  GLY B O     1 
ATOM   4689 N  N     . GLU B 1 93  ? 7.505   16.754  4.735   1.00 24.59  ?  79  GLU B N     1 
ATOM   4690 C  CA    . GLU B 1 93  ? 6.559   16.380  5.780   1.00 24.77  ?  79  GLU B CA    1 
ATOM   4691 C  C     . GLU B 1 93  ? 7.256   15.719  6.962   1.00 26.22  ?  79  GLU B C     1 
ATOM   4692 O  O     . GLU B 1 93  ? 6.881   15.957  8.115   1.00 29.48  ?  79  GLU B O     1 
ATOM   4693 C  CB    . GLU B 1 93  ? 5.464   15.468  5.213   1.00 26.12  ?  79  GLU B CB    1 
ATOM   4694 C  CG    . GLU B 1 93  ? 5.910   14.058  4.818   1.00 23.88  ?  79  GLU B CG    1 
ATOM   4695 C  CD    . GLU B 1 93  ? 4.817   13.298  4.088   1.00 30.73  ?  79  GLU B CD    1 
ATOM   4696 O  OE1   . GLU B 1 93  ? 3.775   13.012  4.723   1.00 24.88  ?  79  GLU B OE1   1 
ATOM   4697 O  OE2   . GLU B 1 93  ? 4.999   12.980  2.889   1.00 24.36  ?  79  GLU B OE2   1 
ATOM   4698 N  N     . LEU B 1 94  ? 8.269   14.884  6.709   1.00 22.40  ?  80  LEU B N     1 
ATOM   4699 C  CA    . LEU B 1 94  ? 8.962   14.249  7.827   1.00 24.65  ?  80  LEU B CA    1 
ATOM   4700 C  C     . LEU B 1 94  ? 9.755   15.265  8.635   1.00 23.55  ?  80  LEU B C     1 
ATOM   4701 O  O     . LEU B 1 94  ? 9.885   15.119  9.857   1.00 26.06  ?  80  LEU B O     1 
ATOM   4702 C  CB    . LEU B 1 94  ? 9.876   13.125  7.325   1.00 22.45  ?  80  LEU B CB    1 
ATOM   4703 C  CG    . LEU B 1 94  ? 9.149   11.902  6.744   1.00 24.74  ?  80  LEU B CG    1 
ATOM   4704 C  CD1   . LEU B 1 94  ? 10.097  10.723  6.597   1.00 21.91  ?  80  LEU B CD1   1 
ATOM   4705 C  CD2   . LEU B 1 94  ? 7.940   11.511  7.586   1.00 26.27  ?  80  LEU B CD2   1 
ATOM   4706 N  N     . SER B 1 95  ? 10.267  16.311  7.983   1.00 21.87  ?  81  SER B N     1 
ATOM   4707 C  CA    . SER B 1 95  ? 10.949  17.371  8.717   1.00 21.84  ?  81  SER B CA    1 
ATOM   4708 C  C     . SER B 1 95  ? 10.000  18.091  9.669   1.00 28.49  ?  81  SER B C     1 
ATOM   4709 O  O     . SER B 1 95  ? 10.429  18.569  10.727  1.00 26.97  ?  81  SER B O     1 
ATOM   4710 C  CB    . SER B 1 95  ? 11.581  18.361  7.739   1.00 25.23  ?  81  SER B CB    1 
ATOM   4711 O  OG    . SER B 1 95  ? 12.697  17.782  7.072   1.00 25.49  ?  81  SER B OG    1 
ATOM   4712 N  N     . ALA B 1 96  ? 8.711   18.159  9.327   1.00 24.78  ?  82  ALA B N     1 
ATOM   4713 C  CA    . ALA B 1 96  ? 7.716   18.861  10.132  1.00 21.85  ?  82  ALA B CA    1 
ATOM   4714 C  C     . ALA B 1 96  ? 7.089   17.990  11.213  1.00 28.24  ?  82  ALA B C     1 
ATOM   4715 O  O     . ALA B 1 96  ? 6.243   18.488  11.970  1.00 24.06  ?  82  ALA B O     1 
ATOM   4716 C  CB    . ALA B 1 96  ? 6.610   19.414  9.230   1.00 21.79  ?  82  ALA B CB    1 
ATOM   4717 N  N     . MET B 1 97  ? 7.512   16.723  11.321  1.00 23.53  ?  83  MET B N     1 
ATOM   4718 C  CA    . MET B 1 97  ? 6.832   15.756  12.182  1.00 22.09  ?  83  MET B CA    1 
ATOM   4719 C  C     . MET B 1 97  ? 6.799   16.212  13.634  1.00 27.93  ?  83  MET B C     1 
ATOM   4720 O  O     . MET B 1 97  ? 5.763   16.108  14.301  1.00 27.23  ?  83  MET B O     1 
ATOM   4721 C  CB    . MET B 1 97  ? 7.524   14.397  12.071  1.00 22.98  ?  83  MET B CB    1 
ATOM   4722 C  CG    . MET B 1 97  ? 6.610   13.203  12.197  1.00 42.61  ?  83  MET B CG    1 
ATOM   4723 S  SD    . MET B 1 97  ? 5.547   13.044  10.752  1.00 77.19  ?  83  MET B SD    1 
ATOM   4724 C  CE    . MET B 1 97  ? 5.598   11.277  10.516  1.00 35.36  ?  83  MET B CE    1 
ATOM   4725 N  N     . ASN B 1 98  ? 7.920   16.721  14.146  1.00 22.57  ?  84  ASN B N     1 
ATOM   4726 C  CA    . ASN B 1 98  ? 7.953   17.143  15.543  1.00 23.95  ?  84  ASN B CA    1 
ATOM   4727 C  C     . ASN B 1 98  ? 7.024   18.326  15.802  1.00 29.55  ?  84  ASN B C     1 
ATOM   4728 O  O     . ASN B 1 98  ? 6.449   18.431  16.893  1.00 27.17  ?  84  ASN B O     1 
ATOM   4729 C  CB    . ASN B 1 98  ? 9.385   17.484  15.955  1.00 23.21  ?  84  ASN B CB    1 
ATOM   4730 C  CG    . ASN B 1 98  ? 9.513   17.738  17.440  1.00 33.60  ?  84  ASN B CG    1 
ATOM   4731 O  OD1   . ASN B 1 98  ? 8.974   16.988  18.251  1.00 28.67  ?  84  ASN B OD1   1 
ATOM   4732 N  ND2   . ASN B 1 98  ? 10.221  18.806  17.807  1.00 26.03  ?  84  ASN B ND2   1 
ATOM   4733 N  N     . GLY B 1 99  ? 6.868   19.226  14.828  1.00 22.86  ?  85  GLY B N     1 
ATOM   4734 C  CA    . GLY B 1 99  ? 5.945   20.338  15.012  1.00 29.24  ?  85  GLY B CA    1 
ATOM   4735 C  C     . GLY B 1 99  ? 4.494   19.893  15.073  1.00 25.78  ?  85  GLY B C     1 
ATOM   4736 O  O     . GLY B 1 99  ? 3.736   20.323  15.946  1.00 25.53  ?  85  GLY B O     1 
ATOM   4737 N  N     . ILE B 1 100 ? 4.094   19.009  14.155  1.00 25.53  ?  86  ILE B N     1 
ATOM   4738 C  CA    . ILE B 1 100 ? 2.724   18.504  14.148  1.00 25.75  ?  86  ILE B CA    1 
ATOM   4739 C  C     . ILE B 1 100 ? 2.427   17.734  15.430  1.00 29.76  ?  86  ILE B C     1 
ATOM   4740 O  O     . ILE B 1 100 ? 1.341   17.859  16.010  1.00 27.86  ?  86  ILE B O     1 
ATOM   4741 C  CB    . ILE B 1 100 ? 2.484   17.640  12.897  1.00 25.42  ?  86  ILE B CB    1 
ATOM   4742 C  CG1   . ILE B 1 100 ? 2.591   18.503  11.635  1.00 28.67  ?  86  ILE B CG1   1 
ATOM   4743 C  CG2   . ILE B 1 100 ? 1.124   16.934  12.972  1.00 22.86  ?  86  ILE B CG2   1 
ATOM   4744 C  CD1   . ILE B 1 100 ? 1.729   19.765  11.675  1.00 24.30  ?  86  ILE B CD1   1 
ATOM   4745 N  N     . ALA B 1 101 ? 3.390   16.936  15.901  1.00 27.85  ?  87  ALA B N     1 
ATOM   4746 C  CA    . ALA B 1 101 ? 3.193   16.197  17.145  1.00 31.31  ?  87  ALA B CA    1 
ATOM   4747 C  C     . ALA B 1 101 ? 2.978   17.141  18.323  1.00 32.64  ?  87  ALA B C     1 
ATOM   4748 O  O     . ALA B 1 101 ? 2.126   16.889  19.184  1.00 28.37  ?  87  ALA B O     1 
ATOM   4749 C  CB    . ALA B 1 101 ? 4.388   15.284  17.407  1.00 23.71  ?  87  ALA B CB    1 
ATOM   4750 N  N     . GLY B 1 102 ? 3.746   18.233  18.383  1.00 25.91  ?  88  GLY B N     1 
ATOM   4751 C  CA    . GLY B 1 102 ? 3.521   19.216  19.430  1.00 28.81  ?  88  GLY B CA    1 
ATOM   4752 C  C     . GLY B 1 102 ? 2.148   19.857  19.343  1.00 27.82  ?  88  GLY B C     1 
ATOM   4753 O  O     . GLY B 1 102 ? 1.505   20.117  20.365  1.00 29.97  ?  88  GLY B O     1 
ATOM   4754 N  N     . SER B 1 103 ? 1.685   20.131  18.123  1.00 24.53  ?  89  SER B N     1 
ATOM   4755 C  CA    . SER B 1 103 ? 0.341   20.674  17.950  1.00 28.40  ?  89  SER B CA    1 
ATOM   4756 C  C     . SER B 1 103 ? -0.720  19.679  18.412  1.00 25.13  ?  89  SER B C     1 
ATOM   4757 O  O     . SER B 1 103 ? -1.712  20.064  19.039  1.00 26.58  ?  89  SER B O     1 
ATOM   4758 C  CB    . SER B 1 103 ? 0.126   21.076  16.492  1.00 25.77  ?  89  SER B CB    1 
ATOM   4759 O  OG    . SER B 1 103 ? 1.091   22.037  16.089  1.00 28.33  ?  89  SER B OG    1 
ATOM   4760 N  N     . TYR B 1 104 ? -0.529  18.392  18.115  1.00 25.26  ?  90  TYR B N     1 
ATOM   4761 C  CA    . TYR B 1 104 ? -1.459  17.382  18.618  1.00 30.17  ?  90  TYR B CA    1 
ATOM   4762 C  C     . TYR B 1 104 ? -1.422  17.300  20.142  1.00 31.65  ?  90  TYR B C     1 
ATOM   4763 O  O     . TYR B 1 104 ? -2.474  17.268  20.794  1.00 29.70  ?  90  TYR B O     1 
ATOM   4764 C  CB    . TYR B 1 104 ? -1.141  16.024  17.992  1.00 30.02  ?  90  TYR B CB    1 
ATOM   4765 C  CG    . TYR B 1 104 ? -2.121  14.926  18.341  1.00 28.45  ?  90  TYR B CG    1 
ATOM   4766 C  CD1   . TYR B 1 104 ? -1.976  14.184  19.507  1.00 28.34  ?  90  TYR B CD1   1 
ATOM   4767 C  CD2   . TYR B 1 104 ? -3.187  14.622  17.498  1.00 27.55  ?  90  TYR B CD2   1 
ATOM   4768 C  CE1   . TYR B 1 104 ? -2.867  13.171  19.830  1.00 32.66  ?  90  TYR B CE1   1 
ATOM   4769 C  CE2   . TYR B 1 104 ? -4.083  13.606  17.813  1.00 32.85  ?  90  TYR B CE2   1 
ATOM   4770 C  CZ    . TYR B 1 104 ? -3.915  12.885  18.980  1.00 33.75  ?  90  TYR B CZ    1 
ATOM   4771 O  OH    . TYR B 1 104 ? -4.796  11.876  19.305  1.00 35.58  ?  90  TYR B OH    1 
ATOM   4772 N  N     . ALA B 1 105 ? -0.219  17.297  20.728  1.00 28.18  ?  91  ALA B N     1 
ATOM   4773 C  CA    . ALA B 1 105 ? -0.094  17.164  22.178  1.00 26.55  ?  91  ALA B CA    1 
ATOM   4774 C  C     . ALA B 1 105 ? -0.774  18.320  22.903  1.00 33.87  ?  91  ALA B C     1 
ATOM   4775 O  O     . ALA B 1 105 ? -1.422  18.124  23.939  1.00 31.27  ?  91  ALA B O     1 
ATOM   4776 C  CB    . ALA B 1 105 ? 1.383   17.085  22.572  1.00 26.77  ?  91  ALA B CB    1 
ATOM   4777 N  N     . GLU B 1 106 ? -0.647  19.532  22.374  1.00 26.92  ?  92  GLU B N     1 
ATOM   4778 C  CA    . GLU B 1 106 ? -1.167  20.716  23.038  1.00 34.16  ?  92  GLU B CA    1 
ATOM   4779 C  C     . GLU B 1 106 ? -2.447  21.234  22.388  1.00 30.63  ?  92  GLU B C     1 
ATOM   4780 O  O     . GLU B 1 106 ? -2.846  22.375  22.652  1.00 28.04  ?  92  GLU B O     1 
ATOM   4781 C  CB    . GLU B 1 106 ? -0.097  21.812  23.076  1.00 29.70  ?  92  GLU B CB    1 
ATOM   4782 C  CG    . GLU B 1 106 ? 1.300   21.332  23.476  1.00 27.57  ?  92  GLU B CG    1 
ATOM   4783 C  CD    . GLU B 1 106 ? 1.906   22.136  24.628  1.00 41.44  ?  92  GLU B CD    1 
ATOM   4784 O  OE1   . GLU B 1 106 ? 1.540   23.330  24.788  1.00 37.30  ?  92  GLU B OE1   1 
ATOM   4785 O  OE2   . GLU B 1 106 ? 2.782   21.594  25.345  1.00 28.18  ?  92  GLU B OE2   1 
ATOM   4786 N  N     . HIS B 1 107 ? -3.077  20.430  21.527  1.00 27.90  ?  93  HIS B N     1 
ATOM   4787 C  CA    . HIS B 1 107 ? -4.393  20.730  20.962  1.00 32.15  ?  93  HIS B CA    1 
ATOM   4788 C  C     . HIS B 1 107 ? -4.373  22.049  20.184  1.00 32.76  ?  93  HIS B C     1 
ATOM   4789 O  O     . HIS B 1 107 ? -5.069  23.008  20.519  1.00 33.98  ?  93  HIS B O     1 
ATOM   4790 C  CB    . HIS B 1 107 ? -5.465  20.761  22.057  1.00 32.20  ?  93  HIS B CB    1 
ATOM   4791 C  CG    . HIS B 1 107 ? -5.630  19.466  22.789  1.00 45.92  ?  93  HIS B CG    1 
ATOM   4792 N  ND1   . HIS B 1 107 ? -6.810  18.751  22.784  1.00 41.70  ?  93  HIS B ND1   1 
ATOM   4793 C  CD2   . HIS B 1 107 ? -4.758  18.747  23.537  1.00 33.40  ?  93  HIS B CD2   1 
ATOM   4794 C  CE1   . HIS B 1 107 ? -6.664  17.661  23.516  1.00 32.67  ?  93  HIS B CE1   1 
ATOM   4795 N  NE2   . HIS B 1 107 ? -5.426  17.633  23.979  1.00 36.22  ?  93  HIS B NE2   1 
ATOM   4796 N  N     . VAL B 1 108 ? -3.558  22.084  19.137  1.00 28.03  ?  94  VAL B N     1 
ATOM   4797 C  CA    . VAL B 1 108 ? -3.440  23.245  18.266  1.00 28.56  ?  94  VAL B CA    1 
ATOM   4798 C  C     . VAL B 1 108 ? -3.894  22.833  16.870  1.00 33.86  ?  94  VAL B C     1 
ATOM   4799 O  O     . VAL B 1 108 ? -3.326  21.906  16.286  1.00 30.70  ?  94  VAL B O     1 
ATOM   4800 C  CB    . VAL B 1 108 ? -2.006  23.804  18.233  1.00 39.14  ?  94  VAL B CB    1 
ATOM   4801 C  CG1   . VAL B 1 108 ? -1.950  25.055  17.391  1.00 28.50  ?  94  VAL B CG1   1 
ATOM   4802 C  CG2   . VAL B 1 108 ? -1.525  24.110  19.641  1.00 32.18  ?  94  VAL B CG2   1 
ATOM   4803 N  N     . PRO B 1 109 ? -4.917  23.474  16.300  1.00 35.90  ?  95  PRO B N     1 
ATOM   4804 C  CA    . PRO B 1 109 ? -5.417  23.058  14.981  1.00 30.80  ?  95  PRO B CA    1 
ATOM   4805 C  C     . PRO B 1 109 ? -4.570  23.546  13.812  1.00 35.99  ?  95  PRO B C     1 
ATOM   4806 O  O     . PRO B 1 109 ? -4.844  24.609  13.242  1.00 31.43  ?  95  PRO B O     1 
ATOM   4807 C  CB    . PRO B 1 109 ? -6.828  23.655  14.944  1.00 28.90  ?  95  PRO B CB    1 
ATOM   4808 C  CG    . PRO B 1 109 ? -6.751  24.843  15.851  1.00 30.09  ?  95  PRO B CG    1 
ATOM   4809 C  CD    . PRO B 1 109 ? -5.790  24.478  16.939  1.00 32.38  ?  95  PRO B CD    1 
ATOM   4810 N  N     . VAL B 1 110 ? -3.535  22.782  13.458  1.00 26.48  ?  96  VAL B N     1 
ATOM   4811 C  CA    . VAL B 1 110 ? -2.665  23.073  12.320  1.00 29.73  ?  96  VAL B CA    1 
ATOM   4812 C  C     . VAL B 1 110 ? -2.948  22.065  11.212  1.00 29.15  ?  96  VAL B C     1 
ATOM   4813 O  O     . VAL B 1 110 ? -2.873  20.850  11.438  1.00 31.11  ?  96  VAL B O     1 
ATOM   4814 C  CB    . VAL B 1 110 ? -1.179  23.035  12.731  1.00 28.76  ?  96  VAL B CB    1 
ATOM   4815 C  CG1   . VAL B 1 110 ? -0.278  23.012  11.511  1.00 23.53  ?  96  VAL B CG1   1 
ATOM   4816 C  CG2   . VAL B 1 110 ? -0.845  24.226  13.624  1.00 31.07  ?  96  VAL B CG2   1 
ATOM   4817 N  N     . LEU B 1 111 ? -3.262  22.560  10.014  1.00 26.24  ?  97  LEU B N     1 
ATOM   4818 C  CA    . LEU B 1 111 ? -3.514  21.692  8.865   1.00 24.01  ?  97  LEU B CA    1 
ATOM   4819 C  C     . LEU B 1 111 ? -2.207  21.451  8.120   1.00 36.58  ?  97  LEU B C     1 
ATOM   4820 O  O     . LEU B 1 111 ? -1.535  22.404  7.703   1.00 27.69  ?  97  LEU B O     1 
ATOM   4821 C  CB    . LEU B 1 111 ? -4.554  22.301  7.924   1.00 24.46  ?  97  LEU B CB    1 
ATOM   4822 C  CG    . LEU B 1 111 ? -4.752  21.555  6.595   1.00 32.35  ?  97  LEU B CG    1 
ATOM   4823 C  CD1   . LEU B 1 111 ? -5.347  20.153  6.797   1.00 26.17  ?  97  LEU B CD1   1 
ATOM   4824 C  CD2   . LEU B 1 111 ? -5.622  22.362  5.638   1.00 31.43  ?  97  LEU B CD2   1 
ATOM   4825 N  N     . HIS B 1 112 ? -1.843  20.181  7.963   1.00 28.73  ?  98  HIS B N     1 
ATOM   4826 C  CA    . HIS B 1 112 ? -0.633  19.794  7.246   1.00 27.65  ?  98  HIS B CA    1 
ATOM   4827 C  C     . HIS B 1 112 ? -1.029  19.361  5.839   1.00 22.82  ?  98  HIS B C     1 
ATOM   4828 O  O     . HIS B 1 112 ? -1.615  18.292  5.655   1.00 25.58  ?  98  HIS B O     1 
ATOM   4829 C  CB    . HIS B 1 112 ? 0.101   18.674  7.982   1.00 26.23  ?  98  HIS B CB    1 
ATOM   4830 C  CG    . HIS B 1 112 ? 1.486   18.420  7.472   1.00 25.98  ?  98  HIS B CG    1 
ATOM   4831 N  ND1   . HIS B 1 112 ? 2.280   17.399  7.949   1.00 25.95  ?  98  HIS B ND1   1 
ATOM   4832 C  CD2   . HIS B 1 112 ? 2.219   19.056  6.526   1.00 27.65  ?  98  HIS B CD2   1 
ATOM   4833 C  CE1   . HIS B 1 112 ? 3.443   17.418  7.322   1.00 28.27  ?  98  HIS B CE1   1 
ATOM   4834 N  NE2   . HIS B 1 112 ? 3.432   18.412  6.453   1.00 26.45  ?  98  HIS B NE2   1 
ATOM   4835 N  N     . ILE B 1 113 ? -0.705  20.189  4.855   1.00 25.42  ?  99  ILE B N     1 
ATOM   4836 C  CA    . ILE B 1 113 ? -0.915  19.877  3.448   1.00 24.68  ?  99  ILE B CA    1 
ATOM   4837 C  C     . ILE B 1 113 ? 0.404   19.378  2.887   1.00 28.18  ?  99  ILE B C     1 
ATOM   4838 O  O     . ILE B 1 113 ? 1.429   20.065  2.988   1.00 28.05  ?  99  ILE B O     1 
ATOM   4839 C  CB    . ILE B 1 113 ? -1.408  21.104  2.664   1.00 28.19  ?  99  ILE B CB    1 
ATOM   4840 C  CG1   . ILE B 1 113 ? -2.589  21.772  3.376   1.00 29.80  ?  99  ILE B CG1   1 
ATOM   4841 C  CG2   . ILE B 1 113 ? -1.768  20.714  1.231   1.00 24.34  ?  99  ILE B CG2   1 
ATOM   4842 C  CD1   . ILE B 1 113 ? -2.854  23.209  2.891   1.00 31.80  ?  99  ILE B CD1   1 
ATOM   4843 N  N     . VAL B 1 114 ? 0.389   18.190  2.294   1.00 26.87  ?  100 VAL B N     1 
ATOM   4844 C  CA    . VAL B 1 114 ? 1.585   17.586  1.725   1.00 26.85  ?  100 VAL B CA    1 
ATOM   4845 C  C     . VAL B 1 114 ? 1.404   17.527  0.215   1.00 28.94  ?  100 VAL B C     1 
ATOM   4846 O  O     . VAL B 1 114 ? 0.500   16.844  -0.281  1.00 29.17  ?  100 VAL B O     1 
ATOM   4847 C  CB    . VAL B 1 114 ? 1.845   16.193  2.318   1.00 31.79  ?  100 VAL B CB    1 
ATOM   4848 C  CG1   . VAL B 1 114 ? 3.057   15.540  1.663   1.00 25.97  ?  100 VAL B CG1   1 
ATOM   4849 C  CG2   . VAL B 1 114 ? 2.038   16.292  3.828   1.00 27.03  ?  100 VAL B CG2   1 
ATOM   4850 N  N     . GLY B 1 115 ? 2.250   18.250  -0.518  1.00 26.20  ?  101 GLY B N     1 
ATOM   4851 C  CA    . GLY B 1 115 ? 2.257   18.138  -1.968  1.00 29.20  ?  101 GLY B CA    1 
ATOM   4852 C  C     . GLY B 1 115 ? 2.950   16.850  -2.381  1.00 36.16  ?  101 GLY B C     1 
ATOM   4853 O  O     . GLY B 1 115 ? 4.088   16.585  -1.978  1.00 28.55  ?  101 GLY B O     1 
ATOM   4854 N  N     . ALA B 1 116 ? 2.276   16.060  -3.204  1.00 28.12  ?  102 ALA B N     1 
ATOM   4855 C  CA    . ALA B 1 116 ? 2.690   14.702  -3.508  1.00 25.77  ?  102 ALA B CA    1 
ATOM   4856 C  C     . ALA B 1 116 ? 2.776   14.503  -5.013  1.00 30.57  ?  102 ALA B C     1 
ATOM   4857 O  O     . ALA B 1 116 ? 2.140   15.235  -5.781  1.00 29.95  ?  102 ALA B O     1 
ATOM   4858 C  CB    . ALA B 1 116 ? 1.707   13.690  -2.894  1.00 27.44  ?  102 ALA B CB    1 
ATOM   4859 N  N     . PRO B 1 117 ? 3.566   13.526  -5.467  1.00 27.60  ?  103 PRO B N     1 
ATOM   4860 C  CA    . PRO B 1 117 ? 3.619   13.216  -6.903  1.00 33.11  ?  103 PRO B CA    1 
ATOM   4861 C  C     . PRO B 1 117 ? 2.256   12.786  -7.427  1.00 29.64  ?  103 PRO B C     1 
ATOM   4862 O  O     . PRO B 1 117 ? 1.394   12.312  -6.683  1.00 25.31  ?  103 PRO B O     1 
ATOM   4863 C  CB    . PRO B 1 117 ? 4.620   12.051  -7.001  1.00 29.19  ?  103 PRO B CB    1 
ATOM   4864 C  CG    . PRO B 1 117 ? 5.053   11.721  -5.635  1.00 29.26  ?  103 PRO B CG    1 
ATOM   4865 C  CD    . PRO B 1 117 ? 4.441   12.662  -4.652  1.00 35.41  ?  103 PRO B CD    1 
ATOM   4866 N  N     . GLY B 1 118 ? 2.095   12.911  -8.743  1.00 26.91  ?  104 GLY B N     1 
ATOM   4867 C  CA    . GLY B 1 118 ? 0.826   12.573  -9.363  1.00 38.73  ?  104 GLY B CA    1 
ATOM   4868 C  C     . GLY B 1 118 ? 0.428   11.129  -9.120  1.00 36.31  ?  104 GLY B C     1 
ATOM   4869 O  O     . GLY B 1 118 ? 1.270   10.239  -8.965  1.00 31.27  ?  104 GLY B O     1 
ATOM   4870 N  N     . THR B 1 119 ? -0.888  10.901  -9.104  1.00 31.08  ?  105 THR B N     1 
ATOM   4871 C  CA    . THR B 1 119 ? -1.420  9.581   -8.783  1.00 30.74  ?  105 THR B CA    1 
ATOM   4872 C  C     . THR B 1 119 ? -0.887  8.517   -9.737  1.00 38.02  ?  105 THR B C     1 
ATOM   4873 O  O     . THR B 1 119 ? -0.567  7.402   -9.310  1.00 34.89  ?  105 THR B O     1 
ATOM   4874 C  CB    . THR B 1 119 ? -2.950  9.603   -8.817  1.00 39.37  ?  105 THR B CB    1 
ATOM   4875 O  OG1   . THR B 1 119 ? -3.390  9.858   -10.154 1.00 48.11  ?  105 THR B OG1   1 
ATOM   4876 C  CG2   . THR B 1 119 ? -3.507  10.696  -7.903  1.00 29.45  ?  105 THR B CG2   1 
ATOM   4877 N  N     . ALA B 1 120 ? -0.770  8.844   -11.027 1.00 35.20  ?  106 ALA B N     1 
ATOM   4878 C  CA    . ALA B 1 120 ? -0.242  7.874   -11.986 1.00 41.17  ?  106 ALA B CA    1 
ATOM   4879 C  C     . ALA B 1 120 ? 1.172   7.441   -11.613 1.00 40.78  ?  106 ALA B C     1 
ATOM   4880 O  O     . ALA B 1 120 ? 1.495   6.246   -11.632 1.00 39.56  ?  106 ALA B O     1 
ATOM   4881 C  CB    . ALA B 1 120 ? -0.268  8.457   -13.399 1.00 38.94  ?  106 ALA B CB    1 
ATOM   4882 N  N     . SER B 1 121 ? 2.029   8.404   -11.260 1.00 43.45  ?  107 SER B N     1 
ATOM   4883 C  CA    . SER B 1 121 ? 3.387   8.074   -10.836 1.00 38.40  ?  107 SER B CA    1 
ATOM   4884 C  C     . SER B 1 121 ? 3.369   7.190   -9.599  1.00 35.27  ?  107 SER B C     1 
ATOM   4885 O  O     . SER B 1 121 ? 4.164   6.249   -9.484  1.00 32.51  ?  107 SER B O     1 
ATOM   4886 C  CB    . SER B 1 121 ? 4.178   9.352   -10.557 1.00 26.46  ?  107 SER B CB    1 
ATOM   4887 O  OG    . SER B 1 121 ? 4.664   9.913   -11.759 1.00 49.56  ?  107 SER B OG    1 
ATOM   4888 N  N     . GLN B 1 122 ? 2.475   7.491   -8.653  1.00 30.64  ?  108 GLN B N     1 
ATOM   4889 C  CA    . GLN B 1 122 ? 2.373   6.680   -7.446  1.00 34.08  ?  108 GLN B CA    1 
ATOM   4890 C  C     . GLN B 1 122 ? 1.914   5.265   -7.776  1.00 39.90  ?  108 GLN B C     1 
ATOM   4891 O  O     . GLN B 1 122 ? 2.497   4.285   -7.296  1.00 36.93  ?  108 GLN B O     1 
ATOM   4892 C  CB    . GLN B 1 122 ? 1.416   7.341   -6.454  1.00 26.34  ?  108 GLN B CB    1 
ATOM   4893 C  CG    . GLN B 1 122 ? 1.921   8.653   -5.875  1.00 29.98  ?  108 GLN B CG    1 
ATOM   4894 C  CD    . GLN B 1 122 ? 1.065   9.138   -4.728  1.00 31.73  ?  108 GLN B CD    1 
ATOM   4895 O  OE1   . GLN B 1 122 ? 0.534   8.336   -3.962  1.00 35.63  ?  108 GLN B OE1   1 
ATOM   4896 N  NE2   . GLN B 1 122 ? 0.916   10.453  -4.607  1.00 29.54  ?  108 GLN B NE2   1 
ATOM   4897 N  N     . GLN B 1 123 ? 0.898   5.138   -8.633  1.00 32.31  ?  109 GLN B N     1 
ATOM   4898 C  CA    . GLN B 1 123 ? 0.342   3.819   -8.917  1.00 43.41  ?  109 GLN B CA    1 
ATOM   4899 C  C     . GLN B 1 123 ? 1.344   2.928   -9.641  1.00 36.55  ?  109 GLN B C     1 
ATOM   4900 O  O     . GLN B 1 123 ? 1.307   1.703   -9.483  1.00 32.82  ?  109 GLN B O     1 
ATOM   4901 C  CB    . GLN B 1 123 ? -0.940  3.959   -9.734  1.00 34.21  ?  109 GLN B CB    1 
ATOM   4902 C  CG    . GLN B 1 123 ? -2.105  4.528   -8.944  1.00 43.84  ?  109 GLN B CG    1 
ATOM   4903 C  CD    . GLN B 1 123 ? -3.269  4.914   -9.831  1.00 53.36  ?  109 GLN B CD    1 
ATOM   4904 O  OE1   . GLN B 1 123 ? -3.102  5.142   -11.030 1.00 51.72  ?  109 GLN B OE1   1 
ATOM   4905 N  NE2   . GLN B 1 123 ? -4.459  4.994   -9.246  1.00 52.93  ?  109 GLN B NE2   1 
ATOM   4906 N  N     . ARG B 1 124 ? 2.256   3.518   -10.414 1.00 42.18  ?  110 ARG B N     1 
ATOM   4907 C  CA    . ARG B 1 124 ? 3.285   2.744   -11.093 1.00 31.66  ?  110 ARG B CA    1 
ATOM   4908 C  C     . ARG B 1 124 ? 4.454   2.378   -10.187 1.00 35.46  ?  110 ARG B C     1 
ATOM   4909 O  O     . ARG B 1 124 ? 5.350   1.650   -10.628 1.00 28.08  ?  110 ARG B O     1 
ATOM   4910 C  CB    . ARG B 1 124 ? 3.803   3.508   -12.313 1.00 38.18  ?  110 ARG B CB    1 
ATOM   4911 C  CG    . ARG B 1 124 ? 2.758   3.736   -13.385 1.00 37.98  ?  110 ARG B CG    1 
ATOM   4912 C  CD    . ARG B 1 124 ? 3.399   4.202   -14.676 1.00 38.07  ?  110 ARG B CD    1 
ATOM   4913 N  NE    . ARG B 1 124 ? 3.769   5.610   -14.603 1.00 64.88  ?  110 ARG B NE    1 
ATOM   4914 C  CZ    . ARG B 1 124 ? 3.055   6.604   -15.116 1.00 65.17  ?  110 ARG B CZ    1 
ATOM   4915 N  NH1   . ARG B 1 124 ? 1.840   6.403   -15.605 1.00 59.05  ?  110 ARG B NH1   1 
ATOM   4916 N  NH2   . ARG B 1 124 ? 3.547   7.840   -15.084 1.00 53.65  ?  110 ARG B NH2   1 
ATOM   4917 N  N     . GLY B 1 125 ? 4.478   2.873   -8.953  1.00 29.50  ?  111 GLY B N     1 
ATOM   4918 C  CA    . GLY B 1 125 ? 5.568   2.553   -8.043  1.00 30.46  ?  111 GLY B CA    1 
ATOM   4919 C  C     . GLY B 1 125 ? 6.922   2.997   -8.552  1.00 31.88  ?  111 GLY B C     1 
ATOM   4920 O  O     . GLY B 1 125 ? 7.906   2.262   -8.412  1.00 33.78  ?  111 GLY B O     1 
ATOM   4921 N  N     . GLU B 1 126 ? 6.995   4.187   -9.140  1.00 31.38  ?  112 GLU B N     1 
ATOM   4922 C  CA    . GLU B 1 126 ? 8.250   4.660   -9.706  1.00 38.84  ?  112 GLU B CA    1 
ATOM   4923 C  C     . GLU B 1 126 ? 9.263   4.984   -8.611  1.00 31.63  ?  112 GLU B C     1 
ATOM   4924 O  O     . GLU B 1 126 ? 8.907   5.334   -7.482  1.00 30.78  ?  112 GLU B O     1 
ATOM   4925 C  CB    . GLU B 1 126 ? 8.012   5.890   -10.578 1.00 32.72  ?  112 GLU B CB    1 
ATOM   4926 C  CG    . GLU B 1 126 ? 6.770   5.820   -11.429 1.00 39.07  ?  112 GLU B CG    1 
ATOM   4927 C  CD    . GLU B 1 126 ? 6.796   6.833   -12.554 1.00 47.50  ?  112 GLU B CD    1 
ATOM   4928 O  OE1   . GLU B 1 126 ? 6.896   8.042   -12.257 1.00 49.84  ?  112 GLU B OE1   1 
ATOM   4929 O  OE2   . GLU B 1 126 ? 6.696   6.425   -13.730 1.00 56.12  ?  112 GLU B OE2   1 
ATOM   4930 N  N     . LEU B 1 127 ? 10.544  4.873   -8.961  1.00 27.21  ?  113 LEU B N     1 
ATOM   4931 C  CA    . LEU B 1 127 ? 11.632  5.196   -8.036  1.00 38.23  ?  113 LEU B CA    1 
ATOM   4932 C  C     . LEU B 1 127 ? 11.870  6.705   -8.086  1.00 35.27  ?  113 LEU B C     1 
ATOM   4933 O  O     . LEU B 1 127 ? 12.813  7.205   -8.704  1.00 28.76  ?  113 LEU B O     1 
ATOM   4934 C  CB    . LEU B 1 127 ? 12.893  4.407   -8.385  1.00 28.72  ?  113 LEU B CB    1 
ATOM   4935 C  CG    . LEU B 1 127 ? 12.786  2.879   -8.411  1.00 39.05  ?  113 LEU B CG    1 
ATOM   4936 C  CD1   . LEU B 1 127 ? 14.136  2.238   -8.730  1.00 38.26  ?  113 LEU B CD1   1 
ATOM   4937 C  CD2   . LEU B 1 127 ? 12.246  2.355   -7.091  1.00 38.44  ?  113 LEU B CD2   1 
ATOM   4938 N  N     . LEU B 1 128 ? 10.985  7.442   -7.420  1.00 34.71  ?  114 LEU B N     1 
ATOM   4939 C  CA    . LEU B 1 128 ? 11.013  8.896   -7.427  1.00 31.48  ?  114 LEU B CA    1 
ATOM   4940 C  C     . LEU B 1 128 ? 11.819  9.439   -6.250  1.00 29.33  ?  114 LEU B C     1 
ATOM   4941 O  O     . LEU B 1 128 ? 11.928  8.808   -5.193  1.00 24.52  ?  114 LEU B O     1 
ATOM   4942 C  CB    . LEU B 1 128 ? 9.588   9.463   -7.374  1.00 26.54  ?  114 LEU B CB    1 
ATOM   4943 C  CG    . LEU B 1 128 ? 8.663   9.143   -8.548  1.00 29.65  ?  114 LEU B CG    1 
ATOM   4944 C  CD1   . LEU B 1 128 ? 7.338   9.902   -8.421  1.00 26.06  ?  114 LEU B CD1   1 
ATOM   4945 C  CD2   . LEU B 1 128 ? 9.340   9.447   -9.879  1.00 30.17  ?  114 LEU B CD2   1 
ATOM   4946 N  N     . HIS B 1 129 ? 12.345  10.650  -6.431  1.00 26.72  ?  115 HIS B N     1 
ATOM   4947 C  CA    . HIS B 1 129 ? 13.019  11.339  -5.339  1.00 29.97  ?  115 HIS B CA    1 
ATOM   4948 C  C     . HIS B 1 129 ? 12.029  11.637  -4.218  1.00 30.55  ?  115 HIS B C     1 
ATOM   4949 O  O     . HIS B 1 129 ? 10.826  11.789  -4.447  1.00 28.18  ?  115 HIS B O     1 
ATOM   4950 C  CB    . HIS B 1 129 ? 13.675  12.634  -5.834  1.00 28.05  ?  115 HIS B CB    1 
ATOM   4951 C  CG    . HIS B 1 129 ? 12.703  13.659  -6.330  1.00 34.50  ?  115 HIS B CG    1 
ATOM   4952 N  ND1   . HIS B 1 129 ? 12.215  13.661  -7.619  1.00 40.50  ?  115 HIS B ND1   1 
ATOM   4953 C  CD2   . HIS B 1 129 ? 12.124  14.714  -5.707  1.00 40.51  ?  115 HIS B CD2   1 
ATOM   4954 C  CE1   . HIS B 1 129 ? 11.381  14.677  -7.771  1.00 36.39  ?  115 HIS B CE1   1 
ATOM   4955 N  NE2   . HIS B 1 129 ? 11.306  15.329  -6.625  1.00 29.39  ?  115 HIS B NE2   1 
ATOM   4956 N  N     . HIS B 1 130 ? 12.554  11.708  -2.991  1.00 23.37  ?  116 HIS B N     1 
ATOM   4957 C  CA    . HIS B 1 130 ? 11.778  11.857  -1.763  1.00 25.76  ?  116 HIS B CA    1 
ATOM   4958 C  C     . HIS B 1 130 ? 10.986  10.597  -1.410  1.00 27.81  ?  116 HIS B C     1 
ATOM   4959 O  O     . HIS B 1 130 ? 10.002  10.672  -0.669  1.00 30.88  ?  116 HIS B O     1 
ATOM   4960 C  CB    . HIS B 1 130 ? 10.829  13.067  -1.819  1.00 26.82  ?  116 HIS B CB    1 
ATOM   4961 C  CG    . HIS B 1 130 ? 11.495  14.347  -2.226  1.00 35.88  ?  116 HIS B CG    1 
ATOM   4962 N  ND1   . HIS B 1 130 ? 12.858  14.544  -2.136  1.00 33.17  ?  116 HIS B ND1   1 
ATOM   4963 C  CD2   . HIS B 1 130 ? 10.982  15.500  -2.715  1.00 35.42  ?  116 HIS B CD2   1 
ATOM   4964 C  CE1   . HIS B 1 130 ? 13.154  15.760  -2.557  1.00 32.34  ?  116 HIS B CE1   1 
ATOM   4965 N  NE2   . HIS B 1 130 ? 12.034  16.362  -2.913  1.00 35.20  ?  116 HIS B NE2   1 
ATOM   4966 N  N     . THR B 1 131 ? 11.385  9.432   -1.918  1.00 26.59  ?  117 THR B N     1 
ATOM   4967 C  CA    . THR B 1 131 ? 10.819  8.156   -1.499  1.00 29.85  ?  117 THR B CA    1 
ATOM   4968 C  C     . THR B 1 131 ? 11.910  7.281   -0.899  1.00 29.84  ?  117 THR B C     1 
ATOM   4969 O  O     . THR B 1 131 ? 13.101  7.588   -0.974  1.00 23.54  ?  117 THR B O     1 
ATOM   4970 C  CB    . THR B 1 131 ? 10.157  7.402   -2.662  1.00 30.96  ?  117 THR B CB    1 
ATOM   4971 O  OG1   . THR B 1 131 ? 11.170  6.862   -3.525  1.00 28.14  ?  117 THR B OG1   1 
ATOM   4972 C  CG2   . THR B 1 131 ? 9.207   8.306   -3.446  1.00 23.52  ?  117 THR B CG2   1 
ATOM   4973 N  N     . LEU B 1 132 ? 11.491  6.163   -0.314  1.00 26.81  ?  118 LEU B N     1 
ATOM   4974 C  CA    . LEU B 1 132 ? 12.446  5.212   0.237   1.00 31.45  ?  118 LEU B CA    1 
ATOM   4975 C  C     . LEU B 1 132 ? 13.025  4.282   -0.826  1.00 32.69  ?  118 LEU B C     1 
ATOM   4976 O  O     . LEU B 1 132 ? 13.745  3.338   -0.482  1.00 27.34  ?  118 LEU B O     1 
ATOM   4977 C  CB    . LEU B 1 132 ? 11.789  4.395   1.352   1.00 31.19  ?  118 LEU B CB    1 
ATOM   4978 C  CG    . LEU B 1 132 ? 11.136  5.203   2.479   1.00 27.19  ?  118 LEU B CG    1 
ATOM   4979 C  CD1   . LEU B 1 132 ? 10.577  4.266   3.532   1.00 27.35  ?  118 LEU B CD1   1 
ATOM   4980 C  CD2   . LEU B 1 132 ? 12.114  6.171   3.110   1.00 24.85  ?  118 LEU B CD2   1 
ATOM   4981 N  N     . GLY B 1 133 ? 12.727  4.524   -2.101  1.00 31.06  ?  119 GLY B N     1 
ATOM   4982 C  CA    . GLY B 1 133 ? 13.250  3.702   -3.171  1.00 25.01  ?  119 GLY B CA    1 
ATOM   4983 C  C     . GLY B 1 133 ? 12.571  2.363   -3.335  1.00 31.09  ?  119 GLY B C     1 
ATOM   4984 O  O     . GLY B 1 133 ? 13.090  1.513   -4.065  1.00 32.96  ?  119 GLY B O     1 
ATOM   4985 N  N     . ASP B 1 134 ? 11.422  2.151   -2.695  1.00 25.62  ?  120 ASP B N     1 
ATOM   4986 C  CA    . ASP B 1 134 ? 10.702  0.888   -2.747  1.00 33.02  ?  120 ASP B CA    1 
ATOM   4987 C  C     . ASP B 1 134 ? 9.395   0.982   -3.528  1.00 35.40  ?  120 ASP B C     1 
ATOM   4988 O  O     . ASP B 1 134 ? 8.662   -0.010  -3.608  1.00 32.05  ?  120 ASP B O     1 
ATOM   4989 C  CB    . ASP B 1 134 ? 10.418  0.391   -1.323  1.00 27.57  ?  120 ASP B CB    1 
ATOM   4990 C  CG    . ASP B 1 134 ? 9.621   1.401   -0.498  1.00 35.39  ?  120 ASP B CG    1 
ATOM   4991 O  OD1   . ASP B 1 134 ? 9.270   2.484   -1.028  1.00 30.36  ?  120 ASP B OD1   1 
ATOM   4992 O  OD2   . ASP B 1 134 ? 9.353   1.115   0.689   1.00 37.36  ?  120 ASP B OD2   1 
ATOM   4993 N  N     . GLY B 1 135 ? 9.072   2.145   -4.086  1.00 29.82  ?  121 GLY B N     1 
ATOM   4994 C  CA    . GLY B 1 135 ? 7.837   2.309   -4.824  1.00 28.23  ?  121 GLY B CA    1 
ATOM   4995 C  C     . GLY B 1 135 ? 6.599   2.488   -3.976  1.00 35.09  ?  121 GLY B C     1 
ATOM   4996 O  O     . GLY B 1 135 ? 5.487   2.474   -4.521  1.00 32.17  ?  121 GLY B O     1 
ATOM   4997 N  N     . GLU B 1 136 ? 6.752   2.633   -2.663  1.00 28.98  ?  122 GLU B N     1 
ATOM   4998 C  CA    . GLU B 1 136 ? 5.636   2.811   -1.744  1.00 31.08  ?  122 GLU B CA    1 
ATOM   4999 C  C     . GLU B 1 136 ? 5.423   4.296   -1.476  1.00 31.66  ?  122 GLU B C     1 
ATOM   5000 O  O     . GLU B 1 136 ? 6.372   5.013   -1.143  1.00 28.40  ?  122 GLU B O     1 
ATOM   5001 C  CB    . GLU B 1 136 ? 5.902   2.065   -0.435  1.00 29.05  ?  122 GLU B CB    1 
ATOM   5002 C  CG    . GLU B 1 136 ? 4.777   2.167   0.582   1.00 53.19  ?  122 GLU B CG    1 
ATOM   5003 C  CD    . GLU B 1 136 ? 3.443   1.693   0.036   1.00 51.85  ?  122 GLU B CD    1 
ATOM   5004 O  OE1   . GLU B 1 136 ? 3.355   0.520   -0.403  1.00 45.72  ?  122 GLU B OE1   1 
ATOM   5005 O  OE2   . GLU B 1 136 ? 2.494   2.507   0.037   1.00 38.43  ?  122 GLU B OE2   1 
ATOM   5006 N  N     . PHE B 1 137 ? 4.178   4.758   -1.604  1.00 32.39  ?  123 PHE B N     1 
ATOM   5007 C  CA    . PHE B 1 137 ? 3.901   6.183   -1.454  1.00 35.58  ?  123 PHE B CA    1 
ATOM   5008 C  C     . PHE B 1 137 ? 2.994   6.501   -0.274  1.00 28.30  ?  123 PHE B C     1 
ATOM   5009 O  O     . PHE B 1 137 ? 2.546   7.647   -0.147  1.00 31.66  ?  123 PHE B O     1 
ATOM   5010 C  CB    . PHE B 1 137 ? 3.306   6.744   -2.749  1.00 25.44  ?  123 PHE B CB    1 
ATOM   5011 C  CG    . PHE B 1 137 ? 4.294   6.806   -3.879  1.00 30.84  ?  123 PHE B CG    1 
ATOM   5012 C  CD1   . PHE B 1 137 ? 4.516   5.698   -4.688  1.00 30.40  ?  123 PHE B CD1   1 
ATOM   5013 C  CD2   . PHE B 1 137 ? 5.027   7.958   -4.112  1.00 27.38  ?  123 PHE B CD2   1 
ATOM   5014 C  CE1   . PHE B 1 137 ? 5.440   5.746   -5.722  1.00 24.91  ?  123 PHE B CE1   1 
ATOM   5015 C  CE2   . PHE B 1 137 ? 5.952   8.015   -5.143  1.00 34.06  ?  123 PHE B CE2   1 
ATOM   5016 C  CZ    . PHE B 1 137 ? 6.159   6.906   -5.949  1.00 34.82  ?  123 PHE B CZ    1 
ATOM   5017 N  N     . ARG B 1 138 ? 2.756   5.546   0.627   1.00 30.32  ?  124 ARG B N     1 
ATOM   5018 C  CA    . ARG B 1 138 ? 1.871   5.781   1.762   1.00 32.10  ?  124 ARG B CA    1 
ATOM   5019 C  C     . ARG B 1 138 ? 2.555   5.576   3.108   1.00 32.73  ?  124 ARG B C     1 
ATOM   5020 O  O     . ARG B 1 138 ? 1.884   5.654   4.145   1.00 29.06  ?  124 ARG B O     1 
ATOM   5021 C  CB    . ARG B 1 138 ? 0.630   4.891   1.656   1.00 37.43  ?  124 ARG B CB    1 
ATOM   5022 C  CG    . ARG B 1 138 ? 0.045   4.860   0.255   1.00 43.23  ?  124 ARG B CG    1 
ATOM   5023 C  CD    . ARG B 1 138 ? -1.462  4.740   0.252   1.00 49.87  ?  124 ARG B CD    1 
ATOM   5024 N  NE    . ARG B 1 138 ? -1.995  4.942   -1.090  1.00 58.39  ?  124 ARG B NE    1 
ATOM   5025 C  CZ    . ARG B 1 138 ? -3.239  4.669   -1.455  1.00 62.59  ?  124 ARG B CZ    1 
ATOM   5026 N  NH1   . ARG B 1 138 ? -4.118  4.172   -0.600  1.00 61.71  ?  124 ARG B NH1   1 
ATOM   5027 N  NH2   . ARG B 1 138 ? -3.614  4.909   -2.708  1.00 60.73  ?  124 ARG B NH2   1 
ATOM   5028 N  N     . HIS B 1 139 ? 3.872   5.340   3.124   1.00 28.56  ?  125 HIS B N     1 
ATOM   5029 C  CA    . HIS B 1 139 ? 4.594   5.210   4.388   1.00 29.86  ?  125 HIS B CA    1 
ATOM   5030 C  C     . HIS B 1 139 ? 4.377   6.439   5.268   1.00 31.00  ?  125 HIS B C     1 
ATOM   5031 O  O     . HIS B 1 139 ? 4.033   6.328   6.452   1.00 24.53  ?  125 HIS B O     1 
ATOM   5032 C  CB    . HIS B 1 139 ? 6.097   5.033   4.131   1.00 27.39  ?  125 HIS B CB    1 
ATOM   5033 C  CG    . HIS B 1 139 ? 6.500   3.679   3.635   1.00 30.88  ?  125 HIS B CG    1 
ATOM   5034 N  ND1   . HIS B 1 139 ? 6.012   2.503   4.166   1.00 28.26  ?  125 HIS B ND1   1 
ATOM   5035 C  CD2   . HIS B 1 139 ? 7.387   3.318   2.676   1.00 31.53  ?  125 HIS B CD2   1 
ATOM   5036 C  CE1   . HIS B 1 139 ? 6.565   1.478   3.539   1.00 37.00  ?  125 HIS B CE1   1 
ATOM   5037 N  NE2   . HIS B 1 139 ? 7.403   1.945   2.631   1.00 29.92  ?  125 HIS B NE2   1 
ATOM   5038 N  N     . PHE B 1 140 ? 4.592   7.627   4.704   1.00 23.24  ?  126 PHE B N     1 
ATOM   5039 C  CA    . PHE B 1 140 ? 4.596   8.839   5.511   1.00 25.31  ?  126 PHE B CA    1 
ATOM   5040 C  C     . PHE B 1 140 ? 3.185   9.262   5.900   1.00 28.23  ?  126 PHE B C     1 
ATOM   5041 O  O     . PHE B 1 140 ? 2.993   9.880   6.955   1.00 25.46  ?  126 PHE B O     1 
ATOM   5042 C  CB    . PHE B 1 140 ? 5.335   9.947   4.755   1.00 24.48  ?  126 PHE B CB    1 
ATOM   5043 C  CG    . PHE B 1 140 ? 6.543   9.450   3.992   1.00 25.50  ?  126 PHE B CG    1 
ATOM   5044 C  CD1   . PHE B 1 140 ? 7.467   8.602   4.599   1.00 23.76  ?  126 PHE B CD1   1 
ATOM   5045 C  CD2   . PHE B 1 140 ? 6.740   9.805   2.665   1.00 22.01  ?  126 PHE B CD2   1 
ATOM   5046 C  CE1   . PHE B 1 140 ? 8.573   8.124   3.900   1.00 24.68  ?  126 PHE B CE1   1 
ATOM   5047 C  CE2   . PHE B 1 140 ? 7.841   9.329   1.960   1.00 24.53  ?  126 PHE B CE2   1 
ATOM   5048 C  CZ    . PHE B 1 140 ? 8.759   8.486   2.582   1.00 22.54  ?  126 PHE B CZ    1 
ATOM   5049 N  N     . TYR B 1 141 ? 2.191   8.941   5.069   1.00 29.23  ?  127 TYR B N     1 
ATOM   5050 C  CA    . TYR B 1 141 ? 0.802   9.146   5.467   1.00 28.34  ?  127 TYR B CA    1 
ATOM   5051 C  C     . TYR B 1 141 ? 0.488   8.375   6.745   1.00 28.30  ?  127 TYR B C     1 
ATOM   5052 O  O     . TYR B 1 141 ? -0.005  8.947   7.724   1.00 25.99  ?  127 TYR B O     1 
ATOM   5053 C  CB    . TYR B 1 141 ? -0.125  8.720   4.325   1.00 29.19  ?  127 TYR B CB    1 
ATOM   5054 C  CG    . TYR B 1 141 ? -1.602  8.672   4.663   1.00 28.26  ?  127 TYR B CG    1 
ATOM   5055 C  CD1   . TYR B 1 141 ? -2.379  9.825   4.634   1.00 30.50  ?  127 TYR B CD1   1 
ATOM   5056 C  CD2   . TYR B 1 141 ? -2.226  7.470   4.983   1.00 32.40  ?  127 TYR B CD2   1 
ATOM   5057 C  CE1   . TYR B 1 141 ? -3.730  9.792   4.924   1.00 33.69  ?  127 TYR B CE1   1 
ATOM   5058 C  CE2   . TYR B 1 141 ? -3.587  7.425   5.278   1.00 36.32  ?  127 TYR B CE2   1 
ATOM   5059 C  CZ    . TYR B 1 141 ? -4.332  8.592   5.245   1.00 37.89  ?  127 TYR B CZ    1 
ATOM   5060 O  OH    . TYR B 1 141 ? -5.683  8.570   5.534   1.00 46.38  ?  127 TYR B OH    1 
ATOM   5061 N  N     . HIS B 1 142 ? 0.831   7.083   6.776   1.00 25.66  ?  128 HIS B N     1 
ATOM   5062 C  CA    . HIS B 1 142 ? 0.530   6.269   7.951   1.00 29.27  ?  128 HIS B CA    1 
ATOM   5063 C  C     . HIS B 1 142 ? 1.333   6.724   9.164   1.00 29.07  ?  128 HIS B C     1 
ATOM   5064 O  O     . HIS B 1 142 ? 0.824   6.704   10.290  1.00 30.24  ?  128 HIS B O     1 
ATOM   5065 C  CB    . HIS B 1 142 ? 0.786   4.789   7.655   1.00 27.93  ?  128 HIS B CB    1 
ATOM   5066 C  CG    . HIS B 1 142 ? -0.131  4.219   6.618   1.00 39.46  ?  128 HIS B CG    1 
ATOM   5067 N  ND1   . HIS B 1 142 ? -1.501  4.372   6.672   1.00 43.39  ?  128 HIS B ND1   1 
ATOM   5068 C  CD2   . HIS B 1 142 ? 0.122   3.491   5.504   1.00 43.88  ?  128 HIS B CD2   1 
ATOM   5069 C  CE1   . HIS B 1 142 ? -2.051  3.768   5.633   1.00 38.56  ?  128 HIS B CE1   1 
ATOM   5070 N  NE2   . HIS B 1 142 ? -1.089  3.226   4.909   1.00 44.52  ?  128 HIS B NE2   1 
ATOM   5071 N  N     . MET B 1 143 ? 2.585   7.145   8.956   1.00 22.73  ?  129 MET B N     1 
ATOM   5072 C  CA    . MET B 1 143 ? 3.395   7.628   10.072  1.00 28.41  ?  129 MET B CA    1 
ATOM   5073 C  C     . MET B 1 143 ? 2.779   8.860   10.737  1.00 27.24  ?  129 MET B C     1 
ATOM   5074 O  O     . MET B 1 143 ? 3.011   9.100   11.927  1.00 25.67  ?  129 MET B O     1 
ATOM   5075 C  CB    . MET B 1 143 ? 4.822   7.923   9.600   1.00 30.25  ?  129 MET B CB    1 
ATOM   5076 C  CG    . MET B 1 143 ? 5.622   6.661   9.230   1.00 25.97  ?  129 MET B CG    1 
ATOM   5077 S  SD    . MET B 1 143 ? 6.999   6.944   8.092   1.00 31.13  ?  129 MET B SD    1 
ATOM   5078 C  CE    . MET B 1 143 ? 8.133   7.878   9.119   1.00 23.06  ?  129 MET B CE    1 
ATOM   5079 N  N     . SER B 1 144 ? 1.972   9.635   10.002  1.00 25.29  ?  130 SER B N     1 
ATOM   5080 C  CA    . SER B 1 144 ? 1.321   10.813  10.564  1.00 30.28  ?  130 SER B CA    1 
ATOM   5081 C  C     . SER B 1 144 ? 0.047   10.493  11.342  1.00 33.17  ?  130 SER B C     1 
ATOM   5082 O  O     . SER B 1 144 ? -0.433  11.360  12.084  1.00 26.28  ?  130 SER B O     1 
ATOM   5083 C  CB    . SER B 1 144 ? 0.984   11.812  9.450   1.00 33.44  ?  130 SER B CB    1 
ATOM   5084 O  OG    . SER B 1 144 ? 2.066   12.691  9.194   1.00 36.84  ?  130 SER B OG    1 
ATOM   5085 N  N     . GLU B 1 145 ? -0.492  9.277   11.219  1.00 27.90  ?  131 GLU B N     1 
ATOM   5086 C  CA    . GLU B 1 145 ? -1.754  8.925   11.874  1.00 33.79  ?  131 GLU B CA    1 
ATOM   5087 C  C     . GLU B 1 145 ? -1.766  9.176   13.378  1.00 30.11  ?  131 GLU B C     1 
ATOM   5088 O  O     . GLU B 1 145 ? -2.767  9.715   13.876  1.00 31.40  ?  131 GLU B O     1 
ATOM   5089 C  CB    . GLU B 1 145 ? -2.099  7.456   11.576  1.00 36.42  ?  131 GLU B CB    1 
ATOM   5090 C  CG    . GLU B 1 145 ? -3.568  7.064   11.801  1.00 45.99  ?  131 GLU B CG    1 
ATOM   5091 C  CD    . GLU B 1 145 ? -3.949  6.926   13.277  1.00 67.04  ?  131 GLU B CD    1 
ATOM   5092 O  OE1   . GLU B 1 145 ? -3.121  6.405   14.061  1.00 48.43  ?  131 GLU B OE1   1 
ATOM   5093 O  OE2   . GLU B 1 145 ? -5.080  7.335   13.648  1.00 55.85  ?  131 GLU B OE2   1 
ATOM   5094 N  N     . PRO B 1 146 ? -0.746  8.792   14.159  1.00 31.73  ?  132 PRO B N     1 
ATOM   5095 C  CA    . PRO B 1 146 ? -0.834  8.992   15.616  1.00 33.55  ?  132 PRO B CA    1 
ATOM   5096 C  C     . PRO B 1 146 ? -0.814  10.451  16.059  1.00 33.46  ?  132 PRO B C     1 
ATOM   5097 O  O     . PRO B 1 146 ? -1.121  10.713  17.229  1.00 30.68  ?  132 PRO B O     1 
ATOM   5098 C  CB    . PRO B 1 146 ? 0.394   8.239   16.155  1.00 34.30  ?  132 PRO B CB    1 
ATOM   5099 C  CG    . PRO B 1 146 ? 0.793   7.311   15.071  1.00 24.95  ?  132 PRO B CG    1 
ATOM   5100 C  CD    . PRO B 1 146 ? 0.458   8.017   13.801  1.00 32.39  ?  132 PRO B CD    1 
ATOM   5101 N  N     . ILE B 1 147 ? -0.453  11.401  15.194  1.00 26.03  ?  133 ILE B N     1 
ATOM   5102 C  CA    . ILE B 1 147 ? -0.351  12.793  15.613  1.00 32.78  ?  133 ILE B CA    1 
ATOM   5103 C  C     . ILE B 1 147 ? -1.343  13.693  14.871  1.00 29.71  ?  133 ILE B C     1 
ATOM   5104 O  O     . ILE B 1 147 ? -1.140  14.901  14.788  1.00 31.62  ?  133 ILE B O     1 
ATOM   5105 C  CB    . ILE B 1 147 ? 1.090   13.318  15.468  1.00 25.01  ?  133 ILE B CB    1 
ATOM   5106 C  CG1   . ILE B 1 147 ? 1.591   13.167  14.028  1.00 26.88  ?  133 ILE B CG1   1 
ATOM   5107 C  CG2   . ILE B 1 147 ? 2.010   12.606  16.452  1.00 28.04  ?  133 ILE B CG2   1 
ATOM   5108 C  CD1   . ILE B 1 147 ? 3.012   13.733  13.807  1.00 28.76  ?  133 ILE B CD1   1 
ATOM   5109 N  N     . THR B 1 148 ? -2.422  13.124  14.336  1.00 29.41  ?  134 THR B N     1 
ATOM   5110 C  CA    . THR B 1 148 ? -3.495  13.903  13.725  1.00 30.47  ?  134 THR B CA    1 
ATOM   5111 C  C     . THR B 1 148 ? -4.837  13.299  14.123  1.00 28.90  ?  134 THR B C     1 
ATOM   5112 O  O     . THR B 1 148 ? -4.942  12.093  14.356  1.00 25.06  ?  134 THR B O     1 
ATOM   5113 C  CB    . THR B 1 148 ? -3.375  13.944  12.187  1.00 29.64  ?  134 THR B CB    1 
ATOM   5114 O  OG1   . THR B 1 148 ? -3.466  12.615  11.657  1.00 36.16  ?  134 THR B OG1   1 
ATOM   5115 C  CG2   . THR B 1 148 ? -2.049  14.573  11.745  1.00 23.55  ?  134 THR B CG2   1 
ATOM   5116 N  N     . VAL B 1 149 ? -5.868  14.146  14.209  1.00 34.43  ?  135 VAL B N     1 
ATOM   5117 C  CA    . VAL B 1 149 ? -7.208  13.632  14.482  1.00 32.45  ?  135 VAL B CA    1 
ATOM   5118 C  C     . VAL B 1 149 ? -7.905  13.173  13.215  1.00 28.64  ?  135 VAL B C     1 
ATOM   5119 O  O     . VAL B 1 149 ? -8.922  12.478  13.296  1.00 26.60  ?  135 VAL B O     1 
ATOM   5120 C  CB    . VAL B 1 149 ? -8.124  14.661  15.172  1.00 33.57  ?  135 VAL B CB    1 
ATOM   5121 C  CG1   . VAL B 1 149 ? -7.725  14.846  16.620  1.00 42.65  ?  135 VAL B CG1   1 
ATOM   5122 C  CG2   . VAL B 1 149 ? -8.120  15.983  14.420  1.00 26.45  ?  135 VAL B CG2   1 
ATOM   5123 N  N     . ALA B 1 150 ? -7.402  13.557  12.048  1.00 27.19  ?  136 ALA B N     1 
ATOM   5124 C  CA    . ALA B 1 150 ? -8.040  13.182  10.797  1.00 25.66  ?  136 ALA B CA    1 
ATOM   5125 C  C     . ALA B 1 150 ? -7.042  13.377  9.673   1.00 29.50  ?  136 ALA B C     1 
ATOM   5126 O  O     . ALA B 1 150 ? -6.218  14.295  9.709   1.00 27.62  ?  136 ALA B O     1 
ATOM   5127 C  CB    . ALA B 1 150 ? -9.305  14.007  10.533  1.00 26.57  ?  136 ALA B CB    1 
ATOM   5128 N  N     . GLN B 1 151 ? -7.128  12.509  8.673   1.00 25.01  ?  137 GLN B N     1 
ATOM   5129 C  CA    . GLN B 1 151 ? -6.262  12.640  7.515   1.00 28.98  ?  137 GLN B CA    1 
ATOM   5130 C  C     . GLN B 1 151 ? -6.968  12.046  6.312   1.00 25.43  ?  137 GLN B C     1 
ATOM   5131 O  O     . GLN B 1 151 ? -7.932  11.285  6.441   1.00 25.39  ?  137 GLN B O     1 
ATOM   5132 C  CB    . GLN B 1 151 ? -4.889  11.972  7.731   1.00 28.63  ?  137 GLN B CB    1 
ATOM   5133 C  CG    . GLN B 1 151 ? -4.895  10.830  8.721   1.00 37.69  ?  137 GLN B CG    1 
ATOM   5134 C  CD    . GLN B 1 151 ? -3.568  10.084  8.771   1.00 54.74  ?  137 GLN B CD    1 
ATOM   5135 O  OE1   . GLN B 1 151 ? -2.496  10.659  8.549   1.00 42.48  ?  137 GLN B OE1   1 
ATOM   5136 N  NE2   . GLN B 1 151 ? -3.640  8.786   9.046   1.00 46.58  ?  137 GLN B NE2   1 
ATOM   5137 N  N     . ALA B 1 152 ? -6.484  12.415  5.132   1.00 24.66  ?  138 ALA B N     1 
ATOM   5138 C  CA    . ALA B 1 152 ? -7.062  11.889  3.908   1.00 32.66  ?  138 ALA B CA    1 
ATOM   5139 C  C     . ALA B 1 152 ? -6.011  11.912  2.812   1.00 28.59  ?  138 ALA B C     1 
ATOM   5140 O  O     . ALA B 1 152 ? -5.111  12.757  2.804   1.00 24.87  ?  138 ALA B O     1 
ATOM   5141 C  CB    . ALA B 1 152 ? -8.305  12.690  3.477   1.00 25.64  ?  138 ALA B CB    1 
ATOM   5142 N  N     . ILE B 1 153 ? -6.124  10.960  1.899   1.00 28.78  ?  139 ILE B N     1 
ATOM   5143 C  CA    . ILE B 1 153 ? -5.430  11.021  0.624   1.00 29.38  ?  139 ILE B CA    1 
ATOM   5144 C  C     . ILE B 1 153 ? -6.455  11.516  -0.382  1.00 32.97  ?  139 ILE B C     1 
ATOM   5145 O  O     . ILE B 1 153 ? -7.444  10.831  -0.668  1.00 34.13  ?  139 ILE B O     1 
ATOM   5146 C  CB    . ILE B 1 153 ? -4.842  9.666   0.214   1.00 25.75  ?  139 ILE B CB    1 
ATOM   5147 C  CG1   . ILE B 1 153 ? -3.805  9.198   1.240   1.00 46.24  ?  139 ILE B CG1   1 
ATOM   5148 C  CG2   . ILE B 1 153 ? -4.197  9.773   -1.163  1.00 30.16  ?  139 ILE B CG2   1 
ATOM   5149 C  CD1   . ILE B 1 153 ? -3.352  7.748   1.044   1.00 35.77  ?  139 ILE B CD1   1 
ATOM   5150 N  N     . LEU B 1 154 ? -6.240  12.722  -0.892  1.00 30.25  ?  140 LEU B N     1 
ATOM   5151 C  CA    . LEU B 1 154 ? -7.208  13.343  -1.777  1.00 26.22  ?  140 LEU B CA    1 
ATOM   5152 C  C     . LEU B 1 154 ? -7.123  12.715  -3.160  1.00 36.43  ?  140 LEU B C     1 
ATOM   5153 O  O     . LEU B 1 154 ? -6.032  12.581  -3.726  1.00 29.19  ?  140 LEU B O     1 
ATOM   5154 C  CB    . LEU B 1 154 ? -6.968  14.849  -1.851  1.00 31.50  ?  140 LEU B CB    1 
ATOM   5155 C  CG    . LEU B 1 154 ? -7.221  15.590  -0.537  1.00 32.70  ?  140 LEU B CG    1 
ATOM   5156 C  CD1   . LEU B 1 154 ? -6.973  17.087  -0.699  1.00 25.75  ?  140 LEU B CD1   1 
ATOM   5157 C  CD2   . LEU B 1 154 ? -8.642  15.319  -0.050  1.00 26.71  ?  140 LEU B CD2   1 
ATOM   5158 N  N     . THR B 1 155 ? -8.277  12.327  -3.695  1.00 28.74  ?  141 THR B N     1 
ATOM   5159 C  CA    . THR B 1 155 ? -8.392  11.771  -5.033  1.00 31.82  ?  141 THR B CA    1 
ATOM   5160 C  C     . THR B 1 155 ? -9.395  12.594  -5.825  1.00 29.40  ?  141 THR B C     1 
ATOM   5161 O  O     . THR B 1 155 ? -10.132 13.416  -5.277  1.00 30.78  ?  141 THR B O     1 
ATOM   5162 C  CB    . THR B 1 155 ? -8.841  10.298  -5.008  1.00 32.87  ?  141 THR B CB    1 
ATOM   5163 O  OG1   . THR B 1 155 ? -10.244 10.235  -4.724  1.00 35.54  ?  141 THR B OG1   1 
ATOM   5164 C  CG2   . THR B 1 155 ? -8.080  9.505   -3.954  1.00 29.43  ?  141 THR B CG2   1 
ATOM   5165 N  N     . GLU B 1 156 ? -9.436  12.335  -7.132  1.00 32.72  ?  142 GLU B N     1 
ATOM   5166 C  CA    . GLU B 1 156 ? -10.423 12.987  -7.981  1.00 30.11  ?  142 GLU B CA    1 
ATOM   5167 C  C     . GLU B 1 156 ? -11.843 12.653  -7.535  1.00 38.94  ?  142 GLU B C     1 
ATOM   5168 O  O     . GLU B 1 156 ? -12.763 13.456  -7.737  1.00 33.22  ?  142 GLU B O     1 
ATOM   5169 C  CB    . GLU B 1 156 ? -10.194 12.568  -9.435  1.00 40.44  ?  142 GLU B CB    1 
ATOM   5170 C  CG    . GLU B 1 156 ? -11.251 13.038  -10.422 1.00 45.13  ?  142 GLU B CG    1 
ATOM   5171 C  CD    . GLU B 1 156 ? -10.964 12.584  -11.842 1.00 48.50  ?  142 GLU B CD    1 
ATOM   5172 O  OE1   . GLU B 1 156 ? -10.526 11.426  -12.016 1.00 46.53  ?  142 GLU B OE1   1 
ATOM   5173 O  OE2   . GLU B 1 156 ? -11.169 13.385  -12.782 1.00 48.77  ?  142 GLU B OE2   1 
ATOM   5174 N  N     . GLN B 1 157 ? -12.031 11.495  -6.897  1.00 30.66  ?  143 GLN B N     1 
ATOM   5175 C  CA    . GLN B 1 157 ? -13.351 11.003  -6.524  1.00 33.66  ?  143 GLN B CA    1 
ATOM   5176 C  C     . GLN B 1 157 ? -13.787 11.399  -5.118  1.00 31.74  ?  143 GLN B C     1 
ATOM   5177 O  O     . GLN B 1 157 ? -14.963 11.216  -4.783  1.00 37.17  ?  143 GLN B O     1 
ATOM   5178 C  CB    . GLN B 1 157 ? -13.390 9.473   -6.636  1.00 31.59  ?  143 GLN B CB    1 
ATOM   5179 C  CG    . GLN B 1 157 ? -13.453 8.977   -8.058  1.00 33.54  ?  143 GLN B CG    1 
ATOM   5180 C  CD    . GLN B 1 157 ? -13.488 7.460   -8.164  1.00 57.66  ?  143 GLN B CD    1 
ATOM   5181 O  OE1   . GLN B 1 157 ? -14.036 6.772   -7.297  1.00 51.49  ?  143 GLN B OE1   1 
ATOM   5182 N  NE2   . GLN B 1 157 ? -12.920 6.933   -9.246  1.00 47.79  ?  143 GLN B NE2   1 
ATOM   5183 N  N     . ASN B 1 158 ? -12.897 11.950  -4.291  1.00 30.62  ?  144 ASN B N     1 
ATOM   5184 C  CA    . ASN B 1 158 ? -13.249 12.236  -2.908  1.00 29.97  ?  144 ASN B CA    1 
ATOM   5185 C  C     . ASN B 1 158 ? -12.890 13.641  -2.443  1.00 36.13  ?  144 ASN B C     1 
ATOM   5186 O  O     . ASN B 1 158 ? -13.210 13.991  -1.301  1.00 33.32  ?  144 ASN B O     1 
ATOM   5187 C  CB    . ASN B 1 158 ? -12.572 11.219  -1.969  1.00 29.25  ?  144 ASN B CB    1 
ATOM   5188 C  CG    . ASN B 1 158 ? -11.049 11.403  -1.880  1.00 32.79  ?  144 ASN B CG    1 
ATOM   5189 O  OD1   . ASN B 1 158 ? -10.484 12.371  -2.393  1.00 28.01  ?  144 ASN B OD1   1 
ATOM   5190 N  ND2   . ASN B 1 158 ? -10.383 10.456  -1.227  1.00 30.41  ?  144 ASN B ND2   1 
ATOM   5191 N  N     . ALA B 1 159 ? -12.263 14.456  -3.297  1.00 30.45  ?  145 ALA B N     1 
ATOM   5192 C  CA    . ALA B 1 159 ? -11.441 15.562  -2.811  1.00 31.68  ?  145 ALA B CA    1 
ATOM   5193 C  C     . ALA B 1 159 ? -12.227 16.515  -1.916  1.00 36.72  ?  145 ALA B C     1 
ATOM   5194 O  O     . ALA B 1 159 ? -11.824 16.789  -0.779  1.00 35.67  ?  145 ALA B O     1 
ATOM   5195 C  CB    . ALA B 1 159 ? -10.837 16.318  -3.993  1.00 31.51  ?  145 ALA B CB    1 
ATOM   5196 N  N     . CYS B 1 160 ? -13.367 17.012  -2.395  1.00 31.79  ?  146 CYS B N     1 
ATOM   5197 C  CA    . CYS B 1 160 ? -13.989 18.135  -1.703  1.00 46.34  ?  146 CYS B CA    1 
ATOM   5198 C  C     . CYS B 1 160 ? -14.616 17.712  -0.377  1.00 35.68  ?  146 CYS B C     1 
ATOM   5199 O  O     . CYS B 1 160 ? -14.521 18.448  0.612   1.00 35.88  ?  146 CYS B O     1 
ATOM   5200 C  CB    . CYS B 1 160 ? -15.002 18.824  -2.618  1.00 40.57  ?  146 CYS B CB    1 
ATOM   5201 S  SG    . CYS B 1 160 ? -14.170 19.757  -3.941  1.00 43.21  ?  146 CYS B SG    1 
ATOM   5202 N  N     . TYR B 1 161 ? -15.241 16.531  -0.312  1.00 32.50  ?  147 TYR B N     1 
ATOM   5203 C  CA    . TYR B 1 161 ? -15.815 16.162  0.978   1.00 30.04  ?  147 TYR B CA    1 
ATOM   5204 C  C     . TYR B 1 161 ? -14.764 15.642  1.952   1.00 30.11  ?  147 TYR B C     1 
ATOM   5205 O  O     . TYR B 1 161 ? -14.936 15.794  3.167   1.00 32.87  ?  147 TYR B O     1 
ATOM   5206 C  CB    . TYR B 1 161 ? -16.971 15.164  0.818   1.00 34.75  ?  147 TYR B CB    1 
ATOM   5207 C  CG    . TYR B 1 161 ? -16.635 13.772  0.335   1.00 40.03  ?  147 TYR B CG    1 
ATOM   5208 C  CD1   . TYR B 1 161 ? -16.331 12.756  1.235   1.00 38.06  ?  147 TYR B CD1   1 
ATOM   5209 C  CD2   . TYR B 1 161 ? -16.704 13.455  -1.016  1.00 38.84  ?  147 TYR B CD2   1 
ATOM   5210 C  CE1   . TYR B 1 161 ? -16.047 11.469  0.794   1.00 44.53  ?  147 TYR B CE1   1 
ATOM   5211 C  CE2   . TYR B 1 161 ? -16.428 12.177  -1.468  1.00 40.50  ?  147 TYR B CE2   1 
ATOM   5212 C  CZ    . TYR B 1 161 ? -16.098 11.183  -0.561  1.00 50.40  ?  147 TYR B CZ    1 
ATOM   5213 O  OH    . TYR B 1 161 ? -15.822 9.907   -1.013  1.00 37.52  ?  147 TYR B OH    1 
ATOM   5214 N  N     . GLU B 1 162 ? -13.657 15.071  1.460   1.00 31.22  ?  148 GLU B N     1 
ATOM   5215 C  CA    . GLU B 1 162 ? -12.570 14.715  2.368   1.00 28.94  ?  148 GLU B CA    1 
ATOM   5216 C  C     . GLU B 1 162 ? -11.902 15.964  2.937   1.00 30.18  ?  148 GLU B C     1 
ATOM   5217 O  O     . GLU B 1 162 ? -11.519 15.989  4.115   1.00 26.12  ?  148 GLU B O     1 
ATOM   5218 C  CB    . GLU B 1 162 ? -11.549 13.825  1.654   1.00 32.24  ?  148 GLU B CB    1 
ATOM   5219 C  CG    . GLU B 1 162 ? -11.965 12.358  1.521   1.00 32.50  ?  148 GLU B CG    1 
ATOM   5220 C  CD    . GLU B 1 162 ? -12.201 11.675  2.859   1.00 30.85  ?  148 GLU B CD    1 
ATOM   5221 O  OE1   . GLU B 1 162 ? -13.282 11.861  3.446   1.00 36.29  ?  148 GLU B OE1   1 
ATOM   5222 O  OE2   . GLU B 1 162 ? -11.306 10.943  3.329   1.00 38.42  ?  148 GLU B OE2   1 
ATOM   5223 N  N     . ILE B 1 163 ? -11.769 17.016  2.125   1.00 25.60  ?  149 ILE B N     1 
ATOM   5224 C  CA    . ILE B 1 163 ? -11.257 18.288  2.633   1.00 25.25  ?  149 ILE B CA    1 
ATOM   5225 C  C     . ILE B 1 163 ? -12.164 18.806  3.743   1.00 28.58  ?  149 ILE B C     1 
ATOM   5226 O  O     . ILE B 1 163 ? -11.705 19.159  4.836   1.00 28.87  ?  149 ILE B O     1 
ATOM   5227 C  CB    . ILE B 1 163 ? -11.129 19.312  1.491   1.00 26.83  ?  149 ILE B CB    1 
ATOM   5228 C  CG1   . ILE B 1 163 ? -9.923  18.993  0.603   1.00 35.72  ?  149 ILE B CG1   1 
ATOM   5229 C  CG2   . ILE B 1 163 ? -10.998 20.732  2.045   1.00 29.61  ?  149 ILE B CG2   1 
ATOM   5230 C  CD1   . ILE B 1 163 ? -9.987  19.642  -0.777  1.00 24.17  ?  149 ILE B CD1   1 
ATOM   5231 N  N     . ASP B 1 164 ? -13.475 18.815  3.492   1.00 27.00  ?  150 ASP B N     1 
ATOM   5232 C  CA    . ASP B 1 164 ? -14.413 19.335  4.480   1.00 27.62  ?  150 ASP B CA    1 
ATOM   5233 C  C     . ASP B 1 164 ? -14.447 18.467  5.732   1.00 33.29  ?  150 ASP B C     1 
ATOM   5234 O  O     . ASP B 1 164 ? -14.538 18.991  6.848   1.00 31.36  ?  150 ASP B O     1 
ATOM   5235 C  CB    . ASP B 1 164 ? -15.809 19.456  3.865   1.00 29.23  ?  150 ASP B CB    1 
ATOM   5236 C  CG    . ASP B 1 164 ? -15.885 20.527  2.785   1.00 31.20  ?  150 ASP B CG    1 
ATOM   5237 O  OD1   . ASP B 1 164 ? -14.980 21.385  2.727   1.00 36.13  ?  150 ASP B OD1   1 
ATOM   5238 O  OD2   . ASP B 1 164 ? -16.858 20.525  2.003   1.00 39.50  ?  150 ASP B OD2   1 
ATOM   5239 N  N     . ARG B 1 165 ? -14.369 17.138  5.570   1.00 28.59  ?  151 ARG B N     1 
ATOM   5240 C  CA    . ARG B 1 165 ? -14.402 16.245  6.728   1.00 28.61  ?  151 ARG B CA    1 
ATOM   5241 C  C     . ARG B 1 165 ? -13.190 16.458  7.628   1.00 29.48  ?  151 ARG B C     1 
ATOM   5242 O  O     . ARG B 1 165 ? -13.324 16.577  8.853   1.00 28.67  ?  151 ARG B O     1 
ATOM   5243 C  CB    . ARG B 1 165 ? -14.463 14.783  6.274   1.00 28.10  ?  151 ARG B CB    1 
ATOM   5244 C  CG    . ARG B 1 165 ? -14.167 13.799  7.399   1.00 27.83  ?  151 ARG B CG    1 
ATOM   5245 C  CD    . ARG B 1 165 ? -14.166 12.342  6.924   1.00 38.59  ?  151 ARG B CD    1 
ATOM   5246 N  NE    . ARG B 1 165 ? -12.936 11.973  6.227   1.00 27.54  ?  151 ARG B NE    1 
ATOM   5247 C  CZ    . ARG B 1 165 ? -11.782 11.714  6.827   1.00 36.19  ?  151 ARG B CZ    1 
ATOM   5248 N  NH1   . ARG B 1 165 ? -11.654 11.792  8.144   1.00 24.85  ?  151 ARG B NH1   1 
ATOM   5249 N  NH2   . ARG B 1 165 ? -10.728 11.376  6.087   1.00 23.20  ?  151 ARG B NH2   1 
ATOM   5250 N  N     . VAL B 1 166 ? -11.993 16.511  7.037   1.00 25.90  ?  152 VAL B N     1 
ATOM   5251 C  CA    . VAL B 1 166 ? -10.781 16.673  7.837   1.00 28.38  ?  152 VAL B CA    1 
ATOM   5252 C  C     . VAL B 1 166 ? -10.799 18.014  8.560   1.00 28.17  ?  152 VAL B C     1 
ATOM   5253 O  O     . VAL B 1 166 ? -10.511 18.097  9.762   1.00 26.07  ?  152 VAL B O     1 
ATOM   5254 C  CB    . VAL B 1 166 ? -9.526  16.524  6.953   1.00 34.12  ?  152 VAL B CB    1 
ATOM   5255 C  CG1   . VAL B 1 166 ? -8.303  17.120  7.648   1.00 24.92  ?  152 VAL B CG1   1 
ATOM   5256 C  CG2   . VAL B 1 166 ? -9.286  15.051  6.604   1.00 32.32  ?  152 VAL B CG2   1 
ATOM   5257 N  N     . LEU B 1 167 ? -11.157 19.085  7.843   1.00 28.63  ?  153 LEU B N     1 
ATOM   5258 C  CA    . LEU B 1 167 ? -11.166 20.412  8.457   1.00 32.71  ?  153 LEU B CA    1 
ATOM   5259 C  C     . LEU B 1 167 ? -12.202 20.500  9.571   1.00 34.04  ?  153 LEU B C     1 
ATOM   5260 O  O     . LEU B 1 167 ? -11.932 21.071  10.636  1.00 30.81  ?  153 LEU B O     1 
ATOM   5261 C  CB    . LEU B 1 167 ? -11.418 21.485  7.393   1.00 30.84  ?  153 LEU B CB    1 
ATOM   5262 C  CG    . LEU B 1 167 ? -10.242 21.744  6.445   1.00 38.36  ?  153 LEU B CG    1 
ATOM   5263 C  CD1   . LEU B 1 167 ? -10.585 22.798  5.409   1.00 36.55  ?  153 LEU B CD1   1 
ATOM   5264 C  CD2   . LEU B 1 167 ? -9.029  22.169  7.234   1.00 30.74  ?  153 LEU B CD2   1 
ATOM   5265 N  N     . THR B 1 168 ? -13.388 19.920  9.351   1.00 25.37  ?  154 THR B N     1 
ATOM   5266 C  CA    . THR B 1 168 ? -14.428 19.934  10.375  1.00 31.80  ?  154 THR B CA    1 
ATOM   5267 C  C     . THR B 1 168 ? -13.987 19.183  11.624  1.00 31.92  ?  154 THR B C     1 
ATOM   5268 O  O     . THR B 1 168 ? -14.238 19.629  12.751  1.00 33.84  ?  154 THR B O     1 
ATOM   5269 C  CB    . THR B 1 168 ? -15.718 19.331  9.818   1.00 31.48  ?  154 THR B CB    1 
ATOM   5270 O  OG1   . THR B 1 168 ? -16.200 20.160  8.754   1.00 38.07  ?  154 THR B OG1   1 
ATOM   5271 C  CG2   . THR B 1 168 ? -16.776 19.254  10.903  1.00 35.22  ?  154 THR B CG2   1 
ATOM   5272 N  N     . THR B 1 169 ? -13.343 18.028  11.449  1.00 25.15  ?  155 THR B N     1 
ATOM   5273 C  CA    . THR B 1 169 ? -12.817 17.312  12.604  1.00 30.24  ?  155 THR B CA    1 
ATOM   5274 C  C     . THR B 1 169 ? -11.775 18.155  13.331  1.00 32.97  ?  155 THR B C     1 
ATOM   5275 O  O     . THR B 1 169 ? -11.783 18.239  14.566  1.00 34.98  ?  155 THR B O     1 
ATOM   5276 C  CB    . THR B 1 169 ? -12.231 15.972  12.159  1.00 32.67  ?  155 THR B CB    1 
ATOM   5277 O  OG1   . THR B 1 169 ? -13.233 15.236  11.441  1.00 30.69  ?  155 THR B OG1   1 
ATOM   5278 C  CG2   . THR B 1 169 ? -11.772 15.152  13.361  1.00 26.80  ?  155 THR B CG2   1 
ATOM   5279 N  N     . MET B 1 170 ? -10.898 18.821  12.575  1.00 30.13  ?  156 MET B N     1 
ATOM   5280 C  CA    . MET B 1 170 ? -9.915  19.722  13.170  1.00 36.58  ?  156 MET B CA    1 
ATOM   5281 C  C     . MET B 1 170 ? -10.590 20.800  14.009  1.00 39.49  ?  156 MET B C     1 
ATOM   5282 O  O     . MET B 1 170 ? -10.160 21.088  15.132  1.00 31.98  ?  156 MET B O     1 
ATOM   5283 C  CB    . MET B 1 170 ? -9.073  20.368  12.072  1.00 30.54  ?  156 MET B CB    1 
ATOM   5284 C  CG    . MET B 1 170 ? -7.874  19.565  11.638  1.00 34.19  ?  156 MET B CG    1 
ATOM   5285 S  SD    . MET B 1 170 ? -7.130  20.370  10.220  1.00 31.91  ?  156 MET B SD    1 
ATOM   5286 C  CE    . MET B 1 170 ? -6.294  21.686  11.103  1.00 28.39  ?  156 MET B CE    1 
ATOM   5287 N  N     . LEU B 1 171 ? -11.652 21.411  13.472  1.00 30.55  ?  157 LEU B N     1 
ATOM   5288 C  CA    . LEU B 1 171 ? -12.386 22.436  14.210  1.00 36.58  ?  157 LEU B CA    1 
ATOM   5289 C  C     . LEU B 1 171 ? -13.047 21.865  15.459  1.00 36.71  ?  157 LEU B C     1 
ATOM   5290 O  O     . LEU B 1 171 ? -13.084 22.523  16.506  1.00 38.63  ?  157 LEU B O     1 
ATOM   5291 C  CB    . LEU B 1 171 ? -13.441 23.077  13.310  1.00 34.55  ?  157 LEU B CB    1 
ATOM   5292 C  CG    . LEU B 1 171 ? -12.955 23.914  12.127  1.00 41.70  ?  157 LEU B CG    1 
ATOM   5293 C  CD1   . LEU B 1 171 ? -14.122 24.258  11.205  1.00 43.38  ?  157 LEU B CD1   1 
ATOM   5294 C  CD2   . LEU B 1 171 ? -12.261 25.170  12.617  1.00 31.70  ?  157 LEU B CD2   1 
ATOM   5295 N  N     . ARG B 1 172 ? -13.615 20.661  15.360  1.00 34.71  ?  158 ARG B N     1 
ATOM   5296 C  CA    . ARG B 1 172 ? -14.281 20.064  16.513  1.00 39.95  ?  158 ARG B CA    1 
ATOM   5297 C  C     . ARG B 1 172 ? -13.284 19.712  17.609  1.00 43.97  ?  158 ARG B C     1 
ATOM   5298 O  O     . ARG B 1 172 ? -13.517 20.002  18.788  1.00 41.01  ?  158 ARG B O     1 
ATOM   5299 C  CB    . ARG B 1 172 ? -15.073 18.826  16.088  1.00 32.75  ?  158 ARG B CB    1 
ATOM   5300 C  CG    . ARG B 1 172 ? -15.842 18.161  17.232  1.00 43.72  ?  158 ARG B CG    1 
ATOM   5301 C  CD    . ARG B 1 172 ? -16.798 17.085  16.715  1.00 41.26  ?  158 ARG B CD    1 
ATOM   5302 N  NE    . ARG B 1 172 ? -16.061 15.990  16.099  1.00 59.27  ?  158 ARG B NE    1 
ATOM   5303 C  CZ    . ARG B 1 172 ? -16.066 15.727  14.800  1.00 57.96  ?  158 ARG B CZ    1 
ATOM   5304 N  NH1   . ARG B 1 172 ? -16.805 16.431  13.955  1.00 44.10  ?  158 ARG B NH1   1 
ATOM   5305 N  NH2   . ARG B 1 172 ? -15.301 14.741  14.335  1.00 48.32  ?  158 ARG B NH2   1 
ATOM   5306 N  N     . GLU B 1 173 ? -12.170 19.081  17.242  1.00 33.18  ?  159 GLU B N     1 
ATOM   5307 C  CA    . GLU B 1 173 ? -11.232 18.582  18.237  1.00 39.58  ?  159 GLU B CA    1 
ATOM   5308 C  C     . GLU B 1 173 ? -10.108 19.556  18.551  1.00 37.46  ?  159 GLU B C     1 
ATOM   5309 O  O     . GLU B 1 173 ? -9.407  19.356  19.550  1.00 41.28  ?  159 GLU B O     1 
ATOM   5310 C  CB    . GLU B 1 173 ? -10.636 17.245  17.775  1.00 35.40  ?  159 GLU B CB    1 
ATOM   5311 C  CG    . GLU B 1 173 ? -11.673 16.225  17.347  1.00 39.32  ?  159 GLU B CG    1 
ATOM   5312 C  CD    . GLU B 1 173 ? -12.622 15.850  18.473  1.00 50.96  ?  159 GLU B CD    1 
ATOM   5313 O  OE1   . GLU B 1 173 ? -12.205 15.916  19.651  1.00 46.53  ?  159 GLU B OE1   1 
ATOM   5314 O  OE2   . GLU B 1 173 ? -13.782 15.485  18.182  1.00 55.01  ?  159 GLU B OE2   1 
ATOM   5315 N  N     . ARG B 1 174 ? -9.927  20.603  17.740  1.00 33.33  ?  160 ARG B N     1 
ATOM   5316 C  CA    . ARG B 1 174 ? -8.834  21.563  17.917  1.00 33.54  ?  160 ARG B CA    1 
ATOM   5317 C  C     . ARG B 1 174 ? -7.477  20.859  17.921  1.00 35.69  ?  160 ARG B C     1 
ATOM   5318 O  O     . ARG B 1 174 ? -6.688  20.987  18.855  1.00 34.98  ?  160 ARG B O     1 
ATOM   5319 C  CB    . ARG B 1 174 ? -9.027  22.393  19.190  1.00 33.32  ?  160 ARG B CB    1 
ATOM   5320 C  CG    . ARG B 1 174 ? -10.366 23.100  19.257  1.00 48.85  ?  160 ARG B CG    1 
ATOM   5321 C  CD    . ARG B 1 174 ? -10.543 24.015  18.062  1.00 36.92  ?  160 ARG B CD    1 
ATOM   5322 N  NE    . ARG B 1 174 ? -11.695 24.892  18.214  1.00 53.37  ?  160 ARG B NE    1 
ATOM   5323 C  CZ    . ARG B 1 174 ? -11.909 25.972  17.476  1.00 56.42  ?  160 ARG B CZ    1 
ATOM   5324 N  NH1   . ARG B 1 174 ? -11.049 26.352  16.543  1.00 61.08  ?  160 ARG B NH1   1 
ATOM   5325 N  NH2   . ARG B 1 174 ? -13.007 26.693  17.686  1.00 69.13  ?  160 ARG B NH2   1 
ATOM   5326 N  N     . ARG B 1 175 ? -7.222  20.084  16.873  1.00 29.55  ?  161 ARG B N     1 
ATOM   5327 C  CA    . ARG B 1 175 ? -6.007  19.291  16.759  1.00 33.27  ?  161 ARG B CA    1 
ATOM   5328 C  C     . ARG B 1 175 ? -5.630  19.214  15.289  1.00 33.69  ?  161 ARG B C     1 
ATOM   5329 O  O     . ARG B 1 175 ? -6.435  19.578  14.423  1.00 27.05  ?  161 ARG B O     1 
ATOM   5330 C  CB    . ARG B 1 175 ? -6.194  17.895  17.363  1.00 34.13  ?  161 ARG B CB    1 
ATOM   5331 C  CG    . ARG B 1 175 ? -6.010  17.854  18.868  1.00 32.97  ?  161 ARG B CG    1 
ATOM   5332 C  CD    . ARG B 1 175 ? -6.083  16.432  19.395  1.00 32.27  ?  161 ARG B CD    1 
ATOM   5333 N  NE    . ARG B 1 175 ? -5.085  16.183  20.428  1.00 35.04  ?  161 ARG B NE    1 
ATOM   5334 C  CZ    . ARG B 1 175 ? -5.233  15.307  21.411  1.00 29.78  ?  161 ARG B CZ    1 
ATOM   5335 N  NH1   . ARG B 1 175 ? -6.326  14.571  21.519  1.00 29.27  ?  161 ARG B NH1   1 
ATOM   5336 N  NH2   . ARG B 1 175 ? -4.264  15.171  22.312  1.00 27.46  ?  161 ARG B NH2   1 
ATOM   5337 N  N     . PRO B 1 176 ? -4.395  18.810  14.974  1.00 33.49  ?  162 PRO B N     1 
ATOM   5338 C  CA    . PRO B 1 176 ? -3.947  18.833  13.576  1.00 27.16  ?  162 PRO B CA    1 
ATOM   5339 C  C     . PRO B 1 176 ? -4.679  17.836  12.693  1.00 27.20  ?  162 PRO B C     1 
ATOM   5340 O  O     . PRO B 1 176 ? -5.195  16.813  13.151  1.00 27.86  ?  162 PRO B O     1 
ATOM   5341 C  CB    . PRO B 1 176 ? -2.456  18.477  13.669  1.00 28.94  ?  162 PRO B CB    1 
ATOM   5342 C  CG    . PRO B 1 176 ? -2.069  18.761  15.064  1.00 29.05  ?  162 PRO B CG    1 
ATOM   5343 C  CD    . PRO B 1 176 ? -3.287  18.497  15.892  1.00 34.12  ?  162 PRO B CD    1 
ATOM   5344 N  N     . GLY B 1 177 ? -4.733  18.175  11.400  1.00 30.91  ?  163 GLY B N     1 
ATOM   5345 C  CA    . GLY B 1 177 ? -5.168  17.252  10.377  1.00 25.61  ?  163 GLY B CA    1 
ATOM   5346 C  C     . GLY B 1 177 ? -4.135  17.192  9.265   1.00 31.37  ?  163 GLY B C     1 
ATOM   5347 O  O     . GLY B 1 177 ? -3.186  17.977  9.227   1.00 27.35  ?  163 GLY B O     1 
ATOM   5348 N  N     . TYR B 1 178 ? -4.343  16.256  8.345   1.00 27.05  ?  164 TYR B N     1 
ATOM   5349 C  CA    . TYR B 1 178 ? -3.341  15.959  7.327   1.00 26.67  ?  164 TYR B CA    1 
ATOM   5350 C  C     . TYR B 1 178 ? -4.033  15.707  5.997   1.00 26.13  ?  164 TYR B C     1 
ATOM   5351 O  O     . TYR B 1 178 ? -4.965  14.902  5.924   1.00 26.14  ?  164 TYR B O     1 
ATOM   5352 C  CB    . TYR B 1 178 ? -2.501  14.745  7.761   1.00 21.93  ?  164 TYR B CB    1 
ATOM   5353 C  CG    . TYR B 1 178 ? -1.452  14.231  6.787   1.00 30.81  ?  164 TYR B CG    1 
ATOM   5354 C  CD1   . TYR B 1 178 ? -1.814  13.601  5.602   1.00 22.38  ?  164 TYR B CD1   1 
ATOM   5355 C  CD2   . TYR B 1 178 ? -0.095  14.315  7.091   1.00 30.86  ?  164 TYR B CD2   1 
ATOM   5356 C  CE1   . TYR B 1 178 ? -0.859  13.108  4.726   1.00 26.44  ?  164 TYR B CE1   1 
ATOM   5357 C  CE2   . TYR B 1 178 ? 0.872   13.813  6.219   1.00 31.38  ?  164 TYR B CE2   1 
ATOM   5358 C  CZ    . TYR B 1 178 ? 0.482   13.212  5.038   1.00 26.08  ?  164 TYR B CZ    1 
ATOM   5359 O  OH    . TYR B 1 178 ? 1.429   12.715  4.162   1.00 23.81  ?  164 TYR B OH    1 
ATOM   5360 N  N     . LEU B 1 179 ? -3.563  16.365  4.944   1.00 26.35  ?  165 LEU B N     1 
ATOM   5361 C  CA    . LEU B 1 179 ? -4.096  16.154  3.603   1.00 27.73  ?  165 LEU B CA    1 
ATOM   5362 C  C     . LEU B 1 179 ? -2.940  15.877  2.657   1.00 30.64  ?  165 LEU B C     1 
ATOM   5363 O  O     . LEU B 1 179 ? -1.999  16.670  2.585   1.00 31.03  ?  165 LEU B O     1 
ATOM   5364 C  CB    . LEU B 1 179 ? -4.895  17.369  3.123   1.00 26.21  ?  165 LEU B CB    1 
ATOM   5365 C  CG    . LEU B 1 179 ? -6.248  17.616  3.784   1.00 28.17  ?  165 LEU B CG    1 
ATOM   5366 C  CD1   . LEU B 1 179 ? -6.776  18.967  3.350   1.00 26.94  ?  165 LEU B CD1   1 
ATOM   5367 C  CD2   . LEU B 1 179 ? -7.226  16.507  3.421   1.00 24.85  ?  165 LEU B CD2   1 
ATOM   5368 N  N     . MET B 1 180 ? -3.002  14.751  1.950   1.00 26.81  ?  166 MET B N     1 
ATOM   5369 C  CA    . MET B 1 180 ? -2.077  14.475  0.859   1.00 32.46  ?  166 MET B CA    1 
ATOM   5370 C  C     . MET B 1 180 ? -2.729  14.912  -0.444  1.00 31.30  ?  166 MET B C     1 
ATOM   5371 O  O     . MET B 1 180 ? -3.826  14.450  -0.783  1.00 26.92  ?  166 MET B O     1 
ATOM   5372 C  CB    . MET B 1 180 ? -1.691  12.994  0.805   1.00 22.09  ?  166 MET B CB    1 
ATOM   5373 C  CG    . MET B 1 180 ? -0.463  12.714  -0.065  1.00 35.72  ?  166 MET B CG    1 
ATOM   5374 S  SD    . MET B 1 180 ? -0.462  11.131  -0.947  1.00 35.83  ?  166 MET B SD    1 
ATOM   5375 C  CE    . MET B 1 180 ? 0.174   10.086  0.350   1.00 23.64  ?  166 MET B CE    1 
ATOM   5376 N  N     . LEU B 1 181 ? -2.045  15.786  -1.179  1.00 25.62  ?  167 LEU B N     1 
ATOM   5377 C  CA    . LEU B 1 181 ? -2.582  16.404  -2.388  1.00 28.87  ?  167 LEU B CA    1 
ATOM   5378 C  C     . LEU B 1 181 ? -1.674  16.055  -3.560  1.00 35.28  ?  167 LEU B C     1 
ATOM   5379 O  O     . LEU B 1 181 ? -0.670  16.743  -3.807  1.00 31.38  ?  167 LEU B O     1 
ATOM   5380 C  CB    . LEU B 1 181 ? -2.704  17.916  -2.210  1.00 29.17  ?  167 LEU B CB    1 
ATOM   5381 C  CG    . LEU B 1 181 ? -3.386  18.716  -3.319  1.00 36.20  ?  167 LEU B CG    1 
ATOM   5382 C  CD1   . LEU B 1 181 ? -4.766  18.150  -3.637  1.00 28.63  ?  167 LEU B CD1   1 
ATOM   5383 C  CD2   . LEU B 1 181 ? -3.474  20.169  -2.917  1.00 32.00  ?  167 LEU B CD2   1 
ATOM   5384 N  N     . PRO B 1 182 ? -1.970  14.979  -4.292  1.00 32.91  ?  168 PRO B N     1 
ATOM   5385 C  CA    . PRO B 1 182 ? -1.240  14.714  -5.536  1.00 31.33  ?  168 PRO B CA    1 
ATOM   5386 C  C     . PRO B 1 182 ? -1.404  15.872  -6.507  1.00 35.56  ?  168 PRO B C     1 
ATOM   5387 O  O     . PRO B 1 182 ? -2.450  16.526  -6.556  1.00 34.99  ?  168 PRO B O     1 
ATOM   5388 C  CB    . PRO B 1 182 ? -1.892  13.432  -6.068  1.00 35.07  ?  168 PRO B CB    1 
ATOM   5389 C  CG    . PRO B 1 182 ? -2.448  12.767  -4.856  1.00 30.08  ?  168 PRO B CG    1 
ATOM   5390 C  CD    . PRO B 1 182 ? -2.888  13.878  -3.944  1.00 27.69  ?  168 PRO B CD    1 
ATOM   5391 N  N     . ALA B 1 183 ? -0.344  16.133  -7.277  1.00 31.74  ?  169 ALA B N     1 
ATOM   5392 C  CA    . ALA B 1 183 ? -0.334  17.306  -8.148  1.00 40.43  ?  169 ALA B CA    1 
ATOM   5393 C  C     . ALA B 1 183 ? -1.473  17.260  -9.162  1.00 33.70  ?  169 ALA B C     1 
ATOM   5394 O  O     . ALA B 1 183 ? -2.067  18.294  -9.483  1.00 35.61  ?  169 ALA B O     1 
ATOM   5395 C  CB    . ALA B 1 183 ? 1.017   17.422  -8.858  1.00 36.02  ?  169 ALA B CB    1 
ATOM   5396 N  N     . ASP B 1 184 ? -1.788  16.069  -9.681  1.00 38.41  ?  170 ASP B N     1 
ATOM   5397 C  CA    . ASP B 1 184 ? -2.865  15.949  -10.663 1.00 36.73  ?  170 ASP B CA    1 
ATOM   5398 C  C     . ASP B 1 184 ? -4.233  16.176  -10.028 1.00 29.77  ?  170 ASP B C     1 
ATOM   5399 O  O     . ASP B 1 184 ? -5.126  16.744  -10.664 1.00 32.12  ?  170 ASP B O     1 
ATOM   5400 C  CB    . ASP B 1 184 ? -2.813  14.579  -11.341 1.00 31.86  ?  170 ASP B CB    1 
ATOM   5401 C  CG    . ASP B 1 184 ? -3.072  13.447  -10.378 1.00 36.99  ?  170 ASP B CG    1 
ATOM   5402 O  OD1   . ASP B 1 184 ? -2.559  13.512  -9.242  1.00 33.93  ?  170 ASP B OD1   1 
ATOM   5403 O  OD2   . ASP B 1 184 ? -3.794  12.500  -10.751 1.00 41.43  ?  170 ASP B OD2   1 
ATOM   5404 N  N     . VAL B 1 185 ? -4.421  15.732  -8.781  1.00 31.68  ?  171 VAL B N     1 
ATOM   5405 C  CA    . VAL B 1 185 ? -5.701  15.936  -8.107  1.00 31.89  ?  171 VAL B CA    1 
ATOM   5406 C  C     . VAL B 1 185 ? -5.948  17.424  -7.872  1.00 36.12  ?  171 VAL B C     1 
ATOM   5407 O  O     . VAL B 1 185 ? -7.085  17.901  -7.970  1.00 29.60  ?  171 VAL B O     1 
ATOM   5408 C  CB    . VAL B 1 185 ? -5.756  15.130  -6.795  1.00 31.93  ?  171 VAL B CB    1 
ATOM   5409 C  CG1   . VAL B 1 185 ? -7.046  15.426  -6.037  1.00 29.04  ?  171 VAL B CG1   1 
ATOM   5410 C  CG2   . VAL B 1 185 ? -5.645  13.624  -7.082  1.00 28.51  ?  171 VAL B CG2   1 
ATOM   5411 N  N     . ALA B 1 186 ? -4.886  18.180  -7.574  1.00 36.43  ?  172 ALA B N     1 
ATOM   5412 C  CA    . ALA B 1 186 ? -5.030  19.602  -7.273  1.00 31.81  ?  172 ALA B CA    1 
ATOM   5413 C  C     . ALA B 1 186 ? -5.635  20.379  -8.433  1.00 34.78  ?  172 ALA B C     1 
ATOM   5414 O  O     . ALA B 1 186 ? -6.268  21.418  -8.215  1.00 35.29  ?  172 ALA B O     1 
ATOM   5415 C  CB    . ALA B 1 186 ? -3.673  20.201  -6.903  1.00 27.42  ?  172 ALA B CB    1 
ATOM   5416 N  N     . LYS B 1 187 ? -5.434  19.914  -9.665  1.00 35.44  ?  173 LYS B N     1 
ATOM   5417 C  CA    . LYS B 1 187 ? -5.955  20.600  -10.839 1.00 40.09  ?  173 LYS B CA    1 
ATOM   5418 C  C     . LYS B 1 187 ? -7.360  20.161  -11.217 1.00 37.67  ?  173 LYS B C     1 
ATOM   5419 O  O     . LYS B 1 187 ? -7.933  20.722  -12.157 1.00 43.85  ?  173 LYS B O     1 
ATOM   5420 C  CB    . LYS B 1 187 ? -5.042  20.375  -12.042 1.00 42.20  ?  173 LYS B CB    1 
ATOM   5421 C  CG    . LYS B 1 187 ? -3.584  20.663  -11.789 1.00 51.54  ?  173 LYS B CG    1 
ATOM   5422 C  CD    . LYS B 1 187 ? -2.773  20.239  -12.993 1.00 55.61  ?  173 LYS B CD    1 
ATOM   5423 C  CE    . LYS B 1 187 ? -1.297  20.350  -12.722 1.00 66.87  ?  173 LYS B CE    1 
ATOM   5424 N  NZ    . LYS B 1 187 ? -0.505  19.750  -13.827 1.00 66.92  ?  173 LYS B NZ    1 
ATOM   5425 N  N     . LYS B 1 188 ? -7.917  19.170  -10.532 1.00 31.13  ?  174 LYS B N     1 
ATOM   5426 C  CA    . LYS B 1 188 ? -9.226  18.650  -10.897 1.00 34.00  ?  174 LYS B CA    1 
ATOM   5427 C  C     . LYS B 1 188 ? -10.294 19.716  -10.693 1.00 37.79  ?  174 LYS B C     1 
ATOM   5428 O  O     . LYS B 1 188 ? -10.215 20.520  -9.762  1.00 32.66  ?  174 LYS B O     1 
ATOM   5429 C  CB    . LYS B 1 188 ? -9.546  17.414  -10.060 1.00 33.49  ?  174 LYS B CB    1 
ATOM   5430 C  CG    . LYS B 1 188 ? -9.475  16.117  -10.826 1.00 39.03  ?  174 LYS B CG    1 
ATOM   5431 C  CD    . LYS B 1 188 ? -8.181  15.974  -11.590 1.00 33.82  ?  174 LYS B CD    1 
ATOM   5432 C  CE    . LYS B 1 188 ? -8.108  14.599  -12.240 1.00 48.87  ?  174 LYS B CE    1 
ATOM   5433 N  NZ    . LYS B 1 188 ? -7.359  14.603  -13.527 1.00 47.61  ?  174 LYS B NZ    1 
ATOM   5434 N  N     . ALA B 1 189 ? -11.292 19.718  -11.574 1.00 42.48  ?  175 ALA B N     1 
ATOM   5435 C  CA    . ALA B 1 189 ? -12.352 20.717  -11.512 1.00 45.34  ?  175 ALA B CA    1 
ATOM   5436 C  C     . ALA B 1 189 ? -13.109 20.619  -10.195 1.00 33.58  ?  175 ALA B C     1 
ATOM   5437 O  O     . ALA B 1 189 ? -13.322 19.530  -9.658  1.00 43.22  ?  175 ALA B O     1 
ATOM   5438 C  CB    . ALA B 1 189 ? -13.327 20.538  -12.679 1.00 37.48  ?  175 ALA B CB    1 
ATOM   5439 N  N     . ALA B 1 190 ? -13.498 21.775  -9.669  1.00 35.68  ?  176 ALA B N     1 
ATOM   5440 C  CA    . ALA B 1 190 ? -14.318 21.858  -8.472  1.00 38.17  ?  176 ALA B CA    1 
ATOM   5441 C  C     . ALA B 1 190 ? -15.310 22.997  -8.656  1.00 36.26  ?  176 ALA B C     1 
ATOM   5442 O  O     . ALA B 1 190 ? -15.255 23.741  -9.639  1.00 35.96  ?  176 ALA B O     1 
ATOM   5443 C  CB    . ALA B 1 190 ? -13.463 22.067  -7.217  1.00 27.70  ?  176 ALA B CB    1 
ATOM   5444 N  N     . THR B 1 191 ? -16.218 23.137  -7.692  1.00 38.23  ?  177 THR B N     1 
ATOM   5445 C  CA    . THR B 1 191 ? -17.221 24.187  -7.704  1.00 32.36  ?  177 THR B CA    1 
ATOM   5446 C  C     . THR B 1 191 ? -17.084 25.011  -6.434  1.00 37.23  ?  177 THR B C     1 
ATOM   5447 O  O     . THR B 1 191 ? -16.977 24.437  -5.340  1.00 36.51  ?  177 THR B O     1 
ATOM   5448 C  CB    . THR B 1 191 ? -18.648 23.594  -7.792  1.00 35.01  ?  177 THR B CB    1 
ATOM   5449 O  OG1   . THR B 1 191 ? -18.769 22.803  -8.979  1.00 37.21  ?  177 THR B OG1   1 
ATOM   5450 C  CG2   . THR B 1 191 ? -19.718 24.702  -7.811  1.00 35.19  ?  177 THR B CG2   1 
ATOM   5451 N  N     . PRO B 1 192 ? -17.053 26.338  -6.526  1.00 39.87  ?  178 PRO B N     1 
ATOM   5452 C  CA    . PRO B 1 192 ? -16.987 27.161  -5.317  1.00 34.84  ?  178 PRO B CA    1 
ATOM   5453 C  C     . PRO B 1 192 ? -18.225 26.946  -4.465  1.00 34.75  ?  178 PRO B C     1 
ATOM   5454 O  O     . PRO B 1 192 ? -19.355 27.004  -4.971  1.00 34.96  ?  178 PRO B O     1 
ATOM   5455 C  CB    . PRO B 1 192 ? -16.927 28.597  -5.862  1.00 38.00  ?  178 PRO B CB    1 
ATOM   5456 C  CG    . PRO B 1 192 ? -16.440 28.455  -7.261  1.00 42.48  ?  178 PRO B CG    1 
ATOM   5457 C  CD    . PRO B 1 192 ? -16.979 27.144  -7.754  1.00 33.63  ?  178 PRO B CD    1 
ATOM   5458 N  N     . PRO B 1 193 ? -18.055 26.706  -3.169  1.00 32.80  ?  179 PRO B N     1 
ATOM   5459 C  CA    . PRO B 1 193 ? -19.220 26.463  -2.314  1.00 33.98  ?  179 PRO B CA    1 
ATOM   5460 C  C     . PRO B 1 193 ? -19.983 27.744  -2.013  1.00 46.04  ?  179 PRO B C     1 
ATOM   5461 O  O     . PRO B 1 193 ? -19.398 28.813  -1.819  1.00 38.77  ?  179 PRO B O     1 
ATOM   5462 C  CB    . PRO B 1 193 ? -18.616 25.860  -1.039  1.00 37.43  ?  179 PRO B CB    1 
ATOM   5463 C  CG    . PRO B 1 193 ? -17.143 26.110  -1.111  1.00 40.60  ?  179 PRO B CG    1 
ATOM   5464 C  CD    . PRO B 1 193 ? -16.791 26.739  -2.421  1.00 32.17  ?  179 PRO B CD    1 
ATOM   5465 N  N     . VAL B 1 194 ? -21.311 27.620  -2.001  1.00 38.70  ?  180 VAL B N     1 
ATOM   5466 C  CA    . VAL B 1 194 ? -22.180 28.725  -1.620  1.00 41.29  ?  180 VAL B CA    1 
ATOM   5467 C  C     . VAL B 1 194 ? -22.089 28.985  -0.119  1.00 44.43  ?  180 VAL B C     1 
ATOM   5468 O  O     . VAL B 1 194 ? -22.201 30.129  0.336   1.00 42.83  ?  180 VAL B O     1 
ATOM   5469 C  CB    . VAL B 1 194 ? -23.622 28.444  -2.082  1.00 47.81  ?  180 VAL B CB    1 
ATOM   5470 C  CG1   . VAL B 1 194 ? -24.626 29.131  -1.187  1.00 56.67  ?  180 VAL B CG1   1 
ATOM   5471 C  CG2   . VAL B 1 194 ? -23.800 28.905  -3.516  1.00 47.21  ?  180 VAL B CG2   1 
ATOM   5472 N  N     . ASN B 1 195 ? -21.912 27.936  0.680   1.00 38.51  ?  181 ASN B N     1 
ATOM   5473 C  CA    . ASN B 1 195 ? -21.911 28.070  2.130   1.00 45.68  ?  181 ASN B CA    1 
ATOM   5474 C  C     . ASN B 1 195 ? -20.498 27.901  2.669   1.00 41.24  ?  181 ASN B C     1 
ATOM   5475 O  O     . ASN B 1 195 ? -19.816 26.924  2.344   1.00 48.83  ?  181 ASN B O     1 
ATOM   5476 C  CB    . ASN B 1 195 ? -22.844 27.042  2.780   1.00 50.35  ?  181 ASN B CB    1 
ATOM   5477 C  CG    . ASN B 1 195 ? -24.221 27.002  2.128   1.00 64.21  ?  181 ASN B CG    1 
ATOM   5478 O  OD1   . ASN B 1 195 ? -24.351 26.711  0.937   1.00 71.54  ?  181 ASN B OD1   1 
ATOM   5479 N  ND2   . ASN B 1 195 ? -25.254 27.304  2.907   1.00 49.35  ?  181 ASN B ND2   1 
ATOM   5480 N  N     . ALA B 1 196 ? -20.075 28.848  3.502   1.00 37.44  ?  182 ALA B N     1 
ATOM   5481 C  CA    . ALA B 1 196 ? -18.768 28.778  4.133   1.00 39.43  ?  182 ALA B CA    1 
ATOM   5482 C  C     . ALA B 1 196 ? -18.752 27.672  5.176   1.00 48.07  ?  182 ALA B C     1 
ATOM   5483 O  O     . ALA B 1 196 ? -19.725 27.481  5.912   1.00 41.23  ?  182 ALA B O     1 
ATOM   5484 C  CB    . ALA B 1 196 ? -18.420 30.122  4.779   1.00 53.33  ?  182 ALA B CB    1 
ATOM   5485 N  N     . LEU B 1 197 ? -17.625 26.963  5.256   1.00 39.86  ?  183 LEU B N     1 
ATOM   5486 C  CA    . LEU B 1 197 ? -17.478 25.877  6.217   1.00 45.29  ?  183 LEU B CA    1 
ATOM   5487 C  C     . LEU B 1 197 ? -17.590 26.402  7.641   1.00 44.39  ?  183 LEU B C     1 
ATOM   5488 O  O     . LEU B 1 197 ? -16.863 27.319  8.033   1.00 45.49  ?  183 LEU B O     1 
ATOM   5489 C  CB    . LEU B 1 197 ? -16.137 25.170  6.008   1.00 40.11  ?  183 LEU B CB    1 
ATOM   5490 C  CG    . LEU B 1 197 ? -15.892 23.893  6.814   1.00 46.76  ?  183 LEU B CG    1 
ATOM   5491 C  CD1   . LEU B 1 197 ? -16.908 22.835  6.437   1.00 42.60  ?  183 LEU B CD1   1 
ATOM   5492 C  CD2   . LEU B 1 197 ? -14.465 23.369  6.610   1.00 34.96  ?  183 LEU B CD2   1 
ATOM   5493 N  N     . THR B 1 198 ? -18.519 25.834  8.404   1.00 57.29  ?  184 THR B N     1 
ATOM   5494 C  CA    . THR B 1 198 ? -18.705 26.175  9.805   1.00 62.50  ?  184 THR B CA    1 
ATOM   5495 C  C     . THR B 1 198 ? -19.082 24.916  10.575  1.00 74.25  ?  184 THR B C     1 
ATOM   5496 O  O     . THR B 1 198 ? -19.610 23.956  10.005  1.00 69.04  ?  184 THR B O     1 
ATOM   5497 C  CB    . THR B 1 198 ? -19.763 27.271  9.984   1.00 60.45  ?  184 THR B CB    1 
ATOM   5498 O  OG1   . THR B 1 198 ? -19.715 27.769  11.328  1.00 72.07  ?  184 THR B OG1   1 
ATOM   5499 C  CG2   . THR B 1 198 ? -21.144 26.735  9.681   1.00 62.68  ?  184 THR B CG2   1 
ATOM   5500 N  N     . LEU B 1 199 ? -18.784 24.918  11.875  1.00 62.44  ?  185 LEU B N     1 
ATOM   5501 C  CA    . LEU B 1 199 ? -19.005 23.736  12.701  1.00 68.16  ?  185 LEU B CA    1 
ATOM   5502 C  C     . LEU B 1 199 ? -20.371 23.711  13.384  1.00 76.83  ?  185 LEU B C     1 
ATOM   5503 O  O     . LEU B 1 199 ? -21.046 22.676  13.372  1.00 91.57  ?  185 LEU B O     1 
ATOM   5504 C  CB    . LEU B 1 199 ? -17.905 23.625  13.756  1.00 65.97  ?  185 LEU B CB    1 
ATOM   5505 C  CG    . LEU B 1 199 ? -17.952 22.346  14.587  1.00 62.75  ?  185 LEU B CG    1 
ATOM   5506 C  CD1   . LEU B 1 199 ? -18.149 21.112  13.712  1.00 67.21  ?  185 LEU B CD1   1 
ATOM   5507 C  CD2   . LEU B 1 199 ? -16.696 22.242  15.402  1.00 58.72  ?  185 LEU B CD2   1 
ATOM   5508 N  N     . ARG B 1 200 ? -20.798 24.831  13.974  1.00 73.87  ?  186 ARG B N     1 
ATOM   5509 C  CA    . ARG B 1 200 ? -22.076 24.911  14.689  1.00 84.76  ?  186 ARG B CA    1 
ATOM   5510 C  C     . ARG B 1 200 ? -22.106 23.921  15.860  1.00 87.22  ?  186 ARG B C     1 
ATOM   5511 O  O     . ARG B 1 200 ? -22.704 22.845  15.789  1.00 100.87 ?  186 ARG B O     1 
ATOM   5512 C  CB    . ARG B 1 200 ? -23.268 24.682  13.753  1.00 84.03  ?  186 ARG B CB    1 
ATOM   5513 C  CG    . ARG B 1 200 ? -23.343 25.636  12.586  1.00 77.40  ?  186 ARG B CG    1 
ATOM   5514 C  CD    . ARG B 1 200 ? -23.647 24.884  11.308  1.00 75.29  ?  186 ARG B CD    1 
ATOM   5515 N  NE    . ARG B 1 200 ? -24.967 25.221  10.792  1.00 73.71  ?  186 ARG B NE    1 
ATOM   5516 C  CZ    . ARG B 1 200 ? -25.237 25.438  9.513   1.00 76.39  ?  186 ARG B CZ    1 
ATOM   5517 N  NH1   . ARG B 1 200 ? -24.296 25.359  8.585   1.00 78.11  ?  186 ARG B NH1   1 
ATOM   5518 N  NH2   . ARG B 1 200 ? -26.480 25.749  9.156   1.00 88.01  ?  186 ARG B NH2   1 
ATOM   5519 N  N     . HIS B 1 201 ? -21.365 24.297  16.910  1.00 88.37  ?  187 HIS B N     1 
ATOM   5520 C  CA    . HIS B 1 201 ? -21.166 23.479  18.108  1.00 93.01  ?  187 HIS B CA    1 
ATOM   5521 C  C     . HIS B 1 201 ? -22.418 22.693  18.488  1.00 90.94  ?  187 HIS B C     1 
ATOM   5522 O  O     . HIS B 1 201 ? -23.535 23.218  18.471  1.00 81.46  ?  187 HIS B O     1 
ATOM   5523 C  CB    . HIS B 1 201 ? -20.733 24.370  19.279  1.00 89.42  ?  187 HIS B CB    1 
ATOM   5524 C  CG    . HIS B 1 201 ? -21.592 25.581  19.472  1.00 82.99  ?  187 HIS B CG    1 
ATOM   5525 N  ND1   . HIS B 1 201 ? -22.958 25.564  19.284  1.00 100.85 ?  187 HIS B ND1   1 
ATOM   5526 C  CD2   . HIS B 1 201 ? -21.280 26.846  19.842  1.00 92.80  ?  187 HIS B CD2   1 
ATOM   5527 C  CE1   . HIS B 1 201 ? -23.450 26.766  19.527  1.00 100.31 ?  187 HIS B CE1   1 
ATOM   5528 N  NE2   . HIS B 1 201 ? -22.453 27.563  19.867  1.00 101.60 ?  187 HIS B NE2   1 
ATOM   5529 N  N     . ALA B 1 202 ? -22.212 21.430  18.849  1.00 84.53  ?  188 ALA B N     1 
ATOM   5530 C  CA    . ALA B 1 202 ? -23.282 20.500  19.163  1.00 74.32  ?  188 ALA B CA    1 
ATOM   5531 C  C     . ALA B 1 202 ? -23.891 20.785  20.536  1.00 74.66  ?  188 ALA B C     1 
ATOM   5532 O  O     . ALA B 1 202 ? -23.400 21.607  21.316  1.00 62.09  ?  188 ALA B O     1 
ATOM   5533 C  CB    . ALA B 1 202 ? -22.763 19.064  19.105  1.00 63.24  ?  188 ALA B CB    1 
ATOM   5534 N  N     . HIS B 1 203 ? -24.996 20.091  20.816  1.00 61.14  ?  189 HIS B N     1 
ATOM   5535 C  CA    . HIS B 1 203 ? -25.726 20.218  22.069  1.00 57.96  ?  189 HIS B CA    1 
ATOM   5536 C  C     . HIS B 1 203 ? -25.886 18.845  22.704  1.00 58.88  ?  189 HIS B C     1 
ATOM   5537 O  O     . HIS B 1 203 ? -26.173 17.860  22.017  1.00 65.78  ?  189 HIS B O     1 
ATOM   5538 C  CB    . HIS B 1 203 ? -27.107 20.854  21.856  1.00 64.59  ?  189 HIS B CB    1 
ATOM   5539 C  CG    . HIS B 1 203 ? -27.069 22.144  21.096  1.00 83.61  ?  189 HIS B CG    1 
ATOM   5540 N  ND1   . HIS B 1 203 ? -27.086 22.197  19.719  1.00 84.65  ?  189 HIS B ND1   1 
ATOM   5541 C  CD2   . HIS B 1 203 ? -27.025 23.429  21.522  1.00 87.50  ?  189 HIS B CD2   1 
ATOM   5542 C  CE1   . HIS B 1 203 ? -27.048 23.459  19.329  1.00 89.76  ?  189 HIS B CE1   1 
ATOM   5543 N  NE2   . HIS B 1 203 ? -27.012 24.227  20.403  1.00 90.47  ?  189 HIS B NE2   1 
ATOM   5544 N  N     . ALA B 1 204 ? -25.688 18.785  24.016  1.00 47.95  ?  190 ALA B N     1 
ATOM   5545 C  CA    . ALA B 1 204 ? -25.898 17.549  24.748  1.00 48.27  ?  190 ALA B CA    1 
ATOM   5546 C  C     . ALA B 1 204 ? -27.366 17.148  24.736  1.00 61.29  ?  190 ALA B C     1 
ATOM   5547 O  O     . ALA B 1 204 ? -28.269 17.988  24.697  1.00 55.37  ?  190 ALA B O     1 
ATOM   5548 C  CB    . ALA B 1 204 ? -25.420 17.693  26.193  1.00 52.70  ?  190 ALA B CB    1 
ATOM   5549 N  N     . ASP B 1 205 ? -27.596 15.839  24.767  1.00 62.25  ?  191 ASP B N     1 
ATOM   5550 C  CA    . ASP B 1 205 ? -28.923 15.323  25.049  1.00 53.01  ?  191 ASP B CA    1 
ATOM   5551 C  C     . ASP B 1 205 ? -29.421 15.925  26.356  1.00 55.37  ?  191 ASP B C     1 
ATOM   5552 O  O     . ASP B 1 205 ? -28.671 16.015  27.333  1.00 54.77  ?  191 ASP B O     1 
ATOM   5553 C  CB    . ASP B 1 205 ? -28.878 13.796  25.130  1.00 55.34  ?  191 ASP B CB    1 
ATOM   5554 C  CG    . ASP B 1 205 ? -30.241 13.190  25.346  1.00 55.03  ?  191 ASP B CG    1 
ATOM   5555 O  OD1   . ASP B 1 205 ? -30.949 12.948  24.343  1.00 55.65  ?  191 ASP B OD1   1 
ATOM   5556 O  OD2   . ASP B 1 205 ? -30.604 12.961  26.520  1.00 57.49  ?  191 ASP B OD2   1 
ATOM   5557 N  N     . SER B 1 206 ? -30.677 16.384  26.355  1.00 55.43  ?  192 SER B N     1 
ATOM   5558 C  CA    . SER B 1 206 ? -31.169 17.189  27.470  1.00 42.03  ?  192 SER B CA    1 
ATOM   5559 C  C     . SER B 1 206 ? -31.224 16.401  28.775  1.00 53.87  ?  192 SER B C     1 
ATOM   5560 O  O     . SER B 1 206 ? -31.049 16.983  29.851  1.00 54.46  ?  192 SER B O     1 
ATOM   5561 C  CB    . SER B 1 206 ? -32.545 17.777  27.140  1.00 48.35  ?  192 SER B CB    1 
ATOM   5562 O  OG    . SER B 1 206 ? -33.409 16.817  26.570  1.00 60.42  ?  192 SER B OG    1 
ATOM   5563 N  N     . ALA B 1 207 ? -31.484 15.090  28.713  1.00 51.86  ?  193 ALA B N     1 
ATOM   5564 C  CA    . ALA B 1 207 ? -31.443 14.286  29.932  1.00 44.07  ?  193 ALA B CA    1 
ATOM   5565 C  C     . ALA B 1 207 ? -30.020 14.153  30.466  1.00 43.81  ?  193 ALA B C     1 
ATOM   5566 O  O     . ALA B 1 207 ? -29.800 14.215  31.682  1.00 49.68  ?  193 ALA B O     1 
ATOM   5567 C  CB    . ALA B 1 207 ? -32.052 12.909  29.683  1.00 45.54  ?  193 ALA B CB    1 
ATOM   5568 N  N     . CYS B 1 208 ? -29.041 13.958  29.578  1.00 42.32  ?  194 CYS B N     1 
ATOM   5569 C  CA    . CYS B 1 208 ? -27.653 13.868  30.023  1.00 44.98  ?  194 CYS B CA    1 
ATOM   5570 C  C     . CYS B 1 208 ? -27.177 15.181  30.635  1.00 49.91  ?  194 CYS B C     1 
ATOM   5571 O  O     . CYS B 1 208 ? -26.547 15.186  31.699  1.00 49.91  ?  194 CYS B O     1 
ATOM   5572 C  CB    . CYS B 1 208 ? -26.749 13.468  28.861  1.00 58.64  ?  194 CYS B CB    1 
ATOM   5573 S  SG    . CYS B 1 208 ? -25.020 13.218  29.346  1.00 65.14  ?  194 CYS B SG    1 
ATOM   5574 N  N     . LEU B 1 209 ? -27.477 16.307  29.983  1.00 48.09  ?  195 LEU B N     1 
ATOM   5575 C  CA    . LEU B 1 209 ? -27.093 17.600  30.541  1.00 46.36  ?  195 LEU B CA    1 
ATOM   5576 C  C     . LEU B 1 209 ? -27.775 17.840  31.881  1.00 48.33  ?  195 LEU B C     1 
ATOM   5577 O  O     . LEU B 1 209 ? -27.142 18.321  32.830  1.00 44.56  ?  195 LEU B O     1 
ATOM   5578 C  CB    . LEU B 1 209 ? -27.428 18.721  29.556  1.00 45.33  ?  195 LEU B CB    1 
ATOM   5579 C  CG    . LEU B 1 209 ? -27.004 20.140  29.958  1.00 57.95  ?  195 LEU B CG    1 
ATOM   5580 C  CD1   . LEU B 1 209 ? -25.588 20.152  30.498  1.00 46.19  ?  195 LEU B CD1   1 
ATOM   5581 C  CD2   . LEU B 1 209 ? -27.136 21.104  28.786  1.00 52.74  ?  195 LEU B CD2   1 
ATOM   5582 N  N     . LYS B 1 210 ? -29.064 17.497  31.981  1.00 43.35  ?  196 LYS B N     1 
ATOM   5583 C  CA    . LYS B 1 210 ? -29.782 17.646  33.243  1.00 42.81  ?  196 LYS B CA    1 
ATOM   5584 C  C     . LYS B 1 210 ? -29.162 16.781  34.334  1.00 46.81  ?  196 LYS B C     1 
ATOM   5585 O  O     . LYS B 1 210 ? -29.056 17.206  35.491  1.00 43.29  ?  196 LYS B O     1 
ATOM   5586 C  CB    . LYS B 1 210 ? -31.260 17.296  33.051  1.00 50.29  ?  196 LYS B CB    1 
ATOM   5587 C  CG    . LYS B 1 210 ? -32.083 17.353  34.328  1.00 46.57  ?  196 LYS B CG    1 
ATOM   5588 C  CD    . LYS B 1 210 ? -33.482 16.778  34.151  1.00 58.20  ?  196 LYS B CD    1 
ATOM   5589 C  CE    . LYS B 1 210 ? -34.266 16.833  35.459  1.00 49.11  ?  196 LYS B CE    1 
ATOM   5590 N  NZ    . LYS B 1 210 ? -35.733 16.685  35.246  1.00 68.60  ?  196 LYS B NZ    1 
ATOM   5591 N  N     . ALA B 1 211 ? -28.761 15.553  33.988  1.00 43.79  ?  197 ALA B N     1 
ATOM   5592 C  CA    . ALA B 1 211 ? -28.101 14.687  34.960  1.00 45.05  ?  197 ALA B CA    1 
ATOM   5593 C  C     . ALA B 1 211 ? -26.793 15.297  35.450  1.00 44.68  ?  197 ALA B C     1 
ATOM   5594 O  O     . ALA B 1 211 ? -26.501 15.273  36.652  1.00 51.52  ?  197 ALA B O     1 
ATOM   5595 C  CB    . ALA B 1 211 ? -27.856 13.308  34.355  1.00 56.96  ?  197 ALA B CB    1 
ATOM   5596 N  N     . PHE B 1 212 ? -25.979 15.835  34.537  1.00 40.50  ?  198 PHE B N     1 
ATOM   5597 C  CA    . PHE B 1 212 ? -24.778 16.534  34.981  1.00 43.52  ?  198 PHE B CA    1 
ATOM   5598 C  C     . PHE B 1 212 ? -25.136 17.750  35.825  1.00 49.91  ?  198 PHE B C     1 
ATOM   5599 O  O     . PHE B 1 212 ? -24.523 17.988  36.871  1.00 45.97  ?  198 PHE B O     1 
ATOM   5600 C  CB    . PHE B 1 212 ? -23.920 16.964  33.794  1.00 45.59  ?  198 PHE B CB    1 
ATOM   5601 C  CG    . PHE B 1 212 ? -22.824 17.929  34.171  1.00 53.57  ?  198 PHE B CG    1 
ATOM   5602 C  CD1   . PHE B 1 212 ? -21.709 17.492  34.873  1.00 38.04  ?  198 PHE B CD1   1 
ATOM   5603 C  CD2   . PHE B 1 212 ? -22.920 19.279  33.850  1.00 49.68  ?  198 PHE B CD2   1 
ATOM   5604 C  CE1   . PHE B 1 212 ? -20.704 18.381  35.233  1.00 44.96  ?  198 PHE B CE1   1 
ATOM   5605 C  CE2   . PHE B 1 212 ? -21.918 20.174  34.207  1.00 37.01  ?  198 PHE B CE2   1 
ATOM   5606 C  CZ    . PHE B 1 212 ? -20.813 19.727  34.901  1.00 39.67  ?  198 PHE B CZ    1 
ATOM   5607 N  N     . ARG B 1 213 ? -26.136 18.526  35.393  1.00 49.84  ?  199 ARG B N     1 
ATOM   5608 C  CA    . ARG B 1 213 ? -26.519 19.716  36.145  1.00 49.74  ?  199 ARG B CA    1 
ATOM   5609 C  C     . ARG B 1 213 ? -26.975 19.352  37.551  1.00 59.53  ?  199 ARG B C     1 
ATOM   5610 O  O     . ARG B 1 213 ? -26.558 19.981  38.530  1.00 50.45  ?  199 ARG B O     1 
ATOM   5611 C  CB    . ARG B 1 213 ? -27.622 20.483  35.413  1.00 48.83  ?  199 ARG B CB    1 
ATOM   5612 C  CG    . ARG B 1 213 ? -28.434 21.379  36.338  1.00 54.12  ?  199 ARG B CG    1 
ATOM   5613 C  CD    . ARG B 1 213 ? -29.498 22.170  35.599  1.00 68.57  ?  199 ARG B CD    1 
ATOM   5614 N  NE    . ARG B 1 213 ? -29.624 23.531  36.110  1.00 81.44  ?  199 ARG B NE    1 
ATOM   5615 C  CZ    . ARG B 1 213 ? -30.183 23.849  37.271  1.00 85.77  ?  199 ARG B CZ    1 
ATOM   5616 N  NH1   . ARG B 1 213 ? -30.693 22.929  38.072  1.00 60.93  ?  199 ARG B NH1   1 
ATOM   5617 N  NH2   . ARG B 1 213 ? -30.237 25.124  37.636  1.00 87.06  ?  199 ARG B NH2   1 
ATOM   5618 N  N     . ASP B 1 214 ? -27.817 18.318  37.670  1.00 57.06  ?  200 ASP B N     1 
ATOM   5619 C  CA    . ASP B 1 214 ? -28.324 17.917  38.980  1.00 47.85  ?  200 ASP B CA    1 
ATOM   5620 C  C     . ASP B 1 214 ? -27.198 17.439  39.891  1.00 52.94  ?  200 ASP B C     1 
ATOM   5621 O  O     . ASP B 1 214 ? -27.172 17.768  41.083  1.00 58.46  ?  200 ASP B O     1 
ATOM   5622 C  CB    . ASP B 1 214 ? -29.392 16.834  38.827  1.00 60.63  ?  200 ASP B CB    1 
ATOM   5623 C  CG    . ASP B 1 214 ? -30.740 17.398  38.410  1.00 70.41  ?  200 ASP B CG    1 
ATOM   5624 O  OD1   . ASP B 1 214 ? -31.343 18.152  39.203  1.00 77.26  ?  200 ASP B OD1   1 
ATOM   5625 O  OD2   . ASP B 1 214 ? -31.197 17.099  37.289  1.00 66.31  ?  200 ASP B OD2   1 
ATOM   5626 N  N     . ALA B 1 215 ? -26.259 16.659  39.354  1.00 43.25  ?  201 ALA B N     1 
ATOM   5627 C  CA    . ALA B 1 215 ? -25.126 16.237  40.169  1.00 53.00  ?  201 ALA B CA    1 
ATOM   5628 C  C     . ALA B 1 215 ? -24.244 17.429  40.522  1.00 46.14  ?  201 ALA B C     1 
ATOM   5629 O  O     . ALA B 1 215 ? -23.751 17.534  41.652  1.00 49.47  ?  201 ALA B O     1 
ATOM   5630 C  CB    . ALA B 1 215 ? -24.325 15.156  39.442  1.00 42.68  ?  201 ALA B CB    1 
ATOM   5631 N  N     . ALA B 1 216 ? -24.017 18.328  39.561  1.00 49.36  ?  202 ALA B N     1 
ATOM   5632 C  CA    . ALA B 1 216 ? -23.262 19.546  39.849  1.00 50.14  ?  202 ALA B CA    1 
ATOM   5633 C  C     . ALA B 1 216 ? -24.043 20.471  40.776  1.00 53.99  ?  202 ALA B C     1 
ATOM   5634 O  O     . ALA B 1 216 ? -23.459 21.110  41.659  1.00 54.72  ?  202 ALA B O     1 
ATOM   5635 C  CB    . ALA B 1 216 ? -22.889 20.262  38.551  1.00 40.91  ?  202 ALA B CB    1 
ATOM   5636 N  N     . GLU B 1 217 ? -25.366 20.556  40.594  1.00 49.25  ?  203 GLU B N     1 
ATOM   5637 C  CA    . GLU B 1 217 ? -26.172 21.385  41.484  1.00 63.00  ?  203 GLU B CA    1 
ATOM   5638 C  C     . GLU B 1 217 ? -26.062 20.898  42.919  1.00 63.78  ?  203 GLU B C     1 
ATOM   5639 O  O     . GLU B 1 217 ? -25.906 21.706  43.843  1.00 65.40  ?  203 GLU B O     1 
ATOM   5640 C  CB    . GLU B 1 217 ? -27.641 21.390  41.045  1.00 59.62  ?  203 GLU B CB    1 
ATOM   5641 C  CG    . GLU B 1 217 ? -28.507 22.405  41.783  1.00 56.01  ?  203 GLU B CG    1 
ATOM   5642 C  CD    . GLU B 1 217 ? -29.122 21.845  43.052  1.00 59.79  ?  203 GLU B CD    1 
ATOM   5643 O  OE1   . GLU B 1 217 ? -29.399 20.626  43.100  1.00 74.09  ?  203 GLU B OE1   1 
ATOM   5644 O  OE2   . GLU B 1 217 ? -29.319 22.627  44.008  1.00 69.84  ?  203 GLU B OE2   1 
ATOM   5645 N  N     . ASN B 1 218 ? -26.146 19.581  43.125  1.00 66.15  ?  204 ASN B N     1 
ATOM   5646 C  CA    . ASN B 1 218 ? -25.993 19.040  44.469  1.00 57.87  ?  204 ASN B CA    1 
ATOM   5647 C  C     . ASN B 1 218 ? -24.617 19.364  45.026  1.00 56.86  ?  204 ASN B C     1 
ATOM   5648 O  O     . ASN B 1 218 ? -24.498 19.961  46.100  1.00 67.63  ?  204 ASN B O     1 
ATOM   5649 C  CB    . ASN B 1 218 ? -26.210 17.527  44.458  1.00 57.34  ?  204 ASN B CB    1 
ATOM   5650 C  CG    . ASN B 1 218 ? -27.598 17.134  44.896  1.00 69.59  ?  204 ASN B CG    1 
ATOM   5651 O  OD1   . ASN B 1 218 ? -28.473 17.982  45.080  1.00 83.01  ?  204 ASN B OD1   1 
ATOM   5652 N  ND2   . ASN B 1 218 ? -27.812 15.837  45.066  1.00 90.89  ?  204 ASN B ND2   1 
ATOM   5653 N  N     . ARG B 1 219 ? -23.567 19.068  44.256  1.00 61.53  ?  205 ARG B N     1 
ATOM   5654 C  CA    . ARG B 1 219 ? -22.209 19.207  44.770  1.00 61.02  ?  205 ARG B CA    1 
ATOM   5655 C  C     . ARG B 1 219 ? -21.902 20.643  45.168  1.00 54.94  ?  205 ARG B C     1 
ATOM   5656 O  O     . ARG B 1 219 ? -21.315 20.885  46.229  1.00 69.67  ?  205 ARG B O     1 
ATOM   5657 C  CB    . ARG B 1 219 ? -21.205 18.714  43.734  1.00 64.83  ?  205 ARG B CB    1 
ATOM   5658 C  CG    . ARG B 1 219 ? -19.767 18.818  44.201  1.00 55.12  ?  205 ARG B CG    1 
ATOM   5659 C  CD    . ARG B 1 219 ? -19.504 17.871  45.362  1.00 48.88  ?  205 ARG B CD    1 
ATOM   5660 N  NE    . ARG B 1 219 ? -18.170 18.057  45.918  1.00 59.17  ?  205 ARG B NE    1 
ATOM   5661 C  CZ    . ARG B 1 219 ? -17.801 19.091  46.660  1.00 61.06  ?  205 ARG B CZ    1 
ATOM   5662 N  NH1   . ARG B 1 219 ? -18.655 20.048  46.986  1.00 66.65  ?  205 ARG B NH1   1 
ATOM   5663 N  NH2   . ARG B 1 219 ? -16.544 19.163  47.091  1.00 57.24  ?  205 ARG B NH2   1 
ATOM   5664 N  N     . LEU B 1 220 ? -22.287 21.612  44.335  1.00 59.40  ?  206 LEU B N     1 
ATOM   5665 C  CA    . LEU B 1 220 ? -22.038 23.007  44.684  1.00 59.34  ?  206 LEU B CA    1 
ATOM   5666 C  C     . LEU B 1 220 ? -22.897 23.448  45.861  1.00 62.26  ?  206 LEU B C     1 
ATOM   5667 O  O     . LEU B 1 220 ? -22.516 24.369  46.592  1.00 70.38  ?  206 LEU B O     1 
ATOM   5668 C  CB    . LEU B 1 220 ? -22.265 23.896  43.463  1.00 51.48  ?  206 LEU B CB    1 
ATOM   5669 C  CG    . LEU B 1 220 ? -21.097 23.772  42.479  1.00 53.51  ?  206 LEU B CG    1 
ATOM   5670 C  CD1   . LEU B 1 220 ? -21.490 24.170  41.075  1.00 51.28  ?  206 LEU B CD1   1 
ATOM   5671 C  CD2   . LEU B 1 220 ? -19.905 24.591  42.948  1.00 56.62  ?  206 LEU B CD2   1 
ATOM   5672 N  N     . ALA B 1 221 ? -24.056 22.810  46.053  1.00 65.03  ?  207 ALA B N     1 
ATOM   5673 C  CA    . ALA B 1 221 ? -24.943 23.189  47.148  1.00 61.02  ?  207 ALA B CA    1 
ATOM   5674 C  C     . ALA B 1 221 ? -24.308 22.952  48.514  1.00 55.61  ?  207 ALA B C     1 
ATOM   5675 O  O     . ALA B 1 221 ? -24.594 23.697  49.457  1.00 69.82  ?  207 ALA B O     1 
ATOM   5676 C  CB    . ALA B 1 221 ? -26.276 22.444  47.042  1.00 54.32  ?  207 ALA B CB    1 
ATOM   5677 N  N     . MET B 1 222 ? -23.461 21.930  48.663  1.00 60.57  ?  208 MET B N     1 
ATOM   5678 C  CA    . MET B 1 222 ? -22.782 21.729  49.941  1.00 70.28  ?  208 MET B CA    1 
ATOM   5679 C  C     . MET B 1 222 ? -21.368 22.299  49.956  1.00 64.48  ?  208 MET B C     1 
ATOM   5680 O  O     . MET B 1 222 ? -20.601 21.997  50.877  1.00 71.57  ?  208 MET B O     1 
ATOM   5681 C  CB    . MET B 1 222 ? -22.685 20.246  50.329  1.00 61.11  ?  208 MET B CB    1 
ATOM   5682 C  CG    . MET B 1 222 ? -21.811 19.379  49.411  1.00 68.12  ?  208 MET B CG    1 
ATOM   5683 S  SD    . MET B 1 222 ? -22.381 17.672  49.170  1.00 88.18  ?  208 MET B SD    1 
ATOM   5684 C  CE    . MET B 1 222 ? -23.579 17.776  47.835  1.00 78.99  ?  208 MET B CE    1 
ATOM   5685 N  N     . SER B 1 223 ? -21.005 23.115  48.971  1.00 63.78  ?  209 SER B N     1 
ATOM   5686 C  CA    . SER B 1 223 ? -19.685 23.731  48.947  1.00 74.61  ?  209 SER B CA    1 
ATOM   5687 C  C     . SER B 1 223 ? -19.659 24.992  49.802  1.00 63.72  ?  209 SER B C     1 
ATOM   5688 O  O     . SER B 1 223 ? -20.475 25.899  49.609  1.00 77.43  ?  209 SER B O     1 
ATOM   5689 C  CB    . SER B 1 223 ? -19.285 24.067  47.513  1.00 71.43  ?  209 SER B CB    1 
ATOM   5690 O  OG    . SER B 1 223 ? -20.167 25.026  46.959  1.00 70.33  ?  209 SER B OG    1 
ATOM   5691 N  N     . LYS B 1 224 ? -18.726 25.047  50.754  1.00 62.41  ?  210 LYS B N     1 
ATOM   5692 C  CA    . LYS B 1 224 ? -18.546 26.259  51.550  1.00 70.24  ?  210 LYS B CA    1 
ATOM   5693 C  C     . LYS B 1 224 ? -17.713 27.291  50.792  1.00 74.81  ?  210 LYS B C     1 
ATOM   5694 O  O     . LYS B 1 224 ? -18.151 28.426  50.579  1.00 78.58  ?  210 LYS B O     1 
ATOM   5695 C  CB    . LYS B 1 224 ? -17.896 25.922  52.896  1.00 73.63  ?  210 LYS B CB    1 
ATOM   5696 C  CG    . LYS B 1 224 ? -18.220 24.528  53.418  1.00 85.90  ?  210 LYS B CG    1 
ATOM   5697 C  CD    . LYS B 1 224 ? -17.016 23.891  54.107  1.00 88.87  ?  210 LYS B CD    1 
ATOM   5698 C  CE    . LYS B 1 224 ? -17.164 22.376  54.210  1.00 77.75  ?  210 LYS B CE    1 
ATOM   5699 N  NZ    . LYS B 1 224 ? -17.221 21.724  52.869  1.00 70.46  ?  210 LYS B NZ    1 
ATOM   5700 N  N     . ARG B 1 225 ? -16.511 26.906  50.369  1.00 58.45  ?  211 ARG B N     1 
ATOM   5701 C  CA    . ARG B 1 225 ? -15.639 27.751  49.564  1.00 72.79  ?  211 ARG B CA    1 
ATOM   5702 C  C     . ARG B 1 225 ? -15.329 27.046  48.252  1.00 62.12  ?  211 ARG B C     1 
ATOM   5703 O  O     . ARG B 1 225 ? -14.862 25.902  48.252  1.00 57.29  ?  211 ARG B O     1 
ATOM   5704 C  CB    . ARG B 1 225 ? -14.337 28.070  50.305  1.00 72.49  ?  211 ARG B CB    1 
ATOM   5705 C  CG    . ARG B 1 225 ? -14.417 29.264  51.243  1.00 74.47  ?  211 ARG B CG    1 
ATOM   5706 C  CD    . ARG B 1 225 ? -13.028 29.705  51.693  1.00 84.14  ?  211 ARG B CD    1 
ATOM   5707 N  NE    . ARG B 1 225 ? -11.985 29.293  50.760  1.00 77.92  ?  211 ARG B NE    1 
ATOM   5708 C  CZ    . ARG B 1 225 ? -11.645 29.966  49.668  1.00 76.51  ?  211 ARG B CZ    1 
ATOM   5709 N  NH1   . ARG B 1 225 ? -12.248 31.097  49.338  1.00 73.28  ?  211 ARG B NH1   1 
ATOM   5710 N  NH2   . ARG B 1 225 ? -10.682 29.486  48.883  1.00 50.93  ?  211 ARG B NH2   1 
ATOM   5711 N  N     . THR B 1 226 ? -15.560 27.741  47.142  1.00 58.88  ?  212 THR B N     1 
ATOM   5712 C  CA    . THR B 1 226 ? -15.357 27.198  45.807  1.00 57.23  ?  212 THR B CA    1 
ATOM   5713 C  C     . THR B 1 226 ? -14.258 27.981  45.102  1.00 52.03  ?  212 THR B C     1 
ATOM   5714 O  O     . THR B 1 226 ? -14.175 29.206  45.236  1.00 56.52  ?  212 THR B O     1 
ATOM   5715 C  CB    . THR B 1 226 ? -16.668 27.249  45.002  1.00 59.39  ?  212 THR B CB    1 
ATOM   5716 O  OG1   . THR B 1 226 ? -17.537 26.203  45.450  1.00 67.81  ?  212 THR B OG1   1 
ATOM   5717 C  CG2   . THR B 1 226 ? -16.417 27.076  43.512  1.00 58.49  ?  212 THR B CG2   1 
ATOM   5718 N  N     . ALA B 1 227 ? -13.409 27.270  44.358  1.00 56.01  ?  213 ALA B N     1 
ATOM   5719 C  CA    . ALA B 1 227 ? -12.329 27.882  43.598  1.00 61.03  ?  213 ALA B CA    1 
ATOM   5720 C  C     . ALA B 1 227 ? -12.361 27.370  42.164  1.00 56.00  ?  213 ALA B C     1 
ATOM   5721 O  O     . ALA B 1 227 ? -12.883 26.288  41.878  1.00 49.24  ?  213 ALA B O     1 
ATOM   5722 C  CB    . ALA B 1 227 ? -10.956 27.601  44.229  1.00 44.20  ?  213 ALA B CB    1 
ATOM   5723 N  N     . LEU B 1 228 ? -11.793 28.165  41.260  1.00 44.46  ?  214 LEU B N     1 
ATOM   5724 C  CA    . LEU B 1 228 ? -11.815 27.882  39.832  1.00 44.75  ?  214 LEU B CA    1 
ATOM   5725 C  C     . LEU B 1 228 ? -10.392 27.737  39.313  1.00 49.34  ?  214 LEU B C     1 
ATOM   5726 O  O     . LEU B 1 228 ? -9.560  28.627  39.509  1.00 51.62  ?  214 LEU B O     1 
ATOM   5727 C  CB    . LEU B 1 228 ? -12.548 28.994  39.076  1.00 51.11  ?  214 LEU B CB    1 
ATOM   5728 C  CG    . LEU B 1 228 ? -12.596 28.945  37.550  1.00 53.75  ?  214 LEU B CG    1 
ATOM   5729 C  CD1   . LEU B 1 228 ? -13.667 27.980  37.086  1.00 43.80  ?  214 LEU B CD1   1 
ATOM   5730 C  CD2   . LEU B 1 228 ? -12.855 30.339  37.002  1.00 65.82  ?  214 LEU B CD2   1 
ATOM   5731 N  N     . LEU B 1 229 ? -10.119 26.624  38.643  1.00 47.76  ?  215 LEU B N     1 
ATOM   5732 C  CA    . LEU B 1 229 ? -8.828  26.381  38.010  1.00 45.66  ?  215 LEU B CA    1 
ATOM   5733 C  C     . LEU B 1 229 ? -9.074  26.078  36.539  1.00 48.26  ?  215 LEU B C     1 
ATOM   5734 O  O     . LEU B 1 229 ? -9.683  25.055  36.207  1.00 47.38  ?  215 LEU B O     1 
ATOM   5735 C  CB    . LEU B 1 229 ? -8.091  25.233  38.694  1.00 39.97  ?  215 LEU B CB    1 
ATOM   5736 C  CG    . LEU B 1 229 ? -6.731  24.858  38.108  1.00 44.73  ?  215 LEU B CG    1 
ATOM   5737 C  CD1   . LEU B 1 229 ? -5.736  25.994  38.294  1.00 40.82  ?  215 LEU B CD1   1 
ATOM   5738 C  CD2   . LEU B 1 229 ? -6.221  23.576  38.749  1.00 54.14  ?  215 LEU B CD2   1 
ATOM   5739 N  N     . ALA B 1 230 ? -8.597  26.957  35.662  1.00 47.19  ?  216 ALA B N     1 
ATOM   5740 C  CA    . ALA B 1 230 ? -8.784  26.812  34.228  1.00 43.58  ?  216 ALA B CA    1 
ATOM   5741 C  C     . ALA B 1 230 ? -7.427  26.679  33.557  1.00 44.91  ?  216 ALA B C     1 
ATOM   5742 O  O     . ALA B 1 230 ? -6.423  27.187  34.062  1.00 49.18  ?  216 ALA B O     1 
ATOM   5743 C  CB    . ALA B 1 230 ? -9.541  28.004  33.644  1.00 39.85  ?  216 ALA B CB    1 
ATOM   5744 N  N     . ASP B 1 231 ? -7.389  25.992  32.422  1.00 44.34  ?  217 ASP B N     1 
ATOM   5745 C  CA    . ASP B 1 231 ? -6.111  25.832  31.738  1.00 41.02  ?  217 ASP B CA    1 
ATOM   5746 C  C     . ASP B 1 231 ? -6.358  25.740  30.235  1.00 41.46  ?  217 ASP B C     1 
ATOM   5747 O  O     . ASP B 1 231 ? -7.430  26.107  29.746  1.00 43.02  ?  217 ASP B O     1 
ATOM   5748 C  CB    . ASP B 1 231 ? -5.337  24.633  32.305  1.00 38.72  ?  217 ASP B CB    1 
ATOM   5749 C  CG    . ASP B 1 231 ? -3.848  24.731  32.022  1.00 53.96  ?  217 ASP B CG    1 
ATOM   5750 O  OD1   . ASP B 1 231 ? -3.140  25.440  32.773  1.00 53.27  ?  217 ASP B OD1   1 
ATOM   5751 O  OD2   . ASP B 1 231 ? -3.383  24.108  31.048  1.00 48.82  ?  217 ASP B OD2   1 
ATOM   5752 N  N     . PHE B 1 232 ? -5.359  25.233  29.507  1.00 33.36  ?  218 PHE B N     1 
ATOM   5753 C  CA    . PHE B 1 232 ? -5.184  25.562  28.096  1.00 38.52  ?  218 PHE B CA    1 
ATOM   5754 C  C     . PHE B 1 232 ? -6.345  25.130  27.214  1.00 31.39  ?  218 PHE B C     1 
ATOM   5755 O  O     . PHE B 1 232 ? -6.518  25.705  26.133  1.00 35.64  ?  218 PHE B O     1 
ATOM   5756 C  CB    . PHE B 1 232 ? -3.874  24.957  27.572  1.00 33.89  ?  218 PHE B CB    1 
ATOM   5757 C  CG    . PHE B 1 232 ? -3.912  23.461  27.387  1.00 32.54  ?  218 PHE B CG    1 
ATOM   5758 C  CD1   . PHE B 1 232 ? -3.819  22.609  28.477  1.00 32.08  ?  218 PHE B CD1   1 
ATOM   5759 C  CD2   . PHE B 1 232 ? -4.010  22.909  26.121  1.00 25.66  ?  218 PHE B CD2   1 
ATOM   5760 C  CE1   . PHE B 1 232 ? -3.847  21.238  28.311  1.00 32.45  ?  218 PHE B CE1   1 
ATOM   5761 C  CE2   . PHE B 1 232 ? -4.036  21.535  25.948  1.00 27.44  ?  218 PHE B CE2   1 
ATOM   5762 C  CZ    . PHE B 1 232 ? -3.956  20.702  27.045  1.00 25.65  ?  218 PHE B CZ    1 
ATOM   5763 N  N     . LEU B 1 233 ? -7.141  24.139  27.627  1.00 35.45  ?  219 LEU B N     1 
ATOM   5764 C  CA    . LEU B 1 233 ? -8.220  23.691  26.751  1.00 31.08  ?  219 LEU B CA    1 
ATOM   5765 C  C     . LEU B 1 233 ? -9.302  24.754  26.591  1.00 33.78  ?  219 LEU B C     1 
ATOM   5766 O  O     . LEU B 1 233 ? -9.941  24.821  25.534  1.00 34.91  ?  219 LEU B O     1 
ATOM   5767 C  CB    . LEU B 1 233 ? -8.807  22.373  27.260  1.00 29.61  ?  219 LEU B CB    1 
ATOM   5768 C  CG    . LEU B 1 233 ? -7.888  21.175  26.960  1.00 38.55  ?  219 LEU B CG    1 
ATOM   5769 C  CD1   . LEU B 1 233 ? -8.267  19.928  27.754  1.00 34.88  ?  219 LEU B CD1   1 
ATOM   5770 C  CD2   . LEU B 1 233 ? -7.855  20.867  25.468  1.00 36.31  ?  219 LEU B CD2   1 
ATOM   5771 N  N     . VAL B 1 234 ? -9.503  25.620  27.591  1.00 36.63  ?  220 VAL B N     1 
ATOM   5772 C  CA    . VAL B 1 234 ? -10.423 26.736  27.382  1.00 36.09  ?  220 VAL B CA    1 
ATOM   5773 C  C     . VAL B 1 234 ? -9.863  27.692  26.333  1.00 29.43  ?  220 VAL B C     1 
ATOM   5774 O  O     . VAL B 1 234 ? -10.616 28.263  25.533  1.00 38.11  ?  220 VAL B O     1 
ATOM   5775 C  CB    . VAL B 1 234 ? -10.781 27.447  28.707  1.00 34.46  ?  220 VAL B CB    1 
ATOM   5776 C  CG1   . VAL B 1 234 ? -10.451 26.589  29.919  1.00 42.06  ?  220 VAL B CG1   1 
ATOM   5777 C  CG2   . VAL B 1 234 ? -10.165 28.827  28.803  1.00 38.96  ?  220 VAL B CG2   1 
ATOM   5778 N  N     . LEU B 1 235 ? -8.539  27.870  26.301  1.00 34.66  ?  221 LEU B N     1 
ATOM   5779 C  CA    . LEU B 1 235 ? -7.932  28.709  25.270  1.00 30.25  ?  221 LEU B CA    1 
ATOM   5780 C  C     . LEU B 1 235 ? -8.176  28.127  23.880  1.00 33.79  ?  221 LEU B C     1 
ATOM   5781 O  O     . LEU B 1 235 ? -8.534  28.850  22.945  1.00 33.68  ?  221 LEU B O     1 
ATOM   5782 C  CB    . LEU B 1 235 ? -6.430  28.867  25.530  1.00 31.30  ?  221 LEU B CB    1 
ATOM   5783 C  CG    . LEU B 1 235 ? -5.947  29.765  26.675  1.00 41.08  ?  221 LEU B CG    1 
ATOM   5784 C  CD1   . LEU B 1 235 ? -4.459  29.560  26.917  1.00 37.31  ?  221 LEU B CD1   1 
ATOM   5785 C  CD2   . LEU B 1 235 ? -6.243  31.243  26.413  1.00 36.78  ?  221 LEU B CD2   1 
ATOM   5786 N  N     . ARG B 1 236 ? -7.974  26.813  23.726  1.00 31.53  ?  222 ARG B N     1 
ATOM   5787 C  CA    . ARG B 1 236 ? -8.101  26.179  22.412  1.00 43.09  ?  222 ARG B CA    1 
ATOM   5788 C  C     . ARG B 1 236 ? -9.540  26.190  21.908  1.00 37.55  ?  222 ARG B C     1 
ATOM   5789 O  O     . ARG B 1 236 ? -9.780  26.299  20.699  1.00 37.66  ?  222 ARG B O     1 
ATOM   5790 C  CB    . ARG B 1 236 ? -7.583  24.742  22.465  1.00 37.62  ?  222 ARG B CB    1 
ATOM   5791 C  CG    . ARG B 1 236 ? -6.232  24.622  23.118  1.00 31.26  ?  222 ARG B CG    1 
ATOM   5792 C  CD    . ARG B 1 236 ? -5.210  25.489  22.414  1.00 26.06  ?  222 ARG B CD    1 
ATOM   5793 N  NE    . ARG B 1 236 ? -3.864  25.020  22.708  1.00 33.42  ?  222 ARG B NE    1 
ATOM   5794 C  CZ    . ARG B 1 236 ? -2.936  25.739  23.318  1.00 35.40  ?  222 ARG B CZ    1 
ATOM   5795 N  NH1   . ARG B 1 236 ? -3.159  26.998  23.669  1.00 32.10  ?  222 ARG B NH1   1 
ATOM   5796 N  NH2   . ARG B 1 236 ? -1.756  25.182  23.584  1.00 38.22  ?  222 ARG B NH2   1 
ATOM   5797 N  N     . HIS B 1 237 ? -10.510 26.047  22.810  1.00 32.01  ?  223 HIS B N     1 
ATOM   5798 C  CA    . HIS B 1 237 ? -11.912 25.971  22.426  1.00 32.77  ?  223 HIS B CA    1 
ATOM   5799 C  C     . HIS B 1 237 ? -12.619 27.324  22.487  1.00 44.35  ?  223 HIS B C     1 
ATOM   5800 O  O     . HIS B 1 237 ? -13.854 27.366  22.544  1.00 45.31  ?  223 HIS B O     1 
ATOM   5801 C  CB    . HIS B 1 237 ? -12.627 24.932  23.293  1.00 35.40  ?  223 HIS B CB    1 
ATOM   5802 C  CG    . HIS B 1 237 ? -12.142 23.533  23.060  1.00 41.23  ?  223 HIS B CG    1 
ATOM   5803 N  ND1   . HIS B 1 237 ? -12.772 22.660  22.200  1.00 36.97  ?  223 HIS B ND1   1 
ATOM   5804 C  CD2   . HIS B 1 237 ? -11.063 22.870  23.543  1.00 41.39  ?  223 HIS B CD2   1 
ATOM   5805 C  CE1   . HIS B 1 237 ? -12.117 21.513  22.179  1.00 36.98  ?  223 HIS B CE1   1 
ATOM   5806 N  NE2   . HIS B 1 237 ? -11.075 21.614  22.985  1.00 40.19  ?  223 HIS B NE2   1 
ATOM   5807 N  N     . GLY B 1 238 ? -11.862 28.422  22.475  1.00 36.76  ?  224 GLY B N     1 
ATOM   5808 C  CA    . GLY B 1 238 ? -12.443 29.748  22.359  1.00 41.01  ?  224 GLY B CA    1 
ATOM   5809 C  C     . GLY B 1 238 ? -13.292 30.173  23.534  1.00 51.70  ?  224 GLY B C     1 
ATOM   5810 O  O     . GLY B 1 238 ? -14.245 30.941  23.357  1.00 46.98  ?  224 GLY B O     1 
ATOM   5811 N  N     . LEU B 1 239 ? -12.974 29.695  24.736  1.00 35.07  ?  225 LEU B N     1 
ATOM   5812 C  CA    . LEU B 1 239 ? -13.777 29.964  25.921  1.00 40.11  ?  225 LEU B CA    1 
ATOM   5813 C  C     . LEU B 1 239 ? -13.106 30.948  26.875  1.00 43.00  ?  225 LEU B C     1 
ATOM   5814 O  O     . LEU B 1 239 ? -13.497 31.033  28.044  1.00 45.47  ?  225 LEU B O     1 
ATOM   5815 C  CB    . LEU B 1 239 ? -14.101 28.652  26.634  1.00 35.41  ?  225 LEU B CB    1 
ATOM   5816 C  CG    . LEU B 1 239 ? -15.073 27.787  25.825  1.00 53.23  ?  225 LEU B CG    1 
ATOM   5817 C  CD1   . LEU B 1 239 ? -15.107 26.354  26.318  1.00 48.12  ?  225 LEU B CD1   1 
ATOM   5818 C  CD2   . LEU B 1 239 ? -16.467 28.404  25.858  1.00 41.65  ?  225 LEU B CD2   1 
ATOM   5819 N  N     . LYS B 1 240 ? -12.108 31.698  26.395  1.00 43.68  ?  226 LYS B N     1 
ATOM   5820 C  CA    . LYS B 1 240 ? -11.411 32.646  27.260  1.00 41.55  ?  226 LYS B CA    1 
ATOM   5821 C  C     . LYS B 1 240 ? -12.362 33.706  27.804  1.00 47.48  ?  226 LYS B C     1 
ATOM   5822 O  O     . LYS B 1 240 ? -12.336 34.020  29.000  1.00 42.08  ?  226 LYS B O     1 
ATOM   5823 C  CB    . LYS B 1 240 ? -10.260 33.299  26.490  1.00 43.87  ?  226 LYS B CB    1 
ATOM   5824 C  CG    . LYS B 1 240 ? -9.285  34.083  27.350  1.00 49.37  ?  226 LYS B CG    1 
ATOM   5825 C  CD    . LYS B 1 240 ? -8.205  34.743  26.498  1.00 49.04  ?  226 LYS B CD    1 
ATOM   5826 C  CE    . LYS B 1 240 ? -7.832  36.116  27.045  1.00 52.51  ?  226 LYS B CE    1 
ATOM   5827 N  NZ    . LYS B 1 240 ? -6.575  36.664  26.440  1.00 53.31  ?  226 LYS B NZ    1 
ATOM   5828 N  N     . HIS B 1 241 ? -13.224 34.255  26.945  1.00 50.42  ?  227 HIS B N     1 
ATOM   5829 C  CA    . HIS B 1 241 ? -14.179 35.260  27.403  1.00 49.40  ?  227 HIS B CA    1 
ATOM   5830 C  C     . HIS B 1 241 ? -15.138 34.683  28.436  1.00 47.98  ?  227 HIS B C     1 
ATOM   5831 O  O     . HIS B 1 241 ? -15.457 35.342  29.433  1.00 51.55  ?  227 HIS B O     1 
ATOM   5832 C  CB    . HIS B 1 241 ? -14.950 35.836  26.214  1.00 54.99  ?  227 HIS B CB    1 
ATOM   5833 C  CG    . HIS B 1 241 ? -15.765 37.046  26.551  1.00 77.72  ?  227 HIS B CG    1 
ATOM   5834 N  ND1   . HIS B 1 241 ? -16.971 36.971  27.215  1.00 79.93  ?  227 HIS B ND1   1 
ATOM   5835 C  CD2   . HIS B 1 241 ? -15.548 38.363  26.314  1.00 82.19  ?  227 HIS B CD2   1 
ATOM   5836 C  CE1   . HIS B 1 241 ? -17.461 38.188  27.374  1.00 76.23  ?  227 HIS B CE1   1 
ATOM   5837 N  NE2   . HIS B 1 241 ? -16.617 39.051  26.836  1.00 73.02  ?  227 HIS B NE2   1 
ATOM   5838 N  N     . ALA B 1 242 ? -15.604 33.450  28.219  1.00 48.39  ?  228 ALA B N     1 
ATOM   5839 C  CA    . ALA B 1 242 ? -16.559 32.846  29.142  1.00 47.02  ?  228 ALA B CA    1 
ATOM   5840 C  C     . ALA B 1 242 ? -15.961 32.679  30.535  1.00 45.04  ?  228 ALA B C     1 
ATOM   5841 O  O     . ALA B 1 242 ? -16.638 32.925  31.539  1.00 46.46  ?  228 ALA B O     1 
ATOM   5842 C  CB    . ALA B 1 242 ? -17.039 31.503  28.597  1.00 43.37  ?  228 ALA B CB    1 
ATOM   5843 N  N     . LEU B 1 243 ? -14.697 32.258  30.617  1.00 45.04  ?  229 LEU B N     1 
ATOM   5844 C  CA    . LEU B 1 243 ? -14.055 32.114  31.921  1.00 37.91  ?  229 LEU B CA    1 
ATOM   5845 C  C     . LEU B 1 243 ? -13.821 33.474  32.571  1.00 42.60  ?  229 LEU B C     1 
ATOM   5846 O  O     . LEU B 1 243 ? -13.936 33.613  33.794  1.00 46.49  ?  229 LEU B O     1 
ATOM   5847 C  CB    . LEU B 1 243 ? -12.739 31.346  31.781  1.00 45.79  ?  229 LEU B CB    1 
ATOM   5848 C  CG    . LEU B 1 243 ? -12.780 29.823  31.990  1.00 46.55  ?  229 LEU B CG    1 
ATOM   5849 C  CD1   . LEU B 1 243 ? -12.809 29.477  33.468  1.00 44.29  ?  229 LEU B CD1   1 
ATOM   5850 C  CD2   . LEU B 1 243 ? -13.967 29.197  31.275  1.00 34.89  ?  229 LEU B CD2   1 
ATOM   5851 N  N     . GLN B 1 244 ? -13.474 34.484  31.771  1.00 44.00  ?  230 GLN B N     1 
ATOM   5852 C  CA    . GLN B 1 244 ? -13.290 35.829  32.310  1.00 51.59  ?  230 GLN B CA    1 
ATOM   5853 C  C     . GLN B 1 244 ? -14.606 36.398  32.827  1.00 53.48  ?  230 GLN B C     1 
ATOM   5854 O  O     . GLN B 1 244 ? -14.672 36.924  33.944  1.00 44.95  ?  230 GLN B O     1 
ATOM   5855 C  CB    . GLN B 1 244 ? -12.685 36.744  31.246  1.00 45.70  ?  230 GLN B CB    1 
ATOM   5856 C  CG    . GLN B 1 244 ? -11.172 36.624  31.123  1.00 62.43  ?  230 GLN B CG    1 
ATOM   5857 C  CD    . GLN B 1 244 ? -10.621 37.348  29.907  1.00 70.91  ?  230 GLN B CD    1 
ATOM   5858 O  OE1   . GLN B 1 244 ? -11.373 37.935  29.126  1.00 59.76  ?  230 GLN B OE1   1 
ATOM   5859 N  NE2   . GLN B 1 244 ? -9.299  37.307  29.739  1.00 51.66  ?  230 GLN B NE2   1 
ATOM   5860 N  N     . LYS B 1 245 ? -15.672 36.293  32.028  1.00 53.79  ?  231 LYS B N     1 
ATOM   5861 C  CA    . LYS B 1 245 ? -16.974 36.769  32.478  1.00 50.36  ?  231 LYS B CA    1 
ATOM   5862 C  C     . LYS B 1 245 ? -17.469 35.975  33.680  1.00 57.93  ?  231 LYS B C     1 
ATOM   5863 O  O     . LYS B 1 245 ? -18.127 36.536  34.564  1.00 54.04  ?  231 LYS B O     1 
ATOM   5864 C  CB    . LYS B 1 245 ? -17.980 36.696  31.326  1.00 54.88  ?  231 LYS B CB    1 
ATOM   5865 C  CG    . LYS B 1 245 ? -19.422 36.944  31.734  1.00 66.09  ?  231 LYS B CG    1 
ATOM   5866 C  CD    . LYS B 1 245 ? -20.217 37.588  30.614  1.00 65.01  ?  231 LYS B CD    1 
ATOM   5867 C  CE    . LYS B 1 245 ? -21.170 38.637  31.160  1.00 72.91  ?  231 LYS B CE    1 
ATOM   5868 N  NZ    . LYS B 1 245 ? -22.395 38.006  31.723  1.00 83.86  ?  231 LYS B NZ    1 
ATOM   5869 N  N     . TRP B 1 246 ? -17.133 34.681  33.744  1.00 53.46  ?  232 TRP B N     1 
ATOM   5870 C  CA    . TRP B 1 246 ? -17.545 33.835  34.863  1.00 53.25  ?  232 TRP B CA    1 
ATOM   5871 C  C     . TRP B 1 246 ? -17.061 34.401  36.193  1.00 55.48  ?  232 TRP B C     1 
ATOM   5872 O  O     . TRP B 1 246 ? -17.836 34.529  37.147  1.00 60.26  ?  232 TRP B O     1 
ATOM   5873 C  CB    . TRP B 1 246 ? -17.011 32.417  34.653  1.00 50.63  ?  232 TRP B CB    1 
ATOM   5874 C  CG    . TRP B 1 246 ? -17.463 31.372  35.649  1.00 48.28  ?  232 TRP B CG    1 
ATOM   5875 C  CD1   . TRP B 1 246 ? -18.159 31.570  36.810  1.00 45.24  ?  232 TRP B CD1   1 
ATOM   5876 C  CD2   . TRP B 1 246 ? -17.226 29.960  35.562  1.00 44.07  ?  232 TRP B CD2   1 
ATOM   5877 N  NE1   . TRP B 1 246 ? -18.375 30.367  37.443  1.00 46.83  ?  232 TRP B NE1   1 
ATOM   5878 C  CE2   . TRP B 1 246 ? -17.810 29.366  36.698  1.00 44.92  ?  232 TRP B CE2   1 
ATOM   5879 C  CE3   . TRP B 1 246 ? -16.577 29.141  34.632  1.00 46.14  ?  232 TRP B CE3   1 
ATOM   5880 C  CZ2   . TRP B 1 246 ? -17.763 27.994  36.927  1.00 54.13  ?  232 TRP B CZ2   1 
ATOM   5881 C  CZ3   . TRP B 1 246 ? -16.533 27.777  34.862  1.00 38.54  ?  232 TRP B CZ3   1 
ATOM   5882 C  CH2   . TRP B 1 246 ? -17.120 27.218  36.001  1.00 49.98  ?  232 TRP B CH2   1 
ATOM   5883 N  N     . VAL B 1 247 ? -15.775 34.743  36.278  1.00 51.80  ?  233 VAL B N     1 
ATOM   5884 C  CA    . VAL B 1 247 ? -15.226 35.206  37.547  1.00 62.13  ?  233 VAL B CA    1 
ATOM   5885 C  C     . VAL B 1 247 ? -15.621 36.650  37.856  1.00 60.89  ?  233 VAL B C     1 
ATOM   5886 O  O     . VAL B 1 247 ? -15.587 37.057  39.023  1.00 72.34  ?  233 VAL B O     1 
ATOM   5887 C  CB    . VAL B 1 247 ? -13.698 35.018  37.544  1.00 65.29  ?  233 VAL B CB    1 
ATOM   5888 C  CG1   . VAL B 1 247 ? -13.049 35.850  36.454  1.00 51.29  ?  233 VAL B CG1   1 
ATOM   5889 C  CG2   . VAL B 1 247 ? -13.096 35.333  38.909  1.00 78.98  ?  233 VAL B CG2   1 
ATOM   5890 N  N     . LYS B 1 248 ? -16.015 37.444  36.856  1.00 59.18  ?  234 LYS B N     1 
ATOM   5891 C  CA    . LYS B 1 248 ? -16.588 38.755  37.162  1.00 66.62  ?  234 LYS B CA    1 
ATOM   5892 C  C     . LYS B 1 248 ? -17.976 38.614  37.785  1.00 61.82  ?  234 LYS B C     1 
ATOM   5893 O  O     . LYS B 1 248 ? -18.263 39.213  38.830  1.00 62.45  ?  234 LYS B O     1 
ATOM   5894 C  CB    . LYS B 1 248 ? -16.660 39.636  35.910  1.00 56.88  ?  234 LYS B CB    1 
ATOM   5895 C  CG    . LYS B 1 248 ? -17.945 40.471  35.901  1.00 84.08  ?  234 LYS B CG    1 
ATOM   5896 C  CD    . LYS B 1 248 ? -18.057 41.511  34.790  1.00 83.53  ?  234 LYS B CD    1 
ATOM   5897 C  CE    . LYS B 1 248 ? -19.486 42.059  34.788  1.00 83.75  ?  234 LYS B CE    1 
ATOM   5898 N  NZ    . LYS B 1 248 ? -19.508 43.551  34.841  1.00 81.10  ?  234 LYS B NZ    1 
ATOM   5899 N  N     . ASP B 1 249 ? -18.839 37.792  37.175  1.00 62.78  ?  235 ASP B N     1 
ATOM   5900 C  CA    . ASP B 1 249 ? -20.192 37.633  37.684  1.00 58.90  ?  235 ASP B CA    1 
ATOM   5901 C  C     . ASP B 1 249 ? -20.220 36.846  38.984  1.00 63.24  ?  235 ASP B C     1 
ATOM   5902 O  O     . ASP B 1 249 ? -21.147 37.022  39.782  1.00 72.97  ?  235 ASP B O     1 
ATOM   5903 C  CB    . ASP B 1 249 ? -21.079 36.944  36.637  1.00 70.95  ?  235 ASP B CB    1 
ATOM   5904 C  CG    . ASP B 1 249 ? -21.095 37.670  35.297  1.00 68.72  ?  235 ASP B CG    1 
ATOM   5905 O  OD1   . ASP B 1 249 ? -20.661 38.841  35.252  1.00 77.68  ?  235 ASP B OD1   1 
ATOM   5906 O  OD2   . ASP B 1 249 ? -21.550 37.076  34.295  1.00 73.56  ?  235 ASP B OD2   1 
ATOM   5907 N  N     . VAL B 1 250 ? -19.218 36.004  39.219  1.00 61.50  ?  236 VAL B N     1 
ATOM   5908 C  CA    . VAL B 1 250 ? -19.130 35.188  40.426  1.00 64.81  ?  236 VAL B CA    1 
ATOM   5909 C  C     . VAL B 1 250 ? -17.701 35.263  40.951  1.00 65.68  ?  236 VAL B C     1 
ATOM   5910 O  O     . VAL B 1 250 ? -16.882 34.387  40.637  1.00 64.10  ?  236 VAL B O     1 
ATOM   5911 C  CB    . VAL B 1 250 ? -19.536 33.729  40.169  1.00 59.46  ?  236 VAL B CB    1 
ATOM   5912 C  CG1   . VAL B 1 250 ? -19.720 33.007  41.487  1.00 60.76  ?  236 VAL B CG1   1 
ATOM   5913 C  CG2   . VAL B 1 250 ? -20.807 33.649  39.338  1.00 73.50  ?  236 VAL B CG2   1 
ATOM   5914 N  N     . PRO B 1 251 ? -17.350 36.288  41.722  1.00 74.17  ?  237 PRO B N     1 
ATOM   5915 C  CA    . PRO B 1 251 ? -15.972 36.399  42.217  1.00 62.88  ?  237 PRO B CA    1 
ATOM   5916 C  C     . PRO B 1 251 ? -15.613 35.234  43.130  1.00 67.37  ?  237 PRO B C     1 
ATOM   5917 O  O     . PRO B 1 251 ? -16.331 34.920  44.082  1.00 71.47  ?  237 PRO B O     1 
ATOM   5918 C  CB    . PRO B 1 251 ? -15.972 37.734  42.971  1.00 57.24  ?  237 PRO B CB    1 
ATOM   5919 C  CG    . PRO B 1 251 ? -17.133 38.493  42.405  1.00 66.83  ?  237 PRO B CG    1 
ATOM   5920 C  CD    . PRO B 1 251 ? -18.168 37.456  42.090  1.00 61.78  ?  237 PRO B CD    1 
ATOM   5921 N  N     . MET B 1 252 ? -14.493 34.585  42.821  1.00 72.17  ?  238 MET B N     1 
ATOM   5922 C  CA    . MET B 1 252 ? -13.955 33.517  43.652  1.00 66.51  ?  238 MET B CA    1 
ATOM   5923 C  C     . MET B 1 252 ? -12.466 33.410  43.375  1.00 60.10  ?  238 MET B C     1 
ATOM   5924 O  O     . MET B 1 252 ? -11.971 33.913  42.364  1.00 61.91  ?  238 MET B O     1 
ATOM   5925 C  CB    . MET B 1 252 ? -14.651 32.176  43.385  1.00 57.38  ?  238 MET B CB    1 
ATOM   5926 C  CG    . MET B 1 252 ? -14.488 31.652  41.961  1.00 62.88  ?  238 MET B CG    1 
ATOM   5927 S  SD    . MET B 1 252 ? -15.744 30.430  41.492  1.00 67.06  ?  238 MET B SD    1 
ATOM   5928 C  CE    . MET B 1 252 ? -16.133 30.963  39.826  1.00 64.28  ?  238 MET B CE    1 
ATOM   5929 N  N     . ALA B 1 253 ? -11.757 32.751  44.288  1.00 62.66  ?  239 ALA B N     1 
ATOM   5930 C  CA    . ALA B 1 253 ? -10.344 32.475  44.066  1.00 55.82  ?  239 ALA B CA    1 
ATOM   5931 C  C     . ALA B 1 253 ? -10.172 31.655  42.796  1.00 50.62  ?  239 ALA B C     1 
ATOM   5932 O  O     . ALA B 1 253 ? -10.836 30.633  42.608  1.00 50.99  ?  239 ALA B O     1 
ATOM   5933 C  CB    . ALA B 1 253 ? -9.749  31.736  45.264  1.00 47.36  ?  239 ALA B CB    1 
ATOM   5934 N  N     . HIS B 1 254 ? -9.279  32.109  41.919  1.00 52.10  ?  240 HIS B N     1 
ATOM   5935 C  CA    . HIS B 1 254 ? -9.092  31.456  40.633  1.00 42.96  ?  240 HIS B CA    1 
ATOM   5936 C  C     . HIS B 1 254 ? -7.627  31.522  40.230  1.00 57.27  ?  240 HIS B C     1 
ATOM   5937 O  O     . HIS B 1 254 ? -6.902  32.449  40.605  1.00 49.13  ?  240 HIS B O     1 
ATOM   5938 C  CB    . HIS B 1 254 ? -9.974  32.081  39.542  1.00 49.14  ?  240 HIS B CB    1 
ATOM   5939 C  CG    . HIS B 1 254 ? -9.749  33.549  39.341  1.00 56.17  ?  240 HIS B CG    1 
ATOM   5940 N  ND1   . HIS B 1 254 ? -10.085 34.493  40.288  1.00 51.40  ?  240 HIS B ND1   1 
ATOM   5941 C  CD2   . HIS B 1 254 ? -9.229  34.236  38.295  1.00 46.86  ?  240 HIS B CD2   1 
ATOM   5942 C  CE1   . HIS B 1 254 ? -9.780  35.696  39.836  1.00 56.64  ?  240 HIS B CE1   1 
ATOM   5943 N  NE2   . HIS B 1 254 ? -9.259  35.568  38.629  1.00 55.43  ?  240 HIS B NE2   1 
ATOM   5944 N  N     . ALA B 1 255 ? -7.207  30.528  39.448  1.00 43.30  ?  241 ALA B N     1 
ATOM   5945 C  CA    . ALA B 1 255 ? -5.840  30.450  38.962  1.00 48.59  ?  241 ALA B CA    1 
ATOM   5946 C  C     . ALA B 1 255 ? -5.828  29.670  37.658  1.00 49.83  ?  241 ALA B C     1 
ATOM   5947 O  O     . ALA B 1 255 ? -6.851  29.141  37.216  1.00 40.55  ?  241 ALA B O     1 
ATOM   5948 C  CB    . ALA B 1 255 ? -4.912  29.787  39.988  1.00 37.94  ?  241 ALA B CB    1 
ATOM   5949 N  N     . THR B 1 256 ? -4.655  29.629  37.031  1.00 37.27  ?  242 THR B N     1 
ATOM   5950 C  CA    . THR B 1 256 ? -4.370  28.708  35.941  1.00 36.33  ?  242 THR B CA    1 
ATOM   5951 C  C     . THR B 1 256 ? -3.110  27.931  36.293  1.00 35.10  ?  242 THR B C     1 
ATOM   5952 O  O     . THR B 1 256 ? -2.477  28.167  37.326  1.00 40.12  ?  242 THR B O     1 
ATOM   5953 C  CB    . THR B 1 256 ? -4.191  29.428  34.597  1.00 36.05  ?  242 THR B CB    1 
ATOM   5954 O  OG1   . THR B 1 256 ? -2.853  29.933  34.495  1.00 40.57  ?  242 THR B OG1   1 
ATOM   5955 C  CG2   . THR B 1 256 ? -5.177  30.575  34.453  1.00 42.67  ?  242 THR B CG2   1 
ATOM   5956 N  N     . MET B 1 257 ? -2.766  26.976  35.445  1.00 40.16  ?  243 MET B N     1 
ATOM   5957 C  CA    . MET B 1 257 ? -1.446  26.374  35.466  1.00 41.57  ?  243 MET B CA    1 
ATOM   5958 C  C     . MET B 1 257 ? -0.619  27.027  34.357  1.00 41.82  ?  243 MET B C     1 
ATOM   5959 O  O     . MET B 1 257 ? -1.052  27.996  33.722  1.00 43.86  ?  243 MET B O     1 
ATOM   5960 C  CB    . MET B 1 257 ? -1.561  24.854  35.342  1.00 30.60  ?  243 MET B CB    1 
ATOM   5961 C  CG    . MET B 1 257 ? -2.535  24.249  36.340  1.00 40.66  ?  243 MET B CG    1 
ATOM   5962 S  SD    . MET B 1 257 ? -2.425  22.455  36.514  1.00 45.04  ?  243 MET B SD    1 
ATOM   5963 C  CE    . MET B 1 257 ? -3.771  21.952  35.446  1.00 36.36  ?  243 MET B CE    1 
ATOM   5964 N  N     . LEU B 1 258 ? 0.586   26.504  34.116  1.00 47.58  ?  244 LEU B N     1 
ATOM   5965 C  CA    . LEU B 1 258 ? 1.495   27.162  33.179  1.00 41.72  ?  244 LEU B CA    1 
ATOM   5966 C  C     . LEU B 1 258 ? 0.916   27.201  31.769  1.00 39.37  ?  244 LEU B C     1 
ATOM   5967 O  O     . LEU B 1 258 ? 0.998   28.228  31.084  1.00 36.09  ?  244 LEU B O     1 
ATOM   5968 C  CB    . LEU B 1 258 ? 2.850   26.456  33.184  1.00 33.74  ?  244 LEU B CB    1 
ATOM   5969 C  CG    . LEU B 1 258 ? 3.909   26.972  32.209  1.00 42.70  ?  244 LEU B CG    1 
ATOM   5970 C  CD1   . LEU B 1 258 ? 4.188   28.448  32.452  1.00 29.68  ?  244 LEU B CD1   1 
ATOM   5971 C  CD2   . LEU B 1 258 ? 5.185   26.148  32.336  1.00 28.55  ?  244 LEU B CD2   1 
ATOM   5972 N  N     . MET B 1 259 ? 0.311   26.096  31.327  1.00 36.23  ?  245 MET B N     1 
ATOM   5973 C  CA    . MET B 1 259 ? -0.184  26.011  29.956  1.00 39.13  ?  245 MET B CA    1 
ATOM   5974 C  C     . MET B 1 259 ? -1.282  27.031  29.686  1.00 42.71  ?  245 MET B C     1 
ATOM   5975 O  O     . MET B 1 259 ? -1.349  27.610  28.595  1.00 48.13  ?  245 MET B O     1 
ATOM   5976 C  CB    . MET B 1 259 ? -0.699  24.603  29.673  1.00 46.73  ?  245 MET B CB    1 
ATOM   5977 C  CG    . MET B 1 259 ? 0.289   23.738  28.969  1.00 34.65  ?  245 MET B CG    1 
ATOM   5978 S  SD    . MET B 1 259 ? -0.156  22.005  28.905  1.00 46.14  ?  245 MET B SD    1 
ATOM   5979 C  CE    . MET B 1 259 ? -0.491  21.846  27.156  1.00 36.44  ?  245 MET B CE    1 
ATOM   5980 N  N     . GLY B 1 260 ? -2.168  27.239  30.650  1.00 36.73  ?  246 GLY B N     1 
ATOM   5981 C  CA    . GLY B 1 260 ? -3.290  28.129  30.473  1.00 38.99  ?  246 GLY B CA    1 
ATOM   5982 C  C     . GLY B 1 260 ? -3.067  29.552  30.922  1.00 41.90  ?  246 GLY B C     1 
ATOM   5983 O  O     . GLY B 1 260 ? -4.036  30.312  30.994  1.00 45.27  ?  246 GLY B O     1 
ATOM   5984 N  N     . LYS B 1 261 ? -1.829  29.940  31.230  1.00 51.20  ?  247 LYS B N     1 
ATOM   5985 C  CA    . LYS B 1 261 ? -1.554  31.322  31.603  1.00 41.74  ?  247 LYS B CA    1 
ATOM   5986 C  C     . LYS B 1 261 ? -1.988  32.263  30.486  1.00 36.54  ?  247 LYS B C     1 
ATOM   5987 O  O     . LYS B 1 261 ? -1.736  32.010  29.304  1.00 37.33  ?  247 LYS B O     1 
ATOM   5988 C  CB    . LYS B 1 261 ? -0.064  31.502  31.909  1.00 41.78  ?  247 LYS B CB    1 
ATOM   5989 C  CG    . LYS B 1 261 ? 0.284   31.540  33.396  1.00 40.52  ?  247 LYS B CG    1 
ATOM   5990 C  CD    . LYS B 1 261 ? 1.685   32.110  33.622  1.00 39.94  ?  247 LYS B CD    1 
ATOM   5991 C  CE    . LYS B 1 261 ? 1.664   33.572  34.064  1.00 40.45  ?  247 LYS B CE    1 
ATOM   5992 N  NZ    . LYS B 1 261 ? 1.715   33.734  35.547  1.00 40.71  ?  247 LYS B NZ    1 
ATOM   5993 N  N     . GLY B 1 262 ? -2.673  33.335  30.864  1.00 37.76  ?  248 GLY B N     1 
ATOM   5994 C  CA    . GLY B 1 262 ? -3.232  34.281  29.920  1.00 46.30  ?  248 GLY B CA    1 
ATOM   5995 C  C     . GLY B 1 262 ? -4.742  34.257  29.840  1.00 45.21  ?  248 GLY B C     1 
ATOM   5996 O  O     . GLY B 1 262 ? -5.326  35.158  29.225  1.00 40.14  ?  248 GLY B O     1 
ATOM   5997 N  N     . ILE B 1 263 ? -5.394  33.258  30.440  1.00 42.36  ?  249 ILE B N     1 
ATOM   5998 C  CA    . ILE B 1 263 ? -6.853  33.231  30.458  1.00 44.05  ?  249 ILE B CA    1 
ATOM   5999 C  C     . ILE B 1 263 ? -7.398  34.393  31.282  1.00 48.36  ?  249 ILE B C     1 
ATOM   6000 O  O     . ILE B 1 263 ? -8.369  35.053  30.890  1.00 44.56  ?  249 ILE B O     1 
ATOM   6001 C  CB    . ILE B 1 263 ? -7.353  31.876  30.996  1.00 43.33  ?  249 ILE B CB    1 
ATOM   6002 C  CG1   . ILE B 1 263 ? -7.051  30.750  30.004  1.00 35.46  ?  249 ILE B CG1   1 
ATOM   6003 C  CG2   . ILE B 1 263 ? -8.849  31.933  31.310  1.00 36.17  ?  249 ILE B CG2   1 
ATOM   6004 C  CD1   . ILE B 1 263 ? -7.115  29.372  30.620  1.00 31.08  ?  249 ILE B CD1   1 
ATOM   6005 N  N     . PHE B 1 264 ? -6.778  34.673  32.424  1.00 45.34  ?  250 PHE B N     1 
ATOM   6006 C  CA    . PHE B 1 264 ? -7.280  35.662  33.363  1.00 40.71  ?  250 PHE B CA    1 
ATOM   6007 C  C     . PHE B 1 264 ? -6.366  36.879  33.413  1.00 50.37  ?  250 PHE B C     1 
ATOM   6008 O  O     . PHE B 1 264 ? -5.142  36.770  33.283  1.00 45.70  ?  250 PHE B O     1 
ATOM   6009 C  CB    . PHE B 1 264 ? -7.401  35.076  34.776  1.00 46.51  ?  250 PHE B CB    1 
ATOM   6010 C  CG    . PHE B 1 264 ? -8.342  33.900  34.882  1.00 47.19  ?  250 PHE B CG    1 
ATOM   6011 C  CD1   . PHE B 1 264 ? -9.692  34.037  34.602  1.00 48.54  ?  250 PHE B CD1   1 
ATOM   6012 C  CD2   . PHE B 1 264 ? -7.870  32.659  35.282  1.00 42.80  ?  250 PHE B CD2   1 
ATOM   6013 C  CE1   . PHE B 1 264 ? -10.556 32.950  34.712  1.00 42.53  ?  250 PHE B CE1   1 
ATOM   6014 C  CE2   . PHE B 1 264 ? -8.725  31.572  35.393  1.00 45.90  ?  250 PHE B CE2   1 
ATOM   6015 C  CZ    . PHE B 1 264 ? -10.069 31.720  35.109  1.00 41.54  ?  250 PHE B CZ    1 
ATOM   6016 N  N     . ASP B 1 265 ? -6.980  38.046  33.602  1.00 45.24  ?  251 ASP B N     1 
ATOM   6017 C  CA    . ASP B 1 265 ? -6.227  39.224  34.002  1.00 42.89  ?  251 ASP B CA    1 
ATOM   6018 C  C     . ASP B 1 265 ? -5.663  38.957  35.388  1.00 44.96  ?  251 ASP B C     1 
ATOM   6019 O  O     . ASP B 1 265 ? -6.417  38.871  36.361  1.00 49.82  ?  251 ASP B O     1 
ATOM   6020 C  CB    . ASP B 1 265 ? -7.122  40.466  33.998  1.00 48.64  ?  251 ASP B CB    1 
ATOM   6021 C  CG    . ASP B 1 265 ? -6.353  41.759  34.262  1.00 58.14  ?  251 ASP B CG    1 
ATOM   6022 O  OD1   . ASP B 1 265 ? -5.326  41.739  34.977  1.00 60.53  ?  251 ASP B OD1   1 
ATOM   6023 O  OD2   . ASP B 1 265 ? -6.793  42.812  33.757  1.00 60.59  ?  251 ASP B OD2   1 
ATOM   6024 N  N     . GLU B 1 266 ? -4.344  38.840  35.496  1.00 42.42  ?  252 GLU B N     1 
ATOM   6025 C  CA    . GLU B 1 266 ? -3.735  38.411  36.747  1.00 47.92  ?  252 GLU B CA    1 
ATOM   6026 C  C     . GLU B 1 266 ? -3.657  39.529  37.777  1.00 45.45  ?  252 GLU B C     1 
ATOM   6027 O  O     . GLU B 1 266 ? -3.255  39.274  38.916  1.00 59.46  ?  252 GLU B O     1 
ATOM   6028 C  CB    . GLU B 1 266 ? -2.348  37.825  36.468  1.00 53.88  ?  252 GLU B CB    1 
ATOM   6029 C  CG    . GLU B 1 266 ? -2.338  36.857  35.277  1.00 53.10  ?  252 GLU B CG    1 
ATOM   6030 C  CD    . GLU B 1 266 ? -1.336  35.723  35.432  1.00 53.71  ?  252 GLU B CD    1 
ATOM   6031 O  OE1   . GLU B 1 266 ? -0.380  35.874  36.226  1.00 61.38  ?  252 GLU B OE1   1 
ATOM   6032 O  OE2   . GLU B 1 266 ? -1.500  34.683  34.755  1.00 48.43  ?  252 GLU B OE2   1 
ATOM   6033 N  N     . ARG B 1 267 ? -4.038  40.752  37.409  1.00 52.47  ?  253 ARG B N     1 
ATOM   6034 C  CA    . ARG B 1 267 ? -4.176  41.836  38.372  1.00 55.38  ?  253 ARG B CA    1 
ATOM   6035 C  C     . ARG B 1 267 ? -5.528  41.826  39.071  1.00 52.40  ?  253 ARG B C     1 
ATOM   6036 O  O     . ARG B 1 267 ? -5.697  42.532  40.069  1.00 67.60  ?  253 ARG B O     1 
ATOM   6037 C  CB    . ARG B 1 267 ? -3.977  43.186  37.679  1.00 50.04  ?  253 ARG B CB    1 
ATOM   6038 C  CG    . ARG B 1 267 ? -2.628  43.364  37.008  1.00 49.26  ?  253 ARG B CG    1 
ATOM   6039 C  CD    . ARG B 1 267 ? -2.690  44.466  35.959  1.00 56.20  ?  253 ARG B CD    1 
ATOM   6040 N  NE    . ARG B 1 267 ? -3.832  44.306  35.065  1.00 54.64  ?  253 ARG B NE    1 
ATOM   6041 C  CZ    . ARG B 1 267 ? -4.141  45.143  34.082  1.00 57.08  ?  253 ARG B CZ    1 
ATOM   6042 N  NH1   . ARG B 1 267 ? -3.430  46.236  33.853  1.00 52.40  ?  253 ARG B NH1   1 
ATOM   6043 N  NH2   . ARG B 1 267 ? -5.190  44.876  33.310  1.00 56.60  ?  253 ARG B NH2   1 
ATOM   6044 N  N     . HIS B 1 268 ? -6.482  41.046  38.569  1.00 57.46  ?  254 HIS B N     1 
ATOM   6045 C  CA    . HIS B 1 268 ? -7.847  41.058  39.077  1.00 59.89  ?  254 HIS B CA    1 
ATOM   6046 C  C     . HIS B 1 268 ? -7.929  40.463  40.479  1.00 62.26  ?  254 HIS B C     1 
ATOM   6047 O  O     . HIS B 1 268 ? -7.115  39.626  40.876  1.00 67.67  ?  254 HIS B O     1 
ATOM   6048 C  CB    . HIS B 1 268 ? -8.756  40.275  38.131  1.00 59.98  ?  254 HIS B CB    1 
ATOM   6049 C  CG    . HIS B 1 268 ? -10.202 40.645  38.228  1.00 69.99  ?  254 HIS B CG    1 
ATOM   6050 N  ND1   . HIS B 1 268 ? -10.749 41.699  37.528  1.00 88.51  ?  254 HIS B ND1   1 
ATOM   6051 C  CD2   . HIS B 1 268 ? -11.220 40.090  38.928  1.00 81.07  ?  254 HIS B CD2   1 
ATOM   6052 C  CE1   . HIS B 1 268 ? -12.039 41.785  37.803  1.00 92.25  ?  254 HIS B CE1   1 
ATOM   6053 N  NE2   . HIS B 1 268 ? -12.350 40.820  38.650  1.00 87.90  ?  254 HIS B NE2   1 
ATOM   6054 N  N     . VAL B 1 269 ? -8.943  40.904  41.227  1.00 66.04  ?  255 VAL B N     1 
ATOM   6055 C  CA    . VAL B 1 269 ? -9.181  40.367  42.559  1.00 60.59  ?  255 VAL B CA    1 
ATOM   6056 C  C     . VAL B 1 269 ? -9.543  38.889  42.456  1.00 61.88  ?  255 VAL B C     1 
ATOM   6057 O  O     . VAL B 1 269 ? -10.250 38.462  41.533  1.00 55.49  ?  255 VAL B O     1 
ATOM   6058 C  CB    . VAL B 1 269 ? -10.283 41.176  43.264  1.00 78.68  ?  255 VAL B CB    1 
ATOM   6059 C  CG1   . VAL B 1 269 ? -11.551 41.212  42.415  1.00 72.68  ?  255 VAL B CG1   1 
ATOM   6060 C  CG2   . VAL B 1 269 ? -10.564 40.626  44.653  1.00 83.58  ?  255 VAL B CG2   1 
ATOM   6061 N  N     . GLY B 1 270 ? -9.041  38.094  43.398  1.00 54.06  ?  256 GLY B N     1 
ATOM   6062 C  CA    . GLY B 1 270 ? -9.250  36.664  43.390  1.00 52.96  ?  256 GLY B CA    1 
ATOM   6063 C  C     . GLY B 1 270 ? -8.139  35.866  42.740  1.00 64.20  ?  256 GLY B C     1 
ATOM   6064 O  O     . GLY B 1 270 ? -8.163  34.630  42.812  1.00 59.94  ?  256 GLY B O     1 
ATOM   6065 N  N     . PHE B 1 271 ? -7.180  36.527  42.099  1.00 47.87  ?  257 PHE B N     1 
ATOM   6066 C  CA    . PHE B 1 271 ? -6.029  35.859  41.508  1.00 56.73  ?  257 PHE B CA    1 
ATOM   6067 C  C     . PHE B 1 271 ? -4.822  36.060  42.415  1.00 63.56  ?  257 PHE B C     1 
ATOM   6068 O  O     . PHE B 1 271 ? -4.500  37.195  42.786  1.00 61.76  ?  257 PHE B O     1 
ATOM   6069 C  CB    . PHE B 1 271 ? -5.746  36.394  40.103  1.00 47.49  ?  257 PHE B CB    1 
ATOM   6070 C  CG    . PHE B 1 271 ? -4.695  35.620  39.361  1.00 55.87  ?  257 PHE B CG    1 
ATOM   6071 C  CD1   . PHE B 1 271 ? -3.354  35.943  39.494  1.00 57.06  ?  257 PHE B CD1   1 
ATOM   6072 C  CD2   . PHE B 1 271 ? -5.044  34.573  38.529  1.00 51.54  ?  257 PHE B CD2   1 
ATOM   6073 C  CE1   . PHE B 1 271 ? -2.388  35.231  38.814  1.00 60.33  ?  257 PHE B CE1   1 
ATOM   6074 C  CE2   . PHE B 1 271 ? -4.079  33.859  37.849  1.00 54.57  ?  257 PHE B CE2   1 
ATOM   6075 C  CZ    . PHE B 1 271 ? -2.750  34.188  37.994  1.00 51.21  ?  257 PHE B CZ    1 
ATOM   6076 N  N     . TYR B 1 272 ? -4.157  34.958  42.770  1.00 54.49  ?  258 TYR B N     1 
ATOM   6077 C  CA    . TYR B 1 272 ? -3.023  35.001  43.682  1.00 47.76  ?  258 TYR B CA    1 
ATOM   6078 C  C     . TYR B 1 272 ? -1.732  34.488  43.062  1.00 46.98  ?  258 TYR B C     1 
ATOM   6079 O  O     . TYR B 1 272 ? -0.697  34.493  43.737  1.00 50.92  ?  258 TYR B O     1 
ATOM   6080 C  CB    . TYR B 1 272 ? -3.331  34.201  44.957  1.00 51.32  ?  258 TYR B CB    1 
ATOM   6081 C  CG    . TYR B 1 272 ? -4.605  34.627  45.660  1.00 58.85  ?  258 TYR B CG    1 
ATOM   6082 C  CD1   . TYR B 1 272 ? -5.849  34.194  45.214  1.00 56.32  ?  258 TYR B CD1   1 
ATOM   6083 C  CD2   . TYR B 1 272 ? -4.564  35.472  46.764  1.00 60.43  ?  258 TYR B CD2   1 
ATOM   6084 C  CE1   . TYR B 1 272 ? -7.012  34.585  45.848  1.00 65.33  ?  258 TYR B CE1   1 
ATOM   6085 C  CE2   . TYR B 1 272 ? -5.724  35.868  47.406  1.00 60.45  ?  258 TYR B CE2   1 
ATOM   6086 C  CZ    . TYR B 1 272 ? -6.945  35.421  46.943  1.00 67.07  ?  258 TYR B CZ    1 
ATOM   6087 O  OH    . TYR B 1 272 ? -8.104  35.807  47.573  1.00 79.21  ?  258 TYR B OH    1 
ATOM   6088 N  N     . GLY B 1 273 ? -1.760  34.053  41.810  1.00 49.22  ?  259 GLY B N     1 
ATOM   6089 C  CA    . GLY B 1 273 ? -0.603  33.487  41.145  1.00 41.30  ?  259 GLY B CA    1 
ATOM   6090 C  C     . GLY B 1 273 ? -0.945  32.179  40.454  1.00 53.40  ?  259 GLY B C     1 
ATOM   6091 O  O     . GLY B 1 273 ? -1.979  31.565  40.685  1.00 51.65  ?  259 GLY B O     1 
ATOM   6092 N  N     . THR B 1 274 ? -0.026  31.772  39.580  1.00 46.44  ?  260 THR B N     1 
ATOM   6093 C  CA    . THR B 1 274 ? -0.217  30.536  38.834  1.00 48.88  ?  260 THR B CA    1 
ATOM   6094 C  C     . THR B 1 274 ? -0.074  29.333  39.758  1.00 48.36  ?  260 THR B C     1 
ATOM   6095 O  O     . THR B 1 274 ? 0.741   29.333  40.685  1.00 50.43  ?  260 THR B O     1 
ATOM   6096 C  CB    . THR B 1 274 ? 0.780   30.456  37.677  1.00 38.57  ?  260 THR B CB    1 
ATOM   6097 O  OG1   . THR B 1 274 ? 0.646   31.623  36.858  1.00 40.51  ?  260 THR B OG1   1 
ATOM   6098 C  CG2   . THR B 1 274 ? 0.522   29.229  36.817  1.00 36.22  ?  260 THR B CG2   1 
ATOM   6099 N  N     . TYR B 1 275 ? -0.889  28.310  39.510  1.00 45.72  ?  261 TYR B N     1 
ATOM   6100 C  CA    . TYR B 1 275 ? -0.874  27.088  40.301  1.00 36.92  ?  261 TYR B CA    1 
ATOM   6101 C  C     . TYR B 1 275 ? 0.098   26.093  39.678  1.00 47.74  ?  261 TYR B C     1 
ATOM   6102 O  O     . TYR B 1 275 ? 0.022   25.808  38.478  1.00 42.80  ?  261 TYR B O     1 
ATOM   6103 C  CB    . TYR B 1 275 ? -2.281  26.494  40.381  1.00 38.64  ?  261 TYR B CB    1 
ATOM   6104 C  CG    . TYR B 1 275 ? -2.372  25.186  41.134  1.00 46.62  ?  261 TYR B CG    1 
ATOM   6105 C  CD1   . TYR B 1 275 ? -2.149  25.134  42.505  1.00 46.75  ?  261 TYR B CD1   1 
ATOM   6106 C  CD2   . TYR B 1 275 ? -2.693  24.007  40.475  1.00 34.78  ?  261 TYR B CD2   1 
ATOM   6107 C  CE1   . TYR B 1 275 ? -2.235  23.941  43.197  1.00 49.38  ?  261 TYR B CE1   1 
ATOM   6108 C  CE2   . TYR B 1 275 ? -2.783  22.808  41.157  1.00 42.53  ?  261 TYR B CE2   1 
ATOM   6109 C  CZ    . TYR B 1 275 ? -2.553  22.779  42.517  1.00 55.43  ?  261 TYR B CZ    1 
ATOM   6110 O  OH    . TYR B 1 275 ? -2.641  21.588  43.203  1.00 42.22  ?  261 TYR B OH    1 
ATOM   6111 N  N     . SER B 1 276 ? 1.027   25.587  40.489  1.00 42.17  ?  262 SER B N     1 
ATOM   6112 C  CA    . SER B 1 276 ? 2.023   24.626  40.027  1.00 46.99  ?  262 SER B CA    1 
ATOM   6113 C  C     . SER B 1 276 ? 2.233   23.528  41.064  1.00 56.77  ?  262 SER B C     1 
ATOM   6114 O  O     . SER B 1 276 ? 3.368   23.150  41.375  1.00 41.84  ?  262 SER B O     1 
ATOM   6115 C  CB    . SER B 1 276 ? 3.342   25.319  39.689  1.00 50.73  ?  262 SER B CB    1 
ATOM   6116 O  OG    . SER B 1 276 ? 4.033   25.699  40.867  1.00 65.31  ?  262 SER B OG    1 
ATOM   6117 N  N     . GLY B 1 277 ? 1.136   23.010  41.620  1.00 45.91  ?  263 GLY B N     1 
ATOM   6118 C  CA    . GLY B 1 277 ? 1.237   21.961  42.625  1.00 39.33  ?  263 GLY B CA    1 
ATOM   6119 C  C     . GLY B 1 277 ? 1.918   22.461  43.885  1.00 51.83  ?  263 GLY B C     1 
ATOM   6120 O  O     . GLY B 1 277 ? 1.702   23.593  44.334  1.00 55.93  ?  263 GLY B O     1 
ATOM   6121 N  N     . SER B 1 278 ? 2.777   21.614  44.456  1.00 53.06  ?  264 SER B N     1 
ATOM   6122 C  CA    . SER B 1 278 ? 3.497   21.974  45.671  1.00 52.56  ?  264 SER B CA    1 
ATOM   6123 C  C     . SER B 1 278 ? 4.500   23.101  45.458  1.00 59.61  ?  264 SER B C     1 
ATOM   6124 O  O     . SER B 1 278 ? 4.994   23.657  46.445  1.00 62.62  ?  264 SER B O     1 
ATOM   6125 C  CB    . SER B 1 278 ? 4.207   20.750  46.243  1.00 55.64  ?  264 SER B CB    1 
ATOM   6126 O  OG    . SER B 1 278 ? 5.576   20.749  45.880  1.00 72.28  ?  264 SER B OG    1 
ATOM   6127 N  N     . ALA B 1 279 ? 4.824   23.439  44.210  1.00 62.62  ?  265 ALA B N     1 
ATOM   6128 C  CA    . ALA B 1 279 ? 5.698   24.570  43.917  1.00 56.80  ?  265 ALA B CA    1 
ATOM   6129 C  C     . ALA B 1 279 ? 4.953   25.897  43.877  1.00 58.52  ?  265 ALA B C     1 
ATOM   6130 O  O     . ALA B 1 279 ? 5.583   26.936  43.653  1.00 67.84  ?  265 ALA B O     1 
ATOM   6131 C  CB    . ALA B 1 279 ? 6.420   24.356  42.586  1.00 48.10  ?  265 ALA B CB    1 
ATOM   6132 N  N     . SER B 1 280 ? 3.638   25.889  44.076  1.00 56.50  ?  266 SER B N     1 
ATOM   6133 C  CA    . SER B 1 280 ? 2.864   27.119  44.037  1.00 56.74  ?  266 SER B CA    1 
ATOM   6134 C  C     . SER B 1 280 ? 3.208   27.999  45.235  1.00 57.30  ?  266 SER B C     1 
ATOM   6135 O  O     . SER B 1 280 ? 3.701   27.531  46.266  1.00 59.41  ?  266 SER B O     1 
ATOM   6136 C  CB    . SER B 1 280 ? 1.361   26.816  44.031  1.00 54.90  ?  266 SER B CB    1 
ATOM   6137 O  OG    . SER B 1 280 ? 0.995   25.960  42.957  1.00 50.21  ?  266 SER B OG    1 
ATOM   6138 N  N     . ALA B 1 281 ? 2.958   29.296  45.079  1.00 42.99  ?  267 ALA B N     1 
ATOM   6139 C  CA    . ALA B 1 281 ? 3.041   30.204  46.213  1.00 45.50  ?  267 ALA B CA    1 
ATOM   6140 C  C     . ALA B 1 281 ? 2.050   29.789  47.293  1.00 57.99  ?  267 ALA B C     1 
ATOM   6141 O  O     . ALA B 1 281 ? 0.996   29.211  47.013  1.00 62.50  ?  267 ALA B O     1 
ATOM   6142 C  CB    . ALA B 1 281 ? 2.766   31.639  45.769  1.00 51.81  ?  267 ALA B CB    1 
ATOM   6143 N  N     . GLY B 1 282 ? 2.403   30.090  48.544  1.00 53.93  ?  268 GLY B N     1 
ATOM   6144 C  CA    . GLY B 1 282 ? 1.560   29.693  49.662  1.00 49.94  ?  268 GLY B CA    1 
ATOM   6145 C  C     . GLY B 1 282 ? 0.138   30.208  49.546  1.00 66.04  ?  268 GLY B C     1 
ATOM   6146 O  O     . GLY B 1 282 ? -0.816  29.497  49.870  1.00 72.03  ?  268 GLY B O     1 
ATOM   6147 N  N     . ALA B 1 283 ? -0.023  31.453  49.090  1.00 67.53  ?  269 ALA B N     1 
ATOM   6148 C  CA    . ALA B 1 283 ? -1.364  31.997  48.900  1.00 56.51  ?  269 ALA B CA    1 
ATOM   6149 C  C     . ALA B 1 283 ? -2.127  31.221  47.833  1.00 55.03  ?  269 ALA B C     1 
ATOM   6150 O  O     . ALA B 1 283 ? -3.336  30.999  47.965  1.00 64.85  ?  269 ALA B O     1 
ATOM   6151 C  CB    . ALA B 1 283 ? -1.286  33.478  48.531  1.00 51.12  ?  269 ALA B CB    1 
ATOM   6152 N  N     . VAL B 1 284 ? -1.441  30.808  46.765  1.00 49.24  ?  270 VAL B N     1 
ATOM   6153 C  CA    . VAL B 1 284 ? -2.091  30.036  45.709  1.00 47.52  ?  270 VAL B CA    1 
ATOM   6154 C  C     . VAL B 1 284 ? -2.514  28.668  46.227  1.00 55.71  ?  270 VAL B C     1 
ATOM   6155 O  O     . VAL B 1 284 ? -3.632  28.210  45.968  1.00 62.53  ?  270 VAL B O     1 
ATOM   6156 C  CB    . VAL B 1 284 ? -1.166  29.902  44.487  1.00 58.45  ?  270 VAL B CB    1 
ATOM   6157 C  CG1   . VAL B 1 284 ? -1.865  29.110  43.386  1.00 54.44  ?  270 VAL B CG1   1 
ATOM   6158 C  CG2   . VAL B 1 284 ? -0.742  31.270  43.989  1.00 58.06  ?  270 VAL B CG2   1 
ATOM   6159 N  N     . LYS B 1 285 ? -1.623  27.996  46.965  1.00 60.84  ?  271 LYS B N     1 
ATOM   6160 C  CA    . LYS B 1 285 ? -1.954  26.689  47.524  1.00 53.03  ?  271 LYS B CA    1 
ATOM   6161 C  C     . LYS B 1 285 ? -3.204  26.763  48.388  1.00 57.89  ?  271 LYS B C     1 
ATOM   6162 O  O     . LYS B 1 285 ? -4.085  25.902  48.293  1.00 69.52  ?  271 LYS B O     1 
ATOM   6163 C  CB    . LYS B 1 285 ? -0.779  26.151  48.341  1.00 49.68  ?  271 LYS B CB    1 
ATOM   6164 C  CG    . LYS B 1 285 ? 0.438   25.773  47.517  1.00 63.95  ?  271 LYS B CG    1 
ATOM   6165 C  CD    . LYS B 1 285 ? 1.212   24.635  48.164  1.00 61.09  ?  271 LYS B CD    1 
ATOM   6166 C  CE    . LYS B 1 285 ? 2.678   24.999  48.349  1.00 68.33  ?  271 LYS B CE    1 
ATOM   6167 N  NZ    . LYS B 1 285 ? 3.497   23.827  48.763  1.00 67.32  ?  271 LYS B NZ    1 
ATOM   6168 N  N     . GLU B 1 286 ? -3.302  27.790  49.232  1.00 56.17  ?  272 GLU B N     1 
ATOM   6169 C  CA    . GLU B 1 286 ? -4.483  27.935  50.074  1.00 67.70  ?  272 GLU B CA    1 
ATOM   6170 C  C     . GLU B 1 286 ? -5.701  28.334  49.250  1.00 71.44  ?  272 GLU B C     1 
ATOM   6171 O  O     . GLU B 1 286 ? -6.824  27.905  49.544  1.00 69.65  ?  272 GLU B O     1 
ATOM   6172 C  CB    . GLU B 1 286 ? -4.221  28.955  51.182  1.00 65.02  ?  272 GLU B CB    1 
ATOM   6173 C  CG    . GLU B 1 286 ? -4.246  28.365  52.590  1.00 83.48  ?  272 GLU B CG    1 
ATOM   6174 C  CD    . GLU B 1 286 ? -5.604  27.791  52.976  1.00 94.51  ?  272 GLU B CD    1 
ATOM   6175 O  OE1   . GLU B 1 286 ? -6.631  28.248  52.429  1.00 101.16 ?  272 GLU B OE1   1 
ATOM   6176 O  OE2   . GLU B 1 286 ? -5.643  26.880  53.831  1.00 89.79  ?  272 GLU B OE2   1 
ATOM   6177 N  N     . ALA B 1 287 ? -5.502  29.167  48.224  1.00 58.54  ?  273 ALA B N     1 
ATOM   6178 C  CA    . ALA B 1 287 ? -6.625  29.617  47.407  1.00 55.02  ?  273 ALA B CA    1 
ATOM   6179 C  C     . ALA B 1 287 ? -7.280  28.452  46.674  1.00 60.69  ?  273 ALA B C     1 
ATOM   6180 O  O     . ALA B 1 287 ? -8.510  28.315  46.674  1.00 57.57  ?  273 ALA B O     1 
ATOM   6181 C  CB    . ALA B 1 287 ? -6.155  30.681  46.415  1.00 50.89  ?  273 ALA B CB    1 
ATOM   6182 N  N     . ILE B 1 288 ? -6.472  27.585  46.066  1.00 52.40  ?  274 ILE B N     1 
ATOM   6183 C  CA    . ILE B 1 288 ? -6.988  26.511  45.226  1.00 49.63  ?  274 ILE B CA    1 
ATOM   6184 C  C     . ILE B 1 288 ? -7.139  25.227  46.031  1.00 64.27  ?  274 ILE B C     1 
ATOM   6185 O  O     . ILE B 1 288 ? -8.256  24.728  46.220  1.00 52.57  ?  274 ILE B O     1 
ATOM   6186 C  CB    . ILE B 1 288 ? -6.077  26.293  44.004  1.00 45.76  ?  274 ILE B CB    1 
ATOM   6187 C  CG1   . ILE B 1 288 ? -5.728  27.635  43.366  1.00 46.80  ?  274 ILE B CG1   1 
ATOM   6188 C  CG2   . ILE B 1 288 ? -6.737  25.373  42.991  1.00 52.73  ?  274 ILE B CG2   1 
ATOM   6189 C  CD1   . ILE B 1 288 ? -6.906  28.298  42.694  1.00 52.78  ?  274 ILE B CD1   1 
ATOM   6190 N  N     . GLU B 1 289 ? -6.022  24.693  46.531  1.00 58.84  ?  275 GLU B N     1 
ATOM   6191 C  CA    . GLU B 1 289 ? -6.067  23.418  47.237  1.00 49.45  ?  275 GLU B CA    1 
ATOM   6192 C  C     . GLU B 1 289 ? -6.789  23.519  48.572  1.00 61.24  ?  275 GLU B C     1 
ATOM   6193 O  O     . GLU B 1 289 ? -7.251  22.497  49.089  1.00 58.98  ?  275 GLU B O     1 
ATOM   6194 C  CB    . GLU B 1 289 ? -4.652  22.881  47.453  1.00 45.42  ?  275 GLU B CB    1 
ATOM   6195 C  CG    . GLU B 1 289 ? -4.067  22.183  46.237  1.00 48.64  ?  275 GLU B CG    1 
ATOM   6196 C  CD    . GLU B 1 289 ? -2.599  21.851  46.404  1.00 56.39  ?  275 GLU B CD    1 
ATOM   6197 O  OE1   . GLU B 1 289 ? -2.089  21.967  47.539  1.00 60.10  ?  275 GLU B OE1   1 
ATOM   6198 O  OE2   . GLU B 1 289 ? -1.958  21.471  45.399  1.00 54.10  ?  275 GLU B OE2   1 
ATOM   6199 N  N     . GLY B 1 290 ? -6.901  24.722  49.140  1.00 60.20  ?  276 GLY B N     1 
ATOM   6200 C  CA    . GLY B 1 290 ? -7.602  24.882  50.401  1.00 58.29  ?  276 GLY B CA    1 
ATOM   6201 C  C     . GLY B 1 290 ? -9.105  24.972  50.277  1.00 54.49  ?  276 GLY B C     1 
ATOM   6202 O  O     . GLY B 1 290 ? -9.804  24.845  51.286  1.00 63.90  ?  276 GLY B O     1 
ATOM   6203 N  N     . ALA B 1 291 ? -9.615  25.200  49.070  1.00 54.17  ?  277 ALA B N     1 
ATOM   6204 C  CA    . ALA B 1 291 ? -11.053 25.221  48.853  1.00 62.91  ?  277 ALA B CA    1 
ATOM   6205 C  C     . ALA B 1 291 ? -11.624 23.810  48.936  1.00 61.36  ?  277 ALA B C     1 
ATOM   6206 O  O     . ALA B 1 291 ? -10.969 22.830  48.573  1.00 58.07  ?  277 ALA B O     1 
ATOM   6207 C  CB    . ALA B 1 291 ? -11.379 25.841  47.495  1.00 53.89  ?  277 ALA B CB    1 
ATOM   6208 N  N     . ASP B 1 292 ? -12.865 23.708  49.422  1.00 54.91  ?  278 ASP B N     1 
ATOM   6209 C  CA    . ASP B 1 292 ? -13.512 22.403  49.494  1.00 56.86  ?  278 ASP B CA    1 
ATOM   6210 C  C     . ASP B 1 292 ? -14.078 21.954  48.154  1.00 59.18  ?  278 ASP B C     1 
ATOM   6211 O  O     . ASP B 1 292 ? -14.368 20.765  47.986  1.00 58.19  ?  278 ASP B O     1 
ATOM   6212 C  CB    . ASP B 1 292 ? -14.624 22.406  50.547  1.00 65.32  ?  278 ASP B CB    1 
ATOM   6213 C  CG    . ASP B 1 292 ? -15.547 23.602  50.424  1.00 72.58  ?  278 ASP B CG    1 
ATOM   6214 O  OD1   . ASP B 1 292 ? -16.336 23.653  49.455  1.00 65.68  ?  278 ASP B OD1   1 
ATOM   6215 O  OD2   . ASP B 1 292 ? -15.485 24.487  51.303  1.00 72.76  ?  278 ASP B OD2   1 
ATOM   6216 N  N     . THR B 1 293 ? -14.241 22.870  47.202  1.00 56.80  ?  279 THR B N     1 
ATOM   6217 C  CA    . THR B 1 293 ? -14.685 22.525  45.856  1.00 53.08  ?  279 THR B CA    1 
ATOM   6218 C  C     . THR B 1 293 ? -13.846 23.310  44.863  1.00 54.18  ?  279 THR B C     1 
ATOM   6219 O  O     . THR B 1 293 ? -13.774 24.541  44.945  1.00 50.57  ?  279 THR B O     1 
ATOM   6220 C  CB    . THR B 1 293 ? -16.177 22.824  45.660  1.00 64.91  ?  279 THR B CB    1 
ATOM   6221 O  OG1   . THR B 1 293 ? -16.933 22.193  46.701  1.00 60.80  ?  279 THR B OG1   1 
ATOM   6222 C  CG2   . THR B 1 293 ? -16.657 22.300  44.311  1.00 48.99  ?  279 THR B CG2   1 
ATOM   6223 N  N     . VAL B 1 294 ? -13.202 22.603  43.940  1.00 51.25  ?  280 VAL B N     1 
ATOM   6224 C  CA    . VAL B 1 294 ? -12.380 23.215  42.904  1.00 44.81  ?  280 VAL B CA    1 
ATOM   6225 C  C     . VAL B 1 294 ? -12.973 22.839  41.555  1.00 46.69  ?  280 VAL B C     1 
ATOM   6226 O  O     . VAL B 1 294 ? -13.133 21.651  41.248  1.00 44.59  ?  280 VAL B O     1 
ATOM   6227 C  CB    . VAL B 1 294 ? -10.909 22.778  42.999  1.00 42.22  ?  280 VAL B CB    1 
ATOM   6228 C  CG1   . VAL B 1 294 ? -10.075 23.517  41.968  1.00 37.97  ?  280 VAL B CG1   1 
ATOM   6229 C  CG2   . VAL B 1 294 ? -10.369 23.022  44.400  1.00 49.00  ?  280 VAL B CG2   1 
ATOM   6230 N  N     . LEU B 1 295 ? -13.300 23.848  40.754  1.00 51.82  ?  281 LEU B N     1 
ATOM   6231 C  CA    . LEU B 1 295 ? -13.794 23.639  39.398  1.00 42.94  ?  281 LEU B CA    1 
ATOM   6232 C  C     . LEU B 1 295 ? -12.598 23.628  38.448  1.00 55.78  ?  281 LEU B C     1 
ATOM   6233 O  O     . LEU B 1 295 ? -11.932 24.653  38.260  1.00 44.58  ?  281 LEU B O     1 
ATOM   6234 C  CB    . LEU B 1 295 ? -14.806 24.721  39.028  1.00 42.05  ?  281 LEU B CB    1 
ATOM   6235 C  CG    . LEU B 1 295 ? -15.970 24.886  40.020  1.00 51.70  ?  281 LEU B CG    1 
ATOM   6236 C  CD1   . LEU B 1 295 ? -17.021 25.847  39.491  1.00 48.71  ?  281 LEU B CD1   1 
ATOM   6237 C  CD2   . LEU B 1 295 ? -16.611 23.544  40.365  1.00 41.33  ?  281 LEU B CD2   1 
ATOM   6238 N  N     . CYS B 1 296 ? -12.317 22.462  37.862  1.00 46.15  ?  282 CYS B N     1 
ATOM   6239 C  CA    . CYS B 1 296 ? -11.199 22.284  36.942  1.00 41.61  ?  282 CYS B CA    1 
ATOM   6240 C  C     . CYS B 1 296 ? -11.737 22.321  35.518  1.00 37.71  ?  282 CYS B C     1 
ATOM   6241 O  O     . CYS B 1 296 ? -12.434 21.397  35.088  1.00 39.61  ?  282 CYS B O     1 
ATOM   6242 C  CB    . CYS B 1 296 ? -10.472 20.972  37.225  1.00 40.03  ?  282 CYS B CB    1 
ATOM   6243 S  SG    . CYS B 1 296 ? -9.819  20.853  38.903  1.00 48.25  ?  282 CYS B SG    1 
ATOM   6244 N  N     . ILE B 1 297 ? -11.424 23.392  34.794  1.00 35.27  ?  283 ILE B N     1 
ATOM   6245 C  CA    . ILE B 1 297 ? -11.966 23.635  33.463  1.00 32.67  ?  283 ILE B CA    1 
ATOM   6246 C  C     . ILE B 1 297 ? -10.834 23.489  32.458  1.00 39.53  ?  283 ILE B C     1 
ATOM   6247 O  O     . ILE B 1 297 ? -9.931  24.334  32.395  1.00 37.94  ?  283 ILE B O     1 
ATOM   6248 C  CB    . ILE B 1 297 ? -12.621 25.018  33.357  1.00 32.34  ?  283 ILE B CB    1 
ATOM   6249 C  CG1   . ILE B 1 297 ? -13.495 25.294  34.585  1.00 40.14  ?  283 ILE B CG1   1 
ATOM   6250 C  CG2   . ILE B 1 297 ? -13.431 25.121  32.077  1.00 34.14  ?  283 ILE B CG2   1 
ATOM   6251 C  CD1   . ILE B 1 297 ? -14.665 24.335  34.730  1.00 37.92  ?  283 ILE B CD1   1 
ATOM   6252 N  N     . GLY B 1 298 ? -10.899 22.434  31.652  1.00 35.49  ?  284 GLY B N     1 
ATOM   6253 C  CA    . GLY B 1 298 ? -9.910  22.205  30.611  1.00 36.96  ?  284 GLY B CA    1 
ATOM   6254 C  C     . GLY B 1 298 ? -8.504  21.979  31.121  1.00 35.91  ?  284 GLY B C     1 
ATOM   6255 O  O     . GLY B 1 298 ? -7.541  22.452  30.506  1.00 43.76  ?  284 GLY B O     1 
ATOM   6256 N  N     . THR B 1 299 ? -8.359  21.228  32.204  1.00 35.84  ?  285 THR B N     1 
ATOM   6257 C  CA    . THR B 1 299 ? -7.080  21.049  32.873  1.00 38.86  ?  285 THR B CA    1 
ATOM   6258 C  C     . THR B 1 299 ? -6.471  19.701  32.515  1.00 46.54  ?  285 THR B C     1 
ATOM   6259 O  O     . THR B 1 299 ? -7.186  18.707  32.349  1.00 41.19  ?  285 THR B O     1 
ATOM   6260 C  CB    . THR B 1 299 ? -7.248  21.140  34.390  1.00 46.51  ?  285 THR B CB    1 
ATOM   6261 O  OG1   . THR B 1 299 ? -8.349  20.314  34.793  1.00 48.50  ?  285 THR B OG1   1 
ATOM   6262 C  CG2   . THR B 1 299 ? -7.525  22.580  34.809  1.00 35.78  ?  285 THR B CG2   1 
ATOM   6263 N  N     . ARG B 1 300 ? -5.144  19.685  32.376  1.00 40.76  ?  286 ARG B N     1 
ATOM   6264 C  CA    . ARG B 1 300 ? -4.360  18.461  32.232  1.00 30.68  ?  286 ARG B CA    1 
ATOM   6265 C  C     . ARG B 1 300 ? -3.184  18.558  33.192  1.00 40.37  ?  286 ARG B C     1 
ATOM   6266 O  O     . ARG B 1 300 ? -2.332  19.441  33.044  1.00 33.95  ?  286 ARG B O     1 
ATOM   6267 C  CB    . ARG B 1 300 ? -3.860  18.270  30.796  1.00 31.33  ?  286 ARG B CB    1 
ATOM   6268 C  CG    . ARG B 1 300 ? -4.946  18.016  29.764  1.00 39.59  ?  286 ARG B CG    1 
ATOM   6269 C  CD    . ARG B 1 300 ? -5.822  16.845  30.152  1.00 37.34  ?  286 ARG B CD    1 
ATOM   6270 N  NE    . ARG B 1 300 ? -7.101  16.862  29.452  1.00 35.37  ?  286 ARG B NE    1 
ATOM   6271 C  CZ    . ARG B 1 300 ? -7.293  16.390  28.227  1.00 39.05  ?  286 ARG B CZ    1 
ATOM   6272 N  NH1   . ARG B 1 300 ? -6.302  15.867  27.524  1.00 27.96  ?  286 ARG B NH1   1 
ATOM   6273 N  NH2   . ARG B 1 300 ? -8.514  16.431  27.699  1.00 31.86  ?  286 ARG B NH2   1 
ATOM   6274 N  N     . PHE B 1 301 ? -3.144  17.665  34.181  1.00 37.57  ?  287 PHE B N     1 
ATOM   6275 C  CA    . PHE B 1 301 ? -2.144  17.740  35.247  1.00 40.58  ?  287 PHE B CA    1 
ATOM   6276 C  C     . PHE B 1 301 ? -0.882  16.993  34.813  1.00 47.23  ?  287 PHE B C     1 
ATOM   6277 O  O     . PHE B 1 301 ? -0.644  15.833  35.165  1.00 43.17  ?  287 PHE B O     1 
ATOM   6278 C  CB    . PHE B 1 301 ? -2.717  17.195  36.548  1.00 43.00  ?  287 PHE B CB    1 
ATOM   6279 C  CG    . PHE B 1 301 ? -3.878  17.990  37.073  1.00 51.13  ?  287 PHE B CG    1 
ATOM   6280 C  CD1   . PHE B 1 301 ? -3.667  19.110  37.867  1.00 45.09  ?  287 PHE B CD1   1 
ATOM   6281 C  CD2   . PHE B 1 301 ? -5.182  17.627  36.763  1.00 44.56  ?  287 PHE B CD2   1 
ATOM   6282 C  CE1   . PHE B 1 301 ? -4.736  19.850  38.349  1.00 43.28  ?  287 PHE B CE1   1 
ATOM   6283 C  CE2   . PHE B 1 301 ? -6.255  18.363  37.241  1.00 46.90  ?  287 PHE B CE2   1 
ATOM   6284 C  CZ    . PHE B 1 301 ? -6.032  19.477  38.034  1.00 40.42  ?  287 PHE B CZ    1 
ATOM   6285 N  N     . THR B 1 302 ? -0.067  17.678  34.016  1.00 34.80  ?  288 THR B N     1 
ATOM   6286 C  CA    . THR B 1 302 ? 1.191   17.112  33.554  1.00 43.31  ?  288 THR B CA    1 
ATOM   6287 C  C     . THR B 1 302 ? 2.271   17.250  34.628  1.00 40.50  ?  288 THR B C     1 
ATOM   6288 O  O     . THR B 1 302 ? 2.116   17.972  35.619  1.00 39.83  ?  288 THR B O     1 
ATOM   6289 C  CB    . THR B 1 302 ? 1.650   17.792  32.267  1.00 44.10  ?  288 THR B CB    1 
ATOM   6290 O  OG1   . THR B 1 302 ? 2.363   18.987  32.602  1.00 40.80  ?  288 THR B OG1   1 
ATOM   6291 C  CG2   . THR B 1 302 ? 0.457   18.143  31.381  1.00 29.79  ?  288 THR B CG2   1 
ATOM   6292 N  N     . ASP B 1 303 ? 3.392   16.554  34.409  1.00 38.09  ?  289 ASP B N     1 
ATOM   6293 C  CA    . ASP B 1 303 ? 4.460   16.544  35.407  1.00 34.20  ?  289 ASP B CA    1 
ATOM   6294 C  C     . ASP B 1 303 ? 5.033   17.939  35.625  1.00 35.23  ?  289 ASP B C     1 
ATOM   6295 O  O     . ASP B 1 303 ? 5.270   18.347  36.768  1.00 41.67  ?  289 ASP B O     1 
ATOM   6296 C  CB    . ASP B 1 303 ? 5.565   15.565  35.000  1.00 33.69  ?  289 ASP B CB    1 
ATOM   6297 C  CG    . ASP B 1 303 ? 6.135   15.853  33.620  1.00 43.21  ?  289 ASP B CG    1 
ATOM   6298 O  OD1   . ASP B 1 303 ? 5.594   16.720  32.898  1.00 46.16  ?  289 ASP B OD1   1 
ATOM   6299 O  OD2   . ASP B 1 303 ? 7.134   15.203  33.257  1.00 43.09  ?  289 ASP B OD2   1 
ATOM   6300 N  N     . THR B 1 304 ? 5.260   18.686  34.541  1.00 36.58  ?  290 THR B N     1 
ATOM   6301 C  CA    . THR B 1 304 ? 5.802   20.037  34.664  1.00 43.65  ?  290 THR B CA    1 
ATOM   6302 C  C     . THR B 1 304 ? 4.797   20.981  35.313  1.00 49.57  ?  290 THR B C     1 
ATOM   6303 O  O     . THR B 1 304 ? 5.161   21.793  36.173  1.00 44.96  ?  290 THR B O     1 
ATOM   6304 C  CB    . THR B 1 304 ? 6.206   20.563  33.288  1.00 48.11  ?  290 THR B CB    1 
ATOM   6305 O  OG1   . THR B 1 304 ? 7.283   19.773  32.773  1.00 47.21  ?  290 THR B OG1   1 
ATOM   6306 C  CG2   . THR B 1 304 ? 6.637   22.025  33.376  1.00 51.08  ?  290 THR B CG2   1 
ATOM   6307 N  N     . LEU B 1 305 ? 3.529   20.891  34.905  1.00 44.80  ?  291 LEU B N     1 
ATOM   6308 C  CA    . LEU B 1 305 ? 2.506   21.790  35.427  1.00 41.54  ?  291 LEU B CA    1 
ATOM   6309 C  C     . LEU B 1 305 ? 2.270   21.573  36.916  1.00 47.43  ?  291 LEU B C     1 
ATOM   6310 O  O     . LEU B 1 305 ? 1.879   22.510  37.621  1.00 50.72  ?  291 LEU B O     1 
ATOM   6311 C  CB    . LEU B 1 305 ? 1.202   21.601  34.650  1.00 38.25  ?  291 LEU B CB    1 
ATOM   6312 C  CG    . LEU B 1 305 ? 0.932   22.570  33.496  1.00 47.63  ?  291 LEU B CG    1 
ATOM   6313 C  CD1   . LEU B 1 305 ? 2.166   22.740  32.621  1.00 39.29  ?  291 LEU B CD1   1 
ATOM   6314 C  CD2   . LEU B 1 305 ? -0.256  22.105  32.662  1.00 43.29  ?  291 LEU B CD2   1 
ATOM   6315 N  N     . THR B 1 306 ? 2.509   20.360  37.414  1.00 45.18  ?  292 THR B N     1 
ATOM   6316 C  CA    . THR B 1 306 ? 2.252   20.021  38.809  1.00 49.23  ?  292 THR B CA    1 
ATOM   6317 C  C     . THR B 1 306 ? 3.531   19.846  39.615  1.00 50.42  ?  292 THR B C     1 
ATOM   6318 O  O     . THR B 1 306 ? 3.471   19.363  40.751  1.00 46.71  ?  292 THR B O     1 
ATOM   6319 C  CB    . THR B 1 306 ? 1.422   18.742  38.897  1.00 43.11  ?  292 THR B CB    1 
ATOM   6320 O  OG1   . THR B 1 306 ? 2.070   17.713  38.141  1.00 43.75  ?  292 THR B OG1   1 
ATOM   6321 C  CG2   . THR B 1 306 ? 0.026   18.967  38.344  1.00 44.26  ?  292 THR B CG2   1 
ATOM   6322 N  N     . ALA B 1 307 ? 4.678   20.235  39.059  1.00 48.23  ?  293 ALA B N     1 
ATOM   6323 C  CA    . ALA B 1 307 ? 5.978   20.097  39.716  1.00 56.48  ?  293 ALA B CA    1 
ATOM   6324 C  C     . ALA B 1 307 ? 6.189   18.676  40.241  1.00 57.58  ?  293 ALA B C     1 
ATOM   6325 O  O     . ALA B 1 307 ? 6.512   18.457  41.410  1.00 61.02  ?  293 ALA B O     1 
ATOM   6326 C  CB    . ALA B 1 307 ? 6.140   21.130  40.833  1.00 58.31  ?  293 ALA B CB    1 
ATOM   6327 N  N     . GLY B 1 308 ? 5.994   17.698  39.356  1.00 51.26  ?  294 GLY B N     1 
ATOM   6328 C  CA    . GLY B 1 308 ? 6.217   16.310  39.708  1.00 37.48  ?  294 GLY B CA    1 
ATOM   6329 C  C     . GLY B 1 308 ? 5.011   15.624  40.315  1.00 48.91  ?  294 GLY B C     1 
ATOM   6330 O  O     . GLY B 1 308 ? 5.154   14.794  41.217  1.00 53.89  ?  294 GLY B O     1 
ATOM   6331 N  N     . PHE B 1 309 ? 3.818   15.972  39.828  1.00 51.09  ?  295 PHE B N     1 
ATOM   6332 C  CA    . PHE B 1 309 ? 2.561   15.385  40.298  1.00 44.14  ?  295 PHE B CA    1 
ATOM   6333 C  C     . PHE B 1 309 ? 2.400   15.553  41.807  1.00 52.44  ?  295 PHE B C     1 
ATOM   6334 O  O     . PHE B 1 309 ? 1.898   14.667  42.501  1.00 52.96  ?  295 PHE B O     1 
ATOM   6335 C  CB    . PHE B 1 309 ? 2.453   13.911  39.896  1.00 41.60  ?  295 PHE B CB    1 
ATOM   6336 C  CG    . PHE B 1 309 ? 2.632   13.669  38.422  1.00 39.53  ?  295 PHE B CG    1 
ATOM   6337 C  CD1   . PHE B 1 309 ? 1.734   14.189  37.507  1.00 41.50  ?  295 PHE B CD1   1 
ATOM   6338 C  CD2   . PHE B 1 309 ? 3.706   12.925  37.953  1.00 49.70  ?  295 PHE B CD2   1 
ATOM   6339 C  CE1   . PHE B 1 309 ? 1.899   13.971  36.152  1.00 42.57  ?  295 PHE B CE1   1 
ATOM   6340 C  CE2   . PHE B 1 309 ? 3.877   12.704  36.598  1.00 36.52  ?  295 PHE B CE2   1 
ATOM   6341 C  CZ    . PHE B 1 309 ? 2.971   13.227  35.697  1.00 41.16  ?  295 PHE B CZ    1 
ATOM   6342 N  N     . THR B 1 310 ? 2.814   16.710  42.320  1.00 48.10  ?  296 THR B N     1 
ATOM   6343 C  CA    . THR B 1 310 ? 2.688   17.018  43.737  1.00 53.10  ?  296 THR B CA    1 
ATOM   6344 C  C     . THR B 1 310 ? 1.443   17.845  44.040  1.00 55.97  ?  296 THR B C     1 
ATOM   6345 O  O     . THR B 1 310 ? 1.307   18.364  45.153  1.00 50.57  ?  296 THR B O     1 
ATOM   6346 C  CB    . THR B 1 310 ? 3.940   17.743  44.237  1.00 47.96  ?  296 THR B CB    1 
ATOM   6347 O  OG1   . THR B 1 310 ? 4.057   19.011  43.578  1.00 52.62  ?  296 THR B OG1   1 
ATOM   6348 C  CG2   . THR B 1 310 ? 5.183   16.911  43.950  1.00 46.63  ?  296 THR B CG2   1 
ATOM   6349 N  N     . HIS B 1 311 ? 0.533   17.971  43.077  1.00 47.07  ?  297 HIS B N     1 
ATOM   6350 C  CA    . HIS B 1 311 ? -0.741  18.631  43.321  1.00 51.59  ?  297 HIS B CA    1 
ATOM   6351 C  C     . HIS B 1 311 ? -1.587  17.803  44.278  1.00 59.23  ?  297 HIS B C     1 
ATOM   6352 O  O     . HIS B 1 311 ? -1.557  16.570  44.251  1.00 60.90  ?  297 HIS B O     1 
ATOM   6353 C  CB    . HIS B 1 311 ? -1.492  18.844  42.008  1.00 41.50  ?  297 HIS B CB    1 
ATOM   6354 C  CG    . HIS B 1 311 ? -1.810  17.575  41.278  1.00 53.27  ?  297 HIS B CG    1 
ATOM   6355 N  ND1   . HIS B 1 311 ? -0.840  16.679  40.880  1.00 49.92  ?  297 HIS B ND1   1 
ATOM   6356 C  CD2   . HIS B 1 311 ? -2.992  17.054  40.868  1.00 46.58  ?  297 HIS B CD2   1 
ATOM   6357 C  CE1   . HIS B 1 311 ? -1.410  15.662  40.258  1.00 44.70  ?  297 HIS B CE1   1 
ATOM   6358 N  NE2   . HIS B 1 311 ? -2.715  15.864  40.238  1.00 46.89  ?  297 HIS B NE2   1 
ATOM   6359 N  N     . GLN B 1 312 ? -2.343  18.486  45.131  1.00 61.40  ?  298 GLN B N     1 
ATOM   6360 C  CA    . GLN B 1 312 ? -3.206  17.830  46.109  1.00 60.83  ?  298 GLN B CA    1 
ATOM   6361 C  C     . GLN B 1 312 ? -4.646  18.227  45.800  1.00 57.08  ?  298 GLN B C     1 
ATOM   6362 O  O     . GLN B 1 312 ? -5.185  19.174  46.379  1.00 58.76  ?  298 GLN B O     1 
ATOM   6363 C  CB    . GLN B 1 312 ? -2.806  18.202  47.529  1.00 61.61  ?  298 GLN B CB    1 
ATOM   6364 C  CG    . GLN B 1 312 ? -2.010  17.121  48.238  1.00 67.73  ?  298 GLN B CG    1 
ATOM   6365 C  CD    . GLN B 1 312 ? -1.266  17.646  49.447  1.00 77.36  ?  298 GLN B CD    1 
ATOM   6366 O  OE1   . GLN B 1 312 ? -0.461  18.569  49.339  1.00 73.24  ?  298 GLN B OE1   1 
ATOM   6367 N  NE2   . GLN B 1 312 ? -1.536  17.061  50.611  1.00 85.48  ?  298 GLN B NE2   1 
ATOM   6368 N  N     . LEU B 1 313 ? -5.267  17.486  44.884  1.00 53.48  ?  299 LEU B N     1 
ATOM   6369 C  CA    . LEU B 1 313 ? -6.665  17.685  44.525  1.00 52.83  ?  299 LEU B CA    1 
ATOM   6370 C  C     . LEU B 1 313 ? -7.308  16.318  44.376  1.00 52.17  ?  299 LEU B C     1 
ATOM   6371 O  O     . LEU B 1 313 ? -6.919  15.545  43.495  1.00 61.20  ?  299 LEU B O     1 
ATOM   6372 C  CB    . LEU B 1 313 ? -6.799  18.484  43.226  1.00 49.12  ?  299 LEU B CB    1 
ATOM   6373 C  CG    . LEU B 1 313 ? -6.377  19.952  43.278  1.00 57.07  ?  299 LEU B CG    1 
ATOM   6374 C  CD1   . LEU B 1 313 ? -6.288  20.521  41.869  1.00 47.38  ?  299 LEU B CD1   1 
ATOM   6375 C  CD2   . LEU B 1 313 ? -7.346  20.754  44.134  1.00 45.77  ?  299 LEU B CD2   1 
ATOM   6376 N  N     . THR B 1 314 ? -8.284  16.027  45.224  1.00 54.07  ?  300 THR B N     1 
ATOM   6377 C  CA    . THR B 1 314 ? -8.957  14.740  45.244  1.00 51.67  ?  300 THR B CA    1 
ATOM   6378 C  C     . THR B 1 314 ? -10.176 14.748  44.332  1.00 57.07  ?  300 THR B C     1 
ATOM   6379 O  O     . THR B 1 314 ? -10.706 15.811  43.991  1.00 50.45  ?  300 THR B O     1 
ATOM   6380 C  CB    . THR B 1 314 ? -9.370  14.393  46.672  1.00 55.92  ?  300 THR B CB    1 
ATOM   6381 O  OG1   . THR B 1 314 ? -10.492 15.197  47.057  1.00 53.07  ?  300 THR B OG1   1 
ATOM   6382 C  CG2   . THR B 1 314 ? -8.215  14.653  47.629  1.00 56.69  ?  300 THR B CG2   1 
ATOM   6383 N  N     . PRO B 1 315 ? -10.625 13.570  43.884  1.00 58.86  ?  301 PRO B N     1 
ATOM   6384 C  CA    . PRO B 1 315 ? -11.853 13.527  43.070  1.00 49.38  ?  301 PRO B CA    1 
ATOM   6385 C  C     . PRO B 1 315 ? -13.071 14.114  43.767  1.00 55.23  ?  301 PRO B C     1 
ATOM   6386 O  O     . PRO B 1 315 ? -13.872 14.801  43.121  1.00 52.35  ?  301 PRO B O     1 
ATOM   6387 C  CB    . PRO B 1 315 ? -12.025 12.029  42.784  1.00 49.54  ?  301 PRO B CB    1 
ATOM   6388 C  CG    . PRO B 1 315 ? -10.635 11.472  42.864  1.00 55.26  ?  301 PRO B CG    1 
ATOM   6389 C  CD    . PRO B 1 315 ? -9.934  12.268  43.924  1.00 58.98  ?  301 PRO B CD    1 
ATOM   6390 N  N     . SER B 1 316 ? -13.229 13.877  45.073  1.00 46.62  ?  302 SER B N     1 
ATOM   6391 C  CA    . SER B 1 316 ? -14.383 14.420  45.783  1.00 53.77  ?  302 SER B CA    1 
ATOM   6392 C  C     . SER B 1 316 ? -14.310 15.935  45.890  1.00 60.29  ?  302 SER B C     1 
ATOM   6393 O  O     . SER B 1 316 ? -15.347 16.602  45.994  1.00 54.18  ?  302 SER B O     1 
ATOM   6394 C  CB    . SER B 1 316 ? -14.483 13.806  47.180  1.00 57.27  ?  302 SER B CB    1 
ATOM   6395 O  OG    . SER B 1 316 ? -13.961 12.488  47.198  1.00 71.26  ?  302 SER B OG    1 
ATOM   6396 N  N     . GLN B 1 317 ? -13.097 16.487  45.879  1.00 53.68  ?  303 GLN B N     1 
ATOM   6397 C  CA    . GLN B 1 317 ? -12.890 17.924  45.973  1.00 48.34  ?  303 GLN B CA    1 
ATOM   6398 C  C     . GLN B 1 317 ? -13.149 18.647  44.658  1.00 56.54  ?  303 GLN B C     1 
ATOM   6399 O  O     . GLN B 1 317 ? -13.300 19.873  44.663  1.00 48.53  ?  303 GLN B O     1 
ATOM   6400 C  CB    . GLN B 1 317 ? -11.456 18.200  46.439  1.00 59.55  ?  303 GLN B CB    1 
ATOM   6401 C  CG    . GLN B 1 317 ? -11.172 19.620  46.898  1.00 50.67  ?  303 GLN B CG    1 
ATOM   6402 C  CD    . GLN B 1 317 ? -9.691  19.863  47.121  1.00 53.84  ?  303 GLN B CD    1 
ATOM   6403 O  OE1   . GLN B 1 317 ? -8.846  19.151  46.579  1.00 50.82  ?  303 GLN B OE1   1 
ATOM   6404 N  NE2   . GLN B 1 317 ? -9.370  20.871  47.923  1.00 44.40  ?  303 GLN B NE2   1 
ATOM   6405 N  N     . THR B 1 318 ? -13.217 17.926  43.539  1.00 48.70  ?  304 THR B N     1 
ATOM   6406 C  CA    . THR B 1 318 ? -13.133 18.547  42.227  1.00 46.59  ?  304 THR B CA    1 
ATOM   6407 C  C     . THR B 1 318 ? -14.352 18.251  41.363  1.00 46.28  ?  304 THR B C     1 
ATOM   6408 O  O     . THR B 1 318 ? -14.967 17.182  41.449  1.00 52.46  ?  304 THR B O     1 
ATOM   6409 C  CB    . THR B 1 318 ? -11.869 18.082  41.480  1.00 46.70  ?  304 THR B CB    1 
ATOM   6410 O  OG1   . THR B 1 318 ? -11.750 16.656  41.567  1.00 40.02  ?  304 THR B OG1   1 
ATOM   6411 C  CG2   . THR B 1 318 ? -10.626 18.731  42.078  1.00 46.17  ?  304 THR B CG2   1 
ATOM   6412 N  N     . ILE B 1 319 ? -14.691 19.232  40.531  1.00 49.41  ?  305 ILE B N     1 
ATOM   6413 C  CA    . ILE B 1 319 ? -15.575 19.066  39.384  1.00 39.04  ?  305 ILE B CA    1 
ATOM   6414 C  C     . ILE B 1 319 ? -14.760 19.436  38.155  1.00 45.36  ?  305 ILE B C     1 
ATOM   6415 O  O     . ILE B 1 319 ? -14.158 20.515  38.108  1.00 40.44  ?  305 ILE B O     1 
ATOM   6416 C  CB    . ILE B 1 319 ? -16.838 19.941  39.496  1.00 41.26  ?  305 ILE B CB    1 
ATOM   6417 C  CG1   . ILE B 1 319 ? -17.697 19.497  40.683  1.00 42.51  ?  305 ILE B CG1   1 
ATOM   6418 C  CG2   . ILE B 1 319 ? -17.640 19.897  38.205  1.00 43.16  ?  305 ILE B CG2   1 
ATOM   6419 C  CD1   . ILE B 1 319 ? -18.964 20.315  40.862  1.00 45.69  ?  305 ILE B CD1   1 
ATOM   6420 N  N     . GLU B 1 320 ? -14.711 18.537  37.181  1.00 40.55  ?  306 GLU B N     1 
ATOM   6421 C  CA    . GLU B 1 320 ? -13.785 18.662  36.065  1.00 32.20  ?  306 GLU B CA    1 
ATOM   6422 C  C     . GLU B 1 320 ? -14.559 18.695  34.756  1.00 36.38  ?  306 GLU B C     1 
ATOM   6423 O  O     . GLU B 1 320 ? -15.486 17.901  34.557  1.00 40.44  ?  306 GLU B O     1 
ATOM   6424 C  CB    . GLU B 1 320 ? -12.769 17.516  36.093  1.00 34.15  ?  306 GLU B CB    1 
ATOM   6425 C  CG    . GLU B 1 320 ? -12.286 17.034  34.744  1.00 46.06  ?  306 GLU B CG    1 
ATOM   6426 C  CD    . GLU B 1 320 ? -11.189 15.990  34.874  1.00 50.02  ?  306 GLU B CD    1 
ATOM   6427 O  OE1   . GLU B 1 320 ? -11.282 15.129  35.780  1.00 41.32  ?  306 GLU B OE1   1 
ATOM   6428 O  OE2   . GLU B 1 320 ? -10.241 16.028  34.064  1.00 42.89  ?  306 GLU B OE2   1 
ATOM   6429 N  N     . VAL B 1 321 ? -14.185 19.621  33.874  1.00 31.08  ?  307 VAL B N     1 
ATOM   6430 C  CA    . VAL B 1 321 ? -14.837 19.803  32.581  1.00 39.69  ?  307 VAL B CA    1 
ATOM   6431 C  C     . VAL B 1 321 ? -13.806 19.587  31.481  1.00 38.87  ?  307 VAL B C     1 
ATOM   6432 O  O     . VAL B 1 321 ? -12.795 20.299  31.421  1.00 30.92  ?  307 VAL B O     1 
ATOM   6433 C  CB    . VAL B 1 321 ? -15.482 21.192  32.458  1.00 33.06  ?  307 VAL B CB    1 
ATOM   6434 C  CG1   . VAL B 1 321 ? -15.981 21.421  31.040  1.00 33.12  ?  307 VAL B CG1   1 
ATOM   6435 C  CG2   . VAL B 1 321 ? -16.624 21.333  33.457  1.00 37.23  ?  307 VAL B CG2   1 
ATOM   6436 N  N     . GLN B 1 322 ? -14.083 18.629  30.591  1.00 35.45  ?  308 GLN B N     1 
ATOM   6437 C  CA    . GLN B 1 322 ? -13.201 18.281  29.482  1.00 36.60  ?  308 GLN B CA    1 
ATOM   6438 C  C     . GLN B 1 322 ? -13.954 18.495  28.169  1.00 33.27  ?  308 GLN B C     1 
ATOM   6439 O  O     . GLN B 1 322 ? -15.161 18.765  28.202  1.00 37.12  ?  308 GLN B O     1 
ATOM   6440 C  CB    . GLN B 1 322 ? -12.702 16.842  29.647  1.00 30.82  ?  308 GLN B CB    1 
ATOM   6441 C  CG    . GLN B 1 322 ? -11.799 16.637  30.862  1.00 32.87  ?  308 GLN B CG    1 
ATOM   6442 C  CD    . GLN B 1 322 ? -10.475 17.396  30.764  1.00 45.93  ?  308 GLN B CD    1 
ATOM   6443 O  OE1   . GLN B 1 322 ? -10.044 17.792  29.676  1.00 36.15  ?  308 GLN B OE1   1 
ATOM   6444 N  NE2   . GLN B 1 322 ? -9.824  17.599  31.909  1.00 30.42  ?  308 GLN B NE2   1 
ATOM   6445 N  N     . PRO B 1 323 ? -13.287 18.440  27.005  1.00 34.51  ?  309 PRO B N     1 
ATOM   6446 C  CA    . PRO B 1 323 ? -13.963 18.873  25.766  1.00 40.06  ?  309 PRO B CA    1 
ATOM   6447 C  C     . PRO B 1 323 ? -15.275 18.165  25.460  1.00 47.90  ?  309 PRO B C     1 
ATOM   6448 O  O     . PRO B 1 323 ? -16.222 18.819  25.001  1.00 54.37  ?  309 PRO B O     1 
ATOM   6449 C  CB    . PRO B 1 323 ? -12.902 18.602  24.691  1.00 44.24  ?  309 PRO B CB    1 
ATOM   6450 C  CG    . PRO B 1 323 ? -11.622 18.811  25.404  1.00 36.63  ?  309 PRO B CG    1 
ATOM   6451 C  CD    . PRO B 1 323 ? -11.843 18.231  26.776  1.00 37.14  ?  309 PRO B CD    1 
ATOM   6452 N  N     . HIS B 1 324 ? -15.376 16.860  25.710  1.00 42.53  ?  310 HIS B N     1 
ATOM   6453 C  CA    . HIS B 1 324 ? -16.590 16.117  25.385  1.00 38.37  ?  310 HIS B CA    1 
ATOM   6454 C  C     . HIS B 1 324 ? -17.227 15.465  26.606  1.00 37.80  ?  310 HIS B C     1 
ATOM   6455 O  O     . HIS B 1 324 ? -18.207 14.725  26.459  1.00 37.97  ?  310 HIS B O     1 
ATOM   6456 C  CB    . HIS B 1 324 ? -16.297 15.040  24.332  1.00 38.11  ?  310 HIS B CB    1 
ATOM   6457 C  CG    . HIS B 1 324 ? -15.745 15.575  23.049  1.00 43.21  ?  310 HIS B CG    1 
ATOM   6458 N  ND1   . HIS B 1 324 ? -16.501 16.314  22.165  1.00 45.52  ?  310 HIS B ND1   1 
ATOM   6459 C  CD2   . HIS B 1 324 ? -14.513 15.470  22.497  1.00 41.14  ?  310 HIS B CD2   1 
ATOM   6460 C  CE1   . HIS B 1 324 ? -15.756 16.647  21.125  1.00 63.41  ?  310 HIS B CE1   1 
ATOM   6461 N  NE2   . HIS B 1 324 ? -14.545 16.147  21.301  1.00 51.65  ?  310 HIS B NE2   1 
ATOM   6462 N  N     . ALA B 1 325 ? -16.702 15.710  27.801  1.00 33.94  ?  311 ALA B N     1 
ATOM   6463 C  CA    . ALA B 1 325 ? -17.222 15.048  28.987  1.00 35.51  ?  311 ALA B CA    1 
ATOM   6464 C  C     . ALA B 1 325 ? -16.869 15.870  30.213  1.00 37.49  ?  311 ALA B C     1 
ATOM   6465 O  O     . ALA B 1 325 ? -15.873 16.597  30.223  1.00 37.88  ?  311 ALA B O     1 
ATOM   6466 C  CB    . ALA B 1 325 ? -16.664 13.630  29.128  1.00 28.98  ?  311 ALA B CB    1 
ATOM   6467 N  N     . SER B 1 326 ? -17.694 15.739  31.246  1.00 34.13  ?  312 SER B N     1 
ATOM   6468 C  CA    . SER B 1 326 ? -17.476 16.423  32.509  1.00 37.95  ?  312 SER B CA    1 
ATOM   6469 C  C     . SER B 1 326 ? -17.676 15.441  33.652  1.00 31.97  ?  312 SER B C     1 
ATOM   6470 O  O     . SER B 1 326 ? -18.384 14.441  33.516  1.00 39.35  ?  312 SER B O     1 
ATOM   6471 C  CB    . SER B 1 326 ? -18.412 17.626  32.663  1.00 36.44  ?  312 SER B CB    1 
ATOM   6472 O  OG    . SER B 1 326 ? -17.977 18.688  31.833  1.00 35.25  ?  312 SER B OG    1 
ATOM   6473 N  N     . ARG B 1 327 ? -17.039 15.731  34.780  1.00 45.14  ?  313 ARG B N     1 
ATOM   6474 C  CA    . ARG B 1 327 ? -17.040 14.839  35.928  1.00 41.80  ?  313 ARG B CA    1 
ATOM   6475 C  C     . ARG B 1 327 ? -17.451 15.599  37.180  1.00 45.80  ?  313 ARG B C     1 
ATOM   6476 O  O     . ARG B 1 327 ? -16.996 16.722  37.415  1.00 43.76  ?  313 ARG B O     1 
ATOM   6477 C  CB    . ARG B 1 327 ? -15.653 14.209  36.128  1.00 35.06  ?  313 ARG B CB    1 
ATOM   6478 C  CG    . ARG B 1 327 ? -15.488 13.451  37.434  1.00 35.84  ?  313 ARG B CG    1 
ATOM   6479 C  CD    . ARG B 1 327 ? -14.056 12.976  37.608  1.00 35.02  ?  313 ARG B CD    1 
ATOM   6480 N  NE    . ARG B 1 327 ? -13.117 14.087  37.701  1.00 38.16  ?  313 ARG B NE    1 
ATOM   6481 C  CZ    . ARG B 1 327 ? -12.855 14.757  38.815  1.00 43.21  ?  313 ARG B CZ    1 
ATOM   6482 N  NH1   . ARG B 1 327 ? -13.451 14.460  39.957  1.00 35.42  ?  313 ARG B NH1   1 
ATOM   6483 N  NH2   . ARG B 1 327 ? -11.969 15.749  38.783  1.00 43.16  ?  313 ARG B NH2   1 
ATOM   6484 N  N     . VAL B 1 328 ? -18.313 14.980  37.980  1.00 42.01  ?  314 VAL B N     1 
ATOM   6485 C  CA    . VAL B 1 328 ? -18.647 15.454  39.316  1.00 46.32  ?  314 VAL B CA    1 
ATOM   6486 C  C     . VAL B 1 328 ? -18.295 14.327  40.277  1.00 47.18  ?  314 VAL B C     1 
ATOM   6487 O  O     . VAL B 1 328 ? -18.915 13.259  40.242  1.00 41.47  ?  314 VAL B O     1 
ATOM   6488 C  CB    . VAL B 1 328 ? -20.124 15.847  39.438  1.00 39.10  ?  314 VAL B CB    1 
ATOM   6489 C  CG1   . VAL B 1 328 ? -20.450 16.267  40.860  1.00 39.87  ?  314 VAL B CG1   1 
ATOM   6490 C  CG2   . VAL B 1 328 ? -20.455 16.957  38.455  1.00 37.76  ?  314 VAL B CG2   1 
ATOM   6491 N  N     . GLY B 1 329 ? -17.309 14.558  41.131  1.00 42.94  ?  315 GLY B N     1 
ATOM   6492 C  CA    . GLY B 1 329 ? -16.876 13.512  42.043  1.00 38.64  ?  315 GLY B CA    1 
ATOM   6493 C  C     . GLY B 1 329 ? -16.309 12.327  41.284  1.00 46.92  ?  315 GLY B C     1 
ATOM   6494 O  O     . GLY B 1 329 ? -15.381 12.461  40.475  1.00 47.75  ?  315 GLY B O     1 
ATOM   6495 N  N     . ASP B 1 330 ? -16.860 11.144  41.541  1.00 48.08  ?  316 ASP B N     1 
ATOM   6496 C  CA    . ASP B 1 330 ? -16.408 9.918   40.898  1.00 46.81  ?  316 ASP B CA    1 
ATOM   6497 C  C     . ASP B 1 330 ? -17.216 9.556   39.661  1.00 47.61  ?  316 ASP B C     1 
ATOM   6498 O  O     . ASP B 1 330 ? -16.907 8.551   39.014  1.00 54.61  ?  316 ASP B O     1 
ATOM   6499 C  CB    . ASP B 1 330 ? -16.454 8.751   41.891  1.00 46.07  ?  316 ASP B CB    1 
ATOM   6500 C  CG    . ASP B 1 330 ? -15.300 8.780   42.875  1.00 71.60  ?  316 ASP B CG    1 
ATOM   6501 O  OD1   . ASP B 1 330 ? -14.156 9.050   42.445  1.00 68.19  ?  316 ASP B OD1   1 
ATOM   6502 O  OD2   . ASP B 1 330 ? -15.536 8.536   44.078  1.00 66.75  ?  316 ASP B OD2   1 
ATOM   6503 N  N     . VAL B 1 331 ? -18.224 10.349  39.306  1.00 41.13  ?  317 VAL B N     1 
ATOM   6504 C  CA    . VAL B 1 331 ? -19.150 10.023  38.227  1.00 42.92  ?  317 VAL B CA    1 
ATOM   6505 C  C     . VAL B 1 331 ? -18.812 10.885  37.020  1.00 46.31  ?  317 VAL B C     1 
ATOM   6506 O  O     . VAL B 1 331 ? -18.658 12.108  37.142  1.00 40.79  ?  317 VAL B O     1 
ATOM   6507 C  CB    . VAL B 1 331 ? -20.612 10.229  38.660  1.00 50.69  ?  317 VAL B CB    1 
ATOM   6508 C  CG1   . VAL B 1 331 ? -21.568 9.834   37.537  1.00 44.98  ?  317 VAL B CG1   1 
ATOM   6509 C  CG2   . VAL B 1 331 ? -20.910 9.433   39.923  1.00 46.61  ?  317 VAL B CG2   1 
ATOM   6510 N  N     . TRP B 1 332 ? -18.686 10.248  35.859  1.00 37.96  ?  318 TRP B N     1 
ATOM   6511 C  CA    . TRP B 1 332 ? -18.417 10.937  34.605  1.00 38.19  ?  318 TRP B CA    1 
ATOM   6512 C  C     . TRP B 1 332 ? -19.710 11.108  33.816  1.00 44.23  ?  318 TRP B C     1 
ATOM   6513 O  O     . TRP B 1 332 ? -20.574 10.227  33.816  1.00 37.12  ?  318 TRP B O     1 
ATOM   6514 C  CB    . TRP B 1 332 ? -17.387 10.170  33.773  1.00 38.94  ?  318 TRP B CB    1 
ATOM   6515 C  CG    . TRP B 1 332 ? -15.969 10.523  34.123  1.00 43.16  ?  318 TRP B CG    1 
ATOM   6516 C  CD1   . TRP B 1 332 ? -15.145 9.853   34.981  1.00 40.93  ?  318 TRP B CD1   1 
ATOM   6517 C  CD2   . TRP B 1 332 ? -15.217 11.638  33.633  1.00 36.55  ?  318 TRP B CD2   1 
ATOM   6518 N  NE1   . TRP B 1 332 ? -13.925 10.477  35.049  1.00 42.94  ?  318 TRP B NE1   1 
ATOM   6519 C  CE2   . TRP B 1 332 ? -13.942 11.577  34.231  1.00 49.45  ?  318 TRP B CE2   1 
ATOM   6520 C  CE3   . TRP B 1 332 ? -15.496 12.681  32.745  1.00 37.87  ?  318 TRP B CE3   1 
ATOM   6521 C  CZ2   . TRP B 1 332 ? -12.947 12.521  33.969  1.00 44.97  ?  318 TRP B CZ2   1 
ATOM   6522 C  CZ3   . TRP B 1 332 ? -14.509 13.617  32.487  1.00 32.70  ?  318 TRP B CZ3   1 
ATOM   6523 C  CH2   . TRP B 1 332 ? -13.251 13.530  33.097  1.00 42.70  ?  318 TRP B CH2   1 
ATOM   6524 N  N     . PHE B 1 333 ? -19.837 12.250  33.148  1.00 40.88  ?  319 PHE B N     1 
ATOM   6525 C  CA    . PHE B 1 333 ? -21.001 12.578  32.329  1.00 40.93  ?  319 PHE B CA    1 
ATOM   6526 C  C     . PHE B 1 333 ? -20.500 12.875  30.919  1.00 42.58  ?  319 PHE B C     1 
ATOM   6527 O  O     . PHE B 1 333 ? -19.987 13.966  30.652  1.00 43.65  ?  319 PHE B O     1 
ATOM   6528 C  CB    . PHE B 1 333 ? -21.766 13.755  32.930  1.00 36.49  ?  319 PHE B CB    1 
ATOM   6529 C  CG    . PHE B 1 333 ? -22.249 13.502  34.333  1.00 39.63  ?  319 PHE B CG    1 
ATOM   6530 C  CD1   . PHE B 1 333 ? -21.422 13.740  35.421  1.00 37.27  ?  319 PHE B CD1   1 
ATOM   6531 C  CD2   . PHE B 1 333 ? -23.525 13.004  34.561  1.00 36.44  ?  319 PHE B CD2   1 
ATOM   6532 C  CE1   . PHE B 1 333 ? -21.862 13.493  36.710  1.00 36.74  ?  319 PHE B CE1   1 
ATOM   6533 C  CE2   . PHE B 1 333 ? -23.974 12.754  35.846  1.00 37.67  ?  319 PHE B CE2   1 
ATOM   6534 C  CZ    . PHE B 1 333 ? -23.147 12.998  36.922  1.00 42.53  ?  319 PHE B CZ    1 
ATOM   6535 N  N     . THR B 1 334 ? -20.639 11.906  30.021  1.00 43.82  ?  320 THR B N     1 
ATOM   6536 C  CA    . THR B 1 334 ? -20.068 11.997  28.686  1.00 49.74  ?  320 THR B CA    1 
ATOM   6537 C  C     . THR B 1 334 ? -21.112 12.477  27.683  1.00 44.76  ?  320 THR B C     1 
ATOM   6538 O  O     . THR B 1 334 ? -22.320 12.373  27.905  1.00 41.93  ?  320 THR B O     1 
ATOM   6539 C  CB    . THR B 1 334 ? -19.487 10.646  28.248  1.00 39.54  ?  320 THR B CB    1 
ATOM   6540 O  OG1   . THR B 1 334 ? -20.549 9.726   27.975  1.00 41.02  ?  320 THR B OG1   1 
ATOM   6541 C  CG2   . THR B 1 334 ? -18.607 10.069  29.345  1.00 34.97  ?  320 THR B CG2   1 
ATOM   6542 N  N     . GLY B 1 335 ? -20.624 13.015  26.567  1.00 43.84  ?  321 GLY B N     1 
ATOM   6543 C  CA    . GLY B 1 335 ? -21.505 13.577  25.563  1.00 42.48  ?  321 GLY B CA    1 
ATOM   6544 C  C     . GLY B 1 335 ? -21.996 14.970  25.875  1.00 56.40  ?  321 GLY B C     1 
ATOM   6545 O  O     . GLY B 1 335 ? -23.064 15.369  25.393  1.00 46.27  ?  321 GLY B O     1 
ATOM   6546 N  N     . ILE B 1 336 ? -21.251 15.726  26.672  1.00 49.83  ?  322 ILE B N     1 
ATOM   6547 C  CA    . ILE B 1 336 ? -21.613 17.086  27.044  1.00 43.04  ?  322 ILE B CA    1 
ATOM   6548 C  C     . ILE B 1 336 ? -20.560 18.036  26.485  1.00 47.17  ?  322 ILE B C     1 
ATOM   6549 O  O     . ILE B 1 336 ? -19.389 17.964  26.874  1.00 36.83  ?  322 ILE B O     1 
ATOM   6550 C  CB    . ILE B 1 336 ? -21.743 17.251  28.566  1.00 37.41  ?  322 ILE B CB    1 
ATOM   6551 C  CG1   . ILE B 1 336 ? -22.966 16.482  29.058  1.00 39.88  ?  322 ILE B CG1   1 
ATOM   6552 C  CG2   . ILE B 1 336 ? -21.839 18.730  28.936  1.00 45.44  ?  322 ILE B CG2   1 
ATOM   6553 C  CD1   . ILE B 1 336 ? -22.874 16.061  30.489  1.00 49.77  ?  322 ILE B CD1   1 
ATOM   6554 N  N     . PRO B 1 337 ? -20.923 18.936  25.575  1.00 40.52  ?  323 PRO B N     1 
ATOM   6555 C  CA    . PRO B 1 337 ? -19.953 19.921  25.092  1.00 49.84  ?  323 PRO B CA    1 
ATOM   6556 C  C     . PRO B 1 337 ? -19.419 20.774  26.233  1.00 47.51  ?  323 PRO B C     1 
ATOM   6557 O  O     . PRO B 1 337 ? -20.133 21.105  27.183  1.00 44.54  ?  323 PRO B O     1 
ATOM   6558 C  CB    . PRO B 1 337 ? -20.762 20.749  24.088  1.00 52.43  ?  323 PRO B CB    1 
ATOM   6559 C  CG    . PRO B 1 337 ? -21.839 19.820  23.633  1.00 52.59  ?  323 PRO B CG    1 
ATOM   6560 C  CD    . PRO B 1 337 ? -22.196 19.008  24.841  1.00 48.50  ?  323 PRO B CD    1 
ATOM   6561 N  N     . MET B 1 338 ? -18.135 21.105  26.136  1.00 51.88  ?  324 MET B N     1 
ATOM   6562 C  CA    . MET B 1 338 ? -17.466 21.846  27.198  1.00 45.17  ?  324 MET B CA    1 
ATOM   6563 C  C     . MET B 1 338 ? -18.112 23.213  27.416  1.00 52.89  ?  324 MET B C     1 
ATOM   6564 O  O     . MET B 1 338 ? -18.241 23.675  28.557  1.00 43.25  ?  324 MET B O     1 
ATOM   6565 C  CB    . MET B 1 338 ? -15.981 21.958  26.844  1.00 43.25  ?  324 MET B CB    1 
ATOM   6566 C  CG    . MET B 1 338 ? -15.171 22.976  27.583  1.00 58.24  ?  324 MET B CG    1 
ATOM   6567 S  SD    . MET B 1 338 ? -13.475 22.975  26.938  1.00 58.38  ?  324 MET B SD    1 
ATOM   6568 C  CE    . MET B 1 338 ? -12.601 22.379  28.371  1.00 50.61  ?  324 MET B CE    1 
ATOM   6569 N  N     . LEU B 1 339 ? -18.549 23.865  26.335  1.00 58.08  ?  325 LEU B N     1 
ATOM   6570 C  CA    . LEU B 1 339 ? -19.242 25.143  26.477  1.00 50.54  ?  325 LEU B CA    1 
ATOM   6571 C  C     . LEU B 1 339 ? -20.555 24.982  27.234  1.00 54.29  ?  325 LEU B C     1 
ATOM   6572 O  O     . LEU B 1 339 ? -20.878 25.793  28.109  1.00 60.58  ?  325 LEU B O     1 
ATOM   6573 C  CB    . LEU B 1 339 ? -19.486 25.761  25.101  1.00 62.82  ?  325 LEU B CB    1 
ATOM   6574 C  CG    . LEU B 1 339 ? -20.486 26.909  25.012  1.00 52.28  ?  325 LEU B CG    1 
ATOM   6575 C  CD1   . LEU B 1 339 ? -20.031 28.090  25.856  1.00 60.05  ?  325 LEU B CD1   1 
ATOM   6576 C  CD2   . LEU B 1 339 ? -20.664 27.320  23.564  1.00 62.29  ?  325 LEU B CD2   1 
ATOM   6577 N  N     . GLN B 1 340 ? -21.327 23.942  26.910  1.00 47.66  ?  326 GLN B N     1 
ATOM   6578 C  CA    . GLN B 1 340 ? -22.598 23.724  27.595  1.00 46.70  ?  326 GLN B CA    1 
ATOM   6579 C  C     . GLN B 1 340 ? -22.385 23.408  29.068  1.00 47.00  ?  326 GLN B C     1 
ATOM   6580 O  O     . GLN B 1 340 ? -23.164 23.849  29.921  1.00 47.88  ?  326 GLN B O     1 
ATOM   6581 C  CB    . GLN B 1 340 ? -23.377 22.602  26.917  1.00 47.65  ?  326 GLN B CB    1 
ATOM   6582 C  CG    . GLN B 1 340 ? -24.368 23.077  25.877  1.00 50.61  ?  326 GLN B CG    1 
ATOM   6583 C  CD    . GLN B 1 340 ? -25.313 21.977  25.453  1.00 59.02  ?  326 GLN B CD    1 
ATOM   6584 O  OE1   . GLN B 1 340 ? -24.945 20.803  25.442  1.00 61.87  ?  326 GLN B OE1   1 
ATOM   6585 N  NE2   . GLN B 1 340 ? -26.536 22.348  25.096  1.00 56.13  ?  326 GLN B NE2   1 
ATOM   6586 N  N     . ALA B 1 341 ? -21.350 22.625  29.385  1.00 51.01  ?  327 ALA B N     1 
ATOM   6587 C  CA    . ALA B 1 341 ? -21.037 22.362  30.785  1.00 46.29  ?  327 ALA B CA    1 
ATOM   6588 C  C     . ALA B 1 341 ? -20.691 23.651  31.517  1.00 46.62  ?  327 ALA B C     1 
ATOM   6589 O  O     . ALA B 1 341 ? -21.218 23.913  32.602  1.00 52.03  ?  327 ALA B O     1 
ATOM   6590 C  CB    . ALA B 1 341 ? -19.888 21.361  30.891  1.00 45.05  ?  327 ALA B CB    1 
ATOM   6591 N  N     . ILE B 1 342 ? -19.864 24.502  30.902  1.00 50.41  ?  328 ILE B N     1 
ATOM   6592 C  CA    . ILE B 1 342 ? -19.454 25.749  31.547  1.00 48.45  ?  328 ILE B CA    1 
ATOM   6593 C  C     . ILE B 1 342 ? -20.660 26.643  31.805  1.00 48.38  ?  328 ILE B C     1 
ATOM   6594 O  O     . ILE B 1 342 ? -20.807 27.211  32.894  1.00 55.65  ?  328 ILE B O     1 
ATOM   6595 C  CB    . ILE B 1 342 ? -18.386 26.460  30.695  1.00 52.62  ?  328 ILE B CB    1 
ATOM   6596 C  CG1   . ILE B 1 342 ? -17.015 25.816  30.913  1.00 46.36  ?  328 ILE B CG1   1 
ATOM   6597 C  CG2   . ILE B 1 342 ? -18.328 27.942  31.026  1.00 46.77  ?  328 ILE B CG2   1 
ATOM   6598 C  CD1   . ILE B 1 342 ? -16.048 26.057  29.777  1.00 46.24  ?  328 ILE B CD1   1 
ATOM   6599 N  N     . GLU B 1 343 ? -21.481 26.824  30.790  1.00 48.62  ?  329 GLU B N     1 
ATOM   6600 C  CA    . GLU B 1 343 ? -22.678 27.630  30.907  1.00 53.23  ?  329 GLU B CA    1 
ATOM   6601 C  C     . GLU B 1 343 ? -23.545 27.125  32.043  1.00 51.93  ?  329 GLU B C     1 
ATOM   6602 O  O     . GLU B 1 343 ? -24.168 27.880  32.734  1.00 53.34  ?  329 GLU B O     1 
ATOM   6603 C  CB    . GLU B 1 343 ? -23.477 27.554  29.634  1.00 57.91  ?  329 GLU B CB    1 
ATOM   6604 C  CG    . GLU B 1 343 ? -23.126 28.564  28.587  1.00 58.77  ?  329 GLU B CG    1 
ATOM   6605 C  CD    . GLU B 1 343 ? -23.840 28.283  27.304  1.00 67.74  ?  329 GLU B CD    1 
ATOM   6606 O  OE1   . GLU B 1 343 ? -24.706 27.419  27.310  1.00 66.80  ?  329 GLU B OE1   1 
ATOM   6607 O  OE2   . GLU B 1 343 ? -23.539 28.894  26.279  1.00 75.29  ?  329 GLU B OE2   1 
ATOM   6608 N  N     . THR B 1 344 ? -23.562 25.816  32.212  1.00 50.68  ?  330 THR B N     1 
ATOM   6609 C  CA    . THR B 1 344 ? -24.315 25.163  33.249  1.00 59.49  ?  330 THR B CA    1 
ATOM   6610 C  C     . THR B 1 344 ? -23.720 25.458  34.585  1.00 52.69  ?  330 THR B C     1 
ATOM   6611 O  O     . THR B 1 344 ? -24.428 25.780  35.477  1.00 54.57  ?  330 THR B O     1 
ATOM   6612 C  CB    . THR B 1 344 ? -24.430 23.640  33.004  1.00 50.81  ?  330 THR B CB    1 
ATOM   6613 O  OG1   . THR B 1 344 ? -25.443 23.414  32.046  1.00 54.81  ?  330 THR B OG1   1 
ATOM   6614 C  CG2   . THR B 1 344 ? -24.761 22.914  34.219  1.00 52.08  ?  330 THR B CG2   1 
ATOM   6615 N  N     . LEU B 1 345 ? -22.411 25.353  34.731  1.00 51.58  ?  331 LEU B N     1 
ATOM   6616 C  CA    . LEU B 1 345 ? -21.778 25.666  36.003  1.00 52.66  ?  331 LEU B CA    1 
ATOM   6617 C  C     . LEU B 1 345 ? -21.852 27.143  36.392  1.00 59.57  ?  331 LEU B C     1 
ATOM   6618 O  O     . LEU B 1 345 ? -21.790 27.460  37.544  1.00 58.83  ?  331 LEU B O     1 
ATOM   6619 C  CB    . LEU B 1 345 ? -20.312 25.270  36.008  1.00 51.26  ?  331 LEU B CB    1 
ATOM   6620 C  CG    . LEU B 1 345 ? -19.816 23.857  36.255  1.00 59.25  ?  331 LEU B CG    1 
ATOM   6621 C  CD1   . LEU B 1 345 ? -20.583 23.159  37.335  1.00 52.20  ?  331 LEU B CD1   1 
ATOM   6622 C  CD2   . LEU B 1 345 ? -19.922 23.093  34.974  1.00 52.50  ?  331 LEU B CD2   1 
ATOM   6623 N  N     . VAL B 1 346 ? -21.946 28.039  35.428  1.00 69.01  ?  332 VAL B N     1 
ATOM   6624 C  CA    . VAL B 1 346 ? -22.013 29.463  35.739  1.00 72.71  ?  332 VAL B CA    1 
ATOM   6625 C  C     . VAL B 1 346 ? -23.312 29.770  36.465  1.00 58.21  ?  332 VAL B C     1 
ATOM   6626 O  O     . VAL B 1 346 ? -23.302 30.380  37.509  1.00 66.55  ?  332 VAL B O     1 
ATOM   6627 C  CB    . VAL B 1 346 ? -21.902 30.307  34.497  1.00 58.75  ?  332 VAL B CB    1 
ATOM   6628 C  CG1   . VAL B 1 346 ? -22.287 31.731  34.813  1.00 62.31  ?  332 VAL B CG1   1 
ATOM   6629 C  CG2   . VAL B 1 346 ? -20.495 30.233  33.980  1.00 53.22  ?  332 VAL B CG2   1 
ATOM   6630 N  N     . GLU B 1 347 ? -24.407 29.284  35.897  1.00 70.95  ?  333 GLU B N     1 
ATOM   6631 C  CA    . GLU B 1 347 ? -25.744 29.361  36.445  1.00 61.62  ?  333 GLU B CA    1 
ATOM   6632 C  C     . GLU B 1 347 ? -25.681 28.891  37.870  1.00 70.20  ?  333 GLU B C     1 
ATOM   6633 O  O     . GLU B 1 347 ? -26.034 29.597  38.766  1.00 74.74  ?  333 GLU B O     1 
ATOM   6634 C  CB    . GLU B 1 347 ? -26.619 28.356  35.737  1.00 96.52  ?  333 GLU B CB    1 
ATOM   6635 C  CG    . GLU B 1 347 ? -27.551 28.810  34.649  1.00 113.28 ?  333 GLU B CG    1 
ATOM   6636 C  CD    . GLU B 1 347 ? -28.613 27.737  34.379  1.00 110.47 ?  333 GLU B CD    1 
ATOM   6637 O  OE1   . GLU B 1 347 ? -28.414 26.893  33.467  1.00 110.91 ?  333 GLU B OE1   1 
ATOM   6638 O  OE2   . GLU B 1 347 ? -29.634 27.704  35.105  1.00 112.06 ?  333 GLU B OE2   1 
ATOM   6639 N  N     . LEU B 1 348 ? -25.183 27.686  38.078  1.00 60.27  ?  334 LEU B N     1 
ATOM   6640 C  CA    . LEU B 1 348 ? -25.056 27.123  39.391  1.00 64.48  ?  334 LEU B CA    1 
ATOM   6641 C  C     . LEU B 1 348 ? -24.157 27.854  40.350  1.00 63.25  ?  334 LEU B C     1 
ATOM   6642 O  O     . LEU B 1 348 ? -24.335 27.735  41.538  1.00 65.29  ?  334 LEU B O     1 
ATOM   6643 C  CB    . LEU B 1 348 ? -24.572 25.686  39.297  1.00 63.49  ?  334 LEU B CB    1 
ATOM   6644 C  CG    . LEU B 1 348 ? -25.528 24.635  38.762  1.00 58.68  ?  334 LEU B CG    1 
ATOM   6645 C  CD1   . LEU B 1 348 ? -24.804 23.330  38.557  1.00 56.74  ?  334 LEU B CD1   1 
ATOM   6646 C  CD2   . LEU B 1 348 ? -26.674 24.438  39.728  1.00 60.92  ?  334 LEU B CD2   1 
ATOM   6647 N  N     . CYS B 1 349 ? -23.149 28.553  39.852  1.00 61.49  ?  335 CYS B N     1 
ATOM   6648 C  CA    . CYS B 1 349 ? -22.240 29.290  40.719  1.00 62.98  ?  335 CYS B CA    1 
ATOM   6649 C  C     . CYS B 1 349 ? -22.937 30.555  41.204  1.00 67.36  ?  335 CYS B C     1 
ATOM   6650 O  O     . CYS B 1 349 ? -22.810 30.937  42.343  1.00 68.24  ?  335 CYS B O     1 
ATOM   6651 C  CB    . CYS B 1 349 ? -20.928 29.588  40.012  1.00 60.89  ?  335 CYS B CB    1 
ATOM   6652 S  SG    . CYS B 1 349 ? -19.795 28.197  40.087  1.00 63.40  ?  335 CYS B SG    1 
ATOM   6653 N  N     . LYS B 1 350 ? -23.740 31.138  40.336  1.00 65.39  ?  336 LYS B N     1 
ATOM   6654 C  CA    . LYS B 1 350 ? -24.534 32.280  40.671  1.00 69.53  ?  336 LYS B CA    1 
ATOM   6655 C  C     . LYS B 1 350 ? -25.512 31.881  41.781  1.00 70.65  ?  336 LYS B C     1 
ATOM   6656 O  O     . LYS B 1 350 ? -25.701 32.607  42.721  1.00 79.48  ?  336 LYS B O     1 
ATOM   6657 C  CB    . LYS B 1 350 ? -25.280 32.791  39.459  1.00 67.63  ?  336 LYS B CB    1 
ATOM   6658 C  CG    . LYS B 1 350 ? -24.430 33.600  38.521  1.00 72.48  ?  336 LYS B CG    1 
ATOM   6659 C  CD    . LYS B 1 350 ? -25.242 34.107  37.375  1.00 69.98  ?  336 LYS B CD    1 
ATOM   6660 C  CE    . LYS B 1 350 ? -24.380 34.349  36.171  1.00 65.67  ?  336 LYS B CE    1 
ATOM   6661 N  NZ    . LYS B 1 350 ? -25.209 34.600  34.973  1.00 86.41  ?  336 LYS B NZ    1 
ATOM   6662 N  N     . GLN B 1 351 ? -26.119 30.716  41.670  1.00 69.91  ?  337 GLN B N     1 
ATOM   6663 C  CA    . GLN B 1 351 ? -27.016 30.221  42.668  1.00 71.70  ?  337 GLN B CA    1 
ATOM   6664 C  C     . GLN B 1 351 ? -26.336 29.693  43.928  1.00 74.22  ?  337 GLN B C     1 
ATOM   6665 O  O     . GLN B 1 351 ? -26.958 29.679  44.952  1.00 76.47  ?  337 GLN B O     1 
ATOM   6666 C  CB    . GLN B 1 351 ? -27.909 29.152  42.011  1.00 69.83  ?  337 GLN B CB    1 
ATOM   6667 C  CG    . GLN B 1 351 ? -28.684 28.205  42.910  1.00 83.37  ?  337 GLN B CG    1 
ATOM   6668 C  CD    . GLN B 1 351 ? -29.246 26.981  42.167  1.00 92.99  ?  337 GLN B CD    1 
ATOM   6669 O  OE1   . GLN B 1 351 ? -29.380 25.906  42.734  1.00 86.90  ?  337 GLN B OE1   1 
ATOM   6670 N  NE2   . GLN B 1 351 ? -29.599 27.160  40.909  1.00 81.98  ?  337 GLN B NE2   1 
ATOM   6671 N  N     . HIS B 1 352 ? -25.066 29.303  43.914  1.00 76.67  ?  338 HIS B N     1 
ATOM   6672 C  CA    . HIS B 1 352 ? -24.489 28.698  45.134  1.00 74.19  ?  338 HIS B CA    1 
ATOM   6673 C  C     . HIS B 1 352 ? -23.133 29.141  45.669  1.00 84.56  ?  338 HIS B C     1 
ATOM   6674 O  O     . HIS B 1 352 ? -22.675 28.606  46.645  1.00 91.34  ?  338 HIS B O     1 
ATOM   6675 C  CB    . HIS B 1 352 ? -24.416 27.194  44.988  1.00 71.23  ?  338 HIS B CB    1 
ATOM   6676 C  CG    . HIS B 1 352 ? -25.738 26.514  44.954  1.00 71.36  ?  338 HIS B CG    1 
ATOM   6677 N  ND1   . HIS B 1 352 ? -26.512 26.344  46.071  1.00 74.34  ?  338 HIS B ND1   1 
ATOM   6678 C  CD2   . HIS B 1 352 ? -26.399 25.916  43.945  1.00 70.23  ?  338 HIS B CD2   1 
ATOM   6679 C  CE1   . HIS B 1 352 ? -27.608 25.695  45.750  1.00 73.70  ?  338 HIS B CE1   1 
ATOM   6680 N  NE2   . HIS B 1 352 ? -27.564 25.421  44.466  1.00 77.93  ?  338 HIS B NE2   1 
ATOM   6681 N  N     . VAL B 1 353 ? -22.472 30.052  44.979  1.00 84.25  ?  339 VAL B N     1 
ATOM   6682 C  CA    . VAL B 1 353 ? -21.204 30.662  45.382  1.00 91.92  ?  339 VAL B CA    1 
ATOM   6683 C  C     . VAL B 1 353 ? -21.460 32.059  45.939  1.00 90.42  ?  339 VAL B C     1 
ATOM   6684 O  O     . VAL B 1 353 ? -22.027 32.919  45.256  1.00 92.34  ?  339 VAL B O     1 
ATOM   6685 C  CB    . VAL B 1 353 ? -20.206 30.706  44.216  1.00 82.71  ?  339 VAL B CB    1 
ATOM   6686 C  CG1   . VAL B 1 353 ? -18.945 31.448  44.631  1.00 80.44  ?  339 VAL B CG1   1 
ATOM   6687 C  CG2   . VAL B 1 353 ? -19.865 29.295  43.761  1.00 78.80  ?  339 VAL B CG2   1 
ATOM   6688 N  N     . HIS B 1 354 ? -21.050 32.275  47.190  1.00 102.56 ?  340 HIS B N     1 
ATOM   6689 C  CA    . HIS B 1 354 ? -21.312 33.500  47.937  1.00 109.82 ?  340 HIS B CA    1 
ATOM   6690 C  C     . HIS B 1 354 ? -20.097 34.393  48.156  1.00 119.68 ?  340 HIS B C     1 
ATOM   6691 O  O     . HIS B 1 354 ? -20.256 35.612  48.252  1.00 124.98 ?  340 HIS B O     1 
ATOM   6692 C  CB    . HIS B 1 354 ? -21.878 33.143  49.314  1.00 114.33 ?  340 HIS B CB    1 
ATOM   6693 C  CG    . HIS B 1 354 ? -21.022 32.171  50.066  1.00 124.70 ?  340 HIS B CG    1 
ATOM   6694 N  ND1   . HIS B 1 354 ? -20.091 32.568  51.001  1.00 124.22 ?  340 HIS B ND1   1 
ATOM   6695 C  CD2   . HIS B 1 354 ? -20.936 30.821  49.998  1.00 122.29 ?  340 HIS B CD2   1 
ATOM   6696 C  CE1   . HIS B 1 354 ? -19.476 31.504  51.486  1.00 126.73 ?  340 HIS B CE1   1 
ATOM   6697 N  NE2   . HIS B 1 354 ? -19.971 30.431  50.894  1.00 128.79 ?  340 HIS B NE2   1 
ATOM   6698 N  N     . ASP B 1 355 ? -18.995 33.754  48.513  1.00 117.67 ?  341 ASP B N     1 
ATOM   6699 C  CA    . ASP B 1 355 ? -17.739 34.399  48.907  1.00 122.23 ?  341 ASP B CA    1 
ATOM   6700 C  C     . ASP B 1 355 ? -17.225 35.579  48.100  1.00 125.62 ?  341 ASP B C     1 
ATOM   6701 O  O     . ASP B 1 355 ? -17.545 35.696  46.929  1.00 122.14 ?  341 ASP B O     1 
ATOM   6702 C  CB    . ASP B 1 355 ? -16.646 33.309  49.131  1.00 126.59 ?  341 ASP B CB    1 
ATOM   6703 C  CG    . ASP B 1 355 ? -15.622 33.184  47.985  1.00 119.37 ?  341 ASP B CG    1 
ATOM   6704 O  OD1   . ASP B 1 355 ? -15.864 33.634  46.849  1.00 120.91 ?  341 ASP B OD1   1 
ATOM   6705 O  OD2   . ASP B 1 355 ? -14.553 32.591  48.230  1.00 100.41 ?  341 ASP B OD2   1 
ATOM   6706 N  N     . THR B 1 356 ? -16.455 36.449  48.761  1.00 117.66 ?  342 THR B N     1 
ATOM   6707 C  CA    . THR B 1 356 ? -15.772 37.582  48.121  1.00 122.88 ?  342 THR B CA    1 
ATOM   6708 C  C     . THR B 1 356 ? -14.294 37.314  48.439  1.00 124.68 ?  342 THR B C     1 
ATOM   6709 O  O     . THR B 1 356 ? -13.934 37.047  49.590  1.00 127.10 ?  342 THR B O     1 
ATOM   6710 C  CB    . THR B 1 356 ? -16.214 38.973  48.620  1.00 125.28 ?  342 THR B CB    1 
ATOM   6711 O  OG1   . THR B 1 356 ? -15.268 39.480  49.578  1.00 132.06 ?  342 THR B OG1   1 
ATOM   6712 C  CG2   . THR B 1 356 ? -17.605 38.928  49.241  1.00 115.35 ?  342 THR B CG2   1 
ATOM   6713 N  N     . PRO B 1 357 ? -13.428 37.402  47.436  1.00 112.04 ?  343 PRO B N     1 
ATOM   6714 C  CA    . PRO B 1 357 ? -12.067 36.980  47.725  1.00 116.53 ?  343 PRO B CA    1 
ATOM   6715 C  C     . PRO B 1 357 ? -11.257 37.791  48.726  1.00 123.85 ?  343 PRO B C     1 
ATOM   6716 O  O     . PRO B 1 357 ? -10.378 37.172  49.315  1.00 126.25 ?  343 PRO B O     1 
ATOM   6717 C  CB    . PRO B 1 357 ? -11.422 36.931  46.351  1.00 97.96  ?  343 PRO B CB    1 
ATOM   6718 C  CG    . PRO B 1 357 ? -12.569 36.889  45.407  1.00 99.82  ?  343 PRO B CG    1 
ATOM   6719 C  CD    . PRO B 1 357 ? -13.583 37.768  46.034  1.00 97.51  ?  343 PRO B CD    1 
ATOM   6720 N  N     . VAL B 1 358 ? -11.532 39.079  48.901  1.00 131.74 ?  344 VAL B N     1 
ATOM   6721 C  CA    . VAL B 1 358 ? -10.787 39.901  49.847  1.00 133.71 ?  344 VAL B CA    1 
ATOM   6722 C  C     . VAL B 1 358 ? -9.293  39.603  49.783  1.00 134.38 ?  344 VAL B C     1 
ATOM   6723 O  O     . VAL B 1 358 ? -8.790  38.765  50.531  1.00 138.01 ?  344 VAL B O     1 
ATOM   6724 C  CB    . VAL B 1 358 ? -11.281 39.689  51.290  1.00 137.26 ?  344 VAL B CB    1 
ATOM   6725 C  CG1   . VAL B 1 358 ? -12.689 40.241  51.456  1.00 128.17 ?  344 VAL B CG1   1 
ATOM   6726 C  CG2   . VAL B 1 358 ? -11.233 38.213  51.656  1.00 132.45 ?  344 VAL B CG2   1 
ATOM   6727 N  N     . PRO B 1 359 ? -8.579  40.293  48.881  1.00 135.23 ?  345 PRO B N     1 
ATOM   6728 C  CA    . PRO B 1 359 ? -7.134  40.111  48.709  1.00 121.45 ?  345 PRO B CA    1 
ATOM   6729 C  C     . PRO B 1 359 ? -6.345  40.729  49.858  1.00 117.68 ?  345 PRO B C     1 
ATOM   6730 O  O     . PRO B 1 359 ? -6.312  41.954  49.968  1.00 115.19 ?  345 PRO B O     1 
ATOM   6731 C  CB    . PRO B 1 359 ? -6.845  40.863  47.409  1.00 122.51 ?  345 PRO B CB    1 
ATOM   6732 C  CG    . PRO B 1 359 ? -7.897  41.917  47.350  1.00 124.03 ?  345 PRO B CG    1 
ATOM   6733 C  CD    . PRO B 1 359 ? -9.126  41.302  47.957  1.00 127.22 ?  345 PRO B CD    1 
ATOM   6734 N  N     . PRO B 1 370 ? 14.981  47.246  41.135  1.00 94.06  ?  356 PRO B N     1 
ATOM   6735 C  CA    . PRO B 1 370 ? 16.209  47.201  40.331  1.00 96.93  ?  356 PRO B CA    1 
ATOM   6736 C  C     . PRO B 1 370 ? 17.418  46.765  41.160  1.00 99.84  ?  356 PRO B C     1 
ATOM   6737 O  O     . PRO B 1 370 ? 17.377  46.864  42.386  1.00 108.19 ?  356 PRO B O     1 
ATOM   6738 C  CB    . PRO B 1 370 ? 16.372  48.647  39.836  1.00 91.63  ?  356 PRO B CB    1 
ATOM   6739 C  CG    . PRO B 1 370 ? 15.341  49.462  40.575  1.00 77.70  ?  356 PRO B CG    1 
ATOM   6740 C  CD    . PRO B 1 370 ? 14.262  48.521  40.982  1.00 82.61  ?  356 PRO B CD    1 
ATOM   6741 N  N     . ASP B 1 371 ? 18.481  46.325  40.497  1.00 87.17  ?  357 ASP B N     1 
ATOM   6742 C  CA    . ASP B 1 371 ? 19.601  45.662  41.161  1.00 97.45  ?  357 ASP B CA    1 
ATOM   6743 C  C     . ASP B 1 371 ? 20.883  46.033  40.418  1.00 94.49  ?  357 ASP B C     1 
ATOM   6744 O  O     . ASP B 1 371 ? 20.922  47.019  39.675  1.00 96.82  ?  357 ASP B O     1 
ATOM   6745 C  CB    . ASP B 1 371 ? 19.367  44.139  41.215  1.00 98.82  ?  357 ASP B CB    1 
ATOM   6746 C  CG    . ASP B 1 371 ? 18.884  43.661  42.578  1.00 107.88 ?  357 ASP B CG    1 
ATOM   6747 O  OD1   . ASP B 1 371 ? 18.194  44.430  43.282  1.00 119.35 ?  357 ASP B OD1   1 
ATOM   6748 O  OD2   . ASP B 1 371 ? 19.189  42.504  42.940  1.00 94.02  ?  357 ASP B OD2   1 
ATOM   6749 N  N     . GLY B 1 372 ? 21.940  45.256  40.641  1.00 80.43  ?  358 GLY B N     1 
ATOM   6750 C  CA    . GLY B 1 372 ? 23.170  45.387  39.883  1.00 62.28  ?  358 GLY B CA    1 
ATOM   6751 C  C     . GLY B 1 372 ? 23.360  44.251  38.897  1.00 65.06  ?  358 GLY B C     1 
ATOM   6752 O  O     . GLY B 1 372 ? 22.755  44.251  37.820  1.00 67.46  ?  358 GLY B O     1 
ATOM   6753 N  N     . SER B 1 373 ? 24.201  43.280  39.255  1.00 58.54  ?  359 SER B N     1 
ATOM   6754 C  CA    . SER B 1 373 ? 24.474  42.148  38.374  1.00 61.65  ?  359 SER B CA    1 
ATOM   6755 C  C     . SER B 1 373 ? 23.222  41.319  38.115  1.00 50.77  ?  359 SER B C     1 
ATOM   6756 O  O     . SER B 1 373 ? 22.455  41.022  39.032  1.00 52.59  ?  359 SER B O     1 
ATOM   6757 C  CB    . SER B 1 373 ? 25.563  41.267  38.969  1.00 52.78  ?  359 SER B CB    1 
ATOM   6758 O  OG    . SER B 1 373 ? 26.223  40.530  37.957  1.00 54.84  ?  359 SER B OG    1 
ATOM   6759 N  N     . LEU B 1 374 ? 23.028  40.939  36.852  1.00 38.41  ?  360 LEU B N     1 
ATOM   6760 C  CA    . LEU B 1 374 ? 21.809  40.250  36.450  1.00 48.90  ?  360 LEU B CA    1 
ATOM   6761 C  C     . LEU B 1 374 ? 21.744  38.859  37.064  1.00 53.54  ?  360 LEU B C     1 
ATOM   6762 O  O     . LEU B 1 374 ? 22.717  38.098  37.023  1.00 48.04  ?  360 LEU B O     1 
ATOM   6763 C  CB    . LEU B 1 374 ? 21.731  40.150  34.927  1.00 48.69  ?  360 LEU B CB    1 
ATOM   6764 C  CG    . LEU B 1 374 ? 20.962  41.278  34.239  1.00 49.71  ?  360 LEU B CG    1 
ATOM   6765 C  CD1   . LEU B 1 374 ? 21.129  41.196  32.729  1.00 33.33  ?  360 LEU B CD1   1 
ATOM   6766 C  CD2   . LEU B 1 374 ? 19.492  41.246  34.634  1.00 46.32  ?  360 LEU B CD2   1 
ATOM   6767 N  N     . THR B 1 375 ? 20.590  38.533  37.634  1.00 49.56  ?  361 THR B N     1 
ATOM   6768 C  CA    . THR B 1 375 ? 20.276  37.201  38.116  1.00 45.35  ?  361 THR B CA    1 
ATOM   6769 C  C     . THR B 1 375 ? 18.908  36.815  37.575  1.00 54.40  ?  361 THR B C     1 
ATOM   6770 O  O     . THR B 1 375 ? 18.192  37.642  37.004  1.00 43.05  ?  361 THR B O     1 
ATOM   6771 C  CB    . THR B 1 375 ? 20.273  37.128  39.649  1.00 46.99  ?  361 THR B CB    1 
ATOM   6772 O  OG1   . THR B 1 375 ? 19.317  38.060  40.168  1.00 52.59  ?  361 THR B OG1   1 
ATOM   6773 C  CG2   . THR B 1 375 ? 21.647  37.456  40.207  1.00 52.75  ?  361 THR B CG2   1 
ATOM   6774 N  N     . GLN B 1 376 ? 18.548  35.541  37.745  1.00 49.44  ?  362 GLN B N     1 
ATOM   6775 C  CA    . GLN B 1 376 ? 17.182  35.135  37.430  1.00 50.62  ?  362 GLN B CA    1 
ATOM   6776 C  C     . GLN B 1 376 ? 16.177  35.979  38.202  1.00 45.18  ?  362 GLN B C     1 
ATOM   6777 O  O     . GLN B 1 376 ? 15.187  36.455  37.635  1.00 42.67  ?  362 GLN B O     1 
ATOM   6778 C  CB    . GLN B 1 376 ? 16.987  33.648  37.734  1.00 48.19  ?  362 GLN B CB    1 
ATOM   6779 C  CG    . GLN B 1 376 ? 17.730  32.726  36.784  1.00 44.45  ?  362 GLN B CG    1 
ATOM   6780 C  CD    . GLN B 1 376 ? 16.972  32.493  35.498  1.00 39.69  ?  362 GLN B CD    1 
ATOM   6781 O  OE1   . GLN B 1 376 ? 15.754  32.662  35.444  1.00 46.19  ?  362 GLN B OE1   1 
ATOM   6782 N  NE2   . GLN B 1 376 ? 17.688  32.108  34.451  1.00 40.31  ?  362 GLN B NE2   1 
ATOM   6783 N  N     . ASP B 1 377 ? 16.450  36.226  39.485  1.00 42.60  ?  363 ASP B N     1 
ATOM   6784 C  CA    . ASP B 1 377 ? 15.503  36.947  40.329  1.00 55.39  ?  363 ASP B CA    1 
ATOM   6785 C  C     . ASP B 1 377 ? 15.242  38.355  39.802  1.00 53.81  ?  363 ASP B C     1 
ATOM   6786 O  O     . ASP B 1 377 ? 14.086  38.743  39.592  1.00 46.08  ?  363 ASP B O     1 
ATOM   6787 C  CB    . ASP B 1 377 ? 16.027  36.993  41.764  1.00 59.70  ?  363 ASP B CB    1 
ATOM   6788 C  CG    . ASP B 1 377 ? 14.918  36.938  42.793  1.00 72.83  ?  363 ASP B CG    1 
ATOM   6789 O  OD1   . ASP B 1 377 ? 14.416  35.827  43.067  1.00 75.93  ?  363 ASP B OD1   1 
ATOM   6790 O  OD2   . ASP B 1 377 ? 14.563  38.001  43.342  1.00 69.76  ?  363 ASP B OD2   1 
ATOM   6791 N  N     . ASN B 1 378 ? 16.304  39.136  39.565  1.00 52.02  ?  364 ASN B N     1 
ATOM   6792 C  CA    . ASN B 1 378 ? 16.097  40.512  39.122  1.00 44.70  ?  364 ASN B CA    1 
ATOM   6793 C  C     . ASN B 1 378 ? 15.780  40.613  37.636  1.00 42.26  ?  364 ASN B C     1 
ATOM   6794 O  O     . ASN B 1 378 ? 15.254  41.642  37.200  1.00 42.73  ?  364 ASN B O     1 
ATOM   6795 C  CB    . ASN B 1 378 ? 17.301  41.399  39.481  1.00 45.64  ?  364 ASN B CB    1 
ATOM   6796 C  CG    . ASN B 1 378 ? 18.612  40.936  38.856  1.00 52.46  ?  364 ASN B CG    1 
ATOM   6797 O  OD1   . ASN B 1 378 ? 18.646  40.348  37.775  1.00 48.69  ?  364 ASN B OD1   1 
ATOM   6798 N  ND2   . ASN B 1 378 ? 19.710  41.216  39.549  1.00 50.09  ?  364 ASN B ND2   1 
ATOM   6799 N  N     . PHE B 1 379 ? 16.082  39.580  36.848  1.00 39.98  ?  365 PHE B N     1 
ATOM   6800 C  CA    . PHE B 1 379 ? 15.659  39.586  35.452  1.00 45.17  ?  365 PHE B CA    1 
ATOM   6801 C  C     . PHE B 1 379 ? 14.137  39.549  35.341  1.00 43.28  ?  365 PHE B C     1 
ATOM   6802 O  O     . PHE B 1 379 ? 13.536  40.352  34.618  1.00 46.21  ?  365 PHE B O     1 
ATOM   6803 C  CB    . PHE B 1 379 ? 16.278  38.407  34.700  1.00 35.87  ?  365 PHE B CB    1 
ATOM   6804 C  CG    . PHE B 1 379 ? 15.704  38.206  33.330  1.00 35.83  ?  365 PHE B CG    1 
ATOM   6805 C  CD1   . PHE B 1 379 ? 16.073  39.034  32.285  1.00 34.31  ?  365 PHE B CD1   1 
ATOM   6806 C  CD2   . PHE B 1 379 ? 14.784  37.201  33.089  1.00 35.68  ?  365 PHE B CD2   1 
ATOM   6807 C  CE1   . PHE B 1 379 ? 15.544  38.861  31.025  1.00 35.74  ?  365 PHE B CE1   1 
ATOM   6808 C  CE2   . PHE B 1 379 ? 14.250  37.025  31.830  1.00 39.38  ?  365 PHE B CE2   1 
ATOM   6809 C  CZ    . PHE B 1 379 ? 14.629  37.855  30.796  1.00 37.31  ?  365 PHE B CZ    1 
ATOM   6810 N  N     . TRP B 1 380 ? 13.497  38.616  36.051  1.00 40.85  ?  366 TRP B N     1 
ATOM   6811 C  CA    . TRP B 1 380 ? 12.046  38.489  35.966  1.00 39.60  ?  366 TRP B CA    1 
ATOM   6812 C  C     . TRP B 1 380 ? 11.340  39.654  36.642  1.00 43.35  ?  366 TRP B C     1 
ATOM   6813 O  O     . TRP B 1 380 ? 10.266  40.070  36.193  1.00 42.88  ?  366 TRP B O     1 
ATOM   6814 C  CB    . TRP B 1 380 ? 11.606  37.155  36.567  1.00 39.76  ?  366 TRP B CB    1 
ATOM   6815 C  CG    . TRP B 1 380 ? 12.112  36.012  35.758  1.00 42.04  ?  366 TRP B CG    1 
ATOM   6816 C  CD1   . TRP B 1 380 ? 13.065  35.106  36.118  1.00 37.40  ?  366 TRP B CD1   1 
ATOM   6817 C  CD2   . TRP B 1 380 ? 11.715  35.670  34.426  1.00 39.51  ?  366 TRP B CD2   1 
ATOM   6818 N  NE1   . TRP B 1 380 ? 13.280  34.216  35.096  1.00 41.38  ?  366 TRP B NE1   1 
ATOM   6819 C  CE2   . TRP B 1 380 ? 12.463  34.540  34.045  1.00 37.56  ?  366 TRP B CE2   1 
ATOM   6820 C  CE3   . TRP B 1 380 ? 10.795  36.206  33.519  1.00 35.35  ?  366 TRP B CE3   1 
ATOM   6821 C  CZ2   . TRP B 1 380 ? 12.319  33.936  32.799  1.00 38.83  ?  366 TRP B CZ2   1 
ATOM   6822 C  CZ3   . TRP B 1 380 ? 10.655  35.605  32.282  1.00 39.50  ?  366 TRP B CZ3   1 
ATOM   6823 C  CH2   . TRP B 1 380 ? 11.412  34.483  31.934  1.00 33.69  ?  366 TRP B CH2   1 
ATOM   6824 N  N     . LYS B 1 381 ? 11.929  40.199  37.708  1.00 43.89  ?  367 LYS B N     1 
ATOM   6825 C  CA    . LYS B 1 381 ? 11.381  41.407  38.311  1.00 46.45  ?  367 LYS B CA    1 
ATOM   6826 C  C     . LYS B 1 381 ? 11.455  42.580  37.341  1.00 55.16  ?  367 LYS B C     1 
ATOM   6827 O  O     . LYS B 1 381 ? 10.514  43.378  37.245  1.00 50.69  ?  367 LYS B O     1 
ATOM   6828 C  CB    . LYS B 1 381 ? 12.133  41.735  39.601  1.00 48.73  ?  367 LYS B CB    1 
ATOM   6829 C  CG    . LYS B 1 381 ? 11.647  40.970  40.817  1.00 52.04  ?  367 LYS B CG    1 
ATOM   6830 C  CD    . LYS B 1 381 ? 12.627  41.114  41.971  1.00 69.11  ?  367 LYS B CD    1 
ATOM   6831 C  CE    . LYS B 1 381 ? 12.280  40.174  43.115  1.00 73.46  ?  367 LYS B CE    1 
ATOM   6832 N  NZ    . LYS B 1 381 ? 13.133  40.437  44.311  1.00 75.74  ?  367 LYS B NZ    1 
ATOM   6833 N  N     . THR B 1 382 ? 12.568  42.697  36.610  1.00 46.86  ?  368 THR B N     1 
ATOM   6834 C  CA    . THR B 1 382 ? 12.692  43.753  35.609  1.00 50.21  ?  368 THR B CA    1 
ATOM   6835 C  C     . THR B 1 382 ? 11.677  43.561  34.493  1.00 47.93  ?  368 THR B C     1 
ATOM   6836 O  O     . THR B 1 382 ? 11.049  44.526  34.037  1.00 54.21  ?  368 THR B O     1 
ATOM   6837 C  CB    . THR B 1 382 ? 14.115  43.779  35.046  1.00 44.56  ?  368 THR B CB    1 
ATOM   6838 O  OG1   . THR B 1 382 ? 15.039  44.073  36.100  1.00 43.79  ?  368 THR B OG1   1 
ATOM   6839 C  CG2   . THR B 1 382 ? 14.246  44.832  33.954  1.00 42.28  ?  368 THR B CG2   1 
ATOM   6840 N  N     . LEU B 1 383 ? 11.498  42.319  34.044  1.00 41.61  ?  369 LEU B N     1 
ATOM   6841 C  CA    . LEU B 1 383 ? 10.517  42.045  33.003  1.00 54.31  ?  369 LEU B CA    1 
ATOM   6842 C  C     . LEU B 1 383 ? 9.100   42.327  33.478  1.00 48.91  ?  369 LEU B C     1 
ATOM   6843 O  O     . LEU B 1 383 ? 8.257   42.755  32.683  1.00 53.48  ?  369 LEU B O     1 
ATOM   6844 C  CB    . LEU B 1 383 ? 10.635  40.593  32.546  1.00 52.67  ?  369 LEU B CB    1 
ATOM   6845 C  CG    . LEU B 1 383 ? 11.040  40.367  31.094  1.00 47.47  ?  369 LEU B CG    1 
ATOM   6846 C  CD1   . LEU B 1 383 ? 10.694  38.946  30.729  1.00 58.02  ?  369 LEU B CD1   1 
ATOM   6847 C  CD2   . LEU B 1 383 ? 10.343  41.342  30.166  1.00 55.07  ?  369 LEU B CD2   1 
ATOM   6848 N  N     . GLN B 1 384 ? 8.830   42.124  34.771  1.00 50.57  ?  370 GLN B N     1 
ATOM   6849 C  CA    . GLN B 1 384 ? 7.485   42.348  35.294  1.00 45.51  ?  370 GLN B CA    1 
ATOM   6850 C  C     . GLN B 1 384 ? 7.031   43.783  35.062  1.00 47.42  ?  370 GLN B C     1 
ATOM   6851 O  O     . GLN B 1 384 ? 5.871   44.024  34.710  1.00 48.24  ?  370 GLN B O     1 
ATOM   6852 C  CB    . GLN B 1 384 ? 7.434   42.012  36.783  1.00 47.15  ?  370 GLN B CB    1 
ATOM   6853 C  CG    . GLN B 1 384 ? 6.103   42.342  37.437  1.00 49.54  ?  370 GLN B CG    1 
ATOM   6854 C  CD    . GLN B 1 384 ? 4.956   41.561  36.825  1.00 48.39  ?  370 GLN B CD    1 
ATOM   6855 O  OE1   . GLN B 1 384 ? 5.014   40.338  36.717  1.00 46.66  ?  370 GLN B OE1   1 
ATOM   6856 N  NE2   . GLN B 1 384 ? 3.914   42.266  36.410  1.00 49.53  ?  370 GLN B NE2   1 
ATOM   6857 N  N     . THR B 1 385 ? 7.927   44.751  35.264  1.00 43.69  ?  371 THR B N     1 
ATOM   6858 C  CA    . THR B 1 385 ? 7.583   46.149  35.036  1.00 46.30  ?  371 THR B CA    1 
ATOM   6859 C  C     . THR B 1 385 ? 7.462   46.502  33.558  1.00 40.59  ?  371 THR B C     1 
ATOM   6860 O  O     . THR B 1 385 ? 6.899   47.551  33.236  1.00 36.45  ?  371 THR B O     1 
ATOM   6861 C  CB    . THR B 1 385 ? 8.624   47.058  35.695  1.00 47.27  ?  371 THR B CB    1 
ATOM   6862 O  OG1   . THR B 1 385 ? 9.805   47.104  34.885  1.00 53.75  ?  371 THR B OG1   1 
ATOM   6863 C  CG2   . THR B 1 385 ? 8.987   46.530  37.075  1.00 44.52  ?  371 THR B CG2   1 
ATOM   6864 N  N     . PHE B 1 386 ? 7.937   45.645  32.657  1.00 42.55  ?  372 PHE B N     1 
ATOM   6865 C  CA    . PHE B 1 386 ? 8.000   45.976  31.238  1.00 42.79  ?  372 PHE B CA    1 
ATOM   6866 C  C     . PHE B 1 386 ? 6.774   45.521  30.454  1.00 49.08  ?  372 PHE B C     1 
ATOM   6867 O  O     . PHE B 1 386 ? 6.371   46.201  29.502  1.00 42.73  ?  372 PHE B O     1 
ATOM   6868 C  CB    . PHE B 1 386 ? 9.258   45.347  30.625  1.00 50.33  ?  372 PHE B CB    1 
ATOM   6869 C  CG    . PHE B 1 386 ? 9.326   45.446  29.128  1.00 36.64  ?  372 PHE B CG    1 
ATOM   6870 C  CD1   . PHE B 1 386 ? 9.583   46.660  28.510  1.00 39.10  ?  372 PHE B CD1   1 
ATOM   6871 C  CD2   . PHE B 1 386 ? 9.147   44.321  28.338  1.00 38.61  ?  372 PHE B CD2   1 
ATOM   6872 C  CE1   . PHE B 1 386 ? 9.653   46.754  27.130  1.00 41.99  ?  372 PHE B CE1   1 
ATOM   6873 C  CE2   . PHE B 1 386 ? 9.215   44.406  26.958  1.00 43.07  ?  372 PHE B CE2   1 
ATOM   6874 C  CZ    . PHE B 1 386 ? 9.469   45.626  26.354  1.00 46.35  ?  372 PHE B CZ    1 
ATOM   6875 N  N     . ILE B 1 387 ? 6.163   44.399  30.836  1.00 40.44  ?  373 ILE B N     1 
ATOM   6876 C  CA    . ILE B 1 387 ? 5.056   43.861  30.057  1.00 42.47  ?  373 ILE B CA    1 
ATOM   6877 C  C     . ILE B 1 387 ? 3.847   44.791  30.161  1.00 46.23  ?  373 ILE B C     1 
ATOM   6878 O  O     . ILE B 1 387 ? 3.660   45.504  31.159  1.00 34.17  ?  373 ILE B O     1 
ATOM   6879 C  CB    . ILE B 1 387 ? 4.722   42.428  30.514  1.00 41.85  ?  373 ILE B CB    1 
ATOM   6880 C  CG1   . ILE B 1 387 ? 4.441   42.380  32.018  1.00 44.93  ?  373 ILE B CG1   1 
ATOM   6881 C  CG2   . ILE B 1 387 ? 5.874   41.484  30.177  1.00 38.51  ?  373 ILE B CG2   1 
ATOM   6882 C  CD1   . ILE B 1 387 ? 4.044   40.995  32.517  1.00 40.64  ?  373 ILE B CD1   1 
ATOM   6883 N  N     . ARG B 1 388 ? 3.034   44.803  29.110  1.00 35.20  ?  374 ARG B N     1 
ATOM   6884 C  CA    . ARG B 1 388 ? 1.902   45.705  28.969  1.00 36.63  ?  374 ARG B CA    1 
ATOM   6885 C  C     . ARG B 1 388 ? 0.705   44.917  28.448  1.00 42.04  ?  374 ARG B C     1 
ATOM   6886 O  O     . ARG B 1 388 ? 0.867   43.803  27.945  1.00 40.29  ?  374 ARG B O     1 
ATOM   6887 C  CB    . ARG B 1 388 ? 2.209   46.861  28.007  1.00 37.15  ?  374 ARG B CB    1 
ATOM   6888 C  CG    . ARG B 1 388 ? 3.224   47.871  28.525  1.00 39.46  ?  374 ARG B CG    1 
ATOM   6889 C  CD    . ARG B 1 388 ? 2.716   48.592  29.762  1.00 46.06  ?  374 ARG B CD    1 
ATOM   6890 N  NE    . ARG B 1 388 ? 3.597   49.693  30.135  1.00 51.83  ?  374 ARG B NE    1 
ATOM   6891 C  CZ    . ARG B 1 388 ? 4.538   49.603  31.065  1.00 56.45  ?  374 ARG B CZ    1 
ATOM   6892 N  NH1   . ARG B 1 388 ? 4.736   48.480  31.740  1.00 45.74  ?  374 ARG B NH1   1 
ATOM   6893 N  NH2   . ARG B 1 388 ? 5.305   50.659  31.318  1.00 47.55  ?  374 ARG B NH2   1 
ATOM   6894 N  N     . PRO B 1 389 ? -0.505  45.461  28.595  1.00 41.50  ?  375 PRO B N     1 
ATOM   6895 C  CA    . PRO B 1 389 ? -1.664  44.838  27.940  1.00 36.23  ?  375 PRO B CA    1 
ATOM   6896 C  C     . PRO B 1 389 ? -1.483  44.769  26.429  1.00 41.69  ?  375 PRO B C     1 
ATOM   6897 O  O     . PRO B 1 389 ? -0.928  45.677  25.807  1.00 42.49  ?  375 PRO B O     1 
ATOM   6898 C  CB    . PRO B 1 389 ? -2.826  45.759  28.327  1.00 36.50  ?  375 PRO B CB    1 
ATOM   6899 C  CG    . PRO B 1 389 ? -2.404  46.376  29.614  1.00 46.12  ?  375 PRO B CG    1 
ATOM   6900 C  CD    . PRO B 1 389 ? -0.903  46.516  29.544  1.00 37.58  ?  375 PRO B CD    1 
ATOM   6901 N  N     . GLY B 1 390 ? -1.969  43.676  25.839  1.00 41.76  ?  376 GLY B N     1 
ATOM   6902 C  CA    . GLY B 1 390 ? -1.837  43.442  24.417  1.00 35.54  ?  376 GLY B CA    1 
ATOM   6903 C  C     . GLY B 1 390 ? -0.581  42.714  24.000  1.00 37.99  ?  376 GLY B C     1 
ATOM   6904 O  O     . GLY B 1 390 ? -0.437  42.391  22.813  1.00 36.77  ?  376 GLY B O     1 
ATOM   6905 N  N     . ASP B 1 391 ? 0.327   42.438  24.931  1.00 32.95  ?  377 ASP B N     1 
ATOM   6906 C  CA    . ASP B 1 391 ? 1.570   41.760  24.592  1.00 36.67  ?  377 ASP B CA    1 
ATOM   6907 C  C     . ASP B 1 391 ? 1.314   40.301  24.237  1.00 41.98  ?  377 ASP B C     1 
ATOM   6908 O  O     . ASP B 1 391 ? 0.419   39.648  24.783  1.00 41.43  ?  377 ASP B O     1 
ATOM   6909 C  CB    . ASP B 1 391 ? 2.560   41.835  25.756  1.00 34.30  ?  377 ASP B CB    1 
ATOM   6910 C  CG    . ASP B 1 391 ? 3.282   43.172  25.826  1.00 43.88  ?  377 ASP B CG    1 
ATOM   6911 O  OD1   . ASP B 1 391 ? 3.230   43.942  24.842  1.00 42.75  ?  377 ASP B OD1   1 
ATOM   6912 O  OD2   . ASP B 1 391 ? 3.896   43.454  26.875  1.00 38.61  ?  377 ASP B OD2   1 
ATOM   6913 N  N     . ILE B 1 392 ? 2.107   39.799  23.298  1.00 39.42  ?  378 ILE B N     1 
ATOM   6914 C  CA    . ILE B 1 392 ? 2.233   38.371  23.040  1.00 34.32  ?  378 ILE B CA    1 
ATOM   6915 C  C     . ILE B 1 392 ? 3.588   37.944  23.582  1.00 39.64  ?  378 ILE B C     1 
ATOM   6916 O  O     . ILE B 1 392 ? 4.628   38.446  23.136  1.00 39.38  ?  378 ILE B O     1 
ATOM   6917 C  CB    . ILE B 1 392 ? 2.100   38.048  21.544  1.00 39.58  ?  378 ILE B CB    1 
ATOM   6918 C  CG1   . ILE B 1 392 ? 0.768   38.591  21.006  1.00 33.39  ?  378 ILE B CG1   1 
ATOM   6919 C  CG2   . ILE B 1 392 ? 2.248   36.541  21.308  1.00 33.83  ?  378 ILE B CG2   1 
ATOM   6920 C  CD1   . ILE B 1 392 ? 0.547   38.356  19.527  1.00 25.55  ?  378 ILE B CD1   1 
ATOM   6921 N  N     . ILE B 1 393 ? 3.578   37.044  24.559  1.00 37.66  ?  379 ILE B N     1 
ATOM   6922 C  CA    . ILE B 1 393 ? 4.784   36.612  25.256  1.00 34.90  ?  379 ILE B CA    1 
ATOM   6923 C  C     . ILE B 1 393 ? 4.962   35.120  25.018  1.00 34.58  ?  379 ILE B C     1 
ATOM   6924 O  O     . ILE B 1 393 ? 4.046   34.333  25.281  1.00 34.56  ?  379 ILE B O     1 
ATOM   6925 C  CB    . ILE B 1 393 ? 4.705   36.919  26.763  1.00 33.68  ?  379 ILE B CB    1 
ATOM   6926 C  CG1   . ILE B 1 393 ? 4.391   38.399  26.993  1.00 39.92  ?  379 ILE B CG1   1 
ATOM   6927 C  CG2   . ILE B 1 393 ? 5.992   36.514  27.461  1.00 34.00  ?  379 ILE B CG2   1 
ATOM   6928 C  CD1   . ILE B 1 393 ? 4.094   38.754  28.441  1.00 30.31  ?  379 ILE B CD1   1 
ATOM   6929 N  N     . LEU B 1 394 ? 6.135   34.733  24.517  1.00 34.44  ?  380 LEU B N     1 
ATOM   6930 C  CA    . LEU B 1 394 ? 6.471   33.334  24.275  1.00 33.46  ?  380 LEU B CA    1 
ATOM   6931 C  C     . LEU B 1 394 ? 7.722   32.984  25.066  1.00 34.37  ?  380 LEU B C     1 
ATOM   6932 O  O     . LEU B 1 394 ? 8.698   33.741  25.056  1.00 29.95  ?  380 LEU B O     1 
ATOM   6933 C  CB    . LEU B 1 394 ? 6.685   33.061  22.787  1.00 28.64  ?  380 LEU B CB    1 
ATOM   6934 C  CG    . LEU B 1 394 ? 5.556   33.508  21.855  1.00 31.37  ?  380 LEU B CG    1 
ATOM   6935 C  CD1   . LEU B 1 394 ? 5.831   34.888  21.305  1.00 23.18  ?  380 LEU B CD1   1 
ATOM   6936 C  CD2   . LEU B 1 394 ? 5.375   32.512  20.721  1.00 29.01  ?  380 LEU B CD2   1 
ATOM   6937 N  N     . ALA B 1 395 ? 7.685   31.846  25.755  1.00 29.88  ?  381 ALA B N     1 
ATOM   6938 C  CA    . ALA B 1 395 ? 8.774   31.405  26.615  1.00 35.39  ?  381 ALA B CA    1 
ATOM   6939 C  C     . ALA B 1 395 ? 9.084   29.943  26.324  1.00 38.51  ?  381 ALA B C     1 
ATOM   6940 O  O     . ALA B 1 395 ? 8.167   29.118  26.262  1.00 35.13  ?  381 ALA B O     1 
ATOM   6941 C  CB    . ALA B 1 395 ? 8.405   31.590  28.092  1.00 27.45  ?  381 ALA B CB    1 
ATOM   6942 N  N     . ASP B 1 396 ? 10.367  29.622  26.147  1.00 33.05  ?  382 ASP B N     1 
ATOM   6943 C  CA    . ASP B 1 396 ? 10.756  28.259  25.812  1.00 31.52  ?  382 ASP B CA    1 
ATOM   6944 C  C     . ASP B 1 396 ? 11.033  27.440  27.059  1.00 35.09  ?  382 ASP B C     1 
ATOM   6945 O  O     . ASP B 1 396 ? 11.295  27.975  28.140  1.00 32.77  ?  382 ASP B O     1 
ATOM   6946 C  CB    . ASP B 1 396 ? 11.990  28.223  24.899  1.00 24.48  ?  382 ASP B CB    1 
ATOM   6947 C  CG    . ASP B 1 396 ? 11.863  27.153  23.795  1.00 44.13  ?  382 ASP B CG    1 
ATOM   6948 O  OD1   . ASP B 1 396 ? 11.336  26.054  24.090  1.00 31.02  ?  382 ASP B OD1   1 
ATOM   6949 O  OD2   . ASP B 1 396 ? 12.248  27.416  22.631  1.00 28.94  ?  382 ASP B OD2   1 
ATOM   6950 N  N     . GLN B 1 397 ? 10.965  26.117  26.888  1.00 34.36  ?  383 GLN B N     1 
ATOM   6951 C  CA    . GLN B 1 397 ? 11.329  25.202  27.959  1.00 34.20  ?  383 GLN B CA    1 
ATOM   6952 C  C     . GLN B 1 397 ? 12.762  25.478  28.392  1.00 34.16  ?  383 GLN B C     1 
ATOM   6953 O  O     . GLN B 1 397 ? 13.654  25.671  27.562  1.00 36.93  ?  383 GLN B O     1 
ATOM   6954 C  CB    . GLN B 1 397 ? 11.188  23.751  27.497  1.00 34.10  ?  383 GLN B CB    1 
ATOM   6955 C  CG    . GLN B 1 397 ? 9.751   23.276  27.327  1.00 38.89  ?  383 GLN B CG    1 
ATOM   6956 C  CD    . GLN B 1 397 ? 8.783   23.946  28.282  1.00 50.83  ?  383 GLN B CD    1 
ATOM   6957 O  OE1   . GLN B 1 397 ? 8.060   24.872  27.906  1.00 50.16  ?  383 GLN B OE1   1 
ATOM   6958 N  NE2   . GLN B 1 397 ? 8.754   23.472  29.523  1.00 51.37  ?  383 GLN B NE2   1 
ATOM   6959 N  N     . GLY B 1 398 ? 12.977  25.496  29.694  1.00 39.34  ?  384 GLY B N     1 
ATOM   6960 C  CA    . GLY B 1 398 ? 14.200  25.989  30.276  1.00 33.50  ?  384 GLY B CA    1 
ATOM   6961 C  C     . GLY B 1 398 ? 13.876  26.983  31.363  1.00 45.60  ?  384 GLY B C     1 
ATOM   6962 O  O     . GLY B 1 398 ? 12.737  27.077  31.835  1.00 35.70  ?  384 GLY B O     1 
ATOM   6963 N  N     . THR B 1 399 ? 14.891  27.751  31.773  1.00 31.62  ?  385 THR B N     1 
ATOM   6964 C  CA    . THR B 1 399 ? 14.653  28.800  32.757  1.00 34.75  ?  385 THR B CA    1 
ATOM   6965 C  C     . THR B 1 399 ? 13.686  29.856  32.236  1.00 32.98  ?  385 THR B C     1 
ATOM   6966 O  O     . THR B 1 399 ? 13.058  30.552  33.038  1.00 46.18  ?  385 THR B O     1 
ATOM   6967 C  CB    . THR B 1 399 ? 15.976  29.449  33.192  1.00 40.20  ?  385 THR B CB    1 
ATOM   6968 O  OG1   . THR B 1 399 ? 16.583  30.131  32.087  1.00 35.99  ?  385 THR B OG1   1 
ATOM   6969 C  CG2   . THR B 1 399 ? 16.937  28.391  33.717  1.00 39.59  ?  385 THR B CG2   1 
ATOM   6970 N  N     . SER B 1 400 ? 13.533  29.971  30.914  1.00 28.50  ?  386 SER B N     1 
ATOM   6971 C  CA    . SER B 1 400 ? 12.597  30.935  30.342  1.00 33.70  ?  386 SER B CA    1 
ATOM   6972 C  C     . SER B 1 400 ? 11.164  30.653  30.789  1.00 41.26  ?  386 SER B C     1 
ATOM   6973 O  O     . SER B 1 400 ? 10.527  31.484  31.448  1.00 36.37  ?  386 SER B O     1 
ATOM   6974 C  CB    . SER B 1 400 ? 12.696  30.916  28.815  1.00 33.89  ?  386 SER B CB    1 
ATOM   6975 O  OG    . SER B 1 400 ? 13.838  31.630  28.368  1.00 35.65  ?  386 SER B OG    1 
ATOM   6976 N  N     . ALA B 1 401 ? 10.635  29.478  30.434  1.00 35.15  ?  387 ALA B N     1 
ATOM   6977 C  CA    . ALA B 1 401 ? 9.263   29.148  30.810  1.00 33.12  ?  387 ALA B CA    1 
ATOM   6978 C  C     . ALA B 1 401 ? 9.113   29.013  32.320  1.00 33.44  ?  387 ALA B C     1 
ATOM   6979 O  O     . ALA B 1 401 ? 8.097   29.428  32.888  1.00 34.06  ?  387 ALA B O     1 
ATOM   6980 C  CB    . ALA B 1 401 ? 8.817   27.864  30.112  1.00 37.55  ?  387 ALA B CB    1 
ATOM   6981 N  N     . PHE B 1 402 ? 10.113  28.436  32.988  1.00 38.83  ?  388 PHE B N     1 
ATOM   6982 C  CA    . PHE B 1 402 ? 9.990   28.169  34.417  1.00 38.02  ?  388 PHE B CA    1 
ATOM   6983 C  C     . PHE B 1 402 ? 10.109  29.432  35.255  1.00 40.45  ?  388 PHE B C     1 
ATOM   6984 O  O     . PHE B 1 402 ? 9.734   29.413  36.433  1.00 38.99  ?  388 PHE B O     1 
ATOM   6985 C  CB    . PHE B 1 402 ? 11.039  27.143  34.847  1.00 37.76  ?  388 PHE B CB    1 
ATOM   6986 C  CG    . PHE B 1 402 ? 10.862  25.797  34.204  1.00 51.80  ?  388 PHE B CG    1 
ATOM   6987 C  CD1   . PHE B 1 402 ? 9.640   25.430  33.661  1.00 49.26  ?  388 PHE B CD1   1 
ATOM   6988 C  CD2   . PHE B 1 402 ? 11.917  24.904  34.129  1.00 49.32  ?  388 PHE B CD2   1 
ATOM   6989 C  CE1   . PHE B 1 402 ? 9.476   24.198  33.065  1.00 59.02  ?  388 PHE B CE1   1 
ATOM   6990 C  CE2   . PHE B 1 402 ? 11.759  23.668  33.534  1.00 46.86  ?  388 PHE B CE2   1 
ATOM   6991 C  CZ    . PHE B 1 402 ? 10.539  23.314  33.002  1.00 57.11  ?  388 PHE B CZ    1 
ATOM   6992 N  N     . GLY B 1 403 ? 10.625  30.518  34.681  1.00 39.05  ?  389 GLY B N     1 
ATOM   6993 C  CA    . GLY B 1 403 ? 10.642  31.800  35.358  1.00 36.00  ?  389 GLY B CA    1 
ATOM   6994 C  C     . GLY B 1 403 ? 9.478   32.679  34.947  1.00 36.80  ?  389 GLY B C     1 
ATOM   6995 O  O     . GLY B 1 403 ? 8.933   33.422  35.767  1.00 38.60  ?  389 GLY B O     1 
ATOM   6996 N  N     . ALA B 1 404 ? 9.068   32.581  33.679  1.00 36.86  ?  390 ALA B N     1 
ATOM   6997 C  CA    . ALA B 1 404 ? 7.955   33.389  33.192  1.00 39.64  ?  390 ALA B CA    1 
ATOM   6998 C  C     . ALA B 1 404 ? 6.651   33.066  33.906  1.00 44.12  ?  390 ALA B C     1 
ATOM   6999 O  O     . ALA B 1 404 ? 5.729   33.890  33.890  1.00 33.91  ?  390 ALA B O     1 
ATOM   7000 C  CB    . ALA B 1 404 ? 7.772   33.194  31.686  1.00 31.72  ?  390 ALA B CB    1 
ATOM   7001 N  N     . ILE B 1 405 ? 6.557   31.894  34.540  1.00 38.90  ?  391 ILE B N     1 
ATOM   7002 C  CA    . ILE B 1 405 ? 5.343   31.513  35.250  1.00 45.17  ?  391 ILE B CA    1 
ATOM   7003 C  C     . ILE B 1 405 ? 5.023   32.476  36.386  1.00 44.56  ?  391 ILE B C     1 
ATOM   7004 O  O     . ILE B 1 405 ? 3.856   32.606  36.776  1.00 46.70  ?  391 ILE B O     1 
ATOM   7005 C  CB    . ILE B 1 405 ? 5.477   30.070  35.775  1.00 43.47  ?  391 ILE B CB    1 
ATOM   7006 C  CG1   . ILE B 1 405 ? 4.114   29.522  36.197  1.00 39.92  ?  391 ILE B CG1   1 
ATOM   7007 C  CG2   . ILE B 1 405 ? 6.480   30.012  36.925  1.00 42.37  ?  391 ILE B CG2   1 
ATOM   7008 C  CD1   . ILE B 1 405 ? 4.151   28.086  36.638  1.00 35.35  ?  391 ILE B CD1   1 
ATOM   7009 N  N     . ASP B 1 406 ? 6.032   33.169  36.917  1.00 44.55  ?  392 ASP B N     1 
ATOM   7010 C  CA    . ASP B 1 406 ? 5.856   34.095  38.027  1.00 44.27  ?  392 ASP B CA    1 
ATOM   7011 C  C     . ASP B 1 406 ? 5.452   35.495  37.583  1.00 45.73  ?  392 ASP B C     1 
ATOM   7012 O  O     . ASP B 1 406 ? 5.176   36.344  38.439  1.00 47.58  ?  392 ASP B O     1 
ATOM   7013 C  CB    . ASP B 1 406 ? 7.151   34.179  38.846  1.00 45.51  ?  392 ASP B CB    1 
ATOM   7014 C  CG    . ASP B 1 406 ? 7.496   32.871  39.542  1.00 40.51  ?  392 ASP B CG    1 
ATOM   7015 O  OD1   . ASP B 1 406 ? 6.598   32.264  40.160  1.00 45.52  ?  392 ASP B OD1   1 
ATOM   7016 O  OD2   . ASP B 1 406 ? 8.671   32.450  39.475  1.00 49.11  ?  392 ASP B OD2   1 
ATOM   7017 N  N     . LEU B 1 407 ? 5.413   35.760  36.280  1.00 35.82  ?  393 LEU B N     1 
ATOM   7018 C  CA    . LEU B 1 407 ? 4.952   37.053  35.798  1.00 45.14  ?  393 LEU B CA    1 
ATOM   7019 C  C     . LEU B 1 407 ? 3.462   37.224  36.080  1.00 48.78  ?  393 LEU B C     1 
ATOM   7020 O  O     . LEU B 1 407 ? 2.674   36.281  35.946  1.00 43.26  ?  393 LEU B O     1 
ATOM   7021 C  CB    . LEU B 1 407 ? 5.226   37.189  34.300  1.00 40.92  ?  393 LEU B CB    1 
ATOM   7022 C  CG    . LEU B 1 407 ? 6.689   37.293  33.864  1.00 44.98  ?  393 LEU B CG    1 
ATOM   7023 C  CD1   . LEU B 1 407 ? 6.806   37.093  32.363  1.00 38.01  ?  393 LEU B CD1   1 
ATOM   7024 C  CD2   . LEU B 1 407 ? 7.285   38.637  34.268  1.00 38.05  ?  393 LEU B CD2   1 
ATOM   7025 N  N     . ARG B 1 408 ? 3.080   38.435  36.486  1.00 43.27  ?  394 ARG B N     1 
ATOM   7026 C  CA    . ARG B 1 408 ? 1.681   38.797  36.719  1.00 37.78  ?  394 ARG B CA    1 
ATOM   7027 C  C     . ARG B 1 408 ? 1.168   39.464  35.448  1.00 40.86  ?  394 ARG B C     1 
ATOM   7028 O  O     . ARG B 1 408 ? 1.441   40.639  35.198  1.00 47.20  ?  394 ARG B O     1 
ATOM   7029 C  CB    . ARG B 1 408 ? 1.552   39.715  37.929  1.00 41.57  ?  394 ARG B CB    1 
ATOM   7030 C  CG    . ARG B 1 408 ? 0.276   39.533  38.735  1.00 58.77  ?  394 ARG B CG    1 
ATOM   7031 C  CD    . ARG B 1 408 ? 0.426   40.104  40.141  1.00 60.06  ?  394 ARG B CD    1 
ATOM   7032 N  NE    . ARG B 1 408 ? -0.815  40.678  40.648  1.00 74.52  ?  394 ARG B NE    1 
ATOM   7033 C  CZ    . ARG B 1 408 ? -1.545  40.147  41.622  1.00 81.65  ?  394 ARG B CZ    1 
ATOM   7034 N  NH1   . ARG B 1 408 ? -1.196  39.012  42.209  1.00 68.64  ?  394 ARG B NH1   1 
ATOM   7035 N  NH2   . ARG B 1 408 ? -2.652  40.771  42.018  1.00 74.18  ?  394 ARG B NH2   1 
ATOM   7036 N  N     . LEU B 1 409 ? 0.430   38.715  34.642  1.00 42.19  ?  395 LEU B N     1 
ATOM   7037 C  CA    . LEU B 1 409 ? 0.074   39.197  33.312  1.00 42.02  ?  395 LEU B CA    1 
ATOM   7038 C  C     . LEU B 1 409 ? -1.077  40.197  33.389  1.00 49.42  ?  395 LEU B C     1 
ATOM   7039 O  O     . LEU B 1 409 ? -2.083  39.928  34.053  1.00 48.01  ?  395 LEU B O     1 
ATOM   7040 C  CB    . LEU B 1 409 ? -0.303  38.034  32.402  1.00 37.18  ?  395 LEU B CB    1 
ATOM   7041 C  CG    . LEU B 1 409 ? 0.748   36.930  32.288  1.00 38.41  ?  395 LEU B CG    1 
ATOM   7042 C  CD1   . LEU B 1 409 ? 0.221   35.749  31.482  1.00 33.13  ?  395 LEU B CD1   1 
ATOM   7043 C  CD2   . LEU B 1 409 ? 2.026   37.480  31.680  1.00 36.92  ?  395 LEU B CD2   1 
ATOM   7044 N  N     . PRO B 1 410 ? -0.966  41.352  32.725  1.00 57.77  ?  396 PRO B N     1 
ATOM   7045 C  CA    . PRO B 1 410 ? -2.118  42.259  32.623  1.00 46.98  ?  396 PRO B CA    1 
ATOM   7046 C  C     . PRO B 1 410 ? -3.149  41.741  31.630  1.00 50.57  ?  396 PRO B C     1 
ATOM   7047 O  O     . PRO B 1 410 ? -3.016  40.628  31.113  1.00 52.23  ?  396 PRO B O     1 
ATOM   7048 C  CB    . PRO B 1 410 ? -1.487  43.572  32.150  1.00 39.63  ?  396 PRO B CB    1 
ATOM   7049 C  CG    . PRO B 1 410 ? -0.280  43.134  31.377  1.00 38.21  ?  396 PRO B CG    1 
ATOM   7050 C  CD    . PRO B 1 410 ? 0.232   41.893  32.057  1.00 39.25  ?  396 PRO B CD    1 
ATOM   7051 N  N     . ALA B 1 411 ? -4.169  42.543  31.344  1.00 50.58  ?  397 ALA B N     1 
ATOM   7052 C  CA    . ALA B 1 411 ? -5.246  42.114  30.465  1.00 48.28  ?  397 ALA B CA    1 
ATOM   7053 C  C     . ALA B 1 411 ? -4.766  41.975  29.024  1.00 45.87  ?  397 ALA B C     1 
ATOM   7054 O  O     . ALA B 1 411 ? -3.780  42.589  28.610  1.00 49.16  ?  397 ALA B O     1 
ATOM   7055 C  CB    . ALA B 1 411 ? -6.409  43.103  30.527  1.00 41.00  ?  397 ALA B CB    1 
ATOM   7056 N  N     . ASP B 1 412 ? -5.472  41.134  28.266  1.00 44.04  ?  398 ASP B N     1 
ATOM   7057 C  CA    . ASP B 1 412 ? -5.276  41.000  26.821  1.00 45.57  ?  398 ASP B CA    1 
ATOM   7058 C  C     . ASP B 1 412 ? -3.856  40.558  26.483  1.00 47.79  ?  398 ASP B C     1 
ATOM   7059 O  O     . ASP B 1 412 ? -3.257  41.028  25.516  1.00 41.82  ?  398 ASP B O     1 
ATOM   7060 C  CB    . ASP B 1 412 ? -5.622  42.302  26.092  1.00 41.05  ?  398 ASP B CB    1 
ATOM   7061 C  CG    . ASP B 1 412 ? -6.891  42.936  26.612  1.00 70.24  ?  398 ASP B CG    1 
ATOM   7062 O  OD1   . ASP B 1 412 ? -7.874  42.195  26.827  1.00 77.32  ?  398 ASP B OD1   1 
ATOM   7063 O  OD2   . ASP B 1 412 ? -6.909  44.173  26.805  1.00 90.39  ?  398 ASP B OD2   1 
ATOM   7064 N  N     . VAL B 1 413 ? -3.313  39.645  27.282  1.00 41.33  ?  399 VAL B N     1 
ATOM   7065 C  CA    . VAL B 1 413 ? -1.990  39.081  27.050  1.00 43.04  ?  399 VAL B CA    1 
ATOM   7066 C  C     . VAL B 1 413 ? -2.157  37.663  26.525  1.00 41.60  ?  399 VAL B C     1 
ATOM   7067 O  O     . VAL B 1 413 ? -2.848  36.842  27.140  1.00 42.29  ?  399 VAL B O     1 
ATOM   7068 C  CB    . VAL B 1 413 ? -1.137  39.104  28.330  1.00 45.27  ?  399 VAL B CB    1 
ATOM   7069 C  CG1   . VAL B 1 413 ? 0.106   38.235  28.169  1.00 41.18  ?  399 VAL B CG1   1 
ATOM   7070 C  CG2   . VAL B 1 413 ? -0.752  40.533  28.675  1.00 34.92  ?  399 VAL B CG2   1 
ATOM   7071 N  N     . ASN B 1 414 ? -1.529  37.378  25.388  1.00 38.37  ?  400 ASN B N     1 
ATOM   7072 C  CA    . ASN B 1 414 ? -1.446  36.028  24.849  1.00 35.30  ?  400 ASN B CA    1 
ATOM   7073 C  C     . ASN B 1 414 ? -0.105  35.443  25.279  1.00 46.57  ?  400 ASN B C     1 
ATOM   7074 O  O     . ASN B 1 414 ? 0.950   35.882  24.812  1.00 40.65  ?  400 ASN B O     1 
ATOM   7075 C  CB    . ASN B 1 414 ? -1.589  36.034  23.329  1.00 34.72  ?  400 ASN B CB    1 
ATOM   7076 C  CG    . ASN B 1 414 ? -1.718  34.635  22.747  1.00 38.39  ?  400 ASN B CG    1 
ATOM   7077 O  OD1   . ASN B 1 414 ? -1.413  33.644  23.410  1.00 37.94  ?  400 ASN B OD1   1 
ATOM   7078 N  ND2   . ASN B 1 414 ? -2.169  34.549  21.501  1.00 40.34  ?  400 ASN B ND2   1 
ATOM   7079 N  N     . PHE B 1 415 ? -0.150  34.456  26.169  1.00 36.06  ?  401 PHE B N     1 
ATOM   7080 C  CA    . PHE B 1 415 ? 1.036   33.836  26.752  1.00 38.13  ?  401 PHE B CA    1 
ATOM   7081 C  C     . PHE B 1 415 ? 1.170   32.449  26.136  1.00 42.93  ?  401 PHE B C     1 
ATOM   7082 O  O     . PHE B 1 415 ? 0.327   31.577  26.373  1.00 34.35  ?  401 PHE B O     1 
ATOM   7083 C  CB    . PHE B 1 415 ? 0.906   33.771  28.275  1.00 34.46  ?  401 PHE B CB    1 
ATOM   7084 C  CG    . PHE B 1 415 ? 2.125   33.244  28.981  1.00 36.04  ?  401 PHE B CG    1 
ATOM   7085 C  CD1   . PHE B 1 415 ? 2.267   31.886  29.231  1.00 34.82  ?  401 PHE B CD1   1 
ATOM   7086 C  CD2   . PHE B 1 415 ? 3.114   34.107  29.422  1.00 39.49  ?  401 PHE B CD2   1 
ATOM   7087 C  CE1   . PHE B 1 415 ? 3.381   31.396  29.893  1.00 35.69  ?  401 PHE B CE1   1 
ATOM   7088 C  CE2   . PHE B 1 415 ? 4.234   33.621  30.081  1.00 43.06  ?  401 PHE B CE2   1 
ATOM   7089 C  CZ    . PHE B 1 415 ? 4.367   32.263  30.316  1.00 31.04  ?  401 PHE B CZ    1 
ATOM   7090 N  N     . ILE B 1 416 ? 2.214   32.251  25.337  1.00 33.34  ?  402 ILE B N     1 
ATOM   7091 C  CA    . ILE B 1 416 ? 2.378   31.035  24.548  1.00 30.37  ?  402 ILE B CA    1 
ATOM   7092 C  C     . ILE B 1 416 ? 3.536   30.231  25.123  1.00 37.02  ?  402 ILE B C     1 
ATOM   7093 O  O     . ILE B 1 416 ? 4.695   30.664  25.069  1.00 31.53  ?  402 ILE B O     1 
ATOM   7094 C  CB    . ILE B 1 416 ? 2.609   31.353  23.063  1.00 30.95  ?  402 ILE B CB    1 
ATOM   7095 C  CG1   . ILE B 1 416 ? 1.315   31.871  22.427  1.00 30.03  ?  402 ILE B CG1   1 
ATOM   7096 C  CG2   . ILE B 1 416 ? 3.115   30.121  22.327  1.00 33.33  ?  402 ILE B CG2   1 
ATOM   7097 C  CD1   . ILE B 1 416 ? 1.532   32.583  21.114  1.00 29.12  ?  402 ILE B CD1   1 
ATOM   7098 N  N     . VAL B 1 417 ? 3.224   29.050  25.652  1.00 34.84  ?  403 VAL B N     1 
ATOM   7099 C  CA    . VAL B 1 417 ? 4.227   28.154  26.209  1.00 29.83  ?  403 VAL B CA    1 
ATOM   7100 C  C     . VAL B 1 417 ? 3.815   26.725  25.882  1.00 38.75  ?  403 VAL B C     1 
ATOM   7101 O  O     . VAL B 1 417 ? 2.628   26.425  25.723  1.00 27.08  ?  403 VAL B O     1 
ATOM   7102 C  CB    . VAL B 1 417 ? 4.404   28.382  27.731  1.00 30.25  ?  403 VAL B CB    1 
ATOM   7103 C  CG1   . VAL B 1 417 ? 3.191   27.884  28.508  1.00 31.85  ?  403 VAL B CG1   1 
ATOM   7104 C  CG2   . VAL B 1 417 ? 5.683   27.738  28.229  1.00 42.32  ?  403 VAL B CG2   1 
ATOM   7105 N  N     . GLN B 1 418 ? 4.806   25.840  25.764  1.00 36.83  ?  404 GLN B N     1 
ATOM   7106 C  CA    . GLN B 1 418 ? 4.598   24.469  25.295  1.00 29.14  ?  404 GLN B CA    1 
ATOM   7107 C  C     . GLN B 1 418 ? 5.213   23.492  26.293  1.00 29.13  ?  404 GLN B C     1 
ATOM   7108 O  O     . GLN B 1 418 ? 6.169   22.779  25.975  1.00 32.83  ?  404 GLN B O     1 
ATOM   7109 C  CB    . GLN B 1 418 ? 5.205   24.295  23.902  1.00 29.36  ?  404 GLN B CB    1 
ATOM   7110 C  CG    . GLN B 1 418 ? 4.835   23.008  23.171  1.00 35.62  ?  404 GLN B CG    1 
ATOM   7111 C  CD    . GLN B 1 418 ? 5.799   22.707  22.037  1.00 32.59  ?  404 GLN B CD    1 
ATOM   7112 O  OE1   . GLN B 1 418 ? 7.016   22.655  22.244  1.00 32.88  ?  404 GLN B OE1   1 
ATOM   7113 N  NE2   . GLN B 1 418 ? 5.266   22.514  20.833  1.00 26.07  ?  404 GLN B NE2   1 
ATOM   7114 N  N     . PRO B 1 419 ? 4.667   23.417  27.511  1.00 31.98  ?  405 PRO B N     1 
ATOM   7115 C  CA    . PRO B 1 419 ? 5.302   22.587  28.545  1.00 28.88  ?  405 PRO B CA    1 
ATOM   7116 C  C     . PRO B 1 419 ? 4.946   21.116  28.480  1.00 32.48  ?  405 PRO B C     1 
ATOM   7117 O  O     . PRO B 1 419 ? 5.620   20.320  29.147  1.00 30.79  ?  405 PRO B O     1 
ATOM   7118 C  CB    . PRO B 1 419 ? 4.793   23.201  29.861  1.00 34.18  ?  405 PRO B CB    1 
ATOM   7119 C  CG    . PRO B 1 419 ? 3.716   24.187  29.479  1.00 45.31  ?  405 PRO B CG    1 
ATOM   7120 C  CD    . PRO B 1 419 ? 3.449   24.064  28.008  1.00 34.00  ?  405 PRO B CD    1 
ATOM   7121 N  N     . LEU B 1 420 ? 3.905   20.724  27.741  1.00 33.74  ?  406 LEU B N     1 
ATOM   7122 C  CA    . LEU B 1 420 ? 3.594   19.302  27.630  1.00 27.80  ?  406 LEU B CA    1 
ATOM   7123 C  C     . LEU B 1 420 ? 4.492   18.630  26.600  1.00 27.83  ?  406 LEU B C     1 
ATOM   7124 O  O     . LEU B 1 420 ? 5.206   17.677  26.917  1.00 29.01  ?  406 LEU B O     1 
ATOM   7125 C  CB    . LEU B 1 420 ? 2.119   19.090  27.273  1.00 28.40  ?  406 LEU B CB    1 
ATOM   7126 C  CG    . LEU B 1 420 ? 1.748   17.641  26.921  1.00 33.34  ?  406 LEU B CG    1 
ATOM   7127 C  CD1   . LEU B 1 420 ? 2.159   16.684  28.030  1.00 29.87  ?  406 LEU B CD1   1 
ATOM   7128 C  CD2   . LEU B 1 420 ? 0.258   17.506  26.642  1.00 28.54  ?  406 LEU B CD2   1 
ATOM   7129 N  N     . TRP B 1 421 ? 4.472   19.114  25.358  1.00 27.10  ?  407 TRP B N     1 
ATOM   7130 C  CA    . TRP B 1 421 ? 5.397   18.579  24.366  1.00 35.84  ?  407 TRP B CA    1 
ATOM   7131 C  C     . TRP B 1 421 ? 6.834   18.969  24.700  1.00 30.06  ?  407 TRP B C     1 
ATOM   7132 O  O     . TRP B 1 421 ? 7.726   18.115  24.733  1.00 32.53  ?  407 TRP B O     1 
ATOM   7133 C  CB    . TRP B 1 421 ? 5.004   19.052  22.967  1.00 29.15  ?  407 TRP B CB    1 
ATOM   7134 C  CG    . TRP B 1 421 ? 5.743   18.339  21.872  1.00 37.52  ?  407 TRP B CG    1 
ATOM   7135 C  CD1   . TRP B 1 421 ? 6.483   18.911  20.874  1.00 33.18  ?  407 TRP B CD1   1 
ATOM   7136 C  CD2   . TRP B 1 421 ? 5.815   16.921  21.662  1.00 24.54  ?  407 TRP B CD2   1 
ATOM   7137 N  NE1   . TRP B 1 421 ? 7.002   17.937  20.054  1.00 31.40  ?  407 TRP B NE1   1 
ATOM   7138 C  CE2   . TRP B 1 421 ? 6.610   16.709  20.518  1.00 29.30  ?  407 TRP B CE2   1 
ATOM   7139 C  CE3   . TRP B 1 421 ? 5.287   15.813  22.332  1.00 31.12  ?  407 TRP B CE3   1 
ATOM   7140 C  CZ2   . TRP B 1 421 ? 6.893   15.429  20.030  1.00 26.73  ?  407 TRP B CZ2   1 
ATOM   7141 C  CZ3   . TRP B 1 421 ? 5.567   14.540  21.843  1.00 32.81  ?  407 TRP B CZ3   1 
ATOM   7142 C  CH2   . TRP B 1 421 ? 6.360   14.362  20.704  1.00 29.04  ?  407 TRP B CH2   1 
ATOM   7143 N  N     . GLY B 1 422 ? 7.067   20.245  24.993  1.00 28.64  ?  408 GLY B N     1 
ATOM   7144 C  CA    . GLY B 1 422 ? 8.353   20.712  25.492  1.00 26.65  ?  408 GLY B CA    1 
ATOM   7145 C  C     . GLY B 1 422 ? 9.525   20.653  24.537  1.00 29.54  ?  408 GLY B C     1 
ATOM   7146 O  O     . GLY B 1 422 ? 10.631  20.277  24.945  1.00 31.52  ?  408 GLY B O     1 
ATOM   7147 N  N     . SER B 1 423 ? 9.325   21.051  23.284  1.00 30.62  ?  409 SER B N     1 
ATOM   7148 C  CA    . SER B 1 423 ? 10.380  21.016  22.275  1.00 33.67  ?  409 SER B CA    1 
ATOM   7149 C  C     . SER B 1 423 ? 11.096  22.366  22.243  1.00 30.53  ?  409 SER B C     1 
ATOM   7150 O  O     . SER B 1 423 ? 10.518  23.370  21.815  1.00 30.63  ?  409 SER B O     1 
ATOM   7151 C  CB    . SER B 1 423 ? 9.782   20.679  20.912  1.00 26.73  ?  409 SER B CB    1 
ATOM   7152 O  OG    . SER B 1 423 ? 10.792  20.387  19.962  1.00 30.18  ?  409 SER B OG    1 
ATOM   7153 N  N     . ILE B 1 424 ? 12.364  22.393  22.664  1.00 26.75  ?  410 ILE B N     1 
ATOM   7154 C  CA    . ILE B 1 424 ? 13.103  23.651  22.645  1.00 28.95  ?  410 ILE B CA    1 
ATOM   7155 C  C     . ILE B 1 424 ? 13.373  24.055  21.201  1.00 29.26  ?  410 ILE B C     1 
ATOM   7156 O  O     . ILE B 1 424 ? 13.537  23.211  20.308  1.00 27.00  ?  410 ILE B O     1 
ATOM   7157 C  CB    . ILE B 1 424 ? 14.413  23.568  23.450  1.00 27.61  ?  410 ILE B CB    1 
ATOM   7158 C  CG1   . ILE B 1 424 ? 15.362  22.525  22.860  1.00 28.21  ?  410 ILE B CG1   1 
ATOM   7159 C  CG2   . ILE B 1 424 ? 14.135  23.283  24.920  1.00 27.09  ?  410 ILE B CG2   1 
ATOM   7160 C  CD1   . ILE B 1 424 ? 16.792  22.746  23.274  1.00 26.28  ?  410 ILE B CD1   1 
ATOM   7161 N  N     . GLY B 1 425 ? 13.404  25.366  20.966  1.00 32.12  ?  411 GLY B N     1 
ATOM   7162 C  CA    . GLY B 1 425 ? 13.406  25.925  19.635  1.00 30.61  ?  411 GLY B CA    1 
ATOM   7163 C  C     . GLY B 1 425 ? 12.031  26.316  19.133  1.00 33.78  ?  411 GLY B C     1 
ATOM   7164 O  O     . GLY B 1 425 ? 11.928  27.066  18.154  1.00 27.64  ?  411 GLY B O     1 
ATOM   7165 N  N     . TYR B 1 426 ? 10.974  25.835  19.786  1.00 31.11  ?  412 TYR B N     1 
ATOM   7166 C  CA    . TYR B 1 426 ? 9.624   26.119  19.321  1.00 29.54  ?  412 TYR B CA    1 
ATOM   7167 C  C     . TYR B 1 426 ? 9.333   27.621  19.318  1.00 29.11  ?  412 TYR B C     1 
ATOM   7168 O  O     . TYR B 1 426 ? 8.830   28.162  18.327  1.00 32.96  ?  412 TYR B O     1 
ATOM   7169 C  CB    . TYR B 1 426 ? 8.615   25.366  20.196  1.00 31.32  ?  412 TYR B CB    1 
ATOM   7170 C  CG    . TYR B 1 426 ? 7.206   25.912  20.149  1.00 24.47  ?  412 TYR B CG    1 
ATOM   7171 C  CD1   . TYR B 1 426 ? 6.327   25.521  19.149  1.00 26.78  ?  412 TYR B CD1   1 
ATOM   7172 C  CD2   . TYR B 1 426 ? 6.757   26.815  21.104  1.00 27.56  ?  412 TYR B CD2   1 
ATOM   7173 C  CE1   . TYR B 1 426 ? 5.036   26.013  19.095  1.00 33.81  ?  412 TYR B CE1   1 
ATOM   7174 C  CE2   . TYR B 1 426 ? 5.460   27.322  21.059  1.00 34.90  ?  412 TYR B CE2   1 
ATOM   7175 C  CZ    . TYR B 1 426 ? 4.608   26.917  20.052  1.00 29.69  ?  412 TYR B CZ    1 
ATOM   7176 O  OH    . TYR B 1 426 ? 3.327   27.410  19.996  1.00 27.60  ?  412 TYR B OH    1 
ATOM   7177 N  N     . THR B 1 427 ? 9.656   28.319  20.411  1.00 24.46  ?  413 THR B N     1 
ATOM   7178 C  CA    . THR B 1 427 ? 9.139   29.681  20.567  1.00 41.49  ?  413 THR B CA    1 
ATOM   7179 C  C     . THR B 1 427 ? 9.707   30.640  19.536  1.00 30.21  ?  413 THR B C     1 
ATOM   7180 O  O     . THR B 1 427 ? 8.974   31.493  19.024  1.00 31.42  ?  413 THR B O     1 
ATOM   7181 C  CB    . THR B 1 427 ? 9.384   30.216  21.965  1.00 37.90  ?  413 THR B CB    1 
ATOM   7182 O  OG1   . THR B 1 427 ? 10.567  31.018  21.987  1.00 47.19  ?  413 THR B OG1   1 
ATOM   7183 C  CG2   . THR B 1 427 ? 9.523   29.085  22.866  1.00 25.18  ?  413 THR B CG2   1 
ATOM   7184 N  N     . LEU B 1 428 ? 11.007  30.553  19.245  1.00 29.56  ?  414 LEU B N     1 
ATOM   7185 C  CA    . LEU B 1 428 ? 11.580  31.484  18.281  1.00 33.42  ?  414 LEU B CA    1 
ATOM   7186 C  C     . LEU B 1 428 ? 10.845  31.386  16.952  1.00 34.38  ?  414 LEU B C     1 
ATOM   7187 O  O     . LEU B 1 428 ? 10.431  32.402  16.381  1.00 27.20  ?  414 LEU B O     1 
ATOM   7188 C  CB    . LEU B 1 428 ? 13.071  31.210  18.098  1.00 24.49  ?  414 LEU B CB    1 
ATOM   7189 C  CG    . LEU B 1 428 ? 13.811  32.173  17.173  1.00 38.04  ?  414 LEU B CG    1 
ATOM   7190 C  CD1   . LEU B 1 428 ? 13.713  33.604  17.707  1.00 31.78  ?  414 LEU B CD1   1 
ATOM   7191 C  CD2   . LEU B 1 428 ? 15.275  31.753  17.009  1.00 28.16  ?  414 LEU B CD2   1 
ATOM   7192 N  N     . ALA B 1 429 ? 10.622  30.160  16.474  1.00 28.33  ?  415 ALA B N     1 
ATOM   7193 C  CA    . ALA B 1 429 ? 9.888   29.976  15.227  1.00 31.45  ?  415 ALA B CA    1 
ATOM   7194 C  C     . ALA B 1 429 ? 8.401   30.260  15.418  1.00 33.86  ?  415 ALA B C     1 
ATOM   7195 O  O     . ALA B 1 429 ? 7.754   30.832  14.533  1.00 31.98  ?  415 ALA B O     1 
ATOM   7196 C  CB    . ALA B 1 429 ? 10.108  28.560  14.695  1.00 26.03  ?  415 ALA B CB    1 
ATOM   7197 N  N     . ALA B 1 430 ? 7.841   29.866  16.566  1.00 24.28  ?  416 ALA B N     1 
ATOM   7198 C  CA    . ALA B 1 430 ? 6.443   30.174  16.844  1.00 28.89  ?  416 ALA B CA    1 
ATOM   7199 C  C     . ALA B 1 430 ? 6.209   31.679  16.926  1.00 34.17  ?  416 ALA B C     1 
ATOM   7200 O  O     . ALA B 1 430 ? 5.125   32.159  16.572  1.00 25.96  ?  416 ALA B O     1 
ATOM   7201 C  CB    . ALA B 1 430 ? 6.005   29.503  18.145  1.00 20.48  ?  416 ALA B CB    1 
ATOM   7202 N  N     . ALA B 1 431 ? 7.208   32.431  17.398  1.00 29.91  ?  417 ALA B N     1 
ATOM   7203 C  CA    . ALA B 1 431 ? 7.097   33.887  17.467  1.00 28.84  ?  417 ALA B CA    1 
ATOM   7204 C  C     . ALA B 1 431 ? 6.962   34.502  16.080  1.00 32.78  ?  417 ALA B C     1 
ATOM   7205 O  O     . ALA B 1 431 ? 6.205   35.462  15.885  1.00 29.96  ?  417 ALA B O     1 
ATOM   7206 C  CB    . ALA B 1 431 ? 8.309   34.468  18.189  1.00 26.89  ?  417 ALA B CB    1 
ATOM   7207 N  N     . PHE B 1 432 ? 7.711   33.983  15.111  1.00 29.51  ?  418 PHE B N     1 
ATOM   7208 C  CA    . PHE B 1 432 ? 7.533   34.422  13.733  1.00 29.19  ?  418 PHE B CA    1 
ATOM   7209 C  C     . PHE B 1 432 ? 6.100   34.182  13.265  1.00 33.02  ?  418 PHE B C     1 
ATOM   7210 O  O     . PHE B 1 432 ? 5.503   35.041  12.603  1.00 31.55  ?  418 PHE B O     1 
ATOM   7211 C  CB    . PHE B 1 432 ? 8.540   33.702  12.836  1.00 23.10  ?  418 PHE B CB    1 
ATOM   7212 C  CG    . PHE B 1 432 ? 8.322   33.926  11.373  1.00 26.02  ?  418 PHE B CG    1 
ATOM   7213 C  CD1   . PHE B 1 432 ? 8.532   35.171  10.811  1.00 21.85  ?  418 PHE B CD1   1 
ATOM   7214 C  CD2   . PHE B 1 432 ? 7.901   32.886  10.557  1.00 22.88  ?  418 PHE B CD2   1 
ATOM   7215 C  CE1   . PHE B 1 432 ? 8.334   35.376  9.466   1.00 24.94  ?  418 PHE B CE1   1 
ATOM   7216 C  CE2   . PHE B 1 432 ? 7.702   33.087  9.207   1.00 27.10  ?  418 PHE B CE2   1 
ATOM   7217 C  CZ    . PHE B 1 432 ? 7.918   34.338  8.661   1.00 22.39  ?  418 PHE B CZ    1 
ATOM   7218 N  N     . GLY B 1 433 ? 5.523   33.027  13.613  1.00 25.74  ?  419 GLY B N     1 
ATOM   7219 C  CA    . GLY B 1 433 ? 4.135   32.770  13.254  1.00 26.55  ?  419 GLY B CA    1 
ATOM   7220 C  C     . GLY B 1 433 ? 3.151   33.676  13.973  1.00 25.39  ?  419 GLY B C     1 
ATOM   7221 O  O     . GLY B 1 433 ? 2.219   34.206  13.360  1.00 25.77  ?  419 GLY B O     1 
ATOM   7222 N  N     . ALA B 1 434 ? 3.344   33.874  15.277  1.00 24.19  ?  420 ALA B N     1 
ATOM   7223 C  CA    . ALA B 1 434 ? 2.446   34.740  16.035  1.00 28.00  ?  420 ALA B CA    1 
ATOM   7224 C  C     . ALA B 1 434 ? 2.520   36.186  15.550  1.00 35.06  ?  420 ALA B C     1 
ATOM   7225 O  O     . ALA B 1 434 ? 1.488   36.857  15.412  1.00 35.14  ?  420 ALA B O     1 
ATOM   7226 C  CB    . ALA B 1 434 ? 2.775   34.660  17.525  1.00 26.61  ?  420 ALA B CB    1 
ATOM   7227 N  N     . GLN B 1 435 ? 3.734   36.689  15.298  1.00 28.73  ?  421 GLN B N     1 
ATOM   7228 C  CA    . GLN B 1 435 ? 3.875   38.053  14.796  1.00 30.46  ?  421 GLN B CA    1 
ATOM   7229 C  C     . GLN B 1 435 ? 3.234   38.196  13.422  1.00 30.96  ?  421 GLN B C     1 
ATOM   7230 O  O     . GLN B 1 435 ? 2.637   39.234  13.113  1.00 35.97  ?  421 GLN B O     1 
ATOM   7231 C  CB    . GLN B 1 435 ? 5.352   38.454  14.756  1.00 31.01  ?  421 GLN B CB    1 
ATOM   7232 C  CG    . GLN B 1 435 ? 5.599   39.918  14.381  1.00 27.93  ?  421 GLN B CG    1 
ATOM   7233 C  CD    . GLN B 1 435 ? 5.312   40.881  15.519  1.00 37.11  ?  421 GLN B CD    1 
ATOM   7234 O  OE1   . GLN B 1 435 ? 6.202   41.214  16.302  1.00 39.85  ?  421 GLN B OE1   1 
ATOM   7235 N  NE2   . GLN B 1 435 ? 4.065   41.336  15.615  1.00 35.91  ?  421 GLN B NE2   1 
ATOM   7236 N  N     . THR B 1 436 ? 3.342   37.159  12.586  1.00 27.20  ?  422 THR B N     1 
ATOM   7237 C  CA    . THR B 1 436 ? 2.635   37.149  11.309  1.00 29.09  ?  422 THR B CA    1 
ATOM   7238 C  C     . THR B 1 436 ? 1.128   37.238  11.521  1.00 36.45  ?  422 THR B C     1 
ATOM   7239 O  O     . THR B 1 436 ? 0.426   37.940  10.784  1.00 30.34  ?  422 THR B O     1 
ATOM   7240 C  CB    . THR B 1 436 ? 2.985   35.880  10.526  1.00 32.51  ?  422 THR B CB    1 
ATOM   7241 O  OG1   . THR B 1 436 ? 4.404   35.806  10.326  1.00 29.73  ?  422 THR B OG1   1 
ATOM   7242 C  CG2   . THR B 1 436 ? 2.277   35.860  9.173   1.00 29.41  ?  422 THR B CG2   1 
ATOM   7243 N  N     . ALA B 1 437 ? 0.614   36.514  12.516  1.00 32.01  ?  423 ALA B N     1 
ATOM   7244 C  CA    . ALA B 1 437 ? -0.811  36.557  12.812  1.00 34.67  ?  423 ALA B CA    1 
ATOM   7245 C  C     . ALA B 1 437 ? -1.232  37.922  13.339  1.00 35.06  ?  423 ALA B C     1 
ATOM   7246 O  O     . ALA B 1 437 ? -2.321  38.411  13.013  1.00 35.03  ?  423 ALA B O     1 
ATOM   7247 C  CB    . ALA B 1 437 ? -1.168  35.463  13.818  1.00 29.24  ?  423 ALA B CB    1 
ATOM   7248 N  N     . CYS B 1 438 ? -0.393  38.551  14.159  1.00 38.69  ?  424 CYS B N     1 
ATOM   7249 C  CA    . CYS B 1 438 ? -0.744  39.796  14.842  1.00 37.74  ?  424 CYS B CA    1 
ATOM   7250 C  C     . CYS B 1 438 ? 0.330   40.847  14.581  1.00 41.72  ?  424 CYS B C     1 
ATOM   7251 O  O     . CYS B 1 438 ? 1.128   41.179  15.467  1.00 35.23  ?  424 CYS B O     1 
ATOM   7252 C  CB    . CYS B 1 438 ? -0.930  39.544  16.339  1.00 32.32  ?  424 CYS B CB    1 
ATOM   7253 S  SG    . CYS B 1 438 ? -2.142  38.232  16.695  1.00 40.88  ?  424 CYS B SG    1 
ATOM   7254 N  N     . PRO B 1 439 ? 0.361   41.410  13.369  1.00 37.72  ?  425 PRO B N     1 
ATOM   7255 C  CA    . PRO B 1 439 ? 1.406   42.394  13.045  1.00 40.36  ?  425 PRO B CA    1 
ATOM   7256 C  C     . PRO B 1 439 ? 1.328   43.675  13.858  1.00 43.18  ?  425 PRO B C     1 
ATOM   7257 O  O     . PRO B 1 439 ? 2.331   44.394  13.932  1.00 44.91  ?  425 PRO B O     1 
ATOM   7258 C  CB    . PRO B 1 439 ? 1.180   42.670  11.552  1.00 37.74  ?  425 PRO B CB    1 
ATOM   7259 C  CG    . PRO B 1 439 ? -0.258  42.330  11.319  1.00 49.36  ?  425 PRO B CG    1 
ATOM   7260 C  CD    . PRO B 1 439 ? -0.565  41.185  12.244  1.00 38.71  ?  425 PRO B CD    1 
ATOM   7261 N  N     . ASN B 1 440 ? 0.189   43.987  14.474  1.00 40.48  ?  426 ASN B N     1 
ATOM   7262 C  CA    . ASN B 1 440 ? 0.036   45.230  15.220  1.00 56.61  ?  426 ASN B CA    1 
ATOM   7263 C  C     . ASN B 1 440 ? 0.204   45.049  16.724  1.00 48.22  ?  426 ASN B C     1 
ATOM   7264 O  O     . ASN B 1 440 ? -0.046  45.992  17.479  1.00 51.16  ?  426 ASN B O     1 
ATOM   7265 C  CB    . ASN B 1 440 ? -1.328  45.864  14.929  1.00 43.16  ?  426 ASN B CB    1 
ATOM   7266 C  CG    . ASN B 1 440 ? -1.505  46.211  13.465  1.00 50.88  ?  426 ASN B CG    1 
ATOM   7267 O  OD1   . ASN B 1 440 ? -0.543  46.551  12.774  1.00 55.22  ?  426 ASN B OD1   1 
ATOM   7268 N  ND2   . ASN B 1 440 ? -2.738  46.119  12.980  1.00 53.06  ?  426 ASN B ND2   1 
ATOM   7269 N  N     . ARG B 1 441 ? 0.618   43.871  17.176  1.00 39.18  ?  427 ARG B N     1 
ATOM   7270 C  CA    . ARG B 1 441 ? 0.811   43.606  18.593  1.00 43.05  ?  427 ARG B CA    1 
ATOM   7271 C  C     . ARG B 1 441 ? 2.292   43.434  18.902  1.00 45.54  ?  427 ARG B C     1 
ATOM   7272 O  O     . ARG B 1 441 ? 3.074   42.983  18.060  1.00 38.09  ?  427 ARG B O     1 
ATOM   7273 C  CB    . ARG B 1 441 ? 0.040   42.353  19.035  1.00 35.62  ?  427 ARG B CB    1 
ATOM   7274 C  CG    . ARG B 1 441 ? -1.471  42.476  18.876  1.00 39.33  ?  427 ARG B CG    1 
ATOM   7275 C  CD    . ARG B 1 441 ? -2.190  41.237  19.375  1.00 39.20  ?  427 ARG B CD    1 
ATOM   7276 N  NE    . ARG B 1 441 ? -1.947  40.991  20.790  1.00 39.16  ?  427 ARG B NE    1 
ATOM   7277 C  CZ    . ARG B 1 441 ? -2.642  40.137  21.529  1.00 40.68  ?  427 ARG B CZ    1 
ATOM   7278 N  NH1   . ARG B 1 441 ? -3.642  39.438  21.018  1.00 39.09  ?  427 ARG B NH1   1 
ATOM   7279 N  NH2   . ARG B 1 441 ? -2.330  39.984  22.813  1.00 37.72  ?  427 ARG B NH2   1 
ATOM   7280 N  N     . ARG B 1 442 ? 2.664   43.782  20.131  1.00 39.04  ?  428 ARG B N     1 
ATOM   7281 C  CA    . ARG B 1 442 ? 4.048   43.660  20.564  1.00 42.30  ?  428 ARG B CA    1 
ATOM   7282 C  C     . ARG B 1 442 ? 4.332   42.217  20.963  1.00 42.87  ?  428 ARG B C     1 
ATOM   7283 O  O     . ARG B 1 442 ? 3.580   41.619  21.739  1.00 38.53  ?  428 ARG B O     1 
ATOM   7284 C  CB    . ARG B 1 442 ? 4.327   44.604  21.734  1.00 30.36  ?  428 ARG B CB    1 
ATOM   7285 C  CG    . ARG B 1 442 ? 5.775   44.608  22.182  1.00 34.53  ?  428 ARG B CG    1 
ATOM   7286 C  CD    . ARG B 1 442 ? 6.052   45.712  23.190  1.00 32.66  ?  428 ARG B CD    1 
ATOM   7287 N  NE    . ARG B 1 442 ? 5.639   45.340  24.538  1.00 38.58  ?  428 ARG B NE    1 
ATOM   7288 C  CZ    . ARG B 1 442 ? 5.915   46.045  25.627  1.00 44.25  ?  428 ARG B CZ    1 
ATOM   7289 N  NH1   . ARG B 1 442 ? 6.607   47.172  25.565  1.00 39.32  ?  428 ARG B NH1   1 
ATOM   7290 N  NH2   . ARG B 1 442 ? 5.483   45.611  26.808  1.00 35.80  ?  428 ARG B NH2   1 
ATOM   7291 N  N     . VAL B 1 443 ? 5.411   41.658  20.422  1.00 38.86  ?  429 VAL B N     1 
ATOM   7292 C  CA    . VAL B 1 443 ? 5.773   40.260  20.630  1.00 31.71  ?  429 VAL B CA    1 
ATOM   7293 C  C     . VAL B 1 443 ? 7.080   40.215  21.409  1.00 36.14  ?  429 VAL B C     1 
ATOM   7294 O  O     . VAL B 1 443 ? 8.087   40.793  20.981  1.00 35.29  ?  429 VAL B O     1 
ATOM   7295 C  CB    . VAL B 1 443 ? 5.902   39.505  19.299  1.00 37.67  ?  429 VAL B CB    1 
ATOM   7296 C  CG1   . VAL B 1 443 ? 6.495   38.116  19.530  1.00 37.52  ?  429 VAL B CG1   1 
ATOM   7297 C  CG2   . VAL B 1 443 ? 4.546   39.414  18.608  1.00 34.57  ?  429 VAL B CG2   1 
ATOM   7298 N  N     . ILE B 1 444 ? 7.063   39.531  22.549  1.00 33.95  ?  430 ILE B N     1 
ATOM   7299 C  CA    . ILE B 1 444 ? 8.231   39.376  23.407  1.00 28.33  ?  430 ILE B CA    1 
ATOM   7300 C  C     . ILE B 1 444 ? 8.622   37.904  23.403  1.00 37.00  ?  430 ILE B C     1 
ATOM   7301 O  O     . ILE B 1 444 ? 7.811   37.039  23.756  1.00 34.43  ?  430 ILE B O     1 
ATOM   7302 C  CB    . ILE B 1 444 ? 7.951   39.876  24.832  1.00 32.71  ?  430 ILE B CB    1 
ATOM   7303 C  CG1   . ILE B 1 444 ? 7.649   41.380  24.808  1.00 31.50  ?  430 ILE B CG1   1 
ATOM   7304 C  CG2   . ILE B 1 444 ? 9.125   39.563  25.754  1.00 27.21  ?  430 ILE B CG2   1 
ATOM   7305 C  CD1   . ILE B 1 444 ? 6.855   41.869  26.005  1.00 28.69  ?  430 ILE B CD1   1 
ATOM   7306 N  N     . VAL B 1 445 ? 9.861   37.620  23.013  1.00 33.56  ?  431 VAL B N     1 
ATOM   7307 C  CA    . VAL B 1 445 ? 10.354  36.255  22.864  1.00 33.31  ?  431 VAL B CA    1 
ATOM   7308 C  C     . VAL B 1 445 ? 11.373  35.989  23.962  1.00 35.69  ?  431 VAL B C     1 
ATOM   7309 O  O     . VAL B 1 445 ? 12.437  36.618  23.998  1.00 34.79  ?  431 VAL B O     1 
ATOM   7310 C  CB    . VAL B 1 445 ? 10.970  36.029  21.477  1.00 33.67  ?  431 VAL B CB    1 
ATOM   7311 C  CG1   . VAL B 1 445 ? 11.264  34.554  21.259  1.00 27.41  ?  431 VAL B CG1   1 
ATOM   7312 C  CG2   . VAL B 1 445 ? 10.038  36.560  20.402  1.00 27.84  ?  431 VAL B CG2   1 
ATOM   7313 N  N     . LEU B 1 446 ? 11.061  35.043  24.841  1.00 35.73  ?  432 LEU B N     1 
ATOM   7314 C  CA    . LEU B 1 446 ? 11.967  34.621  25.906  1.00 38.29  ?  432 LEU B CA    1 
ATOM   7315 C  C     . LEU B 1 446 ? 12.463  33.224  25.557  1.00 40.42  ?  432 LEU B C     1 
ATOM   7316 O  O     . LEU B 1 446 ? 11.745  32.237  25.735  1.00 35.83  ?  432 LEU B O     1 
ATOM   7317 C  CB    . LEU B 1 446 ? 11.270  34.642  27.259  1.00 29.62  ?  432 LEU B CB    1 
ATOM   7318 C  CG    . LEU B 1 446 ? 10.558  35.957  27.559  1.00 44.00  ?  432 LEU B CG    1 
ATOM   7319 C  CD1   . LEU B 1 446 ? 9.509   35.769  28.645  1.00 34.63  ?  432 LEU B CD1   1 
ATOM   7320 C  CD2   . LEU B 1 446 ? 11.579  37.008  27.949  1.00 37.01  ?  432 LEU B CD2   1 
ATOM   7321 N  N     . THR B 1 447 ? 13.694  33.140  25.073  1.00 38.38  ?  433 THR B N     1 
ATOM   7322 C  CA    . THR B 1 447 ? 14.267  31.868  24.673  1.00 28.76  ?  433 THR B CA    1 
ATOM   7323 C  C     . THR B 1 447 ? 15.638  31.721  25.309  1.00 41.28  ?  433 THR B C     1 
ATOM   7324 O  O     . THR B 1 447 ? 16.381  32.700  25.438  1.00 33.25  ?  433 THR B O     1 
ATOM   7325 C  CB    . THR B 1 447 ? 14.381  31.762  23.145  1.00 30.91  ?  433 THR B CB    1 
ATOM   7326 O  OG1   . THR B 1 447 ? 15.076  30.557  22.798  1.00 28.53  ?  433 THR B OG1   1 
ATOM   7327 C  CG2   . THR B 1 447 ? 15.143  32.966  22.572  1.00 25.12  ?  433 THR B CG2   1 
ATOM   7328 N  N     . GLY B 1 448 ? 15.964  30.500  25.726  1.00 29.53  ?  434 GLY B N     1 
ATOM   7329 C  CA    . GLY B 1 448 ? 17.312  30.227  26.165  1.00 28.38  ?  434 GLY B CA    1 
ATOM   7330 C  C     . GLY B 1 448 ? 18.275  30.201  24.997  1.00 31.57  ?  434 GLY B C     1 
ATOM   7331 O  O     . GLY B 1 448 ? 17.880  30.108  23.832  1.00 28.31  ?  434 GLY B O     1 
ATOM   7332 N  N     . ASP B 1 449 ? 19.570  30.296  25.316  1.00 32.31  ?  435 ASP B N     1 
ATOM   7333 C  CA    . ASP B 1 449 ? 20.582  30.218  24.265  1.00 28.61  ?  435 ASP B CA    1 
ATOM   7334 C  C     . ASP B 1 449 ? 20.593  28.839  23.614  1.00 31.36  ?  435 ASP B C     1 
ATOM   7335 O  O     . ASP B 1 449 ? 20.735  28.725  22.391  1.00 35.26  ?  435 ASP B O     1 
ATOM   7336 C  CB    . ASP B 1 449 ? 21.967  30.568  24.816  1.00 26.90  ?  435 ASP B CB    1 
ATOM   7337 C  CG    . ASP B 1 449 ? 22.320  29.793  26.077  1.00 32.49  ?  435 ASP B CG    1 
ATOM   7338 O  OD1   . ASP B 1 449 ? 21.417  29.192  26.698  1.00 33.00  ?  435 ASP B OD1   1 
ATOM   7339 O  OD2   . ASP B 1 449 ? 23.508  29.793  26.454  1.00 31.68  ?  435 ASP B OD2   1 
ATOM   7340 N  N     . GLY B 1 450 ? 20.441  27.778  24.409  1.00 28.73  ?  436 GLY B N     1 
ATOM   7341 C  CA    . GLY B 1 450 ? 20.376  26.448  23.823  1.00 30.48  ?  436 GLY B CA    1 
ATOM   7342 C  C     . GLY B 1 450 ? 19.205  26.296  22.870  1.00 27.39  ?  436 GLY B C     1 
ATOM   7343 O  O     . GLY B 1 450 ? 19.368  25.848  21.733  1.00 30.48  ?  436 GLY B O     1 
ATOM   7344 N  N     . ALA B 1 451 ? 18.017  26.731  23.301  1.00 31.91  ?  437 ALA B N     1 
ATOM   7345 C  CA    . ALA B 1 451 ? 16.814  26.550  22.489  1.00 27.82  ?  437 ALA B CA    1 
ATOM   7346 C  C     . ALA B 1 451 ? 16.905  27.308  21.170  1.00 29.98  ?  437 ALA B C     1 
ATOM   7347 O  O     . ALA B 1 451 ? 16.548  26.775  20.113  1.00 26.69  ?  437 ALA B O     1 
ATOM   7348 C  CB    . ALA B 1 451 ? 15.581  27.004  23.274  1.00 24.98  ?  437 ALA B CB    1 
ATOM   7349 N  N     . ALA B 1 452 ? 17.407  28.547  21.207  1.00 33.02  ?  438 ALA B N     1 
ATOM   7350 C  CA    . ALA B 1 452 ? 17.428  29.382  20.008  1.00 31.66  ?  438 ALA B CA    1 
ATOM   7351 C  C     . ALA B 1 452 ? 18.309  28.794  18.911  1.00 25.99  ?  438 ALA B C     1 
ATOM   7352 O  O     . ALA B 1 452 ? 18.071  29.047  17.724  1.00 28.86  ?  438 ALA B O     1 
ATOM   7353 C  CB    . ALA B 1 452 ? 17.890  30.797  20.366  1.00 27.47  ?  438 ALA B CB    1 
ATOM   7354 N  N     . GLN B 1 453 ? 19.329  28.011  19.279  1.00 26.36  ?  439 GLN B N     1 
ATOM   7355 C  CA    . GLN B 1 453 ? 20.190  27.399  18.269  1.00 26.84  ?  439 GLN B CA    1 
ATOM   7356 C  C     . GLN B 1 453 ? 19.421  26.439  17.369  1.00 29.72  ?  439 GLN B C     1 
ATOM   7357 O  O     . GLN B 1 453 ? 19.776  26.268  16.196  1.00 30.08  ?  439 GLN B O     1 
ATOM   7358 C  CB    . GLN B 1 453 ? 21.356  26.668  18.937  1.00 31.03  ?  439 GLN B CB    1 
ATOM   7359 C  CG    . GLN B 1 453 ? 22.209  27.539  19.848  1.00 25.62  ?  439 GLN B CG    1 
ATOM   7360 C  CD    . GLN B 1 453 ? 23.515  26.869  20.212  1.00 33.63  ?  439 GLN B CD    1 
ATOM   7361 O  OE1   . GLN B 1 453 ? 23.610  25.639  20.219  1.00 33.71  ?  439 GLN B OE1   1 
ATOM   7362 N  NE2   . GLN B 1 453 ? 24.529  27.669  20.525  1.00 26.69  ?  439 GLN B NE2   1 
ATOM   7363 N  N     . LEU B 1 454 ? 18.372  25.800  17.894  1.00 30.16  ?  440 LEU B N     1 
ATOM   7364 C  CA    . LEU B 1 454 ? 17.682  24.759  17.136  1.00 27.93  ?  440 LEU B CA    1 
ATOM   7365 C  C     . LEU B 1 454 ? 16.897  25.322  15.958  1.00 30.63  ?  440 LEU B C     1 
ATOM   7366 O  O     . LEU B 1 454 ? 16.676  24.608  14.971  1.00 28.24  ?  440 LEU B O     1 
ATOM   7367 C  CB    . LEU B 1 454 ? 16.758  23.962  18.059  1.00 22.67  ?  440 LEU B CB    1 
ATOM   7368 C  CG    . LEU B 1 454 ? 17.469  22.835  18.818  1.00 28.09  ?  440 LEU B CG    1 
ATOM   7369 C  CD1   . LEU B 1 454 ? 18.192  23.379  20.042  1.00 20.40  ?  440 LEU B CD1   1 
ATOM   7370 C  CD2   . LEU B 1 454 ? 16.504  21.712  19.198  1.00 24.86  ?  440 LEU B CD2   1 
ATOM   7371 N  N     . THR B 1 455 ? 16.459  26.586  16.036  1.00 27.61  ?  441 THR B N     1 
ATOM   7372 C  CA    . THR B 1 455 ? 15.587  27.165  15.019  1.00 26.86  ?  441 THR B CA    1 
ATOM   7373 C  C     . THR B 1 455 ? 16.054  28.555  14.588  1.00 28.47  ?  441 THR B C     1 
ATOM   7374 O  O     . THR B 1 455 ? 15.249  29.365  14.121  1.00 28.57  ?  441 THR B O     1 
ATOM   7375 C  CB    . THR B 1 455 ? 14.148  27.239  15.529  1.00 31.57  ?  441 THR B CB    1 
ATOM   7376 O  OG1   . THR B 1 455 ? 14.114  28.031  16.725  1.00 29.76  ?  441 THR B OG1   1 
ATOM   7377 C  CG2   . THR B 1 455 ? 13.603  25.845  15.829  1.00 28.12  ?  441 THR B CG2   1 
ATOM   7378 N  N     . ILE B 1 456 ? 17.353  28.833  14.700  1.00 27.12  ?  442 ILE B N     1 
ATOM   7379 C  CA    . ILE B 1 456 ? 17.851  30.204  14.559  1.00 30.38  ?  442 ILE B CA    1 
ATOM   7380 C  C     . ILE B 1 456 ? 17.568  30.786  13.178  1.00 24.66  ?  442 ILE B C     1 
ATOM   7381 O  O     . ILE B 1 456 ? 17.468  32.009  13.028  1.00 26.68  ?  442 ILE B O     1 
ATOM   7382 C  CB    . ILE B 1 456 ? 19.359  30.255  14.883  1.00 26.26  ?  442 ILE B CB    1 
ATOM   7383 C  CG1   . ILE B 1 456 ? 19.818  31.700  15.104  1.00 23.25  ?  442 ILE B CG1   1 
ATOM   7384 C  CG2   . ILE B 1 456 ? 20.163  29.600  13.772  1.00 26.23  ?  442 ILE B CG2   1 
ATOM   7385 C  CD1   . ILE B 1 456 ? 18.999  32.462  16.128  1.00 28.32  ?  442 ILE B CD1   1 
ATOM   7386 N  N     . GLN B 1 457 ? 17.451  29.944  12.147  1.00 29.39  ?  443 GLN B N     1 
ATOM   7387 C  CA    . GLN B 1 457 ? 17.328  30.473  10.792  1.00 26.20  ?  443 GLN B CA    1 
ATOM   7388 C  C     . GLN B 1 457 ? 16.022  31.234  10.576  1.00 31.18  ?  443 GLN B C     1 
ATOM   7389 O  O     . GLN B 1 457 ? 15.932  32.043  9.643   1.00 25.42  ?  443 GLN B O     1 
ATOM   7390 C  CB    . GLN B 1 457 ? 17.468  29.343  9.764   1.00 24.08  ?  443 GLN B CB    1 
ATOM   7391 C  CG    . GLN B 1 457 ? 16.612  28.104  10.038  1.00 29.27  ?  443 GLN B CG    1 
ATOM   7392 C  CD    . GLN B 1 457 ? 17.350  27.052  10.837  1.00 22.84  ?  443 GLN B CD    1 
ATOM   7393 O  OE1   . GLN B 1 457 ? 17.120  26.902  12.035  1.00 24.84  ?  443 GLN B OE1   1 
ATOM   7394 N  NE2   . GLN B 1 457 ? 18.266  26.336  10.184  1.00 19.74  ?  443 GLN B NE2   1 
ATOM   7395 N  N     . GLU B 1 458 ? 15.019  31.019  11.427  1.00 29.92  ?  444 GLU B N     1 
ATOM   7396 C  CA    . GLU B 1 458 ? 13.762  31.735  11.255  1.00 35.92  ?  444 GLU B CA    1 
ATOM   7397 C  C     . GLU B 1 458 ? 13.871  33.201  11.655  1.00 36.48  ?  444 GLU B C     1 
ATOM   7398 O  O     . GLU B 1 458 ? 13.009  33.998  11.272  1.00 26.54  ?  444 GLU B O     1 
ATOM   7399 C  CB    . GLU B 1 458 ? 12.647  31.043  12.041  1.00 24.53  ?  444 GLU B CB    1 
ATOM   7400 C  CG    . GLU B 1 458 ? 11.362  30.849  11.231  1.00 26.60  ?  444 GLU B CG    1 
ATOM   7401 C  CD    . GLU B 1 458 ? 11.607  30.266  9.836   1.00 33.57  ?  444 GLU B CD    1 
ATOM   7402 O  OE1   . GLU B 1 458 ? 12.489  29.390  9.680   1.00 31.03  ?  444 GLU B OE1   1 
ATOM   7403 O  OE2   . GLU B 1 458 ? 10.900  30.673  8.889   1.00 33.75  ?  444 GLU B OE2   1 
ATOM   7404 N  N     . LEU B 1 459 ? 14.910  33.577  12.406  1.00 29.29  ?  445 LEU B N     1 
ATOM   7405 C  CA    . LEU B 1 459 ? 15.177  34.995  12.618  1.00 29.37  ?  445 LEU B CA    1 
ATOM   7406 C  C     . LEU B 1 459 ? 15.380  35.710  11.287  1.00 31.49  ?  445 LEU B C     1 
ATOM   7407 O  O     . LEU B 1 459 ? 14.951  36.855  11.115  1.00 32.92  ?  445 LEU B O     1 
ATOM   7408 C  CB    . LEU B 1 459 ? 16.391  35.173  13.525  1.00 34.12  ?  445 LEU B CB    1 
ATOM   7409 C  CG    . LEU B 1 459 ? 16.897  36.602  13.708  1.00 45.28  ?  445 LEU B CG    1 
ATOM   7410 C  CD1   . LEU B 1 459 ? 15.793  37.501  14.256  1.00 39.28  ?  445 LEU B CD1   1 
ATOM   7411 C  CD2   . LEU B 1 459 ? 18.110  36.612  14.624  1.00 38.91  ?  445 LEU B CD2   1 
ATOM   7412 N  N     . GLY B 1 460 ? 16.001  35.034  10.319  1.00 29.27  ?  446 GLY B N     1 
ATOM   7413 C  CA    . GLY B 1 460 ? 16.086  35.600  8.983   1.00 28.45  ?  446 GLY B CA    1 
ATOM   7414 C  C     . GLY B 1 460 ? 14.719  35.849  8.371   1.00 35.44  ?  446 GLY B C     1 
ATOM   7415 O  O     . GLY B 1 460 ? 14.514  36.849  7.677   1.00 29.12  ?  446 GLY B O     1 
ATOM   7416 N  N     . SER B 1 461 ? 13.767  34.934  8.607   1.00 26.00  ?  447 SER B N     1 
ATOM   7417 C  CA    . SER B 1 461 ? 12.398  35.149  8.140   1.00 29.00  ?  447 SER B CA    1 
ATOM   7418 C  C     . SER B 1 461 ? 11.776  36.371  8.799   1.00 26.93  ?  447 SER B C     1 
ATOM   7419 O  O     . SER B 1 461 ? 11.135  37.188  8.129   1.00 25.85  ?  447 SER B O     1 
ATOM   7420 C  CB    . SER B 1 461 ? 11.539  33.912  8.423   1.00 29.51  ?  447 SER B CB    1 
ATOM   7421 O  OG    . SER B 1 461 ? 11.995  32.784  7.698   1.00 30.20  ?  447 SER B OG    1 
ATOM   7422 N  N     . MET B 1 462 ? 11.978  36.523  10.109  1.00 23.83  ?  448 MET B N     1 
ATOM   7423 C  CA    . MET B 1 462 ? 11.505  37.710  10.809  1.00 24.39  ?  448 MET B CA    1 
ATOM   7424 C  C     . MET B 1 462 ? 12.030  38.975  10.144  1.00 30.76  ?  448 MET B C     1 
ATOM   7425 O  O     . MET B 1 462 ? 11.270  39.912  9.871   1.00 28.29  ?  448 MET B O     1 
ATOM   7426 C  CB    . MET B 1 462 ? 11.949  37.654  12.270  1.00 32.23  ?  448 MET B CB    1 
ATOM   7427 C  CG    . MET B 1 462 ? 11.400  36.478  13.057  1.00 29.01  ?  448 MET B CG    1 
ATOM   7428 S  SD    . MET B 1 462 ? 11.990  36.549  14.759  1.00 32.72  ?  448 MET B SD    1 
ATOM   7429 C  CE    . MET B 1 462 ? 10.878  35.404  15.554  1.00 25.09  ?  448 MET B CE    1 
ATOM   7430 N  N     . LEU B 1 463 ? 13.334  39.013  9.867   1.00 28.76  ?  449 LEU B N     1 
ATOM   7431 C  CA    . LEU B 1 463 ? 13.929  40.205  9.272   1.00 26.90  ?  449 LEU B CA    1 
ATOM   7432 C  C     . LEU B 1 463 ? 13.454  40.414  7.839   1.00 30.61  ?  449 LEU B C     1 
ATOM   7433 O  O     . LEU B 1 463 ? 13.168  41.548  7.437   1.00 28.86  ?  449 LEU B O     1 
ATOM   7434 C  CB    . LEU B 1 463 ? 15.453  40.109  9.339   1.00 30.16  ?  449 LEU B CB    1 
ATOM   7435 C  CG    . LEU B 1 463 ? 16.035  40.082  10.756  1.00 28.90  ?  449 LEU B CG    1 
ATOM   7436 C  CD1   . LEU B 1 463 ? 17.387  39.378  10.784  1.00 31.55  ?  449 LEU B CD1   1 
ATOM   7437 C  CD2   . LEU B 1 463 ? 16.144  41.508  11.323  1.00 24.51  ?  449 LEU B CD2   1 
ATOM   7438 N  N     . ARG B 1 464 ? 13.327  39.335  7.060   1.00 26.05  ?  450 ARG B N     1 
ATOM   7439 C  CA    . ARG B 1 464 ? 12.856  39.482  5.684   1.00 33.17  ?  450 ARG B CA    1 
ATOM   7440 C  C     . ARG B 1 464 ? 11.466  40.106  5.645   1.00 36.99  ?  450 ARG B C     1 
ATOM   7441 O  O     . ARG B 1 464 ? 11.176  40.945  4.783   1.00 30.65  ?  450 ARG B O     1 
ATOM   7442 C  CB    . ARG B 1 464 ? 12.847  38.127  4.975   1.00 30.86  ?  450 ARG B CB    1 
ATOM   7443 C  CG    . ARG B 1 464 ? 12.326  38.169  3.536   1.00 31.81  ?  450 ARG B CG    1 
ATOM   7444 C  CD    . ARG B 1 464 ? 11.768  36.806  3.092   1.00 27.85  ?  450 ARG B CD    1 
ATOM   7445 N  NE    . ARG B 1 464 ? 10.683  36.349  3.954   1.00 30.79  ?  450 ARG B NE    1 
ATOM   7446 C  CZ    . ARG B 1 464 ? 10.336  35.076  4.112   1.00 40.96  ?  450 ARG B CZ    1 
ATOM   7447 N  NH1   . ARG B 1 464 ? 10.959  34.103  3.466   1.00 35.68  ?  450 ARG B NH1   1 
ATOM   7448 N  NH2   . ARG B 1 464 ? 9.345   34.771  4.944   1.00 28.59  ?  450 ARG B NH2   1 
ATOM   7449 N  N     . ASP B 1 465 ? 10.607  39.733  6.585   1.00 28.86  ?  451 ASP B N     1 
ATOM   7450 C  CA    . ASP B 1 465 ? 9.240   40.224  6.631   1.00 31.73  ?  451 ASP B CA    1 
ATOM   7451 C  C     . ASP B 1 465 ? 9.104   41.493  7.466   1.00 28.99  ?  451 ASP B C     1 
ATOM   7452 O  O     . ASP B 1 465 ? 7.982   41.946  7.706   1.00 36.17  ?  451 ASP B O     1 
ATOM   7453 C  CB    . ASP B 1 465 ? 8.317   39.127  7.165   1.00 24.09  ?  451 ASP B CB    1 
ATOM   7454 C  CG    . ASP B 1 465 ? 8.275   37.909  6.255   1.00 33.37  ?  451 ASP B CG    1 
ATOM   7455 O  OD1   . ASP B 1 465 ? 8.722   38.022  5.091   1.00 28.77  ?  451 ASP B OD1   1 
ATOM   7456 O  OD2   . ASP B 1 465 ? 7.791   36.844  6.696   1.00 31.61  ?  451 ASP B OD2   1 
ATOM   7457 N  N     . LYS B 1 466 ? 10.228  42.071  7.898   1.00 33.46  ?  452 LYS B N     1 
ATOM   7458 C  CA    . LYS B 1 466 ? 10.273  43.353  8.606   1.00 34.46  ?  452 LYS B CA    1 
ATOM   7459 C  C     . LYS B 1 466 ? 9.495   43.313  9.919   1.00 43.66  ?  452 LYS B C     1 
ATOM   7460 O  O     . LYS B 1 466 ? 8.880   44.302  10.324  1.00 38.76  ?  452 LYS B O     1 
ATOM   7461 C  CB    . LYS B 1 466 ? 9.781   44.505  7.720   1.00 30.63  ?  452 LYS B CB    1 
ATOM   7462 C  CG    . LYS B 1 466 ? 10.737  44.886  6.589   1.00 43.79  ?  452 LYS B CG    1 
ATOM   7463 C  CD    . LYS B 1 466 ? 12.202  44.991  7.057   1.00 53.55  ?  452 LYS B CD    1 
ATOM   7464 C  CE    . LYS B 1 466 ? 12.404  45.982  8.212   1.00 68.38  ?  452 LYS B CE    1 
ATOM   7465 N  NZ    . LYS B 1 466 ? 13.689  46.735  8.106   1.00 63.85  ?  452 LYS B NZ    1 
ATOM   7466 N  N     . GLN B 1 467 ? 9.541   42.171  10.602  1.00 34.01  ?  453 GLN B N     1 
ATOM   7467 C  CA    . GLN B 1 467 ? 8.938   42.076  11.923  1.00 36.66  ?  453 GLN B CA    1 
ATOM   7468 C  C     . GLN B 1 467 ? 9.799   42.787  12.967  1.00 38.44  ?  453 GLN B C     1 
ATOM   7469 O  O     . GLN B 1 467 ? 11.023  42.903  12.831  1.00 30.88  ?  453 GLN B O     1 
ATOM   7470 C  CB    . GLN B 1 467 ? 8.751   40.616  12.320  1.00 26.66  ?  453 GLN B CB    1 
ATOM   7471 C  CG    . GLN B 1 467 ? 7.898   39.811  11.362  1.00 33.79  ?  453 GLN B CG    1 
ATOM   7472 C  CD    . GLN B 1 467 ? 7.540   38.466  11.939  1.00 30.60  ?  453 GLN B CD    1 
ATOM   7473 O  OE1   . GLN B 1 467 ? 8.280   37.920  12.757  1.00 30.05  ?  453 GLN B OE1   1 
ATOM   7474 N  NE2   . GLN B 1 467 ? 6.395   37.928  11.535  1.00 28.00  ?  453 GLN B NE2   1 
ATOM   7475 N  N     . HIS B 1 468 ? 9.150   43.225  14.049  1.00 31.68  ?  454 HIS B N     1 
ATOM   7476 C  CA    . HIS B 1 468 ? 9.830   43.931  15.138  1.00 29.22  ?  454 HIS B CA    1 
ATOM   7477 C  C     . HIS B 1 468 ? 9.527   43.296  16.495  1.00 31.89  ?  454 HIS B C     1 
ATOM   7478 O  O     . HIS B 1 468 ? 9.017   43.963  17.400  1.00 31.15  ?  454 HIS B O     1 
ATOM   7479 C  CB    . HIS B 1 468 ? 9.434   45.408  15.149  1.00 33.07  ?  454 HIS B CB    1 
ATOM   7480 C  CG    . HIS B 1 468 ? 9.600   46.103  13.830  1.00 41.33  ?  454 HIS B CG    1 
ATOM   7481 N  ND1   . HIS B 1 468 ? 8.742   47.094  13.402  1.00 41.32  ?  454 HIS B ND1   1 
ATOM   7482 C  CD2   . HIS B 1 468 ? 10.526  45.961  12.851  1.00 39.08  ?  454 HIS B CD2   1 
ATOM   7483 C  CE1   . HIS B 1 468 ? 9.124   47.525  12.213  1.00 35.00  ?  454 HIS B CE1   1 
ATOM   7484 N  NE2   . HIS B 1 468 ? 10.208  46.858  11.858  1.00 43.18  ?  454 HIS B NE2   1 
ATOM   7485 N  N     . PRO B 1 469 ? 9.867   42.021  16.691  1.00 33.79  ?  455 PRO B N     1 
ATOM   7486 C  CA    . PRO B 1 469 ? 9.739   41.426  18.024  1.00 32.94  ?  455 PRO B CA    1 
ATOM   7487 C  C     . PRO B 1 469 ? 10.879  41.868  18.930  1.00 40.42  ?  455 PRO B C     1 
ATOM   7488 O  O     . PRO B 1 469 ? 11.943  42.292  18.477  1.00 34.47  ?  455 PRO B O     1 
ATOM   7489 C  CB    . PRO B 1 469 ? 9.826   39.921  17.745  1.00 39.27  ?  455 PRO B CB    1 
ATOM   7490 C  CG    . PRO B 1 469 ? 10.777  39.841  16.605  1.00 32.22  ?  455 PRO B CG    1 
ATOM   7491 C  CD    . PRO B 1 469 ? 10.484  41.068  15.745  1.00 42.78  ?  455 PRO B CD    1 
ATOM   7492 N  N     . ILE B 1 470 ? 10.658  41.707  20.230  1.00 31.42  ?  456 ILE B N     1 
ATOM   7493 C  CA    . ILE B 1 470 ? 11.684  41.947  21.237  1.00 33.50  ?  456 ILE B CA    1 
ATOM   7494 C  C     . ILE B 1 470 ? 12.172  40.576  21.694  1.00 34.86  ?  456 ILE B C     1 
ATOM   7495 O  O     . ILE B 1 470 ? 11.484  39.876  22.443  1.00 40.71  ?  456 ILE B O     1 
ATOM   7496 C  CB    . ILE B 1 470 ? 11.149  42.790  22.398  1.00 34.51  ?  456 ILE B CB    1 
ATOM   7497 C  CG1   . ILE B 1 470 ? 10.779  44.191  21.904  1.00 33.68  ?  456 ILE B CG1   1 
ATOM   7498 C  CG2   . ILE B 1 470 ? 12.168  42.869  23.526  1.00 33.41  ?  456 ILE B CG2   1 
ATOM   7499 C  CD1   . ILE B 1 470 ? 9.824   44.924  22.814  1.00 44.44  ?  456 ILE B CD1   1 
ATOM   7500 N  N     . ILE B 1 471 ? 13.359  40.184  21.235  1.00 34.15  ?  457 ILE B N     1 
ATOM   7501 C  CA    . ILE B 1 471 ? 13.896  38.842  21.457  1.00 26.83  ?  457 ILE B CA    1 
ATOM   7502 C  C     . ILE B 1 471 ? 14.908  38.901  22.589  1.00 31.92  ?  457 ILE B C     1 
ATOM   7503 O  O     . ILE B 1 471 ? 15.967  39.523  22.452  1.00 32.54  ?  457 ILE B O     1 
ATOM   7504 C  CB    . ILE B 1 471 ? 14.550  38.279  20.185  1.00 29.79  ?  457 ILE B CB    1 
ATOM   7505 C  CG1   . ILE B 1 471 ? 13.534  38.145  19.054  1.00 35.57  ?  457 ILE B CG1   1 
ATOM   7506 C  CG2   . ILE B 1 471 ? 15.208  36.930  20.470  1.00 33.66  ?  457 ILE B CG2   1 
ATOM   7507 C  CD1   . ILE B 1 471 ? 14.173  38.070  17.686  1.00 31.86  ?  457 ILE B CD1   1 
ATOM   7508 N  N     . LEU B 1 472 ? 14.608  38.227  23.693  1.00 27.99  ?  458 LEU B N     1 
ATOM   7509 C  CA    . LEU B 1 472 ? 15.517  38.142  24.829  1.00 30.31  ?  458 LEU B CA    1 
ATOM   7510 C  C     . LEU B 1 472 ? 16.116  36.743  24.862  1.00 35.27  ?  458 LEU B C     1 
ATOM   7511 O  O     . LEU B 1 472 ? 15.399  35.758  25.067  1.00 35.57  ?  458 LEU B O     1 
ATOM   7512 C  CB    . LEU B 1 472 ? 14.801  38.475  26.135  1.00 30.79  ?  458 LEU B CB    1 
ATOM   7513 C  CG    . LEU B 1 472 ? 14.313  39.925  26.233  1.00 36.46  ?  458 LEU B CG    1 
ATOM   7514 C  CD1   . LEU B 1 472 ? 12.807  40.012  26.035  1.00 35.80  ?  458 LEU B CD1   1 
ATOM   7515 C  CD2   . LEU B 1 472 ? 14.728  40.566  27.553  1.00 37.85  ?  458 LEU B CD2   1 
ATOM   7516 N  N     . VAL B 1 473 ? 17.426  36.656  24.647  1.00 34.97  ?  459 VAL B N     1 
ATOM   7517 C  CA    . VAL B 1 473 ? 18.147  35.390  24.682  1.00 34.09  ?  459 VAL B CA    1 
ATOM   7518 C  C     . VAL B 1 473 ? 18.810  35.263  26.044  1.00 33.87  ?  459 VAL B C     1 
ATOM   7519 O  O     . VAL B 1 473 ? 19.679  36.070  26.400  1.00 28.31  ?  459 VAL B O     1 
ATOM   7520 C  CB    . VAL B 1 473 ? 19.179  35.297  23.550  1.00 30.54  ?  459 VAL B CB    1 
ATOM   7521 C  CG1   . VAL B 1 473 ? 19.889  33.954  23.605  1.00 32.42  ?  459 VAL B CG1   1 
ATOM   7522 C  CG2   . VAL B 1 473 ? 18.494  35.488  22.207  1.00 25.09  ?  459 VAL B CG2   1 
ATOM   7523 N  N     . LEU B 1 474 ? 18.395  34.259  26.812  1.00 28.85  ?  460 LEU B N     1 
ATOM   7524 C  CA    . LEU B 1 474 ? 18.951  34.027  28.145  1.00 33.90  ?  460 LEU B CA    1 
ATOM   7525 C  C     . LEU B 1 474 ? 20.260  33.269  27.970  1.00 38.58  ?  460 LEU B C     1 
ATOM   7526 O  O     . LEU B 1 474 ? 20.284  32.043  27.841  1.00 37.93  ?  460 LEU B O     1 
ATOM   7527 C  CB    . LEU B 1 474 ? 17.963  33.269  29.025  1.00 32.56  ?  460 LEU B CB    1 
ATOM   7528 C  CG    . LEU B 1 474 ? 16.885  34.099  29.742  1.00 41.45  ?  460 LEU B CG    1 
ATOM   7529 C  CD1   . LEU B 1 474 ? 15.943  34.780  28.758  1.00 41.06  ?  460 LEU B CD1   1 
ATOM   7530 C  CD2   . LEU B 1 474 ? 16.086  33.257  30.730  1.00 32.09  ?  460 LEU B CD2   1 
ATOM   7531 N  N     . ASN B 1 475 ? 21.366  34.016  27.935  1.00 33.39  ?  461 ASN B N     1 
ATOM   7532 C  CA    . ASN B 1 475 ? 22.688  33.434  27.704  1.00 35.73  ?  461 ASN B CA    1 
ATOM   7533 C  C     . ASN B 1 475 ? 23.295  33.037  29.043  1.00 37.91  ?  461 ASN B C     1 
ATOM   7534 O  O     . ASN B 1 475 ? 23.954  33.834  29.712  1.00 39.86  ?  461 ASN B O     1 
ATOM   7535 C  CB    . ASN B 1 475 ? 23.592  34.407  26.954  1.00 33.96  ?  461 ASN B CB    1 
ATOM   7536 C  CG    . ASN B 1 475 ? 24.900  33.765  26.501  1.00 42.90  ?  461 ASN B CG    1 
ATOM   7537 O  OD1   . ASN B 1 475 ? 25.224  32.638  26.885  1.00 42.02  ?  461 ASN B OD1   1 
ATOM   7538 N  ND2   . ASN B 1 475 ? 25.660  34.485  25.684  1.00 35.62  ?  461 ASN B ND2   1 
ATOM   7539 N  N     . ASN B 1 476 ? 23.072  31.781  29.436  1.00 32.62  ?  462 ASN B N     1 
ATOM   7540 C  CA    . ASN B 1 476 ? 23.759  31.185  30.574  1.00 33.84  ?  462 ASN B CA    1 
ATOM   7541 C  C     . ASN B 1 476 ? 24.801  30.165  30.128  1.00 33.80  ?  462 ASN B C     1 
ATOM   7542 O  O     . ASN B 1 476 ? 25.232  29.333  30.930  1.00 35.92  ?  462 ASN B O     1 
ATOM   7543 C  CB    . ASN B 1 476 ? 22.763  30.551  31.547  1.00 32.76  ?  462 ASN B CB    1 
ATOM   7544 C  CG    . ASN B 1 476 ? 21.684  29.749  30.845  1.00 35.45  ?  462 ASN B CG    1 
ATOM   7545 O  OD1   . ASN B 1 476 ? 21.943  29.075  29.847  1.00 35.63  ?  462 ASN B OD1   1 
ATOM   7546 N  ND2   . ASN B 1 476 ? 20.462  29.818  31.365  1.00 38.39  ?  462 ASN B ND2   1 
ATOM   7547 N  N     . GLU B 1 477 ? 25.184  30.199  28.850  1.00 36.30  ?  463 GLU B N     1 
ATOM   7548 C  CA    . GLU B 1 477 ? 26.231  29.348  28.282  1.00 34.83  ?  463 GLU B CA    1 
ATOM   7549 C  C     . GLU B 1 477 ? 25.949  27.863  28.519  1.00 40.52  ?  463 GLU B C     1 
ATOM   7550 O  O     . GLU B 1 477 ? 26.728  27.149  29.155  1.00 38.38  ?  463 GLU B O     1 
ATOM   7551 C  CB    . GLU B 1 477 ? 27.610  29.721  28.830  1.00 30.76  ?  463 GLU B CB    1 
ATOM   7552 C  CG    . GLU B 1 477 ? 27.856  31.194  28.983  1.00 47.03  ?  463 GLU B CG    1 
ATOM   7553 C  CD    . GLU B 1 477 ? 29.300  31.478  29.306  1.00 56.30  ?  463 GLU B CD    1 
ATOM   7554 O  OE1   . GLU B 1 477 ? 29.679  31.335  30.489  1.00 56.99  ?  463 GLU B OE1   1 
ATOM   7555 O  OE2   . GLU B 1 477 ? 30.054  31.830  28.376  1.00 58.65  ?  463 GLU B OE2   1 
ATOM   7556 N  N     . GLY B 1 478 ? 24.827  27.404  27.989  1.00 35.24  ?  464 GLY B N     1 
ATOM   7557 C  CA    . GLY B 1 478 ? 24.563  25.987  27.971  1.00 34.85  ?  464 GLY B CA    1 
ATOM   7558 C  C     . GLY B 1 478 ? 23.139  25.686  28.371  1.00 32.27  ?  464 GLY B C     1 
ATOM   7559 O  O     . GLY B 1 478 ? 22.281  26.567  28.404  1.00 30.41  ?  464 GLY B O     1 
ATOM   7560 N  N     . TYR B 1 479 ? 22.911  24.411  28.680  1.00 31.96  ?  465 TYR B N     1 
ATOM   7561 C  CA    . TYR B 1 479 ? 21.594  23.896  29.046  1.00 35.14  ?  465 TYR B CA    1 
ATOM   7562 C  C     . TYR B 1 479 ? 21.477  23.928  30.564  1.00 34.76  ?  465 TYR B C     1 
ATOM   7563 O  O     . TYR B 1 479 ? 21.723  22.932  31.246  1.00 35.84  ?  465 TYR B O     1 
ATOM   7564 C  CB    . TYR B 1 479 ? 21.411  22.484  28.508  1.00 32.28  ?  465 TYR B CB    1 
ATOM   7565 C  CG    . TYR B 1 479 ? 21.599  22.317  27.011  1.00 28.37  ?  465 TYR B CG    1 
ATOM   7566 C  CD1   . TYR B 1 479 ? 20.983  23.173  26.109  1.00 31.55  ?  465 TYR B CD1   1 
ATOM   7567 C  CD2   . TYR B 1 479 ? 22.368  21.274  26.503  1.00 33.85  ?  465 TYR B CD2   1 
ATOM   7568 C  CE1   . TYR B 1 479 ? 21.138  23.005  24.743  1.00 28.01  ?  465 TYR B CE1   1 
ATOM   7569 C  CE2   . TYR B 1 479 ? 22.532  21.104  25.141  1.00 28.36  ?  465 TYR B CE2   1 
ATOM   7570 C  CZ    . TYR B 1 479 ? 21.911  21.967  24.266  1.00 29.17  ?  465 TYR B CZ    1 
ATOM   7571 O  OH    . TYR B 1 479 ? 22.071  21.793  22.909  1.00 28.66  ?  465 TYR B OH    1 
ATOM   7572 N  N     . THR B 1 480 ? 21.090  25.072  31.080  1.00 32.15  ?  466 THR B N     1 
ATOM   7573 C  CA    . THR B 1 480 ? 21.002  25.236  32.499  1.00 31.73  ?  466 THR B CA    1 
ATOM   7574 C  C     . THR B 1 480 ? 19.991  24.330  33.189  1.00 44.13  ?  466 THR B C     1 
ATOM   7575 O  O     . THR B 1 480 ? 20.240  23.874  34.274  1.00 40.77  ?  466 THR B O     1 
ATOM   7576 C  CB    . THR B 1 480 ? 20.828  26.691  32.908  1.00 28.99  ?  466 THR B CB    1 
ATOM   7577 O  OG1   . THR B 1 480 ? 22.091  27.330  32.877  1.00 33.03  ?  466 THR B OG1   1 
ATOM   7578 C  CG2   . THR B 1 480 ? 20.306  26.770  34.300  1.00 37.53  ?  466 THR B CG2   1 
ATOM   7579 N  N     . VAL B 1 481 ? 18.854  24.082  32.557  1.00 32.04  ?  467 VAL B N     1 
ATOM   7580 C  CA    . VAL B 1 481 ? 17.885  23.190  33.140  1.00 36.98  ?  467 VAL B CA    1 
ATOM   7581 C  C     . VAL B 1 481 ? 18.477  21.783  33.213  1.00 36.96  ?  467 VAL B C     1 
ATOM   7582 O  O     . VAL B 1 481 ? 18.299  21.131  34.182  1.00 45.35  ?  467 VAL B O     1 
ATOM   7583 C  CB    . VAL B 1 481 ? 16.547  23.192  32.402  1.00 41.13  ?  467 VAL B CB    1 
ATOM   7584 C  CG1   . VAL B 1 481 ? 15.733  21.990  32.802  1.00 42.75  ?  467 VAL B CG1   1 
ATOM   7585 C  CG2   . VAL B 1 481 ? 15.769  24.435  32.741  1.00 48.16  ?  467 VAL B CG2   1 
ATOM   7586 N  N     . LEU B 1 482 ? 19.202  21.346  32.200  1.00 34.23  ?  468 LEU B N     1 
ATOM   7587 C  CA    . LEU B 1 482 ? 19.814  20.042  32.250  1.00 40.78  ?  468 LEU B CA    1 
ATOM   7588 C  C     . LEU B 1 482 ? 20.893  19.979  33.332  1.00 42.06  ?  468 LEU B C     1 
ATOM   7589 O  O     . LEU B 1 482 ? 21.010  18.994  34.015  1.00 46.59  ?  468 LEU B O     1 
ATOM   7590 C  CB    . LEU B 1 482 ? 20.299  19.620  30.904  1.00 39.38  ?  468 LEU B CB    1 
ATOM   7591 C  CG    . LEU B 1 482 ? 19.182  19.491  29.891  1.00 37.39  ?  468 LEU B CG    1 
ATOM   7592 C  CD1   . LEU B 1 482 ? 19.753  19.130  28.553  1.00 34.45  ?  468 LEU B CD1   1 
ATOM   7593 C  CD2   . LEU B 1 482 ? 18.159  18.486  30.370  1.00 32.44  ?  468 LEU B CD2   1 
ATOM   7594 N  N     . ARG B 1 483 ? 21.630  21.060  33.519  1.00 37.68  ?  469 ARG B N     1 
ATOM   7595 C  CA    . ARG B 1 483 ? 22.651  21.132  34.552  1.00 32.96  ?  469 ARG B CA    1 
ATOM   7596 C  C     . ARG B 1 483 ? 22.036  20.934  35.905  1.00 43.05  ?  469 ARG B C     1 
ATOM   7597 O  O     . ARG B 1 483 ? 22.574  20.230  36.708  1.00 46.60  ?  469 ARG B O     1 
ATOM   7598 C  CB    . ARG B 1 483 ? 23.400  22.464  34.539  1.00 45.43  ?  469 ARG B CB    1 
ATOM   7599 C  CG    . ARG B 1 483 ? 24.232  22.742  33.317  1.00 34.11  ?  469 ARG B CG    1 
ATOM   7600 C  CD    . ARG B 1 483 ? 25.143  23.931  33.507  1.00 43.69  ?  469 ARG B CD    1 
ATOM   7601 N  NE    . ARG B 1 483 ? 25.661  24.436  32.261  1.00 35.67  ?  469 ARG B NE    1 
ATOM   7602 C  CZ    . ARG B 1 483 ? 26.731  23.971  31.659  1.00 49.71  ?  469 ARG B CZ    1 
ATOM   7603 N  NH1   . ARG B 1 483 ? 27.417  22.982  32.197  1.00 38.02  ?  469 ARG B NH1   1 
ATOM   7604 N  NH2   . ARG B 1 483 ? 27.103  24.494  30.521  1.00 34.44  ?  469 ARG B NH2   1 
ATOM   7605 N  N     . ALA B 1 484 ? 20.904  21.557  36.163  1.00 33.99  ?  470 ALA B N     1 
ATOM   7606 C  CA    . ALA B 1 484 ? 20.247  21.396  37.435  1.00 43.12  ?  470 ALA B CA    1 
ATOM   7607 C  C     . ALA B 1 484 ? 19.621  20.000  37.643  1.00 40.57  ?  470 ALA B C     1 
ATOM   7608 O  O     . ALA B 1 484 ? 19.435  19.572  38.753  1.00 44.20  ?  470 ALA B O     1 
ATOM   7609 C  CB    . ALA B 1 484 ? 19.226  22.482  37.644  1.00 46.62  ?  470 ALA B CB    1 
ATOM   7610 N  N     . ILE B 1 485 ? 19.313  19.297  36.570  1.00 44.18  ?  471 ILE B N     1 
ATOM   7611 C  CA    . ILE B 1 485 ? 18.770  17.968  36.696  1.00 40.70  ?  471 ILE B CA    1 
ATOM   7612 C  C     . ILE B 1 485 ? 19.866  16.963  36.977  1.00 44.00  ?  471 ILE B C     1 
ATOM   7613 O  O     . ILE B 1 485 ? 19.775  16.244  37.919  1.00 42.68  ?  471 ILE B O     1 
ATOM   7614 C  CB    . ILE B 1 485 ? 17.946  17.543  35.483  1.00 59.81  ?  471 ILE B CB    1 
ATOM   7615 C  CG1   . ILE B 1 485 ? 16.677  18.366  35.419  1.00 57.00  ?  471 ILE B CG1   1 
ATOM   7616 C  CG2   . ILE B 1 485 ? 17.582  16.069  35.585  1.00 57.33  ?  471 ILE B CG2   1 
ATOM   7617 C  CD1   . ILE B 1 485 ? 15.778  18.069  34.265  1.00 47.15  ?  471 ILE B CD1   1 
ATOM   7618 N  N     . HIS B 1 486 ? 20.916  16.966  36.179  1.00 38.32  ?  472 HIS B N     1 
ATOM   7619 C  CA    . HIS B 1 486 ? 22.001  16.034  36.332  1.00 41.46  ?  472 HIS B CA    1 
ATOM   7620 C  C     . HIS B 1 486 ? 23.267  16.471  35.614  1.00 43.14  ?  472 HIS B C     1 
ATOM   7621 O  O     . HIS B 1 486 ? 23.233  16.886  34.490  1.00 35.97  ?  472 HIS B O     1 
ATOM   7622 C  CB    . HIS B 1 486 ? 21.568  14.685  35.752  1.00 48.58  ?  472 HIS B CB    1 
ATOM   7623 C  CG    . HIS B 1 486 ? 22.572  13.600  35.895  1.00 38.46  ?  472 HIS B CG    1 
ATOM   7624 N  ND1   . HIS B 1 486 ? 22.744  12.901  37.060  1.00 41.25  ?  472 HIS B ND1   1 
ATOM   7625 C  CD2   . HIS B 1 486 ? 23.438  13.074  35.010  1.00 40.85  ?  472 HIS B CD2   1 
ATOM   7626 C  CE1   . HIS B 1 486 ? 23.683  12.000  36.893  1.00 49.78  ?  472 HIS B CE1   1 
ATOM   7627 N  NE2   . HIS B 1 486 ? 24.122  12.085  35.658  1.00 49.15  ?  472 HIS B NE2   1 
ATOM   7628 N  N     . GLY B 1 487 ? 24.394  16.333  36.282  1.00 41.77  ?  473 GLY B N     1 
ATOM   7629 C  CA    . GLY B 1 487 ? 25.672  16.648  35.687  1.00 43.88  ?  473 GLY B CA    1 
ATOM   7630 C  C     . GLY B 1 487 ? 25.954  18.078  35.316  1.00 43.74  ?  473 GLY B C     1 
ATOM   7631 O  O     . GLY B 1 487 ? 26.248  18.375  34.196  1.00 40.37  ?  473 GLY B O     1 
ATOM   7632 N  N     . PRO B 1 488 ? 25.939  18.954  36.293  1.00 39.58  ?  474 PRO B N     1 
ATOM   7633 C  CA    . PRO B 1 488 ? 26.205  20.367  36.069  1.00 44.94  ?  474 PRO B CA    1 
ATOM   7634 C  C     . PRO B 1 488 ? 27.542  20.664  35.413  1.00 43.19  ?  474 PRO B C     1 
ATOM   7635 O  O     . PRO B 1 488 ? 27.599  21.578  34.636  1.00 46.56  ?  474 PRO B O     1 
ATOM   7636 C  CB    . PRO B 1 488 ? 26.132  20.959  37.455  1.00 48.26  ?  474 PRO B CB    1 
ATOM   7637 C  CG    . PRO B 1 488 ? 26.224  19.819  38.392  1.00 48.12  ?  474 PRO B CG    1 
ATOM   7638 C  CD    . PRO B 1 488 ? 25.604  18.682  37.686  1.00 45.99  ?  474 PRO B CD    1 
ATOM   7639 N  N     . GLU B 1 489 ? 28.582  19.905  35.704  1.00 45.78  ?  475 GLU B N     1 
ATOM   7640 C  CA    . GLU B 1 489 ? 29.879  20.120  35.101  1.00 50.04  ?  475 GLU B CA    1 
ATOM   7641 C  C     . GLU B 1 489 ? 30.167  19.220  33.932  1.00 50.29  ?  475 GLU B C     1 
ATOM   7642 O  O     . GLU B 1 489 ? 31.254  19.236  33.430  1.00 55.80  ?  475 GLU B O     1 
ATOM   7643 C  CB    . GLU B 1 489 ? 30.977  19.923  36.121  1.00 42.83  ?  475 GLU B CB    1 
ATOM   7644 C  CG    . GLU B 1 489 ? 31.116  21.025  37.146  1.00 66.91  ?  475 GLU B CG    1 
ATOM   7645 C  CD    . GLU B 1 489 ? 32.112  20.661  38.247  1.00 87.05  ?  475 GLU B CD    1 
ATOM   7646 O  OE1   . GLU B 1 489 ? 31.702  20.593  39.410  1.00 81.84  ?  475 GLU B OE1   1 
ATOM   7647 O  OE2   . GLU B 1 489 ? 33.306  20.432  37.949  1.00 83.86  ?  475 GLU B OE2   1 
ATOM   7648 N  N     . GLN B 1 490 ? 29.209  18.413  33.509  1.00 50.26  ?  476 GLN B N     1 
ATOM   7649 C  CA    . GLN B 1 490 ? 29.441  17.536  32.369  1.00 40.68  ?  476 GLN B CA    1 
ATOM   7650 C  C     . GLN B 1 490 ? 29.371  18.323  31.067  1.00 46.87  ?  476 GLN B C     1 
ATOM   7651 O  O     . GLN B 1 490 ? 28.531  19.214  30.907  1.00 41.62  ?  476 GLN B O     1 
ATOM   7652 C  CB    . GLN B 1 490 ? 28.417  16.399  32.344  1.00 43.60  ?  476 GLN B CB    1 
ATOM   7653 C  CG    . GLN B 1 490 ? 28.635  15.323  33.403  1.00 37.01  ?  476 GLN B CG    1 
ATOM   7654 C  CD    . GLN B 1 490 ? 29.800  14.406  33.083  1.00 47.11  ?  476 GLN B CD    1 
ATOM   7655 O  OE1   . GLN B 1 490 ? 30.951  14.841  33.028  1.00 44.98  ?  476 GLN B OE1   1 
ATOM   7656 N  NE2   . GLN B 1 490 ? 29.507  13.123  32.878  1.00 49.87  ?  476 GLN B NE2   1 
ATOM   7657 N  N     . ARG B 1 491 ? 30.262  17.988  30.131  1.00 40.63  ?  477 ARG B N     1 
ATOM   7658 C  CA    . ARG B 1 491 ? 30.368  18.756  28.894  1.00 44.69  ?  477 ARG B CA    1 
ATOM   7659 C  C     . ARG B 1 491 ? 29.172  18.568  27.962  1.00 39.07  ?  477 ARG B C     1 
ATOM   7660 O  O     . ARG B 1 491 ? 28.968  19.400  27.073  1.00 44.99  ?  477 ARG B O     1 
ATOM   7661 C  CB    . ARG B 1 491 ? 31.680  18.430  28.174  1.00 40.21  ?  477 ARG B CB    1 
ATOM   7662 C  CG    . ARG B 1 491 ? 31.679  17.175  27.338  1.00 53.90  ?  477 ARG B CG    1 
ATOM   7663 C  CD    . ARG B 1 491 ? 32.745  17.269  26.258  1.00 53.02  ?  477 ARG B CD    1 
ATOM   7664 N  NE    . ARG B 1 491 ? 33.094  15.963  25.714  1.00 50.03  ?  477 ARG B NE    1 
ATOM   7665 C  CZ    . ARG B 1 491 ? 32.743  15.547  24.505  1.00 55.03  ?  477 ARG B CZ    1 
ATOM   7666 N  NH1   . ARG B 1 491 ? 32.010  16.304  23.700  1.00 45.33  ?  477 ARG B NH1   1 
ATOM   7667 N  NH2   . ARG B 1 491 ? 33.135  14.342  24.093  1.00 44.71  ?  477 ARG B NH2   1 
ATOM   7668 N  N     . TYR B 1 492 ? 28.384  17.501  28.113  1.00 32.10  ?  478 TYR B N     1 
ATOM   7669 C  CA    . TYR B 1 492 ? 27.224  17.390  27.230  1.00 33.07  ?  478 TYR B CA    1 
ATOM   7670 C  C     . TYR B 1 492 ? 26.172  18.451  27.519  1.00 39.86  ?  478 TYR B C     1 
ATOM   7671 O  O     . TYR B 1 492 ? 25.284  18.664  26.684  1.00 34.73  ?  478 TYR B O     1 
ATOM   7672 C  CB    . TYR B 1 492 ? 26.590  15.996  27.304  1.00 29.01  ?  478 TYR B CB    1 
ATOM   7673 C  CG    . TYR B 1 492 ? 26.263  15.492  28.692  1.00 31.52  ?  478 TYR B CG    1 
ATOM   7674 C  CD1   . TYR B 1 492 ? 25.233  16.052  29.439  1.00 27.18  ?  478 TYR B CD1   1 
ATOM   7675 C  CD2   . TYR B 1 492 ? 26.976  14.433  29.247  1.00 36.39  ?  478 TYR B CD2   1 
ATOM   7676 C  CE1   . TYR B 1 492 ? 24.930  15.583  30.703  1.00 37.86  ?  478 TYR B CE1   1 
ATOM   7677 C  CE2   . TYR B 1 492 ? 26.678  13.954  30.509  1.00 40.55  ?  478 TYR B CE2   1 
ATOM   7678 C  CZ    . TYR B 1 492 ? 25.654  14.532  31.233  1.00 40.94  ?  478 TYR B CZ    1 
ATOM   7679 O  OH    . TYR B 1 492 ? 25.361  14.056  32.490  1.00 35.15  ?  478 TYR B OH    1 
ATOM   7680 N  N     . ASN B 1 493 ? 26.257  19.122  28.666  1.00 40.53  ?  479 ASN B N     1 
ATOM   7681 C  CA    . ASN B 1 493 ? 25.397  20.254  28.976  1.00 36.95  ?  479 ASN B CA    1 
ATOM   7682 C  C     . ASN B 1 493 ? 25.958  21.570  28.453  1.00 41.08  ?  479 ASN B C     1 
ATOM   7683 O  O     . ASN B 1 493 ? 25.325  22.615  28.635  1.00 44.59  ?  479 ASN B O     1 
ATOM   7684 C  CB    . ASN B 1 493 ? 25.166  20.337  30.489  1.00 30.02  ?  479 ASN B CB    1 
ATOM   7685 C  CG    . ASN B 1 493 ? 24.139  19.323  30.974  1.00 41.05  ?  479 ASN B CG    1 
ATOM   7686 O  OD1   . ASN B 1 493 ? 23.301  18.861  30.197  1.00 33.30  ?  479 ASN B OD1   1 
ATOM   7687 N  ND2   . ASN B 1 493 ? 24.198  18.974  32.257  1.00 27.79  ?  479 ASN B ND2   1 
ATOM   7688 N  N     . ASP B 1 494 ? 27.121  21.545  27.812  1.00 37.16  ?  480 ASP B N     1 
ATOM   7689 C  CA    . ASP B 1 494 ? 27.674  22.717  27.150  1.00 37.06  ?  480 ASP B CA    1 
ATOM   7690 C  C     . ASP B 1 494 ? 27.112  22.840  25.736  1.00 42.93  ?  480 ASP B C     1 
ATOM   7691 O  O     . ASP B 1 494 ? 26.586  21.881  25.161  1.00 43.08  ?  480 ASP B O     1 
ATOM   7692 C  CB    . ASP B 1 494 ? 29.204  22.646  27.098  1.00 38.96  ?  480 ASP B CB    1 
ATOM   7693 C  CG    . ASP B 1 494 ? 29.840  22.629  28.479  1.00 43.11  ?  480 ASP B CG    1 
ATOM   7694 O  OD1   . ASP B 1 494 ? 29.214  23.118  29.440  1.00 49.02  ?  480 ASP B OD1   1 
ATOM   7695 O  OD2   . ASP B 1 494 ? 30.973  22.123  28.606  1.00 43.25  ?  480 ASP B OD2   1 
ATOM   7696 N  N     . ILE B 1 495 ? 27.209  24.052  25.187  1.00 36.76  ?  481 ILE B N     1 
ATOM   7697 C  CA    . ILE B 1 495 ? 26.813  24.339  23.816  1.00 34.25  ?  481 ILE B CA    1 
ATOM   7698 C  C     . ILE B 1 495 ? 27.912  25.157  23.150  1.00 41.88  ?  481 ILE B C     1 
ATOM   7699 O  O     . ILE B 1 495 ? 28.747  25.779  23.811  1.00 37.14  ?  481 ILE B O     1 
ATOM   7700 C  CB    . ILE B 1 495 ? 25.473  25.104  23.739  1.00 37.07  ?  481 ILE B CB    1 
ATOM   7701 C  CG1   . ILE B 1 495 ? 25.623  26.492  24.367  1.00 32.42  ?  481 ILE B CG1   1 
ATOM   7702 C  CG2   . ILE B 1 495 ? 24.359  24.326  24.422  1.00 32.21  ?  481 ILE B CG2   1 
ATOM   7703 C  CD1   . ILE B 1 495 ? 24.353  27.314  24.347  1.00 37.60  ?  481 ILE B CD1   1 
ATOM   7704 N  N     . ALA B 1 496 ? 27.894  25.160  21.819  1.00 32.14  ?  482 ALA B N     1 
ATOM   7705 C  CA    . ALA B 1 496 ? 28.719  26.099  21.077  1.00 32.02  ?  482 ALA B CA    1 
ATOM   7706 C  C     . ALA B 1 496 ? 28.327  27.519  21.453  1.00 36.07  ?  482 ALA B C     1 
ATOM   7707 O  O     . ALA B 1 496 ? 27.138  27.850  21.509  1.00 37.86  ?  482 ALA B O     1 
ATOM   7708 C  CB    . ALA B 1 496 ? 28.550  25.885  19.573  1.00 30.56  ?  482 ALA B CB    1 
ATOM   7709 N  N     . LEU B 1 497 ? 29.328  28.361  21.708  1.00 33.80  ?  483 LEU B N     1 
ATOM   7710 C  CA    . LEU B 1 497 ? 29.100  29.724  22.178  1.00 32.26  ?  483 LEU B CA    1 
ATOM   7711 C  C     . LEU B 1 497 ? 28.977  30.648  20.971  1.00 37.63  ?  483 LEU B C     1 
ATOM   7712 O  O     . LEU B 1 497 ? 29.950  30.860  20.239  1.00 40.48  ?  483 LEU B O     1 
ATOM   7713 C  CB    . LEU B 1 497 ? 30.228  30.164  23.108  1.00 32.48  ?  483 LEU B CB    1 
ATOM   7714 C  CG    . LEU B 1 497 ? 30.351  29.318  24.378  1.00 34.17  ?  483 LEU B CG    1 
ATOM   7715 C  CD1   . LEU B 1 497 ? 31.358  29.905  25.363  1.00 33.50  ?  483 LEU B CD1   1 
ATOM   7716 C  CD2   . LEU B 1 497 ? 28.985  29.156  25.033  1.00 33.28  ?  483 LEU B CD2   1 
ATOM   7717 N  N     . TRP B 1 498 ? 27.779  31.189  20.762  1.00 29.85  ?  484 TRP B N     1 
ATOM   7718 C  CA    . TRP B 1 498 ? 27.486  32.051  19.628  1.00 31.67  ?  484 TRP B CA    1 
ATOM   7719 C  C     . TRP B 1 498 ? 27.667  33.521  20.000  1.00 36.83  ?  484 TRP B C     1 
ATOM   7720 O  O     . TRP B 1 498 ? 27.692  33.893  21.175  1.00 38.57  ?  484 TRP B O     1 
ATOM   7721 C  CB    . TRP B 1 498 ? 26.056  31.821  19.134  1.00 25.93  ?  484 TRP B CB    1 
ATOM   7722 C  CG    . TRP B 1 498 ? 25.864  30.538  18.397  1.00 28.97  ?  484 TRP B CG    1 
ATOM   7723 C  CD1   . TRP B 1 498 ? 26.784  29.538  18.230  1.00 35.98  ?  484 TRP B CD1   1 
ATOM   7724 C  CD2   . TRP B 1 498 ? 24.676  30.107  17.727  1.00 31.80  ?  484 TRP B CD2   1 
ATOM   7725 N  NE1   . TRP B 1 498 ? 26.242  28.516  17.492  1.00 26.72  ?  484 TRP B NE1   1 
ATOM   7726 C  CE2   . TRP B 1 498 ? 24.948  28.835  17.175  1.00 28.98  ?  484 TRP B CE2   1 
ATOM   7727 C  CE3   . TRP B 1 498 ? 23.406  30.669  17.541  1.00 29.67  ?  484 TRP B CE3   1 
ATOM   7728 C  CZ2   . TRP B 1 498 ? 24.000  28.119  16.444  1.00 24.95  ?  484 TRP B CZ2   1 
ATOM   7729 C  CZ3   . TRP B 1 498 ? 22.460  29.953  16.815  1.00 25.76  ?  484 TRP B CZ3   1 
ATOM   7730 C  CH2   . TRP B 1 498 ? 22.765  28.692  16.276  1.00 30.29  ?  484 TRP B CH2   1 
ATOM   7731 N  N     . ASN B 1 499 ? 27.781  34.359  18.967  1.00 33.11  ?  485 ASN B N     1 
ATOM   7732 C  CA    . ASN B 1 499 ? 27.862  35.814  19.120  1.00 29.34  ?  485 ASN B CA    1 
ATOM   7733 C  C     . ASN B 1 499 ? 26.489  36.381  18.768  1.00 32.01  ?  485 ASN B C     1 
ATOM   7734 O  O     . ASN B 1 499 ? 26.241  36.853  17.658  1.00 35.97  ?  485 ASN B O     1 
ATOM   7735 C  CB    . ASN B 1 499 ? 28.964  36.379  18.233  1.00 34.99  ?  485 ASN B CB    1 
ATOM   7736 C  CG    . ASN B 1 499 ? 29.402  37.765  18.651  1.00 35.89  ?  485 ASN B CG    1 
ATOM   7737 O  OD1   . ASN B 1 499 ? 28.813  38.382  19.541  1.00 36.93  ?  485 ASN B OD1   1 
ATOM   7738 N  ND2   . ASN B 1 499 ? 30.441  38.265  18.003  1.00 36.92  ?  485 ASN B ND2   1 
ATOM   7739 N  N     . TRP B 1 500 ? 25.598  36.358  19.763  1.00 33.77  ?  486 TRP B N     1 
ATOM   7740 C  CA    . TRP B 1 500 ? 24.167  36.510  19.506  1.00 33.28  ?  486 TRP B CA    1 
ATOM   7741 C  C     . TRP B 1 500 ? 23.832  37.864  18.894  1.00 34.89  ?  486 TRP B C     1 
ATOM   7742 O  O     . TRP B 1 500 ? 23.003  37.944  17.979  1.00 29.10  ?  486 TRP B O     1 
ATOM   7743 C  CB    . TRP B 1 500 ? 23.382  36.293  20.801  1.00 31.27  ?  486 TRP B CB    1 
ATOM   7744 C  CG    . TRP B 1 500 ? 23.422  34.867  21.271  1.00 33.78  ?  486 TRP B CG    1 
ATOM   7745 C  CD1   . TRP B 1 500 ? 24.258  34.336  22.210  1.00 34.22  ?  486 TRP B CD1   1 
ATOM   7746 C  CD2   . TRP B 1 500 ? 22.598  33.790  20.812  1.00 30.83  ?  486 TRP B CD2   1 
ATOM   7747 N  NE1   . TRP B 1 500 ? 24.001  32.993  22.368  1.00 32.27  ?  486 TRP B NE1   1 
ATOM   7748 C  CE2   . TRP B 1 500 ? 22.985  32.635  21.522  1.00 31.99  ?  486 TRP B CE2   1 
ATOM   7749 C  CE3   . TRP B 1 500 ? 21.564  33.692  19.877  1.00 28.36  ?  486 TRP B CE3   1 
ATOM   7750 C  CZ2   . TRP B 1 500 ? 22.380  31.394  21.319  1.00 27.42  ?  486 TRP B CZ2   1 
ATOM   7751 C  CZ3   . TRP B 1 500 ? 20.965  32.465  19.677  1.00 28.35  ?  486 TRP B CZ3   1 
ATOM   7752 C  CH2   . TRP B 1 500 ? 21.374  31.331  20.394  1.00 34.97  ?  486 TRP B CH2   1 
ATOM   7753 N  N     . THR B 1 501 ? 24.468  38.938  19.372  1.00 31.84  ?  487 THR B N     1 
ATOM   7754 C  CA    . THR B 1 501 ? 24.130  40.269  18.879  1.00 34.77  ?  487 THR B CA    1 
ATOM   7755 C  C     . THR B 1 501 ? 24.527  40.478  17.424  1.00 37.78  ?  487 THR B C     1 
ATOM   7756 O  O     . THR B 1 501 ? 24.097  41.467  16.820  1.00 34.75  ?  487 THR B O     1 
ATOM   7757 C  CB    . THR B 1 501 ? 24.783  41.350  19.747  1.00 36.28  ?  487 THR B CB    1 
ATOM   7758 O  OG1   . THR B 1 501 ? 26.205  41.161  19.769  1.00 33.94  ?  487 THR B OG1   1 
ATOM   7759 C  CG2   . THR B 1 501 ? 24.241  41.300  21.170  1.00 30.63  ?  487 THR B CG2   1 
ATOM   7760 N  N     . GLN B 1 502 ? 25.319  39.577  16.849  1.00 36.81  ?  488 GLN B N     1 
ATOM   7761 C  CA    . GLN B 1 502 ? 25.752  39.690  15.465  1.00 32.93  ?  488 GLN B CA    1 
ATOM   7762 C  C     . GLN B 1 502 ? 24.964  38.787  14.523  1.00 35.17  ?  488 GLN B C     1 
ATOM   7763 O  O     . GLN B 1 502 ? 25.231  38.786  13.318  1.00 35.94  ?  488 GLN B O     1 
ATOM   7764 C  CB    . GLN B 1 502 ? 27.248  39.375  15.357  1.00 40.20  ?  488 GLN B CB    1 
ATOM   7765 C  CG    . GLN B 1 502 ? 28.144  40.204  16.275  1.00 37.98  ?  488 GLN B CG    1 
ATOM   7766 C  CD    . GLN B 1 502 ? 27.929  41.701  16.118  1.00 53.52  ?  488 GLN B CD    1 
ATOM   7767 O  OE1   . GLN B 1 502 ? 28.261  42.284  15.085  1.00 49.67  ?  488 GLN B OE1   1 
ATOM   7768 N  NE2   . GLN B 1 502 ? 27.374  42.331  17.149  1.00 53.87  ?  488 GLN B NE2   1 
ATOM   7769 N  N     . ILE B 1 503 ? 24.001  38.026  15.032  1.00 29.75  ?  489 ILE B N     1 
ATOM   7770 C  CA    . ILE B 1 503 ? 23.225  37.107  14.199  1.00 31.57  ?  489 ILE B CA    1 
ATOM   7771 C  C     . ILE B 1 503 ? 22.324  37.872  13.227  1.00 32.22  ?  489 ILE B C     1 
ATOM   7772 O  O     . ILE B 1 503 ? 22.247  37.483  12.053  1.00 30.72  ?  489 ILE B O     1 
ATOM   7773 C  CB    . ILE B 1 503 ? 22.426  36.117  15.064  1.00 31.74  ?  489 ILE B CB    1 
ATOM   7774 C  CG1   . ILE B 1 503 ? 23.390  35.158  15.773  1.00 34.88  ?  489 ILE B CG1   1 
ATOM   7775 C  CG2   . ILE B 1 503 ? 21.441  35.326  14.216  1.00 34.02  ?  489 ILE B CG2   1 
ATOM   7776 C  CD1   . ILE B 1 503 ? 22.704  34.104  16.618  1.00 27.90  ?  489 ILE B CD1   1 
ATOM   7777 N  N     . PRO B 1 504 ? 21.623  38.947  13.630  1.00 30.27  ?  490 PRO B N     1 
ATOM   7778 C  CA    . PRO B 1 504 ? 20.805  39.663  12.630  1.00 31.01  ?  490 PRO B CA    1 
ATOM   7779 C  C     . PRO B 1 504 ? 21.594  40.176  11.434  1.00 29.21  ?  490 PRO B C     1 
ATOM   7780 O  O     . PRO B 1 504 ? 21.091  40.125  10.305  1.00 36.41  ?  490 PRO B O     1 
ATOM   7781 C  CB    . PRO B 1 504 ? 20.183  40.810  13.442  1.00 29.11  ?  490 PRO B CB    1 
ATOM   7782 C  CG    . PRO B 1 504 ? 20.085  40.263  14.812  1.00 33.84  ?  490 PRO B CG    1 
ATOM   7783 C  CD    . PRO B 1 504 ? 21.357  39.458  14.989  1.00 33.31  ?  490 PRO B CD    1 
ATOM   7784 N  N     . GLN B 1 505 ? 22.820  40.663  11.633  1.00 34.06  ?  491 GLN B N     1 
ATOM   7785 C  CA    . GLN B 1 505 ? 23.570  41.192  10.498  1.00 37.85  ?  491 GLN B CA    1 
ATOM   7786 C  C     . GLN B 1 505 ? 24.111  40.085  9.599   1.00 37.45  ?  491 GLN B C     1 
ATOM   7787 O  O     . GLN B 1 505 ? 24.530  40.370  8.473   1.00 38.95  ?  491 GLN B O     1 
ATOM   7788 C  CB    . GLN B 1 505 ? 24.698  42.108  10.985  1.00 39.08  ?  491 GLN B CB    1 
ATOM   7789 C  CG    . GLN B 1 505 ? 25.773  41.378  11.738  1.00 52.23  ?  491 GLN B CG    1 
ATOM   7790 C  CD    . GLN B 1 505 ? 26.857  40.843  10.823  1.00 64.10  ?  491 GLN B CD    1 
ATOM   7791 O  OE1   . GLN B 1 505 ? 27.209  41.466  9.817   1.00 65.33  ?  491 GLN B OE1   1 
ATOM   7792 N  NE2   . GLN B 1 505 ? 27.326  39.636  11.118  1.00 50.75  ?  491 GLN B NE2   1 
ATOM   7793 N  N     . ALA B 1 506 ? 24.128  38.836  10.072  1.00 33.60  ?  492 ALA B N     1 
ATOM   7794 C  CA    . ALA B 1 506 ? 24.505  37.705  9.232   1.00 37.26  ?  492 ALA B CA    1 
ATOM   7795 C  C     . ALA B 1 506 ? 23.328  37.126  8.458   1.00 37.26  ?  492 ALA B C     1 
ATOM   7796 O  O     . ALA B 1 506 ? 23.523  36.580  7.364   1.00 32.14  ?  492 ALA B O     1 
ATOM   7797 C  CB    . ALA B 1 506 ? 25.134  36.593  10.079  1.00 33.91  ?  492 ALA B CB    1 
ATOM   7798 N  N     . LEU B 1 507 ? 22.114  37.233  8.997   1.00 31.26  ?  493 LEU B N     1 
ATOM   7799 C  CA    . LEU B 1 507 ? 20.932  36.636  8.392   1.00 31.93  ?  493 LEU B CA    1 
ATOM   7800 C  C     . LEU B 1 507 ? 20.111  37.636  7.588   1.00 36.20  ?  493 LEU B C     1 
ATOM   7801 O  O     . LEU B 1 507 ? 18.971  37.334  7.216   1.00 33.72  ?  493 LEU B O     1 
ATOM   7802 C  CB    . LEU B 1 507 ? 20.067  35.976  9.467   1.00 28.13  ?  493 LEU B CB    1 
ATOM   7803 C  CG    . LEU B 1 507 ? 20.736  34.857  10.270  1.00 29.49  ?  493 LEU B CG    1 
ATOM   7804 C  CD1   . LEU B 1 507 ? 19.691  34.095  11.074  1.00 24.70  ?  493 LEU B CD1   1 
ATOM   7805 C  CD2   . LEU B 1 507 ? 21.513  33.913  9.360   1.00 28.58  ?  493 LEU B CD2   1 
ATOM   7806 N  N     . SER B 1 508 ? 20.649  38.826  7.334   1.00 32.79  ?  494 SER B N     1 
ATOM   7807 C  CA    . SER B 1 508 ? 19.961  39.812  6.516   1.00 40.59  ?  494 SER B CA    1 
ATOM   7808 C  C     . SER B 1 508 ? 20.995  40.730  5.887   1.00 33.26  ?  494 SER B C     1 
ATOM   7809 O  O     . SER B 1 508 ? 22.025  41.018  6.500   1.00 33.44  ?  494 SER B O     1 
ATOM   7810 C  CB    . SER B 1 508 ? 18.957  40.628  7.340   1.00 34.39  ?  494 SER B CB    1 
ATOM   7811 O  OG    . SER B 1 508 ? 18.568  41.797  6.640   1.00 39.93  ?  494 SER B OG    1 
ATOM   7812 N  N     . LEU B 1 509 ? 20.728  41.168  4.652   1.00 38.12  ?  495 LEU B N     1 
ATOM   7813 C  CA    . LEU B 1 509 ? 21.625  42.101  3.975   1.00 35.11  ?  495 LEU B CA    1 
ATOM   7814 C  C     . LEU B 1 509 ? 21.482  43.518  4.500   1.00 48.42  ?  495 LEU B C     1 
ATOM   7815 O  O     . LEU B 1 509 ? 22.366  44.351  4.271   1.00 50.80  ?  495 LEU B O     1 
ATOM   7816 C  CB    . LEU B 1 509 ? 21.366  42.097  2.465   1.00 37.79  ?  495 LEU B CB    1 
ATOM   7817 C  CG    . LEU B 1 509 ? 21.743  40.822  1.705   1.00 41.23  ?  495 LEU B CG    1 
ATOM   7818 C  CD1   . LEU B 1 509 ? 21.538  41.011  0.210   1.00 44.77  ?  495 LEU B CD1   1 
ATOM   7819 C  CD2   . LEU B 1 509 ? 23.184  40.438  2.005   1.00 34.91  ?  495 LEU B CD2   1 
ATOM   7820 N  N     . ASP B 1 510 ? 20.387  43.806  5.181   1.00 43.28  ?  496 ASP B N     1 
ATOM   7821 C  CA    . ASP B 1 510 ? 20.139  45.121  5.743   1.00 40.88  ?  496 ASP B CA    1 
ATOM   7822 C  C     . ASP B 1 510 ? 19.163  44.970  6.900   1.00 36.83  ?  496 ASP B C     1 
ATOM   7823 O  O     . ASP B 1 510 ? 17.978  45.299  6.766   1.00 38.62  ?  496 ASP B O     1 
ATOM   7824 C  CB    . ASP B 1 510 ? 19.586  46.064  4.673   1.00 39.81  ?  496 ASP B CB    1 
ATOM   7825 C  CG    . ASP B 1 510 ? 19.244  47.437  5.221   1.00 49.23  ?  496 ASP B CG    1 
ATOM   7826 O  OD1   . ASP B 1 510 ? 19.836  47.829  6.249   1.00 48.99  ?  496 ASP B OD1   1 
ATOM   7827 O  OD2   . ASP B 1 510 ? 18.387  48.122  4.619   1.00 46.28  ?  496 ASP B OD2   1 
ATOM   7828 N  N     . PRO B 1 511 ? 19.600  44.421  8.032   1.00 44.66  ?  497 PRO B N     1 
ATOM   7829 C  CA    . PRO B 1 511 ? 18.684  44.284  9.167   1.00 44.66  ?  497 PRO B CA    1 
ATOM   7830 C  C     . PRO B 1 511 ? 18.493  45.647  9.812   1.00 54.45  ?  497 PRO B C     1 
ATOM   7831 O  O     . PRO B 1 511 ? 19.459  46.365  10.076  1.00 76.71  ?  497 PRO B O     1 
ATOM   7832 C  CB    . PRO B 1 511 ? 19.413  43.312  10.101  1.00 40.68  ?  497 PRO B CB    1 
ATOM   7833 C  CG    . PRO B 1 511 ? 20.868  43.522  9.792   1.00 40.51  ?  497 PRO B CG    1 
ATOM   7834 C  CD    . PRO B 1 511 ? 20.978  44.021  8.372   1.00 37.83  ?  497 PRO B CD    1 
ATOM   7835 N  N     . GLN B 1 512 ? 17.248  46.009  10.068  1.00 77.90  ?  498 GLN B N     1 
ATOM   7836 C  CA    . GLN B 1 512 ? 17.002  47.231  10.828  1.00 76.29  ?  498 GLN B CA    1 
ATOM   7837 C  C     . GLN B 1 512 ? 16.902  46.898  12.308  1.00 72.42  ?  498 GLN B C     1 
ATOM   7838 O  O     . GLN B 1 512 ? 15.933  47.239  12.966  1.00 75.04  ?  498 GLN B O     1 
ATOM   7839 C  CB    . GLN B 1 512 ? 15.744  47.929  10.325  1.00 78.31  ?  498 GLN B CB    1 
ATOM   7840 C  CG    . GLN B 1 512 ? 15.768  49.451  10.466  1.00 91.79  ?  498 GLN B CG    1 
ATOM   7841 C  CD    . GLN B 1 512 ? 14.376  50.038  10.631  1.00 89.48  ?  498 GLN B CD    1 
ATOM   7842 O  OE1   . GLN B 1 512 ? 13.410  49.310  10.868  1.00 91.09  ?  498 GLN B OE1   1 
ATOM   7843 N  NE2   . GLN B 1 512 ? 14.266  51.358  10.510  1.00 94.83  ?  498 GLN B NE2   1 
ATOM   7844 N  N     . ALA B 1 513 ? 17.896  46.208  12.848  1.00 50.23  ?  499 ALA B N     1 
ATOM   7845 C  CA    . ALA B 1 513 ? 17.751  45.619  14.167  1.00 46.52  ?  499 ALA B CA    1 
ATOM   7846 C  C     . ALA B 1 513 ? 18.703  46.290  15.138  1.00 45.83  ?  499 ALA B C     1 
ATOM   7847 O  O     . ALA B 1 513 ? 19.791  46.732  14.765  1.00 54.56  ?  499 ALA B O     1 
ATOM   7848 C  CB    . ALA B 1 513 ? 18.019  44.109  14.134  1.00 38.14  ?  499 ALA B CB    1 
ATOM   7849 N  N     . GLN B 1 514 ? 18.291  46.338  16.400  1.00 41.29  ?  500 GLN B N     1 
ATOM   7850 C  CA    . GLN B 1 514 ? 19.119  46.876  17.465  1.00 42.45  ?  500 GLN B CA    1 
ATOM   7851 C  C     . GLN B 1 514 ? 19.361  45.764  18.468  1.00 41.95  ?  500 GLN B C     1 
ATOM   7852 O  O     . GLN B 1 514 ? 18.411  45.175  18.994  1.00 36.55  ?  500 GLN B O     1 
ATOM   7853 C  CB    . GLN B 1 514 ? 18.437  48.081  18.120  1.00 38.16  ?  500 GLN B CB    1 
ATOM   7854 C  CG    . GLN B 1 514 ? 17.949  49.117  17.114  1.00 40.05  ?  500 GLN B CG    1 
ATOM   7855 C  CD    . GLN B 1 514 ? 17.360  50.359  17.763  1.00 44.91  ?  500 GLN B CD    1 
ATOM   7856 O  OE1   . GLN B 1 514 ? 17.612  51.482  17.322  1.00 50.38  ?  500 GLN B OE1   1 
ATOM   7857 N  NE2   . GLN B 1 514 ? 16.568  50.163  18.809  1.00 41.93  ?  500 GLN B NE2   1 
ATOM   7858 N  N     . CYS B 1 515 ? 20.631  45.481  18.730  1.00 35.65  ?  501 CYS B N     1 
ATOM   7859 C  CA    . CYS B 1 515 ? 21.019  44.389  19.603  1.00 33.91  ?  501 CYS B CA    1 
ATOM   7860 C  C     . CYS B 1 515 ? 21.896  44.918  20.722  1.00 38.10  ?  501 CYS B C     1 
ATOM   7861 O  O     . CYS B 1 515 ? 22.733  45.796  20.504  1.00 37.43  ?  501 CYS B O     1 
ATOM   7862 C  CB    . CYS B 1 515 ? 21.741  43.302  18.812  1.00 31.80  ?  501 CYS B CB    1 
ATOM   7863 S  SG    . CYS B 1 515 ? 20.793  42.775  17.358  1.00 45.04  ?  501 CYS B SG    1 
ATOM   7864 N  N     . TRP B 1 516 ? 21.689  44.383  21.919  1.00 36.95  ?  502 TRP B N     1 
ATOM   7865 C  CA    . TRP B 1 516 ? 22.504  44.706  23.076  1.00 35.68  ?  502 TRP B CA    1 
ATOM   7866 C  C     . TRP B 1 516 ? 22.889  43.420  23.780  1.00 41.44  ?  502 TRP B C     1 
ATOM   7867 O  O     . TRP B 1 516 ? 22.159  42.427  23.737  1.00 43.75  ?  502 TRP B O     1 
ATOM   7868 C  CB    . TRP B 1 516 ? 21.778  45.592  24.090  1.00 38.71  ?  502 TRP B CB    1 
ATOM   7869 C  CG    . TRP B 1 516 ? 21.457  46.982  23.651  1.00 39.57  ?  502 TRP B CG    1 
ATOM   7870 C  CD1   . TRP B 1 516 ? 22.170  48.119  23.924  1.00 43.81  ?  502 TRP B CD1   1 
ATOM   7871 C  CD2   . TRP B 1 516 ? 20.312  47.397  22.905  1.00 43.55  ?  502 TRP B CD2   1 
ATOM   7872 N  NE1   . TRP B 1 516 ? 21.545  49.212  23.378  1.00 40.17  ?  502 TRP B NE1   1 
ATOM   7873 C  CE2   . TRP B 1 516 ? 20.403  48.798  22.745  1.00 43.75  ?  502 TRP B CE2   1 
ATOM   7874 C  CE3   . TRP B 1 516 ? 19.224  46.722  22.345  1.00 36.24  ?  502 TRP B CE3   1 
ATOM   7875 C  CZ2   . TRP B 1 516 ? 19.443  49.533  22.054  1.00 40.38  ?  502 TRP B CZ2   1 
ATOM   7876 C  CZ3   . TRP B 1 516 ? 18.277  47.454  21.656  1.00 40.30  ?  502 TRP B CZ3   1 
ATOM   7877 C  CH2   . TRP B 1 516 ? 18.390  48.843  21.516  1.00 41.13  ?  502 TRP B CH2   1 
ATOM   7878 N  N     . ARG B 1 517 ? 24.026  43.466  24.462  1.00 40.78  ?  503 ARG B N     1 
ATOM   7879 C  CA    . ARG B 1 517 ? 24.419  42.436  25.410  1.00 46.42  ?  503 ARG B CA    1 
ATOM   7880 C  C     . ARG B 1 517 ? 24.443  43.100  26.776  1.00 46.83  ?  503 ARG B C     1 
ATOM   7881 O  O     . ARG B 1 517 ? 25.100  44.131  26.953  1.00 46.37  ?  503 ARG B O     1 
ATOM   7882 C  CB    . ARG B 1 517 ? 25.784  41.847  25.051  1.00 45.54  ?  503 ARG B CB    1 
ATOM   7883 C  CG    . ARG B 1 517 ? 26.430  41.050  26.164  1.00 54.77  ?  503 ARG B CG    1 
ATOM   7884 C  CD    . ARG B 1 517 ? 27.932  40.936  25.950  1.00 74.68  ?  503 ARG B CD    1 
ATOM   7885 N  NE    . ARG B 1 517 ? 28.267  40.658  24.557  1.00 72.93  ?  503 ARG B NE    1 
ATOM   7886 C  CZ    . ARG B 1 517 ? 28.860  41.520  23.741  1.00 74.17  ?  503 ARG B CZ    1 
ATOM   7887 N  NH1   . ARG B 1 517 ? 29.203  42.733  24.145  1.00 72.76  ?  503 ARG B NH1   1 
ATOM   7888 N  NH2   . ARG B 1 517 ? 29.110  41.159  22.487  1.00 70.59  ?  503 ARG B NH2   1 
ATOM   7889 N  N     . VAL B 1 518 ? 23.706  42.534  27.729  1.00 37.02  ?  504 VAL B N     1 
ATOM   7890 C  CA    . VAL B 1 518 ? 23.522  43.154  29.036  1.00 43.61  ?  504 VAL B CA    1 
ATOM   7891 C  C     . VAL B 1 518 ? 23.900  42.163  30.129  1.00 48.26  ?  504 VAL B C     1 
ATOM   7892 O  O     . VAL B 1 518 ? 23.580  40.970  30.048  1.00 39.95  ?  504 VAL B O     1 
ATOM   7893 C  CB    . VAL B 1 518 ? 22.072  43.660  29.242  1.00 43.35  ?  504 VAL B CB    1 
ATOM   7894 C  CG1   . VAL B 1 518 ? 21.707  44.687  28.190  1.00 36.60  ?  504 VAL B CG1   1 
ATOM   7895 C  CG2   . VAL B 1 518 ? 21.077  42.502  29.222  1.00 40.73  ?  504 VAL B CG2   1 
ATOM   7896 N  N     . SER B 1 519 ? 24.580  42.676  31.157  1.00 37.51  ?  505 SER B N     1 
ATOM   7897 C  CA    . SER B 1 519 ? 24.921  41.921  32.349  1.00 43.09  ?  505 SER B CA    1 
ATOM   7898 C  C     . SER B 1 519 ? 24.434  42.600  33.621  1.00 47.28  ?  505 SER B C     1 
ATOM   7899 O  O     . SER B 1 519 ? 24.623  42.045  34.709  1.00 48.91  ?  505 SER B O     1 
ATOM   7900 C  CB    . SER B 1 519 ? 26.440  41.702  32.442  1.00 45.31  ?  505 SER B CB    1 
ATOM   7901 O  OG    . SER B 1 519 ? 27.143  42.915  32.248  1.00 66.16  ?  505 SER B OG    1 
ATOM   7902 N  N     . GLU B 1 520 ? 23.829  43.782  33.521  1.00 44.43  ?  506 GLU B N     1 
ATOM   7903 C  CA    . GLU B 1 520 ? 23.360  44.530  34.677  1.00 47.46  ?  506 GLU B CA    1 
ATOM   7904 C  C     . GLU B 1 520 ? 21.870  44.812  34.538  1.00 40.35  ?  506 GLU B C     1 
ATOM   7905 O  O     . GLU B 1 520 ? 21.375  45.048  33.431  1.00 46.19  ?  506 GLU B O     1 
ATOM   7906 C  CB    . GLU B 1 520 ? 24.129  45.850  34.823  1.00 48.04  ?  506 GLU B CB    1 
ATOM   7907 C  CG    . GLU B 1 520 ? 25.628  45.680  34.969  1.00 49.41  ?  506 GLU B CG    1 
ATOM   7908 C  CD    . GLU B 1 520 ? 26.029  45.356  36.390  1.00 67.70  ?  506 GLU B CD    1 
ATOM   7909 O  OE1   . GLU B 1 520 ? 25.563  46.063  37.309  1.00 76.79  ?  506 GLU B OE1   1 
ATOM   7910 O  OE2   . GLU B 1 520 ? 26.810  44.400  36.590  1.00 71.15  ?  506 GLU B OE2   1 
ATOM   7911 N  N     . ALA B 1 521 ? 21.162  44.788  35.673  1.00 47.12  ?  507 ALA B N     1 
ATOM   7912 C  CA    . ALA B 1 521 ? 19.712  44.973  35.658  1.00 53.92  ?  507 ALA B CA    1 
ATOM   7913 C  C     . ALA B 1 521 ? 19.325  46.374  35.201  1.00 46.10  ?  507 ALA B C     1 
ATOM   7914 O  O     . ALA B 1 521 ? 18.396  46.536  34.400  1.00 44.46  ?  507 ALA B O     1 
ATOM   7915 C  CB    . ALA B 1 521 ? 19.131  44.680  37.040  1.00 56.99  ?  507 ALA B CB    1 
ATOM   7916 N  N     . GLU B 1 522 ? 20.030  47.396  35.691  1.00 47.01  ?  508 GLU B N     1 
ATOM   7917 C  CA    . GLU B 1 522 ? 19.732  48.766  35.277  1.00 51.53  ?  508 GLU B CA    1 
ATOM   7918 C  C     . GLU B 1 522 ? 19.928  48.923  33.780  1.00 45.17  ?  508 GLU B C     1 
ATOM   7919 O  O     . GLU B 1 522 ? 19.134  49.586  33.102  1.00 56.13  ?  508 GLU B O     1 
ATOM   7920 C  CB    . GLU B 1 522 ? 20.623  49.752  36.030  1.00 48.58  ?  508 GLU B CB    1 
ATOM   7921 C  CG    . GLU B 1 522 ? 20.040  50.283  37.323  1.00 61.96  ?  508 GLU B CG    1 
ATOM   7922 C  CD    . GLU B 1 522 ? 21.063  51.050  38.138  1.00 80.56  ?  508 GLU B CD    1 
ATOM   7923 O  OE1   . GLU B 1 522 ? 21.777  51.896  37.555  1.00 80.57  ?  508 GLU B OE1   1 
ATOM   7924 O  OE2   . GLU B 1 522 ? 21.158  50.803  39.360  1.00 89.61  ?  508 GLU B OE2   1 
ATOM   7925 N  N     . GLN B 1 523 ? 20.987  48.312  33.252  1.00 48.14  ?  509 GLN B N     1 
ATOM   7926 C  CA    . GLN B 1 523 ? 21.230  48.315  31.817  1.00 46.60  ?  509 GLN B CA    1 
ATOM   7927 C  C     . GLN B 1 523 ? 20.083  47.637  31.074  1.00 50.50  ?  509 GLN B C     1 
ATOM   7928 O  O     . GLN B 1 523 ? 19.607  48.144  30.050  1.00 43.06  ?  509 GLN B O     1 
ATOM   7929 C  CB    . GLN B 1 523 ? 22.562  47.613  31.556  1.00 44.24  ?  509 GLN B CB    1 
ATOM   7930 C  CG    . GLN B 1 523 ? 23.236  47.874  30.233  1.00 60.36  ?  509 GLN B CG    1 
ATOM   7931 C  CD    . GLN B 1 523 ? 24.390  46.907  29.998  1.00 69.81  ?  509 GLN B CD    1 
ATOM   7932 O  OE1   . GLN B 1 523 ? 24.634  46.004  30.806  1.00 67.33  ?  509 GLN B OE1   1 
ATOM   7933 N  NE2   . GLN B 1 523 ? 25.108  47.096  28.897  1.00 65.64  ?  509 GLN B NE2   1 
ATOM   7934 N  N     . LEU B 1 524 ? 19.612  46.500  31.592  1.00 38.47  ?  510 LEU B N     1 
ATOM   7935 C  CA    . LEU B 1 524 ? 18.471  45.816  30.991  1.00 44.15  ?  510 LEU B CA    1 
ATOM   7936 C  C     . LEU B 1 524 ? 17.226  46.697  31.024  1.00 44.75  ?  510 LEU B C     1 
ATOM   7937 O  O     . LEU B 1 524 ? 16.505  46.811  30.027  1.00 40.64  ?  510 LEU B O     1 
ATOM   7938 C  CB    . LEU B 1 524 ? 18.220  44.492  31.714  1.00 42.52  ?  510 LEU B CB    1 
ATOM   7939 C  CG    . LEU B 1 524 ? 16.969  43.703  31.318  1.00 39.51  ?  510 LEU B CG    1 
ATOM   7940 C  CD1   . LEU B 1 524 ? 16.963  43.406  29.826  1.00 34.15  ?  510 LEU B CD1   1 
ATOM   7941 C  CD2   . LEU B 1 524 ? 16.885  42.422  32.121  1.00 33.27  ?  510 LEU B CD2   1 
ATOM   7942 N  N     . ALA B 1 525 ? 16.955  47.324  32.174  1.00 39.00  ?  511 ALA B N     1 
ATOM   7943 C  CA    . ALA B 1 525 ? 15.794  48.201  32.286  1.00 42.88  ?  511 ALA B CA    1 
ATOM   7944 C  C     . ALA B 1 525 ? 15.883  49.369  31.313  1.00 45.17  ?  511 ALA B C     1 
ATOM   7945 O  O     . ALA B 1 525 ? 14.889  49.727  30.669  1.00 46.18  ?  511 ALA B O     1 
ATOM   7946 C  CB    . ALA B 1 525 ? 15.660  48.715  33.719  1.00 44.05  ?  511 ALA B CB    1 
ATOM   7947 N  N     . ASP B 1 526 ? 17.069  49.970  31.183  1.00 47.13  ?  512 ASP B N     1 
ATOM   7948 C  CA    . ASP B 1 526 ? 17.251  51.052  30.218  1.00 47.97  ?  512 ASP B CA    1 
ATOM   7949 C  C     . ASP B 1 526 ? 17.030  50.562  28.793  1.00 47.77  ?  512 ASP B C     1 
ATOM   7950 O  O     . ASP B 1 526 ? 16.398  51.250  27.982  1.00 45.02  ?  512 ASP B O     1 
ATOM   7951 C  CB    . ASP B 1 526 ? 18.648  51.657  30.359  1.00 48.19  ?  512 ASP B CB    1 
ATOM   7952 C  CG    . ASP B 1 526 ? 18.839  52.375  31.675  1.00 59.27  ?  512 ASP B CG    1 
ATOM   7953 O  OD1   . ASP B 1 526 ? 17.821  52.688  32.332  1.00 72.44  ?  512 ASP B OD1   1 
ATOM   7954 O  OD2   . ASP B 1 526 ? 20.006  52.625  32.049  1.00 67.06  ?  512 ASP B OD2   1 
ATOM   7955 N  N     . VAL B 1 527 ? 17.550  49.378  28.468  1.00 41.82  ?  513 VAL B N     1 
ATOM   7956 C  CA    . VAL B 1 527 ? 17.396  48.842  27.120  1.00 38.44  ?  513 VAL B CA    1 
ATOM   7957 C  C     . VAL B 1 527 ? 15.935  48.511  26.846  1.00 44.85  ?  513 VAL B C     1 
ATOM   7958 O  O     . VAL B 1 527 ? 15.429  48.738  25.739  1.00 40.83  ?  513 VAL B O     1 
ATOM   7959 C  CB    . VAL B 1 527 ? 18.313  47.619  26.929  1.00 43.87  ?  513 VAL B CB    1 
ATOM   7960 C  CG1   . VAL B 1 527 ? 17.859  46.774  25.748  1.00 41.46  ?  513 VAL B CG1   1 
ATOM   7961 C  CG2   . VAL B 1 527 ? 19.762  48.066  26.746  1.00 45.50  ?  513 VAL B CG2   1 
ATOM   7962 N  N     . LEU B 1 528 ? 15.230  47.980  27.849  1.00 42.56  ?  514 LEU B N     1 
ATOM   7963 C  CA    . LEU B 1 528 ? 13.812  47.681  27.675  1.00 42.91  ?  514 LEU B CA    1 
ATOM   7964 C  C     . LEU B 1 528 ? 13.001  48.947  27.427  1.00 38.06  ?  514 LEU B C     1 
ATOM   7965 O  O     . LEU B 1 528 ? 12.056  48.935  26.628  1.00 45.00  ?  514 LEU B O     1 
ATOM   7966 C  CB    . LEU B 1 528 ? 13.284  46.925  28.894  1.00 38.66  ?  514 LEU B CB    1 
ATOM   7967 C  CG    . LEU B 1 528 ? 13.790  45.481  28.989  1.00 33.59  ?  514 LEU B CG    1 
ATOM   7968 C  CD1   . LEU B 1 528 ? 13.543  44.903  30.374  1.00 37.62  ?  514 LEU B CD1   1 
ATOM   7969 C  CD2   . LEU B 1 528 ? 13.161  44.607  27.909  1.00 31.69  ?  514 LEU B CD2   1 
ATOM   7970 N  N     . GLU B 1 529 ? 13.353  50.049  28.101  1.00 41.40  ?  515 GLU B N     1 
ATOM   7971 C  CA    . GLU B 1 529 ? 12.725  51.335  27.800  1.00 42.21  ?  515 GLU B CA    1 
ATOM   7972 C  C     . GLU B 1 529 ? 12.952  51.725  26.347  1.00 52.58  ?  515 GLU B C     1 
ATOM   7973 O  O     . GLU B 1 529 ? 12.034  52.207  25.674  1.00 43.94  ?  515 GLU B O     1 
ATOM   7974 C  CB    . GLU B 1 529 ? 13.262  52.429  28.722  1.00 51.41  ?  515 GLU B CB    1 
ATOM   7975 C  CG    . GLU B 1 529 ? 12.931  52.255  30.191  1.00 66.00  ?  515 GLU B CG    1 
ATOM   7976 C  CD    . GLU B 1 529 ? 13.521  53.362  31.049  1.00 83.03  ?  515 GLU B CD    1 
ATOM   7977 O  OE1   . GLU B 1 529 ? 13.471  54.538  30.623  1.00 76.61  ?  515 GLU B OE1   1 
ATOM   7978 O  OE2   . GLU B 1 529 ? 14.049  53.055  32.141  1.00 83.50  ?  515 GLU B OE2   1 
ATOM   7979 N  N     . LYS B 1 530 ? 14.178  51.531  25.853  1.00 51.69  ?  516 LYS B N     1 
ATOM   7980 C  CA    . LYS B 1 530 ? 14.525  51.961  24.503  1.00 42.45  ?  516 LYS B CA    1 
ATOM   7981 C  C     . LYS B 1 530 ? 13.712  51.205  23.462  1.00 43.13  ?  516 LYS B C     1 
ATOM   7982 O  O     . LYS B 1 530 ? 13.283  51.790  22.460  1.00 49.34  ?  516 LYS B O     1 
ATOM   7983 C  CB    . LYS B 1 530 ? 16.027  51.760  24.272  1.00 49.53  ?  516 LYS B CB    1 
ATOM   7984 C  CG    . LYS B 1 530 ? 16.535  52.063  22.861  1.00 54.45  ?  516 LYS B CG    1 
ATOM   7985 C  CD    . LYS B 1 530 ? 16.171  53.461  22.405  1.00 54.72  ?  516 LYS B CD    1 
ATOM   7986 C  CE    . LYS B 1 530 ? 17.149  53.982  21.364  1.00 47.38  ?  516 LYS B CE    1 
ATOM   7987 N  NZ    . LYS B 1 530 ? 17.697  55.323  21.745  1.00 52.86  ?  516 LYS B NZ    1 
ATOM   7988 N  N     . VAL B 1 531 ? 13.480  49.909  23.684  1.00 38.11  ?  517 VAL B N     1 
ATOM   7989 C  CA    . VAL B 1 531 ? 12.813  49.057  22.703  1.00 44.39  ?  517 VAL B CA    1 
ATOM   7990 C  C     . VAL B 1 531 ? 11.312  48.935  22.967  1.00 36.19  ?  517 VAL B C     1 
ATOM   7991 O  O     . VAL B 1 531 ? 10.646  48.118  22.331  1.00 43.92  ?  517 VAL B O     1 
ATOM   7992 C  CB    . VAL B 1 531 ? 13.468  47.663  22.641  1.00 51.22  ?  517 VAL B CB    1 
ATOM   7993 C  CG1   . VAL B 1 531 ? 14.964  47.791  22.402  1.00 46.76  ?  517 VAL B CG1   1 
ATOM   7994 C  CG2   . VAL B 1 531 ? 13.188  46.865  23.918  1.00 36.44  ?  517 VAL B CG2   1 
ATOM   7995 N  N     . ALA B 1 532 ? 10.759  49.767  23.853  1.00 46.29  ?  518 ALA B N     1 
ATOM   7996 C  CA    . ALA B 1 532 ? 9.391   49.568  24.330  1.00 51.79  ?  518 ALA B CA    1 
ATOM   7997 C  C     . ALA B 1 532 ? 8.385   49.543  23.184  1.00 51.75  ?  518 ALA B C     1 
ATOM   7998 O  O     . ALA B 1 532 ? 7.465   48.716  23.176  1.00 50.94  ?  518 ALA B O     1 
ATOM   7999 C  CB    . ALA B 1 532 ? 9.020   50.654  25.340  1.00 44.42  ?  518 ALA B CB    1 
ATOM   8000 N  N     . HIS B 1 533 ? 8.537   50.443  22.210  1.00 52.64  ?  519 HIS B N     1 
ATOM   8001 C  CA    . HIS B 1 533 ? 7.555   50.611  21.148  1.00 39.61  ?  519 HIS B CA    1 
ATOM   8002 C  C     . HIS B 1 533 ? 7.938   49.871  19.871  1.00 40.07  ?  519 HIS B C     1 
ATOM   8003 O  O     . HIS B 1 533 ? 7.393   50.172  18.803  1.00 38.94  ?  519 HIS B O     1 
ATOM   8004 C  CB    . HIS B 1 533 ? 7.354   52.099  20.861  1.00 42.50  ?  519 HIS B CB    1 
ATOM   8005 C  CG    . HIS B 1 533 ? 6.975   52.894  22.070  1.00 48.83  ?  519 HIS B CG    1 
ATOM   8006 N  ND1   . HIS B 1 533 ? 7.905   53.516  22.874  1.00 65.71  ?  519 HIS B ND1   1 
ATOM   8007 C  CD2   . HIS B 1 533 ? 5.767   53.149  22.625  1.00 67.42  ?  519 HIS B CD2   1 
ATOM   8008 C  CE1   . HIS B 1 533 ? 7.285   54.131  23.865  1.00 57.84  ?  519 HIS B CE1   1 
ATOM   8009 N  NE2   . HIS B 1 533 ? 5.987   53.924  23.738  1.00 69.35  ?  519 HIS B NE2   1 
ATOM   8010 N  N     . HIS B 1 534 ? 8.857   48.909  19.977  1.00 38.67  ?  520 HIS B N     1 
ATOM   8011 C  CA    . HIS B 1 534 ? 9.203   47.943  18.926  1.00 40.59  ?  520 HIS B CA    1 
ATOM   8012 C  C     . HIS B 1 534 ? 9.183   48.559  17.529  1.00 35.94  ?  520 HIS B C     1 
ATOM   8013 O  O     . HIS B 1 534 ? 8.552   48.055  16.599  1.00 38.45  ?  520 HIS B O     1 
ATOM   8014 C  CB    . HIS B 1 534 ? 8.295   46.712  18.993  1.00 34.99  ?  520 HIS B CB    1 
ATOM   8015 C  CG    . HIS B 1 534 ? 6.837   47.024  18.859  1.00 38.27  ?  520 HIS B CG    1 
ATOM   8016 N  ND1   . HIS B 1 534 ? 6.053   47.390  19.931  1.00 40.94  ?  520 HIS B ND1   1 
ATOM   8017 C  CD2   . HIS B 1 534 ? 6.022   47.023  17.778  1.00 38.81  ?  520 HIS B CD2   1 
ATOM   8018 C  CE1   . HIS B 1 534 ? 4.817   47.602  19.517  1.00 40.15  ?  520 HIS B CE1   1 
ATOM   8019 N  NE2   . HIS B 1 534 ? 4.770   47.383  18.215  1.00 50.98  ?  520 HIS B NE2   1 
ATOM   8020 N  N     . GLU B 1 535 ? 9.892   49.674  17.385  1.00 38.54  ?  521 GLU B N     1 
ATOM   8021 C  CA    . GLU B 1 535 ? 10.060  50.267  16.067  1.00 39.15  ?  521 GLU B CA    1 
ATOM   8022 C  C     . GLU B 1 535 ? 10.973  49.424  15.199  1.00 37.90  ?  521 GLU B C     1 
ATOM   8023 O  O     . GLU B 1 535 ? 10.937  49.539  13.971  1.00 39.24  ?  521 GLU B O     1 
ATOM   8024 C  CB    . GLU B 1 535 ? 10.596  51.691  16.181  1.00 41.79  ?  521 GLU B CB    1 
ATOM   8025 C  CG    . GLU B 1 535 ? 9.710   52.609  16.999  1.00 43.85  ?  521 GLU B CG    1 
ATOM   8026 C  CD    . GLU B 1 535 ? 9.991   54.063  16.724  1.00 55.99  ?  521 GLU B CD    1 
ATOM   8027 O  OE1   . GLU B 1 535 ? 11.071  54.540  17.127  1.00 77.29  ?  521 GLU B OE1   1 
ATOM   8028 O  OE2   . GLU B 1 535 ? 9.138   54.727  16.099  1.00 76.48  ?  521 GLU B OE2   1 
ATOM   8029 N  N     . ARG B 1 536 ? 11.790  48.580  15.816  1.00 36.46  ?  522 ARG B N     1 
ATOM   8030 C  CA    . ARG B 1 536 ? 12.720  47.732  15.099  1.00 38.17  ?  522 ARG B CA    1 
ATOM   8031 C  C     . ARG B 1 536 ? 12.822  46.395  15.818  1.00 32.93  ?  522 ARG B C     1 
ATOM   8032 O  O     . ARG B 1 536 ? 12.417  46.256  16.976  1.00 36.22  ?  522 ARG B O     1 
ATOM   8033 C  CB    . ARG B 1 536 ? 14.100  48.397  15.030  1.00 41.70  ?  522 ARG B CB    1 
ATOM   8034 C  CG    . ARG B 1 536 ? 14.250  49.447  13.936  1.00 50.55  ?  522 ARG B CG    1 
ATOM   8035 C  CD    . ARG B 1 536 ? 15.153  50.595  14.370  1.00 67.34  ?  522 ARG B CD    1 
ATOM   8036 N  NE    . ARG B 1 536 ? 15.304  51.596  13.319  1.00 78.41  ?  522 ARG B NE    1 
ATOM   8037 C  CZ    . ARG B 1 536 ? 14.939  52.866  13.429  1.00 79.06  ?  522 ARG B CZ    1 
ATOM   8038 N  NH1   . ARG B 1 536 ? 14.464  53.352  14.565  1.00 79.33  ?  522 ARG B NH1   1 
ATOM   8039 N  NH2   . ARG B 1 536 ? 15.080  53.676  12.382  1.00 87.98  ?  522 ARG B NH2   1 
ATOM   8040 N  N     . LEU B 1 537 ? 13.305  45.386  15.098  1.00 31.87  ?  523 LEU B N     1 
ATOM   8041 C  CA    . LEU B 1 537 ? 13.595  44.110  15.739  1.00 30.45  ?  523 LEU B CA    1 
ATOM   8042 C  C     . LEU B 1 537 ? 14.678  44.320  16.788  1.00 33.60  ?  523 LEU B C     1 
ATOM   8043 O  O     . LEU B 1 537 ? 15.676  44.997  16.534  1.00 35.11  ?  523 LEU B O     1 
ATOM   8044 C  CB    . LEU B 1 537 ? 14.042  43.071  14.712  1.00 29.37  ?  523 LEU B CB    1 
ATOM   8045 C  CG    . LEU B 1 537 ? 14.268  41.640  15.225  1.00 36.07  ?  523 LEU B CG    1 
ATOM   8046 C  CD1   . LEU B 1 537 ? 13.775  40.604  14.214  1.00 29.38  ?  523 LEU B CD1   1 
ATOM   8047 C  CD2   . LEU B 1 537 ? 15.735  41.388  15.562  1.00 29.20  ?  523 LEU B CD2   1 
ATOM   8048 N  N     . SER B 1 538 ? 14.472  43.767  17.977  1.00 36.69  ?  524 SER B N     1 
ATOM   8049 C  CA    . SER B 1 538 ? 15.405  43.935  19.083  1.00 38.09  ?  524 SER B CA    1 
ATOM   8050 C  C     . SER B 1 538 ? 15.846  42.569  19.584  1.00 43.44  ?  524 SER B C     1 
ATOM   8051 O  O     . SER B 1 538 ? 15.013  41.680  19.792  1.00 39.78  ?  524 SER B O     1 
ATOM   8052 C  CB    . SER B 1 538 ? 14.783  44.741  20.223  1.00 36.85  ?  524 SER B CB    1 
ATOM   8053 O  OG    . SER B 1 538 ? 13.975  45.792  19.717  1.00 54.81  ?  524 SER B OG    1 
ATOM   8054 N  N     . LEU B 1 539 ? 17.153  42.396  19.742  1.00 36.92  ?  525 LEU B N     1 
ATOM   8055 C  CA    . LEU B 1 539 ? 17.728  41.176  20.298  1.00 34.70  ?  525 LEU B CA    1 
ATOM   8056 C  C     . LEU B 1 539 ? 18.546  41.572  21.519  1.00 38.42  ?  525 LEU B C     1 
ATOM   8057 O  O     . LEU B 1 539 ? 19.569  42.250  21.392  1.00 32.68  ?  525 LEU B O     1 
ATOM   8058 C  CB    . LEU B 1 539 ? 18.584  40.435  19.271  1.00 31.49  ?  525 LEU B CB    1 
ATOM   8059 C  CG    . LEU B 1 539 ? 18.874  38.966  19.620  1.00 37.21  ?  525 LEU B CG    1 
ATOM   8060 C  CD1   . LEU B 1 539 ? 18.922  38.094  18.374  1.00 35.26  ?  525 LEU B CD1   1 
ATOM   8061 C  CD2   . LEU B 1 539 ? 20.171  38.836  20.404  1.00 37.19  ?  525 LEU B CD2   1 
ATOM   8062 N  N     . ILE B 1 540 ? 18.090  41.175  22.698  1.00 38.05  ?  526 ILE B N     1 
ATOM   8063 C  CA    . ILE B 1 540 ? 18.772  41.492  23.945  1.00 40.82  ?  526 ILE B CA    1 
ATOM   8064 C  C     . ILE B 1 540 ? 19.396  40.200  24.450  1.00 43.15  ?  526 ILE B C     1 
ATOM   8065 O  O     . ILE B 1 540 ? 18.686  39.261  24.832  1.00 31.73  ?  526 ILE B O     1 
ATOM   8066 C  CB    . ILE B 1 540 ? 17.816  42.096  24.981  1.00 36.01  ?  526 ILE B CB    1 
ATOM   8067 C  CG1   . ILE B 1 540 ? 17.113  43.322  24.402  1.00 32.84  ?  526 ILE B CG1   1 
ATOM   8068 C  CG2   . ILE B 1 540 ? 18.572  42.459  26.254  1.00 40.93  ?  526 ILE B CG2   1 
ATOM   8069 C  CD1   . ILE B 1 540 ? 15.868  43.726  25.166  1.00 37.36  ?  526 ILE B CD1   1 
ATOM   8070 N  N     . GLU B 1 541 ? 20.726  40.146  24.441  1.00 37.68  ?  527 GLU B N     1 
ATOM   8071 C  CA    . GLU B 1 541 ? 21.465  38.994  24.944  1.00 37.08  ?  527 GLU B CA    1 
ATOM   8072 C  C     . GLU B 1 541 ? 21.667  39.188  26.443  1.00 36.68  ?  527 GLU B C     1 
ATOM   8073 O  O     . GLU B 1 541 ? 22.490  40.006  26.869  1.00 39.22  ?  527 GLU B O     1 
ATOM   8074 C  CB    . GLU B 1 541 ? 22.795  38.843  24.208  1.00 31.87  ?  527 GLU B CB    1 
ATOM   8075 C  CG    . GLU B 1 541 ? 23.553  37.566  24.527  1.00 36.05  ?  527 GLU B CG    1 
ATOM   8076 C  CD    . GLU B 1 541 ? 24.921  37.498  23.842  1.00 44.49  ?  527 GLU B CD    1 
ATOM   8077 O  OE1   . GLU B 1 541 ? 25.317  38.473  23.162  1.00 39.10  ?  527 GLU B OE1   1 
ATOM   8078 O  OE2   . GLU B 1 541 ? 25.618  36.475  24.012  1.00 42.29  ?  527 GLU B OE2   1 
ATOM   8079 N  N     . VAL B 1 542 ? 20.931  38.420  27.237  1.00 35.79  ?  528 VAL B N     1 
ATOM   8080 C  CA    . VAL B 1 542 ? 20.914  38.567  28.687  1.00 33.06  ?  528 VAL B CA    1 
ATOM   8081 C  C     . VAL B 1 542 ? 21.935  37.608  29.280  1.00 38.51  ?  528 VAL B C     1 
ATOM   8082 O  O     . VAL B 1 542 ? 21.824  36.387  29.118  1.00 39.26  ?  528 VAL B O     1 
ATOM   8083 C  CB    . VAL B 1 542 ? 19.513  38.294  29.253  1.00 31.64  ?  528 VAL B CB    1 
ATOM   8084 C  CG1   . VAL B 1 542 ? 19.475  38.579  30.749  1.00 33.93  ?  528 VAL B CG1   1 
ATOM   8085 C  CG2   . VAL B 1 542 ? 18.473  39.117  28.511  1.00 30.37  ?  528 VAL B CG2   1 
ATOM   8086 N  N     . MET B 1 543 ? 22.921  38.161  29.979  1.00 40.51  ?  529 MET B N     1 
ATOM   8087 C  CA    . MET B 1 543 ? 23.997  37.384  30.573  1.00 33.19  ?  529 MET B CA    1 
ATOM   8088 C  C     . MET B 1 543 ? 23.576  36.937  31.967  1.00 45.93  ?  529 MET B C     1 
ATOM   8089 O  O     . MET B 1 543 ? 23.386  37.770  32.860  1.00 39.29  ?  529 MET B O     1 
ATOM   8090 C  CB    . MET B 1 543 ? 25.271  38.225  30.639  1.00 38.78  ?  529 MET B CB    1 
ATOM   8091 C  CG    . MET B 1 543 ? 25.942  38.465  29.296  1.00 38.03  ?  529 MET B CG    1 
ATOM   8092 S  SD    . MET B 1 543 ? 26.275  36.931  28.416  1.00 59.85  ?  529 MET B SD    1 
ATOM   8093 C  CE    . MET B 1 543 ? 26.500  37.539  26.758  1.00 56.35  ?  529 MET B CE    1 
ATOM   8094 N  N     . LEU B 1 544 ? 23.453  35.628  32.159  1.00 37.88  ?  530 LEU B N     1 
ATOM   8095 C  CA    . LEU B 1 544 ? 22.995  35.082  33.426  1.00 38.87  ?  530 LEU B CA    1 
ATOM   8096 C  C     . LEU B 1 544 ? 23.939  33.981  33.881  1.00 37.62  ?  530 LEU B C     1 
ATOM   8097 O  O     . LEU B 1 544 ? 24.627  33.368  33.056  1.00 42.39  ?  530 LEU B O     1 
ATOM   8098 C  CB    . LEU B 1 544 ? 21.561  34.538  33.305  1.00 32.21  ?  530 LEU B CB    1 
ATOM   8099 C  CG    . LEU B 1 544 ? 20.472  35.593  33.066  1.00 39.14  ?  530 LEU B CG    1 
ATOM   8100 C  CD1   . LEU B 1 544 ? 19.185  34.969  32.531  1.00 32.43  ?  530 LEU B CD1   1 
ATOM   8101 C  CD2   . LEU B 1 544 ? 20.188  36.389  34.337  1.00 38.96  ?  530 LEU B CD2   1 
ATOM   8102 N  N     . PRO B 1 545 ? 24.016  33.726  35.187  1.00 36.35  ?  531 PRO B N     1 
ATOM   8103 C  CA    . PRO B 1 545 ? 24.939  32.697  35.679  1.00 35.64  ?  531 PRO B CA    1 
ATOM   8104 C  C     . PRO B 1 545 ? 24.546  31.311  35.189  1.00 48.60  ?  531 PRO B C     1 
ATOM   8105 O  O     . PRO B 1 545 ? 23.373  31.021  34.934  1.00 37.50  ?  531 PRO B O     1 
ATOM   8106 C  CB    . PRO B 1 545 ? 24.821  32.809  37.204  1.00 37.26  ?  531 PRO B CB    1 
ATOM   8107 C  CG    . PRO B 1 545 ? 24.261  34.178  37.451  1.00 40.07  ?  531 PRO B CG    1 
ATOM   8108 C  CD    . PRO B 1 545 ? 23.353  34.443  36.290  1.00 43.38  ?  531 PRO B CD    1 
ATOM   8109 N  N     . LYS B 1 546 ? 25.559  30.450  35.059  1.00 49.29  ?  532 LYS B N     1 
ATOM   8110 C  CA    . LYS B 1 546 ? 25.343  29.104  34.535  1.00 40.75  ?  532 LYS B CA    1 
ATOM   8111 C  C     . LYS B 1 546 ? 24.415  28.294  35.434  1.00 37.38  ?  532 LYS B C     1 
ATOM   8112 O  O     . LYS B 1 546 ? 23.618  27.484  34.948  1.00 46.08  ?  532 LYS B O     1 
ATOM   8113 C  CB    . LYS B 1 546 ? 26.687  28.396  34.372  1.00 46.85  ?  532 LYS B CB    1 
ATOM   8114 C  CG    . LYS B 1 546 ? 26.718  27.358  33.272  1.00 56.05  ?  532 LYS B CG    1 
ATOM   8115 C  CD    . LYS B 1 546 ? 28.138  26.867  33.025  1.00 48.47  ?  532 LYS B CD    1 
ATOM   8116 C  CE    . LYS B 1 546 ? 28.975  27.908  32.303  1.00 53.73  ?  532 LYS B CE    1 
ATOM   8117 N  NZ    . LYS B 1 546 ? 30.207  27.298  31.711  1.00 58.07  ?  532 LYS B NZ    1 
ATOM   8118 N  N     . ALA B 1 547 ? 24.520  28.482  36.748  1.00 40.55  ?  533 ALA B N     1 
ATOM   8119 C  CA    . ALA B 1 547 ? 23.766  27.703  37.721  1.00 41.31  ?  533 ALA B CA    1 
ATOM   8120 C  C     . ALA B 1 547 ? 22.551  28.434  38.276  1.00 48.85  ?  533 ALA B C     1 
ATOM   8121 O  O     . ALA B 1 547 ? 21.875  27.892  39.156  1.00 46.96  ?  533 ALA B O     1 
ATOM   8122 C  CB    . ALA B 1 547 ? 24.680  27.288  38.880  1.00 41.59  ?  533 ALA B CB    1 
ATOM   8123 N  N     . ASP B 1 548 ? 22.253  29.640  37.794  1.00 44.38  ?  534 ASP B N     1 
ATOM   8124 C  CA    . ASP B 1 548 ? 21.172  30.424  38.380  1.00 47.62  ?  534 ASP B CA    1 
ATOM   8125 C  C     . ASP B 1 548 ? 19.824  29.838  37.984  1.00 42.50  ?  534 ASP B C     1 
ATOM   8126 O  O     . ASP B 1 548 ? 19.579  29.551  36.809  1.00 35.93  ?  534 ASP B O     1 
ATOM   8127 C  CB    . ASP B 1 548 ? 21.264  31.882  37.943  1.00 48.32  ?  534 ASP B CB    1 
ATOM   8128 C  CG    . ASP B 1 548 ? 20.453  32.803  38.831  1.00 51.06  ?  534 ASP B CG    1 
ATOM   8129 O  OD1   . ASP B 1 548 ? 19.798  32.305  39.773  1.00 47.97  ?  534 ASP B OD1   1 
ATOM   8130 O  OD2   . ASP B 1 548 ? 20.467  34.027  38.585  1.00 60.55  ?  534 ASP B OD2   1 
ATOM   8131 N  N     . ILE B 1 549 ? 18.936  29.706  38.964  1.00 48.71  ?  535 ILE B N     1 
ATOM   8132 C  CA    . ILE B 1 549 ? 17.735  28.891  38.812  1.00 47.20  ?  535 ILE B CA    1 
ATOM   8133 C  C     . ILE B 1 549 ? 16.493  29.686  39.211  1.00 40.78  ?  535 ILE B C     1 
ATOM   8134 O  O     . ILE B 1 549 ? 16.535  30.460  40.180  1.00 54.41  ?  535 ILE B O     1 
ATOM   8135 C  CB    . ILE B 1 549 ? 17.882  27.602  39.644  1.00 48.71  ?  535 ILE B CB    1 
ATOM   8136 C  CG1   . ILE B 1 549 ? 17.326  26.402  38.904  1.00 53.23  ?  535 ILE B CG1   1 
ATOM   8137 C  CG2   . ILE B 1 549 ? 17.229  27.714  41.021  1.00 59.96  ?  535 ILE B CG2   1 
ATOM   8138 C  CD1   . ILE B 1 549 ? 17.722  25.093  39.540  1.00 50.44  ?  535 ILE B CD1   1 
ATOM   8139 N  N     . PRO B 1 550 ? 15.395  29.584  38.464  1.00 41.89  ?  536 PRO B N     1 
ATOM   8140 C  CA    . PRO B 1 550 ? 14.127  30.172  38.914  1.00 43.47  ?  536 PRO B CA    1 
ATOM   8141 C  C     . PRO B 1 550 ? 13.493  29.307  39.989  1.00 53.36  ?  536 PRO B C     1 
ATOM   8142 O  O     . PRO B 1 550 ? 13.794  28.107  40.083  1.00 42.48  ?  536 PRO B O     1 
ATOM   8143 C  CB    . PRO B 1 550 ? 13.268  30.199  37.638  1.00 45.50  ?  536 PRO B CB    1 
ATOM   8144 C  CG    . PRO B 1 550 ? 14.196  29.843  36.507  1.00 43.99  ?  536 PRO B CG    1 
ATOM   8145 C  CD    . PRO B 1 550 ? 15.287  29.029  37.107  1.00 48.73  ?  536 PRO B CD    1 
ATOM   8146 N  N     . PRO B 1 551 ? 12.620  29.879  40.828  1.00 50.55  ?  537 PRO B N     1 
ATOM   8147 C  CA    . PRO B 1 551 ? 12.070  29.095  41.952  1.00 46.33  ?  537 PRO B CA    1 
ATOM   8148 C  C     . PRO B 1 551 ? 11.309  27.843  41.537  1.00 53.31  ?  537 PRO B C     1 
ATOM   8149 O  O     . PRO B 1 551 ? 11.403  26.819  42.226  1.00 49.95  ?  537 PRO B O     1 
ATOM   8150 C  CB    . PRO B 1 551 ? 11.161  30.104  42.673  1.00 45.29  ?  537 PRO B CB    1 
ATOM   8151 C  CG    . PRO B 1 551 ? 10.957  31.232  41.702  1.00 58.04  ?  537 PRO B CG    1 
ATOM   8152 C  CD    . PRO B 1 551 ? 12.196  31.287  40.870  1.00 45.62  ?  537 PRO B CD    1 
ATOM   8153 N  N     . LEU B 1 552 ? 10.551  27.888  40.437  1.00 49.60  ?  538 LEU B N     1 
ATOM   8154 C  CA    . LEU B 1 552 ? 9.763   26.720  40.050  1.00 48.06  ?  538 LEU B CA    1 
ATOM   8155 C  C     . LEU B 1 552 ? 10.654  25.547  39.662  1.00 60.34  ?  538 LEU B C     1 
ATOM   8156 O  O     . LEU B 1 552 ? 10.363  24.398  40.017  1.00 65.78  ?  538 LEU B O     1 
ATOM   8157 C  CB    . LEU B 1 552 ? 8.819   27.066  38.900  1.00 51.59  ?  538 LEU B CB    1 
ATOM   8158 C  CG    . LEU B 1 552 ? 8.198   25.859  38.196  1.00 49.63  ?  538 LEU B CG    1 
ATOM   8159 C  CD1   . LEU B 1 552 ? 7.064   25.298  39.029  1.00 44.15  ?  538 LEU B CD1   1 
ATOM   8160 C  CD2   . LEU B 1 552 ? 7.711   26.230  36.806  1.00 51.45  ?  538 LEU B CD2   1 
ATOM   8161 N  N     . LEU B 1 553 ? 11.741  25.809  38.931  1.00 62.33  ?  539 LEU B N     1 
ATOM   8162 C  CA    . LEU B 1 553 ? 12.590  24.708  38.490  1.00 64.68  ?  539 LEU B CA    1 
ATOM   8163 C  C     . LEU B 1 553 ? 13.380  24.113  39.650  1.00 67.39  ?  539 LEU B C     1 
ATOM   8164 O  O     . LEU B 1 553 ? 13.660  22.909  39.651  1.00 66.94  ?  539 LEU B O     1 
ATOM   8165 C  CB    . LEU B 1 553 ? 13.508  25.165  37.352  1.00 49.10  ?  539 LEU B CB    1 
ATOM   8166 C  CG    . LEU B 1 553 ? 14.686  24.269  36.958  1.00 61.57  ?  539 LEU B CG    1 
ATOM   8167 C  CD1   . LEU B 1 553 ? 14.226  23.153  36.036  1.00 61.57  ?  539 LEU B CD1   1 
ATOM   8168 C  CD2   . LEU B 1 553 ? 15.734  25.095  36.238  1.00 52.89  ?  539 LEU B CD2   1 
ATOM   8169 N  N     . GLY B 1 554 ? 13.729  24.926  40.650  1.00 57.79  ?  540 GLY B N     1 
ATOM   8170 C  CA    . GLY B 1 554 ? 14.311  24.373  41.862  1.00 58.10  ?  540 GLY B CA    1 
ATOM   8171 C  C     . GLY B 1 554 ? 13.370  23.413  42.565  1.00 69.82  ?  540 GLY B C     1 
ATOM   8172 O  O     . GLY B 1 554 ? 13.785  22.351  43.036  1.00 62.98  ?  540 GLY B O     1 
ATOM   8173 N  N     . ALA B 1 555 ? 12.089  23.779  42.652  1.00 69.93  ?  541 ALA B N     1 
ATOM   8174 C  CA    . ALA B 1 555 ? 11.093  22.872  43.212  1.00 67.33  ?  541 ALA B CA    1 
ATOM   8175 C  C     . ALA B 1 555 ? 10.920  21.639  42.336  1.00 74.08  ?  541 ALA B C     1 
ATOM   8176 O  O     . ALA B 1 555 ? 10.726  20.530  42.848  1.00 69.38  ?  541 ALA B O     1 
ATOM   8177 C  CB    . ALA B 1 555 ? 9.763   23.597  43.389  1.00 68.82  ?  541 ALA B CB    1 
ATOM   8178 N  N     . ILE B 1 556 ? 10.965  21.816  41.015  1.00 69.90  ?  542 ILE B N     1 
ATOM   8179 C  CA    . ILE B 1 556 ? 10.851  20.674  40.112  1.00 70.99  ?  542 ILE B CA    1 
ATOM   8180 C  C     . ILE B 1 556 ? 12.021  19.721  40.322  1.00 76.55  ?  542 ILE B C     1 
ATOM   8181 O  O     . ILE B 1 556 ? 11.837  18.505  40.448  1.00 74.42  ?  542 ILE B O     1 
ATOM   8182 C  CB    . ILE B 1 556 ? 10.762  21.147  38.651  1.00 72.91  ?  542 ILE B CB    1 
ATOM   8183 C  CG1   . ILE B 1 556 ? 9.332   21.577  38.317  1.00 57.77  ?  542 ILE B CG1   1 
ATOM   8184 C  CG2   . ILE B 1 556 ? 11.224  20.044  37.706  1.00 67.49  ?  542 ILE B CG2   1 
ATOM   8185 C  CD1   . ILE B 1 556 ? 9.107   21.864  36.849  1.00 52.79  ?  542 ILE B CD1   1 
ATOM   8186 N  N     . THR B 1 557 ? 13.243  20.263  40.401  1.00 75.89  ?  543 THR B N     1 
ATOM   8187 C  CA    . THR B 1 557 ? 14.414  19.409  40.590  1.00 74.50  ?  543 THR B CA    1 
ATOM   8188 C  C     . THR B 1 557 ? 14.363  18.696  41.936  1.00 73.31  ?  543 THR B C     1 
ATOM   8189 O  O     . THR B 1 557 ? 14.811  17.550  42.056  1.00 76.91  ?  543 THR B O     1 
ATOM   8190 C  CB    . THR B 1 557 ? 15.705  20.226  40.471  1.00 64.93  ?  543 THR B CB    1 
ATOM   8191 O  OG1   . THR B 1 557 ? 15.682  21.327  41.388  1.00 68.67  ?  543 THR B OG1   1 
ATOM   8192 C  CG2   . THR B 1 557 ? 15.878  20.755  39.053  1.00 55.32  ?  543 THR B CG2   1 
ATOM   8193 N  N     . LYS B 1 558 ? 13.821  19.360  42.960  1.00 72.72  ?  544 LYS B N     1 
ATOM   8194 C  CA    . LYS B 1 558 ? 13.685  18.727  44.268  1.00 77.04  ?  544 LYS B CA    1 
ATOM   8195 C  C     . LYS B 1 558 ? 12.640  17.617  44.262  1.00 84.58  ?  544 LYS B C     1 
ATOM   8196 O  O     . LYS B 1 558 ? 12.764  16.651  45.024  1.00 86.62  ?  544 LYS B O     1 
ATOM   8197 C  CB    . LYS B 1 558 ? 13.328  19.773  45.324  1.00 71.71  ?  544 LYS B CB    1 
ATOM   8198 C  CG    . LYS B 1 558 ? 14.488  20.661  45.743  1.00 83.39  ?  544 LYS B CG    1 
ATOM   8199 C  CD    . LYS B 1 558 ? 15.717  19.836  46.092  1.00 88.84  ?  544 LYS B CD    1 
ATOM   8200 C  CE    . LYS B 1 558 ? 16.419  20.388  47.322  1.00 85.88  ?  544 LYS B CE    1 
ATOM   8201 N  NZ    . LYS B 1 558 ? 16.948  19.300  48.194  1.00 86.81  ?  544 LYS B NZ    1 
ATOM   8202 N  N     . ALA B 1 559 ? 11.621  17.725  43.405  1.00 83.33  ?  545 ALA B N     1 
ATOM   8203 C  CA    . ALA B 1 559 ? 10.605  16.680  43.334  1.00 82.16  ?  545 ALA B CA    1 
ATOM   8204 C  C     . ALA B 1 559 ? 11.149  15.420  42.671  1.00 96.23  ?  545 ALA B C     1 
ATOM   8205 O  O     . ALA B 1 559 ? 10.757  14.303  43.034  1.00 91.70  ?  545 ALA B O     1 
ATOM   8206 C  CB    . ALA B 1 559 ? 9.374   17.196  42.583  1.00 67.51  ?  545 ALA B CB    1 
ATOM   8207 N  N     . LEU B 1 560 ? 12.058  15.578  41.704  1.00 94.07  ?  546 LEU B N     1 
ATOM   8208 C  CA    . LEU B 1 560 ? 12.662  14.441  41.012  1.00 85.88  ?  546 LEU B CA    1 
ATOM   8209 C  C     . LEU B 1 560 ? 13.572  13.591  41.884  1.00 93.09  ?  546 LEU B C     1 
ATOM   8210 O  O     . LEU B 1 560 ? 13.979  12.514  41.440  1.00 107.99 ?  546 LEU B O     1 
ATOM   8211 C  CB    . LEU B 1 560 ? 13.456  14.893  39.772  1.00 80.94  ?  546 LEU B CB    1 
ATOM   8212 C  CG    . LEU B 1 560 ? 12.746  15.251  38.459  1.00 94.67  ?  546 LEU B CG    1 
ATOM   8213 C  CD1   . LEU B 1 560 ? 11.452  16.045  38.635  1.00 98.22  ?  546 LEU B CD1   1 
ATOM   8214 C  CD2   . LEU B 1 560 ? 13.709  15.954  37.508  1.00 76.37  ?  546 LEU B CD2   1 
ATOM   8215 N  N     . GLU B 1 561 ? 13.922  14.015  43.088  1.00 94.54  ?  547 GLU B N     1 
ATOM   8216 C  CA    . GLU B 1 561 ? 14.708  13.111  43.925  1.00 102.04 ?  547 GLU B CA    1 
ATOM   8217 C  C     . GLU B 1 561 ? 13.880  12.047  44.628  1.00 105.08 ?  547 GLU B C     1 
ATOM   8218 O  O     . GLU B 1 561 ? 13.149  12.317  45.582  1.00 98.35  ?  547 GLU B O     1 
ATOM   8219 C  CB    . GLU B 1 561 ? 15.629  13.869  44.862  1.00 101.04 ?  547 GLU B CB    1 
ATOM   8220 C  CG    . GLU B 1 561 ? 16.891  14.192  44.089  1.00 102.45 ?  547 GLU B CG    1 
ATOM   8221 C  CD    . GLU B 1 561 ? 17.680  12.930  43.688  1.00 113.76 ?  547 GLU B CD    1 
ATOM   8222 O  OE1   . GLU B 1 561 ? 18.920  12.987  43.693  1.00 116.28 ?  547 GLU B OE1   1 
ATOM   8223 O  OE2   . GLU B 1 561 ? 17.094  11.853  43.402  1.00 115.64 ?  547 GLU B OE2   1 
ATOM   8224 N  N     . ALA B 1 562 ? 13.985  10.835  44.079  1.00 104.67 ?  548 ALA B N     1 
ATOM   8225 C  CA    . ALA B 1 562 ? 13.317  9.608   44.525  1.00 98.24  ?  548 ALA B CA    1 
ATOM   8226 C  C     . ALA B 1 562 ? 11.813  9.721   44.346  1.00 98.00  ?  548 ALA B C     1 
ATOM   8227 O  O     . ALA B 1 562 ? 11.314  10.714  43.806  1.00 85.67  ?  548 ALA B O     1 
ATOM   8228 C  CB    . ALA B 1 562 ? 13.687  9.297   45.969  1.00 89.30  ?  548 ALA B CB    1 
HETATM 8229 N  "N1'" . TPP C 2 .   ? 12.674  20.671  1.622   1.00 24.14  ?  601 TPP A "N1'" 1 
HETATM 8230 C  "C2'" . TPP C 2 .   ? 13.590  19.708  1.787   1.00 22.97  ?  601 TPP A "C2'" 1 
HETATM 8231 C  CM2   . TPP C 2 .   ? 13.928  19.324  3.191   1.00 21.52  ?  601 TPP A CM2   1 
HETATM 8232 N  "N3'" . TPP C 2 .   ? 14.236  19.073  0.805   1.00 19.30  ?  601 TPP A "N3'" 1 
HETATM 8233 C  "C4'" . TPP C 2 .   ? 13.934  19.409  -0.463  1.00 20.34  ?  601 TPP A "C4'" 1 
HETATM 8234 N  "N4'" . TPP C 2 .   ? 14.581  18.761  -1.435  1.00 22.31  ?  601 TPP A "N4'" 1 
HETATM 8235 C  "C5'" . TPP C 2 .   ? 12.974  20.423  -0.744  1.00 28.97  ?  601 TPP A "C5'" 1 
HETATM 8236 C  "C6'" . TPP C 2 .   ? 12.386  20.998  0.358   1.00 23.86  ?  601 TPP A "C6'" 1 
HETATM 8237 C  "C7'" . TPP C 2 .   ? 12.595  20.842  -2.138  1.00 27.53  ?  601 TPP A "C7'" 1 
HETATM 8238 N  N3    . TPP C 2 .   ? 13.739  21.324  -2.952  1.00 42.80  ?  601 TPP A N3    1 
HETATM 8239 C  C2    . TPP C 2 .   ? 14.479  20.545  -3.722  1.00 62.93  ?  601 TPP A C2    1 
HETATM 8240 S  S1    . TPP C 2 .   ? 15.676  21.390  -4.536  1.00 41.06  ?  601 TPP A S1    1 
HETATM 8241 C  C5    . TPP C 2 .   ? 15.164  22.867  -3.804  1.00 31.57  ?  601 TPP A C5    1 
HETATM 8242 C  C4    . TPP C 2 .   ? 14.114  22.664  -2.979  1.00 34.97  ?  601 TPP A C4    1 
HETATM 8243 C  CM4   . TPP C 2 .   ? 13.386  23.674  -2.162  1.00 35.14  ?  601 TPP A CM4   1 
HETATM 8244 C  C6    . TPP C 2 .   ? 15.864  24.155  -4.118  1.00 41.52  ?  601 TPP A C6    1 
HETATM 8245 C  C7    . TPP C 2 .   ? 17.357  24.075  -3.932  1.00 26.52  ?  601 TPP A C7    1 
HETATM 8246 O  O7    . TPP C 2 .   ? 17.829  25.400  -3.595  1.00 30.94  ?  601 TPP A O7    1 
HETATM 8247 P  PA    . TPP C 2 .   ? 19.338  25.776  -3.444  1.00 29.37  ?  601 TPP A PA    1 
HETATM 8248 O  O1A   . TPP C 2 .   ? 19.889  24.996  -2.315  1.00 22.53  ?  601 TPP A O1A   1 
HETATM 8249 O  O2A   . TPP C 2 .   ? 19.447  27.301  -3.383  1.00 26.34  ?  601 TPP A O2A   1 
HETATM 8250 O  O3A   . TPP C 2 .   ? 19.894  25.321  -4.827  1.00 14.73  ?  601 TPP A O3A   1 
HETATM 8251 P  PB    . TPP C 2 .   ? 20.034  25.860  -6.310  1.00 31.12  ?  601 TPP A PB    1 
HETATM 8252 O  O1B   . TPP C 2 .   ? 19.259  25.040  -7.280  1.00 26.97  ?  601 TPP A O1B   1 
HETATM 8253 O  O2B   . TPP C 2 .   ? 19.546  27.353  -6.223  1.00 25.88  ?  601 TPP A O2B   1 
HETATM 8254 O  O3B   . TPP C 2 .   ? 21.545  25.816  -6.574  1.00 31.42  ?  601 TPP A O3B   1 
HETATM 8255 MG MG    . MG  D 3 .   ? 19.937  28.762  -4.728  1.00 23.30  ?  602 MG  A MG    1 
HETATM 8256 C  CAO   . 3IO E 4 .   ? 12.365  19.106  31.079  1.00 67.94  ?  603 3IO A CAO   1 
HETATM 8257 C  CAG   . 3IO E 4 .   ? 12.904  18.094  31.886  1.00 64.43  ?  603 3IO A CAG   1 
HETATM 8258 C  CAE   . 3IO E 4 .   ? 12.222  17.674  33.021  1.00 69.86  ?  603 3IO A CAE   1 
HETATM 8259 C  CAD   . 3IO E 4 .   ? 11.005  18.256  33.357  1.00 70.26  ?  603 3IO A CAD   1 
HETATM 8260 C  CAF   . 3IO E 4 .   ? 10.471  19.258  32.560  1.00 76.57  ?  603 3IO A CAF   1 
HETATM 8261 C  CAN   . 3IO E 4 .   ? 11.159  19.683  31.412  1.00 71.20  ?  603 3IO A CAN   1 
HETATM 8262 N  NAJ   . 3IO E 4 .   ? 10.866  20.613  30.492  1.00 78.56  ?  603 3IO A NAJ   1 
HETATM 8263 C  CAH   . 3IO E 4 .   ? 11.817  20.670  29.579  1.00 70.49  ?  603 3IO A CAH   1 
HETATM 8264 C  CAM   . 3IO E 4 .   ? 12.796  19.737  29.897  1.00 67.47  ?  603 3IO A CAM   1 
HETATM 8265 C  CAI   . 3IO E 4 .   ? 14.080  19.454  29.121  1.00 60.04  ?  603 3IO A CAI   1 
HETATM 8266 C  CAL   . 3IO E 4 .   ? 13.888  18.377  28.056  1.00 70.01  ?  603 3IO A CAL   1 
HETATM 8267 O  OAB   . 3IO E 4 .   ? 13.070  18.519  27.211  1.00 73.73  ?  603 3IO A OAB   1 
HETATM 8268 C  CAK   . 3IO E 4 .   ? 14.750  17.117  28.081  1.00 66.18  ?  603 3IO A CAK   1 
HETATM 8269 O  OAC   . 3IO E 4 .   ? 15.965  17.179  27.755  1.00 79.52  ?  603 3IO A OAC   1 
HETATM 8270 O  OAA   . 3IO E 4 .   ? 14.246  16.016  28.426  1.00 51.12  -1 603 3IO A OAA   1 
HETATM 8271 N  "N1'" . TPP F 2 .   ? 15.543  18.670  21.881  1.00 31.19  ?  601 TPP B "N1'" 1 
HETATM 8272 C  "C2'" . TPP F 2 .   ? 14.338  19.237  21.745  1.00 23.77  ?  601 TPP B "C2'" 1 
HETATM 8273 C  CM2   . TPP F 2 .   ? 13.835  19.448  20.353  1.00 28.63  ?  601 TPP B CM2   1 
HETATM 8274 N  "N3'" . TPP F 2 .   ? 13.547  19.627  22.747  1.00 29.50  ?  601 TPP B "N3'" 1 
HETATM 8275 C  "C4'" . TPP F 2 .   ? 13.984  19.437  24.006  1.00 25.24  ?  601 TPP B "C4'" 1 
HETATM 8276 N  "N4'" . TPP F 2 .   ? 13.175  19.832  24.991  1.00 29.71  ?  601 TPP B "N4'" 1 
HETATM 8277 C  "C5'" . TPP F 2 .   ? 15.257  18.846  24.257  1.00 27.94  ?  601 TPP B "C5'" 1 
HETATM 8278 C  "C6'" . TPP F 2 .   ? 15.966  18.481  23.136  1.00 26.32  ?  601 TPP B "C6'" 1 
HETATM 8279 C  "C7'" . TPP F 2 .   ? 15.805  18.603  25.639  1.00 30.05  ?  601 TPP B "C7'" 1 
HETATM 8280 N  N3    . TPP F 2 .   ? 15.926  19.843  26.459  1.00 46.92  ?  601 TPP B N3    1 
HETATM 8281 C  C2    . TPP F 2 .   ? 14.944  20.325  27.195  1.00 71.34  ?  601 TPP B C2    1 
HETATM 8282 S  S1    . TPP F 2 .   ? 15.385  21.715  28.025  1.00 49.60  ?  601 TPP B S1    1 
HETATM 8283 C  C5    . TPP F 2 .   ? 16.966  21.654  27.339  1.00 36.46  ?  601 TPP B C5    1 
HETATM 8284 C  C4    . TPP F 2 .   ? 17.101  20.581  26.518  1.00 38.15  ?  601 TPP B C4    1 
HETATM 8285 C  CM4   . TPP F 2 .   ? 18.303  20.179  25.734  1.00 32.47  ?  601 TPP B CM4   1 
HETATM 8286 C  C6    . TPP F 2 .   ? 17.983  22.701  27.682  1.00 39.84  ?  601 TPP B C6    1 
HETATM 8287 C  C7    . TPP F 2 .   ? 17.414  24.098  27.669  1.00 29.85  ?  601 TPP B C7    1 
HETATM 8288 O  O7    . TPP F 2 .   ? 18.458  25.000  27.236  1.00 35.40  ?  601 TPP B O7    1 
HETATM 8289 P  PA    . TPP F 2 .   ? 18.295  26.553  27.150  1.00 35.12  ?  601 TPP B PA    1 
HETATM 8290 O  O1A   . TPP F 2 .   ? 17.383  26.862  26.025  1.00 26.25  ?  601 TPP B O1A   1 
HETATM 8291 O  O2A   . TPP F 2 .   ? 19.698  27.150  27.111  1.00 36.81  ?  601 TPP B O2A   1 
HETATM 8292 O  O3A   . TPP F 2 .   ? 17.666  26.890  28.564  1.00 24.11  ?  601 TPP B O3A   1 
HETATM 8293 P  PB    . TPP F 2 .   ? 18.121  27.301  30.026  1.00 39.19  ?  601 TPP B PB    1 
HETATM 8294 O  O1B   . TPP F 2 .   ? 17.560  28.631  30.411  1.00 32.38  ?  601 TPP B O1B   1 
HETATM 8295 O  O2B   . TPP F 2 .   ? 17.637  26.157  30.913  1.00 32.64  ?  601 TPP B O2B   1 
HETATM 8296 O  O3B   . TPP F 2 .   ? 19.663  27.273  29.966  1.00 34.19  ?  601 TPP B O3B   1 
HETATM 8297 MG MG    . MG  G 3 .   ? 20.838  28.047  28.448  1.00 27.47  ?  602 MG  B MG    1 
HETATM 8298 C  CAO   . 3IO H 4 .   ? 14.126  17.813  -7.631  1.00 64.81  ?  603 3IO B CAO   1 
HETATM 8299 C  CAG   . 3IO H 4 .   ? 13.085  17.911  -8.539  1.00 61.20  ?  603 3IO B CAG   1 
HETATM 8300 C  CAE   . 3IO H 4 .   ? 13.066  17.167  -9.701  1.00 60.64  ?  603 3IO B CAE   1 
HETATM 8301 C  CAD   . 3IO H 4 .   ? 14.087  16.282  -9.930  1.00 73.94  ?  603 3IO B CAD   1 
HETATM 8302 C  CAF   . 3IO H 4 .   ? 15.111  16.168  -9.003  1.00 66.66  ?  603 3IO B CAF   1 
HETATM 8303 C  CAN   . 3IO H 4 .   ? 15.131  16.944  -7.854  1.00 64.74  ?  603 3IO B CAN   1 
HETATM 8304 N  NAJ   . 3IO H 4 .   ? 15.976  17.005  -6.824  1.00 66.25  ?  603 3IO B NAJ   1 
HETATM 8305 C  CAH   . 3IO H 4 .   ? 15.582  17.880  -5.941  1.00 66.18  ?  603 3IO B CAH   1 
HETATM 8306 C  CAM   . 3IO H 4 .   ? 14.408  18.425  -6.416  1.00 64.35  ?  603 3IO B CAM   1 
HETATM 8307 C  CAI   . 3IO H 4 .   ? 13.560  19.472  -5.732  1.00 59.28  ?  603 3IO B CAI   1 
HETATM 8308 C  CAL   . 3IO H 4 .   ? 12.936  18.939  -4.458  1.00 60.09  ?  603 3IO B CAL   1 
HETATM 8309 O  OAB   . 3IO H 4 .   ? 13.586  18.465  -3.579  1.00 68.32  ?  603 3IO B OAB   1 
HETATM 8310 C  CAK   . 3IO H 4 .   ? 11.428  19.025  -4.364  1.00 64.84  ?  603 3IO B CAK   1 
HETATM 8311 O  OAC   . 3IO H 4 .   ? 10.731  18.019  -4.591  1.00 38.90  -1 603 3IO B OAC   1 
HETATM 8312 O  OAA   . 3IO H 4 .   ? 10.906  20.134  -4.088  1.00 62.54  ?  603 3IO B OAA   1 
HETATM 8313 O  O     . HOH I 5 .   ? 23.612  -10.857 -5.895  1.00 24.32  ?  701 HOH A O     1 
HETATM 8314 O  O     . HOH I 5 .   ? 20.382  0.035   -24.731 1.00 51.14  ?  702 HOH A O     1 
HETATM 8315 O  O     . HOH I 5 .   ? 36.007  39.405  -14.434 1.00 59.53  ?  703 HOH A O     1 
HETATM 8316 O  O     . HOH I 5 .   ? 42.285  18.340  -9.829  1.00 40.98  ?  704 HOH A O     1 
HETATM 8317 O  O     . HOH I 5 .   ? 18.850  -9.140  7.031   1.00 53.57  ?  705 HOH A O     1 
HETATM 8318 O  O     . HOH I 5 .   ? 13.687  -12.142 26.840  1.00 32.93  ?  706 HOH A O     1 
HETATM 8319 O  O     . HOH I 5 .   ? 21.411  -10.526 -19.406 1.00 41.09  ?  707 HOH A O     1 
HETATM 8320 O  O     . HOH I 5 .   ? 25.471  37.653  0.892   1.00 34.35  ?  708 HOH A O     1 
HETATM 8321 O  O     . HOH I 5 .   ? 21.929  3.781   -8.112  1.00 25.37  ?  709 HOH A O     1 
HETATM 8322 O  O     . HOH I 5 .   ? 10.708  -1.637  8.852   1.00 27.76  ?  710 HOH A O     1 
HETATM 8323 O  O     . HOH I 5 .   ? 39.308  0.211   -18.360 1.00 45.08  ?  711 HOH A O     1 
HETATM 8324 O  O     . HOH I 5 .   ? 17.143  13.981  -6.904  1.00 41.13  ?  712 HOH A O     1 
HETATM 8325 O  O     . HOH I 5 .   ? 10.337  37.662  -2.960  1.00 41.59  ?  713 HOH A O     1 
HETATM 8326 O  O     . HOH I 5 .   ? 34.099  9.691   26.271  1.00 38.04  ?  714 HOH A O     1 
HETATM 8327 O  O     . HOH I 5 .   ? 46.128  27.319  1.602   1.00 44.18  ?  715 HOH A O     1 
HETATM 8328 O  O     . HOH I 5 .   ? 32.598  36.547  16.590  1.00 35.83  ?  716 HOH A O     1 
HETATM 8329 O  O     . HOH I 5 .   ? 31.210  34.704  -17.982 1.00 61.05  ?  717 HOH A O     1 
HETATM 8330 O  O     . HOH I 5 .   ? 9.227   30.032  -0.515  1.00 26.60  ?  718 HOH A O     1 
HETATM 8331 O  O     . HOH I 5 .   ? 26.279  28.010  -17.119 1.00 40.18  ?  719 HOH A O     1 
HETATM 8332 O  O     . HOH I 5 .   ? 30.908  8.167   -12.390 1.00 35.79  ?  720 HOH A O     1 
HETATM 8333 O  O     . HOH I 5 .   ? 26.627  23.351  17.913  1.00 32.00  ?  721 HOH A O     1 
HETATM 8334 O  O     . HOH I 5 .   ? 21.239  9.428   3.306   1.00 30.10  ?  722 HOH A O     1 
HETATM 8335 O  O     . HOH I 5 .   ? 15.604  27.931  2.284   1.00 32.35  ?  723 HOH A O     1 
HETATM 8336 O  O     . HOH I 5 .   ? 22.468  -6.501  -25.891 1.00 54.86  ?  724 HOH A O     1 
HETATM 8337 O  O     . HOH I 5 .   ? 20.829  16.363  -0.366  1.00 28.37  ?  725 HOH A O     1 
HETATM 8338 O  O     . HOH I 5 .   ? 30.714  13.091  -15.307 1.00 31.50  ?  726 HOH A O     1 
HETATM 8339 O  O     . HOH I 5 .   ? 10.370  7.763   16.431  1.00 26.62  ?  727 HOH A O     1 
HETATM 8340 O  O     . HOH I 5 .   ? 38.950  20.032  5.630   1.00 29.65  ?  728 HOH A O     1 
HETATM 8341 O  O     . HOH I 5 .   ? 28.550  -20.477 -1.347  1.00 40.13  ?  729 HOH A O     1 
HETATM 8342 O  O     . HOH I 5 .   ? 24.304  7.910   -2.056  1.00 36.64  ?  730 HOH A O     1 
HETATM 8343 O  O     . HOH I 5 .   ? 15.760  -4.791  -12.726 1.00 41.93  ?  731 HOH A O     1 
HETATM 8344 O  O     . HOH I 5 .   ? 1.003   11.012  28.592  1.00 28.96  ?  732 HOH A O     1 
HETATM 8345 O  O     . HOH I 5 .   ? 16.319  10.261  -7.261  1.00 29.90  ?  733 HOH A O     1 
HETATM 8346 O  O     . HOH I 5 .   ? 16.847  19.773  5.865   1.00 20.90  ?  734 HOH A O     1 
HETATM 8347 O  O     . HOH I 5 .   ? 19.805  -10.310 13.228  1.00 49.11  ?  735 HOH A O     1 
HETATM 8348 O  O     . HOH I 5 .   ? 21.558  23.006  -2.735  1.00 24.22  ?  736 HOH A O     1 
HETATM 8349 O  O     . HOH I 5 .   ? 11.516  31.565  1.010   1.00 32.68  ?  737 HOH A O     1 
HETATM 8350 O  O     . HOH I 5 .   ? 38.463  34.923  15.099  1.00 51.39  ?  738 HOH A O     1 
HETATM 8351 O  O     . HOH I 5 .   ? 28.351  38.117  2.494   1.00 30.85  ?  739 HOH A O     1 
HETATM 8352 O  O     . HOH I 5 .   ? 32.101  5.973   -18.211 1.00 40.48  ?  740 HOH A O     1 
HETATM 8353 O  O     . HOH I 5 .   ? 2.089   9.931   23.669  1.00 34.15  ?  741 HOH A O     1 
HETATM 8354 O  O     . HOH I 5 .   ? 33.363  16.836  15.841  1.00 26.95  ?  742 HOH A O     1 
HETATM 8355 O  O     . HOH I 5 .   ? 22.653  38.479  -2.178  1.00 46.35  ?  743 HOH A O     1 
HETATM 8356 O  O     . HOH I 5 .   ? 28.059  11.782  -19.145 1.00 40.67  ?  744 HOH A O     1 
HETATM 8357 O  O     . HOH I 5 .   ? 30.522  7.842   -0.522  1.00 29.02  ?  745 HOH A O     1 
HETATM 8358 O  O     . HOH I 5 .   ? 13.673  -0.930  36.717  1.00 50.03  ?  746 HOH A O     1 
HETATM 8359 O  O     . HOH I 5 .   ? 21.724  27.807  -4.762  1.00 25.07  ?  747 HOH A O     1 
HETATM 8360 O  O     . HOH I 5 .   ? 17.222  14.973  21.760  1.00 24.34  ?  748 HOH A O     1 
HETATM 8361 O  O     . HOH I 5 .   ? 33.694  7.454   -9.533  1.00 29.12  ?  749 HOH A O     1 
HETATM 8362 O  O     . HOH I 5 .   ? 28.752  20.948  -14.587 1.00 38.95  ?  750 HOH A O     1 
HETATM 8363 O  O     . HOH I 5 .   ? 8.141   -2.070  27.063  1.00 51.46  ?  751 HOH A O     1 
HETATM 8364 O  O     . HOH I 5 .   ? 7.638   34.334  1.690   1.00 31.32  ?  752 HOH A O     1 
HETATM 8365 O  O     . HOH I 5 .   ? 27.736  35.636  -11.482 1.00 45.43  ?  753 HOH A O     1 
HETATM 8366 O  O     . HOH I 5 .   ? 42.808  15.547  -0.371  1.00 29.20  ?  754 HOH A O     1 
HETATM 8367 O  O     . HOH I 5 .   ? 26.216  25.637  16.506  1.00 26.51  ?  755 HOH A O     1 
HETATM 8368 O  O     . HOH I 5 .   ? 27.682  8.184   -0.665  1.00 29.08  ?  756 HOH A O     1 
HETATM 8369 O  O     . HOH I 5 .   ? 28.603  7.956   14.914  1.00 27.74  ?  757 HOH A O     1 
HETATM 8370 O  O     . HOH I 5 .   ? 14.035  6.924   13.865  1.00 32.37  ?  758 HOH A O     1 
HETATM 8371 O  O     . HOH I 5 .   ? 15.878  -4.177  -9.394  1.00 47.14  ?  759 HOH A O     1 
HETATM 8372 O  O     . HOH I 5 .   ? 29.321  21.705  23.004  1.00 33.29  ?  760 HOH A O     1 
HETATM 8373 O  O     . HOH I 5 .   ? 1.452   0.457   24.265  1.00 59.64  ?  761 HOH A O     1 
HETATM 8374 O  O     . HOH I 5 .   ? 25.451  18.967  -15.226 1.00 36.20  ?  762 HOH A O     1 
HETATM 8375 O  O     . HOH I 5 .   ? 11.102  -0.565  2.203   1.00 34.64  ?  763 HOH A O     1 
HETATM 8376 O  O     . HOH I 5 .   ? 10.098  6.133   21.660  1.00 32.25  ?  764 HOH A O     1 
HETATM 8377 O  O     . HOH I 5 .   ? 21.623  -21.786 -14.610 1.00 34.04  ?  765 HOH A O     1 
HETATM 8378 O  O     . HOH I 5 .   ? 16.281  -8.272  13.232  1.00 29.91  ?  766 HOH A O     1 
HETATM 8379 O  O     . HOH I 5 .   ? 30.465  30.775  -19.117 1.00 48.89  ?  767 HOH A O     1 
HETATM 8380 O  O     . HOH I 5 .   ? 18.012  21.869  11.123  1.00 21.40  ?  768 HOH A O     1 
HETATM 8381 O  O     . HOH I 5 .   ? 21.631  33.859  -0.861  1.00 23.23  ?  769 HOH A O     1 
HETATM 8382 O  O     . HOH I 5 .   ? 22.921  23.953  -5.153  1.00 23.78  ?  770 HOH A O     1 
HETATM 8383 O  O     . HOH I 5 .   ? 9.604   0.457   4.738   1.00 41.44  ?  771 HOH A O     1 
HETATM 8384 O  O     . HOH I 5 .   ? 23.391  21.939  2.739   1.00 24.59  ?  772 HOH A O     1 
HETATM 8385 O  O     . HOH I 5 .   ? 25.784  15.635  0.131   1.00 29.57  ?  773 HOH A O     1 
HETATM 8386 O  O     . HOH I 5 .   ? 20.159  33.672  1.304   1.00 26.03  ?  774 HOH A O     1 
HETATM 8387 O  O     . HOH I 5 .   ? 43.569  4.806   -9.270  1.00 53.05  ?  775 HOH A O     1 
HETATM 8388 O  O     . HOH I 5 .   ? 33.421  12.300  -14.822 1.00 42.88  ?  776 HOH A O     1 
HETATM 8389 O  O     . HOH I 5 .   ? 27.302  9.450   -2.821  1.00 24.22  ?  777 HOH A O     1 
HETATM 8390 O  O     . HOH I 5 .   ? 0.282   4.410   17.847  1.00 34.87  ?  778 HOH A O     1 
HETATM 8391 O  O     . HOH I 5 .   ? 20.712  -24.054 1.902   1.00 41.08  ?  779 HOH A O     1 
HETATM 8392 O  O     . HOH I 5 .   ? 23.292  9.523   -12.745 1.00 26.80  ?  780 HOH A O     1 
HETATM 8393 O  O     . HOH I 5 .   ? 22.353  27.894  -17.980 1.00 44.94  ?  781 HOH A O     1 
HETATM 8394 O  O     . HOH I 5 .   ? 18.105  6.421   28.510  1.00 34.63  ?  782 HOH A O     1 
HETATM 8395 O  O     . HOH I 5 .   ? 16.668  -14.487 -19.576 1.00 46.25  ?  783 HOH A O     1 
HETATM 8396 O  O     . HOH I 5 .   ? 42.422  15.184  1.951   1.00 28.51  ?  784 HOH A O     1 
HETATM 8397 O  O     . HOH I 5 .   ? 37.516  8.351   -7.081  1.00 37.35  ?  785 HOH A O     1 
HETATM 8398 O  O     . HOH I 5 .   ? 32.269  35.728  9.704   1.00 36.42  ?  786 HOH A O     1 
HETATM 8399 O  O     . HOH I 5 .   ? 34.212  6.600   -2.795  1.00 39.89  ?  787 HOH A O     1 
HETATM 8400 O  O     . HOH I 5 .   ? 30.900  27.946  17.468  1.00 29.73  ?  788 HOH A O     1 
HETATM 8401 O  O     . HOH I 5 .   ? 14.570  19.792  16.752  1.00 28.59  ?  789 HOH A O     1 
HETATM 8402 O  O     . HOH I 5 .   ? 28.775  -22.898 -6.098  1.00 36.91  ?  790 HOH A O     1 
HETATM 8403 O  O     . HOH I 5 .   ? 19.563  7.066   -22.784 1.00 43.30  ?  791 HOH A O     1 
HETATM 8404 O  O     . HOH I 5 .   ? 36.428  -4.180  -1.718  1.00 44.94  ?  792 HOH A O     1 
HETATM 8405 O  O     . HOH I 5 .   ? 12.609  15.118  10.783  1.00 25.32  ?  793 HOH A O     1 
HETATM 8406 O  O     . HOH I 5 .   ? 32.117  38.408  -17.943 1.00 57.71  ?  794 HOH A O     1 
HETATM 8407 O  O     . HOH I 5 .   ? 35.244  2.184   10.689  1.00 40.51  ?  795 HOH A O     1 
HETATM 8408 O  O     . HOH I 5 .   ? 1.507   3.001   28.935  1.00 44.64  ?  796 HOH A O     1 
HETATM 8409 O  O     . HOH I 5 .   ? 28.626  14.533  -25.734 1.00 58.17  ?  797 HOH A O     1 
HETATM 8410 O  O     . HOH I 5 .   ? 44.738  32.325  -10.029 1.00 39.13  ?  798 HOH A O     1 
HETATM 8411 O  O     . HOH I 5 .   ? 38.788  -16.850 -15.076 1.00 38.73  ?  799 HOH A O     1 
HETATM 8412 O  O     . HOH I 5 .   ? 37.927  -7.635  -7.645  1.00 41.57  ?  800 HOH A O     1 
HETATM 8413 O  O     . HOH I 5 .   ? 24.677  -8.908  0.929   1.00 33.12  ?  801 HOH A O     1 
HETATM 8414 O  O     . HOH I 5 .   ? 14.166  -7.610  38.212  1.00 53.84  ?  802 HOH A O     1 
HETATM 8415 O  O     . HOH I 5 .   ? 18.395  40.717  3.116   1.00 35.61  ?  803 HOH A O     1 
HETATM 8416 O  O     . HOH I 5 .   ? 37.330  26.208  12.637  1.00 34.91  ?  804 HOH A O     1 
HETATM 8417 O  O     . HOH I 5 .   ? 26.442  -27.711 -5.003  1.00 36.96  ?  805 HOH A O     1 
HETATM 8418 O  O     . HOH I 5 .   ? 13.976  -6.778  11.867  1.00 48.60  ?  806 HOH A O     1 
HETATM 8419 O  O     . HOH I 5 .   ? 43.805  22.133  -4.407  1.00 38.57  ?  807 HOH A O     1 
HETATM 8420 O  O     . HOH I 5 .   ? 41.257  20.668  13.370  1.00 48.45  ?  808 HOH A O     1 
HETATM 8421 O  O     . HOH I 5 .   ? 22.539  15.542  -1.882  1.00 30.96  ?  809 HOH A O     1 
HETATM 8422 O  O     . HOH I 5 .   ? 4.989   35.753  -6.984  1.00 44.72  ?  810 HOH A O     1 
HETATM 8423 O  O     . HOH I 5 .   ? 15.480  35.329  -3.583  1.00 42.10  ?  811 HOH A O     1 
HETATM 8424 O  O     . HOH I 5 .   ? 34.071  -2.158  -23.090 1.00 48.43  ?  812 HOH A O     1 
HETATM 8425 O  O     . HOH I 5 .   ? 16.187  1.622   -4.191  1.00 35.29  ?  813 HOH A O     1 
HETATM 8426 O  O     . HOH I 5 .   ? 20.294  -7.194  34.230  1.00 40.17  ?  814 HOH A O     1 
HETATM 8427 O  O     . HOH I 5 .   ? 39.143  3.813   15.394  1.00 53.37  ?  815 HOH A O     1 
HETATM 8428 O  O     . HOH I 5 .   ? 39.115  -14.066 -10.182 1.00 39.93  ?  816 HOH A O     1 
HETATM 8429 O  O     . HOH I 5 .   ? 29.720  -11.670 20.872  1.00 45.12  ?  817 HOH A O     1 
HETATM 8430 O  O     . HOH I 5 .   ? 22.744  36.342  -8.158  1.00 48.99  ?  818 HOH A O     1 
HETATM 8431 O  O     . HOH I 5 .   ? 45.014  24.109  -7.713  1.00 59.04  ?  819 HOH A O     1 
HETATM 8432 O  O     . HOH I 5 .   ? 36.820  13.875  17.202  1.00 33.30  ?  820 HOH A O     1 
HETATM 8433 O  O     . HOH I 5 .   ? 39.832  -8.510  -9.781  1.00 44.90  ?  821 HOH A O     1 
HETATM 8434 O  O     . HOH I 5 .   ? 14.820  40.193  -8.679  1.00 52.61  ?  822 HOH A O     1 
HETATM 8435 O  O     . HOH I 5 .   ? 35.702  -22.005 -16.777 1.00 42.06  ?  823 HOH A O     1 
HETATM 8436 O  O     . HOH I 5 .   ? 21.384  -19.333 -0.491  1.00 38.96  ?  824 HOH A O     1 
HETATM 8437 O  O     . HOH I 5 .   ? 16.347  2.299   -1.618  1.00 27.05  ?  825 HOH A O     1 
HETATM 8438 O  O     . HOH I 5 .   ? 20.118  11.328  6.141   1.00 31.08  ?  826 HOH A O     1 
HETATM 8439 O  O     . HOH I 5 .   ? 31.283  5.664   1.095   1.00 26.07  ?  827 HOH A O     1 
HETATM 8440 O  O     . HOH I 5 .   ? 31.763  8.046   -3.035  1.00 29.76  ?  828 HOH A O     1 
HETATM 8441 O  O     . HOH I 5 .   ? 20.333  9.613   10.126  1.00 20.35  ?  829 HOH A O     1 
HETATM 8442 O  O     . HOH I 5 .   ? 7.454   5.720   21.349  1.00 28.14  ?  830 HOH A O     1 
HETATM 8443 O  O     . HOH I 5 .   ? 13.263  2.780   -12.770 1.00 39.00  ?  831 HOH A O     1 
HETATM 8444 O  O     . HOH I 5 .   ? 18.608  -7.839  -3.073  1.00 37.46  ?  832 HOH A O     1 
HETATM 8445 O  O     . HOH I 5 .   ? 5.920   23.940  -15.523 1.00 54.21  ?  833 HOH A O     1 
HETATM 8446 O  O     . HOH I 5 .   ? 28.707  4.306   1.622   1.00 30.33  ?  834 HOH A O     1 
HETATM 8447 O  O     . HOH I 5 .   ? 38.436  3.505   -12.668 1.00 31.54  ?  835 HOH A O     1 
HETATM 8448 O  O     . HOH I 5 .   ? 37.927  7.597   0.174   1.00 49.34  ?  836 HOH A O     1 
HETATM 8449 O  O     . HOH I 5 .   ? 24.931  32.301  -16.871 1.00 47.04  ?  837 HOH A O     1 
HETATM 8450 O  O     . HOH I 5 .   ? 8.334   -11.233 33.835  1.00 56.59  ?  838 HOH A O     1 
HETATM 8451 O  O     . HOH I 5 .   ? 22.586  29.314  -10.613 1.00 30.08  ?  839 HOH A O     1 
HETATM 8452 O  O     . HOH I 5 .   ? 19.534  -6.689  31.750  1.00 39.97  ?  840 HOH A O     1 
HETATM 8453 O  O     . HOH I 5 .   ? 28.772  -11.075 2.091   1.00 51.35  ?  841 HOH A O     1 
HETATM 8454 O  O     . HOH I 5 .   ? 37.106  18.204  16.138  1.00 50.30  ?  842 HOH A O     1 
HETATM 8455 O  O     . HOH I 5 .   ? 28.333  3.784   4.364   1.00 29.12  ?  843 HOH A O     1 
HETATM 8456 O  O     . HOH I 5 .   ? 33.350  16.046  20.309  1.00 36.56  ?  844 HOH A O     1 
HETATM 8457 O  O     . HOH I 5 .   ? 28.172  42.268  3.442   1.00 42.93  ?  845 HOH A O     1 
HETATM 8458 O  O     . HOH I 5 .   ? 36.961  -13.638 -8.198  1.00 42.78  ?  846 HOH A O     1 
HETATM 8459 O  O     . HOH I 5 .   ? 25.688  -8.894  29.270  1.00 42.96  ?  847 HOH A O     1 
HETATM 8460 O  O     . HOH I 5 .   ? 16.529  -0.032  -10.604 1.00 32.78  ?  848 HOH A O     1 
HETATM 8461 O  O     . HOH I 5 .   ? 27.783  -9.282  0.126   1.00 38.68  ?  849 HOH A O     1 
HETATM 8462 O  O     . HOH I 5 .   ? 14.211  31.925  3.214   1.00 28.80  ?  850 HOH A O     1 
HETATM 8463 O  O     . HOH I 5 .   ? 38.779  37.460  3.833   1.00 38.70  ?  851 HOH A O     1 
HETATM 8464 O  O     . HOH I 5 .   ? 35.853  17.194  14.220  1.00 36.46  ?  852 HOH A O     1 
HETATM 8465 O  O     . HOH I 5 .   ? 22.066  36.496  -0.087  1.00 30.59  ?  853 HOH A O     1 
HETATM 8466 O  O     . HOH I 5 .   ? 18.586  10.060  32.086  1.00 35.81  ?  854 HOH A O     1 
HETATM 8467 O  O     . HOH I 5 .   ? 37.492  13.891  14.957  1.00 43.44  ?  855 HOH A O     1 
HETATM 8468 O  O     . HOH I 5 .   ? 19.658  35.103  -14.090 1.00 38.36  ?  856 HOH A O     1 
HETATM 8469 O  O     . HOH I 5 .   ? 20.547  36.885  -11.984 1.00 44.82  ?  857 HOH A O     1 
HETATM 8470 O  O     . HOH I 5 .   ? 11.738  -2.031  11.660  1.00 43.06  ?  858 HOH A O     1 
HETATM 8471 O  O     . HOH I 5 .   ? 12.814  -5.440  14.585  1.00 37.82  ?  859 HOH A O     1 
HETATM 8472 O  O     . HOH I 5 .   ? 37.974  7.028   -5.120  1.00 47.22  ?  860 HOH A O     1 
HETATM 8473 O  O     . HOH I 5 .   ? 16.719  -4.015  3.525   1.00 47.11  ?  861 HOH A O     1 
HETATM 8474 O  O     . HOH I 5 .   ? 12.442  -3.363  32.043  1.00 35.45  ?  862 HOH A O     1 
HETATM 8475 O  O     . HOH I 5 .   ? 4.510   7.833   22.462  1.00 27.38  ?  863 HOH A O     1 
HETATM 8476 O  O     . HOH I 5 .   ? 33.284  28.811  18.856  1.00 40.31  ?  864 HOH A O     1 
HETATM 8477 O  O     . HOH I 5 .   ? 48.342  19.063  -4.504  1.00 56.81  ?  865 HOH A O     1 
HETATM 8478 O  O     . HOH I 5 .   ? 41.030  14.376  -12.299 1.00 48.07  ?  866 HOH A O     1 
HETATM 8479 O  O     . HOH I 5 .   ? 15.741  39.284  2.048   1.00 40.08  ?  867 HOH A O     1 
HETATM 8480 O  O     . HOH I 5 .   ? 2.674   2.861   26.658  1.00 33.65  ?  868 HOH A O     1 
HETATM 8481 O  O     . HOH I 5 .   ? 33.167  0.758   0.192   1.00 46.57  ?  869 HOH A O     1 
HETATM 8482 O  O     . HOH I 5 .   ? 34.425  -5.532  22.363  1.00 58.96  ?  870 HOH A O     1 
HETATM 8483 O  O     . HOH I 5 .   ? 42.869  -2.628  -0.601  1.00 54.65  ?  871 HOH A O     1 
HETATM 8484 O  O     . HOH I 5 .   ? 27.725  0.928   5.459   1.00 39.71  ?  872 HOH A O     1 
HETATM 8485 O  O     . HOH I 5 .   ? 16.445  -19.204 -10.505 1.00 35.17  ?  873 HOH A O     1 
HETATM 8486 O  O     . HOH I 5 .   ? 3.371   16.592  -18.238 1.00 60.61  ?  874 HOH A O     1 
HETATM 8487 O  O     . HOH I 5 .   ? 27.149  35.567  -15.431 1.00 60.26  ?  875 HOH A O     1 
HETATM 8488 O  O     . HOH I 5 .   ? 19.579  7.753   30.870  1.00 34.47  ?  876 HOH A O     1 
HETATM 8489 O  O     . HOH I 5 .   ? 38.270  22.501  -16.316 1.00 42.95  ?  877 HOH A O     1 
HETATM 8490 O  O     . HOH I 5 .   ? 15.939  19.490  14.350  1.00 25.36  ?  878 HOH A O     1 
HETATM 8491 O  O     . HOH I 5 .   ? 16.339  -18.172 -7.262  1.00 39.25  ?  879 HOH A O     1 
HETATM 8492 O  O     . HOH I 5 .   ? 37.323  1.856   15.429  1.00 51.29  ?  880 HOH A O     1 
HETATM 8493 O  O     . HOH I 5 .   ? 32.779  18.337  20.687  1.00 43.48  ?  881 HOH A O     1 
HETATM 8494 O  O     . HOH I 5 .   ? 10.875  -8.163  27.071  1.00 33.64  ?  882 HOH A O     1 
HETATM 8495 O  O     . HOH I 5 .   ? 30.142  18.247  22.196  1.00 35.99  ?  883 HOH A O     1 
HETATM 8496 O  O     . HOH I 5 .   ? 35.377  20.695  21.028  1.00 63.68  ?  884 HOH A O     1 
HETATM 8497 O  O     . HOH I 5 .   ? 23.024  -25.520 -10.281 1.00 39.20  ?  885 HOH A O     1 
HETATM 8498 O  O     . HOH I 5 .   ? 39.410  19.659  9.728   1.00 41.80  ?  886 HOH A O     1 
HETATM 8499 O  O     . HOH I 5 .   ? 7.037   32.937  -13.469 1.00 38.07  ?  887 HOH A O     1 
HETATM 8500 O  O     . HOH I 5 .   ? 36.624  35.415  10.900  1.00 59.38  ?  888 HOH A O     1 
HETATM 8501 O  O     . HOH I 5 .   ? 36.415  36.482  7.228   1.00 46.51  ?  889 HOH A O     1 
HETATM 8502 O  O     . HOH I 5 .   ? 10.262  -5.265  23.495  1.00 41.13  ?  890 HOH A O     1 
HETATM 8503 O  O     . HOH I 5 .   ? 46.615  -9.253  -7.960  1.00 54.06  ?  891 HOH A O     1 
HETATM 8504 O  O     . HOH I 5 .   ? 10.842  -1.218  6.638   1.00 38.07  ?  892 HOH A O     1 
HETATM 8505 O  O     . HOH I 5 .   ? 20.504  41.835  -4.591  1.00 61.07  ?  893 HOH A O     1 
HETATM 8506 O  O     . HOH I 5 .   ? 31.226  -19.307 -8.505  1.00 47.05  ?  894 HOH A O     1 
HETATM 8507 O  O     . HOH I 5 .   ? 48.801  21.042  -5.929  1.00 52.57  ?  895 HOH A O     1 
HETATM 8508 O  O     . HOH I 5 .   ? 30.960  13.109  -25.643 1.00 56.94  ?  896 HOH A O     1 
HETATM 8509 O  O     . HOH I 5 .   ? 18.796  -16.106 -18.660 1.00 43.99  ?  897 HOH A O     1 
HETATM 8510 O  O     . HOH I 5 .   ? 11.600  -5.390  21.429  1.00 44.89  ?  898 HOH A O     1 
HETATM 8511 O  O     . HOH I 5 .   ? 20.940  -11.528 18.848  1.00 39.94  ?  899 HOH A O     1 
HETATM 8512 O  O     . HOH I 5 .   ? 12.583  -7.972  -13.313 1.00 50.62  ?  900 HOH A O     1 
HETATM 8513 O  O     . HOH I 5 .   ? 24.716  -8.983  3.406   1.00 55.21  ?  901 HOH A O     1 
HETATM 8514 O  O     . HOH I 5 .   ? 16.542  39.445  -10.567 1.00 51.98  ?  902 HOH A O     1 
HETATM 8515 O  O     . HOH I 5 .   ? 43.564  -10.660 -15.050 1.00 53.18  ?  903 HOH A O     1 
HETATM 8516 O  O     . HOH I 5 .   ? 11.633  -4.066  9.367   1.00 44.96  ?  904 HOH A O     1 
HETATM 8517 O  O     . HOH I 5 .   ? 0.601   35.230  -1.754  1.00 38.65  ?  905 HOH A O     1 
HETATM 8518 O  O     . HOH I 5 .   ? 11.273  -9.058  24.047  1.00 48.06  ?  906 HOH A O     1 
HETATM 8519 O  O     . HOH I 5 .   ? 18.667  -4.457  0.830   1.00 51.61  ?  907 HOH A O     1 
HETATM 8520 O  O     . HOH I 5 .   ? 41.980  21.823  15.162  1.00 53.33  ?  908 HOH A O     1 
HETATM 8521 O  O     . HOH I 5 .   ? 49.012  28.087  -1.664  1.00 48.16  ?  909 HOH A O     1 
HETATM 8522 O  O     . HOH I 5 .   ? 17.685  -4.682  -1.153  1.00 46.00  ?  910 HOH A O     1 
HETATM 8523 O  O     . HOH I 5 .   ? 10.399  -5.703  16.341  1.00 49.10  ?  911 HOH A O     1 
HETATM 8524 O  O     . HOH I 5 .   ? 31.335  0.149   4.247   1.00 50.67  ?  912 HOH A O     1 
HETATM 8525 O  O     . HOH I 5 .   ? 29.564  -7.722  1.425   1.00 45.96  ?  913 HOH A O     1 
HETATM 8526 O  O     . HOH I 5 .   ? 35.949  -0.509  0.364   1.00 42.17  ?  914 HOH A O     1 
HETATM 8527 O  O     . HOH I 5 .   ? 22.264  -11.337 16.701  1.00 47.30  ?  915 HOH A O     1 
HETATM 8528 O  O     . HOH I 5 .   ? 45.013  14.798  -12.058 1.00 57.84  ?  916 HOH A O     1 
HETATM 8529 O  O     . HOH I 5 .   ? 2.836   4.096   12.917  1.00 46.14  ?  917 HOH A O     1 
HETATM 8530 O  O     . HOH I 5 .   ? 41.535  18.416  -14.391 1.00 48.21  ?  918 HOH A O     1 
HETATM 8531 O  O     . HOH I 5 .   ? 7.526   -0.461  28.719  1.00 61.06  ?  919 HOH A O     1 
HETATM 8532 O  O     . HOH I 5 .   ? 35.095  35.321  8.879   1.00 49.32  ?  920 HOH A O     1 
HETATM 8533 O  O     . HOH I 5 .   ? 29.653  -21.702 -8.116  1.00 39.16  ?  921 HOH A O     1 
HETATM 8534 O  O     . HOH I 5 .   ? 41.672  15.746  -15.109 1.00 52.29  ?  922 HOH A O     1 
HETATM 8535 O  O     . HOH I 5 .   ? 12.331  2.348   -15.363 1.00 47.00  ?  923 HOH A O     1 
HETATM 8536 O  O     . HOH I 5 .   ? 2.367   -2.750  31.711  1.00 55.16  ?  924 HOH A O     1 
HETATM 8537 O  O     . HOH I 5 .   ? 39.197  20.457  19.154  1.00 63.25  ?  925 HOH A O     1 
HETATM 8538 O  O     . HOH I 5 .   ? 36.225  6.139   2.057   1.00 44.95  ?  926 HOH A O     1 
HETATM 8539 O  O     . HOH I 5 .   ? 13.317  -3.132  38.672  1.00 51.72  ?  927 HOH A O     1 
HETATM 8540 O  O     . HOH I 5 .   ? 44.932  15.574  -9.593  1.00 64.43  ?  928 HOH A O     1 
HETATM 8541 O  O     . HOH I 5 .   ? 30.384  19.840  -18.912 1.00 54.53  ?  929 HOH A O     1 
HETATM 8542 O  O     . HOH I 5 .   ? 10.830  -8.439  18.374  1.00 55.93  ?  930 HOH A O     1 
HETATM 8543 O  O     . HOH I 5 .   ? 34.358  15.677  18.244  1.00 34.43  ?  931 HOH A O     1 
HETATM 8544 O  O     . HOH I 5 .   ? 32.225  2.344   3.980   1.00 52.78  ?  932 HOH A O     1 
HETATM 8545 O  O     . HOH I 5 .   ? 29.312  -22.101 -3.059  1.00 43.63  ?  933 HOH A O     1 
HETATM 8546 O  O     . HOH I 5 .   ? 37.022  18.136  18.964  1.00 55.64  ?  934 HOH A O     1 
HETATM 8547 O  O     . HOH I 5 .   ? 23.416  28.411  -20.221 1.00 61.93  ?  935 HOH A O     1 
HETATM 8548 O  O     . HOH I 5 .   ? 15.016  38.265  -3.462  1.00 58.48  ?  936 HOH A O     1 
HETATM 8549 O  O     . HOH I 5 .   ? 10.768  -8.628  15.909  1.00 55.56  ?  937 HOH A O     1 
HETATM 8550 O  O     . HOH I 5 .   ? 38.969  -7.913  -4.669  1.00 55.03  ?  938 HOH A O     1 
HETATM 8551 O  O     . HOH I 5 .   ? 2.297   -0.754  29.566  1.00 49.09  ?  939 HOH A O     1 
HETATM 8552 O  O     . HOH I 5 .   ? 36.595  -9.264  -5.918  1.00 42.18  ?  940 HOH A O     1 
HETATM 8553 O  O     . HOH I 5 .   ? 31.894  21.092  -16.824 1.00 50.77  ?  941 HOH A O     1 
HETATM 8554 O  O     . HOH I 5 .   ? 9.979   11.984  -13.650 1.00 51.89  ?  942 HOH A O     1 
HETATM 8555 O  O     . HOH I 5 .   ? 37.471  -6.914  -0.553  1.00 66.09  ?  943 HOH A O     1 
HETATM 8556 O  O     . HOH I 5 .   ? 13.627  -0.230  -11.679 1.00 52.46  ?  944 HOH A O     1 
HETATM 8557 O  O     . HOH I 5 .   ? 32.388  14.327  -23.662 1.00 61.68  ?  945 HOH A O     1 
HETATM 8558 O  O     . HOH I 5 .   ? 14.709  41.424  0.453   1.00 57.40  ?  946 HOH A O     1 
HETATM 8559 O  O     . HOH J 5 .   ? 0.275   32.978  -9.481  1.00 49.64  ?  701 HOH B O     1 
HETATM 8560 O  O     . HOH J 5 .   ? 11.356  11.480  46.593  1.00 76.73  ?  702 HOH B O     1 
HETATM 8561 O  O     . HOH J 5 .   ? 21.113  47.479  8.985   1.00 40.31  ?  703 HOH B O     1 
HETATM 8562 O  O     . HOH J 5 .   ? -9.279  33.828  7.577   1.00 42.69  ?  704 HOH B O     1 
HETATM 8563 O  O     . HOH J 5 .   ? 2.705   9.764   -16.027 1.00 56.44  ?  705 HOH B O     1 
HETATM 8564 O  O     . HOH J 5 .   ? -25.157 27.782  5.160   1.00 52.29  ?  706 HOH B O     1 
HETATM 8565 O  O     . HOH J 5 .   ? 14.325  45.653  12.503  1.00 39.41  ?  707 HOH B O     1 
HETATM 8566 O  O     . HOH J 5 .   ? 30.978  25.109  23.710  1.00 46.97  ?  708 HOH B O     1 
HETATM 8567 O  O     . HOH J 5 .   ? -2.118  35.105  -2.388  1.00 27.59  ?  709 HOH B O     1 
HETATM 8568 O  O     . HOH J 5 .   ? -9.424  19.342  21.957  1.00 36.09  ?  710 HOH B O     1 
HETATM 8569 O  O     . HOH J 5 .   ? -3.398  21.901  32.027  1.00 41.05  ?  711 HOH B O     1 
HETATM 8570 O  O     . HOH J 5 .   ? -4.363  10.667  21.362  1.00 48.71  ?  712 HOH B O     1 
HETATM 8571 O  O     . HOH J 5 .   ? -2.508  5.604   16.274  1.00 46.71  ?  713 HOH B O     1 
HETATM 8572 O  O     . HOH J 5 .   ? -5.217  9.662   14.669  1.00 26.02  ?  714 HOH B O     1 
HETATM 8573 O  O     . HOH J 5 .   ? 13.403  28.933  21.055  1.00 27.66  ?  715 HOH B O     1 
HETATM 8574 O  O     . HOH J 5 .   ? -17.785 23.249  24.057  1.00 45.61  ?  716 HOH B O     1 
HETATM 8575 O  O     . HOH J 5 .   ? -21.092 34.742  33.566  1.00 54.32  ?  717 HOH B O     1 
HETATM 8576 O  O     . HOH J 5 .   ? -8.198  17.115  34.999  1.00 52.04  ?  718 HOH B O     1 
HETATM 8577 O  O     . HOH J 5 .   ? 13.447  32.638  5.665   1.00 32.09  ?  719 HOH B O     1 
HETATM 8578 O  O     . HOH J 5 .   ? 2.135   23.040  20.302  1.00 25.28  ?  720 HOH B O     1 
HETATM 8579 O  O     . HOH J 5 .   ? 7.831   20.634  30.301  1.00 40.89  ?  721 HOH B O     1 
HETATM 8580 O  O     . HOH J 5 .   ? -2.238  31.339  23.981  1.00 40.38  ?  722 HOH B O     1 
HETATM 8581 O  O     . HOH J 5 .   ? -17.756 20.478  -9.045  1.00 37.58  ?  723 HOH B O     1 
HETATM 8582 O  O     . HOH J 5 .   ? 4.019   45.569  33.899  1.00 39.29  ?  724 HOH B O     1 
HETATM 8583 O  O     . HOH J 5 .   ? 15.048  27.723  26.578  1.00 28.77  ?  725 HOH B O     1 
HETATM 8584 O  O     . HOH J 5 .   ? 26.846  39.100  21.128  1.00 30.69  ?  726 HOH B O     1 
HETATM 8585 O  O     . HOH J 5 .   ? -15.510 28.209  1.080   1.00 41.94  ?  727 HOH B O     1 
HETATM 8586 O  O     . HOH J 5 .   ? 4.035   12.281  7.160   1.00 24.93  ?  728 HOH B O     1 
HETATM 8587 O  O     . HOH J 5 .   ? -8.891  37.251  36.729  1.00 44.69  ?  729 HOH B O     1 
HETATM 8588 O  O     . HOH J 5 .   ? 21.482  23.774  21.374  1.00 33.28  ?  730 HOH B O     1 
HETATM 8589 O  O     . HOH J 5 .   ? -4.402  31.314  22.315  1.00 33.20  ?  731 HOH B O     1 
HETATM 8590 O  O     . HOH J 5 .   ? -1.540  29.609  8.754   1.00 28.30  ?  732 HOH B O     1 
HETATM 8591 O  O     . HOH J 5 .   ? -31.666 13.362  33.279  1.00 43.54  ?  733 HOH B O     1 
HETATM 8592 O  O     . HOH J 5 .   ? -12.867 12.813  10.563  1.00 29.94  ?  734 HOH B O     1 
HETATM 8593 O  O     . HOH J 5 .   ? 19.479  29.403  28.438  1.00 30.68  ?  735 HOH B O     1 
HETATM 8594 O  O     . HOH J 5 .   ? 1.354   45.535  23.954  1.00 37.56  ?  736 HOH B O     1 
HETATM 8595 O  O     . HOH J 5 .   ? 9.691   30.074  39.065  1.00 49.95  ?  737 HOH B O     1 
HETATM 8596 O  O     . HOH J 5 .   ? -2.615  9.320   18.879  1.00 37.84  ?  738 HOH B O     1 
HETATM 8597 O  O     . HOH J 5 .   ? 33.021  11.913  25.084  1.00 39.03  ?  739 HOH B O     1 
HETATM 8598 O  O     . HOH J 5 .   ? -17.807 18.756  29.207  1.00 30.36  ?  740 HOH B O     1 
HETATM 8599 O  O     . HOH J 5 .   ? 13.305  22.225  17.743  1.00 23.29  ?  741 HOH B O     1 
HETATM 8600 O  O     . HOH J 5 .   ? 8.841   21.130  1.818   1.00 20.11  ?  742 HOH B O     1 
HETATM 8601 O  O     . HOH J 5 .   ? -15.705 32.799  25.660  1.00 47.97  ?  743 HOH B O     1 
HETATM 8602 O  O     . HOH J 5 .   ? 23.285  42.114  14.390  1.00 34.40  ?  744 HOH B O     1 
HETATM 8603 O  O     . HOH J 5 .   ? 12.760  43.556  10.948  1.00 40.48  ?  745 HOH B O     1 
HETATM 8604 O  O     . HOH J 5 .   ? 30.967  10.948  33.240  1.00 44.27  ?  746 HOH B O     1 
HETATM 8605 O  O     . HOH J 5 .   ? 2.723   11.514  2.181   1.00 24.20  ?  747 HOH B O     1 
HETATM 8606 O  O     . HOH J 5 .   ? 25.682  18.187  24.101  1.00 35.13  ?  748 HOH B O     1 
HETATM 8607 O  O     . HOH J 5 .   ? 2.889   8.682   2.281   1.00 32.06  ?  749 HOH B O     1 
HETATM 8608 O  O     . HOH J 5 .   ? -3.696  15.652  28.034  1.00 35.57  ?  750 HOH B O     1 
HETATM 8609 O  O     . HOH J 5 .   ? 4.536   18.669  31.090  1.00 40.45  ?  751 HOH B O     1 
HETATM 8610 O  O     . HOH J 5 .   ? 7.195   36.736  3.319   1.00 39.94  ?  752 HOH B O     1 
HETATM 8611 O  O     . HOH J 5 .   ? 0.951   35.311  38.472  1.00 49.66  ?  753 HOH B O     1 
HETATM 8612 O  O     . HOH J 5 .   ? -0.956  20.722  -9.154  1.00 42.97  ?  754 HOH B O     1 
HETATM 8613 O  O     . HOH J 5 .   ? 10.307  16.638  12.898  1.00 25.14  ?  755 HOH B O     1 
HETATM 8614 O  O     . HOH J 5 .   ? 4.513   36.660  2.816   1.00 38.17  ?  756 HOH B O     1 
HETATM 8615 O  O     . HOH J 5 .   ? 14.192  20.021  6.740   1.00 28.76  ?  757 HOH B O     1 
HETATM 8616 O  O     . HOH J 5 .   ? 5.356   36.758  7.889   1.00 28.76  ?  758 HOH B O     1 
HETATM 8617 O  O     . HOH J 5 .   ? 10.813  33.751  38.430  1.00 43.90  ?  759 HOH B O     1 
HETATM 8618 O  O     . HOH J 5 .   ? -3.733  34.184  33.290  1.00 41.24  ?  760 HOH B O     1 
HETATM 8619 O  O     . HOH J 5 .   ? 32.687  22.014  30.713  1.00 54.17  ?  761 HOH B O     1 
HETATM 8620 O  O     . HOH J 5 .   ? 22.593  41.592  41.687  1.00 54.83  ?  762 HOH B O     1 
HETATM 8621 O  O     . HOH J 5 .   ? 8.868   5.093   -0.064  1.00 22.49  ?  763 HOH B O     1 
HETATM 8622 O  O     . HOH J 5 .   ? 6.507   43.259  18.179  1.00 32.31  ?  764 HOH B O     1 
HETATM 8623 O  O     . HOH J 5 .   ? 28.376  26.151  27.233  1.00 41.06  ?  765 HOH B O     1 
HETATM 8624 O  O     . HOH J 5 .   ? 4.276   22.586  17.361  1.00 27.32  ?  766 HOH B O     1 
HETATM 8625 O  O     . HOH J 5 .   ? -16.385 20.421  22.796  1.00 39.30  ?  767 HOH B O     1 
HETATM 8626 O  O     . HOH J 5 .   ? 15.541  29.340  28.704  1.00 28.15  ?  768 HOH B O     1 
HETATM 8627 O  O     . HOH J 5 .   ? -1.388  13.427  36.248  1.00 39.59  ?  769 HOH B O     1 
HETATM 8628 O  O     . HOH J 5 .   ? -18.431 18.423  1.208   1.00 46.24  ?  770 HOH B O     1 
HETATM 8629 O  O     . HOH J 5 .   ? -1.595  21.692  -15.430 1.00 58.61  ?  771 HOH B O     1 
HETATM 8630 O  O     . HOH J 5 .   ? 3.098   51.854  28.518  1.00 57.03  ?  772 HOH B O     1 
HETATM 8631 O  O     . HOH J 5 .   ? 24.158  42.747  7.151   1.00 32.42  ?  773 HOH B O     1 
HETATM 8632 O  O     . HOH J 5 .   ? -5.214  10.527  12.032  1.00 35.76  ?  774 HOH B O     1 
HETATM 8633 O  O     . HOH J 5 .   ? -13.476 16.839  -10.229 1.00 37.20  ?  775 HOH B O     1 
HETATM 8634 O  O     . HOH J 5 .   ? -9.509  13.040  36.080  1.00 54.94  ?  776 HOH B O     1 
HETATM 8635 O  O     . HOH J 5 .   ? -20.413 28.319  -7.154  1.00 37.70  ?  777 HOH B O     1 
HETATM 8636 O  O     . HOH J 5 .   ? 0.606   28.801  26.494  1.00 26.40  ?  778 HOH B O     1 
HETATM 8637 O  O     . HOH J 5 .   ? -6.976  30.450  -5.496  1.00 45.46  ?  779 HOH B O     1 
HETATM 8638 O  O     . HOH J 5 .   ? 25.225  31.374  24.428  1.00 29.25  ?  780 HOH B O     1 
HETATM 8639 O  O     . HOH J 5 .   ? 24.848  38.103  35.263  1.00 47.25  ?  781 HOH B O     1 
HETATM 8640 O  O     . HOH J 5 .   ? -1.353  11.252  -12.253 1.00 49.33  ?  782 HOH B O     1 
HETATM 8641 O  O     . HOH J 5 .   ? -1.999  31.990  36.140  1.00 45.41  ?  783 HOH B O     1 
HETATM 8642 O  O     . HOH J 5 .   ? 2.731   22.261  13.869  1.00 27.74  ?  784 HOH B O     1 
HETATM 8643 O  O     . HOH J 5 .   ? 15.038  23.941  12.721  1.00 18.02  ?  785 HOH B O     1 
HETATM 8644 O  O     . HOH J 5 .   ? -0.899  28.842  24.524  1.00 36.62  ?  786 HOH B O     1 
HETATM 8645 O  O     . HOH J 5 .   ? 10.031  4.635   -4.864  1.00 25.57  ?  787 HOH B O     1 
HETATM 8646 O  O     . HOH J 5 .   ? -16.143 8.959   -3.606  1.00 36.05  ?  788 HOH B O     1 
HETATM 8647 O  O     . HOH J 5 .   ? 1.711   25.150  36.361  1.00 37.67  ?  789 HOH B O     1 
HETATM 8648 O  O     . HOH J 5 .   ? 0.531   18.852  -5.179  1.00 27.34  ?  790 HOH B O     1 
HETATM 8649 O  O     . HOH J 5 .   ? -23.234 15.308  43.249  1.00 53.18  ?  791 HOH B O     1 
HETATM 8650 O  O     . HOH J 5 .   ? 7.508   26.485  25.519  1.00 31.18  ?  792 HOH B O     1 
HETATM 8651 O  O     . HOH J 5 .   ? 15.846  33.035  7.036   1.00 34.05  ?  793 HOH B O     1 
HETATM 8652 O  O     . HOH J 5 .   ? 16.542  38.037  6.021   1.00 30.07  ?  794 HOH B O     1 
HETATM 8653 O  O     . HOH J 5 .   ? -0.719  48.257  26.882  1.00 43.61  ?  795 HOH B O     1 
HETATM 8654 O  O     . HOH J 5 .   ? -5.763  6.468   -3.608  1.00 48.71  ?  796 HOH B O     1 
HETATM 8655 O  O     . HOH J 5 .   ? 25.567  30.067  22.204  1.00 32.38  ?  797 HOH B O     1 
HETATM 8656 O  O     . HOH J 5 .   ? 32.280  16.012  30.839  1.00 43.96  ?  798 HOH B O     1 
HETATM 8657 O  O     . HOH J 5 .   ? -2.774  16.199  25.495  1.00 31.97  ?  799 HOH B O     1 
HETATM 8658 O  O     . HOH J 5 .   ? -5.548  28.252  19.345  1.00 37.37  ?  800 HOH B O     1 
HETATM 8659 O  O     . HOH J 5 .   ? -14.912 31.240  -3.893  1.00 43.68  ?  801 HOH B O     1 
HETATM 8660 O  O     . HOH J 5 .   ? 8.925   24.565  24.141  1.00 33.76  ?  802 HOH B O     1 
HETATM 8661 O  O     . HOH J 5 .   ? 11.598  34.570  0.741   1.00 34.04  ?  803 HOH B O     1 
HETATM 8662 O  O     . HOH J 5 .   ? 24.277  26.625  31.100  1.00 36.53  ?  804 HOH B O     1 
HETATM 8663 O  O     . HOH J 5 .   ? -10.835 11.030  11.768  1.00 41.87  ?  805 HOH B O     1 
HETATM 8664 O  O     . HOH J 5 .   ? -13.081 15.451  -12.370 1.00 41.68  ?  806 HOH B O     1 
HETATM 8665 O  O     . HOH J 5 .   ? -17.519 16.179  4.301   1.00 36.14  ?  807 HOH B O     1 
HETATM 8666 O  O     . HOH J 5 .   ? -4.490  32.202  42.110  1.00 44.60  ?  808 HOH B O     1 
HETATM 8667 O  O     . HOH J 5 .   ? -11.093 7.537   -4.345  1.00 36.71  ?  809 HOH B O     1 
HETATM 8668 O  O     . HOH J 5 .   ? 2.500   2.386   -5.159  1.00 39.85  ?  810 HOH B O     1 
HETATM 8669 O  O     . HOH J 5 .   ? 30.359  21.966  31.795  1.00 52.20  ?  811 HOH B O     1 
HETATM 8670 O  O     . HOH J 5 .   ? 2.184   15.408  10.082  1.00 26.69  ?  812 HOH B O     1 
HETATM 8671 O  O     . HOH J 5 .   ? -7.511  10.575  -8.314  1.00 35.81  ?  813 HOH B O     1 
HETATM 8672 O  O     . HOH J 5 .   ? 6.723   29.292  23.568  1.00 37.01  ?  814 HOH B O     1 
HETATM 8673 O  O     . HOH J 5 .   ? 32.755  30.313  20.526  1.00 38.34  ?  815 HOH B O     1 
HETATM 8674 O  O     . HOH J 5 .   ? -4.673  34.568  25.902  1.00 34.70  ?  816 HOH B O     1 
HETATM 8675 O  O     . HOH J 5 .   ? 6.836   48.704  27.995  1.00 39.11  ?  817 HOH B O     1 
HETATM 8676 O  O     . HOH J 5 .   ? 10.890  3.714   -11.578 1.00 35.12  ?  818 HOH B O     1 
HETATM 8677 O  O     . HOH J 5 .   ? 1.322   39.166  5.990   1.00 35.02  ?  819 HOH B O     1 
HETATM 8678 O  O     . HOH J 5 .   ? -19.494 33.137  31.151  1.00 49.43  ?  820 HOH B O     1 
HETATM 8679 O  O     . HOH J 5 .   ? -2.429  32.705  26.537  1.00 31.87  ?  821 HOH B O     1 
HETATM 8680 O  O     . HOH J 5 .   ? 19.535  30.299  41.848  1.00 59.44  ?  822 HOH B O     1 
HETATM 8681 O  O     . HOH J 5 .   ? -15.968 5.796   -5.362  1.00 67.11  ?  823 HOH B O     1 
HETATM 8682 O  O     . HOH J 5 .   ? 6.059   21.034  18.464  1.00 32.97  ?  824 HOH B O     1 
HETATM 8683 O  O     . HOH J 5 .   ? -7.841  26.477  18.526  1.00 39.40  ?  825 HOH B O     1 
HETATM 8684 O  O     . HOH J 5 .   ? 2.570   33.324  39.303  1.00 39.30  ?  826 HOH B O     1 
HETATM 8685 O  O     . HOH J 5 .   ? 14.648  43.657  8.834   1.00 40.07  ?  827 HOH B O     1 
HETATM 8686 O  O     . HOH J 5 .   ? 0.625   45.090  21.794  1.00 33.73  ?  828 HOH B O     1 
HETATM 8687 O  O     . HOH J 5 .   ? 1.896   3.249   -2.744  1.00 29.29  ?  829 HOH B O     1 
HETATM 8688 O  O     . HOH J 5 .   ? -9.886  14.389  -15.230 1.00 59.03  ?  830 HOH B O     1 
HETATM 8689 O  O     . HOH J 5 .   ? -7.016  14.188  40.878  1.00 52.04  ?  831 HOH B O     1 
HETATM 8690 O  O     . HOH J 5 .   ? 32.068  27.626  20.897  1.00 44.37  ?  832 HOH B O     1 
HETATM 8691 O  O     . HOH J 5 .   ? 4.155   14.202  -10.422 1.00 51.89  ?  833 HOH B O     1 
HETATM 8692 O  O     . HOH J 5 .   ? 5.881   6.746   1.209   1.00 34.33  ?  834 HOH B O     1 
HETATM 8693 O  O     . HOH J 5 .   ? 1.172   20.989  -7.162  1.00 28.49  ?  835 HOH B O     1 
HETATM 8694 O  O     . HOH J 5 .   ? -12.479 9.202   37.307  1.00 51.66  ?  836 HOH B O     1 
HETATM 8695 O  O     . HOH J 5 .   ? 25.779  23.613  20.326  1.00 24.83  ?  837 HOH B O     1 
HETATM 8696 O  O     . HOH J 5 .   ? -0.055  1.566   -1.168  1.00 59.25  ?  838 HOH B O     1 
HETATM 8697 O  O     . HOH J 5 .   ? 27.520  32.738  23.917  1.00 33.83  ?  839 HOH B O     1 
HETATM 8698 O  O     . HOH J 5 .   ? 25.232  37.567  38.536  1.00 46.79  ?  840 HOH B O     1 
HETATM 8699 O  O     . HOH J 5 .   ? -5.488  12.189  -13.197 1.00 44.39  ?  841 HOH B O     1 
HETATM 8700 O  O     . HOH J 5 .   ? 1.716   11.195  -12.302 1.00 46.64  ?  842 HOH B O     1 
HETATM 8701 O  O     . HOH J 5 .   ? -8.170  7.962   -0.122  1.00 39.30  ?  843 HOH B O     1 
HETATM 8702 O  O     . HOH J 5 .   ? 1.542   39.837  8.719   1.00 47.28  ?  844 HOH B O     1 
HETATM 8703 O  O     . HOH J 5 .   ? 24.924  15.032  38.955  1.00 46.90  ?  845 HOH B O     1 
HETATM 8704 O  O     . HOH J 5 .   ? 16.234  40.797  4.995   1.00 37.96  ?  846 HOH B O     1 
HETATM 8705 O  O     . HOH J 5 .   ? 5.963   21.257  -10.728 1.00 46.55  ?  847 HOH B O     1 
HETATM 8706 O  O     . HOH J 5 .   ? 3.529   20.716  -8.717  1.00 40.18  ?  848 HOH B O     1 
HETATM 8707 O  O     . HOH J 5 .   ? 6.786   29.359  41.021  1.00 57.55  ?  849 HOH B O     1 
HETATM 8708 O  O     . HOH J 5 .   ? -12.054 10.692  -14.537 1.00 58.74  ?  850 HOH B O     1 
HETATM 8709 O  O     . HOH J 5 .   ? -9.206  10.279  9.128   1.00 32.99  ?  851 HOH B O     1 
HETATM 8710 O  O     . HOH J 5 .   ? -18.912 24.312  -11.624 1.00 39.74  ?  852 HOH B O     1 
HETATM 8711 O  O     . HOH J 5 .   ? -16.606 21.187  -5.375  1.00 43.94  ?  853 HOH B O     1 
HETATM 8712 O  O     . HOH J 5 .   ? -10.020 38.230  33.836  1.00 44.05  ?  854 HOH B O     1 
HETATM 8713 O  O     . HOH J 5 .   ? -5.308  15.509  34.198  1.00 44.69  ?  855 HOH B O     1 
HETATM 8714 O  O     . HOH J 5 .   ? -12.620 16.475  -8.204  1.00 37.32  ?  856 HOH B O     1 
HETATM 8715 O  O     . HOH J 5 .   ? 6.114   43.608  13.977  1.00 33.75  ?  857 HOH B O     1 
HETATM 8716 O  O     . HOH J 5 .   ? 28.322  31.513  35.857  1.00 46.51  ?  858 HOH B O     1 
HETATM 8717 O  O     . HOH J 5 .   ? -11.587 17.717  -13.910 1.00 46.03  ?  859 HOH B O     1 
HETATM 8718 O  O     . HOH J 5 .   ? -2.713  42.940  14.661  1.00 42.25  ?  860 HOH B O     1 
HETATM 8719 O  O     . HOH J 5 .   ? -4.963  38.180  24.249  1.00 50.77  ?  861 HOH B O     1 
HETATM 8720 O  O     . HOH J 5 .   ? -6.765  11.741  -10.181 1.00 49.94  ?  862 HOH B O     1 
HETATM 8721 O  O     . HOH J 5 .   ? -3.718  7.207   -4.824  1.00 44.84  ?  863 HOH B O     1 
HETATM 8722 O  O     . HOH J 5 .   ? 13.406  42.767  3.556   1.00 51.11  ?  864 HOH B O     1 
HETATM 8723 O  O     . HOH J 5 .   ? -12.361 9.144   39.878  1.00 55.59  ?  865 HOH B O     1 
HETATM 8724 O  O     . HOH J 5 .   ? -9.031  14.347  19.947  1.00 51.51  ?  866 HOH B O     1 
HETATM 8725 O  O     . HOH J 5 .   ? 13.454  21.250  9.210   1.00 24.44  ?  867 HOH B O     1 
HETATM 8726 O  O     . HOH J 5 .   ? -9.131  13.592  32.419  1.00 50.86  ?  868 HOH B O     1 
HETATM 8727 O  O     . HOH J 5 .   ? -0.305  26.185  -12.627 1.00 46.22  ?  869 HOH B O     1 
HETATM 8728 O  O     . HOH J 5 .   ? 9.821   1.170   -10.660 1.00 45.26  ?  870 HOH B O     1 
HETATM 8729 O  O     . HOH J 5 .   ? 26.935  30.314  37.904  1.00 41.66  ?  871 HOH B O     1 
HETATM 8730 O  O     . HOH J 5 .   ? 27.311  33.418  31.382  1.00 47.30  ?  872 HOH B O     1 
HETATM 8731 O  O     . HOH J 5 .   ? -5.058  28.738  21.799  1.00 32.58  ?  873 HOH B O     1 
HETATM 8732 O  O     . HOH J 5 .   ? -5.805  41.021  -0.834  1.00 58.49  ?  874 HOH B O     1 
HETATM 8733 O  O     . HOH J 5 .   ? 4.676   39.317  9.235   1.00 40.11  ?  875 HOH B O     1 
HETATM 8734 O  O     . HOH J 5 .   ? -8.512  8.787   2.133   1.00 37.74  ?  876 HOH B O     1 
HETATM 8735 O  O     . HOH J 5 .   ? 15.471  42.897  5.573   1.00 44.28  ?  877 HOH B O     1 
HETATM 8736 O  O     . HOH J 5 .   ? -10.128 39.643  -0.442  1.00 53.06  ?  878 HOH B O     1 
HETATM 8737 O  O     . HOH J 5 .   ? 6.319   39.341  39.575  1.00 52.28  ?  879 HOH B O     1 
HETATM 8738 O  O     . HOH J 5 .   ? -8.818  8.117   7.061   1.00 38.97  ?  880 HOH B O     1 
HETATM 8739 O  O     . HOH J 5 .   ? -24.516 30.927  48.319  1.00 66.31  ?  881 HOH B O     1 
HETATM 8740 O  O     . HOH J 5 .   ? -5.209  14.135  38.661  1.00 46.21  ?  882 HOH B O     1 
HETATM 8741 O  O     . HOH J 5 .   ? -1.959  46.111  20.356  1.00 49.08  ?  883 HOH B O     1 
HETATM 8742 O  O     . HOH J 5 .   ? 13.980  56.970  12.659  1.00 58.49  ?  884 HOH B O     1 
HETATM 8743 O  O     . HOH J 5 .   ? 4.697   43.148  11.671  1.00 50.01  ?  885 HOH B O     1 
HETATM 8744 O  O     . HOH J 5 .   ? 34.669  15.651  28.861  1.00 60.07  ?  886 HOH B O     1 
HETATM 8745 O  O     . HOH J 5 .   ? -17.803 17.432  6.800   1.00 47.00  ?  887 HOH B O     1 
HETATM 8746 O  O     . HOH J 5 .   ? 15.311  21.136  11.639  1.00 24.57  ?  888 HOH B O     1 
HETATM 8747 O  O     . HOH J 5 .   ? -19.287 19.534  -7.383  1.00 50.33  ?  889 HOH B O     1 
HETATM 8748 O  O     . HOH J 5 .   ? 6.989   30.366  43.367  1.00 62.15  ?  890 HOH B O     1 
HETATM 8749 O  O     . HOH J 5 .   ? 3.067   3.577   10.796  1.00 42.23  ?  891 HOH B O     1 
HETATM 8750 O  O     . HOH J 5 .   ? -8.090  15.628  39.215  1.00 46.67  ?  892 HOH B O     1 
HETATM 8751 O  O     . HOH J 5 .   ? 8.549   38.299  39.558  1.00 40.53  ?  893 HOH B O     1 
HETATM 8752 O  O     . HOH J 5 .   ? 4.840   50.765  26.253  1.00 45.47  ?  894 HOH B O     1 
HETATM 8753 O  O     . HOH J 5 .   ? 32.093  22.378  24.683  1.00 48.95  ?  895 HOH B O     1 
HETATM 8754 O  O     . HOH J 5 .   ? -6.419  14.355  32.663  1.00 64.48  ?  896 HOH B O     1 
HETATM 8755 O  O     . HOH J 5 .   ? 8.818   50.352  29.110  1.00 49.81  ?  897 HOH B O     1 
HETATM 8756 O  O     . HOH J 5 .   ? 28.311  27.628  38.355  1.00 52.06  ?  898 HOH B O     1 
HETATM 8757 O  O     . HOH J 5 .   ? 6.955   19.189  -12.185 1.00 46.41  ?  899 HOH B O     1 
HETATM 8758 O  O     . HOH J 5 .   ? 3.801   37.372  5.262   1.00 37.35  ?  900 HOH B O     1 
HETATM 8759 O  O     . HOH J 5 .   ? -17.169 21.145  -12.580 1.00 44.64  ?  901 HOH B O     1 
HETATM 8760 O  O     . HOH J 5 .   ? -14.055 5.210   40.387  1.00 58.89  ?  902 HOH B O     1 
HETATM 8761 O  O     . HOH J 5 .   ? -9.446  11.018  -16.237 1.00 58.33  ?  903 HOH B O     1 
HETATM 8762 O  O     . HOH J 5 .   ? -29.662 33.974  41.388  1.00 52.47  ?  904 HOH B O     1 
HETATM 8763 O  O     . HOH J 5 .   ? -4.695  13.298  35.729  1.00 47.71  ?  905 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   . THR A 17  ? 1.1031 1.1785 1.0981 -0.0260 -0.2073 0.1731  3   THR A N   
2    C CA  . THR A 17  ? 1.0253 1.1017 1.0506 -0.0204 -0.1944 0.1661  3   THR A CA  
3    C C   . THR A 17  ? 0.9543 1.0254 0.9990 -0.0084 -0.1898 0.1772  3   THR A C   
4    O O   . THR A 17  ? 1.0199 1.1031 1.0972 -0.0008 -0.1919 0.1795  3   THR A O   
5    C CB  . THR A 17  ? 1.0332 1.1303 1.0869 -0.0212 -0.2009 0.1596  3   THR A CB  
6    O OG1 . THR A 17  ? 0.9590 1.0726 1.0291 -0.0161 -0.2175 0.1716  3   THR A OG1 
7    C CG2 . THR A 17  ? 1.1126 1.2127 1.1493 -0.0334 -0.2036 0.1469  3   THR A CG2 
8    N N   . PRO A 18  ? 0.7891 0.8419 0.8145 -0.0067 -0.1829 0.1840  4   PRO A N   
9    C CA  . PRO A 18  ? 0.7738 0.8189 0.8169 0.0041  -0.1778 0.1940  4   PRO A CA  
10   C C   . PRO A 18  ? 0.6444 0.6872 0.7122 0.0081  -0.1630 0.1839  4   PRO A C   
11   O O   . PRO A 18  ? 0.7519 0.7909 0.8138 0.0020  -0.1524 0.1707  4   PRO A O   
12   C CB  . PRO A 18  ? 0.7174 0.7419 0.7299 0.0019  -0.1721 0.2013  4   PRO A CB  
13   C CG  . PRO A 18  ? 0.7723 0.7967 0.7507 -0.0091 -0.1776 0.1974  4   PRO A CG  
14   C CD  . PRO A 18  ? 0.8140 0.8514 0.8017 -0.0149 -0.1775 0.1819  4   PRO A CD  
15   N N   . TYR A 19  ? 0.5839 0.6289 0.6793 0.0187  -0.1624 0.1905  5   TYR A N   
16   C CA  . TYR A 19  ? 0.5347 0.5763 0.6525 0.0231  -0.1486 0.1818  5   TYR A CA  
17   C C   . TYR A 19  ? 0.5907 0.6120 0.6915 0.0197  -0.1338 0.1770  5   TYR A C   
18   O O   . TYR A 19  ? 0.5048 0.5116 0.5895 0.0203  -0.1325 0.1862  5   TYR A O   
19   C CB  . TYR A 19  ? 0.4575 0.5016 0.6042 0.0355  -0.1501 0.1908  5   TYR A CB  
20   C CG  . TYR A 19  ? 0.4845 0.5308 0.6576 0.0402  -0.1386 0.1809  5   TYR A CG  
21   C CD1 . TYR A 19  ? 0.4623 0.4912 0.6356 0.0423  -0.1243 0.1768  5   TYR A CD1 
22   C CD2 . TYR A 19  ? 0.4270 0.4929 0.6245 0.0422  -0.1419 0.1758  5   TYR A CD2 
23   C CE1 . TYR A 19  ? 0.4226 0.4530 0.6176 0.0462  -0.1142 0.1676  5   TYR A CE1 
24   C CE2 . TYR A 19  ? 0.3652 0.4327 0.5847 0.0463  -0.1308 0.1670  5   TYR A CE2 
25   C CZ  . TYR A 19  ? 0.3661 0.4155 0.5831 0.0484  -0.1173 0.1628  5   TYR A CZ  
26   O OH  . TYR A 19  ? 0.4265 0.4767 0.6626 0.0521  -0.1066 0.1537  5   TYR A OH  
27   N N   . CYS A 20  ? 0.4693 0.4901 0.5745 0.0159  -0.1228 0.1631  6   CYS A N   
28   C CA  . CYS A 20  ? 0.5343 0.5391 0.6241 0.0112  -0.1096 0.1569  6   CYS A CA  
29   C C   . CYS A 20  ? 0.4714 0.4750 0.5809 0.0137  -0.0980 0.1463  6   CYS A C   
30   O O   . CYS A 20  ? 0.4582 0.4722 0.5914 0.0190  -0.0994 0.1440  6   CYS A O   
31   C CB  . CYS A 20  ? 0.5226 0.5272 0.5863 0.0008  -0.1095 0.1500  6   CYS A CB  
32   S SG  . CYS A 20  ? 0.5530 0.5736 0.6255 -0.0042 -0.1115 0.1361  6   CYS A SG  
33   N N   . VAL A 21  ? 0.4003 0.3916 0.4995 0.0095  -0.0864 0.1398  7   VAL A N   
34   C CA  . VAL A 21  ? 0.4307 0.4193 0.5453 0.0111  -0.0756 0.1300  7   VAL A CA  
35   C C   . VAL A 21  ? 0.4674 0.4701 0.5930 0.0095  -0.0765 0.1197  7   VAL A C   
36   O O   . VAL A 21  ? 0.3885 0.3950 0.5338 0.0139  -0.0724 0.1149  7   VAL A O   
37   C CB  . VAL A 21  ? 0.4047 0.3798 0.5050 0.0057  -0.0646 0.1252  7   VAL A CB  
38   C CG1 . VAL A 21  ? 0.3348 0.3105 0.4470 0.0049  -0.0554 0.1128  7   VAL A CG1 
39   C CG2 . VAL A 21  ? 0.3730 0.3329 0.4701 0.0084  -0.0612 0.1349  7   VAL A CG2 
40   N N   . ALA A 22  ? 0.4099 0.4198 0.5223 0.0028  -0.0814 0.1160  8   ALA A N   
41   C CA  . ALA A 22  ? 0.4506 0.4732 0.5729 0.0006  -0.0829 0.1072  8   ALA A CA  
42   C C   . ALA A 22  ? 0.4630 0.4989 0.6090 0.0070  -0.0894 0.1112  8   ALA A C   
43   O O   . ALA A 22  ? 0.3901 0.4325 0.5533 0.0090  -0.0851 0.1048  8   ALA A O   
44   C CB  . ALA A 22  ? 0.3585 0.3853 0.4621 -0.0076 -0.0886 0.1039  8   ALA A CB  
45   N N   . ASP A 23  ? 0.4164 0.4568 0.5638 0.0105  -0.0996 0.1222  9   ASP A N   
46   C CA  . ASP A 23  ? 0.3867 0.4410 0.5591 0.0173  -0.1060 0.1268  9   ASP A CA  
47   C C   . ASP A 23  ? 0.4389 0.4876 0.6310 0.0262  -0.0974 0.1274  9   ASP A C   
48   O O   . ASP A 23  ? 0.3314 0.3909 0.5463 0.0309  -0.0961 0.1248  9   ASP A O   
49   C CB  . ASP A 23  ? 0.3787 0.4390 0.5480 0.0195  -0.1197 0.1395  9   ASP A CB  
50   C CG  . ASP A 23  ? 0.5129 0.5788 0.6615 0.0102  -0.1290 0.1383  9   ASP A CG  
51   O OD1 . ASP A 23  ? 0.4605 0.5375 0.6137 0.0049  -0.1306 0.1299  9   ASP A OD1 
52   O OD2 . ASP A 23  ? 0.5042 0.5627 0.6312 0.0080  -0.1344 0.1457  9   ASP A OD2 
53   N N   . TYR A 24  ? 0.3270 0.3585 0.5104 0.0283  -0.0910 0.1305  10  TYR A N   
54   C CA  . TYR A 24  ? 0.3823 0.4058 0.5823 0.0361  -0.0825 0.1300  10  TYR A CA  
55   C C   . TYR A 24  ? 0.3584 0.3837 0.5670 0.0345  -0.0727 0.1171  10  TYR A C   
56   O O   . TYR A 24  ? 0.3613 0.3909 0.5901 0.0409  -0.0688 0.1148  10  TYR A O   
57   C CB  . TYR A 24  ? 0.3833 0.3868 0.5703 0.0364  -0.0773 0.1347  10  TYR A CB  
58   C CG  . TYR A 24  ? 0.4323 0.4250 0.6352 0.0441  -0.0695 0.1351  10  TYR A CG  
59   C CD1 . TYR A 24  ? 0.4428 0.4286 0.6492 0.0428  -0.0583 0.1241  10  TYR A CD1 
60   C CD2 . TYR A 24  ? 0.4494 0.4383 0.6635 0.0529  -0.0736 0.1464  10  TYR A CD2 
61   C CE1 . TYR A 24  ? 0.3782 0.3529 0.5977 0.0493  -0.0511 0.1233  10  TYR A CE1 
62   C CE2 . TYR A 24  ? 0.4711 0.4483 0.6997 0.0601  -0.0659 0.1460  10  TYR A CE2 
63   C CZ  . TYR A 24  ? 0.4476 0.4175 0.6782 0.0579  -0.0545 0.1339  10  TYR A CZ  
64   O OH  . TYR A 24  ? 0.4207 0.3779 0.6643 0.0644  -0.0469 0.1325  10  TYR A OH  
65   N N   . LEU A 25  ? 0.2955 0.3177 0.4885 0.0264  -0.0685 0.1087  11  LEU A N   
66   C CA  . LEU A 25  ? 0.3619 0.3857 0.5608 0.0246  -0.0601 0.0973  11  LEU A CA  
67   C C   . LEU A 25  ? 0.3532 0.3941 0.5681 0.0257  -0.0633 0.0945  11  LEU A C   
68   O O   . LEU A 25  ? 0.3350 0.3785 0.5639 0.0291  -0.0568 0.0890  11  LEU A O   
69   C CB  . LEU A 25  ? 0.3330 0.3515 0.5128 0.0161  -0.0566 0.0902  11  LEU A CB  
70   C CG  . LEU A 25  ? 0.4446 0.4651 0.6271 0.0131  -0.0496 0.0791  11  LEU A CG  
71   C CD1 . LEU A 25  ? 0.2954 0.3100 0.4900 0.0182  -0.0416 0.0753  11  LEU A CD1 
72   C CD2 . LEU A 25  ? 0.3282 0.3418 0.4927 0.0060  -0.0462 0.0738  11  LEU A CD2 
73   N N   . LEU A 26  ? 0.3436 0.3962 0.5561 0.0224  -0.0730 0.0980  12  LEU A N   
74   C CA  . LEU A 26  ? 0.3653 0.4351 0.5946 0.0225  -0.0763 0.0958  12  LEU A CA  
75   C C   . LEU A 26  ? 0.3695 0.4468 0.6234 0.0322  -0.0765 0.1011  12  LEU A C   
76   O O   . LEU A 26  ? 0.3428 0.4289 0.6136 0.0344  -0.0716 0.0964  12  LEU A O   
77   C CB  . LEU A 26  ? 0.3188 0.3991 0.5402 0.0162  -0.0877 0.0985  12  LEU A CB  
78   C CG  . LEU A 26  ? 0.3782 0.4521 0.5776 0.0067  -0.0860 0.0911  12  LEU A CG  
79   C CD1 . LEU A 26  ? 0.3405 0.4224 0.5295 0.0003  -0.0974 0.0936  12  LEU A CD1 
80   C CD2 . LEU A 26  ? 0.2639 0.3395 0.4688 0.0040  -0.0777 0.0811  12  LEU A CD2 
81   N N   . ASP A 27  ? 0.2924 0.3654 0.5485 0.0382  -0.0813 0.1110  13  ASP A N   
82   C CA  . ASP A 27  ? 0.3858 0.4643 0.6666 0.0487  -0.0808 0.1162  13  ASP A CA  
83   C C   . ASP A 27  ? 0.3413 0.4104 0.6305 0.0532  -0.0673 0.1087  13  ASP A C   
84   O O   . ASP A 27  ? 0.3470 0.4256 0.6572 0.0586  -0.0630 0.1062  13  ASP A O   
85   C CB  . ASP A 27  ? 0.3988 0.4705 0.6780 0.0546  -0.0878 0.1287  13  ASP A CB  
86   C CG  . ASP A 27  ? 0.4309 0.5191 0.7159 0.0548  -0.1026 0.1381  13  ASP A CG  
87   O OD1 . ASP A 27  ? 0.5370 0.6439 0.8357 0.0527  -0.1064 0.1351  13  ASP A OD1 
88   O OD2 . ASP A 27  ? 0.4050 0.4875 0.6806 0.0567  -0.1106 0.1487  13  ASP A OD2 
89   N N   . ARG A 28  ? 0.3163 0.3674 0.5891 0.0505  -0.0603 0.1045  14  ARG A N   
90   C CA  . ARG A 28  ? 0.3691 0.4105 0.6468 0.0534  -0.0483 0.0963  14  ARG A CA  
91   C C   . ARG A 28  ? 0.3217 0.3725 0.6025 0.0493  -0.0429 0.0862  14  ARG A C   
92   O O   . ARG A 28  ? 0.3566 0.4071 0.6487 0.0536  -0.0345 0.0806  14  ARG A O   
93   C CB  . ARG A 28  ? 0.3314 0.3532 0.5908 0.0498  -0.0433 0.0941  14  ARG A CB  
94   C CG  . ARG A 28  ? 0.2936 0.3028 0.5513 0.0545  -0.0459 0.1040  14  ARG A CG  
95   C CD  . ARG A 28  ? 0.3801 0.3910 0.6604 0.0655  -0.0451 0.1088  14  ARG A CD  
96   N NE  . ARG A 28  ? 0.4488 0.4406 0.7287 0.0704  -0.0416 0.1135  14  ARG A NE  
97   C CZ  . ARG A 28  ? 0.4497 0.4388 0.7465 0.0806  -0.0424 0.1209  14  ARG A CZ  
98   N NH1 . ARG A 28  ? 0.5785 0.5842 0.8955 0.0874  -0.0467 0.1244  14  ARG A NH1 
99   N NH2 . ARG A 28  ? 0.4788 0.4479 0.7734 0.0840  -0.0387 0.1249  14  ARG A NH2 
100  N N   . LEU A 29  ? 0.3555 0.4135 0.6252 0.0410  -0.0474 0.0839  15  LEU A N   
101  C CA  . LEU A 29  ? 0.3078 0.3739 0.5792 0.0366  -0.0430 0.0755  15  LEU A CA  
102  C C   . LEU A 29  ? 0.4217 0.5039 0.7164 0.0413  -0.0422 0.0762  15  LEU A C   
103  O O   . LEU A 29  ? 0.3608 0.4448 0.6621 0.0422  -0.0335 0.0696  15  LEU A O   
104  C CB  . LEU A 29  ? 0.4389 0.5092 0.6957 0.0274  -0.0491 0.0743  15  LEU A CB  
105  C CG  . LEU A 29  ? 0.5442 0.6154 0.7944 0.0211  -0.0440 0.0655  15  LEU A CG  
106  C CD1 . LEU A 29  ? 0.6752 0.7359 0.9238 0.0235  -0.0336 0.0590  15  LEU A CD1 
107  C CD2 . LEU A 29  ? 0.4791 0.5457 0.7095 0.0130  -0.0482 0.0639  15  LEU A CD2 
108  N N   . THR A 30  ? 0.3513 0.4461 0.6586 0.0440  -0.0512 0.0844  16  THR A N   
109  C CA  . THR A 30  ? 0.3512 0.4634 0.6838 0.0488  -0.0504 0.0855  16  THR A CA  
110  C C   . THR A 30  ? 0.4016 0.5089 0.7499 0.0591  -0.0413 0.0850  16  THR A C   
111  O O   . THR A 30  ? 0.3401 0.4566 0.7045 0.0621  -0.0339 0.0809  16  THR A O   
112  C CB  . THR A 30  ? 0.3184 0.4465 0.6624 0.0494  -0.0634 0.0948  16  THR A CB  
113  O OG1 . THR A 30  ? 0.7646 0.8900 1.1197 0.0592  -0.0663 0.1033  16  THR A OG1 
114  C CG2 . THR A 30  ? 0.3348 0.4603 0.6571 0.0404  -0.0732 0.0966  16  THR A CG2 
115  N N   . ASP A 31  ? 0.3573 0.4493 0.7006 0.0645  -0.0410 0.0888  17  ASP A N   
116  C CA  . ASP A 31  ? 0.3274 0.4112 0.6835 0.0740  -0.0317 0.0872  17  ASP A CA  
117  C C   . ASP A 31  ? 0.3121 0.3899 0.6635 0.0720  -0.0190 0.0754  17  ASP A C   
118  O O   . ASP A 31  ? 0.3841 0.4644 0.7510 0.0786  -0.0103 0.0718  17  ASP A O   
119  C CB  . ASP A 31  ? 0.4270 0.4910 0.7734 0.0776  -0.0327 0.0920  17  ASP A CB  
120  C CG  . ASP A 31  ? 0.4658 0.5343 0.8193 0.0823  -0.0443 0.1052  17  ASP A CG  
121  O OD1 . ASP A 31  ? 0.4904 0.5782 0.8609 0.0847  -0.0513 0.1105  17  ASP A OD1 
122  O OD2 . ASP A 31  ? 0.4524 0.5051 0.7942 0.0832  -0.0466 0.1106  17  ASP A OD2 
123  N N   . CYS A 32  ? 0.3009 0.3707 0.6306 0.0632  -0.0178 0.0694  18  CYS A N   
124  C CA  . CYS A 32  ? 0.3020 0.3653 0.6242 0.0607  -0.0072 0.0588  18  CYS A CA  
125  C C   . CYS A 32  ? 0.2922 0.3712 0.6222 0.0579  -0.0038 0.0549  18  CYS A C   
126  O O   . CYS A 32  ? 0.3839 0.4589 0.7089 0.0567  0.0055  0.0468  18  CYS A O   
127  C CB  . CYS A 32  ? 0.3447 0.3946 0.6426 0.0528  -0.0079 0.0547  18  CYS A CB  
128  S SG  . CYS A 32  ? 0.3642 0.3933 0.6530 0.0554  -0.0085 0.0577  18  CYS A SG  
129  N N   . GLY A 33  ? 0.2619 0.3582 0.6031 0.0563  -0.0110 0.0604  19  GLY A N   
130  C CA  . GLY A 33  ? 0.4137 0.5260 0.7662 0.0537  -0.0074 0.0577  19  GLY A CA  
131  C C   . GLY A 33  ? 0.4535 0.5724 0.7953 0.0433  -0.0129 0.0569  19  GLY A C   
132  O O   . GLY A 33  ? 0.4543 0.5847 0.8039 0.0401  -0.0090 0.0545  19  GLY A O   
133  N N   . ALA A 34  ? 0.3027 0.4144 0.6275 0.0379  -0.0212 0.0589  20  ALA A N   
134  C CA  . ALA A 34  ? 0.3863 0.5018 0.7000 0.0283  -0.0262 0.0574  20  ALA A CA  
135  C C   . ALA A 34  ? 0.4172 0.5468 0.7400 0.0259  -0.0378 0.0642  20  ALA A C   
136  O O   . ALA A 34  ? 0.4770 0.6055 0.8000 0.0291  -0.0454 0.0705  20  ALA A O   
137  C CB  . ALA A 34  ? 0.3012 0.4002 0.5901 0.0234  -0.0273 0.0544  20  ALA A CB  
138  N N   . ASP A 35  ? 0.4349 0.5777 0.7649 0.0198  -0.0393 0.0630  21  ASP A N   
139  C CA  . ASP A 35  ? 0.3219 0.4783 0.6587 0.0152  -0.0511 0.0680  21  ASP A CA  
140  C C   . ASP A 35  ? 0.3974 0.5482 0.7144 0.0048  -0.0562 0.0647  21  ASP A C   
141  O O   . ASP A 35  ? 0.3424 0.5023 0.6608 -0.0005 -0.0665 0.0675  21  ASP A O   
142  C CB  . ASP A 35  ? 0.2573 0.4346 0.6208 0.0156  -0.0501 0.0695  21  ASP A CB  
143  C CG  . ASP A 35  ? 0.4734 0.6569 0.8586 0.0267  -0.0437 0.0721  21  ASP A CG  
144  O OD1 . ASP A 35  ? 0.4591 0.6381 0.8462 0.0341  -0.0476 0.0771  21  ASP A OD1 
145  O OD2 . ASP A 35  ? 0.4195 0.6115 0.8196 0.0280  -0.0341 0.0692  21  ASP A OD2 
146  N N   . HIS A 36  ? 0.2995 0.4355 0.5981 0.0018  -0.0494 0.0586  22  HIS A N   
147  C CA  . HIS A 36  ? 0.2960 0.4250 0.5764 -0.0072 -0.0526 0.0549  22  HIS A CA  
148  C C   . HIS A 36  ? 0.3404 0.4510 0.5993 -0.0065 -0.0495 0.0519  22  HIS A C   
149  O O   . HIS A 36  ? 0.3006 0.4034 0.5585 -0.0007 -0.0427 0.0509  22  HIS A O   
150  C CB  . HIS A 36  ? 0.3047 0.4369 0.5878 -0.0130 -0.0469 0.0502  22  HIS A CB  
151  C CG  . HIS A 36  ? 0.3333 0.4843 0.6388 -0.0150 -0.0488 0.0527  22  HIS A CG  
152  N ND1 . HIS A 36  ? 0.2859 0.4480 0.6123 -0.0084 -0.0432 0.0549  22  HIS A ND1 
153  C CD2 . HIS A 36  ? 0.1931 0.3543 0.5044 -0.0232 -0.0554 0.0529  22  HIS A CD2 
154  C CE1 . HIS A 36  ? 0.2770 0.4565 0.6224 -0.0123 -0.0461 0.0569  22  HIS A CE1 
155  N NE2 . HIS A 36  ? 0.2837 0.4630 0.6204 -0.0216 -0.0539 0.0558  22  HIS A NE2 
156  N N   . LEU A 37  ? 0.2855 0.3896 0.5278 -0.0129 -0.0544 0.0502  23  LEU A N   
157  C CA  . LEU A 37  ? 0.3208 0.4090 0.5435 -0.0136 -0.0513 0.0469  23  LEU A CA  
158  C C   . LEU A 37  ? 0.3086 0.3917 0.5207 -0.0207 -0.0497 0.0412  23  LEU A C   
159  O O   . LEU A 37  ? 0.2754 0.3620 0.4842 -0.0270 -0.0558 0.0407  23  LEU A O   
160  C CB  . LEU A 37  ? 0.2393 0.3227 0.4507 -0.0134 -0.0579 0.0508  23  LEU A CB  
161  C CG  . LEU A 37  ? 0.2610 0.3293 0.4531 -0.0146 -0.0544 0.0476  23  LEU A CG  
162  C CD1 . LEU A 37  ? 0.2678 0.3284 0.4620 -0.0092 -0.0460 0.0460  23  LEU A CD1 
163  C CD2 . LEU A 37  ? 0.3199 0.3843 0.5001 -0.0153 -0.0606 0.0522  23  LEU A CD2 
164  N N   . PHE A 38  ? 0.2756 0.3505 0.4829 -0.0198 -0.0418 0.0369  24  PHE A N   
165  C CA  . PHE A 38  ? 0.2845 0.3528 0.4822 -0.0253 -0.0396 0.0321  24  PHE A CA  
166  C C   . PHE A 38  ? 0.3090 0.3651 0.4898 -0.0262 -0.0396 0.0295  24  PHE A C   
167  O O   . PHE A 38  ? 0.3228 0.3740 0.4996 -0.0221 -0.0383 0.0307  24  PHE A O   
168  C CB  . PHE A 38  ? 0.2186 0.2851 0.4199 -0.0237 -0.0317 0.0296  24  PHE A CB  
169  C CG  . PHE A 38  ? 0.2725 0.3509 0.4903 -0.0226 -0.0295 0.0318  24  PHE A CG  
170  C CD1 . PHE A 38  ? 0.2433 0.3268 0.4717 -0.0161 -0.0267 0.0340  24  PHE A CD1 
171  C CD2 . PHE A 38  ? 0.2315 0.3155 0.4549 -0.0284 -0.0295 0.0313  24  PHE A CD2 
172  C CE1 . PHE A 38  ? 0.2392 0.3344 0.4840 -0.0147 -0.0234 0.0356  24  PHE A CE1 
173  C CE2 . PHE A 38  ? 0.2707 0.3667 0.5105 -0.0278 -0.0264 0.0334  24  PHE A CE2 
174  C CZ  . PHE A 38  ? 0.2874 0.3897 0.5382 -0.0207 -0.0231 0.0355  24  PHE A CZ  
175  N N   . GLY A 39  ? 0.2849 0.3356 0.4565 -0.0317 -0.0404 0.0258  25  GLY A N   
176  C CA  . GLY A 39  ? 0.3111 0.3505 0.4685 -0.0320 -0.0382 0.0226  25  GLY A CA  
177  C C   . GLY A 39  ? 0.3637 0.3980 0.5111 -0.0382 -0.0406 0.0188  25  GLY A C   
178  O O   . GLY A 39  ? 0.2924 0.3303 0.4439 -0.0429 -0.0431 0.0178  25  GLY A O   
179  N N   . VAL A 40  ? 0.2910 0.3165 0.4258 -0.0383 -0.0390 0.0163  26  VAL A N   
180  C CA  . VAL A 40  ? 0.3315 0.3498 0.4546 -0.0435 -0.0399 0.0115  26  VAL A CA  
181  C C   . VAL A 40  ? 0.3706 0.3859 0.4810 -0.0440 -0.0418 0.0120  26  VAL A C   
182  O O   . VAL A 40  ? 0.3428 0.3557 0.4513 -0.0399 -0.0383 0.0138  26  VAL A O   
183  C CB  . VAL A 40  ? 0.3347 0.3437 0.4552 -0.0426 -0.0335 0.0070  26  VAL A CB  
184  C CG1 . VAL A 40  ? 0.2470 0.2468 0.3553 -0.0471 -0.0332 0.0014  26  VAL A CG1 
185  C CG2 . VAL A 40  ? 0.2929 0.3041 0.4238 -0.0424 -0.0318 0.0076  26  VAL A CG2 
186  N N   . PRO A 41  ? 0.3306 0.3453 0.4311 -0.0495 -0.0470 0.0105  27  PRO A N   
187  C CA  . PRO A 41  ? 0.2665 0.2781 0.3525 -0.0502 -0.0487 0.0117  27  PRO A CA  
188  C C   . PRO A 41  ? 0.3868 0.3872 0.4605 -0.0499 -0.0412 0.0066  27  PRO A C   
189  O O   . PRO A 41  ? 0.3147 0.3090 0.3895 -0.0502 -0.0362 0.0012  27  PRO A O   
190  C CB  . PRO A 41  ? 0.3184 0.3330 0.3968 -0.0570 -0.0572 0.0106  27  PRO A CB  
191  C CG  . PRO A 41  ? 0.3110 0.3242 0.3955 -0.0610 -0.0566 0.0053  27  PRO A CG  
192  C CD  . PRO A 41  ? 0.3081 0.3251 0.4098 -0.0559 -0.0520 0.0077  27  PRO A CD  
193  N N   . GLY A 42  ? 0.3883 0.3861 0.4510 -0.0492 -0.0402 0.0089  28  GLY A N   
194  C CA  . GLY A 42  ? 0.4360 0.4245 0.4862 -0.0495 -0.0328 0.0044  28  GLY A CA  
195  C C   . GLY A 42  ? 0.3968 0.3837 0.4304 -0.0518 -0.0349 0.0076  28  GLY A C   
196  O O   . GLY A 42  ? 0.4521 0.4451 0.4862 -0.0516 -0.0420 0.0144  28  GLY A O   
197  N N   . ASP A 43  ? 0.4473 0.4258 0.4658 -0.0537 -0.0285 0.0029  29  ASP A N   
198  C CA  . ASP A 43  ? 0.4212 0.3969 0.4201 -0.0567 -0.0300 0.0057  29  ASP A CA  
199  C C   . ASP A 43  ? 0.5153 0.4942 0.5179 -0.0529 -0.0301 0.0151  29  ASP A C   
200  O O   . ASP A 43  ? 0.4898 0.4697 0.4809 -0.0546 -0.0359 0.0212  29  ASP A O   
201  C CB  . ASP A 43  ? 0.5407 0.5066 0.5229 -0.0591 -0.0209 -0.0015 29  ASP A CB  
202  C CG  . ASP A 43  ? 0.5423 0.5058 0.5293 -0.0550 -0.0101 -0.0006 29  ASP A CG  
203  O OD1 . ASP A 43  ? 0.6249 0.5922 0.6311 -0.0504 -0.0078 0.0008  29  ASP A OD1 
204  O OD2 . ASP A 43  ? 0.6666 0.6247 0.6376 -0.0569 -0.0038 -0.0014 29  ASP A OD2 
205  N N   . TYR A 44  ? 0.4446 0.4249 0.4634 -0.0479 -0.0247 0.0166  30  TYR A N   
206  C CA  . TYR A 44  ? 0.5090 0.4905 0.5323 -0.0446 -0.0240 0.0248  30  TYR A CA  
207  C C   . TYR A 44  ? 0.5115 0.5001 0.5451 -0.0421 -0.0331 0.0321  30  TYR A C   
208  O O   . TYR A 44  ? 0.4314 0.4196 0.4671 -0.0394 -0.0336 0.0395  30  TYR A O   
209  C CB  . TYR A 44  ? 0.4150 0.3955 0.4521 -0.0408 -0.0155 0.0230  30  TYR A CB  
210  C CG  . TYR A 44  ? 0.4448 0.4197 0.4748 -0.0423 -0.0056 0.0171  30  TYR A CG  
211  C CD1 . TYR A 44  ? 0.4689 0.4384 0.4803 -0.0457 -0.0017 0.0179  30  TYR A CD1 
212  C CD2 . TYR A 44  ? 0.4720 0.4473 0.5140 -0.0402 -0.0002 0.0110  30  TYR A CD2 
213  C CE1 . TYR A 44  ? 0.4190 0.3842 0.4252 -0.0467 0.0085  0.0122  30  TYR A CE1 
214  C CE2 . TYR A 44  ? 0.3898 0.3613 0.4282 -0.0408 0.0090  0.0058  30  TYR A CE2 
215  C CZ  . TYR A 44  ? 0.4172 0.3839 0.4384 -0.0440 0.0138  0.0060  30  TYR A CZ  
216  O OH  . TYR A 44  ? 0.4685 0.4322 0.4875 -0.0443 0.0241  0.0004  30  TYR A OH  
217  N N   . ASN A 45  ? 0.4395 0.4345 0.4807 -0.0429 -0.0399 0.0303  31  ASN A N   
218  C CA  . ASN A 45  ? 0.4457 0.4492 0.4997 -0.0400 -0.0478 0.0370  31  ASN A CA  
219  C C   . ASN A 45  ? 0.4109 0.4209 0.4602 -0.0439 -0.0583 0.0383  31  ASN A C   
220  O O   . ASN A 45  ? 0.4377 0.4569 0.5010 -0.0416 -0.0649 0.0428  31  ASN A O   
221  C CB  . ASN A 45  ? 0.3959 0.4040 0.4707 -0.0360 -0.0453 0.0350  31  ASN A CB  
222  C CG  . ASN A 45  ? 0.4364 0.4461 0.5147 -0.0390 -0.0452 0.0277  31  ASN A CG  
223  O OD1 . ASN A 45  ? 0.4392 0.4500 0.5096 -0.0439 -0.0502 0.0253  31  ASN A OD1 
224  N ND2 . ASN A 45  ? 0.3486 0.3582 0.4386 -0.0362 -0.0398 0.0245  31  ASN A ND2 
225  N N   . LEU A 46  ? 0.3529 0.3586 0.3833 -0.0499 -0.0601 0.0340  32  LEU A N   
226  C CA  . LEU A 46  ? 0.4612 0.4733 0.4869 -0.0548 -0.0710 0.0343  32  LEU A CA  
227  C C   . LEU A 46  ? 0.4877 0.5062 0.5122 -0.0530 -0.0806 0.0447  32  LEU A C   
228  O O   . LEU A 46  ? 0.3686 0.3982 0.4042 -0.0534 -0.0903 0.0480  32  LEU A O   
229  C CB  . LEU A 46  ? 0.4219 0.4260 0.4250 -0.0619 -0.0702 0.0266  32  LEU A CB  
230  C CG  . LEU A 46  ? 0.4148 0.4127 0.4203 -0.0638 -0.0626 0.0160  32  LEU A CG  
231  C CD1 . LEU A 46  ? 0.3615 0.3530 0.3472 -0.0714 -0.0645 0.0081  32  LEU A CD1 
232  C CD2 . LEU A 46  ? 0.3833 0.3887 0.4116 -0.0623 -0.0643 0.0151  32  LEU A CD2 
233  N N   . GLN A 47  ? 0.4248 0.4368 0.4370 -0.0510 -0.0779 0.0506  33  GLN A N   
234  C CA  . GLN A 47  ? 0.4630 0.4795 0.4726 -0.0489 -0.0872 0.0618  33  GLN A CA  
235  C C   . GLN A 47  ? 0.4562 0.4812 0.4920 -0.0415 -0.0896 0.0684  33  GLN A C   
236  O O   . GLN A 47  ? 0.4203 0.4547 0.4633 -0.0397 -0.1002 0.0758  33  GLN A O   
237  C CB  . GLN A 47  ? 0.5133 0.5190 0.5035 -0.0486 -0.0823 0.0670  33  GLN A CB  
238  C CG  . GLN A 47  ? 0.7205 0.7163 0.6868 -0.0547 -0.0751 0.0591  33  GLN A CG  
239  C CD  . GLN A 47  ? 0.7607 0.7513 0.6994 -0.0585 -0.0794 0.0649  33  GLN A CD  
240  O OE1 . GLN A 47  ? 0.8386 0.8352 0.7739 -0.0585 -0.0917 0.0730  33  GLN A OE1 
241  N NE2 . GLN A 47  ? 0.8919 0.8717 0.8110 -0.0616 -0.0692 0.0611  33  GLN A NE2 
242  N N   . PHE A 48  ? 0.4242 0.4463 0.4746 -0.0371 -0.0799 0.0656  34  PHE A N   
243  C CA  . PHE A 48  ? 0.4493 0.4788 0.5242 -0.0304 -0.0808 0.0697  34  PHE A CA  
244  C C   . PHE A 48  ? 0.4392 0.4819 0.5289 -0.0318 -0.0877 0.0673  34  PHE A C   
245  O O   . PHE A 48  ? 0.4632 0.5160 0.5692 -0.0276 -0.0940 0.0736  34  PHE A O   
246  C CB  . PHE A 48  ? 0.2957 0.3190 0.3804 -0.0269 -0.0693 0.0652  34  PHE A CB  
247  C CG  . PHE A 48  ? 0.4781 0.5076 0.5860 -0.0204 -0.0686 0.0676  34  PHE A CG  
248  C CD1 . PHE A 48  ? 0.4273 0.4567 0.5429 -0.0144 -0.0710 0.0765  34  PHE A CD1 
249  C CD2 . PHE A 48  ? 0.4088 0.4432 0.5302 -0.0200 -0.0649 0.0611  34  PHE A CD2 
250  C CE1 . PHE A 48  ? 0.3562 0.3904 0.4929 -0.0081 -0.0693 0.0777  34  PHE A CE1 
251  C CE2 . PHE A 48  ? 0.3738 0.4134 0.5149 -0.0142 -0.0632 0.0627  34  PHE A CE2 
252  C CZ  . PHE A 48  ? 0.3917 0.4312 0.5407 -0.0081 -0.0651 0.0705  34  PHE A CZ  
253  N N   . LEU A 49  ? 0.4381 0.4808 0.5232 -0.0377 -0.0864 0.0584  35  LEU A N   
254  C CA  . LEU A 49  ? 0.4423 0.4967 0.5420 -0.0402 -0.0917 0.0557  35  LEU A CA  
255  C C   . LEU A 49  ? 0.3417 0.4070 0.4411 -0.0429 -0.1053 0.0613  35  LEU A C   
256  O O   . LEU A 49  ? 0.4083 0.4871 0.5269 -0.0425 -0.1108 0.0629  35  LEU A O   
257  C CB  . LEU A 49  ? 0.3834 0.4326 0.4757 -0.0466 -0.0874 0.0454  35  LEU A CB  
258  C CG  . LEU A 49  ? 0.3975 0.4425 0.5004 -0.0436 -0.0767 0.0404  35  LEU A CG  
259  C CD1 . LEU A 49  ? 0.2843 0.3215 0.3774 -0.0492 -0.0724 0.0311  35  LEU A CD1 
260  C CD2 . LEU A 49  ? 0.3681 0.4245 0.4946 -0.0403 -0.0776 0.0426  35  LEU A CD2 
261  N N   . ASP A 50  ? 0.3489 0.4094 0.4269 -0.0459 -0.1108 0.0645  36  ASP A N   
262  C CA  . ASP A 50  ? 0.3898 0.4611 0.4667 -0.0479 -0.1251 0.0712  36  ASP A CA  
263  C C   . ASP A 50  ? 0.4286 0.5112 0.5291 -0.0395 -0.1297 0.0812  36  ASP A C   
264  O O   . ASP A 50  ? 0.4179 0.5158 0.5329 -0.0400 -0.1402 0.0848  36  ASP A O   
265  C CB  . ASP A 50  ? 0.5355 0.5979 0.5833 -0.0510 -0.1291 0.0746  36  ASP A CB  
266  C CG  . ASP A 50  ? 0.5821 0.6358 0.6062 -0.0602 -0.1272 0.0644  36  ASP A CG  
267  O OD1 . ASP A 50  ? 0.5604 0.6154 0.5918 -0.0643 -0.1243 0.0552  36  ASP A OD1 
268  O OD2 . ASP A 50  ? 0.4918 0.5365 0.4897 -0.0633 -0.1280 0.0656  36  ASP A OD2 
269  N N   . HIS A 51  ? 0.4173 0.4926 0.5229 -0.0317 -0.1217 0.0857  37  HIS A N   
270  C CA  . HIS A 51  ? 0.4144 0.4982 0.5429 -0.0228 -0.1245 0.0945  37  HIS A CA  
271  C C   . HIS A 51  ? 0.3918 0.4865 0.5473 -0.0203 -0.1206 0.0902  37  HIS A C   
272  O O   . HIS A 51  ? 0.3540 0.4620 0.5313 -0.0152 -0.1261 0.0962  37  HIS A O   
273  C CB  . HIS A 51  ? 0.3471 0.4176 0.4718 -0.0161 -0.1166 0.0996  37  HIS A CB  
274  C CG  . HIS A 51  ? 0.3565 0.4169 0.4557 -0.0182 -0.1201 0.1057  37  HIS A CG  
275  N ND1 . HIS A 51  ? 0.3782 0.4408 0.4766 -0.0139 -0.1294 0.1180  37  HIS A ND1 
276  C CD2 . HIS A 51  ? 0.3651 0.4133 0.4383 -0.0243 -0.1154 0.1015  37  HIS A CD2 
277  C CE1 . HIS A 51  ? 0.4424 0.4940 0.5137 -0.0177 -0.1302 0.1214  37  HIS A CE1 
278  N NE2 . HIS A 51  ? 0.3778 0.4208 0.4337 -0.0240 -0.1213 0.1111  37  HIS A NE2 
279  N N   . VAL A 52  ? 0.3909 0.4803 0.5456 -0.0235 -0.1109 0.0805  38  VAL A N   
280  C CA  . VAL A 52  ? 0.3115 0.4107 0.4888 -0.0224 -0.1070 0.0764  38  VAL A CA  
281  C C   . VAL A 52  ? 0.4038 0.5189 0.5906 -0.0281 -0.1171 0.0761  38  VAL A C   
282  O O   . VAL A 52  ? 0.3927 0.5224 0.6038 -0.0249 -0.1192 0.0788  38  VAL A O   
283  C CB  . VAL A 52  ? 0.3437 0.4327 0.5151 -0.0250 -0.0953 0.0668  38  VAL A CB  
284  C CG1 . VAL A 52  ? 0.3295 0.4277 0.5220 -0.0241 -0.0908 0.0633  38  VAL A CG1 
285  C CG2 . VAL A 52  ? 0.3147 0.3895 0.4783 -0.0200 -0.0862 0.0670  38  VAL A CG2 
286  N N   . ILE A 53  ? 0.4269 0.5396 0.5952 -0.0370 -0.1233 0.0723  39  ILE A N   
287  C CA  . ILE A 53  ? 0.4007 0.5279 0.5766 -0.0439 -0.1342 0.0714  39  ILE A CA  
288  C C   . ILE A 53  ? 0.5062 0.6487 0.6956 -0.0397 -0.1465 0.0819  39  ILE A C   
289  O O   . ILE A 53  ? 0.4316 0.5920 0.6444 -0.0401 -0.1523 0.0838  39  ILE A O   
290  C CB  . ILE A 53  ? 0.4044 0.5233 0.5544 -0.0542 -0.1384 0.0648  39  ILE A CB  
291  C CG1 . ILE A 53  ? 0.3231 0.4286 0.4646 -0.0578 -0.1265 0.0545  39  ILE A CG1 
292  C CG2 . ILE A 53  ? 0.3942 0.5281 0.5507 -0.0622 -0.1517 0.0643  39  ILE A CG2 
293  C CD1 . ILE A 53  ? 0.4249 0.5384 0.5877 -0.0597 -0.1224 0.0503  39  ILE A CD1 
294  N N   . ASP A 54  ? 0.4365 0.5725 0.6120 -0.0356 -0.1507 0.0893  40  ASP A N   
295  C CA  . ASP A 54  ? 0.5081 0.6573 0.6938 -0.0313 -0.1637 0.1005  40  ASP A CA  
296  C C   . ASP A 54  ? 0.4869 0.6453 0.7029 -0.0201 -0.1600 0.1070  40  ASP A C   
297  O O   . ASP A 54  ? 0.4954 0.6694 0.7290 -0.0160 -0.1707 0.1155  40  ASP A O   
298  C CB  . ASP A 54  ? 0.5498 0.6871 0.7089 -0.0304 -0.1685 0.1071  40  ASP A CB  
299  C CG  . ASP A 54  ? 0.6783 0.8141 0.8112 -0.0412 -0.1785 0.1038  40  ASP A CG  
300  O OD1 . ASP A 54  ? 0.7098 0.8542 0.8470 -0.0494 -0.1828 0.0965  40  ASP A OD1 
301  O OD2 . ASP A 54  ? 0.7586 0.8838 0.8658 -0.0419 -0.1818 0.1084  40  ASP A OD2 
302  N N   . SER A 55  ? 0.4980 0.6471 0.7204 -0.0149 -0.1455 0.1030  41  SER A N   
303  C CA  . SER A 55  ? 0.4363 0.5916 0.6851 -0.0040 -0.1407 0.1082  41  SER A CA  
304  C C   . SER A 55  ? 0.4514 0.6282 0.7298 -0.0042 -0.1433 0.1073  41  SER A C   
305  O O   . SER A 55  ? 0.4938 0.6742 0.7734 -0.0119 -0.1400 0.0991  41  SER A O   
306  C CB  . SER A 55  ? 0.4787 0.6186 0.7251 0.0001  -0.1246 0.1026  41  SER A CB  
307  O OG  . SER A 55  ? 0.4762 0.6247 0.7498 0.0073  -0.1179 0.1026  41  SER A OG  
308  N N   . PRO A 56  ? 0.5547 0.7460 0.8582 0.0040  -0.1486 0.1159  42  PRO A N   
309  C CA  . PRO A 56  ? 0.4944 0.7073 0.8294 0.0045  -0.1490 0.1149  42  PRO A CA  
310  C C   . PRO A 56  ? 0.4730 0.6838 0.8243 0.0101  -0.1327 0.1097  42  PRO A C   
311  O O   . PRO A 56  ? 0.4452 0.6728 0.8211 0.0096  -0.1302 0.1078  42  PRO A O   
312  C CB  . PRO A 56  ? 0.4932 0.7221 0.8485 0.0122  -0.1613 0.1269  42  PRO A CB  
313  C CG  . PRO A 56  ? 0.4474 0.6586 0.7886 0.0207  -0.1595 0.1335  42  PRO A CG  
314  C CD  . PRO A 56  ? 0.4642 0.6535 0.7691 0.0131  -0.1552 0.1274  42  PRO A CD  
315  N N   . ASP A 57  ? 0.4719 0.6630 0.8100 0.0149  -0.1215 0.1073  43  ASP A N   
316  C CA  . ASP A 57  ? 0.2846 0.4721 0.6355 0.0208  -0.1065 0.1025  43  ASP A CA  
317  C C   . ASP A 57  ? 0.4040 0.5780 0.7373 0.0143  -0.0957 0.0921  43  ASP A C   
318  O O   . ASP A 57  ? 0.4113 0.5858 0.7551 0.0166  -0.0843 0.0871  43  ASP A O   
319  C CB  . ASP A 57  ? 0.5104 0.6860 0.8631 0.0321  -0.1016 0.1073  43  ASP A CB  
320  C CG  . ASP A 57  ? 0.5804 0.7669 0.9499 0.0400  -0.1124 0.1189  43  ASP A CG  
321  O OD1 . ASP A 57  ? 0.4322 0.6367 0.8311 0.0454  -0.1127 0.1215  43  ASP A OD1 
322  O OD2 . ASP A 57  ? 0.5639 0.7412 0.9176 0.0410  -0.1204 0.1257  43  ASP A OD2 
323  N N   . ILE A 58  ? 0.3109 0.4730 0.6178 0.0065  -0.0988 0.0889  44  ILE A N   
324  C CA  . ILE A 58  ? 0.3184 0.4668 0.6082 0.0012  -0.0893 0.0799  44  ILE A CA  
325  C C   . ILE A 58  ? 0.3661 0.5186 0.6471 -0.0100 -0.0948 0.0754  44  ILE A C   
326  O O   . ILE A 58  ? 0.3361 0.4904 0.6064 -0.0148 -0.1057 0.0780  44  ILE A O   
327  C CB  . ILE A 58  ? 0.2985 0.4266 0.5653 0.0027  -0.0857 0.0793  44  ILE A CB  
328  C CG1 . ILE A 58  ? 0.4693 0.5918 0.7451 0.0132  -0.0805 0.0835  44  ILE A CG1 
329  C CG2 . ILE A 58  ? 0.2863 0.4021 0.5378 -0.0024 -0.0767 0.0703  44  ILE A CG2 
330  C CD1 . ILE A 58  ? 0.5048 0.6221 0.7874 0.0167  -0.0673 0.0772  44  ILE A CD1 
331  N N   . CYS A 59  ? 0.3373 0.4901 0.6214 -0.0143 -0.0871 0.0687  45  CYS A N   
332  C CA  . CYS A 59  ? 0.3139 0.4685 0.5909 -0.0249 -0.0906 0.0638  45  CYS A CA  
333  C C   . CYS A 59  ? 0.2809 0.4166 0.5352 -0.0284 -0.0833 0.0569  45  CYS A C   
334  O O   . CYS A 59  ? 0.2655 0.3940 0.5201 -0.0249 -0.0727 0.0538  45  CYS A O   
335  C CB  . CYS A 59  ? 0.3257 0.4953 0.6252 -0.0276 -0.0875 0.0624  45  CYS A CB  
336  S SG  . CYS A 59  ? 0.4543 0.6239 0.7470 -0.0411 -0.0897 0.0559  45  CYS A SG  
337  N N   . TRP A 60  ? 0.3114 0.4395 0.5461 -0.0352 -0.0890 0.0543  46  TRP A N   
338  C CA  . TRP A 60  ? 0.3981 0.5095 0.6133 -0.0385 -0.0823 0.0476  46  TRP A CA  
339  C C   . TRP A 60  ? 0.3233 0.4353 0.5439 -0.0439 -0.0772 0.0422  46  TRP A C   
340  O O   . TRP A 60  ? 0.3416 0.4638 0.5715 -0.0502 -0.0823 0.0418  46  TRP A O   
341  C CB  . TRP A 60  ? 0.3028 0.4058 0.4959 -0.0441 -0.0889 0.0458  46  TRP A CB  
342  C CG  . TRP A 60  ? 0.3226 0.4100 0.4982 -0.0478 -0.0822 0.0385  46  TRP A CG  
343  C CD1 . TRP A 60  ? 0.3386 0.4213 0.5046 -0.0561 -0.0838 0.0324  46  TRP A CD1 
344  C CD2 . TRP A 60  ? 0.2942 0.3689 0.4613 -0.0431 -0.0729 0.0364  46  TRP A CD2 
345  N NE1 . TRP A 60  ? 0.3857 0.4535 0.5385 -0.0560 -0.0758 0.0270  46  TRP A NE1 
346  C CE2 . TRP A 60  ? 0.3949 0.4585 0.5485 -0.0483 -0.0694 0.0295  46  TRP A CE2 
347  C CE3 . TRP A 60  ? 0.2810 0.3525 0.4513 -0.0354 -0.0675 0.0394  46  TRP A CE3 
348  C CZ2 . TRP A 60  ? 0.3060 0.3575 0.4509 -0.0454 -0.0610 0.0261  46  TRP A CZ2 
349  C CZ3 . TRP A 60  ? 0.3349 0.3941 0.4955 -0.0336 -0.0595 0.0356  46  TRP A CZ3 
350  C CH2 . TRP A 60  ? 0.2944 0.3447 0.4431 -0.0384 -0.0566 0.0293  46  TRP A CH2 
351  N N   . VAL A 61  ? 0.3325 0.4334 0.5473 -0.0418 -0.0673 0.0384  47  VAL A N   
352  C CA  . VAL A 61  ? 0.3509 0.4494 0.5681 -0.0464 -0.0616 0.0341  47  VAL A CA  
353  C C   . VAL A 61  ? 0.2802 0.3614 0.4776 -0.0482 -0.0576 0.0289  47  VAL A C   
354  O O   . VAL A 61  ? 0.2603 0.3333 0.4531 -0.0432 -0.0505 0.0278  47  VAL A O   
355  C CB  . VAL A 61  ? 0.2818 0.3853 0.5134 -0.0415 -0.0531 0.0354  47  VAL A CB  
356  C CG1 . VAL A 61  ? 0.2306 0.3312 0.4632 -0.0470 -0.0477 0.0321  47  VAL A CG1 
357  C CG2 . VAL A 61  ? 0.2706 0.3915 0.5235 -0.0383 -0.0560 0.0406  47  VAL A CG2 
358  N N   . GLY A 62  ? 0.3301 0.4060 0.5166 -0.0553 -0.0621 0.0252  48  GLY A N   
359  C CA  . GLY A 62  ? 0.2745 0.3346 0.4445 -0.0568 -0.0577 0.0198  48  GLY A CA  
360  C C   . GLY A 62  ? 0.3909 0.4459 0.5651 -0.0573 -0.0503 0.0177  48  GLY A C   
361  O O   . GLY A 62  ? 0.2803 0.3417 0.4656 -0.0614 -0.0503 0.0183  48  GLY A O   
362  N N   . CYS A 63  ? 0.3003 0.3442 0.4659 -0.0532 -0.0441 0.0157  49  CYS A N   
363  C CA  . CYS A 63  ? 0.3711 0.4091 0.5384 -0.0527 -0.0375 0.0146  49  CYS A CA  
364  C C   . CYS A 63  ? 0.4007 0.4244 0.5557 -0.0552 -0.0357 0.0098  49  CYS A C   
365  O O   . CYS A 63  ? 0.3455 0.3634 0.4898 -0.0565 -0.0381 0.0066  49  CYS A O   
366  C CB  . CYS A 63  ? 0.3545 0.3928 0.5242 -0.0451 -0.0322 0.0167  49  CYS A CB  
367  S SG  . CYS A 63  ? 0.3055 0.3591 0.4911 -0.0413 -0.0323 0.0216  49  CYS A SG  
368  N N   . ALA A 64  ? 0.3924 0.4098 0.5487 -0.0557 -0.0310 0.0094  50  ALA A N   
369  C CA  . ALA A 64  ? 0.4695 0.4728 0.6165 -0.0577 -0.0292 0.0052  50  ALA A CA  
370  C C   . ALA A 64  ? 0.4338 0.4293 0.5731 -0.0514 -0.0257 0.0037  50  ALA A C   
371  O O   . ALA A 64  ? 0.4806 0.4658 0.6118 -0.0521 -0.0246 -0.0006 50  ALA A O   
372  C CB  . ALA A 64  ? 0.3171 0.3158 0.4687 -0.0608 -0.0259 0.0064  50  ALA A CB  
373  N N   . ASN A 65  ? 0.3382 0.3386 0.4807 -0.0454 -0.0235 0.0066  51  ASN A N   
374  C CA  . ASN A 65  ? 0.3950 0.3911 0.5320 -0.0402 -0.0213 0.0051  51  ASN A CA  
375  C C   . ASN A 65  ? 0.3688 0.3730 0.5104 -0.0356 -0.0209 0.0082  51  ASN A C   
376  O O   . ASN A 65  ? 0.2707 0.2826 0.4196 -0.0355 -0.0213 0.0112  51  ASN A O   
377  C CB  . ASN A 65  ? 0.2630 0.2496 0.3978 -0.0376 -0.0176 0.0039  51  ASN A CB  
378  C CG  . ASN A 65  ? 0.3102 0.2982 0.4497 -0.0356 -0.0156 0.0076  51  ASN A CG  
379  O OD1 . ASN A 65  ? 0.3101 0.3060 0.4537 -0.0335 -0.0153 0.0102  51  ASN A OD1 
380  N ND2 . ASN A 65  ? 0.2363 0.2158 0.3744 -0.0360 -0.0139 0.0079  51  ASN A ND2 
381  N N   . GLU A 66  ? 0.3309 0.3330 0.4688 -0.0318 -0.0196 0.0071  52  GLU A N   
382  C CA  . GLU A 66  ? 0.3466 0.3544 0.4881 -0.0281 -0.0194 0.0094  52  GLU A CA  
383  C C   . GLU A 66  ? 0.3406 0.3504 0.4870 -0.0250 -0.0169 0.0108  52  GLU A C   
384  O O   . GLU A 66  ? 0.3270 0.3427 0.4785 -0.0231 -0.0166 0.0128  52  GLU A O   
385  C CB  . GLU A 66  ? 0.2753 0.2797 0.4119 -0.0260 -0.0181 0.0079  52  GLU A CB  
386  C CG  . GLU A 66  ? 0.2939 0.2973 0.4239 -0.0288 -0.0202 0.0073  52  GLU A CG  
387  C CD  . GLU A 66  ? 0.3722 0.3683 0.4948 -0.0316 -0.0192 0.0031  52  GLU A CD  
388  O OE1 . GLU A 66  ? 0.2469 0.2386 0.3712 -0.0313 -0.0173 0.0013  52  GLU A OE1 
389  O OE2 . GLU A 66  ? 0.3316 0.3254 0.4459 -0.0340 -0.0200 0.0016  52  GLU A OE2 
390  N N   . LEU A 67  ? 0.2855 0.2902 0.4299 -0.0242 -0.0150 0.0099  53  LEU A N   
391  C CA  . LEU A 67  ? 0.2561 0.2622 0.4023 -0.0218 -0.0130 0.0113  53  LEU A CA  
392  C C   . LEU A 67  ? 0.3193 0.3312 0.4703 -0.0237 -0.0123 0.0138  53  LEU A C   
393  O O   . LEU A 67  ? 0.2807 0.2974 0.4349 -0.0214 -0.0105 0.0147  53  LEU A O   
394  C CB  . LEU A 67  ? 0.2815 0.2810 0.4241 -0.0209 -0.0122 0.0111  53  LEU A CB  
395  C CG  . LEU A 67  ? 0.2860 0.2863 0.4274 -0.0187 -0.0108 0.0129  53  LEU A CG  
396  C CD1 . LEU A 67  ? 0.2527 0.2570 0.3949 -0.0158 -0.0105 0.0116  53  LEU A CD1 
397  C CD2 . LEU A 67  ? 0.3008 0.2946 0.4384 -0.0172 -0.0113 0.0137  53  LEU A CD2 
398  N N   . ASN A 68  ? 0.2400 0.2514 0.3923 -0.0281 -0.0132 0.0144  54  ASN A N   
399  C CA  . ASN A 68  ? 0.2450 0.2633 0.4042 -0.0308 -0.0123 0.0169  54  ASN A CA  
400  C C   . ASN A 68  ? 0.3033 0.3313 0.4699 -0.0296 -0.0138 0.0179  54  ASN A C   
401  O O   . ASN A 68  ? 0.2465 0.2817 0.4203 -0.0284 -0.0113 0.0197  54  ASN A O   
402  C CB  . ASN A 68  ? 0.2149 0.2306 0.3748 -0.0368 -0.0138 0.0169  54  ASN A CB  
403  C CG  . ASN A 68  ? 0.3418 0.3469 0.4957 -0.0376 -0.0117 0.0169  54  ASN A CG  
404  O OD1 . ASN A 68  ? 0.3701 0.3709 0.5194 -0.0335 -0.0100 0.0174  54  ASN A OD1 
405  N ND2 . ASN A 68  ? 0.3091 0.3098 0.4636 -0.0431 -0.0124 0.0167  54  ASN A ND2 
406  N N   . ALA A 69  ? 0.2769 0.3049 0.4419 -0.0297 -0.0177 0.0169  55  ALA A N   
407  C CA  . ALA A 69  ? 0.2898 0.3260 0.4614 -0.0280 -0.0199 0.0189  55  ALA A CA  
408  C C   . ALA A 69  ? 0.3013 0.3389 0.4758 -0.0223 -0.0164 0.0194  55  ALA A C   
409  O O   . ALA A 69  ? 0.2292 0.2743 0.4128 -0.0201 -0.0157 0.0215  55  ALA A O   
410  C CB  . ALA A 69  ? 0.2347 0.2687 0.4006 -0.0290 -0.0245 0.0184  55  ALA A CB  
411  N N   . SER A 70  ? 0.2623 0.2925 0.4296 -0.0199 -0.0142 0.0172  56  SER A N   
412  C CA  . SER A 70  ? 0.2696 0.2998 0.4384 -0.0154 -0.0111 0.0166  56  SER A CA  
413  C C   . SER A 70  ? 0.2605 0.2938 0.4323 -0.0146 -0.0067 0.0168  56  SER A C   
414  O O   . SER A 70  ? 0.2573 0.2941 0.4345 -0.0113 -0.0038 0.0168  56  SER A O   
415  C CB  . SER A 70  ? 0.2810 0.3037 0.4423 -0.0140 -0.0108 0.0140  56  SER A CB  
416  O OG  . SER A 70  ? 0.2546 0.2734 0.4107 -0.0146 -0.0094 0.0127  56  SER A OG  
417  N N   . TYR A 71  ? 0.2264 0.2579 0.3946 -0.0175 -0.0056 0.0171  57  TYR A N   
418  C CA  . TYR A 71  ? 0.2927 0.3274 0.4628 -0.0176 -0.0007 0.0181  57  TYR A CA  
419  C C   . TYR A 71  ? 0.3144 0.3595 0.4971 -0.0184 0.0005  0.0203  57  TYR A C   
420  O O   . TYR A 71  ? 0.2652 0.3152 0.4529 -0.0160 0.0056  0.0204  57  TYR A O   
421  C CB  . TYR A 71  ? 0.2416 0.2714 0.4055 -0.0212 -0.0001 0.0192  57  TYR A CB  
422  C CG  . TYR A 71  ? 0.2991 0.3201 0.4522 -0.0198 -0.0009 0.0179  57  TYR A CG  
423  C CD1 . TYR A 71  ? 0.2387 0.2577 0.3874 -0.0160 -0.0007 0.0155  57  TYR A CD1 
424  C CD2 . TYR A 71  ? 0.2463 0.2609 0.3944 -0.0223 -0.0020 0.0193  57  TYR A CD2 
425  C CE1 . TYR A 71  ? 0.2445 0.2573 0.3850 -0.0149 -0.0025 0.0146  57  TYR A CE1 
426  C CE2 . TYR A 71  ? 0.2770 0.2846 0.4171 -0.0203 -0.0034 0.0189  57  TYR A CE2 
427  C CZ  . TYR A 71  ? 0.3307 0.3384 0.4674 -0.0167 -0.0040 0.0166  57  TYR A CZ  
428  O OH  . TYR A 71  ? 0.2967 0.2993 0.4273 -0.0149 -0.0063 0.0164  57  TYR A OH  
429  N N   . ALA A 72  ? 0.2669 0.3161 0.4553 -0.0218 -0.0040 0.0218  58  ALA A N   
430  C CA  . ALA A 72  ? 0.3042 0.3652 0.5068 -0.0227 -0.0041 0.0243  58  ALA A CA  
431  C C   . ALA A 72  ? 0.2552 0.3214 0.4657 -0.0169 -0.0038 0.0248  58  ALA A C   
432  O O   . ALA A 72  ? 0.1895 0.2644 0.4115 -0.0146 0.0003  0.0260  58  ALA A O   
433  C CB  . ALA A 72  ? 0.1865 0.2504 0.3920 -0.0281 -0.0107 0.0254  58  ALA A CB  
434  N N   . ALA A 73  ? 0.2230 0.2833 0.4277 -0.0142 -0.0072 0.0240  59  ALA A N   
435  C CA  . ALA A 73  ? 0.3024 0.3649 0.5137 -0.0085 -0.0067 0.0248  59  ALA A CA  
436  C C   . ALA A 73  ? 0.2774 0.3381 0.4893 -0.0043 0.0010  0.0223  59  ALA A C   
437  O O   . ALA A 73  ? 0.3114 0.3781 0.5346 -0.0001 0.0042  0.0232  59  ALA A O   
438  C CB  . ALA A 73  ? 0.1820 0.2362 0.3849 -0.0073 -0.0106 0.0244  59  ALA A CB  
439  N N   . ASP A 74  ? 0.2585 0.3111 0.4582 -0.0054 0.0039  0.0191  60  ASP A N   
440  C CA  . ASP A 74  ? 0.2892 0.3394 0.4860 -0.0025 0.0108  0.0161  60  ASP A CA  
441  C C   . ASP A 74  ? 0.2989 0.3584 0.5054 -0.0024 0.0167  0.0174  60  ASP A C   
442  O O   . ASP A 74  ? 0.2455 0.3083 0.4595 0.0021  0.0221  0.0162  60  ASP A O   
443  C CB  . ASP A 74  ? 0.1929 0.2343 0.3745 -0.0046 0.0112  0.0134  60  ASP A CB  
444  C CG  . ASP A 74  ? 0.2975 0.3345 0.4722 -0.0019 0.0168  0.0094  60  ASP A CG  
445  O OD1 . ASP A 74  ? 0.2725 0.3139 0.4500 -0.0011 0.0233  0.0092  60  ASP A OD1 
446  O OD2 . ASP A 74  ? 0.2724 0.3018 0.4386 -0.0012 0.0150  0.0062  60  ASP A OD2 
447  N N   . GLY A 75  ? 0.2537 0.3177 0.4615 -0.0074 0.0163  0.0198  61  GLY A N   
448  C CA  . GLY A 75  ? 0.2304 0.3043 0.4487 -0.0083 0.0225  0.0215  61  GLY A CA  
449  C C   . GLY A 75  ? 0.2214 0.3075 0.4593 -0.0051 0.0220  0.0237  61  GLY A C   
450  O O   . GLY A 75  ? 0.1959 0.2892 0.4442 -0.0020 0.0293  0.0234  61  GLY A O   
451  N N   . TYR A 76  ? 0.2348 0.3232 0.4779 -0.0057 0.0135  0.0260  62  TYR A N   
452  C CA  . TYR A 76  ? 0.2346 0.3339 0.4956 -0.0018 0.0110  0.0290  62  TYR A CA  
453  C C   . TYR A 76  ? 0.2705 0.3667 0.5350 0.0063  0.0161  0.0271  62  TYR A C   
454  O O   . TYR A 76  ? 0.1968 0.3028 0.4778 0.0107  0.0208  0.0282  62  TYR A O   
455  C CB  . TYR A 76  ? 0.1829 0.2817 0.4425 -0.0039 0.0003  0.0316  62  TYR A CB  
456  C CG  . TYR A 76  ? 0.2662 0.3767 0.5431 -0.0008 -0.0050 0.0361  62  TYR A CG  
457  C CD1 . TYR A 76  ? 0.2387 0.3466 0.5194 0.0064  -0.0058 0.0375  62  TYR A CD1 
458  C CD2 . TYR A 76  ? 0.2081 0.3321 0.4977 -0.0054 -0.0100 0.0394  62  TYR A CD2 
459  C CE1 . TYR A 76  ? 0.1858 0.3043 0.4824 0.0099  -0.0116 0.0427  62  TYR A CE1 
460  C CE2 . TYR A 76  ? 0.2709 0.4069 0.5766 -0.0025 -0.0164 0.0440  62  TYR A CE2 
461  C CZ  . TYR A 76  ? 0.2470 0.3802 0.5561 0.0055  -0.0173 0.0461  62  TYR A CZ  
462  O OH  . TYR A 76  ? 0.2937 0.4388 0.6190 0.0087  -0.0244 0.0518  62  TYR A OH  
463  N N   . ALA A 77  ? 0.2646 0.3474 0.5150 0.0082  0.0156  0.0240  63  ALA A N   
464  C CA  . ALA A 77  ? 0.2304 0.3080 0.4833 0.0152  0.0201  0.0216  63  ALA A CA  
465  C C   . ALA A 77  ? 0.2946 0.3729 0.5483 0.0176  0.0310  0.0175  63  ALA A C   
466  O O   . ALA A 77  ? 0.2399 0.3189 0.5031 0.0240  0.0365  0.0160  63  ALA A O   
467  C CB  . ALA A 77  ? 0.2122 0.2752 0.4497 0.0153  0.0173  0.0188  63  ALA A CB  
468  N N   . ARG A 78  ? 0.2270 0.3047 0.4706 0.0128  0.0347  0.0158  64  ARG A N   
469  C CA  . ARG A 78  ? 0.2119 0.2911 0.4548 0.0145  0.0456  0.0124  64  ARG A CA  
470  C C   . ARG A 78  ? 0.2402 0.3351 0.5044 0.0162  0.0509  0.0154  64  ARG A C   
471  O O   . ARG A 78  ? 0.2315 0.3290 0.4981 0.0186  0.0616  0.0125  64  ARG A O   
472  C CB  . ARG A 78  ? 0.2155 0.2893 0.4405 0.0086  0.0477  0.0111  64  ARG A CB  
473  C CG  . ARG A 78  ? 0.2194 0.2791 0.4246 0.0075  0.0434  0.0077  64  ARG A CG  
474  C CD  . ARG A 78  ? 0.2767 0.3321 0.4657 0.0026  0.0452  0.0075  64  ARG A CD  
475  N NE  . ARG A 78  ? 0.2240 0.2679 0.3959 0.0014  0.0401  0.0048  64  ARG A NE  
476  C CZ  . ARG A 78  ? 0.3328 0.3698 0.4882 0.0006  0.0432  0.0016  64  ARG A CZ  
477  N NH1 . ARG A 78  ? 0.2882 0.3270 0.4393 0.0008  0.0521  0.0003  64  ARG A NH1 
478  N NH2 . ARG A 78  ? 0.2572 0.2858 0.3999 -0.0006 0.0370  -0.0002 64  ARG A NH2 
479  N N   . CYS A 79  ? 0.2044 0.3103 0.4842 0.0149  0.0439  0.0208  65  CYS A N   
480  C CA  . CYS A 79  ? 0.2339 0.3571 0.5376 0.0166  0.0474  0.0240  65  CYS A CA  
481  C C   . CYS A 79  ? 0.2920 0.4213 0.6144 0.0242  0.0440  0.0266  65  CYS A C   
482  O O   . CYS A 79  ? 0.2842 0.4246 0.6260 0.0294  0.0509  0.0271  65  CYS A O   
483  C CB  . CYS A 79  ? 0.2082 0.3418 0.5183 0.0086  0.0415  0.0286  65  CYS A CB  
484  S SG  . CYS A 79  ? 0.3391 0.4676 0.6325 0.0002  0.0475  0.0273  65  CYS A SG  
485  N N   . LYS A 80  ? 0.2064 0.3286 0.5237 0.0253  0.0342  0.0285  66  LYS A N   
486  C CA  . LYS A 80  ? 0.3137 0.4406 0.6475 0.0324  0.0298  0.0324  66  LYS A CA  
487  C C   . LYS A 80  ? 0.4143 0.5256 0.7401 0.0389  0.0319  0.0294  66  LYS A C   
488  O O   . LYS A 80  ? 0.3441 0.4572 0.6838 0.0460  0.0298  0.0327  66  LYS A O   
489  C CB  . LYS A 80  ? 0.3800 0.5123 0.7162 0.0285  0.0162  0.0385  66  LYS A CB  
490  C CG  . LYS A 80  ? 0.4308 0.5832 0.7864 0.0248  0.0129  0.0429  66  LYS A CG  
491  C CD  . LYS A 80  ? 0.3280 0.4861 0.6872 0.0225  -0.0012 0.0488  66  LYS A CD  
492  C CE  . LYS A 80  ? 0.3557 0.5353 0.7430 0.0246  -0.0050 0.0543  66  LYS A CE  
493  N NZ  . LYS A 80  ? 0.8300 1.0147 1.2366 0.0353  0.0030  0.0549  66  LYS A NZ  
494  N N   . GLY A 81  ? 0.2997 0.3958 0.6043 0.0367  0.0357  0.0234  67  GLY A N   
495  C CA  . GLY A 81  ? 0.3050 0.3856 0.6013 0.0414  0.0379  0.0195  67  GLY A CA  
496  C C   . GLY A 81  ? 0.3468 0.4170 0.6319 0.0392  0.0284  0.0218  67  GLY A C   
497  O O   . GLY A 81  ? 0.3668 0.4234 0.6451 0.0421  0.0299  0.0188  67  GLY A O   
498  N N   . PHE A 82  ? 0.3295 0.4054 0.6125 0.0339  0.0193  0.0267  68  PHE A N   
499  C CA  . PHE A 82  ? 0.2362 0.3036 0.5088 0.0316  0.0110  0.0293  68  PHE A CA  
500  C C   . PHE A 82  ? 0.2982 0.3727 0.5665 0.0246  0.0033  0.0326  68  PHE A C   
501  O O   . PHE A 82  ? 0.2023 0.2904 0.4820 0.0229  0.0019  0.0352  68  PHE A O   
502  C CB  . PHE A 82  ? 0.2262 0.2925 0.5101 0.0380  0.0072  0.0348  68  PHE A CB  
503  C CG  . PHE A 82  ? 0.3083 0.3622 0.5795 0.0364  0.0018  0.0366  68  PHE A CG  
504  C CD1 . PHE A 82  ? 0.4012 0.4399 0.6645 0.0383  0.0062  0.0324  68  PHE A CD1 
505  C CD2 . PHE A 82  ? 0.3237 0.3809 0.5905 0.0325  -0.0075 0.0421  68  PHE A CD2 
506  C CE1 . PHE A 82  ? 0.3843 0.4121 0.6372 0.0362  0.0020  0.0343  68  PHE A CE1 
507  C CE2 . PHE A 82  ? 0.3222 0.3679 0.5767 0.0307  -0.0112 0.0439  68  PHE A CE2 
508  C CZ  . PHE A 82  ? 0.2899 0.3214 0.5384 0.0326  -0.0062 0.0403  68  PHE A CZ  
509  N N   . ALA A 83  ? 0.1968 0.2621 0.4494 0.0202  -0.0014 0.0320  69  ALA A N   
510  C CA  . ALA A 83  ? 0.3361 0.4057 0.5828 0.0136  -0.0082 0.0341  69  ALA A CA  
511  C C   . ALA A 83  ? 0.3749 0.4344 0.6084 0.0116  -0.0133 0.0350  69  ALA A C   
512  O O   . ALA A 83  ? 0.3041 0.3531 0.5320 0.0141  -0.0108 0.0334  69  ALA A O   
513  C CB  . ALA A 83  ? 0.2617 0.3320 0.5013 0.0082  -0.0049 0.0301  69  ALA A CB  
514  N N   . ALA A 84  ? 0.2021 0.2647 0.4304 0.0065  -0.0200 0.0373  70  ALA A N   
515  C CA  . ALA A 84  ? 0.2330 0.2870 0.4481 0.0041  -0.0241 0.0382  70  ALA A CA  
516  C C   . ALA A 84  ? 0.3185 0.3718 0.5228 -0.0027 -0.0265 0.0357  70  ALA A C   
517  O O   . ALA A 84  ? 0.2118 0.2733 0.4205 -0.0062 -0.0290 0.0361  70  ALA A O   
518  C CB  . ALA A 84  ? 0.3441 0.4007 0.5627 0.0062  -0.0307 0.0450  70  ALA A CB  
519  N N   . LEU A 85  ? 0.2882 0.3316 0.4796 -0.0047 -0.0255 0.0332  71  LEU A N   
520  C CA  . LEU A 85  ? 0.2763 0.3166 0.4570 -0.0102 -0.0268 0.0302  71  LEU A CA  
521  C C   . LEU A 85  ? 0.2912 0.3258 0.4611 -0.0120 -0.0298 0.0317  71  LEU A C   
522  O O   . LEU A 85  ? 0.3177 0.3465 0.4853 -0.0094 -0.0281 0.0330  71  LEU A O   
523  C CB  . LEU A 85  ? 0.2500 0.2844 0.4261 -0.0104 -0.0214 0.0252  71  LEU A CB  
524  C CG  . LEU A 85  ? 0.3066 0.3349 0.4718 -0.0142 -0.0214 0.0221  71  LEU A CG  
525  C CD1 . LEU A 85  ? 0.3287 0.3600 0.4935 -0.0184 -0.0232 0.0211  71  LEU A CD1 
526  C CD2 . LEU A 85  ? 0.3157 0.3383 0.4781 -0.0127 -0.0171 0.0185  71  LEU A CD2 
527  N N   . LEU A 86  ? 0.2658 0.3014 0.4285 -0.0168 -0.0338 0.0312  72  LEU A N   
528  C CA  . LEU A 86  ? 0.2374 0.2672 0.3872 -0.0192 -0.0359 0.0319  72  LEU A CA  
529  C C   . LEU A 86  ? 0.3233 0.3472 0.4635 -0.0232 -0.0333 0.0263  72  LEU A C   
530  O O   . LEU A 86  ? 0.2849 0.3108 0.4253 -0.0265 -0.0346 0.0237  72  LEU A O   
531  C CB  . LEU A 86  ? 0.2187 0.2541 0.3666 -0.0214 -0.0436 0.0362  72  LEU A CB  
532  C CG  . LEU A 86  ? 0.3000 0.3291 0.4309 -0.0251 -0.0455 0.0362  72  LEU A CG  
533  C CD1 . LEU A 86  ? 0.3069 0.3296 0.4333 -0.0219 -0.0431 0.0402  72  LEU A CD1 
534  C CD2 . LEU A 86  ? 0.2964 0.3315 0.4230 -0.0290 -0.0542 0.0388  72  LEU A CD2 
535  N N   . THR A 87  ? 0.2865 0.3029 0.4193 -0.0227 -0.0292 0.0245  73  THR A N   
536  C CA  . THR A 87  ? 0.3343 0.3451 0.4592 -0.0255 -0.0261 0.0194  73  THR A CA  
537  C C   . THR A 87  ? 0.3188 0.3242 0.4317 -0.0272 -0.0249 0.0196  73  THR A C   
538  O O   . THR A 87  ? 0.3205 0.3258 0.4311 -0.0262 -0.0262 0.0243  73  THR A O   
539  C CB  . THR A 87  ? 0.3729 0.3812 0.5028 -0.0230 -0.0210 0.0161  73  THR A CB  
540  O OG1 . THR A 87  ? 0.3069 0.3135 0.4394 -0.0202 -0.0184 0.0177  73  THR A OG1 
541  C CG2 . THR A 87  ? 0.2410 0.2536 0.3798 -0.0218 -0.0214 0.0159  73  THR A CG2 
542  N N   . THR A 88  ? 0.2801 0.2806 0.3853 -0.0296 -0.0219 0.0148  74  THR A N   
543  C CA  . THR A 88  ? 0.2983 0.2936 0.3919 -0.0313 -0.0187 0.0141  74  THR A CA  
544  C C   . THR A 88  ? 0.3082 0.3008 0.4063 -0.0289 -0.0118 0.0124  74  THR A C   
545  O O   . THR A 88  ? 0.3081 0.3019 0.4157 -0.0266 -0.0101 0.0099  74  THR A O   
546  C CB  . THR A 88  ? 0.4173 0.4084 0.4991 -0.0355 -0.0186 0.0093  74  THR A CB  
547  O OG1 . THR A 88  ? 0.4629 0.4493 0.5312 -0.0374 -0.0154 0.0092  74  THR A OG1 
548  C CG2 . THR A 88  ? 0.3920 0.3799 0.4783 -0.0347 -0.0142 0.0033  74  THR A CG2 
549  N N   . PHE A 89  ? 0.3823 0.3717 0.4736 -0.0297 -0.0083 0.0140  75  PHE A N   
550  C CA  . PHE A 89  ? 0.3236 0.3117 0.4205 -0.0283 -0.0019 0.0130  75  PHE A CA  
551  C C   . PHE A 89  ? 0.3458 0.3338 0.4478 -0.0274 0.0020  0.0068  75  PHE A C   
552  O O   . PHE A 89  ? 0.3404 0.3256 0.4354 -0.0289 0.0036  0.0029  75  PHE A O   
553  C CB  . PHE A 89  ? 0.4157 0.3999 0.5019 -0.0307 0.0023  0.0153  75  PHE A CB  
554  C CG  . PHE A 89  ? 0.4556 0.4391 0.5486 -0.0303 0.0094  0.0146  75  PHE A CG  
555  C CD1 . PHE A 89  ? 0.3759 0.3592 0.4759 -0.0294 0.0096  0.0189  75  PHE A CD1 
556  C CD2 . PHE A 89  ? 0.3804 0.3637 0.4738 -0.0309 0.0160  0.0094  75  PHE A CD2 
557  C CE1 . PHE A 89  ? 0.3784 0.3616 0.4856 -0.0301 0.0158  0.0180  75  PHE A CE1 
558  C CE2 . PHE A 89  ? 0.3347 0.3194 0.4366 -0.0309 0.0223  0.0089  75  PHE A CE2 
559  C CZ  . PHE A 89  ? 0.4476 0.4325 0.5564 -0.0310 0.0219  0.0131  75  PHE A CZ  
560  N N   . GLY A 90  ? 0.2948 0.2855 0.4090 -0.0248 0.0032  0.0060  76  GLY A N   
561  C CA  . GLY A 90  ? 0.2882 0.2797 0.4091 -0.0232 0.0065  0.0014  76  GLY A CA  
562  C C   . GLY A 90  ? 0.2894 0.2808 0.4124 -0.0219 0.0032  -0.0008 76  GLY A C   
563  O O   . GLY A 90  ? 0.3394 0.3335 0.4704 -0.0198 0.0007  -0.0003 76  GLY A O   
564  N N   . VAL A 91  ? 0.3459 0.3334 0.4607 -0.0237 0.0033  -0.0033 77  VAL A N   
565  C CA  . VAL A 91  ? 0.3132 0.2988 0.4301 -0.0230 0.0011  -0.0054 77  VAL A CA  
566  C C   . VAL A 91  ? 0.3431 0.3318 0.4623 -0.0234 -0.0046 -0.0021 77  VAL A C   
567  O O   . VAL A 91  ? 0.3004 0.2895 0.4251 -0.0220 -0.0061 -0.0021 77  VAL A O   
568  C CB  . VAL A 91  ? 0.3665 0.3456 0.4736 -0.0255 0.0028  -0.0095 77  VAL A CB  
569  C CG1 . VAL A 91  ? 0.3297 0.3060 0.4366 -0.0241 0.0100  -0.0135 77  VAL A CG1 
570  C CG2 . VAL A 91  ? 0.2986 0.2770 0.3937 -0.0298 -0.0002 -0.0082 77  VAL A CG2 
571  N N   . GLY A 92  ? 0.3442 0.3352 0.4595 -0.0253 -0.0075 0.0012  78  GLY A N   
572  C CA  . GLY A 92  ? 0.2945 0.2897 0.4140 -0.0253 -0.0122 0.0042  78  GLY A CA  
573  C C   . GLY A 92  ? 0.3559 0.3547 0.4844 -0.0219 -0.0118 0.0062  78  GLY A C   
574  O O   . GLY A 92  ? 0.2593 0.2600 0.3930 -0.0208 -0.0128 0.0063  78  GLY A O   
575  N N   . GLU A 93  ? 0.2687 0.2678 0.3985 -0.0207 -0.0101 0.0076  79  GLU A N   
576  C CA  . GLU A 93  ? 0.2881 0.2893 0.4252 -0.0181 -0.0099 0.0087  79  GLU A CA  
577  C C   . GLU A 93  ? 0.2981 0.2996 0.4400 -0.0165 -0.0087 0.0058  79  GLU A C   
578  O O   . GLU A 93  ? 0.3563 0.3596 0.5020 -0.0149 -0.0097 0.0060  79  GLU A O   
579  C CB  . GLU A 93  ? 0.2693 0.2691 0.4066 -0.0180 -0.0081 0.0106  79  GLU A CB  
580  C CG  . GLU A 93  ? 0.2767 0.2743 0.4131 -0.0190 -0.0039 0.0084  79  GLU A CG  
581  C CD  . GLU A 93  ? 0.3322 0.3276 0.4677 -0.0200 -0.0017 0.0113  79  GLU A CD  
582  O OE1 . GLU A 93  ? 0.3182 0.3132 0.4594 -0.0188 -0.0020 0.0125  79  GLU A OE1 
583  O OE2 . GLU A 93  ? 0.2967 0.2898 0.4251 -0.0221 0.0009  0.0121  79  GLU A OE2 
584  N N   . LEU A 94  ? 0.2763 0.2762 0.4178 -0.0166 -0.0064 0.0032  80  LEU A N   
585  C CA  . LEU A 94  ? 0.2388 0.2397 0.3856 -0.0145 -0.0064 0.0013  80  LEU A CA  
586  C C   . LEU A 94  ? 0.2812 0.2813 0.4269 -0.0139 -0.0086 0.0017  80  LEU A C   
587  O O   . LEU A 94  ? 0.2173 0.2186 0.3657 -0.0122 -0.0099 0.0017  80  LEU A O   
588  C CB  . LEU A 94  ? 0.2204 0.2208 0.3696 -0.0141 -0.0034 -0.0012 80  LEU A CB  
589  C CG  . LEU A 94  ? 0.2589 0.2611 0.4117 -0.0149 -0.0004 -0.0015 80  LEU A CG  
590  C CD1 . LEU A 94  ? 0.2291 0.2333 0.3885 -0.0137 0.0027  -0.0041 80  LEU A CD1 
591  C CD2 . LEU A 94  ? 0.2537 0.2581 0.4111 -0.0147 -0.0024 -0.0006 80  LEU A CD2 
592  N N   . SER A 95  ? 0.2810 0.2788 0.4222 -0.0159 -0.0091 0.0020  81  SER A N   
593  C CA  . SER A 95  ? 0.2845 0.2811 0.4251 -0.0163 -0.0107 0.0030  81  SER A CA  
594  C C   . SER A 95  ? 0.3363 0.3370 0.4791 -0.0160 -0.0120 0.0054  81  SER A C   
595  O O   . SER A 95  ? 0.2675 0.2680 0.4106 -0.0155 -0.0124 0.0064  81  SER A O   
596  C CB  . SER A 95  ? 0.2914 0.2848 0.4274 -0.0196 -0.0112 0.0023  81  SER A CB  
597  O OG  . SER A 95  ? 0.3407 0.3288 0.4739 -0.0196 -0.0090 -0.0008 81  SER A OG  
598  N N   . ALA A 96  ? 0.2752 0.2791 0.4192 -0.0160 -0.0123 0.0065  82  ALA A N   
599  C CA  . ALA A 96  ? 0.2937 0.3014 0.4409 -0.0150 -0.0125 0.0082  82  ALA A CA  
600  C C   . ALA A 96  ? 0.3502 0.3580 0.4990 -0.0125 -0.0114 0.0070  82  ALA A C   
601  O O   . ALA A 96  ? 0.3087 0.3186 0.4594 -0.0113 -0.0105 0.0075  82  ALA A O   
602  C CB  . ALA A 96  ? 0.2669 0.2774 0.4158 -0.0155 -0.0136 0.0104  82  ALA A CB  
603  N N   . MET A 97  ? 0.2560 0.2619 0.4047 -0.0119 -0.0113 0.0050  83  MET A N   
604  C CA  . MET A 97  ? 0.2911 0.2973 0.4415 -0.0106 -0.0111 0.0031  83  MET A CA  
605  C C   . MET A 97  ? 0.2788 0.2857 0.4269 -0.0096 -0.0114 0.0028  83  MET A C   
606  O O   . MET A 97  ? 0.2830 0.2899 0.4311 -0.0088 -0.0105 0.0013  83  MET A O   
607  C CB  . MET A 97  ? 0.3080 0.3140 0.4606 -0.0106 -0.0115 0.0012  83  MET A CB  
608  C CG  . MET A 97  ? 0.4341 0.4409 0.5896 -0.0105 -0.0119 -0.0012 83  MET A CG  
609  S SD  . MET A 97  ? 0.7631 0.7713 0.9249 -0.0117 -0.0110 -0.0028 83  MET A SD  
610  C CE  . MET A 97  ? 0.4101 0.4152 0.5715 -0.0133 -0.0078 -0.0011 83  MET A CE  
611  N N   . ASN A 98  ? 0.3030 0.3093 0.4481 -0.0096 -0.0122 0.0040  84  ASN A N   
612  C CA  . ASN A 98  ? 0.2639 0.2703 0.4046 -0.0090 -0.0121 0.0043  84  ASN A CA  
613  C C   . ASN A 98  ? 0.2822 0.2905 0.4230 -0.0092 -0.0092 0.0052  84  ASN A C   
614  O O   . ASN A 98  ? 0.2760 0.2844 0.4131 -0.0084 -0.0076 0.0041  84  ASN A O   
615  C CB  . ASN A 98  ? 0.2511 0.2553 0.3885 -0.0091 -0.0134 0.0067  84  ASN A CB  
616  C CG  . ASN A 98  ? 0.3351 0.3386 0.4656 -0.0088 -0.0132 0.0080  84  ASN A CG  
617  O OD1 . ASN A 98  ? 0.3126 0.3167 0.4394 -0.0079 -0.0144 0.0061  84  ASN A OD1 
618  N ND2 . ASN A 98  ? 0.2148 0.2170 0.3430 -0.0101 -0.0114 0.0112  84  ASN A ND2 
619  N N   . GLY A 99  ? 0.2062 0.2164 0.3512 -0.0102 -0.0084 0.0071  85  GLY A N   
620  C CA  . GLY A 99  ? 0.2333 0.2473 0.3818 -0.0099 -0.0058 0.0082  85  GLY A CA  
621  C C   . GLY A 99  ? 0.2738 0.2879 0.4253 -0.0075 -0.0043 0.0063  85  GLY A C   
622  O O   . GLY A 99  ? 0.3207 0.3360 0.4726 -0.0060 -0.0011 0.0051  85  GLY A O   
623  N N   . ILE A 100 ? 0.2869 0.2991 0.4405 -0.0073 -0.0061 0.0057  86  ILE A N   
624  C CA  . ILE A 100 ? 0.3231 0.3333 0.4797 -0.0054 -0.0046 0.0042  86  ILE A CA  
625  C C   . ILE A 100 ? 0.2957 0.3028 0.4479 -0.0048 -0.0033 -0.0001 86  ILE A C   
626  O O   . ILE A 100 ? 0.2761 0.2813 0.4295 -0.0030 -0.0005 -0.0023 86  ILE A O   
627  C CB  . ILE A 100 ? 0.2448 0.2527 0.4032 -0.0061 -0.0063 0.0051  86  ILE A CB  
628  C CG1 . ILE A 100 ? 0.2559 0.2667 0.4165 -0.0068 -0.0080 0.0092  86  ILE A CG1 
629  C CG2 . ILE A 100 ? 0.2619 0.2656 0.4233 -0.0045 -0.0046 0.0037  86  ILE A CG2 
630  C CD1 . ILE A 100 ? 0.2714 0.2861 0.4383 -0.0047 -0.0074 0.0118  86  ILE A CD1 
631  N N   . ALA A 101 ? 0.1925 0.1987 0.3397 -0.0063 -0.0057 -0.0015 87  ALA A N   
632  C CA  . ALA A 101 ? 0.2737 0.2776 0.4154 -0.0063 -0.0060 -0.0056 87  ALA A CA  
633  C C   . ALA A 101 ? 0.2053 0.2094 0.3415 -0.0053 -0.0027 -0.0063 87  ALA A C   
634  O O   . ALA A 101 ? 0.3000 0.3013 0.4324 -0.0048 -0.0007 -0.0105 87  ALA A O   
635  C CB  . ALA A 101 ? 0.2162 0.2206 0.3548 -0.0076 -0.0102 -0.0058 87  ALA A CB  
636  N N   . GLY A 102 ? 0.2168 0.2240 0.3521 -0.0056 -0.0016 -0.0027 88  GLY A N   
637  C CA  . GLY A 102 ? 0.2165 0.2248 0.3474 -0.0049 0.0029  -0.0029 88  GLY A CA  
638  C C   . GLY A 102 ? 0.2485 0.2579 0.3861 -0.0026 0.0078  -0.0044 88  GLY A C   
639  O O   . GLY A 102 ? 0.2635 0.2715 0.3967 -0.0013 0.0124  -0.0076 88  GLY A O   
640  N N   . SER A 103 ? 0.2301 0.2416 0.3779 -0.0016 0.0070  -0.0020 89  SER A N   
641  C CA  . SER A 103 ? 0.2361 0.2486 0.3923 0.0016  0.0109  -0.0026 89  SER A CA  
642  C C   . SER A 103 ? 0.3025 0.3078 0.4560 0.0031  0.0124  -0.0080 89  SER A C   
643  O O   . SER A 103 ? 0.2563 0.2600 0.4115 0.0059  0.0177  -0.0109 89  SER A O   
644  C CB  . SER A 103 ? 0.2387 0.2545 0.4049 0.0021  0.0080  0.0019  89  SER A CB  
645  O OG  . SER A 103 ? 0.2848 0.3072 0.4536 0.0000  0.0066  0.0059  89  SER A OG  
646  N N   . TYR A 104 ? 0.2954 0.2961 0.4454 0.0010  0.0082  -0.0097 90  TYR A N   
647  C CA  . TYR A 104 ? 0.3290 0.3223 0.4763 0.0012  0.0092  -0.0153 90  TYR A CA  
648  C C   . TYR A 104 ? 0.3237 0.3147 0.4600 0.0005  0.0115  -0.0207 90  TYR A C   
649  O O   . TYR A 104 ? 0.3197 0.3055 0.4543 0.0022  0.0160  -0.0258 90  TYR A O   
650  C CB  . TYR A 104 ? 0.2677 0.2585 0.4152 -0.0018 0.0042  -0.0158 90  TYR A CB  
651  C CG  . TYR A 104 ? 0.2484 0.2315 0.3950 -0.0028 0.0047  -0.0215 90  TYR A CG  
652  C CD1 . TYR A 104 ? 0.2911 0.2718 0.4289 -0.0053 0.0031  -0.0274 90  TYR A CD1 
653  C CD2 . TYR A 104 ? 0.3221 0.2996 0.4764 -0.0017 0.0065  -0.0210 90  TYR A CD2 
654  C CE1 . TYR A 104 ? 0.2970 0.2703 0.4341 -0.0072 0.0032  -0.0334 90  TYR A CE1 
655  C CE2 . TYR A 104 ? 0.3226 0.2915 0.4765 -0.0033 0.0073  -0.0265 90  TYR A CE2 
656  C CZ  . TYR A 104 ? 0.3528 0.3198 0.4984 -0.0064 0.0056  -0.0332 90  TYR A CZ  
657  O OH  . TYR A 104 ? 0.4127 0.3709 0.5578 -0.0090 0.0059  -0.0394 90  TYR A OH  
658  N N   . ALA A 105 ? 0.2883 0.2825 0.4161 -0.0016 0.0088  -0.0195 91  ALA A N   
659  C CA  . ALA A 105 ? 0.2850 0.2768 0.3993 -0.0027 0.0099  -0.0238 91  ALA A CA  
660  C C   . ALA A 105 ? 0.3398 0.3315 0.4518 -0.0003 0.0181  -0.0255 91  ALA A C   
661  O O   . ALA A 105 ? 0.2985 0.2853 0.4007 -0.0003 0.0214  -0.0317 91  ALA A O   
662  C CB  . ALA A 105 ? 0.2853 0.2806 0.3920 -0.0048 0.0054  -0.0201 91  ALA A CB  
663  N N   . GLU A 106 ? 0.2961 0.2939 0.4173 0.0016  0.0215  -0.0205 92  GLU A N   
664  C CA  . GLU A 106 ? 0.4109 0.4111 0.5326 0.0040  0.0300  -0.0212 92  GLU A CA  
665  C C   . GLU A 106 ? 0.3305 0.3314 0.4671 0.0083  0.0346  -0.0218 92  GLU A C   
666  O O   . GLU A 106 ? 0.3066 0.3122 0.4491 0.0110  0.0416  -0.0212 92  GLU A O   
667  C CB  . GLU A 106 ? 0.3308 0.3385 0.4531 0.0024  0.0310  -0.0150 92  GLU A CB  
668  C CG  . GLU A 106 ? 0.3171 0.3233 0.4267 -0.0013 0.0255  -0.0128 92  GLU A CG  
669  C CD  . GLU A 106 ? 0.3760 0.3839 0.4755 -0.0028 0.0303  -0.0104 92  GLU A CD  
670  O OE1 . GLU A 106 ? 0.4094 0.4225 0.5158 -0.0019 0.0376  -0.0088 92  GLU A OE1 
671  O OE2 . GLU A 106 ? 0.3517 0.3561 0.4368 -0.0051 0.0268  -0.0096 92  GLU A OE2 
672  N N   . HIS A 107 ? 0.3334 0.3299 0.4767 0.0093  0.0308  -0.0224 93  HIS A N   
673  C CA  . HIS A 107 ? 0.3397 0.3343 0.4960 0.0139  0.0345  -0.0227 93  HIS A CA  
674  C C   . HIS A 107 ? 0.3788 0.3838 0.5498 0.0167  0.0357  -0.0159 93  HIS A C   
675  O O   . HIS A 107 ? 0.3148 0.3233 0.4943 0.0208  0.0425  -0.0163 93  HIS A O   
676  C CB  . HIS A 107 ? 0.3011 0.2888 0.4532 0.0168  0.0425  -0.0304 93  HIS A CB  
677  C CG  . HIS A 107 ? 0.4749 0.4517 0.6135 0.0137  0.0406  -0.0379 93  HIS A CG  
678  N ND1 . HIS A 107 ? 0.3887 0.3549 0.5299 0.0154  0.0425  -0.0434 93  HIS A ND1 
679  C CD2 . HIS A 107 ? 0.3743 0.3495 0.4975 0.0089  0.0364  -0.0408 93  HIS A CD2 
680  C CE1 . HIS A 107 ? 0.4732 0.4321 0.6011 0.0109  0.0395  -0.0499 93  HIS A CE1 
681  N NE2 . HIS A 107 ? 0.4502 0.4150 0.5671 0.0072  0.0354  -0.0483 93  HIS A NE2 
682  N N   . VAL A 108 ? 0.2872 0.2973 0.4617 0.0142  0.0291  -0.0099 94  VAL A N   
683  C CA  . VAL A 108 ? 0.3089 0.3292 0.4968 0.0155  0.0281  -0.0035 94  VAL A CA  
684  C C   . VAL A 108 ? 0.2616 0.2803 0.4567 0.0165  0.0222  0.0005  94  VAL A C   
685  O O   . VAL A 108 ? 0.2308 0.2454 0.4191 0.0131  0.0169  0.0011  94  VAL A O   
686  C CB  . VAL A 108 ? 0.3229 0.3503 0.5073 0.0110  0.0256  0.0001  94  VAL A CB  
687  C CG1 . VAL A 108 ? 0.2068 0.2454 0.4059 0.0117  0.0250  0.0057  94  VAL A CG1 
688  C CG2 . VAL A 108 ? 0.2914 0.3182 0.4652 0.0094  0.0311  -0.0031 94  VAL A CG2 
689  N N   . PRO A 109 ? 0.3175 0.3393 0.5263 0.0212  0.0232  0.0037  95  PRO A N   
690  C CA  . PRO A 109 ? 0.2785 0.2975 0.4921 0.0223  0.0177  0.0083  95  PRO A CA  
691  C C   . PRO A 109 ? 0.2592 0.2863 0.4746 0.0190  0.0107  0.0144  95  PRO A C   
692  O O   . PRO A 109 ? 0.2676 0.3037 0.4947 0.0212  0.0088  0.0194  95  PRO A O   
693  C CB  . PRO A 109 ? 0.2825 0.3020 0.5105 0.0293  0.0214  0.0098  95  PRO A CB  
694  C CG  . PRO A 109 ? 0.3204 0.3496 0.5555 0.0313  0.0275  0.0084  95  PRO A CG  
695  C CD  . PRO A 109 ? 0.2768 0.3044 0.4972 0.0263  0.0301  0.0032  95  PRO A CD  
696  N N   . VAL A 110 ? 0.2621 0.2862 0.4664 0.0139  0.0067  0.0139  96  VAL A N   
697  C CA  . VAL A 110 ? 0.2914 0.3207 0.4947 0.0103  0.0005  0.0184  96  VAL A CA  
698  C C   . VAL A 110 ? 0.3129 0.3352 0.5119 0.0097  -0.0033 0.0206  96  VAL A C   
699  O O   . VAL A 110 ? 0.3080 0.3220 0.4998 0.0084  -0.0021 0.0173  96  VAL A O   
700  C CB  . VAL A 110 ? 0.3032 0.3339 0.4977 0.0053  -0.0002 0.0164  96  VAL A CB  
701  C CG1 . VAL A 110 ? 0.2706 0.3039 0.4626 0.0014  -0.0061 0.0197  96  VAL A CG1 
702  C CG2 . VAL A 110 ? 0.2479 0.2856 0.4465 0.0052  0.0039  0.0156  96  VAL A CG2 
703  N N   . LEU A 111 ? 0.3214 0.3475 0.5250 0.0104  -0.0080 0.0264  97  LEU A N   
704  C CA  . LEU A 111 ? 0.2781 0.2976 0.4761 0.0094  -0.0112 0.0296  97  LEU A CA  
705  C C   . LEU A 111 ? 0.3815 0.4021 0.5694 0.0038  -0.0149 0.0296  97  LEU A C   
706  O O   . LEU A 111 ? 0.3035 0.3316 0.4922 0.0016  -0.0185 0.0314  97  LEU A O   
707  C CB  . LEU A 111 ? 0.2979 0.3200 0.5041 0.0133  -0.0148 0.0366  97  LEU A CB  
708  C CG  . LEU A 111 ? 0.3352 0.3514 0.5333 0.0115  -0.0189 0.0414  97  LEU A CG  
709  C CD1 . LEU A 111 ? 0.2753 0.2788 0.4700 0.0124  -0.0149 0.0402  97  LEU A CD1 
710  C CD2 . LEU A 111 ? 0.4226 0.4445 0.6271 0.0144  -0.0249 0.0495  97  LEU A CD2 
711  N N   . HIS A 112 ? 0.3576 0.3706 0.5368 0.0013  -0.0137 0.0272  98  HIS A N   
712  C CA  . HIS A 112 ? 0.2643 0.2770 0.4342 -0.0034 -0.0157 0.0264  98  HIS A CA  
713  C C   . HIS A 112 ? 0.2916 0.3008 0.4563 -0.0043 -0.0183 0.0312  98  HIS A C   
714  O O   . HIS A 112 ? 0.2557 0.2577 0.4186 -0.0038 -0.0159 0.0318  98  HIS A O   
715  C CB  . HIS A 112 ? 0.3038 0.3119 0.4688 -0.0053 -0.0125 0.0210  98  HIS A CB  
716  C CG  . HIS A 112 ? 0.2300 0.2385 0.3878 -0.0091 -0.0137 0.0194  98  HIS A CG  
717  N ND1 . HIS A 112 ? 0.2685 0.2746 0.4235 -0.0105 -0.0116 0.0153  98  HIS A ND1 
718  C CD2 . HIS A 112 ? 0.2956 0.3065 0.4489 -0.0117 -0.0166 0.0211  98  HIS A CD2 
719  C CE1 . HIS A 112 ? 0.2655 0.2719 0.4152 -0.0130 -0.0125 0.0146  98  HIS A CE1 
720  N NE2 . HIS A 112 ? 0.2869 0.2956 0.4346 -0.0141 -0.0154 0.0176  98  HIS A NE2 
721  N N   . ILE A 113 ? 0.2457 0.2596 0.4072 -0.0061 -0.0231 0.0346  99  ILE A N   
722  C CA  . ILE A 113 ? 0.2581 0.2686 0.4109 -0.0079 -0.0258 0.0391  99  ILE A CA  
723  C C   . ILE A 113 ? 0.3458 0.3540 0.4870 -0.0128 -0.0249 0.0353  99  ILE A C   
724  O O   . ILE A 113 ? 0.3246 0.3368 0.4643 -0.0153 -0.0265 0.0322  99  ILE A O   
725  C CB  . ILE A 113 ? 0.2958 0.3129 0.4509 -0.0069 -0.0326 0.0452  99  ILE A CB  
726  C CG1 . ILE A 113 ? 0.3272 0.3485 0.4974 -0.0011 -0.0329 0.0482  99  ILE A CG1 
727  C CG2 . ILE A 113 ? 0.2482 0.2604 0.3923 -0.0083 -0.0356 0.0509  99  ILE A CG2 
728  C CD1 . ILE A 113 ? 0.3051 0.3370 0.4824 -0.0001 -0.0399 0.0532  99  ILE A CD1 
729  N N   . VAL A 114 ? 0.3151 0.3165 0.4489 -0.0143 -0.0216 0.0355  100 VAL A N   
730  C CA  . VAL A 114 ? 0.2803 0.2792 0.4040 -0.0183 -0.0193 0.0317  100 VAL A CA  
731  C C   . VAL A 114 ? 0.3500 0.3458 0.4612 -0.0208 -0.0210 0.0361  100 VAL A C   
732  O O   . VAL A 114 ? 0.3486 0.3394 0.4574 -0.0202 -0.0191 0.0405  100 VAL A O   
733  C CB  . VAL A 114 ? 0.3625 0.3575 0.4889 -0.0184 -0.0131 0.0275  100 VAL A CB  
734  C CG1 . VAL A 114 ? 0.3162 0.3092 0.4341 -0.0217 -0.0098 0.0239  100 VAL A CG1 
735  C CG2 . VAL A 114 ? 0.2391 0.2369 0.3754 -0.0161 -0.0124 0.0235  100 VAL A CG2 
736  N N   . GLY A 115 ? 0.2968 0.2948 0.3989 -0.0240 -0.0245 0.0350  101 GLY A N   
737  C CA  . GLY A 115 ? 0.3889 0.3832 0.4752 -0.0272 -0.0258 0.0380  101 GLY A CA  
738  C C   . GLY A 115 ? 0.4227 0.4111 0.5007 -0.0297 -0.0180 0.0337  101 GLY A C   
739  O O   . GLY A 115 ? 0.3506 0.3391 0.4301 -0.0306 -0.0146 0.0270  101 GLY A O   
740  N N   . ALA A 116 ? 0.3178 0.3009 0.3876 -0.0306 -0.0149 0.0381  102 ALA A N   
741  C CA  . ALA A 116 ? 0.3771 0.3556 0.4427 -0.0326 -0.0060 0.0351  102 ALA A CA  
742  C C   . ALA A 116 ? 0.4113 0.3849 0.4570 -0.0365 -0.0043 0.0376  102 ALA A C   
743  O O   . ALA A 116 ? 0.3875 0.3605 0.4231 -0.0372 -0.0106 0.0437  102 ALA A O   
744  C CB  . ALA A 116 ? 0.3493 0.3254 0.4259 -0.0306 -0.0017 0.0378  102 ALA A CB  
745  N N   . PRO A 117 ? 0.4247 0.3952 0.4642 -0.0389 0.0043  0.0332  103 PRO A N   
746  C CA  . PRO A 117 ? 0.4385 0.4037 0.4574 -0.0429 0.0078  0.0355  103 PRO A CA  
747  C C   . PRO A 117 ? 0.4116 0.3725 0.4258 -0.0431 0.0075  0.0456  103 PRO A C   
748  O O   . PRO A 117 ? 0.4135 0.3743 0.4420 -0.0404 0.0077  0.0493  103 PRO A O   
749  C CB  . PRO A 117 ? 0.4066 0.3703 0.4263 -0.0443 0.0192  0.0288  103 PRO A CB  
750  C CG  . PRO A 117 ? 0.4854 0.4542 0.5238 -0.0412 0.0193  0.0223  103 PRO A CG  
751  C CD  . PRO A 117 ? 0.5089 0.4814 0.5600 -0.0380 0.0110  0.0256  103 PRO A CD  
752  N N   . GLY A 118 ? 0.4518 0.4080 0.4443 -0.0465 0.0070  0.0500  104 GLY A N   
753  C CA  . GLY A 118 ? 0.4711 0.4218 0.4564 -0.0468 0.0063  0.0608  104 GLY A CA  
754  C C   . GLY A 118 ? 0.5276 0.4743 0.5213 -0.0474 0.0169  0.0624  104 GLY A C   
755  O O   . GLY A 118 ? 0.4135 0.3614 0.4117 -0.0490 0.0262  0.0553  104 GLY A O   
756  N N   . THR A 119 ? 0.4840 0.4258 0.4813 -0.0460 0.0152  0.0719  105 THR A N   
757  C CA  . THR A 119 ? 0.5730 0.5104 0.5804 -0.0472 0.0245  0.0738  105 THR A CA  
758  C C   . THR A 119 ? 0.4879 0.4218 0.4814 -0.0526 0.0359  0.0730  105 THR A C   
759  O O   . THR A 119 ? 0.4927 0.4280 0.4981 -0.0544 0.0454  0.0686  105 THR A O   
760  C CB  . THR A 119 ? 0.6266 0.5567 0.6371 -0.0452 0.0208  0.0850  105 THR A CB  
761  O OG1 . THR A 119 ? 0.7654 0.6884 0.7533 -0.0476 0.0199  0.0947  105 THR A OG1 
762  C CG2 . THR A 119 ? 0.4893 0.4233 0.5122 -0.0392 0.0099  0.0861  105 THR A CG2 
763  N N   . ALA A 120 ? 0.5814 0.5112 0.5498 -0.0555 0.0353  0.0770  106 ALA A N   
764  C CA  . ALA A 120 ? 0.5584 0.4846 0.5111 -0.0608 0.0473  0.0759  106 ALA A CA  
765  C C   . ALA A 120 ? 0.7071 0.6401 0.6683 -0.0613 0.0551  0.0631  106 ALA A C   
766  O O   . ALA A 120 ? 0.6756 0.6093 0.6429 -0.0638 0.0672  0.0604  106 ALA A O   
767  C CB  . ALA A 120 ? 0.5360 0.4569 0.4575 -0.0637 0.0439  0.0811  106 ALA A CB  
768  N N   . SER A 121 ? 0.5804 0.5189 0.5438 -0.0587 0.0482  0.0554  107 SER A N   
769  C CA  . SER A 121 ? 0.5806 0.5245 0.5532 -0.0582 0.0547  0.0438  107 SER A CA  
770  C C   . SER A 121 ? 0.5287 0.4782 0.5291 -0.0560 0.0591  0.0408  107 SER A C   
771  O O   . SER A 121 ? 0.4807 0.4338 0.4894 -0.0568 0.0691  0.0346  107 SER A O   
772  C CB  . SER A 121 ? 0.4585 0.4058 0.4301 -0.0559 0.0453  0.0373  107 SER A CB  
773  O OG  . SER A 121 ? 0.7217 0.6651 0.6691 -0.0592 0.0463  0.0339  107 SER A OG  
774  N N   . GLN A 122 ? 0.4609 0.4115 0.4763 -0.0532 0.0517  0.0449  108 GLN A N   
775  C CA  . GLN A 122 ? 0.5034 0.4589 0.5437 -0.0516 0.0544  0.0418  108 GLN A CA  
776  C C   . GLN A 122 ? 0.6109 0.5644 0.6555 -0.0557 0.0654  0.0448  108 GLN A C   
777  O O   . GLN A 122 ? 0.5044 0.4641 0.5650 -0.0563 0.0723  0.0391  108 GLN A O   
778  C CB  . GLN A 122 ? 0.4263 0.3817 0.4784 -0.0481 0.0446  0.0453  108 GLN A CB  
779  C CG  . GLN A 122 ? 0.4635 0.4225 0.5149 -0.0444 0.0344  0.0423  108 GLN A CG  
780  C CD  . GLN A 122 ? 0.4212 0.3822 0.4891 -0.0405 0.0275  0.0430  108 GLN A CD  
781  O OE1 . GLN A 122 ? 0.4765 0.4383 0.5595 -0.0402 0.0305  0.0417  108 GLN A OE1 
782  N NE2 . GLN A 122 ? 0.4424 0.4046 0.5075 -0.0377 0.0184  0.0448  108 GLN A NE2 
783  N N   . GLN A 123 ? 0.4991 0.4443 0.5304 -0.0587 0.0672  0.0542  109 GLN A N   
784  C CA  . GLN A 123 ? 0.5657 0.5080 0.6022 -0.0632 0.0776  0.0582  109 GLN A CA  
785  C C   . GLN A 123 ? 0.4950 0.4411 0.5275 -0.0668 0.0906  0.0532  109 GLN A C   
786  O O   . GLN A 123 ? 0.6217 0.5711 0.6687 -0.0699 0.1000  0.0523  109 GLN A O   
787  C CB  . GLN A 123 ? 0.5153 0.4461 0.5362 -0.0655 0.0764  0.0705  109 GLN A CB  
788  C CG  . GLN A 123 ? 0.5456 0.4725 0.5726 -0.0611 0.0644  0.0757  109 GLN A CG  
789  C CD  . GLN A 123 ? 0.7832 0.6983 0.7961 -0.0623 0.0625  0.0887  109 GLN A CD  
790  O OE1 . GLN A 123 ? 0.7695 0.6797 0.7590 -0.0648 0.0644  0.0944  109 GLN A OE1 
791  N NE2 . GLN A 123 ? 0.7129 0.6224 0.7391 -0.0603 0.0586  0.0935  109 GLN A NE2 
792  N N   . ARG A 124 ? 0.5492 0.4952 0.5632 -0.0665 0.0917  0.0494  110 ARG A N   
793  C CA  . ARG A 124 ? 0.5129 0.4625 0.5236 -0.0689 0.1048  0.0431  110 ARG A CA  
794  C C   . ARG A 124 ? 0.4729 0.4333 0.5059 -0.0652 0.1064  0.0323  110 ARG A C   
795  O O   . ARG A 124 ? 0.5277 0.4923 0.5627 -0.0661 0.1178  0.0264  110 ARG A O   
796  C CB  . ARG A 124 ? 0.6118 0.5555 0.5918 -0.0704 0.1061  0.0425  110 ARG A CB  
797  C CG  . ARG A 124 ? 0.6454 0.5793 0.6017 -0.0723 0.0988  0.0532  110 ARG A CG  
798  C CD  . ARG A 124 ? 0.6701 0.5978 0.5935 -0.0755 0.1020  0.0529  110 ARG A CD  
799  N NE  . ARG A 124 ? 0.9857 0.9151 0.9017 -0.0727 0.0926  0.0455  110 ARG A NE  
800  C CZ  . ARG A 124 ? 0.9821 0.9068 0.8770 -0.0731 0.0813  0.0495  110 ARG A CZ  
801  N NH1 . ARG A 124 ? 0.9708 0.8894 0.8522 -0.0748 0.0758  0.0617  110 ARG A NH1 
802  N NH2 . ARG A 124 ? 0.8199 0.7463 0.7090 -0.0718 0.0744  0.0415  110 ARG A NH2 
803  N N   . GLY A 125 ? 0.4357 0.4003 0.4848 -0.0608 0.0957  0.0297  111 GLY A N   
804  C CA  . GLY A 125 ? 0.4805 0.4547 0.5499 -0.0571 0.0962  0.0206  111 GLY A CA  
805  C C   . GLY A 125 ? 0.5119 0.4862 0.5705 -0.0551 0.0994  0.0130  111 GLY A C   
806  O O   . GLY A 125 ? 0.4165 0.3972 0.4875 -0.0536 0.1076  0.0064  111 GLY A O   
807  N N   . GLU A 126 ? 0.4912 0.4583 0.5275 -0.0551 0.0931  0.0138  112 GLU A N   
808  C CA  . GLU A 126 ? 0.4675 0.4325 0.4910 -0.0541 0.0960  0.0060  112 GLU A CA  
809  C C   . GLU A 126 ? 0.4758 0.4463 0.5174 -0.0488 0.0913  -0.0015 112 GLU A C   
810  O O   . GLU A 126 ? 0.4131 0.3874 0.4696 -0.0461 0.0820  0.0003  112 GLU A O   
811  C CB  . GLU A 126 ? 0.4391 0.3955 0.4347 -0.0562 0.0885  0.0087  112 GLU A CB  
812  C CG  . GLU A 126 ? 0.5622 0.5121 0.5372 -0.0612 0.0915  0.0175  112 GLU A CG  
813  C CD  . GLU A 126 ? 0.6948 0.6372 0.6402 -0.0636 0.0847  0.0192  112 GLU A CD  
814  O OE1 . GLU A 126 ? 0.7248 0.6677 0.6703 -0.0616 0.0721  0.0186  112 GLU A OE1 
815  O OE2 . GLU A 126 ? 0.7856 0.7220 0.7075 -0.0679 0.0919  0.0211  112 GLU A OE2 
816  N N   . LEU A 127 ? 0.4462 0.4161 0.4855 -0.0472 0.0984  -0.0098 113 LEU A N   
817  C CA  . LEU A 127 ? 0.4531 0.4262 0.5073 -0.0420 0.0947  -0.0166 113 LEU A CA  
818  C C   . LEU A 127 ? 0.5085 0.4746 0.5469 -0.0421 0.0844  -0.0182 113 LEU A C   
819  O O   . LEU A 127 ? 0.5315 0.4914 0.5569 -0.0423 0.0872  -0.0248 113 LEU A O   
820  C CB  . LEU A 127 ? 0.4404 0.4153 0.5010 -0.0397 0.1074  -0.0247 113 LEU A CB  
821  C CG  . LEU A 127 ? 0.3991 0.3823 0.4755 -0.0403 0.1194  -0.0238 113 LEU A CG  
822  C CD1 . LEU A 127 ? 0.5247 0.5104 0.6100 -0.0366 0.1314  -0.0324 113 LEU A CD1 
823  C CD2 . LEU A 127 ? 0.5079 0.5009 0.6100 -0.0388 0.1133  -0.0194 113 LEU A CD2 
824  N N   . LEU A 128 ? 0.4058 0.3728 0.4464 -0.0421 0.0726  -0.0123 114 LEU A N   
825  C CA  . LEU A 128 ? 0.4628 0.4252 0.4910 -0.0428 0.0620  -0.0124 114 LEU A CA  
826  C C   . LEU A 128 ? 0.4213 0.3862 0.4649 -0.0386 0.0563  -0.0166 114 LEU A C   
827  O O   . LEU A 128 ? 0.4173 0.3884 0.4817 -0.0349 0.0569  -0.0167 114 LEU A O   
828  C CB  . LEU A 128 ? 0.3354 0.2982 0.3588 -0.0446 0.0528  -0.0033 114 LEU A CB  
829  C CG  . LEU A 128 ? 0.4707 0.4296 0.4769 -0.0487 0.0561  0.0032  114 LEU A CG  
830  C CD1 . LEU A 128 ? 0.3782 0.3371 0.3822 -0.0491 0.0453  0.0123  114 LEU A CD1 
831  C CD2 . LEU A 128 ? 0.4127 0.3646 0.3932 -0.0525 0.0604  -0.0005 114 LEU A CD2 
832  N N   . HIS A 129 ? 0.3901 0.3498 0.4227 -0.0398 0.0502  -0.0197 115 HIS A N   
833  C CA  . HIS A 129 ? 0.3881 0.3490 0.4335 -0.0366 0.0442  -0.0223 115 HIS A CA  
834  C C   . HIS A 129 ? 0.3783 0.3458 0.4370 -0.0349 0.0359  -0.0157 115 HIS A C   
835  O O   . HIS A 129 ? 0.4004 0.3695 0.4545 -0.0367 0.0322  -0.0094 115 HIS A O   
836  C CB  . HIS A 129 ? 0.3771 0.3309 0.4078 -0.0395 0.0391  -0.0265 115 HIS A CB  
837  C CG  . HIS A 129 ? 0.5471 0.5009 0.5639 -0.0438 0.0302  -0.0213 115 HIS A CG  
838  N ND1 . HIS A 129 ? 0.4417 0.3922 0.4383 -0.0479 0.0318  -0.0195 115 HIS A ND1 
839  C CD2 . HIS A 129 ? 0.4904 0.4478 0.5113 -0.0443 0.0196  -0.0171 115 HIS A CD2 
840  C CE1 . HIS A 129 ? 0.5216 0.4739 0.5111 -0.0505 0.0216  -0.0141 115 HIS A CE1 
841  N NE2 . HIS A 129 ? 0.4954 0.4523 0.5004 -0.0483 0.0144  -0.0127 115 HIS A NE2 
842  N N   . HIS A 130 ? 0.3200 0.2906 0.3949 -0.0310 0.0334  -0.0171 116 HIS A N   
843  C CA  . HIS A 130 ? 0.3231 0.2996 0.4113 -0.0289 0.0269  -0.0124 116 HIS A CA  
844  C C   . HIS A 130 ? 0.4054 0.3874 0.5047 -0.0278 0.0305  -0.0093 116 HIS A C   
845  O O   . HIS A 130 ? 0.3688 0.3542 0.4747 -0.0273 0.0256  -0.0049 116 HIS A O   
846  C CB  . HIS A 130 ? 0.3022 0.2787 0.3832 -0.0311 0.0184  -0.0076 116 HIS A CB  
847  C CG  . HIS A 130 ? 0.3984 0.3709 0.4699 -0.0334 0.0139  -0.0104 116 HIS A CG  
848  N ND1 . HIS A 130 ? 0.3741 0.3419 0.4457 -0.0328 0.0164  -0.0166 116 HIS A ND1 
849  C CD2 . HIS A 130 ? 0.3878 0.3602 0.4504 -0.0364 0.0067  -0.0077 116 HIS A CD2 
850  C CE1 . HIS A 130 ? 0.4623 0.4265 0.5248 -0.0361 0.0112  -0.0180 116 HIS A CE1 
851  N NE2 . HIS A 130 ? 0.4640 0.4319 0.5214 -0.0385 0.0050  -0.0128 116 HIS A NE2 
852  N N   . THR A 131 ? 0.3976 0.3805 0.4997 -0.0277 0.0393  -0.0118 117 THR A N   
853  C CA  . THR A 131 ? 0.3557 0.3450 0.4719 -0.0272 0.0430  -0.0099 117 THR A CA  
854  C C   . THR A 131 ? 0.4093 0.4035 0.5415 -0.0234 0.0473  -0.0145 117 THR A C   
855  O O   . THR A 131 ? 0.3384 0.3296 0.4692 -0.0211 0.0490  -0.0191 117 THR A O   
856  C CB  . THR A 131 ? 0.3721 0.3599 0.4800 -0.0310 0.0504  -0.0074 117 THR A CB  
857  O OG1 . THR A 131 ? 0.3405 0.3268 0.4439 -0.0312 0.0599  -0.0124 117 THR A OG1 
858  C CG2 . THR A 131 ? 0.4007 0.3826 0.4903 -0.0342 0.0459  -0.0024 117 THR A CG2 
859  N N   . LEU A 132 ? 0.3436 0.3453 0.4917 -0.0229 0.0489  -0.0132 118 LEU A N   
860  C CA  . LEU A 132 ? 0.3482 0.3570 0.5144 -0.0192 0.0522  -0.0167 118 LEU A CA  
861  C C   . LEU A 132 ? 0.3704 0.3808 0.5383 -0.0197 0.0640  -0.0199 118 LEU A C   
862  O O   . LEU A 132 ? 0.3195 0.3377 0.5054 -0.0165 0.0679  -0.0225 118 LEU A O   
863  C CB  . LEU A 132 ? 0.3786 0.3961 0.5620 -0.0191 0.0479  -0.0145 118 LEU A CB  
864  C CG  . LEU A 132 ? 0.3009 0.3169 0.4825 -0.0186 0.0375  -0.0118 118 LEU A CG  
865  C CD1 . LEU A 132 ? 0.2598 0.2837 0.4571 -0.0191 0.0340  -0.0110 118 LEU A CD1 
866  C CD2 . LEU A 132 ? 0.3615 0.3747 0.5411 -0.0146 0.0323  -0.0135 118 LEU A CD2 
867  N N   . GLY A 133 ? 0.3229 0.3267 0.4729 -0.0234 0.0698  -0.0197 119 GLY A N   
868  C CA  . GLY A 133 ? 0.3185 0.3230 0.4673 -0.0242 0.0824  -0.0230 119 GLY A CA  
869  C C   . GLY A 133 ? 0.3759 0.3883 0.5365 -0.0272 0.0893  -0.0203 119 GLY A C   
870  O O   . GLY A 133 ? 0.3304 0.3463 0.4959 -0.0273 0.1009  -0.0234 119 GLY A O   
871  N N   . ASP A 134 ? 0.3367 0.3517 0.5027 -0.0299 0.0833  -0.0151 120 ASP A N   
872  C CA  . ASP A 134 ? 0.3107 0.3325 0.4893 -0.0337 0.0889  -0.0123 120 ASP A CA  
873  C C   . ASP A 134 ? 0.4537 0.4680 0.6160 -0.0396 0.0904  -0.0062 120 ASP A C   
874  O O   . ASP A 134 ? 0.3267 0.3445 0.4979 -0.0437 0.0951  -0.0032 120 ASP A O   
875  C CB  . ASP A 134 ? 0.2751 0.3057 0.4755 -0.0325 0.0809  -0.0117 120 ASP A CB  
876  C CG  . ASP A 134 ? 0.4260 0.4511 0.6190 -0.0318 0.0685  -0.0090 120 ASP A CG  
877  O OD1 . ASP A 134 ? 0.3193 0.3348 0.4924 -0.0326 0.0659  -0.0067 120 ASP A OD1 
878  O OD2 . ASP A 134 ? 0.4050 0.4358 0.6122 -0.0305 0.0613  -0.0093 120 ASP A OD2 
879  N N   . GLY A 135 ? 0.3511 0.3551 0.4906 -0.0402 0.0861  -0.0039 121 GLY A N   
880  C CA  . GLY A 135 ? 0.3784 0.3752 0.5028 -0.0449 0.0863  0.0030  121 GLY A CA  
881  C C   . GLY A 135 ? 0.4377 0.4334 0.5687 -0.0456 0.0774  0.0080  121 GLY A C   
882  O O   . GLY A 135 ? 0.4016 0.3911 0.5233 -0.0491 0.0779  0.0145  121 GLY A O   
883  N N   . GLU A 136 ? 0.3883 0.3893 0.5345 -0.0422 0.0697  0.0053  122 GLU A N   
884  C CA  . GLU A 136 ? 0.3625 0.3622 0.5150 -0.0424 0.0616  0.0086  122 GLU A CA  
885  C C   . GLU A 136 ? 0.3884 0.3826 0.5288 -0.0395 0.0522  0.0100  122 GLU A C   
886  O O   . GLU A 136 ? 0.3500 0.3460 0.4890 -0.0361 0.0487  0.0060  122 GLU A O   
887  C CB  . GLU A 136 ? 0.3762 0.3851 0.5510 -0.0409 0.0586  0.0046  122 GLU A CB  
888  C CG  . GLU A 136 ? 0.5373 0.5441 0.7181 -0.0419 0.0516  0.0067  122 GLU A CG  
889  C CD  . GLU A 136 ? 0.5869 0.5866 0.7633 -0.0468 0.0556  0.0124  122 GLU A CD  
890  O OE1 . GLU A 136 ? 0.6383 0.6400 0.8188 -0.0509 0.0644  0.0134  122 GLU A OE1 
891  O OE2 . GLU A 136 ? 0.4484 0.4403 0.6177 -0.0464 0.0503  0.0162  122 GLU A OE2 
892  N N   . PHE A 137 ? 0.3671 0.3548 0.5002 -0.0408 0.0484  0.0158  123 PHE A N   
893  C CA  . PHE A 137 ? 0.4585 0.4422 0.5816 -0.0381 0.0399  0.0179  123 PHE A CA  
894  C C   . PHE A 137 ? 0.4207 0.4039 0.5530 -0.0363 0.0331  0.0192  123 PHE A C   
895  O O   . PHE A 137 ? 0.3831 0.3633 0.5091 -0.0341 0.0268  0.0220  123 PHE A O   
896  C CB  . PHE A 137 ? 0.3083 0.2847 0.4122 -0.0402 0.0406  0.0239  123 PHE A CB  
897  C CG  . PHE A 137 ? 0.4603 0.4361 0.5504 -0.0417 0.0459  0.0213  123 PHE A CG  
898  C CD1 . PHE A 137 ? 0.3981 0.3736 0.4785 -0.0401 0.0412  0.0183  123 PHE A CD1 
899  C CD2 . PHE A 137 ? 0.4541 0.4294 0.5413 -0.0452 0.0563  0.0214  123 PHE A CD2 
900  C CE1 . PHE A 137 ? 0.3625 0.3360 0.4292 -0.0418 0.0463  0.0148  123 PHE A CE1 
901  C CE2 . PHE A 137 ? 0.4478 0.4217 0.5211 -0.0464 0.0622  0.0181  123 PHE A CE2 
902  C CZ  . PHE A 137 ? 0.3551 0.3275 0.4177 -0.0447 0.0571  0.0144  123 PHE A CZ  
903  N N   . ARG A 138 ? 0.3273 0.3139 0.4748 -0.0371 0.0342  0.0168  124 ARG A N   
904  C CA  . ARG A 138 ? 0.2603 0.2453 0.4154 -0.0357 0.0286  0.0169  124 ARG A CA  
905  C C   . ARG A 138 ? 0.3089 0.3010 0.4758 -0.0336 0.0250  0.0108  124 ARG A C   
906  O O   . ARG A 138 ? 0.3668 0.3578 0.5393 -0.0328 0.0208  0.0097  124 ARG A O   
907  C CB  . ARG A 138 ? 0.2904 0.2700 0.4506 -0.0394 0.0321  0.0201  124 ARG A CB  
908  C CG  . ARG A 138 ? 0.4020 0.3720 0.5503 -0.0399 0.0324  0.0279  124 ARG A CG  
909  C CD  . ARG A 138 ? 0.5254 0.4885 0.6783 -0.0441 0.0372  0.0317  124 ARG A CD  
910  N NE  . ARG A 138 ? 0.8395 0.7928 0.9800 -0.0442 0.0375  0.0404  124 ARG A NE  
911  C CZ  . ARG A 138 ? 0.6950 0.6416 0.8312 -0.0485 0.0438  0.0462  124 ARG A CZ  
912  N NH1 . ARG A 138 ? 0.7725 0.7219 0.9173 -0.0537 0.0512  0.0439  124 ARG A NH1 
913  N NH2 . ARG A 138 ? 0.7822 0.7196 0.9059 -0.0477 0.0427  0.0550  124 ARG A NH2 
914  N N   . HIS A 139 ? 0.2529 0.2516 0.4228 -0.0325 0.0264  0.0070  125 HIS A N   
915  C CA  . HIS A 139 ? 0.3746 0.3799 0.5546 -0.0301 0.0221  0.0023  125 HIS A CA  
916  C C   . HIS A 139 ? 0.2830 0.2860 0.4584 -0.0269 0.0152  0.0023  125 HIS A C   
917  O O   . HIS A 139 ? 0.2959 0.3005 0.4775 -0.0264 0.0112  0.0001  125 HIS A O   
918  C CB  . HIS A 139 ? 0.3369 0.3476 0.5190 -0.0281 0.0246  -0.0007 125 HIS A CB  
919  C CG  . HIS A 139 ? 0.3277 0.3442 0.5202 -0.0303 0.0314  -0.0023 125 HIS A CG  
920  N ND1 . HIS A 139 ? 0.3600 0.3818 0.5669 -0.0330 0.0319  -0.0033 125 HIS A ND1 
921  C CD2 . HIS A 139 ? 0.3754 0.3937 0.5669 -0.0303 0.0386  -0.0034 125 HIS A CD2 
922  C CE1 . HIS A 139 ? 0.4184 0.4462 0.6342 -0.0346 0.0390  -0.0045 125 HIS A CE1 
923  N NE2 . HIS A 139 ? 0.3688 0.3945 0.5753 -0.0327 0.0437  -0.0046 125 HIS A NE2 
924  N N   . PHE A 140 ? 0.2409 0.2407 0.4053 -0.0253 0.0138  0.0044  126 PHE A N   
925  C CA  . PHE A 140 ? 0.3462 0.3455 0.5076 -0.0224 0.0081  0.0042  126 PHE A CA  
926  C C   . PHE A 140 ? 0.3323 0.3276 0.4935 -0.0221 0.0059  0.0066  126 PHE A C   
927  O O   . PHE A 140 ? 0.3026 0.2985 0.4655 -0.0201 0.0024  0.0052  126 PHE A O   
928  C CB  . PHE A 140 ? 0.2577 0.2557 0.4092 -0.0215 0.0073  0.0053  126 PHE A CB  
929  C CG  . PHE A 140 ? 0.3382 0.3375 0.4881 -0.0221 0.0114  0.0030  126 PHE A CG  
930  C CD1 . PHE A 140 ? 0.2742 0.2780 0.4334 -0.0207 0.0125  -0.0007 126 PHE A CD1 
931  C CD2 . PHE A 140 ? 0.2788 0.2746 0.4178 -0.0240 0.0143  0.0044  126 PHE A CD2 
932  C CE1 . PHE A 140 ? 0.2862 0.2910 0.4457 -0.0204 0.0172  -0.0032 126 PHE A CE1 
933  C CE2 . PHE A 140 ? 0.2997 0.2957 0.4366 -0.0244 0.0193  0.0013  126 PHE A CE2 
934  C CZ  . PHE A 140 ? 0.2991 0.2995 0.4471 -0.0223 0.0212  -0.0026 126 PHE A CZ  
935  N N   . TYR A 141 ? 0.3366 0.3269 0.4955 -0.0240 0.0086  0.0104  127 TYR A N   
936  C CA  . TYR A 141 ? 0.2897 0.2748 0.4504 -0.0234 0.0073  0.0125  127 TYR A CA  
937  C C   . TYR A 141 ? 0.3365 0.3222 0.5062 -0.0240 0.0066  0.0078  127 TYR A C   
938  O O   . TYR A 141 ? 0.2681 0.2523 0.4388 -0.0218 0.0039  0.0062  127 TYR A O   
939  C CB  . TYR A 141 ? 0.3708 0.3494 0.5279 -0.0256 0.0107  0.0179  127 TYR A CB  
940  C CG  . TYR A 141 ? 0.3478 0.3189 0.5081 -0.0249 0.0104  0.0205  127 TYR A CG  
941  C CD1 . TYR A 141 ? 0.3504 0.3184 0.5075 -0.0212 0.0072  0.0246  127 TYR A CD1 
942  C CD2 . TYR A 141 ? 0.4307 0.3975 0.5982 -0.0280 0.0134  0.0189  127 TYR A CD2 
943  C CE1 . TYR A 141 ? 0.3716 0.3317 0.5326 -0.0196 0.0075  0.0270  127 TYR A CE1 
944  C CE2 . TYR A 141 ? 0.4483 0.4061 0.6186 -0.0273 0.0136  0.0209  127 TYR A CE2 
945  C CZ  . TYR A 141 ? 0.4330 0.3871 0.6000 -0.0227 0.0109  0.0250  127 TYR A CZ  
946  O OH  . TYR A 141 ? 0.5626 0.5069 0.7334 -0.0211 0.0116  0.0268  127 TYR A OH  
947  N N   . HIS A 142 ? 0.2680 0.2565 0.4443 -0.0272 0.0091  0.0052  128 HIS A N   
948  C CA  . HIS A 142 ? 0.2744 0.2641 0.4592 -0.0288 0.0075  0.0004  128 HIS A CA  
949  C C   . HIS A 142 ? 0.3451 0.3402 0.5299 -0.0261 0.0027  -0.0035 128 HIS A C   
950  O O   . HIS A 142 ? 0.3523 0.3459 0.5383 -0.0259 -0.0001 -0.0069 128 HIS A O   
951  C CB  . HIS A 142 ? 0.2801 0.2738 0.4740 -0.0333 0.0107  -0.0011 128 HIS A CB  
952  C CG  . HIS A 142 ? 0.4344 0.4215 0.6285 -0.0369 0.0160  0.0029  128 HIS A CG  
953  N ND1 . HIS A 142 ? 0.4123 0.4020 0.6077 -0.0397 0.0217  0.0052  128 HIS A ND1 
954  C CD2 . HIS A 142 ? 0.3910 0.3681 0.5836 -0.0380 0.0171  0.0055  128 HIS A CD2 
955  C CE1 . HIS A 142 ? 0.5526 0.5343 0.7464 -0.0429 0.0259  0.0095  128 HIS A CE1 
956  N NE2 . HIS A 142 ? 0.4801 0.4536 0.6726 -0.0418 0.0229  0.0100  128 HIS A NE2 
957  N N   . MET A 143 ? 0.2945 0.2950 0.4769 -0.0240 0.0019  -0.0032 129 MET A N   
958  C CA  . MET A 143 ? 0.2829 0.2875 0.4643 -0.0214 -0.0025 -0.0057 129 MET A CA  
959  C C   . MET A 143 ? 0.3299 0.3307 0.5047 -0.0190 -0.0045 -0.0052 129 MET A C   
960  O O   . MET A 143 ? 0.3678 0.3704 0.5413 -0.0177 -0.0076 -0.0077 129 MET A O   
961  C CB  . MET A 143 ? 0.2923 0.3010 0.4722 -0.0196 -0.0021 -0.0049 129 MET A CB  
962  C CG  . MET A 143 ? 0.2629 0.2778 0.4521 -0.0206 -0.0006 -0.0067 129 MET A CG  
963  S SD  . MET A 143 ? 0.3396 0.3553 0.5259 -0.0189 0.0033  -0.0055 129 MET A SD  
964  C CE  . MET A 143 ? 0.1838 0.2010 0.3681 -0.0148 -0.0018 -0.0063 129 MET A CE  
965  N N   . SER A 144 ? 0.2779 0.2741 0.4488 -0.0182 -0.0028 -0.0017 130 SER A N   
966  C CA  . SER A 144 ? 0.2803 0.2740 0.4477 -0.0155 -0.0039 -0.0010 130 SER A CA  
967  C C   . SER A 144 ? 0.3627 0.3512 0.5325 -0.0156 -0.0032 -0.0034 130 SER A C   
968  O O   . SER A 144 ? 0.2765 0.2634 0.4443 -0.0130 -0.0034 -0.0041 130 SER A O   
969  C CB  . SER A 144 ? 0.3604 0.3527 0.5243 -0.0143 -0.0032 0.0041  130 SER A CB  
970  O OG  . SER A 144 ? 0.4575 0.4509 0.6201 -0.0114 -0.0045 0.0049  130 SER A OG  
971  N N   . GLU A 145 ? 0.3072 0.2926 0.4815 -0.0188 -0.0019 -0.0051 131 GLU A N   
972  C CA  . GLU A 145 ? 0.3566 0.3347 0.5329 -0.0194 -0.0009 -0.0081 131 GLU A CA  
973  C C   . GLU A 145 ? 0.3467 0.3254 0.5201 -0.0183 -0.0030 -0.0137 131 GLU A C   
974  O O   . GLU A 145 ? 0.3447 0.3175 0.5165 -0.0161 -0.0013 -0.0150 131 GLU A O   
975  C CB  . GLU A 145 ? 0.3225 0.2978 0.5050 -0.0243 0.0005  -0.0096 131 GLU A CB  
976  C CG  . GLU A 145 ? 0.6131 0.5780 0.7978 -0.0255 0.0023  -0.0123 131 GLU A CG  
977  C CD  . GLU A 145 ? 0.6986 0.6634 0.8835 -0.0278 -0.0003 -0.0203 131 GLU A CD  
978  O OE1 . GLU A 145 ? 0.7682 0.7237 0.9525 -0.0278 0.0012  -0.0239 131 GLU A OE1 
979  O OE2 . GLU A 145 ? 0.6823 0.6558 0.8677 -0.0294 -0.0040 -0.0230 131 GLU A OE2 
980  N N   . PRO A 146 ? 0.3333 0.3183 0.5055 -0.0195 -0.0064 -0.0169 132 PRO A N   
981  C CA  . PRO A 146 ? 0.3264 0.3108 0.4931 -0.0191 -0.0084 -0.0221 132 PRO A CA  
982  C C   . PRO A 146 ? 0.3625 0.3469 0.5227 -0.0149 -0.0070 -0.0206 132 PRO A C   
983  O O   . PRO A 146 ? 0.3315 0.3137 0.4859 -0.0143 -0.0069 -0.0249 132 PRO A O   
984  C CB  . PRO A 146 ? 0.3802 0.3725 0.5473 -0.0209 -0.0132 -0.0238 132 PRO A CB  
985  C CG  . PRO A 146 ? 0.3318 0.3275 0.5079 -0.0234 -0.0127 -0.0216 132 PRO A CG  
986  C CD  . PRO A 146 ? 0.3119 0.3044 0.4880 -0.0215 -0.0084 -0.0162 132 PRO A CD  
987  N N   . ILE A 147 ? 0.3306 0.3176 0.4915 -0.0124 -0.0057 -0.0151 133 ILE A N   
988  C CA  . ILE A 147 ? 0.3077 0.2966 0.4646 -0.0091 -0.0045 -0.0136 133 ILE A CA  
989  C C   . ILE A 147 ? 0.3400 0.3262 0.5009 -0.0062 -0.0013 -0.0101 133 ILE A C   
990  O O   . ILE A 147 ? 0.3499 0.3399 0.5109 -0.0039 -0.0005 -0.0072 133 ILE A O   
991  C CB  . ILE A 147 ? 0.2930 0.2883 0.4475 -0.0090 -0.0067 -0.0103 133 ILE A CB  
992  C CG1 . ILE A 147 ? 0.2392 0.2362 0.3976 -0.0098 -0.0071 -0.0063 133 ILE A CG1 
993  C CG2 . ILE A 147 ? 0.2480 0.2459 0.3986 -0.0105 -0.0102 -0.0131 133 ILE A CG2 
994  C CD1 . ILE A 147 ? 0.3037 0.3051 0.4598 -0.0095 -0.0086 -0.0036 133 ILE A CD1 
995  N N   . THR A 148 ? 0.3534 0.3331 0.5187 -0.0064 0.0003  -0.0101 134 THR A N   
996  C CA  . THR A 148 ? 0.3152 0.2917 0.4852 -0.0029 0.0028  -0.0063 134 THR A CA  
997  C C   . THR A 148 ? 0.3933 0.3596 0.5658 -0.0025 0.0057  -0.0100 134 THR A C   
998  O O   . THR A 148 ? 0.4104 0.3722 0.5822 -0.0063 0.0052  -0.0140 134 THR A O   
999  C CB  . THR A 148 ? 0.3250 0.3026 0.4973 -0.0033 0.0014  0.0005  134 THR A CB  
1000 O OG1 . THR A 148 ? 0.3768 0.3511 0.5491 -0.0073 0.0011  -0.0001 134 THR A OG1 
1001 C CG2 . THR A 148 ? 0.2037 0.1899 0.3733 -0.0036 -0.0011 0.0036  134 THR A CG2 
1002 N N   . VAL A 149 ? 0.3170 0.2798 0.4937 0.0022  0.0089  -0.0090 135 VAL A N   
1003 C CA  . VAL A 149 ? 0.3735 0.3244 0.5534 0.0033  0.0123  -0.0122 135 VAL A CA  
1004 C C   . VAL A 149 ? 0.2619 0.2061 0.4472 0.0033  0.0122  -0.0061 135 VAL A C   
1005 O O   . VAL A 149 ? 0.3564 0.2890 0.5444 0.0029  0.0147  -0.0084 135 VAL A O   
1006 C CB  . VAL A 149 ? 0.3313 0.2799 0.5145 0.0091  0.0169  -0.0144 135 VAL A CB  
1007 C CG1 . VAL A 149 ? 0.4413 0.3918 0.6166 0.0081  0.0187  -0.0223 135 VAL A CG1 
1008 C CG2 . VAL A 149 ? 0.2711 0.2281 0.4610 0.0141  0.0165  -0.0069 135 VAL A CG2 
1009 N N   . ALA A 150 ? 0.2834 0.2337 0.4694 0.0035  0.0094  0.0016  136 ALA A N   
1010 C CA  . ALA A 150 ? 0.3590 0.3030 0.5476 0.0034  0.0091  0.0085  136 ALA A CA  
1011 C C   . ALA A 150 ? 0.2972 0.2498 0.4817 0.0014  0.0056  0.0144  136 ALA A C   
1012 O O   . ALA A 150 ? 0.2430 0.2054 0.4258 0.0025  0.0033  0.0150  136 ALA A O   
1013 C CB  . ALA A 150 ? 0.3235 0.2622 0.5192 0.0100  0.0107  0.0133  136 ALA A CB  
1014 N N   . GLN A 151 ? 0.2844 0.2324 0.4669 -0.0021 0.0057  0.0184  137 GLN A N   
1015 C CA  . GLN A 151 ? 0.3174 0.2718 0.4943 -0.0042 0.0032  0.0236  137 GLN A CA  
1016 C C   . GLN A 151 ? 0.3973 0.3436 0.5722 -0.0058 0.0043  0.0306  137 GLN A C   
1017 O O   . GLN A 151 ? 0.3186 0.2544 0.4970 -0.0066 0.0073  0.0306  137 GLN A O   
1018 C CB  . GLN A 151 ? 0.2992 0.2603 0.4724 -0.0088 0.0030  0.0186  137 GLN A CB  
1019 C CG  . GLN A 151 ? 0.3875 0.3439 0.5629 -0.0134 0.0056  0.0143  137 GLN A CG  
1020 C CD  . GLN A 151 ? 0.7248 0.6894 0.8994 -0.0165 0.0046  0.0090  137 GLN A CD  
1021 O OE1 . GLN A 151 ? 0.5498 0.5221 0.7210 -0.0153 0.0024  0.0090  137 GLN A OE1 
1022 N NE2 . GLN A 151 ? 0.5887 0.5516 0.7673 -0.0206 0.0059  0.0047  137 GLN A NE2 
1023 N N   . ALA A 152 ? 0.3062 0.2567 0.4745 -0.0065 0.0020  0.0366  138 ALA A N   
1024 C CA  . ALA A 152 ? 0.3628 0.3058 0.5263 -0.0084 0.0032  0.0442  138 ALA A CA  
1025 C C   . ALA A 152 ? 0.3010 0.2502 0.4539 -0.0116 0.0019  0.0469  138 ALA A C   
1026 O O   . ALA A 152 ? 0.2966 0.2549 0.4469 -0.0108 -0.0014 0.0450  138 ALA A O   
1027 C CB  . ALA A 152 ? 0.2912 0.2280 0.4573 -0.0031 0.0011  0.0522  138 ALA A CB  
1028 N N   . ILE A 153 ? 0.3594 0.3029 0.5063 -0.0158 0.0052  0.0508  139 ILE A N   
1029 C CA  . ILE A 153 ? 0.3548 0.3011 0.4891 -0.0185 0.0048  0.0550  139 ILE A CA  
1030 C C   . ILE A 153 ? 0.4104 0.3501 0.5384 -0.0163 0.0020  0.0656  139 ILE A C   
1031 O O   . ILE A 153 ? 0.4234 0.3525 0.5521 -0.0170 0.0051  0.0708  139 ILE A O   
1032 C CB  . ILE A 153 ? 0.3714 0.3164 0.5023 -0.0245 0.0113  0.0527  139 ILE A CB  
1033 C CG1 . ILE A 153 ? 0.4212 0.3744 0.5589 -0.0259 0.0127  0.0429  139 ILE A CG1 
1034 C CG2 . ILE A 153 ? 0.3776 0.3230 0.4932 -0.0271 0.0119  0.0577  139 ILE A CG2 
1035 C CD1 . ILE A 153 ? 0.3717 0.3248 0.5123 -0.0312 0.0194  0.0401  139 ILE A CD1 
1036 N N   . LEU A 154 ? 0.3693 0.3149 0.4917 -0.0137 -0.0044 0.0693  140 LEU A N   
1037 C CA  . LEU A 154 ? 0.4275 0.3685 0.5449 -0.0108 -0.0090 0.0800  140 LEU A CA  
1038 C C   . LEU A 154 ? 0.4900 0.4252 0.5907 -0.0156 -0.0067 0.0864  140 LEU A C   
1039 O O   . LEU A 154 ? 0.3550 0.2948 0.4448 -0.0200 -0.0052 0.0829  140 LEU A O   
1040 C CB  . LEU A 154 ? 0.3301 0.2811 0.4481 -0.0071 -0.0174 0.0816  140 LEU A CB  
1041 C CG  . LEU A 154 ? 0.3843 0.3416 0.5186 -0.0022 -0.0189 0.0763  140 LEU A CG  
1042 C CD1 . LEU A 154 ? 0.3879 0.3561 0.5245 0.0009  -0.0271 0.0790  140 LEU A CD1 
1043 C CD2 . LEU A 154 ? 0.3509 0.2989 0.4971 0.0023  -0.0160 0.0783  140 LEU A CD2 
1044 N N   . THR A 155 ? 0.4406 0.3647 0.5392 -0.0147 -0.0057 0.0956  141 THR A N   
1045 C CA  . THR A 155 ? 0.4589 0.3760 0.5403 -0.0190 -0.0034 0.1037  141 THR A CA  
1046 C C   . THR A 155 ? 0.5174 0.4303 0.5926 -0.0146 -0.0111 0.1163  141 THR A C   
1047 O O   . THR A 155 ? 0.4735 0.3884 0.5610 -0.0080 -0.0170 0.1187  141 THR A O   
1048 C CB  . THR A 155 ? 0.4371 0.3430 0.5205 -0.0233 0.0062  0.1045  141 THR A CB  
1049 O OG1 . THR A 155 ? 0.4542 0.3490 0.5478 -0.0192 0.0057  0.1105  141 THR A OG1 
1050 C CG2 . THR A 155 ? 0.3893 0.3004 0.4834 -0.0267 0.0124  0.0922  141 THR A CG2 
1051 N N   . GLU A 156 ? 0.5192 0.4267 0.5750 -0.0183 -0.0108 0.1247  142 GLU A N   
1052 C CA  . GLU A 156 ? 0.4541 0.3563 0.5021 -0.0145 -0.0184 0.1384  142 GLU A CA  
1053 C C   . GLU A 156 ? 0.5815 0.4711 0.6431 -0.0096 -0.0167 0.1454  142 GLU A C   
1054 O O   . GLU A 156 ? 0.5078 0.3953 0.5731 -0.0031 -0.0244 0.1550  142 GLU A O   
1055 C CB  . GLU A 156 ? 0.5606 0.4575 0.5825 -0.0204 -0.0168 0.1458  142 GLU A CB  
1056 C CG  . GLU A 156 ? 0.6918 0.5813 0.7022 -0.0172 -0.0244 0.1617  142 GLU A CG  
1057 C CD  . GLU A 156 ? 0.7938 0.6772 0.7755 -0.0238 -0.0218 0.1687  142 GLU A CD  
1058 O OE1 . GLU A 156 ? 0.7722 0.6530 0.7466 -0.0306 -0.0107 0.1627  142 GLU A OE1 
1059 O OE2 . GLU A 156 ? 0.7770 0.6587 0.7435 -0.0221 -0.0308 0.1804  142 GLU A OE2 
1060 N N   . GLN A 157 ? 0.4977 0.3789 0.5681 -0.0126 -0.0069 0.1404  143 GLN A N   
1061 C CA  . GLN A 157 ? 0.4938 0.3602 0.5757 -0.0094 -0.0039 0.1462  143 GLN A CA  
1062 C C   . GLN A 157 ? 0.5045 0.3728 0.6090 -0.0032 -0.0048 0.1385  143 GLN A C   
1063 O O   . GLN A 157 ? 0.4710 0.3264 0.5859 0.0008  -0.0031 0.1429  143 GLN A O   
1064 C CB  . GLN A 157 ? 0.4601 0.3152 0.5391 -0.0171 0.0074  0.1453  143 GLN A CB  
1065 C CG  . GLN A 157 ? 0.5813 0.4335 0.6373 -0.0237 0.0107  0.1527  143 GLN A CG  
1066 C CD  . GLN A 157 ? 0.7743 0.6143 0.8292 -0.0312 0.0223  0.1542  143 GLN A CD  
1067 O OE1 . GLN A 157 ? 0.8501 0.6787 0.9191 -0.0307 0.0262  0.1547  143 GLN A OE1 
1068 N NE2 . GLN A 157 ? 0.7535 0.5958 0.7919 -0.0384 0.0284  0.1546  143 GLN A NE2 
1069 N N   . ASN A 158 ? 0.3910 0.2738 0.5026 -0.0023 -0.0068 0.1272  144 ASN A N   
1070 C CA  . ASN A 158 ? 0.4462 0.3307 0.5771 0.0026  -0.0062 0.1190  144 ASN A CA  
1071 C C   . ASN A 158 ? 0.5076 0.4072 0.6457 0.0083  -0.0136 0.1156  144 ASN A C   
1072 O O   . ASN A 158 ? 0.4308 0.3323 0.5841 0.0127  -0.0126 0.1090  144 ASN A O   
1073 C CB  . ASN A 158 ? 0.4627 0.3478 0.5990 -0.0032 0.0015  0.1063  144 ASN A CB  
1074 C CG  . ASN A 158 ? 0.5050 0.4054 0.6359 -0.0071 0.0007  0.0974  144 ASN A CG  
1075 O OD1 . ASN A 158 ? 0.4289 0.3397 0.5534 -0.0055 -0.0054 0.0990  144 ASN A OD1 
1076 N ND2 . ASN A 158 ? 0.4751 0.3767 0.6093 -0.0123 0.0068  0.0881  144 ASN A ND2 
1077 N N   . ALA A 159 ? 0.4260 0.3056 0.4826 -0.0731 -0.0786 0.0866  145 ALA A N   
1078 C CA  . ALA A 159 ? 0.3928 0.2951 0.4827 -0.0566 -0.0827 0.0855  145 ALA A CA  
1079 C C   . ALA A 159 ? 0.4515 0.3442 0.5578 -0.0394 -0.0874 0.0928  145 ALA A C   
1080 O O   . ALA A 159 ? 0.4328 0.3416 0.5629 -0.0307 -0.0834 0.0882  145 ALA A O   
1081 C CB  . ALA A 159 ? 0.4066 0.3169 0.4960 -0.0572 -0.0914 0.0884  145 ALA A CB  
1082 N N   . CYS A 160 ? 0.5162 0.3824 0.6088 -0.0347 -0.0969 0.1028  146 CYS A N   
1083 C CA  . CYS A 160 ? 0.5209 0.3855 0.6338 -0.0161 -0.1037 0.1068  146 CYS A CA  
1084 C C   . CYS A 160 ? 0.5375 0.3967 0.6576 -0.0110 -0.0964 0.1032  146 CYS A C   
1085 O O   . CYS A 160 ? 0.4724 0.3480 0.6191 0.0012  -0.0956 0.1003  146 CYS A O   
1086 C CB  . CYS A 160 ? 0.5625 0.4009 0.6598 -0.0099 -0.1186 0.1164  146 CYS A CB  
1087 S SG  . CYS A 160 ? 0.6154 0.4682 0.7149 -0.0112 -0.1280 0.1202  146 CYS A SG  
1088 N N   . TYR A 161 ? 0.5479 0.3848 0.6434 -0.0219 -0.0908 0.1029  147 TYR A N   
1089 C CA  . TYR A 161 ? 0.4779 0.3101 0.5808 -0.0170 -0.0837 0.0992  147 TYR A CA  
1090 C C   . TYR A 161 ? 0.4575 0.3185 0.5789 -0.0212 -0.0706 0.0896  147 TYR A C   
1091 O O   . TYR A 161 ? 0.5109 0.3791 0.6498 -0.0136 -0.0656 0.0861  147 TYR A O   
1092 C CB  . TYR A 161 ? 0.5761 0.3702 0.6445 -0.0265 -0.0837 0.1027  147 TYR A CB  
1093 C CG  . TYR A 161 ? 0.6294 0.4202 0.6714 -0.0495 -0.0736 0.0990  147 TYR A CG  
1094 C CD1 . TYR A 161 ? 0.5732 0.3788 0.6213 -0.0566 -0.0596 0.0900  147 TYR A CD1 
1095 C CD2 . TYR A 161 ? 0.6701 0.4429 0.6793 -0.0653 -0.0785 0.1037  147 TYR A CD2 
1096 C CE1 . TYR A 161 ? 0.7234 0.5307 0.7487 -0.0781 -0.0501 0.0840  147 TYR A CE1 
1097 C CE2 . TYR A 161 ? 0.6763 0.4503 0.6607 -0.0889 -0.0683 0.0980  147 TYR A CE2 
1098 C CZ  . TYR A 161 ? 0.7314 0.5245 0.7251 -0.0948 -0.0540 0.0873  147 TYR A CZ  
1099 O OH  . TYR A 161 ? 0.6017 0.4015 0.5728 -0.1186 -0.0436 0.0790  147 TYR A OH  
1100 N N   . GLU A 162 ? 0.3803 0.2586 0.4988 -0.0325 -0.0660 0.0844  148 GLU A N   
1101 C CA  . GLU A 162 ? 0.4033 0.3081 0.5407 -0.0333 -0.0577 0.0745  148 GLU A CA  
1102 C C   . GLU A 162 ? 0.4352 0.3592 0.6005 -0.0209 -0.0624 0.0748  148 GLU A C   
1103 O O   . GLU A 162 ? 0.3678 0.3041 0.5489 -0.0176 -0.0575 0.0699  148 GLU A O   
1104 C CB  . GLU A 162 ? 0.3874 0.3070 0.5158 -0.0464 -0.0539 0.0660  148 GLU A CB  
1105 C CG  . GLU A 162 ? 0.4841 0.3959 0.5896 -0.0622 -0.0443 0.0600  148 GLU A CG  
1106 C CD  . GLU A 162 ? 0.3561 0.2672 0.4680 -0.0607 -0.0354 0.0555  148 GLU A CD  
1107 O OE1 . GLU A 162 ? 0.6851 0.6170 0.8050 -0.0648 -0.0287 0.0436  148 GLU A OE1 
1108 O OE2 . GLU A 162 ? 0.6197 0.5099 0.7287 -0.0550 -0.0358 0.0626  148 GLU A OE2 
1109 N N   . ILE A 163 ? 0.3870 0.3134 0.5564 -0.0155 -0.0721 0.0806  149 ILE A N   
1110 C CA  . ILE A 163 ? 0.4102 0.3542 0.6032 -0.0060 -0.0766 0.0811  149 ILE A CA  
1111 C C   . ILE A 163 ? 0.3422 0.2849 0.5484 0.0030  -0.0746 0.0816  149 ILE A C   
1112 O O   . ILE A 163 ? 0.3013 0.2596 0.5241 0.0047  -0.0709 0.0774  149 ILE A O   
1113 C CB  . ILE A 163 ? 0.3507 0.2970 0.5444 -0.0024 -0.0874 0.0871  149 ILE A CB  
1114 C CG1 . ILE A 163 ? 0.3875 0.3432 0.5749 -0.0105 -0.0892 0.0841  149 ILE A CG1 
1115 C CG2 . ILE A 163 ? 0.3216 0.2839 0.5378 0.0071  -0.0919 0.0881  149 ILE A CG2 
1116 C CD1 . ILE A 163 ? 0.3472 0.2998 0.5279 -0.0099 -0.0989 0.0906  149 ILE A CD1 
1117 N N   . ASP A 164 ? 0.3272 0.2497 0.5243 0.0085  -0.0779 0.0858  150 ASP A N   
1118 C CA  . ASP A 164 ? 0.3327 0.2554 0.5438 0.0191  -0.0772 0.0839  150 ASP A CA  
1119 C C   . ASP A 164 ? 0.3381 0.2616 0.5512 0.0147  -0.0654 0.0781  150 ASP A C   
1120 O O   . ASP A 164 ? 0.3623 0.3001 0.5939 0.0197  -0.0618 0.0736  150 ASP A O   
1121 C CB  . ASP A 164 ? 0.3602 0.2563 0.5584 0.0277  -0.0865 0.0885  150 ASP A CB  
1122 C CG  . ASP A 164 ? 0.4743 0.3736 0.6766 0.0358  -0.0998 0.0929  150 ASP A CG  
1123 O OD1 . ASP A 164 ? 0.4415 0.3658 0.6585 0.0345  -0.1006 0.0922  150 ASP A OD1 
1124 O OD2 . ASP A 164 ? 0.4547 0.3295 0.6440 0.0436  -0.1107 0.0970  150 ASP A OD2 
1125 N N   . ARG A 165 ? 0.3279 0.2383 0.5218 0.0040  -0.0591 0.0773  151 ARG A N   
1126 C CA  . ARG A 165 ? 0.3335 0.2450 0.5284 -0.0006 -0.0480 0.0715  151 ARG A CA  
1127 C C   . ARG A 165 ? 0.3487 0.2856 0.5618 -0.0025 -0.0440 0.0659  151 ARG A C   
1128 O O   . ARG A 165 ? 0.3798 0.3237 0.6044 -0.0007 -0.0383 0.0621  151 ARG A O   
1129 C CB  . ARG A 165 ? 0.4933 0.3900 0.6635 -0.0135 -0.0422 0.0701  151 ARG A CB  
1130 C CG  . ARG A 165 ? 0.3858 0.2901 0.5584 -0.0200 -0.0307 0.0623  151 ARG A CG  
1131 C CD  . ARG A 165 ? 0.3861 0.2816 0.5350 -0.0346 -0.0243 0.0586  151 ARG A CD  
1132 N NE  . ARG A 165 ? 0.3765 0.2902 0.5243 -0.0419 -0.0252 0.0530  151 ARG A NE  
1133 C CZ  . ARG A 165 ? 0.4121 0.3487 0.5741 -0.0419 -0.0229 0.0441  151 ARG A CZ  
1134 N NH1 . ARG A 165 ? 0.3532 0.2968 0.5301 -0.0369 -0.0194 0.0410  151 ARG A NH1 
1135 N NH2 . ARG A 165 ? 0.3731 0.3249 0.5332 -0.0471 -0.0252 0.0371  151 ARG A NH2 
1136 N N   . VAL A 166 ? 0.3251 0.2737 0.5387 -0.0067 -0.0478 0.0651  152 VAL A N   
1137 C CA  . VAL A 166 ? 0.2618 0.2276 0.4870 -0.0089 -0.0471 0.0600  152 VAL A CA  
1138 C C   . VAL A 166 ? 0.2967 0.2743 0.5391 -0.0039 -0.0497 0.0616  152 VAL A C   
1139 O O   . VAL A 166 ? 0.2417 0.2269 0.4915 -0.0065 -0.0457 0.0579  152 VAL A O   
1140 C CB  . VAL A 166 ? 0.2898 0.2626 0.5106 -0.0126 -0.0534 0.0580  152 VAL A CB  
1141 C CG1 . VAL A 166 ? 0.2406 0.2253 0.4711 -0.0133 -0.0576 0.0542  152 VAL A CG1 
1142 C CG2 . VAL A 166 ? 0.3525 0.3219 0.5589 -0.0199 -0.0489 0.0517  152 VAL A CG2 
1143 N N   . LEU A 167 ? 0.2733 0.2539 0.5212 0.0020  -0.0566 0.0663  153 LEU A N   
1144 C CA  . LEU A 167 ? 0.2881 0.2857 0.5530 0.0050  -0.0587 0.0656  153 LEU A CA  
1145 C C   . LEU A 167 ? 0.3241 0.3242 0.5985 0.0089  -0.0517 0.0615  153 LEU A C   
1146 O O   . LEU A 167 ? 0.3308 0.3470 0.6167 0.0054  -0.0484 0.0574  153 LEU A O   
1147 C CB  . LEU A 167 ? 0.3032 0.3059 0.5730 0.0115  -0.0678 0.0698  153 LEU A CB  
1148 C CG  . LEU A 167 ? 0.3608 0.3659 0.6242 0.0069  -0.0750 0.0731  153 LEU A CG  
1149 C CD1 . LEU A 167 ? 0.3791 0.3906 0.6479 0.0131  -0.0839 0.0771  153 LEU A CD1 
1150 C CD2 . LEU A 167 ? 0.3468 0.3631 0.6136 -0.0013 -0.0751 0.0702  153 LEU A CD2 
1151 N N   . THR A 168 ? 0.3027 0.2856 0.5703 0.0151  -0.0500 0.0622  154 THR A N   
1152 C CA  . THR A 168 ? 0.3151 0.2984 0.5913 0.0203  -0.0443 0.0571  154 THR A CA  
1153 C C   . THR A 168 ? 0.3316 0.3188 0.6078 0.0114  -0.0340 0.0527  154 THR A C   
1154 O O   . THR A 168 ? 0.3262 0.3281 0.6157 0.0111  -0.0291 0.0471  154 THR A O   
1155 C CB  . THR A 168 ? 0.3477 0.3040 0.6103 0.0276  -0.0465 0.0595  154 THR A CB  
1156 O OG1 . THR A 168 ? 0.3958 0.3470 0.6578 0.0367  -0.0583 0.0634  154 THR A OG1 
1157 C CG2 . THR A 168 ? 0.4927 0.4471 0.7635 0.0342  -0.0416 0.0530  154 THR A CG2 
1158 N N   . THR A 169 ? 0.2936 0.2698 0.5551 0.0037  -0.0309 0.0539  155 THR A N   
1159 C CA  . THR A 169 ? 0.2847 0.2643 0.5454 -0.0042 -0.0232 0.0493  155 THR A CA  
1160 C C   . THR A 169 ? 0.3185 0.3156 0.5882 -0.0101 -0.0257 0.0477  155 THR A C   
1161 O O   . THR A 169 ? 0.2963 0.3007 0.5712 -0.0149 -0.0201 0.0438  155 THR A O   
1162 C CB  . THR A 169 ? 0.3251 0.2939 0.5700 -0.0103 -0.0214 0.0485  155 THR A CB  
1163 O OG1 . THR A 169 ? 0.3372 0.2880 0.5690 -0.0088 -0.0190 0.0504  155 THR A OG1 
1164 C CG2 . THR A 169 ? 0.2392 0.2112 0.4834 -0.0168 -0.0148 0.0427  155 THR A CG2 
1165 N N   . MET A 170 ? 0.3353 0.3375 0.6043 -0.0112 -0.0344 0.0509  156 MET A N   
1166 C CA  . MET A 170 ? 0.3343 0.3488 0.6071 -0.0186 -0.0385 0.0503  156 MET A CA  
1167 C C   . MET A 170 ? 0.4027 0.4347 0.6896 -0.0196 -0.0346 0.0474  156 MET A C   
1168 O O   . MET A 170 ? 0.3816 0.4214 0.6688 -0.0296 -0.0319 0.0444  156 MET A O   
1169 C CB  . MET A 170 ? 0.2558 0.2721 0.5256 -0.0185 -0.0490 0.0544  156 MET A CB  
1170 C CG  . MET A 170 ? 0.2360 0.2408 0.4931 -0.0198 -0.0545 0.0540  156 MET A CG  
1171 S SD  . MET A 170 ? 0.3206 0.3289 0.5756 -0.0197 -0.0667 0.0582  156 MET A SD  
1172 C CE  . MET A 170 ? 0.2262 0.2425 0.4822 -0.0302 -0.0711 0.0585  156 MET A CE  
1173 N N   . LEU A 171 ? 0.2811 0.3201 0.5791 -0.0098 -0.0351 0.0469  157 LEU A N   
1174 C CA  . LEU A 171 ? 0.3047 0.3658 0.6196 -0.0088 -0.0314 0.0403  157 LEU A CA  
1175 C C   . LEU A 171 ? 0.3892 0.4501 0.7071 -0.0104 -0.0211 0.0343  157 LEU A C   
1176 O O   . LEU A 171 ? 0.3535 0.4335 0.6793 -0.0190 -0.0160 0.0280  157 LEU A O   
1177 C CB  . LEU A 171 ? 0.3181 0.3847 0.6446 0.0057  -0.0365 0.0392  157 LEU A CB  
1178 C CG  . LEU A 171 ? 0.4022 0.4762 0.7299 0.0071  -0.0465 0.0436  157 LEU A CG  
1179 C CD1 . LEU A 171 ? 0.3262 0.3989 0.6619 0.0235  -0.0534 0.0429  157 LEU A CD1 
1180 C CD2 . LEU A 171 ? 0.3356 0.4373 0.6720 -0.0046 -0.0465 0.0394  157 LEU A CD2 
1181 N N   . ARG A 172 ? 0.3029 0.3425 0.6124 -0.0045 -0.0177 0.0358  158 ARG A N   
1182 C CA  . ARG A 172 ? 0.3591 0.3966 0.6704 -0.0056 -0.0080 0.0301  158 ARG A CA  
1183 C C   . ARG A 172 ? 0.4572 0.4979 0.7620 -0.0204 -0.0032 0.0290  158 ARG A C   
1184 O O   . ARG A 172 ? 0.4055 0.4599 0.7175 -0.0265 0.0037  0.0227  158 ARG A O   
1185 C CB  . ARG A 172 ? 0.4045 0.4157 0.7036 0.0012  -0.0060 0.0327  158 ARG A CB  
1186 C CG  . ARG A 172 ? 0.6171 0.6238 0.9178 0.0019  0.0035  0.0267  158 ARG A CG  
1187 C CD  . ARG A 172 ? 0.8623 0.8414 1.1503 0.0097  0.0036  0.0288  158 ARG A CD  
1188 N NE  . ARG A 172 ? 0.8275 0.7880 1.0968 0.0067  -0.0005 0.0363  158 ARG A NE  
1189 C CZ  . ARG A 172 ? 0.8034 0.7494 1.0645 0.0135  -0.0089 0.0413  158 ARG A CZ  
1190 N NH1 . ARG A 172 ? 0.7391 0.6718 0.9826 0.0078  -0.0115 0.0468  158 ARG A NH1 
1191 N NH2 . ARG A 172 ? 0.6850 0.6305 0.9554 0.0261  -0.0156 0.0397  158 ARG A NH2 
1192 N N   . GLU A 173 ? 0.3024 0.3307 0.5929 -0.0261 -0.0078 0.0341  159 GLU A N   
1193 C CA  . GLU A 173 ? 0.2747 0.2996 0.5556 -0.0380 -0.0066 0.0330  159 GLU A CA  
1194 C C   . GLU A 173 ? 0.2957 0.3291 0.5729 -0.0495 -0.0136 0.0344  159 GLU A C   
1195 O O   . GLU A 173 ? 0.3914 0.4209 0.6588 -0.0611 -0.0139 0.0333  159 GLU A O   
1196 C CB  . GLU A 173 ? 0.4099 0.4169 0.6771 -0.0368 -0.0095 0.0347  159 GLU A CB  
1197 C CG  . GLU A 173 ? 0.4941 0.4907 0.7591 -0.0306 -0.0018 0.0330  159 GLU A CG  
1198 C CD  . GLU A 173 ? 0.5457 0.5448 0.8153 -0.0330 0.0087  0.0284  159 GLU A CD  
1199 O OE1 . GLU A 173 ? 0.5743 0.5776 0.8420 -0.0422 0.0104  0.0258  159 GLU A OE1 
1200 O OE2 . GLU A 173 ? 0.5929 0.5877 0.8665 -0.0259 0.0141  0.0272  159 GLU A OE2 
1201 N N   . ARG A 174 ? 0.3179 0.3611 0.6004 -0.0478 -0.0199 0.0368  160 ARG A N   
1202 C CA  . ARG A 174 ? 0.3040 0.3526 0.5792 -0.0604 -0.0277 0.0388  160 ARG A CA  
1203 C C   . ARG A 174 ? 0.3138 0.3403 0.5694 -0.0654 -0.0374 0.0424  160 ARG A C   
1204 O O   . ARG A 174 ? 0.3920 0.4116 0.6339 -0.0788 -0.0416 0.0424  160 ARG A O   
1205 C CB  . ARG A 174 ? 0.3661 0.4327 0.6444 -0.0750 -0.0215 0.0336  160 ARG A CB  
1206 C CG  . ARG A 174 ? 0.4454 0.5399 0.7462 -0.0690 -0.0136 0.0264  160 ARG A CG  
1207 C CD  . ARG A 174 ? 0.3292 0.4345 0.6391 -0.0611 -0.0205 0.0282  160 ARG A CD  
1208 N NE  . ARG A 174 ? 0.5766 0.7091 0.9095 -0.0522 -0.0157 0.0193  160 ARG A NE  
1209 C CZ  . ARG A 174 ? 0.7022 0.8557 1.0467 -0.0495 -0.0204 0.0168  160 ARG A CZ  
1210 N NH1 . ARG A 174 ? 0.5351 0.6851 0.8692 -0.0568 -0.0290 0.0235  160 ARG A NH1 
1211 N NH2 . ARG A 174 ? 0.7279 0.9067 1.0951 -0.0385 -0.0174 0.0061  160 ARG A NH2 
1212 N N   . ARG A 175 ? 0.2975 0.3122 0.5506 -0.0546 -0.0420 0.0442  161 ARG A N   
1213 C CA  . ARG A 175 ? 0.3182 0.3150 0.5561 -0.0554 -0.0519 0.0440  161 ARG A CA  
1214 C C   . ARG A 175 ? 0.3420 0.3360 0.5800 -0.0464 -0.0593 0.0458  161 ARG A C   
1215 O O   . ARG A 175 ? 0.2637 0.2662 0.5117 -0.0394 -0.0551 0.0481  161 ARG A O   
1216 C CB  . ARG A 175 ? 0.3528 0.3415 0.5880 -0.0526 -0.0461 0.0391  161 ARG A CB  
1217 C CG  . ARG A 175 ? 0.2942 0.2782 0.5210 -0.0640 -0.0453 0.0373  161 ARG A CG  
1218 C CD  . ARG A 175 ? 0.3125 0.2889 0.5361 -0.0610 -0.0412 0.0320  161 ARG A CD  
1219 N NE  . ARG A 175 ? 0.3017 0.2640 0.5095 -0.0697 -0.0505 0.0302  161 ARG A NE  
1220 C CZ  . ARG A 175 ? 0.3005 0.2579 0.5043 -0.0718 -0.0466 0.0259  161 ARG A CZ  
1221 N NH1 . ARG A 175 ? 0.2714 0.2373 0.4858 -0.0668 -0.0326 0.0226  161 ARG A NH1 
1222 N NH2 . ARG A 175 ? 0.2756 0.2168 0.4623 -0.0796 -0.0582 0.0249  161 ARG A NH2 
1223 N N   . PRO A 176 ? 0.3102 0.2916 0.5363 -0.0464 -0.0715 0.0442  162 PRO A N   
1224 C CA  . PRO A 176 ? 0.2416 0.2225 0.4675 -0.0394 -0.0790 0.0448  162 PRO A CA  
1225 C C   . PRO A 176 ? 0.2510 0.2359 0.4828 -0.0303 -0.0718 0.0420  162 PRO A C   
1226 O O   . PRO A 176 ? 0.2727 0.2567 0.5051 -0.0290 -0.0637 0.0375  162 PRO A O   
1227 C CB  . PRO A 176 ? 0.3155 0.2811 0.5271 -0.0405 -0.0945 0.0406  162 PRO A CB  
1228 C CG  . PRO A 176 ? 0.3655 0.3206 0.5670 -0.0496 -0.0970 0.0401  162 PRO A CG  
1229 C CD  . PRO A 176 ? 0.2912 0.2571 0.5025 -0.0522 -0.0808 0.0408  162 PRO A CD  
1230 N N   . GLY A 177 ? 0.2774 0.2661 0.5113 -0.0260 -0.0748 0.0447  163 GLY A N   
1231 C CA  . GLY A 177 ? 0.2781 0.2682 0.5117 -0.0208 -0.0707 0.0419  163 GLY A CA  
1232 C C   . GLY A 177 ? 0.3281 0.3185 0.5567 -0.0186 -0.0812 0.0383  163 GLY A C   
1233 O O   . GLY A 177 ? 0.2355 0.2227 0.4612 -0.0197 -0.0923 0.0394  163 GLY A O   
1234 N N   . TYR A 178 ? 0.2839 0.2777 0.5099 -0.0167 -0.0777 0.0334  164 TYR A N   
1235 C CA  . TYR A 178 ? 0.2689 0.2671 0.4912 -0.0148 -0.0862 0.0260  164 TYR A CA  
1236 C C   . TYR A 178 ? 0.3283 0.3310 0.5472 -0.0163 -0.0810 0.0279  164 TYR A C   
1237 O O   . TYR A 178 ? 0.3103 0.3124 0.5252 -0.0195 -0.0707 0.0274  164 TYR A O   
1238 C CB  . TYR A 178 ? 0.2819 0.2836 0.5024 -0.0132 -0.0887 0.0111  164 TYR A CB  
1239 C CG  . TYR A 178 ? 0.3439 0.3550 0.5629 -0.0098 -0.0972 -0.0017 164 TYR A CG  
1240 C CD1 . TYR A 178 ? 0.3218 0.3452 0.5387 -0.0131 -0.0905 -0.0067 164 TYR A CD1 
1241 C CD2 . TYR A 178 ? 0.2734 0.2804 0.4915 -0.0041 -0.1128 -0.0103 164 TYR A CD2 
1242 C CE1 . TYR A 178 ? 0.3207 0.3575 0.5377 -0.0110 -0.0973 -0.0210 164 TYR A CE1 
1243 C CE2 . TYR A 178 ? 0.2985 0.3161 0.5172 0.0008  -0.1215 -0.0249 164 TYR A CE2 
1244 C CZ  . TYR A 178 ? 0.3810 0.4163 0.6008 -0.0027 -0.1129 -0.0310 164 TYR A CZ  
1245 O OH  . TYR A 178 ? 0.2941 0.3445 0.5158 0.0012  -0.1206 -0.0480 164 TYR A OH  
1246 N N   . LEU A 179 ? 0.2364 0.2415 0.4541 -0.0154 -0.0886 0.0301  165 LEU A N   
1247 C CA  . LEU A 179 ? 0.3126 0.3207 0.5239 -0.0184 -0.0856 0.0317  165 LEU A CA  
1248 C C   . LEU A 179 ? 0.3588 0.3769 0.5678 -0.0183 -0.0934 0.0211  165 LEU A C   
1249 O O   . LEU A 179 ? 0.3585 0.3760 0.5707 -0.0145 -0.1043 0.0216  165 LEU A O   
1250 C CB  . LEU A 179 ? 0.2466 0.2487 0.4588 -0.0172 -0.0873 0.0457  165 LEU A CB  
1251 C CG  . LEU A 179 ? 0.2906 0.2850 0.5063 -0.0153 -0.0808 0.0545  165 LEU A CG  
1252 C CD1 . LEU A 179 ? 0.2531 0.2459 0.4720 -0.0118 -0.0858 0.0648  165 LEU A CD1 
1253 C CD2 . LEU A 179 ? 0.2919 0.2787 0.4975 -0.0193 -0.0713 0.0530  165 LEU A CD2 
1254 N N   . MET A 180 ? 0.3402 0.3681 0.5429 -0.0236 -0.0879 0.0106  166 MET A N   
1255 C CA  . MET A 180 ? 0.3311 0.3727 0.5319 -0.0247 -0.0937 -0.0009 166 MET A CA  
1256 C C   . MET A 180 ? 0.3153 0.3539 0.5064 -0.0312 -0.0919 0.0089  166 MET A C   
1257 O O   . MET A 180 ? 0.3382 0.3702 0.5181 -0.0391 -0.0830 0.0149  166 MET A O   
1258 C CB  . MET A 180 ? 0.3112 0.3711 0.5109 -0.0286 -0.0886 -0.0209 166 MET A CB  
1259 C CG  . MET A 180 ? 0.3946 0.4731 0.5977 -0.0261 -0.0974 -0.0382 166 MET A CG  
1260 S SD  . MET A 180 ? 0.4054 0.5136 0.6024 -0.0384 -0.0873 -0.0601 166 MET A SD  
1261 C CE  . MET A 180 ? 0.2518 0.3739 0.4605 -0.0309 -0.0879 -0.0804 166 MET A CE  
1262 N N   . LEU A 181 ? 0.3031 0.3434 0.4961 -0.0282 -0.1016 0.0113  167 LEU A N   
1263 C CA  . LEU A 181 ? 0.3519 0.3879 0.5361 -0.0333 -0.1022 0.0219  167 LEU A CA  
1264 C C   . LEU A 181 ? 0.2852 0.3367 0.4657 -0.0374 -0.1065 0.0098  167 LEU A C   
1265 O O   . LEU A 181 ? 0.3285 0.3829 0.5151 -0.0316 -0.1169 0.0082  167 LEU A O   
1266 C CB  . LEU A 181 ? 0.3757 0.4008 0.5662 -0.0268 -0.1093 0.0372  167 LEU A CB  
1267 C CG  . LEU A 181 ? 0.4362 0.4563 0.6190 -0.0299 -0.1122 0.0485  167 LEU A CG  
1268 C CD1 . LEU A 181 ? 0.3117 0.3194 0.4810 -0.0358 -0.1049 0.0561  167 LEU A CD1 
1269 C CD2 . LEU A 181 ? 0.3764 0.3928 0.5688 -0.0230 -0.1198 0.0595  167 LEU A CD2 
1270 N N   . PRO A 182 ? 0.4030 0.4653 0.5721 -0.0488 -0.0987 0.0002  168 PRO A N   
1271 C CA  . PRO A 182 ? 0.3493 0.4294 0.5142 -0.0548 -0.1017 -0.0119 168 PRO A CA  
1272 C C   . PRO A 182 ? 0.3868 0.4566 0.5457 -0.0557 -0.1082 0.0028  168 PRO A C   
1273 O O   . PRO A 182 ? 0.4352 0.4861 0.5862 -0.0574 -0.1071 0.0208  168 PRO A O   
1274 C CB  . PRO A 182 ? 0.3798 0.4703 0.5288 -0.0716 -0.0896 -0.0211 168 PRO A CB  
1275 C CG  . PRO A 182 ? 0.3199 0.4036 0.4705 -0.0707 -0.0817 -0.0206 168 PRO A CG  
1276 C CD  . PRO A 182 ? 0.3689 0.4287 0.5271 -0.0587 -0.0865 -0.0012 168 PRO A CD  
1277 N N   . ALA A 183 ? 0.3789 0.4618 0.5421 -0.0537 -0.1162 -0.0063 169 ALA A N   
1278 C CA  . ALA A 183 ? 0.4003 0.4752 0.5599 -0.0534 -0.1236 0.0066  169 ALA A CA  
1279 C C   . ALA A 183 ? 0.3877 0.4545 0.5271 -0.0672 -0.1184 0.0173  169 ALA A C   
1280 O O   . ALA A 183 ? 0.4302 0.4810 0.5652 -0.0654 -0.1232 0.0347  169 ALA A O   
1281 C CB  . ALA A 183 ? 0.4557 0.5467 0.6217 -0.0501 -0.1327 -0.0075 169 ALA A CB  
1282 N N   . ASP A 184 ? 0.4016 0.4787 0.5267 -0.0819 -0.1094 0.0065  170 ASP A N   
1283 C CA  . ASP A 184 ? 0.4788 0.5423 0.5779 -0.0980 -0.1060 0.0173  170 ASP A CA  
1284 C C   . ASP A 184 ? 0.4591 0.4935 0.5493 -0.0962 -0.1042 0.0356  170 ASP A C   
1285 O O   . ASP A 184 ? 0.5885 0.6011 0.6622 -0.1000 -0.1088 0.0515  170 ASP A O   
1286 C CB  . ASP A 184 ? 0.3684 0.4511 0.4511 -0.1181 -0.0962 -0.0001 170 ASP A CB  
1287 C CG  . ASP A 184 ? 0.4849 0.5743 0.5695 -0.1209 -0.0861 -0.0108 170 ASP A CG  
1288 O OD1 . ASP A 184 ? 0.5025 0.5958 0.6094 -0.1044 -0.0880 -0.0150 170 ASP A OD1 
1289 O OD2 . ASP A 184 ? 0.5414 0.6315 0.6032 -0.1409 -0.0766 -0.0150 170 ASP A OD2 
1290 N N   . VAL A 185 ? 0.4131 0.4459 0.5136 -0.0894 -0.0989 0.0328  171 VAL A N   
1291 C CA  . VAL A 185 ? 0.4943 0.5008 0.5886 -0.0861 -0.0974 0.0479  171 VAL A CA  
1292 C C   . VAL A 185 ? 0.6130 0.6067 0.7200 -0.0707 -0.1073 0.0634  171 VAL A C   
1293 O O   . VAL A 185 ? 0.4955 0.4663 0.5923 -0.0690 -0.1109 0.0775  171 VAL A O   
1294 C CB  . VAL A 185 ? 0.4541 0.4654 0.5587 -0.0824 -0.0891 0.0397  171 VAL A CB  
1295 C CG1 . VAL A 185 ? 0.4204 0.4057 0.5220 -0.0765 -0.0884 0.0542  171 VAL A CG1 
1296 C CG2 . VAL A 185 ? 0.4486 0.4742 0.5389 -0.0995 -0.0787 0.0237  171 VAL A CG2 
1297 N N   . ALA A 186 ? 0.4657 0.4742 0.5943 -0.0597 -0.1129 0.0597  172 ALA A N   
1298 C CA  . ALA A 186 ? 0.4155 0.4175 0.5572 -0.0474 -0.1213 0.0720  172 ALA A CA  
1299 C C   . ALA A 186 ? 0.4399 0.4314 0.5694 -0.0499 -0.1289 0.0837  172 ALA A C   
1300 O O   . ALA A 186 ? 0.5018 0.4843 0.6378 -0.0407 -0.1350 0.0949  172 ALA A O   
1301 C CB  . ALA A 186 ? 0.3048 0.3224 0.4651 -0.0398 -0.1266 0.0652  172 ALA A CB  
1302 N N   . LYS A 187 ? 0.4825 0.4768 0.5947 -0.0623 -0.1291 0.0801  173 LYS A N   
1303 C CA  . LYS A 187 ? 0.5331 0.5161 0.6307 -0.0661 -0.1374 0.0910  173 LYS A CA  
1304 C C   . LYS A 187 ? 0.5822 0.5374 0.6527 -0.0742 -0.1379 0.1009  173 LYS A C   
1305 O O   . LYS A 187 ? 0.5200 0.4601 0.5755 -0.0764 -0.1471 0.1114  173 LYS A O   
1306 C CB  . LYS A 187 ? 0.4420 0.4412 0.5320 -0.0771 -0.1382 0.0821  173 LYS A CB  
1307 C CG  . LYS A 187 ? 0.4787 0.4974 0.5908 -0.0678 -0.1434 0.0759  173 LYS A CG  
1308 C CD  . LYS A 187 ? 0.7083 0.7492 0.8217 -0.0747 -0.1395 0.0567  173 LYS A CD  
1309 C CE  . LYS A 187 ? 0.8212 0.8692 0.9207 -0.0860 -0.1430 0.0546  173 LYS A CE  
1310 N NZ  . LYS A 187 ? 0.8839 0.9579 0.9898 -0.0894 -0.1411 0.0330  173 LYS A NZ  
1311 N N   . LYS A 188 ? 0.5400 0.4855 0.6017 -0.0791 -0.1296 0.0980  174 LYS A N   
1312 C CA  . LYS A 188 ? 0.4919 0.4056 0.5223 -0.0890 -0.1312 0.1071  174 LYS A CA  
1313 C C   . LYS A 188 ? 0.6186 0.5083 0.6515 -0.0733 -0.1431 0.1216  174 LYS A C   
1314 O O   . LYS A 188 ? 0.5138 0.4134 0.5750 -0.0557 -0.1446 0.1221  174 LYS A O   
1315 C CB  . LYS A 188 ? 0.5688 0.4785 0.5905 -0.0975 -0.1194 0.1000  174 LYS A CB  
1316 C CG  . LYS A 188 ? 0.7284 0.6582 0.7373 -0.1180 -0.1087 0.0848  174 LYS A CG  
1317 C CD  . LYS A 188 ? 0.7040 0.6273 0.6837 -0.1364 -0.1131 0.0875  174 LYS A CD  
1318 C CE  . LYS A 188 ? 0.7376 0.6769 0.6965 -0.1618 -0.1012 0.0721  174 LYS A CE  
1319 N NZ  . LYS A 188 ? 0.6128 0.5942 0.6017 -0.1566 -0.0925 0.0512  174 LYS A NZ  
1320 N N   . ALA A 189 ? 0.6174 0.4756 0.6192 -0.0804 -0.1526 0.1323  175 ALA A N   
1321 C CA  . ALA A 189 ? 0.7406 0.5751 0.7433 -0.0639 -0.1672 0.1441  175 ALA A CA  
1322 C C   . ALA A 189 ? 0.6189 0.4430 0.6331 -0.0509 -0.1647 0.1438  175 ALA A C   
1323 O O   . ALA A 189 ? 0.6364 0.4516 0.6382 -0.0605 -0.1549 0.1398  175 ALA A O   
1324 C CB  . ALA A 189 ? 0.7135 0.5091 0.6740 -0.0754 -0.1797 0.1550  175 ALA A CB  
1325 N N   . ALA A 190 ? 0.6746 0.5029 0.7137 -0.0295 -0.1733 0.1466  176 ALA A N   
1326 C CA  . ALA A 190 ? 0.5688 0.3882 0.6203 -0.0152 -0.1731 0.1456  176 ALA A CA  
1327 C C   . ALA A 190 ? 0.5627 0.3698 0.6211 0.0043  -0.1909 0.1513  176 ALA A C   
1328 O O   . ALA A 190 ? 0.6668 0.4736 0.7213 0.0063  -0.2026 0.1563  176 ALA A O   
1329 C CB  . ALA A 190 ? 0.4868 0.3410 0.5738 -0.0087 -0.1600 0.1360  176 ALA A CB  
1330 N N   . THR A 191 ? 0.5312 0.3289 0.6000 0.0192  -0.1936 0.1492  177 THR A N   
1331 C CA  . THR A 191 ? 0.5663 0.3564 0.6462 0.0408  -0.2109 0.1504  177 THR A CA  
1332 C C   . THR A 191 ? 0.5713 0.3966 0.6938 0.0572  -0.2048 0.1403  177 THR A C   
1333 O O   . THR A 191 ? 0.4998 0.3316 0.6307 0.0546  -0.1913 0.1349  177 THR A O   
1334 C CB  . THR A 191 ? 0.7387 0.4776 0.7858 0.0447  -0.2244 0.1559  177 THR A CB  
1335 O OG1 . THR A 191 ? 0.8719 0.6081 0.9292 0.0515  -0.2165 0.1496  177 THR A OG1 
1336 C CG2 . THR A 191 ? 0.7167 0.4202 0.7159 0.0201  -0.2239 0.1646  177 THR A CG2 
1337 N N   . PRO A 192 ? 0.6029 0.4535 0.7521 0.0722  -0.2138 0.1367  178 PRO A N   
1338 C CA  . PRO A 192 ? 0.5446 0.4317 0.7328 0.0849  -0.2077 0.1256  178 PRO A CA  
1339 C C   . PRO A 192 ? 0.5888 0.4588 0.7786 0.0981  -0.2102 0.1200  178 PRO A C   
1340 O O   . PRO A 192 ? 0.5939 0.4332 0.7616 0.1066  -0.2219 0.1201  178 PRO A O   
1341 C CB  . PRO A 192 ? 0.5654 0.4790 0.7717 0.0960  -0.2172 0.1209  178 PRO A CB  
1342 C CG  . PRO A 192 ? 0.6317 0.5283 0.8124 0.0861  -0.2249 0.1308  178 PRO A CG  
1343 C CD  . PRO A 192 ? 0.5397 0.3885 0.6817 0.0764  -0.2280 0.1402  178 PRO A CD  
1344 N N   . PRO A 193 ? 0.5713 0.4610 0.7809 0.0977  -0.1959 0.1123  179 PRO A N   
1345 C CA  . PRO A 193 ? 0.5772 0.4519 0.7898 0.1105  -0.1981 0.1059  179 PRO A CA  
1346 C C   . PRO A 193 ? 0.6784 0.5757 0.9146 0.1314  -0.2074 0.0931  179 PRO A C   
1347 O O   . PRO A 193 ? 0.5484 0.4876 0.8126 0.1344  -0.2058 0.0865  179 PRO A O   
1348 C CB  . PRO A 193 ? 0.4942 0.3904 0.7211 0.1006  -0.1772 0.1002  179 PRO A CB  
1349 C CG  . PRO A 193 ? 0.4950 0.4196 0.7296 0.0853  -0.1665 0.1024  179 PRO A CG  
1350 C CD  . PRO A 193 ? 0.4935 0.4204 0.7237 0.0863  -0.1788 0.1079  179 PRO A CD  
1351 N N   . VAL A 194 ? 0.6357 0.5054 0.8578 0.1446  -0.2166 0.0885  180 VAL A N   
1352 C CA  . VAL A 194 ? 0.6225 0.5145 0.8663 0.1655  -0.2251 0.0735  180 VAL A CA  
1353 C C   . VAL A 194 ? 0.6400 0.5753 0.9232 0.1707  -0.2135 0.0593  180 VAL A C   
1354 O O   . VAL A 194 ? 0.8134 0.7920 1.1268 0.1799  -0.2142 0.0463  180 VAL A O   
1355 C CB  . VAL A 194 ? 0.7094 0.5572 0.9259 0.1781  -0.2394 0.0718  180 VAL A CB  
1356 C CG1 . VAL A 194 ? 0.6959 0.5698 0.9389 0.2007  -0.2475 0.0535  180 VAL A CG1 
1357 C CG2 . VAL A 194 ? 0.6370 0.4461 0.8157 0.1723  -0.2526 0.0842  180 VAL A CG2 
1358 N N   . ASN A 195 ? 0.6044 0.5300 0.8873 0.1634  -0.2022 0.0610  181 ASN A N   
1359 C CA  . ASN A 195 ? 0.5944 0.5564 0.9115 0.1669  -0.1909 0.0476  181 ASN A CA  
1360 C C   . ASN A 195 ? 0.6590 0.6442 0.9853 0.1460  -0.1725 0.0529  181 ASN A C   
1361 O O   . ASN A 195 ? 0.6111 0.5700 0.9110 0.1299  -0.1651 0.0654  181 ASN A O   
1362 C CB  . ASN A 195 ? 0.6911 0.6250 0.9984 0.1750  -0.1905 0.0426  181 ASN A CB  
1363 C CG  . ASN A 195 ? 0.7451 0.6758 1.0538 0.1967  -0.2041 0.0290  181 ASN A CG  
1364 O OD1 . ASN A 195 ? 0.8157 0.7090 1.0953 0.2028  -0.2188 0.0346  181 ASN A OD1 
1365 N ND2 . ASN A 195 ? 0.7494 0.7204 1.0918 0.2075  -0.1997 0.0102  181 ASN A ND2 
1366 N N   . ALA A 196 ? 0.4766 0.5113 0.8340 0.1433  -0.1635 0.0416  182 ALA A N   
1367 C CA  . ALA A 196 ? 0.5082 0.5631 0.8676 0.1216  -0.1455 0.0448  182 ALA A CA  
1368 C C   . ALA A 196 ? 0.7091 0.7477 1.0592 0.1138  -0.1320 0.0452  182 ALA A C   
1369 O O   . ALA A 196 ? 0.5165 0.5475 0.8718 0.1252  -0.1328 0.0371  182 ALA A O   
1370 C CB  . ALA A 196 ? 0.5543 0.6631 0.9450 0.1186  -0.1402 0.0319  182 ALA A CB  
1371 N N   . LEU A 197 ? 0.5844 0.6168 0.9201 0.0950  -0.1207 0.0540  183 LEU A N   
1372 C CA  . LEU A 197 ? 0.4537 0.4744 0.7812 0.0859  -0.1075 0.0541  183 LEU A CA  
1373 C C   . LEU A 197 ? 0.5699 0.6229 0.9223 0.0866  -0.0986 0.0407  183 LEU A C   
1374 O O   . LEU A 197 ? 0.6119 0.7005 0.9815 0.0795  -0.0949 0.0352  183 LEU A O   
1375 C CB  . LEU A 197 ? 0.4487 0.4653 0.7614 0.0672  -0.0989 0.0626  183 LEU A CB  
1376 C CG  . LEU A 197 ? 0.5091 0.5011 0.8027 0.0582  -0.0895 0.0663  183 LEU A CG  
1377 C CD1 . LEU A 197 ? 0.4601 0.4136 0.7286 0.0620  -0.0960 0.0732  183 LEU A CD1 
1378 C CD2 . LEU A 197 ? 0.4039 0.4020 0.6904 0.0424  -0.0829 0.0701  183 LEU A CD2 
1379 N N   . THR A 198 ? 0.6465 0.6868 0.9989 0.0933  -0.0949 0.0352  184 THR A N   
1380 C CA  . THR A 198 ? 0.7032 0.7734 1.0781 0.0935  -0.0858 0.0212  184 THR A CA  
1381 C C   . THR A 198 ? 0.7344 0.7838 1.0972 0.0874  -0.0748 0.0223  184 THR A C   
1382 O O   . THR A 198 ? 0.7926 0.8032 1.1324 0.0893  -0.0772 0.0305  184 THR A O   
1383 C CB  . THR A 198 ? 0.6923 0.7791 1.0896 0.1147  -0.0959 0.0064  184 THR A CB  
1384 O OG1 . THR A 198 ? 0.9199 1.0303 1.3357 0.1151  -0.0860 -0.0083 184 THR A OG1 
1385 C CG2 . THR A 198 ? 0.7528 0.7957 1.1325 0.1321  -0.1105 0.0111  184 THR A CG2 
1386 N N   . LEU A 199 ? 0.7476 0.8234 1.1245 0.0784  -0.0626 0.0135  185 LEU A N   
1387 C CA  . LEU A 199 ? 0.8342 0.8951 1.2012 0.0704  -0.0510 0.0140  185 LEU A CA  
1388 C C   . LEU A 199 ? 0.8223 0.8775 1.1977 0.0848  -0.0512 0.0030  185 LEU A C   
1389 O O   . LEU A 199 ? 0.9527 0.9755 1.3104 0.0852  -0.0485 0.0073  185 LEU A O   
1390 C CB  . LEU A 199 ? 0.9083 0.9958 1.2815 0.0516  -0.0389 0.0113  185 LEU A CB  
1391 C CG  . LEU A 199 ? 0.7723 0.8462 1.1343 0.0411  -0.0271 0.0125  185 LEU A CG  
1392 C CD1 . LEU A 199 ? 0.6285 0.6662 0.9650 0.0376  -0.0279 0.0249  185 LEU A CD1 
1393 C CD2 . LEU A 199 ? 0.5402 0.6384 0.9060 0.0223  -0.0185 0.0099  185 LEU A CD2 
1394 N N   . ARG A 200 ? 0.8898 0.9772 1.2917 0.0963  -0.0545 -0.0126 186 ARG A N   
1395 C CA  . ARG A 200 ? 1.0620 1.1449 1.4740 0.1133  -0.0573 -0.0258 186 ARG A CA  
1396 C C   . ARG A 200 ? 0.9965 1.0750 1.4045 0.1034  -0.0426 -0.0288 186 ARG A C   
1397 O O   . ARG A 200 ? 1.0857 1.1243 1.4718 0.1044  -0.0422 -0.0212 186 ARG A O   
1398 C CB  . ARG A 200 ? 1.1371 1.1740 1.5304 0.1312  -0.0735 -0.0194 186 ARG A CB  
1399 C CG  . ARG A 200 ? 0.9883 1.0351 1.3937 0.1487  -0.0911 -0.0240 186 ARG A CG  
1400 C CD  . ARG A 200 ? 1.0779 1.0759 1.4529 0.1537  -0.1056 -0.0079 186 ARG A CD  
1401 N NE  . ARG A 200 ? 1.1902 1.1587 1.5605 0.1776  -0.1242 -0.0141 186 ARG A NE  
1402 C CZ  . ARG A 200 ? 1.2033 1.1185 1.5405 0.1823  -0.1383 -0.0014 186 ARG A CZ  
1403 N NH1 . ARG A 200 ? 1.1098 0.9997 1.4179 0.1642  -0.1343 0.0171  186 ARG A NH1 
1404 N NH2 . ARG A 200 ? 1.1133 1.0005 1.4421 0.2032  -0.1562 -0.0082 186 ARG A NH2 
1405 N N   . HIS A 201 ? 0.8018 0.9208 1.2283 0.0913  -0.0305 -0.0395 187 HIS A N   
1406 C CA  . HIS A 201 ? 0.8568 0.9772 1.2798 0.0778  -0.0155 -0.0419 187 HIS A CA  
1407 C C   . HIS A 201 ? 0.8753 0.9606 1.2866 0.0880  -0.0153 -0.0426 187 HIS A C   
1408 O O   . HIS A 201 ? 0.7273 0.8047 1.1468 0.1087  -0.0250 -0.0525 187 HIS A O   
1409 C CB  . HIS A 201 ? 0.7459 0.9168 1.1960 0.0722  -0.0068 -0.0612 187 HIS A CB  
1410 C CG  . HIS A 201 ? 0.9303 1.1395 1.3908 0.0581  -0.0055 -0.0631 187 HIS A CG  
1411 N ND1 . HIS A 201 ? 0.8482 1.0591 1.2939 0.0336  0.0022  -0.0526 187 HIS A ND1 
1412 C CD2 . HIS A 201 ? 0.7551 1.0023 1.2380 0.0643  -0.0116 -0.0755 187 HIS A CD2 
1413 C CE1 . HIS A 201 ? 0.9111 1.1560 1.3670 0.0239  0.0008  -0.0570 187 HIS A CE1 
1414 N NE2 . HIS A 201 ? 0.9153 1.1853 1.3947 0.0416  -0.0065 -0.0712 187 HIS A NE2 
1415 N N   . ALA A 202 ? 0.7214 0.7847 1.1129 0.0738  -0.0052 -0.0331 188 ALA A N   
1416 C CA  . ALA A 202 ? 0.7458 0.7765 1.1239 0.0795  -0.0031 -0.0335 188 ALA A CA  
1417 C C   . ALA A 202 ? 0.6256 0.6822 1.0239 0.0813  0.0058  -0.0512 188 ALA A C   
1418 O O   . ALA A 202 ? 0.5626 0.6628 0.9824 0.0738  0.0124  -0.0620 188 ALA A O   
1419 C CB  . ALA A 202 ? 0.7138 0.7168 1.0650 0.0631  0.0049  -0.0191 188 ALA A CB  
1420 N N   . HIS A 203 ? 0.5357 0.5649 0.9253 0.0899  0.0060  -0.0548 189 HIS A N   
1421 C CA  . HIS A 203 ? 0.4173 0.4674 0.8248 0.0930  0.0141  -0.0725 189 HIS A CA  
1422 C C   . HIS A 203 ? 0.3914 0.4146 0.7787 0.0818  0.0251  -0.0667 189 HIS A C   
1423 O O   . HIS A 203 ? 0.4229 0.4019 0.7830 0.0821  0.0212  -0.0540 189 HIS A O   
1424 C CB  . HIS A 203 ? 0.3716 0.4186 0.7938 0.1200  0.0004  -0.0885 189 HIS A CB  
1425 C CG  . HIS A 203 ? 0.7425 0.8130 1.1834 0.1336  -0.0129 -0.0946 189 HIS A CG  
1426 N ND1 . HIS A 203 ? 0.7559 0.8832 1.2309 0.1357  -0.0102 -0.1142 189 HIS A ND1 
1427 C CD2 . HIS A 203 ? 0.8144 0.8610 1.2440 0.1442  -0.0288 -0.0842 189 HIS A CD2 
1428 C CE1 . HIS A 203 ? 0.6866 0.8248 1.1719 0.1484  -0.0241 -0.1161 189 HIS A CE1 
1429 N NE2 . HIS A 203 ? 0.8393 0.9279 1.2974 0.1542  -0.0359 -0.0975 189 HIS A NE2 
1430 N N   . ALA A 204 ? 0.3602 0.4113 0.7593 0.0697  0.0392  -0.0761 190 ALA A N   
1431 C CA  . ALA A 204 ? 0.3735 0.4031 0.7568 0.0605  0.0498  -0.0736 190 ALA A CA  
1432 C C   . ALA A 204 ? 0.3575 0.3575 0.7365 0.0792  0.0432  -0.0817 190 ALA A C   
1433 O O   . ALA A 204 ? 0.3719 0.3821 0.7694 0.0991  0.0333  -0.0963 190 ALA A O   
1434 C CB  . ALA A 204 ? 0.3680 0.4350 0.7654 0.0440  0.0650  -0.0834 190 ALA A CB  
1435 N N   . ASP A 205 ? 0.3824 0.3440 0.7354 0.0730  0.0474  -0.0729 191 ASP A N   
1436 C CA  . ASP A 205 ? 0.4013 0.3337 0.7470 0.0863  0.0436  -0.0814 191 ASP A CA  
1437 C C   . ASP A 205 ? 0.3937 0.3647 0.7692 0.0914  0.0509  -0.1034 191 ASP A C   
1438 O O   . ASP A 205 ? 0.3748 0.3806 0.7617 0.0742  0.0657  -0.1068 191 ASP A O   
1439 C CB  . ASP A 205 ? 0.4105 0.3054 0.7247 0.0719  0.0517  -0.0697 191 ASP A CB  
1440 C CG  . ASP A 205 ? 0.4510 0.3032 0.7481 0.0841  0.0449  -0.0747 191 ASP A CG  
1441 O OD1 . ASP A 205 ? 0.4532 0.3164 0.7632 0.0882  0.0511  -0.0893 191 ASP A OD1 
1442 O OD2 . ASP A 205 ? 0.4831 0.2893 0.7517 0.0886  0.0327  -0.0641 191 ASP A OD2 
1443 N N   . SER A 206 ? 0.3849 0.2916 0.7329 0.0455  0.0905  0.0397  192 SER A N   
1444 C CA  . SER A 206 ? 0.3947 0.3024 0.7566 0.0491  0.0941  0.0325  192 SER A CA  
1445 C C   . SER A 206 ? 0.3958 0.2965 0.7566 0.0431  0.1022  0.0196  192 SER A C   
1446 O O   . SER A 206 ? 0.4101 0.3148 0.7729 0.0433  0.1050  0.0107  192 SER A O   
1447 C CB  . SER A 206 ? 0.3552 0.2543 0.7335 0.0577  0.0950  0.0402  192 SER A CB  
1448 O OG  . SER A 206 ? 0.4141 0.2966 0.7917 0.0574  0.0986  0.0462  192 SER A OG  
1449 N N   . ALA A 207 ? 0.4330 0.3226 0.7898 0.0373  0.1058  0.0184  193 ALA A N   
1450 C CA  . ALA A 207 ? 0.3750 0.2583 0.7291 0.0305  0.1107  0.0054  193 ALA A CA  
1451 C C   . ALA A 207 ? 0.3388 0.2355 0.6807 0.0251  0.1064  -0.0018 193 ALA A C   
1452 O O   . ALA A 207 ? 0.3386 0.2344 0.6763 0.0226  0.1082  -0.0129 193 ALA A O   
1453 C CB  . ALA A 207 ? 0.3667 0.2363 0.7228 0.0249  0.1145  0.0062  193 ALA A CB  
1454 N N   . CYS A 208 ? 0.3287 0.2365 0.6635 0.0236  0.1008  0.0045  194 CYS A N   
1455 C CA  . CYS A 208 ? 0.3678 0.2882 0.6922 0.0195  0.0964  -0.0013 194 CYS A CA  
1456 C C   . CYS A 208 ? 0.3739 0.3023 0.6964 0.0235  0.0949  -0.0049 194 CYS A C   
1457 O O   . CYS A 208 ? 0.3986 0.3297 0.7139 0.0204  0.0949  -0.0140 194 CYS A O   
1458 C CB  . CYS A 208 ? 0.3809 0.3098 0.6984 0.0184  0.0921  0.0067  194 CYS A CB  
1459 S SG  . CYS A 208 ? 0.5966 0.5406 0.9026 0.0147  0.0868  0.0008  194 CYS A SG  
1460 N N   . LEU A 209 ? 0.4817 0.4139 0.8111 0.0302  0.0934  0.0024  195 LEU A N   
1461 C CA  . LEU A 209 ? 0.3445 0.2847 0.6766 0.0336  0.0932  -0.0006 195 LEU A CA  
1462 C C   . LEU A 209 ? 0.3473 0.2784 0.6834 0.0342  0.1016  -0.0099 195 LEU A C   
1463 O O   . LEU A 209 ? 0.4151 0.3495 0.7446 0.0329  0.1036  -0.0171 195 LEU A O   
1464 C CB  . LEU A 209 ? 0.4402 0.3865 0.7836 0.0406  0.0891  0.0092  195 LEU A CB  
1465 C CG  . LEU A 209 ? 0.3246 0.2822 0.6744 0.0435  0.0880  0.0075  195 LEU A CG  
1466 C CD1 . LEU A 209 ? 0.2771 0.2449 0.6128 0.0389  0.0830  0.0049  195 LEU A CD1 
1467 C CD2 . LEU A 209 ? 0.4288 0.3920 0.7946 0.0504  0.0827  0.0170  195 LEU A CD2 
1468 N N   . LYS A 210 ? 0.3721 0.2897 0.7169 0.0360  0.1072  -0.0100 196 LYS A N   
1469 C CA  . LYS A 210 ? 0.3333 0.2391 0.6798 0.0368  0.1163  -0.0197 196 LYS A CA  
1470 C C   . LYS A 210 ? 0.3367 0.2376 0.6657 0.0294  0.1168  -0.0313 196 LYS A C   
1471 O O   . LYS A 210 ? 0.4014 0.2979 0.7231 0.0295  0.1221  -0.0399 196 LYS A O   
1472 C CB  . LYS A 210 ? 0.3981 0.2883 0.7564 0.0397  0.1219  -0.0177 196 LYS A CB  
1473 C CG  . LYS A 210 ? 0.4742 0.3488 0.8324 0.0403  0.1322  -0.0288 196 LYS A CG  
1474 C CD  . LYS A 210 ? 0.7133 0.5875 1.0890 0.0496  0.1395  -0.0262 196 LYS A CD  
1475 C CE  . LYS A 210 ? 0.6324 0.4909 1.0044 0.0504  0.1518  -0.0384 196 LYS A CE  
1476 N NZ  . LYS A 210 ? 0.6326 0.4991 0.9996 0.0518  0.1565  -0.0435 196 LYS A NZ  
1477 N N   . ALA A 211 ? 0.3505 0.2516 0.6726 0.0230  0.1113  -0.0316 197 ALA A N   
1478 C CA  . ALA A 211 ? 0.3771 0.2750 0.6845 0.0161  0.1090  -0.0421 197 ALA A CA  
1479 C C   . ALA A 211 ? 0.3459 0.2547 0.6410 0.0161  0.1059  -0.0447 197 ALA A C   
1480 O O   . ALA A 211 ? 0.4044 0.3065 0.6861 0.0142  0.1078  -0.0542 197 ALA A O   
1481 C CB  . ALA A 211 ? 0.3355 0.2354 0.6434 0.0096  0.1033  -0.0404 197 ALA A CB  
1482 N N   . PHE A 212 ? 0.3121 0.2358 0.6097 0.0182  0.1012  -0.0365 198 PHE A N   
1483 C CA  . PHE A 212 ? 0.3097 0.2427 0.5971 0.0184  0.0989  -0.0382 198 PHE A CA  
1484 C C   . PHE A 212 ? 0.3104 0.2394 0.5991 0.0227  0.1070  -0.0414 198 PHE A C   
1485 O O   . PHE A 212 ? 0.3158 0.2418 0.5904 0.0213  0.1093  -0.0481 198 PHE A O   
1486 C CB  . PHE A 212 ? 0.3062 0.2540 0.5971 0.0199  0.0926  -0.0290 198 PHE A CB  
1487 C CG  . PHE A 212 ? 0.4055 0.3621 0.6907 0.0213  0.0917  -0.0293 198 PHE A CG  
1488 C CD1 . PHE A 212 ? 0.3354 0.2928 0.6052 0.0178  0.0894  -0.0351 198 PHE A CD1 
1489 C CD2 . PHE A 212 ? 0.2871 0.2508 0.5838 0.0260  0.0925  -0.0234 198 PHE A CD2 
1490 C CE1 . PHE A 212 ? 0.3199 0.2834 0.5843 0.0189  0.0894  -0.0348 198 PHE A CE1 
1491 C CE2 . PHE A 212 ? 0.3330 0.3043 0.6266 0.0264  0.0922  -0.0237 198 PHE A CE2 
1492 C CZ  . PHE A 212 ? 0.3023 0.2728 0.5791 0.0228  0.0913  -0.0293 198 PHE A CZ  
1493 N N   . ARG A 213 ? 0.3352 0.2632 0.6409 0.0283  0.1121  -0.0365 199 ARG A N   
1494 C CA  . ARG A 213 ? 0.3467 0.2722 0.6587 0.0330  0.1215  -0.0390 199 ARG A CA  
1495 C C   . ARG A 213 ? 0.4092 0.3175 0.7075 0.0313  0.1302  -0.0504 199 ARG A C   
1496 O O   . ARG A 213 ? 0.4631 0.3688 0.7522 0.0320  0.1370  -0.0555 199 ARG A O   
1497 C CB  . ARG A 213 ? 0.3353 0.2623 0.6714 0.0398  0.1245  -0.0315 199 ARG A CB  
1498 C CG  . ARG A 213 ? 0.3749 0.3021 0.7241 0.0454  0.1350  -0.0331 199 ARG A CG  
1499 C CD  . ARG A 213 ? 0.4232 0.3509 0.7987 0.0528  0.1372  -0.0259 199 ARG A CD  
1500 N NE  . ARG A 213 ? 0.5956 0.5336 0.9912 0.0582  0.1424  -0.0232 199 ARG A NE  
1501 C CZ  . ARG A 213 ? 0.6722 0.6036 1.0738 0.0613  0.1566  -0.0295 199 ARG A CZ  
1502 N NH1 . ARG A 213 ? 0.8204 0.7331 1.2064 0.0598  0.1666  -0.0393 199 ARG A NH1 
1503 N NH2 . ARG A 213 ? 0.6701 0.6134 1.0941 0.0659  0.1611  -0.0261 199 ARG A NH2 
1504 N N   . ASP A 214 ? 0.3716 0.2667 0.6672 0.0288  0.1305  -0.0548 200 ASP A N   
1505 C CA  . ASP A 214 ? 0.3868 0.2630 0.6670 0.0267  0.1375  -0.0668 200 ASP A CA  
1506 C C   . ASP A 214 ? 0.3830 0.2579 0.6373 0.0213  0.1327  -0.0739 200 ASP A C   
1507 O O   . ASP A 214 ? 0.4320 0.2950 0.6694 0.0216  0.1400  -0.0820 200 ASP A O   
1508 C CB  . ASP A 214 ? 0.4889 0.3516 0.7725 0.0239  0.1367  -0.0700 200 ASP A CB  
1509 C CG  . ASP A 214 ? 0.5481 0.4069 0.8548 0.0302  0.1431  -0.0636 200 ASP A CG  
1510 O OD1 . ASP A 214 ? 0.5558 0.4187 0.8748 0.0372  0.1505  -0.0601 200 ASP A OD1 
1511 O OD2 . ASP A 214 ? 0.5122 0.3639 0.8262 0.0282  0.1408  -0.0618 200 ASP A OD2 
1512 N N   . ALA A 215 ? 0.3639 0.2498 0.6142 0.0168  0.1208  -0.0709 201 ALA A N   
1513 C CA  . ALA A 215 ? 0.4329 0.3182 0.6605 0.0124  0.1146  -0.0766 201 ALA A CA  
1514 C C   . ALA A 215 ? 0.4442 0.3359 0.6640 0.0154  0.1186  -0.0744 201 ALA A C   
1515 O O   . ALA A 215 ? 0.5608 0.4427 0.7584 0.0142  0.1210  -0.0811 201 ALA A O   
1516 C CB  . ALA A 215 ? 0.3535 0.2503 0.5834 0.0077  0.1019  -0.0732 201 ALA A CB  
1517 N N   . ALA A 216 ? 0.3593 0.2662 0.5966 0.0190  0.1191  -0.0650 202 ALA A N   
1518 C CA  . ALA A 216 ? 0.4189 0.3320 0.6524 0.0212  0.1233  -0.0627 202 ALA A CA  
1519 C C   . ALA A 216 ? 0.4207 0.3222 0.6522 0.0247  0.1382  -0.0674 202 ALA A C   
1520 O O   . ALA A 216 ? 0.4855 0.3822 0.7008 0.0244  0.1437  -0.0704 202 ALA A O   
1521 C CB  . ALA A 216 ? 0.4380 0.3694 0.6924 0.0238  0.1194  -0.0523 202 ALA A CB  
1522 N N   . GLU A 217 ? 0.3858 0.2813 0.6334 0.0283  0.1458  -0.0679 203 GLU A N   
1523 C CA  . GLU A 217 ? 0.5052 0.3888 0.7528 0.0324  0.1619  -0.0727 203 GLU A CA  
1524 C C   . GLU A 217 ? 0.4896 0.3520 0.7045 0.0293  0.1668  -0.0841 203 GLU A C   
1525 O O   . GLU A 217 ? 0.5488 0.4030 0.7504 0.0308  0.1784  -0.0877 203 GLU A O   
1526 C CB  . GLU A 217 ? 0.4319 0.3117 0.7034 0.0373  0.1684  -0.0713 203 GLU A CB  
1527 C CG  . GLU A 217 ? 0.5519 0.4145 0.8202 0.0412  0.1861  -0.0789 203 GLU A CG  
1528 C CD  . GLU A 217 ? 0.6402 0.5051 0.9408 0.0485  0.1941  -0.0744 203 GLU A CD  
1529 O OE1 . GLU A 217 ? 0.6878 0.5527 1.0008 0.0491  0.1871  -0.0710 203 GLU A OE1 
1530 O OE2 . GLU A 217 ? 0.6780 0.5445 0.9926 0.0537  0.2078  -0.0738 203 GLU A OE2 
1531 N N   . ASN A 218 ? 0.5630 0.4155 0.7639 0.0248  0.1581  -0.0900 204 ASN A N   
1532 C CA  . ASN A 218 ? 0.6065 0.4378 0.7739 0.0213  0.1595  -0.1014 204 ASN A CA  
1533 C C   . ASN A 218 ? 0.5993 0.4325 0.7428 0.0193  0.1560  -0.1012 204 ASN A C   
1534 O O   . ASN A 218 ? 0.7596 0.5763 0.8773 0.0198  0.1651  -0.1074 204 ASN A O   
1535 C CB  . ASN A 218 ? 0.5358 0.3599 0.6969 0.0158  0.1473  -0.1070 204 ASN A CB  
1536 C CG  . ASN A 218 ? 0.8149 0.6251 0.9871 0.0173  0.1547  -0.1118 204 ASN A CG  
1537 O OD1 . ASN A 218 ? 1.0458 0.8553 1.2270 0.0136  0.1465  -0.1125 204 ASN A OD1 
1538 N ND2 . ASN A 218 ? 0.8924 0.6910 1.0654 0.0227  0.1714  -0.1148 204 ASN A ND2 
1539 N N   . ARG A 219 ? 0.5897 0.4411 0.7397 0.0172  0.1432  -0.0940 205 ARG A N   
1540 C CA  . ARG A 219 ? 0.5380 0.3909 0.6667 0.0156  0.1388  -0.0930 205 ARG A CA  
1541 C C   . ARG A 219 ? 0.5930 0.4464 0.7224 0.0193  0.1533  -0.0895 205 ARG A C   
1542 O O   . ARG A 219 ? 0.7451 0.5855 0.8471 0.0189  0.1589  -0.0929 205 ARG A O   
1543 C CB  . ARG A 219 ? 0.4914 0.3640 0.6314 0.0134  0.1237  -0.0856 205 ARG A CB  
1544 C CG  . ARG A 219 ? 0.5595 0.4332 0.6785 0.0119  0.1176  -0.0843 205 ARG A CG  
1545 C CD  . ARG A 219 ? 0.6279 0.4824 0.7134 0.0091  0.1128  -0.0934 205 ARG A CD  
1546 N NE  . ARG A 219 ? 0.6177 0.4709 0.6811 0.0086  0.1072  -0.0914 205 ARG A NE  
1547 C CZ  . ARG A 219 ? 0.6486 0.4937 0.6959 0.0107  0.1180  -0.0899 205 ARG A CZ  
1548 N NH1 . ARG A 219 ? 0.6797 0.5182 0.7316 0.0134  0.1356  -0.0905 205 ARG A NH1 
1549 N NH2 . ARG A 219 ? 0.6850 0.5279 0.7120 0.0103  0.1117  -0.0873 205 ARG A NH2 
1550 N N   . LEU A 220 ? 0.5241 0.3921 0.6850 0.0229  0.1595  -0.0824 206 LEU A N   
1551 C CA  . LEU A 220 ? 0.5083 0.3795 0.6767 0.0260  0.1732  -0.0787 206 LEU A CA  
1552 C C   . LEU A 220 ? 0.5131 0.3650 0.6712 0.0289  0.1922  -0.0857 206 LEU A C   
1553 O O   . LEU A 220 ? 0.5918 0.4388 0.7420 0.0300  0.2052  -0.0853 206 LEU A O   
1554 C CB  . LEU A 220 ? 0.4358 0.3284 0.6431 0.0289  0.1725  -0.0696 206 LEU A CB  
1555 C CG  . LEU A 220 ? 0.5046 0.4159 0.7201 0.0266  0.1581  -0.0619 206 LEU A CG  
1556 C CD1 . LEU A 220 ? 0.4605 0.3895 0.7108 0.0294  0.1542  -0.0542 206 LEU A CD1 
1557 C CD2 . LEU A 220 ? 0.4013 0.3143 0.6058 0.0251  0.1615  -0.0596 206 LEU A CD2 
1558 N N   . ALA A 221 ? 0.4812 0.3205 0.6388 0.0300  0.1953  -0.0923 207 ALA A N   
1559 C CA  . ALA A 221 ? 0.5963 0.4160 0.7453 0.0335  0.2149  -0.0994 207 ALA A CA  
1560 C C   . ALA A 221 ? 0.5551 0.3525 0.6597 0.0312  0.2209  -0.1068 207 ALA A C   
1561 O O   . ALA A 221 ? 0.7746 0.5588 0.8702 0.0341  0.2405  -0.1099 207 ALA A O   
1562 C CB  . ALA A 221 ? 0.5513 0.3597 0.7066 0.0348  0.2156  -0.1057 207 ALA A CB  
1563 N N   . MET A 222 ? 0.7229 0.5150 0.7992 0.0262  0.2047  -0.1097 208 MET A N   
1564 C CA  . MET A 222 ? 0.8688 0.6395 0.8998 0.0240  0.2068  -0.1156 208 MET A CA  
1565 C C   . MET A 222 ? 0.7679 0.5484 0.7902 0.0225  0.2012  -0.1079 208 MET A C   
1566 O O   . MET A 222 ? 0.7498 0.5144 0.7335 0.0204  0.1970  -0.1110 208 MET A O   
1567 C CB  . MET A 222 ? 0.9097 0.6645 0.9129 0.0198  0.1919  -0.1250 208 MET A CB  
1568 C CG  . MET A 222 ? 0.8850 0.6561 0.8941 0.0155  0.1682  -0.1211 208 MET A CG  
1569 S SD  . MET A 222 ? 1.3062 1.0649 1.3088 0.0111  0.1551  -0.1320 208 MET A SD  
1570 C CE  . MET A 222 ? 0.8896 0.6665 0.8956 0.0061  0.1288  -0.1275 208 MET A CE  
1571 N N   . SER A 223 ? 0.6993 0.5039 0.7554 0.0237  0.2008  -0.0979 209 SER A N   
1572 C CA  . SER A 223 ? 0.6755 0.4885 0.7262 0.0223  0.1975  -0.0907 209 SER A CA  
1573 C C   . SER A 223 ? 0.7647 0.5659 0.8048 0.0244  0.2195  -0.0900 209 SER A C   
1574 O O   . SER A 223 ? 0.8417 0.6477 0.9082 0.0276  0.2358  -0.0888 209 SER A O   
1575 C CB  . SER A 223 ? 0.7015 0.5430 0.7912 0.0223  0.1886  -0.0813 209 SER A CB  
1576 O OG  . SER A 223 ? 0.8193 0.6679 0.9075 0.0213  0.1890  -0.0745 209 SER A OG  
1577 N N   . LYS A 224 ? 0.7566 0.5416 0.7587 0.0227  0.2206  -0.0905 210 LYS A N   
1578 C CA  . LYS A 224 ? 0.7390 0.5111 0.7285 0.0241  0.2428  -0.0890 210 LYS A CA  
1579 C C   . LYS A 224 ? 0.8499 0.6430 0.8696 0.0235  0.2459  -0.0786 210 LYS A C   
1580 O O   . LYS A 224 ? 0.8681 0.6681 0.9150 0.0254  0.2638  -0.0757 210 LYS A O   
1581 C CB  . LYS A 224 ? 0.7953 0.5392 0.7289 0.0228  0.2427  -0.0930 210 LYS A CB  
1582 C CG  . LYS A 224 ? 1.0545 0.7742 0.9633 0.0248  0.2694  -0.0955 210 LYS A CG  
1583 C CD  . LYS A 224 ? 1.0746 0.7617 0.9215 0.0238  0.2666  -0.1013 210 LYS A CD  
1584 C CE  . LYS A 224 ? 1.1792 0.8569 1.0013 0.0230  0.2731  -0.0936 210 LYS A CE  
1585 N NZ  . LYS A 224 ? 1.1304 0.7720 0.9012 0.0243  0.2925  -0.0980 210 LYS A NZ  
1586 N N   . ARG A 225 ? 0.7489 0.5520 0.7653 0.0209  0.2287  -0.0731 211 ARG A N   
1587 C CA  . ARG A 225 ? 0.6256 0.4485 0.6701 0.0196  0.2279  -0.0640 211 ARG A CA  
1588 C C   . ARG A 225 ? 0.6912 0.5369 0.7602 0.0185  0.2060  -0.0608 211 ARG A C   
1589 O O   . ARG A 225 ? 0.6215 0.4646 0.6715 0.0173  0.1890  -0.0626 211 ARG A O   
1590 C CB  . ARG A 225 ? 0.7277 0.5375 0.7417 0.0176  0.2304  -0.0598 211 ARG A CB  
1591 C CG  . ARG A 225 ? 0.7954 0.5993 0.8147 0.0175  0.2544  -0.0560 211 ARG A CG  
1592 C CD  . ARG A 225 ? 0.9248 0.7290 0.9365 0.0147  0.2519  -0.0483 211 ARG A CD  
1593 N NE  . ARG A 225 ? 0.8561 0.6872 0.9056 0.0129  0.2375  -0.0430 211 ARG A NE  
1594 C CZ  . ARG A 225 ? 0.9145 0.7502 0.9561 0.0113  0.2201  -0.0393 211 ARG A CZ  
1595 N NH1 . ARG A 225 ? 0.8364 0.6535 0.8366 0.0115  0.2133  -0.0395 211 ARG A NH1 
1596 N NH2 . ARG A 225 ? 0.7287 0.5874 0.8043 0.0098  0.2088  -0.0354 211 ARG A NH2 
1597 N N   . THR A 226 ? 0.6055 0.4732 0.7165 0.0189  0.2064  -0.0560 212 THR A N   
1598 C CA  . THR A 226 ? 0.4801 0.3684 0.6143 0.0182  0.1877  -0.0527 212 THR A CA  
1599 C C   . THR A 226 ? 0.4742 0.3770 0.6256 0.0160  0.1838  -0.0453 212 THR A C   
1600 O O   . THR A 226 ? 0.4571 0.3625 0.6235 0.0155  0.1970  -0.0422 212 THR A O   
1601 C CB  . THR A 226 ? 0.4882 0.3884 0.6548 0.0208  0.1884  -0.0535 212 THR A CB  
1602 O OG1 . THR A 226 ? 0.5652 0.4496 0.7153 0.0225  0.1930  -0.0610 212 THR A OG1 
1603 C CG2 . THR A 226 ? 0.4358 0.3539 0.6206 0.0201  0.1695  -0.0500 212 THR A CG2 
1604 N N   . ALA A 227 ? 0.4811 0.3926 0.6306 0.0146  0.1661  -0.0430 213 ALA A N   
1605 C CA  . ALA A 227 ? 0.4965 0.4204 0.6602 0.0124  0.1602  -0.0370 213 ALA A CA  
1606 C C   . ALA A 227 ? 0.4701 0.4115 0.6540 0.0125  0.1442  -0.0350 213 ALA A C   
1607 O O   . ALA A 227 ? 0.4610 0.4029 0.6408 0.0138  0.1359  -0.0379 213 ALA A O   
1608 C CB  . ALA A 227 ? 0.4734 0.3856 0.6072 0.0107  0.1564  -0.0355 213 ALA A CB  
1609 N N   . LEU A 228 ? 0.3766 0.3313 0.5817 0.0109  0.1403  -0.0303 214 LEU A N   
1610 C CA  . LEU A 228 ? 0.4066 0.3766 0.6296 0.0111  0.1264  -0.0280 214 LEU A CA  
1611 C C   . LEU A 228 ? 0.4337 0.4055 0.6474 0.0089  0.1164  -0.0255 214 LEU A C   
1612 O O   . LEU A 228 ? 0.4277 0.3976 0.6420 0.0065  0.1208  -0.0233 214 LEU A O   
1613 C CB  . LEU A 228 ? 0.3335 0.3176 0.5912 0.0114  0.1288  -0.0250 214 LEU A CB  
1614 C CG  . LEU A 228 ? 0.4569 0.4539 0.7322 0.0130  0.1164  -0.0229 214 LEU A CG  
1615 C CD1 . LEU A 228 ? 0.5941 0.6022 0.9025 0.0145  0.1201  -0.0203 214 LEU A CD1 
1616 C CD2 . LEU A 228 ? 0.6353 0.6385 0.9073 0.0109  0.1030  -0.0204 214 LEU A CD2 
1617 N N   . LEU A 229 ? 0.3523 0.3272 0.5587 0.0097  0.1040  -0.0260 215 LEU A N   
1618 C CA  . LEU A 229 ? 0.3663 0.3435 0.5662 0.0085  0.0945  -0.0240 215 LEU A CA  
1619 C C   . LEU A 229 ? 0.4400 0.4296 0.6548 0.0090  0.0843  -0.0224 215 LEU A C   
1620 O O   . LEU A 229 ? 0.3867 0.3781 0.5999 0.0107  0.0797  -0.0236 215 LEU A O   
1621 C CB  . LEU A 229 ? 0.3698 0.3371 0.5439 0.0094  0.0900  -0.0259 215 LEU A CB  
1622 C CG  . LEU A 229 ? 0.3813 0.3494 0.5484 0.0092  0.0815  -0.0240 215 LEU A CG  
1623 C CD1 . LEU A 229 ? 0.3423 0.3054 0.5083 0.0071  0.0867  -0.0214 215 LEU A CD1 
1624 C CD2 . LEU A 229 ? 0.3794 0.3402 0.5262 0.0111  0.0755  -0.0259 215 LEU A CD2 
1625 N N   . ALA A 230 ? 0.3837 0.3804 0.6116 0.0073  0.0808  -0.0198 216 ALA A N   
1626 C CA  . ALA A 230 ? 0.3579 0.3642 0.5967 0.0077  0.0712  -0.0181 216 ALA A CA  
1627 C C   . ALA A 230 ? 0.4436 0.4490 0.6732 0.0064  0.0637  -0.0176 216 ALA A C   
1628 O O   . ALA A 230 ? 0.3631 0.3631 0.5867 0.0045  0.0663  -0.0177 216 ALA A O   
1629 C CB  . ALA A 230 ? 0.2849 0.3002 0.5485 0.0070  0.0716  -0.0159 216 ALA A CB  
1630 N N   . ASP A 231 ? 0.3052 0.3145 0.5331 0.0077  0.0556  -0.0170 217 ASP A N   
1631 C CA  . ASP A 231 ? 0.2472 0.2544 0.4658 0.0069  0.0497  -0.0171 217 ASP A CA  
1632 C C   . ASP A 231 ? 0.2858 0.2980 0.5076 0.0074  0.0417  -0.0158 217 ASP A C   
1633 O O   . ASP A 231 ? 0.2819 0.2998 0.5159 0.0079  0.0398  -0.0139 217 ASP A O   
1634 C CB  . ASP A 231 ? 0.3450 0.3457 0.5464 0.0087  0.0500  -0.0187 217 ASP A CB  
1635 C CG  . ASP A 231 ? 0.4324 0.4275 0.6253 0.0078  0.0480  -0.0191 217 ASP A CG  
1636 O OD1 . ASP A 231 ? 0.3855 0.3756 0.5784 0.0056  0.0521  -0.0188 217 ASP A OD1 
1637 O OD2 . ASP A 231 ? 0.4220 0.4167 0.6085 0.0092  0.0434  -0.0196 217 ASP A OD2 
1638 N N   . PHE A 232 ? 0.3000 0.3087 0.5096 0.0078  0.0374  -0.0167 218 PHE A N   
1639 C CA  . PHE A 232 ? 0.2920 0.3015 0.5003 0.0072  0.0299  -0.0161 218 PHE A CA  
1640 C C   . PHE A 232 ? 0.2600 0.2736 0.4708 0.0093  0.0267  -0.0135 218 PHE A C   
1641 O O   . PHE A 232 ? 0.2799 0.2945 0.4919 0.0087  0.0196  -0.0121 218 PHE A O   
1642 C CB  . PHE A 232 ? 0.2858 0.2886 0.4781 0.0080  0.0283  -0.0181 218 PHE A CB  
1643 C CG  . PHE A 232 ? 0.2504 0.2527 0.4339 0.0115  0.0304  -0.0179 218 PHE A CG  
1644 C CD1 . PHE A 232 ? 0.2673 0.2695 0.4499 0.0131  0.0351  -0.0186 218 PHE A CD1 
1645 C CD2 . PHE A 232 ? 0.2754 0.2766 0.4513 0.0130  0.0277  -0.0171 218 PHE A CD2 
1646 C CE1 . PHE A 232 ? 0.3204 0.3237 0.4993 0.0158  0.0366  -0.0186 218 PHE A CE1 
1647 C CE2 . PHE A 232 ? 0.3487 0.3499 0.5195 0.0157  0.0314  -0.0166 218 PHE A CE2 
1648 C CZ  . PHE A 232 ? 0.2504 0.2537 0.4249 0.0169  0.0356  -0.0175 218 PHE A CZ  
1649 N N   . LEU A 233 ? 0.3018 0.3166 0.5128 0.0115  0.0310  -0.0126 219 LEU A N   
1650 C CA  . LEU A 233 ? 0.2538 0.2706 0.4669 0.0134  0.0287  -0.0093 219 LEU A CA  
1651 C C   . LEU A 233 ? 0.2933 0.3152 0.5226 0.0133  0.0257  -0.0067 219 LEU A C   
1652 O O   . LEU A 233 ? 0.3520 0.3745 0.5822 0.0147  0.0202  -0.0032 219 LEU A O   
1653 C CB  . LEU A 233 ? 0.2846 0.3010 0.4964 0.0151  0.0343  -0.0093 219 LEU A CB  
1654 C CG  . LEU A 233 ? 0.4108 0.4241 0.6101 0.0158  0.0358  -0.0110 219 LEU A CG  
1655 C CD1 . LEU A 233 ? 0.3420 0.3561 0.5438 0.0165  0.0404  -0.0119 219 LEU A CD1 
1656 C CD2 . LEU A 233 ? 0.2850 0.2954 0.4742 0.0169  0.0329  -0.0087 219 LEU A CD2 
1657 N N   . VAL A 234 ? 0.2271 0.2520 0.4693 0.0118  0.0295  -0.0081 220 VAL A N   
1658 C CA  . VAL A 234 ? 0.2268 0.2580 0.4890 0.0117  0.0270  -0.0058 220 VAL A CA  
1659 C C   . VAL A 234 ? 0.2746 0.3080 0.5389 0.0099  0.0163  -0.0048 220 VAL A C   
1660 O O   . VAL A 234 ? 0.2725 0.3104 0.5480 0.0111  0.0090  -0.0014 220 VAL A O   
1661 C CB  . VAL A 234 ? 0.2745 0.3075 0.5495 0.0102  0.0358  -0.0078 220 VAL A CB  
1662 C CG1 . VAL A 234 ? 0.2238 0.2651 0.5240 0.0095  0.0335  -0.0058 220 VAL A CG1 
1663 C CG2 . VAL A 234 ? 0.2884 0.3182 0.5613 0.0124  0.0449  -0.0089 220 VAL A CG2 
1664 N N   . LEU A 235 ? 0.3151 0.3441 0.5682 0.0070  0.0143  -0.0078 221 LEU A N   
1665 C CA  . LEU A 235 ? 0.2943 0.3231 0.5466 0.0046  0.0032  -0.0081 221 LEU A CA  
1666 C C   . LEU A 235 ? 0.2550 0.2797 0.4916 0.0071  -0.0049 -0.0057 221 LEU A C   
1667 O O   . LEU A 235 ? 0.2848 0.3119 0.5267 0.0072  -0.0155 -0.0033 221 LEU A O   
1668 C CB  . LEU A 235 ? 0.2490 0.2715 0.4906 0.0011  0.0040  -0.0124 221 LEU A CB  
1669 C CG  . LEU A 235 ? 0.2621 0.2859 0.5165 -0.0021 0.0117  -0.0141 221 LEU A CG  
1670 C CD1 . LEU A 235 ? 0.2530 0.2673 0.4915 -0.0040 0.0138  -0.0175 221 LEU A CD1 
1671 C CD2 . LEU A 235 ? 0.3367 0.3685 0.6160 -0.0057 0.0069  -0.0135 221 LEU A CD2 
1672 N N   . ARG A 236 ? 0.2556 0.2738 0.4730 0.0094  0.0001  -0.0060 222 ARG A N   
1673 C CA  . ARG A 236 ? 0.2683 0.2800 0.4670 0.0116  -0.0050 -0.0037 222 ARG A CA  
1674 C C   . ARG A 236 ? 0.2768 0.2913 0.4826 0.0145  -0.0088 0.0021  222 ARG A C   
1675 O O   . ARG A 236 ? 0.3376 0.3473 0.5316 0.0157  -0.0177 0.0051  222 ARG A O   
1676 C CB  . ARG A 236 ? 0.3201 0.3258 0.5018 0.0133  0.0036  -0.0050 222 ARG A CB  
1677 C CG  . ARG A 236 ? 0.2757 0.2789 0.4532 0.0116  0.0083  -0.0100 222 ARG A CG  
1678 C CD  . ARG A 236 ? 0.3033 0.3000 0.4700 0.0092  0.0012  -0.0133 222 ARG A CD  
1679 N NE  . ARG A 236 ? 0.3249 0.3158 0.4821 0.0091  0.0068  -0.0174 222 ARG A NE  
1680 C CZ  . ARG A 236 ? 0.4474 0.4370 0.6098 0.0063  0.0069  -0.0205 222 ARG A CZ  
1681 N NH1 . ARG A 236 ? 0.3194 0.3137 0.4973 0.0026  0.0024  -0.0205 222 ARG A NH1 
1682 N NH2 . ARG A 236 ? 0.2835 0.2669 0.4369 0.0073  0.0121  -0.0234 222 ARG A NH2 
1683 N N   . HIS A 237 ? 0.2665 0.2870 0.4894 0.0160  -0.0024 0.0039  223 HIS A N   
1684 C CA  . HIS A 237 ? 0.3798 0.4019 0.6111 0.0194  -0.0047 0.0097  223 HIS A CA  
1685 C C   . HIS A 237 ? 0.3653 0.3960 0.6209 0.0197  -0.0119 0.0117  223 HIS A C   
1686 O O   . HIS A 237 ? 0.3577 0.3913 0.6271 0.0231  -0.0116 0.0160  223 HIS A O   
1687 C CB  . HIS A 237 ? 0.3287 0.3508 0.5648 0.0212  0.0066  0.0101  223 HIS A CB  
1688 C CG  . HIS A 237 ? 0.4256 0.4406 0.6425 0.0214  0.0125  0.0095  223 HIS A CG  
1689 N ND1 . HIS A 237 ? 0.4244 0.4333 0.6310 0.0237  0.0126  0.0145  223 HIS A ND1 
1690 C CD2 . HIS A 237 ? 0.4439 0.4573 0.6518 0.0197  0.0185  0.0050  223 HIS A CD2 
1691 C CE1 . HIS A 237 ? 0.5452 0.5499 0.7391 0.0230  0.0195  0.0127  223 HIS A CE1 
1692 N NE2 . HIS A 237 ? 0.4095 0.4175 0.6048 0.0209  0.0225  0.0069  223 HIS A NE2 
1693 N N   . GLY A 238 ? 0.4681 0.5029 0.7312 0.0162  -0.0181 0.0087  224 GLY A N   
1694 C CA  . GLY A 238 ? 0.4154 0.4596 0.7042 0.0160  -0.0267 0.0107  224 GLY A CA  
1695 C C   . GLY A 238 ? 0.3274 0.3806 0.6449 0.0173  -0.0174 0.0111  224 GLY A C   
1696 O O   . GLY A 238 ? 0.3859 0.4469 0.7269 0.0196  -0.0231 0.0148  224 GLY A O   
1697 N N   . LEU A 239 ? 0.3283 0.3799 0.6441 0.0162  -0.0034 0.0074  225 LEU A N   
1698 C CA  . LEU A 239 ? 0.3497 0.4064 0.6871 0.0177  0.0076  0.0071  225 LEU A CA  
1699 C C   . LEU A 239 ? 0.3492 0.4105 0.7009 0.0136  0.0143  0.0033  225 LEU A C   
1700 O O   . LEU A 239 ? 0.2849 0.3471 0.6476 0.0143  0.0268  0.0019  225 LEU A O   
1701 C CB  . LEU A 239 ? 0.3487 0.3980 0.6721 0.0197  0.0187  0.0059  225 LEU A CB  
1702 C CG  . LEU A 239 ? 0.2869 0.3317 0.6017 0.0237  0.0145  0.0106  225 LEU A CG  
1703 C CD1 . LEU A 239 ? 0.3164 0.3533 0.6134 0.0238  0.0231  0.0085  225 LEU A CD1 
1704 C CD2 . LEU A 239 ? 0.3071 0.3566 0.6457 0.0280  0.0143  0.0148  225 LEU A CD2 
1705 N N   . LYS A 240 ? 0.2802 0.3429 0.6311 0.0091  0.0068  0.0016  226 LYS A N   
1706 C CA  . LYS A 240 ? 0.2561 0.3219 0.6209 0.0046  0.0138  -0.0014 226 LYS A CA  
1707 C C   . LYS A 240 ? 0.2877 0.3648 0.6886 0.0054  0.0179  0.0005  226 LYS A C   
1708 O O   . LYS A 240 ? 0.2992 0.3766 0.7103 0.0044  0.0322  -0.0011 226 LYS A O   
1709 C CB  . LYS A 240 ? 0.2375 0.3018 0.5963 -0.0006 0.0034  -0.0037 226 LYS A CB  
1710 C CG  . LYS A 240 ? 0.3026 0.3719 0.6833 -0.0062 0.0074  -0.0057 226 LYS A CG  
1711 C CD  . LYS A 240 ? 0.2572 0.3216 0.6272 -0.0117 -0.0024 -0.0088 226 LYS A CD  
1712 C CE  . LYS A 240 ? 0.5015 0.5696 0.8939 -0.0181 0.0027  -0.0106 226 LYS A CE  
1713 N NZ  . LYS A 240 ? 0.5257 0.5897 0.9136 -0.0242 -0.0088 -0.0140 226 LYS A NZ  
1714 N N   . HIS A 241 ? 0.2288 0.3146 0.6491 0.0078  0.0060  0.0043  227 HIS A N   
1715 C CA  . HIS A 241 ? 0.3342 0.4323 0.7932 0.0095  0.0099  0.0065  227 HIS A CA  
1716 C C   . HIS A 241 ? 0.4426 0.5379 0.9049 0.0146  0.0259  0.0069  227 HIS A C   
1717 O O   . HIS A 241 ? 0.3441 0.4441 0.8294 0.0146  0.0391  0.0059  227 HIS A O   
1718 C CB  . HIS A 241 ? 0.2688 0.3763 0.7468 0.0122  -0.0083 0.0111  227 HIS A CB  
1719 C CG  . HIS A 241 ? 0.5686 0.6902 1.0905 0.0151  -0.0056 0.0139  227 HIS A CG  
1720 N ND1 . HIS A 241 ? 0.6508 0.7809 1.2018 0.0113  0.0057  0.0117  227 HIS A ND1 
1721 C CD2 . HIS A 241 ? 0.5410 0.6694 1.0839 0.0217  -0.0117 0.0191  227 HIS A CD2 
1722 C CE1 . HIS A 241 ? 0.6177 0.7605 1.2076 0.0156  0.0066  0.0150  227 HIS A CE1 
1723 N NE2 . HIS A 241 ? 0.7847 0.9267 1.3708 0.0222  -0.0044 0.0196  227 HIS A NE2 
1724 N N   . ALA A 242 ? 0.4471 0.5337 0.8866 0.0187  0.0256  0.0080  228 ALA A N   
1725 C CA  . ALA A 242 ? 0.3591 0.4410 0.7999 0.0231  0.0397  0.0075  228 ALA A CA  
1726 C C   . ALA A 242 ? 0.3971 0.4718 0.8264 0.0202  0.0563  0.0023  228 ALA A C   
1727 O O   . ALA A 242 ? 0.2332 0.3069 0.6748 0.0223  0.0705  0.0009  228 ALA A O   
1728 C CB  . ALA A 242 ? 0.2711 0.3441 0.6889 0.0267  0.0356  0.0094  228 ALA A CB  
1729 N N   . LEU A 243 ? 0.2939 0.3619 0.6979 0.0158  0.0550  -0.0005 229 LEU A N   
1730 C CA  . LEU A 243 ? 0.2241 0.2837 0.6141 0.0132  0.0690  -0.0046 229 LEU A CA  
1731 C C   . LEU A 243 ? 0.3180 0.3831 0.7312 0.0102  0.0781  -0.0051 229 LEU A C   
1732 O O   . LEU A 243 ? 0.2964 0.3553 0.7076 0.0102  0.0940  -0.0073 229 LEU A O   
1733 C CB  . LEU A 243 ? 0.3310 0.3826 0.6909 0.0100  0.0640  -0.0067 229 LEU A CB  
1734 C CG  . LEU A 243 ? 0.3449 0.3868 0.6777 0.0121  0.0649  -0.0083 229 LEU A CG  
1735 C CD1 . LEU A 243 ? 0.2695 0.3023 0.5918 0.0125  0.0789  -0.0118 229 LEU A CD1 
1736 C CD2 . LEU A 243 ? 0.2934 0.3374 0.6300 0.0163  0.0590  -0.0056 229 LEU A CD2 
1737 N N   . GLN A 244 ? 0.2941 0.3698 0.7288 0.0072  0.0685  -0.0031 230 GLN A N   
1738 C CA  . GLN A 244 ? 0.3333 0.4160 0.7957 0.0036  0.0770  -0.0032 230 GLN A CA  
1739 C C   . GLN A 244 ? 0.3687 0.4585 0.8615 0.0080  0.0884  -0.0018 230 GLN A C   
1740 O O   . GLN A 244 ? 0.2935 0.3806 0.7947 0.0070  0.1063  -0.0033 230 GLN A O   
1741 C CB  . GLN A 244 ? 0.3658 0.4591 0.8469 -0.0009 0.0615  -0.0019 230 GLN A CB  
1742 C CG  . GLN A 244 ? 0.6433 0.7288 1.1025 -0.0070 0.0572  -0.0043 230 GLN A CG  
1743 C CD  . GLN A 244 ? 0.5291 0.6224 1.0014 -0.0113 0.0390  -0.0040 230 GLN A CD  
1744 O OE1 . GLN A 244 ? 0.4602 0.5459 0.9105 -0.0149 0.0313  -0.0062 230 GLN A OE1 
1745 N NE2 . GLN A 244 ? 0.3695 0.4775 0.8777 -0.0107 0.0315  -0.0016 230 GLN A NE2 
1746 N N   . LYS A 245 ? 0.3183 0.4160 0.8273 0.0132  0.0790  0.0012  231 LYS A N   
1747 C CA  . LYS A 245 ? 0.3272 0.4309 0.8660 0.0186  0.0897  0.0026  231 LYS A CA  
1748 C C   . LYS A 245 ? 0.2921 0.3814 0.8098 0.0217  0.1078  -0.0008 231 LYS A C   
1749 O O   . LYS A 245 ? 0.3268 0.4163 0.8631 0.0242  0.1246  -0.0019 231 LYS A O   
1750 C CB  . LYS A 245 ? 0.2807 0.3931 0.8367 0.0242  0.0743  0.0072  231 LYS A CB  
1751 C CG  . LYS A 245 ? 0.5354 0.6572 1.1310 0.0303  0.0828  0.0095  231 LYS A CG  
1752 C CD  . LYS A 245 ? 0.6685 0.8042 1.2929 0.0316  0.0636  0.0148  231 LYS A CD  
1753 C CE  . LYS A 245 ? 0.5637 0.6992 1.2066 0.0381  0.0669  0.0181  231 LYS A CE  
1754 N NZ  . LYS A 245 ? 0.5929 0.7167 1.2294 0.0394  0.0910  0.0144  231 LYS A NZ  
1755 N N   . TRP A 246 ? 0.3224 0.3986 0.8015 0.0216  0.1047  -0.0030 232 TRP A N   
1756 C CA  . TRP A 246 ? 0.3918 0.4530 0.8474 0.0237  0.1190  -0.0071 232 TRP A CA  
1757 C C   . TRP A 246 ? 0.3459 0.3999 0.7966 0.0206  0.1373  -0.0103 232 TRP A C   
1758 O O   . TRP A 246 ? 0.3031 0.3512 0.7592 0.0236  0.1540  -0.0125 232 TRP A O   
1759 C CB  . TRP A 246 ? 0.3178 0.3687 0.7360 0.0227  0.1100  -0.0087 232 TRP A CB  
1760 C CG  . TRP A 246 ? 0.3883 0.4243 0.7820 0.0246  0.1197  -0.0130 232 TRP A CG  
1761 C CD1 . TRP A 246 ? 0.3875 0.4151 0.7824 0.0269  0.1365  -0.0165 232 TRP A CD1 
1762 C CD2 . TRP A 246 ? 0.3249 0.3519 0.6891 0.0242  0.1127  -0.0149 232 TRP A CD2 
1763 N NE1 . TRP A 246 ? 0.3608 0.3740 0.7271 0.0276  0.1389  -0.0209 232 TRP A NE1 
1764 C CE2 . TRP A 246 ? 0.3196 0.3334 0.6690 0.0258  0.1242  -0.0197 232 TRP A CE2 
1765 C CE3 . TRP A 246 ? 0.2531 0.2817 0.6029 0.0226  0.0984  -0.0131 232 TRP A CE3 
1766 C CZ2 . TRP A 246 ? 0.3500 0.3537 0.6735 0.0253  0.1202  -0.0229 232 TRP A CZ2 
1767 C CZ3 . TRP A 246 ? 0.3102 0.3295 0.6358 0.0226  0.0964  -0.0158 232 TRP A CZ3 
1768 C CH2 . TRP A 246 ? 0.2783 0.2861 0.5923 0.0236  0.1064  -0.0206 232 TRP A CH2 
1769 N N   . VAL A 247 ? 0.3089 0.3617 0.7487 0.0149  0.1352  -0.0104 233 VAL A N   
1770 C CA  . VAL A 247 ? 0.3510 0.3939 0.7810 0.0120  0.1530  -0.0126 233 VAL A CA  
1771 C C   . VAL A 247 ? 0.3025 0.3554 0.7712 0.0112  0.1658  -0.0108 233 VAL A C   
1772 O O   . VAL A 247 ? 0.4502 0.4936 0.9145 0.0107  0.1857  -0.0126 233 VAL A O   
1773 C CB  . VAL A 247 ? 0.3176 0.3534 0.7216 0.0064  0.1476  -0.0128 233 VAL A CB  
1774 C CG1 . VAL A 247 ? 0.3885 0.4168 0.7596 0.0076  0.1349  -0.0143 233 VAL A CG1 
1775 C CG2 . VAL A 247 ? 0.3316 0.3807 0.7595 0.0018  0.1372  -0.0099 233 VAL A CG2 
1776 N N   . LYS A 248 ? 0.3600 0.4315 0.8668 0.0113  0.1551  -0.0074 234 LYS A N   
1777 C CA  . LYS A 248 ? 0.3094 0.3916 0.8569 0.0112  0.1658  -0.0056 234 LYS A CA  
1778 C C   . LYS A 248 ? 0.4329 0.5079 0.9828 0.0174  0.1770  -0.0064 234 LYS A C   
1779 O O   . LYS A 248 ? 0.4619 0.5288 1.0143 0.0171  0.1951  -0.0074 234 LYS A O   
1780 C CB  . LYS A 248 ? 0.4677 0.5679 1.0470 0.0094  0.1458  -0.0018 234 LYS A CB  
1781 C CG  . LYS A 248 ? 0.5995 0.7061 1.2115 0.0110  0.1489  0.0006  234 LYS A CG  
1782 C CD  . LYS A 248 ? 0.6667 0.7900 1.3066 0.0119  0.1260  0.0043  234 LYS A CD  
1783 C CE  . LYS A 248 ? 0.4900 0.6174 1.1548 0.0178  0.1276  0.0069  234 LYS A CE  
1784 N NZ  . LYS A 248 ? 0.5596 0.6963 1.2590 0.0146  0.1287  0.0087  234 LYS A NZ  
1785 N N   . ASP A 249 ? 0.4890 0.5657 1.0379 0.0231  0.1671  -0.0060 235 ASP A N   
1786 C CA  . ASP A 249 ? 0.3973 0.4664 0.9489 0.0289  0.1768  -0.0068 235 ASP A CA  
1787 C C   . ASP A 249 ? 0.3668 0.4160 0.8853 0.0301  0.1953  -0.0125 235 ASP A C   
1788 O O   . ASP A 249 ? 0.4906 0.5300 1.0088 0.0333  0.2089  -0.0143 235 ASP A O   
1789 C CB  . ASP A 249 ? 0.3642 0.4387 0.9220 0.0344  0.1611  -0.0043 235 ASP A CB  
1790 C CG  . ASP A 249 ? 0.4394 0.5315 1.0299 0.0347  0.1432  0.0015  235 ASP A CG  
1791 O OD1 . ASP A 249 ? 0.5299 0.6298 1.1447 0.0317  0.1453  0.0032  235 ASP A OD1 
1792 O OD2 . ASP A 249 ? 0.4348 0.5320 1.0261 0.0379  0.1267  0.0045  235 ASP A OD2 
1793 N N   . VAL A 250 ? 0.3754 0.4180 0.8657 0.0278  0.1955  -0.0155 236 VAL A N   
1794 C CA  . VAL A 250 ? 0.3597 0.3810 0.8116 0.0285  0.2089  -0.0212 236 VAL A CA  
1795 C C   . VAL A 250 ? 0.3917 0.4036 0.8157 0.0223  0.2125  -0.0218 236 VAL A C   
1796 O O   . VAL A 250 ? 0.4950 0.5019 0.8902 0.0195  0.1987  -0.0221 236 VAL A O   
1797 C CB  . VAL A 250 ? 0.4726 0.4861 0.8986 0.0309  0.1957  -0.0233 236 VAL A CB  
1798 C CG1 . VAL A 250 ? 0.3204 0.3119 0.7083 0.0311  0.2070  -0.0296 236 VAL A CG1 
1799 C CG2 . VAL A 250 ? 0.3472 0.3692 0.8012 0.0370  0.1911  -0.0215 236 VAL A CG2 
1800 N N   . PRO A 251 ? 0.5175 0.5262 0.9496 0.0201  0.2311  -0.0216 237 PRO A N   
1801 C CA  . PRO A 251 ? 0.3848 0.3830 0.7904 0.0143  0.2346  -0.0210 237 PRO A CA  
1802 C C   . PRO A 251 ? 0.5646 0.5395 0.9176 0.0147  0.2360  -0.0253 237 PRO A C   
1803 O O   . PRO A 251 ? 0.5646 0.5245 0.9004 0.0181  0.2495  -0.0297 237 PRO A O   
1804 C CB  . PRO A 251 ? 0.4417 0.4397 0.8694 0.0128  0.2583  -0.0198 237 PRO A CB  
1805 C CG  . PRO A 251 ? 0.4631 0.4740 0.9286 0.0156  0.2539  -0.0176 237 PRO A CG  
1806 C CD  . PRO A 251 ? 0.5017 0.5121 0.9605 0.0216  0.2452  -0.0204 237 PRO A CD  
1807 N N   . MET A 252 ? 0.5154 0.4872 0.8435 0.0113  0.2212  -0.0242 238 MET A N   
1808 C CA  . MET A 252 ? 0.4704 0.4218 0.7507 0.0111  0.2197  -0.0274 238 MET A CA  
1809 C C   . MET A 252 ? 0.4839 0.4346 0.7494 0.0067  0.2088  -0.0242 238 MET A C   
1810 O O   . MET A 252 ? 0.4431 0.4093 0.7333 0.0039  0.1992  -0.0206 238 MET A O   
1811 C CB  . MET A 252 ? 0.5630 0.5119 0.8282 0.0145  0.2069  -0.0314 238 MET A CB  
1812 C CG  . MET A 252 ? 0.5950 0.5628 0.8831 0.0150  0.1875  -0.0289 238 MET A CG  
1813 S SD  . MET A 252 ? 0.6453 0.6100 0.9246 0.0191  0.1786  -0.0330 238 MET A SD  
1814 C CE  . MET A 252 ? 0.4824 0.4692 0.7931 0.0197  0.1603  -0.0278 238 MET A CE  
1815 N N   . ALA A 253 ? 0.5040 0.4354 0.7284 0.0062  0.2100  -0.0256 239 ALA A N   
1816 C CA  . ALA A 253 ? 0.5284 0.4574 0.7361 0.0032  0.1983  -0.0226 239 ALA A CA  
1817 C C   . ALA A 253 ? 0.5262 0.4697 0.7431 0.0038  0.1767  -0.0226 239 ALA A C   
1818 O O   . ALA A 253 ? 0.4469 0.3917 0.6584 0.0067  0.1691  -0.0258 239 ALA A O   
1819 C CB  . ALA A 253 ? 0.4265 0.3322 0.5877 0.0040  0.2005  -0.0242 239 ALA A CB  
1820 N N   . HIS A 254 ? 0.4277 0.3815 0.6591 0.0007  0.1677  -0.0191 240 HIS A N   
1821 C CA  . HIS A 254 ? 0.3686 0.3352 0.6084 0.0011  0.1490  -0.0189 240 HIS A CA  
1822 C C   . HIS A 254 ? 0.4670 0.4322 0.6986 -0.0019 0.1404  -0.0165 240 HIS A C   
1823 O O   . HIS A 254 ? 0.4599 0.4201 0.6933 -0.0054 0.1483  -0.0141 240 HIS A O   
1824 C CB  . HIS A 254 ? 0.3686 0.3538 0.6460 0.0014  0.1452  -0.0179 240 HIS A CB  
1825 C CG  . HIS A 254 ? 0.4112 0.4049 0.7173 -0.0024 0.1511  -0.0150 240 HIS A CG  
1826 N ND1 . HIS A 254 ? 0.4160 0.4043 0.7300 -0.0038 0.1698  -0.0144 240 HIS A ND1 
1827 C CD2 . HIS A 254 ? 0.3744 0.3814 0.7043 -0.0055 0.1409  -0.0129 240 HIS A CD2 
1828 C CE1 . HIS A 254 ? 0.3901 0.3896 0.7348 -0.0079 0.1709  -0.0118 240 HIS A CE1 
1829 N NE2 . HIS A 254 ? 0.4639 0.4748 0.8183 -0.0091 0.1525  -0.0111 240 HIS A NE2 
1830 N N   . ALA A 255 ? 0.3957 0.3646 0.6188 -0.0006 0.1251  -0.0172 241 ALA A N   
1831 C CA  . ALA A 255 ? 0.3726 0.3398 0.5878 -0.0025 0.1163  -0.0155 241 ALA A CA  
1832 C C   . ALA A 255 ? 0.3656 0.3433 0.5857 -0.0011 0.1011  -0.0164 241 ALA A C   
1833 O O   . ALA A 255 ? 0.3588 0.3441 0.5872 0.0012  0.0976  -0.0176 241 ALA A O   
1834 C CB  . ALA A 255 ? 0.3902 0.3406 0.5728 -0.0013 0.1178  -0.0153 241 ALA A CB  
1835 N N   . THR A 256 ? 0.4083 0.3850 0.6235 -0.0025 0.0932  -0.0155 242 THR A N   
1836 C CA  . THR A 256 ? 0.3644 0.3462 0.5756 -0.0006 0.0806  -0.0164 242 THR A CA  
1837 C C   . THR A 256 ? 0.3621 0.3333 0.5507 0.0008  0.0775  -0.0164 242 THR A C   
1838 O O   . THR A 256 ? 0.4302 0.3899 0.6062 0.0002  0.0840  -0.0152 242 THR A O   
1839 C CB  . THR A 256 ? 0.3827 0.3737 0.6115 -0.0033 0.0728  -0.0160 242 THR A CB  
1840 O OG1 . THR A 256 ? 0.4009 0.3853 0.6259 -0.0064 0.0723  -0.0155 242 THR A OG1 
1841 C CG2 . THR A 256 ? 0.3404 0.3415 0.5953 -0.0051 0.0760  -0.0151 242 THR A CG2 
1842 N N   . MET A 257 ? 0.3351 0.3095 0.5187 0.0030  0.0682  -0.0174 243 MET A N   
1843 C CA  . MET A 257 ? 0.4160 0.3824 0.5842 0.0047  0.0642  -0.0171 243 MET A CA  
1844 C C   . MET A 257 ? 0.3185 0.2859 0.4936 0.0023  0.0599  -0.0172 243 MET A C   
1845 O O   . MET A 257 ? 0.4032 0.3769 0.5941 -0.0012 0.0595  -0.0173 243 MET A O   
1846 C CB  . MET A 257 ? 0.4156 0.3841 0.5750 0.0089  0.0582  -0.0185 243 MET A CB  
1847 C CG  . MET A 257 ? 0.4153 0.3793 0.5643 0.0107  0.0610  -0.0192 243 MET A CG  
1848 S SD  . MET A 257 ? 0.4029 0.3711 0.5469 0.0146  0.0531  -0.0212 243 MET A SD  
1849 C CE  . MET A 257 ? 0.3551 0.3366 0.5172 0.0137  0.0515  -0.0220 243 MET A CE  
1850 N N   . LEU A 258 ? 0.2830 0.2436 0.4467 0.0042  0.0561  -0.0174 244 LEU A N   
1851 C CA  . LEU A 258 ? 0.3708 0.3285 0.5377 0.0017  0.0528  -0.0183 244 LEU A CA  
1852 C C   . LEU A 258 ? 0.4184 0.3856 0.5946 0.0008  0.0462  -0.0204 244 LEU A C   
1853 O O   . LEU A 258 ? 0.3950 0.3634 0.5808 -0.0035 0.0437  -0.0214 244 LEU A O   
1854 C CB  . LEU A 258 ? 0.3142 0.2617 0.4667 0.0052  0.0507  -0.0184 244 LEU A CB  
1855 C CG  . LEU A 258 ? 0.3286 0.2699 0.4811 0.0032  0.0477  -0.0203 244 LEU A CG  
1856 C CD1 . LEU A 258 ? 0.3077 0.2444 0.4691 -0.0033 0.0513  -0.0197 244 LEU A CD1 
1857 C CD2 . LEU A 258 ? 0.3881 0.3186 0.5273 0.0079  0.0469  -0.0200 244 LEU A CD2 
1858 N N   . MET A 259 ? 0.3631 0.3364 0.5364 0.0045  0.0430  -0.0210 245 MET A N   
1859 C CA  . MET A 259 ? 0.3477 0.3270 0.5246 0.0043  0.0371  -0.0222 245 MET A CA  
1860 C C   . MET A 259 ? 0.3066 0.2939 0.4991 0.0009  0.0355  -0.0213 245 MET A C   
1861 O O   . MET A 259 ? 0.4077 0.3967 0.6041 -0.0012 0.0291  -0.0223 245 MET A O   
1862 C CB  . MET A 259 ? 0.3966 0.3804 0.5687 0.0087  0.0362  -0.0221 245 MET A CB  
1863 C CG  . MET A 259 ? 0.3721 0.3509 0.5334 0.0127  0.0368  -0.0229 245 MET A CG  
1864 S SD  . MET A 259 ? 0.4370 0.4225 0.5977 0.0166  0.0363  -0.0229 245 MET A SD  
1865 C CE  . MET A 259 ? 0.4045 0.3888 0.5609 0.0156  0.0330  -0.0238 245 MET A CE  
1866 N N   . GLY A 260 ? 0.3326 0.3243 0.5339 0.0008  0.0407  -0.0197 246 GLY A N   
1867 C CA  . GLY A 260 ? 0.3354 0.3357 0.5549 -0.0012 0.0403  -0.0185 246 GLY A CA  
1868 C C   . GLY A 260 ? 0.3787 0.3790 0.6124 -0.0058 0.0442  -0.0181 246 GLY A C   
1869 O O   . GLY A 260 ? 0.3036 0.3118 0.5560 -0.0071 0.0459  -0.0168 246 GLY A O   
1870 N N   . LYS A 261 ? 0.3962 0.3876 0.6231 -0.0083 0.0465  -0.0188 247 LYS A N   
1871 C CA  . LYS A 261 ? 0.3847 0.3755 0.6267 -0.0135 0.0511  -0.0182 247 LYS A CA  
1872 C C   . LYS A 261 ? 0.4136 0.4138 0.6760 -0.0173 0.0424  -0.0190 247 LYS A C   
1873 O O   . LYS A 261 ? 0.3247 0.3246 0.5807 -0.0173 0.0319  -0.0210 247 LYS A O   
1874 C CB  . LYS A 261 ? 0.3588 0.3364 0.5886 -0.0156 0.0538  -0.0187 247 LYS A CB  
1875 C CG  . LYS A 261 ? 0.4818 0.4563 0.7253 -0.0211 0.0621  -0.0172 247 LYS A CG  
1876 C CD  . LYS A 261 ? 0.6331 0.5934 0.8656 -0.0237 0.0632  -0.0175 247 LYS A CD  
1877 C CE  . LYS A 261 ? 0.5084 0.4564 0.7275 -0.0224 0.0753  -0.0141 247 LYS A CE  
1878 N NZ  . LYS A 261 ? 0.3098 0.2602 0.5459 -0.0266 0.0870  -0.0116 247 LYS A NZ  
1879 N N   . GLY A 262 ? 0.3176 0.3258 0.6043 -0.0202 0.0468  -0.0176 248 GLY A N   
1880 C CA  . GLY A 262 ? 0.3005 0.3199 0.6111 -0.0234 0.0375  -0.0178 248 GLY A CA  
1881 C C   . GLY A 262 ? 0.4090 0.4406 0.7357 -0.0198 0.0368  -0.0156 248 GLY A C   
1882 O O   . GLY A 262 ? 0.3439 0.3862 0.6951 -0.0219 0.0294  -0.0149 248 GLY A O   
1883 N N   . ILE A 263 ? 0.3559 0.3857 0.6706 -0.0145 0.0434  -0.0145 249 ILE A N   
1884 C CA  . ILE A 263 ? 0.2992 0.3386 0.6294 -0.0108 0.0444  -0.0124 249 ILE A CA  
1885 C C   . ILE A 263 ? 0.3332 0.3793 0.6916 -0.0129 0.0546  -0.0112 249 ILE A C   
1886 O O   . ILE A 263 ? 0.3276 0.3854 0.7122 -0.0120 0.0511  -0.0095 249 ILE A O   
1887 C CB  . ILE A 263 ? 0.2644 0.2982 0.5746 -0.0056 0.0498  -0.0124 249 ILE A CB  
1888 C CG1 . ILE A 263 ? 0.2809 0.3115 0.5707 -0.0032 0.0397  -0.0129 249 ILE A CG1 
1889 C CG2 . ILE A 263 ? 0.2478 0.2884 0.5747 -0.0021 0.0551  -0.0107 249 ILE A CG2 
1890 C CD1 . ILE A 263 ? 0.2336 0.2571 0.5020 0.0003  0.0448  -0.0137 249 ILE A CD1 
1891 N N   . PHE A 264 ? 0.3706 0.4090 0.7246 -0.0153 0.0678  -0.0117 250 PHE A N   
1892 C CA  . PHE A 264 ? 0.3036 0.3459 0.6810 -0.0169 0.0818  -0.0105 250 PHE A CA  
1893 C C   . PHE A 264 ? 0.2827 0.3254 0.6763 -0.0240 0.0841  -0.0104 250 PHE A C   
1894 O O   . PHE A 264 ? 0.3287 0.3616 0.7046 -0.0272 0.0810  -0.0115 250 PHE A O   
1895 C CB  . PHE A 264 ? 0.3658 0.3962 0.7231 -0.0141 0.0978  -0.0107 250 PHE A CB  
1896 C CG  . PHE A 264 ? 0.3624 0.3917 0.7064 -0.0080 0.0970  -0.0115 250 PHE A CG  
1897 C CD1 . PHE A 264 ? 0.3244 0.3638 0.6902 -0.0047 0.0971  -0.0106 250 PHE A CD1 
1898 C CD2 . PHE A 264 ? 0.3693 0.3871 0.6808 -0.0056 0.0960  -0.0130 250 PHE A CD2 
1899 C CE1 . PHE A 264 ? 0.3323 0.3690 0.6861 0.0005  0.0968  -0.0115 250 PHE A CE1 
1900 C CE2 . PHE A 264 ? 0.3502 0.3669 0.6515 -0.0010 0.0950  -0.0141 250 PHE A CE2 
1901 C CZ  . PHE A 264 ? 0.3190 0.3444 0.6408 0.0019  0.0959  -0.0134 250 PHE A CZ  
1902 N N   . ASP A 265 ? 0.3390 0.3930 0.7685 -0.0265 0.0899  -0.0090 251 ASP A N   
1903 C CA  . ASP A 265 ? 0.3464 0.3999 0.7947 -0.0337 0.0980  -0.0085 251 ASP A CA  
1904 C C   . ASP A 265 ? 0.3355 0.3725 0.7608 -0.0337 0.1173  -0.0076 251 ASP A C   
1905 O O   . ASP A 265 ? 0.4185 0.4536 0.8441 -0.0302 0.1322  -0.0067 251 ASP A O   
1906 C CB  . ASP A 265 ? 0.3278 0.3987 0.8232 -0.0355 0.1015  -0.0070 251 ASP A CB  
1907 C CG  . ASP A 265 ? 0.4991 0.5721 1.0207 -0.0443 0.1080  -0.0066 251 ASP A CG  
1908 O OD1 . ASP A 265 ? 0.4551 0.5130 0.9561 -0.0482 0.1162  -0.0066 251 ASP A OD1 
1909 O OD2 . ASP A 265 ? 0.4892 0.5791 1.0541 -0.0473 0.1048  -0.0059 251 ASP A OD2 
1910 N N   . GLU A 266 ? 0.3736 0.3971 0.7776 -0.0373 0.1171  -0.0079 252 GLU A N   
1911 C CA  . GLU A 266 ? 0.3826 0.3874 0.7569 -0.0364 0.1321  -0.0064 252 GLU A CA  
1912 C C   . GLU A 266 ? 0.4259 0.4267 0.8166 -0.0409 0.1524  -0.0037 252 GLU A C   
1913 O O   . GLU A 266 ? 0.5327 0.5162 0.8973 -0.0399 0.1665  -0.0018 252 GLU A O   
1914 C CB  . GLU A 266 ? 0.3455 0.3367 0.6913 -0.0376 0.1237  -0.0070 252 GLU A CB  
1915 C CG  . GLU A 266 ? 0.4744 0.4705 0.8092 -0.0345 0.1041  -0.0098 252 GLU A CG  
1916 C CD  . GLU A 266 ? 0.5188 0.4994 0.8173 -0.0316 0.1002  -0.0103 252 GLU A CD  
1917 O OE1 . GLU A 266 ? 0.4660 0.4330 0.7541 -0.0346 0.1067  -0.0088 252 GLU A OE1 
1918 O OE2 . GLU A 266 ? 0.3767 0.3587 0.6590 -0.0264 0.0908  -0.0119 252 GLU A OE2 
1919 N N   . ARG A 267 ? 0.5258 0.5415 0.9590 -0.0458 0.1544  -0.0033 253 ARG A N   
1920 C CA  . ARG A 267 ? 0.5411 0.5552 0.9954 -0.0498 0.1762  -0.0005 253 ARG A CA  
1921 C C   . ARG A 267 ? 0.4837 0.5027 0.9477 -0.0443 0.1909  -0.0001 253 ARG A C   
1922 O O   . ARG A 267 ? 0.4637 0.4772 0.9366 -0.0461 0.2129  0.0021  253 ARG A O   
1923 C CB  . ARG A 267 ? 0.4019 0.4311 0.9026 -0.0581 0.1723  -0.0004 253 ARG A CB  
1924 C CG  . ARG A 267 ? 0.4962 0.5213 0.9911 -0.0641 0.1560  -0.0020 253 ARG A CG  
1925 C CD  . ARG A 267 ? 0.5733 0.6173 1.1164 -0.0714 0.1455  -0.0034 253 ARG A CD  
1926 N NE  . ARG A 267 ? 0.4336 0.4970 0.9957 -0.0671 0.1283  -0.0054 253 ARG A NE  
1927 C CZ  . ARG A 267 ? 0.3711 0.4520 0.9709 -0.0718 0.1127  -0.0070 253 ARG A CZ  
1928 N NH1 . ARG A 267 ? 0.3741 0.4563 0.9977 -0.0810 0.1116  -0.0078 253 ARG A NH1 
1929 N NH2 . ARG A 267 ? 0.3362 0.4317 0.9469 -0.0665 0.0966  -0.0079 253 ARG A NH2 
1930 N N   . HIS A 268 ? 0.5266 0.5544 0.9886 -0.0376 0.1802  -0.0022 254 HIS A N   
1931 C CA  . HIS A 268 ? 0.6231 0.6565 1.0984 -0.0321 0.1924  -0.0024 254 HIS A CA  
1932 C C   . HIS A 268 ? 0.6662 0.6783 1.1031 -0.0282 0.2107  -0.0027 254 HIS A C   
1933 O O   . HIS A 268 ? 0.5834 0.5783 0.9787 -0.0276 0.2079  -0.0029 254 HIS A O   
1934 C CB  . HIS A 268 ? 0.4260 0.4722 0.9074 -0.0262 0.1747  -0.0042 254 HIS A CB  
1935 C CG  . HIS A 268 ? 0.7848 0.8536 1.3123 -0.0283 0.1617  -0.0034 254 HIS A CG  
1936 N ND1 . HIS A 268 ? 0.8067 0.8832 1.3611 -0.0362 0.1576  -0.0026 254 HIS A ND1 
1937 C CD2 . HIS A 268 ? 0.6124 0.6968 1.1639 -0.0236 0.1509  -0.0033 254 HIS A CD2 
1938 C CE1 . HIS A 268 ? 0.6262 0.7230 1.2192 -0.0363 0.1437  -0.0022 254 HIS A CE1 
1939 N NE2 . HIS A 268 ? 0.7404 0.8420 1.3317 -0.0284 0.1393  -0.0022 254 HIS A NE2 
1940 N N   . VAL A 269 ? 0.5751 0.5882 1.0268 -0.0252 0.2294  -0.0028 255 VAL A N   
1941 C CA  . VAL A 269 ? 0.6314 0.6234 1.0464 -0.0213 0.2474  -0.0038 255 VAL A CA  
1942 C C   . VAL A 269 ? 0.5802 0.5650 0.9595 -0.0153 0.2337  -0.0072 255 VAL A C   
1943 O O   . VAL A 269 ? 0.4883 0.4871 0.8816 -0.0121 0.2184  -0.0087 255 VAL A O   
1944 C CB  . VAL A 269 ? 0.6995 0.6949 1.1409 -0.0188 0.2702  -0.0041 255 VAL A CB  
1945 C CG1 . VAL A 269 ? 0.5518 0.5660 1.0238 -0.0135 0.2590  -0.0060 255 VAL A CG1 
1946 C CG2 . VAL A 269 ? 0.7112 0.6815 1.1105 -0.0150 0.2897  -0.0059 255 VAL A CG2 
1947 N N   . GLY A 270 ? 0.4868 0.4491 0.8195 -0.0140 0.2389  -0.0079 256 GLY A N   
1948 C CA  . GLY A 270 ? 0.5050 0.4596 0.8037 -0.0093 0.2259  -0.0111 256 GLY A CA  
1949 C C   . GLY A 270 ? 0.5701 0.5233 0.8491 -0.0108 0.2062  -0.0103 256 GLY A C   
1950 O O   . GLY A 270 ? 0.5484 0.4939 0.7977 -0.0074 0.1964  -0.0127 256 GLY A O   
1951 N N   . PHE A 271 ? 0.4818 0.4419 0.7773 -0.0159 0.2003  -0.0074 257 PHE A N   
1952 C CA  . PHE A 271 ? 0.4749 0.4318 0.7518 -0.0171 0.1837  -0.0069 257 PHE A CA  
1953 C C   . PHE A 271 ? 0.5694 0.5066 0.8206 -0.0199 0.1929  -0.0037 257 PHE A C   
1954 O O   . PHE A 271 ? 0.5315 0.4660 0.7976 -0.0246 0.2069  -0.0008 257 PHE A O   
1955 C CB  . PHE A 271 ? 0.3707 0.3454 0.6788 -0.0208 0.1692  -0.0064 257 PHE A CB  
1956 C CG  . PHE A 271 ? 0.4957 0.4676 0.7846 -0.0207 0.1517  -0.0070 257 PHE A CG  
1957 C CD1 . PHE A 271 ? 0.4758 0.4534 0.7556 -0.0163 0.1372  -0.0094 257 PHE A CD1 
1958 C CD2 . PHE A 271 ? 0.5144 0.4769 0.7948 -0.0249 0.1510  -0.0051 257 PHE A CD2 
1959 C CE1 . PHE A 271 ? 0.4365 0.4114 0.6998 -0.0159 0.1232  -0.0100 257 PHE A CE1 
1960 C CE2 . PHE A 271 ? 0.5353 0.4945 0.7988 -0.0241 0.1363  -0.0059 257 PHE A CE2 
1961 C CZ  . PHE A 271 ? 0.4451 0.4109 0.7005 -0.0195 0.1228  -0.0085 257 PHE A CZ  
1962 N N   . TYR A 272 ? 0.5336 0.4567 0.7474 -0.0169 0.1851  -0.0039 258 TYR A N   
1963 C CA  . TYR A 272 ? 0.5496 0.4518 0.7346 -0.0183 0.1919  -0.0002 258 TYR A CA  
1964 C C   . TYR A 272 ? 0.5742 0.4740 0.7485 -0.0187 0.1761  0.0010  258 TYR A C   
1965 O O   . TYR A 272 ? 0.4476 0.3297 0.5992 -0.0194 0.1799  0.0047  258 TYR A O   
1966 C CB  . TYR A 272 ? 0.5449 0.4276 0.6901 -0.0136 0.1990  -0.0008 258 TYR A CB  
1967 C CG  . TYR A 272 ? 0.6529 0.5342 0.8035 -0.0125 0.2161  -0.0029 258 TYR A CG  
1968 C CD1 . TYR A 272 ? 0.6371 0.5302 0.7984 -0.0090 0.2112  -0.0078 258 TYR A CD1 
1969 C CD2 . TYR A 272 ? 0.6570 0.5237 0.8013 -0.0148 0.2384  0.0001  258 TYR A CD2 
1970 C CE1 . TYR A 272 ? 0.5324 0.4229 0.6988 -0.0074 0.2276  -0.0102 258 TYR A CE1 
1971 C CE2 . TYR A 272 ? 0.6950 0.5594 0.8439 -0.0132 0.2559  -0.0022 258 TYR A CE2 
1972 C CZ  . TYR A 272 ? 0.6802 0.5565 0.8404 -0.0093 0.2501  -0.0076 258 TYR A CZ  
1973 O OH  . TYR A 272 ? 0.8037 0.6765 0.9690 -0.0072 0.2681  -0.0104 258 TYR A OH  
1974 N N   . GLY A 273 ? 0.4893 0.4051 0.6789 -0.0180 0.1593  -0.0018 259 GLY A N   
1975 C CA  . GLY A 273 ? 0.4770 0.3904 0.6566 -0.0176 0.1451  -0.0015 259 GLY A CA  
1976 C C   . GLY A 273 ? 0.4977 0.4194 0.6698 -0.0125 0.1297  -0.0050 259 GLY A C   
1977 O O   . GLY A 273 ? 0.4580 0.3839 0.6268 -0.0092 0.1297  -0.0073 259 GLY A O   
1978 N N   . THR A 274 ? 0.4322 0.3553 0.6023 -0.0122 0.1174  -0.0054 260 THR A N   
1979 C CA  . THR A 274 ? 0.4236 0.3543 0.5883 -0.0078 0.1039  -0.0082 260 THR A CA  
1980 C C   . THR A 274 ? 0.4548 0.3748 0.5912 -0.0026 0.1024  -0.0080 260 THR A C   
1981 O O   . THR A 274 ? 0.4833 0.3872 0.5992 -0.0018 0.1072  -0.0051 260 THR A O   
1982 C CB  . THR A 274 ? 0.4018 0.3346 0.5705 -0.0086 0.0934  -0.0089 260 THR A CB  
1983 O OG1 . THR A 274 ? 0.4071 0.3487 0.6011 -0.0142 0.0934  -0.0096 260 THR A OG1 
1984 C CG2 . THR A 274 ? 0.3503 0.2918 0.5161 -0.0043 0.0814  -0.0117 260 THR A CG2 
1985 N N   . TYR A 275 ? 0.4466 0.3749 0.5823 0.0008  0.0955  -0.0109 261 TYR A N   
1986 C CA  . TYR A 275 ? 0.5084 0.4291 0.6212 0.0052  0.0917  -0.0117 261 TYR A CA  
1987 C C   . TYR A 275 ? 0.4432 0.3649 0.5501 0.0085  0.0796  -0.0117 261 TYR A C   
1988 O O   . TYR A 275 ? 0.4991 0.4327 0.6205 0.0086  0.0728  -0.0134 261 TYR A O   
1989 C CB  . TYR A 275 ? 0.4427 0.3713 0.5602 0.0066  0.0912  -0.0153 261 TYR A CB  
1990 C CG  . TYR A 275 ? 0.4339 0.3562 0.5309 0.0103  0.0852  -0.0172 261 TYR A CG  
1991 C CD1 . TYR A 275 ? 0.4983 0.4036 0.5695 0.0114  0.0897  -0.0164 261 TYR A CD1 
1992 C CD2 . TYR A 275 ? 0.4192 0.3517 0.5222 0.0123  0.0749  -0.0198 261 TYR A CD2 
1993 C CE1 . TYR A 275 ? 0.4723 0.3716 0.5247 0.0144  0.0819  -0.0187 261 TYR A CE1 
1994 C CE2 . TYR A 275 ? 0.4386 0.3664 0.5264 0.0150  0.0683  -0.0220 261 TYR A CE2 
1995 C CZ  . TYR A 275 ? 0.5908 0.5023 0.6534 0.0160  0.0708  -0.0217 261 TYR A CZ  
1996 O OH  . TYR A 275 ? 0.4353 0.3420 0.4827 0.0183  0.0620  -0.0244 261 TYR A OH  
1997 N N   . SER A 276 ? 0.4189 0.3272 0.5042 0.0115  0.0773  -0.0095 262 SER A N   
1998 C CA  . SER A 276 ? 0.4023 0.3111 0.4836 0.0155  0.0666  -0.0092 262 SER A CA  
1999 C C   . SER A 276 ? 0.5067 0.4070 0.5672 0.0201  0.0605  -0.0087 262 SER A C   
2000 O O   . SER A 276 ? 0.4921 0.3840 0.5414 0.0238  0.0549  -0.0059 262 SER A O   
2001 C CB  . SER A 276 ? 0.3704 0.2711 0.4515 0.0147  0.0678  -0.0061 262 SER A CB  
2002 O OG  . SER A 276 ? 0.5321 0.4165 0.5987 0.0131  0.0766  -0.0021 262 SER A OG  
2003 N N   . GLY A 277 ? 0.5350 0.4370 0.5904 0.0201  0.0605  -0.0115 263 GLY A N   
2004 C CA  . GLY A 277 ? 0.4433 0.3368 0.4783 0.0238  0.0529  -0.0119 263 GLY A CA  
2005 C C   . GLY A 277 ? 0.5245 0.3967 0.5321 0.0249  0.0571  -0.0075 263 GLY A C   
2006 O O   . GLY A 277 ? 0.5050 0.3679 0.5061 0.0217  0.0698  -0.0057 263 GLY A O   
2007 N N   . SER A 278 ? 0.5698 0.4337 0.5614 0.0297  0.0465  -0.0052 264 SER A N   
2008 C CA  . SER A 278 ? 0.6103 0.4515 0.5720 0.0317  0.0489  0.0000  264 SER A CA  
2009 C C   . SER A 278 ? 0.6959 0.5286 0.6593 0.0302  0.0581  0.0055  264 SER A C   
2010 O O   . SER A 278 ? 0.7282 0.5404 0.6675 0.0304  0.0647  0.0106  264 SER A O   
2011 C CB  . SER A 278 ? 0.6565 0.4921 0.6036 0.0379  0.0328  0.0017  264 SER A CB  
2012 O OG  . SER A 278 ? 0.6501 0.4914 0.6117 0.0415  0.0265  0.0046  264 SER A OG  
2013 N N   . ALA A 279 ? 0.5699 0.4160 0.5596 0.0284  0.0591  0.0046  265 ALA A N   
2014 C CA  . ALA A 279 ? 0.4687 0.3072 0.4629 0.0257  0.0676  0.0085  265 ALA A CA  
2015 C C   . ALA A 279 ? 0.5266 0.3658 0.5298 0.0189  0.0825  0.0080  265 ALA A C   
2016 O O   . ALA A 279 ? 0.7421 0.5753 0.7516 0.0153  0.0903  0.0109  265 ALA A O   
2017 C CB  . ALA A 279 ? 0.4954 0.3461 0.5119 0.0266  0.0614  0.0069  265 ALA A CB  
2018 N N   . SER A 280 ? 0.5175 0.3637 0.5235 0.0169  0.0868  0.0042  266 SER A N   
2019 C CA  . SER A 280 ? 0.5600 0.4088 0.5788 0.0112  0.1012  0.0036  266 SER A CA  
2020 C C   . SER A 280 ? 0.5979 0.4249 0.5955 0.0095  0.1149  0.0089  266 SER A C   
2021 O O   . SER A 280 ? 0.6386 0.4474 0.6052 0.0131  0.1132  0.0122  266 SER A O   
2022 C CB  . SER A 280 ? 0.5569 0.4162 0.5822 0.0106  0.1029  -0.0016 266 SER A CB  
2023 O OG  . SER A 280 ? 0.5218 0.3983 0.5620 0.0126  0.0906  -0.0058 266 SER A OG  
2024 N N   . ALA A 281 ? 0.5873 0.4162 0.6022 0.0037  0.1286  0.0099  267 ALA A N   
2025 C CA  . ALA A 281 ? 0.6750 0.4846 0.6729 0.0013  0.1455  0.0146  267 ALA A CA  
2026 C C   . ALA A 281 ? 0.7553 0.5561 0.7296 0.0038  0.1510  0.0125  267 ALA A C   
2027 O O   . ALA A 281 ? 0.8321 0.6461 0.8146 0.0051  0.1454  0.0067  267 ALA A O   
2028 C CB  . ALA A 281 ? 0.5453 0.3627 0.5733 -0.0057 0.1595  0.0150  267 ALA A CB  
2029 N N   . GLY A 282 ? 0.7206 0.4967 0.6628 0.0043  0.1619  0.0173  268 GLY A N   
2030 C CA  . GLY A 282 ? 0.7139 0.4771 0.6268 0.0068  0.1670  0.0150  268 GLY A CA  
2031 C C   . GLY A 282 ? 0.7442 0.5200 0.6782 0.0042  0.1785  0.0093  268 GLY A C   
2032 O O   . GLY A 282 ? 0.7956 0.5731 0.7201 0.0067  0.1742  0.0036  268 GLY A O   
2033 N N   . ALA A 283 ? 0.7023 0.4873 0.6671 -0.0010 0.1928  0.0106  269 ALA A N   
2034 C CA  . ALA A 283 ? 0.7270 0.5258 0.7172 -0.0029 0.2036  0.0058  269 ALA A CA  
2035 C C   . ALA A 283 ? 0.6396 0.4624 0.6545 -0.0013 0.1874  -0.0002 269 ALA A C   
2036 O O   . ALA A 283 ? 0.6472 0.4756 0.6668 0.0001  0.1903  -0.0053 269 ALA A O   
2037 C CB  . ALA A 283 ? 0.5286 0.3345 0.5518 -0.0088 0.2200  0.0090  269 ALA A CB  
2038 N N   . VAL A 284 ? 0.6920 0.5280 0.7222 -0.0014 0.1713  0.0004  270 VAL A N   
2039 C CA  . VAL A 284 ? 0.5621 0.4192 0.6135 0.0002  0.1567  -0.0045 270 VAL A CA  
2040 C C   . VAL A 284 ? 0.6394 0.4913 0.6663 0.0048  0.1464  -0.0085 270 VAL A C   
2041 O O   . VAL A 284 ? 0.6364 0.4991 0.6743 0.0058  0.1435  -0.0134 270 VAL A O   
2042 C CB  . VAL A 284 ? 0.5290 0.3978 0.5976 -0.0008 0.1434  -0.0031 270 VAL A CB  
2043 C CG1 . VAL A 284 ? 0.5080 0.3961 0.5942 0.0011  0.1293  -0.0075 270 VAL A CG1 
2044 C CG2 . VAL A 284 ? 0.5598 0.4340 0.6546 -0.0063 0.1522  -0.0003 270 VAL A CG2 
2045 N N   . LYS A 285 ? 0.6964 0.5317 0.6910 0.0076  0.1399  -0.0062 271 LYS A N   
2046 C CA  . LYS A 285 ? 0.6219 0.4515 0.5931 0.0115  0.1287  -0.0101 271 LYS A CA  
2047 C C   . LYS A 285 ? 0.6662 0.4871 0.6247 0.0114  0.1397  -0.0147 271 LYS A C   
2048 O O   . LYS A 285 ? 0.6601 0.4872 0.6203 0.0127  0.1322  -0.0205 271 LYS A O   
2049 C CB  . LYS A 285 ? 0.6023 0.4129 0.5395 0.0147  0.1210  -0.0059 271 LYS A CB  
2050 C CG  . LYS A 285 ? 0.7593 0.5760 0.6919 0.0187  0.1001  -0.0082 271 LYS A CG  
2051 C CD  . LYS A 285 ? 0.7911 0.5899 0.6941 0.0226  0.0917  -0.0029 271 LYS A CD  
2052 C CE  . LYS A 285 ? 0.8325 0.6304 0.7457 0.0220  0.0946  0.0037  271 LYS A CE  
2053 N NZ  . LYS A 285 ? 0.8495 0.6370 0.7443 0.0272  0.0811  0.0084  271 LYS A NZ  
2054 N N   . GLU A 286 ? 0.5995 0.4052 0.5459 0.0097  0.1585  -0.0123 272 GLU A N   
2055 C CA  . GLU A 286 ? 0.7646 0.5598 0.6978 0.0100  0.1716  -0.0170 272 GLU A CA  
2056 C C   . GLU A 286 ? 0.7643 0.5801 0.7361 0.0086  0.1773  -0.0212 272 GLU A C   
2057 O O   . GLU A 286 ? 0.6836 0.4979 0.6513 0.0100  0.1787  -0.0273 272 GLU A O   
2058 C CB  . GLU A 286 ? 0.7564 0.5290 0.6667 0.0088  0.1927  -0.0127 272 GLU A CB  
2059 C CG  . GLU A 286 ? 0.8878 0.6446 0.7776 0.0096  0.2087  -0.0177 272 GLU A CG  
2060 C CD  . GLU A 286 ? 0.9696 0.7198 0.8351 0.0126  0.1949  -0.0251 272 GLU A CD  
2061 O OE1 . GLU A 286 ? 0.9721 0.7327 0.8555 0.0128  0.1962  -0.0317 272 GLU A OE1 
2062 O OE2 . GLU A 286 ? 1.0449 0.7794 0.8744 0.0147  0.1820  -0.0242 272 GLU A OE2 
2063 N N   . ALA A 287 ? 0.6619 0.4959 0.6708 0.0059  0.1797  -0.0180 273 ALA A N   
2064 C CA  . ALA A 287 ? 0.6103 0.4638 0.6568 0.0051  0.1839  -0.0209 273 ALA A CA  
2065 C C   . ALA A 287 ? 0.7385 0.6052 0.7937 0.0072  0.1673  -0.0256 273 ALA A C   
2066 O O   . ALA A 287 ? 0.5952 0.4658 0.6600 0.0084  0.1712  -0.0302 273 ALA A O   
2067 C CB  . ALA A 287 ? 0.5295 0.3995 0.6123 0.0015  0.1861  -0.0165 273 ALA A CB  
2068 N N   . ILE A 288 ? 0.6414 0.5143 0.6940 0.0078  0.1497  -0.0245 274 ILE A N   
2069 C CA  . ILE A 288 ? 0.6460 0.5329 0.7109 0.0092  0.1350  -0.0280 274 ILE A CA  
2070 C C   . ILE A 288 ? 0.5375 0.4122 0.5732 0.0114  0.1266  -0.0324 274 ILE A C   
2071 O O   . ILE A 288 ? 0.5925 0.4666 0.6282 0.0121  0.1272  -0.0377 274 ILE A O   
2072 C CB  . ILE A 288 ? 0.6465 0.5480 0.7281 0.0087  0.1217  -0.0249 274 ILE A CB  
2073 C CG1 . ILE A 288 ? 0.5870 0.4992 0.6961 0.0058  0.1283  -0.0213 274 ILE A CG1 
2074 C CG2 . ILE A 288 ? 0.4855 0.4006 0.5799 0.0100  0.1091  -0.0280 274 ILE A CG2 
2075 C CD1 . ILE A 288 ? 0.5178 0.4412 0.6539 0.0053  0.1360  -0.0230 274 ILE A CD1 
2076 N N   . GLU A 289 ? 0.6039 0.4681 0.6149 0.0126  0.1181  -0.0303 275 GLU A N   
2077 C CA  . GLU A 289 ? 0.5245 0.3788 0.5100 0.0145  0.1066  -0.0343 275 GLU A CA  
2078 C C   . GLU A 289 ? 0.6115 0.4447 0.5675 0.0148  0.1167  -0.0384 275 GLU A C   
2079 O O   . GLU A 289 ? 0.6684 0.4943 0.6072 0.0155  0.1078  -0.0440 275 GLU A O   
2080 C CB  . GLU A 289 ? 0.5212 0.3695 0.4892 0.0165  0.0944  -0.0302 275 GLU A CB  
2081 C CG  . GLU A 289 ? 0.5384 0.4060 0.5318 0.0170  0.0822  -0.0280 275 GLU A CG  
2082 C CD  . GLU A 289 ? 0.6811 0.5426 0.6593 0.0199  0.0703  -0.0243 275 GLU A CD  
2083 O OE1 . GLU A 289 ? 0.6470 0.4889 0.5936 0.0215  0.0704  -0.0227 275 GLU A OE1 
2084 O OE2 . GLU A 289 ? 0.5658 0.4412 0.5627 0.0211  0.0610  -0.0228 275 GLU A OE2 
2085 N N   . GLY A 290 ? 0.5714 0.3938 0.5212 0.0139  0.1353  -0.0362 276 GLY A N   
2086 C CA  . GLY A 290 ? 0.6643 0.4646 0.5843 0.0144  0.1477  -0.0404 276 GLY A CA  
2087 C C   . GLY A 290 ? 0.5893 0.3941 0.5249 0.0141  0.1563  -0.0470 276 GLY A C   
2088 O O   . GLY A 290 ? 0.6659 0.4514 0.5748 0.0149  0.1643  -0.0525 276 GLY A O   
2089 N N   . ALA A 291 ? 0.5616 0.3895 0.5380 0.0134  0.1549  -0.0466 277 ALA A N   
2090 C CA  . ALA A 291 ? 0.5790 0.4118 0.5730 0.0139  0.1615  -0.0521 277 ALA A CA  
2091 C C   . ALA A 291 ? 0.6244 0.4541 0.6066 0.0142  0.1471  -0.0590 277 ALA A C   
2092 O O   . ALA A 291 ? 0.5794 0.4147 0.5578 0.0139  0.1293  -0.0584 277 ALA A O   
2093 C CB  . ALA A 291 ? 0.5037 0.3617 0.5435 0.0134  0.1617  -0.0487 277 ALA A CB  
2094 N N   . ASP A 292 ? 0.5284 0.3485 0.5060 0.0149  0.1556  -0.0659 278 ASP A N   
2095 C CA  . ASP A 292 ? 0.6405 0.4572 0.6101 0.0143  0.1426  -0.0731 278 ASP A CA  
2096 C C   . ASP A 292 ? 0.6103 0.4497 0.6183 0.0138  0.1341  -0.0723 278 ASP A C   
2097 O O   . ASP A 292 ? 0.5925 0.4337 0.5997 0.0125  0.1205  -0.0766 278 ASP A O   
2098 C CB  . ASP A 292 ? 0.6875 0.4821 0.6348 0.0149  0.1548  -0.0816 278 ASP A CB  
2099 C CG  . ASP A 292 ? 0.8232 0.6213 0.7946 0.0168  0.1755  -0.0813 278 ASP A CG  
2100 O OD1 . ASP A 292 ? 0.8786 0.6938 0.8852 0.0173  0.1737  -0.0808 278 ASP A OD1 
2101 O OD2 . ASP A 292 ? 0.7985 0.5820 0.7544 0.0179  0.1938  -0.0810 278 ASP A OD2 
2102 N N   . THR A 293 ? 0.5139 0.3702 0.5550 0.0146  0.1413  -0.0669 279 THR A N   
2103 C CA  . THR A 293 ? 0.5178 0.3945 0.5927 0.0145  0.1332  -0.0647 279 THR A CA  
2104 C C   . THR A 293 ? 0.5366 0.4308 0.6339 0.0145  0.1317  -0.0565 279 THR A C   
2105 O O   . THR A 293 ? 0.5137 0.4094 0.6210 0.0150  0.1441  -0.0532 279 THR A O   
2106 C CB  . THR A 293 ? 0.6068 0.4839 0.7011 0.0162  0.1435  -0.0677 279 THR A CB  
2107 O OG1 . THR A 293 ? 0.6419 0.4998 0.7130 0.0159  0.1458  -0.0764 279 THR A OG1 
2108 C CG2 . THR A 293 ? 0.6466 0.5423 0.7717 0.0163  0.1341  -0.0646 279 THR A CG2 
2109 N N   . VAL A 294 ? 0.4679 0.3750 0.5738 0.0136  0.1170  -0.0535 280 VAL A N   
2110 C CA  . VAL A 294 ? 0.4190 0.3414 0.5439 0.0133  0.1137  -0.0468 280 VAL A CA  
2111 C C   . VAL A 294 ? 0.3787 0.3170 0.5297 0.0136  0.1064  -0.0449 280 VAL A C   
2112 O O   . VAL A 294 ? 0.3641 0.3043 0.5132 0.0131  0.0967  -0.0470 280 VAL A O   
2113 C CB  . VAL A 294 ? 0.4563 0.3770 0.5647 0.0126  0.1043  -0.0443 280 VAL A CB  
2114 C CG1 . VAL A 294 ? 0.4280 0.3632 0.5558 0.0121  0.1008  -0.0384 280 VAL A CG1 
2115 C CG2 . VAL A 294 ? 0.4124 0.3151 0.4928 0.0126  0.1122  -0.0448 280 VAL A CG2 
2116 N N   . LEU A 295 ? 0.3856 0.3348 0.5610 0.0143  0.1109  -0.0409 281 LEU A N   
2117 C CA  . LEU A 295 ? 0.3542 0.3173 0.5520 0.0149  0.1037  -0.0378 281 LEU A CA  
2118 C C   . LEU A 295 ? 0.4175 0.3900 0.6174 0.0138  0.0941  -0.0335 281 LEU A C   
2119 O O   . LEU A 295 ? 0.4273 0.4035 0.6331 0.0130  0.0964  -0.0305 281 LEU A O   
2120 C CB  . LEU A 295 ? 0.2935 0.2629 0.5162 0.0168  0.1115  -0.0355 281 LEU A CB  
2121 C CG  . LEU A 295 ? 0.4381 0.3966 0.6592 0.0184  0.1252  -0.0397 281 LEU A CG  
2122 C CD1 . LEU A 295 ? 0.5194 0.4866 0.7707 0.0211  0.1321  -0.0368 281 LEU A CD1 
2123 C CD2 . LEU A 295 ? 0.3559 0.3040 0.5634 0.0187  0.1234  -0.0454 281 LEU A CD2 
2124 N N   . CYS A 296 ? 0.3522 0.3279 0.5478 0.0135  0.0841  -0.0337 282 CYS A N   
2125 C CA  . CYS A 296 ? 0.2730 0.2561 0.4690 0.0130  0.0758  -0.0304 282 CYS A CA  
2126 C C   . CYS A 296 ? 0.3403 0.3337 0.5538 0.0137  0.0715  -0.0269 282 CYS A C   
2127 O O   . CYS A 296 ? 0.3852 0.3801 0.6014 0.0141  0.0683  -0.0272 282 CYS A O   
2128 C CB  . CYS A 296 ? 0.3005 0.2804 0.4817 0.0128  0.0686  -0.0325 282 CYS A CB  
2129 S SG  . CYS A 296 ? 0.4434 0.4087 0.5997 0.0126  0.0708  -0.0362 282 CYS A SG  
2130 N N   . ILE A 297 ? 0.2865 0.2863 0.5110 0.0135  0.0710  -0.0234 283 ILE A N   
2131 C CA  . ILE A 297 ? 0.3438 0.3517 0.5830 0.0145  0.0664  -0.0196 283 ILE A CA  
2132 C C   . ILE A 297 ? 0.2997 0.3113 0.5337 0.0137  0.0586  -0.0176 283 ILE A C   
2133 O O   . ILE A 297 ? 0.3135 0.3261 0.5479 0.0123  0.0576  -0.0170 283 ILE A O   
2134 C CB  . ILE A 297 ? 0.2391 0.2517 0.4972 0.0150  0.0702  -0.0175 283 ILE A CB  
2135 C CG1 . ILE A 297 ? 0.3530 0.3599 0.6145 0.0161  0.0808  -0.0204 283 ILE A CG1 
2136 C CG2 . ILE A 297 ? 0.2331 0.2528 0.5048 0.0167  0.0636  -0.0132 283 ILE A CG2 
2137 C CD1 . ILE A 297 ? 0.2412 0.2436 0.5013 0.0179  0.0819  -0.0221 283 ILE A CD1 
2138 N N   . GLY A 298 ? 0.2237 0.2365 0.4536 0.0145  0.0540  -0.0166 284 GLY A N   
2139 C CA  . GLY A 298 ? 0.3047 0.3193 0.5280 0.0143  0.0482  -0.0151 284 GLY A CA  
2140 C C   . GLY A 298 ? 0.3852 0.3963 0.5967 0.0136  0.0478  -0.0174 284 GLY A C   
2141 O O   . GLY A 298 ? 0.3824 0.3934 0.5906 0.0129  0.0448  -0.0169 284 GLY A O   
2142 N N   . THR A 299 ? 0.3250 0.3323 0.5296 0.0138  0.0501  -0.0202 285 THR A N   
2143 C CA  . THR A 299 ? 0.3181 0.3208 0.5113 0.0138  0.0494  -0.0218 285 THR A CA  
2144 C C   . THR A 299 ? 0.4334 0.4375 0.6221 0.0153  0.0455  -0.0225 285 THR A C   
2145 O O   . THR A 299 ? 0.3045 0.3114 0.4977 0.0155  0.0451  -0.0230 285 THR A O   
2146 C CB  . THR A 299 ? 0.3385 0.3345 0.5247 0.0135  0.0535  -0.0243 285 THR A CB  
2147 O OG1 . THR A 299 ? 0.4601 0.4559 0.6488 0.0136  0.0544  -0.0263 285 THR A OG1 
2148 C CG2 . THR A 299 ? 0.2499 0.2435 0.4402 0.0121  0.0596  -0.0235 285 THR A CG2 
2149 N N   . ARG A 300 ? 0.3593 0.3614 0.5413 0.0163  0.0433  -0.0224 286 ARG A N   
2150 C CA  . ARG A 300 ? 0.3616 0.3649 0.5412 0.0185  0.0404  -0.0231 286 ARG A CA  
2151 C C   . ARG A 300 ? 0.4051 0.4022 0.5751 0.0199  0.0387  -0.0238 286 ARG A C   
2152 O O   . ARG A 300 ? 0.3760 0.3685 0.5411 0.0198  0.0394  -0.0228 286 ARG A O   
2153 C CB  . ARG A 300 ? 0.3535 0.3597 0.5348 0.0196  0.0400  -0.0218 286 ARG A CB  
2154 C CG  . ARG A 300 ? 0.3691 0.3795 0.5566 0.0187  0.0414  -0.0200 286 ARG A CG  
2155 C CD  . ARG A 300 ? 0.3695 0.3837 0.5643 0.0186  0.0424  -0.0205 286 ARG A CD  
2156 N NE  . ARG A 300 ? 0.3112 0.3269 0.5116 0.0175  0.0443  -0.0182 286 ARG A NE  
2157 C CZ  . ARG A 300 ? 0.3509 0.3676 0.5517 0.0180  0.0459  -0.0155 286 ARG A CZ  
2158 N NH1 . ARG A 300 ? 0.3083 0.3248 0.5043 0.0196  0.0470  -0.0153 286 ARG A NH1 
2159 N NH2 . ARG A 300 ? 0.2279 0.2443 0.4329 0.0174  0.0472  -0.0126 286 ARG A NH2 
2160 N N   . PHE A 301 ? 0.3543 0.3501 0.5211 0.0210  0.0359  -0.0253 287 PHE A N   
2161 C CA  . PHE A 301 ? 0.4274 0.4152 0.5823 0.0227  0.0333  -0.0252 287 PHE A CA  
2162 C C   . PHE A 301 ? 0.4291 0.4185 0.5858 0.0264  0.0295  -0.0244 287 PHE A C   
2163 O O   . PHE A 301 ? 0.3609 0.3532 0.5206 0.0288  0.0242  -0.0252 287 PHE A O   
2164 C CB  . PHE A 301 ? 0.3685 0.3524 0.5166 0.0224  0.0305  -0.0274 287 PHE A CB  
2165 C CG  . PHE A 301 ? 0.4282 0.4074 0.5721 0.0195  0.0361  -0.0286 287 PHE A CG  
2166 C CD1 . PHE A 301 ? 0.3775 0.3476 0.5109 0.0187  0.0415  -0.0273 287 PHE A CD1 
2167 C CD2 . PHE A 301 ? 0.4284 0.4118 0.5804 0.0177  0.0373  -0.0309 287 PHE A CD2 
2168 C CE1 . PHE A 301 ? 0.4418 0.4079 0.5736 0.0165  0.0486  -0.0284 287 PHE A CE1 
2169 C CE2 . PHE A 301 ? 0.4042 0.3827 0.5537 0.0158  0.0434  -0.0322 287 PHE A CE2 
2170 C CZ  . PHE A 301 ? 0.4770 0.4473 0.6168 0.0155  0.0494  -0.0311 287 PHE A CZ  
2171 N N   . THR A 302 ? 0.3297 0.3169 0.4854 0.0270  0.0319  -0.0231 288 THR A N   
2172 C CA  . THR A 302 ? 0.3319 0.3188 0.4889 0.0310  0.0299  -0.0226 288 THR A CA  
2173 C C   . THR A 302 ? 0.2737 0.2510 0.4203 0.0339  0.0267  -0.0211 288 THR A C   
2174 O O   . THR A 302 ? 0.3666 0.3359 0.5022 0.0322  0.0272  -0.0202 288 THR A O   
2175 C CB  . THR A 302 ? 0.3174 0.3029 0.4748 0.0304  0.0335  -0.0226 288 THR A CB  
2176 O OG1 . THR A 302 ? 0.4153 0.3912 0.5639 0.0288  0.0348  -0.0217 288 THR A OG1 
2177 C CG2 . THR A 302 ? 0.3439 0.3358 0.5070 0.0272  0.0361  -0.0230 288 THR A CG2 
2178 N N   . ASP A 303 ? 0.2996 0.2768 0.4493 0.0387  0.0240  -0.0206 289 ASP A N   
2179 C CA  . ASP A 303 ? 0.3336 0.3012 0.4739 0.0426  0.0196  -0.0183 289 ASP A CA  
2180 C C   . ASP A 303 ? 0.4380 0.3920 0.5649 0.0408  0.0237  -0.0164 289 ASP A C   
2181 O O   . ASP A 303 ? 0.3940 0.3376 0.5076 0.0409  0.0224  -0.0139 289 ASP A O   
2182 C CB  . ASP A 303 ? 0.3591 0.3299 0.5091 0.0489  0.0166  -0.0180 289 ASP A CB  
2183 C CG  . ASP A 303 ? 0.4125 0.3831 0.5672 0.0496  0.0231  -0.0192 289 ASP A CG  
2184 O OD1 . ASP A 303 ? 0.4906 0.4604 0.6421 0.0449  0.0281  -0.0205 289 ASP A OD1 
2185 O OD2 . ASP A 303 ? 0.4131 0.3840 0.5748 0.0552  0.0228  -0.0191 289 ASP A OD2 
2186 N N   . THR A 304 ? 0.3798 0.3328 0.5096 0.0386  0.0288  -0.0174 290 THR A N   
2187 C CA  . THR A 304 ? 0.4138 0.3545 0.5345 0.0358  0.0326  -0.0159 290 THR A CA  
2188 C C   . THR A 304 ? 0.4960 0.4353 0.6126 0.0303  0.0362  -0.0153 290 THR A C   
2189 O O   . THR A 304 ? 0.4259 0.3537 0.5320 0.0291  0.0389  -0.0126 290 THR A O   
2190 C CB  . THR A 304 ? 0.4200 0.3600 0.5451 0.0342  0.0355  -0.0182 290 THR A CB  
2191 O OG1 . THR A 304 ? 0.5680 0.5065 0.6953 0.0399  0.0342  -0.0190 290 THR A OG1 
2192 C CG2 . THR A 304 ? 0.5603 0.4884 0.6794 0.0300  0.0389  -0.0173 290 THR A CG2 
2193 N N   . LEU A 305 ? 0.3934 0.3434 0.5185 0.0273  0.0373  -0.0173 291 LEU A N   
2194 C CA  . LEU A 305 ? 0.4465 0.3962 0.5713 0.0226  0.0419  -0.0170 291 LEU A CA  
2195 C C   . LEU A 305 ? 0.4287 0.3712 0.5410 0.0236  0.0424  -0.0156 291 LEU A C   
2196 O O   . LEU A 305 ? 0.5220 0.4584 0.6292 0.0204  0.0486  -0.0145 291 LEU A O   
2197 C CB  . LEU A 305 ? 0.3276 0.2896 0.4644 0.0205  0.0422  -0.0191 291 LEU A CB  
2198 C CG  . LEU A 305 ? 0.3899 0.3560 0.5360 0.0170  0.0436  -0.0198 291 LEU A CG  
2199 C CD1 . LEU A 305 ? 0.3483 0.3117 0.4928 0.0187  0.0410  -0.0207 291 LEU A CD1 
2200 C CD2 . LEU A 305 ? 0.3936 0.3706 0.5497 0.0160  0.0430  -0.0207 291 LEU A CD2 
2201 N N   . THR A 306 ? 0.4298 0.3727 0.5372 0.0278  0.0360  -0.0158 292 THR A N   
2202 C CA  . THR A 306 ? 0.4970 0.4322 0.5895 0.0288  0.0341  -0.0152 292 THR A CA  
2203 C C   . THR A 306 ? 0.5426 0.4649 0.6197 0.0331  0.0298  -0.0117 292 THR A C   
2204 O O   . THR A 306 ? 0.5483 0.4636 0.6108 0.0351  0.0249  -0.0111 292 THR A O   
2205 C CB  . THR A 306 ? 0.5368 0.4818 0.6355 0.0296  0.0282  -0.0184 292 THR A CB  
2206 O OG1 . THR A 306 ? 0.4407 0.3943 0.5508 0.0333  0.0216  -0.0188 292 THR A OG1 
2207 C CG2 . THR A 306 ? 0.3789 0.3334 0.4901 0.0256  0.0333  -0.0210 292 THR A CG2 
2208 N N   . ALA A 307 ? 0.5509 0.4687 0.6299 0.0347  0.0307  -0.0094 293 ALA A N   
2209 C CA  . ALA A 307 ? 0.5972 0.5015 0.6628 0.0395  0.0267  -0.0052 293 ALA A CA  
2210 C C   . ALA A 307 ? 0.5317 0.4395 0.5959 0.0453  0.0153  -0.0052 293 ALA A C   
2211 O O   . ALA A 307 ? 0.6958 0.5922 0.7419 0.0480  0.0101  -0.0024 293 ALA A O   
2212 C CB  . ALA A 307 ? 0.5037 0.3901 0.5484 0.0374  0.0330  -0.0013 293 ALA A CB  
2213 N N   . GLY A 308 ? 0.5373 0.4609 0.6210 0.0470  0.0112  -0.0084 294 GLY A N   
2214 C CA  . GLY A 308 ? 0.4872 0.4172 0.5766 0.0520  0.0001  -0.0087 294 GLY A CA  
2215 C C   . GLY A 308 ? 0.4930 0.4298 0.5823 0.0494  -0.0046 -0.0121 294 GLY A C   
2216 O O   . GLY A 308 ? 0.5262 0.4607 0.6092 0.0524  -0.0152 -0.0117 294 GLY A O   
2217 N N   . PHE A 309 ? 0.5063 0.4504 0.6024 0.0438  0.0023  -0.0154 295 PHE A N   
2218 C CA  . PHE A 309 ? 0.4740 0.4235 0.5712 0.0407  -0.0006 -0.0193 295 PHE A CA  
2219 C C   . PHE A 309 ? 0.4384 0.3728 0.5102 0.0404  -0.0042 -0.0190 295 PHE A C   
2220 O O   . PHE A 309 ? 0.5198 0.4552 0.5884 0.0404  -0.0130 -0.0219 295 PHE A O   
2221 C CB  . PHE A 309 ? 0.4280 0.3921 0.5453 0.0426  -0.0091 -0.0217 295 PHE A CB  
2222 C CG  . PHE A 309 ? 0.4458 0.4229 0.5853 0.0430  -0.0038 -0.0220 295 PHE A CG  
2223 C CD1 . PHE A 309 ? 0.3329 0.3149 0.4786 0.0385  0.0052  -0.0235 295 PHE A CD1 
2224 C CD2 . PHE A 309 ? 0.4397 0.4232 0.5931 0.0482  -0.0076 -0.0207 295 PHE A CD2 
2225 C CE1 . PHE A 309 ? 0.3965 0.3879 0.5578 0.0390  0.0099  -0.0236 295 PHE A CE1 
2226 C CE2 . PHE A 309 ? 0.4529 0.4460 0.6234 0.0487  -0.0011 -0.0213 295 PHE A CE2 
2227 C CZ  . PHE A 309 ? 0.3836 0.3798 0.5561 0.0439  0.0075  -0.0228 295 PHE A CZ  
2228 N N   . THR A 310 ? 0.4518 0.3712 0.5046 0.0399  0.0028  -0.0156 296 THR A N   
2229 C CA  . THR A 310 ? 0.5210 0.4226 0.5451 0.0397  0.0023  -0.0147 296 THR A CA  
2230 C C   . THR A 310 ? 0.5636 0.4614 0.5810 0.0343  0.0135  -0.0176 296 THR A C   
2231 O O   . THR A 310 ? 0.5226 0.4033 0.5144 0.0336  0.0177  -0.0167 296 THR A O   
2232 C CB  . THR A 310 ? 0.5929 0.4777 0.5984 0.0427  0.0044  -0.0083 296 THR A CB  
2233 O OG1 . THR A 310 ? 0.6567 0.5409 0.6693 0.0394  0.0175  -0.0066 296 THR A OG1 
2234 C CG2 . THR A 310 ? 0.5496 0.4370 0.5620 0.0492  -0.0071 -0.0052 296 THR A CG2 
2235 N N   . HIS A 311 ? 0.4725 0.3845 0.5115 0.0309  0.0190  -0.0209 297 HIS A N   
2236 C CA  . HIS A 311 ? 0.4827 0.3925 0.5193 0.0267  0.0288  -0.0239 297 HIS A CA  
2237 C C   . HIS A 311 ? 0.4958 0.3998 0.5186 0.0263  0.0228  -0.0287 297 HIS A C   
2238 O O   . HIS A 311 ? 0.6093 0.5200 0.6380 0.0277  0.0105  -0.0310 297 HIS A O   
2239 C CB  . HIS A 311 ? 0.4164 0.3427 0.4799 0.0240  0.0338  -0.0257 297 HIS A CB  
2240 C CG  . HIS A 311 ? 0.4721 0.4130 0.5538 0.0248  0.0250  -0.0281 297 HIS A CG  
2241 N ND1 . HIS A 311 ? 0.4218 0.3686 0.5108 0.0282  0.0168  -0.0264 297 HIS A ND1 
2242 C CD2 . HIS A 311 ? 0.3984 0.3488 0.4937 0.0227  0.0245  -0.0318 297 HIS A CD2 
2243 C CE1 . HIS A 311 ? 0.4709 0.4307 0.5778 0.0279  0.0122  -0.0290 297 HIS A CE1 
2244 N NE2 . HIS A 311 ? 0.4792 0.4411 0.5897 0.0243  0.0166  -0.0321 297 HIS A NE2 
2245 N N   . GLN A 312 ? 0.5218 0.4129 0.5270 0.0241  0.0319  -0.0305 298 GLN A N   
2246 C CA  . GLN A 312 ? 0.5874 0.4689 0.5749 0.0233  0.0277  -0.0361 298 GLN A CA  
2247 C C   . GLN A 312 ? 0.6301 0.5158 0.6293 0.0198  0.0384  -0.0406 298 GLN A C   
2248 O O   . GLN A 312 ? 0.6129 0.4869 0.5993 0.0186  0.0514  -0.0411 298 GLN A O   
2249 C CB  . GLN A 312 ? 0.5695 0.4271 0.5191 0.0248  0.0291  -0.0345 298 GLN A CB  
2250 C CG  . GLN A 312 ? 0.7720 0.6234 0.7096 0.0290  0.0199  -0.0284 298 GLN A CG  
2251 C CD  . GLN A 312 ? 0.9250 0.7530 0.8226 0.0312  0.0136  -0.0281 298 GLN A CD  
2252 O OE1 . GLN A 312 ? 1.1329 0.9562 1.0180 0.0307  0.0039  -0.0338 298 GLN A OE1 
2253 N NE2 . GLN A 312 ? 0.9299 0.7415 0.8056 0.0334  0.0189  -0.0213 298 GLN A NE2 
2254 N N   . LEU A 313 ? 0.4863 0.3880 0.5103 0.0185  0.0337  -0.0435 299 LEU A N   
2255 C CA  . LEU A 313 ? 0.6088 0.5145 0.6455 0.0158  0.0419  -0.0475 299 LEU A CA  
2256 C C   . LEU A 313 ? 0.5634 0.4752 0.6091 0.0144  0.0312  -0.0529 299 LEU A C   
2257 O O   . LEU A 313 ? 0.5504 0.4766 0.6154 0.0148  0.0228  -0.0515 299 LEU A O   
2258 C CB  . LEU A 313 ? 0.4433 0.3635 0.5068 0.0152  0.0499  -0.0438 299 LEU A CB  
2259 C CG  . LEU A 313 ? 0.4895 0.4056 0.5507 0.0153  0.0613  -0.0392 299 LEU A CG  
2260 C CD1 . LEU A 313 ? 0.4590 0.3911 0.5468 0.0148  0.0631  -0.0356 299 LEU A CD1 
2261 C CD2 . LEU A 313 ? 0.4922 0.3968 0.5441 0.0142  0.0750  -0.0415 299 LEU A CD2 
2262 N N   . THR A 314 ? 0.5319 0.4319 0.5636 0.0126  0.0322  -0.0592 300 THR A N   
2263 C CA  . THR A 314 ? 0.5381 0.4418 0.5778 0.0103  0.0217  -0.0651 300 THR A CA  
2264 C C   . THR A 314 ? 0.6205 0.5344 0.6859 0.0081  0.0289  -0.0664 300 THR A C   
2265 O O   . THR A 314 ? 0.5193 0.4332 0.5906 0.0086  0.0420  -0.0644 300 THR A O   
2266 C CB  . THR A 314 ? 0.5303 0.4139 0.5399 0.0090  0.0176  -0.0722 300 THR A CB  
2267 O OG1 . THR A 314 ? 0.6624 0.5345 0.6641 0.0080  0.0322  -0.0759 300 THR A OG1 
2268 C CG2 . THR A 314 ? 0.5306 0.3999 0.5088 0.0118  0.0123  -0.0698 300 THR A CG2 
2269 N N   . PRO A 315 ? 0.5890 0.5119 0.6719 0.0057  0.0205  -0.0694 301 PRO A N   
2270 C CA  . PRO A 315 ? 0.4420 0.3719 0.5472 0.0037  0.0275  -0.0701 301 PRO A CA  
2271 C C   . PRO A 315 ? 0.4977 0.4133 0.5926 0.0029  0.0379  -0.0750 301 PRO A C   
2272 O O   . PRO A 315 ? 0.4868 0.4064 0.5966 0.0036  0.0485  -0.0725 301 PRO A O   
2273 C CB  . PRO A 315 ? 0.4042 0.3419 0.5248 0.0006  0.0159  -0.0734 301 PRO A CB  
2274 C CG  . PRO A 315 ? 0.4848 0.4287 0.6028 0.0023  0.0041  -0.0710 301 PRO A CG  
2275 C CD  . PRO A 315 ? 0.4745 0.4041 0.5623 0.0051  0.0048  -0.0706 301 PRO A CD  
2276 N N   . SER A 316 ? 0.5378 0.4357 0.6067 0.0018  0.0353  -0.0819 302 SER A N   
2277 C CA  . SER A 316 ? 0.4931 0.3752 0.5504 0.0014  0.0468  -0.0874 302 SER A CA  
2278 C C   . SER A 316 ? 0.5913 0.4692 0.6420 0.0047  0.0621  -0.0830 302 SER A C   
2279 O O   . SER A 316 ? 0.5939 0.4658 0.6486 0.0055  0.0752  -0.0849 302 SER A O   
2280 C CB  . SER A 316 ? 0.6245 0.4863 0.6513 -0.0007 0.0399  -0.0965 302 SER A CB  
2281 O OG  . SER A 316 ? 0.8790 0.7325 0.8786 0.0012  0.0345  -0.0948 302 SER A OG  
2282 N N   . GLN A 317 ? 0.5647 0.4456 0.6075 0.0067  0.0611  -0.0772 303 GLN A N   
2283 C CA  . GLN A 317 ? 0.5304 0.4081 0.5694 0.0091  0.0753  -0.0727 303 GLN A CA  
2284 C C   . GLN A 317 ? 0.5371 0.4326 0.6085 0.0100  0.0819  -0.0666 303 GLN A C   
2285 O O   . GLN A 317 ? 0.5277 0.4221 0.6035 0.0114  0.0948  -0.0640 303 GLN A O   
2286 C CB  . GLN A 317 ? 0.4950 0.3683 0.5141 0.0104  0.0711  -0.0684 303 GLN A CB  
2287 C CG  . GLN A 317 ? 0.5209 0.3881 0.5328 0.0120  0.0860  -0.0637 303 GLN A CG  
2288 C CD  . GLN A 317 ? 0.6627 0.5261 0.6579 0.0132  0.0808  -0.0584 303 GLN A CD  
2289 O OE1 . GLN A 317 ? 0.6699 0.5381 0.6632 0.0136  0.0658  -0.0574 303 GLN A OE1 
2290 N NE2 . GLN A 317 ? 0.5517 0.4061 0.5366 0.0139  0.0940  -0.0546 303 GLN A NE2 
2291 N N   . THR A 318 ? 0.4472 0.3584 0.5415 0.0092  0.0735  -0.0644 304 THR A N   
2292 C CA  . THR A 318 ? 0.4106 0.3379 0.5304 0.0103  0.0765  -0.0578 304 THR A CA  
2293 C C   . THR A 318 ? 0.4633 0.3977 0.6056 0.0100  0.0779  -0.0579 304 THR A C   
2294 O O   . THR A 318 ? 0.4977 0.4291 0.6407 0.0081  0.0732  -0.0623 304 THR A O   
2295 C CB  . THR A 318 ? 0.3621 0.3011 0.4868 0.0104  0.0664  -0.0530 304 THR A CB  
2296 O OG1 . THR A 318 ? 0.4344 0.3754 0.5584 0.0090  0.0550  -0.0560 304 THR A OG1 
2297 C CG2 . THR A 318 ? 0.3944 0.3269 0.5010 0.0115  0.0670  -0.0507 304 THR A CG2 
2298 N N   . ILE A 319 ? 0.4290 0.3721 0.5900 0.0116  0.0843  -0.0529 305 ILE A N   
2299 C CA  . ILE A 319 ? 0.3768 0.3292 0.5604 0.0122  0.0837  -0.0499 305 ILE A CA  
2300 C C   . ILE A 319 ? 0.4207 0.3871 0.6158 0.0128  0.0787  -0.0430 305 ILE A C   
2301 O O   . ILE A 319 ? 0.3398 0.3089 0.5348 0.0135  0.0814  -0.0401 305 ILE A O   
2302 C CB  . ILE A 319 ? 0.3008 0.2498 0.4965 0.0144  0.0947  -0.0501 305 ILE A CB  
2303 C CG1 . ILE A 319 ? 0.3246 0.2573 0.5071 0.0139  0.1004  -0.0579 305 ILE A CG1 
2304 C CG2 . ILE A 319 ? 0.2864 0.2450 0.5050 0.0158  0.0927  -0.0451 305 ILE A CG2 
2305 C CD1 . ILE A 319 ? 0.3304 0.2576 0.5225 0.0169  0.1139  -0.0588 305 ILE A CD1 
2306 N N   . GLU A 320 ? 0.3233 0.2971 0.5269 0.0120  0.0718  -0.0408 306 GLU A N   
2307 C CA  . GLU A 320 ? 0.4134 0.3976 0.6221 0.0124  0.0664  -0.0355 306 GLU A CA  
2308 C C   . GLU A 320 ? 0.3864 0.3773 0.6112 0.0136  0.0663  -0.0305 306 GLU A C   
2309 O O   . GLU A 320 ? 0.3412 0.3299 0.5722 0.0131  0.0669  -0.0310 306 GLU A O   
2310 C CB  . GLU A 320 ? 0.3449 0.3310 0.5465 0.0110  0.0589  -0.0369 306 GLU A CB  
2311 C CG  . GLU A 320 ? 0.4185 0.4140 0.6252 0.0117  0.0546  -0.0322 306 GLU A CG  
2312 C CD  . GLU A 320 ? 0.5772 0.5752 0.7804 0.0110  0.0484  -0.0338 306 GLU A CD  
2313 O OE1 . GLU A 320 ? 0.4101 0.4033 0.6071 0.0098  0.0455  -0.0385 306 GLU A OE1 
2314 O OE2 . GLU A 320 ? 0.5207 0.5253 0.7279 0.0119  0.0463  -0.0306 306 GLU A OE2 
2315 N N   . VAL A 321 ? 0.2684 0.2659 0.4988 0.0148  0.0651  -0.0257 307 VAL A N   
2316 C CA  . VAL A 321 ? 0.2858 0.2883 0.5280 0.0163  0.0632  -0.0202 307 VAL A CA  
2317 C C   . VAL A 321 ? 0.3307 0.3385 0.5681 0.0160  0.0573  -0.0170 307 VAL A C   
2318 O O   . VAL A 321 ? 0.2699 0.2801 0.5028 0.0158  0.0554  -0.0168 307 VAL A O   
2319 C CB  . VAL A 321 ? 0.2319 0.2367 0.4865 0.0184  0.0660  -0.0176 307 VAL A CB  
2320 C CG1 . VAL A 321 ? 0.2357 0.2455 0.4994 0.0203  0.0610  -0.0111 307 VAL A CG1 
2321 C CG2 . VAL A 321 ? 0.2392 0.2377 0.4999 0.0195  0.0737  -0.0207 307 VAL A CG2 
2322 N N   . GLN A 322 ? 0.2440 0.2526 0.4823 0.0160  0.0556  -0.0145 308 GLN A N   
2323 C CA  . GLN A 322 ? 0.3237 0.3354 0.5561 0.0161  0.0520  -0.0115 308 GLN A CA  
2324 C C   . GLN A 322 ? 0.2675 0.2789 0.5034 0.0178  0.0506  -0.0054 308 GLN A C   
2325 O O   . GLN A 322 ? 0.3186 0.3278 0.5632 0.0189  0.0524  -0.0035 308 GLN A O   
2326 C CB  . GLN A 322 ? 0.3042 0.3161 0.5333 0.0146  0.0523  -0.0139 308 GLN A CB  
2327 C CG  . GLN A 322 ? 0.2592 0.2707 0.4828 0.0137  0.0512  -0.0192 308 GLN A CG  
2328 C CD  . GLN A 322 ? 0.4512 0.4640 0.6669 0.0146  0.0489  -0.0190 308 GLN A CD  
2329 O OE1 . GLN A 322 ? 0.2960 0.3106 0.5096 0.0155  0.0474  -0.0160 308 GLN A OE1 
2330 N NE2 . GLN A 322 ? 0.3177 0.3277 0.5273 0.0143  0.0486  -0.0224 308 GLN A NE2 
2331 N N   . PRO A 323 ? 0.3437 0.3557 0.5715 0.0184  0.0476  -0.0021 309 PRO A N   
2332 C CA  . PRO A 323 ? 0.3399 0.3498 0.5669 0.0203  0.0447  0.0042  309 PRO A CA  
2333 C C   . PRO A 323 ? 0.4292 0.4347 0.6618 0.0211  0.0481  0.0081  309 PRO A C   
2334 O O   . PRO A 323 ? 0.3721 0.3756 0.6097 0.0235  0.0455  0.0128  309 PRO A O   
2335 C CB  . PRO A 323 ? 0.3867 0.3950 0.5989 0.0204  0.0428  0.0055  309 PRO A CB  
2336 C CG  . PRO A 323 ? 0.3909 0.4024 0.6000 0.0191  0.0422  0.0001  309 PRO A CG  
2337 C CD  . PRO A 323 ? 0.3400 0.3534 0.5576 0.0178  0.0460  -0.0042 309 PRO A CD  
2338 N N   . HIS A 324 ? 0.3509 0.3545 0.5843 0.0192  0.0533  0.0065  310 HIS A N   
2339 C CA  . HIS A 324 ? 0.4449 0.4428 0.6840 0.0193  0.0573  0.0104  310 HIS A CA  
2340 C C   . HIS A 324 ? 0.2985 0.2952 0.5484 0.0169  0.0614  0.0051  310 HIS A C   
2341 O O   . HIS A 324 ? 0.3057 0.2969 0.5617 0.0160  0.0653  0.0073  310 HIS A O   
2342 C CB  . HIS A 324 ? 0.3828 0.3774 0.6138 0.0185  0.0609  0.0145  310 HIS A CB  
2343 C CG  . HIS A 324 ? 0.5150 0.5078 0.7306 0.0208  0.0573  0.0191  310 HIS A CG  
2344 N ND1 . HIS A 324 ? 0.4404 0.4274 0.6501 0.0237  0.0531  0.0260  310 HIS A ND1 
2345 C CD2 . HIS A 324 ? 0.4338 0.4283 0.6376 0.0207  0.0566  0.0173  310 HIS A CD2 
2346 C CE1 . HIS A 324 ? 0.6020 0.5868 0.7950 0.0249  0.0494  0.0279  310 HIS A CE1 
2347 N NE2 . HIS A 324 ? 0.5268 0.5156 0.7158 0.0230  0.0521  0.0225  310 HIS A NE2 
2348 N N   . ALA A 325 ? 0.2677 0.2679 0.5186 0.0157  0.0605  -0.0017 311 ALA A N   
2349 C CA  . ALA A 325 ? 0.2811 0.2781 0.5379 0.0131  0.0632  -0.0077 311 ALA A CA  
2350 C C   . ALA A 325 ? 0.3215 0.3193 0.5755 0.0134  0.0623  -0.0135 311 ALA A C   
2351 O O   . ALA A 325 ? 0.3251 0.3274 0.5728 0.0143  0.0596  -0.0138 311 ALA A O   
2352 C CB  . ALA A 325 ? 0.2972 0.2962 0.5550 0.0096  0.0638  -0.0105 311 ALA A CB  
2353 N N   . SER A 326 ? 0.2988 0.2905 0.5562 0.0124  0.0652  -0.0184 312 SER A N   
2354 C CA  . SER A 326 ? 0.2865 0.2758 0.5383 0.0126  0.0663  -0.0241 312 SER A CA  
2355 C C   . SER A 326 ? 0.3215 0.3042 0.5690 0.0093  0.0665  -0.0316 312 SER A C   
2356 O O   . SER A 326 ? 0.2767 0.2558 0.5303 0.0070  0.0670  -0.0326 312 SER A O   
2357 C CB  . SER A 326 ? 0.2904 0.2769 0.5494 0.0158  0.0710  -0.0228 312 SER A CB  
2358 O OG  . SER A 326 ? 0.2835 0.2771 0.5465 0.0183  0.0685  -0.0168 312 SER A OG  
2359 N N   . ARG A 327 ? 0.3074 0.2874 0.5434 0.0089  0.0657  -0.0368 313 ARG A N   
2360 C CA  . ARG A 327 ? 0.3987 0.3716 0.6262 0.0058  0.0634  -0.0444 313 ARG A CA  
2361 C C   . ARG A 327 ? 0.4031 0.3650 0.6195 0.0068  0.0685  -0.0497 313 ARG A C   
2362 O O   . ARG A 327 ? 0.4088 0.3715 0.6205 0.0092  0.0723  -0.0480 313 ARG A O   
2363 C CB  . ARG A 327 ? 0.3031 0.2815 0.5229 0.0045  0.0558  -0.0456 313 ARG A CB  
2364 C CG  . ARG A 327 ? 0.4048 0.3754 0.6130 0.0019  0.0509  -0.0534 313 ARG A CG  
2365 C CD  . ARG A 327 ? 0.4343 0.4110 0.6368 0.0018  0.0424  -0.0534 313 ARG A CD  
2366 N NE  . ARG A 327 ? 0.4699 0.4479 0.6620 0.0049  0.0437  -0.0502 313 ARG A NE  
2367 C CZ  . ARG A 327 ? 0.4288 0.3973 0.6035 0.0060  0.0456  -0.0526 313 ARG A CZ  
2368 N NH1 . ARG A 327 ? 0.3490 0.3051 0.5117 0.0046  0.0467  -0.0588 313 ARG A NH1 
2369 N NH2 . ARG A 327 ? 0.3437 0.3139 0.5117 0.0083  0.0472  -0.0489 313 ARG A NH2 
2370 N N   . VAL A 328 ? 0.3300 0.2810 0.5426 0.0045  0.0696  -0.0564 314 VAL A N   
2371 C CA  . VAL A 328 ? 0.3614 0.2986 0.5580 0.0049  0.0745  -0.0632 314 VAL A CA  
2372 C C   . VAL A 328 ? 0.3865 0.3164 0.5679 0.0010  0.0662  -0.0707 314 VAL A C   
2373 O O   . VAL A 328 ? 0.3460 0.2736 0.5342 -0.0025 0.0619  -0.0743 314 VAL A O   
2374 C CB  . VAL A 328 ? 0.3894 0.3169 0.5933 0.0065  0.0840  -0.0653 314 VAL A CB  
2375 C CG1 . VAL A 328 ? 0.3456 0.2573 0.5305 0.0072  0.0911  -0.0728 314 VAL A CG1 
2376 C CG2 . VAL A 328 ? 0.3091 0.2456 0.5315 0.0107  0.0897  -0.0570 314 VAL A CG2 
2377 N N   . GLY A 329 ? 0.4165 0.3428 0.5782 0.0015  0.0631  -0.0727 315 GLY A N   
2378 C CA  . GLY A 329 ? 0.5084 0.4280 0.6546 -0.0017 0.0526  -0.0793 315 GLY A CA  
2379 C C   . GLY A 329 ? 0.4990 0.4323 0.6612 -0.0042 0.0418  -0.0770 315 GLY A C   
2380 O O   . GLY A 329 ? 0.4073 0.3539 0.5781 -0.0023 0.0398  -0.0703 315 GLY A O   
2381 N N   . ASP A 330 ? 0.4663 0.3962 0.6335 -0.0086 0.0352  -0.0829 316 ASP A N   
2382 C CA  . ASP A 330 ? 0.5176 0.4606 0.7034 -0.0116 0.0259  -0.0814 316 ASP A CA  
2383 C C   . ASP A 330 ? 0.5221 0.4727 0.7333 -0.0131 0.0318  -0.0770 316 ASP A C   
2384 O O   . ASP A 330 ? 0.5215 0.4833 0.7505 -0.0156 0.0270  -0.0749 316 ASP A O   
2385 C CB  . ASP A 330 ? 0.5601 0.4962 0.7399 -0.0164 0.0137  -0.0903 316 ASP A CB  
2386 C CG  . ASP A 330 ? 0.7228 0.6519 0.8764 -0.0147 0.0049  -0.0935 316 ASP A CG  
2387 O OD1 . ASP A 330 ? 0.6516 0.5901 0.8041 -0.0111 0.0023  -0.0876 316 ASP A OD1 
2388 O OD2 . ASP A 330 ? 0.9925 0.9049 1.1251 -0.0167 0.0008  -0.1018 316 ASP A OD2 
2389 N N   . VAL A 331 ? 0.4732 0.4177 0.6869 -0.0113 0.0425  -0.0750 317 VAL A N   
2390 C CA  . VAL A 331 ? 0.4234 0.3711 0.6578 -0.0124 0.0481  -0.0706 317 VAL A CA  
2391 C C   . VAL A 331 ? 0.4805 0.4382 0.7215 -0.0077 0.0539  -0.0606 317 VAL A C   
2392 O O   . VAL A 331 ? 0.3907 0.3465 0.6229 -0.0035 0.0586  -0.0586 317 VAL A O   
2393 C CB  . VAL A 331 ? 0.4668 0.3990 0.7006 -0.0133 0.0548  -0.0754 317 VAL A CB  
2394 C CG1 . VAL A 331 ? 0.3588 0.2929 0.6130 -0.0137 0.0608  -0.0692 317 VAL A CG1 
2395 C CG2 . VAL A 331 ? 0.4142 0.3344 0.6395 -0.0187 0.0480  -0.0865 317 VAL A CG2 
2396 N N   . TRP A 332 ? 0.3207 0.2880 0.5770 -0.0086 0.0539  -0.0545 318 TRP A N   
2397 C CA  . TRP A 332 ? 0.2942 0.2694 0.5551 -0.0047 0.0582  -0.0452 318 TRP A CA  
2398 C C   . TRP A 332 ? 0.3551 0.3249 0.6262 -0.0038 0.0651  -0.0404 318 TRP A C   
2399 O O   . TRP A 332 ? 0.3405 0.3044 0.6209 -0.0075 0.0666  -0.0423 318 TRP A O   
2400 C CB  . TRP A 332 ? 0.3912 0.3783 0.6590 -0.0056 0.0550  -0.0412 318 TRP A CB  
2401 C CG  . TRP A 332 ? 0.4067 0.4003 0.6642 -0.0034 0.0499  -0.0418 318 TRP A CG  
2402 C CD1 . TRP A 332 ? 0.3502 0.3466 0.6048 -0.0050 0.0423  -0.0469 318 TRP A CD1 
2403 C CD2 . TRP A 332 ? 0.3861 0.3835 0.6355 0.0009  0.0513  -0.0371 318 TRP A CD2 
2404 N NE1 . TRP A 332 ? 0.4969 0.4976 0.7414 -0.0016 0.0398  -0.0450 318 TRP A NE1 
2405 C CE2 . TRP A 332 ? 0.4687 0.4700 0.7100 0.0017  0.0456  -0.0394 318 TRP A CE2 
2406 C CE3 . TRP A 332 ? 0.4050 0.4025 0.6539 0.0041  0.0559  -0.0312 318 TRP A CE3 
2407 C CZ2 . TRP A 332 ? 0.4252 0.4294 0.6578 0.0051  0.0456  -0.0363 318 TRP A CZ2 
2408 C CZ3 . TRP A 332 ? 0.3601 0.3617 0.6012 0.0070  0.0547  -0.0286 318 TRP A CZ3 
2409 C CH2 . TRP A 332 ? 0.3654 0.3698 0.5984 0.0072  0.0503  -0.0313 318 TRP A CH2 
2410 N N   . PHE A 333 ? 0.3882 0.3596 0.6582 0.0009  0.0686  -0.0340 319 PHE A N   
2411 C CA  . PHE A 333 ? 0.3334 0.2999 0.6122 0.0032  0.0738  -0.0278 319 PHE A CA  
2412 C C   . PHE A 333 ? 0.3011 0.2755 0.5803 0.0058  0.0731  -0.0185 319 PHE A C   
2413 O O   . PHE A 333 ? 0.3208 0.3002 0.5948 0.0094  0.0714  -0.0155 319 PHE A O   
2414 C CB  . PHE A 333 ? 0.2749 0.2349 0.5528 0.0073  0.0778  -0.0291 319 PHE A CB  
2415 C CG  . PHE A 333 ? 0.3431 0.2924 0.6163 0.0051  0.0799  -0.0389 319 PHE A CG  
2416 C CD1 . PHE A 333 ? 0.3769 0.3144 0.6571 0.0034  0.0838  -0.0418 319 PHE A CD1 
2417 C CD2 . PHE A 333 ? 0.3120 0.2610 0.5718 0.0047  0.0781  -0.0454 319 PHE A CD2 
2418 C CE1 . PHE A 333 ? 0.3399 0.2653 0.6130 0.0012  0.0856  -0.0518 319 PHE A CE1 
2419 C CE2 . PHE A 333 ? 0.3053 0.2419 0.5561 0.0028  0.0800  -0.0547 319 PHE A CE2 
2420 C CZ  . PHE A 333 ? 0.3180 0.2427 0.5751 0.0010  0.0835  -0.0584 319 PHE A CZ  
2421 N N   . THR A 334 ? 0.2639 0.2384 0.5486 0.0035  0.0747  -0.0141 320 THR A N   
2422 C CA  . THR A 334 ? 0.4191 0.3989 0.6999 0.0054  0.0747  -0.0061 320 THR A CA  
2423 C C   . THR A 334 ? 0.3284 0.3015 0.6104 0.0089  0.0775  0.0027  320 THR A C   
2424 O O   . THR A 334 ? 0.3807 0.3448 0.6703 0.0088  0.0809  0.0035  320 THR A O   
2425 C CB  . THR A 334 ? 0.3790 0.3630 0.6641 0.0013  0.0763  -0.0061 320 THR A CB  
2426 O OG1 . THR A 334 ? 0.4056 0.3820 0.7007 -0.0016 0.0818  -0.0031 320 THR A OG1 
2427 C CG2 . THR A 334 ? 0.2879 0.2773 0.5755 -0.0022 0.0720  -0.0151 320 THR A CG2 
2428 N N   . GLY A 335 ? 0.3395 0.3158 0.6128 0.0121  0.0755  0.0095  321 GLY A N   
2429 C CA  . GLY A 335 ? 0.3394 0.3091 0.6106 0.0161  0.0756  0.0186  321 GLY A CA  
2430 C C   . GLY A 335 ? 0.4270 0.3971 0.7019 0.0208  0.0716  0.0193  321 GLY A C   
2431 O O   . GLY A 335 ? 0.3856 0.3489 0.6645 0.0245  0.0716  0.0259  321 GLY A O   
2432 N N   . ILE A 336 ? 0.3784 0.3559 0.6530 0.0211  0.0685  0.0132  322 ILE A N   
2433 C CA  . ILE A 336 ? 0.4412 0.4207 0.7226 0.0251  0.0661  0.0134  322 ILE A CA  
2434 C C   . ILE A 336 ? 0.4685 0.4563 0.7429 0.0266  0.0594  0.0153  322 ILE A C   
2435 O O   . ILE A 336 ? 0.3006 0.2940 0.5681 0.0241  0.0585  0.0103  322 ILE A O   
2436 C CB  . ILE A 336 ? 0.2942 0.2732 0.5820 0.0240  0.0701  0.0046  322 ILE A CB  
2437 C CG1 . ILE A 336 ? 0.3693 0.3376 0.6651 0.0233  0.0760  0.0027  322 ILE A CG1 
2438 C CG2 . ILE A 336 ? 0.3223 0.3061 0.6173 0.0278  0.0688  0.0045  322 ILE A CG2 
2439 C CD1 . ILE A 336 ? 0.4890 0.4537 0.7841 0.0205  0.0799  -0.0076 322 ILE A CD1 
2440 N N   . PRO A 337 ? 0.3740 0.3623 0.6500 0.0306  0.0539  0.0223  323 PRO A N   
2441 C CA  . PRO A 337 ? 0.2807 0.2764 0.5513 0.0313  0.0464  0.0230  323 PRO A CA  
2442 C C   . PRO A 337 ? 0.3160 0.3188 0.5953 0.0304  0.0475  0.0163  323 PRO A C   
2443 O O   . PRO A 337 ? 0.2990 0.3014 0.5919 0.0318  0.0520  0.0139  323 PRO A O   
2444 C CB  . PRO A 337 ? 0.3543 0.3483 0.6291 0.0360  0.0392  0.0315  323 PRO A CB  
2445 C CG  . PRO A 337 ? 0.3520 0.3358 0.6269 0.0376  0.0434  0.0369  323 PRO A CG  
2446 C CD  . PRO A 337 ? 0.3631 0.3444 0.6458 0.0347  0.0531  0.0301  323 PRO A CD  
2447 N N   . MET A 338 ? 0.2994 0.3075 0.5700 0.0282  0.0442  0.0134  324 MET A N   
2448 C CA  . MET A 338 ? 0.3532 0.3663 0.6289 0.0267  0.0463  0.0076  324 MET A CA  
2449 C C   . MET A 338 ? 0.3422 0.3601 0.6363 0.0294  0.0449  0.0093  324 MET A C   
2450 O O   . MET A 338 ? 0.2734 0.2924 0.5769 0.0292  0.0514  0.0050  324 MET A O   
2451 C CB  . MET A 338 ? 0.3020 0.3182 0.5647 0.0241  0.0424  0.0054  324 MET A CB  
2452 C CG  . MET A 338 ? 0.2941 0.3159 0.5623 0.0232  0.0400  0.0034  324 MET A CG  
2453 S SD  . MET A 338 ? 0.4143 0.4361 0.6645 0.0204  0.0358  0.0010  324 MET A SD  
2454 C CE  . MET A 338 ? 0.3285 0.3484 0.5740 0.0183  0.0435  -0.0054 324 MET A CE  
2455 N N   . LEU A 339 ? 0.2772 0.2973 0.5769 0.0322  0.0368  0.0158  325 LEU A N   
2456 C CA  . LEU A 339 ? 0.3287 0.3550 0.6509 0.0353  0.0345  0.0180  325 LEU A CA  
2457 C C   . LEU A 339 ? 0.4257 0.4484 0.7629 0.0385  0.0435  0.0175  325 LEU A C   
2458 O O   . LEU A 339 ? 0.3711 0.3980 0.7260 0.0397  0.0490  0.0149  325 LEU A O   
2459 C CB  . LEU A 339 ? 0.3399 0.3683 0.6643 0.0382  0.0218  0.0256  325 LEU A CB  
2460 C CG  . LEU A 339 ? 0.4904 0.5251 0.8420 0.0430  0.0178  0.0299  325 LEU A CG  
2461 C CD1 . LEU A 339 ? 0.3708 0.4165 0.7412 0.0410  0.0187  0.0258  325 LEU A CD1 
2462 C CD2 . LEU A 339 ? 0.3330 0.3668 0.6825 0.0465  0.0035  0.0383  325 LEU A CD2 
2463 N N   . GLN A 340 ? 0.3253 0.3391 0.6559 0.0398  0.0459  0.0198  326 GLN A N   
2464 C CA  . GLN A 340 ? 0.2806 0.2882 0.6239 0.0426  0.0546  0.0187  326 GLN A CA  
2465 C C   . GLN A 340 ? 0.3562 0.3609 0.6962 0.0395  0.0653  0.0094  326 GLN A C   
2466 O O   . GLN A 340 ? 0.2573 0.2600 0.6110 0.0418  0.0733  0.0064  326 GLN A O   
2467 C CB  . GLN A 340 ? 0.2953 0.2926 0.6313 0.0437  0.0548  0.0232  326 GLN A CB  
2468 C CG  . GLN A 340 ? 0.3209 0.3171 0.6648 0.0491  0.0469  0.0332  326 GLN A CG  
2469 C CD  . GLN A 340 ? 0.4086 0.3920 0.7478 0.0505  0.0501  0.0380  326 GLN A CD  
2470 O OE1 . GLN A 340 ? 0.3487 0.3262 0.6705 0.0467  0.0515  0.0382  326 GLN A OE1 
2471 N NE2 . GLN A 340 ? 0.3842 0.3627 0.7406 0.0561  0.0519  0.0420  326 GLN A NE2 
2472 N N   . ALA A 341 ? 0.3026 0.3060 0.6240 0.0346  0.0656  0.0048  327 ALA A N   
2473 C CA  . ALA A 341 ? 0.2657 0.2651 0.5802 0.0317  0.0736  -0.0036 327 ALA A CA  
2474 C C   . ALA A 341 ? 0.3783 0.3833 0.7014 0.0322  0.0774  -0.0061 327 ALA A C   
2475 O O   . ALA A 341 ? 0.3569 0.3566 0.6822 0.0326  0.0870  -0.0113 327 ALA A O   
2476 C CB  . ALA A 341 ? 0.2426 0.2413 0.5378 0.0271  0.0708  -0.0069 327 ALA A CB  
2477 N N   . ILE A 342 ? 0.3109 0.3253 0.6377 0.0318  0.0707  -0.0027 328 ILE A N   
2478 C CA  . ILE A 342 ? 0.2820 0.3022 0.6198 0.0316  0.0747  -0.0044 328 ILE A CA  
2479 C C   . ILE A 342 ? 0.3270 0.3495 0.6902 0.0362  0.0805  -0.0027 328 ILE A C   
2480 O O   . ILE A 342 ? 0.3696 0.3903 0.7399 0.0366  0.0917  -0.0068 328 ILE A O   
2481 C CB  . ILE A 342 ? 0.2633 0.2926 0.6014 0.0296  0.0649  -0.0013 328 ILE A CB  
2482 C CG1 . ILE A 342 ? 0.2809 0.3070 0.5953 0.0253  0.0627  -0.0045 328 ILE A CG1 
2483 C CG2 . ILE A 342 ? 0.2421 0.2793 0.6001 0.0294  0.0682  -0.0015 328 ILE A CG2 
2484 C CD1 . ILE A 342 ? 0.3143 0.3460 0.6244 0.0235  0.0524  -0.0018 328 ILE A CD1 
2485 N N   . GLU A 343 ? 0.2748 0.3002 0.6515 0.0402  0.0736  0.0037  329 GLU A N   
2486 C CA  . GLU A 343 ? 0.3353 0.3632 0.7391 0.0457  0.0785  0.0060  329 GLU A CA  
2487 C C   . GLU A 343 ? 0.2956 0.3117 0.6978 0.0473  0.0926  0.0004  329 GLU A C   
2488 O O   . GLU A 343 ? 0.2772 0.2939 0.6976 0.0504  0.1031  -0.0018 329 GLU A O   
2489 C CB  . GLU A 343 ? 0.3765 0.4068 0.7910 0.0503  0.0673  0.0145  329 GLU A CB  
2490 C CG  . GLU A 343 ? 0.4403 0.4822 0.8615 0.0499  0.0530  0.0199  329 GLU A CG  
2491 C CD  . GLU A 343 ? 0.6299 0.6711 1.0553 0.0546  0.0408  0.0287  329 GLU A CD  
2492 O OE1 . GLU A 343 ? 0.5648 0.5951 0.9801 0.0567  0.0433  0.0308  329 GLU A OE1 
2493 O OE2 . GLU A 343 ? 0.7484 0.7991 1.1868 0.0561  0.0285  0.0336  329 GLU A OE2 
2494 N N   . THR A 344 ? 0.2794 0.2844 0.6606 0.0452  0.0934  -0.0025 330 THR A N   
2495 C CA  . THR A 344 ? 0.3373 0.3289 0.7127 0.0455  0.1054  -0.0094 330 THR A CA  
2496 C C   . THR A 344 ? 0.2722 0.2609 0.6381 0.0428  0.1156  -0.0169 330 THR A C   
2497 O O   . THR A 344 ? 0.3614 0.3434 0.7344 0.0454  0.1282  -0.0212 330 THR A O   
2498 C CB  . THR A 344 ? 0.3874 0.3691 0.7426 0.0422  0.1021  -0.0113 330 THR A CB  
2499 O OG1 . THR A 344 ? 0.3832 0.3648 0.7468 0.0451  0.0954  -0.0037 330 THR A OG1 
2500 C CG2 . THR A 344 ? 0.3240 0.2907 0.6701 0.0412  0.1127  -0.0199 330 THR A CG2 
2501 N N   . LEU A 345 ? 0.2923 0.2845 0.6411 0.0379  0.1110  -0.0184 331 LEU A N   
2502 C CA  . LEU A 345 ? 0.3539 0.3412 0.6899 0.0353  0.1201  -0.0245 331 LEU A CA  
2503 C C   . LEU A 345 ? 0.3140 0.3080 0.6714 0.0377  0.1289  -0.0232 331 LEU A C   
2504 O O   . LEU A 345 ? 0.3665 0.3522 0.7196 0.0380  0.1427  -0.0283 331 LEU A O   
2505 C CB  . LEU A 345 ? 0.2708 0.2606 0.5862 0.0304  0.1122  -0.0250 331 LEU A CB  
2506 C CG  . LEU A 345 ? 0.4396 0.4222 0.7335 0.0275  0.1062  -0.0279 331 LEU A CG  
2507 C CD1 . LEU A 345 ? 0.3772 0.3638 0.6551 0.0238  0.0986  -0.0276 331 LEU A CD1 
2508 C CD2 . LEU A 345 ? 0.3965 0.3639 0.6763 0.0270  0.1148  -0.0358 331 LEU A CD2 
2509 N N   . VAL A 346 ? 0.3105 0.3190 0.6917 0.0395  0.1215  -0.0164 332 VAL A N   
2510 C CA  . VAL A 346 ? 0.3530 0.3706 0.7604 0.0412  0.1289  -0.0149 332 VAL A CA  
2511 C C   . VAL A 346 ? 0.3235 0.3357 0.7488 0.0467  0.1428  -0.0169 332 VAL A C   
2512 O O   . VAL A 346 ? 0.2961 0.3053 0.7275 0.0472  0.1582  -0.0204 332 VAL A O   
2513 C CB  . VAL A 346 ? 0.2807 0.3151 0.7115 0.0419  0.1151  -0.0074 332 VAL A CB  
2514 C CG1 . VAL A 346 ? 0.2520 0.2974 0.7181 0.0443  0.1225  -0.0056 332 VAL A CG1 
2515 C CG2 . VAL A 346 ? 0.3372 0.3754 0.7503 0.0362  0.1043  -0.0067 332 VAL A CG2 
2516 N N   . GLU A 347 ? 0.3248 0.3341 0.7579 0.0511  0.1388  -0.0145 333 GLU A N   
2517 C CA  . GLU A 347 ? 0.2968 0.2981 0.7451 0.0570  0.1522  -0.0170 333 GLU A CA  
2518 C C   . GLU A 347 ? 0.3117 0.2947 0.7342 0.0550  0.1675  -0.0266 333 GLU A C   
2519 O O   . GLU A 347 ? 0.4039 0.3815 0.8356 0.0578  0.1841  -0.0304 333 GLU A O   
2520 C CB  . GLU A 347 ? 0.2893 0.2871 0.7441 0.0612  0.1443  -0.0128 333 GLU A CB  
2521 C CG  . GLU A 347 ? 0.3647 0.3530 0.8331 0.0667  0.1560  -0.0145 333 GLU A CG  
2522 C CD  . GLU A 347 ? 0.7258 0.7164 1.2110 0.0716  0.1457  -0.0064 333 GLU A CD  
2523 O OE1 . GLU A 347 ? 0.6175 0.5985 1.0908 0.0722  0.1411  -0.0062 333 GLU A OE1 
2524 O OE2 . GLU A 347 ? 0.7723 0.7732 1.2825 0.0748  0.1426  -0.0001 333 GLU A OE2 
2525 N N   . LEU A 348 ? 0.3140 0.2865 0.7036 0.0502  0.1619  -0.0307 334 LEU A N   
2526 C CA  . LEU A 348 ? 0.3261 0.2796 0.6880 0.0481  0.1733  -0.0402 334 LEU A CA  
2527 C C   . LEU A 348 ? 0.4521 0.4040 0.8045 0.0459  0.1844  -0.0432 334 LEU A C   
2528 O O   . LEU A 348 ? 0.3544 0.2920 0.6970 0.0472  0.2006  -0.0496 334 LEU A O   
2529 C CB  . LEU A 348 ? 0.3343 0.2798 0.6666 0.0430  0.1623  -0.0433 334 LEU A CB  
2530 C CG  . LEU A 348 ? 0.4952 0.4365 0.8315 0.0442  0.1550  -0.0420 334 LEU A CG  
2531 C CD1 . LEU A 348 ? 0.3236 0.2593 0.6336 0.0382  0.1449  -0.0452 334 LEU A CD1 
2532 C CD2 . LEU A 348 ? 0.4328 0.3590 0.7750 0.0484  0.1678  -0.0472 334 LEU A CD2 
2533 N N   . CYS A 349 ? 0.3358 0.3008 0.6903 0.0425  0.1767  -0.0384 335 CYS A N   
2534 C CA  . CYS A 349 ? 0.3273 0.2906 0.6740 0.0400  0.1873  -0.0400 335 CYS A CA  
2535 C C   . CYS A 349 ? 0.3765 0.3440 0.7530 0.0442  0.2041  -0.0392 335 CYS A C   
2536 O O   . CYS A 349 ? 0.4097 0.3654 0.7746 0.0440  0.2214  -0.0437 335 CYS A O   
2537 C CB  . CYS A 349 ? 0.3107 0.2870 0.6566 0.0355  0.1748  -0.0349 335 CYS A CB  
2538 S SG  . CYS A 349 ? 0.4334 0.4005 0.7376 0.0302  0.1626  -0.0378 335 CYS A SG  
2539 N N   . LYS A 350 ? 0.3756 0.3589 0.7905 0.0483  0.1997  -0.0333 336 LYS A N   
2540 C CA  . LYS A 350 ? 0.4364 0.4235 0.8765 0.0502  0.2112  -0.0311 336 LYS A CA  
2541 C C   . LYS A 350 ? 0.4136 0.3812 0.8394 0.0526  0.2274  -0.0372 336 LYS A C   
2542 O O   . LYS A 350 ? 0.3744 0.3383 0.8069 0.0525  0.2421  -0.0376 336 LYS A O   
2543 C CB  . LYS A 350 ? 0.3590 0.3631 0.8341 0.0530  0.1979  -0.0230 336 LYS A CB  
2544 C CG  . LYS A 350 ? 0.4067 0.4299 0.8981 0.0505  0.1822  -0.0169 336 LYS A CG  
2545 C CD  . LYS A 350 ? 0.4857 0.5234 1.0095 0.0536  0.1690  -0.0093 336 LYS A CD  
2546 C CE  . LYS A 350 ? 0.3188 0.3744 0.8591 0.0504  0.1543  -0.0043 336 LYS A CE  
2547 N NZ  . LYS A 350 ? 0.5881 0.6534 1.1397 0.0536  0.1342  0.0019  336 LYS A NZ  
2548 N N   . GLN A 351 ? 0.4174 0.3714 0.8232 0.0543  0.2252  -0.0424 337 GLN A N   
2549 C CA  . GLN A 351 ? 0.4580 0.3916 0.8476 0.0562  0.2392  -0.0493 337 GLN A CA  
2550 C C   . GLN A 351 ? 0.4707 0.3836 0.8206 0.0535  0.2514  -0.0584 337 GLN A C   
2551 O O   . GLN A 351 ? 0.4533 0.3514 0.7909 0.0539  0.2678  -0.0629 337 GLN A O   
2552 C CB  . GLN A 351 ? 0.3884 0.3152 0.7761 0.0588  0.2306  -0.0509 337 GLN A CB  
2553 C CG  . GLN A 351 ? 0.5502 0.4583 0.9294 0.0612  0.2438  -0.0568 337 GLN A CG  
2554 C CD  . GLN A 351 ? 0.4520 0.3497 0.8250 0.0626  0.2364  -0.0596 337 GLN A CD  
2555 O OE1 . GLN A 351 ? 0.4992 0.4068 0.8835 0.0631  0.2213  -0.0544 337 GLN A OE1 
2556 N NE2 . GLN A 351 ? 0.4454 0.3218 0.7995 0.0631  0.2474  -0.0680 337 GLN A NE2 
2557 N N   . HIS A 352 ? 0.4790 0.3898 0.8063 0.0504  0.2429  -0.0609 338 HIS A N   
2558 C CA  . HIS A 352 ? 0.6314 0.5195 0.9125 0.0467  0.2471  -0.0691 338 HIS A CA  
2559 C C   . HIS A 352 ? 0.5757 0.4620 0.8341 0.0421  0.2490  -0.0680 338 HIS A C   
2560 O O   . HIS A 352 ? 0.6782 0.5432 0.8980 0.0402  0.2558  -0.0746 338 HIS A O   
2561 C CB  . HIS A 352 ? 0.5207 0.4026 0.7797 0.0435  0.2291  -0.0722 338 HIS A CB  
2562 C CG  . HIS A 352 ? 0.4986 0.3732 0.7681 0.0470  0.2297  -0.0756 338 HIS A CG  
2563 N ND1 . HIS A 352 ? 0.4971 0.3483 0.7492 0.0490  0.2436  -0.0851 338 HIS A ND1 
2564 C CD2 . HIS A 352 ? 0.4823 0.3676 0.7755 0.0488  0.2182  -0.0708 338 HIS A CD2 
2565 C CE1 . HIS A 352 ? 0.4851 0.3335 0.7522 0.0518  0.2408  -0.0862 338 HIS A CE1 
2566 N NE2 . HIS A 352 ? 0.5552 0.4240 0.8472 0.0518  0.2256  -0.0770 338 HIS A NE2 
2567 N N   . VAL A 353 ? 1.0985 0.4918 1.1461 0.1406  -0.0393 -0.3373 339 VAL A N   
2568 C CA  . VAL A 353 ? 1.1058 0.4958 1.0943 0.1395  -0.0202 -0.3434 339 VAL A CA  
2569 C C   . VAL A 353 ? 1.1466 0.5302 1.1018 0.1595  0.0278  -0.3640 339 VAL A C   
2570 O O   . VAL A 353 ? 1.2090 0.6289 1.2158 0.1690  0.0510  -0.3569 339 VAL A O   
2571 C CB  . VAL A 353 ? 1.0221 0.4562 1.0468 0.1253  -0.0248 -0.3161 339 VAL A CB  
2572 C CG1 . VAL A 353 ? 0.9873 0.4282 1.0474 0.1060  -0.0676 -0.2937 339 VAL A CG1 
2573 C CG2 . VAL A 353 ? 0.9990 0.4801 1.0888 0.1303  -0.0018 -0.3020 339 VAL A CG2 
2574 N N   . HIS A 354 ? 1.3584 0.6983 1.2309 0.1647  0.0414  -0.3888 340 HIS A N   
2575 C CA  . HIS A 354 ? 1.5834 0.9044 1.4079 0.1826  0.0908  -0.4120 340 HIS A CA  
2576 C C   . HIS A 354 ? 1.5820 0.9415 1.3882 0.1795  0.1098  -0.4174 340 HIS A C   
2577 O O   . HIS A 354 ? 1.6624 0.9986 1.3879 0.1844  0.1182  -0.4329 340 HIS A O   
2578 C CB  . HIS A 354 ? 1.6278 0.9035 1.4154 0.1859  0.0829  -0.4424 340 HIS A CB  
2579 C CG  . HIS A 354 ? 1.8416 1.0930 1.5484 0.1817  0.0713  -0.4617 340 HIS A CG  
2580 N ND1 . HIS A 354 ? 1.8806 1.1449 1.5323 0.1848  0.0931  -0.4640 340 HIS A ND1 
2581 C CD2 . HIS A 354 ? 1.8848 1.0935 1.5441 0.1764  0.0314  -0.4703 340 HIS A CD2 
2582 C CE1 . HIS A 354 ? 1.8662 1.0881 1.4303 0.1811  0.0720  -0.4719 340 HIS A CE1 
2583 N NE2 . HIS A 354 ? 1.8914 1.0812 1.4629 0.1763  0.0328  -0.4779 340 HIS A NE2 
2584 N N   . ASP A 355 ? 1.3644 0.7551 1.1937 0.1802  0.1109  -0.3872 341 ASP A N   
2585 C CA  . ASP A 355 ? 1.4545 0.8664 1.2529 0.1667  0.1304  -0.3741 341 ASP A CA  
2586 C C   . ASP A 355 ? 1.5103 0.9785 1.3541 0.1693  0.1765  -0.3581 341 ASP A C   
2587 O O   . ASP A 355 ? 1.4376 0.9442 1.3649 0.1730  0.1811  -0.3484 341 ASP A O   
2588 C CB  . ASP A 355 ? 1.4859 0.9047 1.3023 0.1453  0.0934  -0.3500 341 ASP A CB  
2589 C CG  . ASP A 355 ? 1.4790 0.8588 1.2064 0.1361  0.0709  -0.3505 341 ASP A CG  
2590 O OD1 . ASP A 355 ? 1.3340 0.7302 1.0270 0.1288  0.0907  -0.3359 341 ASP A OD1 
2591 O OD2 . ASP A 355 ? 1.3734 0.7187 1.0780 0.1321  0.0322  -0.3605 341 ASP A OD2 
2592 N N   . THR A 356 ? 1.5833 1.0565 1.3728 0.1657  0.2077  -0.3530 342 THR A N   
2593 C CA  . THR A 356 ? 1.4291 0.9561 1.2613 0.1613  0.2460  -0.3326 342 THR A CA  
2594 C C   . THR A 356 ? 1.4717 0.9898 1.2362 0.1480  0.2564  -0.3193 342 THR A C   
2595 O O   . THR A 356 ? 1.5359 1.0135 1.2093 0.1503  0.2607  -0.3296 342 THR A O   
2596 C CB  . THR A 356 ? 1.4869 1.0363 1.3432 0.1770  0.2862  -0.3417 342 THR A CB  
2597 O OG1 . THR A 356 ? 1.3546 0.9644 1.2915 0.1717  0.3094  -0.3203 342 THR A OG1 
2598 C CG2 . THR A 356 ? 1.4552 0.9761 1.2219 0.1827  0.3169  -0.3541 342 THR A CG2 
2599 N N   . PRO A 357 ? 1.4163 0.9675 1.2190 0.1335  0.2554  -0.2961 343 PRO A N   
2600 C CA  . PRO A 357 ? 1.4485 0.9906 1.1867 0.1195  0.2502  -0.2799 343 PRO A CA  
2601 C C   . PRO A 357 ? 1.5751 1.1236 1.2767 0.1207  0.3003  -0.2751 343 PRO A C   
2602 O O   . PRO A 357 ? 1.6513 1.1628 1.2623 0.1165  0.3010  -0.2737 343 PRO A O   
2603 C CB  . PRO A 357 ? 1.2020 0.7951 1.0106 0.1026  0.2201  -0.2508 343 PRO A CB  
2604 C CG  . PRO A 357 ? 0.9470 0.5818 0.8552 0.1082  0.2227  -0.2488 343 PRO A CG  
2605 C CD  . PRO A 357 ? 1.2522 0.8641 1.1619 0.1279  0.2485  -0.2765 343 PRO A CD  
2606 N N   . VAL A 358 ? 1.5668 1.1666 1.3424 0.1245  0.3340  -0.2678 344 VAL A N   
2607 C CA  . VAL A 358 ? 1.5963 1.2158 1.3620 0.1233  0.3788  -0.2577 344 VAL A CA  
2608 C C   . VAL A 358 ? 1.7281 1.3312 1.4277 0.1091  0.3811  -0.2406 344 VAL A C   
2609 O O   . VAL A 358 ? 1.8146 1.3707 1.4165 0.1097  0.3848  -0.2452 344 VAL A O   
2610 C CB  . VAL A 358 ? 1.5256 1.1223 1.2524 0.1381  0.4054  -0.2766 344 VAL A CB  
2611 C CG1 . VAL A 358 ? 1.6349 1.1652 1.2589 0.1446  0.3830  -0.2973 344 VAL A CG1 
2612 C CG2 . VAL A 358 ? 1.5128 1.1282 1.2340 0.1348  0.4532  -0.2637 344 VAL A CG2 
2613 N N   . PRO A 359 ? 1.6707 1.3099 1.4195 0.0964  0.3766  -0.2202 345 PRO A N   
2614 C CA  . PRO A 359 ? 1.5914 1.2262 1.3032 0.0807  0.3622  -0.2004 345 PRO A CA  
2615 C C   . PRO A 359 ? 1.5456 1.1251 1.1401 0.0785  0.3739  -0.2003 345 PRO A C   
2616 O O   . PRO A 359 ? 1.3558 0.9318 0.9227 0.0650  0.3494  -0.1818 345 PRO A O   
2617 C CB  . PRO A 359 ? 1.4366 1.1306 1.2309 0.0728  0.3869  -0.1802 345 PRO A CB  
2618 C CG  . PRO A 359 ? 1.4928 1.2129 1.3405 0.0823  0.4188  -0.1860 345 PRO A CG  
2619 C CD  . PRO A 359 ? 1.5947 1.2910 1.4346 0.0972  0.4065  -0.2102 345 PRO A CD  
2620 N N   . PRO A 370 ? 1.1913 1.0959 1.3350 -0.1284 0.2327  0.1202  356 PRO A N   
2621 C CA  . PRO A 370 ? 1.1095 1.0199 1.2888 -0.1332 0.2023  0.1241  356 PRO A CA  
2622 C C   . PRO A 370 ? 1.1630 1.0303 1.2853 -0.1394 0.1893  0.1401  356 PRO A C   
2623 O O   . PRO A 370 ? 1.2296 1.0605 1.2872 -0.1429 0.2096  0.1527  356 PRO A O   
2624 C CB  . PRO A 370 ? 1.0336 0.9722 1.2744 -0.1352 0.2091  0.1238  356 PRO A CB  
2625 C CG  . PRO A 370 ? 0.9864 0.9321 1.2232 -0.1317 0.2443  0.1221  356 PRO A CG  
2626 C CD  . PRO A 370 ? 0.9575 0.8947 1.1516 -0.1243 0.2525  0.1133  356 PRO A CD  
2627 N N   . ASP A 371 ? 1.1282 0.9969 1.2728 -0.1398 0.1552  0.1393  357 ASP A N   
2628 C CA  . ASP A 371 ? 1.1113 0.9409 1.2083 -0.1427 0.1325  0.1512  357 ASP A CA  
2629 C C   . ASP A 371 ? 1.0657 0.9018 1.2163 -0.1480 0.1122  0.1555  357 ASP A C   
2630 O O   . ASP A 371 ? 1.0822 0.9445 1.2963 -0.1525 0.1221  0.1540  357 ASP A O   
2631 C CB  . ASP A 371 ? 1.1873 1.0092 1.2470 -0.1319 0.1027  0.1386  357 ASP A CB  
2632 C CG  . ASP A 371 ? 1.2330 1.0332 1.2254 -0.1278 0.1170  0.1368  357 ASP A CG  
2633 O OD1 . ASP A 371 ? 1.2884 1.1109 1.2927 -0.1237 0.1398  0.1266  357 ASP A OD1 
2634 O OD2 . ASP A 371 ? 1.2251 0.9832 1.1524 -0.1278 0.1023  0.1447  357 ASP A OD2 
2635 N N   . GLY A 372 ? 0.9456 0.7556 1.0732 -0.1472 0.0819  0.1604  358 GLY A N   
2636 C CA  . GLY A 372 ? 0.7951 0.6099 0.9725 -0.1491 0.0571  0.1599  358 GLY A CA  
2637 C C   . GLY A 372 ? 0.8988 0.7332 1.0971 -0.1364 0.0251  0.1388  358 GLY A C   
2638 O O   . GLY A 372 ? 0.7229 0.5933 0.9575 -0.1294 0.0262  0.1207  358 GLY A O   
2639 N N   . SER A 373 ? 0.7024 0.5118 0.8779 -0.1329 -0.0028 0.1415  359 SER A N   
2640 C CA  . SER A 373 ? 0.5478 0.3752 0.7475 -0.1208 -0.0295 0.1224  359 SER A CA  
2641 C C   . SER A 373 ? 0.6464 0.4949 0.8304 -0.1124 -0.0232 0.1083  359 SER A C   
2642 O O   . SER A 373 ? 0.5697 0.4017 0.7044 -0.1137 -0.0132 0.1145  359 SER A O   
2643 C CB  . SER A 373 ? 0.7029 0.4975 0.8843 -0.1189 -0.0598 0.1296  359 SER A CB  
2644 O OG  . SER A 373 ? 0.9144 0.7266 1.1437 -0.1094 -0.0825 0.1133  359 SER A OG  
2645 N N   . LEU A 374 ? 0.4578 0.3395 0.6810 -0.1034 -0.0293 0.0893  360 LEU A N   
2646 C CA  . LEU A 374 ? 0.5056 0.4090 0.7209 -0.0962 -0.0221 0.0769  360 LEU A CA  
2647 C C   . LEU A 374 ? 0.5616 0.4482 0.7457 -0.0918 -0.0384 0.0770  360 LEU A C   
2648 O O   . LEU A 374 ? 0.5422 0.4179 0.7369 -0.0885 -0.0619 0.0765  360 LEU A O   
2649 C CB  . LEU A 374 ? 0.3726 0.3094 0.6313 -0.0877 -0.0258 0.0587  360 LEU A CB  
2650 C CG  . LEU A 374 ? 0.4770 0.4370 0.7586 -0.0889 -0.0089 0.0534  360 LEU A CG  
2651 C CD1 . LEU A 374 ? 0.3509 0.3319 0.6676 -0.0807 -0.0193 0.0367  360 LEU A CD1 
2652 C CD2 . LEU A 374 ? 0.4755 0.4458 0.7360 -0.0877 0.0088  0.0522  360 LEU A CD2 
2653 N N   . THR A 375 ? 0.4887 0.3724 0.6385 -0.0915 -0.0274 0.0769  361 THR A N   
2654 C CA  . THR A 375 ? 0.5122 0.3833 0.6378 -0.0870 -0.0438 0.0739  361 THR A CA  
2655 C C   . THR A 375 ? 0.4638 0.3607 0.5959 -0.0819 -0.0315 0.0619  361 THR A C   
2656 O O   . THR A 375 ? 0.5385 0.4572 0.6844 -0.0821 -0.0105 0.0579  361 THR A O   
2657 C CB  . THR A 375 ? 0.5612 0.3880 0.6233 -0.0923 -0.0477 0.0875  361 THR A CB  
2658 O OG1 . THR A 375 ? 0.6549 0.4789 0.6859 -0.0964 -0.0173 0.0912  361 THR A OG1 
2659 C CG2 . THR A 375 ? 0.5014 0.2974 0.5528 -0.0979 -0.0617 0.1024  361 THR A CG2 
2660 N N   . GLN A 376 ? 0.4463 0.3395 0.5728 -0.0775 -0.0469 0.0565  362 GLN A N   
2661 C CA  . GLN A 376 ? 0.4812 0.3913 0.6073 -0.0739 -0.0362 0.0477  362 GLN A CA  
2662 C C   . GLN A 376 ? 0.4496 0.3472 0.5350 -0.0773 -0.0146 0.0513  362 GLN A C   
2663 O O   . GLN A 376 ? 0.4035 0.3229 0.5015 -0.0752 0.0041  0.0453  362 GLN A O   
2664 C CB  . GLN A 376 ? 0.4348 0.3361 0.5602 -0.0707 -0.0580 0.0437  362 GLN A CB  
2665 C CG  . GLN A 376 ? 0.4165 0.3385 0.5946 -0.0659 -0.0725 0.0377  362 GLN A CG  
2666 C CD  . GLN A 376 ? 0.4657 0.4241 0.6791 -0.0613 -0.0560 0.0284  362 GLN A CD  
2667 O OE1 . GLN A 376 ? 0.3458 0.3117 0.5466 -0.0613 -0.0416 0.0261  362 GLN A OE1 
2668 N NE2 . GLN A 376 ? 0.3434 0.3217 0.5987 -0.0566 -0.0578 0.0231  362 GLN A NE2 
2669 N N   . ASP A 377 ? 0.4726 0.3329 0.5081 -0.0819 -0.0161 0.0613  363 ASP A N   
2670 C CA  . ASP A 377 ? 0.6410 0.4847 0.6318 -0.0841 0.0080  0.0640  363 ASP A CA  
2671 C C   . ASP A 377 ? 0.6161 0.4844 0.6346 -0.0868 0.0382  0.0657  363 ASP A C   
2672 O O   . ASP A 377 ? 0.6301 0.5141 0.6549 -0.0840 0.0583  0.0589  363 ASP A O   
2673 C CB  . ASP A 377 ? 0.6911 0.4847 0.6159 -0.0885 0.0013  0.0761  363 ASP A CB  
2674 C CG  . ASP A 377 ? 0.9112 0.6789 0.7759 -0.0880 0.0226  0.0751  363 ASP A CG  
2675 O OD1 . ASP A 377 ? 0.9690 0.7386 0.8258 -0.0914 0.0559  0.0807  363 ASP A OD1 
2676 O OD2 . ASP A 377 ? 1.1290 0.8739 0.9572 -0.0837 0.0062  0.0680  363 ASP A OD2 
2677 N N   . ASN A 378 ? 0.4888 0.3602 0.5298 -0.0921 0.0398  0.0744  364 ASN A N   
2678 C CA  . ASN A 378 ? 0.4760 0.3696 0.5495 -0.0954 0.0660  0.0759  364 ASN A CA  
2679 C C   . ASN A 378 ? 0.4266 0.3612 0.5579 -0.0901 0.0629  0.0634  364 ASN A C   
2680 O O   . ASN A 378 ? 0.4208 0.3757 0.5802 -0.0905 0.0816  0.0610  364 ASN A O   
2681 C CB  . ASN A 378 ? 0.6019 0.4816 0.6809 -0.1045 0.0709  0.0908  364 ASN A CB  
2682 C CG  . ASN A 378 ? 0.5115 0.3905 0.6154 -0.1045 0.0420  0.0917  364 ASN A CG  
2683 O OD1 . ASN A 378 ? 0.4648 0.3711 0.6111 -0.0987 0.0288  0.0796  364 ASN A OD1 
2684 N ND2 . ASN A 378 ? 0.5502 0.3950 0.6257 -0.1106 0.0333  0.1064  364 ASN A ND2 
2685 N N   . PHE A 379 ? 0.3588 0.3045 0.5076 -0.0846 0.0403  0.0554  365 PHE A N   
2686 C CA  . PHE A 379 ? 0.3660 0.3444 0.5554 -0.0787 0.0389  0.0439  365 PHE A CA  
2687 C C   . PHE A 379 ? 0.3951 0.3845 0.5791 -0.0744 0.0517  0.0376  365 PHE A C   
2688 O O   . PHE A 379 ? 0.3466 0.3567 0.5582 -0.0724 0.0614  0.0331  365 PHE A O   
2689 C CB  . PHE A 379 ? 0.3679 0.3531 0.5722 -0.0732 0.0178  0.0372  365 PHE A CB  
2690 C CG  . PHE A 379 ? 0.3559 0.3678 0.5857 -0.0662 0.0186  0.0263  365 PHE A CG  
2691 C CD1 . PHE A 379 ? 0.3668 0.3943 0.6253 -0.0644 0.0181  0.0210  365 PHE A CD1 
2692 C CD2 . PHE A 379 ? 0.3539 0.3715 0.5761 -0.0618 0.0188  0.0219  365 PHE A CD2 
2693 C CE1 . PHE A 379 ? 0.3586 0.4041 0.6296 -0.0575 0.0176  0.0119  365 PHE A CE1 
2694 C CE2 . PHE A 379 ? 0.3015 0.3392 0.5409 -0.0559 0.0209  0.0146  365 PHE A CE2 
2695 C CZ  . PHE A 379 ? 0.3376 0.3879 0.5973 -0.0534 0.0204  0.0098  365 PHE A CZ  
2696 N N   . TRP A 380 ? 0.4171 0.3907 0.5678 -0.0726 0.0485  0.0367  366 TRP A N   
2697 C CA  . TRP A 380 ? 0.4028 0.3838 0.5495 -0.0680 0.0583  0.0300  366 TRP A CA  
2698 C C   . TRP A 380 ? 0.4295 0.4068 0.5674 -0.0697 0.0834  0.0318  366 TRP A C   
2699 O O   . TRP A 380 ? 0.4304 0.4242 0.5880 -0.0654 0.0942  0.0257  366 TRP A O   
2700 C CB  . TRP A 380 ? 0.3930 0.3554 0.5099 -0.0660 0.0451  0.0274  366 TRP A CB  
2701 C CG  . TRP A 380 ? 0.3600 0.3344 0.5015 -0.0635 0.0256  0.0244  366 TRP A CG  
2702 C CD1 . TRP A 380 ? 0.3642 0.3260 0.5031 -0.0647 0.0060  0.0270  366 TRP A CD1 
2703 C CD2 . TRP A 380 ? 0.3231 0.3237 0.4973 -0.0589 0.0258  0.0189  366 TRP A CD2 
2704 N NE1 . TRP A 380 ? 0.3611 0.3429 0.5346 -0.0611 -0.0025 0.0225  366 TRP A NE1 
2705 C CE2 . TRP A 380 ? 0.3897 0.3938 0.5802 -0.0577 0.0106  0.0181  366 TRP A CE2 
2706 C CE3 . TRP A 380 ? 0.3124 0.3316 0.5028 -0.0553 0.0371  0.0151  366 TRP A CE3 
2707 C CZ2 . TRP A 380 ? 0.2948 0.3196 0.5122 -0.0534 0.0112  0.0142  366 TRP A CZ2 
2708 C CZ3 . TRP A 380 ? 0.2809 0.3172 0.4925 -0.0512 0.0332  0.0121  366 TRP A CZ3 
2709 C CH2 . TRP A 380 ? 0.3745 0.4133 0.5971 -0.0504 0.0228  0.0119  366 TRP A CH2 
2710 N N   . LYS A 381 ? 0.3979 0.3524 0.5078 -0.0756 0.0942  0.0408  367 LYS A N   
2711 C CA  . LYS A 381 ? 0.5240 0.4771 0.6323 -0.0777 0.1244  0.0437  367 LYS A CA  
2712 C C   . LYS A 381 ? 0.4074 0.3920 0.5771 -0.0792 0.1331  0.0436  367 LYS A C   
2713 O O   . LYS A 381 ? 0.4160 0.4150 0.6105 -0.0770 0.1533  0.0400  367 LYS A O   
2714 C CB  . LYS A 381 ? 0.4967 0.4148 0.5566 -0.0845 0.1359  0.0559  367 LYS A CB  
2715 C CG  . LYS A 381 ? 0.5626 0.4439 0.5541 -0.0815 0.1328  0.0537  367 LYS A CG  
2716 C CD  . LYS A 381 ? 0.7302 0.5693 0.6617 -0.0878 0.1402  0.0672  367 LYS A CD  
2717 C CE  . LYS A 381 ? 0.8506 0.6474 0.7086 -0.0838 0.1266  0.0632  367 LYS A CE  
2718 N NZ  . LYS A 381 ? 0.8249 0.5729 0.6133 -0.0895 0.1284  0.0776  367 LYS A NZ  
2719 N N   . THR A 382 ? 0.4068 0.4007 0.6039 -0.0825 0.1167  0.0467  368 THR A N   
2720 C CA  . THR A 382 ? 0.4204 0.4409 0.6756 -0.0834 0.1177  0.0445  368 THR A CA  
2721 C C   . THR A 382 ? 0.4403 0.4845 0.7221 -0.0748 0.1088  0.0326  368 THR A C   
2722 O O   . THR A 382 ? 0.4026 0.4650 0.7241 -0.0733 0.1174  0.0294  368 THR A O   
2723 C CB  . THR A 382 ? 0.3477 0.3672 0.6197 -0.0876 0.0987  0.0480  368 THR A CB  
2724 O OG1 . THR A 382 ? 0.3419 0.3369 0.5914 -0.0964 0.1078  0.0617  368 THR A OG1 
2725 C CG2 . THR A 382 ? 0.3264 0.3694 0.6566 -0.0880 0.0937  0.0435  368 THR A CG2 
2726 N N   . LEU A 383 ? 0.3908 0.4336 0.6528 -0.0692 0.0915  0.0269  369 LEU A N   
2727 C CA  . LEU A 383 ? 0.3733 0.4333 0.6524 -0.0614 0.0836  0.0183  369 LEU A CA  
2728 C C   . LEU A 383 ? 0.3786 0.4407 0.6580 -0.0577 0.0998  0.0155  369 LEU A C   
2729 O O   . LEU A 383 ? 0.3499 0.4278 0.6581 -0.0524 0.0971  0.0103  369 LEU A O   
2730 C CB  . LEU A 383 ? 0.3890 0.4450 0.6467 -0.0575 0.0672  0.0153  369 LEU A CB  
2731 C CG  . LEU A 383 ? 0.4245 0.4946 0.6949 -0.0504 0.0576  0.0092  369 LEU A CG  
2732 C CD1 . LEU A 383 ? 0.3786 0.4618 0.6788 -0.0486 0.0491  0.0057  369 LEU A CD1 
2733 C CD2 . LEU A 383 ? 0.5861 0.6519 0.8396 -0.0483 0.0471  0.0084  369 LEU A CD2 
2734 N N   . GLN A 384 ? 0.3857 0.4288 0.6312 -0.0596 0.1153  0.0180  370 GLN A N   
2735 C CA  . GLN A 384 ? 0.3841 0.4261 0.6277 -0.0548 0.1327  0.0130  370 GLN A CA  
2736 C C   . GLN A 384 ? 0.3993 0.4609 0.6931 -0.0544 0.1493  0.0122  370 GLN A C   
2737 O O   . GLN A 384 ? 0.3848 0.4582 0.7043 -0.0475 0.1524  0.0056  370 GLN A O   
2738 C CB  . GLN A 384 ? 0.3417 0.3540 0.5325 -0.0568 0.1476  0.0150  370 GLN A CB  
2739 C CG  . GLN A 384 ? 0.3404 0.3473 0.5250 -0.0508 0.1694  0.0077  370 GLN A CG  
2740 C CD  . GLN A 384 ? 0.3965 0.4078 0.5857 -0.0429 0.1548  -0.0013 370 GLN A CD  
2741 O OE1 . GLN A 384 ? 0.4397 0.4399 0.6037 -0.0429 0.1345  -0.0020 370 GLN A OE1 
2742 N NE2 . GLN A 384 ? 0.4392 0.4665 0.6658 -0.0365 0.1644  -0.0076 370 GLN A NE2 
2743 N N   . THR A 385 ? 0.4133 0.4783 0.7275 -0.0617 0.1588  0.0194  371 THR A N   
2744 C CA  . THR A 385 ? 0.3906 0.4730 0.7558 -0.0605 0.1698  0.0185  371 THR A CA  
2745 C C   . THR A 385 ? 0.2723 0.3732 0.6769 -0.0544 0.1418  0.0124  371 THR A C   
2746 O O   . THR A 385 ? 0.3558 0.4667 0.7983 -0.0501 0.1423  0.0094  371 THR A O   
2747 C CB  . THR A 385 ? 0.3345 0.4097 0.7021 -0.0685 0.1816  0.0283  371 THR A CB  
2748 O OG1 . THR A 385 ? 0.4314 0.5090 0.8083 -0.0730 0.1573  0.0315  371 THR A OG1 
2749 C CG2 . THR A 385 ? 0.3847 0.4334 0.7002 -0.0753 0.2080  0.0368  371 THR A CG2 
2750 N N   . PHE A 386 ? 0.2601 0.3630 0.6557 -0.0541 0.1182  0.0107  372 PHE A N   
2751 C CA  . PHE A 386 ? 0.3259 0.4402 0.7482 -0.0490 0.0920  0.0055  372 PHE A CA  
2752 C C   . PHE A 386 ? 0.3274 0.4482 0.7547 -0.0407 0.0828  -0.0002 372 PHE A C   
2753 O O   . PHE A 386 ? 0.3343 0.4629 0.7907 -0.0354 0.0660  -0.0041 372 PHE A O   
2754 C CB  . PHE A 386 ? 0.2802 0.3911 0.6891 -0.0526 0.0738  0.0062  372 PHE A CB  
2755 C CG  . PHE A 386 ? 0.3456 0.4640 0.7732 -0.0475 0.0477  -0.0003 372 PHE A CG  
2756 C CD1 . PHE A 386 ? 0.3401 0.4618 0.8010 -0.0468 0.0355  -0.0029 372 PHE A CD1 
2757 C CD2 . PHE A 386 ? 0.4127 0.5276 0.8119 -0.0417 0.0342  -0.0038 372 PHE A CD2 
2758 C CE1 . PHE A 386 ? 0.3235 0.4480 0.7981 -0.0421 0.0085  -0.0102 372 PHE A CE1 
2759 C CE2 . PHE A 386 ? 0.3423 0.4576 0.7451 -0.0359 0.0111  -0.0098 372 PHE A CE2 
2760 C CZ  . PHE A 386 ? 0.3620 0.4831 0.8054 -0.0365 -0.0034 -0.0138 372 PHE A CZ  
2761 N N   . ILE A 387 ? 0.3369 0.4500 0.7325 -0.0389 0.0900  -0.0004 373 ILE A N   
2762 C CA  . ILE A 387 ? 0.3349 0.4483 0.7268 -0.0307 0.0783  -0.0040 373 ILE A CA  
2763 C C   . ILE A 387 ? 0.3202 0.4437 0.7545 -0.0252 0.0863  -0.0080 373 ILE A C   
2764 O O   . ILE A 387 ? 0.3761 0.4996 0.8229 -0.0265 0.1082  -0.0087 373 ILE A O   
2765 C CB  . ILE A 387 ? 0.3164 0.4140 0.6616 -0.0301 0.0814  -0.0032 373 ILE A CB  
2766 C CG1 . ILE A 387 ? 0.3453 0.4324 0.6763 -0.0315 0.1047  -0.0045 373 ILE A CG1 
2767 C CG2 . ILE A 387 ? 0.2393 0.3297 0.5544 -0.0348 0.0724  0.0003  373 ILE A CG2 
2768 C CD1 . ILE A 387 ? 0.4188 0.4861 0.7028 -0.0324 0.1032  -0.0044 373 ILE A CD1 
2769 N N   . ARG A 388 ? 0.2406 0.3672 0.6896 -0.0178 0.0673  -0.0102 374 ARG A N   
2770 C CA  . ARG A 388 ? 0.2704 0.4058 0.7661 -0.0109 0.0674  -0.0143 374 ARG A CA  
2771 C C   . ARG A 388 ? 0.3387 0.4654 0.8212 -0.0029 0.0557  -0.0148 374 ARG A C   
2772 O O   . ARG A 388 ? 0.3039 0.4183 0.7432 -0.0033 0.0435  -0.0107 374 ARG A O   
2773 C CB  . ARG A 388 ? 0.2518 0.3928 0.7824 -0.0094 0.0456  -0.0153 374 ARG A CB  
2774 C CG  . ARG A 388 ? 0.3061 0.4478 0.8471 -0.0163 0.0550  -0.0141 374 ARG A CG  
2775 C CD  . ARG A 388 ? 0.3039 0.4472 0.8751 -0.0154 0.0777  -0.0156 374 ARG A CD  
2776 N NE  . ARG A 388 ? 0.4223 0.5661 1.0069 -0.0223 0.0876  -0.0123 374 ARG A NE  
2777 C CZ  . ARG A 388 ? 0.4786 0.6171 1.0326 -0.0298 0.1051  -0.0070 374 ARG A CZ  
2778 N NH1 . ARG A 388 ? 0.4399 0.5715 0.9481 -0.0317 0.1144  -0.0054 374 ARG A NH1 
2779 N NH2 . ARG A 388 ? 0.4353 0.5739 1.0075 -0.0356 0.1121  -0.0027 374 ARG A NH2 
2780 N N   . PRO A 389 ? 0.2569 0.3882 0.7776 0.0045  0.0598  -0.0193 375 PRO A N   
2781 C CA  . PRO A 389 ? 0.2160 0.3360 0.7286 0.0125  0.0435  -0.0185 375 PRO A CA  
2782 C C   . PRO A 389 ? 0.2383 0.3529 0.7410 0.0146  0.0106  -0.0127 375 PRO A C   
2783 O O   . PRO A 389 ? 0.2712 0.3943 0.7986 0.0140  -0.0045 -0.0135 375 PRO A O   
2784 C CB  . PRO A 389 ? 0.2756 0.4052 0.8476 0.0208  0.0515  -0.0257 375 PRO A CB  
2785 C CG  . PRO A 389 ? 0.2287 0.3602 0.8003 0.0153  0.0824  -0.0299 375 PRO A CG  
2786 C CD  . PRO A 389 ? 0.2621 0.3969 0.8124 0.0053  0.0822  -0.0246 375 PRO A CD  
2787 N N   . GLY A 390 ? 0.2755 0.3728 0.7389 0.0169  -0.0004 -0.0068 376 GLY A N   
2788 C CA  . GLY A 390 ? 0.3075 0.3930 0.7460 0.0193  -0.0276 0.0002  376 GLY A CA  
2789 C C   . GLY A 390 ? 0.3369 0.4173 0.7272 0.0129  -0.0270 0.0041  376 GLY A C   
2790 O O   . GLY A 390 ? 0.3330 0.3998 0.6919 0.0154  -0.0452 0.0097  376 GLY A O   
2791 N N   . ASP A 391 ? 0.2595 0.3479 0.6411 0.0056  -0.0068 0.0014  377 ASP A N   
2792 C CA  . ASP A 391 ? 0.3512 0.4362 0.6956 0.0004  -0.0062 0.0037  377 ASP A CA  
2793 C C   . ASP A 391 ? 0.3674 0.4385 0.6706 -0.0002 -0.0037 0.0114  377 ASP A C   
2794 O O   . ASP A 391 ? 0.2960 0.3617 0.5978 -0.0004 0.0044  0.0141  377 ASP A O   
2795 C CB  . ASP A 391 ? 0.2542 0.3485 0.6023 -0.0071 0.0126  0.0001  377 ASP A CB  
2796 C CG  . ASP A 391 ? 0.3809 0.4870 0.7613 -0.0092 0.0090  -0.0046 377 ASP A CG  
2797 O OD1 . ASP A 391 ? 0.2934 0.3999 0.6892 -0.0050 -0.0119 -0.0065 377 ASP A OD1 
2798 O OD2 . ASP A 391 ? 0.2430 0.3552 0.6325 -0.0153 0.0256  -0.0059 377 ASP A OD2 
2799 N N   . ILE A 392 ? 0.3628 0.4274 0.6346 -0.0005 -0.0096 0.0143  378 ILE A N   
2800 C CA  . ILE A 392 ? 0.3500 0.4060 0.5888 -0.0032 -0.0002 0.0215  378 ILE A CA  
2801 C C   . ILE A 392 ? 0.3135 0.3780 0.5478 -0.0089 0.0109  0.0173  378 ILE A C   
2802 O O   . ILE A 392 ? 0.3309 0.3980 0.5611 -0.0080 0.0054  0.0123  378 ILE A O   
2803 C CB  . ILE A 392 ? 0.3318 0.3715 0.5354 0.0016  -0.0103 0.0287  378 ILE A CB  
2804 C CG1 . ILE A 392 ? 0.2842 0.3116 0.4921 0.0075  -0.0258 0.0343  378 ILE A CG1 
2805 C CG2 . ILE A 392 ? 0.2738 0.3077 0.4513 -0.0023 0.0057  0.0370  378 ILE A CG2 
2806 C CD1 . ILE A 392 ? 0.3272 0.3319 0.4922 0.0129  -0.0391 0.0425  378 ILE A CD1 
2807 N N   . ILE A 393 ? 0.3059 0.3722 0.5425 -0.0141 0.0235  0.0187  379 ILE A N   
2808 C CA  . ILE A 393 ? 0.2241 0.2960 0.4602 -0.0194 0.0311  0.0154  379 ILE A CA  
2809 C C   . ILE A 393 ? 0.2494 0.3177 0.4734 -0.0218 0.0378  0.0211  379 ILE A C   
2810 O O   . ILE A 393 ? 0.2799 0.3424 0.5059 -0.0236 0.0409  0.0263  379 ILE A O   
2811 C CB  . ILE A 393 ? 0.1812 0.2549 0.4306 -0.0235 0.0374  0.0116  379 ILE A CB  
2812 C CG1 . ILE A 393 ? 0.2829 0.3631 0.5523 -0.0218 0.0363  0.0068  379 ILE A CG1 
2813 C CG2 . ILE A 393 ? 0.2361 0.3096 0.4797 -0.0289 0.0412  0.0106  379 ILE A CG2 
2814 C CD1 . ILE A 393 ? 0.2087 0.2872 0.4862 -0.0243 0.0480  0.0038  379 ILE A CD1 
2815 N N   . LEU A 394 ? 0.2287 0.3001 0.4453 -0.0218 0.0405  0.0195  380 LEU A N   
2816 C CA  . LEU A 394 ? 0.2843 0.3559 0.4995 -0.0239 0.0500  0.0241  380 LEU A CA  
2817 C C   . LEU A 394 ? 0.3061 0.3839 0.5347 -0.0272 0.0508  0.0189  380 LEU A C   
2818 O O   . LEU A 394 ? 0.2221 0.3027 0.4499 -0.0256 0.0465  0.0123  380 LEU A O   
2819 C CB  . LEU A 394 ? 0.2329 0.2998 0.4256 -0.0187 0.0557  0.0272  380 LEU A CB  
2820 C CG  . LEU A 394 ? 0.3078 0.3624 0.4777 -0.0141 0.0507  0.0336  380 LEU A CG  
2821 C CD1 . LEU A 394 ? 0.2851 0.3362 0.4439 -0.0085 0.0354  0.0259  380 LEU A CD1 
2822 C CD2 . LEU A 394 ? 0.2792 0.3242 0.4238 -0.0121 0.0643  0.0425  380 LEU A CD2 
2823 N N   . ALA A 395 ? 0.2895 0.3677 0.5333 -0.0319 0.0534  0.0219  381 ALA A N   
2824 C CA  . ALA A 395 ? 0.3036 0.3843 0.5623 -0.0350 0.0496  0.0180  381 ALA A CA  
2825 C C   . ALA A 395 ? 0.3456 0.4312 0.6261 -0.0366 0.0561  0.0217  381 ALA A C   
2826 O O   . ALA A 395 ? 0.2568 0.3403 0.5471 -0.0396 0.0593  0.0282  381 ALA A O   
2827 C CB  . ALA A 395 ? 0.2582 0.3299 0.5161 -0.0396 0.0403  0.0167  381 ALA A CB  
2828 N N   . ASP A 396 ? 0.2584 0.3506 0.5523 -0.0345 0.0582  0.0174  382 ASP A N   
2829 C CA  . ASP A 396 ? 0.2993 0.3996 0.6239 -0.0350 0.0675  0.0199  382 ASP A CA  
2830 C C   . ASP A 396 ? 0.2460 0.3445 0.6016 -0.0403 0.0526  0.0197  382 ASP A C   
2831 O O   . ASP A 396 ? 0.3034 0.3922 0.6487 -0.0424 0.0361  0.0164  382 ASP A O   
2832 C CB  . ASP A 396 ? 0.2235 0.3313 0.5510 -0.0282 0.0789  0.0137  382 ASP A CB  
2833 C CG  . ASP A 396 ? 0.3496 0.4654 0.6935 -0.0263 0.1020  0.0186  382 ASP A CG  
2834 O OD1 . ASP A 396 ? 0.2475 0.3676 0.6233 -0.0321 0.1050  0.0263  382 ASP A OD1 
2835 O OD2 . ASP A 396 ? 0.2982 0.4141 0.6224 -0.0190 0.1178  0.0146  382 ASP A OD2 
2836 N N   . GLN A 397 ? 0.1967 0.3029 0.5908 -0.0427 0.0584  0.0238  383 GLN A N   
2837 C CA  . GLN A 397 ? 0.1729 0.2742 0.5977 -0.0460 0.0396  0.0226  383 GLN A CA  
2838 C C   . GLN A 397 ? 0.2536 0.3552 0.6877 -0.0431 0.0280  0.0156  383 GLN A C   
2839 O O   . GLN A 397 ? 0.3737 0.4854 0.8129 -0.0373 0.0407  0.0112  383 GLN A O   
2840 C CB  . GLN A 397 ? 0.1848 0.2904 0.6417 -0.0450 0.0481  0.0269  383 GLN A CB  
2841 C CG  . GLN A 397 ? 0.2698 0.3716 0.7223 -0.0490 0.0556  0.0354  383 GLN A CG  
2842 C CD  . GLN A 397 ? 0.3322 0.4193 0.7708 -0.0546 0.0348  0.0352  383 GLN A CD  
2843 O OE1 . GLN A 397 ? 0.4501 0.5267 0.9047 -0.0572 0.0125  0.0324  383 GLN A OE1 
2844 N NE2 . GLN A 397 ? 0.2848 0.3690 0.6940 -0.0561 0.0414  0.0374  383 GLN A NE2 
2845 N N   . GLY A 398 ? 0.3149 0.4025 0.7499 -0.0473 0.0029  0.0146  384 GLY A N   
2846 C CA  . GLY A 398 ? 0.2694 0.3491 0.6994 -0.0453 -0.0119 0.0103  384 GLY A CA  
2847 C C   . GLY A 398 ? 0.3649 0.4220 0.7464 -0.0487 -0.0257 0.0113  384 GLY A C   
2848 O O   . GLY A 398 ? 0.3102 0.3571 0.6687 -0.0520 -0.0272 0.0135  384 GLY A O   
2849 N N   . THR A 399 ? 0.2391 0.2867 0.6048 -0.0476 -0.0341 0.0099  385 THR A N   
2850 C CA  . THR A 399 ? 0.2808 0.3068 0.5992 -0.0511 -0.0410 0.0124  385 THR A CA  
2851 C C   . THR A 399 ? 0.2898 0.3224 0.5811 -0.0507 -0.0213 0.0123  385 THR A C   
2852 O O   . THR A 399 ? 0.3540 0.3713 0.6114 -0.0535 -0.0215 0.0140  385 THR A O   
2853 C CB  . THR A 399 ? 0.2880 0.3027 0.5983 -0.0508 -0.0507 0.0134  385 THR A CB  
2854 O OG1 . THR A 399 ? 0.3294 0.3615 0.6505 -0.0466 -0.0357 0.0094  385 THR A OG1 
2855 C CG2 . THR A 399 ? 0.2565 0.2628 0.5973 -0.0501 -0.0740 0.0136  385 THR A CG2 
2856 N N   . SER A 400 ? 0.2621 0.3153 0.5671 -0.0466 -0.0046 0.0100  386 SER A N   
2857 C CA  . SER A 400 ? 0.2531 0.3117 0.5372 -0.0454 0.0094  0.0099  386 SER A CA  
2858 C C   . SER A 400 ? 0.3351 0.3876 0.6086 -0.0477 0.0108  0.0124  386 SER A C   
2859 O O   . SER A 400 ? 0.2983 0.3410 0.5475 -0.0490 0.0123  0.0125  386 SER A O   
2860 C CB  . SER A 400 ? 0.2121 0.2874 0.5066 -0.0398 0.0228  0.0071  386 SER A CB  
2861 O OG  . SER A 400 ? 0.2822 0.3594 0.5787 -0.0367 0.0213  0.0021  386 SER A OG  
2862 N N   . ALA A 401 ? 0.2892 0.3472 0.5841 -0.0481 0.0119  0.0144  387 ALA A N   
2863 C CA  . ALA A 401 ? 0.2922 0.3421 0.5807 -0.0504 0.0109  0.0165  387 ALA A CA  
2864 C C   . ALA A 401 ? 0.3582 0.3851 0.6293 -0.0539 -0.0059 0.0143  387 ALA A C   
2865 O O   . ALA A 401 ? 0.2935 0.3074 0.5408 -0.0541 -0.0053 0.0126  387 ALA A O   
2866 C CB  . ALA A 401 ? 0.2109 0.2702 0.5319 -0.0516 0.0155  0.0208  387 ALA A CB  
2867 N N   . PHE A 402 ? 0.3320 0.3506 0.6122 -0.0557 -0.0220 0.0138  388 PHE A N   
2868 C CA  . PHE A 402 ? 0.4597 0.4497 0.7159 -0.0585 -0.0423 0.0120  388 PHE A CA  
2869 C C   . PHE A 402 ? 0.4652 0.4373 0.6731 -0.0584 -0.0386 0.0115  388 PHE A C   
2870 O O   . PHE A 402 ? 0.3650 0.3085 0.5367 -0.0597 -0.0492 0.0095  388 PHE A O   
2871 C CB  . PHE A 402 ? 0.3357 0.3201 0.6194 -0.0600 -0.0648 0.0126  388 PHE A CB  
2872 C CG  . PHE A 402 ? 0.3971 0.3993 0.7373 -0.0610 -0.0667 0.0135  388 PHE A CG  
2873 C CD1 . PHE A 402 ? 0.4941 0.5057 0.8466 -0.0621 -0.0540 0.0150  388 PHE A CD1 
2874 C CD2 . PHE A 402 ? 0.4350 0.4441 0.8202 -0.0609 -0.0800 0.0138  388 PHE A CD2 
2875 C CE1 . PHE A 402 ? 0.5282 0.5555 0.9352 -0.0643 -0.0521 0.0182  388 PHE A CE1 
2876 C CE2 . PHE A 402 ? 0.4559 0.4829 0.8978 -0.0612 -0.0770 0.0154  388 PHE A CE2 
2877 C CZ  . PHE A 402 ? 0.4706 0.5056 0.9176 -0.0621 -0.0612 0.0182  388 PHE A CZ  
2878 N N   . GLY A 403 ? 0.3275 0.3138 0.5336 -0.0569 -0.0232 0.0130  389 GLY A N   
2879 C CA  . GLY A 403 ? 0.3551 0.3280 0.5247 -0.0578 -0.0147 0.0141  389 GLY A CA  
2880 C C   . GLY A 403 ? 0.3646 0.3467 0.5278 -0.0556 0.0049  0.0117  389 GLY A C   
2881 O O   . GLY A 403 ? 0.3447 0.3114 0.4775 -0.0558 0.0137  0.0107  389 GLY A O   
2882 N N   . ALA A 404 ? 0.2928 0.2985 0.4841 -0.0527 0.0123  0.0109  390 ALA A N   
2883 C CA  . ALA A 404 ? 0.3453 0.3595 0.5363 -0.0497 0.0264  0.0091  390 ALA A CA  
2884 C C   . ALA A 404 ? 0.3376 0.3355 0.5123 -0.0487 0.0263  0.0055  390 ALA A C   
2885 O O   . ALA A 404 ? 0.3518 0.3508 0.5224 -0.0457 0.0382  0.0027  390 ALA A O   
2886 C CB  . ALA A 404 ? 0.2635 0.2991 0.4798 -0.0465 0.0303  0.0104  390 ALA A CB  
2887 N N   . ILE A 405 ? 0.3831 0.3645 0.5518 -0.0508 0.0114  0.0044  391 ILE A N   
2888 C CA  . ILE A 405 ? 0.3988 0.3602 0.5506 -0.0496 0.0076  -0.0011 391 ILE A CA  
2889 C C   . ILE A 405 ? 0.5478 0.4880 0.6585 -0.0476 0.0178  -0.0062 391 ILE A C   
2890 O O   . ILE A 405 ? 0.3724 0.2991 0.4689 -0.0440 0.0226  -0.0131 391 ILE A O   
2891 C CB  . ILE A 405 ? 0.3417 0.2864 0.4975 -0.0528 -0.0156 -0.0021 391 ILE A CB  
2892 C CG1 . ILE A 405 ? 0.3224 0.2513 0.4756 -0.0515 -0.0217 -0.0080 391 ILE A CG1 
2893 C CG2 . ILE A 405 ? 0.4126 0.3308 0.5339 -0.0549 -0.0299 -0.0032 391 ILE A CG2 
2894 C CD1 . ILE A 405 ? 0.3563 0.2685 0.5219 -0.0553 -0.0479 -0.0096 391 ILE A CD1 
2895 N N   . ASP A 406 ? 0.4210 0.3565 0.5126 -0.0498 0.0230  -0.0028 392 ASP A N   
2896 C CA  . ASP A 406 ? 0.3858 0.2999 0.4362 -0.0489 0.0380  -0.0052 392 ASP A CA  
2897 C C   . ASP A 406 ? 0.4032 0.3382 0.4724 -0.0463 0.0639  -0.0053 392 ASP A C   
2898 O O   . ASP A 406 ? 0.4243 0.3457 0.4676 -0.0452 0.0830  -0.0071 392 ASP A O   
2899 C CB  . ASP A 406 ? 0.5581 0.4530 0.5784 -0.0536 0.0312  0.0014  392 ASP A CB  
2900 C CG  . ASP A 406 ? 0.5320 0.3988 0.5294 -0.0553 0.0019  0.0004  392 ASP A CG  
2901 O OD1 . ASP A 406 ? 0.5662 0.4138 0.5470 -0.0528 -0.0079 -0.0076 392 ASP A OD1 
2902 O OD2 . ASP A 406 ? 0.6878 0.5501 0.6869 -0.0589 -0.0136 0.0070  392 ASP A OD2 
2903 N N   . LEU A 407 ? 0.3827 0.3487 0.4961 -0.0450 0.0651  -0.0032 393 LEU A N   
2904 C CA  . LEU A 407 ? 0.3491 0.3342 0.4873 -0.0419 0.0837  -0.0042 393 LEU A CA  
2905 C C   . LEU A 407 ? 0.4363 0.4144 0.5725 -0.0356 0.0941  -0.0125 393 LEU A C   
2906 O O   . LEU A 407 ? 0.3672 0.3371 0.5008 -0.0330 0.0827  -0.0164 393 LEU A O   
2907 C CB  . LEU A 407 ? 0.2772 0.2902 0.4553 -0.0411 0.0765  -0.0009 393 LEU A CB  
2908 C CG  . LEU A 407 ? 0.3996 0.4219 0.5861 -0.0454 0.0690  0.0047  393 LEU A CG  
2909 C CD1 . LEU A 407 ? 0.2690 0.3110 0.4818 -0.0427 0.0601  0.0055  393 LEU A CD1 
2910 C CD2 . LEU A 407 ? 0.3602 0.3855 0.5524 -0.0485 0.0819  0.0073  393 LEU A CD2 
2911 N N   . ARG A 408 ? 0.4224 0.4036 0.5645 -0.0330 0.1166  -0.0152 394 ARG A N   
2912 C CA  . ARG A 408 ? 0.4166 0.3946 0.5664 -0.0252 0.1298  -0.0245 394 ARG A CA  
2913 C C   . ARG A 408 ? 0.4120 0.4198 0.6171 -0.0214 0.1283  -0.0234 394 ARG A C   
2914 O O   . ARG A 408 ? 0.3672 0.3931 0.6032 -0.0219 0.1401  -0.0211 394 ARG A O   
2915 C CB  . ARG A 408 ? 0.4912 0.4538 0.6170 -0.0237 0.1584  -0.0288 394 ARG A CB  
2916 C CG  . ARG A 408 ? 0.5779 0.5349 0.7113 -0.0140 0.1754  -0.0410 394 ARG A CG  
2917 C CD  . ARG A 408 ? 0.6328 0.5541 0.7074 -0.0115 0.1960  -0.0488 394 ARG A CD  
2918 N NE  . ARG A 408 ? 0.7732 0.7009 0.8590 -0.0102 0.2333  -0.0488 394 ARG A NE  
2919 C CZ  . ARG A 408 ? 1.0539 0.9615 1.1149 -0.0026 0.2627  -0.0599 394 ARG A CZ  
2920 N NH1 . ARG A 408 ? 0.9007 0.7779 0.9208 0.0051  0.2565  -0.0737 394 ARG A NH1 
2921 N NH2 . ARG A 408 ? 1.0493 0.9668 1.1292 -0.0026 0.3004  -0.0577 394 ARG A NH2 
2922 N N   . LEU A 409 ? 0.3936 0.4043 0.6116 -0.0181 0.1116  -0.0240 395 LEU A N   
2923 C CA  . LEU A 409 ? 0.3319 0.3648 0.5921 -0.0147 0.1031  -0.0206 395 LEU A CA  
2924 C C   . LEU A 409 ? 0.4170 0.4558 0.7098 -0.0063 0.1154  -0.0278 395 LEU A C   
2925 O O   . LEU A 409 ? 0.3898 0.4128 0.6725 -0.0009 0.1222  -0.0360 395 LEU A O   
2926 C CB  . LEU A 409 ? 0.3487 0.3787 0.6066 -0.0145 0.0832  -0.0161 395 LEU A CB  
2927 C CG  . LEU A 409 ? 0.4520 0.4790 0.6893 -0.0215 0.0714  -0.0094 395 LEU A CG  
2928 C CD1 . LEU A 409 ? 0.3078 0.3340 0.5515 -0.0210 0.0580  -0.0037 395 LEU A CD1 
2929 C CD2 . LEU A 409 ? 0.2828 0.3249 0.5261 -0.0254 0.0709  -0.0047 395 LEU A CD2 
2930 N N   . PRO A 410 ? 0.4300 0.4902 0.7658 -0.0045 0.1165  -0.0261 396 PRO A N   
2931 C CA  . PRO A 410 ? 0.4553 0.5237 0.8348 0.0046  0.1237  -0.0327 396 PRO A CA  
2932 C C   . PRO A 410 ? 0.4015 0.4662 0.7927 0.0108  0.1020  -0.0315 396 PRO A C   
2933 O O   . PRO A 410 ? 0.4305 0.4846 0.7922 0.0076  0.0864  -0.0254 396 PRO A O   
2934 C CB  . PRO A 410 ? 0.3441 0.4363 0.7702 0.0030  0.1254  -0.0299 396 PRO A CB  
2935 C CG  . PRO A 410 ? 0.2967 0.3918 0.7020 -0.0053 0.1099  -0.0213 396 PRO A CG  
2936 C CD  . PRO A 410 ? 0.2582 0.3346 0.6084 -0.0096 0.1059  -0.0188 396 PRO A CD  
2937 N N   . ALA A 411 ? 0.3454 0.4178 0.7824 0.0197  0.1015  -0.0363 397 ALA A N   
2938 C CA  . ALA A 411 ? 0.4711 0.5356 0.9192 0.0264  0.0804  -0.0339 397 ALA A CA  
2939 C C   . ALA A 411 ? 0.3305 0.3994 0.7757 0.0236  0.0536  -0.0218 397 ALA A C   
2940 O O   . ALA A 411 ? 0.3696 0.4524 0.8243 0.0200  0.0491  -0.0188 397 ALA A O   
2941 C CB  . ALA A 411 ? 0.3364 0.4077 0.8403 0.0377  0.0848  -0.0425 397 ALA A CB  
2942 N N   . ASP A 412 ? 0.3289 0.3826 0.7586 0.0256  0.0362  -0.0149 398 ASP A N   
2943 C CA  . ASP A 412 ? 0.3341 0.3849 0.7546 0.0254  0.0118  -0.0029 398 ASP A CA  
2944 C C   . ASP A 412 ? 0.3758 0.4310 0.7616 0.0167  0.0115  0.0031  398 ASP A C   
2945 O O   . ASP A 412 ? 0.3759 0.4351 0.7606 0.0172  -0.0033 0.0075  398 ASP A O   
2946 C CB  . ASP A 412 ? 0.2674 0.3270 0.7327 0.0333  -0.0050 -0.0040 398 ASP A CB  
2947 C CG  . ASP A 412 ? 0.6816 0.7360 1.1869 0.0435  -0.0078 -0.0094 398 ASP A CG  
2948 O OD1 . ASP A 412 ? 0.7795 0.8144 1.2681 0.0457  -0.0157 -0.0041 398 ASP A OD1 
2949 O OD2 . ASP A 412 ? 0.6807 0.7506 1.2389 0.0494  -0.0013 -0.0190 398 ASP A OD2 
2950 N N   . VAL A 413 ? 0.3802 0.4321 0.7375 0.0096  0.0256  0.0024  399 VAL A N   
2951 C CA  . VAL A 413 ? 0.3643 0.4194 0.6927 0.0022  0.0260  0.0073  399 VAL A CA  
2952 C C   . VAL A 413 ? 0.3760 0.4178 0.6765 -0.0010 0.0214  0.0170  399 VAL A C   
2953 O O   . VAL A 413 ? 0.3607 0.3913 0.6578 -0.0022 0.0253  0.0168  399 VAL A O   
2954 C CB  . VAL A 413 ? 0.3057 0.3660 0.6263 -0.0037 0.0427  0.0009  399 VAL A CB  
2955 C CG1 . VAL A 413 ? 0.2600 0.3211 0.5540 -0.0105 0.0413  0.0059  399 VAL A CG1 
2956 C CG2 . VAL A 413 ? 0.2881 0.3627 0.6380 -0.0023 0.0503  -0.0053 399 VAL A CG2 
2957 N N   . ASN A 414 ? 0.2905 0.3316 0.5720 -0.0021 0.0137  0.0250  400 ASN A N   
2958 C CA  . ASN A 414 ? 0.2759 0.3073 0.5329 -0.0065 0.0157  0.0353  400 ASN A CA  
2959 C C   . ASN A 414 ? 0.3578 0.3981 0.6042 -0.0129 0.0257  0.0326  400 ASN A C   
2960 O O   . ASN A 414 ? 0.2869 0.3348 0.5255 -0.0126 0.0245  0.0306  400 ASN A O   
2961 C CB  . ASN A 414 ? 0.2625 0.2837 0.4988 -0.0029 0.0052  0.0460  400 ASN A CB  
2962 C CG  . ASN A 414 ? 0.3648 0.3750 0.5789 -0.0076 0.0130  0.0589  400 ASN A CG  
2963 O OD1 . ASN A 414 ? 0.3495 0.3648 0.5682 -0.0142 0.0248  0.0584  400 ASN A OD1 
2964 N ND2 . ASN A 414 ? 0.3588 0.3524 0.5499 -0.0045 0.0061  0.0712  400 ASN A ND2 
2965 N N   . PHE A 415 ? 0.3050 0.3421 0.5531 -0.0182 0.0325  0.0319  401 PHE A N   
2966 C CA  . PHE A 415 ? 0.3408 0.3840 0.5846 -0.0240 0.0383  0.0290  401 PHE A CA  
2967 C C   . PHE A 415 ? 0.3899 0.4301 0.6309 -0.0283 0.0417  0.0383  401 PHE A C   
2968 O O   . PHE A 415 ? 0.2963 0.3273 0.5458 -0.0312 0.0410  0.0427  401 PHE A O   
2969 C CB  . PHE A 415 ? 0.2838 0.3218 0.5310 -0.0263 0.0403  0.0205  401 PHE A CB  
2970 C CG  . PHE A 415 ? 0.4148 0.4535 0.6563 -0.0319 0.0411  0.0184  401 PHE A CG  
2971 C CD1 . PHE A 415 ? 0.2906 0.3231 0.5368 -0.0367 0.0377  0.0219  401 PHE A CD1 
2972 C CD2 . PHE A 415 ? 0.3942 0.4387 0.6304 -0.0328 0.0436  0.0135  401 PHE A CD2 
2973 C CE1 . PHE A 415 ? 0.2940 0.3259 0.5400 -0.0411 0.0341  0.0197  401 PHE A CE1 
2974 C CE2 . PHE A 415 ? 0.4414 0.4831 0.6721 -0.0375 0.0410  0.0126  401 PHE A CE2 
2975 C CZ  . PHE A 415 ? 0.2977 0.3331 0.5337 -0.0411 0.0350  0.0152  401 PHE A CZ  
2976 N N   . ILE A 416 ? 0.2777 0.3254 0.5102 -0.0285 0.0465  0.0410  402 ILE A N   
2977 C CA  . ILE A 416 ? 0.2565 0.3032 0.4890 -0.0315 0.0554  0.0507  402 ILE A CA  
2978 C C   . ILE A 416 ? 0.3628 0.4188 0.6108 -0.0361 0.0596  0.0467  402 ILE A C   
2979 O O   . ILE A 416 ? 0.2644 0.3285 0.5077 -0.0342 0.0606  0.0405  402 ILE A O   
2980 C CB  . ILE A 416 ? 0.3455 0.3893 0.5526 -0.0266 0.0603  0.0566  402 ILE A CB  
2981 C CG1 . ILE A 416 ? 0.2661 0.2955 0.4591 -0.0226 0.0528  0.0643  402 ILE A CG1 
2982 C CG2 . ILE A 416 ? 0.2593 0.3048 0.4667 -0.0296 0.0770  0.0650  402 ILE A CG2 
2983 C CD1 . ILE A 416 ? 0.2943 0.3146 0.4524 -0.0160 0.0501  0.0676  402 ILE A CD1 
2984 N N   . VAL A 417 ? 0.3525 0.4059 0.6225 -0.0420 0.0598  0.0505  403 VAL A N   
2985 C CA  . VAL A 417 ? 0.3624 0.4229 0.6551 -0.0463 0.0594  0.0475  403 VAL A CA  
2986 C C   . VAL A 417 ? 0.4391 0.4998 0.7607 -0.0519 0.0666  0.0577  403 VAL A C   
2987 O O   . VAL A 417 ? 0.2707 0.3216 0.5945 -0.0540 0.0668  0.0655  403 VAL A O   
2988 C CB  . VAL A 417 ? 0.3931 0.4464 0.6867 -0.0483 0.0441  0.0379  403 VAL A CB  
2989 C CG1 . VAL A 417 ? 0.2567 0.2952 0.5582 -0.0516 0.0349  0.0384  403 VAL A CG1 
2990 C CG2 . VAL A 417 ? 0.4001 0.4589 0.7107 -0.0508 0.0389  0.0339  403 VAL A CG2 
2991 N N   . GLN A 418 ? 0.3786 0.3654 0.5555 0.0039  0.0298  -0.0131 404 GLN A N   
2992 C CA  . GLN A 418 ? 0.3178 0.2970 0.4928 0.0027  0.0237  -0.0126 404 GLN A CA  
2993 C C   . GLN A 418 ? 0.3272 0.3054 0.4893 0.0017  0.0238  -0.0141 404 GLN A C   
2994 O O   . GLN A 418 ? 0.2764 0.2536 0.4332 -0.0008 0.0217  -0.0093 404 GLN A O   
2995 C CB  . GLN A 418 ? 0.3326 0.3103 0.5100 -0.0003 0.0201  -0.0055 404 GLN A CB  
2996 C CG  . GLN A 418 ? 0.3250 0.2977 0.5035 -0.0019 0.0141  -0.0033 404 GLN A CG  
2997 C CD  . GLN A 418 ? 0.3010 0.2749 0.4769 -0.0045 0.0123  0.0033  404 GLN A CD  
2998 O OE1 . GLN A 418 ? 0.3326 0.3081 0.5006 -0.0052 0.0144  0.0049  404 GLN A OE1 
2999 N NE2 . GLN A 418 ? 0.2792 0.2525 0.4618 -0.0056 0.0082  0.0070  404 GLN A NE2 
3000 N N   . PRO A 419 ? 0.3586 0.3379 0.5158 0.0041  0.0259  -0.0211 405 PRO A N   
3001 C CA  . PRO A 419 ? 0.2677 0.2476 0.4117 0.0029  0.0256  -0.0222 405 PRO A CA  
3002 C C   . PRO A 419 ? 0.4495 0.4231 0.5923 0.0013  0.0186  -0.0240 405 PRO A C   
3003 O O   . PRO A 419 ? 0.3436 0.3186 0.4767 -0.0003 0.0170  -0.0232 405 PRO A O   
3004 C CB  . PRO A 419 ? 0.3714 0.3566 0.5096 0.0062  0.0309  -0.0296 405 PRO A CB  
3005 C CG  . PRO A 419 ? 0.3419 0.3280 0.4924 0.0099  0.0334  -0.0337 405 PRO A CG  
3006 C CD  . PRO A 419 ? 0.2794 0.2599 0.4424 0.0086  0.0285  -0.0289 405 PRO A CD  
3007 N N   . LEU A 420 ? 0.3019 0.2692 0.4551 0.0014  0.0140  -0.0257 406 LEU A N   
3008 C CA  . LEU A 420 ? 0.3504 0.3122 0.5041 -0.0015 0.0069  -0.0258 406 LEU A CA  
3009 C C   . LEU A 420 ? 0.2759 0.2401 0.4311 -0.0051 0.0045  -0.0161 406 LEU A C   
3010 O O   . LEU A 420 ? 0.3237 0.2905 0.4730 -0.0074 0.0023  -0.0137 406 LEU A O   
3011 C CB  . LEU A 420 ? 0.2799 0.2328 0.4446 -0.0006 0.0021  -0.0304 406 LEU A CB  
3012 C CG  . LEU A 420 ? 0.2861 0.2332 0.4546 -0.0053 -0.0062 -0.0282 406 LEU A CG  
3013 C CD1 . LEU A 420 ? 0.2907 0.2389 0.4483 -0.0074 -0.0087 -0.0321 406 LEU A CD1 
3014 C CD2 . LEU A 420 ? 0.2916 0.2278 0.4720 -0.0046 -0.0116 -0.0321 406 LEU A CD2 
3015 N N   . TRP A 421 ? 0.2551 0.2197 0.4183 -0.0054 0.0049  -0.0107 407 TRP A N   
3016 C CA  . TRP A 421 ? 0.2928 0.2612 0.4556 -0.0078 0.0039  -0.0026 407 TRP A CA  
3017 C C   . TRP A 421 ? 0.3154 0.2886 0.4692 -0.0068 0.0085  -0.0005 407 TRP A C   
3018 O O   . TRP A 421 ? 0.3561 0.3324 0.5052 -0.0077 0.0075  0.0030  407 TRP A O   
3019 C CB  . TRP A 421 ? 0.2575 0.2256 0.4291 -0.0083 0.0028  0.0021  407 TRP A CB  
3020 C CG  . TRP A 421 ? 0.3026 0.2754 0.4737 -0.0105 0.0015  0.0096  407 TRP A CG  
3021 C CD1 . TRP A 421 ? 0.2518 0.2282 0.4216 -0.0100 0.0037  0.0134  407 TRP A CD1 
3022 C CD2 . TRP A 421 ? 0.2634 0.2390 0.4353 -0.0135 -0.0021 0.0136  407 TRP A CD2 
3023 N NE1 . TRP A 421 ? 0.3375 0.3190 0.5064 -0.0116 0.0023  0.0189  407 TRP A NE1 
3024 C CE2 . TRP A 421 ? 0.3533 0.3355 0.5242 -0.0138 -0.0010 0.0197  407 TRP A CE2 
3025 C CE3 . TRP A 421 ? 0.3213 0.2952 0.4951 -0.0160 -0.0064 0.0123  407 TRP A CE3 
3026 C CZ2 . TRP A 421 ? 0.2708 0.2598 0.4432 -0.0162 -0.0029 0.0253  407 TRP A CZ2 
3027 C CZ3 . TRP A 421 ? 0.3448 0.3250 0.5212 -0.0194 -0.0093 0.0185  407 TRP A CZ3 
3028 C CH2 . TRP A 421 ? 0.2962 0.2847 0.4721 -0.0192 -0.0070 0.0252  407 TRP A CH2 
3029 N N   . GLY A 422 ? 0.2742 0.2483 0.4266 -0.0049 0.0132  -0.0020 408 GLY A N   
3030 C CA  . GLY A 422 ? 0.2434 0.2203 0.3878 -0.0044 0.0171  0.0002  408 GLY A CA  
3031 C C   . GLY A 422 ? 0.2672 0.2447 0.4107 -0.0049 0.0169  0.0059  408 GLY A C   
3032 O O   . GLY A 422 ? 0.2830 0.2615 0.4201 -0.0045 0.0174  0.0084  408 GLY A O   
3033 N N   . SER A 423 ? 0.2931 0.2700 0.4427 -0.0054 0.0161  0.0078  409 SER A N   
3034 C CA  . SER A 423 ? 0.2570 0.2343 0.4050 -0.0052 0.0159  0.0116  409 SER A CA  
3035 C C   . SER A 423 ? 0.3107 0.2860 0.4576 -0.0053 0.0187  0.0118  409 SER A C   
3036 O O   . SER A 423 ? 0.3664 0.3417 0.5189 -0.0062 0.0191  0.0109  409 SER A O   
3037 C CB  . SER A 423 ? 0.2513 0.2301 0.4047 -0.0062 0.0129  0.0136  409 SER A CB  
3038 O OG  . SER A 423 ? 0.3226 0.3027 0.4728 -0.0054 0.0131  0.0159  409 SER A OG  
3039 N N   . ILE A 424 ? 0.3059 0.2793 0.4468 -0.0045 0.0201  0.0135  410 ILE A N   
3040 C CA  . ILE A 424 ? 0.3506 0.3208 0.4916 -0.0056 0.0220  0.0144  410 ILE A CA  
3041 C C   . ILE A 424 ? 0.3340 0.3019 0.4774 -0.0060 0.0199  0.0142  410 ILE A C   
3042 O O   . ILE A 424 ? 0.3124 0.2814 0.4543 -0.0044 0.0179  0.0143  410 ILE A O   
3043 C CB  . ILE A 424 ? 0.2603 0.2273 0.3950 -0.0049 0.0232  0.0172  410 ILE A CB  
3044 C CG1 . ILE A 424 ? 0.3204 0.2849 0.4518 -0.0019 0.0211  0.0183  410 ILE A CG1 
3045 C CG2 . ILE A 424 ? 0.3299 0.3005 0.4604 -0.0049 0.0250  0.0175  410 ILE A CG2 
3046 C CD1 . ILE A 424 ? 0.2939 0.2526 0.4213 -0.0007 0.0214  0.0215  410 ILE A CD1 
3047 N N   . GLY A 425 ? 0.2802 0.2464 0.4273 -0.0083 0.0202  0.0141  411 GLY A N   
3048 C CA  . GLY A 425 ? 0.3116 0.2768 0.4613 -0.0095 0.0175  0.0132  411 GLY A CA  
3049 C C   . GLY A 425 ? 0.3643 0.3348 0.5217 -0.0107 0.0161  0.0127  411 GLY A C   
3050 O O   . GLY A 425 ? 0.2541 0.2250 0.4151 -0.0126 0.0136  0.0125  411 GLY A O   
3051 N N   . TYR A 426 ? 0.3281 0.3022 0.4885 -0.0096 0.0171  0.0124  412 TYR A N   
3052 C CA  . TYR A 426 ? 0.3271 0.3049 0.4962 -0.0098 0.0153  0.0122  412 TYR A CA  
3053 C C   . TYR A 426 ? 0.2959 0.2765 0.4730 -0.0115 0.0162  0.0120  412 TYR A C   
3054 O O   . TYR A 426 ? 0.2401 0.2234 0.4240 -0.0124 0.0131  0.0129  412 TYR A O   
3055 C CB  . TYR A 426 ? 0.2603 0.2389 0.4312 -0.0080 0.0160  0.0106  412 TYR A CB  
3056 C CG  . TYR A 426 ? 0.2951 0.2761 0.4767 -0.0071 0.0150  0.0094  412 TYR A CG  
3057 C CD1 . TYR A 426 ? 0.2560 0.2369 0.4431 -0.0072 0.0104  0.0116  412 TYR A CD1 
3058 C CD2 . TYR A 426 ? 0.3275 0.3115 0.5142 -0.0058 0.0187  0.0066  412 TYR A CD2 
3059 C CE1 . TYR A 426 ? 0.2788 0.2608 0.4770 -0.0057 0.0088  0.0109  412 TYR A CE1 
3060 C CE2 . TYR A 426 ? 0.2976 0.2840 0.4954 -0.0037 0.0179  0.0049  412 TYR A CE2 
3061 C CZ  . TYR A 426 ? 0.2789 0.2634 0.4829 -0.0034 0.0126  0.0070  412 TYR A CZ  
3062 O OH  . TYR A 426 ? 0.2382 0.2240 0.4545 -0.0006 0.0111  0.0058  412 TYR A OH  
3063 N N   . THR A 427 ? 0.2583 0.2397 0.4350 -0.0122 0.0204  0.0117  413 THR A N   
3064 C CA  . THR A 427 ? 0.3070 0.2943 0.4933 -0.0136 0.0224  0.0120  413 THR A CA  
3065 C C   . THR A 427 ? 0.2941 0.2816 0.4852 -0.0172 0.0188  0.0139  413 THR A C   
3066 O O   . THR A 427 ? 0.2941 0.2876 0.4959 -0.0179 0.0171  0.0143  413 THR A O   
3067 C CB  . THR A 427 ? 0.3358 0.3252 0.5190 -0.0145 0.0280  0.0128  413 THR A CB  
3068 O OG1 . THR A 427 ? 0.3688 0.3595 0.5475 -0.0111 0.0308  0.0101  413 THR A OG1 
3069 C CG2 . THR A 427 ? 0.2353 0.2331 0.4293 -0.0167 0.0308  0.0144  413 THR A CG2 
3070 N N   . LEU A 428 ? 0.3350 0.3156 0.5186 -0.0194 0.0170  0.0145  414 LEU A N   
3071 C CA  . LEU A 428 ? 0.2494 0.2286 0.4362 -0.0233 0.0126  0.0150  414 LEU A CA  
3072 C C   . LEU A 428 ? 0.3065 0.2887 0.4962 -0.0228 0.0074  0.0144  414 LEU A C   
3073 O O   . LEU A 428 ? 0.2900 0.2771 0.4885 -0.0255 0.0042  0.0153  414 LEU A O   
3074 C CB  . LEU A 428 ? 0.3365 0.3053 0.5135 -0.0243 0.0111  0.0142  414 LEU A CB  
3075 C CG  . LEU A 428 ? 0.4101 0.3746 0.5888 -0.0287 0.0059  0.0132  414 LEU A CG  
3076 C CD1 . LEU A 428 ? 0.2545 0.2242 0.4452 -0.0341 0.0065  0.0163  414 LEU A CD1 
3077 C CD2 . LEU A 428 ? 0.3222 0.2742 0.4909 -0.0282 0.0045  0.0111  414 LEU A CD2 
3078 N N   . ALA A 429 ? 0.3092 0.2896 0.4918 -0.0197 0.0063  0.0137  415 ALA A N   
3079 C CA  . ALA A 429 ? 0.2457 0.2298 0.4299 -0.0195 0.0013  0.0147  415 ALA A CA  
3080 C C   . ALA A 429 ? 0.3202 0.3109 0.5166 -0.0183 0.0008  0.0167  415 ALA A C   
3081 O O   . ALA A 429 ? 0.3027 0.2981 0.5057 -0.0194 -0.0039 0.0187  415 ALA A O   
3082 C CB  . ALA A 429 ? 0.2548 0.2367 0.4286 -0.0170 0.0008  0.0147  415 ALA A CB  
3083 N N   . ALA A 430 ? 0.2774 0.2684 0.4770 -0.0155 0.0052  0.0159  416 ALA A N   
3084 C CA  . ALA A 430 ? 0.2590 0.2551 0.4711 -0.0131 0.0050  0.0164  416 ALA A CA  
3085 C C   . ALA A 430 ? 0.3600 0.3634 0.5842 -0.0145 0.0053  0.0169  416 ALA A C   
3086 O O   . ALA A 430 ? 0.2924 0.3015 0.5290 -0.0128 0.0027  0.0183  416 ALA A O   
3087 C CB  . ALA A 430 ? 0.2235 0.2178 0.4351 -0.0096 0.0096  0.0135  416 ALA A CB  
3088 N N   . ALA A 431 ? 0.2567 0.2607 0.4791 -0.0176 0.0082  0.0165  417 ALA A N   
3089 C CA  . ALA A 431 ? 0.2921 0.3048 0.5273 -0.0202 0.0084  0.0180  417 ALA A CA  
3090 C C   . ALA A 431 ? 0.2324 0.2479 0.4728 -0.0231 0.0006  0.0203  417 ALA A C   
3091 O O   . ALA A 431 ? 0.2560 0.2809 0.5110 -0.0230 -0.0014 0.0222  417 ALA A O   
3092 C CB  . ALA A 431 ? 0.2301 0.2416 0.4618 -0.0244 0.0121  0.0185  417 ALA A CB  
3093 N N   . PHE A 432 ? 0.2533 0.2615 0.4816 -0.0253 -0.0040 0.0198  418 PHE A N   
3094 C CA  . PHE A 432 ? 0.2646 0.2756 0.4944 -0.0278 -0.0119 0.0215  418 PHE A CA  
3095 C C   . PHE A 432 ? 0.2944 0.3113 0.5328 -0.0243 -0.0151 0.0247  418 PHE A C   
3096 O O   . PHE A 432 ? 0.2718 0.2963 0.5207 -0.0257 -0.0206 0.0276  418 PHE A O   
3097 C CB  . PHE A 432 ? 0.2403 0.2429 0.4530 -0.0291 -0.0149 0.0193  418 PHE A CB  
3098 C CG  . PHE A 432 ? 0.3079 0.3138 0.5180 -0.0312 -0.0230 0.0206  418 PHE A CG  
3099 C CD1 . PHE A 432 ? 0.2507 0.2613 0.4680 -0.0360 -0.0287 0.0209  418 PHE A CD1 
3100 C CD2 . PHE A 432 ? 0.3027 0.3084 0.5033 -0.0289 -0.0252 0.0220  418 PHE A CD2 
3101 C CE1 . PHE A 432 ? 0.2574 0.2718 0.4710 -0.0381 -0.0369 0.0219  418 PHE A CE1 
3102 C CE2 . PHE A 432 ? 0.2722 0.2824 0.4687 -0.0309 -0.0326 0.0238  418 PHE A CE2 
3103 C CZ  . PHE A 432 ? 0.2686 0.2830 0.4710 -0.0354 -0.0387 0.0233  418 PHE A CZ  
3104 N N   . GLY A 433 ? 0.2407 0.2538 0.4757 -0.0200 -0.0124 0.0247  419 GLY A N   
3105 C CA  . GLY A 433 ? 0.2285 0.2448 0.4731 -0.0166 -0.0157 0.0281  419 GLY A CA  
3106 C C   . GLY A 433 ? 0.2569 0.2804 0.5199 -0.0133 -0.0138 0.0280  419 GLY A C   
3107 O O   . GLY A 433 ? 0.2296 0.2590 0.5052 -0.0118 -0.0189 0.0317  419 GLY A O   
3108 N N   . ALA A 434 ? 0.2653 0.2895 0.5303 -0.0117 -0.0062 0.0240  420 ALA A N   
3109 C CA  . ALA A 434 ? 0.2808 0.3140 0.5629 -0.0078 -0.0029 0.0229  420 ALA A CA  
3110 C C   . ALA A 434 ? 0.2877 0.3326 0.5831 -0.0110 -0.0061 0.0261  420 ALA A C   
3111 O O   . ALA A 434 ? 0.3056 0.3595 0.6183 -0.0075 -0.0081 0.0280  420 ALA A O   
3112 C CB  . ALA A 434 ? 0.2236 0.2569 0.5022 -0.0059 0.0064  0.0182  420 ALA A CB  
3113 N N   . GLN A 435 ? 0.2794 0.3243 0.5682 -0.0177 -0.0071 0.0268  421 GLN A N   
3114 C CA  . GLN A 435 ? 0.2978 0.3535 0.5992 -0.0223 -0.0114 0.0299  421 GLN A CA  
3115 C C   . GLN A 435 ? 0.3375 0.3960 0.6436 -0.0226 -0.0214 0.0338  421 GLN A C   
3116 O O   . GLN A 435 ? 0.4078 0.4785 0.7311 -0.0228 -0.0254 0.0372  421 GLN A O   
3117 C CB  . GLN A 435 ? 0.2717 0.3233 0.5637 -0.0300 -0.0118 0.0293  421 GLN A CB  
3118 C CG  . GLN A 435 ? 0.2451 0.3076 0.5512 -0.0362 -0.0163 0.0323  421 GLN A CG  
3119 C CD  . GLN A 435 ? 0.3039 0.3800 0.6269 -0.0358 -0.0090 0.0339  421 GLN A CD  
3120 O OE1 . GLN A 435 ? 0.2473 0.3231 0.5683 -0.0404 -0.0042 0.0342  421 GLN A OE1 
3121 N NE2 . GLN A 435 ? 0.2276 0.3164 0.5679 -0.0300 -0.0080 0.0353  421 GLN A NE2 
3122 N N   . THR A 436 ? 0.2668 0.3156 0.5578 -0.0226 -0.0256 0.0342  422 THR A N   
3123 C CA  . THR A 436 ? 0.2948 0.3466 0.5882 -0.0226 -0.0348 0.0391  422 THR A CA  
3124 C C   . THR A 436 ? 0.3351 0.3925 0.6463 -0.0159 -0.0356 0.0424  422 THR A C   
3125 O O   . THR A 436 ? 0.3330 0.3994 0.6572 -0.0157 -0.0428 0.0474  422 THR A O   
3126 C CB  . THR A 436 ? 0.2906 0.3323 0.5640 -0.0233 -0.0371 0.0393  422 THR A CB  
3127 O OG1 . THR A 436 ? 0.2970 0.3340 0.5550 -0.0285 -0.0375 0.0357  422 THR A OG1 
3128 C CG2 . THR A 436 ? 0.2425 0.2879 0.5173 -0.0229 -0.0460 0.0459  422 THR A CG2 
3129 N N   . ALA A 437 ? 0.2656 0.3173 0.5779 -0.0102 -0.0289 0.0393  423 ALA A N   
3130 C CA  . ALA A 437 ? 0.3542 0.4088 0.6837 -0.0029 -0.0295 0.0408  423 ALA A CA  
3131 C C   . ALA A 437 ? 0.3636 0.4328 0.7143 -0.0003 -0.0273 0.0404  423 ALA A C   
3132 O O   . ALA A 437 ? 0.2813 0.3577 0.6498 0.0041  -0.0320 0.0442  423 ALA A O   
3133 C CB  . ALA A 437 ? 0.2313 0.2754 0.5558 0.0023  -0.0231 0.0359  423 ALA A CB  
3134 N N   . CYS A 438 ? 0.2903 0.3649 0.6403 -0.0031 -0.0201 0.0366  424 CYS A N   
3135 C CA  . CYS A 438 ? 0.2814 0.3722 0.6518 -0.0007 -0.0159 0.0363  424 CYS A CA  
3136 C C   . CYS A 438 ? 0.2944 0.3938 0.6655 -0.0098 -0.0174 0.0386  424 CYS A C   
3137 O O   . CYS A 438 ? 0.3471 0.4489 0.7150 -0.0129 -0.0099 0.0362  424 CYS A O   
3138 C CB  . CYS A 438 ? 0.3181 0.4091 0.6892 0.0052  -0.0045 0.0298  424 CYS A CB  
3139 S SG  . CYS A 438 ? 0.3824 0.4597 0.7508 0.0147  -0.0038 0.0253  424 CYS A SG  
3140 N N   . PRO A 439 ? 0.2402 0.3442 0.6156 -0.0146 -0.0276 0.0437  425 PRO A N   
3141 C CA  . PRO A 439 ? 0.2750 0.3852 0.6507 -0.0242 -0.0307 0.0453  425 PRO A CA  
3142 C C   . PRO A 439 ? 0.3146 0.4429 0.7115 -0.0250 -0.0255 0.0467  425 PRO A C   
3143 O O   . PRO A 439 ? 0.3311 0.4629 0.7280 -0.0336 -0.0257 0.0476  425 PRO A O   
3144 C CB  . PRO A 439 ? 0.3514 0.4640 0.7283 -0.0276 -0.0438 0.0500  425 PRO A CB  
3145 C CG  . PRO A 439 ? 0.3433 0.4597 0.7329 -0.0189 -0.0463 0.0533  425 PRO A CG  
3146 C CD  . PRO A 439 ? 0.2568 0.3611 0.6376 -0.0118 -0.0375 0.0486  425 PRO A CD  
3147 N N   . ASN A 440 ? 0.2968 0.4370 0.7125 -0.0165 -0.0208 0.0468  426 ASN A N   
3148 C CA  . ASN A 440 ? 0.3616 0.5228 0.7995 -0.0163 -0.0150 0.0486  426 ASN A CA  
3149 C C   . ASN A 440 ? 0.3559 0.5188 0.7905 -0.0125 -0.0009 0.0439  426 ASN A C   
3150 O O   . ASN A 440 ? 0.3473 0.5296 0.8002 -0.0106 0.0061  0.0450  426 ASN A O   
3151 C CB  . ASN A 440 ? 0.2738 0.4508 0.7373 -0.0086 -0.0187 0.0518  426 ASN A CB  
3152 C CG  . ASN A 440 ? 0.4631 0.6416 0.9309 -0.0131 -0.0333 0.0579  426 ASN A CG  
3153 O OD1 . ASN A 440 ? 0.4642 0.6452 0.9290 -0.0237 -0.0397 0.0606  426 ASN A OD1 
3154 N ND2 . ASN A 440 ? 0.4216 0.5981 0.8961 -0.0053 -0.0393 0.0600  426 ASN A ND2 
3155 N N   . ARG A 441 ? 0.3288 0.4736 0.7408 -0.0113 0.0034  0.0390  427 ARG A N   
3156 C CA  . ARG A 441 ? 0.3709 0.5167 0.7767 -0.0081 0.0158  0.0346  427 ARG A CA  
3157 C C   . ARG A 441 ? 0.2755 0.4124 0.6635 -0.0176 0.0180  0.0355  427 ARG A C   
3158 O O   . ARG A 441 ? 0.2362 0.3594 0.6111 -0.0240 0.0103  0.0367  427 ARG A O   
3159 C CB  . ARG A 441 ? 0.2708 0.4038 0.6665 0.0017  0.0191  0.0279  427 ARG A CB  
3160 C CG  . ARG A 441 ? 0.2991 0.4412 0.7146 0.0128  0.0194  0.0259  427 ARG A CG  
3161 C CD  . ARG A 441 ? 0.4133 0.5405 0.8189 0.0217  0.0220  0.0186  427 ARG A CD  
3162 N NE  . ARG A 441 ? 0.4211 0.5498 0.8173 0.0246  0.0336  0.0120  427 ARG A NE  
3163 C CZ  . ARG A 441 ? 0.4691 0.5886 0.8585 0.0327  0.0377  0.0039  427 ARG A CZ  
3164 N NH1 . ARG A 441 ? 0.3609 0.4679 0.7532 0.0388  0.0311  0.0017  427 ARG A NH1 
3165 N NH2 . ARG A 441 ? 0.4101 0.5329 0.7893 0.0344  0.0479  -0.0017 427 ARG A NH2 
3166 N N   . ARG A 442 ? 0.2261 0.3715 0.6142 -0.0182 0.0284  0.0352  428 ARG A N   
3167 C CA  . ARG A 442 ? 0.3738 0.5110 0.7467 -0.0267 0.0308  0.0372  428 ARG A CA  
3168 C C   . ARG A 442 ? 0.3337 0.4519 0.6828 -0.0232 0.0335  0.0319  428 ARG A C   
3169 O O   . ARG A 442 ? 0.2468 0.3662 0.5927 -0.0150 0.0404  0.0270  428 ARG A O   
3170 C CB  . ARG A 442 ? 0.3215 0.4774 0.7046 -0.0297 0.0407  0.0411  428 ARG A CB  
3171 C CG  . ARG A 442 ? 0.2455 0.3938 0.6168 -0.0401 0.0415  0.0457  428 ARG A CG  
3172 C CD  . ARG A 442 ? 0.3377 0.5071 0.7218 -0.0444 0.0506  0.0519  428 ARG A CD  
3173 N NE  . ARG A 442 ? 0.2687 0.4461 0.6465 -0.0366 0.0629  0.0485  428 ARG A NE  
3174 C CZ  . ARG A 442 ? 0.3314 0.5256 0.7132 -0.0395 0.0729  0.0536  428 ARG A CZ  
3175 N NH1 . ARG A 442 ? 0.3738 0.5787 0.7678 -0.0506 0.0721  0.0633  428 ARG A NH1 
3176 N NH2 . ARG A 442 ? 0.2509 0.4519 0.6241 -0.0316 0.0836  0.0490  428 ARG A NH2 
3177 N N   . VAL A 443 ? 0.2422 0.3435 0.5751 -0.0292 0.0280  0.0326  429 VAL A N   
3178 C CA  . VAL A 443 ? 0.2535 0.3372 0.5650 -0.0263 0.0289  0.0284  429 VAL A CA  
3179 C C   . VAL A 443 ? 0.3066 0.3850 0.6063 -0.0321 0.0331  0.0308  429 VAL A C   
3180 O O   . VAL A 443 ? 0.2712 0.3465 0.5715 -0.0403 0.0290  0.0349  429 VAL A O   
3181 C CB  . VAL A 443 ? 0.3274 0.3967 0.6297 -0.0267 0.0193  0.0271  429 VAL A CB  
3182 C CG1 . VAL A 443 ? 0.3212 0.3744 0.6028 -0.0247 0.0205  0.0237  429 VAL A CG1 
3183 C CG2 . VAL A 443 ? 0.2448 0.3188 0.5584 -0.0207 0.0150  0.0261  429 VAL A CG2 
3184 N N   . ILE A 444 ? 0.2633 0.3406 0.5528 -0.0280 0.0409  0.0283  430 ILE A N   
3185 C CA  . ILE A 444 ? 0.2578 0.3303 0.5352 -0.0325 0.0451  0.0314  430 ILE A CA  
3186 C C   . ILE A 444 ? 0.3545 0.4096 0.6123 -0.0293 0.0433  0.0274  430 ILE A C   
3187 O O   . ILE A 444 ? 0.2819 0.3356 0.5347 -0.0223 0.0454  0.0220  430 ILE A O   
3188 C CB  . ILE A 444 ? 0.2745 0.3633 0.5556 -0.0308 0.0558  0.0329  430 ILE A CB  
3189 C CG1 . ILE A 444 ? 0.2582 0.3668 0.5607 -0.0346 0.0581  0.0381  430 ILE A CG1 
3190 C CG2 . ILE A 444 ? 0.2784 0.3613 0.5449 -0.0350 0.0596  0.0370  430 ILE A CG2 
3191 C CD1 . ILE A 444 ? 0.2471 0.3763 0.5588 -0.0280 0.0682  0.0359  430 ILE A CD1 
3192 N N   . VAL A 445 ? 0.2521 0.2941 0.5001 -0.0344 0.0390  0.0298  431 VAL A N   
3193 C CA  . VAL A 445 ? 0.2499 0.2765 0.4811 -0.0318 0.0365  0.0268  431 VAL A CA  
3194 C C   . VAL A 445 ? 0.3185 0.3415 0.5391 -0.0338 0.0410  0.0302  431 VAL A C   
3195 O O   . VAL A 445 ? 0.3506 0.3709 0.5725 -0.0401 0.0401  0.0357  431 VAL A O   
3196 C CB  . VAL A 445 ? 0.3249 0.3393 0.5525 -0.0345 0.0279  0.0261  431 VAL A CB  
3197 C CG1 . VAL A 445 ? 0.3297 0.3324 0.5428 -0.0301 0.0260  0.0225  431 VAL A CG1 
3198 C CG2 . VAL A 445 ? 0.2395 0.2601 0.4794 -0.0348 0.0227  0.0252  431 VAL A CG2 
3199 N N   . LEU A 446 ? 0.2817 0.3043 0.4921 -0.0287 0.0451  0.0274  432 LEU A N   
3200 C CA  . LEU A 446 ? 0.3240 0.3434 0.5225 -0.0297 0.0486  0.0308  432 LEU A CA  
3201 C C   . LEU A 446 ? 0.3985 0.4036 0.5842 -0.0270 0.0440  0.0282  432 LEU A C   
3202 O O   . LEU A 446 ? 0.3352 0.3396 0.5155 -0.0218 0.0441  0.0231  432 LEU A O   
3203 C CB  . LEU A 446 ? 0.2822 0.3141 0.4779 -0.0262 0.0565  0.0294  432 LEU A CB  
3204 C CG  . LEU A 446 ? 0.4042 0.4537 0.6131 -0.0279 0.0626  0.0319  432 LEU A CG  
3205 C CD1 . LEU A 446 ? 0.2690 0.3312 0.4747 -0.0220 0.0703  0.0270  432 LEU A CD1 
3206 C CD2 . LEU A 446 ? 0.3386 0.3909 0.5497 -0.0360 0.0642  0.0418  432 LEU A CD2 
3207 N N   . THR A 447 ? 0.4102 0.4039 0.5919 -0.0303 0.0399  0.0316  433 THR A N   
3208 C CA  . THR A 447 ? 0.2841 0.2658 0.4553 -0.0272 0.0359  0.0294  433 THR A CA  
3209 C C   . THR A 447 ? 0.4085 0.3822 0.5724 -0.0293 0.0358  0.0350  433 THR A C   
3210 O O   . THR A 447 ? 0.3445 0.3165 0.5131 -0.0347 0.0357  0.0405  433 THR A O   
3211 C CB  . THR A 447 ? 0.2882 0.2624 0.4617 -0.0271 0.0296  0.0260  433 THR A CB  
3212 O OG1 . THR A 447 ? 0.2926 0.2583 0.4562 -0.0233 0.0270  0.0239  433 THR A OG1 
3213 C CG2 . THR A 447 ? 0.2626 0.2309 0.4414 -0.0329 0.0261  0.0289  433 THR A CG2 
3214 N N   . GLY A 448 ? 0.3688 0.3380 0.5225 -0.0252 0.0353  0.0343  434 GLY A N   
3215 C CA  . GLY A 448 ? 0.3406 0.3007 0.4881 -0.0259 0.0338  0.0396  434 GLY A CA  
3216 C C   . GLY A 448 ? 0.3848 0.3314 0.5337 -0.0261 0.0282  0.0383  434 GLY A C   
3217 O O   . GLY A 448 ? 0.2762 0.2214 0.4281 -0.0250 0.0253  0.0327  434 GLY A O   
3218 N N   . ASP A 449 ? 0.3039 0.2403 0.4503 -0.0273 0.0263  0.0436  435 ASP A N   
3219 C CA  . ASP A 449 ? 0.2997 0.2215 0.4463 -0.0261 0.0208  0.0410  435 ASP A CA  
3220 C C   . ASP A 449 ? 0.2940 0.2140 0.4344 -0.0186 0.0192  0.0349  435 ASP A C   
3221 O O   . ASP A 449 ? 0.3161 0.2309 0.4567 -0.0167 0.0160  0.0289  435 ASP A O   
3222 C CB  . ASP A 449 ? 0.3143 0.2240 0.4607 -0.0284 0.0187  0.0482  435 ASP A CB  
3223 C CG  . ASP A 449 ? 0.3624 0.2753 0.5020 -0.0259 0.0211  0.0549  435 ASP A CG  
3224 O OD1 . ASP A 449 ? 0.3278 0.2525 0.4624 -0.0229 0.0245  0.0531  435 ASP A OD1 
3225 O OD2 . ASP A 449 ? 0.3960 0.2989 0.5352 -0.0271 0.0189  0.0620  435 ASP A OD2 
3226 N N   . GLY A 450 ? 0.3128 0.2385 0.4474 -0.0147 0.0213  0.0366  436 GLY A N   
3227 C CA  . GLY A 450 ? 0.3160 0.2430 0.4466 -0.0085 0.0201  0.0318  436 GLY A CA  
3228 C C   . GLY A 450 ? 0.3029 0.2372 0.4358 -0.0082 0.0203  0.0258  436 GLY A C   
3229 O O   . GLY A 450 ? 0.3127 0.2450 0.4448 -0.0052 0.0181  0.0214  436 GLY A O   
3230 N N   . ALA A 451 ? 0.2836 0.2269 0.4196 -0.0112 0.0229  0.0258  437 ALA A N   
3231 C CA  . ALA A 451 ? 0.2583 0.2082 0.3976 -0.0108 0.0225  0.0213  437 ALA A CA  
3232 C C   . ALA A 451 ? 0.2775 0.2235 0.4206 -0.0126 0.0195  0.0185  437 ALA A C   
3233 O O   . ALA A 451 ? 0.2741 0.2221 0.4166 -0.0106 0.0176  0.0151  437 ALA A O   
3234 C CB  . ALA A 451 ? 0.2538 0.2126 0.3968 -0.0128 0.0258  0.0215  437 ALA A CB  
3235 N N   . ALA A 452 ? 0.2657 0.2071 0.4129 -0.0169 0.0187  0.0202  438 ALA A N   
3236 C CA  . ALA A 452 ? 0.2960 0.2345 0.4471 -0.0196 0.0149  0.0171  438 ALA A CA  
3237 C C   . ALA A 452 ? 0.3001 0.2300 0.4447 -0.0160 0.0113  0.0127  438 ALA A C   
3238 O O   . ALA A 452 ? 0.3277 0.2580 0.4723 -0.0166 0.0080  0.0086  438 ALA A O   
3239 C CB  . ALA A 452 ? 0.2751 0.2103 0.4329 -0.0259 0.0142  0.0205  438 ALA A CB  
3240 N N   . GLN A 453 ? 0.3027 0.2258 0.4418 -0.0120 0.0118  0.0132  439 GLN A N   
3241 C CA  . GLN A 453 ? 0.2898 0.2059 0.4231 -0.0071 0.0092  0.0081  439 GLN A CA  
3242 C C   . GLN A 453 ? 0.3341 0.2599 0.4640 -0.0036 0.0097  0.0048  439 GLN A C   
3243 O O   . GLN A 453 ? 0.3083 0.2324 0.4339 -0.0013 0.0075  -0.0004 439 GLN A O   
3244 C CB  . GLN A 453 ? 0.3190 0.2279 0.4490 -0.0022 0.0099  0.0101  439 GLN A CB  
3245 C CG  . GLN A 453 ? 0.3246 0.2220 0.4576 -0.0057 0.0085  0.0145  439 GLN A CG  
3246 C CD  . GLN A 453 ? 0.3918 0.2798 0.5219 0.0001  0.0078  0.0162  439 GLN A CD  
3247 O OE1 . GLN A 453 ? 0.3841 0.2783 0.5110 0.0061  0.0096  0.0163  439 GLN A OE1 
3248 N NE2 . GLN A 453 ? 0.3303 0.2033 0.4627 -0.0019 0.0046  0.0181  439 GLN A NE2 
3249 N N   . LEU A 454 ? 0.2812 0.2175 0.4128 -0.0034 0.0124  0.0078  440 LEU A N   
3250 C CA  . LEU A 454 ? 0.3466 0.2920 0.4761 -0.0006 0.0126  0.0065  440 LEU A CA  
3251 C C   . LEU A 454 ? 0.3568 0.3062 0.4874 -0.0033 0.0101  0.0044  440 LEU A C   
3252 O O   . LEU A 454 ? 0.3100 0.2649 0.4367 -0.0011 0.0094  0.0029  440 LEU A O   
3253 C CB  . LEU A 454 ? 0.2742 0.2277 0.4062 -0.0006 0.0150  0.0102  440 LEU A CB  
3254 C CG  . LEU A 454 ? 0.3479 0.3018 0.4770 0.0035  0.0165  0.0121  440 LEU A CG  
3255 C CD1 . LEU A 454 ? 0.2587 0.2057 0.3875 0.0027  0.0173  0.0147  440 LEU A CD1 
3256 C CD2 . LEU A 454 ? 0.3005 0.2639 0.4313 0.0034  0.0172  0.0142  440 LEU A CD2 
3257 N N   . THR A 455 ? 0.3033 0.2513 0.4396 -0.0083 0.0085  0.0050  441 THR A N   
3258 C CA  . THR A 455 ? 0.2747 0.2280 0.4137 -0.0110 0.0054  0.0042  441 THR A CA  
3259 C C   . THR A 455 ? 0.4089 0.3564 0.5503 -0.0154 0.0016  0.0020  441 THR A C   
3260 O O   . THR A 455 ? 0.3573 0.3099 0.5045 -0.0190 -0.0011 0.0028  441 THR A O   
3261 C CB  . THR A 455 ? 0.2920 0.2535 0.4390 -0.0127 0.0066  0.0079  441 THR A CB  
3262 O OG1 . THR A 455 ? 0.2803 0.2404 0.4332 -0.0148 0.0091  0.0097  441 THR A OG1 
3263 C CG2 . THR A 455 ? 0.2688 0.2356 0.4139 -0.0095 0.0086  0.0098  441 THR A CG2 
3264 N N   . ILE A 456 ? 0.3588 0.2952 0.4966 -0.0151 0.0007  -0.0007 442 ILE A N   
3265 C CA  . ILE A 456 ? 0.3328 0.2621 0.4749 -0.0206 -0.0032 -0.0019 442 ILE A CA  
3266 C C   . ILE A 456 ? 0.3563 0.2881 0.4968 -0.0230 -0.0089 -0.0060 442 ILE A C   
3267 O O   . ILE A 456 ? 0.3402 0.2717 0.4878 -0.0290 -0.0128 -0.0055 442 ILE A O   
3268 C CB  . ILE A 456 ? 0.3368 0.2513 0.4753 -0.0195 -0.0041 -0.0041 442 ILE A CB  
3269 C CG1 . ILE A 456 ? 0.3877 0.2943 0.5332 -0.0268 -0.0084 -0.0036 442 ILE A CG1 
3270 C CG2 . ILE A 456 ? 0.3090 0.2177 0.4367 -0.0138 -0.0061 -0.0115 442 ILE A CG2 
3271 C CD1 . ILE A 456 ? 0.3348 0.2488 0.4915 -0.0323 -0.0054 0.0040  442 ILE A CD1 
3272 N N   . GLN A 457 ? 0.3042 0.2399 0.4354 -0.0188 -0.0096 -0.0095 443 GLN A N   
3273 C CA  . GLN A 457 ? 0.3004 0.2383 0.4273 -0.0210 -0.0156 -0.0136 443 GLN A CA  
3274 C C   . GLN A 457 ? 0.3455 0.2944 0.4819 -0.0258 -0.0182 -0.0087 443 GLN A C   
3275 O O   . GLN A 457 ? 0.2994 0.2498 0.4355 -0.0295 -0.0244 -0.0110 443 GLN A O   
3276 C CB  . GLN A 457 ? 0.3051 0.2473 0.4190 -0.0153 -0.0149 -0.0176 443 GLN A CB  
3277 C CG  . GLN A 457 ? 0.3135 0.2671 0.4279 -0.0117 -0.0098 -0.0119 443 GLN A CG  
3278 C CD  . GLN A 457 ? 0.3460 0.2958 0.4585 -0.0064 -0.0043 -0.0118 443 GLN A CD  
3279 O OE1 . GLN A 457 ? 0.3941 0.3433 0.5140 -0.0070 -0.0012 -0.0072 443 GLN A OE1 
3280 N NE2 . GLN A 457 ? 0.2994 0.2477 0.4021 -0.0007 -0.0031 -0.0170 443 GLN A NE2 
3281 N N   . GLU A 458 ? 0.3036 0.2598 0.4489 -0.0254 -0.0141 -0.0025 444 GLU A N   
3282 C CA  . GLU A 458 ? 0.3937 0.3599 0.5496 -0.0287 -0.0166 0.0018  444 GLU A CA  
3283 C C   . GLU A 458 ? 0.3564 0.3218 0.5238 -0.0345 -0.0191 0.0027  444 GLU A C   
3284 O O   . GLU A 458 ? 0.3811 0.3550 0.5577 -0.0376 -0.0230 0.0052  444 GLU A O   
3285 C CB  . GLU A 458 ? 0.3648 0.3380 0.5273 -0.0259 -0.0118 0.0068  444 GLU A CB  
3286 C CG  . GLU A 458 ? 0.3766 0.3591 0.5417 -0.0254 -0.0151 0.0103  444 GLU A CG  
3287 C CD  . GLU A 458 ? 0.3934 0.3773 0.5455 -0.0244 -0.0185 0.0085  444 GLU A CD  
3288 O OE1 . GLU A 458 ? 0.3031 0.2828 0.4443 -0.0212 -0.0156 0.0052  444 GLU A OE1 
3289 O OE2 . GLU A 458 ? 0.4910 0.4813 0.6436 -0.0264 -0.0241 0.0104  444 GLU A OE2 
3290 N N   . LEU A 459 ? 0.3165 0.2726 0.4844 -0.0364 -0.0174 0.0015  445 LEU A N   
3291 C CA  . LEU A 459 ? 0.3057 0.2605 0.4840 -0.0433 -0.0207 0.0026  445 LEU A CA  
3292 C C   . LEU A 459 ? 0.3290 0.2827 0.5049 -0.0473 -0.0296 -0.0016 445 LEU A C   
3293 O O   . LEU A 459 ? 0.3168 0.2768 0.5043 -0.0532 -0.0341 0.0006  445 LEU A O   
3294 C CB  . LEU A 459 ? 0.3443 0.2872 0.5217 -0.0448 -0.0182 0.0026  445 LEU A CB  
3295 C CG  . LEU A 459 ? 0.5655 0.5043 0.7529 -0.0531 -0.0221 0.0044  445 LEU A CG  
3296 C CD1 . LEU A 459 ? 0.2916 0.2458 0.4957 -0.0574 -0.0206 0.0106  445 LEU A CD1 
3297 C CD2 . LEU A 459 ? 0.3707 0.2970 0.5563 -0.0537 -0.0191 0.0062  445 LEU A CD2 
3298 N N   . GLY A 460 ? 0.3111 0.2581 0.4718 -0.0440 -0.0324 -0.0080 446 GLY A N   
3299 C CA  . GLY A 460 ? 0.3171 0.2644 0.4724 -0.0472 -0.0410 -0.0129 446 GLY A CA  
3300 C C   . GLY A 460 ? 0.3704 0.3333 0.5316 -0.0484 -0.0443 -0.0083 446 GLY A C   
3301 O O   . GLY A 460 ? 0.3953 0.3623 0.5612 -0.0539 -0.0521 -0.0088 446 GLY A O   
3302 N N   . SER A 461 ? 0.3508 0.3222 0.5125 -0.0434 -0.0392 -0.0035 447 SER A N   
3303 C CA  . SER A 461 ? 0.2906 0.2756 0.4604 -0.0439 -0.0423 0.0023  447 SER A CA  
3304 C C   . SER A 461 ? 0.3044 0.2962 0.4941 -0.0482 -0.0432 0.0070  447 SER A C   
3305 O O   . SER A 461 ? 0.2890 0.2902 0.4871 -0.0514 -0.0497 0.0098  447 SER A O   
3306 C CB  . SER A 461 ? 0.3239 0.3139 0.4921 -0.0380 -0.0366 0.0067  447 SER A CB  
3307 O OG  . SER A 461 ? 0.4391 0.4255 0.5905 -0.0342 -0.0350 0.0033  447 SER A OG  
3308 N N   . MET A 462 ? 0.3093 0.2980 0.5069 -0.0482 -0.0365 0.0084  448 MET A N   
3309 C CA  . MET A 462 ? 0.2737 0.2703 0.4901 -0.0522 -0.0360 0.0127  448 MET A CA  
3310 C C   . MET A 462 ? 0.3176 0.3143 0.5392 -0.0601 -0.0445 0.0113  448 MET A C   
3311 O O   . MET A 462 ? 0.2972 0.3060 0.5331 -0.0634 -0.0491 0.0150  448 MET A O   
3312 C CB  . MET A 462 ? 0.2996 0.2915 0.5189 -0.0516 -0.0275 0.0138  448 MET A CB  
3313 C CG  . MET A 462 ? 0.2583 0.2534 0.4773 -0.0449 -0.0195 0.0158  448 MET A CG  
3314 S SD  . MET A 462 ? 0.2932 0.2846 0.5141 -0.0451 -0.0106 0.0175  448 MET A SD  
3315 C CE  . MET A 462 ? 0.2861 0.2806 0.5037 -0.0371 -0.0035 0.0178  448 MET A CE  
3316 N N   . LEU A 463 ? 0.3345 0.3174 0.5450 -0.0631 -0.0475 0.0055  449 LEU A N   
3317 C CA  . LEU A 463 ? 0.3458 0.3261 0.5608 -0.0714 -0.0565 0.0031  449 LEU A CA  
3318 C C   . LEU A 463 ? 0.3796 0.3668 0.5904 -0.0729 -0.0662 0.0010  449 LEU A C   
3319 O O   . LEU A 463 ? 0.3899 0.3849 0.6127 -0.0796 -0.0738 0.0029  449 LEU A O   
3320 C CB  . LEU A 463 ? 0.3252 0.2862 0.5284 -0.0732 -0.0578 -0.0036 449 LEU A CB  
3321 C CG  . LEU A 463 ? 0.3810 0.3345 0.5889 -0.0732 -0.0498 -0.0002 449 LEU A CG  
3322 C CD1 . LEU A 463 ? 0.3875 0.3205 0.5811 -0.0716 -0.0505 -0.0070 449 LEU A CD1 
3323 C CD2 . LEU A 463 ? 0.4515 0.4115 0.6793 -0.0819 -0.0509 0.0062  449 LEU A CD2 
3324 N N   . ARG A 464 ? 0.3427 0.3290 0.5370 -0.0669 -0.0661 -0.0019 450 ARG A N   
3325 C CA  . ARG A 464 ? 0.4195 0.4135 0.6075 -0.0681 -0.0751 -0.0029 450 ARG A CA  
3326 C C   . ARG A 464 ? 0.4280 0.4395 0.6345 -0.0694 -0.0780 0.0058  450 ARG A C   
3327 O O   . ARG A 464 ? 0.3736 0.3928 0.5843 -0.0745 -0.0879 0.0065  450 ARG A O   
3328 C CB  . ARG A 464 ? 0.3852 0.3779 0.5534 -0.0611 -0.0726 -0.0055 450 ARG A CB  
3329 C CG  . ARG A 464 ? 0.4335 0.4352 0.5920 -0.0622 -0.0815 -0.0058 450 ARG A CG  
3330 C CD  . ARG A 464 ? 0.4237 0.4302 0.5690 -0.0554 -0.0772 -0.0031 450 ARG A CD  
3331 N NE  . ARG A 464 ? 0.3733 0.3858 0.5321 -0.0516 -0.0703 0.0059  450 ARG A NE  
3332 C CZ  . ARG A 464 ? 0.4397 0.4538 0.5919 -0.0461 -0.0643 0.0091  450 ARG A CZ  
3333 N NH1 . ARG A 464 ? 0.4423 0.4548 0.5749 -0.0432 -0.0632 0.0052  450 ARG A NH1 
3334 N NH2 . ARG A 464 ? 0.3998 0.4176 0.5655 -0.0432 -0.0592 0.0162  450 ARG A NH2 
3335 N N   . ASP A 465 ? 0.3225 0.3402 0.5405 -0.0648 -0.0698 0.0121  451 ASP A N   
3336 C CA  . ASP A 465 ? 0.3648 0.3982 0.6013 -0.0639 -0.0715 0.0199  451 ASP A CA  
3337 C C   . ASP A 465 ? 0.3514 0.3926 0.6105 -0.0684 -0.0705 0.0233  451 ASP A C   
3338 O O   . ASP A 465 ? 0.3773 0.4324 0.6546 -0.0664 -0.0701 0.0295  451 ASP A O   
3339 C CB  . ASP A 465 ? 0.2906 0.3260 0.5275 -0.0557 -0.0638 0.0240  451 ASP A CB  
3340 C CG  . ASP A 465 ? 0.3788 0.4112 0.5971 -0.0522 -0.0657 0.0235  451 ASP A CG  
3341 O OD1 . ASP A 465 ? 0.3525 0.3849 0.5587 -0.0553 -0.0735 0.0207  451 ASP A OD1 
3342 O OD2 . ASP A 465 ? 0.3266 0.3575 0.5423 -0.0465 -0.0595 0.0259  451 ASP A OD2 
3343 N N   . LYS A 466 ? 0.3815 0.4147 0.6407 -0.0743 -0.0701 0.0198  452 LYS A N   
3344 C CA  . LYS A 466 ? 0.4392 0.4810 0.7198 -0.0806 -0.0700 0.0238  452 LYS A CA  
3345 C C   . LYS A 466 ? 0.3760 0.4276 0.6716 -0.0754 -0.0590 0.0293  452 LYS A C   
3346 O O   . LYS A 466 ? 0.3764 0.4436 0.6935 -0.0775 -0.0586 0.0345  452 LYS A O   
3347 C CB  . LYS A 466 ? 0.4134 0.4687 0.7075 -0.0866 -0.0814 0.0267  452 LYS A CB  
3348 C CG  . LYS A 466 ? 0.4812 0.5288 0.7585 -0.0908 -0.0932 0.0206  452 LYS A CG  
3349 C CD  . LYS A 466 ? 0.5125 0.5446 0.7825 -0.0985 -0.0965 0.0140  452 LYS A CD  
3350 C CE  . LYS A 466 ? 0.6638 0.6932 0.9248 -0.1050 -0.1108 0.0082  452 LYS A CE  
3351 N NZ  . LYS A 466 ? 0.6156 0.6650 0.8908 -0.1073 -0.1193 0.0143  452 LYS A NZ  
3352 N N   . GLN A 467 ? 0.3243 0.3676 0.6085 -0.0685 -0.0501 0.0276  453 GLN A N   
3353 C CA  . GLN A 467 ? 0.2675 0.3181 0.5625 -0.0636 -0.0395 0.0309  453 GLN A CA  
3354 C C   . GLN A 467 ? 0.3297 0.3798 0.6313 -0.0691 -0.0341 0.0325  453 GLN A C   
3355 O O   . GLN A 467 ? 0.3447 0.3824 0.6377 -0.0751 -0.0371 0.0302  453 GLN A O   
3356 C CB  . GLN A 467 ? 0.3128 0.3543 0.5931 -0.0554 -0.0328 0.0284  453 GLN A CB  
3357 C CG  . GLN A 467 ? 0.3450 0.3870 0.6191 -0.0504 -0.0374 0.0285  453 GLN A CG  
3358 C CD  . GLN A 467 ? 0.3079 0.3426 0.5710 -0.0433 -0.0306 0.0270  453 GLN A CD  
3359 O OE1 . GLN A 467 ? 0.2873 0.3137 0.5420 -0.0426 -0.0240 0.0245  453 GLN A OE1 
3360 N NE2 . GLN A 467 ? 0.2441 0.2817 0.5077 -0.0385 -0.0329 0.0292  453 GLN A NE2 
3361 N N   . HIS A 468 ? 0.2685 0.3320 0.5853 -0.0668 -0.0260 0.0366  454 HIS A N   
3362 C CA  . HIS A 468 ? 0.2734 0.3403 0.5977 -0.0720 -0.0198 0.0401  454 HIS A CA  
3363 C C   . HIS A 468 ? 0.3473 0.4160 0.6682 -0.0652 -0.0076 0.0403  454 HIS A C   
3364 O O   . HIS A 468 ? 0.2819 0.3665 0.6173 -0.0646 -0.0004 0.0442  454 HIS A O   
3365 C CB  . HIS A 468 ? 0.3668 0.4536 0.7159 -0.0779 -0.0220 0.0458  454 HIS A CB  
3366 C CG  . HIS A 468 ? 0.4769 0.5644 0.8310 -0.0848 -0.0351 0.0456  454 HIS A CG  
3367 N ND1 . HIS A 468 ? 0.5133 0.6206 0.8890 -0.0865 -0.0398 0.0499  454 HIS A ND1 
3368 C CD2 . HIS A 468 ? 0.4549 0.5265 0.7951 -0.0901 -0.0448 0.0413  454 HIS A CD2 
3369 C CE1 . HIS A 468 ? 0.3683 0.4718 0.7425 -0.0934 -0.0524 0.0485  454 HIS A CE1 
3370 N NE2 . HIS A 468 ? 0.4317 0.5134 0.7838 -0.0955 -0.0555 0.0427  454 HIS A NE2 
3371 N N   . PRO A 469 ? 0.3000 0.3535 0.6014 -0.0604 -0.0048 0.0362  455 PRO A N   
3372 C CA  . PRO A 469 ? 0.2459 0.3000 0.5421 -0.0552 0.0057  0.0362  455 PRO A CA  
3373 C C   . PRO A 469 ? 0.3025 0.3542 0.5975 -0.0616 0.0101  0.0403  455 PRO A C   
3374 O O   . PRO A 469 ? 0.3584 0.4027 0.6537 -0.0697 0.0043  0.0422  455 PRO A O   
3375 C CB  . PRO A 469 ? 0.2551 0.2938 0.5318 -0.0493 0.0050  0.0311  455 PRO A CB  
3376 C CG  . PRO A 469 ? 0.2507 0.2770 0.5186 -0.0539 -0.0039 0.0291  455 PRO A CG  
3377 C CD  . PRO A 469 ? 0.2640 0.3003 0.5470 -0.0595 -0.0111 0.0313  455 PRO A CD  
3378 N N   . ILE A 470 ? 0.3207 0.3789 0.6146 -0.0580 0.0199  0.0419  456 ILE A N   
3379 C CA  . ILE A 470 ? 0.3006 0.3566 0.5907 -0.0632 0.0249  0.0469  456 ILE A CA  
3380 C C   . ILE A 470 ? 0.4161 0.4566 0.6856 -0.0582 0.0273  0.0436  456 ILE A C   
3381 O O   . ILE A 470 ? 0.3076 0.3520 0.5713 -0.0509 0.0334  0.0408  456 ILE A O   
3382 C CB  . ILE A 470 ? 0.2991 0.3764 0.6021 -0.0634 0.0345  0.0521  456 ILE A CB  
3383 C CG1 . ILE A 470 ? 0.3259 0.4200 0.6517 -0.0691 0.0316  0.0563  456 ILE A CG1 
3384 C CG2 . ILE A 470 ? 0.2654 0.3402 0.5616 -0.0685 0.0400  0.0585  456 ILE A CG2 
3385 C CD1 . ILE A 470 ? 0.3795 0.4984 0.7210 -0.0639 0.0402  0.0574  456 ILE A CD1 
3386 N N   . ILE A 471 ? 0.2949 0.3176 0.5539 -0.0618 0.0218  0.0434  457 ILE A N   
3387 C CA  . ILE A 471 ? 0.2656 0.2736 0.5064 -0.0569 0.0227  0.0403  457 ILE A CA  
3388 C C   . ILE A 471 ? 0.2741 0.2784 0.5104 -0.0606 0.0270  0.0467  457 ILE A C   
3389 O O   . ILE A 471 ? 0.3890 0.3857 0.6286 -0.0680 0.0231  0.0512  457 ILE A O   
3390 C CB  . ILE A 471 ? 0.2688 0.2601 0.5004 -0.0566 0.0142  0.0352  457 ILE A CB  
3391 C CG1 . ILE A 471 ? 0.2887 0.2851 0.5240 -0.0536 0.0097  0.0305  457 ILE A CG1 
3392 C CG2 . ILE A 471 ? 0.2696 0.2483 0.4844 -0.0510 0.0157  0.0326  457 ILE A CG2 
3393 C CD1 . ILE A 471 ? 0.3381 0.3221 0.5661 -0.0549 0.0010  0.0260  457 ILE A CD1 
3394 N N   . LEU A 472 ? 0.2893 0.2984 0.5178 -0.0557 0.0343  0.0474  458 LEU A N   
3395 C CA  . LEU A 472 ? 0.3534 0.3597 0.5752 -0.0583 0.0383  0.0542  458 LEU A CA  
3396 C C   . LEU A 472 ? 0.4357 0.4266 0.6411 -0.0531 0.0363  0.0510  458 LEU A C   
3397 O O   . LEU A 472 ? 0.2803 0.2735 0.4778 -0.0461 0.0387  0.0459  458 LEU A O   
3398 C CB  . LEU A 472 ? 0.2802 0.3054 0.5043 -0.0570 0.0480  0.0576  458 LEU A CB  
3399 C CG  . LEU A 472 ? 0.2800 0.3236 0.5223 -0.0620 0.0511  0.0619  458 LEU A CG  
3400 C CD1 . LEU A 472 ? 0.3850 0.4445 0.6332 -0.0548 0.0560  0.0556  458 LEU A CD1 
3401 C CD2 . LEU A 472 ? 0.2903 0.3438 0.5352 -0.0686 0.0573  0.0727  458 LEU A CD2 
3402 N N   . VAL A 473 ? 0.3219 0.2970 0.5231 -0.0564 0.0314  0.0540  459 VAL A N   
3403 C CA  . VAL A 473 ? 0.2941 0.2553 0.4817 -0.0512 0.0293  0.0518  459 VAL A CA  
3404 C C   . VAL A 473 ? 0.3625 0.3241 0.5443 -0.0525 0.0335  0.0602  459 VAL A C   
3405 O O   . VAL A 473 ? 0.3446 0.3018 0.5310 -0.0593 0.0324  0.0684  459 VAL A O   
3406 C CB  . VAL A 473 ? 0.3581 0.3008 0.5443 -0.0522 0.0212  0.0486  459 VAL A CB  
3407 C CG1 . VAL A 473 ? 0.3219 0.2524 0.4958 -0.0459 0.0199  0.0468  459 VAL A CG1 
3408 C CG2 . VAL A 473 ? 0.3129 0.2571 0.5028 -0.0510 0.0171  0.0406  459 VAL A CG2 
3409 N N   . LEU A 474 ? 0.2987 0.2657 0.4704 -0.0466 0.0375  0.0588  460 LEU A N   
3410 C CA  . LEU A 474 ? 0.3779 0.3469 0.5417 -0.0472 0.0411  0.0667  460 LEU A CA  
3411 C C   . LEU A 474 ? 0.3955 0.3464 0.5526 -0.0453 0.0354  0.0688  460 LEU A C   
3412 O O   . LEU A 474 ? 0.3924 0.3390 0.5409 -0.0387 0.0338  0.0641  460 LEU A O   
3413 C CB  . LEU A 474 ? 0.4349 0.4166 0.5901 -0.0417 0.0466  0.0631  460 LEU A CB  
3414 C CG  . LEU A 474 ? 0.5122 0.5131 0.6728 -0.0422 0.0537  0.0616  460 LEU A CG  
3415 C CD1 . LEU A 474 ? 0.5033 0.5072 0.6751 -0.0410 0.0522  0.0541  460 LEU A CD1 
3416 C CD2 . LEU A 474 ? 0.3745 0.3843 0.5233 -0.0366 0.0582  0.0579  460 LEU A CD2 
3417 N N   . ASN A 475 ? 0.3383 0.2786 0.5005 -0.0513 0.0320  0.0761  461 ASN A N   
3418 C CA  . ASN A 475 ? 0.3386 0.2595 0.4969 -0.0492 0.0259  0.0778  461 ASN A CA  
3419 C C   . ASN A 475 ? 0.4059 0.3282 0.5564 -0.0488 0.0280  0.0879  461 ASN A C   
3420 O O   . ASN A 475 ? 0.3971 0.3178 0.5510 -0.0554 0.0282  0.0992  461 ASN A O   
3421 C CB  . ASN A 475 ? 0.3563 0.2625 0.5243 -0.0557 0.0200  0.0800  461 ASN A CB  
3422 C CG  . ASN A 475 ? 0.4992 0.3834 0.6638 -0.0520 0.0133  0.0797  461 ASN A CG  
3423 O OD1 . ASN A 475 ? 0.4601 0.3417 0.6160 -0.0444 0.0134  0.0786  461 ASN A OD1 
3424 N ND2 . ASN A 475 ? 0.3923 0.2605 0.5646 -0.0573 0.0072  0.0805  461 ASN A ND2 
3425 N N   . ASN A 476 ? 0.3796 0.3053 0.5199 -0.0414 0.0290  0.0845  462 ASN A N   
3426 C CA  . ASN A 476 ? 0.4096 0.3352 0.5413 -0.0400 0.0292  0.0935  462 ASN A CA  
3427 C C   . ASN A 476 ? 0.4229 0.3322 0.5519 -0.0336 0.0228  0.0925  462 ASN A C   
3428 O O   . ASN A 476 ? 0.3643 0.2745 0.4860 -0.0304 0.0220  0.0984  462 ASN A O   
3429 C CB  . ASN A 476 ? 0.3940 0.3375 0.5160 -0.0369 0.0346  0.0913  462 ASN A CB  
3430 C CG  . ASN A 476 ? 0.3938 0.3422 0.5155 -0.0316 0.0353  0.0782  462 ASN A CG  
3431 O OD1 . ASN A 476 ? 0.3517 0.2901 0.4757 -0.0275 0.0309  0.0717  462 ASN A OD1 
3432 N ND2 . ASN A 476 ? 0.4095 0.3735 0.5281 -0.0313 0.0407  0.0744  462 ASN A ND2 
3433 N N   . GLU A 477 ? 0.3575 0.2531 0.4922 -0.0314 0.0183  0.0851  463 GLU A N   
3434 C CA  . GLU A 477 ? 0.3646 0.2445 0.4985 -0.0245 0.0127  0.0827  463 GLU A CA  
3435 C C   . GLU A 477 ? 0.4565 0.3442 0.5827 -0.0162 0.0133  0.0794  463 GLU A C   
3436 O O   . GLU A 477 ? 0.4262 0.3097 0.5492 -0.0121 0.0108  0.0854  463 GLU A O   
3437 C CB  . GLU A 477 ? 0.3849 0.2497 0.5218 -0.0271 0.0084  0.0941  463 GLU A CB  
3438 C CG  . GLU A 477 ? 0.5166 0.3721 0.6629 -0.0363 0.0065  0.0976  463 GLU A CG  
3439 C CD  . GLU A 477 ? 0.6720 0.5066 0.8231 -0.0380 0.0001  0.1067  463 GLU A CD  
3440 O OE1 . GLU A 477 ? 0.6413 0.4744 0.7882 -0.0352 -0.0009 0.1162  463 GLU A OE1 
3441 O OE2 . GLU A 477 ? 0.7202 0.5394 0.8796 -0.0424 -0.0046 0.1044  463 GLU A OE2 
3442 N N   . GLY A 478 ? 0.3691 0.2680 0.4934 -0.0139 0.0161  0.0701  464 GLY A N   
3443 C CA  . GLY A 478 ? 0.3436 0.2492 0.4629 -0.0067 0.0159  0.0658  464 GLY A CA  
3444 C C   . GLY A 478 ? 0.4854 0.4077 0.6007 -0.0080 0.0201  0.0623  464 GLY A C   
3445 O O   . GLY A 478 ? 0.3666 0.2951 0.4840 -0.0129 0.0236  0.0607  464 GLY A O   
3446 N N   . TYR A 479 ? 0.3790 0.3083 0.4894 -0.0032 0.0194  0.0606  465 TYR A N   
3447 C CA  . TYR A 479 ? 0.3159 0.2589 0.4223 -0.0037 0.0221  0.0562  465 TYR A CA  
3448 C C   . TYR A 479 ? 0.3791 0.3302 0.4773 -0.0058 0.0235  0.0627  465 TYR A C   
3449 O O   . TYR A 479 ? 0.3456 0.3011 0.4383 -0.0028 0.0211  0.0646  465 TYR A O   
3450 C CB  . TYR A 479 ? 0.3503 0.2967 0.4569 0.0017  0.0197  0.0507  465 TYR A CB  
3451 C CG  . TYR A 479 ? 0.3535 0.2940 0.4661 0.0049  0.0183  0.0449  465 TYR A CG  
3452 C CD1 . TYR A 479 ? 0.3049 0.2445 0.4215 0.0022  0.0199  0.0396  465 TYR A CD1 
3453 C CD2 . TYR A 479 ? 0.3238 0.2616 0.4379 0.0111  0.0155  0.0447  465 TYR A CD2 
3454 C CE1 . TYR A 479 ? 0.2830 0.2186 0.4030 0.0051  0.0185  0.0342  465 TYR A CE1 
3455 C CE2 . TYR A 479 ? 0.2914 0.2260 0.4094 0.0146  0.0150  0.0388  465 TYR A CE2 
3456 C CZ  . TYR A 479 ? 0.2861 0.2195 0.4060 0.0112  0.0165  0.0336  465 TYR A CZ  
3457 O OH  . TYR A 479 ? 0.3162 0.2475 0.4380 0.0144  0.0158  0.0278  465 TYR A OH  
3458 N N   . THR A 480 ? 0.3181 0.2731 0.4152 -0.0111 0.0276  0.0660  466 THR A N   
3459 C CA  . THR A 480 ? 0.4231 0.3870 0.5107 -0.0132 0.0294  0.0729  466 THR A CA  
3460 C C   . THR A 480 ? 0.3664 0.3423 0.4463 -0.0114 0.0305  0.0662  466 THR A C   
3461 O O   . THR A 480 ? 0.4598 0.4422 0.5296 -0.0112 0.0296  0.0703  466 THR A O   
3462 C CB  . THR A 480 ? 0.3336 0.3012 0.4221 -0.0194 0.0343  0.0791  466 THR A CB  
3463 O OG1 . THR A 480 ? 0.4846 0.4639 0.5730 -0.0208 0.0397  0.0721  466 THR A OG1 
3464 C CG2 . THR A 480 ? 0.3619 0.3170 0.4609 -0.0221 0.0327  0.0821  466 THR A CG2 
3465 N N   . VAL A 481 ? 0.3351 0.3137 0.4192 -0.0104 0.0319  0.0561  467 VAL A N   
3466 C CA  . VAL A 481 ? 0.3078 0.2948 0.3857 -0.0087 0.0315  0.0491  467 VAL A CA  
3467 C C   . VAL A 481 ? 0.3101 0.2961 0.3847 -0.0054 0.0255  0.0503  467 VAL A C   
3468 O O   . VAL A 481 ? 0.4056 0.3988 0.4709 -0.0052 0.0238  0.0504  467 VAL A O   
3469 C CB  . VAL A 481 ? 0.3422 0.3298 0.4275 -0.0081 0.0329  0.0391  467 VAL A CB  
3470 C CG1 . VAL A 481 ? 0.4555 0.4462 0.5381 -0.0058 0.0294  0.0323  467 VAL A CG1 
3471 C CG2 . VAL A 481 ? 0.5077 0.5022 0.5932 -0.0103 0.0390  0.0366  467 VAL A CG2 
3472 N N   . LEU A 482 ? 0.3632 0.3414 0.4455 -0.0027 0.0223  0.0511  468 LEU A N   
3473 C CA  . LEU A 482 ? 0.3547 0.3337 0.4362 0.0009  0.0169  0.0534  468 LEU A CA  
3474 C C   . LEU A 482 ? 0.4270 0.4063 0.5018 0.0012  0.0148  0.0635  468 LEU A C   
3475 O O   . LEU A 482 ? 0.3998 0.3853 0.4694 0.0027  0.0106  0.0657  468 LEU A O   
3476 C CB  . LEU A 482 ? 0.2975 0.2694 0.3888 0.0046  0.0151  0.0521  468 LEU A CB  
3477 C CG  . LEU A 482 ? 0.3195 0.2921 0.4173 0.0045  0.0163  0.0437  468 LEU A CG  
3478 C CD1 . LEU A 482 ? 0.3390 0.3078 0.4439 0.0089  0.0145  0.0430  468 LEU A CD1 
3479 C CD2 . LEU A 482 ? 0.3741 0.3555 0.4695 0.0033  0.0150  0.0387  468 LEU A CD2 
3480 N N   . ARG A 483 ? 0.4054 0.3783 0.4804 -0.0009 0.0170  0.0704  469 ARG A N   
3481 C CA  . ARG A 483 ? 0.4033 0.3760 0.4722 -0.0014 0.0148  0.0819  469 ARG A CA  
3482 C C   . ARG A 483 ? 0.4942 0.4797 0.5497 -0.0041 0.0158  0.0833  469 ARG A C   
3483 O O   . ARG A 483 ? 0.4413 0.4312 0.4897 -0.0029 0.0114  0.0899  469 ARG A O   
3484 C CB  . ARG A 483 ? 0.3846 0.3479 0.4573 -0.0047 0.0171  0.0895  469 ARG A CB  
3485 C CG  . ARG A 483 ? 0.4023 0.3502 0.4862 -0.0018 0.0145  0.0897  469 ARG A CG  
3486 C CD  . ARG A 483 ? 0.3591 0.2976 0.4461 -0.0066 0.0155  0.0986  469 ARG A CD  
3487 N NE  . ARG A 483 ? 0.3582 0.2816 0.4557 -0.0055 0.0140  0.0953  469 ARG A NE  
3488 C CZ  . ARG A 483 ? 0.4676 0.3782 0.5704 0.0001  0.0091  0.0963  469 ARG A CZ  
3489 N NH1 . ARG A 483 ? 0.3706 0.2822 0.4710 0.0055  0.0051  0.1014  469 ARG A NH1 
3490 N NH2 . ARG A 483 ? 0.3657 0.2625 0.4766 0.0006  0.0079  0.0917  469 ARG A NH2 
3491 N N   . ALA A 484 ? 0.4113 0.4035 0.4630 -0.0075 0.0214  0.0772  470 ALA A N   
3492 C CA  . ALA A 484 ? 0.4922 0.4972 0.5301 -0.0092 0.0229  0.0753  470 ALA A CA  
3493 C C   . ALA A 484 ? 0.3524 0.3621 0.3861 -0.0065 0.0172  0.0688  470 ALA A C   
3494 O O   . ALA A 484 ? 0.4582 0.4766 0.4794 -0.0072 0.0146  0.0709  470 ALA A O   
3495 C CB  . ALA A 484 ? 0.4948 0.5056 0.5320 -0.0116 0.0302  0.0676  470 ALA A CB  
3496 N N   . ILE A 485 ? 0.3597 0.3650 0.4036 -0.0043 0.0151  0.0609  471 ILE A N   
3497 C CA  . ILE A 485 ? 0.4101 0.4202 0.4527 -0.0028 0.0093  0.0554  471 ILE A CA  
3498 C C   . ILE A 485 ? 0.5000 0.5115 0.5422 -0.0004 0.0026  0.0643  471 ILE A C   
3499 O O   . ILE A 485 ? 0.4696 0.4894 0.5022 -0.0010 -0.0021 0.0657  471 ILE A O   
3500 C CB  . ILE A 485 ? 0.4018 0.4077 0.4564 -0.0017 0.0090  0.0467  471 ILE A CB  
3501 C CG1 . ILE A 485 ? 0.4081 0.4148 0.4616 -0.0037 0.0139  0.0371  471 ILE A CG1 
3502 C CG2 . ILE A 485 ? 0.4539 0.4645 0.5107 -0.0007 0.0021  0.0441  471 ILE A CG2 
3503 C CD1 . ILE A 485 ? 0.4058 0.4064 0.4722 -0.0031 0.0157  0.0317  471 ILE A CD1 
3504 N N   . HIS A 486 ? 0.4702 0.4739 0.5231 0.0029  0.0015  0.0699  472 HIS A N   
3505 C CA  . HIS A 486 ? 0.5146 0.5199 0.5706 0.0068  -0.0050 0.0773  472 HIS A CA  
3506 C C   . HIS A 486 ? 0.4433 0.4373 0.5091 0.0107  -0.0044 0.0839  472 HIS A C   
3507 O O   . HIS A 486 ? 0.4088 0.3951 0.4832 0.0118  -0.0010 0.0788  472 HIS A O   
3508 C CB  . HIS A 486 ? 0.4415 0.4533 0.5042 0.0085  -0.0095 0.0713  472 HIS A CB  
3509 C CG  . HIS A 486 ? 0.3687 0.3847 0.4370 0.0131  -0.0160 0.0787  472 HIS A CG  
3510 N ND1 . HIS A 486 ? 0.4299 0.4559 0.4908 0.0123  -0.0225 0.0834  472 HIS A ND1 
3511 C CD2 . HIS A 486 ? 0.3922 0.4049 0.4731 0.0190  -0.0171 0.0818  472 HIS A CD2 
3512 C CE1 . HIS A 486 ? 0.3925 0.4215 0.4627 0.0176  -0.0275 0.0900  472 HIS A CE1 
3513 N NE2 . HIS A 486 ? 0.4322 0.4533 0.5148 0.0221  -0.0240 0.0888  472 HIS A NE2 
3514 N N   . GLY A 487 ? 0.4651 0.4577 0.5293 0.0131  -0.0085 0.0949  473 GLY A N   
3515 C CA  . GLY A 487 ? 0.3947 0.3753 0.4685 0.0178  -0.0096 0.1012  473 GLY A CA  
3516 C C   . GLY A 487 ? 0.4551 0.4232 0.5298 0.0147  -0.0048 0.1034  473 GLY A C   
3517 O O   . GLY A 487 ? 0.4527 0.4104 0.5368 0.0169  -0.0029 0.0987  473 GLY A O   
3518 N N   . PRO A 488 ? 0.4354 0.4049 0.5004 0.0093  -0.0032 0.1110  474 PRO A N   
3519 C CA  . PRO A 488 ? 0.4300 0.3893 0.4974 0.0050  0.0013  0.1141  474 PRO A CA  
3520 C C   . PRO A 488 ? 0.4888 0.4309 0.5671 0.0086  -0.0017 0.1194  474 PRO A C   
3521 O O   . PRO A 488 ? 0.4234 0.3549 0.5082 0.0065  0.0012  0.1163  474 PRO A O   
3522 C CB  . PRO A 488 ? 0.4087 0.3760 0.4634 -0.0008 0.0028  0.1242  474 PRO A CB  
3523 C CG  . PRO A 488 ? 0.4400 0.4175 0.4864 0.0018  -0.0029 0.1288  474 PRO A CG  
3524 C CD  . PRO A 488 ? 0.3848 0.3665 0.4364 0.0067  -0.0055 0.1176  474 PRO A CD  
3525 N N   . GLU A 489 ? 0.4675 0.4063 0.5483 0.0142  -0.0078 0.1273  475 GLU A N   
3526 C CA  . GLU A 489 ? 0.5639 0.4848 0.6554 0.0190  -0.0114 0.1320  475 GLU A CA  
3527 C C   . GLU A 489 ? 0.5494 0.4670 0.6513 0.0281  -0.0132 0.1224  475 GLU A C   
3528 O O   . GLU A 489 ? 0.4067 0.3102 0.5175 0.0343  -0.0167 0.1247  475 GLU A O   
3529 C CB  . GLU A 489 ? 0.5171 0.4351 0.6067 0.0202  -0.0174 0.1480  475 GLU A CB  
3530 C CG  . GLU A 489 ? 0.6930 0.6150 0.7720 0.0110  -0.0153 0.1593  475 GLU A CG  
3531 C CD  . GLU A 489 ? 0.8295 0.7451 0.9081 0.0115  -0.0215 0.1771  475 GLU A CD  
3532 O OE1 . GLU A 489 ? 1.1082 1.0070 1.1985 0.0177  -0.0266 0.1806  475 GLU A OE1 
3533 O OE2 . GLU A 489 ? 0.8551 0.7822 0.9215 0.0060  -0.0214 0.1876  475 GLU A OE2 
3534 N N   . GLN A 490 ? 0.4878 0.4180 0.5888 0.0291  -0.0108 0.1119  476 GLN A N   
3535 C CA  . GLN A 490 ? 0.4775 0.4079 0.5880 0.0372  -0.0115 0.1036  476 GLN A CA  
3536 C C   . GLN A 490 ? 0.5223 0.4407 0.6382 0.0374  -0.0079 0.0942  476 GLN A C   
3537 O O   . GLN A 490 ? 0.3956 0.3128 0.5077 0.0304  -0.0038 0.0902  476 GLN A O   
3538 C CB  . GLN A 490 ? 0.3705 0.3193 0.4790 0.0371  -0.0110 0.0973  476 GLN A CB  
3539 C CG  . GLN A 490 ? 0.3627 0.3239 0.4683 0.0389  -0.0165 0.1052  476 GLN A CG  
3540 C CD  . GLN A 490 ? 0.4900 0.4509 0.6067 0.0490  -0.0212 0.1090  476 GLN A CD  
3541 O OE1 . GLN A 490 ? 0.4703 0.4168 0.5928 0.0540  -0.0228 0.1136  476 GLN A OE1 
3542 N NE2 . GLN A 490 ? 0.4138 0.3906 0.5346 0.0521  -0.0238 0.1072  476 GLN A NE2 
3543 N N   . ARG A 491 ? 0.4481 0.3586 0.5728 0.0461  -0.0095 0.0904  477 ARG A N   
3544 C CA  . ARG A 491 ? 0.4512 0.3488 0.5802 0.0475  -0.0072 0.0814  477 ARG A CA  
3545 C C   . ARG A 491 ? 0.4609 0.3684 0.5881 0.0448  -0.0025 0.0704  477 ARG A C   
3546 O O   . ARG A 491 ? 0.4431 0.3418 0.5707 0.0422  -0.0004 0.0639  477 ARG A O   
3547 C CB  . ARG A 491 ? 0.5734 0.4616 0.7113 0.0590  -0.0102 0.0794  477 ARG A CB  
3548 C CG  . ARG A 491 ? 0.6333 0.5136 0.7747 0.0634  -0.0078 0.0669  477 ARG A CG  
3549 C CD  . ARG A 491 ? 0.6672 0.5372 0.8171 0.0759  -0.0108 0.0648  477 ARG A CD  
3550 N NE  . ARG A 491 ? 0.6013 0.4882 0.7558 0.0850  -0.0088 0.0596  477 ARG A NE  
3551 C CZ  . ARG A 491 ? 0.7315 0.6276 0.8853 0.0867  -0.0042 0.0489  477 ARG A CZ  
3552 N NH1 . ARG A 491 ? 0.5330 0.4232 0.6811 0.0802  -0.0015 0.0417  477 ARG A NH1 
3553 N NH2 . ARG A 491 ? 0.7343 0.6472 0.8937 0.0950  -0.0023 0.0462  477 ARG A NH2 
3554 N N   . TYR A 492 ? 0.3404 0.2658 0.4662 0.0447  -0.0015 0.0688  478 TYR A N   
3555 C CA  . TYR A 492 ? 0.3843 0.3181 0.5091 0.0416  0.0024  0.0598  478 TYR A CA  
3556 C C   . TYR A 492 ? 0.4101 0.3430 0.5290 0.0321  0.0051  0.0590  478 TYR A C   
3557 O O   . TYR A 492 ? 0.3101 0.2459 0.4291 0.0294  0.0080  0.0519  478 TYR A O   
3558 C CB  . TYR A 492 ? 0.3507 0.3028 0.4770 0.0432  0.0021  0.0590  478 TYR A CB  
3559 C CG  . TYR A 492 ? 0.4165 0.3777 0.5381 0.0399  -0.0009 0.0661  478 TYR A CG  
3560 C CD1 . TYR A 492 ? 0.3453 0.3092 0.4588 0.0317  0.0005  0.0663  478 TYR A CD1 
3561 C CD2 . TYR A 492 ? 0.3433 0.3119 0.4688 0.0454  -0.0051 0.0720  478 TYR A CD2 
3562 C CE1 . TYR A 492 ? 0.3167 0.2894 0.4240 0.0289  -0.0024 0.0715  478 TYR A CE1 
3563 C CE2 . TYR A 492 ? 0.4147 0.3925 0.5347 0.0420  -0.0087 0.0782  478 TYR A CE2 
3564 C CZ  . TYR A 492 ? 0.3893 0.3687 0.4993 0.0337  -0.0073 0.0775  478 TYR A CZ  
3565 O OH  . TYR A 492 ? 0.3806 0.3693 0.4832 0.0305  -0.0110 0.0824  478 TYR A OH  
3566 N N   . ASN A 493 ? 0.3649 0.2948 0.4790 0.0273  0.0044  0.0665  479 ASN A N   
3567 C CA  . ASN A 493 ? 0.3991 0.3288 0.5088 0.0191  0.0077  0.0662  479 ASN A CA  
3568 C C   . ASN A 493 ? 0.4362 0.3510 0.5492 0.0164  0.0082  0.0665  479 ASN A C   
3569 O O   . ASN A 493 ? 0.4110 0.3266 0.5226 0.0095  0.0110  0.0667  479 ASN A O   
3570 C CB  . ASN A 493 ? 0.4163 0.3533 0.5183 0.0150  0.0074  0.0742  479 ASN A CB  
3571 C CG  . ASN A 493 ? 0.3381 0.2903 0.4356 0.0150  0.0071  0.0712  479 ASN A CG  
3572 O OD1 . ASN A 493 ? 0.3374 0.2949 0.4380 0.0159  0.0081  0.0633  479 ASN A OD1 
3573 N ND2 . ASN A 493 ? 0.3753 0.3345 0.4653 0.0136  0.0051  0.0778  479 ASN A ND2 
3574 N N   . ASP A 494 ? 0.3085 0.3545 0.5341 0.0596  -0.0148 -0.0158 480 ASP A N   
3575 C CA  . ASP A 494 ? 0.3353 0.3479 0.5575 0.0634  -0.0124 -0.0100 480 ASP A CA  
3576 C C   . ASP A 494 ? 0.4447 0.4648 0.6780 0.0506  -0.0032 -0.0165 480 ASP A C   
3577 O O   . ASP A 494 ? 0.3669 0.4195 0.6110 0.0433  0.0002  -0.0271 480 ASP A O   
3578 C CB  . ASP A 494 ? 0.3372 0.3420 0.5589 0.0869  -0.0226 -0.0130 480 ASP A CB  
3579 C CG  . ASP A 494 ? 0.3891 0.3771 0.5933 0.1019  -0.0332 -0.0047 480 ASP A CG  
3580 O OD1 . ASP A 494 ? 0.4615 0.4260 0.6492 0.0930  -0.0306 0.0075  480 ASP A OD1 
3581 O OD2 . ASP A 494 ? 0.4810 0.4786 0.6865 0.1241  -0.0445 -0.0107 480 ASP A OD2 
3582 N N   . ILE A 495 ? 0.3219 0.3117 0.5508 0.0473  0.0005  -0.0102 481 ILE A N   
3583 C CA  . ILE A 495 ? 0.2854 0.2769 0.5212 0.0376  0.0071  -0.0153 481 ILE A CA  
3584 C C   . ILE A 495 ? 0.4138 0.3821 0.6487 0.0471  0.0042  -0.0157 481 ILE A C   
3585 O O   . ILE A 495 ? 0.3703 0.3128 0.5959 0.0569  -0.0011 -0.0090 481 ILE A O   
3586 C CB  . ILE A 495 ? 0.3129 0.2920 0.5434 0.0206  0.0148  -0.0079 481 ILE A CB  
3587 C CG1 . ILE A 495 ? 0.3114 0.2601 0.5335 0.0207  0.0147  0.0042  481 ILE A CG1 
3588 C CG2 . ILE A 495 ? 0.2655 0.2617 0.4927 0.0104  0.0183  -0.0086 481 ILE A CG2 
3589 C CD1 . ILE A 495 ? 0.3249 0.2646 0.5454 0.0076  0.0215  0.0097  481 ILE A CD1 
3590 N N   . ALA A 496 ? 0.3048 0.2794 0.5461 0.0432  0.0078  -0.0237 482 ALA A N   
3591 C CA  . ALA A 496 ? 0.3070 0.2557 0.5451 0.0475  0.0061  -0.0243 482 ALA A CA  
3592 C C   . ALA A 496 ? 0.3100 0.2289 0.5405 0.0372  0.0080  -0.0120 482 ALA A C   
3593 O O   . ALA A 496 ? 0.3410 0.2647 0.5724 0.0242  0.0130  -0.0069 482 ALA A O   
3594 C CB  . ALA A 496 ? 0.3660 0.3277 0.6097 0.0423  0.0103  -0.0349 482 ALA A CB  
3595 N N   . LEU A 497 ? 0.3788 0.2668 0.6008 0.0429  0.0041  -0.0079 483 LEU A N   
3596 C CA  . LEU A 497 ? 0.3666 0.2293 0.5820 0.0315  0.0067  0.0029  483 LEU A CA  
3597 C C   . LEU A 497 ? 0.4135 0.2696 0.6335 0.0210  0.0089  -0.0008 483 LEU A C   
3598 O O   . LEU A 497 ? 0.3565 0.1953 0.5723 0.0255  0.0056  -0.0067 483 LEU A O   
3599 C CB  . LEU A 497 ? 0.4450 0.2741 0.6444 0.0395  0.0022  0.0100  483 LEU A CB  
3600 C CG  . LEU A 497 ? 0.4501 0.2842 0.6416 0.0496  -0.0013 0.0154  483 LEU A CG  
3601 C CD1 . LEU A 497 ? 0.4192 0.2132 0.5883 0.0570  -0.0060 0.0243  483 LEU A CD1 
3602 C CD2 . LEU A 497 ? 0.3945 0.2470 0.5903 0.0372  0.0050  0.0215  483 LEU A CD2 
3603 N N   . TRP A 498 ? 0.3331 0.2014 0.5600 0.0081  0.0136  0.0021  484 TRP A N   
3604 C CA  . TRP A 498 ? 0.3696 0.2373 0.6015 -0.0012 0.0141  -0.0018 484 TRP A CA  
3605 C C   . TRP A 498 ? 0.3804 0.2294 0.6116 -0.0116 0.0150  0.0044  484 TRP A C   
3606 O O   . TRP A 498 ? 0.3881 0.2268 0.6147 -0.0138 0.0175  0.0131  484 TRP A O   
3607 C CB  . TRP A 498 ? 0.3347 0.2250 0.5725 -0.0075 0.0171  -0.0026 484 TRP A CB  
3608 C CG  . TRP A 498 ? 0.4010 0.3087 0.6375 -0.0031 0.0177  -0.0105 484 TRP A CG  
3609 C CD1 . TRP A 498 ? 0.3725 0.2857 0.6081 0.0068  0.0161  -0.0178 484 TRP A CD1 
3610 C CD2 . TRP A 498 ? 0.3179 0.2400 0.5525 -0.0091 0.0204  -0.0123 484 TRP A CD2 
3611 N NE1 . TRP A 498 ? 0.3170 0.2516 0.5527 0.0049  0.0192  -0.0248 484 TRP A NE1 
3612 C CE2 . TRP A 498 ? 0.3589 0.2956 0.5914 -0.0058 0.0220  -0.0208 484 TRP A CE2 
3613 C CE3 . TRP A 498 ? 0.3290 0.2522 0.5620 -0.0162 0.0216  -0.0079 484 TRP A CE3 
3614 C CZ2 . TRP A 498 ? 0.3262 0.2750 0.5521 -0.0128 0.0258  -0.0241 484 TRP A CZ2 
3615 C CZ3 . TRP A 498 ? 0.3724 0.3031 0.5966 -0.0200 0.0238  -0.0105 484 TRP A CZ3 
3616 C CH2 . TRP A 498 ? 0.3446 0.2863 0.5638 -0.0200 0.0264  -0.0181 484 TRP A CH2 
3617 N N   . ASN A 499 ? 0.3999 0.2459 0.6350 -0.0193 0.0133  -0.0008 485 ASN A N   
3618 C CA  . ASN A 499 ? 0.4364 0.2717 0.6743 -0.0329 0.0144  0.0027  485 ASN A CA  
3619 C C   . ASN A 499 ? 0.3875 0.2494 0.6393 -0.0406 0.0160  0.0034  485 ASN A C   
3620 O O   . ASN A 499 ? 0.3597 0.2303 0.6171 -0.0452 0.0123  -0.0029 485 ASN A O   
3621 C CB  . ASN A 499 ? 0.4015 0.2155 0.6334 -0.0367 0.0101  -0.0050 485 ASN A CB  
3622 C CG  . ASN A 499 ? 0.5018 0.2985 0.7326 -0.0530 0.0119  -0.0015 485 ASN A CG  
3623 O OD1 . ASN A 499 ? 0.4943 0.2956 0.7287 -0.0607 0.0172  0.0070  485 ASN A OD1 
3624 N ND2 . ASN A 499 ? 0.4718 0.2488 0.6965 -0.0597 0.0081  -0.0089 485 ASN A ND2 
3625 N N   . TRP A 500 ? 0.3754 0.2489 0.6310 -0.0408 0.0210  0.0108  486 TRP A N   
3626 C CA  . TRP A 500 ? 0.3867 0.2846 0.6521 -0.0414 0.0220  0.0111  486 TRP A CA  
3627 C C   . TRP A 500 ? 0.4147 0.3247 0.6932 -0.0511 0.0199  0.0080  486 TRP A C   
3628 O O   . TRP A 500 ? 0.3808 0.3065 0.6644 -0.0488 0.0156  0.0039  486 TRP A O   
3629 C CB  . TRP A 500 ? 0.3523 0.2566 0.6171 -0.0392 0.0282  0.0186  486 TRP A CB  
3630 C CG  . TRP A 500 ? 0.3440 0.2436 0.5976 -0.0301 0.0288  0.0201  486 TRP A CG  
3631 C CD1 . TRP A 500 ? 0.3542 0.2396 0.5982 -0.0263 0.0295  0.0237  486 TRP A CD1 
3632 C CD2 . TRP A 500 ? 0.3392 0.2489 0.5888 -0.0245 0.0280  0.0172  486 TRP A CD2 
3633 N NE1 . TRP A 500 ? 0.3868 0.2788 0.6250 -0.0183 0.0286  0.0222  486 TRP A NE1 
3634 C CE2 . TRP A 500 ? 0.4419 0.3482 0.6831 -0.0189 0.0287  0.0182  486 TRP A CE2 
3635 C CE3 . TRP A 500 ? 0.3488 0.2683 0.5985 -0.0242 0.0266  0.0141  486 TRP A CE3 
3636 C CZ2 . TRP A 500 ? 0.3501 0.2658 0.5856 -0.0160 0.0291  0.0150  486 TRP A CZ2 
3637 C CZ3 . TRP A 500 ? 0.2895 0.2114 0.5290 -0.0213 0.0275  0.0124  486 TRP A CZ3 
3638 C CH2 . TRP A 500 ? 0.4012 0.3229 0.6350 -0.0187 0.0293  0.0124  486 TRP A CH2 
3639 N N   . THR A 501 ? 0.3084 0.2117 0.5913 -0.0628 0.0226  0.0095  487 THR A N   
3640 C CA  . THR A 501 ? 0.3808 0.3026 0.6797 -0.0742 0.0209  0.0053  487 THR A CA  
3641 C C   . THR A 501 ? 0.4046 0.3250 0.7034 -0.0766 0.0120  -0.0040 487 THR A C   
3642 O O   . THR A 501 ? 0.3992 0.3396 0.7120 -0.0848 0.0081  -0.0092 487 THR A O   
3643 C CB  . THR A 501 ? 0.4083 0.3228 0.7100 -0.0904 0.0275  0.0085  487 THR A CB  
3644 O OG1 . THR A 501 ? 0.4765 0.3546 0.7610 -0.0950 0.0263  0.0082  487 THR A OG1 
3645 C CG2 . THR A 501 ? 0.3232 0.2411 0.6234 -0.0889 0.0370  0.0174  487 THR A CG2 
3646 N N   . GLN A 502 ? 0.3525 0.2521 0.6364 -0.0696 0.0087  -0.0073 488 GLN A N   
3647 C CA  . GLN A 502 ? 0.3441 0.2401 0.6242 -0.0712 0.0010  -0.0169 488 GLN A CA  
3648 C C   . GLN A 502 ? 0.3471 0.2551 0.6223 -0.0602 -0.0032 -0.0200 488 GLN A C   
3649 O O   . GLN A 502 ? 0.4312 0.3373 0.7004 -0.0609 -0.0093 -0.0280 488 GLN A O   
3650 C CB  . GLN A 502 ? 0.3790 0.2418 0.6437 -0.0710 0.0007  -0.0205 488 GLN A CB  
3651 C CG  . GLN A 502 ? 0.4283 0.2702 0.6911 -0.0859 0.0030  -0.0194 488 GLN A CG  
3652 C CD  . GLN A 502 ? 0.7521 0.6046 1.0246 -0.1024 -0.0017 -0.0271 488 GLN A CD  
3653 O OE1 . GLN A 502 ? 0.7933 0.6530 1.0759 -0.1186 0.0017  -0.0251 488 GLN A OE1 
3654 N NE2 . GLN A 502 ? 0.6960 0.5519 0.9652 -0.0995 -0.0093 -0.0367 488 GLN A NE2 
3655 N N   . ILE A 503 ? 0.2983 0.2159 0.5725 -0.0514 0.0003  -0.0140 489 ILE A N   
3656 C CA  . ILE A 503 ? 0.3848 0.3077 0.6487 -0.0433 -0.0022 -0.0160 489 ILE A CA  
3657 C C   . ILE A 503 ? 0.3732 0.3114 0.6400 -0.0439 -0.0099 -0.0188 489 ILE A C   
3658 O O   . ILE A 503 ? 0.3149 0.2501 0.5689 -0.0419 -0.0148 -0.0240 489 ILE A O   
3659 C CB  . ILE A 503 ? 0.4002 0.3249 0.6590 -0.0360 0.0038  -0.0093 489 ILE A CB  
3660 C CG1 . ILE A 503 ? 0.4093 0.3214 0.6626 -0.0330 0.0085  -0.0088 489 ILE A CG1 
3661 C CG2 . ILE A 503 ? 0.3748 0.3023 0.6200 -0.0312 0.0019  -0.0104 489 ILE A CG2 
3662 C CD1 . ILE A 503 ? 0.3954 0.3105 0.6458 -0.0284 0.0141  -0.0026 489 ILE A CD1 
3663 N N   . PRO A 504 ? 0.4067 0.3630 0.6891 -0.0457 -0.0114 -0.0163 490 PRO A N   
3664 C CA  . PRO A 504 ? 0.3810 0.3542 0.6662 -0.0431 -0.0212 -0.0200 490 PRO A CA  
3665 C C   . PRO A 504 ? 0.3055 0.2777 0.5885 -0.0505 -0.0296 -0.0291 490 PRO A C   
3666 O O   . PRO A 504 ? 0.4123 0.3867 0.6834 -0.0457 -0.0381 -0.0325 490 PRO A O   
3667 C CB  . PRO A 504 ? 0.3061 0.3039 0.6142 -0.0445 -0.0201 -0.0178 490 PRO A CB  
3668 C CG  . PRO A 504 ? 0.4059 0.3957 0.7135 -0.0422 -0.0089 -0.0102 490 PRO A CG  
3669 C CD  . PRO A 504 ? 0.3517 0.3166 0.6478 -0.0473 -0.0043 -0.0100 490 PRO A CD  
3670 N N   . GLN A 505 ? 0.3841 0.3486 0.6738 -0.0623 -0.0277 -0.0333 491 GLN A N   
3671 C CA  . GLN A 505 ? 0.4918 0.4529 0.7775 -0.0705 -0.0359 -0.0433 491 GLN A CA  
3672 C C   . GLN A 505 ? 0.4274 0.3663 0.6895 -0.0656 -0.0362 -0.0478 491 GLN A C   
3673 O O   . GLN A 505 ? 0.4855 0.4209 0.7390 -0.0699 -0.0435 -0.0568 491 GLN A O   
3674 C CB  . GLN A 505 ? 0.5454 0.5006 0.8422 -0.0866 -0.0335 -0.0468 491 GLN A CB  
3675 C CG  . GLN A 505 ? 0.6613 0.5845 0.9468 -0.0875 -0.0248 -0.0443 491 GLN A CG  
3676 C CD  . GLN A 505 ? 0.8402 0.7381 1.1068 -0.0868 -0.0280 -0.0532 491 GLN A CD  
3677 O OE1 . GLN A 505 ? 0.8568 0.7528 1.1213 -0.0964 -0.0349 -0.0626 491 GLN A OE1 
3678 N NE2 . GLN A 505 ? 0.6906 0.5721 0.9437 -0.0749 -0.0230 -0.0515 491 GLN A NE2 
3679 N N   . ALA A 506 ? 0.3681 0.2944 0.6202 -0.0574 -0.0281 -0.0430 492 ALA A N   
3680 C CA  . ALA A 506 ? 0.4103 0.3232 0.6423 -0.0524 -0.0268 -0.0483 492 ALA A CA  
3681 C C   . ALA A 506 ? 0.4108 0.3304 0.6277 -0.0462 -0.0293 -0.0464 492 ALA A C   
3682 O O   . ALA A 506 ? 0.3994 0.3122 0.5978 -0.0457 -0.0307 -0.0528 492 ALA A O   
3683 C CB  . ALA A 506 ? 0.3695 0.2700 0.5990 -0.0469 -0.0173 -0.0459 492 ALA A CB  
3684 N N   . LEU A 507 ? 0.3507 0.2805 0.5720 -0.0416 -0.0293 -0.0379 493 LEU A N   
3685 C CA  . LEU A 507 ? 0.3629 0.2909 0.5644 -0.0355 -0.0312 -0.0344 493 LEU A CA  
3686 C C   . LEU A 507 ? 0.3451 0.2826 0.5435 -0.0327 -0.0438 -0.0351 493 LEU A C   
3687 O O   . LEU A 507 ? 0.4121 0.3441 0.5916 -0.0259 -0.0471 -0.0305 493 LEU A O   
3688 C CB  . LEU A 507 ? 0.3208 0.2480 0.5232 -0.0303 -0.0238 -0.0252 493 LEU A CB  
3689 C CG  . LEU A 507 ? 0.4065 0.3270 0.6081 -0.0314 -0.0127 -0.0242 493 LEU A CG  
3690 C CD1 . LEU A 507 ? 0.3064 0.2239 0.5000 -0.0278 -0.0072 -0.0166 493 LEU A CD1 
3691 C CD2 . LEU A 507 ? 0.3710 0.2847 0.5578 -0.0340 -0.0098 -0.0322 493 LEU A CD2 
3692 N N   . SER A 508 ? 0.3478 0.2984 0.5626 -0.0380 -0.0517 -0.0410 494 SER A N   
3693 C CA  . SER A 508 ? 0.4157 0.3809 0.6299 -0.0348 -0.0658 -0.0436 494 SER A CA  
3694 C C   . SER A 508 ? 0.4222 0.3957 0.6468 -0.0460 -0.0728 -0.0543 494 SER A C   
3695 O O   . SER A 508 ? 0.4357 0.4084 0.6770 -0.0559 -0.0668 -0.0571 494 SER A O   
3696 C CB  . SER A 508 ? 0.3647 0.3512 0.5986 -0.0269 -0.0689 -0.0379 494 SER A CB  
3697 O OG  . SER A 508 ? 0.4494 0.4616 0.6982 -0.0271 -0.0824 -0.0440 494 SER A OG  
3698 N N   . LEU A 509 ? 0.3950 0.3730 0.6062 -0.0451 -0.0858 -0.0602 495 LEU A N   
3699 C CA  . LEU A 509 ? 0.4463 0.4320 0.6646 -0.0570 -0.0940 -0.0718 495 LEU A CA  
3700 C C   . LEU A 509 ? 0.5898 0.6078 0.8413 -0.0632 -0.1006 -0.0746 495 LEU A C   
3701 O O   . LEU A 509 ? 0.6622 0.6859 0.9246 -0.0781 -0.1039 -0.0841 495 LEU A O   
3702 C CB  . LEU A 509 ? 0.4441 0.4253 0.6347 -0.0542 -0.1067 -0.0776 495 LEU A CB  
3703 C CG  . LEU A 509 ? 0.4831 0.4348 0.6401 -0.0539 -0.0994 -0.0794 495 LEU A CG  
3704 C CD1 . LEU A 509 ? 0.4723 0.4203 0.6000 -0.0527 -0.1124 -0.0855 495 LEU A CD1 
3705 C CD2 . LEU A 509 ? 0.4401 0.3775 0.6029 -0.0640 -0.0890 -0.0869 495 LEU A CD2 
3706 N N   . ASP A 510 ? 0.5214 0.5606 0.7884 -0.0529 -0.1019 -0.0675 496 ASP A N   
3707 C CA  . ASP A 510 ? 0.5280 0.6055 0.8295 -0.0574 -0.1066 -0.0709 496 ASP A CA  
3708 C C   . ASP A 510 ? 0.4413 0.5285 0.7553 -0.0449 -0.0988 -0.0609 496 ASP A C   
3709 O O   . ASP A 510 ? 0.4199 0.5263 0.7367 -0.0290 -0.1078 -0.0588 496 ASP A O   
3710 C CB  . ASP A 510 ? 0.5478 0.6544 0.8525 -0.0533 -0.1263 -0.0789 496 ASP A CB  
3711 C CG  . ASP A 510 ? 0.7075 0.8626 1.0524 -0.0587 -0.1311 -0.0846 496 ASP A CG  
3712 O OD1 . ASP A 510 ? 0.5698 0.7315 0.9369 -0.0764 -0.1200 -0.0867 496 ASP A OD1 
3713 O OD2 . ASP A 510 ? 0.7431 0.9303 1.0964 -0.0452 -0.1461 -0.0874 496 ASP A OD2 
3714 N N   . PRO A 511 ? 0.4290 0.5021 0.7490 -0.0506 -0.0829 -0.0551 497 PRO A N   
3715 C CA  . PRO A 511 ? 0.3585 0.4357 0.6849 -0.0387 -0.0747 -0.0458 497 PRO A CA  
3716 C C   . PRO A 511 ? 0.4783 0.5985 0.8372 -0.0366 -0.0777 -0.0485 497 PRO A C   
3717 O O   . PRO A 511 ? 0.4847 0.6292 0.8685 -0.0528 -0.0769 -0.0553 497 PRO A O   
3718 C CB  . PRO A 511 ? 0.4827 0.5366 0.8081 -0.0481 -0.0585 -0.0408 497 PRO A CB  
3719 C CG  . PRO A 511 ? 0.5014 0.5361 0.8179 -0.0623 -0.0588 -0.0473 497 PRO A CG  
3720 C CD  . PRO A 511 ? 0.4048 0.4580 0.7258 -0.0678 -0.0729 -0.0574 497 PRO A CD  
3721 N N   . GLN A 512 ? 0.4743 0.6032 0.8313 -0.0168 -0.0807 -0.0438 498 GLN A N   
3722 C CA  . GLN A 512 ? 0.6237 0.7948 1.0112 -0.0095 -0.0818 -0.0464 498 GLN A CA  
3723 C C   . GLN A 512 ? 0.6441 0.8109 1.0408 -0.0121 -0.0638 -0.0399 498 GLN A C   
3724 O O   . GLN A 512 ? 0.5949 0.7676 0.9929 0.0044  -0.0608 -0.0359 498 GLN A O   
3725 C CB  . GLN A 512 ? 0.7026 0.8802 1.0785 0.0167  -0.0959 -0.0455 498 GLN A CB  
3726 C CG  . GLN A 512 ? 0.5411 0.7681 0.9486 0.0295  -0.1016 -0.0512 498 GLN A CG  
3727 C CD  . GLN A 512 ? 0.8063 1.0498 1.2072 0.0525  -0.1230 -0.0553 498 GLN A CD  
3728 O OE1 . GLN A 512 ? 0.6155 0.8702 1.0183 0.0768  -0.1272 -0.0539 498 GLN A OE1 
3729 N NE2 . GLN A 512 ? 0.8312 1.0764 1.2236 0.0460  -0.1372 -0.0608 498 GLN A NE2 
3730 N N   . ALA A 513 ? 0.5483 0.6985 0.9460 -0.0322 -0.0521 -0.0384 499 ALA A N   
3731 C CA  . ALA A 513 ? 0.4273 0.5622 0.8240 -0.0359 -0.0356 -0.0308 499 ALA A CA  
3732 C C   . ALA A 513 ? 0.3410 0.4899 0.7590 -0.0580 -0.0254 -0.0332 499 ALA A C   
3733 O O   . ALA A 513 ? 0.4069 0.5607 0.8320 -0.0752 -0.0293 -0.0399 499 ALA A O   
3734 C CB  . ALA A 513 ? 0.2777 0.3663 0.6439 -0.0355 -0.0305 -0.0239 499 ALA A CB  
3735 N N   . GLN A 514 ? 0.3858 0.5382 0.8104 -0.0586 -0.0120 -0.0278 500 GLN A N   
3736 C CA  . GLN A 514 ? 0.3545 0.5072 0.7888 -0.0801 0.0009  -0.0267 500 GLN A CA  
3737 C C   . GLN A 514 ? 0.3267 0.4425 0.7393 -0.0776 0.0125  -0.0161 500 GLN A C   
3738 O O   . GLN A 514 ? 0.2721 0.3871 0.6789 -0.0617 0.0159  -0.0114 500 GLN A O   
3739 C CB  . GLN A 514 ? 0.3047 0.5058 0.7703 -0.0857 0.0073  -0.0317 500 GLN A CB  
3740 C CG  . GLN A 514 ? 0.6285 0.8777 1.1203 -0.0822 -0.0052 -0.0431 500 GLN A CG  
3741 C CD  . GLN A 514 ? 0.7099 1.0120 1.2330 -0.0784 0.0014  -0.0483 500 GLN A CD  
3742 O OE1 . GLN A 514 ? 0.6948 1.0086 1.2294 -0.0962 0.0167  -0.0477 500 GLN A OE1 
3743 N NE2 . GLN A 514 ? 0.5758 0.9087 1.1105 -0.0542 -0.0098 -0.0534 500 GLN A NE2 
3744 N N   . CYS A 515 ? 0.3770 0.4618 0.7766 -0.0928 0.0179  -0.0129 501 CYS A N   
3745 C CA  . CYS A 515 ? 0.3792 0.4293 0.7573 -0.0897 0.0264  -0.0035 501 CYS A CA  
3746 C C   . CYS A 515 ? 0.3772 0.4200 0.7556 -0.1079 0.0388  0.0007  501 CYS A C   
3747 O O   . CYS A 515 ? 0.3706 0.4158 0.7562 -0.1275 0.0397  -0.0035 501 CYS A O   
3748 C CB  . CYS A 515 ? 0.3825 0.3956 0.7379 -0.0863 0.0206  -0.0026 501 CYS A CB  
3749 S SG  . CYS A 515 ? 0.5176 0.5341 0.8666 -0.0706 0.0073  -0.0077 501 CYS A SG  
3750 N N   . TRP A 516 ? 0.3558 0.3876 0.7235 -0.1025 0.0482  0.0088  502 TRP A N   
3751 C CA  . TRP A 516 ? 0.3308 0.3480 0.6903 -0.1178 0.0604  0.0150  502 TRP A CA  
3752 C C   . TRP A 516 ? 0.3688 0.3473 0.7005 -0.1086 0.0624  0.0242  502 TRP A C   
3753 O O   . TRP A 516 ? 0.3998 0.3751 0.7246 -0.0909 0.0581  0.0255  502 TRP A O   
3754 C CB  . TRP A 516 ? 0.3331 0.3850 0.7092 -0.1217 0.0720  0.0150  502 TRP A CB  
3755 C CG  . TRP A 516 ? 0.3471 0.4447 0.7541 -0.1323 0.0718  0.0051  502 TRP A CG  
3756 C CD1 . TRP A 516 ? 0.3971 0.5087 0.8155 -0.1580 0.0797  0.0019  502 TRP A CD1 
3757 C CD2 . TRP A 516 ? 0.3930 0.5306 0.8233 -0.1175 0.0628  -0.0035 502 TRP A CD2 
3758 N NE1 . TRP A 516 ? 0.3337 0.4978 0.7852 -0.1605 0.0761  -0.0094 502 TRP A NE1 
3759 C CE2 . TRP A 516 ? 0.3906 0.5708 0.8495 -0.1340 0.0648  -0.0126 502 TRP A CE2 
3760 C CE3 . TRP A 516 ? 0.3548 0.4943 0.7820 -0.0924 0.0529  -0.0043 502 TRP A CE3 
3761 C CZ2 . TRP A 516 ? 0.3096 0.5374 0.7961 -0.1230 0.0556  -0.0229 502 TRP A CZ2 
3762 C CZ3 . TRP A 516 ? 0.3730 0.5523 0.8228 -0.0816 0.0442  -0.0131 502 TRP A CZ3 
3763 C CH2 . TRP A 516 ? 0.2690 0.4938 0.7493 -0.0952 0.0448  -0.0225 502 TRP A CH2 
3764 N N   . ARG A 517 ? 0.3928 0.3414 0.7070 -0.1215 0.0686  0.0304  503 ARG A N   
3765 C CA  . ARG A 517 ? 0.3936 0.3095 0.6816 -0.1137 0.0713  0.0397  503 ARG A CA  
3766 C C   . ARG A 517 ? 0.3760 0.2913 0.6568 -0.1262 0.0849  0.0466  503 ARG A C   
3767 O O   . ARG A 517 ? 0.4646 0.3766 0.7460 -0.1472 0.0916  0.0468  503 ARG A O   
3768 C CB  . ARG A 517 ? 0.5539 0.4268 0.8200 -0.1138 0.0646  0.0415  503 ARG A CB  
3769 C CG  . ARG A 517 ? 0.5381 0.3799 0.7777 -0.1021 0.0643  0.0502  503 ARG A CG  
3770 C CD  . ARG A 517 ? 0.6434 0.4411 0.8603 -0.1018 0.0582  0.0516  503 ARG A CD  
3771 N NE  . ARG A 517 ? 0.5984 0.3972 0.8246 -0.0990 0.0492  0.0420  503 ARG A NE  
3772 C CZ  . ARG A 517 ? 0.5894 0.3737 0.8150 -0.1136 0.0479  0.0373  503 ARG A CZ  
3773 N NH1 . ARG A 517 ? 0.5515 0.3212 0.7634 -0.1327 0.0543  0.0410  503 ARG A NH1 
3774 N NH2 . ARG A 517 ? 0.5978 0.3842 0.8300 -0.1091 0.0393  0.0278  503 ARG A NH2 
3775 N N   . VAL A 518 ? 0.4078 0.3262 0.6803 -0.1152 0.0896  0.0516  504 VAL A N   
3776 C CA  . VAL A 518 ? 0.4068 0.3277 0.6710 -0.1257 0.1036  0.0575  504 VAL A CA  
3777 C C   . VAL A 518 ? 0.5094 0.3954 0.7414 -0.1172 0.1035  0.0674  504 VAL A C   
3778 O O   . VAL A 518 ? 0.4841 0.3643 0.7101 -0.0991 0.0949  0.0673  504 VAL A O   
3779 C CB  . VAL A 518 ? 0.3642 0.3304 0.6514 -0.1210 0.1110  0.0521  504 VAL A CB  
3780 C CG1 . VAL A 518 ? 0.4102 0.4144 0.7302 -0.1273 0.1089  0.0417  504 VAL A CG1 
3781 C CG2 . VAL A 518 ? 0.3409 0.3105 0.6250 -0.0979 0.1049  0.0512  504 VAL A CG2 
3782 N N   . SER A 519 ? 0.4379 0.3005 0.6474 -0.1315 0.1129  0.0757  505 SER A N   
3783 C CA  . SER A 519 ? 0.4846 0.3152 0.6607 -0.1239 0.1129  0.0857  505 SER A CA  
3784 C C   . SER A 519 ? 0.6217 0.4589 0.7856 -0.1338 0.1282  0.0911  505 SER A C   
3785 O O   . SER A 519 ? 0.5886 0.4030 0.7240 -0.1266 0.1281  0.0990  505 SER A O   
3786 C CB  . SER A 519 ? 0.5420 0.3215 0.6883 -0.1279 0.1067  0.0930  505 SER A CB  
3787 O OG  . SER A 519 ? 0.6746 0.4394 0.8115 -0.1528 0.1166  0.0962  505 SER A OG  
3788 N N   . GLU A 520 ? 0.4739 0.3444 0.6589 -0.1493 0.1412  0.0862  506 GLU A N   
3789 C CA  . GLU A 520 ? 0.5637 0.4451 0.7389 -0.1606 0.1582  0.0897  506 GLU A CA  
3790 C C   . GLU A 520 ? 0.5203 0.4558 0.7285 -0.1528 0.1646  0.0790  506 GLU A C   
3791 O O   . GLU A 520 ? 0.4294 0.3957 0.6705 -0.1475 0.1586  0.0693  506 GLU A O   
3792 C CB  . GLU A 520 ? 0.5904 0.4608 0.7562 -0.1907 0.1713  0.0935  506 GLU A CB  
3793 C CG  . GLU A 520 ? 0.7390 0.5583 0.8733 -0.1962 0.1588  0.1003  506 GLU A CG  
3794 C CD  . GLU A 520 ? 0.7616 0.5291 0.8499 -0.1869 0.1544  0.1134  506 GLU A CD  
3795 O OE1 . GLU A 520 ? 0.7430 0.5034 0.8068 -0.1945 0.1653  0.1206  506 GLU A OE1 
3796 O OE2 . GLU A 520 ? 0.8110 0.5467 0.8877 -0.1710 0.1395  0.1160  506 GLU A OE2 
3797 N N   . ALA A 521 ? 0.5004 0.4448 0.6968 -0.1505 0.1761  0.0807  507 ALA A N   
3798 C CA  . ALA A 521 ? 0.5832 0.5739 0.8062 -0.1392 0.1822  0.0702  507 ALA A CA  
3799 C C   . ALA A 521 ? 0.5380 0.5752 0.7974 -0.1530 0.1915  0.0604  507 ALA A C   
3800 O O   . ALA A 521 ? 0.4046 0.4798 0.6960 -0.1395 0.1872  0.0496  507 ALA A O   
3801 C CB  . ALA A 521 ? 0.5642 0.5528 0.7639 -0.1364 0.1946  0.0732  507 ALA A CB  
3802 N N   . GLU A 522 ? 0.4808 0.5154 0.7345 -0.1802 0.2040  0.0639  508 GLU A N   
3803 C CA  . GLU A 522 ? 0.4957 0.5792 0.7857 -0.1971 0.2132  0.0535  508 GLU A CA  
3804 C C   . GLU A 522 ? 0.4749 0.5703 0.7931 -0.1933 0.1970  0.0464  508 GLU A C   
3805 O O   . GLU A 522 ? 0.4219 0.5694 0.7790 -0.1896 0.1966  0.0339  508 GLU A O   
3806 C CB  . GLU A 522 ? 0.5057 0.5774 0.7721 -0.2269 0.2241  0.0592  508 GLU A CB  
3807 C CG  . GLU A 522 ? 0.7672 0.7806 0.9988 -0.2390 0.2126  0.0703  508 GLU A CG  
3808 C CD  . GLU A 522 ? 0.9639 0.9201 1.1450 -0.2370 0.2138  0.0853  508 GLU A CD  
3809 O OE1 . GLU A 522 ? 0.9302 0.8887 1.1033 -0.2246 0.2217  0.0873  508 GLU A OE1 
3810 O OE2 . GLU A 522 ? 0.9953 0.9037 1.1436 -0.2469 0.2062  0.0948  508 GLU A OE2 
3811 N N   . GLN A 523 ? 0.4533 0.5022 0.7520 -0.1929 0.1831  0.0534  509 GLN A N   
3812 C CA  . GLN A 523 ? 0.5701 0.6277 0.8918 -0.1883 0.1676  0.0464  509 GLN A CA  
3813 C C   . GLN A 523 ? 0.3802 0.4658 0.7238 -0.1596 0.1565  0.0386  509 GLN A C   
3814 O O   . GLN A 523 ? 0.4168 0.5373 0.7913 -0.1562 0.1493  0.0285  509 GLN A O   
3815 C CB  . GLN A 523 ? 0.5472 0.5481 0.8412 -0.1885 0.1550  0.0545  509 GLN A CB  
3816 C CG  . GLN A 523 ? 0.6575 0.6119 0.9110 -0.2067 0.1597  0.0652  509 GLN A CG  
3817 C CD  . GLN A 523 ? 0.7331 0.6369 0.9627 -0.2008 0.1442  0.0700  509 GLN A CD  
3818 O OE1 . GLN A 523 ? 0.6596 0.5339 0.8724 -0.1827 0.1378  0.0764  509 GLN A OE1 
3819 N NE2 . GLN A 523 ? 0.6531 0.5486 0.8816 -0.2155 0.1379  0.0662  509 GLN A NE2 
3820 N N   . LEU A 524 ? 0.4714 0.5386 0.7962 -0.1392 0.1539  0.0432  510 LEU A N   
3821 C CA  . LEU A 524 ? 0.4110 0.4964 0.7496 -0.1135 0.1442  0.0367  510 LEU A CA  
3822 C C   . LEU A 524 ? 0.3329 0.4724 0.7025 -0.1080 0.1517  0.0257  510 LEU A C   
3823 O O   . LEU A 524 ? 0.3350 0.5014 0.7290 -0.0958 0.1418  0.0171  510 LEU A O   
3824 C CB  . LEU A 524 ? 0.3917 0.4471 0.7016 -0.0976 0.1427  0.0431  510 LEU A CB  
3825 C CG  . LEU A 524 ? 0.3475 0.4118 0.6627 -0.0731 0.1345  0.0375  510 LEU A CG  
3826 C CD1 . LEU A 524 ? 0.3038 0.3674 0.6312 -0.0654 0.1186  0.0337  510 LEU A CD1 
3827 C CD2 . LEU A 524 ? 0.3499 0.3823 0.6344 -0.0637 0.1336  0.0437  510 LEU A CD2 
3828 N N   . ALA A 525 ? 0.3482 0.5054 0.7167 -0.1166 0.1691  0.0254  511 ALA A N   
3829 C CA  . ALA A 525 ? 0.3796 0.5931 0.7793 -0.1099 0.1776  0.0133  511 ALA A CA  
3830 C C   . ALA A 525 ? 0.4586 0.7149 0.8953 -0.1221 0.1746  0.0038  511 ALA A C   
3831 O O   . ALA A 525 ? 0.3703 0.6705 0.8374 -0.1060 0.1691  -0.0077 511 ALA A O   
3832 C CB  . ALA A 525 ? 0.3629 0.5882 0.7532 -0.1212 0.1992  0.0142  511 ALA A CB  
3833 N N   . ASP A 526 ? 0.4826 0.7251 0.9150 -0.1502 0.1773  0.0081  512 ASP A N   
3834 C CA  . ASP A 526 ? 0.4708 0.7490 0.9350 -0.1659 0.1731  -0.0011 512 ASP A CA  
3835 C C   . ASP A 526 ? 0.4140 0.6907 0.8895 -0.1471 0.1510  -0.0054 512 ASP A C   
3836 O O   . ASP A 526 ? 0.3114 0.6364 0.8211 -0.1421 0.1442  -0.0173 512 ASP A O   
3837 C CB  . ASP A 526 ? 0.5424 0.7871 0.9837 -0.1984 0.1776  0.0066  512 ASP A CB  
3838 C CG  . ASP A 526 ? 0.6299 0.9006 1.0891 -0.2149 0.1689  -0.0014 512 ASP A CG  
3839 O OD1 . ASP A 526 ? 0.6760 1.0034 1.1724 -0.2059 0.1638  -0.0141 512 ASP A OD1 
3840 O OD2 . ASP A 526 ? 0.8325 1.0636 1.2661 -0.2355 0.1658  0.0054  512 ASP A OD2 
3841 N N   . VAL A 527 ? 0.3201 0.5438 0.7669 -0.1365 0.1393  0.0038  513 VAL A N   
3842 C CA  . VAL A 527 ? 0.3141 0.5325 0.7667 -0.1206 0.1197  0.0003  513 VAL A CA  
3843 C C   . VAL A 527 ? 0.4193 0.6637 0.8845 -0.0907 0.1131  -0.0060 513 VAL A C   
3844 O O   . VAL A 527 ? 0.3409 0.6104 0.8259 -0.0796 0.1001  -0.0140 513 VAL A O   
3845 C CB  . VAL A 527 ? 0.3743 0.5326 0.7931 -0.1182 0.1112  0.0107  513 VAL A CB  
3846 C CG1 . VAL A 527 ? 0.3185 0.4705 0.7384 -0.0988 0.0934  0.0075  513 VAL A CG1 
3847 C CG2 . VAL A 527 ? 0.3461 0.4781 0.7540 -0.1449 0.1137  0.0146  513 VAL A CG2 
3848 N N   . LEU A 528 ? 0.3556 0.5918 0.8067 -0.0767 0.1213  -0.0027 514 LEU A N   
3849 C CA  . LEU A 528 ? 0.3124 0.5678 0.7712 -0.0481 0.1162  -0.0091 514 LEU A CA  
3850 C C   . LEU A 528 ? 0.3261 0.6458 0.8241 -0.0443 0.1187  -0.0224 514 LEU A C   
3851 O O   . LEU A 528 ? 0.3770 0.7172 0.8881 -0.0208 0.1068  -0.0297 514 LEU A O   
3852 C CB  . LEU A 528 ? 0.2835 0.5164 0.7177 -0.0371 0.1262  -0.0042 514 LEU A CB  
3853 C CG  . LEU A 528 ? 0.2899 0.4655 0.6875 -0.0348 0.1205  0.0067  514 LEU A CG  
3854 C CD1 . LEU A 528 ? 0.2949 0.4520 0.6685 -0.0293 0.1317  0.0107  514 LEU A CD1 
3855 C CD2 . LEU A 528 ? 0.3277 0.4866 0.7189 -0.0161 0.1034  0.0056  514 LEU A CD2 
3856 N N   . GLU A 529 ? 0.3382 0.6906 0.8542 -0.0675 0.1340  -0.0259 515 GLU A N   
3857 C CA  . GLU A 529 ? 0.2969 0.7192 0.8554 -0.0688 0.1371  -0.0403 515 GLU A CA  
3858 C C   . GLU A 529 ? 0.2712 0.7141 0.8515 -0.0669 0.1180  -0.0472 515 GLU A C   
3859 O O   . GLU A 529 ? 0.2649 0.7527 0.8720 -0.0459 0.1086  -0.0585 515 GLU A O   
3860 C CB  . GLU A 529 ? 0.3621 0.8081 0.9312 -0.1032 0.1574  -0.0414 515 GLU A CB  
3861 C CG  . GLU A 529 ? 0.5668 1.0555 1.1489 -0.1011 0.1769  -0.0484 515 GLU A CG  
3862 C CD  . GLU A 529 ? 0.8947 1.3781 1.4584 -0.1361 0.1938  -0.0418 515 GLU A CD  
3863 O OE1 . GLU A 529 ? 0.8679 1.3441 1.4282 -0.1625 0.1896  -0.0386 515 GLU A OE1 
3864 O OE2 . GLU A 529 ? 0.8567 1.3399 1.4066 -0.1370 0.2110  -0.0397 515 GLU A OE2 
3865 N N   . LYS A 530 ? 0.2729 0.6815 0.8397 -0.0868 0.1112  -0.0407 516 LYS A N   
3866 C CA  . LYS A 530 ? 0.3452 0.7712 0.9297 -0.0898 0.0940  -0.0476 516 LYS A CA  
3867 C C   . LYS A 530 ? 0.3587 0.7732 0.9359 -0.0569 0.0740  -0.0484 516 LYS A C   
3868 O O   . LYS A 530 ? 0.3429 0.7948 0.9435 -0.0475 0.0598  -0.0583 516 LYS A O   
3869 C CB  . LYS A 530 ? 0.2769 0.6599 0.8421 -0.1177 0.0925  -0.0405 516 LYS A CB  
3870 C CG  . LYS A 530 ? 0.4574 0.8718 1.0437 -0.1529 0.1015  -0.0471 516 LYS A CG  
3871 C CD  . LYS A 530 ? 0.3717 0.7294 0.9222 -0.1804 0.1106  -0.0354 516 LYS A CD  
3872 C CE  . LYS A 530 ? 0.5123 0.8909 1.0617 -0.2112 0.1189  -0.0374 516 LYS A CE  
3873 N NZ  . LYS A 530 ? 0.4859 0.8262 1.0143 -0.2358 0.1125  -0.0342 516 LYS A NZ  
3874 N N   . VAL A 531 ? 0.3179 0.6806 0.8608 -0.0402 0.0722  -0.0383 517 VAL A N   
3875 C CA  . VAL A 531 ? 0.2527 0.5921 0.7796 -0.0141 0.0545  -0.0369 517 VAL A CA  
3876 C C   . VAL A 531 ? 0.3377 0.6940 0.8674 0.0177  0.0526  -0.0415 517 VAL A C   
3877 O O   . VAL A 531 ? 0.7016 1.0265 1.2081 0.0398  0.0410  -0.0381 517 VAL A O   
3878 C CB  . VAL A 531 ? 0.5094 0.7829 0.9963 -0.0158 0.0531  -0.0244 517 VAL A CB  
3879 C CG1 . VAL A 531 ? 0.3868 0.6394 0.8679 -0.0436 0.0557  -0.0201 517 VAL A CG1 
3880 C CG2 . VAL A 531 ? 0.3092 0.5573 0.7747 -0.0081 0.0656  -0.0176 517 VAL A CG2 
3881 N N   . ALA A 532 ? 0.2983 0.7026 0.8545 0.0201  0.0642  -0.0498 518 ALA A N   
3882 C CA  . ALA A 532 ? 0.3924 0.8043 0.9455 0.0503  0.0666  -0.0536 518 ALA A CA  
3883 C C   . ALA A 532 ? 0.7603 1.1710 1.3094 0.0827  0.0459  -0.0578 518 ALA A C   
3884 O O   . ALA A 532 ? 0.6023 0.9754 1.1226 0.1063  0.0426  -0.0538 518 ALA A O   
3885 C CB  . ALA A 532 ? 0.4369 0.9124 1.0256 0.0478  0.0816  -0.0651 518 ALA A CB  
3886 N N   . HIS A 533 ? 0.6847 1.1333 1.2591 0.0838  0.0313  -0.0657 519 HIS A N   
3887 C CA  . HIS A 533 ? 0.7571 1.2108 1.3289 0.1168  0.0107  -0.0705 519 HIS A CA  
3888 C C   . HIS A 533 ? 0.6972 1.1031 1.2388 0.1163  -0.0066 -0.0623 519 HIS A C   
3889 O O   . HIS A 533 ? 0.6982 1.1156 1.2415 0.1360  -0.0260 -0.0669 519 HIS A O   
3890 C CB  . HIS A 533 ? 0.5858 1.1191 1.2054 0.1244  0.0037  -0.0865 519 HIS A CB  
3891 C CG  . HIS A 533 ? 0.7427 1.3233 1.3876 0.1398  0.0169  -0.0968 519 HIS A CG  
3892 N ND1 . HIS A 533 ? 0.7780 1.3936 1.4439 0.1133  0.0384  -0.0996 519 HIS A ND1 
3893 C CD2 . HIS A 533 ? 0.7797 1.3625 1.4149 0.1762  0.0127  -0.1003 519 HIS A CD2 
3894 C CE1 . HIS A 533 ? 0.7424 1.3831 1.4123 0.1327  0.0470  -0.1047 519 HIS A CE1 
3895 N NE2 . HIS A 533 ? 0.8546 1.4757 1.5071 0.1712  0.0317  -0.1055 519 HIS A NE2 
3896 N N   . HIS A 534 ? 0.6612 1.0151 1.1746 0.0956  -0.0001 -0.0508 520 HIS A N   
3897 C CA  . HIS A 534 ? 0.6295 0.9338 1.1102 0.0940  -0.0128 -0.0428 520 HIS A CA  
3898 C C   . HIS A 534 ? 0.6986 1.0303 1.1938 0.0970  -0.0321 -0.0497 520 HIS A C   
3899 O O   . HIS A 534 ? 0.6337 0.9448 1.1071 0.1169  -0.0486 -0.0483 520 HIS A O   
3900 C CB  . HIS A 534 ? 0.5187 0.7701 0.9580 0.1170  -0.0167 -0.0355 520 HIS A CB  
3901 C CG  . HIS A 534 ? 0.4636 0.7303 0.9043 0.1513  -0.0256 -0.0417 520 HIS A CG  
3902 N ND1 . HIS A 534 ? 0.7101 0.9985 1.1637 0.1648  -0.0143 -0.0469 520 HIS A ND1 
3903 C CD2 . HIS A 534 ? 0.6064 0.8675 1.0343 0.1766  -0.0450 -0.0437 520 HIS A CD2 
3904 C CE1 . HIS A 534 ? 0.6027 0.8990 1.0532 0.1984  -0.0266 -0.0527 520 HIS A CE1 
3905 N NE2 . HIS A 534 ? 0.7043 0.9829 1.1382 0.2065  -0.0459 -0.0502 520 HIS A NE2 
3906 N N   . GLU A 535 ? 0.6898 1.0668 1.2198 0.0747  -0.0295 -0.0572 521 GLU A N   
3907 C CA  . GLU A 535 ? 0.3867 0.7921 0.9316 0.0726  -0.0475 -0.0649 521 GLU A CA  
3908 C C   . GLU A 535 ? 0.4146 0.7688 0.9260 0.0627  -0.0561 -0.0573 521 GLU A C   
3909 O O   . GLU A 535 ? 0.4441 0.8002 0.9483 0.0728  -0.0748 -0.0605 521 GLU A O   
3910 C CB  . GLU A 535 ? 0.4505 0.9109 1.0371 0.0450  -0.0403 -0.0748 521 GLU A CB  
3911 C CG  . GLU A 535 ? 0.4481 0.8903 1.0326 0.0182  -0.0170 -0.0684 521 GLU A CG  
3912 C CD  . GLU A 535 ? 0.7288 1.2271 1.3531 -0.0073 -0.0055 -0.0781 521 GLU A CD  
3913 O OE1 . GLU A 535 ? 0.6131 1.0944 1.2338 -0.0393 0.0038  -0.0750 521 GLU A OE1 
3914 O OE2 . GLU A 535 ? 0.7029 1.2619 1.3608 0.0046  -0.0058 -0.0893 521 GLU A OE2 
3915 N N   . ARG A 536 ? 0.3592 0.6680 0.8485 0.0451  -0.0430 -0.0478 522 ARG A N   
3916 C CA  . ARG A 536 ? 0.2907 0.5512 0.7484 0.0357  -0.0478 -0.0413 522 ARG A CA  
3917 C C   . ARG A 536 ? 0.2752 0.4867 0.7051 0.0314  -0.0338 -0.0303 522 ARG A C   
3918 O O   . ARG A 536 ? 0.3058 0.5202 0.7416 0.0310  -0.0199 -0.0277 522 ARG A O   
3919 C CB  . ARG A 536 ? 0.4108 0.6869 0.8839 0.0100  -0.0514 -0.0475 522 ARG A CB  
3920 C CG  . ARG A 536 ? 0.7105 1.0120 1.1892 0.0224  -0.0723 -0.0556 522 ARG A CG  
3921 C CD  . ARG A 536 ? 0.7993 1.1358 1.2996 0.0069  -0.0838 -0.0667 522 ARG A CD  
3922 N NE  . ARG A 536 ? 0.9585 1.3615 1.5004 0.0104  -0.0871 -0.0778 522 ARG A NE  
3923 C CZ  . ARG A 536 ? 0.8280 1.2723 1.3856 0.0241  -0.1065 -0.0877 522 ARG A CZ  
3924 N NH1 . ARG A 536 ? 0.9340 1.3583 1.4650 0.0514  -0.1238 -0.0847 522 ARG A NH1 
3925 N NH2 . ARG A 536 ? 0.7568 1.2639 1.3562 0.0095  -0.1089 -0.1011 522 ARG A NH2 
3926 N N   . LEU A 537 ? 0.2804 0.4488 0.6790 0.0292  -0.0380 -0.0248 523 LEU A N   
3927 C CA  . LEU A 537 ? 0.2762 0.4027 0.6501 0.0241  -0.0263 -0.0159 523 LEU A CA  
3928 C C   . LEU A 537 ? 0.3333 0.4646 0.7222 0.0032  -0.0123 -0.0148 523 LEU A C   
3929 O O   . LEU A 537 ? 0.2704 0.4140 0.6736 -0.0141 -0.0133 -0.0191 523 LEU A O   
3930 C CB  . LEU A 537 ? 0.2835 0.3726 0.6273 0.0211  -0.0324 -0.0127 523 LEU A CB  
3931 C CG  . LEU A 537 ? 0.2806 0.3305 0.5990 0.0165  -0.0222 -0.0053 523 LEU A CG  
3932 C CD1 . LEU A 537 ? 0.2963 0.3150 0.5811 0.0247  -0.0291 -0.0024 523 LEU A CD1 
3933 C CD2 . LEU A 537 ? 0.2789 0.3206 0.6018 -0.0027 -0.0151 -0.0051 523 LEU A CD2 
3934 N N   . SER A 538 ? 0.3335 0.4520 0.7158 0.0044  0.0003  -0.0091 524 SER A N   
3935 C CA  . SER A 538 ? 0.2534 0.3723 0.6443 -0.0133 0.0139  -0.0065 524 SER A CA  
3936 C C   . SER A 538 ? 0.2900 0.3678 0.6539 -0.0155 0.0200  0.0015  524 SER A C   
3937 O O   . SER A 538 ? 0.3276 0.3885 0.6738 -0.0029 0.0214  0.0052  524 SER A O   
3938 C CB  . SER A 538 ? 0.2519 0.4007 0.6617 -0.0103 0.0242  -0.0082 524 SER A CB  
3939 O OG  . SER A 538 ? 0.2527 0.4470 0.6910 -0.0065 0.0182  -0.0173 524 SER A OG  
3940 N N   . LEU A 539 ? 0.3589 0.4211 0.7195 -0.0313 0.0232  0.0034  525 LEU A N   
3941 C CA  . LEU A 539 ? 0.2826 0.3115 0.6212 -0.0331 0.0281  0.0098  525 LEU A CA  
3942 C C   . LEU A 539 ? 0.3633 0.3896 0.7058 -0.0462 0.0389  0.0137  525 LEU A C   
3943 O O   . LEU A 539 ? 0.3098 0.3366 0.6599 -0.0608 0.0395  0.0120  525 LEU A O   
3944 C CB  . LEU A 539 ? 0.3817 0.3901 0.7080 -0.0361 0.0205  0.0080  525 LEU A CB  
3945 C CG  . LEU A 539 ? 0.4985 0.4791 0.8026 -0.0324 0.0224  0.0119  525 LEU A CG  
3946 C CD1 . LEU A 539 ? 0.4644 0.4348 0.7565 -0.0292 0.0142  0.0079  525 LEU A CD1 
3947 C CD2 . LEU A 539 ? 0.4515 0.4164 0.7521 -0.0413 0.0280  0.0152  525 LEU A CD2 
3948 N N   . ILE A 540 ? 0.3592 0.3804 0.6936 -0.0419 0.0476  0.0188  526 ILE A N   
3949 C CA  . ILE A 540 ? 0.3068 0.3224 0.6389 -0.0532 0.0584  0.0238  526 ILE A CA  
3950 C C   . ILE A 540 ? 0.3885 0.3715 0.6966 -0.0509 0.0589  0.0301  526 ILE A C   
3951 O O   . ILE A 540 ? 0.3225 0.2988 0.6185 -0.0403 0.0594  0.0320  526 ILE A O   
3952 C CB  . ILE A 540 ? 0.2684 0.3068 0.6094 -0.0503 0.0684  0.0238  526 ILE A CB  
3953 C CG1 . ILE A 540 ? 0.2618 0.3394 0.6298 -0.0481 0.0657  0.0155  526 ILE A CG1 
3954 C CG2 . ILE A 540 ? 0.3040 0.3358 0.6397 -0.0651 0.0805  0.0292  526 ILE A CG2 
3955 C CD1 . ILE A 540 ? 0.2623 0.3680 0.6418 -0.0406 0.0750  0.0128  526 ILE A CD1 
3956 N N   . GLU A 541 ? 0.3290 0.2915 0.6294 -0.0603 0.0581  0.0325  527 GLU A N   
3957 C CA  . GLU A 541 ? 0.3553 0.2899 0.6345 -0.0563 0.0573  0.0377  527 GLU A CA  
3958 C C   . GLU A 541 ? 0.3801 0.3068 0.6486 -0.0615 0.0670  0.0450  527 GLU A C   
3959 O O   . GLU A 541 ? 0.4487 0.3675 0.7157 -0.0747 0.0722  0.0481  527 GLU A O   
3960 C CB  . GLU A 541 ? 0.3836 0.2968 0.6567 -0.0602 0.0510  0.0362  527 GLU A CB  
3961 C CG  . GLU A 541 ? 0.4204 0.3068 0.6729 -0.0546 0.0496  0.0411  527 GLU A CG  
3962 C CD  . GLU A 541 ? 0.4587 0.3219 0.7040 -0.0554 0.0432  0.0384  527 GLU A CD  
3963 O OE1 . GLU A 541 ? 0.4287 0.2923 0.6825 -0.0650 0.0416  0.0340  527 GLU A OE1 
3964 O OE2 . GLU A 541 ? 0.5292 0.3746 0.7600 -0.0457 0.0392  0.0398  527 GLU A OE2 
3965 N N   . VAL A 542 ? 0.3998 0.3272 0.6585 -0.0527 0.0698  0.0476  528 VAL A N   
3966 C CA  . VAL A 542 ? 0.3670 0.2886 0.6130 -0.0564 0.0791  0.0541  528 VAL A CA  
3967 C C   . VAL A 542 ? 0.4040 0.2972 0.6265 -0.0529 0.0750  0.0600  528 VAL A C   
3968 O O   . VAL A 542 ? 0.3874 0.2775 0.6032 -0.0423 0.0685  0.0583  528 VAL A O   
3969 C CB  . VAL A 542 ? 0.3560 0.2941 0.6027 -0.0482 0.0842  0.0522  528 VAL A CB  
3970 C CG1 . VAL A 542 ? 0.3740 0.3086 0.6075 -0.0534 0.0953  0.0577  528 VAL A CG1 
3971 C CG2 . VAL A 542 ? 0.2906 0.2566 0.5602 -0.0457 0.0849  0.0451  528 VAL A CG2 
3972 N N   . MET A 543 ? 0.4063 0.2786 0.6150 -0.0620 0.0786  0.0666  529 MET A N   
3973 C CA  . MET A 543 ? 0.4778 0.3205 0.6618 -0.0562 0.0730  0.0727  529 MET A CA  
3974 C C   . MET A 543 ? 0.4707 0.3098 0.6357 -0.0537 0.0782  0.0787  529 MET A C   
3975 O O   . MET A 543 ? 0.5419 0.3796 0.6996 -0.0645 0.0891  0.0836  529 MET A O   
3976 C CB  . MET A 543 ? 0.4093 0.2220 0.5809 -0.0660 0.0727  0.0775  529 MET A CB  
3977 C CG  . MET A 543 ? 0.5445 0.3615 0.7344 -0.0721 0.0692  0.0705  529 MET A CG  
3978 S SD  . MET A 543 ? 0.7556 0.5676 0.9493 -0.0560 0.0549  0.0630  529 MET A SD  
3979 C CE  . MET A 543 ? 0.8182 0.6090 0.9863 -0.0396 0.0484  0.0687  529 MET A CE  
3980 N N   . LEU A 544 ? 0.4422 0.2814 0.5985 -0.0409 0.0709  0.0776  530 LEU A N   
3981 C CA  . LEU A 544 ? 0.4710 0.3085 0.6085 -0.0376 0.0738  0.0815  530 LEU A CA  
3982 C C   . LEU A 544 ? 0.5727 0.3918 0.6895 -0.0269 0.0627  0.0850  530 LEU A C   
3983 O O   . LEU A 544 ? 0.4642 0.2811 0.5873 -0.0187 0.0526  0.0811  530 LEU A O   
3984 C CB  . LEU A 544 ? 0.3675 0.2293 0.5156 -0.0331 0.0758  0.0744  530 LEU A CB  
3985 C CG  . LEU A 544 ? 0.4008 0.2822 0.5665 -0.0391 0.0862  0.0707  530 LEU A CG  
3986 C CD1 . LEU A 544 ? 0.3306 0.2283 0.5073 -0.0317 0.0838  0.0626  530 LEU A CD1 
3987 C CD2 . LEU A 544 ? 0.4324 0.3139 0.5856 -0.0455 0.0987  0.0751  530 LEU A CD2 
3988 N N   . PRO A 545 ? 0.5239 0.3308 0.6154 -0.0257 0.0639  0.0916  531 PRO A N   
3989 C CA  . PRO A 545 ? 0.4537 0.2446 0.5245 -0.0132 0.0513  0.0948  531 PRO A CA  
3990 C C   . PRO A 545 ? 0.5231 0.3382 0.6064 -0.0021 0.0415  0.0853  531 PRO A C   
3991 O O   . PRO A 545 ? 0.4604 0.2981 0.5562 -0.0053 0.0457  0.0787  531 PRO A O   
3992 C CB  . PRO A 545 ? 0.5580 0.3340 0.5981 -0.0163 0.0561  0.1035  531 PRO A CB  
3993 C CG  . PRO A 545 ? 0.6002 0.3768 0.6435 -0.0329 0.0730  0.1065  531 PRO A CG  
3994 C CD  . PRO A 545 ? 0.5400 0.3465 0.6188 -0.0354 0.0769  0.0964  531 PRO A CD  
3995 N N   . LYS A 546 ? 0.5141 0.3231 0.5916 0.0111  0.0283  0.0844  532 LYS A N   
3996 C CA  . LYS A 546 ? 0.5431 0.3793 0.6348 0.0204  0.0190  0.0740  532 LYS A CA  
3997 C C   . LYS A 546 ? 0.4455 0.2988 0.5291 0.0190  0.0189  0.0713  532 LYS A C   
3998 O O   . LYS A 546 ? 0.4434 0.3221 0.5417 0.0167  0.0185  0.0618  532 LYS A O   
3999 C CB  . LYS A 546 ? 0.6148 0.4430 0.7005 0.0372  0.0049  0.0733  532 LYS A CB  
4000 C CG  . LYS A 546 ? 0.5963 0.4387 0.7057 0.0431  0.0005  0.0634  532 LYS A CG  
4001 C CD  . LYS A 546 ? 0.5538 0.3890 0.6557 0.0635  -0.0138 0.0616  532 LYS A CD  
4002 C CE  . LYS A 546 ? 0.5345 0.3614 0.6489 0.0685  -0.0152 0.0564  532 LYS A CE  
4003 N NZ  . LYS A 546 ? 0.7117 0.5376 0.8224 0.0918  -0.0293 0.0513  532 LYS A NZ  
4004 N N   . ALA A 547 ? 0.4453 0.2825 0.5023 0.0190  0.0195  0.0795  533 ALA A N   
4005 C CA  . ALA A 547 ? 0.5286 0.3792 0.5734 0.0182  0.0178  0.0765  533 ALA A CA  
4006 C C   . ALA A 547 ? 0.5611 0.4107 0.6007 0.0054  0.0324  0.0774  533 ALA A C   
4007 O O   . ALA A 547 ? 0.5958 0.4524 0.6219 0.0035  0.0324  0.0745  533 ALA A O   
4008 C CB  . ALA A 547 ? 0.4829 0.3178 0.4977 0.0287  0.0071  0.0837  533 ALA A CB  
4009 N N   . ASP A 548 ? 0.5332 0.3763 0.5837 -0.0028 0.0445  0.0801  534 ASP A N   
4010 C CA  . ASP A 548 ? 0.5313 0.3753 0.5774 -0.0120 0.0587  0.0803  534 ASP A CA  
4011 C C   . ASP A 548 ? 0.4870 0.3501 0.5467 -0.0140 0.0611  0.0697  534 ASP A C   
4012 O O   . ASP A 548 ? 0.4363 0.3101 0.5179 -0.0136 0.0590  0.0640  534 ASP A O   
4013 C CB  . ASP A 548 ? 0.6151 0.4520 0.6714 -0.0198 0.0700  0.0851  534 ASP A CB  
4014 C CG  . ASP A 548 ? 0.5712 0.4086 0.6182 -0.0278 0.0851  0.0869  534 ASP A CG  
4015 O OD1 . ASP A 548 ? 0.6685 0.5079 0.6987 -0.0265 0.0868  0.0845  534 ASP A OD1 
4016 O OD2 . ASP A 548 ? 0.6957 0.5333 0.7523 -0.0358 0.0955  0.0896  534 ASP A OD2 
4017 N N   . ILE A 549 ? 0.4794 0.3428 0.5227 -0.0166 0.0664  0.0672  535 ILE A N   
4018 C CA  . ILE A 549 ? 0.5343 0.4077 0.5805 -0.0185 0.0670  0.0571  535 ILE A CA  
4019 C C   . ILE A 549 ? 0.4712 0.3403 0.5107 -0.0215 0.0808  0.0551  535 ILE A C   
4020 O O   . ILE A 549 ? 0.5594 0.4208 0.5810 -0.0229 0.0880  0.0599  535 ILE A O   
4021 C CB  . ILE A 549 ? 0.5092 0.3876 0.5390 -0.0178 0.0565  0.0526  535 ILE A CB  
4022 C CG1 . ILE A 549 ? 0.6254 0.5175 0.6705 -0.0135 0.0434  0.0498  535 ILE A CG1 
4023 C CG2 . ILE A 549 ? 0.7173 0.5972 0.7382 -0.0235 0.0602  0.0431  535 ILE A CG2 
4024 C CD1 . ILE A 549 ? 0.5301 0.4303 0.6004 -0.0153 0.0451  0.0451  535 ILE A CD1 
4025 N N   . PRO A 550 ? 0.4467 0.3193 0.4973 -0.0216 0.0850  0.0479  536 PRO A N   
4026 C CA  . PRO A 550 ? 0.4848 0.3530 0.5270 -0.0206 0.0971  0.0440  536 PRO A CA  
4027 C C   . PRO A 550 ? 0.6915 0.5506 0.7056 -0.0226 0.0969  0.0387  536 PRO A C   
4028 O O   . PRO A 550 ? 0.6325 0.4920 0.6385 -0.0260 0.0867  0.0355  536 PRO A O   
4029 C CB  . PRO A 550 ? 0.4952 0.3654 0.5544 -0.0175 0.0978  0.0380  536 PRO A CB  
4030 C CG  . PRO A 550 ? 0.4980 0.3737 0.5722 -0.0193 0.0871  0.0385  536 PRO A CG  
4031 C CD  . PRO A 550 ? 0.4672 0.3460 0.5358 -0.0214 0.0788  0.0430  536 PRO A CD  
4032 N N   . PRO A 551 ? 0.7319 0.5848 0.7312 -0.0209 0.1084  0.0361  537 PRO A N   
4033 C CA  . PRO A 551 ? 0.5269 0.3688 0.4952 -0.0236 0.1085  0.0308  537 PRO A CA  
4034 C C   . PRO A 551 ? 0.6102 0.4441 0.5698 -0.0274 0.1012  0.0213  537 PRO A C   
4035 O O   . PRO A 551 ? 0.6952 0.5264 0.6345 -0.0332 0.0944  0.0180  537 PRO A O   
4036 C CB  . PRO A 551 ? 0.6590 0.4969 0.6182 -0.0191 0.1243  0.0277  537 PRO A CB  
4037 C CG  . PRO A 551 ? 0.6738 0.5258 0.6571 -0.0170 0.1318  0.0346  537 PRO A CG  
4038 C CD  . PRO A 551 ? 0.6707 0.5298 0.6810 -0.0170 0.1219  0.0375  537 PRO A CD  
4039 N N   . LEU A 552 ? 0.5529 0.3820 0.5248 -0.0253 0.1021  0.0167  538 LEU A N   
4040 C CA  . LEU A 552 ? 0.6572 0.4730 0.6153 -0.0320 0.0970  0.0078  538 LEU A CA  
4041 C C   . LEU A 552 ? 0.7235 0.5533 0.6876 -0.0413 0.0843  0.0078  538 LEU A C   
4042 O O   . LEU A 552 ? 0.6814 0.5078 0.6277 -0.0510 0.0792  0.0006  538 LEU A O   
4043 C CB  . LEU A 552 ? 0.5093 0.3130 0.4761 -0.0273 0.0998  0.0046  538 LEU A CB  
4044 C CG  . LEU A 552 ? 0.5794 0.3667 0.5326 -0.0376 0.0942  -0.0026 538 LEU A CG  
4045 C CD1 . LEU A 552 ? 0.5317 0.2963 0.4502 -0.0439 0.0967  -0.0115 538 LEU A CD1 
4046 C CD2 . LEU A 552 ? 0.5573 0.3299 0.5167 -0.0321 0.0955  -0.0032 538 LEU A CD2 
4047 N N   . LEU A 553 ? 0.6897 0.5370 0.6789 -0.0385 0.0792  0.0148  539 LEU A N   
4048 C CA  . LEU A 553 ? 0.6873 0.5518 0.6853 -0.0443 0.0674  0.0134  539 LEU A CA  
4049 C C   . LEU A 553 ? 0.6349 0.5091 0.6192 -0.0451 0.0599  0.0142  539 LEU A C   
4050 O O   . LEU A 553 ? 0.6625 0.5516 0.6459 -0.0515 0.0500  0.0083  539 LEU A O   
4051 C CB  . LEU A 553 ? 0.5193 0.3966 0.5456 -0.0390 0.0643  0.0195  539 LEU A CB  
4052 C CG  . LEU A 553 ? 0.7281 0.6267 0.7673 -0.0398 0.0526  0.0188  539 LEU A CG  
4053 C CD1 . LEU A 553 ? 0.5829 0.4907 0.6199 -0.0514 0.0482  0.0082  539 LEU A CD1 
4054 C CD2 . LEU A 553 ? 0.5524 0.4563 0.6158 -0.0336 0.0521  0.0242  539 LEU A CD2 
4055 N N   . GLY A 554 ? 0.6246 0.4919 0.5969 -0.0392 0.0643  0.0211  540 GLY A N   
4056 C CA  . GLY A 554 ? 0.5923 0.4636 0.5439 -0.0395 0.0568  0.0220  540 GLY A CA  
4057 C C   . GLY A 554 ? 0.7861 0.6536 0.7145 -0.0490 0.0549  0.0109  540 GLY A C   
4058 O O   . GLY A 554 ? 0.9190 0.8013 0.8404 -0.0530 0.0429  0.0065  540 GLY A O   
4059 N N   . ALA A 555 ? 0.7218 0.5695 0.6376 -0.0523 0.0661  0.0052  541 ALA A N   
4060 C CA  . ALA A 555 ? 0.8093 0.6467 0.6998 -0.0631 0.0650  -0.0066 541 ALA A CA  
4061 C C   . ALA A 555 ? 0.7771 0.6259 0.6776 -0.0753 0.0568  -0.0150 541 ALA A C   
4062 O O   . ALA A 555 ? 0.8761 0.7324 0.7621 -0.0869 0.0492  -0.0240 541 ALA A O   
4063 C CB  . ALA A 555 ? 0.6546 0.4633 0.5280 -0.0610 0.0791  -0.0110 541 ALA A CB  
4064 N N   . ILE A 556 ? 0.7114 0.5634 0.6359 -0.0744 0.0583  -0.0130 542 ILE A N   
4065 C CA  . ILE A 556 ? 0.7589 0.6227 0.6923 -0.0879 0.0526  -0.0210 542 ILE A CA  
4066 C C   . ILE A 556 ? 0.8825 0.7834 0.8291 -0.0901 0.0389  -0.0229 542 ILE A C   
4067 O O   . ILE A 556 ? 0.9041 0.8199 0.8450 -0.1047 0.0326  -0.0336 542 ILE A O   
4068 C CB  . ILE A 556 ? 0.7911 0.6508 0.7456 -0.0850 0.0570  -0.0173 542 ILE A CB  
4069 C CG1 . ILE A 556 ? 0.6108 0.4337 0.5481 -0.0844 0.0677  -0.0189 542 ILE A CG1 
4070 C CG2 . ILE A 556 ? 0.7244 0.6063 0.6932 -0.0980 0.0506  -0.0238 542 ILE A CG2 
4071 C CD1 . ILE A 556 ? 0.6433 0.4598 0.5957 -0.0828 0.0703  -0.0164 542 ILE A CD1 
4072 N N   . THR A 557 ? 0.7269 0.6430 0.6902 -0.0755 0.0339  -0.0133 543 THR A N   
4073 C CA  . THR A 557 ? 0.8264 0.7769 0.8022 -0.0727 0.0194  -0.0151 543 THR A CA  
4074 C C   . THR A 557 ? 0.8290 0.7875 0.7815 -0.0769 0.0109  -0.0208 543 THR A C   
4075 O O   . THR A 557 ? 0.8509 0.8419 0.8106 -0.0822 -0.0013 -0.0295 543 THR A O   
4076 C CB  . THR A 557 ? 0.6810 0.6366 0.6720 -0.0546 0.0154  -0.0030 543 THR A CB  
4077 O OG1 . THR A 557 ? 0.7627 0.6935 0.7347 -0.0467 0.0216  0.0070  543 THR A OG1 
4078 C CG2 . THR A 557 ? 0.6214 0.5765 0.6384 -0.0515 0.0207  0.0003  543 THR A CG2 
4079 N N   . LYS A 558 ? 0.8436 0.7757 0.7684 -0.0747 0.0171  -0.0170 544 LYS A N   
4080 C CA  . LYS A 558 ? 1.0227 0.9586 0.9203 -0.0796 0.0095  -0.0229 544 LYS A CA  
4081 C C   . LYS A 558 ? 0.9385 0.8758 0.8248 -0.1007 0.0097  -0.0387 544 LYS A C   
4082 O O   . LYS A 558 ? 0.8851 0.8408 0.7587 -0.1090 -0.0012 -0.0478 544 LYS A O   
4083 C CB  . LYS A 558 ? 0.9562 0.8631 0.8246 -0.0719 0.0176  -0.0150 544 LYS A CB  
4084 C CG  . LYS A 558 ? 1.0623 0.9713 0.9417 -0.0552 0.0152  -0.0001 544 LYS A CG  
4085 C CD  . LYS A 558 ? 1.1455 1.0430 1.0015 -0.0448 0.0134  0.0108  544 LYS A CD  
4086 C CE  . LYS A 558 ? 1.1469 1.0551 1.0265 -0.0322 0.0058  0.0207  544 LYS A CE  
4087 N NZ  . LYS A 558 ? 1.2316 1.1465 1.0964 -0.0211 -0.0099 0.0267  544 LYS A NZ  
4088 N N   . ALA A 559 ? 0.9568 0.8736 0.8455 -0.1104 0.0212  -0.0424 545 ALA A N   
4089 C CA  . ALA A 559 ? 0.9824 0.8955 0.8579 -0.1331 0.0219  -0.0571 545 ALA A CA  
4090 C C   . ALA A 559 ? 0.9232 0.8797 0.8240 -0.1447 0.0115  -0.0654 545 ALA A C   
4091 O O   . ALA A 559 ? 0.9562 0.9271 0.8471 -0.1648 0.0063  -0.0790 545 ALA A O   
4092 C CB  . ALA A 559 ? 0.8237 0.6960 0.6886 -0.1389 0.0366  -0.0579 545 ALA A CB  
4093 N N   . LEU A 560 ? 1.0188 0.9985 0.9522 -0.1333 0.0088  -0.0587 546 LEU A N   
4094 C CA  . LEU A 560 ? 1.0046 1.0304 0.9650 -0.1416 -0.0001 -0.0675 546 LEU A CA  
4095 C C   . LEU A 560 ? 1.0289 1.0968 0.9925 -0.1391 -0.0170 -0.0743 546 LEU A C   
4096 O O   . LEU A 560 ? 0.9814 1.0938 0.9655 -0.1494 -0.0247 -0.0859 546 LEU A O   
4097 C CB  . LEU A 560 ? 0.8621 0.9009 0.8545 -0.1262 0.0007  -0.0589 546 LEU A CB  
4098 C CG  . LEU A 560 ? 0.9442 0.9694 0.9469 -0.1356 0.0122  -0.0591 546 LEU A CG  
4099 C CD1 . LEU A 560 ? 0.9349 0.9770 0.9361 -0.1634 0.0138  -0.0742 546 LEU A CD1 
4100 C CD2 . LEU A 560 ? 1.0150 0.9882 0.9979 -0.1321 0.0251  -0.0505 546 LEU A CD2 
4101 N N   . GLU A 561 ? 1.0821 1.1391 1.0253 -0.1262 -0.0230 -0.0682 547 GLU A N   
4102 C CA  . GLU A 561 ? 1.1549 1.2468 1.0928 -0.1248 -0.0404 -0.0755 547 GLU A CA  
4103 C C   . GLU A 561 ? 1.1622 1.2502 1.0757 -0.1514 -0.0392 -0.0907 547 GLU A C   
4104 O O   . GLU A 561 ? 1.1390 1.1901 1.0181 -0.1548 -0.0337 -0.0895 547 GLU A O   
4105 C CB  . GLU A 561 ? 1.1559 1.2314 1.0748 -0.1021 -0.0466 -0.0622 547 GLU A CB  
4106 C CG  . GLU A 561 ? 1.2642 1.3707 1.1714 -0.0979 -0.0663 -0.0684 547 GLU A CG  
4107 C CD  . GLU A 561 ? 1.3362 1.4750 1.2647 -0.0732 -0.0828 -0.0623 547 GLU A CD  
4108 O OE1 . GLU A 561 ? 1.2707 1.4005 1.2189 -0.0592 -0.0775 -0.0518 547 GLU A OE1 
4109 O OE2 . GLU A 561 ? 1.3097 1.4817 1.2340 -0.0670 -0.1019 -0.0685 547 GLU A OE2 
4110 N N   . ALA A 562 ? 1.1233 1.2499 1.0539 -0.1717 -0.0437 -0.1061 548 ALA A N   
4111 C CA  . ALA A 562 ? 1.1138 1.2374 1.0217 -0.2019 -0.0423 -0.1222 548 ALA A CA  
4112 C C   . ALA A 562 ? 1.1131 1.3014 1.0465 -0.2197 -0.0539 -0.1399 548 ALA A C   
4113 O O   . ALA A 562 ? 1.0648 1.2767 1.0259 -0.2293 -0.0487 -0.1444 548 ALA A O   
4114 C CB  . ALA A 562 ? 0.9287 1.0006 0.8187 -0.2199 -0.0228 -0.1224 548 ALA A CB  
4115 N N   . THR B 17  ? 1.1027 1.0417 1.1964 0.0506  -0.1291 0.0878  3   THR B N   
4116 C CA  . THR B 17  ? 0.9844 0.9358 1.1039 0.0508  -0.1204 0.0817  3   THR B CA  
4117 C C   . THR B 17  ? 0.9330 0.9019 1.0797 0.0545  -0.1286 0.0785  3   THR B C   
4118 O O   . THR B 17  ? 0.9180 0.8920 1.0857 0.0598  -0.1273 0.0791  3   THR B O   
4119 C CB  . THR B 17  ? 1.1763 1.1202 1.3018 0.0540  -0.1115 0.0848  3   THR B CB  
4120 O OG1 . THR B 17  ? 1.0296 0.9729 1.1669 0.0617  -0.1200 0.0902  3   THR B OG1 
4121 C CG2 . THR B 17  ? 0.9798 0.9059 1.0796 0.0507  -0.1045 0.0892  3   THR B CG2 
4122 N N   . PRO B 18  ? 0.8751 0.8528 1.0218 0.0516  -0.1367 0.0750  4   PRO B N   
4123 C CA  . PRO B 18  ? 0.7055 0.7010 0.8798 0.0542  -0.1439 0.0716  4   PRO B CA  
4124 C C   . PRO B 18  ? 0.6874 0.6941 0.8837 0.0527  -0.1323 0.0649  4   PRO B C   
4125 O O   . PRO B 18  ? 0.6330 0.6366 0.8216 0.0476  -0.1211 0.0610  4   PRO B O   
4126 C CB  . PRO B 18  ? 0.7353 0.7354 0.9004 0.0493  -0.1535 0.0685  4   PRO B CB  
4127 C CG  . PRO B 18  ? 0.8677 0.8502 0.9981 0.0460  -0.1538 0.0720  4   PRO B CG  
4128 C CD  . PRO B 18  ? 0.8254 0.7976 0.9481 0.0453  -0.1389 0.0731  4   PRO B CD  
4129 N N   . TYR B 19  ? 0.4674 0.4871 0.6913 0.0574  -0.1350 0.0638  5   TYR B N   
4130 C CA  . TYR B 19  ? 0.4087 0.4391 0.6535 0.0562  -0.1242 0.0576  5   TYR B CA  
4131 C C   . TYR B 19  ? 0.4165 0.4535 0.6589 0.0485  -0.1208 0.0510  5   TYR B C   
4132 O O   . TYR B 19  ? 0.3676 0.4108 0.6095 0.0458  -0.1300 0.0494  5   TYR B O   
4133 C CB  . TYR B 19  ? 0.3582 0.4028 0.6332 0.0622  -0.1288 0.0572  5   TYR B CB  
4134 C CG  . TYR B 19  ? 0.3922 0.4451 0.6875 0.0624  -0.1165 0.0520  5   TYR B CG  
4135 C CD1 . TYR B 19  ? 0.3153 0.3616 0.6151 0.0672  -0.1085 0.0535  5   TYR B CD1 
4136 C CD2 . TYR B 19  ? 0.3198 0.3859 0.6287 0.0576  -0.1128 0.0455  5   TYR B CD2 
4137 C CE1 . TYR B 19  ? 0.3003 0.3531 0.6164 0.0672  -0.0973 0.0485  5   TYR B CE1 
4138 C CE2 . TYR B 19  ? 0.2890 0.3615 0.6142 0.0576  -0.1013 0.0410  5   TYR B CE2 
4139 C CZ  . TYR B 19  ? 0.2875 0.3533 0.6156 0.0624  -0.0937 0.0424  5   TYR B CZ  
4140 O OH  . TYR B 19  ? 0.2750 0.3460 0.6169 0.0622  -0.0823 0.0377  5   TYR B OH  
4141 N N   . CYS B 20  ? 0.3181 0.3533 0.5589 0.0449  -0.1079 0.0471  6   CYS B N   
4142 C CA  . CYS B 20  ? 0.3105 0.3485 0.5458 0.0378  -0.1037 0.0415  6   CYS B CA  
4143 C C   . CYS B 20  ? 0.2991 0.3437 0.5493 0.0363  -0.0921 0.0368  6   CYS B C   
4144 O O   . CYS B 20  ? 0.3129 0.3594 0.5762 0.0405  -0.0871 0.0374  6   CYS B O   
4145 C CB  . CYS B 20  ? 0.3614 0.3853 0.5687 0.0339  -0.1006 0.0427  6   CYS B CB  
4146 S SG  . CYS B 20  ? 0.4056 0.4176 0.6041 0.0351  -0.0883 0.0450  6   CYS B SG  
4147 N N   . VAL B 21  ? 0.2848 0.3312 0.5308 0.0301  -0.0875 0.0320  7   VAL B N   
4148 C CA  . VAL B 21  ? 0.2759 0.3281 0.5341 0.0279  -0.0774 0.0275  7   VAL B CA  
4149 C C   . VAL B 21  ? 0.2934 0.3379 0.5477 0.0300  -0.0677 0.0287  7   VAL B C   
4150 O O   . VAL B 21  ? 0.2543 0.3037 0.5225 0.0314  -0.0612 0.0268  7   VAL B O   
4151 C CB  . VAL B 21  ? 0.2740 0.3261 0.5242 0.0210  -0.0749 0.0231  7   VAL B CB  
4152 C CG1 . VAL B 21  ? 0.2522 0.3060 0.5087 0.0187  -0.0636 0.0196  7   VAL B CG1 
4153 C CG2 . VAL B 21  ? 0.2742 0.3360 0.5335 0.0184  -0.0837 0.0206  7   VAL B CG2 
4154 N N   . ALA B 22  ? 0.2708 0.3031 0.5061 0.0299  -0.0664 0.0317  8   ALA B N   
4155 C CA  . ALA B 22  ? 0.3313 0.3559 0.5631 0.0315  -0.0582 0.0330  8   ALA B CA  
4156 C C   . ALA B 22  ? 0.3098 0.3362 0.5555 0.0375  -0.0586 0.0350  8   ALA B C   
4157 O O   . ALA B 22  ? 0.2726 0.2988 0.5254 0.0385  -0.0509 0.0332  8   ALA B O   
4158 C CB  . ALA B 22  ? 0.2777 0.2895 0.4884 0.0305  -0.0579 0.0365  8   ALA B CB  
4159 N N   . ASP B 23  ? 0.2893 0.3167 0.5386 0.0418  -0.0677 0.0388  9   ASP B N   
4160 C CA  . ASP B 23  ? 0.2798 0.3088 0.5440 0.0483  -0.0684 0.0408  9   ASP B CA  
4161 C C   . ASP B 23  ? 0.3378 0.3804 0.6251 0.0493  -0.0654 0.0363  9   ASP B C   
4162 O O   . ASP B 23  ? 0.3286 0.3716 0.6272 0.0530  -0.0596 0.0353  9   ASP B O   
4163 C CB  . ASP B 23  ? 0.3141 0.3409 0.5767 0.0530  -0.0800 0.0465  9   ASP B CB  
4164 C CG  . ASP B 23  ? 0.4336 0.4462 0.6714 0.0515  -0.0826 0.0512  9   ASP B CG  
4165 O OD1 . ASP B 23  ? 0.3720 0.3740 0.5996 0.0506  -0.0749 0.0523  9   ASP B OD1 
4166 O OD2 . ASP B 23  ? 0.4201 0.4319 0.6483 0.0508  -0.0920 0.0537  9   ASP B OD2 
4167 N N   . TYR B 24  ? 0.2986 0.3520 0.5930 0.0458  -0.0688 0.0332  10  TYR B N   
4168 C CA  . TYR B 24  ? 0.2549 0.3215 0.5715 0.0459  -0.0650 0.0290  10  TYR B CA  
4169 C C   . TYR B 24  ? 0.2449 0.3091 0.5610 0.0436  -0.0523 0.0252  10  TYR B C   
4170 O O   . TYR B 24  ? 0.2587 0.3273 0.5896 0.0465  -0.0464 0.0232  10  TYR B O   
4171 C CB  . TYR B 24  ? 0.2530 0.3301 0.5751 0.0411  -0.0705 0.0263  10  TYR B CB  
4172 C CG  . TYR B 24  ? 0.2491 0.3409 0.5958 0.0407  -0.0672 0.0222  10  TYR B CG  
4173 C CD1 . TYR B 24  ? 0.3031 0.3971 0.6518 0.0359  -0.0569 0.0179  10  TYR B CD1 
4174 C CD2 . TYR B 24  ? 0.2481 0.3517 0.6162 0.0449  -0.0745 0.0230  10  TYR B CD2 
4175 C CE1 . TYR B 24  ? 0.2308 0.3377 0.6013 0.0349  -0.0528 0.0143  10  TYR B CE1 
4176 C CE2 . TYR B 24  ? 0.2649 0.3829 0.6571 0.0442  -0.0706 0.0191  10  TYR B CE2 
4177 C CZ  . TYR B 24  ? 0.3126 0.4318 0.7053 0.0389  -0.0592 0.0148  10  TYR B CZ  
4178 O OH  . TYR B 24  ? 0.2570 0.3899 0.6730 0.0377  -0.0543 0.0111  10  TYR B OH  
4179 N N   . LEU B 25  ? 0.2421 0.2986 0.5407 0.0385  -0.0481 0.0243  11  LEU B N   
4180 C CA  . LEU B 25  ? 0.2342 0.2876 0.5303 0.0361  -0.0374 0.0211  11  LEU B CA  
4181 C C   . LEU B 25  ? 0.2552 0.3012 0.5512 0.0406  -0.0326 0.0223  11  LEU B C   
4182 O O   . LEU B 25  ? 0.3545 0.4020 0.6582 0.0412  -0.0250 0.0192  11  LEU B O   
4183 C CB  . LEU B 25  ? 0.2323 0.2786 0.5102 0.0307  -0.0352 0.0206  11  LEU B CB  
4184 C CG  . LEU B 25  ? 0.2266 0.2672 0.4979 0.0284  -0.0259 0.0184  11  LEU B CG  
4185 C CD1 . LEU B 25  ? 0.2204 0.2679 0.5041 0.0276  -0.0195 0.0147  11  LEU B CD1 
4186 C CD2 . LEU B 25  ? 0.2482 0.2838 0.5046 0.0235  -0.0251 0.0180  11  LEU B CD2 
4187 N N   . LEU B 26  ? 0.2682 0.3050 0.5547 0.0434  -0.0368 0.0266  12  LEU B N   
4188 C CA  . LEU B 26  ? 0.3040 0.3324 0.5904 0.0474  -0.0327 0.0277  12  LEU B CA  
4189 C C   . LEU B 26  ? 0.3157 0.3505 0.6218 0.0534  -0.0325 0.0268  12  LEU B C   
4190 O O   . LEU B 26  ? 0.2500 0.2817 0.5610 0.0555  -0.0253 0.0244  12  LEU B O   
4191 C CB  . LEU B 26  ? 0.3505 0.3673 0.6228 0.0489  -0.0374 0.0330  12  LEU B CB  
4192 C CG  . LEU B 26  ? 0.3359 0.3455 0.5892 0.0433  -0.0359 0.0337  12  LEU B CG  
4193 C CD1 . LEU B 26  ? 0.3477 0.3461 0.5876 0.0446  -0.0400 0.0394  12  LEU B CD1 
4194 C CD2 . LEU B 26  ? 0.2666 0.2727 0.5162 0.0400  -0.0269 0.0301  12  LEU B CD2 
4195 N N   . ASP B 27  ? 0.2839 0.3278 0.6021 0.0563  -0.0404 0.0285  13  ASP B N   
4196 C CA  . ASP B 27  ? 0.2677 0.3197 0.6079 0.0623  -0.0403 0.0275  13  ASP B CA  
4197 C C   . ASP B 27  ? 0.3467 0.4070 0.6990 0.0602  -0.0305 0.0216  13  ASP B C   
4198 O O   . ASP B 27  ? 0.2861 0.3462 0.6490 0.0642  -0.0239 0.0193  13  ASP B O   
4199 C CB  . ASP B 27  ? 0.3792 0.4414 0.7312 0.0649  -0.0517 0.0302  13  ASP B CB  
4200 C CG  . ASP B 27  ? 0.5104 0.5652 0.8597 0.0713  -0.0605 0.0363  13  ASP B CG  
4201 O OD1 . ASP B 27  ? 0.6516 0.6958 0.9983 0.0754  -0.0563 0.0378  13  ASP B OD1 
4202 O OD2 . ASP B 27  ? 0.3564 0.4150 0.7056 0.0720  -0.0718 0.0397  13  ASP B OD2 
4203 N N   . ARG B 28  ? 0.3255 0.3923 0.6756 0.0538  -0.0291 0.0189  14  ARG B N   
4204 C CA  . ARG B 28  ? 0.2470 0.3204 0.6061 0.0511  -0.0194 0.0138  14  ARG B CA  
4205 C C   . ARG B 28  ? 0.2984 0.3607 0.6448 0.0497  -0.0097 0.0116  14  ARG B C   
4206 O O   . ARG B 28  ? 0.2472 0.3112 0.6014 0.0507  -0.0009 0.0079  14  ARG B O   
4207 C CB  . ARG B 28  ? 0.2883 0.3690 0.6462 0.0443  -0.0205 0.0121  14  ARG B CB  
4208 C CG  . ARG B 28  ? 0.2264 0.3185 0.5972 0.0446  -0.0304 0.0134  14  ARG B CG  
4209 C CD  . ARG B 28  ? 0.2287 0.3314 0.6244 0.0508  -0.0313 0.0130  14  ARG B CD  
4210 N NE  . ARG B 28  ? 0.2283 0.3466 0.6436 0.0479  -0.0315 0.0102  14  ARG B NE  
4211 C CZ  . ARG B 28  ? 0.3086 0.4398 0.7495 0.0523  -0.0330 0.0094  14  ARG B CZ  
4212 N NH1 . ARG B 28  ? 0.2650 0.3952 0.7155 0.0604  -0.0346 0.0113  14  ARG B NH1 
4213 N NH2 . ARG B 28  ? 0.2488 0.3943 0.7074 0.0483  -0.0325 0.0065  14  ARG B NH2 
4214 N N   . LEU B 29  ? 0.2420 0.2931 0.5688 0.0473  -0.0111 0.0137  15  LEU B N   
4215 C CA  . LEU B 29  ? 0.3450 0.3856 0.6595 0.0457  -0.0035 0.0117  15  LEU B CA  
4216 C C   . LEU B 29  ? 0.3744 0.4095 0.6951 0.0513  0.0004  0.0108  15  LEU B C   
4217 O O   . LEU B 29  ? 0.3084 0.3403 0.6282 0.0508  0.0089  0.0068  15  LEU B O   
4218 C CB  . LEU B 29  ? 0.3762 0.4072 0.6720 0.0426  -0.0069 0.0145  15  LEU B CB  
4219 C CG  . LEU B 29  ? 0.4341 0.4558 0.7174 0.0396  -0.0004 0.0123  15  LEU B CG  
4220 C CD1 . LEU B 29  ? 0.4530 0.4794 0.7358 0.0352  0.0052  0.0086  15  LEU B CD1 
4221 C CD2 . LEU B 29  ? 0.4051 0.4187 0.6731 0.0370  -0.0038 0.0153  15  LEU B CD2 
4222 N N   . THR B 30  ? 0.3177 0.3504 0.6432 0.0568  -0.0056 0.0145  16  THR B N   
4223 C CA  . THR B 30  ? 0.3742 0.4005 0.7062 0.0626  -0.0020 0.0137  16  THR B CA  
4224 C C   . THR B 30  ? 0.3222 0.3583 0.6741 0.0662  0.0038  0.0096  16  THR B C   
4225 O O   . THR B 30  ? 0.4385 0.4692 0.7931 0.0688  0.0115  0.0061  16  THR B O   
4226 C CB  . THR B 30  ? 0.3319 0.3524 0.6642 0.0679  -0.0103 0.0194  16  THR B CB  
4227 O OG1 . THR B 30  ? 0.5267 0.5581 0.8694 0.0698  -0.0190 0.0224  16  THR B OG1 
4228 C CG2 . THR B 30  ? 0.4783 0.4869 0.7900 0.0641  -0.0130 0.0228  16  THR B CG2 
4229 N N   . ASP B 31  ? 0.4159 0.4664 0.7821 0.0660  0.0005  0.0096  17  ASP B N   
4230 C CA  . ASP B 31  ? 0.3691 0.4308 0.7558 0.0684  0.0071  0.0054  17  ASP B CA  
4231 C C   . ASP B 31  ? 0.3342 0.3929 0.7138 0.0639  0.0192  0.0000  17  ASP B C   
4232 O O   . ASP B 31  ? 0.3195 0.3792 0.7093 0.0670  0.0279  -0.0041 17  ASP B O   
4233 C CB  . ASP B 31  ? 0.4099 0.4877 0.8117 0.0668  0.0015  0.0061  17  ASP B CB  
4234 C CG  . ASP B 31  ? 0.4783 0.5609 0.8909 0.0722  -0.0107 0.0110  17  ASP B CG  
4235 O OD1 . ASP B 31  ? 0.4100 0.4833 0.8198 0.0779  -0.0141 0.0140  17  ASP B OD1 
4236 O OD2 . ASP B 31  ? 0.3562 0.4513 0.7794 0.0705  -0.0174 0.0118  17  ASP B OD2 
4237 N N   . CYS B 32  ? 0.3639 0.4184 0.7257 0.0569  0.0199  -0.0002 18  CYS B N   
4238 C CA  . CYS B 32  ? 0.2454 0.2967 0.5983 0.0522  0.0300  -0.0046 18  CYS B CA  
4239 C C   . CYS B 32  ? 0.3846 0.4216 0.7245 0.0533  0.0355  -0.0069 18  CYS B C   
4240 O O   . CYS B 32  ? 0.2998 0.3331 0.6323 0.0503  0.0442  -0.0110 18  CYS B O   
4241 C CB  . CYS B 32  ? 0.3261 0.3775 0.6650 0.0448  0.0277  -0.0035 18  CYS B CB  
4242 S SG  . CYS B 32  ? 0.3402 0.4074 0.6934 0.0420  0.0225  -0.0021 18  CYS B SG  
4243 N N   . GLY B 33  ? 0.2914 0.3198 0.6281 0.0573  0.0308  -0.0044 19  GLY B N   
4244 C CA  . GLY B 33  ? 0.3264 0.3412 0.6535 0.0587  0.0357  -0.0070 19  GLY B CA  
4245 C C   . GLY B 33  ? 0.3968 0.3997 0.7048 0.0552  0.0316  -0.0047 19  GLY B C   
4246 O O   . GLY B 33  ? 0.4030 0.3944 0.7021 0.0550  0.0356  -0.0074 19  GLY B O   
4247 N N   . ALA B 34  ? 0.3724 0.3777 0.6744 0.0521  0.0241  -0.0003 20  ALA B N   
4248 C CA  . ALA B 34  ? 0.3303 0.3257 0.6162 0.0487  0.0207  0.0019  20  ALA B CA  
4249 C C   . ALA B 34  ? 0.4402 0.4302 0.7275 0.0527  0.0144  0.0068  20  ALA B C   
4250 O O   . ALA B 34  ? 0.4571 0.4539 0.7524 0.0554  0.0083  0.0106  20  ALA B O   
4251 C CB  . ALA B 34  ? 0.3232 0.3232 0.6003 0.0428  0.0176  0.0035  20  ALA B CB  
4252 N N   . ASP B 35  ? 0.4040 0.3812 0.6832 0.0528  0.0155  0.0069  21  ASP B N   
4253 C CA  . ASP B 35  ? 0.3747 0.3440 0.6522 0.0557  0.0102  0.0120  21  ASP B CA  
4254 C C   . ASP B 35  ? 0.4111 0.3740 0.6739 0.0504  0.0074  0.0149  21  ASP B C   
4255 O O   . ASP B 35  ? 0.2988 0.2542 0.5579 0.0517  0.0035  0.0197  21  ASP B O   
4256 C CB  . ASP B 35  ? 0.3562 0.3147 0.6376 0.0603  0.0139  0.0101  21  ASP B CB  
4257 C CG  . ASP B 35  ? 0.4963 0.4609 0.7933 0.0659  0.0182  0.0064  21  ASP B CG  
4258 O OD1 . ASP B 35  ? 0.5229 0.4990 0.8324 0.0693  0.0145  0.0086  21  ASP B OD1 
4259 O OD2 . ASP B 35  ? 0.4970 0.4553 0.7941 0.0667  0.0255  0.0011  21  ASP B OD2 
4260 N N   . HIS B 36  ? 0.3219 0.2873 0.5765 0.0444  0.0096  0.0124  22  HIS B N   
4261 C CA  . HIS B 36  ? 0.3698 0.3308 0.6126 0.0392  0.0078  0.0145  22  HIS B CA  
4262 C C   . HIS B 36  ? 0.3548 0.3253 0.5945 0.0352  0.0066  0.0142  22  HIS B C   
4263 O O   . HIS B 36  ? 0.3180 0.2963 0.5624 0.0351  0.0086  0.0113  22  HIS B O   
4264 C CB  . HIS B 36  ? 0.3426 0.2941 0.5784 0.0359  0.0119  0.0109  22  HIS B CB  
4265 C CG  . HIS B 36  ? 0.3515 0.2917 0.5894 0.0392  0.0136  0.0106  22  HIS B CG  
4266 N ND1 . HIS B 36  ? 0.3434 0.2824 0.5893 0.0440  0.0171  0.0072  22  HIS B ND1 
4267 C CD2 . HIS B 36  ? 0.2904 0.2194 0.5238 0.0384  0.0127  0.0132  22  HIS B CD2 
4268 C CE1 . HIS B 36  ? 0.3519 0.2789 0.5979 0.0463  0.0180  0.0076  22  HIS B CE1 
4269 N NE2 . HIS B 36  ? 0.3914 0.3119 0.6297 0.0428  0.0153  0.0114  22  HIS B NE2 
4270 N N   . LEU B 37  ? 0.3237 0.2929 0.5555 0.0320  0.0037  0.0174  23  LEU B N   
4271 C CA  . LEU B 37  ? 0.3091 0.2853 0.5369 0.0281  0.0028  0.0171  23  LEU B CA  
4272 C C   . LEU B 37  ? 0.3173 0.2885 0.5367 0.0234  0.0042  0.0168  23  LEU B C   
4273 O O   . LEU B 37  ? 0.2888 0.2541 0.5039 0.0227  0.0031  0.0199  23  LEU B O   
4274 C CB  . LEU B 37  ? 0.3052 0.2861 0.5329 0.0291  -0.0022 0.0209  23  LEU B CB  
4275 C CG  . LEU B 37  ? 0.2957 0.2822 0.5185 0.0252  -0.0033 0.0207  23  LEU B CG  
4276 C CD1 . LEU B 37  ? 0.2942 0.2882 0.5219 0.0240  -0.0012 0.0170  23  LEU B CD1 
4277 C CD2 . LEU B 37  ? 0.2888 0.2774 0.5094 0.0262  -0.0086 0.0243  23  LEU B CD2 
4278 N N   . PHE B 38  ? 0.3094 0.2830 0.5269 0.0204  0.0065  0.0132  24  PHE B N   
4279 C CA  . PHE B 38  ? 0.3429 0.3137 0.5546 0.0161  0.0070  0.0126  24  PHE B CA  
4280 C C   . PHE B 38  ? 0.3093 0.2858 0.5184 0.0138  0.0054  0.0141  24  PHE B C   
4281 O O   . PHE B 38  ? 0.2985 0.2812 0.5093 0.0146  0.0044  0.0141  24  PHE B O   
4282 C CB  . PHE B 38  ? 0.3375 0.3070 0.5476 0.0142  0.0094  0.0081  24  PHE B CB  
4283 C CG  . PHE B 38  ? 0.2959 0.2588 0.5074 0.0162  0.0119  0.0055  24  PHE B CG  
4284 C CD1 . PHE B 38  ? 0.2760 0.2412 0.4920 0.0196  0.0141  0.0036  24  PHE B CD1 
4285 C CD2 . PHE B 38  ? 0.2724 0.2268 0.4815 0.0146  0.0123  0.0046  24  PHE B CD2 
4286 C CE1 . PHE B 38  ? 0.3442 0.3029 0.5618 0.0219  0.0172  0.0007  24  PHE B CE1 
4287 C CE2 . PHE B 38  ? 0.2931 0.2400 0.5029 0.0165  0.0149  0.0017  24  PHE B CE2 
4288 C CZ  . PHE B 38  ? 0.2942 0.2431 0.5081 0.0205  0.0175  -0.0003 24  PHE B CZ  
4289 N N   . GLY B 39  ? 0.3289 0.3033 0.5348 0.0109  0.0055  0.0151  25  GLY B N   
4290 C CA  . GLY B 39  ? 0.3564 0.3357 0.5603 0.0089  0.0049  0.0157  25  GLY B CA  
4291 C C   . GLY B 39  ? 0.4080 0.3848 0.6098 0.0065  0.0057  0.0177  25  GLY B C   
4292 O O   . GLY B 39  ? 0.2810 0.2524 0.4830 0.0053  0.0068  0.0183  25  GLY B O   
4293 N N   . VAL B 40  ? 0.3019 0.2826 0.5018 0.0056  0.0056  0.0185  26  VAL B N   
4294 C CA  . VAL B 40  ? 0.3052 0.2847 0.5033 0.0034  0.0076  0.0201  26  VAL B CA  
4295 C C   . VAL B 40  ? 0.2993 0.2794 0.4920 0.0044  0.0072  0.0223  26  VAL B C   
4296 O O   . VAL B 40  ? 0.2655 0.2498 0.4577 0.0053  0.0055  0.0211  26  VAL B O   
4297 C CB  . VAL B 40  ? 0.2968 0.2805 0.4987 0.0010  0.0084  0.0178  26  VAL B CB  
4298 C CG1 . VAL B 40  ? 0.2739 0.2578 0.4761 -0.0011 0.0115  0.0191  26  VAL B CG1 
4299 C CG2 . VAL B 40  ? 0.2735 0.2561 0.4792 -0.0003 0.0077  0.0155  26  VAL B CG2 
4300 N N   . PRO B 41  ? 0.2925 0.2677 0.4801 0.0038  0.0087  0.0253  27  PRO B N   
4301 C CA  . PRO B 41  ? 0.2480 0.2224 0.4278 0.0046  0.0078  0.0273  27  PRO B CA  
4302 C C   . PRO B 41  ? 0.3130 0.2907 0.4910 0.0028  0.0103  0.0256  27  PRO B C   
4303 O O   . PRO B 41  ? 0.3261 0.3063 0.5092 0.0010  0.0133  0.0239  27  PRO B O   
4304 C CB  . PRO B 41  ? 0.3167 0.2830 0.4900 0.0041  0.0093  0.0315  27  PRO B CB  
4305 C CG  . PRO B 41  ? 0.3478 0.3124 0.5267 0.0014  0.0131  0.0309  27  PRO B CG  
4306 C CD  . PRO B 41  ? 0.2541 0.2234 0.4418 0.0019  0.0114  0.0272  27  PRO B CD  
4307 N N   . GLY B 42  ? 0.3947 0.3724 0.5657 0.0036  0.0086  0.0259  28  GLY B N   
4308 C CA  . GLY B 42  ? 0.2732 0.2520 0.4402 0.0022  0.0114  0.0242  28  GLY B CA  
4309 C C   . GLY B 42  ? 0.3940 0.3688 0.5490 0.0026  0.0096  0.0257  28  GLY B C   
4310 O O   . GLY B 42  ? 0.4012 0.3743 0.5530 0.0043  0.0048  0.0278  28  GLY B O   
4311 N N   . ASP B 43  ? 0.2912 0.2643 0.4394 0.0011  0.0134  0.0244  29  ASP B N   
4312 C CA  . ASP B 43  ? 0.3563 0.3242 0.4902 0.0010  0.0117  0.0255  29  ASP B CA  
4313 C C   . ASP B 43  ? 0.4424 0.4132 0.5759 0.0023  0.0046  0.0240  29  ASP B C   
4314 O O   . ASP B 43  ? 0.4806 0.4478 0.6045 0.0028  -0.0001 0.0260  29  ASP B O   
4315 C CB  . ASP B 43  ? 0.4020 0.3672 0.5285 -0.0009 0.0182  0.0235  29  ASP B CB  
4316 C CG  . ASP B 43  ? 0.5979 0.5670 0.7275 -0.0008 0.0181  0.0186  29  ASP B CG  
4317 O OD1 . ASP B 43  ? 0.4357 0.4108 0.5772 0.0001  0.0160  0.0167  29  ASP B OD1 
4318 O OD2 . ASP B 43  ? 0.4775 0.4427 0.5966 -0.0017 0.0206  0.0166  29  ASP B OD2 
4319 N N   . TYR B 44  ? 0.3458 0.3231 0.4901 0.0027  0.0033  0.0209  30  TYR B N   
4320 C CA  . TYR B 44  ? 0.3759 0.3566 0.5219 0.0033  -0.0028 0.0194  30  TYR B CA  
4321 C C   . TYR B 44  ? 0.4310 0.4139 0.5824 0.0054  -0.0080 0.0219  30  TYR B C   
4322 O O   . TYR B 44  ? 0.3466 0.3328 0.4998 0.0060  -0.0135 0.0211  30  TYR B O   
4323 C CB  . TYR B 44  ? 0.3526 0.3384 0.5077 0.0028  -0.0016 0.0156  30  TYR B CB  
4324 C CG  . TYR B 44  ? 0.3560 0.3397 0.5072 0.0014  0.0027  0.0126  30  TYR B CG  
4325 C CD1 . TYR B 44  ? 0.4473 0.4263 0.5864 0.0003  0.0028  0.0114  30  TYR B CD1 
4326 C CD2 . TYR B 44  ? 0.4475 0.4337 0.6069 0.0015  0.0064  0.0109  30  TYR B CD2 
4327 C CE1 . TYR B 44  ? 0.3495 0.3259 0.4854 -0.0006 0.0075  0.0081  30  TYR B CE1 
4328 C CE2 . TYR B 44  ? 0.2983 0.2826 0.4558 0.0010  0.0105  0.0082  30  TYR B CE2 
4329 C CZ  . TYR B 44  ? 0.3449 0.3243 0.4910 0.0000  0.0115  0.0065  30  TYR B CZ  
4330 O OH  . TYR B 44  ? 0.3226 0.2996 0.4673 -0.0002 0.0163  0.0033  30  TYR B OH  
4331 N N   . ASN B 45  ? 0.4237 0.4050 0.5786 0.0067  -0.0065 0.0246  31  ASN B N   
4332 C CA  . ASN B 45  ? 0.3501 0.3329 0.5111 0.0093  -0.0108 0.0267  31  ASN B CA  
4333 C C   . ASN B 45  ? 0.3299 0.3057 0.4849 0.0107  -0.0115 0.0314  31  ASN B C   
4334 O O   . ASN B 45  ? 0.3881 0.3642 0.5494 0.0134  -0.0142 0.0332  31  ASN B O   
4335 C CB  . ASN B 45  ? 0.2693 0.2568 0.4429 0.0099  -0.0089 0.0248  31  ASN B CB  
4336 C CG  . ASN B 45  ? 0.4154 0.3999 0.5905 0.0089  -0.0037 0.0251  31  ASN B CG  
4337 O OD1 . ASN B 45  ? 0.3146 0.2933 0.4843 0.0086  -0.0019 0.0279  31  ASN B OD1 
4338 N ND2 . ASN B 45  ? 0.2503 0.2384 0.4326 0.0082  -0.0016 0.0224  31  ASN B ND2 
4339 N N   . LEU B 46  ? 0.3671 0.3361 0.5102 0.0090  -0.0086 0.0335  32  LEU B N   
4340 C CA  . LEU B 46  ? 0.3343 0.2952 0.4708 0.0100  -0.0086 0.0385  32  LEU B CA  
4341 C C   . LEU B 46  ? 0.4058 0.3648 0.5384 0.0130  -0.0166 0.0418  32  LEU B C   
4342 O O   . LEU B 46  ? 0.3821 0.3375 0.5176 0.0157  -0.0187 0.0453  32  LEU B O   
4343 C CB  . LEU B 46  ? 0.3722 0.3259 0.4955 0.0071  -0.0031 0.0401  32  LEU B CB  
4344 C CG  . LEU B 46  ? 0.3380 0.2932 0.4663 0.0042  0.0051  0.0377  32  LEU B CG  
4345 C CD1 . LEU B 46  ? 0.3341 0.2816 0.4497 0.0015  0.0112  0.0399  32  LEU B CD1 
4346 C CD2 . LEU B 46  ? 0.2852 0.2418 0.4259 0.0046  0.0067  0.0378  32  LEU B CD2 
4347 N N   . GLN B 47  ? 0.3583 0.3197 0.4851 0.0128  -0.0217 0.0405  33  GLN B N   
4348 C CA  . GLN B 47  ? 0.4655 0.4259 0.5890 0.0157  -0.0306 0.0437  33  GLN B CA  
4349 C C   . GLN B 47  ? 0.4020 0.3702 0.5430 0.0192  -0.0348 0.0431  33  GLN B C   
4350 O O   . GLN B 47  ? 0.3609 0.3270 0.5037 0.0229  -0.0405 0.0469  33  GLN B O   
4351 C CB  . GLN B 47  ? 0.4630 0.4244 0.5764 0.0139  -0.0354 0.0417  33  GLN B CB  
4352 C CG  . GLN B 47  ? 0.6899 0.6440 0.7868 0.0102  -0.0292 0.0409  33  GLN B CG  
4353 C CD  . GLN B 47  ? 0.6405 0.5891 0.7193 0.0091  -0.0348 0.0415  33  GLN B CD  
4354 O OE1 . GLN B 47  ? 0.8540 0.8062 0.9311 0.0071  -0.0370 0.0370  33  GLN B OE1 
4355 N NE2 . GLN B 47  ? 0.9014 0.8403 0.9655 0.0100  -0.0372 0.0472  33  GLN B NE2 
4356 N N   . PHE B 48  ? 0.3871 0.3638 0.5410 0.0183  -0.0319 0.0383  34  PHE B N   
4357 C CA  . PHE B 48  ? 0.3283 0.3117 0.4986 0.0214  -0.0335 0.0374  34  PHE B CA  
4358 C C   . PHE B 48  ? 0.3981 0.3757 0.5716 0.0239  -0.0304 0.0401  34  PHE B C   
4359 O O   . PHE B 48  ? 0.3577 0.3365 0.5401 0.0279  -0.0337 0.0417  34  PHE B O   
4360 C CB  . PHE B 48  ? 0.2671 0.2586 0.4476 0.0193  -0.0295 0.0321  34  PHE B CB  
4361 C CG  . PHE B 48  ? 0.3281 0.3255 0.5240 0.0219  -0.0290 0.0307  34  PHE B CG  
4362 C CD1 . PHE B 48  ? 0.3702 0.3742 0.5762 0.0247  -0.0347 0.0308  34  PHE B CD1 
4363 C CD2 . PHE B 48  ? 0.2670 0.2635 0.4677 0.0215  -0.0226 0.0289  34  PHE B CD2 
4364 C CE1 . PHE B 48  ? 0.2608 0.2704 0.4816 0.0272  -0.0328 0.0292  34  PHE B CE1 
4365 C CE2 . PHE B 48  ? 0.2742 0.2752 0.4873 0.0238  -0.0213 0.0271  34  PHE B CE2 
4366 C CZ  . PHE B 48  ? 0.2765 0.2839 0.4998 0.0267  -0.0257 0.0272  34  PHE B CZ  
4367 N N   . LEU B 49  ? 0.3131 0.2846 0.4806 0.0214  -0.0239 0.0404  35  LEU B N   
4368 C CA  . LEU B 49  ? 0.3210 0.2862 0.4914 0.0228  -0.0206 0.0424  35  LEU B CA  
4369 C C   . LEU B 49  ? 0.2971 0.2538 0.4616 0.0260  -0.0249 0.0483  35  LEU B C   
4370 O O   . LEU B 49  ? 0.3235 0.2760 0.4940 0.0288  -0.0244 0.0499  35  LEU B O   
4371 C CB  . LEU B 49  ? 0.3101 0.2712 0.4759 0.0187  -0.0134 0.0415  35  LEU B CB  
4372 C CG  . LEU B 49  ? 0.3443 0.3118 0.5193 0.0168  -0.0092 0.0364  35  LEU B CG  
4373 C CD1 . LEU B 49  ? 0.2928 0.2581 0.4633 0.0127  -0.0036 0.0355  35  LEU B CD1 
4374 C CD2 . LEU B 49  ? 0.3018 0.2687 0.4864 0.0189  -0.0083 0.0353  35  LEU B CD2 
4375 N N   . ASP B 50  ? 0.3336 0.2864 0.4852 0.0256  -0.0291 0.0516  36  ASP B N   
4376 C CA  . ASP B 50  ? 0.3889 0.3332 0.5336 0.0291  -0.0346 0.0579  36  ASP B CA  
4377 C C   . ASP B 50  ? 0.4299 0.3795 0.5889 0.0347  -0.0410 0.0583  36  ASP B C   
4378 O O   . ASP B 50  ? 0.4738 0.4164 0.6346 0.0387  -0.0429 0.0625  36  ASP B O   
4379 C CB  . ASP B 50  ? 0.3624 0.3031 0.4902 0.0277  -0.0394 0.0607  36  ASP B CB  
4380 C CG  . ASP B 50  ? 0.5023 0.4352 0.6145 0.0229  -0.0323 0.0613  36  ASP B CG  
4381 O OD1 . ASP B 50  ? 0.4868 0.4164 0.6019 0.0208  -0.0245 0.0609  36  ASP B OD1 
4382 O OD2 . ASP B 50  ? 0.5313 0.4615 0.6287 0.0209  -0.0344 0.0620  36  ASP B OD2 
4383 N N   . HIS B 51  ? 0.3843 0.3462 0.5543 0.0352  -0.0440 0.0540  37  HIS B N   
4384 C CA  . HIS B 51  ? 0.3732 0.3419 0.5595 0.0405  -0.0491 0.0539  37  HIS B CA  
4385 C C   . HIS B 51  ? 0.3545 0.3233 0.5536 0.0423  -0.0427 0.0514  37  HIS B C   
4386 O O   . HIS B 51  ? 0.3943 0.3628 0.6039 0.0476  -0.0451 0.0530  37  HIS B O   
4387 C CB  . HIS B 51  ? 0.3332 0.3151 0.5283 0.0396  -0.0532 0.0497  37  HIS B CB  
4388 C CG  . HIS B 51  ? 0.3610 0.3426 0.5441 0.0381  -0.0609 0.0516  37  HIS B CG  
4389 N ND1 . HIS B 51  ? 0.3210 0.3054 0.5073 0.0419  -0.0714 0.0547  37  HIS B ND1 
4390 C CD2 . HIS B 51  ? 0.4016 0.3797 0.5688 0.0332  -0.0598 0.0507  37  HIS B CD2 
4391 C CE1 . HIS B 51  ? 0.3840 0.3663 0.5555 0.0390  -0.0768 0.0555  37  HIS B CE1 
4392 N NE2 . HIS B 51  ? 0.4332 0.4114 0.5926 0.0338  -0.0694 0.0529  37  HIS B NE2 
4393 N N   . VAL B 52  ? 0.3440 0.3129 0.5421 0.0381  -0.0347 0.0475  38  VAL B N   
4394 C CA  . VAL B 52  ? 0.3442 0.3112 0.5511 0.0392  -0.0288 0.0450  38  VAL B CA  
4395 C C   . VAL B 52  ? 0.3665 0.3204 0.5683 0.0412  -0.0279 0.0495  38  VAL B C   
4396 O O   . VAL B 52  ? 0.3889 0.3400 0.5998 0.0454  -0.0274 0.0495  38  VAL B O   
4397 C CB  . VAL B 52  ? 0.3413 0.3107 0.5466 0.0340  -0.0218 0.0402  38  VAL B CB  
4398 C CG1 . VAL B 52  ? 0.2715 0.2376 0.4834 0.0345  -0.0163 0.0374  38  VAL B CG1 
4399 C CG2 . VAL B 52  ? 0.2637 0.2446 0.4742 0.0322  -0.0225 0.0361  38  VAL B CG2 
4400 N N   . ILE B 53  ? 0.3446 0.2897 0.5316 0.0382  -0.0274 0.0534  39  ILE B N   
4401 C CA  . ILE B 53  ? 0.4534 0.3848 0.6340 0.0394  -0.0263 0.0583  39  ILE B CA  
4402 C C   . ILE B 53  ? 0.5590 0.4866 0.7425 0.0460  -0.0337 0.0633  39  ILE B C   
4403 O O   . ILE B 53  ? 0.4675 0.3872 0.6561 0.0497  -0.0329 0.0651  39  ILE B O   
4404 C CB  . ILE B 53  ? 0.4656 0.3891 0.6293 0.0344  -0.0238 0.0618  39  ILE B CB  
4405 C CG1 . ILE B 53  ? 0.4240 0.3495 0.5877 0.0285  -0.0158 0.0573  39  ILE B CG1 
4406 C CG2 . ILE B 53  ? 0.5317 0.4401 0.6867 0.0359  -0.0243 0.0686  39  ILE B CG2 
4407 C CD1 . ILE B 53  ? 0.4154 0.3410 0.5904 0.0285  -0.0115 0.0531  39  ILE B CD1 
4408 N N   . ASP B 54  ? 0.5021 0.4352 0.6830 0.0478  -0.0413 0.0654  40  ASP B N   
4409 C CA  . ASP B 54  ? 0.5570 0.4868 0.7400 0.0541  -0.0499 0.0709  40  ASP B CA  
4410 C C   . ASP B 54  ? 0.4827 0.4208 0.6869 0.0602  -0.0519 0.0681  40  ASP B C   
4411 O O   . ASP B 54  ? 0.4961 0.4298 0.7054 0.0665  -0.0576 0.0725  40  ASP B O   
4412 C CB  . ASP B 54  ? 0.6188 0.5522 0.7920 0.0537  -0.0585 0.0736  40  ASP B CB  
4413 C CG  . ASP B 54  ? 0.7821 0.7031 0.9321 0.0498  -0.0578 0.0786  40  ASP B CG  
4414 O OD1 . ASP B 54  ? 0.8294 0.7385 0.9723 0.0482  -0.0516 0.0812  40  ASP B OD1 
4415 O OD2 . ASP B 54  ? 0.8729 0.7958 1.0114 0.0480  -0.0632 0.0796  40  ASP B OD2 
4416 N N   . SER B 55  ? 0.3866 0.3363 0.6031 0.0585  -0.0473 0.0611  41  SER B N   
4417 C CA  . SER B 55  ? 0.4394 0.3978 0.6762 0.0640  -0.0480 0.0581  41  SER B CA  
4418 C C   . SER B 55  ? 0.5832 0.5317 0.8259 0.0679  -0.0434 0.0583  41  SER B C   
4419 O O   . SER B 55  ? 0.4933 0.4332 0.7287 0.0642  -0.0362 0.0568  41  SER B O   
4420 C CB  . SER B 55  ? 0.4807 0.4523 0.7268 0.0605  -0.0430 0.0507  41  SER B CB  
4421 O OG  . SER B 55  ? 0.5236 0.5001 0.7873 0.0647  -0.0394 0.0469  41  SER B OG  
4422 N N   . PRO B 56  ? 0.4924 0.4417 0.7489 0.0755  -0.0474 0.0600  42  PRO B N   
4423 C CA  . PRO B 56  ? 0.4908 0.4306 0.7543 0.0796  -0.0421 0.0591  42  PRO B CA  
4424 C C   . PRO B 56  ? 0.4123 0.3597 0.6889 0.0792  -0.0337 0.0509  42  PRO B C   
4425 O O   . PRO B 56  ? 0.5069 0.4458 0.7878 0.0817  -0.0281 0.0487  42  PRO B O   
4426 C CB  . PRO B 56  ? 0.4893 0.4278 0.7636 0.0886  -0.0503 0.0643  42  PRO B CB  
4427 C CG  . PRO B 56  ? 0.4331 0.3854 0.7111 0.0891  -0.0596 0.0659  42  PRO B CG  
4428 C CD  . PRO B 56  ? 0.4561 0.4162 0.7246 0.0807  -0.0567 0.0620  42  PRO B CD  
4429 N N   . ASP B 57  ? 0.3504 0.3122 0.6322 0.0758  -0.0324 0.0461  43  ASP B N   
4430 C CA  . ASP B 57  ? 0.3390 0.3081 0.6326 0.0756  -0.0245 0.0388  43  ASP B CA  
4431 C C   . ASP B 57  ? 0.3649 0.3333 0.6480 0.0680  -0.0173 0.0340  43  ASP B C   
4432 O O   . ASP B 57  ? 0.4054 0.3746 0.6936 0.0675  -0.0099 0.0283  43  ASP B O   
4433 C CB  . ASP B 57  ? 0.3522 0.3385 0.6622 0.0777  -0.0274 0.0367  43  ASP B CB  
4434 C CG  . ASP B 57  ? 0.4710 0.4604 0.7942 0.0856  -0.0359 0.0412  43  ASP B CG  
4435 O OD1 . ASP B 57  ? 0.4674 0.4493 0.7981 0.0920  -0.0346 0.0422  43  ASP B OD1 
4436 O OD2 . ASP B 57  ? 0.4670 0.4660 0.7931 0.0855  -0.0441 0.0437  43  ASP B OD2 
4437 N N   . ILE B 58  ? 0.3362 0.3028 0.6047 0.0622  -0.0192 0.0362  44  ILE B N   
4438 C CA  . ILE B 58  ? 0.3502 0.3172 0.6099 0.0553  -0.0135 0.0321  44  ILE B CA  
4439 C C   . ILE B 58  ? 0.3945 0.3490 0.6395 0.0516  -0.0126 0.0350  44  ILE B C   
4440 O O   . ILE B 58  ? 0.3087 0.2582 0.5459 0.0518  -0.0173 0.0407  44  ILE B O   
4441 C CB  . ILE B 58  ? 0.3688 0.3477 0.6275 0.0514  -0.0156 0.0309  44  ILE B CB  
4442 C CG1 . ILE B 58  ? 0.3573 0.3365 0.6081 0.0450  -0.0099 0.0269  44  ILE B CG1 
4443 C CG2 . ILE B 58  ? 0.5476 0.5264 0.7984 0.0509  -0.0230 0.0362  44  ILE B CG2 
4444 C CD1 . ILE B 58  ? 0.4814 0.4677 0.7404 0.0445  -0.0046 0.0211  44  ILE B CD1 
4445 N N   . CYS B 59  ? 0.2860 0.2353 0.5272 0.0480  -0.0064 0.0311  45  CYS B N   
4446 C CA  . CYS B 59  ? 0.4042 0.3427 0.6342 0.0438  -0.0047 0.0330  45  CYS B CA  
4447 C C   . CYS B 59  ? 0.4332 0.3769 0.6563 0.0372  -0.0026 0.0306  45  CYS B C   
4448 O O   . CYS B 59  ? 0.3347 0.2841 0.5607 0.0353  0.0006  0.0254  45  CYS B O   
4449 C CB  . CYS B 59  ? 0.3750 0.3027 0.6066 0.0445  -0.0002 0.0303  45  CYS B CB  
4450 S SG  . CYS B 59  ? 0.5838 0.4992 0.8043 0.0382  0.0026  0.0315  45  CYS B SG  
4451 N N   . TRP B 60  ? 0.3633 0.3048 0.5772 0.0339  -0.0042 0.0344  46  TRP B N   
4452 C CA  . TRP B 60  ? 0.3974 0.3431 0.6059 0.0281  -0.0019 0.0322  46  TRP B CA  
4453 C C   . TRP B 60  ? 0.3495 0.2892 0.5569 0.0244  0.0025  0.0293  46  TRP B C   
4454 O O   . TRP B 60  ? 0.4216 0.3508 0.6272 0.0243  0.0037  0.0311  46  TRP B O   
4455 C CB  . TRP B 60  ? 0.3101 0.2546 0.5093 0.0259  -0.0038 0.0367  46  TRP B CB  
4456 C CG  . TRP B 60  ? 0.3822 0.3300 0.5772 0.0203  -0.0008 0.0347  46  TRP B CG  
4457 C CD1 . TRP B 60  ? 0.3403 0.2824 0.5298 0.0162  0.0023  0.0362  46  TRP B CD1 
4458 C CD2 . TRP B 60  ? 0.3056 0.2631 0.5026 0.0185  -0.0004 0.0309  46  TRP B CD2 
4459 N NE1 . TRP B 60  ? 0.3597 0.3083 0.5490 0.0125  0.0043  0.0335  46  TRP B NE1 
4460 C CE2 . TRP B 60  ? 0.3250 0.2824 0.5182 0.0139  0.0025  0.0304  46  TRP B CE2 
4461 C CE3 . TRP B 60  ? 0.3191 0.2853 0.5216 0.0201  -0.0020 0.0281  46  TRP B CE3 
4462 C CZ2 . TRP B 60  ? 0.2712 0.2362 0.4654 0.0116  0.0032  0.0273  46  TRP B CZ2 
4463 C CZ3 . TRP B 60  ? 0.2826 0.2554 0.4848 0.0173  -0.0009 0.0253  46  TRP B CZ3 
4464 C CH2 . TRP B 60  ? 0.2912 0.2631 0.4891 0.0134  0.0014  0.0249  46  TRP B CH2 
4465 N N   . VAL B 61  ? 0.3354 0.2810 0.5437 0.0212  0.0045  0.0247  47  VAL B N   
4466 C CA  . VAL B 61  ? 0.3498 0.2912 0.5570 0.0170  0.0074  0.0215  47  VAL B CA  
4467 C C   . VAL B 61  ? 0.3151 0.2629 0.5195 0.0125  0.0076  0.0209  47  VAL B C   
4468 O O   . VAL B 61  ? 0.3239 0.2791 0.5295 0.0119  0.0074  0.0179  47  VAL B O   
4469 C CB  . VAL B 61  ? 0.3473 0.2885 0.5579 0.0180  0.0093  0.0160  47  VAL B CB  
4470 C CG1 . VAL B 61  ? 0.2784 0.2153 0.4866 0.0131  0.0110  0.0125  47  VAL B CG1 
4471 C CG2 . VAL B 61  ? 0.3062 0.2410 0.5210 0.0230  0.0099  0.0162  47  VAL B CG2 
4472 N N   . GLY B 62  ? 0.2696 0.2143 0.4707 0.0096  0.0084  0.0239  48  GLY B N   
4473 C CA  . GLY B 62  ? 0.3465 0.2971 0.5469 0.0056  0.0092  0.0231  48  GLY B CA  
4474 C C   . GLY B 62  ? 0.3582 0.3096 0.5619 0.0022  0.0100  0.0187  48  GLY B C   
4475 O O   . GLY B 62  ? 0.3314 0.2759 0.5362 0.0007  0.0109  0.0174  48  GLY B O   
4476 N N   . CYS B 63  ? 0.3126 0.2718 0.5173 0.0010  0.0092  0.0165  49  CYS B N   
4477 C CA  . CYS B 63  ? 0.3217 0.2822 0.5287 -0.0020 0.0085  0.0125  49  CYS B CA  
4478 C C   . CYS B 63  ? 0.3360 0.3012 0.5462 -0.0056 0.0088  0.0130  49  CYS B C   
4479 O O   . CYS B 63  ? 0.3034 0.2709 0.5134 -0.0056 0.0104  0.0158  49  CYS B O   
4480 C CB  . CYS B 63  ? 0.2852 0.2501 0.4909 -0.0002 0.0071  0.0097  49  CYS B CB  
4481 S SG  . CYS B 63  ? 0.3528 0.3130 0.5571 0.0038  0.0080  0.0081  49  CYS B SG  
4482 N N   . ALA B 64  ? 0.2839 0.2502 0.4973 -0.0086 0.0072  0.0098  50  ALA B N   
4483 C CA  . ALA B 64  ? 0.3579 0.3293 0.5773 -0.0120 0.0072  0.0100  50  ALA B CA  
4484 C C   . ALA B 64  ? 0.3050 0.2848 0.5256 -0.0106 0.0058  0.0098  50  ALA B C   
4485 O O   . ALA B 64  ? 0.3289 0.3137 0.5549 -0.0119 0.0071  0.0108  50  ALA B O   
4486 C CB  . ALA B 64  ? 0.2441 0.2138 0.4678 -0.0160 0.0050  0.0068  50  ALA B CB  
4487 N N   . ASN B 65  ? 0.2843 0.2652 0.5004 -0.0081 0.0037  0.0085  51  ASN B N   
4488 C CA  . ASN B 65  ? 0.2571 0.2440 0.4730 -0.0063 0.0030  0.0090  51  ASN B CA  
4489 C C   . ASN B 65  ? 0.2834 0.2692 0.4932 -0.0036 0.0024  0.0085  51  ASN B C   
4490 O O   . ASN B 65  ? 0.2706 0.2519 0.4773 -0.0030 0.0026  0.0072  51  ASN B O   
4491 C CB  . ASN B 65  ? 0.2207 0.2125 0.4416 -0.0079 0.0000  0.0076  51  ASN B CB  
4492 C CG  . ASN B 65  ? 0.3126 0.3022 0.5302 -0.0088 -0.0041 0.0049  51  ASN B CG  
4493 O OD1 . ASN B 65  ? 0.2695 0.2552 0.4799 -0.0075 -0.0041 0.0039  51  ASN B OD1 
4494 N ND2 . ASN B 65  ? 0.2261 0.2186 0.4492 -0.0112 -0.0077 0.0036  51  ASN B ND2 
4495 N N   . GLU B 66  ? 0.2169 0.2066 0.4258 -0.0020 0.0023  0.0093  52  GLU B N   
4496 C CA  . GLU B 66  ? 0.2328 0.2223 0.4376 0.0001  0.0025  0.0091  52  GLU B CA  
4497 C C   . GLU B 66  ? 0.2607 0.2484 0.4619 -0.0002 0.0012  0.0068  52  GLU B C   
4498 O O   . GLU B 66  ? 0.2559 0.2418 0.4545 0.0011  0.0026  0.0059  52  GLU B O   
4499 C CB  . GLU B 66  ? 0.2142 0.2075 0.4188 0.0012  0.0027  0.0102  52  GLU B CB  
4500 C CG  . GLU B 66  ? 0.2114 0.2053 0.4162 0.0018  0.0043  0.0121  52  GLU B CG  
4501 C CD  . GLU B 66  ? 0.3374 0.3324 0.5451 0.0004  0.0056  0.0128  52  GLU B CD  
4502 O OE1 . GLU B 66  ? 0.2421 0.2386 0.4540 -0.0010 0.0046  0.0117  52  GLU B OE1 
4503 O OE2 . GLU B 66  ? 0.2795 0.2741 0.4855 0.0006  0.0075  0.0143  52  GLU B OE2 
4504 N N   . LEU B 67  ? 0.2702 0.2585 0.4713 -0.0018 -0.0014 0.0058  53  LEU B N   
4505 C CA  . LEU B 67  ? 0.2252 0.2103 0.4200 -0.0025 -0.0029 0.0038  53  LEU B CA  
4506 C C   . LEU B 67  ? 0.2702 0.2498 0.4622 -0.0031 -0.0017 0.0014  53  LEU B C   
4507 O O   . LEU B 67  ? 0.3257 0.3022 0.5123 -0.0022 0.0003  -0.0001 53  LEU B O   
4508 C CB  . LEU B 67  ? 0.2389 0.2251 0.4339 -0.0040 -0.0073 0.0035  53  LEU B CB  
4509 C CG  . LEU B 67  ? 0.3203 0.3021 0.5058 -0.0048 -0.0094 0.0019  53  LEU B CG  
4510 C CD1 . LEU B 67  ? 0.2426 0.2232 0.4222 -0.0034 -0.0064 0.0026  53  LEU B CD1 
4511 C CD2 . LEU B 67  ? 0.2552 0.2381 0.4408 -0.0060 -0.0152 0.0022  53  LEU B CD2 
4512 N N   . ASN B 68  ? 0.2941 0.2721 0.4901 -0.0046 -0.0022 0.0011  54  ASN B N   
4513 C CA  . ASN B 68  ? 0.2481 0.2195 0.4418 -0.0051 -0.0009 -0.0013 54  ASN B CA  
4514 C C   . ASN B 68  ? 0.2394 0.2093 0.4333 -0.0019 0.0030  -0.0005 54  ASN B C   
4515 O O   . ASN B 68  ? 0.2829 0.2479 0.4735 -0.0009 0.0050  -0.0030 54  ASN B O   
4516 C CB  . ASN B 68  ? 0.2423 0.2120 0.4413 -0.0077 -0.0018 -0.0014 54  ASN B CB  
4517 C CG  . ASN B 68  ? 0.3348 0.3068 0.5358 -0.0110 -0.0063 -0.0027 54  ASN B CG  
4518 O OD1 . ASN B 68  ? 0.3382 0.3127 0.5360 -0.0109 -0.0093 -0.0031 54  ASN B OD1 
4519 N ND2 . ASN B 68  ? 0.3386 0.3097 0.5457 -0.0140 -0.0071 -0.0031 54  ASN B ND2 
4520 N N   . ALA B 69  ? 0.2748 0.2488 0.4729 -0.0002 0.0039  0.0027  55  ALA B N   
4521 C CA  . ALA B 69  ? 0.2442 0.2179 0.4437 0.0030  0.0062  0.0038  55  ALA B CA  
4522 C C   . ALA B 69  ? 0.2725 0.2478 0.4697 0.0046  0.0078  0.0021  55  ALA B C   
4523 O O   . ALA B 69  ? 0.2615 0.2346 0.4599 0.0069  0.0102  0.0009  55  ALA B O   
4524 C CB  . ALA B 69  ? 0.2374 0.2153 0.4398 0.0041  0.0058  0.0074  55  ALA B CB  
4525 N N   . SER B 70  ? 0.2807 0.2595 0.4752 0.0034  0.0069  0.0020  56  SER B N   
4526 C CA  . SER B 70  ? 0.3053 0.2850 0.4972 0.0041  0.0092  0.0007  56  SER B CA  
4527 C C   . SER B 70  ? 0.2846 0.2582 0.4701 0.0034  0.0111  -0.0029 56  SER B C   
4528 O O   . SER B 70  ? 0.3135 0.2862 0.4986 0.0048  0.0151  -0.0046 56  SER B O   
4529 C CB  . SER B 70  ? 0.2734 0.2566 0.4631 0.0029  0.0078  0.0020  56  SER B CB  
4530 O OG  . SER B 70  ? 0.2530 0.2338 0.4374 0.0007  0.0051  0.0014  56  SER B OG  
4531 N N   . TYR B 71  ? 0.2860 0.2553 0.4668 0.0010  0.0084  -0.0043 57  TYR B N   
4532 C CA  . TYR B 71  ? 0.2954 0.2574 0.4687 -0.0001 0.0097  -0.0083 57  TYR B CA  
4533 C C   . TYR B 71  ? 0.3157 0.2736 0.4926 0.0021  0.0132  -0.0101 57  TYR B C   
4534 O O   . TYR B 71  ? 0.3441 0.2976 0.5169 0.0031  0.0174  -0.0134 57  TYR B O   
4535 C CB  . TYR B 71  ? 0.3827 0.3414 0.5519 -0.0034 0.0049  -0.0095 57  TYR B CB  
4536 C CG  . TYR B 71  ? 0.2732 0.2342 0.4376 -0.0053 0.0006  -0.0083 57  TYR B CG  
4537 C CD1 . TYR B 71  ? 0.2723 0.2344 0.4312 -0.0047 0.0021  -0.0073 57  TYR B CD1 
4538 C CD2 . TYR B 71  ? 0.3327 0.2945 0.4987 -0.0077 -0.0050 -0.0082 57  TYR B CD2 
4539 C CE1 . TYR B 71  ? 0.2640 0.2268 0.4180 -0.0060 -0.0022 -0.0056 57  TYR B CE1 
4540 C CE2 . TYR B 71  ? 0.2904 0.2543 0.4532 -0.0088 -0.0097 -0.0068 57  TYR B CE2 
4541 C CZ  . TYR B 71  ? 0.3125 0.2762 0.4686 -0.0077 -0.0084 -0.0054 57  TYR B CZ  
4542 O OH  . TYR B 71  ? 0.3446 0.3091 0.4972 -0.0084 -0.0134 -0.0035 57  TYR B OH  
4543 N N   . ALA B 72  ? 0.2656 0.2240 0.4496 0.0029  0.0120  -0.0081 58  ALA B N   
4544 C CA  . ALA B 72  ? 0.3287 0.2819 0.5164 0.0054  0.0147  -0.0091 58  ALA B CA  
4545 C C   . ALA B 72  ? 0.3033 0.2600 0.4959 0.0095  0.0185  -0.0087 58  ALA B C   
4546 O O   . ALA B 72  ? 0.3002 0.2523 0.4936 0.0118  0.0224  -0.0116 58  ALA B O   
4547 C CB  . ALA B 72  ? 0.2584 0.2110 0.4518 0.0052  0.0125  -0.0059 58  ALA B CB  
4548 N N   . ALA B 73  ? 0.2578 0.2228 0.4546 0.0104  0.0176  -0.0056 59  ALA B N   
4549 C CA  . ALA B 73  ? 0.3347 0.3046 0.5379 0.0137  0.0206  -0.0053 59  ALA B CA  
4550 C C   . ALA B 73  ? 0.2613 0.2297 0.4603 0.0134  0.0256  -0.0092 59  ALA B C   
4551 O O   . ALA B 73  ? 0.3720 0.3405 0.5764 0.0165  0.0300  -0.0111 59  ALA B O   
4552 C CB  . ALA B 73  ? 0.2386 0.2170 0.4457 0.0135  0.0181  -0.0018 59  ALA B CB  
4553 N N   . ASP B 74  ? 0.2766 0.2433 0.4658 0.0099  0.0252  -0.0104 60  ASP B N   
4554 C CA  . ASP B 74  ? 0.2741 0.2374 0.4558 0.0090  0.0302  -0.0139 60  ASP B CA  
4555 C C   . ASP B 74  ? 0.3638 0.3186 0.5424 0.0103  0.0341  -0.0185 60  ASP B C   
4556 O O   . ASP B 74  ? 0.3161 0.2705 0.4970 0.0125  0.0405  -0.0212 60  ASP B O   
4557 C CB  . ASP B 74  ? 0.2692 0.2301 0.4389 0.0050  0.0274  -0.0137 60  ASP B CB  
4558 C CG  . ASP B 74  ? 0.3846 0.3421 0.5445 0.0036  0.0327  -0.0162 60  ASP B CG  
4559 O OD1 . ASP B 74  ? 0.3558 0.3063 0.5095 0.0039  0.0369  -0.0204 60  ASP B OD1 
4560 O OD2 . ASP B 74  ? 0.2772 0.2380 0.4346 0.0021  0.0328  -0.0139 60  ASP B OD2 
4561 N N   . GLY B 75  ? 0.3467 0.2948 0.5211 0.0088  0.0306  -0.0196 61  GLY B N   
4562 C CA  . GLY B 75  ? 0.2946 0.2331 0.4656 0.0097  0.0340  -0.0244 61  GLY B CA  
4563 C C   . GLY B 75  ? 0.3110 0.2502 0.4942 0.0149  0.0376  -0.0243 61  GLY B C   
4564 O O   . GLY B 75  ? 0.3039 0.2378 0.4868 0.0172  0.0435  -0.0285 61  GLY B O   
4565 N N   . TYR B 76  ? 0.2950 0.2404 0.4888 0.0169  0.0339  -0.0194 62  TYR B N   
4566 C CA  . TYR B 76  ? 0.2883 0.2356 0.4944 0.0223  0.0360  -0.0182 62  TYR B CA  
4567 C C   . TYR B 76  ? 0.3432 0.2967 0.5553 0.0251  0.0419  -0.0201 62  TYR B C   
4568 O O   . TYR B 76  ? 0.2907 0.2413 0.5087 0.0290  0.0470  -0.0230 62  TYR B O   
4569 C CB  . TYR B 76  ? 0.2717 0.2252 0.4852 0.0233  0.0303  -0.0123 62  TYR B CB  
4570 C CG  . TYR B 76  ? 0.3561 0.3104 0.5811 0.0288  0.0300  -0.0099 62  TYR B CG  
4571 C CD1 . TYR B 76  ? 0.3110 0.2744 0.5468 0.0325  0.0310  -0.0087 62  TYR B CD1 
4572 C CD2 . TYR B 76  ? 0.3100 0.2557 0.5354 0.0302  0.0281  -0.0084 62  TYR B CD2 
4573 C CE1 . TYR B 76  ? 0.2692 0.2337 0.5161 0.0379  0.0294  -0.0061 62  TYR B CE1 
4574 C CE2 . TYR B 76  ? 0.2959 0.2413 0.5310 0.0356  0.0270  -0.0055 62  TYR B CE2 
4575 C CZ  . TYR B 76  ? 0.3774 0.3325 0.6233 0.0397  0.0272  -0.0043 62  TYR B CZ  
4576 O OH  . TYR B 76  ? 0.4094 0.3646 0.6655 0.0454  0.0249  -0.0011 62  TYR B OH  
4577 N N   . ALA B 77  ? 0.2962 0.2577 0.5074 0.0228  0.0418  -0.0185 63  ALA B N   
4578 C CA  . ALA B 77  ? 0.3280 0.2964 0.5463 0.0246  0.0477  -0.0199 63  ALA B CA  
4579 C C   . ALA B 77  ? 0.3353 0.2968 0.5458 0.0242  0.0559  -0.0257 63  ALA B C   
4580 O O   . ALA B 77  ? 0.3283 0.2933 0.5476 0.0272  0.0628  -0.0280 63  ALA B O   
4581 C CB  . ALA B 77  ? 0.2668 0.2435 0.4843 0.0214  0.0458  -0.0170 63  ALA B CB  
4582 N N   . ARG B 78  ? 0.2979 0.2496 0.4922 0.0204  0.0554  -0.0283 64  ARG B N   
4583 C CA  . ARG B 78  ? 0.3138 0.2568 0.4979 0.0199  0.0630  -0.0343 64  ARG B CA  
4584 C C   . ARG B 78  ? 0.3374 0.2734 0.5271 0.0243  0.0667  -0.0382 64  ARG B C   
4585 O O   . ARG B 78  ? 0.3799 0.3083 0.5627 0.0247  0.0742  -0.0439 64  ARG B O   
4586 C CB  . ARG B 78  ? 0.3600 0.2941 0.5241 0.0145  0.0598  -0.0360 64  ARG B CB  
4587 C CG  . ARG B 78  ? 0.3504 0.2896 0.5076 0.0106  0.0568  -0.0324 64  ARG B CG  
4588 C CD  . ARG B 78  ? 0.3874 0.3173 0.5251 0.0059  0.0532  -0.0342 64  ARG B CD  
4589 N NE  . ARG B 78  ? 0.3289 0.2625 0.4599 0.0026  0.0498  -0.0305 64  ARG B NE  
4590 C CZ  . ARG B 78  ? 0.4532 0.3799 0.5663 -0.0009 0.0501  -0.0317 64  ARG B CZ  
4591 N NH1 . ARG B 78  ? 0.3551 0.2709 0.4539 -0.0021 0.0539  -0.0371 64  ARG B NH1 
4592 N NH2 . ARG B 78  ? 0.4308 0.3606 0.5392 -0.0032 0.0462  -0.0275 64  ARG B NH2 
4593 N N   . CYS B 79  ? 0.3354 0.2724 0.5363 0.0275  0.0618  -0.0352 65  CYS B N   
4594 C CA  . CYS B 79  ? 0.3369 0.2670 0.5450 0.0324  0.0650  -0.0380 65  CYS B CA  
4595 C C   . CYS B 79  ? 0.3462 0.2857 0.5747 0.0389  0.0668  -0.0357 65  CYS B C   
4596 O O   . CYS B 79  ? 0.3528 0.2888 0.5887 0.0437  0.0731  -0.0394 65  CYS B O   
4597 C CB  . CYS B 79  ? 0.4116 0.3334 0.6168 0.0315  0.0583  -0.0364 65  CYS B CB  
4598 S SG  . CYS B 79  ? 0.4007 0.3114 0.5849 0.0241  0.0553  -0.0400 65  CYS B SG  
4599 N N   . LYS B 80  ? 0.3606 0.3117 0.5983 0.0392  0.0613  -0.0298 66  LYS B N   
4600 C CA  . LYS B 80  ? 0.4069 0.3676 0.6643 0.0451  0.0610  -0.0272 66  LYS B CA  
4601 C C   . LYS B 80  ? 0.4008 0.3750 0.6671 0.0447  0.0642  -0.0268 66  LYS B C   
4602 O O   . LYS B 80  ? 0.4295 0.4129 0.7139 0.0495  0.0643  -0.0253 66  LYS B O   
4603 C CB  . LYS B 80  ? 0.4044 0.3674 0.6666 0.0463  0.0513  -0.0207 66  LYS B CB  
4604 C CG  . LYS B 80  ? 0.4670 0.4171 0.7196 0.0452  0.0478  -0.0201 66  LYS B CG  
4605 C CD  . LYS B 80  ? 0.4873 0.4317 0.7502 0.0517  0.0473  -0.0191 66  LYS B CD  
4606 C CE  . LYS B 80  ? 0.4867 0.4378 0.7588 0.0545  0.0395  -0.0119 66  LYS B CE  
4607 N NZ  . LYS B 80  ? 0.7077 0.6498 0.9855 0.0600  0.0373  -0.0095 66  LYS B NZ  
4608 N N   . GLY B 81  ? 0.3632 0.3385 0.6180 0.0391  0.0666  -0.0279 67  GLY B N   
4609 C CA  . GLY B 81  ? 0.4031 0.3899 0.6655 0.0377  0.0703  -0.0275 67  GLY B CA  
4610 C C   . GLY B 81  ? 0.3615 0.3580 0.6281 0.0354  0.0624  -0.0220 67  GLY B C   
4611 O O   . GLY B 81  ? 0.3533 0.3590 0.6260 0.0335  0.0650  -0.0215 67  GLY B O   
4612 N N   . PHE B 82  ? 0.3238 0.3179 0.5869 0.0352  0.0536  -0.0181 68  PHE B N   
4613 C CA  . PHE B 82  ? 0.2891 0.2911 0.5553 0.0334  0.0461  -0.0132 68  PHE B CA  
4614 C C   . PHE B 82  ? 0.3159 0.3112 0.5732 0.0325  0.0388  -0.0101 68  PHE B C   
4615 O O   . PHE B 82  ? 0.3033 0.2905 0.5587 0.0349  0.0384  -0.0107 68  PHE B O   
4616 C CB  . PHE B 82  ? 0.2941 0.3074 0.5800 0.0376  0.0438  -0.0112 68  PHE B CB  
4617 C CG  . PHE B 82  ? 0.3387 0.3617 0.6284 0.0347  0.0389  -0.0081 68  PHE B CG  
4618 C CD1 . PHE B 82  ? 0.2654 0.2887 0.5522 0.0342  0.0301  -0.0039 68  PHE B CD1 
4619 C CD2 . PHE B 82  ? 0.4538 0.4852 0.7501 0.0321  0.0436  -0.0097 68  PHE B CD2 
4620 C CE1 . PHE B 82  ? 0.2889 0.3200 0.5782 0.0314  0.0256  -0.0017 68  PHE B CE1 
4621 C CE2 . PHE B 82  ? 0.2827 0.3222 0.5827 0.0290  0.0390  -0.0072 68  PHE B CE2 
4622 C CZ  . PHE B 82  ? 0.3664 0.4057 0.6629 0.0288  0.0298  -0.0035 68  PHE B CZ  
4623 N N   . ALA B 83  ? 0.2532 0.2515 0.5051 0.0289  0.0337  -0.0070 69  ALA B N   
4624 C CA  . ALA B 83  ? 0.2966 0.2899 0.5412 0.0277  0.0275  -0.0040 69  ALA B CA  
4625 C C   . ALA B 83  ? 0.3537 0.3537 0.5987 0.0256  0.0222  -0.0004 69  ALA B C   
4626 O O   . ALA B 83  ? 0.3375 0.3447 0.5863 0.0240  0.0232  -0.0007 69  ALA B O   
4627 C CB  . ALA B 83  ? 0.2811 0.2654 0.5117 0.0241  0.0286  -0.0060 69  ALA B CB  
4628 N N   . ALA B 84  ? 0.2753 0.2722 0.5161 0.0253  0.0170  0.0028  70  ALA B N   
4629 C CA  . ALA B 84  ? 0.2888 0.2904 0.5282 0.0234  0.0123  0.0058  70  ALA B CA  
4630 C C   . ALA B 84  ? 0.3804 0.3763 0.6096 0.0206  0.0101  0.0073  70  ALA B C   
4631 O O   . ALA B 84  ? 0.2857 0.2746 0.5118 0.0211  0.0102  0.0076  70  ALA B O   
4632 C CB  . ALA B 84  ? 0.3094 0.3154 0.5569 0.0267  0.0077  0.0088  70  ALA B CB  
4633 N N   . LEU B 85  ? 0.2814 0.2803 0.5066 0.0175  0.0086  0.0080  71  LEU B N   
4634 C CA  . LEU B 85  ? 0.3628 0.3582 0.5804 0.0149  0.0069  0.0092  71  LEU B CA  
4635 C C   . LEU B 85  ? 0.3115 0.3105 0.5287 0.0144  0.0035  0.0118  71  LEU B C   
4636 O O   . LEU B 85  ? 0.2995 0.3040 0.5200 0.0143  0.0025  0.0115  71  LEU B O   
4637 C CB  . LEU B 85  ? 0.3862 0.3809 0.5987 0.0118  0.0087  0.0071  71  LEU B CB  
4638 C CG  . LEU B 85  ? 0.3770 0.3716 0.5848 0.0092  0.0068  0.0083  71  LEU B CG  
4639 C CD1 . LEU B 85  ? 0.3241 0.3139 0.5297 0.0085  0.0061  0.0089  71  LEU B CD1 
4640 C CD2 . LEU B 85  ? 0.3739 0.3688 0.5779 0.0070  0.0077  0.0068  71  LEU B CD2 
4641 N N   . LEU B 86  ? 0.2575 0.2527 0.4703 0.0140  0.0019  0.0140  72  LEU B N   
4642 C CA  . LEU B 86  ? 0.2888 0.2857 0.4984 0.0132  -0.0006 0.0160  72  LEU B CA  
4643 C C   . LEU B 86  ? 0.3376 0.3326 0.5420 0.0104  0.0006  0.0159  72  LEU B C   
4644 O O   . LEU B 86  ? 0.2798 0.2706 0.4826 0.0096  0.0020  0.0164  72  LEU B O   
4645 C CB  . LEU B 86  ? 0.2545 0.2483 0.4627 0.0155  -0.0032 0.0193  72  LEU B CB  
4646 C CG  . LEU B 86  ? 0.3068 0.2999 0.5081 0.0142  -0.0053 0.0213  72  LEU B CG  
4647 C CD1 . LEU B 86  ? 0.2262 0.2252 0.4290 0.0142  -0.0085 0.0205  72  LEU B CD1 
4648 C CD2 . LEU B 86  ? 0.3191 0.3061 0.5156 0.0157  -0.0069 0.0252  72  LEU B CD2 
4649 N N   . THR B 87  ? 0.2823 0.2803 0.4851 0.0089  0.0003  0.0151  73  THR B N   
4650 C CA  . THR B 87  ? 0.2565 0.2535 0.4561 0.0069  0.0016  0.0150  73  THR B CA  
4651 C C   . THR B 87  ? 0.2881 0.2857 0.4837 0.0065  0.0006  0.0156  73  THR B C   
4652 O O   . THR B 87  ? 0.2903 0.2895 0.4854 0.0073  -0.0019 0.0159  73  THR B O   
4653 C CB  . THR B 87  ? 0.2804 0.2788 0.4814 0.0057  0.0025  0.0129  73  THR B CB  
4654 O OG1 . THR B 87  ? 0.2915 0.2928 0.4931 0.0054  0.0019  0.0120  73  THR B OG1 
4655 C CG2 . THR B 87  ? 0.2097 0.2066 0.4123 0.0058  0.0033  0.0118  73  THR B CG2 
4656 N N   . THR B 88  ? 0.2693 0.2657 0.4623 0.0052  0.0025  0.0155  74  THR B N   
4657 C CA  . THR B 88  ? 0.3031 0.2990 0.4911 0.0046  0.0026  0.0152  74  THR B CA  
4658 C C   . THR B 88  ? 0.3093 0.3073 0.4991 0.0039  0.0028  0.0129  74  THR B C   
4659 O O   . THR B 88  ? 0.2820 0.2812 0.4760 0.0037  0.0035  0.0120  74  THR B O   
4660 C CB  . THR B 88  ? 0.3580 0.3508 0.5421 0.0038  0.0058  0.0163  74  THR B CB  
4661 O OG1 . THR B 88  ? 0.4631 0.4540 0.6396 0.0034  0.0059  0.0161  74  THR B OG1 
4662 C CG2 . THR B 88  ? 0.3087 0.3032 0.4980 0.0029  0.0086  0.0149  74  THR B CG2 
4663 N N   . PHE B 89  ? 0.3001 0.2977 0.4859 0.0034  0.0018  0.0119  75  PHE B N   
4664 C CA  . PHE B 89  ? 0.2180 0.2161 0.4048 0.0025  0.0020  0.0096  75  PHE B CA  
4665 C C   . PHE B 89  ? 0.2620 0.2594 0.4513 0.0027  0.0049  0.0090  75  PHE B C   
4666 O O   . PHE B 89  ? 0.2435 0.2396 0.4316 0.0029  0.0075  0.0093  75  PHE B O   
4667 C CB  . PHE B 89  ? 0.2777 0.2739 0.4582 0.0016  0.0009  0.0082  75  PHE B CB  
4668 C CG  . PHE B 89  ? 0.3385 0.3336 0.5195 0.0005  0.0013  0.0057  75  PHE B CG  
4669 C CD1 . PHE B 89  ? 0.3355 0.3325 0.5196 -0.0008 -0.0012 0.0047  75  PHE B CD1 
4670 C CD2 . PHE B 89  ? 0.2583 0.2503 0.4377 0.0008  0.0046  0.0042  75  PHE B CD2 
4671 C CE1 . PHE B 89  ? 0.3087 0.3034 0.4931 -0.0022 -0.0007 0.0026  75  PHE B CE1 
4672 C CE2 . PHE B 89  ? 0.3063 0.2960 0.4862 0.0001  0.0050  0.0019  75  PHE B CE2 
4673 C CZ  . PHE B 89  ? 0.2856 0.2762 0.4675 -0.0016 0.0023  0.0012  75  PHE B CZ  
4674 N N   . GLY B 90  ? 0.2626 0.2606 0.4556 0.0027  0.0045  0.0084  76  GLY B N   
4675 C CA  . GLY B 90  ? 0.2707 0.2679 0.4666 0.0033  0.0060  0.0079  76  GLY B CA  
4676 C C   . GLY B 90  ? 0.2519 0.2509 0.4522 0.0038  0.0060  0.0091  76  GLY B C   
4677 O O   . GLY B 90  ? 0.2644 0.2636 0.4662 0.0037  0.0043  0.0096  76  GLY B O   
4678 N N   . VAL B 91  ? 0.2324 0.2320 0.4341 0.0039  0.0081  0.0095  77  VAL B N   
4679 C CA  . VAL B 91  ? 0.3032 0.3048 0.5104 0.0038  0.0079  0.0102  77  VAL B CA  
4680 C C   . VAL B 91  ? 0.2603 0.2615 0.4665 0.0031  0.0060  0.0110  77  VAL B C   
4681 O O   . VAL B 91  ? 0.2940 0.2959 0.5032 0.0028  0.0043  0.0109  77  VAL B O   
4682 C CB  . VAL B 91  ? 0.2736 0.2761 0.4835 0.0034  0.0115  0.0103  77  VAL B CB  
4683 C CG1 . VAL B 91  ? 0.2231 0.2260 0.4354 0.0046  0.0141  0.0089  77  VAL B CG1 
4684 C CG2 . VAL B 91  ? 0.2557 0.2557 0.4590 0.0026  0.0131  0.0114  77  VAL B CG2 
4685 N N   . GLY B 92  ? 0.2824 0.2824 0.4845 0.0031  0.0060  0.0116  78  GLY B N   
4686 C CA  . GLY B 92  ? 0.2569 0.2561 0.4589 0.0030  0.0048  0.0121  78  GLY B CA  
4687 C C   . GLY B 92  ? 0.3267 0.3261 0.5283 0.0032  0.0033  0.0112  78  GLY B C   
4688 O O   . GLY B 92  ? 0.2693 0.2680 0.4716 0.0028  0.0026  0.0107  78  GLY B O   
4689 N N   . GLU B 93  ? 0.2446 0.2449 0.4449 0.0034  0.0030  0.0109  79  GLU B N   
4690 C CA  . GLU B 93  ? 0.2469 0.2473 0.4469 0.0031  0.0027  0.0102  79  GLU B CA  
4691 C C   . GLU B 93  ? 0.2662 0.2650 0.4652 0.0025  0.0023  0.0100  79  GLU B C   
4692 O O   . GLU B 93  ? 0.3085 0.3060 0.5056 0.0021  0.0024  0.0097  79  GLU B O   
4693 C CB  . GLU B 93  ? 0.2635 0.2654 0.4636 0.0027  0.0026  0.0098  79  GLU B CB  
4694 C CG  . GLU B 93  ? 0.2360 0.2367 0.4348 0.0020  0.0026  0.0093  79  GLU B CG  
4695 C CD  . GLU B 93  ? 0.3224 0.3241 0.5211 0.0010  0.0019  0.0084  79  GLU B CD  
4696 O OE1 . GLU B 93  ? 0.2472 0.2502 0.4479 0.0000  0.0021  0.0081  79  GLU B OE1 
4697 O OE2 . GLU B 93  ? 0.2427 0.2437 0.4392 0.0009  0.0014  0.0079  79  GLU B OE2 
4698 N N   . LEU B 94  ? 0.2176 0.2161 0.4175 0.0027  0.0018  0.0103  80  LEU B N   
4699 C CA  . LEU B 94  ? 0.2470 0.2436 0.4460 0.0027  0.0002  0.0107  80  LEU B CA  
4700 C C   . LEU B 94  ? 0.2329 0.2294 0.4324 0.0025  -0.0015 0.0106  80  LEU B C   
4701 O O   . LEU B 94  ? 0.2666 0.2608 0.4627 0.0020  -0.0033 0.0108  80  LEU B O   
4702 C CB  . LEU B 94  ? 0.2183 0.2148 0.4200 0.0037  -0.0001 0.0109  80  LEU B CB  
4703 C CG  . LEU B 94  ? 0.2484 0.2431 0.4484 0.0036  0.0012  0.0105  80  LEU B CG  
4704 C CD1 . LEU B 94  ? 0.2125 0.2053 0.4148 0.0050  0.0009  0.0106  80  LEU B CD1 
4705 C CD2 . LEU B 94  ? 0.2697 0.2624 0.4660 0.0021  0.0013  0.0108  80  LEU B CD2 
4706 N N   . SER B 95  ? 0.2098 0.2082 0.4128 0.0024  -0.0009 0.0103  81  SER B N   
4707 C CA  . SER B 95  ? 0.2094 0.2072 0.4132 0.0014  -0.0026 0.0098  81  SER B CA  
4708 C C   . SER B 95  ? 0.2965 0.2912 0.4949 0.0008  -0.0023 0.0088  81  SER B C   
4709 O O   . SER B 95  ? 0.2788 0.2713 0.4746 -0.0002 -0.0044 0.0079  81  SER B O   
4710 C CB  . SER B 95  ? 0.2503 0.2497 0.4588 0.0009  -0.0011 0.0098  81  SER B CB  
4711 O OG  . SER B 95  ? 0.2506 0.2530 0.4649 0.0012  -0.0006 0.0103  81  SER B OG  
4712 N N   . ALA B 96  ? 0.2501 0.2446 0.4469 0.0015  0.0001  0.0087  82  ALA B N   
4713 C CA  . ALA B 96  ? 0.2148 0.2070 0.4083 0.0014  0.0015  0.0075  82  ALA B CA  
4714 C C   . ALA B 96  ? 0.2982 0.2885 0.4863 0.0008  0.0023  0.0073  82  ALA B C   
4715 O O   . ALA B 96  ? 0.2470 0.2353 0.4319 0.0006  0.0046  0.0059  82  ALA B O   
4716 C CB  . ALA B 96  ? 0.2125 0.2064 0.4090 0.0027  0.0037  0.0077  82  ALA B CB  
4717 N N   . MET B 97  ? 0.2389 0.2292 0.4258 0.0005  0.0008  0.0086  83  MET B N   
4718 C CA  . MET B 97  ? 0.2235 0.2110 0.4049 -0.0003 0.0021  0.0091  83  MET B CA  
4719 C C   . MET B 97  ? 0.3018 0.2845 0.4748 -0.0014 0.0022  0.0082  83  MET B C   
4720 O O   . MET B 97  ? 0.2951 0.2757 0.4637 -0.0022 0.0059  0.0076  83  MET B O   
4721 C CB  . MET B 97  ? 0.2350 0.2217 0.4163 -0.0001 -0.0001 0.0109  83  MET B CB  
4722 C CG  . MET B 97  ? 0.4850 0.4699 0.6641 -0.0010 0.0021  0.0119  83  MET B CG  
4723 S SD  . MET B 97  ? 0.9188 0.9088 1.1053 -0.0010 0.0046  0.0109  83  MET B SD  
4724 C CE  . MET B 97  ? 0.3902 0.3772 0.5761 -0.0018 0.0043  0.0122  83  MET B CE  
4725 N N   . ASN B 98  ? 0.2355 0.2162 0.4060 -0.0017 -0.0016 0.0078  84  ASN B N   
4726 C CA  . ASN B 98  ? 0.2582 0.2332 0.4185 -0.0030 -0.0022 0.0065  84  ASN B CA  
4727 C C   . ASN B 98  ? 0.3302 0.3037 0.4889 -0.0032 0.0022  0.0037  84  ASN B C   
4728 O O   . ASN B 98  ? 0.3049 0.2733 0.4542 -0.0042 0.0048  0.0024  84  ASN B O   
4729 C CB  . ASN B 98  ? 0.2495 0.2235 0.4089 -0.0035 -0.0083 0.0063  84  ASN B CB  
4730 C CG  . ASN B 98  ? 0.3878 0.3547 0.5341 -0.0052 -0.0104 0.0051  84  ASN B CG  
4731 O OD1 . ASN B 98  ? 0.3303 0.2924 0.4667 -0.0058 -0.0090 0.0063  84  ASN B OD1 
4732 N ND2 . ASN B 98  ? 0.2927 0.2581 0.4381 -0.0064 -0.0136 0.0027  84  ASN B ND2 
4733 N N   . GLY B 99  ? 0.2414 0.2185 0.4086 -0.0020 0.0033  0.0028  85  GLY B N   
4734 C CA  . GLY B 99  ? 0.3228 0.2983 0.4901 -0.0014 0.0075  0.0003  85  GLY B CA  
4735 C C   . GLY B 99  ? 0.2779 0.2551 0.4464 -0.0007 0.0128  0.0002  85  GLY B C   
4736 O O   . GLY B 99  ? 0.2774 0.2513 0.4412 -0.0009 0.0171  -0.0021 85  GLY B O   
4737 N N   . ILE B 100 ? 0.2707 0.2532 0.4459 -0.0002 0.0129  0.0023  86  ILE B N   
4738 C CA  . ILE B 100 ? 0.2715 0.2569 0.4500 -0.0001 0.0174  0.0023  86  ILE B CA  
4739 C C   . ILE B 100 ? 0.3269 0.3078 0.4959 -0.0023 0.0205  0.0022  86  ILE B C   
4740 O O   . ILE B 100 ? 0.3030 0.2837 0.4717 -0.0027 0.0262  0.0007  86  ILE B O   
4741 C CB  . ILE B 100 ? 0.2628 0.2540 0.4492 0.0002  0.0157  0.0043  86  ILE B CB  
4742 C CG1 . ILE B 100 ? 0.3002 0.2949 0.4941 0.0023  0.0135  0.0045  86  ILE B CG1 
4743 C CG2 . ILE B 100 ? 0.2277 0.2223 0.4184 -0.0007 0.0198  0.0042  86  ILE B CG2 
4744 C CD1 . ILE B 100 ? 0.2431 0.2386 0.4416 0.0043  0.0161  0.0028  86  ILE B CD1 
4745 N N   . ALA B 101 ? 0.3068 0.2836 0.4679 -0.0036 0.0169  0.0040  87  ALA B N   
4746 C CA  . ALA B 101 ? 0.3566 0.3271 0.5060 -0.0058 0.0192  0.0048  87  ALA B CA  
4747 C C   . ALA B 101 ? 0.3786 0.3433 0.5182 -0.0064 0.0225  0.0019  87  ALA B C   
4748 O O   . ALA B 101 ? 0.3279 0.2892 0.4607 -0.0079 0.0284  0.0013  87  ALA B O   
4749 C CB  . ALA B 101 ? 0.2637 0.2304 0.4067 -0.0063 0.0134  0.0076  87  ALA B CB  
4750 N N   . GLY B 102 ? 0.2944 0.2574 0.4326 -0.0056 0.0191  -0.0001 88  GLY B N   
4751 C CA  . GLY B 102 ? 0.3364 0.2931 0.4651 -0.0062 0.0223  -0.0037 88  GLY B CA  
4752 C C   . GLY B 102 ? 0.3209 0.2801 0.4561 -0.0049 0.0303  -0.0064 88  GLY B C   
4753 O O   . GLY B 102 ? 0.3528 0.3067 0.4792 -0.0058 0.0364  -0.0089 88  GLY B O   
4754 N N   . SER B 103 ? 0.2715 0.2386 0.4220 -0.0026 0.0304  -0.0059 89  SER B N   
4755 C CA  . SER B 103 ? 0.3161 0.2871 0.4759 -0.0007 0.0371  -0.0079 89  SER B CA  
4756 C C   . SER B 103 ? 0.2740 0.2470 0.4337 -0.0024 0.0433  -0.0073 89  SER B C   
4757 O O   . SER B 103 ? 0.2923 0.2649 0.4527 -0.0021 0.0509  -0.0099 89  SER B O   
4758 C CB  . SER B 103 ? 0.2750 0.2538 0.4502 0.0020  0.0342  -0.0067 89  SER B CB  
4759 O OG  . SER B 103 ? 0.3085 0.2845 0.4833 0.0031  0.0295  -0.0072 89  SER B OG  
4760 N N   . TYR B 104 ? 0.2751 0.2501 0.4347 -0.0043 0.0407  -0.0038 90  TYR B N   
4761 C CA  . TYR B 104 ? 0.3374 0.3129 0.4960 -0.0067 0.0468  -0.0029 90  TYR B CA  
4762 C C   . TYR B 104 ? 0.3653 0.3310 0.5063 -0.0091 0.0517  -0.0039 90  TYR B C   
4763 O O   . TYR B 104 ? 0.3409 0.3063 0.4814 -0.0103 0.0604  -0.0055 90  TYR B O   
4764 C CB  . TYR B 104 ? 0.3341 0.3117 0.4949 -0.0083 0.0426  0.0009  90  TYR B CB  
4765 C CG  . TYR B 104 ? 0.3136 0.2920 0.4755 -0.0114 0.0485  0.0021  90  TYR B CG  
4766 C CD1 . TYR B 104 ? 0.3203 0.2896 0.4669 -0.0144 0.0516  0.0038  90  TYR B CD1 
4767 C CD2 . TYR B 104 ? 0.2937 0.2814 0.4717 -0.0116 0.0507  0.0019  90  TYR B CD2 
4768 C CE1 . TYR B 104 ? 0.3749 0.3440 0.5222 -0.0178 0.0578  0.0052  90  TYR B CE1 
4769 C CE2 . TYR B 104 ? 0.3596 0.3483 0.5400 -0.0151 0.0564  0.0028  90  TYR B CE2 
4770 C CZ  . TYR B 104 ? 0.3794 0.3584 0.5444 -0.0183 0.0603  0.0046  90  TYR B CZ  
4771 O OH  . TYR B 104 ? 0.4019 0.3810 0.5690 -0.0224 0.0666  0.0059  90  TYR B OH  
4772 N N   . ALA B 105 ? 0.3290 0.2866 0.4553 -0.0099 0.0462  -0.0031 91  ALA B N   
4773 C CA  . ALA B 105 ? 0.3185 0.2653 0.4249 -0.0124 0.0494  -0.0036 91  ALA B CA  
4774 C C   . ALA B 105 ? 0.4136 0.3571 0.5161 -0.0119 0.0570  -0.0087 91  ALA B C   
4775 O O   . ALA B 105 ? 0.3865 0.3240 0.4777 -0.0140 0.0649  -0.0098 91  ALA B O   
4776 C CB  . ALA B 105 ? 0.3280 0.2678 0.4215 -0.0129 0.0401  -0.0021 91  ALA B CB  
4777 N N   . GLU B 106 ? 0.3216 0.2682 0.4329 -0.0090 0.0552  -0.0118 92  GLU B N   
4778 C CA  . GLU B 106 ? 0.4161 0.3583 0.5236 -0.0079 0.0618  -0.0171 92  GLU B CA  
4779 C C   . GLU B 106 ? 0.3620 0.3132 0.4888 -0.0049 0.0687  -0.0191 92  GLU B C   
4780 O O   . GLU B 106 ? 0.3293 0.2782 0.4579 -0.0027 0.0734  -0.0236 92  GLU B O   
4781 C CB  . GLU B 106 ? 0.3632 0.3000 0.4653 -0.0070 0.0552  -0.0196 92  GLU B CB  
4782 C CG  . GLU B 106 ? 0.3429 0.2737 0.4310 -0.0095 0.0459  -0.0173 92  GLU B CG  
4783 C CD  . GLU B 106 ? 0.5287 0.4478 0.5981 -0.0112 0.0447  -0.0214 92  GLU B CD  
4784 O OE1 . GLU B 106 ? 0.4768 0.3930 0.5473 -0.0099 0.0490  -0.0265 92  GLU B OE1 
4785 O OE2 . GLU B 106 ? 0.3681 0.2806 0.4219 -0.0138 0.0387  -0.0197 92  GLU B OE2 
4786 N N   . HIS B 107 ? 0.3190 0.2802 0.4608 -0.0046 0.0689  -0.0160 93  HIS B N   
4787 C CA  . HIS B 107 ? 0.3631 0.3341 0.5243 -0.0021 0.0749  -0.0175 93  HIS B CA  
4788 C C   . HIS B 107 ? 0.3658 0.3399 0.5389 0.0025  0.0719  -0.0196 93  HIS B C   
4789 O O   . HIS B 107 ? 0.3800 0.3534 0.5577 0.0052  0.0783  -0.0235 93  HIS B O   
4790 C CB  . HIS B 107 ? 0.3656 0.3343 0.5234 -0.0033 0.0873  -0.0207 93  HIS B CB  
4791 C CG  . HIS B 107 ? 0.5443 0.5095 0.6909 -0.0081 0.0914  -0.0181 93  HIS B CG  
4792 N ND1 . HIS B 107 ? 0.4847 0.4571 0.6426 -0.0099 0.0993  -0.0175 93  HIS B ND1 
4793 C CD2 . HIS B 107 ? 0.3961 0.3511 0.5218 -0.0117 0.0885  -0.0156 93  HIS B CD2 
4794 C CE1 . HIS B 107 ? 0.3774 0.3432 0.5207 -0.0145 0.1018  -0.0147 93  HIS B CE1 
4795 N NE2 . HIS B 107 ? 0.4326 0.3876 0.5558 -0.0154 0.0950  -0.0133 93  HIS B NE2 
4796 N N   . VAL B 108 ? 0.3036 0.2803 0.4811 0.0035  0.0625  -0.0168 94  VAL B N   
4797 C CA  . VAL B 108 ? 0.3063 0.2850 0.4940 0.0075  0.0588  -0.0175 94  VAL B CA  
4798 C C   . VAL B 108 ? 0.3642 0.3538 0.5687 0.0093  0.0545  -0.0142 94  VAL B C   
4799 O O   . VAL B 108 ? 0.3239 0.3158 0.5269 0.0072  0.0489  -0.0108 94  VAL B O   
4800 C CB  . VAL B 108 ? 0.4463 0.4174 0.6235 0.0069  0.0518  -0.0174 94  VAL B CB  
4801 C CG1 . VAL B 108 ? 0.3082 0.2798 0.4951 0.0107  0.0491  -0.0180 94  VAL B CG1 
4802 C CG2 . VAL B 108 ? 0.3679 0.3279 0.5269 0.0045  0.0547  -0.0208 94  VAL B CG2 
4803 N N   . PRO B 109 ? 0.3825 0.3787 0.6029 0.0131  0.0566  -0.0151 95  PRO B N   
4804 C CA  . PRO B 109 ? 0.3095 0.3160 0.5448 0.0145  0.0516  -0.0120 95  PRO B CA  
4805 C C   . PRO B 109 ? 0.3754 0.3808 0.6111 0.0163  0.0430  -0.0093 95  PRO B C   
4806 O O   . PRO B 109 ? 0.3149 0.3207 0.5585 0.0204  0.0415  -0.0094 95  PRO B O   
4807 C CB  . PRO B 109 ? 0.2775 0.2910 0.5297 0.0183  0.0569  -0.0141 95  PRO B CB  
4808 C CG  . PRO B 109 ? 0.2972 0.3023 0.5437 0.0206  0.0625  -0.0181 95  PRO B CG  
4809 C CD  . PRO B 109 ? 0.3366 0.3315 0.5623 0.0163  0.0643  -0.0192 95  PRO B CD  
4810 N N   . VAL B 110 ? 0.2584 0.2620 0.4856 0.0133  0.0377  -0.0068 96  VAL B N   
4811 C CA  . VAL B 110 ? 0.3001 0.3028 0.5268 0.0142  0.0305  -0.0041 96  VAL B CA  
4812 C C   . VAL B 110 ? 0.2881 0.2983 0.5211 0.0134  0.0262  -0.0013 96  VAL B C   
4813 O O   . VAL B 110 ? 0.3135 0.3252 0.5431 0.0101  0.0266  -0.0007 96  VAL B O   
4814 C CB  . VAL B 110 ? 0.2948 0.2899 0.5080 0.0116  0.0280  -0.0039 96  VAL B CB  
4815 C CG1 . VAL B 110 ? 0.2283 0.2240 0.4418 0.0116  0.0217  -0.0009 96  VAL B CG1 
4816 C CG2 . VAL B 110 ? 0.3288 0.3158 0.5359 0.0124  0.0307  -0.0069 96  VAL B CG2 
4817 N N   . LEU B 111 ? 0.2474 0.2612 0.4883 0.0162  0.0219  0.0006  97  LEU B N   
4818 C CA  . LEU B 111 ? 0.2156 0.2356 0.4610 0.0153  0.0171  0.0028  97  LEU B CA  
4819 C C   . LEU B 111 ? 0.3794 0.3950 0.6154 0.0139  0.0126  0.0050  97  LEU B C   
4820 O O   . LEU B 111 ? 0.2695 0.2804 0.5023 0.0155  0.0107  0.0061  97  LEU B O   
4821 C CB  . LEU B 111 ? 0.2151 0.2411 0.4729 0.0191  0.0140  0.0039  97  LEU B CB  
4822 C CG  . LEU B 111 ? 0.3126 0.3436 0.5728 0.0182  0.0075  0.0062  97  LEU B CG  
4823 C CD1 . LEU B 111 ? 0.2310 0.2682 0.4951 0.0145  0.0087  0.0050  97  LEU B CD1 
4824 C CD2 . LEU B 111 ? 0.2962 0.3315 0.5665 0.0224  0.0028  0.0078  97  LEU B CD2 
4825 N N   . HIS B 112 ? 0.2809 0.2976 0.5130 0.0107  0.0114  0.0055  98  HIS B N   
4826 C CA  . HIS B 112 ? 0.2709 0.2843 0.4955 0.0094  0.0080  0.0071  98  HIS B CA  
4827 C C   . HIS B 112 ? 0.2074 0.2246 0.4349 0.0096  0.0036  0.0086  98  HIS B C   
4828 O O   . HIS B 112 ? 0.2401 0.2614 0.4705 0.0078  0.0030  0.0080  98  HIS B O   
4829 C CB  . HIS B 112 ? 0.2559 0.2668 0.4738 0.0064  0.0095  0.0066  98  HIS B CB  
4830 C CG  . HIS B 112 ? 0.2562 0.2635 0.4677 0.0056  0.0070  0.0078  98  HIS B CG  
4831 N ND1 . HIS B 112 ? 0.2581 0.2631 0.4647 0.0036  0.0072  0.0078  98  HIS B ND1 
4832 C CD2 . HIS B 112 ? 0.2783 0.2840 0.4884 0.0066  0.0047  0.0091  98  HIS B CD2 
4833 C CE1 . HIS B 112 ? 0.2890 0.2922 0.4929 0.0037  0.0052  0.0087  98  HIS B CE1 
4834 N NE2 . HIS B 112 ? 0.2653 0.2688 0.4709 0.0052  0.0041  0.0095  98  HIS B NE2 
4835 N N   . ILE B 113 ? 0.2416 0.2569 0.4675 0.0116  0.0005  0.0104  99  ILE B N   
4836 C CA  . ILE B 113 ? 0.2318 0.2488 0.4570 0.0117  -0.0041 0.0120  99  ILE B CA  
4837 C C   . ILE B 113 ? 0.2808 0.2933 0.4965 0.0098  -0.0044 0.0127  99  ILE B C   
4838 O O   . ILE B 113 ? 0.2822 0.2900 0.4937 0.0101  -0.0030 0.0135  99  ILE B O   
4839 C CB  . ILE B 113 ? 0.2756 0.2921 0.5034 0.0152  -0.0073 0.0142  99  ILE B CB  
4840 C CG1 . ILE B 113 ? 0.2908 0.3115 0.5298 0.0180  -0.0060 0.0133  99  ILE B CG1 
4841 C CG2 . ILE B 113 ? 0.2270 0.2452 0.4526 0.0151  -0.0130 0.0159  99  ILE B CG2 
4842 C CD1 . ILE B 113 ? 0.3163 0.3341 0.5578 0.0223  -0.0082 0.0156  99  ILE B CD1 
4843 N N   . VAL B 114 ? 0.2645 0.2784 0.4779 0.0078  -0.0059 0.0120  100 VAL B N   
4844 C CA  . VAL B 114 ? 0.2682 0.2781 0.4737 0.0063  -0.0054 0.0121  100 VAL B CA  
4845 C C   . VAL B 114 ? 0.2967 0.3057 0.4972 0.0063  -0.0090 0.0131  100 VAL B C   
4846 O O   . VAL B 114 ? 0.2980 0.3101 0.5001 0.0054  -0.0122 0.0122  100 VAL B O   
4847 C CB  . VAL B 114 ? 0.3308 0.3410 0.5361 0.0039  -0.0036 0.0102  100 VAL B CB  
4848 C CG1 . VAL B 114 ? 0.2605 0.2668 0.4593 0.0030  -0.0029 0.0100  100 VAL B CG1 
4849 C CG2 . VAL B 114 ? 0.2699 0.2797 0.4775 0.0038  -0.0005 0.0097  100 VAL B CG2 
4850 N N   . GLY B 115 ? 0.2657 0.2702 0.4597 0.0071  -0.0087 0.0151  101 GLY B N   
4851 C CA  . GLY B 115 ? 0.3073 0.3091 0.4931 0.0068  -0.0113 0.0161  101 GLY B CA  
4852 C C   . GLY B 115 ? 0.3980 0.3979 0.5781 0.0044  -0.0095 0.0138  101 GLY B C   
4853 O O   . GLY B 115 ? 0.3023 0.3004 0.4819 0.0039  -0.0053 0.0131  101 GLY B O   
4854 N N   . ALA B 116 ? 0.2972 0.2975 0.4736 0.0032  -0.0129 0.0124  102 ALA B N   
4855 C CA  . ALA B 116 ? 0.2696 0.2679 0.4418 0.0010  -0.0114 0.0094  102 ALA B CA  
4856 C C   . ALA B 116 ? 0.3361 0.3295 0.4959 0.0001  -0.0133 0.0090  102 ALA B C   
4857 O O   . ALA B 116 ? 0.3299 0.3228 0.4853 0.0009  -0.0178 0.0111  102 ALA B O   
4858 C CB  . ALA B 116 ? 0.2868 0.2893 0.4663 -0.0006 -0.0134 0.0070  102 ALA B CB  
4859 N N   . PRO B 117 ? 0.3020 0.2913 0.4555 -0.0013 -0.0100 0.0064  103 PRO B N   
4860 C CA  . PRO B 117 ? 0.3783 0.3618 0.5179 -0.0026 -0.0112 0.0051  103 PRO B CA  
4861 C C   . PRO B 117 ? 0.3344 0.3195 0.4723 -0.0041 -0.0187 0.0037  103 PRO B C   
4862 O O   . PRO B 117 ? 0.2742 0.2648 0.4227 -0.0049 -0.0214 0.0024  103 PRO B O   
4863 C CB  . PRO B 117 ? 0.3311 0.3105 0.4676 -0.0036 -0.0055 0.0015  103 PRO B CB  
4864 C CG  . PRO B 117 ? 0.3266 0.3097 0.4756 -0.0027 -0.0024 0.0013  103 PRO B CG  
4865 C CD  . PRO B 117 ? 0.3993 0.3882 0.5577 -0.0016 -0.0050 0.0043  103 PRO B CD  
4866 N N   . GLY B 118 ? 0.3062 0.2862 0.4302 -0.0049 -0.0219 0.0037  104 GLY B N   
4867 C CA  . GLY B 118 ? 0.4561 0.4377 0.5777 -0.0066 -0.0304 0.0024  104 GLY B CA  
4868 C C   . GLY B 118 ? 0.4237 0.4063 0.5495 -0.0097 -0.0310 -0.0027 104 GLY B C   
4869 O O   . GLY B 118 ? 0.3620 0.3403 0.4857 -0.0106 -0.0250 -0.0057 104 GLY B O   
4870 N N   . THR B 119 ? 0.3533 0.3416 0.4862 -0.0112 -0.0386 -0.0036 105 THR B N   
4871 C CA  . THR B 119 ? 0.3463 0.3361 0.4854 -0.0148 -0.0395 -0.0082 105 THR B CA  
4872 C C   . THR B 119 ? 0.4468 0.4269 0.5709 -0.0176 -0.0381 -0.0129 105 THR B C   
4873 O O   . THR B 119 ? 0.4072 0.3845 0.5341 -0.0194 -0.0338 -0.0165 105 THR B O   
4874 C CB  . THR B 119 ? 0.4496 0.4475 0.5987 -0.0165 -0.0484 -0.0085 105 THR B CB  
4875 O OG1 . THR B 119 ? 0.5655 0.5605 0.7020 -0.0173 -0.0564 -0.0087 105 THR B OG1 
4876 C CG2 . THR B 119 ? 0.3159 0.3231 0.4802 -0.0133 -0.0490 -0.0043 105 THR B CG2 
4877 N N   . ALA B 120 ? 0.4188 0.3928 0.5259 -0.0178 -0.0413 -0.0130 106 ALA B N   
4878 C CA  . ALA B 120 ? 0.5033 0.4669 0.5942 -0.0204 -0.0392 -0.0181 106 ALA B CA  
4879 C C   . ALA B 120 ? 0.5005 0.4587 0.5901 -0.0188 -0.0281 -0.0193 106 ALA B C   
4880 O O   . ALA B 120 ? 0.4875 0.4403 0.5753 -0.0206 -0.0245 -0.0242 106 ALA B O   
4881 C CB  . ALA B 120 ? 0.4840 0.4410 0.5545 -0.0206 -0.0436 -0.0172 106 ALA B CB  
4882 N N   . SER B 121 ? 0.5332 0.4929 0.6248 -0.0153 -0.0226 -0.0150 107 SER B N   
4883 C CA  . SER B 121 ? 0.4697 0.4261 0.5632 -0.0135 -0.0127 -0.0158 107 SER B CA  
4884 C C   . SER B 121 ? 0.4237 0.3838 0.5327 -0.0136 -0.0107 -0.0173 107 SER B C   
4885 O O   . SER B 121 ? 0.3905 0.3455 0.4993 -0.0134 -0.0049 -0.0205 107 SER B O   
4886 C CB  . SER B 121 ? 0.3168 0.2758 0.4127 -0.0104 -0.0086 -0.0106 107 SER B CB  
4887 O OG  . SER B 121 ? 0.6172 0.5694 0.6963 -0.0104 -0.0066 -0.0097 107 SER B OG  
4888 N N   . GLN B 122 ? 0.3579 0.3261 0.4801 -0.0137 -0.0151 -0.0148 108 GLN B N   
4889 C CA  . GLN B 122 ? 0.3963 0.3671 0.5315 -0.0142 -0.0131 -0.0157 108 GLN B CA  
4890 C C   . GLN B 122 ? 0.4726 0.4381 0.6051 -0.0178 -0.0146 -0.0209 108 GLN B C   
4891 O O   . GLN B 122 ? 0.4356 0.3965 0.5709 -0.0178 -0.0099 -0.0230 108 GLN B O   
4892 C CB  . GLN B 122 ? 0.2908 0.2708 0.4391 -0.0140 -0.0169 -0.0123 108 GLN B CB  
4893 C CG  . GLN B 122 ? 0.3341 0.3184 0.4866 -0.0105 -0.0146 -0.0076 108 GLN B CG  
4894 C CD  . GLN B 122 ? 0.3492 0.3415 0.5150 -0.0101 -0.0166 -0.0052 108 GLN B CD  
4895 O OE1 . GLN B 122 ? 0.3954 0.3895 0.5689 -0.0120 -0.0164 -0.0065 108 GLN B OE1 
4896 N NE2 . GLN B 122 ? 0.3193 0.3156 0.4875 -0.0077 -0.0179 -0.0017 108 GLN B NE2 
4897 N N   . GLN B 123 ? 0.3786 0.3439 0.5053 -0.0210 -0.0214 -0.0231 109 GLN B N   
4898 C CA  . GLN B 123 ? 0.5213 0.4817 0.6464 -0.0253 -0.0236 -0.0285 109 GLN B CA  
4899 C C   . GLN B 123 ? 0.4426 0.3912 0.5550 -0.0253 -0.0181 -0.0331 109 GLN B C   
4900 O O   . GLN B 123 ? 0.3967 0.3395 0.5106 -0.0276 -0.0165 -0.0372 109 GLN B O   
4901 C CB  . GLN B 123 ? 0.4048 0.3682 0.5267 -0.0288 -0.0332 -0.0300 109 GLN B CB  
4902 C CG  . GLN B 123 ? 0.5173 0.4927 0.6556 -0.0293 -0.0384 -0.0267 109 GLN B CG  
4903 C CD  . GLN B 123 ? 0.6372 0.6171 0.7733 -0.0316 -0.0488 -0.0273 109 GLN B CD  
4904 O OE1 . GLN B 123 ? 0.6236 0.5979 0.7436 -0.0317 -0.0523 -0.0285 109 GLN B OE1 
4905 N NE2 . GLN B 123 ? 0.6228 0.6130 0.7752 -0.0334 -0.0536 -0.0265 109 GLN B NE2 
4906 N N   . ARG B 124 ? 0.5192 0.4638 0.6197 -0.0227 -0.0145 -0.0325 110 ARG B N   
4907 C CA  . ARG B 124 ? 0.3933 0.3272 0.4826 -0.0222 -0.0077 -0.0371 110 ARG B CA  
4908 C C   . ARG B 124 ? 0.4383 0.3715 0.5375 -0.0185 0.0008  -0.0361 110 ARG B C   
4909 O O   . ARG B 124 ? 0.3496 0.2744 0.4428 -0.0174 0.0071  -0.0400 110 ARG B O   
4910 C CB  . ARG B 124 ? 0.4830 0.4125 0.5551 -0.0212 -0.0061 -0.0369 110 ARG B CB  
4911 C CG  . ARG B 124 ? 0.4856 0.4132 0.5441 -0.0247 -0.0150 -0.0384 110 ARG B CG  
4912 C CD  . ARG B 124 ? 0.4967 0.4160 0.5338 -0.0243 -0.0119 -0.0391 110 ARG B CD  
4913 N NE  . ARG B 124 ? 0.8343 0.7587 0.8720 -0.0212 -0.0107 -0.0325 110 ARG B NE  
4914 C CZ  . ARG B 124 ? 0.8396 0.7663 0.8704 -0.0216 -0.0182 -0.0285 110 ARG B CZ  
4915 N NH1 . ARG B 124 ? 0.7636 0.6907 0.7895 -0.0247 -0.0288 -0.0301 110 ARG B NH1 
4916 N NH2 . ARG B 124 ? 0.6931 0.6222 0.7233 -0.0188 -0.0156 -0.0227 110 ARG B NH2 
4917 N N   . GLY B 125 ? 0.3551 0.2966 0.4689 -0.0164 0.0008  -0.0312 111 GLY B N   
4918 C CA  . GLY B 125 ? 0.3643 0.3055 0.4876 -0.0129 0.0073  -0.0298 111 GLY B CA  
4919 C C   . GLY B 125 ? 0.3844 0.3237 0.5032 -0.0095 0.0142  -0.0297 111 GLY B C   
4920 O O   . GLY B 125 ? 0.4089 0.3437 0.5308 -0.0071 0.0203  -0.0317 111 GLY B O   
4921 N N   . GLU B 126 ? 0.3791 0.3215 0.4915 -0.0091 0.0138  -0.0271 112 GLU B N   
4922 C CA  . GLU B 126 ? 0.4758 0.4163 0.5836 -0.0067 0.0211  -0.0269 112 GLU B CA  
4923 C C   . GLU B 126 ? 0.3774 0.3240 0.5004 -0.0031 0.0253  -0.0235 112 GLU B C   
4924 O O   . GLU B 126 ? 0.3608 0.3140 0.4948 -0.0026 0.0215  -0.0199 112 GLU B O   
4925 C CB  . GLU B 126 ? 0.4018 0.3432 0.4982 -0.0077 0.0193  -0.0243 112 GLU B CB  
4926 C CG  . GLU B 126 ? 0.4876 0.4256 0.5711 -0.0111 0.0118  -0.0260 112 GLU B CG  
4927 C CD  . GLU B 126 ? 0.6007 0.5357 0.6685 -0.0117 0.0114  -0.0240 112 GLU B CD  
4928 O OE1 . GLU B 126 ? 0.6272 0.5675 0.6990 -0.0102 0.0108  -0.0185 112 GLU B OE1 
4929 O OE2 . GLU B 126 ? 0.7186 0.6449 0.7688 -0.0138 0.0116  -0.0278 112 GLU B OE2 
4930 N N   . LEU B 127 ? 0.3219 0.2664 0.4455 -0.0007 0.0332  -0.0250 113 LEU B N   
4931 C CA  . LEU B 127 ? 0.4544 0.4051 0.5929 0.0026  0.0368  -0.0221 113 LEU B CA  
4932 C C   . LEU B 127 ? 0.4149 0.3715 0.5537 0.0024  0.0370  -0.0176 113 LEU B C   
4933 O O   . LEU B 127 ? 0.3332 0.2896 0.4700 0.0031  0.0435  -0.0176 113 LEU B O   
4934 C CB  . LEU B 127 ? 0.3341 0.2811 0.4760 0.0054  0.0452  -0.0258 113 LEU B CB  
4935 C CG  . LEU B 127 ? 0.4677 0.4068 0.6092 0.0061  0.0461  -0.0306 113 LEU B CG  
4936 C CD1 . LEU B 127 ? 0.4568 0.3931 0.6039 0.0099  0.0552  -0.0340 113 LEU B CD1 
4937 C CD2 . LEU B 127 ? 0.4557 0.3970 0.6078 0.0065  0.0400  -0.0283 113 LEU B CD2 
4938 N N   . LEU B 128 ? 0.4052 0.3667 0.5467 0.0013  0.0303  -0.0139 114 LEU B N   
4939 C CA  . LEU B 128 ? 0.3630 0.3288 0.5041 0.0009  0.0295  -0.0096 114 LEU B CA  
4940 C C   . LEU B 128 ? 0.3285 0.3012 0.4847 0.0028  0.0305  -0.0066 114 LEU B C   
4941 O O   . LEU B 128 ? 0.2635 0.2386 0.4297 0.0042  0.0288  -0.0068 114 LEU B O   
4942 C CB  . LEU B 128 ? 0.3015 0.2686 0.4381 -0.0009 0.0217  -0.0074 114 LEU B CB  
4943 C CG  . LEU B 128 ? 0.3479 0.3093 0.4695 -0.0032 0.0184  -0.0097 114 LEU B CG  
4944 C CD1 . LEU B 128 ? 0.3014 0.2663 0.4223 -0.0043 0.0103  -0.0068 114 LEU B CD1 
4945 C CD2 . LEU B 128 ? 0.3613 0.3164 0.4688 -0.0037 0.0238  -0.0106 114 LEU B CD2 
4946 N N   . HIS B 129 ? 0.2944 0.2696 0.4511 0.0026  0.0328  -0.0038 115 HIS B N   
4947 C CA  . HIS B 129 ? 0.3290 0.3106 0.4990 0.0037  0.0326  -0.0011 115 HIS B CA  
4948 C C   . HIS B 129 ? 0.3340 0.3187 0.5081 0.0035  0.0255  0.0010  115 HIS B C   
4949 O O   . HIS B 129 ? 0.3069 0.2900 0.4740 0.0023  0.0212  0.0015  115 HIS B O   
4950 C CB  . HIS B 129 ? 0.3048 0.2874 0.4737 0.0026  0.0365  0.0015  115 HIS B CB  
4951 C CG  . HIS B 129 ? 0.3909 0.3707 0.5492 0.0010  0.0330  0.0043  115 HIS B CG  
4952 N ND1 . HIS B 129 ? 0.4743 0.4477 0.6171 -0.0002 0.0337  0.0039  115 HIS B ND1 
4953 C CD2 . HIS B 129 ? 0.4655 0.4475 0.6264 0.0007  0.0284  0.0076  115 HIS B CD2 
4954 C CE1 . HIS B 129 ? 0.4244 0.3967 0.5615 -0.0009 0.0291  0.0073  115 HIS B CE1 
4955 N NE2 . HIS B 129 ? 0.3302 0.3077 0.4787 -0.0002 0.0263  0.0094  115 HIS B NE2 
4956 N N   . HIS B 130 ? 0.2376 0.2269 0.4233 0.0047  0.0244  0.0021  116 HIS B N   
4957 C CA  . HIS B 130 ? 0.2658 0.2575 0.4553 0.0046  0.0189  0.0037  116 HIS B CA  
4958 C C   . HIS B 130 ? 0.2931 0.2824 0.4813 0.0047  0.0163  0.0020  116 HIS B C   
4959 O O   . HIS B 130 ? 0.3315 0.3218 0.5201 0.0039  0.0124  0.0030  116 HIS B O   
4960 C CB  . HIS B 130 ? 0.2805 0.2727 0.4657 0.0034  0.0159  0.0060  116 HIS B CB  
4961 C CG  . HIS B 130 ? 0.3951 0.3879 0.5803 0.0029  0.0185  0.0080  116 HIS B CG  
4962 N ND1 . HIS B 130 ? 0.3577 0.3526 0.5498 0.0031  0.0225  0.0079  116 HIS B ND1 
4963 C CD2 . HIS B 130 ? 0.3916 0.3828 0.5714 0.0021  0.0175  0.0102  116 HIS B CD2 
4964 C CE1 . HIS B 130 ? 0.3479 0.3422 0.5385 0.0019  0.0244  0.0100  116 HIS B CE1 
4965 N NE2 . HIS B 130 ? 0.3878 0.3792 0.5703 0.0015  0.0214  0.0116  116 HIS B NE2 
4966 N N   . THR B 131 ? 0.2791 0.2649 0.4662 0.0054  0.0190  -0.0007 117 THR B N   
4967 C CA  . THR B 131 ? 0.3216 0.3040 0.5086 0.0053  0.0171  -0.0022 117 THR B CA  
4968 C C   . THR B 131 ? 0.3190 0.3006 0.5141 0.0080  0.0189  -0.0027 117 THR B C   
4969 O O   . THR B 131 ? 0.2364 0.2207 0.4375 0.0098  0.0219  -0.0025 117 THR B O   
4970 C CB  . THR B 131 ? 0.3405 0.3175 0.5182 0.0037  0.0177  -0.0055 117 THR B CB  
4971 O OG1 . THR B 131 ? 0.3066 0.2800 0.4826 0.0051  0.0231  -0.0083 117 THR B OG1 
4972 C CG2 . THR B 131 ? 0.2488 0.2265 0.4183 0.0016  0.0152  -0.0049 117 THR B CG2 
4973 N N   . LEU B 132 ? 0.2818 0.2595 0.4775 0.0081  0.0171  -0.0032 118 LEU B N   
4974 C CA  . LEU B 132 ? 0.3389 0.3143 0.5416 0.0111  0.0181  -0.0033 118 LEU B CA  
4975 C C   . LEU B 132 ? 0.3567 0.3271 0.5583 0.0127  0.0230  -0.0072 118 LEU B C   
4976 O O   . LEU B 132 ? 0.2879 0.2552 0.4957 0.0157  0.0240  -0.0077 118 LEU B O   
4977 C CB  . LEU B 132 ? 0.3369 0.3085 0.5398 0.0107  0.0145  -0.0017 118 LEU B CB  
4978 C CG  . LEU B 132 ? 0.2849 0.2604 0.4876 0.0090  0.0106  0.0017  118 LEU B CG  
4979 C CD1 . LEU B 132 ? 0.2891 0.2594 0.4907 0.0084  0.0083  0.0034  118 LEU B CD1 
4980 C CD2 . LEU B 132 ? 0.2513 0.2326 0.4601 0.0108  0.0095  0.0039  118 LEU B CD2 
4981 N N   . GLY B 133 ? 0.3395 0.3081 0.5326 0.0109  0.0259  -0.0099 119 GLY B N   
4982 C CA  . GLY B 133 ? 0.2659 0.2287 0.4557 0.0120  0.0313  -0.0143 119 GLY B CA  
4983 C C   . GLY B 133 ? 0.3475 0.3015 0.5322 0.0111  0.0305  -0.0174 119 GLY B C   
4984 O O   . GLY B 133 ? 0.3738 0.3216 0.5567 0.0126  0.0352  -0.0214 119 GLY B O   
4985 N N   . ASP B 134 ? 0.2793 0.2323 0.4619 0.0084  0.0253  -0.0159 120 ASP B N   
4986 C CA  . ASP B 134 ? 0.3771 0.3216 0.5559 0.0067  0.0242  -0.0186 120 ASP B CA  
4987 C C   . ASP B 134 ? 0.4111 0.3540 0.5798 0.0018  0.0215  -0.0209 120 ASP B C   
4988 O O   . ASP B 134 ? 0.3719 0.3082 0.5375 -0.0007 0.0201  -0.0234 120 ASP B O   
4989 C CB  . ASP B 134 ? 0.3062 0.2499 0.4915 0.0069  0.0208  -0.0149 120 ASP B CB  
4990 C CG  . ASP B 134 ? 0.4025 0.3536 0.5887 0.0047  0.0165  -0.0109 120 ASP B CG  
4991 O OD1 . ASP B 134 ? 0.3380 0.2949 0.5209 0.0032  0.0158  -0.0107 120 ASP B OD1 
4992 O OD2 . ASP B 134 ? 0.4265 0.3769 0.6162 0.0045  0.0142  -0.0077 120 ASP B OD2 
4993 N N   . GLY B 135 ? 0.3402 0.2888 0.5041 0.0004  0.0202  -0.0200 121 GLY B N   
4994 C CA  . GLY B 135 ? 0.3231 0.2711 0.4783 -0.0037 0.0163  -0.0217 121 GLY B CA  
4995 C C   . GLY B 135 ? 0.4070 0.3596 0.5668 -0.0065 0.0108  -0.0192 121 GLY B C   
4996 O O   . GLY B 135 ? 0.3713 0.3242 0.5266 -0.0100 0.0069  -0.0208 121 GLY B O   
4997 N N   . GLU B 136 ? 0.3253 0.2816 0.4941 -0.0050 0.0105  -0.0153 122 GLU B N   
4998 C CA  . GLU B 136 ? 0.3489 0.3094 0.5224 -0.0075 0.0069  -0.0129 122 GLU B CA  
4999 C C   . GLU B 136 ? 0.3527 0.3218 0.5284 -0.0067 0.0051  -0.0095 122 GLU B C   
5000 O O   . GLU B 136 ? 0.3098 0.2815 0.4877 -0.0037 0.0070  -0.0073 122 GLU B O   
5001 C CB  . GLU B 136 ? 0.3223 0.2798 0.5018 -0.0066 0.0080  -0.0106 122 GLU B CB  
5002 C CG  . GLU B 136 ? 0.6256 0.5864 0.8091 -0.0094 0.0058  -0.0082 122 GLU B CG  
5003 C CD  . GLU B 136 ? 0.6090 0.5694 0.7915 -0.0142 0.0035  -0.0109 122 GLU B CD  
5004 O OE1 . GLU B 136 ? 0.5348 0.4875 0.7148 -0.0162 0.0040  -0.0141 122 GLU B OE1 
5005 O OE2 . GLU B 136 ? 0.4358 0.4036 0.6208 -0.0160 0.0009  -0.0101 122 GLU B OE2 
5006 N N   . PHE B 137 ? 0.3603 0.3339 0.5363 -0.0093 0.0014  -0.0093 123 PHE B N   
5007 C CA  . PHE B 137 ? 0.3976 0.3784 0.5757 -0.0082 -0.0003 -0.0065 123 PHE B CA  
5008 C C   . PHE B 137 ? 0.3012 0.2872 0.4869 -0.0093 -0.0016 -0.0042 123 PHE B C   
5009 O O   . PHE B 137 ? 0.3410 0.3327 0.5292 -0.0085 -0.0031 -0.0023 123 PHE B O   
5010 C CB  . PHE B 137 ? 0.2709 0.2531 0.4428 -0.0093 -0.0036 -0.0077 123 PHE B CB  
5011 C CG  . PHE B 137 ? 0.3440 0.3213 0.5065 -0.0080 -0.0012 -0.0092 123 PHE B CG  
5012 C CD1 . PHE B 137 ? 0.3430 0.3133 0.4987 -0.0093 0.0001  -0.0133 123 PHE B CD1 
5013 C CD2 . PHE B 137 ? 0.3001 0.2793 0.4607 -0.0056 0.0006  -0.0067 123 PHE B CD2 
5014 C CE1 . PHE B 137 ? 0.2782 0.2436 0.4248 -0.0081 0.0036  -0.0151 123 PHE B CE1 
5015 C CE2 . PHE B 137 ? 0.3891 0.3637 0.5412 -0.0048 0.0040  -0.0080 123 PHE B CE2 
5016 C CZ  . PHE B 137 ? 0.4034 0.3713 0.5483 -0.0059 0.0058  -0.0122 123 PHE B CZ  
5017 N N   . ARG B 138 ? 0.3265 0.3098 0.5156 -0.0108 -0.0003 -0.0041 124 ARG B N   
5018 C CA  . ARG B 138 ? 0.3457 0.3331 0.5409 -0.0122 -0.0002 -0.0022 124 ARG B CA  
5019 C C   . ARG B 138 ? 0.3544 0.3389 0.5503 -0.0108 0.0025  0.0004  124 ARG B C   
5020 O O   . ARG B 138 ? 0.3064 0.2925 0.5054 -0.0122 0.0036  0.0020  124 ARG B O   
5021 C CB  . ARG B 138 ? 0.4120 0.3995 0.6106 -0.0167 -0.0014 -0.0042 124 ARG B CB  
5022 C CG  . ARG B 138 ? 0.4856 0.4747 0.6822 -0.0184 -0.0054 -0.0073 124 ARG B CG  
5023 C CD  . ARG B 138 ? 0.5652 0.5602 0.7695 -0.0223 -0.0082 -0.0084 124 ARG B CD  
5024 N NE  . ARG B 138 ? 0.6731 0.6705 0.8750 -0.0234 -0.0136 -0.0108 124 ARG B NE  
5025 C CZ  . ARG B 138 ? 0.7226 0.7248 0.9308 -0.0272 -0.0177 -0.0128 124 ARG B CZ  
5026 N NH1 . ARG B 138 ? 0.7069 0.7125 0.9253 -0.0306 -0.0161 -0.0128 124 ARG B NH1 
5027 N NH2 . ARG B 138 ? 0.6999 0.7036 0.9040 -0.0278 -0.0237 -0.0148 124 ARG B NH2 
5028 N N   . HIS B 139 ? 0.3040 0.2841 0.4970 -0.0080 0.0037  0.0009  125 HIS B N   
5029 C CA  . HIS B 139 ? 0.3214 0.2988 0.5146 -0.0063 0.0049  0.0037  125 HIS B CA  
5030 C C   . HIS B 139 ? 0.3335 0.3161 0.5281 -0.0057 0.0047  0.0058  125 HIS B C   
5031 O O   . HIS B 139 ? 0.2523 0.2335 0.4463 -0.0067 0.0056  0.0077  125 HIS B O   
5032 C CB  . HIS B 139 ? 0.2912 0.2657 0.4837 -0.0028 0.0053  0.0037  125 HIS B CB  
5033 C CG  . HIS B 139 ? 0.3382 0.3055 0.5297 -0.0025 0.0064  0.0019  125 HIS B CG  
5034 N ND1 . HIS B 139 ? 0.3075 0.2682 0.4982 -0.0045 0.0068  0.0023  125 HIS B ND1 
5035 C CD2 . HIS B 139 ? 0.3474 0.3123 0.5384 -0.0004 0.0078  -0.0004 125 HIS B CD2 
5036 C CE1 . HIS B 139 ? 0.4206 0.3748 0.6105 -0.0034 0.0079  0.0001  125 HIS B CE1 
5037 N NE2 . HIS B 139 ? 0.3300 0.2867 0.5201 -0.0008 0.0087  -0.0017 125 HIS B NE2 
5038 N N   . PHE B 140 ? 0.2333 0.2209 0.4286 -0.0042 0.0039  0.0056  126 PHE B N   
5039 C CA  . PHE B 140 ? 0.2581 0.2492 0.4543 -0.0032 0.0038  0.0072  126 PHE B CA  
5040 C C   . PHE B 140 ? 0.2930 0.2879 0.4919 -0.0051 0.0044  0.0071  126 PHE B C   
5041 O O   . PHE B 140 ? 0.2576 0.2533 0.4565 -0.0049 0.0056  0.0082  126 PHE B O   
5042 C CB  . PHE B 140 ? 0.2466 0.2405 0.4430 -0.0012 0.0032  0.0071  126 PHE B CB  
5043 C CG  . PHE B 140 ? 0.2607 0.2521 0.4561 0.0003  0.0037  0.0064  126 PHE B CG  
5044 C CD1 . PHE B 140 ? 0.2396 0.2275 0.4358 0.0014  0.0040  0.0070  126 PHE B CD1 
5045 C CD2 . PHE B 140 ? 0.2167 0.2090 0.4104 0.0007  0.0040  0.0052  126 PHE B CD2 
5046 C CE1 . PHE B 140 ? 0.2514 0.2377 0.4487 0.0032  0.0051  0.0060  126 PHE B CE1 
5047 C CE2 . PHE B 140 ? 0.2497 0.2397 0.4427 0.0019  0.0058  0.0042  126 PHE B CE2 
5048 C CZ  . PHE B 140 ? 0.2244 0.2118 0.4203 0.0034  0.0066  0.0044  126 PHE B CZ  
5049 N N   . TYR B 141 ? 0.3040 0.3013 0.5055 -0.0069 0.0035  0.0055  127 TYR B N   
5050 C CA  . TYR B 141 ? 0.2894 0.2913 0.4963 -0.0089 0.0042  0.0052  127 TYR B CA  
5051 C C   . TYR B 141 ? 0.2901 0.2886 0.4964 -0.0111 0.0075  0.0062  127 TYR B C   
5052 O O   . TYR B 141 ? 0.2598 0.2602 0.4675 -0.0113 0.0100  0.0070  127 TYR B O   
5053 C CB  . TYR B 141 ? 0.2979 0.3029 0.5084 -0.0110 0.0017  0.0032  127 TYR B CB  
5054 C CG  . TYR B 141 ? 0.2813 0.2921 0.5003 -0.0135 0.0023  0.0025  127 TYR B CG  
5055 C CD1 . TYR B 141 ? 0.3051 0.3231 0.5306 -0.0120 0.0015  0.0027  127 TYR B CD1 
5056 C CD2 . TYR B 141 ? 0.3335 0.3425 0.5550 -0.0175 0.0039  0.0016  127 TYR B CD2 
5057 C CE1 . TYR B 141 ? 0.3399 0.3644 0.5756 -0.0141 0.0023  0.0019  127 TYR B CE1 
5058 C CE2 . TYR B 141 ? 0.3778 0.3932 0.6091 -0.0204 0.0050  0.0008  127 TYR B CE2 
5059 C CZ  . TYR B 141 ? 0.3923 0.4161 0.6313 -0.0185 0.0043  0.0009  127 TYR B CZ  
5060 O OH  . TYR B 141 ? 0.4932 0.5246 0.7443 -0.0209 0.0058  -0.0001 127 TYR B OH  
5061 N N   . HIS B 142 ? 0.2598 0.2522 0.4631 -0.0127 0.0079  0.0062  128 HIS B N   
5062 C CA  . HIS B 142 ? 0.3078 0.2952 0.5090 -0.0150 0.0110  0.0078  128 HIS B CA  
5063 C C   . HIS B 142 ? 0.3086 0.2925 0.5037 -0.0130 0.0120  0.0103  128 HIS B C   
5064 O O   . HIS B 142 ? 0.3248 0.3068 0.5174 -0.0147 0.0152  0.0116  128 HIS B O   
5065 C CB  . HIS B 142 ? 0.2941 0.2742 0.4931 -0.0168 0.0108  0.0075  128 HIS B CB  
5066 C CG  . HIS B 142 ? 0.4375 0.4200 0.6418 -0.0200 0.0097  0.0047  128 HIS B CG  
5067 N ND1 . HIS B 142 ? 0.4828 0.4716 0.6944 -0.0234 0.0108  0.0036  128 HIS B ND1 
5068 C CD2 . HIS B 142 ? 0.4949 0.4743 0.6982 -0.0205 0.0075  0.0022  128 HIS B CD2 
5069 C CE1 . HIS B 142 ? 0.4200 0.4099 0.6352 -0.0260 0.0084  0.0008  128 HIS B CE1 
5070 N NE2 . HIS B 142 ? 0.4996 0.4832 0.7087 -0.0244 0.0065  -0.0002 128 HIS B NE2 
5071 N N   . MET B 143 ? 0.2295 0.2124 0.4219 -0.0096 0.0095  0.0108  129 MET B N   
5072 C CA  . MET B 143 ? 0.3042 0.2841 0.4911 -0.0079 0.0092  0.0128  129 MET B CA  
5073 C C   . MET B 143 ? 0.2880 0.2719 0.4749 -0.0081 0.0110  0.0124  129 MET B C   
5074 O O   . MET B 143 ? 0.2716 0.2517 0.4520 -0.0081 0.0119  0.0137  129 MET B O   
5075 C CB  . MET B 143 ? 0.3275 0.3075 0.5145 -0.0046 0.0060  0.0129  129 MET B CB  
5076 C CG  . MET B 143 ? 0.2751 0.2498 0.4617 -0.0036 0.0047  0.0134  129 MET B CG  
5077 S SD  . MET B 143 ? 0.3382 0.3156 0.5291 -0.0002 0.0028  0.0121  129 MET B SD  
5078 C CE  . MET B 143 ? 0.2357 0.2144 0.4259 0.0019  0.0002  0.0139  129 MET B CE  
5079 N N   . SER B 144 ? 0.2589 0.2496 0.4522 -0.0081 0.0115  0.0105  130 SER B N   
5080 C CA  . SER B 144 ? 0.3205 0.3147 0.5153 -0.0077 0.0137  0.0098  130 SER B CA  
5081 C C   . SER B 144 ? 0.3564 0.3512 0.5528 -0.0104 0.0185  0.0096  130 SER B C   
5082 O O   . SER B 144 ? 0.2687 0.2649 0.4650 -0.0101 0.0217  0.0088  130 SER B O   
5083 C CB  . SER B 144 ? 0.3560 0.3568 0.5578 -0.0059 0.0120  0.0084  130 SER B CB  
5084 O OG  . SER B 144 ? 0.4002 0.4001 0.5995 -0.0034 0.0096  0.0086  130 SER B OG  
5085 N N   . GLU B 145 ? 0.2895 0.2830 0.4876 -0.0133 0.0198  0.0099  131 GLU B N   
5086 C CA  . GLU B 145 ? 0.3625 0.3574 0.5641 -0.0167 0.0251  0.0096  131 GLU B CA  
5087 C C   . GLU B 145 ? 0.3205 0.3102 0.5133 -0.0174 0.0299  0.0108  131 GLU B C   
5088 O O   . GLU B 145 ? 0.3341 0.3278 0.5312 -0.0183 0.0350  0.0095  131 GLU B O   
5089 C CB  . GLU B 145 ? 0.3963 0.3882 0.5994 -0.0203 0.0255  0.0102  131 GLU B CB  
5090 C CG  . GLU B 145 ? 0.5131 0.5095 0.7248 -0.0245 0.0305  0.0092  131 GLU B CG  
5091 C CD  . GLU B 145 ? 0.7835 0.7749 0.9888 -0.0269 0.0375  0.0109  131 GLU B CD  
5092 O OE1 . GLU B 145 ? 0.5555 0.5367 0.7480 -0.0270 0.0377  0.0136  131 GLU B OE1 
5093 O OE2 . GLU B 145 ? 0.6371 0.6347 0.8503 -0.0286 0.0429  0.0095  131 GLU B OE2 
5094 N N   . PRO B 146 ? 0.3481 0.3288 0.5286 -0.0170 0.0287  0.0131  132 PRO B N   
5095 C CA  . PRO B 146 ? 0.3769 0.3514 0.5465 -0.0182 0.0331  0.0142  132 PRO B CA  
5096 C C   . PRO B 146 ? 0.3755 0.3525 0.5435 -0.0159 0.0342  0.0121  132 PRO B C   
5097 O O   . PRO B 146 ? 0.3447 0.3171 0.5040 -0.0172 0.0391  0.0120  132 PRO B O   
5098 C CB  . PRO B 146 ? 0.3938 0.3584 0.5511 -0.0176 0.0291  0.0174  132 PRO B CB  
5099 C CG  . PRO B 146 ? 0.2731 0.2383 0.4367 -0.0172 0.0251  0.0180  132 PRO B CG  
5100 C CD  . PRO B 146 ? 0.3598 0.3351 0.5357 -0.0157 0.0235  0.0150  132 PRO B CD  
5101 N N   . ILE B 147 ? 0.2771 0.2600 0.4521 -0.0128 0.0302  0.0103  133 ILE B N   
5102 C CA  . ILE B 147 ? 0.3630 0.3465 0.5361 -0.0107 0.0311  0.0083  133 ILE B CA  
5103 C C   . ILE B 147 ? 0.3166 0.3091 0.5031 -0.0091 0.0330  0.0058  133 ILE B C   
5104 O O   . ILE B 147 ? 0.3400 0.3336 0.5277 -0.0066 0.0321  0.0042  133 ILE B O   
5105 C CB  . ILE B 147 ? 0.2672 0.2479 0.4352 -0.0084 0.0248  0.0087  133 ILE B CB  
5106 C CG1 . ILE B 147 ? 0.2862 0.2720 0.4630 -0.0067 0.0198  0.0091  133 ILE B CG1 
5107 C CG2 . ILE B 147 ? 0.3129 0.2849 0.4676 -0.0095 0.0226  0.0110  133 ILE B CG2 
5108 C CD1 . ILE B 147 ? 0.3114 0.2956 0.4857 -0.0047 0.0145  0.0094  133 ILE B CD1 
5109 N N   . THR B 148 ? 0.3073 0.3058 0.5042 -0.0106 0.0352  0.0056  134 THR B N   
5110 C CA  . THR B 148 ? 0.3132 0.3207 0.5240 -0.0090 0.0367  0.0035  134 THR B CA  
5111 C C   . THR B 148 ? 0.2891 0.3010 0.5078 -0.0121 0.0432  0.0028  134 THR B C   
5112 O O   . THR B 148 ? 0.2425 0.2515 0.4582 -0.0158 0.0447  0.0043  134 THR B O   
5113 C CB  . THR B 148 ? 0.2978 0.3112 0.5173 -0.0073 0.0301  0.0038  134 THR B CB  
5114 O OG1 . THR B 148 ? 0.3798 0.3934 0.6007 -0.0103 0.0283  0.0048  134 THR B OG1 
5115 C CG2 . THR B 148 ? 0.2241 0.2336 0.4369 -0.0047 0.0248  0.0046  134 THR B CG2 
5116 N N   . VAL B 149 ? 0.3533 0.3719 0.5829 -0.0105 0.0473  0.0006  135 VAL B N   
5117 C CA  . VAL B 149 ? 0.3223 0.3474 0.5632 -0.0134 0.0537  -0.0004 135 VAL B CA  
5118 C C   . VAL B 149 ? 0.2655 0.3004 0.5223 -0.0141 0.0489  -0.0005 135 VAL B C   
5119 O O   . VAL B 149 ? 0.2343 0.2748 0.5015 -0.0176 0.0528  -0.0011 135 VAL B O   
5120 C CB  . VAL B 149 ? 0.3327 0.3618 0.5810 -0.0113 0.0612  -0.0032 135 VAL B CB  
5121 C CG1 . VAL B 149 ? 0.4567 0.4755 0.6883 -0.0124 0.0681  -0.0037 135 VAL B CG1 
5122 C CG2 . VAL B 149 ? 0.2381 0.2720 0.4948 -0.0058 0.0567  -0.0045 135 VAL B CG2 
5123 N N   . ALA B 150 ? 0.2457 0.2827 0.5045 -0.0111 0.0406  -0.0001 136 ALA B N   
5124 C CA  . ALA B 150 ? 0.2192 0.2647 0.4909 -0.0117 0.0350  -0.0003 136 ALA B CA  
5125 C C   . ALA B 150 ? 0.2710 0.3136 0.5361 -0.0093 0.0265  0.0009  136 ALA B C   
5126 O O   . ALA B 150 ? 0.2511 0.2893 0.5088 -0.0059 0.0251  0.0015  136 ALA B O   
5127 C CB  . ALA B 150 ? 0.2209 0.2778 0.5109 -0.0093 0.0359  -0.0021 136 ALA B CB  
5128 N N   . GLN B 151 ? 0.2127 0.2572 0.4803 -0.0116 0.0213  0.0010  137 GLN B N   
5129 C CA  . GLN B 151 ? 0.2661 0.3079 0.5273 -0.0096 0.0141  0.0018  137 GLN B CA  
5130 C C   . GLN B 151 ? 0.2163 0.2641 0.4857 -0.0115 0.0084  0.0009  137 GLN B C   
5131 O O   . GLN B 151 ? 0.2110 0.2638 0.4898 -0.0153 0.0099  -0.0004 137 GLN B O   
5132 C CB  . GLN B 151 ? 0.2699 0.3016 0.5163 -0.0105 0.0141  0.0030  137 GLN B CB  
5133 C CG  . GLN B 151 ? 0.3877 0.4144 0.6299 -0.0145 0.0190  0.0034  137 GLN B CG  
5134 C CD  . GLN B 151 ? 0.6110 0.6283 0.8405 -0.0148 0.0175  0.0048  137 GLN B CD  
5135 O OE1 . GLN B 151 ? 0.4591 0.4731 0.6820 -0.0118 0.0150  0.0055  137 GLN B OE1 
5136 N NE2 . GLN B 151 ? 0.5099 0.5227 0.7371 -0.0184 0.0192  0.0052  137 GLN B NE2 
5137 N N   . ALA B 152 ? 0.2082 0.2552 0.4734 -0.0093 0.0019  0.0014  138 ALA B N   
5138 C CA  . ALA B 152 ? 0.3066 0.3578 0.5763 -0.0111 -0.0047 0.0004  138 ALA B CA  
5139 C C   . ALA B 152 ? 0.2616 0.3063 0.5185 -0.0097 -0.0096 0.0011  138 ALA B C   
5140 O O   . ALA B 152 ? 0.2185 0.2588 0.4678 -0.0063 -0.0091 0.0027  138 ALA B O   
5141 C CB  . ALA B 152 ? 0.2092 0.2711 0.4939 -0.0090 -0.0084 0.0001  138 ALA B CB  
5142 N N   . ILE B 153 ? 0.2651 0.3088 0.5197 -0.0128 -0.0138 -0.0005 139 ILE B N   
5143 C CA  . ILE B 153 ? 0.2779 0.3169 0.5216 -0.0117 -0.0190 -0.0004 139 ILE B CA  
5144 C C   . ILE B 153 ? 0.3187 0.3648 0.5691 -0.0110 -0.0265 -0.0006 139 ILE B C   
5145 O O   . ILE B 153 ? 0.3289 0.3804 0.5876 -0.0144 -0.0299 -0.0027 139 ILE B O   
5146 C CB  . ILE B 153 ? 0.2372 0.2690 0.4721 -0.0153 -0.0188 -0.0025 139 ILE B CB  
5147 C CG1 . ILE B 153 ? 0.5009 0.5258 0.7302 -0.0152 -0.0122 -0.0017 139 ILE B CG1 
5148 C CG2 . ILE B 153 ? 0.2986 0.3255 0.5217 -0.0142 -0.0234 -0.0028 139 ILE B CG2 
5149 C CD1 . ILE B 153 ? 0.3728 0.3903 0.5961 -0.0186 -0.0113 -0.0037 139 ILE B CD1 
5150 N N   . LEU B 154 ? 0.2855 0.3314 0.5326 -0.0067 -0.0294 0.0018  140 LEU B N   
5151 C CA  . LEU B 154 ? 0.2301 0.2824 0.4836 -0.0050 -0.0372 0.0026  140 LEU B CA  
5152 C C   . LEU B 154 ? 0.3642 0.4128 0.6071 -0.0074 -0.0442 0.0013  140 LEU B C   
5153 O O   . LEU B 154 ? 0.2809 0.3202 0.5079 -0.0074 -0.0432 0.0016  140 LEU B O   
5154 C CB  . LEU B 154 ? 0.2978 0.3491 0.5500 0.0005  -0.0379 0.0061  140 LEU B CB  
5155 C CG  . LEU B 154 ? 0.3082 0.3631 0.5713 0.0031  -0.0316 0.0067  140 LEU B CG  
5156 C CD1 . LEU B 154 ? 0.2215 0.2740 0.4829 0.0085  -0.0326 0.0099  140 LEU B CD1 
5157 C CD2 . LEU B 154 ? 0.2221 0.2884 0.5042 0.0020  -0.0319 0.0049  140 LEU B CD2 
5158 N N   . THR B 155 ? 0.2615 0.3173 0.5133 -0.0097 -0.0512 -0.0004 141 THR B N   
5159 C CA  . THR B 155 ? 0.3048 0.3575 0.5467 -0.0123 -0.0592 -0.0021 141 THR B CA  
5160 C C   . THR B 155 ? 0.2696 0.3294 0.5180 -0.0097 -0.0693 -0.0003 141 THR B C   
5161 O O   . THR B 155 ? 0.2789 0.3474 0.5431 -0.0064 -0.0697 0.0017  141 THR B O   
5162 C CB  . THR B 155 ? 0.3165 0.3702 0.5622 -0.0186 -0.0596 -0.0067 141 THR B CB  
5163 O OG1 . THR B 155 ? 0.3394 0.4056 0.6055 -0.0203 -0.0635 -0.0077 141 THR B OG1 
5164 C CG2 . THR B 155 ? 0.2754 0.3236 0.5194 -0.0206 -0.0495 -0.0078 141 THR B CG2 
5165 N N   . GLU B 156 ? 0.3172 0.3728 0.5531 -0.0113 -0.0777 -0.0010 142 GLU B N   
5166 C CA  . GLU B 156 ? 0.2804 0.3423 0.5214 -0.0092 -0.0892 0.0008  142 GLU B CA  
5167 C C   . GLU B 156 ? 0.3791 0.4556 0.6448 -0.0113 -0.0933 -0.0014 142 GLU B C   
5168 O O   . GLU B 156 ? 0.2994 0.3849 0.5781 -0.0077 -0.1006 0.0009  142 GLU B O   
5169 C CB  . GLU B 156 ? 0.4209 0.4744 0.6414 -0.0117 -0.0974 -0.0004 142 GLU B CB  
5170 C CG  . GLU B 156 ? 0.4773 0.5365 0.7008 -0.0105 -0.1115 0.0011  142 GLU B CG  
5171 C CD  . GLU B 156 ? 0.5313 0.5805 0.7310 -0.0134 -0.1192 -0.0005 142 GLU B CD  
5172 O OE1 . GLU B 156 ? 0.5118 0.5547 0.7016 -0.0188 -0.1160 -0.0054 142 GLU B OE1 
5173 O OE2 . GLU B 156 ? 0.5390 0.5854 0.7288 -0.0103 -0.1284 0.0033  142 GLU B OE2 
5174 N N   . GLN B 157 ? 0.2708 0.3499 0.5443 -0.0168 -0.0884 -0.0055 143 GLN B N   
5175 C CA  . GLN B 157 ? 0.2965 0.3891 0.5935 -0.0202 -0.0914 -0.0082 143 GLN B CA  
5176 C C   . GLN B 157 ? 0.2622 0.3639 0.5797 -0.0182 -0.0824 -0.0072 143 GLN B C   
5177 O O   . GLN B 157 ? 0.3193 0.4339 0.6592 -0.0201 -0.0843 -0.0088 143 GLN B O   
5178 C CB  . GLN B 157 ? 0.2722 0.3617 0.5664 -0.0282 -0.0908 -0.0134 143 GLN B CB  
5179 C CG  . GLN B 157 ? 0.3034 0.3877 0.5832 -0.0313 -0.1019 -0.0159 143 GLN B CG  
5180 C CD  . GLN B 157 ? 0.6113 0.6912 0.8882 -0.0394 -0.1010 -0.0216 143 GLN B CD  
5181 O OE1 . GLN B 157 ? 0.5255 0.6116 0.8192 -0.0435 -0.0960 -0.0237 143 GLN B OE1 
5182 N NE2 . GLN B 157 ? 0.4974 0.5657 0.7525 -0.0417 -0.1056 -0.0241 143 GLN B NE2 
5183 N N   . ASN B 158 ? 0.2525 0.3478 0.5633 -0.0146 -0.0726 -0.0048 144 ASN B N   
5184 C CA  . ASN B 158 ? 0.2366 0.3384 0.5636 -0.0133 -0.0632 -0.0045 144 ASN B CA  
5185 C C   . ASN B 158 ? 0.3152 0.4156 0.6418 -0.0061 -0.0595 -0.0008 144 ASN B C   
5186 O O   . ASN B 158 ? 0.2738 0.3792 0.6130 -0.0046 -0.0515 -0.0008 144 ASN B O   
5187 C CB  . ASN B 158 ? 0.2320 0.3268 0.5526 -0.0178 -0.0527 -0.0064 144 ASN B CB  
5188 C CG  . ASN B 158 ? 0.2887 0.3696 0.5876 -0.0156 -0.0477 -0.0046 144 ASN B CG  
5189 O OD1 . ASN B 158 ? 0.2327 0.3094 0.5220 -0.0108 -0.0504 -0.0019 144 ASN B OD1 
5190 N ND2 . ASN B 158 ? 0.2633 0.3372 0.5551 -0.0191 -0.0405 -0.0060 144 ASN B ND2 
5191 N N   . ALA B 159 ? 0.3184 0.3096 0.5289 -0.0252 -0.0883 0.0272  145 ALA B N   
5192 C CA  . ALA B 159 ? 0.3287 0.3249 0.5500 -0.0128 -0.0809 0.0257  145 ALA B CA  
5193 C C   . ALA B 159 ? 0.3758 0.3931 0.6263 -0.0080 -0.0782 0.0286  145 ALA B C   
5194 O O   . ALA B 159 ? 0.3602 0.3785 0.6167 -0.0019 -0.0694 0.0252  145 ALA B O   
5195 C CB  . ALA B 159 ? 0.3311 0.3224 0.5439 -0.0100 -0.0849 0.0277  145 ALA B CB  
5196 N N   . CYS B 160 ? 0.3019 0.3359 0.5702 -0.0103 -0.0856 0.0351  146 CYS B N   
5197 C CA  . CYS B 160 ? 0.4711 0.5233 0.7664 -0.0013 -0.0818 0.0379  146 CYS B CA  
5198 C C   . CYS B 160 ? 0.3276 0.3918 0.6362 -0.0018 -0.0738 0.0360  146 CYS B C   
5199 O O   . CYS B 160 ? 0.3256 0.3931 0.6446 0.0073  -0.0645 0.0335  146 CYS B O   
5200 C CB  . CYS B 160 ? 0.3867 0.4552 0.6994 -0.0014 -0.0921 0.0468  146 CYS B CB  
5201 S SG  . CYS B 160 ? 0.4299 0.4835 0.7284 0.0016  -0.0995 0.0491  146 CYS B SG  
5202 N N   . TYR B 161 ? 0.2870 0.3556 0.5924 -0.0135 -0.0769 0.0372  147 TYR B N   
5203 C CA  . TYR B 161 ? 0.2476 0.3287 0.5650 -0.0150 -0.0688 0.0358  147 TYR B CA  
5204 C C   . TYR B 161 ? 0.2613 0.3226 0.5602 -0.0141 -0.0599 0.0279  147 TYR B C   
5205 O O   . TYR B 161 ? 0.2910 0.3591 0.5987 -0.0113 -0.0505 0.0255  147 TYR B O   
5206 C CB  . TYR B 161 ? 0.3005 0.3967 0.6232 -0.0297 -0.0757 0.0416  147 TYR B CB  
5207 C CG  . TYR B 161 ? 0.3848 0.4586 0.6777 -0.0439 -0.0825 0.0397  147 TYR B CG  
5208 C CD1 . TYR B 161 ? 0.3694 0.4298 0.6469 -0.0499 -0.0773 0.0348  147 TYR B CD1 
5209 C CD2 . TYR B 161 ? 0.3777 0.4420 0.6560 -0.0520 -0.0946 0.0431  147 TYR B CD2 
5210 C CE1 . TYR B 161 ? 0.4698 0.5049 0.7171 -0.0617 -0.0835 0.0330  147 TYR B CE1 
5211 C CE2 . TYR B 161 ? 0.4178 0.4565 0.6644 -0.0645 -0.1001 0.0407  147 TYR B CE2 
5212 C CZ  . TYR B 161 ? 0.5537 0.5768 0.7847 -0.0686 -0.0944 0.0355  147 TYR B CZ  
5213 O OH  . TYR B 161 ? 0.4121 0.4048 0.6085 -0.0797 -0.0998 0.0330  147 TYR B OH  
5214 N N   . GLU B 162 ? 0.2917 0.3293 0.5653 -0.0155 -0.0621 0.0242  148 GLU B N   
5215 C CA  . GLU B 162 ? 0.2729 0.2945 0.5321 -0.0124 -0.0542 0.0184  148 GLU B CA  
5216 C C   . GLU B 162 ? 0.2858 0.3086 0.5524 -0.0015 -0.0472 0.0166  148 GLU B C   
5217 O O   . GLU B 162 ? 0.2360 0.2554 0.5010 0.0001  -0.0395 0.0134  148 GLU B O   
5218 C CB  . GLU B 162 ? 0.3313 0.3298 0.5639 -0.0141 -0.0574 0.0159  148 GLU B CB  
5219 C CG  . GLU B 162 ? 0.3444 0.3306 0.5600 -0.0254 -0.0620 0.0156  148 GLU B CG  
5220 C CD  . GLU B 162 ? 0.3234 0.3093 0.5393 -0.0303 -0.0570 0.0140  148 GLU B CD  
5221 O OE1 . GLU B 162 ? 0.3797 0.3854 0.6138 -0.0356 -0.0560 0.0167  148 GLU B OE1 
5222 O OE2 . GLU B 162 ? 0.4317 0.3985 0.6297 -0.0286 -0.0538 0.0107  148 GLU B OE2 
5223 N N   . ILE B 163 ? 0.2251 0.2503 0.4972 0.0046  -0.0505 0.0189  149 ILE B N   
5224 C CA  . ILE B 163 ? 0.2198 0.2433 0.4965 0.0133  -0.0451 0.0179  149 ILE B CA  
5225 C C   . ILE B 163 ? 0.2525 0.2874 0.5460 0.0168  -0.0377 0.0172  149 ILE B C   
5226 O O   . ILE B 163 ? 0.2600 0.2879 0.5490 0.0193  -0.0296 0.0135  149 ILE B O   
5227 C CB  . ILE B 163 ? 0.2392 0.2622 0.5180 0.0179  -0.0515 0.0216  149 ILE B CB  
5228 C CG1 . ILE B 163 ? 0.3627 0.3730 0.6216 0.0158  -0.0552 0.0213  149 ILE B CG1 
5229 C CG2 . ILE B 163 ? 0.2733 0.2937 0.5582 0.0262  -0.0469 0.0214  149 ILE B CG2 
5230 C CD1 . ILE B 163 ? 0.2166 0.2272 0.4745 0.0162  -0.0637 0.0257  149 ILE B CD1 
5231 N N   . ASP B 164 ? 0.2199 0.2735 0.5324 0.0164  -0.0400 0.0212  150 ASP B N   
5232 C CA  . ASP B 164 ? 0.2168 0.2849 0.5476 0.0218  -0.0312 0.0210  150 ASP B CA  
5233 C C   . ASP B 164 ? 0.2906 0.3586 0.6159 0.0151  -0.0231 0.0169  150 ASP B C   
5234 O O   . ASP B 164 ? 0.2655 0.3329 0.5931 0.0199  -0.0125 0.0135  150 ASP B O   
5235 C CB  . ASP B 164 ? 0.2204 0.3143 0.5760 0.0228  -0.0362 0.0282  150 ASP B CB  
5236 C CG  . ASP B 164 ? 0.2427 0.3368 0.6059 0.0311  -0.0436 0.0331  150 ASP B CG  
5237 O OD1 . ASP B 164 ? 0.3157 0.3905 0.6666 0.0377  -0.0424 0.0303  150 ASP B OD1 
5238 O OD2 . ASP B 164 ? 0.3354 0.4492 0.7161 0.0301  -0.0516 0.0408  150 ASP B OD2 
5239 N N   . ARG B 165 ? 0.2353 0.3008 0.5502 0.0036  -0.0280 0.0172  151 ARG B N   
5240 C CA  . ARG B 165 ? 0.2387 0.3022 0.5463 -0.0042 -0.0218 0.0142  151 ARG B CA  
5241 C C   . ARG B 165 ? 0.2622 0.3056 0.5525 -0.0014 -0.0155 0.0090  151 ARG B C   
5242 O O   . ARG B 165 ? 0.2520 0.2957 0.5418 -0.0022 -0.0064 0.0061  151 ARG B O   
5243 C CB  . ARG B 165 ? 0.2383 0.2963 0.5331 -0.0169 -0.0299 0.0159  151 ARG B CB  
5244 C CG  . ARG B 165 ? 0.2433 0.2905 0.5234 -0.0251 -0.0254 0.0128  151 ARG B CG  
5245 C CD  . ARG B 165 ? 0.3897 0.4243 0.6521 -0.0371 -0.0339 0.0142  151 ARG B CD  
5246 N NE  . ARG B 165 ? 0.2650 0.2750 0.5062 -0.0332 -0.0386 0.0120  151 ARG B NE  
5247 C CZ  . ARG B 165 ? 0.3855 0.3778 0.6116 -0.0295 -0.0351 0.0089  151 ARG B CZ  
5248 N NH1 . ARG B 165 ? 0.2414 0.2346 0.4683 -0.0306 -0.0280 0.0073  151 ARG B NH1 
5249 N NH2 . ARG B 165 ? 0.2324 0.2069 0.4423 -0.0244 -0.0386 0.0079  151 ARG B NH2 
5250 N N   . VAL B 166 ? 0.2272 0.2541 0.5029 0.0009  -0.0203 0.0083  152 VAL B N   
5251 C CA  . VAL B 166 ? 0.2689 0.2801 0.5294 0.0020  -0.0161 0.0054  152 VAL B CA  
5252 C C   . VAL B 166 ? 0.2653 0.2754 0.5298 0.0083  -0.0087 0.0035  152 VAL B C   
5253 O O   . VAL B 166 ? 0.2440 0.2467 0.5000 0.0057  -0.0019 0.0007  152 VAL B O   
5254 C CB  . VAL B 166 ? 0.3497 0.3493 0.5972 0.0041  -0.0224 0.0067  152 VAL B CB  
5255 C CG1 . VAL B 166 ? 0.2401 0.2297 0.4773 0.0061  -0.0191 0.0061  152 VAL B CG1 
5256 C CG2 . VAL B 166 ? 0.3334 0.3257 0.5690 -0.0013 -0.0269 0.0070  152 VAL B CG2 
5257 N N   . LEU B 167 ? 0.2661 0.2807 0.5411 0.0161  -0.0103 0.0050  153 LEU B N   
5258 C CA  . LEU B 167 ? 0.3204 0.3277 0.5949 0.0231  -0.0034 0.0029  153 LEU B CA  
5259 C C   . LEU B 167 ? 0.3316 0.3470 0.6147 0.0246  0.0076  0.0000  153 LEU B C   
5260 O O   . LEU B 167 ? 0.2989 0.3012 0.5705 0.0254  0.0160  -0.0040 153 LEU B O   
5261 C CB  . LEU B 167 ? 0.2932 0.3018 0.5767 0.0318  -0.0083 0.0059  153 LEU B CB  
5262 C CG  . LEU B 167 ? 0.3963 0.3939 0.6674 0.0305  -0.0170 0.0084  153 LEU B CG  
5263 C CD1 . LEU B 167 ? 0.3707 0.3686 0.6494 0.0377  -0.0225 0.0120  153 LEU B CD1 
5264 C CD2 . LEU B 167 ? 0.3121 0.2922 0.5638 0.0272  -0.0141 0.0065  153 LEU B CD2 
5265 N N   . THR B 168 ? 0.2083 0.2456 0.5101 0.0238  0.0078  0.0024  154 THR B N   
5266 C CA  . THR B 168 ? 0.2817 0.3323 0.5941 0.0250  0.0194  0.0005  154 THR B CA  
5267 C C   . THR B 168 ? 0.2923 0.3331 0.5874 0.0147  0.0254  -0.0034 154 THR B C   
5268 O O   . THR B 168 ? 0.3195 0.3565 0.6099 0.0164  0.0372  -0.0075 154 THR B O   
5269 C CB  . THR B 168 ? 0.2597 0.3400 0.5963 0.0230  0.0164  0.0061  154 THR B CB  
5270 O OG1 . THR B 168 ? 0.3341 0.4244 0.6880 0.0334  0.0111  0.0107  154 THR B OG1 
5271 C CG2 . THR B 168 ? 0.2968 0.3957 0.6457 0.0232  0.0294  0.0051  154 THR B CG2 
5272 N N   . THR B 169 ? 0.2122 0.2474 0.4960 0.0041  0.0175  -0.0021 155 THR B N   
5273 C CA  . THR B 169 ? 0.2865 0.3100 0.5524 -0.0056 0.0212  -0.0047 155 THR B CA  
5274 C C   . THR B 169 ? 0.3344 0.3363 0.5820 -0.0036 0.0251  -0.0080 155 THR B C   
5275 O O   . THR B 169 ? 0.3662 0.3606 0.6024 -0.0081 0.0337  -0.0112 155 THR B O   
5276 C CB  . THR B 169 ? 0.3225 0.3401 0.5786 -0.0144 0.0111  -0.0020 155 THR B CB  
5277 O OG1 . THR B 169 ? 0.2876 0.3218 0.5568 -0.0185 0.0063  0.0013  155 THR B OG1 
5278 C CG2 . THR B 169 ? 0.2580 0.2640 0.4966 -0.0246 0.0137  -0.0033 155 THR B CG2 
5279 N N   . MET B 170 ? 0.3033 0.2951 0.5463 0.0017  0.0187  -0.0067 156 MET B N   
5280 C CA  . MET B 170 ? 0.3977 0.3695 0.6226 0.0017  0.0207  -0.0084 156 MET B CA  
5281 C C   . MET B 170 ? 0.4377 0.4027 0.6599 0.0068  0.0326  -0.0132 156 MET B C   
5282 O O   . MET B 170 ? 0.3547 0.3030 0.5572 0.0013  0.0383  -0.0162 156 MET B O   
5283 C CB  . MET B 170 ? 0.3235 0.2897 0.5470 0.0064  0.0121  -0.0053 156 MET B CB  
5284 C CG  . MET B 170 ? 0.3729 0.3374 0.5887 0.0011  0.0031  -0.0012 156 MET B CG  
5285 S SD  . MET B 170 ? 0.3439 0.3075 0.5612 0.0069  -0.0052 0.0027  156 MET B SD  
5286 C CE  . MET B 170 ? 0.3120 0.2562 0.5103 0.0034  -0.0027 0.0024  156 MET B CE  
5287 N N   . LEU B 171 ? 0.3144 0.2913 0.5552 0.0179  0.0364  -0.0135 157 LEU B N   
5288 C CA  . LEU B 171 ? 0.3933 0.3638 0.6328 0.0265  0.0495  -0.0182 157 LEU B CA  
5289 C C   . LEU B 171 ? 0.3936 0.3707 0.6306 0.0209  0.0616  -0.0218 157 LEU B C   
5290 O O   . LEU B 171 ? 0.4292 0.3892 0.6492 0.0220  0.0730  -0.0272 157 LEU B O   
5291 C CB  . LEU B 171 ? 0.3538 0.3407 0.6182 0.0411  0.0504  -0.0159 157 LEU B CB  
5292 C CG  . LEU B 171 ? 0.4473 0.4248 0.7124 0.0480  0.0401  -0.0126 157 LEU B CG  
5293 C CD1 . LEU B 171 ? 0.4517 0.4512 0.7454 0.0606  0.0390  -0.0083 157 LEU B CD1 
5294 C CD2 . LEU B 171 ? 0.3400 0.2845 0.5800 0.0511  0.0437  -0.0164 157 LEU B CD2 
5295 N N   . ARG B 172 ? 0.3557 0.3559 0.6073 0.0142  0.0594  -0.0189 158 ARG B N   
5296 C CA  . ARG B 172 ? 0.4198 0.4286 0.6693 0.0070  0.0704  -0.0214 158 ARG B CA  
5297 C C   . ARG B 172 ? 0.4886 0.4737 0.7082 -0.0060 0.0709  -0.0240 158 ARG B C   
5298 O O   . ARG B 172 ? 0.4591 0.4349 0.6643 -0.0088 0.0832  -0.0288 158 ARG B O   
5299 C CB  . ARG B 172 ? 0.3127 0.3498 0.5820 0.0000  0.0657  -0.0163 158 ARG B CB  
5300 C CG  . ARG B 172 ? 0.4478 0.4972 0.7161 -0.0093 0.0767  -0.0176 158 ARG B CG  
5301 C CD  . ARG B 172 ? 0.3995 0.4792 0.6891 -0.0167 0.0717  -0.0114 158 ARG B CD  
5302 N NE  . ARG B 172 ? 0.6341 0.7039 0.9140 -0.0276 0.0559  -0.0079 158 ARG B NE  
5303 C CZ  . ARG B 172 ? 0.6116 0.6880 0.9028 -0.0255 0.0437  -0.0034 158 ARG B CZ  
5304 N NH1 . ARG B 172 ? 0.4218 0.5174 0.7364 -0.0147 0.0435  -0.0007 158 ARG B NH1 
5305 N NH2 . ARG B 172 ? 0.4990 0.5609 0.7761 -0.0340 0.0315  -0.0015 158 ARG B NH2 
5306 N N   . GLU B 173 ? 0.3585 0.3340 0.5682 -0.0139 0.0577  -0.0205 159 GLU B N   
5307 C CA  . GLU B 173 ? 0.4539 0.4114 0.6386 -0.0268 0.0559  -0.0206 159 GLU B CA  
5308 C C   . GLU B 173 ? 0.4429 0.3750 0.6056 -0.0274 0.0540  -0.0216 159 GLU B C   
5309 O O   . GLU B 173 ? 0.5039 0.4203 0.6441 -0.0387 0.0537  -0.0215 159 GLU B O   
5310 C CB  . GLU B 173 ? 0.3991 0.3608 0.5850 -0.0346 0.0431  -0.0150 159 GLU B CB  
5311 C CG  . GLU B 173 ? 0.4359 0.4187 0.6393 -0.0369 0.0422  -0.0131 159 GLU B CG  
5312 C CD  . GLU B 173 ? 0.5814 0.5720 0.7827 -0.0450 0.0531  -0.0153 159 GLU B CD  
5313 O OE1 . GLU B 173 ? 0.5374 0.5127 0.7178 -0.0528 0.0583  -0.0176 159 GLU B OE1 
5314 O OE2 . GLU B 173 ? 0.6189 0.6323 0.8388 -0.0450 0.0563  -0.0140 159 GLU B OE2 
5315 N N   . ARG B 174 ? 0.3907 0.3179 0.5578 -0.0171 0.0517  -0.0218 160 ARG B N   
5316 C CA  . ARG B 174 ? 0.4089 0.3117 0.5540 -0.0196 0.0480  -0.0215 160 ARG B CA  
5317 C C   . ARG B 174 ? 0.4403 0.3402 0.5755 -0.0306 0.0356  -0.0150 160 ARG B C   
5318 O O   . ARG B 174 ? 0.4445 0.3279 0.5567 -0.0416 0.0345  -0.0139 160 ARG B O   
5319 C CB  . ARG B 174 ? 0.4221 0.3016 0.5423 -0.0228 0.0601  -0.0278 160 ARG B CB  
5320 C CG  . ARG B 174 ? 0.6144 0.4971 0.7446 -0.0090 0.0746  -0.0341 160 ARG B CG  
5321 C CD  . ARG B 174 ? 0.4581 0.3421 0.6027 0.0055  0.0709  -0.0329 160 ARG B CD  
5322 N NE  . ARG B 174 ? 0.6649 0.5471 0.8158 0.0207  0.0850  -0.0383 160 ARG B NE  
5323 C CZ  . ARG B 174 ? 0.7049 0.5784 0.8605 0.0346  0.0845  -0.0384 160 ARG B CZ  
5324 N NH1 . ARG B 174 ? 0.7676 0.6329 0.9204 0.0333  0.0707  -0.0338 160 ARG B NH1 
5325 N NH2 . ARG B 174 ? 0.8635 0.7368 1.0264 0.0506  0.0986  -0.0428 160 ARG B NH2 
5326 N N   . ARG B 175 ? 0.3513 0.2678 0.5037 -0.0275 0.0264  -0.0102 161 ARG B N   
5327 C CA  . ARG B 175 ? 0.3997 0.3174 0.5471 -0.0341 0.0158  -0.0035 161 ARG B CA  
5328 C C   . ARG B 175 ? 0.3960 0.3254 0.5586 -0.0259 0.0077  0.0004  161 ARG B C   
5329 O O   . ARG B 175 ? 0.3046 0.2416 0.4816 -0.0171 0.0094  -0.0021 161 ARG B O   
5330 C CB  . ARG B 175 ? 0.4089 0.3318 0.5559 -0.0410 0.0155  -0.0023 161 ARG B CB  
5331 C CG  . ARG B 175 ? 0.4060 0.3150 0.5318 -0.0531 0.0197  -0.0031 161 ARG B CG  
5332 C CD  . ARG B 175 ? 0.3966 0.3091 0.5206 -0.0607 0.0171  -0.0005 161 ARG B CD  
5333 N NE  . ARG B 175 ? 0.4425 0.3426 0.5463 -0.0724 0.0123  0.0045  161 ARG B NE  
5334 C CZ  . ARG B 175 ? 0.3813 0.2763 0.4740 -0.0828 0.0127  0.0057  161 ARG B CZ  
5335 N NH1 . ARG B 175 ? 0.3706 0.2720 0.4695 -0.0839 0.0182  0.0022  161 ARG B NH1 
5336 N NH2 . ARG B 175 ? 0.3617 0.2456 0.4360 -0.0938 0.0068  0.0116  161 ARG B NH2 
5337 N N   . PRO B 176 ? 0.3939 0.3254 0.5531 -0.0284 -0.0010 0.0069  162 PRO B N   
5338 C CA  . PRO B 176 ? 0.3066 0.2482 0.4771 -0.0207 -0.0073 0.0104  162 PRO B CA  
5339 C C   . PRO B 176 ? 0.2988 0.2511 0.4836 -0.0144 -0.0081 0.0089  162 PRO B C   
5340 O O   . PRO B 176 ? 0.3068 0.2599 0.4919 -0.0174 -0.0065 0.0075  162 PRO B O   
5341 C CB  . PRO B 176 ? 0.3305 0.2747 0.4943 -0.0249 -0.0144 0.0184  162 PRO B CB  
5342 C CG  . PRO B 176 ? 0.3413 0.2741 0.4885 -0.0360 -0.0133 0.0197  162 PRO B CG  
5343 C CD  . PRO B 176 ? 0.4089 0.3343 0.5533 -0.0382 -0.0052 0.0124  162 PRO B CD  
5344 N N   . GLY B 177 ? 0.3405 0.2994 0.5346 -0.0073 -0.0113 0.0096  163 GLY B N   
5345 C CA  . GLY B 177 ? 0.2678 0.2343 0.4709 -0.0028 -0.0143 0.0094  163 GLY B CA  
5346 C C   . GLY B 177 ? 0.3399 0.3100 0.5422 0.0018  -0.0199 0.0137  163 GLY B C   
5347 O O   . GLY B 177 ? 0.2902 0.2607 0.4884 0.0013  -0.0216 0.0174  163 GLY B O   
5348 N N   . TYR B 178 ? 0.2836 0.2559 0.4881 0.0054  -0.0225 0.0134  164 TYR B N   
5349 C CA  . TYR B 178 ? 0.2791 0.2539 0.4803 0.0107  -0.0258 0.0169  164 TYR B CA  
5350 C C   . TYR B 178 ? 0.2713 0.2467 0.4750 0.0140  -0.0283 0.0148  164 TYR B C   
5351 O O   . TYR B 178 ? 0.2727 0.2441 0.4763 0.0118  -0.0289 0.0120  164 TYR B O   
5352 C CB  . TYR B 178 ? 0.2230 0.1939 0.4164 0.0122  -0.0259 0.0196  164 TYR B CB  
5353 C CG  . TYR B 178 ? 0.3357 0.3095 0.5254 0.0204  -0.0270 0.0231  164 TYR B CG  
5354 C CD1 . TYR B 178 ? 0.2323 0.2005 0.4175 0.0251  -0.0277 0.0203  164 TYR B CD1 
5355 C CD2 . TYR B 178 ? 0.3336 0.3159 0.5231 0.0231  -0.0270 0.0299  164 TYR B CD2 
5356 C CE1 . TYR B 178 ? 0.2855 0.2545 0.4647 0.0338  -0.0266 0.0227  164 TYR B CE1 
5357 C CE2 . TYR B 178 ? 0.3388 0.3269 0.5266 0.0325  -0.0261 0.0336  164 TYR B CE2 
5358 C CZ  . TYR B 178 ? 0.2764 0.2565 0.4581 0.0386  -0.0250 0.0293  164 TYR B CZ  
5359 O OH  . TYR B 178 ? 0.2477 0.2318 0.4252 0.0492  -0.0221 0.0320  164 TYR B OH  
5360 N N   . LEU B 179 ? 0.2723 0.2522 0.4766 0.0175  -0.0305 0.0169  165 LEU B N   
5361 C CA  . LEU B 179 ? 0.2903 0.2695 0.4938 0.0194  -0.0337 0.0157  165 LEU B CA  
5362 C C   . LEU B 179 ? 0.3298 0.3098 0.5244 0.0246  -0.0337 0.0183  165 LEU B C   
5363 O O   . LEU B 179 ? 0.3318 0.3197 0.5276 0.0256  -0.0332 0.0224  165 LEU B O   
5364 C CB  . LEU B 179 ? 0.2663 0.2503 0.4792 0.0184  -0.0364 0.0159  165 LEU B CB  
5365 C CG  . LEU B 179 ? 0.2866 0.2730 0.5108 0.0159  -0.0354 0.0135  165 LEU B CG  
5366 C CD1 . LEU B 179 ? 0.2667 0.2570 0.5000 0.0182  -0.0376 0.0150  165 LEU B CD1 
5367 C CD2 . LEU B 179 ? 0.2444 0.2307 0.4692 0.0126  -0.0379 0.0120  165 LEU B CD2 
5368 N N   . MET B 180 ? 0.2878 0.2589 0.4719 0.0272  -0.0339 0.0163  166 MET B N   
5369 C CA  . MET B 180 ? 0.3630 0.3336 0.5368 0.0334  -0.0324 0.0177  166 MET B CA  
5370 C C   . MET B 180 ? 0.3500 0.3189 0.5205 0.0306  -0.0366 0.0166  166 MET B C   
5371 O O   . MET B 180 ? 0.2986 0.2586 0.4656 0.0259  -0.0406 0.0136  166 MET B O   
5372 C CB  . MET B 180 ? 0.2411 0.1977 0.4004 0.0395  -0.0292 0.0156  166 MET B CB  
5373 C CG  . MET B 180 ? 0.4162 0.3749 0.5660 0.0494  -0.0243 0.0177  166 MET B CG  
5374 S SD  . MET B 180 ? 0.4352 0.3673 0.5587 0.0568  -0.0211 0.0125  166 MET B SD  
5375 C CE  . MET B 180 ? 0.2832 0.2089 0.4063 0.0645  -0.0177 0.0144  166 MET B CE  
5376 N N   . LEU B 181 ? 0.2749 0.2529 0.4457 0.0319  -0.0366 0.0200  167 LEU B N   
5377 C CA  . LEU B 181 ? 0.3172 0.2945 0.4850 0.0281  -0.0417 0.0204  167 LEU B CA  
5378 C C   . LEU B 181 ? 0.4043 0.3799 0.5562 0.0323  -0.0383 0.0210  167 LEU B C   
5379 O O   . LEU B 181 ? 0.3503 0.3382 0.5037 0.0340  -0.0358 0.0254  167 LEU B O   
5380 C CB  . LEU B 181 ? 0.3137 0.3008 0.4939 0.0245  -0.0453 0.0242  167 LEU B CB  
5381 C CG  . LEU B 181 ? 0.4032 0.3895 0.5829 0.0203  -0.0524 0.0260  167 LEU B CG  
5382 C CD1 . LEU B 181 ? 0.3091 0.2888 0.4901 0.0170  -0.0576 0.0235  167 LEU B CD1 
5383 C CD2 . LEU B 181 ? 0.3449 0.3359 0.5351 0.0184  -0.0555 0.0297  167 LEU B CD2 
5384 N N   . PRO B 182 ? 0.3853 0.3451 0.5200 0.0334  -0.0377 0.0168  168 PRO B N   
5385 C CA  . PRO B 182 ? 0.3730 0.3284 0.4892 0.0372  -0.0336 0.0165  168 PRO B CA  
5386 C C   . PRO B 182 ? 0.4238 0.3867 0.5407 0.0304  -0.0391 0.0200  168 PRO B C   
5387 O O   . PRO B 182 ? 0.4137 0.3767 0.5392 0.0227  -0.0479 0.0211  168 PRO B O   
5388 C CB  . PRO B 182 ? 0.4362 0.3662 0.5302 0.0362  -0.0344 0.0105  168 PRO B CB  
5389 C CG  . PRO B 182 ? 0.3724 0.2965 0.4739 0.0356  -0.0356 0.0086  168 PRO B CG  
5390 C CD  . PRO B 182 ? 0.3269 0.2702 0.4548 0.0309  -0.0398 0.0123  168 PRO B CD  
5391 N N   . ALA B 183 ? 0.3757 0.3462 0.4839 0.0338  -0.0336 0.0225  169 ALA B N   
5392 C CA  . ALA B 183 ? 0.4834 0.4617 0.5911 0.0265  -0.0388 0.0270  169 ALA B CA  
5393 C C   . ALA B 183 ? 0.4075 0.3702 0.5026 0.0181  -0.0476 0.0251  169 ALA B C   
5394 O O   . ALA B 183 ? 0.4280 0.3945 0.5304 0.0106  -0.0567 0.0292  169 ALA B O   
5395 C CB  . ALA B 183 ? 0.4269 0.4169 0.5249 0.0307  -0.0302 0.0302  169 ALA B CB  
5396 N N   . ASP B 184 ? 0.4804 0.4240 0.5550 0.0189  -0.0457 0.0195  170 ASP B N   
5397 C CA  . ASP B 184 ? 0.4691 0.3973 0.5291 0.0085  -0.0553 0.0187  170 ASP B CA  
5398 C C   . ASP B 184 ? 0.3739 0.3043 0.4528 0.0019  -0.0662 0.0203  170 ASP B C   
5399 O O   . ASP B 184 ? 0.4029 0.3337 0.4839 -0.0072 -0.0771 0.0242  170 ASP B O   
5400 C CB  . ASP B 184 ? 0.4266 0.3294 0.4547 0.0097  -0.0505 0.0121  170 ASP B CB  
5401 C CG  . ASP B 184 ? 0.4956 0.3864 0.5237 0.0145  -0.0475 0.0073  170 ASP B CG  
5402 O OD1 . ASP B 184 ? 0.4457 0.3500 0.4936 0.0228  -0.0421 0.0082  170 ASP B OD1 
5403 O OD2 . ASP B 184 ? 0.5670 0.4337 0.5736 0.0083  -0.0515 0.0034  170 ASP B OD2 
5404 N N   . VAL B 185 ? 0.3923 0.3255 0.4857 0.0063  -0.0632 0.0182  171 VAL B N   
5405 C CA  . VAL B 185 ? 0.3867 0.3255 0.4996 0.0008  -0.0714 0.0200  171 VAL B CA  
5406 C C   . VAL B 185 ? 0.4267 0.3828 0.5627 0.0006  -0.0762 0.0257  171 VAL B C   
5407 O O   . VAL B 185 ? 0.3382 0.2996 0.4871 -0.0045 -0.0853 0.0294  171 VAL B O   
5408 C CB  . VAL B 185 ? 0.3851 0.3226 0.5057 0.0051  -0.0660 0.0164  171 VAL B CB  
5409 C CG1 . VAL B 185 ? 0.3377 0.2854 0.4805 -0.0001 -0.0724 0.0186  171 VAL B CG1 
5410 C CG2 . VAL B 185 ? 0.3583 0.2726 0.4523 0.0048  -0.0629 0.0110  171 VAL B CG2 
5411 N N   . ALA B 186 ? 0.4263 0.3909 0.5670 0.0061  -0.0706 0.0273  172 ALA B N   
5412 C CA  . ALA B 186 ? 0.3587 0.3336 0.5164 0.0059  -0.0748 0.0323  172 ALA B CA  
5413 C C   . ALA B 186 ? 0.3978 0.3713 0.5525 -0.0004 -0.0852 0.0374  172 ALA B C   
5414 O O   . ALA B 186 ? 0.3975 0.3757 0.5676 -0.0003 -0.0914 0.0417  172 ALA B O   
5415 C CB  . ALA B 186 ? 0.3010 0.2829 0.4581 0.0095  -0.0681 0.0341  172 ALA B CB  
5416 N N   . LYS B 187 ? 0.4159 0.3812 0.5493 -0.0053 -0.0871 0.0373  173 LYS B N   
5417 C CA  . LYS B 187 ? 0.4778 0.4405 0.6051 -0.0130 -0.0981 0.0429  173 LYS B CA  
5418 C C   . LYS B 187 ? 0.4471 0.4067 0.5774 -0.0196 -0.1085 0.0446  173 LYS B C   
5419 O O   . LYS B 187 ? 0.5267 0.4854 0.6541 -0.0265 -0.1196 0.0508  173 LYS B O   
5420 C CB  . LYS B 187 ? 0.5162 0.4712 0.6159 -0.0169 -0.0950 0.0424  173 LYS B CB  
5421 C CG  . LYS B 187 ? 0.6330 0.5957 0.7295 -0.0115 -0.0842 0.0420  173 LYS B CG  
5422 C CD  . LYS B 187 ? 0.6958 0.6525 0.7647 -0.0143 -0.0789 0.0408  173 LYS B CD  
5423 C CE  . LYS B 187 ? 0.8344 0.8040 0.9023 -0.0080 -0.0666 0.0412  173 LYS B CE  
5424 N NZ  . LYS B 187 ? 0.8454 0.8105 0.8866 -0.0078 -0.0581 0.0390  173 LYS B NZ  
5425 N N   . LYS B 188 ? 0.3630 0.3216 0.4981 -0.0189 -0.1062 0.0406  174 LYS B N   
5426 C CA  . LYS B 188 ? 0.3991 0.3569 0.5358 -0.0278 -0.1166 0.0434  174 LYS B CA  
5427 C C   . LYS B 188 ? 0.4318 0.4066 0.5974 -0.0271 -0.1262 0.0515  174 LYS B C   
5428 O O   . LYS B 188 ? 0.3565 0.3411 0.5431 -0.0179 -0.1217 0.0519  174 LYS B O   
5429 C CB  . LYS B 188 ? 0.3940 0.3479 0.5304 -0.0279 -0.1116 0.0379  174 LYS B CB  
5430 C CG  . LYS B 188 ? 0.4824 0.4144 0.5860 -0.0362 -0.1122 0.0336  174 LYS B CG  
5431 C CD  . LYS B 188 ? 0.4308 0.3477 0.5067 -0.0325 -0.1042 0.0292  174 LYS B CD  
5432 C CE  . LYS B 188 ? 0.6426 0.5321 0.6820 -0.0385 -0.1026 0.0234  174 LYS B CE  
5433 N NZ  . LYS B 188 ? 0.6422 0.5163 0.6504 -0.0404 -0.1001 0.0218  174 LYS B NZ  
5434 N N   . ALA B 189 ? 0.4906 0.4676 0.6557 -0.0368 -0.1395 0.0584  175 ALA B N   
5435 C CA  . ALA B 189 ? 0.5115 0.5060 0.7050 -0.0347 -0.1494 0.0678  175 ALA B CA  
5436 C C   . ALA B 189 ? 0.3471 0.3587 0.5700 -0.0275 -0.1446 0.0673  175 ALA B C   
5437 O O   . ALA B 189 ? 0.4701 0.4816 0.6904 -0.0312 -0.1403 0.0628  175 ALA B O   
5438 C CB  . ALA B 189 ? 0.4132 0.4097 0.6013 -0.0481 -0.1657 0.0767  175 ALA B CB  
5439 N N   . ALA B 190 ? 0.3609 0.3851 0.6098 -0.0170 -0.1448 0.0718  176 ALA B N   
5440 C CA  . ALA B 190 ? 0.3768 0.4189 0.6547 -0.0089 -0.1396 0.0722  176 ALA B CA  
5441 C C   . ALA B 190 ? 0.3384 0.3964 0.6430 -0.0017 -0.1480 0.0826  176 ALA B C   
5442 O O   . ALA B 190 ? 0.3383 0.3908 0.6374 -0.0030 -0.1580 0.0892  176 ALA B O   
5443 C CB  . ALA B 190 ? 0.2460 0.2817 0.5246 0.0014  -0.1245 0.0634  176 ALA B CB  
5444 N N   . THR B 191 ? 0.3470 0.4249 0.6805 0.0067  -0.1434 0.0845  177 THR B N   
5445 C CA  . THR B 191 ? 0.2572 0.3525 0.6198 0.0176  -0.1488 0.0945  177 THR B CA  
5446 C C   . THR B 191 ? 0.3152 0.4085 0.6910 0.0348  -0.1349 0.0892  177 THR B C   
5447 O O   . THR B 191 ? 0.3044 0.4006 0.6823 0.0362  -0.1226 0.0814  177 THR B O   
5448 C CB  . THR B 191 ? 0.2717 0.3984 0.6601 0.0120  -0.1564 0.1040  177 THR B CB  
5449 O OG1 . THR B 191 ? 0.3062 0.4304 0.6770 -0.0066 -0.1704 0.1089  177 THR B OG1 
5450 C CG2 . THR B 191 ? 0.2601 0.4041 0.6728 0.0249  -0.1575 0.1134  177 THR B CG2 
5451 N N   . PRO B 192 ? 0.3497 0.4344 0.7308 0.0474  -0.1365 0.0929  178 PRO B N   
5452 C CA  . PRO B 192 ? 0.2870 0.3640 0.6726 0.0627  -0.1219 0.0867  178 PRO B CA  
5453 C C   . PRO B 192 ? 0.2693 0.3720 0.6789 0.0699  -0.1127 0.0876  178 PRO B C   
5454 O O   . PRO B 192 ? 0.2593 0.3838 0.6851 0.0705  -0.1188 0.0966  178 PRO B O   
5455 C CB  . PRO B 192 ? 0.3354 0.3953 0.7131 0.0712  -0.1266 0.0913  178 PRO B CB  
5456 C CG  . PRO B 192 ? 0.3992 0.4518 0.7629 0.0585  -0.1426 0.0975  178 PRO B CG  
5457 C CD  . PRO B 192 ? 0.2771 0.3517 0.6491 0.0455  -0.1498 0.1010  178 PRO B CD  
5458 N N   . PRO B 193 ? 0.2440 0.3461 0.6561 0.0751  -0.0982 0.0791  179 PRO B N   
5459 C CA  . PRO B 193 ? 0.2427 0.3711 0.6772 0.0814  -0.0886 0.0800  179 PRO B CA  
5460 C C   . PRO B 193 ? 0.3919 0.5218 0.8355 0.0998  -0.0822 0.0827  179 PRO B C   
5461 O O   . PRO B 193 ? 0.3138 0.4166 0.7425 0.1099  -0.0785 0.0788  179 PRO B O   
5462 C CB  . PRO B 193 ? 0.2901 0.4120 0.7200 0.0803  -0.0754 0.0695  179 PRO B CB  
5463 C CG  . PRO B 193 ? 0.3494 0.4390 0.7541 0.0776  -0.0764 0.0629  179 PRO B CG  
5464 C CD  . PRO B 193 ? 0.2504 0.3277 0.6444 0.0755  -0.0900 0.0690  179 PRO B CD  
5465 N N   . VAL B 194 ? 0.2804 0.4423 0.7478 0.1040  -0.0816 0.0900  180 VAL B N   
5466 C CA  . VAL B 194 ? 0.3070 0.4754 0.7864 0.1240  -0.0740 0.0926  180 VAL B CA  
5467 C C   . VAL B 194 ? 0.3500 0.5106 0.8276 0.1362  -0.0546 0.0824  180 VAL B C   
5468 O O   . VAL B 194 ? 0.3369 0.4814 0.8091 0.1541  -0.0465 0.0797  180 VAL B O   
5469 C CB  . VAL B 194 ? 0.3669 0.5760 0.8737 0.1242  -0.0796 0.1044  180 VAL B CB  
5470 C CG1 . VAL B 194 ? 0.4674 0.6936 0.9923 0.1448  -0.0658 0.1044  180 VAL B CG1 
5471 C CG2 . VAL B 194 ? 0.3602 0.5677 0.8658 0.1209  -0.0971 0.1149  180 VAL B CG2 
5472 N N   . ASN B 195 ? 0.2709 0.4410 0.7512 0.1266  -0.0471 0.0768  181 ASN B N   
5473 C CA  . ASN B 195 ? 0.3636 0.5290 0.8430 0.1361  -0.0285 0.0677  181 ASN B CA  
5474 C C   . ASN B 195 ? 0.3269 0.4585 0.7815 0.1292  -0.0247 0.0572  181 ASN B C   
5475 O O   . ASN B 195 ? 0.4253 0.5558 0.8743 0.1130  -0.0322 0.0562  181 ASN B O   
5476 C CB  . ASN B 195 ? 0.4025 0.6060 0.9046 0.1307  -0.0214 0.0698  181 ASN B CB  
5477 C CG  . ASN B 195 ? 0.5565 0.7988 1.0844 0.1329  -0.0281 0.0819  181 ASN B CG  
5478 O OD1 . ASN B 195 ? 0.6458 0.8961 1.1764 0.1224  -0.0446 0.0905  181 ASN B OD1 
5479 N ND2 . ASN B 195 ? 0.3540 0.6206 0.9003 0.1464  -0.0154 0.0829  181 ASN B ND2 
5480 N N   . ALA B 196 ? 0.2936 0.3969 0.7322 0.1415  -0.0133 0.0496  182 ALA B N   
5481 C CA  . ALA B 196 ? 0.3375 0.4086 0.7521 0.1350  -0.0090 0.0401  182 ALA B CA  
5482 C C   . ALA B 196 ? 0.4399 0.5247 0.8619 0.1270  0.0013  0.0345  182 ALA B C   
5483 O O   . ALA B 196 ? 0.3399 0.4478 0.7788 0.1332  0.0128  0.0344  182 ALA B O   
5484 C CB  . ALA B 196 ? 0.5329 0.5678 0.9257 0.1490  0.0001  0.0340  182 ALA B CB  
5485 N N   . LEU B 197 ? 0.3476 0.4171 0.7497 0.1117  -0.0025 0.0295  183 LEU B N   
5486 C CA  . LEU B 197 ? 0.4160 0.4926 0.8122 0.1000  0.0056  0.0237  183 LEU B CA  
5487 C C   . LEU B 197 ? 0.4118 0.4754 0.7994 0.1086  0.0235  0.0158  183 LEU B C   
5488 O O   . LEU B 197 ? 0.4449 0.4749 0.8087 0.1134  0.0274  0.0104  183 LEU B O   
5489 C CB  . LEU B 197 ? 0.3655 0.4233 0.7353 0.0836  -0.0020 0.0202  183 LEU B CB  
5490 C CG  . LEU B 197 ? 0.4503 0.5137 0.8126 0.0701  0.0027  0.0158  183 LEU B CG  
5491 C CD1 . LEU B 197 ? 0.3794 0.4753 0.7639 0.0635  -0.0015 0.0216  183 LEU B CD1 
5492 C CD2 . LEU B 197 ? 0.3164 0.3590 0.6527 0.0581  -0.0041 0.0130  183 LEU B CD2 
5493 N N   . THR B 198 ? 0.5606 0.6503 0.9657 0.1094  0.0343  0.0156  184 THR B N   
5494 C CA  . THR B 198 ? 0.6329 0.7129 1.0288 0.1159  0.0528  0.0077  184 THR B CA  
5495 C C   . THR B 198 ? 0.7721 0.8754 1.1738 0.1026  0.0591  0.0065  184 THR B C   
5496 O O   . THR B 198 ? 0.6895 0.8231 1.1108 0.0933  0.0508  0.0134  184 THR B O   
5497 C CB  . THR B 198 ? 0.5980 0.6859 1.0130 0.1393  0.0643  0.0094  184 THR B CB  
5498 O OG1 . THR B 198 ? 0.7587 0.8251 1.1545 0.1461  0.0831  -0.0002 184 THR B OG1 
5499 C CG2 . THR B 198 ? 0.5955 0.7341 1.0519 0.1435  0.0653  0.0188  184 THR B CG2 
5500 N N   . LEU B 199 ? 0.6350 0.7213 1.0162 0.1000  0.0728  -0.0020 185 LEU B N   
5501 C CA  . LEU B 199 ? 0.7021 0.8049 1.0829 0.0854  0.0784  -0.0035 185 LEU B CA  
5502 C C   . LEU B 199 ? 0.7927 0.9285 1.1982 0.0936  0.0943  -0.0020 185 LEU B C   
5503 O O   . LEU B 199 ? 0.9621 1.1311 1.3859 0.0827  0.0925  0.0034  185 LEU B O   
5504 C CB  . LEU B 199 ? 0.6981 0.7664 1.0422 0.0750  0.0833  -0.0123 185 LEU B CB  
5505 C CG  . LEU B 199 ? 0.6553 0.7348 0.9939 0.0577  0.0865  -0.0134 185 LEU B CG  
5506 C CD1 . LEU B 199 ? 0.6985 0.8022 1.0529 0.0453  0.0721  -0.0059 185 LEU B CD1 
5507 C CD2 . LEU B 199 ? 0.6280 0.6725 0.9306 0.0467  0.0864  -0.0198 185 LEU B CD2 
5508 N N   . ARG B 200 ? 0.7581 0.8852 1.1634 0.1125  0.1102  -0.0063 186 ARG B N   
5509 C CA  . ARG B 200 ? 0.8776 1.0367 1.3063 0.1234  0.1285  -0.0052 186 ARG B CA  
5510 C C   . ARG B 200 ? 0.9106 1.0765 1.3269 0.1062  0.1383  -0.0096 186 ARG B C   
5511 O O   . ARG B 200 ? 1.0652 1.2669 1.5008 0.0930  0.1348  -0.0031 186 ARG B O   
5512 C CB  . ARG B 200 ? 0.8362 1.0459 1.3106 0.1298  0.1224  0.0077  186 ARG B CB  
5513 C CG  . ARG B 200 ? 0.7489 0.9546 1.2374 0.1465  0.1120  0.0136  186 ARG B CG  
5514 C CD  . ARG B 200 ? 0.7051 0.9405 1.2151 0.1346  0.0909  0.0255  186 ARG B CD  
5515 N NE  . ARG B 200 ? 0.6652 0.9371 1.1986 0.1450  0.0885  0.0353  186 ARG B NE  
5516 C CZ  . ARG B 200 ? 0.6929 0.9740 1.2355 0.1461  0.0710  0.0444  186 ARG B CZ  
5517 N NH1 . ARG B 200 ? 0.7273 0.9840 1.2566 0.1375  0.0547  0.0450  186 ARG B NH1 
5518 N NH2 . ARG B 200 ? 0.8209 1.1368 1.3863 0.1558  0.0702  0.0530  186 ARG B NH2 
5519 N N   . HIS B 201 ? 0.9503 1.0773 1.3300 0.1041  0.1487  -0.0203 187 HIS B N   
5520 C CA  . HIS B 201 ? 1.0175 1.1401 1.3764 0.0867  0.1571  -0.0255 187 HIS B CA  
5521 C C   . HIS B 201 ? 0.9654 1.1367 1.3530 0.0827  0.1670  -0.0200 187 HIS B C   
5522 O O   . HIS B 201 ? 0.8258 1.0273 1.2419 0.1002  0.1798  -0.0167 187 HIS B O   
5523 C CB  . HIS B 201 ? 0.9975 1.0796 1.3205 0.0929  0.1739  -0.0369 187 HIS B CB  
5524 C CG  . HIS B 201 ? 0.9123 0.9956 1.2455 0.1193  0.1924  -0.0399 187 HIS B CG  
5525 N ND1 . HIS B 201 ? 1.1089 1.2399 1.4830 0.1335  0.2027  -0.0334 187 HIS B ND1 
5526 C CD2 . HIS B 201 ? 1.0591 1.1008 1.3659 0.1348  0.2025  -0.0481 187 HIS B CD2 
5527 C CE1 . HIS B 201 ? 1.1059 1.2254 1.4801 0.1589  0.2193  -0.0377 187 HIS B CE1 
5528 N NE2 . HIS B 201 ? 1.1554 1.2180 1.4869 0.1600  0.2195  -0.0471 187 HIS B NE2 
5529 N N   . ALA B 202 ? 0.8846 1.0632 1.2638 0.0593  0.1609  -0.0184 188 ALA B N   
5530 C CA  . ALA B 202 ? 0.7326 0.9560 1.1351 0.0491  0.1664  -0.0119 188 ALA B CA  
5531 C C   . ALA B 202 ? 0.7372 0.9668 1.1326 0.0534  0.1919  -0.0180 188 ALA B C   
5532 O O   . ALA B 202 ? 0.5996 0.7931 0.9664 0.0618  0.2046  -0.0283 188 ALA B O   
5533 C CB  . ALA B 202 ? 0.5976 0.8182 0.9869 0.0221  0.1504  -0.0086 188 ALA B CB  
5534 N N   . HIS B 203 ? 0.5420 0.8184 0.9628 0.0463  0.1994  -0.0110 189 HIS B N   
5535 C CA  . HIS B 203 ? 0.4972 0.7891 0.9159 0.0488  0.2246  -0.0151 189 HIS B CA  
5536 C C   . HIS B 203 ? 0.5061 0.8143 0.9169 0.0201  0.2221  -0.0115 189 HIS B C   
5537 O O   . HIS B 203 ? 0.5785 0.9133 1.0075 0.0043  0.2057  -0.0012 189 HIS B O   
5538 C CB  . HIS B 203 ? 0.5500 0.8916 1.0126 0.0714  0.2404  -0.0086 189 HIS B CB  
5539 C CG  . HIS B 203 ? 0.7913 1.1200 1.2657 0.1003  0.2405  -0.0097 189 HIS B CG  
5540 N ND1 . HIS B 203 ? 0.7917 1.1332 1.2916 0.1048  0.2201  -0.0004 189 HIS B ND1 
5541 C CD2 . HIS B 203 ? 0.8539 1.1552 1.3155 0.1255  0.2582  -0.0189 189 HIS B CD2 
5542 C CE1 . HIS B 203 ? 0.8611 1.1848 1.3646 0.1313  0.2246  -0.0032 189 HIS B CE1 
5543 N NE2 . HIS B 203 ? 0.8867 1.1845 1.3664 0.1446  0.2474  -0.0145 189 HIS B NE2 
5544 N N   . ALA B 204 ? 0.3844 0.6732 0.7644 0.0121  0.2378  -0.0199 190 ALA B N   
5545 C CA  . ALA B 204 ? 0.3871 0.6901 0.7571 -0.0150 0.2376  -0.0165 190 ALA B CA  
5546 C C   . ALA B 204 ? 0.5170 0.8846 0.9274 -0.0166 0.2477  -0.0059 190 ALA B C   
5547 O O   . ALA B 204 ? 0.4216 0.8208 0.8612 0.0061  0.2652  -0.0046 190 ALA B O   
5548 C CB  . ALA B 204 ? 0.4689 0.7373 0.7962 -0.0223 0.2537  -0.0275 190 ALA B CB  
5549 N N   . ASP B 205 ? 0.5222 0.9093 0.9337 -0.0440 0.2361  0.0024  191 ASP B N   
5550 C CA  . ASP B 205 ? 0.3752 0.8220 0.8169 -0.0526 0.2470  0.0126  191 ASP B CA  
5551 C C   . ASP B 205 ? 0.4050 0.8600 0.8387 -0.0433 0.2784  0.0050  191 ASP B C   
5552 O O   . ASP B 205 ? 0.4264 0.8373 0.8175 -0.0492 0.2860  -0.0063 191 ASP B O   
5553 C CB  . ASP B 205 ? 0.4076 0.8585 0.8365 -0.0878 0.2299  0.0204  191 ASP B CB  
5554 C CG  . ASP B 205 ? 0.3722 0.8868 0.8320 -0.1011 0.2381  0.0329  191 ASP B CG  
5555 O OD1 . ASP B 205 ? 0.3543 0.9096 0.8506 -0.1022 0.2263  0.0457  191 ASP B OD1 
5556 O OD2 . ASP B 205 ? 0.4043 0.9290 0.8511 -0.1116 0.2562  0.0307  191 ASP B OD2 
5557 N N   . SER B 206 ? 0.4533 0.6504 1.0024 -0.0212 0.1586  -0.0994 192 SER B N   
5558 C CA  . SER B 206 ? 0.2792 0.4754 0.8425 -0.0155 0.1727  -0.1090 192 SER B CA  
5559 C C   . SER B 206 ? 0.4409 0.6270 0.9789 -0.0247 0.1909  -0.1169 192 SER B C   
5560 O O   . SER B 206 ? 0.4554 0.6302 0.9837 -0.0224 0.2022  -0.1239 192 SER B O   
5561 C CB  . SER B 206 ? 0.3402 0.5562 0.9407 -0.0091 0.1681  -0.1103 192 SER B CB  
5562 O OG  . SER B 206 ? 0.4837 0.7182 1.0939 -0.0166 0.1641  -0.1089 192 SER B OG  
5563 N N   . ALA B 207 ? 0.4181 0.6077 0.9447 -0.0357 0.1938  -0.1159 193 ALA B N   
5564 C CA  . ALA B 207 ? 0.3319 0.5103 0.8323 -0.0449 0.2100  -0.1207 193 ALA B CA  
5565 C C   . ALA B 207 ? 0.3470 0.5042 0.8133 -0.0470 0.2143  -0.1178 193 ALA B C   
5566 O O   . ALA B 207 ? 0.4315 0.5782 0.8779 -0.0497 0.2272  -0.1225 193 ALA B O   
5567 C CB  . ALA B 207 ? 0.3491 0.5344 0.8468 -0.0561 0.2114  -0.1193 193 ALA B CB  
5568 N N   . CYS B 208 ? 0.3362 0.4842 0.7877 -0.0459 0.2005  -0.1087 194 CYS B N   
5569 C CA  . CYS B 208 ? 0.3906 0.5151 0.8034 -0.0465 0.1995  -0.1038 194 CYS B CA  
5570 C C   . CYS B 208 ? 0.4568 0.5732 0.8663 -0.0383 0.2013  -0.1079 194 CYS B C   
5571 O O   . CYS B 208 ? 0.4698 0.5733 0.8534 -0.0412 0.2105  -0.1102 194 CYS B O   
5572 C CB  . CYS B 208 ? 0.5709 0.6875 0.9695 -0.0463 0.1830  -0.0938 194 CYS B CB  
5573 S SG  . CYS B 208 ? 0.6769 0.7671 1.0309 -0.0472 0.1812  -0.0870 194 CYS B SG  
5574 N N   . LEU B 209 ? 0.4223 0.5464 0.8584 -0.0286 0.1925  -0.1087 195 LEU B N   
5575 C CA  . LEU B 209 ? 0.4030 0.5185 0.8399 -0.0210 0.1952  -0.1138 195 LEU B CA  
5576 C C   . LEU B 209 ? 0.4246 0.5442 0.8677 -0.0233 0.2153  -0.1270 195 LEU B C   
5577 O O   . LEU B 209 ? 0.3878 0.4949 0.8104 -0.0240 0.2232  -0.1325 195 LEU B O   
5578 C CB  . LEU B 209 ? 0.3767 0.4999 0.8457 -0.0099 0.1826  -0.1111 195 LEU B CB  
5579 C CG  . LEU B 209 ? 0.5387 0.6508 1.0123 -0.0013 0.1839  -0.1158 195 LEU B CG  
5580 C CD1 . LEU B 209 ? 0.4106 0.5012 0.8433 -0.0048 0.1840  -0.1144 195 LEU B CD1 
5581 C CD2 . LEU B 209 ? 0.4621 0.5786 0.9632 0.0090  0.1680  -0.1082 195 LEU B CD2 
5582 N N   . LYS B 210 ? 0.3473 0.4844 0.8156 -0.0257 0.2228  -0.1323 196 LYS B N   
5583 C CA  . LYS B 210 ? 0.3416 0.4789 0.8061 -0.0294 0.2379  -0.1431 196 LYS B CA  
5584 C C   . LYS B 210 ? 0.4089 0.5352 0.8343 -0.0406 0.2500  -0.1437 196 LYS B C   
5585 O O   . LYS B 210 ? 0.3718 0.4916 0.7816 -0.0432 0.2614  -0.1520 196 LYS B O   
5586 C CB  . LYS B 210 ? 0.4215 0.5767 0.9127 -0.0308 0.2393  -0.1457 196 LYS B CB  
5587 C CG  . LYS B 210 ? 0.3744 0.5318 0.8631 -0.0357 0.2555  -0.1569 196 LYS B CG  
5588 C CD  . LYS B 210 ? 0.5080 0.6836 1.0198 -0.0389 0.2576  -0.1588 196 LYS B CD  
5589 C CE  . LYS B 210 ? 0.3931 0.5712 0.9016 -0.0445 0.2746  -0.1703 196 LYS B CE  
5590 N NZ  . LYS B 210 ? 0.6228 0.8205 1.1630 -0.0443 0.2762  -0.1741 196 LYS B NZ  
5591 N N   . ALA B 211 ? 0.3769 0.5009 0.7860 -0.0478 0.2473  -0.1346 197 ALA B N   
5592 C CA  . ALA B 211 ? 0.4091 0.5216 0.7811 -0.0580 0.2572  -0.1319 197 ALA B CA  
5593 C C   . ALA B 211 ? 0.4189 0.5158 0.7631 -0.0559 0.2558  -0.1310 197 ALA B C   
5594 O O   . ALA B 211 ? 0.5154 0.6069 0.8354 -0.0622 0.2678  -0.1352 197 ALA B O   
5595 C CB  . ALA B 211 ? 0.5639 0.6741 0.9263 -0.0649 0.2527  -0.1211 197 ALA B CB  
5596 N N   . PHE B 212 ? 0.3689 0.4576 0.7124 -0.0479 0.2391  -0.1247 198 PHE B N   
5597 C CA  . PHE B 212 ? 0.4207 0.4944 0.7386 -0.0456 0.2356  -0.1244 198 PHE B CA  
5598 C C   . PHE B 212 ? 0.4972 0.5735 0.8257 -0.0428 0.2471  -0.1389 198 PHE B C   
5599 O O   . PHE B 212 ? 0.4587 0.5273 0.7608 -0.0476 0.2548  -0.1436 198 PHE B O   
5600 C CB  . PHE B 212 ? 0.4493 0.5151 0.7680 -0.0378 0.2165  -0.1156 198 PHE B CB  
5601 C CG  . PHE B 212 ? 0.5607 0.6135 0.8611 -0.0346 0.2130  -0.1174 198 PHE B CG  
5602 C CD1 . PHE B 212 ? 0.3803 0.4216 0.6434 -0.0405 0.2134  -0.1130 198 PHE B CD1 
5603 C CD2 . PHE B 212 ? 0.5045 0.5569 0.8263 -0.0260 0.2094  -0.1234 198 PHE B CD2 
5604 C CE1 . PHE B 212 ? 0.4768 0.5080 0.7236 -0.0387 0.2101  -0.1154 198 PHE B CE1 
5605 C CE2 . PHE B 212 ? 0.3537 0.3934 0.6593 -0.0243 0.2070  -0.1260 198 PHE B CE2 
5606 C CZ  . PHE B 212 ? 0.4031 0.4332 0.6709 -0.0311 0.2073  -0.1226 198 PHE B CZ  
5607 N N   . ARG B 213 ? 0.4792 0.5673 0.8472 -0.0353 0.2486  -0.1465 199 ARG B N   
5608 C CA  . ARG B 213 ? 0.4735 0.5622 0.8544 -0.0319 0.2591  -0.1610 199 ARG B CA  
5609 C C   . ARG B 213 ? 0.6037 0.6938 0.9643 -0.0424 0.2750  -0.1695 199 ARG B C   
5610 O O   . ARG B 213 ? 0.4971 0.5801 0.8396 -0.0455 0.2831  -0.1787 199 ARG B O   
5611 C CB  . ARG B 213 ? 0.4444 0.5429 0.8681 -0.0221 0.2531  -0.1635 199 ARG B CB  
5612 C CG  . ARG B 213 ? 0.5070 0.6067 0.9425 -0.0214 0.2642  -0.1776 199 ARG B CG  
5613 C CD  . ARG B 213 ? 0.6722 0.7814 1.1518 -0.0109 0.2579  -0.1785 199 ARG B CD  
5614 N NE  . ARG B 213 ? 0.8333 0.9352 1.3257 -0.0057 0.2628  -0.1895 199 ARG B NE  
5615 C CZ  . ARG B 213 ? 0.8889 0.9915 1.3784 -0.0108 0.2776  -0.2032 199 ARG B CZ  
5616 N NH1 . ARG B 213 ? 0.5769 0.6875 1.0509 -0.0211 0.2888  -0.2072 199 ARG B NH1 
5617 N NH2 . ARG B 213 ? 0.9033 0.9984 1.4063 -0.0060 0.2814  -0.2132 199 ARG B NH2 
5618 N N   . ASP B 214 ? 0.5687 0.6682 0.9310 -0.0488 0.2795  -0.1666 200 ASP B N   
5619 C CA  . ASP B 214 ? 0.4574 0.5594 0.8013 -0.0593 0.2944  -0.1736 200 ASP B CA  
5620 C C   . ASP B 214 ? 0.5400 0.6317 0.8396 -0.0688 0.2999  -0.1702 200 ASP B C   
5621 O O   . ASP B 214 ? 0.6169 0.7072 0.8970 -0.0753 0.3108  -0.1792 200 ASP B O   
5622 C CB  . ASP B 214 ? 0.6119 0.7252 0.9665 -0.0645 0.2971  -0.1696 200 ASP B CB  
5623 C CG  . ASP B 214 ? 0.7177 0.8445 1.1132 -0.0579 0.2966  -0.1769 200 ASP B CG  
5624 O OD1 . ASP B 214 ? 0.8008 0.9307 1.2041 -0.0578 0.3063  -0.1892 200 ASP B OD1 
5625 O OD2 . ASP B 214 ? 0.6547 0.7899 1.0748 -0.0531 0.2863  -0.1704 200 ASP B OD2 
5626 N N   . ALA B 215 ? 0.4249 0.5103 0.7080 -0.0700 0.2923  -0.1571 201 ALA B N   
5627 C CA  . ALA B 215 ? 0.5653 0.6414 0.8072 -0.0783 0.2961  -0.1520 201 ALA B CA  
5628 C C   . ALA B 215 ? 0.4849 0.5531 0.7149 -0.0748 0.2939  -0.1596 201 ALA B C   
5629 O O   . ALA B 215 ? 0.5380 0.6037 0.7379 -0.0831 0.3022  -0.1639 201 ALA B O   
5630 C CB  . ALA B 215 ? 0.4431 0.5097 0.6689 -0.0786 0.2819  -0.1335 201 ALA B CB  
5631 N N   . ALA B 216 ? 0.5198 0.5838 0.7718 -0.0634 0.2817  -0.1605 202 ALA B N   
5632 C CA  . ALA B 216 ? 0.5349 0.5904 0.7796 -0.0602 0.2797  -0.1688 202 ALA B CA  
5633 C C   . ALA B 216 ? 0.5779 0.6391 0.8346 -0.0620 0.2959  -0.1881 202 ALA B C   
5634 O O   . ALA B 216 ? 0.5960 0.6518 0.8313 -0.0669 0.3014  -0.1973 202 ALA B O   
5635 C CB  . ALA B 216 ? 0.4130 0.4619 0.6795 -0.0480 0.2626  -0.1635 202 ALA B CB  
5636 N N   . GLU B 217 ? 0.5046 0.5748 0.7919 -0.0587 0.2988  -0.1925 203 GLU B N   
5637 C CA  . GLU B 217 ? 0.6746 0.7480 0.9713 -0.0607 0.3098  -0.2083 203 GLU B CA  
5638 C C   . GLU B 217 ? 0.6960 0.7713 0.9559 -0.0750 0.3227  -0.2134 203 GLU B C   
5639 O O   . GLU B 217 ? 0.7213 0.7938 0.9698 -0.0795 0.3306  -0.2265 203 GLU B O   
5640 C CB  . GLU B 217 ? 0.6149 0.6999 0.9503 -0.0554 0.3109  -0.2105 203 GLU B CB  
5641 C CG  . GLU B 217 ? 0.5623 0.6504 0.9156 -0.0550 0.3215  -0.2271 203 GLU B CG  
5642 C CD  . GLU B 217 ? 0.6139 0.7095 0.9482 -0.0676 0.3368  -0.2347 203 GLU B CD  
5643 O OE1 . GLU B 217 ? 0.7969 0.8990 1.1194 -0.0739 0.3383  -0.2258 203 GLU B OE1 
5644 O OE2 . GLU B 217 ? 0.7426 0.8375 1.0736 -0.0718 0.3475  -0.2495 203 GLU B OE2 
5645 N N   . ASN B 218 ? 0.7309 0.8107 0.9718 -0.0828 0.3249  -0.2027 204 ASN B N   
5646 C CA  . ASN B 218 ? 0.6378 0.7195 0.8413 -0.0969 0.3358  -0.2042 204 ASN B CA  
5647 C C   . ASN B 218 ? 0.6398 0.7132 0.8074 -0.1019 0.3341  -0.2043 204 ASN B C   
5648 O O   . ASN B 218 ? 0.7821 0.8562 0.9315 -0.1094 0.3423  -0.2162 204 ASN B O   
5649 C CB  . ASN B 218 ? 0.6344 0.7197 0.8246 -0.1036 0.3364  -0.1894 204 ASN B CB  
5650 C CG  . ASN B 218 ? 0.7812 0.8772 0.9856 -0.1082 0.3465  -0.1945 204 ASN B CG  
5651 O OD1 . ASN B 218 ? 0.9411 1.0430 1.1699 -0.1049 0.3525  -0.2088 204 ASN B OD1 
5652 N ND2 . ASN B 218 ? 1.0550 1.1533 1.2453 -0.1159 0.3488  -0.1826 204 ASN B ND2 
5653 N N   . ARG B 219 ? 0.7039 0.7703 0.8635 -0.0977 0.3231  -0.1921 205 ARG B N   
5654 C CA  . ARG B 219 ? 0.7118 0.7719 0.8349 -0.1035 0.3207  -0.1899 205 ARG B CA  
5655 C C   . ARG B 219 ? 0.6355 0.6915 0.7604 -0.1021 0.3227  -0.2071 205 ARG B C   
5656 O O   . ARG B 219 ? 0.8327 0.8890 0.9253 -0.1124 0.3273  -0.2131 205 ARG B O   
5657 C CB  . ARG B 219 ? 0.7648 0.8153 0.8831 -0.0968 0.3018  -0.1716 205 ARG B CB  
5658 C CG  . ARG B 219 ? 0.6568 0.6999 0.7376 -0.1014 0.2922  -0.1653 205 ARG B CG  
5659 C CD  . ARG B 219 ? 0.5891 0.6370 0.6310 -0.1152 0.2988  -0.1575 205 ARG B CD  
5660 N NE  . ARG B 219 ? 0.7324 0.7765 0.7392 -0.1204 0.2900  -0.1528 205 ARG B NE  
5661 C CZ  . ARG B 219 ? 0.7600 0.8063 0.7538 -0.1258 0.2953  -0.1683 205 ARG B CZ  
5662 N NH1 . ARG B 219 ? 0.8231 0.8737 0.8356 -0.1265 0.3106  -0.1905 205 ARG B NH1 
5663 N NH2 . ARG B 219 ? 0.7227 0.7672 0.6851 -0.1308 0.2852  -0.1621 205 ARG B NH2 
5664 N N   . LEU B 220 ? 0.6808 0.7330 0.8432 -0.0901 0.3186  -0.2147 206 LEU B N   
5665 C CA  . LEU B 220 ? 0.6804 0.7263 0.8479 -0.0888 0.3206  -0.2308 206 LEU B CA  
5666 C C   . LEU B 220 ? 0.7158 0.7679 0.8821 -0.0969 0.3344  -0.2465 206 LEU B C   
5667 O O   . LEU B 220 ? 0.8235 0.8720 0.9788 -0.1021 0.3390  -0.2602 206 LEU B O   
5668 C CB  . LEU B 220 ? 0.5691 0.6084 0.7784 -0.0737 0.3119  -0.2319 206 LEU B CB  
5669 C CG  . LEU B 220 ? 0.5994 0.6303 0.8032 -0.0675 0.2985  -0.2200 206 LEU B CG  
5670 C CD1 . LEU B 220 ? 0.5590 0.5864 0.8031 -0.0528 0.2868  -0.2134 206 LEU B CD1 
5671 C CD2 . LEU B 220 ? 0.6505 0.6711 0.8296 -0.0719 0.2949  -0.2263 206 LEU B CD2 
5672 N N   . ALA B 221 ? 0.7436 0.8055 0.9218 -0.0988 0.3414  -0.2455 207 ALA B N   
5673 C CA  . ALA B 221 ? 0.6902 0.7590 0.8692 -0.1065 0.3554  -0.2607 207 ALA B CA  
5674 C C   . ALA B 221 ? 0.6364 0.7079 0.7686 -0.1226 0.3627  -0.2647 207 ALA B C   
5675 O O   . ALA B 221 ? 0.8169 0.8908 0.9452 -0.1296 0.3728  -0.2812 207 ALA B O   
5676 C CB  . ALA B 221 ? 0.5950 0.6743 0.7946 -0.1058 0.3610  -0.2576 207 ALA B CB  
5677 N N   . MET B 222 ? 0.7109 0.7829 0.8076 -0.1292 0.3576  -0.2494 208 MET B N   
5678 C CA  . MET B 222 ? 0.8479 0.9237 0.8987 -0.1445 0.3621  -0.2509 208 MET B CA  
5679 C C   . MET B 222 ? 0.7844 0.8532 0.8124 -0.1461 0.3537  -0.2515 208 MET B C   
5680 O O   . MET B 222 ? 0.8865 0.9594 0.8734 -0.1586 0.3536  -0.2484 208 MET B O   
5681 C CB  . MET B 222 ? 0.7398 0.8215 0.7605 -0.1531 0.3619  -0.2323 208 MET B CB  
5682 C CG  . MET B 222 ? 0.8331 0.9089 0.8462 -0.1478 0.3493  -0.2113 208 MET B CG  
5683 S SD  . MET B 222 ? 1.0868 1.1660 1.0976 -0.1499 0.3495  -0.1898 208 MET B SD  
5684 C CE  . MET B 222 ? 0.9519 1.0307 1.0185 -0.1352 0.3484  -0.1931 208 MET B CE  
5685 N N   . SER B 223 ? 0.7703 0.8293 0.8238 -0.1342 0.3461  -0.2549 209 SER B N   
5686 C CA  . SER B 223 ? 0.9161 0.9682 0.9506 -0.1357 0.3383  -0.2570 209 SER B CA  
5687 C C   . SER B 223 ? 0.7793 0.8300 0.8117 -0.1424 0.3455  -0.2785 209 SER B C   
5688 O O   . SER B 223 ? 0.9424 0.9895 1.0100 -0.1359 0.3512  -0.2918 209 SER B O   
5689 C CB  . SER B 223 ? 0.8700 0.9114 0.9325 -0.1206 0.3271  -0.2510 209 SER B CB  
5690 O OG  . SER B 223 ? 0.8431 0.8795 0.9496 -0.1100 0.3294  -0.2619 209 SER B OG  
5691 N N   . LYS B 224 ? 0.7749 0.8294 0.7668 -0.1558 0.3449  -0.2812 210 LYS B N   
5692 C CA  . LYS B 224 ? 0.8759 0.9291 0.8640 -0.1635 0.3508  -0.3018 210 LYS B CA  
5693 C C   . LYS B 224 ? 0.9332 0.9733 0.9361 -0.1559 0.3422  -0.3072 210 LYS B C   
5694 O O   . LYS B 224 ? 0.9730 1.0050 1.0078 -0.1502 0.3466  -0.3216 210 LYS B O   
5695 C CB  . LYS B 224 ? 0.9314 0.9959 0.8702 -0.1821 0.3525  -0.3026 210 LYS B CB  
5696 C CG  . LYS B 224 ? 1.0915 1.1675 1.0047 -0.1892 0.3544  -0.2865 210 LYS B CG  
5697 C CD  . LYS B 224 ? 1.1431 1.2270 1.0066 -0.2016 0.3456  -0.2737 210 LYS B CD  
5698 C CE  . LYS B 224 ? 1.0066 1.0973 0.8504 -0.2040 0.3434  -0.2504 210 LYS B CE  
5699 N NZ  . LYS B 224 ? 0.9090 0.9913 0.7767 -0.1894 0.3367  -0.2346 210 LYS B NZ  
5700 N N   . ARG B 225 ? 0.7342 0.7718 0.7150 -0.1558 0.3300  -0.2948 211 ARG B N   
5701 C CA  . ARG B 225 ? 0.9160 0.9408 0.9087 -0.1486 0.3207  -0.2975 211 ARG B CA  
5702 C C   . ARG B 225 ? 0.7788 0.7982 0.7832 -0.1357 0.3099  -0.2792 211 ARG B C   
5703 O O   . ARG B 225 ? 0.7237 0.7497 0.7032 -0.1385 0.3019  -0.2605 211 ARG B O   
5704 C CB  . ARG B 225 ? 0.9241 0.9520 0.8782 -0.1621 0.3154  -0.3020 211 ARG B CB  
5705 C CG  . ARG B 225 ? 0.9492 0.9769 0.9033 -0.1721 0.3238  -0.3241 211 ARG B CG  
5706 C CD  . ARG B 225 ? 1.0817 1.1109 1.0044 -0.1835 0.3157  -0.3281 211 ARG B CD  
5707 N NE  . ARG B 225 ? 1.0071 1.0314 0.9219 -0.1771 0.3011  -0.3132 211 ARG B NE  
5708 C CZ  . ARG B 225 ? 0.9856 0.9943 0.9273 -0.1656 0.2946  -0.3141 211 ARG B CZ  
5709 N NH1 . ARG B 225 ? 0.9364 0.9323 0.9157 -0.1584 0.3004  -0.3272 211 ARG B NH1 
5710 N NH2 . ARG B 225 ? 0.6650 0.6710 0.5989 -0.1604 0.2777  -0.2959 211 ARG B NH2 
5711 N N   . THR B 226 ? 0.7290 0.7358 0.7724 -0.1215 0.3058  -0.2808 212 THR B N   
5712 C CA  . THR B 226 ? 0.7045 0.7052 0.7650 -0.1081 0.2892  -0.2593 212 THR B CA  
5713 C C   . THR B 226 ? 0.6417 0.6295 0.7056 -0.1036 0.2742  -0.2560 212 THR B C   
5714 O O   . THR B 226 ? 0.6973 0.6763 0.7737 -0.1042 0.2802  -0.2738 212 THR B O   
5715 C CB  . THR B 226 ? 0.7175 0.7166 0.8226 -0.0951 0.2948  -0.2599 212 THR B CB  
5716 O OG1 . THR B 226 ? 0.8216 0.8337 0.9212 -0.0990 0.3043  -0.2560 212 THR B OG1 
5717 C CG2 . THR B 226 ? 0.7014 0.6922 0.8286 -0.0813 0.2759  -0.2406 212 THR B CG2 
5718 N N   . ALA B 227 ? 0.6961 0.6826 0.7495 -0.0997 0.2553  -0.2338 213 ALA B N   
5719 C CA  . ALA B 227 ? 0.7623 0.7381 0.8186 -0.0956 0.2402  -0.2281 213 ALA B CA  
5720 C C   . ALA B 227 ? 0.6930 0.6639 0.7706 -0.0823 0.2256  -0.2079 213 ALA B C   
5721 O O   . ALA B 227 ? 0.6048 0.5822 0.6840 -0.0789 0.2240  -0.1952 213 ALA B O   
5722 C CB  . ALA B 227 ? 0.5606 0.5421 0.5769 -0.1068 0.2310  -0.2227 213 ALA B CB  
5723 N N   . LEU B 228 ? 0.5455 0.5049 0.6389 -0.0759 0.2153  -0.2055 214 LEU B N   
5724 C CA  . LEU B 228 ? 0.5437 0.4982 0.6585 -0.0641 0.2018  -0.1883 214 LEU B CA  
5725 C C   . LEU B 228 ? 0.6085 0.5603 0.7057 -0.0655 0.1852  -0.1752 214 LEU B C   
5726 O O   . LEU B 228 ? 0.6418 0.5873 0.7321 -0.0701 0.1830  -0.1827 214 LEU B O   
5727 C CB  . LEU B 228 ? 0.6147 0.5584 0.7690 -0.0543 0.2045  -0.1954 214 LEU B CB  
5728 C CG  . LEU B 228 ? 0.6419 0.5805 0.8199 -0.0428 0.1903  -0.1788 214 LEU B CG  
5729 C CD1 . LEU B 228 ? 0.5078 0.4560 0.7005 -0.0366 0.1910  -0.1699 214 LEU B CD1 
5730 C CD2 . LEU B 228 ? 0.7887 0.7139 0.9983 -0.0359 0.1911  -0.1860 214 LEU B CD2 
5731 N N   . LEU B 229 ? 0.5889 0.5454 0.6801 -0.0618 0.1744  -0.1566 215 LEU B N   
5732 C CA  . LEU B 229 ? 0.5669 0.5222 0.6457 -0.0616 0.1589  -0.1432 215 LEU B CA  
5733 C C   . LEU B 229 ? 0.5937 0.5453 0.6948 -0.0512 0.1491  -0.1296 215 LEU B C   
5734 O O   . LEU B 229 ? 0.5793 0.5365 0.6844 -0.0476 0.1488  -0.1207 215 LEU B O   
5735 C CB  . LEU B 229 ? 0.5019 0.4677 0.5491 -0.0684 0.1551  -0.1338 215 LEU B CB  
5736 C CG  . LEU B 229 ? 0.5658 0.5327 0.6013 -0.0680 0.1398  -0.1198 215 LEU B CG  
5737 C CD1 . LEU B 229 ? 0.5195 0.4825 0.5488 -0.0733 0.1361  -0.1283 215 LEU B CD1 
5738 C CD2 . LEU B 229 ? 0.6899 0.6674 0.6998 -0.0724 0.1368  -0.1083 215 LEU B CD2 
5739 N N   . ALA B 230 ? 0.5786 0.5213 0.6931 -0.0474 0.1412  -0.1280 216 ALA B N   
5740 C CA  . ALA B 230 ? 0.5272 0.4671 0.6614 -0.0388 0.1315  -0.1154 216 ALA B CA  
5741 C C   . ALA B 230 ? 0.5485 0.4876 0.6701 -0.0403 0.1183  -0.1045 216 ALA B C   
5742 O O   . ALA B 230 ? 0.6083 0.5455 0.7148 -0.0465 0.1166  -0.1090 216 ALA B O   
5743 C CB  . ALA B 230 ? 0.4728 0.4033 0.6380 -0.0324 0.1337  -0.1211 216 ALA B CB  
5744 N N   . ASP B 231 ? 0.5385 0.4800 0.6664 -0.0352 0.1093  -0.0909 217 ASP B N   
5745 C CA  . ASP B 231 ? 0.4998 0.4417 0.6171 -0.0366 0.0979  -0.0812 217 ASP B CA  
5746 C C   . ASP B 231 ? 0.5001 0.4408 0.6345 -0.0305 0.0897  -0.0706 217 ASP B C   
5747 O O   . ASP B 231 ? 0.5135 0.4518 0.6693 -0.0253 0.0916  -0.0713 217 ASP B O   
5748 C CB  . ASP B 231 ? 0.4755 0.4265 0.5690 -0.0406 0.0959  -0.0753 217 ASP B CB  
5749 C CG  . ASP B 231 ? 0.6722 0.6247 0.7534 -0.0439 0.0865  -0.0698 217 ASP B CG  
5750 O OD1 . ASP B 231 ? 0.6673 0.6193 0.7375 -0.0500 0.0872  -0.0771 217 ASP B OD1 
5751 O OD2 . ASP B 231 ? 0.6056 0.5608 0.6887 -0.0410 0.0788  -0.0592 217 ASP B OD2 
5752 N N   . PHE B 232 ? 0.3995 0.3434 0.5247 -0.0314 0.0805  -0.0608 218 PHE B N   
5753 C CA  . PHE B 232 ? 0.4617 0.4033 0.5987 -0.0286 0.0718  -0.0523 218 PHE B CA  
5754 C C   . PHE B 232 ? 0.3646 0.3095 0.5187 -0.0231 0.0707  -0.0471 218 PHE B C   
5755 O O   . PHE B 232 ? 0.4148 0.3573 0.5823 -0.0207 0.0644  -0.0414 218 PHE B O   
5756 C CB  . PHE B 232 ? 0.4061 0.3528 0.5288 -0.0314 0.0640  -0.0443 218 PHE B CB  
5757 C CG  . PHE B 232 ? 0.3884 0.3435 0.5044 -0.0301 0.0635  -0.0381 218 PHE B CG  
5758 C CD1 . PHE B 232 ? 0.3856 0.3449 0.4883 -0.0316 0.0686  -0.0400 218 PHE B CD1 
5759 C CD2 . PHE B 232 ? 0.2979 0.2566 0.4206 -0.0280 0.0582  -0.0304 218 PHE B CD2 
5760 C CE1 . PHE B 232 ? 0.3898 0.3546 0.4883 -0.0303 0.0687  -0.0338 218 PHE B CE1 
5761 C CE2 . PHE B 232 ? 0.3199 0.2848 0.4379 -0.0272 0.0588  -0.0262 218 PHE B CE2 
5762 C CZ  . PHE B 232 ? 0.3002 0.2671 0.4072 -0.0279 0.0642  -0.0277 218 PHE B CZ  
5763 N N   . LEU B 233 ? 0.4140 0.3650 0.5680 -0.0219 0.0763  -0.0483 219 LEU B N   
5764 C CA  . LEU B 233 ? 0.3514 0.3076 0.5220 -0.0178 0.0747  -0.0437 219 LEU B CA  
5765 C C   . LEU B 233 ? 0.3786 0.3314 0.5733 -0.0133 0.0766  -0.0473 219 LEU B C   
5766 O O   . LEU B 233 ? 0.3862 0.3430 0.5973 -0.0099 0.0707  -0.0408 219 LEU B O   
5767 C CB  . LEU B 233 ? 0.3322 0.2952 0.4978 -0.0185 0.0809  -0.0445 219 LEU B CB  
5768 C CG  . LEU B 233 ? 0.4498 0.4162 0.5988 -0.0211 0.0770  -0.0376 219 LEU B CG  
5769 C CD1 . LEU B 233 ? 0.4048 0.3746 0.5458 -0.0226 0.0844  -0.0382 219 LEU B CD1 
5770 C CD2 . LEU B 233 ? 0.4176 0.3880 0.5741 -0.0201 0.0687  -0.0301 219 LEU B CD2 
5771 N N   . VAL B 234 ? 0.4157 0.3619 0.6141 -0.0132 0.0844  -0.0574 220 VAL B N   
5772 C CA  . VAL B 234 ? 0.4017 0.3431 0.6265 -0.0079 0.0861  -0.0606 220 VAL B CA  
5773 C C   . VAL B 234 ? 0.3172 0.2513 0.5496 -0.0066 0.0760  -0.0525 220 VAL B C   
5774 O O   . VAL B 234 ? 0.4196 0.3534 0.6751 -0.0012 0.0716  -0.0470 220 VAL B O   
5775 C CB  . VAL B 234 ? 0.3818 0.3173 0.6100 -0.0086 0.0986  -0.0755 220 VAL B CB  
5776 C CG1 . VAL B 234 ? 0.4849 0.4250 0.6884 -0.0148 0.1066  -0.0823 220 VAL B CG1 
5777 C CG2 . VAL B 234 ? 0.4420 0.3640 0.6742 -0.0094 0.0981  -0.0801 220 VAL B CG2 
5778 N N   . LEU B 235 ? 0.3914 0.3206 0.6050 -0.0117 0.0717  -0.0506 221 LEU B N   
5779 C CA  . LEU B 235 ? 0.3361 0.2587 0.5546 -0.0119 0.0624  -0.0419 221 LEU B CA  
5780 C C   . LEU B 235 ? 0.3764 0.3080 0.5994 -0.0102 0.0525  -0.0286 221 LEU B C   
5781 O O   . LEU B 235 ? 0.3704 0.2996 0.6097 -0.0072 0.0458  -0.0203 221 LEU B O   
5782 C CB  . LEU B 235 ? 0.3580 0.2764 0.5547 -0.0188 0.0603  -0.0430 221 LEU B CB  
5783 C CG  . LEU B 235 ? 0.4868 0.3952 0.6787 -0.0227 0.0675  -0.0553 221 LEU B CG  
5784 C CD1 . LEU B 235 ? 0.4462 0.3567 0.6146 -0.0302 0.0642  -0.0553 221 LEU B CD1 
5785 C CD2 . LEU B 235 ? 0.4302 0.3242 0.6433 -0.0203 0.0679  -0.0569 221 LEU B CD2 
5786 N N   . ARG B 236 ? 0.3491 0.2913 0.5576 -0.0125 0.0515  -0.0262 222 ARG B N   
5787 C CA  . ARG B 236 ? 0.4920 0.4436 0.7016 -0.0129 0.0429  -0.0157 222 ARG B CA  
5788 C C   . ARG B 236 ? 0.4120 0.3704 0.6443 -0.0078 0.0413  -0.0126 222 ARG B C   
5789 O O   . ARG B 236 ? 0.4089 0.3732 0.6487 -0.0076 0.0322  -0.0027 222 ARG B O   
5790 C CB  . ARG B 236 ? 0.4261 0.3860 0.6173 -0.0165 0.0441  -0.0160 222 ARG B CB  
5791 C CG  . ARG B 236 ? 0.3536 0.3095 0.5247 -0.0206 0.0460  -0.0190 222 ARG B CG  
5792 C CD  . ARG B 236 ? 0.2905 0.2418 0.4578 -0.0237 0.0391  -0.0138 222 ARG B CD  
5793 N NE  . ARG B 236 ? 0.3892 0.3424 0.5380 -0.0281 0.0390  -0.0147 222 ARG B NE  
5794 C CZ  . ARG B 236 ? 0.4187 0.3661 0.5601 -0.0313 0.0397  -0.0183 222 ARG B CZ  
5795 N NH1 . ARG B 236 ? 0.3775 0.3147 0.5276 -0.0311 0.0411  -0.0221 222 ARG B NH1 
5796 N NH2 . ARG B 236 ? 0.4578 0.4102 0.5841 -0.0348 0.0390  -0.0184 222 ARG B NH2 
5797 N N   . HIS B 237 ? 0.3377 0.2975 0.5810 -0.0043 0.0500  -0.0209 223 HIS B N   
5798 C CA  . HIS B 237 ? 0.3365 0.3054 0.6034 0.0005  0.0493  -0.0191 223 HIS B CA  
5799 C C   . HIS B 237 ? 0.4764 0.4387 0.7698 0.0070  0.0495  -0.0193 223 HIS B C   
5800 O O   . HIS B 237 ? 0.4785 0.4480 0.7952 0.0121  0.0520  -0.0209 223 HIS B O   
5801 C CB  . HIS B 237 ? 0.3679 0.3439 0.6335 0.0000  0.0592  -0.0276 223 HIS B CB  
5802 C CG  . HIS B 237 ? 0.4461 0.4287 0.6917 -0.0053 0.0583  -0.0255 223 HIS B CG  
5803 N ND1 . HIS B 237 ? 0.3862 0.3810 0.6374 -0.0066 0.0540  -0.0210 223 HIS B ND1 
5804 C CD2 . HIS B 237 ? 0.4576 0.4361 0.6790 -0.0097 0.0609  -0.0273 223 HIS B CD2 
5805 C CE1 . HIS B 237 ? 0.3923 0.3885 0.6242 -0.0115 0.0552  -0.0210 223 HIS B CE1 
5806 N NE2 . HIS B 237 ? 0.4420 0.4286 0.6566 -0.0128 0.0591  -0.0240 223 HIS B NE2 
5807 N N   . GLY B 238 ? 0.3852 0.3340 0.6774 0.0069  0.0474  -0.0178 224 GLY B N   
5808 C CA  . GLY B 238 ? 0.4329 0.3732 0.7522 0.0133  0.0466  -0.0160 224 GLY B CA  
5809 C C   . GLY B 238 ? 0.5636 0.4997 0.9010 0.0182  0.0594  -0.0297 224 GLY B C   
5810 O O   . GLY B 238 ? 0.4939 0.4290 0.8620 0.0258  0.0594  -0.0281 224 GLY B O   
5811 N N   . LEU B 239 ? 0.3594 0.2938 0.6791 0.0140  0.0705  -0.0430 225 LEU B N   
5812 C CA  . LEU B 239 ? 0.4194 0.3521 0.7524 0.0168  0.0845  -0.0578 225 LEU B CA  
5813 C C   . LEU B 239 ? 0.4634 0.3799 0.7905 0.0142  0.0928  -0.0698 225 LEU B C   
5814 O O   . LEU B 239 ? 0.4947 0.4100 0.8230 0.0133  0.1061  -0.0849 225 LEU B O   
5815 C CB  . LEU B 239 ? 0.3609 0.3056 0.6789 0.0130  0.0921  -0.0643 225 LEU B CB  
5816 C CG  . LEU B 239 ? 0.5768 0.5376 0.9081 0.0158  0.0868  -0.0561 225 LEU B CG  
5817 C CD1 . LEU B 239 ? 0.5156 0.4860 0.8268 0.0102  0.0920  -0.0592 225 LEU B CD1 
5818 C CD2 . LEU B 239 ? 0.4161 0.3818 0.7845 0.0239  0.0911  -0.0595 225 LEU B CD2 
5819 N N   . LYS B 240 ? 0.4782 0.3828 0.7987 0.0118  0.0857  -0.0641 226 LYS B N   
5820 C CA  . LYS B 240 ? 0.4583 0.3476 0.7729 0.0078  0.0932  -0.0761 226 LYS B CA  
5821 C C   . LYS B 240 ? 0.5262 0.4061 0.8719 0.0142  0.1036  -0.0873 226 LYS B C   
5822 O O   . LYS B 240 ? 0.4611 0.3357 0.8022 0.0106  0.1166  -0.1048 226 LYS B O   
5823 C CB  . LYS B 240 ? 0.4940 0.3727 0.8003 0.0043  0.0831  -0.0664 226 LYS B CB  
5824 C CG  . LYS B 240 ? 0.5725 0.4375 0.8659 -0.0028 0.0894  -0.0786 226 LYS B CG  
5825 C CD  . LYS B 240 ? 0.5733 0.4284 0.8614 -0.0067 0.0795  -0.0681 226 LYS B CD  
5826 C CE  . LYS B 240 ? 0.6207 0.4562 0.9181 -0.0094 0.0862  -0.0788 226 LYS B CE  
5827 N NZ  . LYS B 240 ? 0.6376 0.4643 0.9237 -0.0163 0.0782  -0.0710 226 LYS B NZ  
5828 N N   . HIS B 241 ? 0.5529 0.4318 0.9311 0.0234  0.0982  -0.0777 227 HIS B N   
5829 C CA  . HIS B 241 ? 0.5312 0.4015 0.9443 0.0311  0.1083  -0.0877 227 HIS B CA  
5830 C C   . HIS B 241 ? 0.5075 0.3894 0.9259 0.0321  0.1224  -0.1031 227 HIS B C   
5831 O O   . HIS B 241 ? 0.5518 0.4255 0.9815 0.0324  0.1370  -0.1208 227 HIS B O   
5832 C CB  . HIS B 241 ? 0.5902 0.4605 1.0385 0.0416  0.0978  -0.0713 227 HIS B CB  
5833 C CG  . HIS B 241 ? 0.8689 0.7268 1.3572 0.0506  0.1067  -0.0792 227 HIS B CG  
5834 N ND1 . HIS B 241 ? 0.8858 0.7520 1.3993 0.0570  0.1186  -0.0914 227 HIS B ND1 
5835 C CD2 . HIS B 241 ? 0.9256 0.7627 1.4347 0.0544  0.1061  -0.0769 227 HIS B CD2 
5836 C CE1 . HIS B 241 ? 0.8328 0.6893 1.3743 0.0624  0.1232  -0.0948 227 HIS B CE1 
5837 N NE2 . HIS B 241 ? 0.7989 0.6379 1.3375 0.0609  0.1155  -0.0858 227 HIS B NE2 
5838 N N   . ALA B 242 ? 0.5093 0.4099 0.9195 0.0317  0.1192  -0.0973 228 ALA B N   
5839 C CA  . ALA B 242 ? 0.4861 0.3987 0.9016 0.0320  0.1326  -0.1104 228 ALA B CA  
5840 C C   . ALA B 242 ? 0.4720 0.3805 0.8588 0.0223  0.1461  -0.1280 228 ALA B C   
5841 O O   . ALA B 242 ? 0.4862 0.3957 0.8835 0.0224  0.1616  -0.1447 228 ALA B O   
5842 C CB  . ALA B 242 ? 0.4355 0.3676 0.8446 0.0316  0.1260  -0.0999 228 ALA B CB  
5843 N N   . LEU B 243 ? 0.4850 0.3907 0.8358 0.0136  0.1404  -0.1244 229 LEU B N   
5844 C CA  . LEU B 243 ? 0.4048 0.3085 0.7269 0.0037  0.1511  -0.1394 229 LEU B CA  
5845 C C   . LEU B 243 ? 0.4666 0.3540 0.7980 0.0022  0.1604  -0.1549 229 LEU B C   
5846 O O   . LEU B 243 ? 0.5187 0.4062 0.8413 -0.0037 0.1749  -0.1731 229 LEU B O   
5847 C CB  . LEU B 243 ? 0.5163 0.4223 0.8012 -0.0043 0.1412  -0.1303 229 LEU B CB  
5848 C CG  . LEU B 243 ? 0.5283 0.4495 0.7910 -0.0080 0.1404  -0.1247 229 LEU B CG  
5849 C CD1 . LEU B 243 ? 0.5049 0.4306 0.7474 -0.0158 0.1542  -0.1393 229 LEU B CD1 
5850 C CD2 . LEU B 243 ? 0.3695 0.3016 0.6545 -0.0008 0.1383  -0.1168 229 LEU B CD2 
5851 N N   . GLN B 244 ? 0.4834 0.3566 0.8317 0.0065  0.1527  -0.1482 230 GLN B N   
5852 C CA  . GLN B 244 ? 0.5813 0.4365 0.9426 0.0054  0.1619  -0.1630 230 GLN B CA  
5853 C C   . GLN B 244 ? 0.5939 0.4478 0.9903 0.0127  0.1767  -0.1772 230 GLN B C   
5854 O O   . GLN B 244 ? 0.4882 0.3390 0.8806 0.0069  0.1907  -0.1963 230 GLN B O   
5855 C CB  . GLN B 244 ? 0.5076 0.3471 0.8815 0.0087  0.1499  -0.1501 230 GLN B CB  
5856 C CG  . GLN B 244 ? 0.7322 0.5680 1.0720 -0.0016 0.1411  -0.1449 230 GLN B CG  
5857 C CD  . GLN B 244 ? 0.8399 0.6633 1.1909 0.0012  0.1280  -0.1286 230 GLN B CD  
5858 O OE1 . GLN B 244 ? 0.6900 0.5071 1.0735 0.0112  0.1244  -0.1195 230 GLN B OE1 
5859 N NE2 . GLN B 244 ? 0.6059 0.4266 0.9303 -0.0077 0.1207  -0.1242 230 GLN B NE2 
5860 N N   . LYS B 245 ? 0.5848 0.4456 1.0133 0.0243  0.1722  -0.1662 231 LYS B N   
5861 C CA  . LYS B 245 ? 0.5293 0.3976 0.9867 0.0296  0.1821  -0.1741 231 LYS B CA  
5862 C C   . LYS B 245 ? 0.6255 0.5082 1.0673 0.0230  0.1968  -0.1901 231 LYS B C   
5863 O O   . LYS B 245 ? 0.5721 0.4570 1.0240 0.0209  0.2095  -0.2043 231 LYS B O   
5864 C CB  . LYS B 245 ? 0.5720 0.4492 1.0640 0.0420  0.1715  -0.1567 231 LYS B CB  
5865 C CG  . LYS B 245 ? 0.7000 0.5892 1.2219 0.0473  0.1806  -0.1633 231 LYS B CG  
5866 C CD  . LYS B 245 ? 0.6728 0.5632 1.2342 0.0593  0.1693  -0.1469 231 LYS B CD  
5867 C CE  . LYS B 245 ? 0.7630 0.6521 1.3550 0.0631  0.1795  -0.1569 231 LYS B CE  
5868 N NZ  . LYS B 245 ? 0.8912 0.7996 1.4953 0.0640  0.1891  -0.1654 231 LYS B NZ  
5869 N N   . TRP B 246 ? 0.5744 0.4663 0.9906 0.0189  0.1958  -0.1877 232 TRP B N   
5870 C CA  . TRP B 246 ? 0.5732 0.4791 0.9710 0.0115  0.2094  -0.2005 232 TRP B CA  
5871 C C   . TRP B 246 ? 0.6107 0.5110 0.9864 0.0001  0.2222  -0.2199 232 TRP B C   
5872 O O   . TRP B 246 ? 0.6673 0.5756 1.0466 -0.0037 0.2354  -0.2330 232 TRP B O   
5873 C CB  . TRP B 246 ? 0.5475 0.4657 0.9106 0.0055  0.1994  -0.1867 232 TRP B CB  
5874 C CG  . TRP B 246 ? 0.5192 0.4524 0.8629 -0.0018 0.2111  -0.1946 232 TRP B CG  
5875 C CD1 . TRP B 246 ? 0.4778 0.4152 0.8259 -0.0056 0.2304  -0.2144 232 TRP B CD1 
5876 C CD2 . TRP B 246 ? 0.4708 0.4161 0.7875 -0.0068 0.2046  -0.1824 232 TRP B CD2 
5877 N NE1 . TRP B 246 ? 0.5011 0.4529 0.8252 -0.0131 0.2357  -0.2140 232 TRP B NE1 
5878 C CE2 . TRP B 246 ? 0.4817 0.4377 0.7872 -0.0136 0.2200  -0.1942 232 TRP B CE2 
5879 C CE3 . TRP B 246 ? 0.5013 0.4490 0.8029 -0.0065 0.1880  -0.1631 232 TRP B CE3 
5880 C CZ2 . TRP B 246 ? 0.6030 0.5704 0.8834 -0.0196 0.2188  -0.1858 232 TRP B CZ2 
5881 C CZ3 . TRP B 246 ? 0.4091 0.3680 0.6874 -0.0120 0.1874  -0.1564 232 TRP B CZ3 
5882 C CH2 . TRP B 246 ? 0.5544 0.5222 0.8225 -0.0183 0.2023  -0.1670 232 TRP B CH2 
5883 N N   . VAL B 247 ? 0.5763 0.4635 0.9285 -0.0065 0.2182  -0.2221 233 VAL B N   
5884 C CA  . VAL B 247 ? 0.7161 0.6004 1.0439 -0.0190 0.2293  -0.2406 233 VAL B CA  
5885 C C   . VAL B 247 ? 0.6951 0.5705 1.0477 -0.0180 0.2358  -0.2507 233 VAL B C   
5886 O O   . VAL B 247 ? 0.8439 0.7209 1.1838 -0.0278 0.2482  -0.2684 233 VAL B O   
5887 C CB  . VAL B 247 ? 0.7702 0.6482 1.0622 -0.0281 0.2202  -0.2371 233 VAL B CB  
5888 C CG1 . VAL B 247 ? 0.5934 0.4551 0.9002 -0.0228 0.2070  -0.2257 233 VAL B CG1 
5889 C CG2 . VAL B 247 ? 0.9533 0.8307 1.2169 -0.0426 0.2324  -0.2582 233 VAL B CG2 
5890 N N   . LYS B 248 ? 0.6648 0.5313 1.0525 -0.0066 0.2280  -0.2399 234 LYS B N   
5891 C CA  . LYS B 248 ? 0.7521 0.6115 1.1678 -0.0042 0.2357  -0.2492 234 LYS B CA  
5892 C C   . LYS B 248 ? 0.6803 0.5534 1.1153 -0.0020 0.2481  -0.2582 234 LYS B C   
5893 O O   . LYS B 248 ? 0.6879 0.5614 1.1237 -0.0086 0.2621  -0.2762 234 LYS B O   
5894 C CB  . LYS B 248 ? 0.6221 0.4687 1.0703 0.0074  0.2237  -0.2334 234 LYS B CB  
5895 C CG  . LYS B 248 ? 0.9522 0.8002 1.4422 0.0162  0.2301  -0.2361 234 LYS B CG  
5896 C CD  . LYS B 248 ? 0.9386 0.7733 1.4618 0.0270  0.2196  -0.2212 234 LYS B CD  
5897 C CE  . LYS B 248 ? 0.9255 0.7661 1.4904 0.0364  0.2256  -0.2228 234 LYS B CE  
5898 N NZ  . LYS B 248 ? 0.8891 0.7134 1.4790 0.0389  0.2300  -0.2277 234 LYS B NZ  
5899 N N   . ASP B 249 ? 0.6832 0.5689 1.1332 0.0063  0.2433  -0.2464 235 ASP B N   
5900 C CA  . ASP B 249 ? 0.6227 0.5221 1.0930 0.0084  0.2541  -0.2538 235 ASP B CA  
5901 C C   . ASP B 249 ? 0.6844 0.5955 1.1230 -0.0043 0.2677  -0.2689 235 ASP B C   
5902 O O   . ASP B 249 ? 0.8011 0.7202 1.2511 -0.0069 0.2808  -0.2816 235 ASP B O   
5903 C CB  . ASP B 249 ? 0.7635 0.6744 1.2579 0.0198  0.2442  -0.2366 235 ASP B CB  
5904 C CG  . ASP B 249 ? 0.7283 0.6298 1.2530 0.0320  0.2293  -0.2192 235 ASP B CG  
5905 O OD1 . ASP B 249 ? 0.8439 0.7296 1.3779 0.0328  0.2290  -0.2217 235 ASP B OD1 
5906 O OD2 . ASP B 249 ? 0.7819 0.6923 1.3210 0.0402  0.2179  -0.2028 235 ASP B OD2 
5907 N N   . VAL B 250 ? 0.6751 0.5875 1.0743 -0.0127 0.2648  -0.2676 236 VAL B N   
5908 C CA  . VAL B 250 ? 0.7247 0.6485 1.0893 -0.0256 0.2762  -0.2792 236 VAL B CA  
5909 C C   . VAL B 250 ? 0.7512 0.6673 1.0768 -0.0371 0.2751  -0.2853 236 VAL B C   
5910 O O   . VAL B 250 ? 0.7395 0.6568 1.0392 -0.0392 0.2669  -0.2760 236 VAL B O   
5911 C CB  . VAL B 250 ? 0.6553 0.5939 1.0102 -0.0242 0.2735  -0.2683 236 VAL B CB  
5912 C CG1 . VAL B 250 ? 0.6776 0.6288 1.0023 -0.0373 0.2870  -0.2800 236 VAL B CG1 
5913 C CG2 . VAL B 250 ? 0.8172 0.7631 1.2126 -0.0117 0.2700  -0.2587 236 VAL B CG2 
5914 N N   . PRO B 251 ? 0.8627 0.7714 1.1840 -0.0449 0.2827  -0.3008 237 PRO B N   
5915 C CA  . PRO B 251 ? 0.7339 0.6369 1.0185 -0.0568 0.2807  -0.3068 237 PRO B CA  
5916 C C   . PRO B 251 ? 0.8003 0.7177 1.0419 -0.0692 0.2851  -0.3102 237 PRO B C   
5917 O O   . PRO B 251 ? 0.8505 0.7802 1.0850 -0.0759 0.2972  -0.3197 237 PRO B O   
5918 C CB  . PRO B 251 ? 0.6619 0.5575 0.9556 -0.0631 0.2908  -0.3247 237 PRO B CB  
5919 C CG  . PRO B 251 ? 0.7687 0.6597 1.1107 -0.0500 0.2933  -0.3226 237 PRO B CG  
5920 C CD  . PRO B 251 ? 0.6967 0.6015 1.0492 -0.0428 0.2929  -0.3130 237 PRO B CD  
5921 N N   . MET B 252 ? 0.8711 0.7871 1.0840 -0.0725 0.2750  -0.3016 238 MET B N   
5922 C CA  . MET B 252 ? 0.8097 0.7388 0.9787 -0.0847 0.2774  -0.3027 238 MET B CA  
5923 C C   . MET B 252 ? 0.7396 0.6628 0.8811 -0.0899 0.2654  -0.2972 238 MET B C   
5924 O O   . MET B 252 ? 0.7612 0.6718 0.9193 -0.0823 0.2529  -0.2874 238 MET B O   
5925 C CB  . MET B 252 ? 0.6903 0.6318 0.8582 -0.0795 0.2777  -0.2903 238 MET B CB  
5926 C CG  . MET B 252 ? 0.7563 0.6938 0.9391 -0.0669 0.2604  -0.2672 238 MET B CG  
5927 S SD  . MET B 252 ? 0.7991 0.7502 0.9985 -0.0585 0.2612  -0.2536 238 MET B SD  
5928 C CE  . MET B 252 ? 0.7523 0.6930 0.9971 -0.0409 0.2482  -0.2402 238 MET B CE  
5929 N N   . ALA B 253 ? 0.7818 0.7180 0.8810 -0.1035 0.2643  -0.2971 239 ALA B N   
5930 C CA  . ALA B 253 ? 0.7037 0.6413 0.7759 -0.1086 0.2468  -0.2833 239 ALA B CA  
5931 C C   . ALA B 253 ? 0.6348 0.5720 0.7166 -0.0966 0.2292  -0.2563 239 ALA B C   
5932 O O   . ALA B 253 ? 0.6361 0.5818 0.7196 -0.0915 0.2289  -0.2446 239 ALA B O   
5933 C CB  . ALA B 253 ? 0.6058 0.5607 0.6327 -0.1241 0.2478  -0.2844 239 ALA B CB  
5934 N N   . HIS B 254 ? 0.6548 0.5821 0.7427 -0.0929 0.2154  -0.2472 240 HIS B N   
5935 C CA  . HIS B 254 ? 0.5360 0.4621 0.6344 -0.0820 0.1995  -0.2236 240 HIS B CA  
5936 C C   . HIS B 254 ? 0.7233 0.6480 0.8047 -0.0859 0.1841  -0.2136 240 HIS B C   
5937 O O   . HIS B 254 ? 0.6243 0.5430 0.6994 -0.0937 0.1852  -0.2254 240 HIS B O   
5938 C CB  . HIS B 254 ? 0.6043 0.5180 0.7448 -0.0683 0.1998  -0.2214 240 HIS B CB  
5939 C CG  . HIS B 254 ? 0.6924 0.5890 0.8526 -0.0677 0.2025  -0.2334 240 HIS B CG  
5940 N ND1 . HIS B 254 ? 0.6324 0.5229 0.7977 -0.0738 0.2187  -0.2575 240 HIS B ND1 
5941 C CD2 . HIS B 254 ? 0.5735 0.4568 0.7501 -0.0622 0.1917  -0.2247 240 HIS B CD2 
5942 C CE1 . HIS B 254 ? 0.6979 0.5708 0.8833 -0.0717 0.2177  -0.2631 240 HIS B CE1 
5943 N NE2 . HIS B 254 ? 0.6819 0.5502 0.8740 -0.0647 0.2012  -0.2427 240 HIS B NE2 
5944 N N   . ALA B 255 ? 0.5463 0.4768 0.6221 -0.0807 0.1705  -0.1924 241 ALA B N   
5945 C CA  . ALA B 255 ? 0.6175 0.5489 0.6799 -0.0832 0.1557  -0.1810 241 ALA B CA  
5946 C C   . ALA B 255 ? 0.6292 0.5609 0.7031 -0.0728 0.1436  -0.1602 241 ALA B C   
5947 O O   . ALA B 255 ? 0.5063 0.4388 0.5957 -0.0648 0.1462  -0.1547 241 ALA B O   
5948 C CB  . ALA B 255 ? 0.4897 0.4360 0.5158 -0.0946 0.1527  -0.1800 241 ALA B CB  
5949 N N   . THR B 256 ? 0.4725 0.4045 0.5392 -0.0736 0.1307  -0.1496 242 THR B N   
5950 C CA  . THR B 256 ? 0.4583 0.3941 0.5280 -0.0666 0.1191  -0.1304 242 THR B CA  
5951 C C   . THR B 256 ? 0.4475 0.3952 0.4910 -0.0725 0.1105  -0.1220 242 THR B C   
5952 O O   . THR B 256 ? 0.5156 0.4694 0.5395 -0.0821 0.1122  -0.1301 242 THR B O   
5953 C CB  . THR B 256 ? 0.4513 0.3760 0.5426 -0.0605 0.1115  -0.1241 242 THR B CB  
5954 O OG1 . THR B 256 ? 0.5122 0.4361 0.5931 -0.0668 0.1039  -0.1234 242 THR B OG1 
5955 C CG2 . THR B 256 ? 0.5309 0.4422 0.6482 -0.0564 0.1197  -0.1346 242 THR B CG2 
5956 N N   . MET B 257 ? 0.5098 0.4622 0.5539 -0.0670 0.1012  -0.1059 243 MET B N   
5957 C CA  . MET B 257 ? 0.5300 0.4923 0.5571 -0.0704 0.0913  -0.0963 243 MET B CA  
5958 C C   . MET B 257 ? 0.5314 0.4883 0.5694 -0.0690 0.0824  -0.0920 243 MET B C   
5959 O O   . MET B 257 ? 0.5552 0.5001 0.6111 -0.0665 0.0842  -0.0966 243 MET B O   
5960 C CB  . MET B 257 ? 0.3903 0.3609 0.4113 -0.0658 0.0884  -0.0825 243 MET B CB  
5961 C CG  . MET B 257 ? 0.5193 0.4935 0.5320 -0.0674 0.0983  -0.0860 243 MET B CG  
5962 S SD  . MET B 257 ? 0.5757 0.5594 0.5762 -0.0648 0.0952  -0.0695 243 MET B SD  
5963 C CE  . MET B 257 ? 0.4604 0.4365 0.4847 -0.0556 0.0993  -0.0659 243 MET B CE  
5964 N N   . LEU B 258 ? 0.6045 0.5706 0.6326 -0.0706 0.0730  -0.0826 244 LEU B N   
5965 C CA  . LEU B 258 ? 0.5287 0.4917 0.5646 -0.0715 0.0655  -0.0796 244 LEU B CA  
5966 C C   . LEU B 258 ? 0.4954 0.4495 0.5511 -0.0636 0.0635  -0.0723 244 LEU B C   
5967 O O   . LEU B 258 ? 0.4531 0.3974 0.5209 -0.0641 0.0621  -0.0742 244 LEU B O   
5968 C CB  . LEU B 258 ? 0.4270 0.4042 0.4509 -0.0740 0.0564  -0.0706 244 LEU B CB  
5969 C CG  . LEU B 258 ? 0.5381 0.5153 0.5691 -0.0756 0.0488  -0.0665 244 LEU B CG  
5970 C CD1 . LEU B 258 ? 0.3752 0.3441 0.4083 -0.0835 0.0508  -0.0785 244 LEU B CD1 
5971 C CD2 . LEU B 258 ? 0.3566 0.3506 0.3777 -0.0772 0.0409  -0.0581 244 LEU B CD2 
5972 N N   . MET B 259 ? 0.4533 0.4108 0.5124 -0.0568 0.0634  -0.0637 245 MET B N   
5973 C CA  . MET B 259 ? 0.4862 0.4387 0.5618 -0.0505 0.0603  -0.0562 245 MET B CA  
5974 C C   . MET B 259 ? 0.5298 0.4702 0.6230 -0.0478 0.0650  -0.0621 245 MET B C   
5975 O O   . MET B 259 ? 0.5961 0.5302 0.7025 -0.0456 0.0607  -0.0573 245 MET B O   
5976 C CB  . MET B 259 ? 0.5804 0.5391 0.6559 -0.0452 0.0606  -0.0482 245 MET B CB  
5977 C CG  . MET B 259 ? 0.4262 0.3928 0.4974 -0.0444 0.0536  -0.0383 245 MET B CG  
5978 S SD  . MET B 259 ? 0.5704 0.5430 0.6396 -0.0395 0.0554  -0.0306 245 MET B SD  
5979 C CE  . MET B 259 ? 0.4432 0.4139 0.5275 -0.0357 0.0514  -0.0249 245 MET B CE  
5980 N N   . GLY B 260 ? 0.4546 0.3921 0.5488 -0.0479 0.0739  -0.0718 246 GLY B N   
5981 C CA  . GLY B 260 ? 0.4800 0.4071 0.5942 -0.0441 0.0794  -0.0778 246 GLY B CA  
5982 C C   . GLY B 260 ? 0.5189 0.4351 0.6381 -0.0484 0.0832  -0.0892 246 GLY B C   
5983 O O   . GLY B 260 ? 0.5586 0.4655 0.6958 -0.0450 0.0897  -0.0962 246 GLY B O   
5984 N N   . LYS B 261 ? 0.6410 0.5579 0.7463 -0.0560 0.0797  -0.0917 247 LYS B N   
5985 C CA  . LYS B 261 ? 0.5233 0.4286 0.6338 -0.0614 0.0835  -0.1033 247 LYS B CA  
5986 C C   . LYS B 261 ? 0.4541 0.3450 0.5891 -0.0562 0.0812  -0.0985 247 LYS B C   
5987 O O   . LYS B 261 ? 0.4621 0.3544 0.6019 -0.0528 0.0725  -0.0847 247 LYS B O   
5988 C CB  . LYS B 261 ? 0.5279 0.4387 0.6207 -0.0709 0.0781  -0.1046 247 LYS B CB  
5989 C CG  . LYS B 261 ? 0.5162 0.4339 0.5896 -0.0800 0.0839  -0.1181 247 LYS B CG  
5990 C CD  . LYS B 261 ? 0.5114 0.4325 0.5734 -0.0903 0.0787  -0.1217 247 LYS B CD  
5991 C CE  . LYS B 261 ? 0.5203 0.4268 0.5898 -0.0973 0.0859  -0.1381 247 LYS B CE  
5992 N NZ  . LYS B 261 ? 0.5273 0.4401 0.5795 -0.1070 0.0936  -0.1549 247 LYS B NZ  
5993 N N   . GLY B 262 ? 0.4688 0.3462 0.6199 -0.0554 0.0895  -0.1098 248 GLY B N   
5994 C CA  . GLY B 262 ? 0.5729 0.4356 0.7505 -0.0494 0.0881  -0.1048 248 GLY B CA  
5995 C C   . GLY B 262 ? 0.5525 0.4128 0.7526 -0.0396 0.0938  -0.1057 248 GLY B C   
5996 O O   . GLY B 262 ? 0.4840 0.3315 0.7096 -0.0339 0.0938  -0.1028 248 GLY B O   
5997 N N   . ILE B 263 ? 0.5147 0.3872 0.7075 -0.0376 0.0987  -0.1088 249 ILE B N   
5998 C CA  . ILE B 263 ? 0.5287 0.4010 0.7441 -0.0290 0.1054  -0.1113 249 ILE B CA  
5999 C C   . ILE B 263 ? 0.5820 0.4414 0.8140 -0.0292 0.1179  -0.1288 249 ILE B C   
6000 O O   . ILE B 263 ? 0.5266 0.3778 0.7888 -0.0210 0.1209  -0.1288 249 ILE B O   
6001 C CB  . ILE B 263 ? 0.5187 0.4070 0.7207 -0.0287 0.1089  -0.1115 249 ILE B CB  
6002 C CG1 . ILE B 263 ? 0.4183 0.3172 0.6117 -0.0265 0.0974  -0.0944 249 ILE B CG1 
6003 C CG2 . ILE B 263 ? 0.4201 0.3094 0.6448 -0.0219 0.1188  -0.1186 249 ILE B CG2 
6004 C CD1 . ILE B 263 ? 0.3648 0.2774 0.5388 -0.0287 0.1000  -0.0940 249 ILE B CD1 
6005 N N   . PHE B 264 ? 0.5504 0.4084 0.7641 -0.0388 0.1255  -0.1441 250 PHE B N   
6006 C CA  . PHE B 264 ? 0.4911 0.3384 0.7171 -0.0408 0.1397  -0.1643 250 PHE B CA  
6007 C C   . PHE B 264 ? 0.6186 0.4499 0.8455 -0.0477 0.1397  -0.1716 250 PHE B C   
6008 O O   . PHE B 264 ? 0.5655 0.3995 0.7712 -0.0555 0.1314  -0.1667 250 PHE B O   
6009 C CB  . PHE B 264 ? 0.5682 0.4273 0.7716 -0.0485 0.1508  -0.1795 250 PHE B CB  
6010 C CG  . PHE B 264 ? 0.5722 0.4462 0.7746 -0.0433 0.1532  -0.1743 250 PHE B CG  
6011 C CD1 . PHE B 264 ? 0.5798 0.4521 0.8123 -0.0334 0.1594  -0.1753 250 PHE B CD1 
6012 C CD2 . PHE B 264 ? 0.5214 0.4109 0.6940 -0.0485 0.1494  -0.1681 250 PHE B CD2 
6013 C CE1 . PHE B 264 ? 0.4991 0.3857 0.7311 -0.0298 0.1620  -0.1711 250 PHE B CE1 
6014 C CE2 . PHE B 264 ? 0.5568 0.4584 0.7287 -0.0446 0.1522  -0.1632 250 PHE B CE2 
6015 C CZ  . PHE B 264 ? 0.4923 0.3927 0.6934 -0.0358 0.1588  -0.1653 250 PHE B CZ  
6016 N N   . ASP B 265 ? 0.5503 0.3649 0.8039 -0.0448 0.1496  -0.1838 251 ASP B N   
6017 C CA  . ASP B 265 ? 0.5258 0.3242 0.7794 -0.0535 0.1543  -0.1972 251 ASP B CA  
6018 C C   . ASP B 265 ? 0.5590 0.3677 0.7814 -0.0671 0.1624  -0.2157 251 ASP B C   
6019 O O   . ASP B 265 ? 0.6192 0.4322 0.8415 -0.0683 0.1758  -0.2318 251 ASP B O   
6020 C CB  . ASP B 265 ? 0.5930 0.3706 0.8844 -0.0468 0.1653  -0.2078 251 ASP B CB  
6021 C CG  . ASP B 265 ? 0.7179 0.4811 1.0100 -0.0549 0.1679  -0.2168 251 ASP B CG  
6022 O OD1 . ASP B 265 ? 0.7564 0.5224 1.0211 -0.0689 0.1694  -0.2285 251 ASP B OD1 
6023 O OD2 . ASP B 265 ? 0.7437 0.4945 1.0641 -0.0475 0.1679  -0.2114 251 ASP B OD2 
6024 N N   . GLU B 266 ? 0.5339 0.3478 0.7300 -0.0779 0.1545  -0.2135 252 GLU B N   
6025 C CA  . GLU B 266 ? 0.6097 0.4382 0.7730 -0.0909 0.1588  -0.2270 252 GLU B CA  
6026 C C   . GLU B 266 ? 0.5818 0.3992 0.7459 -0.1016 0.1728  -0.2533 252 GLU B C   
6027 O O   . GLU B 266 ? 0.7641 0.5942 0.9009 -0.1138 0.1778  -0.2670 252 GLU B O   
6028 C CB  . GLU B 266 ? 0.6897 0.5307 0.8267 -0.0980 0.1443  -0.2142 252 GLU B CB  
6029 C CG  . GLU B 266 ? 0.6763 0.5251 0.8160 -0.0877 0.1308  -0.1890 252 GLU B CG  
6030 C CD  . GLU B 266 ? 0.6871 0.5566 0.7970 -0.0930 0.1206  -0.1788 252 GLU B CD  
6031 O OE1 . GLU B 266 ? 0.7888 0.6655 0.8777 -0.1051 0.1202  -0.1878 252 GLU B OE1 
6032 O OE2 . GLU B 266 ? 0.6177 0.4964 0.7262 -0.0852 0.1130  -0.1620 252 GLU B OE2 
6033 N N   . ARG B 267 ? 0.6681 0.4623 0.8631 -0.0977 0.1793  -0.2606 253 ARG B N   
6034 C CA  . ARG B 267 ? 0.7052 0.4949 0.9041 -0.1044 0.1919  -0.2805 253 ARG B CA  
6035 C C   . ARG B 267 ? 0.6611 0.4567 0.8733 -0.0983 0.2058  -0.2906 253 ARG B C   
6036 O O   . ARG B 267 ? 0.8536 0.6507 1.0644 -0.1055 0.2177  -0.3084 253 ARG B O   
6037 C CB  . ARG B 267 ? 0.6354 0.4055 0.8604 -0.1008 0.1898  -0.2759 253 ARG B CB  
6038 C CG  . ARG B 267 ? 0.6312 0.3952 0.8451 -0.1083 0.1773  -0.2665 253 ARG B CG  
6039 C CD  . ARG B 267 ? 0.7160 0.4595 0.9599 -0.1002 0.1731  -0.2543 253 ARG B CD  
6040 N NE  . ARG B 267 ? 0.6885 0.4269 0.9608 -0.0831 0.1708  -0.2388 253 ARG B NE  
6041 C CZ  . ARG B 267 ? 0.7152 0.4379 1.0158 -0.0736 0.1664  -0.2251 253 ARG B CZ  
6042 N NH1 . ARG B 267 ? 0.6592 0.3673 0.9647 -0.0790 0.1650  -0.2250 253 ARG B NH1 
6043 N NH2 . ARG B 267 ? 0.7013 0.4238 1.0255 -0.0588 0.1631  -0.2106 253 ARG B NH2 
6044 N N   . HIS B 268 ? 0.7193 0.5191 0.9447 -0.0860 0.2048  -0.2798 254 HIS B N   
6045 C CA  . HIS B 268 ? 0.7421 0.5480 0.9855 -0.0790 0.2172  -0.2871 254 HIS B CA  
6046 C C   . HIS B 268 ? 0.7762 0.5994 0.9901 -0.0909 0.2282  -0.3041 254 HIS B C   
6047 O O   . HIS B 268 ? 0.8528 0.6865 1.0318 -0.1010 0.2239  -0.3051 254 HIS B O   
6048 C CB  . HIS B 268 ? 0.7357 0.5443 0.9989 -0.0640 0.2115  -0.2699 254 HIS B CB  
6049 C CG  . HIS B 268 ? 0.8510 0.6617 1.1467 -0.0536 0.2211  -0.2726 254 HIS B CG  
6050 N ND1 . HIS B 268 ? 1.0773 0.8754 1.4101 -0.0432 0.2198  -0.2662 254 HIS B ND1 
6051 C CD2 . HIS B 268 ? 0.9861 0.8109 1.2833 -0.0524 0.2317  -0.2804 254 HIS B CD2 
6052 C CE1 . HIS B 268 ? 1.1144 0.9192 1.4713 -0.0360 0.2290  -0.2706 254 HIS B CE1 
6053 N NE2 . HIS B 268 ? 1.0609 0.8820 1.3970 -0.0417 0.2366  -0.2794 254 HIS B NE2 
6054 N N   . VAL B 269 ? 0.8178 0.6449 1.0464 -0.0900 0.2423  -0.3169 255 VAL B N   
6055 C CA  . VAL B 269 ? 0.7516 0.5961 0.9542 -0.1013 0.2537  -0.3321 255 VAL B CA  
6056 C C   . VAL B 269 ? 0.7686 0.6268 0.9559 -0.0978 0.2507  -0.3221 255 VAL B C   
6057 O O   . VAL B 269 ? 0.6808 0.5367 0.8910 -0.0838 0.2462  -0.3080 255 VAL B O   
6058 C CB  . VAL B 269 ? 0.9727 0.8176 1.1993 -0.1003 0.2697  -0.3469 255 VAL B CB  
6059 C CG1 . VAL B 269 ? 0.8845 0.7251 1.1519 -0.0826 0.2699  -0.3359 255 VAL B CG1 
6060 C CG2 . VAL B 269 ? 1.0378 0.9011 1.2368 -0.1131 0.2817  -0.3620 255 VAL B CG2 
6061 N N   . GLY B 270 ? 0.6777 0.5511 0.8254 -0.1109 0.2529  -0.3286 256 GLY B N   
6062 C CA  . GLY B 270 ? 0.6657 0.5524 0.7941 -0.1094 0.2506  -0.3193 256 GLY B CA  
6063 C C   . GLY B 270 ? 0.8140 0.7046 0.9205 -0.1098 0.2324  -0.2999 256 GLY B C   
6064 O O   . GLY B 270 ? 0.7613 0.6678 0.8484 -0.1094 0.2262  -0.2851 256 GLY B O   
6065 N N   . PHE B 271 ? 0.6097 0.4889 0.7203 -0.1104 0.2217  -0.2952 257 PHE B N   
6066 C CA  . PHE B 271 ? 0.7260 0.6126 0.8169 -0.1114 0.2025  -0.2740 257 PHE B CA  
6067 C C   . PHE B 271 ? 0.8207 0.7158 0.8784 -0.1284 0.2004  -0.2841 257 PHE B C   
6068 O O   . PHE B 271 ? 0.8002 0.6843 0.8620 -0.1366 0.2074  -0.3028 257 PHE B O   
6069 C CB  . PHE B 271 ? 0.6054 0.4762 0.7228 -0.1011 0.1912  -0.2600 257 PHE B CB  
6070 C CG  . PHE B 271 ? 0.7140 0.5934 0.8153 -0.1004 0.1726  -0.2376 257 PHE B CG  
6071 C CD1 . PHE B 271 ? 0.7346 0.6158 0.8175 -0.1109 0.1647  -0.2385 257 PHE B CD1 
6072 C CD2 . PHE B 271 ? 0.6553 0.5418 0.7613 -0.0897 0.1637  -0.2168 257 PHE B CD2 
6073 C CE1 . PHE B 271 ? 0.7771 0.6674 0.8478 -0.1098 0.1487  -0.2188 257 PHE B CE1 
6074 C CE2 . PHE B 271 ? 0.6955 0.5898 0.7882 -0.0891 0.1481  -0.1980 257 PHE B CE2 
6075 C CZ  . PHE B 271 ? 0.6578 0.5543 0.7336 -0.0988 0.1408  -0.1989 257 PHE B CZ  
6076 N N   . TYR B 272 ? 0.7098 0.6246 0.7359 -0.1338 0.1908  -0.2715 258 TYR B N   
6077 C CA  . TYR B 272 ? 0.6314 0.5591 0.6243 -0.1501 0.1870  -0.2786 258 TYR B CA  
6078 C C   . TYR B 272 ? 0.6228 0.5587 0.6036 -0.1502 0.1676  -0.2585 258 TYR B C   
6079 O O   . TYR B 272 ? 0.6769 0.6258 0.6320 -0.1632 0.1621  -0.2620 258 TYR B O   
6080 C CB  . TYR B 272 ? 0.6801 0.6273 0.6424 -0.1596 0.1943  -0.2840 258 TYR B CB  
6081 C CG  . TYR B 272 ? 0.7739 0.7162 0.7460 -0.1609 0.2151  -0.3051 258 TYR B CG  
6082 C CD1 . TYR B 272 ? 0.7357 0.6735 0.7306 -0.1477 0.2217  -0.2992 258 TYR B CD1 
6083 C CD2 . TYR B 272 ? 0.7979 0.7410 0.7573 -0.1760 0.2287  -0.3321 258 TYR B CD2 
6084 C CE1 . TYR B 272 ? 0.8469 0.7817 0.8535 -0.1487 0.2413  -0.3189 258 TYR B CE1 
6085 C CE2 . TYR B 272 ? 0.7948 0.7357 0.7664 -0.1765 0.2472  -0.3490 258 TYR B CE2 
6086 C CZ  . TYR B 272 ? 0.8721 0.8087 0.8676 -0.1627 0.2538  -0.3429 258 TYR B CZ  
6087 O OH  . TYR B 272 ? 1.0197 0.9581 1.0316 -0.1621 0.2687  -0.3539 258 TYR B OH  
6088 N N   . GLY B 273 ? 0.6470 0.5772 0.6460 -0.1366 0.1574  -0.2382 259 GLY B N   
6089 C CA  . GLY B 273 ? 0.5467 0.4853 0.5371 -0.1354 0.1402  -0.2190 259 GLY B CA  
6090 C C   . GLY B 273 ? 0.6968 0.6421 0.6898 -0.1234 0.1328  -0.1969 259 GLY B C   
6091 O O   . GLY B 273 ? 0.6733 0.6206 0.6684 -0.1182 0.1400  -0.1957 259 GLY B O   
6092 N N   . THR B 274 ? 0.6074 0.5563 0.6010 -0.1196 0.1186  -0.1800 260 THR B N   
6093 C CA  . THR B 274 ? 0.6353 0.5899 0.6321 -0.1089 0.1112  -0.1596 260 THR B CA  
6094 C C   . THR B 274 ? 0.6312 0.6040 0.6023 -0.1127 0.1098  -0.1530 260 THR B C   
6095 O O   . THR B 274 ? 0.6607 0.6463 0.6090 -0.1236 0.1072  -0.1571 260 THR B O   
6096 C CB  . THR B 274 ? 0.5023 0.4566 0.5065 -0.1050 0.0977  -0.1453 260 THR B CB  
6097 O OG1 . THR B 274 ? 0.5253 0.4621 0.5519 -0.1026 0.0991  -0.1504 260 THR B OG1 
6098 C CG2 . THR B 274 ? 0.4693 0.4277 0.4792 -0.0940 0.0915  -0.1264 260 THR B CG2 
6099 N N   . TYR B 275 ? 0.5959 0.5702 0.5711 -0.1042 0.1115  -0.1424 261 TYR B N   
6100 C CA  . TYR B 275 ? 0.4867 0.4758 0.4403 -0.1066 0.1107  -0.1335 261 TYR B CA  
6101 C C   . TYR B 275 ? 0.6221 0.6197 0.5720 -0.1019 0.0967  -0.1135 261 TYR B C   
6102 O O   . TYR B 275 ? 0.5558 0.5465 0.5240 -0.0922 0.0918  -0.1036 261 TYR B O   
6103 C CB  . TYR B 275 ? 0.5071 0.4927 0.4684 -0.1008 0.1210  -0.1332 261 TYR B CB  
6104 C CG  . TYR B 275 ? 0.6108 0.6092 0.5514 -0.1030 0.1211  -0.1224 261 TYR B CG  
6105 C CD1 . TYR B 275 ? 0.6176 0.6279 0.5309 -0.1149 0.1251  -0.1286 261 TYR B CD1 
6106 C CD2 . TYR B 275 ? 0.4584 0.4566 0.4065 -0.0940 0.1174  -0.1058 261 TYR B CD2 
6107 C CE1 . TYR B 275 ? 0.6536 0.6751 0.5475 -0.1173 0.1249  -0.1166 261 TYR B CE1 
6108 C CE2 . TYR B 275 ? 0.5592 0.5670 0.4898 -0.0960 0.1179  -0.0949 261 TYR B CE2 
6109 C CZ  . TYR B 275 ? 0.7278 0.7470 0.6314 -0.1074 0.1213  -0.0994 261 TYR B CZ  
6110 O OH  . TYR B 275 ? 0.5635 0.5917 0.4492 -0.1097 0.1215  -0.0865 261 TYR B OH  
6111 N N   . SER B 276 ? 0.5540 0.5673 0.4809 -0.1091 0.0902  -0.1079 262 SER B N   
6112 C CA  . SER B 276 ? 0.6127 0.6356 0.5372 -0.1046 0.0773  -0.0893 262 SER B CA  
6113 C C   . SER B 276 ? 0.7390 0.7773 0.6408 -0.1083 0.0750  -0.0789 262 SER B C   
6114 O O   . SER B 276 ? 0.5490 0.6017 0.4392 -0.1115 0.0644  -0.0696 262 SER B O   
6115 C CB  . SER B 276 ? 0.6580 0.6858 0.5838 -0.1088 0.0675  -0.0906 262 SER B CB  
6116 O OG  . SER B 276 ? 0.8453 0.8870 0.7492 -0.1214 0.0656  -0.0979 262 SER B OG  
6117 N N   . GLY B 277 ? 0.6042 0.6402 0.5000 -0.1082 0.0848  -0.0795 263 GLY B N   
6118 C CA  . GLY B 277 ? 0.5239 0.5730 0.3974 -0.1123 0.0834  -0.0682 263 GLY B CA  
6119 C C   . GLY B 277 ? 0.6858 0.7505 0.5329 -0.1264 0.0814  -0.0755 263 GLY B C   
6120 O O   . GLY B 277 ? 0.7400 0.8025 0.5826 -0.1351 0.0886  -0.0951 263 GLY B O   
6121 N N   . SER B 278 ? 0.7017 0.7826 0.5317 -0.1290 0.0711  -0.0596 264 SER B N   
6122 C CA  . SER B 278 ? 0.6982 0.7979 0.5011 -0.1432 0.0669  -0.0640 264 SER B CA  
6123 C C   . SER B 278 ? 0.7848 0.8890 0.5913 -0.1490 0.0601  -0.0756 264 SER B C   
6124 O O   . SER B 278 ? 0.8253 0.9439 0.6103 -0.1629 0.0585  -0.0849 264 SER B O   
6125 C CB  . SER B 278 ? 0.7368 0.8536 0.5238 -0.1431 0.0555  -0.0409 264 SER B CB  
6126 O OG  . SER B 278 ? 0.9416 1.0702 0.7345 -0.1412 0.0404  -0.0320 264 SER B OG  
6127 N N   . ALA B 279 ? 0.8181 0.9112 0.6500 -0.1399 0.0563  -0.0753 265 ALA B N   
6128 C CA  . ALA B 279 ? 0.7419 0.8365 0.5796 -0.1457 0.0514  -0.0869 265 ALA B CA  
6129 C C   . ALA B 279 ? 0.7668 0.8453 0.6115 -0.1508 0.0641  -0.1106 265 ALA B C   
6130 O O   . ALA B 279 ? 0.8836 0.9602 0.7339 -0.1565 0.0619  -0.1220 265 ALA B O   
6131 C CB  . ALA B 279 ? 0.6252 0.7158 0.4866 -0.1346 0.0421  -0.0755 265 ALA B CB  
6132 N N   . SER B 280 ? 0.7445 0.8111 0.5910 -0.1486 0.0776  -0.1181 266 SER B N   
6133 C CA  . SER B 280 ? 0.7493 0.8001 0.6064 -0.1519 0.0905  -0.1402 266 SER B CA  
6134 C C   . SER B 280 ? 0.7605 0.8208 0.5958 -0.1692 0.0948  -0.1593 266 SER B C   
6135 O O   . SER B 280 ? 0.7897 0.8699 0.5979 -0.1791 0.0903  -0.1556 266 SER B O   
6136 C CB  . SER B 280 ? 0.7272 0.7662 0.5927 -0.1454 0.1040  -0.1433 266 SER B CB  
6137 O OG  . SER B 280 ? 0.6641 0.6954 0.5484 -0.1309 0.1003  -0.1265 266 SER B OG  
6138 N N   . ALA B 281 ? 0.5799 0.6259 0.4278 -0.1732 0.1034  -0.1799 267 ALA B N   
6139 C CA  . ALA B 281 ? 0.6158 0.6674 0.4455 -0.1900 0.1115  -0.2026 267 ALA B CA  
6140 C C   . ALA B 281 ? 0.7783 0.8360 0.5891 -0.1955 0.1240  -0.2094 267 ALA B C   
6141 O O   . ALA B 281 ? 0.8347 0.8840 0.6560 -0.1853 0.1312  -0.2034 267 ALA B O   
6142 C CB  . ALA B 281 ? 0.6954 0.7259 0.5473 -0.1912 0.1209  -0.2235 267 ALA B CB  
6143 N N   . GLY B 282 ? 0.7312 0.8049 0.5130 -0.2130 0.1267  -0.2226 268 GLY B N   
6144 C CA  . GLY B 282 ? 0.6852 0.7678 0.4445 -0.2210 0.1387  -0.2292 268 GLY B CA  
6145 C C   . GLY B 282 ? 0.8891 0.9524 0.6679 -0.2160 0.1584  -0.2463 268 GLY B C   
6146 O O   . GLY B 282 ? 0.9659 1.0308 0.7402 -0.2129 0.1670  -0.2420 268 GLY B O   
6147 N N   . ALA B 283 ? 0.9062 0.9511 0.7085 -0.2151 0.1661  -0.2656 269 ALA B N   
6148 C CA  . ALA B 283 ? 0.7647 0.7909 0.5914 -0.2085 0.1843  -0.2812 269 ALA B CA  
6149 C C   . ALA B 283 ? 0.7409 0.7567 0.5931 -0.1891 0.1819  -0.2617 269 ALA B C   
6150 O O   . ALA B 283 ? 0.8637 0.8750 0.7254 -0.1842 0.1950  -0.2662 269 ALA B O   
6151 C CB  . ALA B 283 ? 0.6951 0.7021 0.5451 -0.2102 0.1911  -0.3028 269 ALA B CB  
6152 N N   . VAL B 284 ? 0.6647 0.6777 0.5287 -0.1785 0.1657  -0.2409 270 VAL B N   
6153 C CA  . VAL B 284 ? 0.6381 0.6426 0.5247 -0.1613 0.1625  -0.2225 270 VAL B CA  
6154 C C   . VAL B 284 ? 0.7435 0.7617 0.6116 -0.1607 0.1626  -0.2080 270 VAL B C   
6155 O O   . VAL B 284 ? 0.8270 0.8394 0.7093 -0.1523 0.1708  -0.2051 270 VAL B O   
6156 C CB  . VAL B 284 ? 0.7735 0.7735 0.6739 -0.1522 0.1457  -0.2050 270 VAL B CB  
6157 C CG1 . VAL B 284 ? 0.7179 0.7101 0.6405 -0.1359 0.1429  -0.1877 270 VAL B CG1 
6158 C CG2 . VAL B 284 ? 0.7674 0.7532 0.6854 -0.1540 0.1459  -0.2184 270 VAL B CG2 
6159 N N   . LYS B 285 ? 0.8125 0.8494 0.6498 -0.1698 0.1533  -0.1979 271 LYS B N   
6160 C CA  . LYS B 285 ? 0.7157 0.7651 0.5340 -0.1702 0.1531  -0.1824 271 LYS B CA  
6161 C C   . LYS B 285 ? 0.7794 0.8292 0.5910 -0.1763 0.1721  -0.1974 271 LYS B C   
6162 O O   . LYS B 285 ? 0.9254 0.9740 0.7419 -0.1699 0.1774  -0.1878 271 LYS B O   
6163 C CB  . LYS B 285 ? 0.6773 0.7479 0.4626 -0.1810 0.1406  -0.1712 271 LYS B CB  
6164 C CG  . LYS B 285 ? 0.8546 0.9283 0.6470 -0.1737 0.1215  -0.1524 271 LYS B CG  
6165 C CD  . LYS B 285 ? 0.8201 0.9143 0.5867 -0.1777 0.1094  -0.1314 271 LYS B CD  
6166 C CE  . LYS B 285 ? 0.9105 1.0196 0.6660 -0.1852 0.0947  -0.1294 271 LYS B CE  
6167 N NZ  . LYS B 285 ? 0.8972 1.0257 0.6349 -0.1854 0.0803  -0.1050 271 LYS B NZ  
6168 N N   . GLU B 286 ? 0.7604 0.8121 0.5617 -0.1893 0.1834  -0.2221 272 GLU B N   
6169 C CA  . GLU B 286 ? 0.9078 0.9607 0.7038 -0.1959 0.2034  -0.2391 272 GLU B CA  
6170 C C   . GLU B 286 ? 0.9483 0.9826 0.7835 -0.1824 0.2151  -0.2473 272 GLU B C   
6171 O O   . GLU B 286 ? 0.9240 0.9594 0.7630 -0.1810 0.2281  -0.2498 272 GLU B O   
6172 C CB  . GLU B 286 ? 0.8784 0.9386 0.6535 -0.2142 0.2131  -0.2655 272 GLU B CB  
6173 C CG  . GLU B 286 ? 1.1188 1.2009 0.8520 -0.2311 0.2182  -0.2664 272 GLU B CG  
6174 C CD  . GLU B 286 ? 1.2580 1.3406 0.9924 -0.2299 0.2350  -0.2683 272 GLU B CD  
6175 O OE1 . GLU B 286 ? 1.3364 1.4035 1.1038 -0.2200 0.2478  -0.2801 272 GLU B OE1 
6176 O OE2 . GLU B 286 ? 1.2030 1.3024 0.9061 -0.2391 0.2351  -0.2572 272 GLU B OE2 
6177 N N   . ALA B 287 ? 0.7804 0.7984 0.6454 -0.1729 0.2107  -0.2510 273 ALA B N   
6178 C CA  . ALA B 287 ? 0.7284 0.7296 0.6324 -0.1597 0.2202  -0.2575 273 ALA B CA  
6179 C C   . ALA B 287 ? 0.7960 0.7972 0.7130 -0.1468 0.2159  -0.2362 273 ALA B C   
6180 O O   . ALA B 287 ? 0.7516 0.7504 0.6855 -0.1420 0.2286  -0.2415 273 ALA B O   
6181 C CB  . ALA B 287 ? 0.6728 0.6570 0.6037 -0.1526 0.2137  -0.2616 273 ALA B CB  
6182 N N   . ILE B 288 ? 0.6921 0.6969 0.6021 -0.1416 0.1986  -0.2128 274 ILE B N   
6183 C CA  . ILE B 288 ? 0.6529 0.6558 0.5772 -0.1293 0.1936  -0.1930 274 ILE B CA  
6184 C C   . ILE B 288 ? 0.8425 0.8593 0.7403 -0.1352 0.1950  -0.1809 274 ILE B C   
6185 O O   . ILE B 288 ? 0.6917 0.7096 0.5959 -0.1335 0.2062  -0.1817 274 ILE B O   
6186 C CB  . ILE B 288 ? 0.6020 0.5992 0.5373 -0.1198 0.1755  -0.1754 274 ILE B CB  
6187 C CG1 . ILE B 288 ? 0.6128 0.5973 0.5683 -0.1172 0.1735  -0.1869 274 ILE B CG1 
6188 C CG2 . ILE B 288 ? 0.6849 0.6779 0.6405 -0.1070 0.1720  -0.1592 274 ILE B CG2 
6189 C CD1 . ILE B 288 ? 0.6813 0.6522 0.6719 -0.1076 0.1829  -0.1959 274 ILE B CD1 
6190 N N   . GLU B 289 ? 0.7796 0.8077 0.6484 -0.1424 0.1837  -0.1690 275 GLU B N   
6191 C CA  . GLU B 289 ? 0.6648 0.7051 0.5089 -0.1472 0.1830  -0.1535 275 GLU B CA  
6192 C C   . GLU B 289 ? 0.8181 0.8681 0.6406 -0.1607 0.1994  -0.1677 275 GLU B C   
6193 O O   . GLU B 289 ? 0.7919 0.8490 0.6000 -0.1637 0.2035  -0.1566 275 GLU B O   
6194 C CB  . GLU B 289 ? 0.6180 0.6691 0.4387 -0.1510 0.1659  -0.1365 275 GLU B CB  
6195 C CG  . GLU B 289 ? 0.6551 0.7000 0.4932 -0.1375 0.1509  -0.1160 275 GLU B CG  
6196 C CD  . GLU B 289 ? 0.7554 0.8116 0.5757 -0.1405 0.1344  -0.1020 275 GLU B CD  
6197 O OE1 . GLU B 289 ? 0.8072 0.8779 0.5987 -0.1534 0.1335  -0.1048 275 GLU B OE1 
6198 O OE2 . GLU B 289 ? 0.7227 0.7746 0.5582 -0.1303 0.1224  -0.0884 275 GLU B OE2 
6199 N N   . GLY B 290 ? 0.8058 0.8557 0.6258 -0.1694 0.2097  -0.1924 276 GLY B N   
6200 C CA  . GLY B 290 ? 0.7852 0.8449 0.5848 -0.1832 0.2272  -0.2087 276 GLY B CA  
6201 C C   . GLY B 290 ? 0.7311 0.7840 0.5552 -0.1781 0.2454  -0.2204 276 GLY B C   
6202 O O   . GLY B 290 ? 0.8526 0.9151 0.6603 -0.1890 0.2609  -0.2307 276 GLY B O   
6203 N N   . ALA B 291 ? 0.7189 0.7573 0.5820 -0.1625 0.2439  -0.2190 277 ALA B N   
6204 C CA  . ALA B 291 ? 0.8220 0.8558 0.7125 -0.1562 0.2594  -0.2278 277 ALA B CA  
6205 C C   . ALA B 291 ? 0.8025 0.8433 0.6856 -0.1551 0.2604  -0.2093 277 ALA B C   
6206 O O   . ALA B 291 ? 0.7641 0.8060 0.6364 -0.1518 0.2456  -0.1860 277 ALA B O   
6207 C CB  . ALA B 291 ? 0.6985 0.7166 0.6324 -0.1398 0.2551  -0.2289 277 ALA B CB  
6208 N N   . ASP B 292 ? 0.7169 0.7622 0.6074 -0.1583 0.2787  -0.2203 278 ASP B N   
6209 C CA  . ASP B 292 ? 0.7411 0.7920 0.6271 -0.1581 0.2815  -0.2040 278 ASP B CA  
6210 C C   . ASP B 292 ? 0.7614 0.8028 0.6843 -0.1419 0.2753  -0.1922 278 ASP B C   
6211 O O   . ASP B 292 ? 0.7492 0.7927 0.6692 -0.1404 0.2729  -0.1748 278 ASP B O   
6212 C CB  . ASP B 292 ? 0.8472 0.9084 0.7262 -0.1690 0.3042  -0.2199 278 ASP B CB  
6213 C CG  . ASP B 292 ? 0.9294 0.9854 0.8429 -0.1642 0.3167  -0.2444 278 ASP B CG  
6214 O OD1 . ASP B 292 ? 0.8313 0.8806 0.7835 -0.1510 0.3183  -0.2442 278 ASP B OD1 
6215 O OD2 . ASP B 292 ? 0.9341 0.9923 0.8381 -0.1731 0.3217  -0.2615 278 ASP B OD2 
6216 N N   . THR B 293 ? 0.7234 0.7545 0.6802 -0.1305 0.2725  -0.2009 279 THR B N   
6217 C CA  . THR B 293 ? 0.6676 0.6910 0.6581 -0.1158 0.2644  -0.1895 279 THR B CA  
6218 C C   . THR B 293 ? 0.6804 0.6926 0.6855 -0.1067 0.2496  -0.1877 279 THR B C   
6219 O O   . THR B 293 ? 0.6329 0.6400 0.6484 -0.1067 0.2538  -0.2046 279 THR B O   
6220 C CB  . THR B 293 ? 0.8054 0.8304 0.8304 -0.1107 0.2796  -0.2025 279 THR B CB  
6221 O OG1 . THR B 293 ? 0.7547 0.7912 0.7643 -0.1213 0.2955  -0.2067 279 THR B OG1 
6222 C CG2 . THR B 293 ? 0.5948 0.6154 0.6511 -0.0974 0.2702  -0.1887 279 THR B CG2 
6223 N N   . VAL B 294 ? 0.6444 0.6525 0.6502 -0.0997 0.2330  -0.1676 280 VAL B N   
6224 C CA  . VAL B 294 ? 0.5618 0.5603 0.5805 -0.0915 0.2184  -0.1633 280 VAL B CA  
6225 C C   . VAL B 294 ? 0.5768 0.5705 0.6267 -0.0790 0.2120  -0.1530 280 VAL B C   
6226 O O   . VAL B 294 ? 0.5502 0.5470 0.5971 -0.0774 0.2082  -0.1384 280 VAL B O   
6227 C CB  . VAL B 294 ? 0.5381 0.5379 0.5283 -0.0954 0.2037  -0.1496 280 VAL B CB  
6228 C CG1 . VAL B 294 ? 0.4827 0.4734 0.4867 -0.0882 0.1905  -0.1473 280 VAL B CG1 
6229 C CG2 . VAL B 294 ? 0.6323 0.6405 0.5891 -0.1093 0.2093  -0.1584 280 VAL B CG2 
6230 N N   . LEU B 295 ? 0.6343 0.6205 0.7140 -0.0707 0.2107  -0.1605 281 LEU B N   
6231 C CA  . LEU B 295 ? 0.5132 0.4962 0.6222 -0.0594 0.2028  -0.1507 281 LEU B CA  
6232 C C   . LEU B 295 ? 0.6797 0.6562 0.7837 -0.0555 0.1852  -0.1375 281 LEU B C   
6233 O O   . LEU B 295 ? 0.5395 0.5088 0.6457 -0.0548 0.1805  -0.1427 281 LEU B O   
6234 C CB  . LEU B 295 ? 0.4911 0.4707 0.6361 -0.0524 0.2101  -0.1636 281 LEU B CB  
6235 C CG  . LEU B 295 ? 0.6082 0.5950 0.7611 -0.0564 0.2295  -0.1799 281 LEU B CG  
6236 C CD1 . LEU B 295 ? 0.5571 0.5415 0.7522 -0.0470 0.2354  -0.1901 281 LEU B CD1 
6237 C CD2 . LEU B 295 ? 0.4764 0.4740 0.6199 -0.0605 0.2351  -0.1725 281 LEU B CD2 
6238 N N   . CYS B 296 ? 0.5590 0.5378 0.6566 -0.0535 0.1762  -0.1212 282 CYS B N   
6239 C CA  . CYS B 296 ? 0.5045 0.4790 0.5973 -0.0501 0.1606  -0.1085 282 CYS B CA  
6240 C C   . CYS B 296 ? 0.4466 0.4186 0.5678 -0.0409 0.1538  -0.1025 282 CYS B C   
6241 O O   . CYS B 296 ? 0.4663 0.4426 0.5960 -0.0386 0.1544  -0.0959 282 CYS B O   
6242 C CB  . CYS B 296 ? 0.4913 0.4701 0.5596 -0.0539 0.1556  -0.0949 282 CYS B CB  
6243 S SG  . CYS B 296 ? 0.6052 0.5901 0.6380 -0.0655 0.1615  -0.0988 282 CYS B SG  
6244 N N   . ILE B 297 ? 0.4133 0.3785 0.5485 -0.0365 0.1474  -0.1046 283 ILE B N   
6245 C CA  . ILE B 297 ? 0.3717 0.3353 0.5341 -0.0284 0.1405  -0.0991 283 ILE B CA  
6246 C C   . ILE B 297 ? 0.4621 0.4225 0.6172 -0.0270 0.1262  -0.0871 283 ILE B C   
6247 O O   . ILE B 297 ? 0.4460 0.4000 0.5957 -0.0282 0.1214  -0.0887 283 ILE B O   
6248 C CB  . ILE B 297 ? 0.3609 0.3190 0.5489 -0.0238 0.1449  -0.1095 283 ILE B CB  
6249 C CG1 . ILE B 297 ? 0.4576 0.4186 0.6489 -0.0269 0.1612  -0.1248 283 ILE B CG1 
6250 C CG2 . ILE B 297 ? 0.3732 0.3332 0.5907 -0.0156 0.1384  -0.1023 283 ILE B CG2 
6251 C CD1 . ILE B 297 ? 0.4231 0.3947 0.6232 -0.0264 0.1687  -0.1240 283 ILE B CD1 
6252 N N   . GLY B 298 ? 0.4091 0.3741 0.5652 -0.0251 0.1202  -0.0763 284 GLY B N   
6253 C CA  . GLY B 298 ? 0.4301 0.3934 0.5809 -0.0240 0.1079  -0.0657 284 GLY B CA  
6254 C C   . GLY B 298 ? 0.4255 0.3876 0.5514 -0.0286 0.1042  -0.0629 284 GLY B C   
6255 O O   . GLY B 298 ? 0.5268 0.4857 0.6500 -0.0285 0.0957  -0.0591 284 GLY B O   
6256 N N   . THR B 299 ? 0.4295 0.3949 0.5374 -0.0329 0.1101  -0.0635 285 THR B N   
6257 C CA  . THR B 299 ? 0.4751 0.4417 0.5598 -0.0376 0.1067  -0.0608 285 THR B CA  
6258 C C   . THR B 299 ? 0.5742 0.5442 0.6501 -0.0368 0.1013  -0.0484 285 THR B C   
6259 O O   . THR B 299 ? 0.5043 0.4757 0.5849 -0.0354 0.1047  -0.0443 285 THR B O   
6260 C CB  . THR B 299 ? 0.5764 0.5457 0.6450 -0.0438 0.1161  -0.0687 285 THR B CB  
6261 O OG1 . THR B 299 ? 0.5996 0.5721 0.6709 -0.0440 0.1250  -0.0687 285 THR B OG1 
6262 C CG2 . THR B 299 ? 0.4397 0.4048 0.5151 -0.0456 0.1215  -0.0829 285 THR B CG2 
6263 N N   . ARG B 300 ? 0.5043 0.4754 0.5692 -0.0378 0.0931  -0.0431 286 ARG B N   
6264 C CA  . ARG B 300 ? 0.3783 0.3528 0.4345 -0.0370 0.0885  -0.0319 286 ARG B CA  
6265 C C   . ARG B 300 ? 0.5059 0.4853 0.5428 -0.0413 0.0852  -0.0301 286 ARG B C   
6266 O O   . ARG B 300 ? 0.4249 0.4051 0.4598 -0.0429 0.0796  -0.0330 286 ARG B O   
6267 C CB  . ARG B 300 ? 0.3831 0.3568 0.4505 -0.0330 0.0806  -0.0263 286 ARG B CB  
6268 C CG  . ARG B 300 ? 0.4826 0.4541 0.5676 -0.0297 0.0822  -0.0266 286 ARG B CG  
6269 C CD  . ARG B 300 ? 0.4538 0.4257 0.5393 -0.0297 0.0893  -0.0244 286 ARG B CD  
6270 N NE  . ARG B 300 ? 0.4229 0.3949 0.5259 -0.0280 0.0923  -0.0278 286 ARG B NE  
6271 C CZ  . ARG B 300 ? 0.4655 0.4386 0.5796 -0.0263 0.0884  -0.0247 286 ARG B CZ  
6272 N NH1 . ARG B 300 ? 0.3263 0.2996 0.4365 -0.0257 0.0825  -0.0192 286 ARG B NH1 
6273 N NH2 . ARG B 300 ? 0.3684 0.3439 0.4983 -0.0255 0.0907  -0.0278 286 ARG B NH2 
6274 N N   . PHE B 301 ? 0.4737 0.4571 0.4965 -0.0437 0.0883  -0.0246 287 PHE B N   
6275 C CA  . PHE B 301 ? 0.5160 0.5067 0.5190 -0.0487 0.0849  -0.0222 287 PHE B CA  
6276 C C   . PHE B 301 ? 0.5991 0.5943 0.6010 -0.0455 0.0754  -0.0101 287 PHE B C   
6277 O O   . PHE B 301 ? 0.5487 0.5463 0.5452 -0.0440 0.0746  0.0010  287 PHE B O   
6278 C CB  . PHE B 301 ? 0.5509 0.5448 0.5381 -0.0536 0.0925  -0.0211 287 PHE B CB  
6279 C CG  . PHE B 301 ? 0.6542 0.6456 0.6427 -0.0575 0.1031  -0.0348 287 PHE B CG  
6280 C CD1 . PHE B 301 ? 0.5803 0.5748 0.5582 -0.0641 0.1053  -0.0465 287 PHE B CD1 
6281 C CD2 . PHE B 301 ? 0.5682 0.5548 0.5701 -0.0549 0.1114  -0.0371 287 PHE B CD2 
6282 C CE1 . PHE B 301 ? 0.5570 0.5489 0.5384 -0.0673 0.1165  -0.0606 287 PHE B CE1 
6283 C CE2 . PHE B 301 ? 0.5967 0.5823 0.6030 -0.0578 0.1218  -0.0503 287 PHE B CE2 
6284 C CZ  . PHE B 301 ? 0.5172 0.5049 0.5137 -0.0636 0.1248  -0.0622 287 PHE B CZ  
6285 N N   . THR B 302 ? 0.4391 0.4351 0.4481 -0.0443 0.0684  -0.0122 288 THR B N   
6286 C CA  . THR B 302 ? 0.5443 0.5462 0.5550 -0.0413 0.0599  -0.0027 288 THR B CA  
6287 C C   . THR B 302 ? 0.5104 0.5238 0.5048 -0.0461 0.0543  0.0006  288 THR B C   
6288 O O   . THR B 302 ? 0.5054 0.5219 0.4862 -0.0529 0.0566  -0.0066 288 THR B O   
6289 C CB  . THR B 302 ? 0.5505 0.5504 0.5746 -0.0393 0.0553  -0.0062 288 THR B CB  
6290 O OG1 . THR B 302 ? 0.5095 0.5134 0.5274 -0.0447 0.0514  -0.0127 288 THR B OG1 
6291 C CG2 . THR B 302 ? 0.3681 0.3583 0.4055 -0.0371 0.0601  -0.0121 288 THR B CG2 
6292 N N   . ASP B 303 ? 0.4765 0.4974 0.4732 -0.0427 0.0469  0.0110  289 ASP B N   
6293 C CA  . ASP B 303 ? 0.4272 0.4620 0.4103 -0.0467 0.0400  0.0165  289 ASP B CA  
6294 C C   . ASP B 303 ? 0.4404 0.4810 0.4174 -0.0541 0.0365  0.0056  289 ASP B C   
6295 O O   . ASP B 303 ? 0.5247 0.5739 0.4847 -0.0616 0.0352  0.0029  289 ASP B O   
6296 C CB  . ASP B 303 ? 0.4152 0.4575 0.4075 -0.0404 0.0327  0.0296  289 ASP B CB  
6297 C CG  . ASP B 303 ? 0.5304 0.5713 0.5403 -0.0366 0.0300  0.0264  289 ASP B CG  
6298 O OD1 . ASP B 303 ? 0.5687 0.6015 0.5838 -0.0383 0.0333  0.0160  289 ASP B OD1 
6299 O OD2 . ASP B 303 ? 0.5230 0.5717 0.5423 -0.0319 0.0246  0.0347  289 ASP B OD2 
6300 N N   . THR B 304 ? 0.4546 0.4905 0.4448 -0.0530 0.0352  -0.0008 290 THR B N   
6301 C CA  . THR B 304 ? 0.5442 0.5833 0.5308 -0.0604 0.0325  -0.0113 290 THR B CA  
6302 C C   . THR B 304 ? 0.6247 0.6554 0.6034 -0.0663 0.0404  -0.0244 290 THR B C   
6303 O O   . THR B 304 ? 0.5685 0.6050 0.5350 -0.0749 0.0397  -0.0325 290 THR B O   
6304 C CB  . THR B 304 ? 0.5969 0.6313 0.5998 -0.0579 0.0300  -0.0134 290 THR B CB  
6305 O OG1 . THR B 304 ? 0.5796 0.6242 0.5899 -0.0536 0.0234  -0.0033 290 THR B OG1 
6306 C CG2 . THR B 304 ? 0.6352 0.6694 0.6360 -0.0661 0.0286  -0.0245 290 THR B CG2 
6307 N N   . LEU B 305 ? 0.5658 0.5838 0.5527 -0.0621 0.0483  -0.0274 291 LEU B N   
6308 C CA  . LEU B 305 ? 0.5280 0.5378 0.5123 -0.0664 0.0569  -0.0405 291 LEU B CA  
6309 C C   . LEU B 305 ? 0.6070 0.6241 0.5710 -0.0730 0.0612  -0.0431 291 LEU B C   
6310 O O   . LEU B 305 ? 0.6517 0.6666 0.6088 -0.0799 0.0672  -0.0565 291 LEU B O   
6311 C CB  . LEU B 305 ? 0.4852 0.4829 0.4851 -0.0598 0.0636  -0.0414 291 LEU B CB  
6312 C CG  . LEU B 305 ? 0.6014 0.5889 0.6193 -0.0572 0.0632  -0.0468 291 LEU B CG  
6313 C CD1 . LEU B 305 ? 0.4932 0.4843 0.5153 -0.0570 0.0540  -0.0414 291 LEU B CD1 
6314 C CD2 . LEU B 305 ? 0.5439 0.5239 0.5770 -0.0503 0.0673  -0.0442 291 LEU B CD2 
6315 N N   . THR B 306 ? 0.5790 0.6044 0.5332 -0.0714 0.0585  -0.0305 292 THR B N   
6316 C CA  . THR B 306 ? 0.6348 0.6679 0.5678 -0.0781 0.0623  -0.0301 292 THR B CA  
6317 C C   . THR B 306 ? 0.6497 0.7000 0.5659 -0.0838 0.0525  -0.0230 292 THR B C   
6318 O O   . THR B 306 ? 0.6062 0.6656 0.5028 -0.0893 0.0533  -0.0183 292 THR B O   
6319 C CB  . THR B 306 ? 0.5583 0.5878 0.4918 -0.0729 0.0673  -0.0194 292 THR B CB  
6320 O OG1 . THR B 306 ? 0.5626 0.5931 0.5064 -0.0648 0.0598  -0.0044 292 THR B OG1 
6321 C CG2 . THR B 306 ? 0.5725 0.5886 0.5206 -0.0694 0.0777  -0.0281 292 THR B CG2 
6322 N N   . ALA B 307 ? 0.6177 0.6738 0.5410 -0.0833 0.0432  -0.0217 293 ALA B N   
6323 C CA  . ALA B 307 ? 0.7199 0.7949 0.6311 -0.0883 0.0325  -0.0147 293 ALA B CA  
6324 C C   . ALA B 307 ? 0.7333 0.8172 0.6373 -0.0842 0.0281  0.0042  293 ALA B C   
6325 O O   . ALA B 307 ? 0.7790 0.8769 0.6627 -0.0912 0.0244  0.0092  293 ALA B O   
6326 C CB  . ALA B 307 ? 0.7469 0.8304 0.6382 -0.1019 0.0337  -0.0283 293 ALA B CB  
6327 N N   . GLY B 308 ? 0.6504 0.7259 0.5713 -0.0731 0.0285  0.0150  294 GLY B N   
6328 C CA  . GLY B 308 ? 0.4748 0.5555 0.3938 -0.0677 0.0247  0.0338  294 GLY B CA  
6329 C C   . GLY B 308 ? 0.6256 0.6979 0.5348 -0.0683 0.0340  0.0373  294 GLY B C   
6330 O O   . GLY B 308 ? 0.6905 0.7706 0.5864 -0.0698 0.0313  0.0510  294 GLY B O   
6331 N N   . PHE B 309 ? 0.6560 0.7131 0.5723 -0.0674 0.0448  0.0258  295 PHE B N   
6332 C CA  . PHE B 309 ? 0.5728 0.6215 0.4828 -0.0683 0.0553  0.0271  295 PHE B CA  
6333 C C   . PHE B 309 ? 0.6836 0.7428 0.5661 -0.0794 0.0577  0.0262  295 PHE B C   
6334 O O   . PHE B 309 ? 0.6938 0.7531 0.5654 -0.0809 0.0617  0.0365  295 PHE B O   
6335 C CB  . PHE B 309 ? 0.5391 0.5816 0.4598 -0.0596 0.0550  0.0438  295 PHE B CB  
6336 C CG  . PHE B 309 ? 0.5075 0.5410 0.4536 -0.0500 0.0533  0.0438  295 PHE B CG  
6337 C CD1 . PHE B 309 ? 0.5317 0.5538 0.4913 -0.0482 0.0602  0.0313  295 PHE B CD1 
6338 C CD2 . PHE B 309 ? 0.6311 0.6691 0.5880 -0.0431 0.0449  0.0563  295 PHE B CD2 
6339 C CE1 . PHE B 309 ? 0.5405 0.5561 0.5207 -0.0409 0.0585  0.0313  295 PHE B CE1 
6340 C CE2 . PHE B 309 ? 0.4593 0.4901 0.4382 -0.0355 0.0445  0.0547  295 PHE B CE2 
6341 C CZ  . PHE B 309 ? 0.5183 0.5382 0.5073 -0.0350 0.0511  0.0423  295 PHE B CZ  
6342 N N   . THR B 310 ? 0.6297 0.6977 0.5003 -0.0882 0.0558  0.0134  296 THR B N   
6343 C CA  . THR B 310 ? 0.6985 0.7781 0.5412 -0.1008 0.0587  0.0092  296 THR B CA  
6344 C C   . THR B 310 ? 0.7388 0.8099 0.5779 -0.1070 0.0734  -0.0105 296 THR B C   
6345 O O   . THR B 310 ? 0.6748 0.7550 0.4914 -0.1189 0.0778  -0.0197 296 THR B O   
6346 C CB  . THR B 310 ? 0.6317 0.7285 0.4620 -0.1086 0.0479  0.0062  296 THR B CB  
6347 O OG1 . THR B 310 ? 0.6887 0.7793 0.5313 -0.1097 0.0495  -0.0120 296 THR B OG1 
6348 C CG2 . THR B 310 ? 0.6091 0.7165 0.4463 -0.1017 0.0333  0.0261  296 THR B CG2 
6349 N N   . HIS B 311 ? 0.6241 0.6791 0.4854 -0.0993 0.0812  -0.0174 297 HIS B N   
6350 C CA  . HIS B 311 ? 0.6834 0.7305 0.5461 -0.1033 0.0956  -0.0345 297 HIS B CA  
6351 C C   . HIS B 311 ? 0.7846 0.8347 0.6311 -0.1083 0.1047  -0.0289 297 HIS B C   
6352 O O   . HIS B 311 ? 0.8062 0.8561 0.6516 -0.1040 0.1017  -0.0108 297 HIS B O   
6353 C CB  . HIS B 311 ? 0.5510 0.5825 0.4433 -0.0931 0.0998  -0.0399 297 HIS B CB  
6354 C CG  . HIS B 311 ? 0.6979 0.7231 0.6032 -0.0837 0.0986  -0.0245 297 HIS B CG  
6355 N ND1 . HIS B 311 ? 0.6537 0.6821 0.5609 -0.0782 0.0876  -0.0076 297 HIS B ND1 
6356 C CD2 . HIS B 311 ? 0.6116 0.6279 0.5302 -0.0793 0.1073  -0.0244 297 HIS B CD2 
6357 C CE1 . HIS B 311 ? 0.5859 0.6060 0.5063 -0.0711 0.0903  0.0015  297 HIS B CE1 
6358 N NE2 . HIS B 311 ? 0.6139 0.6270 0.5408 -0.0721 0.1018  -0.0083 297 HIS B NE2 
6359 N N   . GLN B 312 ? 0.8155 0.8678 0.6498 -0.1178 0.1166  -0.0450 298 GLN B N   
6360 C CA  . GLN B 312 ? 0.8127 0.8690 0.6298 -0.1247 0.1273  -0.0421 298 GLN B CA  
6361 C C   . GLN B 312 ? 0.7626 0.8082 0.5979 -0.1226 0.1429  -0.0576 298 GLN B C   
6362 O O   . GLN B 312 ? 0.7849 0.8323 0.6154 -0.1302 0.1538  -0.0771 298 GLN B O   
6363 C CB  . GLN B 312 ? 0.8284 0.9007 0.6120 -0.1400 0.1284  -0.0473 298 GLN B CB  
6364 C CG  . GLN B 312 ? 0.9094 0.9946 0.6697 -0.1436 0.1179  -0.0241 298 GLN B CG  
6365 C CD  . GLN B 312 ? 1.0357 1.1399 0.7639 -0.1584 0.1137  -0.0286 298 GLN B CD  
6366 O OE1 . GLN B 312 ? 0.9816 1.0910 0.7102 -0.1612 0.1069  -0.0391 298 GLN B OE1 
6367 N NE2 . GLN B 312 ? 1.1443 1.2597 0.8439 -0.1692 0.1178  -0.0207 298 GLN B NE2 
6368 N N   . LEU B 313 ? 0.7131 0.7484 0.5704 -0.1124 0.1441  -0.0491 299 LEU B N   
6369 C CA  . LEU B 313 ? 0.7009 0.7281 0.5782 -0.1094 0.1576  -0.0607 299 LEU B CA  
6370 C C   . LEU B 313 ? 0.6923 0.7163 0.5736 -0.1062 0.1608  -0.0456 299 LEU B C   
6371 O O   . LEU B 313 ? 0.8045 0.8226 0.6981 -0.0975 0.1518  -0.0314 299 LEU B O   
6372 C CB  . LEU B 313 ? 0.6471 0.6641 0.5552 -0.0994 0.1546  -0.0696 299 LEU B CB  
6373 C CG  . LEU B 313 ? 0.7474 0.7640 0.6571 -0.1022 0.1540  -0.0867 299 LEU B CG  
6374 C CD1 . LEU B 313 ? 0.6186 0.6246 0.5572 -0.0916 0.1474  -0.0884 299 LEU B CD1 
6375 C CD2 . LEU B 313 ? 0.6045 0.6229 0.5117 -0.1099 0.1702  -0.1069 299 LEU B CD2 
6376 N N   . THR B 314 ? 0.7183 0.7460 0.5899 -0.1137 0.1745  -0.0494 300 THR B N   
6377 C CA  . THR B 314 ? 0.6885 0.7132 0.5616 -0.1131 0.1795  -0.0357 300 THR B CA  
6378 C C   . THR B 314 ? 0.7490 0.7659 0.6536 -0.1062 0.1878  -0.0439 300 THR B C   
6379 O O   . THR B 314 ? 0.6598 0.6757 0.5815 -0.1039 0.1929  -0.0615 300 THR B O   
6380 C CB  . THR B 314 ? 0.7486 0.7828 0.5933 -0.1264 0.1902  -0.0345 300 THR B CB  
6381 O OG1 . THR B 314 ? 0.7096 0.7468 0.5601 -0.1318 0.2065  -0.0558 300 THR B OG1 
6382 C CG2 . THR B 314 ? 0.7653 0.8106 0.5781 -0.1348 0.1820  -0.0301 300 THR B CG2 
6383 N N   . PRO B 315 ? 0.7703 0.7816 0.6847 -0.1027 0.1887  -0.0310 301 PRO B N   
6384 C CA  . PRO B 315 ? 0.6420 0.6487 0.5857 -0.0977 0.1966  -0.0389 301 PRO B CA  
6385 C C   . PRO B 315 ? 0.7128 0.7261 0.6594 -0.1045 0.2134  -0.0557 301 PRO B C   
6386 O O   . PRO B 315 ? 0.6678 0.6804 0.6410 -0.0993 0.2180  -0.0692 301 PRO B O   
6387 C CB  . PRO B 315 ? 0.6451 0.6458 0.5915 -0.0964 0.1959  -0.0213 301 PRO B CB  
6388 C CG  . PRO B 315 ? 0.7238 0.7222 0.6535 -0.0945 0.1824  -0.0042 301 PRO B CG  
6389 C CD  . PRO B 315 ? 0.7765 0.7844 0.6800 -0.1016 0.1806  -0.0085 301 PRO B CD  
6390 N N   . SER B 316 ? 0.6102 0.6309 0.5305 -0.1160 0.2229  -0.0552 302 SER B N   
6391 C CA  . SER B 316 ? 0.6974 0.7256 0.6200 -0.1233 0.2407  -0.0726 302 SER B CA  
6392 C C   . SER B 316 ? 0.7770 0.8082 0.7053 -0.1229 0.2433  -0.0937 302 SER B C   
6393 O O   . SER B 316 ? 0.6927 0.7273 0.6385 -0.1235 0.2567  -0.1114 302 SER B O   
6394 C CB  . SER B 316 ? 0.7501 0.7864 0.6395 -0.1373 0.2502  -0.0666 302 SER B CB  
6395 O OG  . SER B 316 ? 0.9332 0.9649 0.8093 -0.1377 0.2423  -0.0425 302 SER B OG  
6396 N N   . GLN B 317 ? 0.6982 0.7281 0.6134 -0.1218 0.2311  -0.0924 303 GLN B N   
6397 C CA  . GLN B 317 ? 0.6288 0.6593 0.5484 -0.1221 0.2326  -0.1118 303 GLN B CA  
6398 C C   . GLN B 317 ? 0.7234 0.7450 0.6799 -0.1092 0.2277  -0.1186 303 GLN B C   
6399 O O   . GLN B 317 ? 0.6186 0.6388 0.5868 -0.1083 0.2322  -0.1363 303 GLN B O   
6400 C CB  . GLN B 317 ? 0.7791 0.8125 0.6710 -0.1269 0.2207  -0.1070 303 GLN B CB  
6401 C CG  . GLN B 317 ? 0.6673 0.7030 0.5549 -0.1320 0.2246  -0.1280 303 GLN B CG  
6402 C CD  . GLN B 317 ? 0.7139 0.7527 0.5790 -0.1356 0.2101  -0.1220 303 GLN B CD  
6403 O OE1 . GLN B 317 ? 0.6771 0.7139 0.5398 -0.1300 0.1953  -0.1030 303 GLN B OE1 
6404 N NE2 . GLN B 317 ? 0.5976 0.6420 0.4473 -0.1454 0.2149  -0.1392 303 GLN B NE2 
6405 N N   . THR B 318 ? 0.6199 0.6354 0.5949 -0.0997 0.2189  -0.1052 304 THR B N   
6406 C CA  . THR B 318 ? 0.5861 0.5941 0.5898 -0.0883 0.2097  -0.1072 304 THR B CA  
6407 C C   . THR B 318 ? 0.5719 0.5790 0.6076 -0.0813 0.2141  -0.1080 304 THR B C   
6408 O O   . THR B 318 ? 0.6493 0.6590 0.6849 -0.0834 0.2191  -0.1002 304 THR B O   
6409 C CB  . THR B 318 ? 0.5915 0.5943 0.5884 -0.0833 0.1921  -0.0910 304 THR B CB  
6410 O OG1 . THR B 318 ? 0.5106 0.5139 0.4960 -0.0847 0.1897  -0.0739 304 THR B OG1 
6411 C CG2 . THR B 318 ? 0.5921 0.5965 0.5658 -0.0883 0.1854  -0.0931 304 THR B CG2 
6412 N N   . ILE B 319 ? 0.6034 0.6069 0.6670 -0.0733 0.2120  -0.1171 305 ILE B N   
6413 C CA  . ILE B 319 ? 0.4613 0.4644 0.5575 -0.0647 0.2100  -0.1149 305 ILE B CA  
6414 C C   . ILE B 319 ? 0.5406 0.5365 0.6465 -0.0565 0.1937  -0.1077 305 ILE B C   
6415 O O   . ILE B 319 ? 0.4799 0.4710 0.5858 -0.0549 0.1898  -0.1141 305 ILE B O   
6416 C CB  . ILE B 319 ? 0.4786 0.4864 0.6027 -0.0624 0.2225  -0.1315 305 ILE B CB  
6417 C CG1 . ILE B 319 ? 0.4945 0.5112 0.6096 -0.0714 0.2401  -0.1390 305 ILE B CG1 
6418 C CG2 . ILE B 319 ? 0.4905 0.4996 0.6498 -0.0529 0.2172  -0.1280 305 ILE B CG2 
6419 C CD1 . ILE B 319 ? 0.5228 0.5457 0.6674 -0.0692 0.2543  -0.1565 305 ILE B CD1 
6420 N N   . GLU B 320 ? 0.4777 0.4724 0.5905 -0.0524 0.1850  -0.0949 306 GLU B N   
6421 C CA  . GLU B 320 ? 0.3729 0.3618 0.4887 -0.0466 0.1697  -0.0863 306 GLU B CA  
6422 C C   . GLU B 320 ? 0.4154 0.4058 0.5611 -0.0395 0.1650  -0.0845 306 GLU B C   
6423 O O   . GLU B 320 ? 0.4613 0.4570 0.6183 -0.0399 0.1696  -0.0827 306 GLU B O   
6424 C CB  . GLU B 320 ? 0.4059 0.3926 0.4991 -0.0491 0.1626  -0.0721 306 GLU B CB  
6425 C CG  . GLU B 320 ? 0.5548 0.5382 0.6571 -0.0435 0.1503  -0.0619 306 GLU B CG  
6426 C CD  . GLU B 320 ? 0.6127 0.5934 0.6945 -0.0454 0.1443  -0.0492 306 GLU B CD  
6427 O OE1 . GLU B 320 ? 0.5071 0.4889 0.5739 -0.0504 0.1507  -0.0446 306 GLU B OE1 
6428 O OE2 . GLU B 320 ? 0.5235 0.5012 0.6051 -0.0418 0.1335  -0.0434 306 GLU B OE2 
6429 N N   . VAL B 321 ? 0.3454 0.3318 0.5036 -0.0337 0.1556  -0.0848 307 VAL B N   
6430 C CA  . VAL B 321 ? 0.4446 0.4336 0.6300 -0.0273 0.1491  -0.0820 307 VAL B CA  
6431 C C   . VAL B 321 ? 0.4376 0.4225 0.6169 -0.0251 0.1348  -0.0712 307 VAL B C   
6432 O O   . VAL B 321 ? 0.3421 0.3208 0.5121 -0.0246 0.1287  -0.0706 307 VAL B O   
6433 C CB  . VAL B 321 ? 0.3525 0.3411 0.5625 -0.0221 0.1514  -0.0915 307 VAL B CB  
6434 C CG1 . VAL B 321 ? 0.3434 0.3354 0.5795 -0.0154 0.1414  -0.0854 307 VAL B CG1 
6435 C CG2 . VAL B 321 ? 0.3999 0.3945 0.6202 -0.0240 0.1670  -0.1035 307 VAL B CG2 
6436 N N   . GLN B 322 ? 0.3907 0.3796 0.5764 -0.0245 0.1301  -0.0637 308 GLN B N   
6437 C CA  . GLN B 322 ? 0.4078 0.3945 0.5885 -0.0233 0.1181  -0.0545 308 GLN B CA  
6438 C C   . GLN B 322 ? 0.3556 0.3485 0.5600 -0.0196 0.1113  -0.0524 308 GLN B C   
6439 O O   . GLN B 322 ? 0.3953 0.3948 0.6203 -0.0178 0.1160  -0.0571 308 GLN B O   
6440 C CB  . GLN B 322 ? 0.3405 0.3260 0.5044 -0.0271 0.1191  -0.0478 308 GLN B CB  
6441 C CG  . GLN B 322 ? 0.3763 0.3570 0.5156 -0.0305 0.1229  -0.0468 308 GLN B CG  
6442 C CD  . GLN B 322 ? 0.5469 0.5233 0.6747 -0.0295 0.1146  -0.0451 308 GLN B CD  
6443 O OE1 . GLN B 322 ? 0.4209 0.3965 0.5559 -0.0266 0.1056  -0.0423 308 GLN B OE1 
6444 N NE2 . GLN B 322 ? 0.3573 0.3321 0.4663 -0.0328 0.1177  -0.0467 308 GLN B NE2 
6445 N N   . PRO B 323 ? 0.3719 0.3644 0.5750 -0.0188 0.1003  -0.0454 309 PRO B N   
6446 C CA  . PRO B 323 ? 0.4327 0.4323 0.6569 -0.0159 0.0924  -0.0427 309 PRO B CA  
6447 C C   . PRO B 323 ? 0.5226 0.5333 0.7641 -0.0169 0.0956  -0.0441 309 PRO B C   
6448 O O   . PRO B 323 ? 0.5941 0.6128 0.8588 -0.0134 0.0930  -0.0449 309 PRO B O   
6449 C CB  . PRO B 323 ? 0.4900 0.4880 0.7028 -0.0174 0.0820  -0.0352 309 PRO B CB  
6450 C CG  . PRO B 323 ? 0.4037 0.3922 0.5961 -0.0183 0.0829  -0.0352 309 PRO B CG  
6451 C CD  . PRO B 323 ? 0.4138 0.4002 0.5971 -0.0202 0.0940  -0.0399 309 PRO B CD  
6452 N N   . HIS B 324 ? 0.4571 0.4690 0.6900 -0.0216 0.1010  -0.0441 310 HIS B N   
6453 C CA  . HIS B 324 ? 0.3952 0.4180 0.6444 -0.0240 0.1042  -0.0459 310 HIS B CA  
6454 C C   . HIS B 324 ? 0.3888 0.4114 0.6362 -0.0272 0.1179  -0.0511 310 HIS B C   
6455 O O   . HIS B 324 ? 0.3839 0.4150 0.6437 -0.0306 0.1222  -0.0531 310 HIS B O   
6456 C CB  . HIS B 324 ? 0.3928 0.4182 0.6368 -0.0285 0.0984  -0.0416 310 HIS B CB  
6457 C CG  . HIS B 324 ? 0.4564 0.4845 0.7011 -0.0272 0.0855  -0.0365 310 HIS B CG  
6458 N ND1 . HIS B 324 ? 0.4752 0.5147 0.7395 -0.0251 0.0775  -0.0348 310 HIS B ND1 
6459 C CD2 . HIS B 324 ? 0.4376 0.4594 0.6659 -0.0282 0.0794  -0.0322 310 HIS B CD2 
6460 C CE1 . HIS B 324 ? 0.7039 0.7435 0.9617 -0.0255 0.0669  -0.0291 310 HIS B CE1 
6461 N NE2 . HIS B 324 ? 0.5658 0.5948 0.8019 -0.0275 0.0684  -0.0283 310 HIS B NE2 
6462 N N   . ALA B 325 ? 0.3479 0.3619 0.5796 -0.0273 0.1249  -0.0534 311 ALA B N   
6463 C CA  . ALA B 325 ? 0.3699 0.3837 0.5957 -0.0316 0.1381  -0.0571 311 ALA B CA  
6464 C C   . ALA B 325 ? 0.4005 0.4091 0.6147 -0.0310 0.1446  -0.0621 311 ALA B C   
6465 O O   . ALA B 325 ? 0.4115 0.4133 0.6146 -0.0286 0.1387  -0.0608 311 ALA B O   
6466 C CB  . ALA B 325 ? 0.2953 0.3028 0.5031 -0.0368 0.1401  -0.0509 311 ALA B CB  
6467 N N   . SER B 326 ? 0.3561 0.3685 0.5724 -0.0343 0.1575  -0.0685 312 SER B N   
6468 C CA  . SER B 326 ? 0.4097 0.4188 0.6134 -0.0358 0.1660  -0.0752 312 SER B CA  
6469 C C   . SER B 326 ? 0.3397 0.3489 0.5260 -0.0434 0.1778  -0.0746 312 SER B C   
6470 O O   . SER B 326 ? 0.4297 0.4430 0.6226 -0.0469 0.1823  -0.0720 312 SER B O   
6471 C CB  . SER B 326 ? 0.3804 0.3957 0.6083 -0.0317 0.1715  -0.0864 312 SER B CB  
6472 O OG  . SER B 326 ? 0.3630 0.3747 0.6015 -0.0250 0.1606  -0.0855 312 SER B OG  
6473 N N   . ARG B 327 ? 0.5156 0.5205 0.6790 -0.0470 0.1827  -0.0767 313 ARG B N   
6474 C CA  . ARG B 327 ? 0.4807 0.4853 0.6224 -0.0550 0.1926  -0.0737 313 ARG B CA  
6475 C C   . ARG B 327 ? 0.5320 0.5411 0.6672 -0.0595 0.2053  -0.0856 313 ARG B C   
6476 O O   . ARG B 327 ? 0.5077 0.5149 0.6401 -0.0575 0.2037  -0.0931 313 ARG B O   
6477 C CB  . ARG B 327 ? 0.4073 0.4035 0.5214 -0.0567 0.1846  -0.0616 313 ARG B CB  
6478 C CG  . ARG B 327 ? 0.4258 0.4216 0.5142 -0.0650 0.1932  -0.0565 313 ARG B CG  
6479 C CD  . ARG B 327 ? 0.4257 0.4149 0.4902 -0.0651 0.1836  -0.0440 313 ARG B CD  
6480 N NE  . ARG B 327 ? 0.4684 0.4573 0.5244 -0.0628 0.1762  -0.0484 313 ARG B NE  
6481 C CZ  . ARG B 327 ? 0.5372 0.5297 0.5750 -0.0681 0.1810  -0.0547 313 ARG B CZ  
6482 N NH1 . ARG B 327 ? 0.4412 0.4385 0.4659 -0.0762 0.1932  -0.0572 313 ARG B NH1 
6483 N NH2 . ARG B 327 ? 0.5388 0.5304 0.5708 -0.0664 0.1737  -0.0591 313 ARG B NH2 
6484 N N   . VAL B 328 ? 0.4829 0.4978 0.6156 -0.0664 0.2188  -0.0879 314 VAL B N   
6485 C CA  . VAL B 328 ? 0.5400 0.5598 0.6601 -0.0734 0.2329  -0.0985 314 VAL B CA  
6486 C C   . VAL B 328 ? 0.5616 0.5800 0.6511 -0.0830 0.2378  -0.0881 314 VAL B C   
6487 O O   . VAL B 328 ? 0.4876 0.5073 0.5807 -0.0867 0.2430  -0.0814 314 VAL B O   
6488 C CB  . VAL B 328 ? 0.4357 0.4662 0.5836 -0.0735 0.2465  -0.1121 314 VAL B CB  
6489 C CG1 . VAL B 328 ? 0.4485 0.4848 0.5816 -0.0821 0.2629  -0.1243 314 VAL B CG1 
6490 C CG2 . VAL B 328 ? 0.4075 0.4393 0.5879 -0.0630 0.2401  -0.1200 314 VAL B CG2 
6491 N N   . GLY B 329 ? 0.5186 0.5346 0.5783 -0.0875 0.2360  -0.0859 315 GLY B N   
6492 C CA  . GLY B 329 ? 0.4746 0.4896 0.5041 -0.0962 0.2386  -0.0732 315 GLY B CA  
6493 C C   . GLY B 329 ? 0.5824 0.5888 0.6115 -0.0924 0.2275  -0.0550 315 GLY B C   
6494 O O   . GLY B 329 ? 0.5941 0.5944 0.6257 -0.0851 0.2135  -0.0494 315 GLY B O   
6495 N N   . ASP B 330 ? 0.5984 0.6037 0.6249 -0.0979 0.2346  -0.0460 316 ASP B N   
6496 C CA  . ASP B 330 ? 0.5852 0.5807 0.6127 -0.0952 0.2266  -0.0295 316 ASP B CA  
6497 C C   . ASP B 330 ? 0.5852 0.5795 0.6442 -0.0904 0.2259  -0.0325 316 ASP B C   
6498 O O   . ASP B 330 ? 0.6754 0.6612 0.7382 -0.0884 0.2203  -0.0214 316 ASP B O   
6499 C CB  . ASP B 330 ? 0.5840 0.5769 0.5898 -0.1046 0.2342  -0.0159 316 ASP B CB  
6500 C CG  . ASP B 330 ? 0.9183 0.9110 0.8910 -0.1082 0.2289  -0.0058 316 ASP B CG  
6501 O OD1 . ASP B 330 ? 0.8776 0.8667 0.8465 -0.1014 0.2151  -0.0010 316 ASP B OD1 
6502 O OD2 . ASP B 330 ? 0.8628 0.8603 0.8132 -0.1184 0.2384  -0.0025 316 ASP B OD2 
6503 N N   . VAL B 331 ? 0.4925 0.4955 0.5749 -0.0884 0.2313  -0.0474 317 VAL B N   
6504 C CA  . VAL B 331 ? 0.5040 0.5099 0.6168 -0.0855 0.2313  -0.0508 317 VAL B CA  
6505 C C   . VAL B 331 ? 0.5409 0.5471 0.6716 -0.0755 0.2183  -0.0555 317 VAL B C   
6506 O O   . VAL B 331 ? 0.4691 0.4788 0.6020 -0.0716 0.2165  -0.0644 317 VAL B O   
6507 C CB  . VAL B 331 ? 0.5927 0.6107 0.7225 -0.0906 0.2465  -0.0627 317 VAL B CB  
6508 C CG1 . VAL B 331 ? 0.5080 0.5313 0.6697 -0.0884 0.2454  -0.0654 317 VAL B CG1 
6509 C CG2 . VAL B 331 ? 0.5479 0.5661 0.6568 -0.1019 0.2603  -0.0577 317 VAL B CG2 
6510 N N   . TRP B 332 ? 0.4324 0.4346 0.5754 -0.0721 0.2096  -0.0496 318 TRP B N   
6511 C CA  . TRP B 332 ? 0.4293 0.4328 0.5889 -0.0639 0.1970  -0.0525 318 TRP B CA  
6512 C C   . TRP B 332 ? 0.4916 0.5064 0.6825 -0.0628 0.1990  -0.0604 318 TRP B C   
6513 O O   . TRP B 332 ? 0.3972 0.4158 0.5975 -0.0683 0.2064  -0.0603 318 TRP B O   
6514 C CB  . TRP B 332 ? 0.4445 0.4381 0.5968 -0.0614 0.1859  -0.0418 318 TRP B CB  
6515 C CG  . TRP B 332 ? 0.5079 0.4942 0.6379 -0.0585 0.1783  -0.0359 318 TRP B CG  
6516 C CD1 . TRP B 332 ? 0.4899 0.4690 0.5961 -0.0616 0.1795  -0.0261 318 TRP B CD1 
6517 C CD2 . TRP B 332 ? 0.4239 0.4104 0.5542 -0.0524 0.1681  -0.0389 318 TRP B CD2 
6518 N NE1 . TRP B 332 ? 0.5208 0.4972 0.6133 -0.0577 0.1703  -0.0234 318 TRP B NE1 
6519 C CE2 . TRP B 332 ? 0.5973 0.5776 0.7039 -0.0525 0.1637  -0.0316 318 TRP B CE2 
6520 C CE3 . TRP B 332 ? 0.4328 0.4243 0.5817 -0.0471 0.1619  -0.0460 318 TRP B CE3 
6521 C CZ2 . TRP B 332 ? 0.5427 0.5220 0.6439 -0.0481 0.1542  -0.0327 318 TRP B CZ2 
6522 C CZ3 . TRP B 332 ? 0.3703 0.3589 0.5131 -0.0427 0.1527  -0.0461 318 TRP B CZ3 
6523 C CH2 . TRP B 332 ? 0.5069 0.4896 0.6260 -0.0436 0.1493  -0.0402 318 TRP B CH2 
6524 N N   . PHE B 333 ? 0.4416 0.4622 0.6494 -0.0559 0.1919  -0.0667 319 PHE B N   
6525 C CA  . PHE B 333 ? 0.4274 0.4608 0.6671 -0.0534 0.1911  -0.0730 319 PHE B CA  
6526 C C   . PHE B 333 ? 0.4455 0.4784 0.6938 -0.0475 0.1752  -0.0688 319 PHE B C   
6527 O O   . PHE B 333 ? 0.4593 0.4904 0.7087 -0.0412 0.1677  -0.0699 319 PHE B O   
6528 C CB  . PHE B 333 ? 0.3630 0.4053 0.6183 -0.0505 0.1988  -0.0842 319 PHE B CB  
6529 C CG  . PHE B 333 ? 0.4055 0.4497 0.6505 -0.0576 0.2156  -0.0896 319 PHE B CG  
6530 C CD1 . PHE B 333 ? 0.3879 0.4237 0.6044 -0.0604 0.2200  -0.0895 319 PHE B CD1 
6531 C CD2 . PHE B 333 ? 0.3552 0.4112 0.6182 -0.0626 0.2270  -0.0947 319 PHE B CD2 
6532 C CE1 . PHE B 333 ? 0.3843 0.4231 0.5886 -0.0683 0.2355  -0.0941 319 PHE B CE1 
6533 C CE2 . PHE B 333 ? 0.3735 0.4320 0.6257 -0.0703 0.2433  -0.0995 319 PHE B CE2 
6534 C CZ  . PHE B 333 ? 0.4481 0.4979 0.6700 -0.0733 0.2477  -0.0991 319 PHE B CZ  
6535 N N   . THR B 334 ? 0.4590 0.4934 0.7126 -0.0504 0.1706  -0.0645 320 THR B N   
6536 C CA  . THR B 334 ? 0.5330 0.5670 0.7899 -0.0470 0.1563  -0.0601 320 THR B CA  
6537 C C   . THR B 334 ? 0.4547 0.5049 0.7410 -0.0448 0.1504  -0.0639 320 THR B C   
6538 O O   . THR B 334 ? 0.4084 0.4705 0.7143 -0.0471 0.1577  -0.0692 320 THR B O   
6539 C CB  . THR B 334 ? 0.4108 0.4365 0.6549 -0.0520 0.1547  -0.0540 320 THR B CB  
6540 O OG1 . THR B 334 ? 0.4220 0.4556 0.6812 -0.0584 0.1603  -0.0568 320 THR B OG1 
6541 C CG2 . THR B 334 ? 0.3663 0.3778 0.5847 -0.0540 0.1611  -0.0487 320 THR B CG2 
6542 N N   . GLY B 335 ? 0.4415 0.4931 0.7310 -0.0407 0.1369  -0.0603 321 GLY B N   
6543 C CA  . GLY B 335 ? 0.4101 0.4778 0.7262 -0.0381 0.1288  -0.0613 321 GLY B CA  
6544 C C   . GLY B 335 ? 0.5785 0.6517 0.9127 -0.0305 0.1287  -0.0646 321 GLY B C   
6545 O O   . GLY B 335 ? 0.4356 0.5247 0.7979 -0.0282 0.1259  -0.0664 321 GLY B O   
6546 N N   . ILE B 336 ? 0.5040 0.5648 0.8246 -0.0265 0.1318  -0.0656 322 ILE B N   
6547 C CA  . ILE B 336 ? 0.4118 0.4743 0.7491 -0.0193 0.1333  -0.0701 322 ILE B CA  
6548 C C   . ILE B 336 ? 0.4701 0.5230 0.7991 -0.0142 0.1218  -0.0646 322 ILE B C   
6549 O O   . ILE B 336 ? 0.3524 0.3917 0.6551 -0.0158 0.1217  -0.0628 322 ILE B O   
6550 C CB  . ILE B 336 ? 0.3449 0.4020 0.6745 -0.0207 0.1490  -0.0787 322 ILE B CB  
6551 C CG1 . ILE B 336 ? 0.3675 0.4367 0.7109 -0.0256 0.1609  -0.0844 322 ILE B CG1 
6552 C CG2 . ILE B 336 ? 0.4428 0.4976 0.7863 -0.0133 0.1507  -0.0846 322 ILE B CG2 
6553 C CD1 . ILE B 336 ? 0.5014 0.5642 0.8255 -0.0314 0.1764  -0.0897 322 ILE B CD1 
6554 N N   . PRO B 337 ? 0.3762 0.4360 0.7272 -0.0083 0.1117  -0.0610 323 PRO B N   
6555 C CA  . PRO B 337 ? 0.5001 0.5497 0.8440 -0.0039 0.1017  -0.0555 323 PRO B CA  
6556 C C   . PRO B 337 ? 0.4781 0.5140 0.8132 -0.0014 0.1101  -0.0622 323 PRO B C   
6557 O O   . PRO B 337 ? 0.4359 0.4736 0.7829 0.0002  0.1219  -0.0714 323 PRO B O   
6558 C CB  . PRO B 337 ? 0.5187 0.5801 0.8935 0.0022  0.0915  -0.0504 323 PRO B CB  
6559 C CG  . PRO B 337 ? 0.5096 0.5892 0.8995 -0.0015 0.0913  -0.0505 323 PRO B CG  
6560 C CD  . PRO B 337 ? 0.4605 0.5389 0.8434 -0.0061 0.1073  -0.0601 323 PRO B CD  
6561 N N   . MET B 338 ? 0.4395 0.4846 1.0472 -0.0492 0.1675  -0.1017 324 MET B N   
6562 C CA  . MET B 338 ? 0.3730 0.3923 0.9509 -0.0425 0.1660  -0.0952 324 MET B CA  
6563 C C   . MET B 338 ? 0.4736 0.4860 1.0498 -0.0330 0.1592  -0.0970 324 MET B C   
6564 O O   . MET B 338 ? 0.3597 0.3589 0.9246 -0.0266 0.1671  -0.0996 324 MET B O   
6565 C CB  . MET B 338 ? 0.3593 0.3686 0.9152 -0.0492 0.1549  -0.0895 324 MET B CB  
6566 C CG  . MET B 338 ? 0.5673 0.5538 1.0916 -0.0444 0.1479  -0.0843 324 MET B CG  
6567 S SD  . MET B 338 ? 0.5786 0.5571 1.0823 -0.0537 0.1344  -0.0784 324 MET B SD  
6568 C CE  . MET B 338 ? 0.4917 0.4551 0.9761 -0.0537 0.1454  -0.0699 324 MET B CE  
6569 N N   . LEU B 339 ? 0.5297 0.5549 1.1222 -0.0334 0.1451  -0.0956 325 LEU B N   
6570 C CA  . LEU B 339 ? 0.4314 0.4513 1.0376 -0.0239 0.1387  -0.0953 325 LEU B CA  
6571 C C   . LEU B 339 ? 0.4705 0.4939 1.0984 -0.0162 0.1548  -0.1048 325 LEU B C   
6572 O O   . LEU B 339 ? 0.5535 0.5637 1.1848 -0.0082 0.1605  -0.1116 325 LEU B O   
6573 C CB  . LEU B 339 ? 0.5737 0.6134 1.1999 -0.0278 0.1189  -0.0854 325 LEU B CB  
6574 C CG  . LEU B 339 ? 0.4281 0.4702 1.0882 -0.0185 0.1117  -0.0811 325 LEU B CG  
6575 C CD1 . LEU B 339 ? 0.5374 0.5506 1.1935 -0.0096 0.1110  -0.0833 325 LEU B CD1 
6576 C CD2 . LEU B 339 ? 0.5385 0.6095 1.2187 -0.0261 0.0902  -0.0645 325 LEU B CD2 
6577 N N   . GLN B 340 ? 0.3741 0.4171 1.0198 -0.0195 0.1635  -0.1080 326 GLN B N   
6578 C CA  . GLN B 340 ? 0.3532 0.4010 1.0203 -0.0128 0.1792  -0.1171 326 GLN B CA  
6579 C C   . GLN B 340 ? 0.3687 0.4022 1.0149 -0.0109 0.1972  -0.1226 326 GLN B C   
6580 O O   . GLN B 340 ? 0.3776 0.4088 1.0327 -0.0049 0.2082  -0.1322 326 GLN B O   
6581 C CB  . GLN B 340 ? 0.3489 0.4219 1.0395 -0.0181 0.1853  -0.1198 326 GLN B CB  
6582 C CG  . GLN B 340 ? 0.3680 0.4642 1.0908 -0.0175 0.1736  -0.1179 326 GLN B CG  
6583 C CD  . GLN B 340 ? 0.4638 0.5797 1.1989 -0.0224 0.1808  -0.1239 326 GLN B CD  
6584 O OE1 . GLN B 340 ? 0.5083 0.6202 1.2222 -0.0294 0.1868  -0.1271 326 GLN B OE1 
6585 N NE2 . GLN B 340 ? 0.4144 0.5441 1.1742 -0.0184 0.1765  -0.1239 326 GLN B NE2 
6586 N N   . ALA B 341 ? 0.4296 0.4575 1.0510 -0.0177 0.2006  -0.1161 327 ALA B N   
6587 C CA  . ALA B 341 ? 0.3795 0.4004 0.9789 -0.0187 0.2148  -0.1157 327 ALA B CA  
6588 C C   . ALA B 341 ? 0.3946 0.4023 0.9746 -0.0152 0.2120  -0.1225 327 ALA B C   
6589 O O   . ALA B 341 ? 0.4629 0.4742 1.0400 -0.0142 0.2258  -0.1325 327 ALA B O   
6590 C CB  . ALA B 341 ? 0.3699 0.3886 0.9531 -0.0269 0.2155  -0.1026 327 ALA B CB  
6591 N N   . ILE B 342 ? 0.4498 0.4452 1.0203 -0.0145 0.1952  -0.1195 328 ILE B N   
6592 C CA  . ILE B 342 ? 0.4337 0.4160 0.9913 -0.0118 0.1930  -0.1281 328 ILE B CA  
6593 C C   . ILE B 342 ? 0.4211 0.4059 1.0114 -0.0042 0.1996  -0.1440 328 ILE B C   
6594 O O   . ILE B 342 ? 0.5147 0.4990 1.1007 -0.0044 0.2121  -0.1599 328 ILE B O   
6595 C CB  . ILE B 342 ? 0.4941 0.4631 1.0421 -0.0123 0.1729  -0.1199 328 ILE B CB  
6596 C CG1 . ILE B 342 ? 0.4288 0.3920 0.9407 -0.0202 0.1703  -0.1095 328 ILE B CG1 
6597 C CG2 . ILE B 342 ? 0.4214 0.3779 0.9778 -0.0071 0.1693  -0.1307 328 ILE B CG2 
6598 C CD1 . ILE B 342 ? 0.4318 0.3878 0.9375 -0.0231 0.1511  -0.0995 328 ILE B CD1 
6599 N N   . GLU B 343 ? 0.4096 0.4012 1.0364 0.0012  0.1920  -0.1411 329 GLU B N   
6600 C CA  . GLU B 343 ? 0.4532 0.4481 1.1210 0.0090  0.1982  -0.1544 329 GLU B CA  
6601 C C   . GLU B 343 ? 0.4332 0.4387 1.1010 0.0079  0.2218  -0.1697 329 GLU B C   
6602 O O   . GLU B 343 ? 0.4442 0.4502 1.1325 0.0110  0.2338  -0.1892 329 GLU B O   
6603 C CB  . GLU B 343 ? 0.4956 0.5024 1.2023 0.0130  0.1846  -0.1433 329 GLU B CB  
6604 C CG  . GLU B 343 ? 0.5044 0.5071 1.2213 0.0134  0.1608  -0.1275 329 GLU B CG  
6605 C CD  . GLU B 343 ? 0.5996 0.6250 1.3491 0.0128  0.1461  -0.1123 329 GLU B CD  
6606 O OE1 . GLU B 343 ? 0.5786 0.6211 1.3384 0.0118  0.1550  -0.1159 329 GLU B OE1 
6607 O OE2 . GLU B 343 ? 0.6887 0.7182 1.4539 0.0119  0.1255  -0.0957 329 GLU B OE2 
6608 N N   . THR B 344 ? 0.4196 0.4358 1.0701 0.0025  0.2297  -0.1618 330 THR B N   
6609 C CA  . THR B 344 ? 0.5280 0.5573 1.1753 -0.0007 0.2518  -0.1718 330 THR B CA  
6610 C C   . THR B 344 ? 0.4524 0.4826 1.0669 -0.0079 0.2629  -0.1814 330 THR B C   
6611 O O   . THR B 344 ? 0.4701 0.5104 1.0928 -0.0095 0.2791  -0.2015 330 THR B O   
6612 C CB  . THR B 344 ? 0.4165 0.4567 1.0573 -0.0057 0.2569  -0.1574 330 THR B CB  
6613 O OG1 . THR B 344 ? 0.4537 0.5009 1.1282 -0.0011 0.2509  -0.1550 330 THR B OG1 
6614 C CG2 . THR B 344 ? 0.4300 0.4856 1.0634 -0.0111 0.2789  -0.1621 330 THR B CG2 
6615 N N   . LEU B 345 ? 0.4528 0.4758 1.0313 -0.0139 0.2547  -0.1688 331 LEU B N   
6616 C CA  . LEU B 345 ? 0.4751 0.5047 1.0209 -0.0230 0.2638  -0.1773 331 LEU B CA  
6617 C C   . LEU B 345 ? 0.5588 0.5832 1.1215 -0.0200 0.2670  -0.2042 331 LEU B C   
6618 O O   . LEU B 345 ? 0.5504 0.5892 1.0958 -0.0292 0.2810  -0.2220 331 LEU B O   
6619 C CB  . LEU B 345 ? 0.4724 0.4943 0.9809 -0.0293 0.2519  -0.1586 331 LEU B CB  
6620 C CG  . LEU B 345 ? 0.5758 0.6084 1.0672 -0.0369 0.2542  -0.1333 331 LEU B CG  
6621 C CD1 . LEU B 345 ? 0.4775 0.5362 0.9696 -0.0439 0.2740  -0.1334 331 LEU B CD1 
6622 C CD2 . LEU B 345 ? 0.4870 0.5093 0.9986 -0.0318 0.2431  -0.1181 331 LEU B CD2 
6623 N N   . VAL B 346 ? 0.6720 0.6792 1.2707 -0.0089 0.2538  -0.2065 332 VAL B N   
6624 C CA  . VAL B 346 ? 0.7119 0.7115 1.3390 -0.0053 0.2560  -0.2301 332 VAL B CA  
6625 C C   . VAL B 346 ? 0.5120 0.5271 1.1725 -0.0055 0.2780  -0.2589 332 VAL B C   
6626 O O   . VAL B 346 ? 0.6130 0.6318 1.2839 -0.0099 0.2898  -0.2870 332 VAL B O   
6627 C CB  . VAL B 346 ? 0.5305 0.5103 1.1916 0.0053  0.2341  -0.2184 332 VAL B CB  
6628 C CG1 . VAL B 346 ? 0.5614 0.5344 1.2716 0.0106  0.2386  -0.2416 332 VAL B CG1 
6629 C CG2 . VAL B 346 ? 0.4777 0.4452 1.0991 0.0012  0.2186  -0.2018 332 VAL B CG2 
6630 N N   . GLU B 347 ? 0.6615 0.6865 1.3476 -0.0010 0.2847  -0.2568 333 GLU B N   
6631 C CA  . GLU B 347 ? 0.5342 0.5733 1.2336 -0.0079 0.3013  -0.2825 333 GLU B CA  
6632 C C   . GLU B 347 ? 0.6471 0.7138 1.3064 -0.0218 0.3256  -0.2961 333 GLU B C   
6633 O O   . GLU B 347 ? 0.7011 0.7819 1.3569 -0.0324 0.3398  -0.3246 333 GLU B O   
6634 C CB  . GLU B 347 ? 0.9649 1.0079 1.6943 -0.0050 0.3006  -0.2808 333 GLU B CB  
6635 C CG  . GLU B 347 ? 1.1668 1.2009 1.9364 0.0047  0.2828  -0.2631 333 GLU B CG  
6636 C CD  . GLU B 347 ? 1.1313 1.1804 1.8855 0.0013  0.2940  -0.2586 333 GLU B CD  
6637 O OE1 . GLU B 347 ? 1.1349 1.1848 1.8945 0.0049  0.2860  -0.2419 333 GLU B OE1 
6638 O OE2 . GLU B 347 ? 1.1528 1.2165 1.8885 -0.0078 0.3139  -0.2769 333 GLU B OE2 
6639 N N   . LEU B 348 ? 0.5319 0.6066 1.1515 -0.0269 0.3231  -0.2693 334 LEU B N   
6640 C CA  . LEU B 348 ? 0.5894 0.6943 1.1662 -0.0440 0.3389  -0.2687 334 LEU B CA  
6641 C C   . LEU B 348 ? 0.5796 0.6962 1.1276 -0.0570 0.3441  -0.2875 334 LEU B C   
6642 O O   . LEU B 348 ? 0.5986 0.7484 1.1336 -0.0726 0.3645  -0.3104 334 LEU B O   
6643 C CB  . LEU B 348 ? 0.5866 0.6921 1.1337 -0.0465 0.3294  -0.2302 334 LEU B CB  
6644 C CG  . LEU B 348 ? 0.5155 0.6181 1.0960 -0.0370 0.3309  -0.2212 334 LEU B CG  
6645 C CD1 . LEU B 348 ? 0.4961 0.5946 1.0651 -0.0370 0.3212  -0.1873 334 LEU B CD1 
6646 C CD2 . LEU B 348 ? 0.5301 0.6584 1.1261 -0.0424 0.3538  -0.2400 334 LEU B CD2 
6647 N N   . CYS B 349 ? 0.5674 0.6598 1.1093 -0.0518 0.3269  -0.2822 335 CYS B N   
6648 C CA  . CYS B 349 ? 0.5894 0.6907 1.1129 -0.0628 0.3319  -0.3051 335 CYS B CA  
6649 C C   . CYS B 349 ? 0.6275 0.7323 1.1994 -0.0618 0.3480  -0.3499 335 CYS B C   
6650 O O   . CYS B 349 ? 0.6324 0.7673 1.1932 -0.0784 0.3672  -0.3814 335 CYS B O   
6651 C CB  . CYS B 349 ? 0.5774 0.6500 1.0861 -0.0566 0.3092  -0.2873 335 CYS B CB  
6652 S SG  . CYS B 349 ? 0.6261 0.7013 1.0814 -0.0624 0.2951  -0.2415 335 CYS B SG  
6653 N N   . LYS B 350 ? 0.5917 0.6704 1.2223 -0.0441 0.3412  -0.3538 336 LYS B N   
6654 C CA  . LYS B 350 ? 0.6298 0.7073 1.3049 -0.0466 0.3459  -0.3834 336 LYS B CA  
6655 C C   . LYS B 350 ? 0.6348 0.7435 1.3058 -0.0601 0.3666  -0.4044 336 LYS B C   
6656 O O   . LYS B 350 ? 0.7351 0.8548 1.4300 -0.0706 0.3767  -0.4369 336 LYS B O   
6657 C CB  . LYS B 350 ? 0.5978 0.6457 1.3262 -0.0303 0.3244  -0.3655 336 LYS B CB  
6658 C CG  . LYS B 350 ? 0.6626 0.6837 1.4078 -0.0206 0.3032  -0.3505 336 LYS B CG  
6659 C CD  . LYS B 350 ? 0.6171 0.6220 1.4199 -0.0089 0.2841  -0.3326 336 LYS B CD  
6660 C CE  . LYS B 350 ? 0.5683 0.5517 1.3750 0.0017  0.2596  -0.3032 336 LYS B CE  
6661 N NZ  . LYS B 350 ? 0.8180 0.7953 1.6698 0.0119  0.2409  -0.2773 336 LYS B NZ  
6662 N N   . GLN B 351 ? 0.6290 0.7535 1.2736 -0.0611 0.3731  -0.3860 337 GLN B N   
6663 C CA  . GLN B 351 ? 0.6444 0.7996 1.2804 -0.0740 0.3912  -0.3997 337 GLN B CA  
6664 C C   . GLN B 351 ? 0.6779 0.8794 1.2629 -0.0978 0.4110  -0.4126 337 GLN B C   
6665 O O   . GLN B 351 ? 0.6977 0.9293 1.2784 -0.1146 0.4268  -0.4400 337 GLN B O   
6666 C CB  . GLN B 351 ? 0.6223 0.7730 1.2578 -0.0643 0.3865  -0.3687 337 GLN B CB  
6667 C CG  . GLN B 351 ? 0.7857 0.9592 1.4226 -0.0729 0.4009  -0.3786 337 GLN B CG  
6668 C CD  . GLN B 351 ? 0.9102 1.0799 1.5433 -0.0644 0.3959  -0.3457 337 GLN B CD  
6669 O OE1 . GLN B 351 ? 0.8323 1.0313 1.4380 -0.0755 0.4087  -0.3356 337 GLN B OE1 
6670 N NE2 . GLN B 351 ? 0.7721 0.9089 1.4337 -0.0467 0.3762  -0.3272 337 GLN B NE2 
6671 N N   . HIS B 352 ? 0.7182 0.9304 1.2644 -0.1020 0.4098  -0.3912 338 HIS B N   
6672 C CA  . HIS B 352 ? 0.6901 0.9500 1.1786 -0.1274 0.4203  -0.3852 338 HIS B CA  
6673 C C   . HIS B 352 ? 0.8304 1.1007 1.2817 -0.1406 0.4150  -0.3913 338 HIS B C   
6674 O O   . HIS B 352 ? 0.9149 1.2344 1.3213 -0.1657 0.4256  -0.3925 338 HIS B O   
6675 C CB  . HIS B 352 ? 0.6619 0.9250 1.1196 -0.1269 0.4095  -0.3338 338 HIS B CB  
6676 C CG  . HIS B 352 ? 0.6530 0.9192 1.1392 -0.1204 0.4192  -0.3294 338 HIS B CG  
6677 N ND1 . HIS B 352 ? 0.6779 0.9800 1.1669 -0.1345 0.4400  -0.3544 338 HIS B ND1 
6678 C CD2 . HIS B 352 ? 0.6402 0.8772 1.1509 -0.1021 0.4080  -0.3033 338 HIS B CD2 
6679 C CE1 . HIS B 352 ? 0.6666 0.9565 1.1774 -0.1236 0.4384  -0.3405 338 HIS B CE1 
6680 N NE2 . HIS B 352 ? 0.7258 0.9805 1.2546 -0.1046 0.4231  -0.3123 338 HIS B NE2 
6681 N N   . VAL B 353 ? 0.8343 1.0643 1.3026 -0.1262 0.3989  -0.3934 339 VAL B N   
6682 C CA  . VAL B 353 ? 0.9396 1.1772 1.3757 -0.1378 0.3938  -0.4010 339 VAL B CA  
6683 C C   . VAL B 353 ? 0.9046 1.1553 1.3757 -0.1461 0.4135  -0.4594 339 VAL B C   
6684 O O   . VAL B 353 ? 0.9212 1.1362 1.4513 -0.1294 0.4098  -0.4772 339 VAL B O   
6685 C CB  . VAL B 353 ? 0.8401 1.0291 1.2733 -0.1196 0.3655  -0.3694 339 VAL B CB  
6686 C CG1 . VAL B 353 ? 0.8186 1.0140 1.2238 -0.1309 0.3615  -0.3815 339 VAL B CG1 
6687 C CG2 . VAL B 353 ? 0.8033 0.9851 1.2056 -0.1151 0.3493  -0.3169 339 VAL B CG2 
6688 N N   . HIS B 354 ? 1.0528 1.3559 1.4882 -0.1741 0.4303  -0.4849 340 HIS B N   
6689 C CA  . HIS B 354 ? 1.1327 1.4498 1.5900 -0.1890 0.4396  -0.5345 340 HIS B CA  
6690 C C   . HIS B 354 ? 1.2610 1.5806 1.7059 -0.1982 0.4363  -0.5531 340 HIS B C   
6691 O O   . HIS B 354 ? 1.3172 1.6249 1.8065 -0.2005 0.4373  -0.5883 340 HIS B O   
6692 C CB  . HIS B 354 ? 1.1803 1.5592 1.6047 -0.2188 0.4566  -0.5521 340 HIS B CB  
6693 C CG  . HIS B 354 ? 1.3187 1.7499 1.6696 -0.2406 0.4585  -0.5236 340 HIS B CG  
6694 N ND1 . HIS B 354 ? 1.3120 1.7870 1.6208 -0.2673 0.4609  -0.5390 340 HIS B ND1 
6695 C CD2 . HIS B 354 ? 1.2940 1.7418 1.6109 -0.2410 0.4559  -0.4755 340 HIS B CD2 
6696 C CE1 . HIS B 354 ? 1.3494 1.8667 1.5989 -0.2831 0.4577  -0.4985 340 HIS B CE1 
6697 N NE2 . HIS B 354 ? 1.3787 1.8797 1.6349 -0.2678 0.4549  -0.4586 340 HIS B NE2 
6698 N N   . ASP B 355 ? 1.2480 1.5844 1.6386 -0.2047 0.4322  -0.5283 341 ASP B N   
6699 C CA  . ASP B 355 ? 1.3080 1.6671 1.6691 -0.2232 0.4321  -0.5475 341 ASP B CA  
6700 C C   . ASP B 355 ? 1.3537 1.6593 1.7601 -0.2045 0.4202  -0.5624 341 ASP B C   
6701 O O   . ASP B 355 ? 1.3151 1.5646 1.7611 -0.1757 0.4065  -0.5431 341 ASP B O   
6702 C CB  . ASP B 355 ? 1.3804 1.7620 1.6674 -0.2348 0.4157  -0.4988 341 ASP B CB  
6703 C CG  . ASP B 355 ? 1.3107 1.6306 1.5945 -0.2072 0.3844  -0.4444 341 ASP B CG  
6704 O OD1 . ASP B 355 ? 1.3314 1.5998 1.6626 -0.1808 0.3767  -0.4384 341 ASP B OD1 
6705 O OD2 . ASP B 355 ? 1.0843 1.4108 1.3199 -0.2136 0.3676  -0.4083 341 ASP B OD2 
6706 N N   . THR B 356 ? 1.2473 1.5746 1.6486 -0.2237 0.4235  -0.5947 342 THR B N   
6707 C CA  . THR B 356 ? 1.3162 1.6070 1.7457 -0.2137 0.4121  -0.6045 342 THR B CA  
6708 C C   . THR B 356 ? 1.3537 1.6687 1.7150 -0.2274 0.4081  -0.5925 342 THR B C   
6709 O O   . THR B 356 ? 1.3797 1.7571 1.6922 -0.2580 0.4177  -0.6036 342 THR B O   
6710 C CB  . THR B 356 ? 1.3235 1.6255 1.8111 -0.2270 0.4208  -0.6506 342 THR B CB  
6711 O OG1 . THR B 356 ? 1.4036 1.7650 1.8493 -0.2607 0.4316  -0.6783 342 THR B OG1 
6712 C CG2 . THR B 356 ? 1.1792 1.4862 1.7175 -0.2275 0.4318  -0.6678 342 THR B CG2 
6713 N N   . PRO B 357 ? 1.2121 1.4785 1.5663 -0.2077 0.3846  -0.5591 343 PRO B N   
6714 C CA  . PRO B 357 ? 1.2883 1.5684 1.5707 -0.2175 0.3658  -0.5191 343 PRO B CA  
6715 C C   . PRO B 357 ? 1.3764 1.7009 1.6284 -0.2443 0.3750  -0.5512 343 PRO B C   
6716 O O   . PRO B 357 ? 1.4209 1.7608 1.6152 -0.2538 0.3591  -0.5172 343 PRO B O   
6717 C CB  . PRO B 357 ? 1.0717 1.2821 1.3680 -0.1880 0.3366  -0.4787 343 PRO B CB  
6718 C CG  . PRO B 357 ? 1.0831 1.2516 1.4579 -0.1687 0.3416  -0.5081 343 PRO B CG  
6719 C CD  . PRO B 357 ? 1.0320 1.2288 1.4442 -0.1758 0.3683  -0.5456 343 PRO B CD  
6720 N N   . VAL B 358 ? 1.4559 1.8006 1.7489 -0.2570 0.3965  -0.6110 344 VAL B N   
6721 C CA  . VAL B 358 ? 1.4725 1.8615 1.7463 -0.2850 0.4000  -0.6397 344 VAL B CA  
6722 C C   . VAL B 358 ? 1.4995 1.8692 1.7374 -0.2807 0.3846  -0.6218 344 VAL B C   
6723 O O   . VAL B 358 ? 1.5552 1.9656 1.7231 -0.2989 0.3786  -0.5974 344 VAL B O   
6724 C CB  . VAL B 358 ? 1.5068 1.9802 1.7284 -0.3223 0.4120  -0.6479 344 VAL B CB  
6725 C CG1 . VAL B 358 ? 1.3715 1.8615 1.6370 -0.3289 0.4275  -0.6760 344 VAL B CG1 
6726 C CG2 . VAL B 358 ? 1.4606 1.9657 1.6062 -0.3294 0.4061  -0.5969 344 VAL B CG2 
6727 N N   . PRO B 359 ? 1.5143 1.8223 1.8015 -0.2572 0.3726  -0.6240 345 PRO B N   
6728 C CA  . PRO B 359 ? 1.3588 1.6294 1.6264 -0.2463 0.3537  -0.6052 345 PRO B CA  
6729 C C   . PRO B 359 ? 1.3197 1.6392 1.5122 -0.2719 0.3473  -0.5928 345 PRO B C   
6730 O O   . PRO B 359 ? 1.2992 1.5958 1.4815 -0.2678 0.3324  -0.5844 345 PRO B O   
6731 C CB  . PRO B 359 ? 1.3558 1.5984 1.7005 -0.2372 0.3519  -0.6295 345 PRO B CB  
6732 C CG  . PRO B 359 ? 1.3456 1.6212 1.7459 -0.2487 0.3724  -0.6649 345 PRO B CG  
6733 C CD  . PRO B 359 ? 1.3910 1.6748 1.7678 -0.2464 0.3779  -0.6501 345 PRO B CD  
6734 N N   . PRO B 370 ? 1.2082 1.0964 1.2692 -0.1798 0.0774  -0.3909 356 PRO B N   
6735 C CA  . PRO B 370 ? 1.2614 1.1176 1.3039 -0.1721 0.0560  -0.3630 356 PRO B CA  
6736 C C   . PRO B 370 ? 1.3043 1.1931 1.2961 -0.1911 0.0520  -0.3660 356 PRO B C   
6737 O O   . PRO B 370 ? 1.3976 1.3376 1.3754 -0.2101 0.0675  -0.3931 356 PRO B O   
6738 C CB  . PRO B 370 ? 1.1845 1.0199 1.2772 -0.1583 0.0585  -0.3696 356 PRO B CB  
6739 C CG  . PRO B 370 ? 0.9831 0.8465 1.1225 -0.1619 0.0832  -0.4058 356 PRO B CG  
6740 C CD  . PRO B 370 ? 1.0438 0.9252 1.1699 -0.1684 0.0911  -0.4103 356 PRO B CD  
6741 N N   . ASP B 371 ? 1.1604 1.0243 1.1275 -0.1869 0.0316  -0.3375 357 ASP B N   
6742 C CA  . ASP B 371 ? 1.2970 1.1905 1.2151 -0.2048 0.0240  -0.3312 357 ASP B CA  
6743 C C   . ASP B 371 ? 1.2701 1.1322 1.1879 -0.1941 0.0072  -0.3131 357 ASP B C   
6744 O O   . ASP B 371 ? 1.2989 1.1283 1.2516 -0.1774 0.0055  -0.3129 357 ASP B O   
6745 C CB  . ASP B 371 ? 1.3235 1.2276 1.2037 -0.2171 0.0158  -0.3084 357 ASP B CB  
6746 C CG  . ASP B 371 ? 1.4270 1.3949 1.2769 -0.2424 0.0290  -0.3251 357 ASP B CG  
6747 O OD1 . ASP B 371 ? 1.5562 1.5516 1.4268 -0.2456 0.0491  -0.3578 357 ASP B OD1 
6748 O OD2 . ASP B 371 ? 1.2553 1.2503 1.0668 -0.2548 0.0186  -0.2954 357 ASP B OD2 
6749 N N   . GLY B 372 ? 1.1004 0.9764 0.9793 -0.2054 -0.0053 -0.2961 358 GLY B N   
6750 C CA  . GLY B 372 ? 0.8806 0.7277 0.7581 -0.1953 -0.0225 -0.2761 358 GLY B CA  
6751 C C   . GLY B 372 ? 0.9281 0.7470 0.7970 -0.1890 -0.0395 -0.2408 358 GLY B C   
6752 O O   . GLY B 372 ? 0.9614 0.7452 0.8564 -0.1722 -0.0442 -0.2277 358 GLY B O   
6753 N N   . SER B 373 ? 0.8505 0.6885 0.6853 -0.2040 -0.0490 -0.2229 359 SER B N   
6754 C CA  . SER B 373 ? 0.8995 0.7130 0.7300 -0.2003 -0.0633 -0.1882 359 SER B CA  
6755 C C   . SER B 373 ? 0.7646 0.5680 0.5963 -0.2022 -0.0603 -0.1782 359 SER B C   
6756 O O   . SER B 373 ? 0.7788 0.6186 0.6007 -0.2103 -0.0503 -0.1828 359 SER B O   
6757 C CB  . SER B 373 ? 0.7904 0.6290 0.5862 -0.2195 -0.0753 -0.1677 359 SER B CB  
6758 O OG  . SER B 373 ? 0.8226 0.6317 0.6293 -0.2092 -0.0889 -0.1372 359 SER B OG  
6759 N N   . LEU B 374 ? 0.6115 0.3803 0.4678 -0.1840 -0.0671 -0.1568 360 LEU B N   
6760 C CA  . LEU B 374 ? 0.7444 0.5024 0.6111 -0.1796 -0.0637 -0.1460 360 LEU B CA  
6761 C C   . LEU B 374 ? 0.7971 0.5870 0.6500 -0.1857 -0.0660 -0.1172 360 LEU B C   
6762 O O   . LEU B 374 ? 0.7283 0.5229 0.5743 -0.1899 -0.0772 -0.0932 360 LEU B O   
6763 C CB  . LEU B 374 ? 0.7384 0.4710 0.6406 -0.1572 -0.0687 -0.1285 360 LEU B CB  
6764 C CG  . LEU B 374 ? 0.7409 0.4649 0.6829 -0.1403 -0.0620 -0.1432 360 LEU B CG  
6765 C CD1 . LEU B 374 ? 0.5246 0.2466 0.4951 -0.1261 -0.0591 -0.1243 360 LEU B CD1 
6766 C CD2 . LEU B 374 ? 0.6994 0.4182 0.6426 -0.1435 -0.0540 -0.1543 360 LEU B CD2 
6767 N N   . THR B 375 ? 0.7388 0.5513 0.5931 -0.1864 -0.0552 -0.1186 361 THR B N   
6768 C CA  . THR B 375 ? 0.6773 0.5182 0.5275 -0.1905 -0.0562 -0.0885 361 THR B CA  
6769 C C   . THR B 375 ? 0.7892 0.6162 0.6614 -0.1792 -0.0486 -0.0858 361 THR B C   
6770 O O   . THR B 375 ? 0.6484 0.4509 0.5363 -0.1700 -0.0424 -0.1078 361 THR B O   
6771 C CB  . THR B 375 ? 0.6879 0.5862 0.5115 -0.2084 -0.0501 -0.0908 361 THR B CB  
6772 O OG1 . THR B 375 ? 0.7550 0.6660 0.5771 -0.2110 -0.0338 -0.1271 361 THR B OG1 
6773 C CG2 . THR B 375 ? 0.7617 0.6799 0.5629 -0.2215 -0.0586 -0.0915 361 THR B CG2 
6774 N N   . GLN B 376 ? 0.7187 0.5626 0.5971 -0.1799 -0.0494 -0.0569 362 GLN B N   
6775 C CA  . GLN B 376 ? 0.7293 0.5679 0.6263 -0.1712 -0.0405 -0.0556 362 GLN B CA  
6776 C C   . GLN B 376 ? 0.6565 0.5142 0.5459 -0.1743 -0.0257 -0.0849 362 GLN B C   
6777 O O   . GLN B 376 ? 0.6253 0.4617 0.5343 -0.1639 -0.0185 -0.1011 362 GLN B O   
6778 C CB  . GLN B 376 ? 0.6878 0.5488 0.5945 -0.1742 -0.0419 -0.0207 362 GLN B CB  
6779 C CG  . GLN B 376 ? 0.6399 0.4782 0.5707 -0.1693 -0.0527 0.0038  362 GLN B CG  
6780 C CD  . GLN B 376 ? 0.5812 0.3870 0.5396 -0.1568 -0.0502 -0.0006 362 GLN B CD  
6781 O OE1 . GLN B 376 ? 0.6620 0.4675 0.6255 -0.1512 -0.0408 -0.0113 362 GLN B OE1 
6782 N NE2 . GLN B 376 ? 0.5908 0.3727 0.5681 -0.1538 -0.0580 0.0065  362 GLN B NE2 
6783 N N   . ASP B 377 ? 0.6181 0.5189 0.4817 -0.1901 -0.0207 -0.0937 363 ASP B N   
6784 C CA  . ASP B 377 ? 0.7728 0.7004 0.6314 -0.1969 -0.0038 -0.1253 363 ASP B CA  
6785 C C   . ASP B 377 ? 0.7570 0.6521 0.6353 -0.1884 0.0030  -0.1641 363 ASP B C   
6786 O O   . ASP B 377 ? 0.6547 0.5394 0.5566 -0.1805 0.0142  -0.1816 363 ASP B O   
6787 C CB  . ASP B 377 ? 0.8187 0.8057 0.6440 -0.2198 -0.0004 -0.1298 363 ASP B CB  
6788 C CG  . ASP B 377 ? 0.9721 1.0055 0.7894 -0.2315 0.0163  -0.1439 363 ASP B CG  
6789 O OD1 . ASP B 377 ? 1.0046 1.0598 0.8206 -0.2337 0.0155  -0.1128 363 ASP B OD1 
6790 O OD2 . ASP B 377 ? 0.9281 0.9783 0.7441 -0.2396 0.0312  -0.1871 363 ASP B OD2 
6791 N N   . ASN B 378 ? 0.7411 0.6198 0.6155 -0.1898 -0.0038 -0.1760 364 ASN B N   
6792 C CA  . ASN B 378 ? 0.6491 0.4993 0.5502 -0.1827 0.0029  -0.2107 364 ASN B CA  
6793 C C   . ASN B 378 ? 0.6247 0.4235 0.5575 -0.1638 -0.0055 -0.1979 364 ASN B C   
6794 O O   . ASN B 378 ? 0.6270 0.4035 0.5929 -0.1560 0.0004  -0.2196 364 ASN B O   
6795 C CB  . ASN B 378 ? 0.6635 0.5182 0.5524 -0.1926 0.0006  -0.2312 364 ASN B CB  
6796 C CG  . ASN B 378 ? 0.7615 0.5966 0.6352 -0.1906 -0.0185 -0.2028 364 ASN B CG  
6797 O OD1 . ASN B 378 ? 0.7208 0.5234 0.6059 -0.1784 -0.0296 -0.1764 364 ASN B OD1 
6798 N ND2 . ASN B 378 ? 0.7318 0.5901 0.5814 -0.2044 -0.0215 -0.2108 364 ASN B ND2 
6799 N N   . PHE B 379 ? 0.6026 0.3860 0.5306 -0.1578 -0.0187 -0.1634 365 PHE B N   
6800 C CA  . PHE B 379 ? 0.6716 0.4173 0.6275 -0.1435 -0.0256 -0.1518 365 PHE B CA  
6801 C C   . PHE B 379 ? 0.6392 0.3858 0.6194 -0.1358 -0.0152 -0.1569 365 PHE B C   
6802 O O   . PHE B 379 ? 0.6732 0.3970 0.6856 -0.1266 -0.0143 -0.1663 365 PHE B O   
6803 C CB  . PHE B 379 ? 0.5593 0.2959 0.5076 -0.1421 -0.0388 -0.1194 365 PHE B CB  
6804 C CG  . PHE B 379 ? 0.5590 0.2697 0.5326 -0.1316 -0.0440 -0.1078 365 PHE B CG  
6805 C CD1 . PHE B 379 ? 0.5367 0.2356 0.5314 -0.1225 -0.0472 -0.1088 365 PHE B CD1 
6806 C CD2 . PHE B 379 ? 0.5513 0.2693 0.5351 -0.1278 -0.0406 -0.0933 365 PHE B CD2 
6807 C CE1 . PHE B 379 ? 0.5493 0.2490 0.5595 -0.1133 -0.0435 -0.0936 365 PHE B CE1 
6808 C CE2 . PHE B 379 ? 0.5964 0.2973 0.6024 -0.1209 -0.0451 -0.0846 365 PHE B CE2 
6809 C CZ  . PHE B 379 ? 0.5664 0.2683 0.5830 -0.1123 -0.0433 -0.0834 365 PHE B CZ  
6810 N N   . TRP B 380 ? 0.6030 0.3776 0.5716 -0.1398 -0.0079 -0.1484 366 TRP B N   
6811 C CA  . TRP B 380 ? 0.5789 0.3557 0.5700 -0.1327 0.0022  -0.1526 366 TRP B CA  
6812 C C   . TRP B 380 ? 0.6174 0.4032 0.6264 -0.1343 0.0176  -0.1888 366 TRP B C   
6813 O O   . TRP B 380 ? 0.6044 0.3770 0.6478 -0.1248 0.0235  -0.1973 366 TRP B O   
6814 C CB  . TRP B 380 ? 0.5766 0.3819 0.5521 -0.1375 0.0060  -0.1326 366 TRP B CB  
6815 C CG  . TRP B 380 ? 0.6097 0.4028 0.5850 -0.1343 -0.0064 -0.1003 366 TRP B CG  
6816 C CD1 . TRP B 380 ? 0.5518 0.3597 0.5095 -0.1422 -0.0136 -0.0779 366 TRP B CD1 
6817 C CD2 . TRP B 380 ? 0.5783 0.3450 0.5778 -0.1238 -0.0126 -0.0885 366 TRP B CD2 
6818 N NE1 . TRP B 380 ? 0.6029 0.3926 0.5769 -0.1367 -0.0220 -0.0561 366 TRP B NE1 
6819 C CE2 . TRP B 380 ? 0.5547 0.3212 0.5513 -0.1265 -0.0212 -0.0637 366 TRP B CE2 
6820 C CE3 . TRP B 380 ? 0.5231 0.2705 0.5495 -0.1138 -0.0116 -0.0962 366 TRP B CE3 
6821 C CZ2 . TRP B 380 ? 0.5695 0.3191 0.5870 -0.1212 -0.0267 -0.0518 366 TRP B CZ2 
6822 C CZ3 . TRP B 380 ? 0.5751 0.3084 0.6174 -0.1091 -0.0194 -0.0799 366 TRP B CZ3 
6823 C CH2 . TRP B 380 ? 0.5026 0.2380 0.5394 -0.1134 -0.0258 -0.0607 366 TRP B CH2 
6824 N N   . LYS B 381 ? 0.6222 0.4328 0.6126 -0.1474 0.0249  -0.2117 367 LYS B N   
6825 C CA  . LYS B 381 ? 0.6433 0.4628 0.6587 -0.1508 0.0416  -0.2531 367 LYS B CA  
6826 C C   . LYS B 381 ? 0.7527 0.5313 0.8119 -0.1390 0.0375  -0.2640 367 LYS B C   
6827 O O   . LYS B 381 ? 0.6833 0.4570 0.7857 -0.1303 0.0474  -0.2802 367 LYS B O   
6828 C CB  . LYS B 381 ? 0.6687 0.5286 0.6542 -0.1705 0.0500  -0.2774 367 LYS B CB  
6829 C CG  . LYS B 381 ? 0.7027 0.6161 0.6585 -0.1860 0.0611  -0.2784 367 LYS B CG  
6830 C CD  . LYS B 381 ? 0.9161 0.8758 0.8341 -0.2084 0.0638  -0.2919 367 LYS B CD  
6831 C CE  . LYS B 381 ? 0.9626 0.9822 0.8462 -0.2263 0.0702  -0.2804 367 LYS B CE  
6832 N NZ  . LYS B 381 ? 0.9846 1.0604 0.8327 -0.2521 0.0742  -0.2970 367 LYS B NZ  
6833 N N   . THR B 382 ? 0.6585 0.4134 0.7085 -0.1360 0.0213  -0.2470 368 THR B N   
6834 C CA  . THR B 382 ? 0.6987 0.4291 0.7799 -0.1185 0.0118  -0.2340 368 THR B CA  
6835 C C   . THR B 382 ? 0.6666 0.3793 0.7752 -0.1045 0.0061  -0.2107 368 THR B C   
6836 O O   . THR B 382 ? 0.7349 0.4417 0.8831 -0.0938 0.0085  -0.2108 368 THR B O   
6837 C CB  . THR B 382 ? 0.6403 0.3561 0.6967 -0.1184 -0.0051 -0.2147 368 THR B CB  
6838 O OG1 . THR B 382 ? 0.6312 0.3672 0.6655 -0.1312 0.0002  -0.2367 368 THR B OG1 
6839 C CG2 . THR B 382 ? 0.6102 0.3045 0.6916 -0.1052 -0.0130 -0.1991 368 THR B CG2 
6840 N N   . LEU B 383 ? 0.5937 0.3019 0.6853 -0.1058 -0.0008 -0.1903 369 LEU B N   
6841 C CA  . LEU B 383 ? 0.7501 0.4489 0.8644 -0.0947 -0.0057 -0.1689 369 LEU B CA  
6842 C C   . LEU B 383 ? 0.6670 0.3757 0.8158 -0.0907 0.0093  -0.1868 369 LEU B C   
6843 O O   . LEU B 383 ? 0.7155 0.4186 0.8979 -0.0796 0.0067  -0.1749 369 LEU B O   
6844 C CB  . LEU B 383 ? 0.7373 0.4345 0.8294 -0.0984 -0.0135 -0.1470 369 LEU B CB  
6845 C CG  . LEU B 383 ? 0.6767 0.3648 0.7621 -0.0929 -0.0281 -0.1167 369 LEU B CG  
6846 C CD1 . LEU B 383 ? 0.8107 0.5044 0.8893 -0.0952 -0.0301 -0.1012 369 LEU B CD1 
6847 C CD2 . LEU B 383 ? 0.7633 0.4486 0.8804 -0.0828 -0.0300 -0.1089 369 LEU B CD2 
6848 N N   . GLN B 384 ? 0.6844 0.4120 0.8252 -0.1017 0.0262  -0.2163 370 GLN B N   
6849 C CA  . GLN B 384 ? 0.6055 0.3462 0.7774 -0.0995 0.0431  -0.2366 370 GLN B CA  
6850 C C   . GLN B 384 ? 0.6140 0.3525 0.8351 -0.0881 0.0467  -0.2452 370 GLN B C   
6851 O O   . GLN B 384 ? 0.6112 0.3493 0.8724 -0.0787 0.0508  -0.2425 370 GLN B O   
6852 C CB  . GLN B 384 ? 0.6238 0.4011 0.7666 -0.1150 0.0604  -0.2628 370 GLN B CB  
6853 C CG  . GLN B 384 ? 0.6374 0.4327 0.8124 -0.1154 0.0807  -0.2907 370 GLN B CG  
6854 C CD  . GLN B 384 ? 0.6203 0.4096 0.8088 -0.1045 0.0784  -0.2679 370 GLN B CD  
6855 O OE1 . GLN B 384 ? 0.6074 0.4050 0.7606 -0.1055 0.0712  -0.2402 370 GLN B OE1 
6856 N NE2 . GLN B 384 ? 0.6204 0.3959 0.8655 -0.0944 0.0845  -0.2791 370 GLN B NE2 
6857 N N   . THR B 385 ? 0.5987 0.4343 0.6270 -0.0605 0.0798  -0.1936 371 THR B N   
6858 C CA  . THR B 385 ? 0.6343 0.4521 0.6727 -0.0536 0.0824  -0.2023 371 THR B CA  
6859 C C   . THR B 385 ? 0.5551 0.3705 0.6165 -0.0450 0.0775  -0.1918 371 THR B C   
6860 O O   . THR B 385 ? 0.5030 0.3054 0.5765 -0.0366 0.0802  -0.1975 371 THR B O   
6861 C CB  . THR B 385 ? 0.6584 0.4563 0.6812 -0.0625 0.0777  -0.2098 371 THR B CB  
6862 O OG1 . THR B 385 ? 0.7403 0.5347 0.7671 -0.0678 0.0660  -0.1978 371 THR B OG1 
6863 C CG2 . THR B 385 ? 0.6309 0.4327 0.6280 -0.0733 0.0795  -0.2169 371 THR B CG2 
6864 N N   . PHE B 386 ? 0.5740 0.4014 0.6413 -0.0466 0.0704  -0.1770 372 PHE B N   
6865 C CA  . PHE B 386 ? 0.5719 0.3965 0.6575 -0.0407 0.0647  -0.1662 372 PHE B CA  
6866 C C   . PHE B 386 ? 0.6413 0.4790 0.7447 -0.0297 0.0686  -0.1615 372 PHE B C   
6867 O O   . PHE B 386 ? 0.5578 0.3886 0.6772 -0.0216 0.0667  -0.1579 372 PHE B O   
6868 C CB  . PHE B 386 ? 0.6665 0.4969 0.7488 -0.0487 0.0550  -0.1532 372 PHE B CB  
6869 C CG  . PHE B 386 ? 0.4875 0.3187 0.5860 -0.0437 0.0497  -0.1409 372 PHE B CG  
6870 C CD1 . PHE B 386 ? 0.5222 0.3354 0.6279 -0.0421 0.0462  -0.1400 372 PHE B CD1 
6871 C CD2 . PHE B 386 ? 0.5043 0.3531 0.6095 -0.0413 0.0480  -0.1302 372 PHE B CD2 
6872 C CE1 . PHE B 386 ? 0.5545 0.3682 0.6729 -0.0385 0.0413  -0.1280 372 PHE B CE1 
6873 C CE2 . PHE B 386 ? 0.5564 0.4059 0.6743 -0.0374 0.0432  -0.1192 372 PHE B CE2 
6874 C CZ  . PHE B 386 ? 0.6015 0.4338 0.7256 -0.0362 0.0399  -0.1178 372 PHE B CZ  
6875 N N   . ILE B 387 ? 0.5265 0.3828 0.6273 -0.0297 0.0736  -0.1612 373 ILE B N   
6876 C CA  . ILE B 387 ? 0.5417 0.4124 0.6596 -0.0208 0.0762  -0.1558 373 ILE B CA  
6877 C C   . ILE B 387 ? 0.5862 0.4521 0.7183 -0.0098 0.0837  -0.1658 373 ILE B C   
6878 O O   . ILE B 387 ? 0.4390 0.2952 0.5641 -0.0098 0.0902  -0.1793 373 ILE B O   
6879 C CB  . ILE B 387 ? 0.5296 0.4203 0.6403 -0.0249 0.0796  -0.1533 373 ILE B CB  
6880 C CG1 . ILE B 387 ? 0.5736 0.4650 0.6685 -0.0297 0.0884  -0.1660 373 ILE B CG1 
6881 C CG2 . ILE B 387 ? 0.4889 0.3843 0.5901 -0.0332 0.0710  -0.1419 373 ILE B CG2 
6882 C CD1 . ILE B 387 ? 0.5159 0.4255 0.6026 -0.0346 0.0921  -0.1631 373 ILE B CD1 
6883 N N   . ARG B 388 ? 0.4376 0.3100 0.5899 -0.0003 0.0825  -0.1594 374 ARG B N   
6884 C CA  . ARG B 388 ? 0.4510 0.3195 0.6214 0.0120  0.0875  -0.1667 374 ARG B CA  
6885 C C   . ARG B 388 ? 0.5064 0.3970 0.6938 0.0190  0.0904  -0.1623 374 ARG B C   
6886 O O   . ARG B 388 ? 0.4803 0.3848 0.6657 0.0145  0.0865  -0.1518 374 ARG B O   
6887 C CB  . ARG B 388 ? 0.4607 0.3095 0.6414 0.0175  0.0797  -0.1619 374 ARG B CB  
6888 C CG  . ARG B 388 ? 0.5025 0.3271 0.6697 0.0116  0.0773  -0.1680 374 ARG B CG  
6889 C CD  . ARG B 388 ? 0.5905 0.4062 0.7535 0.0145  0.0870  -0.1860 374 ARG B CD  
6890 N NE  . ARG B 388 ? 0.6759 0.4657 0.8279 0.0097  0.0838  -0.1920 374 ARG B NE  
6891 C CZ  . ARG B 388 ? 0.7434 0.5276 0.8738 -0.0022 0.0838  -0.1974 374 ARG B CZ  
6892 N NH1 . ARG B 388 ? 0.6065 0.4081 0.7232 -0.0101 0.0867  -0.1972 374 ARG B NH1 
6893 N NH2 . ARG B 388 ? 0.6416 0.4016 0.7637 -0.0066 0.0801  -0.2027 374 ARG B NH2 
6894 N N   . PRO B 389 ? 0.4926 0.3870 0.6971 0.0298  0.0973  -0.1707 375 PRO B N   
6895 C CA  . PRO B 389 ? 0.4122 0.3277 0.6366 0.0371  0.0985  -0.1656 375 PRO B CA  
6896 C C   . PRO B 389 ? 0.4783 0.3925 0.7134 0.0402  0.0868  -0.1503 375 PRO B C   
6897 O O   . PRO B 389 ? 0.4942 0.3894 0.7307 0.0427  0.0796  -0.1463 375 PRO B O   
6898 C CB  . PRO B 389 ? 0.4095 0.3251 0.6524 0.0494  0.1068  -0.1783 375 PRO B CB  
6899 C CG  . PRO B 389 ? 0.5415 0.4432 0.7676 0.0454  0.1145  -0.1928 375 PRO B CG  
6900 C CD  . PRO B 389 ? 0.4467 0.3294 0.6518 0.0349  0.1058  -0.1870 375 PRO B CD  
6901 N N   . GLY B 390 ? 0.4702 0.4045 0.7119 0.0395  0.0849  -0.1418 376 GLY B N   
6902 C CA  . GLY B 390 ? 0.3885 0.3240 0.6379 0.0413  0.0742  -0.1275 376 GLY B CA  
6903 C C   . GLY B 390 ? 0.4266 0.3588 0.6580 0.0306  0.0673  -0.1174 376 GLY B C   
6904 O O   . GLY B 390 ? 0.4089 0.3436 0.6445 0.0311  0.0592  -0.1057 376 GLY B O   
6905 N N   . ASP B 391 ? 0.3710 0.2983 0.5828 0.0212  0.0702  -0.1217 377 ASP B N   
6906 C CA  . ASP B 391 ? 0.4239 0.3491 0.6203 0.0117  0.0637  -0.1128 377 ASP B CA  
6907 C C   . ASP B 391 ? 0.4852 0.4291 0.6807 0.0083  0.0626  -0.1057 377 ASP B C   
6908 O O   . ASP B 391 ? 0.4723 0.4305 0.6712 0.0087  0.0689  -0.1099 377 ASP B O   
6909 C CB  . ASP B 391 ? 0.4033 0.3197 0.5802 0.0027  0.0663  -0.1196 377 ASP B CB  
6910 C CG  . ASP B 391 ? 0.5329 0.4275 0.7068 0.0028  0.0637  -0.1231 377 ASP B CG  
6911 O OD1 . ASP B 391 ? 0.5181 0.4033 0.7030 0.0084  0.0585  -0.1177 377 ASP B OD1 
6912 O OD2 . ASP B 391 ? 0.4737 0.3599 0.6334 -0.0034 0.0665  -0.1311 377 ASP B OD2 
6913 N N   . ILE B 392 ? 0.4545 0.3979 0.6455 0.0046  0.0548  -0.0950 378 ILE B N   
6914 C CA  . ILE B 392 ? 0.3874 0.3441 0.5726 -0.0005 0.0529  -0.0885 378 ILE B CA  
6915 C C   . ILE B 392 ? 0.4627 0.4140 0.6295 -0.0096 0.0509  -0.0877 378 ILE B C   
6916 O O   . ILE B 392 ? 0.4643 0.4052 0.6269 -0.0118 0.0458  -0.0839 378 ILE B O   
6917 C CB  . ILE B 392 ? 0.4498 0.4109 0.6433 0.0026  0.0456  -0.0778 378 ILE B CB  
6918 C CG1 . ILE B 392 ? 0.3633 0.3293 0.5762 0.0121  0.0460  -0.0782 378 ILE B CG1 
6919 C CG2 . ILE B 392 ? 0.3752 0.3483 0.5618 -0.0028 0.0437  -0.0723 378 ILE B CG2 
6920 C CD1 . ILE B 392 ? 0.2602 0.2301 0.4807 0.0151  0.0381  -0.0677 378 ILE B CD1 
6921 N N   . ILE B 393 ? 0.4387 0.3972 0.5950 -0.0153 0.0549  -0.0912 379 ILE B N   
6922 C CA  . ILE B 393 ? 0.4109 0.3651 0.5501 -0.0236 0.0528  -0.0911 379 ILE B CA  
6923 C C   . ILE B 393 ? 0.4052 0.3697 0.5388 -0.0276 0.0498  -0.0842 379 ILE B C   
6924 O O   . ILE B 393 ? 0.4011 0.3757 0.5362 -0.0278 0.0536  -0.0849 379 ILE B O   
6925 C CB  . ILE B 393 ? 0.4002 0.3509 0.5284 -0.0275 0.0594  -0.1015 379 ILE B CB  
6926 C CG1 . ILE B 393 ? 0.4809 0.4203 0.6156 -0.0225 0.0630  -0.1098 379 ILE B CG1 
6927 C CG2 . ILE B 393 ? 0.4118 0.3578 0.5223 -0.0363 0.0555  -0.1007 379 ILE B CG2 
6928 C CD1 . ILE B 393 ? 0.3634 0.3000 0.4881 -0.0253 0.0711  -0.1219 379 ILE B CD1 
6929 N N   . LEU B 394 ? 0.4062 0.3681 0.5341 -0.0308 0.0432  -0.0777 380 LEU B N   
6930 C CA  . LEU B 394 ? 0.3934 0.3625 0.5155 -0.0341 0.0396  -0.0716 380 LEU B CA  
6931 C C   . LEU B 394 ? 0.4108 0.3760 0.5190 -0.0406 0.0364  -0.0716 380 LEU B C   
6932 O O   . LEU B 394 ? 0.3578 0.3160 0.4643 -0.0422 0.0336  -0.0721 380 LEU B O   
6933 C CB  . LEU B 394 ? 0.3288 0.3005 0.4589 -0.0307 0.0343  -0.0635 380 LEU B CB  
6934 C CG  . LEU B 394 ? 0.3576 0.3324 0.5017 -0.0241 0.0353  -0.0622 380 LEU B CG  
6935 C CD1 . LEU B 394 ? 0.2549 0.2205 0.4055 -0.0206 0.0338  -0.0619 380 LEU B CD1 
6936 C CD2 . LEU B 394 ? 0.3244 0.3064 0.4715 -0.0229 0.0312  -0.0550 380 LEU B CD2 
6937 N N   . ALA B 395 ? 0.3558 0.3253 0.4542 -0.0449 0.0364  -0.0709 381 ALA B N   
6938 C CA  . ALA B 395 ? 0.4312 0.3976 0.5159 -0.0510 0.0325  -0.0705 381 ALA B CA  
6939 C C   . ALA B 395 ? 0.4704 0.4415 0.5514 -0.0522 0.0277  -0.0637 381 ALA B C   
6940 O O   . ALA B 395 ? 0.4259 0.4016 0.5073 -0.0520 0.0300  -0.0622 381 ALA B O   
6941 C CB  . ALA B 395 ? 0.3355 0.2995 0.4080 -0.0559 0.0374  -0.0776 381 ALA B CB  
6942 N N   . ASP B 396 ? 0.4025 0.3724 0.4807 -0.0536 0.0210  -0.0598 382 ASP B N   
6943 C CA  . ASP B 396 ? 0.3829 0.3558 0.4588 -0.0535 0.0160  -0.0538 382 ASP B CA  
6944 C C   . ASP B 396 ? 0.4338 0.4044 0.4950 -0.0592 0.0134  -0.0534 382 ASP B C   
6945 O O   . ASP B 396 ? 0.4086 0.3757 0.4606 -0.0637 0.0141  -0.0574 382 ASP B O   
6946 C CB  . ASP B 396 ? 0.2911 0.2656 0.3734 -0.0510 0.0103  -0.0497 382 ASP B CB  
6947 C CG  . ASP B 396 ? 0.5370 0.5153 0.6244 -0.0470 0.0082  -0.0447 382 ASP B CG  
6948 O OD1 . ASP B 396 ? 0.3730 0.3509 0.4547 -0.0480 0.0076  -0.0431 382 ASP B OD1 
6949 O OD2 . ASP B 396 ? 0.3409 0.3218 0.4369 -0.0434 0.0073  -0.0426 382 ASP B OD2 
6950 N N   . GLN B 397 ? 0.4253 0.3968 0.4835 -0.0591 0.0101  -0.0485 383 GLN B N   
6951 C CA  . GLN B 397 ? 0.4293 0.3970 0.4732 -0.0642 0.0059  -0.0462 383 GLN B CA  
6952 C C   . GLN B 397 ? 0.4304 0.3965 0.4711 -0.0656 -0.0009 -0.0456 383 GLN B C   
6953 O O   . GLN B 397 ? 0.4610 0.4302 0.5120 -0.0615 -0.0045 -0.0439 383 GLN B O   
6954 C CB  . GLN B 397 ? 0.4284 0.3954 0.4717 -0.0629 0.0020  -0.0403 383 GLN B CB  
6955 C CG  . GLN B 397 ? 0.4884 0.4570 0.5321 -0.0641 0.0077  -0.0404 383 GLN B CG  
6956 C CD  . GLN B 397 ? 0.6410 0.6111 0.6790 -0.0688 0.0155  -0.0455 383 GLN B CD  
6957 O OE1 . GLN B 397 ? 0.6278 0.6026 0.6756 -0.0661 0.0219  -0.0500 383 GLN B OE1 
6958 N NE2 . GLN B 397 ? 0.6544 0.6207 0.6765 -0.0758 0.0152  -0.0449 383 GLN B NE2 
6959 N N   . GLY B 398 ? 0.5020 0.4643 0.5284 -0.0718 -0.0026 -0.0470 384 GLY B N   
6960 C CA  . GLY B 398 ? 0.4296 0.3911 0.4523 -0.0744 -0.0087 -0.0478 384 GLY B CA  
6961 C C   . GLY B 398 ? 0.5878 0.5455 0.5993 -0.0804 -0.0042 -0.0546 384 GLY B C   
6962 O O   . GLY B 398 ? 0.4651 0.4213 0.4699 -0.0827 0.0034  -0.0582 384 GLY B O   
6963 N N   . THR B 399 ? 0.4115 0.3684 0.4215 -0.0831 -0.0086 -0.0570 385 THR B N   
6964 C CA  . THR B 399 ? 0.4565 0.4084 0.4557 -0.0887 -0.0045 -0.0648 385 THR B CA  
6965 C C   . THR B 399 ? 0.4313 0.3823 0.4396 -0.0853 0.0056  -0.0712 385 THR B C   
6966 O O   . THR B 399 ? 0.6029 0.5496 0.6022 -0.0886 0.0118  -0.0786 385 THR B O   
6967 C CB  . THR B 399 ? 0.5264 0.4774 0.5235 -0.0928 -0.0121 -0.0661 385 THR B CB  
6968 O OG1 . THR B 399 ? 0.4659 0.4205 0.4812 -0.0884 -0.0129 -0.0657 385 THR B OG1 
6969 C CG2 . THR B 399 ? 0.5206 0.4735 0.5103 -0.0953 -0.0231 -0.0593 385 THR B CG2 
6970 N N   . SER B 400 ? 0.3675 0.3222 0.3932 -0.0784 0.0071  -0.0686 386 SER B N   
6971 C CA  . SER B 400 ? 0.4304 0.3839 0.4660 -0.0742 0.0153  -0.0734 386 SER B CA  
6972 C C   . SER B 400 ? 0.5274 0.4820 0.5584 -0.0742 0.0235  -0.0768 386 SER B C   
6973 O O   . SER B 400 ? 0.4679 0.4192 0.4948 -0.0756 0.0302  -0.0847 386 SER B O   
6974 C CB  . SER B 400 ? 0.4256 0.3834 0.4785 -0.0675 0.0142  -0.0684 386 SER B CB  
6975 O OG  . SER B 400 ? 0.4462 0.4031 0.5055 -0.0679 0.0096  -0.0675 386 SER B OG  
6976 N N   . ALA B 401 ? 0.4479 0.4075 0.4802 -0.0727 0.0233  -0.0712 387 ALA B N   
6977 C CA  . ALA B 401 ? 0.4221 0.3847 0.4516 -0.0736 0.0313  -0.0738 387 ALA B CA  
6978 C C   . ALA B 401 ? 0.4337 0.3935 0.4435 -0.0815 0.0339  -0.0778 387 ALA B C   
6979 O O   . ALA B 401 ? 0.4419 0.4033 0.4489 -0.0829 0.0430  -0.0845 387 ALA B O   
6980 C CB  . ALA B 401 ? 0.4750 0.4426 0.5090 -0.0717 0.0294  -0.0665 387 ALA B CB  
6981 N N   . PHE B 402 ? 0.5079 0.4637 0.5038 -0.0868 0.0261  -0.0740 388 PHE B N   
6982 C CA  . PHE B 402 ? 0.5059 0.4585 0.4802 -0.0954 0.0275  -0.0764 388 PHE B CA  
6983 C C   . PHE B 402 ? 0.5409 0.4889 0.5070 -0.0986 0.0316  -0.0863 388 PHE B C   
6984 O O   . PHE B 402 ? 0.5292 0.4751 0.4771 -0.1056 0.0359  -0.0907 388 PHE B O   
6985 C CB  . PHE B 402 ? 0.5077 0.4570 0.4700 -0.0997 0.0162  -0.0683 388 PHE B CB  
6986 C CG  . PHE B 402 ? 0.6833 0.6346 0.6503 -0.0973 0.0124  -0.0594 388 PHE B CG  
6987 C CD1 . PHE B 402 ? 0.6470 0.6029 0.6219 -0.0951 0.0198  -0.0591 388 PHE B CD1 
6988 C CD2 . PHE B 402 ? 0.6537 0.6023 0.6180 -0.0971 0.0010  -0.0515 388 PHE B CD2 
6989 C CE1 . PHE B 402 ? 0.7692 0.7255 0.7476 -0.0936 0.0159  -0.0514 388 PHE B CE1 
6990 C CE2 . PHE B 402 ? 0.6212 0.5696 0.5895 -0.0946 -0.0025 -0.0441 388 PHE B CE2 
6991 C CZ  . PHE B 402 ? 0.7480 0.6995 0.7225 -0.0932 0.0049  -0.0441 388 PHE B CZ  
6992 N N   . GLY B 403 ? 0.5201 0.4656 0.4981 -0.0943 0.0304  -0.0899 389 GLY B N   
6993 C CA  . GLY B 403 ? 0.4854 0.4247 0.4575 -0.0967 0.0348  -0.1003 389 GLY B CA  
6994 C C   . GLY B 403 ? 0.4910 0.4313 0.4759 -0.0905 0.0457  -0.1078 389 GLY B C   
6995 O O   . GLY B 403 ? 0.5176 0.4544 0.4946 -0.0926 0.0535  -0.1179 389 GLY B O   
6996 N N   . ALA B 404 ? 0.4835 0.4288 0.4883 -0.0827 0.0463  -0.1032 390 ALA B N   
6997 C CA  . ALA B 404 ? 0.5132 0.4602 0.5327 -0.0758 0.0551  -0.1092 390 ALA B CA  
6998 C C   . ALA B 404 ? 0.5694 0.5229 0.5841 -0.0772 0.0655  -0.1144 390 ALA B C   
6999 O O   . ALA B 404 ? 0.4366 0.3913 0.4607 -0.0723 0.0741  -0.1223 390 ALA B O   
7000 C CB  . ALA B 404 ? 0.4045 0.3564 0.4443 -0.0680 0.0523  -0.1018 390 ALA B CB  
7001 N N   . ILE B 405 ? 0.5065 0.4644 0.5073 -0.0838 0.0649  -0.1100 391 ILE B N   
7002 C CA  . ILE B 405 ? 0.5853 0.5506 0.5804 -0.0869 0.0751  -0.1142 391 ILE B CA  
7003 C C   . ILE B 405 ? 0.5826 0.5441 0.5663 -0.0899 0.0841  -0.1270 391 ILE B C   
7004 O O   . ILE B 405 ? 0.6064 0.5755 0.5926 -0.0893 0.0955  -0.1338 391 ILE B O   
7005 C CB  . ILE B 405 ? 0.5683 0.5360 0.5473 -0.0951 0.0713  -0.1059 391 ILE B CB  
7006 C CG1 . ILE B 405 ? 0.5203 0.4983 0.4981 -0.0982 0.0819  -0.1079 391 ILE B CG1 
7007 C CG2 . ILE B 405 ? 0.5655 0.5244 0.5199 -0.1038 0.0660  -0.1066 391 ILE B CG2 
7008 C CD1 . ILE B 405 ? 0.4673 0.4462 0.4298 -0.1067 0.0782  -0.0988 391 ILE B CD1 
7009 N N   . ASP B 406 ? 0.5902 0.5406 0.5619 -0.0931 0.0793  -0.1310 392 ASP B N   
7010 C CA  . ASP B 406 ? 0.5932 0.5376 0.5512 -0.0967 0.0869  -0.1439 392 ASP B CA  
7011 C C   . ASP B 406 ? 0.6077 0.5475 0.5825 -0.0878 0.0926  -0.1538 392 ASP B C   
7012 O O   . ASP B 406 ? 0.6360 0.5701 0.6016 -0.0893 0.1002  -0.1663 392 ASP B O   
7013 C CB  . ASP B 406 ? 0.6197 0.5537 0.5558 -0.1053 0.0780  -0.1439 392 ASP B CB  
7014 C CG  . ASP B 406 ? 0.5623 0.4990 0.4781 -0.1146 0.0727  -0.1354 392 ASP B CG  
7015 O OD1 . ASP B 406 ? 0.6268 0.5700 0.5328 -0.1189 0.0808  -0.1365 392 ASP B OD1 
7016 O OD2 . ASP B 406 ? 0.6744 0.6069 0.5845 -0.1178 0.0602  -0.1275 392 ASP B OD2 
7017 N N   . LEU B 407 ? 0.4741 0.4148 0.4720 -0.0789 0.0889  -0.1486 393 LEU B N   
7018 C CA  . LEU B 407 ? 0.5883 0.5237 0.6031 -0.0699 0.0936  -0.1566 393 LEU B CA  
7019 C C   . LEU B 407 ? 0.6283 0.5733 0.6518 -0.0650 0.1070  -0.1651 393 LEU B C   
7020 O O   . LEU B 407 ? 0.5522 0.5112 0.5804 -0.0653 0.1107  -0.1604 393 LEU B O   
7021 C CB  . LEU B 407 ? 0.5279 0.4629 0.5639 -0.0623 0.0860  -0.1474 393 LEU B CB  
7022 C CG  . LEU B 407 ? 0.5836 0.5097 0.6159 -0.0655 0.0741  -0.1404 393 LEU B CG  
7023 C CD1 . LEU B 407 ? 0.4877 0.4175 0.5392 -0.0590 0.0681  -0.1299 393 LEU B CD1 
7024 C CD2 . LEU B 407 ? 0.5025 0.4131 0.5301 -0.0667 0.0734  -0.1493 393 LEU B CD2 
7025 N N   . ARG B 408 ? 0.5601 0.4975 0.5864 -0.0606 0.1143  -0.1781 394 ARG B N   
7026 C CA  . ARG B 408 ? 0.4834 0.4301 0.5218 -0.0540 0.1275  -0.1880 394 ARG B CA  
7027 C C   . ARG B 408 ? 0.5128 0.4596 0.5803 -0.0411 0.1257  -0.1858 394 ARG B C   
7028 O O   . ARG B 408 ? 0.5955 0.5281 0.6696 -0.0354 0.1239  -0.1912 394 ARG B O   
7029 C CB  . ARG B 408 ? 0.5393 0.4770 0.5633 -0.0561 0.1368  -0.2045 394 ARG B CB  
7030 C CG  . ARG B 408 ? 0.7524 0.7045 0.7760 -0.0559 0.1522  -0.2145 394 ARG B CG  
7031 C CD  . ARG B 408 ? 0.7800 0.7231 0.7790 -0.0625 0.1603  -0.2294 394 ARG B CD  
7032 N NE  . ARG B 408 ? 0.9573 0.9087 0.9653 -0.0562 0.1764  -0.2444 394 ARG B NE  
7033 C CZ  . ARG B 408 ? 1.0473 1.0122 1.0427 -0.0625 0.1889  -0.2507 394 ARG B CZ  
7034 N NH1 . ARG B 408 ? 0.8884 0.8590 0.8607 -0.0756 0.1866  -0.2427 394 ARG B NH1 
7035 N NH2 . ARG B 408 ? 0.9463 0.9194 0.9529 -0.0554 0.2040  -0.2654 394 ARG B NH2 
7036 N N   . LEU B 409 ? 0.5189 0.4810 0.6031 -0.0371 0.1256  -0.1775 395 LEU B N   
7037 C CA  . LEU B 409 ? 0.5081 0.4705 0.6181 -0.0259 0.1210  -0.1724 395 LEU B CA  
7038 C C   . LEU B 409 ? 0.5948 0.5597 0.7234 -0.0151 0.1307  -0.1840 395 LEU B C   
7039 O O   . LEU B 409 ? 0.5712 0.5504 0.7024 -0.0150 0.1419  -0.1914 395 LEU B O   
7040 C CB  . LEU B 409 ? 0.4381 0.4158 0.5587 -0.0258 0.1166  -0.1598 395 LEU B CB  
7041 C CG  . LEU B 409 ? 0.4597 0.4359 0.5639 -0.0352 0.1074  -0.1484 395 LEU B CG  
7042 C CD1 . LEU B 409 ? 0.3846 0.3755 0.4986 -0.0351 0.1045  -0.1379 395 LEU B CD1 
7043 C CD2 . LEU B 409 ? 0.4470 0.4075 0.5484 -0.0349 0.0968  -0.1434 395 LEU B CD2 
7044 N N   . PRO B 410 ? 0.7004 0.6520 0.8428 -0.0060 0.1267  -0.1858 396 PRO B N   
7045 C CA  . PRO B 410 ? 0.5555 0.5098 0.7198 0.0064  0.1343  -0.1953 396 PRO B CA  
7046 C C   . PRO B 410 ? 0.5862 0.5595 0.7755 0.0139  0.1333  -0.1875 396 PRO B C   
7047 O O   . PRO B 410 ? 0.6044 0.5884 0.7917 0.0084  0.1279  -0.1757 396 PRO B O   
7048 C CB  . PRO B 410 ? 0.4689 0.3996 0.6374 0.0123  0.1276  -0.1970 396 PRO B CB  
7049 C CG  . PRO B 410 ? 0.4563 0.3796 0.6158 0.0056  0.1146  -0.1827 396 PRO B CG  
7050 C CD  . PRO B 410 ? 0.4733 0.4062 0.6117 -0.0069 0.1150  -0.1791 396 PRO B CD  
7051 N N   . ALA B 411 ? 0.5772 0.5542 0.7904 0.0264  0.1379  -0.1939 397 ALA B N   
7052 C CA  . ALA B 411 ? 0.5330 0.5297 0.7716 0.0338  0.1370  -0.1875 397 ALA B CA  
7053 C C   . ALA B 411 ? 0.5020 0.4930 0.7478 0.0359  0.1225  -0.1720 397 ALA B C   
7054 O O   . ALA B 411 ? 0.5531 0.5237 0.7911 0.0355  0.1142  -0.1680 397 ALA B O   
7055 C CB  . ALA B 411 ? 0.4308 0.4322 0.6947 0.0479  0.1445  -0.1987 397 ALA B CB  
7056 N N   . ASP B 412 ? 0.4678 0.4778 0.7278 0.0371  0.1196  -0.1633 398 ASP B N   
7057 C CA  . ASP B 412 ? 0.4846 0.4926 0.7542 0.0403  0.1068  -0.1494 398 ASP B CA  
7058 C C   . ASP B 412 ? 0.5246 0.5189 0.7722 0.0308  0.0978  -0.1398 398 ASP B C   
7059 O O   . ASP B 412 ? 0.4527 0.4341 0.7021 0.0334  0.0881  -0.1319 398 ASP B O   
7060 C CB  . ASP B 412 ? 0.4244 0.4212 0.7139 0.0537  0.1022  -0.1502 398 ASP B CB  
7061 C CG  . ASP B 412 ? 0.7835 0.7909 1.0946 0.0644  0.1120  -0.1624 398 ASP B CG  
7062 O OD1 . ASP B 412 ? 0.8612 0.8930 1.1836 0.0642  0.1185  -0.1642 398 ASP B OD1 
7063 O OD2 . ASP B 412 ? 1.0418 1.0334 1.3593 0.0730  0.1135  -0.1703 398 ASP B OD2 
7064 N N   . VAL B 413 ? 0.4485 0.4461 0.6756 0.0195  0.1010  -0.1404 399 VAL B N   
7065 C CA  . VAL B 413 ? 0.4800 0.4678 0.6876 0.0105  0.0930  -0.1317 399 VAL B CA  
7066 C C   . VAL B 413 ? 0.4572 0.4599 0.6638 0.0053  0.0894  -0.1219 399 VAL B C   
7067 O O   . VAL B 413 ? 0.4613 0.4788 0.6668 0.0012  0.0960  -0.1245 399 VAL B O   
7068 C CB  . VAL B 413 ? 0.5192 0.4975 0.7033 0.0017  0.0973  -0.1389 399 VAL B CB  
7069 C CG1 . VAL B 413 ? 0.4749 0.4488 0.6409 -0.0079 0.0894  -0.1296 399 VAL B CG1 
7070 C CG2 . VAL B 413 ? 0.3947 0.3542 0.5778 0.0058  0.0984  -0.1475 399 VAL B CG2 
7071 N N   . ASN B 414 ? 0.4177 0.4161 0.6242 0.0050  0.0792  -0.1109 400 ASN B N   
7072 C CA  . ASN B 414 ? 0.3769 0.3852 0.5791 -0.0006 0.0746  -0.1018 400 ASN B CA  
7073 C C   . ASN B 414 ? 0.5301 0.5294 0.7100 -0.0098 0.0714  -0.0989 400 ASN B C   
7074 O O   . ASN B 414 ? 0.4611 0.4481 0.6355 -0.0101 0.0651  -0.0950 400 ASN B O   
7075 C CB  . ASN B 414 ? 0.3650 0.3746 0.5798 0.0047  0.0657  -0.0922 400 ASN B CB  
7076 C CG  . ASN B 414 ? 0.4086 0.4293 0.6209 -0.0002 0.0617  -0.0843 400 ASN B CG  
7077 O OD1 . ASN B 414 ? 0.4063 0.4301 0.6050 -0.0082 0.0638  -0.0843 400 ASN B OD1 
7078 N ND2 . ASN B 414 ? 0.4275 0.4532 0.6520 0.0042  0.0552  -0.0774 400 ASN B ND2 
7079 N N   . PHE B 415 ? 0.3989 0.4049 0.5665 -0.0174 0.0755  -0.1004 401 PHE B N   
7080 C CA  . PHE B 415 ? 0.4344 0.4331 0.5812 -0.0260 0.0724  -0.0981 401 PHE B CA  
7081 C C   . PHE B 415 ? 0.4941 0.4993 0.6377 -0.0299 0.0668  -0.0887 401 PHE B C   
7082 O O   . PHE B 415 ? 0.3813 0.3976 0.5262 -0.0329 0.0703  -0.0882 401 PHE B O   
7083 C CB  . PHE B 415 ? 0.3925 0.3916 0.5253 -0.0321 0.0806  -0.1065 401 PHE B CB  
7084 C CG  . PHE B 415 ? 0.4225 0.4134 0.5335 -0.0407 0.0766  -0.1044 401 PHE B CG  
7085 C CD1 . PHE B 415 ? 0.4091 0.4050 0.5091 -0.0477 0.0744  -0.0985 401 PHE B CD1 
7086 C CD2 . PHE B 415 ? 0.4735 0.4515 0.5754 -0.0420 0.0746  -0.1083 401 PHE B CD2 
7087 C CE1 . PHE B 415 ? 0.4289 0.4173 0.5098 -0.0549 0.0697  -0.0961 401 PHE B CE1 
7088 C CE2 . PHE B 415 ? 0.5270 0.4989 0.6101 -0.0499 0.0700  -0.1062 401 PHE B CE2 
7089 C CZ  . PHE B 415 ? 0.3764 0.3538 0.4494 -0.0559 0.0673  -0.0999 401 PHE B CZ  
7090 N N   . ILE B 416 ? 0.3763 0.3745 0.5161 -0.0302 0.0585  -0.0817 402 ILE B N   
7091 C CA  . ILE B 416 ? 0.3376 0.3403 0.4761 -0.0322 0.0526  -0.0734 402 ILE B CA  
7092 C C   . ILE B 416 ? 0.4296 0.4265 0.5506 -0.0390 0.0489  -0.0707 402 ILE B C   
7093 O O   . ILE B 416 ? 0.3646 0.3532 0.4802 -0.0393 0.0448  -0.0698 402 ILE B O   
7094 C CB  . ILE B 416 ? 0.3421 0.3431 0.4909 -0.0266 0.0462  -0.0674 402 ILE B CB  
7095 C CG1 . ILE B 416 ? 0.3220 0.3306 0.4886 -0.0200 0.0481  -0.0682 402 ILE B CG1 
7096 C CG2 . ILE B 416 ? 0.3735 0.3759 0.5168 -0.0293 0.0400  -0.0599 402 ILE B CG2 
7097 C CD1 . ILE B 416 ? 0.3089 0.3130 0.4845 -0.0141 0.0422  -0.0632 402 ILE B CD1 
7098 N N   . VAL B 417 ? 0.4031 0.4045 0.5160 -0.0445 0.0499  -0.0690 403 VAL B N   
7099 C CA  . VAL B 417 ? 0.3470 0.3428 0.4437 -0.0506 0.0454  -0.0657 403 VAL B CA  
7100 C C   . VAL B 417 ? 0.4592 0.4592 0.5540 -0.0535 0.0429  -0.0600 403 VAL B C   
7101 O O   . VAL B 417 ? 0.3060 0.3144 0.4084 -0.0538 0.0469  -0.0604 403 VAL B O   
7102 C CB  . VAL B 417 ? 0.3583 0.3506 0.4405 -0.0565 0.0498  -0.0712 403 VAL B CB  
7103 C CG1 . VAL B 417 ? 0.3769 0.3770 0.4563 -0.0610 0.0574  -0.0740 403 VAL B CG1 
7104 C CG2 . VAL B 417 ? 0.5187 0.5037 0.5855 -0.0614 0.0430  -0.0673 403 VAL B CG2 
7105 N N   . GLN B 418 ? 0.4399 0.4341 0.5255 -0.0557 0.0360  -0.0547 404 GLN B N   
7106 C CA  . GLN B 418 ? 0.3429 0.3378 0.4266 -0.0577 0.0321  -0.0491 404 GLN B CA  
7107 C C   . GLN B 418 ? 0.3507 0.3388 0.4175 -0.0642 0.0289  -0.0464 404 GLN B C   
7108 O O   . GLN B 418 ? 0.4010 0.3832 0.4633 -0.0634 0.0217  -0.0420 404 GLN B O   
7109 C CB  . GLN B 418 ? 0.3438 0.3372 0.4348 -0.0522 0.0258  -0.0452 404 GLN B CB  
7110 C CG  . GLN B 418 ? 0.4227 0.4166 0.5140 -0.0530 0.0221  -0.0407 404 GLN B CG  
7111 C CD  . GLN B 418 ? 0.3850 0.3751 0.4782 -0.0484 0.0158  -0.0375 404 GLN B CD  
7112 O OE1 . GLN B 418 ? 0.3922 0.3772 0.4799 -0.0476 0.0122  -0.0366 404 GLN B OE1 
7113 N NE2 . GLN B 418 ? 0.2986 0.2922 0.3997 -0.0455 0.0145  -0.0361 404 GLN B NE2 
7114 N N   . PRO B 419 ? 0.3897 0.3787 0.4467 -0.0707 0.0341  -0.0488 405 PRO B N   
7115 C CA  . PRO B 419 ? 0.3591 0.3404 0.3979 -0.0773 0.0303  -0.0456 405 PRO B CA  
7116 C C   . PRO B 419 ? 0.4076 0.3859 0.4405 -0.0819 0.0269  -0.0394 405 PRO B C   
7117 O O   . PRO B 419 ? 0.3940 0.3636 0.4124 -0.0862 0.0214  -0.0350 405 PRO B O   
7118 C CB  . PRO B 419 ? 0.4285 0.4121 0.4578 -0.0831 0.0382  -0.0512 405 PRO B CB  
7119 C CG  . PRO B 419 ? 0.5610 0.5546 0.6059 -0.0789 0.0468  -0.0575 405 PRO B CG  
7120 C CD  . PRO B 419 ? 0.4107 0.4083 0.4727 -0.0722 0.0437  -0.0546 405 PRO B CD  
7121 N N   . LEU B 420 ? 0.4182 0.4027 0.4612 -0.0816 0.0295  -0.0386 406 LEU B N   
7122 C CA  . LEU B 420 ? 0.3465 0.3263 0.3836 -0.0865 0.0256  -0.0328 406 LEU B CA  
7123 C C   . LEU B 420 ? 0.3486 0.3205 0.3883 -0.0809 0.0164  -0.0287 406 LEU B C   
7124 O O   . LEU B 420 ? 0.3708 0.3321 0.3994 -0.0830 0.0097  -0.0240 406 LEU B O   
7125 C CB  . LEU B 420 ? 0.3474 0.3374 0.3943 -0.0896 0.0315  -0.0338 406 LEU B CB  
7126 C CG  . LEU B 420 ? 0.4131 0.3976 0.4561 -0.0948 0.0269  -0.0279 406 LEU B CG  
7127 C CD1 . LEU B 420 ? 0.3797 0.3525 0.4027 -0.1031 0.0237  -0.0229 406 LEU B CD1 
7128 C CD2 . LEU B 420 ? 0.3445 0.3415 0.3984 -0.0989 0.0328  -0.0292 406 LEU B CD2 
7129 N N   . TRP B 421 ? 0.3329 0.3099 0.3870 -0.0736 0.0159  -0.0305 407 TRP B N   
7130 C CA  . TRP B 421 ? 0.4449 0.4156 0.5011 -0.0680 0.0084  -0.0278 407 TRP B CA  
7131 C C   . TRP B 421 ? 0.3748 0.3407 0.4267 -0.0645 0.0044  -0.0277 407 TRP B C   
7132 O O   . TRP B 421 ? 0.4109 0.3685 0.4566 -0.0635 -0.0024 -0.0244 407 TRP B O   
7133 C CB  . TRP B 421 ? 0.3532 0.3308 0.4238 -0.0620 0.0093  -0.0295 407 TRP B CB  
7134 C CG  . TRP B 421 ? 0.4607 0.4326 0.5323 -0.0573 0.0028  -0.0274 407 TRP B CG  
7135 C CD1 . TRP B 421 ? 0.4028 0.3767 0.4814 -0.0504 0.0012  -0.0285 407 TRP B CD1 
7136 C CD2 . TRP B 421 ? 0.3016 0.2643 0.3666 -0.0593 -0.0025 -0.0243 407 TRP B CD2 
7137 N NE1 . TRP B 421 ? 0.3828 0.3507 0.4595 -0.0477 -0.0040 -0.0269 407 TRP B NE1 
7138 C CE2 . TRP B 421 ? 0.3615 0.3217 0.4302 -0.0526 -0.0067 -0.0246 407 TRP B CE2 
7139 C CE3 . TRP B 421 ? 0.3904 0.3461 0.4461 -0.0664 -0.0040 -0.0213 407 TRP B CE3 
7140 C CZ2 . TRP B 421 ? 0.3338 0.2841 0.3977 -0.0519 -0.0122 -0.0230 407 TRP B CZ2 
7141 C CZ3 . TRP B 421 ? 0.4172 0.3617 0.4679 -0.0661 -0.0103 -0.0189 407 TRP B CZ3 
7142 C CH2 . TRP B 421 ? 0.3689 0.3106 0.4240 -0.0585 -0.0143 -0.0202 407 TRP B CH2 
7143 N N   . GLY B 422 ? 0.3539 0.3249 0.4094 -0.0627 0.0082  -0.0316 408 GLY B N   
7144 C CA  . GLY B 422 ? 0.3313 0.2990 0.3825 -0.0613 0.0047  -0.0319 408 GLY B CA  
7145 C C   . GLY B 422 ? 0.3658 0.3327 0.4237 -0.0547 -0.0009 -0.0305 408 GLY B C   
7146 O O   . GLY B 422 ? 0.3940 0.3567 0.4469 -0.0542 -0.0068 -0.0285 408 GLY B O   
7147 N N   . SER B 423 ? 0.3741 0.3458 0.4434 -0.0497 0.0007  -0.0316 409 SER B N   
7148 C CA  . SER B 423 ? 0.4104 0.3829 0.4860 -0.0439 -0.0031 -0.0306 409 SER B CA  
7149 C C   . SER B 423 ? 0.3673 0.3441 0.4485 -0.0422 -0.0014 -0.0329 409 SER B C   
7150 O O   . SER B 423 ? 0.3652 0.3457 0.4529 -0.0413 0.0030  -0.0350 409 SER B O   
7151 C CB  . SER B 423 ? 0.3196 0.2943 0.4019 -0.0406 -0.0024 -0.0302 409 SER B CB  
7152 O OG  . SER B 423 ? 0.3619 0.3368 0.4479 -0.0355 -0.0057 -0.0296 409 SER B OG  
7153 N N   . ILE B 424 ? 0.3203 0.2964 0.3998 -0.0419 -0.0056 -0.0323 410 ILE B N   
7154 C CA  . ILE B 424 ? 0.3450 0.3249 0.4299 -0.0415 -0.0045 -0.0343 410 ILE B CA  
7155 C C   . ILE B 424 ? 0.3440 0.3287 0.4392 -0.0369 -0.0032 -0.0338 410 ILE B C   
7156 O O   . ILE B 424 ? 0.3142 0.2999 0.4117 -0.0333 -0.0049 -0.0321 410 ILE B O   
7157 C CB  . ILE B 424 ? 0.3293 0.3089 0.4109 -0.0430 -0.0100 -0.0336 410 ILE B CB  
7158 C CG1 . ILE B 424 ? 0.3350 0.3164 0.4206 -0.0384 -0.0155 -0.0308 410 ILE B CG1 
7159 C CG2 . ILE B 424 ? 0.3287 0.3030 0.3975 -0.0486 -0.0115 -0.0338 410 ILE B CG2 
7160 C CD1 . ILE B 424 ? 0.3080 0.2935 0.3969 -0.0383 -0.0206 -0.0304 410 ILE B CD1 
7161 N N   . GLY B 425 ? 0.3778 0.3645 0.4781 -0.0373 0.0000  -0.0355 411 GLY B N   
7162 C CA  . GLY B 425 ? 0.3549 0.3450 0.4631 -0.0342 0.0020  -0.0344 411 GLY B CA  
7163 C C   . GLY B 425 ? 0.3946 0.3837 0.5052 -0.0332 0.0057  -0.0347 411 GLY B C   
7164 O O   . GLY B 425 ? 0.3144 0.3050 0.4306 -0.0313 0.0071  -0.0336 411 GLY B O   
7165 N N   . TYR B 426 ? 0.3626 0.3500 0.4694 -0.0347 0.0070  -0.0359 412 TYR B N   
7166 C CA  . TYR B 426 ? 0.3408 0.3297 0.4521 -0.0334 0.0101  -0.0363 412 TYR B CA  
7167 C C   . TYR B 426 ? 0.3336 0.3217 0.4509 -0.0325 0.0133  -0.0382 412 TYR B C   
7168 O O   . TYR B 426 ? 0.3797 0.3691 0.5036 -0.0296 0.0137  -0.0366 412 TYR B O   
7169 C CB  . TYR B 426 ? 0.3650 0.3535 0.4716 -0.0363 0.0117  -0.0376 412 TYR B CB  
7170 C CG  . TYR B 426 ? 0.2748 0.2669 0.3879 -0.0358 0.0159  -0.0395 412 TYR B CG  
7171 C CD1 . TYR B 426 ? 0.3007 0.2969 0.4197 -0.0338 0.0152  -0.0375 412 TYR B CD1 
7172 C CD2 . TYR B 426 ? 0.3137 0.3057 0.4277 -0.0370 0.0206  -0.0437 412 TYR B CD2 
7173 C CE1 . TYR B 426 ? 0.3853 0.3867 0.5126 -0.0328 0.0184  -0.0390 412 TYR B CE1 
7174 C CE2 . TYR B 426 ? 0.4023 0.3990 0.5246 -0.0354 0.0248  -0.0459 412 TYR B CE2 
7175 C CZ  . TYR B 426 ? 0.3320 0.3340 0.4619 -0.0331 0.0235  -0.0433 412 TYR B CZ  
7176 O OH  . TYR B 426 ? 0.2999 0.3085 0.4404 -0.0311 0.0270  -0.0454 412 TYR B OH  
7177 N N   . THR B 427 ? 0.2767 0.2615 0.3910 -0.0351 0.0149  -0.0416 413 THR B N   
7178 C CA  . THR B 427 ? 0.4916 0.4737 0.6111 -0.0340 0.0185  -0.0446 413 THR B CA  
7179 C C   . THR B 427 ? 0.3474 0.3274 0.4730 -0.0319 0.0170  -0.0420 413 THR B C   
7180 O O   . THR B 427 ? 0.3610 0.3393 0.4936 -0.0289 0.0185  -0.0419 413 THR B O   
7181 C CB  . THR B 427 ? 0.4497 0.4275 0.5630 -0.0378 0.0206  -0.0498 413 THR B CB  
7182 O OG1 . THR B 427 ? 0.5689 0.5426 0.6817 -0.0394 0.0185  -0.0499 413 THR B OG1 
7183 C CG2 . THR B 427 ? 0.2914 0.2704 0.3949 -0.0415 0.0195  -0.0499 413 THR B CG2 
7184 N N   . LEU B 428 ? 0.3397 0.3200 0.4633 -0.0336 0.0141  -0.0397 414 LEU B N   
7185 C CA  . LEU B 428 ? 0.3876 0.3662 0.5160 -0.0331 0.0133  -0.0367 414 LEU B CA  
7186 C C   . LEU B 428 ? 0.3976 0.3784 0.5304 -0.0293 0.0130  -0.0326 414 LEU B C   
7187 O O   . LEU B 428 ? 0.3064 0.2832 0.4439 -0.0276 0.0133  -0.0310 414 LEU B O   
7188 C CB  . LEU B 428 ? 0.2738 0.2559 0.4007 -0.0357 0.0108  -0.0348 414 LEU B CB  
7189 C CG  . LEU B 428 ? 0.4444 0.4257 0.5754 -0.0370 0.0106  -0.0314 414 LEU B CG  
7190 C CD1 . LEU B 428 ? 0.3675 0.3398 0.5001 -0.0393 0.0118  -0.0337 414 LEU B CD1 
7191 C CD2 . LEU B 428 ? 0.3167 0.3050 0.4481 -0.0395 0.0088  -0.0300 414 LEU B CD2 
7192 N N   . ALA B 429 ? 0.3198 0.3060 0.4505 -0.0279 0.0117  -0.0310 415 ALA B N   
7193 C CA  . ALA B 429 ? 0.3578 0.3463 0.4911 -0.0250 0.0106  -0.0275 415 ALA B CA  
7194 C C   . ALA B 429 ? 0.3865 0.3748 0.5250 -0.0227 0.0117  -0.0288 415 ALA B C   
7195 O O   . ALA B 429 ? 0.3612 0.3492 0.5047 -0.0200 0.0105  -0.0259 415 ALA B O   
7196 C CB  . ALA B 429 ? 0.2890 0.2821 0.4178 -0.0246 0.0087  -0.0264 415 ALA B CB  
7197 N N   . ALA B 430 ? 0.2651 0.2543 0.4029 -0.0237 0.0139  -0.0330 416 ALA B N   
7198 C CA  . ALA B 430 ? 0.3206 0.3119 0.4652 -0.0215 0.0161  -0.0352 416 ALA B CA  
7199 C C   . ALA B 430 ? 0.3870 0.3730 0.5385 -0.0189 0.0177  -0.0365 416 ALA B C   
7200 O O   . ALA B 430 ? 0.2793 0.2673 0.4399 -0.0149 0.0179  -0.0363 416 ALA B O   
7201 C CB  . ALA B 430 ? 0.2145 0.2081 0.3555 -0.0244 0.0194  -0.0396 416 ALA B CB  
7202 N N   . ALA B 431 ? 0.3365 0.3157 0.4845 -0.0209 0.0184  -0.0380 417 ALA B N   
7203 C CA  . ALA B 431 ? 0.3237 0.2950 0.4772 -0.0189 0.0194  -0.0394 417 ALA B CA  
7204 C C   . ALA B 431 ? 0.3727 0.3415 0.5314 -0.0159 0.0158  -0.0331 417 ALA B C   
7205 O O   . ALA B 431 ? 0.3358 0.3000 0.5025 -0.0116 0.0156  -0.0331 417 ALA B O   
7206 C CB  . ALA B 431 ? 0.3033 0.2676 0.4507 -0.0233 0.0199  -0.0419 417 ALA B CB  
7207 N N   . PHE B 432 ? 0.3320 0.3033 0.4858 -0.0178 0.0128  -0.0276 418 PHE B N   
7208 C CA  . PHE B 432 ? 0.3277 0.2975 0.4838 -0.0158 0.0093  -0.0209 418 PHE B CA  
7209 C C   . PHE B 432 ? 0.3721 0.3469 0.5354 -0.0111 0.0075  -0.0198 418 PHE B C   
7210 O O   . PHE B 432 ? 0.3529 0.3237 0.5224 -0.0075 0.0047  -0.0161 418 PHE B O   
7211 C CB  . PHE B 432 ? 0.2517 0.2257 0.4002 -0.0191 0.0076  -0.0166 418 PHE B CB  
7212 C CG  . PHE B 432 ? 0.2892 0.2629 0.4367 -0.0180 0.0041  -0.0097 418 PHE B CG  
7213 C CD1 . PHE B 432 ? 0.2387 0.2040 0.3873 -0.0185 0.0025  -0.0050 418 PHE B CD1 
7214 C CD2 . PHE B 432 ? 0.2481 0.2289 0.3924 -0.0172 0.0021  -0.0078 418 PHE B CD2 
7215 C CE1 . PHE B 432 ? 0.2791 0.2436 0.4248 -0.0182 -0.0012 0.0022  418 PHE B CE1 
7216 C CE2 . PHE B 432 ? 0.3026 0.2832 0.4440 -0.0169 -0.0015 -0.0015 418 PHE B CE2 
7217 C CZ  . PHE B 432 ? 0.2454 0.2180 0.3872 -0.0174 -0.0032 0.0039  418 PHE B CZ  
7218 N N   . GLY B 433 ? 0.2772 0.2606 0.4403 -0.0112 0.0085  -0.0225 419 GLY B N   
7219 C CA  . GLY B 433 ? 0.2824 0.2725 0.4538 -0.0076 0.0068  -0.0219 419 GLY B CA  
7220 C C   . GLY B 433 ? 0.2640 0.2533 0.4473 -0.0031 0.0093  -0.0259 419 GLY B C   
7221 O O   . GLY B 433 ? 0.2649 0.2558 0.4583 0.0017  0.0062  -0.0233 419 GLY B O   
7222 N N   . ALA B 434 ? 0.2499 0.2369 0.4322 -0.0044 0.0146  -0.0325 420 ALA B N   
7223 C CA  . ALA B 434 ? 0.2949 0.2811 0.4880 0.0000  0.0183  -0.0380 420 ALA B CA  
7224 C C   . ALA B 434 ? 0.3861 0.3610 0.5852 0.0045  0.0158  -0.0358 420 ALA B C   
7225 O O   . ALA B 434 ? 0.3824 0.3582 0.5946 0.0110  0.0153  -0.0365 420 ALA B O   
7226 C CB  . ALA B 434 ? 0.2797 0.2643 0.4670 -0.0034 0.0247  -0.0458 420 ALA B CB  
7227 N N   . GLN B 435 ? 0.3123 0.2767 0.5027 0.0011  0.0141  -0.0328 421 GLN B N   
7228 C CA  . GLN B 435 ? 0.3371 0.2887 0.5316 0.0041  0.0112  -0.0297 421 GLN B CA  
7229 C C   . GLN B 435 ? 0.3410 0.2942 0.5413 0.0081  0.0047  -0.0213 421 GLN B C   
7230 O O   . GLN B 435 ? 0.4039 0.3495 0.6135 0.0138  0.0019  -0.0195 421 GLN B O   
7231 C CB  . GLN B 435 ? 0.3510 0.2926 0.5345 -0.0022 0.0107  -0.0275 421 GLN B CB  
7232 C CG  . GLN B 435 ? 0.3164 0.2422 0.5026 -0.0008 0.0080  -0.0245 421 GLN B CG  
7233 C CD  . GLN B 435 ? 0.4343 0.3500 0.6256 0.0019  0.0118  -0.0330 421 GLN B CD  
7234 O OE1 . GLN B 435 ? 0.4737 0.3823 0.6581 -0.0032 0.0143  -0.0375 421 GLN B OE1 
7235 N NE2 . GLN B 435 ? 0.4150 0.3304 0.6189 0.0102  0.0121  -0.0358 421 GLN B NE2 
7236 N N   . THR B 436 ? 0.2924 0.2545 0.4867 0.0053  0.0018  -0.0163 422 THR B N   
7237 C CA  . THR B 436 ? 0.3139 0.2791 0.5122 0.0085  -0.0048 -0.0088 422 THR B CA  
7238 C C   . THR B 436 ? 0.3991 0.3722 0.6136 0.0155  -0.0056 -0.0114 422 THR B C   
7239 O O   . THR B 436 ? 0.3196 0.2902 0.5430 0.0209  -0.0113 -0.0064 422 THR B O   
7240 C CB  . THR B 436 ? 0.3577 0.3317 0.5458 0.0038  -0.0068 -0.0052 422 THR B CB  
7241 O OG1 . THR B 436 ? 0.3286 0.2973 0.5038 -0.0021 -0.0055 -0.0033 422 THR B OG1 
7242 C CG2 . THR B 436 ? 0.3169 0.2940 0.5068 0.0061  -0.0143 0.0025  422 THR B CG2 
7243 N N   . ALA B 437 ? 0.3380 0.3213 0.5567 0.0153  -0.0001 -0.0189 423 ALA B N   
7244 C CA  . ALA B 437 ? 0.3627 0.3563 0.5983 0.0213  0.0006  -0.0223 423 ALA B CA  
7245 C C   . ALA B 437 ? 0.3662 0.3516 0.6143 0.0285  0.0024  -0.0263 423 ALA B C   
7246 O O   . ALA B 437 ? 0.3589 0.3487 0.6232 0.0360  -0.0008 -0.0253 423 ALA B O   
7247 C CB  . ALA B 437 ? 0.2899 0.2960 0.5253 0.0177  0.0071  -0.0293 423 ALA B CB  
7248 N N   . CYS B 438 ? 0.4186 0.3917 0.6597 0.0267  0.0072  -0.0311 424 CYS B N   
7249 C CA  . CYS B 438 ? 0.4064 0.3699 0.6577 0.0331  0.0102  -0.0371 424 CYS B CA  
7250 C C   . CYS B 438 ? 0.4665 0.4097 0.7091 0.0313  0.0075  -0.0336 424 CYS B C   
7251 O O   . CYS B 438 ? 0.3900 0.3241 0.6244 0.0273  0.0123  -0.0395 424 CYS B O   
7252 C CB  . CYS B 438 ? 0.3359 0.3047 0.5874 0.0318  0.0200  -0.0487 424 CYS B CB  
7253 S SG  . CYS B 438 ? 0.4332 0.4265 0.6937 0.0316  0.0241  -0.0522 424 CYS B SG  
7254 N N   . PRO B 439 ? 0.4180 0.3534 0.6619 0.0334  -0.0007 -0.0239 425 PRO B N   
7255 C CA  . PRO B 439 ? 0.4610 0.3769 0.6958 0.0302  -0.0034 -0.0194 425 PRO B CA  
7256 C C   . PRO B 439 ? 0.4998 0.3996 0.7411 0.0348  -0.0008 -0.0262 425 PRO B C   
7257 O O   . PRO B 439 ? 0.5302 0.4138 0.7624 0.0299  -0.0012 -0.0251 425 PRO B O   
7258 C CB  . PRO B 439 ? 0.4285 0.3411 0.6642 0.0321  -0.0130 -0.0070 425 PRO B CB  
7259 C CG  . PRO B 439 ? 0.5658 0.4923 0.8174 0.0402  -0.0156 -0.0073 425 PRO B CG  
7260 C CD  . PRO B 439 ? 0.4246 0.3686 0.6775 0.0382  -0.0081 -0.0162 425 PRO B CD  
7261 N N   . ASN B 440 ? 0.4590 0.3628 0.7162 0.0438  0.0022  -0.0337 426 ASN B N   
7262 C CA  . ASN B 440 ? 0.6664 0.5540 0.9307 0.0494  0.0050  -0.0413 426 ASN B CA  
7263 C C   . ASN B 440 ? 0.5606 0.4507 0.8208 0.0468  0.0153  -0.0550 426 ASN B C   
7264 O O   . ASN B 440 ? 0.5997 0.4781 0.8659 0.0520  0.0190  -0.0638 426 ASN B O   
7265 C CB  . ASN B 440 ? 0.4884 0.3771 0.7742 0.0625  0.0018  -0.0417 426 ASN B CB  
7266 C CG  . ASN B 440 ? 0.5871 0.4702 0.8760 0.0653  -0.0098 -0.0277 426 ASN B CG  
7267 O OD1 . ASN B 440 ? 0.6512 0.5202 0.9265 0.0588  -0.0148 -0.0189 426 ASN B OD1 
7268 N ND2 . ASN B 440 ? 0.6048 0.4998 0.9115 0.0745  -0.0141 -0.0252 426 ASN B ND2 
7269 N N   . ARG B 441 ? 0.4450 0.3491 0.6946 0.0391  0.0196  -0.0570 427 ARG B N   
7270 C CA  . ARG B 441 ? 0.4953 0.4022 0.7383 0.0353  0.0286  -0.0688 427 ARG B CA  
7271 C C   . ARG B 441 ? 0.5359 0.4348 0.7598 0.0244  0.0285  -0.0678 427 ARG B C   
7272 O O   . ARG B 441 ? 0.4438 0.3439 0.6597 0.0187  0.0234  -0.0584 427 ARG B O   
7273 C CB  . ARG B 441 ? 0.3925 0.3222 0.6387 0.0349  0.0338  -0.0723 427 ARG B CB  
7274 C CG  . ARG B 441 ? 0.4286 0.3699 0.6959 0.0452  0.0349  -0.0746 427 ARG B CG  
7275 C CD  . ARG B 441 ? 0.4186 0.3824 0.6884 0.0428  0.0406  -0.0781 427 ARG B CD  
7276 N NE  . ARG B 441 ? 0.4210 0.3861 0.6806 0.0377  0.0501  -0.0887 427 ARG B NE  
7277 C CZ  . ARG B 441 ? 0.4340 0.4163 0.6954 0.0356  0.0573  -0.0942 427 ARG B CZ  
7278 N NH1 . ARG B 441 ? 0.4034 0.4038 0.6780 0.0381  0.0563  -0.0907 427 ARG B NH1 
7279 N NH2 . ARG B 441 ? 0.4009 0.3822 0.6501 0.0301  0.0655  -0.1032 427 ARG B NH2 
7280 N N   . ARG B 442 ? 0.4582 0.3501 0.6750 0.0213  0.0345  -0.0781 428 ARG B N   
7281 C CA  . ARG B 442 ? 0.5072 0.3926 0.7072 0.0109  0.0341  -0.0783 428 ARG B CA  
7282 C C   . ARG B 442 ? 0.5120 0.4144 0.7026 0.0045  0.0364  -0.0779 428 ARG B C   
7283 O O   . ARG B 442 ? 0.4527 0.3664 0.6448 0.0060  0.0423  -0.0845 428 ARG B O   
7284 C CB  . ARG B 442 ? 0.3627 0.2332 0.5576 0.0095  0.0386  -0.0896 428 ARG B CB  
7285 C CG  . ARG B 442 ? 0.4233 0.2865 0.6021 -0.0016 0.0370  -0.0898 428 ARG B CG  
7286 C CD  . ARG B 442 ? 0.4074 0.2526 0.5811 -0.0031 0.0399  -0.1006 428 ARG B CD  
7287 N NE  . ARG B 442 ? 0.4822 0.3340 0.6498 -0.0038 0.0477  -0.1126 428 ARG B NE  
7288 C CZ  . ARG B 442 ? 0.5611 0.4002 0.7201 -0.0069 0.0513  -0.1238 428 ARG B CZ  
7289 N NH1 . ARG B 442 ? 0.5064 0.3249 0.6627 -0.0096 0.0476  -0.1250 428 ARG B NH1 
7290 N NH2 . ARG B 442 ? 0.4538 0.3006 0.6058 -0.0079 0.0588  -0.1342 428 ARG B NH2 
7291 N N   . VAL B 443 ? 0.4636 0.3680 0.6450 -0.0025 0.0319  -0.0702 429 VAL B N   
7292 C CA  . VAL B 443 ? 0.3711 0.2898 0.5441 -0.0079 0.0326  -0.0684 429 VAL B CA  
7293 C C   . VAL B 443 ? 0.4332 0.3471 0.5927 -0.0165 0.0325  -0.0711 429 VAL B C   
7294 O O   . VAL B 443 ? 0.4265 0.3316 0.5829 -0.0205 0.0285  -0.0671 429 VAL B O   
7295 C CB  . VAL B 443 ? 0.4431 0.3703 0.6179 -0.0078 0.0273  -0.0577 429 VAL B CB  
7296 C CG1 . VAL B 443 ? 0.4407 0.3792 0.6058 -0.0136 0.0274  -0.0562 429 VAL B CG1 
7297 C CG2 . VAL B 443 ? 0.3972 0.3314 0.5849 0.0001  0.0267  -0.0553 429 VAL B CG2 
7298 N N   . ILE B 444 ? 0.4061 0.3262 0.5575 -0.0200 0.0364  -0.0774 430 ILE B N   
7299 C CA  . ILE B 444 ? 0.3404 0.2575 0.4786 -0.0283 0.0356  -0.0800 430 ILE B CA  
7300 C C   . ILE B 444 ? 0.4479 0.3781 0.5797 -0.0319 0.0337  -0.0754 430 ILE B C   
7301 O O   . ILE B 444 ? 0.4125 0.3520 0.5438 -0.0305 0.0369  -0.0768 430 ILE B O   
7302 C CB  . ILE B 444 ? 0.4001 0.3111 0.5316 -0.0299 0.0410  -0.0915 430 ILE B CB  
7303 C CG1 . ILE B 444 ? 0.3879 0.2833 0.5259 -0.0257 0.0424  -0.0968 430 ILE B CG1 
7304 C CG2 . ILE B 444 ? 0.3359 0.2457 0.4525 -0.0390 0.0390  -0.0937 430 ILE B CG2 
7305 C CD1 . ILE B 444 ? 0.3544 0.2455 0.4901 -0.0235 0.0499  -0.1094 430 ILE B CD1 
7306 N N   . VAL B 445 ? 0.4055 0.3366 0.5331 -0.0367 0.0287  -0.0699 431 VAL B N   
7307 C CA  . VAL B 445 ? 0.4001 0.3423 0.5232 -0.0392 0.0260  -0.0650 431 VAL B CA  
7308 C C   . VAL B 445 ? 0.4342 0.3757 0.5460 -0.0461 0.0242  -0.0680 431 VAL B C   
7309 O O   . VAL B 445 ? 0.4249 0.3617 0.5354 -0.0503 0.0211  -0.0678 431 VAL B O   
7310 C CB  . VAL B 445 ? 0.4018 0.3476 0.5300 -0.0383 0.0218  -0.0564 431 VAL B CB  
7311 C CG1 . VAL B 445 ? 0.3199 0.2766 0.4448 -0.0389 0.0197  -0.0524 431 VAL B CG1 
7312 C CG2 . VAL B 445 ? 0.3253 0.2692 0.4633 -0.0322 0.0224  -0.0531 431 VAL B CG2 
7313 N N   . LEU B 446 ? 0.4356 0.3823 0.5395 -0.0478 0.0256  -0.0703 432 LEU B N   
7314 C CA  . LEU B 446 ? 0.4720 0.4188 0.5639 -0.0543 0.0226  -0.0722 432 LEU B CA  
7315 C C   . LEU B 446 ? 0.4965 0.4524 0.5870 -0.0545 0.0182  -0.0655 432 LEU B C   
7316 O O   . LEU B 446 ? 0.4378 0.3982 0.5253 -0.0534 0.0197  -0.0644 432 LEU B O   
7317 C CB  . LEU B 446 ? 0.3666 0.3107 0.4480 -0.0569 0.0274  -0.0798 432 LEU B CB  
7318 C CG  . LEU B 446 ? 0.5508 0.4861 0.6350 -0.0548 0.0331  -0.0878 432 LEU B CG  
7319 C CD1 . LEU B 446 ? 0.4342 0.3708 0.5109 -0.0553 0.0402  -0.0951 432 LEU B CD1 
7320 C CD2 . LEU B 446 ? 0.4669 0.3922 0.5469 -0.0596 0.0301  -0.0914 432 LEU B CD2 
7321 N N   . THR B 447 ? 0.4688 0.4273 0.5621 -0.0561 0.0129  -0.0612 433 THR B N   
7322 C CA  . THR B 447 ? 0.3442 0.3107 0.4377 -0.0552 0.0086  -0.0555 433 THR B CA  
7323 C C   . THR B 447 ? 0.5035 0.4720 0.5929 -0.0601 0.0026  -0.0550 433 THR B C   
7324 O O   . THR B 447 ? 0.4020 0.3680 0.4933 -0.0637 0.0012  -0.0568 433 THR B O   
7325 C CB  . THR B 447 ? 0.3663 0.3374 0.4706 -0.0507 0.0083  -0.0502 433 THR B CB  
7326 O OG1 . THR B 447 ? 0.3337 0.3120 0.4383 -0.0495 0.0042  -0.0459 433 THR B OG1 
7327 C CG2 . THR B 447 ? 0.2917 0.2604 0.4024 -0.0524 0.0078  -0.0495 433 THR B CG2 
7328 N N   . GLY B 448 ? 0.3551 0.3278 0.4392 -0.0604 -0.0015 -0.0524 434 GLY B N   
7329 C CA  . GLY B 448 ? 0.3394 0.3162 0.4225 -0.0636 -0.0085 -0.0507 434 GLY B CA  
7330 C C   . GLY B 448 ? 0.3727 0.3577 0.4689 -0.0609 -0.0107 -0.0466 434 GLY B C   
7331 O O   . GLY B 448 ? 0.3283 0.3155 0.4318 -0.0563 -0.0073 -0.0443 434 GLY B O   
7332 N N   . ASP B 449 ? 0.3793 0.3698 0.4784 -0.0642 -0.0164 -0.0459 435 ASP B N   
7333 C CA  . ASP B 449 ? 0.3245 0.3254 0.4370 -0.0620 -0.0179 -0.0424 435 ASP B CA  
7334 C C   . ASP B 449 ? 0.3563 0.3630 0.4723 -0.0553 -0.0190 -0.0388 435 ASP B C   
7335 O O   . ASP B 449 ? 0.4009 0.4133 0.5257 -0.0515 -0.0162 -0.0367 435 ASP B O   
7336 C CB  . ASP B 449 ? 0.2993 0.3069 0.4159 -0.0673 -0.0241 -0.0426 435 ASP B CB  
7337 C CG  . ASP B 449 ? 0.3729 0.3806 0.4810 -0.0691 -0.0315 -0.0427 435 ASP B CG  
7338 O OD1 . ASP B 449 ? 0.3859 0.3859 0.4820 -0.0680 -0.0309 -0.0432 435 ASP B OD1 
7339 O OD2 . ASP B 449 ? 0.3582 0.3741 0.4715 -0.0720 -0.0382 -0.0418 435 ASP B OD2 
7340 N N   . GLY B 450 ? 0.3262 0.3308 0.4345 -0.0542 -0.0233 -0.0380 436 GLY B N   
7341 C CA  . GLY B 450 ? 0.3467 0.3539 0.4574 -0.0478 -0.0246 -0.0350 436 GLY B CA  
7342 C C   . GLY B 450 ? 0.3091 0.3123 0.4194 -0.0442 -0.0181 -0.0349 436 GLY B C   
7343 O O   . GLY B 450 ? 0.3441 0.3523 0.4618 -0.0394 -0.0166 -0.0334 436 GLY B O   
7344 N N   . ALA B 451 ? 0.3717 0.3670 0.4740 -0.0466 -0.0141 -0.0369 437 ALA B N   
7345 C CA  . ALA B 451 ? 0.3206 0.3132 0.4233 -0.0434 -0.0090 -0.0366 437 ALA B CA  
7346 C C   . ALA B 451 ? 0.3436 0.3400 0.4556 -0.0412 -0.0053 -0.0359 437 ALA B C   
7347 O O   . ALA B 451 ? 0.3002 0.2986 0.4153 -0.0372 -0.0037 -0.0342 437 ALA B O   
7348 C CB  . ALA B 451 ? 0.2895 0.2751 0.3843 -0.0464 -0.0050 -0.0395 437 ALA B CB  
7349 N N   . ALA B 452 ? 0.3807 0.3775 0.4965 -0.0445 -0.0042 -0.0371 438 ALA B N   
7350 C CA  . ALA B 452 ? 0.3605 0.3591 0.4834 -0.0436 -0.0008 -0.0356 438 ALA B CA  
7351 C C   . ALA B 452 ? 0.2833 0.2912 0.4130 -0.0408 -0.0015 -0.0327 438 ALA B C   
7352 O O   . ALA B 452 ? 0.3181 0.3275 0.4509 -0.0390 0.0016  -0.0307 438 ALA B O   
7353 C CB  . ALA B 452 ? 0.3079 0.3034 0.4327 -0.0488 -0.0003 -0.0372 438 ALA B CB  
7354 N N   . GLN B 453 ? 0.2850 0.2996 0.4170 -0.0401 -0.0055 -0.0326 439 GLN B N   
7355 C CA  . GLN B 453 ? 0.2852 0.3098 0.4248 -0.0365 -0.0054 -0.0311 439 GLN B CA  
7356 C C   . GLN B 453 ? 0.3232 0.3460 0.4600 -0.0311 -0.0034 -0.0305 439 GLN B C   
7357 O O   . GLN B 453 ? 0.3243 0.3533 0.4654 -0.0286 -0.0008 -0.0297 439 GLN B O   
7358 C CB  . GLN B 453 ? 0.3343 0.3663 0.4784 -0.0355 -0.0108 -0.0314 439 GLN B CB  
7359 C CG  . GLN B 453 ? 0.2638 0.2990 0.4109 -0.0415 -0.0140 -0.0321 439 GLN B CG  
7360 C CD  . GLN B 453 ? 0.3587 0.4050 0.5141 -0.0399 -0.0197 -0.0318 439 GLN B CD  
7361 O OE1 . GLN B 453 ? 0.3592 0.4066 0.5150 -0.0340 -0.0227 -0.0314 439 GLN B OE1 
7362 N NE2 . GLN B 453 ? 0.2656 0.3200 0.4285 -0.0451 -0.0218 -0.0320 439 GLN B NE2 
7363 N N   . LEU B 454 ? 0.3342 0.3487 0.4633 -0.0299 -0.0045 -0.0311 440 LEU B N   
7364 C CA  . LEU B 454 ? 0.3076 0.3199 0.4338 -0.0255 -0.0038 -0.0308 440 LEU B CA  
7365 C C   . LEU B 454 ? 0.3420 0.3537 0.4682 -0.0252 0.0005  -0.0298 440 LEU B C   
7366 O O   . LEU B 454 ? 0.3118 0.3244 0.4369 -0.0219 0.0013  -0.0296 440 LEU B O   
7367 C CB  . LEU B 454 ? 0.2464 0.2503 0.3645 -0.0259 -0.0062 -0.0311 440 LEU B CB  
7368 C CG  . LEU B 454 ? 0.3161 0.3191 0.4324 -0.0242 -0.0118 -0.0309 440 LEU B CG  
7369 C CD1 . LEU B 454 ? 0.2184 0.2226 0.3343 -0.0281 -0.0151 -0.0310 440 LEU B CD1 
7370 C CD2 . LEU B 454 ? 0.2809 0.2750 0.3887 -0.0239 -0.0137 -0.0303 440 LEU B CD2 
7371 N N   . THR B 455 ? 0.3044 0.3135 0.4312 -0.0285 0.0027  -0.0291 441 THR B N   
7372 C CA  . THR B 455 ? 0.2957 0.3027 0.4222 -0.0280 0.0055  -0.0273 441 THR B CA  
7373 C C   . THR B 455 ? 0.3145 0.3224 0.4449 -0.0310 0.0075  -0.0254 441 THR B C   
7374 O O   . THR B 455 ? 0.3174 0.3207 0.4476 -0.0314 0.0089  -0.0236 441 THR B O   
7375 C CB  . THR B 455 ? 0.3586 0.3590 0.4820 -0.0280 0.0058  -0.0282 441 THR B CB  
7376 O OG1 . THR B 455 ? 0.3368 0.3335 0.4602 -0.0310 0.0061  -0.0301 441 THR B OG1 
7377 C CG2 . THR B 455 ? 0.3168 0.3159 0.4358 -0.0263 0.0039  -0.0293 441 THR B CG2 
7378 N N   . ILE B 456 ? 0.2940 0.3078 0.4286 -0.0334 0.0074  -0.0253 442 ILE B N   
7379 C CA  . ILE B 456 ? 0.3344 0.3475 0.4724 -0.0380 0.0088  -0.0236 442 ILE B CA  
7380 C C   . ILE B 456 ? 0.2624 0.2749 0.3997 -0.0383 0.0114  -0.0195 442 ILE B C   
7381 O O   . ILE B 456 ? 0.2896 0.2964 0.4277 -0.0418 0.0122  -0.0172 442 ILE B O   
7382 C CB  . ILE B 456 ? 0.2773 0.2994 0.4212 -0.0411 0.0079  -0.0241 442 ILE B CB  
7383 C CG1 . ILE B 456 ? 0.2393 0.2583 0.3860 -0.0476 0.0085  -0.0230 442 ILE B CG1 
7384 C CG2 . ILE B 456 ? 0.2719 0.3054 0.4194 -0.0390 0.0100  -0.0229 442 ILE B CG2 
7385 C CD1 . ILE B 456 ? 0.3088 0.3155 0.4516 -0.0493 0.0073  -0.0253 442 ILE B CD1 
7386 N N   . GLN B 457 ? 0.3216 0.3388 0.4564 -0.0351 0.0125  -0.0185 443 GLN B N   
7387 C CA  . GLN B 457 ? 0.2819 0.2995 0.4142 -0.0363 0.0147  -0.0142 443 GLN B CA  
7388 C C   . GLN B 457 ? 0.3493 0.3566 0.4788 -0.0359 0.0134  -0.0114 443 GLN B C   
7389 O O   . GLN B 457 ? 0.2779 0.2826 0.4053 -0.0381 0.0141  -0.0067 443 GLN B O   
7390 C CB  . GLN B 457 ? 0.2539 0.2784 0.3825 -0.0330 0.0161  -0.0148 443 GLN B CB  
7391 C CG  . GLN B 457 ? 0.3217 0.3435 0.4470 -0.0281 0.0138  -0.0181 443 GLN B CG  
7392 C CD  . GLN B 457 ? 0.2377 0.2640 0.3662 -0.0255 0.0126  -0.0223 443 GLN B CD  
7393 O OE1 . GLN B 457 ? 0.2640 0.2861 0.3937 -0.0254 0.0100  -0.0240 443 GLN B OE1 
7394 N NE2 . GLN B 457 ? 0.1952 0.2298 0.3250 -0.0234 0.0146  -0.0240 443 GLN B NE2 
7395 N N   . GLU B 458 ? 0.3351 0.3368 0.4649 -0.0332 0.0115  -0.0141 444 GLU B N   
7396 C CA  . GLU B 458 ? 0.4137 0.4074 0.5435 -0.0318 0.0104  -0.0121 444 GLU B CA  
7397 C C   . GLU B 458 ? 0.4223 0.4081 0.5555 -0.0346 0.0105  -0.0108 444 GLU B C   
7398 O O   . GLU B 458 ? 0.2985 0.2771 0.4327 -0.0333 0.0093  -0.0079 444 GLU B O   
7399 C CB  . GLU B 458 ? 0.2697 0.2620 0.4001 -0.0284 0.0093  -0.0158 444 GLU B CB  
7400 C CG  . GLU B 458 ? 0.2964 0.2880 0.4263 -0.0253 0.0075  -0.0135 444 GLU B CG  
7401 C CD  . GLU B 458 ? 0.3851 0.3811 0.5094 -0.0252 0.0068  -0.0103 444 GLU B CD  
7402 O OE1 . GLU B 458 ? 0.3523 0.3535 0.4733 -0.0256 0.0080  -0.0122 444 GLU B OE1 
7403 O OE2 . GLU B 458 ? 0.3884 0.3825 0.5113 -0.0244 0.0048  -0.0062 444 GLU B OE2 
7404 N N   . LEU B 459 ? 0.3305 0.3167 0.4656 -0.0386 0.0114  -0.0128 445 LEU B N   
7405 C CA  . LEU B 459 ? 0.3337 0.3113 0.4710 -0.0425 0.0114  -0.0113 445 LEU B CA  
7406 C C   . LEU B 459 ? 0.3618 0.3372 0.4974 -0.0451 0.0115  -0.0043 445 LEU B C   
7407 O O   . LEU B 459 ? 0.3834 0.3476 0.5198 -0.0460 0.0103  -0.0013 445 LEU B O   
7408 C CB  . LEU B 459 ? 0.3922 0.3726 0.5315 -0.0475 0.0117  -0.0144 445 LEU B CB  
7409 C CG  . LEU B 459 ? 0.5359 0.5074 0.6770 -0.0534 0.0115  -0.0131 445 LEU B CG  
7410 C CD1 . LEU B 459 ? 0.4648 0.4217 0.6060 -0.0510 0.0107  -0.0153 445 LEU B CD1 
7411 C CD2 . LEU B 459 ? 0.4528 0.4294 0.5961 -0.0588 0.0109  -0.0165 445 LEU B CD2 
7412 N N   . GLY B 460 ? 0.3313 0.3166 0.4640 -0.0461 0.0130  -0.0016 446 GLY B N   
7413 C CA  . GLY B 460 ? 0.3230 0.3066 0.4514 -0.0488 0.0133  0.0055  446 GLY B CA  
7414 C C   . GLY B 460 ? 0.4152 0.3907 0.5408 -0.0446 0.0103  0.0091  446 GLY B C   
7415 O O   . GLY B 460 ? 0.3386 0.3056 0.4620 -0.0468 0.0086  0.0154  446 GLY B O   
7416 N N   . SER B 461 ? 0.2945 0.2727 0.4206 -0.0387 0.0089  0.0055  447 SER B N   
7417 C CA  . SER B 461 ? 0.3345 0.3069 0.4606 -0.0344 0.0054  0.0084  447 SER B CA  
7418 C C   . SER B 461 ? 0.3102 0.2705 0.4426 -0.0330 0.0036  0.0085  447 SER B C   
7419 O O   . SER B 461 ? 0.2991 0.2515 0.4317 -0.0317 0.0003  0.0141  447 SER B O   
7420 C CB  . SER B 461 ? 0.3386 0.3172 0.4654 -0.0296 0.0046  0.0038  447 SER B CB  
7421 O OG  . SER B 461 ? 0.3466 0.3339 0.4670 -0.0302 0.0056  0.0034  447 SER B OG  
7422 N N   . MET B 462 ? 0.2701 0.2284 0.4072 -0.0331 0.0055  0.0022  448 MET B N   
7423 C CA  . MET B 462 ? 0.2794 0.2254 0.4220 -0.0319 0.0047  0.0008  448 MET B CA  
7424 C C   . MET B 462 ? 0.3642 0.2995 0.5051 -0.0362 0.0032  0.0073  448 MET B C   
7425 O O   . MET B 462 ? 0.3357 0.2595 0.4796 -0.0333 0.0002  0.0107  448 MET B O   
7426 C CB  . MET B 462 ? 0.3781 0.3240 0.5226 -0.0334 0.0074  -0.0071 448 MET B CB  
7427 C CG  . MET B 462 ? 0.3343 0.2887 0.4793 -0.0300 0.0088  -0.0132 448 MET B CG  
7428 S SD  . MET B 462 ? 0.3821 0.3347 0.5265 -0.0332 0.0112  -0.0214 448 MET B SD  
7429 C CE  . MET B 462 ? 0.2831 0.2424 0.4278 -0.0287 0.0127  -0.0268 448 MET B CE  
7430 N N   . LEU B 463 ? 0.3391 0.2779 0.4757 -0.0432 0.0051  0.0096  449 LEU B N   
7431 C CA  . LEU B 463 ? 0.3197 0.2484 0.4541 -0.0492 0.0041  0.0163  449 LEU B CA  
7432 C C   . LEU B 463 ? 0.3694 0.2953 0.4983 -0.0487 0.0011  0.0255  449 LEU B C   
7433 O O   . LEU B 463 ? 0.3522 0.2638 0.4807 -0.0497 -0.0021 0.0315  449 LEU B O   
7434 C CB  . LEU B 463 ? 0.3589 0.2955 0.4915 -0.0576 0.0073  0.0161  449 LEU B CB  
7435 C CG  . LEU B 463 ? 0.3410 0.2789 0.4782 -0.0595 0.0087  0.0080  449 LEU B CG  
7436 C CD1 . LEU B 463 ? 0.3693 0.3227 0.5067 -0.0648 0.0115  0.0067  449 LEU B CD1 
7437 C CD2 . LEU B 463 ? 0.2904 0.2112 0.4295 -0.0635 0.0072  0.0077  449 LEU B CD2 
7438 N N   . ARG B 464 ? 0.3092 0.2474 0.4332 -0.0471 0.0017  0.0268  450 ARG B N   
7439 C CA  . ARG B 464 ? 0.4025 0.3385 0.5192 -0.0471 -0.0016 0.0355  450 ARG B CA  
7440 C C   . ARG B 464 ? 0.4532 0.3778 0.5747 -0.0404 -0.0075 0.0380  450 ARG B C   
7441 O O   . ARG B 464 ? 0.3775 0.2918 0.4951 -0.0415 -0.0119 0.0468  450 ARG B O   
7442 C CB  . ARG B 464 ? 0.3705 0.3211 0.4809 -0.0459 -0.0002 0.0344  450 ARG B CB  
7443 C CG  . ARG B 464 ? 0.3863 0.3354 0.4869 -0.0464 -0.0040 0.0427  450 ARG B CG  
7444 C CD  . ARG B 464 ? 0.3337 0.2941 0.4303 -0.0424 -0.0045 0.0393  450 ARG B CD  
7445 N NE  . ARG B 464 ? 0.3675 0.3286 0.4738 -0.0352 -0.0069 0.0334  450 ARG B NE  
7446 C CZ  . ARG B 464 ? 0.4931 0.4638 0.5994 -0.0321 -0.0061 0.0276  450 ARG B CZ  
7447 N NH1 . ARG B 464 ? 0.4262 0.4057 0.5237 -0.0345 -0.0034 0.0262  450 ARG B NH1 
7448 N NH2 . ARG B 464 ? 0.3332 0.3044 0.4486 -0.0267 -0.0079 0.0229  450 ARG B NH2 
7449 N N   . ASP B 465 ? 0.3465 0.2730 0.4769 -0.0335 -0.0077 0.0307  451 ASP B N   
7450 C CA  . ASP B 465 ? 0.3827 0.3019 0.5208 -0.0260 -0.0126 0.0317  451 ASP B CA  
7451 C C   . ASP B 465 ? 0.3506 0.2544 0.4965 -0.0243 -0.0131 0.0297  451 ASP B C   
7452 O O   . ASP B 465 ? 0.4404 0.3384 0.5955 -0.0169 -0.0163 0.0286  451 ASP B O   
7453 C CB  . ASP B 465 ? 0.2801 0.2111 0.4243 -0.0199 -0.0119 0.0247  451 ASP B CB  
7454 C CG  . ASP B 465 ? 0.3960 0.3395 0.5323 -0.0210 -0.0126 0.0267  451 ASP B CG  
7455 O OD1 . ASP B 465 ? 0.3414 0.2840 0.4678 -0.0251 -0.0145 0.0341  451 ASP B OD1 
7456 O OD2 . ASP B 465 ? 0.3695 0.3229 0.5087 -0.0182 -0.0113 0.0208  451 ASP B OD2 
7457 N N   . LYS B 466 ? 0.4102 0.3076 0.5533 -0.0310 -0.0101 0.0288  452 LYS B N   
7458 C CA  . LYS B 466 ? 0.4271 0.3072 0.5752 -0.0311 -0.0107 0.0270  452 LYS B CA  
7459 C C   . LYS B 466 ? 0.5404 0.4200 0.6984 -0.0241 -0.0086 0.0163  452 LYS B C   
7460 O O   . LYS B 466 ? 0.4808 0.3462 0.6457 -0.0194 -0.0104 0.0144  452 LYS B O   
7461 C CB  . LYS B 466 ? 0.3842 0.2475 0.5322 -0.0296 -0.0171 0.0366  452 LYS B CB  
7462 C CG  . LYS B 466 ? 0.5561 0.4154 0.6925 -0.0391 -0.0184 0.0474  452 LYS B CG  
7463 C CD  . LYS B 466 ? 0.6805 0.5416 0.8127 -0.0494 -0.0131 0.0448  452 LYS B CD  
7464 C CE  . LYS B 466 ? 0.8713 0.7170 1.0096 -0.0503 -0.0125 0.0386  452 LYS B CE  
7465 N NZ  . LYS B 466 ? 0.8183 0.6564 0.9512 -0.0621 -0.0113 0.0426  452 LYS B NZ  
7466 N N   . GLN B 467 ? 0.4132 0.3077 0.5713 -0.0235 -0.0045 0.0090  453 GLN B N   
7467 C CA  . GLN B 467 ? 0.4443 0.3394 0.6093 -0.0188 -0.0013 -0.0013 453 GLN B CA  
7468 C C   . GLN B 467 ? 0.4707 0.3559 0.6339 -0.0240 0.0015  -0.0073 453 GLN B C   
7469 O O   . GLN B 467 ? 0.3772 0.2619 0.5341 -0.0322 0.0019  -0.0047 453 GLN B O   
7470 C CB  . GLN B 467 ? 0.3122 0.2248 0.4761 -0.0178 0.0018  -0.0061 453 GLN B CB  
7471 C CG  . GLN B 467 ? 0.3986 0.3214 0.5638 -0.0137 -0.0011 -0.0015 453 GLN B CG  
7472 C CD  . GLN B 467 ? 0.3534 0.2904 0.5188 -0.0124 0.0018  -0.0073 453 GLN B CD  
7473 O OE1 . GLN B 467 ? 0.3466 0.2877 0.5076 -0.0163 0.0054  -0.0123 453 GLN B OE1 
7474 N NE2 . GLN B 467 ? 0.3163 0.2608 0.4869 -0.0074 -0.0002 -0.0063 453 GLN B NE2 
7475 N N   . HIS B 468 ? 0.3853 0.2642 0.5543 -0.0194 0.0037  -0.0159 454 HIS B N   
7476 C CA  . HIS B 468 ? 0.3585 0.2268 0.5249 -0.0240 0.0060  -0.0230 454 HIS B CA  
7477 C C   . HIS B 468 ? 0.3899 0.2659 0.5560 -0.0224 0.0109  -0.0341 454 HIS B C   
7478 O O   . HIS B 468 ? 0.3826 0.2492 0.5518 -0.0192 0.0133  -0.0422 454 HIS B O   
7479 C CB  . HIS B 468 ? 0.4127 0.2596 0.5840 -0.0209 0.0038  -0.0233 454 HIS B CB  
7480 C CG  . HIS B 468 ? 0.5210 0.3578 0.6917 -0.0223 -0.0016 -0.0115 454 HIS B CG  
7481 N ND1 . HIS B 468 ? 0.5236 0.3450 0.7013 -0.0154 -0.0056 -0.0084 454 HIS B ND1 
7482 C CD2 . HIS B 468 ? 0.4938 0.3338 0.6574 -0.0300 -0.0038 -0.0020 454 HIS B CD2 
7483 C CE1 . HIS B 468 ? 0.4474 0.2618 0.6208 -0.0193 -0.0106 0.0034  454 HIS B CE1 
7484 N NE2 . HIS B 468 ? 0.5501 0.3759 0.7146 -0.0285 -0.0090 0.0073  454 HIS B NE2 
7485 N N   . PRO B 469 ? 0.4100 0.3022 0.5716 -0.0250 0.0126  -0.0347 455 PRO B N   
7486 C CA  . PRO B 469 ? 0.3982 0.2965 0.5568 -0.0255 0.0167  -0.0441 455 PRO B CA  
7487 C C   . PRO B 469 ? 0.4976 0.3892 0.6490 -0.0333 0.0171  -0.0489 455 PRO B C   
7488 O O   . PRO B 469 ? 0.4244 0.3119 0.5733 -0.0395 0.0144  -0.0441 455 PRO B O   
7489 C CB  . PRO B 469 ? 0.4736 0.3892 0.6293 -0.0261 0.0168  -0.0412 455 PRO B CB  
7490 C CG  . PRO B 469 ? 0.3845 0.3021 0.5377 -0.0302 0.0134  -0.0325 455 PRO B CG  
7491 C CD  . PRO B 469 ? 0.5210 0.4256 0.6787 -0.0283 0.0108  -0.0272 455 PRO B CD  
7492 N N   . ILE B 470 ? 0.3848 0.2766 0.5323 -0.0337 0.0206  -0.0582 456 ILE B N   
7493 C CA  . ILE B 470 ? 0.4154 0.3030 0.5545 -0.0415 0.0204  -0.0635 456 ILE B CA  
7494 C C   . ILE B 470 ? 0.4295 0.3326 0.5623 -0.0449 0.0203  -0.0633 456 ILE B C   
7495 O O   . ILE B 470 ? 0.5026 0.4118 0.6324 -0.0425 0.0235  -0.0681 456 ILE B O   
7496 C CB  . ILE B 470 ? 0.4330 0.3082 0.5699 -0.0403 0.0240  -0.0745 456 ILE B CB  
7497 C CG1 . ILE B 470 ? 0.4262 0.2835 0.5700 -0.0367 0.0232  -0.0743 456 ILE B CG1 
7498 C CG2 . ILE B 470 ? 0.4236 0.2961 0.5496 -0.0492 0.0233  -0.0805 456 ILE B CG2 
7499 C CD1 . ILE B 470 ? 0.5654 0.4121 0.7110 -0.0313 0.0279  -0.0854 456 ILE B CD1 
7500 N N   . ILE B 471 ? 0.4189 0.3285 0.5500 -0.0503 0.0167  -0.0576 457 ILE B N   
7501 C CA  . ILE B 471 ? 0.3228 0.2468 0.4498 -0.0523 0.0155  -0.0560 457 ILE B CA  
7502 C C   . ILE B 471 ? 0.3900 0.3133 0.5096 -0.0596 0.0135  -0.0606 457 ILE B C   
7503 O O   . ILE B 471 ? 0.3984 0.3190 0.5190 -0.0656 0.0105  -0.0590 457 ILE B O   
7504 C CB  . ILE B 471 ? 0.3557 0.2893 0.4869 -0.0524 0.0131  -0.0472 457 ILE B CB  
7505 C CG1 . ILE B 471 ? 0.4268 0.3614 0.5634 -0.0458 0.0142  -0.0424 457 ILE B CG1 
7506 C CG2 . ILE B 471 ? 0.4013 0.3482 0.5292 -0.0539 0.0113  -0.0463 457 ILE B CG2 
7507 C CD1 . ILE B 471 ? 0.3773 0.3166 0.5166 -0.0469 0.0123  -0.0342 457 ILE B CD1 
7508 N N   . LEU B 472 ? 0.3416 0.2682 0.4537 -0.0600 0.0146  -0.0658 458 LEU B N   
7509 C CA  . LEU B 472 ? 0.3738 0.3006 0.4771 -0.0671 0.0116  -0.0698 458 LEU B CA  
7510 C C   . LEU B 472 ? 0.4328 0.3733 0.5342 -0.0676 0.0080  -0.0654 458 LEU B C   
7511 O O   . LEU B 472 ? 0.4360 0.3814 0.5341 -0.0641 0.0097  -0.0651 458 LEU B O   
7512 C CB  . LEU B 472 ? 0.3858 0.3046 0.4795 -0.0680 0.0151  -0.0792 458 LEU B CB  
7513 C CG  . LEU B 472 ? 0.4622 0.3654 0.5577 -0.0671 0.0183  -0.0853 458 LEU B CG  
7514 C CD1 . LEU B 472 ? 0.4528 0.3541 0.5534 -0.0587 0.0245  -0.0879 458 LEU B CD1 
7515 C CD2 . LEU B 472 ? 0.4867 0.3806 0.5707 -0.0740 0.0178  -0.0943 458 LEU B CD2 
7516 N N   . VAL B 473 ? 0.4259 0.3725 0.5302 -0.0721 0.0031  -0.0618 459 VAL B N   
7517 C CA  . VAL B 473 ? 0.4105 0.3699 0.5148 -0.0721 -0.0011 -0.0578 459 VAL B CA  
7518 C C   . VAL B 473 ? 0.4109 0.3701 0.5058 -0.0782 -0.0057 -0.0617 459 VAL B C   
7519 O O   . VAL B 473 ? 0.3412 0.2981 0.4363 -0.0846 -0.0089 -0.0637 459 VAL B O   
7520 C CB  . VAL B 473 ? 0.3587 0.3276 0.4739 -0.0723 -0.0033 -0.0516 459 VAL B CB  
7521 C CG1 . VAL B 473 ? 0.3779 0.3596 0.4944 -0.0707 -0.0075 -0.0484 459 VAL B CG1 
7522 C CG2 . VAL B 473 ? 0.2879 0.2557 0.4096 -0.0671 0.0010  -0.0477 459 VAL B CG2 
7523 N N   . LEU B 474 ? 0.3497 0.3109 0.4357 -0.0770 -0.0066 -0.0625 460 LEU B N   
7524 C CA  . LEU B 474 ? 0.4176 0.3782 0.4921 -0.0830 -0.0117 -0.0653 460 LEU B CA  
7525 C C   . LEU B 474 ? 0.4708 0.4434 0.5515 -0.0839 -0.0195 -0.0599 460 LEU B C   
7526 O O   . LEU B 474 ? 0.4604 0.4394 0.5415 -0.0798 -0.0219 -0.0556 460 LEU B O   
7527 C CB  . LEU B 474 ? 0.4061 0.3635 0.4674 -0.0820 -0.0094 -0.0675 460 LEU B CB  
7528 C CG  . LEU B 474 ? 0.5253 0.4720 0.5774 -0.0835 -0.0025 -0.0755 460 LEU B CG  
7529 C CD1 . LEU B 474 ? 0.5181 0.4611 0.5808 -0.0775 0.0047  -0.0765 460 LEU B CD1 
7530 C CD2 . LEU B 474 ? 0.4118 0.3577 0.4496 -0.0845 -0.0003 -0.0773 460 LEU B CD2 
7531 N N   . ASN B 475 ? 0.4022 0.3777 0.4890 -0.0892 -0.0235 -0.0601 461 ASN B N   
7532 C CA  . ASN B 475 ? 0.4239 0.4132 0.5203 -0.0899 -0.0306 -0.0554 461 ASN B CA  
7533 C C   . ASN B 475 ? 0.4545 0.4451 0.5409 -0.0950 -0.0389 -0.0567 461 ASN B C   
7534 O O   . ASN B 475 ? 0.4807 0.4697 0.5642 -0.1028 -0.0432 -0.0600 461 ASN B O   
7535 C CB  . ASN B 475 ? 0.3955 0.3897 0.5049 -0.0939 -0.0307 -0.0544 461 ASN B CB  
7536 C CG  . ASN B 475 ? 0.4983 0.5102 0.6216 -0.0933 -0.0362 -0.0495 461 ASN B CG  
7537 O OD1 . ASN B 475 ? 0.4848 0.5041 0.6076 -0.0899 -0.0414 -0.0473 461 ASN B OD1 
7538 N ND2 . ASN B 475 ? 0.3996 0.4183 0.5355 -0.0966 -0.0349 -0.0478 461 ASN B ND2 
7539 N N   . ASN B 476 ? 0.3887 0.3816 0.4690 -0.0912 -0.0420 -0.0537 462 ASN B N   
7540 C CA  . ASN B 476 ? 0.4061 0.4017 0.4779 -0.0950 -0.0517 -0.0527 462 ASN B CA  
7541 C C   . ASN B 476 ? 0.3963 0.4062 0.4817 -0.0903 -0.0590 -0.0464 462 ASN B C   
7542 O O   . ASN B 476 ? 0.4244 0.4364 0.5038 -0.0907 -0.0676 -0.0436 462 ASN B O   
7543 C CB  . ASN B 476 ? 0.4024 0.3880 0.4545 -0.0955 -0.0508 -0.0538 462 ASN B CB  
7544 C CG  . ASN B 476 ? 0.4367 0.4201 0.4899 -0.0879 -0.0440 -0.0512 462 ASN B CG  
7545 O OD1 . ASN B 476 ? 0.4321 0.4230 0.4985 -0.0813 -0.0442 -0.0467 462 ASN B OD1 
7546 N ND2 . ASN B 476 ? 0.4818 0.4555 0.5213 -0.0891 -0.0376 -0.0547 462 ASN B ND2 
7547 N N   . GLU B 477 ? 0.4189 0.4383 0.5222 -0.0855 -0.0555 -0.0441 463 GLU B N   
7548 C CA  . GLU B 477 ? 0.3899 0.4245 0.5091 -0.0802 -0.0607 -0.0395 463 GLU B CA  
7549 C C   . GLU B 477 ? 0.4641 0.4971 0.5783 -0.0733 -0.0647 -0.0357 463 GLU B C   
7550 O O   . GLU B 477 ? 0.4348 0.4734 0.5502 -0.0726 -0.0745 -0.0329 463 GLU B O   
7551 C CB  . GLU B 477 ? 0.3318 0.3779 0.4592 -0.0861 -0.0699 -0.0393 463 GLU B CB  
7552 C CG  . GLU B 477 ? 0.5386 0.5823 0.6659 -0.0956 -0.0681 -0.0435 463 GLU B CG  
7553 C CD  . GLU B 477 ? 0.6471 0.7056 0.7866 -0.1013 -0.0771 -0.0427 463 GLU B CD  
7554 O OE1 . GLU B 477 ? 0.6591 0.7166 0.7896 -0.1061 -0.0866 -0.0432 463 GLU B OE1 
7555 O OE2 . GLU B 477 ? 0.6662 0.7380 0.8243 -0.1014 -0.0748 -0.0413 463 GLU B OE2 
7556 N N   . GLY B 478 ? 0.4017 0.4267 0.5107 -0.0683 -0.0577 -0.0355 464 GLY B N   
7557 C CA  . GLY B 478 ? 0.3984 0.4213 0.5046 -0.0616 -0.0606 -0.0317 464 GLY B CA  
7558 C C   . GLY B 478 ? 0.3762 0.3848 0.4652 -0.0624 -0.0559 -0.0324 464 GLY B C   
7559 O O   . GLY B 478 ? 0.3569 0.3590 0.4396 -0.0661 -0.0486 -0.0362 464 GLY B O   
7560 N N   . TYR B 479 ? 0.3759 0.3800 0.4586 -0.0589 -0.0603 -0.0286 465 TYR B N   
7561 C CA  . TYR B 479 ? 0.4254 0.4172 0.4926 -0.0599 -0.0563 -0.0282 465 TYR B CA  
7562 C C   . TYR B 479 ? 0.4293 0.4137 0.4777 -0.0676 -0.0613 -0.0280 465 TYR B C   
7563 O O   . TYR B 479 ? 0.4470 0.4275 0.4872 -0.0676 -0.0694 -0.0233 465 TYR B O   
7564 C CB  . TYR B 479 ? 0.3892 0.3786 0.4588 -0.0528 -0.0584 -0.0239 465 TYR B CB  
7565 C CG  . TYR B 479 ? 0.3316 0.3283 0.4181 -0.0451 -0.0540 -0.0244 465 TYR B CG  
7566 C CD1 . TYR B 479 ? 0.3696 0.3682 0.4611 -0.0451 -0.0446 -0.0277 465 TYR B CD1 
7567 C CD2 . TYR B 479 ? 0.3963 0.3972 0.4927 -0.0376 -0.0594 -0.0217 465 TYR B CD2 
7568 C CE1 . TYR B 479 ? 0.3184 0.3232 0.4227 -0.0389 -0.0407 -0.0280 465 TYR B CE1 
7569 C CE2 . TYR B 479 ? 0.3200 0.3276 0.4300 -0.0310 -0.0546 -0.0230 465 TYR B CE2 
7570 C CZ  . TYR B 479 ? 0.3286 0.3381 0.4415 -0.0321 -0.0453 -0.0259 465 TYR B CZ  
7571 O OH  . TYR B 479 ? 0.3164 0.3322 0.4403 -0.0263 -0.0407 -0.0270 465 TYR B OH  
7572 N N   . THR B 480 ? 0.4000 0.3813 0.4402 -0.0743 -0.0564 -0.0333 466 THR B N   
7573 C CA  . THR B 480 ? 0.4031 0.3782 0.4243 -0.0825 -0.0609 -0.0342 466 THR B CA  
7574 C C   . THR B 480 ? 0.5696 0.5347 0.5726 -0.0847 -0.0593 -0.0318 466 THR B C   
7575 O O   . THR B 480 ? 0.5337 0.4941 0.5213 -0.0896 -0.0670 -0.0286 466 THR B O   
7576 C CB  . THR B 480 ? 0.3705 0.3435 0.3874 -0.0887 -0.0552 -0.0417 466 THR B CB  
7577 O OG1 . THR B 480 ? 0.4158 0.3965 0.4427 -0.0908 -0.0616 -0.0426 466 THR B OG1 
7578 C CG2 . THR B 480 ? 0.4897 0.4534 0.4828 -0.0970 -0.0545 -0.0448 466 THR B CG2 
7579 N N   . VAL B 481 ? 0.4168 0.3790 0.4214 -0.0817 -0.0501 -0.0326 467 VAL B N   
7580 C CA  . VAL B 481 ? 0.4874 0.4414 0.4763 -0.0845 -0.0484 -0.0298 467 VAL B CA  
7581 C C   . VAL B 481 ? 0.4889 0.4398 0.4757 -0.0818 -0.0589 -0.0216 467 VAL B C   
7582 O O   . VAL B 481 ? 0.6037 0.5469 0.5726 -0.0873 -0.0637 -0.0175 467 VAL B O   
7583 C CB  . VAL B 481 ? 0.5383 0.4919 0.5326 -0.0816 -0.0372 -0.0321 467 VAL B CB  
7584 C CG1 . VAL B 481 ? 0.5644 0.5114 0.5484 -0.0829 -0.0374 -0.0270 467 VAL B CG1 
7585 C CG2 . VAL B 481 ? 0.6295 0.5823 0.6182 -0.0862 -0.0276 -0.0397 467 VAL B CG2 
7586 N N   . LEU B 482 ? 0.4464 0.4028 0.4512 -0.0734 -0.0625 -0.0190 468 LEU B N   
7587 C CA  . LEU B 482 ? 0.5305 0.4835 0.5354 -0.0694 -0.0731 -0.0119 468 LEU B CA  
7588 C C   . LEU B 482 ? 0.5490 0.5024 0.5466 -0.0731 -0.0852 -0.0087 468 LEU B C   
7589 O O   . LEU B 482 ? 0.6120 0.5579 0.6003 -0.0732 -0.0946 -0.0020 468 LEU B O   
7590 C CB  . LEU B 482 ? 0.5032 0.4634 0.5299 -0.0591 -0.0734 -0.0116 468 LEU B CB  
7591 C CG  . LEU B 482 ? 0.4770 0.4350 0.5085 -0.0556 -0.0637 -0.0134 468 LEU B CG  
7592 C CD1 . LEU B 482 ? 0.4319 0.3955 0.4814 -0.0458 -0.0650 -0.0130 468 LEU B CD1 
7593 C CD2 . LEU B 482 ? 0.4240 0.3695 0.4391 -0.0596 -0.0630 -0.0099 468 LEU B CD2 
7594 N N   . ARG B 483 ? 0.4894 0.4509 0.4912 -0.0762 -0.0861 -0.0130 469 ARG B N   
7595 C CA  . ARG B 483 ? 0.4316 0.3945 0.4262 -0.0807 -0.0983 -0.0103 469 ARG B CA  
7596 C C   . ARG B 483 ? 0.5726 0.5238 0.5391 -0.0904 -0.1004 -0.0083 469 ARG B C   
7597 O O   . ARG B 483 ? 0.6228 0.5693 0.5786 -0.0924 -0.1124 -0.0017 469 ARG B O   
7598 C CB  . ARG B 483 ? 0.5827 0.5563 0.5872 -0.0835 -0.0978 -0.0161 469 ARG B CB  
7599 C CG  . ARG B 483 ? 0.4258 0.4128 0.4575 -0.0754 -0.0968 -0.0172 469 ARG B CG  
7600 C CD  . ARG B 483 ? 0.5409 0.5381 0.5810 -0.0801 -0.0988 -0.0215 469 ARG B CD  
7601 N NE  . ARG B 483 ? 0.4272 0.4368 0.4912 -0.0746 -0.0940 -0.0236 469 ARG B NE  
7602 C CZ  . ARG B 483 ? 0.5942 0.6168 0.6778 -0.0683 -0.1003 -0.0207 469 ARG B CZ  
7603 N NH1 . ARG B 483 ? 0.4451 0.4700 0.5294 -0.0656 -0.1126 -0.0154 469 ARG B NH1 
7604 N NH2 . ARG B 483 ? 0.3904 0.4243 0.4937 -0.0645 -0.0940 -0.0231 469 ARG B NH2 
7605 N N   . ALA B 484 ? 0.4635 0.4102 0.4177 -0.0965 -0.0888 -0.0141 470 ALA B N   
7606 C CA  . ALA B 484 ? 0.5917 0.5276 0.5190 -0.1055 -0.0877 -0.0127 470 ALA B CA  
7607 C C   . ALA B 484 ? 0.5646 0.4916 0.4851 -0.1036 -0.0911 -0.0042 470 ALA B C   
7608 O O   . ALA B 484 ? 0.6210 0.5389 0.5194 -0.1108 -0.0967 0.0010  470 ALA B O   
7609 C CB  . ALA B 484 ? 0.6388 0.5735 0.5589 -0.1104 -0.0726 -0.0214 470 ALA B CB  
7610 N N   . ILE B 485 ? 0.6043 0.5325 0.5417 -0.0949 -0.0876 -0.0027 471 ILE B N   
7611 C CA  . ILE B 485 ? 0.5660 0.4838 0.4966 -0.0937 -0.0906 0.0048  471 ILE B CA  
7612 C C   . ILE B 485 ? 0.6117 0.5236 0.5364 -0.0928 -0.1069 0.0136  471 ILE B C   
7613 O O   . ILE B 485 ? 0.6061 0.5068 0.5085 -0.1001 -0.1125 0.0199  471 ILE B O   
7614 C CB  . ILE B 485 ? 0.8003 0.7206 0.7516 -0.0837 -0.0861 0.0043  471 ILE B CB  
7615 C CG1 . ILE B 485 ? 0.7623 0.6855 0.7181 -0.0842 -0.0711 -0.0018 471 ILE B CG1 
7616 C CG2 . ILE B 485 ? 0.7748 0.6826 0.7208 -0.0813 -0.0937 0.0130  471 ILE B CG2 
7617 C CD1 . ILE B 485 ? 0.6463 0.5626 0.5826 -0.0937 -0.0635 -0.0019 471 ILE B CD1 
7618 N N   . HIS B 486 ? 0.5302 0.4502 0.4756 -0.0836 -0.1146 0.0143  472 HIS B N   
7619 C CA  . HIS B 486 ? 0.5695 0.4865 0.5192 -0.0779 -0.1300 0.0222  472 HIS B CA  
7620 C C   . HIS B 486 ? 0.5765 0.5096 0.5530 -0.0691 -0.1334 0.0186  472 HIS B C   
7621 O O   . HIS B 486 ? 0.4770 0.4186 0.4710 -0.0636 -0.1236 0.0126  472 HIS B O   
7622 C CB  . HIS B 486 ? 0.6637 0.5683 0.6138 -0.0725 -0.1312 0.0278  472 HIS B CB  
7623 C CG  . HIS B 486 ? 0.5341 0.4347 0.4926 -0.0641 -0.1463 0.0351  472 HIS B CG  
7624 N ND1 . HIS B 486 ? 0.5790 0.4684 0.5201 -0.0683 -0.1601 0.0442  472 HIS B ND1 
7625 C CD2 . HIS B 486 ? 0.5547 0.4604 0.5370 -0.0513 -0.1498 0.0347  472 HIS B CD2 
7626 C CE1 . HIS B 486 ? 0.6828 0.5706 0.6382 -0.0578 -0.1722 0.0492  472 HIS B CE1 
7627 N NE2 . HIS B 486 ? 0.6630 0.5609 0.6437 -0.0471 -0.1657 0.0430  472 HIS B NE2 
7628 N N   . GLY B 487 ? 0.5566 0.4945 0.5360 -0.0683 -0.1471 0.0224  473 GLY B N   
7629 C CA  . GLY B 487 ? 0.5688 0.5233 0.5751 -0.0598 -0.1516 0.0201  473 GLY B CA  
7630 C C   . GLY B 487 ? 0.5587 0.5278 0.5755 -0.0631 -0.1429 0.0115  473 GLY B C   
7631 O O   . GLY B 487 ? 0.5055 0.4851 0.5433 -0.0565 -0.1353 0.0069  473 GLY B O   
7632 N N   . PRO B 488 ? 0.5111 0.4802 0.5126 -0.0738 -0.1443 0.0093  474 PRO B N   
7633 C CA  . PRO B 488 ? 0.5718 0.5527 0.5829 -0.0775 -0.1369 0.0012  474 PRO B CA  
7634 C C   . PRO B 488 ? 0.5344 0.5335 0.5731 -0.0712 -0.1425 0.0004  474 PRO B C   
7635 O O   . PRO B 488 ? 0.5687 0.5779 0.6227 -0.0703 -0.1336 -0.0055 474 PRO B O   
7636 C CB  . PRO B 488 ? 0.6236 0.5992 0.6110 -0.0900 -0.1406 -0.0003 474 PRO B CB  
7637 C CG  . PRO B 488 ? 0.6336 0.5959 0.5987 -0.0931 -0.1502 0.0077  474 PRO B CG  
7638 C CD  . PRO B 488 ? 0.6035 0.5632 0.5807 -0.0823 -0.1554 0.0148  474 PRO B CD  
7639 N N   . GLU B 489 ? 0.5633 0.5671 0.6091 -0.0669 -0.1571 0.0066  475 GLU B N   
7640 C CA  . GLU B 489 ? 0.6014 0.6250 0.6748 -0.0612 -0.1636 0.0062  475 GLU B CA  
7641 C C   . GLU B 489 ? 0.5947 0.6247 0.6912 -0.0473 -0.1621 0.0076  475 GLU B C   
7642 O O   . GLU B 489 ? 0.6503 0.6982 0.7716 -0.0412 -0.1671 0.0073  475 GLU B O   
7643 C CB  . GLU B 489 ? 0.5101 0.5376 0.5799 -0.0643 -0.1817 0.0117  475 GLU B CB  
7644 C CG  . GLU B 489 ? 0.8141 0.8493 0.8788 -0.0760 -0.1848 0.0076  475 GLU B CG  
7645 C CD  . GLU B 489 ? 1.0662 1.1088 1.1323 -0.0779 -0.2042 0.0134  475 GLU B CD  
7646 O OE1 . GLU B 489 ? 1.0136 1.0425 1.0533 -0.0846 -0.2130 0.0180  475 GLU B OE1 
7647 O OE2 . GLU B 489 ? 1.0102 1.0726 1.1035 -0.0728 -0.2108 0.0136  475 GLU B OE2 
7648 N N   . GLN B 490 ? 0.6012 0.6178 0.6907 -0.0425 -0.1551 0.0086  476 GLN B N   
7649 C CA  . GLN B 490 ? 0.4721 0.4925 0.5812 -0.0296 -0.1528 0.0087  476 GLN B CA  
7650 C C   . GLN B 490 ? 0.5408 0.5735 0.6667 -0.0272 -0.1386 0.0015  476 GLN B C   
7651 O O   . GLN B 490 ? 0.4788 0.5076 0.5948 -0.0343 -0.1278 -0.0026 476 GLN B O   
7652 C CB  . GLN B 490 ? 0.5210 0.5209 0.6147 -0.0265 -0.1514 0.0125  476 GLN B CB  
7653 C CG  . GLN B 490 ? 0.4461 0.4331 0.5270 -0.0259 -0.1667 0.0212  476 GLN B CG  
7654 C CD  . GLN B 490 ? 0.5641 0.5587 0.6672 -0.0131 -0.1780 0.0245  476 GLN B CD  
7655 O OE1 . GLN B 490 ? 0.5240 0.5379 0.6471 -0.0102 -0.1835 0.0231  476 GLN B OE1 
7656 N NE2 . GLN B 490 ? 0.6049 0.5844 0.7055 -0.0053 -0.1817 0.0287  476 GLN B NE2 
7657 N N   . ARG B 491 ? 0.4484 0.4960 0.5996 -0.0171 -0.1388 0.0001  477 ARG B N   
7658 C CA  . ARG B 491 ? 0.4898 0.5510 0.6572 -0.0156 -0.1262 -0.0060 477 ARG B CA  
7659 C C   . ARG B 491 ? 0.4249 0.4748 0.5847 -0.0135 -0.1135 -0.0088 477 ARG B C   
7660 O O   . ARG B 491 ? 0.4955 0.5525 0.6616 -0.0153 -0.1024 -0.0133 477 ARG B O   
7661 C CB  . ARG B 491 ? 0.4163 0.4985 0.6129 -0.0059 -0.1293 -0.0072 477 ARG B CB  
7662 C CG  . ARG B 491 ? 0.5877 0.6666 0.7937 0.0073  -0.1281 -0.0073 477 ARG B CG  
7663 C CD  . ARG B 491 ? 0.5590 0.6615 0.7940 0.0152  -0.1237 -0.0117 477 ARG B CD  
7664 N NE  . ARG B 491 ? 0.5173 0.6191 0.7645 0.0293  -0.1265 -0.0120 477 ARG B NE  
7665 C CZ  . ARG B 491 ? 0.5796 0.6799 0.8313 0.0363  -0.1160 -0.0167 477 ARG B CZ  
7666 N NH1 . ARG B 491 ? 0.4594 0.5588 0.7041 0.0306  -0.1026 -0.0204 477 ARG B NH1 
7667 N NH2 . ARG B 491 ? 0.4458 0.5444 0.7087 0.0494  -0.1195 -0.0176 477 ARG B NH2 
7668 N N   . TYR B 492 ? 0.3469 0.3792 0.4934 -0.0101 -0.1152 -0.0058 478 TYR B N   
7669 C CA  . TYR B 492 ? 0.3646 0.3874 0.5044 -0.0092 -0.1035 -0.0086 478 TYR B CA  
7670 C C   . TYR B 492 ? 0.4580 0.4747 0.5819 -0.0198 -0.0952 -0.0106 478 TYR B C   
7671 O O   . TYR B 492 ? 0.3949 0.4080 0.5167 -0.0197 -0.0848 -0.0136 478 TYR B O   
7672 C CB  . TYR B 492 ? 0.3226 0.3275 0.4521 -0.0042 -0.1072 -0.0050 478 TYR B CB  
7673 C CG  . TYR B 492 ? 0.3661 0.3559 0.4757 -0.0098 -0.1170 0.0013  478 TYR B CG  
7674 C CD1 . TYR B 492 ? 0.3213 0.3015 0.4097 -0.0208 -0.1130 0.0019  478 TYR B CD1 
7675 C CD2 . TYR B 492 ? 0.4287 0.4137 0.5404 -0.0040 -0.1303 0.0069  478 TYR B CD2 
7676 C CE1 . TYR B 492 ? 0.4679 0.4346 0.5362 -0.0269 -0.1212 0.0077  478 TYR B CE1 
7677 C CE2 . TYR B 492 ? 0.4930 0.4631 0.5845 -0.0099 -0.1398 0.0137  478 TYR B CE2 
7678 C CZ  . TYR B 492 ? 0.5084 0.4696 0.5774 -0.0219 -0.1349 0.0141  478 TYR B CZ  
7679 O OH  . TYR B 492 ? 0.4471 0.3941 0.4943 -0.0287 -0.1436 0.0209  478 TYR B OH  
7680 N N   . ASN B 493 ? 0.4705 0.4860 0.5836 -0.0286 -0.0998 -0.0095 479 ASN B N   
7681 C CA  . ASN B 493 ? 0.4309 0.4420 0.5311 -0.0381 -0.0919 -0.0128 479 ASN B CA  
7682 C C   . ASN B 493 ? 0.4742 0.4992 0.5876 -0.0409 -0.0866 -0.0173 479 ASN B C   
7683 O O   . ASN B 493 ? 0.5226 0.5439 0.6276 -0.0480 -0.0800 -0.0207 479 ASN B O   
7684 C CB  . ASN B 493 ? 0.3532 0.3547 0.4328 -0.0468 -0.0987 -0.0103 479 ASN B CB  
7685 C CG  . ASN B 493 ? 0.5047 0.4894 0.5658 -0.0476 -0.0994 -0.0064 479 ASN B CG  
7686 O OD1 . ASN B 493 ? 0.4083 0.3873 0.4698 -0.0439 -0.0921 -0.0071 479 ASN B OD1 
7687 N ND2 . ASN B 493 ? 0.3451 0.3216 0.3891 -0.0533 -0.1083 -0.0021 479 ASN B ND2 
7688 N N   . ASP B 494 ? 0.4491 0.3934 0.5694 0.0011  -0.0687 0.1121  480 ASP B N   
7689 C CA  . ASP B 494 ? 0.4242 0.4021 0.5817 -0.0020 -0.0748 0.0982  480 ASP B CA  
7690 C C   . ASP B 494 ? 0.4972 0.4637 0.6703 -0.0127 -0.0609 0.0897  480 ASP B C   
7691 O O   . ASP B 494 ? 0.5131 0.4498 0.6740 -0.0146 -0.0474 0.0945  480 ASP B O   
7692 C CB  . ASP B 494 ? 0.4332 0.4336 0.6134 0.0163  -0.0863 0.1018  480 ASP B CB  
7693 C CG  . ASP B 494 ? 0.4833 0.5042 0.6505 0.0282  -0.1021 0.1089  480 ASP B CG  
7694 O OD1 . ASP B 494 ? 0.5617 0.5899 0.7108 0.0185  -0.1063 0.1062  480 ASP B OD1 
7695 O OD2 . ASP B 494 ? 0.4783 0.5112 0.6538 0.0480  -0.1107 0.1166  480 ASP B OD2 
7696 N N   . ILE B 495 ? 0.4026 0.3930 0.6010 -0.0206 -0.0638 0.0766  481 ILE B N   
7697 C CA  . ILE B 495 ? 0.3669 0.3527 0.5818 -0.0292 -0.0530 0.0689  481 ILE B CA  
7698 C C   . ILE B 495 ? 0.4448 0.4544 0.6921 -0.0266 -0.0587 0.0623  481 ILE B C   
7699 O O   . ILE B 495 ? 0.3733 0.4069 0.6308 -0.0227 -0.0706 0.0594  481 ILE B O   
7700 C CB  . ILE B 495 ? 0.4054 0.3911 0.6122 -0.0443 -0.0476 0.0591  481 ILE B CB  
7701 C CG1 . ILE B 495 ? 0.3352 0.3453 0.5515 -0.0481 -0.0585 0.0497  481 ILE B CG1 
7702 C CG2 . ILE B 495 ? 0.3609 0.3272 0.5357 -0.0499 -0.0408 0.0629  481 ILE B CG2 
7703 C CD1 . ILE B 495 ? 0.4025 0.4137 0.6124 -0.0594 -0.0542 0.0395  481 ILE B CD1 
7704 N N   . ALA B 496 ? 0.3180 0.3225 0.5805 -0.0307 -0.0493 0.0587  482 ALA B N   
7705 C CA  . ALA B 496 ? 0.3007 0.3253 0.5908 -0.0333 -0.0518 0.0507  482 ALA B CA  
7706 C C   . ALA B 496 ? 0.3474 0.3841 0.6390 -0.0433 -0.0567 0.0413  482 ALA B C   
7707 O O   . ALA B 496 ? 0.3780 0.4048 0.6556 -0.0505 -0.0525 0.0386  482 ALA B O   
7708 C CB  . ALA B 496 ? 0.2817 0.2969 0.5826 -0.0381 -0.0395 0.0487  482 ALA B CB  
7709 N N   . LEU B 497 ? 0.3053 0.3645 0.6144 -0.0438 -0.0648 0.0348  483 LEU B N   
7710 C CA  . LEU B 497 ? 0.2822 0.3508 0.5927 -0.0534 -0.0688 0.0247  483 LEU B CA  
7711 C C   . LEU B 497 ? 0.3484 0.4105 0.6710 -0.0625 -0.0608 0.0185  483 LEU B C   
7712 O O   . LEU B 497 ? 0.3753 0.4462 0.7167 -0.0643 -0.0590 0.0157  483 LEU B O   
7713 C CB  . LEU B 497 ? 0.2721 0.3686 0.5933 -0.0517 -0.0801 0.0191  483 LEU B CB  
7714 C CG  . LEU B 497 ? 0.2959 0.4007 0.6017 -0.0412 -0.0896 0.0267  483 LEU B CG  
7715 C CD1 . LEU B 497 ? 0.2726 0.4120 0.5881 -0.0408 -0.1016 0.0188  483 LEU B CD1 
7716 C CD2 . LEU B 497 ? 0.2998 0.3862 0.5786 -0.0445 -0.0873 0.0300  483 LEU B CD2 
7717 N N   . TRP B 498 ? 0.2587 0.3061 0.5695 -0.0676 -0.0558 0.0165  484 TRP B N   
7718 C CA  . TRP B 498 ? 0.2832 0.3206 0.5997 -0.0737 -0.0483 0.0132  484 TRP B CA  
7719 C C   . TRP B 498 ? 0.3467 0.3856 0.6673 -0.0807 -0.0508 0.0035  484 TRP B C   
7720 O O   . TRP B 498 ? 0.3670 0.4148 0.6836 -0.0819 -0.0575 -0.0022 484 TRP B O   
7721 C CB  . TRP B 498 ? 0.2202 0.2434 0.5215 -0.0729 -0.0417 0.0160  484 TRP B CB  
7722 C CG  . TRP B 498 ? 0.2612 0.2796 0.5600 -0.0699 -0.0350 0.0230  484 TRP B CG  
7723 C CD1 . TRP B 498 ? 0.3460 0.3676 0.6533 -0.0659 -0.0345 0.0279  484 TRP B CD1 
7724 C CD2 . TRP B 498 ? 0.3034 0.3142 0.5907 -0.0709 -0.0269 0.0242  484 TRP B CD2 
7725 N NE1 . TRP B 498 ? 0.2339 0.2461 0.5351 -0.0653 -0.0254 0.0320  484 TRP B NE1 
7726 C CE2 . TRP B 498 ? 0.2683 0.2757 0.5572 -0.0695 -0.0206 0.0293  484 TRP B CE2 
7727 C CE3 . TRP B 498 ? 0.2805 0.2897 0.5570 -0.0723 -0.0242 0.0203  484 TRP B CE3 
7728 C CZ2 . TRP B 498 ? 0.2219 0.2244 0.5015 -0.0723 -0.0107 0.0296  484 TRP B CZ2 
7729 C CZ3 . TRP B 498 ? 0.2339 0.2428 0.5021 -0.0736 -0.0158 0.0207  484 TRP B CZ3 
7730 C CH2 . TRP B 498 ? 0.2919 0.2975 0.5614 -0.0750 -0.0087 0.0249  484 TRP B CH2 
7731 N N   . ASN B 499 ? 0.3010 0.3292 0.6278 -0.0861 -0.0441 0.0016  485 ASN B N   
7732 C CA  . ASN B 499 ? 0.2558 0.2757 0.5834 -0.0935 -0.0428 -0.0071 485 ASN B CA  
7733 C C   . ASN B 499 ? 0.3013 0.3011 0.6139 -0.0897 -0.0386 -0.0056 485 ASN B C   
7734 O O   . ASN B 499 ? 0.3573 0.3415 0.6677 -0.0898 -0.0317 -0.0020 485 ASN B O   
7735 C CB  . ASN B 499 ? 0.3235 0.3419 0.6639 -0.1020 -0.0370 -0.0097 485 ASN B CB  
7736 C CG  . ASN B 499 ? 0.3375 0.3494 0.6766 -0.1116 -0.0349 -0.0207 485 ASN B CG  
7737 O OD1 . ASN B 499 ? 0.3538 0.3605 0.6888 -0.1129 -0.0382 -0.0270 485 ASN B OD1 
7738 N ND2 . ASN B 499 ? 0.3501 0.3619 0.6908 -0.1194 -0.0283 -0.0243 485 ASN B ND2 
7739 N N   . TRP B 500 ? 0.3264 0.3289 0.6279 -0.0857 -0.0431 -0.0090 486 TRP B N   
7740 C CA  . TRP B 500 ? 0.3280 0.3207 0.6160 -0.0791 -0.0403 -0.0079 486 TRP B CA  
7741 C C   . TRP B 500 ? 0.3562 0.3282 0.6413 -0.0781 -0.0353 -0.0105 486 TRP B C   
7742 O O   . TRP B 500 ? 0.2881 0.2516 0.5661 -0.0712 -0.0312 -0.0054 486 TRP B O   
7743 C CB  . TRP B 500 ? 0.3026 0.3052 0.5804 -0.0772 -0.0456 -0.0136 486 TRP B CB  
7744 C CG  . TRP B 500 ? 0.3314 0.3471 0.6048 -0.0764 -0.0485 -0.0080 486 TRP B CG  
7745 C CD1 . TRP B 500 ? 0.3322 0.3603 0.6078 -0.0783 -0.0549 -0.0075 486 TRP B CD1 
7746 C CD2 . TRP B 500 ? 0.2972 0.3131 0.5613 -0.0732 -0.0442 -0.0020 486 TRP B CD2 
7747 N NE1 . TRP B 500 ? 0.3097 0.3405 0.5760 -0.0752 -0.0547 0.0003  486 TRP B NE1 
7748 C CE2 . TRP B 500 ? 0.3111 0.3337 0.5705 -0.0736 -0.0472 0.0028  486 TRP B CE2 
7749 C CE3 . TRP B 500 ? 0.2689 0.2813 0.5273 -0.0702 -0.0378 -0.0009 486 TRP B CE3 
7750 C CZ2 . TRP B 500 ? 0.2578 0.2779 0.5060 -0.0729 -0.0421 0.0083  486 TRP B CZ2 
7751 C CZ3 . TRP B 500 ? 0.2703 0.2868 0.5200 -0.0708 -0.0332 0.0026  486 TRP B CZ3 
7752 C CH2 . TRP B 500 ? 0.3556 0.3732 0.5998 -0.0730 -0.0344 0.0070  486 TRP B CH2 
7753 N N   . THR B 501 ? 0.3191 0.2823 0.6085 -0.0847 -0.0352 -0.0185 487 THR B N   
7754 C CA  . THR B 501 ? 0.3672 0.3033 0.6504 -0.0830 -0.0291 -0.0206 487 THR B CA  
7755 C C   . THR B 501 ? 0.4109 0.3304 0.6942 -0.0840 -0.0218 -0.0112 487 THR B C   
7756 O O   . THR B 501 ? 0.3846 0.2778 0.6579 -0.0794 -0.0163 -0.0089 487 THR B O   
7757 C CB  . THR B 501 ? 0.3878 0.3157 0.6748 -0.0928 -0.0283 -0.0332 487 THR B CB  
7758 O OG1 . THR B 501 ? 0.3498 0.2896 0.6502 -0.1057 -0.0281 -0.0357 487 THR B OG1 
7759 C CG2 . THR B 501 ? 0.3121 0.2555 0.5963 -0.0916 -0.0349 -0.0435 487 THR B CG2 
7760 N N   . GLN B 502 ? 0.3909 0.3242 0.6837 -0.0891 -0.0213 -0.0055 488 GLN B N   
7761 C CA  . GLN B 502 ? 0.3455 0.2670 0.6386 -0.0921 -0.0139 0.0026  488 GLN B CA  
7762 C C   . GLN B 502 ? 0.3730 0.3024 0.6608 -0.0832 -0.0130 0.0124  488 GLN B C   
7763 O O   . GLN B 502 ? 0.3854 0.3083 0.6721 -0.0854 -0.0069 0.0195  488 GLN B O   
7764 C CB  . GLN B 502 ? 0.4295 0.3649 0.7332 -0.1031 -0.0122 -0.0004 488 GLN B CB  
7765 C CG  . GLN B 502 ? 0.4001 0.3361 0.7070 -0.1133 -0.0124 -0.0124 488 GLN B CG  
7766 C CD  . GLN B 502 ? 0.6121 0.5143 0.9073 -0.1176 -0.0050 -0.0157 488 GLN B CD  
7767 O OE1 . GLN B 502 ? 0.5735 0.4558 0.8578 -0.1215 0.0038  -0.0110 488 GLN B OE1 
7768 N NE2 . GLN B 502 ? 0.6192 0.5128 0.9150 -0.1170 -0.0079 -0.0242 488 GLN B NE2 
7769 N N   . ILE B 503 ? 0.3008 0.2451 0.5843 -0.0751 -0.0178 0.0118  489 ILE B N   
7770 C CA  . ILE B 503 ? 0.3218 0.2773 0.6005 -0.0692 -0.0156 0.0182  489 ILE B CA  
7771 C C   . ILE B 503 ? 0.3384 0.2817 0.6043 -0.0602 -0.0121 0.0233  489 ILE B C   
7772 O O   . ILE B 503 ? 0.3186 0.2661 0.5824 -0.0598 -0.0076 0.0301  489 ILE B O   
7773 C CB  . ILE B 503 ? 0.3189 0.2926 0.5946 -0.0657 -0.0199 0.0145  489 ILE B CB  
7774 C CG1 . ILE B 503 ? 0.3516 0.3361 0.6375 -0.0721 -0.0228 0.0135  489 ILE B CG1 
7775 C CG2 . ILE B 503 ? 0.3462 0.3316 0.6150 -0.0612 -0.0160 0.0178  489 ILE B CG2 
7776 C CD1 . ILE B 503 ? 0.2615 0.2582 0.5404 -0.0702 -0.0255 0.0118  489 ILE B CD1 
7777 N N   . PRO B 504 ? 0.3216 0.2505 0.5779 -0.0518 -0.0139 0.0203  490 PRO B N   
7778 C CA  . PRO B 504 ? 0.3396 0.2566 0.5822 -0.0396 -0.0112 0.0271  490 PRO B CA  
7779 C C   . PRO B 504 ? 0.3248 0.2214 0.5637 -0.0445 -0.0044 0.0368  490 PRO B C   
7780 O O   . PRO B 504 ? 0.4183 0.3176 0.6477 -0.0374 -0.0019 0.0453  490 PRO B O   
7781 C CB  . PRO B 504 ? 0.3236 0.2236 0.5588 -0.0299 -0.0137 0.0209  490 PRO B CB  
7782 C CG  . PRO B 504 ? 0.3748 0.2931 0.6180 -0.0347 -0.0190 0.0099  490 PRO B CG  
7783 C CD  . PRO B 504 ? 0.3610 0.2874 0.6171 -0.0502 -0.0187 0.0104  490 PRO B CD  
7784 N N   . GLN B 505 ? 0.3899 0.2689 0.6352 -0.0576 -0.0009 0.0350  491 GLN B N   
7785 C CA  . GLN B 505 ? 0.4467 0.3051 0.6863 -0.0647 0.0071  0.0433  491 GLN B CA  
7786 C C   . GLN B 505 ? 0.4312 0.3119 0.6799 -0.0729 0.0099  0.0475  491 GLN B C   
7787 O O   . GLN B 505 ? 0.4561 0.3255 0.6981 -0.0778 0.0168  0.0553  491 GLN B O   
7788 C CB  . GLN B 505 ? 0.4691 0.3033 0.7124 -0.0787 0.0119  0.0374  491 GLN B CB  
7789 C CG  . GLN B 505 ? 0.6206 0.4785 0.8853 -0.0929 0.0094  0.0276  491 GLN B CG  
7790 C CD  . GLN B 505 ? 0.7660 0.6375 1.0322 -0.1029 0.0146  0.0295  491 GLN B CD  
7791 O OE1 . GLN B 505 ? 0.7922 0.6447 1.0454 -0.1079 0.0227  0.0352  491 GLN B OE1 
7792 N NE2 . GLN B 505 ? 0.5822 0.4861 0.8601 -0.1039 0.0102  0.0253  491 GLN B NE2 
7793 N N   . ALA B 506 ? 0.3680 0.2781 0.6306 -0.0748 0.0057  0.0423  492 ALA B N   
7794 C CA  . ALA B 506 ? 0.4048 0.3353 0.6758 -0.0807 0.0092  0.0450  492 ALA B CA  
7795 C C   . ALA B 506 ? 0.4029 0.3488 0.6641 -0.0713 0.0097  0.0495  492 ALA B C   
7796 O O   . ALA B 506 ? 0.3343 0.2905 0.5965 -0.0759 0.0153  0.0535  492 ALA B O   
7797 C CB  . ALA B 506 ? 0.3496 0.3003 0.6385 -0.0863 0.0058  0.0378  492 ALA B CB  
7798 N N   . LEU B 507 ? 0.3278 0.2792 0.5805 -0.0592 0.0046  0.0472  493 LEU B N   
7799 C CA  . LEU B 507 ? 0.3316 0.3052 0.5766 -0.0512 0.0048  0.0481  493 LEU B CA  
7800 C C   . LEU B 507 ? 0.3942 0.3598 0.6216 -0.0377 0.0045  0.0556  493 LEU B C   
7801 O O   . LEU B 507 ? 0.3576 0.3459 0.5777 -0.0280 0.0030  0.0546  493 LEU B O   
7802 C CB  . LEU B 507 ? 0.2768 0.2682 0.5237 -0.0474 0.0002  0.0390  493 LEU B CB  
7803 C CG  . LEU B 507 ? 0.2873 0.2859 0.5471 -0.0579 0.0003  0.0336  493 LEU B CG  
7804 C CD1 . LEU B 507 ? 0.2221 0.2383 0.4779 -0.0555 -0.0017 0.0260  493 LEU B CD1 
7805 C CD2 . LEU B 507 ? 0.2704 0.2765 0.5390 -0.0675 0.0071  0.0363  493 LEU B CD2 
7806 N N   . SER B 508 ? 0.3643 0.2982 0.5834 -0.0365 0.0063  0.0626  494 SER B N   
7807 C CA  . SER B 508 ? 0.4746 0.3944 0.6734 -0.0216 0.0066  0.0726  494 SER B CA  
7808 C C   . SER B 508 ? 0.3967 0.2801 0.5868 -0.0295 0.0134  0.0821  494 SER B C   
7809 O O   . SER B 508 ? 0.4022 0.2667 0.6015 -0.0426 0.0161  0.0775  494 SER B O   
7810 C CB  . SER B 508 ? 0.4016 0.3127 0.5925 -0.0038 0.0003  0.0691  494 SER B CB  
7811 O OG  . SER B 508 ? 0.4872 0.3724 0.6574 0.0118  0.0012  0.0804  494 SER B OG  
7812 N N   . LEU B 509 ? 0.4669 0.3429 0.6385 -0.0224 0.0166  0.0947  495 LEU B N   
7813 C CA  . LEU B 509 ? 0.4463 0.2837 0.6041 -0.0304 0.0247  0.1050  495 LEU B CA  
7814 C C   . LEU B 509 ? 0.6354 0.4271 0.7773 -0.0202 0.0253  0.1087  495 LEU B C   
7815 O O   . LEU B 509 ? 0.6817 0.4346 0.8138 -0.0313 0.0338  0.1136  495 LEU B O   
7816 C CB  . LEU B 509 ? 0.4844 0.3278 0.6235 -0.0262 0.0283  0.1187  495 LEU B CB  
7817 C CG  . LEU B 509 ? 0.5108 0.3925 0.6632 -0.0406 0.0316  0.1154  495 LEU B CG  
7818 C CD1 . LEU B 509 ? 0.5619 0.4466 0.6926 -0.0375 0.0358  0.1292  495 LEU B CD1 
7819 C CD2 . LEU B 509 ? 0.4258 0.3025 0.5982 -0.0645 0.0379  0.1074  495 LEU B CD2 
7820 N N   . ASP B 510 ? 0.5700 0.3654 0.7090 -0.0004 0.0177  0.1051  496 ASP B N   
7821 C CA  . ASP B 510 ? 0.5587 0.3110 0.6837 0.0118  0.0185  0.1067  496 ASP B CA  
7822 C C   . ASP B 510 ? 0.4968 0.2699 0.6326 0.0256  0.0094  0.0940  496 ASP B C   
7823 O O   . ASP B 510 ? 0.5210 0.3008 0.6456 0.0499  0.0039  0.0971  496 ASP B O   
7824 C CB  . ASP B 510 ? 0.5652 0.2882 0.6592 0.0312  0.0208  0.1248  496 ASP B CB  
7825 C CG  . ASP B 510 ? 0.7065 0.3800 0.7839 0.0472  0.0226  0.1269  496 ASP B CG  
7826 O OD1 . ASP B 510 ? 0.7073 0.3589 0.7951 0.0346  0.0262  0.1153  496 ASP B OD1 
7827 O OD2 . ASP B 510 ? 0.6825 0.3398 0.7363 0.0729  0.0205  0.1398  496 ASP B OD2 
7828 N N   . PRO B 511 ? 0.5838 0.3720 0.7411 0.0114  0.0074  0.0793  497 PRO B N   
7829 C CA  . PRO B 511 ? 0.5745 0.3823 0.7403 0.0224  -0.0002 0.0668  497 PRO B CA  
7830 C C   . PRO B 511 ? 0.7156 0.4823 0.8711 0.0330  0.0015  0.0642  497 PRO B C   
7831 O O   . PRO B 511 ? 1.0104 0.7401 1.1641 0.0197  0.0087  0.0632  497 PRO B O   
7832 C CB  . PRO B 511 ? 0.5088 0.3399 0.6971 0.0019  -0.0017 0.0545  497 PRO B CB  
7833 C CG  . PRO B 511 ? 0.5131 0.3212 0.7048 -0.0182 0.0059  0.0578  497 PRO B CG  
7834 C CD  . PRO B 511 ? 0.4925 0.2790 0.6659 -0.0145 0.0122  0.0733  497 PRO B CD  
7835 N N   . GLN B 512 ? 1.0123 0.7862 1.1614 0.0566  -0.0042 0.0616  498 GLN B N   
7836 C CA  . GLN B 512 ? 1.0067 0.7435 1.1486 0.0675  -0.0023 0.0560  498 GLN B CA  
7837 C C   . GLN B 512 ? 0.9443 0.7024 1.1049 0.0591  -0.0064 0.0365  498 GLN B C   
7838 O O   . GLN B 512 ? 0.9749 0.7406 1.1357 0.0754  -0.0106 0.0273  498 GLN B O   
7839 C CB  . GLN B 512 ? 1.0402 0.7706 1.1646 0.1003  -0.0060 0.0631  498 GLN B CB  
7840 C CG  . GLN B 512 ? 1.2373 0.9065 1.3437 0.1136  0.0006  0.0668  498 GLN B CG  
7841 C CD  . GLN B 512 ? 1.2091 0.8828 1.3078 0.1481  -0.0056 0.0644  498 GLN B CD  
7842 O OE1 . GLN B 512 ? 1.2077 0.9350 1.3181 0.1585  -0.0149 0.0556  498 GLN B OE1 
7843 N NE2 . GLN B 512 ? 1.3026 0.9196 1.3811 0.1658  0.0004  0.0713  498 GLN B NE2 
7844 N N   . ALA B 513 ? 0.6540 0.4245 0.8301 0.0341  -0.0053 0.0298  499 ALA B N   
7845 C CA  . ALA B 513 ? 0.5919 0.3917 0.7839 0.0261  -0.0106 0.0136  499 ALA B CA  
7846 C C   . ALA B 513 ? 0.5897 0.3642 0.7874 0.0100  -0.0061 0.0034  499 ALA B C   
7847 O O   . ALA B 513 ? 0.7104 0.4567 0.9058 -0.0039 0.0012  0.0078  499 ALA B O   
7848 C CB  . ALA B 513 ? 0.4675 0.3092 0.6725 0.0127  -0.0145 0.0134  499 ALA B CB  
7849 N N   . GLN B 514 ? 0.5253 0.3133 0.7302 0.0101  -0.0100 -0.0119 500 GLN B N   
7850 C CA  . GLN B 514 ? 0.5425 0.3162 0.7543 -0.0064 -0.0066 -0.0249 500 GLN B CA  
7851 C C   . GLN B 514 ? 0.5171 0.3331 0.7436 -0.0199 -0.0137 -0.0342 500 GLN B C   
7852 O O   . GLN B 514 ? 0.4383 0.2838 0.6665 -0.0119 -0.0200 -0.0396 500 GLN B O   
7853 C CB  . GLN B 514 ? 0.4992 0.2468 0.7040 0.0061  -0.0037 -0.0358 500 GLN B CB  
7854 C CG  . GLN B 514 ? 0.5435 0.2483 0.7300 0.0264  0.0023  -0.0243 500 GLN B CG  
7855 C CD  . GLN B 514 ? 0.6182 0.2908 0.7975 0.0398  0.0067  -0.0355 500 GLN B CD  
7856 O OE1 . GLN B 514 ? 0.7100 0.3297 0.8746 0.0445  0.0165  -0.0304 500 GLN B OE1 
7857 N NE2 . GLN B 514 ? 0.5673 0.2698 0.7559 0.0456  0.0007  -0.0512 500 GLN B NE2 
7858 N N   . CYS B 515 ? 0.4330 0.2525 0.6690 -0.0401 -0.0124 -0.0360 501 CYS B N   
7859 C CA  . CYS B 515 ? 0.3946 0.2515 0.6423 -0.0515 -0.0193 -0.0417 501 CYS B CA  
7860 C C   . CYS B 515 ? 0.4456 0.3012 0.7006 -0.0674 -0.0183 -0.0560 501 CYS B C   
7861 O O   . CYS B 515 ? 0.4459 0.2753 0.7011 -0.0774 -0.0107 -0.0588 501 CYS B O   
7862 C CB  . CYS B 515 ? 0.3604 0.2332 0.6145 -0.0584 -0.0204 -0.0300 501 CYS B CB  
7863 S SG  . CYS B 515 ? 0.5305 0.4053 0.7755 -0.0426 -0.0196 -0.0148 501 CYS B SG  
7864 N N   . TRP B 516 ? 0.4199 0.3046 0.6794 -0.0709 -0.0253 -0.0656 502 TRP B N   
7865 C CA  . TRP B 516 ? 0.3983 0.2926 0.6650 -0.0864 -0.0262 -0.0799 502 TRP B CA  
7866 C C   . TRP B 516 ? 0.4560 0.3897 0.7288 -0.0925 -0.0355 -0.0786 502 TRP B C   
7867 O O   . TRP B 516 ? 0.4811 0.4317 0.7496 -0.0841 -0.0404 -0.0712 502 TRP B O   
7868 C CB  . TRP B 516 ? 0.4402 0.3282 0.7026 -0.0839 -0.0249 -0.0962 502 TRP B CB  
7869 C CG  . TRP B 516 ? 0.4679 0.3126 0.7231 -0.0775 -0.0149 -0.1002 502 TRP B CG  
7870 C CD1 . TRP B 516 ? 0.5303 0.3481 0.7862 -0.0898 -0.0059 -0.1118 502 TRP B CD1 
7871 C CD2 . TRP B 516 ? 0.5292 0.3518 0.7740 -0.0563 -0.0125 -0.0932 502 TRP B CD2 
7872 N NE1 . TRP B 516 ? 0.5025 0.2764 0.7472 -0.0771 0.0029  -0.1110 502 TRP B NE1 
7873 C CE2 . TRP B 516 ? 0.5490 0.3265 0.7869 -0.0548 -0.0019 -0.0991 502 TRP B CE2 
7874 C CE3 . TRP B 516 ? 0.4330 0.2706 0.6731 -0.0385 -0.0177 -0.0833 502 TRP B CE3 
7875 C CZ2 . TRP B 516 ? 0.5209 0.2667 0.7466 -0.0328 0.0022  -0.0932 502 TRP B CZ2 
7876 C CZ3 . TRP B 516 ? 0.4960 0.3090 0.7261 -0.0179 -0.0142 -0.0792 502 TRP B CZ3 
7877 C CH2 . TRP B 516 ? 0.5244 0.2913 0.7470 -0.0135 -0.0050 -0.0831 502 TRP B CH2 
7878 N N   . ARG B 517 ? 0.4398 0.3881 0.7216 -0.1070 -0.0373 -0.0865 503 ARG B N   
7879 C CA  . ARG B 517 ? 0.4978 0.4829 0.7830 -0.1115 -0.0469 -0.0872 503 ARG B CA  
7880 C C   . ARG B 517 ? 0.4992 0.4963 0.7840 -0.1203 -0.0486 -0.1054 503 ARG B C   
7881 O O   . ARG B 517 ? 0.4947 0.4818 0.7852 -0.1316 -0.0428 -0.1179 503 ARG B O   
7882 C CB  . ARG B 517 ? 0.4776 0.4779 0.7748 -0.1191 -0.0491 -0.0814 503 ARG B CB  
7883 C CG  . ARG B 517 ? 0.5809 0.6185 0.8818 -0.1235 -0.0591 -0.0844 503 ARG B CG  
7884 C CD  . ARG B 517 ? 0.8222 0.8770 1.1384 -0.1324 -0.0603 -0.0858 503 ARG B CD  
7885 N NE  . ARG B 517 ? 0.8031 0.8426 1.1252 -0.1295 -0.0548 -0.0742 503 ARG B NE  
7886 C CZ  . ARG B 517 ? 0.8227 0.8438 1.1514 -0.1386 -0.0455 -0.0782 503 ARG B CZ  
7887 N NH1 . ARG B 517 ? 0.8074 0.8197 1.1376 -0.1517 -0.0394 -0.0938 503 ARG B NH1 
7888 N NH2 . ARG B 517 ? 0.7799 0.7899 1.1122 -0.1359 -0.0409 -0.0669 503 ARG B NH2 
7889 N N   . VAL B 518 ? 0.3707 0.3885 0.6475 -0.1168 -0.0551 -0.1079 504 VAL B N   
7890 C CA  . VAL B 518 ? 0.4507 0.4813 0.7250 -0.1246 -0.0564 -0.1259 504 VAL B CA  
7891 C C   . VAL B 518 ? 0.4980 0.5667 0.7688 -0.1293 -0.0669 -0.1250 504 VAL B C   
7892 O O   . VAL B 518 ? 0.3920 0.4708 0.6552 -0.1219 -0.0722 -0.1110 504 VAL B O   
7893 C CB  . VAL B 518 ? 0.4548 0.4722 0.7199 -0.1155 -0.0527 -0.1332 504 VAL B CB  
7894 C CG1 . VAL B 518 ? 0.3821 0.3601 0.6482 -0.1075 -0.0430 -0.1328 504 VAL B CG1 
7895 C CG2 . VAL B 518 ? 0.4205 0.4519 0.6752 -0.1055 -0.0576 -0.1225 504 VAL B CG2 
7896 N N   . SER B 519 ? 0.3538 0.4429 0.6286 -0.1420 -0.0692 -0.1403 505 SER B N   
7897 C CA  . SER B 519 ? 0.4137 0.5409 0.6826 -0.1463 -0.0796 -0.1413 505 SER B CA  
7898 C C   . SER B 519 ? 0.4641 0.6055 0.7268 -0.1551 -0.0794 -0.1610 505 SER B C   
7899 O O   . SER B 519 ? 0.4766 0.6507 0.7311 -0.1594 -0.0880 -0.1626 505 SER B O   
7900 C CB  . SER B 519 ? 0.4293 0.5817 0.7103 -0.1535 -0.0851 -0.1409 505 SER B CB  
7901 O OG  . SER B 519 ? 0.6915 0.8364 0.9861 -0.1663 -0.0773 -0.1572 505 SER B OG  
7902 N N   . GLU B 520 ? 0.4352 0.5525 0.7004 -0.1573 -0.0697 -0.1759 506 GLU B N   
7903 C CA  . GLU B 520 ? 0.4712 0.5998 0.7324 -0.1661 -0.0675 -0.1976 506 GLU B CA  
7904 C C   . GLU B 520 ? 0.3906 0.4985 0.6441 -0.1553 -0.0620 -0.2007 506 GLU B C   
7905 O O   . GLU B 520 ? 0.4746 0.5504 0.7302 -0.1433 -0.0562 -0.1925 506 GLU B O   
7906 C CB  . GLU B 520 ? 0.4791 0.5976 0.7488 -0.1787 -0.0585 -0.2154 506 GLU B CB  
7907 C CG  . GLU B 520 ? 0.4871 0.6291 0.7611 -0.1876 -0.0622 -0.2121 506 GLU B CG  
7908 C CD  . GLU B 520 ? 0.7072 0.8932 0.9720 -0.1942 -0.0706 -0.2178 506 GLU B CD  
7909 O OE1 . GLU B 520 ? 0.8237 1.0133 1.0809 -0.1997 -0.0659 -0.2335 506 GLU B OE1 
7910 O OE2 . GLU B 520 ? 0.7402 0.9574 1.0056 -0.1932 -0.0818 -0.2069 506 GLU B OE2 
7911 N N   . ALA B 521 ? 0.5742 0.5413 0.6749 -0.1314 -0.0228 -0.2663 507 ALA B N   
7912 C CA  . ALA B 521 ? 0.6716 0.6188 0.7585 -0.1177 -0.0132 -0.2661 507 ALA B CA  
7913 C C   . ALA B 521 ? 0.5827 0.4903 0.6786 -0.1174 -0.0083 -0.2703 507 ALA B C   
7914 O O   . ALA B 521 ? 0.5685 0.4541 0.6667 -0.1090 0.0013  -0.2608 507 ALA B O   
7915 C CB  . ALA B 521 ? 0.7121 0.6812 0.7719 -0.1074 -0.0160 -0.2801 507 ALA B CB  
7916 N N   . GLU B 522 ? 0.5962 0.4939 0.6960 -0.1256 -0.0157 -0.2829 508 GLU B N   
7917 C CA  . GLU B 522 ? 0.6658 0.5210 0.7712 -0.1256 -0.0127 -0.2852 508 GLU B CA  
7918 C C   . GLU B 522 ? 0.5857 0.4201 0.7106 -0.1317 -0.0057 -0.2623 508 GLU B C   
7919 O O   . GLU B 522 ? 0.7353 0.5368 0.8607 -0.1237 0.0016  -0.2560 508 GLU B O   
7920 C CB  . GLU B 522 ? 0.6303 0.4781 0.7373 -0.1376 -0.0234 -0.3023 508 GLU B CB  
7921 C CG  . GLU B 522 ? 0.8079 0.6532 0.8932 -0.1270 -0.0278 -0.3274 508 GLU B CG  
7922 C CD  . GLU B 522 ? 1.0431 0.8882 1.1296 -0.1406 -0.0404 -0.3454 508 GLU B CD  
7923 O OE1 . GLU B 522 ? 1.0466 0.8651 1.1494 -0.1560 -0.0431 -0.3411 508 GLU B OE1 
7924 O OE2 . GLU B 522 ? 1.1539 1.0266 1.2244 -0.1363 -0.0476 -0.3634 508 GLU B OE2 
7925 N N   . GLN B 523 ? 0.6109 0.4669 0.7512 -0.1444 -0.0078 -0.2499 509 GLN B N   
7926 C CA  . GLN B 523 ? 0.5895 0.4338 0.7472 -0.1496 -0.0004 -0.2274 509 GLN B CA  
7927 C C   . GLN B 523 ? 0.6424 0.4818 0.7944 -0.1342 0.0096  -0.2144 509 GLN B C   
7928 O O   . GLN B 523 ? 0.5552 0.3680 0.7129 -0.1302 0.0174  -0.2012 509 GLN B O   
7929 C CB  . GLN B 523 ? 0.5428 0.4214 0.7167 -0.1634 -0.0048 -0.2198 509 GLN B CB  
7930 C CG  . GLN B 523 ? 0.7417 0.6144 0.9371 -0.1745 0.0010  -0.2001 509 GLN B CG  
7931 C CD  . GLN B 523 ? 0.8420 0.7581 1.0525 -0.1831 -0.0022 -0.1939 509 GLN B CD  
7932 O OE1 . GLN B 523 ? 0.8023 0.7500 1.0058 -0.1794 -0.0096 -0.2036 509 GLN B OE1 
7933 N NE2 . GLN B 523 ? 0.7811 0.7010 1.0121 -0.1940 0.0033  -0.1776 509 GLN B NE2 
7934 N N   . LEU B 524 ? 0.4857 0.3505 0.6255 -0.1258 0.0090  -0.2181 510 LEU B N   
7935 C CA  . LEU B 524 ? 0.5606 0.4236 0.6932 -0.1118 0.0174  -0.2062 510 LEU B CA  
7936 C C   . LEU B 524 ? 0.5799 0.4143 0.7060 -0.0994 0.0236  -0.2141 510 LEU B C   
7937 O O   . LEU B 524 ? 0.5318 0.3512 0.6610 -0.0902 0.0312  -0.1994 510 LEU B O   
7938 C CB  . LEU B 524 ? 0.5346 0.4316 0.6492 -0.1043 0.0140  -0.2034 510 LEU B CB  
7939 C CG  . LEU B 524 ? 0.4989 0.4004 0.6021 -0.0901 0.0209  -0.1892 510 LEU B CG  
7940 C CD1 . LEU B 524 ? 0.4299 0.3232 0.5445 -0.0885 0.0260  -0.1682 510 LEU B CD1 
7941 C CD2 . LEU B 524 ? 0.4158 0.3468 0.5016 -0.0870 0.0168  -0.1855 510 LEU B CD2 
7942 N N   . ALA B 525 ? 0.5121 0.3435 0.6261 -0.0955 0.0195  -0.2345 511 ALA B N   
7943 C CA  . ALA B 525 ? 0.5720 0.3791 0.6782 -0.0801 0.0246  -0.2430 511 ALA B CA  
7944 C C   . ALA B 525 ? 0.6108 0.3775 0.7279 -0.0808 0.0271  -0.2329 511 ALA B C   
7945 O O   . ALA B 525 ? 0.6301 0.3776 0.7468 -0.0664 0.0343  -0.2269 511 ALA B O   
7946 C CB  . ALA B 525 ? 0.5904 0.4025 0.6806 -0.0759 0.0187  -0.2680 511 ALA B CB  
7947 N N   . ASP B 526 ? 0.6363 0.3912 0.7632 -0.0975 0.0213  -0.2306 512 ASP B N   
7948 C CA  . ASP B 526 ? 0.6568 0.3727 0.7932 -0.1014 0.0239  -0.2185 512 ASP B CA  
7949 C C   . ASP B 526 ? 0.6508 0.3666 0.7977 -0.0983 0.0329  -0.1936 512 ASP B C   
7950 O O   . ASP B 526 ? 0.6259 0.3111 0.7735 -0.0886 0.0387  -0.1834 512 ASP B O   
7951 C CB  . ASP B 526 ? 0.6581 0.3682 0.8049 -0.1237 0.0163  -0.2202 512 ASP B CB  
7952 C CG  . ASP B 526 ? 0.8047 0.5067 0.9405 -0.1265 0.0067  -0.2456 512 ASP B CG  
7953 O OD1 . ASP B 526 ? 0.9807 0.6714 1.1001 -0.1094 0.0074  -0.2606 512 ASP B OD1 
7954 O OD2 . ASP B 526 ? 0.8984 0.6075 1.0421 -0.1454 -0.0014 -0.2512 512 ASP B OD2 
7955 N N   . VAL B 527 ? 0.5619 0.3111 0.7160 -0.1051 0.0337  -0.1838 513 VAL B N   
7956 C CA  . VAL B 527 ? 0.5154 0.2668 0.6784 -0.1020 0.0418  -0.1616 513 VAL B CA  
7957 C C   . VAL B 527 ? 0.6006 0.3486 0.7549 -0.0814 0.0482  -0.1601 513 VAL B C   
7958 O O   . VAL B 527 ? 0.5535 0.2880 0.7099 -0.0720 0.0545  -0.1428 513 VAL B O   
7959 C CB  . VAL B 527 ? 0.5693 0.3573 0.7403 -0.1126 0.0399  -0.1546 513 VAL B CB  
7960 C CG1 . VAL B 527 ? 0.5352 0.3360 0.7042 -0.1016 0.0459  -0.1326 513 VAL B CG1 
7961 C CG2 . VAL B 527 ? 0.5836 0.3758 0.7696 -0.1322 0.0364  -0.1501 513 VAL B CG2 
7962 N N   . LEU B 528 ? 0.5695 0.3378 0.7098 -0.0723 0.0457  -0.1739 514 LEU B N   
7963 C CA  . LEU B 528 ? 0.5746 0.3510 0.7046 -0.0522 0.0505  -0.1699 514 LEU B CA  
7964 C C   . LEU B 528 ? 0.5251 0.2656 0.6556 -0.0380 0.0548  -0.1746 514 LEU B C   
7965 O O   . LEU B 528 ? 0.6134 0.3538 0.7426 -0.0222 0.0599  -0.1622 514 LEU B O   
7966 C CB  . LEU B 528 ? 0.5152 0.3227 0.6310 -0.0479 0.0478  -0.1832 514 LEU B CB  
7967 C CG  . LEU B 528 ? 0.4407 0.2825 0.5529 -0.0565 0.0442  -0.1732 514 LEU B CG  
7968 C CD1 . LEU B 528 ? 0.4883 0.3558 0.5853 -0.0559 0.0409  -0.1864 514 LEU B CD1 
7969 C CD2 . LEU B 528 ? 0.4123 0.2668 0.5251 -0.0494 0.0480  -0.1528 514 LEU B CD2 
7970 N N   . GLU B 529 ? 0.5772 0.2886 0.7071 -0.0420 0.0513  -0.1914 515 GLU B N   
7971 C CA  . GLU B 529 ? 0.6017 0.2740 0.7282 -0.0277 0.0532  -0.1917 515 GLU B CA  
7972 C C   . GLU B 529 ? 0.7377 0.3855 0.8744 -0.0289 0.0579  -0.1668 515 GLU B C   
7973 O O   . GLU B 529 ? 0.6352 0.2639 0.7703 -0.0098 0.0630  -0.1588 515 GLU B O   
7974 C CB  . GLU B 529 ? 0.7292 0.3761 0.8479 -0.0344 0.0453  -0.2087 515 GLU B CB  
7975 C CG  . GLU B 529 ? 0.9115 0.5794 1.0166 -0.0290 0.0411  -0.2347 515 GLU B CG  
7976 C CD  . GLU B 529 ? 1.1391 0.7797 1.2359 -0.0360 0.0325  -0.2522 515 GLU B CD  
7977 O OE1 . GLU B 529 ? 1.0736 0.6686 1.1686 -0.0324 0.0316  -0.2495 515 GLU B OE1 
7978 O OE2 . GLU B 529 ? 1.1395 0.8029 1.2303 -0.0451 0.0261  -0.2685 515 GLU B OE2 
7979 N N   . LYS B 530 ? 0.7219 0.3730 0.8690 -0.0501 0.0565  -0.1539 516 LYS B N   
7980 C CA  . LYS B 530 ? 0.6090 0.2388 0.7651 -0.0535 0.0618  -0.1293 516 LYS B CA  
7981 C C   . LYS B 530 ? 0.6121 0.2569 0.7699 -0.0378 0.0696  -0.1126 516 LYS B C   
7982 O O   . LYS B 530 ? 0.6983 0.3205 0.8557 -0.0261 0.0747  -0.0953 516 LYS B O   
7983 C CB  . LYS B 530 ? 0.6906 0.3325 0.8587 -0.0794 0.0596  -0.1206 516 LYS B CB  
7984 C CG  . LYS B 530 ? 0.7538 0.3827 0.9325 -0.0860 0.0668  -0.0933 516 LYS B CG  
7985 C CD  . LYS B 530 ? 0.7752 0.3551 0.9488 -0.0793 0.0684  -0.0846 516 LYS B CD  
7986 C CE  . LYS B 530 ? 0.6832 0.2499 0.8673 -0.0965 0.0731  -0.0603 516 LYS B CE  
7987 N NZ  . LYS B 530 ? 0.7665 0.2932 0.9489 -0.1106 0.0671  -0.0648 516 LYS B NZ  
7988 N N   . VAL B 531 ? 0.5350 0.2256 0.6874 -0.0356 0.0675  -0.1138 517 VAL B N   
7989 C CA  . VAL B 531 ? 0.6069 0.3247 0.7551 -0.0228 0.0703  -0.0962 517 VAL B CA  
7990 C C   . VAL B 531 ? 0.5021 0.2318 0.6410 -0.0008 0.0709  -0.1032 517 VAL B C   
7991 O O   . VAL B 531 ? 0.5916 0.3497 0.7274 0.0085  0.0716  -0.0928 517 VAL B O   
7992 C CB  . VAL B 531 ? 0.6800 0.4373 0.8287 -0.0342 0.0672  -0.0916 517 VAL B CB  
7993 C CG1 . VAL B 531 ? 0.6212 0.3743 0.7811 -0.0544 0.0669  -0.0856 517 VAL B CG1 
7994 C CG2 . VAL B 531 ? 0.4871 0.2692 0.6283 -0.0358 0.0622  -0.1095 517 VAL B CG2 
7995 N N   . ALA B 532 ? 0.6379 0.3479 0.7731 0.0083  0.0706  -0.1212 518 ALA B N   
7996 C CA  . ALA B 532 ? 0.7027 0.4346 0.8304 0.0281  0.0715  -0.1311 518 ALA B CA  
7997 C C   . ALA B 532 ? 0.6992 0.4403 0.8269 0.0479  0.0747  -0.1142 518 ALA B C   
7998 O O   . ALA B 532 ? 0.6765 0.4570 0.8021 0.0563  0.0746  -0.1138 518 ALA B O   
7999 C CB  . ALA B 532 ? 0.6198 0.3248 0.7431 0.0381  0.0712  -0.1536 518 ALA B CB  
8000 N N   . HIS B 533 ? 0.7212 0.4277 0.8513 0.0549  0.0772  -0.0996 519 HIS B N   
8001 C CA  . HIS B 533 ? 0.5547 0.2674 0.6830 0.0774  0.0795  -0.0842 519 HIS B CA  
8002 C C   . HIS B 533 ? 0.5537 0.2856 0.6833 0.0714  0.0798  -0.0615 519 HIS B C   
8003 O O   . HIS B 533 ? 0.5406 0.2712 0.6678 0.0883  0.0815  -0.0452 519 HIS B O   
8004 C CB  . HIS B 533 ? 0.6091 0.2701 0.7356 0.0936  0.0819  -0.0807 519 HIS B CB  
8005 C CG  . HIS B 533 ? 0.6980 0.3360 0.8215 0.1026  0.0810  -0.1057 519 HIS B CG  
8006 N ND1 . HIS B 533 ? 0.9237 0.5243 1.0486 0.0858  0.0792  -0.1203 519 HIS B ND1 
8007 C CD2 . HIS B 533 ? 0.9304 0.5816 1.0496 0.1272  0.0812  -0.1205 519 HIS B CD2 
8008 C CE1 . HIS B 533 ? 0.8301 0.4182 0.9495 0.1006  0.0781  -0.1439 519 HIS B CE1 
8009 N NE2 . HIS B 533 ? 0.9666 0.5860 1.0825 0.1266  0.0799  -0.1441 519 HIS B NE2 
8010 N N   . HIS B 534 ? 0.5287 0.2797 0.6607 0.0499  0.0779  -0.0609 520 HIS B N   
8011 C CA  . HIS B 534 ? 0.5443 0.3219 0.6761 0.0448  0.0772  -0.0448 520 HIS B CA  
8012 C C   . HIS B 534 ? 0.4909 0.2540 0.6205 0.0565  0.0809  -0.0223 520 HIS B C   
8013 O O   . HIS B 534 ? 0.5156 0.3045 0.6409 0.0690  0.0797  -0.0119 520 HIS B O   
8014 C CB  . HIS B 534 ? 0.4594 0.2815 0.5884 0.0497  0.0732  -0.0501 520 HIS B CB  
8015 C CG  . HIS B 534 ? 0.4971 0.3323 0.6247 0.0721  0.0734  -0.0521 520 HIS B CG  
8016 N ND1 . HIS B 534 ? 0.5300 0.3677 0.6581 0.0800  0.0740  -0.0686 520 HIS B ND1 
8017 C CD2 . HIS B 534 ? 0.4992 0.3503 0.6251 0.0896  0.0728  -0.0402 520 HIS B CD2 
8018 C CE1 . HIS B 534 ? 0.5137 0.3696 0.6423 0.1016  0.0742  -0.0666 520 HIS B CE1 
8019 N NE2 . HIS B 534 ? 0.6484 0.5128 0.7758 0.1075  0.0728  -0.0494 520 HIS B NE2 
8020 N N   . GLU B 535 ? 0.5370 0.2583 0.6693 0.0515  0.0850  -0.0143 521 GLU B N   
8021 C CA  . GLU B 535 ? 0.5509 0.2565 0.6800 0.0594  0.0897  0.0110  521 GLU B CA  
8022 C C   . GLU B 535 ? 0.5260 0.2586 0.6555 0.0468  0.0911  0.0251  521 GLU B C   
8023 O O   . GLU B 535 ? 0.5433 0.2810 0.6666 0.0566  0.0944  0.0463  521 GLU B O   
8024 C CB  . GLU B 535 ? 0.6019 0.2515 0.7343 0.0543  0.0941  0.0172  521 GLU B CB  
8025 C CG  . GLU B 535 ? 0.6395 0.2570 0.7696 0.0703  0.0925  0.0017  521 GLU B CG  
8026 C CD  . GLU B 535 ? 0.8139 0.3698 0.9436 0.0725  0.0965  0.0137  521 GLU B CD  
8027 O OE1 . GLU B 535 ? 1.0910 0.6166 1.2289 0.0484  0.0977  0.0110  521 GLU B OE1 
8028 O OE2 . GLU B 535 ? 1.0823 0.6197 1.2038 0.0979  0.0979  0.0262  521 GLU B OE2 
8029 N N   . ARG B 536 ? 0.4995 0.2509 0.6347 0.0276  0.0884  0.0136  522 ARG B N   
8030 C CA  . ARG B 536 ? 0.5120 0.2905 0.6478 0.0174  0.0893  0.0236  522 ARG B CA  
8031 C C   . ARG B 536 ? 0.4351 0.2450 0.5711 0.0097  0.0826  0.0061  522 ARG B C   
8032 O O   . ARG B 536 ? 0.4769 0.2849 0.6142 0.0070  0.0786  -0.0120 522 ARG B O   
8033 C CB  . ARG B 536 ? 0.5600 0.3188 0.7057 -0.0025 0.0950  0.0332  522 ARG B CB  
8034 C CG  . ARG B 536 ? 0.6808 0.4153 0.8246 0.0022  0.1031  0.0590  522 ARG B CG  
8035 C CD  . ARG B 536 ? 0.9027 0.5970 1.0589 -0.0179 0.1077  0.0624  522 ARG B CD  
8036 N NE  . ARG B 536 ? 1.0527 0.7202 1.2063 -0.0152 0.1163  0.0905  522 ARG B NE  
8037 C CZ  . ARG B 536 ? 1.0786 0.6938 1.2314 -0.0114 0.1186  0.0964  522 ARG B CZ  
8038 N NH1 . ARG B 536 ? 1.0915 0.6759 1.2468 -0.0101 0.1131  0.0738  522 ARG B NH1 
8039 N NH2 . ARG B 536 ? 1.2009 0.7929 1.3491 -0.0082 0.1267  0.1260  522 ARG B NH2 
8040 N N   . LEU B 537 ? 0.4130 0.2522 0.5459 0.0083  0.0813  0.0121  523 LEU B N   
8041 C CA  . LEU B 537 ? 0.3872 0.2499 0.5198 0.0002  0.0747  -0.0021 523 LEU B CA  
8042 C C   . LEU B 537 ? 0.4272 0.2800 0.5694 -0.0184 0.0745  -0.0112 523 LEU B C   
8043 O O   . LEU B 537 ? 0.4467 0.2897 0.5975 -0.0287 0.0795  -0.0024 523 LEU B O   
8044 C CB  . LEU B 537 ? 0.3662 0.2570 0.4929 0.0038  0.0732  0.0052  523 LEU B CB  
8045 C CG  . LEU B 537 ? 0.4453 0.3562 0.5689 -0.0010 0.0654  -0.0081 523 LEU B CG  
8046 C CD1 . LEU B 537 ? 0.3568 0.2899 0.4696 0.0110  0.0608  -0.0065 523 LEU B CD1 
8047 C CD2 . LEU B 537 ? 0.3540 0.2707 0.4846 -0.0140 0.0659  -0.0093 523 LEU B CD2 
8048 N N   . SER B 538 ? 0.4651 0.3226 0.6064 -0.0235 0.0687  -0.0283 524 SER B N   
8049 C CA  . SER B 538 ? 0.4822 0.3342 0.6309 -0.0394 0.0667  -0.0394 524 SER B CA  
8050 C C   . SER B 538 ? 0.5429 0.4199 0.6876 -0.0437 0.0600  -0.0470 524 SER B C   
8051 O O   . SER B 538 ? 0.4961 0.3838 0.6315 -0.0369 0.0558  -0.0518 524 SER B O   
8052 C CB  . SER B 538 ? 0.4736 0.3042 0.6224 -0.0401 0.0660  -0.0537 524 SER B CB  
8053 O OG  . SER B 538 ? 0.7091 0.5162 0.8572 -0.0286 0.0709  -0.0474 524 SER B OG  
8054 N N   . LEU B 539 ? 0.4546 0.3413 0.6068 -0.0549 0.0588  -0.0471 525 LEU B N   
8055 C CA  . LEU B 539 ? 0.4209 0.3286 0.5691 -0.0576 0.0517  -0.0540 525 LEU B CA  
8056 C C   . LEU B 539 ? 0.4658 0.3726 0.6215 -0.0712 0.0483  -0.0656 525 LEU B C   
8057 O O   . LEU B 539 ? 0.3882 0.2962 0.5575 -0.0821 0.0507  -0.0633 525 LEU B O   
8058 C CB  . LEU B 539 ? 0.3728 0.3016 0.5222 -0.0538 0.0520  -0.0441 525 LEU B CB  
8059 C CG  . LEU B 539 ? 0.4426 0.3881 0.5830 -0.0494 0.0437  -0.0500 525 LEU B CG  
8060 C CD1 . LEU B 539 ? 0.4158 0.3746 0.5493 -0.0370 0.0434  -0.0425 525 LEU B CD1 
8061 C CD2 . LEU B 539 ? 0.4348 0.3946 0.5835 -0.0585 0.0398  -0.0557 525 LEU B CD2 
8062 N N   . ILE B 540 ? 0.4639 0.3709 0.6109 -0.0715 0.0429  -0.0780 526 ILE B N   
8063 C CA  . ILE B 540 ? 0.4970 0.4064 0.6476 -0.0826 0.0382  -0.0913 526 ILE B CA  
8064 C C   . ILE B 540 ? 0.5210 0.4537 0.6647 -0.0815 0.0304  -0.0931 526 ILE B C   
8065 O O   . ILE B 540 ? 0.3804 0.3157 0.5095 -0.0746 0.0271  -0.0936 526 ILE B O   
8066 C CB  . ILE B 540 ? 0.4435 0.3377 0.5869 -0.0818 0.0381  -0.1045 526 ILE B CB  
8067 C CG1 . ILE B 540 ? 0.4106 0.2783 0.5590 -0.0781 0.0452  -0.1020 526 ILE B CG1 
8068 C CG2 . ILE B 540 ? 0.5037 0.4023 0.6492 -0.0928 0.0322  -0.1203 526 ILE B CG2 
8069 C CD1 . ILE B 540 ? 0.4746 0.3313 0.6136 -0.0699 0.0463  -0.1133 526 ILE B CD1 
8070 N N   . GLU B 541 ? 0.4423 0.3924 0.5968 -0.0884 0.0275  -0.0930 527 GLU B N   
8071 C CA  . GLU B 541 ? 0.4292 0.4019 0.5778 -0.0851 0.0192  -0.0947 527 GLU B CA  
8072 C C   . GLU B 541 ? 0.4239 0.4014 0.5683 -0.0921 0.0125  -0.1089 527 GLU B C   
8073 O O   . GLU B 541 ? 0.4492 0.4341 0.6070 -0.1039 0.0106  -0.1174 527 GLU B O   
8074 C CB  . GLU B 541 ? 0.3504 0.3468 0.5136 -0.0866 0.0193  -0.0884 527 GLU B CB  
8075 C CG  . GLU B 541 ? 0.3979 0.4175 0.5543 -0.0776 0.0106  -0.0886 527 GLU B CG  
8076 C CD  . GLU B 541 ? 0.4888 0.5393 0.6621 -0.0776 0.0112  -0.0840 527 GLU B CD  
8077 O OE1 . GLU B 541 ? 0.4132 0.4682 0.6044 -0.0880 0.0189  -0.0795 527 GLU B OE1 
8078 O OE2 . GLU B 541 ? 0.4556 0.5268 0.6243 -0.0670 0.0040  -0.0842 527 GLU B OE2 
8079 N N   . VAL B 542 ? 0.4198 0.3949 0.5453 -0.0856 0.0086  -0.1113 528 VAL B N   
8080 C CA  . VAL B 542 ? 0.3864 0.3672 0.5026 -0.0897 0.0030  -0.1240 528 VAL B CA  
8081 C C   . VAL B 542 ? 0.4491 0.4540 0.5599 -0.0866 -0.0068 -0.1235 528 VAL B C   
8082 O O   . VAL B 542 ? 0.4624 0.4686 0.5607 -0.0766 -0.0098 -0.1135 528 VAL B O   
8083 C CB  . VAL B 542 ? 0.3782 0.3476 0.4764 -0.0844 0.0056  -0.1248 528 VAL B CB  
8084 C CG1 . VAL B 542 ? 0.4080 0.3862 0.4950 -0.0877 0.0012  -0.1387 528 VAL B CG1 
8085 C CG2 . VAL B 542 ? 0.3669 0.3161 0.4709 -0.0831 0.0148  -0.1235 528 VAL B CG2 
8086 N N   . MET B 543 ? 0.4655 0.4884 0.5853 -0.0949 -0.0127 -0.1349 529 MET B N   
8087 C CA  . MET B 543 ? 0.3643 0.4156 0.4811 -0.0909 -0.0231 -0.1355 529 MET B CA  
8088 C C   . MET B 543 ? 0.5321 0.5876 0.6253 -0.0868 -0.0294 -0.1410 529 MET B C   
8089 O O   . MET B 543 ? 0.4483 0.5052 0.5392 -0.0943 -0.0307 -0.1558 529 MET B O   
8090 C CB  . MET B 543 ? 0.4194 0.4944 0.5596 -0.1032 -0.0270 -0.1456 529 MET B CB  
8091 C CG  . MET B 543 ? 0.4000 0.4815 0.5634 -0.1067 -0.0209 -0.1366 529 MET B CG  
8092 S SD  . MET B 543 ? 0.6749 0.7684 0.8309 -0.0867 -0.0222 -0.1200 529 MET B SD  
8093 C CE  . MET B 543 ? 0.6237 0.7157 0.8017 -0.0914 -0.0102 -0.1099 529 MET B CE  
8094 N N   . LEU B 544 ? 0.4359 0.4926 0.5105 -0.0745 -0.0336 -0.1292 530 LEU B N   
8095 C CA  . LEU B 544 ? 0.4558 0.5160 0.5052 -0.0702 -0.0384 -0.1293 530 LEU B CA  
8096 C C   . LEU B 544 ? 0.4373 0.5164 0.4758 -0.0589 -0.0496 -0.1219 530 LEU B C   
8097 O O   . LEU B 544 ? 0.4938 0.5759 0.5408 -0.0510 -0.0520 -0.1139 530 LEU B O   
8098 C CB  . LEU B 544 ? 0.3851 0.4205 0.4181 -0.0673 -0.0308 -0.1185 530 LEU B CB  
8099 C CG  . LEU B 544 ? 0.4756 0.4960 0.5154 -0.0748 -0.0204 -0.1262 530 LEU B CG  
8100 C CD1 . LEU B 544 ? 0.3998 0.4011 0.4314 -0.0719 -0.0132 -0.1136 530 LEU B CD1 
8101 C CD2 . LEU B 544 ? 0.4729 0.5039 0.5036 -0.0790 -0.0210 -0.1419 530 LEU B CD2 
8102 N N   . PRO B 545 ? 0.4228 0.5169 0.4415 -0.0558 -0.0567 -0.1247 531 PRO B N   
8103 C CA  . PRO B 545 ? 0.4116 0.5242 0.4182 -0.0425 -0.0685 -0.1166 531 PRO B CA  
8104 C C   . PRO B 545 ? 0.5896 0.6764 0.5804 -0.0300 -0.0681 -0.0959 531 PRO B C   
8105 O O   . PRO B 545 ? 0.4617 0.5202 0.4429 -0.0334 -0.0601 -0.0874 531 PRO B O   
8106 C CB  . PRO B 545 ? 0.4335 0.5642 0.4179 -0.0424 -0.0744 -0.1229 531 PRO B CB  
8107 C CG  . PRO B 545 ? 0.4662 0.5965 0.4599 -0.0571 -0.0677 -0.1419 531 PRO B CG  
8108 C CD  . PRO B 545 ? 0.5144 0.6130 0.5209 -0.0627 -0.0550 -0.1368 531 PRO B CD  
8109 N N   . LYS B 546 ? 0.5954 0.6931 0.5844 -0.0152 -0.0777 -0.0888 532 LYS B N   
8110 C CA  . LYS B 546 ? 0.5016 0.5706 0.4762 -0.0015 -0.0794 -0.0712 532 LYS B CA  
8111 C C   . LYS B 546 ? 0.4769 0.5232 0.4200 -0.0004 -0.0796 -0.0567 532 LYS B C   
8112 O O   . LYS B 546 ? 0.6023 0.6133 0.5352 0.0003  -0.0759 -0.0438 532 LYS B O   
8113 C CB  . LYS B 546 ? 0.5716 0.6598 0.5489 0.0176  -0.0908 -0.0683 532 LYS B CB  
8114 C CG  . LYS B 546 ? 0.6979 0.7584 0.6734 0.0318  -0.0911 -0.0580 532 LYS B CG  
8115 C CD  . LYS B 546 ? 0.5901 0.6779 0.5735 0.0525  -0.1013 -0.0591 532 LYS B CD  
8116 C CE  . LYS B 546 ? 0.6322 0.7592 0.6499 0.0455  -0.0975 -0.0734 532 LYS B CE  
8117 N NZ  . LYS B 546 ? 0.6755 0.8278 0.7033 0.0674  -0.1045 -0.0732 532 LYS B NZ  
8118 N N   . ALA B 547 ? 0.5153 0.5831 0.4423 -0.0008 -0.0843 -0.0585 533 ALA B N   
8119 C CA  . ALA B 547 ? 0.5406 0.5936 0.4356 0.0008  -0.0844 -0.0422 533 ALA B CA  
8120 C C   . ALA B 547 ? 0.6376 0.6916 0.5270 -0.0154 -0.0734 -0.0470 533 ALA B C   
8121 O O   . ALA B 547 ? 0.6240 0.6727 0.4873 -0.0162 -0.0716 -0.0334 533 ALA B O   
8122 C CB  . ALA B 547 ? 0.5419 0.6215 0.4169 0.0148  -0.0973 -0.0379 533 ALA B CB  
8123 N N   . ASP B 548 ? 0.5709 0.6319 0.4834 -0.0272 -0.0656 -0.0650 534 ASP B N   
8124 C CA  . ASP B 548 ? 0.6120 0.6779 0.5194 -0.0388 -0.0559 -0.0728 534 ASP B CA  
8125 C C   . ASP B 548 ? 0.5587 0.5967 0.4592 -0.0450 -0.0456 -0.0576 534 ASP B C   
8126 O O   . ASP B 548 ? 0.4787 0.4929 0.3934 -0.0465 -0.0425 -0.0530 534 ASP B O   
8127 C CB  . ASP B 548 ? 0.6088 0.6846 0.5425 -0.0478 -0.0515 -0.0960 534 ASP B CB  
8128 C CG  . ASP B 548 ? 0.6421 0.7303 0.5677 -0.0547 -0.0451 -0.1096 534 ASP B CG  
8129 O OD1 . ASP B 548 ? 0.6093 0.7039 0.5094 -0.0528 -0.0430 -0.1003 534 ASP B OD1 
8130 O OD2 . ASP B 548 ? 0.7550 0.8462 0.6993 -0.0614 -0.0420 -0.1292 534 ASP B OD2 
8131 N N   . ILE B 549 ? 0.6421 0.6872 0.5215 -0.0492 -0.0402 -0.0509 535 ILE B N   
8132 C CA  . ILE B 549 ? 0.6333 0.6571 0.5028 -0.0562 -0.0321 -0.0319 535 ILE B CA  
8133 C C   . ILE B 549 ? 0.5466 0.5859 0.4169 -0.0660 -0.0193 -0.0397 535 ILE B C   
8134 O O   . ILE B 549 ? 0.7128 0.7802 0.5745 -0.0643 -0.0183 -0.0528 535 ILE B O   
8135 C CB  . ILE B 549 ? 0.6650 0.6815 0.5043 -0.0510 -0.0378 -0.0080 535 ILE B CB  
8136 C CG1 . ILE B 549 ? 0.7361 0.7134 0.5731 -0.0555 -0.0366 0.0128  535 ILE B CG1 
8137 C CG2 . ILE B 549 ? 0.8072 0.8492 0.6218 -0.0547 -0.0320 -0.0025 535 ILE B CG2 
8138 C CD1 . ILE B 549 ? 0.7160 0.6756 0.5249 -0.0478 -0.0448 0.0370  535 ILE B CD1 
8139 N N   . PRO B 550 ? 0.5617 0.5866 0.4432 -0.0748 -0.0101 -0.0346 536 PRO B N   
8140 C CA  . PRO B 550 ? 0.5757 0.6198 0.4562 -0.0821 0.0023  -0.0390 536 PRO B CA  
8141 C C   . PRO B 550 ? 0.7061 0.7613 0.5599 -0.0869 0.0065  -0.0186 536 PRO B C   
8142 O O   . PRO B 550 ? 0.5797 0.6154 0.4189 -0.0876 0.0008  0.0029  536 PRO B O   
8143 C CB  . PRO B 550 ? 0.5998 0.6264 0.5029 -0.0890 0.0087  -0.0382 536 PRO B CB  
8144 C CG  . PRO B 550 ? 0.5853 0.5849 0.5014 -0.0844 -0.0003 -0.0378 536 PRO B CG  
8145 C CD  . PRO B 550 ? 0.6531 0.6476 0.5507 -0.0771 -0.0110 -0.0279 536 PRO B CD  
8146 N N   . PRO B 551 ? 0.6629 0.7490 0.5087 -0.0896 0.0167  -0.0239 537 PRO B N   
8147 C CA  . PRO B 551 ? 0.6131 0.7162 0.4311 -0.0944 0.0219  -0.0028 537 PRO B CA  
8148 C C   . PRO B 551 ? 0.7093 0.7900 0.5262 -0.1083 0.0259  0.0249  537 PRO B C   
8149 O O   . PRO B 551 ? 0.6769 0.7514 0.4696 -0.1115 0.0241  0.0492  537 PRO B O   
8150 C CB  . PRO B 551 ? 0.5871 0.7306 0.4031 -0.0937 0.0340  -0.0182 537 PRO B CB  
8151 C CG  . PRO B 551 ? 0.7405 0.8784 0.5864 -0.0910 0.0362  -0.0427 537 PRO B CG  
8152 C CD  . PRO B 551 ? 0.5889 0.6967 0.4479 -0.0861 0.0234  -0.0498 537 PRO B CD  
8153 N N   . LEU B 552 ? 0.6584 0.7260 0.5002 -0.1172 0.0307  0.0225  538 LEU B N   
8154 C CA  . LEU B 552 ? 0.6454 0.6929 0.4879 -0.1333 0.0338  0.0464  538 LEU B CA  
8155 C C   . LEU B 552 ? 0.8192 0.8212 0.6522 -0.1317 0.0209  0.0623  538 LEU B C   
8156 O O   . LEU B 552 ? 0.8995 0.8835 0.7162 -0.1421 0.0208  0.0879  538 LEU B O   
8157 C CB  . LEU B 552 ? 0.6804 0.7270 0.5526 -0.1416 0.0396  0.0371  538 LEU B CB  
8158 C CG  . LEU B 552 ? 0.6631 0.6813 0.5414 -0.1588 0.0384  0.0565  538 LEU B CG  
8159 C CD1 . LEU B 552 ? 0.5889 0.6310 0.4575 -0.1769 0.0498  0.0772  538 LEU B CD1 
8160 C CD2 . LEU B 552 ? 0.6787 0.6896 0.5866 -0.1610 0.0382  0.0424  538 LEU B CD2 
8161 N N   . LEU B 553 ? 0.8476 0.8302 0.6904 -0.1184 0.0101  0.0481  539 LEU B N   
8162 C CA  . LEU B 553 ? 0.8939 0.8349 0.7287 -0.1131 -0.0022 0.0608  539 LEU B CA  
8163 C C   . LEU B 553 ? 0.9385 0.8795 0.7426 -0.1039 -0.0089 0.0764  539 LEU B C   
8164 O O   . LEU B 553 ? 0.9497 0.8553 0.7384 -0.1034 -0.0161 0.0972  539 LEU B O   
8165 C CB  . LEU B 553 ? 0.6943 0.6218 0.5494 -0.1007 -0.0105 0.0415  539 LEU B CB  
8166 C CG  . LEU B 553 ? 0.8660 0.7603 0.7132 -0.0876 -0.0243 0.0481  539 LEU B CG  
8167 C CD1 . LEU B 553 ? 0.8793 0.7308 0.7293 -0.0951 -0.0274 0.0598  539 LEU B CD1 
8168 C CD2 . LEU B 553 ? 0.7468 0.6501 0.6126 -0.0738 -0.0298 0.0264  539 LEU B CD2 
8169 N N   . GLY B 554 ? 0.8077 0.7867 0.6012 -0.0958 -0.0074 0.0666  540 GLY B N   
8170 C CA  . GLY B 554 ? 0.8199 0.8064 0.5812 -0.0875 -0.0128 0.0830  540 GLY B CA  
8171 C C   . GLY B 554 ? 0.9779 0.9581 0.7169 -0.1015 -0.0049 0.1135  540 GLY B C   
8172 O O   . GLY B 554 ? 0.9075 0.8637 0.6217 -0.0976 -0.0117 0.1381  540 GLY B O   
8173 N N   . ALA B 555 ? 0.9688 0.9717 0.7167 -0.1179 0.0098  0.1133  541 ALA B N   
8174 C CA  . ALA B 555 ? 0.9421 0.9422 0.6739 -0.1359 0.0192  0.1433  541 ALA B CA  
8175 C C   . ALA B 555 ? 1.0444 0.9885 0.7818 -0.1479 0.0138  0.1623  541 ALA B C   
8176 O O   . ALA B 555 ? 1.0003 0.9204 0.7155 -0.1571 0.0138  0.1930  541 ALA B O   
8177 C CB  . ALA B 555 ? 0.9422 0.9855 0.6874 -0.1499 0.0362  0.1359  541 ALA B CB  
8178 N N   . ILE B 556 ? 0.9896 0.9109 0.7553 -0.1481 0.0092  0.1446  542 ILE B N   
8179 C CA  . ILE B 556 ? 1.0199 0.8866 0.7907 -0.1577 0.0023  0.1576  542 ILE B CA  
8180 C C   . ILE B 556 ? 1.1125 0.9369 0.8592 -0.1417 -0.0123 0.1723  542 ILE B C   
8181 O O   . ILE B 556 ? 1.1051 0.8872 0.8354 -0.1508 -0.0156 0.1983  542 ILE B O   
8182 C CB  . ILE B 556 ? 1.0366 0.8934 0.8403 -0.1571 -0.0005 0.1328  542 ILE B CB  
8183 C CG1 . ILE B 556 ? 0.8284 0.7124 0.6543 -0.1778 0.0125  0.1280  542 ILE B CG1 
8184 C CG2 . ILE B 556 ? 0.9878 0.7851 0.7915 -0.1551 -0.0134 0.1387  542 ILE B CG2 
8185 C CD1 . ILE B 556 ? 0.7595 0.6313 0.6149 -0.1788 0.0093  0.1082  542 ILE B CD1 
8186 N N   . THR B 557 ? 1.1012 0.9371 0.8451 -0.1174 -0.0213 0.1564  543 THR B N   
8187 C CA  . THR B 557 ? 1.1020 0.9042 0.8243 -0.0980 -0.0359 0.1686  543 THR B CA  
8188 C C   . THR B 557 ? 1.0994 0.9009 0.7853 -0.0988 -0.0349 0.1996  543 THR B C   
8189 O O   . THR B 557 ? 1.1673 0.9230 0.8318 -0.0917 -0.0445 0.2221  543 THR B O   
8190 C CB  . THR B 557 ? 0.9702 0.7970 0.7000 -0.0735 -0.0450 0.1445  543 THR B CB  
8191 O OG1 . THR B 557 ? 1.0000 0.8823 0.7270 -0.0721 -0.0383 0.1328  543 THR B OG1 
8192 C CG2 . THR B 557 ? 0.8397 0.6596 0.6025 -0.0714 -0.0468 0.1189  543 THR B CG2 
8193 N N   . LYS B 558 ? 1.0784 0.9297 0.7549 -0.1058 -0.0234 0.2017  544 LYS B N   
8194 C CA  . LYS B 558 ? 1.1433 1.0004 0.7833 -0.1075 -0.0204 0.2329  544 LYS B CA  
8195 C C   . LYS B 558 ? 1.2539 1.0736 0.8861 -0.1329 -0.0131 0.2649  544 LYS B C   
8196 O O   . LYS B 558 ? 1.2986 1.0937 0.8990 -0.1326 -0.0156 0.2978  544 LYS B O   
8197 C CB  . LYS B 558 ? 1.0559 0.9807 0.6881 -0.1078 -0.0092 0.2238  544 LYS B CB  
8198 C CG  . LYS B 558 ? 1.1935 1.1535 0.8215 -0.0828 -0.0188 0.1996  544 LYS B CG  
8199 C CD  . LYS B 558 ? 1.2794 1.2140 0.8821 -0.0609 -0.0353 0.2153  544 LYS B CD  
8200 C CE  . LYS B 558 ? 1.2334 1.2184 0.8114 -0.0430 -0.0399 0.2100  544 LYS B CE  
8201 N NZ  . LYS B 558 ? 1.2643 1.2319 0.8021 -0.0297 -0.0485 0.2441  544 LYS B NZ  
8202 N N   . ALA B 559 ? 1.2302 1.0447 0.8912 -0.1554 -0.0048 0.2567  545 ALA B N   
8203 C CA  . ALA B 559 ? 1.2277 1.0081 0.8859 -0.1836 0.0015  0.2852  545 ALA B CA  
8204 C C   . ALA B 559 ? 1.4346 1.1364 1.0852 -0.1800 -0.0136 0.2988  545 ALA B C   
8205 O O   . ALA B 559 ? 1.3972 1.0581 1.0288 -0.1958 -0.0130 0.3319  545 ALA B O   
8206 C CB  . ALA B 559 ? 1.0226 0.8264 0.7161 -0.2076 0.0133  0.2697  545 ALA B CB  
8207 N N   . LEU B 560 ? 1.4101 1.0893 1.0747 -0.1591 -0.0269 0.2740  546 LEU B N   
8208 C CA  . LEU B 560 ? 1.3333 0.9393 0.9905 -0.1502 -0.0423 0.2817  546 LEU B CA  
8209 C C   . LEU B 560 ? 1.4478 1.0223 1.0666 -0.1299 -0.0526 0.3085  546 LEU B C   
8210 O O   . LEU B 560 ? 1.6625 1.1699 1.2705 -0.1226 -0.0650 0.3196  546 LEU B O   
8211 C CB  . LEU B 560 ? 1.2649 0.8642 0.9462 -0.1298 -0.0529 0.2473  546 LEU B CB  
8212 C CG  . LEU B 560 ? 1.4273 1.0256 1.1440 -0.1451 -0.0497 0.2232  546 LEU B CG  
8213 C CD1 . LEU B 560 ? 1.4490 1.0979 1.1849 -0.1714 -0.0327 0.2191  546 LEU B CD1 
8214 C CD2 . LEU B 560 ? 1.1856 0.7952 0.9210 -0.1202 -0.0578 0.1911  546 LEU B CD2 
8215 N N   . GLU B 561 ? 1.4590 1.0778 1.0554 -0.1185 -0.0490 0.3185  547 GLU B N   
8216 C CA  . GLU B 561 ? 1.5775 1.1647 1.1349 -0.0993 -0.0592 0.3479  547 GLU B CA  
8217 C C   . GLU B 561 ? 1.6370 1.1874 1.1683 -0.1228 -0.0523 0.3912  547 GLU B C   
8218 O O   . GLU B 561 ? 1.5416 1.1342 1.0612 -0.1397 -0.0378 0.4086  547 GLU B O   
8219 C CB  . GLU B 561 ? 1.5512 1.1956 1.0923 -0.0727 -0.0625 0.3405  547 GLU B CB  
8220 C CG  . GLU B 561 ? 1.5645 1.2070 1.1209 -0.0426 -0.0778 0.3111  547 GLU B CG  
8221 C CD  . GLU B 561 ? 1.7371 1.3081 1.2770 -0.0220 -0.0946 0.3264  547 GLU B CD  
8222 O OE1 . GLU B 561 ? 1.7681 1.3474 1.3027 0.0104  -0.1083 0.3163  547 GLU B OE1 
8223 O OE2 . GLU B 561 ? 1.7856 1.2914 1.3168 -0.0370 -0.0950 0.3489  547 GLU B OE2 
8224 N N   . ALA B 562 ? 1.6613 1.1308 1.1848 -0.1243 -0.0629 0.4073  548 ALA B N   
8225 C CA  . ALA B 562 ? 1.6002 1.0228 1.1097 -0.1429 -0.0571 0.4428  548 ALA B CA  
8226 C C   . ALA B 562 ? 1.5801 1.0253 1.1184 -0.1837 -0.0383 0.4419  548 ALA B C   
8227 O O   . ALA B 562 ? 1.4028 0.8879 0.9643 -0.1988 -0.0330 0.4192  548 ALA B O   
8228 C CB  . ALA B 562 ? 1.4938 0.9340 0.9652 -0.1279 -0.0539 0.4748  548 ALA B CB  
# 
