data_9G4N
# 
_entry.id   9G4N 
# 
_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   9G4N         pdb_00009g4n 10.2210/pdb9g4n/pdb 
WWPDB D_1292139632 ?            ?                   
# 
_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                        9G4N 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-15 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              pedrobule@fmv.ulisboa.pt 
_pdbx_contact_author.name_first         Pedro 
_pdbx_contact_author.name_last          Bule 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2531-9926 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Caseiro, C.'    1 0009-0009-7984-1198 
'Alves, V.D.'    2 0000-0002-8430-4380 
'Carvalho, A.L.' 3 0000-0002-3824-0240 
'Bule, P.'       4 0000-0003-2531-9926 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Int.J.Biol.Macromol. 
_citation.journal_id_ASTM           IJBMDR 
_citation.journal_id_CSD            0708 
_citation.journal_id_ISSN           0141-8130 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            282 
_citation.language                  ? 
_citation.page_first                137402 
_citation.page_last                 137402 
_citation.title                     
'Family GH157 enzyme exhibits broad linkage tolerance and a dual endo/exo-beta-glucanase activity on beta-glucans.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ijbiomac.2024.137402 
_citation.pdbx_database_id_PubMed   39528173 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Caseiro, C.'      1 ? 
primary 'McGregor, N.G.S.' 2 ? 
primary 'Alves, V.D.'      3 ? 
primary 'Carvalho, A.L.'   4 ? 
primary 'Romao, M.J.'      5 ? 
primary 'Davies, G.J.'     6 ? 
primary 'Fontes, C.M.G.A.' 7 ? 
primary 'Bule, P.'         8 ? 
# 
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 'Glycoside hydrolase family 2 catalytic domain-containing protein'           61456.016 4   ? ? ? ? 
2 branched    man 'beta-D-glucopyranose-(1-3)-beta-D-glucopyranose-(1-3)-beta-D-glucopyranose' 504.438   4   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                                               62.068    5   ? ? ? ? 
4 non-polymer syn beta-D-glucopyranose                                                         180.156   3   ? ? ? ? 
5 non-polymer syn GLYCEROL                                                                     92.094    10  ? ? ? ? 
6 non-polymer nat 'TRIETHYLENE GLYCOL'                                                         150.173   1   ? ? ? ? 
7 water       nat water                                                                        18.015    969 ? ? ? ? 
# 
_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       
;MQSKTKIELKDNWYHLDGEKYFIKAIGYEIGARPGQAPYEDERKDELELMKFDLENIKEGGYNTIRTWSQYSENQLKLVQ
ESGLKLIMGIDIKPEEDYGDPEFVKDSEIELKRVLNYAKKYDCIITYLVINEPQTDHIHSVTGKAFVDLMNTLINIIHKG
HPGIPVTLSANAMISDYMDESIFDVYAYNCYDHNEGQTATMGFKDYIKGLNELNGLDKPFITTAFGYSVSPEGGNGQYGS
NTLKQQSDGLISNYRDLIDAGAVGMCPFYYADGWWKGGEKSDHSLNQPEEWFGFWGYSDLNDKYGTPRPVWFAMRDYMKG
LIISPKNKSIHTNTKIPLELYNDKDVKKVVVKFRDKVIYSKNITSEGYMADELTIDPVGIEDMELAFEFYDSDNKIIKNE
SINILASKTAFELPELTIEVTPEKDLNEGKIASIKTKIETSENFTLLDDLKISYNTHLGWAIGSQASVSISDQLDKKIIT
SENFFNIPDNCWVVNASAGISVRYGKFTFKIHDQKIIYRGDWAKEVGRKLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQSKTKIELKDNWYHLDGEKYFIKAIGYEIGARPGQAPYEDERKDELELMKFDLENIKEGGYNTIRTWSQYSENQLKLVQ
ESGLKLIMGIDIKPEEDYGDPEFVKDSEIELKRVLNYAKKYDCIITYLVINEPQTDHIHSVTGKAFVDLMNTLINIIHKG
HPGIPVTLSANAMISDYMDESIFDVYAYNCYDHNEGQTATMGFKDYIKGLNELNGLDKPFITTAFGYSVSPEGGNGQYGS
NTLKQQSDGLISNYRDLIDAGAVGMCPFYYADGWWKGGEKSDHSLNQPEEWFGFWGYSDLNDKYGTPRPVWFAMRDYMKG
LIISPKNKSIHTNTKIPLELYNDKDVKKVVVKFRDKVIYSKNITSEGYMADELTIDPVGIEDMELAFEFYDSDNKIIKNE
SINILASKTAFELPELTIEVTPEKDLNEGKIASIKTKIETSENFTLLDDLKISYNTHLGWAIGSQASVSISDQLDKKIIT
SENFFNIPDNCWVVNASAGISVRYGKFTFKIHDQKIIYRGDWAKEVGRKLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 1,2-ETHANEDIOL       EDO 
4 beta-D-glucopyranose BGC 
5 GLYCEROL             GOL 
6 'TRIETHYLENE GLYCOL' PGE 
7 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   GLN n 
1 3   SER n 
1 4   LYS n 
1 5   THR n 
1 6   LYS n 
1 7   ILE n 
1 8   GLU n 
1 9   LEU n 
1 10  LYS n 
1 11  ASP n 
1 12  ASN n 
1 13  TRP n 
1 14  TYR n 
1 15  HIS n 
1 16  LEU n 
1 17  ASP n 
1 18  GLY n 
1 19  GLU n 
1 20  LYS n 
1 21  TYR n 
1 22  PHE n 
1 23  ILE n 
1 24  LYS n 
1 25  ALA n 
1 26  ILE n 
1 27  GLY n 
1 28  TYR n 
1 29  GLU n 
1 30  ILE n 
1 31  GLY n 
1 32  ALA n 
1 33  ARG n 
1 34  PRO n 
1 35  GLY n 
1 36  GLN n 
1 37  ALA n 
1 38  PRO n 
1 39  TYR n 
1 40  GLU n 
1 41  ASP n 
1 42  GLU n 
1 43  ARG n 
1 44  LYS n 
1 45  ASP n 
1 46  GLU n 
1 47  LEU n 
1 48  GLU n 
1 49  LEU n 
1 50  MET n 
1 51  LYS n 
1 52  PHE n 
1 53  ASP n 
1 54  LEU n 
1 55  GLU n 
1 56  ASN n 
1 57  ILE n 
1 58  LYS n 
1 59  GLU n 
1 60  GLY n 
1 61  GLY n 
1 62  TYR n 
1 63  ASN n 
1 64  THR n 
1 65  ILE n 
1 66  ARG n 
1 67  THR n 
1 68  TRP n 
1 69  SER n 
1 70  GLN n 
1 71  TYR n 
1 72  SER n 
1 73  GLU n 
1 74  ASN n 
1 75  GLN n 
1 76  LEU n 
1 77  LYS n 
1 78  LEU n 
1 79  VAL n 
1 80  GLN n 
1 81  GLU n 
1 82  SER n 
1 83  GLY n 
1 84  LEU n 
1 85  LYS n 
1 86  LEU n 
1 87  ILE n 
1 88  MET n 
1 89  GLY n 
1 90  ILE n 
1 91  ASP n 
1 92  ILE n 
1 93  LYS n 
1 94  PRO n 
1 95  GLU n 
1 96  GLU n 
1 97  ASP n 
1 98  TYR n 
1 99  GLY n 
1 100 ASP n 
1 101 PRO n 
1 102 GLU n 
1 103 PHE n 
1 104 VAL n 
1 105 LYS n 
1 106 ASP n 
1 107 SER n 
1 108 GLU n 
1 109 ILE n 
1 110 GLU n 
1 111 LEU n 
1 112 LYS n 
1 113 ARG n 
1 114 VAL n 
1 115 LEU n 
1 116 ASN n 
1 117 TYR n 
1 118 ALA n 
1 119 LYS n 
1 120 LYS n 
1 121 TYR n 
1 122 ASP n 
1 123 CYS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 TYR n 
1 128 LEU n 
1 129 VAL n 
1 130 ILE n 
1 131 ASN n 
1 132 GLU n 
1 133 PRO n 
1 134 GLN n 
1 135 THR n 
1 136 ASP n 
1 137 HIS n 
1 138 ILE n 
1 139 HIS n 
1 140 SER n 
1 141 VAL n 
1 142 THR n 
1 143 GLY n 
1 144 LYS n 
1 145 ALA n 
1 146 PHE n 
1 147 VAL n 
1 148 ASP n 
1 149 LEU n 
1 150 MET n 
1 151 ASN n 
1 152 THR n 
1 153 LEU n 
1 154 ILE n 
1 155 ASN n 
1 156 ILE n 
1 157 ILE n 
1 158 HIS n 
1 159 LYS n 
1 160 GLY n 
1 161 HIS n 
1 162 PRO n 
1 163 GLY n 
1 164 ILE n 
1 165 PRO n 
1 166 VAL n 
1 167 THR n 
1 168 LEU n 
1 169 SER n 
1 170 ALA n 
1 171 ASN n 
1 172 ALA n 
1 173 MET n 
1 174 ILE n 
1 175 SER n 
1 176 ASP n 
1 177 TYR n 
1 178 MET n 
1 179 ASP n 
1 180 GLU n 
1 181 SER n 
1 182 ILE n 
1 183 PHE n 
1 184 ASP n 
1 185 VAL n 
1 186 TYR n 
1 187 ALA n 
1 188 TYR n 
1 189 ASN n 
1 190 CYS n 
1 191 TYR n 
1 192 ASP n 
1 193 HIS n 
1 194 ASN n 
1 195 GLU n 
1 196 GLY n 
1 197 GLN n 
1 198 THR n 
1 199 ALA n 
1 200 THR n 
1 201 MET n 
1 202 GLY n 
1 203 PHE n 
1 204 LYS n 
1 205 ASP n 
1 206 TYR n 
1 207 ILE n 
1 208 LYS n 
1 209 GLY n 
1 210 LEU n 
1 211 ASN n 
1 212 GLU n 
1 213 LEU n 
1 214 ASN n 
1 215 GLY n 
1 216 LEU n 
1 217 ASP n 
1 218 LYS n 
1 219 PRO n 
1 220 PHE n 
1 221 ILE n 
1 222 THR n 
1 223 THR n 
1 224 ALA n 
1 225 PHE n 
1 226 GLY n 
1 227 TYR n 
1 228 SER n 
1 229 VAL n 
1 230 SER n 
1 231 PRO n 
1 232 GLU n 
1 233 GLY n 
1 234 GLY n 
1 235 ASN n 
1 236 GLY n 
1 237 GLN n 
1 238 TYR n 
1 239 GLY n 
1 240 SER n 
1 241 ASN n 
1 242 THR n 
1 243 LEU n 
1 244 LYS n 
1 245 GLN n 
1 246 GLN n 
1 247 SER n 
1 248 ASP n 
1 249 GLY n 
1 250 LEU n 
1 251 ILE n 
1 252 SER n 
1 253 ASN n 
1 254 TYR n 
1 255 ARG n 
1 256 ASP n 
1 257 LEU n 
1 258 ILE n 
1 259 ASP n 
1 260 ALA n 
1 261 GLY n 
1 262 ALA n 
1 263 VAL n 
1 264 GLY n 
1 265 MET n 
1 266 CYS n 
1 267 PRO n 
1 268 PHE n 
1 269 TYR n 
1 270 TYR n 
1 271 ALA n 
1 272 ASP n 
1 273 GLY n 
1 274 TRP n 
1 275 TRP n 
1 276 LYS n 
1 277 GLY n 
1 278 GLY n 
1 279 GLU n 
1 280 LYS n 
1 281 SER n 
1 282 ASP n 
1 283 HIS n 
1 284 SER n 
1 285 LEU n 
1 286 ASN n 
1 287 GLN n 
1 288 PRO n 
1 289 GLU n 
1 290 GLU n 
1 291 TRP n 
1 292 PHE n 
1 293 GLY n 
1 294 PHE n 
1 295 TRP n 
1 296 GLY n 
1 297 TYR n 
1 298 SER n 
1 299 ASP n 
1 300 LEU n 
1 301 ASN n 
1 302 ASP n 
1 303 LYS n 
1 304 TYR n 
1 305 GLY n 
1 306 THR n 
1 307 PRO n 
1 308 ARG n 
1 309 PRO n 
1 310 VAL n 
1 311 TRP n 
1 312 PHE n 
1 313 ALA n 
1 314 MET n 
1 315 ARG n 
1 316 ASP n 
1 317 TYR n 
1 318 MET n 
1 319 LYS n 
1 320 GLY n 
1 321 LEU n 
1 322 ILE n 
1 323 ILE n 
1 324 SER n 
1 325 PRO n 
1 326 LYS n 
1 327 ASN n 
1 328 LYS n 
1 329 SER n 
1 330 ILE n 
1 331 HIS n 
1 332 THR n 
1 333 ASN n 
1 334 THR n 
1 335 LYS n 
1 336 ILE n 
1 337 PRO n 
1 338 LEU n 
1 339 GLU n 
1 340 LEU n 
1 341 TYR n 
1 342 ASN n 
1 343 ASP n 
1 344 LYS n 
1 345 ASP n 
1 346 VAL n 
1 347 LYS n 
1 348 LYS n 
1 349 VAL n 
1 350 VAL n 
1 351 VAL n 
1 352 LYS n 
1 353 PHE n 
1 354 ARG n 
1 355 ASP n 
1 356 LYS n 
1 357 VAL n 
1 358 ILE n 
1 359 TYR n 
1 360 SER n 
1 361 LYS n 
1 362 ASN n 
1 363 ILE n 
1 364 THR n 
1 365 SER n 
1 366 GLU n 
1 367 GLY n 
1 368 TYR n 
1 369 MET n 
1 370 ALA n 
1 371 ASP n 
1 372 GLU n 
1 373 LEU n 
1 374 THR n 
1 375 ILE n 
1 376 ASP n 
1 377 PRO n 
1 378 VAL n 
1 379 GLY n 
1 380 ILE n 
1 381 GLU n 
1 382 ASP n 
1 383 MET n 
1 384 GLU n 
1 385 LEU n 
1 386 ALA n 
1 387 PHE n 
1 388 GLU n 
1 389 PHE n 
1 390 TYR n 
1 391 ASP n 
1 392 SER n 
1 393 ASP n 
1 394 ASN n 
1 395 LYS n 
1 396 ILE n 
1 397 ILE n 
1 398 LYS n 
1 399 ASN n 
1 400 GLU n 
1 401 SER n 
1 402 ILE n 
1 403 ASN n 
1 404 ILE n 
1 405 LEU n 
1 406 ALA n 
1 407 SER n 
1 408 LYS n 
1 409 THR n 
1 410 ALA n 
1 411 PHE n 
1 412 GLU n 
1 413 LEU n 
1 414 PRO n 
1 415 GLU n 
1 416 LEU n 
1 417 THR n 
1 418 ILE n 
1 419 GLU n 
1 420 VAL n 
1 421 THR n 
1 422 PRO n 
1 423 GLU n 
1 424 LYS n 
1 425 ASP n 
1 426 LEU n 
1 427 ASN n 
1 428 GLU n 
1 429 GLY n 
1 430 LYS n 
1 431 ILE n 
1 432 ALA n 
1 433 SER n 
1 434 ILE n 
1 435 LYS n 
1 436 THR n 
1 437 LYS n 
1 438 ILE n 
1 439 GLU n 
1 440 THR n 
1 441 SER n 
1 442 GLU n 
1 443 ASN n 
1 444 PHE n 
1 445 THR n 
1 446 LEU n 
1 447 LEU n 
1 448 ASP n 
1 449 ASP n 
1 450 LEU n 
1 451 LYS n 
1 452 ILE n 
1 453 SER n 
1 454 TYR n 
1 455 ASN n 
1 456 THR n 
1 457 HIS n 
1 458 LEU n 
1 459 GLY n 
1 460 TRP n 
1 461 ALA n 
1 462 ILE n 
1 463 GLY n 
1 464 SER n 
1 465 GLN n 
1 466 ALA n 
1 467 SER n 
1 468 VAL n 
1 469 SER n 
1 470 ILE n 
1 471 SER n 
1 472 ASP n 
1 473 GLN n 
1 474 LEU n 
1 475 ASP n 
1 476 LYS n 
1 477 LYS n 
1 478 ILE n 
1 479 ILE n 
1 480 THR n 
1 481 SER n 
1 482 GLU n 
1 483 ASN n 
1 484 PHE n 
1 485 PHE n 
1 486 ASN n 
1 487 ILE n 
1 488 PRO n 
1 489 ASP n 
1 490 ASN n 
1 491 CYS n 
1 492 TRP n 
1 493 VAL n 
1 494 VAL n 
1 495 ASN n 
1 496 ALA n 
1 497 SER n 
1 498 ALA n 
1 499 GLY n 
1 500 ILE n 
1 501 SER n 
1 502 VAL n 
1 503 ARG n 
1 504 TYR n 
1 505 GLY n 
1 506 LYS n 
1 507 PHE n 
1 508 THR n 
1 509 PHE n 
1 510 LYS n 
1 511 ILE n 
1 512 HIS n 
1 513 ASP n 
1 514 GLN n 
1 515 LYS n 
1 516 ILE n 
1 517 ILE n 
1 518 TYR n 
1 519 ARG n 
1 520 GLY n 
1 521 ASP n 
1 522 TRP n 
1 523 ALA n 
1 524 LYS n 
1 525 GLU n 
1 526 VAL n 
1 527 GLY n 
1 528 ARG n 
1 529 LYS n 
1 530 LEU n 
1 531 GLU n 
1 532 HIS n 
1 533 HIS n 
1 534 HIS n 
1 535 HIS n 
1 536 HIS n 
1 537 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   537 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ALGA_4297 
_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      'Labilibaculum antarcticum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1717717 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_branch.entity_id   2 
_pdbx_entity_branch.type        oligosaccharide 
# 
loop_
_pdbx_entity_branch_descriptor.ordinal 
_pdbx_entity_branch_descriptor.entity_id 
_pdbx_entity_branch_descriptor.descriptor 
_pdbx_entity_branch_descriptor.type 
_pdbx_entity_branch_descriptor.program 
_pdbx_entity_branch_descriptor.program_version 
1 2 DGlcpb1-3DGlcpb1-3DGlcpb1-ROH                          'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,3,2/[a2122h-1b_1-5]/1-1-1/a3-b1_b3-c1'    WURCS                       PDB2Glycan 1.1.0 
3 2 '[][b-D-Glcp]{[(3+1)][b-D-Glcp]{[(3+1)][b-D-Glcp]{}}}' LINUCS                      PDB-CARE   ?     
# 
loop_
_pdbx_entity_branch_link.link_id 
_pdbx_entity_branch_link.entity_id 
_pdbx_entity_branch_link.entity_branch_list_num_1 
_pdbx_entity_branch_link.comp_id_1 
_pdbx_entity_branch_link.atom_id_1 
_pdbx_entity_branch_link.leaving_atom_id_1 
_pdbx_entity_branch_link.entity_branch_list_num_2 
_pdbx_entity_branch_link.comp_id_2 
_pdbx_entity_branch_link.atom_id_2 
_pdbx_entity_branch_link.leaving_atom_id_2 
_pdbx_entity_branch_link.value_order 
_pdbx_entity_branch_link.details 
1 2 2 BGC C1 O1 1 BGC O3 HO3 sing ? 
2 2 3 BGC C1 O1 2 BGC O3 HO3 sing ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking'          y ALANINE              ?                                    'C3 H7 N O2'     89.093  
ARG 'L-peptide linking'          y ARGININE             ?                                    'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking'          y ASPARAGINE           ?                                    'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking'          y 'ASPARTIC ACID'      ?                                    'C4 H7 N O4'     133.103 
BGC 'D-saccharide, beta linking' . beta-D-glucopyranose 'beta-D-glucose; D-glucose; glucose' 'C6 H12 O6'      180.156 
CYS 'L-peptide linking'          y CYSTEINE             ?                                    'C3 H7 N O2 S'   121.158 
EDO non-polymer                  . 1,2-ETHANEDIOL       'ETHYLENE GLYCOL'                    'C2 H6 O2'       62.068  
GLN 'L-peptide linking'          y GLUTAMINE            ?                                    'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'      ?                                    'C5 H9 N O4'     147.129 
GLY 'peptide linking'            y GLYCINE              ?                                    'C2 H5 N O2'     75.067  
GOL non-polymer                  . GLYCEROL             'GLYCERIN; PROPANE-1,2,3-TRIOL'      'C3 H8 O3'       92.094  
HIS 'L-peptide linking'          y HISTIDINE            ?                                    'C6 H10 N3 O2 1' 156.162 
HOH non-polymer                  . WATER                ?                                    'H2 O'           18.015  
ILE 'L-peptide linking'          y ISOLEUCINE           ?                                    'C6 H13 N O2'    131.173 
LEU 'L-peptide linking'          y LEUCINE              ?                                    'C6 H13 N O2'    131.173 
LYS 'L-peptide linking'          y LYSINE               ?                                    'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking'          y METHIONINE           ?                                    'C5 H11 N O2 S'  149.211 
PGE non-polymer                  . 'TRIETHYLENE GLYCOL' ?                                    'C6 H14 O4'      150.173 
PHE 'L-peptide linking'          y PHENYLALANINE        ?                                    'C9 H11 N O2'    165.189 
PRO 'L-peptide linking'          y PROLINE              ?                                    'C5 H9 N O2'     115.130 
SER 'L-peptide linking'          y SERINE               ?                                    'C3 H7 N O3'     105.093 
THR 'L-peptide linking'          y THREONINE            ?                                    'C4 H9 N O3'     119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN           ?                                    'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking'          y TYROSINE             ?                                    'C9 H11 N O3'    181.189 
VAL 'L-peptide linking'          y VALINE               ?                                    'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
BGC 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpb            
BGC 'COMMON NAME'                         GMML     1.0 b-D-glucopyranose 
BGC 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-Glcp          
BGC 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 Glc               
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   GLN 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   LYS 4   4   4   LYS LYS A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   LYS 6   6   6   LYS LYS A . n 
A 1 7   ILE 7   7   7   ILE ILE A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  TRP 13  13  13  TRP TRP A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  LEU 16  16  16  LEU LEU A . n 
A 1 17  ASP 17  17  17  ASP ASP A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  LYS 20  20  20  LYS LYS A . n 
A 1 21  TYR 21  21  21  TYR TYR A . n 
A 1 22  PHE 22  22  22  PHE PHE A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ILE 26  26  26  ILE ILE A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  TYR 28  28  28  TYR TYR A . n 
A 1 29  GLU 29  29  29  GLU GLU A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  ARG 33  33  33  ARG ARG A . n 
A 1 34  PRO 34  34  34  PRO PRO A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  GLN 36  36  36  GLN GLN A . n 
A 1 37  ALA 37  37  37  ALA ALA A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ARG 43  43  43  ARG ARG A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ASP 45  45  45  ASP ASP A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  GLU 48  48  48  GLU GLU A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  MET 50  50  50  MET MET A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  PHE 52  52  52  PHE PHE A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  GLU 59  59  59  GLU GLU A . n 
A 1 60  GLY 60  60  60  GLY GLY A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  TYR 62  62  62  TYR TYR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  ILE 65  65  65  ILE ILE A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  TRP 68  68  68  TRP TRP A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  GLN 70  70  70  GLN GLN A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  GLN 75  75  75  GLN GLN A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  LYS 77  77  77  LYS LYS A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  VAL 79  79  79  VAL VAL A . n 
A 1 80  GLN 80  80  80  GLN GLN A . n 
A 1 81  GLU 81  81  81  GLU GLU A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  LYS 85  85  85  LYS LYS A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ILE 87  87  87  ILE ILE A . n 
A 1 88  MET 88  88  88  MET MET A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ILE 90  90  90  ILE ILE A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ILE 92  92  92  ILE ILE A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  PRO 94  94  94  PRO PRO A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  TYR 98  98  98  TYR TYR A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ASP 100 100 100 ASP ASP A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 LYS 105 105 105 LYS LYS A . n 
A 1 106 ASP 106 106 106 ASP ASP A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLU 108 108 108 GLU GLU A . n 
A 1 109 ILE 109 109 109 ILE ILE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 ARG 113 113 113 ARG ARG A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ASN 116 116 116 ASN ASN A . n 
A 1 117 TYR 117 117 117 TYR TYR A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 LYS 119 119 119 LYS LYS A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 CYS 123 123 123 CYS CYS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 LEU 128 128 128 LEU LEU A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 ILE 130 130 130 ILE ILE A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLN 134 134 134 GLN GLN A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ASP 136 136 136 ASP ASP A . n 
A 1 137 HIS 137 137 137 HIS HIS A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 HIS 139 139 139 HIS HIS A . n 
A 1 140 SER 140 140 140 SER SER A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 LYS 144 144 144 LYS LYS A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 LEU 149 149 149 LEU LEU A . n 
A 1 150 MET 150 150 150 MET MET A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 THR 152 152 152 THR THR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ILE 154 154 154 ILE ILE A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 ILE 156 156 156 ILE ILE A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 HIS 158 158 158 HIS HIS A . n 
A 1 159 LYS 159 159 159 LYS LYS A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 PRO 162 162 162 PRO PRO A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ILE 164 164 164 ILE ILE A . n 
A 1 165 PRO 165 165 165 PRO PRO A . n 
A 1 166 VAL 166 166 166 VAL VAL A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 ALA 170 170 170 ALA ALA A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 ILE 174 174 174 ILE ILE A . n 
A 1 175 SER 175 175 175 SER SER A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 TYR 177 177 177 TYR TYR A . n 
A 1 178 MET 178 178 178 MET MET A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ILE 182 182 182 ILE ILE A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 ALA 187 187 187 ALA ALA A . n 
A 1 188 TYR 188 188 188 TYR TYR A . n 
A 1 189 ASN 189 189 189 ASN ASN A . n 
A 1 190 CYS 190 190 190 CYS CYS A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ASP 192 192 192 ASP ASP A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 GLY 196 196 196 GLY GLY A . n 
A 1 197 GLN 197 197 197 GLN GLN A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 MET 201 201 201 MET MET A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 LYS 204 204 204 LYS LYS A . n 
A 1 205 ASP 205 205 205 ASP ASP A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 ILE 207 207 207 ILE ILE A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 LEU 210 210 210 LEU LEU A . n 
A 1 211 ASN 211 211 211 ASN ASN A . n 
A 1 212 GLU 212 212 212 GLU GLU A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ASP 217 217 217 ASP ASP A . n 
A 1 218 LYS 218 218 218 LYS LYS A . n 
A 1 219 PRO 219 219 219 PRO PRO A . n 
A 1 220 PHE 220 220 220 PHE PHE A . n 
A 1 221 ILE 221 221 221 ILE ILE A . n 
A 1 222 THR 222 222 222 THR THR A . n 
A 1 223 THR 223 223 223 THR THR A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 GLY 226 226 226 GLY GLY A . n 
A 1 227 TYR 227 227 227 TYR TYR A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 VAL 229 229 229 VAL VAL A . n 
A 1 230 SER 230 230 230 SER SER A . n 
A 1 231 PRO 231 231 231 PRO PRO A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 GLY 233 233 233 GLY GLY A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 GLN 237 237 237 GLN GLN A . n 
A 1 238 TYR 238 238 238 TYR TYR A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 SER 240 240 240 SER SER A . n 
A 1 241 ASN 241 241 241 ASN ASN A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 LEU 243 243 243 LEU LEU A . n 
A 1 244 LYS 244 244 244 LYS LYS A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 GLN 246 246 246 GLN GLN A . n 
A 1 247 SER 247 247 247 SER SER A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 ILE 251 251 251 ILE ILE A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 ASN 253 253 253 ASN ASN A . n 
A 1 254 TYR 254 254 254 TYR TYR A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 ASP 256 256 256 ASP ASP A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 GLY 261 261 261 GLY GLY A . n 
A 1 262 ALA 262 262 262 ALA ALA A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 MET 265 265 265 MET MET A . n 
A 1 266 CYS 266 266 266 CYS CYS A . n 
A 1 267 PRO 267 267 267 PRO PRO A . n 
A 1 268 PHE 268 268 268 PHE PHE A . n 
A 1 269 TYR 269 269 269 TYR TYR A . n 
A 1 270 TYR 270 270 270 TYR TYR A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 ASP 272 272 272 ASP ASP A . n 
A 1 273 GLY 273 273 273 GLY GLY A . n 
A 1 274 TRP 274 274 274 TRP TRP A . n 
A 1 275 TRP 275 275 275 TRP TRP A . n 
A 1 276 LYS 276 276 276 LYS LYS A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 GLU 279 279 279 GLU GLU A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 SER 281 281 281 SER SER A . n 
A 1 282 ASP 282 282 282 ASP ASP A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ASN 286 286 286 ASN ASN A . n 
A 1 287 GLN 287 287 287 GLN GLN A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 GLU 289 289 289 GLU GLU A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 TRP 291 291 291 TRP TRP A . n 
A 1 292 PHE 292 292 292 PHE PHE A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 TRP 295 295 295 TRP TRP A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 TYR 297 297 297 TYR TYR A . n 
A 1 298 SER 298 298 298 SER SER A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 LEU 300 300 300 LEU LEU A . n 
A 1 301 ASN 301 301 301 ASN ASN A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 LYS 303 303 303 LYS LYS A . n 
A 1 304 TYR 304 304 304 TYR TYR A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 THR 306 306 306 THR THR A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 ARG 308 308 308 ARG ARG A . n 
A 1 309 PRO 309 309 309 PRO PRO A . n 
A 1 310 VAL 310 310 310 VAL VAL A . n 
A 1 311 TRP 311 311 311 TRP TRP A . n 
A 1 312 PHE 312 312 312 PHE PHE A . n 
A 1 313 ALA 313 313 313 ALA ALA A . n 
A 1 314 MET 314 314 314 MET MET A . n 
A 1 315 ARG 315 315 315 ARG ARG A . n 
A 1 316 ASP 316 316 316 ASP ASP A . n 
A 1 317 TYR 317 317 317 TYR TYR A . n 
A 1 318 MET 318 318 318 MET MET A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ILE 323 323 323 ILE ILE A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 PRO 325 325 325 PRO PRO A . n 
A 1 326 LYS 326 326 326 LYS LYS A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 LYS 328 328 328 LYS LYS A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 ILE 330 330 330 ILE ILE A . n 
A 1 331 HIS 331 331 331 HIS HIS A . n 
A 1 332 THR 332 332 332 THR THR A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 THR 334 334 334 THR THR A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 ILE 336 336 336 ILE ILE A . n 
A 1 337 PRO 337 337 337 PRO PRO A . n 
A 1 338 LEU 338 338 338 LEU LEU A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 LEU 340 340 340 LEU LEU A . n 
A 1 341 TYR 341 341 341 TYR TYR A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 ASP 343 343 343 ASP ASP A . n 
A 1 344 LYS 344 344 344 LYS LYS A . n 
A 1 345 ASP 345 345 345 ASP ASP A . n 
A 1 346 VAL 346 346 346 VAL VAL A . n 
A 1 347 LYS 347 347 347 LYS LYS A . n 
A 1 348 LYS 348 348 348 LYS LYS A . n 
A 1 349 VAL 349 349 349 VAL VAL A . n 
A 1 350 VAL 350 350 350 VAL VAL A . n 
A 1 351 VAL 351 351 351 VAL VAL A . n 
A 1 352 LYS 352 352 352 LYS LYS A . n 
A 1 353 PHE 353 353 353 PHE PHE A . n 
A 1 354 ARG 354 354 354 ARG ARG A . n 
A 1 355 ASP 355 355 355 ASP ASP A . n 
A 1 356 LYS 356 356 356 LYS LYS A . n 
A 1 357 VAL 357 357 357 VAL VAL A . n 
A 1 358 ILE 358 358 358 ILE ILE A . n 
A 1 359 TYR 359 359 359 TYR TYR A . n 
A 1 360 SER 360 360 360 SER SER A . n 
A 1 361 LYS 361 361 361 LYS LYS A . n 
A 1 362 ASN 362 362 362 ASN ASN A . n 
A 1 363 ILE 363 363 363 ILE ILE A . n 
A 1 364 THR 364 364 364 THR THR A . n 
A 1 365 SER 365 365 365 SER SER A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 GLY 367 367 367 GLY GLY A . n 
A 1 368 TYR 368 368 368 TYR TYR A . n 
A 1 369 MET 369 369 369 MET MET A . n 
A 1 370 ALA 370 370 370 ALA ALA A . n 
A 1 371 ASP 371 371 371 ASP ASP A . n 
A 1 372 GLU 372 372 372 GLU GLU A . n 
A 1 373 LEU 373 373 373 LEU LEU A . n 
A 1 374 THR 374 374 374 THR THR A . n 
A 1 375 ILE 375 375 375 ILE ILE A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 GLY 379 379 379 GLY GLY A . n 
A 1 380 ILE 380 380 380 ILE ILE A . n 
A 1 381 GLU 381 381 381 GLU GLU A . n 
A 1 382 ASP 382 382 382 ASP ASP A . n 
A 1 383 MET 383 383 383 MET MET A . n 
A 1 384 GLU 384 384 384 GLU GLU A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 ALA 386 386 386 ALA ALA A . n 
A 1 387 PHE 387 387 387 PHE PHE A . n 
A 1 388 GLU 388 388 388 GLU GLU A . n 
A 1 389 PHE 389 389 389 PHE PHE A . n 
A 1 390 TYR 390 390 390 TYR TYR A . n 
A 1 391 ASP 391 391 391 ASP ASP A . n 
A 1 392 SER 392 392 392 SER SER A . n 
A 1 393 ASP 393 393 393 ASP ASP A . n 
A 1 394 ASN 394 394 394 ASN ASN A . n 
A 1 395 LYS 395 395 395 LYS LYS A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 ILE 397 397 397 ILE ILE A . n 
A 1 398 LYS 398 398 398 LYS LYS A . n 
A 1 399 ASN 399 399 399 ASN ASN A . n 
A 1 400 GLU 400 400 400 GLU GLU A . n 
A 1 401 SER 401 401 401 SER SER A . n 
A 1 402 ILE 402 402 402 ILE ILE A . n 
A 1 403 ASN 403 403 403 ASN ASN A . n 
A 1 404 ILE 404 404 404 ILE ILE A . n 
A 1 405 LEU 405 405 405 LEU LEU A . n 
A 1 406 ALA 406 406 406 ALA ALA A . n 
A 1 407 SER 407 407 407 SER SER A . n 
A 1 408 LYS 408 408 408 LYS LYS A . n 
A 1 409 THR 409 409 409 THR THR A . n 
A 1 410 ALA 410 410 410 ALA ALA A . n 
A 1 411 PHE 411 411 411 PHE PHE A . n 
A 1 412 GLU 412 412 412 GLU GLU A . n 
A 1 413 LEU 413 413 413 LEU LEU A . n 
A 1 414 PRO 414 414 414 PRO PRO A . n 
A 1 415 GLU 415 415 415 GLU GLU A . n 
A 1 416 LEU 416 416 416 LEU LEU A . n 
A 1 417 THR 417 417 417 THR THR A . n 
A 1 418 ILE 418 418 418 ILE ILE A . n 
A 1 419 GLU 419 419 419 GLU GLU A . n 
A 1 420 VAL 420 420 420 VAL VAL A . n 
A 1 421 THR 421 421 421 THR THR A . n 
A 1 422 PRO 422 422 422 PRO PRO A . n 
A 1 423 GLU 423 423 423 GLU GLU A . n 
A 1 424 LYS 424 424 424 LYS LYS A . n 
A 1 425 ASP 425 425 425 ASP ASP A . n 
A 1 426 LEU 426 426 426 LEU LEU A . n 
A 1 427 ASN 427 427 427 ASN ASN A . n 
A 1 428 GLU 428 428 428 GLU GLU A . n 
A 1 429 GLY 429 429 429 GLY GLY A . n 
A 1 430 LYS 430 430 430 LYS LYS A . n 
A 1 431 ILE 431 431 431 ILE ILE A . n 
A 1 432 ALA 432 432 432 ALA ALA A . n 
A 1 433 SER 433 433 433 SER SER A . n 
A 1 434 ILE 434 434 434 ILE ILE A . n 
A 1 435 LYS 435 435 435 LYS LYS A . n 
A 1 436 THR 436 436 436 THR THR A . n 
A 1 437 LYS 437 437 437 LYS LYS A . n 
A 1 438 ILE 438 438 438 ILE ILE A . n 
A 1 439 GLU 439 439 439 GLU GLU A . n 
A 1 440 THR 440 440 440 THR THR A . n 
A 1 441 SER 441 441 441 SER SER A . n 
A 1 442 GLU 442 442 442 GLU GLU A . n 
A 1 443 ASN 443 443 443 ASN ASN A . n 
A 1 444 PHE 444 444 444 PHE PHE A . n 
A 1 445 THR 445 445 445 THR THR A . n 
A 1 446 LEU 446 446 446 LEU LEU A . n 
A 1 447 LEU 447 447 447 LEU LEU A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 ASP 449 449 449 ASP ASP A . n 
A 1 450 LEU 450 450 450 LEU LEU A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 ILE 452 452 452 ILE ILE A . n 
A 1 453 SER 453 453 453 SER SER A . n 
A 1 454 TYR 454 454 454 TYR TYR A . n 
A 1 455 ASN 455 455 455 ASN ASN A . n 
A 1 456 THR 456 456 456 THR THR A . n 
A 1 457 HIS 457 457 457 HIS HIS A . n 
A 1 458 LEU 458 458 458 LEU LEU A . n 
A 1 459 GLY 459 459 459 GLY GLY A . n 
A 1 460 TRP 460 460 460 TRP TRP A . n 
A 1 461 ALA 461 461 461 ALA ALA A . n 
A 1 462 ILE 462 462 462 ILE ILE A . n 
A 1 463 GLY 463 463 463 GLY GLY A . n 
A 1 464 SER 464 464 464 SER SER A . n 
A 1 465 GLN 465 465 465 GLN GLN A . n 
A 1 466 ALA 466 466 466 ALA ALA A . n 
A 1 467 SER 467 467 467 SER SER A . n 
A 1 468 VAL 468 468 468 VAL VAL A . n 
A 1 469 SER 469 469 469 SER SER A . n 
A 1 470 ILE 470 470 470 ILE ILE A . n 
A 1 471 SER 471 471 471 SER SER A . n 
A 1 472 ASP 472 472 472 ASP ASP A . n 
A 1 473 GLN 473 473 473 GLN GLN A . n 
A 1 474 LEU 474 474 474 LEU LEU A . n 
A 1 475 ASP 475 475 475 ASP ASP A . n 
A 1 476 LYS 476 476 476 LYS LYS A . n 
A 1 477 LYS 477 477 477 LYS LYS A . n 
A 1 478 ILE 478 478 478 ILE ILE A . n 
A 1 479 ILE 479 479 479 ILE ILE A . n 
A 1 480 THR 480 480 480 THR THR A . n 
A 1 481 SER 481 481 481 SER SER A . n 
A 1 482 GLU 482 482 482 GLU GLU A . n 
A 1 483 ASN 483 483 483 ASN ASN A . n 
A 1 484 PHE 484 484 484 PHE PHE A . n 
A 1 485 PHE 485 485 485 PHE PHE A . n 
A 1 486 ASN 486 486 486 ASN ASN A . n 
A 1 487 ILE 487 487 487 ILE ILE A . n 
A 1 488 PRO 488 488 488 PRO PRO A . n 
A 1 489 ASP 489 489 489 ASP ASP A . n 
A 1 490 ASN 490 490 490 ASN ASN A . n 
A 1 491 CYS 491 491 491 CYS CYS A . n 
A 1 492 TRP 492 492 492 TRP TRP A . n 
A 1 493 VAL 493 493 493 VAL VAL A . n 
A 1 494 VAL 494 494 494 VAL VAL A . n 
A 1 495 ASN 495 495 495 ASN ASN A . n 
A 1 496 ALA 496 496 496 ALA ALA A . n 
A 1 497 SER 497 497 497 SER SER A . n 
A 1 498 ALA 498 498 498 ALA ALA A . n 
A 1 499 GLY 499 499 499 GLY GLY A . n 
A 1 500 ILE 500 500 500 ILE ILE A . n 
A 1 501 SER 501 501 501 SER SER A . n 
A 1 502 VAL 502 502 502 VAL VAL A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 TYR 504 504 504 TYR TYR A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 LYS 506 506 506 LYS LYS A . n 
A 1 507 PHE 507 507 507 PHE PHE A . n 
A 1 508 THR 508 508 508 THR THR A . n 
A 1 509 PHE 509 509 509 PHE PHE A . n 
A 1 510 LYS 510 510 510 LYS LYS A . n 
A 1 511 ILE 511 511 511 ILE ILE A . n 
A 1 512 HIS 512 512 512 HIS HIS A . n 
A 1 513 ASP 513 513 513 ASP ASP A . n 
A 1 514 GLN 514 514 514 GLN GLN A . n 
A 1 515 LYS 515 515 515 LYS LYS A . n 
A 1 516 ILE 516 516 516 ILE ILE A . n 
A 1 517 ILE 517 517 517 ILE ILE A . n 
A 1 518 TYR 518 518 518 TYR TYR A . n 
A 1 519 ARG 519 519 519 ARG ARG A . n 
A 1 520 GLY 520 520 520 GLY GLY A . n 
A 1 521 ASP 521 521 521 ASP ASP A . n 
A 1 522 TRP 522 522 522 TRP TRP A . n 
A 1 523 ALA 523 523 523 ALA ALA A . n 
A 1 524 LYS 524 524 524 LYS LYS A . n 
A 1 525 GLU 525 525 525 GLU GLU A . n 
A 1 526 VAL 526 526 526 VAL VAL A . n 
A 1 527 GLY 527 527 527 GLY GLY A . n 
A 1 528 ARG 528 528 528 ARG ARG A . n 
A 1 529 LYS 529 529 529 LYS LYS A . n 
A 1 530 LEU 530 530 530 LEU LEU A . n 
A 1 531 GLU 531 531 ?   ?   ?   A . n 
A 1 532 HIS 532 532 ?   ?   ?   A . n 
A 1 533 HIS 533 533 ?   ?   ?   A . n 
A 1 534 HIS 534 534 ?   ?   ?   A . n 
A 1 535 HIS 535 535 ?   ?   ?   A . n 
A 1 536 HIS 536 536 ?   ?   ?   A . n 
A 1 537 HIS 537 537 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   GLN 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   LYS 4   4   4   LYS LYS B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   LYS 6   6   6   LYS LYS B . n 
B 1 7   ILE 7   7   7   ILE ILE B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  ASN 12  12  12  ASN ASN B . n 
B 1 13  TRP 13  13  13  TRP TRP B . n 
B 1 14  TYR 14  14  14  TYR TYR B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  LEU 16  16  16  LEU LEU B . n 
B 1 17  ASP 17  17  17  ASP ASP B . n 
B 1 18  GLY 18  18  18  GLY GLY B . n 
B 1 19  GLU 19  19  19  GLU GLU B . n 
B 1 20  LYS 20  20  20  LYS LYS B . n 
B 1 21  TYR 21  21  21  TYR TYR B . n 
B 1 22  PHE 22  22  22  PHE PHE B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  LYS 24  24  24  LYS LYS B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ILE 26  26  26  ILE ILE B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  TYR 28  28  28  TYR TYR B . n 
B 1 29  GLU 29  29  29  GLU GLU B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  ARG 33  33  33  ARG ARG B . n 
B 1 34  PRO 34  34  34  PRO PRO B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  GLN 36  36  36  GLN GLN B . n 
B 1 37  ALA 37  37  37  ALA ALA B . n 
B 1 38  PRO 38  38  38  PRO PRO B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  ASP 41  41  41  ASP ASP B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  ARG 43  43  43  ARG ARG B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  ASP 45  45  45  ASP ASP B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  LEU 47  47  47  LEU LEU B . n 
B 1 48  GLU 48  48  48  GLU GLU B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  MET 50  50  50  MET MET B . n 
B 1 51  LYS 51  51  51  LYS LYS B . n 
B 1 52  PHE 52  52  52  PHE PHE B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  GLU 59  59  59  GLU GLU B . n 
B 1 60  GLY 60  60  60  GLY GLY B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  TYR 62  62  62  TYR TYR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  THR 64  64  64  THR THR B . n 
B 1 65  ILE 65  65  65  ILE ILE B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  THR 67  67  67  THR THR B . n 
B 1 68  TRP 68  68  68  TRP TRP B . n 
B 1 69  SER 69  69  69  SER SER B . n 
B 1 70  GLN 70  70  70  GLN GLN B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  GLN 75  75  75  GLN GLN B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  LYS 77  77  77  LYS LYS B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  VAL 79  79  79  VAL VAL B . n 
B 1 80  GLN 80  80  80  GLN GLN B . n 
B 1 81  GLU 81  81  81  GLU GLU B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  LYS 85  85  85  LYS LYS B . n 
B 1 86  LEU 86  86  86  LEU LEU B . n 
B 1 87  ILE 87  87  87  ILE ILE B . n 
B 1 88  MET 88  88  88  MET MET B . n 
B 1 89  GLY 89  89  89  GLY GLY B . n 
B 1 90  ILE 90  90  90  ILE ILE B . n 
B 1 91  ASP 91  91  91  ASP ASP B . n 
B 1 92  ILE 92  92  92  ILE ILE B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  PRO 94  94  94  PRO PRO B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  GLU 96  96  96  GLU GLU B . n 
B 1 97  ASP 97  97  97  ASP ASP B . n 
B 1 98  TYR 98  98  98  TYR TYR B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 ASP 100 100 100 ASP ASP B . n 
B 1 101 PRO 101 101 101 PRO PRO B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 LYS 105 105 105 LYS LYS B . n 
B 1 106 ASP 106 106 106 ASP ASP B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLU 108 108 108 GLU GLU B . n 
B 1 109 ILE 109 109 109 ILE ILE B . n 
B 1 110 GLU 110 110 110 GLU GLU B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 LYS 112 112 112 LYS LYS B . n 
B 1 113 ARG 113 113 113 ARG ARG B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ASN 116 116 116 ASN ASN B . n 
B 1 117 TYR 117 117 117 TYR TYR B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 LYS 119 119 119 LYS LYS B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 CYS 123 123 123 CYS CYS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 TYR 127 127 127 TYR TYR B . n 
B 1 128 LEU 128 128 128 LEU LEU B . n 
B 1 129 VAL 129 129 129 VAL VAL B . n 
B 1 130 ILE 130 130 130 ILE ILE B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 GLN 134 134 134 GLN GLN B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ASP 136 136 136 ASP ASP B . n 
B 1 137 HIS 137 137 137 HIS HIS B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 HIS 139 139 139 HIS HIS B . n 
B 1 140 SER 140 140 140 SER SER B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 LYS 144 144 144 LYS LYS B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 LEU 149 149 149 LEU LEU B . n 
B 1 150 MET 150 150 150 MET MET B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 THR 152 152 152 THR THR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ILE 154 154 154 ILE ILE B . n 
B 1 155 ASN 155 155 155 ASN ASN B . n 
B 1 156 ILE 156 156 156 ILE ILE B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 HIS 158 158 158 HIS HIS B . n 
B 1 159 LYS 159 159 159 LYS LYS B . n 
B 1 160 GLY 160 160 160 GLY GLY B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 PRO 162 162 162 PRO PRO B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 ILE 164 164 164 ILE ILE B . n 
B 1 165 PRO 165 165 165 PRO PRO B . n 
B 1 166 VAL 166 166 166 VAL VAL B . n 
B 1 167 THR 167 167 167 THR THR B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 ALA 170 170 170 ALA ALA B . n 
B 1 171 ASN 171 171 171 ASN ASN B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 MET 173 173 173 MET MET B . n 
B 1 174 ILE 174 174 174 ILE ILE B . n 
B 1 175 SER 175 175 175 SER SER B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 TYR 177 177 177 TYR TYR B . n 
B 1 178 MET 178 178 178 MET MET B . n 
B 1 179 ASP 179 179 179 ASP ASP B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 ILE 182 182 182 ILE ILE B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 VAL 185 185 185 VAL VAL B . n 
B 1 186 TYR 186 186 186 TYR TYR B . n 
B 1 187 ALA 187 187 187 ALA ALA B . n 
B 1 188 TYR 188 188 188 TYR TYR B . n 
B 1 189 ASN 189 189 189 ASN ASN B . n 
B 1 190 CYS 190 190 190 CYS CYS B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ASP 192 192 192 ASP ASP B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 GLY 196 196 196 GLY GLY B . n 
B 1 197 GLN 197 197 197 GLN GLN B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 ALA 199 199 199 ALA ALA B . n 
B 1 200 THR 200 200 200 THR THR B . n 
B 1 201 MET 201 201 201 MET MET B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 LYS 204 204 204 LYS LYS B . n 
B 1 205 ASP 205 205 205 ASP ASP B . n 
B 1 206 TYR 206 206 206 TYR TYR B . n 
B 1 207 ILE 207 207 207 ILE ILE B . n 
B 1 208 LYS 208 208 208 LYS LYS B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 LEU 210 210 210 LEU LEU B . n 
B 1 211 ASN 211 211 211 ASN ASN B . n 
B 1 212 GLU 212 212 212 GLU GLU B . n 
B 1 213 LEU 213 213 213 LEU LEU B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 ASP 217 217 217 ASP ASP B . n 
B 1 218 LYS 218 218 218 LYS LYS B . n 
B 1 219 PRO 219 219 219 PRO PRO B . n 
B 1 220 PHE 220 220 220 PHE PHE B . n 
B 1 221 ILE 221 221 221 ILE ILE B . n 
B 1 222 THR 222 222 222 THR THR B . n 
B 1 223 THR 223 223 223 THR THR B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 PHE 225 225 225 PHE PHE B . n 
B 1 226 GLY 226 226 226 GLY GLY B . n 
B 1 227 TYR 227 227 227 TYR TYR B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 VAL 229 229 229 VAL VAL B . n 
B 1 230 SER 230 230 230 SER SER B . n 
B 1 231 PRO 231 231 231 PRO PRO B . n 
B 1 232 GLU 232 232 232 GLU GLU B . n 
B 1 233 GLY 233 233 233 GLY GLY B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 GLY 236 236 236 GLY GLY B . n 
B 1 237 GLN 237 237 237 GLN GLN B . n 
B 1 238 TYR 238 238 238 TYR TYR B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 SER 240 240 240 SER SER B . n 
B 1 241 ASN 241 241 241 ASN ASN B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 LEU 243 243 243 LEU LEU B . n 
B 1 244 LYS 244 244 244 LYS LYS B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 GLN 246 246 246 GLN GLN B . n 
B 1 247 SER 247 247 247 SER SER B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 ILE 251 251 251 ILE ILE B . n 
B 1 252 SER 252 252 252 SER SER B . n 
B 1 253 ASN 253 253 253 ASN ASN B . n 
B 1 254 TYR 254 254 254 TYR TYR B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 ASP 256 256 256 ASP ASP B . n 
B 1 257 LEU 257 257 257 LEU LEU B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 ASP 259 259 259 ASP ASP B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 GLY 261 261 261 GLY GLY B . n 
B 1 262 ALA 262 262 262 ALA ALA B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 MET 265 265 265 MET MET B . n 
B 1 266 CYS 266 266 266 CYS CYS B . n 
B 1 267 PRO 267 267 267 PRO PRO B . n 
B 1 268 PHE 268 268 268 PHE PHE B . n 
B 1 269 TYR 269 269 269 TYR TYR B . n 
B 1 270 TYR 270 270 270 TYR TYR B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 ASP 272 272 272 ASP ASP B . n 
B 1 273 GLY 273 273 273 GLY GLY B . n 
B 1 274 TRP 274 274 274 TRP TRP B . n 
B 1 275 TRP 275 275 275 TRP TRP B . n 
B 1 276 LYS 276 276 276 LYS LYS B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 GLU 279 279 279 GLU GLU B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 SER 281 281 281 SER SER B . n 
B 1 282 ASP 282 282 282 ASP ASP B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 ASN 286 286 286 ASN ASN B . n 
B 1 287 GLN 287 287 287 GLN GLN B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 GLU 289 289 289 GLU GLU B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 TRP 291 291 291 TRP TRP B . n 
B 1 292 PHE 292 292 292 PHE PHE B . n 
B 1 293 GLY 293 293 293 GLY GLY B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 TRP 295 295 295 TRP TRP B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 TYR 297 297 297 TYR TYR B . n 
B 1 298 SER 298 298 298 SER SER B . n 
B 1 299 ASP 299 299 299 ASP ASP B . n 
B 1 300 LEU 300 300 300 LEU LEU B . n 
B 1 301 ASN 301 301 301 ASN ASN B . n 
B 1 302 ASP 302 302 302 ASP ASP B . n 
B 1 303 LYS 303 303 303 LYS LYS B . n 
B 1 304 TYR 304 304 304 TYR TYR B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 THR 306 306 306 THR THR B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 ARG 308 308 308 ARG ARG B . n 
B 1 309 PRO 309 309 309 PRO PRO B . n 
B 1 310 VAL 310 310 310 VAL VAL B . n 
B 1 311 TRP 311 311 311 TRP TRP B . n 
B 1 312 PHE 312 312 312 PHE PHE B . n 
B 1 313 ALA 313 313 313 ALA ALA B . n 
B 1 314 MET 314 314 314 MET MET B . n 
B 1 315 ARG 315 315 315 ARG ARG B . n 
B 1 316 ASP 316 316 316 ASP ASP B . n 
B 1 317 TYR 317 317 317 TYR TYR B . n 
B 1 318 MET 318 318 318 MET MET B . n 
B 1 319 LYS 319 319 319 LYS LYS B . n 
B 1 320 GLY 320 320 320 GLY GLY B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 ILE 322 322 322 ILE ILE B . n 
B 1 323 ILE 323 323 323 ILE ILE B . n 
B 1 324 SER 324 324 324 SER SER B . n 
B 1 325 PRO 325 325 325 PRO PRO B . n 
B 1 326 LYS 326 326 326 LYS LYS B . n 
B 1 327 ASN 327 327 327 ASN ASN B . n 
B 1 328 LYS 328 328 328 LYS LYS B . n 
B 1 329 SER 329 329 329 SER SER B . n 
B 1 330 ILE 330 330 330 ILE ILE B . n 
B 1 331 HIS 331 331 331 HIS HIS B . n 
B 1 332 THR 332 332 332 THR THR B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 THR 334 334 334 THR THR B . n 
B 1 335 LYS 335 335 335 LYS LYS B . n 
B 1 336 ILE 336 336 336 ILE ILE B . n 
B 1 337 PRO 337 337 337 PRO PRO B . n 
B 1 338 LEU 338 338 338 LEU LEU B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 LEU 340 340 340 LEU LEU B . n 
B 1 341 TYR 341 341 341 TYR TYR B . n 
B 1 342 ASN 342 342 342 ASN ASN B . n 
B 1 343 ASP 343 343 343 ASP ASP B . n 
B 1 344 LYS 344 344 344 LYS LYS B . n 
B 1 345 ASP 345 345 345 ASP ASP B . n 
B 1 346 VAL 346 346 346 VAL VAL B . n 
B 1 347 LYS 347 347 347 LYS LYS B . n 
B 1 348 LYS 348 348 348 LYS LYS B . n 
B 1 349 VAL 349 349 349 VAL VAL B . n 
B 1 350 VAL 350 350 350 VAL VAL B . n 
B 1 351 VAL 351 351 351 VAL VAL B . n 
B 1 352 LYS 352 352 352 LYS LYS B . n 
B 1 353 PHE 353 353 353 PHE PHE B . n 
B 1 354 ARG 354 354 354 ARG ARG B . n 
B 1 355 ASP 355 355 355 ASP ASP B . n 
B 1 356 LYS 356 356 356 LYS LYS B . n 
B 1 357 VAL 357 357 357 VAL VAL B . n 
B 1 358 ILE 358 358 358 ILE ILE B . n 
B 1 359 TYR 359 359 359 TYR TYR B . n 
B 1 360 SER 360 360 360 SER SER B . n 
B 1 361 LYS 361 361 361 LYS LYS B . n 
B 1 362 ASN 362 362 362 ASN ASN B . n 
B 1 363 ILE 363 363 363 ILE ILE B . n 
B 1 364 THR 364 364 364 THR THR B . n 
B 1 365 SER 365 365 365 SER SER B . n 
B 1 366 GLU 366 366 366 GLU GLU B . n 
B 1 367 GLY 367 367 367 GLY GLY B . n 
B 1 368 TYR 368 368 368 TYR TYR B . n 
B 1 369 MET 369 369 369 MET MET B . n 
B 1 370 ALA 370 370 370 ALA ALA B . n 
B 1 371 ASP 371 371 371 ASP ASP B . n 
B 1 372 GLU 372 372 372 GLU GLU B . n 
B 1 373 LEU 373 373 373 LEU LEU B . n 
B 1 374 THR 374 374 374 THR THR B . n 
B 1 375 ILE 375 375 375 ILE ILE B . n 
B 1 376 ASP 376 376 376 ASP ASP B . n 
B 1 377 PRO 377 377 377 PRO PRO B . n 
B 1 378 VAL 378 378 378 VAL VAL B . n 
B 1 379 GLY 379 379 379 GLY GLY B . n 
B 1 380 ILE 380 380 380 ILE ILE B . n 
B 1 381 GLU 381 381 381 GLU GLU B . n 
B 1 382 ASP 382 382 382 ASP ASP B . n 
B 1 383 MET 383 383 383 MET MET B . n 
B 1 384 GLU 384 384 384 GLU GLU B . n 
B 1 385 LEU 385 385 385 LEU LEU B . n 
B 1 386 ALA 386 386 386 ALA ALA B . n 
B 1 387 PHE 387 387 387 PHE PHE B . n 
B 1 388 GLU 388 388 388 GLU GLU B . n 
B 1 389 PHE 389 389 389 PHE PHE B . n 
B 1 390 TYR 390 390 390 TYR TYR B . n 
B 1 391 ASP 391 391 391 ASP ASP B . n 
B 1 392 SER 392 392 392 SER SER B . n 
B 1 393 ASP 393 393 393 ASP ASP B . n 
B 1 394 ASN 394 394 394 ASN ASN B . n 
B 1 395 LYS 395 395 395 LYS LYS B . n 
B 1 396 ILE 396 396 396 ILE ILE B . n 
B 1 397 ILE 397 397 397 ILE ILE B . n 
B 1 398 LYS 398 398 398 LYS LYS B . n 
B 1 399 ASN 399 399 399 ASN ASN B . n 
B 1 400 GLU 400 400 400 GLU GLU B . n 
B 1 401 SER 401 401 401 SER SER B . n 
B 1 402 ILE 402 402 402 ILE ILE B . n 
B 1 403 ASN 403 403 403 ASN ASN B . n 
B 1 404 ILE 404 404 404 ILE ILE B . n 
B 1 405 LEU 405 405 405 LEU LEU B . n 
B 1 406 ALA 406 406 406 ALA ALA B . n 
B 1 407 SER 407 407 407 SER SER B . n 
B 1 408 LYS 408 408 408 LYS LYS B . n 
B 1 409 THR 409 409 409 THR THR B . n 
B 1 410 ALA 410 410 410 ALA ALA B . n 
B 1 411 PHE 411 411 411 PHE PHE B . n 
B 1 412 GLU 412 412 412 GLU GLU B . n 
B 1 413 LEU 413 413 413 LEU LEU B . n 
B 1 414 PRO 414 414 414 PRO PRO B . n 
B 1 415 GLU 415 415 415 GLU GLU B . n 
B 1 416 LEU 416 416 416 LEU LEU B . n 
B 1 417 THR 417 417 417 THR THR B . n 
B 1 418 ILE 418 418 418 ILE ILE B . n 
B 1 419 GLU 419 419 419 GLU GLU B . n 
B 1 420 VAL 420 420 420 VAL VAL B . n 
B 1 421 THR 421 421 421 THR THR B . n 
B 1 422 PRO 422 422 422 PRO PRO B . n 
B 1 423 GLU 423 423 423 GLU GLU B . n 
B 1 424 LYS 424 424 424 LYS LYS B . n 
B 1 425 ASP 425 425 425 ASP ASP B . n 
B 1 426 LEU 426 426 426 LEU LEU B . n 
B 1 427 ASN 427 427 427 ASN ASN B . n 
B 1 428 GLU 428 428 428 GLU GLU B . n 
B 1 429 GLY 429 429 429 GLY GLY B . n 
B 1 430 LYS 430 430 430 LYS LYS B . n 
B 1 431 ILE 431 431 431 ILE ILE B . n 
B 1 432 ALA 432 432 432 ALA ALA B . n 
B 1 433 SER 433 433 433 SER SER B . n 
B 1 434 ILE 434 434 434 ILE ILE B . n 
B 1 435 LYS 435 435 435 LYS LYS B . n 
B 1 436 THR 436 436 436 THR THR B . n 
B 1 437 LYS 437 437 437 LYS LYS B . n 
B 1 438 ILE 438 438 438 ILE ILE B . n 
B 1 439 GLU 439 439 439 GLU GLU B . n 
B 1 440 THR 440 440 440 THR THR B . n 
B 1 441 SER 441 441 441 SER SER B . n 
B 1 442 GLU 442 442 442 GLU GLU B . n 
B 1 443 ASN 443 443 443 ASN ASN B . n 
B 1 444 PHE 444 444 444 PHE PHE B . n 
B 1 445 THR 445 445 445 THR THR B . n 
B 1 446 LEU 446 446 446 LEU LEU B . n 
B 1 447 LEU 447 447 447 LEU LEU B . n 
B 1 448 ASP 448 448 448 ASP ASP B . n 
B 1 449 ASP 449 449 449 ASP ASP B . n 
B 1 450 LEU 450 450 450 LEU LEU B . n 
B 1 451 LYS 451 451 451 LYS LYS B . n 
B 1 452 ILE 452 452 452 ILE ILE B . n 
B 1 453 SER 453 453 453 SER SER B . n 
B 1 454 TYR 454 454 454 TYR TYR B . n 
B 1 455 ASN 455 455 455 ASN ASN B . n 
B 1 456 THR 456 456 456 THR THR B . n 
B 1 457 HIS 457 457 457 HIS HIS B . n 
B 1 458 LEU 458 458 458 LEU LEU B . n 
B 1 459 GLY 459 459 459 GLY GLY B . n 
B 1 460 TRP 460 460 460 TRP TRP B . n 
B 1 461 ALA 461 461 461 ALA ALA B . n 
B 1 462 ILE 462 462 462 ILE ILE B . n 
B 1 463 GLY 463 463 463 GLY GLY B . n 
B 1 464 SER 464 464 464 SER SER B . n 
B 1 465 GLN 465 465 465 GLN GLN B . n 
B 1 466 ALA 466 466 466 ALA ALA B . n 
B 1 467 SER 467 467 467 SER SER B . n 
B 1 468 VAL 468 468 468 VAL VAL B . n 
B 1 469 SER 469 469 469 SER SER B . n 
B 1 470 ILE 470 470 470 ILE ILE B . n 
B 1 471 SER 471 471 471 SER SER B . n 
B 1 472 ASP 472 472 472 ASP ASP B . n 
B 1 473 GLN 473 473 473 GLN GLN B . n 
B 1 474 LEU 474 474 474 LEU LEU B . n 
B 1 475 ASP 475 475 475 ASP ASP B . n 
B 1 476 LYS 476 476 476 LYS LYS B . n 
B 1 477 LYS 477 477 477 LYS LYS B . n 
B 1 478 ILE 478 478 478 ILE ILE B . n 
B 1 479 ILE 479 479 479 ILE ILE B . n 
B 1 480 THR 480 480 480 THR THR B . n 
B 1 481 SER 481 481 481 SER SER B . n 
B 1 482 GLU 482 482 482 GLU GLU B . n 
B 1 483 ASN 483 483 483 ASN ASN B . n 
B 1 484 PHE 484 484 484 PHE PHE B . n 
B 1 485 PHE 485 485 485 PHE PHE B . n 
B 1 486 ASN 486 486 486 ASN ASN B . n 
B 1 487 ILE 487 487 487 ILE ILE B . n 
B 1 488 PRO 488 488 488 PRO PRO B . n 
B 1 489 ASP 489 489 489 ASP ASP B . n 
B 1 490 ASN 490 490 490 ASN ASN B . n 
B 1 491 CYS 491 491 491 CYS CYS B . n 
B 1 492 TRP 492 492 492 TRP TRP B . n 
B 1 493 VAL 493 493 493 VAL VAL B . n 
B 1 494 VAL 494 494 494 VAL VAL B . n 
B 1 495 ASN 495 495 495 ASN ASN B . n 
B 1 496 ALA 496 496 496 ALA ALA B . n 
B 1 497 SER 497 497 497 SER SER B . n 
B 1 498 ALA 498 498 498 ALA ALA B . n 
B 1 499 GLY 499 499 499 GLY GLY B . n 
B 1 500 ILE 500 500 500 ILE ILE B . n 
B 1 501 SER 501 501 501 SER SER B . n 
B 1 502 VAL 502 502 502 VAL VAL B . n 
B 1 503 ARG 503 503 503 ARG ARG B . n 
B 1 504 TYR 504 504 504 TYR TYR B . n 
B 1 505 GLY 505 505 505 GLY GLY B . n 
B 1 506 LYS 506 506 506 LYS LYS B . n 
B 1 507 PHE 507 507 507 PHE PHE B . n 
B 1 508 THR 508 508 508 THR THR B . n 
B 1 509 PHE 509 509 509 PHE PHE B . n 
B 1 510 LYS 510 510 510 LYS LYS B . n 
B 1 511 ILE 511 511 511 ILE ILE B . n 
B 1 512 HIS 512 512 512 HIS HIS B . n 
B 1 513 ASP 513 513 513 ASP ASP B . n 
B 1 514 GLN 514 514 514 GLN GLN B . n 
B 1 515 LYS 515 515 515 LYS LYS B . n 
B 1 516 ILE 516 516 516 ILE ILE B . n 
B 1 517 ILE 517 517 517 ILE ILE B . n 
B 1 518 TYR 518 518 518 TYR TYR B . n 
B 1 519 ARG 519 519 519 ARG ARG B . n 
B 1 520 GLY 520 520 520 GLY GLY B . n 
B 1 521 ASP 521 521 521 ASP ASP B . n 
B 1 522 TRP 522 522 522 TRP TRP B . n 
B 1 523 ALA 523 523 523 ALA ALA B . n 
B 1 524 LYS 524 524 524 LYS LYS B . n 
B 1 525 GLU 525 525 525 GLU GLU B . n 
B 1 526 VAL 526 526 526 VAL VAL B . n 
B 1 527 GLY 527 527 527 GLY GLY B . n 
B 1 528 ARG 528 528 528 ARG ARG B . n 
B 1 529 LYS 529 529 529 LYS LYS B . n 
B 1 530 LEU 530 530 ?   ?   ?   B . n 
B 1 531 GLU 531 531 ?   ?   ?   B . n 
B 1 532 HIS 532 532 ?   ?   ?   B . n 
B 1 533 HIS 533 533 ?   ?   ?   B . n 
B 1 534 HIS 534 534 ?   ?   ?   B . n 
B 1 535 HIS 535 535 ?   ?   ?   B . n 
B 1 536 HIS 536 536 ?   ?   ?   B . n 
B 1 537 HIS 537 537 ?   ?   ?   B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   GLN 2   2   ?   ?   ?   C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   LYS 4   4   4   LYS LYS C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   LYS 6   6   6   LYS LYS C . n 
C 1 7   ILE 7   7   7   ILE ILE C . n 
C 1 8   GLU 8   8   8   GLU GLU C . n 
C 1 9   LEU 9   9   9   LEU LEU C . n 
C 1 10  LYS 10  10  10  LYS LYS C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  ASN 12  12  12  ASN ASN C . n 
C 1 13  TRP 13  13  13  TRP TRP C . n 
C 1 14  TYR 14  14  14  TYR TYR C . n 
C 1 15  HIS 15  15  15  HIS HIS C . n 
C 1 16  LEU 16  16  16  LEU LEU C . n 
C 1 17  ASP 17  17  17  ASP ASP C . n 
C 1 18  GLY 18  18  18  GLY GLY C . n 
C 1 19  GLU 19  19  19  GLU GLU C . n 
C 1 20  LYS 20  20  20  LYS LYS C . n 
C 1 21  TYR 21  21  21  TYR TYR C . n 
C 1 22  PHE 22  22  22  PHE PHE C . n 
C 1 23  ILE 23  23  23  ILE ILE C . n 
C 1 24  LYS 24  24  24  LYS LYS C . n 
C 1 25  ALA 25  25  25  ALA ALA C . n 
C 1 26  ILE 26  26  26  ILE ILE C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  TYR 28  28  28  TYR TYR C . n 
C 1 29  GLU 29  29  29  GLU GLU C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  ALA 32  32  32  ALA ALA C . n 
C 1 33  ARG 33  33  33  ARG ARG C . n 
C 1 34  PRO 34  34  34  PRO PRO C . n 
C 1 35  GLY 35  35  35  GLY GLY C . n 
C 1 36  GLN 36  36  36  GLN GLN C . n 
C 1 37  ALA 37  37  37  ALA ALA C . n 
C 1 38  PRO 38  38  38  PRO PRO C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  ASP 41  41  41  ASP ASP C . n 
C 1 42  GLU 42  42  42  GLU GLU C . n 
C 1 43  ARG 43  43  43  ARG ARG C . n 
C 1 44  LYS 44  44  44  LYS LYS C . n 
C 1 45  ASP 45  45  45  ASP ASP C . n 
C 1 46  GLU 46  46  46  GLU GLU C . n 
C 1 47  LEU 47  47  47  LEU LEU C . n 
C 1 48  GLU 48  48  48  GLU GLU C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  MET 50  50  50  MET MET C . n 
C 1 51  LYS 51  51  51  LYS LYS C . n 
C 1 52  PHE 52  52  52  PHE PHE C . n 
C 1 53  ASP 53  53  53  ASP ASP C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  GLU 55  55  55  GLU GLU C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  ILE 57  57  57  ILE ILE C . n 
C 1 58  LYS 58  58  58  LYS LYS C . n 
C 1 59  GLU 59  59  59  GLU GLU C . n 
C 1 60  GLY 60  60  60  GLY GLY C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  TYR 62  62  62  TYR TYR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  THR 64  64  64  THR THR C . n 
C 1 65  ILE 65  65  65  ILE ILE C . n 
C 1 66  ARG 66  66  66  ARG ARG C . n 
C 1 67  THR 67  67  67  THR THR C . n 
C 1 68  TRP 68  68  68  TRP TRP C . n 
C 1 69  SER 69  69  69  SER SER C . n 
C 1 70  GLN 70  70  70  GLN GLN C . n 
C 1 71  TYR 71  71  71  TYR TYR C . n 
C 1 72  SER 72  72  72  SER SER C . n 
C 1 73  GLU 73  73  73  GLU GLU C . n 
C 1 74  ASN 74  74  74  ASN ASN C . n 
C 1 75  GLN 75  75  75  GLN GLN C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  LYS 77  77  77  LYS LYS C . n 
C 1 78  LEU 78  78  78  LEU LEU C . n 
C 1 79  VAL 79  79  79  VAL VAL C . n 
C 1 80  GLN 80  80  80  GLN GLN C . n 
C 1 81  GLU 81  81  81  GLU GLU C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  GLY 83  83  83  GLY GLY C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  LYS 85  85  85  LYS LYS C . n 
C 1 86  LEU 86  86  86  LEU LEU C . n 
C 1 87  ILE 87  87  87  ILE ILE C . n 
C 1 88  MET 88  88  88  MET MET C . n 
C 1 89  GLY 89  89  89  GLY GLY C . n 
C 1 90  ILE 90  90  90  ILE ILE C . n 
C 1 91  ASP 91  91  91  ASP ASP C . n 
C 1 92  ILE 92  92  92  ILE ILE C . n 
C 1 93  LYS 93  93  93  LYS LYS C . n 
C 1 94  PRO 94  94  94  PRO PRO C . n 
C 1 95  GLU 95  95  95  GLU GLU C . n 
C 1 96  GLU 96  96  96  GLU GLU C . n 
C 1 97  ASP 97  97  97  ASP ASP C . n 
C 1 98  TYR 98  98  98  TYR TYR C . n 
C 1 99  GLY 99  99  99  GLY GLY C . n 
C 1 100 ASP 100 100 100 ASP ASP C . n 
C 1 101 PRO 101 101 101 PRO PRO C . n 
C 1 102 GLU 102 102 102 GLU GLU C . n 
C 1 103 PHE 103 103 103 PHE PHE C . n 
C 1 104 VAL 104 104 104 VAL VAL C . n 
C 1 105 LYS 105 105 105 LYS LYS C . n 
C 1 106 ASP 106 106 106 ASP ASP C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLU 108 108 108 GLU GLU C . n 
C 1 109 ILE 109 109 109 ILE ILE C . n 
C 1 110 GLU 110 110 110 GLU GLU C . n 
C 1 111 LEU 111 111 111 LEU LEU C . n 
C 1 112 LYS 112 112 112 LYS LYS C . n 
C 1 113 ARG 113 113 113 ARG ARG C . n 
C 1 114 VAL 114 114 114 VAL VAL C . n 
C 1 115 LEU 115 115 115 LEU LEU C . n 
C 1 116 ASN 116 116 116 ASN ASN C . n 
C 1 117 TYR 117 117 117 TYR TYR C . n 
C 1 118 ALA 118 118 118 ALA ALA C . n 
C 1 119 LYS 119 119 119 LYS LYS C . n 
C 1 120 LYS 120 120 120 LYS LYS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASP 122 122 122 ASP ASP C . n 
C 1 123 CYS 123 123 123 CYS CYS C . n 
C 1 124 ILE 124 124 124 ILE ILE C . n 
C 1 125 ILE 125 125 125 ILE ILE C . n 
C 1 126 THR 126 126 126 THR THR C . n 
C 1 127 TYR 127 127 127 TYR TYR C . n 
C 1 128 LEU 128 128 128 LEU LEU C . n 
C 1 129 VAL 129 129 129 VAL VAL C . n 
C 1 130 ILE 130 130 130 ILE ILE C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 PRO 133 133 133 PRO PRO C . n 
C 1 134 GLN 134 134 134 GLN GLN C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 ASP 136 136 136 ASP ASP C . n 
C 1 137 HIS 137 137 137 HIS HIS C . n 
C 1 138 ILE 138 138 138 ILE ILE C . n 
C 1 139 HIS 139 139 139 HIS HIS C . n 
C 1 140 SER 140 140 140 SER SER C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 THR 142 142 142 THR THR C . n 
C 1 143 GLY 143 143 143 GLY GLY C . n 
C 1 144 LYS 144 144 144 LYS LYS C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 PHE 146 146 146 PHE PHE C . n 
C 1 147 VAL 147 147 147 VAL VAL C . n 
C 1 148 ASP 148 148 148 ASP ASP C . n 
C 1 149 LEU 149 149 149 LEU LEU C . n 
C 1 150 MET 150 150 150 MET MET C . n 
C 1 151 ASN 151 151 151 ASN ASN C . n 
C 1 152 THR 152 152 152 THR THR C . n 
C 1 153 LEU 153 153 153 LEU LEU C . n 
C 1 154 ILE 154 154 154 ILE ILE C . n 
C 1 155 ASN 155 155 155 ASN ASN C . n 
C 1 156 ILE 156 156 156 ILE ILE C . n 
C 1 157 ILE 157 157 157 ILE ILE C . n 
C 1 158 HIS 158 158 158 HIS HIS C . n 
C 1 159 LYS 159 159 159 LYS LYS C . n 
C 1 160 GLY 160 160 160 GLY GLY C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 PRO 162 162 162 PRO PRO C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 ILE 164 164 164 ILE ILE C . n 
C 1 165 PRO 165 165 165 PRO PRO C . n 
C 1 166 VAL 166 166 166 VAL VAL C . n 
C 1 167 THR 167 167 167 THR THR C . n 
C 1 168 LEU 168 168 168 LEU LEU C . n 
C 1 169 SER 169 169 169 SER SER C . n 
C 1 170 ALA 170 170 170 ALA ALA C . n 
C 1 171 ASN 171 171 171 ASN ASN C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 MET 173 173 173 MET MET C . n 
C 1 174 ILE 174 174 174 ILE ILE C . n 
C 1 175 SER 175 175 175 SER SER C . n 
C 1 176 ASP 176 176 176 ASP ASP C . n 
C 1 177 TYR 177 177 177 TYR TYR C . n 
C 1 178 MET 178 178 178 MET MET C . n 
C 1 179 ASP 179 179 179 ASP ASP C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 SER 181 181 181 SER SER C . n 
C 1 182 ILE 182 182 182 ILE ILE C . n 
C 1 183 PHE 183 183 183 PHE PHE C . n 
C 1 184 ASP 184 184 184 ASP ASP C . n 
C 1 185 VAL 185 185 185 VAL VAL C . n 
C 1 186 TYR 186 186 186 TYR TYR C . n 
C 1 187 ALA 187 187 187 ALA ALA C . n 
C 1 188 TYR 188 188 188 TYR TYR C . n 
C 1 189 ASN 189 189 189 ASN ASN C . n 
C 1 190 CYS 190 190 190 CYS CYS C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ASP 192 192 192 ASP ASP C . n 
C 1 193 HIS 193 193 193 HIS HIS C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 GLU 195 195 195 GLU GLU C . n 
C 1 196 GLY 196 196 196 GLY GLY C . n 
C 1 197 GLN 197 197 197 GLN GLN C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 ALA 199 199 199 ALA ALA C . n 
C 1 200 THR 200 200 200 THR THR C . n 
C 1 201 MET 201 201 201 MET MET C . n 
C 1 202 GLY 202 202 202 GLY GLY C . n 
C 1 203 PHE 203 203 203 PHE PHE C . n 
C 1 204 LYS 204 204 204 LYS LYS C . n 
C 1 205 ASP 205 205 205 ASP ASP C . n 
C 1 206 TYR 206 206 206 TYR TYR C . n 
C 1 207 ILE 207 207 207 ILE ILE C . n 
C 1 208 LYS 208 208 208 LYS LYS C . n 
C 1 209 GLY 209 209 209 GLY GLY C . n 
C 1 210 LEU 210 210 210 LEU LEU C . n 
C 1 211 ASN 211 211 211 ASN ASN C . n 
C 1 212 GLU 212 212 212 GLU GLU C . n 
C 1 213 LEU 213 213 213 LEU LEU C . n 
C 1 214 ASN 214 214 214 ASN ASN C . n 
C 1 215 GLY 215 215 215 GLY GLY C . n 
C 1 216 LEU 216 216 216 LEU LEU C . n 
C 1 217 ASP 217 217 217 ASP ASP C . n 
C 1 218 LYS 218 218 218 LYS LYS C . n 
C 1 219 PRO 219 219 219 PRO PRO C . n 
C 1 220 PHE 220 220 220 PHE PHE C . n 
C 1 221 ILE 221 221 221 ILE ILE C . n 
C 1 222 THR 222 222 222 THR THR C . n 
C 1 223 THR 223 223 223 THR THR C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 PHE 225 225 225 PHE PHE C . n 
C 1 226 GLY 226 226 226 GLY GLY C . n 
C 1 227 TYR 227 227 227 TYR TYR C . n 
C 1 228 SER 228 228 228 SER SER C . n 
C 1 229 VAL 229 229 229 VAL VAL C . n 
C 1 230 SER 230 230 230 SER SER C . n 
C 1 231 PRO 231 231 231 PRO PRO C . n 
C 1 232 GLU 232 232 232 GLU GLU C . n 
C 1 233 GLY 233 233 233 GLY GLY C . n 
C 1 234 GLY 234 234 234 GLY GLY C . n 
C 1 235 ASN 235 235 235 ASN ASN C . n 
C 1 236 GLY 236 236 236 GLY GLY C . n 
C 1 237 GLN 237 237 237 GLN GLN C . n 
C 1 238 TYR 238 238 238 TYR TYR C . n 
C 1 239 GLY 239 239 239 GLY GLY C . n 
C 1 240 SER 240 240 240 SER SER C . n 
C 1 241 ASN 241 241 241 ASN ASN C . n 
C 1 242 THR 242 242 242 THR THR C . n 
C 1 243 LEU 243 243 243 LEU LEU C . n 
C 1 244 LYS 244 244 244 LYS LYS C . n 
C 1 245 GLN 245 245 245 GLN GLN C . n 
C 1 246 GLN 246 246 246 GLN GLN C . n 
C 1 247 SER 247 247 247 SER SER C . n 
C 1 248 ASP 248 248 248 ASP ASP C . n 
C 1 249 GLY 249 249 249 GLY GLY C . n 
C 1 250 LEU 250 250 250 LEU LEU C . n 
C 1 251 ILE 251 251 251 ILE ILE C . n 
C 1 252 SER 252 252 252 SER SER C . n 
C 1 253 ASN 253 253 253 ASN ASN C . n 
C 1 254 TYR 254 254 254 TYR TYR C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 ASP 256 256 256 ASP ASP C . n 
C 1 257 LEU 257 257 257 LEU LEU C . n 
C 1 258 ILE 258 258 258 ILE ILE C . n 
C 1 259 ASP 259 259 259 ASP ASP C . n 
C 1 260 ALA 260 260 260 ALA ALA C . n 
C 1 261 GLY 261 261 261 GLY GLY C . n 
C 1 262 ALA 262 262 262 ALA ALA C . n 
C 1 263 VAL 263 263 263 VAL VAL C . n 
C 1 264 GLY 264 264 264 GLY GLY C . n 
C 1 265 MET 265 265 265 MET MET C . n 
C 1 266 CYS 266 266 266 CYS CYS C . n 
C 1 267 PRO 267 267 267 PRO PRO C . n 
C 1 268 PHE 268 268 268 PHE PHE C . n 
C 1 269 TYR 269 269 269 TYR TYR C . n 
C 1 270 TYR 270 270 270 TYR TYR C . n 
C 1 271 ALA 271 271 271 ALA ALA C . n 
C 1 272 ASP 272 272 272 ASP ASP C . n 
C 1 273 GLY 273 273 273 GLY GLY C . n 
C 1 274 TRP 274 274 274 TRP TRP C . n 
C 1 275 TRP 275 275 275 TRP TRP C . n 
C 1 276 LYS 276 276 276 LYS LYS C . n 
C 1 277 GLY 277 277 277 GLY GLY C . n 
C 1 278 GLY 278 278 278 GLY GLY C . n 
C 1 279 GLU 279 279 279 GLU GLU C . n 
C 1 280 LYS 280 280 280 LYS LYS C . n 
C 1 281 SER 281 281 281 SER SER C . n 
C 1 282 ASP 282 282 282 ASP ASP C . n 
C 1 283 HIS 283 283 283 HIS HIS C . n 
C 1 284 SER 284 284 284 SER SER C . n 
C 1 285 LEU 285 285 285 LEU LEU C . n 
C 1 286 ASN 286 286 286 ASN ASN C . n 
C 1 287 GLN 287 287 287 GLN GLN C . n 
C 1 288 PRO 288 288 288 PRO PRO C . n 
C 1 289 GLU 289 289 289 GLU GLU C . n 
C 1 290 GLU 290 290 290 GLU GLU C . n 
C 1 291 TRP 291 291 291 TRP TRP C . n 
C 1 292 PHE 292 292 292 PHE PHE C . n 
C 1 293 GLY 293 293 293 GLY GLY C . n 
C 1 294 PHE 294 294 294 PHE PHE C . n 
C 1 295 TRP 295 295 295 TRP TRP C . n 
C 1 296 GLY 296 296 296 GLY GLY C . n 
C 1 297 TYR 297 297 297 TYR TYR C . n 
C 1 298 SER 298 298 298 SER SER C . n 
C 1 299 ASP 299 299 299 ASP ASP C . n 
C 1 300 LEU 300 300 300 LEU LEU C . n 
C 1 301 ASN 301 301 301 ASN ASN C . n 
C 1 302 ASP 302 302 302 ASP ASP C . n 
C 1 303 LYS 303 303 303 LYS LYS C . n 
C 1 304 TYR 304 304 304 TYR TYR C . n 
C 1 305 GLY 305 305 305 GLY GLY C . n 
C 1 306 THR 306 306 306 THR THR C . n 
C 1 307 PRO 307 307 307 PRO PRO C . n 
C 1 308 ARG 308 308 308 ARG ARG C . n 
C 1 309 PRO 309 309 309 PRO PRO C . n 
C 1 310 VAL 310 310 310 VAL VAL C . n 
C 1 311 TRP 311 311 311 TRP TRP C . n 
C 1 312 PHE 312 312 312 PHE PHE C . n 
C 1 313 ALA 313 313 313 ALA ALA C . n 
C 1 314 MET 314 314 314 MET MET C . n 
C 1 315 ARG 315 315 315 ARG ARG C . n 
C 1 316 ASP 316 316 316 ASP ASP C . n 
C 1 317 TYR 317 317 317 TYR TYR C . n 
C 1 318 MET 318 318 318 MET MET C . n 
C 1 319 LYS 319 319 319 LYS LYS C . n 
C 1 320 GLY 320 320 320 GLY GLY C . n 
C 1 321 LEU 321 321 321 LEU LEU C . n 
C 1 322 ILE 322 322 322 ILE ILE C . n 
C 1 323 ILE 323 323 323 ILE ILE C . n 
C 1 324 SER 324 324 324 SER SER C . n 
C 1 325 PRO 325 325 325 PRO PRO C . n 
C 1 326 LYS 326 326 326 LYS LYS C . n 
C 1 327 ASN 327 327 327 ASN ASN C . n 
C 1 328 LYS 328 328 328 LYS LYS C . n 
C 1 329 SER 329 329 329 SER SER C . n 
C 1 330 ILE 330 330 330 ILE ILE C . n 
C 1 331 HIS 331 331 331 HIS HIS C . n 
C 1 332 THR 332 332 332 THR THR C . n 
C 1 333 ASN 333 333 333 ASN ASN C . n 
C 1 334 THR 334 334 334 THR THR C . n 
C 1 335 LYS 335 335 335 LYS LYS C . n 
C 1 336 ILE 336 336 336 ILE ILE C . n 
C 1 337 PRO 337 337 337 PRO PRO C . n 
C 1 338 LEU 338 338 338 LEU LEU C . n 
C 1 339 GLU 339 339 339 GLU GLU C . n 
C 1 340 LEU 340 340 340 LEU LEU C . n 
C 1 341 TYR 341 341 341 TYR TYR C . n 
C 1 342 ASN 342 342 342 ASN ASN C . n 
C 1 343 ASP 343 343 343 ASP ASP C . n 
C 1 344 LYS 344 344 344 LYS LYS C . n 
C 1 345 ASP 345 345 345 ASP ASP C . n 
C 1 346 VAL 346 346 346 VAL VAL C . n 
C 1 347 LYS 347 347 347 LYS LYS C . n 
C 1 348 LYS 348 348 348 LYS LYS C . n 
C 1 349 VAL 349 349 349 VAL VAL C . n 
C 1 350 VAL 350 350 350 VAL VAL C . n 
C 1 351 VAL 351 351 351 VAL VAL C . n 
C 1 352 LYS 352 352 352 LYS LYS C . n 
C 1 353 PHE 353 353 353 PHE PHE C . n 
C 1 354 ARG 354 354 354 ARG ARG C . n 
C 1 355 ASP 355 355 355 ASP ASP C . n 
C 1 356 LYS 356 356 356 LYS LYS C . n 
C 1 357 VAL 357 357 357 VAL VAL C . n 
C 1 358 ILE 358 358 358 ILE ILE C . n 
C 1 359 TYR 359 359 359 TYR TYR C . n 
C 1 360 SER 360 360 360 SER SER C . n 
C 1 361 LYS 361 361 361 LYS LYS C . n 
C 1 362 ASN 362 362 362 ASN ASN C . n 
C 1 363 ILE 363 363 363 ILE ILE C . n 
C 1 364 THR 364 364 364 THR THR C . n 
C 1 365 SER 365 365 365 SER SER C . n 
C 1 366 GLU 366 366 366 GLU GLU C . n 
C 1 367 GLY 367 367 367 GLY GLY C . n 
C 1 368 TYR 368 368 368 TYR TYR C . n 
C 1 369 MET 369 369 369 MET MET C . n 
C 1 370 ALA 370 370 370 ALA ALA C . n 
C 1 371 ASP 371 371 371 ASP ASP C . n 
C 1 372 GLU 372 372 372 GLU GLU C . n 
C 1 373 LEU 373 373 373 LEU LEU C . n 
C 1 374 THR 374 374 374 THR THR C . n 
C 1 375 ILE 375 375 375 ILE ILE C . n 
C 1 376 ASP 376 376 376 ASP ASP C . n 
C 1 377 PRO 377 377 377 PRO PRO C . n 
C 1 378 VAL 378 378 378 VAL VAL C . n 
C 1 379 GLY 379 379 379 GLY GLY C . n 
C 1 380 ILE 380 380 380 ILE ILE C . n 
C 1 381 GLU 381 381 381 GLU GLU C . n 
C 1 382 ASP 382 382 382 ASP ASP C . n 
C 1 383 MET 383 383 383 MET MET C . n 
C 1 384 GLU 384 384 384 GLU GLU C . n 
C 1 385 LEU 385 385 385 LEU LEU C . n 
C 1 386 ALA 386 386 386 ALA ALA C . n 
C 1 387 PHE 387 387 387 PHE PHE C . n 
C 1 388 GLU 388 388 388 GLU GLU C . n 
C 1 389 PHE 389 389 389 PHE PHE C . n 
C 1 390 TYR 390 390 390 TYR TYR C . n 
C 1 391 ASP 391 391 391 ASP ASP C . n 
C 1 392 SER 392 392 392 SER SER C . n 
C 1 393 ASP 393 393 393 ASP ASP C . n 
C 1 394 ASN 394 394 394 ASN ASN C . n 
C 1 395 LYS 395 395 395 LYS LYS C . n 
C 1 396 ILE 396 396 396 ILE ILE C . n 
C 1 397 ILE 397 397 397 ILE ILE C . n 
C 1 398 LYS 398 398 398 LYS LYS C . n 
C 1 399 ASN 399 399 399 ASN ASN C . n 
C 1 400 GLU 400 400 400 GLU GLU C . n 
C 1 401 SER 401 401 401 SER SER C . n 
C 1 402 ILE 402 402 402 ILE ILE C . n 
C 1 403 ASN 403 403 403 ASN ASN C . n 
C 1 404 ILE 404 404 404 ILE ILE C . n 
C 1 405 LEU 405 405 405 LEU LEU C . n 
C 1 406 ALA 406 406 406 ALA ALA C . n 
C 1 407 SER 407 407 407 SER SER C . n 
C 1 408 LYS 408 408 408 LYS LYS C . n 
C 1 409 THR 409 409 409 THR THR C . n 
C 1 410 ALA 410 410 410 ALA ALA C . n 
C 1 411 PHE 411 411 411 PHE PHE C . n 
C 1 412 GLU 412 412 412 GLU GLU C . n 
C 1 413 LEU 413 413 413 LEU LEU C . n 
C 1 414 PRO 414 414 414 PRO PRO C . n 
C 1 415 GLU 415 415 415 GLU GLU C . n 
C 1 416 LEU 416 416 416 LEU LEU C . n 
C 1 417 THR 417 417 417 THR THR C . n 
C 1 418 ILE 418 418 418 ILE ILE C . n 
C 1 419 GLU 419 419 419 GLU GLU C . n 
C 1 420 VAL 420 420 420 VAL VAL C . n 
C 1 421 THR 421 421 421 THR THR C . n 
C 1 422 PRO 422 422 422 PRO PRO C . n 
C 1 423 GLU 423 423 423 GLU GLU C . n 
C 1 424 LYS 424 424 424 LYS LYS C . n 
C 1 425 ASP 425 425 425 ASP ASP C . n 
C 1 426 LEU 426 426 426 LEU LEU C . n 
C 1 427 ASN 427 427 427 ASN ASN C . n 
C 1 428 GLU 428 428 428 GLU GLU C . n 
C 1 429 GLY 429 429 429 GLY GLY C . n 
C 1 430 LYS 430 430 430 LYS LYS C . n 
C 1 431 ILE 431 431 431 ILE ILE C . n 
C 1 432 ALA 432 432 432 ALA ALA C . n 
C 1 433 SER 433 433 433 SER SER C . n 
C 1 434 ILE 434 434 434 ILE ILE C . n 
C 1 435 LYS 435 435 435 LYS LYS C . n 
C 1 436 THR 436 436 436 THR THR C . n 
C 1 437 LYS 437 437 437 LYS LYS C . n 
C 1 438 ILE 438 438 438 ILE ILE C . n 
C 1 439 GLU 439 439 439 GLU GLU C . n 
C 1 440 THR 440 440 440 THR THR C . n 
C 1 441 SER 441 441 441 SER SER C . n 
C 1 442 GLU 442 442 442 GLU GLU C . n 
C 1 443 ASN 443 443 443 ASN ASN C . n 
C 1 444 PHE 444 444 444 PHE PHE C . n 
C 1 445 THR 445 445 445 THR THR C . n 
C 1 446 LEU 446 446 446 LEU LEU C . n 
C 1 447 LEU 447 447 447 LEU LEU C . n 
C 1 448 ASP 448 448 448 ASP ASP C . n 
C 1 449 ASP 449 449 449 ASP ASP C . n 
C 1 450 LEU 450 450 450 LEU LEU C . n 
C 1 451 LYS 451 451 451 LYS LYS C . n 
C 1 452 ILE 452 452 452 ILE ILE C . n 
C 1 453 SER 453 453 453 SER SER C . n 
C 1 454 TYR 454 454 454 TYR TYR C . n 
C 1 455 ASN 455 455 455 ASN ASN C . n 
C 1 456 THR 456 456 456 THR THR C . n 
C 1 457 HIS 457 457 457 HIS HIS C . n 
C 1 458 LEU 458 458 458 LEU LEU C . n 
C 1 459 GLY 459 459 459 GLY GLY C . n 
C 1 460 TRP 460 460 460 TRP TRP C . n 
C 1 461 ALA 461 461 461 ALA ALA C . n 
C 1 462 ILE 462 462 462 ILE ILE C . n 
C 1 463 GLY 463 463 463 GLY GLY C . n 
C 1 464 SER 464 464 464 SER SER C . n 
C 1 465 GLN 465 465 465 GLN GLN C . n 
C 1 466 ALA 466 466 466 ALA ALA C . n 
C 1 467 SER 467 467 467 SER SER C . n 
C 1 468 VAL 468 468 468 VAL VAL C . n 
C 1 469 SER 469 469 469 SER SER C . n 
C 1 470 ILE 470 470 470 ILE ILE C . n 
C 1 471 SER 471 471 471 SER SER C . n 
C 1 472 ASP 472 472 472 ASP ASP C . n 
C 1 473 GLN 473 473 473 GLN GLN C . n 
C 1 474 LEU 474 474 474 LEU LEU C . n 
C 1 475 ASP 475 475 475 ASP ASP C . n 
C 1 476 LYS 476 476 476 LYS LYS C . n 
C 1 477 LYS 477 477 477 LYS LYS C . n 
C 1 478 ILE 478 478 478 ILE ILE C . n 
C 1 479 ILE 479 479 479 ILE ILE C . n 
C 1 480 THR 480 480 480 THR THR C . n 
C 1 481 SER 481 481 481 SER SER C . n 
C 1 482 GLU 482 482 482 GLU GLU C . n 
C 1 483 ASN 483 483 483 ASN ASN C . n 
C 1 484 PHE 484 484 484 PHE PHE C . n 
C 1 485 PHE 485 485 485 PHE PHE C . n 
C 1 486 ASN 486 486 486 ASN ASN C . n 
C 1 487 ILE 487 487 487 ILE ILE C . n 
C 1 488 PRO 488 488 488 PRO PRO C . n 
C 1 489 ASP 489 489 489 ASP ASP C . n 
C 1 490 ASN 490 490 490 ASN ASN C . n 
C 1 491 CYS 491 491 491 CYS CYS C . n 
C 1 492 TRP 492 492 492 TRP TRP C . n 
C 1 493 VAL 493 493 493 VAL VAL C . n 
C 1 494 VAL 494 494 494 VAL VAL C . n 
C 1 495 ASN 495 495 495 ASN ASN C . n 
C 1 496 ALA 496 496 496 ALA ALA C . n 
C 1 497 SER 497 497 497 SER SER C . n 
C 1 498 ALA 498 498 498 ALA ALA C . n 
C 1 499 GLY 499 499 499 GLY GLY C . n 
C 1 500 ILE 500 500 500 ILE ILE C . n 
C 1 501 SER 501 501 501 SER SER C . n 
C 1 502 VAL 502 502 502 VAL VAL C . n 
C 1 503 ARG 503 503 503 ARG ARG C . n 
C 1 504 TYR 504 504 504 TYR TYR C . n 
C 1 505 GLY 505 505 505 GLY GLY C . n 
C 1 506 LYS 506 506 506 LYS LYS C . n 
C 1 507 PHE 507 507 507 PHE PHE C . n 
C 1 508 THR 508 508 508 THR THR C . n 
C 1 509 PHE 509 509 509 PHE PHE C . n 
C 1 510 LYS 510 510 510 LYS LYS C . n 
C 1 511 ILE 511 511 511 ILE ILE C . n 
C 1 512 HIS 512 512 512 HIS HIS C . n 
C 1 513 ASP 513 513 513 ASP ASP C . n 
C 1 514 GLN 514 514 514 GLN GLN C . n 
C 1 515 LYS 515 515 515 LYS LYS C . n 
C 1 516 ILE 516 516 516 ILE ILE C . n 
C 1 517 ILE 517 517 517 ILE ILE C . n 
C 1 518 TYR 518 518 518 TYR TYR C . n 
C 1 519 ARG 519 519 519 ARG ARG C . n 
C 1 520 GLY 520 520 520 GLY GLY C . n 
C 1 521 ASP 521 521 521 ASP ASP C . n 
C 1 522 TRP 522 522 522 TRP TRP C . n 
C 1 523 ALA 523 523 523 ALA ALA C . n 
C 1 524 LYS 524 524 524 LYS LYS C . n 
C 1 525 GLU 525 525 525 GLU GLU C . n 
C 1 526 VAL 526 526 526 VAL VAL C . n 
C 1 527 GLY 527 527 527 GLY GLY C . n 
C 1 528 ARG 528 528 528 ARG ARG C . n 
C 1 529 LYS 529 529 529 LYS LYS C . n 
C 1 530 LEU 530 530 ?   ?   ?   C . n 
C 1 531 GLU 531 531 ?   ?   ?   C . n 
C 1 532 HIS 532 532 ?   ?   ?   C . n 
C 1 533 HIS 533 533 ?   ?   ?   C . n 
C 1 534 HIS 534 534 ?   ?   ?   C . n 
C 1 535 HIS 535 535 ?   ?   ?   C . n 
C 1 536 HIS 536 536 ?   ?   ?   C . n 
C 1 537 HIS 537 537 ?   ?   ?   C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   GLN 2   2   ?   ?   ?   D . n 
D 1 3   SER 3   3   3   SER SER D . n 
D 1 4   LYS 4   4   4   LYS LYS D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   LYS 6   6   6   LYS LYS D . n 
D 1 7   ILE 7   7   7   ILE ILE D . n 
D 1 8   GLU 8   8   8   GLU GLU D . n 
D 1 9   LEU 9   9   9   LEU LEU D . n 
D 1 10  LYS 10  10  10  LYS LYS D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  ASN 12  12  12  ASN ASN D . n 
D 1 13  TRP 13  13  13  TRP TRP D . n 
D 1 14  TYR 14  14  14  TYR TYR D . n 
D 1 15  HIS 15  15  15  HIS HIS D . n 
D 1 16  LEU 16  16  16  LEU LEU D . n 
D 1 17  ASP 17  17  17  ASP ASP D . n 
D 1 18  GLY 18  18  18  GLY GLY D . n 
D 1 19  GLU 19  19  19  GLU GLU D . n 
D 1 20  LYS 20  20  20  LYS LYS D . n 
D 1 21  TYR 21  21  21  TYR TYR D . n 
D 1 22  PHE 22  22  22  PHE PHE D . n 
D 1 23  ILE 23  23  23  ILE ILE D . n 
D 1 24  LYS 24  24  24  LYS LYS D . n 
D 1 25  ALA 25  25  25  ALA ALA D . n 
D 1 26  ILE 26  26  26  ILE ILE D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  TYR 28  28  28  TYR TYR D . n 
D 1 29  GLU 29  29  29  GLU GLU D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  GLY 31  31  31  GLY GLY D . n 
D 1 32  ALA 32  32  32  ALA ALA D . n 
D 1 33  ARG 33  33  33  ARG ARG D . n 
D 1 34  PRO 34  34  34  PRO PRO D . n 
D 1 35  GLY 35  35  35  GLY GLY D . n 
D 1 36  GLN 36  36  36  GLN GLN D . n 
D 1 37  ALA 37  37  37  ALA ALA D . n 
D 1 38  PRO 38  38  38  PRO PRO D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  ASP 41  41  41  ASP ASP D . n 
D 1 42  GLU 42  42  42  GLU GLU D . n 
D 1 43  ARG 43  43  43  ARG ARG D . n 
D 1 44  LYS 44  44  44  LYS LYS D . n 
D 1 45  ASP 45  45  45  ASP ASP D . n 
D 1 46  GLU 46  46  46  GLU GLU D . n 
D 1 47  LEU 47  47  47  LEU LEU D . n 
D 1 48  GLU 48  48  48  GLU GLU D . n 
D 1 49  LEU 49  49  49  LEU LEU D . n 
D 1 50  MET 50  50  50  MET MET D . n 
D 1 51  LYS 51  51  51  LYS LYS D . n 
D 1 52  PHE 52  52  52  PHE PHE D . n 
D 1 53  ASP 53  53  53  ASP ASP D . n 
D 1 54  LEU 54  54  54  LEU LEU D . n 
D 1 55  GLU 55  55  55  GLU GLU D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  ILE 57  57  57  ILE ILE D . n 
D 1 58  LYS 58  58  58  LYS LYS D . n 
D 1 59  GLU 59  59  59  GLU GLU D . n 
D 1 60  GLY 60  60  60  GLY GLY D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  TYR 62  62  62  TYR TYR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  THR 64  64  64  THR THR D . n 
D 1 65  ILE 65  65  65  ILE ILE D . n 
D 1 66  ARG 66  66  66  ARG ARG D . n 
D 1 67  THR 67  67  67  THR THR D . n 
D 1 68  TRP 68  68  68  TRP TRP D . n 
D 1 69  SER 69  69  69  SER SER D . n 
D 1 70  GLN 70  70  70  GLN GLN D . n 
D 1 71  TYR 71  71  71  TYR TYR D . n 
D 1 72  SER 72  72  72  SER SER D . n 
D 1 73  GLU 73  73  73  GLU GLU D . n 
D 1 74  ASN 74  74  74  ASN ASN D . n 
D 1 75  GLN 75  75  75  GLN GLN D . n 
D 1 76  LEU 76  76  76  LEU LEU D . n 
D 1 77  LYS 77  77  77  LYS LYS D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  VAL 79  79  79  VAL VAL D . n 
D 1 80  GLN 80  80  80  GLN GLN D . n 
D 1 81  GLU 81  81  81  GLU GLU D . n 
D 1 82  SER 82  82  82  SER SER D . n 
D 1 83  GLY 83  83  83  GLY GLY D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  LYS 85  85  85  LYS LYS D . n 
D 1 86  LEU 86  86  86  LEU LEU D . n 
D 1 87  ILE 87  87  87  ILE ILE D . n 
D 1 88  MET 88  88  88  MET MET D . n 
D 1 89  GLY 89  89  89  GLY GLY D . n 
D 1 90  ILE 90  90  90  ILE ILE D . n 
D 1 91  ASP 91  91  91  ASP ASP D . n 
D 1 92  ILE 92  92  92  ILE ILE D . n 
D 1 93  LYS 93  93  93  LYS LYS D . n 
D 1 94  PRO 94  94  94  PRO PRO D . n 
D 1 95  GLU 95  95  95  GLU GLU D . n 
D 1 96  GLU 96  96  96  GLU GLU D . n 
D 1 97  ASP 97  97  97  ASP ASP D . n 
D 1 98  TYR 98  98  98  TYR TYR D . n 
D 1 99  GLY 99  99  99  GLY GLY D . n 
D 1 100 ASP 100 100 100 ASP ASP D . n 
D 1 101 PRO 101 101 101 PRO PRO D . n 
D 1 102 GLU 102 102 102 GLU GLU D . n 
D 1 103 PHE 103 103 103 PHE PHE D . n 
D 1 104 VAL 104 104 104 VAL VAL D . n 
D 1 105 LYS 105 105 105 LYS LYS D . n 
D 1 106 ASP 106 106 106 ASP ASP D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLU 108 108 108 GLU GLU D . n 
D 1 109 ILE 109 109 109 ILE ILE D . n 
D 1 110 GLU 110 110 110 GLU GLU D . n 
D 1 111 LEU 111 111 111 LEU LEU D . n 
D 1 112 LYS 112 112 112 LYS LYS D . n 
D 1 113 ARG 113 113 113 ARG ARG D . n 
D 1 114 VAL 114 114 114 VAL VAL D . n 
D 1 115 LEU 115 115 115 LEU LEU D . n 
D 1 116 ASN 116 116 116 ASN ASN D . n 
D 1 117 TYR 117 117 117 TYR TYR D . n 
D 1 118 ALA 118 118 118 ALA ALA D . n 
D 1 119 LYS 119 119 119 LYS LYS D . n 
D 1 120 LYS 120 120 120 LYS LYS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASP 122 122 122 ASP ASP D . n 
D 1 123 CYS 123 123 123 CYS CYS D . n 
D 1 124 ILE 124 124 124 ILE ILE D . n 
D 1 125 ILE 125 125 125 ILE ILE D . n 
D 1 126 THR 126 126 126 THR THR D . n 
D 1 127 TYR 127 127 127 TYR TYR D . n 
D 1 128 LEU 128 128 128 LEU LEU D . n 
D 1 129 VAL 129 129 129 VAL VAL D . n 
D 1 130 ILE 130 130 130 ILE ILE D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 PRO 133 133 133 PRO PRO D . n 
D 1 134 GLN 134 134 134 GLN GLN D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 ASP 136 136 136 ASP ASP D . n 
D 1 137 HIS 137 137 137 HIS HIS D . n 
D 1 138 ILE 138 138 138 ILE ILE D . n 
D 1 139 HIS 139 139 139 HIS HIS D . n 
D 1 140 SER 140 140 140 SER SER D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 THR 142 142 142 THR THR D . n 
D 1 143 GLY 143 143 143 GLY GLY D . n 
D 1 144 LYS 144 144 144 LYS LYS D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 PHE 146 146 146 PHE PHE D . n 
D 1 147 VAL 147 147 147 VAL VAL D . n 
D 1 148 ASP 148 148 148 ASP ASP D . n 
D 1 149 LEU 149 149 149 LEU LEU D . n 
D 1 150 MET 150 150 150 MET MET D . n 
D 1 151 ASN 151 151 151 ASN ASN D . n 
D 1 152 THR 152 152 152 THR THR D . n 
D 1 153 LEU 153 153 153 LEU LEU D . n 
D 1 154 ILE 154 154 154 ILE ILE D . n 
D 1 155 ASN 155 155 155 ASN ASN D . n 
D 1 156 ILE 156 156 156 ILE ILE D . n 
D 1 157 ILE 157 157 157 ILE ILE D . n 
D 1 158 HIS 158 158 158 HIS HIS D . n 
D 1 159 LYS 159 159 159 LYS LYS D . n 
D 1 160 GLY 160 160 160 GLY GLY D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 PRO 162 162 162 PRO PRO D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 ILE 164 164 164 ILE ILE D . n 
D 1 165 PRO 165 165 165 PRO PRO D . n 
D 1 166 VAL 166 166 166 VAL VAL D . n 
D 1 167 THR 167 167 167 THR THR D . n 
D 1 168 LEU 168 168 168 LEU LEU D . n 
D 1 169 SER 169 169 169 SER SER D . n 
D 1 170 ALA 170 170 170 ALA ALA D . n 
D 1 171 ASN 171 171 171 ASN ASN D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 MET 173 173 173 MET MET D . n 
D 1 174 ILE 174 174 174 ILE ILE D . n 
D 1 175 SER 175 175 175 SER SER D . n 
D 1 176 ASP 176 176 176 ASP ASP D . n 
D 1 177 TYR 177 177 177 TYR TYR D . n 
D 1 178 MET 178 178 178 MET MET D . n 
D 1 179 ASP 179 179 179 ASP ASP D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 SER 181 181 181 SER SER D . n 
D 1 182 ILE 182 182 182 ILE ILE D . n 
D 1 183 PHE 183 183 183 PHE PHE D . n 
D 1 184 ASP 184 184 184 ASP ASP D . n 
D 1 185 VAL 185 185 185 VAL VAL D . n 
D 1 186 TYR 186 186 186 TYR TYR D . n 
D 1 187 ALA 187 187 187 ALA ALA D . n 
D 1 188 TYR 188 188 188 TYR TYR D . n 
D 1 189 ASN 189 189 189 ASN ASN D . n 
D 1 190 CYS 190 190 190 CYS CYS D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ASP 192 192 192 ASP ASP D . n 
D 1 193 HIS 193 193 193 HIS HIS D . n 
D 1 194 ASN 194 194 194 ASN ASN D . n 
D 1 195 GLU 195 195 195 GLU GLU D . n 
D 1 196 GLY 196 196 196 GLY GLY D . n 
D 1 197 GLN 197 197 197 GLN GLN D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 ALA 199 199 199 ALA ALA D . n 
D 1 200 THR 200 200 200 THR THR D . n 
D 1 201 MET 201 201 201 MET MET D . n 
D 1 202 GLY 202 202 202 GLY GLY D . n 
D 1 203 PHE 203 203 203 PHE PHE D . n 
D 1 204 LYS 204 204 204 LYS LYS D . n 
D 1 205 ASP 205 205 205 ASP ASP D . n 
D 1 206 TYR 206 206 206 TYR TYR D . n 
D 1 207 ILE 207 207 207 ILE ILE D . n 
D 1 208 LYS 208 208 208 LYS LYS D . n 
D 1 209 GLY 209 209 209 GLY GLY D . n 
D 1 210 LEU 210 210 210 LEU LEU D . n 
D 1 211 ASN 211 211 211 ASN ASN D . n 
D 1 212 GLU 212 212 212 GLU GLU D . n 
D 1 213 LEU 213 213 213 LEU LEU D . n 
D 1 214 ASN 214 214 214 ASN ASN D . n 
D 1 215 GLY 215 215 215 GLY GLY D . n 
D 1 216 LEU 216 216 216 LEU LEU D . n 
D 1 217 ASP 217 217 217 ASP ASP D . n 
D 1 218 LYS 218 218 218 LYS LYS D . n 
D 1 219 PRO 219 219 219 PRO PRO D . n 
D 1 220 PHE 220 220 220 PHE PHE D . n 
D 1 221 ILE 221 221 221 ILE ILE D . n 
D 1 222 THR 222 222 222 THR THR D . n 
D 1 223 THR 223 223 223 THR THR D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 PHE 225 225 225 PHE PHE D . n 
D 1 226 GLY 226 226 226 GLY GLY D . n 
D 1 227 TYR 227 227 227 TYR TYR D . n 
D 1 228 SER 228 228 228 SER SER D . n 
D 1 229 VAL 229 229 229 VAL VAL D . n 
D 1 230 SER 230 230 230 SER SER D . n 
D 1 231 PRO 231 231 231 PRO PRO D . n 
D 1 232 GLU 232 232 232 GLU GLU D . n 
D 1 233 GLY 233 233 233 GLY GLY D . n 
D 1 234 GLY 234 234 234 GLY GLY D . n 
D 1 235 ASN 235 235 235 ASN ASN D . n 
D 1 236 GLY 236 236 236 GLY GLY D . n 
D 1 237 GLN 237 237 237 GLN GLN D . n 
D 1 238 TYR 238 238 238 TYR TYR D . n 
D 1 239 GLY 239 239 239 GLY GLY D . n 
D 1 240 SER 240 240 240 SER SER D . n 
D 1 241 ASN 241 241 241 ASN ASN D . n 
D 1 242 THR 242 242 242 THR THR D . n 
D 1 243 LEU 243 243 243 LEU LEU D . n 
D 1 244 LYS 244 244 244 LYS LYS D . n 
D 1 245 GLN 245 245 245 GLN GLN D . n 
D 1 246 GLN 246 246 246 GLN GLN D . n 
D 1 247 SER 247 247 247 SER SER D . n 
D 1 248 ASP 248 248 248 ASP ASP D . n 
D 1 249 GLY 249 249 249 GLY GLY D . n 
D 1 250 LEU 250 250 250 LEU LEU D . n 
D 1 251 ILE 251 251 251 ILE ILE D . n 
D 1 252 SER 252 252 252 SER SER D . n 
D 1 253 ASN 253 253 253 ASN ASN D . n 
D 1 254 TYR 254 254 254 TYR TYR D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 ASP 256 256 256 ASP ASP D . n 
D 1 257 LEU 257 257 257 LEU LEU D . n 
D 1 258 ILE 258 258 258 ILE ILE D . n 
D 1 259 ASP 259 259 259 ASP ASP D . n 
D 1 260 ALA 260 260 260 ALA ALA D . n 
D 1 261 GLY 261 261 261 GLY GLY D . n 
D 1 262 ALA 262 262 262 ALA ALA D . n 
D 1 263 VAL 263 263 263 VAL VAL D . n 
D 1 264 GLY 264 264 264 GLY GLY D . n 
D 1 265 MET 265 265 265 MET MET D . n 
D 1 266 CYS 266 266 266 CYS CYS D . n 
D 1 267 PRO 267 267 267 PRO PRO D . n 
D 1 268 PHE 268 268 268 PHE PHE D . n 
D 1 269 TYR 269 269 269 TYR TYR D . n 
D 1 270 TYR 270 270 270 TYR TYR D . n 
D 1 271 ALA 271 271 271 ALA ALA D . n 
D 1 272 ASP 272 272 272 ASP ASP D . n 
D 1 273 GLY 273 273 273 GLY GLY D . n 
D 1 274 TRP 274 274 274 TRP TRP D . n 
D 1 275 TRP 275 275 275 TRP TRP D . n 
D 1 276 LYS 276 276 276 LYS LYS D . n 
D 1 277 GLY 277 277 277 GLY GLY D . n 
D 1 278 GLY 278 278 278 GLY GLY D . n 
D 1 279 GLU 279 279 279 GLU GLU D . n 
D 1 280 LYS 280 280 280 LYS LYS D . n 
D 1 281 SER 281 281 281 SER SER D . n 
D 1 282 ASP 282 282 282 ASP ASP D . n 
D 1 283 HIS 283 283 283 HIS HIS D . n 
D 1 284 SER 284 284 284 SER SER D . n 
D 1 285 LEU 285 285 285 LEU LEU D . n 
D 1 286 ASN 286 286 286 ASN ASN D . n 
D 1 287 GLN 287 287 287 GLN GLN D . n 
D 1 288 PRO 288 288 288 PRO PRO D . n 
D 1 289 GLU 289 289 289 GLU GLU D . n 
D 1 290 GLU 290 290 290 GLU GLU D . n 
D 1 291 TRP 291 291 291 TRP TRP D . n 
D 1 292 PHE 292 292 292 PHE PHE D . n 
D 1 293 GLY 293 293 293 GLY GLY D . n 
D 1 294 PHE 294 294 294 PHE PHE D . n 
D 1 295 TRP 295 295 295 TRP TRP D . n 
D 1 296 GLY 296 296 296 GLY GLY D . n 
D 1 297 TYR 297 297 297 TYR TYR D . n 
D 1 298 SER 298 298 298 SER SER D . n 
D 1 299 ASP 299 299 299 ASP ASP D . n 
D 1 300 LEU 300 300 300 LEU LEU D . n 
D 1 301 ASN 301 301 301 ASN ASN D . n 
D 1 302 ASP 302 302 302 ASP ASP D . n 
D 1 303 LYS 303 303 303 LYS LYS D . n 
D 1 304 TYR 304 304 304 TYR TYR D . n 
D 1 305 GLY 305 305 305 GLY GLY D . n 
D 1 306 THR 306 306 306 THR THR D . n 
D 1 307 PRO 307 307 307 PRO PRO D . n 
D 1 308 ARG 308 308 308 ARG ARG D . n 
D 1 309 PRO 309 309 309 PRO PRO D . n 
D 1 310 VAL 310 310 310 VAL VAL D . n 
D 1 311 TRP 311 311 311 TRP TRP D . n 
D 1 312 PHE 312 312 312 PHE PHE D . n 
D 1 313 ALA 313 313 313 ALA ALA D . n 
D 1 314 MET 314 314 314 MET MET D . n 
D 1 315 ARG 315 315 315 ARG ARG D . n 
D 1 316 ASP 316 316 316 ASP ASP D . n 
D 1 317 TYR 317 317 317 TYR TYR D . n 
D 1 318 MET 318 318 318 MET MET D . n 
D 1 319 LYS 319 319 319 LYS LYS D . n 
D 1 320 GLY 320 320 320 GLY GLY D . n 
D 1 321 LEU 321 321 321 LEU LEU D . n 
D 1 322 ILE 322 322 322 ILE ILE D . n 
D 1 323 ILE 323 323 323 ILE ILE D . n 
D 1 324 SER 324 324 324 SER SER D . n 
D 1 325 PRO 325 325 325 PRO PRO D . n 
D 1 326 LYS 326 326 326 LYS LYS D . n 
D 1 327 ASN 327 327 327 ASN ASN D . n 
D 1 328 LYS 328 328 328 LYS LYS D . n 
D 1 329 SER 329 329 329 SER SER D . n 
D 1 330 ILE 330 330 330 ILE ILE D . n 
D 1 331 HIS 331 331 331 HIS HIS D . n 
D 1 332 THR 332 332 332 THR THR D . n 
D 1 333 ASN 333 333 333 ASN ASN D . n 
D 1 334 THR 334 334 334 THR THR D . n 
D 1 335 LYS 335 335 335 LYS LYS D . n 
D 1 336 ILE 336 336 336 ILE ILE D . n 
D 1 337 PRO 337 337 337 PRO PRO D . n 
D 1 338 LEU 338 338 338 LEU LEU D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 LEU 340 340 340 LEU LEU D . n 
D 1 341 TYR 341 341 341 TYR TYR D . n 
D 1 342 ASN 342 342 342 ASN ASN D . n 
D 1 343 ASP 343 343 343 ASP ASP D . n 
D 1 344 LYS 344 344 344 LYS LYS D . n 
D 1 345 ASP 345 345 345 ASP ASP D . n 
D 1 346 VAL 346 346 346 VAL VAL D . n 
D 1 347 LYS 347 347 347 LYS LYS D . n 
D 1 348 LYS 348 348 348 LYS LYS D . n 
D 1 349 VAL 349 349 349 VAL VAL D . n 
D 1 350 VAL 350 350 350 VAL VAL D . n 
D 1 351 VAL 351 351 351 VAL VAL D . n 
D 1 352 LYS 352 352 352 LYS LYS D . n 
D 1 353 PHE 353 353 353 PHE PHE D . n 
D 1 354 ARG 354 354 354 ARG ARG D . n 
D 1 355 ASP 355 355 355 ASP ASP D . n 
D 1 356 LYS 356 356 356 LYS LYS D . n 
D 1 357 VAL 357 357 357 VAL VAL D . n 
D 1 358 ILE 358 358 358 ILE ILE D . n 
D 1 359 TYR 359 359 359 TYR TYR D . n 
D 1 360 SER 360 360 360 SER SER D . n 
D 1 361 LYS 361 361 361 LYS LYS D . n 
D 1 362 ASN 362 362 362 ASN ASN D . n 
D 1 363 ILE 363 363 363 ILE ILE D . n 
D 1 364 THR 364 364 364 THR THR D . n 
D 1 365 SER 365 365 365 SER SER D . n 
D 1 366 GLU 366 366 366 GLU GLU D . n 
D 1 367 GLY 367 367 367 GLY GLY D . n 
D 1 368 TYR 368 368 368 TYR TYR D . n 
D 1 369 MET 369 369 369 MET MET D . n 
D 1 370 ALA 370 370 370 ALA ALA D . n 
D 1 371 ASP 371 371 371 ASP ASP D . n 
D 1 372 GLU 372 372 372 GLU GLU D . n 
D 1 373 LEU 373 373 373 LEU LEU D . n 
D 1 374 THR 374 374 374 THR THR D . n 
D 1 375 ILE 375 375 375 ILE ILE D . n 
D 1 376 ASP 376 376 376 ASP ASP D . n 
D 1 377 PRO 377 377 377 PRO PRO D . n 
D 1 378 VAL 378 378 378 VAL VAL D . n 
D 1 379 GLY 379 379 379 GLY GLY D . n 
D 1 380 ILE 380 380 380 ILE ILE D . n 
D 1 381 GLU 381 381 381 GLU GLU D . n 
D 1 382 ASP 382 382 382 ASP ASP D . n 
D 1 383 MET 383 383 383 MET MET D . n 
D 1 384 GLU 384 384 384 GLU GLU D . n 
D 1 385 LEU 385 385 385 LEU LEU D . n 
D 1 386 ALA 386 386 386 ALA ALA D . n 
D 1 387 PHE 387 387 387 PHE PHE D . n 
D 1 388 GLU 388 388 388 GLU GLU D . n 
D 1 389 PHE 389 389 389 PHE PHE D . n 
D 1 390 TYR 390 390 390 TYR TYR D . n 
D 1 391 ASP 391 391 391 ASP ASP D . n 
D 1 392 SER 392 392 392 SER SER D . n 
D 1 393 ASP 393 393 393 ASP ASP D . n 
D 1 394 ASN 394 394 394 ASN ASN D . n 
D 1 395 LYS 395 395 395 LYS LYS D . n 
D 1 396 ILE 396 396 396 ILE ILE D . n 
D 1 397 ILE 397 397 397 ILE ILE D . n 
D 1 398 LYS 398 398 398 LYS LYS D . n 
D 1 399 ASN 399 399 399 ASN ASN D . n 
D 1 400 GLU 400 400 400 GLU GLU D . n 
D 1 401 SER 401 401 401 SER SER D . n 
D 1 402 ILE 402 402 402 ILE ILE D . n 
D 1 403 ASN 403 403 403 ASN ASN D . n 
D 1 404 ILE 404 404 404 ILE ILE D . n 
D 1 405 LEU 405 405 405 LEU LEU D . n 
D 1 406 ALA 406 406 406 ALA ALA D . n 
D 1 407 SER 407 407 407 SER SER D . n 
D 1 408 LYS 408 408 408 LYS LYS D . n 
D 1 409 THR 409 409 409 THR THR D . n 
D 1 410 ALA 410 410 410 ALA ALA D . n 
D 1 411 PHE 411 411 411 PHE PHE D . n 
D 1 412 GLU 412 412 412 GLU GLU D . n 
D 1 413 LEU 413 413 413 LEU LEU D . n 
D 1 414 PRO 414 414 414 PRO PRO D . n 
D 1 415 GLU 415 415 415 GLU GLU D . n 
D 1 416 LEU 416 416 416 LEU LEU D . n 
D 1 417 THR 417 417 417 THR THR D . n 
D 1 418 ILE 418 418 418 ILE ILE D . n 
D 1 419 GLU 419 419 419 GLU GLU D . n 
D 1 420 VAL 420 420 420 VAL VAL D . n 
D 1 421 THR 421 421 421 THR THR D . n 
D 1 422 PRO 422 422 422 PRO PRO D . n 
D 1 423 GLU 423 423 423 GLU GLU D . n 
D 1 424 LYS 424 424 424 LYS LYS D . n 
D 1 425 ASP 425 425 425 ASP ASP D . n 
D 1 426 LEU 426 426 426 LEU LEU D . n 
D 1 427 ASN 427 427 427 ASN ASN D . n 
D 1 428 GLU 428 428 428 GLU GLU D . n 
D 1 429 GLY 429 429 429 GLY GLY D . n 
D 1 430 LYS 430 430 430 LYS LYS D . n 
D 1 431 ILE 431 431 431 ILE ILE D . n 
D 1 432 ALA 432 432 432 ALA ALA D . n 
D 1 433 SER 433 433 433 SER SER D . n 
D 1 434 ILE 434 434 434 ILE ILE D . n 
D 1 435 LYS 435 435 435 LYS LYS D . n 
D 1 436 THR 436 436 436 THR THR D . n 
D 1 437 LYS 437 437 437 LYS LYS D . n 
D 1 438 ILE 438 438 438 ILE ILE D . n 
D 1 439 GLU 439 439 439 GLU GLU D . n 
D 1 440 THR 440 440 440 THR THR D . n 
D 1 441 SER 441 441 441 SER SER D . n 
D 1 442 GLU 442 442 442 GLU GLU D . n 
D 1 443 ASN 443 443 443 ASN ASN D . n 
D 1 444 PHE 444 444 444 PHE PHE D . n 
D 1 445 THR 445 445 445 THR THR D . n 
D 1 446 LEU 446 446 446 LEU LEU D . n 
D 1 447 LEU 447 447 447 LEU LEU D . n 
D 1 448 ASP 448 448 448 ASP ASP D . n 
D 1 449 ASP 449 449 449 ASP ASP D . n 
D 1 450 LEU 450 450 450 LEU LEU D . n 
D 1 451 LYS 451 451 451 LYS LYS D . n 
D 1 452 ILE 452 452 452 ILE ILE D . n 
D 1 453 SER 453 453 453 SER SER D . n 
D 1 454 TYR 454 454 454 TYR TYR D . n 
D 1 455 ASN 455 455 455 ASN ASN D . n 
D 1 456 THR 456 456 456 THR THR D . n 
D 1 457 HIS 457 457 457 HIS HIS D . n 
D 1 458 LEU 458 458 458 LEU LEU D . n 
D 1 459 GLY 459 459 459 GLY GLY D . n 
D 1 460 TRP 460 460 460 TRP TRP D . n 
D 1 461 ALA 461 461 461 ALA ALA D . n 
D 1 462 ILE 462 462 462 ILE ILE D . n 
D 1 463 GLY 463 463 463 GLY GLY D . n 
D 1 464 SER 464 464 464 SER SER D . n 
D 1 465 GLN 465 465 465 GLN GLN D . n 
D 1 466 ALA 466 466 466 ALA ALA D . n 
D 1 467 SER 467 467 467 SER SER D . n 
D 1 468 VAL 468 468 468 VAL VAL D . n 
D 1 469 SER 469 469 469 SER SER D . n 
D 1 470 ILE 470 470 470 ILE ILE D . n 
D 1 471 SER 471 471 471 SER SER D . n 
D 1 472 ASP 472 472 472 ASP ASP D . n 
D 1 473 GLN 473 473 473 GLN GLN D . n 
D 1 474 LEU 474 474 474 LEU LEU D . n 
D 1 475 ASP 475 475 475 ASP ASP D . n 
D 1 476 LYS 476 476 476 LYS LYS D . n 
D 1 477 LYS 477 477 477 LYS LYS D . n 
D 1 478 ILE 478 478 478 ILE ILE D . n 
D 1 479 ILE 479 479 479 ILE ILE D . n 
D 1 480 THR 480 480 480 THR THR D . n 
D 1 481 SER 481 481 481 SER SER D . n 
D 1 482 GLU 482 482 482 GLU GLU D . n 
D 1 483 ASN 483 483 483 ASN ASN D . n 
D 1 484 PHE 484 484 484 PHE PHE D . n 
D 1 485 PHE 485 485 485 PHE PHE D . n 
D 1 486 ASN 486 486 486 ASN ASN D . n 
D 1 487 ILE 487 487 487 ILE ILE D . n 
D 1 488 PRO 488 488 488 PRO PRO D . n 
D 1 489 ASP 489 489 489 ASP ASP D . n 
D 1 490 ASN 490 490 490 ASN ASN D . n 
D 1 491 CYS 491 491 491 CYS CYS D . n 
D 1 492 TRP 492 492 492 TRP TRP D . n 
D 1 493 VAL 493 493 493 VAL VAL D . n 
D 1 494 VAL 494 494 494 VAL VAL D . n 
D 1 495 ASN 495 495 495 ASN ASN D . n 
D 1 496 ALA 496 496 496 ALA ALA D . n 
D 1 497 SER 497 497 497 SER SER D . n 
D 1 498 ALA 498 498 498 ALA ALA D . n 
D 1 499 GLY 499 499 499 GLY GLY D . n 
D 1 500 ILE 500 500 500 ILE ILE D . n 
D 1 501 SER 501 501 501 SER SER D . n 
D 1 502 VAL 502 502 502 VAL VAL D . n 
D 1 503 ARG 503 503 503 ARG ARG D . n 
D 1 504 TYR 504 504 504 TYR TYR D . n 
D 1 505 GLY 505 505 505 GLY GLY D . n 
D 1 506 LYS 506 506 506 LYS LYS D . n 
D 1 507 PHE 507 507 507 PHE PHE D . n 
D 1 508 THR 508 508 508 THR THR D . n 
D 1 509 PHE 509 509 509 PHE PHE D . n 
D 1 510 LYS 510 510 510 LYS LYS D . n 
D 1 511 ILE 511 511 511 ILE ILE D . n 
D 1 512 HIS 512 512 512 HIS HIS D . n 
D 1 513 ASP 513 513 513 ASP ASP D . n 
D 1 514 GLN 514 514 514 GLN GLN D . n 
D 1 515 LYS 515 515 515 LYS LYS D . n 
D 1 516 ILE 516 516 516 ILE ILE D . n 
D 1 517 ILE 517 517 517 ILE ILE D . n 
D 1 518 TYR 518 518 518 TYR TYR D . n 
D 1 519 ARG 519 519 519 ARG ARG D . n 
D 1 520 GLY 520 520 520 GLY GLY D . n 
D 1 521 ASP 521 521 521 ASP ASP D . n 
D 1 522 TRP 522 522 522 TRP TRP D . n 
D 1 523 ALA 523 523 523 ALA ALA D . n 
D 1 524 LYS 524 524 524 LYS LYS D . n 
D 1 525 GLU 525 525 525 GLU GLU D . n 
D 1 526 VAL 526 526 526 VAL VAL D . n 
D 1 527 GLY 527 527 527 GLY GLY D . n 
D 1 528 ARG 528 528 528 ARG ARG D . n 
D 1 529 LYS 529 529 529 LYS LYS D . n 
D 1 530 LEU 530 530 ?   ?   ?   D . n 
D 1 531 GLU 531 531 ?   ?   ?   D . n 
D 1 532 HIS 532 532 ?   ?   ?   D . n 
D 1 533 HIS 533 533 ?   ?   ?   D . n 
D 1 534 HIS 534 534 ?   ?   ?   D . n 
D 1 535 HIS 535 535 ?   ?   ?   D . n 
D 1 536 HIS 536 536 ?   ?   ?   D . n 
D 1 537 HIS 537 537 ?   ?   ?   D . n 
# 
loop_
_pdbx_branch_scheme.asym_id 
_pdbx_branch_scheme.entity_id 
_pdbx_branch_scheme.mon_id 
_pdbx_branch_scheme.num 
_pdbx_branch_scheme.pdb_asym_id 
_pdbx_branch_scheme.pdb_mon_id 
_pdbx_branch_scheme.pdb_seq_num 
_pdbx_branch_scheme.auth_asym_id 
_pdbx_branch_scheme.auth_mon_id 
_pdbx_branch_scheme.auth_seq_num 
_pdbx_branch_scheme.hetero 
E 2 BGC 1 E BGC 1 E BGC 1 n 
E 2 BGC 2 E BGC 2 E BGC 2 n 
E 2 BGC 3 E BGC 3 E BGC 3 n 
F 2 BGC 1 F BGC 1 F BGC 1 n 
F 2 BGC 2 F BGC 2 F BGC 2 n 
F 2 BGC 3 F BGC 3 F BGC 3 n 
G 2 BGC 1 G BGC 1 G BGC 1 n 
G 2 BGC 2 G BGC 2 G BGC 2 n 
G 2 BGC 3 G BGC 3 G BGC 3 n 
H 2 BGC 1 H BGC 1 H BGC 1 n 
H 2 BGC 2 H BGC 2 H BGC 2 n 
H 2 BGC 3 H BGC 3 H BGC 3 n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        BGC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   BGC 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
I  3 EDO 1   601 605  EDO EDO A . 
J  4 BGC 1   602 606  BGC BGC A . 
K  5 GOL 1   603 607  GOL GOL A . 
L  3 EDO 1   601 606  EDO EDO B . 
M  4 BGC 1   602 607  BGC BGC B . 
N  5 GOL 1   603 608  GOL GOL B . 
O  3 EDO 1   604 605  EDO EDO B . 
P  5 GOL 1   605 609  GOL GOL B . 
Q  5 GOL 1   606 610  GOL GOL B . 
R  3 EDO 1   601 604  EDO EDO C . 
S  6 PGE 1   602 605  PGE PG4 C . 
T  5 GOL 1   603 606  GOL GOL C . 
U  4 BGC 1   601 604  BGC BGC D . 
V  5 GOL 1   602 608  GOL GOL D . 
W  3 EDO 1   603 609  EDO EDO D . 
X  5 GOL 1   604 613  GOL GOL D . 
Y  5 GOL 1   605 614  GOL GOL D . 
Z  5 GOL 1   606 615  GOL GOL D . 
AA 5 GOL 1   607 616  GOL GOL D . 
BA 7 HOH 1   701 584  HOH HOH A . 
BA 7 HOH 2   702 758  HOH HOH A . 
BA 7 HOH 3   703 519  HOH HOH A . 
BA 7 HOH 4   704 819  HOH HOH A . 
BA 7 HOH 5   705 831  HOH HOH A . 
BA 7 HOH 6   706 719  HOH HOH A . 
BA 7 HOH 7   707 291  HOH HOH A . 
BA 7 HOH 8   708 360  HOH HOH A . 
BA 7 HOH 9   709 750  HOH HOH A . 
BA 7 HOH 10  710 250  HOH HOH A . 
BA 7 HOH 11  711 718  HOH HOH A . 
BA 7 HOH 12  712 249  HOH HOH A . 
BA 7 HOH 13  713 532  HOH HOH A . 
BA 7 HOH 14  714 262  HOH HOH A . 
BA 7 HOH 15  715 789  HOH HOH A . 
BA 7 HOH 16  716 968  HOH HOH A . 
BA 7 HOH 17  717 494  HOH HOH A . 
BA 7 HOH 18  718 79   HOH HOH A . 
BA 7 HOH 19  719 337  HOH HOH A . 
BA 7 HOH 20  720 630  HOH HOH A . 
BA 7 HOH 21  721 200  HOH HOH A . 
BA 7 HOH 22  722 83   HOH HOH A . 
BA 7 HOH 23  723 1025 HOH HOH A . 
BA 7 HOH 24  724 28   HOH HOH A . 
BA 7 HOH 25  725 988  HOH HOH A . 
BA 7 HOH 26  726 136  HOH HOH A . 
BA 7 HOH 27  727 127  HOH HOH A . 
BA 7 HOH 28  728 975  HOH HOH A . 
BA 7 HOH 29  729 18   HOH HOH A . 
BA 7 HOH 30  730 944  HOH HOH A . 
BA 7 HOH 31  731 237  HOH HOH A . 
BA 7 HOH 32  732 111  HOH HOH A . 
BA 7 HOH 33  733 899  HOH HOH A . 
BA 7 HOH 34  734 633  HOH HOH A . 
BA 7 HOH 35  735 14   HOH HOH A . 
BA 7 HOH 36  736 345  HOH HOH A . 
BA 7 HOH 37  737 352  HOH HOH A . 
BA 7 HOH 38  738 124  HOH HOH A . 
BA 7 HOH 39  739 947  HOH HOH A . 
BA 7 HOH 40  740 847  HOH HOH A . 
BA 7 HOH 41  741 575  HOH HOH A . 
BA 7 HOH 42  742 261  HOH HOH A . 
BA 7 HOH 43  743 113  HOH HOH A . 
BA 7 HOH 44  744 531  HOH HOH A . 
BA 7 HOH 45  745 942  HOH HOH A . 
BA 7 HOH 46  746 301  HOH HOH A . 
BA 7 HOH 47  747 122  HOH HOH A . 
BA 7 HOH 48  748 547  HOH HOH A . 
BA 7 HOH 49  749 116  HOH HOH A . 
BA 7 HOH 50  750 408  HOH HOH A . 
BA 7 HOH 51  751 535  HOH HOH A . 
BA 7 HOH 52  752 508  HOH HOH A . 
BA 7 HOH 53  753 527  HOH HOH A . 
BA 7 HOH 54  754 889  HOH HOH A . 
BA 7 HOH 55  755 490  HOH HOH A . 
BA 7 HOH 56  756 929  HOH HOH A . 
BA 7 HOH 57  757 797  HOH HOH A . 
BA 7 HOH 58  758 982  HOH HOH A . 
BA 7 HOH 59  759 821  HOH HOH A . 
BA 7 HOH 60  760 394  HOH HOH A . 
BA 7 HOH 61  761 25   HOH HOH A . 
BA 7 HOH 62  762 37   HOH HOH A . 
BA 7 HOH 63  763 306  HOH HOH A . 
BA 7 HOH 64  764 873  HOH HOH A . 
BA 7 HOH 65  765 763  HOH HOH A . 
BA 7 HOH 66  766 329  HOH HOH A . 
BA 7 HOH 67  767 986  HOH HOH A . 
BA 7 HOH 68  768 772  HOH HOH A . 
BA 7 HOH 69  769 886  HOH HOH A . 
BA 7 HOH 70  770 312  HOH HOH A . 
BA 7 HOH 71  771 358  HOH HOH A . 
BA 7 HOH 72  772 951  HOH HOH A . 
BA 7 HOH 73  773 792  HOH HOH A . 
BA 7 HOH 74  774 643  HOH HOH A . 
BA 7 HOH 75  775 385  HOH HOH A . 
BA 7 HOH 76  776 552  HOH HOH A . 
BA 7 HOH 77  777 64   HOH HOH A . 
BA 7 HOH 78  778 436  HOH HOH A . 
BA 7 HOH 79  779 587  HOH HOH A . 
BA 7 HOH 80  780 585  HOH HOH A . 
BA 7 HOH 81  781 15   HOH HOH A . 
BA 7 HOH 82  782 946  HOH HOH A . 
BA 7 HOH 83  783 273  HOH HOH A . 
BA 7 HOH 84  784 438  HOH HOH A . 
BA 7 HOH 85  785 534  HOH HOH A . 
BA 7 HOH 86  786 4    HOH HOH A . 
BA 7 HOH 87  787 832  HOH HOH A . 
BA 7 HOH 88  788 70   HOH HOH A . 
BA 7 HOH 89  789 511  HOH HOH A . 
BA 7 HOH 90  790 372  HOH HOH A . 
BA 7 HOH 91  791 515  HOH HOH A . 
BA 7 HOH 92  792 877  HOH HOH A . 
BA 7 HOH 93  793 303  HOH HOH A . 
BA 7 HOH 94  794 660  HOH HOH A . 
BA 7 HOH 95  795 86   HOH HOH A . 
BA 7 HOH 96  796 489  HOH HOH A . 
BA 7 HOH 97  797 918  HOH HOH A . 
BA 7 HOH 98  798 42   HOH HOH A . 
BA 7 HOH 99  799 943  HOH HOH A . 
BA 7 HOH 100 800 888  HOH HOH A . 
BA 7 HOH 101 801 121  HOH HOH A . 
BA 7 HOH 102 802 498  HOH HOH A . 
BA 7 HOH 103 803 1019 HOH HOH A . 
BA 7 HOH 104 804 715  HOH HOH A . 
BA 7 HOH 105 805 193  HOH HOH A . 
BA 7 HOH 106 806 336  HOH HOH A . 
BA 7 HOH 107 807 488  HOH HOH A . 
BA 7 HOH 108 808 297  HOH HOH A . 
BA 7 HOH 109 809 618  HOH HOH A . 
BA 7 HOH 110 810 355  HOH HOH A . 
BA 7 HOH 111 811 785  HOH HOH A . 
BA 7 HOH 112 812 398  HOH HOH A . 
BA 7 HOH 113 813 6    HOH HOH A . 
BA 7 HOH 114 814 544  HOH HOH A . 
BA 7 HOH 115 815 466  HOH HOH A . 
BA 7 HOH 116 816 884  HOH HOH A . 
BA 7 HOH 117 817 560  HOH HOH A . 
BA 7 HOH 118 818 115  HOH HOH A . 
BA 7 HOH 119 819 45   HOH HOH A . 
BA 7 HOH 120 820 781  HOH HOH A . 
BA 7 HOH 121 821 626  HOH HOH A . 
BA 7 HOH 122 822 50   HOH HOH A . 
BA 7 HOH 123 823 393  HOH HOH A . 
BA 7 HOH 124 824 137  HOH HOH A . 
BA 7 HOH 125 825 219  HOH HOH A . 
BA 7 HOH 126 826 51   HOH HOH A . 
BA 7 HOH 127 827 449  HOH HOH A . 
BA 7 HOH 128 828 628  HOH HOH A . 
BA 7 HOH 129 829 680  HOH HOH A . 
BA 7 HOH 130 830 148  HOH HOH A . 
BA 7 HOH 131 831 221  HOH HOH A . 
BA 7 HOH 132 832 106  HOH HOH A . 
BA 7 HOH 133 833 191  HOH HOH A . 
BA 7 HOH 134 834 406  HOH HOH A . 
BA 7 HOH 135 835 305  HOH HOH A . 
BA 7 HOH 136 836 639  HOH HOH A . 
BA 7 HOH 137 837 597  HOH HOH A . 
BA 7 HOH 138 838 545  HOH HOH A . 
BA 7 HOH 139 839 596  HOH HOH A . 
BA 7 HOH 140 840 568  HOH HOH A . 
BA 7 HOH 141 841 863  HOH HOH A . 
BA 7 HOH 142 842 564  HOH HOH A . 
BA 7 HOH 143 843 513  HOH HOH A . 
BA 7 HOH 144 844 374  HOH HOH A . 
BA 7 HOH 145 845 388  HOH HOH A . 
BA 7 HOH 146 846 391  HOH HOH A . 
BA 7 HOH 147 847 826  HOH HOH A . 
BA 7 HOH 148 848 8    HOH HOH A . 
BA 7 HOH 149 849 562  HOH HOH A . 
BA 7 HOH 150 850 493  HOH HOH A . 
BA 7 HOH 151 851 13   HOH HOH A . 
BA 7 HOH 152 852 203  HOH HOH A . 
BA 7 HOH 153 853 915  HOH HOH A . 
BA 7 HOH 154 854 202  HOH HOH A . 
BA 7 HOH 155 855 924  HOH HOH A . 
BA 7 HOH 156 856 187  HOH HOH A . 
BA 7 HOH 157 857 445  HOH HOH A . 
BA 7 HOH 158 858 112  HOH HOH A . 
BA 7 HOH 159 859 325  HOH HOH A . 
BA 7 HOH 160 860 196  HOH HOH A . 
BA 7 HOH 161 861 145  HOH HOH A . 
BA 7 HOH 162 862 165  HOH HOH A . 
BA 7 HOH 163 863 621  HOH HOH A . 
BA 7 HOH 164 864 971  HOH HOH A . 
BA 7 HOH 165 865 142  HOH HOH A . 
BA 7 HOH 166 866 834  HOH HOH A . 
BA 7 HOH 167 867 809  HOH HOH A . 
BA 7 HOH 168 868 216  HOH HOH A . 
BA 7 HOH 169 869 599  HOH HOH A . 
BA 7 HOH 170 870 617  HOH HOH A . 
BA 7 HOH 171 871 522  HOH HOH A . 
BA 7 HOH 172 872 467  HOH HOH A . 
BA 7 HOH 173 873 524  HOH HOH A . 
BA 7 HOH 174 874 666  HOH HOH A . 
BA 7 HOH 175 875 654  HOH HOH A . 
BA 7 HOH 176 876 843  HOH HOH A . 
BA 7 HOH 177 877 99   HOH HOH A . 
BA 7 HOH 178 878 376  HOH HOH A . 
BA 7 HOH 179 879 712  HOH HOH A . 
BA 7 HOH 180 880 766  HOH HOH A . 
BA 7 HOH 181 881 321  HOH HOH A . 
BA 7 HOH 182 882 504  HOH HOH A . 
BA 7 HOH 183 883 992  HOH HOH A . 
BA 7 HOH 184 884 271  HOH HOH A . 
BA 7 HOH 185 885 598  HOH HOH A . 
BA 7 HOH 186 886 243  HOH HOH A . 
BA 7 HOH 187 887 672  HOH HOH A . 
BA 7 HOH 188 888 407  HOH HOH A . 
BA 7 HOH 189 889 235  HOH HOH A . 
BA 7 HOH 190 890 304  HOH HOH A . 
BA 7 HOH 191 891 131  HOH HOH A . 
BA 7 HOH 192 892 695  HOH HOH A . 
BA 7 HOH 193 893 659  HOH HOH A . 
BA 7 HOH 194 894 998  HOH HOH A . 
BA 7 HOH 195 895 309  HOH HOH A . 
BA 7 HOH 196 896 554  HOH HOH A . 
BA 7 HOH 197 897 317  HOH HOH A . 
BA 7 HOH 198 898 804  HOH HOH A . 
BA 7 HOH 199 899 164  HOH HOH A . 
BA 7 HOH 200 900 315  HOH HOH A . 
BA 7 HOH 201 901 684  HOH HOH A . 
BA 7 HOH 202 902 1    HOH HOH A . 
BA 7 HOH 203 903 85   HOH HOH A . 
BA 7 HOH 204 904 509  HOH HOH A . 
BA 7 HOH 205 905 248  HOH HOH A . 
BA 7 HOH 206 906 649  HOH HOH A . 
BA 7 HOH 207 907 381  HOH HOH A . 
BA 7 HOH 208 908 605  HOH HOH A . 
BA 7 HOH 209 909 459  HOH HOH A . 
BA 7 HOH 210 910 412  HOH HOH A . 
BA 7 HOH 211 911 266  HOH HOH A . 
BA 7 HOH 212 912 223  HOH HOH A . 
BA 7 HOH 213 913 963  HOH HOH A . 
BA 7 HOH 214 914 227  HOH HOH A . 
BA 7 HOH 215 915 296  HOH HOH A . 
BA 7 HOH 216 916 919  HOH HOH A . 
BA 7 HOH 217 917 144  HOH HOH A . 
BA 7 HOH 218 918 681  HOH HOH A . 
BA 7 HOH 219 919 668  HOH HOH A . 
BA 7 HOH 220 920 683  HOH HOH A . 
BA 7 HOH 221 921 169  HOH HOH A . 
BA 7 HOH 222 922 382  HOH HOH A . 
BA 7 HOH 223 923 67   HOH HOH A . 
BA 7 HOH 224 924 211  HOH HOH A . 
BA 7 HOH 225 925 245  HOH HOH A . 
BA 7 HOH 226 926 561  HOH HOH A . 
BA 7 HOH 227 927 670  HOH HOH A . 
BA 7 HOH 228 928 281  HOH HOH A . 
BA 7 HOH 229 929 392  HOH HOH A . 
BA 7 HOH 230 930 555  HOH HOH A . 
BA 7 HOH 231 931 80   HOH HOH A . 
BA 7 HOH 232 932 326  HOH HOH A . 
BA 7 HOH 233 933 1021 HOH HOH A . 
BA 7 HOH 234 934 1010 HOH HOH A . 
BA 7 HOH 235 935 984  HOH HOH A . 
BA 7 HOH 236 936 922  HOH HOH A . 
BA 7 HOH 237 937 367  HOH HOH A . 
BA 7 HOH 238 938 416  HOH HOH A . 
BA 7 HOH 239 939 404  HOH HOH A . 
BA 7 HOH 240 940 1006 HOH HOH A . 
BA 7 HOH 241 941 159  HOH HOH A . 
BA 7 HOH 242 942 853  HOH HOH A . 
BA 7 HOH 243 943 422  HOH HOH A . 
BA 7 HOH 244 944 740  HOH HOH A . 
BA 7 HOH 245 945 983  HOH HOH A . 
BA 7 HOH 246 946 647  HOH HOH A . 
BA 7 HOH 247 947 421  HOH HOH A . 
BA 7 HOH 248 948 215  HOH HOH A . 
BA 7 HOH 249 949 482  HOH HOH A . 
BA 7 HOH 250 950 742  HOH HOH A . 
BA 7 HOH 251 951 906  HOH HOH A . 
BA 7 HOH 252 952 846  HOH HOH A . 
BA 7 HOH 253 953 450  HOH HOH A . 
BA 7 HOH 254 954 744  HOH HOH A . 
BA 7 HOH 255 955 485  HOH HOH A . 
BA 7 HOH 256 956 820  HOH HOH A . 
BA 7 HOH 257 957 765  HOH HOH A . 
BA 7 HOH 258 958 236  HOH HOH A . 
BA 7 HOH 259 959 487  HOH HOH A . 
BA 7 HOH 260 960 472  HOH HOH A . 
BA 7 HOH 261 961 830  HOH HOH A . 
BA 7 HOH 262 962 827  HOH HOH A . 
BA 7 HOH 263 963 871  HOH HOH A . 
BA 7 HOH 264 964 913  HOH HOH A . 
BA 7 HOH 265 965 859  HOH HOH A . 
BA 7 HOH 266 966 732  HOH HOH A . 
BA 7 HOH 267 967 840  HOH HOH A . 
BA 7 HOH 268 968 729  HOH HOH A . 
BA 7 HOH 269 969 443  HOH HOH A . 
BA 7 HOH 270 970 1007 HOH HOH A . 
BA 7 HOH 271 971 477  HOH HOH A . 
BA 7 HOH 272 972 1026 HOH HOH A . 
BA 7 HOH 273 973 212  HOH HOH A . 
BA 7 HOH 274 974 578  HOH HOH A . 
BA 7 HOH 275 975 1003 HOH HOH A . 
CA 7 HOH 1   701 934  HOH HOH B . 
CA 7 HOH 2   702 759  HOH HOH B . 
CA 7 HOH 3   703 967  HOH HOH B . 
CA 7 HOH 4   704 771  HOH HOH B . 
CA 7 HOH 5   705 254  HOH HOH B . 
CA 7 HOH 6   706 90   HOH HOH B . 
CA 7 HOH 7   707 512  HOH HOH B . 
CA 7 HOH 8   708 667  HOH HOH B . 
CA 7 HOH 9   709 264  HOH HOH B . 
CA 7 HOH 10  710 460  HOH HOH B . 
CA 7 HOH 11  711 813  HOH HOH B . 
CA 7 HOH 12  712 807  HOH HOH B . 
CA 7 HOH 13  713 960  HOH HOH B . 
CA 7 HOH 14  714 959  HOH HOH B . 
CA 7 HOH 15  715 192  HOH HOH B . 
CA 7 HOH 16  716 91   HOH HOH B . 
CA 7 HOH 17  717 747  HOH HOH B . 
CA 7 HOH 18  718 141  HOH HOH B . 
CA 7 HOH 19  719 65   HOH HOH B . 
CA 7 HOH 20  720 829  HOH HOH B . 
CA 7 HOH 21  721 776  HOH HOH B . 
CA 7 HOH 22  722 916  HOH HOH B . 
CA 7 HOH 23  723 499  HOH HOH B . 
CA 7 HOH 24  724 641  HOH HOH B . 
CA 7 HOH 25  725 501  HOH HOH B . 
CA 7 HOH 26  726 81   HOH HOH B . 
CA 7 HOH 27  727 330  HOH HOH B . 
CA 7 HOH 28  728 663  HOH HOH B . 
CA 7 HOH 29  729 939  HOH HOH B . 
CA 7 HOH 30  730 569  HOH HOH B . 
CA 7 HOH 31  731 239  HOH HOH B . 
CA 7 HOH 32  732 366  HOH HOH B . 
CA 7 HOH 33  733 9    HOH HOH B . 
CA 7 HOH 34  734 267  HOH HOH B . 
CA 7 HOH 35  735 954  HOH HOH B . 
CA 7 HOH 36  736 480  HOH HOH B . 
CA 7 HOH 37  737 205  HOH HOH B . 
CA 7 HOH 38  738 186  HOH HOH B . 
CA 7 HOH 39  739 864  HOH HOH B . 
CA 7 HOH 40  740 24   HOH HOH B . 
CA 7 HOH 41  741 627  HOH HOH B . 
CA 7 HOH 42  742 812  HOH HOH B . 
CA 7 HOH 43  743 313  HOH HOH B . 
CA 7 HOH 44  744 94   HOH HOH B . 
CA 7 HOH 45  745 182  HOH HOH B . 
CA 7 HOH 46  746 948  HOH HOH B . 
CA 7 HOH 47  747 276  HOH HOH B . 
CA 7 HOH 48  748 731  HOH HOH B . 
CA 7 HOH 49  749 46   HOH HOH B . 
CA 7 HOH 50  750 454  HOH HOH B . 
CA 7 HOH 51  751 1008 HOH HOH B . 
CA 7 HOH 52  752 259  HOH HOH B . 
CA 7 HOH 53  753 949  HOH HOH B . 
CA 7 HOH 54  754 71   HOH HOH B . 
CA 7 HOH 55  755 691  HOH HOH B . 
CA 7 HOH 56  756 1032 HOH HOH B . 
CA 7 HOH 57  757 453  HOH HOH B . 
CA 7 HOH 58  758 774  HOH HOH B . 
CA 7 HOH 59  759 300  HOH HOH B . 
CA 7 HOH 60  760 333  HOH HOH B . 
CA 7 HOH 61  761 52   HOH HOH B . 
CA 7 HOH 62  762 54   HOH HOH B . 
CA 7 HOH 63  763 811  HOH HOH B . 
CA 7 HOH 64  764 858  HOH HOH B . 
CA 7 HOH 65  765 188  HOH HOH B . 
CA 7 HOH 66  766 502  HOH HOH B . 
CA 7 HOH 67  767 140  HOH HOH B . 
CA 7 HOH 68  768 464  HOH HOH B . 
CA 7 HOH 69  769 375  HOH HOH B . 
CA 7 HOH 70  770 937  HOH HOH B . 
CA 7 HOH 71  771 11   HOH HOH B . 
CA 7 HOH 72  772 114  HOH HOH B . 
CA 7 HOH 73  773 425  HOH HOH B . 
CA 7 HOH 74  774 634  HOH HOH B . 
CA 7 HOH 75  775 189  HOH HOH B . 
CA 7 HOH 76  776 748  HOH HOH B . 
CA 7 HOH 77  777 415  HOH HOH B . 
CA 7 HOH 78  778 218  HOH HOH B . 
CA 7 HOH 79  779 717  HOH HOH B . 
CA 7 HOH 80  780 346  HOH HOH B . 
CA 7 HOH 81  781 335  HOH HOH B . 
CA 7 HOH 82  782 323  HOH HOH B . 
CA 7 HOH 83  783 163  HOH HOH B . 
CA 7 HOH 84  784 815  HOH HOH B . 
CA 7 HOH 85  785 339  HOH HOH B . 
CA 7 HOH 86  786 22   HOH HOH B . 
CA 7 HOH 87  787 156  HOH HOH B . 
CA 7 HOH 88  788 1031 HOH HOH B . 
CA 7 HOH 89  789 134  HOH HOH B . 
CA 7 HOH 90  790 354  HOH HOH B . 
CA 7 HOH 91  791 229  HOH HOH B . 
CA 7 HOH 92  792 708  HOH HOH B . 
CA 7 HOH 93  793 69   HOH HOH B . 
CA 7 HOH 94  794 39   HOH HOH B . 
CA 7 HOH 95  795 161  HOH HOH B . 
CA 7 HOH 96  796 257  HOH HOH B . 
CA 7 HOH 97  797 469  HOH HOH B . 
CA 7 HOH 98  798 537  HOH HOH B . 
CA 7 HOH 99  799 41   HOH HOH B . 
CA 7 HOH 100 800 895  HOH HOH B . 
CA 7 HOH 101 801 816  HOH HOH B . 
CA 7 HOH 102 802 980  HOH HOH B . 
CA 7 HOH 103 803 451  HOH HOH B . 
CA 7 HOH 104 804 423  HOH HOH B . 
CA 7 HOH 105 805 10   HOH HOH B . 
CA 7 HOH 106 806 93   HOH HOH B . 
CA 7 HOH 107 807 861  HOH HOH B . 
CA 7 HOH 108 808 318  HOH HOH B . 
CA 7 HOH 109 809 35   HOH HOH B . 
CA 7 HOH 110 810 255  HOH HOH B . 
CA 7 HOH 111 811 108  HOH HOH B . 
CA 7 HOH 112 812 997  HOH HOH B . 
CA 7 HOH 113 813 456  HOH HOH B . 
CA 7 HOH 114 814 73   HOH HOH B . 
CA 7 HOH 115 815 762  HOH HOH B . 
CA 7 HOH 116 816 147  HOH HOH B . 
CA 7 HOH 117 817 767  HOH HOH B . 
CA 7 HOH 118 818 645  HOH HOH B . 
CA 7 HOH 119 819 338  HOH HOH B . 
CA 7 HOH 120 820 125  HOH HOH B . 
CA 7 HOH 121 821 941  HOH HOH B . 
CA 7 HOH 122 822 876  HOH HOH B . 
CA 7 HOH 123 823 174  HOH HOH B . 
CA 7 HOH 124 824 138  HOH HOH B . 
CA 7 HOH 125 825 730  HOH HOH B . 
CA 7 HOH 126 826 175  HOH HOH B . 
CA 7 HOH 127 827 287  HOH HOH B . 
CA 7 HOH 128 828 208  HOH HOH B . 
CA 7 HOH 129 829 1002 HOH HOH B . 
CA 7 HOH 130 830 342  HOH HOH B . 
CA 7 HOH 131 831 736  HOH HOH B . 
CA 7 HOH 132 832 343  HOH HOH B . 
CA 7 HOH 133 833 796  HOH HOH B . 
CA 7 HOH 134 834 324  HOH HOH B . 
CA 7 HOH 135 835 68   HOH HOH B . 
CA 7 HOH 136 836 571  HOH HOH B . 
CA 7 HOH 137 837 441  HOH HOH B . 
CA 7 HOH 138 838 455  HOH HOH B . 
CA 7 HOH 139 839 32   HOH HOH B . 
CA 7 HOH 140 840 133  HOH HOH B . 
CA 7 HOH 141 841 98   HOH HOH B . 
CA 7 HOH 142 842 132  HOH HOH B . 
CA 7 HOH 143 843 976  HOH HOH B . 
CA 7 HOH 144 844 154  HOH HOH B . 
CA 7 HOH 145 845 322  HOH HOH B . 
CA 7 HOH 146 846 177  HOH HOH B . 
CA 7 HOH 147 847 657  HOH HOH B . 
CA 7 HOH 148 848 529  HOH HOH B . 
CA 7 HOH 149 849 149  HOH HOH B . 
CA 7 HOH 150 850 746  HOH HOH B . 
CA 7 HOH 151 851 556  HOH HOH B . 
CA 7 HOH 152 852 420  HOH HOH B . 
CA 7 HOH 153 853 503  HOH HOH B . 
CA 7 HOH 154 854 574  HOH HOH B . 
CA 7 HOH 155 855 299  HOH HOH B . 
CA 7 HOH 156 856 656  HOH HOH B . 
CA 7 HOH 157 857 369  HOH HOH B . 
CA 7 HOH 158 858 648  HOH HOH B . 
CA 7 HOH 159 859 23   HOH HOH B . 
CA 7 HOH 160 860 405  HOH HOH B . 
CA 7 HOH 161 861 567  HOH HOH B . 
CA 7 HOH 162 862 768  HOH HOH B . 
CA 7 HOH 163 863 226  HOH HOH B . 
CA 7 HOH 164 864 210  HOH HOH B . 
CA 7 HOH 165 865 981  HOH HOH B . 
CA 7 HOH 166 866 492  HOH HOH B . 
CA 7 HOH 167 867 548  HOH HOH B . 
CA 7 HOH 168 868 678  HOH HOH B . 
CA 7 HOH 169 869 361  HOH HOH B . 
CA 7 HOH 170 870 818  HOH HOH B . 
CA 7 HOH 171 871 799  HOH HOH B . 
CA 7 HOH 172 872 465  HOH HOH B . 
CA 7 HOH 173 873 514  HOH HOH B . 
CA 7 HOH 174 874 711  HOH HOH B . 
CA 7 HOH 175 875 373  HOH HOH B . 
CA 7 HOH 176 876 594  HOH HOH B . 
CA 7 HOH 177 877 1011 HOH HOH B . 
CA 7 HOH 178 878 418  HOH HOH B . 
CA 7 HOH 179 879 349  HOH HOH B . 
CA 7 HOH 180 880 280  HOH HOH B . 
CA 7 HOH 181 881 269  HOH HOH B . 
CA 7 HOH 182 882 927  HOH HOH B . 
CA 7 HOH 183 883 197  HOH HOH B . 
CA 7 HOH 184 884 444  HOH HOH B . 
CA 7 HOH 185 885 278  HOH HOH B . 
CA 7 HOH 186 886 357  HOH HOH B . 
CA 7 HOH 187 887 898  HOH HOH B . 
CA 7 HOH 188 888 686  HOH HOH B . 
CA 7 HOH 189 889 1014 HOH HOH B . 
CA 7 HOH 190 890 687  HOH HOH B . 
CA 7 HOH 191 891 696  HOH HOH B . 
CA 7 HOH 192 892 625  HOH HOH B . 
CA 7 HOH 193 893 87   HOH HOH B . 
CA 7 HOH 194 894 288  HOH HOH B . 
CA 7 HOH 195 895 179  HOH HOH B . 
CA 7 HOH 196 896 808  HOH HOH B . 
CA 7 HOH 197 897 403  HOH HOH B . 
CA 7 HOH 198 898 688  HOH HOH B . 
CA 7 HOH 199 899 883  HOH HOH B . 
CA 7 HOH 200 900 582  HOH HOH B . 
CA 7 HOH 201 901 75   HOH HOH B . 
CA 7 HOH 202 902 644  HOH HOH B . 
CA 7 HOH 203 903 285  HOH HOH B . 
CA 7 HOH 204 904 685  HOH HOH B . 
CA 7 HOH 205 905 351  HOH HOH B . 
CA 7 HOH 206 906 225  HOH HOH B . 
CA 7 HOH 207 907 123  HOH HOH B . 
CA 7 HOH 208 908 653  HOH HOH B . 
CA 7 HOH 209 909 609  HOH HOH B . 
CA 7 HOH 210 910 289  HOH HOH B . 
CA 7 HOH 211 911 909  HOH HOH B . 
CA 7 HOH 212 912 88   HOH HOH B . 
CA 7 HOH 213 913 525  HOH HOH B . 
CA 7 HOH 214 914 814  HOH HOH B . 
CA 7 HOH 215 915 932  HOH HOH B . 
CA 7 HOH 216 916 1030 HOH HOH B . 
CA 7 HOH 217 917 591  HOH HOH B . 
CA 7 HOH 218 918 706  HOH HOH B . 
CA 7 HOH 219 919 439  HOH HOH B . 
CA 7 HOH 220 920 1012 HOH HOH B . 
CA 7 HOH 221 921 209  HOH HOH B . 
CA 7 HOH 222 922 1018 HOH HOH B . 
CA 7 HOH 223 923 921  HOH HOH B . 
CA 7 HOH 224 924 401  HOH HOH B . 
CA 7 HOH 225 925 844  HOH HOH B . 
CA 7 HOH 226 926 969  HOH HOH B . 
CA 7 HOH 227 927 879  HOH HOH B . 
CA 7 HOH 228 928 866  HOH HOH B . 
CA 7 HOH 229 929 810  HOH HOH B . 
CA 7 HOH 230 930 782  HOH HOH B . 
CA 7 HOH 231 931 857  HOH HOH B . 
CA 7 HOH 232 932 474  HOH HOH B . 
CA 7 HOH 233 933 447  HOH HOH B . 
CA 7 HOH 234 934 950  HOH HOH B . 
CA 7 HOH 235 935 955  HOH HOH B . 
CA 7 HOH 236 936 977  HOH HOH B . 
CA 7 HOH 237 937 258  HOH HOH B . 
CA 7 HOH 238 938 798  HOH HOH B . 
CA 7 HOH 239 939 908  HOH HOH B . 
CA 7 HOH 240 940 293  HOH HOH B . 
CA 7 HOH 241 941 735  HOH HOH B . 
CA 7 HOH 242 942 945  HOH HOH B . 
DA 7 HOH 1   701 754  HOH HOH C . 
DA 7 HOH 2   702 240  HOH HOH C . 
DA 7 HOH 3   703 347  HOH HOH C . 
DA 7 HOH 4   704 842  HOH HOH C . 
DA 7 HOH 5   705 769  HOH HOH C . 
DA 7 HOH 6   706 850  HOH HOH C . 
DA 7 HOH 7   707 752  HOH HOH C . 
DA 7 HOH 8   708 44   HOH HOH C . 
DA 7 HOH 9   709 428  HOH HOH C . 
DA 7 HOH 10  710 110  HOH HOH C . 
DA 7 HOH 11  711 365  HOH HOH C . 
DA 7 HOH 12  712 817  HOH HOH C . 
DA 7 HOH 13  713 104  HOH HOH C . 
DA 7 HOH 14  714 135  HOH HOH C . 
DA 7 HOH 15  715 794  HOH HOH C . 
DA 7 HOH 16  716 623  HOH HOH C . 
DA 7 HOH 17  717 779  HOH HOH C . 
DA 7 HOH 18  718 996  HOH HOH C . 
DA 7 HOH 19  719 57   HOH HOH C . 
DA 7 HOH 20  720 716  HOH HOH C . 
DA 7 HOH 21  721 707  HOH HOH C . 
DA 7 HOH 22  722 484  HOH HOH C . 
DA 7 HOH 23  723 256  HOH HOH C . 
DA 7 HOH 24  724 253  HOH HOH C . 
DA 7 HOH 25  725 380  HOH HOH C . 
DA 7 HOH 26  726 180  HOH HOH C . 
DA 7 HOH 27  727 928  HOH HOH C . 
DA 7 HOH 28  728 579  HOH HOH C . 
DA 7 HOH 29  729 510  HOH HOH C . 
DA 7 HOH 30  730 72   HOH HOH C . 
DA 7 HOH 31  731 100  HOH HOH C . 
DA 7 HOH 32  732 788  HOH HOH C . 
DA 7 HOH 33  733 620  HOH HOH C . 
DA 7 HOH 34  734 30   HOH HOH C . 
DA 7 HOH 35  735 773  HOH HOH C . 
DA 7 HOH 36  736 397  HOH HOH C . 
DA 7 HOH 37  737 931  HOH HOH C . 
DA 7 HOH 38  738 150  HOH HOH C . 
DA 7 HOH 39  739 274  HOH HOH C . 
DA 7 HOH 40  740 698  HOH HOH C . 
DA 7 HOH 41  741 823  HOH HOH C . 
DA 7 HOH 42  742 413  HOH HOH C . 
DA 7 HOH 43  743 583  HOH HOH C . 
DA 7 HOH 44  744 892  HOH HOH C . 
DA 7 HOH 45  745 675  HOH HOH C . 
DA 7 HOH 46  746 632  HOH HOH C . 
DA 7 HOH 47  747 371  HOH HOH C . 
DA 7 HOH 48  748 615  HOH HOH C . 
DA 7 HOH 49  749 34   HOH HOH C . 
DA 7 HOH 50  750 341  HOH HOH C . 
DA 7 HOH 51  751 96   HOH HOH C . 
DA 7 HOH 52  752 837  HOH HOH C . 
DA 7 HOH 53  753 206  HOH HOH C . 
DA 7 HOH 54  754 194  HOH HOH C . 
DA 7 HOH 55  755 448  HOH HOH C . 
DA 7 HOH 56  756 546  HOH HOH C . 
DA 7 HOH 57  757 662  HOH HOH C . 
DA 7 HOH 58  758 940  HOH HOH C . 
DA 7 HOH 59  759 500  HOH HOH C . 
DA 7 HOH 60  760 78   HOH HOH C . 
DA 7 HOH 61  761 753  HOH HOH C . 
DA 7 HOH 62  762 855  HOH HOH C . 
DA 7 HOH 63  763 851  HOH HOH C . 
DA 7 HOH 64  764 153  HOH HOH C . 
DA 7 HOH 65  765 33   HOH HOH C . 
DA 7 HOH 66  766 805  HOH HOH C . 
DA 7 HOH 67  767 294  HOH HOH C . 
DA 7 HOH 68  768 399  HOH HOH C . 
DA 7 HOH 69  769 29   HOH HOH C . 
DA 7 HOH 70  770 824  HOH HOH C . 
DA 7 HOH 71  771 183  HOH HOH C . 
DA 7 HOH 72  772 56   HOH HOH C . 
DA 7 HOH 73  773 1013 HOH HOH C . 
DA 7 HOH 74  774 40   HOH HOH C . 
DA 7 HOH 75  775 12   HOH HOH C . 
DA 7 HOH 76  776 117  HOH HOH C . 
DA 7 HOH 77  777 674  HOH HOH C . 
DA 7 HOH 78  778 801  HOH HOH C . 
DA 7 HOH 79  779 646  HOH HOH C . 
DA 7 HOH 80  780 260  HOH HOH C . 
DA 7 HOH 81  781 721  HOH HOH C . 
DA 7 HOH 82  782 903  HOH HOH C . 
DA 7 HOH 83  783 669  HOH HOH C . 
DA 7 HOH 84  784 105  HOH HOH C . 
DA 7 HOH 85  785 224  HOH HOH C . 
DA 7 HOH 86  786 389  HOH HOH C . 
DA 7 HOH 87  787 638  HOH HOH C . 
DA 7 HOH 88  788 431  HOH HOH C . 
DA 7 HOH 89  789 43   HOH HOH C . 
DA 7 HOH 90  790 170  HOH HOH C . 
DA 7 HOH 91  791 563  HOH HOH C . 
DA 7 HOH 92  792 979  HOH HOH C . 
DA 7 HOH 93  793 424  HOH HOH C . 
DA 7 HOH 94  794 327  HOH HOH C . 
DA 7 HOH 95  795 58   HOH HOH C . 
DA 7 HOH 96  796 310  HOH HOH C . 
DA 7 HOH 97  797 334  HOH HOH C . 
DA 7 HOH 98  798 540  HOH HOH C . 
DA 7 HOH 99  799 878  HOH HOH C . 
DA 7 HOH 100 800 682  HOH HOH C . 
DA 7 HOH 101 801 690  HOH HOH C . 
DA 7 HOH 102 802 541  HOH HOH C . 
DA 7 HOH 103 803 679  HOH HOH C . 
DA 7 HOH 104 804 885  HOH HOH C . 
DA 7 HOH 105 805 833  HOH HOH C . 
DA 7 HOH 106 806 926  HOH HOH C . 
DA 7 HOH 107 807 520  HOH HOH C . 
DA 7 HOH 108 808 592  HOH HOH C . 
DA 7 HOH 109 809 434  HOH HOH C . 
DA 7 HOH 110 810 292  HOH HOH C . 
DA 7 HOH 111 811 764  HOH HOH C . 
DA 7 HOH 112 812 21   HOH HOH C . 
DA 7 HOH 113 813 384  HOH HOH C . 
DA 7 HOH 114 814 714  HOH HOH C . 
DA 7 HOH 115 815 201  HOH HOH C . 
DA 7 HOH 116 816 526  HOH HOH C . 
DA 7 HOH 117 817 581  HOH HOH C . 
DA 7 HOH 118 818 938  HOH HOH C . 
DA 7 HOH 119 819 713  HOH HOH C . 
DA 7 HOH 120 820 800  HOH HOH C . 
DA 7 HOH 121 821 7    HOH HOH C . 
DA 7 HOH 122 822 551  HOH HOH C . 
DA 7 HOH 123 823 603  HOH HOH C . 
DA 7 HOH 124 824 95   HOH HOH C . 
DA 7 HOH 125 825 283  HOH HOH C . 
DA 7 HOH 126 826 359  HOH HOH C . 
DA 7 HOH 127 827 143  HOH HOH C . 
DA 7 HOH 128 828 664  HOH HOH C . 
DA 7 HOH 129 829 612  HOH HOH C . 
DA 7 HOH 130 830 178  HOH HOH C . 
DA 7 HOH 131 831 328  HOH HOH C . 
DA 7 HOH 132 832 377  HOH HOH C . 
DA 7 HOH 133 833 935  HOH HOH C . 
DA 7 HOH 134 834 233  HOH HOH C . 
DA 7 HOH 135 835 66   HOH HOH C . 
DA 7 HOH 136 836 806  HOH HOH C . 
DA 7 HOH 137 837 536  HOH HOH C . 
DA 7 HOH 138 838 590  HOH HOH C . 
DA 7 HOH 139 839 1029 HOH HOH C . 
DA 7 HOH 140 840 437  HOH HOH C . 
DA 7 HOH 141 841 446  HOH HOH C . 
DA 7 HOH 142 842 268  HOH HOH C . 
DA 7 HOH 143 843 572  HOH HOH C . 
DA 7 HOH 144 844 316  HOH HOH C . 
DA 7 HOH 145 845 185  HOH HOH C . 
DA 7 HOH 146 846 637  HOH HOH C . 
DA 7 HOH 147 847 199  HOH HOH C . 
DA 7 HOH 148 848 580  HOH HOH C . 
DA 7 HOH 149 849 411  HOH HOH C . 
DA 7 HOH 150 850 340  HOH HOH C . 
DA 7 HOH 151 851 775  HOH HOH C . 
DA 7 HOH 152 852 207  HOH HOH C . 
DA 7 HOH 153 853 390  HOH HOH C . 
DA 7 HOH 154 854 265  HOH HOH C . 
DA 7 HOH 155 855 379  HOH HOH C . 
DA 7 HOH 156 856 426  HOH HOH C . 
DA 7 HOH 157 857 907  HOH HOH C . 
DA 7 HOH 158 858 1017 HOH HOH C . 
DA 7 HOH 159 859 741  HOH HOH C . 
DA 7 HOH 160 860 803  HOH HOH C . 
DA 7 HOH 161 861 604  HOH HOH C . 
DA 7 HOH 162 862 573  HOH HOH C . 
DA 7 HOH 163 863 655  HOH HOH C . 
DA 7 HOH 164 864 231  HOH HOH C . 
DA 7 HOH 165 865 751  HOH HOH C . 
DA 7 HOH 166 866 872  HOH HOH C . 
DA 7 HOH 167 867 692  HOH HOH C . 
DA 7 HOH 168 868 822  HOH HOH C . 
DA 7 HOH 169 869 483  HOH HOH C . 
DA 7 HOH 170 870 839  HOH HOH C . 
DA 7 HOH 171 871 478  HOH HOH C . 
DA 7 HOH 172 872 738  HOH HOH C . 
DA 7 HOH 173 873 471  HOH HOH C . 
DA 7 HOH 174 874 914  HOH HOH C . 
DA 7 HOH 175 875 757  HOH HOH C . 
DA 7 HOH 176 876 1015 HOH HOH C . 
DA 7 HOH 177 877 901  HOH HOH C . 
DA 7 HOH 178 878 689  HOH HOH C . 
DA 7 HOH 179 879 743  HOH HOH C . 
DA 7 HOH 180 880 784  HOH HOH C . 
DA 7 HOH 181 881 973  HOH HOH C . 
DA 7 HOH 182 882 966  HOH HOH C . 
DA 7 HOH 183 883 860  HOH HOH C . 
DA 7 HOH 184 884 862  HOH HOH C . 
DA 7 HOH 185 885 476  HOH HOH C . 
DA 7 HOH 186 886 835  HOH HOH C . 
DA 7 HOH 187 887 849  HOH HOH C . 
DA 7 HOH 188 888 745  HOH HOH C . 
EA 7 HOH 1   701 756  HOH HOH D . 
EA 7 HOH 2   702 848  HOH HOH D . 
EA 7 HOH 3   703 865  HOH HOH D . 
EA 7 HOH 4   704 101  HOH HOH D . 
EA 7 HOH 5   705 1022 HOH HOH D . 
EA 7 HOH 6   706 588  HOH HOH D . 
EA 7 HOH 7   707 586  HOH HOH D . 
EA 7 HOH 8   708 636  HOH HOH D . 
EA 7 HOH 9   709 720  HOH HOH D . 
EA 7 HOH 10  710 640  HOH HOH D . 
EA 7 HOH 11  711 55   HOH HOH D . 
EA 7 HOH 12  712 198  HOH HOH D . 
EA 7 HOH 13  713 987  HOH HOH D . 
EA 7 HOH 14  714 624  HOH HOH D . 
EA 7 HOH 15  715 786  HOH HOH D . 
EA 7 HOH 16  716 173  HOH HOH D . 
EA 7 HOH 17  717 755  HOH HOH D . 
EA 7 HOH 18  718 1024 HOH HOH D . 
EA 7 HOH 19  719 693  HOH HOH D . 
EA 7 HOH 20  720 993  HOH HOH D . 
EA 7 HOH 21  721 378  HOH HOH D . 
EA 7 HOH 22  722 26   HOH HOH D . 
EA 7 HOH 23  723 286  HOH HOH D . 
EA 7 HOH 24  724 516  HOH HOH D . 
EA 7 HOH 25  725 994  HOH HOH D . 
EA 7 HOH 26  726 60   HOH HOH D . 
EA 7 HOH 27  727 214  HOH HOH D . 
EA 7 HOH 28  728 1027 HOH HOH D . 
EA 7 HOH 29  729 868  HOH HOH D . 
EA 7 HOH 30  730 904  HOH HOH D . 
EA 7 HOH 31  731 204  HOH HOH D . 
EA 7 HOH 32  732 151  HOH HOH D . 
EA 7 HOH 33  733 869  HOH HOH D . 
EA 7 HOH 34  734 74   HOH HOH D . 
EA 7 HOH 35  735 651  HOH HOH D . 
EA 7 HOH 36  736 961  HOH HOH D . 
EA 7 HOH 37  737 53   HOH HOH D . 
EA 7 HOH 38  738 700  HOH HOH D . 
EA 7 HOH 39  739 251  HOH HOH D . 
EA 7 HOH 40  740 917  HOH HOH D . 
EA 7 HOH 41  741 181  HOH HOH D . 
EA 7 HOH 42  742 38   HOH HOH D . 
EA 7 HOH 43  743 62   HOH HOH D . 
EA 7 HOH 44  744 845  HOH HOH D . 
EA 7 HOH 45  745 230  HOH HOH D . 
EA 7 HOH 46  746 27   HOH HOH D . 
EA 7 HOH 47  747 48   HOH HOH D . 
EA 7 HOH 48  748 410  HOH HOH D . 
EA 7 HOH 49  749 972  HOH HOH D . 
EA 7 HOH 50  750 593  HOH HOH D . 
EA 7 HOH 51  751 19   HOH HOH D . 
EA 7 HOH 52  752 1028 HOH HOH D . 
EA 7 HOH 53  753 777  HOH HOH D . 
EA 7 HOH 54  754 47   HOH HOH D . 
EA 7 HOH 55  755 383  HOH HOH D . 
EA 7 HOH 56  756 1016 HOH HOH D . 
EA 7 HOH 57  757 496  HOH HOH D . 
EA 7 HOH 58  758 63   HOH HOH D . 
EA 7 HOH 59  759 217  HOH HOH D . 
EA 7 HOH 60  760 852  HOH HOH D . 
EA 7 HOH 61  761 432  HOH HOH D . 
EA 7 HOH 62  762 314  HOH HOH D . 
EA 7 HOH 63  763 241  HOH HOH D . 
EA 7 HOH 64  764 704  HOH HOH D . 
EA 7 HOH 65  765 220  HOH HOH D . 
EA 7 HOH 66  766 497  HOH HOH D . 
EA 7 HOH 67  767 761  HOH HOH D . 
EA 7 HOH 68  768 5    HOH HOH D . 
EA 7 HOH 69  769 565  HOH HOH D . 
EA 7 HOH 70  770 613  HOH HOH D . 
EA 7 HOH 71  771 559  HOH HOH D . 
EA 7 HOH 72  772 642  HOH HOH D . 
EA 7 HOH 73  773 710  HOH HOH D . 
EA 7 HOH 74  774 2    HOH HOH D . 
EA 7 HOH 75  775 89   HOH HOH D . 
EA 7 HOH 76  776 912  HOH HOH D . 
EA 7 HOH 77  777 897  HOH HOH D . 
EA 7 HOH 78  778 97   HOH HOH D . 
EA 7 HOH 79  779 893  HOH HOH D . 
EA 7 HOH 80  780 409  HOH HOH D . 
EA 7 HOH 81  781 440  HOH HOH D . 
EA 7 HOH 82  782 673  HOH HOH D . 
EA 7 HOH 83  783 463  HOH HOH D . 
EA 7 HOH 84  784 344  HOH HOH D . 
EA 7 HOH 85  785 701  HOH HOH D . 
EA 7 HOH 86  786 589  HOH HOH D . 
EA 7 HOH 87  787 31   HOH HOH D . 
EA 7 HOH 88  788 20   HOH HOH D . 
EA 7 HOH 89  789 119  HOH HOH D . 
EA 7 HOH 90  790 724  HOH HOH D . 
EA 7 HOH 91  791 435  HOH HOH D . 
EA 7 HOH 92  792 570  HOH HOH D . 
EA 7 HOH 93  793 709  HOH HOH D . 
EA 7 HOH 94  794 549  HOH HOH D . 
EA 7 HOH 95  795 195  HOH HOH D . 
EA 7 HOH 96  796 473  HOH HOH D . 
EA 7 HOH 97  797 16   HOH HOH D . 
EA 7 HOH 98  798 77   HOH HOH D . 
EA 7 HOH 99  799 157  HOH HOH D . 
EA 7 HOH 100 800 614  HOH HOH D . 
EA 7 HOH 101 801 242  HOH HOH D . 
EA 7 HOH 102 802 452  HOH HOH D . 
EA 7 HOH 103 803 282  HOH HOH D . 
EA 7 HOH 104 804 461  HOH HOH D . 
EA 7 HOH 105 805 964  HOH HOH D . 
EA 7 HOH 106 806 228  HOH HOH D . 
EA 7 HOH 107 807 331  HOH HOH D . 
EA 7 HOH 108 808 102  HOH HOH D . 
EA 7 HOH 109 809 244  HOH HOH D . 
EA 7 HOH 110 810 433  HOH HOH D . 
EA 7 HOH 111 811 760  HOH HOH D . 
EA 7 HOH 112 812 902  HOH HOH D . 
EA 7 HOH 113 813 213  HOH HOH D . 
EA 7 HOH 114 814 462  HOH HOH D . 
EA 7 HOH 115 815 430  HOH HOH D . 
EA 7 HOH 116 816 870  HOH HOH D . 
EA 7 HOH 117 817 595  HOH HOH D . 
EA 7 HOH 118 818 76   HOH HOH D . 
EA 7 HOH 119 819 491  HOH HOH D . 
EA 7 HOH 120 820 36   HOH HOH D . 
EA 7 HOH 121 821 677  HOH HOH D . 
EA 7 HOH 122 822 457  HOH HOH D . 
EA 7 HOH 123 823 270  HOH HOH D . 
EA 7 HOH 124 824 723  HOH HOH D . 
EA 7 HOH 125 825 275  HOH HOH D . 
EA 7 HOH 126 826 146  HOH HOH D . 
EA 7 HOH 127 827 290  HOH HOH D . 
EA 7 HOH 128 828 176  HOH HOH D . 
EA 7 HOH 129 829 184  HOH HOH D . 
EA 7 HOH 130 830 521  HOH HOH D . 
EA 7 HOH 131 831 874  HOH HOH D . 
EA 7 HOH 132 832 263  HOH HOH D . 
EA 7 HOH 133 833 991  HOH HOH D . 
EA 7 HOH 134 834 728  HOH HOH D . 
EA 7 HOH 135 835 307  HOH HOH D . 
EA 7 HOH 136 836 442  HOH HOH D . 
EA 7 HOH 137 837 468  HOH HOH D . 
EA 7 HOH 138 838 495  HOH HOH D . 
EA 7 HOH 139 839 576  HOH HOH D . 
EA 7 HOH 140 840 523  HOH HOH D . 
EA 7 HOH 141 841 109  HOH HOH D . 
EA 7 HOH 142 842 566  HOH HOH D . 
EA 7 HOH 143 843 558  HOH HOH D . 
EA 7 HOH 144 844 308  HOH HOH D . 
EA 7 HOH 145 845 168  HOH HOH D . 
EA 7 HOH 146 846 61   HOH HOH D . 
EA 7 HOH 147 847 129  HOH HOH D . 
EA 7 HOH 148 848 158  HOH HOH D . 
EA 7 HOH 149 849 364  HOH HOH D . 
EA 7 HOH 150 850 167  HOH HOH D . 
EA 7 HOH 151 851 533  HOH HOH D . 
EA 7 HOH 152 852 17   HOH HOH D . 
EA 7 HOH 153 853 370  HOH HOH D . 
EA 7 HOH 154 854 302  HOH HOH D . 
EA 7 HOH 155 855 414  HOH HOH D . 
EA 7 HOH 156 856 887  HOH HOH D . 
EA 7 HOH 157 857 279  HOH HOH D . 
EA 7 HOH 158 858 238  HOH HOH D . 
EA 7 HOH 159 859 429  HOH HOH D . 
EA 7 HOH 160 860 770  HOH HOH D . 
EA 7 HOH 161 861 234  HOH HOH D . 
EA 7 HOH 162 862 890  HOH HOH D . 
EA 7 HOH 163 863 995  HOH HOH D . 
EA 7 HOH 164 864 676  HOH HOH D . 
EA 7 HOH 165 865 362  HOH HOH D . 
EA 7 HOH 166 866 49   HOH HOH D . 
EA 7 HOH 167 867 505  HOH HOH D . 
EA 7 HOH 168 868 222  HOH HOH D . 
EA 7 HOH 169 869 356  HOH HOH D . 
EA 7 HOH 170 870 152  HOH HOH D . 
EA 7 HOH 171 871 602  HOH HOH D . 
EA 7 HOH 172 872 166  HOH HOH D . 
EA 7 HOH 173 873 368  HOH HOH D . 
EA 7 HOH 174 874 272  HOH HOH D . 
EA 7 HOH 175 875 128  HOH HOH D . 
EA 7 HOH 176 876 749  HOH HOH D . 
EA 7 HOH 177 877 155  HOH HOH D . 
EA 7 HOH 178 878 985  HOH HOH D . 
EA 7 HOH 179 879 629  HOH HOH D . 
EA 7 HOH 180 880 320  HOH HOH D . 
EA 7 HOH 181 881 610  HOH HOH D . 
EA 7 HOH 182 882 702  HOH HOH D . 
EA 7 HOH 183 883 956  HOH HOH D . 
EA 7 HOH 184 884 606  HOH HOH D . 
EA 7 HOH 185 885 246  HOH HOH D . 
EA 7 HOH 186 886 671  HOH HOH D . 
EA 7 HOH 187 887 506  HOH HOH D . 
EA 7 HOH 188 888 530  HOH HOH D . 
EA 7 HOH 189 889 172  HOH HOH D . 
EA 7 HOH 190 890 553  HOH HOH D . 
EA 7 HOH 191 891 550  HOH HOH D . 
EA 7 HOH 192 892 650  HOH HOH D . 
EA 7 HOH 193 893 974  HOH HOH D . 
EA 7 HOH 194 894 171  HOH HOH D . 
EA 7 HOH 195 895 611  HOH HOH D . 
EA 7 HOH 196 896 387  HOH HOH D . 
EA 7 HOH 197 897 925  HOH HOH D . 
EA 7 HOH 198 898 1020 HOH HOH D . 
EA 7 HOH 199 899 694  HOH HOH D . 
EA 7 HOH 200 900 923  HOH HOH D . 
EA 7 HOH 201 901 542  HOH HOH D . 
EA 7 HOH 202 902 978  HOH HOH D . 
EA 7 HOH 203 903 190  HOH HOH D . 
EA 7 HOH 204 904 298  HOH HOH D . 
EA 7 HOH 205 905 419  HOH HOH D . 
EA 7 HOH 206 906 118  HOH HOH D . 
EA 7 HOH 207 907 284  HOH HOH D . 
EA 7 HOH 208 908 896  HOH HOH D . 
EA 7 HOH 209 909 722  HOH HOH D . 
EA 7 HOH 210 910 652  HOH HOH D . 
EA 7 HOH 211 911 82   HOH HOH D . 
EA 7 HOH 212 912 103  HOH HOH D . 
EA 7 HOH 213 913 1004 HOH HOH D . 
EA 7 HOH 214 914 952  HOH HOH D . 
EA 7 HOH 215 915 601  HOH HOH D . 
EA 7 HOH 216 916 894  HOH HOH D . 
EA 7 HOH 217 917 311  HOH HOH D . 
EA 7 HOH 218 918 543  HOH HOH D . 
EA 7 HOH 219 919 557  HOH HOH D . 
EA 7 HOH 220 920 348  HOH HOH D . 
EA 7 HOH 221 921 1023 HOH HOH D . 
EA 7 HOH 222 922 900  HOH HOH D . 
EA 7 HOH 223 923 350  HOH HOH D . 
EA 7 HOH 224 924 126  HOH HOH D . 
EA 7 HOH 225 925 120  HOH HOH D . 
EA 7 HOH 226 926 417  HOH HOH D . 
EA 7 HOH 227 927 661  HOH HOH D . 
EA 7 HOH 228 928 665  HOH HOH D . 
EA 7 HOH 229 929 881  HOH HOH D . 
EA 7 HOH 230 930 725  HOH HOH D . 
EA 7 HOH 231 931 277  HOH HOH D . 
EA 7 HOH 232 932 936  HOH HOH D . 
EA 7 HOH 233 933 507  HOH HOH D . 
EA 7 HOH 234 934 3    HOH HOH D . 
EA 7 HOH 235 935 232  HOH HOH D . 
EA 7 HOH 236 936 705  HOH HOH D . 
EA 7 HOH 237 937 882  HOH HOH D . 
EA 7 HOH 238 938 386  HOH HOH D . 
EA 7 HOH 239 939 470  HOH HOH D . 
EA 7 HOH 240 940 911  HOH HOH D . 
EA 7 HOH 241 941 458  HOH HOH D . 
EA 7 HOH 242 942 953  HOH HOH D . 
EA 7 HOH 243 943 854  HOH HOH D . 
EA 7 HOH 244 944 481  HOH HOH D . 
EA 7 HOH 245 945 838  HOH HOH D . 
EA 7 HOH 246 946 990  HOH HOH D . 
EA 7 HOH 247 947 319  HOH HOH D . 
EA 7 HOH 248 948 739  HOH HOH D . 
EA 7 HOH 249 949 475  HOH HOH D . 
EA 7 HOH 250 950 910  HOH HOH D . 
EA 7 HOH 251 951 989  HOH HOH D . 
EA 7 HOH 252 952 486  HOH HOH D . 
EA 7 HOH 253 953 841  HOH HOH D . 
EA 7 HOH 254 954 600  HOH HOH D . 
EA 7 HOH 255 955 427  HOH HOH D . 
EA 7 HOH 256 956 699  HOH HOH D . 
EA 7 HOH 257 957 697  HOH HOH D . 
EA 7 HOH 258 958 780  HOH HOH D . 
EA 7 HOH 259 959 402  HOH HOH D . 
EA 7 HOH 260 960 836  HOH HOH D . 
EA 7 HOH 261 961 957  HOH HOH D . 
EA 7 HOH 262 962 658  HOH HOH D . 
EA 7 HOH 263 963 608  HOH HOH D . 
EA 7 HOH 264 964 737  HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 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                     9G4N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     114.854 
_cell.length_a_esd                 ? 
_cell.length_b                     127.548 
_cell.length_b_esd                 ? 
_cell.length_c                     171.411 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9G4N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G4N 
_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             2.55 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.76 
_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    '0,1 M Sodium Malonate pH4, 10% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_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 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-10-13 
_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   0.9677 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9677 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G4N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.32 
_reflns.d_resolution_low                               47.71 
_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                                     109278 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.3 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.99 
_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                                0.204 
_reflns.pdbx_Rpim_I_all                                0.069 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       929935 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.192 
_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                                    2.32 
_reflns_shell.d_res_low                                     2.40 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           94107 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             10641 
_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                               8.8 
_reflns_shell.pdbx_chi_squared                              0.82 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               2.180 
_reflns_shell.pdbx_Rpim_I_all                               0.720 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.629 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.056 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.53 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][2]                            -0.27 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.26 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               36.698 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.919 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_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                                 9G4N 
_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                            2.32 
_refine.ls_d_res_low                             47.71 
_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                     103930 
_refine.ls_number_reflns_R_free                  5264 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20659 
_refine.ls_R_factor_R_free                       0.24718 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20453 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.369 
_refine.pdbx_overall_ESU_R_Free                  0.244 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             14.011 
_refine.overall_SU_ML                            0.171 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.32 
_refine_hist.d_res_low                        47.71 
_refine_hist.number_atoms_solvent             969 
_refine_hist.number_atoms_total               18185 
_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        16954 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         262 
_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' ? 0.009  0.012  17616 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  16304 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.702  1.821  23812 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.575  1.776  37872 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.663  5.000  2107  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.285  5.000  44    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.702 10.000 3103  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.078  0.200  2584  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.020  20144 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  3832  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.694  1.994  8434  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.693  1.994  8434  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 2.602  3.579  10536 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.602  3.580  10537 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.264  2.226  9182  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.264  2.227  9183  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.516  3.981  13276 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.148  21.33  19896 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.130  20.61  19684 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.320 
_refine_ls_shell.d_res_low                        2.380 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             338 
_refine_ls_shell.number_reflns_R_work             7657 
_refine_ls_shell.percent_reflns_obs               99.99 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.581 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.622 
# 
_struct.entry_id                     9G4N 
_struct.title                        
'Glycoside Hydrolase Family 157 from Labilibaculum antarcticum (LaGH157) E224A mutant in complex with Laminaritriose and Glucose' 
_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        9G4N 
_struct_keywords.text            'GH157, endo-1, 3(4)-beta-glucanase, Labilibaculum antarcticum, glycoside hydrolase, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 2 ? 
I  N N 3 ? 
J  N N 4 ? 
K  N N 5 ? 
L  N N 3 ? 
M  N N 4 ? 
N  N N 5 ? 
O  N N 3 ? 
P  N N 5 ? 
Q  N N 5 ? 
R  N N 3 ? 
S  N N 6 ? 
T  N N 5 ? 
U  N N 4 ? 
V  N N 5 ? 
W  N N 3 ? 
X  N N 5 ? 
Y  N N 5 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 7 ? 
CA N N 7 ? 
DA N N 7 ? 
EA N N 7 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A1Y1CQ89_9BACT 
_struct_ref.pdbx_db_accession          A0A1Y1CQ89 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;QSKTKIELKDNWYHLDGEKYFIKAIGYEIGARPGQAPYEDERKDELELMKFDLENIKEGGYNTIRTWSQYSENQLKLVQE
SGLKLIMGIDIKPEEDYGDPEFVKDSEIELKRVLNYAKKYDCIITYLVINEPQTDHIHSVTGKAFVDLMNTLINIIHKGH
PGIPVTLSANAMISDYMDESIFDVYAYNCYDHNEGQTATMGFKDYIKGLNELNGLDKPFITTEFGYSVSPEGGNGQYGSN
TLKQQSDGLISNYRDLIDAGAVGMCPFYYADGWWKGGEKSDHSLNQPEEWFGFWGYSDLNDKYGTPRPVWFAMRDYMKGL
IISPKNKSIHTNTKIPLELYNDKDVKKVVVKFRDKVIYSKNITSEGYMADELTIDPVGIEDMELAFEFYDSDNKIIKNES
INILASKTAFELPELTIEVTPEKDLNEGKIASIKTKIETSENFTLLDDLKISYNTHLGWAIGSQASVSISDQLDKKIITS
ENFFNIPDNCWVVNASAGISVRYGKFTFKIHDQKIIYRGDWAKEVGRK
;
_struct_ref.pdbx_align_begin           22 
# 
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 9G4N A 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
2 1 9G4N B 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
3 1 9G4N C 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
4 1 9G4N D 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
# 
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 9G4N MET A 1   ? UNP A0A1Y1CQ89 ?   ?   'initiating methionine' 1   1  
1 9G4N ALA A 224 ? UNP A0A1Y1CQ89 GLU 244 'engineered mutation'   224 2  
1 9G4N LEU A 530 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        530 3  
1 9G4N GLU A 531 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        531 4  
1 9G4N HIS A 532 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        532 5  
1 9G4N HIS A 533 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        533 6  
1 9G4N HIS A 534 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        534 7  
1 9G4N HIS A 535 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        535 8  
1 9G4N HIS A 536 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        536 9  
1 9G4N HIS A 537 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        537 10 
2 9G4N MET B 1   ? UNP A0A1Y1CQ89 ?   ?   'initiating methionine' 1   11 
2 9G4N ALA B 224 ? UNP A0A1Y1CQ89 GLU 244 'engineered mutation'   224 12 
2 9G4N LEU B 530 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        530 13 
2 9G4N GLU B 531 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        531 14 
2 9G4N HIS B 532 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        532 15 
2 9G4N HIS B 533 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        533 16 
2 9G4N HIS B 534 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        534 17 
2 9G4N HIS B 535 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        535 18 
2 9G4N HIS B 536 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        536 19 
2 9G4N HIS B 537 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        537 20 
3 9G4N MET C 1   ? UNP A0A1Y1CQ89 ?   ?   'initiating methionine' 1   21 
3 9G4N ALA C 224 ? UNP A0A1Y1CQ89 GLU 244 'engineered mutation'   224 22 
3 9G4N LEU C 530 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        530 23 
3 9G4N GLU C 531 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        531 24 
3 9G4N HIS C 532 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        532 25 
3 9G4N HIS C 533 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        533 26 
3 9G4N HIS C 534 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        534 27 
3 9G4N HIS C 535 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        535 28 
3 9G4N HIS C 536 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        536 29 
3 9G4N HIS C 537 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        537 30 
4 9G4N MET D 1   ? UNP A0A1Y1CQ89 ?   ?   'initiating methionine' 1   31 
4 9G4N ALA D 224 ? UNP A0A1Y1CQ89 GLU 244 'engineered mutation'   224 32 
4 9G4N LEU D 530 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        530 33 
4 9G4N GLU D 531 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        531 34 
4 9G4N HIS D 532 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        532 35 
4 9G4N HIS D 533 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        533 36 
4 9G4N HIS D 534 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        534 37 
4 9G4N HIS D 535 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        535 38 
4 9G4N HIS D 536 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        536 39 
4 9G4N HIS D 537 ? UNP A0A1Y1CQ89 ?   ?   'expression tag'        537 40 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
3 author_defined_assembly ? monomeric 1 
4 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E,I,J,K,BA          
2 1 B,F,L,M,N,O,P,Q,CA    
3 1 C,G,R,S,T,DA          
4 1 D,H,U,V,W,X,Y,Z,AA,EA 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 46  ? GLY A 60  ? GLU A 46  GLY A 60  1 ? 15 
HELX_P HELX_P2  AA2 SER A 72  ? GLY A 83  ? SER A 72  GLY A 83  1 ? 12 
HELX_P HELX_P3  AA3 ASP A 100 ? LYS A 119 ? ASP A 100 LYS A 119 1 ? 20 
HELX_P HELX_P4  AA4 GLN A 134 ? THR A 142 ? GLN A 134 THR A 142 1 ? 9  
HELX_P HELX_P5  AA5 THR A 142 ? HIS A 161 ? THR A 142 HIS A 161 1 ? 20 
HELX_P HELX_P6  AA6 GLY A 196 ? MET A 201 ? GLY A 196 MET A 201 1 ? 6  
HELX_P HELX_P7  AA7 GLY A 202 ? GLY A 215 ? GLY A 202 GLY A 215 1 ? 14 
HELX_P HELX_P8  AA8 THR A 242 ? ALA A 260 ? THR A 242 ALA A 260 1 ? 19 
HELX_P HELX_P9  AA9 GLY A 273 ? GLY A 278 ? GLY A 273 GLY A 278 5 ? 6  
HELX_P HELX_P10 AB1 GLN A 287 ? TRP A 291 ? GLN A 287 TRP A 291 5 ? 5  
HELX_P HELX_P11 AB2 ARG A 308 ? MET A 318 ? ARG A 308 MET A 318 1 ? 11 
HELX_P HELX_P12 AB3 ASP A 425 ? GLY A 429 ? ASP A 425 GLY A 429 5 ? 5  
HELX_P HELX_P13 AB4 ILE A 470 ? LEU A 474 ? ILE A 470 LEU A 474 5 ? 5  
HELX_P HELX_P14 AB5 GLU B 46  ? GLY B 60  ? GLU B 46  GLY B 60  1 ? 15 
HELX_P HELX_P15 AB6 SER B 72  ? GLY B 83  ? SER B 72  GLY B 83  1 ? 12 
HELX_P HELX_P16 AB7 ASP B 100 ? LYS B 119 ? ASP B 100 LYS B 119 1 ? 20 
HELX_P HELX_P17 AB8 GLN B 134 ? THR B 142 ? GLN B 134 THR B 142 1 ? 9  
HELX_P HELX_P18 AB9 THR B 142 ? HIS B 161 ? THR B 142 HIS B 161 1 ? 20 
HELX_P HELX_P19 AC1 ASN B 171 ? ASP B 176 ? ASN B 171 ASP B 176 1 ? 6  
HELX_P HELX_P20 AC2 GLY B 196 ? MET B 201 ? GLY B 196 MET B 201 1 ? 6  
HELX_P HELX_P21 AC3 GLY B 202 ? GLY B 215 ? GLY B 202 GLY B 215 1 ? 14 
HELX_P HELX_P22 AC4 THR B 242 ? ALA B 260 ? THR B 242 ALA B 260 1 ? 19 
HELX_P HELX_P23 AC5 GLY B 273 ? GLY B 278 ? GLY B 273 GLY B 278 5 ? 6  
HELX_P HELX_P24 AC6 GLN B 287 ? TRP B 291 ? GLN B 287 TRP B 291 5 ? 5  
HELX_P HELX_P25 AC7 ARG B 308 ? MET B 318 ? ARG B 308 MET B 318 1 ? 11 
HELX_P HELX_P26 AC8 ASP B 425 ? GLY B 429 ? ASP B 425 GLY B 429 5 ? 5  
HELX_P HELX_P27 AC9 SER B 471 ? LEU B 474 ? SER B 471 LEU B 474 5 ? 4  
HELX_P HELX_P28 AD1 GLU C 46  ? GLY C 60  ? GLU C 46  GLY C 60  1 ? 15 
HELX_P HELX_P29 AD2 SER C 72  ? GLY C 83  ? SER C 72  GLY C 83  1 ? 12 
HELX_P HELX_P30 AD3 ASP C 100 ? LYS C 119 ? ASP C 100 LYS C 119 1 ? 20 
HELX_P HELX_P31 AD4 GLN C 134 ? THR C 142 ? GLN C 134 THR C 142 1 ? 9  
HELX_P HELX_P32 AD5 THR C 142 ? HIS C 161 ? THR C 142 HIS C 161 1 ? 20 
HELX_P HELX_P33 AD6 GLY C 196 ? MET C 201 ? GLY C 196 MET C 201 1 ? 6  
HELX_P HELX_P34 AD7 GLY C 202 ? GLY C 215 ? GLY C 202 GLY C 215 1 ? 14 
HELX_P HELX_P35 AD8 THR C 242 ? ALA C 260 ? THR C 242 ALA C 260 1 ? 19 
HELX_P HELX_P36 AD9 GLY C 273 ? GLY C 278 ? GLY C 273 GLY C 278 5 ? 6  
HELX_P HELX_P37 AE1 GLN C 287 ? TRP C 291 ? GLN C 287 TRP C 291 5 ? 5  
HELX_P HELX_P38 AE2 ARG C 308 ? LYS C 319 ? ARG C 308 LYS C 319 1 ? 12 
HELX_P HELX_P39 AE3 ASP C 425 ? GLY C 429 ? ASP C 425 GLY C 429 5 ? 5  
HELX_P HELX_P40 AE4 ILE C 470 ? LEU C 474 ? ILE C 470 LEU C 474 5 ? 5  
HELX_P HELX_P41 AE5 GLU D 46  ? GLY D 60  ? GLU D 46  GLY D 60  1 ? 15 
HELX_P HELX_P42 AE6 SER D 72  ? GLY D 83  ? SER D 72  GLY D 83  1 ? 12 
HELX_P HELX_P43 AE7 ASP D 100 ? LYS D 119 ? ASP D 100 LYS D 119 1 ? 20 
HELX_P HELX_P44 AE8 GLN D 134 ? THR D 142 ? GLN D 134 THR D 142 1 ? 9  
HELX_P HELX_P45 AE9 THR D 142 ? HIS D 161 ? THR D 142 HIS D 161 1 ? 20 
HELX_P HELX_P46 AF1 ASN D 171 ? ASP D 176 ? ASN D 171 ASP D 176 1 ? 6  
HELX_P HELX_P47 AF2 GLY D 196 ? MET D 201 ? GLY D 196 MET D 201 1 ? 6  
HELX_P HELX_P48 AF3 GLY D 202 ? GLY D 215 ? GLY D 202 GLY D 215 1 ? 14 
HELX_P HELX_P49 AF4 THR D 242 ? ALA D 260 ? THR D 242 ALA D 260 1 ? 19 
HELX_P HELX_P50 AF5 GLY D 273 ? GLY D 278 ? GLY D 273 GLY D 278 5 ? 6  
HELX_P HELX_P51 AF6 GLN D 287 ? TRP D 291 ? GLN D 287 TRP D 291 5 ? 5  
HELX_P HELX_P52 AF7 ARG D 308 ? MET D 318 ? ARG D 308 MET D 318 1 ? 11 
HELX_P HELX_P53 AF8 ASP D 425 ? GLY D 429 ? ASP D 425 GLY D 429 5 ? 5  
HELX_P HELX_P54 AF9 ILE D 470 ? LEU D 474 ? ILE D 470 LEU D 474 5 ? 5  
# 
_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 
covale1 covale both ? E BGC . O3 ? ? ? 1_555 E BGC . C1 ? ? E BGC 1 E BGC 2 1_555 ? ? ? ? ? ? ? 1.402 ? ? 
covale2 covale both ? E BGC . O3 ? ? ? 1_555 E BGC . C1 ? ? E BGC 2 E BGC 3 1_555 ? ? ? ? ? ? ? 1.392 ? ? 
covale3 covale both ? F BGC . O3 ? ? ? 1_555 F BGC . C1 ? ? F BGC 1 F BGC 2 1_555 ? ? ? ? ? ? ? 1.386 ? ? 
covale4 covale both ? F BGC . O3 ? ? ? 1_555 F BGC . C1 ? ? F BGC 2 F BGC 3 1_555 ? ? ? ? ? ? ? 1.399 ? ? 
covale5 covale both ? G BGC . O3 ? ? ? 1_555 G BGC . C1 ? ? G BGC 1 G BGC 2 1_555 ? ? ? ? ? ? ? 1.403 ? ? 
covale6 covale both ? G BGC . O3 ? ? ? 1_555 G BGC . C1 ? ? G BGC 2 G BGC 3 1_555 ? ? ? ? ? ? ? 1.395 ? ? 
covale7 covale both ? H BGC . O3 ? ? ? 1_555 H BGC . C1 ? ? H BGC 1 H BGC 2 1_555 ? ? ? ? ? ? ? 1.393 ? ? 
covale8 covale both ? H BGC . O3 ? ? ? 1_555 H BGC . C1 ? ? H BGC 2 H BGC 3 1_555 ? ? ? ? ? ? ? 1.389 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  PHE 268 A . ? PHE 268 A TYR 269 A ? TYR 269 A 1 -4.63  
2  SER 324 A . ? SER 324 A PRO 325 A ? PRO 325 A 1 1.36   
3  THR 421 A . ? THR 421 A PRO 422 A ? PRO 422 A 1 -20.24 
4  PHE 268 B . ? PHE 268 B TYR 269 B ? TYR 269 B 1 -5.40  
5  SER 324 B . ? SER 324 B PRO 325 B ? PRO 325 B 1 -6.16  
6  THR 421 B . ? THR 421 B PRO 422 B ? PRO 422 B 1 -15.55 
7  PHE 268 C . ? PHE 268 C TYR 269 C ? TYR 269 C 1 -11.78 
8  SER 324 C . ? SER 324 C PRO 325 C ? PRO 325 C 1 0.24   
9  THR 421 C . ? THR 421 C PRO 422 C ? PRO 422 C 1 -23.79 
10 PHE 268 D . ? PHE 268 D TYR 269 D ? TYR 269 D 1 -2.27  
11 SER 324 D . ? SER 324 D PRO 325 D ? PRO 325 D 1 -6.81  
12 THR 421 D . ? THR 421 D PRO 422 D ? PRO 422 D 1 -13.94 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 5 ? 
AA7 ? 3 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 6 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 3 ? 
AB5 ? 5 ? 
AB6 ? 3 ? 
AB7 ? 4 ? 
AB8 ? 3 ? 
AB9 ? 3 ? 
AC1 ? 8 ? 
AC2 ? 2 ? 
AC3 ? 3 ? 
AC4 ? 5 ? 
AC5 ? 3 ? 
AC6 ? 4 ? 
AC7 ? 3 ? 
AC8 ? 6 ? 
AC9 ? 2 ? 
AD1 ? 2 ? 
AD2 ? 3 ? 
AD3 ? 5 ? 
AD4 ? 3 ? 
AD5 ? 4 ? 
AD6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA3 1 2 ? parallel      
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? parallel      
AB2 1 2 ? parallel      
AB3 1 2 ? anti-parallel 
AB4 1 2 ? anti-parallel 
AB4 2 3 ? anti-parallel 
AB5 1 2 ? parallel      
AB5 2 3 ? anti-parallel 
AB5 3 4 ? anti-parallel 
AB5 4 5 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? parallel      
AC1 3 4 ? parallel      
AC1 4 5 ? parallel      
AC1 5 6 ? parallel      
AC1 6 7 ? parallel      
AC1 7 8 ? parallel      
AC2 1 2 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC4 1 2 ? parallel      
AC4 2 3 ? anti-parallel 
AC4 3 4 ? anti-parallel 
AC4 4 5 ? anti-parallel 
AC5 1 2 ? anti-parallel 
AC5 2 3 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC6 3 4 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC8 1 2 ? parallel      
AC8 2 3 ? parallel      
AC8 3 4 ? parallel      
AC8 4 5 ? parallel      
AC8 5 6 ? parallel      
AC9 1 2 ? parallel      
AD1 1 2 ? anti-parallel 
AD2 1 2 ? anti-parallel 
AD2 2 3 ? anti-parallel 
AD3 1 2 ? parallel      
AD3 2 3 ? anti-parallel 
AD3 3 4 ? anti-parallel 
AD3 4 5 ? anti-parallel 
AD4 1 2 ? anti-parallel 
AD4 2 3 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD5 3 4 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 7   ? LYS A 10  ? ILE A 7   LYS A 10  
AA1 2 TRP A 13  ? LEU A 16  ? TRP A 13  LEU A 16  
AA1 3 GLU A 19  ? LYS A 20  ? GLU A 19  LYS A 20  
AA2 1 VAL A 166 ? SER A 169 ? VAL A 166 SER A 169 
AA2 2 ILE A 124 ? ASN A 131 ? ILE A 124 ASN A 131 
AA2 3 LYS A 85  ? GLY A 89  ? LYS A 85  GLY A 89  
AA2 4 THR A 64  ? ARG A 66  ? THR A 64  ARG A 66  
AA2 5 ILE A 23  ? GLY A 27  ? ILE A 23  GLY A 27  
AA2 6 GLY A 264 ? MET A 265 ? GLY A 264 MET A 265 
AA3 1 TYR A 186 ? ASN A 189 ? TYR A 186 ASN A 189 
AA3 2 PHE A 220 ? ALA A 224 ? PHE A 220 ALA A 224 
AA4 1 TRP A 295 ? GLY A 296 ? TRP A 295 GLY A 296 
AA4 2 THR A 306 ? PRO A 307 ? THR A 306 PRO A 307 
AA5 1 GLY A 320 ? SER A 324 ? GLY A 320 SER A 324 
AA5 2 LYS A 335 ? ASN A 342 ? LYS A 335 ASN A 342 
AA5 3 GLY A 367 ? THR A 374 ? GLY A 367 THR A 374 
AA6 1 SER A 329 ? HIS A 331 ? SER A 329 HIS A 331 
AA6 2 ILE A 396 ? ALA A 406 ? ILE A 396 ALA A 406 
AA6 3 GLU A 381 ? TYR A 390 ? GLU A 381 TYR A 390 
AA6 4 LYS A 348 ? PHE A 353 ? LYS A 348 PHE A 353 
AA6 5 LYS A 356 ? ASN A 362 ? LYS A 356 ASN A 362 
AA7 1 GLU A 415 ? THR A 421 ? GLU A 415 THR A 421 
AA7 2 ILE A 431 ? GLU A 439 ? ILE A 431 GLU A 439 
AA7 3 ILE A 478 ? ASN A 486 ? ILE A 478 ASN A 486 
AA8 1 SER A 464 ? VAL A 468 ? SER A 464 VAL A 468 
AA8 2 THR A 445 ? ASN A 455 ? THR A 445 ASN A 455 
AA8 3 VAL A 493 ? TYR A 504 ? VAL A 493 TYR A 504 
AA8 4 PHE A 507 ? TYR A 518 ? PHE A 507 TYR A 518 
AA9 1 ILE B 7   ? LYS B 10  ? ILE B 7   LYS B 10  
AA9 2 TRP B 13  ? LEU B 16  ? TRP B 13  LEU B 16  
AA9 3 GLU B 19  ? LYS B 20  ? GLU B 19  LYS B 20  
AB1 1 VAL B 166 ? SER B 169 ? VAL B 166 SER B 169 
AB1 2 ILE B 124 ? ASN B 131 ? ILE B 124 ASN B 131 
AB1 3 LYS B 85  ? GLY B 89  ? LYS B 85  GLY B 89  
AB1 4 THR B 64  ? ARG B 66  ? THR B 64  ARG B 66  
AB1 5 ILE B 23  ? GLY B 27  ? ILE B 23  GLY B 27  
AB1 6 GLY B 264 ? MET B 265 ? GLY B 264 MET B 265 
AB2 1 TYR B 186 ? ASN B 189 ? TYR B 186 ASN B 189 
AB2 2 PHE B 220 ? ALA B 224 ? PHE B 220 ALA B 224 
AB3 1 TRP B 295 ? GLY B 296 ? TRP B 295 GLY B 296 
AB3 2 THR B 306 ? PRO B 307 ? THR B 306 PRO B 307 
AB4 1 GLY B 320 ? SER B 324 ? GLY B 320 SER B 324 
AB4 2 LYS B 335 ? ASN B 342 ? LYS B 335 ASN B 342 
AB4 3 GLY B 367 ? THR B 374 ? GLY B 367 THR B 374 
AB5 1 SER B 329 ? HIS B 331 ? SER B 329 HIS B 331 
AB5 2 ILE B 396 ? ALA B 406 ? ILE B 396 ALA B 406 
AB5 3 GLU B 381 ? TYR B 390 ? GLU B 381 TYR B 390 
AB5 4 LYS B 348 ? PHE B 353 ? LYS B 348 PHE B 353 
AB5 5 LYS B 356 ? ASN B 362 ? LYS B 356 ASN B 362 
AB6 1 GLU B 415 ? THR B 421 ? GLU B 415 THR B 421 
AB6 2 ILE B 431 ? GLU B 439 ? ILE B 431 GLU B 439 
AB6 3 ILE B 478 ? ASN B 486 ? ILE B 478 ASN B 486 
AB7 1 THR B 445 ? LEU B 446 ? THR B 445 LEU B 446 
AB7 2 VAL B 493 ? TYR B 504 ? VAL B 493 TYR B 504 
AB7 3 ASP B 449 ? ASN B 455 ? ASP B 449 ASN B 455 
AB7 4 SER B 464 ? SER B 469 ? SER B 464 SER B 469 
AB8 1 THR B 445 ? LEU B 446 ? THR B 445 LEU B 446 
AB8 2 VAL B 493 ? TYR B 504 ? VAL B 493 TYR B 504 
AB8 3 PHE B 507 ? TYR B 518 ? PHE B 507 TYR B 518 
AB9 1 ILE C 7   ? LYS C 10  ? ILE C 7   LYS C 10  
AB9 2 TRP C 13  ? LEU C 16  ? TRP C 13  LEU C 16  
AB9 3 GLU C 19  ? LYS C 20  ? GLU C 19  LYS C 20  
AC1 1 VAL C 166 ? SER C 169 ? VAL C 166 SER C 169 
AC1 2 ILE C 124 ? ASN C 131 ? ILE C 124 ASN C 131 
AC1 3 LYS C 85  ? GLY C 89  ? LYS C 85  GLY C 89  
AC1 4 THR C 64  ? ARG C 66  ? THR C 64  ARG C 66  
AC1 5 ILE C 23  ? GLY C 27  ? ILE C 23  GLY C 27  
AC1 6 GLY C 264 ? MET C 265 ? GLY C 264 MET C 265 
AC1 7 PHE C 220 ? ALA C 224 ? PHE C 220 ALA C 224 
AC1 8 TYR C 186 ? ASN C 189 ? TYR C 186 ASN C 189 
AC2 1 TRP C 295 ? GLY C 296 ? TRP C 295 GLY C 296 
AC2 2 THR C 306 ? PRO C 307 ? THR C 306 PRO C 307 
AC3 1 GLY C 320 ? SER C 324 ? GLY C 320 SER C 324 
AC3 2 LYS C 335 ? ASN C 342 ? LYS C 335 ASN C 342 
AC3 3 GLY C 367 ? THR C 374 ? GLY C 367 THR C 374 
AC4 1 SER C 329 ? HIS C 331 ? SER C 329 HIS C 331 
AC4 2 ILE C 396 ? ALA C 406 ? ILE C 396 ALA C 406 
AC4 3 GLU C 381 ? TYR C 390 ? GLU C 381 TYR C 390 
AC4 4 LYS C 348 ? PHE C 353 ? LYS C 348 PHE C 353 
AC4 5 LYS C 356 ? ASN C 362 ? LYS C 356 ASN C 362 
AC5 1 GLU C 415 ? THR C 421 ? GLU C 415 THR C 421 
AC5 2 ILE C 431 ? GLU C 439 ? ILE C 431 GLU C 439 
AC5 3 ILE C 478 ? ASN C 486 ? ILE C 478 ASN C 486 
AC6 1 SER C 464 ? VAL C 468 ? SER C 464 VAL C 468 
AC6 2 THR C 445 ? ASN C 455 ? THR C 445 ASN C 455 
AC6 3 VAL C 493 ? TYR C 504 ? VAL C 493 TYR C 504 
AC6 4 PHE C 507 ? TYR C 518 ? PHE C 507 TYR C 518 
AC7 1 ILE D 7   ? LYS D 10  ? ILE D 7   LYS D 10  
AC7 2 TRP D 13  ? LEU D 16  ? TRP D 13  LEU D 16  
AC7 3 GLU D 19  ? LYS D 20  ? GLU D 19  LYS D 20  
AC8 1 VAL D 166 ? SER D 169 ? VAL D 166 SER D 169 
AC8 2 ILE D 124 ? ASN D 131 ? ILE D 124 ASN D 131 
AC8 3 LYS D 85  ? GLY D 89  ? LYS D 85  GLY D 89  
AC8 4 THR D 64  ? ARG D 66  ? THR D 64  ARG D 66  
AC8 5 ILE D 23  ? GLY D 27  ? ILE D 23  GLY D 27  
AC8 6 GLY D 264 ? MET D 265 ? GLY D 264 MET D 265 
AC9 1 TYR D 186 ? ASN D 189 ? TYR D 186 ASN D 189 
AC9 2 PHE D 220 ? ALA D 224 ? PHE D 220 ALA D 224 
AD1 1 TRP D 295 ? GLY D 296 ? TRP D 295 GLY D 296 
AD1 2 THR D 306 ? PRO D 307 ? THR D 306 PRO D 307 
AD2 1 GLY D 320 ? SER D 324 ? GLY D 320 SER D 324 
AD2 2 LYS D 335 ? ASN D 342 ? LYS D 335 ASN D 342 
AD2 3 GLY D 367 ? THR D 374 ? GLY D 367 THR D 374 
AD3 1 SER D 329 ? HIS D 331 ? SER D 329 HIS D 331 
AD3 2 ILE D 396 ? SER D 407 ? ILE D 396 SER D 407 
AD3 3 ILE D 380 ? TYR D 390 ? ILE D 380 TYR D 390 
AD3 4 LYS D 348 ? PHE D 353 ? LYS D 348 PHE D 353 
AD3 5 LYS D 356 ? ASN D 362 ? LYS D 356 ASN D 362 
AD4 1 GLU D 415 ? THR D 421 ? GLU D 415 THR D 421 
AD4 2 ILE D 431 ? GLU D 439 ? ILE D 431 GLU D 439 
AD4 3 ILE D 478 ? ASN D 486 ? ILE D 478 ASN D 486 
AD5 1 THR D 445 ? LEU D 446 ? THR D 445 LEU D 446 
AD5 2 VAL D 493 ? TYR D 504 ? VAL D 493 TYR D 504 
AD5 3 LEU D 450 ? ASN D 455 ? LEU D 450 ASN D 455 
AD5 4 SER D 464 ? VAL D 468 ? SER D 464 VAL D 468 
AD6 1 THR D 445 ? LEU D 446 ? THR D 445 LEU D 446 
AD6 2 VAL D 493 ? TYR D 504 ? VAL D 493 TYR D 504 
AD6 3 PHE D 507 ? TYR D 518 ? PHE D 507 TYR D 518 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 10  ? N LYS A 10  O TRP A 13  ? O TRP A 13  
AA1 2 3 N LEU A 16  ? N LEU A 16  O GLU A 19  ? O GLU A 19  
AA2 1 2 O SER A 169 ? O SER A 169 N ILE A 130 ? N ILE A 130 
AA2 2 3 O ILE A 125 ? O ILE A 125 N LEU A 86  ? N LEU A 86  
AA2 3 4 O ILE A 87  ? O ILE A 87  N ILE A 65  ? N ILE A 65  
AA2 4 5 O ARG A 66  ? O ARG A 66  N ILE A 26  ? N ILE A 26  
AA2 5 6 N ILE A 23  ? N ILE A 23  O MET A 265 ? O MET A 265 
AA3 1 2 N TYR A 186 ? N TYR A 186 O ILE A 221 ? O ILE A 221 
AA4 1 2 N GLY A 296 ? N GLY A 296 O THR A 306 ? O THR A 306 
AA5 1 2 N ILE A 323 ? N ILE A 323 O GLU A 339 ? O GLU A 339 
AA5 2 3 N ILE A 336 ? N ILE A 336 O LEU A 373 ? O LEU A 373 
AA6 1 2 N HIS A 331 ? N HIS A 331 O LEU A 405 ? O LEU A 405 
AA6 2 3 O ILE A 397 ? O ILE A 397 N PHE A 389 ? N PHE A 389 
AA6 3 4 O GLU A 388 ? O GLU A 388 N VAL A 350 ? N VAL A 350 
AA6 4 5 N VAL A 351 ? N VAL A 351 O ILE A 358 ? O ILE A 358 
AA7 1 2 N GLU A 415 ? N GLU A 415 O GLU A 439 ? O GLU A 439 
AA7 2 3 N ALA A 432 ? N ALA A 432 O PHE A 485 ? O PHE A 485 
AA8 1 2 O VAL A 468 ? O VAL A 468 N LEU A 450 ? N LEU A 450 
AA8 2 3 N LEU A 447 ? N LEU A 447 O SER A 501 ? O SER A 501 
AA8 3 4 N ALA A 496 ? N ALA A 496 O LYS A 515 ? O LYS A 515 
AA9 1 2 N GLU B 8   ? N GLU B 8   O HIS B 15  ? O HIS B 15  
AA9 2 3 N LEU B 16  ? N LEU B 16  O GLU B 19  ? O GLU B 19  
AB1 1 2 O SER B 169 ? O SER B 169 N ILE B 130 ? N ILE B 130 
AB1 2 3 O ILE B 125 ? O ILE B 125 N LEU B 86  ? N LEU B 86  
AB1 3 4 O ILE B 87  ? O ILE B 87  N ILE B 65  ? N ILE B 65  
AB1 4 5 O ARG B 66  ? O ARG B 66  N ILE B 26  ? N ILE B 26  
AB1 5 6 N ILE B 23  ? N ILE B 23  O MET B 265 ? O MET B 265 
AB2 1 2 N TYR B 186 ? N TYR B 186 O ILE B 221 ? O ILE B 221 
AB3 1 2 N GLY B 296 ? N GLY B 296 O THR B 306 ? O THR B 306 
AB4 1 2 N SER B 324 ? N SER B 324 O GLU B 339 ? O GLU B 339 
AB4 2 3 N ASN B 342 ? N ASN B 342 O GLY B 367 ? O GLY B 367 
AB5 1 2 N HIS B 331 ? N HIS B 331 O LEU B 405 ? O LEU B 405 
AB5 2 3 O GLU B 400 ? O GLU B 400 N PHE B 387 ? N PHE B 387 
AB5 3 4 O GLU B 388 ? O GLU B 388 N VAL B 350 ? N VAL B 350 
AB5 4 5 N VAL B 351 ? N VAL B 351 O TYR B 359 ? O TYR B 359 
AB6 1 2 N GLU B 415 ? N GLU B 415 O GLU B 439 ? O GLU B 439 
AB6 2 3 N ALA B 432 ? N ALA B 432 O PHE B 485 ? O PHE B 485 
AB7 1 2 N THR B 445 ? N THR B 445 O ARG B 503 ? O ARG B 503 
AB7 2 3 O SER B 497 ? O SER B 497 N SER B 453 ? N SER B 453 
AB7 3 4 N LEU B 450 ? N LEU B 450 O VAL B 468 ? O VAL B 468 
AB8 1 2 N THR B 445 ? N THR B 445 O ARG B 503 ? O ARG B 503 
AB8 2 3 N ALA B 496 ? N ALA B 496 O LYS B 515 ? O LYS B 515 
AB9 1 2 N GLU C 8   ? N GLU C 8   O HIS C 15  ? O HIS C 15  
AB9 2 3 N LEU C 16  ? N LEU C 16  O GLU C 19  ? O GLU C 19  
AC1 1 2 O THR C 167 ? O THR C 167 N TYR C 127 ? N TYR C 127 
AC1 2 3 O ILE C 125 ? O ILE C 125 N LEU C 86  ? N LEU C 86  
AC1 3 4 O ILE C 87  ? O ILE C 87  N ILE C 65  ? N ILE C 65  
AC1 4 5 O ARG C 66  ? O ARG C 66  N ILE C 26  ? N ILE C 26  
AC1 5 6 N ILE C 23  ? N ILE C 23  O MET C 265 ? O MET C 265 
AC1 6 7 O GLY C 264 ? O GLY C 264 N THR C 222 ? N THR C 222 
AC1 7 8 O THR C 223 ? O THR C 223 N TYR C 188 ? N TYR C 188 
AC2 1 2 N GLY C 296 ? N GLY C 296 O THR C 306 ? O THR C 306 
AC3 1 2 N SER C 324 ? N SER C 324 O GLU C 339 ? O GLU C 339 
AC3 2 3 N ASN C 342 ? N ASN C 342 O GLY C 367 ? O GLY C 367 
AC4 1 2 N HIS C 331 ? N HIS C 331 O LEU C 405 ? O LEU C 405 
AC4 2 3 O ILE C 397 ? O ILE C 397 N PHE C 389 ? N PHE C 389 
AC4 3 4 O GLU C 388 ? O GLU C 388 N VAL C 350 ? N VAL C 350 
AC4 4 5 N VAL C 351 ? N VAL C 351 O TYR C 359 ? O TYR C 359 
AC5 1 2 N GLU C 415 ? N GLU C 415 O GLU C 439 ? O GLU C 439 
AC5 2 3 N ALA C 432 ? N ALA C 432 O PHE C 485 ? O PHE C 485 
AC6 1 2 O SER C 464 ? O SER C 464 N TYR C 454 ? N TYR C 454 
AC6 2 3 N SER C 453 ? N SER C 453 O SER C 497 ? O SER C 497 
AC6 3 4 N VAL C 502 ? N VAL C 502 O PHE C 509 ? O PHE C 509 
AC7 1 2 N GLU D 8   ? N GLU D 8   O HIS D 15  ? O HIS D 15  
AC7 2 3 N LEU D 16  ? N LEU D 16  O GLU D 19  ? O GLU D 19  
AC8 1 2 O SER D 169 ? O SER D 169 N ILE D 130 ? N ILE D 130 
AC8 2 3 O ILE D 125 ? O ILE D 125 N LEU D 86  ? N LEU D 86  
AC8 3 4 O ILE D 87  ? O ILE D 87  N ILE D 65  ? N ILE D 65  
AC8 4 5 O ARG D 66  ? O ARG D 66  N ILE D 26  ? N ILE D 26  
AC8 5 6 N ILE D 23  ? N ILE D 23  O MET D 265 ? O MET D 265 
AC9 1 2 N TYR D 188 ? N TYR D 188 O THR D 223 ? O THR D 223 
AD1 1 2 N GLY D 296 ? N GLY D 296 O THR D 306 ? O THR D 306 
AD2 1 2 N LEU D 321 ? N LEU D 321 O TYR D 341 ? O TYR D 341 
AD2 2 3 N ASN D 342 ? N ASN D 342 O GLY D 367 ? O GLY D 367 
AD3 1 2 N HIS D 331 ? N HIS D 331 O LEU D 405 ? O LEU D 405 
AD3 2 3 O GLU D 400 ? O GLU D 400 N PHE D 387 ? N PHE D 387 
AD3 3 4 O ALA D 386 ? O ALA D 386 N LYS D 352 ? N LYS D 352 
AD3 4 5 N VAL D 351 ? N VAL D 351 O TYR D 359 ? O TYR D 359 
AD4 1 2 N THR D 417 ? N THR D 417 O LYS D 437 ? O LYS D 437 
AD4 2 3 N ALA D 432 ? N ALA D 432 O PHE D 485 ? O PHE D 485 
AD5 1 2 N THR D 445 ? N THR D 445 O ARG D 503 ? O ARG D 503 
AD5 2 3 O GLY D 499 ? O GLY D 499 N LYS D 451 ? N LYS D 451 
AD5 3 4 N LEU D 450 ? N LEU D 450 O VAL D 468 ? O VAL D 468 
AD6 1 2 N THR D 445 ? N THR D 445 O ARG D 503 ? O ARG D 503 
AD6 2 3 N ALA D 496 ? N ALA D 496 O LYS D 515 ? O LYS D 515 
# 
_pdbx_entry_details.entry_id                   9G4N 
_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 GLU A 132 ? ? 73.80   57.87   
2  1 THR A 142 ? ? 90.71   141.14  
3  1 THR A 167 ? ? -147.63 -156.69 
4  1 ALA A 224 ? ? 176.03  145.94  
5  1 ASP A 371 ? ? -163.52 -165.65 
6  1 ALA A 410 ? ? -38.08  140.63  
7  1 ASN A 443 ? ? 84.28   -16.67  
8  1 ASP A 448 ? ? 66.22   -142.70 
9  1 ASP A 472 ? ? -64.86  0.07    
10 1 ARG A 519 ? ? -65.79  -88.68  
11 1 LYS B 24  ? ? -100.01 77.07   
12 1 ASP B 91  ? ? -90.41  59.65   
13 1 GLU B 132 ? ? 76.56   55.96   
14 1 THR B 142 ? ? 99.76   139.42  
15 1 THR B 167 ? ? -153.32 -157.13 
16 1 ALA B 224 ? ? -178.08 146.39  
17 1 GLU B 279 ? ? 55.51   83.05   
18 1 ASP B 371 ? ? -168.40 -163.58 
19 1 LYS B 424 ? ? -134.92 -33.22  
20 1 ASP B 448 ? ? 44.59   -120.44 
21 1 LYS C 105 ? ? -39.40  -71.56  
22 1 THR C 142 ? ? 111.11  140.16  
23 1 GLU C 279 ? ? 53.15   88.16   
24 1 ASP C 371 ? ? -154.98 -159.34 
25 1 ASN C 394 ? ? 70.12   30.01   
26 1 ASP C 448 ? ? 58.24   -128.24 
27 1 ASN C 490 ? ? -99.98  31.70   
28 1 ARG C 519 ? ? -74.30  -99.62  
29 1 ASP D 11  ? ? 49.80   28.66   
30 1 LYS D 24  ? ? -107.34 77.08   
31 1 GLU D 132 ? ? 74.90   54.12   
32 1 THR D 142 ? ? 87.55   139.75  
33 1 THR D 167 ? ? -143.76 -157.12 
34 1 PHE D 225 ? ? -174.77 146.70  
35 1 GLU D 279 ? ? 64.68   78.60   
36 1 ASP D 371 ? ? -164.08 -163.35 
37 1 LYS D 424 ? ? -131.24 -34.51  
38 1 ASN D 443 ? ? 93.49   -23.08  
39 1 ASP D 448 ? ? 35.35   -133.66 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 503 ? ? 0.218 'SIDE CHAIN' 
2 1 ARG B 33  ? ? 0.108 'SIDE CHAIN' 
3 1 ARG C 43  ? ? 0.146 'SIDE CHAIN' 
4 1 ARG D 308 ? ? 0.103 'SIDE CHAIN' 
# 
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 -67.6100 15.1040 -76.6750 0.0425 ? -0.0099 ? 0.0311  ? 0.0116 ? -0.0012 ? 0.2293 ? 0.5432 ? 0.0446 
? 0.2135  ? 1.0121 ? 0.0185  ? 0.6364 ? 0.0605  ? -0.0471 ? 0.0173  ? 0.1303  ? -0.0356 ? 0.0396 ? 0.0043  ? -0.0768 ? -0.0250 ? 
2 'X-RAY DIFFRACTION' ? refined -19.0060 -4.4120 -65.6940 0.0271 ? -0.0021 ? 0.0066  ? 0.0046 ? 0.0095  ? 0.2686 ? 0.5127 ? 0.0049 
? -0.0622 ? 0.6997 ? -0.0524 ? 1.1923 ? 0.0130  ? -0.0273 ? -0.0245 ? 0.0816  ? 0.0025  ? 0.0066 ? 0.0389  ? -0.0555 ? -0.0155 ? 
3 'X-RAY DIFFRACTION' ? refined -19.9940 55.2580 -54.9780 0.2235 ? 0.0057  ? 0.0073  ? 0.0149 ? 0.0087  ? 0.2175 ? 0.7181 ? 
-0.1176 ? 0.0694  ? 1.4149 ? -0.2394 ? 0.6392 ? -0.0169 ? -0.0893 ? 0.0218  ? 0.4381  ? 0.0620  ? 0.0687 ? -0.1763 ? 0.0108  ? 
-0.0450 ? 
4 'X-RAY DIFFRACTION' ? refined -49.0020 10.8100 -19.6050 0.0290 ? -0.0053 ? -0.0294 ? 0.0061 ? -0.0137 ? 0.2668 ? 0.4635 ? 0.0354 
? 0.0216  ? 0.7379 ? -0.3256 ? 0.8956 ? 0.0037  ? 0.0113  ? -0.0249 ? -0.0869 ? 0.0259  ? 0.0644 ? 0.0502  ? -0.0623 ? -0.0296 ? 
# 
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 ? ? A 3 ? ? ? A 530 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 3 ? ? ? B 529 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? C 3 ? ? ? C 529 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? D 3 ? ? ? D 529 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A GLN 2   ? A GLN 2   
3  1 Y 1 A GLU 531 ? A GLU 531 
4  1 Y 1 A HIS 532 ? A HIS 532 
5  1 Y 1 A HIS 533 ? A HIS 533 
6  1 Y 1 A HIS 534 ? A HIS 534 
7  1 Y 1 A HIS 535 ? A HIS 535 
8  1 Y 1 A HIS 536 ? A HIS 536 
9  1 Y 1 A HIS 537 ? A HIS 537 
10 1 Y 1 B MET 1   ? B MET 1   
11 1 Y 1 B GLN 2   ? B GLN 2   
12 1 Y 1 B SER 3   ? B SER 3   
13 1 Y 1 B LEU 530 ? B LEU 530 
14 1 Y 1 B GLU 531 ? B GLU 531 
15 1 Y 1 B HIS 532 ? B HIS 532 
16 1 Y 1 B HIS 533 ? B HIS 533 
17 1 Y 1 B HIS 534 ? B HIS 534 
18 1 Y 1 B HIS 535 ? B HIS 535 
19 1 Y 1 B HIS 536 ? B HIS 536 
20 1 Y 1 B HIS 537 ? B HIS 537 
21 1 Y 1 C MET 1   ? C MET 1   
22 1 Y 1 C GLN 2   ? C GLN 2   
23 1 Y 1 C LEU 530 ? C LEU 530 
24 1 Y 1 C GLU 531 ? C GLU 531 
25 1 Y 1 C HIS 532 ? C HIS 532 
26 1 Y 1 C HIS 533 ? C HIS 533 
27 1 Y 1 C HIS 534 ? C HIS 534 
28 1 Y 1 C HIS 535 ? C HIS 535 
29 1 Y 1 C HIS 536 ? C HIS 536 
30 1 Y 1 C HIS 537 ? C HIS 537 
31 1 Y 1 D MET 1   ? D MET 1   
32 1 Y 1 D GLN 2   ? D GLN 2   
33 1 Y 1 D LEU 530 ? D LEU 530 
34 1 Y 1 D GLU 531 ? D GLU 531 
35 1 Y 1 D HIS 532 ? D HIS 532 
36 1 Y 1 D HIS 533 ? D HIS 533 
37 1 Y 1 D HIS 534 ? D HIS 534 
38 1 Y 1 D HIS 535 ? D HIS 535 
39 1 Y 1 D HIS 536 ? D HIS 536 
40 1 Y 1 D HIS 537 ? D HIS 537 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
BGC C2   C N R 74  
BGC C3   C N S 75  
BGC C4   C N S 76  
BGC C5   C N R 77  
BGC C6   C N N 78  
BGC C1   C N R 79  
BGC O1   O N N 80  
BGC O2   O N N 81  
BGC O3   O N N 82  
BGC O4   O N N 83  
BGC O5   O N N 84  
BGC O6   O N N 85  
BGC H2   H N N 86  
BGC H3   H N N 87  
BGC H4   H N N 88  
BGC H5   H N N 89  
BGC H61  H N N 90  
BGC H62  H N N 91  
BGC H1   H N N 92  
BGC HO1  H N N 93  
BGC HO2  H N N 94  
BGC HO3  H N N 95  
BGC HO4  H N N 96  
BGC HO6  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 
EDO C1   C N N 112 
EDO O1   O N N 113 
EDO C2   C N N 114 
EDO O2   O N N 115 
EDO H11  H N N 116 
EDO H12  H N N 117 
EDO HO1  H N N 118 
EDO H21  H N N 119 
EDO H22  H N N 120 
EDO HO2  H N N 121 
GLN N    N N N 122 
GLN CA   C N S 123 
GLN C    C N N 124 
GLN O    O N N 125 
GLN CB   C N N 126 
GLN CG   C N N 127 
GLN CD   C N N 128 
GLN OE1  O N N 129 
GLN NE2  N N N 130 
GLN OXT  O N N 131 
GLN H    H N N 132 
GLN H2   H N N 133 
GLN HA   H N N 134 
GLN HB2  H N N 135 
GLN HB3  H N N 136 
GLN HG2  H N N 137 
GLN HG3  H N N 138 
GLN HE21 H N N 139 
GLN HE22 H N N 140 
GLN HXT  H N N 141 
GLU N    N N N 142 
GLU CA   C N S 143 
GLU C    C N N 144 
GLU O    O N N 145 
GLU CB   C N N 146 
GLU CG   C N N 147 
GLU CD   C N N 148 
GLU OE1  O N N 149 
GLU OE2  O N N 150 
GLU OXT  O N N 151 
GLU H    H N N 152 
GLU H2   H N N 153 
GLU HA   H N N 154 
GLU HB2  H N N 155 
GLU HB3  H N N 156 
GLU HG2  H N N 157 
GLU HG3  H N N 158 
GLU HE2  H N N 159 
GLU HXT  H N N 160 
GLY N    N N N 161 
GLY CA   C N N 162 
GLY C    C N N 163 
GLY O    O N N 164 
GLY OXT  O N N 165 
GLY H    H N N 166 
GLY H2   H N N 167 
GLY HA2  H N N 168 
GLY HA3  H N N 169 
GLY HXT  H N N 170 
GOL C1   C N N 171 
GOL O1   O N N 172 
GOL C2   C N N 173 
GOL O2   O N N 174 
GOL C3   C N N 175 
GOL O3   O N N 176 
GOL H11  H N N 177 
GOL H12  H N N 178 
GOL HO1  H N N 179 
GOL H2   H N N 180 
GOL HO2  H N N 181 
GOL H31  H N N 182 
GOL H32  H N N 183 
GOL HO3  H N N 184 
HIS N    N N N 185 
HIS CA   C N S 186 
HIS C    C N N 187 
HIS O    O N N 188 
HIS CB   C N N 189 
HIS CG   C Y N 190 
HIS ND1  N Y N 191 
HIS CD2  C Y N 192 
HIS CE1  C Y N 193 
HIS NE2  N Y N 194 
HIS OXT  O N N 195 
HIS H    H N N 196 
HIS H2   H N N 197 
HIS HA   H N N 198 
HIS HB2  H N N 199 
HIS HB3  H N N 200 
HIS HD1  H N N 201 
HIS HD2  H N N 202 
HIS HE1  H N N 203 
HIS HE2  H N N 204 
HIS HXT  H N N 205 
HOH O    O N N 206 
HOH H1   H N N 207 
HOH H2   H N N 208 
ILE N    N N N 209 
ILE CA   C N S 210 
ILE C    C N N 211 
ILE O    O N N 212 
ILE CB   C N S 213 
ILE CG1  C N N 214 
ILE CG2  C N N 215 
ILE CD1  C N N 216 
ILE OXT  O N N 217 
ILE H    H N N 218 
ILE H2   H N N 219 
ILE HA   H N N 220 
ILE HB   H N N 221 
ILE HG12 H N N 222 
ILE HG13 H N N 223 
ILE HG21 H N N 224 
ILE HG22 H N N 225 
ILE HG23 H N N 226 
ILE HD11 H N N 227 
ILE HD12 H N N 228 
ILE HD13 H N N 229 
ILE HXT  H N N 230 
LEU N    N N N 231 
LEU CA   C N S 232 
LEU C    C N N 233 
LEU O    O N N 234 
LEU CB   C N N 235 
LEU CG   C N N 236 
LEU CD1  C N N 237 
LEU CD2  C N N 238 
LEU OXT  O N N 239 
LEU H    H N N 240 
LEU H2   H N N 241 
LEU HA   H N N 242 
LEU HB2  H N N 243 
LEU HB3  H N N 244 
LEU HG   H N N 245 
LEU HD11 H N N 246 
LEU HD12 H N N 247 
LEU HD13 H N N 248 
LEU HD21 H N N 249 
LEU HD22 H N N 250 
LEU HD23 H N N 251 
LEU HXT  H N N 252 
LYS N    N N N 253 
LYS CA   C N S 254 
LYS C    C N N 255 
LYS O    O N N 256 
LYS CB   C N N 257 
LYS CG   C N N 258 
LYS CD   C N N 259 
LYS CE   C N N 260 
LYS NZ   N N N 261 
LYS OXT  O N N 262 
LYS H    H N N 263 
LYS H2   H N N 264 
LYS HA   H N N 265 
LYS HB2  H N N 266 
LYS HB3  H N N 267 
LYS HG2  H N N 268 
LYS HG3  H N N 269 
LYS HD2  H N N 270 
LYS HD3  H N N 271 
LYS HE2  H N N 272 
LYS HE3  H N N 273 
LYS HZ1  H N N 274 
LYS HZ2  H N N 275 
LYS HZ3  H N N 276 
LYS HXT  H N N 277 
MET N    N N N 278 
MET CA   C N S 279 
MET C    C N N 280 
MET O    O N N 281 
MET CB   C N N 282 
MET CG   C N N 283 
MET SD   S N N 284 
MET CE   C N N 285 
MET OXT  O N N 286 
MET H    H N N 287 
MET H2   H N N 288 
MET HA   H N N 289 
MET HB2  H N N 290 
MET HB3  H N N 291 
MET HG2  H N N 292 
MET HG3  H N N 293 
MET HE1  H N N 294 
MET HE2  H N N 295 
MET HE3  H N N 296 
MET HXT  H N N 297 
PGE C1   C N N 298 
PGE O1   O N N 299 
PGE C2   C N N 300 
PGE O2   O N N 301 
PGE C3   C N N 302 
PGE C4   C N N 303 
PGE O4   O N N 304 
PGE C6   C N N 305 
PGE C5   C N N 306 
PGE O3   O N N 307 
PGE H1   H N N 308 
PGE H12  H N N 309 
PGE HO1  H N N 310 
PGE H2   H N N 311 
PGE H22  H N N 312 
PGE H3   H N N 313 
PGE H32  H N N 314 
PGE H4   H N N 315 
PGE H42  H N N 316 
PGE HO4  H N N 317 
PGE H6   H N N 318 
PGE H62  H N N 319 
PGE H5   H N N 320 
PGE H52  H N N 321 
PHE N    N N N 322 
PHE CA   C N S 323 
PHE C    C N N 324 
PHE O    O N N 325 
PHE CB   C N N 326 
PHE CG   C Y N 327 
PHE CD1  C Y N 328 
PHE CD2  C Y N 329 
PHE CE1  C Y N 330 
PHE CE2  C Y N 331 
PHE CZ   C Y N 332 
PHE OXT  O N N 333 
PHE H    H N N 334 
PHE H2   H N N 335 
PHE HA   H N N 336 
PHE HB2  H N N 337 
PHE HB3  H N N 338 
PHE HD1  H N N 339 
PHE HD2  H N N 340 
PHE HE1  H N N 341 
PHE HE2  H N N 342 
PHE HZ   H N N 343 
PHE HXT  H N N 344 
PRO N    N N N 345 
PRO CA   C N S 346 
PRO C    C N N 347 
PRO O    O N N 348 
PRO CB   C N N 349 
PRO CG   C N N 350 
PRO CD   C N N 351 
PRO OXT  O N N 352 
PRO H    H N N 353 
PRO HA   H N N 354 
PRO HB2  H N N 355 
PRO HB3  H N N 356 
PRO HG2  H N N 357 
PRO HG3  H N N 358 
PRO HD2  H N N 359 
PRO HD3  H N N 360 
PRO HXT  H N N 361 
SER N    N N N 362 
SER CA   C N S 363 
SER C    C N N 364 
SER O    O N N 365 
SER CB   C N N 366 
SER OG   O N N 367 
SER OXT  O N N 368 
SER H    H N N 369 
SER H2   H N N 370 
SER HA   H N N 371 
SER HB2  H N N 372 
SER HB3  H N N 373 
SER HG   H N N 374 
SER HXT  H N N 375 
THR N    N N N 376 
THR CA   C N S 377 
THR C    C N N 378 
THR O    O N N 379 
THR CB   C N R 380 
THR OG1  O N N 381 
THR CG2  C N N 382 
THR OXT  O N N 383 
THR H    H N N 384 
THR H2   H N N 385 
THR HA   H N N 386 
THR HB   H N N 387 
THR HG1  H N N 388 
THR HG21 H N N 389 
THR HG22 H N N 390 
THR HG23 H N N 391 
THR HXT  H N N 392 
TRP N    N N N 393 
TRP CA   C N S 394 
TRP C    C N N 395 
TRP O    O N N 396 
TRP CB   C N N 397 
TRP CG   C Y N 398 
TRP CD1  C Y N 399 
TRP CD2  C Y N 400 
TRP NE1  N Y N 401 
TRP CE2  C Y N 402 
TRP CE3  C Y N 403 
TRP CZ2  C Y N 404 
TRP CZ3  C Y N 405 
TRP CH2  C Y N 406 
TRP OXT  O N N 407 
TRP H    H N N 408 
TRP H2   H N N 409 
TRP HA   H N N 410 
TRP HB2  H N N 411 
TRP HB3  H N N 412 
TRP HD1  H N N 413 
TRP HE1  H N N 414 
TRP HE3  H N N 415 
TRP HZ2  H N N 416 
TRP HZ3  H N N 417 
TRP HH2  H N N 418 
TRP HXT  H N N 419 
TYR N    N N N 420 
TYR CA   C N S 421 
TYR C    C N N 422 
TYR O    O N N 423 
TYR CB   C N N 424 
TYR CG   C Y N 425 
TYR CD1  C Y N 426 
TYR CD2  C Y N 427 
TYR CE1  C Y N 428 
TYR CE2  C Y N 429 
TYR CZ   C Y N 430 
TYR OH   O N N 431 
TYR OXT  O N N 432 
TYR H    H N N 433 
TYR H2   H N N 434 
TYR HA   H N N 435 
TYR HB2  H N N 436 
TYR HB3  H N N 437 
TYR HD1  H N N 438 
TYR HD2  H N N 439 
TYR HE1  H N N 440 
TYR HE2  H N N 441 
TYR HH   H N N 442 
TYR HXT  H N N 443 
VAL N    N N N 444 
VAL CA   C N S 445 
VAL C    C N N 446 
VAL O    O N N 447 
VAL CB   C N N 448 
VAL CG1  C N N 449 
VAL CG2  C N N 450 
VAL OXT  O N N 451 
VAL H    H N N 452 
VAL H2   H N N 453 
VAL HA   H N N 454 
VAL HB   H N N 455 
VAL HG11 H N N 456 
VAL HG12 H N N 457 
VAL HG13 H N N 458 
VAL HG21 H N N 459 
VAL HG22 H N N 460 
VAL HG23 H N N 461 
VAL HXT  H N N 462 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BGC C2  C3   sing N N 70  
BGC C2  C1   sing N N 71  
BGC C2  O2   sing N N 72  
BGC C2  H2   sing N N 73  
BGC C3  C4   sing N N 74  
BGC C3  O3   sing N N 75  
BGC C3  H3   sing N N 76  
BGC C4  C5   sing N N 77  
BGC C4  O4   sing N N 78  
BGC C4  H4   sing N N 79  
BGC C5  C6   sing N N 80  
BGC C5  O5   sing N N 81  
BGC C5  H5   sing N N 82  
BGC C6  O6   sing N N 83  
BGC C6  H61  sing N N 84  
BGC C6  H62  sing N N 85  
BGC C1  O1   sing N N 86  
BGC C1  O5   sing N N 87  
BGC C1  H1   sing N N 88  
BGC O1  HO1  sing N N 89  
BGC O2  HO2  sing N N 90  
BGC O3  HO3  sing N N 91  
BGC O4  HO4  sing N N 92  
BGC O6  HO6  sing N N 93  
CYS N   CA   sing N N 94  
CYS N   H    sing N N 95  
CYS N   H2   sing N N 96  
CYS CA  C    sing N N 97  
CYS CA  CB   sing N N 98  
CYS CA  HA   sing N N 99  
CYS C   O    doub N N 100 
CYS C   OXT  sing N N 101 
CYS CB  SG   sing N N 102 
CYS CB  HB2  sing N N 103 
CYS CB  HB3  sing N N 104 
CYS SG  HG   sing N N 105 
CYS OXT HXT  sing N N 106 
EDO C1  O1   sing N N 107 
EDO C1  C2   sing N N 108 
EDO C1  H11  sing N N 109 
EDO C1  H12  sing N N 110 
EDO O1  HO1  sing N N 111 
EDO C2  O2   sing N N 112 
EDO C2  H21  sing N N 113 
EDO C2  H22  sing N N 114 
EDO O2  HO2  sing N N 115 
GLN N   CA   sing N N 116 
GLN N   H    sing N N 117 
GLN N   H2   sing N N 118 
GLN CA  C    sing N N 119 
GLN CA  CB   sing N N 120 
GLN CA  HA   sing N N 121 
GLN C   O    doub N N 122 
GLN C   OXT  sing N N 123 
GLN CB  CG   sing N N 124 
GLN CB  HB2  sing N N 125 
GLN CB  HB3  sing N N 126 
GLN CG  CD   sing N N 127 
GLN CG  HG2  sing N N 128 
GLN CG  HG3  sing N N 129 
GLN CD  OE1  doub N N 130 
GLN CD  NE2  sing N N 131 
GLN NE2 HE21 sing N N 132 
GLN NE2 HE22 sing N N 133 
GLN OXT HXT  sing N N 134 
GLU N   CA   sing N N 135 
GLU N   H    sing N N 136 
GLU N   H2   sing N N 137 
GLU CA  C    sing N N 138 
GLU CA  CB   sing N N 139 
GLU CA  HA   sing N N 140 
GLU C   O    doub N N 141 
GLU C   OXT  sing N N 142 
GLU CB  CG   sing N N 143 
GLU CB  HB2  sing N N 144 
GLU CB  HB3  sing N N 145 
GLU CG  CD   sing N N 146 
GLU CG  HG2  sing N N 147 
GLU CG  HG3  sing N N 148 
GLU CD  OE1  doub N N 149 
GLU CD  OE2  sing N N 150 
GLU OE2 HE2  sing N N 151 
GLU OXT HXT  sing N N 152 
GLY N   CA   sing N N 153 
GLY N   H    sing N N 154 
GLY N   H2   sing N N 155 
GLY CA  C    sing N N 156 
GLY CA  HA2  sing N N 157 
GLY CA  HA3  sing N N 158 
GLY C   O    doub N N 159 
GLY C   OXT  sing N N 160 
GLY OXT HXT  sing N N 161 
GOL C1  O1   sing N N 162 
GOL C1  C2   sing N N 163 
GOL C1  H11  sing N N 164 
GOL C1  H12  sing N N 165 
GOL O1  HO1  sing N N 166 
GOL C2  O2   sing N N 167 
GOL C2  C3   sing N N 168 
GOL C2  H2   sing N N 169 
GOL O2  HO2  sing N N 170 
GOL C3  O3   sing N N 171 
GOL C3  H31  sing N N 172 
GOL C3  H32  sing N N 173 
GOL O3  HO3  sing N N 174 
HIS N   CA   sing N N 175 
HIS N   H    sing N N 176 
HIS N   H2   sing N N 177 
HIS CA  C    sing N N 178 
HIS CA  CB   sing N N 179 
HIS CA  HA   sing N N 180 
HIS C   O    doub N N 181 
HIS C   OXT  sing N N 182 
HIS CB  CG   sing N N 183 
HIS CB  HB2  sing N N 184 
HIS CB  HB3  sing N N 185 
HIS CG  ND1  sing Y N 186 
HIS CG  CD2  doub Y N 187 
HIS ND1 CE1  doub Y N 188 
HIS ND1 HD1  sing N N 189 
HIS CD2 NE2  sing Y N 190 
HIS CD2 HD2  sing N N 191 
HIS CE1 NE2  sing Y N 192 
HIS CE1 HE1  sing N N 193 
HIS NE2 HE2  sing N N 194 
HIS OXT HXT  sing N N 195 
HOH O   H1   sing N N 196 
HOH O   H2   sing N N 197 
ILE N   CA   sing N N 198 
ILE N   H    sing N N 199 
ILE N   H2   sing N N 200 
ILE CA  C    sing N N 201 
ILE CA  CB   sing N N 202 
ILE CA  HA   sing N N 203 
ILE C   O    doub N N 204 
ILE C   OXT  sing N N 205 
ILE CB  CG1  sing N N 206 
ILE CB  CG2  sing N N 207 
ILE CB  HB   sing N N 208 
ILE CG1 CD1  sing N N 209 
ILE CG1 HG12 sing N N 210 
ILE CG1 HG13 sing N N 211 
ILE CG2 HG21 sing N N 212 
ILE CG2 HG22 sing N N 213 
ILE CG2 HG23 sing N N 214 
ILE CD1 HD11 sing N N 215 
ILE CD1 HD12 sing N N 216 
ILE CD1 HD13 sing N N 217 
ILE OXT HXT  sing N N 218 
LEU N   CA   sing N N 219 
LEU N   H    sing N N 220 
LEU N   H2   sing N N 221 
LEU CA  C    sing N N 222 
LEU CA  CB   sing N N 223 
LEU CA  HA   sing N N 224 
LEU C   O    doub N N 225 
LEU C   OXT  sing N N 226 
LEU CB  CG   sing N N 227 
LEU CB  HB2  sing N N 228 
LEU CB  HB3  sing N N 229 
LEU CG  CD1  sing N N 230 
LEU CG  CD2  sing N N 231 
LEU CG  HG   sing N N 232 
LEU CD1 HD11 sing N N 233 
LEU CD1 HD12 sing N N 234 
LEU CD1 HD13 sing N N 235 
LEU CD2 HD21 sing N N 236 
LEU CD2 HD22 sing N N 237 
LEU CD2 HD23 sing N N 238 
LEU OXT HXT  sing N N 239 
LYS N   CA   sing N N 240 
LYS N   H    sing N N 241 
LYS N   H2   sing N N 242 
LYS CA  C    sing N N 243 
LYS CA  CB   sing N N 244 
LYS CA  HA   sing N N 245 
LYS C   O    doub N N 246 
LYS C   OXT  sing N N 247 
LYS CB  CG   sing N N 248 
LYS CB  HB2  sing N N 249 
LYS CB  HB3  sing N N 250 
LYS CG  CD   sing N N 251 
LYS CG  HG2  sing N N 252 
LYS CG  HG3  sing N N 253 
LYS CD  CE   sing N N 254 
LYS CD  HD2  sing N N 255 
LYS CD  HD3  sing N N 256 
LYS CE  NZ   sing N N 257 
LYS CE  HE2  sing N N 258 
LYS CE  HE3  sing N N 259 
LYS NZ  HZ1  sing N N 260 
LYS NZ  HZ2  sing N N 261 
LYS NZ  HZ3  sing N N 262 
LYS OXT HXT  sing N N 263 
MET N   CA   sing N N 264 
MET N   H    sing N N 265 
MET N   H2   sing N N 266 
MET CA  C    sing N N 267 
MET CA  CB   sing N N 268 
MET CA  HA   sing N N 269 
MET C   O    doub N N 270 
MET C   OXT  sing N N 271 
MET CB  CG   sing N N 272 
MET CB  HB2  sing N N 273 
MET CB  HB3  sing N N 274 
MET CG  SD   sing N N 275 
MET CG  HG2  sing N N 276 
MET CG  HG3  sing N N 277 
MET SD  CE   sing N N 278 
MET CE  HE1  sing N N 279 
MET CE  HE2  sing N N 280 
MET CE  HE3  sing N N 281 
MET OXT HXT  sing N N 282 
PGE C1  O1   sing N N 283 
PGE C1  C2   sing N N 284 
PGE C1  H1   sing N N 285 
PGE C1  H12  sing N N 286 
PGE O1  HO1  sing N N 287 
PGE C2  O2   sing N N 288 
PGE C2  H2   sing N N 289 
PGE C2  H22  sing N N 290 
PGE O2  C3   sing N N 291 
PGE C3  C4   sing N N 292 
PGE C3  H3   sing N N 293 
PGE C3  H32  sing N N 294 
PGE C4  O3   sing N N 295 
PGE C4  H4   sing N N 296 
PGE C4  H42  sing N N 297 
PGE O4  C6   sing N N 298 
PGE O4  HO4  sing N N 299 
PGE C6  C5   sing N N 300 
PGE C6  H6   sing N N 301 
PGE C6  H62  sing N N 302 
PGE C5  O3   sing N N 303 
PGE C5  H5   sing N N 304 
PGE C5  H52  sing N N 305 
PHE N   CA   sing N N 306 
PHE N   H    sing N N 307 
PHE N   H2   sing N N 308 
PHE CA  C    sing N N 309 
PHE CA  CB   sing N N 310 
PHE CA  HA   sing N N 311 
PHE C   O    doub N N 312 
PHE C   OXT  sing N N 313 
PHE CB  CG   sing N N 314 
PHE CB  HB2  sing N N 315 
PHE CB  HB3  sing N N 316 
PHE CG  CD1  doub Y N 317 
PHE CG  CD2  sing Y N 318 
PHE CD1 CE1  sing Y N 319 
PHE CD1 HD1  sing N N 320 
PHE CD2 CE2  doub Y N 321 
PHE CD2 HD2  sing N N 322 
PHE CE1 CZ   doub Y N 323 
PHE CE1 HE1  sing N N 324 
PHE CE2 CZ   sing Y N 325 
PHE CE2 HE2  sing N N 326 
PHE CZ  HZ   sing N N 327 
PHE OXT HXT  sing N N 328 
PRO N   CA   sing N N 329 
PRO N   CD   sing N N 330 
PRO N   H    sing N N 331 
PRO CA  C    sing N N 332 
PRO CA  CB   sing N N 333 
PRO CA  HA   sing N N 334 
PRO C   O    doub N N 335 
PRO C   OXT  sing N N 336 
PRO CB  CG   sing N N 337 
PRO CB  HB2  sing N N 338 
PRO CB  HB3  sing N N 339 
PRO CG  CD   sing N N 340 
PRO CG  HG2  sing N N 341 
PRO CG  HG3  sing N N 342 
PRO CD  HD2  sing N N 343 
PRO CD  HD3  sing N N 344 
PRO OXT HXT  sing N N 345 
SER N   CA   sing N N 346 
SER N   H    sing N N 347 
SER N   H2   sing N N 348 
SER CA  C    sing N N 349 
SER CA  CB   sing N N 350 
SER CA  HA   sing N N 351 
SER C   O    doub N N 352 
SER C   OXT  sing N N 353 
SER CB  OG   sing N N 354 
SER CB  HB2  sing N N 355 
SER CB  HB3  sing N N 356 
SER OG  HG   sing N N 357 
SER OXT HXT  sing N N 358 
THR N   CA   sing N N 359 
THR N   H    sing N N 360 
THR N   H2   sing N N 361 
THR CA  C    sing N N 362 
THR CA  CB   sing N N 363 
THR CA  HA   sing N N 364 
THR C   O    doub N N 365 
THR C   OXT  sing N N 366 
THR CB  OG1  sing N N 367 
THR CB  CG2  sing N N 368 
THR CB  HB   sing N N 369 
THR OG1 HG1  sing N N 370 
THR CG2 HG21 sing N N 371 
THR CG2 HG22 sing N N 372 
THR CG2 HG23 sing N N 373 
THR OXT HXT  sing N N 374 
TRP N   CA   sing N N 375 
TRP N   H    sing N N 376 
TRP N   H2   sing N N 377 
TRP CA  C    sing N N 378 
TRP CA  CB   sing N N 379 
TRP CA  HA   sing N N 380 
TRP C   O    doub N N 381 
TRP C   OXT  sing N N 382 
TRP CB  CG   sing N N 383 
TRP CB  HB2  sing N N 384 
TRP CB  HB3  sing N N 385 
TRP CG  CD1  doub Y N 386 
TRP CG  CD2  sing Y N 387 
TRP CD1 NE1  sing Y N 388 
TRP CD1 HD1  sing N N 389 
TRP CD2 CE2  doub Y N 390 
TRP CD2 CE3  sing Y N 391 
TRP NE1 CE2  sing Y N 392 
TRP NE1 HE1  sing N N 393 
TRP CE2 CZ2  sing Y N 394 
TRP CE3 CZ3  doub Y N 395 
TRP CE3 HE3  sing N N 396 
TRP CZ2 CH2  doub Y N 397 
TRP CZ2 HZ2  sing N N 398 
TRP CZ3 CH2  sing Y N 399 
TRP CZ3 HZ3  sing N N 400 
TRP CH2 HH2  sing N N 401 
TRP OXT HXT  sing N N 402 
TYR N   CA   sing N N 403 
TYR N   H    sing N N 404 
TYR N   H2   sing N N 405 
TYR CA  C    sing N N 406 
TYR CA  CB   sing N N 407 
TYR CA  HA   sing N N 408 
TYR C   O    doub N N 409 
TYR C   OXT  sing N N 410 
TYR CB  CG   sing N N 411 
TYR CB  HB2  sing N N 412 
TYR CB  HB3  sing N N 413 
TYR CG  CD1  doub Y N 414 
TYR CG  CD2  sing Y N 415 
TYR CD1 CE1  sing Y N 416 
TYR CD1 HD1  sing N N 417 
TYR CD2 CE2  doub Y N 418 
TYR CD2 HD2  sing N N 419 
TYR CE1 CZ   doub Y N 420 
TYR CE1 HE1  sing N N 421 
TYR CE2 CZ   sing Y N 422 
TYR CE2 HE2  sing N N 423 
TYR CZ  OH   sing N N 424 
TYR OH  HH   sing N N 425 
TYR OXT HXT  sing N N 426 
VAL N   CA   sing N N 427 
VAL N   H    sing N N 428 
VAL N   H2   sing N N 429 
VAL CA  C    sing N N 430 
VAL CA  CB   sing N N 431 
VAL CA  HA   sing N N 432 
VAL C   O    doub N N 433 
VAL C   OXT  sing N N 434 
VAL CB  CG1  sing N N 435 
VAL CB  CG2  sing N N 436 
VAL CB  HB   sing N N 437 
VAL CG1 HG11 sing N N 438 
VAL CG1 HG12 sing N N 439 
VAL CG1 HG13 sing N N 440 
VAL CG2 HG21 sing N N 441 
VAL CG2 HG22 sing N N 442 
VAL CG2 HG23 sing N N 443 
VAL OXT HXT  sing N N 444 
# 
_pdbx_audit_support.funding_organization   'Foundation for Science and Technology (FCT)' 
_pdbx_audit_support.country                Portugal 
_pdbx_audit_support.grant_number           SFRH/BD/147152/2019 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_branch_list.entity_id 
_pdbx_entity_branch_list.comp_id 
_pdbx_entity_branch_list.num 
_pdbx_entity_branch_list.hetero 
2 BGC 1 n 
2 BGC 2 n 
2 BGC 3 n 
# 
_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   9FZ9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G4N 
_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]   0.008707 
_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]   0.007840 
_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]   0.005834 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N N   . SER A  1 3   ? -66.410  44.751  -63.577  1.00 71.93  ? 3   SER A N   1 
ATOM   2     C CA  . SER A  1 3   ? -67.634  44.587  -64.405  1.00 72.03  ? 3   SER A CA  1 
ATOM   3     C C   . SER A  1 3   ? -67.521  43.309  -65.237  1.00 64.35  ? 3   SER A C   1 
ATOM   4     O O   . SER A  1 3   ? -67.606  43.339  -66.457  1.00 74.80  ? 3   SER A O   1 
ATOM   5     C CB  . SER A  1 3   ? -67.862  45.821  -65.259  1.00 70.59  ? 3   SER A CB  1 
ATOM   6     O OG  . SER A  1 3   ? -68.836  45.568  -66.258  1.00 67.70  ? 3   SER A OG  1 
ATOM   7     N N   . LYS A  1 4   ? -67.363  42.175  -64.561  1.00 53.89  ? 4   LYS A N   1 
ATOM   8     C CA  . LYS A  1 4   ? -66.956  40.954  -65.227  1.00 52.50  ? 4   LYS A CA  1 
ATOM   9     C C   . LYS A  1 4   ? -68.145  40.013  -65.435  1.00 43.67  ? 4   LYS A C   1 
ATOM   10    O O   . LYS A  1 4   ? -69.143  40.127  -64.739  1.00 43.14  ? 4   LYS A O   1 
ATOM   11    C CB  . LYS A  1 4   ? -65.820  40.285  -64.444  1.00 58.35  ? 4   LYS A CB  1 
ATOM   12    C CG  . LYS A  1 4   ? -66.156  39.657  -63.104  1.00 61.41  ? 4   LYS A CG  1 
ATOM   13    C CD  . LYS A  1 4   ? -64.924  39.311  -62.272  1.00 65.98  ? 4   LYS A CD  1 
ATOM   14    C CE  . LYS A  1 4   ? -65.283  38.942  -60.857  1.00 71.48  ? 4   LYS A CE  1 
ATOM   15    N NZ  . LYS A  1 4   ? -66.264  37.854  -60.810  1.00 67.90  ? 4   LYS A NZ  1 
ATOM   16    N N   . THR A  1 5   ? -67.997  39.109  -66.410  1.00 35.94  ? 5   THR A N   1 
ATOM   17    C CA  . THR A  1 5   ? -69.022  38.189  -66.845  1.00 35.78  ? 5   THR A CA  1 
ATOM   18    C C   . THR A  1 5   ? -69.458  37.318  -65.661  1.00 37.45  ? 5   THR A C   1 
ATOM   19    O O   . THR A  1 5   ? -68.627  36.705  -65.002  1.00 37.05  ? 5   THR A O   1 
ATOM   20    C CB  . THR A  1 5   ? -68.445  37.327  -67.970  1.00 34.71  ? 5   THR A CB  1 
ATOM   21    O OG1 . THR A  1 5   ? -67.860  38.166  -68.961  1.00 31.93  ? 5   THR A OG1 1 
ATOM   22    C CG2 . THR A  1 5   ? -69.485  36.429  -68.628  1.00 34.00  ? 5   THR A CG2 1 
ATOM   23    N N   . LYS A  1 6   ? -70.766  37.272  -65.379  1.00 38.20  ? 6   LYS A N   1 
ATOM   24    C CA  . LYS A  1 6   ? -71.300  36.332  -64.403  1.00 42.17  ? 6   LYS A CA  1 
ATOM   25    C C   . LYS A  1 6   ? -71.601  35.007  -65.119  1.00 37.49  ? 6   LYS A C   1 
ATOM   26    O O   . LYS A  1 6   ? -72.335  34.984  -66.121  1.00 33.89  ? 6   LYS A O   1 
ATOM   27    C CB  . LYS A  1 6   ? -72.513  36.990  -63.716  1.00 49.35  ? 6   LYS A CB  1 
ATOM   28    C CG  . LYS A  1 6   ? -73.327  36.102  -62.758  1.00 58.53  ? 6   LYS A CG  1 
ATOM   29    C CD  . LYS A  1 6   ? -74.395  36.766  -61.876  1.00 68.83  ? 6   LYS A CD  1 
ATOM   30    C CE  . LYS A  1 6   ? -75.431  37.672  -62.560  1.00 77.56  ? 6   LYS A CE  1 
ATOM   31    N NZ  . LYS A  1 6   ? -76.469  37.067  -63.418  1.00 73.81  ? 6   LYS A NZ  1 
ATOM   32    N N   . ILE A  1 7   ? -70.995  33.919  -64.624  1.00 34.98  ? 7   ILE A N   1 
ATOM   33    C CA  . ILE A  1 7   ? -71.230  32.592  -65.171  1.00 33.76  ? 7   ILE A CA  1 
ATOM   34    C C   . ILE A  1 7   ? -72.075  31.838  -64.168  1.00 34.62  ? 7   ILE A C   1 
ATOM   35    O O   . ILE A  1 7   ? -71.632  31.669  -63.038  1.00 33.79  ? 7   ILE A O   1 
ATOM   36    C CB  . ILE A  1 7   ? -69.930  31.796  -65.427  1.00 33.09  ? 7   ILE A CB  1 
ATOM   37    C CG1 . ILE A  1 7   ? -69.010  32.487  -66.429  1.00 32.94  ? 7   ILE A CG1 1 
ATOM   38    C CG2 . ILE A  1 7   ? -70.260  30.373  -65.860  1.00 31.02  ? 7   ILE A CG2 1 
ATOM   39    C CD1 . ILE A  1 7   ? -67.624  31.894  -66.513  1.00 31.96  ? 7   ILE A CD1 1 
ATOM   40    N N   . GLU A  1 8   ? -73.233  31.337  -64.619  1.00 36.96  ? 8   GLU A N   1 
ATOM   41    C CA  . GLU A  1 8   ? -74.093  30.502  -63.787  1.00 40.13  ? 8   GLU A CA  1 
ATOM   42    C C   . GLU A  1 8   ? -74.410  29.207  -64.516  1.00 36.45  ? 8   GLU A C   1 
ATOM   43    O O   . GLU A  1 8   ? -74.801  29.210  -65.677  1.00 33.77  ? 8   GLU A O   1 
ATOM   44    C CB  . GLU A  1 8   ? -75.440  31.115  -63.414  1.00 44.66  ? 8   GLU A CB  1 
ATOM   45    C CG  . GLU A  1 8   ? -75.293  32.252  -62.418  1.00 53.36  ? 8   GLU A CG  1 
ATOM   46    C CD  . GLU A  1 8   ? -76.367  33.318  -62.591  1.00 60.26  ? 8   GLU A CD  1 
ATOM   47    O OE1 . GLU A  1 8   ? -76.318  34.173  -63.521  1.00 58.08  ? 8   GLU A OE1 1 
ATOM   48    O OE2 . GLU A  1 8   ? -77.292  33.242  -61.773  1.00 64.40  ? 8   GLU A OE2 1 
ATOM   49    N N   . LEU A  1 9   ? -74.260  28.107  -63.786  1.00 36.80  ? 9   LEU A N   1 
ATOM   50    C CA  . LEU A  1 9   ? -74.588  26.791  -64.301  1.00 35.39  ? 9   LEU A CA  1 
ATOM   51    C C   . LEU A  1 9   ? -75.942  26.381  -63.739  1.00 35.20  ? 9   LEU A C   1 
ATOM   52    O O   . LEU A  1 9   ? -76.066  26.242  -62.538  1.00 35.88  ? 9   LEU A O   1 
ATOM   53    C CB  . LEU A  1 9   ? -73.474  25.847  -63.856  1.00 34.01  ? 9   LEU A CB  1 
ATOM   54    C CG  . LEU A  1 9   ? -72.046  26.292  -64.183  1.00 33.64  ? 9   LEU A CG  1 
ATOM   55    C CD1 . LEU A  1 9   ? -71.070  25.205  -63.802  1.00 34.16  ? 9   LEU A CD1 1 
ATOM   56    C CD2 . LEU A  1 9   ? -71.854  26.637  -65.634  1.00 32.37  ? 9   LEU A CD2 1 
ATOM   57    N N   . LYS A  1 10  ? -76.955  26.205  -64.589  1.00 37.16  ? 10  LYS A N   1 
ATOM   58    C CA  . LYS A  1 10  ? -78.199  25.586  -64.154  1.00 40.01  ? 10  LYS A CA  1 
ATOM   59    C C   . LYS A  1 10  ? -79.004  25.104  -65.361  1.00 37.31  ? 10  LYS A C   1 
ATOM   60    O O   . LYS A  1 10  ? -78.761  25.541  -66.488  1.00 33.37  ? 10  LYS A O   1 
ATOM   61    C CB  . LYS A  1 10  ? -79.052  26.458  -63.225  1.00 47.51  ? 10  LYS A CB  1 
ATOM   62    C CG  . LYS A  1 10  ? -79.722  27.684  -63.818  1.00 55.74  ? 10  LYS A CG  1 
ATOM   63    C CD  . LYS A  1 10  ? -80.632  28.440  -62.838  1.00 63.37  ? 10  LYS A CD  1 
ATOM   64    C CE  . LYS A  1 10  ? -81.718  27.611  -62.165  1.00 67.78  ? 10  LYS A CE  1 
ATOM   65    N NZ  . LYS A  1 10  ? -82.756  28.494  -61.613  1.00 67.76  ? 10  LYS A NZ  1 
ATOM   66    N N   . ASP A  1 11  ? -79.924  24.158  -65.097  1.00 35.94  ? 11  ASP A N   1 
ATOM   67    C CA  . ASP A  1 11  ? -80.631  23.422  -66.126  1.00 36.06  ? 11  ASP A CA  1 
ATOM   68    C C   . ASP A  1 11  ? -79.652  22.759  -67.089  1.00 33.03  ? 11  ASP A C   1 
ATOM   69    O O   . ASP A  1 11  ? -79.935  22.672  -68.271  1.00 31.78  ? 11  ASP A O   1 
ATOM   70    C CB  . ASP A  1 11  ? -81.616  24.347  -66.811  1.00 39.80  ? 11  ASP A CB  1 
ATOM   71    C CG  . ASP A  1 11  ? -82.442  25.154  -65.820  1.00 44.83  ? 11  ASP A CG  1 
ATOM   72    O OD1 . ASP A  1 11  ? -83.028  24.530  -64.921  1.00 45.84  ? 11  ASP A OD1 1 
ATOM   73    O OD2 . ASP A  1 11  ? -82.435  26.401  -65.919  1.00 54.43  ? 11  ASP A OD2 1 
ATOM   74    N N   . ASN A  1 12  ? -78.476  22.382  -66.582  1.00 32.31  ? 12  ASN A N   1 
ATOM   75    C CA  . ASN A  1 12  ? -77.395  21.833  -67.384  1.00 33.80  ? 12  ASN A CA  1 
ATOM   76    C C   . ASN A  1 12  ? -76.978  22.735  -68.563  1.00 31.75  ? 12  ASN A C   1 
ATOM   77    O O   . ASN A  1 12  ? -76.478  22.258  -69.572  1.00 30.23  ? 12  ASN A O   1 
ATOM   78    C CB  . ASN A  1 12  ? -77.745  20.407  -67.809  1.00 35.41  ? 12  ASN A CB  1 
ATOM   79    C CG  . ASN A  1 12  ? -78.275  19.585  -66.648  1.00 37.58  ? 12  ASN A CG  1 
ATOM   80    O OD1 . ASN A  1 12  ? -77.794  19.673  -65.511  1.00 40.85  ? 12  ASN A OD1 1 
ATOM   81    N ND2 . ASN A  1 12  ? -79.295  18.787  -66.891  1.00 36.78  ? 12  ASN A ND2 1 
ATOM   82    N N   . TRP A  1 13  ? -77.104  24.048  -68.428  1.00 31.46  ? 13  TRP A N   1 
ATOM   83    C CA  . TRP A  1 13  ? -76.515  24.987  -69.384  1.00 33.00  ? 13  TRP A CA  1 
ATOM   84    C C   . TRP A  1 13  ? -75.513  25.925  -68.702  1.00 31.27  ? 13  TRP A C   1 
ATOM   85    O O   . TRP A  1 13  ? -75.724  26.348  -67.569  1.00 31.63  ? 13  TRP A O   1 
ATOM   86    C CB  . TRP A  1 13  ? -77.622  25.849  -70.016  1.00 33.94  ? 13  TRP A CB  1 
ATOM   87    C CG  . TRP A  1 13  ? -78.326  25.223  -71.180  1.00 32.44  ? 13  TRP A CG  1 
ATOM   88    C CD1 . TRP A  1 13  ? -79.343  24.321  -71.149  1.00 32.47  ? 13  TRP A CD1 1 
ATOM   89    C CD2 . TRP A  1 13  ? -78.072  25.522  -72.564  1.00 32.15  ? 13  TRP A CD2 1 
ATOM   90    N NE1 . TRP A  1 13  ? -79.711  24.003  -72.426  1.00 33.10  ? 13  TRP A NE1 1 
ATOM   91    C CE2 . TRP A  1 13  ? -78.960  24.728  -73.311  1.00 31.74  ? 13  TRP A CE2 1 
ATOM   92    C CE3 . TRP A  1 13  ? -77.202  26.396  -73.229  1.00 32.18  ? 13  TRP A CE3 1 
ATOM   93    C CZ2 . TRP A  1 13  ? -78.986  24.762  -74.696  1.00 31.03  ? 13  TRP A CZ2 1 
ATOM   94    C CZ3 . TRP A  1 13  ? -77.258  26.461  -74.602  1.00 31.82  ? 13  TRP A CZ3 1 
ATOM   95    C CH2 . TRP A  1 13  ? -78.127  25.637  -75.322  1.00 30.73  ? 13  TRP A CH2 1 
ATOM   96    N N   . TYR A  1 14  ? -74.481  26.351  -69.435  1.00 30.58  ? 14  TYR A N   1 
ATOM   97    C CA  . TYR A  1 14  ? -73.781  27.568  -69.039  1.00 29.64  ? 14  TYR A CA  1 
ATOM   98    C C   . TYR A  1 14  ? -74.653  28.774  -69.374  1.00 29.56  ? 14  TYR A C   1 
ATOM   99    O O   . TYR A  1 14  ? -75.242  28.845  -70.447  1.00 28.28  ? 14  TYR A O   1 
ATOM   100   C CB  . TYR A  1 14  ? -72.481  27.857  -69.790  1.00 29.16  ? 14  TYR A CB  1 
ATOM   101   C CG  . TYR A  1 14  ? -71.271  26.995  -69.496  1.00 28.71  ? 14  TYR A CG  1 
ATOM   102   C CD1 . TYR A  1 14  ? -71.266  25.631  -69.790  1.00 29.04  ? 14  TYR A CD1 1 
ATOM   103   C CD2 . TYR A  1 14  ? -70.095  27.560  -69.042  1.00 28.56  ? 14  TYR A CD2 1 
ATOM   104   C CE1 . TYR A  1 14  ? -70.140  24.853  -69.588  1.00 27.46  ? 14  TYR A CE1 1 
ATOM   105   C CE2 . TYR A  1 14  ? -68.959  26.787  -68.851  1.00 29.24  ? 14  TYR A CE2 1 
ATOM   106   C CZ  . TYR A  1 14  ? -68.969  25.427  -69.125  1.00 28.19  ? 14  TYR A CZ  1 
ATOM   107   O OH  . TYR A  1 14  ? -67.828  24.662  -68.911  1.00 27.78  ? 14  TYR A OH  1 
ATOM   108   N N   . HIS A  1 15  ? -74.680  29.742  -68.460  1.00 32.07  ? 15  HIS A N   1 
ATOM   109   C CA  . HIS A  1 15  ? -75.254  31.052  -68.699  1.00 32.74  ? 15  HIS A CA  1 
ATOM   110   C C   . HIS A  1 15  ? -74.162  32.133  -68.538  1.00 32.49  ? 15  HIS A C   1 
ATOM   111   O O   . HIS A  1 15  ? -73.444  32.142  -67.553  1.00 31.99  ? 15  HIS A O   1 
ATOM   112   C CB  . HIS A  1 15  ? -76.376  31.272  -67.680  1.00 33.75  ? 15  HIS A CB  1 
ATOM   113   C CG  . HIS A  1 15  ? -77.549  30.351  -67.707  1.00 35.57  ? 15  HIS A CG  1 
ATOM   114   N ND1 . HIS A  1 15  ? -77.556  29.032  -67.276  1.00 33.30  ? 15  HIS A ND1 1 
ATOM   115   C CD2 . HIS A  1 15  ? -78.849  30.641  -68.021  1.00 35.24  ? 15  HIS A CD2 1 
ATOM   116   C CE1 . HIS A  1 15  ? -78.802  28.570  -67.336  1.00 31.33  ? 15  HIS A CE1 1 
ATOM   117   N NE2 . HIS A  1 15  ? -79.599  29.518  -67.794  1.00 31.96  ? 15  HIS A NE2 1 
ATOM   118   N N   . LEU A  1 16  ? -74.014  33.049  -69.508  1.00 32.93  ? 16  LEU A N   1 
ATOM   119   C CA  . LEU A  1 16  ? -73.162  34.220  -69.373  1.00 32.48  ? 16  LEU A CA  1 
ATOM   120   C C   . LEU A  1 16  ? -74.087  35.434  -69.274  1.00 32.87  ? 16  LEU A C   1 
ATOM   121   O O   . LEU A  1 16  ? -74.848  35.709  -70.198  1.00 32.01  ? 16  LEU A O   1 
ATOM   122   C CB  . LEU A  1 16  ? -72.204  34.423  -70.544  1.00 31.35  ? 16  LEU A CB  1 
ATOM   123   C CG  . LEU A  1 16  ? -71.361  33.235  -70.978  1.00 32.82  ? 16  LEU A CG  1 
ATOM   124   C CD1 . LEU A  1 16  ? -70.355  33.739  -71.989  1.00 33.18  ? 16  LEU A CD1 1 
ATOM   125   C CD2 . LEU A  1 16  ? -70.675  32.509  -69.854  1.00 34.08  ? 16  LEU A CD2 1 
ATOM   126   N N   . ASP A  1 17  ? -74.044  36.121  -68.140  1.00 33.76  ? 17  ASP A N   1 
ATOM   127   C CA  . ASP A  1 17  ? -74.823  37.343  -67.930  1.00 36.02  ? 17  ASP A CA  1 
ATOM   128   C C   . ASP A  1 17  ? -76.314  37.053  -68.154  1.00 35.75  ? 17  ASP A C   1 
ATOM   129   O O   . ASP A  1 17  ? -77.033  37.836  -68.764  1.00 35.22  ? 17  ASP A O   1 
ATOM   130   C CB  . ASP A  1 17  ? -74.274  38.550  -68.704  1.00 36.34  ? 17  ASP A CB  1 
ATOM   131   C CG  . ASP A  1 17  ? -72.822  38.953  -68.425  1.00 37.42  ? 17  ASP A CG  1 
ATOM   132   O OD1 . ASP A  1 17  ? -72.432  38.967  -67.254  1.00 39.41  ? 17  ASP A OD1 1 
ATOM   133   O OD2 . ASP A  1 17  ? -72.049  39.198  -69.376  1.00 36.85  ? 17  ASP A OD2 1 
ATOM   134   N N   . GLY A  1 18  ? -76.780  35.927  -67.608  1.00 37.26  ? 18  GLY A N   1 
ATOM   135   C CA  . GLY A  1 18  ? -78.193  35.586  -67.597  1.00 38.55  ? 18  GLY A CA  1 
ATOM   136   C C   . GLY A  1 18  ? -78.649  34.825  -68.846  1.00 39.78  ? 18  GLY A C   1 
ATOM   137   O O   . GLY A  1 18  ? -79.729  34.243  -68.802  1.00 41.14  ? 18  GLY A O   1 
ATOM   138   N N   . GLU A  1 19  ? -77.833  34.806  -69.921  1.00 39.45  ? 19  GLU A N   1 
ATOM   139   C CA  . GLU A  1 19  ? -78.207  34.252  -71.218  1.00 38.85  ? 19  GLU A CA  1 
ATOM   140   C C   . GLU A  1 19  ? -77.619  32.845  -71.380  1.00 38.43  ? 19  GLU A C   1 
ATOM   141   O O   . GLU A  1 19  ? -76.410  32.618  -71.194  1.00 33.25  ? 19  GLU A O   1 
ATOM   142   C CB  . GLU A  1 19  ? -77.600  35.070  -72.367  1.00 43.99  ? 19  GLU A CB  1 
ATOM   143   C CG  . GLU A  1 19  ? -78.070  36.519  -72.524  1.00 49.27  ? 19  GLU A CG  1 
ATOM   144   C CD  . GLU A  1 19  ? -79.585  36.658  -72.610  1.00 54.85  ? 19  GLU A CD  1 
ATOM   145   O OE1 . GLU A  1 19  ? -80.294  36.067  -73.467  1.00 54.32  ? 19  GLU A OE1 1 
ATOM   146   O OE2 . GLU A  1 19  ? -80.071  37.357  -71.711  1.00 63.14  ? 19  GLU A OE2 1 
ATOM   147   N N   . LYS A  1 20  ? -78.464  31.887  -71.785  1.00 36.72  ? 20  LYS A N   1 
ATOM   148   C CA  . LYS A  1 20  ? -77.934  30.567  -72.085  1.00 35.96  ? 20  LYS A CA  1 
ATOM   149   C C   . LYS A  1 20  ? -76.944  30.703  -73.238  1.00 32.76  ? 20  LYS A C   1 
ATOM   150   O O   . LYS A  1 20  ? -77.192  31.473  -74.169  1.00 31.28  ? 20  LYS A O   1 
ATOM   151   C CB  . LYS A  1 20  ? -79.020  29.537  -72.411  1.00 38.12  ? 20  LYS A CB  1 
ATOM   152   C CG  . LYS A  1 20  ? -79.954  29.258  -71.247  1.00 40.76  ? 20  LYS A CG  1 
ATOM   153   C CD  . LYS A  1 20  ? -80.810  28.020  -71.409  1.00 43.10  ? 20  LYS A CD  1 
ATOM   154   C CE  . LYS A  1 20  ? -81.701  27.859  -70.235  1.00 46.94  ? 20  LYS A CE  1 
ATOM   155   N NZ  . LYS A  1 20  ? -82.614  26.741  -70.460  1.00 50.23  ? 20  LYS A NZ  1 
ATOM   156   N N   . TYR A  1 21  ? -75.843  29.945  -73.156  1.00 29.17  ? 21  TYR A N   1 
ATOM   157   C CA  . TYR A  1 21  ? -74.707  30.139  -74.031  1.00 28.13  ? 21  TYR A CA  1 
ATOM   158   C C   . TYR A  1 21  ? -74.132  28.788  -74.445  1.00 28.23  ? 21  TYR A C   1 
ATOM   159   O O   . TYR A  1 21  ? -73.434  28.140  -73.667  1.00 26.62  ? 21  TYR A O   1 
ATOM   160   C CB  . TYR A  1 21  ? -73.686  31.011  -73.297  1.00 28.89  ? 21  TYR A CB  1 
ATOM   161   C CG  . TYR A  1 21  ? -72.518  31.475  -74.159  1.00 29.47  ? 21  TYR A CG  1 
ATOM   162   C CD1 . TYR A  1 21  ? -71.353  30.707  -74.305  1.00 27.93  ? 21  TYR A CD1 1 
ATOM   163   C CD2 . TYR A  1 21  ? -72.597  32.685  -74.839  1.00 29.41  ? 21  TYR A CD2 1 
ATOM   164   C CE1 . TYR A  1 21  ? -70.288  31.167  -75.064  1.00 27.51  ? 21  TYR A CE1 1 
ATOM   165   C CE2 . TYR A  1 21  ? -71.542  33.147  -75.611  1.00 29.39  ? 21  TYR A CE2 1 
ATOM   166   C CZ  . TYR A  1 21  ? -70.393  32.384  -75.718  1.00 28.96  ? 21  TYR A CZ  1 
ATOM   167   O OH  . TYR A  1 21  ? -69.412  32.892  -76.502  1.00 28.83  ? 21  TYR A OH  1 
ATOM   168   N N   . PHE A  1 22  ? -74.459  28.392  -75.681  1.00 27.49  ? 22  PHE A N   1 
ATOM   169   C CA  . PHE A  1 22  ? -73.875  27.231  -76.298  1.00 26.50  ? 22  PHE A CA  1 
ATOM   170   C C   . PHE A  1 22  ? -72.424  27.556  -76.650  1.00 27.20  ? 22  PHE A C   1 
ATOM   171   O O   . PHE A  1 22  ? -72.165  28.456  -77.451  1.00 25.30  ? 22  PHE A O   1 
ATOM   172   C CB  . PHE A  1 22  ? -74.644  26.785  -77.545  1.00 25.64  ? 22  PHE A CB  1 
ATOM   173   C CG  . PHE A  1 22  ? -74.333  25.342  -77.940  1.00 24.65  ? 22  PHE A CG  1 
ATOM   174   C CD1 . PHE A  1 22  ? -73.181  25.029  -78.645  1.00 24.22  ? 22  PHE A CD1 1 
ATOM   175   C CD2 . PHE A  1 22  ? -75.188  24.300  -77.579  1.00 25.12  ? 22  PHE A CD2 1 
ATOM   176   C CE1 . PHE A  1 22  ? -72.879  23.708  -78.980  1.00 25.59  ? 22  PHE A CE1 1 
ATOM   177   C CE2 . PHE A  1 22  ? -74.889  22.982  -77.911  1.00 26.07  ? 22  PHE A CE2 1 
ATOM   178   C CZ  . PHE A  1 22  ? -73.721  22.681  -78.609  1.00 24.95  ? 22  PHE A CZ  1 
ATOM   179   N N   . ILE A  1 23  ? -71.494  26.755  -76.106  1.00 27.01  ? 23  ILE A N   1 
ATOM   180   C CA  . ILE A  1 23  ? -70.077  26.951  -76.370  1.00 27.11  ? 23  ILE A CA  1 
ATOM   181   C C   . ILE A  1 23  ? -69.767  26.288  -77.696  1.00 27.69  ? 23  ILE A C   1 
ATOM   182   O O   . ILE A  1 23  ? -69.797  25.056  -77.798  1.00 30.12  ? 23  ILE A O   1 
ATOM   183   C CB  . ILE A  1 23  ? -69.191  26.416  -75.226  1.00 27.26  ? 23  ILE A CB  1 
ATOM   184   C CG1 . ILE A  1 23  ? -69.554  27.083  -73.892  1.00 27.82  ? 23  ILE A CG1 1 
ATOM   185   C CG2 . ILE A  1 23  ? -67.704  26.585  -75.530  1.00 26.65  ? 23  ILE A CG2 1 
ATOM   186   C CD1 . ILE A  1 23  ? -69.037  26.334  -72.679  1.00 28.61  ? 23  ILE A CD1 1 
ATOM   187   N N   . LYS A  1 24  ? -69.475  27.135  -78.684  1.00 28.13  ? 24  LYS A N   1 
ATOM   188   C CA  . LYS A  1 24  ? -68.998  26.721  -79.989  1.00 28.84  ? 24  LYS A CA  1 
ATOM   189   C C   . LYS A  1 24  ? -67.478  26.885  -80.063  1.00 30.03  ? 24  LYS A C   1 
ATOM   190   O O   . LYS A  1 24  ? -66.937  27.769  -80.732  1.00 31.29  ? 24  LYS A O   1 
ATOM   191   C CB  . LYS A  1 24  ? -69.777  27.551  -81.016  1.00 30.24  ? 24  LYS A CB  1 
ATOM   192   C CG  . LYS A  1 24  ? -71.294  27.372  -80.956  1.00 30.52  ? 24  LYS A CG  1 
ATOM   193   C CD  . LYS A  1 24  ? -71.994  27.924  -82.198  1.00 31.72  ? 24  LYS A CD  1 
ATOM   194   C CE  . LYS A  1 24  ? -71.984  29.376  -82.332  1.00 33.63  ? 24  LYS A CE  1 
ATOM   195   N NZ  . LYS A  1 24  ? -72.577  29.884  -83.585  1.00 35.11  ? 24  LYS A NZ  1 
ATOM   196   N N   . ALA A  1 25  ? -66.763  25.987  -79.401  1.00 29.21  ? 25  ALA A N   1 
ATOM   197   C CA  . ALA A  1 25  ? -65.320  26.093  -79.366  1.00 28.27  ? 25  ALA A CA  1 
ATOM   198   C C   . ALA A  1 25  ? -64.679  25.311  -80.509  1.00 28.63  ? 25  ALA A C   1 
ATOM   199   O O   . ALA A  1 25  ? -65.348  24.660  -81.326  1.00 28.40  ? 25  ALA A O   1 
ATOM   200   C CB  . ALA A  1 25  ? -64.815  25.633  -78.021  1.00 29.07  ? 25  ALA A CB  1 
ATOM   201   N N   . ILE A  1 26  ? -63.347  25.449  -80.564  1.00 27.64  ? 26  ILE A N   1 
ATOM   202   C CA  . ILE A  1 26  ? -62.482  24.598  -81.356  1.00 26.18  ? 26  ILE A CA  1 
ATOM   203   C C   . ILE A  1 26  ? -61.182  24.448  -80.578  1.00 27.43  ? 26  ILE A C   1 
ATOM   204   O O   . ILE A  1 26  ? -60.741  25.372  -79.885  1.00 26.87  ? 26  ILE A O   1 
ATOM   205   C CB  . ILE A  1 26  ? -62.213  25.189  -82.752  1.00 25.91  ? 26  ILE A CB  1 
ATOM   206   C CG1 . ILE A  1 26  ? -61.508  24.173  -83.644  1.00 24.36  ? 26  ILE A CG1 1 
ATOM   207   C CG2 . ILE A  1 26  ? -61.436  26.514  -82.647  1.00 26.19  ? 26  ILE A CG2 1 
ATOM   208   C CD1 . ILE A  1 26  ? -61.283  24.604  -85.076  1.00 24.63  ? 26  ILE A CD1 1 
ATOM   209   N N   . GLY A  1 27  ? -60.578  23.266  -80.670  1.00 27.53  ? 27  GLY A N   1 
ATOM   210   C CA  . GLY A  1 27  ? -59.283  23.086  -80.033  1.00 28.41  ? 27  GLY A CA  1 
ATOM   211   C C   . GLY A  1 27  ? -58.234  23.921  -80.762  1.00 26.41  ? 27  GLY A C   1 
ATOM   212   O O   . GLY A  1 27  ? -58.193  23.939  -81.995  1.00 26.85  ? 27  GLY A O   1 
ATOM   213   N N   . TYR A  1 28  ? -57.360  24.563  -80.001  1.00 25.58  ? 28  TYR A N   1 
ATOM   214   C CA  . TYR A  1 28  ? -56.400  25.471  -80.606  1.00 28.10  ? 28  TYR A CA  1 
ATOM   215   C C   . TYR A  1 28  ? -55.051  25.319  -79.905  1.00 26.75  ? 28  TYR A C   1 
ATOM   216   O O   . TYR A  1 28  ? -54.963  25.611  -78.728  1.00 27.18  ? 28  TYR A O   1 
ATOM   217   C CB  . TYR A  1 28  ? -56.941  26.914  -80.540  1.00 26.27  ? 28  TYR A CB  1 
ATOM   218   C CG  . TYR A  1 28  ? -55.911  27.940  -80.988  1.00 27.93  ? 28  TYR A CG  1 
ATOM   219   C CD1 . TYR A  1 28  ? -55.296  27.857  -82.235  1.00 27.94  ? 28  TYR A CD1 1 
ATOM   220   C CD2 . TYR A  1 28  ? -55.513  28.975  -80.148  1.00 29.21  ? 28  TYR A CD2 1 
ATOM   221   C CE1 . TYR A  1 28  ? -54.368  28.805  -82.644  1.00 28.66  ? 28  TYR A CE1 1 
ATOM   222   C CE2 . TYR A  1 28  ? -54.564  29.902  -80.542  1.00 27.87  ? 28  TYR A CE2 1 
ATOM   223   C CZ  . TYR A  1 28  ? -53.976  29.806  -81.784  1.00 28.17  ? 28  TYR A CZ  1 
ATOM   224   O OH  . TYR A  1 28  ? -53.017  30.713  -82.164  1.00 32.81  ? 28  TYR A OH  1 
ATOM   225   N N   . GLU A  1 29  ? -54.000  24.947  -80.641  1.00 26.42  ? 29  GLU A N   1 
ATOM   226   C CA  . GLU A  1 29  ? -52.660  24.871  -80.056  1.00 27.89  ? 29  GLU A CA  1 
ATOM   227   C C   . GLU A  1 29  ? -51.685  25.810  -80.785  1.00 27.54  ? 29  GLU A C   1 
ATOM   228   O O   . GLU A  1 29  ? -51.277  25.533  -81.926  1.00 27.64  ? 29  GLU A O   1 
ATOM   229   C CB  . GLU A  1 29  ? -52.162  23.413  -80.081  1.00 26.94  ? 29  GLU A CB  1 
ATOM   230   C CG  . GLU A  1 29  ? -50.774  23.207  -79.463  1.00 28.17  ? 29  GLU A CG  1 
ATOM   231   C CD  . GLU A  1 29  ? -50.376  21.728  -79.301  1.00 27.76  ? 29  GLU A CD  1 
ATOM   232   O OE1 . GLU A  1 29  ? -50.332  21.012  -80.341  1.00 26.51  ? 29  GLU A OE1 1 
ATOM   233   O OE2 . GLU A  1 29  ? -50.130  21.306  -78.143  1.00 24.55  ? 29  GLU A OE2 1 
ATOM   234   N N   . ILE A  1 30  ? -51.292  26.901  -80.112  1.00 27.09  ? 30  ILE A N   1 
ATOM   235   C CA  . ILE A  1 30  ? -50.191  27.745  -80.567  1.00 27.24  ? 30  ILE A CA  1 
ATOM   236   C C   . ILE A  1 30  ? -48.880  27.023  -80.247  1.00 29.14  ? 30  ILE A C   1 
ATOM   237   O O   . ILE A  1 30  ? -48.794  26.215  -79.316  1.00 28.92  ? 30  ILE A O   1 
ATOM   238   C CB  . ILE A  1 30  ? -50.220  29.130  -79.903  1.00 27.30  ? 30  ILE A CB  1 
ATOM   239   C CG1 . ILE A  1 30  ? -49.311  30.173  -80.578  1.00 27.31  ? 30  ILE A CG1 1 
ATOM   240   C CG2 . ILE A  1 30  ? -49.851  29.010  -78.424  1.00 27.36  ? 30  ILE A CG2 1 
ATOM   241   C CD1 . ILE A  1 30  ? -49.644  30.513  -82.013  1.00 27.49  ? 30  ILE A CD1 1 
ATOM   242   N N   . GLY A  1 31  ? -47.873  27.318  -81.064  1.00 31.15  ? 31  GLY A N   1 
ATOM   243   C CA  . GLY A  1 31  ? -46.531  26.797  -80.886  1.00 31.42  ? 31  GLY A CA  1 
ATOM   244   C C   . GLY A  1 31  ? -46.367  25.421  -81.536  1.00 31.22  ? 31  GLY A C   1 
ATOM   245   O O   . GLY A  1 31  ? -45.450  24.692  -81.149  1.00 33.73  ? 31  GLY A O   1 
ATOM   246   N N   . ALA A  1 32  ? -47.224  25.096  -82.528  1.00 29.10  ? 32  ALA A N   1 
ATOM   247   C CA  . ALA A  1 32  ? -47.252  23.776  -83.160  1.00 28.76  ? 32  ALA A CA  1 
ATOM   248   C C   . ALA A  1 32  ? -47.166  23.860  -84.694  1.00 29.13  ? 32  ALA A C   1 
ATOM   249   O O   . ALA A  1 32  ? -47.631  22.969  -85.405  1.00 28.20  ? 32  ALA A O   1 
ATOM   250   C CB  . ALA A  1 32  ? -48.485  23.007  -82.707  1.00 27.58  ? 32  ALA A CB  1 
ATOM   251   N N   . ARG A  1 33  ? -46.526  24.916  -85.217  1.00 30.41  ? 33  ARG A N   1 
ATOM   252   C CA  . ARG A  1 33  ? -46.222  25.011  -86.632  1.00 30.70  ? 33  ARG A CA  1 
ATOM   253   C C   . ARG A  1 33  ? -45.229  23.916  -86.969  1.00 32.25  ? 33  ARG A C   1 
ATOM   254   O O   . ARG A  1 33  ? -44.622  23.327  -86.069  1.00 33.30  ? 33  ARG A O   1 
ATOM   255   C CB  . ARG A  1 33  ? -45.560  26.353  -86.997  1.00 32.78  ? 33  ARG A CB  1 
ATOM   256   C CG  . ARG A  1 33  ? -46.495  27.375  -87.622  1.00 30.81  ? 33  ARG A CG  1 
ATOM   257   C CD  . ARG A  1 33  ? -47.775  27.470  -86.814  1.00 30.24  ? 33  ARG A CD  1 
ATOM   258   N NE  . ARG A  1 33  ? -48.662  28.477  -87.406  1.00 31.96  ? 33  ARG A NE  1 
ATOM   259   C CZ  . ARG A  1 33  ? -49.651  29.115  -86.787  1.00 32.50  ? 33  ARG A CZ  1 
ATOM   260   N NH1 . ARG A  1 33  ? -50.057  28.764  -85.572  1.00 31.71  ? 33  ARG A NH1 1 
ATOM   261   N NH2 . ARG A  1 33  ? -50.253  30.110  -87.414  1.00 35.47  ? 33  ARG A NH2 1 
ATOM   262   N N   . PRO A  1 34  ? -45.092  23.554  -88.260  1.00 32.77  ? 34  PRO A N   1 
ATOM   263   C CA  . PRO A  1 34  ? -44.062  22.589  -88.666  1.00 35.00  ? 34  PRO A CA  1 
ATOM   264   C C   . PRO A  1 34  ? -42.745  23.098  -88.087  1.00 34.48  ? 34  PRO A C   1 
ATOM   265   O O   . PRO A  1 34  ? -42.568  24.306  -87.967  1.00 36.60  ? 34  PRO A O   1 
ATOM   266   C CB  . PRO A  1 34  ? -44.097  22.607  -90.196  1.00 34.18  ? 34  PRO A CB  1 
ATOM   267   C CG  . PRO A  1 34  ? -45.499  23.115  -90.519  1.00 32.64  ? 34  PRO A CG  1 
ATOM   268   C CD  . PRO A  1 34  ? -45.941  24.009  -89.368  1.00 31.08  ? 34  PRO A CD  1 
ATOM   269   N N   . GLY A  1 35  ? -41.904  22.185  -87.592  1.00 35.27  ? 35  GLY A N   1 
ATOM   270   C CA  . GLY A  1 35  ? -40.610  22.560  -87.020  1.00 34.75  ? 35  GLY A CA  1 
ATOM   271   C C   . GLY A  1 35  ? -40.700  22.993  -85.551  1.00 33.87  ? 35  GLY A C   1 
ATOM   272   O O   . GLY A  1 35  ? -39.692  23.279  -84.944  1.00 33.23  ? 35  GLY A O   1 
ATOM   273   N N   . GLN A  1 36  ? -41.902  23.005  -84.943  1.00 34.28  ? 36  GLN A N   1 
ATOM   274   C CA  . GLN A  1 36  ? -42.061  23.442  -83.559  1.00 32.19  ? 36  GLN A CA  1 
ATOM   275   C C   . GLN A  1 36  ? -42.600  22.301  -82.696  1.00 31.40  ? 36  GLN A C   1 
ATOM   276   O O   . GLN A  1 36  ? -43.387  21.498  -83.159  1.00 33.69  ? 36  GLN A O   1 
ATOM   277   C CB  . GLN A  1 36  ? -43.039  24.619  -83.447  1.00 30.04  ? 36  GLN A CB  1 
ATOM   278   C CG  . GLN A  1 36  ? -42.703  25.845  -84.304  1.00 29.08  ? 36  GLN A CG  1 
ATOM   279   C CD  . GLN A  1 36  ? -43.544  27.056  -83.943  1.00 27.79  ? 36  GLN A CD  1 
ATOM   280   O OE1 . GLN A  1 36  ? -44.761  26.981  -83.768  1.00 29.24  ? 36  GLN A OE1 1 
ATOM   281   N NE2 . GLN A  1 36  ? -42.938  28.206  -83.791  1.00 27.85  ? 36  GLN A NE2 1 
ATOM   282   N N   . ALA A  1 37  ? -42.244  22.281  -81.413  1.00 31.39  ? 37  ALA A N   1 
ATOM   283   C CA  . ALA A  1 37  ? -42.839  21.366  -80.455  1.00 31.74  ? 37  ALA A CA  1 
ATOM   284   C C   . ALA A  1 37  ? -43.169  22.143  -79.176  1.00 32.54  ? 37  ALA A C   1 
ATOM   285   O O   . ALA A  1 37  ? -42.264  22.562  -78.433  1.00 35.02  ? 37  ALA A O   1 
ATOM   286   C CB  . ALA A  1 37  ? -41.855  20.229  -80.178  1.00 33.07  ? 37  ALA A CB  1 
ATOM   287   N N   . PRO A  1 38  ? -44.456  22.384  -78.858  1.00 31.19  ? 38  PRO A N   1 
ATOM   288   C CA  . PRO A  1 38  ? -44.799  23.291  -77.760  1.00 31.79  ? 38  PRO A CA  1 
ATOM   289   C C   . PRO A  1 38  ? -44.335  22.884  -76.365  1.00 32.25  ? 38  PRO A C   1 
ATOM   290   O O   . PRO A  1 38  ? -44.148  23.751  -75.518  1.00 31.51  ? 38  PRO A O   1 
ATOM   291   C CB  . PRO A  1 38  ? -46.334  23.379  -77.836  1.00 32.46  ? 38  PRO A CB  1 
ATOM   292   C CG  . PRO A  1 38  ? -46.741  22.098  -78.559  1.00 31.30  ? 38  PRO A CG  1 
ATOM   293   C CD  . PRO A  1 38  ? -45.628  21.828  -79.553  1.00 31.15  ? 38  PRO A CD  1 
ATOM   294   N N   . TYR A  1 39  ? -44.112  21.585  -76.137  1.00 33.70  ? 39  TYR A N   1 
ATOM   295   C CA  . TYR A  1 39  ? -43.665  21.106  -74.833  1.00 36.26  ? 39  TYR A CA  1 
ATOM   296   C C   . TYR A  1 39  ? -42.137  21.002  -74.714  1.00 37.51  ? 39  TYR A C   1 
ATOM   297   O O   . TYR A  1 39  ? -41.648  20.694  -73.638  1.00 36.55  ? 39  TYR A O   1 
ATOM   298   C CB  . TYR A  1 39  ? -44.351  19.777  -74.478  1.00 33.96  ? 39  TYR A CB  1 
ATOM   299   C CG  . TYR A  1 39  ? -45.855  19.961  -74.377  1.00 33.18  ? 39  TYR A CG  1 
ATOM   300   C CD1 . TYR A  1 39  ? -46.410  20.777  -73.401  1.00 33.96  ? 39  TYR A CD1 1 
ATOM   301   C CD2 . TYR A  1 39  ? -46.720  19.392  -75.306  1.00 33.21  ? 39  TYR A CD2 1 
ATOM   302   C CE1 . TYR A  1 39  ? -47.776  21.022  -73.350  1.00 35.20  ? 39  TYR A CE1 1 
ATOM   303   C CE2 . TYR A  1 39  ? -48.092  19.611  -75.258  1.00 31.66  ? 39  TYR A CE2 1 
ATOM   304   C CZ  . TYR A  1 39  ? -48.626  20.417  -74.268  1.00 33.07  ? 39  TYR A CZ  1 
ATOM   305   O OH  . TYR A  1 39  ? -49.969  20.649  -74.201  1.00 29.73  ? 39  TYR A OH  1 
ATOM   306   N N   . GLU A  1 40  ? -41.359  21.261  -75.773  1.00 41.77  ? 40  GLU A N   1 
ATOM   307   C CA  . GLU A  1 40  ? -39.909  21.071  -75.687  1.00 45.55  ? 40  GLU A CA  1 
ATOM   308   C C   . GLU A  1 40  ? -39.154  22.354  -76.032  1.00 46.34  ? 40  GLU A C   1 
ATOM   309   O O   . GLU A  1 40  ? -38.042  22.567  -75.547  1.00 46.95  ? 40  GLU A O   1 
ATOM   310   C CB  . GLU A  1 40  ? -39.359  20.008  -76.634  1.00 45.59  ? 40  GLU A CB  1 
ATOM   311   C CG  . GLU A  1 40  ? -39.911  18.607  -76.410  1.00 51.76  ? 40  GLU A CG  1 
ATOM   312   C CD  . GLU A  1 40  ? -39.472  17.677  -77.541  1.00 60.96  ? 40  GLU A CD  1 
ATOM   313   O OE1 . GLU A  1 40  ? -38.731  18.125  -78.449  1.00 62.24  ? 40  GLU A OE1 1 
ATOM   314   O OE2 . GLU A  1 40  ? -39.879  16.501  -77.553  1.00 73.34  ? 40  GLU A OE2 1 
ATOM   315   N N   . ASP A  1 41  ? -39.738  23.165  -76.924  1.00 46.18  ? 41  ASP A N   1 
ATOM   316   C CA  . ASP A  1 41  ? -39.105  24.378  -77.413  1.00 48.58  ? 41  ASP A CA  1 
ATOM   317   C C   . ASP A  1 41  ? -39.086  25.432  -76.304  1.00 48.71  ? 41  ASP A C   1 
ATOM   318   O O   . ASP A  1 41  ? -39.995  25.460  -75.471  1.00 47.72  ? 41  ASP A O   1 
ATOM   319   C CB  . ASP A  1 41  ? -39.838  24.880  -78.650  1.00 47.94  ? 41  ASP A CB  1 
ATOM   320   C CG  . ASP A  1 41  ? -39.647  24.033  -79.906  1.00 50.40  ? 41  ASP A CG  1 
ATOM   321   O OD1 . ASP A  1 41  ? -38.715  23.153  -79.928  1.00 48.59  ? 41  ASP A OD1 1 
ATOM   322   O OD2 . ASP A  1 41  ? -40.429  24.256  -80.861  1.00 47.39  ? 41  ASP A OD2 1 
ATOM   323   N N   . GLU A  1 42  ? -38.063  26.298  -76.325  1.00 46.93  ? 42  GLU A N   1 
ATOM   324   C CA  . GLU A  1 42  ? -38.092  27.544  -75.571  1.00 49.77  ? 42  GLU A CA  1 
ATOM   325   C C   . GLU A  1 42  ? -39.433  28.234  -75.836  1.00 44.74  ? 42  GLU A C   1 
ATOM   326   O O   . GLU A  1 42  ? -39.866  28.324  -76.984  1.00 40.49  ? 42  GLU A O   1 
ATOM   327   C CB  . GLU A  1 42  ? -36.900  28.453  -75.887  1.00 54.19  ? 42  GLU A CB  1 
ATOM   328   C CG  . GLU A  1 42  ? -36.554  29.388  -74.727  1.00 64.70  ? 42  GLU A CG  1 
ATOM   329   C CD  . GLU A  1 42  ? -35.385  30.361  -74.919  1.00 76.37  ? 42  GLU A CD  1 
ATOM   330   O OE1 . GLU A  1 42  ? -35.540  31.442  -75.563  1.00 76.41  ? 42  GLU A OE1 1 
ATOM   331   O OE2 . GLU A  1 42  ? -34.293  30.020  -74.403  1.00 74.72  ? 42  GLU A OE2 1 
ATOM   332   N N   . ARG A  1 43  ? -40.104  28.664  -74.758  1.00 42.73  ? 43  ARG A N   1 
ATOM   333   C CA  . ARG A  1 43  ? -41.473  29.148  -74.847  1.00 41.63  ? 43  ARG A CA  1 
ATOM   334   C C   . ARG A  1 43  ? -41.475  30.569  -75.413  1.00 37.61  ? 43  ARG A C   1 
ATOM   335   O O   . ARG A  1 43  ? -40.744  31.408  -74.926  1.00 36.57  ? 43  ARG A O   1 
ATOM   336   C CB  . ARG A  1 43  ? -42.194  29.125  -73.496  1.00 43.68  ? 43  ARG A CB  1 
ATOM   337   C CG  . ARG A  1 43  ? -43.698  28.875  -73.640  1.00 48.33  ? 43  ARG A CG  1 
ATOM   338   C CD  . ARG A  1 43  ? -44.550  29.495  -72.517  1.00 49.92  ? 43  ARG A CD  1 
ATOM   339   N NE  . ARG A  1 43  ? -44.055  30.834  -72.146  1.00 53.08  ? 43  ARG A NE  1 
ATOM   340   C CZ  . ARG A  1 43  ? -44.489  32.035  -72.616  1.00 49.74  ? 43  ARG A CZ  1 
ATOM   341   N NH1 . ARG A  1 43  ? -45.542  32.113  -73.434  1.00 46.36  ? 43  ARG A NH1 1 
ATOM   342   N NH2 . ARG A  1 43  ? -43.876  33.138  -72.198  1.00 43.22  ? 43  ARG A NH2 1 
ATOM   343   N N   . LYS A  1 44  ? -42.252  30.773  -76.481  1.00 35.97  ? 44  LYS A N   1 
ATOM   344   C CA  . LYS A  1 44  ? -42.459  32.046  -77.149  1.00 38.61  ? 44  LYS A CA  1 
ATOM   345   C C   . LYS A  1 44  ? -43.951  32.357  -77.175  1.00 35.54  ? 44  LYS A C   1 
ATOM   346   O O   . LYS A  1 44  ? -44.744  31.435  -77.221  1.00 35.71  ? 44  LYS A O   1 
ATOM   347   C CB  . LYS A  1 44  ? -42.022  31.932  -78.613  1.00 40.15  ? 44  LYS A CB  1 
ATOM   348   C CG  . LYS A  1 44  ? -40.555  31.787  -78.804  1.00 42.60  ? 44  LYS A CG  1 
ATOM   349   C CD  . LYS A  1 44  ? -40.053  31.701  -80.234  1.00 45.79  ? 44  LYS A CD  1 
ATOM   350   C CE  . LYS A  1 44  ? -38.571  31.415  -80.132  1.00 51.65  ? 44  LYS A CE  1 
ATOM   351   N NZ  . LYS A  1 44  ? -37.826  31.339  -81.393  1.00 54.75  ? 44  LYS A NZ  1 
ATOM   352   N N   . ASP A  1 45  ? -44.311  33.645  -77.242  1.00 36.17  ? 45  ASP A N   1 
ATOM   353   C CA  . ASP A  1 45  ? -45.697  34.106  -77.182  1.00 35.81  ? 45  ASP A CA  1 
ATOM   354   C C   . ASP A  1 45  ? -46.365  33.936  -78.548  1.00 34.65  ? 45  ASP A C   1 
ATOM   355   O O   . ASP A  1 45  ? -47.558  33.648  -78.606  1.00 34.52  ? 45  ASP A O   1 
ATOM   356   C CB  . ASP A  1 45  ? -45.796  35.524  -76.614  1.00 37.65  ? 45  ASP A CB  1 
ATOM   357   C CG  . ASP A  1 45  ? -45.731  35.644  -75.092  1.00 38.16  ? 45  ASP A CG  1 
ATOM   358   O OD1 . ASP A  1 45  ? -45.964  34.621  -74.408  1.00 39.52  ? 45  ASP A OD1 1 
ATOM   359   O OD2 . ASP A  1 45  ? -45.447  36.749  -74.585  1.00 38.01  ? 45  ASP A OD2 1 
ATOM   360   N N   . GLU A  1 46  ? -45.593  34.131  -79.630  1.00 33.70  ? 46  GLU A N   1 
ATOM   361   C CA  . GLU A  1 46  ? -46.032  33.880  -80.992  1.00 33.59  ? 46  GLU A CA  1 
ATOM   362   C C   . GLU A  1 46  ? -47.258  34.731  -81.349  1.00 33.14  ? 46  GLU A C   1 
ATOM   363   O O   . GLU A  1 46  ? -48.189  34.246  -82.012  1.00 32.11  ? 46  GLU A O   1 
ATOM   364   C CB  . GLU A  1 46  ? -46.407  32.405  -81.115  1.00 35.63  ? 46  GLU A CB  1 
ATOM   365   C CG  . GLU A  1 46  ? -45.285  31.432  -80.771  1.00 38.80  ? 46  GLU A CG  1 
ATOM   366   C CD  . GLU A  1 46  ? -44.439  30.989  -81.940  1.00 41.55  ? 46  GLU A CD  1 
ATOM   367   O OE1 . GLU A  1 46  ? -43.518  31.607  -82.486  1.00 47.80  ? 46  GLU A OE1 1 
ATOM   368   O OE2 . GLU A  1 46  ? -44.772  29.885  -82.317  1.00 52.15  ? 46  GLU A OE2 1 
ATOM   369   N N   . LEU A  1 47  ? -47.256  35.994  -80.919  1.00 31.15  ? 47  LEU A N   1 
ATOM   370   C CA  . LEU A  1 47  ? -48.443  36.838  -80.968  1.00 31.58  ? 47  LEU A CA  1 
ATOM   371   C C   . LEU A  1 47  ? -48.932  37.083  -82.395  1.00 32.88  ? 47  LEU A C   1 
ATOM   372   O O   . LEU A  1 47  ? -50.140  37.187  -82.626  1.00 31.56  ? 47  LEU A O   1 
ATOM   373   C CB  . LEU A  1 47  ? -48.149  38.163  -80.258  1.00 31.52  ? 47  LEU A CB  1 
ATOM   374   C CG  . LEU A  1 47  ? -47.862  38.085  -78.756  1.00 32.40  ? 47  LEU A CG  1 
ATOM   375   C CD1 . LEU A  1 47  ? -47.535  39.463  -78.166  1.00 34.83  ? 47  LEU A CD1 1 
ATOM   376   C CD2 . LEU A  1 47  ? -49.012  37.487  -77.988  1.00 31.00  ? 47  LEU A CD2 1 
ATOM   377   N N   . GLU A  1 48  ? -48.002  37.248  -83.343  1.00 36.74  ? 48  GLU A N   1 
ATOM   378   C CA  . GLU A  1 48  ? -48.363  37.536  -84.724  1.00 39.54  ? 48  GLU A CA  1 
ATOM   379   C C   . GLU A  1 48  ? -49.153  36.340  -85.260  1.00 38.40  ? 48  GLU A C   1 
ATOM   380   O O   . GLU A  1 48  ? -50.224  36.516  -85.841  1.00 40.39  ? 48  GLU A O   1 
ATOM   381   C CB  . GLU A  1 48  ? -47.183  37.922  -85.623  1.00 43.28  ? 48  GLU A CB  1 
ATOM   382   C CG  . GLU A  1 48  ? -46.496  39.244  -85.256  1.00 52.21  ? 48  GLU A CG  1 
ATOM   383   C CD  . GLU A  1 48  ? -47.406  40.477  -85.056  1.00 60.61  ? 48  GLU A CD  1 
ATOM   384   O OE1 . GLU A  1 48  ? -48.313  40.750  -85.892  1.00 56.76  ? 48  GLU A OE1 1 
ATOM   385   O OE2 . GLU A  1 48  ? -47.218  41.192  -84.030  1.00 66.18  ? 48  GLU A OE2 1 
ATOM   386   N N   . LEU A  1 49  ? -48.661  35.126  -85.019  1.00 34.39  ? 49  LEU A N   1 
ATOM   387   C CA  . LEU A  1 49  ? -49.362  33.965  -85.536  1.00 35.38  ? 49  LEU A CA  1 
ATOM   388   C C   . LEU A  1 49  ? -50.698  33.761  -84.819  1.00 31.28  ? 49  LEU A C   1 
ATOM   389   O O   . LEU A  1 49  ? -51.647  33.318  -85.447  1.00 30.12  ? 49  LEU A O   1 
ATOM   390   C CB  . LEU A  1 49  ? -48.474  32.719  -85.506  1.00 35.11  ? 49  LEU A CB  1 
ATOM   391   C CG  . LEU A  1 49  ? -47.263  32.791  -86.446  1.00 35.51  ? 49  LEU A CG  1 
ATOM   392   C CD1 . LEU A  1 49  ? -46.328  31.593  -86.287  1.00 34.72  ? 49  LEU A CD1 1 
ATOM   393   C CD2 . LEU A  1 49  ? -47.752  32.881  -87.885  1.00 35.54  ? 49  LEU A CD2 1 
ATOM   394   N N   . MET A  1 50  ? -50.783  34.099  -83.531  1.00 30.72  ? 50  MET A N   1 
ATOM   395   C CA  . MET A  1 50  ? -52.057  34.057  -82.827  1.00 32.99  ? 50  MET A CA  1 
ATOM   396   C C   . MET A  1 50  ? -53.083  35.025  -83.419  1.00 32.25  ? 50  MET A C   1 
ATOM   397   O O   . MET A  1 50  ? -54.239  34.679  -83.513  1.00 34.86  ? 50  MET A O   1 
ATOM   398   C CB  . MET A  1 50  ? -51.910  34.375  -81.337  1.00 33.64  ? 50  MET A CB  1 
ATOM   399   C CG  . MET A  1 50  ? -51.186  33.294  -80.558  1.00 33.42  ? 50  MET A CG  1 
ATOM   400   S SD  . MET A  1 50  ? -51.334  33.434  -78.764  1.00 33.22  ? 50  MET A SD  1 
ATOM   401   C CE  . MET A  1 50  ? -53.116  33.314  -78.542  1.00 30.76  ? 50  MET A CE  1 
ATOM   402   N N   . LYS A  1 51  ? -52.677  36.240  -83.786  1.00 35.16  ? 51  LYS A N   1 
ATOM   403   C CA  . LYS A  1 51  ? -53.611  37.200  -84.350  1.00 36.06  ? 51  LYS A CA  1 
ATOM   404   C C   . LYS A  1 51  ? -54.234  36.573  -85.582  1.00 35.02  ? 51  LYS A C   1 
ATOM   405   O O   . LYS A  1 51  ? -55.437  36.669  -85.757  1.00 35.73  ? 51  LYS A O   1 
ATOM   406   C CB  . LYS A  1 51  ? -53.043  38.552  -84.804  1.00 37.12  ? 51  LYS A CB  1 
ATOM   407   C CG  . LYS A  1 51  ? -52.910  39.567  -83.696  1.00 41.63  ? 51  LYS A CG  1 
ATOM   408   C CD  . LYS A  1 51  ? -51.856  40.656  -83.883  1.00 46.28  ? 51  LYS A CD  1 
ATOM   409   C CE  . LYS A  1 51  ? -51.192  41.079  -82.589  1.00 48.32  ? 51  LYS A CE  1 
ATOM   410   N NZ  . LYS A  1 51  ? -50.036  41.950  -82.854  1.00 50.41  ? 51  LYS A NZ  1 
ATOM   411   N N   . PHE A  1 52  ? -53.382  36.007  -86.447  1.00 33.34  ? 52  PHE A N   1 
ATOM   412   C CA  . PHE A  1 52  ? -53.815  35.388  -87.688  1.00 31.53  ? 52  PHE A CA  1 
ATOM   413   C C   . PHE A  1 52  ? -54.813  34.280  -87.358  1.00 32.48  ? 52  PHE A C   1 
ATOM   414   O O   . PHE A  1 52  ? -55.903  34.265  -87.922  1.00 33.24  ? 52  PHE A O   1 
ATOM   415   C CB  . PHE A  1 52  ? -52.573  34.917  -88.449  1.00 30.75  ? 52  PHE A CB  1 
ATOM   416   C CG  . PHE A  1 52  ? -52.823  33.928  -89.578  1.00 30.24  ? 52  PHE A CG  1 
ATOM   417   C CD1 . PHE A  1 52  ? -53.217  34.370  -90.837  1.00 30.46  ? 52  PHE A CD1 1 
ATOM   418   C CD2 . PHE A  1 52  ? -52.643  32.568  -89.374  1.00 28.87  ? 52  PHE A CD2 1 
ATOM   419   C CE1 . PHE A  1 52  ? -53.464  33.476  -91.859  1.00 31.31  ? 52  PHE A CE1 1 
ATOM   420   C CE2 . PHE A  1 52  ? -52.870  31.674  -90.399  1.00 29.60  ? 52  PHE A CE2 1 
ATOM   421   C CZ  . PHE A  1 52  ? -53.289  32.122  -91.639  1.00 31.10  ? 52  PHE A CZ  1 
ATOM   422   N N   . ASP A  1 53  ? -54.444  33.423  -86.392  1.00 30.97  ? 53  ASP A N   1 
ATOM   423   C CA  . ASP A  1 53  ? -55.243  32.276  -86.009  1.00 31.06  ? 53  ASP A CA  1 
ATOM   424   C C   . ASP A  1 53  ? -56.565  32.742  -85.386  1.00 30.18  ? 53  ASP A C   1 
ATOM   425   O O   . ASP A  1 53  ? -57.611  32.281  -85.798  1.00 29.66  ? 53  ASP A O   1 
ATOM   426   C CB  . ASP A  1 53  ? -54.457  31.342  -85.088  1.00 30.29  ? 53  ASP A CB  1 
ATOM   427   C CG  . ASP A  1 53  ? -53.220  30.665  -85.664  1.00 29.50  ? 53  ASP A CG  1 
ATOM   428   O OD1 . ASP A  1 53  ? -53.168  30.435  -86.895  1.00 26.80  ? 53  ASP A OD1 1 
ATOM   429   O OD2 . ASP A  1 53  ? -52.305  30.380  -84.849  1.00 29.82  ? 53  ASP A OD2 1 
ATOM   430   N N   . LEU A  1 54  ? -56.535  33.648  -84.397  1.00 29.41  ? 54  LEU A N   1 
ATOM   431   C CA  . LEU A  1 54  ? -57.757  34.064  -83.726  1.00 30.27  ? 54  LEU A CA  1 
ATOM   432   C C   . LEU A  1 54  ? -58.764  34.680  -84.709  1.00 30.48  ? 54  LEU A C   1 
ATOM   433   O O   . LEU A  1 54  ? -59.963  34.392  -84.621  1.00 29.83  ? 54  LEU A O   1 
ATOM   434   C CB  . LEU A  1 54  ? -57.438  35.002  -82.569  1.00 30.71  ? 54  LEU A CB  1 
ATOM   435   C CG  . LEU A  1 54  ? -56.719  34.369  -81.377  1.00 31.25  ? 54  LEU A CG  1 
ATOM   436   C CD1 . LEU A  1 54  ? -56.598  35.379  -80.263  1.00 31.77  ? 54  LEU A CD1 1 
ATOM   437   C CD2 . LEU A  1 54  ? -57.381  33.075  -80.845  1.00 31.17  ? 54  LEU A CD2 1 
ATOM   438   N N   . GLU A  1 55  ? -58.260  35.435  -85.689  1.00 28.86  ? 55  GLU A N   1 
ATOM   439   C CA  . GLU A  1 55  ? -59.069  35.988  -86.760  1.00 29.82  ? 55  GLU A CA  1 
ATOM   440   C C   . GLU A  1 55  ? -59.692  34.873  -87.600  1.00 31.06  ? 55  GLU A C   1 
ATOM   441   O O   . GLU A  1 55  ? -60.894  34.893  -87.896  1.00 30.52  ? 55  GLU A O   1 
ATOM   442   C CB  . GLU A  1 55  ? -58.218  36.918  -87.629  1.00 30.61  ? 55  GLU A CB  1 
ATOM   443   C CG  . GLU A  1 55  ? -59.054  37.734  -88.610  1.00 34.32  ? 55  GLU A CG  1 
ATOM   444   C CD  . GLU A  1 55  ? -60.252  38.478  -87.972  1.00 35.98  ? 55  GLU A CD  1 
ATOM   445   O OE1 . GLU A  1 55  ? -60.170  39.038  -86.813  1.00 35.31  ? 55  GLU A OE1 1 
ATOM   446   O OE2 . GLU A  1 55  ? -61.281  38.461  -88.678  1.00 33.22  ? 55  GLU A OE2 1 
ATOM   447   N N   . ASN A  1 56  ? -58.872  33.877  -87.977  1.00 31.76  ? 56  ASN A N   1 
ATOM   448   C CA  . ASN A  1 56  ? -59.362  32.763  -88.773  1.00 31.52  ? 56  ASN A CA  1 
ATOM   449   C C   . ASN A  1 56  ? -60.522  32.079  -88.048  1.00 31.69  ? 56  ASN A C   1 
ATOM   450   O O   . ASN A  1 56  ? -61.566  31.808  -88.645  1.00 34.53  ? 56  ASN A O   1 
ATOM   451   C CB  . ASN A  1 56  ? -58.281  31.738  -89.085  1.00 31.89  ? 56  ASN A CB  1 
ATOM   452   C CG  . ASN A  1 56  ? -57.244  32.239  -90.067  1.00 33.37  ? 56  ASN A CG  1 
ATOM   453   O OD1 . ASN A  1 56  ? -57.528  33.025  -90.965  1.00 33.92  ? 56  ASN A OD1 1 
ATOM   454   N ND2 . ASN A  1 56  ? -56.034  31.725  -89.975  1.00 35.45  ? 56  ASN A ND2 1 
ATOM   455   N N   . ILE A  1 57  ? -60.325  31.802  -86.759  1.00 30.75  ? 57  ILE A N   1 
ATOM   456   C CA  . ILE A  1 57  ? -61.269  31.038  -85.943  1.00 30.47  ? 57  ILE A CA  1 
ATOM   457   C C   . ILE A  1 57  ? -62.583  31.819  -85.760  1.00 34.68  ? 57  ILE A C   1 
ATOM   458   O O   . ILE A  1 57  ? -63.648  31.212  -85.698  1.00 35.74  ? 57  ILE A O   1 
ATOM   459   C CB  . ILE A  1 57  ? -60.604  30.695  -84.603  1.00 26.99  ? 57  ILE A CB  1 
ATOM   460   C CG1 . ILE A  1 57  ? -59.493  29.689  -84.832  1.00 26.57  ? 57  ILE A CG1 1 
ATOM   461   C CG2 . ILE A  1 57  ? -61.639  30.207  -83.596  1.00 27.49  ? 57  ILE A CG2 1 
ATOM   462   C CD1 . ILE A  1 57  ? -58.610  29.396  -83.632  1.00 27.45  ? 57  ILE A CD1 1 
ATOM   463   N N   . LYS A  1 58  ? -62.512  33.168  -85.713  1.00 32.61  ? 58  LYS A N   1 
ATOM   464   C CA  . LYS A  1 58  ? -63.709  33.981  -85.632  1.00 31.73  ? 58  LYS A CA  1 
ATOM   465   C C   . LYS A  1 58  ? -64.484  33.896  -86.948  1.00 31.13  ? 58  LYS A C   1 
ATOM   466   O O   . LYS A  1 58  ? -65.705  33.720  -86.916  1.00 29.33  ? 58  LYS A O   1 
ATOM   467   C CB  . LYS A  1 58  ? -63.364  35.421  -85.250  1.00 32.06  ? 58  LYS A CB  1 
ATOM   468   C CG  . LYS A  1 58  ? -63.004  35.629  -83.793  1.00 32.08  ? 58  LYS A CG  1 
ATOM   469   C CD  . LYS A  1 58  ? -62.257  36.935  -83.567  1.00 33.44  ? 58  LYS A CD  1 
ATOM   470   C CE  . LYS A  1 58  ? -63.078  38.134  -83.825  1.00 35.40  ? 58  LYS A CE  1 
ATOM   471   N NZ  . LYS A  1 58  ? -62.251  39.273  -83.443  1.00 37.22  ? 58  LYS A NZ  1 
ATOM   472   N N   . GLU A  1 59  ? -63.769  34.007  -88.083  1.00 30.26  ? 59  GLU A N   1 
ATOM   473   C CA  . GLU A  1 59  ? -64.336  33.811  -89.416  1.00 29.65  ? 59  GLU A CA  1 
ATOM   474   C C   . GLU A  1 59  ? -64.815  32.374  -89.672  1.00 29.76  ? 59  GLU A C   1 
ATOM   475   O O   . GLU A  1 59  ? -65.603  32.147  -90.575  1.00 30.76  ? 59  GLU A O   1 
ATOM   476   C CB  . GLU A  1 59  ? -63.330  34.274  -90.470  1.00 31.51  ? 59  GLU A CB  1 
ATOM   477   C CG  . GLU A  1 59  ? -63.168  35.802  -90.511  1.00 35.04  ? 59  GLU A CG  1 
ATOM   478   C CD  . GLU A  1 59  ? -62.031  36.266  -91.401  1.00 37.86  ? 59  GLU A CD  1 
ATOM   479   O OE1 . GLU A  1 59  ? -61.953  35.677  -92.499  1.00 39.82  ? 59  GLU A OE1 1 
ATOM   480   O OE2 . GLU A  1 59  ? -61.224  37.153  -91.026  1.00 37.99  ? 59  GLU A OE2 1 
ATOM   481   N N   . GLY A  1 60  ? -64.362  31.386  -88.893  1.00 28.77  ? 60  GLY A N   1 
ATOM   482   C CA  . GLY A  1 60  ? -64.840  30.023  -89.042  1.00 27.66  ? 60  GLY A CA  1 
ATOM   483   C C   . GLY A  1 60  ? -66.137  29.760  -88.268  1.00 28.33  ? 60  GLY A C   1 
ATOM   484   O O   . GLY A  1 60  ? -66.711  28.678  -88.407  1.00 30.14  ? 60  GLY A O   1 
ATOM   485   N N   . GLY A  1 61  ? -66.518  30.686  -87.369  1.00 25.68  ? 61  GLY A N   1 
ATOM   486   C CA  . GLY A  1 61  ? -67.836  30.712  -86.764  1.00 24.05  ? 61  GLY A CA  1 
ATOM   487   C C   . GLY A  1 61  ? -67.812  30.405  -85.276  1.00 23.87  ? 61  GLY A C   1 
ATOM   488   O O   . GLY A  1 61  ? -68.882  30.334  -84.664  1.00 23.75  ? 61  GLY A O   1 
ATOM   489   N N   . TYR A  1 62  ? -66.611  30.174  -84.721  1.00 24.18  ? 62  TYR A N   1 
ATOM   490   C CA  . TYR A  1 62  ? -66.463  29.749  -83.323  1.00 24.35  ? 62  TYR A CA  1 
ATOM   491   C C   . TYR A  1 62  ? -66.663  30.957  -82.403  1.00 24.32  ? 62  TYR A C   1 
ATOM   492   O O   . TYR A  1 62  ? -66.451  32.096  -82.810  1.00 26.00  ? 62  TYR A O   1 
ATOM   493   C CB  . TYR A  1 62  ? -65.092  29.051  -83.170  1.00 24.71  ? 62  TYR A CB  1 
ATOM   494   C CG  . TYR A  1 62  ? -64.883  27.891  -84.147  1.00 25.87  ? 62  TYR A CG  1 
ATOM   495   C CD1 . TYR A  1 62  ? -65.454  26.646  -83.906  1.00 25.19  ? 62  TYR A CD1 1 
ATOM   496   C CD2 . TYR A  1 62  ? -64.222  28.065  -85.355  1.00 27.73  ? 62  TYR A CD2 1 
ATOM   497   C CE1 . TYR A  1 62  ? -65.354  25.601  -84.807  1.00 25.24  ? 62  TYR A CE1 1 
ATOM   498   C CE2 . TYR A  1 62  ? -64.120  27.029  -86.271  1.00 29.82  ? 62  TYR A CE2 1 
ATOM   499   C CZ  . TYR A  1 62  ? -64.682  25.789  -85.987  1.00 27.42  ? 62  TYR A CZ  1 
ATOM   500   O OH  . TYR A  1 62  ? -64.611  24.764  -86.867  1.00 26.94  ? 62  TYR A OH  1 
ATOM   501   N N   . ASN A  1 63  ? -67.050  30.719  -81.150  1.00 24.13  ? 63  ASN A N   1 
ATOM   502   C CA  . ASN A  1 63  ? -67.158  31.783  -80.163  1.00 24.96  ? 63  ASN A CA  1 
ATOM   503   C C   . ASN A  1 63  ? -66.142  31.558  -79.043  1.00 25.28  ? 63  ASN A C   1 
ATOM   504   O O   . ASN A  1 63  ? -66.065  32.381  -78.143  1.00 25.81  ? 63  ASN A O   1 
ATOM   505   C CB  . ASN A  1 63  ? -68.592  31.983  -79.665  1.00 24.96  ? 63  ASN A CB  1 
ATOM   506   C CG  . ASN A  1 63  ? -69.157  30.762  -78.966  1.00 25.92  ? 63  ASN A CG  1 
ATOM   507   O OD1 . ASN A  1 63  ? -68.406  29.904  -78.515  1.00 26.23  ? 63  ASN A OD1 1 
ATOM   508   N ND2 . ASN A  1 63  ? -70.473  30.672  -78.788  1.00 26.80  ? 63  ASN A ND2 1 
ATOM   509   N N   . THR A  1 64  ? -65.376  30.452  -79.098  1.00 26.39  ? 64  THR A N   1 
ATOM   510   C CA  . THR A  1 64  ? -64.499  30.023  -78.008  1.00 25.66  ? 64  THR A CA  1 
ATOM   511   C C   . THR A  1 64  ? -63.319  29.249  -78.576  1.00 25.89  ? 64  THR A C   1 
ATOM   512   O O   . THR A  1 64  ? -63.507  28.512  -79.538  1.00 27.43  ? 64  THR A O   1 
ATOM   513   C CB  . THR A  1 64  ? -65.272  29.114  -77.054  1.00 24.57  ? 64  THR A CB  1 
ATOM   514   O OG1 . THR A  1 64  ? -66.408  29.831  -76.576  1.00 23.19  ? 64  THR A OG1 1 
ATOM   515   C CG2 . THR A  1 64  ? -64.435  28.634  -75.880  1.00 24.14  ? 64  THR A CG2 1 
ATOM   516   N N   . ILE A  1 65  ? -62.152  29.323  -77.910  1.00 26.23  ? 65  ILE A N   1 
ATOM   517   C CA  . ILE A  1 65  ? -61.054  28.382  -78.136  1.00 25.95  ? 65  ILE A CA  1 
ATOM   518   C C   . ILE A  1 65  ? -60.836  27.512  -76.889  1.00 24.91  ? 65  ILE A C   1 
ATOM   519   O O   . ILE A  1 65  ? -61.159  27.914  -75.772  1.00 24.52  ? 65  ILE A O   1 
ATOM   520   C CB  . ILE A  1 65  ? -59.757  29.109  -78.552  1.00 27.80  ? 65  ILE A CB  1 
ATOM   521   C CG1 . ILE A  1 65  ? -59.372  30.239  -77.564  1.00 29.06  ? 65  ILE A CG1 1 
ATOM   522   C CG2 . ILE A  1 65  ? -59.875  29.623  -79.994  1.00 27.82  ? 65  ILE A CG2 1 
ATOM   523   C CD1 . ILE A  1 65  ? -57.973  30.810  -77.756  1.00 29.82  ? 65  ILE A CD1 1 
ATOM   524   N N   . ARG A  1 66  ? -60.228  26.337  -77.094  1.00 24.47  ? 66  ARG A N   1 
ATOM   525   C CA  . ARG A  1 66  ? -59.926  25.373  -76.040  1.00 24.47  ? 66  ARG A CA  1 
ATOM   526   C C   . ARG A  1 66  ? -58.470  24.958  -76.172  1.00 23.83  ? 66  ARG A C   1 
ATOM   527   O O   . ARG A  1 66  ? -58.036  24.626  -77.261  1.00 22.58  ? 66  ARG A O   1 
ATOM   528   C CB  . ARG A  1 66  ? -60.872  24.167  -76.176  1.00 25.27  ? 66  ARG A CB  1 
ATOM   529   C CG  . ARG A  1 66  ? -60.591  22.918  -75.349  1.00 26.11  ? 66  ARG A CG  1 
ATOM   530   C CD  . ARG A  1 66  ? -59.457  22.005  -75.820  1.00 27.18  ? 66  ARG A CD  1 
ATOM   531   N NE  . ARG A  1 66  ? -59.600  20.648  -75.283  1.00 29.38  ? 66  ARG A NE  1 
ATOM   532   C CZ  . ARG A  1 66  ? -58.828  20.026  -74.385  1.00 31.74  ? 66  ARG A CZ  1 
ATOM   533   N NH1 . ARG A  1 66  ? -57.817  20.658  -73.779  1.00 30.86  ? 66  ARG A NH1 1 
ATOM   534   N NH2 . ARG A  1 66  ? -59.092  18.760  -74.100  1.00 31.10  ? 66  ARG A NH2 1 
ATOM   535   N N   . THR A  1 67  ? -57.726  24.975  -75.058  1.00 25.03  ? 67  THR A N   1 
ATOM   536   C CA  . THR A  1 67  ? -56.274  24.828  -75.077  1.00 25.46  ? 67  THR A CA  1 
ATOM   537   C C   . THR A  1 67  ? -55.875  23.742  -74.089  1.00 24.98  ? 67  THR A C   1 
ATOM   538   O O   . THR A  1 67  ? -56.681  23.308  -73.276  1.00 25.43  ? 67  THR A O   1 
ATOM   539   C CB  . THR A  1 67  ? -55.580  26.142  -74.694  1.00 25.91  ? 67  THR A CB  1 
ATOM   540   O OG1 . THR A  1 67  ? -55.895  26.339  -73.326  1.00 23.34  ? 67  THR A OG1 1 
ATOM   541   C CG2 . THR A  1 67  ? -56.039  27.321  -75.536  1.00 26.85  ? 67  THR A CG2 1 
ATOM   542   N N   . TRP A  1 68  ? -54.607  23.355  -74.145  1.00 24.83  ? 68  TRP A N   1 
ATOM   543   C CA  . TRP A  1 68  ? -54.096  22.259  -73.338  1.00 26.24  ? 68  TRP A CA  1 
ATOM   544   C C   . TRP A  1 68  ? -53.093  22.769  -72.314  1.00 27.32  ? 68  TRP A C   1 
ATOM   545   O O   . TRP A  1 68  ? -52.940  22.177  -71.264  1.00 31.35  ? 68  TRP A O   1 
ATOM   546   C CB  . TRP A  1 68  ? -53.470  21.173  -74.222  1.00 25.51  ? 68  TRP A CB  1 
ATOM   547   C CG  . TRP A  1 68  ? -54.505  20.348  -74.904  1.00 25.13  ? 68  TRP A CG  1 
ATOM   548   C CD1 . TRP A  1 68  ? -55.011  19.162  -74.472  1.00 27.45  ? 68  TRP A CD1 1 
ATOM   549   C CD2 . TRP A  1 68  ? -55.199  20.681  -76.120  1.00 26.13  ? 68  TRP A CD2 1 
ATOM   550   N NE1 . TRP A  1 68  ? -55.983  18.722  -75.340  1.00 29.33  ? 68  TRP A NE1 1 
ATOM   551   C CE2 . TRP A  1 68  ? -56.126  19.646  -76.356  1.00 26.74  ? 68  TRP A CE2 1 
ATOM   552   C CE3 . TRP A  1 68  ? -55.123  21.747  -77.015  1.00 27.52  ? 68  TRP A CE3 1 
ATOM   553   C CZ2 . TRP A  1 68  ? -56.965  19.640  -77.458  1.00 26.18  ? 68  TRP A CZ2 1 
ATOM   554   C CZ3 . TRP A  1 68  ? -55.899  21.718  -78.143  1.00 28.88  ? 68  TRP A CZ3 1 
ATOM   555   C CH2 . TRP A  1 68  ? -56.832  20.683  -78.342  1.00 29.98  ? 68  TRP A CH2 1 
ATOM   556   N N   . SER A  1 69  ? -52.535  23.934  -72.595  1.00 28.98  ? 69  SER A N   1 
ATOM   557   C CA  . SER A  1 69  ? -51.415  24.493  -71.878  1.00 29.23  ? 69  SER A CA  1 
ATOM   558   C C   . SER A  1 69  ? -51.706  25.965  -71.590  1.00 29.12  ? 69  SER A C   1 
ATOM   559   O O   . SER A  1 69  ? -52.150  26.673  -72.484  1.00 29.31  ? 69  SER A O   1 
ATOM   560   C CB  . SER A  1 69  ? -50.210  24.354  -72.760  1.00 30.60  ? 69  SER A CB  1 
ATOM   561   O OG  . SER A  1 69  ? -49.040  24.368  -71.989  1.00 33.56  ? 69  SER A OG  1 
ATOM   562   N N   . GLN A  1 70  ? -51.380  26.424  -70.377  1.00 29.26  ? 70  GLN A N   1 
ATOM   563   C CA  . GLN A  1 70  ? -51.674  27.781  -69.931  1.00 30.69  ? 70  GLN A CA  1 
ATOM   564   C C   . GLN A  1 70  ? -51.033  28.861  -70.809  1.00 30.35  ? 70  GLN A C   1 
ATOM   565   O O   . GLN A  1 70  ? -49.847  28.843  -71.122  1.00 29.17  ? 70  GLN A O   1 
ATOM   566   C CB  . GLN A  1 70  ? -51.166  28.030  -68.504  1.00 30.95  ? 70  GLN A CB  1 
ATOM   567   C CG  . GLN A  1 70  ? -49.700  27.669  -68.250  1.00 30.13  ? 70  GLN A CG  1 
ATOM   568   C CD  . GLN A  1 70  ? -49.566  26.277  -67.666  1.00 29.11  ? 70  GLN A CD  1 
ATOM   569   O OE1 . GLN A  1 70  ? -50.243  25.351  -68.103  1.00 27.09  ? 70  GLN A OE1 1 
ATOM   570   N NE2 . GLN A  1 70  ? -48.791  26.143  -66.601  1.00 29.66  ? 70  GLN A NE2 1 
ATOM   571   N N   . TYR A  1 71  ? -51.811  29.896  -71.106  1.00 29.80  ? 71  TYR A N   1 
ATOM   572   C CA  . TYR A  1 71  ? -51.275  31.048  -71.822  1.00 29.06  ? 71  TYR A CA  1 
ATOM   573   C C   . TYR A  1 71  ? -50.526  31.986  -70.876  1.00 27.60  ? 71  TYR A C   1 
ATOM   574   O O   . TYR A  1 71  ? -50.841  32.001  -69.694  1.00 29.41  ? 71  TYR A O   1 
ATOM   575   C CB  . TYR A  1 71  ? -52.408  31.851  -72.458  1.00 28.45  ? 71  TYR A CB  1 
ATOM   576   C CG  . TYR A  1 71  ? -52.932  31.317  -73.774  1.00 27.94  ? 71  TYR A CG  1 
ATOM   577   C CD1 . TYR A  1 71  ? -52.121  30.584  -74.649  1.00 27.22  ? 71  TYR A CD1 1 
ATOM   578   C CD2 . TYR A  1 71  ? -54.252  31.567  -74.144  1.00 27.13  ? 71  TYR A CD2 1 
ATOM   579   C CE1 . TYR A  1 71  ? -52.621  30.096  -75.844  1.00 26.43  ? 71  TYR A CE1 1 
ATOM   580   C CE2 . TYR A  1 71  ? -54.763  31.055  -75.326  1.00 27.34  ? 71  TYR A CE2 1 
ATOM   581   C CZ  . TYR A  1 71  ? -53.940  30.337  -76.174  1.00 27.02  ? 71  TYR A CZ  1 
ATOM   582   O OH  . TYR A  1 71  ? -54.483  29.884  -77.327  1.00 29.95  ? 71  TYR A OH  1 
ATOM   583   N N   . SER A  1 72  ? -49.550  32.737  -71.400  1.00 25.32  ? 72  SER A N   1 
ATOM   584   C CA  . SER A  1 72  ? -48.945  33.847  -70.675  1.00 26.85  ? 72  SER A CA  1 
ATOM   585   C C   . SER A  1 72  ? -49.947  34.999  -70.606  1.00 27.55  ? 72  SER A C   1 
ATOM   586   O O   . SER A  1 72  ? -50.961  34.968  -71.291  1.00 27.81  ? 72  SER A O   1 
ATOM   587   C CB  . SER A  1 72  ? -47.677  34.341  -71.354  1.00 27.20  ? 72  SER A CB  1 
ATOM   588   O OG  . SER A  1 72  ? -47.981  35.009  -72.583  1.00 26.07  ? 72  SER A OG  1 
ATOM   589   N N   . GLU A  1 73  ? -49.658  36.032  -69.814  1.00 29.31  ? 73  GLU A N   1 
ATOM   590   C CA  . GLU A  1 73  ? -50.554  37.171  -69.729  1.00 30.46  ? 73  GLU A CA  1 
ATOM   591   C C   . GLU A  1 73  ? -50.683  37.836  -71.104  1.00 31.48  ? 73  GLU A C   1 
ATOM   592   O O   . GLU A  1 73  ? -51.778  38.138  -71.560  1.00 32.37  ? 73  GLU A O   1 
ATOM   593   C CB  . GLU A  1 73  ? -50.115  38.160  -68.651  1.00 31.21  ? 73  GLU A CB  1 
ATOM   594   C CG  . GLU A  1 73  ? -51.176  39.243  -68.464  1.00 30.93  ? 73  GLU A CG  1 
ATOM   595   C CD  . GLU A  1 73  ? -51.075  40.040  -67.205  1.00 31.94  ? 73  GLU A CD  1 
ATOM   596   O OE1 . GLU A  1 73  ? -50.149  39.869  -66.386  1.00 31.52  ? 73  GLU A OE1 1 
ATOM   597   O OE2 . GLU A  1 73  ? -52.003  40.860  -67.063  1.00 34.84  ? 73  GLU A OE2 1 
ATOM   598   N N   . ASN A  1 74  ? -49.549  38.054  -71.771  1.00 33.16  ? 74  ASN A N   1 
ATOM   599   C CA  . ASN A  1 74  ? -49.526  38.585  -73.124  1.00 34.20  ? 74  ASN A CA  1 
ATOM   600   C C   . ASN A  1 74  ? -50.464  37.791  -74.039  1.00 30.96  ? 74  ASN A C   1 
ATOM   601   O O   . ASN A  1 74  ? -51.234  38.344  -74.791  1.00 30.21  ? 74  ASN A O   1 
ATOM   602   C CB  . ASN A  1 74  ? -48.110  38.592  -73.700  1.00 35.57  ? 74  ASN A CB  1 
ATOM   603   C CG  . ASN A  1 74  ? -47.269  39.776  -73.298  1.00 38.38  ? 74  ASN A CG  1 
ATOM   604   O OD1 . ASN A  1 74  ? -47.788  40.815  -72.848  1.00 38.26  ? 74  ASN A OD1 1 
ATOM   605   N ND2 . ASN A  1 74  ? -45.954  39.628  -73.477  1.00 37.44  ? 74  ASN A ND2 1 
ATOM   606   N N   . GLN A  1 75  ? -50.385  36.470  -74.022  1.00 31.74  ? 75  GLN A N   1 
ATOM   607   C CA  . GLN A  1 75  ? -51.225  35.655  -74.937  1.00 32.74  ? 75  GLN A CA  1 
ATOM   608   C C   . GLN A  1 75  ? -52.705  35.758  -74.523  1.00 33.35  ? 75  GLN A C   1 
ATOM   609   O O   . GLN A  1 75  ? -53.558  35.799  -75.412  1.00 34.60  ? 75  GLN A O   1 
ATOM   610   C CB  . GLN A  1 75  ? -50.767  34.199  -74.947  1.00 31.95  ? 75  GLN A CB  1 
ATOM   611   C CG  . GLN A  1 75  ? -49.404  33.948  -75.574  1.00 32.88  ? 75  GLN A CG  1 
ATOM   612   C CD  . GLN A  1 75  ? -48.928  32.530  -75.354  1.00 33.81  ? 75  GLN A CD  1 
ATOM   613   O OE1 . GLN A  1 75  ? -48.934  32.016  -74.232  1.00 32.71  ? 75  GLN A OE1 1 
ATOM   614   N NE2 . GLN A  1 75  ? -48.522  31.878  -76.430  1.00 34.39  ? 75  GLN A NE2 1 
ATOM   615   N N   . LEU A  1 76  ? -52.974  35.803  -73.223  1.00 34.78  ? 76  LEU A N   1 
ATOM   616   C CA  . LEU A  1 76  ? -54.359  35.891  -72.704  1.00 35.63  ? 76  LEU A CA  1 
ATOM   617   C C   . LEU A  1 76  ? -54.998  37.222  -73.116  1.00 33.15  ? 76  LEU A C   1 
ATOM   618   O O   . LEU A  1 76  ? -56.166  37.202  -73.511  1.00 32.52  ? 76  LEU A O   1 
ATOM   619   C CB  . LEU A  1 76  ? -54.306  35.745  -71.187  1.00 36.21  ? 76  LEU A CB  1 
ATOM   620   C CG  . LEU A  1 76  ? -55.146  34.631  -70.562  1.00 37.36  ? 76  LEU A CG  1 
ATOM   621   C CD1 . LEU A  1 76  ? -55.303  34.983  -69.102  1.00 37.20  ? 76  LEU A CD1 1 
ATOM   622   C CD2 . LEU A  1 76  ? -56.499  34.504  -71.224  1.00 37.12  ? 76  LEU A CD2 1 
ATOM   623   N N   . LYS A  1 77  ? -54.250  38.317  -73.018  1.00 31.42  ? 77  LYS A N   1 
ATOM   624   C CA  . LYS A  1 77  ? -54.782  39.661  -73.336  1.00 33.61  ? 77  LYS A CA  1 
ATOM   625   C C   . LYS A  1 77  ? -55.211  39.704  -74.798  1.00 32.09  ? 77  LYS A C   1 
ATOM   626   O O   . LYS A  1 77  ? -56.247  40.308  -75.088  1.00 31.01  ? 77  LYS A O   1 
ATOM   627   C CB  . LYS A  1 77  ? -53.708  40.711  -73.033  1.00 37.90  ? 77  LYS A CB  1 
ATOM   628   C CG  . LYS A  1 77  ? -54.171  42.152  -72.984  1.00 39.32  ? 77  LYS A CG  1 
ATOM   629   C CD  . LYS A  1 77  ? -53.009  43.084  -72.670  1.00 44.07  ? 77  LYS A CD  1 
ATOM   630   C CE  . LYS A  1 77  ? -53.389  44.525  -72.738  1.00 47.24  ? 77  LYS A CE  1 
ATOM   631   N NZ  . LYS A  1 77  ? -54.485  44.816  -71.814  1.00 47.28  ? 77  LYS A NZ  1 
ATOM   632   N N   . LEU A  1 78  ? -54.432  39.079  -75.667  1.00 30.40  ? 78  LEU A N   1 
ATOM   633   C CA  . LEU A  1 78  ? -54.788  39.017  -77.073  1.00 31.90  ? 78  LEU A CA  1 
ATOM   634   C C   . LEU A  1 78  ? -56.112  38.279  -77.267  1.00 31.38  ? 78  LEU A C   1 
ATOM   635   O O   . LEU A  1 78  ? -56.936  38.694  -78.067  1.00 31.87  ? 78  LEU A O   1 
ATOM   636   C CB  . LEU A  1 78  ? -53.672  38.333  -77.843  1.00 33.34  ? 78  LEU A CB  1 
ATOM   637   C CG  . LEU A  1 78  ? -53.787  38.380  -79.366  1.00 36.20  ? 78  LEU A CG  1 
ATOM   638   C CD1 . LEU A  1 78  ? -53.607  39.818  -79.825  1.00 37.09  ? 78  LEU A CD1 1 
ATOM   639   C CD2 . LEU A  1 78  ? -52.746  37.463  -79.995  1.00 38.54  ? 78  LEU A CD2 1 
ATOM   640   N N   . VAL A  1 79  ? -56.303  37.167  -76.545  1.00 32.14  ? 79  VAL A N   1 
ATOM   641   C CA  . VAL A  1 79  ? -57.541  36.410  -76.642  1.00 30.28  ? 79  VAL A CA  1 
ATOM   642   C C   . VAL A  1 79  ? -58.668  37.278  -76.097  1.00 29.74  ? 79  VAL A C   1 
ATOM   643   O O   . VAL A  1 79  ? -59.767  37.311  -76.662  1.00 28.33  ? 79  VAL A O   1 
ATOM   644   C CB  . VAL A  1 79  ? -57.495  35.068  -75.896  1.00 29.96  ? 79  VAL A CB  1 
ATOM   645   C CG1 . VAL A  1 79  ? -58.829  34.328  -76.000  1.00 29.21  ? 79  VAL A CG1 1 
ATOM   646   C CG2 . VAL A  1 79  ? -56.354  34.189  -76.399  1.00 30.75  ? 79  VAL A CG2 1 
ATOM   647   N N   . GLN A  1 80  ? -58.378  37.959  -74.982  1.00 29.78  ? 80  GLN A N   1 
ATOM   648   C CA  . GLN A  1 80  ? -59.381  38.791  -74.353  1.00 32.25  ? 80  GLN A CA  1 
ATOM   649   C C   . GLN A  1 80  ? -59.880  39.774  -75.423  1.00 32.55  ? 80  GLN A C   1 
ATOM   650   O O   . GLN A  1 80  ? -61.077  39.865  -75.654  1.00 32.09  ? 80  GLN A O   1 
ATOM   651   C CB  . GLN A  1 80  ? -58.838  39.427  -73.062  1.00 33.50  ? 80  GLN A CB  1 
ATOM   652   C CG  . GLN A  1 80  ? -59.816  40.344  -72.304  1.00 31.69  ? 80  GLN A CG  1 
ATOM   653   C CD  . GLN A  1 80  ? -60.866  39.550  -71.548  1.00 32.37  ? 80  GLN A CD  1 
ATOM   654   O OE1 . GLN A  1 80  ? -60.642  38.396  -71.162  1.00 32.85  ? 80  GLN A OE1 1 
ATOM   655   N NE2 . GLN A  1 80  ? -62.061  40.095  -71.393  1.00 32.48  ? 80  GLN A NE2 1 
ATOM   656   N N   . GLU A  1 81  ? -58.954  40.429  -76.137  1.00 33.06  ? 81  GLU A N   1 
ATOM   657   C CA  . GLU A  1 81  ? -59.296  41.550  -77.010  1.00 33.88  ? 81  GLU A CA  1 
ATOM   658   C C   . GLU A  1 81  ? -59.880  41.026  -78.326  1.00 33.10  ? 81  GLU A C   1 
ATOM   659   O O   . GLU A  1 81  ? -60.528  41.788  -79.046  1.00 33.43  ? 81  GLU A O   1 
ATOM   660   C CB  . GLU A  1 81  ? -58.078  42.464  -77.139  1.00 36.65  ? 81  GLU A CB  1 
ATOM   661   C CG  . GLU A  1 81  ? -57.692  43.080  -75.793  1.00 41.34  ? 81  GLU A CG  1 
ATOM   662   C CD  . GLU A  1 81  ? -56.531  44.091  -75.710  1.00 48.02  ? 81  GLU A CD  1 
ATOM   663   O OE1 . GLU A  1 81  ? -55.797  44.382  -76.710  1.00 45.42  ? 81  GLU A OE1 1 
ATOM   664   O OE2 . GLU A  1 81  ? -56.394  44.618  -74.560  1.00 46.30  ? 81  GLU A OE2 1 
ATOM   665   N N   . SER A  1 82  ? -59.749  39.702  -78.585  1.00 29.08  ? 82  SER A N   1 
ATOM   666   C CA  . SER A  1 82  ? -60.286  39.090  -79.784  1.00 26.79  ? 82  SER A CA  1 
ATOM   667   C C   . SER A  1 82  ? -61.815  39.000  -79.724  1.00 27.87  ? 82  SER A C   1 
ATOM   668   O O   . SER A  1 82  ? -62.444  38.950  -80.781  1.00 27.98  ? 82  SER A O   1 
ATOM   669   C CB  . SER A  1 82  ? -59.713  37.734  -79.974  1.00 26.65  ? 82  SER A CB  1 
ATOM   670   O OG  . SER A  1 82  ? -60.381  36.767  -79.168  1.00 25.13  ? 82  SER A OG  1 
ATOM   671   N N   . GLY A  1 83  ? -62.392  38.910  -78.511  1.00 27.11  ? 83  GLY A N   1 
ATOM   672   C CA  . GLY A  1 83  ? -63.810  38.654  -78.334  1.00 28.12  ? 83  GLY A CA  1 
ATOM   673   C C   . GLY A  1 83  ? -64.095  37.164  -78.098  1.00 30.12  ? 83  GLY A C   1 
ATOM   674   O O   . GLY A  1 83  ? -65.156  36.816  -77.595  1.00 29.85  ? 83  GLY A O   1 
ATOM   675   N N   . LEU A  1 84  ? -63.151  36.258  -78.447  1.00 29.55  ? 84  LEU A N   1 
ATOM   676   C CA  . LEU A  1 84  ? -63.385  34.833  -78.238  1.00 26.39  ? 84  LEU A CA  1 
ATOM   677   C C   . LEU A  1 84  ? -63.337  34.518  -76.749  1.00 26.13  ? 84  LEU A C   1 
ATOM   678   O O   . LEU A  1 84  ? -62.632  35.208  -76.021  1.00 24.93  ? 84  LEU A O   1 
ATOM   679   C CB  . LEU A  1 84  ? -62.355  33.997  -78.980  1.00 25.46  ? 84  LEU A CB  1 
ATOM   680   C CG  . LEU A  1 84  ? -62.417  34.064  -80.499  1.00 25.89  ? 84  LEU A CG  1 
ATOM   681   C CD1 . LEU A  1 84  ? -61.100  33.593  -81.027  1.00 26.18  ? 84  LEU A CD1 1 
ATOM   682   C CD2 . LEU A  1 84  ? -63.573  33.261  -81.065  1.00 25.95  ? 84  LEU A CD2 1 
ATOM   683   N N   . LYS A  1 85  ? -64.042  33.434  -76.347  1.00 24.58  ? 85  LYS A N   1 
ATOM   684   C CA  . LYS A  1 85  ? -63.960  32.906  -75.008  1.00 24.07  ? 85  LYS A CA  1 
ATOM   685   C C   . LYS A  1 85  ? -62.870  31.846  -74.997  1.00 25.55  ? 85  LYS A C   1 
ATOM   686   O O   . LYS A  1 85  ? -62.414  31.400  -76.056  1.00 24.60  ? 85  LYS A O   1 
ATOM   687   C CB  . LYS A  1 85  ? -65.286  32.284  -74.578  1.00 24.26  ? 85  LYS A CB  1 
ATOM   688   C CG  . LYS A  1 85  ? -66.497  33.196  -74.739  1.00 25.12  ? 85  LYS A CG  1 
ATOM   689   C CD  . LYS A  1 85  ? -66.421  34.518  -73.982  1.00 25.45  ? 85  LYS A CD  1 
ATOM   690   C CE  . LYS A  1 85  ? -67.498  35.478  -74.405  1.00 26.95  ? 85  LYS A CE  1 
ATOM   691   N NZ  . LYS A  1 85  ? -67.454  36.674  -73.558  1.00 28.24  ? 85  LYS A NZ  1 
ATOM   692   N N   . LEU A  1 86  ? -62.439  31.467  -73.786  1.00 26.02  ? 86  LEU A N   1 
ATOM   693   C CA  . LEU A  1 86  ? -61.302  30.573  -73.660  1.00 26.38  ? 86  LEU A CA  1 
ATOM   694   C C   . LEU A  1 86  ? -61.669  29.484  -72.661  1.00 26.87  ? 86  LEU A C   1 
ATOM   695   O O   . LEU A  1 86  ? -62.163  29.754  -71.570  1.00 28.80  ? 86  LEU A O   1 
ATOM   696   C CB  . LEU A  1 86  ? -60.030  31.339  -73.271  1.00 24.98  ? 86  LEU A CB  1 
ATOM   697   C CG  . LEU A  1 86  ? -58.833  30.495  -72.853  1.00 25.68  ? 86  LEU A CG  1 
ATOM   698   C CD1 . LEU A  1 86  ? -58.411  29.566  -73.972  1.00 25.32  ? 86  LEU A CD1 1 
ATOM   699   C CD2 . LEU A  1 86  ? -57.632  31.303  -72.430  1.00 25.68  ? 86  LEU A CD2 1 
ATOM   700   N N   . ILE A  1 87  ? -61.437  28.235  -73.060  1.00 27.30  ? 87  ILE A N   1 
ATOM   701   C CA  . ILE A  1 87  ? -61.408  27.121  -72.111  1.00 26.09  ? 87  ILE A CA  1 
ATOM   702   C C   . ILE A  1 87  ? -59.936  26.744  -71.963  1.00 25.67  ? 87  ILE A C   1 
ATOM   703   O O   . ILE A  1 87  ? -59.370  26.220  -72.911  1.00 25.11  ? 87  ILE A O   1 
ATOM   704   C CB  . ILE A  1 87  ? -62.272  25.951  -72.609  1.00 24.25  ? 87  ILE A CB  1 
ATOM   705   C CG1 . ILE A  1 87  ? -63.740  26.327  -72.693  1.00 24.42  ? 87  ILE A CG1 1 
ATOM   706   C CG2 . ILE A  1 87  ? -62.060  24.716  -71.732  1.00 25.77  ? 87  ILE A CG2 1 
ATOM   707   C CD1 . ILE A  1 87  ? -64.595  25.296  -73.413  1.00 24.70  ? 87  ILE A CD1 1 
ATOM   708   N N   . MET A  1 88  ? -59.316  27.101  -70.833  1.00 26.30  ? 88  MET A N   1 
ATOM   709   C CA  . MET A  1 88  ? -57.868  27.064  -70.698  1.00 27.57  ? 88  MET A CA  1 
ATOM   710   C C   . MET A  1 88  ? -57.432  25.804  -69.946  1.00 26.76  ? 88  MET A C   1 
ATOM   711   O O   . MET A  1 88  ? -57.753  25.625  -68.776  1.00 25.08  ? 88  MET A O   1 
ATOM   712   C CB  . MET A  1 88  ? -57.327  28.288  -69.943  1.00 28.30  ? 88  MET A CB  1 
ATOM   713   C CG  . MET A  1 88  ? -55.803  28.310  -69.874  1.00 28.39  ? 88  MET A CG  1 
ATOM   714   S SD  . MET A  1 88  ? -55.108  29.955  -69.614  1.00 29.66  ? 88  MET A SD  1 
ATOM   715   C CE  . MET A  1 88  ? -55.582  30.095  -67.898  1.00 30.23  ? 88  MET A CE  1 
ATOM   716   N N   . GLY A  1 89  ? -56.624  24.979  -70.615  1.00 26.65  ? 89  GLY A N   1 
ATOM   717   C CA  . GLY A  1 89  ? -56.040  23.803  -69.987  1.00 27.61  ? 89  GLY A CA  1 
ATOM   718   C C   . GLY A  1 89  ? -54.755  24.171  -69.261  1.00 28.83  ? 89  GLY A C   1 
ATOM   719   O O   . GLY A  1 89  ? -54.053  25.117  -69.661  1.00 26.69  ? 89  GLY A O   1 
ATOM   720   N N   . ILE A  1 90  ? -54.524  23.439  -68.162  1.00 28.94  ? 90  ILE A N   1 
ATOM   721   C CA  . ILE A  1 90  ? -53.323  23.591  -67.370  1.00 30.22  ? 90  ILE A CA  1 
ATOM   722   C C   . ILE A  1 90  ? -52.467  22.361  -67.634  1.00 30.49  ? 90  ILE A C   1 
ATOM   723   O O   . ILE A  1 90  ? -52.997  21.258  -67.791  1.00 29.67  ? 90  ILE A O   1 
ATOM   724   C CB  . ILE A  1 90  ? -53.660  23.788  -65.879  1.00 32.49  ? 90  ILE A CB  1 
ATOM   725   C CG1 . ILE A  1 90  ? -54.656  24.948  -65.660  1.00 31.70  ? 90  ILE A CG1 1 
ATOM   726   C CG2 . ILE A  1 90  ? -52.402  23.980  -65.012  1.00 32.09  ? 90  ILE A CG2 1 
ATOM   727   C CD1 . ILE A  1 90  ? -54.109  26.311  -66.022  1.00 31.74  ? 90  ILE A CD1 1 
ATOM   728   N N   . ASP A  1 91  ? -51.159  22.595  -67.793  1.00 30.86  ? 91  ASP A N   1 
ATOM   729   C CA  . ASP A  1 91  ? -50.191  21.551  -68.129  1.00 33.16  ? 91  ASP A CA  1 
ATOM   730   C C   . ASP A  1 91  ? -49.808  20.794  -66.856  1.00 33.46  ? 91  ASP A C   1 
ATOM   731   O O   . ASP A  1 91  ? -48.819  21.119  -66.202  1.00 35.81  ? 91  ASP A O   1 
ATOM   732   C CB  . ASP A  1 91  ? -48.960  22.142  -68.817  1.00 33.17  ? 91  ASP A CB  1 
ATOM   733   C CG  . ASP A  1 91  ? -47.909  21.164  -69.336  1.00 36.08  ? 91  ASP A CG  1 
ATOM   734   O OD1 . ASP A  1 91  ? -48.083  19.925  -69.216  1.00 32.16  ? 91  ASP A OD1 1 
ATOM   735   O OD2 . ASP A  1 91  ? -46.917  21.664  -69.879  1.00 42.93  ? 91  ASP A OD2 1 
ATOM   736   N N   . ILE A  1 92  ? -50.641  19.838  -66.461  1.00 32.42  ? 92  ILE A N   1 
ATOM   737   C CA  . ILE A  1 92  ? -50.367  19.010  -65.302  1.00 34.09  ? 92  ILE A CA  1 
ATOM   738   C C   . ILE A  1 92  ? -50.022  17.637  -65.874  1.00 35.16  ? 92  ILE A C   1 
ATOM   739   O O   . ILE A  1 92  ? -50.935  16.935  -66.314  1.00 33.52  ? 92  ILE A O   1 
ATOM   740   C CB  . ILE A  1 92  ? -51.571  18.993  -64.327  1.00 33.48  ? 92  ILE A CB  1 
ATOM   741   C CG1 . ILE A  1 92  ? -51.965  20.379  -63.853  1.00 31.81  ? 92  ILE A CG1 1 
ATOM   742   C CG2 . ILE A  1 92  ? -51.330  18.085  -63.125  1.00 34.80  ? 92  ILE A CG2 1 
ATOM   743   C CD1 . ILE A  1 92  ? -50.938  21.076  -62.990  1.00 33.63  ? 92  ILE A CD1 1 
ATOM   744   N N   . LYS A  1 93  ? -48.714  17.315  -65.945  1.00 36.00  ? 93  LYS A N   1 
ATOM   745   C CA  . LYS A  1 93  ? -48.223  16.107  -66.611  1.00 40.07  ? 93  LYS A CA  1 
ATOM   746   C C   . LYS A  1 93  ? -49.000  14.872  -66.135  1.00 36.56  ? 93  LYS A C   1 
ATOM   747   O O   . LYS A  1 93  ? -48.949  14.503  -64.963  1.00 33.54  ? 93  LYS A O   1 
ATOM   748   C CB  . LYS A  1 93  ? -46.741  15.805  -66.315  1.00 46.46  ? 93  LYS A CB  1 
ATOM   749   C CG  . LYS A  1 93  ? -45.682  16.722  -66.906  1.00 54.44  ? 93  LYS A CG  1 
ATOM   750   C CD  . LYS A  1 93  ? -45.628  16.761  -68.434  1.00 64.13  ? 93  LYS A CD  1 
ATOM   751   C CE  . LYS A  1 93  ? -44.682  17.806  -69.013  1.00 66.63  ? 93  LYS A CE  1 
ATOM   752   N NZ  . LYS A  1 93  ? -44.823  17.963  -70.468  1.00 64.41  ? 93  LYS A NZ  1 
ATOM   753   N N   . PRO A  1 94  ? -49.715  14.168  -67.027  1.00 36.86  ? 94  PRO A N   1 
ATOM   754   C CA  . PRO A  1 94  ? -50.501  12.995  -66.618  1.00 39.21  ? 94  PRO A CA  1 
ATOM   755   C C   . PRO A  1 94  ? -49.756  11.745  -66.149  1.00 37.71  ? 94  PRO A C   1 
ATOM   756   O O   . PRO A  1 94  ? -50.333  10.904  -65.490  1.00 39.71  ? 94  PRO A O   1 
ATOM   757   C CB  . PRO A  1 94  ? -51.346  12.662  -67.879  1.00 40.27  ? 94  PRO A CB  1 
ATOM   758   C CG  . PRO A  1 94  ? -50.608  13.323  -69.047  1.00 41.91  ? 94  PRO A CG  1 
ATOM   759   C CD  . PRO A  1 94  ? -49.791  14.472  -68.466  1.00 37.91  ? 94  PRO A CD  1 
ATOM   760   N N   . GLU A  1 95  ? -48.487  11.604  -66.518  1.00 39.13  ? 95  GLU A N   1 
ATOM   761   C CA  . GLU A  1 95  ? -47.733  10.383  -66.268  1.00 41.29  ? 95  GLU A CA  1 
ATOM   762   C C   . GLU A  1 95  ? -46.925  10.539  -64.970  1.00 38.70  ? 95  GLU A C   1 
ATOM   763   O O   . GLU A  1 95  ? -46.366  9.584   -64.458  1.00 35.38  ? 95  GLU A O   1 
ATOM   764   C CB  . GLU A  1 95  ? -46.995  9.993   -67.561  1.00 44.41  ? 95  GLU A CB  1 
ATOM   765   C CG  . GLU A  1 95  ? -45.985  11.028  -68.060  1.00 56.34  ? 95  GLU A CG  1 
ATOM   766   C CD  . GLU A  1 95  ? -46.541  12.384  -68.522  1.00 61.17  ? 95  GLU A CD  1 
ATOM   767   O OE1 . GLU A  1 95  ? -47.485  12.386  -69.346  1.00 59.08  ? 95  GLU A OE1 1 
ATOM   768   O OE2 . GLU A  1 95  ? -46.049  13.450  -68.067  1.00 68.61  ? 95  GLU A OE2 1 
ATOM   769   N N   . GLU A  1 96  ? -46.933  11.734  -64.365  1.00 39.58  ? 96  GLU A N   1 
ATOM   770   C CA  . GLU A  1 96  ? -46.281  11.980  -63.082  1.00 37.99  ? 96  GLU A CA  1 
ATOM   771   C C   . GLU A  1 96  ? -47.066  11.350  -61.922  1.00 35.43  ? 96  GLU A C   1 
ATOM   772   O O   . GLU A  1 96  ? -48.266  11.076  -62.029  1.00 34.07  ? 96  GLU A O   1 
ATOM   773   C CB  . GLU A  1 96  ? -46.131  13.482  -62.832  1.00 40.75  ? 96  GLU A CB  1 
ATOM   774   C CG  . GLU A  1 96  ? -45.101  14.158  -63.736  1.00 46.95  ? 96  GLU A CG  1 
ATOM   775   C CD  . GLU A  1 96  ? -43.669  13.730  -63.456  1.00 50.35  ? 96  GLU A CD  1 
ATOM   776   O OE1 . GLU A  1 96  ? -43.149  14.119  -62.400  1.00 48.74  ? 96  GLU A OE1 1 
ATOM   777   O OE2 . GLU A  1 96  ? -43.104  12.963  -64.259  1.00 57.95  ? 96  GLU A OE2 1 
ATOM   778   N N   . ASP A  1 97  ? -46.367  11.171  -60.794  1.00 33.20  ? 97  ASP A N   1 
ATOM   779   C CA  . ASP A  1 97  ? -46.940  10.687  -59.561  1.00 33.56  ? 97  ASP A CA  1 
ATOM   780   C C   . ASP A  1 97  ? -47.689  11.823  -58.852  1.00 33.84  ? 97  ASP A C   1 
ATOM   781   O O   . ASP A  1 97  ? -47.082  12.635  -58.144  1.00 30.46  ? 97  ASP A O   1 
ATOM   782   C CB  . ASP A  1 97  ? -45.868  10.066  -58.679  1.00 35.69  ? 97  ASP A CB  1 
ATOM   783   C CG  . ASP A  1 97  ? -46.358  9.337   -57.432  1.00 36.34  ? 97  ASP A CG  1 
ATOM   784   O OD1 . ASP A  1 97  ? -47.582  9.366   -57.167  1.00 32.88  ? 97  ASP A OD1 1 
ATOM   785   O OD2 . ASP A  1 97  ? -45.498  8.761   -56.727  1.00 40.29  ? 97  ASP A OD2 1 
ATOM   786   N N   . TYR A  1 98  ? -49.038  11.759  -58.936  1.00 35.40  ? 98  TYR A N   1 
ATOM   787   C CA  . TYR A  1 98  ? -49.947  12.727  -58.322  1.00 35.94  ? 98  TYR A CA  1 
ATOM   788   C C   . TYR A  1 98  ? -49.757  12.832  -56.798  1.00 35.80  ? 98  TYR A C   1 
ATOM   789   O O   . TYR A  1 98  ? -50.161  13.825  -56.172  1.00 35.53  ? 98  TYR A O   1 
ATOM   790   C CB  . TYR A  1 98  ? -51.364  12.262  -58.672  1.00 37.02  ? 98  TYR A CB  1 
ATOM   791   C CG  . TYR A  1 98  ? -51.667  11.969  -60.133  1.00 36.06  ? 98  TYR A CG  1 
ATOM   792   C CD1 . TYR A  1 98  ? -51.100  12.709  -61.154  1.00 35.52  ? 98  TYR A CD1 1 
ATOM   793   C CD2 . TYR A  1 98  ? -52.526  10.937  -60.488  1.00 34.93  ? 98  TYR A CD2 1 
ATOM   794   C CE1 . TYR A  1 98  ? -51.395  12.449  -62.481  1.00 34.41  ? 98  TYR A CE1 1 
ATOM   795   C CE2 . TYR A  1 98  ? -52.822  10.669  -61.808  1.00 33.38  ? 98  TYR A CE2 1 
ATOM   796   C CZ  . TYR A  1 98  ? -52.264  11.430  -62.809  1.00 33.39  ? 98  TYR A CZ  1 
ATOM   797   O OH  . TYR A  1 98  ? -52.566  11.189  -64.125  1.00 33.96  ? 98  TYR A OH  1 
ATOM   798   N N   . GLY A  1 99  ? -49.152  11.794  -56.195  1.00 35.30  ? 99  GLY A N   1 
ATOM   799   C CA  . GLY A  1 99  ? -48.977  11.698  -54.751  1.00 34.87  ? 99  GLY A CA  1 
ATOM   800   C C   . GLY A  1 99  ? -47.625  12.222  -54.287  1.00 35.47  ? 99  GLY A C   1 
ATOM   801   O O   . GLY A  1 99  ? -47.412  12.345  -53.083  1.00 36.35  ? 99  GLY A O   1 
ATOM   802   N N   . ASP A  1 100 ? -46.742  12.566  -55.237  1.00 34.47  ? 100 ASP A N   1 
ATOM   803   C CA  . ASP A  1 100 ? -45.416  13.078  -54.911  1.00 35.49  ? 100 ASP A CA  1 
ATOM   804   C C   . ASP A  1 100 ? -45.528  14.533  -54.425  1.00 34.16  ? 100 ASP A C   1 
ATOM   805   O O   . ASP A  1 100 ? -45.942  15.390  -55.197  1.00 31.33  ? 100 ASP A O   1 
ATOM   806   C CB  . ASP A  1 100 ? -44.515  12.957  -56.137  1.00 35.30  ? 100 ASP A CB  1 
ATOM   807   C CG  . ASP A  1 100 ? -43.080  13.433  -55.972  1.00 36.48  ? 100 ASP A CG  1 
ATOM   808   O OD1 . ASP A  1 100 ? -42.834  14.315  -55.106  1.00 37.33  ? 100 ASP A OD1 1 
ATOM   809   O OD2 . ASP A  1 100 ? -42.211  12.889  -56.694  1.00 37.61  ? 100 ASP A OD2 1 
ATOM   810   N N   . PRO A  1 101 ? -45.121  14.870  -53.176  1.00 34.71  ? 101 PRO A N   1 
ATOM   811   C CA  . PRO A  1 101 ? -45.318  16.227  -52.625  1.00 35.79  ? 101 PRO A CA  1 
ATOM   812   C C   . PRO A  1 101 ? -44.650  17.386  -53.390  1.00 35.54  ? 101 PRO A C   1 
ATOM   813   O O   . PRO A  1 101 ? -45.110  18.536  -53.322  1.00 35.90  ? 101 PRO A O   1 
ATOM   814   C CB  . PRO A  1 101 ? -44.755  16.135  -51.171  1.00 36.43  ? 101 PRO A CB  1 
ATOM   815   C CG  . PRO A  1 101 ? -44.514  14.655  -50.920  1.00 36.51  ? 101 PRO A CG  1 
ATOM   816   C CD  . PRO A  1 101 ? -44.360  13.995  -52.265  1.00 35.52  ? 101 PRO A CD  1 
ATOM   817   N N   . GLU A  1 102 ? -43.565  17.048  -54.106  1.00 34.96  ? 102 GLU A N   1 
ATOM   818   C CA  . GLU A  1 102 ? -42.794  17.962  -54.925  1.00 34.56  ? 102 GLU A CA  1 
ATOM   819   C C   . GLU A  1 102 ? -43.586  18.281  -56.180  1.00 33.90  ? 102 GLU A C   1 
ATOM   820   O O   . GLU A  1 102 ? -43.683  19.447  -56.595  1.00 34.74  ? 102 GLU A O   1 
ATOM   821   C CB  . GLU A  1 102 ? -41.435  17.371  -55.308  1.00 34.62  ? 102 GLU A CB  1 
ATOM   822   C CG  . GLU A  1 102 ? -40.432  17.356  -54.159  1.00 36.16  ? 102 GLU A CG  1 
ATOM   823   C CD  . GLU A  1 102 ? -39.106  16.680  -54.440  1.00 37.04  ? 102 GLU A CD  1 
ATOM   824   O OE1 . GLU A  1 102 ? -39.074  15.987  -55.453  1.00 38.44  ? 102 GLU A OE1 1 
ATOM   825   O OE2 . GLU A  1 102 ? -38.124  16.797  -53.702  1.00 38.61  ? 102 GLU A OE2 1 
ATOM   826   N N   . PHE A  1 103 ? -44.116  17.216  -56.793  1.00 33.36  ? 103 PHE A N   1 
ATOM   827   C CA  . PHE A  1 103 ? -44.984  17.349  -57.955  1.00 32.18  ? 103 PHE A CA  1 
ATOM   828   C C   . PHE A  1 103 ? -46.216  18.181  -57.593  1.00 32.51  ? 103 PHE A C   1 
ATOM   829   O O   . PHE A  1 103 ? -46.584  19.044  -58.367  1.00 34.91  ? 103 PHE A O   1 
ATOM   830   C CB  . PHE A  1 103 ? -45.431  15.997  -58.526  1.00 30.47  ? 103 PHE A CB  1 
ATOM   831   C CG  . PHE A  1 103 ? -46.341  16.208  -59.716  1.00 28.93  ? 103 PHE A CG  1 
ATOM   832   C CD1 . PHE A  1 103 ? -45.825  16.659  -60.922  1.00 28.54  ? 103 PHE A CD1 1 
ATOM   833   C CD2 . PHE A  1 103 ? -47.713  16.024  -59.604  1.00 29.14  ? 103 PHE A CD2 1 
ATOM   834   C CE1 . PHE A  1 103 ? -46.658  16.900  -61.993  1.00 27.40  ? 103 PHE A CE1 1 
ATOM   835   C CE2 . PHE A  1 103 ? -48.552  16.267  -60.682  1.00 27.80  ? 103 PHE A CE2 1 
ATOM   836   C CZ  . PHE A  1 103 ? -48.023  16.722  -61.863  1.00 27.16  ? 103 PHE A CZ  1 
ATOM   837   N N   . VAL A  1 104 ? -46.834  17.919  -56.432  1.00 33.00  ? 104 VAL A N   1 
ATOM   838   C CA  . VAL A  1 104 ? -48.047  18.589  -56.003  1.00 34.68  ? 104 VAL A CA  1 
ATOM   839   C C   . VAL A  1 104 ? -47.734  20.084  -55.818  1.00 35.34  ? 104 VAL A C   1 
ATOM   840   O O   . VAL A  1 104 ? -48.407  20.965  -56.352  1.00 33.65  ? 104 VAL A O   1 
ATOM   841   C CB  . VAL A  1 104 ? -48.645  17.915  -54.735  1.00 36.06  ? 104 VAL A CB  1 
ATOM   842   C CG1 . VAL A  1 104 ? -49.815  18.681  -54.126  1.00 36.52  ? 104 VAL A CG1 1 
ATOM   843   C CG2 . VAL A  1 104 ? -49.131  16.498  -54.995  1.00 36.10  ? 104 VAL A CG2 1 
ATOM   844   N N   . LYS A  1 105 ? -46.672  20.351  -55.079  1.00 36.65  ? 105 LYS A N   1 
ATOM   845   C CA  . LYS A  1 105 ? -46.251  21.704  -54.788  1.00 37.63  ? 105 LYS A CA  1 
ATOM   846   C C   . LYS A  1 105 ? -45.909  22.460  -56.074  1.00 37.48  ? 105 LYS A C   1 
ATOM   847   O O   . LYS A  1 105 ? -46.301  23.605  -56.205  1.00 37.94  ? 105 LYS A O   1 
ATOM   848   C CB  . LYS A  1 105 ? -45.101  21.596  -53.776  1.00 40.48  ? 105 LYS A CB  1 
ATOM   849   C CG  . LYS A  1 105 ? -44.367  22.888  -53.424  1.00 42.89  ? 105 LYS A CG  1 
ATOM   850   C CD  . LYS A  1 105 ? -45.222  23.975  -52.802  1.00 46.09  ? 105 LYS A CD  1 
ATOM   851   C CE  . LYS A  1 105 ? -45.942  23.557  -51.566  1.00 50.85  ? 105 LYS A CE  1 
ATOM   852   N NZ  . LYS A  1 105 ? -46.361  24.767  -50.845  1.00 54.02  ? 105 LYS A NZ  1 
ATOM   853   N N   . ASP A  1 106 ? -45.226  21.840  -57.045  1.00 38.43  ? 106 ASP A N   1 
ATOM   854   C CA  . ASP A  1 106 ? -44.822  22.552  -58.250  1.00 37.19  ? 106 ASP A CA  1 
ATOM   855   C C   . ASP A  1 106 ? -46.071  22.901  -59.055  1.00 36.48  ? 106 ASP A C   1 
ATOM   856   O O   . ASP A  1 106 ? -46.167  23.971  -59.678  1.00 36.01  ? 106 ASP A O   1 
ATOM   857   C CB  . ASP A  1 106 ? -43.824  21.757  -59.085  1.00 36.75  ? 106 ASP A CB  1 
ATOM   858   C CG  . ASP A  1 106 ? -42.404  21.640  -58.543  1.00 38.43  ? 106 ASP A CG  1 
ATOM   859   O OD1 . ASP A  1 106 ? -42.038  22.349  -57.588  1.00 40.46  ? 106 ASP A OD1 1 
ATOM   860   O OD2 . ASP A  1 106 ? -41.668  20.809  -59.061  1.00 40.60  ? 106 ASP A OD2 1 
ATOM   861   N N   . SER A  1 107 ? -47.037  21.982  -59.012  1.00 34.30  ? 107 SER A N   1 
ATOM   862   C CA  . SER A  1 107 ? -48.268  22.158  -59.744  1.00 34.92  ? 107 SER A CA  1 
ATOM   863   C C   . SER A  1 107 ? -49.061  23.301  -59.113  1.00 36.03  ? 107 SER A C   1 
ATOM   864   O O   . SER A  1 107 ? -49.629  24.130  -59.818  1.00 36.25  ? 107 SER A O   1 
ATOM   865   C CB  . SER A  1 107 ? -49.045  20.860  -59.792  1.00 35.18  ? 107 SER A CB  1 
ATOM   866   O OG  . SER A  1 107 ? -48.298  19.822  -60.432  1.00 34.90  ? 107 SER A OG  1 
ATOM   867   N N   . GLU A  1 108 ? -49.067  23.362  -57.778  1.00 37.42  ? 108 GLU A N   1 
ATOM   868   C CA  . GLU A  1 108 ? -49.780  24.406  -57.054  1.00 38.67  ? 108 GLU A CA  1 
ATOM   869   C C   . GLU A  1 108 ? -49.146  25.772  -57.283  1.00 37.98  ? 108 GLU A C   1 
ATOM   870   O O   . GLU A  1 108 ? -49.867  26.732  -57.535  1.00 37.09  ? 108 GLU A O   1 
ATOM   871   C CB  . GLU A  1 108 ? -49.788  24.190  -55.542  1.00 40.56  ? 108 GLU A CB  1 
ATOM   872   C CG  . GLU A  1 108 ? -50.557  22.944  -55.090  1.00 39.92  ? 108 GLU A CG  1 
ATOM   873   C CD  . GLU A  1 108 ? -50.379  22.669  -53.605  1.00 40.29  ? 108 GLU A CD  1 
ATOM   874   O OE1 . GLU A  1 108 ? -49.241  22.712  -53.113  1.00 41.16  ? 108 GLU A OE1 1 
ATOM   875   O OE2 . GLU A  1 108 ? -51.368  22.427  -52.908  1.00 43.11  ? 108 GLU A OE2 1 
ATOM   876   N N   . ILE A  1 109 ? -47.809  25.856  -57.189  1.00 37.83  ? 109 ILE A N   1 
ATOM   877   C CA  . ILE A  1 109 ? -47.112  27.122  -57.414  1.00 38.12  ? 109 ILE A CA  1 
ATOM   878   C C   . ILE A  1 109 ? -47.403  27.585  -58.841  1.00 36.85  ? 109 ILE A C   1 
ATOM   879   O O   . ILE A  1 109 ? -47.709  28.743  -59.059  1.00 40.01  ? 109 ILE A O   1 
ATOM   880   C CB  . ILE A  1 109 ? -45.593  27.032  -57.147  1.00 39.30  ? 109 ILE A CB  1 
ATOM   881   C CG1 . ILE A  1 109 ? -45.282  26.779  -55.663  1.00 40.93  ? 109 ILE A CG1 1 
ATOM   882   C CG2 . ILE A  1 109 ? -44.837  28.274  -57.638  1.00 40.02  ? 109 ILE A CG2 1 
ATOM   883   C CD1 . ILE A  1 109 ? -43.857  26.288  -55.383  1.00 41.63  ? 109 ILE A CD1 1 
ATOM   884   N N   . GLU A  1 110 ? -47.337  26.669  -59.808  1.00 35.76  ? 110 GLU A N   1 
ATOM   885   C CA  . GLU A  1 110 ? -47.549  27.043  -61.196  1.00 33.62  ? 110 GLU A CA  1 
ATOM   886   C C   . GLU A  1 110 ? -48.992  27.539  -61.359  1.00 32.81  ? 110 GLU A C   1 
ATOM   887   O O   . GLU A  1 110 ? -49.211  28.646  -61.834  1.00 32.06  ? 110 GLU A O   1 
ATOM   888   C CB  . GLU A  1 110 ? -47.066  25.948  -62.151  1.00 31.24  ? 110 GLU A CB  1 
ATOM   889   C CG  . GLU A  1 110 ? -47.227  26.280  -63.635  1.00 31.16  ? 110 GLU A CG  1 
ATOM   890   C CD  . GLU A  1 110 ? -46.633  27.595  -64.158  1.00 32.68  ? 110 GLU A CD  1 
ATOM   891   O OE1 . GLU A  1 110 ? -45.693  28.161  -63.541  1.00 33.41  ? 110 GLU A OE1 1 
ATOM   892   O OE2 . GLU A  1 110 ? -47.114  28.075  -65.209  1.00 31.59  ? 110 GLU A OE2 1 
ATOM   893   N N   . LEU A  1 111 ? -49.980  26.757  -60.919  1.00 33.02  ? 111 LEU A N   1 
ATOM   894   C CA  . LEU A  1 111 ? -51.368  27.167  -61.072  1.00 32.56  ? 111 LEU A CA  1 
ATOM   895   C C   . LEU A  1 111 ? -51.606  28.541  -60.443  1.00 31.82  ? 111 LEU A C   1 
ATOM   896   O O   . LEU A  1 111 ? -52.315  29.350  -61.027  1.00 30.37  ? 111 LEU A O   1 
ATOM   897   C CB  . LEU A  1 111 ? -52.278  26.108  -60.460  1.00 33.99  ? 111 LEU A CB  1 
ATOM   898   C CG  . LEU A  1 111 ? -53.790  26.311  -60.624  1.00 35.01  ? 111 LEU A CG  1 
ATOM   899   C CD1 . LEU A  1 111 ? -54.202  26.822  -61.992  1.00 34.50  ? 111 LEU A CD1 1 
ATOM   900   C CD2 . LEU A  1 111 ? -54.511  24.968  -60.371  1.00 35.05  ? 111 LEU A CD2 1 
ATOM   901   N N   . LYS A  1 112 ? -51.024  28.808  -59.265  1.00 32.83  ? 112 LYS A N   1 
ATOM   902   C CA  . LYS A  1 112 ? -51.244  30.085  -58.601  1.00 34.97  ? 112 LYS A CA  1 
ATOM   903   C C   . LYS A  1 112 ? -50.617  31.239  -59.389  1.00 35.34  ? 112 LYS A C   1 
ATOM   904   O O   . LYS A  1 112 ? -51.152  32.366  -59.405  1.00 33.73  ? 112 LYS A O   1 
ATOM   905   C CB  . LYS A  1 112 ? -50.749  30.107  -57.156  1.00 36.71  ? 112 LYS A CB  1 
ATOM   906   C CG  . LYS A  1 112 ? -51.744  29.559  -56.157  1.00 39.20  ? 112 LYS A CG  1 
ATOM   907   C CD  . LYS A  1 112 ? -51.174  29.491  -54.747  1.00 43.56  ? 112 LYS A CD  1 
ATOM   908   C CE  . LYS A  1 112 ? -51.877  28.489  -53.865  1.00 47.59  ? 112 LYS A CE  1 
ATOM   909   N NZ  . LYS A  1 112 ? -51.060  28.235  -52.670  1.00 49.94  ? 112 LYS A NZ  1 
ATOM   910   N N   . ARG A  1 113 ? -49.481  30.956  -60.042  1.00 36.06  ? 113 ARG A N   1 
ATOM   911   C CA  . ARG A  1 113 ? -48.808  31.969  -60.844  1.00 37.03  ? 113 ARG A CA  1 
ATOM   912   C C   . ARG A  1 113 ? -49.726  32.407  -61.988  1.00 35.47  ? 113 ARG A C   1 
ATOM   913   O O   . ARG A  1 113 ? -49.910  33.608  -62.220  1.00 34.48  ? 113 ARG A O   1 
ATOM   914   C CB  . ARG A  1 113 ? -47.512  31.397  -61.416  1.00 37.70  ? 113 ARG A CB  1 
ATOM   915   C CG  . ARG A  1 113 ? -46.577  32.449  -62.005  1.00 38.48  ? 113 ARG A CG  1 
ATOM   916   C CD  . ARG A  1 113 ? -45.406  31.686  -62.643  1.00 36.69  ? 113 ARG A CD  1 
ATOM   917   N NE  . ARG A  1 113 ? -45.848  30.939  -63.819  1.00 33.46  ? 113 ARG A NE  1 
ATOM   918   C CZ  . ARG A  1 113 ? -46.212  31.466  -64.978  1.00 33.18  ? 113 ARG A CZ  1 
ATOM   919   N NH1 . ARG A  1 113 ? -46.125  32.776  -65.195  1.00 35.04  ? 113 ARG A NH1 1 
ATOM   920   N NH2 . ARG A  1 113 ? -46.650  30.683  -65.943  1.00 31.62  ? 113 ARG A NH2 1 
ATOM   921   N N   . VAL A  1 114 ? -50.324  31.401  -62.648  1.00 32.44  ? 114 VAL A N   1 
ATOM   922   C CA  . VAL A  1 114 ? -51.262  31.621  -63.731  1.00 32.29  ? 114 VAL A CA  1 
ATOM   923   C C   . VAL A  1 114 ? -52.465  32.434  -63.232  1.00 31.75  ? 114 VAL A C   1 
ATOM   924   O O   . VAL A  1 114 ? -52.761  33.489  -63.796  1.00 31.63  ? 114 VAL A O   1 
ATOM   925   C CB  . VAL A  1 114 ? -51.691  30.291  -64.380  1.00 33.28  ? 114 VAL A CB  1 
ATOM   926   C CG1 . VAL A  1 114 ? -52.745  30.522  -65.455  1.00 33.56  ? 114 VAL A CG1 1 
ATOM   927   C CG2 . VAL A  1 114 ? -50.506  29.503  -64.967  1.00 33.08  ? 114 VAL A CG2 1 
ATOM   928   N N   . LEU A  1 115 ? -53.113  31.993  -62.139  1.00 31.25  ? 115 LEU A N   1 
ATOM   929   C CA  . LEU A  1 115 ? -54.358  32.603  -61.694  1.00 31.33  ? 115 LEU A CA  1 
ATOM   930   C C   . LEU A  1 115 ? -54.145  34.079  -61.346  1.00 34.24  ? 115 LEU A C   1 
ATOM   931   O O   . LEU A  1 115 ? -55.054  34.881  -61.531  1.00 33.67  ? 115 LEU A O   1 
ATOM   932   C CB  . LEU A  1 115 ? -54.889  31.852  -60.492  1.00 31.94  ? 115 LEU A CB  1 
ATOM   933   C CG  . LEU A  1 115 ? -55.338  30.421  -60.771  1.00 34.33  ? 115 LEU A CG  1 
ATOM   934   C CD1 . LEU A  1 115 ? -55.770  29.710  -59.500  1.00 35.32  ? 115 LEU A CD1 1 
ATOM   935   C CD2 . LEU A  1 115 ? -56.468  30.405  -61.777  1.00 34.50  ? 115 LEU A CD2 1 
ATOM   936   N N   . ASN A  1 116 ? -52.941  34.418  -60.861  1.00 33.89  ? 116 ASN A N   1 
ATOM   937   C CA  . ASN A  1 116 ? -52.657  35.715  -60.299  1.00 35.71  ? 116 ASN A CA  1 
ATOM   938   C C   . ASN A  1 116 ? -52.869  36.824  -61.331  1.00 34.95  ? 116 ASN A C   1 
ATOM   939   O O   . ASN A  1 116 ? -53.251  37.934  -60.974  1.00 33.12  ? 116 ASN A O   1 
ATOM   940   C CB  . ASN A  1 116 ? -51.262  35.751  -59.698  1.00 39.60  ? 116 ASN A CB  1 
ATOM   941   C CG  . ASN A  1 116 ? -51.092  37.021  -58.911  1.00 45.23  ? 116 ASN A CG  1 
ATOM   942   O OD1 . ASN A  1 116 ? -51.939  37.340  -58.066  1.00 54.04  ? 116 ASN A OD1 1 
ATOM   943   N ND2 . ASN A  1 116 ? -50.073  37.803  -59.223  1.00 46.55  ? 116 ASN A ND2 1 
ATOM   944   N N   . TYR A  1 117 ? -52.672  36.504  -62.613  1.00 34.16  ? 117 TYR A N   1 
ATOM   945   C CA  . TYR A  1 117 ? -53.018  37.424  -63.681  1.00 32.83  ? 117 TYR A CA  1 
ATOM   946   C C   . TYR A  1 117 ? -54.261  36.942  -64.443  1.00 32.28  ? 117 TYR A C   1 
ATOM   947   O O   . TYR A  1 117 ? -55.049  37.767  -64.909  1.00 31.20  ? 117 TYR A O   1 
ATOM   948   C CB  . TYR A  1 117 ? -51.840  37.596  -64.639  1.00 32.06  ? 117 TYR A CB  1 
ATOM   949   C CG  . TYR A  1 117 ? -51.350  36.329  -65.344  1.00 30.78  ? 117 TYR A CG  1 
ATOM   950   C CD1 . TYR A  1 117 ? -51.979  35.837  -66.480  1.00 29.49  ? 117 TYR A CD1 1 
ATOM   951   C CD2 . TYR A  1 117 ? -50.181  35.695  -64.940  1.00 29.30  ? 117 TYR A CD2 1 
ATOM   952   C CE1 . TYR A  1 117 ? -51.508  34.714  -67.136  1.00 28.19  ? 117 TYR A CE1 1 
ATOM   953   C CE2 . TYR A  1 117 ? -49.675  34.608  -65.622  1.00 27.96  ? 117 TYR A CE2 1 
ATOM   954   C CZ  . TYR A  1 117 ? -50.338  34.117  -66.713  1.00 27.59  ? 117 TYR A CZ  1 
ATOM   955   O OH  . TYR A  1 117 ? -49.857  33.010  -67.339  1.00 28.00  ? 117 TYR A OH  1 
ATOM   956   N N   . ALA A  1 118 ? -54.455  35.620  -64.576  1.00 30.72  ? 118 ALA A N   1 
ATOM   957   C CA  . ALA A  1 118 ? -55.544  35.135  -65.412  1.00 30.46  ? 118 ALA A CA  1 
ATOM   958   C C   . ALA A  1 118 ? -56.900  35.581  -64.869  1.00 32.13  ? 118 ALA A C   1 
ATOM   959   O O   . ALA A  1 118 ? -57.854  35.595  -65.619  1.00 35.67  ? 118 ALA A O   1 
ATOM   960   C CB  . ALA A  1 118 ? -55.515  33.625  -65.548  1.00 29.25  ? 118 ALA A CB  1 
ATOM   961   N N   . LYS A  1 119 ? -57.002  35.867  -63.571  1.00 33.86  ? 119 LYS A N   1 
ATOM   962   C CA  . LYS A  1 119 ? -58.260  36.197  -62.927  1.00 35.48  ? 119 LYS A CA  1 
ATOM   963   C C   . LYS A  1 119 ? -58.777  37.566  -63.359  1.00 35.33  ? 119 LYS A C   1 
ATOM   964   O O   . LYS A  1 119 ? -59.900  37.933  -63.007  1.00 34.72  ? 119 LYS A O   1 
ATOM   965   C CB  . LYS A  1 119 ? -58.101  36.231  -61.403  1.00 37.35  ? 119 LYS A CB  1 
ATOM   966   C CG  . LYS A  1 119 ? -57.285  37.427  -60.880  1.00 38.50  ? 119 LYS A CG  1 
ATOM   967   C CD  . LYS A  1 119 ? -56.974  37.390  -59.384  1.00 40.39  ? 119 LYS A CD  1 
ATOM   968   C CE  . LYS A  1 119 ? -56.125  38.555  -58.992  1.00 44.04  ? 119 LYS A CE  1 
ATOM   969   N NZ  . LYS A  1 119 ? -55.586  38.388  -57.644  1.00 46.49  ? 119 LYS A NZ  1 
ATOM   970   N N   . LYS A  1 120 ? -57.933  38.325  -64.059  1.00 34.87  ? 120 LYS A N   1 
ATOM   971   C CA  . LYS A  1 120 ? -58.310  39.624  -64.581  1.00 35.81  ? 120 LYS A CA  1 
ATOM   972   C C   . LYS A  1 120 ? -59.030  39.492  -65.923  1.00 35.33  ? 120 LYS A C   1 
ATOM   973   O O   . LYS A  1 120 ? -59.651  40.450  -66.397  1.00 32.90  ? 120 LYS A O   1 
ATOM   974   C CB  . LYS A  1 120 ? -57.034  40.440  -64.796  1.00 38.84  ? 120 LYS A CB  1 
ATOM   975   C CG  . LYS A  1 120 ? -56.226  40.720  -63.530  1.00 41.59  ? 120 LYS A CG  1 
ATOM   976   C CD  . LYS A  1 120 ? -55.156  41.789  -63.724  1.00 43.51  ? 120 LYS A CD  1 
ATOM   977   C CE  . LYS A  1 120 ? -54.090  41.306  -64.664  1.00 45.62  ? 120 LYS A CE  1 
ATOM   978   N NZ  . LYS A  1 120 ? -53.006  42.294  -64.782  1.00 46.70  ? 120 LYS A NZ  1 
ATOM   979   N N   . TYR A  1 121 ? -58.962  38.302  -66.541  1.00 32.68  ? 121 TYR A N   1 
ATOM   980   C CA  . TYR A  1 121 ? -59.399  38.152  -67.918  1.00 31.62  ? 121 TYR A CA  1 
ATOM   981   C C   . TYR A  1 121 ? -60.685  37.324  -67.958  1.00 32.28  ? 121 TYR A C   1 
ATOM   982   O O   . TYR A  1 121 ? -60.644  36.089  -67.825  1.00 31.05  ? 121 TYR A O   1 
ATOM   983   C CB  . TYR A  1 121 ? -58.218  37.544  -68.682  1.00 31.09  ? 121 TYR A CB  1 
ATOM   984   C CG  . TYR A  1 121 ? -57.010  38.460  -68.731  1.00 30.74  ? 121 TYR A CG  1 
ATOM   985   C CD1 . TYR A  1 121 ? -56.938  39.491  -69.672  1.00 32.87  ? 121 TYR A CD1 1 
ATOM   986   C CD2 . TYR A  1 121 ? -55.989  38.363  -67.800  1.00 30.55  ? 121 TYR A CD2 1 
ATOM   987   C CE1 . TYR A  1 121 ? -55.877  40.391  -69.696  1.00 32.60  ? 121 TYR A CE1 1 
ATOM   988   C CE2 . TYR A  1 121 ? -54.918  39.252  -67.821  1.00 32.42  ? 121 TYR A CE2 1 
ATOM   989   C CZ  . TYR A  1 121 ? -54.852  40.243  -68.785  1.00 32.18  ? 121 TYR A CZ  1 
ATOM   990   O OH  . TYR A  1 121 ? -53.818  41.097  -68.862  1.00 33.73  ? 121 TYR A OH  1 
ATOM   991   N N   . ASP A  1 122 ? -61.826  38.009  -68.176  1.00 31.71  ? 122 ASP A N   1 
ATOM   992   C CA  . ASP A  1 122 ? -63.120  37.348  -68.081  1.00 32.34  ? 122 ASP A CA  1 
ATOM   993   C C   . ASP A  1 122 ? -63.481  36.567  -69.347  1.00 30.28  ? 122 ASP A C   1 
ATOM   994   O O   . ASP A  1 122 ? -64.540  35.960  -69.382  1.00 32.96  ? 122 ASP A O   1 
ATOM   995   C CB  . ASP A  1 122 ? -64.229  38.268  -67.597  1.00 33.03  ? 122 ASP A CB  1 
ATOM   996   C CG  . ASP A  1 122 ? -64.713  39.344  -68.551  1.00 34.00  ? 122 ASP A CG  1 
ATOM   997   O OD1 . ASP A  1 122 ? -64.308  39.350  -69.718  1.00 34.64  ? 122 ASP A OD1 1 
ATOM   998   O OD2 . ASP A  1 122 ? -65.486  40.201  -68.098  1.00 37.66  ? 122 ASP A OD2 1 
ATOM   999   N N   . CYS A  1 123 ? -62.624  36.556  -70.369  1.00 28.11  ? 123 CYS A N   1 
ATOM   1000  C CA  . CYS A  1 123 ? -62.827  35.671  -71.498  1.00 27.40  ? 123 CYS A CA  1 
ATOM   1001  C C   . CYS A  1 123 ? -62.681  34.205  -71.090  1.00 28.01  ? 123 CYS A C   1 
ATOM   1002  O O   . CYS A  1 123 ? -63.169  33.339  -71.815  1.00 29.57  ? 123 CYS A O   1 
ATOM   1003  C CB  . CYS A  1 123 ? -61.880  35.983  -72.646  1.00 27.71  ? 123 CYS A CB  1 
ATOM   1004  S SG  . CYS A  1 123 ? -60.126  35.609  -72.333  1.00 29.07  ? 123 CYS A SG  1 
ATOM   1005  N N   . ILE A  1 124 ? -62.007  33.924  -69.954  1.00 27.42  ? 124 ILE A N   1 
ATOM   1006  C CA  . ILE A  1 124 ? -61.904  32.552  -69.457  1.00 27.60  ? 124 ILE A CA  1 
ATOM   1007  C C   . ILE A  1 124 ? -63.239  32.068  -68.892  1.00 26.66  ? 124 ILE A C   1 
ATOM   1008  O O   . ILE A  1 124 ? -63.715  32.630  -67.921  1.00 26.35  ? 124 ILE A O   1 
ATOM   1009  C CB  . ILE A  1 124 ? -60.782  32.393  -68.409  1.00 27.20  ? 124 ILE A CB  1 
ATOM   1010  C CG1 . ILE A  1 124 ? -59.425  32.807  -69.013  1.00 26.43  ? 124 ILE A CG1 1 
ATOM   1011  C CG2 . ILE A  1 124 ? -60.770  30.945  -67.908  1.00 26.75  ? 124 ILE A CG2 1 
ATOM   1012  C CD1 . ILE A  1 124 ? -58.305  32.922  -68.009  1.00 26.91  ? 124 ILE A CD1 1 
ATOM   1013  N N   . ILE A  1 125 ? -63.799  30.985  -69.459  1.00 28.17  ? 125 ILE A N   1 
ATOM   1014  C CA  . ILE A  1 125 ? -65.103  30.477  -69.019  1.00 28.54  ? 125 ILE A CA  1 
ATOM   1015  C C   . ILE A  1 125 ? -65.030  29.036  -68.512  1.00 27.78  ? 125 ILE A C   1 
ATOM   1016  O O   . ILE A  1 125 ? -66.048  28.487  -68.088  1.00 30.27  ? 125 ILE A O   1 
ATOM   1017  C CB  . ILE A  1 125 ? -66.160  30.608  -70.131  1.00 28.47  ? 125 ILE A CB  1 
ATOM   1018  C CG1 . ILE A  1 125 ? -65.793  29.792  -71.372  1.00 29.21  ? 125 ILE A CG1 1 
ATOM   1019  C CG2 . ILE A  1 125 ? -66.418  32.078  -70.456  1.00 28.83  ? 125 ILE A CG2 1 
ATOM   1020  C CD1 . ILE A  1 125 ? -66.967  29.447  -72.291  1.00 29.09  ? 125 ILE A CD1 1 
ATOM   1021  N N   . THR A  1 126 ? -63.867  28.392  -68.592  1.00 26.03  ? 126 THR A N   1 
ATOM   1022  C CA  . THR A  1 126 ? -63.678  27.100  -67.945  1.00 25.84  ? 126 THR A CA  1 
ATOM   1023  C C   . THR A  1 126 ? -62.168  26.869  -67.831  1.00 26.30  ? 126 THR A C   1 
ATOM   1024  O O   . THR A  1 126 ? -61.416  27.335  -68.675  1.00 24.29  ? 126 THR A O   1 
ATOM   1025  C CB  . THR A  1 126 ? -64.410  25.974  -68.703  1.00 25.15  ? 126 THR A CB  1 
ATOM   1026  O OG1 . THR A  1 126 ? -65.807  26.041  -68.397  1.00 25.71  ? 126 THR A OG1 1 
ATOM   1027  C CG2 . THR A  1 126 ? -64.039  24.573  -68.240  1.00 24.74  ? 126 THR A CG2 1 
ATOM   1028  N N   . TYR A  1 127 ? -61.738  26.214  -66.740  1.00 26.45  ? 127 TYR A N   1 
ATOM   1029  C CA  . TYR A  1 127 ? -60.404  25.662  -66.605  1.00 26.42  ? 127 TYR A CA  1 
ATOM   1030  C C   . TYR A  1 127 ? -60.495  24.140  -66.699  1.00 26.58  ? 127 TYR A C   1 
ATOM   1031  O O   . TYR A  1 127 ? -61.390  23.540  -66.123  1.00 25.59  ? 127 TYR A O   1 
ATOM   1032  C CB  . TYR A  1 127 ? -59.775  26.026  -65.249  1.00 27.67  ? 127 TYR A CB  1 
ATOM   1033  C CG  . TYR A  1 127 ? -59.304  27.460  -65.103  1.00 26.85  ? 127 TYR A CG  1 
ATOM   1034  C CD1 . TYR A  1 127 ? -58.009  27.821  -65.455  1.00 27.38  ? 127 TYR A CD1 1 
ATOM   1035  C CD2 . TYR A  1 127 ? -60.147  28.463  -64.621  1.00 27.67  ? 127 TYR A CD2 1 
ATOM   1036  C CE1 . TYR A  1 127 ? -57.571  29.135  -65.345  1.00 27.96  ? 127 TYR A CE1 1 
ATOM   1037  C CE2 . TYR A  1 127 ? -59.724  29.788  -64.537  1.00 26.84  ? 127 TYR A CE2 1 
ATOM   1038  C CZ  . TYR A  1 127 ? -58.439  30.130  -64.919  1.00 27.05  ? 127 TYR A CZ  1 
ATOM   1039  O OH  . TYR A  1 127 ? -57.973  31.419  -64.851  1.00 28.47  ? 127 TYR A OH  1 
ATOM   1040  N N   . LEU A  1 128 ? -59.528  23.533  -67.408  1.00 28.62  ? 128 LEU A N   1 
ATOM   1041  C CA  . LEU A  1 128 ? -59.310  22.092  -67.465  1.00 28.85  ? 128 LEU A CA  1 
ATOM   1042  C C   . LEU A  1 128 ? -58.009  21.764  -66.747  1.00 29.74  ? 128 LEU A C   1 
ATOM   1043  O O   . LEU A  1 128 ? -56.938  22.202  -67.177  1.00 31.38  ? 128 LEU A O   1 
ATOM   1044  C CB  . LEU A  1 128 ? -59.234  21.612  -68.910  1.00 29.96  ? 128 LEU A CB  1 
ATOM   1045  C CG  . LEU A  1 128 ? -60.444  21.953  -69.785  1.00 29.83  ? 128 LEU A CG  1 
ATOM   1046  C CD1 . LEU A  1 128 ? -60.150  21.499  -71.196  1.00 29.75  ? 128 LEU A CD1 1 
ATOM   1047  C CD2 . LEU A  1 128 ? -61.775  21.389  -69.274  1.00 29.35  ? 128 LEU A CD2 1 
ATOM   1048  N N   . VAL A  1 129 ? -58.123  20.997  -65.657  1.00 29.65  ? 129 VAL A N   1 
ATOM   1049  C CA  . VAL A  1 129 ? -57.056  20.857  -64.684  1.00 29.98  ? 129 VAL A CA  1 
ATOM   1050  C C   . VAL A  1 129 ? -56.142  19.684  -65.012  1.00 30.78  ? 129 VAL A C   1 
ATOM   1051  O O   . VAL A  1 129 ? -55.075  19.587  -64.414  1.00 31.59  ? 129 VAL A O   1 
ATOM   1052  C CB  . VAL A  1 129 ? -57.529  20.764  -63.224  1.00 30.85  ? 129 VAL A CB  1 
ATOM   1053  C CG1 . VAL A  1 129 ? -57.956  22.148  -62.720  1.00 31.27  ? 129 VAL A CG1 1 
ATOM   1054  C CG2 . VAL A  1 129 ? -58.595  19.697  -63.009  1.00 30.53  ? 129 VAL A CG2 1 
ATOM   1055  N N   . ILE A  1 130 ? -56.532  18.797  -65.929  1.00 30.40  ? 130 ILE A N   1 
ATOM   1056  C CA  . ILE A  1 130 ? -55.588  17.774  -66.364  1.00 30.79  ? 130 ILE A CA  1 
ATOM   1057  C C   . ILE A  1 130 ? -56.088  17.162  -67.665  1.00 30.83  ? 130 ILE A C   1 
ATOM   1058  O O   . ILE A  1 130 ? -57.281  17.197  -67.934  1.00 30.51  ? 130 ILE A O   1 
ATOM   1059  C CB  . ILE A  1 130 ? -55.362  16.703  -65.288  1.00 29.45  ? 130 ILE A CB  1 
ATOM   1060  C CG1 . ILE A  1 130 ? -54.234  15.787  -65.660  1.00 30.77  ? 130 ILE A CG1 1 
ATOM   1061  C CG2 . ILE A  1 130 ? -56.643  15.926  -65.043  1.00 30.28  ? 130 ILE A CG2 1 
ATOM   1062  C CD1 . ILE A  1 130 ? -53.756  14.906  -64.520  1.00 31.98  ? 130 ILE A CD1 1 
ATOM   1063  N N   . ASN A  1 131 ? -55.142  16.654  -68.461  1.00 31.26  ? 131 ASN A N   1 
ATOM   1064  C CA  . ASN A  1 131 ? -55.417  16.050  -69.747  1.00 32.61  ? 131 ASN A CA  1 
ATOM   1065  C C   . ASN A  1 131 ? -55.084  14.557  -69.685  1.00 32.93  ? 131 ASN A C   1 
ATOM   1066  O O   . ASN A  1 131 ? -53.919  14.152  -69.672  1.00 32.45  ? 131 ASN A O   1 
ATOM   1067  C CB  . ASN A  1 131 ? -54.651  16.779  -70.847  1.00 32.23  ? 131 ASN A CB  1 
ATOM   1068  C CG  . ASN A  1 131 ? -55.002  16.274  -72.233  1.00 35.52  ? 131 ASN A CG  1 
ATOM   1069  O OD1 . ASN A  1 131 ? -56.181  16.218  -72.614  1.00 39.89  ? 131 ASN A OD1 1 
ATOM   1070  N ND2 . ASN A  1 131 ? -54.002  15.923  -73.032  1.00 35.61  ? 131 ASN A ND2 1 
ATOM   1071  N N   . GLU A  1 132 ? -56.128  13.737  -69.631  1.00 32.87  ? 132 GLU A N   1 
ATOM   1072  C CA  . GLU A  1 132 ? -56.058  12.373  -70.142  1.00 33.75  ? 132 GLU A CA  1 
ATOM   1073  C C   . GLU A  1 132 ? -55.248  11.454  -69.228  1.00 32.62  ? 132 GLU A C   1 
ATOM   1074  O O   . GLU A  1 132 ? -54.269  10.852  -69.660  1.00 35.26  ? 132 GLU A O   1 
ATOM   1075  C CB  . GLU A  1 132 ? -55.442  12.455  -71.540  1.00 35.26  ? 132 GLU A CB  1 
ATOM   1076  C CG  . GLU A  1 132 ? -55.893  11.368  -72.512  1.00 34.64  ? 132 GLU A CG  1 
ATOM   1077  C CD  . GLU A  1 132 ? -57.384  11.498  -72.705  1.00 38.62  ? 132 GLU A CD  1 
ATOM   1078  O OE1 . GLU A  1 132 ? -58.071  10.928  -71.772  1.00 41.01  ? 132 GLU A OE1 1 
ATOM   1079  O OE2 . GLU A  1 132 ? -57.837  12.178  -73.692  1.00 33.63  ? 132 GLU A OE2 1 
ATOM   1080  N N   . PRO A  1 133 ? -55.624  11.305  -67.941  1.00 32.48  ? 133 PRO A N   1 
ATOM   1081  C CA  . PRO A  1 133 ? -54.966  10.351  -67.056  1.00 34.99  ? 133 PRO A CA  1 
ATOM   1082  C C   . PRO A  1 133 ? -55.393  8.935   -67.453  1.00 36.12  ? 133 PRO A C   1 
ATOM   1083  O O   . PRO A  1 133 ? -56.574  8.653   -67.662  1.00 32.81  ? 133 PRO A O   1 
ATOM   1084  C CB  . PRO A  1 133 ? -55.467  10.780  -65.656  1.00 32.50  ? 133 PRO A CB  1 
ATOM   1085  C CG  . PRO A  1 133 ? -56.859  11.286  -65.938  1.00 31.30  ? 133 PRO A CG  1 
ATOM   1086  C CD  . PRO A  1 133 ? -56.707  12.033  -67.248  1.00 32.65  ? 133 PRO A CD  1 
ATOM   1087  N N   . GLN A  1 134 ? -54.384  8.082   -67.584  1.00 36.28  ? 134 GLN A N   1 
ATOM   1088  C CA  . GLN A  1 134 ? -54.550  6.722   -68.041  1.00 36.06  ? 134 GLN A CA  1 
ATOM   1089  C C   . GLN A  1 134 ? -55.025  5.866   -66.874  1.00 36.21  ? 134 GLN A C   1 
ATOM   1090  O O   . GLN A  1 134 ? -54.549  6.024   -65.747  1.00 39.25  ? 134 GLN A O   1 
ATOM   1091  C CB  . GLN A  1 134 ? -53.203  6.227   -68.577  1.00 36.87  ? 134 GLN A CB  1 
ATOM   1092  C CG  . GLN A  1 134 ? -52.853  6.675   -69.997  1.00 37.81  ? 134 GLN A CG  1 
ATOM   1093  C CD  . GLN A  1 134 ? -53.812  6.147   -71.044  1.00 40.78  ? 134 GLN A CD  1 
ATOM   1094  O OE1 . GLN A  1 134 ? -54.385  5.044   -70.978  1.00 44.81  ? 134 GLN A OE1 1 
ATOM   1095  N NE2 . GLN A  1 134 ? -54.112  7.020   -71.974  1.00 42.74  ? 134 GLN A NE2 1 
ATOM   1096  N N   . THR A  1 135 ? -55.909  4.911   -67.171  1.00 35.26  ? 135 THR A N   1 
ATOM   1097  C CA  . THR A  1 135 ? -56.427  3.970   -66.182  1.00 32.56  ? 135 THR A CA  1 
ATOM   1098  C C   . THR A  1 135 ? -55.305  3.327   -65.367  1.00 32.72  ? 135 THR A C   1 
ATOM   1099  O O   . THR A  1 135 ? -55.348  3.360   -64.143  1.00 34.46  ? 135 THR A O   1 
ATOM   1100  C CB  . THR A  1 135 ? -57.300  2.924   -66.876  1.00 32.51  ? 135 THR A CB  1 
ATOM   1101  O OG1 . THR A  1 135 ? -58.291  3.614   -67.647  1.00 33.02  ? 135 THR A OG1 1 
ATOM   1102  C CG2 . THR A  1 135 ? -57.970  1.999   -65.873  1.00 33.32  ? 135 THR A CG2 1 
ATOM   1103  N N   . ASP A  1 136 ? -54.306  2.707   -66.010  1.00 32.73  ? 136 ASP A N   1 
ATOM   1104  C CA  . ASP A  1 136 ? -53.310  1.920   -65.281  1.00 32.24  ? 136 ASP A CA  1 
ATOM   1105  C C   . ASP A  1 136 ? -52.489  2.825   -64.345  1.00 33.10  ? 136 ASP A C   1 
ATOM   1106  O O   . ASP A  1 136 ? -52.153  2.457   -63.204  1.00 33.73  ? 136 ASP A O   1 
ATOM   1107  C CB  . ASP A  1 136 ? -52.442  1.117   -66.244  1.00 32.13  ? 136 ASP A CB  1 
ATOM   1108  C CG  . ASP A  1 136 ? -51.364  0.245   -65.616  1.00 34.27  ? 136 ASP A CG  1 
ATOM   1109  O OD1 . ASP A  1 136 ? -51.685  -0.888  -65.174  1.00 33.93  ? 136 ASP A OD1 1 
ATOM   1110  O OD2 . ASP A  1 136 ? -50.198  0.700   -65.580  1.00 37.24  ? 136 ASP A OD2 1 
ATOM   1111  N N   . HIS A  1 137 ? -52.148  4.025   -64.831  1.00 31.91  ? 137 HIS A N   1 
ATOM   1112  C CA  . HIS A  1 137 ? -51.342  4.965   -64.062  1.00 32.51  ? 137 HIS A CA  1 
ATOM   1113  C C   . HIS A  1 137 ? -52.050  5.314   -62.756  1.00 32.50  ? 137 HIS A C   1 
ATOM   1114  O O   . HIS A  1 137 ? -51.438  5.284   -61.695  1.00 35.25  ? 137 HIS A O   1 
ATOM   1115  C CB  . HIS A  1 137 ? -51.005  6.197   -64.918  1.00 32.16  ? 137 HIS A CB  1 
ATOM   1116  C CG  . HIS A  1 137 ? -50.211  7.216   -64.180  1.00 33.12  ? 137 HIS A CG  1 
ATOM   1117  N ND1 . HIS A  1 137 ? -48.934  6.960   -63.752  1.00 32.54  ? 137 HIS A ND1 1 
ATOM   1118  C CD2 . HIS A  1 137 ? -50.522  8.467   -63.722  1.00 34.13  ? 137 HIS A CD2 1 
ATOM   1119  C CE1 . HIS A  1 137 ? -48.474  8.029   -63.098  1.00 35.13  ? 137 HIS A CE1 1 
ATOM   1120  N NE2 . HIS A  1 137 ? -49.413  8.958   -63.083  1.00 33.75  ? 137 HIS A NE2 1 
ATOM   1121  N N   . ILE A  1 138 ? -53.329  5.691   -62.851  1.00 32.22  ? 138 ILE A N   1 
ATOM   1122  C CA  . ILE A  1 138 ? -54.158  5.987   -61.686  1.00 32.37  ? 138 ILE A CA  1 
ATOM   1123  C C   . ILE A  1 138 ? -54.162  4.770   -60.756  1.00 34.97  ? 138 ILE A C   1 
ATOM   1124  O O   . ILE A  1 138 ? -54.027  4.923   -59.526  1.00 37.32  ? 138 ILE A O   1 
ATOM   1125  C CB  . ILE A  1 138 ? -55.602  6.371   -62.095  1.00 30.74  ? 138 ILE A CB  1 
ATOM   1126  C CG1 . ILE A  1 138 ? -55.663  7.618   -62.938  1.00 31.08  ? 138 ILE A CG1 1 
ATOM   1127  C CG2 . ILE A  1 138 ? -56.476  6.527   -60.867  1.00 31.10  ? 138 ILE A CG2 1 
ATOM   1128  C CD1 . ILE A  1 138 ? -57.075  8.061   -63.270  1.00 31.73  ? 138 ILE A CD1 1 
ATOM   1129  N N   . HIS A  1 139 ? -54.367  3.564   -61.332  1.00 31.67  ? 139 HIS A N   1 
ATOM   1130  C CA  . HIS A  1 139 ? -54.295  2.361   -60.520  1.00 32.52  ? 139 HIS A CA  1 
ATOM   1131  C C   . HIS A  1 139 ? -52.963  2.310   -59.758  1.00 34.12  ? 139 HIS A C   1 
ATOM   1132  O O   . HIS A  1 139 ? -52.909  1.977   -58.569  1.00 33.76  ? 139 HIS A O   1 
ATOM   1133  C CB  . HIS A  1 139 ? -54.491  1.080   -61.347  1.00 31.88  ? 139 HIS A CB  1 
ATOM   1134  C CG  . HIS A  1 139 ? -54.402  -0.126  -60.479  1.00 32.58  ? 139 HIS A CG  1 
ATOM   1135  N ND1 . HIS A  1 139 ? -53.220  -0.780  -60.195  1.00 31.96  ? 139 HIS A ND1 1 
ATOM   1136  C CD2 . HIS A  1 139 ? -55.367  -0.750  -59.792  1.00 32.65  ? 139 HIS A CD2 1 
ATOM   1137  C CE1 . HIS A  1 139 ? -53.497  -1.781  -59.379  1.00 33.25  ? 139 HIS A CE1 1 
ATOM   1138  N NE2 . HIS A  1 139 ? -54.796  -1.802  -59.150  1.00 32.90  ? 139 HIS A NE2 1 
ATOM   1139  N N   . SER A  1 140 ? -51.879  2.633   -60.468  1.00 33.83  ? 140 SER A N   1 
ATOM   1140  C CA  . SER A  1 140 ? -50.538  2.498   -59.924  1.00 34.77  ? 140 SER A CA  1 
ATOM   1141  C C   . SER A  1 140 ? -50.242  3.549   -58.849  1.00 35.77  ? 140 SER A C   1 
ATOM   1142  O O   . SER A  1 140 ? -49.610  3.245   -57.861  1.00 38.43  ? 140 SER A O   1 
ATOM   1143  C CB  . SER A  1 140 ? -49.532  2.552   -61.042  1.00 34.01  ? 140 SER A CB  1 
ATOM   1144  O OG  . SER A  1 140 ? -48.239  2.491   -60.483  1.00 35.34  ? 140 SER A OG  1 
ATOM   1145  N N   . VAL A  1 141 ? -50.677  4.798   -59.004  1.00 35.10  ? 141 VAL A N   1 
ATOM   1146  C CA  . VAL A  1 141 ? -50.313  5.797   -58.003  1.00 35.38  ? 141 VAL A CA  1 
ATOM   1147  C C   . VAL A  1 141 ? -51.450  5.963   -57.005  1.00 36.55  ? 141 VAL A C   1 
ATOM   1148  O O   . VAL A  1 141 ? -51.284  6.704   -56.051  1.00 35.82  ? 141 VAL A O   1 
ATOM   1149  C CB  . VAL A  1 141 ? -49.941  7.153   -58.618  1.00 34.46  ? 141 VAL A CB  1 
ATOM   1150  C CG1 . VAL A  1 141 ? -48.772  7.000   -59.581  1.00 33.30  ? 141 VAL A CG1 1 
ATOM   1151  C CG2 . VAL A  1 141 ? -51.148  7.836   -59.272  1.00 33.68  ? 141 VAL A CG2 1 
ATOM   1152  N N   . THR A  1 142 ? -52.585  5.276   -57.261  1.00 37.69  ? 142 THR A N   1 
ATOM   1153  C CA  . THR A  1 142 ? -53.780  5.231   -56.421  1.00 36.98  ? 142 THR A CA  1 
ATOM   1154  C C   . THR A  1 142 ? -54.764  6.339   -56.814  1.00 37.10  ? 142 THR A C   1 
ATOM   1155  O O   . THR A  1 142 ? -54.404  7.453   -57.200  1.00 37.34  ? 142 THR A O   1 
ATOM   1156  C CB  . THR A  1 142 ? -53.530  5.208   -54.912  1.00 36.76  ? 142 THR A CB  1 
ATOM   1157  O OG1 . THR A  1 142 ? -53.186  6.530   -54.528  1.00 35.85  ? 142 THR A OG1 1 
ATOM   1158  C CG2 . THR A  1 142 ? -52.471  4.209   -54.464  1.00 35.41  ? 142 THR A CG2 1 
ATOM   1159  N N   . GLY A  1 143 ? -56.038  5.952   -56.772  1.00 37.60  ? 143 GLY A N   1 
ATOM   1160  C CA  . GLY A  1 143 ? -57.145  6.829   -57.070  1.00 39.75  ? 143 GLY A CA  1 
ATOM   1161  C C   . GLY A  1 143 ? -57.219  7.956   -56.043  1.00 41.21  ? 143 GLY A C   1 
ATOM   1162  O O   . GLY A  1 143 ? -57.613  9.066   -56.374  1.00 38.87  ? 143 GLY A O   1 
ATOM   1163  N N   . LYS A  1 144 ? -56.847  7.648   -54.799  1.00 41.53  ? 144 LYS A N   1 
ATOM   1164  C CA  . LYS A  1 144 ? -56.873  8.648   -53.756  1.00 45.05  ? 144 LYS A CA  1 
ATOM   1165  C C   . LYS A  1 144 ? -55.858  9.740   -54.109  1.00 44.19  ? 144 LYS A C   1 
ATOM   1166  O O   . LYS A  1 144 ? -56.187  10.921  -54.027  1.00 44.13  ? 144 LYS A O   1 
ATOM   1167  C CB  . LYS A  1 144 ? -56.723  8.054   -52.347  1.00 48.74  ? 144 LYS A CB  1 
ATOM   1168  C CG  . LYS A  1 144 ? -56.823  9.113   -51.231  1.00 52.85  ? 144 LYS A CG  1 
ATOM   1169  C CD  . LYS A  1 144 ? -57.102  8.598   -49.819  1.00 56.49  ? 144 LYS A CD  1 
ATOM   1170  C CE  . LYS A  1 144 ? -56.383  9.345   -48.720  1.00 56.29  ? 144 LYS A CE  1 
ATOM   1171  N NZ  . LYS A  1 144 ? -56.551  10.781  -48.920  1.00 55.37  ? 144 LYS A NZ  1 
ATOM   1172  N N   . ALA A  1 145 ? -54.646  9.361   -54.532  1.00 41.30  ? 145 ALA A N   1 
ATOM   1173  C CA  . ALA A  1 145 ? -53.661  10.360  -54.909  1.00 40.55  ? 145 ALA A CA  1 
ATOM   1174  C C   . ALA A  1 145 ? -54.259  11.242  -56.003  1.00 40.16  ? 145 ALA A C   1 
ATOM   1175  O O   . ALA A  1 145 ? -54.183  12.454  -55.925  1.00 37.28  ? 145 ALA A O   1 
ATOM   1176  C CB  . ALA A  1 145 ? -52.387  9.693   -55.352  1.00 39.66  ? 145 ALA A CB  1 
ATOM   1177  N N   . PHE A  1 146 ? -54.890  10.599  -57.001  1.00 40.07  ? 146 PHE A N   1 
ATOM   1178  C CA  . PHE A  1 146 ? -55.539  11.291  -58.103  1.00 36.92  ? 146 PHE A CA  1 
ATOM   1179  C C   . PHE A  1 146 ? -56.609  12.265  -57.589  1.00 35.44  ? 146 PHE A C   1 
ATOM   1180  O O   . PHE A  1 146 ? -56.581  13.468  -57.896  1.00 32.94  ? 146 PHE A O   1 
ATOM   1181  C CB  . PHE A  1 146 ? -56.163  10.283  -59.081  1.00 35.59  ? 146 PHE A CB  1 
ATOM   1182  C CG  . PHE A  1 146 ? -56.926  10.986  -60.193  1.00 34.57  ? 146 PHE A CG  1 
ATOM   1183  C CD1 . PHE A  1 146 ? -56.257  11.817  -61.102  1.00 33.86  ? 146 PHE A CD1 1 
ATOM   1184  C CD2 . PHE A  1 146 ? -58.311  10.900  -60.275  1.00 32.88  ? 146 PHE A CD2 1 
ATOM   1185  C CE1 . PHE A  1 146 ? -56.965  12.521  -62.076  1.00 32.66  ? 146 PHE A CE1 1 
ATOM   1186  C CE2 . PHE A  1 146 ? -59.007  11.606  -61.248  1.00 32.80  ? 146 PHE A CE2 1 
ATOM   1187  C CZ  . PHE A  1 146 ? -58.336  12.397  -62.164  1.00 31.49  ? 146 PHE A CZ  1 
ATOM   1188  N N   . VAL A  1 147 ? -57.567  11.725  -56.829  1.00 33.46  ? 147 VAL A N   1 
ATOM   1189  C CA  . VAL A  1 147 ? -58.709  12.498  -56.391  1.00 35.02  ? 147 VAL A CA  1 
ATOM   1190  C C   . VAL A  1 147 ? -58.255  13.669  -55.492  1.00 35.78  ? 147 VAL A C   1 
ATOM   1191  O O   . VAL A  1 147 ? -58.771  14.766  -55.604  1.00 33.63  ? 147 VAL A O   1 
ATOM   1192  C CB  . VAL A  1 147 ? -59.775  11.555  -55.779  1.00 34.86  ? 147 VAL A CB  1 
ATOM   1193  C CG1 . VAL A  1 147 ? -60.902  12.301  -55.066  1.00 35.55  ? 147 VAL A CG1 1 
ATOM   1194  C CG2 . VAL A  1 147 ? -60.406  10.646  -56.833  1.00 33.11  ? 147 VAL A CG2 1 
ATOM   1195  N N   . ASP A  1 148 ? -57.275  13.456  -54.612  1.00 37.70  ? 148 ASP A N   1 
ATOM   1196  C CA  . ASP A  1 148 ? -56.745  14.494  -53.751  1.00 38.21  ? 148 ASP A CA  1 
ATOM   1197  C C   . ASP A  1 148 ? -56.104  15.621  -54.553  1.00 38.38  ? 148 ASP A C   1 
ATOM   1198  O O   . ASP A  1 148 ? -56.141  16.794  -54.159  1.00 38.71  ? 148 ASP A O   1 
ATOM   1199  C CB  . ASP A  1 148 ? -55.731  13.908  -52.789  1.00 40.46  ? 148 ASP A CB  1 
ATOM   1200  C CG  . ASP A  1 148 ? -56.348  13.076  -51.674  1.00 44.04  ? 148 ASP A CG  1 
ATOM   1201  O OD1 . ASP A  1 148 ? -57.603  13.106  -51.552  1.00 45.40  ? 148 ASP A OD1 1 
ATOM   1202  O OD2 . ASP A  1 148 ? -55.571  12.409  -50.944  1.00 46.24  ? 148 ASP A OD2 1 
ATOM   1203  N N   . LEU A  1 149 ? -55.450  15.260  -55.650  1.00 37.43  ? 149 LEU A N   1 
ATOM   1204  C CA  . LEU A  1 149 ? -54.785  16.261  -56.463  1.00 37.17  ? 149 LEU A CA  1 
ATOM   1205  C C   . LEU A  1 149 ? -55.856  17.107  -57.155  1.00 37.55  ? 149 LEU A C   1 
ATOM   1206  O O   . LEU A  1 149 ? -55.812  18.332  -57.101  1.00 34.69  ? 149 LEU A O   1 
ATOM   1207  C CB  . LEU A  1 149 ? -53.813  15.597  -57.440  1.00 36.59  ? 149 LEU A CB  1 
ATOM   1208  C CG  . LEU A  1 149 ? -53.156  16.508  -58.487  1.00 36.10  ? 149 LEU A CG  1 
ATOM   1209  C CD1 . LEU A  1 149 ? -52.249  17.519  -57.799  1.00 37.40  ? 149 LEU A CD1 1 
ATOM   1210  C CD2 . LEU A  1 149 ? -52.399  15.740  -59.565  1.00 33.90  ? 149 LEU A CD2 1 
ATOM   1211  N N   . MET A  1 150 ? -56.846  16.447  -57.782  1.00 37.15  ? 150 MET A N   1 
ATOM   1212  C CA  . MET A  1 150 ? -57.938  17.164  -58.433  1.00 35.12  ? 150 MET A CA  1 
ATOM   1213  C C   . MET A  1 150 ? -58.565  18.149  -57.444  1.00 36.10  ? 150 MET A C   1 
ATOM   1214  O O   . MET A  1 150 ? -58.626  19.330  -57.749  1.00 35.24  ? 150 MET A O   1 
ATOM   1215  C CB  . MET A  1 150 ? -59.003  16.234  -59.021  1.00 34.27  ? 150 MET A CB  1 
ATOM   1216  C CG  . MET A  1 150 ? -58.481  15.280  -60.100  1.00 34.26  ? 150 MET A CG  1 
ATOM   1217  S SD  . MET A  1 150 ? -57.787  16.077  -61.565  1.00 35.65  ? 150 MET A SD  1 
ATOM   1218  C CE  . MET A  1 150 ? -56.038  16.175  -61.163  1.00 35.45  ? 150 MET A CE  1 
ATOM   1219  N N   . ASN A  1 151 ? -58.957  17.693  -56.241  1.00 36.86  ? 151 ASN A N   1 
ATOM   1220  C CA  . ASN A  1 151 ? -59.546  18.585  -55.248  1.00 38.91  ? 151 ASN A CA  1 
ATOM   1221  C C   . ASN A  1 151 ? -58.614  19.786  -54.966  1.00 39.79  ? 151 ASN A C   1 
ATOM   1222  O O   . ASN A  1 151 ? -59.047  20.928  -55.063  1.00 39.77  ? 151 ASN A O   1 
ATOM   1223  C CB  . ASN A  1 151 ? -60.031  17.845  -53.998  1.00 38.19  ? 151 ASN A CB  1 
ATOM   1224  C CG  . ASN A  1 151 ? -61.267  16.999  -54.245  1.00 38.19  ? 151 ASN A CG  1 
ATOM   1225  O OD1 . ASN A  1 151 ? -61.330  15.855  -53.790  1.00 42.72  ? 151 ASN A OD1 1 
ATOM   1226  N ND2 . ASN A  1 151 ? -62.272  17.491  -54.944  1.00 35.10  ? 151 ASN A ND2 1 
ATOM   1227  N N   . THR A  1 152 ? -57.327  19.546  -54.691  1.00 38.45  ? 152 THR A N   1 
ATOM   1228  C CA  . THR A  1 152 ? -56.372  20.604  -54.406  1.00 37.92  ? 152 THR A CA  1 
ATOM   1229  C C   . THR A  1 152 ? -56.426  21.681  -55.493  1.00 34.97  ? 152 THR A C   1 
ATOM   1230  O O   . THR A  1 152 ? -56.534  22.865  -55.201  1.00 35.37  ? 152 THR A O   1 
ATOM   1231  C CB  . THR A  1 152 ? -54.976  19.985  -54.295  1.00 39.49  ? 152 THR A CB  1 
ATOM   1232  O OG1 . THR A  1 152 ? -55.067  19.103  -53.184  1.00 41.50  ? 152 THR A OG1 1 
ATOM   1233  C CG2 . THR A  1 152 ? -53.867  20.992  -54.061  1.00 38.64  ? 152 THR A CG2 1 
ATOM   1234  N N   . LEU A  1 153 ? -56.379  21.276  -56.754  1.00 32.31  ? 153 LEU A N   1 
ATOM   1235  C CA  . LEU A  1 153 ? -56.310  22.221  -57.852  1.00 31.08  ? 153 LEU A CA  1 
ATOM   1236  C C   . LEU A  1 153 ? -57.654  22.900  -58.104  1.00 32.06  ? 153 LEU A C   1 
ATOM   1237  O O   . LEU A  1 153 ? -57.684  24.066  -58.522  1.00 32.11  ? 153 LEU A O   1 
ATOM   1238  C CB  . LEU A  1 153 ? -55.830  21.500  -59.102  1.00 29.86  ? 153 LEU A CB  1 
ATOM   1239  C CG  . LEU A  1 153 ? -54.521  20.726  -58.936  1.00 30.83  ? 153 LEU A CG  1 
ATOM   1240  C CD1 . LEU A  1 153 ? -54.037  20.191  -60.255  1.00 30.55  ? 153 LEU A CD1 1 
ATOM   1241  C CD2 . LEU A  1 153 ? -53.451  21.550  -58.260  1.00 32.47  ? 153 LEU A CD2 1 
ATOM   1242  N N   . ILE A  1 154 ? -58.748  22.157  -57.901  1.00 31.44  ? 154 ILE A N   1 
ATOM   1243  C CA  . ILE A  1 154 ? -60.074  22.713  -58.088  1.00 32.63  ? 154 ILE A CA  1 
ATOM   1244  C C   . ILE A  1 154 ? -60.256  23.852  -57.096  1.00 34.11  ? 154 ILE A C   1 
ATOM   1245  O O   . ILE A  1 154 ? -60.797  24.894  -57.468  1.00 32.68  ? 154 ILE A O   1 
ATOM   1246  C CB  . ILE A  1 154 ? -61.182  21.656  -57.930  1.00 31.00  ? 154 ILE A CB  1 
ATOM   1247  C CG1 . ILE A  1 154 ? -61.166  20.699  -59.084  1.00 30.94  ? 154 ILE A CG1 1 
ATOM   1248  C CG2 . ILE A  1 154 ? -62.551  22.318  -57.782  1.00 30.51  ? 154 ILE A CG2 1 
ATOM   1249  C CD1 . ILE A  1 154 ? -61.925  19.414  -58.804  1.00 32.04  ? 154 ILE A CD1 1 
ATOM   1250  N N   . ASN A  1 155 ? -59.815  23.602  -55.854  1.00 35.30  ? 155 ASN A N   1 
ATOM   1251  C CA  . ASN A  1 155 ? -60.031  24.528  -54.754  1.00 39.25  ? 155 ASN A CA  1 
ATOM   1252  C C   . ASN A  1 155 ? -59.191  25.780  -54.956  1.00 38.25  ? 155 ASN A C   1 
ATOM   1253  O O   . ASN A  1 155 ? -59.656  26.843  -54.606  1.00 41.80  ? 155 ASN A O   1 
ATOM   1254  C CB  . ASN A  1 155 ? -59.823  23.873  -53.385  1.00 41.17  ? 155 ASN A CB  1 
ATOM   1255  C CG  . ASN A  1 155 ? -60.943  22.896  -53.049  1.00 43.67  ? 155 ASN A CG  1 
ATOM   1256  O OD1 . ASN A  1 155 ? -62.017  22.888  -53.674  1.00 44.44  ? 155 ASN A OD1 1 
ATOM   1257  N ND2 . ASN A  1 155 ? -60.731  22.057  -52.051  1.00 43.49  ? 155 ASN A ND2 1 
ATOM   1258  N N   . ILE A  1 156 ? -57.968  25.634  -55.482  1.00 36.57  ? 156 ILE A N   1 
ATOM   1259  C CA  . ILE A  1 156 ? -57.073  26.749  -55.718  1.00 35.17  ? 156 ILE A CA  1 
ATOM   1260  C C   . ILE A  1 156 ? -57.677  27.632  -56.808  1.00 35.10  ? 156 ILE A C   1 
ATOM   1261  O O   . ILE A  1 156 ? -57.600  28.854  -56.727  1.00 33.21  ? 156 ILE A O   1 
ATOM   1262  C CB  . ILE A  1 156 ? -55.674  26.231  -56.087  1.00 35.11  ? 156 ILE A CB  1 
ATOM   1263  C CG1 . ILE A  1 156 ? -54.905  25.816  -54.861  1.00 36.24  ? 156 ILE A CG1 1 
ATOM   1264  C CG2 . ILE A  1 156 ? -54.868  27.235  -56.913  1.00 35.39  ? 156 ILE A CG2 1 
ATOM   1265  C CD1 . ILE A  1 156 ? -53.664  24.996  -55.179  1.00 36.99  ? 156 ILE A CD1 1 
ATOM   1266  N N   . ILE A  1 157 ? -58.333  27.004  -57.805  1.00 34.49  ? 157 ILE A N   1 
ATOM   1267  C CA  . ILE A  1 157 ? -58.973  27.786  -58.851  1.00 33.55  ? 157 ILE A CA  1 
ATOM   1268  C C   . ILE A  1 157 ? -60.228  28.507  -58.341  1.00 35.51  ? 157 ILE A C   1 
ATOM   1269  O O   . ILE A  1 157 ? -60.426  29.694  -58.654  1.00 34.73  ? 157 ILE A O   1 
ATOM   1270  C CB  . ILE A  1 157 ? -59.251  26.950  -60.100  1.00 30.76  ? 157 ILE A CB  1 
ATOM   1271  C CG1 . ILE A  1 157 ? -57.970  26.542  -60.780  1.00 30.60  ? 157 ILE A CG1 1 
ATOM   1272  C CG2 . ILE A  1 157 ? -60.139  27.709  -61.068  1.00 30.34  ? 157 ILE A CG2 1 
ATOM   1273  C CD1 . ILE A  1 157 ? -58.179  25.438  -61.792  1.00 29.84  ? 157 ILE A CD1 1 
ATOM   1274  N N   . HIS A  1 158 ? -61.075  27.805  -57.569  1.00 36.02  ? 158 HIS A N   1 
ATOM   1275  C CA  . HIS A  1 158 ? -62.267  28.423  -57.004  1.00 37.72  ? 158 HIS A CA  1 
ATOM   1276  C C   . HIS A  1 158 ? -61.919  29.686  -56.192  1.00 41.13  ? 158 HIS A C   1 
ATOM   1277  O O   . HIS A  1 158 ? -62.661  30.664  -56.256  1.00 41.79  ? 158 HIS A O   1 
ATOM   1278  C CB  . HIS A  1 158 ? -63.077  27.439  -56.153  1.00 36.58  ? 158 HIS A CB  1 
ATOM   1279  C CG  . HIS A  1 158 ? -63.784  26.357  -56.889  1.00 35.05  ? 158 HIS A CG  1 
ATOM   1280  N ND1 . HIS A  1 158 ? -64.120  26.420  -58.224  1.00 34.00  ? 158 HIS A ND1 1 
ATOM   1281  C CD2 . HIS A  1 158 ? -64.234  25.173  -56.443  1.00 33.00  ? 158 HIS A CD2 1 
ATOM   1282  C CE1 . HIS A  1 158 ? -64.739  25.295  -58.560  1.00 31.76  ? 158 HIS A CE1 1 
ATOM   1283  N NE2 . HIS A  1 158 ? -64.814  24.547  -57.491  1.00 31.70  ? 158 HIS A NE2 1 
ATOM   1284  N N   . LYS A  1 159 ? -60.822  29.667  -55.413  1.00 42.79  ? 159 LYS A N   1 
ATOM   1285  C CA  . LYS A  1 159 ? -60.398  30.835  -54.658  1.00 46.87  ? 159 LYS A CA  1 
ATOM   1286  C C   . LYS A  1 159 ? -59.631  31.843  -55.525  1.00 43.13  ? 159 LYS A C   1 
ATOM   1287  O O   . LYS A  1 159 ? -59.861  33.035  -55.407  1.00 41.72  ? 159 LYS A O   1 
ATOM   1288  C CB  . LYS A  1 159 ? -59.568  30.441  -53.434  1.00 55.66  ? 159 LYS A CB  1 
ATOM   1289  C CG  . LYS A  1 159 ? -60.416  29.854  -52.323  1.00 67.69  ? 159 LYS A CG  1 
ATOM   1290  C CD  . LYS A  1 159 ? -59.658  29.362  -51.090  1.00 75.23  ? 159 LYS A CD  1 
ATOM   1291  C CE  . LYS A  1 159 ? -60.482  28.364  -50.321  1.00 76.89  ? 159 LYS A CE  1 
ATOM   1292  N NZ  . LYS A  1 159 ? -59.733  27.119  -50.105  1.00 76.81  ? 159 LYS A NZ  1 
ATOM   1293  N N   . GLY A  1 160 ? -58.728  31.383  -56.400  1.00 41.43  ? 160 GLY A N   1 
ATOM   1294  C CA  . GLY A  1 160 ? -57.845  32.275  -57.149  1.00 40.15  ? 160 GLY A CA  1 
ATOM   1295  C C   . GLY A  1 160 ? -58.527  32.990  -58.328  1.00 38.91  ? 160 GLY A C   1 
ATOM   1296  O O   . GLY A  1 160 ? -58.134  34.099  -58.686  1.00 43.62  ? 160 GLY A O   1 
ATOM   1297  N N   . HIS A  1 161 ? -59.523  32.351  -58.959  1.00 34.12  ? 161 HIS A N   1 
ATOM   1298  C CA  . HIS A  1 161 ? -60.276  32.945  -60.045  1.00 31.80  ? 161 HIS A CA  1 
ATOM   1299  C C   . HIS A  1 161 ? -61.746  32.581  -59.873  1.00 32.18  ? 161 HIS A C   1 
ATOM   1300  O O   . HIS A  1 161 ? -62.232  31.624  -60.471  1.00 30.23  ? 161 HIS A O   1 
ATOM   1301  C CB  . HIS A  1 161 ? -59.741  32.516  -61.413  1.00 30.30  ? 161 HIS A CB  1 
ATOM   1302  C CG  . HIS A  1 161 ? -60.307  33.348  -62.514  1.00 29.62  ? 161 HIS A CG  1 
ATOM   1303  N ND1 . HIS A  1 161 ? -59.915  33.217  -63.834  1.00 28.38  ? 161 HIS A ND1 1 
ATOM   1304  C CD2 . HIS A  1 161 ? -61.245  34.318  -62.473  1.00 29.12  ? 161 HIS A CD2 1 
ATOM   1305  C CE1 . HIS A  1 161 ? -60.616  34.066  -64.568  1.00 29.11  ? 161 HIS A CE1 1 
ATOM   1306  N NE2 . HIS A  1 161 ? -61.441  34.746  -63.760  1.00 29.84  ? 161 HIS A NE2 1 
ATOM   1307  N N   . PRO A  1 162 ? -62.486  33.330  -59.023  1.00 34.56  ? 162 PRO A N   1 
ATOM   1308  C CA  . PRO A  1 162 ? -63.815  32.894  -58.580  1.00 34.93  ? 162 PRO A CA  1 
ATOM   1309  C C   . PRO A  1 162 ? -64.849  32.922  -59.696  1.00 34.56  ? 162 PRO A C   1 
ATOM   1310  O O   . PRO A  1 162 ? -64.808  33.770  -60.588  1.00 36.60  ? 162 PRO A O   1 
ATOM   1311  C CB  . PRO A  1 162 ? -64.180  33.846  -57.435  1.00 35.63  ? 162 PRO A CB  1 
ATOM   1312  C CG  . PRO A  1 162 ? -62.869  34.552  -57.112  1.00 35.95  ? 162 PRO A CG  1 
ATOM   1313  C CD  . PRO A  1 162 ? -62.057  34.591  -58.384  1.00 34.33  ? 162 PRO A CD  1 
ATOM   1314  N N   . GLY A  1 163 ? -65.766  31.967  -59.616  1.00 33.89  ? 163 GLY A N   1 
ATOM   1315  C CA  . GLY A  1 163 ? -66.940  31.936  -60.457  1.00 32.96  ? 163 GLY A CA  1 
ATOM   1316  C C   . GLY A  1 163 ? -66.646  31.248  -61.773  1.00 32.47  ? 163 GLY A C   1 
ATOM   1317  O O   . GLY A  1 163 ? -67.523  31.251  -62.614  1.00 35.62  ? 163 GLY A O   1 
ATOM   1318  N N   . ILE A  1 164 ? -65.434  30.706  -61.967  1.00 29.54  ? 164 ILE A N   1 
ATOM   1319  C CA  . ILE A  1 164 ? -65.105  30.080  -63.238  1.00 28.67  ? 164 ILE A CA  1 
ATOM   1320  C C   . ILE A  1 164 ? -65.231  28.574  -63.072  1.00 30.48  ? 164 ILE A C   1 
ATOM   1321  O O   . ILE A  1 164 ? -64.588  27.990  -62.197  1.00 32.18  ? 164 ILE A O   1 
ATOM   1322  C CB  . ILE A  1 164 ? -63.677  30.385  -63.709  1.00 28.79  ? 164 ILE A CB  1 
ATOM   1323  C CG1 . ILE A  1 164 ? -63.286  31.890  -63.675  1.00 30.39  ? 164 ILE A CG1 1 
ATOM   1324  C CG2 . ILE A  1 164 ? -63.445  29.761  -65.075  1.00 27.40  ? 164 ILE A CG2 1 
ATOM   1325  C CD1 . ILE A  1 164 ? -64.168  32.815  -64.498  1.00 30.86  ? 164 ILE A CD1 1 
ATOM   1326  N N   . PRO A  1 165 ? -66.051  27.881  -63.886  1.00 30.33  ? 165 PRO A N   1 
ATOM   1327  C CA  . PRO A  1 165 ? -66.105  26.431  -63.795  1.00 29.87  ? 165 PRO A CA  1 
ATOM   1328  C C   . PRO A  1 165 ? -64.776  25.718  -64.079  1.00 30.30  ? 165 PRO A C   1 
ATOM   1329  O O   . PRO A  1 165 ? -63.969  26.172  -64.894  1.00 29.86  ? 165 PRO A O   1 
ATOM   1330  C CB  . PRO A  1 165 ? -67.188  26.139  -64.844  1.00 29.63  ? 165 PRO A CB  1 
ATOM   1331  C CG  . PRO A  1 165 ? -68.085  27.325  -64.807  1.00 30.38  ? 165 PRO A CG  1 
ATOM   1332  C CD  . PRO A  1 165 ? -67.060  28.456  -64.796  1.00 30.28  ? 165 PRO A CD  1 
ATOM   1333  N N   . VAL A  1 166 ? -64.582  24.581  -63.393  1.00 30.91  ? 166 VAL A N   1 
ATOM   1334  C CA  . VAL A  1 166 ? -63.411  23.718  -63.524  1.00 30.57  ? 166 VAL A CA  1 
ATOM   1335  C C   . VAL A  1 166 ? -63.863  22.298  -63.865  1.00 29.80  ? 166 VAL A C   1 
ATOM   1336  O O   . VAL A  1 166 ? -64.795  21.762  -63.241  1.00 30.32  ? 166 VAL A O   1 
ATOM   1337  C CB  . VAL A  1 166 ? -62.649  23.746  -62.185  1.00 31.53  ? 166 VAL A CB  1 
ATOM   1338  C CG1 . VAL A  1 166 ? -61.370  22.906  -62.228  1.00 31.78  ? 166 VAL A CG1 1 
ATOM   1339  C CG2 . VAL A  1 166 ? -62.348  25.182  -61.751  1.00 32.12  ? 166 VAL A CG2 1 
ATOM   1340  N N   . THR A  1 167 ? -63.218  21.692  -64.862  1.00 28.33  ? 167 THR A N   1 
ATOM   1341  C CA  . THR A  1 167 ? -63.441  20.280  -65.154  1.00 27.72  ? 167 THR A CA  1 
ATOM   1342  C C   . THR A  1 167 ? -62.133  19.693  -65.684  1.00 26.90  ? 167 THR A C   1 
ATOM   1343  O O   . THR A  1 167 ? -61.073  20.205  -65.344  1.00 25.01  ? 167 THR A O   1 
ATOM   1344  C CB  . THR A  1 167 ? -64.643  20.110  -66.081  1.00 26.46  ? 167 THR A CB  1 
ATOM   1345  O OG1 . THR A  1 167 ? -64.878  18.717  -66.263  1.00 25.85  ? 167 THR A OG1 1 
ATOM   1346  C CG2 . THR A  1 167 ? -64.454  20.726  -67.451  1.00 26.40  ? 167 THR A CG2 1 
ATOM   1347  N N   . LEU A  1 168 ? -62.191  18.597  -66.442  1.00 26.73  ? 168 LEU A N   1 
ATOM   1348  C CA  . LEU A  1 168 ? -60.955  18.004  -66.934  1.00 28.15  ? 168 LEU A CA  1 
ATOM   1349  C C   . LEU A  1 168 ? -61.149  17.473  -68.356  1.00 27.90  ? 168 LEU A C   1 
ATOM   1350  O O   . LEU A  1 168 ? -62.261  17.372  -68.847  1.00 28.32  ? 168 LEU A O   1 
ATOM   1351  C CB  . LEU A  1 168 ? -60.455  16.917  -65.968  1.00 29.30  ? 168 LEU A CB  1 
ATOM   1352  C CG  . LEU A  1 168 ? -60.927  15.470  -66.210  1.00 30.24  ? 168 LEU A CG  1 
ATOM   1353  C CD1 . LEU A  1 168 ? -60.290  14.454  -65.243  1.00 30.73  ? 168 LEU A CD1 1 
ATOM   1354  C CD2 . LEU A  1 168 ? -62.435  15.356  -66.085  1.00 30.62  ? 168 LEU A CD2 1 
ATOM   1355  N N   . SER A  1 169 ? -60.030  17.128  -68.998  1.00 28.44  ? 169 SER A N   1 
ATOM   1356  C CA  . SER A  1 169 ? -59.960  16.524  -70.318  1.00 26.29  ? 169 SER A CA  1 
ATOM   1357  C C   . SER A  1 169 ? -59.791  15.013  -70.140  1.00 29.25  ? 169 SER A C   1 
ATOM   1358  O O   . SER A  1 169 ? -58.750  14.548  -69.697  1.00 31.56  ? 169 SER A O   1 
ATOM   1359  C CB  . SER A  1 169 ? -58.811  17.196  -71.036  1.00 25.79  ? 169 SER A CB  1 
ATOM   1360  O OG  . SER A  1 169 ? -58.332  16.557  -72.211  1.00 24.89  ? 169 SER A OG  1 
ATOM   1361  N N   . ALA A  1 170 ? -60.841  14.231  -70.403  1.00 29.88  ? 170 ALA A N   1 
ATOM   1362  C CA  . ALA A  1 170 ? -60.790  12.807  -70.098  1.00 28.96  ? 170 ALA A CA  1 
ATOM   1363  C C   . ALA A  1 170 ? -61.483  12.038  -71.203  1.00 26.71  ? 170 ALA A C   1 
ATOM   1364  O O   . ALA A  1 170 ? -62.600  12.344  -71.558  1.00 26.74  ? 170 ALA A O   1 
ATOM   1365  C CB  . ALA A  1 170 ? -61.414  12.503  -68.755  1.00 29.74  ? 170 ALA A CB  1 
ATOM   1366  N N   . ASN A  1 171 ? -60.761  11.100  -71.805  1.00 27.12  ? 171 ASN A N   1 
ATOM   1367  C CA  . ASN A  1 171 ? -61.296  10.375  -72.931  1.00 29.50  ? 171 ASN A CA  1 
ATOM   1368  C C   . ASN A  1 171 ? -62.388  9.419   -72.423  1.00 28.40  ? 171 ASN A C   1 
ATOM   1369  O O   . ASN A  1 171 ? -62.188  8.695   -71.452  1.00 30.29  ? 171 ASN A O   1 
ATOM   1370  C CB  . ASN A  1 171 ? -60.188  9.672   -73.704  1.00 30.68  ? 171 ASN A CB  1 
ATOM   1371  C CG  . ASN A  1 171 ? -60.730  8.931   -74.906  1.00 32.06  ? 171 ASN A CG  1 
ATOM   1372  O OD1 . ASN A  1 171 ? -61.555  8.024   -74.757  1.00 32.97  ? 171 ASN A OD1 1 
ATOM   1373  N ND2 . ASN A  1 171 ? -60.309  9.318   -76.097  1.00 31.64  ? 171 ASN A ND2 1 
ATOM   1374  N N   . ALA A  1 172 ? -63.532  9.444   -73.104  1.00 26.38  ? 172 ALA A N   1 
ATOM   1375  C CA  . ALA A  1 172 ? -64.706  8.663   -72.743  1.00 26.52  ? 172 ALA A CA  1 
ATOM   1376  C C   . ALA A  1 172 ? -64.469  7.156   -72.901  1.00 26.11  ? 172 ALA A C   1 
ATOM   1377  O O   . ALA A  1 172 ? -65.120  6.357   -72.244  1.00 29.27  ? 172 ALA A O   1 
ATOM   1378  C CB  . ALA A  1 172 ? -65.888  9.132   -73.583  1.00 25.03  ? 172 ALA A CB  1 
ATOM   1379  N N   . MET A  1 173 ? -63.577  6.751   -73.800  1.00 26.66  ? 173 MET A N   1 
ATOM   1380  C CA  . MET A  1 173 ? -63.346  5.331   -74.040  1.00 26.44  ? 173 MET A CA  1 
ATOM   1381  C C   . MET A  1 173 ? -62.533  4.695   -72.917  1.00 26.68  ? 173 MET A C   1 
ATOM   1382  O O   . MET A  1 173 ? -62.728  3.503   -72.693  1.00 26.35  ? 173 MET A O   1 
ATOM   1383  C CB  . MET A  1 173 ? -62.660  5.098   -75.384  1.00 25.51  ? 173 MET A CB  1 
ATOM   1384  C CG  . MET A  1 173 ? -63.556  5.363   -76.559  1.00 26.10  ? 173 MET A CG  1 
ATOM   1385  S SD  . MET A  1 173 ? -64.948  4.214   -76.588  1.00 29.18  ? 173 MET A SD  1 
ATOM   1386  C CE  . MET A  1 173 ? -64.130  2.786   -77.304  1.00 25.71  ? 173 MET A CE  1 
ATOM   1387  N N   . ILE A  1 174 ? -61.718  5.487   -72.161  1.00 27.23  ? 174 ILE A N   1 
ATOM   1388  C CA  . ILE A  1 174 ? -60.862  4.933   -71.111  1.00 26.19  ? 174 ILE A CA  1 
ATOM   1389  C C   . ILE A  1 174 ? -61.252  5.393   -69.710  1.00 27.45  ? 174 ILE A C   1 
ATOM   1390  O O   . ILE A  1 174 ? -60.810  4.767   -68.733  1.00 26.86  ? 174 ILE A O   1 
ATOM   1391  C CB  . ILE A  1 174 ? -59.383  5.248   -71.369  1.00 25.88  ? 174 ILE A CB  1 
ATOM   1392  C CG1 . ILE A  1 174 ? -59.157  6.743   -71.523  1.00 25.23  ? 174 ILE A CG1 1 
ATOM   1393  C CG2 . ILE A  1 174 ? -58.861  4.434   -72.554  1.00 26.03  ? 174 ILE A CG2 1 
ATOM   1394  C CD1 . ILE A  1 174 ? -57.730  7.160   -71.285  1.00 25.88  ? 174 ILE A CD1 1 
ATOM   1395  N N   . SER A  1 175 ? -62.017  6.494   -69.602  1.00 28.59  ? 175 SER A N   1 
ATOM   1396  C CA  . SER A  1 175 ? -62.363  7.059   -68.296  1.00 29.03  ? 175 SER A CA  1 
ATOM   1397  C C   . SER A  1 175 ? -63.881  7.142   -68.097  1.00 28.59  ? 175 SER A C   1 
ATOM   1398  O O   . SER A  1 175 ? -64.397  7.876   -67.257  1.00 28.82  ? 175 SER A O   1 
ATOM   1399  C CB  . SER A  1 175 ? -61.682  8.394   -68.102  1.00 30.45  ? 175 SER A CB  1 
ATOM   1400  O OG  . SER A  1 175 ? -60.262  8.297   -68.221  1.00 30.02  ? 175 SER A OG  1 
ATOM   1401  N N   . ASP A  1 176 ? -64.610  6.268   -68.780  1.00 28.68  ? 176 ASP A N   1 
ATOM   1402  C CA  . ASP A  1 176 ? -66.019  6.007   -68.488  1.00 28.18  ? 176 ASP A CA  1 
ATOM   1403  C C   . ASP A  1 176 ? -66.313  5.721   -67.016  1.00 27.12  ? 176 ASP A C   1 
ATOM   1404  O O   . ASP A  1 176 ? -67.383  6.103   -66.535  1.00 27.33  ? 176 ASP A O   1 
ATOM   1405  C CB  . ASP A  1 176 ? -66.526  4.846   -69.326  1.00 29.17  ? 176 ASP A CB  1 
ATOM   1406  C CG  . ASP A  1 176 ? -65.637  3.605   -69.343  1.00 29.35  ? 176 ASP A CG  1 
ATOM   1407  O OD1 . ASP A  1 176 ? -64.539  3.672   -68.760  1.00 30.04  ? 176 ASP A OD1 1 
ATOM   1408  O OD2 . ASP A  1 176 ? -66.040  2.595   -69.986  1.00 29.38  ? 176 ASP A OD2 1 
ATOM   1409  N N   . TYR A  1 177 ? -65.409  5.021   -66.314  1.00 26.59  ? 177 TYR A N   1 
ATOM   1410  C CA  . TYR A  1 177 ? -65.620  4.608   -64.929  1.00 26.97  ? 177 TYR A CA  1 
ATOM   1411  C C   . TYR A  1 177 ? -65.446  5.762   -63.925  1.00 28.88  ? 177 TYR A C   1 
ATOM   1412  O O   . TYR A  1 177 ? -65.887  5.639   -62.782  1.00 30.56  ? 177 TYR A O   1 
ATOM   1413  C CB  . TYR A  1 177 ? -64.619  3.510   -64.553  1.00 27.76  ? 177 TYR A CB  1 
ATOM   1414  C CG  . TYR A  1 177 ? -63.186  4.018   -64.541  1.00 27.52  ? 177 TYR A CG  1 
ATOM   1415  C CD1 . TYR A  1 177 ? -62.636  4.556   -63.397  1.00 28.71  ? 177 TYR A CD1 1 
ATOM   1416  C CD2 . TYR A  1 177 ? -62.404  4.010   -65.678  1.00 28.43  ? 177 TYR A CD2 1 
ATOM   1417  C CE1 . TYR A  1 177 ? -61.348  5.073   -63.382  1.00 30.34  ? 177 TYR A CE1 1 
ATOM   1418  C CE2 . TYR A  1 177 ? -61.112  4.517   -65.681  1.00 28.71  ? 177 TYR A CE2 1 
ATOM   1419  C CZ  . TYR A  1 177 ? -60.585  5.071   -64.533  1.00 29.30  ? 177 TYR A CZ  1 
ATOM   1420  O OH  . TYR A  1 177 ? -59.326  5.608   -64.514  1.00 28.92  ? 177 TYR A OH  1 
ATOM   1421  N N   . MET A  1 178 ? -64.809  6.875   -64.315  1.00 27.76  ? 178 MET A N   1 
ATOM   1422  C CA  . MET A  1 178 ? -64.326  7.876   -63.374  1.00 31.03  ? 178 MET A CA  1 
ATOM   1423  C C   . MET A  1 178 ? -65.462  8.727   -62.798  1.00 30.98  ? 178 MET A C   1 
ATOM   1424  O O   . MET A  1 178 ? -66.326  9.172   -63.543  1.00 33.48  ? 178 MET A O   1 
ATOM   1425  C CB  . MET A  1 178 ? -63.370  8.833   -64.107  1.00 31.97  ? 178 MET A CB  1 
ATOM   1426  C CG  . MET A  1 178 ? -62.863  10.003  -63.306  1.00 32.30  ? 178 MET A CG  1 
ATOM   1427  S SD  . MET A  1 178 ? -61.521  10.873  -64.152  1.00 34.24  ? 178 MET A SD  1 
ATOM   1428  C CE  . MET A  1 178 ? -60.190  9.677   -64.349  1.00 32.69  ? 178 MET A CE  1 
ATOM   1429  N N   . ASP A  1 179 ? -65.412  8.992   -61.491  1.00 30.50  ? 179 ASP A N   1 
ATOM   1430  C CA  . ASP A  1 179 ? -66.288  9.963   -60.871  1.00 35.39  ? 179 ASP A CA  1 
ATOM   1431  C C   . ASP A  1 179 ? -65.915  11.375  -61.336  1.00 34.09  ? 179 ASP A C   1 
ATOM   1432  O O   . ASP A  1 179 ? -64.771  11.774  -61.154  1.00 32.70  ? 179 ASP A O   1 
ATOM   1433  C CB  . ASP A  1 179 ? -66.194  9.962   -59.356  1.00 37.63  ? 179 ASP A CB  1 
ATOM   1434  C CG  . ASP A  1 179 ? -67.318  10.738  -58.676  1.00 41.73  ? 179 ASP A CG  1 
ATOM   1435  O OD1 . ASP A  1 179 ? -68.421  10.169  -58.467  1.00 41.68  ? 179 ASP A OD1 1 
ATOM   1436  O OD2 . ASP A  1 179 ? -67.093  11.917  -58.389  1.00 46.90  ? 179 ASP A OD2 1 
ATOM   1437  N N   . GLU A  1 180 ? -66.864  12.097  -61.952  1.00 32.01  ? 180 GLU A N   1 
ATOM   1438  C CA  . GLU A  1 180 ? -66.612  13.472  -62.363  1.00 33.59  ? 180 GLU A CA  1 
ATOM   1439  C C   . GLU A  1 180 ? -67.393  14.490  -61.516  1.00 33.99  ? 180 GLU A C   1 
ATOM   1440  O O   . GLU A  1 180 ? -67.481  15.670  -61.874  1.00 34.12  ? 180 GLU A O   1 
ATOM   1441  C CB  . GLU A  1 180 ? -66.927  13.685  -63.846  1.00 33.44  ? 180 GLU A CB  1 
ATOM   1442  C CG  . GLU A  1 180 ? -65.862  13.172  -64.814  1.00 31.75  ? 180 GLU A CG  1 
ATOM   1443  C CD  . GLU A  1 180 ? -66.077  13.766  -66.190  1.00 33.95  ? 180 GLU A CD  1 
ATOM   1444  O OE1 . GLU A  1 180 ? -67.003  14.613  -66.293  1.00 34.16  ? 180 GLU A OE1 1 
ATOM   1445  O OE2 . GLU A  1 180 ? -65.340  13.405  -67.145  1.00 32.59  ? 180 GLU A OE2 1 
ATOM   1446  N N   . SER A  1 181 ? -67.897  14.056  -60.359  1.00 33.72  ? 181 SER A N   1 
ATOM   1447  C CA  . SER A  1 181 ? -68.872  14.835  -59.625  1.00 34.37  ? 181 SER A CA  1 
ATOM   1448  C C   . SER A  1 181 ? -68.166  15.903  -58.801  1.00 34.36  ? 181 SER A C   1 
ATOM   1449  O O   . SER A  1 181 ? -68.814  16.835  -58.357  1.00 33.30  ? 181 SER A O   1 
ATOM   1450  C CB  . SER A  1 181 ? -69.740  13.982  -58.764  1.00 34.25  ? 181 SER A CB  1 
ATOM   1451  O OG  . SER A  1 181 ? -68.941  13.445  -57.729  1.00 35.97  ? 181 SER A OG  1 
ATOM   1452  N N   . ILE A  1 182 ? -66.850  15.773  -58.607  1.00 35.86  ? 182 ILE A N   1 
ATOM   1453  C CA  . ILE A  1 182 ? -66.074  16.794  -57.900  1.00 34.51  ? 182 ILE A CA  1 
ATOM   1454  C C   . ILE A  1 182 ? -65.892  18.033  -58.771  1.00 33.84  ? 182 ILE A C   1 
ATOM   1455  O O   . ILE A  1 182 ? -65.618  19.108  -58.248  1.00 34.98  ? 182 ILE A O   1 
ATOM   1456  C CB  . ILE A  1 182 ? -64.722  16.228  -57.447  1.00 34.44  ? 182 ILE A CB  1 
ATOM   1457  C CG1 . ILE A  1 182 ? -63.850  15.874  -58.664  1.00 34.45  ? 182 ILE A CG1 1 
ATOM   1458  C CG2 . ILE A  1 182 ? -64.931  15.038  -56.492  1.00 35.13  ? 182 ILE A CG2 1 
ATOM   1459  C CD1 . ILE A  1 182 ? -62.639  15.015  -58.342  1.00 36.04  ? 182 ILE A CD1 1 
ATOM   1460  N N   . PHE A  1 183 ? -66.003  17.875  -60.096  1.00 33.59  ? 183 PHE A N   1 
ATOM   1461  C CA  . PHE A  1 183 ? -65.831  18.989  -61.019  1.00 32.51  ? 183 PHE A CA  1 
ATOM   1462  C C   . PHE A  1 183 ? -67.145  19.752  -61.171  1.00 31.92  ? 183 PHE A C   1 
ATOM   1463  O O   . PHE A  1 183 ? -68.179  19.275  -60.738  1.00 30.86  ? 183 PHE A O   1 
ATOM   1464  C CB  . PHE A  1 183 ? -65.364  18.443  -62.365  1.00 31.88  ? 183 PHE A CB  1 
ATOM   1465  C CG  . PHE A  1 183 ? -64.065  17.668  -62.259  1.00 32.02  ? 183 PHE A CG  1 
ATOM   1466  C CD1 . PHE A  1 183 ? -62.850  18.330  -62.134  1.00 31.92  ? 183 PHE A CD1 1 
ATOM   1467  C CD2 . PHE A  1 183 ? -64.065  16.271  -62.294  1.00 33.82  ? 183 PHE A CD2 1 
ATOM   1468  C CE1 . PHE A  1 183 ? -61.659  17.621  -62.033  1.00 31.47  ? 183 PHE A CE1 1 
ATOM   1469  C CE2 . PHE A  1 183 ? -62.872  15.562  -62.207  1.00 33.76  ? 183 PHE A CE2 1 
ATOM   1470  C CZ  . PHE A  1 183 ? -61.670  16.240  -62.069  1.00 32.45  ? 183 PHE A CZ  1 
ATOM   1471  N N   . ASP A  1 184 ? -67.097  20.941  -61.790  1.00 32.48  ? 184 ASP A N   1 
ATOM   1472  C CA  . ASP A  1 184 ? -68.268  21.808  -61.906  1.00 32.32  ? 184 ASP A CA  1 
ATOM   1473  C C   . ASP A  1 184 ? -69.095  21.456  -63.143  1.00 32.48  ? 184 ASP A C   1 
ATOM   1474  O O   . ASP A  1 184 ? -70.261  21.826  -63.240  1.00 33.02  ? 184 ASP A O   1 
ATOM   1475  C CB  . ASP A  1 184 ? -67.892  23.280  -61.923  1.00 30.19  ? 184 ASP A CB  1 
ATOM   1476  C CG  . ASP A  1 184 ? -67.067  23.683  -60.715  1.00 31.67  ? 184 ASP A CG  1 
ATOM   1477  O OD1 . ASP A  1 184 ? -67.483  23.267  -59.621  1.00 30.88  ? 184 ASP A OD1 1 
ATOM   1478  O OD2 . ASP A  1 184 ? -65.984  24.348  -60.890  1.00 31.80  ? 184 ASP A OD2 1 
ATOM   1479  N N   . VAL A  1 185 ? -68.434  20.861  -64.138  1.00 32.28  ? 185 VAL A N   1 
ATOM   1480  C CA  . VAL A  1 185 ? -69.123  20.437  -65.329  1.00 32.36  ? 185 VAL A CA  1 
ATOM   1481  C C   . VAL A  1 185 ? -68.524  19.098  -65.749  1.00 29.99  ? 185 VAL A C   1 
ATOM   1482  O O   . VAL A  1 185 ? -67.408  18.743  -65.377  1.00 28.27  ? 185 VAL A O   1 
ATOM   1483  C CB  . VAL A  1 185 ? -69.142  21.469  -66.479  1.00 34.51  ? 185 VAL A CB  1 
ATOM   1484  C CG1 . VAL A  1 185 ? -69.297  22.925  -66.005  1.00 34.75  ? 185 VAL A CG1 1 
ATOM   1485  C CG2 . VAL A  1 185 ? -67.940  21.330  -67.370  1.00 35.59  ? 185 VAL A CG2 1 
ATOM   1486  N N   . TYR A  1 186 ? -69.345  18.330  -66.463  1.00 30.46  ? 186 TYR A N   1 
ATOM   1487  C CA  . TYR A  1 186 ? -68.967  17.004  -66.918  1.00 30.02  ? 186 TYR A CA  1 
ATOM   1488  C C   . TYR A  1 186 ? -68.413  17.226  -68.307  1.00 29.49  ? 186 TYR A C   1 
ATOM   1489  O O   . TYR A  1 186 ? -68.902  18.108  -69.003  1.00 33.54  ? 186 TYR A O   1 
ATOM   1490  C CB  . TYR A  1 186 ? -70.112  15.983  -66.928  1.00 29.80  ? 186 TYR A CB  1 
ATOM   1491  C CG  . TYR A  1 186 ? -70.820  15.747  -65.601  1.00 28.93  ? 186 TYR A CG  1 
ATOM   1492  C CD1 . TYR A  1 186 ? -70.108  15.364  -64.479  1.00 30.27  ? 186 TYR A CD1 1 
ATOM   1493  C CD2 . TYR A  1 186 ? -72.197  15.943  -65.468  1.00 28.56  ? 186 TYR A CD2 1 
ATOM   1494  C CE1 . TYR A  1 186 ? -70.750  15.164  -63.261  1.00 32.56  ? 186 TYR A CE1 1 
ATOM   1495  C CE2 . TYR A  1 186 ? -72.854  15.736  -64.264  1.00 28.76  ? 186 TYR A CE2 1 
ATOM   1496  C CZ  . TYR A  1 186 ? -72.128  15.337  -63.155  1.00 30.37  ? 186 TYR A CZ  1 
ATOM   1497  O OH  . TYR A  1 186 ? -72.728  15.158  -61.950  1.00 29.79  ? 186 TYR A OH  1 
ATOM   1498  N N   . ALA A  1 187 ? -67.386  16.458  -68.657  1.00 28.23  ? 187 ALA A N   1 
ATOM   1499  C CA  . ALA A  1 187 ? -66.672  16.631  -69.904  1.00 28.43  ? 187 ALA A CA  1 
ATOM   1500  C C   . ALA A  1 187 ? -66.002  15.312  -70.328  1.00 28.47  ? 187 ALA A C   1 
ATOM   1501  O O   . ALA A  1 187 ? -65.427  14.601  -69.498  1.00 29.81  ? 187 ALA A O   1 
ATOM   1502  C CB  . ALA A  1 187 ? -65.643  17.729  -69.710  1.00 28.61  ? 187 ALA A CB  1 
ATOM   1503  N N   . TYR A  1 188 ? -66.021  15.019  -71.630  1.00 26.17  ? 188 TYR A N   1 
ATOM   1504  C CA  . TYR A  1 188 ? -65.204  13.952  -72.172  1.00 27.48  ? 188 TYR A CA  1 
ATOM   1505  C C   . TYR A  1 188 ? -64.679  14.363  -73.544  1.00 28.13  ? 188 TYR A C   1 
ATOM   1506  O O   . TYR A  1 188 ? -65.349  15.086  -74.251  1.00 30.56  ? 188 TYR A O   1 
ATOM   1507  C CB  . TYR A  1 188 ? -65.933  12.609  -72.347  1.00 26.79  ? 188 TYR A CB  1 
ATOM   1508  C CG  . TYR A  1 188 ? -66.531  12.029  -71.077  1.00 26.55  ? 188 TYR A CG  1 
ATOM   1509  C CD1 . TYR A  1 188 ? -65.723  11.398  -70.133  1.00 26.48  ? 188 TYR A CD1 1 
ATOM   1510  C CD2 . TYR A  1 188 ? -67.900  12.128  -70.812  1.00 26.57  ? 188 TYR A CD2 1 
ATOM   1511  C CE1 . TYR A  1 188 ? -66.263  10.852  -68.974  1.00 27.64  ? 188 TYR A CE1 1 
ATOM   1512  C CE2 . TYR A  1 188 ? -68.450  11.581  -69.654  1.00 27.62  ? 188 TYR A CE2 1 
ATOM   1513  C CZ  . TYR A  1 188 ? -67.628  10.954  -68.734  1.00 27.79  ? 188 TYR A CZ  1 
ATOM   1514  O OH  . TYR A  1 188 ? -68.152  10.422  -67.599  1.00 28.83  ? 188 TYR A OH  1 
ATOM   1515  N N   . ASN A  1 189 ? -63.480  13.887  -73.888  1.00 28.31  ? 189 ASN A N   1 
ATOM   1516  C CA  . ASN A  1 189 ? -63.056  13.731  -75.272  1.00 30.00  ? 189 ASN A CA  1 
ATOM   1517  C C   . ASN A  1 189 ? -63.789  12.524  -75.869  1.00 27.56  ? 189 ASN A C   1 
ATOM   1518  O O   . ASN A  1 189 ? -63.716  11.420  -75.334  1.00 28.02  ? 189 ASN A O   1 
ATOM   1519  C CB  . ASN A  1 189 ? -61.536  13.549  -75.406  1.00 28.20  ? 189 ASN A CB  1 
ATOM   1520  C CG  . ASN A  1 189 ? -60.771  14.639  -74.686  1.00 29.08  ? 189 ASN A CG  1 
ATOM   1521  O OD1 . ASN A  1 189 ? -61.168  15.805  -74.720  1.00 30.46  ? 189 ASN A OD1 1 
ATOM   1522  N ND2 . ASN A  1 189 ? -59.703  14.293  -73.984  1.00 30.53  ? 189 ASN A ND2 1 
ATOM   1523  N N   . CYS A  1 190 ? -64.443  12.731  -77.009  1.00 25.98  ? 190 CYS A N   1 
ATOM   1524  C CA  . CYS A  1 190 ? -65.407  11.771  -77.521  1.00 25.34  ? 190 CYS A CA  1 
ATOM   1525  C C   . CYS A  1 190 ? -65.062  11.449  -78.966  1.00 24.15  ? 190 CYS A C   1 
ATOM   1526  O O   . CYS A  1 190 ? -65.090  12.334  -79.806  1.00 25.11  ? 190 CYS A O   1 
ATOM   1527  C CB  . CYS A  1 190 ? -66.811  12.360  -77.465  1.00 25.74  ? 190 CYS A CB  1 
ATOM   1528  S SG  . CYS A  1 190 ? -67.359  12.760  -75.791  1.00 28.04  ? 190 CYS A SG  1 
ATOM   1529  N N   . TYR A  1 191 ? -64.689  10.202  -79.242  1.00 24.01  ? 191 TYR A N   1 
ATOM   1530  C CA  . TYR A  1 191 ? -64.355  9.784   -80.592  1.00 24.28  ? 191 TYR A CA  1 
ATOM   1531  C C   . TYR A  1 191 ? -65.190  8.582   -81.015  1.00 25.32  ? 191 TYR A C   1 
ATOM   1532  O O   . TYR A  1 191 ? -65.427  7.654   -80.221  1.00 25.86  ? 191 TYR A O   1 
ATOM   1533  C CB  . TYR A  1 191 ? -62.876  9.420   -80.682  1.00 25.47  ? 191 TYR A CB  1 
ATOM   1534  C CG  . TYR A  1 191 ? -61.994  10.646  -80.637  1.00 24.20  ? 191 TYR A CG  1 
ATOM   1535  C CD1 . TYR A  1 191 ? -61.854  11.427  -81.780  1.00 25.53  ? 191 TYR A CD1 1 
ATOM   1536  C CD2 . TYR A  1 191 ? -61.364  11.045  -79.466  1.00 22.45  ? 191 TYR A CD2 1 
ATOM   1537  C CE1 . TYR A  1 191 ? -61.089  12.582  -81.778  1.00 24.72  ? 191 TYR A CE1 1 
ATOM   1538  C CE2 . TYR A  1 191 ? -60.621  12.213  -79.457  1.00 24.52  ? 191 TYR A CE2 1 
ATOM   1539  C CZ  . TYR A  1 191 ? -60.482  12.979  -80.607  1.00 24.48  ? 191 TYR A CZ  1 
ATOM   1540  O OH  . TYR A  1 191 ? -59.727  14.119  -80.647  1.00 26.75  ? 191 TYR A OH  1 
ATOM   1541  N N   . ASP A  1 192 ? -65.592  8.607   -82.289  1.00 24.72  ? 192 ASP A N   1 
ATOM   1542  C CA  . ASP A  1 192 ? -66.474  7.598   -82.836  1.00 26.14  ? 192 ASP A CA  1 
ATOM   1543  C C   . ASP A  1 192 ? -65.727  6.770   -83.875  1.00 25.35  ? 192 ASP A C   1 
ATOM   1544  O O   . ASP A  1 192 ? -65.688  7.156   -85.039  1.00 25.13  ? 192 ASP A O   1 
ATOM   1545  C CB  . ASP A  1 192 ? -67.694  8.240   -83.463  1.00 27.85  ? 192 ASP A CB  1 
ATOM   1546  C CG  . ASP A  1 192 ? -68.695  7.265   -84.065  1.00 29.00  ? 192 ASP A CG  1 
ATOM   1547  O OD1 . ASP A  1 192 ? -68.464  6.027   -83.957  1.00 29.53  ? 192 ASP A OD1 1 
ATOM   1548  O OD2 . ASP A  1 192 ? -69.651  7.758   -84.668  1.00 29.24  ? 192 ASP A OD2 1 
ATOM   1549  N N   . HIS A  1 193 ? -65.148  5.644   -83.449  1.00 24.05  ? 193 HIS A N   1 
ATOM   1550  C CA  . HIS A  1 193 ? -64.402  4.770   -84.343  1.00 25.21  ? 193 HIS A CA  1 
ATOM   1551  C C   . HIS A  1 193 ? -65.123  3.439   -84.594  1.00 25.95  ? 193 HIS A C   1 
ATOM   1552  O O   . HIS A  1 193 ? -64.535  2.539   -85.201  1.00 28.05  ? 193 HIS A O   1 
ATOM   1553  C CB  . HIS A  1 193 ? -63.021  4.488   -83.761  1.00 26.22  ? 193 HIS A CB  1 
ATOM   1554  C CG  . HIS A  1 193 ? -62.172  5.692   -83.493  1.00 28.29  ? 193 HIS A CG  1 
ATOM   1555  N ND1 . HIS A  1 193 ? -61.925  6.728   -84.380  1.00 29.53  ? 193 HIS A ND1 1 
ATOM   1556  C CD2 . HIS A  1 193 ? -61.460  5.974   -82.391  1.00 28.36  ? 193 HIS A CD2 1 
ATOM   1557  C CE1 . HIS A  1 193 ? -61.103  7.591   -83.813  1.00 27.97  ? 193 HIS A CE1 1 
ATOM   1558  N NE2 . HIS A  1 193 ? -60.824  7.170   -82.603  1.00 29.21  ? 193 HIS A NE2 1 
ATOM   1559  N N   . ASN A  1 194 ? -66.358  3.321   -84.077  1.00 25.27  ? 194 ASN A N   1 
ATOM   1560  C CA  . ASN A  1 194 ? -67.236  2.184   -84.267  1.00 25.51  ? 194 ASN A CA  1 
ATOM   1561  C C   . ASN A  1 194 ? -66.522  0.906   -83.804  1.00 25.61  ? 194 ASN A C   1 
ATOM   1562  O O   . ASN A  1 194 ? -66.239  0.018   -84.596  1.00 23.81  ? 194 ASN A O   1 
ATOM   1563  C CB  . ASN A  1 194 ? -67.763  2.165   -85.693  1.00 27.20  ? 194 ASN A CB  1 
ATOM   1564  C CG  . ASN A  1 194 ? -68.771  1.054   -85.941  1.00 29.23  ? 194 ASN A CG  1 
ATOM   1565  O OD1 . ASN A  1 194 ? -69.461  0.582   -85.034  1.00 28.86  ? 194 ASN A OD1 1 
ATOM   1566  N ND2 . ASN A  1 194 ? -68.892  0.634   -87.185  1.00 29.50  ? 194 ASN A ND2 1 
ATOM   1567  N N   . GLU A  1 195 ? -66.193  0.888   -82.507  1.00 25.09  ? 195 GLU A N   1 
ATOM   1568  C CA  . GLU A  1 195 ? -65.409  -0.152  -81.861  1.00 25.75  ? 195 GLU A CA  1 
ATOM   1569  C C   . GLU A  1 195 ? -65.662  -0.049  -80.358  1.00 26.05  ? 195 GLU A C   1 
ATOM   1570  O O   . GLU A  1 195 ? -65.966  1.026   -79.827  1.00 25.81  ? 195 GLU A O   1 
ATOM   1571  C CB  . GLU A  1 195 ? -63.918  -0.090  -82.180  1.00 24.34  ? 195 GLU A CB  1 
ATOM   1572  C CG  . GLU A  1 195 ? -63.264  1.197   -81.707  1.00 24.18  ? 195 GLU A CG  1 
ATOM   1573  C CD  . GLU A  1 195 ? -61.772  1.315   -81.950  1.00 24.27  ? 195 GLU A CD  1 
ATOM   1574  O OE1 . GLU A  1 195 ? -61.239  0.361   -82.537  1.00 23.25  ? 195 GLU A OE1 1 
ATOM   1575  O OE2 . GLU A  1 195 ? -61.176  2.352   -81.574  1.00 24.28  ? 195 GLU A OE2 1 
ATOM   1576  N N   . GLY A  1 196 ? -65.604  -1.202  -79.709  1.00 27.96  ? 196 GLY A N   1 
ATOM   1577  C CA  . GLY A  1 196 ? -65.960  -1.330  -78.310  1.00 28.19  ? 196 GLY A CA  1 
ATOM   1578  C C   . GLY A  1 196 ? -67.298  -0.663  -78.010  1.00 28.92  ? 196 GLY A C   1 
ATOM   1579  O O   . GLY A  1 196 ? -68.337  -0.963  -78.610  1.00 27.67  ? 196 GLY A O   1 
ATOM   1580  N N   . GLN A  1 197 ? -67.244  0.269   -77.059  1.00 30.38  ? 197 GLN A N   1 
ATOM   1581  C CA  . GLN A  1 197 ? -68.430  0.950   -76.572  1.00 28.09  ? 197 GLN A CA  1 
ATOM   1582  C C   . GLN A  1 197 ? -69.179  1.633   -77.711  1.00 26.63  ? 197 GLN A C   1 
ATOM   1583  O O   . GLN A  1 197 ? -70.402  1.613   -77.669  1.00 26.15  ? 197 GLN A O   1 
ATOM   1584  C CB  . GLN A  1 197 ? -68.084  1.969   -75.480  1.00 27.18  ? 197 GLN A CB  1 
ATOM   1585  C CG  . GLN A  1 197 ? -67.559  1.325   -74.202  1.00 26.89  ? 197 GLN A CG  1 
ATOM   1586  C CD  . GLN A  1 197 ? -66.054  1.302   -74.180  1.00 25.76  ? 197 GLN A CD  1 
ATOM   1587  O OE1 . GLN A  1 197 ? -65.406  0.872   -75.136  1.00 24.65  ? 197 GLN A OE1 1 
ATOM   1588  N NE2 . GLN A  1 197 ? -65.501  1.919   -73.153  1.00 25.94  ? 197 GLN A NE2 1 
ATOM   1589  N N   . THR A  1 198 ? -68.477  2.199   -78.714  1.00 25.41  ? 198 THR A N   1 
ATOM   1590  C CA  . THR A  1 198 ? -69.173  2.957   -79.746  1.00 27.12  ? 198 THR A CA  1 
ATOM   1591  C C   . THR A  1 198 ? -69.747  2.010   -80.792  1.00 26.50  ? 198 THR A C   1 
ATOM   1592  O O   . THR A  1 198 ? -70.598  2.452   -81.550  1.00 26.59  ? 198 THR A O   1 
ATOM   1593  C CB  . THR A  1 198 ? -68.323  4.037   -80.417  1.00 26.72  ? 198 THR A CB  1 
ATOM   1594  O OG1 . THR A  1 198 ? -67.180  3.425   -80.993  1.00 31.59  ? 198 THR A OG1 1 
ATOM   1595  C CG2 . THR A  1 198 ? -67.806  5.075   -79.449  1.00 25.73  ? 198 THR A CG2 1 
ATOM   1596  N N   . ALA A  1 199 ? -69.256  0.761   -80.863  1.00 25.72  ? 199 ALA A N   1 
ATOM   1597  C CA  . ALA A  1 199 ? -69.827  -0.243  -81.762  1.00 27.04  ? 199 ALA A CA  1 
ATOM   1598  C C   . ALA A  1 199 ? -71.105  -0.864  -81.179  1.00 26.37  ? 199 ALA A C   1 
ATOM   1599  O O   . ALA A  1 199 ? -71.992  -1.227  -81.929  1.00 27.44  ? 199 ALA A O   1 
ATOM   1600  C CB  . ALA A  1 199 ? -68.809  -1.346  -82.082  1.00 27.52  ? 199 ALA A CB  1 
ATOM   1601  N N   . THR A  1 200 ? -71.175  -1.018  -79.856  1.00 26.05  ? 200 THR A N   1 
ATOM   1602  C CA  . THR A  1 200 ? -72.292  -1.671  -79.199  1.00 27.37  ? 200 THR A CA  1 
ATOM   1603  C C   . THR A  1 200 ? -73.433  -0.666  -79.050  1.00 28.18  ? 200 THR A C   1 
ATOM   1604  O O   . THR A  1 200 ? -74.563  -0.947  -79.436  1.00 29.34  ? 200 THR A O   1 
ATOM   1605  C CB  . THR A  1 200 ? -71.862  -2.226  -77.838  1.00 28.31  ? 200 THR A CB  1 
ATOM   1606  O OG1 . THR A  1 200 ? -71.178  -1.208  -77.096  1.00 27.06  ? 200 THR A OG1 1 
ATOM   1607  C CG2 . THR A  1 200 ? -71.002  -3.472  -77.973  1.00 29.64  ? 200 THR A CG2 1 
ATOM   1608  N N   . MET A  1 201 ? -73.117  0.501   -78.470  1.00 27.25  ? 201 MET A N   1 
ATOM   1609  C CA  . MET A  1 201 ? -74.117  1.453   -78.042  1.00 27.65  ? 201 MET A CA  1 
ATOM   1610  C C   . MET A  1 201 ? -74.392  2.473   -79.134  1.00 26.62  ? 201 MET A C   1 
ATOM   1611  O O   . MET A  1 201 ? -75.484  3.036   -79.180  1.00 25.88  ? 201 MET A O   1 
ATOM   1612  C CB  . MET A  1 201 ? -73.696  2.113   -76.725  1.00 29.19  ? 201 MET A CB  1 
ATOM   1613  C CG  . MET A  1 201 ? -73.855  1.154   -75.554  1.00 29.32  ? 201 MET A CG  1 
ATOM   1614  S SD  . MET A  1 201 ? -73.107  1.688   -74.010  1.00 30.24  ? 201 MET A SD  1 
ATOM   1615  C CE  . MET A  1 201 ? -71.411  1.146   -74.299  1.00 31.55  ? 201 MET A CE  1 
ATOM   1616  N N   . GLY A  1 202 ? -73.433  2.634   -80.050  1.00 26.17  ? 202 GLY A N   1 
ATOM   1617  C CA  . GLY A  1 202 ? -73.427  3.755   -80.968  1.00 24.48  ? 202 GLY A CA  1 
ATOM   1618  C C   . GLY A  1 202 ? -72.906  4.982   -80.237  1.00 24.22  ? 202 GLY A C   1 
ATOM   1619  O O   . GLY A  1 202 ? -72.868  4.997   -79.016  1.00 24.85  ? 202 GLY A O   1 
ATOM   1620  N N   . PHE A  1 203 ? -72.492  6.015   -80.976  1.00 25.61  ? 203 PHE A N   1 
ATOM   1621  C CA  . PHE A  1 203 ? -71.778  7.128   -80.367  1.00 24.97  ? 203 PHE A CA  1 
ATOM   1622  C C   . PHE A  1 203 ? -72.715  7.963   -79.499  1.00 25.45  ? 203 PHE A C   1 
ATOM   1623  O O   . PHE A  1 203 ? -72.449  8.181   -78.327  1.00 26.55  ? 203 PHE A O   1 
ATOM   1624  C CB  . PHE A  1 203 ? -71.192  7.961   -81.501  1.00 26.53  ? 203 PHE A CB  1 
ATOM   1625  C CG  . PHE A  1 203 ? -70.196  9.036   -81.107  1.00 24.55  ? 203 PHE A CG  1 
ATOM   1626  C CD1 . PHE A  1 203 ? -69.250  8.799   -80.141  1.00 23.34  ? 203 PHE A CD1 1 
ATOM   1627  C CD2 . PHE A  1 203 ? -70.228  10.283  -81.724  1.00 24.94  ? 203 PHE A CD2 1 
ATOM   1628  C CE1 . PHE A  1 203 ? -68.298  9.773   -79.842  1.00 24.44  ? 203 PHE A CE1 1 
ATOM   1629  C CE2 . PHE A  1 203 ? -69.300  11.254  -81.403  1.00 23.69  ? 203 PHE A CE2 1 
ATOM   1630  C CZ  . PHE A  1 203 ? -68.343  11.004  -80.452  1.00 23.69  ? 203 PHE A CZ  1 
ATOM   1631  N N   . LYS A  1 204 ? -73.824  8.429   -80.073  1.00 26.77  ? 204 LYS A N   1 
ATOM   1632  C CA  . LYS A  1 204 ? -74.842  9.126   -79.299  1.00 27.21  ? 204 LYS A CA  1 
ATOM   1633  C C   . LYS A  1 204 ? -75.138  8.419   -77.974  1.00 29.24  ? 204 LYS A C   1 
ATOM   1634  O O   . LYS A  1 204 ? -75.016  9.024   -76.912  1.00 32.55  ? 204 LYS A O   1 
ATOM   1635  C CB  . LYS A  1 204 ? -76.165  9.274   -80.049  1.00 25.48  ? 204 LYS A CB  1 
ATOM   1636  C CG  . LYS A  1 204 ? -77.282  9.926   -79.245  1.00 26.02  ? 204 LYS A CG  1 
ATOM   1637  C CD  . LYS A  1 204 ? -78.693  9.727   -79.821  1.00 25.93  ? 204 LYS A CD  1 
ATOM   1638  C CE  . LYS A  1 204 ? -79.771  10.103  -78.873  1.00 25.91  ? 204 LYS A CE  1 
ATOM   1639  N NZ  . LYS A  1 204 ? -81.113  9.869   -79.409  1.00 26.41  ? 204 LYS A NZ  1 
ATOM   1640  N N   . ASP A  1 205 ? -75.582  7.155   -78.020  1.00 31.45  ? 205 ASP A N   1 
ATOM   1641  C CA  . ASP A  1 205 ? -76.088  6.499   -76.819  1.00 29.60  ? 205 ASP A CA  1 
ATOM   1642  C C   . ASP A  1 205 ? -74.956  6.250   -75.825  1.00 27.74  ? 205 ASP A C   1 
ATOM   1643  O O   . ASP A  1 205 ? -75.193  6.249   -74.622  1.00 28.33  ? 205 ASP A O   1 
ATOM   1644  C CB  . ASP A  1 205 ? -76.958  5.292   -77.138  1.00 29.89  ? 205 ASP A CB  1 
ATOM   1645  C CG  . ASP A  1 205 ? -78.318  5.645   -77.692  1.00 31.59  ? 205 ASP A CG  1 
ATOM   1646  O OD1 . ASP A  1 205 ? -78.529  6.861   -77.915  1.00 31.27  ? 205 ASP A OD1 1 
ATOM   1647  O OD2 . ASP A  1 205 ? -79.159  4.721   -77.879  1.00 34.21  ? 205 ASP A OD2 1 
ATOM   1648  N N   . TYR A  1 206 ? -73.725  6.058   -76.306  1.00 27.89  ? 206 TYR A N   1 
ATOM   1649  C CA  . TYR A  1 206 ? -72.639  5.789   -75.378  1.00 28.04  ? 206 TYR A CA  1 
ATOM   1650  C C   . TYR A  1 206 ? -72.436  7.018   -74.500  1.00 28.41  ? 206 TYR A C   1 
ATOM   1651  O O   . TYR A  1 206 ? -72.491  6.937   -73.277  1.00 29.48  ? 206 TYR A O   1 
ATOM   1652  C CB  . TYR A  1 206 ? -71.368  5.340   -76.098  1.00 27.43  ? 206 TYR A CB  1 
ATOM   1653  C CG  . TYR A  1 206 ? -70.182  5.108   -75.172  1.00 26.14  ? 206 TYR A CG  1 
ATOM   1654  C CD1 . TYR A  1 206 ? -70.313  4.356   -74.022  1.00 26.91  ? 206 TYR A CD1 1 
ATOM   1655  C CD2 . TYR A  1 206 ? -68.961  5.711   -75.428  1.00 27.12  ? 206 TYR A CD2 1 
ATOM   1656  C CE1 . TYR A  1 206 ? -69.246  4.163   -73.165  1.00 28.45  ? 206 TYR A CE1 1 
ATOM   1657  C CE2 . TYR A  1 206 ? -67.887  5.544   -74.576  1.00 29.63  ? 206 TYR A CE2 1 
ATOM   1658  C CZ  . TYR A  1 206 ? -68.021  4.739   -73.454  1.00 31.13  ? 206 TYR A CZ  1 
ATOM   1659  O OH  . TYR A  1 206 ? -66.950  4.551   -72.619  1.00 33.51  ? 206 TYR A OH  1 
ATOM   1660  N N   . ILE A  1 207 ? -72.275  8.184   -75.128  1.00 29.67  ? 207 ILE A N   1 
ATOM   1661  C CA  . ILE A  1 207 ? -71.935  9.383   -74.383  1.00 28.30  ? 207 ILE A CA  1 
ATOM   1662  C C   . ILE A  1 207 ? -73.130  9.804   -73.538  1.00 28.89  ? 207 ILE A C   1 
ATOM   1663  O O   . ILE A  1 207 ? -72.958  10.232  -72.407  1.00 30.43  ? 207 ILE A O   1 
ATOM   1664  C CB  . ILE A  1 207 ? -71.465  10.480  -75.344  1.00 28.61  ? 207 ILE A CB  1 
ATOM   1665  C CG1 . ILE A  1 207 ? -70.293  9.961   -76.186  1.00 27.35  ? 207 ILE A CG1 1 
ATOM   1666  C CG2 . ILE A  1 207 ? -71.143  11.775  -74.582  1.00 28.70  ? 207 ILE A CG2 1 
ATOM   1667  C CD1 . ILE A  1 207 ? -69.067  9.547   -75.383  1.00 28.19  ? 207 ILE A CD1 1 
ATOM   1668  N N   . LYS A  1 208 ? -74.345  9.605   -74.048  1.00 31.15  ? 208 LYS A N   1 
ATOM   1669  C CA  . LYS A  1 208 ? -75.559  9.926   -73.294  1.00 32.53  ? 208 LYS A CA  1 
ATOM   1670  C C   . LYS A  1 208 ? -75.663  9.054   -72.040  1.00 32.72  ? 208 LYS A C   1 
ATOM   1671  O O   . LYS A  1 208 ? -76.075  9.518   -70.974  1.00 31.95  ? 208 LYS A O   1 
ATOM   1672  C CB  . LYS A  1 208 ? -76.784  9.717   -74.190  1.00 33.24  ? 208 LYS A CB  1 
ATOM   1673  C CG  . LYS A  1 208 ? -78.162  9.883   -73.524  1.00 36.56  ? 208 LYS A CG  1 
ATOM   1674  C CD  . LYS A  1 208 ? -79.283  9.816   -74.556  1.00 38.37  ? 208 LYS A CD  1 
ATOM   1675  C CE  . LYS A  1 208 ? -80.656  9.594   -73.984  1.00 44.62  ? 208 LYS A CE  1 
ATOM   1676  N NZ  . LYS A  1 208 ? -80.969  8.160   -73.857  1.00 44.63  ? 208 LYS A NZ  1 
ATOM   1677  N N   . GLY A  1 209 ? -75.294  7.775   -72.188  1.00 33.38  ? 209 GLY A N   1 
ATOM   1678  C CA  . GLY A  1 209 ? -75.298  6.850   -71.072  1.00 33.07  ? 209 GLY A CA  1 
ATOM   1679  C C   . GLY A  1 209 ? -74.411  7.382   -69.954  1.00 32.72  ? 209 GLY A C   1 
ATOM   1680  O O   . GLY A  1 209 ? -74.783  7.309   -68.778  1.00 33.55  ? 209 GLY A O   1 
ATOM   1681  N N   . LEU A  1 210 ? -73.251  7.929   -70.331  1.00 29.33  ? 210 LEU A N   1 
ATOM   1682  C CA  . LEU A  1 210 ? -72.322  8.430   -69.332  1.00 29.35  ? 210 LEU A CA  1 
ATOM   1683  C C   . LEU A  1 210 ? -72.865  9.669   -68.631  1.00 30.16  ? 210 LEU A C   1 
ATOM   1684  O O   . LEU A  1 210 ? -72.598  9.904   -67.460  1.00 31.86  ? 210 LEU A O   1 
ATOM   1685  C CB  . LEU A  1 210 ? -70.986  8.718   -69.992  1.00 28.44  ? 210 LEU A CB  1 
ATOM   1686  C CG  . LEU A  1 210 ? -70.247  7.494   -70.542  1.00 26.49  ? 210 LEU A CG  1 
ATOM   1687  C CD1 . LEU A  1 210 ? -68.816  7.870   -70.909  1.00 26.09  ? 210 LEU A CD1 1 
ATOM   1688  C CD2 . LEU A  1 210 ? -70.274  6.385   -69.554  1.00 25.37  ? 210 LEU A CD2 1 
ATOM   1689  N N   . ASN A  1 211 ? -73.606  10.477  -69.369  1.00 31.37  ? 211 ASN A N   1 
ATOM   1690  C CA  . ASN A  1 211 ? -74.250  11.667  -68.836  1.00 31.24  ? 211 ASN A CA  1 
ATOM   1691  C C   . ASN A  1 211 ? -75.386  11.270  -67.877  1.00 32.86  ? 211 ASN A C   1 
ATOM   1692  O O   . ASN A  1 211 ? -75.594  11.887  -66.829  1.00 33.05  ? 211 ASN A O   1 
ATOM   1693  C CB  . ASN A  1 211 ? -74.677  12.514  -70.030  1.00 31.04  ? 211 ASN A CB  1 
ATOM   1694  C CG  . ASN A  1 211 ? -74.901  13.962  -69.677  1.00 31.69  ? 211 ASN A CG  1 
ATOM   1695  O OD1 . ASN A  1 211 ? -74.169  14.540  -68.856  1.00 30.52  ? 211 ASN A OD1 1 
ATOM   1696  N ND2 . ASN A  1 211 ? -75.919  14.544  -70.285  1.00 31.43  ? 211 ASN A ND2 1 
ATOM   1697  N N   . GLU A  1 212 ? -76.123  10.204  -68.211  1.00 31.35  ? 212 GLU A N   1 
ATOM   1698  C CA  . GLU A  1 212 ? -77.147  9.690   -67.313  1.00 32.02  ? 212 GLU A CA  1 
ATOM   1699  C C   . GLU A  1 212 ? -76.518  9.132   -66.042  1.00 30.74  ? 212 GLU A C   1 
ATOM   1700  O O   . GLU A  1 212 ? -77.012  9.390   -64.961  1.00 30.81  ? 212 GLU A O   1 
ATOM   1701  C CB  . GLU A  1 212 ? -78.068  8.681   -68.011  1.00 32.54  ? 212 GLU A CB  1 
ATOM   1702  C CG  . GLU A  1 212 ? -78.948  9.371   -69.054  1.00 33.98  ? 212 GLU A CG  1 
ATOM   1703  C CD  . GLU A  1 212 ? -79.535  8.408   -70.052  1.00 37.18  ? 212 GLU A CD  1 
ATOM   1704  O OE1 . GLU A  1 212 ? -79.235  7.210   -69.906  1.00 40.54  ? 212 GLU A OE1 1 
ATOM   1705  O OE2 . GLU A  1 212 ? -80.244  8.844   -70.973  1.00 37.84  ? 212 GLU A OE2 1 
ATOM   1706  N N   . LEU A  1 213 ? -75.444  8.351   -66.167  1.00 33.14  ? 213 LEU A N   1 
ATOM   1707  C CA  . LEU A  1 213 ? -74.754  7.774   -65.013  1.00 33.00  ? 213 LEU A CA  1 
ATOM   1708  C C   . LEU A  1 213 ? -74.183  8.898   -64.135  1.00 31.66  ? 213 LEU A C   1 
ATOM   1709  O O   . LEU A  1 213 ? -74.253  8.848   -62.904  1.00 30.97  ? 213 LEU A O   1 
ATOM   1710  C CB  . LEU A  1 213 ? -73.676  6.791   -65.489  1.00 33.51  ? 213 LEU A CB  1 
ATOM   1711  C CG  . LEU A  1 213 ? -74.151  5.453   -66.088  1.00 36.30  ? 213 LEU A CG  1 
ATOM   1712  C CD1 . LEU A  1 213 ? -72.938  4.680   -66.591  1.00 34.11  ? 213 LEU A CD1 1 
ATOM   1713  C CD2 . LEU A  1 213 ? -75.008  4.530   -65.191  1.00 35.49  ? 213 LEU A CD2 1 
ATOM   1714  N N   . ASN A  1 214 ? -73.635  9.934   -64.787  1.00 32.34  ? 214 ASN A N   1 
ATOM   1715  C CA  . ASN A  1 214 ? -73.172  11.135  -64.103  1.00 32.38  ? 214 ASN A CA  1 
ATOM   1716  C C   . ASN A  1 214 ? -74.311  11.795  -63.306  1.00 34.37  ? 214 ASN A C   1 
ATOM   1717  O O   . ASN A  1 214 ? -74.000  12.437  -62.308  1.00 36.65  ? 214 ASN A O   1 
ATOM   1718  C CB  . ASN A  1 214 ? -72.430  12.060  -65.058  1.00 30.41  ? 214 ASN A CB  1 
ATOM   1719  C CG  . ASN A  1 214 ? -71.114  11.483  -65.540  1.00 30.53  ? 214 ASN A CG  1 
ATOM   1720  O OD1 . ASN A  1 214 ? -70.442  10.733  -64.828  1.00 30.18  ? 214 ASN A OD1 1 
ATOM   1721  N ND2 . ASN A  1 214 ? -70.685  11.857  -66.733  1.00 30.77  ? 214 ASN A ND2 1 
ATOM   1722  N N   . GLY A  1 215 ? -75.598  11.658  -63.717  1.00 34.32  ? 215 GLY A N   1 
ATOM   1723  C CA  . GLY A  1 215 ? -76.761  12.104  -62.928  1.00 34.66  ? 215 GLY A CA  1 
ATOM   1724  C C   . GLY A  1 215 ? -77.561  13.302  -63.496  1.00 36.67  ? 215 GLY A C   1 
ATOM   1725  O O   . GLY A  1 215 ? -78.483  13.794  -62.851  1.00 39.25  ? 215 GLY A O   1 
ATOM   1726  N N   . LEU A  1 216 ? -77.178  13.854  -64.661  1.00 37.18  ? 216 LEU A N   1 
ATOM   1727  C CA  . LEU A  1 216 ? -77.963  14.870  -65.353  1.00 34.53  ? 216 LEU A CA  1 
ATOM   1728  C C   . LEU A  1 216 ? -78.157  16.102  -64.483  1.00 33.59  ? 216 LEU A C   1 
ATOM   1729  O O   . LEU A  1 216 ? -79.180  16.754  -64.591  1.00 33.10  ? 216 LEU A O   1 
ATOM   1730  C CB  . LEU A  1 216 ? -79.305  14.284  -65.802  1.00 36.70  ? 216 LEU A CB  1 
ATOM   1731  C CG  . LEU A  1 216 ? -79.241  13.110  -66.793  1.00 35.88  ? 216 LEU A CG  1 
ATOM   1732  C CD1 . LEU A  1 216 ? -80.617  12.641  -67.203  1.00 36.48  ? 216 LEU A CD1 1 
ATOM   1733  C CD2 . LEU A  1 216 ? -78.435  13.501  -68.018  1.00 35.41  ? 216 LEU A CD2 1 
ATOM   1734  N N   . ASP A  1 217 ? -77.124  16.481  -63.720  1.00 33.50  ? 217 ASP A N   1 
ATOM   1735  C CA  . ASP A  1 217 ? -77.225  17.522  -62.707  1.00 34.06  ? 217 ASP A CA  1 
ATOM   1736  C C   . ASP A  1 217 ? -76.135  18.590  -62.860  1.00 34.45  ? 217 ASP A C   1 
ATOM   1737  O O   . ASP A  1 217 ? -76.012  19.490  -62.040  1.00 35.64  ? 217 ASP A O   1 
ATOM   1738  C CB  . ASP A  1 217 ? -77.149  16.888  -61.333  1.00 34.52  ? 217 ASP A CB  1 
ATOM   1739  C CG  . ASP A  1 217 ? -75.916  16.029  -61.095  1.00 34.58  ? 217 ASP A CG  1 
ATOM   1740  O OD1 . ASP A  1 217 ? -75.255  15.621  -62.057  1.00 33.46  ? 217 ASP A OD1 1 
ATOM   1741  O OD2 . ASP A  1 217 ? -75.608  15.789  -59.946  1.00 38.26  ? 217 ASP A OD2 1 
ATOM   1742  N N   . LYS A  1 218 ? -75.334  18.500  -63.919  1.00 36.26  ? 218 LYS A N   1 
ATOM   1743  C CA  . LYS A  1 218 ? -74.418  19.564  -64.297  1.00 36.69  ? 218 LYS A CA  1 
ATOM   1744  C C   . LYS A  1 218 ? -74.378  19.711  -65.816  1.00 33.95  ? 218 LYS A C   1 
ATOM   1745  O O   . LYS A  1 218 ? -74.653  18.784  -66.547  1.00 34.01  ? 218 LYS A O   1 
ATOM   1746  C CB  . LYS A  1 218 ? -72.993  19.261  -63.828  1.00 36.95  ? 218 LYS A CB  1 
ATOM   1747  C CG  . LYS A  1 218 ? -72.881  19.069  -62.355  1.00 40.42  ? 218 LYS A CG  1 
ATOM   1748  C CD  . LYS A  1 218 ? -71.541  18.513  -61.873  1.00 43.35  ? 218 LYS A CD  1 
ATOM   1749  C CE  . LYS A  1 218 ? -71.547  18.787  -60.376  1.00 45.26  ? 218 LYS A CE  1 
ATOM   1750  N NZ  . LYS A  1 218 ? -70.371  18.158  -59.798  1.00 45.16  ? 218 LYS A NZ  1 
ATOM   1751  N N   . PRO A  1 219 ? -73.966  20.866  -66.362  1.00 33.51  ? 219 PRO A N   1 
ATOM   1752  C CA  . PRO A  1 219 ? -73.715  20.954  -67.796  1.00 31.91  ? 219 PRO A CA  1 
ATOM   1753  C C   . PRO A  1 219 ? -72.652  19.919  -68.190  1.00 30.37  ? 219 PRO A C   1 
ATOM   1754  O O   . PRO A  1 219 ? -71.784  19.570  -67.393  1.00 28.85  ? 219 PRO A O   1 
ATOM   1755  C CB  . PRO A  1 219 ? -73.226  22.404  -67.994  1.00 32.58  ? 219 PRO A CB  1 
ATOM   1756  C CG  . PRO A  1 219 ? -73.661  23.137  -66.749  1.00 32.85  ? 219 PRO A CG  1 
ATOM   1757  C CD  . PRO A  1 219 ? -73.648  22.101  -65.632  1.00 33.75  ? 219 PRO A CD  1 
ATOM   1758  N N   . PHE A  1 220 ? -72.780  19.425  -69.431  1.00 29.22  ? 220 PHE A N   1 
ATOM   1759  C CA  . PHE A  1 220 ? -71.894  18.480  -70.070  1.00 26.01  ? 220 PHE A CA  1 
ATOM   1760  C C   . PHE A  1 220 ? -71.311  19.109  -71.330  1.00 26.35  ? 220 PHE A C   1 
ATOM   1761  O O   . PHE A  1 220 ? -72.057  19.648  -72.156  1.00 27.21  ? 220 PHE A O   1 
ATOM   1762  C CB  . PHE A  1 220 ? -72.709  17.254  -70.501  1.00 25.78  ? 220 PHE A CB  1 
ATOM   1763  C CG  . PHE A  1 220 ? -71.946  16.337  -71.449  1.00 24.72  ? 220 PHE A CG  1 
ATOM   1764  C CD1 . PHE A  1 220 ? -70.605  16.037  -71.228  1.00 23.94  ? 220 PHE A CD1 1 
ATOM   1765  C CD2 . PHE A  1 220 ? -72.560  15.828  -72.586  1.00 25.11  ? 220 PHE A CD2 1 
ATOM   1766  C CE1 . PHE A  1 220 ? -69.917  15.228  -72.110  1.00 24.81  ? 220 PHE A CE1 1 
ATOM   1767  C CE2 . PHE A  1 220 ? -71.877  14.997  -73.462  1.00 23.88  ? 220 PHE A CE2 1 
ATOM   1768  C CZ  . PHE A  1 220 ? -70.566  14.698  -73.224  1.00 24.31  ? 220 PHE A CZ  1 
ATOM   1769  N N   . ILE A  1 221 ? -69.985  19.032  -71.486  1.00 25.93  ? 221 ILE A N   1 
ATOM   1770  C CA  . ILE A  1 221 ? -69.346  19.532  -72.687  1.00 27.39  ? 221 ILE A CA  1 
ATOM   1771  C C   . ILE A  1 221 ? -68.427  18.453  -73.246  1.00 27.46  ? 221 ILE A C   1 
ATOM   1772  O O   . ILE A  1 221 ? -68.038  17.531  -72.532  1.00 26.99  ? 221 ILE A O   1 
ATOM   1773  C CB  . ILE A  1 221 ? -68.597  20.861  -72.437  1.00 27.93  ? 221 ILE A CB  1 
ATOM   1774  C CG1 . ILE A  1 221 ? -67.351  20.680  -71.574  1.00 29.09  ? 221 ILE A CG1 1 
ATOM   1775  C CG2 . ILE A  1 221 ? -69.548  21.915  -71.847  1.00 28.59  ? 221 ILE A CG2 1 
ATOM   1776  C CD1 . ILE A  1 221 ? -66.526  21.956  -71.387  1.00 31.44  ? 221 ILE A CD1 1 
ATOM   1777  N N   . THR A  1 222 ? -68.108  18.592  -74.544  1.00 27.82  ? 222 THR A N   1 
ATOM   1778  C CA  . THR A  1 222 ? -67.076  17.791  -75.171  1.00 28.16  ? 222 THR A CA  1 
ATOM   1779  C C   . THR A  1 222 ? -65.834  18.659  -75.326  1.00 27.31  ? 222 THR A C   1 
ATOM   1780  O O   . THR A  1 222 ? -65.931  19.783  -75.825  1.00 23.31  ? 222 THR A O   1 
ATOM   1781  C CB  . THR A  1 222 ? -67.575  17.231  -76.502  1.00 27.23  ? 222 THR A CB  1 
ATOM   1782  O OG1 . THR A  1 222 ? -67.783  18.321  -77.389  1.00 27.09  ? 222 THR A OG1 1 
ATOM   1783  C CG2 . THR A  1 222 ? -68.899  16.520  -76.335  1.00 26.96  ? 222 THR A CG2 1 
ATOM   1784  N N   . THR A  1 223 ? -64.686  18.061  -74.962  1.00 26.52  ? 223 THR A N   1 
ATOM   1785  C CA  . THR A  1 223 ? -63.402  18.730  -75.017  1.00 26.17  ? 223 THR A CA  1 
ATOM   1786  C C   . THR A  1 223 ? -62.605  18.282  -76.240  1.00 25.72  ? 223 THR A C   1 
ATOM   1787  O O   . THR A  1 223 ? -61.503  18.786  -76.493  1.00 24.92  ? 223 THR A O   1 
ATOM   1788  C CB  . THR A  1 223 ? -62.687  18.474  -73.696  1.00 28.03  ? 223 THR A CB  1 
ATOM   1789  O OG1 . THR A  1 223 ? -62.744  17.077  -73.395  1.00 26.44  ? 223 THR A OG1 1 
ATOM   1790  C CG2 . THR A  1 223 ? -63.305  19.312  -72.587  1.00 28.70  ? 223 THR A CG2 1 
ATOM   1791  N N   . ALA A  1 224 ? -63.201  17.414  -77.063  1.00 24.71  ? 224 ALA A N   1 
ATOM   1792  C CA  . ALA A  1 224 ? -62.522  16.974  -78.275  1.00 25.86  ? 224 ALA A CA  1 
ATOM   1793  C C   . ALA A  1 224 ? -63.347  15.913  -79.007  1.00 27.38  ? 224 ALA A C   1 
ATOM   1794  O O   . ALA A  1 224 ? -64.020  15.101  -78.362  1.00 28.02  ? 224 ALA A O   1 
ATOM   1795  C CB  . ALA A  1 224 ? -61.142  16.423  -77.955  1.00 25.52  ? 224 ALA A CB  1 
ATOM   1796  N N   . PHE A  1 225 ? -63.269  15.936  -80.356  1.00 27.82  ? 225 PHE A N   1 
ATOM   1797  C CA  . PHE A  1 225 ? -63.817  14.904  -81.229  1.00 27.29  ? 225 PHE A CA  1 
ATOM   1798  C C   . PHE A  1 225 ? -63.306  15.185  -82.638  1.00 27.28  ? 225 PHE A C   1 
ATOM   1799  O O   . PHE A  1 225 ? -63.050  16.339  -82.973  1.00 25.01  ? 225 PHE A O   1 
ATOM   1800  C CB  . PHE A  1 225 ? -65.349  14.892  -81.127  1.00 27.54  ? 225 PHE A CB  1 
ATOM   1801  C CG  . PHE A  1 225 ? -66.069  16.184  -81.518  1.00 26.46  ? 225 PHE A CG  1 
ATOM   1802  C CD1 . PHE A  1 225 ? -66.305  17.192  -80.584  1.00 27.72  ? 225 PHE A CD1 1 
ATOM   1803  C CD2 . PHE A  1 225 ? -66.534  16.380  -82.805  1.00 25.80  ? 225 PHE A CD2 1 
ATOM   1804  C CE1 . PHE A  1 225 ? -66.996  18.347  -80.927  1.00 27.32  ? 225 PHE A CE1 1 
ATOM   1805  C CE2 . PHE A  1 225 ? -67.192  17.553  -83.155  1.00 27.47  ? 225 PHE A CE2 1 
ATOM   1806  C CZ  . PHE A  1 225 ? -67.458  18.517  -82.205  1.00 26.58  ? 225 PHE A CZ  1 
ATOM   1807  N N   . GLY A  1 226 ? -63.205  14.152  -83.483  1.00 25.93  ? 226 GLY A N   1 
ATOM   1808  C CA  . GLY A  1 226 ? -62.895  14.414  -84.878  1.00 26.57  ? 226 GLY A CA  1 
ATOM   1809  C C   . GLY A  1 226 ? -62.083  13.294  -85.495  1.00 27.61  ? 226 GLY A C   1 
ATOM   1810  O O   . GLY A  1 226 ? -62.012  12.228  -84.914  1.00 28.21  ? 226 GLY A O   1 
ATOM   1811  N N   . TYR A  1 227 ? -61.487  13.576  -86.665  1.00 29.18  ? 227 TYR A N   1 
ATOM   1812  C CA  . TYR A  1 227 ? -60.891  12.567  -87.544  1.00 26.01  ? 227 TYR A CA  1 
ATOM   1813  C C   . TYR A  1 227 ? -59.579  13.067  -88.146  1.00 25.72  ? 227 TYR A C   1 
ATOM   1814  O O   . TYR A  1 227 ? -59.436  14.256  -88.436  1.00 26.05  ? 227 TYR A O   1 
ATOM   1815  C CB  . TYR A  1 227 ? -61.884  12.184  -88.650  1.00 25.04  ? 227 TYR A CB  1 
ATOM   1816  C CG  . TYR A  1 227 ? -63.109  11.510  -88.050  1.00 24.23  ? 227 TYR A CG  1 
ATOM   1817  C CD1 . TYR A  1 227 ? -63.063  10.183  -87.682  1.00 23.95  ? 227 TYR A CD1 1 
ATOM   1818  C CD2 . TYR A  1 227 ? -64.278  12.220  -87.783  1.00 25.13  ? 227 TYR A CD2 1 
ATOM   1819  C CE1 . TYR A  1 227 ? -64.158  9.561   -87.112  1.00 26.87  ? 227 TYR A CE1 1 
ATOM   1820  C CE2 . TYR A  1 227 ? -65.381  11.617  -87.204  1.00 24.91  ? 227 TYR A CE2 1 
ATOM   1821  C CZ  . TYR A  1 227 ? -65.328  10.273  -86.876  1.00 24.88  ? 227 TYR A CZ  1 
ATOM   1822  O OH  . TYR A  1 227 ? -66.366  9.625   -86.286  1.00 21.49  ? 227 TYR A OH  1 
ATOM   1823  N N   . SER A  1 228 ? -58.680  12.114  -88.418  1.00 25.38  ? 228 SER A N   1 
ATOM   1824  C CA  . SER A  1 228 ? -57.355  12.352  -88.946  1.00 25.39  ? 228 SER A CA  1 
ATOM   1825  C C   . SER A  1 228 ? -57.328  11.980  -90.417  1.00 25.60  ? 228 SER A C   1 
ATOM   1826  O O   . SER A  1 228 ? -57.809  10.886  -90.793  1.00 24.17  ? 228 SER A O   1 
ATOM   1827  C CB  . SER A  1 228 ? -56.317  11.553  -88.184  1.00 27.01  ? 228 SER A CB  1 
ATOM   1828  O OG  . SER A  1 228 ? -55.042  11.585  -88.822  1.00 27.05  ? 228 SER A OG  1 
ATOM   1829  N N   . VAL A  1 229 ? -56.649  12.832  -91.218  1.00 24.60  ? 229 VAL A N   1 
ATOM   1830  C CA  . VAL A  1 229 ? -56.564  12.555  -92.644  1.00 26.02  ? 229 VAL A CA  1 
ATOM   1831  C C   . VAL A  1 229 ? -55.160  12.099  -93.052  1.00 27.68  ? 229 VAL A C   1 
ATOM   1832  O O   . VAL A  1 229 ? -54.668  12.389  -94.158  1.00 26.93  ? 229 VAL A O   1 
ATOM   1833  C CB  . VAL A  1 229 ? -57.107  13.742  -93.453  1.00 25.39  ? 229 VAL A CB  1 
ATOM   1834  C CG1 . VAL A  1 229 ? -58.566  13.967  -93.081  1.00 24.89  ? 229 VAL A CG1 1 
ATOM   1835  C CG2 . VAL A  1 229 ? -56.249  15.001  -93.306  1.00 26.50  ? 229 VAL A CG2 1 
ATOM   1836  N N   . SER A  1 230 ? -54.536  11.300  -92.178  1.00 27.95  ? 230 SER A N   1 
ATOM   1837  C CA  . SER A  1 230 ? -53.178  10.836  -92.448  1.00 29.12  ? 230 SER A CA  1 
ATOM   1838  C C   . SER A  1 230 ? -53.181  10.031  -93.749  1.00 29.10  ? 230 SER A C   1 
ATOM   1839  O O   . SER A  1 230 ? -54.152  9.370   -94.093  1.00 29.80  ? 230 SER A O   1 
ATOM   1840  C CB  . SER A  1 230 ? -52.624  10.031  -91.273  1.00 30.69  ? 230 SER A CB  1 
ATOM   1841  O OG  . SER A  1 230 ? -53.281  8.771   -91.107  1.00 27.71  ? 230 SER A OG  1 
ATOM   1842  N N   . PRO A  1 231 ? -52.140  10.108  -94.585  1.00 30.08  ? 231 PRO A N   1 
ATOM   1843  C CA  . PRO A  1 231 ? -52.068  9.226   -95.750  1.00 31.00  ? 231 PRO A CA  1 
ATOM   1844  C C   . PRO A  1 231 ? -52.222  7.725   -95.462  1.00 29.71  ? 231 PRO A C   1 
ATOM   1845  O O   . PRO A  1 231 ? -52.828  7.014   -96.237  1.00 28.52  ? 231 PRO A O   1 
ATOM   1846  C CB  . PRO A  1 231 ? -50.676  9.578   -96.302  1.00 32.06  ? 231 PRO A CB  1 
ATOM   1847  C CG  . PRO A  1 231 ? -50.519  11.053  -95.916  1.00 32.94  ? 231 PRO A CG  1 
ATOM   1848  C CD  . PRO A  1 231 ? -51.043  11.087  -94.495  1.00 32.01  ? 231 PRO A CD  1 
ATOM   1849  N N   . GLU A  1 232 ? -51.655  7.259   -94.351  1.00 29.43  ? 232 GLU A N   1 
ATOM   1850  C CA  . GLU A  1 232 ? -51.880  5.918   -93.869  1.00 31.17  ? 232 GLU A CA  1 
ATOM   1851  C C   . GLU A  1 232 ? -51.696  5.909   -92.354  1.00 29.94  ? 232 GLU A C   1 
ATOM   1852  O O   . GLU A  1 232 ? -51.657  6.974   -91.722  1.00 28.04  ? 232 GLU A O   1 
ATOM   1853  C CB  . GLU A  1 232 ? -50.962  4.982   -94.659  1.00 33.37  ? 232 GLU A CB  1 
ATOM   1854  C CG  . GLU A  1 232 ? -49.503  5.358   -94.508  1.00 36.47  ? 232 GLU A CG  1 
ATOM   1855  C CD  . GLU A  1 232 ? -48.476  4.490   -95.218  1.00 39.29  ? 232 GLU A CD  1 
ATOM   1856  O OE1 . GLU A  1 232 ? -48.372  3.255   -95.019  1.00 40.97  ? 232 GLU A OE1 1 
ATOM   1857  O OE2 . GLU A  1 232 ? -47.687  5.140   -95.922  1.00 41.71  ? 232 GLU A OE2 1 
ATOM   1858  N N   . GLY A  1 233 ? -51.593  4.691   -91.799  1.00 29.45  ? 233 GLY A N   1 
ATOM   1859  C CA  . GLY A  1 233 ? -51.414  4.459   -90.377  1.00 27.64  ? 233 GLY A CA  1 
ATOM   1860  C C   . GLY A  1 233 ? -52.761  4.367   -89.664  1.00 27.12  ? 233 GLY A C   1 
ATOM   1861  O O   . GLY A  1 233 ? -53.803  4.610   -90.264  1.00 25.80  ? 233 GLY A O   1 
ATOM   1862  N N   . GLY A  1 234 ? -52.703  4.063   -88.367  1.00 26.56  ? 234 GLY A N   1 
ATOM   1863  C CA  . GLY A  1 234 ? -53.883  3.943   -87.539  1.00 27.63  ? 234 GLY A CA  1 
ATOM   1864  C C   . GLY A  1 234 ? -54.542  2.564   -87.663  1.00 29.97  ? 234 GLY A C   1 
ATOM   1865  O O   . GLY A  1 234 ? -53.885  1.560   -87.878  1.00 28.82  ? 234 GLY A O   1 
ATOM   1866  N N   . ASN A  1 235 ? -55.867  2.549   -87.512  1.00 33.67  ? 235 ASN A N   1 
ATOM   1867  C CA  . ASN A  1 235 ? -56.683  1.346   -87.533  1.00 34.92  ? 235 ASN A CA  1 
ATOM   1868  C C   . ASN A  1 235 ? -58.163  1.753   -87.678  1.00 31.51  ? 235 ASN A C   1 
ATOM   1869  O O   . ASN A  1 235 ? -58.655  2.597   -86.935  1.00 32.23  ? 235 ASN A O   1 
ATOM   1870  C CB  . ASN A  1 235 ? -56.417  0.533   -86.273  1.00 38.25  ? 235 ASN A CB  1 
ATOM   1871  C CG  . ASN A  1 235 ? -57.173  -0.772  -86.318  1.00 50.72  ? 235 ASN A CG  1 
ATOM   1872  O OD1 . ASN A  1 235 ? -56.871  -1.662  -87.135  1.00 52.42  ? 235 ASN A OD1 1 
ATOM   1873  N ND2 . ASN A  1 235 ? -58.188  -0.887  -85.470  1.00 53.47  ? 235 ASN A ND2 1 
ATOM   1874  N N   . GLY A  1 236 ? -58.864  1.201   -88.665  1.00 29.52  ? 236 GLY A N   1 
ATOM   1875  C CA  . GLY A  1 236 ? -60.239  1.563   -88.937  1.00 30.16  ? 236 GLY A CA  1 
ATOM   1876  C C   . GLY A  1 236 ? -60.363  3.069   -89.193  1.00 33.42  ? 236 GLY A C   1 
ATOM   1877  O O   . GLY A  1 236 ? -59.612  3.656   -89.989  1.00 31.87  ? 236 GLY A O   1 
ATOM   1878  N N   . GLN A  1 237 ? -61.295  3.719   -88.482  1.00 30.54  ? 237 GLN A N   1 
ATOM   1879  C CA  . GLN A  1 237 ? -61.463  5.138   -88.710  1.00 30.84  ? 237 GLN A CA  1 
ATOM   1880  C C   . GLN A  1 237 ? -60.439  5.979   -87.941  1.00 29.27  ? 237 GLN A C   1 
ATOM   1881  O O   . GLN A  1 237 ? -60.511  7.169   -88.005  1.00 27.72  ? 237 GLN A O   1 
ATOM   1882  C CB  . GLN A  1 237 ? -62.867  5.548   -88.317  1.00 30.03  ? 237 GLN A CB  1 
ATOM   1883  C CG  . GLN A  1 237 ? -63.953  4.922   -89.166  1.00 29.97  ? 237 GLN A CG  1 
ATOM   1884  C CD  . GLN A  1 237 ? -65.295  5.410   -88.670  1.00 30.34  ? 237 GLN A CD  1 
ATOM   1885  O OE1 . GLN A  1 237 ? -65.626  6.614   -88.705  1.00 32.86  ? 237 GLN A OE1 1 
ATOM   1886  N NE2 . GLN A  1 237 ? -66.020  4.478   -88.087  1.00 28.76  ? 237 GLN A NE2 1 
ATOM   1887  N N   . TYR A  1 238 ? -59.512  5.395   -87.180  1.00 30.08  ? 238 TYR A N   1 
ATOM   1888  C CA  . TYR A  1 238 ? -58.484  6.187   -86.522  1.00 31.00  ? 238 TYR A CA  1 
ATOM   1889  C C   . TYR A  1 238 ? -57.297  6.314   -87.476  1.00 32.77  ? 238 TYR A C   1 
ATOM   1890  O O   . TYR A  1 238 ? -56.629  5.316   -87.752  1.00 34.14  ? 238 TYR A O   1 
ATOM   1891  C CB  . TYR A  1 238 ? -58.014  5.558   -85.195  1.00 30.15  ? 238 TYR A CB  1 
ATOM   1892  C CG  . TYR A  1 238 ? -56.842  6.280   -84.547  1.00 26.76  ? 238 TYR A CG  1 
ATOM   1893  C CD1 . TYR A  1 238 ? -57.007  7.521   -83.945  1.00 26.77  ? 238 TYR A CD1 1 
ATOM   1894  C CD2 . TYR A  1 238 ? -55.573  5.723   -84.537  1.00 27.00  ? 238 TYR A CD2 1 
ATOM   1895  C CE1 . TYR A  1 238 ? -55.946  8.188   -83.349  1.00 27.44  ? 238 TYR A CE1 1 
ATOM   1896  C CE2 . TYR A  1 238 ? -54.488  6.393   -83.978  1.00 28.60  ? 238 TYR A CE2 1 
ATOM   1897  C CZ  . TYR A  1 238 ? -54.677  7.634   -83.386  1.00 27.75  ? 238 TYR A CZ  1 
ATOM   1898  O OH  . TYR A  1 238 ? -53.625  8.279   -82.806  1.00 29.24  ? 238 TYR A OH  1 
ATOM   1899  N N   . GLY A  1 239 ? -57.066  7.527   -87.986  1.00 31.01  ? 239 GLY A N   1 
ATOM   1900  C CA  . GLY A  1 239 ? -56.137  7.751   -89.077  1.00 30.20  ? 239 GLY A CA  1 
ATOM   1901  C C   . GLY A  1 239 ? -56.809  7.431   -90.409  1.00 31.24  ? 239 GLY A C   1 
ATOM   1902  O O   . GLY A  1 239 ? -57.920  6.867   -90.423  1.00 28.65  ? 239 GLY A O   1 
ATOM   1903  N N   . SER A  1 240 ? -56.130  7.855   -91.498  1.00 29.68  ? 240 SER A N   1 
ATOM   1904  C CA  . SER A  1 240 ? -56.359  7.375   -92.845  1.00 29.25  ? 240 SER A CA  1 
ATOM   1905  C C   . SER A  1 240 ? -57.753  7.716   -93.400  1.00 28.62  ? 240 SER A C   1 
ATOM   1906  O O   . SER A  1 240 ? -58.241  7.087   -94.329  1.00 28.88  ? 240 SER A O   1 
ATOM   1907  C CB  . SER A  1 240 ? -56.040  5.864   -92.871  1.00 30.10  ? 240 SER A CB  1 
ATOM   1908  O OG  . SER A  1 240 ? -54.665  5.646   -92.546  1.00 29.36  ? 240 SER A OG  1 
ATOM   1909  N N   . ASN A  1 241 ? -58.414  8.762   -92.899  1.00 30.10  ? 241 ASN A N   1 
ATOM   1910  C CA  . ASN A  1 241 ? -59.653  9.202   -93.522  1.00 27.31  ? 241 ASN A CA  1 
ATOM   1911  C C   . ASN A  1 241 ? -59.339  10.068  -94.735  1.00 27.26  ? 241 ASN A C   1 
ATOM   1912  O O   . ASN A  1 241 ? -58.300  10.733  -94.774  1.00 27.32  ? 241 ASN A O   1 
ATOM   1913  C CB  . ASN A  1 241 ? -60.511  9.992   -92.549  1.00 27.73  ? 241 ASN A CB  1 
ATOM   1914  C CG  . ASN A  1 241 ? -61.041  9.130   -91.434  1.00 26.83  ? 241 ASN A CG  1 
ATOM   1915  O OD1 . ASN A  1 241 ? -62.210  8.727   -91.448  1.00 31.43  ? 241 ASN A OD1 1 
ATOM   1916  N ND2 . ASN A  1 241 ? -60.236  8.903   -90.420  1.00 26.28  ? 241 ASN A ND2 1 
ATOM   1917  N N   . THR A  1 242 ? -60.265  10.115  -95.704  1.00 27.81  ? 242 THR A N   1 
ATOM   1918  C CA  . THR A  1 242 ? -60.219  11.138  -96.748  1.00 26.83  ? 242 THR A CA  1 
ATOM   1919  C C   . THR A  1 242 ? -60.649  12.466  -96.138  1.00 27.12  ? 242 THR A C   1 
ATOM   1920  O O   . THR A  1 242 ? -61.245  12.493  -95.068  1.00 26.81  ? 242 THR A O   1 
ATOM   1921  C CB  . THR A  1 242 ? -61.140  10.812  -97.924  1.00 27.35  ? 242 THR A CB  1 
ATOM   1922  O OG1 . THR A  1 242 ? -62.487  10.798  -97.446  1.00 24.77  ? 242 THR A OG1 1 
ATOM   1923  C CG2 . THR A  1 242 ? -60.763  9.528   -98.647  1.00 29.19  ? 242 THR A CG2 1 
ATOM   1924  N N   . LEU A  1 243 ? -60.447  13.545  -96.897  1.00 29.03  ? 243 LEU A N   1 
ATOM   1925  C CA  . LEU A  1 243 ? -60.908  14.871  -96.511  1.00 29.65  ? 243 LEU A CA  1 
ATOM   1926  C C   . LEU A  1 243 ? -62.434  14.904  -96.422  1.00 28.39  ? 243 LEU A C   1 
ATOM   1927  O O   . LEU A  1 243 ? -62.985  15.567  -95.559  1.00 27.96  ? 243 LEU A O   1 
ATOM   1928  C CB  . LEU A  1 243 ? -60.397  15.871  -97.539  1.00 30.15  ? 243 LEU A CB  1 
ATOM   1929  C CG  . LEU A  1 243 ? -58.894  16.139  -97.579  1.00 31.94  ? 243 LEU A CG  1 
ATOM   1930  C CD1 . LEU A  1 243 ? -58.712  17.174  -98.659  1.00 33.27  ? 243 LEU A CD1 1 
ATOM   1931  C CD2 . LEU A  1 243 ? -58.239  16.628  -96.291  1.00 32.20  ? 243 LEU A CD2 1 
ATOM   1932  N N   . LYS A  1 244 ? -63.112  14.186  -97.313  1.00 29.06  ? 244 LYS A N   1 
ATOM   1933  C CA  . LYS A  1 244 ? -64.562  14.075  -97.278  1.00 30.38  ? 244 LYS A CA  1 
ATOM   1934  C C   . LYS A  1 244 ? -65.031  13.305  -96.047  1.00 31.14  ? 244 LYS A C   1 
ATOM   1935  O O   . LYS A  1 244 ? -66.005  13.703  -95.419  1.00 34.64  ? 244 LYS A O   1 
ATOM   1936  C CB  . LYS A  1 244 ? -65.135  13.384  -98.517  1.00 34.92  ? 244 LYS A CB  1 
ATOM   1937  C CG  . LYS A  1 244 ? -66.659  13.494  -98.584  1.00 40.97  ? 244 LYS A CG  1 
ATOM   1938  C CD  . LYS A  1 244 ? -67.322  12.664  -99.680  1.00 50.17  ? 244 LYS A CD  1 
ATOM   1939  C CE  . LYS A  1 244 ? -68.824  12.514  -99.473  1.00 53.45  ? 244 LYS A CE  1 
ATOM   1940  N NZ  . LYS A  1 244 ? -69.441  13.707  -98.867  1.00 53.22  ? 244 LYS A NZ  1 
ATOM   1941  N N   . GLN A  1 245 ? -64.367  12.190  -95.720  1.00 28.86  ? 245 GLN A N   1 
ATOM   1942  C CA  . GLN A  1 245 ? -64.675  11.434  -94.518  1.00 28.51  ? 245 GLN A CA  1 
ATOM   1943  C C   . GLN A  1 245 ? -64.501  12.312  -93.283  1.00 28.07  ? 245 GLN A C   1 
ATOM   1944  O O   . GLN A  1 245 ? -65.271  12.204  -92.325  1.00 25.92  ? 245 GLN A O   1 
ATOM   1945  C CB  . GLN A  1 245 ? -63.795  10.174  -94.420  1.00 27.82  ? 245 GLN A CB  1 
ATOM   1946  C CG  . GLN A  1 245 ? -64.300  9.079   -95.354  1.00 28.20  ? 245 GLN A CG  1 
ATOM   1947  C CD  . GLN A  1 245 ? -63.407  7.865   -95.464  1.00 28.55  ? 245 GLN A CD  1 
ATOM   1948  O OE1 . GLN A  1 245 ? -62.181  7.900   -95.548  1.00 27.34  ? 245 GLN A OE1 1 
ATOM   1949  N NE2 . GLN A  1 245 ? -64.059  6.731   -95.464  1.00 31.24  ? 245 GLN A NE2 1 
ATOM   1950  N N   . GLN A  1 246 ? -63.424  13.116  -93.281  1.00 28.04  ? 246 GLN A N   1 
ATOM   1951  C CA  . GLN A  1 246 ? -63.143  13.977  -92.147  1.00 27.09  ? 246 GLN A CA  1 
ATOM   1952  C C   . GLN A  1 246 ? -64.299  14.966  -91.986  1.00 26.27  ? 246 GLN A C   1 
ATOM   1953  O O   . GLN A  1 246 ? -64.782  15.181  -90.874  1.00 27.06  ? 246 GLN A O   1 
ATOM   1954  C CB  . GLN A  1 246 ? -61.797  14.689  -92.319  1.00 27.65  ? 246 GLN A CB  1 
ATOM   1955  C CG  . GLN A  1 246 ? -61.482  15.666  -91.188  1.00 28.26  ? 246 GLN A CG  1 
ATOM   1956  C CD  . GLN A  1 246 ? -60.238  16.500  -91.444  1.00 27.96  ? 246 GLN A CD  1 
ATOM   1957  O OE1 . GLN A  1 246 ? -60.033  17.003  -92.542  1.00 27.88  ? 246 GLN A OE1 1 
ATOM   1958  N NE2 . GLN A  1 246 ? -59.401  16.672  -90.435  1.00 27.38  ? 246 GLN A NE2 1 
ATOM   1959  N N   . SER A  1 247 ? -64.713  15.587  -93.093  1.00 26.32  ? 247 SER A N   1 
ATOM   1960  C CA  . SER A  1 247 ? -65.728  16.638  -93.061  1.00 28.13  ? 247 SER A CA  1 
ATOM   1961  C C   . SER A  1 247 ? -67.070  16.016  -92.686  1.00 28.35  ? 247 SER A C   1 
ATOM   1962  O O   . SER A  1 247 ? -67.704  16.462  -91.741  1.00 29.63  ? 247 SER A O   1 
ATOM   1963  C CB  . SER A  1 247 ? -65.771  17.401  -94.371  1.00 28.60  ? 247 SER A CB  1 
ATOM   1964  O OG  . SER A  1 247 ? -66.751  18.428  -94.386  1.00 30.51  ? 247 SER A OG  1 
ATOM   1965  N N   . ASP A  1 248 ? -67.470  14.927  -93.350  1.00 29.01  ? 248 ASP A N   1 
ATOM   1966  C CA  . ASP A  1 248 ? -68.744  14.287  -93.008  1.00 28.29  ? 248 ASP A CA  1 
ATOM   1967  C C   . ASP A  1 248 ? -68.724  13.753  -91.579  1.00 27.28  ? 248 ASP A C   1 
ATOM   1968  O O   . ASP A  1 248 ? -69.735  13.827  -90.898  1.00 27.83  ? 248 ASP A O   1 
ATOM   1969  C CB  . ASP A  1 248 ? -69.130  13.165  -93.957  1.00 27.61  ? 248 ASP A CB  1 
ATOM   1970  C CG  . ASP A  1 248 ? -69.384  13.546  -95.410  1.00 27.05  ? 248 ASP A CG  1 
ATOM   1971  O OD1 . ASP A  1 248 ? -69.574  14.736  -95.698  1.00 26.56  ? 248 ASP A OD1 1 
ATOM   1972  O OD2 . ASP A  1 248 ? -69.357  12.639  -96.271  1.00 28.97  ? 248 ASP A OD2 1 
ATOM   1973  N N   . GLY A  1 249 ? -67.580  13.250  -91.102  1.00 26.67  ? 249 GLY A N   1 
ATOM   1974  C CA  . GLY A  1 249 ? -67.465  12.757  -89.728  1.00 26.96  ? 249 GLY A CA  1 
ATOM   1975  C C   . GLY A  1 249 ? -67.648  13.808  -88.618  1.00 29.26  ? 249 GLY A C   1 
ATOM   1976  O O   . GLY A  1 249 ? -68.316  13.545  -87.598  1.00 30.33  ? 249 GLY A O   1 
ATOM   1977  N N   . LEU A  1 250 ? -67.002  14.984  -88.763  1.00 27.81  ? 250 LEU A N   1 
ATOM   1978  C CA  . LEU A  1 250 ? -67.198  16.068  -87.807  1.00 26.54  ? 250 LEU A CA  1 
ATOM   1979  C C   . LEU A  1 250 ? -68.681  16.434  -87.692  1.00 27.29  ? 250 LEU A C   1 
ATOM   1980  O O   . LEU A  1 250 ? -69.140  16.718  -86.592  1.00 27.12  ? 250 LEU A O   1 
ATOM   1981  C CB  . LEU A  1 250 ? -66.330  17.283  -88.144  1.00 27.61  ? 250 LEU A CB  1 
ATOM   1982  C CG  . LEU A  1 250 ? -64.936  17.333  -87.501  1.00 26.76  ? 250 LEU A CG  1 
ATOM   1983  C CD1 . LEU A  1 250 ? -65.034  17.286  -85.986  1.00 27.88  ? 250 LEU A CD1 1 
ATOM   1984  C CD2 . LEU A  1 250 ? -64.076  16.204  -87.948  1.00 25.54  ? 250 LEU A CD2 1 
ATOM   1985  N N   . ILE A  1 251 ? -69.441  16.413  -88.801  1.00 27.23  ? 251 ILE A N   1 
ATOM   1986  C CA  . ILE A  1 251 ? -70.832  16.856  -88.765  1.00 29.00  ? 251 ILE A CA  1 
ATOM   1987  C C   . ILE A  1 251 ? -71.697  15.795  -88.077  1.00 26.36  ? 251 ILE A C   1 
ATOM   1988  O O   . ILE A  1 251 ? -72.547  16.102  -87.254  1.00 26.23  ? 251 ILE A O   1 
ATOM   1989  C CB  . ILE A  1 251 ? -71.362  17.225  -90.169  1.00 32.91  ? 251 ILE A CB  1 
ATOM   1990  C CG1 . ILE A  1 251 ? -70.465  18.281  -90.858  1.00 34.18  ? 251 ILE A CG1 1 
ATOM   1991  C CG2 . ILE A  1 251 ? -72.808  17.709  -90.118  1.00 33.01  ? 251 ILE A CG2 1 
ATOM   1992  C CD1 . ILE A  1 251 ? -70.294  19.556  -90.082  1.00 33.35  ? 251 ILE A CD1 1 
ATOM   1993  N N   . SER A  1 252 ? -71.466  14.530  -88.400  1.00 26.88  ? 252 SER A N   1 
ATOM   1994  C CA  . SER A  1 252 ? -72.088  13.414  -87.709  1.00 25.34  ? 252 SER A CA  1 
ATOM   1995  C C   . SER A  1 252 ? -71.785  13.477  -86.207  1.00 25.37  ? 252 SER A C   1 
ATOM   1996  O O   . SER A  1 252 ? -72.696  13.346  -85.380  1.00 25.05  ? 252 SER A O   1 
ATOM   1997  C CB  . SER A  1 252 ? -71.638  12.122  -88.357  1.00 25.91  ? 252 SER A CB  1 
ATOM   1998  O OG  . SER A  1 252 ? -72.184  11.024  -87.658  1.00 29.62  ? 252 SER A OG  1 
ATOM   1999  N N   . ASN A  1 253 ? -70.502  13.709  -85.840  1.00 25.06  ? 253 ASN A N   1 
ATOM   2000  C CA  . ASN A  1 253 ? -70.118  13.830  -84.441  1.00 23.80  ? 253 ASN A CA  1 
ATOM   2001  C C   . ASN A  1 253 ? -70.901  14.985  -83.786  1.00 26.10  ? 253 ASN A C   1 
ATOM   2002  O O   . ASN A  1 253 ? -71.382  14.856  -82.650  1.00 30.07  ? 253 ASN A O   1 
ATOM   2003  C CB  . ASN A  1 253 ? -68.613  14.053  -84.247  1.00 24.52  ? 253 ASN A CB  1 
ATOM   2004  C CG  . ASN A  1 253 ? -67.689  12.892  -84.592  1.00 23.65  ? 253 ASN A CG  1 
ATOM   2005  O OD1 . ASN A  1 253 ? -66.468  13.024  -84.443  1.00 22.07  ? 253 ASN A OD1 1 
ATOM   2006  N ND2 . ASN A  1 253 ? -68.206  11.769  -85.063  1.00 22.41  ? 253 ASN A ND2 1 
ATOM   2007  N N   . TYR A  1 254 ? -71.070  16.124  -84.485  1.00 24.40  ? 254 TYR A N   1 
ATOM   2008  C CA  . TYR A  1 254 ? -71.576  17.321  -83.819  1.00 24.29  ? 254 TYR A CA  1 
ATOM   2009  C C   . TYR A  1 254 ? -73.032  17.086  -83.407  1.00 23.54  ? 254 TYR A C   1 
ATOM   2010  O O   . TYR A  1 254 ? -73.421  17.406  -82.296  1.00 22.69  ? 254 TYR A O   1 
ATOM   2011  C CB  . TYR A  1 254 ? -71.394  18.560  -84.720  1.00 23.68  ? 254 TYR A CB  1 
ATOM   2012  C CG  . TYR A  1 254 ? -71.157  19.853  -83.967  1.00 23.17  ? 254 TYR A CG  1 
ATOM   2013  C CD1 . TYR A  1 254 ? -72.168  20.466  -83.239  1.00 24.67  ? 254 TYR A CD1 1 
ATOM   2014  C CD2 . TYR A  1 254 ? -69.929  20.473  -83.996  1.00 24.40  ? 254 TYR A CD2 1 
ATOM   2015  C CE1 . TYR A  1 254 ? -71.963  21.670  -82.575  1.00 25.15  ? 254 TYR A CE1 1 
ATOM   2016  C CE2 . TYR A  1 254 ? -69.705  21.663  -83.322  1.00 25.40  ? 254 TYR A CE2 1 
ATOM   2017  C CZ  . TYR A  1 254 ? -70.731  22.292  -82.639  1.00 25.39  ? 254 TYR A CZ  1 
ATOM   2018  O OH  . TYR A  1 254 ? -70.482  23.449  -81.938  1.00 25.92  ? 254 TYR A OH  1 
ATOM   2019  N N   . ARG A  1 255 ? -73.837  16.569  -84.342  1.00 24.43  ? 255 ARG A N   1 
ATOM   2020  C CA  . ARG A  1 255 ? -75.225  16.170  -84.123  1.00 25.97  ? 255 ARG A CA  1 
ATOM   2021  C C   . ARG A  1 255 ? -75.337  15.157  -82.976  1.00 26.66  ? 255 ARG A C   1 
ATOM   2022  O O   . ARG A  1 255 ? -76.132  15.346  -82.045  1.00 23.66  ? 255 ARG A O   1 
ATOM   2023  C CB  . ARG A  1 255 ? -75.742  15.590  -85.453  1.00 27.39  ? 255 ARG A CB  1 
ATOM   2024  C CG  . ARG A  1 255 ? -77.103  14.921  -85.451  1.00 27.27  ? 255 ARG A CG  1 
ATOM   2025  C CD  . ARG A  1 255 ? -78.218  15.974  -85.391  1.00 27.33  ? 255 ARG A CD  1 
ATOM   2026  N NE  . ARG A  1 255 ? -78.540  16.319  -84.012  1.00 26.37  ? 255 ARG A NE  1 
ATOM   2027  C CZ  . ARG A  1 255 ? -78.715  17.503  -83.489  1.00 27.58  ? 255 ARG A CZ  1 
ATOM   2028  N NH1 . ARG A  1 255 ? -78.733  18.572  -84.260  1.00 29.50  ? 255 ARG A NH1 1 
ATOM   2029  N NH2 . ARG A  1 255 ? -78.955  17.612  -82.196  1.00 27.87  ? 255 ARG A NH2 1 
ATOM   2030  N N   . ASP A  1 256 ? -74.493  14.107  -83.027  1.00 27.54  ? 256 ASP A N   1 
ATOM   2031  C CA  . ASP A  1 256 ? -74.588  12.998  -82.084  1.00 27.25  ? 256 ASP A CA  1 
ATOM   2032  C C   . ASP A  1 256 ? -74.351  13.492  -80.663  1.00 26.02  ? 256 ASP A C   1 
ATOM   2033  O O   . ASP A  1 256 ? -75.032  13.081  -79.722  1.00 26.51  ? 256 ASP A O   1 
ATOM   2034  C CB  . ASP A  1 256 ? -73.592  11.898  -82.417  1.00 27.70  ? 256 ASP A CB  1 
ATOM   2035  C CG  . ASP A  1 256 ? -74.023  11.040  -83.587  1.00 29.98  ? 256 ASP A CG  1 
ATOM   2036  O OD1 . ASP A  1 256 ? -75.064  11.408  -84.143  1.00 29.77  ? 256 ASP A OD1 1 
ATOM   2037  O OD2 . ASP A  1 256 ? -73.331  10.012  -83.913  1.00 32.87  ? 256 ASP A OD2 1 
ATOM   2038  N N   . LEU A  1 257 ? -73.335  14.336  -80.501  1.00 24.59  ? 257 LEU A N   1 
ATOM   2039  C CA  . LEU A  1 257 ? -72.918  14.732  -79.170  1.00 25.30  ? 257 LEU A CA  1 
ATOM   2040  C C   . LEU A  1 257 ? -73.922  15.742  -78.618  1.00 25.81  ? 257 LEU A C   1 
ATOM   2041  O O   . LEU A  1 257 ? -74.197  15.763  -77.421  1.00 27.22  ? 257 LEU A O   1 
ATOM   2042  C CB  . LEU A  1 257 ? -71.489  15.283  -79.250  1.00 25.18  ? 257 LEU A CB  1 
ATOM   2043  C CG  . LEU A  1 257 ? -70.416  14.235  -79.552  1.00 25.05  ? 257 LEU A CG  1 
ATOM   2044  C CD1 . LEU A  1 257 ? -69.061  14.775  -79.993  1.00 23.52  ? 257 LEU A CD1 1 
ATOM   2045  C CD2 . LEU A  1 257 ? -70.254  13.327  -78.305  1.00 25.69  ? 257 LEU A CD2 1 
ATOM   2046  N N   . ILE A  1 258 ? -74.496  16.595  -79.479  1.00 27.11  ? 258 ILE A N   1 
ATOM   2047  C CA  . ILE A  1 258 ? -75.598  17.424  -79.018  1.00 26.91  ? 258 ILE A CA  1 
ATOM   2048  C C   . ILE A  1 258 ? -76.699  16.491  -78.524  1.00 26.79  ? 258 ILE A C   1 
ATOM   2049  O O   . ILE A  1 258 ? -77.315  16.752  -77.480  1.00 27.74  ? 258 ILE A O   1 
ATOM   2050  C CB  . ILE A  1 258 ? -76.099  18.422  -80.078  1.00 28.14  ? 258 ILE A CB  1 
ATOM   2051  C CG1 . ILE A  1 258 ? -75.019  19.475  -80.399  1.00 29.83  ? 258 ILE A CG1 1 
ATOM   2052  C CG2 . ILE A  1 258 ? -77.406  19.105  -79.631  1.00 28.82  ? 258 ILE A CG2 1 
ATOM   2053  C CD1 . ILE A  1 258 ? -75.343  20.399  -81.577  1.00 29.64  ? 258 ILE A CD1 1 
ATOM   2054  N N   . ASP A  1 259 ? -76.942  15.403  -79.270  1.00 26.93  ? 259 ASP A N   1 
ATOM   2055  C CA  . ASP A  1 259 ? -78.037  14.486  -78.943  1.00 28.64  ? 259 ASP A CA  1 
ATOM   2056  C C   . ASP A  1 259 ? -77.771  13.761  -77.627  1.00 27.90  ? 259 ASP A C   1 
ATOM   2057  O O   . ASP A  1 259 ? -78.725  13.269  -77.028  1.00 29.12  ? 259 ASP A O   1 
ATOM   2058  C CB  . ASP A  1 259 ? -78.324  13.453  -80.022  1.00 27.96  ? 259 ASP A CB  1 
ATOM   2059  C CG  . ASP A  1 259 ? -78.766  14.065  -81.330  1.00 28.43  ? 259 ASP A CG  1 
ATOM   2060  O OD1 . ASP A  1 259 ? -79.475  15.117  -81.244  1.00 28.68  ? 259 ASP A OD1 1 
ATOM   2061  O OD2 . ASP A  1 259 ? -78.370  13.509  -82.395  1.00 27.36  ? 259 ASP A OD2 1 
ATOM   2062  N N   . ALA A  1 260 ? -76.507  13.751  -77.176  1.00 25.63  ? 260 ALA A N   1 
ATOM   2063  C CA  . ALA A  1 260 ? -76.150  13.135  -75.901  1.00 27.48  ? 260 ALA A CA  1 
ATOM   2064  C C   . ALA A  1 260 ? -76.277  14.088  -74.714  1.00 27.98  ? 260 ALA A C   1 
ATOM   2065  O O   . ALA A  1 260 ? -76.037  13.673  -73.586  1.00 31.64  ? 260 ALA A O   1 
ATOM   2066  C CB  . ALA A  1 260 ? -74.729  12.566  -75.986  1.00 28.04  ? 260 ALA A CB  1 
ATOM   2067  N N   . GLY A  1 261 ? -76.630  15.352  -74.973  1.00 27.75  ? 261 GLY A N   1 
ATOM   2068  C CA  . GLY A  1 261 ? -76.827  16.358  -73.946  1.00 28.80  ? 261 GLY A CA  1 
ATOM   2069  C C   . GLY A  1 261 ? -75.742  17.443  -73.906  1.00 28.56  ? 261 GLY A C   1 
ATOM   2070  O O   . GLY A  1 261 ? -75.758  18.277  -73.018  1.00 30.91  ? 261 GLY A O   1 
ATOM   2071  N N   . ALA A  1 262 ? -74.769  17.447  -74.817  1.00 28.15  ? 262 ALA A N   1 
ATOM   2072  C CA  . ALA A  1 262 ? -73.705  18.462  -74.748  1.00 27.69  ? 262 ALA A CA  1 
ATOM   2073  C C   . ALA A  1 262 ? -74.310  19.835  -74.969  1.00 28.04  ? 262 ALA A C   1 
ATOM   2074  O O   . ALA A  1 262 ? -75.152  19.975  -75.839  1.00 29.48  ? 262 ALA A O   1 
ATOM   2075  C CB  . ALA A  1 262 ? -72.607  18.221  -75.778  1.00 26.24  ? 262 ALA A CB  1 
ATOM   2076  N N   . VAL A  1 263 ? -73.901  20.818  -74.157  1.00 29.64  ? 263 VAL A N   1 
ATOM   2077  C CA  . VAL A  1 263 ? -74.225  22.223  -74.373  1.00 28.37  ? 263 VAL A CA  1 
ATOM   2078  C C   . VAL A  1 263 ? -72.945  23.023  -74.620  1.00 29.79  ? 263 VAL A C   1 
ATOM   2079  O O   . VAL A  1 263 ? -72.927  24.256  -74.518  1.00 29.00  ? 263 VAL A O   1 
ATOM   2080  C CB  . VAL A  1 263 ? -74.994  22.784  -73.166  1.00 30.14  ? 263 VAL A CB  1 
ATOM   2081  C CG1 . VAL A  1 263 ? -76.382  22.149  -73.062  1.00 34.52  ? 263 VAL A CG1 1 
ATOM   2082  C CG2 . VAL A  1 263 ? -74.227  22.638  -71.867  1.00 28.60  ? 263 VAL A CG2 1 
ATOM   2083  N N   . GLY A  1 264 ? -71.862  22.305  -74.932  1.00 28.14  ? 264 GLY A N   1 
ATOM   2084  C CA  . GLY A  1 264 ? -70.631  22.951  -75.325  1.00 29.11  ? 264 GLY A CA  1 
ATOM   2085  C C   . GLY A  1 264 ? -69.821  21.934  -76.105  1.00 28.56  ? 264 GLY A C   1 
ATOM   2086  O O   . GLY A  1 264 ? -69.870  20.752  -75.777  1.00 27.80  ? 264 GLY A O   1 
ATOM   2087  N N   . MET A  1 265 ? -69.130  22.420  -77.144  1.00 27.51  ? 265 MET A N   1 
ATOM   2088  C CA  . MET A  1 265 ? -68.487  21.556  -78.118  1.00 26.33  ? 265 MET A CA  1 
ATOM   2089  C C   . MET A  1 265 ? -67.097  22.098  -78.460  1.00 25.70  ? 265 MET A C   1 
ATOM   2090  O O   . MET A  1 265 ? -66.951  23.277  -78.737  1.00 23.91  ? 265 MET A O   1 
ATOM   2091  C CB  . MET A  1 265 ? -69.390  21.439  -79.347  1.00 26.09  ? 265 MET A CB  1 
ATOM   2092  C CG  . MET A  1 265 ? -70.749  20.805  -79.010  1.00 26.97  ? 265 MET A CG  1 
ATOM   2093  S SD  . MET A  1 265 ? -70.641  19.016  -78.752  1.00 25.93  ? 265 MET A SD  1 
ATOM   2094  C CE  . MET A  1 265 ? -70.587  18.538  -80.474  1.00 23.84  ? 265 MET A CE  1 
ATOM   2095  N N   . CYS A  1 266 ? -66.083  21.219  -78.388  1.00 25.93  ? 266 CYS A N   1 
ATOM   2096  C CA  . CYS A  1 266 ? -64.712  21.570  -78.737  1.00 25.59  ? 266 CYS A CA  1 
ATOM   2097  C C   . CYS A  1 266 ? -64.256  20.594  -79.815  1.00 23.95  ? 266 CYS A C   1 
ATOM   2098  O O   . CYS A  1 266 ? -63.427  19.748  -79.564  1.00 23.31  ? 266 CYS A O   1 
ATOM   2099  C CB  . CYS A  1 266 ? -63.722  21.528  -77.565  1.00 25.77  ? 266 CYS A CB  1 
ATOM   2100  S SG  . CYS A  1 266 ? -64.203  22.471  -76.090  1.00 28.74  ? 266 CYS A SG  1 
ATOM   2101  N N   . PRO A  1 267 ? -64.711  20.697  -81.076  1.00 24.44  ? 267 PRO A N   1 
ATOM   2102  C CA  . PRO A  1 267 ? -64.153  19.867  -82.137  1.00 24.50  ? 267 PRO A CA  1 
ATOM   2103  C C   . PRO A  1 267 ? -62.627  19.949  -82.092  1.00 25.69  ? 267 PRO A C   1 
ATOM   2104  O O   . PRO A  1 267 ? -62.052  21.016  -81.821  1.00 28.80  ? 267 PRO A O   1 
ATOM   2105  C CB  . PRO A  1 267 ? -64.727  20.461  -83.422  1.00 24.63  ? 267 PRO A CB  1 
ATOM   2106  C CG  . PRO A  1 267 ? -65.184  21.854  -83.022  1.00 25.84  ? 267 PRO A CG  1 
ATOM   2107  C CD  . PRO A  1 267 ? -65.648  21.703  -81.580  1.00 25.92  ? 267 PRO A CD  1 
ATOM   2108  N N   . PHE A  1 268 ? -61.985  18.821  -82.405  1.00 25.37  ? 268 PHE A N   1 
ATOM   2109  C CA  . PHE A  1 268 ? -60.535  18.717  -82.485  1.00 25.40  ? 268 PHE A CA  1 
ATOM   2110  C C   . PHE A  1 268 ? -60.098  18.620  -83.944  1.00 26.42  ? 268 PHE A C   1 
ATOM   2111  O O   . PHE A  1 268 ? -60.432  17.610  -84.592  1.00 26.03  ? 268 PHE A O   1 
ATOM   2112  C CB  . PHE A  1 268 ? -60.037  17.480  -81.729  1.00 24.87  ? 268 PHE A CB  1 
ATOM   2113  C CG  . PHE A  1 268 ? -58.519  17.364  -81.600  1.00 24.18  ? 268 PHE A CG  1 
ATOM   2114  C CD1 . PHE A  1 268 ? -57.759  16.740  -82.582  1.00 24.70  ? 268 PHE A CD1 1 
ATOM   2115  C CD2 . PHE A  1 268 ? -57.855  17.884  -80.495  1.00 24.24  ? 268 PHE A CD2 1 
ATOM   2116  C CE1 . PHE A  1 268 ? -56.382  16.617  -82.433  1.00 26.48  ? 268 PHE A CE1 1 
ATOM   2117  C CE2 . PHE A  1 268 ? -56.467  17.779  -80.350  1.00 24.63  ? 268 PHE A CE2 1 
ATOM   2118  C CZ  . PHE A  1 268 ? -55.735  17.138  -81.312  1.00 26.27  ? 268 PHE A CZ  1 
ATOM   2119  N N   . TYR A  1 269 ? -59.345  19.619  -84.479  1.00 26.30  ? 269 TYR A N   1 
ATOM   2120  C CA  . TYR A  1 269 ? -58.941  20.883  -83.860  1.00 26.57  ? 269 TYR A CA  1 
ATOM   2121  C C   . TYR A  1 269 ? -58.415  21.774  -84.979  1.00 24.85  ? 269 TYR A C   1 
ATOM   2122  O O   . TYR A  1 269 ? -58.453  21.371  -86.131  1.00 27.00  ? 269 TYR A O   1 
ATOM   2123  C CB  . TYR A  1 269 ? -57.876  20.786  -82.753  1.00 27.69  ? 269 TYR A CB  1 
ATOM   2124  C CG  . TYR A  1 269 ? -56.453  20.367  -83.111  1.00 27.78  ? 269 TYR A CG  1 
ATOM   2125  C CD1 . TYR A  1 269 ? -56.153  19.664  -84.265  1.00 27.65  ? 269 TYR A CD1 1 
ATOM   2126  C CD2 . TYR A  1 269 ? -55.400  20.619  -82.231  1.00 29.19  ? 269 TYR A CD2 1 
ATOM   2127  C CE1 . TYR A  1 269 ? -54.861  19.235  -84.528  1.00 28.30  ? 269 TYR A CE1 1 
ATOM   2128  C CE2 . TYR A  1 269 ? -54.112  20.173  -82.470  1.00 27.67  ? 269 TYR A CE2 1 
ATOM   2129  C CZ  . TYR A  1 269 ? -53.833  19.485  -83.635  1.00 28.44  ? 269 TYR A CZ  1 
ATOM   2130  O OH  . TYR A  1 269 ? -52.562  19.040  -83.919  1.00 27.25  ? 269 TYR A OH  1 
ATOM   2131  N N   . TYR A  1 270 ? -57.816  22.921  -84.656  1.00 25.87  ? 270 TYR A N   1 
ATOM   2132  C CA  . TYR A  1 270 ? -57.580  23.965  -85.661  1.00 26.32  ? 270 TYR A CA  1 
ATOM   2133  C C   . TYR A  1 270 ? -56.583  23.545  -86.744  1.00 28.19  ? 270 TYR A C   1 
ATOM   2134  O O   . TYR A  1 270 ? -56.864  23.740  -87.927  1.00 27.97  ? 270 TYR A O   1 
ATOM   2135  C CB  . TYR A  1 270 ? -57.093  25.241  -84.968  1.00 26.95  ? 270 TYR A CB  1 
ATOM   2136  C CG  . TYR A  1 270 ? -56.535  26.347  -85.859  1.00 25.81  ? 270 TYR A CG  1 
ATOM   2137  C CD1 . TYR A  1 270 ? -57.338  27.023  -86.764  1.00 25.50  ? 270 TYR A CD1 1 
ATOM   2138  C CD2 . TYR A  1 270 ? -55.226  26.769  -85.723  1.00 25.93  ? 270 TYR A CD2 1 
ATOM   2139  C CE1 . TYR A  1 270 ? -56.831  28.045  -87.551  1.00 25.74  ? 270 TYR A CE1 1 
ATOM   2140  C CE2 . TYR A  1 270 ? -54.707  27.810  -86.491  1.00 26.54  ? 270 TYR A CE2 1 
ATOM   2141  C CZ  . TYR A  1 270 ? -55.511  28.442  -87.417  1.00 25.51  ? 270 TYR A CZ  1 
ATOM   2142  O OH  . TYR A  1 270 ? -55.007  29.453  -88.172  1.00 25.47  ? 270 TYR A OH  1 
ATOM   2143  N N   . ALA A  1 271 ? -55.397  23.026  -86.358  1.00 27.32  ? 271 ALA A N   1 
ATOM   2144  C CA  . ALA A  1 271 ? -54.367  22.777  -87.358  1.00 27.56  ? 271 ALA A CA  1 
ATOM   2145  C C   . ALA A  1 271 ? -53.382  21.680  -86.928  1.00 25.90  ? 271 ALA A C   1 
ATOM   2146  O O   . ALA A  1 271 ? -53.026  21.542  -85.764  1.00 25.43  ? 271 ALA A O   1 
ATOM   2147  C CB  . ALA A  1 271 ? -53.638  24.067  -87.706  1.00 27.72  ? 271 ALA A CB  1 
ATOM   2148  N N   . ASP A  1 272 ? -52.894  20.954  -87.930  1.00 25.75  ? 272 ASP A N   1 
ATOM   2149  C CA  . ASP A  1 272 ? -51.924  19.876  -87.750  1.00 26.98  ? 272 ASP A CA  1 
ATOM   2150  C C   . ASP A  1 272 ? -50.701  20.295  -86.940  1.00 26.31  ? 272 ASP A C   1 
ATOM   2151  O O   . ASP A  1 272 ? -50.187  21.431  -87.045  1.00 28.26  ? 272 ASP A O   1 
ATOM   2152  C CB  . ASP A  1 272 ? -51.396  19.355  -89.078  1.00 27.60  ? 272 ASP A CB  1 
ATOM   2153  C CG  . ASP A  1 272 ? -52.418  18.634  -89.946  1.00 25.94  ? 272 ASP A CG  1 
ATOM   2154  O OD1 . ASP A  1 272 ? -53.484  18.304  -89.412  1.00 24.10  ? 272 ASP A OD1 1 
ATOM   2155  O OD2 . ASP A  1 272 ? -52.121  18.407  -91.144  1.00 27.88  ? 272 ASP A OD2 1 
ATOM   2156  N N   . GLY A  1 273 ? -50.293  19.344  -86.101  1.00 25.58  ? 273 GLY A N   1 
ATOM   2157  C CA  . GLY A  1 273 ? -49.112  19.461  -85.273  1.00 27.30  ? 273 GLY A CA  1 
ATOM   2158  C C   . GLY A  1 273 ? -48.149  18.344  -85.651  1.00 28.50  ? 273 GLY A C   1 
ATOM   2159  O O   . GLY A  1 273 ? -48.353  17.192  -85.276  1.00 29.92  ? 273 GLY A O   1 
ATOM   2160  N N   . TRP A  1 274 ? -47.171  18.674  -86.495  1.00 27.41  ? 274 TRP A N   1 
ATOM   2161  C CA  . TRP A  1 274 ? -46.254  17.660  -86.968  1.00 27.69  ? 274 TRP A CA  1 
ATOM   2162  C C   . TRP A  1 274 ? -45.498  17.015  -85.807  1.00 29.51  ? 274 TRP A C   1 
ATOM   2163  O O   . TRP A  1 274 ? -45.040  15.882  -85.907  1.00 32.09  ? 274 TRP A O   1 
ATOM   2164  C CB  . TRP A  1 274 ? -45.272  18.289  -87.948  1.00 27.04  ? 274 TRP A CB  1 
ATOM   2165  C CG  . TRP A  1 274 ? -45.908  18.761  -89.218  1.00 25.68  ? 274 TRP A CG  1 
ATOM   2166  C CD1 . TRP A  1 274 ? -47.229  18.976  -89.494  1.00 24.30  ? 274 TRP A CD1 1 
ATOM   2167  C CD2 . TRP A  1 274 ? -45.180  19.049  -90.425  1.00 25.83  ? 274 TRP A CD2 1 
ATOM   2168  N NE1 . TRP A  1 274 ? -47.365  19.359  -90.805  1.00 24.09  ? 274 TRP A NE1 1 
ATOM   2169  C CE2 . TRP A  1 274 ? -46.132  19.423  -91.386  1.00 25.08  ? 274 TRP A CE2 1 
ATOM   2170  C CE3 . TRP A  1 274 ? -43.821  19.001  -90.781  1.00 27.00  ? 274 TRP A CE3 1 
ATOM   2171  C CZ2 . TRP A  1 274 ? -45.748  19.749  -92.678  1.00 27.18  ? 274 TRP A CZ2 1 
ATOM   2172  C CZ3 . TRP A  1 274 ? -43.449  19.284  -92.070  1.00 27.22  ? 274 TRP A CZ3 1 
ATOM   2173  C CH2 . TRP A  1 274 ? -44.406  19.669  -93.000  1.00 27.99  ? 274 TRP A CH2 1 
ATOM   2174  N N   . TRP A  1 275 ? -45.337  17.758  -84.713  1.00 29.90  ? 275 TRP A N   1 
ATOM   2175  C CA  . TRP A  1 275 ? -44.603  17.292  -83.555  1.00 29.23  ? 275 TRP A CA  1 
ATOM   2176  C C   . TRP A  1 275 ? -45.209  16.025  -82.971  1.00 29.25  ? 275 TRP A C   1 
ATOM   2177  O O   . TRP A  1 275 ? -44.519  15.312  -82.266  1.00 27.00  ? 275 TRP A O   1 
ATOM   2178  C CB  . TRP A  1 275 ? -44.570  18.404  -82.502  1.00 29.78  ? 275 TRP A CB  1 
ATOM   2179  C CG  . TRP A  1 275 ? -45.864  18.709  -81.777  1.00 28.60  ? 275 TRP A CG  1 
ATOM   2180  C CD1 . TRP A  1 275 ? -46.778  19.691  -82.066  1.00 28.30  ? 275 TRP A CD1 1 
ATOM   2181  C CD2 . TRP A  1 275 ? -46.308  18.109  -80.540  1.00 27.09  ? 275 TRP A CD2 1 
ATOM   2182  N NE1 . TRP A  1 275 ? -47.785  19.707  -81.133  1.00 26.46  ? 275 TRP A NE1 1 
ATOM   2183  C CE2 . TRP A  1 275 ? -47.511  18.768  -80.175  1.00 26.55  ? 275 TRP A CE2 1 
ATOM   2184  C CE3 . TRP A  1 275 ? -45.805  17.086  -79.715  1.00 26.50  ? 275 TRP A CE3 1 
ATOM   2185  C CZ2 . TRP A  1 275 ? -48.217  18.418  -79.027  1.00 25.51  ? 275 TRP A CZ2 1 
ATOM   2186  C CZ3 . TRP A  1 275 ? -46.510  16.731  -78.592  1.00 24.84  ? 275 TRP A CZ3 1 
ATOM   2187  C CH2 . TRP A  1 275 ? -47.690  17.395  -78.257  1.00 25.71  ? 275 TRP A CH2 1 
ATOM   2188  N N   . LYS A  1 276 ? -46.506  15.775  -83.235  1.00 30.43  ? 276 LYS A N   1 
ATOM   2189  C CA  . LYS A  1 276 ? -47.295  14.901  -82.377  1.00 29.10  ? 276 LYS A CA  1 
ATOM   2190  C C   . LYS A  1 276 ? -46.955  13.435  -82.619  1.00 31.13  ? 276 LYS A C   1 
ATOM   2191  O O   . LYS A  1 276 ? -47.217  12.610  -81.757  1.00 32.52  ? 276 LYS A O   1 
ATOM   2192  C CB  . LYS A  1 276 ? -48.796  15.152  -82.538  1.00 27.76  ? 276 LYS A CB  1 
ATOM   2193  C CG  . LYS A  1 276 ? -49.249  16.525  -82.014  1.00 28.33  ? 276 LYS A CG  1 
ATOM   2194  C CD  . LYS A  1 276 ? -50.662  16.927  -82.421  1.00 27.17  ? 276 LYS A CD  1 
ATOM   2195  C CE  . LYS A  1 276 ? -51.727  15.987  -81.940  1.00 25.22  ? 276 LYS A CE  1 
ATOM   2196  N NZ  . LYS A  1 276 ? -51.953  16.199  -80.510  1.00 25.54  ? 276 LYS A NZ  1 
ATOM   2197  N N   . GLY A  1 277 ? -46.386  13.102  -83.776  1.00 32.04  ? 277 GLY A N   1 
ATOM   2198  C CA  . GLY A  1 277 ? -45.989  11.728  -84.031  1.00 33.88  ? 277 GLY A CA  1 
ATOM   2199  C C   . GLY A  1 277 ? -44.509  11.461  -83.749  1.00 35.85  ? 277 GLY A C   1 
ATOM   2200  O O   . GLY A  1 277 ? -44.076  10.361  -84.009  1.00 36.47  ? 277 GLY A O   1 
ATOM   2201  N N   . GLY A  1 278 ? -43.723  12.457  -83.278  1.00 39.11  ? 278 GLY A N   1 
ATOM   2202  C CA  . GLY A  1 278 ? -42.373  12.208  -82.779  1.00 36.67  ? 278 GLY A CA  1 
ATOM   2203  C C   . GLY A  1 278 ? -41.283  13.128  -83.342  1.00 37.97  ? 278 GLY A C   1 
ATOM   2204  O O   . GLY A  1 278 ? -40.276  13.367  -82.661  1.00 38.01  ? 278 GLY A O   1 
ATOM   2205  N N   . GLU A  1 279 ? -41.407  13.545  -84.611  1.00 36.63  ? 279 GLU A N   1 
ATOM   2206  C CA  . GLU A  1 279 ? -40.382  14.355  -85.257  1.00 36.83  ? 279 GLU A CA  1 
ATOM   2207  C C   . GLU A  1 279 ? -41.018  15.610  -85.849  1.00 35.93  ? 279 GLU A C   1 
ATOM   2208  O O   . GLU A  1 279 ? -41.636  15.560  -86.894  1.00 36.44  ? 279 GLU A O   1 
ATOM   2209  C CB  . GLU A  1 279 ? -39.630  13.584  -86.341  1.00 37.67  ? 279 GLU A CB  1 
ATOM   2210  C CG  . GLU A  1 279 ? -38.633  14.434  -87.123  1.00 40.14  ? 279 GLU A CG  1 
ATOM   2211  C CD  . GLU A  1 279 ? -37.721  15.346  -86.300  1.00 44.90  ? 279 GLU A CD  1 
ATOM   2212  O OE1 . GLU A  1 279 ? -37.052  14.863  -85.363  1.00 50.28  ? 279 GLU A OE1 1 
ATOM   2213  O OE2 . GLU A  1 279 ? -37.630  16.560  -86.603  1.00 50.19  ? 279 GLU A OE2 1 
ATOM   2214  N N   . LYS A  1 280 ? -40.800  16.760  -85.211  1.00 35.53  ? 280 LYS A N   1 
ATOM   2215  C CA  . LYS A  1 280 ? -41.527  17.977  -85.537  1.00 33.45  ? 280 LYS A CA  1 
ATOM   2216  C C   . LYS A  1 280 ? -41.212  18.560  -86.923  1.00 32.67  ? 280 LYS A C   1 
ATOM   2217  O O   . LYS A  1 280 ? -41.974  19.403  -87.423  1.00 31.41  ? 280 LYS A O   1 
ATOM   2218  C CB  . LYS A  1 280 ? -41.163  18.987  -84.445  1.00 34.93  ? 280 LYS A CB  1 
ATOM   2219  C CG  . LYS A  1 280 ? -39.698  19.330  -84.446  1.00 35.36  ? 280 LYS A CG  1 
ATOM   2220  C CD  . LYS A  1 280 ? -39.305  20.133  -83.238  1.00 38.11  ? 280 LYS A CD  1 
ATOM   2221  C CE  . LYS A  1 280 ? -37.875  20.567  -83.376  1.00 41.88  ? 280 LYS A CE  1 
ATOM   2222  N NZ  . LYS A  1 280 ? -37.430  20.807  -82.012  1.00 44.68  ? 280 LYS A NZ  1 
ATOM   2223  N N   . SER A  1 281 ? -40.087  18.160  -87.527  1.00 33.49  ? 281 SER A N   1 
ATOM   2224  C CA  . SER A  1 281 ? -39.618  18.725  -88.799  1.00 35.82  ? 281 SER A CA  1 
ATOM   2225  C C   . SER A  1 281 ? -40.093  17.949  -90.024  1.00 35.10  ? 281 SER A C   1 
ATOM   2226  O O   . SER A  1 281 ? -39.804  18.326  -91.168  1.00 33.43  ? 281 SER A O   1 
ATOM   2227  C CB  . SER A  1 281 ? -38.114  18.787  -88.823  1.00 37.26  ? 281 SER A CB  1 
ATOM   2228  O OG  . SER A  1 281 ? -37.717  19.844  -87.958  1.00 40.20  ? 281 SER A OG  1 
ATOM   2229  N N   . ASP A  1 282 ? -40.758  16.828  -89.744  1.00 35.43  ? 282 ASP A N   1 
ATOM   2230  C CA  . ASP A  1 282 ? -41.178  15.888  -90.750  1.00 38.35  ? 282 ASP A CA  1 
ATOM   2231  C C   . ASP A  1 282 ? -42.677  15.698  -90.569  1.00 34.58  ? 282 ASP A C   1 
ATOM   2232  O O   . ASP A  1 282 ? -43.185  15.714  -89.444  1.00 32.86  ? 282 ASP A O   1 
ATOM   2233  C CB  . ASP A  1 282 ? -40.338  14.624  -90.644  1.00 44.76  ? 282 ASP A CB  1 
ATOM   2234  C CG  . ASP A  1 282 ? -40.771  13.525  -91.593  1.00 53.27  ? 282 ASP A CG  1 
ATOM   2235  O OD1 . ASP A  1 282 ? -40.361  13.588  -92.783  1.00 59.38  ? 282 ASP A OD1 1 
ATOM   2236  O OD2 . ASP A  1 282 ? -41.567  12.660  -91.151  1.00 59.45  ? 282 ASP A OD2 1 
ATOM   2237  N N   . HIS A  1 283 ? -43.392  15.588  -91.687  1.00 33.54  ? 283 HIS A N   1 
ATOM   2238  C CA  . HIS A  1 283 ? -44.824  15.315  -91.628  1.00 32.72  ? 283 HIS A CA  1 
ATOM   2239  C C   . HIS A  1 283 ? -44.982  13.853  -92.020  1.00 32.22  ? 283 HIS A C   1 
ATOM   2240  O O   . HIS A  1 283 ? -44.966  13.527  -93.202  1.00 32.09  ? 283 HIS A O   1 
ATOM   2241  C CB  . HIS A  1 283 ? -45.624  16.273  -92.520  1.00 30.29  ? 283 HIS A CB  1 
ATOM   2242  C CG  . HIS A  1 283 ? -47.062  16.389  -92.143  1.00 29.02  ? 283 HIS A CG  1 
ATOM   2243  N ND1 . HIS A  1 283 ? -48.031  16.838  -93.018  1.00 28.73  ? 283 HIS A ND1 1 
ATOM   2244  C CD2 . HIS A  1 283 ? -47.699  16.119  -90.999  1.00 27.32  ? 283 HIS A CD2 1 
ATOM   2245  C CE1 . HIS A  1 283 ? -49.215  16.794  -92.410  1.00 27.49  ? 283 HIS A CE1 1 
ATOM   2246  N NE2 . HIS A  1 283 ? -49.040  16.371  -91.184  1.00 26.36  ? 283 HIS A NE2 1 
ATOM   2247  N N   . SER A  1 284 ? -45.016  12.987  -91.009  1.00 31.91  ? 284 SER A N   1 
ATOM   2248  C CA  . SER A  1 284 ? -44.944  11.546  -91.223  1.00 30.99  ? 284 SER A CA  1 
ATOM   2249  C C   . SER A  1 284 ? -46.230  11.039  -91.897  1.00 28.98  ? 284 SER A C   1 
ATOM   2250  O O   . SER A  1 284 ? -47.338  11.356  -91.501  1.00 28.77  ? 284 SER A O   1 
ATOM   2251  C CB  . SER A  1 284 ? -44.647  10.856  -89.916  1.00 30.95  ? 284 SER A CB  1 
ATOM   2252  O OG  . SER A  1 284 ? -45.065  9.499   -89.981  1.00 33.17  ? 284 SER A OG  1 
ATOM   2253  N N   . LEU A  1 285 ? -46.092  10.263  -92.963  1.00 29.99  ? 285 LEU A N   1 
ATOM   2254  C CA  . LEU A  1 285 ? -47.222  9.744   -93.718  1.00 29.61  ? 285 LEU A CA  1 
ATOM   2255  C C   . LEU A  1 285 ? -48.102  8.806   -92.890  1.00 28.75  ? 285 LEU A C   1 
ATOM   2256  O O   . LEU A  1 285 ? -49.273  8.639   -93.210  1.00 28.29  ? 285 LEU A O   1 
ATOM   2257  C CB  . LEU A  1 285 ? -46.720  9.047   -94.985  1.00 31.21  ? 285 LEU A CB  1 
ATOM   2258  C CG  . LEU A  1 285 ? -45.768  9.859   -95.882  1.00 34.26  ? 285 LEU A CG  1 
ATOM   2259  C CD1 . LEU A  1 285 ? -45.358  9.113   -97.169  1.00 35.05  ? 285 LEU A CD1 1 
ATOM   2260  C CD2 . LEU A  1 285 ? -46.349  11.231  -96.235  1.00 33.52  ? 285 LEU A CD2 1 
ATOM   2261  N N   . ASN A  1 286 ? -47.575  8.225   -91.808  1.00 29.25  ? 286 ASN A N   1 
ATOM   2262  C CA  . ASN A  1 286 ? -48.275  7.138   -91.137  1.00 29.27  ? 286 ASN A CA  1 
ATOM   2263  C C   . ASN A  1 286 ? -48.499  7.401   -89.664  1.00 27.54  ? 286 ASN A C   1 
ATOM   2264  O O   . ASN A  1 286 ? -48.734  6.457   -88.940  1.00 27.40  ? 286 ASN A O   1 
ATOM   2265  C CB  . ASN A  1 286 ? -47.554  5.806   -91.297  1.00 31.06  ? 286 ASN A CB  1 
ATOM   2266  C CG  . ASN A  1 286 ? -46.240  5.730   -90.553  1.00 32.93  ? 286 ASN A CG  1 
ATOM   2267  O OD1 . ASN A  1 286 ? -45.674  6.719   -90.085  1.00 33.37  ? 286 ASN A OD1 1 
ATOM   2268  N ND2 . ASN A  1 286 ? -45.782  4.513   -90.358  1.00 35.92  ? 286 ASN A ND2 1 
ATOM   2269  N N   . GLN A  1 287 ? -48.545  8.672   -89.265  1.00 29.12  ? 287 GLN A N   1 
ATOM   2270  C CA  . GLN A  1 287 ? -48.871  9.066   -87.904  1.00 28.92  ? 287 GLN A CA  1 
ATOM   2271  C C   . GLN A  1 287 ? -50.230  9.756   -87.885  1.00 28.04  ? 287 GLN A C   1 
ATOM   2272  O O   . GLN A  1 287 ? -50.323  10.953  -88.139  1.00 29.31  ? 287 GLN A O   1 
ATOM   2273  C CB  . GLN A  1 287 ? -47.782  10.031  -87.422  1.00 29.61  ? 287 GLN A CB  1 
ATOM   2274  C CG  . GLN A  1 287 ? -46.454  9.345   -87.125  1.00 30.12  ? 287 GLN A CG  1 
ATOM   2275  C CD  . GLN A  1 287 ? -46.584  8.363   -85.971  1.00 29.88  ? 287 GLN A CD  1 
ATOM   2276  O OE1 . GLN A  1 287 ? -47.458  8.499   -85.099  1.00 31.08  ? 287 GLN A OE1 1 
ATOM   2277  N NE2 . GLN A  1 287 ? -45.718  7.372   -85.954  1.00 28.13  ? 287 GLN A NE2 1 
ATOM   2278  N N   . PRO A  1 288 ? -51.332  9.069   -87.547  1.00 26.16  ? 288 PRO A N   1 
ATOM   2279  C CA  . PRO A  1 288 ? -52.640  9.728   -87.513  1.00 26.33  ? 288 PRO A CA  1 
ATOM   2280  C C   . PRO A  1 288 ? -52.622  11.069  -86.782  1.00 26.16  ? 288 PRO A C   1 
ATOM   2281  O O   . PRO A  1 288 ? -53.266  12.008  -87.241  1.00 27.95  ? 288 PRO A O   1 
ATOM   2282  C CB  . PRO A  1 288 ? -53.457  8.669   -86.795  1.00 25.70  ? 288 PRO A CB  1 
ATOM   2283  C CG  . PRO A  1 288 ? -52.845  7.380   -87.328  1.00 25.66  ? 288 PRO A CG  1 
ATOM   2284  C CD  . PRO A  1 288 ? -51.385  7.652   -87.183  1.00 26.40  ? 288 PRO A CD  1 
ATOM   2285  N N   . GLU A  1 289 ? -51.791  11.172  -85.731  1.00 25.87  ? 289 GLU A N   1 
ATOM   2286  C CA  . GLU A  1 289 ? -51.845  12.266  -84.770  1.00 27.50  ? 289 GLU A CA  1 
ATOM   2287  C C   . GLU A  1 289 ? -51.384  13.604  -85.377  1.00 27.24  ? 289 GLU A C   1 
ATOM   2288  O O   . GLU A  1 289 ? -51.549  14.643  -84.745  1.00 27.37  ? 289 GLU A O   1 
ATOM   2289  C CB  . GLU A  1 289 ? -51.062  11.936  -83.495  1.00 26.32  ? 289 GLU A CB  1 
ATOM   2290  C CG  . GLU A  1 289 ? -51.786  10.966  -82.570  1.00 28.47  ? 289 GLU A CG  1 
ATOM   2291  C CD  . GLU A  1 289 ? -53.105  11.476  -81.984  1.00 28.41  ? 289 GLU A CD  1 
ATOM   2292  O OE1 . GLU A  1 289 ? -53.101  12.651  -81.609  1.00 29.34  ? 289 GLU A OE1 1 
ATOM   2293  O OE2 . GLU A  1 289 ? -54.107  10.732  -81.862  1.00 26.74  ? 289 GLU A OE2 1 
ATOM   2294  N N   . GLU A  1 290 ? -50.757  13.567  -86.554  1.00 26.94  ? 290 GLU A N   1 
ATOM   2295  C CA  . GLU A  1 290 ? -50.161  14.734  -87.175  1.00 27.22  ? 290 GLU A CA  1 
ATOM   2296  C C   . GLU A  1 290 ? -51.057  15.321  -88.256  1.00 27.62  ? 290 GLU A C   1 
ATOM   2297  O O   . GLU A  1 290 ? -50.635  16.234  -88.943  1.00 28.32  ? 290 GLU A O   1 
ATOM   2298  C CB  . GLU A  1 290 ? -48.856  14.325  -87.846  1.00 28.49  ? 290 GLU A CB  1 
ATOM   2299  C CG  . GLU A  1 290 ? -47.778  13.965  -86.837  1.00 29.15  ? 290 GLU A CG  1 
ATOM   2300  C CD  . GLU A  1 290 ? -46.416  13.751  -87.437  1.00 30.74  ? 290 GLU A CD  1 
ATOM   2301  O OE1 . GLU A  1 290 ? -45.989  14.411  -88.409  1.00 32.19  ? 290 GLU A OE1 1 
ATOM   2302  O OE2 . GLU A  1 290 ? -45.723  12.939  -86.810  1.00 34.16  ? 290 GLU A OE2 1 
ATOM   2303  N N   . TRP A  1 291 ? -52.290  14.804  -88.385  1.00 28.04  ? 291 TRP A N   1 
ATOM   2304  C CA  . TRP A  1 291 ? -53.175  15.140  -89.484  1.00 25.65  ? 291 TRP A CA  1 
ATOM   2305  C C   . TRP A  1 291 ? -54.598  15.305  -88.956  1.00 25.70  ? 291 TRP A C   1 
ATOM   2306  O O   . TRP A  1 291 ? -55.533  14.922  -89.645  1.00 26.04  ? 291 TRP A O   1 
ATOM   2307  C CB  . TRP A  1 291 ? -53.132  14.003  -90.524  1.00 25.85  ? 291 TRP A CB  1 
ATOM   2308  C CG  . TRP A  1 291 ? -51.795  13.749  -91.157  1.00 25.22  ? 291 TRP A CG  1 
ATOM   2309  C CD1 . TRP A  1 291 ? -50.764  12.979  -90.685  1.00 25.24  ? 291 TRP A CD1 1 
ATOM   2310  C CD2 . TRP A  1 291 ? -51.362  14.256  -92.434  1.00 25.78  ? 291 TRP A CD2 1 
ATOM   2311  N NE1 . TRP A  1 291 ? -49.718  12.982  -91.573  1.00 24.94  ? 291 TRP A NE1 1 
ATOM   2312  C CE2 . TRP A  1 291 ? -50.065  13.748  -92.656  1.00 25.98  ? 291 TRP A CE2 1 
ATOM   2313  C CE3 . TRP A  1 291 ? -51.938  15.105  -93.390  1.00 27.05  ? 291 TRP A CE3 1 
ATOM   2314  C CZ2 . TRP A  1 291 ? -49.352  14.059  -93.806  1.00 28.29  ? 291 TRP A CZ2 1 
ATOM   2315  C CZ3 . TRP A  1 291 ? -51.228  15.426  -94.518  1.00 27.74  ? 291 TRP A CZ3 1 
ATOM   2316  C CH2 . TRP A  1 291 ? -49.943  14.899  -94.721  1.00 28.93  ? 291 TRP A CH2 1 
ATOM   2317  N N   . PHE A  1 292 ? -54.786  15.803  -87.724  1.00 25.71  ? 292 PHE A N   1 
ATOM   2318  C CA  . PHE A  1 292 ? -56.138  16.031  -87.222  1.00 26.91  ? 292 PHE A CA  1 
ATOM   2319  C C   . PHE A  1 292 ? -56.655  17.441  -87.549  1.00 25.50  ? 292 PHE A C   1 
ATOM   2320  O O   . PHE A  1 292 ? -57.801  17.753  -87.251  1.00 25.12  ? 292 PHE A O   1 
ATOM   2321  C CB  . PHE A  1 292 ? -56.261  15.870  -85.701  1.00 29.36  ? 292 PHE A CB  1 
ATOM   2322  C CG  . PHE A  1 292 ? -56.535  14.447  -85.251  1.00 29.48  ? 292 PHE A CG  1 
ATOM   2323  C CD1 . PHE A  1 292 ? -57.820  13.979  -85.197  1.00 30.06  ? 292 PHE A CD1 1 
ATOM   2324  C CD2 . PHE A  1 292 ? -55.497  13.565  -84.981  1.00 32.31  ? 292 PHE A CD2 1 
ATOM   2325  C CE1 . PHE A  1 292 ? -58.073  12.661  -84.869  1.00 29.83  ? 292 PHE A CE1 1 
ATOM   2326  C CE2 . PHE A  1 292 ? -55.760  12.244  -84.656  1.00 32.02  ? 292 PHE A CE2 1 
ATOM   2327  C CZ  . PHE A  1 292 ? -57.050  11.808  -84.579  1.00 30.01  ? 292 PHE A CZ  1 
ATOM   2328  N N   . GLY A  1 293 ? -55.833  18.328  -88.103  1.00 24.70  ? 293 GLY A N   1 
ATOM   2329  C CA  . GLY A  1 293 ? -56.236  19.743  -88.215  1.00 25.01  ? 293 GLY A CA  1 
ATOM   2330  C C   . GLY A  1 293 ? -57.400  19.990  -89.185  1.00 23.41  ? 293 GLY A C   1 
ATOM   2331  O O   . GLY A  1 293 ? -57.610  19.278  -90.188  1.00 21.84  ? 293 GLY A O   1 
ATOM   2332  N N   . PHE A  1 294 ? -58.163  21.048  -88.898  1.00 24.16  ? 294 PHE A N   1 
ATOM   2333  C CA  . PHE A  1 294 ? -59.042  21.617  -89.909  1.00 23.61  ? 294 PHE A CA  1 
ATOM   2334  C C   . PHE A  1 294 ? -58.236  22.418  -90.934  1.00 23.99  ? 294 PHE A C   1 
ATOM   2335  O O   . PHE A  1 294 ? -58.757  22.694  -92.027  1.00 26.16  ? 294 PHE A O   1 
ATOM   2336  C CB  . PHE A  1 294 ? -60.129  22.464  -89.252  1.00 25.10  ? 294 PHE A CB  1 
ATOM   2337  C CG  . PHE A  1 294 ? -61.148  21.709  -88.426  1.00 23.53  ? 294 PHE A CG  1 
ATOM   2338  C CD1 . PHE A  1 294 ? -61.020  20.350  -88.178  1.00 23.14  ? 294 PHE A CD1 1 
ATOM   2339  C CD2 . PHE A  1 294 ? -62.213  22.393  -87.851  1.00 23.48  ? 294 PHE A CD2 1 
ATOM   2340  C CE1 . PHE A  1 294 ? -61.970  19.693  -87.393  1.00 23.01  ? 294 PHE A CE1 1 
ATOM   2341  C CE2 . PHE A  1 294 ? -63.152  21.740  -87.068  1.00 22.41  ? 294 PHE A CE2 1 
ATOM   2342  C CZ  . PHE A  1 294 ? -63.018  20.392  -86.832  1.00 23.51  ? 294 PHE A CZ  1 
ATOM   2343  N N   . TRP A  1 295 ? -56.988  22.772  -90.575  1.00 23.24  ? 295 TRP A N   1 
ATOM   2344  C CA  . TRP A  1 295 ? -56.033  23.440  -91.452  1.00 24.03  ? 295 TRP A CA  1 
ATOM   2345  C C   . TRP A  1 295 ? -54.777  22.587  -91.587  1.00 24.98  ? 295 TRP A C   1 
ATOM   2346  O O   . TRP A  1 295 ? -54.310  22.001  -90.618  1.00 27.05  ? 295 TRP A O   1 
ATOM   2347  C CB  . TRP A  1 295 ? -55.625  24.817  -90.891  1.00 24.33  ? 295 TRP A CB  1 
ATOM   2348  C CG  . TRP A  1 295 ? -56.676  25.902  -90.950  1.00 24.13  ? 295 TRP A CG  1 
ATOM   2349  C CD1 . TRP A  1 295 ? -57.949  25.836  -90.461  1.00 24.74  ? 295 TRP A CD1 1 
ATOM   2350  C CD2 . TRP A  1 295 ? -56.546  27.219  -91.566  1.00 23.65  ? 295 TRP A CD2 1 
ATOM   2351  N NE1 . TRP A  1 295 ? -58.618  27.007  -90.734  1.00 26.55  ? 295 TRP A NE1 1 
ATOM   2352  C CE2 . TRP A  1 295 ? -57.779  27.881  -91.398  1.00 24.01  ? 295 TRP A CE2 1 
ATOM   2353  C CE3 . TRP A  1 295 ? -55.529  27.893  -92.245  1.00 23.98  ? 295 TRP A CE3 1 
ATOM   2354  C CZ2 . TRP A  1 295 ? -58.008  29.173  -91.875  1.00 23.96  ? 295 TRP A CZ2 1 
ATOM   2355  C CZ3 . TRP A  1 295 ? -55.758  29.167  -92.731  1.00 24.87  ? 295 TRP A CZ3 1 
ATOM   2356  C CH2 . TRP A  1 295 ? -56.986  29.810  -92.544  1.00 24.15  ? 295 TRP A CH2 1 
ATOM   2357  N N   . GLY A  1 296 ? -54.201  22.540  -92.785  1.00 26.05  ? 296 GLY A N   1 
ATOM   2358  C CA  . GLY A  1 296 ? -52.949  21.848  -93.011  1.00 26.31  ? 296 GLY A CA  1 
ATOM   2359  C C   . GLY A  1 296 ? -51.908  22.775  -93.652  1.00 26.63  ? 296 GLY A C   1 
ATOM   2360  O O   . GLY A  1 296 ? -52.263  23.708  -94.393  1.00 26.75  ? 296 GLY A O   1 
ATOM   2361  N N   . TYR A  1 297 ? -50.634  22.424  -93.418  1.00 27.65  ? 297 TYR A N   1 
ATOM   2362  C CA  . TYR A  1 297 ? -49.454  23.168  -93.860  1.00 29.50  ? 297 TYR A CA  1 
ATOM   2363  C C   . TYR A  1 297 ? -48.868  22.486  -95.098  1.00 30.22  ? 297 TYR A C   1 
ATOM   2364  O O   . TYR A  1 297 ? -48.843  21.257  -95.164  1.00 30.29  ? 297 TYR A O   1 
ATOM   2365  C CB  . TYR A  1 297 ? -48.447  23.279  -92.704  1.00 28.18  ? 297 TYR A CB  1 
ATOM   2366  C CG  . TYR A  1 297 ? -49.030  23.937  -91.459  1.00 26.68  ? 297 TYR A CG  1 
ATOM   2367  C CD1 . TYR A  1 297 ? -49.141  25.316  -91.370  1.00 27.93  ? 297 TYR A CD1 1 
ATOM   2368  C CD2 . TYR A  1 297 ? -49.492  23.196  -90.389  1.00 25.36  ? 297 TYR A CD2 1 
ATOM   2369  C CE1 . TYR A  1 297 ? -49.723  25.930  -90.274  1.00 26.74  ? 297 TYR A CE1 1 
ATOM   2370  C CE2 . TYR A  1 297 ? -50.058  23.802  -89.280  1.00 25.41  ? 297 TYR A CE2 1 
ATOM   2371  C CZ  . TYR A  1 297 ? -50.183  25.175  -89.225  1.00 25.37  ? 297 TYR A CZ  1 
ATOM   2372  O OH  . TYR A  1 297 ? -50.727  25.803  -88.146  1.00 24.43  ? 297 TYR A OH  1 
ATOM   2373  N N   . SER A  1 298 ? -48.434  23.292  -96.079  1.00 30.61  ? 298 SER A N   1 
ATOM   2374  C CA  . SER A  1 298 ? -47.989  22.767  -97.358  1.00 32.44  ? 298 SER A CA  1 
ATOM   2375  C C   . SER A  1 298 ? -46.621  22.101  -97.211  1.00 33.39  ? 298 SER A C   1 
ATOM   2376  O O   . SER A  1 298 ? -46.375  21.078  -97.839  1.00 33.92  ? 298 SER A O   1 
ATOM   2377  C CB  . SER A  1 298 ? -47.940  23.836  -98.418  1.00 33.50  ? 298 SER A CB  1 
ATOM   2378  O OG  . SER A  1 298 ? -46.844  24.683  -98.125  1.00 36.51  ? 298 SER A OG  1 
ATOM   2379  N N   . ASP A  1 299 ? -45.736  22.705  -96.404  1.00 34.38  ? 299 ASP A N   1 
ATOM   2380  C CA  . ASP A  1 299 ? -44.370  22.228  -96.254  1.00 34.52  ? 299 ASP A CA  1 
ATOM   2381  C C   . ASP A  1 299 ? -43.804  22.792  -94.957  1.00 34.76  ? 299 ASP A C   1 
ATOM   2382  O O   . ASP A  1 299 ? -44.525  23.459  -94.217  1.00 33.70  ? 299 ASP A O   1 
ATOM   2383  C CB  . ASP A  1 299 ? -43.547  22.508  -97.495  1.00 35.65  ? 299 ASP A CB  1 
ATOM   2384  C CG  . ASP A  1 299 ? -43.210  23.975  -97.716  1.00 38.54  ? 299 ASP A CG  1 
ATOM   2385  O OD1 . ASP A  1 299 ? -43.329  24.770  -96.775  1.00 40.23  ? 299 ASP A OD1 1 
ATOM   2386  O OD2 . ASP A  1 299 ? -42.838  24.320  -98.837  1.00 41.21  ? 299 ASP A OD2 1 
ATOM   2387  N N   . LEU A  1 300 ? -42.527  22.480  -94.674  1.00 36.23  ? 300 LEU A N   1 
ATOM   2388  C CA  . LEU A  1 300 ? -41.899  22.819  -93.401  1.00 35.57  ? 300 LEU A CA  1 
ATOM   2389  C C   . LEU A  1 300 ? -41.866  24.331  -93.165  1.00 35.82  ? 300 LEU A C   1 
ATOM   2390  O O   . LEU A  1 300 ? -41.716  24.744  -92.025  1.00 37.08  ? 300 LEU A O   1 
ATOM   2391  C CB  . LEU A  1 300 ? -40.476  22.257  -93.358  1.00 34.87  ? 300 LEU A CB  1 
ATOM   2392  C CG  . LEU A  1 300 ? -39.633  22.579  -92.111  1.00 33.24  ? 300 LEU A CG  1 
ATOM   2393  C CD1 . LEU A  1 300 ? -40.324  22.141  -90.832  1.00 31.37  ? 300 LEU A CD1 1 
ATOM   2394  C CD2 . LEU A  1 300 ? -38.252  21.915  -92.185  1.00 33.68  ? 300 LEU A CD2 1 
ATOM   2395  N N   . ASN A  1 301 ? -41.892  25.135  -94.241  1.00 35.76  ? 301 ASN A N   1 
ATOM   2396  C CA  . ASN A  1 301 ? -41.714  26.581  -94.177  1.00 35.00  ? 301 ASN A CA  1 
ATOM   2397  C C   . ASN A  1 301 ? -43.050  27.312  -94.113  1.00 34.72  ? 301 ASN A C   1 
ATOM   2398  O O   . ASN A  1 301 ? -43.089  28.530  -93.965  1.00 35.23  ? 301 ASN A O   1 
ATOM   2399  C CB  . ASN A  1 301 ? -40.939  27.096  -95.384  1.00 34.85  ? 301 ASN A CB  1 
ATOM   2400  C CG  . ASN A  1 301 ? -39.543  26.531  -95.343  1.00 36.82  ? 301 ASN A CG  1 
ATOM   2401  O OD1 . ASN A  1 301 ? -39.059  25.980  -96.330  1.00 36.92  ? 301 ASN A OD1 1 
ATOM   2402  N ND2 . ASN A  1 301 ? -38.882  26.645  -94.203  1.00 36.75  ? 301 ASN A ND2 1 
ATOM   2403  N N   . ASP A  1 302 ? -44.141  26.576  -94.258  1.00 33.60  ? 302 ASP A N   1 
ATOM   2404  C CA  . ASP A  1 302 ? -45.447  27.175  -94.243  1.00 32.67  ? 302 ASP A CA  1 
ATOM   2405  C C   . ASP A  1 302 ? -45.804  27.384  -92.787  1.00 34.85  ? 302 ASP A C   1 
ATOM   2406  O O   . ASP A  1 302 ? -45.894  26.411  -92.048  1.00 33.01  ? 302 ASP A O   1 
ATOM   2407  C CB  . ASP A  1 302 ? -46.453  26.297  -94.959  1.00 32.36  ? 302 ASP A CB  1 
ATOM   2408  C CG  . ASP A  1 302 ? -47.833  26.913  -95.112  1.00 29.84  ? 302 ASP A CG  1 
ATOM   2409  O OD1 . ASP A  1 302 ? -47.955  28.074  -94.759  1.00 29.51  ? 302 ASP A OD1 1 
ATOM   2410  O OD2 . ASP A  1 302 ? -48.741  26.242  -95.622  1.00 29.58  ? 302 ASP A OD2 1 
ATOM   2411  N N   . LYS A  1 303 ? -46.007  28.658  -92.407  1.00 36.85  ? 303 LYS A N   1 
ATOM   2412  C CA  . LYS A  1 303 ? -46.361  29.020  -91.046  1.00 39.29  ? 303 LYS A CA  1 
ATOM   2413  C C   . LYS A  1 303 ? -47.853  29.338  -90.908  1.00 36.11  ? 303 LYS A C   1 
ATOM   2414  O O   . LYS A  1 303 ? -48.278  29.676  -89.808  1.00 36.93  ? 303 LYS A O   1 
ATOM   2415  C CB  . LYS A  1 303 ? -45.664  30.307  -90.585  1.00 47.82  ? 303 LYS A CB  1 
ATOM   2416  C CG  . LYS A  1 303 ? -44.147  30.368  -90.680  1.00 53.25  ? 303 LYS A CG  1 
ATOM   2417  C CD  . LYS A  1 303 ? -43.393  29.577  -89.617  1.00 57.49  ? 303 LYS A CD  1 
ATOM   2418  C CE  . LYS A  1 303 ? -41.913  29.609  -89.891  1.00 59.90  ? 303 LYS A CE  1 
ATOM   2419  N NZ  . LYS A  1 303 ? -41.296  28.594  -89.047  1.00 58.54  ? 303 LYS A NZ  1 
ATOM   2420  N N   . TYR A  1 304 ? -48.632  29.223  -91.999  1.00 34.29  ? 304 TYR A N   1 
ATOM   2421  C CA  . TYR A  1 304 ? -50.000  29.727  -92.085  1.00 32.17  ? 304 TYR A CA  1 
ATOM   2422  C C   . TYR A  1 304 ? -50.974  28.599  -92.365  1.00 30.78  ? 304 TYR A C   1 
ATOM   2423  O O   . TYR A  1 304 ? -51.963  28.449  -91.639  1.00 31.52  ? 304 TYR A O   1 
ATOM   2424  C CB  . TYR A  1 304 ? -50.145  30.818  -93.157  1.00 33.46  ? 304 TYR A CB  1 
ATOM   2425  C CG  . TYR A  1 304 ? -49.282  32.024  -92.812  1.00 34.44  ? 304 TYR A CG  1 
ATOM   2426  C CD1 . TYR A  1 304 ? -49.635  32.853  -91.752  1.00 35.99  ? 304 TYR A CD1 1 
ATOM   2427  C CD2 . TYR A  1 304 ? -48.098  32.290  -93.483  1.00 36.94  ? 304 TYR A CD2 1 
ATOM   2428  C CE1 . TYR A  1 304 ? -48.859  33.942  -91.390  1.00 35.98  ? 304 TYR A CE1 1 
ATOM   2429  C CE2 . TYR A  1 304 ? -47.285  33.346  -93.101  1.00 39.39  ? 304 TYR A CE2 1 
ATOM   2430  C CZ  . TYR A  1 304 ? -47.677  34.176  -92.056  1.00 38.30  ? 304 TYR A CZ  1 
ATOM   2431  O OH  . TYR A  1 304 ? -46.908  35.200  -91.617  1.00 37.93  ? 304 TYR A OH  1 
ATOM   2432  N N   . GLY A  1 305 ? -50.736  27.856  -93.448  1.00 30.63  ? 305 GLY A N   1 
ATOM   2433  C CA  . GLY A  1 305 ? -51.622  26.752  -93.799  1.00 31.91  ? 305 GLY A CA  1 
ATOM   2434  C C   . GLY A  1 305 ? -52.889  27.228  -94.529  1.00 31.09  ? 305 GLY A C   1 
ATOM   2435  O O   . GLY A  1 305 ? -53.062  28.430  -94.762  1.00 30.45  ? 305 GLY A O   1 
ATOM   2436  N N   . THR A  1 306 ? -53.709  26.268  -94.996  1.00 29.51  ? 306 THR A N   1 
ATOM   2437  C CA  . THR A  1 306 ? -55.011  26.568  -95.593  1.00 28.45  ? 306 THR A CA  1 
ATOM   2438  C C   . THR A  1 306 ? -56.068  25.634  -95.003  1.00 27.44  ? 306 THR A C   1 
ATOM   2439  O O   . THR A  1 306 ? -55.757  24.507  -94.603  1.00 26.57  ? 306 THR A O   1 
ATOM   2440  C CB  . THR A  1 306 ? -54.948  26.451  -97.116  1.00 29.21  ? 306 THR A CB  1 
ATOM   2441  O OG1 . THR A  1 306 ? -54.624  25.098  -97.409  1.00 30.25  ? 306 THR A OG1 1 
ATOM   2442  C CG2 . THR A  1 306 ? -53.902  27.354  -97.750  1.00 29.47  ? 306 THR A CG2 1 
ATOM   2443  N N   . PRO A  1 307 ? -57.351  26.055  -94.953  1.00 26.75  ? 307 PRO A N   1 
ATOM   2444  C CA  . PRO A  1 307 ? -58.422  25.202  -94.436  1.00 26.17  ? 307 PRO A CA  1 
ATOM   2445  C C   . PRO A  1 307 ? -58.781  24.064  -95.389  1.00 26.93  ? 307 PRO A C   1 
ATOM   2446  O O   . PRO A  1 307 ? -58.806  24.265  -96.611  1.00 27.96  ? 307 PRO A O   1 
ATOM   2447  C CB  . PRO A  1 307 ? -59.581  26.188  -94.290  1.00 25.72  ? 307 PRO A CB  1 
ATOM   2448  C CG  . PRO A  1 307 ? -59.366  27.188  -95.434  1.00 26.13  ? 307 PRO A CG  1 
ATOM   2449  C CD  . PRO A  1 307 ? -57.858  27.327  -95.495  1.00 26.62  ? 307 PRO A CD  1 
ATOM   2450  N N   . ARG A  1 308 ? -59.055  22.886  -94.808  1.00 27.60  ? 308 ARG A N   1 
ATOM   2451  C CA  . ARG A  1 308 ? -59.543  21.711  -95.522  1.00 27.48  ? 308 ARG A CA  1 
ATOM   2452  C C   . ARG A  1 308 ? -61.059  21.775  -95.592  1.00 26.76  ? 308 ARG A C   1 
ATOM   2453  O O   . ARG A  1 308 ? -61.655  22.597  -94.912  1.00 28.23  ? 308 ARG A O   1 
ATOM   2454  C CB  . ARG A  1 308 ? -59.179  20.484  -94.689  1.00 28.96  ? 308 ARG A CB  1 
ATOM   2455  C CG  . ARG A  1 308 ? -57.676  20.245  -94.705  1.00 31.49  ? 308 ARG A CG  1 
ATOM   2456  C CD  . ARG A  1 308 ? -57.174  19.269  -93.639  1.00 31.86  ? 308 ARG A CD  1 
ATOM   2457  N NE  . ARG A  1 308 ? -55.760  18.954  -93.884  1.00 30.24  ? 308 ARG A NE  1 
ATOM   2458  C CZ  . ARG A  1 308 ? -54.959  18.412  -92.994  1.00 29.71  ? 308 ARG A CZ  1 
ATOM   2459  N NH1 . ARG A  1 308 ? -55.376  18.207  -91.757  1.00 30.02  ? 308 ARG A NH1 1 
ATOM   2460  N NH2 . ARG A  1 308 ? -53.728  18.081  -93.352  1.00 31.27  ? 308 ARG A NH2 1 
ATOM   2461  N N   . PRO A  1 309 ? -61.749  20.924  -96.371  1.00 26.18  ? 309 PRO A N   1 
ATOM   2462  C CA  . PRO A  1 309 ? -63.210  21.039  -96.514  1.00 26.48  ? 309 PRO A CA  1 
ATOM   2463  C C   . PRO A  1 309 ? -64.045  21.088  -95.236  1.00 26.78  ? 309 PRO A C   1 
ATOM   2464  O O   . PRO A  1 309 ? -65.063  21.782  -95.166  1.00 29.58  ? 309 PRO A O   1 
ATOM   2465  C CB  . PRO A  1 309 ? -63.534  19.837  -97.370  1.00 26.36  ? 309 PRO A CB  1 
ATOM   2466  C CG  . PRO A  1 309 ? -62.290  19.689  -98.218  1.00 27.41  ? 309 PRO A CG  1 
ATOM   2467  C CD  . PRO A  1 309 ? -61.168  19.885  -97.223  1.00 27.20  ? 309 PRO A CD  1 
ATOM   2468  N N   . VAL A  1 310 ? -63.559  20.397  -94.210  1.00 26.90  ? 310 VAL A N   1 
ATOM   2469  C CA  . VAL A  1 310 ? -64.205  20.319  -92.916  1.00 27.20  ? 310 VAL A CA  1 
ATOM   2470  C C   . VAL A  1 310 ? -64.439  21.717  -92.340  1.00 26.73  ? 310 VAL A C   1 
ATOM   2471  O O   . VAL A  1 310 ? -65.465  21.967  -91.720  1.00 26.78  ? 310 VAL A O   1 
ATOM   2472  C CB  . VAL A  1 310 ? -63.414  19.388  -91.971  1.00 26.89  ? 310 VAL A CB  1 
ATOM   2473  C CG1 . VAL A  1 310 ? -61.952  19.770  -91.766  1.00 26.99  ? 310 VAL A CG1 1 
ATOM   2474  C CG2 . VAL A  1 310 ? -64.110  19.197  -90.628  1.00 26.40  ? 310 VAL A CG2 1 
ATOM   2475  N N   . TRP A  1 311 ? -63.485  22.617  -92.533  1.00 25.74  ? 311 TRP A N   1 
ATOM   2476  C CA  . TRP A  1 311 ? -63.588  23.972  -92.001  1.00 26.08  ? 311 TRP A CA  1 
ATOM   2477  C C   . TRP A  1 311 ? -64.887  24.652  -92.421  1.00 25.03  ? 311 TRP A C   1 
ATOM   2478  O O   . TRP A  1 311 ? -65.544  25.280  -91.592  1.00 23.59  ? 311 TRP A O   1 
ATOM   2479  C CB  . TRP A  1 311 ? -62.405  24.779  -92.529  1.00 25.45  ? 311 TRP A CB  1 
ATOM   2480  C CG  . TRP A  1 311 ? -62.301  26.177  -92.031  1.00 26.28  ? 311 TRP A CG  1 
ATOM   2481  C CD1 . TRP A  1 311 ? -62.489  27.301  -92.781  1.00 27.96  ? 311 TRP A CD1 1 
ATOM   2482  C CD2 . TRP A  1 311 ? -61.891  26.624  -90.724  1.00 28.23  ? 311 TRP A CD2 1 
ATOM   2483  N NE1 . TRP A  1 311 ? -62.249  28.419  -92.038  1.00 28.86  ? 311 TRP A NE1 1 
ATOM   2484  C CE2 . TRP A  1 311 ? -61.876  28.041  -90.771  1.00 29.39  ? 311 TRP A CE2 1 
ATOM   2485  C CE3 . TRP A  1 311 ? -61.535  25.988  -89.534  1.00 28.57  ? 311 TRP A CE3 1 
ATOM   2486  C CZ2 . TRP A  1 311 ? -61.537  28.819  -89.668  1.00 27.81  ? 311 TRP A CZ2 1 
ATOM   2487  C CZ3 . TRP A  1 311 ? -61.201  26.757  -88.443  1.00 28.54  ? 311 TRP A CZ3 1 
ATOM   2488  C CH2 . TRP A  1 311 ? -61.200  28.149  -88.518  1.00 29.40  ? 311 TRP A CH2 1 
ATOM   2489  N N   . PHE A  1 312 ? -65.189  24.534  -93.719  1.00 25.73  ? 312 PHE A N   1 
ATOM   2490  C CA  . PHE A  1 312 ? -66.324  25.180  -94.367  1.00 26.68  ? 312 PHE A CA  1 
ATOM   2491  C C   . PHE A  1 312 ? -67.619  24.469  -93.976  1.00 27.00  ? 312 PHE A C   1 
ATOM   2492  O O   . PHE A  1 312 ? -68.647  25.108  -93.738  1.00 27.93  ? 312 PHE A O   1 
ATOM   2493  C CB  . PHE A  1 312 ? -66.089  25.252  -95.885  1.00 25.56  ? 312 PHE A CB  1 
ATOM   2494  C CG  . PHE A  1 312 ? -64.893  26.115  -96.255  1.00 25.54  ? 312 PHE A CG  1 
ATOM   2495  C CD1 . PHE A  1 312 ? -64.968  27.507  -96.209  1.00 28.16  ? 312 PHE A CD1 1 
ATOM   2496  C CD2 . PHE A  1 312 ? -63.665  25.539  -96.589  1.00 25.37  ? 312 PHE A CD2 1 
ATOM   2497  C CE1 . PHE A  1 312 ? -63.853  28.302  -96.530  1.00 27.93  ? 312 PHE A CE1 1 
ATOM   2498  C CE2 . PHE A  1 312 ? -62.561  26.316  -96.892  1.00 25.79  ? 312 PHE A CE2 1 
ATOM   2499  C CZ  . PHE A  1 312 ? -62.649  27.698  -96.854  1.00 27.36  ? 312 PHE A CZ  1 
ATOM   2500  N N   . ALA A  1 313 ? -67.561  23.137  -93.837  1.00 27.96  ? 313 ALA A N   1 
ATOM   2501  C CA  . ALA A  1 313 ? -68.751  22.370  -93.459  1.00 26.43  ? 313 ALA A CA  1 
ATOM   2502  C C   . ALA A  1 313 ? -69.142  22.708  -92.022  1.00 26.24  ? 313 ALA A C   1 
ATOM   2503  O O   . ALA A  1 313 ? -70.325  22.913  -91.724  1.00 24.69  ? 313 ALA A O   1 
ATOM   2504  C CB  . ALA A  1 313 ? -68.528  20.898  -93.665  1.00 25.63  ? 313 ALA A CB  1 
ATOM   2505  N N   . MET A  1 314 ? -68.123  22.869  -91.170  1.00 24.78  ? 314 MET A N   1 
ATOM   2506  C CA  . MET A  1 314 ? -68.351  23.227  -89.783  1.00 26.09  ? 314 MET A CA  1 
ATOM   2507  C C   . MET A  1 314 ? -68.890  24.660  -89.665  1.00 26.26  ? 314 MET A C   1 
ATOM   2508  O O   . MET A  1 314 ? -69.837  24.890  -88.919  1.00 25.15  ? 314 MET A O   1 
ATOM   2509  C CB  . MET A  1 314 ? -67.069  23.051  -88.965  1.00 27.90  ? 314 MET A CB  1 
ATOM   2510  C CG  . MET A  1 314 ? -66.745  21.576  -88.712  1.00 29.81  ? 314 MET A CG  1 
ATOM   2511  S SD  . MET A  1 314 ? -67.757  20.945  -87.370  1.00 30.30  ? 314 MET A SD  1 
ATOM   2512  C CE  . MET A  1 314 ? -67.187  21.972  -86.017  1.00 28.23  ? 314 MET A CE  1 
ATOM   2513  N N   . ARG A  1 315 ? -68.279  25.619  -90.359  1.00 25.30  ? 315 ARG A N   1 
ATOM   2514  C CA  . ARG A  1 315 ? -68.763  26.983  -90.341  1.00 26.58  ? 315 ARG A CA  1 
ATOM   2515  C C   . ARG A  1 315 ? -70.244  27.001  -90.719  1.00 26.91  ? 315 ARG A C   1 
ATOM   2516  O O   . ARG A  1 315 ? -71.032  27.634  -90.047  1.00 25.29  ? 315 ARG A O   1 
ATOM   2517  C CB  . ARG A  1 315 ? -67.988  27.878  -91.312  1.00 26.28  ? 315 ARG A CB  1 
ATOM   2518  C CG  . ARG A  1 315 ? -68.429  29.335  -91.282  1.00 27.68  ? 315 ARG A CG  1 
ATOM   2519  C CD  . ARG A  1 315 ? -67.858  30.165  -92.424  1.00 28.94  ? 315 ARG A CD  1 
ATOM   2520  N NE  . ARG A  1 315 ? -68.309  29.545  -93.677  1.00 32.70  ? 315 ARG A NE  1 
ATOM   2521  C CZ  . ARG A  1 315 ? -67.909  29.834  -94.904  1.00 32.82  ? 315 ARG A CZ  1 
ATOM   2522  N NH1 . ARG A  1 315 ? -67.018  30.773  -95.089  1.00 33.44  ? 315 ARG A NH1 1 
ATOM   2523  N NH2 . ARG A  1 315 ? -68.387  29.145  -95.931  1.00 33.28  ? 315 ARG A NH2 1 
ATOM   2524  N N   . ASP A  1 316 ? -70.613  26.290  -91.786  1.00 28.90  ? 316 ASP A N   1 
ATOM   2525  C CA  . ASP A  1 316 ? -71.991  26.295  -92.277  1.00 30.93  ? 316 ASP A CA  1 
ATOM   2526  C C   . ASP A  1 316 ? -72.951  25.656  -91.257  1.00 29.41  ? 316 ASP A C   1 
ATOM   2527  O O   . ASP A  1 316 ? -74.028  26.200  -90.999  1.00 29.62  ? 316 ASP A O   1 
ATOM   2528  C CB  . ASP A  1 316 ? -72.057  25.707  -93.688  1.00 32.57  ? 316 ASP A CB  1 
ATOM   2529  C CG  . ASP A  1 316 ? -71.376  26.491  -94.813  1.00 37.55  ? 316 ASP A CG  1 
ATOM   2530  O OD1 . ASP A  1 316 ? -70.938  27.693  -94.608  1.00 36.91  ? 316 ASP A OD1 1 
ATOM   2531  O OD2 . ASP A  1 316 ? -71.279  25.903  -95.917  1.00 41.69  ? 316 ASP A OD2 1 
ATOM   2532  N N   . TYR A  1 317 ? -72.543  24.508  -90.686  1.00 27.11  ? 317 TYR A N   1 
ATOM   2533  C CA  . TYR A  1 317 ? -73.291  23.750  -89.702  1.00 25.55  ? 317 TYR A CA  1 
ATOM   2534  C C   . TYR A  1 317 ? -73.554  24.575  -88.447  1.00 26.36  ? 317 TYR A C   1 
ATOM   2535  O O   . TYR A  1 317 ? -74.652  24.522  -87.891  1.00 28.68  ? 317 TYR A O   1 
ATOM   2536  C CB  . TYR A  1 317 ? -72.585  22.447  -89.329  1.00 24.30  ? 317 TYR A CB  1 
ATOM   2537  C CG  . TYR A  1 317 ? -73.451  21.568  -88.447  1.00 24.29  ? 317 TYR A CG  1 
ATOM   2538  C CD1 . TYR A  1 317 ? -74.455  20.772  -88.980  1.00 26.41  ? 317 TYR A CD1 1 
ATOM   2539  C CD2 . TYR A  1 317 ? -73.295  21.546  -87.082  1.00 24.38  ? 317 TYR A CD2 1 
ATOM   2540  C CE1 . TYR A  1 317 ? -75.281  19.978  -88.186  1.00 26.44  ? 317 TYR A CE1 1 
ATOM   2541  C CE2 . TYR A  1 317 ? -74.110  20.765  -86.267  1.00 26.19  ? 317 TYR A CE2 1 
ATOM   2542  C CZ  . TYR A  1 317 ? -75.113  19.969  -86.811  1.00 26.78  ? 317 TYR A CZ  1 
ATOM   2543  O OH  . TYR A  1 317 ? -75.898  19.174  -85.991  1.00 24.65  ? 317 TYR A OH  1 
ATOM   2544  N N   . MET A  1 318 ? -72.584  25.389  -88.030  1.00 25.62  ? 318 MET A N   1 
ATOM   2545  C CA  . MET A  1 318 ? -72.713  26.140  -86.788  1.00 25.66  ? 318 MET A CA  1 
ATOM   2546  C C   . MET A  1 318 ? -73.606  27.390  -86.892  1.00 26.28  ? 318 MET A C   1 
ATOM   2547  O O   . MET A  1 318 ? -73.859  28.036  -85.877  1.00 26.25  ? 318 MET A O   1 
ATOM   2548  C CB  . MET A  1 318 ? -71.344  26.577  -86.279  1.00 25.04  ? 318 MET A CB  1 
ATOM   2549  C CG  . MET A  1 318 ? -70.571  25.484  -85.625  1.00 25.19  ? 318 MET A CG  1 
ATOM   2550  S SD  . MET A  1 318 ? -69.065  26.161  -84.907  1.00 27.74  ? 318 MET A SD  1 
ATOM   2551  C CE  . MET A  1 318 ? -68.176  26.853  -86.305  1.00 25.68  ? 318 MET A CE  1 
ATOM   2552  N N   . LYS A  1 319 ? -74.143  27.719  -88.070  1.00 27.03  ? 319 LYS A N   1 
ATOM   2553  C CA  . LYS A  1 319 ? -74.930  28.936  -88.191  1.00 30.35  ? 319 LYS A CA  1 
ATOM   2554  C C   . LYS A  1 319 ? -76.209  28.830  -87.369  1.00 30.75  ? 319 LYS A C   1 
ATOM   2555  O O   . LYS A  1 319 ? -76.693  29.831  -86.846  1.00 29.94  ? 319 LYS A O   1 
ATOM   2556  C CB  . LYS A  1 319 ? -75.197  29.238  -89.663  1.00 34.50  ? 319 LYS A CB  1 
ATOM   2557  C CG  . LYS A  1 319 ? -73.962  29.717  -90.459  1.00 37.79  ? 319 LYS A CG  1 
ATOM   2558  C CD  . LYS A  1 319 ? -74.399  30.403  -91.752  1.00 43.35  ? 319 LYS A CD  1 
ATOM   2559  C CE  . LYS A  1 319 ? -73.322  30.881  -92.682  1.00 48.97  ? 319 LYS A CE  1 
ATOM   2560  N NZ  . LYS A  1 319 ? -73.663  30.544  -94.081  1.00 50.84  ? 319 LYS A NZ  1 
ATOM   2561  N N   . GLY A  1 320 ? -76.768  27.611  -87.265  1.00 29.54  ? 320 GLY A N   1 
ATOM   2562  C CA  . GLY A  1 320 ? -77.988  27.411  -86.501  1.00 28.66  ? 320 GLY A CA  1 
ATOM   2563  C C   . GLY A  1 320 ? -78.033  26.000  -85.927  1.00 28.25  ? 320 GLY A C   1 
ATOM   2564  O O   . GLY A  1 320 ? -78.121  25.038  -86.677  1.00 27.98  ? 320 GLY A O   1 
ATOM   2565  N N   . LEU A  1 321 ? -77.955  25.897  -84.603  1.00 27.22  ? 321 LEU A N   1 
ATOM   2566  C CA  . LEU A  1 321 ? -77.816  24.630  -83.929  1.00 26.59  ? 321 LEU A CA  1 
ATOM   2567  C C   . LEU A  1 321 ? -79.170  24.228  -83.338  1.00 29.15  ? 321 LEU A C   1 
ATOM   2568  O O   . LEU A  1 321 ? -79.910  25.081  -82.810  1.00 27.97  ? 321 LEU A O   1 
ATOM   2569  C CB  . LEU A  1 321 ? -76.759  24.809  -82.858  1.00 26.37  ? 321 LEU A CB  1 
ATOM   2570  C CG  . LEU A  1 321 ? -75.315  24.887  -83.353  1.00 26.17  ? 321 LEU A CG  1 
ATOM   2571  C CD1 . LEU A  1 321 ? -74.468  25.062  -82.114  1.00 26.06  ? 321 LEU A CD1 1 
ATOM   2572  C CD2 . LEU A  1 321 ? -74.866  23.665  -84.185  1.00 25.69  ? 321 LEU A CD2 1 
ATOM   2573  N N   . ILE A  1 322 ? -79.500  22.929  -83.539  1.00 28.23  ? 322 ILE A N   1 
ATOM   2574  C CA  . ILE A  1 322 ? -80.680  22.298  -82.980  1.00 26.94  ? 322 ILE A CA  1 
ATOM   2575  C C   . ILE A  1 322 ? -80.257  21.469  -81.781  1.00 26.99  ? 322 ILE A C   1 
ATOM   2576  O O   . ILE A  1 322 ? -79.570  20.444  -81.959  1.00 28.03  ? 322 ILE A O   1 
ATOM   2577  C CB  . ILE A  1 322 ? -81.384  21.406  -84.005  1.00 26.62  ? 322 ILE A CB  1 
ATOM   2578  C CG1 . ILE A  1 322 ? -81.590  22.137  -85.321  1.00 27.37  ? 322 ILE A CG1 1 
ATOM   2579  C CG2 . ILE A  1 322 ? -82.680  20.872  -83.393  1.00 27.01  ? 322 ILE A CG2 1 
ATOM   2580  C CD1 . ILE A  1 322 ? -81.935  21.230  -86.498  1.00 27.41  ? 322 ILE A CD1 1 
ATOM   2581  N N   . ILE A  1 323 ? -80.703  21.912  -80.599  1.00 26.69  ? 323 ILE A N   1 
ATOM   2582  C CA  . ILE A  1 323 ? -80.453  21.211  -79.362  1.00 28.07  ? 323 ILE A CA  1 
ATOM   2583  C C   . ILE A  1 323 ? -81.630  20.298  -79.034  1.00 29.29  ? 323 ILE A C   1 
ATOM   2584  O O   . ILE A  1 323 ? -81.371  19.183  -78.612  1.00 31.31  ? 323 ILE A O   1 
ATOM   2585  C CB  . ILE A  1 323 ? -80.130  22.184  -78.216  1.00 30.71  ? 323 ILE A CB  1 
ATOM   2586  C CG1 . ILE A  1 323 ? -78.715  22.752  -78.340  1.00 30.92  ? 323 ILE A CG1 1 
ATOM   2587  C CG2 . ILE A  1 323 ? -80.281  21.492  -76.862  1.00 32.80  ? 323 ILE A CG2 1 
ATOM   2588  C CD1 . ILE A  1 323 ? -78.516  23.733  -79.465  1.00 32.08  ? 323 ILE A CD1 1 
ATOM   2589  N N   . SER A  1 324 ? -82.889  20.751  -79.197  1.00 28.71  ? 324 SER A N   1 
ATOM   2590  C CA  . SER A  1 324 ? -84.064  19.890  -79.091  1.00 29.25  ? 324 SER A CA  1 
ATOM   2591  C C   . SER A  1 324 ? -85.037  20.194  -80.228  1.00 30.86  ? 324 SER A C   1 
ATOM   2592  O O   . SER A  1 324 ? -85.169  21.349  -80.645  1.00 32.38  ? 324 SER A O   1 
ATOM   2593  C CB  . SER A  1 324 ? -84.785  20.012  -77.767  1.00 29.86  ? 324 SER A CB  1 
ATOM   2594  O OG  . SER A  1 324 ? -83.868  20.037  -76.680  1.00 30.66  ? 324 SER A OG  1 
ATOM   2595  N N   . PRO A  1 325 ? -85.746  19.193  -80.796  1.00 30.14  ? 325 PRO A N   1 
ATOM   2596  C CA  . PRO A  1 325 ? -85.676  17.796  -80.378  1.00 30.03  ? 325 PRO A CA  1 
ATOM   2597  C C   . PRO A  1 325 ? -84.368  17.195  -80.872  1.00 29.78  ? 325 PRO A C   1 
ATOM   2598  O O   . PRO A  1 325 ? -83.688  17.794  -81.707  1.00 27.75  ? 325 PRO A O   1 
ATOM   2599  C CB  . PRO A  1 325 ? -86.873  17.143  -81.058  1.00 30.99  ? 325 PRO A CB  1 
ATOM   2600  C CG  . PRO A  1 325 ? -87.031  17.945  -82.332  1.00 31.09  ? 325 PRO A CG  1 
ATOM   2601  C CD  . PRO A  1 325 ? -86.579  19.360  -81.986  1.00 31.06  ? 325 PRO A CD  1 
ATOM   2602  N N   . LYS A  1 326 ? -84.037  16.017  -80.335  1.00 29.85  ? 326 LYS A N   1 
ATOM   2603  C CA  . LYS A  1 326 ? -82.758  15.404  -80.633  1.00 29.15  ? 326 LYS A CA  1 
ATOM   2604  C C   . LYS A  1 326 ? -82.945  14.332  -81.700  1.00 28.83  ? 326 LYS A C   1 
ATOM   2605  O O   . LYS A  1 326 ? -84.021  13.738  -81.841  1.00 27.98  ? 326 LYS A O   1 
ATOM   2606  C CB  . LYS A  1 326 ? -82.198  14.873  -79.315  1.00 29.52  ? 326 LYS A CB  1 
ATOM   2607  C CG  . LYS A  1 326 ? -81.724  15.944  -78.377  1.00 29.08  ? 326 LYS A CG  1 
ATOM   2608  C CD  . LYS A  1 326 ? -81.423  15.448  -76.977  1.00 29.34  ? 326 LYS A CD  1 
ATOM   2609  C CE  . LYS A  1 326 ? -80.565  16.445  -76.250  1.00 31.03  ? 326 LYS A CE  1 
ATOM   2610  N NZ  . LYS A  1 326 ? -81.320  17.667  -75.968  1.00 33.23  ? 326 LYS A NZ  1 
ATOM   2611  N N   . ASN A  1 327 ? -81.877  14.104  -82.461  1.00 27.14  ? 327 ASN A N   1 
ATOM   2612  C CA  . ASN A  1 327 ? -81.921  13.072  -83.479  1.00 28.30  ? 327 ASN A CA  1 
ATOM   2613  C C   . ASN A  1 327 ? -81.987  11.709  -82.778  1.00 27.46  ? 327 ASN A C   1 
ATOM   2614  O O   . ASN A  1 327 ? -81.233  11.463  -81.829  1.00 26.54  ? 327 ASN A O   1 
ATOM   2615  C CB  . ASN A  1 327 ? -80.772  13.255  -84.467  1.00 27.65  ? 327 ASN A CB  1 
ATOM   2616  C CG  . ASN A  1 327 ? -80.810  12.319  -85.656  1.00 28.10  ? 327 ASN A CG  1 
ATOM   2617  O OD1 . ASN A  1 327 ? -81.795  12.255  -86.403  1.00 27.88  ? 327 ASN A OD1 1 
ATOM   2618  N ND2 . ASN A  1 327 ? -79.703  11.632  -85.903  1.00 30.40  ? 327 ASN A ND2 1 
ATOM   2619  N N   . LYS A  1 328 ? -82.857  10.840  -83.306  1.00 26.54  ? 328 LYS A N   1 
ATOM   2620  C CA  . LYS A  1 328 ? -83.062  9.483   -82.818  1.00 28.87  ? 328 LYS A CA  1 
ATOM   2621  C C   . LYS A  1 328 ? -83.666  9.527   -81.414  1.00 28.68  ? 328 LYS A C   1 
ATOM   2622  O O   . LYS A  1 328 ? -83.380  8.675   -80.580  1.00 26.65  ? 328 LYS A O   1 
ATOM   2623  C CB  . LYS A  1 328 ? -81.795  8.614   -82.902  1.00 29.79  ? 328 LYS A CB  1 
ATOM   2624  C CG  . LYS A  1 328 ? -81.121  8.571   -84.293  1.00 31.45  ? 328 LYS A CG  1 
ATOM   2625  C CD  . LYS A  1 328 ? -82.005  7.960   -85.386  1.00 34.02  ? 328 LYS A CD  1 
ATOM   2626  C CE  . LYS A  1 328 ? -81.476  7.961   -86.778  1.00 32.16  ? 328 LYS A CE  1 
ATOM   2627  N NZ  . LYS A  1 328 ? -80.343  7.066   -86.836  1.00 30.83  ? 328 LYS A NZ  1 
ATOM   2628  N N   . SER A  1 329 ? -84.558  10.503  -81.182  1.00 29.52  ? 329 SER A N   1 
ATOM   2629  C CA  . SER A  1 329 ? -85.218  10.649  -79.897  1.00 30.35  ? 329 SER A CA  1 
ATOM   2630  C C   . SER A  1 329 ? -86.613  10.037  -79.986  1.00 34.11  ? 329 SER A C   1 
ATOM   2631  O O   . SER A  1 329 ? -87.215  9.991   -81.061  1.00 35.23  ? 329 SER A O   1 
ATOM   2632  C CB  . SER A  1 329 ? -85.256  12.118  -79.459  1.00 28.87  ? 329 SER A CB  1 
ATOM   2633  O OG  . SER A  1 329 ? -85.960  12.932  -80.385  1.00 27.35  ? 329 SER A OG  1 
ATOM   2634  N N   . ILE A  1 330 ? -87.147  9.605   -78.840  1.00 36.66  ? 330 ILE A N   1 
ATOM   2635  C CA  . ILE A  1 330 ? -88.464  8.999   -78.805  1.00 37.78  ? 330 ILE A CA  1 
ATOM   2636  C C   . ILE A  1 330 ? -89.411  9.939   -78.059  1.00 38.98  ? 330 ILE A C   1 
ATOM   2637  O O   . ILE A  1 330 ? -89.052  10.459  -77.026  1.00 37.95  ? 330 ILE A O   1 
ATOM   2638  C CB  . ILE A  1 330 ? -88.319  7.606   -78.164  1.00 38.98  ? 330 ILE A CB  1 
ATOM   2639  C CG1 . ILE A  1 330 ? -87.440  6.716   -79.055  1.00 38.95  ? 330 ILE A CG1 1 
ATOM   2640  C CG2 . ILE A  1 330 ? -89.682  6.970   -77.881  1.00 39.17  ? 330 ILE A CG2 1 
ATOM   2641  C CD1 . ILE A  1 330 ? -86.593  5.705   -78.305  1.00 41.18  ? 330 ILE A CD1 1 
ATOM   2642  N N   . HIS A  1 331 ? -90.624  10.144  -78.578  1.00 40.32  ? 331 HIS A N   1 
ATOM   2643  C CA  . HIS A  1 331 ? -91.582  11.093  -78.015  1.00 40.73  ? 331 HIS A CA  1 
ATOM   2644  C C   . HIS A  1 331 ? -92.950  10.434  -77.873  1.00 42.08  ? 331 HIS A C   1 
ATOM   2645  O O   . HIS A  1 331 ? -93.367  9.676   -78.746  1.00 41.26  ? 331 HIS A O   1 
ATOM   2646  C CB  . HIS A  1 331 ? -91.624  12.374  -78.862  1.00 40.01  ? 331 HIS A CB  1 
ATOM   2647  C CG  . HIS A  1 331 ? -90.327  13.122  -78.747  1.00 38.85  ? 331 HIS A CG  1 
ATOM   2648  N ND1 . HIS A  1 331 ? -90.097  14.083  -77.788  1.00 38.47  ? 331 HIS A ND1 1 
ATOM   2649  C CD2 . HIS A  1 331 ? -89.167  12.956  -79.376  1.00 38.43  ? 331 HIS A CD2 1 
ATOM   2650  C CE1 . HIS A  1 331 ? -88.839  14.483  -77.866  1.00 38.28  ? 331 HIS A CE1 1 
ATOM   2651  N NE2 . HIS A  1 331 ? -88.264  13.843  -78.847  1.00 37.49  ? 331 HIS A NE2 1 
ATOM   2652  N N   . THR A  1 332 ? -93.611  10.694  -76.739  1.00 44.55  ? 332 THR A N   1 
ATOM   2653  C CA  . THR A  1 332 ? -94.909  10.116  -76.438  1.00 46.54  ? 332 THR A CA  1 
ATOM   2654  C C   . THR A  1 332 ? -95.850  11.261  -76.081  1.00 50.69  ? 332 THR A C   1 
ATOM   2655  O O   . THR A  1 332 ? -96.835  11.075  -75.392  1.00 66.00  ? 332 THR A O   1 
ATOM   2656  C CB  . THR A  1 332 ? -94.804  9.057   -75.333  1.00 45.17  ? 332 THR A CB  1 
ATOM   2657  O OG1 . THR A  1 332 ? -94.079  9.731   -74.319  1.00 48.27  ? 332 THR A OG1 1 
ATOM   2658  C CG2 . THR A  1 332 ? -93.961  7.840   -75.671  1.00 43.14  ? 332 THR A CG2 1 
ATOM   2659  N N   . ASN A  1 333 ? -95.594  12.437  -76.637  1.00 54.43  ? 333 ASN A N   1 
ATOM   2660  C CA  . ASN A  1 333 ? -96.420  13.620  -76.449  1.00 55.23  ? 333 ASN A CA  1 
ATOM   2661  C C   . ASN A  1 333 ? -96.728  14.156  -77.852  1.00 54.82  ? 333 ASN A C   1 
ATOM   2662  O O   . ASN A  1 333 ? -96.078  13.747  -78.819  1.00 62.60  ? 333 ASN A O   1 
ATOM   2663  C CB  . ASN A  1 333 ? -95.664  14.594  -75.545  1.00 59.97  ? 333 ASN A CB  1 
ATOM   2664  C CG  . ASN A  1 333 ? -96.551  15.490  -74.705  1.00 69.71  ? 333 ASN A CG  1 
ATOM   2665  O OD1 . ASN A  1 333 ? -97.363  16.273  -75.222  1.00 66.63  ? 333 ASN A OD1 1 
ATOM   2666  N ND2 . ASN A  1 333 ? -96.376  15.428  -73.394  1.00 74.73  ? 333 ASN A ND2 1 
ATOM   2667  N N   . THR A  1 334 ? -97.727  15.039  -77.989  1.00 50.95  ? 334 THR A N   1 
ATOM   2668  C CA  . THR A  1 334 ? -97.936  15.786  -79.222  1.00 48.79  ? 334 THR A CA  1 
ATOM   2669  C C   . THR A  1 334 ? -97.131  17.084  -79.149  1.00 47.88  ? 334 THR A C   1 
ATOM   2670  O O   . THR A  1 334 ? -96.968  17.763  -80.151  1.00 45.01  ? 334 THR A O   1 
ATOM   2671  C CB  . THR A  1 334 ? -99.419  16.079  -79.475  1.00 52.50  ? 334 THR A CB  1 
ATOM   2672  O OG1 . THR A  1 334 ? -99.963  16.762  -78.353  1.00 53.48  ? 334 THR A OG1 1 
ATOM   2673  C CG2 . THR A  1 334 ? -100.288 14.844  -79.624  1.00 54.40  ? 334 THR A CG2 1 
ATOM   2674  N N   . LYS A  1 335 ? -96.646  17.436  -77.952  1.00 48.62  ? 335 LYS A N   1 
ATOM   2675  C CA  . LYS A  1 335 ? -95.839  18.624  -77.749  1.00 47.86  ? 335 LYS A CA  1 
ATOM   2676  C C   . LYS A  1 335 ? -94.399  18.204  -77.534  1.00 45.79  ? 335 LYS A C   1 
ATOM   2677  O O   . LYS A  1 335 ? -94.127  17.414  -76.635  1.00 46.76  ? 335 LYS A O   1 
ATOM   2678  C CB  . LYS A  1 335 ? -96.273  19.429  -76.522  1.00 53.98  ? 335 LYS A CB  1 
ATOM   2679  C CG  . LYS A  1 335 ? -97.725  19.954  -76.536  1.00 56.37  ? 335 LYS A CG  1 
ATOM   2680  C CD  . LYS A  1 335 ? -98.088  20.874  -77.698  1.00 59.16  ? 335 LYS A CD  1 
ATOM   2681  C CE  . LYS A  1 335 ? -99.492  21.421  -77.564  1.00 65.67  ? 335 LYS A CE  1 
ATOM   2682  N NZ  . LYS A  1 335 ? -99.826  22.392  -78.612  1.00 67.37  ? 335 LYS A NZ  1 
ATOM   2683  N N   . ILE A  1 336 ? -93.525  18.747  -78.391  1.00 43.83  ? 336 ILE A N   1 
ATOM   2684  C CA  . ILE A  1 336 ? -92.110  18.422  -78.473  1.00 43.89  ? 336 ILE A CA  1 
ATOM   2685  C C   . ILE A  1 336 ? -91.349  19.706  -78.120  1.00 42.01  ? 336 ILE A C   1 
ATOM   2686  O O   . ILE A  1 336 ? -91.525  20.743  -78.770  1.00 40.28  ? 336 ILE A O   1 
ATOM   2687  C CB  . ILE A  1 336 ? -91.761  17.915  -79.899  1.00 45.86  ? 336 ILE A CB  1 
ATOM   2688  C CG1 . ILE A  1 336 ? -92.514  16.645  -80.271  1.00 49.86  ? 336 ILE A CG1 1 
ATOM   2689  C CG2 . ILE A  1 336 ? -90.264  17.713  -80.120  1.00 46.39  ? 336 ILE A CG2 1 
ATOM   2690  C CD1 . ILE A  1 336 ? -92.576  15.624  -79.155  1.00 50.59  ? 336 ILE A CD1 1 
ATOM   2691  N N   . PRO A  1 337 ? -90.515  19.715  -77.055  1.00 38.84  ? 337 PRO A N   1 
ATOM   2692  C CA  . PRO A  1 337 ? -89.651  20.870  -76.815  1.00 36.47  ? 337 PRO A CA  1 
ATOM   2693  C C   . PRO A  1 337 ? -88.783  21.160  -78.038  1.00 35.00  ? 337 PRO A C   1 
ATOM   2694  O O   . PRO A  1 337 ? -88.287  20.235  -78.679  1.00 32.40  ? 337 PRO A O   1 
ATOM   2695  C CB  . PRO A  1 337 ? -88.859  20.530  -75.545  1.00 35.94  ? 337 PRO A CB  1 
ATOM   2696  C CG  . PRO A  1 337 ? -89.715  19.484  -74.856  1.00 38.18  ? 337 PRO A CG  1 
ATOM   2697  C CD  . PRO A  1 337 ? -90.472  18.721  -75.964  1.00 37.72  ? 337 PRO A CD  1 
ATOM   2698  N N   . LEU A  1 338 ? -88.711  22.460  -78.385  1.00 34.95  ? 338 LEU A N   1 
ATOM   2699  C CA  . LEU A  1 338 ? -87.798  23.003  -79.376  1.00 35.31  ? 338 LEU A CA  1 
ATOM   2700  C C   . LEU A  1 338 ? -86.757  23.892  -78.691  1.00 34.31  ? 338 LEU A C   1 
ATOM   2701  O O   . LEU A  1 338 ? -87.099  24.802  -77.942  1.00 32.22  ? 338 LEU A O   1 
ATOM   2702  C CB  . LEU A  1 338 ? -88.613  23.787  -80.405  1.00 38.34  ? 338 LEU A CB  1 
ATOM   2703  C CG  . LEU A  1 338 ? -87.806  24.571  -81.453  1.00 38.73  ? 338 LEU A CG  1 
ATOM   2704  C CD1 . LEU A  1 338 ? -87.148  23.657  -82.447  1.00 38.25  ? 338 LEU A CD1 1 
ATOM   2705  C CD2 . LEU A  1 338 ? -88.686  25.562  -82.206  1.00 42.22  ? 338 LEU A CD2 1 
ATOM   2706  N N   . GLU A  1 339 ? -85.468  23.628  -78.972  1.00 36.46  ? 339 GLU A N   1 
ATOM   2707  C CA  . GLU A  1 339 ? -84.372  24.417  -78.427  1.00 34.78  ? 339 GLU A CA  1 
ATOM   2708  C C   . GLU A  1 339 ? -83.376  24.701  -79.536  1.00 34.70  ? 339 GLU A C   1 
ATOM   2709  O O   . GLU A  1 339 ? -82.805  23.762  -80.101  1.00 33.67  ? 339 GLU A O   1 
ATOM   2710  C CB  . GLU A  1 339 ? -83.684  23.686  -77.276  1.00 34.81  ? 339 GLU A CB  1 
ATOM   2711  C CG  . GLU A  1 339 ? -84.521  23.607  -75.998  1.00 36.02  ? 339 GLU A CG  1 
ATOM   2712  C CD  . GLU A  1 339 ? -83.753  23.103  -74.786  1.00 37.57  ? 339 GLU A CD  1 
ATOM   2713  O OE1 . GLU A  1 339 ? -83.474  21.891  -74.720  1.00 38.65  ? 339 GLU A OE1 1 
ATOM   2714  O OE2 . GLU A  1 339 ? -83.372  23.926  -73.933  1.00 37.89  ? 339 GLU A OE2 1 
ATOM   2715  N N   . LEU A  1 340 ? -83.140  25.998  -79.799  1.00 33.85  ? 340 LEU A N   1 
ATOM   2716  C CA  . LEU A  1 340 ? -82.229  26.407  -80.863  1.00 32.99  ? 340 LEU A CA  1 
ATOM   2717  C C   . LEU A  1 340 ? -81.161  27.352  -80.333  1.00 31.70  ? 340 LEU A C   1 
ATOM   2718  O O   . LEU A  1 340 ? -81.395  28.097  -79.394  1.00 34.99  ? 340 LEU A O   1 
ATOM   2719  C CB  . LEU A  1 340 ? -82.993  27.070  -82.008  1.00 33.04  ? 340 LEU A CB  1 
ATOM   2720  C CG  . LEU A  1 340 ? -84.029  26.209  -82.736  1.00 34.21  ? 340 LEU A CG  1 
ATOM   2721  C CD1 . LEU A  1 340 ? -84.593  27.088  -83.864  1.00 35.02  ? 340 LEU A CD1 1 
ATOM   2722  C CD2 . LEU A  1 340 ? -83.432  24.892  -83.274  1.00 33.88  ? 340 LEU A CD2 1 
ATOM   2723  N N   . TYR A  1 341 ? -80.002  27.343  -80.993  1.00 31.12  ? 341 TYR A N   1 
ATOM   2724  C CA  . TYR A  1 341 ? -78.940  28.307  -80.739  1.00 30.78  ? 341 TYR A CA  1 
ATOM   2725  C C   . TYR A  1 341 ? -78.511  28.878  -82.091  1.00 30.32  ? 341 TYR A C   1 
ATOM   2726  O O   . TYR A  1 341 ? -77.758  28.226  -82.820  1.00 28.99  ? 341 TYR A O   1 
ATOM   2727  C CB  . TYR A  1 341 ? -77.730  27.749  -79.970  1.00 30.40  ? 341 TYR A CB  1 
ATOM   2728  C CG  . TYR A  1 341 ? -76.879  28.882  -79.392  1.00 29.95  ? 341 TYR A CG  1 
ATOM   2729  C CD1 . TYR A  1 341 ? -77.293  29.576  -78.267  1.00 29.69  ? 341 TYR A CD1 1 
ATOM   2730  C CD2 . TYR A  1 341 ? -75.676  29.259  -79.960  1.00 30.23  ? 341 TYR A CD2 1 
ATOM   2731  C CE1 . TYR A  1 341 ? -76.557  30.604  -77.719  1.00 29.60  ? 341 TYR A CE1 1 
ATOM   2732  C CE2 . TYR A  1 341 ? -74.918  30.292  -79.428  1.00 30.84  ? 341 TYR A CE2 1 
ATOM   2733  C CZ  . TYR A  1 341 ? -75.361  30.975  -78.305  1.00 31.17  ? 341 TYR A CZ  1 
ATOM   2734  O OH  . TYR A  1 341 ? -74.639  31.992  -77.747  1.00 28.96  ? 341 TYR A OH  1 
ATOM   2735  N N   . ASN A  1 342 ? -79.014  30.090  -82.402  1.00 31.28  ? 342 ASN A N   1 
ATOM   2736  C CA  . ASN A  1 342 ? -78.860  30.705  -83.712  1.00 31.56  ? 342 ASN A CA  1 
ATOM   2737  C C   . ASN A  1 342 ? -77.750  31.745  -83.702  1.00 31.34  ? 342 ASN A C   1 
ATOM   2738  O O   . ASN A  1 342 ? -77.644  32.536  -82.776  1.00 34.45  ? 342 ASN A O   1 
ATOM   2739  C CB  . ASN A  1 342 ? -80.145  31.386  -84.165  1.00 30.70  ? 342 ASN A CB  1 
ATOM   2740  C CG  . ASN A  1 342 ? -81.276  30.393  -84.268  1.00 31.16  ? 342 ASN A CG  1 
ATOM   2741  O OD1 . ASN A  1 342 ? -81.098  29.369  -84.916  1.00 30.91  ? 342 ASN A OD1 1 
ATOM   2742  N ND2 . ASN A  1 342 ? -82.417  30.635  -83.637  1.00 31.50  ? 342 ASN A ND2 1 
ATOM   2743  N N   . ASP A  1 343 ? -76.985  31.836  -84.784  1.00 32.85  ? 343 ASP A N   1 
ATOM   2744  C CA  . ASP A  1 343 ? -76.078  32.969  -84.912  1.00 35.28  ? 343 ASP A CA  1 
ATOM   2745  C C   . ASP A  1 343 ? -76.874  34.132  -85.475  1.00 33.13  ? 343 ASP A C   1 
ATOM   2746  O O   . ASP A  1 343 ? -78.013  33.946  -85.838  1.00 32.52  ? 343 ASP A O   1 
ATOM   2747  C CB  . ASP A  1 343 ? -74.791  32.619  -85.646  1.00 34.72  ? 343 ASP A CB  1 
ATOM   2748  C CG  . ASP A  1 343 ? -74.841  32.654  -87.159  1.00 36.33  ? 343 ASP A CG  1 
ATOM   2749  O OD1 . ASP A  1 343 ? -75.878  33.108  -87.717  1.00 39.43  ? 343 ASP A OD1 1 
ATOM   2750  O OD2 . ASP A  1 343 ? -73.870  32.167  -87.759  1.00 38.98  ? 343 ASP A OD2 1 
ATOM   2751  N N   . LYS A  1 344 ? -76.232  35.289  -85.637  1.00 37.61  ? 344 LYS A N   1 
ATOM   2752  C CA  . LYS A  1 344 ? -76.937  36.552  -85.893  1.00 42.92  ? 344 LYS A CA  1 
ATOM   2753  C C   . LYS A  1 344 ? -77.478  36.634  -87.328  1.00 39.39  ? 344 LYS A C   1 
ATOM   2754  O O   . LYS A  1 344 ? -78.273  37.539  -87.609  1.00 40.00  ? 344 LYS A O   1 
ATOM   2755  C CB  . LYS A  1 344 ? -76.098  37.785  -85.517  1.00 49.62  ? 344 LYS A CB  1 
ATOM   2756  C CG  . LYS A  1 344 ? -74.861  38.003  -86.371  1.00 61.86  ? 344 LYS A CG  1 
ATOM   2757  C CD  . LYS A  1 344 ? -73.702  38.712  -85.666  1.00 75.32  ? 344 LYS A CD  1 
ATOM   2758  C CE  . LYS A  1 344 ? -72.488  38.931  -86.558  1.00 78.03  ? 344 LYS A CE  1 
ATOM   2759  N NZ  . LYS A  1 344 ? -72.063  37.754  -87.334  1.00 74.30  ? 344 LYS A NZ  1 
ATOM   2760  N N   . ASP A  1 345 ? -77.148  35.638  -88.184  1.00 36.45  ? 345 ASP A N   1 
ATOM   2761  C CA  . ASP A  1 345 ? -77.572  35.608  -89.583  1.00 36.70  ? 345 ASP A CA  1 
ATOM   2762  C C   . ASP A  1 345 ? -78.912  34.886  -89.792  1.00 36.70  ? 345 ASP A C   1 
ATOM   2763  O O   . ASP A  1 345 ? -79.549  35.074  -90.826  1.00 34.40  ? 345 ASP A O   1 
ATOM   2764  C CB  . ASP A  1 345 ? -76.483  35.005  -90.447  1.00 37.53  ? 345 ASP A CB  1 
ATOM   2765  C CG  . ASP A  1 345 ? -75.245  35.876  -90.585  1.00 38.86  ? 345 ASP A CG  1 
ATOM   2766  O OD1 . ASP A  1 345 ? -75.364  37.114  -90.426  1.00 42.93  ? 345 ASP A OD1 1 
ATOM   2767  O OD2 . ASP A  1 345 ? -74.193  35.316  -90.875  1.00 38.49  ? 345 ASP A OD2 1 
ATOM   2768  N N   . VAL A  1 346 ? -79.335  34.071  -88.809  1.00 35.80  ? 346 VAL A N   1 
ATOM   2769  C CA  . VAL A  1 346 ? -80.586  33.348  -88.876  1.00 34.25  ? 346 VAL A CA  1 
ATOM   2770  C C   . VAL A  1 346 ? -81.705  34.295  -88.487  1.00 37.18  ? 346 VAL A C   1 
ATOM   2771  O O   . VAL A  1 346 ? -81.702  34.797  -87.362  1.00 37.94  ? 346 VAL A O   1 
ATOM   2772  C CB  . VAL A  1 346 ? -80.571  32.144  -87.924  1.00 34.28  ? 346 VAL A CB  1 
ATOM   2773  C CG1 . VAL A  1 346 ? -81.949  31.507  -87.871  1.00 33.73  ? 346 VAL A CG1 1 
ATOM   2774  C CG2 . VAL A  1 346 ? -79.490  31.105  -88.296  1.00 33.75  ? 346 VAL A CG2 1 
ATOM   2775  N N   . LYS A  1 347 ? -82.630  34.543  -89.421  1.00 37.37  ? 347 LYS A N   1 
ATOM   2776  C CA  . LYS A  1 347 ? -83.748  35.442  -89.176  1.00 38.22  ? 347 LYS A CA  1 
ATOM   2777  C C   . LYS A  1 347 ? -85.073  34.699  -89.237  1.00 38.76  ? 347 LYS A C   1 
ATOM   2778  O O   . LYS A  1 347 ? -86.111  35.299  -88.926  1.00 39.53  ? 347 LYS A O   1 
ATOM   2779  C CB  . LYS A  1 347 ? -83.904  36.547  -90.231  1.00 40.49  ? 347 LYS A CB  1 
ATOM   2780  C CG  . LYS A  1 347 ? -82.707  37.466  -90.384  1.00 41.94  ? 347 LYS A CG  1 
ATOM   2781  C CD  . LYS A  1 347 ? -82.238  38.122  -89.088  1.00 42.68  ? 347 LYS A CD  1 
ATOM   2782  C CE  . LYS A  1 347 ? -80.945  38.828  -89.313  1.00 44.91  ? 347 LYS A CE  1 
ATOM   2783  N NZ  . LYS A  1 347 ? -80.543  39.494  -88.080  1.00 46.67  ? 347 LYS A NZ  1 
ATOM   2784  N N   . LYS A  1 348 ? -85.049  33.424  -89.670  1.00 37.68  ? 348 LYS A N   1 
ATOM   2785  C CA  . LYS A  1 348 ? -86.269  32.621  -89.716  1.00 37.78  ? 348 LYS A CA  1 
ATOM   2786  C C   . LYS A  1 348 ? -85.910  31.143  -89.632  1.00 34.94  ? 348 LYS A C   1 
ATOM   2787  O O   . LYS A  1 348 ? -84.949  30.686  -90.238  1.00 32.70  ? 348 LYS A O   1 
ATOM   2788  C CB  . LYS A  1 348 ? -87.114  32.901  -90.970  1.00 38.58  ? 348 LYS A CB  1 
ATOM   2789  C CG  . LYS A  1 348 ? -88.483  32.266  -90.983  1.00 40.29  ? 348 LYS A CG  1 
ATOM   2790  C CD  . LYS A  1 348 ? -89.360  32.602  -92.182  1.00 42.32  ? 348 LYS A CD  1 
ATOM   2791  C CE  . LYS A  1 348 ? -88.818  32.052  -93.477  1.00 45.02  ? 348 LYS A CE  1 
ATOM   2792  N NZ  . LYS A  1 348 ? -89.755  32.185  -94.612  1.00 47.64  ? 348 LYS A NZ  1 
ATOM   2793  N N   . VAL A  1 349 ? -86.727  30.403  -88.890  1.00 36.51  ? 349 VAL A N   1 
ATOM   2794  C CA  . VAL A  1 349 ? -86.614  28.961  -88.825  1.00 36.36  ? 349 VAL A CA  1 
ATOM   2795  C C   . VAL A  1 349 ? -87.951  28.304  -89.151  1.00 37.24  ? 349 VAL A C   1 
ATOM   2796  O O   . VAL A  1 349 ? -88.994  28.633  -88.544  1.00 37.05  ? 349 VAL A O   1 
ATOM   2797  C CB  . VAL A  1 349 ? -86.133  28.565  -87.432  1.00 37.19  ? 349 VAL A CB  1 
ATOM   2798  C CG1 . VAL A  1 349 ? -86.068  27.040  -87.334  1.00 37.77  ? 349 VAL A CG1 1 
ATOM   2799  C CG2 . VAL A  1 349 ? -84.786  29.230  -87.144  1.00 36.29  ? 349 VAL A CG2 1 
ATOM   2800  N N   . VAL A  1 350 ? -87.884  27.351  -90.096  1.00 35.30  ? 350 VAL A N   1 
ATOM   2801  C CA  . VAL A  1 350 ? -89.042  26.552  -90.458  1.00 34.73  ? 350 VAL A CA  1 
ATOM   2802  C C   . VAL A  1 350 ? -88.761  25.075  -90.190  1.00 32.97  ? 350 VAL A C   1 
ATOM   2803  O O   . VAL A  1 350 ? -87.638  24.612  -90.380  1.00 31.43  ? 350 VAL A O   1 
ATOM   2804  C CB  . VAL A  1 350 ? -89.402  26.789  -91.931  1.00 34.80  ? 350 VAL A CB  1 
ATOM   2805  C CG1 . VAL A  1 350 ? -90.528  25.882  -92.414  1.00 36.51  ? 350 VAL A CG1 1 
ATOM   2806  C CG2 . VAL A  1 350 ? -89.746  28.234  -92.181  1.00 34.92  ? 350 VAL A CG2 1 
ATOM   2807  N N   . VAL A  1 351 ? -89.810  24.358  -89.754  1.00 33.46  ? 351 VAL A N   1 
ATOM   2808  C CA  . VAL A  1 351 ? -89.792  22.900  -89.626  1.00 31.17  ? 351 VAL A CA  1 
ATOM   2809  C C   . VAL A  1 351 ? -90.924  22.313  -90.462  1.00 31.38  ? 351 VAL A C   1 
ATOM   2810  O O   . VAL A  1 351 ? -92.089  22.727  -90.376  1.00 30.03  ? 351 VAL A O   1 
ATOM   2811  C CB  . VAL A  1 351 ? -89.881  22.375  -88.184  1.00 31.03  ? 351 VAL A CB  1 
ATOM   2812  C CG1 . VAL A  1 351 ? -89.765  20.854  -88.131  1.00 31.19  ? 351 VAL A CG1 1 
ATOM   2813  C CG2 . VAL A  1 351 ? -88.809  23.006  -87.307  1.00 30.63  ? 351 VAL A CG2 1 
ATOM   2814  N N   . LYS A  1 352 ? -90.553  21.307  -91.258  1.00 31.48  ? 352 LYS A N   1 
ATOM   2815  C CA  . LYS A  1 352 ? -91.495  20.680  -92.162  1.00 33.98  ? 352 LYS A CA  1 
ATOM   2816  C C   . LYS A  1 352 ? -91.536  19.180  -91.905  1.00 32.39  ? 352 LYS A C   1 
ATOM   2817  O O   . LYS A  1 352 ? -90.527  18.578  -91.551  1.00 32.59  ? 352 LYS A O   1 
ATOM   2818  C CB  . LYS A  1 352 ? -91.062  20.921  -93.611  1.00 36.92  ? 352 LYS A CB  1 
ATOM   2819  C CG  . LYS A  1 352 ? -91.588  22.175  -94.280  1.00 38.33  ? 352 LYS A CG  1 
ATOM   2820  C CD  . LYS A  1 352 ? -90.721  22.541  -95.480  1.00 40.66  ? 352 LYS A CD  1 
ATOM   2821  C CE  . LYS A  1 352 ? -91.232  23.840  -96.031  1.00 45.11  ? 352 LYS A CE  1 
ATOM   2822  N NZ  . LYS A  1 352 ? -90.399  24.408  -97.092  1.00 48.06  ? 352 LYS A NZ  1 
ATOM   2823  N N   . PHE A  1 353 ? -92.720  18.601  -92.089  1.00 31.54  ? 353 PHE A N   1 
ATOM   2824  C CA  . PHE A  1 353 ? -92.883  17.164  -92.126  1.00 30.69  ? 353 PHE A CA  1 
ATOM   2825  C C   . PHE A  1 353 ? -93.603  16.840  -93.427  1.00 31.53  ? 353 PHE A C   1 
ATOM   2826  O O   . PHE A  1 353 ? -94.679  17.382  -93.678  1.00 34.59  ? 353 PHE A O   1 
ATOM   2827  C CB  . PHE A  1 353 ? -93.610  16.660  -90.861  1.00 31.04  ? 353 PHE A CB  1 
ATOM   2828  C CG  . PHE A  1 353 ? -93.814  15.143  -90.846  1.00 30.72  ? 353 PHE A CG  1 
ATOM   2829  C CD1 . PHE A  1 353 ? -92.725  14.275  -91.002  1.00 29.04  ? 353 PHE A CD1 1 
ATOM   2830  C CD2 . PHE A  1 353 ? -95.100  14.595  -90.787  1.00 31.10  ? 353 PHE A CD2 1 
ATOM   2831  C CE1 . PHE A  1 353 ? -92.919  12.906  -91.088  1.00 29.90  ? 353 PHE A CE1 1 
ATOM   2832  C CE2 . PHE A  1 353 ? -95.287  13.225  -90.879  1.00 31.09  ? 353 PHE A CE2 1 
ATOM   2833  C CZ  . PHE A  1 353 ? -94.200  12.373  -91.009  1.00 30.66  ? 353 PHE A CZ  1 
ATOM   2834  N N   . ARG A  1 354 ? -93.016  15.979  -94.262  1.00 31.28  ? 354 ARG A N   1 
ATOM   2835  C CA  . ARG A  1 354 ? -93.651  15.569  -95.502  1.00 32.69  ? 354 ARG A CA  1 
ATOM   2836  C C   . ARG A  1 354 ? -94.067  16.797  -96.303  1.00 33.75  ? 354 ARG A C   1 
ATOM   2837  O O   . ARG A  1 354 ? -95.157  16.828  -96.869  1.00 34.81  ? 354 ARG A O   1 
ATOM   2838  C CB  . ARG A  1 354 ? -94.871  14.677  -95.243  1.00 34.09  ? 354 ARG A CB  1 
ATOM   2839  C CG  . ARG A  1 354 ? -94.463  13.316  -94.664  1.00 34.07  ? 354 ARG A CG  1 
ATOM   2840  C CD  . ARG A  1 354 ? -95.662  12.406  -94.500  1.00 33.62  ? 354 ARG A CD  1 
ATOM   2841  N NE  . ARG A  1 354 ? -95.315  11.169  -93.804  1.00 33.11  ? 354 ARG A NE  1 
ATOM   2842  C CZ  . ARG A  1 354 ? -96.208  10.304  -93.332  1.00 33.09  ? 354 ARG A CZ  1 
ATOM   2843  N NH1 . ARG A  1 354 ? -97.481  10.506  -93.524  1.00 34.60  ? 354 ARG A NH1 1 
ATOM   2844  N NH2 . ARG A  1 354 ? -95.828  9.249   -92.636  1.00 32.64  ? 354 ARG A NH2 1 
ATOM   2845  N N   . ASP A  1 355 ? -93.169  17.801  -96.329  1.00 33.14  ? 355 ASP A N   1 
ATOM   2846  C CA  . ASP A  1 355 ? -93.269  18.932  -97.228  1.00 33.79  ? 355 ASP A CA  1 
ATOM   2847  C C   . ASP A  1 355 ? -94.330  19.913  -96.749  1.00 34.63  ? 355 ASP A C   1 
ATOM   2848  O O   . ASP A  1 355 ? -94.629  20.852  -97.486  1.00 35.49  ? 355 ASP A O   1 
ATOM   2849  C CB  . ASP A  1 355 ? -93.464  18.484  -98.665  1.00 34.25  ? 355 ASP A CB  1 
ATOM   2850  C CG  . ASP A  1 355 ? -92.415  17.470  -99.095  1.00 35.44  ? 355 ASP A CG  1 
ATOM   2851  O OD1 . ASP A  1 355 ? -91.188  17.839  -99.106  1.00 35.07  ? 355 ASP A OD1 1 
ATOM   2852  O OD2 . ASP A  1 355 ? -92.816  16.287  -99.301  1.00 35.55  ? 355 ASP A OD2 1 
ATOM   2853  N N   . LYS A  1 356 ? -94.812  19.742  -95.504  1.00 35.45  ? 356 LYS A N   1 
ATOM   2854  C CA  . LYS A  1 356 ? -95.791  20.637  -94.886  1.00 36.96  ? 356 LYS A CA  1 
ATOM   2855  C C   . LYS A  1 356 ? -95.177  21.369  -93.683  1.00 35.33  ? 356 LYS A C   1 
ATOM   2856  O O   . LYS A  1 356 ? -94.516  20.782  -92.825  1.00 35.28  ? 356 LYS A O   1 
ATOM   2857  C CB  . LYS A  1 356 ? -97.041  19.829  -94.531  1.00 38.84  ? 356 LYS A CB  1 
ATOM   2858  C CG  . LYS A  1 356 ? -98.053  20.457  -93.593  1.00 41.45  ? 356 LYS A CG  1 
ATOM   2859  C CD  . LYS A  1 356 ? -99.270  19.545  -93.468  1.00 46.29  ? 356 LYS A CD  1 
ATOM   2860  C CE  . LYS A  1 356 ? -99.797  19.388  -92.062  1.00 50.47  ? 356 LYS A CE  1 
ATOM   2861  N NZ  . LYS A  1 356 ? -101.054 20.105  -91.812  1.00 52.76  ? 356 LYS A NZ  1 
ATOM   2862  N N   . VAL A  1 357 ? -95.409  22.676  -93.634  1.00 34.53  ? 357 VAL A N   1 
ATOM   2863  C CA  . VAL A  1 357 ? -94.956  23.520  -92.544  1.00 33.51  ? 357 VAL A CA  1 
ATOM   2864  C C   . VAL A  1 357 ? -95.708  23.111  -91.286  1.00 33.73  ? 357 VAL A C   1 
ATOM   2865  O O   . VAL A  1 357 ? -96.940  23.141  -91.281  1.00 33.34  ? 357 VAL A O   1 
ATOM   2866  C CB  . VAL A  1 357 ? -95.164  25.028  -92.846  1.00 32.84  ? 357 VAL A CB  1 
ATOM   2867  C CG1 . VAL A  1 357 ? -94.890  25.883  -91.612  1.00 32.26  ? 357 VAL A CG1 1 
ATOM   2868  C CG2 . VAL A  1 357 ? -94.297  25.491  -94.015  1.00 32.18  ? 357 VAL A CG2 1 
ATOM   2869  N N   . ILE A  1 358 ? -94.948  22.759  -90.233  1.00 34.99  ? 358 ILE A N   1 
ATOM   2870  C CA  . ILE A  1 358 ? -95.519  22.547  -88.904  1.00 37.56  ? 358 ILE A CA  1 
ATOM   2871  C C   . ILE A  1 358 ? -95.019  23.609  -87.916  1.00 36.23  ? 358 ILE A C   1 
ATOM   2872  O O   . ILE A  1 358 ? -95.649  23.819  -86.897  1.00 36.64  ? 358 ILE A O   1 
ATOM   2873  C CB  . ILE A  1 358 ? -95.278  21.108  -88.385  1.00 38.17  ? 358 ILE A CB  1 
ATOM   2874  C CG1 . ILE A  1 358 ? -93.814  20.807  -88.159  1.00 38.80  ? 358 ILE A CG1 1 
ATOM   2875  C CG2 . ILE A  1 358 ? -95.932  20.077  -89.309  1.00 38.03  ? 358 ILE A CG2 1 
ATOM   2876  C CD1 . ILE A  1 358 ? -93.585  19.549  -87.340  1.00 40.12  ? 358 ILE A CD1 1 
ATOM   2877  N N   . TYR A  1 359 ? -93.918  24.276  -88.258  1.00 35.03  ? 359 TYR A N   1 
ATOM   2878  C CA  . TYR A  1 359 ? -93.360  25.349  -87.398  1.00 34.05  ? 359 TYR A CA  1 
ATOM   2879  C C   . TYR A  1 359 ? -92.713  26.434  -88.254  1.00 34.54  ? 359 TYR A C   1 
ATOM   2880  O O   . TYR A  1 359 ? -91.950  26.099  -89.162  1.00 34.87  ? 359 TYR A O   1 
ATOM   2881  C CB  . TYR A  1 359 ? -92.372  24.818  -86.362  1.00 32.48  ? 359 TYR A CB  1 
ATOM   2882  C CG  . TYR A  1 359 ? -91.844  25.868  -85.399  1.00 34.24  ? 359 TYR A CG  1 
ATOM   2883  C CD1 . TYR A  1 359 ? -90.728  26.634  -85.709  1.00 35.10  ? 359 TYR A CD1 1 
ATOM   2884  C CD2 . TYR A  1 359 ? -92.469  26.093  -84.181  1.00 36.10  ? 359 TYR A CD2 1 
ATOM   2885  C CE1 . TYR A  1 359 ? -90.253  27.599  -84.841  1.00 34.31  ? 359 TYR A CE1 1 
ATOM   2886  C CE2 . TYR A  1 359 ? -91.998  27.049  -83.301  1.00 37.21  ? 359 TYR A CE2 1 
ATOM   2887  C CZ  . TYR A  1 359 ? -90.890  27.807  -83.634  1.00 36.60  ? 359 TYR A CZ  1 
ATOM   2888  O OH  . TYR A  1 359 ? -90.425  28.746  -82.768  1.00 35.20  ? 359 TYR A OH  1 
ATOM   2889  N N   . SER A  1 360 ? -93.049  27.695  -87.984  1.00 33.88  ? 360 SER A N   1 
ATOM   2890  C CA  . SER A  1 360 ? -92.409  28.849  -88.663  1.00 34.95  ? 360 SER A CA  1 
ATOM   2891  C C   . SER A  1 360 ? -92.238  29.949  -87.610  1.00 36.97  ? 360 SER A C   1 
ATOM   2892  O O   . SER A  1 360 ? -93.163  30.151  -86.817  1.00 39.11  ? 360 SER A O   1 
ATOM   2893  C CB  . SER A  1 360 ? -93.169  29.336  -89.850  1.00 35.41  ? 360 SER A CB  1 
ATOM   2894  O OG  . SER A  1 360 ? -92.312  29.963  -90.788  1.00 34.43  ? 360 SER A OG  1 
ATOM   2895  N N   . LYS A  1 361 ? -91.072  30.588  -87.580  1.00 37.66  ? 361 LYS A N   1 
ATOM   2896  C CA  . LYS A  1 361 ? -90.855  31.683  -86.613  1.00 40.48  ? 361 LYS A CA  1 
ATOM   2897  C C   . LYS A  1 361 ? -89.753  32.658  -87.028  1.00 39.21  ? 361 LYS A C   1 
ATOM   2898  O O   . LYS A  1 361 ? -88.635  32.203  -87.303  1.00 39.84  ? 361 LYS A O   1 
ATOM   2899  C CB  . LYS A  1 361 ? -90.522  31.165  -85.214  1.00 45.62  ? 361 LYS A CB  1 
ATOM   2900  C CG  . LYS A  1 361 ? -90.783  32.127  -84.073  1.00 53.66  ? 361 LYS A CG  1 
ATOM   2901  C CD  . LYS A  1 361 ? -89.677  32.098  -83.028  1.00 60.57  ? 361 LYS A CD  1 
ATOM   2902  C CE  . LYS A  1 361 ? -89.907  33.059  -81.908  1.00 61.82  ? 361 LYS A CE  1 
ATOM   2903  N NZ  . LYS A  1 361 ? -90.756  32.490  -80.860  1.00 61.73  ? 361 LYS A NZ  1 
ATOM   2904  N N   . ASN A  1 362 ? -90.087  33.940  -87.114  1.00 39.90  ? 362 ASN A N   1 
ATOM   2905  C CA  . ASN A  1 362 ? -89.120  35.006  -87.291  1.00 40.15  ? 362 ASN A CA  1 
ATOM   2906  C C   . ASN A  1 362 ? -88.290  35.147  -86.016  1.00 38.45  ? 362 ASN A C   1 
ATOM   2907  O O   . ASN A  1 362 ? -88.835  35.279  -84.930  1.00 38.30  ? 362 ASN A O   1 
ATOM   2908  C CB  . ASN A  1 362 ? -89.823  36.301  -87.697  1.00 43.79  ? 362 ASN A CB  1 
ATOM   2909  C CG  . ASN A  1 362 ? -90.565  36.149  -89.004  1.00 46.47  ? 362 ASN A CG  1 
ATOM   2910  O OD1 . ASN A  1 362 ? -91.791  36.304  -89.037  1.00 54.22  ? 362 ASN A OD1 1 
ATOM   2911  N ND2 . ASN A  1 362 ? -89.864  35.809  -90.076  1.00 46.42  ? 362 ASN A ND2 1 
ATOM   2912  N N   . ILE A  1 363 ? -86.967  35.065  -86.183  1.00 38.62  ? 363 ILE A N   1 
ATOM   2913  C CA  . ILE A  1 363 ? -85.983  35.247  -85.129  1.00 40.13  ? 363 ILE A CA  1 
ATOM   2914  C C   . ILE A  1 363 ? -85.549  36.710  -85.123  1.00 42.50  ? 363 ILE A C   1 
ATOM   2915  O O   . ILE A  1 363 ? -84.949  37.170  -86.096  1.00 42.10  ? 363 ILE A O   1 
ATOM   2916  C CB  . ILE A  1 363 ? -84.750  34.378  -85.402  1.00 38.91  ? 363 ILE A CB  1 
ATOM   2917  C CG1 . ILE A  1 363 ? -85.098  32.936  -85.712  1.00 42.96  ? 363 ILE A CG1 1 
ATOM   2918  C CG2 . ILE A  1 363 ? -83.770  34.477  -84.250  1.00 38.68  ? 363 ILE A CG2 1 
ATOM   2919  C CD1 . ILE A  1 363 ? -86.024  32.292  -84.686  1.00 45.27  ? 363 ILE A CD1 1 
ATOM   2920  N N   . THR A  1 364 ? -85.754  37.412  -84.009  1.00 45.00  ? 364 THR A N   1 
ATOM   2921  C CA  . THR A  1 364 ? -85.339  38.810  -83.940  1.00 51.46  ? 364 THR A CA  1 
ATOM   2922  C C   . THR A  1 364 ? -84.034  38.964  -83.164  1.00 50.82  ? 364 THR A C   1 
ATOM   2923  O O   . THR A  1 364 ? -83.389  40.010  -83.294  1.00 53.24  ? 364 THR A O   1 
ATOM   2924  C CB  . THR A  1 364 ? -86.453  39.688  -83.364  1.00 52.02  ? 364 THR A CB  1 
ATOM   2925  O OG1 . THR A  1 364 ? -87.118  38.884  -82.393  1.00 53.10  ? 364 THR A OG1 1 
ATOM   2926  C CG2 . THR A  1 364 ? -87.470  40.089  -84.416  1.00 52.37  ? 364 THR A CG2 1 
ATOM   2927  N N   . SER A  1 365 ? -83.691  37.958  -82.339  1.00 47.52  ? 365 SER A N   1 
ATOM   2928  C CA  . SER A  1 365 ? -82.442  37.972  -81.589  1.00 46.61  ? 365 SER A CA  1 
ATOM   2929  C C   . SER A  1 365 ? -81.745  36.620  -81.631  1.00 41.73  ? 365 SER A C   1 
ATOM   2930  O O   . SER A  1 365 ? -82.364  35.564  -81.539  1.00 35.70  ? 365 SER A O   1 
ATOM   2931  C CB  . SER A  1 365 ? -82.632  38.402  -80.156  1.00 51.66  ? 365 SER A CB  1 
ATOM   2932  O OG  . SER A  1 365 ? -83.607  37.589  -79.524  1.00 53.20  ? 365 SER A OG  1 
ATOM   2933  N N   . GLU A  1 366 ? -80.421  36.729  -81.683  1.00 38.08  ? 366 GLU A N   1 
ATOM   2934  C CA  . GLU A  1 366 ? -79.530  35.610  -81.792  1.00 38.64  ? 366 GLU A CA  1 
ATOM   2935  C C   . GLU A  1 366 ? -79.466  34.888  -80.453  1.00 36.57  ? 366 GLU A C   1 
ATOM   2936  O O   . GLU A  1 366 ? -80.093  35.309  -79.494  1.00 37.55  ? 366 GLU A O   1 
ATOM   2937  C CB  . GLU A  1 366 ? -78.169  36.151  -82.228  1.00 40.98  ? 366 GLU A CB  1 
ATOM   2938  C CG  . GLU A  1 366 ? -77.382  36.860  -81.138  1.00 41.36  ? 366 GLU A CG  1 
ATOM   2939  C CD  . GLU A  1 366 ? -76.006  37.237  -81.650  1.00 44.36  ? 366 GLU A CD  1 
ATOM   2940  O OE1 . GLU A  1 366 ? -75.183  36.320  -81.799  1.00 47.33  ? 366 GLU A OE1 1 
ATOM   2941  O OE2 . GLU A  1 366 ? -75.739  38.429  -81.900  1.00 47.10  ? 366 GLU A OE2 1 
ATOM   2942  N N   . GLY A  1 367 ? -78.738  33.772  -80.431  1.00 32.66  ? 367 GLY A N   1 
ATOM   2943  C CA  . GLY A  1 367 ? -78.556  33.009  -79.211  1.00 31.88  ? 367 GLY A CA  1 
ATOM   2944  C C   . GLY A  1 367 ? -79.640  31.953  -79.012  1.00 31.12  ? 367 GLY A C   1 
ATOM   2945  O O   . GLY A  1 367 ? -80.252  31.471  -79.970  1.00 29.23  ? 367 GLY A O   1 
ATOM   2946  N N   . TYR A  1 368 ? -79.836  31.605  -77.735  1.00 30.97  ? 368 TYR A N   1 
ATOM   2947  C CA  . TYR A  1 368 ? -80.757  30.554  -77.349  1.00 31.27  ? 368 TYR A CA  1 
ATOM   2948  C C   . TYR A  1 368 ? -82.195  30.996  -77.612  1.00 33.15  ? 368 TYR A C   1 
ATOM   2949  O O   . TYR A  1 368 ? -82.527  32.163  -77.398  1.00 31.06  ? 368 TYR A O   1 
ATOM   2950  C CB  . TYR A  1 368 ? -80.535  30.243  -75.870  1.00 30.87  ? 368 TYR A CB  1 
ATOM   2951  C CG  . TYR A  1 368 ? -81.467  29.183  -75.300  1.00 31.53  ? 368 TYR A CG  1 
ATOM   2952  C CD1 . TYR A  1 368 ? -81.187  27.827  -75.415  1.00 31.96  ? 368 TYR A CD1 1 
ATOM   2953  C CD2 . TYR A  1 368 ? -82.631  29.542  -74.659  1.00 33.53  ? 368 TYR A CD2 1 
ATOM   2954  C CE1 . TYR A  1 368 ? -82.035  26.866  -74.890  1.00 33.16  ? 368 TYR A CE1 1 
ATOM   2955  C CE2 . TYR A  1 368 ? -83.511  28.591  -74.167  1.00 36.26  ? 368 TYR A CE2 1 
ATOM   2956  C CZ  . TYR A  1 368 ? -83.207  27.248  -74.267  1.00 34.86  ? 368 TYR A CZ  1 
ATOM   2957  O OH  . TYR A  1 368 ? -84.102  26.353  -73.763  1.00 37.34  ? 368 TYR A OH  1 
ATOM   2958  N N   . MET A  1 369 ? -83.032  30.048  -78.077  1.00 35.26  ? 369 MET A N   1 
ATOM   2959  C CA  . MET A  1 369 ? -84.479  30.189  -77.959  1.00 37.60  ? 369 MET A CA  1 
ATOM   2960  C C   . MET A  1 369 ? -85.133  28.821  -77.699  1.00 37.12  ? 369 MET A C   1 
ATOM   2961  O O   . MET A  1 369 ? -84.699  27.795  -78.224  1.00 36.25  ? 369 MET A O   1 
ATOM   2962  C CB  . MET A  1 369 ? -85.087  30.875  -79.189  1.00 40.66  ? 369 MET A CB  1 
ATOM   2963  C CG  . MET A  1 369 ? -84.809  30.168  -80.509  1.00 47.28  ? 369 MET A CG  1 
ATOM   2964  S SD  . MET A  1 369 ? -86.179  30.128  -81.693  1.00 58.20  ? 369 MET A SD  1 
ATOM   2965  C CE  . MET A  1 369 ? -87.553  29.800  -80.582  1.00 54.28  ? 369 MET A CE  1 
ATOM   2966  N N   . ALA A  1 370 ? -86.200  28.834  -76.888  1.00 35.64  ? 370 ALA A N   1 
ATOM   2967  C CA  . ALA A  1 370 ? -87.049  27.683  -76.645  1.00 37.27  ? 370 ALA A CA  1 
ATOM   2968  C C   . ALA A  1 370 ? -88.456  27.958  -77.164  1.00 37.20  ? 370 ALA A C   1 
ATOM   2969  O O   . ALA A  1 370 ? -88.892  29.086  -77.145  1.00 39.39  ? 370 ALA A O   1 
ATOM   2970  C CB  . ALA A  1 370 ? -87.082  27.364  -75.157  1.00 38.32  ? 370 ALA A CB  1 
ATOM   2971  N N   . ASP A  1 371 ? -89.167  26.901  -77.571  1.00 37.63  ? 371 ASP A N   1 
ATOM   2972  C CA  . ASP A  1 371 ? -90.561  26.961  -77.984  1.00 37.72  ? 371 ASP A CA  1 
ATOM   2973  C C   . ASP A  1 371 ? -91.065  25.518  -77.955  1.00 37.94  ? 371 ASP A C   1 
ATOM   2974  O O   . ASP A  1 371 ? -90.382  24.660  -77.409  1.00 36.89  ? 371 ASP A O   1 
ATOM   2975  C CB  . ASP A  1 371 ? -90.645  27.656  -79.337  1.00 36.99  ? 371 ASP A CB  1 
ATOM   2976  C CG  . ASP A  1 371 ? -91.987  28.262  -79.725  1.00 35.81  ? 371 ASP A CG  1 
ATOM   2977  O OD1 . ASP A  1 371 ? -92.951  28.058  -79.002  1.00 35.13  ? 371 ASP A OD1 1 
ATOM   2978  O OD2 . ASP A  1 371 ? -92.041  28.939  -80.763  1.00 35.81  ? 371 ASP A OD2 1 
ATOM   2979  N N   . GLU A  1 372 ? -92.222  25.218  -78.559  1.00 41.75  ? 372 GLU A N   1 
ATOM   2980  C CA  . GLU A  1 372 ? -92.616  23.817  -78.703  1.00 45.16  ? 372 GLU A CA  1 
ATOM   2981  C C   . GLU A  1 372 ? -93.139  23.530  -80.119  1.00 42.34  ? 372 GLU A C   1 
ATOM   2982  O O   . GLU A  1 372 ? -93.680  24.403  -80.776  1.00 39.96  ? 372 GLU A O   1 
ATOM   2983  C CB  . GLU A  1 372 ? -93.493  23.333  -77.539  1.00 47.81  ? 372 GLU A CB  1 
ATOM   2984  C CG  . GLU A  1 372 ? -94.761  24.133  -77.306  1.00 51.28  ? 372 GLU A CG  1 
ATOM   2985  C CD  . GLU A  1 372 ? -95.611  23.642  -76.121  1.00 55.23  ? 372 GLU A CD  1 
ATOM   2986  O OE1 . GLU A  1 372 ? -95.093  22.820  -75.314  1.00 50.70  ? 372 GLU A OE1 1 
ATOM   2987  O OE2 . GLU A  1 372 ? -96.795  24.091  -76.019  1.00 50.37  ? 372 GLU A OE2 1 
ATOM   2988  N N   . LEU A  1 373 ? -92.855  22.311  -80.609  1.00 42.20  ? 373 LEU A N   1 
ATOM   2989  C CA  . LEU A  1 373 ? -93.415  21.798  -81.857  1.00 43.42  ? 373 LEU A CA  1 
ATOM   2990  C C   . LEU A  1 373 ? -94.688  21.040  -81.524  1.00 40.77  ? 373 LEU A C   1 
ATOM   2991  O O   . LEU A  1 373 ? -94.697  20.304  -80.557  1.00 42.86  ? 373 LEU A O   1 
ATOM   2992  C CB  . LEU A  1 373 ? -92.510  20.822  -82.612  1.00 42.81  ? 373 LEU A CB  1 
ATOM   2993  C CG  . LEU A  1 373 ? -91.193  21.351  -83.144  1.00 43.99  ? 373 LEU A CG  1 
ATOM   2994  C CD1 . LEU A  1 373 ? -90.433  20.194  -83.741  1.00 43.83  ? 373 LEU A CD1 1 
ATOM   2995  C CD2 . LEU A  1 373 ? -91.449  22.433  -84.178  1.00 49.04  ? 373 LEU A CD2 1 
ATOM   2996  N N   . THR A  1 374 ? -95.697  21.165  -82.375  1.00 40.69  ? 374 THR A N   1 
ATOM   2997  C CA  . THR A  1 374 ? -96.864  20.313  -82.337  1.00 42.74  ? 374 THR A CA  1 
ATOM   2998  C C   . THR A  1 374 ? -96.760  19.333  -83.497  1.00 44.07  ? 374 THR A C   1 
ATOM   2999  O O   . THR A  1 374 ? -96.600  19.748  -84.635  1.00 45.65  ? 374 THR A O   1 
ATOM   3000  C CB  . THR A  1 374 ? -98.113  21.170  -82.443  1.00 43.79  ? 374 THR A CB  1 
ATOM   3001  O OG1 . THR A  1 374 ? -97.998  22.030  -81.313  1.00 46.19  ? 374 THR A OG1 1 
ATOM   3002  C CG2 . THR A  1 374 ? -99.375  20.333  -82.411  1.00 43.88  ? 374 THR A CG2 1 
ATOM   3003  N N   . ILE A  1 375 ? -96.803  18.040  -83.179  1.00 45.56  ? 375 ILE A N   1 
ATOM   3004  C CA  . ILE A  1 375 ? -96.791  16.975  -84.173  1.00 45.28  ? 375 ILE A CA  1 
ATOM   3005  C C   . ILE A  1 375 ? -98.076  16.178  -84.019  1.00 45.48  ? 375 ILE A C   1 
ATOM   3006  O O   . ILE A  1 375 ? -98.694  16.200  -82.960  1.00 43.89  ? 375 ILE A O   1 
ATOM   3007  C CB  . ILE A  1 375 ? -95.571  16.053  -84.021  1.00 42.66  ? 375 ILE A CB  1 
ATOM   3008  C CG1 . ILE A  1 375 ? -95.494  15.451  -82.616  1.00 43.19  ? 375 ILE A CG1 1 
ATOM   3009  C CG2 . ILE A  1 375 ? -94.280  16.767  -84.415  1.00 41.36  ? 375 ILE A CG2 1 
ATOM   3010  C CD1 . ILE A  1 375 ? -94.394  14.416  -82.455  1.00 42.56  ? 375 ILE A CD1 1 
ATOM   3011  N N   . ASP A  1 376 ? -98.445  15.439  -85.062  1.00 47.80  ? 376 ASP A N   1 
ATOM   3012  C CA  . ASP A  1 376 ? -99.660  14.653  -84.961  1.00 53.15  ? 376 ASP A CA  1 
ATOM   3013  C C   . ASP A  1 376 ? -99.415  13.210  -85.439  1.00 54.00  ? 376 ASP A C   1 
ATOM   3014  O O   . ASP A  1 376 ? -99.969  12.790  -86.458  1.00 54.99  ? 376 ASP A O   1 
ATOM   3015  C CB  . ASP A  1 376 ? -100.784 15.417  -85.627  1.00 54.66  ? 376 ASP A CB  1 
ATOM   3016  C CG  . ASP A  1 376 ? -102.144 14.751  -85.507  1.00 59.70  ? 376 ASP A CG  1 
ATOM   3017  O OD1 . ASP A  1 376 ? -102.595 14.503  -84.354  1.00 62.57  ? 376 ASP A OD1 1 
ATOM   3018  O OD2 . ASP A  1 376 ? -102.735 14.494  -86.568  1.00 61.58  ? 376 ASP A OD2 1 
ATOM   3019  N N   . PRO A  1 377 ? -98.631  12.380  -84.698  1.00 47.84  ? 377 PRO A N   1 
ATOM   3020  C CA  . PRO A  1 377 ? -98.346  11.000  -85.117  1.00 45.36  ? 377 PRO A CA  1 
ATOM   3021  C C   . PRO A  1 377 ? -99.556  10.036  -85.089  1.00 45.20  ? 377 PRO A C   1 
ATOM   3022  O O   . PRO A  1 377 ? -100.400 10.091  -84.192  1.00 43.41  ? 377 PRO A O   1 
ATOM   3023  C CB  . PRO A  1 377 ? -97.283  10.644  -84.083  1.00 41.33  ? 377 PRO A CB  1 
ATOM   3024  C CG  . PRO A  1 377 ? -97.784  11.295  -82.823  1.00 42.33  ? 377 PRO A CG  1 
ATOM   3025  C CD  . PRO A  1 377 ? -98.085  12.675  -83.361  1.00 44.74  ? 377 PRO A CD  1 
ATOM   3026  N N   . VAL A  1 378 ? -99.640  9.178   -86.118  1.00 45.34  ? 378 VAL A N   1 
ATOM   3027  C CA  . VAL A  1 378 ? -100.600 8.080   -86.193  1.00 47.47  ? 378 VAL A CA  1 
ATOM   3028  C C   . VAL A  1 378 ? -99.921  6.788   -85.733  1.00 44.44  ? 378 VAL A C   1 
ATOM   3029  O O   . VAL A  1 378 ? -98.916  6.366   -86.314  1.00 45.10  ? 378 VAL A O   1 
ATOM   3030  C CB  . VAL A  1 378 ? -101.094 7.980   -87.643  1.00 50.91  ? 378 VAL A CB  1 
ATOM   3031  C CG1 . VAL A  1 378 ? -102.192 6.930   -87.805  1.00 55.31  ? 378 VAL A CG1 1 
ATOM   3032  C CG2 . VAL A  1 378 ? -101.586 9.332   -88.153  1.00 51.96  ? 378 VAL A CG2 1 
ATOM   3033  N N   . GLY A  1 379 ? -100.444 6.220   -84.641  1.00 42.94  ? 379 GLY A N   1 
ATOM   3034  C CA  . GLY A  1 379 ? -99.877  5.064   -83.976  1.00 41.47  ? 379 GLY A CA  1 
ATOM   3035  C C   . GLY A  1 379 ? -98.447  5.356   -83.556  1.00 41.78  ? 379 GLY A C   1 
ATOM   3036  O O   . GLY A  1 379 ? -98.181  6.372   -82.919  1.00 42.54  ? 379 GLY A O   1 
ATOM   3037  N N   . ILE A  1 380 ? -97.525  4.451   -83.909  1.00 42.74  ? 380 ILE A N   1 
ATOM   3038  C CA  . ILE A  1 380 ? -96.094  4.714   -83.760  1.00 39.47  ? 380 ILE A CA  1 
ATOM   3039  C C   . ILE A  1 380 ? -95.584  5.141   -85.124  1.00 36.76  ? 380 ILE A C   1 
ATOM   3040  O O   . ILE A  1 380 ? -95.747  4.378   -86.080  1.00 35.16  ? 380 ILE A O   1 
ATOM   3041  C CB  . ILE A  1 380 ? -95.330  3.484   -83.258  1.00 40.46  ? 380 ILE A CB  1 
ATOM   3042  C CG1 . ILE A  1 380 ? -95.960  2.945   -81.987  1.00 42.98  ? 380 ILE A CG1 1 
ATOM   3043  C CG2 . ILE A  1 380 ? -93.834  3.794   -83.092  1.00 39.46  ? 380 ILE A CG2 1 
ATOM   3044  C CD1 . ILE A  1 380 ? -95.533  1.525   -81.628  1.00 45.05  ? 380 ILE A CD1 1 
ATOM   3045  N N   . GLU A  1 381 ? -95.042  6.381   -85.184  1.00 35.32  ? 381 GLU A N   1 
ATOM   3046  C CA  . GLU A  1 381 ? -94.718  7.051   -86.442  1.00 34.41  ? 381 GLU A CA  1 
ATOM   3047  C C   . GLU A  1 381 ? -93.287  7.529   -86.389  1.00 32.31  ? 381 GLU A C   1 
ATOM   3048  O O   . GLU A  1 381 ? -92.942  8.336   -85.528  1.00 33.51  ? 381 GLU A O   1 
ATOM   3049  C CB  . GLU A  1 381 ? -95.620  8.235   -86.790  1.00 34.72  ? 381 GLU A CB  1 
ATOM   3050  C CG  . GLU A  1 381 ? -95.725  8.538   -88.282  1.00 35.27  ? 381 GLU A CG  1 
ATOM   3051  C CD  . GLU A  1 381 ? -96.708  9.670   -88.612  1.00 37.64  ? 381 GLU A CD  1 
ATOM   3052  O OE1 . GLU A  1 381 ? -97.774  9.781   -87.956  1.00 38.49  ? 381 GLU A OE1 1 
ATOM   3053  O OE2 . GLU A  1 381 ? -96.436  10.435  -89.555  1.00 37.42  ? 381 GLU A OE2 1 
ATOM   3054  N N   . ASP A  1 382 ? -92.469  6.992   -87.293  1.00 31.72  ? 382 ASP A N   1 
ATOM   3055  C CA  . ASP A  1 382 ? -91.152  7.555   -87.558  1.00 30.52  ? 382 ASP A CA  1 
ATOM   3056  C C   . ASP A  1 382 ? -91.313  8.835   -88.385  1.00 30.74  ? 382 ASP A C   1 
ATOM   3057  O O   . ASP A  1 382 ? -92.126  8.905   -89.307  1.00 31.08  ? 382 ASP A O   1 
ATOM   3058  C CB  . ASP A  1 382 ? -90.278  6.577   -88.302  1.00 28.88  ? 382 ASP A CB  1 
ATOM   3059  C CG  . ASP A  1 382 ? -90.878  6.009   -89.571  1.00 28.53  ? 382 ASP A CG  1 
ATOM   3060  O OD1 . ASP A  1 382 ? -91.919  5.351   -89.496  1.00 31.31  ? 382 ASP A OD1 1 
ATOM   3061  O OD2 . ASP A  1 382 ? -90.278  6.200   -90.626  1.00 27.74  ? 382 ASP A OD2 1 
ATOM   3062  N N   . MET A  1 383 ? -90.560  9.865   -88.027  1.00 30.82  ? 383 MET A N   1 
ATOM   3063  C CA  . MET A  1 383 ? -90.773  11.176  -88.631  1.00 31.84  ? 383 MET A CA  1 
ATOM   3064  C C   . MET A  1 383 ? -89.424  11.832  -88.877  1.00 29.53  ? 383 MET A C   1 
ATOM   3065  O O   . MET A  1 383 ? -88.704  12.056  -87.920  1.00 28.80  ? 383 MET A O   1 
ATOM   3066  C CB  . MET A  1 383 ? -91.589  12.086  -87.694  1.00 32.96  ? 383 MET A CB  1 
ATOM   3067  C CG  . MET A  1 383 ? -93.001  11.645  -87.413  1.00 34.56  ? 383 MET A CG  1 
ATOM   3068  S SD  . MET A  1 383 ? -93.894  12.778  -86.310  1.00 37.07  ? 383 MET A SD  1 
ATOM   3069  C CE  . MET A  1 383 ? -94.341  14.142  -87.383  1.00 39.21  ? 383 MET A CE  1 
ATOM   3070  N N   . GLU A  1 384 ? -89.100  12.149  -90.141  1.00 30.07  ? 384 GLU A N   1 
ATOM   3071  C CA  . GLU A  1 384 ? -87.948  13.001  -90.441  1.00 29.73  ? 384 GLU A CA  1 
ATOM   3072  C C   . GLU A  1 384 ? -88.359  14.485  -90.396  1.00 29.78  ? 384 GLU A C   1 
ATOM   3073  O O   . GLU A  1 384 ? -89.015  14.984  -91.317  1.00 29.92  ? 384 GLU A O   1 
ATOM   3074  C CB  . GLU A  1 384 ? -87.321  12.640  -91.793  1.00 30.23  ? 384 GLU A CB  1 
ATOM   3075  C CG  . GLU A  1 384 ? -85.951  13.279  -92.068  1.00 29.88  ? 384 GLU A CG  1 
ATOM   3076  C CD  . GLU A  1 384 ? -85.290  12.993  -93.420  1.00 30.45  ? 384 GLU A CD  1 
ATOM   3077  O OE1 . GLU A  1 384 ? -85.921  12.411  -94.330  1.00 29.20  ? 384 GLU A OE1 1 
ATOM   3078  O OE2 . GLU A  1 384 ? -84.081  13.346  -93.566  1.00 32.44  ? 384 GLU A OE2 1 
ATOM   3079  N N   . LEU A  1 385 ? -87.963  15.179  -89.315  1.00 30.25  ? 385 LEU A N   1 
ATOM   3080  C CA  . LEU A  1 385 ? -88.259  16.608  -89.126  1.00 31.67  ? 385 LEU A CA  1 
ATOM   3081  C C   . LEU A  1 385 ? -87.216  17.442  -89.870  1.00 30.43  ? 385 LEU A C   1 
ATOM   3082  O O   . LEU A  1 385 ? -86.040  17.484  -89.518  1.00 27.91  ? 385 LEU A O   1 
ATOM   3083  C CB  . LEU A  1 385 ? -88.357  17.039  -87.657  1.00 32.20  ? 385 LEU A CB  1 
ATOM   3084  C CG  . LEU A  1 385 ? -89.372  16.276  -86.796  1.00 34.65  ? 385 LEU A CG  1 
ATOM   3085  C CD1 . LEU A  1 385 ? -89.404  16.737  -85.344  1.00 34.91  ? 385 LEU A CD1 1 
ATOM   3086  C CD2 . LEU A  1 385 ? -90.794  16.378  -87.377  1.00 36.33  ? 385 LEU A CD2 1 
ATOM   3087  N N   . ALA A  1 386 ? -87.687  18.129  -90.916  1.00 32.30  ? 386 ALA A N   1 
ATOM   3088  C CA  . ALA A  1 386 ? -86.849  18.914  -91.805  1.00 31.61  ? 386 ALA A CA  1 
ATOM   3089  C C   . ALA A  1 386 ? -86.800  20.386  -91.358  1.00 29.97  ? 386 ALA A C   1 
ATOM   3090  O O   . ALA A  1 386 ? -87.751  21.115  -91.587  1.00 28.07  ? 386 ALA A O   1 
ATOM   3091  C CB  . ALA A  1 386 ? -87.425  18.750  -93.188  1.00 33.05  ? 386 ALA A CB  1 
ATOM   3092  N N   . PHE A  1 387 ? -85.664  20.792  -90.761  1.00 30.33  ? 387 PHE A N   1 
ATOM   3093  C CA  . PHE A  1 387 ? -85.401  22.157  -90.311  1.00 30.71  ? 387 PHE A CA  1 
ATOM   3094  C C   . PHE A  1 387 ? -84.747  22.944  -91.439  1.00 31.72  ? 387 PHE A C   1 
ATOM   3095  O O   . PHE A  1 387 ? -83.917  22.422  -92.175  1.00 33.83  ? 387 PHE A O   1 
ATOM   3096  C CB  . PHE A  1 387 ? -84.480  22.178  -89.088  1.00 29.34  ? 387 PHE A CB  1 
ATOM   3097  C CG  . PHE A  1 387 ? -85.140  21.718  -87.797  1.00 29.53  ? 387 PHE A CG  1 
ATOM   3098  C CD1 . PHE A  1 387 ? -85.576  20.402  -87.639  1.00 29.72  ? 387 PHE A CD1 1 
ATOM   3099  C CD2 . PHE A  1 387 ? -85.386  22.614  -86.764  1.00 30.80  ? 387 PHE A CD2 1 
ATOM   3100  C CE1 . PHE A  1 387 ? -86.229  19.991  -86.488  1.00 29.48  ? 387 PHE A CE1 1 
ATOM   3101  C CE2 . PHE A  1 387 ? -86.018  22.192  -85.605  1.00 31.46  ? 387 PHE A CE2 1 
ATOM   3102  C CZ  . PHE A  1 387 ? -86.445  20.884  -85.474  1.00 30.58  ? 387 PHE A CZ  1 
ATOM   3103  N N   . GLU A  1 388 ? -85.149  24.211  -91.553  1.00 34.27  ? 388 GLU A N   1 
ATOM   3104  C CA  . GLU A  1 388 ? -84.647  25.149  -92.549  1.00 32.95  ? 388 GLU A CA  1 
ATOM   3105  C C   . GLU A  1 388 ? -84.364  26.472  -91.842  1.00 32.76  ? 388 GLU A C   1 
ATOM   3106  O O   . GLU A  1 388 ? -85.273  27.035  -91.213  1.00 32.88  ? 388 GLU A O   1 
ATOM   3107  C CB  . GLU A  1 388 ? -85.674  25.441  -93.649  1.00 33.39  ? 388 GLU A CB  1 
ATOM   3108  C CG  . GLU A  1 388 ? -86.266  24.185  -94.287  1.00 35.13  ? 388 GLU A CG  1 
ATOM   3109  C CD  . GLU A  1 388 ? -87.359  24.459  -95.288  1.00 35.12  ? 388 GLU A CD  1 
ATOM   3110  O OE1 . GLU A  1 388 ? -88.029  25.500  -95.135  1.00 35.95  ? 388 GLU A OE1 1 
ATOM   3111  O OE2 . GLU A  1 388 ? -87.537  23.663  -96.219  1.00 35.37  ? 388 GLU A OE2 1 
ATOM   3112  N N   . PHE A  1 389 ? -83.113  26.943  -91.972  1.00 31.21  ? 389 PHE A N   1 
ATOM   3113  C CA  . PHE A  1 389 ? -82.680  28.225  -91.444  1.00 31.23  ? 389 PHE A CA  1 
ATOM   3114  C C   . PHE A  1 389 ? -82.484  29.197  -92.596  1.00 31.40  ? 389 PHE A C   1 
ATOM   3115  O O   . PHE A  1 389 ? -81.826  28.859  -93.573  1.00 30.47  ? 389 PHE A O   1 
ATOM   3116  C CB  . PHE A  1 389 ? -81.352  28.044  -90.706  1.00 30.29  ? 389 PHE A CB  1 
ATOM   3117  C CG  . PHE A  1 389 ? -81.426  27.100  -89.528  1.00 27.63  ? 389 PHE A CG  1 
ATOM   3118  C CD1 . PHE A  1 389 ? -81.423  25.740  -89.725  1.00 29.00  ? 389 PHE A CD1 1 
ATOM   3119  C CD2 . PHE A  1 389 ? -81.507  27.581  -88.238  1.00 27.88  ? 389 PHE A CD2 1 
ATOM   3120  C CE1 . PHE A  1 389 ? -81.461  24.867  -88.644  1.00 30.23  ? 389 PHE A CE1 1 
ATOM   3121  C CE2 . PHE A  1 389 ? -81.559  26.724  -87.149  1.00 28.57  ? 389 PHE A CE2 1 
ATOM   3122  C CZ  . PHE A  1 389 ? -81.532  25.356  -87.355  1.00 30.56  ? 389 PHE A CZ  1 
ATOM   3123  N N   . TYR A  1 390 ? -83.061  30.392  -92.456  1.00 32.09  ? 390 TYR A N   1 
ATOM   3124  C CA  . TYR A  1 390 ? -83.043  31.401  -93.507  1.00 33.92  ? 390 TYR A CA  1 
ATOM   3125  C C   . TYR A  1 390 ? -82.329  32.659  -93.014  1.00 32.95  ? 390 TYR A C   1 
ATOM   3126  O O   . TYR A  1 390 ? -82.332  32.966  -91.831  1.00 32.40  ? 390 TYR A O   1 
ATOM   3127  C CB  . TYR A  1 390 ? -84.474  31.804  -93.858  1.00 36.26  ? 390 TYR A CB  1 
ATOM   3128  C CG  . TYR A  1 390 ? -85.362  30.749  -94.487  1.00 38.44  ? 390 TYR A CG  1 
ATOM   3129  C CD1 . TYR A  1 390 ? -85.921  29.706  -93.731  1.00 39.78  ? 390 TYR A CD1 1 
ATOM   3130  C CD2 . TYR A  1 390 ? -85.697  30.832  -95.832  1.00 41.34  ? 390 TYR A CD2 1 
ATOM   3131  C CE1 . TYR A  1 390 ? -86.764  28.762  -94.303  1.00 38.15  ? 390 TYR A CE1 1 
ATOM   3132  C CE2 . TYR A  1 390 ? -86.557  29.907  -96.407  1.00 44.53  ? 390 TYR A CE2 1 
ATOM   3133  C CZ  . TYR A  1 390 ? -87.067  28.856  -95.652  1.00 41.22  ? 390 TYR A CZ  1 
ATOM   3134  O OH  . TYR A  1 390 ? -87.877  27.973  -96.293  1.00 39.52  ? 390 TYR A OH  1 
ATOM   3135  N N   . ASP A  1 391 ? -81.775  33.434  -93.942  1.00 35.16  ? 391 ASP A N   1 
ATOM   3136  C CA  . ASP A  1 391 ? -81.095  34.693  -93.613  1.00 35.36  ? 391 ASP A CA  1 
ATOM   3137  C C   . ASP A  1 391 ? -82.034  35.849  -93.934  1.00 34.62  ? 391 ASP A C   1 
ATOM   3138  O O   . ASP A  1 391 ? -83.180  35.623  -94.282  1.00 33.60  ? 391 ASP A O   1 
ATOM   3139  C CB  . ASP A  1 391 ? -79.769  34.818  -94.350  1.00 33.46  ? 391 ASP A CB  1 
ATOM   3140  C CG  . ASP A  1 391 ? -79.922  34.910  -95.854  1.00 33.30  ? 391 ASP A CG  1 
ATOM   3141  O OD1 . ASP A  1 391 ? -81.042  35.256  -96.308  1.00 33.93  ? 391 ASP A OD1 1 
ATOM   3142  O OD2 . ASP A  1 391 ? -78.958  34.554  -96.545  1.00 34.69  ? 391 ASP A OD2 1 
ATOM   3143  N N   . SER A  1 392 ? -81.524  37.076  -93.847  1.00 37.12  ? 392 SER A N   1 
ATOM   3144  C CA  . SER A  1 392 ? -82.355  38.275  -93.899  1.00 39.36  ? 392 SER A CA  1 
ATOM   3145  C C   . SER A  1 392 ? -82.975  38.493  -95.275  1.00 40.08  ? 392 SER A C   1 
ATOM   3146  O O   . SER A  1 392 ? -83.864  39.332  -95.390  1.00 41.01  ? 392 SER A O   1 
ATOM   3147  C CB  . SER A  1 392 ? -81.565  39.507  -93.510  1.00 40.18  ? 392 SER A CB  1 
ATOM   3148  O OG  . SER A  1 392 ? -80.441  39.675  -94.366  1.00 40.16  ? 392 SER A OG  1 
ATOM   3149  N N   . ASP A  1 393 ? -82.473  37.788  -96.304  1.00 41.21  ? 393 ASP A N   1 
ATOM   3150  C CA  . ASP A  1 393 ? -83.060  37.827  -97.636  1.00 42.68  ? 393 ASP A CA  1 
ATOM   3151  C C   . ASP A  1 393 ? -84.029  36.668  -97.891  1.00 40.84  ? 393 ASP A C   1 
ATOM   3152  O O   . ASP A  1 393 ? -84.440  36.469  -99.021  1.00 38.63  ? 393 ASP A O   1 
ATOM   3153  C CB  . ASP A  1 393 ? -81.983  37.846  -98.708  1.00 45.00  ? 393 ASP A CB  1 
ATOM   3154  C CG  . ASP A  1 393 ? -81.036  39.035  -98.639  1.00 46.55  ? 393 ASP A CG  1 
ATOM   3155  O OD1 . ASP A  1 393 ? -81.502  40.162  -98.402  1.00 48.24  ? 393 ASP A OD1 1 
ATOM   3156  O OD2 . ASP A  1 393 ? -79.844  38.822  -98.843  1.00 50.84  ? 393 ASP A OD2 1 
ATOM   3157  N N   . ASN A  1 394 ? -84.380  35.894  -96.860  1.00 41.21  ? 394 ASN A N   1 
ATOM   3158  C CA  . ASN A  1 394 ? -85.325  34.792  -96.991  1.00 43.06  ? 394 ASN A CA  1 
ATOM   3159  C C   . ASN A  1 394 ? -84.732  33.676  -97.865  1.00 41.61  ? 394 ASN A C   1 
ATOM   3160  O O   . ASN A  1 394 ? -85.454  33.016  -98.607  1.00 39.72  ? 394 ASN A O   1 
ATOM   3161  C CB  . ASN A  1 394 ? -86.680  35.334  -97.457  1.00 44.91  ? 394 ASN A CB  1 
ATOM   3162  C CG  . ASN A  1 394 ? -87.828  34.442  -97.029  1.00 47.13  ? 394 ASN A CG  1 
ATOM   3163  O OD1 . ASN A  1 394 ? -87.790  33.840  -95.956  1.00 45.05  ? 394 ASN A OD1 1 
ATOM   3164  N ND2 . ASN A  1 394 ? -88.882  34.345  -97.820  1.00 48.85  ? 394 ASN A ND2 1 
ATOM   3165  N N   . LYS A  1 395 ? -83.409  33.484  -97.784  1.00 41.45  ? 395 LYS A N   1 
ATOM   3166  C CA  . LYS A  1 395 ? -82.718  32.386  -98.449  1.00 45.85  ? 395 LYS A CA  1 
ATOM   3167  C C   . LYS A  1 395 ? -82.156  31.349  -97.460  1.00 41.94  ? 395 LYS A C   1 
ATOM   3168  O O   . LYS A  1 395 ? -81.431  31.670  -96.520  1.00 42.52  ? 395 LYS A O   1 
ATOM   3169  C CB  . LYS A  1 395 ? -81.544  32.943  -99.258  1.00 51.59  ? 395 LYS A CB  1 
ATOM   3170  C CG  . LYS A  1 395 ? -81.957  33.716  -100.494 1.00 59.40  ? 395 LYS A CG  1 
ATOM   3171  C CD  . LYS A  1 395 ? -80.741  34.237  -101.243 1.00 68.44  ? 395 LYS A CD  1 
ATOM   3172  C CE  . LYS A  1 395 ? -81.108  35.160  -102.361 1.00 76.00  ? 395 LYS A CE  1 
ATOM   3173  N NZ  . LYS A  1 395 ? -79.902  35.855  -102.819 1.00 77.72  ? 395 LYS A NZ  1 
ATOM   3174  N N   . ILE A  1 396 ? -82.413  30.075  -97.742  1.00 38.51  ? 396 ILE A N   1 
ATOM   3175  C CA  . ILE A  1 396 ? -82.029  28.996  -96.848  1.00 38.11  ? 396 ILE A CA  1 
ATOM   3176  C C   . ILE A  1 396 ? -80.502  28.931  -96.775  1.00 37.11  ? 396 ILE A C   1 
ATOM   3177  O O   . ILE A  1 396 ? -79.861  28.898  -97.805  1.00 37.64  ? 396 ILE A O   1 
ATOM   3178  C CB  . ILE A  1 396 ? -82.705  27.681  -97.302  1.00 37.93  ? 396 ILE A CB  1 
ATOM   3179  C CG1 . ILE A  1 396 ? -84.250  27.768  -97.139  1.00 43.26  ? 396 ILE A CG1 1 
ATOM   3180  C CG2 . ILE A  1 396 ? -82.175  26.477  -96.549  1.00 35.99  ? 396 ILE A CG2 1 
ATOM   3181  C CD1 . ILE A  1 396 ? -85.048  26.525  -97.545  1.00 42.86  ? 396 ILE A CD1 1 
ATOM   3182  N N   . ILE A  1 397 ? -79.931  28.945  -95.561  1.00 36.16  ? 397 ILE A N   1 
ATOM   3183  C CA  . ILE A  1 397 ? -78.488  28.872  -95.361  1.00 36.52  ? 397 ILE A CA  1 
ATOM   3184  C C   . ILE A  1 397 ? -78.115  27.575  -94.655  1.00 34.88  ? 397 ILE A C   1 
ATOM   3185  O O   . ILE A  1 397 ? -76.934  27.215  -94.670  1.00 35.49  ? 397 ILE A O   1 
ATOM   3186  C CB  . ILE A  1 397 ? -77.947  30.080  -94.575  1.00 39.49  ? 397 ILE A CB  1 
ATOM   3187  C CG1 . ILE A  1 397 ? -78.709  30.261  -93.264  1.00 41.16  ? 397 ILE A CG1 1 
ATOM   3188  C CG2 . ILE A  1 397 ? -77.994  31.346  -95.442  1.00 42.98  ? 397 ILE A CG2 1 
ATOM   3189  C CD1 . ILE A  1 397 ? -78.214  31.366  -92.363  1.00 41.14  ? 397 ILE A CD1 1 
ATOM   3190  N N   . LYS A  1 398 ? -79.091  26.873  -94.052  1.00 32.33  ? 398 LYS A N   1 
ATOM   3191  C CA  . LYS A  1 398 ? -78.825  25.534  -93.516  1.00 30.27  ? 398 LYS A CA  1 
ATOM   3192  C C   . LYS A  1 398 ? -80.083  24.649  -93.525  1.00 32.53  ? 398 LYS A C   1 
ATOM   3193  O O   . LYS A  1 398 ? -81.191  25.114  -93.220  1.00 33.17  ? 398 LYS A O   1 
ATOM   3194  C CB  . LYS A  1 398 ? -78.253  25.584  -92.098  1.00 27.96  ? 398 LYS A CB  1 
ATOM   3195  C CG  . LYS A  1 398 ? -77.880  24.241  -91.487  1.00 27.66  ? 398 LYS A CG  1 
ATOM   3196  C CD  . LYS A  1 398 ? -77.467  24.337  -90.021  1.00 27.18  ? 398 LYS A CD  1 
ATOM   3197  C CE  . LYS A  1 398 ? -77.412  22.988  -89.394  1.00 26.00  ? 398 LYS A CE  1 
ATOM   3198  N NZ  . LYS A  1 398 ? -76.909  22.944  -88.021  1.00 25.02  ? 398 LYS A NZ  1 
ATOM   3199  N N   . ASN A  1 399 ? -79.878  23.366  -93.885  1.00 32.58  ? 399 ASN A N   1 
ATOM   3200  C CA  . ASN A  1 399 ? -80.858  22.298  -93.754  1.00 31.01  ? 399 ASN A CA  1 
ATOM   3201  C C   . ASN A  1 399 ? -80.334  21.265  -92.765  1.00 30.79  ? 399 ASN A C   1 
ATOM   3202  O O   . ASN A  1 399 ? -79.152  20.921  -92.785  1.00 28.34  ? 399 ASN A O   1 
ATOM   3203  C CB  . ASN A  1 399 ? -81.116  21.543  -95.049  1.00 31.12  ? 399 ASN A CB  1 
ATOM   3204  C CG  . ASN A  1 399 ? -81.841  22.344  -96.107  1.00 33.58  ? 399 ASN A CG  1 
ATOM   3205  O OD1 . ASN A  1 399 ? -83.020  22.711  -95.971  1.00 35.07  ? 399 ASN A OD1 1 
ATOM   3206  N ND2 . ASN A  1 399 ? -81.147  22.605  -97.197  1.00 33.52  ? 399 ASN A ND2 1 
ATOM   3207  N N   . GLU A  1 400 ? -81.232  20.745  -91.920  1.00 29.49  ? 400 GLU A N   1 
ATOM   3208  C CA  . GLU A  1 400 ? -80.855  19.683  -91.020  1.00 29.26  ? 400 GLU A CA  1 
ATOM   3209  C C   . GLU A  1 400 ? -82.110  18.916  -90.655  1.00 29.65  ? 400 GLU A C   1 
ATOM   3210  O O   . GLU A  1 400 ? -83.151  19.518  -90.351  1.00 27.70  ? 400 GLU A O   1 
ATOM   3211  C CB  . GLU A  1 400 ? -80.158  20.148  -89.745  1.00 31.27  ? 400 GLU A CB  1 
ATOM   3212  C CG  . GLU A  1 400 ? -79.597  19.017  -88.879  1.00 30.75  ? 400 GLU A CG  1 
ATOM   3213  C CD  . GLU A  1 400 ? -78.622  19.490  -87.803  1.00 31.16  ? 400 GLU A CD  1 
ATOM   3214  O OE1 . GLU A  1 400 ? -78.535  20.732  -87.557  1.00 28.79  ? 400 GLU A OE1 1 
ATOM   3215  O OE2 . GLU A  1 400 ? -77.946  18.604  -87.211  1.00 30.24  ? 400 GLU A OE2 1 
ATOM   3216  N N   . SER A  1 401 ? -81.970  17.585  -90.757  1.00 27.03  ? 401 SER A N   1 
ATOM   3217  C CA  . SER A  1 401 ? -83.020  16.684  -90.372  1.00 27.36  ? 401 SER A CA  1 
ATOM   3218  C C   . SER A  1 401 ? -82.787  16.331  -88.916  1.00 26.51  ? 401 SER A C   1 
ATOM   3219  O O   . SER A  1 401 ? -81.639  16.273  -88.488  1.00 26.59  ? 401 SER A O   1 
ATOM   3220  C CB  . SER A  1 401 ? -83.055  15.463  -91.275  1.00 29.11  ? 401 SER A CB  1 
ATOM   3221  O OG  . SER A  1 401 ? -83.640  15.751  -92.537  1.00 30.12  ? 401 SER A OG  1 
ATOM   3222  N N   . ILE A  1 402 ? -83.889  16.112  -88.195  1.00 27.64  ? 402 ILE A N   1 
ATOM   3223  C CA  . ILE A  1 402 ? -83.945  15.460  -86.892  1.00 27.08  ? 402 ILE A CA  1 
ATOM   3224  C C   . ILE A  1 402 ? -84.971  14.323  -87.005  1.00 28.04  ? 402 ILE A C   1 
ATOM   3225  O O   . ILE A  1 402 ? -86.153  14.548  -87.284  1.00 27.79  ? 402 ILE A O   1 
ATOM   3226  C CB  . ILE A  1 402 ? -84.356  16.476  -85.805  1.00 26.83  ? 402 ILE A CB  1 
ATOM   3227  C CG1 . ILE A  1 402 ? -83.391  17.682  -85.703  1.00 26.78  ? 402 ILE A CG1 1 
ATOM   3228  C CG2 . ILE A  1 402 ? -84.563  15.812  -84.446  1.00 26.73  ? 402 ILE A CG2 1 
ATOM   3229  C CD1 . ILE A  1 402 ? -82.008  17.350  -85.131  1.00 26.59  ? 402 ILE A CD1 1 
ATOM   3230  N N   . ASN A  1 403 ? -84.511  13.091  -86.794  1.00 29.03  ? 403 ASN A N   1 
ATOM   3231  C CA  . ASN A  1 403 ? -85.374  11.930  -86.921  1.00 30.20  ? 403 ASN A CA  1 
ATOM   3232  C C   . ASN A  1 403 ? -85.932  11.523  -85.561  1.00 29.51  ? 403 ASN A C   1 
ATOM   3233  O O   . ASN A  1 403 ? -85.163  11.226  -84.657  1.00 29.94  ? 403 ASN A O   1 
ATOM   3234  C CB  . ASN A  1 403 ? -84.627  10.744  -87.523  1.00 30.16  ? 403 ASN A CB  1 
ATOM   3235  C CG  . ASN A  1 403 ? -84.150  11.032  -88.917  1.00 29.54  ? 403 ASN A CG  1 
ATOM   3236  O OD1 . ASN A  1 403 ? -84.893  10.858  -89.880  1.00 29.24  ? 403 ASN A OD1 1 
ATOM   3237  N ND2 . ASN A  1 403 ? -82.894  11.427  -89.030  1.00 31.02  ? 403 ASN A ND2 1 
ATOM   3238  N N   . ILE A  1 404 ? -87.256  11.432  -85.440  1.00 28.51  ? 404 ILE A N   1 
ATOM   3239  C CA  . ILE A  1 404 ? -87.850  11.053  -84.173  1.00 29.48  ? 404 ILE A CA  1 
ATOM   3240  C C   . ILE A  1 404 ? -88.755  9.847   -84.390  1.00 30.08  ? 404 ILE A C   1 
ATOM   3241  O O   . ILE A  1 404 ? -89.259  9.639   -85.500  1.00 30.96  ? 404 ILE A O   1 
ATOM   3242  C CB  . ILE A  1 404 ? -88.620  12.231  -83.530  1.00 29.60  ? 404 ILE A CB  1 
ATOM   3243  C CG1 . ILE A  1 404 ? -89.852  12.632  -84.289  1.00 30.32  ? 404 ILE A CG1 1 
ATOM   3244  C CG2 . ILE A  1 404 ? -87.731  13.446  -83.312  1.00 28.91  ? 404 ILE A CG2 1 
ATOM   3245  C CD1 . ILE A  1 404 ? -90.732  13.594  -83.501  1.00 30.46  ? 404 ILE A CD1 1 
ATOM   3246  N N   . LEU A  1 405 ? -89.016  9.120   -83.296  1.00 29.77  ? 405 LEU A N   1 
ATOM   3247  C CA  . LEU A  1 405 ? -90.047  8.094   -83.270  1.00 29.66  ? 405 LEU A CA  1 
ATOM   3248  C C   . LEU A  1 405 ? -91.144  8.549   -82.320  1.00 29.57  ? 405 LEU A C   1 
ATOM   3249  O O   . LEU A  1 405 ? -90.856  8.802   -81.171  1.00 30.81  ? 405 LEU A O   1 
ATOM   3250  C CB  . LEU A  1 405 ? -89.379  6.780   -82.863  1.00 30.23  ? 405 LEU A CB  1 
ATOM   3251  C CG  . LEU A  1 405 ? -90.249  5.521   -82.981  1.00 31.38  ? 405 LEU A CG  1 
ATOM   3252  C CD1 . LEU A  1 405 ? -90.652  5.270   -84.419  1.00 32.16  ? 405 LEU A CD1 1 
ATOM   3253  C CD2 . LEU A  1 405 ? -89.615  4.255   -82.393  1.00 30.43  ? 405 LEU A CD2 1 
ATOM   3254  N N   . ALA A  1 406 ? -92.389  8.716   -82.795  1.00 29.39  ? 406 ALA A N   1 
ATOM   3255  C CA  . ALA A  1 406 ? -93.386  9.435   -82.022  1.00 30.26  ? 406 ALA A CA  1 
ATOM   3256  C C   . ALA A  1 406 ? -94.719  8.690   -81.936  1.00 32.55  ? 406 ALA A C   1 
ATOM   3257  O O   . ALA A  1 406 ? -95.173  8.087   -82.907  1.00 33.20  ? 406 ALA A O   1 
ATOM   3258  C CB  . ALA A  1 406 ? -93.607  10.798  -82.642  1.00 30.27  ? 406 ALA A CB  1 
ATOM   3259  N N   . SER A  1 407 ? -95.415  8.881   -80.810  1.00 33.97  ? 407 SER A N   1 
ATOM   3260  C CA  . SER A  1 407 ? -96.769  8.390   -80.608  1.00 36.18  ? 407 SER A CA  1 
ATOM   3261  C C   . SER A  1 407 ? -97.452  9.302   -79.599  1.00 37.63  ? 407 SER A C   1 
ATOM   3262  O O   . SER A  1 407 ? -96.786  9.886   -78.764  1.00 37.63  ? 407 SER A O   1 
ATOM   3263  C CB  . SER A  1 407 ? -96.737  6.932   -80.105  1.00 36.58  ? 407 SER A CB  1 
ATOM   3264  O OG  . SER A  1 407 ? -98.025  6.379   -79.868  1.00 36.74  ? 407 SER A OG  1 
ATOM   3265  N N   . LYS A  1 408 ? -98.772  9.377   -79.648  1.00 41.13  ? 408 LYS A N   1 
ATOM   3266  C CA  . LYS A  1 408 ? -99.536  10.090  -78.642  1.00 44.98  ? 408 LYS A CA  1 
ATOM   3267  C C   . LYS A  1 408 ? -99.669  9.265   -77.369  1.00 47.59  ? 408 LYS A C   1 
ATOM   3268  O O   . LYS A  1 408 ? -100.180 9.778   -76.386  1.00 50.14  ? 408 LYS A O   1 
ATOM   3269  C CB  . LYS A  1 408 ? -100.962 10.348  -79.126  1.00 47.75  ? 408 LYS A CB  1 
ATOM   3270  C CG  . LYS A  1 408 ? -101.018 11.108  -80.432  1.00 49.86  ? 408 LYS A CG  1 
ATOM   3271  C CD  . LYS A  1 408 ? -102.403 11.227  -81.044  1.00 53.31  ? 408 LYS A CD  1 
ATOM   3272  C CE  . LYS A  1 408 ? -102.359 12.211  -82.169  1.00 55.80  ? 408 LYS A CE  1 
ATOM   3273  N NZ  . LYS A  1 408 ? -103.629 12.311  -82.880  1.00 58.22  ? 408 LYS A NZ  1 
ATOM   3274  N N   . THR A  1 409 ? -99.255  7.990   -77.402  1.00 48.89  ? 409 THR A N   1 
ATOM   3275  C CA  . THR A  1 409 ? -99.460  7.080   -76.287  1.00 49.40  ? 409 THR A CA  1 
ATOM   3276  C C   . THR A  1 409 ? -98.186  6.263   -76.064  1.00 50.15  ? 409 THR A C   1 
ATOM   3277  O O   . THR A  1 409 ? -97.495  5.887   -77.011  1.00 52.00  ? 409 THR A O   1 
ATOM   3278  C CB  . THR A  1 409 ? -100.703 6.224   -76.562  1.00 51.06  ? 409 THR A CB  1 
ATOM   3279  O OG1 . THR A  1 409 ? -100.673 5.725   -77.895  1.00 47.80  ? 409 THR A OG1 1 
ATOM   3280  C CG2 . THR A  1 409 ? -102.017 7.001   -76.474  1.00 52.94  ? 409 THR A CG2 1 
ATOM   3281  N N   . ALA A  1 410 ? -97.846  6.067   -74.786  1.00 49.92  ? 410 ALA A N   1 
ATOM   3282  C CA  . ALA A  1 410 ? -96.815  5.142   -74.341  1.00 48.16  ? 410 ALA A CA  1 
ATOM   3283  C C   . ALA A  1 410 ? -96.824  3.859   -75.177  1.00 48.74  ? 410 ALA A C   1 
ATOM   3284  O O   . ALA A  1 410 ? -97.907  3.338   -75.476  1.00 49.94  ? 410 ALA A O   1 
ATOM   3285  C CB  . ALA A  1 410 ? -97.072  4.803   -72.887  1.00 47.83  ? 410 ALA A CB  1 
ATOM   3286  N N   . PHE A  1 411 ? -95.627  3.328   -75.499  1.00 44.85  ? 411 PHE A N   1 
ATOM   3287  C CA  . PHE A  1 411 ? -95.535  2.118   -76.316  1.00 45.05  ? 411 PHE A CA  1 
ATOM   3288  C C   . PHE A  1 411 ? -94.263  1.335   -75.982  1.00 45.30  ? 411 PHE A C   1 
ATOM   3289  O O   . PHE A  1 411 ? -93.349  1.848   -75.359  1.00 42.31  ? 411 PHE A O   1 
ATOM   3290  C CB  . PHE A  1 411 ? -95.561  2.416   -77.822  1.00 42.48  ? 411 PHE A CB  1 
ATOM   3291  C CG  . PHE A  1 411 ? -94.447  3.340   -78.307  1.00 39.80  ? 411 PHE A CG  1 
ATOM   3292  C CD1 . PHE A  1 411 ? -93.215  2.840   -78.708  1.00 39.05  ? 411 PHE A CD1 1 
ATOM   3293  C CD2 . PHE A  1 411 ? -94.615  4.721   -78.303  1.00 38.79  ? 411 PHE A CD2 1 
ATOM   3294  C CE1 . PHE A  1 411 ? -92.198  3.705   -79.130  1.00 37.42  ? 411 PHE A CE1 1 
ATOM   3295  C CE2 . PHE A  1 411 ? -93.608  5.571   -78.717  1.00 36.72  ? 411 PHE A CE2 1 
ATOM   3296  C CZ  . PHE A  1 411 ? -92.403  5.057   -79.133  1.00 37.09  ? 411 PHE A CZ  1 
ATOM   3297  N N   . GLU A  1 412 ? -94.237  0.077   -76.427  1.00 51.25  ? 412 GLU A N   1 
ATOM   3298  C CA  . GLU A  1 412 ? -93.168  -0.859  -76.120  1.00 54.13  ? 412 GLU A CA  1 
ATOM   3299  C C   . GLU A  1 412 ? -92.051  -0.701  -77.125  1.00 45.41  ? 412 GLU A C   1 
ATOM   3300  O O   . GLU A  1 412 ? -92.309  -0.745  -78.313  1.00 44.61  ? 412 GLU A O   1 
ATOM   3301  C CB  . GLU A  1 412 ? -93.586  -2.325  -76.297  1.00 62.86  ? 412 GLU A CB  1 
ATOM   3302  C CG  . GLU A  1 412 ? -94.685  -2.776  -75.339  1.00 75.37  ? 412 GLU A CG  1 
ATOM   3303  C CD  . GLU A  1 412 ? -94.310  -2.716  -73.862  1.00 81.67  ? 412 GLU A CD  1 
ATOM   3304  O OE1 . GLU A  1 412 ? -93.782  -1.691  -73.342  1.00 74.03  ? 412 GLU A OE1 1 
ATOM   3305  O OE2 . GLU A  1 412 ? -94.609  -3.742  -73.222  1.00 81.13  ? 412 GLU A OE2 1 
ATOM   3306  N N   . LEU A  1 413 ? -90.821  -0.599  -76.628  1.00 44.58  ? 413 LEU A N   1 
ATOM   3307  C CA  . LEU A  1 413 ? -89.627  -0.779  -77.452  1.00 41.98  ? 413 LEU A CA  1 
ATOM   3308  C C   . LEU A  1 413 ? -89.073  -2.187  -77.268  1.00 38.38  ? 413 LEU A C   1 
ATOM   3309  O O   . LEU A  1 413 ? -89.245  -2.808  -76.231  1.00 37.70  ? 413 LEU A O   1 
ATOM   3310  C CB  . LEU A  1 413 ? -88.567  0.254   -77.067  1.00 41.57  ? 413 LEU A CB  1 
ATOM   3311  C CG  . LEU A  1 413 ? -88.929  1.717   -77.347  1.00 40.83  ? 413 LEU A CG  1 
ATOM   3312  C CD1 . LEU A  1 413 ? -88.035  2.641   -76.552  1.00 39.84  ? 413 LEU A CD1 1 
ATOM   3313  C CD2 . LEU A  1 413 ? -88.823  2.013   -78.840  1.00 41.17  ? 413 LEU A CD2 1 
ATOM   3314  N N   . PRO A  1 414 ? -88.319  -2.729  -78.242  1.00 38.88  ? 414 PRO A N   1 
ATOM   3315  C CA  . PRO A  1 414 ? -87.545  -3.938  -77.987  1.00 37.73  ? 414 PRO A CA  1 
ATOM   3316  C C   . PRO A  1 414 ? -86.423  -3.543  -77.040  1.00 36.19  ? 414 PRO A C   1 
ATOM   3317  O O   . PRO A  1 414 ? -85.945  -2.421  -77.099  1.00 36.98  ? 414 PRO A O   1 
ATOM   3318  C CB  . PRO A  1 414 ? -87.093  -4.338  -79.368  1.00 37.85  ? 414 PRO A CB  1 
ATOM   3319  C CG  . PRO A  1 414 ? -86.935  -3.036  -80.083  1.00 37.66  ? 414 PRO A CG  1 
ATOM   3320  C CD  . PRO A  1 414 ? -88.132  -2.216  -79.608  1.00 38.53  ? 414 PRO A CD  1 
ATOM   3321  N N   . GLU A  1 415 ? -86.007  -4.484  -76.194  1.00 37.79  ? 415 GLU A N   1 
ATOM   3322  C CA  . GLU A  1 415 ? -85.149  -4.220  -75.059  1.00 38.67  ? 415 GLU A CA  1 
ATOM   3323  C C   . GLU A  1 415 ? -84.002  -5.221  -75.035  1.00 36.61  ? 415 GLU A C   1 
ATOM   3324  O O   . GLU A  1 415 ? -84.242  -6.425  -75.172  1.00 37.24  ? 415 GLU A O   1 
ATOM   3325  C CB  . GLU A  1 415 ? -85.943  -4.375  -73.762  1.00 44.53  ? 415 GLU A CB  1 
ATOM   3326  C CG  . GLU A  1 415 ? -85.462  -3.422  -72.672  1.00 51.04  ? 415 GLU A CG  1 
ATOM   3327  C CD  . GLU A  1 415 ? -86.245  -3.409  -71.373  1.00 57.26  ? 415 GLU A CD  1 
ATOM   3328  O OE1 . GLU A  1 415 ? -87.497  -3.468  -71.537  1.00 60.42  ? 415 GLU A OE1 1 
ATOM   3329  O OE2 . GLU A  1 415 ? -85.627  -3.307  -70.256  1.00 51.44  ? 415 GLU A OE2 1 
ATOM   3330  N N   . LEU A  1 416 ? -82.780  -4.711  -74.812  1.00 32.51  ? 416 LEU A N   1 
ATOM   3331  C CA  . LEU A  1 416 ? -81.596  -5.530  -74.673  1.00 31.57  ? 416 LEU A CA  1 
ATOM   3332  C C   . LEU A  1 416 ? -81.018  -5.335  -73.275  1.00 32.13  ? 416 LEU A C   1 
ATOM   3333  O O   . LEU A  1 416 ? -80.601  -4.237  -72.944  1.00 31.75  ? 416 LEU A O   1 
ATOM   3334  C CB  . LEU A  1 416 ? -80.577  -5.208  -75.762  1.00 30.37  ? 416 LEU A CB  1 
ATOM   3335  C CG  . LEU A  1 416 ? -79.371  -6.155  -75.866  1.00 30.43  ? 416 LEU A CG  1 
ATOM   3336  C CD1 . LEU A  1 416 ? -78.772  -6.056  -77.235  1.00 30.83  ? 416 LEU A CD1 1 
ATOM   3337  C CD2 . LEU A  1 416 ? -78.272  -5.880  -74.863  1.00 30.15  ? 416 LEU A CD2 1 
ATOM   3338  N N   . THR A  1 417 ? -80.929  -6.428  -72.500  1.00 33.70  ? 417 THR A N   1 
ATOM   3339  C CA  . THR A  1 417 ? -80.215  -6.418  -71.229  1.00 35.16  ? 417 THR A CA  1 
ATOM   3340  C C   . THR A  1 417 ? -79.091  -7.465  -71.223  1.00 34.58  ? 417 THR A C   1 
ATOM   3341  O O   . THR A  1 417 ? -79.159  -8.501  -71.895  1.00 34.19  ? 417 THR A O   1 
ATOM   3342  C CB  . THR A  1 417 ? -81.202  -6.626  -70.077  1.00 36.40  ? 417 THR A CB  1 
ATOM   3343  O OG1 . THR A  1 417 ? -81.920  -7.821  -70.300  1.00 35.38  ? 417 THR A OG1 1 
ATOM   3344  C CG2 . THR A  1 417 ? -82.242  -5.519  -70.029  1.00 38.33  ? 417 THR A CG2 1 
ATOM   3345  N N   . ILE A  1 418 ? -78.046  -7.198  -70.431  1.00 32.24  ? 418 ILE A N   1 
ATOM   3346  C CA  . ILE A  1 418 ? -76.979  -8.168  -70.265  1.00 31.84  ? 418 ILE A CA  1 
ATOM   3347  C C   . ILE A  1 418 ? -76.855  -8.514  -68.793  1.00 31.85  ? 418 ILE A C   1 
ATOM   3348  O O   . ILE A  1 418 ? -77.129  -7.679  -67.940  1.00 31.18  ? 418 ILE A O   1 
ATOM   3349  C CB  . ILE A  1 418 ? -75.644  -7.652  -70.848  1.00 30.89  ? 418 ILE A CB  1 
ATOM   3350  C CG1 . ILE A  1 418 ? -75.096  -6.467  -70.069  1.00 31.01  ? 418 ILE A CG1 1 
ATOM   3351  C CG2 . ILE A  1 418 ? -75.790  -7.326  -72.332  1.00 29.77  ? 418 ILE A CG2 1 
ATOM   3352  C CD1 . ILE A  1 418 ? -73.824  -5.878  -70.657  1.00 31.08  ? 418 ILE A CD1 1 
ATOM   3353  N N   . GLU A  1 419 ? -76.412  -9.748  -68.533  1.00 33.35  ? 419 GLU A N   1 
ATOM   3354  C CA  . GLU A  1 419 ? -75.947  -10.186 -67.227  1.00 35.39  ? 419 GLU A CA  1 
ATOM   3355  C C   . GLU A  1 419 ? -74.485  -10.561 -67.400  1.00 33.81  ? 419 GLU A C   1 
ATOM   3356  O O   . GLU A  1 419 ? -74.193  -11.377 -68.263  1.00 32.66  ? 419 GLU A O   1 
ATOM   3357  C CB  . GLU A  1 419 ? -76.634  -11.444 -66.681  1.00 37.33  ? 419 GLU A CB  1 
ATOM   3358  C CG  . GLU A  1 419 ? -78.077  -11.208 -66.246  1.00 41.95  ? 419 GLU A CG  1 
ATOM   3359  C CD  . GLU A  1 419 ? -78.900  -12.493 -66.133  1.00 45.61  ? 419 GLU A CD  1 
ATOM   3360  O OE1 . GLU A  1 419 ? -78.343  -13.614 -66.139  1.00 53.09  ? 419 GLU A OE1 1 
ATOM   3361  O OE2 . GLU A  1 419 ? -80.128  -12.383 -66.060  1.00 44.45  ? 419 GLU A OE2 1 
ATOM   3362  N N   . VAL A  1 420 ? -73.615  -10.012 -66.541  1.00 33.92  ? 420 VAL A N   1 
ATOM   3363  C CA  . VAL A  1 420 ? -72.176  -10.178 -66.655  1.00 33.62  ? 420 VAL A CA  1 
ATOM   3364  C C   . VAL A  1 420 ? -71.650  -10.944 -65.439  1.00 34.76  ? 420 VAL A C   1 
ATOM   3365  O O   . VAL A  1 420 ? -72.136  -10.759 -64.325  1.00 33.41  ? 420 VAL A O   1 
ATOM   3366  C CB  . VAL A  1 420 ? -71.476  -8.822  -66.854  1.00 33.88  ? 420 VAL A CB  1 
ATOM   3367  C CG1 . VAL A  1 420 ? -69.959  -8.929  -66.874  1.00 35.21  ? 420 VAL A CG1 1 
ATOM   3368  C CG2 . VAL A  1 420 ? -71.946  -8.147  -68.127  1.00 33.27  ? 420 VAL A CG2 1 
ATOM   3369  N N   . THR A  1 421 ? -70.691  -11.858 -65.713  1.00 35.73  ? 421 THR A N   1 
ATOM   3370  C CA  . THR A  1 421 ? -69.987  -12.649 -64.705  1.00 35.75  ? 421 THR A CA  1 
ATOM   3371  C C   . THR A  1 421 ? -68.473  -12.485 -64.883  1.00 33.88  ? 421 THR A C   1 
ATOM   3372  O O   . THR A  1 421 ? -67.993  -12.411 -66.004  1.00 31.64  ? 421 THR A O   1 
ATOM   3373  C CB  . THR A  1 421 ? -70.380  -14.113 -64.878  1.00 37.34  ? 421 THR A CB  1 
ATOM   3374  O OG1 . THR A  1 421 ? -71.800  -14.134 -64.784  1.00 37.84  ? 421 THR A OG1 1 
ATOM   3375  C CG2 . THR A  1 421 ? -69.758  -15.007 -63.827  1.00 38.62  ? 421 THR A CG2 1 
ATOM   3376  N N   . PRO A  1 422 ? -67.660  -12.284 -63.825  1.00 34.04  ? 422 PRO A N   1 
ATOM   3377  C CA  . PRO A  1 422 ? -68.121  -11.785 -62.524  1.00 35.57  ? 422 PRO A CA  1 
ATOM   3378  C C   . PRO A  1 422 ? -68.944  -10.514 -62.671  1.00 35.48  ? 422 PRO A C   1 
ATOM   3379  O O   . PRO A  1 422 ? -68.590  -9.637  -63.446  1.00 36.23  ? 422 PRO A O   1 
ATOM   3380  C CB  . PRO A  1 422 ? -66.836  -11.485 -61.763  1.00 34.41  ? 422 PRO A CB  1 
ATOM   3381  C CG  . PRO A  1 422 ? -65.883  -12.458 -62.380  1.00 34.27  ? 422 PRO A CG  1 
ATOM   3382  C CD  . PRO A  1 422 ? -66.206  -12.451 -63.866  1.00 33.52  ? 422 PRO A CD  1 
ATOM   3383  N N   . GLU A  1 423 ? -70.015  -10.458 -61.891  1.00 38.91  ? 423 GLU A N   1 
ATOM   3384  C CA  . GLU A  1 423 ? -70.969  -9.374  -61.878  1.00 41.05  ? 423 GLU A CA  1 
ATOM   3385  C C   . GLU A  1 423 ? -70.375  -8.113  -61.255  1.00 39.99  ? 423 GLU A C   1 
ATOM   3386  O O   . GLU A  1 423 ? -70.679  -7.035  -61.744  1.00 41.16  ? 423 GLU A O   1 
ATOM   3387  C CB  . GLU A  1 423 ? -72.217  -9.816  -61.126  1.00 44.34  ? 423 GLU A CB  1 
ATOM   3388  C CG  . GLU A  1 423 ? -73.292  -8.735  -61.125  1.00 50.68  ? 423 GLU A CG  1 
ATOM   3389  C CD  . GLU A  1 423 ? -74.632  -9.169  -60.544  1.00 53.47  ? 423 GLU A CD  1 
ATOM   3390  O OE1 . GLU A  1 423 ? -74.734  -10.360 -60.191  1.00 50.66  ? 423 GLU A OE1 1 
ATOM   3391  O OE2 . GLU A  1 423 ? -75.535  -8.304  -60.425  1.00 53.73  ? 423 GLU A OE2 1 
ATOM   3392  N N   . LYS A  1 424 ? -69.549  -8.239  -60.207  1.00 41.33  ? 424 LYS A N   1 
ATOM   3393  C CA  . LYS A  1 424 ? -69.205  -7.093  -59.377  1.00 45.87  ? 424 LYS A CA  1 
ATOM   3394  C C   . LYS A  1 424 ? -67.713  -6.999  -59.032  1.00 43.61  ? 424 LYS A C   1 
ATOM   3395  O O   . LYS A  1 424 ? -67.234  -5.899  -58.707  1.00 43.50  ? 424 LYS A O   1 
ATOM   3396  C CB  . LYS A  1 424 ? -70.081  -7.072  -58.115  1.00 53.23  ? 424 LYS A CB  1 
ATOM   3397  C CG  . LYS A  1 424 ? -71.620  -6.796  -58.293  1.00 60.34  ? 424 LYS A CG  1 
ATOM   3398  C CD  . LYS A  1 424 ? -72.129  -5.345  -58.354  1.00 63.28  ? 424 LYS A CD  1 
ATOM   3399  C CE  . LYS A  1 424 ? -73.641  -5.179  -58.155  1.00 67.02  ? 424 LYS A CE  1 
ATOM   3400  N NZ  . LYS A  1 424 ? -74.150  -5.568  -56.823  1.00 64.16  ? 424 LYS A NZ  1 
ATOM   3401  N N   . ASP A  1 425 ? -66.980  -8.114  -59.104  1.00 39.15  ? 425 ASP A N   1 
ATOM   3402  C CA  . ASP A  1 425 ? -65.586  -8.136  -58.681  1.00 38.62  ? 425 ASP A CA  1 
ATOM   3403  C C   . ASP A  1 425 ? -64.801  -9.100  -59.569  1.00 37.00  ? 425 ASP A C   1 
ATOM   3404  O O   . ASP A  1 425 ? -64.928  -10.316 -59.453  1.00 36.11  ? 425 ASP A O   1 
ATOM   3405  C CB  . ASP A  1 425 ? -65.477  -8.432  -57.186  1.00 39.86  ? 425 ASP A CB  1 
ATOM   3406  C CG  . ASP A  1 425 ? -64.100  -8.377  -56.520  1.00 39.48  ? 425 ASP A CG  1 
ATOM   3407  O OD1 . ASP A  1 425 ? -63.080  -8.236  -57.221  1.00 37.88  ? 425 ASP A OD1 1 
ATOM   3408  O OD2 . ASP A  1 425 ? -64.051  -8.522  -55.287  1.00 40.97  ? 425 ASP A OD2 1 
ATOM   3409  N N   . LEU A  1 426 ? -63.950  -8.529  -60.419  1.00 35.80  ? 426 LEU A N   1 
ATOM   3410  C CA  . LEU A  1 426 ? -63.134  -9.289  -61.350  1.00 36.95  ? 426 LEU A CA  1 
ATOM   3411  C C   . LEU A  1 426 ? -62.222  -10.288 -60.633  1.00 37.73  ? 426 LEU A C   1 
ATOM   3412  O O   . LEU A  1 426 ? -61.762  -11.222 -61.281  1.00 39.37  ? 426 LEU A O   1 
ATOM   3413  C CB  . LEU A  1 426 ? -62.303  -8.375  -62.249  1.00 36.71  ? 426 LEU A CB  1 
ATOM   3414  C CG  . LEU A  1 426 ? -63.106  -7.383  -63.098  1.00 38.72  ? 426 LEU A CG  1 
ATOM   3415  C CD1 . LEU A  1 426 ? -62.159  -6.561  -63.940  1.00 39.27  ? 426 LEU A CD1 1 
ATOM   3416  C CD2 . LEU A  1 426 ? -64.158  -8.017  -63.990  1.00 38.92  ? 426 LEU A CD2 1 
ATOM   3417  N N   . ASN A  1 427 ? -61.932  -10.103 -59.337  1.00 37.75  ? 427 ASN A N   1 
ATOM   3418  C CA  . ASN A  1 427 ? -61.049  -11.028 -58.642  1.00 40.35  ? 427 ASN A CA  1 
ATOM   3419  C C   . ASN A  1 427 ? -61.691  -12.405 -58.461  1.00 40.31  ? 427 ASN A C   1 
ATOM   3420  O O   . ASN A  1 427 ? -61.002  -13.339 -58.063  1.00 37.99  ? 427 ASN A O   1 
ATOM   3421  C CB  . ASN A  1 427 ? -60.636  -10.569 -57.243  1.00 42.45  ? 427 ASN A CB  1 
ATOM   3422  C CG  . ASN A  1 427 ? -59.439  -9.642  -57.218  1.00 41.92  ? 427 ASN A CG  1 
ATOM   3423  O OD1 . ASN A  1 427 ? -58.515  -9.759  -58.025  1.00 40.98  ? 427 ASN A OD1 1 
ATOM   3424  N ND2 . ASN A  1 427 ? -59.455  -8.690  -56.304  1.00 41.78  ? 427 ASN A ND2 1 
ATOM   3425  N N   . GLU A  1 428 ? -63.005  -12.500 -58.698  1.00 42.05  ? 428 GLU A N   1 
ATOM   3426  C CA  . GLU A  1 428 ? -63.752  -13.703 -58.373  1.00 47.26  ? 428 GLU A CA  1 
ATOM   3427  C C   . GLU A  1 428 ? -63.574  -14.771 -59.453  1.00 43.83  ? 428 GLU A C   1 
ATOM   3428  O O   . GLU A  1 428 ? -64.084  -15.855 -59.280  1.00 42.06  ? 428 GLU A O   1 
ATOM   3429  C CB  . GLU A  1 428 ? -65.239  -13.395 -58.177  1.00 52.86  ? 428 GLU A CB  1 
ATOM   3430  C CG  . GLU A  1 428 ? -65.570  -12.671 -56.868  1.00 59.04  ? 428 GLU A CG  1 
ATOM   3431  C CD  . GLU A  1 428 ? -67.049  -12.273 -56.735  1.00 65.39  ? 428 GLU A CD  1 
ATOM   3432  O OE1 . GLU A  1 428 ? -67.803  -12.736 -57.639  1.00 66.43  ? 428 GLU A OE1 1 
ATOM   3433  O OE2 . GLU A  1 428 ? -67.475  -11.516 -55.802  1.00 63.50  ? 428 GLU A OE2 1 
ATOM   3434  N N   . GLY A  1 429 ? -62.855  -14.478 -60.556  1.00 42.40  ? 429 GLY A N   1 
ATOM   3435  C CA  . GLY A  1 429 ? -62.502  -15.505 -61.528  1.00 41.22  ? 429 GLY A CA  1 
ATOM   3436  C C   . GLY A  1 429 ? -61.618  -15.004 -62.664  1.00 39.53  ? 429 GLY A C   1 
ATOM   3437  O O   . GLY A  1 429 ? -61.480  -13.801 -62.865  1.00 42.33  ? 429 GLY A O   1 
ATOM   3438  N N   . LYS A  1 430 ? -61.074  -15.928 -63.456  1.00 38.11  ? 430 LYS A N   1 
ATOM   3439  C CA  . LYS A  1 430 ? -60.121  -15.568 -64.496  1.00 39.64  ? 430 LYS A CA  1 
ATOM   3440  C C   . LYS A  1 430 ? -60.844  -15.424 -65.831  1.00 36.49  ? 430 LYS A C   1 
ATOM   3441  O O   . LYS A  1 430 ? -60.318  -14.856 -66.786  1.00 34.27  ? 430 LYS A O   1 
ATOM   3442  C CB  . LYS A  1 430 ? -58.955  -16.565 -64.588  1.00 45.55  ? 430 LYS A CB  1 
ATOM   3443  C CG  . LYS A  1 430 ? -58.185  -16.702 -63.290  1.00 51.73  ? 430 LYS A CG  1 
ATOM   3444  C CD  . LYS A  1 430 ? -56.675  -16.891 -63.390  1.00 62.19  ? 430 LYS A CD  1 
ATOM   3445  C CE  . LYS A  1 430 ? -56.008  -15.749 -62.625  1.00 69.13  ? 430 LYS A CE  1 
ATOM   3446  N NZ  . LYS A  1 430 ? -54.562  -15.920 -62.468  1.00 76.07  ? 430 LYS A NZ  1 
ATOM   3447  N N   . ILE A  1 431 ? -62.096  -15.883 -65.863  1.00 34.82  ? 431 ILE A N   1 
ATOM   3448  C CA  . ILE A  1 431 ? -62.862  -15.912 -67.086  1.00 32.53  ? 431 ILE A CA  1 
ATOM   3449  C C   . ILE A  1 431 ? -64.163  -15.157 -66.897  1.00 31.73  ? 431 ILE A C   1 
ATOM   3450  O O   . ILE A  1 431 ? -64.828  -15.322 -65.870  1.00 31.36  ? 431 ILE A O   1 
ATOM   3451  C CB  . ILE A  1 431 ? -63.153  -17.357 -67.491  1.00 33.14  ? 431 ILE A CB  1 
ATOM   3452  C CG1 . ILE A  1 431 ? -61.883  -18.110 -67.817  1.00 33.38  ? 431 ILE A CG1 1 
ATOM   3453  C CG2 . ILE A  1 431 ? -64.131  -17.346 -68.659  1.00 33.15  ? 431 ILE A CG2 1 
ATOM   3454  C CD1 . ILE A  1 431 ? -62.098  -19.613 -67.907  1.00 34.43  ? 431 ILE A CD1 1 
ATOM   3455  N N   . ALA A  1 432 ? -64.537  -14.390 -67.931  1.00 30.58  ? 432 ALA A N   1 
ATOM   3456  C CA  . ALA A  1 432 ? -65.791  -13.663 -67.875  1.00 31.29  ? 432 ALA A CA  1 
ATOM   3457  C C   . ALA A  1 432 ? -66.839  -14.231 -68.835  1.00 30.65  ? 432 ALA A C   1 
ATOM   3458  O O   . ALA A  1 432 ? -66.522  -14.982 -69.768  1.00 30.54  ? 432 ALA A O   1 
ATOM   3459  C CB  . ALA A  1 432 ? -65.538  -12.178 -68.102  1.00 30.95  ? 432 ALA A CB  1 
ATOM   3460  N N   . SER A  1 433 ? -68.108  -13.904 -68.552  1.00 30.37  ? 433 SER A N   1 
ATOM   3461  C CA  . SER A  1 433 ? -69.163  -14.090 -69.542  1.00 31.17  ? 433 SER A CA  1 
ATOM   3462  C C   . SER A  1 433 ? -70.094  -12.878 -69.636  1.00 31.09  ? 433 SER A C   1 
ATOM   3463  O O   . SER A  1 433 ? -70.366  -12.216 -68.628  1.00 29.99  ? 433 SER A O   1 
ATOM   3464  C CB  . SER A  1 433 ? -69.954  -15.341 -69.291  1.00 30.49  ? 433 SER A CB  1 
ATOM   3465  O OG  . SER A  1 433 ? -70.863  -15.211 -68.211  1.00 30.39  ? 433 SER A OG  1 
ATOM   3466  N N   . ILE A  1 434 ? -70.649  -12.687 -70.848  1.00 31.93  ? 434 ILE A N   1 
ATOM   3467  C CA  . ILE A  1 434 ? -71.748  -11.762 -71.085  1.00 31.76  ? 434 ILE A CA  1 
ATOM   3468  C C   . ILE A  1 434 ? -72.917  -12.549 -71.676  1.00 33.13  ? 434 ILE A C   1 
ATOM   3469  O O   . ILE A  1 434 ? -72.862  -12.962 -72.825  1.00 33.64  ? 434 ILE A O   1 
ATOM   3470  C CB  . ILE A  1 434 ? -71.345  -10.602 -72.004  1.00 29.94  ? 434 ILE A CB  1 
ATOM   3471  C CG1 . ILE A  1 434 ? -70.290  -9.727  -71.390  1.00 31.02  ? 434 ILE A CG1 1 
ATOM   3472  C CG2 . ILE A  1 434 ? -72.586  -9.814  -72.376  1.00 30.24  ? 434 ILE A CG2 1 
ATOM   3473  C CD1 . ILE A  1 434 ? -69.872  -8.515  -72.227  1.00 30.98  ? 434 ILE A CD1 1 
ATOM   3474  N N   . LYS A  1 435 ? -74.000  -12.677 -70.903  1.00 34.83  ? 435 LYS A N   1 
ATOM   3475  C CA  . LYS A  1 435 ? -75.258  -13.239 -71.375  1.00 36.19  ? 435 LYS A CA  1 
ATOM   3476  C C   . LYS A  1 435 ? -76.177  -12.107 -71.849  1.00 36.62  ? 435 LYS A C   1 
ATOM   3477  O O   . LYS A  1 435 ? -76.547  -11.240 -71.053  1.00 36.42  ? 435 LYS A O   1 
ATOM   3478  C CB  . LYS A  1 435 ? -75.893  -14.015 -70.216  1.00 38.22  ? 435 LYS A CB  1 
ATOM   3479  C CG  . LYS A  1 435 ? -75.293  -15.390 -69.955  1.00 43.24  ? 435 LYS A CG  1 
ATOM   3480  C CD  . LYS A  1 435 ? -75.921  -16.230 -68.842  1.00 46.38  ? 435 LYS A CD  1 
ATOM   3481  C CE  . LYS A  1 435 ? -75.751  -15.544 -67.532  1.00 49.81  ? 435 LYS A CE  1 
ATOM   3482  N NZ  . LYS A  1 435 ? -75.667  -16.531 -66.463  1.00 54.90  ? 435 LYS A NZ  1 
ATOM   3483  N N   . THR A  1 436 ? -76.512  -12.090 -73.149  1.00 35.21  ? 436 THR A N   1 
ATOM   3484  C CA  . THR A  1 436 ? -77.371  -11.050 -73.709  1.00 33.52  ? 436 THR A CA  1 
ATOM   3485  C C   . THR A  1 436 ? -78.790  -11.611 -73.846  1.00 35.49  ? 436 THR A C   1 
ATOM   3486  O O   . THR A  1 436 ? -78.964  -12.779 -74.191  1.00 32.91  ? 436 THR A O   1 
ATOM   3487  C CB  . THR A  1 436 ? -76.858  -10.623 -75.080  1.00 31.33  ? 436 THR A CB  1 
ATOM   3488  O OG1 . THR A  1 436 ? -75.559  -10.064 -74.989  1.00 29.91  ? 436 THR A OG1 1 
ATOM   3489  C CG2 . THR A  1 436 ? -77.768  -9.611  -75.745  1.00 31.25  ? 436 THR A CG2 1 
ATOM   3490  N N   . LYS A  1 437 ? -79.780  -10.733 -73.638  1.00 36.01  ? 437 LYS A N   1 
ATOM   3491  C CA  . LYS A  1 437 ? -81.187  -11.069 -73.778  1.00 38.81  ? 437 LYS A CA  1 
ATOM   3492  C C   . LYS A  1 437 ? -81.884  -9.923  -74.506  1.00 36.52  ? 437 LYS A C   1 
ATOM   3493  O O   . LYS A  1 437 ? -81.823  -8.779  -74.072  1.00 35.02  ? 437 LYS A O   1 
ATOM   3494  C CB  . LYS A  1 437 ? -81.780  -11.331 -72.393  1.00 43.53  ? 437 LYS A CB  1 
ATOM   3495  C CG  . LYS A  1 437 ? -83.278  -11.567 -72.348  1.00 48.98  ? 437 LYS A CG  1 
ATOM   3496  C CD  . LYS A  1 437 ? -83.810  -11.587 -70.922  1.00 52.82  ? 437 LYS A CD  1 
ATOM   3497  C CE  . LYS A  1 437 ? -85.287  -11.356 -70.884  1.00 56.71  ? 437 LYS A CE  1 
ATOM   3498  N NZ  . LYS A  1 437 ? -85.809  -11.327 -69.514  1.00 56.87  ? 437 LYS A NZ  1 
ATOM   3499  N N   . ILE A  1 438 ? -82.471  -10.248 -75.658  1.00 35.56  ? 438 ILE A N   1 
ATOM   3500  C CA  . ILE A  1 438 ? -83.215  -9.307  -76.460  1.00 34.96  ? 438 ILE A CA  1 
ATOM   3501  C C   . ILE A  1 438 ? -84.690  -9.696  -76.407  1.00 38.03  ? 438 ILE A C   1 
ATOM   3502  O O   . ILE A  1 438 ? -85.077  -10.786 -76.852  1.00 39.47  ? 438 ILE A O   1 
ATOM   3503  C CB  . ILE A  1 438 ? -82.721  -9.264  -77.912  1.00 34.08  ? 438 ILE A CB  1 
ATOM   3504  C CG1 . ILE A  1 438 ? -81.234  -9.022  -78.017  1.00 32.05  ? 438 ILE A CG1 1 
ATOM   3505  C CG2 . ILE A  1 438 ? -83.508  -8.203  -78.695  1.00 34.60  ? 438 ILE A CG2 1 
ATOM   3506  C CD1 . ILE A  1 438 ? -80.686  -9.162  -79.417  1.00 30.84  ? 438 ILE A CD1 1 
ATOM   3507  N N   . GLU A  1 439 ? -85.483  -8.791  -75.823  1.00 39.45  ? 439 GLU A N   1 
ATOM   3508  C CA  . GLU A  1 439 ? -86.927  -8.836  -75.879  1.00 42.03  ? 439 GLU A CA  1 
ATOM   3509  C C   . GLU A  1 439 ? -87.340  -8.110  -77.146  1.00 38.77  ? 439 GLU A C   1 
ATOM   3510  O O   . GLU A  1 439 ? -87.232  -6.894  -77.237  1.00 36.94  ? 439 GLU A O   1 
ATOM   3511  C CB  . GLU A  1 439 ? -87.605  -8.173  -74.681  1.00 48.72  ? 439 GLU A CB  1 
ATOM   3512  C CG  . GLU A  1 439 ? -87.664  -9.040  -73.427  1.00 57.94  ? 439 GLU A CG  1 
ATOM   3513  C CD  . GLU A  1 439 ? -88.715  -8.539  -72.444  1.00 70.01  ? 439 GLU A CD  1 
ATOM   3514  O OE1 . GLU A  1 439 ? -89.857  -8.150  -72.864  1.00 68.43  ? 439 GLU A OE1 1 
ATOM   3515  O OE2 . GLU A  1 439 ? -88.360  -8.562  -71.238  1.00 72.59  ? 439 GLU A OE2 1 
ATOM   3516  N N   . THR A  1 440 ? -87.818  -8.881  -78.119  1.00 38.11  ? 440 THR A N   1 
ATOM   3517  C CA  . THR A  1 440 ? -88.212  -8.329  -79.393  1.00 36.43  ? 440 THR A CA  1 
ATOM   3518  C C   . THR A  1 440 ? -89.603  -7.712  -79.269  1.00 37.36  ? 440 THR A C   1 
ATOM   3519  O O   . THR A  1 440 ? -90.354  -7.902  -78.305  1.00 38.03  ? 440 THR A O   1 
ATOM   3520  C CB  . THR A  1 440 ? -88.185  -9.400  -80.492  1.00 35.75  ? 440 THR A CB  1 
ATOM   3521  O OG1 . THR A  1 440 ? -89.131  -10.426 -80.209  1.00 35.49  ? 440 THR A OG1 1 
ATOM   3522  C CG2 . THR A  1 440 ? -86.798  -9.962  -80.715  1.00 35.29  ? 440 THR A CG2 1 
ATOM   3523  N N   . SER A  1 441 ? -89.918  -7.040  -80.361  1.00 38.31  ? 441 SER A N   1 
ATOM   3524  C CA  . SER A  1 441 ? -91.133  -6.316  -80.618  1.00 40.16  ? 441 SER A CA  1 
ATOM   3525  C C   . SER A  1 441 ? -91.320  -6.378  -82.128  1.00 39.65  ? 441 SER A C   1 
ATOM   3526  O O   . SER A  1 441 ? -90.457  -5.941  -82.897  1.00 37.23  ? 441 SER A O   1 
ATOM   3527  C CB  . SER A  1 441 ? -90.957  -4.879  -80.147  1.00 41.76  ? 441 SER A CB  1 
ATOM   3528  O OG  . SER A  1 441 ? -92.158  -4.373  -79.606  1.00 43.95  ? 441 SER A OG  1 
ATOM   3529  N N   . GLU A  1 442 ? -92.450  -6.916  -82.555  1.00 42.40  ? 442 GLU A N   1 
ATOM   3530  C CA  . GLU A  1 442 ? -92.765  -6.975  -83.975  1.00 42.89  ? 442 GLU A CA  1 
ATOM   3531  C C   . GLU A  1 442 ? -92.979  -5.533  -84.445  1.00 43.02  ? 442 GLU A C   1 
ATOM   3532  O O   . GLU A  1 442 ? -93.275  -4.627  -83.643  1.00 45.90  ? 442 GLU A O   1 
ATOM   3533  C CB  . GLU A  1 442 ? -93.902  -7.998  -84.137  1.00 45.69  ? 442 GLU A CB  1 
ATOM   3534  C CG  . GLU A  1 442 ? -95.062  -7.721  -83.190  1.00 46.30  ? 442 GLU A CG  1 
ATOM   3535  C CD  . GLU A  1 442 ? -96.154  -8.749  -83.229  1.00 46.81  ? 442 GLU A CD  1 
ATOM   3536  O OE1 . GLU A  1 442 ? -95.866  -9.926  -82.957  1.00 49.99  ? 442 GLU A OE1 1 
ATOM   3537  O OE2 . GLU A  1 442 ? -97.302  -8.358  -83.466  1.00 46.05  ? 442 GLU A OE2 1 
ATOM   3538  N N   . ASN A  1 443 ? -92.745  -5.307  -85.738  1.00 39.47  ? 443 ASN A N   1 
ATOM   3539  C CA  . ASN A  1 443 ? -92.740  -3.976  -86.321  1.00 38.50  ? 443 ASN A CA  1 
ATOM   3540  C C   . ASN A  1 443 ? -91.366  -3.343  -86.121  1.00 36.98  ? 443 ASN A C   1 
ATOM   3541  O O   . ASN A  1 443 ? -91.055  -2.379  -86.812  1.00 37.18  ? 443 ASN A O   1 
ATOM   3542  C CB  . ASN A  1 443 ? -93.916  -3.107  -85.861  1.00 41.15  ? 443 ASN A CB  1 
ATOM   3543  C CG  . ASN A  1 443 ? -95.260  -3.717  -86.191  1.00 43.38  ? 443 ASN A CG  1 
ATOM   3544  O OD1 . ASN A  1 443 ? -96.176  -3.815  -85.353  1.00 46.11  ? 443 ASN A OD1 1 
ATOM   3545  N ND2 . ASN A  1 443 ? -95.387  -4.153  -87.430  1.00 43.47  ? 443 ASN A ND2 1 
ATOM   3546  N N   . PHE A  1 444 ? -90.540  -3.881  -85.209  1.00 36.54  ? 444 PHE A N   1 
ATOM   3547  C CA  . PHE A  1 444 ? -89.156  -3.433  -85.068  1.00 37.15  ? 444 PHE A CA  1 
ATOM   3548  C C   . PHE A  1 444 ? -88.224  -4.529  -85.602  1.00 38.62  ? 444 PHE A C   1 
ATOM   3549  O O   . PHE A  1 444 ? -88.162  -5.615  -85.047  1.00 40.65  ? 444 PHE A O   1 
ATOM   3550  C CB  . PHE A  1 444 ? -88.757  -3.078  -83.626  1.00 34.45  ? 444 PHE A CB  1 
ATOM   3551  C CG  . PHE A  1 444 ? -89.417  -1.859  -82.988  1.00 34.31  ? 444 PHE A CG  1 
ATOM   3552  C CD1 . PHE A  1 444 ? -90.691  -1.936  -82.433  1.00 35.39  ? 444 PHE A CD1 1 
ATOM   3553  C CD2 . PHE A  1 444 ? -88.749  -0.638  -82.907  1.00 33.41  ? 444 PHE A CD2 1 
ATOM   3554  C CE1 . PHE A  1 444 ? -91.276  -0.827  -81.838  1.00 34.71  ? 444 PHE A CE1 1 
ATOM   3555  C CE2 . PHE A  1 444 ? -89.356  0.463   -82.328  1.00 32.86  ? 444 PHE A CE2 1 
ATOM   3556  C CZ  . PHE A  1 444 ? -90.602  0.368   -81.790  1.00 32.84  ? 444 PHE A CZ  1 
ATOM   3557  N N   . THR A  1 445 ? -87.447  -4.210  -86.644  1.00 40.60  ? 445 THR A N   1 
ATOM   3558  C CA  . THR A  1 445 ? -86.534  -5.158  -87.249  1.00 39.11  ? 445 THR A CA  1 
ATOM   3559  C C   . THR A  1 445 ? -85.143  -5.014  -86.638  1.00 37.92  ? 445 THR A C   1 
ATOM   3560  O O   . THR A  1 445 ? -84.556  -3.928  -86.573  1.00 37.21  ? 445 THR A O   1 
ATOM   3561  C CB  . THR A  1 445 ? -86.488  -4.936  -88.757  1.00 39.01  ? 445 THR A CB  1 
ATOM   3562  O OG1 . THR A  1 445 ? -87.816  -5.011  -89.253  1.00 36.46  ? 445 THR A OG1 1 
ATOM   3563  C CG2 . THR A  1 445 ? -85.710  -6.046  -89.446  1.00 37.99  ? 445 THR A CG2 1 
ATOM   3564  N N   . LEU A  1 446 ? -84.620  -6.149  -86.202  1.00 37.15  ? 446 LEU A N   1 
ATOM   3565  C CA  . LEU A  1 446 ? -83.233  -6.236  -85.789  1.00 36.75  ? 446 LEU A CA  1 
ATOM   3566  C C   . LEU A  1 446 ? -82.371  -6.385  -87.037  1.00 35.77  ? 446 LEU A C   1 
ATOM   3567  O O   . LEU A  1 446 ? -82.730  -7.121  -87.938  1.00 35.02  ? 446 LEU A O   1 
ATOM   3568  C CB  . LEU A  1 446 ? -83.135  -7.416  -84.823  1.00 37.60  ? 446 LEU A CB  1 
ATOM   3569  C CG  . LEU A  1 446 ? -84.061  -7.373  -83.600  1.00 37.17  ? 446 LEU A CG  1 
ATOM   3570  C CD1 . LEU A  1 446 ? -83.781  -8.575  -82.715  1.00 39.96  ? 446 LEU A CD1 1 
ATOM   3571  C CD2 . LEU A  1 446 ? -83.876  -6.120  -82.800  1.00 36.77  ? 446 LEU A CD2 1 
ATOM   3572  N N   . LEU A  1 447 ? -81.292  -5.607  -87.111  1.00 37.65  ? 447 LEU A N   1 
ATOM   3573  C CA  . LEU A  1 447 ? -80.461  -5.500  -88.295  1.00 39.79  ? 447 LEU A CA  1 
ATOM   3574  C C   . LEU A  1 447 ? -79.073  -6.039  -87.989  1.00 44.40  ? 447 LEU A C   1 
ATOM   3575  O O   . LEU A  1 447 ? -78.409  -5.542  -87.072  1.00 42.20  ? 447 LEU A O   1 
ATOM   3576  C CB  . LEU A  1 447 ? -80.295  -4.035  -88.665  1.00 41.61  ? 447 LEU A CB  1 
ATOM   3577  C CG  . LEU A  1 447 ? -81.522  -3.278  -89.161  1.00 44.03  ? 447 LEU A CG  1 
ATOM   3578  C CD1 . LEU A  1 447 ? -81.111  -1.857  -89.554  1.00 41.78  ? 447 LEU A CD1 1 
ATOM   3579  C CD2 . LEU A  1 447 ? -82.106  -4.037  -90.325  1.00 46.56  ? 447 LEU A CD2 1 
ATOM   3580  N N   . ASP A  1 448 ? -78.625  -7.006  -88.801  1.00 51.52  ? 448 ASP A N   1 
ATOM   3581  C CA  . ASP A  1 448 ? -77.237  -7.454  -88.799  1.00 52.29  ? 448 ASP A CA  1 
ATOM   3582  C C   . ASP A  1 448 ? -76.927  -8.128  -87.467  1.00 43.13  ? 448 ASP A C   1 
ATOM   3583  O O   . ASP A  1 448 ? -77.778  -8.751  -86.870  1.00 42.42  ? 448 ASP A O   1 
ATOM   3584  C CB  . ASP A  1 448 ? -76.267  -6.320  -89.158  1.00 55.01  ? 448 ASP A CB  1 
ATOM   3585  C CG  . ASP A  1 448 ? -76.439  -5.704  -90.543  1.00 56.82  ? 448 ASP A CG  1 
ATOM   3586  O OD1 . ASP A  1 448 ? -76.531  -6.498  -91.520  1.00 55.24  ? 448 ASP A OD1 1 
ATOM   3587  O OD2 . ASP A  1 448 ? -76.471  -4.445  -90.630  1.00 57.61  ? 448 ASP A OD2 1 
ATOM   3588  N N   . ASP A  1 449 ? -75.720  -7.910  -86.978  1.00 41.73  ? 449 ASP A N   1 
ATOM   3589  C CA  . ASP A  1 449 ? -75.144  -8.743  -85.950  1.00 43.48  ? 449 ASP A CA  1 
ATOM   3590  C C   . ASP A  1 449 ? -75.239  -8.030  -84.615  1.00 38.25  ? 449 ASP A C   1 
ATOM   3591  O O   . ASP A  1 449 ? -75.038  -6.815  -84.518  1.00 35.88  ? 449 ASP A O   1 
ATOM   3592  C CB  . ASP A  1 449 ? -73.704  -9.127  -86.277  1.00 44.94  ? 449 ASP A CB  1 
ATOM   3593  C CG  . ASP A  1 449 ? -73.515  -10.252 -87.298  1.00 46.96  ? 449 ASP A CG  1 
ATOM   3594  O OD1 . ASP A  1 449 ? -74.495  -10.972 -87.614  1.00 47.21  ? 449 ASP A OD1 1 
ATOM   3595  O OD2 . ASP A  1 449 ? -72.374  -10.415 -87.764  1.00 49.61  ? 449 ASP A OD2 1 
ATOM   3596  N N   . LEU A  1 450 ? -75.556  -8.838  -83.600  1.00 35.96  ? 450 LEU A N   1 
ATOM   3597  C CA  . LEU A  1 450 ? -75.314  -8.464  -82.218  1.00 34.99  ? 450 LEU A CA  1 
ATOM   3598  C C   . LEU A  1 450 ? -73.809  -8.236  -82.019  1.00 34.20  ? 450 LEU A C   1 
ATOM   3599  O O   . LEU A  1 450 ? -72.986  -9.088  -82.386  1.00 35.36  ? 450 LEU A O   1 
ATOM   3600  C CB  . LEU A  1 450 ? -75.854  -9.601  -81.352  1.00 32.27  ? 450 LEU A CB  1 
ATOM   3601  C CG  . LEU A  1 450 ? -75.615  -9.482  -79.845  1.00 31.74  ? 450 LEU A CG  1 
ATOM   3602  C CD1 . LEU A  1 450 ? -76.329  -8.246  -79.270  1.00 31.14  ? 450 LEU A CD1 1 
ATOM   3603  C CD2 . LEU A  1 450 ? -76.036  -10.763 -79.118  1.00 32.27  ? 450 LEU A CD2 1 
ATOM   3604  N N   . LYS A  1 451 ? -73.443  -7.114  -81.401  1.00 31.47  ? 451 LYS A N   1 
ATOM   3605  C CA  . LYS A  1 451 ? -72.034  -6.859  -81.088  1.00 34.09  ? 451 LYS A CA  1 
ATOM   3606  C C   . LYS A  1 451 ? -71.820  -6.906  -79.573  1.00 30.60  ? 451 LYS A C   1 
ATOM   3607  O O   . LYS A  1 451 ? -72.687  -6.469  -78.819  1.00 30.32  ? 451 LYS A O   1 
ATOM   3608  C CB  . LYS A  1 451 ? -71.561  -5.560  -81.740  1.00 36.36  ? 451 LYS A CB  1 
ATOM   3609  C CG  . LYS A  1 451 ? -71.674  -5.659  -83.252  1.00 42.16  ? 451 LYS A CG  1 
ATOM   3610  C CD  . LYS A  1 451 ? -71.003  -4.519  -83.997  1.00 46.15  ? 451 LYS A CD  1 
ATOM   3611  C CE  . LYS A  1 451 ? -71.488  -4.402  -85.402  1.00 47.62  ? 451 LYS A CE  1 
ATOM   3612  N NZ  . LYS A  1 451 ? -70.888  -3.181  -85.949  1.00 47.14  ? 451 LYS A NZ  1 
ATOM   3613  N N   . ILE A  1 452 ? -70.694  -7.508  -79.154  1.00 28.56  ? 452 ILE A N   1 
ATOM   3614  C CA  . ILE A  1 452 ? -70.331  -7.686  -77.751  1.00 28.36  ? 452 ILE A CA  1 
ATOM   3615  C C   . ILE A  1 452 ? -68.966  -7.033  -77.534  1.00 26.28  ? 452 ILE A C   1 
ATOM   3616  O O   . ILE A  1 452 ? -68.123  -7.138  -78.403  1.00 25.87  ? 452 ILE A O   1 
ATOM   3617  C CB  . ILE A  1 452 ? -70.301  -9.175  -77.338  1.00 30.20  ? 452 ILE A CB  1 
ATOM   3618  C CG1 . ILE A  1 452 ? -71.490  -10.022 -77.898  1.00 32.03  ? 452 ILE A CG1 1 
ATOM   3619  C CG2 . ILE A  1 452 ? -70.178  -9.306  -75.820  1.00 30.07  ? 452 ILE A CG2 1 
ATOM   3620  C CD1 . ILE A  1 452 ? -72.851  -9.632  -77.375  1.00 32.75  ? 452 ILE A CD1 1 
ATOM   3621  N N   . SER A  1 453 ? -68.782  -6.320  -76.417  1.00 26.04  ? 453 SER A N   1 
ATOM   3622  C CA  . SER A  1 453 ? -67.522  -5.678  -76.091  1.00 25.80  ? 453 SER A CA  1 
ATOM   3623  C C   . SER A  1 453 ? -67.189  -5.958  -74.636  1.00 27.42  ? 453 SER A C   1 
ATOM   3624  O O   . SER A  1 453 ? -68.037  -5.810  -73.781  1.00 29.12  ? 453 SER A O   1 
ATOM   3625  C CB  . SER A  1 453 ? -67.533  -4.196  -76.345  1.00 25.31  ? 453 SER A CB  1 
ATOM   3626  O OG  . SER A  1 453 ? -66.398  -3.564  -75.743  1.00 24.23  ? 453 SER A OG  1 
ATOM   3627  N N   . TYR A  1 454 ? -65.953  -6.399  -74.384  1.00 28.01  ? 454 TYR A N   1 
ATOM   3628  C CA  . TYR A  1 454 ? -65.423  -6.552  -73.042  1.00 28.52  ? 454 TYR A CA  1 
ATOM   3629  C C   . TYR A  1 454 ? -64.161  -5.681  -72.955  1.00 27.93  ? 454 TYR A C   1 
ATOM   3630  O O   . TYR A  1 454 ? -63.047  -6.176  -73.076  1.00 25.72  ? 454 TYR A O   1 
ATOM   3631  C CB  . TYR A  1 454 ? -65.195  -8.046  -72.747  1.00 29.37  ? 454 TYR A CB  1 
ATOM   3632  C CG  . TYR A  1 454 ? -65.024  -8.383  -71.271  1.00 30.36  ? 454 TYR A CG  1 
ATOM   3633  C CD1 . TYR A  1 454 ? -66.129  -8.418  -70.431  1.00 31.05  ? 454 TYR A CD1 1 
ATOM   3634  C CD2 . TYR A  1 454 ? -63.779  -8.643  -70.704  1.00 29.65  ? 454 TYR A CD2 1 
ATOM   3635  C CE1 . TYR A  1 454 ? -66.009  -8.704  -69.080  1.00 32.18  ? 454 TYR A CE1 1 
ATOM   3636  C CE2 . TYR A  1 454 ? -63.652  -8.946  -69.355  1.00 30.05  ? 454 TYR A CE2 1 
ATOM   3637  C CZ  . TYR A  1 454 ? -64.769  -8.981  -68.533  1.00 30.44  ? 454 TYR A CZ  1 
ATOM   3638  O OH  . TYR A  1 454 ? -64.732  -9.282  -67.194  1.00 28.77  ? 454 TYR A OH  1 
ATOM   3639  N N   . ASN A  1 455 ? -64.345  -4.362  -72.742  1.00 27.89  ? 455 ASN A N   1 
ATOM   3640  C CA  . ASN A  1 455 ? -63.241  -3.433  -72.889  1.00 25.99  ? 455 ASN A CA  1 
ATOM   3641  C C   . ASN A  1 455 ? -62.468  -3.400  -71.582  1.00 27.21  ? 455 ASN A C   1 
ATOM   3642  O O   . ASN A  1 455 ? -62.948  -2.889  -70.586  1.00 28.95  ? 455 ASN A O   1 
ATOM   3643  C CB  . ASN A  1 455 ? -63.715  -2.090  -73.402  1.00 25.32  ? 455 ASN A CB  1 
ATOM   3644  C CG  . ASN A  1 455 ? -62.547  -1.175  -73.686  1.00 25.13  ? 455 ASN A CG  1 
ATOM   3645  O OD1 . ASN A  1 455 ? -61.426  -1.412  -73.196  1.00 24.46  ? 455 ASN A OD1 1 
ATOM   3646  N ND2 . ASN A  1 455 ? -62.789  -0.155  -74.485  1.00 23.12  ? 455 ASN A ND2 1 
ATOM   3647  N N   . THR A  1 456 ? -61.301  -4.052  -71.569  1.00 27.74  ? 456 THR A N   1 
ATOM   3648  C CA  . THR A  1 456 ? -60.551  -4.282  -70.343  1.00 27.51  ? 456 THR A CA  1 
ATOM   3649  C C   . THR A  1 456 ? -59.644  -3.090  -70.002  1.00 26.75  ? 456 THR A C   1 
ATOM   3650  O O   . THR A  1 456 ? -58.979  -3.100  -68.979  1.00 25.27  ? 456 THR A O   1 
ATOM   3651  C CB  . THR A  1 456 ? -59.774  -5.590  -70.520  1.00 28.07  ? 456 THR A CB  1 
ATOM   3652  O OG1 . THR A  1 456 ? -59.191  -5.605  -71.820  1.00 27.66  ? 456 THR A OG1 1 
ATOM   3653  C CG2 . THR A  1 456 ? -60.671  -6.801  -70.399  1.00 28.75  ? 456 THR A CG2 1 
ATOM   3654  N N   . HIS A  1 457 ? -59.617  -2.064  -70.864  1.00 27.99  ? 457 HIS A N   1 
ATOM   3655  C CA  . HIS A  1 457 ? -59.054  -0.753  -70.550  1.00 28.24  ? 457 HIS A CA  1 
ATOM   3656  C C   . HIS A  1 457 ? -57.534  -0.770  -70.378  1.00 28.53  ? 457 HIS A C   1 
ATOM   3657  O O   . HIS A  1 457 ? -56.991  -0.033  -69.548  1.00 28.17  ? 457 HIS A O   1 
ATOM   3658  C CB  . HIS A  1 457 ? -59.700  -0.179  -69.290  1.00 29.84  ? 457 HIS A CB  1 
ATOM   3659  C CG  . HIS A  1 457 ? -61.079  0.356   -69.449  1.00 29.10  ? 457 HIS A CG  1 
ATOM   3660  N ND1 . HIS A  1 457 ? -61.336  1.694   -69.205  1.00 29.29  ? 457 HIS A ND1 1 
ATOM   3661  C CD2 . HIS A  1 457 ? -62.251  -0.227  -69.670  1.00 27.84  ? 457 HIS A CD2 1 
ATOM   3662  C CE1 . HIS A  1 457 ? -62.644  1.900   -69.339  1.00 28.29  ? 457 HIS A CE1 1 
ATOM   3663  N NE2 . HIS A  1 457 ? -63.216  0.745   -69.632  1.00 27.31  ? 457 HIS A NE2 1 
ATOM   3664  N N   . LEU A  1 458 ? -56.849  -1.609  -71.168  1.00 29.99  ? 458 LEU A N   1 
ATOM   3665  C CA  . LEU A  1 458 ? -55.409  -1.727  -71.104  1.00 29.98  ? 458 LEU A CA  1 
ATOM   3666  C C   . LEU A  1 458 ? -54.833  -0.645  -72.009  1.00 29.79  ? 458 LEU A C   1 
ATOM   3667  O O   . LEU A  1 458 ? -54.746  -0.818  -73.220  1.00 30.67  ? 458 LEU A O   1 
ATOM   3668  C CB  . LEU A  1 458 ? -54.932  -3.124  -71.508  1.00 32.05  ? 458 LEU A CB  1 
ATOM   3669  C CG  . LEU A  1 458 ? -55.454  -4.307  -70.681  1.00 32.72  ? 458 LEU A CG  1 
ATOM   3670  C CD1 . LEU A  1 458 ? -54.712  -5.571  -71.059  1.00 32.42  ? 458 LEU A CD1 1 
ATOM   3671  C CD2 . LEU A  1 458 ? -55.379  -4.128  -69.187  1.00 33.52  ? 458 LEU A CD2 1 
ATOM   3672  N N   . GLY A  1 459 ? -54.439  0.483   -71.415  1.00 30.28  ? 459 GLY A N   1 
ATOM   3673  C CA  . GLY A  1 459 ? -54.058  1.634   -72.210  1.00 29.42  ? 459 GLY A CA  1 
ATOM   3674  C C   . GLY A  1 459 ? -55.204  1.995   -73.148  1.00 29.83  ? 459 GLY A C   1 
ATOM   3675  O O   . GLY A  1 459 ? -56.361  2.107   -72.716  1.00 29.86  ? 459 GLY A O   1 
ATOM   3676  N N   . TRP A  1 460 ? -54.874  2.143   -74.436  1.00 30.87  ? 460 TRP A N   1 
ATOM   3677  C CA  . TRP A  1 460 ? -55.857  2.490   -75.459  1.00 29.70  ? 460 TRP A CA  1 
ATOM   3678  C C   . TRP A  1 460 ? -56.525  1.261   -76.091  1.00 27.91  ? 460 TRP A C   1 
ATOM   3679  O O   . TRP A  1 460 ? -57.465  1.420   -76.856  1.00 26.70  ? 460 TRP A O   1 
ATOM   3680  C CB  . TRP A  1 460 ? -55.209  3.344   -76.548  1.00 28.71  ? 460 TRP A CB  1 
ATOM   3681  C CG  . TRP A  1 460 ? -54.822  4.706   -76.057  1.00 31.29  ? 460 TRP A CG  1 
ATOM   3682  C CD1 . TRP A  1 460 ? -53.547  5.168   -75.879  1.00 31.54  ? 460 TRP A CD1 1 
ATOM   3683  C CD2 . TRP A  1 460 ? -55.706  5.782   -75.646  1.00 31.34  ? 460 TRP A CD2 1 
ATOM   3684  N NE1 . TRP A  1 460 ? -53.574  6.465   -75.433  1.00 32.30  ? 460 TRP A NE1 1 
ATOM   3685  C CE2 . TRP A  1 460 ? -54.877  6.874   -75.277  1.00 32.13  ? 460 TRP A CE2 1 
ATOM   3686  C CE3 . TRP A  1 460 ? -57.089  5.946   -75.578  1.00 28.47  ? 460 TRP A CE3 1 
ATOM   3687  C CZ2 . TRP A  1 460 ? -55.394  8.091   -74.825  1.00 30.97  ? 460 TRP A CZ2 1 
ATOM   3688  C CZ3 . TRP A  1 460 ? -57.596  7.147   -75.137  1.00 30.54  ? 460 TRP A CZ3 1 
ATOM   3689  C CH2 . TRP A  1 460 ? -56.765  8.211   -74.759  1.00 30.25  ? 460 TRP A CH2 1 
ATOM   3690  N N   . ALA A  1 461 ? -56.052  0.046   -75.781  1.00 26.87  ? 461 ALA A N   1 
ATOM   3691  C CA  . ALA A  1 461 ? -56.521  -1.141  -76.471  1.00 26.88  ? 461 ALA A CA  1 
ATOM   3692  C C   . ALA A  1 461 ? -57.988  -1.417  -76.097  1.00 27.67  ? 461 ALA A C   1 
ATOM   3693  O O   . ALA A  1 461 ? -58.382  -1.291  -74.949  1.00 28.21  ? 461 ALA A O   1 
ATOM   3694  C CB  . ALA A  1 461 ? -55.605  -2.300  -76.141  1.00 26.51  ? 461 ALA A CB  1 
ATOM   3695  N N   . ILE A  1 462 ? -58.785  -1.858  -77.076  1.00 30.52  ? 462 ILE A N   1 
ATOM   3696  C CA  . ILE A  1 462 ? -60.242  -1.994  -76.955  1.00 30.44  ? 462 ILE A CA  1 
ATOM   3697  C C   . ILE A  1 462 ? -60.642  -3.261  -76.207  1.00 28.88  ? 462 ILE A C   1 
ATOM   3698  O O   . ILE A  1 462 ? -61.742  -3.323  -75.692  1.00 29.87  ? 462 ILE A O   1 
ATOM   3699  C CB  . ILE A  1 462 ? -60.861  -1.931  -78.364  1.00 31.78  ? 462 ILE A CB  1 
ATOM   3700  C CG1 . ILE A  1 462 ? -60.646  -0.561  -78.943  1.00 34.58  ? 462 ILE A CG1 1 
ATOM   3701  C CG2 . ILE A  1 462 ? -62.341  -2.269  -78.372  1.00 36.20  ? 462 ILE A CG2 1 
ATOM   3702  C CD1 . ILE A  1 462 ? -61.184  0.563   -78.068  1.00 33.39  ? 462 ILE A CD1 1 
ATOM   3703  N N   . GLY A  1 463 ? -59.778  -4.283  -76.184  1.00 29.60  ? 463 GLY A N   1 
ATOM   3704  C CA  . GLY A  1 463 ? -60.122  -5.597  -75.659  1.00 27.90  ? 463 GLY A CA  1 
ATOM   3705  C C   . GLY A  1 463 ? -60.850  -6.391  -76.730  1.00 28.94  ? 463 GLY A C   1 
ATOM   3706  O O   . GLY A  1 463 ? -61.025  -5.925  -77.846  1.00 31.05  ? 463 GLY A O   1 
ATOM   3707  N N   . SER A  1 464 ? -61.362  -7.551  -76.344  1.00 31.01  ? 464 SER A N   1 
ATOM   3708  C CA  . SER A  1 464 ? -62.143  -8.430  -77.189  1.00 31.70  ? 464 SER A CA  1 
ATOM   3709  C C   . SER A  1 464 ? -63.499  -7.840  -77.592  1.00 31.94  ? 464 SER A C   1 
ATOM   3710  O O   . SER A  1 464 ? -64.211  -7.239  -76.797  1.00 31.45  ? 464 SER A O   1 
ATOM   3711  C CB  . SER A  1 464 ? -62.373  -9.736  -76.458  1.00 32.91  ? 464 SER A CB  1 
ATOM   3712  O OG  . SER A  1 464 ? -61.140  -10.345 -76.107  1.00 37.22  ? 464 SER A OG  1 
ATOM   3713  N N   . GLN A  1 465 ? -63.898  -8.166  -78.827  1.00 32.90  ? 465 GLN A N   1 
ATOM   3714  C CA  . GLN A  1 465 ? -65.237  -7.955  -79.335  1.00 32.96  ? 465 GLN A CA  1 
ATOM   3715  C C   . GLN A  1 465 ? -65.758  -9.252  -79.957  1.00 33.69  ? 465 GLN A C   1 
ATOM   3716  O O   . GLN A  1 465 ? -65.021  -10.215 -80.153  1.00 32.19  ? 465 GLN A O   1 
ATOM   3717  C CB  . GLN A  1 465 ? -65.230  -6.912  -80.437  1.00 31.50  ? 465 GLN A CB  1 
ATOM   3718  C CG  . GLN A  1 465 ? -64.573  -5.616  -80.017  1.00 35.54  ? 465 GLN A CG  1 
ATOM   3719  C CD  . GLN A  1 465 ? -64.770  -4.516  -81.038  1.00 34.92  ? 465 GLN A CD  1 
ATOM   3720  O OE1 . GLN A  1 465 ? -63.811  -4.110  -81.696  1.00 37.47  ? 465 GLN A OE1 1 
ATOM   3721  N NE2 . GLN A  1 465 ? -66.000  -4.046  -81.189  1.00 31.62  ? 465 GLN A NE2 1 
ATOM   3722  N N   . ALA A  1 466 ? -67.040  -9.270  -80.301  1.00 31.95  ? 466 ALA A N   1 
ATOM   3723  C CA  . ALA A  1 466 ? -67.558  -10.419 -81.007  1.00 32.98  ? 466 ALA A CA  1 
ATOM   3724  C C   . ALA A  1 466 ? -68.789  -9.963  -81.758  1.00 31.74  ? 466 ALA A C   1 
ATOM   3725  O O   . ALA A  1 466 ? -69.459  -9.067  -81.267  1.00 31.06  ? 466 ALA A O   1 
ATOM   3726  C CB  . ALA A  1 466 ? -67.845  -11.546 -80.028  1.00 32.42  ? 466 ALA A CB  1 
ATOM   3727  N N   . SER A  1 467 ? -68.983  -10.512 -82.963  1.00 32.27  ? 467 SER A N   1 
ATOM   3728  C CA  . SER A  1 467 ? -70.194  -10.354 -83.746  1.00 34.36  ? 467 SER A CA  1 
ATOM   3729  C C   . SER A  1 467 ? -70.944  -11.661 -83.685  1.00 34.24  ? 467 SER A C   1 
ATOM   3730  O O   . SER A  1 467 ? -70.381  -12.641 -84.092  1.00 37.41  ? 467 SER A O   1 
ATOM   3731  C CB  . SER A  1 467 ? -69.932  -10.091 -85.185  1.00 34.61  ? 467 SER A CB  1 
ATOM   3732  O OG  . SER A  1 467 ? -69.672  -8.730  -85.404  1.00 37.47  ? 467 SER A OG  1 
ATOM   3733  N N   . VAL A  1 468 ? -72.220  -11.641 -83.314  1.00 36.73  ? 468 VAL A N   1 
ATOM   3734  C CA  . VAL A  1 468 ? -73.021  -12.847 -83.247  1.00 36.05  ? 468 VAL A CA  1 
ATOM   3735  C C   . VAL A  1 468 ? -74.222  -12.677 -84.164  1.00 39.16  ? 468 VAL A C   1 
ATOM   3736  O O   . VAL A  1 468 ? -75.016  -11.740 -83.976  1.00 38.28  ? 468 VAL A O   1 
ATOM   3737  C CB  . VAL A  1 468 ? -73.483  -13.161 -81.818  1.00 34.35  ? 468 VAL A CB  1 
ATOM   3738  C CG1 . VAL A  1 468 ? -74.176  -14.526 -81.771  1.00 35.67  ? 468 VAL A CG1 1 
ATOM   3739  C CG2 . VAL A  1 468 ? -72.328  -13.127 -80.838  1.00 33.34  ? 468 VAL A CG2 1 
ATOM   3740  N N   . SER A  1 469 ? -74.348  -13.616 -85.119  1.00 42.48  ? 469 SER A N   1 
ATOM   3741  C CA  . SER A  1 469 ? -75.538  -13.746 -85.953  1.00 44.00  ? 469 SER A CA  1 
ATOM   3742  C C   . SER A  1 469 ? -76.703  -14.204 -85.090  1.00 43.16  ? 469 SER A C   1 
ATOM   3743  O O   . SER A  1 469 ? -76.557  -15.129 -84.296  1.00 41.16  ? 469 SER A O   1 
ATOM   3744  C CB  . SER A  1 469 ? -75.361  -14.725 -87.099  1.00 44.45  ? 469 SER A CB  1 
ATOM   3745  O OG  . SER A  1 469 ? -76.463  -14.658 -87.995  1.00 43.58  ? 469 SER A OG  1 
ATOM   3746  N N   . ILE A  1 470 ? -77.853  -13.556 -85.290  1.00 45.63  ? 470 ILE A N   1 
ATOM   3747  C CA  . ILE A  1 470 ? -79.098  -13.985 -84.666  1.00 47.26  ? 470 ILE A CA  1 
ATOM   3748  C C   . ILE A  1 470 ? -80.132  -14.395 -85.718  1.00 46.67  ? 470 ILE A C   1 
ATOM   3749  O O   . ILE A  1 470 ? -81.282  -14.538 -85.367  1.00 50.04  ? 470 ILE A O   1 
ATOM   3750  C CB  . ILE A  1 470 ? -79.650  -12.886 -83.746  1.00 45.00  ? 470 ILE A CB  1 
ATOM   3751  C CG1 . ILE A  1 470 ? -79.781  -11.562 -84.483  1.00 45.78  ? 470 ILE A CG1 1 
ATOM   3752  C CG2 . ILE A  1 470 ? -78.790  -12.748 -82.499  1.00 43.47  ? 470 ILE A CG2 1 
ATOM   3753  C CD1 . ILE A  1 470 ? -80.704  -10.587 -83.792  1.00 45.53  ? 470 ILE A CD1 1 
ATOM   3754  N N   . SER A  1 471 ? -79.733  -14.609 -86.979  1.00 49.17  ? 471 SER A N   1 
ATOM   3755  C CA  . SER A  1 471 ? -80.624  -15.085 -88.037  1.00 50.69  ? 471 SER A CA  1 
ATOM   3756  C C   . SER A  1 471 ? -81.491  -16.261 -87.599  1.00 49.04  ? 471 SER A C   1 
ATOM   3757  O O   . SER A  1 471 ? -82.705  -16.235 -87.781  1.00 53.38  ? 471 SER A O   1 
ATOM   3758  C CB  . SER A  1 471 ? -79.842  -15.470 -89.256  1.00 51.46  ? 471 SER A CB  1 
ATOM   3759  O OG  . SER A  1 471 ? -79.323  -14.294 -89.856  1.00 55.17  ? 471 SER A OG  1 
ATOM   3760  N N   . ASP A  1 472 ? -80.851  -17.267 -87.006  1.00 47.42  ? 472 ASP A N   1 
ATOM   3761  C CA  . ASP A  1 472 ? -81.485  -18.514 -86.599  1.00 50.38  ? 472 ASP A CA  1 
ATOM   3762  C C   . ASP A  1 472 ? -82.539  -18.313 -85.491  1.00 51.33  ? 472 ASP A C   1 
ATOM   3763  O O   . ASP A  1 472 ? -83.145  -19.289 -85.051  1.00 51.85  ? 472 ASP A O   1 
ATOM   3764  C CB  . ASP A  1 472 ? -80.420  -19.550 -86.233  1.00 48.27  ? 472 ASP A CB  1 
ATOM   3765  C CG  . ASP A  1 472 ? -79.399  -19.136 -85.169  1.00 53.06  ? 472 ASP A CG  1 
ATOM   3766  O OD1 . ASP A  1 472 ? -78.886  -17.983 -85.223  1.00 57.30  ? 472 ASP A OD1 1 
ATOM   3767  O OD2 . ASP A  1 472 ? -79.068  -19.975 -84.299  1.00 55.42  ? 472 ASP A OD2 1 
ATOM   3768  N N   . GLN A  1 473 ? -82.770  -17.076 -85.024  1.00 49.13  ? 473 GLN A N   1 
ATOM   3769  C CA  . GLN A  1 473 ? -83.568  -16.835 -83.828  1.00 48.78  ? 473 GLN A CA  1 
ATOM   3770  C C   . GLN A  1 473 ? -84.548  -15.669 -84.012  1.00 48.93  ? 473 GLN A C   1 
ATOM   3771  O O   . GLN A  1 473 ? -85.202  -15.276 -83.036  1.00 45.66  ? 473 GLN A O   1 
ATOM   3772  C CB  . GLN A  1 473 ? -82.721  -16.395 -82.625  1.00 49.40  ? 473 GLN A CB  1 
ATOM   3773  C CG  . GLN A  1 473 ? -81.849  -17.459 -81.949  1.00 48.56  ? 473 GLN A CG  1 
ATOM   3774  C CD  . GLN A  1 473 ? -81.274  -16.981 -80.623  1.00 44.86  ? 473 GLN A CD  1 
ATOM   3775  O OE1 . GLN A  1 473 ? -81.889  -17.075 -79.546  1.00 45.15  ? 473 GLN A OE1 1 
ATOM   3776  N NE2 . GLN A  1 473 ? -80.060  -16.464 -80.686  1.00 40.34  ? 473 GLN A NE2 1 
ATOM   3777  N N   . LEU A  1 474 ? -84.665  -15.117 -85.235  1.00 49.84  ? 474 LEU A N   1 
ATOM   3778  C CA  . LEU A  1 474 ? -85.344  -13.832 -85.444  1.00 53.89  ? 474 LEU A CA  1 
ATOM   3779  C C   . LEU A  1 474 ? -86.834  -13.886 -85.084  1.00 55.86  ? 474 LEU A C   1 
ATOM   3780  O O   . LEU A  1 474 ? -87.387  -12.866 -84.640  1.00 51.37  ? 474 LEU A O   1 
ATOM   3781  C CB  . LEU A  1 474 ? -85.146  -13.285 -86.860  1.00 54.93  ? 474 LEU A CB  1 
ATOM   3782  C CG  . LEU A  1 474 ? -83.794  -12.610 -87.133  1.00 57.18  ? 474 LEU A CG  1 
ATOM   3783  C CD1 . LEU A  1 474 ? -83.705  -12.130 -88.574  1.00 57.67  ? 474 LEU A CD1 1 
ATOM   3784  C CD2 . LEU A  1 474 ? -83.540  -11.452 -86.173  1.00 53.72  ? 474 LEU A CD2 1 
ATOM   3785  N N   . ASP A  1 475 ? -87.440  -15.079 -85.232  1.00 54.83  ? 475 ASP A N   1 
ATOM   3786  C CA  . ASP A  1 475 ? -88.857  -15.293 -84.998  1.00 60.41  ? 475 ASP A CA  1 
ATOM   3787  C C   . ASP A  1 475 ? -89.178  -15.544 -83.523  1.00 59.39  ? 475 ASP A C   1 
ATOM   3788  O O   . ASP A  1 475 ? -90.342  -15.717 -83.213  1.00 63.54  ? 475 ASP A O   1 
ATOM   3789  C CB  . ASP A  1 475 ? -89.391  -16.468 -85.815  1.00 65.40  ? 475 ASP A CB  1 
ATOM   3790  C CG  . ASP A  1 475 ? -89.893  -16.116 -87.214  1.00 69.45  ? 475 ASP A CG  1 
ATOM   3791  O OD1 . ASP A  1 475 ? -89.779  -14.905 -87.622  1.00 61.11  ? 475 ASP A OD1 1 
ATOM   3792  O OD2 . ASP A  1 475 ? -90.413  -17.050 -87.876  1.00 67.40  ? 475 ASP A OD2 1 
ATOM   3793  N N   . LYS A  1 476 ? -88.188  -15.586 -82.622  1.00 54.44  ? 476 LYS A N   1 
ATOM   3794  C CA  . LYS A  1 476 ? -88.459  -15.798 -81.205  1.00 53.04  ? 476 LYS A CA  1 
ATOM   3795  C C   . LYS A  1 476 ? -88.782  -14.473 -80.511  1.00 50.67  ? 476 LYS A C   1 
ATOM   3796  O O   . LYS A  1 476 ? -88.303  -13.416 -80.903  1.00 50.88  ? 476 LYS A O   1 
ATOM   3797  C CB  . LYS A  1 476 ? -87.265  -16.446 -80.494  1.00 53.82  ? 476 LYS A CB  1 
ATOM   3798  C CG  . LYS A  1 476 ? -86.949  -17.870 -80.919  1.00 58.21  ? 476 LYS A CG  1 
ATOM   3799  C CD  . LYS A  1 476 ? -85.569  -18.381 -80.495  1.00 60.78  ? 476 LYS A CD  1 
ATOM   3800  C CE  . LYS A  1 476 ? -85.398  -18.704 -79.028  1.00 61.94  ? 476 LYS A CE  1 
ATOM   3801  N NZ  . LYS A  1 476 ? -84.019  -18.470 -78.573  1.00 59.57  ? 476 LYS A NZ  1 
ATOM   3802  N N   . LYS A  1 477 ? -89.580  -14.543 -79.442  1.00 50.71  ? 477 LYS A N   1 
ATOM   3803  C CA  . LYS A  1 477 ? -89.895  -13.388 -78.617  1.00 48.32  ? 477 LYS A CA  1 
ATOM   3804  C C   . LYS A  1 477 ? -88.650  -12.940 -77.838  1.00 45.75  ? 477 LYS A C   1 
ATOM   3805  O O   . LYS A  1 477 ? -88.365  -11.737 -77.705  1.00 42.21  ? 477 LYS A O   1 
ATOM   3806  C CB  . LYS A  1 477 ? -91.105  -13.772 -77.752  1.00 49.55  ? 477 LYS A CB  1 
ATOM   3807  C CG  . LYS A  1 477 ? -91.510  -12.782 -76.657  1.00 52.24  ? 477 LYS A CG  1 
ATOM   3808  C CD  . LYS A  1 477 ? -91.954  -11.402 -77.136  1.00 52.61  ? 477 LYS A CD  1 
ATOM   3809  C CE  . LYS A  1 477 ? -92.197  -10.418 -76.030  1.00 52.58  ? 477 LYS A CE  1 
ATOM   3810  N NZ  . LYS A  1 477 ? -92.320  -9.083  -76.622  1.00 51.24  ? 477 LYS A NZ  1 
ATOM   3811  N N   . ILE A  1 478 ? -87.921  -13.925 -77.297  1.00 44.40  ? 478 ILE A N   1 
ATOM   3812  C CA  . ILE A  1 478 ? -86.733  -13.672 -76.497  1.00 42.80  ? 478 ILE A CA  1 
ATOM   3813  C C   . ILE A  1 478 ? -85.536  -14.296 -77.199  1.00 40.43  ? 478 ILE A C   1 
ATOM   3814  O O   . ILE A  1 478 ? -85.538  -15.466 -77.510  1.00 42.14  ? 478 ILE A O   1 
ATOM   3815  C CB  . ILE A  1 478 ? -86.916  -14.175 -75.056  1.00 43.12  ? 478 ILE A CB  1 
ATOM   3816  C CG1 . ILE A  1 478 ? -88.173  -13.546 -74.407  1.00 44.40  ? 478 ILE A CG1 1 
ATOM   3817  C CG2 . ILE A  1 478 ? -85.657  -13.894 -74.243  1.00 42.73  ? 478 ILE A CG2 1 
ATOM   3818  C CD1 . ILE A  1 478 ? -88.526  -14.080 -73.029  1.00 45.78  ? 478 ILE A CD1 1 
ATOM   3819  N N   . ILE A  1 479 ? -84.544  -13.478 -77.503  1.00 39.33  ? 479 ILE A N   1 
ATOM   3820  C CA  . ILE A  1 479 ? -83.357  -13.927 -78.214  1.00 39.96  ? 479 ILE A CA  1 
ATOM   3821  C C   . ILE A  1 479 ? -82.167  -13.832 -77.262  1.00 38.79  ? 479 ILE A C   1 
ATOM   3822  O O   . ILE A  1 479 ? -81.971  -12.760 -76.670  1.00 37.81  ? 479 ILE A O   1 
ATOM   3823  C CB  . ILE A  1 479 ? -83.122  -13.028 -79.437  1.00 38.26  ? 479 ILE A CB  1 
ATOM   3824  C CG1 . ILE A  1 479 ? -84.235  -13.214 -80.480  1.00 38.26  ? 479 ILE A CG1 1 
ATOM   3825  C CG2 . ILE A  1 479 ? -81.719  -13.258 -80.001  1.00 38.80  ? 479 ILE A CG2 1 
ATOM   3826  C CD1 . ILE A  1 479 ? -84.039  -12.456 -81.787  1.00 36.79  ? 479 ILE A CD1 1 
ATOM   3827  N N   . THR A  1 480 ? -81.382  -14.915 -77.152  1.00 36.47  ? 480 THR A N   1 
ATOM   3828  C CA  . THR A  1 480 ? -80.288  -14.968 -76.190  1.00 36.11  ? 480 THR A CA  1 
ATOM   3829  C C   . THR A  1 480 ? -78.950  -15.221 -76.889  1.00 36.06  ? 480 THR A C   1 
ATOM   3830  O O   . THR A  1 480 ? -78.858  -15.669 -78.027  1.00 35.91  ? 480 THR A O   1 
ATOM   3831  C CB  . THR A  1 480 ? -80.570  -15.994 -75.090  1.00 38.39  ? 480 THR A CB  1 
ATOM   3832  O OG1 . THR A  1 480 ? -80.586  -17.331 -75.614  1.00 39.83  ? 480 THR A OG1 1 
ATOM   3833  C CG2 . THR A  1 480 ? -81.885  -15.709 -74.377  1.00 38.80  ? 480 THR A CG2 1 
ATOM   3834  N N   . SER A  1 481 ? -77.874  -14.898 -76.181  1.00 36.19  ? 481 SER A N   1 
ATOM   3835  C CA  . SER A  1 481 ? -76.532  -15.243 -76.610  1.00 34.35  ? 481 SER A CA  1 
ATOM   3836  C C   . SER A  1 481 ? -75.670  -15.257 -75.364  1.00 34.21  ? 481 SER A C   1 
ATOM   3837  O O   . SER A  1 481 ? -75.998  -14.577 -74.407  1.00 35.37  ? 481 SER A O   1 
ATOM   3838  C CB  . SER A  1 481 ? -76.014  -14.277 -77.619  1.00 33.89  ? 481 SER A CB  1 
ATOM   3839  O OG  . SER A  1 481 ? -74.630  -14.470 -77.856  1.00 34.56  ? 481 SER A OG  1 
ATOM   3840  N N   . GLU A  1 482 ? -74.620  -16.072 -75.371  1.00 34.54  ? 482 GLU A N   1 
ATOM   3841  C CA  . GLU A  1 482 ? -73.674  -16.129 -74.266  1.00 34.02  ? 482 GLU A CA  1 
ATOM   3842  C C   . GLU A  1 482 ? -72.243  -16.091 -74.834  1.00 32.61  ? 482 GLU A C   1 
ATOM   3843  O O   . GLU A  1 482 ? -71.881  -16.956 -75.623  1.00 32.99  ? 482 GLU A O   1 
ATOM   3844  C CB  . GLU A  1 482 ? -74.085  -17.374 -73.474  1.00 32.94  ? 482 GLU A CB  1 
ATOM   3845  C CG  . GLU A  1 482 ? -73.246  -17.594 -72.220  1.00 33.35  ? 482 GLU A CG  1 
ATOM   3846  C CD  . GLU A  1 482 ? -73.467  -18.894 -71.479  1.00 34.41  ? 482 GLU A CD  1 
ATOM   3847  O OE1 . GLU A  1 482 ? -73.617  -19.947 -72.146  1.00 36.76  ? 482 GLU A OE1 1 
ATOM   3848  O OE2 . GLU A  1 482 ? -73.438  -18.861 -70.244  1.00 33.40  ? 482 GLU A OE2 1 
ATOM   3849  N N   . ASN A  1 483 ? -71.423  -15.124 -74.435  1.00 29.80  ? 483 ASN A N   1 
ATOM   3850  C CA  . ASN A  1 483 ? -70.093  -15.002 -75.009  1.00 31.43  ? 483 ASN A CA  1 
ATOM   3851  C C   . ASN A  1 483 ? -69.078  -14.909 -73.877  1.00 31.13  ? 483 ASN A C   1 
ATOM   3852  O O   . ASN A  1 483 ? -69.351  -14.278 -72.870  1.00 32.79  ? 483 ASN A O   1 
ATOM   3853  C CB  . ASN A  1 483 ? -70.019  -13.836 -75.997  1.00 34.16  ? 483 ASN A CB  1 
ATOM   3854  C CG  . ASN A  1 483 ? -71.002  -14.002 -77.139  1.00 36.84  ? 483 ASN A CG  1 
ATOM   3855  O OD1 . ASN A  1 483 ? -70.624  -14.540 -78.178  1.00 37.47  ? 483 ASN A OD1 1 
ATOM   3856  N ND2 . ASN A  1 483 ? -72.269  -13.636 -76.967  1.00 37.16  ? 483 ASN A ND2 1 
ATOM   3857  N N   . PHE A  1 484 ? -67.917  -15.563 -74.021  1.00 31.42  ? 484 PHE A N   1 
ATOM   3858  C CA  . PHE A  1 484 ? -66.930  -15.702 -72.944  1.00 30.79  ? 484 PHE A CA  1 
ATOM   3859  C C   . PHE A  1 484 ? -65.644  -14.922 -73.276  1.00 30.75  ? 484 PHE A C   1 
ATOM   3860  O O   . PHE A  1 484 ? -65.244  -14.799 -74.433  1.00 31.96  ? 484 PHE A O   1 
ATOM   3861  C CB  . PHE A  1 484 ? -66.661  -17.198 -72.706  1.00 30.70  ? 484 PHE A CB  1 
ATOM   3862  C CG  . PHE A  1 484 ? -67.862  -18.040 -72.283  1.00 30.95  ? 484 PHE A CG  1 
ATOM   3863  C CD1 . PHE A  1 484 ? -68.210  -18.175 -70.941  1.00 31.12  ? 484 PHE A CD1 1 
ATOM   3864  C CD2 . PHE A  1 484 ? -68.645  -18.707 -73.221  1.00 31.51  ? 484 PHE A CD2 1 
ATOM   3865  C CE1 . PHE A  1 484 ? -69.325  -18.906 -70.554  1.00 31.63  ? 484 PHE A CE1 1 
ATOM   3866  C CE2 . PHE A  1 484 ? -69.737  -19.483 -72.829  1.00 32.06  ? 484 PHE A CE2 1 
ATOM   3867  C CZ  . PHE A  1 484 ? -70.064  -19.600 -71.501  1.00 32.51  ? 484 PHE A CZ  1 
ATOM   3868  N N   . PHE A  1 485 ? -64.987  -14.374 -72.249  1.00 30.69  ? 485 PHE A N   1 
ATOM   3869  C CA  . PHE A  1 485 ? -63.785  -13.577 -72.406  1.00 29.45  ? 485 PHE A CA  1 
ATOM   3870  C C   . PHE A  1 485 ? -62.803  -13.884 -71.275  1.00 29.99  ? 485 PHE A C   1 
ATOM   3871  O O   . PHE A  1 485 ? -63.212  -13.977 -70.097  1.00 30.39  ? 485 PHE A O   1 
ATOM   3872  C CB  . PHE A  1 485 ? -64.209  -12.110 -72.374  1.00 30.16  ? 485 PHE A CB  1 
ATOM   3873  C CG  . PHE A  1 485 ? -65.169  -11.752 -73.490  1.00 29.95  ? 485 PHE A CG  1 
ATOM   3874  C CD1 . PHE A  1 485 ? -64.715  -11.534 -74.780  1.00 30.62  ? 485 PHE A CD1 1 
ATOM   3875  C CD2 . PHE A  1 485 ? -66.531  -11.687 -73.254  1.00 31.26  ? 485 PHE A CD2 1 
ATOM   3876  C CE1 . PHE A  1 485 ? -65.605  -11.235 -75.803  1.00 31.36  ? 485 PHE A CE1 1 
ATOM   3877  C CE2 . PHE A  1 485 ? -67.418  -11.375 -74.273  1.00 31.51  ? 485 PHE A CE2 1 
ATOM   3878  C CZ  . PHE A  1 485 ? -66.955  -11.163 -75.551  1.00 30.91  ? 485 PHE A CZ  1 
ATOM   3879  N N   . ASN A  1 486 ? -61.512  -14.056 -71.636  1.00 29.05  ? 486 ASN A N   1 
ATOM   3880  C CA  . ASN A  1 486 ? -60.479  -14.245 -70.624  1.00 29.62  ? 486 ASN A CA  1 
ATOM   3881  C C   . ASN A  1 486 ? -60.238  -12.897 -69.970  1.00 29.66  ? 486 ASN A C   1 
ATOM   3882  O O   . ASN A  1 486 ? -60.282  -11.896 -70.662  1.00 29.69  ? 486 ASN A O   1 
ATOM   3883  C CB  . ASN A  1 486 ? -59.200  -14.875 -71.169  1.00 29.66  ? 486 ASN A CB  1 
ATOM   3884  C CG  . ASN A  1 486 ? -59.405  -16.328 -71.527  1.00 29.27  ? 486 ASN A CG  1 
ATOM   3885  O OD1 . ASN A  1 486 ? -59.420  -16.679 -72.698  1.00 28.51  ? 486 ASN A OD1 1 
ATOM   3886  N ND2 . ASN A  1 486 ? -59.660  -17.182 -70.555  1.00 30.81  ? 486 ASN A ND2 1 
ATOM   3887  N N   . ILE A  1 487 ? -60.094  -12.865 -68.637  1.00 31.28  ? 487 ILE A N   1 
ATOM   3888  C CA  . ILE A  1 487 ? -59.864  -11.601 -67.945  1.00 31.50  ? 487 ILE A CA  1 
ATOM   3889  C C   . ILE A  1 487 ? -58.362  -11.439 -67.752  1.00 30.93  ? 487 ILE A C   1 
ATOM   3890  O O   . ILE A  1 487 ? -57.738  -12.268 -67.093  1.00 31.89  ? 487 ILE A O   1 
ATOM   3891  C CB  . ILE A  1 487 ? -60.637  -11.508 -66.604  1.00 32.18  ? 487 ILE A CB  1 
ATOM   3892  C CG1 . ILE A  1 487 ? -62.131  -11.781 -66.747  1.00 32.02  ? 487 ILE A CG1 1 
ATOM   3893  C CG2 . ILE A  1 487 ? -60.417  -10.150 -65.937  1.00 32.08  ? 487 ILE A CG2 1 
ATOM   3894  C CD1 . ILE A  1 487 ? -62.823  -11.978 -65.417  1.00 32.37  ? 487 ILE A CD1 1 
ATOM   3895  N N   . PRO A  1 488 ? -57.725  -10.380 -68.293  1.00 31.52  ? 488 PRO A N   1 
ATOM   3896  C CA  . PRO A  1 488 ? -56.304  -10.132 -68.014  1.00 31.78  ? 488 PRO A CA  1 
ATOM   3897  C C   . PRO A  1 488 ? -56.107  -9.803  -66.530  1.00 33.01  ? 488 PRO A C   1 
ATOM   3898  O O   . PRO A  1 488 ? -56.934  -9.159  -65.907  1.00 31.78  ? 488 PRO A O   1 
ATOM   3899  C CB  . PRO A  1 488 ? -55.912  -8.963  -68.932  1.00 31.19  ? 488 PRO A CB  1 
ATOM   3900  C CG  . PRO A  1 488 ? -57.085  -8.785  -69.865  1.00 31.85  ? 488 PRO A CG  1 
ATOM   3901  C CD  . PRO A  1 488 ? -58.328  -9.363  -69.175  1.00 31.49  ? 488 PRO A CD  1 
ATOM   3902  N N   . ASP A  1 489 ? -55.019  -10.300 -65.947  1.00 35.78  ? 489 ASP A N   1 
ATOM   3903  C CA  . ASP A  1 489 ? -54.666  -10.061 -64.553  1.00 37.54  ? 489 ASP A CA  1 
ATOM   3904  C C   . ASP A  1 489 ? -54.509  -8.565  -64.254  1.00 36.96  ? 489 ASP A C   1 
ATOM   3905  O O   . ASP A  1 489 ? -54.697  -8.136  -63.108  1.00 36.35  ? 489 ASP A O   1 
ATOM   3906  C CB  . ASP A  1 489 ? -53.366  -10.782 -64.224  1.00 38.48  ? 489 ASP A CB  1 
ATOM   3907  C CG  . ASP A  1 489 ? -53.513  -12.292 -64.198  1.00 41.71  ? 489 ASP A CG  1 
ATOM   3908  O OD1 . ASP A  1 489 ? -54.671  -12.772 -64.094  1.00 40.96  ? 489 ASP A OD1 1 
ATOM   3909  O OD2 . ASP A  1 489 ? -52.474  -12.970 -64.262  1.00 44.03  ? 489 ASP A OD2 1 
ATOM   3910  N N   . ASN A  1 490 ? -54.132  -7.784  -65.281  1.00 34.82  ? 490 ASN A N   1 
ATOM   3911  C CA  . ASN A  1 490 ? -53.891  -6.365  -65.103  1.00 33.48  ? 490 ASN A CA  1 
ATOM   3912  C C   . ASN A  1 490 ? -55.085  -5.549  -65.593  1.00 31.21  ? 490 ASN A C   1 
ATOM   3913  O O   . ASN A  1 490 ? -54.964  -4.357  -65.850  1.00 29.46  ? 490 ASN A O   1 
ATOM   3914  C CB  . ASN A  1 490 ? -52.559  -5.945  -65.724  1.00 32.81  ? 490 ASN A CB  1 
ATOM   3915  C CG  . ASN A  1 490 ? -52.535  -6.109  -67.219  1.00 32.25  ? 490 ASN A CG  1 
ATOM   3916  O OD1 . ASN A  1 490 ? -53.226  -6.967  -67.800  1.00 31.41  ? 490 ASN A OD1 1 
ATOM   3917  N ND2 . ASN A  1 490 ? -51.698  -5.300  -67.844  1.00 32.35  ? 490 ASN A ND2 1 
ATOM   3918  N N   . CYS A  1 491 ? -56.244  -6.196  -65.720  1.00 32.22  ? 491 CYS A N   1 
ATOM   3919  C CA  . CYS A  1 491 ? -57.493  -5.472  -65.886  1.00 31.52  ? 491 CYS A CA  1 
ATOM   3920  C C   . CYS A  1 491 ? -57.921  -5.017  -64.496  1.00 31.81  ? 491 CYS A C   1 
ATOM   3921  O O   . CYS A  1 491 ? -58.140  -5.852  -63.606  1.00 31.64  ? 491 CYS A O   1 
ATOM   3922  C CB  . CYS A  1 491 ? -58.592  -6.322  -66.525  1.00 31.82  ? 491 CYS A CB  1 
ATOM   3923  S SG  . CYS A  1 491 ? -60.152  -5.423  -66.765  1.00 31.72  ? 491 CYS A SG  1 
ATOM   3924  N N   . TRP A  1 492 ? -58.039  -3.694  -64.324  1.00 29.78  ? 492 TRP A N   1 
ATOM   3925  C CA  . TRP A  1 492 ? -58.487  -3.143  -63.063  1.00 30.21  ? 492 TRP A CA  1 
ATOM   3926  C C   . TRP A  1 492 ? -59.966  -2.781  -63.176  1.00 31.37  ? 492 TRP A C   1 
ATOM   3927  O O   . TRP A  1 492 ? -60.701  -2.833  -62.182  1.00 33.79  ? 492 TRP A O   1 
ATOM   3928  C CB  . TRP A  1 492 ? -57.617  -1.938  -62.697  1.00 30.36  ? 492 TRP A CB  1 
ATOM   3929  C CG  . TRP A  1 492 ? -56.140  -2.168  -62.905  1.00 30.20  ? 492 TRP A CG  1 
ATOM   3930  C CD1 . TRP A  1 492 ? -55.329  -1.399  -63.688  1.00 30.90  ? 492 TRP A CD1 1 
ATOM   3931  C CD2 . TRP A  1 492 ? -55.293  -3.194  -62.355  1.00 31.69  ? 492 TRP A CD2 1 
ATOM   3932  N NE1 . TRP A  1 492 ? -54.046  -1.862  -63.668  1.00 31.57  ? 492 TRP A NE1 1 
ATOM   3933  C CE2 . TRP A  1 492 ? -53.991  -2.966  -62.856  1.00 32.46  ? 492 TRP A CE2 1 
ATOM   3934  C CE3 . TRP A  1 492 ? -55.494  -4.288  -61.510  1.00 34.18  ? 492 TRP A CE3 1 
ATOM   3935  C CZ2 . TRP A  1 492 ? -52.908  -3.775  -62.528  1.00 32.44  ? 492 TRP A CZ2 1 
ATOM   3936  C CZ3 . TRP A  1 492 ? -54.424  -5.105  -61.205  1.00 34.50  ? 492 TRP A CZ3 1 
ATOM   3937  C CH2 . TRP A  1 492 ? -53.140  -4.825  -61.676  1.00 33.91  ? 492 TRP A CH2 1 
ATOM   3938  N N   . VAL A  1 493 ? -60.403  -2.440  -64.396  1.00 29.85  ? 493 VAL A N   1 
ATOM   3939  C CA  . VAL A  1 493 ? -61.798  -2.110  -64.640  1.00 29.84  ? 493 VAL A CA  1 
ATOM   3940  C C   . VAL A  1 493 ? -62.164  -2.590  -66.040  1.00 28.52  ? 493 VAL A C   1 
ATOM   3941  O O   . VAL A  1 493 ? -61.299  -2.608  -66.912  1.00 27.12  ? 493 VAL A O   1 
ATOM   3942  C CB  . VAL A  1 493 ? -62.137  -0.615  -64.482  1.00 29.48  ? 493 VAL A CB  1 
ATOM   3943  C CG1 . VAL A  1 493 ? -61.155  0.275   -65.247  1.00 28.17  ? 493 VAL A CG1 1 
ATOM   3944  C CG2 . VAL A  1 493 ? -63.586  -0.316  -64.880  1.00 28.81  ? 493 VAL A CG2 1 
ATOM   3945  N N   . VAL A  1 494 ? -63.436  -2.991  -66.213  1.00 28.60  ? 494 VAL A N   1 
ATOM   3946  C CA  . VAL A  1 494 ? -63.949  -3.360  -67.521  1.00 28.49  ? 494 VAL A CA  1 
ATOM   3947  C C   . VAL A  1 494 ? -65.300  -2.698  -67.758  1.00 27.13  ? 494 VAL A C   1 
ATOM   3948  O O   . VAL A  1 494 ? -66.153  -2.650  -66.885  1.00 27.67  ? 494 VAL A O   1 
ATOM   3949  C CB  . VAL A  1 494 ? -64.052  -4.895  -67.674  1.00 29.29  ? 494 VAL A CB  1 
ATOM   3950  C CG1 . VAL A  1 494 ? -65.066  -5.522  -66.742  1.00 29.51  ? 494 VAL A CG1 1 
ATOM   3951  C CG2 . VAL A  1 494 ? -64.398  -5.277  -69.096  1.00 29.70  ? 494 VAL A CG2 1 
ATOM   3952  N N   . ASN A  1 495 ? -65.501  -2.279  -68.997  1.00 28.10  ? 495 ASN A N   1 
ATOM   3953  C CA  . ASN A  1 495 ? -66.798  -1.907  -69.529  1.00 27.33  ? 495 ASN A CA  1 
ATOM   3954  C C   . ASN A  1 495 ? -67.263  -3.053  -70.412  1.00 27.62  ? 495 ASN A C   1 
ATOM   3955  O O   . ASN A  1 495 ? -66.791  -3.219  -71.535  1.00 27.38  ? 495 ASN A O   1 
ATOM   3956  C CB  . ASN A  1 495 ? -66.755  -0.599  -70.317  1.00 26.01  ? 495 ASN A CB  1 
ATOM   3957  C CG  . ASN A  1 495 ? -68.138  -0.214  -70.801  1.00 27.60  ? 495 ASN A CG  1 
ATOM   3958  O OD1 . ASN A  1 495 ? -68.912  -1.106  -71.230  1.00 29.62  ? 495 ASN A OD1 1 
ATOM   3959  N ND2 . ASN A  1 495 ? -68.472  1.081   -70.743  1.00 25.63  ? 495 ASN A ND2 1 
ATOM   3960  N N   . ALA A  1 496 ? -68.219  -3.819  -69.897  1.00 29.24  ? 496 ALA A N   1 
ATOM   3961  C CA  . ALA A  1 496 ? -68.839  -4.898  -70.649  1.00 29.04  ? 496 ALA A CA  1 
ATOM   3962  C C   . ALA A  1 496 ? -70.143  -4.405  -71.255  1.00 27.39  ? 496 ALA A C   1 
ATOM   3963  O O   . ALA A  1 496 ? -70.982  -3.929  -70.495  1.00 26.88  ? 496 ALA A O   1 
ATOM   3964  C CB  . ALA A  1 496 ? -69.116  -6.037  -69.724  1.00 30.62  ? 496 ALA A CB  1 
ATOM   3965  N N   . SER A  1 497 ? -70.281  -4.509  -72.591  1.00 25.89  ? 497 SER A N   1 
ATOM   3966  C CA  . SER A  1 497 ? -71.456  -3.998  -73.274  1.00 26.59  ? 497 SER A CA  1 
ATOM   3967  C C   . SER A  1 497 ? -71.892  -4.891  -74.439  1.00 26.93  ? 497 SER A C   1 
ATOM   3968  O O   . SER A  1 497 ? -71.166  -5.767  -74.929  1.00 25.86  ? 497 SER A O   1 
ATOM   3969  C CB  . SER A  1 497 ? -71.239  -2.572  -73.727  1.00 26.48  ? 497 SER A CB  1 
ATOM   3970  O OG  . SER A  1 497 ? -70.440  -2.526  -74.903  1.00 26.90  ? 497 SER A OG  1 
ATOM   3971  N N   . ALA A  1 498 ? -73.130  -4.657  -74.875  1.00 27.12  ? 498 ALA A N   1 
ATOM   3972  C CA  . ALA A  1 498 ? -73.667  -5.367  -76.026  1.00 28.55  ? 498 ALA A CA  1 
ATOM   3973  C C   . ALA A  1 498 ? -74.754  -4.517  -76.666  1.00 29.52  ? 498 ALA A C   1 
ATOM   3974  O O   . ALA A  1 498 ? -75.389  -3.704  -75.994  1.00 29.20  ? 498 ALA A O   1 
ATOM   3975  C CB  . ALA A  1 498 ? -74.199  -6.728  -75.612  1.00 29.19  ? 498 ALA A CB  1 
ATOM   3976  N N   . GLY A  1 499 ? -74.960  -4.716  -77.963  1.00 29.12  ? 499 GLY A N   1 
ATOM   3977  C CA  . GLY A  1 499 ? -75.919  -3.880  -78.641  1.00 29.25  ? 499 GLY A CA  1 
ATOM   3978  C C   . GLY A  1 499 ? -76.191  -4.356  -80.047  1.00 28.37  ? 499 GLY A C   1 
ATOM   3979  O O   . GLY A  1 499 ? -75.388  -5.049  -80.613  1.00 28.35  ? 499 GLY A O   1 
ATOM   3980  N N   . ILE A  1 500 ? -77.362  -3.997  -80.561  1.00 29.36  ? 500 ILE A N   1 
ATOM   3981  C CA  . ILE A  1 500 ? -77.751  -4.352  -81.908  1.00 29.56  ? 500 ILE A CA  1 
ATOM   3982  C C   . ILE A  1 500 ? -78.502  -3.173  -82.519  1.00 30.10  ? 500 ILE A C   1 
ATOM   3983  O O   . ILE A  1 500 ? -79.127  -2.391  -81.807  1.00 31.42  ? 500 ILE A O   1 
ATOM   3984  C CB  . ILE A  1 500 ? -78.573  -5.655  -81.893  1.00 31.01  ? 500 ILE A CB  1 
ATOM   3985  C CG1 . ILE A  1 500 ? -78.675  -6.271  -83.278  1.00 31.84  ? 500 ILE A CG1 1 
ATOM   3986  C CG2 . ILE A  1 500 ? -79.955  -5.487  -81.257  1.00 32.27  ? 500 ILE A CG2 1 
ATOM   3987  C CD1 . ILE A  1 500 ? -79.468  -7.553  -83.274  1.00 32.13  ? 500 ILE A CD1 1 
ATOM   3988  N N   . SER A  1 501 ? -78.427  -3.061  -83.843  1.00 30.71  ? 501 SER A N   1 
ATOM   3989  C CA  . SER A  1 501 ? -79.170  -2.062  -84.597  1.00 31.13  ? 501 SER A CA  1 
ATOM   3990  C C   . SER A  1 501 ? -80.619  -2.517  -84.831  1.00 33.11  ? 501 SER A C   1 
ATOM   3991  O O   . SER A  1 501 ? -80.889  -3.719  -85.017  1.00 32.53  ? 501 SER A O   1 
ATOM   3992  C CB  . SER A  1 501 ? -78.459  -1.763  -85.881  1.00 29.72  ? 501 SER A CB  1 
ATOM   3993  O OG  . SER A  1 501 ? -77.295  -1.025  -85.571  1.00 30.57  ? 501 SER A OG  1 
ATOM   3994  N N   . VAL A  1 502 ? -81.527  -1.548  -84.691  1.00 32.23  ? 502 VAL A N   1 
ATOM   3995  C CA  . VAL A  1 502 ? -82.985  -1.794  -84.821  1.00 33.36  ? 502 VAL A CA  1 
ATOM   3996  C C   . VAL A  1 502 ? -83.555  -0.767  -85.808  1.00 35.52  ? 502 VAL A C   1 
ATOM   3997  O O   . VAL A  1 502 ? -82.971  0.315   -85.937  1.00 34.57  ? 502 VAL A O   1 
ATOM   3998  C CB  . VAL A  1 502 ? -83.641  -1.650  -83.439  1.00 34.01  ? 502 VAL A CB  1 
ATOM   3999  C CG1 . VAL A  1 502 ? -85.112  -2.044  -83.451  1.00 34.87  ? 502 VAL A CG1 1 
ATOM   4000  C CG2 . VAL A  1 502 ? -82.886  -2.408  -82.358  1.00 33.31  ? 502 VAL A CG2 1 
ATOM   4001  N N   . ARG A  1 503 ? -84.652  -1.109  -86.477  1.00 37.66  ? 503 ARG A N   1 
ATOM   4002  C CA  . ARG A  1 503 ? -85.261  -0.204  -87.477  1.00 38.90  ? 503 ARG A CA  1 
ATOM   4003  C C   . ARG A  1 503 ? -86.788  -0.141  -87.339  1.00 38.83  ? 503 ARG A C   1 
ATOM   4004  O O   . ARG A  1 503 ? -87.397  -1.189  -87.092  1.00 41.52  ? 503 ARG A O   1 
ATOM   4005  C CB  . ARG A  1 503 ? -84.906  -0.662  -88.891  1.00 42.17  ? 503 ARG A CB  1 
ATOM   4006  C CG  . ARG A  1 503 ? -85.084  0.388   -89.973  1.00 49.22  ? 503 ARG A CG  1 
ATOM   4007  C CD  . ARG A  1 503 ? -85.369  -0.283  -91.299  1.00 54.25  ? 503 ARG A CD  1 
ATOM   4008  N NE  . ARG A  1 503 ? -84.201  -0.304  -92.183  1.00 61.79  ? 503 ARG A NE  1 
ATOM   4009  C CZ  . ARG A  1 503 ? -83.384  0.719   -92.381  1.00 70.79  ? 503 ARG A CZ  1 
ATOM   4010  N NH1 . ARG A  1 503 ? -83.872  1.912   -92.671  1.00 76.48  ? 503 ARG A NH1 1 
ATOM   4011  N NH2 . ARG A  1 503 ? -82.078  0.542   -92.298  1.00 65.29  ? 503 ARG A NH2 1 
ATOM   4012  N N   . TYR A  1 504 ? -87.365  1.051   -87.467  1.00 36.15  ? 504 TYR A N   1 
ATOM   4013  C CA  . TYR A  1 504 ? -88.835  1.246   -87.495  1.00 35.36  ? 504 TYR A CA  1 
ATOM   4014  C C   . TYR A  1 504 ? -89.049  2.223   -88.633  1.00 35.19  ? 504 TYR A C   1 
ATOM   4015  O O   . TYR A  1 504 ? -88.747  3.411   -88.462  1.00 34.98  ? 504 TYR A O   1 
ATOM   4016  C CB  . TYR A  1 504 ? -89.431  1.747   -86.179  1.00 36.55  ? 504 TYR A CB  1 
ATOM   4017  C CG  . TYR A  1 504 ? -90.946  1.650   -86.106  1.00 38.01  ? 504 TYR A CG  1 
ATOM   4018  C CD1 . TYR A  1 504 ? -91.756  2.603   -86.710  1.00 39.31  ? 504 TYR A CD1 1 
ATOM   4019  C CD2 . TYR A  1 504 ? -91.563  0.598   -85.446  1.00 39.81  ? 504 TYR A CD2 1 
ATOM   4020  C CE1 . TYR A  1 504 ? -93.134  2.512   -86.657  1.00 38.66  ? 504 TYR A CE1 1 
ATOM   4021  C CE2 . TYR A  1 504 ? -92.940  0.497   -85.384  1.00 39.73  ? 504 TYR A CE2 1 
ATOM   4022  C CZ  . TYR A  1 504 ? -93.727  1.456   -85.992  1.00 39.72  ? 504 TYR A CZ  1 
ATOM   4023  O OH  . TYR A  1 504 ? -95.084  1.361   -85.933  1.00 43.06  ? 504 TYR A OH  1 
ATOM   4024  N N   . GLY A  1 505 ? -89.562  1.748   -89.760  1.00 32.69  ? 505 GLY A N   1 
ATOM   4025  C CA  . GLY A  1 505 ? -89.651  2.591   -90.938  1.00 32.49  ? 505 GLY A CA  1 
ATOM   4026  C C   . GLY A  1 505 ? -88.246  3.048   -91.322  1.00 32.17  ? 505 GLY A C   1 
ATOM   4027  O O   . GLY A  1 505 ? -87.393  2.220   -91.581  1.00 32.09  ? 505 GLY A O   1 
ATOM   4028  N N   . LYS A  1 506 ? -87.988  4.360   -91.319  1.00 32.50  ? 506 LYS A N   1 
ATOM   4029  C CA  . LYS A  1 506 ? -86.686  4.889   -91.685  1.00 31.10  ? 506 LYS A CA  1 
ATOM   4030  C C   . LYS A  1 506 ? -85.873  5.263   -90.447  1.00 31.56  ? 506 LYS A C   1 
ATOM   4031  O O   . LYS A  1 506 ? -84.738  5.691   -90.555  1.00 34.43  ? 506 LYS A O   1 
ATOM   4032  C CB  . LYS A  1 506 ? -86.883  6.137   -92.543  1.00 32.52  ? 506 LYS A CB  1 
ATOM   4033  C CG  . LYS A  1 506 ? -87.740  6.009   -93.797  1.00 34.09  ? 506 LYS A CG  1 
ATOM   4034  C CD  . LYS A  1 506 ? -87.677  7.308   -94.585  1.00 35.39  ? 506 LYS A CD  1 
ATOM   4035  C CE  . LYS A  1 506 ? -88.657  7.459   -95.694  1.00 36.26  ? 506 LYS A CE  1 
ATOM   4036  N NZ  . LYS A  1 506 ? -88.649  8.830   -96.204  1.00 37.04  ? 506 LYS A NZ  1 
ATOM   4037  N N   . PHE A  1 507 ? -86.469  5.137   -89.264  1.00 33.58  ? 507 PHE A N   1 
ATOM   4038  C CA  . PHE A  1 507 ? -85.796  5.376   -87.996  1.00 32.97  ? 507 PHE A CA  1 
ATOM   4039  C C   . PHE A  1 507 ? -84.952  4.160   -87.579  1.00 32.91  ? 507 PHE A C   1 
ATOM   4040  O O   . PHE A  1 507 ? -85.504  3.090   -87.264  1.00 32.40  ? 507 PHE A O   1 
ATOM   4041  C CB  . PHE A  1 507 ? -86.911  5.682   -86.983  1.00 31.80  ? 507 PHE A CB  1 
ATOM   4042  C CG  . PHE A  1 507 ? -86.423  6.147   -85.617  1.00 30.56  ? 507 PHE A CG  1 
ATOM   4043  C CD1 . PHE A  1 507 ? -86.109  5.222   -84.625  1.00 29.15  ? 507 PHE A CD1 1 
ATOM   4044  C CD2 . PHE A  1 507 ? -86.330  7.515   -85.313  1.00 29.97  ? 507 PHE A CD2 1 
ATOM   4045  C CE1 . PHE A  1 507 ? -85.712  5.647   -83.365  1.00 29.07  ? 507 PHE A CE1 1 
ATOM   4046  C CE2 . PHE A  1 507 ? -85.940  7.933   -84.048  1.00 29.39  ? 507 PHE A CE2 1 
ATOM   4047  C CZ  . PHE A  1 507 ? -85.625  7.002   -83.075  1.00 28.98  ? 507 PHE A CZ  1 
ATOM   4048  N N   . THR A  1 508 ? -83.624  4.347   -87.562  1.00 32.92  ? 508 THR A N   1 
ATOM   4049  C CA  . THR A  1 508 ? -82.662  3.333   -87.119  1.00 33.69  ? 508 THR A CA  1 
ATOM   4050  C C   . THR A  1 508 ? -81.957  3.809   -85.842  1.00 32.23  ? 508 THR A C   1 
ATOM   4051  O O   . THR A  1 508 ? -81.597  4.984   -85.702  1.00 30.66  ? 508 THR A O   1 
ATOM   4052  C CB  . THR A  1 508 ? -81.598  3.034   -88.180  1.00 34.34  ? 508 THR A CB  1 
ATOM   4053  O OG1 . THR A  1 508 ? -80.997  4.309   -88.369  1.00 37.96  ? 508 THR A OG1 1 
ATOM   4054  C CG2 . THR A  1 508 ? -82.129  2.554   -89.515  1.00 35.11  ? 508 THR A CG2 1 
ATOM   4055  N N   . PHE A  1 509 ? -81.735  2.865   -84.916  1.00 32.58  ? 509 PHE A N   1 
ATOM   4056  C CA  . PHE A  1 509 ? -81.165  3.183   -83.622  1.00 30.89  ? 509 PHE A CA  1 
ATOM   4057  C C   . PHE A  1 509 ? -80.543  1.923   -83.065  1.00 32.41  ? 509 PHE A C   1 
ATOM   4058  O O   . PHE A  1 509 ? -80.545  0.892   -83.713  1.00 33.38  ? 509 PHE A O   1 
ATOM   4059  C CB  . PHE A  1 509 ? -82.239  3.779   -82.708  1.00 31.51  ? 509 PHE A CB  1 
ATOM   4060  C CG  . PHE A  1 509 ? -83.418  2.899   -82.337  1.00 28.79  ? 509 PHE A CG  1 
ATOM   4061  C CD1 . PHE A  1 509 ? -84.391  2.574   -83.271  1.00 29.64  ? 509 PHE A CD1 1 
ATOM   4062  C CD2 . PHE A  1 509 ? -83.570  2.445   -81.039  1.00 28.48  ? 509 PHE A CD2 1 
ATOM   4063  C CE1 . PHE A  1 509 ? -85.468  1.767   -82.925  1.00 30.60  ? 509 PHE A CE1 1 
ATOM   4064  C CE2 . PHE A  1 509 ? -84.646  1.639   -80.699  1.00 30.44  ? 509 PHE A CE2 1 
ATOM   4065  C CZ  . PHE A  1 509 ? -85.589  1.289   -81.644  1.00 30.60  ? 509 PHE A CZ  1 
ATOM   4066  N N   . LYS A  1 510 ? -79.997  2.014   -81.861  1.00 34.88  ? 510 LYS A N   1 
ATOM   4067  C CA  . LYS A  1 510 ? -79.412  0.841   -81.236  1.00 33.94  ? 510 LYS A CA  1 
ATOM   4068  C C   . LYS A  1 510 ? -80.052  0.619   -79.869  1.00 32.14  ? 510 LYS A C   1 
ATOM   4069  O O   . LYS A  1 510 ? -80.488  1.568   -79.198  1.00 30.32  ? 510 LYS A O   1 
ATOM   4070  C CB  . LYS A  1 510 ? -77.897  0.987   -81.109  1.00 35.85  ? 510 LYS A CB  1 
ATOM   4071  C CG  . LYS A  1 510 ? -77.133  0.794   -82.395  1.00 40.51  ? 510 LYS A CG  1 
ATOM   4072  C CD  . LYS A  1 510 ? -75.623  0.869   -82.190  1.00 43.73  ? 510 LYS A CD  1 
ATOM   4073  C CE  . LYS A  1 510 ? -74.847  0.825   -83.461  1.00 47.46  ? 510 LYS A CE  1 
ATOM   4074  N NZ  . LYS A  1 510 ? -75.051  -0.497  -84.036  1.00 50.06  ? 510 LYS A NZ  1 
ATOM   4075  N N   . ILE A  1 511 ? -80.128  -0.665  -79.502  1.00 28.04  ? 511 ILE A N   1 
ATOM   4076  C CA  . ILE A  1 511 ? -80.493  -1.076  -78.166  1.00 28.01  ? 511 ILE A CA  1 
ATOM   4077  C C   . ILE A  1 511 ? -79.275  -1.808  -77.621  1.00 27.42  ? 511 ILE A C   1 
ATOM   4078  O O   . ILE A  1 511 ? -78.537  -2.430  -78.380  1.00 26.74  ? 511 ILE A O   1 
ATOM   4079  C CB  . ILE A  1 511 ? -81.785  -1.931  -78.184  1.00 29.81  ? 511 ILE A CB  1 
ATOM   4080  C CG1 . ILE A  1 511 ? -81.636  -3.212  -79.021  1.00 29.46  ? 511 ILE A CG1 1 
ATOM   4081  C CG2 . ILE A  1 511 ? -82.970  -1.086  -78.663  1.00 29.78  ? 511 ILE A CG2 1 
ATOM   4082  C CD1 . ILE A  1 511 ? -82.836  -4.123  -78.953  1.00 31.61  ? 511 ILE A CD1 1 
ATOM   4083  N N   . HIS A  1 512 ? -79.059  -1.715  -76.312  1.00 27.70  ? 512 HIS A N   1 
ATOM   4084  C CA  . HIS A  1 512 ? -77.744  -1.958  -75.756  1.00 28.08  ? 512 HIS A CA  1 
ATOM   4085  C C   . HIS A  1 512 ? -77.855  -1.930  -74.239  1.00 28.28  ? 512 HIS A C   1 
ATOM   4086  O O   . HIS A  1 512 ? -78.839  -1.435  -73.710  1.00 28.36  ? 512 HIS A O   1 
ATOM   4087  C CB  . HIS A  1 512 ? -76.756  -0.885  -76.265  1.00 27.89  ? 512 HIS A CB  1 
ATOM   4088  C CG  . HIS A  1 512 ? -77.338  0.495   -76.178  1.00 29.26  ? 512 HIS A CG  1 
ATOM   4089  N ND1 . HIS A  1 512 ? -77.582  1.138   -74.979  1.00 28.56  ? 512 HIS A ND1 1 
ATOM   4090  C CD2 . HIS A  1 512 ? -77.841  1.290   -77.131  1.00 30.41  ? 512 HIS A CD2 1 
ATOM   4091  C CE1 . HIS A  1 512 ? -78.166  2.302   -75.221  1.00 29.56  ? 512 HIS A CE1 1 
ATOM   4092  N NE2 . HIS A  1 512 ? -78.323  2.425   -76.524  1.00 30.26  ? 512 HIS A NE2 1 
ATOM   4093  N N   . ASP A  1 513 ? -76.831  -2.461  -73.567  1.00 28.79  ? 513 ASP A N   1 
ATOM   4094  C CA  . ASP A  1 513 ? -76.700  -2.395  -72.121  1.00 29.08  ? 513 ASP A CA  1 
ATOM   4095  C C   . ASP A  1 513 ? -75.213  -2.414  -71.793  1.00 29.36  ? 513 ASP A C   1 
ATOM   4096  O O   . ASP A  1 513 ? -74.370  -2.784  -72.617  1.00 28.44  ? 513 ASP A O   1 
ATOM   4097  C CB  . ASP A  1 513 ? -77.420  -3.558  -71.464  1.00 30.96  ? 513 ASP A CB  1 
ATOM   4098  C CG  . ASP A  1 513 ? -77.743  -3.436  -69.985  1.00 31.87  ? 513 ASP A CG  1 
ATOM   4099  O OD1 . ASP A  1 513 ? -77.584  -2.339  -69.416  1.00 29.30  ? 513 ASP A OD1 1 
ATOM   4100  O OD2 . ASP A  1 513 ? -78.193  -4.462  -69.423  1.00 35.75  ? 513 ASP A OD2 1 
ATOM   4101  N N   . GLN A  1 514 ? -74.903  -2.044  -70.554  1.00 31.01  ? 514 GLN A N   1 
ATOM   4102  C CA  . GLN A  1 514 ? -73.549  -1.665  -70.207  1.00 30.70  ? 514 GLN A CA  1 
ATOM   4103  C C   . GLN A  1 514 ? -73.322  -1.952  -68.735  1.00 30.96  ? 514 GLN A C   1 
ATOM   4104  O O   . GLN A  1 514 ? -74.155  -1.601  -67.904  1.00 30.40  ? 514 GLN A O   1 
ATOM   4105  C CB  . GLN A  1 514 ? -73.336  -0.175  -70.493  1.00 29.06  ? 514 GLN A CB  1 
ATOM   4106  C CG  . GLN A  1 514 ? -71.949  0.348   -70.129  1.00 27.90  ? 514 GLN A CG  1 
ATOM   4107  C CD  . GLN A  1 514 ? -71.812  1.852   -70.323  1.00 26.38  ? 514 GLN A CD  1 
ATOM   4108  O OE1 . GLN A  1 514 ? -71.226  2.337   -71.286  1.00 25.18  ? 514 GLN A OE1 1 
ATOM   4109  N NE2 . GLN A  1 514 ? -72.328  2.624   -69.392  1.00 26.36  ? 514 GLN A NE2 1 
ATOM   4110  N N   . LYS A  1 515 ? -72.179  -2.586  -68.448  1.00 31.00  ? 515 LYS A N   1 
ATOM   4111  C CA  . LYS A  1 515 ? -71.748  -2.797  -67.082  1.00 31.41  ? 515 LYS A CA  1 
ATOM   4112  C C   . LYS A  1 515 ? -70.286  -2.353  -66.949  1.00 29.72  ? 515 LYS A C   1 
ATOM   4113  O O   . LYS A  1 515 ? -69.421  -2.701  -67.755  1.00 27.58  ? 515 LYS A O   1 
ATOM   4114  C CB  . LYS A  1 515 ? -71.963  -4.260  -66.676  1.00 32.37  ? 515 LYS A CB  1 
ATOM   4115  C CG  . LYS A  1 515 ? -73.363  -4.802  -66.870  1.00 34.95  ? 515 LYS A CG  1 
ATOM   4116  C CD  . LYS A  1 515 ? -74.428  -4.292  -65.891  1.00 35.66  ? 515 LYS A CD  1 
ATOM   4117  C CE  . LYS A  1 515 ? -75.814  -4.787  -66.243  1.00 36.54  ? 515 LYS A CE  1 
ATOM   4118  N NZ  . LYS A  1 515 ? -76.942  -4.084  -65.622  1.00 35.86  ? 515 LYS A NZ  1 
ATOM   4119  N N   . ILE A  1 516 ? -70.036  -1.594  -65.887  1.00 29.75  ? 516 ILE A N   1 
ATOM   4120  C CA  . ILE A  1 516 ? -68.708  -1.165  -65.533  1.00 30.23  ? 516 ILE A CA  1 
ATOM   4121  C C   . ILE A  1 516 ? -68.353  -1.920  -64.269  1.00 29.96  ? 516 ILE A C   1 
ATOM   4122  O O   . ILE A  1 516 ? -69.109  -1.895  -63.317  1.00 28.00  ? 516 ILE A O   1 
ATOM   4123  C CB  . ILE A  1 516 ? -68.665  0.357   -65.379  1.00 32.46  ? 516 ILE A CB  1 
ATOM   4124  C CG1 . ILE A  1 516 ? -69.079  1.027   -66.706  1.00 32.42  ? 516 ILE A CG1 1 
ATOM   4125  C CG2 . ILE A  1 516 ? -67.283  0.820   -64.900  1.00 33.91  ? 516 ILE A CG2 1 
ATOM   4126  C CD1 . ILE A  1 516 ? -69.078  2.557   -66.681  1.00 32.44  ? 516 ILE A CD1 1 
ATOM   4127  N N   . ILE A  1 517 ? -67.264  -2.705  -64.328  1.00 30.35  ? 517 ILE A N   1 
ATOM   4128  C CA  . ILE A  1 517 ? -67.001  -3.638  -63.256  1.00 30.67  ? 517 ILE A CA  1 
ATOM   4129  C C   . ILE A  1 517 ? -65.534  -3.553  -62.889  1.00 31.29  ? 517 ILE A C   1 
ATOM   4130  O O   . ILE A  1 517 ? -64.668  -3.670  -63.769  1.00 32.51  ? 517 ILE A O   1 
ATOM   4131  C CB  . ILE A  1 517 ? -67.401  -5.066  -63.658  1.00 30.05  ? 517 ILE A CB  1 
ATOM   4132  C CG1 . ILE A  1 517 ? -68.856  -5.191  -64.017  1.00 29.98  ? 517 ILE A CG1 1 
ATOM   4133  C CG2 . ILE A  1 517 ? -67.046  -6.038  -62.556  1.00 30.40  ? 517 ILE A CG2 1 
ATOM   4134  C CD1 . ILE A  1 517 ? -69.135  -6.481  -64.762  1.00 30.57  ? 517 ILE A CD1 1 
ATOM   4135  N N   . TYR A  1 518 ? -65.298  -3.441  -61.578  1.00 32.00  ? 518 TYR A N   1 
ATOM   4136  C CA  . TYR A  1 518 ? -63.962  -3.209  -61.048  1.00 32.79  ? 518 TYR A CA  1 
ATOM   4137  C C   . TYR A  1 518 ? -63.345  -4.467  -60.459  1.00 35.01  ? 518 TYR A C   1 
ATOM   4138  O O   . TYR A  1 518 ? -64.051  -5.331  -59.932  1.00 33.39  ? 518 TYR A O   1 
ATOM   4139  C CB  . TYR A  1 518 ? -64.046  -2.191  -59.916  1.00 32.86  ? 518 TYR A CB  1 
ATOM   4140  C CG  . TYR A  1 518 ? -64.583  -0.839  -60.356  1.00 32.17  ? 518 TYR A CG  1 
ATOM   4141  C CD1 . TYR A  1 518 ? -63.725  0.131   -60.862  1.00 30.46  ? 518 TYR A CD1 1 
ATOM   4142  C CD2 . TYR A  1 518 ? -65.941  -0.551  -60.257  1.00 32.20  ? 518 TYR A CD2 1 
ATOM   4143  C CE1 . TYR A  1 518 ? -64.206  1.366   -61.244  1.00 30.93  ? 518 TYR A CE1 1 
ATOM   4144  C CE2 . TYR A  1 518 ? -66.436  0.670   -60.676  1.00 32.98  ? 518 TYR A CE2 1 
ATOM   4145  C CZ  . TYR A  1 518 ? -65.561  1.640   -61.143  1.00 32.49  ? 518 TYR A CZ  1 
ATOM   4146  O OH  . TYR A  1 518 ? -66.036  2.863   -61.528  1.00 32.77  ? 518 TYR A OH  1 
ATOM   4147  N N   . ARG A  1 519 ? -62.020  -4.514  -60.537  1.00 37.35  ? 519 ARG A N   1 
ATOM   4148  C CA  . ARG A  1 519 ? -61.300  -5.631  -59.898  1.00 39.90  ? 519 ARG A CA  1 
ATOM   4149  C C   . ARG A  1 519 ? -61.519  -5.484  -58.398  1.00 45.31  ? 519 ARG A C   1 
ATOM   4150  O O   . ARG A  1 519 ? -62.526  -5.932  -57.904  1.00 50.29  ? 519 ARG A O   1 
ATOM   4151  C CB  . ARG A  1 519 ? -59.806  -5.669  -60.212  1.00 37.58  ? 519 ARG A CB  1 
ATOM   4152  C CG  . ARG A  1 519 ? -59.160  -6.953  -59.718  1.00 36.61  ? 519 ARG A CG  1 
ATOM   4153  C CD  . ARG A  1 519 ? -57.726  -7.119  -60.178  1.00 35.82  ? 519 ARG A CD  1 
ATOM   4154  N NE  . ARG A  1 519 ? -57.610  -7.591  -61.561  1.00 34.43  ? 519 ARG A NE  1 
ATOM   4155  C CZ  . ARG A  1 519 ? -58.061  -8.745  -62.029  1.00 34.06  ? 519 ARG A CZ  1 
ATOM   4156  N NH1 . ARG A  1 519 ? -58.410  -9.712  -61.203  1.00 34.26  ? 519 ARG A NH1 1 
ATOM   4157  N NH2 . ARG A  1 519 ? -58.153  -8.928  -63.330  1.00 34.33  ? 519 ARG A NH2 1 
ATOM   4158  N N   . GLY A  1 520 ? -60.682  -4.750  -57.698  1.00 49.33  ? 520 GLY A N   1 
ATOM   4159  C CA  . GLY A  1 520 ? -60.927  -4.760  -56.247  1.00 54.69  ? 520 GLY A CA  1 
ATOM   4160  C C   . GLY A  1 520 ? -61.654  -3.550  -55.735  1.00 49.66  ? 520 GLY A C   1 
ATOM   4161  O O   . GLY A  1 520 ? -62.724  -3.225  -56.268  1.00 43.86  ? 520 GLY A O   1 
ATOM   4162  N N   . ASP A  1 521 ? -61.118  -2.966  -54.675  1.00 50.10  ? 521 ASP A N   1 
ATOM   4163  C CA  . ASP A  1 521 ? -61.679  -1.719  -54.112  1.00 50.88  ? 521 ASP A CA  1 
ATOM   4164  C C   . ASP A  1 521 ? -60.695  -0.607  -54.469  1.00 45.30  ? 521 ASP A C   1 
ATOM   4165  O O   . ASP A  1 521 ? -60.580  0.340   -53.694  1.00 51.22  ? 521 ASP A O   1 
ATOM   4166  C CB  . ASP A  1 521 ? -61.914  -1.884  -52.623  1.00 54.94  ? 521 ASP A CB  1 
ATOM   4167  C CG  . ASP A  1 521 ? -60.669  -2.098  -51.773  1.00 61.66  ? 521 ASP A CG  1 
ATOM   4168  O OD1 . ASP A  1 521 ? -59.642  -2.544  -52.324  1.00 58.69  ? 521 ASP A OD1 1 
ATOM   4169  O OD2 . ASP A  1 521 ? -60.736  -1.813  -50.562  1.00 68.93  ? 521 ASP A OD2 1 
ATOM   4170  N N   . TRP A  1 522 ? -60.016  -0.730  -55.603  1.00 39.99  ? 522 TRP A N   1 
ATOM   4171  C CA  . TRP A  1 522 ? -58.984  0.243   -55.930  1.00 39.60  ? 522 TRP A CA  1 
ATOM   4172  C C   . TRP A  1 522 ? -59.628  1.590   -56.270  1.00 39.96  ? 522 TRP A C   1 
ATOM   4173  O O   . TRP A  1 522 ? -59.025  2.645   -56.087  1.00 41.79  ? 522 TRP A O   1 
ATOM   4174  C CB  . TRP A  1 522 ? -58.068  -0.226  -57.076  1.00 38.71  ? 522 TRP A CB  1 
ATOM   4175  C CG  . TRP A  1 522 ? -58.695  -0.125  -58.443  1.00 39.34  ? 522 TRP A CG  1 
ATOM   4176  C CD1 . TRP A  1 522 ? -59.481  -1.072  -59.019  1.00 39.84  ? 522 TRP A CD1 1 
ATOM   4177  C CD2 . TRP A  1 522 ? -58.654  0.973   -59.396  1.00 42.34  ? 522 TRP A CD2 1 
ATOM   4178  N NE1 . TRP A  1 522 ? -59.927  -0.660  -60.244  1.00 39.63  ? 522 TRP A NE1 1 
ATOM   4179  C CE2 . TRP A  1 522 ? -59.437  0.586   -60.510  1.00 40.32  ? 522 TRP A CE2 1 
ATOM   4180  C CE3 . TRP A  1 522 ? -58.037  2.234   -59.434  1.00 41.76  ? 522 TRP A CE3 1 
ATOM   4181  C CZ2 . TRP A  1 522 ? -59.616  1.404   -61.626  1.00 39.86  ? 522 TRP A CZ2 1 
ATOM   4182  C CZ3 . TRP A  1 522 ? -58.200  3.039   -60.548  1.00 39.48  ? 522 TRP A CZ3 1 
ATOM   4183  C CH2 . TRP A  1 522 ? -58.989  2.632   -61.623  1.00 40.42  ? 522 TRP A CH2 1 
ATOM   4184  N N   . ALA A  1 523 ? -60.857  1.536   -56.770  1.00 39.27  ? 523 ALA A N   1 
ATOM   4185  C CA  . ALA A  1 523 ? -61.545  2.691   -57.295  1.00 40.26  ? 523 ALA A CA  1 
ATOM   4186  C C   . ALA A  1 523 ? -62.614  3.179   -56.325  1.00 42.78  ? 523 ALA A C   1 
ATOM   4187  O O   . ALA A  1 523 ? -63.527  3.903   -56.720  1.00 42.31  ? 523 ALA A O   1 
ATOM   4188  C CB  . ALA A  1 523 ? -62.155  2.332   -58.614  1.00 41.14  ? 523 ALA A CB  1 
ATOM   4189  N N   . LYS A  1 524 ? -62.478  2.815   -55.045  1.00 45.27  ? 524 LYS A N   1 
ATOM   4190  C CA  . LYS A  1 524 ? -63.341  3.370   -54.011  1.00 46.50  ? 524 LYS A CA  1 
ATOM   4191  C C   . LYS A  1 524 ? -63.411  4.899   -54.143  1.00 44.09  ? 524 LYS A C   1 
ATOM   4192  O O   . LYS A  1 524 ? -64.508  5.454   -54.078  1.00 39.66  ? 524 LYS A O   1 
ATOM   4193  C CB  . LYS A  1 524 ? -62.835  2.953   -52.631  1.00 49.29  ? 524 LYS A CB  1 
ATOM   4194  C CG  . LYS A  1 524 ? -63.784  3.351   -51.524  1.00 57.80  ? 524 LYS A CG  1 
ATOM   4195  C CD  . LYS A  1 524 ? -63.255  3.094   -50.113  1.00 63.64  ? 524 LYS A CD  1 
ATOM   4196  C CE  . LYS A  1 524 ? -64.371  3.142   -49.111  1.00 65.76  ? 524 LYS A CE  1 
ATOM   4197  N NZ  . LYS A  1 524 ? -63.863  2.805   -47.779  1.00 67.06  ? 524 LYS A NZ  1 
ATOM   4198  N N   . GLU A  1 525 ? -62.254  5.573   -54.343  1.00 40.72  ? 525 GLU A N   1 
ATOM   4199  C CA  . GLU A  1 525 ? -62.267  7.036   -54.394  1.00 41.30  ? 525 GLU A CA  1 
ATOM   4200  C C   . GLU A  1 525 ? -62.606  7.523   -55.812  1.00 37.49  ? 525 GLU A C   1 
ATOM   4201  O O   . GLU A  1 525 ? -63.514  8.321   -55.991  1.00 37.31  ? 525 GLU A O   1 
ATOM   4202  C CB  . GLU A  1 525 ? -61.003  7.731   -53.860  1.00 40.46  ? 525 GLU A CB  1 
ATOM   4203  C CG  . GLU A  1 525 ? -60.639  7.376   -52.423  1.00 41.15  ? 525 GLU A CG  1 
ATOM   4204  C CD  . GLU A  1 525 ? -59.887  6.052   -52.276  1.00 43.77  ? 525 GLU A CD  1 
ATOM   4205  O OE1 . GLU A  1 525 ? -59.274  5.535   -53.260  1.00 40.00  ? 525 GLU A OE1 1 
ATOM   4206  O OE2 . GLU A  1 525 ? -59.943  5.529   -51.137  1.00 44.38  ? 525 GLU A OE2 1 
ATOM   4207  N N   . VAL A  1 526 ? -61.895  7.040   -56.833  1.00 35.91  ? 526 VAL A N   1 
ATOM   4208  C CA  . VAL A  1 526 ? -61.949  7.658   -58.151  1.00 35.29  ? 526 VAL A CA  1 
ATOM   4209  C C   . VAL A  1 526 ? -63.148  7.179   -58.976  1.00 34.23  ? 526 VAL A C   1 
ATOM   4210  O O   . VAL A  1 526 ? -63.563  7.873   -59.899  1.00 32.23  ? 526 VAL A O   1 
ATOM   4211  C CB  . VAL A  1 526 ? -60.616  7.440   -58.900  1.00 36.08  ? 526 VAL A CB  1 
ATOM   4212  C CG1 . VAL A  1 526 ? -60.291  5.972   -59.094  1.00 37.03  ? 526 VAL A CG1 1 
ATOM   4213  C CG2 . VAL A  1 526 ? -60.571  8.168   -60.240  1.00 34.70  ? 526 VAL A CG2 1 
ATOM   4214  N N   . GLY A  1 527 ? -63.670  5.977   -58.690  1.00 34.66  ? 527 GLY A N   1 
ATOM   4215  C CA  . GLY A  1 527 ? -64.758  5.414   -59.475  1.00 33.42  ? 527 GLY A CA  1 
ATOM   4216  C C   . GLY A  1 527 ? -66.063  6.153   -59.200  1.00 34.11  ? 527 GLY A C   1 
ATOM   4217  O O   . GLY A  1 527 ? -66.261  6.638   -58.098  1.00 34.48  ? 527 GLY A O   1 
ATOM   4218  N N   . ARG A  1 528 ? -66.946  6.204   -60.203  1.00 36.58  ? 528 ARG A N   1 
ATOM   4219  C CA  . ARG A  1 528 ? -68.236  6.873   -60.100  1.00 41.40  ? 528 ARG A CA  1 
ATOM   4220  C C   . ARG A  1 528 ? -69.096  6.214   -59.034  1.00 45.64  ? 528 ARG A C   1 
ATOM   4221  O O   . ARG A  1 528 ? -69.249  4.989   -59.071  1.00 44.40  ? 528 ARG A O   1 
ATOM   4222  C CB  . ARG A  1 528 ? -69.067  6.729   -61.382  1.00 41.94  ? 528 ARG A CB  1 
ATOM   4223  C CG  . ARG A  1 528 ? -70.437  7.398   -61.336  1.00 41.57  ? 528 ARG A CG  1 
ATOM   4224  C CD  . ARG A  1 528 ? -71.197  7.170   -62.641  1.00 40.54  ? 528 ARG A CD  1 
ATOM   4225  N NE  . ARG A  1 528 ? -70.613  7.884   -63.779  1.00 38.07  ? 528 ARG A NE  1 
ATOM   4226  C CZ  . ARG A  1 528 ? -69.875  7.342   -64.730  1.00 36.97  ? 528 ARG A CZ  1 
ATOM   4227  N NH1 . ARG A  1 528 ? -69.611  6.054   -64.715  1.00 38.06  ? 528 ARG A NH1 1 
ATOM   4228  N NH2 . ARG A  1 528 ? -69.367  8.100   -65.688  1.00 37.21  ? 528 ARG A NH2 1 
ATOM   4229  N N   . LYS A  1 529 ? -69.680  7.031   -58.142  1.00 51.69  ? 529 LYS A N   1 
ATOM   4230  C CA  . LYS A  1 529 ? -70.664  6.518   -57.197  1.00 62.15  ? 529 LYS A CA  1 
ATOM   4231  C C   . LYS A  1 529 ? -72.043  6.899   -57.702  1.00 57.69  ? 529 LYS A C   1 
ATOM   4232  O O   . LYS A  1 529 ? -72.246  8.025   -58.140  1.00 58.99  ? 529 LYS A O   1 
ATOM   4233  C CB  . LYS A  1 529 ? -70.498  6.977   -55.746  1.00 72.43  ? 529 LYS A CB  1 
ATOM   4234  C CG  . LYS A  1 529 ? -69.360  6.302   -54.982  1.00 82.33  ? 529 LYS A CG  1 
ATOM   4235  C CD  . LYS A  1 529 ? -68.001  6.950   -55.252  1.00 89.92  ? 529 LYS A CD  1 
ATOM   4236  C CE  . LYS A  1 529 ? -67.848  8.349   -54.704  1.00 87.69  ? 529 LYS A CE  1 
ATOM   4237  N NZ  . LYS A  1 529 ? -66.558  8.944   -55.059  1.00 85.24  ? 529 LYS A NZ  1 
ATOM   4238  N N   . LEU A  1 530 ? -72.958  5.937   -57.660  1.00 58.08  ? 530 LEU A N   1 
ATOM   4239  C CA  . LEU A  1 530 ? -74.306  6.130   -58.167  1.00 66.50  ? 530 LEU A CA  1 
ATOM   4240  C C   . LEU A  1 530 ? -75.242  6.590   -57.023  1.00 68.17  ? 530 LEU A C   1 
ATOM   4241  O O   . LEU A  1 530 ? -74.916  6.347   -55.828  1.00 63.30  ? 530 LEU A O   1 
ATOM   4242  C CB  . LEU A  1 530 ? -74.801  4.845   -58.843  1.00 69.92  ? 530 LEU A CB  1 
ATOM   4243  C CG  . LEU A  1 530 ? -74.288  4.522   -60.260  1.00 67.17  ? 530 LEU A CG  1 
ATOM   4244  C CD1 . LEU A  1 530 ? -74.525  5.720   -61.201  1.00 67.19  ? 530 LEU A CD1 1 
ATOM   4245  C CD2 . LEU A  1 530 ? -72.838  4.005   -60.303  1.00 58.42  ? 530 LEU A CD2 1 
ATOM   4246  N N   . LYS B  1 4   ? -25.050  22.665  -54.838  1.00 54.90  ? 4   LYS B N   1 
ATOM   4247  C CA  . LYS B  1 4   ? -24.460  21.304  -54.962  1.00 55.03  ? 4   LYS B CA  1 
ATOM   4248  C C   . LYS B  1 4   ? -25.328  20.412  -55.867  1.00 45.90  ? 4   LYS B C   1 
ATOM   4249  O O   . LYS B  1 4   ? -26.560  20.586  -55.885  1.00 42.63  ? 4   LYS B O   1 
ATOM   4250  C CB  . LYS B  1 4   ? -24.204  20.669  -53.588  1.00 60.06  ? 4   LYS B CB  1 
ATOM   4251  C CG  . LYS B  1 4   ? -25.028  19.454  -53.198  1.00 63.27  ? 4   LYS B CG  1 
ATOM   4252  C CD  . LYS B  1 4   ? -24.913  19.150  -51.710  1.00 66.38  ? 4   LYS B CD  1 
ATOM   4253  C CE  . LYS B  1 4   ? -26.157  18.555  -51.133  1.00 67.56  ? 4   LYS B CE  1 
ATOM   4254  N NZ  . LYS B  1 4   ? -26.846  17.682  -52.086  1.00 69.18  ? 4   LYS B NZ  1 
ATOM   4255  N N   . THR B  1 5   ? -24.695  19.487  -56.583  1.00 41.27  ? 5   THR B N   1 
ATOM   4256  C CA  . THR B  1 5   ? -25.408  18.574  -57.503  1.00 38.18  ? 5   THR B CA  1 
ATOM   4257  C C   . THR B  1 5   ? -26.340  17.646  -56.753  1.00 36.26  ? 5   THR B C   1 
ATOM   4258  O O   . THR B  1 5   ? -25.903  17.071  -55.757  1.00 35.50  ? 5   THR B O   1 
ATOM   4259  C CB  . THR B  1 5   ? -24.375  17.810  -58.330  1.00 36.92  ? 5   THR B CB  1 
ATOM   4260  O OG1 . THR B  1 5   ? -23.711  18.782  -59.127  1.00 34.89  ? 5   THR B OG1 1 
ATOM   4261  C CG2 . THR B  1 5   ? -25.007  16.753  -59.217  1.00 35.82  ? 5   THR B CG2 1 
ATOM   4262  N N   . LYS B  1 6   ? -27.599  17.555  -57.179  1.00 38.01  ? 6   LYS B N   1 
ATOM   4263  C CA  . LYS B  1 6   ? -28.563  16.619  -56.616  1.00 38.93  ? 6   LYS B CA  1 
ATOM   4264  C C   . LYS B  1 6   ? -28.436  15.298  -57.378  1.00 38.01  ? 6   LYS B C   1 
ATOM   4265  O O   . LYS B  1 6   ? -28.592  15.246  -58.599  1.00 35.79  ? 6   LYS B O   1 
ATOM   4266  C CB  . LYS B  1 6   ? -29.972  17.218  -56.684  1.00 42.59  ? 6   LYS B CB  1 
ATOM   4267  C CG  . LYS B  1 6   ? -30.982  16.515  -55.797  1.00 47.76  ? 6   LYS B CG  1 
ATOM   4268  C CD  . LYS B  1 6   ? -32.432  16.927  -56.042  1.00 54.79  ? 6   LYS B CD  1 
ATOM   4269  C CE  . LYS B  1 6   ? -33.432  15.873  -55.583  1.00 59.24  ? 6   LYS B CE  1 
ATOM   4270  N NZ  . LYS B  1 6   ? -34.788  16.435  -55.421  1.00 62.00  ? 6   LYS B NZ  1 
ATOM   4271  N N   . ILE B  1 7   ? -28.055  14.239  -56.661  1.00 37.69  ? 7   ILE B N   1 
ATOM   4272  C CA  . ILE B  1 7   ? -27.953  12.924  -57.264  1.00 35.57  ? 7   ILE B CA  1 
ATOM   4273  C C   . ILE B  1 7   ? -29.196  12.149  -56.868  1.00 34.63  ? 7   ILE B C   1 
ATOM   4274  O O   . ILE B  1 7   ? -29.484  12.046  -55.687  1.00 34.39  ? 7   ILE B O   1 
ATOM   4275  C CB  . ILE B  1 7   ? -26.673  12.186  -56.837  1.00 33.94  ? 7   ILE B CB  1 
ATOM   4276  C CG1 . ILE B  1 7   ? -25.452  13.000  -57.176  1.00 34.95  ? 7   ILE B CG1 1 
ATOM   4277  C CG2 . ILE B  1 7   ? -26.622  10.794  -57.483  1.00 34.42  ? 7   ILE B CG2 1 
ATOM   4278  C CD1 . ILE B  1 7   ? -24.129  12.308  -56.884  1.00 35.41  ? 7   ILE B CD1 1 
ATOM   4279  N N   . GLU B  1 8   ? -29.886  11.567  -57.847  1.00 35.21  ? 8   GLU B N   1 
ATOM   4280  C CA  . GLU B  1 8   ? -31.060  10.772  -57.539  1.00 36.55  ? 8   GLU B CA  1 
ATOM   4281  C C   . GLU B  1 8   ? -31.019  9.420   -58.269  1.00 35.62  ? 8   GLU B C   1 
ATOM   4282  O O   . GLU B  1 8   ? -30.771  9.332   -59.476  1.00 35.03  ? 8   GLU B O   1 
ATOM   4283  C CB  . GLU B  1 8   ? -32.249  11.689  -57.783  1.00 36.64  ? 8   GLU B CB  1 
ATOM   4284  C CG  . GLU B  1 8   ? -33.558  10.959  -57.569  1.00 42.89  ? 8   GLU B CG  1 
ATOM   4285  C CD  . GLU B  1 8   ? -34.809  11.788  -57.360  1.00 48.81  ? 8   GLU B CD  1 
ATOM   4286  O OE1 . GLU B  1 8   ? -34.744  13.062  -57.336  1.00 56.65  ? 8   GLU B OE1 1 
ATOM   4287  O OE2 . GLU B  1 8   ? -35.843  11.086  -57.194  1.00 47.30  ? 8   GLU B OE2 1 
ATOM   4288  N N   . LEU B  1 9   ? -31.274  8.349   -57.508  1.00 34.59  ? 9   LEU B N   1 
ATOM   4289  C CA  . LEU B  1 9   ? -31.273  6.997   -58.047  1.00 33.73  ? 9   LEU B CA  1 
ATOM   4290  C C   . LEU B  1 9   ? -32.712  6.533   -58.251  1.00 33.10  ? 9   LEU B C   1 
ATOM   4291  O O   . LEU B  1 9   ? -33.469  6.433   -57.305  1.00 31.45  ? 9   LEU B O   1 
ATOM   4292  C CB  . LEU B  1 9   ? -30.527  6.095   -57.066  1.00 34.27  ? 9   LEU B CB  1 
ATOM   4293  C CG  . LEU B  1 9   ? -29.079  6.510   -56.727  1.00 34.88  ? 9   LEU B CG  1 
ATOM   4294  C CD1 . LEU B  1 9   ? -28.509  5.443   -55.811  1.00 33.76  ? 9   LEU B CD1 1 
ATOM   4295  C CD2 . LEU B  1 9   ? -28.117  6.771   -57.898  1.00 32.71  ? 9   LEU B CD2 1 
ATOM   4296  N N   . LYS B  1 10  ? -33.087  6.222   -59.489  1.00 34.46  ? 10  LYS B N   1 
ATOM   4297  C CA  . LYS B  1 10  ? -34.477  5.949   -59.806  1.00 37.71  ? 10  LYS B CA  1 
ATOM   4298  C C   . LYS B  1 10  ? -34.539  5.314   -61.194  1.00 36.29  ? 10  LYS B C   1 
ATOM   4299  O O   . LYS B  1 10  ? -33.741  5.656   -62.078  1.00 31.54  ? 10  LYS B O   1 
ATOM   4300  C CB  . LYS B  1 10  ? -35.233  7.272   -59.609  1.00 42.89  ? 10  LYS B CB  1 
ATOM   4301  C CG  . LYS B  1 10  ? -36.635  7.426   -60.126  1.00 48.05  ? 10  LYS B CG  1 
ATOM   4302  C CD  . LYS B  1 10  ? -37.774  6.970   -59.223  1.00 55.82  ? 10  LYS B CD  1 
ATOM   4303  C CE  . LYS B  1 10  ? -39.091  7.551   -59.731  1.00 61.94  ? 10  LYS B CE  1 
ATOM   4304  N NZ  . LYS B  1 10  ? -40.225  6.629   -59.568  1.00 64.05  ? 10  LYS B NZ  1 
ATOM   4305  N N   . ASP B  1 11  ? -35.462  4.336   -61.318  1.00 36.65  ? 11  ASP B N   1 
ATOM   4306  C CA  . ASP B  1 11  ? -35.676  3.567   -62.530  1.00 35.02  ? 11  ASP B CA  1 
ATOM   4307  C C   . ASP B  1 11  ? -34.365  2.930   -62.934  1.00 32.04  ? 11  ASP B C   1 
ATOM   4308  O O   . ASP B  1 11  ? -34.082  2.816   -64.113  1.00 31.89  ? 11  ASP B O   1 
ATOM   4309  C CB  . ASP B  1 11  ? -36.192  4.425   -63.681  1.00 37.40  ? 11  ASP B CB  1 
ATOM   4310  C CG  . ASP B  1 11  ? -37.485  5.147   -63.383  1.00 42.14  ? 11  ASP B CG  1 
ATOM   4311  O OD1 . ASP B  1 11  ? -38.352  4.443   -62.847  1.00 45.87  ? 11  ASP B OD1 1 
ATOM   4312  O OD2 . ASP B  1 11  ? -37.564  6.398   -63.617  1.00 48.06  ? 11  ASP B OD2 1 
ATOM   4313  N N   . ASN B  1 12  ? -33.535  2.624   -61.942  1.00 32.80  ? 12  ASN B N   1 
ATOM   4314  C CA  . ASN B  1 12  ? -32.216  2.038   -62.147  1.00 31.57  ? 12  ASN B CA  1 
ATOM   4315  C C   . ASN B  1 12  ? -31.315  2.922   -62.996  1.00 29.25  ? 12  ASN B C   1 
ATOM   4316  O O   . ASN B  1 12  ? -30.496  2.373   -63.720  1.00 27.93  ? 12  ASN B O   1 
ATOM   4317  C CB  . ASN B  1 12  ? -32.304  0.637   -62.742  1.00 30.02  ? 12  ASN B CB  1 
ATOM   4318  C CG  . ASN B  1 12  ? -33.220  -0.194  -61.893  1.00 30.20  ? 12  ASN B CG  1 
ATOM   4319  O OD1 . ASN B  1 12  ? -33.313  0.002   -60.677  1.00 31.09  ? 12  ASN B OD1 1 
ATOM   4320  N ND2 . ASN B  1 12  ? -33.964  -1.071  -62.521  1.00 31.87  ? 12  ASN B ND2 1 
ATOM   4321  N N   . TRP B  1 13  ? -31.442  4.255   -62.847  1.00 30.34  ? 13  TRP B N   1 
ATOM   4322  C CA  . TRP B  1 13  ? -30.533  5.220   -63.462  1.00 29.71  ? 13  TRP B CA  1 
ATOM   4323  C C   . TRP B  1 13  ? -30.038  6.200   -62.422  1.00 29.18  ? 13  TRP B C   1 
ATOM   4324  O O   . TRP B  1 13  ? -30.807  6.634   -61.547  1.00 29.08  ? 13  TRP B O   1 
ATOM   4325  C CB  . TRP B  1 13  ? -31.251  6.036   -64.541  1.00 31.06  ? 13  TRP B CB  1 
ATOM   4326  C CG  . TRP B  1 13  ? -31.337  5.387   -65.899  1.00 32.97  ? 13  TRP B CG  1 
ATOM   4327  C CD1 . TRP B  1 13  ? -32.232  4.451   -66.340  1.00 31.15  ? 13  TRP B CD1 1 
ATOM   4328  C CD2 . TRP B  1 13  ? -30.488  5.703   -67.024  1.00 33.47  ? 13  TRP B CD2 1 
ATOM   4329  N NE1 . TRP B  1 13  ? -31.981  4.149   -67.650  1.00 32.08  ? 13  TRP B NE1 1 
ATOM   4330  C CE2 . TRP B  1 13  ? -30.918  4.893   -68.092  1.00 32.44  ? 13  TRP B CE2 1 
ATOM   4331  C CE3 . TRP B  1 13  ? -29.413  6.574   -67.214  1.00 33.87  ? 13  TRP B CE3 1 
ATOM   4332  C CZ2 . TRP B  1 13  ? -30.313  4.948   -69.337  1.00 32.43  ? 13  TRP B CZ2 1 
ATOM   4333  C CZ3 . TRP B  1 13  ? -28.809  6.620   -68.450  1.00 35.31  ? 13  TRP B CZ3 1 
ATOM   4334  C CH2 . TRP B  1 13  ? -29.252  5.807   -69.494  1.00 33.81  ? 13  TRP B CH2 1 
ATOM   4335  N N   . TYR B  1 14  ? -28.819  6.686   -62.650  1.00 28.29  ? 14  TYR B N   1 
ATOM   4336  C CA  . TYR B  1 14  ? -28.387  7.883   -61.955  1.00 27.44  ? 14  TYR B CA  1 
ATOM   4337  C C   . TYR B  1 14  ? -29.065  9.073   -62.618  1.00 28.10  ? 14  TYR B C   1 
ATOM   4338  O O   . TYR B  1 14  ? -29.110  9.178   -63.844  1.00 28.23  ? 14  TYR B O   1 
ATOM   4339  C CB  . TYR B  1 14  ? -26.903  8.206   -62.000  1.00 26.42  ? 14  TYR B CB  1 
ATOM   4340  C CG  . TYR B  1 14  ? -26.003  7.368   -61.121  1.00 26.90  ? 14  TYR B CG  1 
ATOM   4341  C CD1 . TYR B  1 14  ? -25.908  5.993   -61.306  1.00 26.22  ? 14  TYR B CD1 1 
ATOM   4342  C CD2 . TYR B  1 14  ? -25.135  7.970   -60.209  1.00 27.30  ? 14  TYR B CD2 1 
ATOM   4343  C CE1 . TYR B  1 14  ? -25.015  5.233   -60.569  1.00 25.99  ? 14  TYR B CE1 1 
ATOM   4344  C CE2 . TYR B  1 14  ? -24.249  7.210   -59.454  1.00 27.59  ? 14  TYR B CE2 1 
ATOM   4345  C CZ  . TYR B  1 14  ? -24.181  5.840   -59.653  1.00 25.73  ? 14  TYR B CZ  1 
ATOM   4346  O OH  . TYR B  1 14  ? -23.312  5.078   -58.956  1.00 24.88  ? 14  TYR B OH  1 
ATOM   4347  N N   . HIS B  1 15  ? -29.597  9.958   -61.789  1.00 28.47  ? 15  HIS B N   1 
ATOM   4348  C CA  . HIS B  1 15  ? -29.986  11.277  -62.244  1.00 29.96  ? 15  HIS B CA  1 
ATOM   4349  C C   . HIS B  1 15  ? -29.051  12.312  -61.606  1.00 30.84  ? 15  HIS B C   1 
ATOM   4350  O O   . HIS B  1 15  ? -28.801  12.255  -60.405  1.00 29.17  ? 15  HIS B O   1 
ATOM   4351  C CB  . HIS B  1 15  ? -31.435  11.560  -61.849  1.00 30.08  ? 15  HIS B CB  1 
ATOM   4352  C CG  . HIS B  1 15  ? -32.382  10.570  -62.377  1.00 30.88  ? 15  HIS B CG  1 
ATOM   4353  N ND1 . HIS B  1 15  ? -32.380  9.245   -61.980  1.00 31.36  ? 15  HIS B ND1 1 
ATOM   4354  C CD2 . HIS B  1 15  ? -33.366  10.720  -63.277  1.00 31.50  ? 15  HIS B CD2 1 
ATOM   4355  C CE1 . HIS B  1 15  ? -33.337  8.623   -62.657  1.00 31.62  ? 15  HIS B CE1 1 
ATOM   4356  N NE2 . HIS B  1 15  ? -33.947  9.505   -63.447  1.00 31.17  ? 15  HIS B NE2 1 
ATOM   4357  N N   . LEU B  1 16  ? -28.536  13.239  -62.423  1.00 32.36  ? 16  LEU B N   1 
ATOM   4358  C CA  . LEU B  1 16  ? -27.855  14.429  -61.938  1.00 34.54  ? 16  LEU B CA  1 
ATOM   4359  C C   . LEU B  1 16  ? -28.746  15.603  -62.297  1.00 34.88  ? 16  LEU B C   1 
ATOM   4360  O O   . LEU B  1 16  ? -28.972  15.836  -63.476  1.00 32.89  ? 16  LEU B O   1 
ATOM   4361  C CB  . LEU B  1 16  ? -26.459  14.613  -62.536  1.00 35.35  ? 16  LEU B CB  1 
ATOM   4362  C CG  . LEU B  1 16  ? -25.303  13.862  -61.854  1.00 37.24  ? 16  LEU B CG  1 
ATOM   4363  C CD1 . LEU B  1 16  ? -25.669  12.426  -61.630  1.00 38.50  ? 16  LEU B CD1 1 
ATOM   4364  C CD2 . LEU B  1 16  ? -24.001  13.937  -62.640  1.00 36.14  ? 16  LEU B CD2 1 
ATOM   4365  N N   . ASP B  1 17  ? -29.236  16.300  -61.265  1.00 37.20  ? 17  ASP B N   1 
ATOM   4366  C CA  . ASP B  1 17  ? -29.987  17.527  -61.430  1.00 39.30  ? 17  ASP B CA  1 
ATOM   4367  C C   . ASP B  1 17  ? -31.199  17.241  -62.311  1.00 40.87  ? 17  ASP B C   1 
ATOM   4368  O O   . ASP B  1 17  ? -31.493  18.020  -63.223  1.00 40.48  ? 17  ASP B O   1 
ATOM   4369  C CB  . ASP B  1 17  ? -29.104  18.641  -61.981  1.00 39.33  ? 17  ASP B CB  1 
ATOM   4370  C CG  . ASP B  1 17  ? -28.073  19.238  -61.028  1.00 41.72  ? 17  ASP B CG  1 
ATOM   4371  O OD1 . ASP B  1 17  ? -28.229  19.105  -59.786  1.00 41.78  ? 17  ASP B OD1 1 
ATOM   4372  O OD2 . ASP B  1 17  ? -27.106  19.839  -61.530  1.00 41.82  ? 17  ASP B OD2 1 
ATOM   4373  N N   . GLY B  1 18  ? -31.870  16.107  -62.054  1.00 40.49  ? 18  GLY B N   1 
ATOM   4374  C CA  . GLY B  1 18  ? -33.120  15.780  -62.738  1.00 41.91  ? 18  GLY B CA  1 
ATOM   4375  C C   . GLY B  1 18  ? -32.949  15.006  -64.056  1.00 42.45  ? 18  GLY B C   1 
ATOM   4376  O O   . GLY B  1 18  ? -33.938  14.539  -64.618  1.00 48.57  ? 18  GLY B O   1 
ATOM   4377  N N   . GLU B  1 19  ? -31.717  14.871  -64.565  1.00 39.41  ? 19  GLU B N   1 
ATOM   4378  C CA  . GLU B  1 19  ? -31.479  14.319  -65.892  1.00 39.01  ? 19  GLU B CA  1 
ATOM   4379  C C   . GLU B  1 19  ? -30.844  12.944  -65.750  1.00 35.07  ? 19  GLU B C   1 
ATOM   4380  O O   . GLU B  1 19  ? -29.822  12.804  -65.087  1.00 35.05  ? 19  GLU B O   1 
ATOM   4381  C CB  . GLU B  1 19  ? -30.532  15.168  -66.753  1.00 43.67  ? 19  GLU B CB  1 
ATOM   4382  C CG  . GLU B  1 19  ? -30.896  16.656  -66.865  1.00 49.38  ? 19  GLU B CG  1 
ATOM   4383  C CD  . GLU B  1 19  ? -32.315  16.906  -67.342  1.00 56.42  ? 19  GLU B CD  1 
ATOM   4384  O OE1 . GLU B  1 19  ? -32.609  16.468  -68.475  1.00 61.18  ? 19  GLU B OE1 1 
ATOM   4385  O OE2 . GLU B  1 19  ? -33.134  17.481  -66.588  1.00 62.31  ? 19  GLU B OE2 1 
ATOM   4386  N N   . LYS B  1 20  ? -31.420  11.933  -66.393  1.00 32.52  ? 20  LYS B N   1 
ATOM   4387  C CA  . LYS B  1 20  ? -30.763  10.649  -66.490  1.00 30.83  ? 20  LYS B CA  1 
ATOM   4388  C C   . LYS B  1 20  ? -29.336  10.878  -66.995  1.00 30.75  ? 20  LYS B C   1 
ATOM   4389  O O   . LYS B  1 20  ? -29.145  11.630  -67.956  1.00 29.51  ? 20  LYS B O   1 
ATOM   4390  C CB  . LYS B  1 20  ? -31.530  9.692   -67.411  1.00 32.21  ? 20  LYS B CB  1 
ATOM   4391  C CG  . LYS B  1 20  ? -32.717  9.024   -66.751  1.00 34.95  ? 20  LYS B CG  1 
ATOM   4392  C CD  . LYS B  1 20  ? -33.642  8.153   -67.593  1.00 36.37  ? 20  LYS B CD  1 
ATOM   4393  C CE  . LYS B  1 20  ? -34.825  7.818   -66.729  1.00 42.05  ? 20  LYS B CE  1 
ATOM   4394  N NZ  . LYS B  1 20  ? -36.061  7.513   -67.456  1.00 46.36  ? 20  LYS B NZ  1 
ATOM   4395  N N   . TYR B  1 21  ? -28.351  10.206  -66.360  1.00 29.24  ? 21  TYR B N   1 
ATOM   4396  C CA  . TYR B  1 21  ? -26.947  10.456  -66.637  1.00 28.65  ? 21  TYR B CA  1 
ATOM   4397  C C   . TYR B  1 21  ? -26.192  9.135   -66.745  1.00 28.86  ? 21  TYR B C   1 
ATOM   4398  O O   . TYR B  1 21  ? -25.966  8.483   -65.729  1.00 27.02  ? 21  TYR B O   1 
ATOM   4399  C CB  . TYR B  1 21  ? -26.361  11.306  -65.505  1.00 28.34  ? 21  TYR B CB  1 
ATOM   4400  C CG  . TYR B  1 21  ? -24.933  11.785  -65.732  1.00 27.58  ? 21  TYR B CG  1 
ATOM   4401  C CD1 . TYR B  1 21  ? -24.670  13.028  -66.338  1.00 28.28  ? 21  TYR B CD1 1 
ATOM   4402  C CD2 . TYR B  1 21  ? -23.850  11.032  -65.296  1.00 26.44  ? 21  TYR B CD2 1 
ATOM   4403  C CE1 . TYR B  1 21  ? -23.375  13.492  -66.529  1.00 26.43  ? 21  TYR B CE1 1 
ATOM   4404  C CE2 . TYR B  1 21  ? -22.552  11.483  -65.481  1.00 26.63  ? 21  TYR B CE2 1 
ATOM   4405  C CZ  . TYR B  1 21  ? -22.315  12.705  -66.113  1.00 26.79  ? 21  TYR B CZ  1 
ATOM   4406  O OH  . TYR B  1 21  ? -21.034  13.125  -66.311  1.00 26.89  ? 21  TYR B OH  1 
ATOM   4407  N N   . PHE B  1 22  ? -25.792  8.776   -67.976  1.00 29.22  ? 22  PHE B N   1 
ATOM   4408  C CA  . PHE B  1 22  ? -25.000  7.584   -68.229  1.00 29.38  ? 22  PHE B CA  1 
ATOM   4409  C C   . PHE B  1 22  ? -23.538  7.877   -67.898  1.00 29.52  ? 22  PHE B C   1 
ATOM   4410  O O   . PHE B  1 22  ? -22.926  8.764   -68.480  1.00 29.13  ? 22  PHE B O   1 
ATOM   4411  C CB  . PHE B  1 22  ? -25.149  7.133   -69.680  1.00 28.79  ? 22  PHE B CB  1 
ATOM   4412  C CG  . PHE B  1 22  ? -24.636  5.714   -69.894  1.00 30.11  ? 22  PHE B CG  1 
ATOM   4413  C CD1 . PHE B  1 22  ? -23.285  5.462   -70.067  1.00 30.54  ? 22  PHE B CD1 1 
ATOM   4414  C CD2 . PHE B  1 22  ? -25.509  4.634   -69.923  1.00 27.96  ? 22  PHE B CD2 1 
ATOM   4415  C CE1 . PHE B  1 22  ? -22.826  4.168   -70.227  1.00 30.71  ? 22  PHE B CE1 1 
ATOM   4416  C CE2 . PHE B  1 22  ? -25.037  3.360   -70.107  1.00 27.21  ? 22  PHE B CE2 1 
ATOM   4417  C CZ  . PHE B  1 22  ? -23.713  3.126   -70.270  1.00 28.75  ? 22  PHE B CZ  1 
ATOM   4418  N N   . ILE B  1 23  ? -22.988  7.138   -66.944  1.00 30.31  ? 23  ILE B N   1 
ATOM   4419  C CA  . ILE B  1 23  ? -21.618  7.359   -66.517  1.00 31.28  ? 23  ILE B CA  1 
ATOM   4420  C C   . ILE B  1 23  ? -20.646  6.745   -67.536  1.00 30.72  ? 23  ILE B C   1 
ATOM   4421  O O   . ILE B  1 23  ? -20.529  5.525   -67.625  1.00 27.93  ? 23  ILE B O   1 
ATOM   4422  C CB  . ILE B  1 23  ? -21.390  6.793   -65.102  1.00 31.79  ? 23  ILE B CB  1 
ATOM   4423  C CG1 . ILE B  1 23  ? -22.324  7.447   -64.098  1.00 31.39  ? 23  ILE B CG1 1 
ATOM   4424  C CG2 . ILE B  1 23  ? -19.912  6.935   -64.709  1.00 33.98  ? 23  ILE B CG2 1 
ATOM   4425  C CD1 . ILE B  1 23  ? -22.325  6.792   -62.730  1.00 32.40  ? 23  ILE B CD1 1 
ATOM   4426  N N   . LYS B  1 24  ? -19.962  7.622   -68.290  1.00 30.09  ? 24  LYS B N   1 
ATOM   4427  C CA  . LYS B  1 24  ? -18.928  7.228   -69.230  1.00 29.97  ? 24  LYS B CA  1 
ATOM   4428  C C   . LYS B  1 24  ? -17.551  7.444   -68.610  1.00 28.89  ? 24  LYS B C   1 
ATOM   4429  O O   . LYS B  1 24  ? -16.854  8.409   -68.924  1.00 28.13  ? 24  LYS B O   1 
ATOM   4430  C CB  . LYS B  1 24  ? -19.110  8.037   -70.516  1.00 31.01  ? 24  LYS B CB  1 
ATOM   4431  C CG  . LYS B  1 24  ? -20.454  7.864   -71.178  1.00 32.26  ? 24  LYS B CG  1 
ATOM   4432  C CD  . LYS B  1 24  ? -20.477  8.371   -72.614  1.00 33.31  ? 24  LYS B CD  1 
ATOM   4433  C CE  . LYS B  1 24  ? -20.785  9.805   -72.739  1.00 32.93  ? 24  LYS B CE  1 
ATOM   4434  N NZ  . LYS B  1 24  ? -20.512  10.248  -74.108  1.00 34.32  ? 24  LYS B NZ  1 
ATOM   4435  N N   . ALA B  1 25  ? -17.177  6.524   -67.721  1.00 28.38  ? 25  ALA B N   1 
ATOM   4436  C CA  . ALA B  1 25  ? -15.943  6.660   -66.976  1.00 26.61  ? 25  ALA B CA  1 
ATOM   4437  C C   . ALA B  1 25  ? -14.816  5.898   -67.650  1.00 26.82  ? 25  ALA B C   1 
ATOM   4438  O O   . ALA B  1 25  ? -15.014  5.214   -68.661  1.00 25.91  ? 25  ALA B O   1 
ATOM   4439  C CB  . ALA B  1 25  ? -16.107  6.173   -65.573  1.00 27.35  ? 25  ALA B CB  1 
ATOM   4440  N N   . ILE B  1 26  ? -13.624  6.131   -67.089  1.00 26.75  ? 26  ILE B N   1 
ATOM   4441  C CA  . ILE B  1 26  ? -12.436  5.328   -67.327  1.00 26.19  ? 26  ILE B CA  1 
ATOM   4442  C C   . ILE B  1 26  ? -11.725  5.220   -65.992  1.00 24.57  ? 26  ILE B C   1 
ATOM   4443  O O   . ILE B  1 26  ? -11.669  6.186   -65.248  1.00 25.98  ? 26  ILE B O   1 
ATOM   4444  C CB  . ILE B  1 26  ? -11.517  5.924   -68.415  1.00 27.12  ? 26  ILE B CB  1 
ATOM   4445  C CG1 . ILE B  1 26  ? -10.364  4.987   -68.744  1.00 28.56  ? 26  ILE B CG1 1 
ATOM   4446  C CG2 . ILE B  1 26  ? -11.001  7.318   -68.038  1.00 29.56  ? 26  ILE B CG2 1 
ATOM   4447  C CD1 . ILE B  1 26  ? -9.486   5.431   -69.897  1.00 29.12  ? 26  ILE B CD1 1 
ATOM   4448  N N   . GLY B  1 27  ? -11.197  4.034   -65.688  1.00 24.55  ? 27  GLY B N   1 
ATOM   4449  C CA  . GLY B  1 27  ? -10.317  3.872   -64.536  1.00 23.50  ? 27  GLY B CA  1 
ATOM   4450  C C   . GLY B  1 27  ? -9.079   4.741   -64.710  1.00 22.80  ? 27  GLY B C   1 
ATOM   4451  O O   . GLY B  1 27  ? -8.578   4.861   -65.799  1.00 24.02  ? 27  GLY B O   1 
ATOM   4452  N N   . TYR B  1 28  ? -8.590   5.343   -63.648  1.00 23.36  ? 28  TYR B N   1 
ATOM   4453  C CA  . TYR B  1 28  ? -7.493   6.285   -63.767  1.00 25.24  ? 28  TYR B CA  1 
ATOM   4454  C C   . TYR B  1 28  ? -6.666   6.212   -62.498  1.00 25.49  ? 28  TYR B C   1 
ATOM   4455  O O   . TYR B  1 28  ? -7.202   6.476   -61.450  1.00 25.07  ? 28  TYR B O   1 
ATOM   4456  C CB  . TYR B  1 28  ? -8.022   7.720   -63.949  1.00 25.37  ? 28  TYR B CB  1 
ATOM   4457  C CG  . TYR B  1 28  ? -6.925   8.746   -63.834  1.00 26.87  ? 28  TYR B CG  1 
ATOM   4458  C CD1 . TYR B  1 28  ? -5.747   8.628   -64.562  1.00 27.31  ? 28  TYR B CD1 1 
ATOM   4459  C CD2 . TYR B  1 28  ? -7.035   9.804   -62.962  1.00 28.72  ? 28  TYR B CD2 1 
ATOM   4460  C CE1 . TYR B  1 28  ? -4.743   9.564   -64.480  1.00 26.83  ? 28  TYR B CE1 1 
ATOM   4461  C CE2 . TYR B  1 28  ? -6.023   10.745  -62.861  1.00 29.63  ? 28  TYR B CE2 1 
ATOM   4462  C CZ  . TYR B  1 28  ? -4.866   10.605  -63.592  1.00 28.68  ? 28  TYR B CZ  1 
ATOM   4463  O OH  . TYR B  1 28  ? -3.871   11.516  -63.414  1.00 31.11  ? 28  TYR B OH  1 
ATOM   4464  N N   . GLU B  1 29  ? -5.370   5.896   -62.626  1.00 26.80  ? 29  GLU B N   1 
ATOM   4465  C CA  . GLU B  1 29  ? -4.480   5.772   -61.480  1.00 27.71  ? 29  GLU B CA  1 
ATOM   4466  C C   . GLU B  1 29  ? -3.278   6.705   -61.640  1.00 28.51  ? 29  GLU B C   1 
ATOM   4467  O O   . GLU B  1 29  ? -2.328   6.365   -62.366  1.00 28.12  ? 29  GLU B O   1 
ATOM   4468  C CB  . GLU B  1 29  ? -3.989   4.327   -61.354  1.00 28.67  ? 29  GLU B CB  1 
ATOM   4469  C CG  . GLU B  1 29  ? -3.130   4.060   -60.113  1.00 30.26  ? 29  GLU B CG  1 
ATOM   4470  C CD  . GLU B  1 29  ? -2.888   2.582   -59.767  1.00 29.74  ? 29  GLU B CD  1 
ATOM   4471  O OE1 . GLU B  1 29  ? -2.204   1.879   -60.561  1.00 28.18  ? 29  GLU B OE1 1 
ATOM   4472  O OE2 . GLU B  1 29  ? -3.433   2.132   -58.723  1.00 28.76  ? 29  GLU B OE2 1 
ATOM   4473  N N   . ILE B  1 30  ? -3.326   7.852   -60.934  1.00 27.83  ? 30  ILE B N   1 
ATOM   4474  C CA  . ILE B  1 30  ? -2.164   8.720   -60.805  1.00 30.74  ? 30  ILE B CA  1 
ATOM   4475  C C   . ILE B  1 30  ? -1.088   7.977   -60.015  1.00 32.58  ? 30  ILE B C   1 
ATOM   4476  O O   . ILE B  1 30  ? -1.380   7.110   -59.206  1.00 34.63  ? 30  ILE B O   1 
ATOM   4477  C CB  . ILE B  1 30  ? -2.508   10.082  -60.162  1.00 30.98  ? 30  ILE B CB  1 
ATOM   4478  C CG1 . ILE B  1 30  ? -1.356   11.113  -60.330  1.00 32.50  ? 30  ILE B CG1 1 
ATOM   4479  C CG2 . ILE B  1 30  ? -2.897   9.917   -58.686  1.00 29.71  ? 30  ILE B CG2 1 
ATOM   4480  C CD1 . ILE B  1 30  ? -0.933   11.400  -61.762  1.00 32.45  ? 30  ILE B CD1 1 
ATOM   4481  N N   . GLY B  1 31  ? 0.169    8.303   -60.292  1.00 35.67  ? 31  GLY B N   1 
ATOM   4482  C CA  . GLY B  1 31  ? 1.283    7.894   -59.446  1.00 36.29  ? 31  GLY B CA  1 
ATOM   4483  C C   . GLY B  1 31  ? 1.760    6.482   -59.775  1.00 36.10  ? 31  GLY B C   1 
ATOM   4484  O O   . GLY B  1 31  ? 2.363    5.806   -58.926  1.00 35.84  ? 31  GLY B O   1 
ATOM   4485  N N   . ALA B  1 32  ? 1.521    6.087   -61.023  1.00 35.22  ? 32  ALA B N   1 
ATOM   4486  C CA  . ALA B  1 32  ? 1.862    4.728   -61.493  1.00 34.58  ? 32  ALA B CA  1 
ATOM   4487  C C   . ALA B  1 32  ? 2.549    4.821   -62.850  1.00 34.17  ? 32  ALA B C   1 
ATOM   4488  O O   . ALA B  1 32  ? 2.278    3.979   -63.715  1.00 37.65  ? 32  ALA B O   1 
ATOM   4489  C CB  . ALA B  1 32  ? 0.608    3.908   -61.586  1.00 31.09  ? 32  ALA B CB  1 
ATOM   4490  N N   . ARG B  1 33  ? 3.389    5.827   -63.035  1.00 32.86  ? 33  ARG B N   1 
ATOM   4491  C CA  . ARG B  1 33  ? 4.190    5.935   -64.274  1.00 33.12  ? 33  ARG B CA  1 
ATOM   4492  C C   . ARG B  1 33  ? 5.359    4.958   -64.145  1.00 33.72  ? 33  ARG B C   1 
ATOM   4493  O O   . ARG B  1 33  ? 5.580    4.444   -63.046  1.00 33.96  ? 33  ARG B O   1 
ATOM   4494  C CB  . ARG B  1 33  ? 4.692    7.374   -64.434  1.00 32.90  ? 33  ARG B CB  1 
ATOM   4495  C CG  . ARG B  1 33  ? 4.095    8.164   -65.586  1.00 33.09  ? 33  ARG B CG  1 
ATOM   4496  C CD  . ARG B  1 33  ? 2.810    8.837   -65.170  1.00 32.67  ? 33  ARG B CD  1 
ATOM   4497  N NE  . ARG B  1 33  ? 2.213    9.521   -66.318  1.00 34.01  ? 33  ARG B NE  1 
ATOM   4498  C CZ  . ARG B  1 33  ? 1.124    10.264  -66.267  1.00 34.73  ? 33  ARG B CZ  1 
ATOM   4499  N NH1 . ARG B  1 33  ? 0.258    10.100  -65.287  1.00 33.80  ? 33  ARG B NH1 1 
ATOM   4500  N NH2 . ARG B  1 33  ? 0.908    11.169  -67.199  1.00 34.76  ? 33  ARG B NH2 1 
ATOM   4501  N N   . PRO B  1 34  ? 6.100    4.646   -65.221  1.00 33.64  ? 34  PRO B N   1 
ATOM   4502  C CA  . PRO B  1 34  ? 7.283    3.813   -65.069  1.00 34.94  ? 34  PRO B CA  1 
ATOM   4503  C C   . PRO B  1 34  ? 8.199    4.364   -63.966  1.00 37.27  ? 34  PRO B C   1 
ATOM   4504  O O   . PRO B  1 34  ? 8.404    5.587   -63.920  1.00 37.65  ? 34  PRO B O   1 
ATOM   4505  C CB  . PRO B  1 34  ? 7.851    3.863   -66.478  1.00 34.29  ? 34  PRO B CB  1 
ATOM   4506  C CG  . PRO B  1 34  ? 6.651    4.046   -67.357  1.00 33.11  ? 34  PRO B CG  1 
ATOM   4507  C CD  . PRO B  1 34  ? 5.818    5.039   -66.586  1.00 32.59  ? 34  PRO B CD  1 
ATOM   4508  N N   . GLY B  1 35  ? 8.700    3.500   -63.077  1.00 38.52  ? 35  GLY B N   1 
ATOM   4509  C CA  . GLY B  1 35  ? 9.530    3.908   -61.945  1.00 40.45  ? 35  GLY B CA  1 
ATOM   4510  C C   . GLY B  1 35  ? 8.727    4.215   -60.664  1.00 39.26  ? 35  GLY B C   1 
ATOM   4511  O O   . GLY B  1 35  ? 9.305    4.472   -59.617  1.00 40.89  ? 35  GLY B O   1 
ATOM   4512  N N   . GLN B  1 36  ? 7.394    4.161   -60.724  1.00 37.21  ? 36  GLN B N   1 
ATOM   4513  C CA  . GLN B  1 36  ? 6.567    4.580   -59.608  1.00 37.17  ? 36  GLN B CA  1 
ATOM   4514  C C   . GLN B  1 36  ? 5.656    3.424   -59.194  1.00 37.61  ? 36  GLN B C   1 
ATOM   4515  O O   . GLN B  1 36  ? 5.230    2.634   -60.029  1.00 38.03  ? 36  GLN B O   1 
ATOM   4516  C CB  . GLN B  1 36  ? 5.607    5.725   -59.926  1.00 36.35  ? 36  GLN B CB  1 
ATOM   4517  C CG  . GLN B  1 36  ? 6.218    6.928   -60.638  1.00 36.00  ? 36  GLN B CG  1 
ATOM   4518  C CD  . GLN B  1 36  ? 5.304    8.147   -60.607  1.00 34.70  ? 36  GLN B CD  1 
ATOM   4519  O OE1 . GLN B  1 36  ? 4.145    8.140   -61.013  1.00 31.93  ? 36  GLN B OE1 1 
ATOM   4520  N NE2 . GLN B  1 36  ? 5.820    9.247   -60.113  1.00 36.69  ? 36  GLN B NE2 1 
ATOM   4521  N N   . ALA B  1 37  ? 5.374    3.367   -57.894  1.00 38.56  ? 37  ALA B N   1 
ATOM   4522  C CA  . ALA B  1 37  ? 4.425    2.449   -57.297  1.00 40.73  ? 37  ALA B CA  1 
ATOM   4523  C C   . ALA B  1 37  ? 3.552    3.253   -56.331  1.00 39.45  ? 37  ALA B C   1 
ATOM   4524  O O   . ALA B  1 37  ? 3.994    3.738   -55.309  1.00 37.76  ? 37  ALA B O   1 
ATOM   4525  C CB  . ALA B  1 37  ? 5.176    1.320   -56.602  1.00 42.22  ? 37  ALA B CB  1 
ATOM   4526  N N   . PRO B  1 38  ? 2.270    3.471   -56.631  1.00 40.28  ? 38  PRO B N   1 
ATOM   4527  C CA  . PRO B  1 38  ? 1.484    4.397   -55.822  1.00 42.90  ? 38  PRO B CA  1 
ATOM   4528  C C   . PRO B  1 38  ? 1.308    3.995   -54.357  1.00 45.23  ? 38  PRO B C   1 
ATOM   4529  O O   . PRO B  1 38  ? 1.120    4.871   -53.522  1.00 44.28  ? 38  PRO B O   1 
ATOM   4530  C CB  . PRO B  1 38  ? 0.163    4.455   -56.579  1.00 41.90  ? 38  PRO B CB  1 
ATOM   4531  C CG  . PRO B  1 38  ? 0.100    3.125   -57.294  1.00 42.31  ? 38  PRO B CG  1 
ATOM   4532  C CD  . PRO B  1 38  ? 1.525    2.814   -57.706  1.00 39.93  ? 38  PRO B CD  1 
ATOM   4533  N N   . TYR B  1 39  ? 1.406    2.691   -54.032  1.00 47.70  ? 39  TYR B N   1 
ATOM   4534  C CA  . TYR B  1 39  ? 1.156    2.219   -52.668  1.00 45.76  ? 39  TYR B CA  1 
ATOM   4535  C C   . TYR B  1 39  ? 2.437    2.159   -51.836  1.00 45.11  ? 39  TYR B C   1 
ATOM   4536  O O   . TYR B  1 39  ? 2.333    2.052   -50.629  1.00 44.27  ? 39  TYR B O   1 
ATOM   4537  C CB  . TYR B  1 39  ? 0.388    0.888   -52.633  1.00 43.63  ? 39  TYR B CB  1 
ATOM   4538  C CG  . TYR B  1 39  ? -1.012   1.043   -53.221  1.00 42.09  ? 39  TYR B CG  1 
ATOM   4539  C CD1 . TYR B  1 39  ? -2.027   1.723   -52.549  1.00 40.99  ? 39  TYR B CD1 1 
ATOM   4540  C CD2 . TYR B  1 39  ? -1.297   0.557   -54.495  1.00 41.58  ? 39  TYR B CD2 1 
ATOM   4541  C CE1 . TYR B  1 39  ? -3.284   1.899   -53.131  1.00 42.59  ? 39  TYR B CE1 1 
ATOM   4542  C CE2 . TYR B  1 39  ? -2.534   0.752   -55.094  1.00 40.39  ? 39  TYR B CE2 1 
ATOM   4543  C CZ  . TYR B  1 39  ? -3.540   1.415   -54.410  1.00 39.79  ? 39  TYR B CZ  1 
ATOM   4544  O OH  . TYR B  1 39  ? -4.741   1.519   -55.056  1.00 36.50  ? 39  TYR B OH  1 
ATOM   4545  N N   . GLU B  1 40  ? 3.626    2.254   -52.447  1.00 48.61  ? 40  GLU B N   1 
ATOM   4546  C CA  . GLU B  1 40  ? 4.881    2.139   -51.703  1.00 55.08  ? 40  GLU B CA  1 
ATOM   4547  C C   . GLU B  1 40  ? 5.602    3.484   -51.639  1.00 54.60  ? 40  GLU B C   1 
ATOM   4548  O O   . GLU B  1 40  ? 6.321    3.768   -50.683  1.00 54.36  ? 40  GLU B O   1 
ATOM   4549  C CB  . GLU B  1 40  ? 5.929    1.196   -52.304  1.00 58.33  ? 40  GLU B CB  1 
ATOM   4550  C CG  . GLU B  1 40  ? 5.491    -0.245  -52.578  1.00 61.13  ? 40  GLU B CG  1 
ATOM   4551  C CD  . GLU B  1 40  ? 6.491    -0.952  -53.494  1.00 63.39  ? 40  GLU B CD  1 
ATOM   4552  O OE1 . GLU B  1 40  ? 7.490    -0.302  -53.888  1.00 63.08  ? 40  GLU B OE1 1 
ATOM   4553  O OE2 . GLU B  1 40  ? 6.295    -2.131  -53.848  1.00 63.91  ? 40  GLU B OE2 1 
ATOM   4554  N N   . ASP B  1 41  ? 5.436    4.267   -52.705  1.00 55.64  ? 41  ASP B N   1 
ATOM   4555  C CA  . ASP B  1 41  ? 6.071    5.560   -52.879  1.00 59.97  ? 41  ASP B CA  1 
ATOM   4556  C C   . ASP B  1 41  ? 5.562    6.557   -51.829  1.00 62.24  ? 41  ASP B C   1 
ATOM   4557  O O   . ASP B  1 41  ? 4.398    6.517   -51.427  1.00 61.66  ? 41  ASP B O   1 
ATOM   4558  C CB  . ASP B  1 41  ? 5.866    6.051   -54.315  1.00 57.93  ? 41  ASP B CB  1 
ATOM   4559  C CG  . ASP B  1 41  ? 6.754    5.418   -55.391  1.00 57.84  ? 41  ASP B CG  1 
ATOM   4560  O OD1 . ASP B  1 41  ? 7.659    4.589   -55.060  1.00 55.22  ? 41  ASP B OD1 1 
ATOM   4561  O OD2 . ASP B  1 41  ? 6.545    5.761   -56.567  1.00 52.23  ? 41  ASP B OD2 1 
ATOM   4562  N N   . GLU B  1 42  ? 6.446    7.470   -51.403  1.00 62.28  ? 42  GLU B N   1 
ATOM   4563  C CA  . GLU B  1 42  ? 6.027    8.675   -50.707  1.00 65.07  ? 42  GLU B CA  1 
ATOM   4564  C C   . GLU B  1 42  ? 4.900    9.312   -51.524  1.00 61.91  ? 42  GLU B C   1 
ATOM   4565  O O   . GLU B  1 42  ? 4.987    9.389   -52.744  1.00 55.78  ? 42  GLU B O   1 
ATOM   4566  C CB  . GLU B  1 42  ? 7.274    9.546   -50.542  1.00 71.33  ? 42  GLU B CB  1 
ATOM   4567  C CG  . GLU B  1 42  ? 7.025    10.909  -49.903  1.00 75.72  ? 42  GLU B CG  1 
ATOM   4568  C CD  . GLU B  1 42  ? 8.073    11.912  -50.350  1.00 83.27  ? 42  GLU B CD  1 
ATOM   4569  O OE1 . GLU B  1 42  ? 9.264    11.639  -50.075  1.00 83.32  ? 42  GLU B OE1 1 
ATOM   4570  O OE2 . GLU B  1 42  ? 7.713    12.922  -51.010  1.00 85.23  ? 42  GLU B OE2 1 
ATOM   4571  N N   . ARG B  1 43  ? 3.822    9.735   -50.861  1.00 61.18  ? 43  ARG B N   1 
ATOM   4572  C CA  . ARG B  1 43  ? 2.623    10.141  -51.576  1.00 66.02  ? 43  ARG B CA  1 
ATOM   4573  C C   . ARG B  1 43  ? 2.827    11.566  -52.097  1.00 58.07  ? 43  ARG B C   1 
ATOM   4574  O O   . ARG B  1 43  ? 3.233    12.447  -51.342  1.00 53.19  ? 43  ARG B O   1 
ATOM   4575  C CB  . ARG B  1 43  ? 1.413    9.914   -50.653  1.00 75.87  ? 43  ARG B CB  1 
ATOM   4576  C CG  . ARG B  1 43  ? 0.073    9.602   -51.314  1.00 81.91  ? 43  ARG B CG  1 
ATOM   4577  C CD  . ARG B  1 43  ? -0.690   10.860  -51.770  1.00 93.25  ? 43  ARG B CD  1 
ATOM   4578  N NE  . ARG B  1 43  ? -0.810   11.939  -50.768  1.00 94.86  ? 43  ARG B NE  1 
ATOM   4579  C CZ  . ARG B  1 43  ? -0.794   13.273  -50.980  1.00 86.98  ? 43  ARG B CZ  1 
ATOM   4580  N NH1 . ARG B  1 43  ? -0.918   13.760  -52.204  1.00 85.84  ? 43  ARG B NH1 1 
ATOM   4581  N NH2 . ARG B  1 43  ? -0.707   14.123  -49.963  1.00 76.79  ? 43  ARG B NH2 1 
ATOM   4582  N N   . LYS B  1 44  ? 2.586    11.764  -53.403  1.00 53.58  ? 44  LYS B N   1 
ATOM   4583  C CA  . LYS B  1 44  ? 2.705    13.072  -54.031  1.00 52.94  ? 44  LYS B CA  1 
ATOM   4584  C C   . LYS B  1 44  ? 1.418    13.409  -54.806  1.00 49.18  ? 44  LYS B C   1 
ATOM   4585  O O   . LYS B  1 44  ? 0.705    12.523  -55.295  1.00 42.28  ? 44  LYS B O   1 
ATOM   4586  C CB  . LYS B  1 44  ? 3.991    13.160  -54.866  1.00 54.98  ? 44  LYS B CB  1 
ATOM   4587  C CG  . LYS B  1 44  ? 5.311    13.056  -54.092  1.00 62.84  ? 44  LYS B CG  1 
ATOM   4588  C CD  . LYS B  1 44  ? 6.531    13.757  -54.696  1.00 72.46  ? 44  LYS B CD  1 
ATOM   4589  C CE  . LYS B  1 44  ? 6.760    13.477  -56.173  1.00 78.14  ? 44  LYS B CE  1 
ATOM   4590  N NZ  . LYS B  1 44  ? 6.956    12.060  -56.497  1.00 74.70  ? 44  LYS B NZ  1 
ATOM   4591  N N   . ASP B  1 45  ? 1.126    14.723  -54.894  1.00 45.80  ? 45  ASP B N   1 
ATOM   4592  C CA  . ASP B  1 45  ? -0.079   15.240  -55.533  1.00 42.34  ? 45  ASP B CA  1 
ATOM   4593  C C   . ASP B  1 45  ? -0.003   15.047  -57.050  1.00 39.65  ? 45  ASP B C   1 
ATOM   4594  O O   . ASP B  1 45  ? -0.977   14.631  -57.651  1.00 38.80  ? 45  ASP B O   1 
ATOM   4595  C CB  . ASP B  1 45  ? -0.329   16.702  -55.143  1.00 42.82  ? 45  ASP B CB  1 
ATOM   4596  C CG  . ASP B  1 45  ? -1.035   16.976  -53.817  1.00 41.17  ? 45  ASP B CG  1 
ATOM   4597  O OD1 . ASP B  1 45  ? -1.724   16.082  -53.278  1.00 41.89  ? 45  ASP B OD1 1 
ATOM   4598  O OD2 . ASP B  1 45  ? -0.889   18.075  -53.315  1.00 39.78  ? 45  ASP B OD2 1 
ATOM   4599  N N   . GLU B  1 46  ? 1.132    15.402  -57.678  1.00 40.84  ? 46  GLU B N   1 
ATOM   4600  C CA  . GLU B  1 46  ? 1.369    15.133  -59.094  1.00 40.86  ? 46  GLU B CA  1 
ATOM   4601  C C   . GLU B  1 46  ? 0.434    15.946  -59.996  1.00 38.74  ? 46  GLU B C   1 
ATOM   4602  O O   . GLU B  1 46  ? -0.089   15.447  -60.996  1.00 38.12  ? 46  GLU B O   1 
ATOM   4603  C CB  . GLU B  1 46  ? 1.233    13.633  -59.365  1.00 41.31  ? 46  GLU B CB  1 
ATOM   4604  C CG  . GLU B  1 46  ? 2.291    12.811  -58.641  1.00 44.08  ? 46  GLU B CG  1 
ATOM   4605  C CD  . GLU B  1 46  ? 3.326    12.238  -59.586  1.00 46.99  ? 46  GLU B CD  1 
ATOM   4606  O OE1 . GLU B  1 46  ? 4.032    12.924  -60.358  1.00 55.77  ? 46  GLU B OE1 1 
ATOM   4607  O OE2 . GLU B  1 46  ? 3.375    11.018  -59.553  1.00 51.13  ? 46  GLU B OE2 1 
ATOM   4608  N N   . LEU B  1 47  ? 0.295    17.237  -59.697  1.00 37.59  ? 47  LEU B N   1 
ATOM   4609  C CA  . LEU B  1 47  ? -0.754   18.035  -60.298  1.00 37.19  ? 47  LEU B CA  1 
ATOM   4610  C C   . LEU B  1 47  ? -0.482   18.223  -61.776  1.00 37.36  ? 47  LEU B C   1 
ATOM   4611  O O   . LEU B  1 47  ? -1.422   18.210  -62.554  1.00 36.73  ? 47  LEU B O   1 
ATOM   4612  C CB  . LEU B  1 47  ? -0.895   19.364  -59.556  1.00 38.01  ? 47  LEU B CB  1 
ATOM   4613  C CG  . LEU B  1 47  ? -1.341   19.215  -58.100  1.00 37.33  ? 47  LEU B CG  1 
ATOM   4614  C CD1 . LEU B  1 47  ? -1.415   20.558  -57.474  1.00 37.93  ? 47  LEU B CD1 1 
ATOM   4615  C CD2 . LEU B  1 47  ? -2.694   18.480  -57.961  1.00 36.90  ? 47  LEU B CD2 1 
ATOM   4616  N N   . GLU B  1 48  ? 0.791    18.365  -62.156  1.00 40.05  ? 48  GLU B N   1 
ATOM   4617  C CA  . GLU B  1 48  ? 1.143    18.648  -63.545  1.00 41.83  ? 48  GLU B CA  1 
ATOM   4618  C C   . GLU B  1 48  ? 0.769    17.457  -64.415  1.00 38.92  ? 48  GLU B C   1 
ATOM   4619  O O   . GLU B  1 48  ? 0.181    17.651  -65.466  1.00 37.29  ? 48  GLU B O   1 
ATOM   4620  C CB  . GLU B  1 48  ? 2.601    19.050  -63.805  1.00 45.50  ? 48  GLU B CB  1 
ATOM   4621  C CG  . GLU B  1 48  ? 2.988    20.411  -63.221  1.00 51.18  ? 48  GLU B CG  1 
ATOM   4622  C CD  . GLU B  1 48  ? 1.916    21.504  -63.327  1.00 56.36  ? 48  GLU B CD  1 
ATOM   4623  O OE1 . GLU B  1 48  ? 1.536    21.852  -64.479  1.00 59.43  ? 48  GLU B OE1 1 
ATOM   4624  O OE2 . GLU B  1 48  ? 1.429    21.993  -62.262  1.00 57.39  ? 48  GLU B OE2 1 
ATOM   4625  N N   . LEU B  1 49  ? 1.102    16.241  -63.969  1.00 38.73  ? 49  LEU B N   1 
ATOM   4626  C CA  . LEU B  1 49  ? 0.762    15.037  -64.720  1.00 38.07  ? 49  LEU B CA  1 
ATOM   4627  C C   . LEU B  1 49  ? -0.749   14.819  -64.685  1.00 34.87  ? 49  LEU B C   1 
ATOM   4628  O O   . LEU B  1 49  ? -1.336   14.327  -65.642  1.00 33.62  ? 49  LEU B O   1 
ATOM   4629  C CB  . LEU B  1 49  ? 1.530    13.795  -64.232  1.00 37.46  ? 49  LEU B CB  1 
ATOM   4630  C CG  . LEU B  1 49  ? 3.049    13.805  -64.461  1.00 37.91  ? 49  LEU B CG  1 
ATOM   4631  C CD1 . LEU B  1 49  ? 3.809    12.592  -63.931  1.00 35.96  ? 49  LEU B CD1 1 
ATOM   4632  C CD2 . LEU B  1 49  ? 3.372    14.006  -65.945  1.00 38.53  ? 49  LEU B CD2 1 
ATOM   4633  N N   . MET B  1 50  ? -1.404   15.201  -63.586  1.00 36.22  ? 50  MET B N   1 
ATOM   4634  C CA  . MET B  1 50  ? -2.855   15.036  -63.515  1.00 34.18  ? 50  MET B CA  1 
ATOM   4635  C C   . MET B  1 50  ? -3.575   15.920  -64.535  1.00 32.85  ? 50  MET B C   1 
ATOM   4636  O O   . MET B  1 50  ? -4.547   15.482  -65.139  1.00 30.72  ? 50  MET B O   1 
ATOM   4637  C CB  . MET B  1 50  ? -3.390   15.319  -62.112  1.00 35.52  ? 50  MET B CB  1 
ATOM   4638  C CG  . MET B  1 50  ? -3.340   14.130  -61.193  1.00 34.48  ? 50  MET B CG  1 
ATOM   4639  S SD  . MET B  1 50  ? -4.280   14.427  -59.684  1.00 35.25  ? 50  MET B SD  1 
ATOM   4640  C CE  . MET B  1 50  ? -5.891   14.077  -60.386  1.00 35.93  ? 50  MET B CE  1 
ATOM   4641  N N   . LYS B  1 51  ? -3.093   17.156  -64.728  1.00 34.18  ? 51  LYS B N   1 
ATOM   4642  C CA  . LYS B  1 51  ? -3.646   18.073  -65.723  1.00 36.05  ? 51  LYS B CA  1 
ATOM   4643  C C   . LYS B  1 51  ? -3.570   17.468  -67.119  1.00 33.82  ? 51  LYS B C   1 
ATOM   4644  O O   . LYS B  1 51  ? -4.522   17.547  -67.888  1.00 33.09  ? 51  LYS B O   1 
ATOM   4645  C CB  . LYS B  1 51  ? -2.926   19.437  -65.745  1.00 39.77  ? 51  LYS B CB  1 
ATOM   4646  C CG  . LYS B  1 51  ? -3.283   20.364  -64.589  1.00 42.97  ? 51  LYS B CG  1 
ATOM   4647  C CD  . LYS B  1 51  ? -2.366   21.569  -64.425  1.00 46.33  ? 51  LYS B CD  1 
ATOM   4648  C CE  . LYS B  1 51  ? -2.839   22.455  -63.321  1.00 49.19  ? 51  LYS B CE  1 
ATOM   4649  N NZ  . LYS B  1 51  ? -1.680   23.154  -62.758  1.00 52.81  ? 51  LYS B NZ  1 
ATOM   4650  N N   . PHE B  1 52  ? -2.395   16.939  -67.462  1.00 33.58  ? 52  PHE B N   1 
ATOM   4651  C CA  . PHE B  1 52  ? -2.186   16.286  -68.743  1.00 32.84  ? 52  PHE B CA  1 
ATOM   4652  C C   . PHE B  1 52  ? -3.189   15.153  -68.907  1.00 30.75  ? 52  PHE B C   1 
ATOM   4653  O O   . PHE B  1 52  ? -3.874   15.108  -69.920  1.00 28.59  ? 52  PHE B O   1 
ATOM   4654  C CB  . PHE B  1 52  ? -0.740   15.792  -68.762  1.00 34.16  ? 52  PHE B CB  1 
ATOM   4655  C CG  . PHE B  1 52  ? -0.382   14.868  -69.907  1.00 34.35  ? 52  PHE B CG  1 
ATOM   4656  C CD1 . PHE B  1 52  ? -0.053   15.384  -71.155  1.00 36.22  ? 52  PHE B CD1 1 
ATOM   4657  C CD2 . PHE B  1 52  ? -0.278   13.501  -69.697  1.00 33.29  ? 52  PHE B CD2 1 
ATOM   4658  C CE1 . PHE B  1 52  ? 0.310    14.540  -72.186  1.00 37.62  ? 52  PHE B CE1 1 
ATOM   4659  C CE2 . PHE B  1 52  ? 0.097    12.655  -70.730  1.00 33.74  ? 52  PHE B CE2 1 
ATOM   4660  C CZ  . PHE B  1 52  ? 0.374    13.168  -71.973  1.00 36.22  ? 52  PHE B CZ  1 
ATOM   4661  N N   . ASP B  1 53  ? -3.253   14.279  -67.887  1.00 30.51  ? 53  ASP B N   1 
ATOM   4662  C CA  . ASP B  1 53  ? -4.105   13.085  -67.896  1.00 31.36  ? 53  ASP B CA  1 
ATOM   4663  C C   . ASP B  1 53  ? -5.580   13.468  -68.030  1.00 31.64  ? 53  ASP B C   1 
ATOM   4664  O O   . ASP B  1 53  ? -6.280   12.915  -68.877  1.00 32.04  ? 53  ASP B O   1 
ATOM   4665  C CB  . ASP B  1 53  ? -3.939   12.221  -66.647  1.00 29.72  ? 53  ASP B CB  1 
ATOM   4666  C CG  . ASP B  1 53  ? -2.579   11.542  -66.482  1.00 29.53  ? 53  ASP B CG  1 
ATOM   4667  O OD1 . ASP B  1 53  ? -1.857   11.373  -67.489  1.00 27.72  ? 53  ASP B OD1 1 
ATOM   4668  O OD2 . ASP B  1 53  ? -2.251   11.181  -65.342  1.00 28.78  ? 53  ASP B OD2 1 
ATOM   4669  N N   . LEU B  1 54  ? -6.043   14.421  -67.218  1.00 32.94  ? 54  LEU B N   1 
ATOM   4670  C CA  . LEU B  1 54  ? -7.456   14.782  -67.219  1.00 35.13  ? 54  LEU B CA  1 
ATOM   4671  C C   . LEU B  1 54  ? -7.853   15.450  -68.540  1.00 34.23  ? 54  LEU B C   1 
ATOM   4672  O O   . LEU B  1 54  ? -8.909   15.137  -69.095  1.00 35.39  ? 54  LEU B O   1 
ATOM   4673  C CB  . LEU B  1 54  ? -7.831   15.658  -66.028  1.00 37.73  ? 54  LEU B CB  1 
ATOM   4674  C CG  . LEU B  1 54  ? -7.665   15.059  -64.630  1.00 37.79  ? 54  LEU B CG  1 
ATOM   4675  C CD1 . LEU B  1 54  ? -8.080   16.139  -63.656  1.00 41.58  ? 54  LEU B CD1 1 
ATOM   4676  C CD2 . LEU B  1 54  ? -8.433   13.807  -64.377  1.00 35.39  ? 54  LEU B CD2 1 
ATOM   4677  N N   . GLU B  1 55  ? -7.001   16.323  -69.079  1.00 33.40  ? 55  GLU B N   1 
ATOM   4678  C CA  . GLU B  1 55  ? -7.206   16.830  -70.431  1.00 34.06  ? 55  GLU B CA  1 
ATOM   4679  C C   . GLU B  1 55  ? -7.303   15.686  -71.455  1.00 34.21  ? 55  GLU B C   1 
ATOM   4680  O O   . GLU B  1 55  ? -8.162   15.734  -72.346  1.00 37.78  ? 55  GLU B O   1 
ATOM   4681  C CB  . GLU B  1 55  ? -6.099   17.818  -70.799  1.00 35.42  ? 55  GLU B CB  1 
ATOM   4682  C CG  . GLU B  1 55  ? -6.368   18.600  -72.083  1.00 39.17  ? 55  GLU B CG  1 
ATOM   4683  C CD  . GLU B  1 55  ? -7.759   19.217  -72.214  1.00 42.04  ? 55  GLU B CD  1 
ATOM   4684  O OE1 . GLU B  1 55  ? -8.298   19.790  -71.214  1.00 42.14  ? 55  GLU B OE1 1 
ATOM   4685  O OE2 . GLU B  1 55  ? -8.291   19.126  -73.354  1.00 40.29  ? 55  GLU B OE2 1 
ATOM   4686  N N   . ASN B  1 56  ? -6.430   14.660  -71.380  1.00 30.92  ? 56  ASN B N   1 
ATOM   4687  C CA  . ASN B  1 56  ? -6.512   13.590  -72.361  1.00 30.06  ? 56  ASN B CA  1 
ATOM   4688  C C   . ASN B  1 56  ? -7.844   12.856  -72.226  1.00 28.53  ? 56  ASN B C   1 
ATOM   4689  O O   . ASN B  1 56  ? -8.419   12.432  -73.222  1.00 27.69  ? 56  ASN B O   1 
ATOM   4690  C CB  . ASN B  1 56  ? -5.420   12.536  -72.235  1.00 30.43  ? 56  ASN B CB  1 
ATOM   4691  C CG  . ASN B  1 56  ? -4.056   13.084  -72.542  1.00 31.91  ? 56  ASN B CG  1 
ATOM   4692  O OD1 . ASN B  1 56  ? -3.895   13.944  -73.416  1.00 32.89  ? 56  ASN B OD1 1 
ATOM   4693  N ND2 . ASN B  1 56  ? -3.060   12.596  -71.822  1.00 32.00  ? 56  ASN B ND2 1 
ATOM   4694  N N   . ILE B  1 57  ? -8.272   12.643  -70.983  1.00 28.06  ? 57  ILE B N   1 
ATOM   4695  C CA  . ILE B  1 57  ? -9.419   11.802  -70.685  1.00 28.52  ? 57  ILE B CA  1 
ATOM   4696  C C   . ILE B  1 57  ? -10.692  12.500  -71.187  1.00 30.01  ? 57  ILE B C   1 
ATOM   4697  O O   . ILE B  1 57  ? -11.592  11.840  -71.703  1.00 26.90  ? 57  ILE B O   1 
ATOM   4698  C CB  . ILE B  1 57  ? -9.409   11.453  -69.184  1.00 28.46  ? 57  ILE B CB  1 
ATOM   4699  C CG1 . ILE B  1 57  ? -8.322   10.389  -68.927  1.00 28.58  ? 57  ILE B CG1 1 
ATOM   4700  C CG2 . ILE B  1 57  ? -10.777  10.992  -68.670  1.00 28.50  ? 57  ILE B CG2 1 
ATOM   4701  C CD1 . ILE B  1 57  ? -8.118   9.990   -67.472  1.00 28.51  ? 57  ILE B CD1 1 
ATOM   4702  N N   . LYS B  1 58  ? -10.692  13.846  -71.153  1.00 30.32  ? 58  LYS B N   1 
ATOM   4703  C CA  . LYS B  1 58  ? -11.781  14.628  -71.705  1.00 32.44  ? 58  LYS B CA  1 
ATOM   4704  C C   . LYS B  1 58  ? -11.816  14.510  -73.232  1.00 32.86  ? 58  LYS B C   1 
ATOM   4705  O O   . LYS B  1 58  ? -12.900  14.293  -73.789  1.00 31.78  ? 58  LYS B O   1 
ATOM   4706  C CB  . LYS B  1 58  ? -11.682  16.098  -71.278  1.00 33.73  ? 58  LYS B CB  1 
ATOM   4707  C CG  . LYS B  1 58  ? -12.053  16.370  -69.824  1.00 33.86  ? 58  LYS B CG  1 
ATOM   4708  C CD  . LYS B  1 58  ? -11.491  17.666  -69.248  1.00 36.34  ? 58  LYS B CD  1 
ATOM   4709  C CE  . LYS B  1 58  ? -12.101  18.959  -69.755  1.00 37.34  ? 58  LYS B CE  1 
ATOM   4710  N NZ  . LYS B  1 58  ? -11.461  20.090  -69.088  1.00 37.12  ? 58  LYS B NZ  1 
ATOM   4711  N N   . GLU B  1 59  ? -10.634  14.585  -73.878  1.00 31.94  ? 59  GLU B N   1 
ATOM   4712  C CA  . GLU B  1 59  ? -10.494  14.471  -75.328  1.00 30.78  ? 59  GLU B CA  1 
ATOM   4713  C C   . GLU B  1 59  ? -10.887  13.074  -75.823  1.00 30.71  ? 59  GLU B C   1 
ATOM   4714  O O   . GLU B  1 59  ? -11.344  12.918  -76.955  1.00 31.40  ? 59  GLU B O   1 
ATOM   4715  C CB  . GLU B  1 59  ? -9.092   14.922  -75.739  1.00 32.04  ? 59  GLU B CB  1 
ATOM   4716  C CG  . GLU B  1 59  ? -8.948   16.441  -75.600  1.00 35.93  ? 59  GLU B CG  1 
ATOM   4717  C CD  . GLU B  1 59  ? -7.585   17.032  -75.918  1.00 40.23  ? 59  GLU B CD  1 
ATOM   4718  O OE1 . GLU B  1 59  ? -6.745   16.310  -76.473  1.00 41.90  ? 59  GLU B OE1 1 
ATOM   4719  O OE2 . GLU B  1 59  ? -7.332   18.212  -75.592  1.00 43.66  ? 59  GLU B OE2 1 
ATOM   4720  N N   . GLY B  1 60  ? -10.702  12.048  -74.981  1.00 30.25  ? 60  GLY B N   1 
ATOM   4721  C CA  . GLY B  1 60  ? -11.097  10.687  -75.318  1.00 29.80  ? 60  GLY B CA  1 
ATOM   4722  C C   . GLY B  1 60  ? -12.582  10.390  -75.093  1.00 28.50  ? 60  GLY B C   1 
ATOM   4723  O O   . GLY B  1 60  ? -12.982  9.248   -75.319  1.00 26.36  ? 60  GLY B O   1 
ATOM   4724  N N   . GLY B  1 61  ? -13.377  11.401  -74.643  1.00 28.34  ? 61  GLY B N   1 
ATOM   4725  C CA  . GLY B  1 61  ? -14.841  11.339  -74.666  1.00 27.73  ? 61  GLY B CA  1 
ATOM   4726  C C   . GLY B  1 61  ? -15.499  10.896  -73.348  1.00 29.60  ? 61  GLY B C   1 
ATOM   4727  O O   . GLY B  1 61  ? -16.697  10.636  -73.341  1.00 33.41  ? 61  GLY B O   1 
ATOM   4728  N N   . TYR B  1 62  ? -14.728  10.837  -72.236  1.00 30.38  ? 62  TYR B N   1 
ATOM   4729  C CA  . TYR B  1 62  ? -15.196  10.420  -70.918  1.00 28.10  ? 62  TYR B CA  1 
ATOM   4730  C C   . TYR B  1 62  ? -15.820  11.608  -70.180  1.00 28.14  ? 62  TYR B C   1 
ATOM   4731  O O   . TYR B  1 62  ? -15.440  12.755  -70.434  1.00 27.74  ? 62  TYR B O   1 
ATOM   4732  C CB  . TYR B  1 62  ? -13.986  9.824   -70.193  1.00 26.66  ? 62  TYR B CB  1 
ATOM   4733  C CG  . TYR B  1 62  ? -13.417  8.635   -70.950  1.00 26.17  ? 62  TYR B CG  1 
ATOM   4734  C CD1 . TYR B  1 62  ? -13.976  7.370   -70.826  1.00 27.14  ? 62  TYR B CD1 1 
ATOM   4735  C CD2 . TYR B  1 62  ? -12.329  8.767   -71.787  1.00 26.08  ? 62  TYR B CD2 1 
ATOM   4736  C CE1 . TYR B  1 62  ? -13.472  6.285   -71.521  1.00 26.60  ? 62  TYR B CE1 1 
ATOM   4737  C CE2 . TYR B  1 62  ? -11.820  7.695   -72.501  1.00 27.35  ? 62  TYR B CE2 1 
ATOM   4738  C CZ  . TYR B  1 62  ? -12.378  6.441   -72.347  1.00 26.86  ? 62  TYR B CZ  1 
ATOM   4739  O OH  . TYR B  1 62  ? -11.938  5.394   -73.105  1.00 28.77  ? 62  TYR B OH  1 
ATOM   4740  N N   . ASN B  1 63  ? -16.791  11.326  -69.292  1.00 26.89  ? 63  ASN B N   1 
ATOM   4741  C CA  . ASN B  1 63  ? -17.373  12.354  -68.438  1.00 27.90  ? 63  ASN B CA  1 
ATOM   4742  C C   . ASN B  1 63  ? -16.975  12.100  -66.979  1.00 27.77  ? 63  ASN B C   1 
ATOM   4743  O O   . ASN B  1 63  ? -17.234  12.937  -66.119  1.00 28.88  ? 63  ASN B O   1 
ATOM   4744  C CB  . ASN B  1 63  ? -18.883  12.493  -68.680  1.00 27.86  ? 63  ASN B CB  1 
ATOM   4745  C CG  . ASN B  1 63  ? -19.735  11.264  -68.342  1.00 28.43  ? 63  ASN B CG  1 
ATOM   4746  O OD1 . ASN B  1 63  ? -19.320  10.309  -67.669  1.00 26.21  ? 63  ASN B OD1 1 
ATOM   4747  N ND2 . ASN B  1 63  ? -20.979  11.272  -68.788  1.00 27.01  ? 63  ASN B ND2 1 
ATOM   4748  N N   . THR B  1 64  ? -16.348  10.943  -66.708  1.00 26.58  ? 64  THR B N   1 
ATOM   4749  C CA  . THR B  1 64  ? -16.040  10.480  -65.364  1.00 25.11  ? 64  THR B CA  1 
ATOM   4750  C C   . THR B  1 64  ? -14.701  9.756   -65.327  1.00 24.57  ? 64  THR B C   1 
ATOM   4751  O O   . THR B  1 64  ? -14.360  9.061   -66.283  1.00 24.35  ? 64  THR B O   1 
ATOM   4752  C CB  . THR B  1 64  ? -17.107  9.501   -64.901  1.00 24.18  ? 64  THR B CB  1 
ATOM   4753  O OG1 . THR B  1 64  ? -18.333  10.217  -64.922  1.00 25.13  ? 64  THR B OG1 1 
ATOM   4754  C CG2 . THR B  1 64  ? -16.849  9.052   -63.480  1.00 24.17  ? 64  THR B CG2 1 
ATOM   4755  N N   . ILE B  1 65  ? -13.991  9.862   -64.191  1.00 24.49  ? 65  ILE B N   1 
ATOM   4756  C CA  . ILE B  1 65  ? -12.883  8.962   -63.903  1.00 24.52  ? 65  ILE B CA  1 
ATOM   4757  C C   . ILE B  1 65  ? -13.246  8.076   -62.715  1.00 24.87  ? 65  ILE B C   1 
ATOM   4758  O O   . ILE B  1 65  ? -13.982  8.507   -61.811  1.00 25.99  ? 65  ILE B O   1 
ATOM   4759  C CB  . ILE B  1 65  ? -11.588  9.739   -63.599  1.00 24.54  ? 65  ILE B CB  1 
ATOM   4760  C CG1 . ILE B  1 65  ? -11.810  10.798  -62.528  1.00 24.35  ? 65  ILE B CG1 1 
ATOM   4761  C CG2 . ILE B  1 65  ? -11.006  10.301  -64.885  1.00 25.29  ? 65  ILE B CG2 1 
ATOM   4762  C CD1 . ILE B  1 65  ? -10.556  11.482  -62.024  1.00 25.22  ? 65  ILE B CD1 1 
ATOM   4763  N N   . ARG B  1 66  ? -12.632  6.884   -62.662  1.00 25.21  ? 66  ARG B N   1 
ATOM   4764  C CA  . ARG B  1 66  ? -12.814  5.976   -61.533  1.00 25.46  ? 66  ARG B CA  1 
ATOM   4765  C C   . ARG B  1 66  ? -11.460  5.673   -60.890  1.00 26.01  ? 66  ARG B C   1 
ATOM   4766  O O   . ARG B  1 66  ? -10.492  5.366   -61.585  1.00 26.30  ? 66  ARG B O   1 
ATOM   4767  C CB  . ARG B  1 66  ? -13.560  4.737   -62.048  1.00 26.31  ? 66  ARG B CB  1 
ATOM   4768  C CG  . ARG B  1 66  ? -13.631  3.502   -61.153  1.00 26.02  ? 66  ARG B CG  1 
ATOM   4769  C CD  . ARG B  1 66  ? -12.401  2.577   -61.201  1.00 28.41  ? 66  ARG B CD  1 
ATOM   4770  N NE  . ARG B  1 66  ? -12.775  1.220   -60.731  1.00 30.32  ? 66  ARG B NE  1 
ATOM   4771  C CZ  . ARG B  1 66  ? -12.535  0.729   -59.528  1.00 30.68  ? 66  ARG B CZ  1 
ATOM   4772  N NH1 . ARG B  1 66  ? -11.988  1.484   -58.578  1.00 32.10  ? 66  ARG B NH1 1 
ATOM   4773  N NH2 . ARG B  1 66  ? -12.819  -0.528  -59.274  1.00 32.78  ? 66  ARG B NH2 1 
ATOM   4774  N N   . THR B  1 67  ? -11.385  5.693   -59.554  1.00 26.45  ? 67  THR B N   1 
ATOM   4775  C CA  . THR B  1 67  ? -10.096  5.518   -58.898  1.00 28.01  ? 67  THR B CA  1 
ATOM   4776  C C   . THR B  1 67  ? -10.164  4.436   -57.812  1.00 28.76  ? 67  THR B C   1 
ATOM   4777  O O   . THR B  1 67  ? -11.269  4.012   -57.438  1.00 26.79  ? 67  THR B O   1 
ATOM   4778  C CB  . THR B  1 67  ? -9.673   6.862   -58.312  1.00 28.15  ? 67  THR B CB  1 
ATOM   4779  O OG1 . THR B  1 67  ? -10.567  7.056   -57.215  1.00 27.28  ? 67  THR B OG1 1 
ATOM   4780  C CG2 . THR B  1 67  ? -9.736   7.985   -59.339  1.00 28.91  ? 67  THR B CG2 1 
ATOM   4781  N N   . TRP B  1 68  ? -8.976   4.112   -57.253  1.00 28.53  ? 68  TRP B N   1 
ATOM   4782  C CA  . TRP B  1 68  ? -8.811   3.043   -56.269  1.00 31.54  ? 68  TRP B CA  1 
ATOM   4783  C C   . TRP B  1 68  ? -8.403   3.586   -54.894  1.00 33.47  ? 68  TRP B C   1 
ATOM   4784  O O   . TRP B  1 68  ? -8.604   2.898   -53.900  1.00 37.30  ? 68  TRP B O   1 
ATOM   4785  C CB  . TRP B  1 68  ? -7.802   1.975   -56.761  1.00 29.29  ? 68  TRP B CB  1 
ATOM   4786  C CG  . TRP B  1 68  ? -8.370   1.136   -57.871  1.00 28.03  ? 68  TRP B CG  1 
ATOM   4787  C CD1 . TRP B  1 68  ? -8.968   -0.081  -57.746  1.00 27.91  ? 68  TRP B CD1 1 
ATOM   4788  C CD2 . TRP B  1 68  ? -8.484   1.479   -59.270  1.00 29.22  ? 68  TRP B CD2 1 
ATOM   4789  N NE1 . TRP B  1 68  ? -9.426   -0.526  -58.953  1.00 27.00  ? 68  TRP B NE1 1 
ATOM   4790  C CE2 . TRP B  1 68  ? -9.175   0.420   -59.904  1.00 26.97  ? 68  TRP B CE2 1 
ATOM   4791  C CE3 . TRP B  1 68  ? -8.097   2.575   -60.049  1.00 29.44  ? 68  TRP B CE3 1 
ATOM   4792  C CZ2 . TRP B  1 68  ? -9.479   0.430   -61.261  1.00 26.52  ? 68  TRP B CZ2 1 
ATOM   4793  C CZ3 . TRP B  1 68  ? -8.420   2.587   -61.389  1.00 27.94  ? 68  TRP B CZ3 1 
ATOM   4794  C CH2 . TRP B  1 68  ? -9.111   1.537   -61.986  1.00 26.45  ? 68  TRP B CH2 1 
ATOM   4795  N N   . SER B  1 69  ? -7.760   4.764   -54.826  1.00 33.39  ? 69  SER B N   1 
ATOM   4796  C CA  . SER B  1 69  ? -7.461   5.374   -53.537  1.00 31.60  ? 69  SER B CA  1 
ATOM   4797  C C   . SER B  1 69  ? -7.722   6.867   -53.562  1.00 30.25  ? 69  SER B C   1 
ATOM   4798  O O   . SER B  1 69  ? -7.584   7.531   -54.578  1.00 29.80  ? 69  SER B O   1 
ATOM   4799  C CB  . SER B  1 69  ? -6.053   5.112   -53.058  1.00 30.71  ? 69  SER B CB  1 
ATOM   4800  O OG  . SER B  1 69  ? -5.180   5.270   -54.148  1.00 32.00  ? 69  SER B OG  1 
ATOM   4801  N N   . GLN B  1 70  ? -7.968   7.356   -52.359  1.00 31.82  ? 70  GLN B N   1 
ATOM   4802  C CA  . GLN B  1 70  ? -8.529   8.670   -52.120  1.00 33.59  ? 70  GLN B CA  1 
ATOM   4803  C C   . GLN B  1 70  ? -7.537   9.728   -52.567  1.00 33.21  ? 70  GLN B C   1 
ATOM   4804  O O   . GLN B  1 70  ? -6.353   9.599   -52.324  1.00 35.44  ? 70  GLN B O   1 
ATOM   4805  C CB  . GLN B  1 70  ? -8.811   8.848   -50.626  1.00 33.14  ? 70  GLN B CB  1 
ATOM   4806  C CG  . GLN B  1 70  ? -7.644   8.408   -49.737  1.00 33.49  ? 70  GLN B CG  1 
ATOM   4807  C CD  . GLN B  1 70  ? -7.821   7.000   -49.200  1.00 31.98  ? 70  GLN B CD  1 
ATOM   4808  O OE1 . GLN B  1 70  ? -8.240   6.075   -49.897  1.00 30.04  ? 70  GLN B OE1 1 
ATOM   4809  N NE2 . GLN B  1 70  ? -7.587   6.837   -47.919  1.00 32.67  ? 70  GLN B NE2 1 
ATOM   4810  N N   . TYR B  1 71  ? -8.054   10.782  -53.189  1.00 33.40  ? 71  TYR B N   1 
ATOM   4811  C CA  . TYR B  1 71  ? -7.277   11.971  -53.505  1.00 32.80  ? 71  TYR B CA  1 
ATOM   4812  C C   . TYR B  1 71  ? -7.157   12.920  -52.311  1.00 32.50  ? 71  TYR B C   1 
ATOM   4813  O O   . TYR B  1 71  ? -8.008   12.968  -51.428  1.00 33.79  ? 71  TYR B O   1 
ATOM   4814  C CB  . TYR B  1 71  ? -7.926   12.743  -54.651  1.00 32.61  ? 71  TYR B CB  1 
ATOM   4815  C CG  . TYR B  1 71  ? -7.808   12.146  -56.044  1.00 31.32  ? 71  TYR B CG  1 
ATOM   4816  C CD1 . TYR B  1 71  ? -6.663   11.493  -56.506  1.00 32.17  ? 71  TYR B CD1 1 
ATOM   4817  C CD2 . TYR B  1 71  ? -8.856   12.286  -56.929  1.00 30.42  ? 71  TYR B CD2 1 
ATOM   4818  C CE1 . TYR B  1 71  ? -6.595   10.990  -57.800  1.00 30.50  ? 71  TYR B CE1 1 
ATOM   4819  C CE2 . TYR B  1 71  ? -8.800   11.780  -58.213  1.00 29.18  ? 71  TYR B CE2 1 
ATOM   4820  C CZ  . TYR B  1 71  ? -7.673   11.134  -58.654  1.00 28.39  ? 71  TYR B CZ  1 
ATOM   4821  O OH  . TYR B  1 71  ? -7.739   10.701  -59.946  1.00 27.91  ? 71  TYR B OH  1 
ATOM   4822  N N   . SER B  1 72  ? -6.055   13.665  -52.297  1.00 32.33  ? 72  SER B N   1 
ATOM   4823  C CA  . SER B  1 72  ? -5.900   14.807  -51.417  1.00 34.21  ? 72  SER B CA  1 
ATOM   4824  C C   . SER B  1 72  ? -6.850   15.927  -51.871  1.00 35.53  ? 72  SER B C   1 
ATOM   4825  O O   . SER B  1 72  ? -7.392   15.913  -52.988  1.00 35.07  ? 72  SER B O   1 
ATOM   4826  C CB  . SER B  1 72  ? -4.468   15.283  -51.419  1.00 33.96  ? 72  SER B CB  1 
ATOM   4827  O OG  . SER B  1 72  ? -4.164   15.828  -52.698  1.00 33.93  ? 72  SER B OG  1 
ATOM   4828  N N   . GLU B  1 73  ? -7.052   16.911  -50.998  1.00 35.19  ? 73  GLU B N   1 
ATOM   4829  C CA  . GLU B  1 73  ? -7.879   18.033  -51.370  1.00 36.72  ? 73  GLU B CA  1 
ATOM   4830  C C   . GLU B  1 73  ? -7.344   18.686  -52.645  1.00 38.35  ? 73  GLU B C   1 
ATOM   4831  O O   . GLU B  1 73  ? -8.123   19.037  -53.531  1.00 39.22  ? 73  GLU B O   1 
ATOM   4832  C CB  . GLU B  1 73  ? -7.943   19.064  -50.246  1.00 37.89  ? 73  GLU B CB  1 
ATOM   4833  C CG  . GLU B  1 73  ? -9.036   20.076  -50.537  1.00 37.16  ? 73  GLU B CG  1 
ATOM   4834  C CD  . GLU B  1 73  ? -9.476   20.863  -49.340  1.00 38.88  ? 73  GLU B CD  1 
ATOM   4835  O OE1 . GLU B  1 73  ? -8.980   20.636  -48.203  1.00 39.26  ? 73  GLU B OE1 1 
ATOM   4836  O OE2 . GLU B  1 73  ? -10.364  21.705  -49.618  1.00 38.61  ? 73  GLU B OE2 1 
ATOM   4837  N N   . ASN B  1 74  ? -6.016   18.893  -52.716  1.00 38.35  ? 74  ASN B N   1 
ATOM   4838  C CA  . ASN B  1 74  ? -5.415   19.557  -53.865  1.00 36.59  ? 74  ASN B CA  1 
ATOM   4839  C C   . ASN B  1 74  ? -5.767   18.787  -55.127  1.00 34.59  ? 74  ASN B C   1 
ATOM   4840  O O   . ASN B  1 74  ? -6.073   19.399  -56.152  1.00 33.39  ? 74  ASN B O   1 
ATOM   4841  C CB  . ASN B  1 74  ? -3.902   19.685  -53.744  1.00 36.76  ? 74  ASN B CB  1 
ATOM   4842  C CG  . ASN B  1 74  ? -3.506   20.731  -52.733  1.00 37.63  ? 74  ASN B CG  1 
ATOM   4843  O OD1 . ASN B  1 74  ? -4.353   21.474  -52.235  1.00 38.06  ? 74  ASN B OD1 1 
ATOM   4844  N ND2 . ASN B  1 74  ? -2.228   20.789  -52.409  1.00 38.30  ? 74  ASN B ND2 1 
ATOM   4845  N N   . GLN B  1 75  ? -5.705   17.453  -55.048  1.00 33.06  ? 75  GLN B N   1 
ATOM   4846  C CA  . GLN B  1 75  ? -6.027   16.655  -56.217  1.00 34.38  ? 75  GLN B CA  1 
ATOM   4847  C C   . GLN B  1 75  ? -7.515   16.801  -56.550  1.00 34.25  ? 75  GLN B C   1 
ATOM   4848  O O   . GLN B  1 75  ? -7.855   16.959  -57.709  1.00 32.66  ? 75  GLN B O   1 
ATOM   4849  C CB  . GLN B  1 75  ? -5.610   15.192  -56.076  1.00 36.34  ? 75  GLN B CB  1 
ATOM   4850  C CG  . GLN B  1 75  ? -4.100   14.977  -55.948  1.00 37.61  ? 75  GLN B CG  1 
ATOM   4851  C CD  . GLN B  1 75  ? -3.759   13.548  -55.596  1.00 37.99  ? 75  GLN B CD  1 
ATOM   4852  O OE1 . GLN B  1 75  ? -4.382   12.968  -54.697  1.00 36.05  ? 75  GLN B OE1 1 
ATOM   4853  N NE2 . GLN B  1 75  ? -2.800   12.972  -56.322  1.00 37.88  ? 75  GLN B NE2 1 
ATOM   4854  N N   . LEU B  1 76  ? -8.397   16.776  -55.540  1.00 36.35  ? 76  LEU B N   1 
ATOM   4855  C CA  . LEU B  1 76  ? -9.826   17.017  -55.736  1.00 35.75  ? 76  LEU B CA  1 
ATOM   4856  C C   . LEU B  1 76  ? -10.094  18.381  -56.370  1.00 36.06  ? 76  LEU B C   1 
ATOM   4857  O O   . LEU B  1 76  ? -11.024  18.475  -57.174  1.00 38.11  ? 76  LEU B O   1 
ATOM   4858  C CB  . LEU B  1 76  ? -10.630  16.889  -54.447  1.00 36.19  ? 76  LEU B CB  1 
ATOM   4859  C CG  . LEU B  1 76  ? -10.967  15.461  -54.010  1.00 38.20  ? 76  LEU B CG  1 
ATOM   4860  C CD1 . LEU B  1 76  ? -11.896  15.550  -52.817  1.00 39.11  ? 76  LEU B CD1 1 
ATOM   4861  C CD2 . LEU B  1 76  ? -11.620  14.621  -55.094  1.00 36.99  ? 76  LEU B CD2 1 
ATOM   4862  N N   . LYS B  1 77  ? -9.331   19.424  -56.009  1.00 33.79  ? 77  LYS B N   1 
ATOM   4863  C CA  . LYS B  1 77  ? -9.574   20.742  -56.591  1.00 35.69  ? 77  LYS B CA  1 
ATOM   4864  C C   . LYS B  1 77  ? -9.426   20.662  -58.108  1.00 35.86  ? 77  LYS B C   1 
ATOM   4865  O O   . LYS B  1 77  ? -10.227  21.216  -58.853  1.00 35.36  ? 77  LYS B O   1 
ATOM   4866  C CB  . LYS B  1 77  ? -8.693   21.887  -56.060  1.00 35.32  ? 77  LYS B CB  1 
ATOM   4867  C CG  . LYS B  1 77  ? -9.130   22.414  -54.693  1.00 36.33  ? 77  LYS B CG  1 
ATOM   4868  C CD  . LYS B  1 77  ? -8.237   23.482  -54.048  1.00 37.56  ? 77  LYS B CD  1 
ATOM   4869  C CE  . LYS B  1 77  ? -8.683   23.865  -52.671  1.00 37.70  ? 77  LYS B CE  1 
ATOM   4870  N NZ  . LYS B  1 77  ? -7.626   24.488  -51.873  1.00 38.60  ? 77  LYS B NZ  1 
ATOM   4871  N N   . LEU B  1 78  ? -8.419   19.913  -58.553  1.00 36.96  ? 78  LEU B N   1 
ATOM   4872  C CA  . LEU B  1 78  ? -8.111   19.811  -59.964  1.00 37.33  ? 78  LEU B CA  1 
ATOM   4873  C C   . LEU B  1 78  ? -9.233   19.103  -60.708  1.00 34.96  ? 78  LEU B C   1 
ATOM   4874  O O   . LEU B  1 78  ? -9.675   19.583  -61.760  1.00 34.30  ? 78  LEU B O   1 
ATOM   4875  C CB  . LEU B  1 78  ? -6.787   19.068  -60.101  1.00 39.79  ? 78  LEU B CB  1 
ATOM   4876  C CG  . LEU B  1 78  ? -6.115   19.130  -61.469  1.00 41.17  ? 78  LEU B CG  1 
ATOM   4877  C CD1 . LEU B  1 78  ? -5.894   20.568  -61.931  1.00 44.99  ? 78  LEU B CD1 1 
ATOM   4878  C CD2 . LEU B  1 78  ? -4.803   18.423  -61.326  1.00 43.32  ? 78  LEU B CD2 1 
ATOM   4879  N N   . VAL B  1 79  ? -9.680   17.974  -60.138  1.00 34.35  ? 79  VAL B N   1 
ATOM   4880  C CA  . VAL B  1 79  ? -10.754  17.171  -60.710  1.00 32.58  ? 79  VAL B CA  1 
ATOM   4881  C C   . VAL B  1 79  ? -12.011  18.040  -60.784  1.00 31.77  ? 79  VAL B C   1 
ATOM   4882  O O   . VAL B  1 79  ? -12.664  18.083  -61.820  1.00 32.07  ? 79  VAL B O   1 
ATOM   4883  C CB  . VAL B  1 79  ? -11.061  15.865  -59.955  1.00 32.11  ? 79  VAL B CB  1 
ATOM   4884  C CG1 . VAL B  1 79  ? -12.122  15.032  -60.655  1.00 30.26  ? 79  VAL B CG1 1 
ATOM   4885  C CG2 . VAL B  1 79  ? -9.820   15.014  -59.749  1.00 33.95  ? 79  VAL B CG2 1 
ATOM   4886  N N   . GLN B  1 80  ? -12.359  18.709  -59.689  1.00 32.12  ? 80  GLN B N   1 
ATOM   4887  C CA  . GLN B  1 80  ? -13.512  19.592  -59.675  1.00 34.39  ? 80  GLN B CA  1 
ATOM   4888  C C   . GLN B  1 80  ? -13.466  20.579  -60.851  1.00 34.82  ? 80  GLN B C   1 
ATOM   4889  O O   . GLN B  1 80  ? -14.490  20.823  -61.504  1.00 34.26  ? 80  GLN B O   1 
ATOM   4890  C CB  . GLN B  1 80  ? -13.560  20.390  -58.368  1.00 35.52  ? 80  GLN B CB  1 
ATOM   4891  C CG  . GLN B  1 80  ? -14.843  21.192  -58.162  1.00 34.91  ? 80  GLN B CG  1 
ATOM   4892  C CD  . GLN B  1 80  ? -16.042  20.304  -57.916  1.00 34.90  ? 80  GLN B CD  1 
ATOM   4893  O OE1 . GLN B  1 80  ? -15.942  19.225  -57.341  1.00 37.12  ? 80  GLN B OE1 1 
ATOM   4894  N NE2 . GLN B  1 80  ? -17.194  20.712  -58.397  1.00 35.20  ? 80  GLN B NE2 1 
ATOM   4895  N N   . GLU B  1 81  ? -12.293  21.191  -61.086  1.00 34.73  ? 81  GLU B N   1 
ATOM   4896  C CA  . GLU B  1 81  ? -12.161  22.286  -62.052  1.00 34.98  ? 81  GLU B CA  1 
ATOM   4897  C C   . GLU B  1 81  ? -12.197  21.738  -63.481  1.00 33.00  ? 81  GLU B C   1 
ATOM   4898  O O   . GLU B  1 81  ? -12.545  22.442  -64.410  1.00 31.25  ? 81  GLU B O   1 
ATOM   4899  C CB  . GLU B  1 81  ? -10.818  23.021  -61.913  1.00 36.01  ? 81  GLU B CB  1 
ATOM   4900  C CG  . GLU B  1 81  ? -10.580  23.718  -60.571  1.00 37.50  ? 81  GLU B CG  1 
ATOM   4901  C CD  . GLU B  1 81  ? -9.097   23.915  -60.198  1.00 40.26  ? 81  GLU B CD  1 
ATOM   4902  O OE1 . GLU B  1 81  ? -8.170   23.446  -60.914  1.00 41.82  ? 81  GLU B OE1 1 
ATOM   4903  O OE2 . GLU B  1 81  ? -8.835   24.584  -59.182  1.00 42.04  ? 81  GLU B OE2 1 
ATOM   4904  N N   . SER B  1 82  ? -11.810  20.467  -63.655  1.00 31.88  ? 82  SER B N   1 
ATOM   4905  C CA  . SER B  1 82  ? -11.732  19.823  -64.955  1.00 30.79  ? 82  SER B CA  1 
ATOM   4906  C C   . SER B  1 82  ? -13.098  19.653  -65.629  1.00 30.48  ? 82  SER B C   1 
ATOM   4907  O O   . SER B  1 82  ? -13.121  19.538  -66.863  1.00 28.26  ? 82  SER B O   1 
ATOM   4908  C CB  . SER B  1 82  ? -11.082  18.457  -64.822  1.00 30.75  ? 82  SER B CB  1 
ATOM   4909  O OG  . SER B  1 82  ? -12.023  17.499  -64.355  1.00 30.94  ? 82  SER B OG  1 
ATOM   4910  N N   . GLY B  1 83  ? -14.189  19.538  -64.818  1.00 30.77  ? 83  GLY B N   1 
ATOM   4911  C CA  . GLY B  1 83  ? -15.539  19.246  -65.279  1.00 29.84  ? 83  GLY B CA  1 
ATOM   4912  C C   . GLY B  1 83  ? -15.873  17.751  -65.163  1.00 31.29  ? 83  GLY B C   1 
ATOM   4913  O O   . GLY B  1 83  ? -17.039  17.368  -65.178  1.00 29.98  ? 83  GLY B O   1 
ATOM   4914  N N   . LEU B  1 84  ? -14.844  16.889  -65.088  1.00 32.63  ? 84  LEU B N   1 
ATOM   4915  C CA  . LEU B  1 84  ? -15.030  15.439  -64.983  1.00 31.67  ? 84  LEU B CA  1 
ATOM   4916  C C   . LEU B  1 84  ? -15.693  15.094  -63.655  1.00 31.82  ? 84  LEU B C   1 
ATOM   4917  O O   . LEU B  1 84  ? -15.413  15.747  -62.655  1.00 31.10  ? 84  LEU B O   1 
ATOM   4918  C CB  . LEU B  1 84  ? -13.704  14.695  -65.087  1.00 30.70  ? 84  LEU B CB  1 
ATOM   4919  C CG  . LEU B  1 84  ? -13.035  14.686  -66.466  1.00 33.21  ? 84  LEU B CG  1 
ATOM   4920  C CD1 . LEU B  1 84  ? -11.544  14.241  -66.465  1.00 31.82  ? 84  LEU B CD1 1 
ATOM   4921  C CD2 . LEU B  1 84  ? -13.852  13.823  -67.423  1.00 31.43  ? 84  LEU B CD2 1 
ATOM   4922  N N   . LYS B  1 85  ? -16.562  14.064  -63.665  1.00 30.75  ? 85  LYS B N   1 
ATOM   4923  C CA  . LYS B  1 85  ? -17.084  13.511  -62.437  1.00 29.58  ? 85  LYS B CA  1 
ATOM   4924  C C   . LYS B  1 85  ? -16.070  12.498  -61.940  1.00 30.60  ? 85  LYS B C   1 
ATOM   4925  O O   . LYS B  1 85  ? -15.180  12.091  -62.706  1.00 29.53  ? 85  LYS B O   1 
ATOM   4926  C CB  . LYS B  1 85  ? -18.460  12.869  -62.595  1.00 29.91  ? 85  LYS B CB  1 
ATOM   4927  C CG  . LYS B  1 85  ? -19.520  13.703  -63.280  1.00 31.57  ? 85  LYS B CG  1 
ATOM   4928  C CD  . LYS B  1 85  ? -19.746  15.076  -62.627  1.00 31.85  ? 85  LYS B CD  1 
ATOM   4929  C CE  . LYS B  1 85  ? -20.674  15.988  -63.404  1.00 31.35  ? 85  LYS B CE  1 
ATOM   4930  N NZ  . LYS B  1 85  ? -21.021  17.156  -62.587  1.00 30.88  ? 85  LYS B NZ  1 
ATOM   4931  N N   . LEU B  1 86  ? -16.271  12.074  -60.677  1.00 30.25  ? 86  LEU B N   1 
ATOM   4932  C CA  . LEU B  1 86  ? -15.353  11.182  -59.992  1.00 29.06  ? 86  LEU B CA  1 
ATOM   4933  C C   . LEU B  1 86  ? -16.124  10.085  -59.253  1.00 28.24  ? 86  LEU B C   1 
ATOM   4934  O O   . LEU B  1 86  ? -17.003  10.398  -58.464  1.00 27.15  ? 86  LEU B O   1 
ATOM   4935  C CB  . LEU B  1 86  ? -14.510  12.021  -59.037  1.00 29.70  ? 86  LEU B CB  1 
ATOM   4936  C CG  . LEU B  1 86  ? -13.526  11.255  -58.132  1.00 29.55  ? 86  LEU B CG  1 
ATOM   4937  C CD1 . LEU B  1 86  ? -12.585  10.293  -58.820  1.00 27.97  ? 86  LEU B CD1 1 
ATOM   4938  C CD2 . LEU B  1 86  ? -12.691  12.284  -57.366  1.00 30.29  ? 86  LEU B CD2 1 
ATOM   4939  N N   . ILE B  1 87  ? -15.793  8.820   -59.556  1.00 25.47  ? 87  ILE B N   1 
ATOM   4940  C CA  . ILE B  1 87  ? -16.097  7.691   -58.698  1.00 26.64  ? 87  ILE B CA  1 
ATOM   4941  C C   . ILE B  1 87  ? -14.831  7.399   -57.900  1.00 26.58  ? 87  ILE B C   1 
ATOM   4942  O O   . ILE B  1 87  ? -13.881  6.893   -58.485  1.00 26.56  ? 87  ILE B O   1 
ATOM   4943  C CB  . ILE B  1 87  ? -16.540  6.471   -59.550  1.00 27.77  ? 87  ILE B CB  1 
ATOM   4944  C CG1 . ILE B  1 87  ? -17.847  6.761   -60.273  1.00 27.90  ? 87  ILE B CG1 1 
ATOM   4945  C CG2 . ILE B  1 87  ? -16.682  5.198   -58.715  1.00 29.39  ? 87  ILE B CG2 1 
ATOM   4946  C CD1 . ILE B  1 87  ? -18.174  5.806   -61.403  1.00 27.80  ? 87  ILE B CD1 1 
ATOM   4947  N N   . MET B  1 88  ? -14.821  7.704   -56.597  1.00 26.65  ? 88  MET B N   1 
ATOM   4948  C CA  . MET B  1 88  ? -13.598  7.685   -55.811  1.00 28.28  ? 88  MET B CA  1 
ATOM   4949  C C   . MET B  1 88  ? -13.513  6.410   -54.965  1.00 30.28  ? 88  MET B C   1 
ATOM   4950  O O   . MET B  1 88  ? -14.388  6.107   -54.162  1.00 30.64  ? 88  MET B O   1 
ATOM   4951  C CB  . MET B  1 88  ? -13.497  8.899   -54.884  1.00 28.91  ? 88  MET B CB  1 
ATOM   4952  C CG  . MET B  1 88  ? -12.214  8.940   -54.081  1.00 31.28  ? 88  MET B CG  1 
ATOM   4953  S SD  . MET B  1 88  ? -11.697  10.562  -53.460  1.00 33.79  ? 88  MET B SD  1 
ATOM   4954  C CE  . MET B  1 88  ? -13.000  10.916  -52.273  1.00 34.42  ? 88  MET B CE  1 
ATOM   4955  N N   . GLY B  1 89  ? -12.433  5.650   -55.149  1.00 31.92  ? 89  GLY B N   1 
ATOM   4956  C CA  . GLY B  1 89  ? -12.184  4.461   -54.353  1.00 31.75  ? 89  GLY B CA  1 
ATOM   4957  C C   . GLY B  1 89  ? -11.441  4.821   -53.072  1.00 30.45  ? 89  GLY B C   1 
ATOM   4958  O O   . GLY B  1 89  ? -10.595  5.713   -53.088  1.00 32.03  ? 89  GLY B O   1 
ATOM   4959  N N   . ILE B  1 90  ? -11.822  4.159   -51.977  1.00 29.10  ? 90  ILE B N   1 
ATOM   4960  C CA  . ILE B  1 90  ? -11.155  4.293   -50.704  1.00 30.68  ? 90  ILE B CA  1 
ATOM   4961  C C   . ILE B  1 90  ? -10.248  3.086   -50.516  1.00 32.40  ? 90  ILE B C   1 
ATOM   4962  O O   . ILE B  1 90  ? -10.621  1.979   -50.872  1.00 34.96  ? 90  ILE B O   1 
ATOM   4963  C CB  . ILE B  1 90  ? -12.169  4.426   -49.563  1.00 31.07  ? 90  ILE B CB  1 
ATOM   4964  C CG1 . ILE B  1 90  ? -13.183  5.543   -49.852  1.00 33.60  ? 90  ILE B CG1 1 
ATOM   4965  C CG2 . ILE B  1 90  ? -11.454  4.648   -48.229  1.00 31.10  ? 90  ILE B CG2 1 
ATOM   4966  C CD1 . ILE B  1 90  ? -12.580  6.931   -50.037  1.00 33.06  ? 90  ILE B CD1 1 
ATOM   4967  N N   . ASP B  1 91  ? -9.086   3.312   -49.916  1.00 33.75  ? 91  ASP B N   1 
ATOM   4968  C CA  . ASP B  1 91  ? -8.046   2.312   -49.796  1.00 38.47  ? 91  ASP B CA  1 
ATOM   4969  C C   . ASP B  1 91  ? -8.211   1.513   -48.500  1.00 39.53  ? 91  ASP B C   1 
ATOM   4970  O O   . ASP B  1 91  ? -7.340   1.526   -47.644  1.00 40.93  ? 91  ASP B O   1 
ATOM   4971  C CB  . ASP B  1 91  ? -6.700   3.009   -49.826  1.00 42.18  ? 91  ASP B CB  1 
ATOM   4972  C CG  . ASP B  1 91  ? -5.493   2.087   -49.793  1.00 49.35  ? 91  ASP B CG  1 
ATOM   4973  O OD1 . ASP B  1 91  ? -5.694   0.835   -49.772  1.00 47.98  ? 91  ASP B OD1 1 
ATOM   4974  O OD2 . ASP B  1 91  ? -4.367   2.648   -49.784  1.00 54.79  ? 91  ASP B OD2 1 
ATOM   4975  N N   . ILE B  1 92  ? -9.345   0.842   -48.325  1.00 38.95  ? 92  ILE B N   1 
ATOM   4976  C CA  . ILE B  1 92  ? -9.506   -0.044  -47.194  1.00 41.57  ? 92  ILE B CA  1 
ATOM   4977  C C   . ILE B  1 92  ? -8.798   -1.334  -47.589  1.00 41.93  ? 92  ILE B C   1 
ATOM   4978  O O   . ILE B  1 92  ? -9.188   -1.963  -48.563  1.00 45.35  ? 92  ILE B O   1 
ATOM   4979  C CB  . ILE B  1 92  ? -11.001  -0.219  -46.895  1.00 44.07  ? 92  ILE B CB  1 
ATOM   4980  C CG1 . ILE B  1 92  ? -11.678  1.122   -46.565  1.00 44.64  ? 92  ILE B CG1 1 
ATOM   4981  C CG2 . ILE B  1 92  ? -11.246  -1.239  -45.791  1.00 47.38  ? 92  ILE B CG2 1 
ATOM   4982  C CD1 . ILE B  1 92  ? -11.045  1.882   -45.411  1.00 44.96  ? 92  ILE B CD1 1 
ATOM   4983  N N   . LYS B  1 93  ? -7.682   -1.638  -46.922  1.00 46.97  ? 93  LYS B N   1 
ATOM   4984  C CA  . LYS B  1 93  ? -6.818   -2.766  -47.266  1.00 50.89  ? 93  LYS B CA  1 
ATOM   4985  C C   . LYS B  1 93  ? -7.623   -4.068  -47.290  1.00 47.78  ? 93  LYS B C   1 
ATOM   4986  O O   . LYS B  1 93  ? -8.156   -4.476  -46.261  1.00 52.32  ? 93  LYS B O   1 
ATOM   4987  C CB  . LYS B  1 93  ? -5.688   -2.820  -46.223  1.00 61.54  ? 93  LYS B CB  1 
ATOM   4988  C CG  . LYS B  1 93  ? -4.460   -1.903  -46.433  1.00 70.72  ? 93  LYS B CG  1 
ATOM   4989  C CD  . LYS B  1 93  ? -3.252   -2.568  -47.101  1.00 77.08  ? 93  LYS B CD  1 
ATOM   4990  C CE  . LYS B  1 93  ? -2.048   -1.692  -47.322  1.00 80.22  ? 93  LYS B CE  1 
ATOM   4991  N NZ  . LYS B  1 93  ? -2.265   -0.745  -48.428  1.00 84.71  ? 93  LYS B NZ  1 
ATOM   4992  N N   . PRO B  1 94  ? -7.797   -4.738  -48.451  1.00 43.53  ? 94  PRO B N   1 
ATOM   4993  C CA  . PRO B  1 94  ? -8.605   -5.968  -48.534  1.00 44.47  ? 94  PRO B CA  1 
ATOM   4994  C C   . PRO B  1 94  ? -8.208   -7.222  -47.749  1.00 44.42  ? 94  PRO B C   1 
ATOM   4995  O O   . PRO B  1 94  ? -9.073   -8.064  -47.506  1.00 38.82  ? 94  PRO B O   1 
ATOM   4996  C CB  . PRO B  1 94  ? -8.644   -6.309  -50.047  1.00 43.44  ? 94  PRO B CB  1 
ATOM   4997  C CG  . PRO B  1 94  ? -7.487   -5.539  -50.640  1.00 45.05  ? 94  PRO B CG  1 
ATOM   4998  C CD  . PRO B  1 94  ? -7.303   -4.293  -49.762  1.00 43.88  ? 94  PRO B CD  1 
ATOM   4999  N N   . GLU B  1 95  ? -6.917   -7.353  -47.388  1.00 45.45  ? 95  GLU B N   1 
ATOM   5000  C CA  . GLU B  1 95  ? -6.410   -8.570  -46.748  1.00 46.47  ? 95  GLU B CA  1 
ATOM   5001  C C   . GLU B  1 95  ? -6.425   -8.415  -45.227  1.00 44.16  ? 95  GLU B C   1 
ATOM   5002  O O   . GLU B  1 95  ? -6.080   -9.344  -44.498  1.00 40.70  ? 95  GLU B O   1 
ATOM   5003  C CB  . GLU B  1 95  ? -5.011   -8.969  -47.224  1.00 49.76  ? 95  GLU B CB  1 
ATOM   5004  C CG  . GLU B  1 95  ? -4.971   -9.405  -48.688  1.00 56.00  ? 95  GLU B CG  1 
ATOM   5005  C CD  . GLU B  1 95  ? -4.815   -8.280  -49.714  1.00 68.50  ? 95  GLU B CD  1 
ATOM   5006  O OE1 . GLU B  1 95  ? -4.313   -7.174  -49.343  1.00 64.56  ? 95  GLU B OE1 1 
ATOM   5007  O OE2 . GLU B  1 95  ? -5.229   -8.503  -50.891  1.00 67.29  ? 95  GLU B OE2 1 
ATOM   5008  N N   . GLU B  1 96  ? -6.887   -7.255  -44.742  1.00 42.47  ? 96  GLU B N   1 
ATOM   5009  C CA  . GLU B  1 96  ? -6.898   -7.014  -43.310  1.00 44.30  ? 96  GLU B CA  1 
ATOM   5010  C C   . GLU B  1 96  ? -8.085   -7.724  -42.661  1.00 40.45  ? 96  GLU B C   1 
ATOM   5011  O O   . GLU B  1 96  ? -9.049   -8.093  -43.326  1.00 41.09  ? 96  GLU B O   1 
ATOM   5012  C CB  . GLU B  1 96  ? -6.925   -5.510  -43.031  1.00 47.96  ? 96  GLU B CB  1 
ATOM   5013  C CG  . GLU B  1 96  ? -5.572   -4.838  -43.264  1.00 51.20  ? 96  GLU B CG  1 
ATOM   5014  C CD  . GLU B  1 96  ? -4.458   -5.379  -42.384  1.00 54.52  ? 96  GLU B CD  1 
ATOM   5015  O OE1 . GLU B  1 96  ? -4.389   -5.079  -41.163  1.00 59.28  ? 96  GLU B OE1 1 
ATOM   5016  O OE2 . GLU B  1 96  ? -3.670   -6.160  -42.958  1.00 54.42  ? 96  GLU B OE2 1 
ATOM   5017  N N   . ASP B  1 97  ? -7.995   -7.899  -41.342  1.00 37.89  ? 97  ASP B N   1 
ATOM   5018  C CA  . ASP B  1 97  ? -9.037   -8.547  -40.585  1.00 37.45  ? 97  ASP B CA  1 
ATOM   5019  C C   . ASP B  1 97  ? -10.158  -7.530  -40.351  1.00 35.74  ? 97  ASP B C   1 
ATOM   5020  O O   . ASP B  1 97  ? -10.056  -6.675  -39.480  1.00 35.03  ? 97  ASP B O   1 
ATOM   5021  C CB  . ASP B  1 97  ? -8.506   -9.163  -39.299  1.00 37.57  ? 97  ASP B CB  1 
ATOM   5022  C CG  . ASP B  1 97  ? -9.583   -9.764  -38.404  1.00 38.68  ? 97  ASP B CG  1 
ATOM   5023  O OD1 . ASP B  1 97  ? -10.791  -9.747  -38.792  1.00 37.87  ? 97  ASP B OD1 1 
ATOM   5024  O OD2 . ASP B  1 97  ? -9.225   -10.190 -37.293  1.00 41.61  ? 97  ASP B OD2 1 
ATOM   5025  N N   . TYR B  1 98  ? -11.248  -7.694  -41.101  1.00 34.56  ? 98  TYR B N   1 
ATOM   5026  C CA  . TYR B  1 98  ? -12.367  -6.773  -41.078  1.00 35.76  ? 98  TYR B CA  1 
ATOM   5027  C C   . TYR B  1 98  ? -13.004  -6.733  -39.698  1.00 35.84  ? 98  TYR B C   1 
ATOM   5028  O O   . TYR B  1 98  ? -13.654  -5.754  -39.362  1.00 37.70  ? 98  TYR B O   1 
ATOM   5029  C CB  . TYR B  1 98  ? -13.426  -7.200  -42.100  1.00 36.04  ? 98  TYR B CB  1 
ATOM   5030  C CG  . TYR B  1 98  ? -12.953  -7.428  -43.532  1.00 35.67  ? 98  TYR B CG  1 
ATOM   5031  C CD1 . TYR B  1 98  ? -11.932  -6.660  -44.075  1.00 36.63  ? 98  TYR B CD1 1 
ATOM   5032  C CD2 . TYR B  1 98  ? -13.566  -8.368  -44.353  1.00 33.99  ? 98  TYR B CD2 1 
ATOM   5033  C CE1 . TYR B  1 98  ? -11.510  -6.849  -45.380  1.00 36.72  ? 98  TYR B CE1 1 
ATOM   5034  C CE2 . TYR B  1 98  ? -13.135  -8.581  -45.652  1.00 34.21  ? 98  TYR B CE2 1 
ATOM   5035  C CZ  . TYR B  1 98  ? -12.100  -7.821  -46.175  1.00 35.14  ? 98  TYR B CZ  1 
ATOM   5036  O OH  . TYR B  1 98  ? -11.667  -7.949  -47.484  1.00 32.98  ? 98  TYR B OH  1 
ATOM   5037  N N   . GLY B  1 99  ? -12.854  -7.828  -38.946  1.00 37.52  ? 99  GLY B N   1 
ATOM   5038  C CA  . GLY B  1 99  ? -13.484  -7.982  -37.647  1.00 37.09  ? 99  GLY B CA  1 
ATOM   5039  C C   . GLY B  1 99  ? -12.581  -7.503  -36.517  1.00 38.04  ? 99  GLY B C   1 
ATOM   5040  O O   . GLY B  1 99  ? -13.028  -7.429  -35.387  1.00 38.39  ? 99  GLY B O   1 
ATOM   5041  N N   . ASP B  1 100 ? -11.328  -7.142  -36.826  1.00 40.05  ? 100 ASP B N   1 
ATOM   5042  C CA  . ASP B  1 100 ? -10.409  -6.565  -35.843  1.00 42.73  ? 100 ASP B CA  1 
ATOM   5043  C C   . ASP B  1 100 ? -10.834  -5.133  -35.542  1.00 40.09  ? 100 ASP B C   1 
ATOM   5044  O O   . ASP B  1 100 ? -10.869  -4.303  -36.436  1.00 38.80  ? 100 ASP B O   1 
ATOM   5045  C CB  . ASP B  1 100 ? -8.955   -6.630  -36.304  1.00 45.86  ? 100 ASP B CB  1 
ATOM   5046  C CG  . ASP B  1 100 ? -7.884   -6.082  -35.368  1.00 49.53  ? 100 ASP B CG  1 
ATOM   5047  O OD1 . ASP B  1 100 ? -8.210   -5.569  -34.271  1.00 47.98  ? 100 ASP B OD1 1 
ATOM   5048  O OD2 . ASP B  1 100 ? -6.707   -6.159  -35.769  1.00 58.30  ? 100 ASP B OD2 1 
ATOM   5049  N N   . PRO B  1 101 ? -11.237  -4.824  -34.293  1.00 39.67  ? 101 PRO B N   1 
ATOM   5050  C CA  . PRO B  1 101 ? -11.775  -3.502  -33.971  1.00 40.85  ? 101 PRO B CA  1 
ATOM   5051  C C   . PRO B  1 101 ? -10.820  -2.327  -34.154  1.00 42.82  ? 101 PRO B C   1 
ATOM   5052  O O   . PRO B  1 101 ? -11.302  -1.213  -34.376  1.00 44.74  ? 101 PRO B O   1 
ATOM   5053  C CB  . PRO B  1 101 ? -12.289  -3.586  -32.538  1.00 40.66  ? 101 PRO B CB  1 
ATOM   5054  C CG  . PRO B  1 101 ? -12.008  -5.011  -32.086  1.00 41.00  ? 101 PRO B CG  1 
ATOM   5055  C CD  . PRO B  1 101 ? -11.336  -5.777  -33.186  1.00 39.38  ? 101 PRO B CD  1 
ATOM   5056  N N   . GLU B  1 102 ? -9.503   -2.583  -34.063  1.00 43.86  ? 102 GLU B N   1 
ATOM   5057  C CA  . GLU B  1 102 ? -8.491   -1.556  -34.302  1.00 44.53  ? 102 GLU B CA  1 
ATOM   5058  C C   . GLU B  1 102 ? -8.478   -1.207  -35.781  1.00 40.13  ? 102 GLU B C   1 
ATOM   5059  O O   . GLU B  1 102 ? -8.398   -0.041  -36.132  1.00 42.04  ? 102 GLU B O   1 
ATOM   5060  C CB  . GLU B  1 102 ? -7.076   -1.935  -33.840  1.00 48.32  ? 102 GLU B CB  1 
ATOM   5061  C CG  . GLU B  1 102 ? -6.110   -0.751  -33.770  1.00 52.69  ? 102 GLU B CG  1 
ATOM   5062  C CD  . GLU B  1 102 ? -6.413   0.396   -32.787  1.00 56.56  ? 102 GLU B CD  1 
ATOM   5063  O OE1 . GLU B  1 102 ? -6.653   0.129   -31.571  1.00 59.50  ? 102 GLU B OE1 1 
ATOM   5064  O OE2 . GLU B  1 102 ? -6.352   1.575   -33.232  1.00 53.18  ? 102 GLU B OE2 1 
ATOM   5065  N N   . PHE B  1 103 ? -8.598   -2.221  -36.635  1.00 38.81  ? 103 PHE B N   1 
ATOM   5066  C CA  . PHE B  1 103 ? -8.705   -2.019  -38.068  1.00 38.07  ? 103 PHE B CA  1 
ATOM   5067  C C   . PHE B  1 103 ? -9.967   -1.203  -38.414  1.00 40.58  ? 103 PHE B C   1 
ATOM   5068  O O   . PHE B  1 103 ? -9.900   -0.308  -39.260  1.00 42.18  ? 103 PHE B O   1 
ATOM   5069  C CB  . PHE B  1 103 ? -8.668   -3.373  -38.780  1.00 36.29  ? 103 PHE B CB  1 
ATOM   5070  C CG  . PHE B  1 103 ? -8.837   -3.185  -40.272  1.00 35.69  ? 103 PHE B CG  1 
ATOM   5071  C CD1 . PHE B  1 103 ? -7.830   -2.571  -41.017  1.00 35.40  ? 103 PHE B CD1 1 
ATOM   5072  C CD2 . PHE B  1 103 ? -10.045  -3.496  -40.891  1.00 35.32  ? 103 PHE B CD2 1 
ATOM   5073  C CE1 . PHE B  1 103 ? -8.000   -2.329  -42.372  1.00 34.88  ? 103 PHE B CE1 1 
ATOM   5074  C CE2 . PHE B  1 103 ? -10.217  -3.263  -42.250  1.00 35.35  ? 103 PHE B CE2 1 
ATOM   5075  C CZ  . PHE B  1 103 ? -9.190   -2.699  -42.993  1.00 35.45  ? 103 PHE B CZ  1 
ATOM   5076  N N   . VAL B  1 104 ? -11.122  -1.498  -37.786  1.00 38.80  ? 104 VAL B N   1 
ATOM   5077  C CA  . VAL B  1 104 ? -12.344  -0.746  -38.042  1.00 37.66  ? 104 VAL B CA  1 
ATOM   5078  C C   . VAL B  1 104 ? -12.090  0.724   -37.668  1.00 39.55  ? 104 VAL B C   1 
ATOM   5079  O O   . VAL B  1 104 ? -12.243  1.636   -38.487  1.00 38.12  ? 104 VAL B O   1 
ATOM   5080  C CB  . VAL B  1 104 ? -13.579  -1.363  -37.326  1.00 37.80  ? 104 VAL B CB  1 
ATOM   5081  C CG1 . VAL B  1 104 ? -14.826  -0.500  -37.483  1.00 37.53  ? 104 VAL B CG1 1 
ATOM   5082  C CG2 . VAL B  1 104 ? -13.911  -2.801  -37.790  1.00 36.48  ? 104 VAL B CG2 1 
ATOM   5083  N N   . LYS B  1 105 ? -11.643  0.953   -36.426  1.00 42.49  ? 105 LYS B N   1 
ATOM   5084  C CA  . LYS B  1 105 ? -11.268  2.273   -35.947  1.00 42.75  ? 105 LYS B CA  1 
ATOM   5085  C C   . LYS B  1 105 ? -10.359  2.997   -36.944  1.00 40.08  ? 105 LYS B C   1 
ATOM   5086  O O   . LYS B  1 105 ? -10.705  4.081   -37.343  1.00 38.42  ? 105 LYS B O   1 
ATOM   5087  C CB  . LYS B  1 105 ? -10.581  2.181   -34.581  1.00 44.76  ? 105 LYS B CB  1 
ATOM   5088  C CG  . LYS B  1 105 ? -10.272  3.536   -33.963  1.00 46.41  ? 105 LYS B CG  1 
ATOM   5089  C CD  . LYS B  1 105 ? -9.529   3.476   -32.630  1.00 49.97  ? 105 LYS B CD  1 
ATOM   5090  C CE  . LYS B  1 105 ? -9.261   4.792   -31.939  1.00 49.97  ? 105 LYS B CE  1 
ATOM   5091  N NZ  . LYS B  1 105 ? -8.837   4.557   -30.553  1.00 52.18  ? 105 LYS B NZ  1 
ATOM   5092  N N   . ASP B  1 106 ? -9.233   2.406   -37.381  1.00 39.59  ? 106 ASP B N   1 
ATOM   5093  C CA  . ASP B  1 106 ? -8.302   3.131   -38.238  1.00 40.69  ? 106 ASP B CA  1 
ATOM   5094  C C   . ASP B  1 106 ? -8.967   3.428   -39.565  1.00 38.28  ? 106 ASP B C   1 
ATOM   5095  O O   . ASP B  1 106 ? -8.737   4.476   -40.150  1.00 38.57  ? 106 ASP B O   1 
ATOM   5096  C CB  . ASP B  1 106 ? -6.967   2.421   -38.460  1.00 43.00  ? 106 ASP B CB  1 
ATOM   5097  C CG  . ASP B  1 106 ? -6.158   2.190   -37.185  1.00 44.41  ? 106 ASP B CG  1 
ATOM   5098  O OD1 . ASP B  1 106 ? -6.407   2.911   -36.202  1.00 44.49  ? 106 ASP B OD1 1 
ATOM   5099  O OD2 . ASP B  1 106 ? -5.357   1.236   -37.146  1.00 45.07  ? 106 ASP B OD2 1 
ATOM   5100  N N   . SER B  1 107 ? -9.800   2.502   -40.027  1.00 37.65  ? 107 SER B N   1 
ATOM   5101  C CA  . SER B  1 107 ? -10.507  2.675   -41.281  1.00 35.67  ? 107 SER B CA  1 
ATOM   5102  C C   . SER B  1 107 ? -11.463  3.864   -41.189  1.00 36.55  ? 107 SER B C   1 
ATOM   5103  O O   . SER B  1 107 ? -11.592  4.616   -42.154  1.00 34.79  ? 107 SER B O   1 
ATOM   5104  C CB  . SER B  1 107 ? -11.204  1.400   -41.685  1.00 34.48  ? 107 SER B CB  1 
ATOM   5105  O OG  . SER B  1 107 ? -10.272  0.388   -42.092  1.00 33.60  ? 107 SER B OG  1 
ATOM   5106  N N   . GLU B  1 108 ? -12.117  4.021   -40.025  1.00 38.26  ? 108 GLU B N   1 
ATOM   5107  C CA  . GLU B  1 108 ? -13.129  5.055   -39.794  1.00 38.89  ? 108 GLU B CA  1 
ATOM   5108  C C   . GLU B  1 108 ? -12.490  6.447   -39.713  1.00 38.90  ? 108 GLU B C   1 
ATOM   5109  O O   . GLU B  1 108 ? -13.066  7.429   -40.193  1.00 37.29  ? 108 GLU B O   1 
ATOM   5110  C CB  . GLU B  1 108 ? -13.921  4.797   -38.505  1.00 40.14  ? 108 GLU B CB  1 
ATOM   5111  C CG  . GLU B  1 108 ? -14.798  3.546   -38.554  1.00 42.67  ? 108 GLU B CG  1 
ATOM   5112  C CD  . GLU B  1 108 ? -15.517  3.198   -37.264  1.00 46.51  ? 108 GLU B CD  1 
ATOM   5113  O OE1 . GLU B  1 108 ? -14.860  3.315   -36.237  1.00 52.14  ? 108 GLU B OE1 1 
ATOM   5114  O OE2 . GLU B  1 108 ? -16.680  2.772   -37.250  1.00 49.81  ? 108 GLU B OE2 1 
ATOM   5115  N N   . ILE B  1 109 ? -11.321  6.514   -39.049  1.00 38.37  ? 109 ILE B N   1 
ATOM   5116  C CA  . ILE B  1 109 ? -10.571  7.743   -38.846  1.00 37.36  ? 109 ILE B CA  1 
ATOM   5117  C C   . ILE B  1 109 ? -10.090  8.266   -40.194  1.00 36.29  ? 109 ILE B C   1 
ATOM   5118  O O   . ILE B  1 109 ? -10.194  9.450   -40.481  1.00 38.17  ? 109 ILE B O   1 
ATOM   5119  C CB  . ILE B  1 109 ? -9.416   7.456   -37.884  1.00 38.54  ? 109 ILE B CB  1 
ATOM   5120  C CG1 . ILE B  1 109 ? -9.951   7.221   -36.475  1.00 38.65  ? 109 ILE B CG1 1 
ATOM   5121  C CG2 . ILE B  1 109 ? -8.347   8.555   -37.948  1.00 38.65  ? 109 ILE B CG2 1 
ATOM   5122  C CD1 . ILE B  1 109 ? -8.876   6.841   -35.466  1.00 39.50  ? 109 ILE B CD1 1 
ATOM   5123  N N   . GLU B  1 110 ? -9.677   7.339   -41.056  1.00 34.90  ? 110 GLU B N   1 
ATOM   5124  C CA  . GLU B  1 110 ? -9.135   7.668   -42.357  1.00 33.90  ? 110 GLU B CA  1 
ATOM   5125  C C   . GLU B  1 110 ? -10.270  8.133   -43.270  1.00 32.59  ? 110 GLU B C   1 
ATOM   5126  O O   . GLU B  1 110 ? -10.144  9.150   -43.957  1.00 31.23  ? 110 GLU B O   1 
ATOM   5127  C CB  . GLU B  1 110 ? -8.305   6.499   -42.898  1.00 33.59  ? 110 GLU B CB  1 
ATOM   5128  C CG  . GLU B  1 110 ? -7.656   6.777   -44.254  1.00 34.96  ? 110 GLU B CG  1 
ATOM   5129  C CD  . GLU B  1 110 ? -6.872   8.084   -44.435  1.00 38.27  ? 110 GLU B CD  1 
ATOM   5130  O OE1 . GLU B  1 110 ? -6.422   8.756   -43.457  1.00 40.94  ? 110 GLU B OE1 1 
ATOM   5131  O OE2 . GLU B  1 110 ? -6.739   8.472   -45.611  1.00 38.15  ? 110 GLU B OE2 1 
ATOM   5132  N N   . LEU B  1 111 ? -11.378  7.396   -43.288  1.00 31.18  ? 111 LEU B N   1 
ATOM   5133  C CA  . LEU B  1 111 ? -12.515  7.803   -44.108  1.00 31.65  ? 111 LEU B CA  1 
ATOM   5134  C C   . LEU B  1 111 ? -13.059  9.148   -43.635  1.00 31.76  ? 111 LEU B C   1 
ATOM   5135  O O   . LEU B  1 111 ? -13.371  9.997   -44.442  1.00 31.83  ? 111 LEU B O   1 
ATOM   5136  C CB  . LEU B  1 111 ? -13.579  6.714   -44.059  1.00 32.79  ? 111 LEU B CB  1 
ATOM   5137  C CG  . LEU B  1 111 ? -14.815  6.864   -44.934  1.00 31.89  ? 111 LEU B CG  1 
ATOM   5138  C CD1 . LEU B  1 111 ? -14.429  6.977   -46.367  1.00 32.48  ? 111 LEU B CD1 1 
ATOM   5139  C CD2 . LEU B  1 111 ? -15.657  5.633   -44.693  1.00 32.67  ? 111 LEU B CD2 1 
ATOM   5140  N N   . LYS B  1 112 ? -13.137  9.376   -42.330  1.00 33.39  ? 112 LYS B N   1 
ATOM   5141  C CA  . LYS B  1 112 ? -13.655  10.643  -41.841  1.00 35.38  ? 112 LYS B CA  1 
ATOM   5142  C C   . LYS B  1 112 ? -12.777  11.811  -42.303  1.00 35.90  ? 112 LYS B C   1 
ATOM   5143  O O   . LYS B  1 112 ? -13.305  12.836  -42.738  1.00 33.94  ? 112 LYS B O   1 
ATOM   5144  C CB  . LYS B  1 112 ? -13.832  10.614  -40.319  1.00 37.41  ? 112 LYS B CB  1 
ATOM   5145  C CG  . LYS B  1 112 ? -15.122  9.945   -39.888  1.00 38.86  ? 112 LYS B CG  1 
ATOM   5146  C CD  . LYS B  1 112 ? -15.489  10.023  -38.404  1.00 41.80  ? 112 LYS B CD  1 
ATOM   5147  C CE  . LYS B  1 112 ? -16.622  9.050   -38.097  1.00 43.45  ? 112 LYS B CE  1 
ATOM   5148  N NZ  . LYS B  1 112 ? -16.699  8.717   -36.673  1.00 45.52  ? 112 LYS B NZ  1 
ATOM   5149  N N   . ARG B  1 113 ? -11.444  11.636  -42.214  1.00 38.26  ? 113 ARG B N   1 
ATOM   5150  C CA  . ARG B  1 113 ? -10.486  12.682  -42.568  1.00 39.42  ? 113 ARG B CA  1 
ATOM   5151  C C   . ARG B  1 113 ? -10.667  13.084  -44.037  1.00 38.50  ? 113 ARG B C   1 
ATOM   5152  O O   . ARG B  1 113 ? -10.647  14.272  -44.359  1.00 36.59  ? 113 ARG B O   1 
ATOM   5153  C CB  . ARG B  1 113 ? -9.054   12.207  -42.295  1.00 39.84  ? 113 ARG B CB  1 
ATOM   5154  C CG  . ARG B  1 113 ? -7.993   13.235  -42.648  1.00 41.04  ? 113 ARG B CG  1 
ATOM   5155  C CD  . ARG B  1 113 ? -6.600   12.623  -42.687  1.00 42.68  ? 113 ARG B CD  1 
ATOM   5156  N NE  . ARG B  1 113 ? -6.450   11.724  -43.833  1.00 42.15  ? 113 ARG B NE  1 
ATOM   5157  C CZ  . ARG B  1 113 ? -6.147   12.082  -45.075  1.00 41.56  ? 113 ARG B CZ  1 
ATOM   5158  N NH1 . ARG B  1 113 ? -5.918   13.349  -45.362  1.00 43.59  ? 113 ARG B NH1 1 
ATOM   5159  N NH2 . ARG B  1 113 ? -6.045   11.167  -46.023  1.00 39.29  ? 113 ARG B NH2 1 
ATOM   5160  N N   . VAL B  1 114 ? -10.879  12.084  -44.906  1.00 37.57  ? 114 VAL B N   1 
ATOM   5161  C CA  . VAL B  1 114 ? -11.142  12.322  -46.317  1.00 38.07  ? 114 VAL B CA  1 
ATOM   5162  C C   . VAL B  1 114 ? -12.463  13.080  -46.482  1.00 38.13  ? 114 VAL B C   1 
ATOM   5163  O O   . VAL B  1 114 ? -12.513  14.138  -47.127  1.00 38.78  ? 114 VAL B O   1 
ATOM   5164  C CB  . VAL B  1 114 ? -11.162  11.023  -47.146  1.00 36.99  ? 114 VAL B CB  1 
ATOM   5165  C CG1 . VAL B  1 114 ? -11.558  11.285  -48.596  1.00 37.37  ? 114 VAL B CG1 1 
ATOM   5166  C CG2 . VAL B  1 114 ? -9.815   10.318  -47.149  1.00 38.56  ? 114 VAL B CG2 1 
ATOM   5167  N N   . LEU B  1 115 ? -13.527  12.534  -45.883  1.00 35.78  ? 115 LEU B N   1 
ATOM   5168  C CA  . LEU B  1 115 ? -14.853  13.100  -46.059  1.00 34.54  ? 115 LEU B CA  1 
ATOM   5169  C C   . LEU B  1 115 ? -14.833  14.564  -45.652  1.00 35.15  ? 115 LEU B C   1 
ATOM   5170  O O   . LEU B  1 115 ? -15.501  15.387  -46.270  1.00 35.08  ? 115 LEU B O   1 
ATOM   5171  C CB  . LEU B  1 115 ? -15.921  12.304  -45.320  1.00 33.46  ? 115 LEU B CB  1 
ATOM   5172  C CG  . LEU B  1 115 ? -16.090  10.854  -45.803  1.00 34.27  ? 115 LEU B CG  1 
ATOM   5173  C CD1 . LEU B  1 115 ? -17.045  10.052  -44.920  1.00 35.78  ? 115 LEU B CD1 1 
ATOM   5174  C CD2 . LEU B  1 115 ? -16.532  10.721  -47.243  1.00 32.33  ? 115 LEU B CD2 1 
ATOM   5175  N N   . ASN B  1 116 ? -14.022  14.884  -44.650  1.00 36.32  ? 116 ASN B N   1 
ATOM   5176  C CA  . ASN B  1 116 ? -14.031  16.205  -44.059  1.00 38.01  ? 116 ASN B CA  1 
ATOM   5177  C C   . ASN B  1 116 ? -13.802  17.290  -45.117  1.00 38.36  ? 116 ASN B C   1 
ATOM   5178  O O   . ASN B  1 116 ? -14.379  18.355  -44.974  1.00 39.06  ? 116 ASN B O   1 
ATOM   5179  C CB  . ASN B  1 116 ? -13.039  16.288  -42.907  1.00 40.37  ? 116 ASN B CB  1 
ATOM   5180  C CG  . ASN B  1 116 ? -13.245  17.557  -42.116  1.00 42.53  ? 116 ASN B CG  1 
ATOM   5181  O OD1 . ASN B  1 116 ? -14.285  17.719  -41.479  1.00 45.05  ? 116 ASN B OD1 1 
ATOM   5182  N ND2 . ASN B  1 116 ? -12.298  18.478  -42.163  1.00 42.89  ? 116 ASN B ND2 1 
ATOM   5183  N N   . TYR B  1 117 ? -12.984  17.026  -46.162  1.00 37.25  ? 117 TYR B N   1 
ATOM   5184  C CA  . TYR B  1 117 ? -12.757  17.966  -47.260  1.00 36.30  ? 117 TYR B CA  1 
ATOM   5185  C C   . TYR B  1 117 ? -13.466  17.480  -48.539  1.00 35.22  ? 117 TYR B C   1 
ATOM   5186  O O   . TYR B  1 117 ? -13.914  18.290  -49.351  1.00 36.26  ? 117 TYR B O   1 
ATOM   5187  C CB  . TYR B  1 117 ? -11.248  18.220  -47.480  1.00 36.30  ? 117 TYR B CB  1 
ATOM   5188  C CG  . TYR B  1 117 ? -10.402  17.005  -47.858  1.00 34.41  ? 117 TYR B CG  1 
ATOM   5189  C CD1 . TYR B  1 117 ? -10.445  16.485  -49.143  1.00 33.38  ? 117 TYR B CD1 1 
ATOM   5190  C CD2 . TYR B  1 117 ? -9.581   16.374  -46.932  1.00 34.78  ? 117 TYR B CD2 1 
ATOM   5191  C CE1 . TYR B  1 117 ? -9.721   15.359  -49.496  1.00 33.31  ? 117 TYR B CE1 1 
ATOM   5192  C CE2 . TYR B  1 117 ? -8.868   15.224  -47.257  1.00 34.96  ? 117 TYR B CE2 1 
ATOM   5193  C CZ  . TYR B  1 117 ? -8.951   14.711  -48.541  1.00 33.98  ? 117 TYR B CZ  1 
ATOM   5194  O OH  . TYR B  1 117 ? -8.270   13.606  -48.911  1.00 32.31  ? 117 TYR B OH  1 
ATOM   5195  N N   . ALA B  1 118 ? -13.559  16.159  -48.747  1.00 32.30  ? 118 ALA B N   1 
ATOM   5196  C CA  . ALA B  1 118 ? -14.192  15.627  -49.942  1.00 30.63  ? 118 ALA B CA  1 
ATOM   5197  C C   . ALA B  1 118 ? -15.642  16.120  -50.091  1.00 30.17  ? 118 ALA B C   1 
ATOM   5198  O O   . ALA B  1 118 ? -16.095  16.373  -51.203  1.00 28.79  ? 118 ALA B O   1 
ATOM   5199  C CB  . ALA B  1 118 ? -14.117  14.113  -49.945  1.00 29.24  ? 118 ALA B CB  1 
ATOM   5200  N N   . LYS B  1 119 ? -16.389  16.232  -48.995  1.00 30.84  ? 119 LYS B N   1 
ATOM   5201  C CA  . LYS B  1 119 ? -17.799  16.589  -49.094  1.00 33.13  ? 119 LYS B CA  1 
ATOM   5202  C C   . LYS B  1 119 ? -17.998  17.991  -49.705  1.00 36.13  ? 119 LYS B C   1 
ATOM   5203  O O   . LYS B  1 119 ? -19.129  18.383  -49.971  1.00 38.53  ? 119 LYS B O   1 
ATOM   5204  C CB  . LYS B  1 119 ? -18.441  16.559  -47.701  1.00 34.35  ? 119 LYS B CB  1 
ATOM   5205  C CG  . LYS B  1 119 ? -17.982  17.730  -46.803  1.00 36.95  ? 119 LYS B CG  1 
ATOM   5206  C CD  . LYS B  1 119 ? -18.478  17.800  -45.361  1.00 38.07  ? 119 LYS B CD  1 
ATOM   5207  C CE  . LYS B  1 119 ? -17.601  18.778  -44.632  1.00 39.57  ? 119 LYS B CE  1 
ATOM   5208  N NZ  . LYS B  1 119 ? -17.969  19.057  -43.244  1.00 40.61  ? 119 LYS B NZ  1 
ATOM   5209  N N   . LYS B  1 120 ? -16.931  18.766  -49.948  1.00 34.68  ? 120 LYS B N   1 
ATOM   5210  C CA  . LYS B  1 120 ? -17.111  20.057  -50.595  1.00 36.57  ? 120 LYS B CA  1 
ATOM   5211  C C   . LYS B  1 120 ? -17.029  19.952  -52.117  1.00 35.17  ? 120 LYS B C   1 
ATOM   5212  O O   . LYS B  1 120 ? -17.283  20.934  -52.821  1.00 33.95  ? 120 LYS B O   1 
ATOM   5213  C CB  . LYS B  1 120 ? -16.074  21.080  -50.119  1.00 37.79  ? 120 LYS B CB  1 
ATOM   5214  C CG  . LYS B  1 120 ? -16.209  21.499  -48.664  1.00 39.77  ? 120 LYS B CG  1 
ATOM   5215  C CD  . LYS B  1 120 ? -15.118  22.461  -48.210  1.00 43.19  ? 120 LYS B CD  1 
ATOM   5216  C CE  . LYS B  1 120 ? -13.743  21.934  -48.493  1.00 43.44  ? 120 LYS B CE  1 
ATOM   5217  N NZ  . LYS B  1 120 ? -12.726  22.886  -48.064  1.00 46.08  ? 120 LYS B NZ  1 
ATOM   5218  N N   . TYR B  1 121 ? -16.706  18.764  -52.635  1.00 33.71  ? 121 TYR B N   1 
ATOM   5219  C CA  . TYR B  1 121 ? -16.452  18.638  -54.057  1.00 33.21  ? 121 TYR B CA  1 
ATOM   5220  C C   . TYR B  1 121 ? -17.536  17.756  -54.665  1.00 33.99  ? 121 TYR B C   1 
ATOM   5221  O O   . TYR B  1 121 ? -17.483  16.518  -54.595  1.00 36.10  ? 121 TYR B O   1 
ATOM   5222  C CB  . TYR B  1 121 ? -14.986  18.205  -54.231  1.00 32.48  ? 121 TYR B CB  1 
ATOM   5223  C CG  . TYR B  1 121 ? -13.983  19.188  -53.633  1.00 31.74  ? 121 TYR B CG  1 
ATOM   5224  C CD1 . TYR B  1 121 ? -13.575  19.089  -52.307  1.00 32.19  ? 121 TYR B CD1 1 
ATOM   5225  C CD2 . TYR B  1 121 ? -13.482  20.244  -54.373  1.00 32.75  ? 121 TYR B CD2 1 
ATOM   5226  C CE1 . TYR B  1 121 ? -12.698  19.998  -51.743  1.00 32.97  ? 121 TYR B CE1 1 
ATOM   5227  C CE2 . TYR B  1 121 ? -12.609  21.178  -53.814  1.00 33.46  ? 121 TYR B CE2 1 
ATOM   5228  C CZ  . TYR B  1 121 ? -12.209  21.046  -52.501  1.00 33.35  ? 121 TYR B CZ  1 
ATOM   5229  O OH  . TYR B  1 121 ? -11.352  21.952  -51.961  1.00 36.11  ? 121 TYR B OH  1 
ATOM   5230  N N   . ASP B  1 122 ? -18.501  18.401  -55.328  1.00 34.27  ? 122 ASP B N   1 
ATOM   5231  C CA  . ASP B  1 122 ? -19.624  17.665  -55.900  1.00 33.91  ? 122 ASP B CA  1 
ATOM   5232  C C   . ASP B  1 122 ? -19.268  16.956  -57.214  1.00 32.25  ? 122 ASP B C   1 
ATOM   5233  O O   . ASP B  1 122 ? -20.131  16.301  -57.807  1.00 32.46  ? 122 ASP B O   1 
ATOM   5234  C CB  . ASP B  1 122 ? -20.878  18.519  -55.975  1.00 33.72  ? 122 ASP B CB  1 
ATOM   5235  C CG  . ASP B  1 122 ? -20.866  19.640  -56.997  1.00 33.71  ? 122 ASP B CG  1 
ATOM   5236  O OD1 . ASP B  1 122 ? -19.844  19.799  -57.688  1.00 30.11  ? 122 ASP B OD1 1 
ATOM   5237  O OD2 . ASP B  1 122 ? -21.909  20.349  -57.079  1.00 37.56  ? 122 ASP B OD2 1 
ATOM   5238  N N   . CYS B  1 123 ? -18.027  17.080  -57.693  1.00 30.24  ? 123 CYS B N   1 
ATOM   5239  C CA  . CYS B  1 123 ? -17.611  16.224  -58.794  1.00 30.01  ? 123 CYS B CA  1 
ATOM   5240  C C   . CYS B  1 123 ? -17.601  14.758  -58.348  1.00 29.39  ? 123 CYS B C   1 
ATOM   5241  O O   . CYS B  1 123 ? -17.552  13.863  -59.186  1.00 29.83  ? 123 CYS B O   1 
ATOM   5242  C CB  . CYS B  1 123 ? -16.227  16.574  -59.337  1.00 29.62  ? 123 CYS B CB  1 
ATOM   5243  S SG  . CYS B  1 123 ? -14.866  16.267  -58.178  1.00 29.81  ? 123 CYS B SG  1 
ATOM   5244  N N   . ILE B  1 124 ? -17.622  14.493  -57.040  1.00 29.87  ? 124 ILE B N   1 
ATOM   5245  C CA  . ILE B  1 124 ? -17.722  13.122  -56.571  1.00 29.98  ? 124 ILE B CA  1 
ATOM   5246  C C   . ILE B  1 124 ? -19.181  12.678  -56.650  1.00 29.87  ? 124 ILE B C   1 
ATOM   5247  O O   . ILE B  1 124 ? -20.036  13.291  -55.996  1.00 32.40  ? 124 ILE B O   1 
ATOM   5248  C CB  . ILE B  1 124 ? -17.190  12.997  -55.139  1.00 32.60  ? 124 ILE B CB  1 
ATOM   5249  C CG1 . ILE B  1 124 ? -15.717  13.373  -55.062  1.00 34.69  ? 124 ILE B CG1 1 
ATOM   5250  C CG2 . ILE B  1 124 ? -17.429  11.595  -54.572  1.00 32.76  ? 124 ILE B CG2 1 
ATOM   5251  C CD1 . ILE B  1 124 ? -15.244  13.588  -53.635  1.00 35.82  ? 124 ILE B CD1 1 
ATOM   5252  N N   . ILE B  1 125 ? -19.437  11.617  -57.430  1.00 27.91  ? 125 ILE B N   1 
ATOM   5253  C CA  . ILE B  1 125 ? -20.774  11.069  -57.651  1.00 28.61  ? 125 ILE B CA  1 
ATOM   5254  C C   . ILE B  1 125 ? -20.924  9.616   -57.172  1.00 28.06  ? 125 ILE B C   1 
ATOM   5255  O O   . ILE B  1 125 ? -22.034  9.098   -57.171  1.00 25.16  ? 125 ILE B O   1 
ATOM   5256  C CB  . ILE B  1 125 ? -21.186  11.174  -59.131  1.00 27.90  ? 125 ILE B CB  1 
ATOM   5257  C CG1 . ILE B  1 125 ? -20.246  10.425  -60.060  1.00 28.29  ? 125 ILE B CG1 1 
ATOM   5258  C CG2 . ILE B  1 125 ? -21.339  12.632  -59.539  1.00 28.35  ? 125 ILE B CG2 1 
ATOM   5259  C CD1 . ILE B  1 125 ? -20.834  10.163  -61.442  1.00 28.70  ? 125 ILE B CD1 1 
ATOM   5260  N N   . THR B  1 126 ? -19.829  8.941   -56.785  1.00 28.83  ? 126 THR B N   1 
ATOM   5261  C CA  . THR B  1 126 ? -19.947  7.683   -56.057  1.00 27.68  ? 126 THR B CA  1 
ATOM   5262  C C   . THR B  1 126 ? -18.657  7.432   -55.291  1.00 28.56  ? 126 THR B C   1 
ATOM   5263  O O   . THR B  1 126 ? -17.558  7.806   -55.736  1.00 28.38  ? 126 THR B O   1 
ATOM   5264  C CB  . THR B  1 126 ? -20.206  6.523   -57.017  1.00 28.79  ? 126 THR B CB  1 
ATOM   5265  O OG1 . THR B  1 126 ? -21.522  6.616   -57.573  1.00 28.85  ? 126 THR B OG1 1 
ATOM   5266  C CG2 . THR B  1 126 ? -20.040  5.167   -56.344  1.00 29.69  ? 126 THR B CG2 1 
ATOM   5267  N N   . TYR B  1 127 ? -18.809  6.745   -54.157  1.00 28.11  ? 127 TYR B N   1 
ATOM   5268  C CA  . TYR B  1 127 ? -17.689  6.232   -53.398  1.00 28.04  ? 127 TYR B CA  1 
ATOM   5269  C C   . TYR B  1 127 ? -17.662  4.716   -53.495  1.00 29.13  ? 127 TYR B C   1 
ATOM   5270  O O   . TYR B  1 127 ? -18.725  4.101   -53.348  1.00 29.09  ? 127 TYR B O   1 
ATOM   5271  C CB  . TYR B  1 127 ? -17.803  6.493   -51.903  1.00 27.43  ? 127 TYR B CB  1 
ATOM   5272  C CG  . TYR B  1 127 ? -17.499  7.926   -51.551  1.00 27.52  ? 127 TYR B CG  1 
ATOM   5273  C CD1 . TYR B  1 127 ? -16.189  8.345   -51.387  1.00 27.59  ? 127 TYR B CD1 1 
ATOM   5274  C CD2 . TYR B  1 127 ? -18.520  8.863   -51.420  1.00 26.96  ? 127 TYR B CD2 1 
ATOM   5275  C CE1 . TYR B  1 127 ? -15.902  9.655   -51.033  1.00 28.34  ? 127 TYR B CE1 1 
ATOM   5276  C CE2 . TYR B  1 127 ? -18.235  10.172  -51.073  1.00 27.70  ? 127 TYR B CE2 1 
ATOM   5277  C CZ  . TYR B  1 127 ? -16.925  10.566  -50.872  1.00 27.52  ? 127 TYR B CZ  1 
ATOM   5278  O OH  . TYR B  1 127 ? -16.648  11.850  -50.549  1.00 29.45  ? 127 TYR B OH  1 
ATOM   5279  N N   . LEU B  1 128 ? -16.445  4.154   -53.658  1.00 28.22  ? 128 LEU B N   1 
ATOM   5280  C CA  . LEU B  1 128 ? -16.246  2.706   -53.640  1.00 29.47  ? 128 LEU B CA  1 
ATOM   5281  C C   . LEU B  1 128 ? -15.500  2.359   -52.353  1.00 30.23  ? 128 LEU B C   1 
ATOM   5282  O O   . LEU B  1 128 ? -14.327  2.710   -52.189  1.00 33.23  ? 128 LEU B O   1 
ATOM   5283  C CB  . LEU B  1 128 ? -15.509  2.125   -54.848  1.00 30.18  ? 128 LEU B CB  1 
ATOM   5284  C CG  . LEU B  1 128 ? -16.012  2.557   -56.231  1.00 31.07  ? 128 LEU B CG  1 
ATOM   5285  C CD1 . LEU B  1 128 ? -15.104  1.949   -57.291  1.00 31.48  ? 128 LEU B CD1 1 
ATOM   5286  C CD2 . LEU B  1 128 ? -17.489  2.251   -56.467  1.00 31.11  ? 128 LEU B CD2 1 
ATOM   5287  N N   . VAL B  1 129 ? -16.185  1.650   -51.453  1.00 28.47  ? 129 VAL B N   1 
ATOM   5288  C CA  . VAL B  1 129 ? -15.757  1.597   -50.076  1.00 30.55  ? 129 VAL B CA  1 
ATOM   5289  C C   . VAL B  1 129 ? -14.754  0.459   -49.855  1.00 31.18  ? 129 VAL B C   1 
ATOM   5290  O O   . VAL B  1 129 ? -14.038  0.465   -48.870  1.00 31.00  ? 129 VAL B O   1 
ATOM   5291  C CB  . VAL B  1 129 ? -17.041  1.483   -49.245  1.00 32.90  ? 129 VAL B CB  1 
ATOM   5292  C CG1 . VAL B  1 129 ? -17.510  0.037   -49.127  1.00 34.55  ? 129 VAL B CG1 1 
ATOM   5293  C CG2 . VAL B  1 129 ? -16.895  2.125   -47.873  1.00 35.09  ? 129 VAL B CG2 1 
ATOM   5294  N N   . ILE B  1 130 ? -14.664  -0.509  -50.774  1.00 31.53  ? 130 ILE B N   1 
ATOM   5295  C CA  . ILE B  1 130 ? -13.579  -1.477  -50.711  1.00 33.67  ? 130 ILE B CA  1 
ATOM   5296  C C   . ILE B  1 130 ? -13.339  -2.045  -52.109  1.00 33.61  ? 130 ILE B C   1 
ATOM   5297  O O   . ILE B  1 130 ? -14.237  -2.055  -52.968  1.00 33.46  ? 130 ILE B O   1 
ATOM   5298  C CB  . ILE B  1 130 ? -13.864  -2.575  -49.665  1.00 35.85  ? 130 ILE B CB  1 
ATOM   5299  C CG1 . ILE B  1 130 ? -12.593  -3.322  -49.237  1.00 38.51  ? 130 ILE B CG1 1 
ATOM   5300  C CG2 . ILE B  1 130 ? -14.936  -3.555  -50.149  1.00 35.79  ? 130 ILE B CG2 1 
ATOM   5301  C CD1 . ILE B  1 130 ? -12.784  -4.223  -48.029  1.00 38.15  ? 130 ILE B CD1 1 
ATOM   5302  N N   . ASN B  1 131 ? -12.099  -2.509  -52.301  1.00 32.52  ? 131 ASN B N   1 
ATOM   5303  C CA  . ASN B  1 131 ? -11.654  -3.135  -53.535  1.00 32.79  ? 131 ASN B CA  1 
ATOM   5304  C C   . ASN B  1 131 ? -11.308  -4.616  -53.326  1.00 32.97  ? 131 ASN B C   1 
ATOM   5305  O O   . ASN B  1 131 ? -10.263  -4.973  -52.788  1.00 31.94  ? 131 ASN B O   1 
ATOM   5306  C CB  . ASN B  1 131 ? -10.462  -2.356  -54.071  1.00 33.82  ? 131 ASN B CB  1 
ATOM   5307  C CG  . ASN B  1 131 ? -10.086  -2.779  -55.462  1.00 35.47  ? 131 ASN B CG  1 
ATOM   5308  O OD1 . ASN B  1 131 ? -10.910  -2.710  -56.384  1.00 38.99  ? 131 ASN B OD1 1 
ATOM   5309  N ND2 . ASN B  1 131 ? -8.850   -3.221  -55.625  1.00 37.72  ? 131 ASN B ND2 1 
ATOM   5310  N N   . GLU B  1 132 ? -12.209  -5.482  -53.771  1.00 34.11  ? 132 GLU B N   1 
ATOM   5311  C CA  . GLU B  1 132 ? -11.876  -6.852  -54.139  1.00 34.63  ? 132 GLU B CA  1 
ATOM   5312  C C   . GLU B  1 132 ? -11.666  -7.787  -52.940  1.00 34.47  ? 132 GLU B C   1 
ATOM   5313  O O   . GLU B  1 132 ? -10.662  -8.495  -52.862  1.00 37.37  ? 132 GLU B O   1 
ATOM   5314  C CB  . GLU B  1 132 ? -10.675  -6.787  -55.081  1.00 34.97  ? 132 GLU B CB  1 
ATOM   5315  C CG  . GLU B  1 132 ? -10.653  -7.960  -56.055  1.00 35.07  ? 132 GLU B CG  1 
ATOM   5316  C CD  . GLU B  1 132 ? -11.834  -7.924  -57.007  1.00 34.77  ? 132 GLU B CD  1 
ATOM   5317  O OE1 . GLU B  1 132 ? -11.705  -7.245  -58.063  1.00 34.12  ? 132 GLU B OE1 1 
ATOM   5318  O OE2 . GLU B  1 132 ? -12.890  -8.546  -56.643  1.00 34.79  ? 132 GLU B OE2 1 
ATOM   5319  N N   . PRO B  1 133 ? -12.643  -7.921  -52.023  1.00 32.35  ? 133 PRO B N   1 
ATOM   5320  C CA  . PRO B  1 133 ? -12.564  -8.923  -50.976  1.00 32.88  ? 133 PRO B CA  1 
ATOM   5321  C C   . PRO B  1 133 ? -12.692  -10.309 -51.611  1.00 34.70  ? 133 PRO B C   1 
ATOM   5322  O O   . PRO B  1 133 ? -13.642  -10.587 -52.359  1.00 31.00  ? 133 PRO B O   1 
ATOM   5323  C CB  . PRO B  1 133 ? -13.735  -8.559  -50.094  1.00 33.08  ? 133 PRO B CB  1 
ATOM   5324  C CG  . PRO B  1 133 ? -14.759  -8.070  -51.064  1.00 32.18  ? 133 PRO B CG  1 
ATOM   5325  C CD  . PRO B  1 133 ? -13.939  -7.232  -52.026  1.00 33.23  ? 133 PRO B CD  1 
ATOM   5326  N N   . GLN B  1 134 ? -11.656  -11.115 -51.352  1.00 35.70  ? 134 GLN B N   1 
ATOM   5327  C CA  . GLN B  1 134 ? -11.552  -12.486 -51.815  1.00 38.55  ? 134 GLN B CA  1 
ATOM   5328  C C   . GLN B  1 134 ? -12.439  -13.398 -50.975  1.00 36.09  ? 134 GLN B C   1 
ATOM   5329  O O   . GLN B  1 134 ? -12.516  -13.261 -49.761  1.00 37.85  ? 134 GLN B O   1 
ATOM   5330  C CB  . GLN B  1 134 ? -10.088  -12.901 -51.667  1.00 45.05  ? 134 GLN B CB  1 
ATOM   5331  C CG  . GLN B  1 134 ? -9.131   -12.299 -52.692  1.00 46.29  ? 134 GLN B CG  1 
ATOM   5332  C CD  . GLN B  1 134 ? -9.323   -12.896 -54.071  1.00 54.20  ? 134 GLN B CD  1 
ATOM   5333  O OE1 . GLN B  1 134 ? -9.866   -13.998 -54.270  1.00 57.46  ? 134 GLN B OE1 1 
ATOM   5334  N NE2 . GLN B  1 134 ? -8.906   -12.128 -55.061  1.00 62.09  ? 134 GLN B NE2 1 
ATOM   5335  N N   . THR B  1 135 ? -13.089  -14.349 -51.638  1.00 36.10  ? 135 THR B N   1 
ATOM   5336  C CA  . THR B  1 135 ? -13.967  -15.305 -50.982  1.00 35.51  ? 135 THR B CA  1 
ATOM   5337  C C   . THR B  1 135 ? -13.299  -15.957 -49.774  1.00 36.15  ? 135 THR B C   1 
ATOM   5338  O O   . THR B  1 135 ? -13.852  -15.941 -48.678  1.00 36.95  ? 135 THR B O   1 
ATOM   5339  C CB  . THR B  1 135 ? -14.374  -16.377 -51.976  1.00 35.15  ? 135 THR B CB  1 
ATOM   5340  O OG1 . THR B  1 135 ? -14.736  -15.708 -53.182  1.00 34.95  ? 135 THR B OG1 1 
ATOM   5341  C CG2 . THR B  1 135 ? -15.551  -17.165 -51.443  1.00 36.17  ? 135 THR B CG2 1 
ATOM   5342  N N   . ASP B  1 136 ? -12.107  -16.529 -49.952  1.00 36.21  ? 136 ASP B N   1 
ATOM   5343  C CA  . ASP B  1 136 ? -11.500  -17.305 -48.874  1.00 37.07  ? 136 ASP B CA  1 
ATOM   5344  C C   . ASP B  1 136 ? -11.187  -16.399 -47.680  1.00 37.31  ? 136 ASP B C   1 
ATOM   5345  O O   . ASP B  1 136 ? -11.305  -16.821 -46.525  1.00 38.53  ? 136 ASP B O   1 
ATOM   5346  C CB  . ASP B  1 136 ? -10.257  -18.056 -49.329  1.00 36.97  ? 136 ASP B CB  1 
ATOM   5347  C CG  . ASP B  1 136 ? -9.625   -18.947 -48.268  1.00 37.98  ? 136 ASP B CG  1 
ATOM   5348  O OD1 . ASP B  1 136 ? -10.074  -20.123 -48.095  1.00 38.04  ? 136 ASP B OD1 1 
ATOM   5349  O OD2 . ASP B  1 136 ? -8.707   -18.455 -47.601  1.00 37.59  ? 136 ASP B OD2 1 
ATOM   5350  N N   . HIS B  1 137 ? -10.815  -15.143 -47.973  1.00 35.81  ? 137 HIS B N   1 
ATOM   5351  C CA  . HIS B  1 137 ? -10.504  -14.162 -46.946  1.00 34.54  ? 137 HIS B CA  1 
ATOM   5352  C C   . HIS B  1 137 ? -11.749  -13.856 -46.109  1.00 33.39  ? 137 HIS B C   1 
ATOM   5353  O O   . HIS B  1 137 ? -11.703  -13.936 -44.885  1.00 33.76  ? 137 HIS B O   1 
ATOM   5354  C CB  . HIS B  1 137 ? -9.910   -12.893 -47.561  1.00 33.28  ? 137 HIS B CB  1 
ATOM   5355  C CG  . HIS B  1 137 ? -9.476   -11.978 -46.475  1.00 35.27  ? 137 HIS B CG  1 
ATOM   5356  N ND1 . HIS B  1 137 ? -8.652   -12.393 -45.445  1.00 37.34  ? 137 HIS B ND1 1 
ATOM   5357  C CD2 . HIS B  1 137 ? -9.779   -10.690 -46.227  1.00 34.42  ? 137 HIS B CD2 1 
ATOM   5358  C CE1 . HIS B  1 137 ? -8.463   -11.375 -44.610  1.00 38.64  ? 137 HIS B CE1 1 
ATOM   5359  N NE2 . HIS B  1 137 ? -9.150   -10.340 -45.058  1.00 35.39  ? 137 HIS B NE2 1 
ATOM   5360  N N   . ILE B  1 138 ? -12.872  -13.571 -46.779  1.00 31.70  ? 138 ILE B N   1 
ATOM   5361  C CA  . ILE B  1 138 ? -14.127  -13.289 -46.095  1.00 31.37  ? 138 ILE B CA  1 
ATOM   5362  C C   . ILE B  1 138 ? -14.557  -14.463 -45.214  1.00 34.76  ? 138 ILE B C   1 
ATOM   5363  O O   . ILE B  1 138 ? -15.007  -14.259 -44.082  1.00 35.44  ? 138 ILE B O   1 
ATOM   5364  C CB  . ILE B  1 138 ? -15.230  -12.949 -47.101  1.00 30.09  ? 138 ILE B CB  1 
ATOM   5365  C CG1 . ILE B  1 138 ? -14.890  -11.763 -47.998  1.00 29.11  ? 138 ILE B CG1 1 
ATOM   5366  C CG2 . ILE B  1 138 ? -16.508  -12.698 -46.336  1.00 31.44  ? 138 ILE B CG2 1 
ATOM   5367  C CD1 . ILE B  1 138 ? -15.966  -11.394 -49.002  1.00 28.60  ? 138 ILE B CD1 1 
ATOM   5368  N N   . HIS B  1 139 ? -14.421  -15.696 -45.735  1.00 34.59  ? 139 HIS B N   1 
ATOM   5369  C CA  . HIS B  1 139 ? -14.718  -16.899 -44.969  1.00 35.92  ? 139 HIS B CA  1 
ATOM   5370  C C   . HIS B  1 139 ? -13.893  -16.923 -43.692  1.00 37.04  ? 139 HIS B C   1 
ATOM   5371  O O   . HIS B  1 139 ? -14.418  -17.248 -42.630  1.00 38.35  ? 139 HIS B O   1 
ATOM   5372  C CB  . HIS B  1 139 ? -14.479  -18.174 -45.809  1.00 36.27  ? 139 HIS B CB  1 
ATOM   5373  C CG  . HIS B  1 139 ? -14.774  -19.443 -45.100  1.00 35.15  ? 139 HIS B CG  1 
ATOM   5374  N ND1 . HIS B  1 139 ? -13.780  -20.113 -44.417  1.00 34.72  ? 139 HIS B ND1 1 
ATOM   5375  C CD2 . HIS B  1 139 ? -15.900  -20.178 -44.955  1.00 35.15  ? 139 HIS B CD2 1 
ATOM   5376  C CE1 . HIS B  1 139 ? -14.297  -21.232 -43.893  1.00 35.13  ? 139 HIS B CE1 1 
ATOM   5377  N NE2 . HIS B  1 139 ? -15.571  -21.289 -44.197  1.00 35.73  ? 139 HIS B NE2 1 
ATOM   5378  N N   . SER B  1 140 ? -12.606  -16.566 -43.798  1.00 37.79  ? 140 SER B N   1 
ATOM   5379  C CA  . SER B  1 140 ? -11.682  -16.684 -42.666  1.00 38.91  ? 140 SER B CA  1 
ATOM   5380  C C   . SER B  1 140 ? -11.976  -15.657 -41.561  1.00 38.22  ? 140 SER B C   1 
ATOM   5381  O O   . SER B  1 140 ? -11.889  -15.975 -40.375  1.00 38.68  ? 140 SER B O   1 
ATOM   5382  C CB  . SER B  1 140 ? -10.231  -16.586 -43.153  1.00 39.28  ? 140 SER B CB  1 
ATOM   5383  O OG  . SER B  1 140 ? -9.326   -16.674 -42.063  1.00 42.50  ? 140 SER B OG  1 
ATOM   5384  N N   . VAL B  1 141 ? -12.317  -14.415 -41.947  1.00 36.78  ? 141 VAL B N   1 
ATOM   5385  C CA  . VAL B  1 141 ? -12.590  -13.353 -40.991  1.00 35.38  ? 141 VAL B CA  1 
ATOM   5386  C C   . VAL B  1 141 ? -14.077  -13.276 -40.638  1.00 36.14  ? 141 VAL B C   1 
ATOM   5387  O O   . VAL B  1 141 ? -14.415  -12.656 -39.630  1.00 35.82  ? 141 VAL B O   1 
ATOM   5388  C CB  . VAL B  1 141 ? -12.054  -12.012 -41.525  1.00 35.14  ? 141 VAL B CB  1 
ATOM   5389  C CG1 . VAL B  1 141 ? -10.561  -12.106 -41.833  1.00 35.56  ? 141 VAL B CG1 1 
ATOM   5390  C CG2 . VAL B  1 141 ? -12.824  -11.469 -42.722  1.00 32.96  ? 141 VAL B CG2 1 
ATOM   5391  N N   . THR B  1 142 ? -14.933  -13.945 -41.447  1.00 38.10  ? 142 THR B N   1 
ATOM   5392  C CA  . THR B  1 142 ? -16.378  -14.172 -41.254  1.00 35.93  ? 142 THR B CA  1 
ATOM   5393  C C   . THR B  1 142 ? -17.152  -13.165 -42.099  1.00 36.23  ? 142 THR B C   1 
ATOM   5394  O O   . THR B  1 142 ? -16.757  -11.996 -42.204  1.00 35.72  ? 142 THR B O   1 
ATOM   5395  C CB  . THR B  1 142 ? -16.918  -14.156 -39.820  1.00 35.61  ? 142 THR B CB  1 
ATOM   5396  O OG1 . THR B  1 142 ? -16.873  -12.836 -39.303  1.00 34.37  ? 142 THR B OG1 1 
ATOM   5397  C CG2 . THR B  1 142 ? -16.220  -15.147 -38.901  1.00 36.07  ? 142 THR B CG2 1 
ATOM   5398  N N   . GLY B  1 143 ? -18.239  -13.659 -42.718  1.00 35.35  ? 143 GLY B N   1 
ATOM   5399  C CA  . GLY B  1 143 ? -19.175  -12.836 -43.462  1.00 33.56  ? 143 GLY B CA  1 
ATOM   5400  C C   . GLY B  1 143 ? -19.726  -11.737 -42.558  1.00 34.96  ? 143 GLY B C   1 
ATOM   5401  O O   . GLY B  1 143 ? -19.826  -10.594 -42.972  1.00 36.08  ? 143 GLY B O   1 
ATOM   5402  N N   . LYS B  1 144 ? -19.995  -12.068 -41.294  1.00 36.83  ? 144 LYS B N   1 
ATOM   5403  C CA  . LYS B  1 144 ? -20.498  -11.090 -40.348  1.00 39.60  ? 144 LYS B CA  1 
ATOM   5404  C C   . LYS B  1 144 ? -19.542  -9.890  -40.265  1.00 39.85  ? 144 LYS B C   1 
ATOM   5405  O O   . LYS B  1 144 ? -19.992  -8.754  -40.373  1.00 36.82  ? 144 LYS B O   1 
ATOM   5406  C CB  . LYS B  1 144 ? -20.761  -11.702 -38.974  1.00 41.58  ? 144 LYS B CB  1 
ATOM   5407  C CG  . LYS B  1 144 ? -21.407  -10.756 -37.980  1.00 43.73  ? 144 LYS B CG  1 
ATOM   5408  C CD  . LYS B  1 144 ? -21.770  -11.460 -36.671  1.00 46.61  ? 144 LYS B CD  1 
ATOM   5409  C CE  . LYS B  1 144 ? -22.017  -10.522 -35.522  1.00 49.44  ? 144 LYS B CE  1 
ATOM   5410  N NZ  . LYS B  1 144 ? -22.773  -9.348  -35.974  1.00 50.17  ? 144 LYS B NZ  1 
ATOM   5411  N N   . ALA B  1 145 ? -18.233  -10.128 -40.111  1.00 36.57  ? 145 ALA B N   1 
ATOM   5412  C CA  . ALA B  1 145 ? -17.320  -9.015  -39.914  1.00 36.12  ? 145 ALA B CA  1 
ATOM   5413  C C   . ALA B  1 145 ? -17.283  -8.149  -41.170  1.00 34.19  ? 145 ALA B C   1 
ATOM   5414  O O   . ALA B  1 145 ? -17.145  -6.932  -41.090  1.00 33.79  ? 145 ALA B O   1 
ATOM   5415  C CB  . ALA B  1 145 ? -15.933  -9.522  -39.554  1.00 36.37  ? 145 ALA B CB  1 
ATOM   5416  N N   . PHE B  1 146 ? -17.364  -8.804  -42.332  1.00 33.99  ? 146 PHE B N   1 
ATOM   5417  C CA  . PHE B  1 146 ? -17.370  -8.098  -43.599  1.00 33.63  ? 146 PHE B CA  1 
ATOM   5418  C C   . PHE B  1 146 ? -18.614  -7.216  -43.711  1.00 35.45  ? 146 PHE B C   1 
ATOM   5419  O O   . PHE B  1 146 ? -18.514  -6.024  -44.026  1.00 38.01  ? 146 PHE B O   1 
ATOM   5420  C CB  . PHE B  1 146 ? -17.323  -9.056  -44.786  1.00 33.04  ? 146 PHE B CB  1 
ATOM   5421  C CG  . PHE B  1 146 ? -17.560  -8.386  -46.138  1.00 31.88  ? 146 PHE B CG  1 
ATOM   5422  C CD1 . PHE B  1 146 ? -16.584  -7.594  -46.723  1.00 30.44  ? 146 PHE B CD1 1 
ATOM   5423  C CD2 . PHE B  1 146 ? -18.775  -8.532  -46.817  1.00 31.16  ? 146 PHE B CD2 1 
ATOM   5424  C CE1 . PHE B  1 146 ? -16.800  -6.991  -47.951  1.00 28.56  ? 146 PHE B CE1 1 
ATOM   5425  C CE2 . PHE B  1 146 ? -18.980  -7.903  -48.029  1.00 29.17  ? 146 PHE B CE2 1 
ATOM   5426  C CZ  . PHE B  1 146 ? -17.968  -7.181  -48.613  1.00 28.01  ? 146 PHE B CZ  1 
ATOM   5427  N N   . VAL B  1 147 ? -19.790  -7.797  -43.458  1.00 33.88  ? 147 VAL B N   1 
ATOM   5428  C CA  . VAL B  1 147 ? -21.029  -7.041  -43.569  1.00 34.16  ? 147 VAL B CA  1 
ATOM   5429  C C   . VAL B  1 147 ? -21.035  -5.842  -42.607  1.00 33.05  ? 147 VAL B C   1 
ATOM   5430  O O   . VAL B  1 147 ? -21.470  -4.758  -42.990  1.00 30.73  ? 147 VAL B O   1 
ATOM   5431  C CB  . VAL B  1 147 ? -22.242  -7.968  -43.351  1.00 33.22  ? 147 VAL B CB  1 
ATOM   5432  C CG1 . VAL B  1 147 ? -23.551  -7.196  -43.173  1.00 32.79  ? 147 VAL B CG1 1 
ATOM   5433  C CG2 . VAL B  1 147 ? -22.347  -8.982  -44.485  1.00 33.38  ? 147 VAL B CG2 1 
ATOM   5434  N N   . ASP B  1 148 ? -20.640  -6.086  -41.350  1.00 34.13  ? 148 ASP B N   1 
ATOM   5435  C CA  . ASP B  1 148 ? -20.633  -5.086  -40.294  1.00 37.11  ? 148 ASP B CA  1 
ATOM   5436  C C   . ASP B  1 148 ? -19.717  -3.935  -40.704  1.00 37.34  ? 148 ASP B C   1 
ATOM   5437  O O   . ASP B  1 148 ? -20.067  -2.770  -40.514  1.00 35.18  ? 148 ASP B O   1 
ATOM   5438  C CB  . ASP B  1 148 ? -20.204  -5.661  -38.951  1.00 37.04  ? 148 ASP B CB  1 
ATOM   5439  C CG  . ASP B  1 148 ? -21.211  -6.570  -38.257  1.00 38.73  ? 148 ASP B CG  1 
ATOM   5440  O OD1 . ASP B  1 148 ? -22.353  -6.693  -38.739  1.00 37.79  ? 148 ASP B OD1 1 
ATOM   5441  O OD2 . ASP B  1 148 ? -20.832  -7.180  -37.242  1.00 42.02  ? 148 ASP B OD2 1 
ATOM   5442  N N   . LEU B  1 149 ? -18.565  -4.292  -41.284  1.00 35.85  ? 149 LEU B N   1 
ATOM   5443  C CA  . LEU B  1 149 ? -17.617  -3.296  -41.730  1.00 36.40  ? 149 LEU B CA  1 
ATOM   5444  C C   . LEU B  1 149 ? -18.236  -2.468  -42.852  1.00 34.84  ? 149 LEU B C   1 
ATOM   5445  O O   . LEU B  1 149 ? -18.127  -1.253  -42.878  1.00 35.04  ? 149 LEU B O   1 
ATOM   5446  C CB  . LEU B  1 149 ? -16.307  -3.926  -42.193  1.00 38.11  ? 149 LEU B CB  1 
ATOM   5447  C CG  . LEU B  1 149 ? -15.276  -2.922  -42.728  1.00 38.76  ? 149 LEU B CG  1 
ATOM   5448  C CD1 . LEU B  1 149 ? -14.882  -1.882  -41.666  1.00 39.23  ? 149 LEU B CD1 1 
ATOM   5449  C CD2 . LEU B  1 149 ? -14.065  -3.636  -43.264  1.00 39.13  ? 149 LEU B CD2 1 
ATOM   5450  N N   . MET B  1 150 ? -18.866  -3.135  -43.801  1.00 34.21  ? 150 MET B N   1 
ATOM   5451  C CA  . MET B  1 150 ? -19.457  -2.435  -44.917  1.00 34.07  ? 150 MET B CA  1 
ATOM   5452  C C   . MET B  1 150 ? -20.506  -1.449  -44.396  1.00 34.56  ? 150 MET B C   1 
ATOM   5453  O O   . MET B  1 150 ? -20.452  -0.278  -44.740  1.00 33.77  ? 150 MET B O   1 
ATOM   5454  C CB  . MET B  1 150 ? -20.044  -3.423  -45.920  1.00 33.39  ? 150 MET B CB  1 
ATOM   5455  C CG  . MET B  1 150 ? -19.027  -4.216  -46.688  1.00 33.35  ? 150 MET B CG  1 
ATOM   5456  S SD  . MET B  1 150 ? -17.869  -3.255  -47.682  1.00 35.45  ? 150 MET B SD  1 
ATOM   5457  C CE  . MET B  1 150 ? -16.436  -3.286  -46.597  1.00 37.63  ? 150 MET B CE  1 
ATOM   5458  N N   . ASN B  1 151 ? -21.426  -1.911  -43.545  1.00 35.35  ? 151 ASN B N   1 
ATOM   5459  C CA  . ASN B  1 151 ? -22.509  -1.061  -43.076  1.00 37.80  ? 151 ASN B CA  1 
ATOM   5460  C C   . ASN B  1 151 ? -21.956  0.151   -42.309  1.00 38.90  ? 151 ASN B C   1 
ATOM   5461  O O   . ASN B  1 151 ? -22.545  1.239   -42.355  1.00 40.13  ? 151 ASN B O   1 
ATOM   5462  C CB  . ASN B  1 151 ? -23.534  -1.807  -42.224  1.00 37.15  ? 151 ASN B CB  1 
ATOM   5463  C CG  . ASN B  1 151 ? -24.491  -2.661  -43.028  1.00 38.01  ? 151 ASN B CG  1 
ATOM   5464  O OD1 . ASN B  1 151 ? -24.821  -2.348  -44.177  1.00 38.47  ? 151 ASN B OD1 1 
ATOM   5465  N ND2 . ASN B  1 151 ? -24.972  -3.742  -42.430  1.00 36.62  ? 151 ASN B ND2 1 
ATOM   5466  N N   . THR B  1 152 ? -20.865  -0.045  -41.568  1.00 37.51  ? 152 THR B N   1 
ATOM   5467  C CA  . THR B  1 152 ? -20.293  1.015   -40.749  1.00 39.21  ? 152 THR B CA  1 
ATOM   5468  C C   . THR B  1 152 ? -19.788  2.146   -41.650  1.00 38.44  ? 152 THR B C   1 
ATOM   5469  O O   . THR B  1 152 ? -20.033  3.318   -41.371  1.00 38.88  ? 152 THR B O   1 
ATOM   5470  C CB  . THR B  1 152 ? -19.176  0.427   -39.888  1.00 40.28  ? 152 THR B CB  1 
ATOM   5471  O OG1 . THR B  1 152 ? -19.913  -0.442  -39.034  1.00 43.67  ? 152 THR B OG1 1 
ATOM   5472  C CG2 . THR B  1 152 ? -18.410  1.478   -39.103  1.00 39.42  ? 152 THR B CG2 1 
ATOM   5473  N N   . LEU B  1 153 ? -19.123  1.767   -42.752  1.00 35.96  ? 153 LEU B N   1 
ATOM   5474  C CA  . LEU B  1 153 ? -18.444  2.712   -43.605  1.00 35.49  ? 153 LEU B CA  1 
ATOM   5475  C C   . LEU B  1 153 ? -19.463  3.439   -44.492  1.00 35.62  ? 153 LEU B C   1 
ATOM   5476  O O   . LEU B  1 153 ? -19.314  4.644   -44.731  1.00 35.17  ? 153 LEU B O   1 
ATOM   5477  C CB  . LEU B  1 153 ? -17.407  1.952   -44.432  1.00 35.04  ? 153 LEU B CB  1 
ATOM   5478  C CG  . LEU B  1 153 ? -16.264  1.275   -43.668  1.00 34.82  ? 153 LEU B CG  1 
ATOM   5479  C CD1 . LEU B  1 153 ? -15.324  0.632   -44.652  1.00 34.61  ? 153 LEU B CD1 1 
ATOM   5480  C CD2 . LEU B  1 153 ? -15.482  2.233   -42.818  1.00 36.73  ? 153 LEU B CD2 1 
ATOM   5481  N N   . ILE B  1 154 ? -20.419  2.673   -45.047  1.00 32.71  ? 154 ILE B N   1 
ATOM   5482  C CA  . ILE B  1 154 ? -21.556  3.223   -45.778  1.00 32.52  ? 154 ILE B CA  1 
ATOM   5483  C C   . ILE B  1 154 ? -22.246  4.296   -44.937  1.00 32.53  ? 154 ILE B C   1 
ATOM   5484  O O   . ILE B  1 154 ? -22.537  5.378   -45.425  1.00 31.98  ? 154 ILE B O   1 
ATOM   5485  C CB  . ILE B  1 154 ? -22.563  2.129   -46.180  1.00 30.21  ? 154 ILE B CB  1 
ATOM   5486  C CG1 . ILE B  1 154 ? -21.976  1.169   -47.195  1.00 30.76  ? 154 ILE B CG1 1 
ATOM   5487  C CG2 . ILE B  1 154 ? -23.876  2.723   -46.693  1.00 29.32  ? 154 ILE B CG2 1 
ATOM   5488  C CD1 . ILE B  1 154 ? -22.631  -0.202  -47.173  1.00 31.37  ? 154 ILE B CD1 1 
ATOM   5489  N N   . ASN B  1 155 ? -22.514  3.986   -43.673  1.00 33.27  ? 155 ASN B N   1 
ATOM   5490  C CA  . ASN B  1 155 ? -23.175  4.931   -42.802  1.00 37.24  ? 155 ASN B CA  1 
ATOM   5491  C C   . ASN B  1 155 ? -22.322  6.203   -42.625  1.00 37.92  ? 155 ASN B C   1 
ATOM   5492  O O   . ASN B  1 155 ? -22.846  7.308   -42.589  1.00 38.36  ? 155 ASN B O   1 
ATOM   5493  C CB  . ASN B  1 155 ? -23.530  4.272   -41.483  1.00 39.31  ? 155 ASN B CB  1 
ATOM   5494  C CG  . ASN B  1 155 ? -24.255  5.262   -40.607  1.00 44.55  ? 155 ASN B CG  1 
ATOM   5495  O OD1 . ASN B  1 155 ? -25.319  5.768   -40.995  1.00 50.51  ? 155 ASN B OD1 1 
ATOM   5496  N ND2 . ASN B  1 155 ? -23.681  5.593   -39.457  1.00 45.63  ? 155 ASN B ND2 1 
ATOM   5497  N N   . ILE B  1 156 ? -21.003  6.058   -42.471  1.00 36.83  ? 156 ILE B N   1 
ATOM   5498  C CA  . ILE B  1 156 ? -20.142  7.206   -42.258  1.00 35.98  ? 156 ILE B CA  1 
ATOM   5499  C C   . ILE B  1 156 ? -20.192  8.098   -43.503  1.00 34.77  ? 156 ILE B C   1 
ATOM   5500  O O   . ILE B  1 156 ? -20.198  9.331   -43.359  1.00 33.05  ? 156 ILE B O   1 
ATOM   5501  C CB  . ILE B  1 156 ? -18.722  6.735   -41.876  1.00 35.73  ? 156 ILE B CB  1 
ATOM   5502  C CG1 . ILE B  1 156 ? -18.608  6.425   -40.394  1.00 37.77  ? 156 ILE B CG1 1 
ATOM   5503  C CG2 . ILE B  1 156 ? -17.641  7.724   -42.270  1.00 35.56  ? 156 ILE B CG2 1 
ATOM   5504  C CD1 . ILE B  1 156 ? -17.461  5.474   -40.053  1.00 38.09  ? 156 ILE B CD1 1 
ATOM   5505  N N   . ILE B  1 157 ? -20.268  7.488   -44.703  1.00 31.28  ? 157 ILE B N   1 
ATOM   5506  C CA  . ILE B  1 157 ? -20.285  8.284   -45.919  1.00 32.97  ? 157 ILE B CA  1 
ATOM   5507  C C   . ILE B  1 157 ? -21.630  8.996   -46.081  1.00 34.76  ? 157 ILE B C   1 
ATOM   5508  O O   . ILE B  1 157 ? -21.673  10.152  -46.489  1.00 37.02  ? 157 ILE B O   1 
ATOM   5509  C CB  . ILE B  1 157 ? -19.920  7.475   -47.176  1.00 33.18  ? 157 ILE B CB  1 
ATOM   5510  C CG1 . ILE B  1 157 ? -18.481  6.919   -47.110  1.00 34.33  ? 157 ILE B CG1 1 
ATOM   5511  C CG2 . ILE B  1 157 ? -20.117  8.316   -48.438  1.00 33.19  ? 157 ILE B CG2 1 
ATOM   5512  C CD1 . ILE B  1 157 ? -18.235  5.696   -47.968  1.00 32.55  ? 157 ILE B CD1 1 
ATOM   5513  N N   . HIS B  1 158 ? -22.732  8.320   -45.762  1.00 33.80  ? 158 HIS B N   1 
ATOM   5514  C CA  . HIS B  1 158 ? -24.043  8.916   -45.921  1.00 33.38  ? 158 HIS B CA  1 
ATOM   5515  C C   . HIS B  1 158 ? -24.198  10.125  -45.000  1.00 36.08  ? 158 HIS B C   1 
ATOM   5516  O O   . HIS B  1 158 ? -24.903  11.078  -45.358  1.00 35.45  ? 158 HIS B O   1 
ATOM   5517  C CB  . HIS B  1 158 ? -25.146  7.889   -45.661  1.00 31.90  ? 158 HIS B CB  1 
ATOM   5518  C CG  . HIS B  1 158 ? -25.352  6.836   -46.703  1.00 29.87  ? 158 HIS B CG  1 
ATOM   5519  N ND1 . HIS B  1 158 ? -26.108  5.712   -46.437  1.00 30.10  ? 158 HIS B ND1 1 
ATOM   5520  C CD2 . HIS B  1 158 ? -24.958  6.719   -47.969  1.00 28.90  ? 158 HIS B CD2 1 
ATOM   5521  C CE1 . HIS B  1 158 ? -26.200  4.974   -47.543  1.00 29.62  ? 158 HIS B CE1 1 
ATOM   5522  N NE2 . HIS B  1 158 ? -25.474  5.552   -48.478  1.00 28.46  ? 158 HIS B NE2 1 
ATOM   5523  N N   . LYS B  1 159 ? -23.553  10.099  -43.822  1.00 37.88  ? 159 LYS B N   1 
ATOM   5524  C CA  . LYS B  1 159 ? -23.663  11.222  -42.896  1.00 40.38  ? 159 LYS B CA  1 
ATOM   5525  C C   . LYS B  1 159 ? -22.641  12.309  -43.212  1.00 39.47  ? 159 LYS B C   1 
ATOM   5526  O O   . LYS B  1 159 ? -22.953  13.488  -43.064  1.00 43.01  ? 159 LYS B O   1 
ATOM   5527  C CB  . LYS B  1 159 ? -23.505  10.827  -41.427  1.00 45.71  ? 159 LYS B CB  1 
ATOM   5528  C CG  . LYS B  1 159 ? -24.725  10.090  -40.895  1.00 53.31  ? 159 LYS B CG  1 
ATOM   5529  C CD  . LYS B  1 159 ? -24.788  9.789   -39.400  1.00 63.33  ? 159 LYS B CD  1 
ATOM   5530  C CE  . LYS B  1 159 ? -25.637  8.561   -39.056  1.00 67.97  ? 159 LYS B CE  1 
ATOM   5531  N NZ  . LYS B  1 159 ? -26.817  8.267   -39.889  1.00 66.05  ? 159 LYS B NZ  1 
ATOM   5532  N N   . GLY B  1 160 ? -21.442  11.911  -43.654  1.00 37.61  ? 160 GLY B N   1 
ATOM   5533  C CA  . GLY B  1 160 ? -20.305  12.805  -43.810  1.00 36.17  ? 160 GLY B CA  1 
ATOM   5534  C C   . GLY B  1 160 ? -20.317  13.501  -45.170  1.00 35.68  ? 160 GLY B C   1 
ATOM   5535  O O   . GLY B  1 160 ? -19.945  14.674  -45.279  1.00 37.88  ? 160 GLY B O   1 
ATOM   5536  N N   . HIS B  1 161 ? -20.732  12.766  -46.213  1.00 32.95  ? 161 HIS B N   1 
ATOM   5537  C CA  . HIS B  1 161 ? -20.923  13.347  -47.529  1.00 30.72  ? 161 HIS B CA  1 
ATOM   5538  C C   . HIS B  1 161 ? -22.330  12.988  -48.010  1.00 30.10  ? 161 HIS B C   1 
ATOM   5539  O O   . HIS B  1 161 ? -22.524  12.084  -48.816  1.00 29.22  ? 161 HIS B O   1 
ATOM   5540  C CB  . HIS B  1 161 ? -19.793  12.928  -48.465  1.00 29.15  ? 161 HIS B CB  1 
ATOM   5541  C CG  . HIS B  1 161 ? -19.735  13.749  -49.710  1.00 29.23  ? 161 HIS B CG  1 
ATOM   5542  N ND1 . HIS B  1 161 ? -18.730  13.621  -50.641  1.00 28.50  ? 161 HIS B ND1 1 
ATOM   5543  C CD2 . HIS B  1 161 ? -20.570  14.695  -50.197  1.00 29.43  ? 161 HIS B CD2 1 
ATOM   5544  C CE1 . HIS B  1 161 ? -18.969  14.466  -51.638  1.00 28.88  ? 161 HIS B CE1 1 
ATOM   5545  N NE2 . HIS B  1 161 ? -20.069  15.132  -51.392  1.00 28.22  ? 161 HIS B NE2 1 
ATOM   5546  N N   . PRO B  1 162 ? -23.373  13.701  -47.545  1.00 31.53  ? 162 PRO B N   1 
ATOM   5547  C CA  . PRO B  1 162 ? -24.760  13.318  -47.844  1.00 31.61  ? 162 PRO B CA  1 
ATOM   5548  C C   . PRO B  1 162 ? -25.088  13.270  -49.330  1.00 31.77  ? 162 PRO B C   1 
ATOM   5549  O O   . PRO B  1 162 ? -24.645  14.124  -50.095  1.00 33.62  ? 162 PRO B O   1 
ATOM   5550  C CB  . PRO B  1 162 ? -25.585  14.367  -47.120  1.00 32.66  ? 162 PRO B CB  1 
ATOM   5551  C CG  . PRO B  1 162 ? -24.657  14.865  -46.037  1.00 33.25  ? 162 PRO B CG  1 
ATOM   5552  C CD  . PRO B  1 162 ? -23.276  14.884  -46.674  1.00 32.75  ? 162 PRO B CD  1 
ATOM   5553  N N   . GLY B  1 163 ? -25.843  12.244  -49.736  1.00 31.63  ? 163 GLY B N   1 
ATOM   5554  C CA  . GLY B  1 163 ? -26.466  12.249  -51.051  1.00 31.25  ? 163 GLY B CA  1 
ATOM   5555  C C   . GLY B  1 163 ? -25.616  11.547  -52.104  1.00 32.14  ? 163 GLY B C   1 
ATOM   5556  O O   . GLY B  1 163 ? -26.052  11.480  -53.245  1.00 36.00  ? 163 GLY B O   1 
ATOM   5557  N N   . ILE B  1 164 ? -24.418  11.061  -51.733  1.00 30.46  ? 164 ILE B N   1 
ATOM   5558  C CA  . ILE B  1 164 ? -23.508  10.446  -52.686  1.00 29.32  ? 164 ILE B CA  1 
ATOM   5559  C C   . ILE B  1 164 ? -23.625  8.925   -52.607  1.00 29.87  ? 164 ILE B C   1 
ATOM   5560  O O   . ILE B  1 164 ? -23.345  8.343   -51.558  1.00 29.91  ? 164 ILE B O   1 
ATOM   5561  C CB  . ILE B  1 164 ? -22.055  10.855  -52.430  1.00 27.71  ? 164 ILE B CB  1 
ATOM   5562  C CG1 . ILE B  1 164 ? -21.890  12.347  -52.300  1.00 29.06  ? 164 ILE B CG1 1 
ATOM   5563  C CG2 . ILE B  1 164 ? -21.194  10.294  -53.543  1.00 26.93  ? 164 ILE B CG2 1 
ATOM   5564  C CD1 . ILE B  1 164 ? -22.323  13.120  -53.526  1.00 28.79  ? 164 ILE B CD1 1 
ATOM   5565  N N   . PRO B  1 165 ? -24.073  8.246   -53.692  1.00 30.46  ? 165 PRO B N   1 
ATOM   5566  C CA  . PRO B  1 165 ? -24.192  6.782   -53.701  1.00 30.68  ? 165 PRO B CA  1 
ATOM   5567  C C   . PRO B  1 165 ? -22.893  6.098   -53.305  1.00 32.02  ? 165 PRO B C   1 
ATOM   5568  O O   . PRO B  1 165 ? -21.810  6.558   -53.689  1.00 33.54  ? 165 PRO B O   1 
ATOM   5569  C CB  . PRO B  1 165 ? -24.548  6.481   -55.159  1.00 30.28  ? 165 PRO B CB  1 
ATOM   5570  C CG  . PRO B  1 165 ? -25.307  7.726   -55.609  1.00 31.24  ? 165 PRO B CG  1 
ATOM   5571  C CD  . PRO B  1 165 ? -24.601  8.866   -54.919  1.00 29.89  ? 165 PRO B CD  1 
ATOM   5572  N N   . VAL B  1 166 ? -23.026  5.031   -52.518  1.00 31.18  ? 166 VAL B N   1 
ATOM   5573  C CA  . VAL B  1 166 ? -21.906  4.183   -52.126  1.00 31.51  ? 166 VAL B CA  1 
ATOM   5574  C C   . VAL B  1 166 ? -22.102  2.766   -52.681  1.00 29.65  ? 166 VAL B C   1 
ATOM   5575  O O   . VAL B  1 166 ? -23.221  2.259   -52.674  1.00 29.84  ? 166 VAL B O   1 
ATOM   5576  C CB  . VAL B  1 166 ? -21.931  4.185   -50.581  1.00 33.41  ? 166 VAL B CB  1 
ATOM   5577  C CG1 . VAL B  1 166 ? -20.758  3.415   -49.950  1.00 33.52  ? 166 VAL B CG1 1 
ATOM   5578  C CG2 . VAL B  1 166 ? -22.014  5.608   -50.032  1.00 33.14  ? 166 VAL B CG2 1 
ATOM   5579  N N   . THR B  1 167 ? -21.021  2.139   -53.161  1.00 28.86  ? 167 THR B N   1 
ATOM   5580  C CA  . THR B  1 167 ? -20.995  0.734   -53.561  1.00 28.09  ? 167 THR B CA  1 
ATOM   5581  C C   . THR B  1 167 ? -19.557  0.256   -53.395  1.00 28.69  ? 167 THR B C   1 
ATOM   5582  O O   . THR B  1 167 ? -18.838  0.855   -52.592  1.00 30.22  ? 167 THR B O   1 
ATOM   5583  C CB  . THR B  1 167 ? -21.547  0.550   -54.974  1.00 27.04  ? 167 THR B CB  1 
ATOM   5584  O OG1 . THR B  1 167 ? -21.697  -0.865  -55.105  1.00 26.61  ? 167 THR B OG1 1 
ATOM   5585  C CG2 . THR B  1 167 ? -20.700  1.200   -56.057  1.00 26.66  ? 167 THR B CG2 1 
ATOM   5586  N N   . LEU B  1 168 ? -19.156  -0.811  -54.107  1.00 28.52  ? 168 LEU B N   1 
ATOM   5587  C CA  . LEU B  1 168 ? -17.828  -1.410  -53.938  1.00 29.77  ? 168 LEU B CA  1 
ATOM   5588  C C   . LEU B  1 168 ? -17.267  -1.932  -55.266  1.00 28.91  ? 168 LEU B C   1 
ATOM   5589  O O   . LEU B  1 168 ? -17.995  -2.107  -56.233  1.00 28.32  ? 168 LEU B O   1 
ATOM   5590  C CB  . LEU B  1 168 ? -17.857  -2.530  -52.887  1.00 28.30  ? 168 LEU B CB  1 
ATOM   5591  C CG  . LEU B  1 168 ? -18.228  -3.930  -53.387  1.00 28.40  ? 168 LEU B CG  1 
ATOM   5592  C CD1 . LEU B  1 168 ? -18.065  -5.002  -52.286  1.00 28.36  ? 168 LEU B CD1 1 
ATOM   5593  C CD2 . LEU B  1 168 ? -19.647  -3.986  -53.952  1.00 27.91  ? 168 LEU B CD2 1 
ATOM   5594  N N   . SER B  1 169 ? -15.976  -2.283  -55.260  1.00 30.47  ? 169 SER B N   1 
ATOM   5595  C CA  . SER B  1 169 ? -15.301  -2.921  -56.388  1.00 29.61  ? 169 SER B CA  1 
ATOM   5596  C C   . SER B  1 169 ? -15.239  -4.437  -56.148  1.00 31.89  ? 169 SER B C   1 
ATOM   5597  O O   . SER B  1 169 ? -14.509  -4.924  -55.287  1.00 33.27  ? 169 SER B O   1 
ATOM   5598  C CB  . SER B  1 169 ? -13.945  -2.280  -56.552  1.00 30.55  ? 169 SER B CB  1 
ATOM   5599  O OG  . SER B  1 169 ? -13.053  -2.941  -57.441  1.00 33.24  ? 169 SER B OG  1 
ATOM   5600  N N   . ALA B  1 170 ? -16.075  -5.192  -56.859  1.00 31.95  ? 170 ALA B N   1 
ATOM   5601  C CA  . ALA B  1 170 ? -16.220  -6.623  -56.605  1.00 30.83  ? 170 ALA B CA  1 
ATOM   5602  C C   . ALA B  1 170 ? -16.280  -7.374  -57.933  1.00 30.02  ? 170 ALA B C   1 
ATOM   5603  O O   . ALA B  1 170 ? -17.157  -7.123  -58.758  1.00 30.13  ? 170 ALA B O   1 
ATOM   5604  C CB  . ALA B  1 170 ? -17.452  -6.890  -55.799  1.00 30.10  ? 170 ALA B CB  1 
ATOM   5605  N N   . ASN B  1 171 ? -15.315  -8.273  -58.151  1.00 29.25  ? 171 ASN B N   1 
ATOM   5606  C CA  . ASN B  1 171 ? -15.210  -9.026  -59.392  1.00 29.54  ? 171 ASN B CA  1 
ATOM   5607  C C   . ASN B  1 171 ? -16.349  -10.029 -59.524  1.00 28.46  ? 171 ASN B C   1 
ATOM   5608  O O   . ASN B  1 171 ? -16.587  -10.808 -58.621  1.00 29.22  ? 171 ASN B O   1 
ATOM   5609  C CB  . ASN B  1 171 ? -13.874  -9.752  -59.466  1.00 30.70  ? 171 ASN B CB  1 
ATOM   5610  C CG  . ASN B  1 171 ? -13.623  -10.295 -60.843  1.00 31.33  ? 171 ASN B CG  1 
ATOM   5611  O OD1 . ASN B  1 171 ? -14.361  -11.182 -61.286  1.00 34.46  ? 171 ASN B OD1 1 
ATOM   5612  N ND2 . ASN B  1 171 ? -12.612  -9.774  -61.527  1.00 30.75  ? 171 ASN B ND2 1 
ATOM   5613  N N   . ALA B  1 172 ? -17.023  -10.022 -60.678  1.00 28.71  ? 172 ALA B N   1 
ATOM   5614  C CA  . ALA B  1 172 ? -18.225  -10.809 -60.889  1.00 27.16  ? 172 ALA B CA  1 
ATOM   5615  C C   . ALA B  1 172 ? -17.893  -12.301 -60.892  1.00 28.31  ? 172 ALA B C   1 
ATOM   5616  O O   . ALA B  1 172 ? -18.766  -13.124 -60.635  1.00 29.36  ? 172 ALA B O   1 
ATOM   5617  C CB  . ALA B  1 172 ? -18.902  -10.403 -62.194  1.00 26.14  ? 172 ALA B CB  1 
ATOM   5618  N N   . MET B  1 173 ? -16.642  -12.667 -61.211  1.00 28.40  ? 173 MET B N   1 
ATOM   5619  C CA  . MET B  1 173 ? -16.292  -14.078 -61.293  1.00 28.28  ? 173 MET B CA  1 
ATOM   5620  C C   . MET B  1 173 ? -16.134  -14.711 -59.902  1.00 27.49  ? 173 MET B C   1 
ATOM   5621  O O   . MET B  1 173 ? -16.314  -15.903 -59.769  1.00 28.01  ? 173 MET B O   1 
ATOM   5622  C CB  . MET B  1 173 ? -15.068  -14.271 -62.186  1.00 27.49  ? 173 MET B CB  1 
ATOM   5623  C CG  . MET B  1 173 ? -15.345  -13.987 -63.640  1.00 27.60  ? 173 MET B CG  1 
ATOM   5624  S SD  . MET B  1 173 ? -16.419  -15.215 -64.408  1.00 30.42  ? 173 MET B SD  1 
ATOM   5625  C CE  . MET B  1 173 ? -15.244  -16.576 -64.482  1.00 30.27  ? 173 MET B CE  1 
ATOM   5626  N N   . ILE B  1 174 ? -15.862  -13.929 -58.849  1.00 28.57  ? 174 ILE B N   1 
ATOM   5627  C CA  . ILE B  1 174 ? -15.616  -14.475 -57.521  1.00 28.91  ? 174 ILE B CA  1 
ATOM   5628  C C   . ILE B  1 174 ? -16.621  -13.980 -56.482  1.00 30.81  ? 174 ILE B C   1 
ATOM   5629  O O   . ILE B  1 174 ? -16.707  -14.566 -55.408  1.00 32.14  ? 174 ILE B O   1 
ATOM   5630  C CB  . ILE B  1 174 ? -14.185  -14.142 -57.076  1.00 30.52  ? 174 ILE B CB  1 
ATOM   5631  C CG1 . ILE B  1 174 ? -13.949  -12.637 -57.055  1.00 31.60  ? 174 ILE B CG1 1 
ATOM   5632  C CG2 . ILE B  1 174 ? -13.164  -14.866 -57.956  1.00 30.60  ? 174 ILE B CG2 1 
ATOM   5633  C CD1 . ILE B  1 174 ? -12.734  -12.202 -56.246  1.00 33.20  ? 174 ILE B CD1 1 
ATOM   5634  N N   . SER B  1 175 ? -17.336  -12.875 -56.756  1.00 31.75  ? 175 SER B N   1 
ATOM   5635  C CA  . SER B  1 175 ? -18.271  -12.299 -55.799  1.00 31.79  ? 175 SER B CA  1 
ATOM   5636  C C   . SER B  1 175 ? -19.716  -12.277 -56.324  1.00 30.81  ? 175 SER B C   1 
ATOM   5637  O O   . SER B  1 175 ? -20.595  -11.679 -55.709  1.00 31.14  ? 175 SER B O   1 
ATOM   5638  C CB  . SER B  1 175 ? -17.768  -10.968 -55.343  1.00 33.13  ? 175 SER B CB  1 
ATOM   5639  O OG  . SER B  1 175 ? -16.603  -11.195 -54.564  1.00 33.23  ? 175 SER B OG  1 
ATOM   5640  N N   . ASP B  1 176 ? -19.974  -13.080 -57.365  1.00 30.52  ? 176 ASP B N   1 
ATOM   5641  C CA  . ASP B  1 176 ? -21.301  -13.493 -57.788  1.00 29.12  ? 176 ASP B CA  1 
ATOM   5642  C C   . ASP B  1 176 ? -22.226  -13.852 -56.625  1.00 29.29  ? 176 ASP B C   1 
ATOM   5643  O O   . ASP B  1 176 ? -23.400  -13.536 -56.676  1.00 27.72  ? 176 ASP B O   1 
ATOM   5644  C CB  . ASP B  1 176 ? -21.185  -14.642 -58.778  1.00 28.89  ? 176 ASP B CB  1 
ATOM   5645  C CG  . ASP B  1 176 ? -20.480  -15.898 -58.297  1.00 29.50  ? 176 ASP B CG  1 
ATOM   5646  O OD1 . ASP B  1 176 ? -19.838  -15.861 -57.248  1.00 29.85  ? 176 ASP B OD1 1 
ATOM   5647  O OD2 . ASP B  1 176 ? -20.593  -16.911 -58.983  1.00 29.69  ? 176 ASP B OD2 1 
ATOM   5648  N N   . TYR B  1 177 ? -21.737  -14.551 -55.592  1.00 31.39  ? 177 TYR B N   1 
ATOM   5649  C CA  . TYR B  1 177 ? -22.607  -14.997 -54.499  1.00 32.58  ? 177 TYR B CA  1 
ATOM   5650  C C   . TYR B  1 177 ? -23.030  -13.870 -53.543  1.00 32.85  ? 177 TYR B C   1 
ATOM   5651  O O   . TYR B  1 177 ? -23.931  -14.062 -52.738  1.00 31.48  ? 177 TYR B O   1 
ATOM   5652  C CB  . TYR B  1 177 ? -21.898  -16.038 -53.629  1.00 33.68  ? 177 TYR B CB  1 
ATOM   5653  C CG  . TYR B  1 177 ? -20.688  -15.489 -52.897  1.00 33.20  ? 177 TYR B CG  1 
ATOM   5654  C CD1 . TYR B  1 177 ? -19.444  -15.387 -53.518  1.00 34.42  ? 177 TYR B CD1 1 
ATOM   5655  C CD2 . TYR B  1 177 ? -20.787  -15.066 -51.586  1.00 33.55  ? 177 TYR B CD2 1 
ATOM   5656  C CE1 . TYR B  1 177 ? -18.341  -14.854 -52.861  1.00 31.89  ? 177 TYR B CE1 1 
ATOM   5657  C CE2 . TYR B  1 177 ? -19.691  -14.538 -50.915  1.00 34.72  ? 177 TYR B CE2 1 
ATOM   5658  C CZ  . TYR B  1 177 ? -18.466  -14.425 -51.554  1.00 33.15  ? 177 TYR B CZ  1 
ATOM   5659  O OH  . TYR B  1 177 ? -17.390  -13.871 -50.896  1.00 34.97  ? 177 TYR B OH  1 
ATOM   5660  N N   . MET B  1 178 ? -22.358  -12.710 -53.582  1.00 33.95  ? 178 MET B N   1 
ATOM   5661  C CA  . MET B  1 178 ? -22.433  -11.732 -52.512  1.00 33.72  ? 178 MET B CA  1 
ATOM   5662  C C   . MET B  1 178 ? -23.738  -10.927 -52.590  1.00 34.27  ? 178 MET B C   1 
ATOM   5663  O O   . MET B  1 178 ? -24.198  -10.558 -53.672  1.00 34.38  ? 178 MET B O   1 
ATOM   5664  C CB  . MET B  1 178 ? -21.230  -10.780 -52.597  1.00 34.21  ? 178 MET B CB  1 
ATOM   5665  C CG  . MET B  1 178 ? -21.212  -9.665  -51.554  1.00 33.69  ? 178 MET B CG  1 
ATOM   5666  S SD  . MET B  1 178 ? -19.821  -8.555  -51.812  1.00 35.16  ? 178 MET B SD  1 
ATOM   5667  C CE  . MET B  1 178 ? -18.423  -9.610  -51.411  1.00 35.66  ? 178 MET B CE  1 
ATOM   5668  N N   . ASP B  1 179 ? -24.285  -10.644 -51.402  1.00 33.30  ? 179 ASP B N   1 
ATOM   5669  C CA  . ASP B  1 179 ? -25.368  -9.707  -51.202  1.00 33.32  ? 179 ASP B CA  1 
ATOM   5670  C C   . ASP B  1 179 ? -24.868  -8.263  -51.279  1.00 31.13  ? 179 ASP B C   1 
ATOM   5671  O O   . ASP B  1 179 ? -24.206  -7.775  -50.371  1.00 30.98  ? 179 ASP B O   1 
ATOM   5672  C CB  . ASP B  1 179 ? -26.011  -9.910  -49.846  1.00 34.22  ? 179 ASP B CB  1 
ATOM   5673  C CG  . ASP B  1 179 ? -27.267  -9.074  -49.637  1.00 39.88  ? 179 ASP B CG  1 
ATOM   5674  O OD1 . ASP B  1 179 ? -27.734  -8.415  -50.594  1.00 40.46  ? 179 ASP B OD1 1 
ATOM   5675  O OD2 . ASP B  1 179 ? -27.798  -9.103  -48.522  1.00 49.54  ? 179 ASP B OD2 1 
ATOM   5676  N N   . GLU B  1 180 ? -25.315  -7.547  -52.316  1.00 30.82  ? 180 GLU B N   1 
ATOM   5677  C CA  . GLU B  1 180 ? -24.988  -6.146  -52.544  1.00 29.33  ? 180 GLU B CA  1 
ATOM   5678  C C   . GLU B  1 180 ? -26.156  -5.229  -52.163  1.00 29.73  ? 180 GLU B C   1 
ATOM   5679  O O   . GLU B  1 180 ? -26.120  -4.027  -52.415  1.00 30.82  ? 180 GLU B O   1 
ATOM   5680  C CB  . GLU B  1 180 ? -24.629  -5.894  -54.013  1.00 28.97  ? 180 GLU B CB  1 
ATOM   5681  C CG  . GLU B  1 180 ? -23.272  -6.458  -54.449  1.00 30.40  ? 180 GLU B CG  1 
ATOM   5682  C CD  . GLU B  1 180 ? -22.687  -5.836  -55.708  1.00 31.08  ? 180 GLU B CD  1 
ATOM   5683  O OE1 . GLU B  1 180 ? -23.378  -4.906  -56.251  1.00 29.73  ? 180 GLU B OE1 1 
ATOM   5684  O OE2 . GLU B  1 180 ? -21.567  -6.257  -56.124  1.00 28.59  ? 180 GLU B OE2 1 
ATOM   5685  N N   . SER B  1 181 ? -27.170  -5.771  -51.505  1.00 29.27  ? 181 SER B N   1 
ATOM   5686  C CA  . SER B  1 181 ? -28.370  -4.997  -51.253  1.00 30.81  ? 181 SER B CA  1 
ATOM   5687  C C   . SER B  1 181 ? -28.100  -3.966  -50.169  1.00 31.41  ? 181 SER B C   1 
ATOM   5688  O O   . SER B  1 181 ? -28.908  -3.083  -49.989  1.00 34.82  ? 181 SER B O   1 
ATOM   5689  C CB  . SER B  1 181 ? -29.588  -5.889  -50.937  1.00 29.54  ? 181 SER B CB  1 
ATOM   5690  O OG  . SER B  1 181 ? -29.447  -6.371  -49.626  1.00 29.95  ? 181 SER B OG  1 
ATOM   5691  N N   . ILE B  1 182 ? -26.946  -4.026  -49.490  1.00 32.34  ? 182 ILE B N   1 
ATOM   5692  C CA  . ILE B  1 182 ? -26.597  -3.043  -48.469  1.00 31.10  ? 182 ILE B CA  1 
ATOM   5693  C C   . ILE B  1 182 ? -26.046  -1.768  -49.112  1.00 30.52  ? 182 ILE B C   1 
ATOM   5694  O O   . ILE B  1 182 ? -25.973  -0.750  -48.436  1.00 30.10  ? 182 ILE B O   1 
ATOM   5695  C CB  . ILE B  1 182 ? -25.586  -3.619  -47.469  1.00 31.66  ? 182 ILE B CB  1 
ATOM   5696  C CG1 . ILE B  1 182 ? -24.268  -4.022  -48.166  1.00 32.44  ? 182 ILE B CG1 1 
ATOM   5697  C CG2 . ILE B  1 182 ? -26.207  -4.784  -46.682  1.00 32.36  ? 182 ILE B CG2 1 
ATOM   5698  C CD1 . ILE B  1 182 ? -23.254  -4.738  -47.272  1.00 32.18  ? 182 ILE B CD1 1 
ATOM   5699  N N   . PHE B  1 183 ? -25.651  -1.831  -50.391  1.00 29.65  ? 183 PHE B N   1 
ATOM   5700  C CA  . PHE B  1 183 ? -25.094  -0.677  -51.081  1.00 31.47  ? 183 PHE B CA  1 
ATOM   5701  C C   . PHE B  1 183 ? -26.161  0.111   -51.850  1.00 32.10  ? 183 PHE B C   1 
ATOM   5702  O O   . PHE B  1 183 ? -27.285  -0.327  -52.054  1.00 33.70  ? 183 PHE B O   1 
ATOM   5703  C CB  . PHE B  1 183 ? -23.993  -1.113  -52.034  1.00 29.89  ? 183 PHE B CB  1 
ATOM   5704  C CG  . PHE B  1 183 ? -22.932  -1.976  -51.373  1.00 31.23  ? 183 PHE B CG  1 
ATOM   5705  C CD1 . PHE B  1 183 ? -21.976  -1.413  -50.548  1.00 31.80  ? 183 PHE B CD1 1 
ATOM   5706  C CD2 . PHE B  1 183 ? -22.844  -3.333  -51.645  1.00 30.83  ? 183 PHE B CD2 1 
ATOM   5707  C CE1 . PHE B  1 183 ? -20.997  -2.197  -49.953  1.00 32.42  ? 183 PHE B CE1 1 
ATOM   5708  C CE2 . PHE B  1 183 ? -21.859  -4.103  -51.050  1.00 33.17  ? 183 PHE B CE2 1 
ATOM   5709  C CZ  . PHE B  1 183 ? -20.928  -3.533  -50.220  1.00 32.24  ? 183 PHE B CZ  1 
ATOM   5710  N N   . ASP B  1 184 ? -25.792  1.289   -52.311  1.00 30.21  ? 184 ASP B N   1 
ATOM   5711  C CA  . ASP B  1 184 ? -26.767  2.132   -52.964  1.00 31.22  ? 184 ASP B CA  1 
ATOM   5712  C C   . ASP B  1 184 ? -26.888  1.737   -54.426  1.00 31.00  ? 184 ASP B C   1 
ATOM   5713  O O   . ASP B  1 184 ? -27.889  2.052   -55.051  1.00 32.16  ? 184 ASP B O   1 
ATOM   5714  C CB  . ASP B  1 184 ? -26.431  3.607   -52.813  1.00 29.94  ? 184 ASP B CB  1 
ATOM   5715  C CG  . ASP B  1 184 ? -26.301  4.046   -51.370  1.00 30.95  ? 184 ASP B CG  1 
ATOM   5716  O OD1 . ASP B  1 184 ? -27.112  3.571   -50.554  1.00 32.15  ? 184 ASP B OD1 1 
ATOM   5717  O OD2 . ASP B  1 184 ? -25.357  4.800   -51.065  1.00 32.53  ? 184 ASP B OD2 1 
ATOM   5718  N N   . VAL B  1 185 ? -25.839  1.128   -54.982  1.00 31.37  ? 185 VAL B N   1 
ATOM   5719  C CA  . VAL B  1 185 ? -25.868  0.749   -56.383  1.00 30.90  ? 185 VAL B CA  1 
ATOM   5720  C C   . VAL B  1 185 ? -25.109  -0.567  -56.526  1.00 30.04  ? 185 VAL B C   1 
ATOM   5721  O O   . VAL B  1 185 ? -24.154  -0.845  -55.779  1.00 28.13  ? 185 VAL B O   1 
ATOM   5722  C CB  . VAL B  1 185 ? -25.360  1.791   -57.405  1.00 32.17  ? 185 VAL B CB  1 
ATOM   5723  C CG1 . VAL B  1 185 ? -25.719  3.234   -57.050  1.00 32.06  ? 185 VAL B CG1 1 
ATOM   5724  C CG2 . VAL B  1 185 ? -23.883  1.676   -57.636  1.00 32.47  ? 185 VAL B CG2 1 
ATOM   5725  N N   . TYR B  1 186 ? -25.577  -1.369  -57.495  1.00 28.80  ? 186 TYR B N   1 
ATOM   5726  C CA  . TYR B  1 186 ? -25.011  -2.676  -57.762  1.00 27.70  ? 186 TYR B CA  1 
ATOM   5727  C C   . TYR B  1 186 ? -23.806  -2.466  -58.661  1.00 28.80  ? 186 TYR B C   1 
ATOM   5728  O O   . TYR B  1 186 ? -23.853  -1.635  -59.563  1.00 30.98  ? 186 TYR B O   1 
ATOM   5729  C CB  . TYR B  1 186 ? -26.051  -3.589  -58.396  1.00 27.20  ? 186 TYR B CB  1 
ATOM   5730  C CG  . TYR B  1 186 ? -27.224  -3.926  -57.486  1.00 28.09  ? 186 TYR B CG  1 
ATOM   5731  C CD1 . TYR B  1 186 ? -27.027  -4.352  -56.180  1.00 27.66  ? 186 TYR B CD1 1 
ATOM   5732  C CD2 . TYR B  1 186 ? -28.537  -3.831  -57.944  1.00 29.07  ? 186 TYR B CD2 1 
ATOM   5733  C CE1 . TYR B  1 186 ? -28.089  -4.681  -55.358  1.00 27.89  ? 186 TYR B CE1 1 
ATOM   5734  C CE2 . TYR B  1 186 ? -29.613  -4.138  -57.131  1.00 28.57  ? 186 TYR B CE2 1 
ATOM   5735  C CZ  . TYR B  1 186 ? -29.387  -4.559  -55.832  1.00 28.92  ? 186 TYR B CZ  1 
ATOM   5736  O OH  . TYR B  1 186 ? -30.443  -4.851  -55.017  1.00 28.22  ? 186 TYR B OH  1 
ATOM   5737  N N   . ALA B  1 187 ? -22.725  -3.212  -58.407  1.00 29.97  ? 187 ALA B N   1 
ATOM   5738  C CA  . ALA B  1 187 ? -21.509  -3.020  -59.182  1.00 30.06  ? 187 ALA B CA  1 
ATOM   5739  C C   . ALA B  1 187 ? -20.718  -4.318  -59.241  1.00 28.42  ? 187 ALA B C   1 
ATOM   5740  O O   . ALA B  1 187 ? -20.700  -5.059  -58.269  1.00 27.54  ? 187 ALA B O   1 
ATOM   5741  C CB  . ALA B  1 187 ? -20.691  -1.893  -58.589  1.00 29.86  ? 187 ALA B CB  1 
ATOM   5742  N N   . TYR B  1 188 ? -20.066  -4.540  -60.390  1.00 28.38  ? 188 TYR B N   1 
ATOM   5743  C CA  . TYR B  1 188 ? -19.064  -5.575  -60.550  1.00 29.72  ? 188 TYR B CA  1 
ATOM   5744  C C   . TYR B  1 188 ? -17.891  -5.112  -61.430  1.00 30.69  ? 188 TYR B C   1 
ATOM   5745  O O   . TYR B  1 188 ? -18.051  -4.293  -62.331  1.00 29.53  ? 188 TYR B O   1 
ATOM   5746  C CB  . TYR B  1 188 ? -19.718  -6.822  -61.167  1.00 30.33  ? 188 TYR B CB  1 
ATOM   5747  C CG  . TYR B  1 188 ? -20.816  -7.436  -60.318  1.00 27.99  ? 188 TYR B CG  1 
ATOM   5748  C CD1 . TYR B  1 188 ? -20.538  -7.954  -59.077  1.00 28.03  ? 188 TYR B CD1 1 
ATOM   5749  C CD2 . TYR B  1 188 ? -22.113  -7.536  -60.775  1.00 31.09  ? 188 TYR B CD2 1 
ATOM   5750  C CE1 . TYR B  1 188 ? -21.525  -8.525  -58.295  1.00 30.47  ? 188 TYR B CE1 1 
ATOM   5751  C CE2 . TYR B  1 188 ? -23.119  -8.123  -60.010  1.00 32.18  ? 188 TYR B CE2 1 
ATOM   5752  C CZ  . TYR B  1 188 ? -22.827  -8.601  -58.749  1.00 30.67  ? 188 TYR B CZ  1 
ATOM   5753  O OH  . TYR B  1 188 ? -23.788  -9.178  -57.962  1.00 31.19  ? 188 TYR B OH  1 
ATOM   5754  N N   . ASN B  1 189 ? -16.714  -5.725  -61.185  1.00 32.24  ? 189 ASN B N   1 
ATOM   5755  C CA  . ASN B  1 189 ? -15.638  -5.886  -62.157  1.00 30.37  ? 189 ASN B CA  1 
ATOM   5756  C C   . ASN B  1 189 ? -15.958  -7.064  -63.089  1.00 29.30  ? 189 ASN B C   1 
ATOM   5757  O O   . ASN B  1 189 ? -16.130  -8.199  -62.660  1.00 31.61  ? 189 ASN B O   1 
ATOM   5758  C CB  . ASN B  1 189 ? -14.291  -6.022  -61.443  1.00 31.13  ? 189 ASN B CB  1 
ATOM   5759  C CG  . ASN B  1 189 ? -13.984  -4.860  -60.511  1.00 32.30  ? 189 ASN B CG  1 
ATOM   5760  O OD1 . ASN B  1 189 ? -13.521  -5.071  -59.381  1.00 38.17  ? 189 ASN B OD1 1 
ATOM   5761  N ND2 . ASN B  1 189 ? -14.157  -3.628  -60.955  1.00 29.30  ? 189 ASN B ND2 1 
ATOM   5762  N N   . CYS B  1 190 ? -16.044  -6.795  -64.390  1.00 28.32  ? 190 CYS B N   1 
ATOM   5763  C CA  . CYS B  1 190 ? -16.669  -7.701  -65.336  1.00 27.64  ? 190 CYS B CA  1 
ATOM   5764  C C   . CYS B  1 190 ? -15.663  -8.019  -66.444  1.00 28.32  ? 190 CYS B C   1 
ATOM   5765  O O   . CYS B  1 190 ? -15.329  -7.111  -67.191  1.00 27.29  ? 190 CYS B O   1 
ATOM   5766  C CB  . CYS B  1 190 ? -17.932  -7.063  -65.918  1.00 26.50  ? 190 CYS B CB  1 
ATOM   5767  S SG  . CYS B  1 190 ? -19.235  -6.737  -64.696  1.00 28.64  ? 190 CYS B SG  1 
ATOM   5768  N N   . TYR B  1 191 ? -15.134  -9.260  -66.512  1.00 25.88  ? 191 TYR B N   1 
ATOM   5769  C CA  . TYR B  1 191 ? -14.194  -9.608  -67.563  1.00 26.17  ? 191 TYR B CA  1 
ATOM   5770  C C   . TYR B  1 191 ? -14.770  -10.771 -68.372  1.00 27.00  ? 191 TYR B C   1 
ATOM   5771  O O   . TYR B  1 191 ? -15.422  -11.648 -67.818  1.00 28.25  ? 191 TYR B O   1 
ATOM   5772  C CB  . TYR B  1 191 ? -12.779  -9.910  -67.032  1.00 27.78  ? 191 TYR B CB  1 
ATOM   5773  C CG  . TYR B  1 191 ? -11.994  -8.699  -66.546  1.00 26.10  ? 191 TYR B CG  1 
ATOM   5774  C CD1 . TYR B  1 191 ? -11.261  -7.933  -67.422  1.00 25.52  ? 191 TYR B CD1 1 
ATOM   5775  C CD2 . TYR B  1 191 ? -12.117  -8.243  -65.243  1.00 27.03  ? 191 TYR B CD2 1 
ATOM   5776  C CE1 . TYR B  1 191 ? -10.623  -6.784  -67.008  1.00 26.50  ? 191 TYR B CE1 1 
ATOM   5777  C CE2 . TYR B  1 191 ? -11.481  -7.092  -64.811  1.00 26.57  ? 191 TYR B CE2 1 
ATOM   5778  C CZ  . TYR B  1 191 ? -10.720  -6.362  -65.692  1.00 27.64  ? 191 TYR B CZ  1 
ATOM   5779  O OH  . TYR B  1 191 ? -10.084  -5.223  -65.231  1.00 29.12  ? 191 TYR B OH  1 
ATOM   5780  N N   . ASP B  1 192 ? -14.524  -10.741 -69.689  1.00 27.37  ? 192 ASP B N   1 
ATOM   5781  C CA  . ASP B  1 192 ? -15.021  -11.727 -70.626  1.00 28.85  ? 192 ASP B CA  1 
ATOM   5782  C C   . ASP B  1 192 ? -13.823  -12.494 -71.182  1.00 29.22  ? 192 ASP B C   1 
ATOM   5783  O O   . ASP B  1 192 ? -13.226  -12.100 -72.172  1.00 30.05  ? 192 ASP B O   1 
ATOM   5784  C CB  . ASP B  1 192 ? -15.891  -11.132 -71.726  1.00 29.92  ? 192 ASP B CB  1 
ATOM   5785  C CG  . ASP B  1 192 ? -16.418  -12.147 -72.734  1.00 30.76  ? 192 ASP B CG  1 
ATOM   5786  O OD1 . ASP B  1 192 ? -16.269  -13.359 -72.459  1.00 33.06  ? 192 ASP B OD1 1 
ATOM   5787  O OD2 . ASP B  1 192 ? -16.966  -11.736 -73.783  1.00 30.76  ? 192 ASP B OD2 1 
ATOM   5788  N N   . HIS B  1 193 ? -13.487  -13.597 -70.513  1.00 28.83  ? 193 HIS B N   1 
ATOM   5789  C CA  . HIS B  1 193 ? -12.405  -14.456 -70.940  1.00 29.27  ? 193 HIS B CA  1 
ATOM   5790  C C   . HIS B  1 193 ? -12.929  -15.821 -71.403  1.00 30.03  ? 193 HIS B C   1 
ATOM   5791  O O   . HIS B  1 193 ? -12.117  -16.709 -71.704  1.00 27.36  ? 193 HIS B O   1 
ATOM   5792  C CB  . HIS B  1 193 ? -11.458  -14.698 -69.773  1.00 28.16  ? 193 HIS B CB  1 
ATOM   5793  C CG  . HIS B  1 193 ? -10.817  -13.491 -69.239  1.00 27.88  ? 193 HIS B CG  1 
ATOM   5794  N ND1 . HIS B  1 193 ? -10.782  -13.270 -67.885  1.00 27.29  ? 193 HIS B ND1 1 
ATOM   5795  C CD2 . HIS B  1 193 ? -10.163  -12.457 -69.826  1.00 28.47  ? 193 HIS B CD2 1 
ATOM   5796  C CE1 . HIS B  1 193 ? -10.114  -12.145 -67.657  1.00 29.12  ? 193 HIS B CE1 1 
ATOM   5797  N NE2 . HIS B  1 193 ? -9.733   -11.639 -68.824  1.00 28.94  ? 193 HIS B NE2 1 
ATOM   5798  N N   . ASN B  1 194 ? -14.264  -15.952 -71.513  1.00 28.41  ? 194 ASN B N   1 
ATOM   5799  C CA  . ASN B  1 194 ? -14.885  -17.125 -72.121  1.00 28.52  ? 194 ASN B CA  1 
ATOM   5800  C C   . ASN B  1 194 ? -14.424  -18.405 -71.424  1.00 28.42  ? 194 ASN B C   1 
ATOM   5801  O O   . ASN B  1 194 ? -13.879  -19.316 -72.030  1.00 29.62  ? 194 ASN B O   1 
ATOM   5802  C CB  . ASN B  1 194 ? -14.658  -17.150 -73.623  1.00 29.07  ? 194 ASN B CB  1 
ATOM   5803  C CG  . ASN B  1 194 ? -15.415  -18.246 -74.334  1.00 30.19  ? 194 ASN B CG  1 
ATOM   5804  O OD1 . ASN B  1 194 ? -16.500  -18.663 -73.930  1.00 30.77  ? 194 ASN B OD1 1 
ATOM   5805  N ND2 . ASN B  1 194 ? -14.813  -18.794 -75.369  1.00 31.95  ? 194 ASN B ND2 1 
ATOM   5806  N N   . GLU B  1 195 ? -14.693  -18.451 -70.125  1.00 28.73  ? 195 GLU B N   1 
ATOM   5807  C CA  . GLU B  1 195 ? -14.328  -19.546 -69.251  1.00 30.27  ? 195 GLU B CA  1 
ATOM   5808  C C   . GLU B  1 195 ? -15.261  -19.455 -68.044  1.00 30.24  ? 195 GLU B C   1 
ATOM   5809  O O   . GLU B  1 195 ? -15.694  -18.374 -67.671  1.00 28.90  ? 195 GLU B O   1 
ATOM   5810  C CB  . GLU B  1 195 ? -12.862  -19.530 -68.816  1.00 30.31  ? 195 GLU B CB  1 
ATOM   5811  C CG  . GLU B  1 195 ? -12.526  -18.303 -67.971  1.00 31.34  ? 195 GLU B CG  1 
ATOM   5812  C CD  . GLU B  1 195 ? -11.061  -18.087 -67.657  1.00 31.26  ? 195 GLU B CD  1 
ATOM   5813  O OE1 . GLU B  1 195 ? -10.188  -18.788 -68.184  1.00 32.53  ? 195 GLU B OE1 1 
ATOM   5814  O OE2 . GLU B  1 195 ? -10.826  -17.229 -66.800  1.00 31.26  ? 195 GLU B OE2 1 
ATOM   5815  N N   . GLY B  1 196 ? -15.564  -20.616 -67.453  1.00 31.64  ? 196 GLY B N   1 
ATOM   5816  C CA  . GLY B  1 196 ? -16.466  -20.722 -66.325  1.00 29.62  ? 196 GLY B CA  1 
ATOM   5817  C C   . GLY B  1 196 ? -17.812  -20.133 -66.681  1.00 28.19  ? 196 GLY B C   1 
ATOM   5818  O O   . GLY B  1 196 ? -18.355  -20.426 -67.721  1.00 28.27  ? 196 GLY B O   1 
ATOM   5819  N N   . GLN B  1 197 ? -18.280  -19.238 -65.822  1.00 28.68  ? 197 GLN B N   1 
ATOM   5820  C CA  . GLN B  1 197 ? -19.546  -18.565 -65.978  1.00 28.95  ? 197 GLN B CA  1 
ATOM   5821  C C   . GLN B  1 197 ? -19.666  -17.901 -67.357  1.00 28.67  ? 197 GLN B C   1 
ATOM   5822  O O   . GLN B  1 197 ? -20.788  -17.832 -67.879  1.00 28.96  ? 197 GLN B O   1 
ATOM   5823  C CB  . GLN B  1 197 ? -19.705  -17.530 -64.853  1.00 29.12  ? 197 GLN B CB  1 
ATOM   5824  C CG  . GLN B  1 197 ? -19.774  -18.097 -63.439  1.00 28.34  ? 197 GLN B CG  1 
ATOM   5825  C CD  . GLN B  1 197 ? -18.432  -18.138 -62.746  1.00 29.40  ? 197 GLN B CD  1 
ATOM   5826  O OE1 . GLN B  1 197 ? -17.476  -18.716 -63.267  1.00 31.36  ? 197 GLN B OE1 1 
ATOM   5827  N NE2 . GLN B  1 197 ? -18.339  -17.571 -61.550  1.00 28.90  ? 197 GLN B NE2 1 
ATOM   5828  N N   . THR B  1 198 ? -18.566  -17.348 -67.922  1.00 27.58  ? 198 THR B N   1 
ATOM   5829  C CA  . THR B  1 198 ? -18.685  -16.554 -69.140  1.00 27.02  ? 198 THR B CA  1 
ATOM   5830  C C   . THR B  1 198 ? -18.612  -17.447 -70.373  1.00 29.44  ? 198 THR B C   1 
ATOM   5831  O O   . THR B  1 198 ? -18.986  -16.992 -71.461  1.00 31.75  ? 198 THR B O   1 
ATOM   5832  C CB  . THR B  1 198 ? -17.678  -15.407 -69.232  1.00 27.31  ? 198 THR B CB  1 
ATOM   5833  O OG1 . THR B  1 198 ? -16.318  -15.840 -69.144  1.00 26.39  ? 198 THR B OG1 1 
ATOM   5834  C CG2 . THR B  1 198 ? -17.928  -14.360 -68.164  1.00 26.61  ? 198 THR B CG2 1 
ATOM   5835  N N   . ALA B  1 199 ? -18.144  -18.699 -70.210  1.00 29.24  ? 199 ALA B N   1 
ATOM   5836  C CA  . ALA B  1 199 ? -18.209  -19.717 -71.263  1.00 30.55  ? 199 ALA B CA  1 
ATOM   5837  C C   . ALA B  1 199 ? -19.608  -20.357 -71.314  1.00 31.63  ? 199 ALA B C   1 
ATOM   5838  O O   . ALA B  1 199 ? -20.097  -20.676 -72.407  1.00 31.01  ? 199 ALA B O   1 
ATOM   5839  C CB  . ALA B  1 199 ? -17.148  -20.813 -71.053  1.00 30.33  ? 199 ALA B CB  1 
ATOM   5840  N N   . THR B  1 200 ? -20.225  -20.575 -70.135  1.00 30.48  ? 200 THR B N   1 
ATOM   5841  C CA  . THR B  1 200 ? -21.516  -21.246 -70.075  1.00 32.13  ? 200 THR B CA  1 
ATOM   5842  C C   . THR B  1 200 ? -22.646  -20.262 -70.410  1.00 32.48  ? 200 THR B C   1 
ATOM   5843  O O   . THR B  1 200 ? -23.410  -20.520 -71.320  1.00 33.04  ? 200 THR B O   1 
ATOM   5844  C CB  . THR B  1 200 ? -21.687  -21.922 -68.718  1.00 32.11  ? 200 THR B CB  1 
ATOM   5845  O OG1 . THR B  1 200 ? -21.536  -20.945 -67.690  1.00 29.40  ? 200 THR B OG1 1 
ATOM   5846  C CG2 . THR B  1 200 ? -20.652  -23.027 -68.517  1.00 32.57  ? 200 THR B CG2 1 
ATOM   5847  N N   . MET B  1 201 ? -22.740  -19.119 -69.728  1.00 31.10  ? 201 MET B N   1 
ATOM   5848  C CA  . MET B  1 201 ? -23.882  -18.226 -69.926  1.00 31.63  ? 201 MET B CA  1 
ATOM   5849  C C   . MET B  1 201 ? -23.585  -17.139 -70.960  1.00 29.97  ? 201 MET B C   1 
ATOM   5850  O O   . MET B  1 201 ? -24.505  -16.482 -71.428  1.00 29.17  ? 201 MET B O   1 
ATOM   5851  C CB  . MET B  1 201 ? -24.261  -17.555 -68.601  1.00 31.42  ? 201 MET B CB  1 
ATOM   5852  C CG  . MET B  1 201 ? -24.872  -18.504 -67.613  1.00 30.77  ? 201 MET B CG  1 
ATOM   5853  S SD  . MET B  1 201 ? -24.822  -17.965 -65.899  1.00 32.24  ? 201 MET B SD  1 
ATOM   5854  C CE  . MET B  1 201 ? -23.122  -18.503 -65.607  1.00 32.25  ? 201 MET B CE  1 
ATOM   5855  N N   . GLY B  1 202 ? -22.301  -16.972 -71.335  1.00 29.67  ? 202 GLY B N   1 
ATOM   5856  C CA  . GLY B  1 202 ? -21.875  -15.863 -72.168  1.00 26.89  ? 202 GLY B CA  1 
ATOM   5857  C C   . GLY B  1 202 ? -21.806  -14.611 -71.302  1.00 26.63  ? 202 GLY B C   1 
ATOM   5858  O O   . GLY B  1 202 ? -22.339  -14.588 -70.204  1.00 27.62  ? 202 GLY B O   1 
ATOM   5859  N N   . PHE B  1 203 ? -21.207  -13.545 -71.818  1.00 27.00  ? 203 PHE B N   1 
ATOM   5860  C CA  . PHE B  1 203 ? -20.812  -12.432 -70.974  1.00 26.24  ? 203 PHE B CA  1 
ATOM   5861  C C   . PHE B  1 203 ? -22.037  -11.603 -70.630  1.00 26.42  ? 203 PHE B C   1 
ATOM   5862  O O   . PHE B  1 203 ? -22.259  -11.320 -69.470  1.00 27.59  ? 203 PHE B O   1 
ATOM   5863  C CB  . PHE B  1 203 ? -19.744  -11.590 -71.676  1.00 25.58  ? 203 PHE B CB  1 
ATOM   5864  C CG  . PHE B  1 203 ? -19.108  -10.485 -70.850  1.00 25.27  ? 203 PHE B CG  1 
ATOM   5865  C CD1 . PHE B  1 203 ? -18.676  -10.717 -69.552  1.00 26.09  ? 203 PHE B CD1 1 
ATOM   5866  C CD2 . PHE B  1 203 ? -18.874  -9.219  -71.411  1.00 26.53  ? 203 PHE B CD2 1 
ATOM   5867  C CE1 . PHE B  1 203 ? -17.989  -9.718  -68.856  1.00 28.07  ? 203 PHE B CE1 1 
ATOM   5868  C CE2 . PHE B  1 203 ? -18.216  -8.220  -70.701  1.00 24.24  ? 203 PHE B CE2 1 
ATOM   5869  C CZ  . PHE B  1 203 ? -17.774  -8.468  -69.434  1.00 24.55  ? 203 PHE B CZ  1 
ATOM   5870  N N   . LYS B  1 204 ? -22.808  -11.178 -71.634  1.00 27.98  ? 204 LYS B N   1 
ATOM   5871  C CA  . LYS B  1 204 ? -24.057  -10.466 -71.376  1.00 28.18  ? 204 LYS B CA  1 
ATOM   5872  C C   . LYS B  1 204 ? -24.921  -11.218 -70.361  1.00 28.70  ? 204 LYS B C   1 
ATOM   5873  O O   . LYS B  1 204 ? -25.269  -10.725 -69.278  1.00 28.52  ? 204 LYS B O   1 
ATOM   5874  C CB  . LYS B  1 204 ? -24.870  -10.296 -72.663  1.00 26.59  ? 204 LYS B CB  1 
ATOM   5875  C CG  . LYS B  1 204 ? -26.241  -9.681  -72.441  1.00 26.38  ? 204 LYS B CG  1 
ATOM   5876  C CD  . LYS B  1 204 ? -27.195  -9.806  -73.618  1.00 25.84  ? 204 LYS B CD  1 
ATOM   5877  C CE  . LYS B  1 204 ? -28.604  -9.575  -73.250  1.00 26.45  ? 204 LYS B CE  1 
ATOM   5878  N NZ  . LYS B  1 204 ? -29.459  -9.859  -74.400  1.00 27.66  ? 204 LYS B NZ  1 
ATOM   5879  N N   . ASP B  1 205 ? -25.316  -12.426 -70.729  1.00 30.62  ? 205 ASP B N   1 
ATOM   5880  C CA  . ASP B  1 205 ? -26.264  -13.168 -69.916  1.00 30.33  ? 205 ASP B CA  1 
ATOM   5881  C C   . ASP B  1 205 ? -25.700  -13.478 -68.521  1.00 29.08  ? 205 ASP B C   1 
ATOM   5882  O O   . ASP B  1 205 ? -26.431  -13.473 -67.533  1.00 29.15  ? 205 ASP B O   1 
ATOM   5883  C CB  . ASP B  1 205 ? -26.790  -14.369 -70.682  1.00 31.76  ? 205 ASP B CB  1 
ATOM   5884  C CG  . ASP B  1 205 ? -27.841  -14.079 -71.746  1.00 31.75  ? 205 ASP B CG  1 
ATOM   5885  O OD1 . ASP B  1 205 ? -28.046  -12.891 -72.080  1.00 29.21  ? 205 ASP B OD1 1 
ATOM   5886  O OD2 . ASP B  1 205 ? -28.420  -15.070 -72.261  1.00 32.80  ? 205 ASP B OD2 1 
ATOM   5887  N N   . TYR B  1 206 ? -24.400  -13.722 -68.373  1.00 28.99  ? 206 TYR B N   1 
ATOM   5888  C CA  . TYR B  1 206 ? -23.904  -13.935 -67.015  1.00 30.84  ? 206 TYR B CA  1 
ATOM   5889  C C   . TYR B  1 206 ? -24.132  -12.706 -66.113  1.00 29.25  ? 206 TYR B C   1 
ATOM   5890  O O   . TYR B  1 206 ? -24.657  -12.823 -65.010  1.00 28.35  ? 206 TYR B O   1 
ATOM   5891  C CB  . TYR B  1 206 ? -22.419  -14.282 -66.982  1.00 30.70  ? 206 TYR B CB  1 
ATOM   5892  C CG  . TYR B  1 206 ? -21.839  -14.456 -65.586  1.00 29.78  ? 206 TYR B CG  1 
ATOM   5893  C CD1 . TYR B  1 206 ? -22.460  -15.238 -64.621  1.00 29.63  ? 206 TYR B CD1 1 
ATOM   5894  C CD2 . TYR B  1 206 ? -20.655  -13.806 -65.253  1.00 29.54  ? 206 TYR B CD2 1 
ATOM   5895  C CE1 . TYR B  1 206 ? -21.892  -15.387 -63.368  1.00 30.75  ? 206 TYR B CE1 1 
ATOM   5896  C CE2 . TYR B  1 206 ? -20.075  -13.959 -64.015  1.00 29.09  ? 206 TYR B CE2 1 
ATOM   5897  C CZ  . TYR B  1 206 ? -20.696  -14.746 -63.071  1.00 30.31  ? 206 TYR B CZ  1 
ATOM   5898  O OH  . TYR B  1 206 ? -20.076  -14.830 -61.858  1.00 31.41  ? 206 TYR B OH  1 
ATOM   5899  N N   . ILE B  1 207 ? -23.745  -11.522 -66.584  1.00 29.25  ? 207 ILE B N   1 
ATOM   5900  C CA  . ILE B  1 207 ? -23.835  -10.298 -65.794  1.00 30.00  ? 207 ILE B CA  1 
ATOM   5901  C C   . ILE B  1 207 ? -25.292  -9.857  -65.645  1.00 28.84  ? 207 ILE B C   1 
ATOM   5902  O O   . ILE B  1 207 ? -25.703  -9.356  -64.602  1.00 27.68  ? 207 ILE B O   1 
ATOM   5903  C CB  . ILE B  1 207 ? -22.962  -9.217  -66.446  1.00 30.00  ? 207 ILE B CB  1 
ATOM   5904  C CG1 . ILE B  1 207 ? -21.482  -9.679  -66.529  1.00 32.00  ? 207 ILE B CG1 1 
ATOM   5905  C CG2 . ILE B  1 207 ? -23.099  -7.892  -65.707  1.00 29.11  ? 207 ILE B CG2 1 
ATOM   5906  C CD1 . ILE B  1 207 ? -20.958  -10.246 -65.220  1.00 32.84  ? 207 ILE B CD1 1 
ATOM   5907  N N   . LYS B  1 208 ? -26.085  -10.073 -66.690  1.00 30.62  ? 208 LYS B N   1 
ATOM   5908  C CA  . LYS B  1 208 ? -27.503  -9.793  -66.610  1.00 32.26  ? 208 LYS B CA  1 
ATOM   5909  C C   . LYS B  1 208 ? -28.137  -10.694 -65.566  1.00 32.43  ? 208 LYS B C   1 
ATOM   5910  O O   . LYS B  1 208 ? -29.061  -10.270 -64.881  1.00 35.23  ? 208 LYS B O   1 
ATOM   5911  C CB  . LYS B  1 208 ? -28.233  -10.099 -67.919  1.00 35.40  ? 208 LYS B CB  1 
ATOM   5912  C CG  . LYS B  1 208 ? -29.750  -9.876  -67.868  1.00 37.05  ? 208 LYS B CG  1 
ATOM   5913  C CD  . LYS B  1 208 ? -30.360  -9.558  -69.215  1.00 37.86  ? 208 LYS B CD  1 
ATOM   5914  C CE  . LYS B  1 208 ? -30.523  -10.789 -69.993  1.00 42.11  ? 208 LYS B CE  1 
ATOM   5915  N NZ  . LYS B  1 208 ? -31.830  -11.330 -69.623  1.00 49.13  ? 208 LYS B NZ  1 
ATOM   5916  N N   . GLY B  1 209 ? -27.693  -11.959 -65.499  1.00 31.70  ? 209 GLY B N   1 
ATOM   5917  C CA  . GLY B  1 209 ? -28.245  -12.900 -64.533  1.00 30.55  ? 209 GLY B CA  1 
ATOM   5918  C C   . GLY B  1 209 ? -28.020  -12.415 -63.101  1.00 29.98  ? 209 GLY B C   1 
ATOM   5919  O O   . GLY B  1 209 ? -28.919  -12.529 -62.270  1.00 32.96  ? 209 GLY B O   1 
ATOM   5920  N N   . LEU B  1 210 ? -26.818  -11.899 -62.803  1.00 28.43  ? 210 LEU B N   1 
ATOM   5921  C CA  . LEU B  1 210 ? -26.510  -11.352 -61.479  1.00 29.59  ? 210 LEU B CA  1 
ATOM   5922  C C   . LEU B  1 210 ? -27.372  -10.126 -61.147  1.00 29.01  ? 210 LEU B C   1 
ATOM   5923  O O   . LEU B  1 210 ? -27.871  -9.981  -60.030  1.00 29.84  ? 210 LEU B O   1 
ATOM   5924  C CB  . LEU B  1 210 ? -25.016  -11.014 -61.371  1.00 31.05  ? 210 LEU B CB  1 
ATOM   5925  C CG  . LEU B  1 210 ? -24.013  -12.172 -61.513  1.00 29.40  ? 210 LEU B CG  1 
ATOM   5926  C CD1 . LEU B  1 210 ? -22.642  -11.638 -61.266  1.00 28.68  ? 210 LEU B CD1 1 
ATOM   5927  C CD2 . LEU B  1 210 ? -24.316  -13.345 -60.608  1.00 28.94  ? 210 LEU B CD2 1 
ATOM   5928  N N   . ASN B  1 211 ? -27.576  -9.239  -62.121  1.00 29.06  ? 211 ASN B N   1 
ATOM   5929  C CA  . ASN B  1 211 ? -28.520  -8.141  -61.974  1.00 29.25  ? 211 ASN B CA  1 
ATOM   5930  C C   . ASN B  1 211 ? -29.947  -8.633  -61.666  1.00 31.68  ? 211 ASN B C   1 
ATOM   5931  O O   . ASN B  1 211 ? -30.646  -8.078  -60.812  1.00 33.55  ? 211 ASN B O   1 
ATOM   5932  C CB  . ASN B  1 211 ? -28.443  -7.272  -63.221  1.00 30.17  ? 211 ASN B CB  1 
ATOM   5933  C CG  . ASN B  1 211 ? -28.798  -5.833  -62.955  1.00 30.46  ? 211 ASN B CG  1 
ATOM   5934  O OD1 . ASN B  1 211 ? -28.524  -5.313  -61.875  1.00 29.39  ? 211 ASN B OD1 1 
ATOM   5935  N ND2 . ASN B  1 211 ? -29.434  -5.196  -63.917  1.00 31.38  ? 211 ASN B ND2 1 
ATOM   5936  N N   . GLU B  1 212 ? -30.417  -9.700  -62.317  1.00 32.83  ? 212 GLU B N   1 
ATOM   5937  C CA  . GLU B  1 212 ? -31.747  -10.228 -62.021  1.00 34.19  ? 212 GLU B CA  1 
ATOM   5938  C C   . GLU B  1 212 ? -31.802  -10.746 -60.589  1.00 33.79  ? 212 GLU B C   1 
ATOM   5939  O O   . GLU B  1 212 ? -32.716  -10.412 -59.843  1.00 37.10  ? 212 GLU B O   1 
ATOM   5940  C CB  . GLU B  1 212 ? -32.233  -11.274 -63.032  1.00 35.33  ? 212 GLU B CB  1 
ATOM   5941  C CG  . GLU B  1 212 ? -32.556  -10.639 -64.389  1.00 36.52  ? 212 GLU B CG  1 
ATOM   5942  C CD  . GLU B  1 212 ? -32.513  -11.543 -65.602  1.00 38.80  ? 212 GLU B CD  1 
ATOM   5943  O OE1 . GLU B  1 212 ? -32.266  -12.734 -65.409  1.00 44.27  ? 212 GLU B OE1 1 
ATOM   5944  O OE2 . GLU B  1 212 ? -32.719  -11.081 -66.733  1.00 40.68  ? 212 GLU B OE2 1 
ATOM   5945  N N   . LEU B  1 213 ? -30.801  -11.512 -60.168  1.00 33.05  ? 213 LEU B N   1 
ATOM   5946  C CA  . LEU B  1 213 ? -30.809  -12.065 -58.814  1.00 33.08  ? 213 LEU B CA  1 
ATOM   5947  C C   . LEU B  1 213 ? -30.686  -10.921 -57.791  1.00 33.03  ? 213 LEU B C   1 
ATOM   5948  O O   . LEU B  1 213 ? -31.240  -10.997 -56.702  1.00 31.38  ? 213 LEU B O   1 
ATOM   5949  C CB  . LEU B  1 213 ? -29.672  -13.095 -58.677  1.00 32.74  ? 213 LEU B CB  1 
ATOM   5950  C CG  . LEU B  1 213 ? -29.789  -14.436 -59.434  1.00 31.75  ? 213 LEU B CG  1 
ATOM   5951  C CD1 . LEU B  1 213 ? -28.417  -15.162 -59.544  1.00 30.18  ? 213 LEU B CD1 1 
ATOM   5952  C CD2 . LEU B  1 213 ? -30.806  -15.391 -58.783  1.00 30.27  ? 213 LEU B CD2 1 
ATOM   5953  N N   . ASN B  1 214 ? -29.909  -9.870  -58.127  1.00 31.46  ? 214 ASN B N   1 
ATOM   5954  C CA  . ASN B  1 214 ? -29.764  -8.683  -57.290  1.00 30.43  ? 214 ASN B CA  1 
ATOM   5955  C C   . ASN B  1 214 ? -31.106  -7.980  -57.061  1.00 32.84  ? 214 ASN B C   1 
ATOM   5956  O O   . ASN B  1 214 ? -31.245  -7.334  -56.022  1.00 30.70  ? 214 ASN B O   1 
ATOM   5957  C CB  . ASN B  1 214 ? -28.677  -7.755  -57.822  1.00 28.87  ? 214 ASN B CB  1 
ATOM   5958  C CG  . ASN B  1 214 ? -27.292  -8.275  -57.496  1.00 29.06  ? 214 ASN B CG  1 
ATOM   5959  O OD1 . ASN B  1 214 ? -27.111  -9.045  -56.543  1.00 30.83  ? 214 ASN B OD1 1 
ATOM   5960  N ND2 . ASN B  1 214 ? -26.288  -7.841  -58.228  1.00 27.79  ? 214 ASN B ND2 1 
ATOM   5961  N N   . GLY B  1 215 ? -32.070  -8.112  -58.012  1.00 34.38  ? 215 GLY B N   1 
ATOM   5962  C CA  . GLY B  1 215 ? -33.461  -7.707  -57.819  1.00 33.40  ? 215 GLY B CA  1 
ATOM   5963  C C   . GLY B  1 215 ? -33.917  -6.511  -58.671  1.00 35.40  ? 215 GLY B C   1 
ATOM   5964  O O   . GLY B  1 215 ? -35.020  -6.000  -58.463  1.00 35.11  ? 215 GLY B O   1 
ATOM   5965  N N   . LEU B  1 216 ? -33.068  -6.026  -59.596  1.00 35.38  ? 216 LEU B N   1 
ATOM   5966  C CA  . LEU B  1 216 ? -33.429  -5.004  -60.578  1.00 34.46  ? 216 LEU B CA  1 
ATOM   5967  C C   . LEU B  1 216 ? -34.031  -3.765  -59.912  1.00 32.58  ? 216 LEU B C   1 
ATOM   5968  O O   . LEU B  1 216 ? -34.842  -3.102  -60.516  1.00 30.89  ? 216 LEU B O   1 
ATOM   5969  C CB  . LEU B  1 216 ? -34.377  -5.574  -61.631  1.00 35.56  ? 216 LEU B CB  1 
ATOM   5970  C CG  . LEU B  1 216 ? -33.761  -6.572  -62.619  1.00 37.68  ? 216 LEU B CG  1 
ATOM   5971  C CD1 . LEU B  1 216 ? -34.816  -7.040  -63.623  1.00 37.25  ? 216 LEU B CD1 1 
ATOM   5972  C CD2 . LEU B  1 216 ? -32.566  -5.937  -63.321  1.00 37.11  ? 216 LEU B CD2 1 
ATOM   5973  N N   . ASP B  1 217 ? -33.563  -3.418  -58.717  1.00 32.30  ? 217 ASP B N   1 
ATOM   5974  C CA  . ASP B  1 217 ? -34.167  -2.382  -57.894  1.00 33.77  ? 217 ASP B CA  1 
ATOM   5975  C C   . ASP B  1 217 ? -33.177  -1.239  -57.626  1.00 33.04  ? 217 ASP B C   1 
ATOM   5976  O O   . ASP B  1 217 ? -33.485  -0.359  -56.846  1.00 35.80  ? 217 ASP B O   1 
ATOM   5977  C CB  . ASP B  1 217 ? -34.698  -2.975  -56.593  1.00 34.65  ? 217 ASP B CB  1 
ATOM   5978  C CG  . ASP B  1 217 ? -33.704  -3.836  -55.810  1.00 35.52  ? 217 ASP B CG  1 
ATOM   5979  O OD1 . ASP B  1 217 ? -32.676  -4.278  -56.395  1.00 32.78  ? 217 ASP B OD1 1 
ATOM   5980  O OD2 . ASP B  1 217 ? -33.932  -4.031  -54.610  1.00 35.82  ? 217 ASP B OD2 1 
ATOM   5981  N N   . LYS B  1 218 ? -32.002  -1.229  -58.259  1.00 32.79  ? 218 LYS B N   1 
ATOM   5982  C CA  . LYS B  1 218 ? -31.023  -0.154  -58.110  1.00 33.16  ? 218 LYS B CA  1 
ATOM   5983  C C   . LYS B  1 218 ? -30.229  -0.021  -59.408  1.00 30.91  ? 218 LYS B C   1 
ATOM   5984  O O   . LYS B  1 218 ? -30.165  -0.965  -60.188  1.00 27.49  ? 218 LYS B O   1 
ATOM   5985  C CB  . LYS B  1 218 ? -29.947  -0.430  -57.047  1.00 36.42  ? 218 LYS B CB  1 
ATOM   5986  C CG  . LYS B  1 218 ? -30.500  -0.928  -55.727  1.00 39.61  ? 218 LYS B CG  1 
ATOM   5987  C CD  . LYS B  1 218 ? -29.527  -1.191  -54.585  1.00 40.47  ? 218 LYS B CD  1 
ATOM   5988  C CE  . LYS B  1 218 ? -30.289  -1.123  -53.274  1.00 42.20  ? 218 LYS B CE  1 
ATOM   5989  N NZ  . LYS B  1 218 ? -29.470  -1.655  -52.189  1.00 42.94  ? 218 LYS B NZ  1 
ATOM   5990  N N   . PRO B  1 219 ? -29.593  1.144   -59.676  1.00 31.02  ? 219 PRO B N   1 
ATOM   5991  C CA  . PRO B  1 219 ? -28.703  1.281   -60.832  1.00 30.26  ? 219 PRO B CA  1 
ATOM   5992  C C   . PRO B  1 219 ? -27.634  0.195   -60.755  1.00 29.73  ? 219 PRO B C   1 
ATOM   5993  O O   . PRO B  1 219 ? -27.250  -0.228  -59.679  1.00 29.09  ? 219 PRO B O   1 
ATOM   5994  C CB  . PRO B  1 219 ? -28.125  2.664   -60.670  1.00 30.51  ? 219 PRO B CB  1 
ATOM   5995  C CG  . PRO B  1 219 ? -29.159  3.416   -59.829  1.00 31.49  ? 219 PRO B CG  1 
ATOM   5996  C CD  . PRO B  1 219 ? -29.695  2.372   -58.877  1.00 31.83  ? 219 PRO B CD  1 
ATOM   5997  N N   . PHE B  1 220 ? -27.176  -0.282  -61.909  1.00 31.43  ? 220 PHE B N   1 
ATOM   5998  C CA  . PHE B  1 220 ? -26.046  -1.209  -61.989  1.00 28.70  ? 220 PHE B CA  1 
ATOM   5999  C C   . PHE B  1 220 ? -24.951  -0.530  -62.791  1.00 28.10  ? 220 PHE B C   1 
ATOM   6000  O O   . PHE B  1 220 ? -25.252  0.017   -63.848  1.00 27.76  ? 220 PHE B O   1 
ATOM   6001  C CB  . PHE B  1 220 ? -26.507  -2.515  -62.653  1.00 27.89  ? 220 PHE B CB  1 
ATOM   6002  C CG  . PHE B  1 220 ? -25.367  -3.393  -63.123  1.00 26.21  ? 220 PHE B CG  1 
ATOM   6003  C CD1 . PHE B  1 220 ? -24.358  -3.767  -62.262  1.00 26.09  ? 220 PHE B CD1 1 
ATOM   6004  C CD2 . PHE B  1 220 ? -25.280  -3.797  -64.443  1.00 26.36  ? 220 PHE B CD2 1 
ATOM   6005  C CE1 . PHE B  1 220 ? -23.300  -4.535  -62.718  1.00 26.18  ? 220 PHE B CE1 1 
ATOM   6006  C CE2 . PHE B  1 220 ? -24.210  -4.563  -64.887  1.00 25.57  ? 220 PHE B CE2 1 
ATOM   6007  C CZ  . PHE B  1 220 ? -23.230  -4.935  -64.027  1.00 25.01  ? 220 PHE B CZ  1 
ATOM   6008  N N   . ILE B  1 221 ? -23.715  -0.536  -62.275  1.00 27.96  ? 221 ILE B N   1 
ATOM   6009  C CA  . ILE B  1 221 ? -22.571  -0.053  -63.045  1.00 27.16  ? 221 ILE B CA  1 
ATOM   6010  C C   . ILE B  1 221 ? -21.487  -1.131  -63.082  1.00 27.48  ? 221 ILE B C   1 
ATOM   6011  O O   . ILE B  1 221 ? -21.457  -2.009  -62.199  1.00 27.77  ? 221 ILE B O   1 
ATOM   6012  C CB  . ILE B  1 221 ? -21.978  1.231   -62.465  1.00 25.93  ? 221 ILE B CB  1 
ATOM   6013  C CG1 . ILE B  1 221 ? -21.295  0.959   -61.144  1.00 25.96  ? 221 ILE B CG1 1 
ATOM   6014  C CG2 . ILE B  1 221 ? -23.040  2.327   -62.349  1.00 27.79  ? 221 ILE B CG2 1 
ATOM   6015  C CD1 . ILE B  1 221 ? -20.799  2.214   -60.438  1.00 28.22  ? 221 ILE B CD1 1 
ATOM   6016  N N   . THR B  1 222 ? -20.575  -0.975  -64.062  1.00 25.98  ? 222 THR B N   1 
ATOM   6017  C CA  . THR B  1 222 ? -19.332  -1.730  -64.129  1.00 27.76  ? 222 THR B CA  1 
ATOM   6018  C C   . THR B  1 222 ? -18.180  -0.816  -63.704  1.00 28.30  ? 222 THR B C   1 
ATOM   6019  O O   . THR B  1 222 ? -18.133  0.309   -64.141  1.00 28.62  ? 222 THR B O   1 
ATOM   6020  C CB  . THR B  1 222 ? -19.115  -2.330  -65.525  1.00 26.66  ? 222 THR B CB  1 
ATOM   6021  O OG1 . THR B  1 222 ? -18.698  -1.318  -66.441  1.00 26.63  ? 222 THR B OG1 1 
ATOM   6022  C CG2 . THR B  1 222 ? -20.377  -2.991  -66.049  1.00 27.06  ? 222 THR B CG2 1 
ATOM   6023  N N   . THR B  1 223 ? -17.264  -1.348  -62.882  1.00 29.37  ? 223 THR B N   1 
ATOM   6024  C CA  . THR B  1 223 ? -16.154  -0.629  -62.294  1.00 29.39  ? 223 THR B CA  1 
ATOM   6025  C C   . THR B  1 223 ? -14.819  -1.093  -62.890  1.00 30.49  ? 223 THR B C   1 
ATOM   6026  O O   . THR B  1 223 ? -13.786  -0.549  -62.510  1.00 30.11  ? 223 THR B O   1 
ATOM   6027  C CB  . THR B  1 223 ? -16.199  -0.791  -60.775  1.00 29.48  ? 223 THR B CB  1 
ATOM   6028  O OG1 . THR B  1 223 ? -16.311  -2.172  -60.505  1.00 25.56  ? 223 THR B OG1 1 
ATOM   6029  C CG2 . THR B  1 223 ? -17.377  -0.058  -60.148  1.00 31.23  ? 223 THR B CG2 1 
ATOM   6030  N N   . ALA B  1 224 ? -14.866  -2.029  -63.856  1.00 28.93  ? 224 ALA B N   1 
ATOM   6031  C CA  . ALA B  1 224 ? -13.719  -2.480  -64.629  1.00 28.35  ? 224 ALA B CA  1 
ATOM   6032  C C   . ALA B  1 224 ? -14.152  -3.518  -65.671  1.00 28.23  ? 224 ALA B C   1 
ATOM   6033  O O   . ALA B  1 224 ? -15.073  -4.307  -65.435  1.00 30.21  ? 224 ALA B O   1 
ATOM   6034  C CB  . ALA B  1 224 ? -12.672  -3.071  -63.734  1.00 29.86  ? 224 ALA B CB  1 
ATOM   6035  N N   . PHE B  1 225 ? -13.468  -3.496  -66.820  1.00 26.26  ? 225 PHE B N   1 
ATOM   6036  C CA  . PHE B  1 225 ? -13.580  -4.466  -67.898  1.00 24.95  ? 225 PHE B CA  1 
ATOM   6037  C C   . PHE B  1 225 ? -12.484  -4.147  -68.910  1.00 26.26  ? 225 PHE B C   1 
ATOM   6038  O O   . PHE B  1 225 ? -12.048  -3.001  -69.020  1.00 27.60  ? 225 PHE B O   1 
ATOM   6039  C CB  . PHE B  1 225 ? -14.963  -4.460  -68.538  1.00 25.11  ? 225 PHE B CB  1 
ATOM   6040  C CG  . PHE B  1 225 ? -15.447  -3.193  -69.230  1.00 25.40  ? 225 PHE B CG  1 
ATOM   6041  C CD1 . PHE B  1 225 ? -15.188  -2.971  -70.580  1.00 25.32  ? 225 PHE B CD1 1 
ATOM   6042  C CD2 . PHE B  1 225 ? -16.227  -2.260  -68.547  1.00 26.30  ? 225 PHE B CD2 1 
ATOM   6043  C CE1 . PHE B  1 225 ? -15.655  -1.834  -71.212  1.00 25.20  ? 225 PHE B CE1 1 
ATOM   6044  C CE2 . PHE B  1 225 ? -16.660  -1.108  -69.181  1.00 25.51  ? 225 PHE B CE2 1 
ATOM   6045  C CZ  . PHE B  1 225 ? -16.377  -0.908  -70.511  1.00 24.76  ? 225 PHE B CZ  1 
ATOM   6046  N N   . GLY B  1 226 ? -12.014  -5.148  -69.652  1.00 26.81  ? 226 GLY B N   1 
ATOM   6047  C CA  . GLY B  1 226 ? -10.991  -4.888  -70.658  1.00 26.54  ? 226 GLY B CA  1 
ATOM   6048  C C   . GLY B  1 226 ? -9.975   -6.015  -70.761  1.00 27.86  ? 226 GLY B C   1 
ATOM   6049  O O   . GLY B  1 226 ? -10.213  -7.088  -70.202  1.00 29.81  ? 226 GLY B O   1 
ATOM   6050  N N   . TYR B  1 227 ? -8.877   -5.721  -71.486  1.00 26.48  ? 227 TYR B N   1 
ATOM   6051  C CA  . TYR B  1 227 ? -7.917   -6.679  -71.992  1.00 25.03  ? 227 TYR B CA  1 
ATOM   6052  C C   . TYR B  1 227 ? -6.501   -6.120  -71.907  1.00 26.24  ? 227 TYR B C   1 
ATOM   6053  O O   . TYR B  1 227 ? -6.263   -4.910  -72.099  1.00 26.26  ? 227 TYR B O   1 
ATOM   6054  C CB  . TYR B  1 227 ? -8.292   -7.060  -73.430  1.00 24.68  ? 227 TYR B CB  1 
ATOM   6055  C CG  . TYR B  1 227 ? -9.614   -7.806  -73.460  1.00 25.88  ? 227 TYR B CG  1 
ATOM   6056  C CD1 . TYR B  1 227 ? -9.698   -9.134  -73.067  1.00 26.38  ? 227 TYR B CD1 1 
ATOM   6057  C CD2 . TYR B  1 227 ? -10.790  -7.194  -73.851  1.00 27.23  ? 227 TYR B CD2 1 
ATOM   6058  C CE1 . TYR B  1 227 ? -10.908  -9.810  -73.056  1.00 27.08  ? 227 TYR B CE1 1 
ATOM   6059  C CE2 . TYR B  1 227 ? -12.013  -7.860  -73.835  1.00 26.38  ? 227 TYR B CE2 1 
ATOM   6060  C CZ  . TYR B  1 227 ? -12.072  -9.174  -73.424  1.00 26.68  ? 227 TYR B CZ  1 
ATOM   6061  O OH  . TYR B  1 227 ? -13.249  -9.871  -73.385  1.00 29.76  ? 227 TYR B OH  1 
ATOM   6062  N N   . SER B  1 228 ? -5.574   -7.065  -71.688  1.00 26.32  ? 228 SER B N   1 
ATOM   6063  C CA  . SER B  1 228 ? -4.146   -6.841  -71.523  1.00 25.97  ? 228 SER B CA  1 
ATOM   6064  C C   . SER B  1 228 ? -3.428   -7.170  -72.817  1.00 26.39  ? 228 SER B C   1 
ATOM   6065  O O   . SER B  1 228 ? -3.694   -8.223  -73.402  1.00 25.79  ? 228 SER B O   1 
ATOM   6066  C CB  . SER B  1 228 ? -3.575   -7.710  -70.446  1.00 26.67  ? 228 SER B CB  1 
ATOM   6067  O OG  . SER B  1 228 ? -2.148   -7.662  -70.446  1.00 28.64  ? 228 SER B OG  1 
ATOM   6068  N N   . VAL B  1 229 ? -2.474   -6.306  -73.209  1.00 25.30  ? 229 VAL B N   1 
ATOM   6069  C CA  . VAL B  1 229 ? -1.738   -6.539  -74.435  1.00 25.18  ? 229 VAL B CA  1 
ATOM   6070  C C   . VAL B  1 229 ? -0.299   -6.953  -74.122  1.00 25.99  ? 229 VAL B C   1 
ATOM   6071  O O   . VAL B  1 229 ? 0.599    -6.720  -74.913  1.00 25.45  ? 229 VAL B O   1 
ATOM   6072  C CB  . VAL B  1 229 ? -1.797   -5.371  -75.423  1.00 25.13  ? 229 VAL B CB  1 
ATOM   6073  C CG1 . VAL B  1 229 ? -3.245   -5.066  -75.795  1.00 23.89  ? 229 VAL B CG1 1 
ATOM   6074  C CG2 . VAL B  1 229 ? -1.028   -4.120  -74.925  1.00 26.06  ? 229 VAL B CG2 1 
ATOM   6075  N N   . SER B  1 230 ? -0.119   -7.700  -73.037  1.00 27.87  ? 230 SER B N   1 
ATOM   6076  C CA  . SER B  1 230 ? 1.189    -8.182  -72.646  1.00 31.29  ? 230 SER B CA  1 
ATOM   6077  C C   . SER B  1 230 ? 1.819    -8.985  -73.792  1.00 33.17  ? 230 SER B C   1 
ATOM   6078  O O   . SER B  1 230 ? 1.108    -9.653  -74.539  1.00 34.03  ? 230 SER B O   1 
ATOM   6079  C CB  . SER B  1 230 ? 1.060    -8.997  -71.355  1.00 32.62  ? 230 SER B CB  1 
ATOM   6080  O OG  . SER B  1 230 ? 0.431    -10.251 -71.588  1.00 34.57  ? 230 SER B OG  1 
ATOM   6081  N N   . PRO B  1 231 ? 3.151    -8.903  -74.009  1.00 32.76  ? 231 PRO B N   1 
ATOM   6082  C CA  . PRO B  1 231 ? 3.840    -9.743  -74.987  1.00 33.35  ? 231 PRO B CA  1 
ATOM   6083  C C   . PRO B  1 231 ? 3.568    -11.234 -74.844  1.00 33.86  ? 231 PRO B C   1 
ATOM   6084  O O   . PRO B  1 231 ? 3.520    -11.962 -75.833  1.00 31.56  ? 231 PRO B O   1 
ATOM   6085  C CB  . PRO B  1 231 ? 5.347    -9.436  -74.772  1.00 33.51  ? 231 PRO B CB  1 
ATOM   6086  C CG  . PRO B  1 231 ? 5.374    -8.036  -74.180  1.00 33.80  ? 231 PRO B CG  1 
ATOM   6087  C CD  . PRO B  1 231 ? 4.043    -7.886  -73.421  1.00 34.33  ? 231 PRO B CD  1 
ATOM   6088  N N   . GLU B  1 232 ? 3.450    -11.667 -73.587  1.00 36.55  ? 232 GLU B N   1 
ATOM   6089  C CA  . GLU B  1 232 ? 3.144    -13.052 -73.248  1.00 36.86  ? 232 GLU B CA  1 
ATOM   6090  C C   . GLU B  1 232 ? 2.636    -13.115 -71.796  1.00 36.86  ? 232 GLU B C   1 
ATOM   6091  O O   . GLU B  1 232 ? 2.376    -12.070 -71.151  1.00 35.67  ? 232 GLU B O   1 
ATOM   6092  C CB  . GLU B  1 232 ? 4.370    -13.925 -73.536  1.00 38.87  ? 232 GLU B CB  1 
ATOM   6093  C CG  . GLU B  1 232 ? 5.511    -13.579 -72.603  1.00 42.05  ? 232 GLU B CG  1 
ATOM   6094  C CD  . GLU B  1 232 ? 6.910    -13.990 -72.982  1.00 46.11  ? 232 GLU B CD  1 
ATOM   6095  O OE1 . GLU B  1 232 ? 7.583    -13.300 -73.785  1.00 53.74  ? 232 GLU B OE1 1 
ATOM   6096  O OE2 . GLU B  1 232 ? 7.308    -15.004 -72.391  1.00 47.17  ? 232 GLU B OE2 1 
ATOM   6097  N N   . GLY B  1 233 ? 2.428    -14.364 -71.333  1.00 35.36  ? 233 GLY B N   1 
ATOM   6098  C CA  . GLY B  1 233 ? 1.946    -14.654 -69.998  1.00 33.29  ? 233 GLY B CA  1 
ATOM   6099  C C   . GLY B  1 233 ? 0.420    -14.663 -69.922  1.00 31.60  ? 233 GLY B C   1 
ATOM   6100  O O   . GLY B  1 233 ? -0.277   -14.339 -70.883  1.00 32.28  ? 233 GLY B O   1 
ATOM   6101  N N   . GLY B  1 234 ? -0.070   -15.042 -68.747  1.00 32.45  ? 234 GLY B N   1 
ATOM   6102  C CA  . GLY B  1 234 ? -1.514   -15.180 -68.523  1.00 32.47  ? 234 GLY B CA  1 
ATOM   6103  C C   . GLY B  1 234 ? -2.037   -16.506 -69.025  1.00 31.87  ? 234 GLY B C   1 
ATOM   6104  O O   . GLY B  1 234 ? -1.235   -17.424 -69.209  1.00 30.48  ? 234 GLY B O   1 
ATOM   6105  N N   . ASN B  1 235 ? -3.345   -16.602 -69.208  1.00 34.37  ? 235 ASN B N   1 
ATOM   6106  C CA  . ASN B  1 235 ? -3.964   -17.822 -69.783  1.00 37.01  ? 235 ASN B CA  1 
ATOM   6107  C C   . ASN B  1 235 ? -5.101   -17.366 -70.696  1.00 34.72  ? 235 ASN B C   1 
ATOM   6108  O O   . ASN B  1 235 ? -5.914   -16.544 -70.263  1.00 34.33  ? 235 ASN B O   1 
ATOM   6109  C CB  . ASN B  1 235 ? -4.409   -18.831 -68.728  1.00 40.89  ? 235 ASN B CB  1 
ATOM   6110  C CG  . ASN B  1 235 ? -5.427   -18.271 -67.765  1.00 48.78  ? 235 ASN B CG  1 
ATOM   6111  O OD1 . ASN B  1 235 ? -5.203   -17.214 -67.166  1.00 55.88  ? 235 ASN B OD1 1 
ATOM   6112  N ND2 . ASN B  1 235 ? -6.546   -18.960 -67.603  1.00 53.67  ? 235 ASN B ND2 1 
ATOM   6113  N N   . GLY B  1 236 ? -5.120   -17.865 -71.921  1.00 32.27  ? 236 GLY B N   1 
ATOM   6114  C CA  . GLY B  1 236 ? -6.193   -17.538 -72.864  1.00 31.06  ? 236 GLY B CA  1 
ATOM   6115  C C   . GLY B  1 236 ? -6.318   -16.060 -73.124  1.00 32.73  ? 236 GLY B C   1 
ATOM   6116  O O   . GLY B  1 236 ? -5.298   -15.420 -73.409  1.00 30.91  ? 236 GLY B O   1 
ATOM   6117  N N   . GLN B  1 237 ? -7.542   -15.553 -73.036  1.00 29.54  ? 237 GLN B N   1 
ATOM   6118  C CA  . GLN B  1 237 ? -7.773   -14.151 -73.279  1.00 30.39  ? 237 GLN B CA  1 
ATOM   6119  C C   . GLN B  1 237 ? -7.278   -13.273 -72.126  1.00 29.54  ? 237 GLN B C   1 
ATOM   6120  O O   . GLN B  1 237 ? -7.333   -12.065 -72.263  1.00 28.18  ? 237 GLN B O   1 
ATOM   6121  C CB  . GLN B  1 237 ? -9.263   -13.894 -73.506  1.00 29.25  ? 237 GLN B CB  1 
ATOM   6122  C CG  . GLN B  1 237 ? -9.807   -14.438 -74.820  1.00 28.68  ? 237 GLN B CG  1 
ATOM   6123  C CD  . GLN B  1 237 ? -11.240  -14.002 -75.048  1.00 29.72  ? 237 GLN B CD  1 
ATOM   6124  O OE1 . GLN B  1 237 ? -11.568  -12.817 -75.201  1.00 32.57  ? 237 GLN B OE1 1 
ATOM   6125  N NE2 . GLN B  1 237 ? -12.134  -14.959 -75.028  1.00 29.79  ? 237 GLN B NE2 1 
ATOM   6126  N N   . TYR B  1 238 ? -6.825   -13.854 -70.995  1.00 29.94  ? 238 TYR B N   1 
ATOM   6127  C CA  . TYR B  1 238 ? -6.203   -13.088 -69.923  1.00 28.65  ? 238 TYR B CA  1 
ATOM   6128  C C   . TYR B  1 238 ? -4.713   -12.951 -70.187  1.00 28.44  ? 238 TYR B C   1 
ATOM   6129  O O   . TYR B  1 238 ? -3.966   -13.918 -70.048  1.00 31.56  ? 238 TYR B O   1 
ATOM   6130  C CB  . TYR B  1 238 ? -6.390   -13.662 -68.521  1.00 29.52  ? 238 TYR B CB  1 
ATOM   6131  C CG  . TYR B  1 238 ? -5.661   -12.906 -67.413  1.00 31.07  ? 238 TYR B CG  1 
ATOM   6132  C CD1 . TYR B  1 238 ? -6.130   -11.695 -66.951  1.00 30.01  ? 238 TYR B CD1 1 
ATOM   6133  C CD2 . TYR B  1 238 ? -4.510   -13.412 -66.816  1.00 33.16  ? 238 TYR B CD2 1 
ATOM   6134  C CE1 . TYR B  1 238 ? -5.487   -11.017 -65.935  1.00 30.80  ? 238 TYR B CE1 1 
ATOM   6135  C CE2 . TYR B  1 238 ? -3.843   -12.732 -65.812  1.00 31.31  ? 238 TYR B CE2 1 
ATOM   6136  C CZ  . TYR B  1 238 ? -4.348   -11.542 -65.359  1.00 31.89  ? 238 TYR B CZ  1 
ATOM   6137  O OH  . TYR B  1 238 ? -3.730   -10.875 -64.345  1.00 35.97  ? 238 TYR B OH  1 
ATOM   6138  N N   . GLY B  1 239 ? -4.300   -11.737 -70.546  1.00 26.69  ? 239 GLY B N   1 
ATOM   6139  C CA  . GLY B  1 239 ? -2.972   -11.469 -71.050  1.00 27.66  ? 239 GLY B CA  1 
ATOM   6140  C C   . GLY B  1 239 ? -2.888   -11.750 -72.545  1.00 28.32  ? 239 GLY B C   1 
ATOM   6141  O O   . GLY B  1 239 ? -3.828   -12.290 -73.121  1.00 25.77  ? 239 GLY B O   1 
ATOM   6142  N N   . SER B  1 240 ? -1.772   -11.298 -73.156  1.00 29.54  ? 240 SER B N   1 
ATOM   6143  C CA  . SER B  1 240 ? -1.285   -11.796 -74.440  1.00 30.77  ? 240 SER B CA  1 
ATOM   6144  C C   . SER B  1 240 ? -2.183   -11.413 -75.622  1.00 30.89  ? 240 SER B C   1 
ATOM   6145  O O   . SER B  1 240 ? -2.011   -11.972 -76.699  1.00 30.25  ? 240 SER B O   1 
ATOM   6146  C CB  . SER B  1 240 ? -1.021   -13.302 -74.422  1.00 30.63  ? 240 SER B CB  1 
ATOM   6147  O OG  . SER B  1 240 ? 0.003    -13.653 -73.499  1.00 30.04  ? 240 SER B OG  1 
ATOM   6148  N N   . ASN B  1 241 ? -3.018   -10.367 -75.492  1.00 31.27  ? 241 ASN B N   1 
ATOM   6149  C CA  . ASN B  1 241 ? -3.859   -9.919  -76.601  1.00 30.57  ? 241 ASN B CA  1 
ATOM   6150  C C   . ASN B  1 241 ? -3.050   -9.052  -77.572  1.00 28.12  ? 241 ASN B C   1 
ATOM   6151  O O   . ASN B  1 241 ? -2.058   -8.456  -77.191  1.00 26.93  ? 241 ASN B O   1 
ATOM   6152  C CB  . ASN B  1 241 ? -5.123   -9.172  -76.142  1.00 32.81  ? 241 ASN B CB  1 
ATOM   6153  C CG  . ASN B  1 241 ? -6.076   -10.054 -75.368  1.00 31.98  ? 241 ASN B CG  1 
ATOM   6154  O OD1 . ASN B  1 241 ? -6.966   -10.662 -75.953  1.00 33.55  ? 241 ASN B OD1 1 
ATOM   6155  N ND2 . ASN B  1 241 ? -5.885   -10.181 -74.063  1.00 33.05  ? 241 ASN B ND2 1 
ATOM   6156  N N   . THR B  1 242 ? -3.442   -9.049  -78.852  1.00 26.84  ? 242 THR B N   1 
ATOM   6157  C CA  . THR B  1 242 ? -2.972   -8.062  -79.798  1.00 27.62  ? 242 THR B CA  1 
ATOM   6158  C C   . THR B  1 242 ? -3.674   -6.740  -79.471  1.00 28.52  ? 242 THR B C   1 
ATOM   6159  O O   . THR B  1 242 ? -4.680   -6.719  -78.732  1.00 26.29  ? 242 THR B O   1 
ATOM   6160  C CB  . THR B  1 242 ? -3.284   -8.548  -81.211  1.00 28.45  ? 242 THR B CB  1 
ATOM   6161  O OG1 . THR B  1 242 ? -4.696   -8.626  -81.418  1.00 29.67  ? 242 THR B OG1 1 
ATOM   6162  C CG2 . THR B  1 242 ? -2.723   -9.925  -81.479  1.00 28.35  ? 242 THR B CG2 1 
ATOM   6163  N N   . LEU B  1 243 ? -3.152   -5.649  -80.040  1.00 28.62  ? 243 LEU B N   1 
ATOM   6164  C CA  . LEU B  1 243 ? -3.787   -4.339  -79.905  1.00 28.53  ? 243 LEU B CA  1 
ATOM   6165  C C   . LEU B  1 243 ? -5.181   -4.373  -80.534  1.00 28.59  ? 243 LEU B C   1 
ATOM   6166  O O   . LEU B  1 243 ? -6.130   -3.772  -80.016  1.00 28.13  ? 243 LEU B O   1 
ATOM   6167  C CB  . LEU B  1 243 ? -2.923   -3.250  -80.548  1.00 28.57  ? 243 LEU B CB  1 
ATOM   6168  C CG  . LEU B  1 243 ? -1.514   -3.041  -79.968  1.00 28.96  ? 243 LEU B CG  1 
ATOM   6169  C CD1 . LEU B  1 243 ? -0.687   -2.111  -80.857  1.00 28.59  ? 243 LEU B CD1 1 
ATOM   6170  C CD2 . LEU B  1 243 ? -1.563   -2.461  -78.562  1.00 28.82  ? 243 LEU B CD2 1 
ATOM   6171  N N   . LYS B  1 244 ? -5.314   -5.078  -81.665  1.00 30.78  ? 244 LYS B N   1 
ATOM   6172  C CA  . LYS B  1 244 ? -6.607   -5.151  -82.332  1.00 32.58  ? 244 LYS B CA  1 
ATOM   6173  C C   . LYS B  1 244 ? -7.608   -5.914  -81.463  1.00 31.82  ? 244 LYS B C   1 
ATOM   6174  O O   . LYS B  1 244 ? -8.785   -5.527  -81.373  1.00 33.98  ? 244 LYS B O   1 
ATOM   6175  C CB  . LYS B  1 244 ? -6.484   -5.764  -83.727  1.00 36.46  ? 244 LYS B CB  1 
ATOM   6176  C CG  . LYS B  1 244 ? -7.750   -5.700  -84.608  1.00 37.53  ? 244 LYS B CG  1 
ATOM   6177  C CD  . LYS B  1 244 ? -7.760   -6.915  -85.552  1.00 40.35  ? 244 LYS B CD  1 
ATOM   6178  C CE  . LYS B  1 244 ? -8.858   -7.065  -86.580  1.00 39.18  ? 244 LYS B CE  1 
ATOM   6179  N NZ  . LYS B  1 244 ? -10.118  -6.468  -86.109  1.00 40.07  ? 244 LYS B NZ  1 
ATOM   6180  N N   . GLN B  1 245 ? -7.136   -6.993  -80.817  1.00 29.77  ? 245 GLN B N   1 
ATOM   6181  C CA  . GLN B  1 245 ? -7.981   -7.778  -79.934  1.00 28.22  ? 245 GLN B CA  1 
ATOM   6182  C C   . GLN B  1 245 ? -8.369   -6.945  -78.721  1.00 28.45  ? 245 GLN B C   1 
ATOM   6183  O O   . GLN B  1 245 ? -9.503   -7.049  -78.257  1.00 28.76  ? 245 GLN B O   1 
ATOM   6184  C CB  . GLN B  1 245 ? -7.301   -9.046  -79.422  1.00 28.76  ? 245 GLN B CB  1 
ATOM   6185  C CG  . GLN B  1 245 ? -7.250   -10.193 -80.435  1.00 28.87  ? 245 GLN B CG  1 
ATOM   6186  C CD  . GLN B  1 245 ? -6.216   -11.245 -80.095  1.00 28.09  ? 245 GLN B CD  1 
ATOM   6187  O OE1 . GLN B  1 245 ? -5.292   -11.056 -79.317  1.00 28.37  ? 245 GLN B OE1 1 
ATOM   6188  N NE2 . GLN B  1 245 ? -6.350   -12.397 -80.691  1.00 30.13  ? 245 GLN B NE2 1 
ATOM   6189  N N   . GLN B  1 246 ? -7.425   -6.152  -78.192  1.00 26.96  ? 246 GLN B N   1 
ATOM   6190  C CA  . GLN B  1 246 ? -7.749   -5.286  -77.078  1.00 27.73  ? 246 GLN B CA  1 
ATOM   6191  C C   . GLN B  1 246 ? -8.884   -4.358  -77.498  1.00 28.98  ? 246 GLN B C   1 
ATOM   6192  O O   . GLN B  1 246 ? -9.920   -4.263  -76.839  1.00 31.42  ? 246 GLN B O   1 
ATOM   6193  C CB  . GLN B  1 246 ? -6.510   -4.522  -76.620  1.00 27.56  ? 246 GLN B CB  1 
ATOM   6194  C CG  . GLN B  1 246 ? -6.777   -3.619  -75.424  1.00 26.56  ? 246 GLN B CG  1 
ATOM   6195  C CD  . GLN B  1 246 ? -5.633   -2.677  -75.120  1.00 25.94  ? 246 GLN B CD  1 
ATOM   6196  O OE1 . GLN B  1 246 ? -5.006   -2.086  -76.002  1.00 26.80  ? 246 GLN B OE1 1 
ATOM   6197  N NE2 . GLN B  1 246 ? -5.346   -2.525  -73.847  1.00 25.99  ? 246 GLN B NE2 1 
ATOM   6198  N N   . SER B  1 247 ? -8.712   -3.731  -78.656  1.00 30.59  ? 247 SER B N   1 
ATOM   6199  C CA  . SER B  1 247 ? -9.666   -2.733  -79.134  1.00 31.22  ? 247 SER B CA  1 
ATOM   6200  C C   . SER B  1 247 ? -11.009  -3.381  -79.470  1.00 29.33  ? 247 SER B C   1 
ATOM   6201  O O   . SER B  1 247 ? -12.028  -2.895  -79.021  1.00 25.44  ? 247 SER B O   1 
ATOM   6202  C CB  . SER B  1 247 ? -9.116   -1.955  -80.321  1.00 31.35  ? 247 SER B CB  1 
ATOM   6203  O OG  . SER B  1 247 ? -10.068  -0.984  -80.731  1.00 33.67  ? 247 SER B OG  1 
ATOM   6204  N N   . ASP B  1 248 ? -11.017  -4.485  -80.237  1.00 29.47  ? 248 ASP B N   1 
ATOM   6205  C CA  . ASP B  1 248 ? -12.272  -5.178  -80.543  1.00 29.01  ? 248 ASP B CA  1 
ATOM   6206  C C   . ASP B  1 248 ? -12.976  -5.647  -79.270  1.00 27.84  ? 248 ASP B C   1 
ATOM   6207  O O   . ASP B  1 248 ? -14.189  -5.450  -79.130  1.00 26.90  ? 248 ASP B O   1 
ATOM   6208  C CB  . ASP B  1 248 ? -12.087  -6.342  -81.502  1.00 29.10  ? 248 ASP B CB  1 
ATOM   6209  C CG  . ASP B  1 248 ? -11.720  -5.886  -82.900  1.00 28.40  ? 248 ASP B CG  1 
ATOM   6210  O OD1 . ASP B  1 248 ? -11.853  -4.671  -83.206  1.00 29.45  ? 248 ASP B OD1 1 
ATOM   6211  O OD2 . ASP B  1 248 ? -11.245  -6.722  -83.624  1.00 28.00  ? 248 ASP B OD2 1 
ATOM   6212  N N   . GLY B  1 249 ? -12.182  -6.130  -78.315  1.00 26.19  ? 249 GLY B N   1 
ATOM   6213  C CA  . GLY B  1 249 ? -12.699  -6.610  -77.054  1.00 26.89  ? 249 GLY B CA  1 
ATOM   6214  C C   . GLY B  1 249 ? -13.391  -5.533  -76.221  1.00 27.74  ? 249 GLY B C   1 
ATOM   6215  O O   . GLY B  1 249 ? -14.473  -5.780  -75.695  1.00 29.23  ? 249 GLY B O   1 
ATOM   6216  N N   . LEU B  1 250 ? -12.761  -4.363  -76.041  1.00 27.58  ? 250 LEU B N   1 
ATOM   6217  C CA  . LEU B  1 250 ? -13.397  -3.295  -75.285  1.00 26.70  ? 250 LEU B CA  1 
ATOM   6218  C C   . LEU B  1 250 ? -14.778  -2.974  -75.862  1.00 26.85  ? 250 LEU B C   1 
ATOM   6219  O O   . LEU B  1 250 ? -15.764  -2.824  -75.134  1.00 28.67  ? 250 LEU B O   1 
ATOM   6220  C CB  . LEU B  1 250 ? -12.495  -2.064  -75.215  1.00 28.05  ? 250 LEU B CB  1 
ATOM   6221  C CG  . LEU B  1 250 ? -11.601  -1.965  -73.984  1.00 27.74  ? 250 LEU B CG  1 
ATOM   6222  C CD1 . LEU B  1 250 ? -12.435  -1.919  -72.735  1.00 29.45  ? 250 LEU B CD1 1 
ATOM   6223  C CD2 . LEU B  1 250 ? -10.691  -3.134  -73.933  1.00 28.70  ? 250 LEU B CD2 1 
ATOM   6224  N N   . ILE B  1 251 ? -14.884  -2.943  -77.185  1.00 27.70  ? 251 ILE B N   1 
ATOM   6225  C CA  . ILE B  1 251 ? -16.123  -2.545  -77.846  1.00 27.64  ? 251 ILE B CA  1 
ATOM   6226  C C   . ILE B  1 251 ? -17.173  -3.640  -77.717  1.00 27.40  ? 251 ILE B C   1 
ATOM   6227  O O   . ILE B  1 251 ? -18.363  -3.366  -77.620  1.00 27.30  ? 251 ILE B O   1 
ATOM   6228  C CB  . ILE B  1 251 ? -15.813  -2.205  -79.316  1.00 30.41  ? 251 ILE B CB  1 
ATOM   6229  C CG1 . ILE B  1 251 ? -14.733  -1.107  -79.416  1.00 33.60  ? 251 ILE B CG1 1 
ATOM   6230  C CG2 . ILE B  1 251 ? -17.063  -1.831  -80.098  1.00 30.80  ? 251 ILE B CG2 1 
ATOM   6231  C CD1 . ILE B  1 251 ? -14.989  0.124   -78.561  1.00 33.98  ? 251 ILE B CD1 1 
ATOM   6232  N N   . SER B  1 252 ? -16.726  -4.899  -77.742  1.00 28.51  ? 252 SER B N   1 
ATOM   6233  C CA  . SER B  1 252 ? -17.627  -6.024  -77.555  1.00 29.20  ? 252 SER B CA  1 
ATOM   6234  C C   . SER B  1 252 ? -18.137  -6.032  -76.113  1.00 28.20  ? 252 SER B C   1 
ATOM   6235  O O   . SER B  1 252 ? -19.323  -6.242  -75.879  1.00 24.33  ? 252 SER B O   1 
ATOM   6236  C CB  . SER B  1 252 ? -16.967  -7.323  -77.938  1.00 30.38  ? 252 SER B CB  1 
ATOM   6237  O OG  . SER B  1 252 ? -17.631  -8.384  -77.270  1.00 34.27  ? 252 SER B OG  1 
ATOM   6238  N N   . ASN B  1 253 ? -17.230  -5.745  -75.158  1.00 27.65  ? 253 ASN B N   1 
ATOM   6239  C CA  . ASN B  1 253 ? -17.595  -5.693  -73.751  1.00 26.44  ? 253 ASN B CA  1 
ATOM   6240  C C   . ASN B  1 253 ? -18.586  -4.560  -73.485  1.00 25.32  ? 253 ASN B C   1 
ATOM   6241  O O   . ASN B  1 253 ? -19.480  -4.749  -72.683  1.00 26.05  ? 253 ASN B O   1 
ATOM   6242  C CB  . ASN B  1 253 ? -16.426  -5.452  -72.807  1.00 27.09  ? 253 ASN B CB  1 
ATOM   6243  C CG  . ASN B  1 253 ? -15.431  -6.583  -72.743  1.00 29.42  ? 253 ASN B CG  1 
ATOM   6244  O OD1 . ASN B  1 253 ? -15.603  -7.671  -73.319  1.00 31.69  ? 253 ASN B OD1 1 
ATOM   6245  N ND2 . ASN B  1 253 ? -14.379  -6.342  -71.988  1.00 28.50  ? 253 ASN B ND2 1 
ATOM   6246  N N   . TYR B  1 254 ? -18.400  -3.373  -74.085  1.00 25.23  ? 254 TYR B N   1 
ATOM   6247  C CA  . TYR B  1 254 ? -19.231  -2.214  -73.753  1.00 24.91  ? 254 TYR B CA  1 
ATOM   6248  C C   . TYR B  1 254 ? -20.697  -2.464  -74.137  1.00 25.43  ? 254 TYR B C   1 
ATOM   6249  O O   . TYR B  1 254 ? -21.622  -2.083  -73.416  1.00 25.20  ? 254 TYR B O   1 
ATOM   6250  C CB  . TYR B  1 254 ? -18.745  -0.958  -74.492  1.00 25.01  ? 254 TYR B CB  1 
ATOM   6251  C CG  . TYR B  1 254 ? -18.878  0.345   -73.719  1.00 26.46  ? 254 TYR B CG  1 
ATOM   6252  C CD1 . TYR B  1 254 ? -20.126  0.909   -73.460  1.00 28.43  ? 254 TYR B CD1 1 
ATOM   6253  C CD2 . TYR B  1 254 ? -17.764  1.055   -73.300  1.00 27.75  ? 254 TYR B CD2 1 
ATOM   6254  C CE1 . TYR B  1 254 ? -20.259  2.141   -72.820  1.00 29.39  ? 254 TYR B CE1 1 
ATOM   6255  C CE2 . TYR B  1 254 ? -17.886  2.290   -72.667  1.00 29.49  ? 254 TYR B CE2 1 
ATOM   6256  C CZ  . TYR B  1 254 ? -19.141  2.837   -72.411  1.00 28.32  ? 254 TYR B CZ  1 
ATOM   6257  O OH  . TYR B  1 254 ? -19.310  4.014   -71.727  1.00 25.69  ? 254 TYR B OH  1 
ATOM   6258  N N   . ARG B  1 255 ? -20.884  -3.069  -75.314  1.00 25.91  ? 255 ARG B N   1 
ATOM   6259  C CA  . ARG B  1 255 ? -22.183  -3.452  -75.839  1.00 27.38  ? 255 ARG B CA  1 
ATOM   6260  C C   . ARG B  1 255 ? -22.838  -4.478  -74.915  1.00 27.96  ? 255 ARG B C   1 
ATOM   6261  O O   . ARG B  1 255 ? -23.973  -4.300  -74.459  1.00 25.75  ? 255 ARG B O   1 
ATOM   6262  C CB  . ARG B  1 255 ? -21.959  -3.961  -77.272  1.00 28.93  ? 255 ARG B CB  1 
ATOM   6263  C CG  . ARG B  1 255 ? -23.097  -4.686  -77.981  1.00 31.64  ? 255 ARG B CG  1 
ATOM   6264  C CD  . ARG B  1 255 ? -24.240  -3.760  -78.378  1.00 32.67  ? 255 ARG B CD  1 
ATOM   6265  N NE  . ARG B  1 255 ? -25.144  -3.427  -77.274  1.00 32.64  ? 255 ARG B NE  1 
ATOM   6266  C CZ  . ARG B  1 255 ? -25.649  -2.243  -76.974  1.00 33.74  ? 255 ARG B CZ  1 
ATOM   6267  N NH1 . ARG B  1 255 ? -25.231  -1.126  -77.560  1.00 33.36  ? 255 ARG B NH1 1 
ATOM   6268  N NH2 . ARG B  1 255 ? -26.581  -2.188  -76.051  1.00 33.01  ? 255 ARG B NH2 1 
ATOM   6269  N N   . ASP B  1 256 ? -22.114  -5.571  -74.672  1.00 27.80  ? 256 ASP B N   1 
ATOM   6270  C CA  . ASP B  1 256 ? -22.604  -6.663  -73.844  1.00 26.77  ? 256 ASP B CA  1 
ATOM   6271  C C   . ASP B  1 256 ? -23.023  -6.152  -72.458  1.00 27.32  ? 256 ASP B C   1 
ATOM   6272  O O   . ASP B  1 256 ? -24.047  -6.560  -71.915  1.00 26.65  ? 256 ASP B O   1 
ATOM   6273  C CB  . ASP B  1 256 ? -21.504  -7.699  -73.679  1.00 26.06  ? 256 ASP B CB  1 
ATOM   6274  C CG  . ASP B  1 256 ? -21.191  -8.567  -74.883  1.00 26.62  ? 256 ASP B CG  1 
ATOM   6275  O OD1 . ASP B  1 256 ? -21.900  -8.425  -75.912  1.00 26.94  ? 256 ASP B OD1 1 
ATOM   6276  O OD2 . ASP B  1 256 ? -20.258  -9.415  -74.764  1.00 29.01  ? 256 ASP B OD2 1 
ATOM   6277  N N   . LEU B  1 257 ? -22.204  -5.278  -71.854  1.00 27.25  ? 257 LEU B N   1 
ATOM   6278  C CA  . LEU B  1 257 ? -22.439  -4.858  -70.490  1.00 26.83  ? 257 LEU B CA  1 
ATOM   6279  C C   . LEU B  1 257 ? -23.650  -3.933  -70.381  1.00 28.18  ? 257 LEU B C   1 
ATOM   6280  O O   . LEU B  1 257 ? -24.405  -4.027  -69.414  1.00 29.79  ? 257 LEU B O   1 
ATOM   6281  C CB  . LEU B  1 257 ? -21.141  -4.259  -69.973  1.00 26.98  ? 257 LEU B CB  1 
ATOM   6282  C CG  . LEU B  1 257 ? -20.085  -5.305  -69.598  1.00 29.24  ? 257 LEU B CG  1 
ATOM   6283  C CD1 . LEU B  1 257 ? -18.706  -4.689  -69.322  1.00 28.99  ? 257 LEU B CD1 1 
ATOM   6284  C CD2 . LEU B  1 257 ? -20.546  -6.199  -68.428  1.00 28.74  ? 257 LEU B CD2 1 
ATOM   6285  N N   . ILE B  1 258 ? -23.880  -3.068  -71.374  1.00 26.42  ? 258 ILE B N   1 
ATOM   6286  C CA  . ILE B  1 258 ? -25.112  -2.290  -71.413  1.00 26.28  ? 258 ILE B CA  1 
ATOM   6287  C C   . ILE B  1 258 ? -26.315  -3.223  -71.596  1.00 26.89  ? 258 ILE B C   1 
ATOM   6288  O O   . ILE B  1 258 ? -27.384  -3.006  -71.031  1.00 26.11  ? 258 ILE B O   1 
ATOM   6289  C CB  . ILE B  1 258 ? -25.033  -1.278  -72.552  1.00 26.16  ? 258 ILE B CB  1 
ATOM   6290  C CG1 . ILE B  1 258 ? -24.036  -0.187  -72.216  1.00 27.39  ? 258 ILE B CG1 1 
ATOM   6291  C CG2 . ILE B  1 258 ? -26.403  -0.712  -72.894  1.00 27.85  ? 258 ILE B CG2 1 
ATOM   6292  C CD1 . ILE B  1 258 ? -23.697  0.674   -73.405  1.00 27.99  ? 258 ILE B CD1 1 
ATOM   6293  N N   . ASP B  1 259 ? -26.144  -4.231  -72.451  1.00 25.39  ? 259 ASP B N   1 
ATOM   6294  C CA  . ASP B  1 259 ? -27.166  -5.230  -72.687  1.00 26.45  ? 259 ASP B CA  1 
ATOM   6295  C C   . ASP B  1 259 ? -27.499  -5.989  -71.409  1.00 25.86  ? 259 ASP B C   1 
ATOM   6296  O O   . ASP B  1 259 ? -28.576  -6.537  -71.335  1.00 25.36  ? 259 ASP B O   1 
ATOM   6297  C CB  . ASP B  1 259 ? -26.750  -6.207  -73.770  1.00 26.72  ? 259 ASP B CB  1 
ATOM   6298  C CG  . ASP B  1 259 ? -26.637  -5.583  -75.150  1.00 26.04  ? 259 ASP B CG  1 
ATOM   6299  O OD1 . ASP B  1 259 ? -27.485  -4.718  -75.443  1.00 25.22  ? 259 ASP B OD1 1 
ATOM   6300  O OD2 . ASP B  1 259 ? -25.776  -6.044  -75.946  1.00 25.84  ? 259 ASP B OD2 1 
ATOM   6301  N N   . ALA B  1 260 ? -26.603  -5.979  -70.410  1.00 26.25  ? 260 ALA B N   1 
ATOM   6302  C CA  . ALA B  1 260 ? -26.875  -6.557  -69.099  1.00 26.62  ? 260 ALA B CA  1 
ATOM   6303  C C   . ALA B  1 260 ? -27.592  -5.594  -68.146  1.00 28.65  ? 260 ALA B C   1 
ATOM   6304  O O   . ALA B  1 260 ? -27.848  -5.944  -67.000  1.00 31.18  ? 260 ALA B O   1 
ATOM   6305  C CB  . ALA B  1 260 ? -25.583  -7.015  -68.486  1.00 25.87  ? 260 ALA B CB  1 
ATOM   6306  N N   . GLY B  1 261 ? -27.892  -4.363  -68.577  1.00 31.54  ? 261 GLY B N   1 
ATOM   6307  C CA  . GLY B  1 261 ? -28.595  -3.398  -67.742  1.00 29.73  ? 261 GLY B CA  1 
ATOM   6308  C C   . GLY B  1 261 ? -27.708  -2.296  -67.154  1.00 27.90  ? 261 GLY B C   1 
ATOM   6309  O O   . GLY B  1 261 ? -28.215  -1.475  -66.401  1.00 32.62  ? 261 GLY B O   1 
ATOM   6310  N N   . ALA B  1 262 ? -26.420  -2.226  -67.495  1.00 27.22  ? 262 ALA B N   1 
ATOM   6311  C CA  . ALA B  1 262 ? -25.533  -1.212  -66.909  1.00 26.12  ? 262 ALA B CA  1 
ATOM   6312  C C   . ALA B  1 262 ? -25.868  0.194   -67.405  1.00 26.30  ? 262 ALA B C   1 
ATOM   6313  O O   . ALA B  1 262 ? -26.165  0.386   -68.579  1.00 25.32  ? 262 ALA B O   1 
ATOM   6314  C CB  . ALA B  1 262 ? -24.093  -1.526  -67.206  1.00 25.99  ? 262 ALA B CB  1 
ATOM   6315  N N   . VAL B  1 263 ? -25.811  1.178   -66.492  1.00 28.28  ? 263 VAL B N   1 
ATOM   6316  C CA  . VAL B  1 263 ? -26.050  2.593   -66.806  1.00 28.81  ? 263 VAL B CA  1 
ATOM   6317  C C   . VAL B  1 263 ? -24.863  3.457   -66.395  1.00 28.80  ? 263 VAL B C   1 
ATOM   6318  O O   . VAL B  1 263 ? -24.961  4.703   -66.312  1.00 29.11  ? 263 VAL B O   1 
ATOM   6319  C CB  . VAL B  1 263 ? -27.319  3.081   -66.103  1.00 29.80  ? 263 VAL B CB  1 
ATOM   6320  C CG1 . VAL B  1 263 ? -28.552  2.410   -66.704  1.00 31.30  ? 263 VAL B CG1 1 
ATOM   6321  C CG2 . VAL B  1 263 ? -27.217  2.856   -64.604  1.00 30.48  ? 263 VAL B CG2 1 
ATOM   6322  N N   . GLY B  1 264 ? -23.742  2.761   -66.161  1.00 26.45  ? 264 GLY B N   1 
ATOM   6323  C CA  . GLY B  1 264 ? -22.466  3.363   -65.829  1.00 26.04  ? 264 GLY B CA  1 
ATOM   6324  C C   . GLY B  1 264 ? -21.358  2.364   -66.143  1.00 27.17  ? 264 GLY B C   1 
ATOM   6325  O O   . GLY B  1 264 ? -21.499  1.157   -65.895  1.00 23.95  ? 264 GLY B O   1 
ATOM   6326  N N   . MET B  1 265 ? -20.283  2.875   -66.751  1.00 27.51  ? 265 MET B N   1 
ATOM   6327  C CA  . MET B  1 265 ? -19.263  2.018   -67.320  1.00 27.52  ? 265 MET B CA  1 
ATOM   6328  C C   . MET B  1 265 ? -17.892  2.581   -66.978  1.00 27.73  ? 265 MET B C   1 
ATOM   6329  O O   . MET B  1 265 ? -17.595  3.748   -67.264  1.00 26.50  ? 265 MET B O   1 
ATOM   6330  C CB  . MET B  1 265 ? -19.439  1.898   -68.836  1.00 28.75  ? 265 MET B CB  1 
ATOM   6331  C CG  . MET B  1 265 ? -20.799  1.323   -69.249  1.00 29.72  ? 265 MET B CG  1 
ATOM   6332  S SD  . MET B  1 265 ? -20.801  -0.446  -68.971  1.00 30.10  ? 265 MET B SD  1 
ATOM   6333  C CE  . MET B  1 265 ? -19.928  -1.084  -70.401  1.00 30.99  ? 265 MET B CE  1 
ATOM   6334  N N   . CYS B  1 266 ? -17.058  1.698   -66.400  1.00 26.30  ? 266 CYS B N   1 
ATOM   6335  C CA  . CYS B  1 266 ? -15.695  2.036   -66.041  1.00 26.49  ? 266 CYS B CA  1 
ATOM   6336  C C   . CYS B  1 266 ? -14.730  1.117   -66.777  1.00 26.99  ? 266 CYS B C   1 
ATOM   6337  O O   . CYS B  1 266 ? -14.042  0.317   -66.159  1.00 25.19  ? 266 CYS B O   1 
ATOM   6338  C CB  . CYS B  1 266 ? -15.460  1.982   -64.532  1.00 26.29  ? 266 CYS B CB  1 
ATOM   6339  S SG  . CYS B  1 266 ? -16.523  3.110   -63.579  1.00 25.70  ? 266 CYS B SG  1 
ATOM   6340  N N   . PRO B  1 267 ? -14.557  1.250   -68.111  1.00 27.98  ? 267 PRO B N   1 
ATOM   6341  C CA  . PRO B  1 267 ? -13.498  0.505   -68.796  1.00 27.63  ? 267 PRO B CA  1 
ATOM   6342  C C   . PRO B  1 267 ? -12.140  0.620   -68.095  1.00 29.19  ? 267 PRO B C   1 
ATOM   6343  O O   . PRO B  1 267 ? -11.794  1.657   -67.511  1.00 30.35  ? 267 PRO B O   1 
ATOM   6344  C CB  . PRO B  1 267 ? -13.514  1.142   -70.203  1.00 26.57  ? 267 PRO B CB  1 
ATOM   6345  C CG  . PRO B  1 267 ? -14.168  2.485   -69.988  1.00 26.48  ? 267 PRO B CG  1 
ATOM   6346  C CD  . PRO B  1 267 ? -15.290  2.143   -69.012  1.00 26.53  ? 267 PRO B CD  1 
ATOM   6347  N N   . PHE B  1 268 ? -11.395  -0.486  -68.139  1.00 28.43  ? 268 PHE B N   1 
ATOM   6348  C CA  . PHE B  1 268 ? -10.105  -0.588  -67.493  1.00 29.51  ? 268 PHE B CA  1 
ATOM   6349  C C   . PHE B  1 268 ? -9.014   -0.686  -68.547  1.00 28.21  ? 268 PHE B C   1 
ATOM   6350  O O   . PHE B  1 268 ? -8.986   -1.686  -69.275  1.00 28.14  ? 268 PHE B O   1 
ATOM   6351  C CB  . PHE B  1 268 ? -10.103  -1.847  -66.618  1.00 29.90  ? 268 PHE B CB  1 
ATOM   6352  C CG  . PHE B  1 268 ? -8.880   -1.903  -65.712  1.00 30.95  ? 268 PHE B CG  1 
ATOM   6353  C CD1 . PHE B  1 268 ? -7.697   -2.484  -66.157  1.00 33.38  ? 268 PHE B CD1 1 
ATOM   6354  C CD2 . PHE B  1 268 ? -8.878   -1.295  -64.462  1.00 29.89  ? 268 PHE B CD2 1 
ATOM   6355  C CE1 . PHE B  1 268 ? -6.571   -2.514  -65.339  1.00 32.70  ? 268 PHE B CE1 1 
ATOM   6356  C CE2 . PHE B  1 268 ? -7.742   -1.304  -63.666  1.00 32.62  ? 268 PHE B CE2 1 
ATOM   6357  C CZ  . PHE B  1 268 ? -6.592   -1.924  -64.102  1.00 31.98  ? 268 PHE B CZ  1 
ATOM   6358  N N   . TYR B  1 269 ? -8.130   0.318   -68.661  1.00 27.01  ? 269 TYR B N   1 
ATOM   6359  C CA  . TYR B  1 269 ? -8.121   1.600   -67.957  1.00 28.17  ? 269 TYR B CA  1 
ATOM   6360  C C   . TYR B  1 269 ? -7.130   2.547   -68.663  1.00 27.21  ? 269 TYR B C   1 
ATOM   6361  O O   . TYR B  1 269 ? -6.520   2.190   -69.653  1.00 26.99  ? 269 TYR B O   1 
ATOM   6362  C CB  . TYR B  1 269 ? -7.749   1.538   -66.468  1.00 28.93  ? 269 TYR B CB  1 
ATOM   6363  C CG  . TYR B  1 269 ? -6.333   1.153   -66.045  1.00 28.43  ? 269 TYR B CG  1 
ATOM   6364  C CD1 . TYR B  1 269 ? -5.475   0.431   -66.861  1.00 28.59  ? 269 TYR B CD1 1 
ATOM   6365  C CD2 . TYR B  1 269 ? -5.878   1.443   -64.759  1.00 31.47  ? 269 TYR B CD2 1 
ATOM   6366  C CE1 . TYR B  1 269 ? -4.197   0.068   -66.450  1.00 28.21  ? 269 TYR B CE1 1 
ATOM   6367  C CE2 . TYR B  1 269 ? -4.609   1.077   -64.325  1.00 31.19  ? 269 TYR B CE2 1 
ATOM   6368  C CZ  . TYR B  1 269 ? -3.772   0.371   -65.173  1.00 28.95  ? 269 TYR B CZ  1 
ATOM   6369  O OH  . TYR B  1 269 ? -2.550   -0.035  -64.739  1.00 29.70  ? 269 TYR B OH  1 
ATOM   6370  N N   . TYR B  1 270 ? -6.917   3.749   -68.123  1.00 28.30  ? 270 TYR B N   1 
ATOM   6371  C CA  . TYR B  1 270 ? -6.171   4.813   -68.783  1.00 26.74  ? 270 TYR B CA  1 
ATOM   6372  C C   . TYR B  1 270 ? -4.785   4.405   -69.301  1.00 26.42  ? 270 TYR B C   1 
ATOM   6373  O O   . TYR B  1 270 ? -4.515   4.492   -70.498  1.00 24.61  ? 270 TYR B O   1 
ATOM   6374  C CB  . TYR B  1 270 ? -6.045   5.942   -67.765  1.00 26.73  ? 270 TYR B CB  1 
ATOM   6375  C CG  . TYR B  1 270 ? -5.188   7.088   -68.289  1.00 26.93  ? 270 TYR B CG  1 
ATOM   6376  C CD1 . TYR B  1 270 ? -5.431   7.664   -69.529  1.00 28.14  ? 270 TYR B CD1 1 
ATOM   6377  C CD2 . TYR B  1 270 ? -4.127   7.581   -67.555  1.00 26.37  ? 270 TYR B CD2 1 
ATOM   6378  C CE1 . TYR B  1 270 ? -4.644   8.708   -70.009  1.00 28.92  ? 270 TYR B CE1 1 
ATOM   6379  C CE2 . TYR B  1 270 ? -3.330   8.607   -68.033  1.00 27.74  ? 270 TYR B CE2 1 
ATOM   6380  C CZ  . TYR B  1 270 ? -3.578   9.180   -69.267  1.00 27.68  ? 270 TYR B CZ  1 
ATOM   6381  O OH  . TYR B  1 270 ? -2.773   10.192  -69.743  1.00 26.91  ? 270 TYR B OH  1 
ATOM   6382  N N   . ALA B  1 271 ? -3.882   4.005   -68.400  1.00 27.90  ? 271 ALA B N   1 
ATOM   6383  C CA  . ALA B  1 271 ? -2.474   3.819   -68.734  1.00 28.33  ? 271 ALA B CA  1 
ATOM   6384  C C   . ALA B  1 271 ? -1.854   2.640   -67.987  1.00 27.67  ? 271 ALA B C   1 
ATOM   6385  O O   . ALA B  1 271 ? -2.173   2.395   -66.833  1.00 27.87  ? 271 ALA B O   1 
ATOM   6386  C CB  . ALA B  1 271 ? -1.715   5.089   -68.402  1.00 29.00  ? 271 ALA B CB  1 
ATOM   6387  N N   . ASP B  1 272 ? -0.889   1.982   -68.636  1.00 29.19  ? 272 ASP B N   1 
ATOM   6388  C CA  . ASP B  1 272 ? -0.088   0.928   -68.023  1.00 30.43  ? 272 ASP B CA  1 
ATOM   6389  C C   . ASP B  1 272 ? 0.516    1.344   -66.683  1.00 30.35  ? 272 ASP B C   1 
ATOM   6390  O O   . ASP B  1 272 ? 0.992    2.480   -66.516  1.00 31.84  ? 272 ASP B O   1 
ATOM   6391  C CB  . ASP B  1 272 ? 1.080    0.540   -68.908  1.00 30.46  ? 272 ASP B CB  1 
ATOM   6392  C CG  . ASP B  1 272 ? 0.740    -0.364  -70.080  1.00 31.69  ? 272 ASP B CG  1 
ATOM   6393  O OD1 . ASP B  1 272 ? -0.424   -0.899  -70.097  1.00 32.08  ? 272 ASP B OD1 1 
ATOM   6394  O OD2 . ASP B  1 272 ? 1.620    -0.500  -70.980  1.00 29.72  ? 272 ASP B OD2 1 
ATOM   6395  N N   . GLY B  1 273 ? 0.501    0.390   -65.744  1.00 28.84  ? 273 GLY B N   1 
ATOM   6396  C CA  . GLY B  1 273 ? 1.222    0.517   -64.490  1.00 28.95  ? 273 GLY B CA  1 
ATOM   6397  C C   . GLY B  1 273 ? 2.257    -0.593  -64.321  1.00 28.61  ? 273 GLY B C   1 
ATOM   6398  O O   . GLY B  1 273 ? 1.908    -1.691  -63.935  1.00 28.59  ? 273 GLY B O   1 
ATOM   6399  N N   . TRP B  1 274 ? 3.533    -0.267  -64.520  1.00 28.90  ? 274 TRP B N   1 
ATOM   6400  C CA  . TRP B  1 274 ? 4.600    -1.249  -64.489  1.00 30.09  ? 274 TRP B CA  1 
ATOM   6401  C C   . TRP B  1 274 ? 4.741    -1.888  -63.113  1.00 31.50  ? 274 TRP B C   1 
ATOM   6402  O O   . TRP B  1 274 ? 5.326    -2.964  -63.008  1.00 32.46  ? 274 TRP B O   1 
ATOM   6403  C CB  . TRP B  1 274 ? 5.921    -0.598  -64.907  1.00 30.43  ? 274 TRP B CB  1 
ATOM   6404  C CG  . TRP B  1 274 ? 5.964    -0.177  -66.348  1.00 29.05  ? 274 TRP B CG  1 
ATOM   6405  C CD1 . TRP B  1 274 ? 4.913    -0.046  -67.199  1.00 29.44  ? 274 TRP B CD1 1 
ATOM   6406  C CD2 . TRP B  1 274 ? 7.133    0.199   -67.091  1.00 29.55  ? 274 TRP B CD2 1 
ATOM   6407  N NE1 . TRP B  1 274 ? 5.357    0.361   -68.431  1.00 29.94  ? 274 TRP B NE1 1 
ATOM   6408  C CE2 . TRP B  1 274 ? 6.707    0.534   -68.391  1.00 29.23  ? 274 TRP B CE2 1 
ATOM   6409  C CE3 . TRP B  1 274 ? 8.501    0.265   -66.791  1.00 30.45  ? 274 TRP B CE3 1 
ATOM   6410  C CZ2 . TRP B  1 274 ? 7.593    0.948   -69.385  1.00 30.10  ? 274 TRP B CZ2 1 
ATOM   6411  C CZ3 . TRP B  1 274 ? 9.378    0.682   -67.769  1.00 30.83  ? 274 TRP B CZ3 1 
ATOM   6412  C CH2 . TRP B  1 274 ? 8.929    1.051   -69.039  1.00 30.55  ? 274 TRP B CH2 1 
ATOM   6413  N N   . TRP B  1 275 ? 4.227    -1.220  -62.064  1.00 32.05  ? 275 TRP B N   1 
ATOM   6414  C CA  . TRP B  1 275 ? 4.380    -1.716  -60.702  1.00 32.00  ? 275 TRP B CA  1 
ATOM   6415  C C   . TRP B  1 275 ? 3.538    -2.970  -60.501  1.00 32.49  ? 275 TRP B C   1 
ATOM   6416  O O   . TRP B  1 275 ? 3.816    -3.763  -59.617  1.00 34.99  ? 275 TRP B O   1 
ATOM   6417  C CB  . TRP B  1 275 ? 4.039    -0.656  -59.645  1.00 30.55  ? 275 TRP B CB  1 
ATOM   6418  C CG  . TRP B  1 275 ? 2.567    -0.330  -59.584  1.00 32.19  ? 275 TRP B CG  1 
ATOM   6419  C CD1 . TRP B  1 275 ? 1.912    0.619   -60.318  1.00 31.61  ? 275 TRP B CD1 1 
ATOM   6420  C CD2 . TRP B  1 275 ? 1.561    -0.939  -58.737  1.00 31.27  ? 275 TRP B CD2 1 
ATOM   6421  N NE1 . TRP B  1 275 ? 0.578    0.624   -60.004  1.00 30.80  ? 275 TRP B NE1 1 
ATOM   6422  C CE2 . TRP B  1 275 ? 0.334    -0.303  -59.030  1.00 31.30  ? 275 TRP B CE2 1 
ATOM   6423  C CE3 . TRP B  1 275 ? 1.576    -1.946  -57.762  1.00 32.86  ? 275 TRP B CE3 1 
ATOM   6424  C CZ2 . TRP B  1 275 ? -0.860   -0.643  -58.381  1.00 32.66  ? 275 TRP B CZ2 1 
ATOM   6425  C CZ3 . TRP B  1 275 ? 0.402    -2.292  -57.131  1.00 31.75  ? 275 TRP B CZ3 1 
ATOM   6426  C CH2 . TRP B  1 275 ? -0.795   -1.647  -57.430  1.00 32.73  ? 275 TRP B CH2 1 
ATOM   6427  N N   . LYS B  1 276 ? 2.500    -3.138  -61.305  1.00 33.65  ? 276 LYS B N   1 
ATOM   6428  C CA  . LYS B  1 276 ? 1.441    -4.087  -60.979  1.00 34.03  ? 276 LYS B CA  1 
ATOM   6429  C C   . LYS B  1 276 ? 1.941    -5.530  -60.893  1.00 34.97  ? 276 LYS B C   1 
ATOM   6430  O O   . LYS B  1 276 ? 1.391    -6.304  -60.125  1.00 37.69  ? 276 LYS B O   1 
ATOM   6431  C CB  . LYS B  1 276 ? 0.267    -3.879  -61.932  1.00 31.51  ? 276 LYS B CB  1 
ATOM   6432  C CG  . LYS B  1 276 ? -0.414   -2.534  -61.643  1.00 32.32  ? 276 LYS B CG  1 
ATOM   6433  C CD  . LYS B  1 276 ? -1.501   -2.173  -62.631  1.00 32.67  ? 276 LYS B CD  1 
ATOM   6434  C CE  . LYS B  1 276 ? -2.615   -3.172  -62.610  1.00 33.02  ? 276 LYS B CE  1 
ATOM   6435  N NZ  . LYS B  1 276 ? -3.488   -3.040  -61.432  1.00 34.21  ? 276 LYS B NZ  1 
ATOM   6436  N N   . GLY B  1 277 ? 2.970    -5.902  -61.642  1.00 35.21  ? 277 GLY B N   1 
ATOM   6437  C CA  . GLY B  1 277 ? 3.475    -7.258  -61.512  1.00 37.59  ? 277 GLY B CA  1 
ATOM   6438  C C   . GLY B  1 277 ? 4.771    -7.339  -60.708  1.00 39.27  ? 277 GLY B C   1 
ATOM   6439  O O   . GLY B  1 277 ? 5.507    -8.313  -60.863  1.00 40.68  ? 277 GLY B O   1 
ATOM   6440  N N   . GLY B  1 278 ? 5.041    -6.330  -59.857  1.00 39.26  ? 278 GLY B N   1 
ATOM   6441  C CA  . GLY B  1 278 ? 6.325    -6.198  -59.173  1.00 41.79  ? 278 GLY B CA  1 
ATOM   6442  C C   . GLY B  1 278 ? 7.392    -5.561  -60.076  1.00 44.57  ? 278 GLY B C   1 
ATOM   6443  O O   . GLY B  1 278 ? 7.278    -5.590  -61.312  1.00 49.71  ? 278 GLY B O   1 
ATOM   6444  N N   . GLU B  1 279 ? 8.426    -4.983  -59.453  1.00 43.88  ? 279 GLU B N   1 
ATOM   6445  C CA  . GLU B  1 279 ? 9.473    -4.218  -60.130  1.00 47.18  ? 279 GLU B CA  1 
ATOM   6446  C C   . GLU B  1 279 ? 8.869    -3.084  -60.957  1.00 45.50  ? 279 GLU B C   1 
ATOM   6447  O O   . GLU B  1 279 ? 8.721    -3.179  -62.171  1.00 47.49  ? 279 GLU B O   1 
ATOM   6448  C CB  . GLU B  1 279 ? 10.400   -5.128  -60.939  1.00 52.10  ? 279 GLU B CB  1 
ATOM   6449  C CG  . GLU B  1 279 ? 11.251   -6.051  -60.064  1.00 58.76  ? 279 GLU B CG  1 
ATOM   6450  C CD  . GLU B  1 279 ? 11.697   -7.333  -60.752  1.00 67.37  ? 279 GLU B CD  1 
ATOM   6451  O OE1 . GLU B  1 279 ? 12.497   -7.301  -61.716  1.00 66.60  ? 279 GLU B OE1 1 
ATOM   6452  O OE2 . GLU B  1 279 ? 11.210   -8.399  -60.323  1.00 76.64  ? 279 GLU B OE2 1 
ATOM   6453  N N   . LYS B  1 280 ? 8.584    -1.968  -60.289  1.00 44.10  ? 280 LYS B N   1 
ATOM   6454  C CA  . LYS B  1 280 ? 8.070    -0.767  -60.935  1.00 41.86  ? 280 LYS B CA  1 
ATOM   6455  C C   . LYS B  1 280 ? 8.968    -0.174  -62.042  1.00 39.51  ? 280 LYS B C   1 
ATOM   6456  O O   . LYS B  1 280 ? 8.492    0.605   -62.862  1.00 37.05  ? 280 LYS B O   1 
ATOM   6457  C CB  . LYS B  1 280 ? 7.877    0.252   -59.808  1.00 43.51  ? 280 LYS B CB  1 
ATOM   6458  C CG  . LYS B  1 280 ? 9.140    0.780   -59.111  1.00 44.17  ? 280 LYS B CG  1 
ATOM   6459  C CD  . LYS B  1 280 ? 8.736    1.716   -57.974  1.00 45.63  ? 280 LYS B CD  1 
ATOM   6460  C CE  . LYS B  1 280 ? 9.787    2.609   -57.401  1.00 47.44  ? 280 LYS B CE  1 
ATOM   6461  N NZ  . LYS B  1 280 ? 10.663   1.806   -56.548  1.00 51.17  ? 280 LYS B NZ  1 
ATOM   6462  N N   . SER B  1 281 ? 10.267   -0.488  -62.069  1.00 38.27  ? 281 SER B N   1 
ATOM   6463  C CA  . SER B  1 281 ? 11.207   0.123   -63.004  1.00 38.60  ? 281 SER B CA  1 
ATOM   6464  C C   . SER B  1 281 ? 11.383   -0.756  -64.244  1.00 38.43  ? 281 SER B C   1 
ATOM   6465  O O   . SER B  1 281 ? 12.150   -0.425  -65.146  1.00 39.74  ? 281 SER B O   1 
ATOM   6466  C CB  . SER B  1 281 ? 12.558   0.418   -62.323  1.00 39.39  ? 281 SER B CB  1 
ATOM   6467  O OG  . SER B  1 281 ? 12.425   1.344   -61.239  1.00 38.98  ? 281 SER B OG  1 
ATOM   6468  N N   . ASP B  1 282 ? 10.622   -1.855  -64.303  1.00 38.76  ? 282 ASP B N   1 
ATOM   6469  C CA  . ASP B  1 282 ? 10.720   -2.823  -65.377  1.00 39.96  ? 282 ASP B CA  1 
ATOM   6470  C C   . ASP B  1 282 ? 9.339    -3.111  -65.956  1.00 37.13  ? 282 ASP B C   1 
ATOM   6471  O O   . ASP B  1 282 ? 8.345    -3.198  -65.229  1.00 34.25  ? 282 ASP B O   1 
ATOM   6472  C CB  . ASP B  1 282 ? 11.337   -4.121  -64.892  1.00 44.21  ? 282 ASP B CB  1 
ATOM   6473  C CG  . ASP B  1 282 ? 11.806   -5.025  -66.019  1.00 49.55  ? 282 ASP B CG  1 
ATOM   6474  O OD1 . ASP B  1 282 ? 12.946   -4.801  -66.498  1.00 55.74  ? 282 ASP B OD1 1 
ATOM   6475  O OD2 . ASP B  1 282 ? 11.023   -5.915  -66.428  1.00 51.08  ? 282 ASP B OD2 1 
ATOM   6476  N N   . HIS B  1 283 ? 9.302    -3.235  -67.287  1.00 36.03  ? 283 HIS B N   1 
ATOM   6477  C CA  . HIS B  1 283 ? 8.075    -3.582  -67.987  1.00 35.04  ? 283 HIS B CA  1 
ATOM   6478  C C   . HIS B  1 283 ? 8.155    -5.059  -68.368  1.00 36.12  ? 283 HIS B C   1 
ATOM   6479  O O   . HIS B  1 283 ? 8.687    -5.415  -69.422  1.00 36.07  ? 283 HIS B O   1 
ATOM   6480  C CB  . HIS B  1 283 ? 7.825    -2.662  -69.190  1.00 32.91  ? 283 HIS B CB  1 
ATOM   6481  C CG  . HIS B  1 283 ? 6.380    -2.556  -69.514  1.00 29.68  ? 283 HIS B CG  1 
ATOM   6482  N ND1 . HIS B  1 283 ? 5.899    -2.107  -70.725  1.00 27.89  ? 283 HIS B ND1 1 
ATOM   6483  C CD2 . HIS B  1 283 ? 5.307    -2.799  -68.738  1.00 28.62  ? 283 HIS B CD2 1 
ATOM   6484  C CE1 . HIS B  1 283 ? 4.569    -2.123  -70.679  1.00 27.64  ? 283 HIS B CE1 1 
ATOM   6485  N NE2 . HIS B  1 283 ? 4.180    -2.566  -69.490  1.00 27.31  ? 283 HIS B NE2 1 
ATOM   6486  N N   . SER B  1 284 ? 7.696    -5.912  -67.454  1.00 36.91  ? 284 SER B N   1 
ATOM   6487  C CA  . SER B  1 284 ? 7.872    -7.340  -67.602  1.00 38.94  ? 284 SER B CA  1 
ATOM   6488  C C   . SER B  1 284 ? 7.095    -7.835  -68.828  1.00 37.56  ? 284 SER B C   1 
ATOM   6489  O O   . SER B  1 284 ? 5.930    -7.504  -69.026  1.00 33.17  ? 284 SER B O   1 
ATOM   6490  C CB  . SER B  1 284 ? 7.441    -8.048  -66.335  1.00 42.60  ? 284 SER B CB  1 
ATOM   6491  O OG  . SER B  1 284 ? 7.059    -9.393  -66.607  1.00 44.22  ? 284 SER B OG  1 
ATOM   6492  N N   . LEU B  1 285 ? 7.759    -8.663  -69.641  1.00 38.40  ? 285 LEU B N   1 
ATOM   6493  C CA  . LEU B  1 285 ? 7.168    -9.208  -70.851  1.00 39.05  ? 285 LEU B CA  1 
ATOM   6494  C C   . LEU B  1 285 ? 6.011    -10.164 -70.548  1.00 37.24  ? 285 LEU B C   1 
ATOM   6495  O O   . LEU B  1 285 ? 5.140    -10.330 -71.408  1.00 33.98  ? 285 LEU B O   1 
ATOM   6496  C CB  . LEU B  1 285 ? 8.253    -9.858  -71.715  1.00 40.86  ? 285 LEU B CB  1 
ATOM   6497  C CG  . LEU B  1 285 ? 9.420    -8.926  -72.099  1.00 43.15  ? 285 LEU B CG  1 
ATOM   6498  C CD1 . LEU B  1 285 ? 10.357   -9.664  -73.066  1.00 41.40  ? 285 LEU B CD1 1 
ATOM   6499  C CD2 . LEU B  1 285 ? 8.981    -7.516  -72.632  1.00 39.10  ? 285 LEU B CD2 1 
ATOM   6500  N N   . ASN B  1 286 ? 5.977    -10.745 -69.335  1.00 37.15  ? 286 ASN B N   1 
ATOM   6501  C CA  . ASN B  1 286 ? 5.019    -11.806 -69.056  1.00 38.51  ? 286 ASN B CA  1 
ATOM   6502  C C   . ASN B  1 286 ? 4.093    -11.462 -67.889  1.00 35.46  ? 286 ASN B C   1 
ATOM   6503  O O   . ASN B  1 286 ? 3.495    -12.365 -67.314  1.00 37.35  ? 286 ASN B O   1 
ATOM   6504  C CB  . ASN B  1 286 ? 5.703    -13.173 -68.886  1.00 39.38  ? 286 ASN B CB  1 
ATOM   6505  C CG  . ASN B  1 286 ? 6.530    -13.303 -67.628  1.00 41.96  ? 286 ASN B CG  1 
ATOM   6506  O OD1 . ASN B  1 286 ? 6.862    -12.312 -66.969  1.00 45.17  ? 286 ASN B OD1 1 
ATOM   6507  N ND2 . ASN B  1 286 ? 6.865    -14.522 -67.254  1.00 43.55  ? 286 ASN B ND2 1 
ATOM   6508  N N   . GLN B  1 287 ? 3.899    -10.182 -67.585  1.00 34.50  ? 287 GLN B N   1 
ATOM   6509  C CA  . GLN B  1 287 ? 2.950    -9.778  -66.558  1.00 34.05  ? 287 GLN B CA  1 
ATOM   6510  C C   . GLN B  1 287 ? 1.766    -9.081  -67.193  1.00 34.43  ? 287 GLN B C   1 
ATOM   6511  O O   . GLN B  1 287 ? 1.773    -7.858  -67.403  1.00 36.29  ? 287 GLN B O   1 
ATOM   6512  C CB  . GLN B  1 287 ? 3.503    -8.867  -65.465  1.00 36.14  ? 287 GLN B CB  1 
ATOM   6513  C CG  . GLN B  1 287 ? 4.600    -9.539  -64.643  1.00 37.78  ? 287 GLN B CG  1 
ATOM   6514  C CD  . GLN B  1 287 ? 4.076    -10.602 -63.691  1.00 37.86  ? 287 GLN B CD  1 
ATOM   6515  O OE1 . GLN B  1 287 ? 2.906    -10.605 -63.265  1.00 37.42  ? 287 GLN B OE1 1 
ATOM   6516  N NE2 . GLN B  1 287 ? 4.971    -11.499 -63.307  1.00 37.19  ? 287 GLN B NE2 1 
ATOM   6517  N N   . PRO B  1 288 ? 0.669    -9.841  -67.405  1.00 33.47  ? 288 PRO B N   1 
ATOM   6518  C CA  . PRO B  1 288 ? -0.568   -9.282  -67.949  1.00 32.70  ? 288 PRO B CA  1 
ATOM   6519  C C   . PRO B  1 288 ? -0.978   -7.957  -67.328  1.00 30.25  ? 288 PRO B C   1 
ATOM   6520  O O   . PRO B  1 288 ? -1.483   -7.082  -68.021  1.00 29.87  ? 288 PRO B O   1 
ATOM   6521  C CB  . PRO B  1 288 ? -1.554   -10.376 -67.599  1.00 32.11  ? 288 PRO B CB  1 
ATOM   6522  C CG  . PRO B  1 288 ? -0.744   -11.634 -67.787  1.00 33.79  ? 288 PRO B CG  1 
ATOM   6523  C CD  . PRO B  1 288 ? 0.559    -11.276 -67.104  1.00 34.41  ? 288 PRO B CD  1 
ATOM   6524  N N   . GLU B  1 289 ? -0.765   -7.869  -66.015  1.00 29.95  ? 289 GLU B N   1 
ATOM   6525  C CA  . GLU B  1 289 ? -1.256   -6.774  -65.194  1.00 31.13  ? 289 GLU B CA  1 
ATOM   6526  C C   . GLU B  1 289 ? -0.616   -5.441  -65.573  1.00 30.17  ? 289 GLU B C   1 
ATOM   6527  O O   . GLU B  1 289 ? -1.241   -4.393  -65.344  1.00 29.52  ? 289 GLU B O   1 
ATOM   6528  C CB  . GLU B  1 289 ? -1.116   -7.142  -63.719  1.00 31.82  ? 289 GLU B CB  1 
ATOM   6529  C CG  . GLU B  1 289 ? -2.142   -8.194  -63.277  1.00 32.10  ? 289 GLU B CG  1 
ATOM   6530  C CD  . GLU B  1 289 ? -3.593   -7.738  -63.348  1.00 33.68  ? 289 GLU B CD  1 
ATOM   6531  O OE1 . GLU B  1 289 ? -3.804   -6.541  -63.049  1.00 32.73  ? 289 GLU B OE1 1 
ATOM   6532  O OE2 . GLU B  1 289 ? -4.501   -8.549  -63.687  1.00 33.90  ? 289 GLU B OE2 1 
ATOM   6533  N N   . GLU B  1 290 ? 0.555    -5.514  -66.218  1.00 29.45  ? 290 GLU B N   1 
ATOM   6534  C CA  . GLU B  1 290 ? 1.350    -4.351  -66.581  1.00 29.50  ? 290 GLU B CA  1 
ATOM   6535  C C   . GLU B  1 290 ? 1.013    -3.801  -67.965  1.00 28.16  ? 290 GLU B C   1 
ATOM   6536  O O   . GLU B  1 290 ? 1.603    -2.795  -68.378  1.00 30.03  ? 290 GLU B O   1 
ATOM   6537  C CB  . GLU B  1 290 ? 2.836    -4.732  -66.526  1.00 31.84  ? 290 GLU B CB  1 
ATOM   6538  C CG  . GLU B  1 290 ? 3.323    -4.999  -65.109  1.00 33.03  ? 290 GLU B CG  1 
ATOM   6539  C CD  . GLU B  1 290 ? 4.792    -5.307  -64.969  1.00 34.90  ? 290 GLU B CD  1 
ATOM   6540  O OE1 . GLU B  1 290 ? 5.612    -4.751  -65.751  1.00 36.23  ? 290 GLU B OE1 1 
ATOM   6541  O OE2 . GLU B  1 290 ? 5.100    -6.031  -64.002  1.00 33.46  ? 290 GLU B OE2 1 
ATOM   6542  N N   . TRP B  1 291 ? 0.051    -4.411  -68.669  1.00 27.01  ? 291 TRP B N   1 
ATOM   6543  C CA  . TRP B  1 291 ? -0.235   -4.052  -70.047  1.00 25.78  ? 291 TRP B CA  1 
ATOM   6544  C C   . TRP B  1 291 ? -1.729   -3.885  -70.272  1.00 25.26  ? 291 TRP B C   1 
ATOM   6545  O O   . TRP B  1 291 ? -2.225   -4.299  -71.310  1.00 25.44  ? 291 TRP B O   1 
ATOM   6546  C CB  . TRP B  1 291 ? 0.332    -5.109  -71.019  1.00 25.94  ? 291 TRP B CB  1 
ATOM   6547  C CG  . TRP B  1 291 ? 1.828    -5.285  -70.952  1.00 27.01  ? 291 TRP B CG  1 
ATOM   6548  C CD1 . TRP B  1 291 ? 2.496    -5.934  -69.956  1.00 27.27  ? 291 TRP B CD1 1 
ATOM   6549  C CD2 . TRP B  1 291 ? 2.844    -4.816  -71.876  1.00 27.34  ? 291 TRP B CD2 1 
ATOM   6550  N NE1 . TRP B  1 291 ? 3.842    -5.899  -70.201  1.00 29.19  ? 291 TRP B NE1 1 
ATOM   6551  C CE2 . TRP B  1 291 ? 4.090    -5.224  -71.362  1.00 27.59  ? 291 TRP B CE2 1 
ATOM   6552  C CE3 . TRP B  1 291 ? 2.833    -4.061  -73.058  1.00 27.24  ? 291 TRP B CE3 1 
ATOM   6553  C CZ2 . TRP B  1 291 ? 5.292    -4.948  -71.998  1.00 27.51  ? 291 TRP B CZ2 1 
ATOM   6554  C CZ3 . TRP B  1 291 ? 4.015    -3.778  -73.697  1.00 26.71  ? 291 TRP B CZ3 1 
ATOM   6555  C CH2 . TRP B  1 291 ? 5.237    -4.231  -73.175  1.00 27.77  ? 291 TRP B CH2 1 
ATOM   6556  N N   . PHE B  1 292 ? -2.449   -3.249  -69.346  1.00 26.28  ? 292 PHE B N   1 
ATOM   6557  C CA  . PHE B  1 292 ? -3.888   -3.102  -69.512  1.00 26.12  ? 292 PHE B CA  1 
ATOM   6558  C C   . PHE B  1 292 ? -4.307   -1.738  -70.030  1.00 26.52  ? 292 PHE B C   1 
ATOM   6559  O O   . PHE B  1 292 ? -5.494   -1.516  -70.339  1.00 25.73  ? 292 PHE B O   1 
ATOM   6560  C CB  . PHE B  1 292 ? -4.577   -3.259  -68.166  1.00 28.24  ? 292 PHE B CB  1 
ATOM   6561  C CG  . PHE B  1 292 ? -5.067   -4.676  -67.939  1.00 28.41  ? 292 PHE B CG  1 
ATOM   6562  C CD1 . PHE B  1 292 ? -6.276   -5.077  -68.455  1.00 29.64  ? 292 PHE B CD1 1 
ATOM   6563  C CD2 . PHE B  1 292 ? -4.302   -5.586  -67.222  1.00 29.88  ? 292 PHE B CD2 1 
ATOM   6564  C CE1 . PHE B  1 292 ? -6.721   -6.372  -68.259  1.00 31.01  ? 292 PHE B CE1 1 
ATOM   6565  C CE2 . PHE B  1 292 ? -4.748   -6.869  -67.019  1.00 31.22  ? 292 PHE B CE2 1 
ATOM   6566  C CZ  . PHE B  1 292 ? -5.969   -7.256  -67.517  1.00 31.04  ? 292 PHE B CZ  1 
ATOM   6567  N N   . GLY B  1 293 ? -3.344   -0.811  -70.101  1.00 28.05  ? 293 GLY B N   1 
ATOM   6568  C CA  . GLY B  1 293 ? -3.674   0.590   -70.330  1.00 27.75  ? 293 GLY B CA  1 
ATOM   6569  C C   . GLY B  1 293 ? -4.176   0.844   -71.744  1.00 26.52  ? 293 GLY B C   1 
ATOM   6570  O O   . GLY B  1 293 ? -3.730   0.176   -72.668  1.00 26.47  ? 293 GLY B O   1 
ATOM   6571  N N   . PHE B  1 294 ? -5.077   1.830   -71.885  1.00 25.87  ? 294 PHE B N   1 
ATOM   6572  C CA  . PHE B  1 294 ? -5.367   2.433   -73.174  1.00 26.33  ? 294 PHE B CA  1 
ATOM   6573  C C   . PHE B  1 294 ? -4.171   3.250   -73.677  1.00 28.29  ? 294 PHE B C   1 
ATOM   6574  O O   . PHE B  1 294 ? -4.060   3.514   -74.879  1.00 30.26  ? 294 PHE B O   1 
ATOM   6575  C CB  . PHE B  1 294 ? -6.638   3.286   -73.079  1.00 25.03  ? 294 PHE B CB  1 
ATOM   6576  C CG  . PHE B  1 294 ? -7.930   2.500   -72.897  1.00 24.35  ? 294 PHE B CG  1 
ATOM   6577  C CD1 . PHE B  1 294 ? -7.908   1.128   -72.664  1.00 23.85  ? 294 PHE B CD1 1 
ATOM   6578  C CD2 . PHE B  1 294 ? -9.160   3.160   -72.869  1.00 24.51  ? 294 PHE B CD2 1 
ATOM   6579  C CE1 . PHE B  1 294 ? -9.081   0.427   -72.436  1.00 23.96  ? 294 PHE B CE1 1 
ATOM   6580  C CE2 . PHE B  1 294 ? -10.335  2.463   -72.637  1.00 25.66  ? 294 PHE B CE2 1 
ATOM   6581  C CZ  . PHE B  1 294 ? -10.294  1.080   -72.427  1.00 25.36  ? 294 PHE B CZ  1 
ATOM   6582  N N   . TRP B  1 295 ? -3.298   3.693   -72.763  1.00 30.43  ? 295 TRP B N   1 
ATOM   6583  C CA  . TRP B  1 295 ? -2.066   4.400   -73.125  1.00 31.29  ? 295 TRP B CA  1 
ATOM   6584  C C   . TRP B  1 295 ? -0.886   3.543   -72.717  1.00 30.85  ? 295 TRP B C   1 
ATOM   6585  O O   . TRP B  1 295 ? -0.980   2.819   -71.735  1.00 33.59  ? 295 TRP B O   1 
ATOM   6586  C CB  . TRP B  1 295 ? -1.966   5.774   -72.443  1.00 29.82  ? 295 TRP B CB  1 
ATOM   6587  C CG  . TRP B  1 295 ? -2.878   6.833   -73.000  1.00 29.96  ? 295 TRP B CG  1 
ATOM   6588  C CD1 . TRP B  1 295 ? -4.243   6.771   -73.153  1.00 30.78  ? 295 TRP B CD1 1 
ATOM   6589  C CD2 . TRP B  1 295 ? -2.480   8.136   -73.491  1.00 28.31  ? 295 TRP B CD2 1 
ATOM   6590  N NE1 . TRP B  1 295 ? -4.712   7.940   -73.703  1.00 29.16  ? 295 TRP B NE1 1 
ATOM   6591  C CE2 . TRP B  1 295 ? -3.649   8.788   -73.935  1.00 27.86  ? 295 TRP B CE2 1 
ATOM   6592  C CE3 . TRP B  1 295 ? -1.259   8.797   -73.615  1.00 28.88  ? 295 TRP B CE3 1 
ATOM   6593  C CZ2 . TRP B  1 295 ? -3.627   10.068  -74.484  1.00 28.45  ? 295 TRP B CZ2 1 
ATOM   6594  C CZ3 . TRP B  1 295 ? -1.240   10.059  -74.178  1.00 30.11  ? 295 TRP B CZ3 1 
ATOM   6595  C CH2 . TRP B  1 295 ? -2.409   10.688  -74.614  1.00 29.05  ? 295 TRP B CH2 1 
ATOM   6596  N N   . GLY B  1 296 ? 0.210    3.627   -73.467  1.00 30.93  ? 296 GLY B N   1 
ATOM   6597  C CA  . GLY B  1 296 ? 1.422    2.895   -73.127  1.00 29.75  ? 296 GLY B CA  1 
ATOM   6598  C C   . GLY B  1 296 ? 2.658    3.796   -73.127  1.00 29.74  ? 296 GLY B C   1 
ATOM   6599  O O   . GLY B  1 296 ? 2.724    4.755   -73.875  1.00 28.36  ? 296 GLY B O   1 
ATOM   6600  N N   . TYR B  1 297 ? 3.671    3.421   -72.332  1.00 30.36  ? 297 TYR B N   1 
ATOM   6601  C CA  . TYR B  1 297 ? 4.877    4.223   -72.185  1.00 30.21  ? 297 TYR B CA  1 
ATOM   6602  C C   . TYR B  1 297 ? 6.020    3.561   -72.948  1.00 30.42  ? 297 TYR B C   1 
ATOM   6603  O O   . TYR B  1 297 ? 6.159    2.335   -72.960  1.00 29.98  ? 297 TYR B O   1 
ATOM   6604  C CB  . TYR B  1 297 ? 5.225    4.392   -70.705  1.00 30.82  ? 297 TYR B CB  1 
ATOM   6605  C CG  . TYR B  1 297 ? 4.120    5.015   -69.870  1.00 31.60  ? 297 TYR B CG  1 
ATOM   6606  C CD1 . TYR B  1 297 ? 3.907    6.395   -69.869  1.00 32.90  ? 297 TYR B CD1 1 
ATOM   6607  C CD2 . TYR B  1 297 ? 3.251    4.226   -69.124  1.00 30.98  ? 297 TYR B CD2 1 
ATOM   6608  C CE1 . TYR B  1 297 ? 2.892    6.975   -69.119  1.00 31.42  ? 297 TYR B CE1 1 
ATOM   6609  C CE2 . TYR B  1 297 ? 2.242    4.796   -68.374  1.00 29.85  ? 297 TYR B CE2 1 
ATOM   6610  C CZ  . TYR B  1 297 ? 2.057    6.164   -68.370  1.00 30.60  ? 297 TYR B CZ  1 
ATOM   6611  O OH  . TYR B  1 297 ? 1.035    6.699   -67.628  1.00 30.44  ? 297 TYR B OH  1 
ATOM   6612  N N   . SER B  1 298 ? 6.839    4.400   -73.597  1.00 30.67  ? 298 SER B N   1 
ATOM   6613  C CA  . SER B  1 298 ? 7.849    3.937   -74.523  1.00 30.70  ? 298 SER B CA  1 
ATOM   6614  C C   . SER B  1 298 ? 8.974    3.279   -73.749  1.00 31.71  ? 298 SER B C   1 
ATOM   6615  O O   . SER B  1 298 ? 9.548    2.313   -74.232  1.00 31.52  ? 298 SER B O   1 
ATOM   6616  C CB  . SER B  1 298 ? 8.399    5.053   -75.373  1.00 31.33  ? 298 SER B CB  1 
ATOM   6617  O OG  . SER B  1 298 ? 9.063    5.993   -74.547  1.00 31.86  ? 298 SER B OG  1 
ATOM   6618  N N   . ASP B  1 299 ? 9.332    3.870   -72.597  1.00 33.20  ? 299 ASP B N   1 
ATOM   6619  C CA  . ASP B  1 299 ? 10.436   3.361   -71.795  1.00 34.00  ? 299 ASP B CA  1 
ATOM   6620  C C   . ASP B  1 299 ? 10.352   3.956   -70.393  1.00 35.15  ? 299 ASP B C   1 
ATOM   6621  O O   . ASP B  1 299 ? 9.453    4.739   -70.097  1.00 36.13  ? 299 ASP B O   1 
ATOM   6622  C CB  . ASP B  1 299 ? 11.744   3.575   -72.524  1.00 34.82  ? 299 ASP B CB  1 
ATOM   6623  C CG  . ASP B  1 299 ? 12.183   5.023   -72.726  1.00 37.02  ? 299 ASP B CG  1 
ATOM   6624  O OD1 . ASP B  1 299 ? 11.631   5.965   -72.081  1.00 35.84  ? 299 ASP B OD1 1 
ATOM   6625  O OD2 . ASP B  1 299 ? 13.176   5.196   -73.465  1.00 41.24  ? 299 ASP B OD2 1 
ATOM   6626  N N   . LEU B  1 300 ? 11.304   3.581   -69.533  1.00 37.05  ? 300 LEU B N   1 
ATOM   6627  C CA  . LEU B  1 300 ? 11.315   3.981   -68.133  1.00 37.31  ? 300 LEU B CA  1 
ATOM   6628  C C   . LEU B  1 300 ? 11.239   5.499   -67.941  1.00 37.20  ? 300 LEU B C   1 
ATOM   6629  O O   . LEU B  1 300 ? 10.791   5.939   -66.895  1.00 35.57  ? 300 LEU B O   1 
ATOM   6630  C CB  . LEU B  1 300 ? 12.578   3.436   -67.462  1.00 37.10  ? 300 LEU B CB  1 
ATOM   6631  C CG  . LEU B  1 300 ? 12.740   3.797   -65.981  1.00 35.74  ? 300 LEU B CG  1 
ATOM   6632  C CD1 . LEU B  1 300 ? 11.442   3.465   -65.227  1.00 34.35  ? 300 LEU B CD1 1 
ATOM   6633  C CD2 . LEU B  1 300 ? 13.938   3.090   -65.381  1.00 35.94  ? 300 LEU B CD2 1 
ATOM   6634  N N   . ASN B  1 301 ? 11.744   6.277   -68.905  1.00 38.47  ? 301 ASN B N   1 
ATOM   6635  C CA  . ASN B  1 301 ? 11.816   7.728   -68.779  1.00 39.43  ? 301 ASN B CA  1 
ATOM   6636  C C   . ASN B  1 301 ? 10.599   8.440   -69.379  1.00 38.84  ? 301 ASN B C   1 
ATOM   6637  O O   . ASN B  1 301 ? 10.560   9.664   -69.396  1.00 38.31  ? 301 ASN B O   1 
ATOM   6638  C CB  . ASN B  1 301 ? 13.055   8.247   -69.489  1.00 40.76  ? 301 ASN B CB  1 
ATOM   6639  C CG  . ASN B  1 301 ? 14.274   7.934   -68.680  1.00 43.95  ? 301 ASN B CG  1 
ATOM   6640  O OD1 . ASN B  1 301 ? 15.208   7.300   -69.168  1.00 47.26  ? 301 ASN B OD1 1 
ATOM   6641  N ND2 . ASN B  1 301 ? 14.272   8.344   -67.426  1.00 46.48  ? 301 ASN B ND2 1 
ATOM   6642  N N   . ASP B  1 302 ? 9.627    7.694   -69.912  1.00 36.65  ? 302 ASP B N   1 
ATOM   6643  C CA  . ASP B  1 302 ? 8.478    8.328   -70.523  1.00 37.10  ? 302 ASP B CA  1 
ATOM   6644  C C   . ASP B  1 302 ? 7.436    8.594   -69.429  1.00 36.85  ? 302 ASP B C   1 
ATOM   6645  O O   . ASP B  1 302 ? 6.963    7.698   -68.745  1.00 35.57  ? 302 ASP B O   1 
ATOM   6646  C CB  . ASP B  1 302 ? 8.025    7.532   -71.746  1.00 37.81  ? 302 ASP B CB  1 
ATOM   6647  C CG  . ASP B  1 302 ? 6.800    8.061   -72.497  1.00 35.85  ? 302 ASP B CG  1 
ATOM   6648  O OD1 . ASP B  1 302 ? 6.297    9.130   -72.077  1.00 35.79  ? 302 ASP B OD1 1 
ATOM   6649  O OD2 . ASP B  1 302 ? 6.364    7.415   -73.500  1.00 32.26  ? 302 ASP B OD2 1 
ATOM   6650  N N   . LYS B  1 303 ? 7.047    9.853   -69.260  1.00 37.49  ? 303 LYS B N   1 
ATOM   6651  C CA  . LYS B  1 303 ? 6.067    10.199  -68.247  1.00 37.38  ? 303 LYS B CA  1 
ATOM   6652  C C   . LYS B  1 303 ? 4.695    10.429  -68.887  1.00 32.76  ? 303 LYS B C   1 
ATOM   6653  O O   . LYS B  1 303 ? 3.749    10.765  -68.193  1.00 29.77  ? 303 LYS B O   1 
ATOM   6654  C CB  . LYS B  1 303 ? 6.526    11.488  -67.541  1.00 43.58  ? 303 LYS B CB  1 
ATOM   6655  C CG  . LYS B  1 303 ? 7.871    11.484  -66.821  1.00 48.99  ? 303 LYS B CG  1 
ATOM   6656  C CD  . LYS B  1 303 ? 7.929    10.743  -65.487  1.00 54.22  ? 303 LYS B CD  1 
ATOM   6657  C CE  . LYS B  1 303 ? 9.359    10.715  -64.985  1.00 59.99  ? 303 LYS B CE  1 
ATOM   6658  N NZ  . LYS B  1 303 ? 9.434    9.855   -63.804  1.00 63.42  ? 303 LYS B NZ  1 
ATOM   6659  N N   . TYR B  1 304 ? 4.601    10.302  -70.216  1.00 32.37  ? 304 TYR B N   1 
ATOM   6660  C CA  . TYR B  1 304 ? 3.457    10.819  -70.954  1.00 33.29  ? 304 TYR B CA  1 
ATOM   6661  C C   . TYR B  1 304 ? 2.736    9.665   -71.647  1.00 32.10  ? 304 TYR B C   1 
ATOM   6662  O O   . TYR B  1 304 ? 1.561    9.433   -71.389  1.00 32.10  ? 304 TYR B O   1 
ATOM   6663  C CB  . TYR B  1 304 ? 3.859    11.963  -71.908  1.00 34.46  ? 304 TYR B CB  1 
ATOM   6664  C CG  . TYR B  1 304 ? 4.409    13.167  -71.153  1.00 35.58  ? 304 TYR B CG  1 
ATOM   6665  C CD1 . TYR B  1 304 ? 3.564    14.026  -70.456  1.00 34.46  ? 304 TYR B CD1 1 
ATOM   6666  C CD2 . TYR B  1 304 ? 5.782    13.391  -71.066  1.00 37.76  ? 304 TYR B CD2 1 
ATOM   6667  C CE1 . TYR B  1 304 ? 4.065    15.091  -69.726  1.00 34.90  ? 304 TYR B CE1 1 
ATOM   6668  C CE2 . TYR B  1 304 ? 6.295    14.466  -70.345  1.00 38.75  ? 304 TYR B CE2 1 
ATOM   6669  C CZ  . TYR B  1 304 ? 5.425    15.303  -69.672  1.00 37.07  ? 304 TYR B CZ  1 
ATOM   6670  O OH  . TYR B  1 304 ? 5.913    16.324  -68.952  1.00 39.45  ? 304 TYR B OH  1 
ATOM   6671  N N   . GLY B  1 305 ? 3.469    8.945   -72.497  1.00 30.77  ? 305 GLY B N   1 
ATOM   6672  C CA  . GLY B  1 305 ? 2.936    7.802   -73.207  1.00 29.68  ? 305 GLY B CA  1 
ATOM   6673  C C   . GLY B  1 305 ? 2.119    8.214   -74.419  1.00 29.40  ? 305 GLY B C   1 
ATOM   6674  O O   . GLY B  1 305 ? 1.962    9.418   -74.653  1.00 29.22  ? 305 GLY B O   1 
ATOM   6675  N N   . THR B  1 306 ? 1.574    7.206   -75.140  1.00 28.82  ? 306 THR B N   1 
ATOM   6676  C CA  . THR B  1 306 ? 0.746    7.443   -76.321  1.00 27.98  ? 306 THR B CA  1 
ATOM   6677  C C   . THR B  1 306 ? -0.452   6.496   -76.300  1.00 27.43  ? 306 THR B C   1 
ATOM   6678  O O   . THR B  1 306 ? -0.395   5.442   -75.683  1.00 26.86  ? 306 THR B O   1 
ATOM   6679  C CB  . THR B  1 306 ? 1.568    7.312   -77.614  1.00 28.22  ? 306 THR B CB  1 
ATOM   6680  O OG1 . THR B  1 306 ? 2.055    5.964   -77.796  1.00 25.94  ? 306 THR B OG1 1 
ATOM   6681  C CG2 . THR B  1 306 ? 2.681    8.365   -77.682  1.00 28.50  ? 306 THR B CG2 1 
ATOM   6682  N N   . PRO B  1 307 ? -1.573   6.872   -76.959  1.00 27.93  ? 307 PRO B N   1 
ATOM   6683  C CA  . PRO B  1 307 ? -2.781   6.054   -76.966  1.00 27.20  ? 307 PRO B CA  1 
ATOM   6684  C C   . PRO B  1 307 ? -2.650   4.865   -77.906  1.00 28.40  ? 307 PRO B C   1 
ATOM   6685  O O   . PRO B  1 307 ? -2.190   5.013   -79.017  1.00 30.15  ? 307 PRO B O   1 
ATOM   6686  C CB  . PRO B  1 307 ? -3.886   7.019   -77.415  1.00 27.03  ? 307 PRO B CB  1 
ATOM   6687  C CG  . PRO B  1 307 ? -3.148   8.131   -78.206  1.00 27.00  ? 307 PRO B CG  1 
ATOM   6688  C CD  . PRO B  1 307 ? -1.765   8.173   -77.640  1.00 28.19  ? 307 PRO B CD  1 
ATOM   6689  N N   . ARG B  1 308 ? -3.094   3.695   -77.446  1.00 27.93  ? 308 ARG B N   1 
ATOM   6690  C CA  . ARG B  1 308 ? -3.259   2.517   -78.295  1.00 28.67  ? 308 ARG B CA  1 
ATOM   6691  C C   . ARG B  1 308 ? -4.565   2.615   -79.110  1.00 26.62  ? 308 ARG B C   1 
ATOM   6692  O O   . ARG B  1 308 ? -5.423   3.454   -78.806  1.00 25.31  ? 308 ARG B O   1 
ATOM   6693  C CB  . ARG B  1 308 ? -3.235   1.279   -77.379  1.00 27.73  ? 308 ARG B CB  1 
ATOM   6694  C CG  . ARG B  1 308 ? -1.873   1.065   -76.733  1.00 28.41  ? 308 ARG B CG  1 
ATOM   6695  C CD  . ARG B  1 308 ? -1.948   0.038   -75.603  1.00 28.41  ? 308 ARG B CD  1 
ATOM   6696  N NE  . ARG B  1 308 ? -0.602   -0.305  -75.137  1.00 28.25  ? 308 ARG B NE  1 
ATOM   6697  C CZ  . ARG B  1 308 ? -0.252   -0.623  -73.900  1.00 29.32  ? 308 ARG B CZ  1 
ATOM   6698  N NH1 . ARG B  1 308 ? -1.165   -0.764  -72.967  1.00 31.54  ? 308 ARG B NH1 1 
ATOM   6699  N NH2 . ARG B  1 308 ? 1.006    -0.882  -73.609  1.00 29.49  ? 308 ARG B NH2 1 
ATOM   6700  N N   . PRO B  1 309 ? -4.740   1.794   -80.181  1.00 25.98  ? 309 PRO B N   1 
ATOM   6701  C CA  . PRO B  1 309 ? -5.946   1.818   -81.006  1.00 26.78  ? 309 PRO B CA  1 
ATOM   6702  C C   . PRO B  1 309 ? -7.268   1.817   -80.242  1.00 28.49  ? 309 PRO B C   1 
ATOM   6703  O O   . PRO B  1 309 ? -8.204   2.527   -80.632  1.00 30.96  ? 309 PRO B O   1 
ATOM   6704  C CB  . PRO B  1 309 ? -5.784   0.585   -81.881  1.00 26.62  ? 309 PRO B CB  1 
ATOM   6705  C CG  . PRO B  1 309 ? -4.292   0.523   -82.103  1.00 28.18  ? 309 PRO B CG  1 
ATOM   6706  C CD  . PRO B  1 309 ? -3.731   0.867   -80.730  1.00 27.32  ? 309 PRO B CD  1 
ATOM   6707  N N   . VAL B  1 310 ? -7.328   1.043   -79.149  1.00 27.21  ? 310 VAL B N   1 
ATOM   6708  C CA  . VAL B  1 310 ? -8.525   0.985   -78.317  1.00 27.90  ? 310 VAL B CA  1 
ATOM   6709  C C   . VAL B  1 310 ? -9.024   2.372   -77.878  1.00 27.72  ? 310 VAL B C   1 
ATOM   6710  O O   . VAL B  1 310 ? -10.236  2.588   -77.775  1.00 26.43  ? 310 VAL B O   1 
ATOM   6711  C CB  . VAL B  1 310 ? -8.274   0.076   -77.110  1.00 27.35  ? 310 VAL B CB  1 
ATOM   6712  C CG1 . VAL B  1 310 ? -7.053   0.514   -76.310  1.00 29.03  ? 310 VAL B CG1 1 
ATOM   6713  C CG2 . VAL B  1 310 ? -9.509   -0.015  -76.243  1.00 26.60  ? 310 VAL B CG2 1 
ATOM   6714  N N   . TRP B  1 311 ? -8.093   3.300   -77.606  1.00 26.21  ? 311 TRP B N   1 
ATOM   6715  C CA  . TRP B  1 311 ? -8.437   4.644   -77.176  1.00 26.41  ? 311 TRP B CA  1 
ATOM   6716  C C   . TRP B  1 311 ? -9.377   5.328   -78.150  1.00 25.90  ? 311 TRP B C   1 
ATOM   6717  O O   . TRP B  1 311 ? -10.325  5.970   -77.717  1.00 25.94  ? 311 TRP B O   1 
ATOM   6718  C CB  . TRP B  1 311 ? -7.159   5.472   -77.054  1.00 27.83  ? 311 TRP B CB  1 
ATOM   6719  C CG  . TRP B  1 311 ? -7.373   6.900   -76.631  1.00 28.91  ? 311 TRP B CG  1 
ATOM   6720  C CD1 . TRP B  1 311 ? -7.278   8.008   -77.421  1.00 28.22  ? 311 TRP B CD1 1 
ATOM   6721  C CD2 . TRP B  1 311 ? -7.659   7.373   -75.296  1.00 29.39  ? 311 TRP B CD2 1 
ATOM   6722  N NE1 . TRP B  1 311 ? -7.432   9.126   -76.672  1.00 28.33  ? 311 TRP B NE1 1 
ATOM   6723  C CE2 . TRP B  1 311 ? -7.684   8.779   -75.371  1.00 28.49  ? 311 TRP B CE2 1 
ATOM   6724  C CE3 . TRP B  1 311 ? -7.894   6.749   -74.061  1.00 29.91  ? 311 TRP B CE3 1 
ATOM   6725  C CZ2 . TRP B  1 311 ? -7.898   9.580   -74.253  1.00 28.80  ? 311 TRP B CZ2 1 
ATOM   6726  C CZ3 . TRP B  1 311 ? -8.129   7.538   -72.957  1.00 30.77  ? 311 TRP B CZ3 1 
ATOM   6727  C CH2 . TRP B  1 311 ? -8.084   8.940   -73.051  1.00 30.58  ? 311 TRP B CH2 1 
ATOM   6728  N N   . PHE B  1 312 ? -9.060   5.187   -79.443  1.00 27.71  ? 312 PHE B N   1 
ATOM   6729  C CA  . PHE B  1 312 ? -9.782   5.809   -80.538  1.00 29.47  ? 312 PHE B CA  1 
ATOM   6730  C C   . PHE B  1 312 ? -11.094  5.083   -80.824  1.00 29.73  ? 312 PHE B C   1 
ATOM   6731  O O   . PHE B  1 312 ? -12.100  5.734   -81.108  1.00 30.29  ? 312 PHE B O   1 
ATOM   6732  C CB  . PHE B  1 312 ? -8.880   5.879   -81.776  1.00 29.88  ? 312 PHE B CB  1 
ATOM   6733  C CG  . PHE B  1 312 ? -7.671   6.765   -81.536  1.00 30.78  ? 312 PHE B CG  1 
ATOM   6734  C CD1 . PHE B  1 312 ? -7.785   8.153   -81.528  1.00 32.04  ? 312 PHE B CD1 1 
ATOM   6735  C CD2 . PHE B  1 312 ? -6.427   6.208   -81.286  1.00 31.89  ? 312 PHE B CD2 1 
ATOM   6736  C CE1 . PHE B  1 312 ? -6.683   8.969   -81.268  1.00 32.91  ? 312 PHE B CE1 1 
ATOM   6737  C CE2 . PHE B  1 312 ? -5.317   7.033   -81.069  1.00 33.99  ? 312 PHE B CE2 1 
ATOM   6738  C CZ  . PHE B  1 312 ? -5.443   8.410   -81.060  1.00 31.85  ? 312 PHE B CZ  1 
ATOM   6739  N N   . ALA B  1 313 ? -11.102  3.749   -80.763  1.00 29.95  ? 313 ALA B N   1 
ATOM   6740  C CA  . ALA B  1 313 ? -12.341  3.019   -81.007  1.00 29.05  ? 313 ALA B CA  1 
ATOM   6741  C C   . ALA B  1 313 ? -13.357  3.370   -79.929  1.00 29.54  ? 313 ALA B C   1 
ATOM   6742  O O   . ALA B  1 313 ? -14.533  3.632   -80.249  1.00 31.32  ? 313 ALA B O   1 
ATOM   6743  C CB  . ALA B  1 313 ? -12.098  1.542   -81.075  1.00 28.53  ? 313 ALA B CB  1 
ATOM   6744  N N   . MET B  1 314 ? -12.867  3.440   -78.680  1.00 29.28  ? 314 MET B N   1 
ATOM   6745  C CA  . MET B  1 314 ? -13.702  3.753   -77.520  1.00 30.61  ? 314 MET B CA  1 
ATOM   6746  C C   . MET B  1 314 ? -14.279  5.170   -77.606  1.00 30.82  ? 314 MET B C   1 
ATOM   6747  O O   . MET B  1 314 ? -15.482  5.376   -77.426  1.00 27.71  ? 314 MET B O   1 
ATOM   6748  C CB  . MET B  1 314 ? -12.884  3.631   -76.237  1.00 32.37  ? 314 MET B CB  1 
ATOM   6749  C CG  . MET B  1 314 ? -12.665  2.176   -75.801  1.00 33.08  ? 314 MET B CG  1 
ATOM   6750  S SD  . MET B  1 314 ? -14.190  1.478   -75.132  1.00 32.37  ? 314 MET B SD  1 
ATOM   6751  C CE  . MET B  1 314 ? -14.217  2.290   -73.534  1.00 32.56  ? 314 MET B CE  1 
ATOM   6752  N N   . ARG B  1 315 ? -13.415  6.153   -77.902  1.00 31.80  ? 315 ARG B N   1 
ATOM   6753  C CA  . ARG B  1 315 ? -13.886  7.507   -78.179  1.00 33.01  ? 315 ARG B CA  1 
ATOM   6754  C C   . ARG B  1 315 ? -15.029  7.480   -79.208  1.00 32.27  ? 315 ARG B C   1 
ATOM   6755  O O   . ARG B  1 315 ? -16.068  8.075   -78.970  1.00 30.90  ? 315 ARG B O   1 
ATOM   6756  C CB  . ARG B  1 315 ? -12.776  8.448   -78.679  1.00 32.09  ? 315 ARG B CB  1 
ATOM   6757  C CG  . ARG B  1 315 ? -13.248  9.868   -78.972  1.00 31.91  ? 315 ARG B CG  1 
ATOM   6758  C CD  . ARG B  1 315 ? -12.164  10.712  -79.611  1.00 31.49  ? 315 ARG B CD  1 
ATOM   6759  N NE  . ARG B  1 315 ? -11.928  10.200  -80.967  1.00 34.04  ? 315 ARG B NE  1 
ATOM   6760  C CZ  . ARG B  1 315 ? -10.871  10.479  -81.747  1.00 33.76  ? 315 ARG B CZ  1 
ATOM   6761  N NH1 . ARG B  1 315 ? -9.960   11.322  -81.336  1.00 34.02  ? 315 ARG B NH1 1 
ATOM   6762  N NH2 . ARG B  1 315 ? -10.720  9.911   -82.930  1.00 34.08  ? 315 ARG B NH2 1 
ATOM   6763  N N   . ASP B  1 316 ? -14.824  6.810   -80.354  1.00 31.46  ? 316 ASP B N   1 
ATOM   6764  C CA  . ASP B  1 316 ? -15.792  6.826   -81.437  1.00 31.10  ? 316 ASP B CA  1 
ATOM   6765  C C   . ASP B  1 316 ? -17.045  6.082   -81.007  1.00 29.24  ? 316 ASP B C   1 
ATOM   6766  O O   . ASP B  1 316 ? -18.156  6.492   -81.330  1.00 29.31  ? 316 ASP B O   1 
ATOM   6767  C CB  . ASP B  1 316 ? -15.218  6.301   -82.744  1.00 32.96  ? 316 ASP B CB  1 
ATOM   6768  C CG  . ASP B  1 316 ? -14.110  7.128   -83.403  1.00 33.07  ? 316 ASP B CG  1 
ATOM   6769  O OD1 . ASP B  1 316 ? -13.825  8.247   -82.933  1.00 31.40  ? 316 ASP B OD1 1 
ATOM   6770  O OD2 . ASP B  1 316 ? -13.521  6.628   -84.390  1.00 34.80  ? 316 ASP B OD2 1 
ATOM   6771  N N   . TYR B  1 317 ? -16.868  5.032   -80.217  1.00 27.08  ? 317 TYR B N   1 
ATOM   6772  C CA  . TYR B  1 317 ? -18.024  4.257   -79.792  1.00 26.94  ? 317 TYR B CA  1 
ATOM   6773  C C   . TYR B  1 317 ? -18.943  5.091   -78.902  1.00 26.97  ? 317 TYR B C   1 
ATOM   6774  O O   . TYR B  1 317 ? -20.161  4.941   -78.939  1.00 26.63  ? 317 TYR B O   1 
ATOM   6775  C CB  . TYR B  1 317 ? -17.582  2.980   -79.064  1.00 26.07  ? 317 TYR B CB  1 
ATOM   6776  C CG  . TYR B  1 317 ? -18.737  2.066   -78.708  1.00 24.09  ? 317 TYR B CG  1 
ATOM   6777  C CD1 . TYR B  1 317 ? -19.270  1.210   -79.664  1.00 24.95  ? 317 TYR B CD1 1 
ATOM   6778  C CD2 . TYR B  1 317 ? -19.279  2.043   -77.425  1.00 22.65  ? 317 TYR B CD2 1 
ATOM   6779  C CE1 . TYR B  1 317 ? -20.357  0.387   -79.375  1.00 23.83  ? 317 TYR B CE1 1 
ATOM   6780  C CE2 . TYR B  1 317 ? -20.371  1.236   -77.133  1.00 23.26  ? 317 TYR B CE2 1 
ATOM   6781  C CZ  . TYR B  1 317 ? -20.902  0.399   -78.108  1.00 22.81  ? 317 TYR B CZ  1 
ATOM   6782  O OH  . TYR B  1 317 ? -21.981  -0.396  -77.854  1.00 22.91  ? 317 TYR B OH  1 
ATOM   6783  N N   . MET B  1 318 ? -18.343  5.932   -78.062  1.00 28.65  ? 318 MET B N   1 
ATOM   6784  C CA  . MET B  1 318 ? -19.061  6.612   -76.991  1.00 29.31  ? 318 MET B CA  1 
ATOM   6785  C C   . MET B  1 318 ? -19.880  7.795   -77.528  1.00 27.69  ? 318 MET B C   1 
ATOM   6786  O O   . MET B  1 318 ? -20.657  8.368   -76.778  1.00 26.13  ? 318 MET B O   1 
ATOM   6787  C CB  . MET B  1 318 ? -18.108  7.102   -75.880  1.00 29.54  ? 318 MET B CB  1 
ATOM   6788  C CG  . MET B  1 318 ? -17.637  6.022   -74.902  1.00 28.95  ? 318 MET B CG  1 
ATOM   6789  S SD  . MET B  1 318 ? -16.661  6.635   -73.506  1.00 31.05  ? 318 MET B SD  1 
ATOM   6790  C CE  . MET B  1 318 ? -15.241  7.330   -74.360  1.00 31.81  ? 318 MET B CE  1 
ATOM   6791  N N   . LYS B  1 319 ? -19.751  8.158   -78.803  1.00 28.24  ? 319 LYS B N   1 
ATOM   6792  C CA  . LYS B  1 319 ? -20.410  9.381   -79.238  1.00 32.59  ? 319 LYS B CA  1 
ATOM   6793  C C   . LYS B  1 319 ? -21.929  9.232   -79.146  1.00 34.06  ? 319 LYS B C   1 
ATOM   6794  O O   . LYS B  1 319 ? -22.610  10.209  -78.844  1.00 33.77  ? 319 LYS B O   1 
ATOM   6795  C CB  . LYS B  1 319 ? -19.964  9.795   -80.638  1.00 35.83  ? 319 LYS B CB  1 
ATOM   6796  C CG  . LYS B  1 319 ? -18.485  10.223  -80.742  1.00 38.51  ? 319 LYS B CG  1 
ATOM   6797  C CD  . LYS B  1 319 ? -18.157  10.795  -82.124  1.00 44.25  ? 319 LYS B CD  1 
ATOM   6798  C CE  . LYS B  1 319 ? -16.684  10.936  -82.483  1.00 50.11  ? 319 LYS B CE  1 
ATOM   6799  N NZ  . LYS B  1 319 ? -16.464  10.890  -83.939  1.00 49.58  ? 319 LYS B NZ  1 
ATOM   6800  N N   . GLY B  1 320 ? -22.427  8.004   -79.381  1.00 31.29  ? 320 GLY B N   1 
ATOM   6801  C CA  . GLY B  1 320 ? -23.837  7.689   -79.241  1.00 31.07  ? 320 GLY B CA  1 
ATOM   6802  C C   . GLY B  1 320 ? -24.052  6.244   -78.765  1.00 30.13  ? 320 GLY B C   1 
ATOM   6803  O O   . GLY B  1 320 ? -23.669  5.279   -79.411  1.00 30.94  ? 320 GLY B O   1 
ATOM   6804  N N   . LEU B  1 321 ? -24.660  6.093   -77.600  1.00 28.79  ? 321 LEU B N   1 
ATOM   6805  C CA  . LEU B  1 321 ? -24.855  4.789   -77.005  1.00 27.51  ? 321 LEU B CA  1 
ATOM   6806  C C   . LEU B  1 321 ? -26.310  4.365   -77.156  1.00 29.60  ? 321 LEU B C   1 
ATOM   6807  O O   . LEU B  1 321 ? -27.221  5.177   -76.968  1.00 29.55  ? 321 LEU B O   1 
ATOM   6808  C CB  . LEU B  1 321 ? -24.477  4.860   -75.534  1.00 27.31  ? 321 LEU B CB  1 
ATOM   6809  C CG  . LEU B  1 321 ? -23.010  5.162   -75.244  1.00 25.51  ? 321 LEU B CG  1 
ATOM   6810  C CD1 . LEU B  1 321 ? -22.933  5.345   -73.751  1.00 27.00  ? 321 LEU B CD1 1 
ATOM   6811  C CD2 . LEU B  1 321 ? -22.091  4.085   -75.732  1.00 24.03  ? 321 LEU B CD2 1 
ATOM   6812  N N   . ILE B  1 322 ? -26.483  3.081   -77.513  1.00 29.50  ? 322 ILE B N   1 
ATOM   6813  C CA  . ILE B  1 322 ? -27.773  2.435   -77.531  1.00 28.71  ? 322 ILE B CA  1 
ATOM   6814  C C   . ILE B  1 322 ? -27.891  1.597   -76.261  1.00 27.69  ? 322 ILE B C   1 
ATOM   6815  O O   . ILE B  1 322 ? -27.100  0.680   -76.035  1.00 26.10  ? 322 ILE B O   1 
ATOM   6816  C CB  . ILE B  1 322 ? -27.929  1.599   -78.809  1.00 29.66  ? 322 ILE B CB  1 
ATOM   6817  C CG1 . ILE B  1 322 ? -27.544  2.382   -80.038  1.00 30.20  ? 322 ILE B CG1 1 
ATOM   6818  C CG2 . ILE B  1 322 ? -29.339  1.032   -78.926  1.00 29.25  ? 322 ILE B CG2 1 
ATOM   6819  C CD1 . ILE B  1 322 ? -27.320  1.501   -81.259  1.00 31.01  ? 322 ILE B CD1 1 
ATOM   6820  N N   . ILE B  1 323 ? -28.875  1.986   -75.434  1.00 28.30  ? 323 ILE B N   1 
ATOM   6821  C CA  . ILE B  1 323 ? -29.230  1.319   -74.194  1.00 27.48  ? 323 ILE B CA  1 
ATOM   6822  C C   . ILE B  1 323 ? -30.414  0.387   -74.464  1.00 27.68  ? 323 ILE B C   1 
ATOM   6823  O O   . ILE B  1 323 ? -30.484  -0.729  -73.968  1.00 26.70  ? 323 ILE B O   1 
ATOM   6824  C CB  . ILE B  1 323 ? -29.534  2.358   -73.090  1.00 27.31  ? 323 ILE B CB  1 
ATOM   6825  C CG1 . ILE B  1 323 ? -28.279  3.061   -72.568  1.00 28.19  ? 323 ILE B CG1 1 
ATOM   6826  C CG2 . ILE B  1 323 ? -30.234  1.717   -71.905  1.00 27.38  ? 323 ILE B CG2 1 
ATOM   6827  C CD1 . ILE B  1 323 ? -27.745  4.143   -73.456  1.00 29.26  ? 323 ILE B CD1 1 
ATOM   6828  N N   . SER B  1 324 ? -31.388  0.870   -75.211  1.00 27.56  ? 324 SER B N   1 
ATOM   6829  C CA  . SER B  1 324 ? -32.473  0.014   -75.616  1.00 29.99  ? 324 SER B CA  1 
ATOM   6830  C C   . SER B  1 324 ? -32.757  0.331   -77.078  1.00 30.93  ? 324 SER B C   1 
ATOM   6831  O O   . SER B  1 324 ? -32.598  1.493   -77.460  1.00 31.81  ? 324 SER B O   1 
ATOM   6832  C CB  . SER B  1 324 ? -33.720  0.192   -74.726  1.00 31.23  ? 324 SER B CB  1 
ATOM   6833  O OG  . SER B  1 324 ? -33.426  0.153   -73.329  1.00 30.49  ? 324 SER B OG  1 
ATOM   6834  N N   . PRO B  1 325 ? -33.130  -0.662  -77.932  1.00 28.78  ? 325 PRO B N   1 
ATOM   6835  C CA  . PRO B  1 325 ? -33.156  -2.080  -77.560  1.00 28.36  ? 325 PRO B CA  1 
ATOM   6836  C C   . PRO B  1 325 ? -31.769  -2.695  -77.401  1.00 28.13  ? 325 PRO B C   1 
ATOM   6837  O O   . PRO B  1 325 ? -30.798  -2.173  -77.920  1.00 26.64  ? 325 PRO B O   1 
ATOM   6838  C CB  . PRO B  1 325 ? -33.898  -2.721  -78.731  1.00 29.36  ? 325 PRO B CB  1 
ATOM   6839  C CG  . PRO B  1 325 ? -33.556  -1.837  -79.900  1.00 29.11  ? 325 PRO B CG  1 
ATOM   6840  C CD  . PRO B  1 325 ? -33.553  -0.437  -79.316  1.00 29.21  ? 325 PRO B CD  1 
ATOM   6841  N N   . LYS B  1 326 ? -31.723  -3.852  -76.750  1.00 27.93  ? 326 LYS B N   1 
ATOM   6842  C CA  . LYS B  1 326 ? -30.486  -4.536  -76.418  1.00 27.74  ? 326 LYS B CA  1 
ATOM   6843  C C   . LYS B  1 326 ? -30.137  -5.650  -77.430  1.00 28.72  ? 326 LYS B C   1 
ATOM   6844  O O   . LYS B  1 326 ? -30.981  -6.384  -77.966  1.00 27.96  ? 326 LYS B O   1 
ATOM   6845  C CB  . LYS B  1 326 ? -30.700  -5.077  -75.004  1.00 27.58  ? 326 LYS B CB  1 
ATOM   6846  C CG  . LYS B  1 326 ? -30.759  -4.005  -73.948  1.00 27.76  ? 326 LYS B CG  1 
ATOM   6847  C CD  . LYS B  1 326 ? -31.228  -4.435  -72.570  1.00 27.79  ? 326 LYS B CD  1 
ATOM   6848  C CE  . LYS B  1 326 ? -30.937  -3.380  -71.539  1.00 28.56  ? 326 LYS B CE  1 
ATOM   6849  N NZ  . LYS B  1 326 ? -31.410  -2.025  -71.810  1.00 27.79  ? 326 LYS B NZ  1 
ATOM   6850  N N   . ASN B  1 327 ? -28.837  -5.827  -77.654  1.00 26.51  ? 327 ASN B N   1 
ATOM   6851  C CA  . ASN B  1 327 ? -28.386  -6.851  -78.578  1.00 27.40  ? 327 ASN B CA  1 
ATOM   6852  C C   . ASN B  1 327 ? -28.726  -8.219  -77.977  1.00 26.14  ? 327 ASN B C   1 
ATOM   6853  O O   . ASN B  1 327 ? -28.696  -8.383  -76.776  1.00 25.04  ? 327 ASN B O   1 
ATOM   6854  C CB  . ASN B  1 327 ? -26.921  -6.613  -78.932  1.00 26.93  ? 327 ASN B CB  1 
ATOM   6855  C CG  . ASN B  1 327 ? -26.396  -7.520  -80.024  1.00 26.15  ? 327 ASN B CG  1 
ATOM   6856  O OD1 . ASN B  1 327 ? -26.913  -7.560  -81.146  1.00 25.53  ? 327 ASN B OD1 1 
ATOM   6857  N ND2 . ASN B  1 327 ? -25.319  -8.227  -79.725  1.00 27.77  ? 327 ASN B ND2 1 
ATOM   6858  N N   . LYS B  1 328 ? -29.106  -9.159  -78.831  1.00 26.83  ? 328 LYS B N   1 
ATOM   6859  C CA  . LYS B  1 328 ? -29.627  -10.466 -78.425  1.00 30.86  ? 328 LYS B CA  1 
ATOM   6860  C C   . LYS B  1 328 ? -30.845  -10.351 -77.501  1.00 31.53  ? 328 LYS B C   1 
ATOM   6861  O O   . LYS B  1 328 ? -31.034  -11.179 -76.635  1.00 33.09  ? 328 LYS B O   1 
ATOM   6862  C CB  . LYS B  1 328 ? -28.552  -11.373 -77.819  1.00 30.08  ? 328 LYS B CB  1 
ATOM   6863  C CG  . LYS B  1 328 ? -27.284  -11.463 -78.683  1.00 31.30  ? 328 LYS B CG  1 
ATOM   6864  C CD  . LYS B  1 328 ? -27.534  -11.705 -80.171  1.00 34.56  ? 328 LYS B CD  1 
ATOM   6865  C CE  . LYS B  1 328 ? -26.315  -11.679 -81.074  1.00 35.51  ? 328 LYS B CE  1 
ATOM   6866  N NZ  . LYS B  1 328 ? -25.433  -12.840 -80.856  1.00 36.02  ? 328 LYS B NZ  1 
ATOM   6867  N N   . SER B  1 329 ? -31.699  -9.354  -77.720  1.00 31.84  ? 329 SER B N   1 
ATOM   6868  C CA  . SER B  1 329 ? -32.919  -9.221  -76.950  1.00 31.77  ? 329 SER B CA  1 
ATOM   6869  C C   . SER B  1 329 ? -34.046  -9.860  -77.727  1.00 31.71  ? 329 SER B C   1 
ATOM   6870  O O   . SER B  1 329 ? -34.020  -9.925  -78.955  1.00 31.40  ? 329 SER B O   1 
ATOM   6871  C CB  . SER B  1 329 ? -33.252  -7.777  -76.609  1.00 32.21  ? 329 SER B CB  1 
ATOM   6872  O OG  . SER B  1 329 ? -33.390  -6.987  -77.773  1.00 29.88  ? 329 SER B OG  1 
ATOM   6873  N N   . ILE B  1 330 ? -35.028  -10.327 -76.970  1.00 33.86  ? 330 ILE B N   1 
ATOM   6874  C CA  . ILE B  1 330 ? -36.142  -11.065 -77.542  1.00 36.89  ? 330 ILE B CA  1 
ATOM   6875  C C   . ILE B  1 330 ? -37.417  -10.268 -77.289  1.00 36.10  ? 330 ILE B C   1 
ATOM   6876  O O   . ILE B  1 330 ? -37.654  -9.800  -76.188  1.00 35.12  ? 330 ILE B O   1 
ATOM   6877  C CB  . ILE B  1 330 ? -36.155  -12.494 -76.967  1.00 38.02  ? 330 ILE B CB  1 
ATOM   6878  C CG1 . ILE B  1 330 ? -34.838  -13.202 -77.333  1.00 39.94  ? 330 ILE B CG1 1 
ATOM   6879  C CG2 . ILE B  1 330 ? -37.365  -13.254 -77.456  1.00 39.47  ? 330 ILE B CG2 1 
ATOM   6880  C CD1 . ILE B  1 330 ? -34.714  -14.651 -76.907  1.00 41.38  ? 330 ILE B CD1 1 
ATOM   6881  N N   . HIS B  1 331 ? -38.187  -10.036 -78.350  1.00 37.68  ? 331 HIS B N   1 
ATOM   6882  C CA  . HIS B  1 331 ? -39.316  -9.126  -78.283  1.00 37.97  ? 331 HIS B CA  1 
ATOM   6883  C C   . HIS B  1 331 ? -40.522  -9.815  -78.884  1.00 38.64  ? 331 HIS B C   1 
ATOM   6884  O O   . HIS B  1 331 ? -40.423  -10.370 -79.977  1.00 39.87  ? 331 HIS B O   1 
ATOM   6885  C CB  . HIS B  1 331 ? -39.017  -7.825  -79.030  1.00 36.41  ? 331 HIS B CB  1 
ATOM   6886  C CG  . HIS B  1 331 ? -37.950  -7.049  -78.351  1.00 36.27  ? 331 HIS B CG  1 
ATOM   6887  N ND1 . HIS B  1 331 ? -38.230  -6.137  -77.357  1.00 36.38  ? 331 HIS B ND1 1 
ATOM   6888  C CD2 . HIS B  1 331 ? -36.609  -7.092  -78.469  1.00 33.84  ? 331 HIS B CD2 1 
ATOM   6889  C CE1 . HIS B  1 331 ? -37.082  -5.615  -76.917  1.00 36.28  ? 331 HIS B CE1 1 
ATOM   6890  N NE2 . HIS B  1 331 ? -36.095  -6.196  -77.566  1.00 34.53  ? 331 HIS B NE2 1 
ATOM   6891  N N   . THR B  1 332 ? -41.640  -9.738  -78.158  1.00 39.83  ? 332 THR B N   1 
ATOM   6892  C CA  . THR B  1 332 ? -42.890  -10.345 -78.587  1.00 41.23  ? 332 THR B CA  1 
ATOM   6893  C C   . THR B  1 332 ? -43.950  -9.251  -78.716  1.00 42.22  ? 332 THR B C   1 
ATOM   6894  O O   . THR B  1 332 ? -45.116  -9.487  -78.475  1.00 48.34  ? 332 THR B O   1 
ATOM   6895  C CB  . THR B  1 332 ? -43.306  -11.458 -77.624  1.00 40.26  ? 332 THR B CB  1 
ATOM   6896  O OG1 . THR B  1 332 ? -43.509  -10.824 -76.372  1.00 41.97  ? 332 THR B OG1 1 
ATOM   6897  C CG2 . THR B  1 332 ? -42.241  -12.514 -77.411  1.00 39.00  ? 332 THR B CG2 1 
ATOM   6898  N N   . ASN B  1 333 ? -43.535  -8.104  -79.234  1.00 44.60  ? 333 ASN B N   1 
ATOM   6899  C CA  . ASN B  1 333 ? -44.372  -6.929  -79.381  1.00 46.06  ? 333 ASN B CA  1 
ATOM   6900  C C   . ASN B  1 333 ? -43.878  -6.148  -80.600  1.00 44.31  ? 333 ASN B C   1 
ATOM   6901  O O   . ASN B  1 333 ? -42.678  -6.188  -80.886  1.00 47.59  ? 333 ASN B O   1 
ATOM   6902  C CB  . ASN B  1 333 ? -44.282  -6.093  -78.111  1.00 48.34  ? 333 ASN B CB  1 
ATOM   6903  C CG  . ASN B  1 333 ? -45.439  -5.144  -78.015  1.00 54.45  ? 333 ASN B CG  1 
ATOM   6904  O OD1 . ASN B  1 333 ? -45.582  -4.246  -78.851  1.00 60.30  ? 333 ASN B OD1 1 
ATOM   6905  N ND2 . ASN B  1 333 ? -46.323  -5.380  -77.061  1.00 60.79  ? 333 ASN B ND2 1 
ATOM   6906  N N   . THR B  1 334 ? -44.772  -5.432  -81.298  1.00 41.85  ? 334 THR B N   1 
ATOM   6907  C CA  . THR B  1 334 ? -44.392  -4.601  -82.436  1.00 40.74  ? 334 THR B CA  1 
ATOM   6908  C C   . THR B  1 334 ? -43.766  -3.279  -81.988  1.00 40.48  ? 334 THR B C   1 
ATOM   6909  O O   . THR B  1 334 ? -43.198  -2.575  -82.815  1.00 36.66  ? 334 THR B O   1 
ATOM   6910  C CB  . THR B  1 334 ? -45.571  -4.310  -83.358  1.00 42.18  ? 334 THR B CB  1 
ATOM   6911  O OG1 . THR B  1 334 ? -46.524  -3.663  -82.523  1.00 42.13  ? 334 THR B OG1 1 
ATOM   6912  C CG2 . THR B  1 334 ? -46.140  -5.561  -83.990  1.00 43.61  ? 334 THR B CG2 1 
ATOM   6913  N N   . LYS B  1 335 ? -43.855  -2.959  -80.689  1.00 43.14  ? 335 LYS B N   1 
ATOM   6914  C CA  . LYS B  1 335 ? -43.363  -1.705  -80.150  1.00 43.84  ? 335 LYS B CA  1 
ATOM   6915  C C   . LYS B  1 335 ? -42.150  -1.963  -79.286  1.00 42.20  ? 335 LYS B C   1 
ATOM   6916  O O   . LYS B  1 335 ? -42.242  -2.682  -78.297  1.00 48.67  ? 335 LYS B O   1 
ATOM   6917  C CB  . LYS B  1 335 ? -44.416  -1.024  -79.271  1.00 47.94  ? 335 LYS B CB  1 
ATOM   6918  C CG  . LYS B  1 335 ? -45.653  -0.531  -80.015  1.00 54.17  ? 335 LYS B CG  1 
ATOM   6919  C CD  . LYS B  1 335 ? -45.400  0.462   -81.154  1.00 58.86  ? 335 LYS B CD  1 
ATOM   6920  C CE  . LYS B  1 335 ? -46.708  1.021   -81.722  1.00 61.03  ? 335 LYS B CE  1 
ATOM   6921  N NZ  . LYS B  1 335 ? -46.506  1.780   -82.963  1.00 59.68  ? 335 LYS B NZ  1 
ATOM   6922  N N   . ILE B  1 336 ? -41.024  -1.381  -79.682  1.00 40.45  ? 336 ILE B N   1 
ATOM   6923  C CA  . ILE B  1 336 ? -39.731  -1.650  -79.059  1.00 39.83  ? 336 ILE B CA  1 
ATOM   6924  C C   . ILE B  1 336 ? -39.289  -0.366  -78.346  1.00 35.94  ? 336 ILE B C   1 
ATOM   6925  O O   . ILE B  1 336 ? -39.075  0.645   -79.003  1.00 34.10  ? 336 ILE B O   1 
ATOM   6926  C CB  . ILE B  1 336 ? -38.701  -2.099  -80.131  1.00 42.09  ? 336 ILE B CB  1 
ATOM   6927  C CG1 . ILE B  1 336 ? -39.227  -3.246  -80.999  1.00 47.83  ? 336 ILE B CG1 1 
ATOM   6928  C CG2 . ILE B  1 336 ? -37.325  -2.449  -79.558  1.00 39.96  ? 336 ILE B CG2 1 
ATOM   6929  C CD1 . ILE B  1 336 ? -39.769  -4.426  -80.213  1.00 50.47  ? 336 ILE B CD1 1 
ATOM   6930  N N   . PRO B  1 337 ? -39.140  -0.339  -76.996  1.00 34.04  ? 337 PRO B N   1 
ATOM   6931  C CA  . PRO B  1 337 ? -38.554  0.820   -76.329  1.00 34.45  ? 337 PRO B CA  1 
ATOM   6932  C C   . PRO B  1 337 ? -37.211  1.185   -76.956  1.00 34.80  ? 337 PRO B C   1 
ATOM   6933  O O   . PRO B  1 337 ? -36.446  0.308   -77.366  1.00 32.45  ? 337 PRO B O   1 
ATOM   6934  C CB  . PRO B  1 337 ? -38.484  0.431   -74.831  1.00 32.77  ? 337 PRO B CB  1 
ATOM   6935  C CG  . PRO B  1 337 ? -39.566  -0.621  -74.699  1.00 33.50  ? 337 PRO B CG  1 
ATOM   6936  C CD  . PRO B  1 337 ? -39.567  -1.366  -76.029  1.00 33.91  ? 337 PRO B CD  1 
ATOM   6937  N N   . LEU B  1 338 ? -37.020  2.500   -77.143  1.00 36.42  ? 338 LEU B N   1 
ATOM   6938  C CA  . LEU B  1 338 ? -35.752  3.049   -77.599  1.00 35.31  ? 338 LEU B CA  1 
ATOM   6939  C C   . LEU B  1 338 ? -35.183  3.946   -76.501  1.00 32.67  ? 338 LEU B C   1 
ATOM   6940  O O   . LEU B  1 338 ? -35.885  4.772   -75.923  1.00 31.63  ? 338 LEU B O   1 
ATOM   6941  C CB  . LEU B  1 338 ? -35.949  3.793   -78.912  1.00 36.84  ? 338 LEU B CB  1 
ATOM   6942  C CG  . LEU B  1 338 ? -34.661  4.356   -79.520  1.00 40.92  ? 338 LEU B CG  1 
ATOM   6943  C CD1 . LEU B  1 338 ? -33.803  3.225   -80.049  1.00 40.17  ? 338 LEU B CD1 1 
ATOM   6944  C CD2 . LEU B  1 338 ? -34.878  5.430   -80.597  1.00 41.57  ? 338 LEU B CD2 1 
ATOM   6945  N N   . GLU B  1 339 ? -33.910  3.709   -76.171  1.00 30.79  ? 339 GLU B N   1 
ATOM   6946  C CA  . GLU B  1 339 ? -33.196  4.514   -75.200  1.00 30.00  ? 339 GLU B CA  1 
ATOM   6947  C C   . GLU B  1 339 ? -31.820  4.805   -75.773  1.00 29.17  ? 339 GLU B C   1 
ATOM   6948  O O   . GLU B  1 339 ? -31.070  3.876   -76.066  1.00 28.37  ? 339 GLU B O   1 
ATOM   6949  C CB  . GLU B  1 339 ? -33.135  3.812   -73.843  1.00 30.54  ? 339 GLU B CB  1 
ATOM   6950  C CG  . GLU B  1 339 ? -34.498  3.733   -73.150  1.00 31.61  ? 339 GLU B CG  1 
ATOM   6951  C CD  . GLU B  1 339 ? -34.430  3.187   -71.740  1.00 31.82  ? 339 GLU B CD  1 
ATOM   6952  O OE1 . GLU B  1 339 ? -34.200  1.976   -71.670  1.00 36.11  ? 339 GLU B OE1 1 
ATOM   6953  O OE2 . GLU B  1 339 ? -34.601  3.909   -70.725  1.00 31.98  ? 339 GLU B OE2 1 
ATOM   6954  N N   . LEU B  1 340 ? -31.510  6.094   -75.947  1.00 30.02  ? 340 LEU B N   1 
ATOM   6955  C CA  . LEU B  1 340 ? -30.191  6.510   -76.417  1.00 30.05  ? 340 LEU B CA  1 
ATOM   6956  C C   . LEU B  1 340 ? -29.528  7.474   -75.434  1.00 29.06  ? 340 LEU B C   1 
ATOM   6957  O O   . LEU B  1 340 ? -30.199  8.166   -74.669  1.00 31.48  ? 340 LEU B O   1 
ATOM   6958  C CB  . LEU B  1 340 ? -30.342  7.157   -77.790  1.00 31.92  ? 340 LEU B CB  1 
ATOM   6959  C CG  . LEU B  1 340 ? -30.878  6.271   -78.922  1.00 32.13  ? 340 LEU B CG  1 
ATOM   6960  C CD1 . LEU B  1 340 ? -31.007  7.109   -80.149  1.00 32.26  ? 340 LEU B CD1 1 
ATOM   6961  C CD2 . LEU B  1 340 ? -30.012  5.086   -79.226  1.00 30.31  ? 340 LEU B CD2 1 
ATOM   6962  N N   . TYR B  1 341 ? -28.198  7.525   -75.456  1.00 28.11  ? 341 TYR B N   1 
ATOM   6963  C CA  . TYR B  1 341 ? -27.487  8.543   -74.706  1.00 28.24  ? 341 TYR B CA  1 
ATOM   6964  C C   . TYR B  1 341 ? -26.444  9.148   -75.634  1.00 28.25  ? 341 TYR B C   1 
ATOM   6965  O O   . TYR B  1 341 ? -25.451  8.520   -75.967  1.00 30.13  ? 341 TYR B O   1 
ATOM   6966  C CB  . TYR B  1 341 ? -26.878  8.020   -73.405  1.00 28.90  ? 341 TYR B CB  1 
ATOM   6967  C CG  . TYR B  1 341 ? -26.351  9.140   -72.505  1.00 29.86  ? 341 TYR B CG  1 
ATOM   6968  C CD1 . TYR B  1 341 ? -25.046  9.619   -72.664  1.00 30.17  ? 341 TYR B CD1 1 
ATOM   6969  C CD2 . TYR B  1 341 ? -27.153  9.753   -71.544  1.00 29.17  ? 341 TYR B CD2 1 
ATOM   6970  C CE1 . TYR B  1 341 ? -24.556  10.642  -71.867  1.00 31.30  ? 341 TYR B CE1 1 
ATOM   6971  C CE2 . TYR B  1 341 ? -26.665  10.774  -70.735  1.00 31.18  ? 341 TYR B CE2 1 
ATOM   6972  C CZ  . TYR B  1 341 ? -25.367  11.233  -70.901  1.00 33.15  ? 341 TYR B CZ  1 
ATOM   6973  O OH  . TYR B  1 341 ? -24.830  12.238  -70.123  1.00 32.37  ? 341 TYR B OH  1 
ATOM   6974  N N   . ASN B  1 342 ? -26.718  10.368  -76.069  1.00 28.94  ? 342 ASN B N   1 
ATOM   6975  C CA  . ASN B  1 342 ? -26.018  10.987  -77.172  1.00 29.99  ? 342 ASN B CA  1 
ATOM   6976  C C   . ASN B  1 342 ? -25.071  12.045  -76.621  1.00 31.87  ? 342 ASN B C   1 
ATOM   6977  O O   . ASN B  1 342 ? -25.432  12.769  -75.690  1.00 33.15  ? 342 ASN B O   1 
ATOM   6978  C CB  . ASN B  1 342 ? -27.003  11.609  -78.165  1.00 29.32  ? 342 ASN B CB  1 
ATOM   6979  C CG  . ASN B  1 342 ? -27.833  10.569  -78.888  1.00 29.47  ? 342 ASN B CG  1 
ATOM   6980  O OD1 . ASN B  1 342 ? -27.291  9.612   -79.464  1.00 27.36  ? 342 ASN B OD1 1 
ATOM   6981  N ND2 . ASN B  1 342 ? -29.150  10.755  -78.892  1.00 30.73  ? 342 ASN B ND2 1 
ATOM   6982  N N   . ASP B  1 343 ? -23.907  12.188  -77.269  1.00 33.09  ? 343 ASP B N   1 
ATOM   6983  C CA  . ASP B  1 343 ? -23.013  13.296  -76.972  1.00 35.00  ? 343 ASP B CA  1 
ATOM   6984  C C   . ASP B  1 343 ? -23.475  14.496  -77.788  1.00 37.39  ? 343 ASP B C   1 
ATOM   6985  O O   . ASP B  1 343 ? -24.416  14.362  -78.569  1.00 38.61  ? 343 ASP B O   1 
ATOM   6986  C CB  . ASP B  1 343 ? -21.559  12.862  -77.107  1.00 36.63  ? 343 ASP B CB  1 
ATOM   6987  C CG  . ASP B  1 343 ? -20.880  12.947  -78.468  1.00 36.99  ? 343 ASP B CG  1 
ATOM   6988  O OD1 . ASP B  1 343 ? -21.516  13.472  -79.429  1.00 35.87  ? 343 ASP B OD1 1 
ATOM   6989  O OD2 . ASP B  1 343 ? -19.677  12.532  -78.526  1.00 35.79  ? 343 ASP B OD2 1 
ATOM   6990  N N   . LYS B  1 344 ? -22.818  15.657  -77.637  1.00 40.15  ? 344 LYS B N   1 
ATOM   6991  C CA  . LYS B  1 344 ? -23.359  16.894  -78.200  1.00 43.39  ? 344 LYS B CA  1 
ATOM   6992  C C   . LYS B  1 344 ? -23.159  16.974  -79.715  1.00 38.02  ? 344 LYS B C   1 
ATOM   6993  O O   . LYS B  1 344 ? -23.796  17.771  -80.380  1.00 35.79  ? 344 LYS B O   1 
ATOM   6994  C CB  . LYS B  1 344 ? -22.791  18.144  -77.510  1.00 52.41  ? 344 LYS B CB  1 
ATOM   6995  C CG  . LYS B  1 344 ? -21.294  18.349  -77.650  1.00 61.96  ? 344 LYS B CG  1 
ATOM   6996  C CD  . LYS B  1 344 ? -20.760  19.631  -76.999  1.00 75.54  ? 344 LYS B CD  1 
ATOM   6997  C CE  . LYS B  1 344 ? -19.302  19.880  -77.299  1.00 78.31  ? 344 LYS B CE  1 
ATOM   6998  N NZ  . LYS B  1 344 ? -18.455  18.688  -77.130  1.00 75.36  ? 344 LYS B NZ  1 
ATOM   6999  N N   . ASP B  1 345 ? -22.327  16.109  -80.286  1.00 35.47  ? 345 ASP B N   1 
ATOM   7000  C CA  . ASP B  1 345 ? -22.131  16.113  -81.721  1.00 33.77  ? 345 ASP B CA  1 
ATOM   7001  C C   . ASP B  1 345 ? -23.224  15.383  -82.487  1.00 32.66  ? 345 ASP B C   1 
ATOM   7002  O O   . ASP B  1 345 ? -23.303  15.553  -83.691  1.00 33.91  ? 345 ASP B O   1 
ATOM   7003  C CB  . ASP B  1 345 ? -20.811  15.459  -82.078  1.00 34.99  ? 345 ASP B CB  1 
ATOM   7004  C CG  . ASP B  1 345 ? -19.590  16.277  -81.683  1.00 35.28  ? 345 ASP B CG  1 
ATOM   7005  O OD1 . ASP B  1 345 ? -19.737  17.520  -81.504  1.00 33.07  ? 345 ASP B OD1 1 
ATOM   7006  O OD2 . ASP B  1 345 ? -18.527  15.650  -81.562  1.00 34.69  ? 345 ASP B OD2 1 
ATOM   7007  N N   . VAL B  1 346 ? -24.008  14.514  -81.851  1.00 31.85  ? 346 VAL B N   1 
ATOM   7008  C CA  . VAL B  1 346 ? -25.067  13.794  -82.553  1.00 30.93  ? 346 VAL B CA  1 
ATOM   7009  C C   . VAL B  1 346 ? -26.282  14.695  -82.755  1.00 30.63  ? 346 VAL B C   1 
ATOM   7010  O O   . VAL B  1 346 ? -26.853  15.151  -81.770  1.00 29.91  ? 346 VAL B O   1 
ATOM   7011  C CB  . VAL B  1 346 ? -25.510  12.572  -81.738  1.00 30.39  ? 346 VAL B CB  1 
ATOM   7012  C CG1 . VAL B  1 346 ? -26.693  11.866  -82.379  1.00 31.83  ? 346 VAL B CG1 1 
ATOM   7013  C CG2 . VAL B  1 346 ? -24.378  11.586  -81.515  1.00 32.24  ? 346 VAL B CG2 1 
ATOM   7014  N N   . LYS B  1 347 ? -26.723  14.828  -84.012  1.00 31.97  ? 347 LYS B N   1 
ATOM   7015  C CA  . LYS B  1 347 ? -27.883  15.634  -84.394  1.00 35.91  ? 347 LYS B CA  1 
ATOM   7016  C C   . LYS B  1 347 ? -28.985  14.840  -85.109  1.00 36.38  ? 347 LYS B C   1 
ATOM   7017  O O   . LYS B  1 347 ? -30.070  15.383  -85.347  1.00 35.43  ? 347 LYS B O   1 
ATOM   7018  C CB  . LYS B  1 347 ? -27.475  16.741  -85.375  1.00 38.93  ? 347 LYS B CB  1 
ATOM   7019  C CG  . LYS B  1 347 ? -26.384  17.643  -84.849  1.00 40.82  ? 347 LYS B CG  1 
ATOM   7020  C CD  . LYS B  1 347 ? -26.752  18.344  -83.545  1.00 44.56  ? 347 LYS B CD  1 
ATOM   7021  C CE  . LYS B  1 347 ? -25.546  19.099  -83.063  1.00 49.68  ? 347 LYS B CE  1 
ATOM   7022  N NZ  . LYS B  1 347 ? -25.845  19.909  -81.884  1.00 54.49  ? 347 LYS B NZ  1 
ATOM   7023  N N   . LYS B  1 348 ? -28.708  13.567  -85.438  1.00 34.39  ? 348 LYS B N   1 
ATOM   7024  C CA  . LYS B  1 348 ? -29.707  12.714  -86.043  1.00 34.78  ? 348 LYS B CA  1 
ATOM   7025  C C   . LYS B  1 348 ? -29.365  11.248  -85.758  1.00 33.52  ? 348 LYS B C   1 
ATOM   7026  O O   . LYS B  1 348 ? -28.207  10.817  -85.751  1.00 29.71  ? 348 LYS B O   1 
ATOM   7027  C CB  . LYS B  1 348 ? -29.855  13.023  -87.538  1.00 36.21  ? 348 LYS B CB  1 
ATOM   7028  C CG  . LYS B  1 348 ? -31.041  12.317  -88.213  1.00 39.04  ? 348 LYS B CG  1 
ATOM   7029  C CD  . LYS B  1 348 ? -31.369  12.724  -89.646  1.00 40.02  ? 348 LYS B CD  1 
ATOM   7030  C CE  . LYS B  1 348 ? -30.195  12.471  -90.531  1.00 41.55  ? 348 LYS B CE  1 
ATOM   7031  N NZ  . LYS B  1 348 ? -30.502  12.563  -91.967  1.00 43.56  ? 348 LYS B NZ  1 
ATOM   7032  N N   . VAL B  1 349 ? -30.419  10.479  -85.502  1.00 33.17  ? 349 VAL B N   1 
ATOM   7033  C CA  . VAL B  1 349 ? -30.299  9.042   -85.397  1.00 32.13  ? 349 VAL B CA  1 
ATOM   7034  C C   . VAL B  1 349 ? -31.291  8.420   -86.363  1.00 33.95  ? 349 VAL B C   1 
ATOM   7035  O O   . VAL B  1 349 ? -32.477  8.804   -86.381  1.00 31.76  ? 349 VAL B O   1 
ATOM   7036  C CB  . VAL B  1 349 ? -30.543  8.604   -83.958  1.00 31.74  ? 349 VAL B CB  1 
ATOM   7037  C CG1 . VAL B  1 349 ? -30.481  7.089   -83.833  1.00 31.23  ? 349 VAL B CG1 1 
ATOM   7038  C CG2 . VAL B  1 349 ? -29.500  9.258   -83.061  1.00 32.36  ? 349 VAL B CG2 1 
ATOM   7039  N N   . VAL B  1 350 ? -30.770  7.479   -87.168  1.00 33.31  ? 350 VAL B N   1 
ATOM   7040  C CA  . VAL B  1 350 ? -31.600  6.698   -88.080  1.00 32.78  ? 350 VAL B CA  1 
ATOM   7041  C C   . VAL B  1 350 ? -31.468  5.217   -87.709  1.00 32.15  ? 350 VAL B C   1 
ATOM   7042  O O   . VAL B  1 350 ? -30.373  4.762   -87.333  1.00 29.76  ? 350 VAL B O   1 
ATOM   7043  C CB  . VAL B  1 350 ? -31.159  7.004   -89.521  1.00 32.26  ? 350 VAL B CB  1 
ATOM   7044  C CG1 . VAL B  1 350 ? -31.898  6.158   -90.543  1.00 32.35  ? 350 VAL B CG1 1 
ATOM   7045  C CG2 . VAL B  1 350 ? -31.318  8.496   -89.851  1.00 33.45  ? 350 VAL B CG2 1 
ATOM   7046  N N   . VAL B  1 351 ? -32.600  4.484   -87.795  1.00 31.90  ? 351 VAL B N   1 
ATOM   7047  C CA  . VAL B  1 351 ? -32.590  3.036   -87.695  1.00 31.07  ? 351 VAL B CA  1 
ATOM   7048  C C   . VAL B  1 351 ? -33.117  2.431   -88.993  1.00 32.67  ? 351 VAL B C   1 
ATOM   7049  O O   . VAL B  1 351 ? -34.237  2.721   -89.399  1.00 36.59  ? 351 VAL B O   1 
ATOM   7050  C CB  . VAL B  1 351 ? -33.360  2.489   -86.483  1.00 31.07  ? 351 VAL B CB  1 
ATOM   7051  C CG1 . VAL B  1 351 ? -33.139  0.994   -86.282  1.00 30.96  ? 351 VAL B CG1 1 
ATOM   7052  C CG2 . VAL B  1 351 ? -32.988  3.196   -85.199  1.00 31.19  ? 351 VAL B CG2 1 
ATOM   7053  N N   . LYS B  1 352 ? -32.334  1.506   -89.584  1.00 32.31  ? 352 LYS B N   1 
ATOM   7054  C CA  . LYS B  1 352 ? -32.749  0.793   -90.777  1.00 31.65  ? 352 LYS B CA  1 
ATOM   7055  C C   . LYS B  1 352 ? -32.878  -0.713  -90.540  1.00 29.52  ? 352 LYS B C   1 
ATOM   7056  O O   . LYS B  1 352 ? -32.234  -1.316  -89.702  1.00 28.40  ? 352 LYS B O   1 
ATOM   7057  C CB  . LYS B  1 352 ? -31.717  1.015   -91.873  1.00 33.42  ? 352 LYS B CB  1 
ATOM   7058  C CG  . LYS B  1 352 ? -31.891  2.298   -92.593  1.00 36.72  ? 352 LYS B CG  1 
ATOM   7059  C CD  . LYS B  1 352 ? -30.632  2.733   -93.320  1.00 40.21  ? 352 LYS B CD  1 
ATOM   7060  C CE  . LYS B  1 352 ? -30.956  4.013   -94.029  1.00 42.70  ? 352 LYS B CE  1 
ATOM   7061  N NZ  . LYS B  1 352 ? -29.708  4.704   -94.362  1.00 43.53  ? 352 LYS B NZ  1 
ATOM   7062  N N   . PHE B  1 353 ? -33.710  -1.317  -91.357  1.00 29.22  ? 353 PHE B N   1 
ATOM   7063  C CA  . PHE B  1 353 ? -33.849  -2.752  -91.412  1.00 29.95  ? 353 PHE B CA  1 
ATOM   7064  C C   . PHE B  1 353 ? -33.966  -3.069  -92.892  1.00 30.13  ? 353 PHE B C   1 
ATOM   7065  O O   . PHE B  1 353 ? -34.869  -2.529  -93.539  1.00 30.19  ? 353 PHE B O   1 
ATOM   7066  C CB  . PHE B  1 353 ? -35.051  -3.302  -90.616  1.00 30.00  ? 353 PHE B CB  1 
ATOM   7067  C CG  . PHE B  1 353 ? -35.146  -4.812  -90.693  1.00 29.71  ? 353 PHE B CG  1 
ATOM   7068  C CD1 . PHE B  1 353 ? -34.093  -5.617  -90.259  1.00 29.50  ? 353 PHE B CD1 1 
ATOM   7069  C CD2 . PHE B  1 353 ? -36.255  -5.420  -91.262  1.00 30.67  ? 353 PHE B CD2 1 
ATOM   7070  C CE1 . PHE B  1 353 ? -34.166  -7.004  -90.368  1.00 29.26  ? 353 PHE B CE1 1 
ATOM   7071  C CE2 . PHE B  1 353 ? -36.320  -6.800  -91.374  1.00 30.93  ? 353 PHE B CE2 1 
ATOM   7072  C CZ  . PHE B  1 353 ? -35.265  -7.587  -90.953  1.00 30.08  ? 353 PHE B CZ  1 
ATOM   7073  N N   . ARG B  1 354 ? -33.023  -3.883  -93.400  1.00 29.13  ? 354 ARG B N   1 
ATOM   7074  C CA  . ARG B  1 354 ? -32.979  -4.240  -94.813  1.00 30.56  ? 354 ARG B CA  1 
ATOM   7075  C C   . ARG B  1 354 ? -32.951  -2.980  -95.674  1.00 31.30  ? 354 ARG B C   1 
ATOM   7076  O O   . ARG B  1 354 ? -33.611  -2.906  -96.706  1.00 31.80  ? 354 ARG B O   1 
ATOM   7077  C CB  . ARG B  1 354 ? -34.124  -5.181  -95.217  1.00 32.11  ? 354 ARG B CB  1 
ATOM   7078  C CG  . ARG B  1 354 ? -34.002  -6.552  -94.569  1.00 32.10  ? 354 ARG B CG  1 
ATOM   7079  C CD  . ARG B  1 354 ? -35.134  -7.448  -94.999  1.00 33.22  ? 354 ARG B CD  1 
ATOM   7080  N NE  . ARG B  1 354 ? -35.071  -8.665  -94.168  1.00 32.91  ? 354 ARG B NE  1 
ATOM   7081  C CZ  . ARG B  1 354 ? -36.115  -9.446  -94.007  1.00 31.81  ? 354 ARG B CZ  1 
ATOM   7082  N NH1 . ARG B  1 354 ? -37.185  -9.263  -94.758  1.00 33.22  ? 354 ARG B NH1 1 
ATOM   7083  N NH2 . ARG B  1 354 ? -36.090  -10.390 -93.119  1.00 30.77  ? 354 ARG B NH2 1 
ATOM   7084  N N   . ASP B  1 355 ? -32.158  -1.997  -95.239  1.00 31.87  ? 355 ASP B N   1 
ATOM   7085  C CA  . ASP B  1 355 ? -31.882  -0.814  -96.036  1.00 33.74  ? 355 ASP B CA  1 
ATOM   7086  C C   . ASP B  1 355 ? -33.113  0.094   -96.117  1.00 33.75  ? 355 ASP B C   1 
ATOM   7087  O O   . ASP B  1 355 ? -33.115  1.045   -96.891  1.00 33.39  ? 355 ASP B O   1 
ATOM   7088  C CB  . ASP B  1 355 ? -31.313  -1.205  -97.389  1.00 34.07  ? 355 ASP B CB  1 
ATOM   7089  C CG  . ASP B  1 355 ? -30.230  -2.267  -97.326  1.00 33.67  ? 355 ASP B CG  1 
ATOM   7090  O OD1 . ASP B  1 355 ? -29.139  -1.936  -96.862  1.00 32.16  ? 355 ASP B OD1 1 
ATOM   7091  O OD2 . ASP B  1 355 ? -30.524  -3.434  -97.690  1.00 35.05  ? 355 ASP B OD2 1 
ATOM   7092  N N   . LYS B  1 356 ? -34.118  -0.159  -95.271  1.00 34.24  ? 356 LYS B N   1 
ATOM   7093  C CA  . LYS B  1 356 ? -35.292  0.704   -95.192  1.00 36.47  ? 356 LYS B CA  1 
ATOM   7094  C C   . LYS B  1 356 ? -35.306  1.437   -93.845  1.00 34.12  ? 356 LYS B C   1 
ATOM   7095  O O   . LYS B  1 356 ? -35.079  0.831   -92.803  1.00 32.25  ? 356 LYS B O   1 
ATOM   7096  C CB  . LYS B  1 356 ? -36.606  -0.060  -95.421  1.00 39.12  ? 356 LYS B CB  1 
ATOM   7097  C CG  . LYS B  1 356 ? -37.866  0.756   -95.377  1.00 41.01  ? 356 LYS B CG  1 
ATOM   7098  C CD  . LYS B  1 356 ? -39.139  -0.081  -95.372  1.00 46.80  ? 356 LYS B CD  1 
ATOM   7099  C CE  . LYS B  1 356 ? -39.351  -0.795  -96.670  1.00 51.16  ? 356 LYS B CE  1 
ATOM   7100  N NZ  . LYS B  1 356 ? -40.732  -1.282  -96.837  1.00 56.07  ? 356 LYS B NZ  1 
ATOM   7101  N N   . VAL B  1 357 ? -35.628  2.744   -93.887  1.00 33.34  ? 357 VAL B N   1 
ATOM   7102  C CA  . VAL B  1 357 ? -35.759  3.543   -92.682  1.00 32.13  ? 357 VAL B CA  1 
ATOM   7103  C C   . VAL B  1 357 ? -37.047  3.127   -91.975  1.00 31.74  ? 357 VAL B C   1 
ATOM   7104  O O   . VAL B  1 357 ? -38.116  3.163   -92.566  1.00 30.47  ? 357 VAL B O   1 
ATOM   7105  C CB  . VAL B  1 357 ? -35.753  5.052   -93.033  1.00 32.40  ? 357 VAL B CB  1 
ATOM   7106  C CG1 . VAL B  1 357 ? -36.217  5.935   -91.880  1.00 32.19  ? 357 VAL B CG1 1 
ATOM   7107  C CG2 . VAL B  1 357 ? -34.409  5.509   -93.570  1.00 31.52  ? 357 VAL B CG2 1 
ATOM   7108  N N   . ILE B  1 358 ? -36.906  2.751   -90.696  1.00 32.71  ? 358 ILE B N   1 
ATOM   7109  C CA  . ILE B  1 358 ? -38.039  2.474   -89.821  1.00 34.26  ? 358 ILE B CA  1 
ATOM   7110  C C   . ILE B  1 358 ? -38.072  3.476   -88.673  1.00 33.85  ? 358 ILE B C   1 
ATOM   7111  O O   . ILE B  1 358 ? -39.085  3.555   -87.992  1.00 34.73  ? 358 ILE B O   1 
ATOM   7112  C CB  . ILE B  1 358 ? -37.997  1.023   -89.290  1.00 33.88  ? 358 ILE B CB  1 
ATOM   7113  C CG1 . ILE B  1 358 ? -36.829  0.791   -88.353  1.00 34.75  ? 358 ILE B CG1 1 
ATOM   7114  C CG2 . ILE B  1 358 ? -37.990  0.041   -90.459  1.00 33.86  ? 358 ILE B CG2 1 
ATOM   7115  C CD1 . ILE B  1 358 ? -36.909  -0.511  -87.565  1.00 36.08  ? 358 ILE B CD1 1 
ATOM   7116  N N   . TYR B  1 359 ? -36.969  4.208   -88.457  1.00 33.77  ? 359 TYR B N   1 
ATOM   7117  C CA  . TYR B  1 359 ? -36.970  5.269   -87.471  1.00 35.85  ? 359 TYR B CA  1 
ATOM   7118  C C   . TYR B  1 359 ? -35.969  6.367   -87.858  1.00 37.32  ? 359 TYR B C   1 
ATOM   7119  O O   . TYR B  1 359 ? -34.863  6.088   -88.321  1.00 34.44  ? 359 TYR B O   1 
ATOM   7120  C CB  . TYR B  1 359 ? -36.671  4.689   -86.085  1.00 35.85  ? 359 TYR B CB  1 
ATOM   7121  C CG  . TYR B  1 359 ? -36.591  5.733   -84.973  1.00 35.46  ? 359 TYR B CG  1 
ATOM   7122  C CD1 . TYR B  1 359 ? -35.388  6.407   -84.678  1.00 32.68  ? 359 TYR B CD1 1 
ATOM   7123  C CD2 . TYR B  1 359 ? -37.733  6.068   -84.235  1.00 33.93  ? 359 TYR B CD2 1 
ATOM   7124  C CE1 . TYR B  1 359 ? -35.332  7.357   -83.669  1.00 32.12  ? 359 TYR B CE1 1 
ATOM   7125  C CE2 . TYR B  1 359 ? -37.686  7.027   -83.237  1.00 32.78  ? 359 TYR B CE2 1 
ATOM   7126  C CZ  . TYR B  1 359 ? -36.485  7.669   -82.959  1.00 33.47  ? 359 TYR B CZ  1 
ATOM   7127  O OH  . TYR B  1 359 ? -36.445  8.592   -81.960  1.00 34.77  ? 359 TYR B OH  1 
ATOM   7128  N N   . SER B  1 360 ? -36.397  7.628   -87.645  1.00 38.11  ? 360 SER B N   1 
ATOM   7129  C CA  . SER B  1 360 ? -35.629  8.813   -87.995  1.00 37.76  ? 360 SER B CA  1 
ATOM   7130  C C   . SER B  1 360 ? -36.003  9.988   -87.080  1.00 38.45  ? 360 SER B C   1 
ATOM   7131  O O   . SER B  1 360 ? -37.148  10.437  -87.085  1.00 42.87  ? 360 SER B O   1 
ATOM   7132  C CB  . SER B  1 360 ? -35.839  9.139   -89.427  1.00 37.62  ? 360 SER B CB  1 
ATOM   7133  O OG  . SER B  1 360 ? -34.931  10.162  -89.787  1.00 40.60  ? 360 SER B OG  1 
ATOM   7134  N N   . LYS B  1 361 ? -35.049  10.459  -86.268  1.00 37.99  ? 361 LYS B N   1 
ATOM   7135  C CA  . LYS B  1 361 ? -35.262  11.553  -85.321  1.00 41.33  ? 361 LYS B CA  1 
ATOM   7136  C C   . LYS B  1 361 ? -34.085  12.531  -85.371  1.00 37.49  ? 361 LYS B C   1 
ATOM   7137  O O   . LYS B  1 361 ? -32.939  12.104  -85.337  1.00 34.11  ? 361 LYS B O   1 
ATOM   7138  C CB  . LYS B  1 361 ? -35.434  11.013  -83.894  1.00 44.07  ? 361 LYS B CB  1 
ATOM   7139  C CG  . LYS B  1 361 ? -35.686  12.010  -82.755  1.00 45.98  ? 361 LYS B CG  1 
ATOM   7140  C CD  . LYS B  1 361 ? -37.029  12.728  -82.793  1.00 51.55  ? 361 LYS B CD  1 
ATOM   7141  C CE  . LYS B  1 361 ? -37.208  13.943  -81.885  1.00 53.18  ? 361 LYS B CE  1 
ATOM   7142  N NZ  . LYS B  1 361 ? -37.065  13.507  -80.498  1.00 53.37  ? 361 LYS B NZ  1 
ATOM   7143  N N   . ASN B  1 362 ? -34.390  13.834  -85.514  1.00 38.41  ? 362 ASN B N   1 
ATOM   7144  C CA  . ASN B  1 362 ? -33.443  14.915  -85.257  1.00 37.52  ? 362 ASN B CA  1 
ATOM   7145  C C   . ASN B  1 362 ? -33.255  15.092  -83.751  1.00 37.69  ? 362 ASN B C   1 
ATOM   7146  O O   . ASN B  1 362 ? -34.244  15.183  -83.033  1.00 37.58  ? 362 ASN B O   1 
ATOM   7147  C CB  . ASN B  1 362 ? -33.937  16.230  -85.827  1.00 37.55  ? 362 ASN B CB  1 
ATOM   7148  C CG  . ASN B  1 362 ? -33.956  16.225  -87.335  1.00 39.13  ? 362 ASN B CG  1 
ATOM   7149  O OD1 . ASN B  1 362 ? -33.240  15.467  -87.988  1.00 41.04  ? 362 ASN B OD1 1 
ATOM   7150  N ND2 . ASN B  1 362 ? -34.773  17.065  -87.930  1.00 42.94  ? 362 ASN B ND2 1 
ATOM   7151  N N   . ILE B  1 363 ? -31.990  15.101  -83.282  1.00 37.22  ? 363 ILE B N   1 
ATOM   7152  C CA  . ILE B  1 363 ? -31.674  15.329  -81.872  1.00 37.63  ? 363 ILE B CA  1 
ATOM   7153  C C   . ILE B  1 363 ? -31.385  16.818  -81.624  1.00 41.52  ? 363 ILE B C   1 
ATOM   7154  O O   . ILE B  1 363 ? -30.429  17.360  -82.182  1.00 43.06  ? 363 ILE B O   1 
ATOM   7155  C CB  . ILE B  1 363 ? -30.468  14.474  -81.452  1.00 36.39  ? 363 ILE B CB  1 
ATOM   7156  C CG1 . ILE B  1 363 ? -30.554  13.018  -81.982  1.00 35.03  ? 363 ILE B CG1 1 
ATOM   7157  C CG2 . ILE B  1 363 ? -30.248  14.539  -79.934  1.00 35.84  ? 363 ILE B CG2 1 
ATOM   7158  C CD1 . ILE B  1 363 ? -31.769  12.256  -81.510  1.00 35.28  ? 363 ILE B CD1 1 
ATOM   7159  N N   . THR B  1 364 ? -32.193  17.458  -80.761  1.00 46.34  ? 364 THR B N   1 
ATOM   7160  C CA  . THR B  1 364 ? -32.049  18.870  -80.399  1.00 52.40  ? 364 THR B CA  1 
ATOM   7161  C C   . THR B  1 364 ? -31.432  19.043  -79.001  1.00 52.08  ? 364 THR B C   1 
ATOM   7162  O O   . THR B  1 364 ? -31.118  20.146  -78.582  1.00 55.41  ? 364 THR B O   1 
ATOM   7163  C CB  . THR B  1 364 ? -33.408  19.583  -80.482  1.00 54.64  ? 364 THR B CB  1 
ATOM   7164  O OG1 . THR B  1 364 ? -34.329  18.896  -79.639  1.00 54.43  ? 364 THR B OG1 1 
ATOM   7165  C CG2 . THR B  1 364 ? -33.962  19.609  -81.897  1.00 56.52  ? 364 THR B CG2 1 
ATOM   7166  N N   . SER B  1 365 ? -31.255  17.945  -78.275  1.00 54.10  ? 365 SER B N   1 
ATOM   7167  C CA  . SER B  1 365 ? -30.891  17.962  -76.873  1.00 47.51  ? 365 SER B CA  1 
ATOM   7168  C C   . SER B  1 365 ? -29.968  16.778  -76.656  1.00 42.41  ? 365 SER B C   1 
ATOM   7169  O O   . SER B  1 365 ? -30.307  15.676  -77.050  1.00 39.46  ? 365 SER B O   1 
ATOM   7170  C CB  . SER B  1 365 ? -32.140  17.852  -76.055  1.00 48.83  ? 365 SER B CB  1 
ATOM   7171  O OG  . SER B  1 365 ? -31.873  17.969  -74.679  1.00 51.17  ? 365 SER B OG  1 
ATOM   7172  N N   . GLU B  1 366 ? -28.786  17.016  -76.108  1.00 39.59  ? 366 GLU B N   1 
ATOM   7173  C CA  . GLU B  1 366 ? -27.853  15.928  -75.888  1.00 38.20  ? 366 GLU B CA  1 
ATOM   7174  C C   . GLU B  1 366 ? -28.279  15.108  -74.674  1.00 34.65  ? 366 GLU B C   1 
ATOM   7175  O O   . GLU B  1 366 ? -29.182  15.520  -73.954  1.00 34.67  ? 366 GLU B O   1 
ATOM   7176  C CB  . GLU B  1 366 ? -26.461  16.493  -75.639  1.00 40.26  ? 366 GLU B CB  1 
ATOM   7177  C CG  . GLU B  1 366 ? -26.393  17.268  -74.333  1.00 44.61  ? 366 GLU B CG  1 
ATOM   7178  C CD  . GLU B  1 366 ? -25.024  17.858  -74.075  1.00 50.06  ? 366 GLU B CD  1 
ATOM   7179  O OE1 . GLU B  1 366 ? -24.059  17.066  -73.907  1.00 46.91  ? 366 GLU B OE1 1 
ATOM   7180  O OE2 . GLU B  1 366 ? -24.967  19.120  -74.034  1.00 51.92  ? 366 GLU B OE2 1 
ATOM   7181  N N   . GLY B  1 367 ? -27.598  13.969  -74.451  1.00 31.00  ? 367 GLY B N   1 
ATOM   7182  C CA  . GLY B  1 367 ? -27.843  13.101  -73.300  1.00 30.50  ? 367 GLY B CA  1 
ATOM   7183  C C   . GLY B  1 367 ? -28.980  12.100  -73.537  1.00 30.33  ? 367 GLY B C   1 
ATOM   7184  O O   . GLY B  1 367 ? -29.180  11.624  -74.648  1.00 30.22  ? 367 GLY B O   1 
ATOM   7185  N N   . TYR B  1 368 ? -29.753  11.818  -72.493  1.00 29.88  ? 368 TYR B N   1 
ATOM   7186  C CA  . TYR B  1 368 ? -30.745  10.762  -72.540  1.00 31.28  ? 368 TYR B CA  1 
ATOM   7187  C C   . TYR B  1 368 ? -31.877  11.162  -73.482  1.00 32.67  ? 368 TYR B C   1 
ATOM   7188  O O   . TYR B  1 368 ? -32.363  12.281  -73.407  1.00 31.01  ? 368 TYR B O   1 
ATOM   7189  C CB  . TYR B  1 368 ? -31.322  10.471  -71.143  1.00 31.84  ? 368 TYR B CB  1 
ATOM   7190  C CG  . TYR B  1 368 ? -32.335  9.323   -71.090  1.00 31.51  ? 368 TYR B CG  1 
ATOM   7191  C CD1 . TYR B  1 368 ? -31.914  7.999   -71.060  1.00 30.24  ? 368 TYR B CD1 1 
ATOM   7192  C CD2 . TYR B  1 368 ? -33.712  9.574   -71.102  1.00 30.88  ? 368 TYR B CD2 1 
ATOM   7193  C CE1 . TYR B  1 368 ? -32.838  6.964   -71.032  1.00 31.84  ? 368 TYR B CE1 1 
ATOM   7194  C CE2 . TYR B  1 368 ? -34.642  8.553   -71.079  1.00 30.71  ? 368 TYR B CE2 1 
ATOM   7195  C CZ  . TYR B  1 368 ? -34.197  7.247   -71.038  1.00 32.02  ? 368 TYR B CZ  1 
ATOM   7196  O OH  . TYR B  1 368 ? -35.084  6.231   -71.058  1.00 31.44  ? 368 TYR B OH  1 
ATOM   7197  N N   . MET B  1 369 ? -32.328  10.220  -74.329  1.00 34.53  ? 369 MET B N   1 
ATOM   7198  C CA  . MET B  1 369 ? -33.670  10.320  -74.884  1.00 36.79  ? 369 MET B CA  1 
ATOM   7199  C C   . MET B  1 369 ? -34.306  8.936   -74.922  1.00 35.89  ? 369 MET B C   1 
ATOM   7200  O O   . MET B  1 369 ? -33.599  7.922   -74.998  1.00 34.72  ? 369 MET B O   1 
ATOM   7201  C CB  . MET B  1 369 ? -33.682  10.940  -76.280  1.00 39.01  ? 369 MET B CB  1 
ATOM   7202  C CG  . MET B  1 369 ? -32.734  10.247  -77.225  1.00 43.29  ? 369 MET B CG  1 
ATOM   7203  S SD  . MET B  1 369 ? -33.395  9.963   -78.874  1.00 53.04  ? 369 MET B SD  1 
ATOM   7204  C CE  . MET B  1 369 ? -35.159  9.665   -78.676  1.00 43.00  ? 369 MET B CE  1 
ATOM   7205  N N   . ALA B  1 370 ? -35.651  8.937   -74.874  1.00 34.84  ? 370 ALA B N   1 
ATOM   7206  C CA  . ALA B  1 370 ? -36.461  7.727   -74.961  1.00 34.17  ? 370 ALA B CA  1 
ATOM   7207  C C   . ALA B  1 370 ? -37.508  7.896   -76.053  1.00 35.35  ? 370 ALA B C   1 
ATOM   7208  O O   . ALA B  1 370 ? -37.949  8.999   -76.350  1.00 36.79  ? 370 ALA B O   1 
ATOM   7209  C CB  . ALA B  1 370 ? -37.114  7.409   -73.636  1.00 32.63  ? 370 ALA B CB  1 
ATOM   7210  N N   . ASP B  1 371 ? -37.884  6.785   -76.678  1.00 36.08  ? 371 ASP B N   1 
ATOM   7211  C CA  . ASP B  1 371 ? -38.832  6.814   -77.776  1.00 36.47  ? 371 ASP B CA  1 
ATOM   7212  C C   . ASP B  1 371 ? -39.215  5.364   -78.012  1.00 35.13  ? 371 ASP B C   1 
ATOM   7213  O O   . ASP B  1 371 ? -38.930  4.541   -77.149  1.00 34.71  ? 371 ASP B O   1 
ATOM   7214  C CB  . ASP B  1 371 ? -38.206  7.528   -78.970  1.00 37.51  ? 371 ASP B CB  1 
ATOM   7215  C CG  . ASP B  1 371 ? -39.196  8.057   -79.994  1.00 36.87  ? 371 ASP B CG  1 
ATOM   7216  O OD1 . ASP B  1 371 ? -40.365  7.725   -79.827  1.00 37.25  ? 371 ASP B OD1 1 
ATOM   7217  O OD2 . ASP B  1 371 ? -38.776  8.803   -80.906  1.00 35.93  ? 371 ASP B OD2 1 
ATOM   7218  N N   . GLU B  1 372 ? -39.811  5.047   -79.165  1.00 37.86  ? 372 GLU B N   1 
ATOM   7219  C CA  . GLU B  1 372 ? -40.058  3.646   -79.496  1.00 40.77  ? 372 GLU B CA  1 
ATOM   7220  C C   . GLU B  1 372 ? -40.021  3.393   -81.009  1.00 40.26  ? 372 GLU B C   1 
ATOM   7221  O O   . GLU B  1 372 ? -40.495  4.207   -81.792  1.00 42.82  ? 372 GLU B O   1 
ATOM   7222  C CB  . GLU B  1 372 ? -41.338  3.130   -78.827  1.00 42.09  ? 372 GLU B CB  1 
ATOM   7223  C CG  . GLU B  1 372 ? -42.620  3.663   -79.440  1.00 44.74  ? 372 GLU B CG  1 
ATOM   7224  C CD  . GLU B  1 372 ? -43.903  3.158   -78.780  1.00 48.03  ? 372 GLU B CD  1 
ATOM   7225  O OE1 . GLU B  1 372 ? -43.904  2.426   -77.740  1.00 47.38  ? 372 GLU B OE1 1 
ATOM   7226  O OE2 . GLU B  1 372 ? -44.942  3.535   -79.376  1.00 48.68  ? 372 GLU B OE2 1 
ATOM   7227  N N   . LEU B  1 373 ? -39.437  2.243   -81.389  1.00 39.86  ? 373 LEU B N   1 
ATOM   7228  C CA  . LEU B  1 373 ? -39.447  1.734   -82.754  1.00 40.64  ? 373 LEU B CA  1 
ATOM   7229  C C   . LEU B  1 373 ? -40.701  0.903   -82.945  1.00 38.46  ? 373 LEU B C   1 
ATOM   7230  O O   . LEU B  1 373 ? -41.105  0.202   -82.031  1.00 39.14  ? 373 LEU B O   1 
ATOM   7231  C CB  . LEU B  1 373 ? -38.259  0.820   -83.067  1.00 41.71  ? 373 LEU B CB  1 
ATOM   7232  C CG  . LEU B  1 373 ? -36.880  1.338   -82.691  1.00 43.23  ? 373 LEU B CG  1 
ATOM   7233  C CD1 . LEU B  1 373 ? -35.895  0.194   -82.695  1.00 44.30  ? 373 LEU B CD1 1 
ATOM   7234  C CD2 . LEU B  1 373 ? -36.466  2.432   -83.651  1.00 47.76  ? 373 LEU B CD2 1 
ATOM   7235  N N   . THR B  1 374 ? -41.227  0.941   -84.161  1.00 38.77  ? 374 THR B N   1 
ATOM   7236  C CA  . THR B  1 374 ? -42.266  0.046   -84.620  1.00 40.32  ? 374 THR B CA  1 
ATOM   7237  C C   . THR B  1 374 ? -41.637  -0.910  -85.631  1.00 41.70  ? 374 THR B C   1 
ATOM   7238  O O   . THR B  1 374 ? -41.039  -0.457  -86.596  1.00 41.74  ? 374 THR B O   1 
ATOM   7239  C CB  . THR B  1 374 ? -43.383  0.885   -85.238  1.00 42.68  ? 374 THR B CB  1 
ATOM   7240  O OG1 . THR B  1 374 ? -43.782  1.824   -84.236  1.00 44.10  ? 374 THR B OG1 1 
ATOM   7241  C CG2 . THR B  1 374 ? -44.560  0.038   -85.682  1.00 43.85  ? 374 THR B CG2 1 
ATOM   7242  N N   . ILE B  1 375 ? -41.745  -2.222  -85.386  1.00 42.40  ? 375 ILE B N   1 
ATOM   7243  C CA  . ILE B  1 375 ? -41.359  -3.255  -86.337  1.00 41.88  ? 375 ILE B CA  1 
ATOM   7244  C C   . ILE B  1 375 ? -42.600  -4.045  -86.767  1.00 43.34  ? 375 ILE B C   1 
ATOM   7245  O O   . ILE B  1 375 ? -43.631  -4.005  -86.083  1.00 43.70  ? 375 ILE B O   1 
ATOM   7246  C CB  . ILE B  1 375 ? -40.305  -4.170  -85.698  1.00 42.67  ? 375 ILE B CB  1 
ATOM   7247  C CG1 . ILE B  1 375 ? -40.834  -4.896  -84.457  1.00 41.72  ? 375 ILE B CG1 1 
ATOM   7248  C CG2 . ILE B  1 375 ? -39.018  -3.399  -85.374  1.00 43.31  ? 375 ILE B CG2 1 
ATOM   7249  C CD1 . ILE B  1 375 ? -39.908  -5.995  -83.955  1.00 41.74  ? 375 ILE B CD1 1 
ATOM   7250  N N   . ASP B  1 376 ? -42.498  -4.765  -87.900  1.00 43.66  ? 376 ASP B N   1 
ATOM   7251  C CA  . ASP B  1 376 ? -43.575  -5.633  -88.391  1.00 45.63  ? 376 ASP B CA  1 
ATOM   7252  C C   . ASP B  1 376 ? -42.954  -6.976  -88.781  1.00 43.39  ? 376 ASP B C   1 
ATOM   7253  O O   . ASP B  1 376 ? -42.615  -7.206  -89.931  1.00 46.11  ? 376 ASP B O   1 
ATOM   7254  C CB  . ASP B  1 376 ? -44.343  -5.029  -89.563  1.00 46.77  ? 376 ASP B CB  1 
ATOM   7255  C CG  . ASP B  1 376 ? -45.692  -5.659  -89.923  1.00 49.69  ? 376 ASP B CG  1 
ATOM   7256  O OD1 . ASP B  1 376 ? -46.283  -6.395  -89.099  1.00 49.44  ? 376 ASP B OD1 1 
ATOM   7257  O OD2 . ASP B  1 376 ? -46.179  -5.394  -91.039  1.00 53.10  ? 376 ASP B OD2 1 
ATOM   7258  N N   . PRO B  1 377 ? -42.690  -7.869  -87.816  1.00 39.92  ? 377 PRO B N   1 
ATOM   7259  C CA  . PRO B  1 377 ? -41.998  -9.124  -88.102  1.00 38.95  ? 377 PRO B CA  1 
ATOM   7260  C C   . PRO B  1 377 ? -42.948  -10.235 -88.539  1.00 39.99  ? 377 PRO B C   1 
ATOM   7261  O O   . PRO B  1 377 ? -44.078  -10.292 -88.065  1.00 40.36  ? 377 PRO B O   1 
ATOM   7262  C CB  . PRO B  1 377 ? -41.386  -9.377  -86.745  1.00 38.81  ? 377 PRO B CB  1 
ATOM   7263  C CG  . PRO B  1 377 ? -42.442  -8.923  -85.757  1.00 39.33  ? 377 PRO B CG  1 
ATOM   7264  C CD  . PRO B  1 377 ? -43.063  -7.706  -86.403  1.00 39.88  ? 377 PRO B CD  1 
ATOM   7265  N N   . VAL B  1 378 ? -42.504  -11.062 -89.490  1.00 40.89  ? 378 VAL B N   1 
ATOM   7266  C CA  . VAL B  1 378 ? -43.294  -12.161 -90.028  1.00 43.92  ? 378 VAL B CA  1 
ATOM   7267  C C   . VAL B  1 378 ? -42.901  -13.427 -89.276  1.00 43.42  ? 378 VAL B C   1 
ATOM   7268  O O   . VAL B  1 378 ? -41.714  -13.714 -89.162  1.00 43.45  ? 378 VAL B O   1 
ATOM   7269  C CB  . VAL B  1 378 ? -43.102  -12.374 -91.541  1.00 46.85  ? 378 VAL B CB  1 
ATOM   7270  C CG1 . VAL B  1 378 ? -44.133  -13.343 -92.103  1.00 49.18  ? 378 VAL B CG1 1 
ATOM   7271  C CG2 . VAL B  1 378 ? -43.117  -11.065 -92.330  1.00 47.53  ? 378 VAL B CG2 1 
ATOM   7272  N N   . GLY B  1 379 ? -43.904  -14.152 -88.759  1.00 44.67  ? 379 GLY B N   1 
ATOM   7273  C CA  . GLY B  1 379 ? -43.705  -15.296 -87.874  1.00 43.79  ? 379 GLY B CA  1 
ATOM   7274  C C   . GLY B  1 379 ? -42.701  -14.933 -86.794  1.00 43.78  ? 379 GLY B C   1 
ATOM   7275  O O   . GLY B  1 379 ? -42.868  -13.939 -86.096  1.00 47.44  ? 379 GLY B O   1 
ATOM   7276  N N   . ILE B  1 380 ? -41.633  -15.720 -86.694  1.00 41.44  ? 380 ILE B N   1 
ATOM   7277  C CA  . ILE B  1 380 ? -40.518  -15.406 -85.825  1.00 38.25  ? 380 ILE B CA  1 
ATOM   7278  C C   . ILE B  1 380 ? -39.399  -14.941 -86.736  1.00 36.37  ? 380 ILE B C   1 
ATOM   7279  O O   . ILE B  1 380 ? -39.128  -15.608 -87.719  1.00 39.15  ? 380 ILE B O   1 
ATOM   7280  C CB  . ILE B  1 380 ? -40.088  -16.637 -85.026  1.00 38.73  ? 380 ILE B CB  1 
ATOM   7281  C CG1 . ILE B  1 380 ? -41.263  -17.216 -84.166  1.00 40.66  ? 380 ILE B CG1 1 
ATOM   7282  C CG2 . ILE B  1 380 ? -38.853  -16.309 -84.196  1.00 37.24  ? 380 ILE B CG2 1 
ATOM   7283  C CD1 . ILE B  1 380 ? -41.066  -18.653 -83.672  1.00 39.35  ? 380 ILE B CD1 1 
ATOM   7284  N N   . GLU B  1 381 ? -38.803  -13.790 -86.449  1.00 33.68  ? 381 GLU B N   1 
ATOM   7285  C CA  . GLU B  1 381 ? -37.922  -13.148 -87.411  1.00 33.39  ? 381 GLU B CA  1 
ATOM   7286  C C   . GLU B  1 381 ? -36.699  -12.604 -86.674  1.00 31.28  ? 381 GLU B C   1 
ATOM   7287  O O   . GLU B  1 381 ? -36.825  -11.753 -85.797  1.00 30.94  ? 381 GLU B O   1 
ATOM   7288  C CB  . GLU B  1 381 ? -38.737  -12.078 -88.143  1.00 34.07  ? 381 GLU B CB  1 
ATOM   7289  C CG  . GLU B  1 381 ? -38.038  -11.505 -89.372  1.00 34.64  ? 381 GLU B CG  1 
ATOM   7290  C CD  . GLU B  1 381 ? -38.770  -10.395 -90.117  1.00 36.89  ? 381 GLU B CD  1 
ATOM   7291  O OE1 . GLU B  1 381 ? -39.983  -10.456 -90.311  1.00 38.33  ? 381 GLU B OE1 1 
ATOM   7292  O OE2 . GLU B  1 381 ? -38.113  -9.445  -90.562  1.00 39.37  ? 381 GLU B OE2 1 
ATOM   7293  N N   . ASP B  1 382 ? -35.517  -13.118 -87.005  1.00 30.02  ? 382 ASP B N   1 
ATOM   7294  C CA  . ASP B  1 382 ? -34.285  -12.467 -86.596  1.00 28.37  ? 382 ASP B CA  1 
ATOM   7295  C C   . ASP B  1 382 ? -34.167  -11.147 -87.340  1.00 27.75  ? 382 ASP B C   1 
ATOM   7296  O O   . ASP B  1 382 ? -34.458  -11.101 -88.518  1.00 27.12  ? 382 ASP B O   1 
ATOM   7297  C CB  . ASP B  1 382 ? -33.078  -13.318 -86.946  1.00 28.73  ? 382 ASP B CB  1 
ATOM   7298  C CG  . ASP B  1 382 ? -33.046  -13.877 -88.372  1.00 29.10  ? 382 ASP B CG  1 
ATOM   7299  O OD1 . ASP B  1 382 ? -34.038  -14.526 -88.748  1.00 28.35  ? 382 ASP B OD1 1 
ATOM   7300  O OD2 . ASP B  1 382 ? -32.008  -13.678 -89.082  1.00 27.63  ? 382 ASP B OD2 1 
ATOM   7301  N N   . MET B  1 383 ? -33.678  -10.090 -86.680  1.00 27.98  ? 383 MET B N   1 
ATOM   7302  C CA  . MET B  1 383 ? -33.567  -8.789  -87.330  1.00 28.14  ? 383 MET B CA  1 
ATOM   7303  C C   . MET B  1 383 ? -32.316  -8.072  -86.849  1.00 26.32  ? 383 MET B C   1 
ATOM   7304  O O   . MET B  1 383 ? -32.112  -7.921  -85.654  1.00 25.76  ? 383 MET B O   1 
ATOM   7305  C CB  . MET B  1 383 ? -34.768  -7.890  -87.004  1.00 29.36  ? 383 MET B CB  1 
ATOM   7306  C CG  . MET B  1 383 ? -36.136  -8.462  -87.342  1.00 31.30  ? 383 MET B CG  1 
ATOM   7307  S SD  . MET B  1 383 ? -37.507  -7.363  -86.908  1.00 32.93  ? 383 MET B SD  1 
ATOM   7308  C CE  . MET B  1 383 ? -37.387  -5.992  -88.057  1.00 35.20  ? 383 MET B CE  1 
ATOM   7309  N N   . GLU B  1 384 ? -31.465  -7.652  -87.787  1.00 26.58  ? 384 GLU B N   1 
ATOM   7310  C CA  . GLU B  1 384 ? -30.341  -6.790  -87.461  1.00 25.48  ? 384 GLU B CA  1 
ATOM   7311  C C   . GLU B  1 384 ? -30.772  -5.335  -87.667  1.00 25.65  ? 384 GLU B C   1 
ATOM   7312  O O   . GLU B  1 384 ? -30.943  -4.896  -88.813  1.00 25.80  ? 384 GLU B O   1 
ATOM   7313  C CB  . GLU B  1 384 ? -29.143  -7.152  -88.342  1.00 26.04  ? 384 GLU B CB  1 
ATOM   7314  C CG  . GLU B  1 384 ? -27.870  -6.406  -87.915  1.00 25.94  ? 384 GLU B CG  1 
ATOM   7315  C CD  . GLU B  1 384 ? -26.647  -6.674  -88.752  1.00 26.47  ? 384 GLU B CD  1 
ATOM   7316  O OE1 . GLU B  1 384 ? -26.874  -7.239  -89.845  1.00 26.54  ? 384 GLU B OE1 1 
ATOM   7317  O OE2 . GLU B  1 384 ? -25.481  -6.341  -88.317  1.00 27.84  ? 384 GLU B OE2 1 
ATOM   7318  N N   . LEU B  1 385 ? -31.018  -4.613  -86.562  1.00 25.66  ? 385 LEU B N   1 
ATOM   7319  C CA  . LEU B  1 385 ? -31.446  -3.218  -86.646  1.00 26.27  ? 385 LEU B CA  1 
ATOM   7320  C C   . LEU B  1 385 ? -30.177  -2.374  -86.779  1.00 26.45  ? 385 LEU B C   1 
ATOM   7321  O O   . LEU B  1 385 ? -29.291  -2.474  -85.920  1.00 25.12  ? 385 LEU B O   1 
ATOM   7322  C CB  . LEU B  1 385 ? -32.245  -2.771  -85.428  1.00 25.98  ? 385 LEU B CB  1 
ATOM   7323  C CG  . LEU B  1 385 ? -33.409  -3.662  -85.008  1.00 26.97  ? 385 LEU B CG  1 
ATOM   7324  C CD1 . LEU B  1 385 ? -34.021  -3.206  -83.674  1.00 26.35  ? 385 LEU B CD1 1 
ATOM   7325  C CD2 . LEU B  1 385 ? -34.432  -3.732  -86.112  1.00 27.71  ? 385 LEU B CD2 1 
ATOM   7326  N N   . ALA B  1 386 ? -30.071  -1.618  -87.888  1.00 26.79  ? 386 ALA B N   1 
ATOM   7327  C CA  . ALA B  1 386 ? -28.854  -0.872  -88.186  1.00 27.71  ? 386 ALA B CA  1 
ATOM   7328  C C   . ALA B  1 386 ? -29.026  0.595   -87.774  1.00 28.36  ? 386 ALA B C   1 
ATOM   7329  O O   . ALA B  1 386 ? -29.819  1.340   -88.378  1.00 26.11  ? 386 ALA B O   1 
ATOM   7330  C CB  . ALA B  1 386 ? -28.526  -0.995  -89.646  1.00 28.29  ? 386 ALA B CB  1 
ATOM   7331  N N   . PHE B  1 387 ? -28.279  0.972   -86.724  1.00 28.90  ? 387 PHE B N   1 
ATOM   7332  C CA  . PHE B  1 387 ? -28.330  2.312   -86.164  1.00 27.98  ? 387 PHE B CA  1 
ATOM   7333  C C   . PHE B  1 387 ? -27.264  3.171   -86.824  1.00 28.39  ? 387 PHE B C   1 
ATOM   7334  O O   . PHE B  1 387 ? -26.109  2.747   -86.955  1.00 27.78  ? 387 PHE B O   1 
ATOM   7335  C CB  . PHE B  1 387 ? -28.112  2.329   -84.661  1.00 26.39  ? 387 PHE B CB  1 
ATOM   7336  C CG  . PHE B  1 387 ? -29.333  1.887   -83.879  1.00 28.06  ? 387 PHE B CG  1 
ATOM   7337  C CD1 . PHE B  1 387 ? -29.721  0.555   -83.858  1.00 29.82  ? 387 PHE B CD1 1 
ATOM   7338  C CD2 . PHE B  1 387 ? -30.055  2.794   -83.105  1.00 30.45  ? 387 PHE B CD2 1 
ATOM   7339  C CE1 . PHE B  1 387 ? -30.847  0.155   -83.140  1.00 31.52  ? 387 PHE B CE1 1 
ATOM   7340  C CE2 . PHE B  1 387 ? -31.163  2.381   -82.367  1.00 30.23  ? 387 PHE B CE2 1 
ATOM   7341  C CZ  . PHE B  1 387 ? -31.563  1.075   -82.393  1.00 30.22  ? 387 PHE B CZ  1 
ATOM   7342  N N   . GLU B  1 388 ? -27.687  4.393   -87.183  1.00 29.38  ? 388 GLU B N   1 
ATOM   7343  C CA  . GLU B  1 388 ? -26.820  5.411   -87.771  1.00 30.56  ? 388 GLU B CA  1 
ATOM   7344  C C   . GLU B  1 388 ? -26.895  6.722   -86.988  1.00 30.31  ? 388 GLU B C   1 
ATOM   7345  O O   . GLU B  1 388 ? -27.989  7.258   -86.849  1.00 30.25  ? 388 GLU B O   1 
ATOM   7346  C CB  . GLU B  1 388 ? -27.292  5.689   -89.191  1.00 30.63  ? 388 GLU B CB  1 
ATOM   7347  C CG  . GLU B  1 388 ? -27.139  4.457   -90.063  1.00 30.73  ? 388 GLU B CG  1 
ATOM   7348  C CD  . GLU B  1 388 ? -27.747  4.623   -91.408  1.00 32.43  ? 388 GLU B CD  1 
ATOM   7349  O OE1 . GLU B  1 388 ? -28.375  5.679   -91.712  1.00 32.35  ? 388 GLU B OE1 1 
ATOM   7350  O OE2 . GLU B  1 388 ? -27.606  3.609   -92.113  1.00 34.29  ? 388 GLU B OE2 1 
ATOM   7351  N N   . PHE B  1 389 ? -25.740  7.199   -86.484  1.00 29.32  ? 389 PHE B N   1 
ATOM   7352  C CA  . PHE B  1 389 ? -25.656  8.486   -85.808  1.00 30.96  ? 389 PHE B CA  1 
ATOM   7353  C C   . PHE B  1 389 ? -25.020  9.504   -86.754  1.00 29.76  ? 389 PHE B C   1 
ATOM   7354  O O   . PHE B  1 389 ? -23.982  9.230   -87.341  1.00 29.05  ? 389 PHE B O   1 
ATOM   7355  C CB  . PHE B  1 389 ? -24.888  8.364   -84.488  1.00 30.71  ? 389 PHE B CB  1 
ATOM   7356  C CG  . PHE B  1 389 ? -25.446  7.329   -83.523  1.00 29.23  ? 389 PHE B CG  1 
ATOM   7357  C CD1 . PHE B  1 389 ? -25.183  5.976   -83.695  1.00 30.61  ? 389 PHE B CD1 1 
ATOM   7358  C CD2 . PHE B  1 389 ? -26.214  7.715   -82.444  1.00 28.84  ? 389 PHE B CD2 1 
ATOM   7359  C CE1 . PHE B  1 389 ? -25.709  5.027   -82.824  1.00 30.06  ? 389 PHE B CE1 1 
ATOM   7360  C CE2 . PHE B  1 389 ? -26.729  6.778   -81.577  1.00 28.76  ? 389 PHE B CE2 1 
ATOM   7361  C CZ  . PHE B  1 389 ? -26.467  5.438   -81.757  1.00 30.41  ? 389 PHE B CZ  1 
ATOM   7362  N N   . TYR B  1 390 ? -25.658  10.668  -86.909  1.00 30.61  ? 390 TYR B N   1 
ATOM   7363  C CA  . TYR B  1 390 ? -25.163  11.712  -87.818  1.00 32.53  ? 390 TYR B CA  1 
ATOM   7364  C C   . TYR B  1 390 ? -24.789  12.998  -87.066  1.00 30.67  ? 390 TYR B C   1 
ATOM   7365  O O   . TYR B  1 390 ? -25.425  13.360  -86.087  1.00 29.88  ? 390 TYR B O   1 
ATOM   7366  C CB  . TYR B  1 390 ? -26.194  12.087  -88.885  1.00 34.05  ? 390 TYR B CB  1 
ATOM   7367  C CG  . TYR B  1 390 ? -26.587  10.964  -89.840  1.00 37.87  ? 390 TYR B CG  1 
ATOM   7368  C CD1 . TYR B  1 390 ? -27.535  10.010  -89.482  1.00 36.88  ? 390 TYR B CD1 1 
ATOM   7369  C CD2 . TYR B  1 390 ? -26.027  10.866  -91.114  1.00 40.39  ? 390 TYR B CD2 1 
ATOM   7370  C CE1 . TYR B  1 390 ? -27.900  8.999   -90.353  1.00 38.40  ? 390 TYR B CE1 1 
ATOM   7371  C CE2 . TYR B  1 390 ? -26.405  9.871   -92.004  1.00 40.68  ? 390 TYR B CE2 1 
ATOM   7372  C CZ  . TYR B  1 390 ? -27.351  8.933   -91.626  1.00 40.70  ? 390 TYR B CZ  1 
ATOM   7373  O OH  . TYR B  1 390 ? -27.704  7.919   -92.484  1.00 40.51  ? 390 TYR B OH  1 
ATOM   7374  N N   . ASP B  1 391 ? -23.785  13.718  -87.573  1.00 30.66  ? 391 ASP B N   1 
ATOM   7375  C CA  . ASP B  1 391 ? -23.383  15.019  -87.042  1.00 32.72  ? 391 ASP B CA  1 
ATOM   7376  C C   . ASP B  1 391 ? -24.166  16.137  -87.721  1.00 34.65  ? 391 ASP B C   1 
ATOM   7377  O O   . ASP B  1 391 ? -25.099  15.861  -88.450  1.00 36.85  ? 391 ASP B O   1 
ATOM   7378  C CB  . ASP B  1 391 ? -21.872  15.200  -87.128  1.00 32.34  ? 391 ASP B CB  1 
ATOM   7379  C CG  . ASP B  1 391 ? -21.235  15.350  -88.493  1.00 30.88  ? 391 ASP B CG  1 
ATOM   7380  O OD1 . ASP B  1 391 ? -21.968  15.629  -89.457  1.00 31.03  ? 391 ASP B OD1 1 
ATOM   7381  O OD2 . ASP B  1 391 ? -19.998  15.229  -88.538  1.00 30.75  ? 391 ASP B OD2 1 
ATOM   7382  N N   . SER B  1 392 ? -23.782  17.396  -87.490  1.00 37.14  ? 392 SER B N   1 
ATOM   7383  C CA  . SER B  1 392 ? -24.520  18.550  -88.002  1.00 36.93  ? 392 SER B CA  1 
ATOM   7384  C C   . SER B  1 392 ? -24.295  18.794  -89.499  1.00 35.99  ? 392 SER B C   1 
ATOM   7385  O O   . SER B  1 392 ? -25.052  19.554  -90.120  1.00 36.17  ? 392 SER B O   1 
ATOM   7386  C CB  . SER B  1 392 ? -24.192  19.793  -87.202  1.00 38.85  ? 392 SER B CB  1 
ATOM   7387  O OG  . SER B  1 392 ? -22.810  20.123  -87.311  1.00 40.81  ? 392 SER B OG  1 
ATOM   7388  N N   . ASP B  1 393 ? -23.269  18.162  -90.098  1.00 35.37  ? 393 ASP B N   1 
ATOM   7389  C CA  . ASP B  1 393 ? -23.087  18.221  -91.546  1.00 37.06  ? 393 ASP B CA  1 
ATOM   7390  C C   . ASP B  1 393 ? -23.759  17.021  -92.230  1.00 35.73  ? 393 ASP B C   1 
ATOM   7391  O O   . ASP B  1 393 ? -23.530  16.727  -93.389  1.00 34.42  ? 393 ASP B O   1 
ATOM   7392  C CB  . ASP B  1 393 ? -21.616  18.444  -91.897  1.00 40.86  ? 393 ASP B CB  1 
ATOM   7393  C CG  . ASP B  1 393 ? -20.975  19.704  -91.311  1.00 43.66  ? 393 ASP B CG  1 
ATOM   7394  O OD1 . ASP B  1 393 ? -21.609  20.804  -91.414  1.00 45.92  ? 393 ASP B OD1 1 
ATOM   7395  O OD2 . ASP B  1 393 ? -19.863  19.593  -90.728  1.00 40.88  ? 393 ASP B OD2 1 
ATOM   7396  N N   . ASN B  1 394 ? -24.592  16.296  -91.485  1.00 36.95  ? 394 ASN B N   1 
ATOM   7397  C CA  . ASN B  1 394 ? -25.335  15.177  -92.006  1.00 38.43  ? 394 ASN B CA  1 
ATOM   7398  C C   . ASN B  1 394 ? -24.394  14.064  -92.482  1.00 37.94  ? 394 ASN B C   1 
ATOM   7399  O O   . ASN B  1 394 ? -24.707  13.385  -93.457  1.00 36.63  ? 394 ASN B O   1 
ATOM   7400  C CB  . ASN B  1 394 ? -26.316  15.657  -93.069  1.00 40.00  ? 394 ASN B CB  1 
ATOM   7401  C CG  . ASN B  1 394 ? -27.450  14.672  -93.199  1.00 43.62  ? 394 ASN B CG  1 
ATOM   7402  O OD1 . ASN B  1 394 ? -28.083  14.300  -92.200  1.00 45.29  ? 394 ASN B OD1 1 
ATOM   7403  N ND2 . ASN B  1 394 ? -27.647  14.157  -94.399  1.00 45.64  ? 394 ASN B ND2 1 
ATOM   7404  N N   . LYS B  1 395 ? -23.254  13.893  -91.790  1.00 37.43  ? 395 LYS B N   1 
ATOM   7405  C CA  . LYS B  1 395 ? -22.318  12.805  -92.037  1.00 40.41  ? 395 LYS B CA  1 
ATOM   7406  C C   . LYS B  1 395 ? -22.429  11.763  -90.916  1.00 37.53  ? 395 LYS B C   1 
ATOM   7407  O O   . LYS B  1 395 ? -22.667  12.115  -89.765  1.00 34.61  ? 395 LYS B O   1 
ATOM   7408  C CB  . LYS B  1 395 ? -20.881  13.324  -92.137  1.00 41.56  ? 395 LYS B CB  1 
ATOM   7409  C CG  . LYS B  1 395 ? -20.603  14.082  -93.419  1.00 49.06  ? 395 LYS B CG  1 
ATOM   7410  C CD  . LYS B  1 395 ? -19.293  14.856  -93.258  1.00 56.90  ? 395 LYS B CD  1 
ATOM   7411  C CE  . LYS B  1 395 ? -18.942  15.759  -94.396  1.00 61.48  ? 395 LYS B CE  1 
ATOM   7412  N NZ  . LYS B  1 395 ? -19.679  17.021  -94.298  1.00 67.84  ? 395 LYS B NZ  1 
ATOM   7413  N N   . ILE B  1 396 ? -22.277  10.476  -91.263  1.00 38.18  ? 396 ILE B N   1 
ATOM   7414  C CA  . ILE B  1 396 ? -22.359  9.393   -90.284  1.00 39.08  ? 396 ILE B CA  1 
ATOM   7415  C C   . ILE B  1 396 ? -21.065  9.379   -89.477  1.00 38.18  ? 396 ILE B C   1 
ATOM   7416  O O   . ILE B  1 396 ? -19.985  9.342   -90.041  1.00 40.95  ? 396 ILE B O   1 
ATOM   7417  C CB  . ILE B  1 396 ? -22.680  8.035   -90.947  1.00 39.01  ? 396 ILE B CB  1 
ATOM   7418  C CG1 . ILE B  1 396 ? -24.135  8.012   -91.402  1.00 44.86  ? 396 ILE B CG1 1 
ATOM   7419  C CG2 . ILE B  1 396 ? -22.408  6.846   -90.019  1.00 38.84  ? 396 ILE B CG2 1 
ATOM   7420  C CD1 . ILE B  1 396 ? -24.620  6.715   -92.041  1.00 48.73  ? 396 ILE B CD1 1 
ATOM   7421  N N   . ILE B  1 397 ? -21.188  9.407   -88.152  1.00 37.19  ? 397 ILE B N   1 
ATOM   7422  C CA  . ILE B  1 397 ? -20.032  9.326   -87.275  1.00 35.96  ? 397 ILE B CA  1 
ATOM   7423  C C   . ILE B  1 397 ? -20.022  8.035   -86.466  1.00 34.16  ? 397 ILE B C   1 
ATOM   7424  O O   . ILE B  1 397 ? -19.034  7.780   -85.801  1.00 31.91  ? 397 ILE B O   1 
ATOM   7425  C CB  . ILE B  1 397 ? -19.971  10.547  -86.352  1.00 34.43  ? 397 ILE B CB  1 
ATOM   7426  C CG1 . ILE B  1 397 ? -21.253  10.680  -85.568  1.00 35.09  ? 397 ILE B CG1 1 
ATOM   7427  C CG2 . ILE B  1 397 ? -19.624  11.787  -87.178  1.00 35.41  ? 397 ILE B CG2 1 
ATOM   7428  C CD1 . ILE B  1 397 ? -21.283  11.848  -84.600  1.00 37.61  ? 397 ILE B CD1 1 
ATOM   7429  N N   . LYS B  1 398 ? -21.114  7.251   -86.495  1.00 34.63  ? 398 LYS B N   1 
ATOM   7430  C CA  . LYS B  1 398 ? -21.122  5.926   -85.886  1.00 32.53  ? 398 LYS B CA  1 
ATOM   7431  C C   . LYS B  1 398 ? -22.177  5.027   -86.543  1.00 34.75  ? 398 LYS B C   1 
ATOM   7432  O O   . LYS B  1 398 ? -23.294  5.466   -86.831  1.00 34.25  ? 398 LYS B O   1 
ATOM   7433  C CB  . LYS B  1 398 ? -21.385  6.017   -84.376  1.00 30.65  ? 398 LYS B CB  1 
ATOM   7434  C CG  . LYS B  1 398 ? -21.273  4.683   -83.651  1.00 30.53  ? 398 LYS B CG  1 
ATOM   7435  C CD  . LYS B  1 398 ? -21.562  4.683   -82.163  1.00 29.41  ? 398 LYS B CD  1 
ATOM   7436  C CE  . LYS B  1 398 ? -21.838  3.317   -81.619  1.00 29.71  ? 398 LYS B CE  1 
ATOM   7437  N NZ  . LYS B  1 398 ? -22.062  3.450   -80.173  1.00 30.23  ? 398 LYS B NZ  1 
ATOM   7438  N N   . ASN B  1 399 ? -21.782  3.761   -86.760  1.00 35.21  ? 399 ASN B N   1 
ATOM   7439  C CA  . ASN B  1 399 ? -22.673  2.667   -87.097  1.00 33.83  ? 399 ASN B CA  1 
ATOM   7440  C C   . ASN B  1 399 ? -22.683  1.670   -85.944  1.00 32.75  ? 399 ASN B C   1 
ATOM   7441  O O   . ASN B  1 399 ? -21.652  1.479   -85.315  1.00 33.91  ? 399 ASN B O   1 
ATOM   7442  C CB  . ASN B  1 399 ? -22.209  1.950   -88.353  1.00 32.95  ? 399 ASN B CB  1 
ATOM   7443  C CG  . ASN B  1 399 ? -22.332  2.804   -89.585  1.00 33.57  ? 399 ASN B CG  1 
ATOM   7444  O OD1 . ASN B  1 399 ? -21.327  3.063   -90.249  1.00 32.61  ? 399 ASN B OD1 1 
ATOM   7445  N ND2 . ASN B  1 399 ? -23.549  3.180   -89.958  1.00 36.16  ? 399 ASN B ND2 1 
ATOM   7446  N N   . GLU B  1 400 ? -23.835  1.033   -85.678  1.00 31.38  ? 400 GLU B N   1 
ATOM   7447  C CA  . GLU B  1 400 ? -23.912  -0.067  -84.724  1.00 28.69  ? 400 GLU B CA  1 
ATOM   7448  C C   . GLU B  1 400 ? -25.185  -0.882  -84.964  1.00 27.59  ? 400 GLU B C   1 
ATOM   7449  O O   . GLU B  1 400 ? -26.246  -0.339  -85.263  1.00 28.56  ? 400 GLU B O   1 
ATOM   7450  C CB  . GLU B  1 400 ? -23.895  0.434   -83.281  1.00 28.81  ? 400 GLU B CB  1 
ATOM   7451  C CG  . GLU B  1 400 ? -23.708  -0.682  -82.259  1.00 29.79  ? 400 GLU B CG  1 
ATOM   7452  C CD  . GLU B  1 400 ? -23.580  -0.235  -80.807  1.00 31.49  ? 400 GLU B CD  1 
ATOM   7453  O OE1 . GLU B  1 400 ? -23.764  0.987   -80.535  1.00 26.66  ? 400 GLU B OE1 1 
ATOM   7454  O OE2 . GLU B  1 400 ? -23.260  -1.136  -79.956  1.00 31.02  ? 400 GLU B OE2 1 
ATOM   7455  N N   . SER B  1 401 ? -25.084  -2.198  -84.813  1.00 26.09  ? 401 SER B N   1 
ATOM   7456  C CA  . SER B  1 401 ? -26.210  -3.082  -85.056  1.00 25.93  ? 401 SER B CA  1 
ATOM   7457  C C   . SER B  1 401 ? -26.765  -3.503  -83.716  1.00 24.67  ? 401 SER B C   1 
ATOM   7458  O O   . SER B  1 401 ? -26.020  -3.583  -82.749  1.00 24.39  ? 401 SER B O   1 
ATOM   7459  C CB  . SER B  1 401 ? -25.853  -4.308  -85.859  1.00 26.19  ? 401 SER B CB  1 
ATOM   7460  O OG  . SER B  1 401 ? -25.565  -3.969  -87.198  1.00 26.02  ? 401 SER B OG  1 
ATOM   7461  N N   . ILE B  1 402 ? -28.081  -3.703  -83.670  1.00 24.64  ? 402 ILE B N   1 
ATOM   7462  C CA  . ILE B  1 402 ? -28.693  -4.382  -82.544  1.00 24.97  ? 402 ILE B CA  1 
ATOM   7463  C C   . ILE B  1 402 ? -29.433  -5.594  -83.094  1.00 25.05  ? 402 ILE B C   1 
ATOM   7464  O O   . ILE B  1 402 ? -30.356  -5.431  -83.900  1.00 26.49  ? 402 ILE B O   1 
ATOM   7465  C CB  . ILE B  1 402 ? -29.644  -3.438  -81.791  1.00 26.22  ? 402 ILE B CB  1 
ATOM   7466  C CG1 . ILE B  1 402 ? -28.903  -2.212  -81.225  1.00 26.00  ? 402 ILE B CG1 1 
ATOM   7467  C CG2 . ILE B  1 402 ? -30.386  -4.189  -80.685  1.00 27.06  ? 402 ILE B CG2 1 
ATOM   7468  C CD1 . ILE B  1 402 ? -28.041  -2.550  -80.016  1.00 25.62  ? 402 ILE B CD1 1 
ATOM   7469  N N   . ASN B  1 403 ? -29.055  -6.780  -82.633  1.00 23.74  ? 403 ASN B N   1 
ATOM   7470  C CA  . ASN B  1 403 ? -29.685  -7.980  -83.138  1.00 25.07  ? 403 ASN B CA  1 
ATOM   7471  C C   . ASN B  1 403 ? -30.830  -8.366  -82.225  1.00 25.42  ? 403 ASN B C   1 
ATOM   7472  O O   . ASN B  1 403 ? -30.594  -8.641  -81.057  1.00 25.68  ? 403 ASN B O   1 
ATOM   7473  C CB  . ASN B  1 403 ? -28.711  -9.143  -83.232  1.00 25.18  ? 403 ASN B CB  1 
ATOM   7474  C CG  . ASN B  1 403 ? -27.733  -8.895  -84.341  1.00 25.22  ? 403 ASN B CG  1 
ATOM   7475  O OD1 . ASN B  1 403 ? -28.139  -8.883  -85.499  1.00 28.25  ? 403 ASN B OD1 1 
ATOM   7476  N ND2 . ASN B  1 403 ? -26.513  -8.539  -84.014  1.00 24.02  ? 403 ASN B ND2 1 
ATOM   7477  N N   . ILE B  1 404 ? -32.035  -8.465  -82.783  1.00 25.57  ? 404 ILE B N   1 
ATOM   7478  C CA  . ILE B  1 404 ? -33.159  -8.922  -81.984  1.00 27.08  ? 404 ILE B CA  1 
ATOM   7479  C C   . ILE B  1 404 ? -33.793  -10.139 -82.676  1.00 29.04  ? 404 ILE B C   1 
ATOM   7480  O O   . ILE B  1 404 ? -33.595  -10.343 -83.871  1.00 29.73  ? 404 ILE B O   1 
ATOM   7481  C CB  . ILE B  1 404 ? -34.201  -7.802  -81.753  1.00 27.16  ? 404 ILE B CB  1 
ATOM   7482  C CG1 . ILE B  1 404 ? -34.968  -7.441  -83.029  1.00 27.85  ? 404 ILE B CG1 1 
ATOM   7483  C CG2 . ILE B  1 404 ? -33.582  -6.563  -81.102  1.00 26.82  ? 404 ILE B CG2 1 
ATOM   7484  C CD1 . ILE B  1 404 ? -36.120  -6.465  -82.806  1.00 28.35  ? 404 ILE B CD1 1 
ATOM   7485  N N   . LEU B  1 405 ? -34.568  -10.914 -81.904  1.00 28.47  ? 405 LEU B N   1 
ATOM   7486  C CA  . LEU B  1 405 ? -35.448  -11.930 -82.430  1.00 30.43  ? 405 LEU B CA  1 
ATOM   7487  C C   . LEU B  1 405 ? -36.866  -11.504 -82.072  1.00 31.03  ? 405 LEU B C   1 
ATOM   7488  O O   . LEU B  1 405 ? -37.141  -11.294 -80.899  1.00 31.32  ? 405 LEU B O   1 
ATOM   7489  C CB  . LEU B  1 405 ? -35.045  -13.256 -81.777  1.00 31.15  ? 405 LEU B CB  1 
ATOM   7490  C CG  . LEU B  1 405 ? -35.794  -14.498 -82.257  1.00 32.90  ? 405 LEU B CG  1 
ATOM   7491  C CD1 . LEU B  1 405 ? -35.433  -14.771 -83.690  1.00 34.80  ? 405 LEU B CD1 1 
ATOM   7492  C CD2 . LEU B  1 405 ? -35.521  -15.728 -81.372  1.00 33.81  ? 405 LEU B CD2 1 
ATOM   7493  N N   . ALA B  1 406 ? -37.754  -11.362 -83.061  1.00 30.90  ? 406 ALA B N   1 
ATOM   7494  C CA  . ALA B  1 406 ? -39.022  -10.707 -82.792  1.00 31.72  ? 406 ALA B CA  1 
ATOM   7495  C C   . ALA B  1 406 ? -40.194  -11.480 -83.373  1.00 32.97  ? 406 ALA B C   1 
ATOM   7496  O O   . ALA B  1 406 ? -40.115  -12.007 -84.473  1.00 32.53  ? 406 ALA B O   1 
ATOM   7497  C CB  . ALA B  1 406 ? -39.004  -9.317  -83.361  1.00 31.36  ? 406 ALA B CB  1 
ATOM   7498  N N   . SER B  1 407 ? -41.310  -11.433 -82.655  1.00 34.33  ? 407 SER B N   1 
ATOM   7499  C CA  . SER B  1 407 ? -42.575  -11.894 -83.190  1.00 37.19  ? 407 SER B CA  1 
ATOM   7500  C C   . SER B  1 407 ? -43.734  -11.043 -82.683  1.00 38.29  ? 407 SER B C   1 
ATOM   7501  O O   . SER B  1 407 ? -43.618  -10.373 -81.675  1.00 38.55  ? 407 SER B O   1 
ATOM   7502  C CB  . SER B  1 407 ? -42.794  -13.337 -82.829  1.00 37.63  ? 407 SER B CB  1 
ATOM   7503  O OG  . SER B  1 407 ? -43.962  -13.803 -83.484  1.00 38.78  ? 407 SER B OG  1 
ATOM   7504  N N   . LYS B  1 408 ? -44.873  -11.113 -83.363  1.00 43.01  ? 408 LYS B N   1 
ATOM   7505  C CA  . LYS B  1 408 ? -46.047  -10.369 -82.935  1.00 48.03  ? 408 LYS B CA  1 
ATOM   7506  C C   . LYS B  1 408 ? -46.644  -10.986 -81.672  1.00 50.66  ? 408 LYS B C   1 
ATOM   7507  O O   . LYS B  1 408 ? -47.256  -10.262 -80.873  1.00 48.92  ? 408 LYS B O   1 
ATOM   7508  C CB  . LYS B  1 408 ? -47.092  -10.296 -84.045  1.00 51.60  ? 408 LYS B CB  1 
ATOM   7509  C CG  . LYS B  1 408 ? -46.854  -9.177  -85.042  1.00 54.07  ? 408 LYS B CG  1 
ATOM   7510  C CD  . LYS B  1 408 ? -47.773  -9.190  -86.265  1.00 57.53  ? 408 LYS B CD  1 
ATOM   7511  C CE  . LYS B  1 408 ? -47.338  -8.144  -87.252  1.00 62.00  ? 408 LYS B CE  1 
ATOM   7512  N NZ  . LYS B  1 408 ? -47.702  -8.485  -88.629  1.00 63.96  ? 408 LYS B NZ  1 
ATOM   7513  N N   . THR B  1 409 ? -46.426  -12.305 -81.498  1.00 52.15  ? 409 THR B N   1 
ATOM   7514  C CA  . THR B  1 409 ? -46.948  -13.050 -80.358  1.00 53.63  ? 409 THR B CA  1 
ATOM   7515  C C   . THR B  1 409 ? -45.838  -13.865 -79.696  1.00 53.73  ? 409 THR B C   1 
ATOM   7516  O O   . THR B  1 409 ? -44.756  -14.003 -80.250  1.00 53.81  ? 409 THR B O   1 
ATOM   7517  C CB  . THR B  1 409 ? -48.091  -13.950 -80.825  1.00 54.60  ? 409 THR B CB  1 
ATOM   7518  O OG1 . THR B  1 409 ? -47.522  -14.800 -81.811  1.00 52.07  ? 409 THR B OG1 1 
ATOM   7519  C CG2 . THR B  1 409 ? -49.254  -13.180 -81.432  1.00 55.65  ? 409 THR B CG2 1 
ATOM   7520  N N   . ALA B  1 410 ? -46.152  -14.446 -78.529  1.00 55.80  ? 410 ALA B N   1 
ATOM   7521  C CA  . ALA B  1 410 ? -45.229  -15.279 -77.768  1.00 53.16  ? 410 ALA B CA  1 
ATOM   7522  C C   . ALA B  1 410 ? -44.892  -16.532 -78.569  1.00 49.94  ? 410 ALA B C   1 
ATOM   7523  O O   . ALA B  1 410 ? -45.628  -16.897 -79.475  1.00 49.86  ? 410 ALA B O   1 
ATOM   7524  C CB  . ALA B  1 410 ? -45.828  -15.639 -76.430  1.00 53.26  ? 410 ALA B CB  1 
ATOM   7525  N N   . PHE B  1 411 ? -43.741  -17.140 -78.262  1.00 46.73  ? 411 PHE B N   1 
ATOM   7526  C CA  . PHE B  1 411 ? -43.284  -18.319 -78.975  1.00 44.84  ? 411 PHE B CA  1 
ATOM   7527  C C   . PHE B  1 411 ? -42.361  -19.113 -78.053  1.00 44.18  ? 411 PHE B C   1 
ATOM   7528  O O   . PHE B  1 411 ? -41.724  -18.566 -77.154  1.00 40.87  ? 411 PHE B O   1 
ATOM   7529  C CB  . PHE B  1 411 ? -42.599  -17.985 -80.309  1.00 42.71  ? 411 PHE B CB  1 
ATOM   7530  C CG  . PHE B  1 411 ? -41.415  -17.016 -80.215  1.00 42.00  ? 411 PHE B CG  1 
ATOM   7531  C CD1 . PHE B  1 411 ? -41.600  -15.640 -80.290  1.00 40.46  ? 411 PHE B CD1 1 
ATOM   7532  C CD2 . PHE B  1 411 ? -40.109  -17.482 -80.092  1.00 40.42  ? 411 PHE B CD2 1 
ATOM   7533  C CE1 . PHE B  1 411 ? -40.525  -14.758 -80.216  1.00 40.17  ? 411 PHE B CE1 1 
ATOM   7534  C CE2 . PHE B  1 411 ? -39.035  -16.595 -80.022  1.00 39.60  ? 411 PHE B CE2 1 
ATOM   7535  C CZ  . PHE B  1 411 ? -39.245  -15.235 -80.078  1.00 39.18  ? 411 PHE B CZ  1 
ATOM   7536  N N   . GLU B  1 412 ? -42.289  -20.411 -78.334  1.00 46.58  ? 412 GLU B N   1 
ATOM   7537  C CA  . GLU B  1 412 ? -41.463  -21.330 -77.579  1.00 50.47  ? 412 GLU B CA  1 
ATOM   7538  C C   . GLU B  1 412 ? -40.007  -21.192 -77.992  1.00 47.17  ? 412 GLU B C   1 
ATOM   7539  O O   . GLU B  1 412 ? -39.693  -21.234 -79.175  1.00 46.45  ? 412 GLU B O   1 
ATOM   7540  C CB  . GLU B  1 412 ? -41.896  -22.773 -77.836  1.00 53.91  ? 412 GLU B CB  1 
ATOM   7541  C CG  . GLU B  1 412 ? -43.125  -23.184 -77.030  1.00 58.69  ? 412 GLU B CG  1 
ATOM   7542  C CD  . GLU B  1 412 ? -43.463  -24.655 -77.225  1.00 63.59  ? 412 GLU B CD  1 
ATOM   7543  O OE1 . GLU B  1 412 ? -42.511  -25.477 -77.285  1.00 64.02  ? 412 GLU B OE1 1 
ATOM   7544  O OE2 . GLU B  1 412 ? -44.667  -24.969 -77.316  1.00 62.50  ? 412 GLU B OE2 1 
ATOM   7545  N N   . LEU B  1 413 ? -39.146  -21.076 -76.976  1.00 47.70  ? 413 LEU B N   1 
ATOM   7546  C CA  . LEU B  1 413 ? -37.695  -21.187 -77.104  1.00 45.15  ? 413 LEU B CA  1 
ATOM   7547  C C   . LEU B  1 413 ? -37.216  -22.554 -76.604  1.00 43.39  ? 413 LEU B C   1 
ATOM   7548  O O   . LEU B  1 413 ? -37.847  -23.159 -75.757  1.00 42.03  ? 413 LEU B O   1 
ATOM   7549  C CB  . LEU B  1 413 ? -37.053  -20.104 -76.241  1.00 42.31  ? 413 LEU B CB  1 
ATOM   7550  C CG  . LEU B  1 413 ? -37.255  -18.646 -76.646  1.00 43.28  ? 413 LEU B CG  1 
ATOM   7551  C CD1 . LEU B  1 413 ? -36.666  -17.700 -75.615  1.00 41.20  ? 413 LEU B CD1 1 
ATOM   7552  C CD2 . LEU B  1 413 ? -36.578  -18.398 -77.972  1.00 46.43  ? 413 LEU B CD2 1 
ATOM   7553  N N   . PRO B  1 414 ? -36.029  -23.052 -77.010  1.00 43.65  ? 414 PRO B N   1 
ATOM   7554  C CA  . PRO B  1 414 ? -35.397  -24.148 -76.281  1.00 43.96  ? 414 PRO B CA  1 
ATOM   7555  C C   . PRO B  1 414 ? -34.926  -23.673 -74.903  1.00 43.16  ? 414 PRO B C   1 
ATOM   7556  O O   . PRO B  1 414 ? -34.647  -22.481 -74.698  1.00 42.15  ? 414 PRO B O   1 
ATOM   7557  C CB  . PRO B  1 414 ? -34.274  -24.602 -77.203  1.00 44.46  ? 414 PRO B CB  1 
ATOM   7558  C CG  . PRO B  1 414 ? -33.967  -23.387 -78.050  1.00 45.39  ? 414 PRO B CG  1 
ATOM   7559  C CD  . PRO B  1 414 ? -35.249  -22.597 -78.165  1.00 44.44  ? 414 PRO B CD  1 
ATOM   7560  N N   . GLU B  1 415 ? -34.898  -24.614 -73.946  1.00 42.69  ? 415 GLU B N   1 
ATOM   7561  C CA  . GLU B  1 415 ? -34.603  -24.327 -72.549  1.00 42.28  ? 415 GLU B CA  1 
ATOM   7562  C C   . GLU B  1 415 ? -33.596  -25.345 -72.011  1.00 41.55  ? 415 GLU B C   1 
ATOM   7563  O O   . GLU B  1 415 ? -33.714  -26.567 -72.212  1.00 42.34  ? 415 GLU B O   1 
ATOM   7564  C CB  . GLU B  1 415 ? -35.773  -24.409 -71.561  1.00 46.45  ? 415 GLU B CB  1 
ATOM   7565  C CG  . GLU B  1 415 ? -37.095  -23.792 -72.020  1.00 51.05  ? 415 GLU B CG  1 
ATOM   7566  C CD  . GLU B  1 415 ? -38.186  -23.938 -70.969  1.00 55.68  ? 415 GLU B CD  1 
ATOM   7567  O OE1 . GLU B  1 415 ? -37.867  -23.460 -69.867  1.00 64.12  ? 415 GLU B OE1 1 
ATOM   7568  O OE2 . GLU B  1 415 ? -39.286  -24.506 -71.188  1.00 59.15  ? 415 GLU B OE2 1 
ATOM   7569  N N   . LEU B  1 416 ? -32.623  -24.801 -71.271  1.00 39.37  ? 416 LEU B N   1 
ATOM   7570  C CA  . LEU B  1 416 ? -31.600  -25.559 -70.574  1.00 37.86  ? 416 LEU B CA  1 
ATOM   7571  C C   . LEU B  1 416 ? -31.804  -25.291 -69.086  1.00 36.42  ? 416 LEU B C   1 
ATOM   7572  O O   . LEU B  1 416 ? -31.841  -24.129 -68.666  1.00 35.17  ? 416 LEU B O   1 
ATOM   7573  C CB  . LEU B  1 416 ? -30.204  -25.157 -71.072  1.00 36.76  ? 416 LEU B CB  1 
ATOM   7574  C CG  . LEU B  1 416 ? -29.010  -25.966 -70.543  1.00 36.29  ? 416 LEU B CG  1 
ATOM   7575  C CD1 . LEU B  1 416 ? -27.751  -25.795 -71.429  1.00 36.49  ? 416 LEU B CD1 1 
ATOM   7576  C CD2 . LEU B  1 416 ? -28.681  -25.591 -69.121  1.00 34.20  ? 416 LEU B CD2 1 
ATOM   7577  N N   . THR B  1 417 ? -31.965  -26.386 -68.323  1.00 36.77  ? 417 THR B N   1 
ATOM   7578  C CA  . THR B  1 417 ? -32.025  -26.357 -66.867  1.00 36.66  ? 417 THR B CA  1 
ATOM   7579  C C   . THR B  1 417 ? -31.041  -27.396 -66.373  1.00 35.77  ? 417 THR B C   1 
ATOM   7580  O O   . THR B  1 417 ? -30.758  -28.333 -67.107  1.00 35.85  ? 417 THR B O   1 
ATOM   7581  C CB  . THR B  1 417 ? -33.438  -26.622 -66.333  1.00 38.43  ? 417 THR B CB  1 
ATOM   7582  O OG1 . THR B  1 417 ? -33.933  -27.842 -66.884  1.00 39.59  ? 417 THR B OG1 1 
ATOM   7583  C CG2 . THR B  1 417 ? -34.381  -25.489 -66.702  1.00 39.13  ? 417 THR B CG2 1 
ATOM   7584  N N   . ILE B  1 418 ? -30.527  -27.192 -65.155  1.00 35.83  ? 418 ILE B N   1 
ATOM   7585  C CA  . ILE B  1 418 ? -29.650  -28.154 -64.507  1.00 36.46  ? 418 ILE B CA  1 
ATOM   7586  C C   . ILE B  1 418 ? -30.241  -28.501 -63.153  1.00 38.45  ? 418 ILE B C   1 
ATOM   7587  O O   . ILE B  1 418 ? -30.970  -27.684 -62.607  1.00 40.83  ? 418 ILE B O   1 
ATOM   7588  C CB  . ILE B  1 418 ? -28.218  -27.610 -64.368  1.00 33.63  ? 418 ILE B CB  1 
ATOM   7589  C CG1 . ILE B  1 418 ? -28.164  -26.334 -63.502  1.00 34.31  ? 418 ILE B CG1 1 
ATOM   7590  C CG2 . ILE B  1 418 ? -27.619  -27.395 -65.747  1.00 32.35  ? 418 ILE B CG2 1 
ATOM   7591  C CD1 . ILE B  1 418 ? -26.795  -25.641 -63.462  1.00 34.08  ? 418 ILE B CD1 1 
ATOM   7592  N N   . GLU B  1 419 ? -29.900  -29.695 -62.640  1.00 40.39  ? 419 GLU B N   1 
ATOM   7593  C CA  . GLU B  1 419 ? -30.046  -30.063 -61.236  1.00 41.74  ? 419 GLU B CA  1 
ATOM   7594  C C   . GLU B  1 419 ? -28.656  -30.415 -60.716  1.00 41.41  ? 419 GLU B C   1 
ATOM   7595  O O   . GLU B  1 419 ? -27.925  -31.139 -61.392  1.00 42.07  ? 419 GLU B O   1 
ATOM   7596  C CB  . GLU B  1 419 ? -30.943  -31.285 -61.048  1.00 44.26  ? 419 GLU B CB  1 
ATOM   7597  C CG  . GLU B  1 419 ? -32.349  -31.128 -61.622  1.00 46.52  ? 419 GLU B CG  1 
ATOM   7598  C CD  . GLU B  1 419 ? -33.130  -32.438 -61.544  1.00 50.80  ? 419 GLU B CD  1 
ATOM   7599  O OE1 . GLU B  1 419 ? -32.781  -33.439 -62.227  1.00 49.83  ? 419 GLU B OE1 1 
ATOM   7600  O OE2 . GLU B  1 419 ? -34.106  -32.478 -60.758  1.00 56.01  ? 419 GLU B OE2 1 
ATOM   7601  N N   . VAL B  1 420 ? -28.287  -29.899 -59.535  1.00 39.89  ? 420 VAL B N   1 
ATOM   7602  C CA  . VAL B  1 420 ? -26.922  -29.985 -59.014  1.00 37.28  ? 420 VAL B CA  1 
ATOM   7603  C C   . VAL B  1 420 ? -26.917  -30.768 -57.698  1.00 37.19  ? 420 VAL B C   1 
ATOM   7604  O O   . VAL B  1 420 ? -27.796  -30.601 -56.872  1.00 37.83  ? 420 VAL B O   1 
ATOM   7605  C CB  . VAL B  1 420 ? -26.312  -28.588 -58.812  1.00 35.44  ? 420 VAL B CB  1 
ATOM   7606  C CG1 . VAL B  1 420 ? -24.864  -28.678 -58.424  1.00 35.20  ? 420 VAL B CG1 1 
ATOM   7607  C CG2 . VAL B  1 420 ? -26.427  -27.715 -60.046  1.00 34.66  ? 420 VAL B CG2 1 
ATOM   7608  N N   . THR B  1 421 ? -25.905  -31.618 -57.500  1.00 37.14  ? 421 THR B N   1 
ATOM   7609  C CA  . THR B  1 421 ? -25.698  -32.350 -56.261  1.00 37.23  ? 421 THR B CA  1 
ATOM   7610  C C   . THR B  1 421 ? -24.299  -32.063 -55.697  1.00 37.22  ? 421 THR B C   1 
ATOM   7611  O O   . THR B  1 421 ? -23.316  -31.976 -56.433  1.00 34.83  ? 421 THR B O   1 
ATOM   7612  C CB  . THR B  1 421 ? -25.854  -33.829 -56.574  1.00 38.49  ? 421 THR B CB  1 
ATOM   7613  O OG1 . THR B  1 421 ? -27.058  -33.920 -57.318  1.00 37.89  ? 421 THR B OG1 1 
ATOM   7614  C CG2 . THR B  1 421 ? -25.911  -34.679 -55.323  1.00 39.45  ? 421 THR B CG2 1 
ATOM   7615  N N   . PRO B  1 422 ? -24.138  -31.856 -54.371  1.00 39.24  ? 422 PRO B N   1 
ATOM   7616  C CA  . PRO B  1 422 ? -25.246  -31.561 -53.456  1.00 39.74  ? 422 PRO B CA  1 
ATOM   7617  C C   . PRO B  1 422 ? -25.981  -30.292 -53.854  1.00 39.29  ? 422 PRO B C   1 
ATOM   7618  O O   . PRO B  1 422 ? -25.352  -29.363 -54.371  1.00 39.91  ? 422 PRO B O   1 
ATOM   7619  C CB  . PRO B  1 422 ? -24.526  -31.408 -52.114  1.00 40.06  ? 422 PRO B CB  1 
ATOM   7620  C CG  . PRO B  1 422 ? -23.306  -32.301 -52.257  1.00 40.46  ? 422 PRO B CG  1 
ATOM   7621  C CD  . PRO B  1 422 ? -22.848  -31.970 -53.666  1.00 39.67  ? 422 PRO B CD  1 
ATOM   7622  N N   . GLU B  1 423 ? -27.297  -30.280 -53.587  1.00 40.97  ? 423 GLU B N   1 
ATOM   7623  C CA  . GLU B  1 423 ? -28.235  -29.271 -54.075  1.00 41.53  ? 423 GLU B CA  1 
ATOM   7624  C C   . GLU B  1 423 ? -28.081  -27.937 -53.329  1.00 39.39  ? 423 GLU B C   1 
ATOM   7625  O O   . GLU B  1 423 ? -28.183  -26.894 -53.976  1.00 36.00  ? 423 GLU B O   1 
ATOM   7626  C CB  . GLU B  1 423 ? -29.700  -29.733 -53.969  1.00 43.67  ? 423 GLU B CB  1 
ATOM   7627  C CG  . GLU B  1 423 ? -30.677  -28.764 -54.633  1.00 44.02  ? 423 GLU B CG  1 
ATOM   7628  C CD  . GLU B  1 423 ? -32.154  -29.041 -54.453  1.00 46.02  ? 423 GLU B CD  1 
ATOM   7629  O OE1 . GLU B  1 423 ? -32.556  -30.123 -53.994  1.00 47.32  ? 423 GLU B OE1 1 
ATOM   7630  O OE2 . GLU B  1 423 ? -32.911  -28.108 -54.773  1.00 46.64  ? 423 GLU B OE2 1 
ATOM   7631  N N   . LYS B  1 424 ? -27.802  -28.005 -52.010  1.00 40.65  ? 424 LYS B N   1 
ATOM   7632  C CA  . LYS B  1 424 ? -27.955  -26.893 -51.072  1.00 42.80  ? 424 LYS B CA  1 
ATOM   7633  C C   . LYS B  1 424 ? -26.764  -26.723 -50.124  1.00 39.84  ? 424 LYS B C   1 
ATOM   7634  O O   . LYS B  1 424 ? -26.470  -25.618 -49.659  1.00 38.74  ? 424 LYS B O   1 
ATOM   7635  C CB  . LYS B  1 424 ? -29.179  -27.129 -50.173  1.00 47.14  ? 424 LYS B CB  1 
ATOM   7636  C CG  . LYS B  1 424 ? -30.526  -26.884 -50.848  1.00 53.30  ? 424 LYS B CG  1 
ATOM   7637  C CD  . LYS B  1 424 ? -31.763  -27.058 -49.963  1.00 58.49  ? 424 LYS B CD  1 
ATOM   7638  C CE  . LYS B  1 424 ? -33.046  -27.038 -50.748  1.00 62.01  ? 424 LYS B CE  1 
ATOM   7639  N NZ  . LYS B  1 424 ? -34.118  -27.710 -50.002  1.00 66.71  ? 424 LYS B NZ  1 
ATOM   7640  N N   . ASP B  1 425 ? -26.123  -27.825 -49.745  1.00 38.59  ? 425 ASP B N   1 
ATOM   7641  C CA  . ASP B  1 425 ? -25.087  -27.759 -48.733  1.00 37.47  ? 425 ASP B CA  1 
ATOM   7642  C C   . ASP B  1 425 ? -23.931  -28.632 -49.193  1.00 38.13  ? 425 ASP B C   1 
ATOM   7643  O O   . ASP B  1 425 ? -24.093  -29.853 -49.286  1.00 39.41  ? 425 ASP B O   1 
ATOM   7644  C CB  . ASP B  1 425 ? -25.615  -28.184 -47.373  1.00 37.56  ? 425 ASP B CB  1 
ATOM   7645  C CG  . ASP B  1 425 ? -24.610  -28.080 -46.234  1.00 37.88  ? 425 ASP B CG  1 
ATOM   7646  O OD1 . ASP B  1 425 ? -23.423  -27.841 -46.528  1.00 38.23  ? 425 ASP B OD1 1 
ATOM   7647  O OD2 . ASP B  1 425 ? -25.009  -28.204 -45.057  1.00 38.79  ? 425 ASP B OD2 1 
ATOM   7648  N N   . LEU B  1 426 ? -22.751  -28.021 -49.363  1.00 36.93  ? 426 LEU B N   1 
ATOM   7649  C CA  . LEU B  1 426 ? -21.599  -28.735 -49.908  1.00 38.67  ? 426 LEU B CA  1 
ATOM   7650  C C   . LEU B  1 426 ? -21.054  -29.749 -48.894  1.00 38.96  ? 426 LEU B C   1 
ATOM   7651  O O   . LEU B  1 426 ? -20.245  -30.572 -49.289  1.00 38.08  ? 426 LEU B O   1 
ATOM   7652  C CB  . LEU B  1 426 ? -20.480  -27.826 -50.433  1.00 37.69  ? 426 LEU B CB  1 
ATOM   7653  C CG  . LEU B  1 426 ? -20.882  -26.829 -51.537  1.00 37.79  ? 426 LEU B CG  1 
ATOM   7654  C CD1 . LEU B  1 426 ? -19.753  -25.856 -51.892  1.00 36.55  ? 426 LEU B CD1 1 
ATOM   7655  C CD2 . LEU B  1 426 ? -21.410  -27.543 -52.785  1.00 38.30  ? 426 LEU B CD2 1 
ATOM   7656  N N   . ASN B  1 427 ? -21.526  -29.729 -47.631  1.00 39.63  ? 427 ASN B N   1 
ATOM   7657  C CA  . ASN B  1 427 ? -21.033  -30.657 -46.621  1.00 42.25  ? 427 ASN B CA  1 
ATOM   7658  C C   . ASN B  1 427 ? -21.714  -32.016 -46.744  1.00 43.23  ? 427 ASN B C   1 
ATOM   7659  O O   . ASN B  1 427 ? -21.412  -32.866 -45.923  1.00 43.56  ? 427 ASN B O   1 
ATOM   7660  C CB  . ASN B  1 427 ? -21.190  -30.185 -45.172  1.00 41.48  ? 427 ASN B CB  1 
ATOM   7661  C CG  . ASN B  1 427 ? -20.222  -29.086 -44.793  1.00 40.66  ? 427 ASN B CG  1 
ATOM   7662  O OD1 . ASN B  1 427 ? -19.052  -29.128 -45.183  1.00 38.69  ? 427 ASN B OD1 1 
ATOM   7663  N ND2 . ASN B  1 427 ? -20.692  -28.078 -44.063  1.00 39.38  ? 427 ASN B ND2 1 
ATOM   7664  N N   . GLU B  1 428 ? -22.662  -32.174 -47.689  1.00 45.60  ? 428 GLU B N   1 
ATOM   7665  C CA  . GLU B  1 428 ? -23.401  -33.424 -47.877  1.00 47.24  ? 428 GLU B CA  1 
ATOM   7666  C C   . GLU B  1 428 ? -22.585  -34.387 -48.741  1.00 46.29  ? 428 GLU B C   1 
ATOM   7667  O O   . GLU B  1 428 ? -22.896  -35.570 -48.801  1.00 48.62  ? 428 GLU B O   1 
ATOM   7668  C CB  . GLU B  1 428 ? -24.780  -33.357 -48.554  1.00 50.63  ? 428 GLU B CB  1 
ATOM   7669  C CG  . GLU B  1 428 ? -25.798  -32.361 -47.987  1.00 55.22  ? 428 GLU B CG  1 
ATOM   7670  C CD  . GLU B  1 428 ? -26.456  -32.591 -46.626  1.00 59.92  ? 428 GLU B CD  1 
ATOM   7671  O OE1 . GLU B  1 428 ? -26.182  -33.629 -45.968  1.00 66.60  ? 428 GLU B OE1 1 
ATOM   7672  O OE2 . GLU B  1 428 ? -27.260  -31.706 -46.214  1.00 58.15  ? 428 GLU B OE2 1 
ATOM   7673  N N   . GLY B  1 429 ? -21.545  -33.912 -49.431  1.00 44.60  ? 429 GLY B N   1 
ATOM   7674  C CA  . GLY B  1 429 ? -20.668  -34.853 -50.115  1.00 44.82  ? 429 GLY B CA  1 
ATOM   7675  C C   . GLY B  1 429 ? -19.342  -34.244 -50.546  1.00 43.11  ? 429 GLY B C   1 
ATOM   7676  O O   . GLY B  1 429 ? -19.194  -33.024 -50.606  1.00 42.74  ? 429 GLY B O   1 
ATOM   7677  N N   . LYS B  1 430 ? -18.403  -35.126 -50.894  1.00 43.31  ? 430 LYS B N   1 
ATOM   7678  C CA  . LYS B  1 430 ? -17.092  -34.741 -51.400  1.00 44.02  ? 430 LYS B CA  1 
ATOM   7679  C C   . LYS B  1 430 ? -17.093  -34.658 -52.931  1.00 40.55  ? 430 LYS B C   1 
ATOM   7680  O O   . LYS B  1 430 ? -16.175  -34.082 -53.529  1.00 38.44  ? 430 LYS B O   1 
ATOM   7681  C CB  . LYS B  1 430 ? -16.054  -35.744 -50.875  1.00 49.65  ? 430 LYS B CB  1 
ATOM   7682  C CG  . LYS B  1 430 ? -15.685  -35.641 -49.388  1.00 55.37  ? 430 LYS B CG  1 
ATOM   7683  C CD  . LYS B  1 430 ? -14.660  -36.706 -48.958  1.00 63.73  ? 430 LYS B CD  1 
ATOM   7684  C CE  . LYS B  1 430 ? -14.156  -36.625 -47.528  1.00 66.66  ? 430 LYS B CE  1 
ATOM   7685  N NZ  . LYS B  1 430 ? -13.723  -35.239 -47.260  1.00 67.91  ? 430 LYS B NZ  1 
ATOM   7686  N N   . ILE B  1 431 ? -18.138  -35.227 -53.559  1.00 39.30  ? 431 ILE B N   1 
ATOM   7687  C CA  . ILE B  1 431 ? -18.288  -35.277 -55.010  1.00 37.67  ? 431 ILE B CA  1 
ATOM   7688  C C   . ILE B  1 431 ? -19.572  -34.548 -55.416  1.00 36.18  ? 431 ILE B C   1 
ATOM   7689  O O   . ILE B  1 431 ? -20.603  -34.695 -54.764  1.00 35.82  ? 431 ILE B O   1 
ATOM   7690  C CB  . ILE B  1 431 ? -18.303  -36.736 -55.503  1.00 38.28  ? 431 ILE B CB  1 
ATOM   7691  C CG1 . ILE B  1 431 ? -17.037  -37.485 -55.075  1.00 39.96  ? 431 ILE B CG1 1 
ATOM   7692  C CG2 . ILE B  1 431 ? -18.493  -36.786 -57.009  1.00 37.68  ? 431 ILE B CG2 1 
ATOM   7693  C CD1 . ILE B  1 431 ? -17.016  -38.981 -55.379  1.00 41.25  ? 431 ILE B CD1 1 
ATOM   7694  N N   . ALA B  1 432 ? -19.517  -33.821 -56.539  1.00 35.36  ? 432 ALA B N   1 
ATOM   7695  C CA  . ALA B  1 432 ? -20.682  -33.127 -57.086  1.00 35.18  ? 432 ALA B CA  1 
ATOM   7696  C C   . ALA B  1 432 ? -21.054  -33.675 -58.454  1.00 35.49  ? 432 ALA B C   1 
ATOM   7697  O O   . ALA B  1 432 ? -20.243  -34.342 -59.095  1.00 35.79  ? 432 ALA B O   1 
ATOM   7698  C CB  . ALA B  1 432 ? -20.404  -31.647 -57.178  1.00 34.32  ? 432 ALA B CB  1 
ATOM   7699  N N   . SER B  1 433 ? -22.300  -33.428 -58.873  1.00 36.48  ? 433 SER B N   1 
ATOM   7700  C CA  . SER B  1 433 ? -22.699  -33.664 -60.256  1.00 38.11  ? 433 SER B CA  1 
ATOM   7701  C C   . SER B  1 433 ? -23.547  -32.496 -60.777  1.00 38.16  ? 433 SER B C   1 
ATOM   7702  O O   . SER B  1 433 ? -24.107  -31.728 -60.007  1.00 39.01  ? 433 SER B O   1 
ATOM   7703  C CB  . SER B  1 433 ? -23.414  -34.979 -60.434  1.00 38.73  ? 433 SER B CB  1 
ATOM   7704  O OG  . SER B  1 433 ? -24.775  -34.851 -60.040  1.00 39.20  ? 433 SER B OG  1 
ATOM   7705  N N   . ILE B  1 434 ? -23.607  -32.351 -62.107  1.00 39.50  ? 434 ILE B N   1 
ATOM   7706  C CA  . ILE B  1 434 ? -24.541  -31.452 -62.777  1.00 37.95  ? 434 ILE B CA  1 
ATOM   7707  C C   . ILE B  1 434 ? -25.254  -32.242 -63.873  1.00 38.70  ? 434 ILE B C   1 
ATOM   7708  O O   . ILE B  1 434 ? -24.624  -32.732 -64.806  1.00 37.87  ? 434 ILE B O   1 
ATOM   7709  C CB  . ILE B  1 434 ? -23.846  -30.227 -63.382  1.00 36.06  ? 434 ILE B CB  1 
ATOM   7710  C CG1 . ILE B  1 434 ? -23.150  -29.341 -62.337  1.00 34.95  ? 434 ILE B CG1 1 
ATOM   7711  C CG2 . ILE B  1 434 ? -24.852  -29.421 -64.190  1.00 36.76  ? 434 ILE B CG2 1 
ATOM   7712  C CD1 . ILE B  1 434 ? -22.254  -28.277 -62.939  1.00 33.05  ? 434 ILE B CD1 1 
ATOM   7713  N N   . LYS B  1 435 ? -26.575  -32.367 -63.717  1.00 39.84  ? 435 LYS B N   1 
ATOM   7714  C CA  . LYS B  1 435 ? -27.440  -33.000 -64.690  1.00 39.63  ? 435 LYS B CA  1 
ATOM   7715  C C   . LYS B  1 435 ? -28.058  -31.906 -65.537  1.00 39.80  ? 435 LYS B C   1 
ATOM   7716  O O   . LYS B  1 435 ? -28.759  -31.040 -65.030  1.00 40.00  ? 435 LYS B O   1 
ATOM   7717  C CB  . LYS B  1 435 ? -28.489  -33.810 -63.956  1.00 41.51  ? 435 LYS B CB  1 
ATOM   7718  C CG  . LYS B  1 435 ? -27.925  -35.098 -63.431  1.00 45.41  ? 435 LYS B CG  1 
ATOM   7719  C CD  . LYS B  1 435 ? -28.992  -36.013 -62.844  1.00 48.38  ? 435 LYS B CD  1 
ATOM   7720  C CE  . LYS B  1 435 ? -29.551  -35.408 -61.601  1.00 50.57  ? 435 LYS B CE  1 
ATOM   7721  N NZ  . LYS B  1 435 ? -30.373  -36.414 -60.931  1.00 55.29  ? 435 LYS B NZ  1 
ATOM   7722  N N   . THR B  1 436 ? -27.697  -31.908 -66.817  1.00 40.12  ? 436 THR B N   1 
ATOM   7723  C CA  . THR B  1 436 ? -28.196  -30.928 -67.753  1.00 38.96  ? 436 THR B CA  1 
ATOM   7724  C C   . THR B  1 436 ? -29.386  -31.534 -68.477  1.00 40.39  ? 436 THR B C   1 
ATOM   7725  O O   . THR B  1 436 ? -29.357  -32.727 -68.808  1.00 41.30  ? 436 THR B O   1 
ATOM   7726  C CB  . THR B  1 436 ? -27.084  -30.523 -68.709  1.00 37.70  ? 436 THR B CB  1 
ATOM   7727  O OG1 . THR B  1 436 ? -26.150  -29.916 -67.823  1.00 36.96  ? 436 THR B OG1 1 
ATOM   7728  C CG2 . THR B  1 436 ? -27.558  -29.546 -69.760  1.00 36.49  ? 436 THR B CG2 1 
ATOM   7729  N N   . LYS B  1 437 ? -30.409  -30.682 -68.671  1.00 39.96  ? 437 LYS B N   1 
ATOM   7730  C CA  . LYS B  1 437 ? -31.593  -30.995 -69.446  1.00 42.04  ? 437 LYS B CA  1 
ATOM   7731  C C   . LYS B  1 437 ? -31.839  -29.889 -70.481  1.00 41.13  ? 437 LYS B C   1 
ATOM   7732  O O   . LYS B  1 437 ? -32.074  -28.740 -70.115  1.00 38.54  ? 437 LYS B O   1 
ATOM   7733  C CB  . LYS B  1 437 ? -32.714  -31.169 -68.422  1.00 45.11  ? 437 LYS B CB  1 
ATOM   7734  C CG  . LYS B  1 437 ? -34.045  -31.465 -69.046  1.00 49.16  ? 437 LYS B CG  1 
ATOM   7735  C CD  . LYS B  1 437 ? -35.153  -31.717 -68.039  1.00 53.51  ? 437 LYS B CD  1 
ATOM   7736  C CE  . LYS B  1 437 ? -36.460  -31.759 -68.776  1.00 58.89  ? 437 LYS B CE  1 
ATOM   7737  N NZ  . LYS B  1 437 ? -37.604  -31.908 -67.871  1.00 63.51  ? 437 LYS B NZ  1 
ATOM   7738  N N   . ILE B  1 438 ? -31.801  -30.256 -71.775  1.00 41.50  ? 438 ILE B N   1 
ATOM   7739  C CA  . ILE B  1 438 ? -32.155  -29.343 -72.846  1.00 43.03  ? 438 ILE B CA  1 
ATOM   7740  C C   . ILE B  1 438 ? -33.416  -29.795 -73.576  1.00 46.95  ? 438 ILE B C   1 
ATOM   7741  O O   . ILE B  1 438 ? -33.427  -30.832 -74.257  1.00 49.80  ? 438 ILE B O   1 
ATOM   7742  C CB  . ILE B  1 438 ? -31.016  -29.164 -73.855  1.00 42.72  ? 438 ILE B CB  1 
ATOM   7743  C CG1 . ILE B  1 438 ? -29.707  -28.796 -73.171  1.00 40.88  ? 438 ILE B CG1 1 
ATOM   7744  C CG2 . ILE B  1 438 ? -31.420  -28.127 -74.907  1.00 41.97  ? 438 ILE B CG2 1 
ATOM   7745  C CD1 . ILE B  1 438 ? -28.523  -28.803 -74.116  1.00 40.70  ? 438 ILE B CD1 1 
ATOM   7746  N N   . GLU B  1 439 ? -34.452  -28.947 -73.469  1.00 47.84  ? 439 GLU B N   1 
ATOM   7747  C CA  . GLU B  1 439 ? -35.681  -29.090 -74.231  1.00 47.88  ? 439 GLU B CA  1 
ATOM   7748  C C   . GLU B  1 439 ? -35.515  -28.363 -75.561  1.00 44.64  ? 439 GLU B C   1 
ATOM   7749  O O   . GLU B  1 439 ? -35.235  -27.167 -75.591  1.00 43.86  ? 439 GLU B O   1 
ATOM   7750  C CB  . GLU B  1 439 ? -36.853  -28.522 -73.436  1.00 51.67  ? 439 GLU B CB  1 
ATOM   7751  C CG  . GLU B  1 439 ? -37.243  -29.399 -72.251  1.00 55.13  ? 439 GLU B CG  1 
ATOM   7752  C CD  . GLU B  1 439 ? -38.453  -28.933 -71.469  1.00 57.86  ? 439 GLU B CD  1 
ATOM   7753  O OE1 . GLU B  1 439 ? -38.852  -27.736 -71.475  1.00 60.41  ? 439 GLU B OE1 1 
ATOM   7754  O OE2 . GLU B  1 439 ? -39.010  -29.851 -70.846  1.00 60.32  ? 439 GLU B OE2 1 
ATOM   7755  N N   . THR B  1 440 ? -35.648  -29.110 -76.658  1.00 43.47  ? 440 THR B N   1 
ATOM   7756  C CA  . THR B  1 440 ? -35.337  -28.595 -77.980  1.00 42.63  ? 440 THR B CA  1 
ATOM   7757  C C   . THR B  1 440 ? -36.596  -27.959 -78.544  1.00 43.50  ? 440 THR B C   1 
ATOM   7758  O O   . THR B  1 440 ? -37.699  -28.234 -78.090  1.00 40.48  ? 440 THR B O   1 
ATOM   7759  C CB  . THR B  1 440 ? -34.804  -29.703 -78.894  1.00 41.47  ? 440 THR B CB  1 
ATOM   7760  O OG1 . THR B  1 440 ? -35.770  -30.735 -78.815  1.00 41.25  ? 440 THR B OG1 1 
ATOM   7761  C CG2 . THR B  1 440 ? -33.465  -30.252 -78.436  1.00 40.58  ? 440 THR B CG2 1 
ATOM   7762  N N   . SER B  1 441 ? -36.406  -27.106 -79.547  1.00 45.90  ? 441 SER B N   1 
ATOM   7763  C CA  . SER B  1 441 ? -37.545  -26.522 -80.230  1.00 49.96  ? 441 SER B CA  1 
ATOM   7764  C C   . SER B  1 441 ? -37.247  -26.475 -81.725  1.00 52.81  ? 441 SER B C   1 
ATOM   7765  O O   . SER B  1 441 ? -36.100  -26.271 -82.138  1.00 52.10  ? 441 SER B O   1 
ATOM   7766  C CB  . SER B  1 441 ? -37.906  -25.176 -79.639  1.00 49.87  ? 441 SER B CB  1 
ATOM   7767  O OG  . SER B  1 441 ? -39.167  -24.748 -80.127  1.00 51.71  ? 441 SER B OG  1 
ATOM   7768  N N   . GLU B  1 442 ? -38.300  -26.679 -82.524  1.00 58.55  ? 442 GLU B N   1 
ATOM   7769  C CA  . GLU B  1 442 ? -38.132  -27.194 -83.871  1.00 64.28  ? 442 GLU B CA  1 
ATOM   7770  C C   . GLU B  1 442 ? -37.363  -26.175 -84.701  1.00 61.53  ? 442 GLU B C   1 
ATOM   7771  O O   . GLU B  1 442 ? -36.506  -26.547 -85.500  1.00 61.24  ? 442 GLU B O   1 
ATOM   7772  C CB  . GLU B  1 442 ? -39.483  -27.582 -84.472  1.00 72.48  ? 442 GLU B CB  1 
ATOM   7773  C CG  . GLU B  1 442 ? -39.376  -28.392 -85.762  1.00 77.75  ? 442 GLU B CG  1 
ATOM   7774  C CD  . GLU B  1 442 ? -40.702  -28.458 -86.500  1.00 84.38  ? 442 GLU B CD  1 
ATOM   7775  O OE1 . GLU B  1 442 ? -41.589  -29.280 -86.149  1.00 86.64  ? 442 GLU B OE1 1 
ATOM   7776  O OE2 . GLU B  1 442 ? -40.853  -27.616 -87.414  1.00 81.85  ? 442 GLU B OE2 1 
ATOM   7777  N N   . ASN B  1 443 ? -37.628  -24.888 -84.461  1.00 58.44  ? 443 ASN B N   1 
ATOM   7778  C CA  . ASN B  1 443 ? -37.129  -23.862 -85.361  1.00 61.20  ? 443 ASN B CA  1 
ATOM   7779  C C   . ASN B  1 443 ? -35.692  -23.429 -85.018  1.00 57.34  ? 443 ASN B C   1 
ATOM   7780  O O   . ASN B  1 443 ? -35.061  -22.702 -85.797  1.00 55.57  ? 443 ASN B O   1 
ATOM   7781  C CB  . ASN B  1 443 ? -38.147  -22.725 -85.418  1.00 69.13  ? 443 ASN B CB  1 
ATOM   7782  C CG  . ASN B  1 443 ? -39.548  -23.212 -85.749  1.00 71.31  ? 443 ASN B CG  1 
ATOM   7783  O OD1 . ASN B  1 443 ? -40.535  -22.776 -85.135  1.00 64.66  ? 443 ASN B OD1 1 
ATOM   7784  N ND2 . ASN B  1 443 ? -39.656  -24.083 -86.744  1.00 67.90  ? 443 ASN B ND2 1 
ATOM   7785  N N   . PHE B  1 444 ? -35.161  -23.878 -83.861  1.00 51.32  ? 444 PHE B N   1 
ATOM   7786  C CA  . PHE B  1 444 ? -33.879  -23.421 -83.344  1.00 43.88  ? 444 PHE B CA  1 
ATOM   7787  C C   . PHE B  1 444 ? -32.826  -24.508 -83.500  1.00 43.06  ? 444 PHE B C   1 
ATOM   7788  O O   . PHE B  1 444 ? -33.102  -25.663 -83.210  1.00 43.13  ? 444 PHE B O   1 
ATOM   7789  C CB  . PHE B  1 444 ? -34.078  -23.050 -81.869  1.00 42.19  ? 444 PHE B CB  1 
ATOM   7790  C CG  . PHE B  1 444 ? -35.015  -21.867 -81.722  1.00 40.34  ? 444 PHE B CG  1 
ATOM   7791  C CD1 . PHE B  1 444 ? -36.393  -22.038 -81.775  1.00 41.82  ? 444 PHE B CD1 1 
ATOM   7792  C CD2 . PHE B  1 444 ? -34.509  -20.584 -81.628  1.00 40.03  ? 444 PHE B CD2 1 
ATOM   7793  C CE1 . PHE B  1 444 ? -37.241  -20.953 -81.678  1.00 40.76  ? 444 PHE B CE1 1 
ATOM   7794  C CE2 . PHE B  1 444 ? -35.359  -19.496 -81.574  1.00 39.88  ? 444 PHE B CE2 1 
ATOM   7795  C CZ  . PHE B  1 444 ? -36.724  -19.689 -81.600  1.00 40.67  ? 444 PHE B CZ  1 
ATOM   7796  N N   . THR B  1 445 ? -31.612  -24.101 -83.861  1.00 41.94  ? 445 THR B N   1 
ATOM   7797  C CA  . THR B  1 445 ? -30.485  -25.001 -84.002  1.00 44.40  ? 445 THR B CA  1 
ATOM   7798  C C   . THR B  1 445 ? -29.557  -24.838 -82.807  1.00 45.45  ? 445 THR B C   1 
ATOM   7799  O O   . THR B  1 445 ? -29.176  -23.726 -82.483  1.00 42.02  ? 445 THR B O   1 
ATOM   7800  C CB  . THR B  1 445 ? -29.740  -24.701 -85.299  1.00 43.96  ? 445 THR B CB  1 
ATOM   7801  O OG1 . THR B  1 445 ? -30.742  -25.011 -86.255  1.00 45.35  ? 445 THR B OG1 1 
ATOM   7802  C CG2 . THR B  1 445 ? -28.539  -25.600 -85.539  1.00 45.06  ? 445 THR B CG2 1 
ATOM   7803  N N   . LEU B  1 446 ? -29.185  -25.978 -82.211  1.00 48.80  ? 446 LEU B N   1 
ATOM   7804  C CA  . LEU B  1 446 ? -28.162  -26.068 -81.185  1.00 49.43  ? 446 LEU B CA  1 
ATOM   7805  C C   . LEU B  1 446 ? -26.800  -26.251 -81.841  1.00 48.65  ? 446 LEU B C   1 
ATOM   7806  O O   . LEU B  1 446 ? -26.645  -27.103 -82.700  1.00 49.75  ? 446 LEU B O   1 
ATOM   7807  C CB  . LEU B  1 446 ? -28.476  -27.280 -80.306  1.00 50.67  ? 446 LEU B CB  1 
ATOM   7808  C CG  . LEU B  1 446 ? -29.784  -27.246 -79.518  1.00 49.57  ? 446 LEU B CG  1 
ATOM   7809  C CD1 . LEU B  1 446 ? -29.843  -28.501 -78.671  1.00 49.83  ? 446 LEU B CD1 1 
ATOM   7810  C CD2 . LEU B  1 446 ? -29.912  -26.009 -78.652  1.00 50.18  ? 446 LEU B CD2 1 
ATOM   7811  N N   . LEU B  1 447 ? -25.805  -25.521 -81.351  1.00 49.63  ? 447 LEU B N   1 
ATOM   7812  C CA  . LEU B  1 447 ? -24.493  -25.475 -81.972  1.00 59.96  ? 447 LEU B CA  1 
ATOM   7813  C C   . LEU B  1 447 ? -23.488  -26.287 -81.160  1.00 72.34  ? 447 LEU B C   1 
ATOM   7814  O O   . LEU B  1 447 ? -23.646  -26.453 -79.951  1.00 88.88  ? 447 LEU B O   1 
ATOM   7815  C CB  . LEU B  1 447 ? -24.014  -24.028 -82.108  1.00 56.43  ? 447 LEU B CB  1 
ATOM   7816  C CG  . LEU B  1 447 ? -24.832  -23.133 -83.040  1.00 56.43  ? 447 LEU B CG  1 
ATOM   7817  C CD1 . LEU B  1 447 ? -24.193  -21.742 -83.074  1.00 59.52  ? 447 LEU B CD1 1 
ATOM   7818  C CD2 . LEU B  1 447 ? -24.943  -23.727 -84.438  1.00 56.74  ? 447 LEU B CD2 1 
ATOM   7819  N N   . ASP B  1 448 ? -22.461  -26.789 -81.860  1.00 74.79  ? 448 ASP B N   1 
ATOM   7820  C CA  . ASP B  1 448 ? -21.178  -27.144 -81.263  1.00 76.63  ? 448 ASP B CA  1 
ATOM   7821  C C   . ASP B  1 448 ? -21.413  -27.909 -79.962  1.00 62.73  ? 448 ASP B C   1 
ATOM   7822  O O   . ASP B  1 448 ? -22.126  -28.909 -79.988  1.00 63.78  ? 448 ASP B O   1 
ATOM   7823  C CB  . ASP B  1 448 ? -20.279  -25.922 -81.038  1.00 78.58  ? 448 ASP B CB  1 
ATOM   7824  C CG  . ASP B  1 448 ? -19.859  -25.077 -82.240  1.00 74.42  ? 448 ASP B CG  1 
ATOM   7825  O OD1 . ASP B  1 448 ? -19.540  -25.660 -83.317  1.00 64.44  ? 448 ASP B OD1 1 
ATOM   7826  O OD2 . ASP B  1 448 ? -19.799  -23.829 -82.060  1.00 71.96  ? 448 ASP B OD2 1 
ATOM   7827  N N   . ASP B  1 449 ? -20.890  -27.346 -78.848  1.00 59.76  ? 449 ASP B N   1 
ATOM   7828  C CA  . ASP B  1 449 ? -20.692  -28.049 -77.585  1.00 61.74  ? 449 ASP B CA  1 
ATOM   7829  C C   . ASP B  1 449 ? -21.399  -27.333 -76.434  1.00 53.40  ? 449 ASP B C   1 
ATOM   7830  O O   . ASP B  1 449 ? -21.267  -26.118 -76.232  1.00 47.49  ? 449 ASP B O   1 
ATOM   7831  C CB  . ASP B  1 449 ? -19.228  -28.332 -77.235  1.00 61.37  ? 449 ASP B CB  1 
ATOM   7832  C CG  . ASP B  1 449 ? -18.602  -29.565 -77.889  1.00 63.39  ? 449 ASP B CG  1 
ATOM   7833  O OD1 . ASP B  1 449 ? -19.319  -30.286 -78.628  1.00 57.83  ? 449 ASP B OD1 1 
ATOM   7834  O OD2 . ASP B  1 449 ? -17.385  -29.789 -77.680  1.00 64.83  ? 449 ASP B OD2 1 
ATOM   7835  N N   . LEU B  1 450 ? -22.148  -28.173 -75.701  1.00 49.47  ? 450 LEU B N   1 
ATOM   7836  C CA  . LEU B  1 450 ? -22.547  -27.917 -74.341  1.00 44.75  ? 450 LEU B CA  1 
ATOM   7837  C C   . LEU B  1 450 ? -21.301  -27.716 -73.486  1.00 42.93  ? 450 LEU B C   1 
ATOM   7838  O O   . LEU B  1 450 ? -20.389  -28.546 -73.536  1.00 44.42  ? 450 LEU B O   1 
ATOM   7839  C CB  . LEU B  1 450 ? -23.352  -29.134 -73.922  1.00 44.71  ? 450 LEU B CB  1 
ATOM   7840  C CG  . LEU B  1 450 ? -23.835  -29.123 -72.474  1.00 46.97  ? 450 LEU B CG  1 
ATOM   7841  C CD1 . LEU B  1 450 ? -24.698  -27.921 -72.151  1.00 44.97  ? 450 LEU B CD1 1 
ATOM   7842  C CD2 . LEU B  1 450 ? -24.584  -30.416 -72.216  1.00 52.30  ? 450 LEU B CD2 1 
ATOM   7843  N N   . LYS B  1 451 ? -21.287  -26.612 -72.716  1.00 38.76  ? 451 LYS B N   1 
ATOM   7844  C CA  . LYS B  1 451 ? -20.235  -26.320 -71.753  1.00 38.76  ? 451 LYS B CA  1 
ATOM   7845  C C   . LYS B  1 451 ? -20.773  -26.371 -70.323  1.00 37.31  ? 451 LYS B C   1 
ATOM   7846  O O   . LYS B  1 451 ? -21.912  -25.988 -70.086  1.00 34.81  ? 451 LYS B O   1 
ATOM   7847  C CB  . LYS B  1 451 ? -19.622  -24.959 -72.087  1.00 41.35  ? 451 LYS B CB  1 
ATOM   7848  C CG  . LYS B  1 451 ? -18.994  -24.953 -73.471  1.00 45.75  ? 451 LYS B CG  1 
ATOM   7849  C CD  . LYS B  1 451 ? -17.656  -24.236 -73.483  1.00 51.30  ? 451 LYS B CD  1 
ATOM   7850  C CE  . LYS B  1 451 ? -16.969  -24.311 -74.811  1.00 54.71  ? 451 LYS B CE  1 
ATOM   7851  N NZ  . LYS B  1 451 ? -17.700  -23.430 -75.724  1.00 52.93  ? 451 LYS B NZ  1 
ATOM   7852  N N   . ILE B  1 452 ? -19.949  -26.895 -69.393  1.00 35.71  ? 452 ILE B N   1 
ATOM   7853  C CA  . ILE B  1 452 ? -20.320  -27.124 -68.008  1.00 34.92  ? 452 ILE B CA  1 
ATOM   7854  C C   . ILE B  1 452 ? -19.259  -26.484 -67.125  1.00 34.43  ? 452 ILE B C   1 
ATOM   7855  O O   . ILE B  1 452 ? -18.091  -26.601 -67.431  1.00 36.29  ? 452 ILE B O   1 
ATOM   7856  C CB  . ILE B  1 452 ? -20.361  -28.625 -67.715  1.00 37.19  ? 452 ILE B CB  1 
ATOM   7857  C CG1 . ILE B  1 452 ? -20.916  -29.450 -68.892  1.00 38.83  ? 452 ILE B CG1 1 
ATOM   7858  C CG2 . ILE B  1 452 ? -21.109  -28.892 -66.411  1.00 37.55  ? 452 ILE B CG2 1 
ATOM   7859  C CD1 . ILE B  1 452 ? -22.410  -29.332 -69.109  1.00 39.04  ? 452 ILE B CD1 1 
ATOM   7860  N N   . SER B  1 453 ? -19.640  -25.836 -66.024  1.00 33.92  ? 453 SER B N   1 
ATOM   7861  C CA  . SER B  1 453 ? -18.668  -25.173 -65.176  1.00 32.85  ? 453 SER B CA  1 
ATOM   7862  C C   . SER B  1 453 ? -19.025  -25.411 -63.729  1.00 33.05  ? 453 SER B C   1 
ATOM   7863  O O   . SER B  1 453 ? -20.175  -25.226 -63.372  1.00 31.30  ? 453 SER B O   1 
ATOM   7864  C CB  . SER B  1 453 ? -18.627  -23.714 -65.428  1.00 33.28  ? 453 SER B CB  1 
ATOM   7865  O OG  . SER B  1 453 ? -17.822  -23.085 -64.449  1.00 32.65  ? 453 SER B OG  1 
ATOM   7866  N N   . TYR B  1 454 ? -18.024  -25.828 -62.936  1.00 34.26  ? 454 TYR B N   1 
ATOM   7867  C CA  . TYR B  1 454 ? -18.167  -25.992 -61.491  1.00 33.63  ? 454 TYR B CA  1 
ATOM   7868  C C   . TYR B  1 454 ? -17.125  -25.088 -60.817  1.00 32.29  ? 454 TYR B C   1 
ATOM   7869  O O   . TYR B  1 454 ? -16.055  -25.526 -60.426  1.00 31.87  ? 454 TYR B O   1 
ATOM   7870  C CB  . TYR B  1 454 ? -18.127  -27.478 -61.083  1.00 32.83  ? 454 TYR B CB  1 
ATOM   7871  C CG  . TYR B  1 454 ? -18.657  -27.805 -59.689  1.00 32.55  ? 454 TYR B CG  1 
ATOM   7872  C CD1 . TYR B  1 454 ? -20.017  -27.871 -59.422  1.00 33.12  ? 454 TYR B CD1 1 
ATOM   7873  C CD2 . TYR B  1 454 ? -17.793  -28.111 -58.647  1.00 32.66  ? 454 TYR B CD2 1 
ATOM   7874  C CE1 . TYR B  1 454 ? -20.494  -28.195 -58.158  1.00 34.38  ? 454 TYR B CE1 1 
ATOM   7875  C CE2 . TYR B  1 454 ? -18.252  -28.428 -57.382  1.00 33.29  ? 454 TYR B CE2 1 
ATOM   7876  C CZ  . TYR B  1 454 ? -19.607  -28.466 -57.129  1.00 34.61  ? 454 TYR B CZ  1 
ATOM   7877  O OH  . TYR B  1 454 ? -20.037  -28.773 -55.863  1.00 34.97  ? 454 TYR B OH  1 
ATOM   7878  N N   . ASN B  1 455 ? -17.446  -23.795 -60.712  1.00 32.15  ? 455 ASN B N   1 
ATOM   7879  C CA  . ASN B  1 455 ? -16.452  -22.817 -60.297  1.00 31.52  ? 455 ASN B CA  1 
ATOM   7880  C C   . ASN B  1 455 ? -16.410  -22.727 -58.779  1.00 30.81  ? 455 ASN B C   1 
ATOM   7881  O O   . ASN B  1 455 ? -17.267  -22.126 -58.179  1.00 30.84  ? 455 ASN B O   1 
ATOM   7882  C CB  . ASN B  1 455 ? -16.663  -21.465 -60.957  1.00 31.87  ? 455 ASN B CB  1 
ATOM   7883  C CG  . ASN B  1 455 ? -15.539  -20.526 -60.600  1.00 32.29  ? 455 ASN B CG  1 
ATOM   7884  O OD1 . ASN B  1 455 ? -14.779  -20.792 -59.653  1.00 33.36  ? 455 ASN B OD1 1 
ATOM   7885  N ND2 . ASN B  1 455 ? -15.429  -19.440 -61.340  1.00 30.90  ? 455 ASN B ND2 1 
ATOM   7886  N N   . THR B  1 456 ? -15.359  -23.281 -58.181  1.00 31.02  ? 456 THR B N   1 
ATOM   7887  C CA  . THR B  1 456 ? -15.301  -23.518 -56.755  1.00 30.43  ? 456 THR B CA  1 
ATOM   7888  C C   . THR B  1 456 ? -14.709  -22.323 -56.021  1.00 29.58  ? 456 THR B C   1 
ATOM   7889  O O   . THR B  1 456 ? -14.540  -22.399 -54.810  1.00 30.13  ? 456 THR B O   1 
ATOM   7890  C CB  . THR B  1 456 ? -14.481  -24.785 -56.513  1.00 30.43  ? 456 THR B CB  1 
ATOM   7891  O OG1 . THR B  1 456 ? -13.301  -24.608 -57.293  1.00 28.79  ? 456 THR B OG1 1 
ATOM   7892  C CG2 . THR B  1 456 ? -15.229  -26.028 -56.952  1.00 30.75  ? 456 THR B CG2 1 
ATOM   7893  N N   . HIS B  1 457 ? -14.386  -21.241 -56.737  1.00 30.03  ? 457 HIS B N   1 
ATOM   7894  C CA  . HIS B  1 457 ? -14.044  -19.964 -56.107  1.00 30.03  ? 457 HIS B CA  1 
ATOM   7895  C C   . HIS B  1 457 ? -12.764  -19.991 -55.264  1.00 31.77  ? 457 HIS B C   1 
ATOM   7896  O O   . HIS B  1 457 ? -12.671  -19.246 -54.298  1.00 34.62  ? 457 HIS B O   1 
ATOM   7897  C CB  . HIS B  1 457 ? -15.215  -19.499 -55.242  1.00 28.91  ? 457 HIS B CB  1 
ATOM   7898  C CG  . HIS B  1 457 ? -16.367  -18.958 -56.043  1.00 30.01  ? 457 HIS B CG  1 
ATOM   7899  N ND1 . HIS B  1 457 ? -17.126  -19.726 -56.903  1.00 28.59  ? 457 HIS B ND1 1 
ATOM   7900  C CD2 . HIS B  1 457 ? -16.893  -17.677 -56.098  1.00 28.31  ? 457 HIS B CD2 1 
ATOM   7901  C CE1 . HIS B  1 457 ? -18.050  -18.945 -57.465  1.00 29.01  ? 457 HIS B CE1 1 
ATOM   7902  N NE2 . HIS B  1 457 ? -17.929  -17.702 -56.987  1.00 28.07  ? 457 HIS B NE2 1 
ATOM   7903  N N   . LEU B  1 458 ? -11.807  -20.873 -55.581  1.00 33.02  ? 458 LEU B N   1 
ATOM   7904  C CA  . LEU B  1 458 ? -10.502  -20.876 -54.925  1.00 34.25  ? 458 LEU B CA  1 
ATOM   7905  C C   . LEU B  1 458 ? -9.632   -19.754 -55.507  1.00 34.53  ? 458 LEU B C   1 
ATOM   7906  O O   . LEU B  1 458 ? -9.047   -19.907 -56.581  1.00 33.59  ? 458 LEU B O   1 
ATOM   7907  C CB  . LEU B  1 458 ? -9.824   -22.232 -55.088  1.00 33.52  ? 458 LEU B CB  1 
ATOM   7908  C CG  . LEU B  1 458 ? -10.633  -23.440 -54.599  1.00 33.79  ? 458 LEU B CG  1 
ATOM   7909  C CD1 . LEU B  1 458 ? -9.778   -24.684 -54.697  1.00 34.69  ? 458 LEU B CD1 1 
ATOM   7910  C CD2 . LEU B  1 458 ? -11.181  -23.287 -53.185  1.00 32.97  ? 458 LEU B CD2 1 
ATOM   7911  N N   . GLY B  1 459 ? -9.565   -18.617 -54.804  1.00 33.40  ? 459 GLY B N   1 
ATOM   7912  C CA  . GLY B  1 459 ? -8.926   -17.439 -55.371  1.00 32.93  ? 459 GLY B CA  1 
ATOM   7913  C C   . GLY B  1 459 ? -9.485   -17.167 -56.765  1.00 32.22  ? 459 GLY B C   1 
ATOM   7914  O O   . GLY B  1 459 ? -10.710  -17.128 -56.961  1.00 32.71  ? 459 GLY B O   1 
ATOM   7915  N N   . TRP B  1 460 ? -8.581   -17.039 -57.742  1.00 32.80  ? 460 TRP B N   1 
ATOM   7916  C CA  . TRP B  1 460 ? -8.961   -16.700 -59.108  1.00 33.22  ? 460 TRP B CA  1 
ATOM   7917  C C   . TRP B  1 460 ? -9.139   -17.943 -59.984  1.00 31.24  ? 460 TRP B C   1 
ATOM   7918  O O   . TRP B  1 460 ? -9.642   -17.834 -61.102  1.00 28.84  ? 460 TRP B O   1 
ATOM   7919  C CB  . TRP B  1 460 ? -7.958   -15.732 -59.736  1.00 33.23  ? 460 TRP B CB  1 
ATOM   7920  C CG  . TRP B  1 460 ? -7.865   -14.407 -59.036  1.00 34.90  ? 460 TRP B CG  1 
ATOM   7921  C CD1 . TRP B  1 460 ? -6.824   -13.962 -58.275  1.00 34.61  ? 460 TRP B CD1 1 
ATOM   7922  C CD2 . TRP B  1 460 ? -8.834   -13.333 -59.071  1.00 35.88  ? 460 TRP B CD2 1 
ATOM   7923  N NE1 . TRP B  1 460 ? -7.086   -12.698 -57.824  1.00 36.03  ? 460 TRP B NE1 1 
ATOM   7924  C CE2 . TRP B  1 460 ? -8.303   -12.279 -58.298  1.00 36.20  ? 460 TRP B CE2 1 
ATOM   7925  C CE3 . TRP B  1 460 ? -10.093  -13.158 -59.670  1.00 36.09  ? 460 TRP B CE3 1 
ATOM   7926  C CZ2 . TRP B  1 460 ? -8.987   -11.069 -58.119  1.00 39.03  ? 460 TRP B CZ2 1 
ATOM   7927  C CZ3 . TRP B  1 460 ? -10.777  -11.976 -59.475  1.00 34.27  ? 460 TRP B CZ3 1 
ATOM   7928  C CH2 . TRP B  1 460 ? -10.222  -10.932 -58.731  1.00 36.86  ? 460 TRP B CH2 1 
ATOM   7929  N N   . ALA B  1 461 ? -8.809   -19.125 -59.455  1.00 31.79  ? 461 ALA B N   1 
ATOM   7930  C CA  . ALA B  1 461 ? -8.927   -20.347 -60.233  1.00 33.43  ? 461 ALA B CA  1 
ATOM   7931  C C   . ALA B  1 461 ? -10.398  -20.613 -60.559  1.00 35.18  ? 461 ALA B C   1 
ATOM   7932  O O   . ALA B  1 461 ? -11.287  -20.428 -59.724  1.00 34.54  ? 461 ALA B O   1 
ATOM   7933  C CB  . ALA B  1 461 ? -8.300   -21.522 -59.498  1.00 34.49  ? 461 ALA B CB  1 
ATOM   7934  N N   . ILE B  1 462 ? -10.607  -21.112 -61.780  1.00 36.67  ? 462 ILE B N   1 
ATOM   7935  C CA  . ILE B  1 462 ? -11.907  -21.221 -62.421  1.00 37.59  ? 462 ILE B CA  1 
ATOM   7936  C C   . ILE B  1 462 ? -12.609  -22.515 -62.021  1.00 35.72  ? 462 ILE B C   1 
ATOM   7937  O O   . ILE B  1 462 ? -13.838  -22.610 -62.102  1.00 33.19  ? 462 ILE B O   1 
ATOM   7938  C CB  . ILE B  1 462 ? -11.664  -21.112 -63.940  1.00 41.13  ? 462 ILE B CB  1 
ATOM   7939  C CG1 . ILE B  1 462 ? -11.394  -19.674 -64.289  1.00 43.59  ? 462 ILE B CG1 1 
ATOM   7940  C CG2 . ILE B  1 462 ? -12.799  -21.665 -64.792  1.00 42.64  ? 462 ILE B CG2 1 
ATOM   7941  C CD1 . ILE B  1 462 ? -12.481  -18.717 -63.835  1.00 44.52  ? 462 ILE B CD1 1 
ATOM   7942  N N   . GLY B  1 463 ? -11.822  -23.509 -61.595  1.00 34.97  ? 463 GLY B N   1 
ATOM   7943  C CA  . GLY B  1 463 ? -12.391  -24.796 -61.258  1.00 35.22  ? 463 GLY B CA  1 
ATOM   7944  C C   . GLY B  1 463 ? -12.593  -25.608 -62.529  1.00 36.36  ? 463 GLY B C   1 
ATOM   7945  O O   . GLY B  1 463 ? -12.206  -25.193 -63.610  1.00 36.46  ? 463 GLY B O   1 
ATOM   7946  N N   . SER B  1 464 ? -13.240  -26.758 -62.400  1.00 39.86  ? 464 SER B N   1 
ATOM   7947  C CA  . SER B  1 464 ? -13.397  -27.671 -63.512  1.00 39.28  ? 464 SER B CA  1 
ATOM   7948  C C   . SER B  1 464 ? -14.306  -27.088 -64.592  1.00 37.59  ? 464 SER B C   1 
ATOM   7949  O O   . SER B  1 464 ? -15.235  -26.346 -64.279  1.00 35.38  ? 464 SER B O   1 
ATOM   7950  C CB  . SER B  1 464 ? -13.911  -28.949 -62.978  1.00 40.62  ? 464 SER B CB  1 
ATOM   7951  O OG  . SER B  1 464 ? -12.872  -29.557 -62.238  1.00 43.80  ? 464 SER B OG  1 
ATOM   7952  N N   . GLN B  1 465 ? -13.992  -27.424 -65.852  1.00 37.60  ? 465 GLN B N   1 
ATOM   7953  C CA  . GLN B  1 465 ? -14.892  -27.232 -66.976  1.00 39.11  ? 465 GLN B CA  1 
ATOM   7954  C C   . GLN B  1 465 ? -15.005  -28.546 -67.745  1.00 38.55  ? 465 GLN B C   1 
ATOM   7955  O O   . GLN B  1 465 ? -14.108  -29.363 -67.667  1.00 40.51  ? 465 GLN B O   1 
ATOM   7956  C CB  . GLN B  1 465 ? -14.411  -26.169 -67.958  1.00 37.98  ? 465 GLN B CB  1 
ATOM   7957  C CG  . GLN B  1 465 ? -14.244  -24.792 -67.340  1.00 42.03  ? 465 GLN B CG  1 
ATOM   7958  C CD  . GLN B  1 465 ? -14.090  -23.677 -68.370  1.00 44.12  ? 465 GLN B CD  1 
ATOM   7959  O OE1 . GLN B  1 465 ? -13.004  -23.103 -68.535  1.00 48.88  ? 465 GLN B OE1 1 
ATOM   7960  N NE2 . GLN B  1 465 ? -15.158  -23.364 -69.093  1.00 40.39  ? 465 GLN B NE2 1 
ATOM   7961  N N   . ALA B  1 466 ? -16.097  -28.741 -68.488  1.00 37.46  ? 466 ALA B N   1 
ATOM   7962  C CA  . ALA B  1 466 ? -16.179  -29.814 -69.466  1.00 37.81  ? 466 ALA B CA  1 
ATOM   7963  C C   . ALA B  1 466 ? -16.876  -29.317 -70.732  1.00 39.63  ? 466 ALA B C   1 
ATOM   7964  O O   . ALA B  1 466 ? -17.738  -28.431 -70.666  1.00 38.54  ? 466 ALA B O   1 
ATOM   7965  C CB  . ALA B  1 466 ? -16.900  -30.991 -68.869  1.00 38.49  ? 466 ALA B CB  1 
ATOM   7966  N N   . SER B  1 467 ? -16.443  -29.868 -71.883  1.00 40.15  ? 467 SER B N   1 
ATOM   7967  C CA  . SER B  1 467 ? -17.124  -29.740 -73.163  1.00 40.17  ? 467 SER B CA  1 
ATOM   7968  C C   . SER B  1 467 ? -17.762  -31.074 -73.502  1.00 41.30  ? 467 SER B C   1 
ATOM   7969  O O   . SER B  1 467 ? -17.039  -32.042 -73.641  1.00 43.47  ? 467 SER B O   1 
ATOM   7970  C CB  . SER B  1 467 ? -16.185  -29.339 -74.274  1.00 42.00  ? 467 SER B CB  1 
ATOM   7971  O OG  . SER B  1 467 ? -16.083  -27.928 -74.358  1.00 44.40  ? 467 SER B OG  1 
ATOM   7972  N N   . VAL B  1 468 ? -19.097  -31.109 -73.623  1.00 42.18  ? 468 VAL B N   1 
ATOM   7973  C CA  . VAL B  1 468 ? -19.831  -32.324 -73.945  1.00 42.78  ? 468 VAL B CA  1 
ATOM   7974  C C   . VAL B  1 468 ? -20.452  -32.168 -75.335  1.00 41.20  ? 468 VAL B C   1 
ATOM   7975  O O   . VAL B  1 468 ? -21.191  -31.203 -75.576  1.00 41.27  ? 468 VAL B O   1 
ATOM   7976  C CB  . VAL B  1 468 ? -20.906  -32.656 -72.878  1.00 42.96  ? 468 VAL B CB  1 
ATOM   7977  C CG1 . VAL B  1 468 ? -21.604  -33.974 -73.176  1.00 42.55  ? 468 VAL B CG1 1 
ATOM   7978  C CG2 . VAL B  1 468 ? -20.358  -32.654 -71.446  1.00 42.25  ? 468 VAL B CG2 1 
ATOM   7979  N N   . SER B  1 469 ? -20.124  -33.122 -76.223  1.00 42.11  ? 469 SER B N   1 
ATOM   7980  C CA  . SER B  1 469 ? -20.711  -33.245 -77.551  1.00 45.60  ? 469 SER B CA  1 
ATOM   7981  C C   . SER B  1 469 ? -22.098  -33.858 -77.461  1.00 47.45  ? 469 SER B C   1 
ATOM   7982  O O   . SER B  1 469 ? -22.285  -34.861 -76.792  1.00 47.49  ? 469 SER B O   1 
ATOM   7983  C CB  . SER B  1 469 ? -19.893  -34.083 -78.484  1.00 46.97  ? 469 SER B CB  1 
ATOM   7984  O OG  . SER B  1 469 ? -20.563  -34.172 -79.735  1.00 48.58  ? 469 SER B OG  1 
ATOM   7985  N N   . ILE B  1 470 ? -23.043  -33.253 -78.179  1.00 50.51  ? 470 ILE B N   1 
ATOM   7986  C CA  . ILE B  1 470 ? -24.430  -33.675 -78.158  1.00 52.52  ? 470 ILE B CA  1 
ATOM   7987  C C   . ILE B  1 470 ? -24.892  -33.984 -79.576  1.00 55.52  ? 470 ILE B C   1 
ATOM   7988  O O   . ILE B  1 470 ? -26.079  -34.192 -79.779  1.00 58.18  ? 470 ILE B O   1 
ATOM   7989  C CB  . ILE B  1 470 ? -25.300  -32.571 -77.540  1.00 55.48  ? 470 ILE B CB  1 
ATOM   7990  C CG1 . ILE B  1 470 ? -25.358  -31.307 -78.437  1.00 56.69  ? 470 ILE B CG1 1 
ATOM   7991  C CG2 . ILE B  1 470 ? -24.814  -32.241 -76.132  1.00 56.57  ? 470 ILE B CG2 1 
ATOM   7992  C CD1 . ILE B  1 470 ? -26.436  -30.304 -78.058  1.00 55.39  ? 470 ILE B CD1 1 
ATOM   7993  N N   . SER B  1 471 ? -23.970  -33.956 -80.551  1.00 60.62  ? 471 SER B N   1 
ATOM   7994  C CA  . SER B  1 471 ? -24.236  -34.340 -81.932  1.00 63.80  ? 471 SER B CA  1 
ATOM   7995  C C   . SER B  1 471 ? -25.014  -35.665 -82.004  1.00 63.88  ? 471 SER B C   1 
ATOM   7996  O O   . SER B  1 471 ? -25.942  -35.769 -82.794  1.00 64.84  ? 471 SER B O   1 
ATOM   7997  C CB  . SER B  1 471 ? -22.934  -34.418 -82.704  1.00 66.40  ? 471 SER B CB  1 
ATOM   7998  O OG  . SER B  1 471 ? -22.111  -35.455 -82.174  1.00 68.87  ? 471 SER B OG  1 
ATOM   7999  N N   . ASP B  1 472 ? -24.689  -36.646 -81.143  1.00 60.98  ? 472 ASP B N   1 
ATOM   8000  C CA  . ASP B  1 472 ? -25.345  -37.949 -81.141  1.00 63.64  ? 472 ASP B CA  1 
ATOM   8001  C C   . ASP B  1 472 ? -26.811  -37.902 -80.661  1.00 66.86  ? 472 ASP B C   1 
ATOM   8002  O O   . ASP B  1 472 ? -27.472  -38.942 -80.670  1.00 68.78  ? 472 ASP B O   1 
ATOM   8003  C CB  . ASP B  1 472 ? -24.526  -38.978 -80.363  1.00 62.28  ? 472 ASP B CB  1 
ATOM   8004  C CG  . ASP B  1 472 ? -24.343  -38.770 -78.859  1.00 60.93  ? 472 ASP B CG  1 
ATOM   8005  O OD1 . ASP B  1 472 ? -24.195  -37.619 -78.404  1.00 58.78  ? 472 ASP B OD1 1 
ATOM   8006  O OD2 . ASP B  1 472 ? -24.289  -39.782 -78.137  1.00 64.27  ? 472 ASP B OD2 1 
ATOM   8007  N N   . GLN B  1 473 ? -27.337  -36.716 -80.286  1.00 65.09  ? 473 GLN B N   1 
ATOM   8008  C CA  . GLN B  1 473 ? -28.658  -36.557 -79.677  1.00 60.47  ? 473 GLN B CA  1 
ATOM   8009  C C   . GLN B  1 473 ? -29.489  -35.401 -80.266  1.00 61.00  ? 473 GLN B C   1 
ATOM   8010  O O   . GLN B  1 473 ? -30.533  -35.080 -79.695  1.00 58.20  ? 473 GLN B O   1 
ATOM   8011  C CB  . GLN B  1 473 ? -28.515  -36.147 -78.210  1.00 59.47  ? 473 GLN B CB  1 
ATOM   8012  C CG  . GLN B  1 473 ? -27.905  -37.182 -77.267  1.00 59.24  ? 473 GLN B CG  1 
ATOM   8013  C CD  . GLN B  1 473 ? -28.004  -36.761 -75.806  1.00 56.12  ? 473 GLN B CD  1 
ATOM   8014  O OE1 . GLN B  1 473 ? -29.074  -36.729 -75.185  1.00 52.88  ? 473 GLN B OE1 1 
ATOM   8015  N NE2 . GLN B  1 473 ? -26.871  -36.418 -75.224  1.00 54.05  ? 473 GLN B NE2 1 
ATOM   8016  N N   . LEU B  1 474 ? -29.012  -34.736 -81.316  1.00 61.73  ? 474 LEU B N   1 
ATOM   8017  C CA  . LEU B  1 474 ? -29.674  -33.492 -81.803  1.00 63.03  ? 474 LEU B CA  1 
ATOM   8018  C C   . LEU B  1 474 ? -31.116  -33.722 -82.259  1.00 63.55  ? 474 LEU B C   1 
ATOM   8019  O O   . LEU B  1 474 ? -31.891  -32.748 -82.249  1.00 58.91  ? 474 LEU B O   1 
ATOM   8020  C CB  . LEU B  1 474 ? -28.828  -32.868 -82.909  1.00 64.14  ? 474 LEU B CB  1 
ATOM   8021  C CG  . LEU B  1 474 ? -27.578  -32.119 -82.442  1.00 66.39  ? 474 LEU B CG  1 
ATOM   8022  C CD1 . LEU B  1 474 ? -27.051  -31.216 -83.539  1.00 63.68  ? 474 LEU B CD1 1 
ATOM   8023  C CD2 . LEU B  1 474 ? -27.901  -31.317 -81.202  1.00 64.82  ? 474 LEU B CD2 1 
ATOM   8024  N N   . ASP B  1 475 ? -31.460  -34.953 -82.616  1.00 70.30  ? 475 ASP B N   1 
ATOM   8025  C CA  . ASP B  1 475 ? -32.824  -35.272 -83.117  1.00 75.09  ? 475 ASP B CA  1 
ATOM   8026  C C   . ASP B  1 475 ? -33.815  -35.388 -81.962  1.00 71.49  ? 475 ASP B C   1 
ATOM   8027  O O   . ASP B  1 475 ? -35.020  -35.256 -82.214  1.00 68.12  ? 475 ASP B O   1 
ATOM   8028  C CB  . ASP B  1 475 ? -32.801  -36.556 -83.925  1.00 78.00  ? 475 ASP B CB  1 
ATOM   8029  C CG  . ASP B  1 475 ? -31.967  -37.692 -83.347  1.00 83.98  ? 475 ASP B CG  1 
ATOM   8030  O OD1 . ASP B  1 475 ? -31.460  -37.539 -82.215  1.00 81.35  ? 475 ASP B OD1 1 
ATOM   8031  O OD2 . ASP B  1 475 ? -31.833  -38.725 -84.037  1.00 76.60  ? 475 ASP B OD2 1 
ATOM   8032  N N   . LYS B  1 476 ? -33.326  -35.582 -80.743  1.00 68.51  ? 476 LYS B N   1 
ATOM   8033  C CA  . LYS B  1 476 ? -34.234  -35.838 -79.599  1.00 66.22  ? 476 LYS B CA  1 
ATOM   8034  C C   . LYS B  1 476 ? -34.963  -34.584 -79.119  1.00 60.49  ? 476 LYS B C   1 
ATOM   8035  O O   . LYS B  1 476 ? -34.425  -33.483 -79.285  1.00 57.89  ? 476 LYS B O   1 
ATOM   8036  C CB  . LYS B  1 476 ? -33.440  -36.445 -78.438  1.00 68.65  ? 476 LYS B CB  1 
ATOM   8037  C CG  . LYS B  1 476 ? -32.596  -37.652 -78.785  1.00 74.63  ? 476 LYS B CG  1 
ATOM   8038  C CD  . LYS B  1 476 ? -32.564  -38.653 -77.640  1.00 76.81  ? 476 LYS B CD  1 
ATOM   8039  C CE  . LYS B  1 476 ? -31.202  -38.822 -77.060  1.00 73.69  ? 476 LYS B CE  1 
ATOM   8040  N NZ  . LYS B  1 476 ? -31.228  -38.638 -75.609  1.00 74.22  ? 476 LYS B NZ  1 
ATOM   8041  N N   . LYS B  1 477 ? -36.146  -34.773 -78.548  1.00 58.25  ? 477 LYS B N   1 
ATOM   8042  C CA  . LYS B  1 477 ? -36.919  -33.684 -77.967  1.00 57.85  ? 477 LYS B CA  1 
ATOM   8043  C C   . LYS B  1 477 ? -36.242  -33.171 -76.701  1.00 53.50  ? 477 LYS B C   1 
ATOM   8044  O O   . LYS B  1 477 ? -36.340  -31.976 -76.403  1.00 48.05  ? 477 LYS B O   1 
ATOM   8045  C CB  . LYS B  1 477 ? -38.341  -34.072 -77.557  1.00 61.90  ? 477 LYS B CB  1 
ATOM   8046  C CG  . LYS B  1 477 ? -39.361  -34.162 -78.688  1.00 71.30  ? 477 LYS B CG  1 
ATOM   8047  C CD  . LYS B  1 477 ? -40.758  -34.578 -78.210  1.00 82.27  ? 477 LYS B CD  1 
ATOM   8048  C CE  . LYS B  1 477 ? -41.650  -35.182 -79.267  1.00 88.36  ? 477 LYS B CE  1 
ATOM   8049  N NZ  . LYS B  1 477 ? -41.645  -34.302 -80.441  1.00 92.33  ? 477 LYS B NZ  1 
ATOM   8050  N N   . ILE B  1 478 ? -35.592  -34.106 -75.975  1.00 50.02  ? 478 ILE B N   1 
ATOM   8051  C CA  . ILE B  1 478 ? -34.907  -33.842 -74.722  1.00 46.66  ? 478 ILE B CA  1 
ATOM   8052  C C   . ILE B  1 478 ? -33.494  -34.411 -74.761  1.00 45.39  ? 478 ILE B C   1 
ATOM   8053  O O   . ILE B  1 478 ? -33.281  -35.583 -75.008  1.00 46.28  ? 478 ILE B O   1 
ATOM   8054  C CB  . ILE B  1 478 ? -35.690  -34.426 -73.539  1.00 47.12  ? 478 ILE B CB  1 
ATOM   8055  C CG1 . ILE B  1 478 ? -37.126  -33.862 -73.492  1.00 47.51  ? 478 ILE B CG1 1 
ATOM   8056  C CG2 . ILE B  1 478 ? -34.914  -34.191 -72.241  1.00 46.98  ? 478 ILE B CG2 1 
ATOM   8057  C CD1 . ILE B  1 478 ? -37.952  -34.266 -72.280  1.00 48.85  ? 478 ILE B CD1 1 
ATOM   8058  N N   . ILE B  1 479 ? -32.523  -33.572 -74.431  1.00 44.77  ? 479 ILE B N   1 
ATOM   8059  C CA  . ILE B  1 479 ? -31.120  -33.943 -74.481  1.00 44.11  ? 479 ILE B CA  1 
ATOM   8060  C C   . ILE B  1 479 ? -30.534  -33.797 -73.079  1.00 43.84  ? 479 ILE B C   1 
ATOM   8061  O O   . ILE B  1 479 ? -30.641  -32.721 -72.481  1.00 42.74  ? 479 ILE B O   1 
ATOM   8062  C CB  . ILE B  1 479 ? -30.379  -33.040 -75.482  1.00 43.05  ? 479 ILE B CB  1 
ATOM   8063  C CG1 . ILE B  1 479 ? -30.937  -33.182 -76.901  1.00 43.67  ? 479 ILE B CG1 1 
ATOM   8064  C CG2 . ILE B  1 479 ? -28.870  -33.297 -75.425  1.00 43.87  ? 479 ILE B CG2 1 
ATOM   8065  C CD1 . ILE B  1 479 ? -30.460  -32.116 -77.874  1.00 42.41  ? 479 ILE B CD1 1 
ATOM   8066  N N   . THR B  1 480 ? -29.900  -34.867 -72.569  1.00 43.24  ? 480 THR B N   1 
ATOM   8067  C CA  . THR B  1 480 ? -29.434  -34.877 -71.186  1.00 41.65  ? 480 THR B CA  1 
ATOM   8068  C C   . THR B  1 480 ? -27.931  -35.118 -71.125  1.00 40.39  ? 480 THR B C   1 
ATOM   8069  O O   . THR B  1 480 ? -27.343  -35.694 -72.010  1.00 41.10  ? 480 THR B O   1 
ATOM   8070  C CB  . THR B  1 480 ? -30.180  -35.919 -70.358  1.00 41.35  ? 480 THR B CB  1 
ATOM   8071  O OG1 . THR B  1 480 ? -29.741  -37.146 -70.909  1.00 40.57  ? 480 THR B OG1 1 
ATOM   8072  C CG2 . THR B  1 480 ? -31.683  -35.749 -70.425  1.00 42.41  ? 480 THR B CG2 1 
ATOM   8073  N N   . SER B  1 481 ? -27.318  -34.651 -70.055  1.00 40.37  ? 481 SER B N   1 
ATOM   8074  C CA  . SER B  1 481 ? -25.912  -34.870 -69.826  1.00 41.07  ? 481 SER B CA  1 
ATOM   8075  C C   . SER B  1 481 ? -25.688  -34.918 -68.331  1.00 40.46  ? 481 SER B C   1 
ATOM   8076  O O   . SER B  1 481 ? -26.430  -34.298 -67.589  1.00 41.87  ? 481 SER B O   1 
ATOM   8077  C CB  . SER B  1 481 ? -25.078  -33.798 -70.429  1.00 42.32  ? 481 SER B CB  1 
ATOM   8078  O OG  . SER B  1 481 ? -23.717  -34.150 -70.238  1.00 44.52  ? 481 SER B OG  1 
ATOM   8079  N N   . GLU B  1 482 ? -24.671  -35.664 -67.911  1.00 40.76  ? 482 GLU B N   1 
ATOM   8080  C CA  . GLU B  1 482 ? -24.342  -35.815 -66.508  1.00 39.77  ? 482 GLU B CA  1 
ATOM   8081  C C   . GLU B  1 482 ? -22.831  -35.725 -66.374  1.00 39.68  ? 482 GLU B C   1 
ATOM   8082  O O   . GLU B  1 482 ? -22.125  -36.449 -67.058  1.00 40.39  ? 482 GLU B O   1 
ATOM   8083  C CB  . GLU B  1 482 ? -24.800  -37.177 -66.010  1.00 40.06  ? 482 GLU B CB  1 
ATOM   8084  C CG  . GLU B  1 482 ? -24.580  -37.374 -64.508  1.00 39.93  ? 482 GLU B CG  1 
ATOM   8085  C CD  . GLU B  1 482 ? -25.234  -38.641 -63.957  1.00 39.94  ? 482 GLU B CD  1 
ATOM   8086  O OE1 . GLU B  1 482 ? -25.149  -39.662 -64.659  1.00 40.66  ? 482 GLU B OE1 1 
ATOM   8087  O OE2 . GLU B  1 482 ? -25.825  -38.610 -62.860  1.00 39.74  ? 482 GLU B OE2 1 
ATOM   8088  N N   . ASN B  1 483 ? -22.360  -34.872 -65.465  1.00 38.84  ? 483 ASN B N   1 
ATOM   8089  C CA  . ASN B  1 483 ? -20.945  -34.574 -65.373  1.00 39.38  ? 483 ASN B CA  1 
ATOM   8090  C C   . ASN B  1 483 ? -20.543  -34.463 -63.912  1.00 38.96  ? 483 ASN B C   1 
ATOM   8091  O O   . ASN B  1 483 ? -21.148  -33.695 -63.183  1.00 40.58  ? 483 ASN B O   1 
ATOM   8092  C CB  . ASN B  1 483 ? -20.639  -33.283 -66.108  1.00 39.30  ? 483 ASN B CB  1 
ATOM   8093  C CG  . ASN B  1 483 ? -20.798  -33.434 -67.597  1.00 41.68  ? 483 ASN B CG  1 
ATOM   8094  O OD1 . ASN B  1 483 ? -19.807  -33.697 -68.295  1.00 46.42  ? 483 ASN B OD1 1 
ATOM   8095  N ND2 . ASN B  1 483 ? -22.016  -33.283 -68.092  1.00 41.67  ? 483 ASN B ND2 1 
ATOM   8096  N N   . PHE B  1 484 ? -19.508  -35.197 -63.498  1.00 39.93  ? 484 PHE B N   1 
ATOM   8097  C CA  . PHE B  1 484 ? -19.123  -35.261 -62.092  1.00 39.03  ? 484 PHE B CA  1 
ATOM   8098  C C   . PHE B  1 484 ? -17.898  -34.387 -61.808  1.00 37.93  ? 484 PHE B C   1 
ATOM   8099  O O   . PHE B  1 484 ? -17.061  -34.179 -62.674  1.00 37.46  ? 484 PHE B O   1 
ATOM   8100  C CB  . PHE B  1 484 ? -18.873  -36.734 -61.792  1.00 38.85  ? 484 PHE B CB  1 
ATOM   8101  C CG  . PHE B  1 484 ? -20.104  -37.603 -61.947  1.00 39.63  ? 484 PHE B CG  1 
ATOM   8102  C CD1 . PHE B  1 484 ? -21.057  -37.677 -60.939  1.00 40.04  ? 484 PHE B CD1 1 
ATOM   8103  C CD2 . PHE B  1 484 ? -20.267  -38.413 -63.068  1.00 40.70  ? 484 PHE B CD2 1 
ATOM   8104  C CE1 . PHE B  1 484 ? -22.178  -38.486 -61.082  1.00 40.79  ? 484 PHE B CE1 1 
ATOM   8105  C CE2 . PHE B  1 484 ? -21.370  -39.261 -63.195  1.00 40.75  ? 484 PHE B CE2 1 
ATOM   8106  C CZ  . PHE B  1 484 ? -22.319  -39.299 -62.201  1.00 41.21  ? 484 PHE B CZ  1 
ATOM   8107  N N   . PHE B  1 485 ? -17.790  -33.870 -60.581  1.00 37.93  ? 485 PHE B N   1 
ATOM   8108  C CA  . PHE B  1 485 ? -16.674  -33.017 -60.211  1.00 37.86  ? 485 PHE B CA  1 
ATOM   8109  C C   . PHE B  1 485 ? -16.353  -33.240 -58.747  1.00 38.59  ? 485 PHE B C   1 
ATOM   8110  O O   . PHE B  1 485 ? -17.286  -33.383 -57.957  1.00 38.61  ? 485 PHE B O   1 
ATOM   8111  C CB  . PHE B  1 485 ? -17.009  -31.541 -60.422  1.00 38.58  ? 485 PHE B CB  1 
ATOM   8112  C CG  . PHE B  1 485 ? -17.479  -31.215 -61.831  1.00 39.93  ? 485 PHE B CG  1 
ATOM   8113  C CD1 . PHE B  1 485 ? -16.567  -30.936 -62.840  1.00 40.83  ? 485 PHE B CD1 1 
ATOM   8114  C CD2 . PHE B  1 485 ? -18.836  -31.180 -62.148  1.00 40.52  ? 485 PHE B CD2 1 
ATOM   8115  C CE1 . PHE B  1 485 ? -16.998  -30.588 -64.120  1.00 40.04  ? 485 PHE B CE1 1 
ATOM   8116  C CE2 . PHE B  1 485 ? -19.256  -30.856 -63.435  1.00 39.88  ? 485 PHE B CE2 1 
ATOM   8117  C CZ  . PHE B  1 485 ? -18.338  -30.571 -64.417  1.00 38.63  ? 485 PHE B CZ  1 
ATOM   8118  N N   . ASN B  1 486 ? -15.045  -33.260 -58.412  1.00 38.84  ? 486 ASN B N   1 
ATOM   8119  C CA  . ASN B  1 486 ? -14.600  -33.392 -57.029  1.00 39.42  ? 486 ASN B CA  1 
ATOM   8120  C C   . ASN B  1 486 ? -14.750  -32.032 -56.363  1.00 37.85  ? 486 ASN B C   1 
ATOM   8121  O O   . ASN B  1 486 ? -14.560  -31.030 -57.029  1.00 36.39  ? 486 ASN B O   1 
ATOM   8122  C CB  . ASN B  1 486 ? -13.188  -33.955 -56.910  1.00 40.25  ? 486 ASN B CB  1 
ATOM   8123  C CG  . ASN B  1 486 ? -13.147  -35.439 -57.220  1.00 42.20  ? 486 ASN B CG  1 
ATOM   8124  O OD1 . ASN B  1 486 ? -12.520  -35.841 -58.205  1.00 44.18  ? 486 ASN B OD1 1 
ATOM   8125  N ND2 . ASN B  1 486 ? -13.795  -36.284 -56.423  1.00 42.40  ? 486 ASN B ND2 1 
ATOM   8126  N N   . ILE B  1 487 ? -15.173  -32.021 -55.084  1.00 38.33  ? 487 ILE B N   1 
ATOM   8127  C CA  . ILE B  1 487 ? -15.414  -30.784 -54.359  1.00 37.58  ? 487 ILE B CA  1 
ATOM   8128  C C   . ILE B  1 487 ? -14.252  -30.570 -53.395  1.00 37.45  ? 487 ILE B C   1 
ATOM   8129  O O   . ILE B  1 487 ? -14.064  -31.354 -52.471  1.00 38.26  ? 487 ILE B O   1 
ATOM   8130  C CB  . ILE B  1 487 ? -16.751  -30.817 -53.596  1.00 37.36  ? 487 ILE B CB  1 
ATOM   8131  C CG1 . ILE B  1 487 ? -17.947  -31.044 -54.494  1.00 36.79  ? 487 ILE B CG1 1 
ATOM   8132  C CG2 . ILE B  1 487 ? -16.914  -29.544 -52.768  1.00 37.07  ? 487 ILE B CG2 1 
ATOM   8133  C CD1 . ILE B  1 487 ? -19.246  -31.229 -53.717  1.00 37.25  ? 487 ILE B CD1 1 
ATOM   8134  N N   . PRO B  1 488 ? -13.431  -29.516 -53.552  1.00 36.52  ? 488 PRO B N   1 
ATOM   8135  C CA  . PRO B  1 488 ? -12.330  -29.311 -52.623  1.00 36.84  ? 488 PRO B CA  1 
ATOM   8136  C C   . PRO B  1 488 ? -12.858  -29.090 -51.199  1.00 38.87  ? 488 PRO B C   1 
ATOM   8137  O O   . PRO B  1 488 ? -13.913  -28.504 -50.987  1.00 39.16  ? 488 PRO B O   1 
ATOM   8138  C CB  . PRO B  1 488 ? -11.564  -28.107 -53.203  1.00 35.10  ? 488 PRO B CB  1 
ATOM   8139  C CG  . PRO B  1 488 ? -12.074  -27.930 -54.609  1.00 34.67  ? 488 PRO B CG  1 
ATOM   8140  C CD  . PRO B  1 488 ? -13.489  -28.493 -54.611  1.00 36.21  ? 488 PRO B CD  1 
ATOM   8141  N N   . ASP B  1 489 ? -12.119  -29.599 -50.208  1.00 41.71  ? 489 ASP B N   1 
ATOM   8142  C CA  . ASP B  1 489 ? -12.434  -29.398 -48.806  1.00 42.16  ? 489 ASP B CA  1 
ATOM   8143  C C   . ASP B  1 489 ? -12.631  -27.909 -48.520  1.00 41.75  ? 489 ASP B C   1 
ATOM   8144  O O   . ASP B  1 489 ? -13.501  -27.571 -47.727  1.00 43.26  ? 489 ASP B O   1 
ATOM   8145  C CB  . ASP B  1 489 ? -11.408  -30.086 -47.917  1.00 42.44  ? 489 ASP B CB  1 
ATOM   8146  C CG  . ASP B  1 489 ? -11.534  -31.606 -47.867  1.00 44.97  ? 489 ASP B CG  1 
ATOM   8147  O OD1 . ASP B  1 489 ? -12.576  -32.121 -48.336  1.00 44.46  ? 489 ASP B OD1 1 
ATOM   8148  O OD2 . ASP B  1 489 ? -10.588  -32.273 -47.378  1.00 44.45  ? 489 ASP B OD2 1 
ATOM   8149  N N   . ASN B  1 490 ? -11.833  -27.042 -49.156  1.00 40.31  ? 490 ASN B N   1 
ATOM   8150  C CA  . ASN B  1 490 ? -11.816  -25.614 -48.856  1.00 39.30  ? 490 ASN B CA  1 
ATOM   8151  C C   . ASN B  1 490 ? -12.585  -24.789 -49.895  1.00 37.30  ? 490 ASN B C   1 
ATOM   8152  O O   . ASN B  1 490 ? -12.298  -23.625 -50.059  1.00 37.26  ? 490 ASN B O   1 
ATOM   8153  C CB  . ASN B  1 490 ? -10.381  -25.128 -48.732  1.00 38.57  ? 490 ASN B CB  1 
ATOM   8154  C CG  . ASN B  1 490 ? -9.655   -25.227 -50.048  1.00 39.52  ? 490 ASN B CG  1 
ATOM   8155  O OD1 . ASN B  1 490 ? -9.837   -26.208 -50.790  1.00 39.51  ? 490 ASN B OD1 1 
ATOM   8156  N ND2 . ASN B  1 490 ? -8.839   -24.225 -50.353  1.00 37.87  ? 490 ASN B ND2 1 
ATOM   8157  N N   . CYS B  1 491 ? -13.529  -25.404 -50.616  1.00 37.53  ? 491 CYS B N   1 
ATOM   8158  C CA  . CYS B  1 491 ? -14.527  -24.718 -51.415  1.00 35.78  ? 491 CYS B CA  1 
ATOM   8159  C C   . CYS B  1 491 ? -15.658  -24.308 -50.491  1.00 36.14  ? 491 CYS B C   1 
ATOM   8160  O O   . CYS B  1 491 ? -16.278  -25.173 -49.868  1.00 37.02  ? 491 CYS B O   1 
ATOM   8161  C CB  . CYS B  1 491 ? -15.177  -25.637 -52.438  1.00 36.32  ? 491 CYS B CB  1 
ATOM   8162  S SG  . CYS B  1 491 ? -16.466  -24.818 -53.411  1.00 34.76  ? 491 CYS B SG  1 
ATOM   8163  N N   . TRP B  1 492 ? -15.892  -22.992 -50.393  1.00 35.08  ? 492 TRP B N   1 
ATOM   8164  C CA  . TRP B  1 492 ? -16.868  -22.462 -49.463  1.00 35.10  ? 492 TRP B CA  1 
ATOM   8165  C C   . TRP B  1 492 ? -18.165  -22.159 -50.206  1.00 34.53  ? 492 TRP B C   1 
ATOM   8166  O O   . TRP B  1 492 ? -19.273  -22.190 -49.644  1.00 34.09  ? 492 TRP B O   1 
ATOM   8167  C CB  . TRP B  1 492 ? -16.302  -21.215 -48.764  1.00 35.80  ? 492 TRP B CB  1 
ATOM   8168  C CG  . TRP B  1 492 ? -14.918  -21.394 -48.188  1.00 33.58  ? 492 TRP B CG  1 
ATOM   8169  C CD1 . TRP B  1 492 ? -13.874  -20.558 -48.434  1.00 33.36  ? 492 TRP B CD1 1 
ATOM   8170  C CD2 . TRP B  1 492 ? -14.430  -22.388 -47.269  1.00 33.36  ? 492 TRP B CD2 1 
ATOM   8171  N NE1 . TRP B  1 492 ? -12.766  -20.966 -47.745  1.00 33.75  ? 492 TRP B NE1 1 
ATOM   8172  C CE2 . TRP B  1 492 ? -13.069  -22.089 -47.028  1.00 34.63  ? 492 TRP B CE2 1 
ATOM   8173  C CE3 . TRP B  1 492 ? -14.982  -23.505 -46.634  1.00 34.95  ? 492 TRP B CE3 1 
ATOM   8174  C CZ2 . TRP B  1 492 ? -12.259  -22.866 -46.194  1.00 35.18  ? 492 TRP B CZ2 1 
ATOM   8175  C CZ3 . TRP B  1 492 ? -14.187  -24.291 -45.829  1.00 34.98  ? 492 TRP B CZ3 1 
ATOM   8176  C CH2 . TRP B  1 492 ? -12.845  -23.963 -45.602  1.00 35.97  ? 492 TRP B CH2 1 
ATOM   8177  N N   . VAL B  1 493 ? -18.011  -21.880 -51.498  1.00 33.86  ? 493 VAL B N   1 
ATOM   8178  C CA  . VAL B  1 493 ? -19.156  -21.615 -52.349  1.00 33.18  ? 493 VAL B CA  1 
ATOM   8179  C C   . VAL B  1 493 ? -18.773  -22.036 -53.762  1.00 31.56  ? 493 VAL B C   1 
ATOM   8180  O O   . VAL B  1 493 ? -17.605  -21.896 -54.129  1.00 30.56  ? 493 VAL B O   1 
ATOM   8181  C CB  . VAL B  1 493 ? -19.588  -20.129 -52.291  1.00 32.56  ? 493 VAL B CB  1 
ATOM   8182  C CG1 . VAL B  1 493 ? -18.427  -19.193 -52.574  1.00 31.45  ? 493 VAL B CG1 1 
ATOM   8183  C CG2 . VAL B  1 493 ? -20.751  -19.830 -53.247  1.00 32.81  ? 493 VAL B CG2 1 
ATOM   8184  N N   . VAL B  1 494 ? -19.766  -22.554 -54.511  1.00 31.26  ? 494 VAL B N   1 
ATOM   8185  C CA  . VAL B  1 494 ? -19.609  -22.884 -55.920  1.00 30.55  ? 494 VAL B CA  1 
ATOM   8186  C C   . VAL B  1 494 ? -20.663  -22.155 -56.761  1.00 30.38  ? 494 VAL B C   1 
ATOM   8187  O O   . VAL B  1 494 ? -21.797  -21.970 -56.326  1.00 29.89  ? 494 VAL B O   1 
ATOM   8188  C CB  . VAL B  1 494 ? -19.655  -24.407 -56.150  1.00 30.59  ? 494 VAL B CB  1 
ATOM   8189  C CG1 . VAL B  1 494 ? -21.015  -25.026 -55.838  1.00 32.41  ? 494 VAL B CG1 1 
ATOM   8190  C CG2 . VAL B  1 494 ? -19.246  -24.749 -57.573  1.00 30.51  ? 494 VAL B CG2 1 
ATOM   8191  N N   . ASN B  1 495 ? -20.252  -21.725 -57.962  1.00 29.71  ? 495 ASN B N   1 
ATOM   8192  C CA  . ASN B  1 495 ? -21.164  -21.429 -59.053  1.00 30.05  ? 495 ASN B CA  1 
ATOM   8193  C C   . ASN B  1 495 ? -21.151  -22.587 -60.054  1.00 29.25  ? 495 ASN B C   1 
ATOM   8194  O O   . ASN B  1 495 ? -20.170  -22.818 -60.759  1.00 27.35  ? 495 ASN B O   1 
ATOM   8195  C CB  . ASN B  1 495 ? -20.783  -20.138 -59.765  1.00 29.07  ? 495 ASN B CB  1 
ATOM   8196  C CG  . ASN B  1 495 ? -21.830  -19.675 -60.746  1.00 29.06  ? 495 ASN B CG  1 
ATOM   8197  O OD1 . ASN B  1 495 ? -22.421  -20.466 -61.476  1.00 29.03  ? 495 ASN B OD1 1 
ATOM   8198  N ND2 . ASN B  1 495 ? -22.060  -18.376 -60.807  1.00 30.48  ? 495 ASN B ND2 1 
ATOM   8199  N N   . ALA B  1 496 ? -22.288  -23.267 -60.155  1.00 29.74  ? 496 ALA B N   1 
ATOM   8200  C CA  . ALA B  1 496 ? -22.406  -24.409 -61.033  1.00 30.09  ? 496 ALA B CA  1 
ATOM   8201  C C   . ALA B  1 496 ? -23.319  -24.005 -62.171  1.00 29.97  ? 496 ALA B C   1 
ATOM   8202  O O   . ALA B  1 496 ? -24.406  -23.517 -61.918  1.00 31.49  ? 496 ALA B O   1 
ATOM   8203  C CB  . ALA B  1 496 ? -22.883  -25.601 -60.257  1.00 30.32  ? 496 ALA B CB  1 
ATOM   8204  N N   . SER B  1 497 ? -22.842  -24.152 -63.408  1.00 30.88  ? 497 SER B N   1 
ATOM   8205  C CA  . SER B  1 497 ? -23.572  -23.688 -64.572  1.00 31.26  ? 497 SER B CA  1 
ATOM   8206  C C   . SER B  1 497 ? -23.294  -24.574 -65.793  1.00 33.14  ? 497 SER B C   1 
ATOM   8207  O O   . SER B  1 497 ? -22.355  -25.361 -65.827  1.00 33.84  ? 497 SER B O   1 
ATOM   8208  C CB  . SER B  1 497 ? -23.250  -22.250 -64.843  1.00 29.21  ? 497 SER B CB  1 
ATOM   8209  O OG  . SER B  1 497 ? -21.872  -22.146 -65.119  1.00 27.64  ? 497 SER B OG  1 
ATOM   8210  N N   . ALA B  1 498 ? -24.188  -24.453 -66.780  1.00 34.93  ? 498 ALA B N   1 
ATOM   8211  C CA  . ALA B  1 498 ? -24.108  -25.114 -68.072  1.00 34.68  ? 498 ALA B CA  1 
ATOM   8212  C C   . ALA B  1 498 ? -24.785  -24.225 -69.107  1.00 34.16  ? 498 ALA B C   1 
ATOM   8213  O O   . ALA B  1 498 ? -25.762  -23.573 -68.779  1.00 36.39  ? 498 ALA B O   1 
ATOM   8214  C CB  . ALA B  1 498 ? -24.781  -26.455 -68.018  1.00 34.60  ? 498 ALA B CB  1 
ATOM   8215  N N   . GLY B  1 499 ? -24.269  -24.197 -70.337  1.00 34.12  ? 499 GLY B N   1 
ATOM   8216  C CA  . GLY B  1 499 ? -24.892  -23.454 -71.423  1.00 32.88  ? 499 GLY B CA  1 
ATOM   8217  C C   . GLY B  1 499 ? -24.474  -23.989 -72.791  1.00 32.91  ? 499 GLY B C   1 
ATOM   8218  O O   . GLY B  1 499 ? -23.506  -24.730 -72.927  1.00 32.01  ? 499 GLY B O   1 
ATOM   8219  N N   . ILE B  1 500 ? -25.202  -23.548 -73.815  1.00 34.29  ? 500 ILE B N   1 
ATOM   8220  C CA  . ILE B  1 500 ? -24.963  -23.937 -75.196  1.00 35.98  ? 500 ILE B CA  1 
ATOM   8221  C C   . ILE B  1 500 ? -25.478  -22.820 -76.107  1.00 37.41  ? 500 ILE B C   1 
ATOM   8222  O O   . ILE B  1 500 ? -26.511  -22.209 -75.794  1.00 39.53  ? 500 ILE B O   1 
ATOM   8223  C CB  . ILE B  1 500 ? -25.604  -25.310 -75.507  1.00 35.06  ? 500 ILE B CB  1 
ATOM   8224  C CG1 . ILE B  1 500 ? -25.020  -25.908 -76.801  1.00 37.29  ? 500 ILE B CG1 1 
ATOM   8225  C CG2 . ILE B  1 500 ? -27.131  -25.262 -75.533  1.00 33.86  ? 500 ILE B CG2 1 
ATOM   8226  C CD1 . ILE B  1 500 ? -25.606  -27.271 -77.193  1.00 38.73  ? 500 ILE B CD1 1 
ATOM   8227  N N   . SER B  1 501 ? -24.764  -22.583 -77.228  1.00 35.94  ? 501 SER B N   1 
ATOM   8228  C CA  . SER B  1 501 ? -25.198  -21.637 -78.246  1.00 35.38  ? 501 SER B CA  1 
ATOM   8229  C C   . SER B  1 501 ? -26.390  -22.174 -79.043  1.00 36.50  ? 501 SER B C   1 
ATOM   8230  O O   . SER B  1 501 ? -26.606  -23.396 -79.123  1.00 36.35  ? 501 SER B O   1 
ATOM   8231  C CB  . SER B  1 501 ? -24.077  -21.261 -79.128  1.00 35.81  ? 501 SER B CB  1 
ATOM   8232  O OG  . SER B  1 501 ? -23.020  -20.774 -78.318  1.00 36.85  ? 501 SER B OG  1 
ATOM   8233  N N   . VAL B  1 502 ? -27.187  -21.227 -79.562  1.00 34.14  ? 502 VAL B N   1 
ATOM   8234  C CA  . VAL B  1 502 ? -28.409  -21.484 -80.317  1.00 36.57  ? 502 VAL B CA  1 
ATOM   8235  C C   . VAL B  1 502 ? -28.527  -20.476 -81.463  1.00 37.25  ? 502 VAL B C   1 
ATOM   8236  O O   . VAL B  1 502 ? -28.251  -19.285 -81.286  1.00 36.54  ? 502 VAL B O   1 
ATOM   8237  C CB  . VAL B  1 502 ? -29.631  -21.361 -79.396  1.00 37.82  ? 502 VAL B CB  1 
ATOM   8238  C CG1 . VAL B  1 502 ? -30.910  -21.767 -80.101  1.00 40.66  ? 502 VAL B CG1 1 
ATOM   8239  C CG2 . VAL B  1 502 ? -29.451  -22.161 -78.120  1.00 40.45  ? 502 VAL B CG2 1 
ATOM   8240  N N   . ARG B  1 503 ? -28.976  -20.939 -82.632  1.00 37.81  ? 503 ARG B N   1 
ATOM   8241  C CA  . ARG B  1 503 ? -29.137  -20.065 -83.786  1.00 38.65  ? 503 ARG B CA  1 
ATOM   8242  C C   . ARG B  1 503 ? -30.584  -20.072 -84.270  1.00 36.93  ? 503 ARG B C   1 
ATOM   8243  O O   . ARG B  1 503 ? -31.208  -21.138 -84.341  1.00 35.54  ? 503 ARG B O   1 
ATOM   8244  C CB  . ARG B  1 503 ? -28.262  -20.509 -84.965  1.00 43.79  ? 503 ARG B CB  1 
ATOM   8245  C CG  . ARG B  1 503 ? -28.350  -19.648 -86.221  1.00 46.44  ? 503 ARG B CG  1 
ATOM   8246  C CD  . ARG B  1 503 ? -27.622  -20.304 -87.413  1.00 51.68  ? 503 ARG B CD  1 
ATOM   8247  N NE  . ARG B  1 503 ? -26.170  -20.327 -87.183  1.00 55.80  ? 503 ARG B NE  1 
ATOM   8248  C CZ  . ARG B  1 503 ? -25.339  -19.263 -87.158  1.00 57.99  ? 503 ARG B CZ  1 
ATOM   8249  N NH1 . ARG B  1 503 ? -25.736  -18.051 -87.562  1.00 59.37  ? 503 ARG B NH1 1 
ATOM   8250  N NH2 . ARG B  1 503 ? -24.085  -19.424 -86.749  1.00 55.42  ? 503 ARG B NH2 1 
ATOM   8251  N N   . TYR B  1 504 ? -31.086  -18.869 -84.621  1.00 34.52  ? 504 TYR B N   1 
ATOM   8252  C CA  . TYR B  1 504 ? -32.264  -18.695 -85.470  1.00 32.04  ? 504 TYR B CA  1 
ATOM   8253  C C   . TYR B  1 504 ? -31.855  -17.672 -86.523  1.00 31.70  ? 504 TYR B C   1 
ATOM   8254  O O   . TYR B  1 504 ? -31.556  -16.530 -86.175  1.00 32.59  ? 504 TYR B O   1 
ATOM   8255  C CB  . TYR B  1 504 ? -33.501  -18.252 -84.665  1.00 31.29  ? 504 TYR B CB  1 
ATOM   8256  C CG  . TYR B  1 504 ? -34.802  -18.206 -85.445  1.00 31.92  ? 504 TYR B CG  1 
ATOM   8257  C CD1 . TYR B  1 504 ? -35.126  -17.137 -86.262  1.00 32.02  ? 504 TYR B CD1 1 
ATOM   8258  C CD2 . TYR B  1 504 ? -35.692  -19.281 -85.425  1.00 33.29  ? 504 TYR B CD2 1 
ATOM   8259  C CE1 . TYR B  1 504 ? -36.294  -17.133 -87.021  1.00 33.10  ? 504 TYR B CE1 1 
ATOM   8260  C CE2 . TYR B  1 504 ? -36.864  -19.275 -86.163  1.00 33.40  ? 504 TYR B CE2 1 
ATOM   8261  C CZ  . TYR B  1 504 ? -37.185  -18.202 -86.971  1.00 33.68  ? 504 TYR B CZ  1 
ATOM   8262  O OH  . TYR B  1 504 ? -38.383  -18.208 -87.691  1.00 33.80  ? 504 TYR B OH  1 
ATOM   8263  N N   . GLY B  1 505 ? -31.762  -18.093 -87.784  1.00 31.13  ? 505 GLY B N   1 
ATOM   8264  C CA  . GLY B  1 505 ? -31.298  -17.228 -88.850  1.00 31.15  ? 505 GLY B CA  1 
ATOM   8265  C C   . GLY B  1 505 ? -29.894  -16.709 -88.550  1.00 30.93  ? 505 GLY B C   1 
ATOM   8266  O O   . GLY B  1 505 ? -28.993  -17.474 -88.289  1.00 30.39  ? 505 GLY B O   1 
ATOM   8267  N N   . LYS B  1 506 ? -29.732  -15.392 -88.498  1.00 32.02  ? 506 LYS B N   1 
ATOM   8268  C CA  . LYS B  1 506 ? -28.450  -14.795 -88.171  1.00 31.05  ? 506 LYS B CA  1 
ATOM   8269  C C   . LYS B  1 506 ? -28.311  -14.505 -86.683  1.00 30.54  ? 506 LYS B C   1 
ATOM   8270  O O   . LYS B  1 506 ? -27.248  -14.027 -86.261  1.00 32.86  ? 506 LYS B O   1 
ATOM   8271  C CB  . LYS B  1 506 ? -28.263  -13.494 -88.944  1.00 31.15  ? 506 LYS B CB  1 
ATOM   8272  C CG  . LYS B  1 506 ? -28.324  -13.603 -90.470  1.00 32.71  ? 506 LYS B CG  1 
ATOM   8273  C CD  . LYS B  1 506 ? -28.226  -12.202 -91.073  1.00 34.77  ? 506 LYS B CD  1 
ATOM   8274  C CE  . LYS B  1 506 ? -28.596  -12.134 -92.516  1.00 35.73  ? 506 LYS B CE  1 
ATOM   8275  N NZ  . LYS B  1 506 ? -28.182  -10.849 -93.067  1.00 34.83  ? 506 LYS B NZ  1 
ATOM   8276  N N   . PHE B  1 507 ? -29.334  -14.849 -85.889  1.00 30.60  ? 507 PHE B N   1 
ATOM   8277  C CA  . PHE B  1 507 ? -29.370  -14.517 -84.465  1.00 30.19  ? 507 PHE B CA  1 
ATOM   8278  C C   . PHE B  1 507 ? -28.915  -15.688 -83.587  1.00 32.45  ? 507 PHE B C   1 
ATOM   8279  O O   . PHE B  1 507 ? -29.637  -16.671 -83.441  1.00 34.17  ? 507 PHE B O   1 
ATOM   8280  C CB  . PHE B  1 507 ? -30.830  -14.186 -84.172  1.00 29.55  ? 507 PHE B CB  1 
ATOM   8281  C CG  . PHE B  1 507 ? -31.117  -13.741 -82.749  1.00 28.52  ? 507 PHE B CG  1 
ATOM   8282  C CD1 . PHE B  1 507 ? -31.380  -14.680 -81.754  1.00 28.00  ? 507 PHE B CD1 1 
ATOM   8283  C CD2 . PHE B  1 507 ? -31.135  -12.379 -82.428  1.00 27.56  ? 507 PHE B CD2 1 
ATOM   8284  C CE1 . PHE B  1 507 ? -31.639  -14.272 -80.458  1.00 27.75  ? 507 PHE B CE1 1 
ATOM   8285  C CE2 . PHE B  1 507 ? -31.412  -11.974 -81.138  1.00 27.09  ? 507 PHE B CE2 1 
ATOM   8286  C CZ  . PHE B  1 507 ? -31.660  -12.916 -80.155  1.00 27.62  ? 507 PHE B CZ  1 
ATOM   8287  N N   . THR B  1 508 ? -27.735  -15.571 -82.988  1.00 32.71  ? 508 THR B N   1 
ATOM   8288  C CA  . THR B  1 508 ? -27.170  -16.592 -82.121  1.00 35.71  ? 508 THR B CA  1 
ATOM   8289  C C   . THR B  1 508 ? -27.182  -16.082 -80.679  1.00 34.91  ? 508 THR B C   1 
ATOM   8290  O O   . THR B  1 508 ? -26.862  -14.933 -80.434  1.00 36.19  ? 508 THR B O   1 
ATOM   8291  C CB  . THR B  1 508 ? -25.733  -16.914 -82.566  1.00 38.50  ? 508 THR B CB  1 
ATOM   8292  O OG1 . THR B  1 508 ? -25.031  -15.677 -82.651  1.00 41.07  ? 508 THR B OG1 1 
ATOM   8293  C CG2 . THR B  1 508 ? -25.646  -17.541 -83.942  1.00 39.37  ? 508 THR B CG2 1 
ATOM   8294  N N   . PHE B  1 509 ? -27.513  -16.947 -79.721  1.00 35.21  ? 509 PHE B N   1 
ATOM   8295  C CA  . PHE B  1 509 ? -27.531  -16.584 -78.314  1.00 34.78  ? 509 PHE B CA  1 
ATOM   8296  C C   . PHE B  1 509 ? -27.267  -17.827 -77.460  1.00 36.17  ? 509 PHE B C   1 
ATOM   8297  O O   . PHE B  1 509 ? -27.094  -18.912 -77.999  1.00 38.22  ? 509 PHE B O   1 
ATOM   8298  C CB  . PHE B  1 509 ? -28.913  -16.008 -78.014  1.00 35.22  ? 509 PHE B CB  1 
ATOM   8299  C CG  . PHE B  1 509 ? -30.074  -16.985 -78.163  1.00 34.01  ? 509 PHE B CG  1 
ATOM   8300  C CD1 . PHE B  1 509 ? -30.557  -17.336 -79.419  1.00 35.94  ? 509 PHE B CD1 1 
ATOM   8301  C CD2 . PHE B  1 509 ? -30.727  -17.493 -77.055  1.00 34.56  ? 509 PHE B CD2 1 
ATOM   8302  C CE1 . PHE B  1 509 ? -31.672  -18.163 -79.566  1.00 36.08  ? 509 PHE B CE1 1 
ATOM   8303  C CE2 . PHE B  1 509 ? -31.839  -18.333 -77.204  1.00 36.46  ? 509 PHE B CE2 1 
ATOM   8304  C CZ  . PHE B  1 509 ? -32.312  -18.661 -78.457  1.00 35.93  ? 509 PHE B CZ  1 
ATOM   8305  N N   . LYS B  1 510 ? -27.272  -17.689 -76.130  1.00 35.86  ? 510 LYS B N   1 
ATOM   8306  C CA  . LYS B  1 510 ? -27.014  -18.824 -75.254  1.00 37.09  ? 510 LYS B CA  1 
ATOM   8307  C C   . LYS B  1 510 ? -28.230  -19.079 -74.379  1.00 33.82  ? 510 LYS B C   1 
ATOM   8308  O O   . LYS B  1 510 ? -28.817  -18.155 -73.847  1.00 30.86  ? 510 LYS B O   1 
ATOM   8309  C CB  . LYS B  1 510 ? -25.709  -18.575 -74.477  1.00 40.12  ? 510 LYS B CB  1 
ATOM   8310  C CG  . LYS B  1 510 ? -24.505  -18.564 -75.439  1.00 43.98  ? 510 LYS B CG  1 
ATOM   8311  C CD  . LYS B  1 510 ? -23.107  -18.358 -74.877  1.00 47.22  ? 510 LYS B CD  1 
ATOM   8312  C CE  . LYS B  1 510 ? -22.651  -19.513 -74.068  1.00 49.81  ? 510 LYS B CE  1 
ATOM   8313  N NZ  . LYS B  1 510 ? -22.250  -20.665 -74.868  1.00 55.35  ? 510 LYS B NZ  1 
ATOM   8314  N N   . ILE B  1 511 ? -28.611  -20.350 -74.257  1.00 34.59  ? 511 ILE B N   1 
ATOM   8315  C CA  . ILE B  1 511 ? -29.439  -20.823 -73.158  1.00 34.56  ? 511 ILE B CA  1 
ATOM   8316  C C   . ILE B  1 511 ? -28.516  -21.508 -72.148  1.00 34.42  ? 511 ILE B C   1 
ATOM   8317  O O   . ILE B  1 511 ? -27.524  -22.098 -72.543  1.00 34.98  ? 511 ILE B O   1 
ATOM   8318  C CB  . ILE B  1 511 ? -30.566  -21.761 -73.636  1.00 35.73  ? 511 ILE B CB  1 
ATOM   8319  C CG1 . ILE B  1 511 ? -29.999  -23.088 -74.283  1.00 34.70  ? 511 ILE B CG1 1 
ATOM   8320  C CG2 . ILE B  1 511 ? -31.550  -21.001 -74.540  1.00 34.39  ? 511 ILE B CG2 1 
ATOM   8321  C CD1 . ILE B  1 511 ? -31.051  -24.133 -74.605  1.00 34.90  ? 511 ILE B CD1 1 
ATOM   8322  N N   . HIS B  1 512 ? -28.930  -21.500 -70.870  1.00 33.62  ? 512 HIS B N   1 
ATOM   8323  C CA  . HIS B  1 512 ? -28.060  -21.725 -69.730  1.00 31.51  ? 512 HIS B CA  1 
ATOM   8324  C C   . HIS B  1 512 ? -28.893  -21.706 -68.445  1.00 30.11  ? 512 HIS B C   1 
ATOM   8325  O O   . HIS B  1 512 ? -30.035  -21.251 -68.422  1.00 28.78  ? 512 HIS B O   1 
ATOM   8326  C CB  . HIS B  1 512 ? -26.960  -20.645 -69.664  1.00 31.64  ? 512 HIS B CB  1 
ATOM   8327  C CG  . HIS B  1 512 ? -27.502  -19.256 -69.872  1.00 31.84  ? 512 HIS B CG  1 
ATOM   8328  N ND1 . HIS B  1 512 ? -28.327  -18.606 -68.964  1.00 30.20  ? 512 HIS B ND1 1 
ATOM   8329  C CD2 . HIS B  1 512 ? -27.426  -18.457 -70.939  1.00 31.79  ? 512 HIS B CD2 1 
ATOM   8330  C CE1 . HIS B  1 512 ? -28.659  -17.423 -69.457  1.00 31.14  ? 512 HIS B CE1 1 
ATOM   8331  N NE2 . HIS B  1 512 ? -28.152  -17.318 -70.661  1.00 31.03  ? 512 HIS B NE2 1 
ATOM   8332  N N   . ASP B  1 513 ? -28.286  -22.244 -67.382  1.00 30.07  ? 513 ASP B N   1 
ATOM   8333  C CA  . ASP B  1 513 ? -28.822  -22.241 -66.041  1.00 30.17  ? 513 ASP B CA  1 
ATOM   8334  C C   . ASP B  1 513 ? -27.638  -22.225 -65.082  1.00 30.33  ? 513 ASP B C   1 
ATOM   8335  O O   . ASP B  1 513 ? -26.500  -22.543 -65.457  1.00 28.49  ? 513 ASP B O   1 
ATOM   8336  C CB  . ASP B  1 513 ? -29.692  -23.465 -65.825  1.00 33.33  ? 513 ASP B CB  1 
ATOM   8337  C CG  . ASP B  1 513 ? -30.657  -23.394 -64.649  1.00 33.21  ? 513 ASP B CG  1 
ATOM   8338  O OD1 . ASP B  1 513 ? -30.705  -22.307 -64.000  1.00 30.61  ? 513 ASP B OD1 1 
ATOM   8339  O OD2 . ASP B  1 513 ? -31.309  -24.450 -64.386  1.00 33.41  ? 513 ASP B OD2 1 
ATOM   8340  N N   . GLN B  1 514 ? -27.928  -21.836 -63.836  1.00 32.25  ? 514 GLN B N   1 
ATOM   8341  C CA  . GLN B  1 514 ? -26.894  -21.467 -62.879  1.00 32.41  ? 514 GLN B CA  1 
ATOM   8342  C C   . GLN B  1 514 ? -27.452  -21.707 -61.492  1.00 32.12  ? 514 GLN B C   1 
ATOM   8343  O O   . GLN B  1 514 ? -28.602  -21.366 -61.262  1.00 32.66  ? 514 GLN B O   1 
ATOM   8344  C CB  . GLN B  1 514 ? -26.572  -19.977 -63.005  1.00 31.90  ? 514 GLN B CB  1 
ATOM   8345  C CG  . GLN B  1 514 ? -25.446  -19.472 -62.113  1.00 31.12  ? 514 GLN B CG  1 
ATOM   8346  C CD  . GLN B  1 514 ? -25.422  -17.953 -62.008  1.00 30.72  ? 514 GLN B CD  1 
ATOM   8347  O OE1 . GLN B  1 514 ? -26.292  -17.330 -61.398  1.00 30.88  ? 514 GLN B OE1 1 
ATOM   8348  N NE2 . GLN B  1 514 ? -24.416  -17.320 -62.588  1.00 29.40  ? 514 GLN B NE2 1 
ATOM   8349  N N   . LYS B  1 515 ? -26.635  -22.311 -60.627  1.00 32.55  ? 515 LYS B N   1 
ATOM   8350  C CA  . LYS B  1 515 ? -26.938  -22.482 -59.222  1.00 33.39  ? 515 LYS B CA  1 
ATOM   8351  C C   . LYS B  1 515 ? -25.720  -22.086 -58.386  1.00 35.00  ? 515 LYS B C   1 
ATOM   8352  O O   . LYS B  1 515 ? -24.594  -22.482 -58.701  1.00 37.22  ? 515 LYS B O   1 
ATOM   8353  C CB  . LYS B  1 515 ? -27.213  -23.944 -58.921  1.00 34.69  ? 515 LYS B CB  1 
ATOM   8354  C CG  . LYS B  1 515 ? -28.265  -24.583 -59.778  1.00 36.22  ? 515 LYS B CG  1 
ATOM   8355  C CD  . LYS B  1 515 ? -29.689  -24.158 -59.444  1.00 37.15  ? 515 LYS B CD  1 
ATOM   8356  C CE  . LYS B  1 515 ? -30.596  -24.794 -60.432  1.00 37.22  ? 515 LYS B CE  1 
ATOM   8357  N NZ  . LYS B  1 515 ? -31.930  -24.243 -60.323  1.00 37.38  ? 515 LYS B NZ  1 
ATOM   8358  N N   . ILE B  1 516 ? -25.957  -21.297 -57.328  1.00 33.17  ? 516 ILE B N   1 
ATOM   8359  C CA  . ILE B  1 516 ? -24.913  -20.935 -56.391  1.00 32.01  ? 516 ILE B CA  1 
ATOM   8360  C C   . ILE B  1 516 ? -25.183  -21.683 -55.096  1.00 30.96  ? 516 ILE B C   1 
ATOM   8361  O O   . ILE B  1 516 ? -26.277  -21.642 -54.582  1.00 30.27  ? 516 ILE B O   1 
ATOM   8362  C CB  . ILE B  1 516 ? -24.846  -19.405 -56.227  1.00 30.61  ? 516 ILE B CB  1 
ATOM   8363  C CG1 . ILE B  1 516 ? -24.413  -18.750 -57.530  1.00 31.10  ? 516 ILE B CG1 1 
ATOM   8364  C CG2 . ILE B  1 516 ? -23.918  -19.008 -55.089  1.00 29.60  ? 516 ILE B CG2 1 
ATOM   8365  C CD1 . ILE B  1 516 ? -24.705  -17.257 -57.614  1.00 31.62  ? 516 ILE B CD1 1 
ATOM   8366  N N   . ILE B  1 517 ? -24.178  -22.396 -54.594  1.00 32.94  ? 517 ILE B N   1 
ATOM   8367  C CA  . ILE B  1 517 ? -24.362  -23.323 -53.484  1.00 33.01  ? 517 ILE B CA  1 
ATOM   8368  C C   . ILE B  1 517 ? -23.226  -23.185 -52.479  1.00 33.92  ? 517 ILE B C   1 
ATOM   8369  O O   . ILE B  1 517 ? -22.050  -23.140 -52.842  1.00 33.55  ? 517 ILE B O   1 
ATOM   8370  C CB  . ILE B  1 517 ? -24.437  -24.755 -54.009  1.00 33.20  ? 517 ILE B CB  1 
ATOM   8371  C CG1 . ILE B  1 517 ? -25.426  -24.880 -55.123  1.00 33.85  ? 517 ILE B CG1 1 
ATOM   8372  C CG2 . ILE B  1 517 ? -24.764  -25.699 -52.865  1.00 34.40  ? 517 ILE B CG2 1 
ATOM   8373  C CD1 . ILE B  1 517 ? -25.403  -26.240 -55.788  1.00 35.59  ? 517 ILE B CD1 1 
ATOM   8374  N N   . TYR B  1 518 ? -23.604  -23.164 -51.197  1.00 35.31  ? 518 TYR B N   1 
ATOM   8375  C CA  . TYR B  1 518 ? -22.708  -22.830 -50.100  1.00 33.65  ? 518 TYR B CA  1 
ATOM   8376  C C   . TYR B  1 518 ? -22.356  -24.079 -49.297  1.00 35.00  ? 518 TYR B C   1 
ATOM   8377  O O   . TYR B  1 518 ? -23.160  -25.003 -49.211  1.00 34.91  ? 518 TYR B O   1 
ATOM   8378  C CB  . TYR B  1 518 ? -23.485  -21.866 -49.211  1.00 34.07  ? 518 TYR B CB  1 
ATOM   8379  C CG  . TYR B  1 518 ? -23.778  -20.519 -49.865  1.00 35.29  ? 518 TYR B CG  1 
ATOM   8380  C CD1 . TYR B  1 518 ? -22.763  -19.584 -50.005  1.00 33.67  ? 518 TYR B CD1 1 
ATOM   8381  C CD2 . TYR B  1 518 ? -25.057  -20.178 -50.296  1.00 34.68  ? 518 TYR B CD2 1 
ATOM   8382  C CE1 . TYR B  1 518 ? -23.000  -18.361 -50.584  1.00 34.72  ? 518 TYR B CE1 1 
ATOM   8383  C CE2 . TYR B  1 518 ? -25.295  -18.962 -50.896  1.00 35.04  ? 518 TYR B CE2 1 
ATOM   8384  C CZ  . TYR B  1 518 ? -24.268  -18.043 -51.016  1.00 35.16  ? 518 TYR B CZ  1 
ATOM   8385  O OH  . TYR B  1 518 ? -24.420  -16.805 -51.563  1.00 34.67  ? 518 TYR B OH  1 
ATOM   8386  N N   . ARG B  1 519 ? -21.169  -24.076 -48.678  1.00 34.79  ? 519 ARG B N   1 
ATOM   8387  C CA  . ARG B  1 519 ? -20.868  -25.036 -47.641  1.00 35.33  ? 519 ARG B CA  1 
ATOM   8388  C C   . ARG B  1 519 ? -21.432  -24.522 -46.324  1.00 37.27  ? 519 ARG B C   1 
ATOM   8389  O O   . ARG B  1 519 ? -20.876  -23.609 -45.720  1.00 37.99  ? 519 ARG B O   1 
ATOM   8390  C CB  . ARG B  1 519 ? -19.368  -25.296 -47.515  1.00 34.05  ? 519 ARG B CB  1 
ATOM   8391  C CG  . ARG B  1 519 ? -18.998  -26.463 -46.609  1.00 33.60  ? 519 ARG B CG  1 
ATOM   8392  C CD  . ARG B  1 519 ? -17.502  -26.512 -46.417  1.00 33.01  ? 519 ARG B CD  1 
ATOM   8393  N NE  . ARG B  1 519 ? -16.880  -26.962 -47.667  1.00 32.88  ? 519 ARG B NE  1 
ATOM   8394  C CZ  . ARG B  1 519 ? -16.926  -28.221 -48.144  1.00 32.14  ? 519 ARG B CZ  1 
ATOM   8395  N NH1 . ARG B  1 519 ? -17.499  -29.173 -47.463  1.00 32.12  ? 519 ARG B NH1 1 
ATOM   8396  N NH2 . ARG B  1 519 ? -16.426  -28.507 -49.319  1.00 31.77  ? 519 ARG B NH2 1 
ATOM   8397  N N   . GLY B  1 520 ? -22.514  -25.155 -45.855  1.00 38.98  ? 520 GLY B N   1 
ATOM   8398  C CA  . GLY B  1 520 ? -23.033  -24.885 -44.523  1.00 39.04  ? 520 GLY B CA  1 
ATOM   8399  C C   . GLY B  1 520 ? -23.562  -23.461 -44.465  1.00 37.93  ? 520 GLY B C   1 
ATOM   8400  O O   . GLY B  1 520 ? -24.102  -22.993 -45.456  1.00 36.55  ? 520 GLY B O   1 
ATOM   8401  N N   . ASP B  1 521 ? -23.330  -22.772 -43.343  1.00 38.99  ? 521 ASP B N   1 
ATOM   8402  C CA  . ASP B  1 521 ? -24.049  -21.539 -43.056  1.00 41.85  ? 521 ASP B CA  1 
ATOM   8403  C C   . ASP B  1 521 ? -23.122  -20.310 -43.060  1.00 38.52  ? 521 ASP B C   1 
ATOM   8404  O O   . ASP B  1 521 ? -23.542  -19.238 -42.639  1.00 36.35  ? 521 ASP B O   1 
ATOM   8405  C CB  . ASP B  1 521 ? -24.873  -21.707 -41.787  1.00 44.46  ? 521 ASP B CB  1 
ATOM   8406  C CG  . ASP B  1 521 ? -24.078  -21.854 -40.496  1.00 49.63  ? 521 ASP B CG  1 
ATOM   8407  O OD1 . ASP B  1 521 ? -22.845  -21.576 -40.492  1.00 51.04  ? 521 ASP B OD1 1 
ATOM   8408  O OD2 . ASP B  1 521 ? -24.694  -22.277 -39.500  1.00 56.46  ? 521 ASP B OD2 1 
ATOM   8409  N N   . TRP B  1 522 ? -21.891  -20.444 -43.581  1.00 36.73  ? 522 TRP B N   1 
ATOM   8410  C CA  . TRP B  1 522 ? -20.895  -19.398 -43.419  1.00 36.77  ? 522 TRP B CA  1 
ATOM   8411  C C   . TRP B  1 522 ? -21.375  -18.098 -44.058  1.00 36.72  ? 522 TRP B C   1 
ATOM   8412  O O   . TRP B  1 522 ? -20.980  -17.033 -43.606  1.00 37.76  ? 522 TRP B O   1 
ATOM   8413  C CB  . TRP B  1 522 ? -19.517  -19.798 -43.966  1.00 35.51  ? 522 TRP B CB  1 
ATOM   8414  C CG  . TRP B  1 522 ? -19.403  -19.711 -45.457  1.00 34.53  ? 522 TRP B CG  1 
ATOM   8415  C CD1 . TRP B  1 522 ? -19.717  -20.697 -46.342  1.00 35.73  ? 522 TRP B CD1 1 
ATOM   8416  C CD2 . TRP B  1 522 ? -18.952  -18.593 -46.252  1.00 34.41  ? 522 TRP B CD2 1 
ATOM   8417  N NE1 . TRP B  1 522 ? -19.523  -20.269 -47.625  1.00 35.11  ? 522 TRP B NE1 1 
ATOM   8418  C CE2 . TRP B  1 522 ? -19.044  -18.985 -47.603  1.00 34.18  ? 522 TRP B CE2 1 
ATOM   8419  C CE3 . TRP B  1 522 ? -18.464  -17.316 -45.967  1.00 33.98  ? 522 TRP B CE3 1 
ATOM   8420  C CZ2 . TRP B  1 522 ? -18.679  -18.142 -48.652  1.00 33.74  ? 522 TRP B CZ2 1 
ATOM   8421  C CZ3 . TRP B  1 522 ? -18.109  -16.485 -47.007  1.00 33.70  ? 522 TRP B CZ3 1 
ATOM   8422  C CH2 . TRP B  1 522 ? -18.213  -16.894 -48.335  1.00 33.45  ? 522 TRP B CH2 1 
ATOM   8423  N N   . ALA B  1 523 ? -22.232  -18.194 -45.074  1.00 36.73  ? 523 ALA B N   1 
ATOM   8424  C CA  . ALA B  1 523 ? -22.636  -17.033 -45.835  1.00 38.28  ? 523 ALA B CA  1 
ATOM   8425  C C   . ALA B  1 523 ? -24.036  -16.514 -45.451  1.00 40.60  ? 523 ALA B C   1 
ATOM   8426  O O   . ALA B  1 523 ? -24.627  -15.740 -46.212  1.00 42.44  ? 523 ALA B O   1 
ATOM   8427  C CB  . ALA B  1 523 ? -22.531  -17.358 -47.316  1.00 35.34  ? 523 ALA B CB  1 
ATOM   8428  N N   . LYS B  1 524 ? -24.551  -16.824 -44.261  1.00 40.97  ? 524 LYS B N   1 
ATOM   8429  C CA  . LYS B  1 524 ? -25.894  -16.363 -43.927  1.00 44.62  ? 524 LYS B CA  1 
ATOM   8430  C C   . LYS B  1 524 ? -25.983  -14.831 -43.985  1.00 44.22  ? 524 LYS B C   1 
ATOM   8431  O O   . LYS B  1 524 ? -26.984  -14.274 -44.436  1.00 43.20  ? 524 LYS B O   1 
ATOM   8432  C CB  . LYS B  1 524 ? -26.442  -16.926 -42.612  1.00 48.56  ? 524 LYS B CB  1 
ATOM   8433  C CG  . LYS B  1 524 ? -25.590  -16.757 -41.366  1.00 56.08  ? 524 LYS B CG  1 
ATOM   8434  C CD  . LYS B  1 524 ? -26.175  -17.452 -40.128  1.00 65.54  ? 524 LYS B CD  1 
ATOM   8435  C CE  . LYS B  1 524 ? -25.406  -17.262 -38.834  1.00 69.53  ? 524 LYS B CE  1 
ATOM   8436  N NZ  . LYS B  1 524 ? -23.947  -17.384 -38.971  1.00 68.75  ? 524 LYS B NZ  1 
ATOM   8437  N N   . GLU B  1 525 ? -24.920  -14.135 -43.572  1.00 42.54  ? 525 GLU B N   1 
ATOM   8438  C CA  . GLU B  1 525 ? -24.910  -12.681 -43.610  1.00 39.41  ? 525 GLU B CA  1 
ATOM   8439  C C   . GLU B  1 525 ? -24.462  -12.200 -44.995  1.00 37.47  ? 525 GLU B C   1 
ATOM   8440  O O   . GLU B  1 525 ? -25.151  -11.406 -45.624  1.00 35.41  ? 525 GLU B O   1 
ATOM   8441  C CB  . GLU B  1 525 ? -24.063  -12.049 -42.494  1.00 40.43  ? 525 GLU B CB  1 
ATOM   8442  C CG  . GLU B  1 525 ? -24.480  -12.384 -41.059  1.00 39.85  ? 525 GLU B CG  1 
ATOM   8443  C CD  . GLU B  1 525 ? -23.722  -13.559 -40.441  1.00 41.99  ? 525 GLU B CD  1 
ATOM   8444  O OE1 . GLU B  1 525 ? -22.740  -14.107 -41.025  1.00 40.44  ? 525 GLU B OE1 1 
ATOM   8445  O OE2 . GLU B  1 525 ? -24.134  -13.942 -39.337  1.00 42.03  ? 525 GLU B OE2 1 
ATOM   8446  N N   . VAL B  1 526 ? -23.311  -12.677 -45.498  1.00 37.30  ? 526 VAL B N   1 
ATOM   8447  C CA  . VAL B  1 526 ? -22.698  -12.062 -46.669  1.00 35.64  ? 526 VAL B CA  1 
ATOM   8448  C C   . VAL B  1 526 ? -23.331  -12.532 -47.988  1.00 33.83  ? 526 VAL B C   1 
ATOM   8449  O O   . VAL B  1 526 ? -23.214  -11.835 -48.998  1.00 29.76  ? 526 VAL B O   1 
ATOM   8450  C CB  . VAL B  1 526 ? -21.176  -12.287 -46.679  1.00 35.84  ? 526 VAL B CB  1 
ATOM   8451  C CG1 . VAL B  1 526 ? -20.819  -13.750 -46.882  1.00 35.81  ? 526 VAL B CG1 1 
ATOM   8452  C CG2 . VAL B  1 526 ? -20.511  -11.419 -47.748  1.00 35.91  ? 526 VAL B CG2 1 
ATOM   8453  N N   . GLY B  1 527 ? -23.979  -13.714 -47.992  1.00 33.85  ? 527 GLY B N   1 
ATOM   8454  C CA  . GLY B  1 527 ? -24.510  -14.290 -49.224  1.00 33.63  ? 527 GLY B CA  1 
ATOM   8455  C C   . GLY B  1 527 ? -25.878  -13.727 -49.619  1.00 33.92  ? 527 GLY B C   1 
ATOM   8456  O O   . GLY B  1 527 ? -26.674  -13.367 -48.758  1.00 31.74  ? 527 GLY B O   1 
ATOM   8457  N N   . ARG B  1 528 ? -26.164  -13.707 -50.933  1.00 36.56  ? 528 ARG B N   1 
ATOM   8458  C CA  . ARG B  1 528 ? -27.444  -13.219 -51.426  1.00 41.45  ? 528 ARG B CA  1 
ATOM   8459  C C   . ARG B  1 528 ? -28.563  -14.077 -50.839  1.00 44.64  ? 528 ARG B C   1 
ATOM   8460  O O   . ARG B  1 528 ? -28.413  -15.286 -50.742  1.00 38.35  ? 528 ARG B O   1 
ATOM   8461  C CB  . ARG B  1 528 ? -27.556  -13.229 -52.958  1.00 43.38  ? 528 ARG B CB  1 
ATOM   8462  C CG  . ARG B  1 528 ? -28.695  -12.383 -53.549  1.00 40.43  ? 528 ARG B CG  1 
ATOM   8463  C CD  . ARG B  1 528 ? -28.839  -12.578 -55.073  1.00 38.44  ? 528 ARG B CD  1 
ATOM   8464  N NE  . ARG B  1 528 ? -27.812  -11.868 -55.852  1.00 35.98  ? 528 ARG B NE  1 
ATOM   8465  C CZ  . ARG B  1 528 ? -26.630  -12.351 -56.240  1.00 35.51  ? 528 ARG B CZ  1 
ATOM   8466  N NH1 . ARG B  1 528 ? -26.357  -13.640 -56.126  1.00 36.13  ? 528 ARG B NH1 1 
ATOM   8467  N NH2 . ARG B  1 528 ? -25.692  -11.544 -56.709  1.00 32.91  ? 528 ARG B NH2 1 
ATOM   8468  N N   . LYS B  1 529 ? -29.667  -13.418 -50.441  1.00 54.38  ? 529 LYS B N   1 
ATOM   8469  C CA  . LYS B  1 529 ? -30.820  -14.081 -49.840  1.00 57.28  ? 529 LYS B CA  1 
ATOM   8470  C C   . LYS B  1 529 ? -31.856  -14.426 -50.925  1.00 60.65  ? 529 LYS B C   1 
ATOM   8471  O O   . LYS B  1 529 ? -32.099  -13.527 -51.780  1.00 56.67  ? 529 LYS B O   1 
ATOM   8472  C CB  . LYS B  1 529 ? -31.483  -13.209 -48.767  1.00 59.14  ? 529 LYS B CB  1 
ATOM   8473  C CG  . LYS B  1 529 ? -30.802  -13.225 -47.401  1.00 64.18  ? 529 LYS B CG  1 
ATOM   8474  C CD  . LYS B  1 529 ? -29.825  -12.078 -47.190  1.00 69.12  ? 529 LYS B CD  1 
ATOM   8475  C CE  . LYS B  1 529 ? -28.961  -12.238 -45.967  1.00 69.75  ? 529 LYS B CE  1 
ATOM   8476  N NZ  . LYS B  1 529 ? -27.757  -11.408 -46.106  1.00 61.42  ? 529 LYS B NZ  1 
ATOM   8477  N N   . SER C  1 3   ? -22.812  29.449  -34.702  1.00 66.84  ? 3   SER C N   1 
ATOM   8478  C CA  . SER C  1 3   ? -22.011  30.685  -34.497  1.00 67.68  ? 3   SER C CA  1 
ATOM   8479  C C   . SER C  1 3   ? -22.286  31.667  -35.637  1.00 66.86  ? 3   SER C C   1 
ATOM   8480  O O   . SER C  1 3   ? -22.237  31.275  -36.803  1.00 68.06  ? 3   SER C O   1 
ATOM   8481  C CB  . SER C  1 3   ? -20.535  30.366  -34.387  1.00 66.94  ? 3   SER C CB  1 
ATOM   8482  O OG  . SER C  1 3   ? -19.817  31.475  -33.863  1.00 63.27  ? 3   SER C OG  1 
ATOM   8483  N N   . LYS C  1 4   ? -22.568  32.935  -35.297  1.00 61.35  ? 4   LYS C N   1 
ATOM   8484  C CA  . LYS C  1 4   ? -22.948  33.922  -36.297  1.00 58.70  ? 4   LYS C CA  1 
ATOM   8485  C C   . LYS C  1 4   ? -21.764  34.816  -36.678  1.00 51.52  ? 4   LYS C C   1 
ATOM   8486  O O   . LYS C  1 4   ? -20.888  35.085  -35.864  1.00 48.62  ? 4   LYS C O   1 
ATOM   8487  C CB  . LYS C  1 4   ? -24.175  34.727  -35.848  1.00 64.34  ? 4   LYS C CB  1 
ATOM   8488  C CG  . LYS C  1 4   ? -24.009  35.864  -34.817  1.00 67.90  ? 4   LYS C CG  1 
ATOM   8489  C CD  . LYS C  1 4   ? -25.202  35.980  -33.853  1.00 72.67  ? 4   LYS C CD  1 
ATOM   8490  C CE  . LYS C  1 4   ? -25.367  37.277  -33.106  1.00 74.30  ? 4   LYS C CE  1 
ATOM   8491  N NZ  . LYS C  1 4   ? -24.127  37.830  -32.551  1.00 75.98  ? 4   LYS C NZ  1 
ATOM   8492  N N   . THR C  1 5   ? -21.803  35.288  -37.935  1.00 48.00  ? 5   THR C N   1 
ATOM   8493  C CA  . THR C  1 5   ? -20.780  36.117  -38.572  1.00 48.22  ? 5   THR C CA  1 
ATOM   8494  C C   . THR C  1 5   ? -20.329  37.279  -37.676  1.00 46.70  ? 5   THR C C   1 
ATOM   8495  O O   . THR C  1 5   ? -21.137  37.993  -37.102  1.00 43.76  ? 5   THR C O   1 
ATOM   8496  C CB  . THR C  1 5   ? -21.315  36.634  -39.913  1.00 46.24  ? 5   THR C CB  1 
ATOM   8497  O OG1 . THR C  1 5   ? -21.765  35.446  -40.554  1.00 45.77  ? 5   THR C OG1 1 
ATOM   8498  C CG2 . THR C  1 5   ? -20.266  37.326  -40.763  1.00 44.16  ? 5   THR C CG2 1 
ATOM   8499  N N   . LYS C  1 6   ? -19.006  37.397  -37.539  1.00 47.33  ? 6   LYS C N   1 
ATOM   8500  C CA  . LYS C  1 6   ? -18.348  38.488  -36.859  1.00 48.27  ? 6   LYS C CA  1 
ATOM   8501  C C   . LYS C  1 6   ? -17.891  39.491  -37.913  1.00 45.69  ? 6   LYS C C   1 
ATOM   8502  O O   . LYS C  1 6   ? -17.090  39.176  -38.796  1.00 42.43  ? 6   LYS C O   1 
ATOM   8503  C CB  . LYS C  1 6   ? -17.172  37.907  -36.069  1.00 51.95  ? 6   LYS C CB  1 
ATOM   8504  C CG  . LYS C  1 6   ? -16.331  38.931  -35.314  1.00 56.32  ? 6   LYS C CG  1 
ATOM   8505  C CD  . LYS C  1 6   ? -15.072  38.345  -34.683  1.00 60.29  ? 6   LYS C CD  1 
ATOM   8506  C CE  . LYS C  1 6   ? -14.463  39.275  -33.665  1.00 63.96  ? 6   LYS C CE  1 
ATOM   8507  N NZ  . LYS C  1 6   ? -13.700  38.504  -32.670  1.00 66.28  ? 6   LYS C NZ  1 
ATOM   8508  N N   . ILE C  1 7   ? -18.422  40.707  -37.812  1.00 47.08  ? 7   ILE C N   1 
ATOM   8509  C CA  . ILE C  1 7   ? -18.035  41.799  -38.690  1.00 45.47  ? 7   ILE C CA  1 
ATOM   8510  C C   . ILE C  1 7   ? -17.095  42.745  -37.937  1.00 49.12  ? 7   ILE C C   1 
ATOM   8511  O O   . ILE C  1 7   ? -17.432  43.271  -36.880  1.00 48.36  ? 7   ILE C O   1 
ATOM   8512  C CB  . ILE C  1 7   ? -19.278  42.529  -39.215  1.00 43.32  ? 7   ILE C CB  1 
ATOM   8513  C CG1 . ILE C  1 7   ? -20.289  41.563  -39.798  1.00 43.21  ? 7   ILE C CG1 1 
ATOM   8514  C CG2 . ILE C  1 7   ? -18.883  43.605  -40.228  1.00 41.90  ? 7   ILE C CG2 1 
ATOM   8515  C CD1 . ILE C  1 7   ? -21.472  42.258  -40.469  1.00 43.99  ? 7   ILE C CD1 1 
ATOM   8516  N N   . GLU C  1 8   ? -15.932  43.021  -38.542  1.00 52.94  ? 8   GLU C N   1 
ATOM   8517  C CA  . GLU C  1 8   ? -14.929  43.884  -37.942  1.00 54.22  ? 8   GLU C CA  1 
ATOM   8518  C C   . GLU C  1 8   ? -14.469  44.917  -38.971  1.00 49.96  ? 8   GLU C C   1 
ATOM   8519  O O   . GLU C  1 8   ? -14.047  44.581  -40.082  1.00 47.57  ? 8   GLU C O   1 
ATOM   8520  C CB  . GLU C  1 8   ? -13.880  42.888  -37.446  1.00 60.32  ? 8   GLU C CB  1 
ATOM   8521  C CG  . GLU C  1 8   ? -12.849  43.445  -36.473  1.00 67.95  ? 8   GLU C CG  1 
ATOM   8522  C CD  . GLU C  1 8   ? -12.126  42.348  -35.702  1.00 74.61  ? 8   GLU C CD  1 
ATOM   8523  O OE1 . GLU C  1 8   ? -12.508  41.144  -35.727  1.00 71.85  ? 8   GLU C OE1 1 
ATOM   8524  O OE2 . GLU C  1 8   ? -11.139  42.746  -35.057  1.00 80.61  ? 8   GLU C OE2 1 
ATOM   8525  N N   . LEU C  1 9   ? -14.538  46.193  -38.588  1.00 49.84  ? 9   LEU C N   1 
ATOM   8526  C CA  . LEU C  1 9   ? -14.109  47.283  -39.450  1.00 46.22  ? 9   LEU C CA  1 
ATOM   8527  C C   . LEU C  1 9   ? -12.735  47.757  -39.001  1.00 47.27  ? 9   LEU C C   1 
ATOM   8528  O O   . LEU C  1 9   ? -12.577  48.154  -37.862  1.00 50.03  ? 9   LEU C O   1 
ATOM   8529  C CB  . LEU C  1 9   ? -15.160  48.377  -39.320  1.00 46.60  ? 9   LEU C CB  1 
ATOM   8530  C CG  . LEU C  1 9   ? -16.602  47.913  -39.537  1.00 45.88  ? 9   LEU C CG  1 
ATOM   8531  C CD1 . LEU C  1 9   ? -17.513  49.120  -39.501  1.00 48.65  ? 9   LEU C CD1 1 
ATOM   8532  C CD2 . LEU C  1 9   ? -16.775  47.171  -40.836  1.00 42.11  ? 9   LEU C CD2 1 
ATOM   8533  N N   . LYS C  1 10  ? -11.737  47.691  -39.882  1.00 47.29  ? 10  LYS C N   1 
ATOM   8534  C CA  . LYS C  1 10  ? -10.356  47.911  -39.494  1.00 47.90  ? 10  LYS C CA  1 
ATOM   8535  C C   . LYS C  1 10  ? -9.540   48.047  -40.764  1.00 46.98  ? 10  LYS C C   1 
ATOM   8536  O O   . LYS C  1 10  ? -9.837   47.371  -41.734  1.00 48.82  ? 10  LYS C O   1 
ATOM   8537  C CB  . LYS C  1 10  ? -9.883   46.701  -38.685  1.00 54.12  ? 10  LYS C CB  1 
ATOM   8538  C CG  . LYS C  1 10  ? -8.481   46.802  -38.122  1.00 58.50  ? 10  LYS C CG  1 
ATOM   8539  C CD  . LYS C  1 10  ? -8.094   45.584  -37.289  1.00 66.08  ? 10  LYS C CD  1 
ATOM   8540  C CE  . LYS C  1 10  ? -6.667   45.626  -36.831  1.00 70.63  ? 10  LYS C CE  1 
ATOM   8541  N NZ  . LYS C  1 10  ? -6.339   46.967  -36.323  1.00 71.99  ? 10  LYS C NZ  1 
ATOM   8542  N N   . ASP C  1 11  ? -8.568   48.960  -40.770  1.00 49.38  ? 11  ASP C N   1 
ATOM   8543  C CA  . ASP C  1 11  ? -7.766   49.297  -41.941  1.00 48.15  ? 11  ASP C CA  1 
ATOM   8544  C C   . ASP C  1 11  ? -8.664   49.732  -43.096  1.00 44.95  ? 11  ASP C C   1 
ATOM   8545  O O   . ASP C  1 11  ? -8.322   49.504  -44.255  1.00 44.10  ? 11  ASP C O   1 
ATOM   8546  C CB  . ASP C  1 11  ? -6.823   48.158  -42.303  1.00 52.61  ? 11  ASP C CB  1 
ATOM   8547  C CG  . ASP C  1 11  ? -5.963   47.652  -41.151  1.00 57.79  ? 11  ASP C CG  1 
ATOM   8548  O OD1 . ASP C  1 11  ? -5.432   48.510  -40.413  1.00 61.66  ? 11  ASP C OD1 1 
ATOM   8549  O OD2 . ASP C  1 11  ? -5.829   46.411  -40.997  1.00 65.46  ? 11  ASP C OD2 1 
ATOM   8550  N N   . ASN C  1 12  ? -9.808   50.360  -42.769  1.00 44.45  ? 12  ASN C N   1 
ATOM   8551  C CA  . ASN C  1 12  ? -10.797  50.815  -43.746  1.00 42.21  ? 12  ASN C CA  1 
ATOM   8552  C C   . ASN C  1 12  ? -11.388  49.657  -44.592  1.00 40.37  ? 12  ASN C C   1 
ATOM   8553  O O   . ASN C  1 12  ? -11.800  49.875  -45.726  1.00 36.27  ? 12  ASN C O   1 
ATOM   8554  C CB  . ASN C  1 12  ? -10.183  51.927  -44.591  1.00 41.08  ? 12  ASN C CB  1 
ATOM   8555  C CG  . ASN C  1 12  ? -9.710   53.097  -43.768  1.00 40.66  ? 12  ASN C CG  1 
ATOM   8556  O OD1 . ASN C  1 12  ? -10.183  53.367  -42.661  1.00 41.36  ? 12  ASN C OD1 1 
ATOM   8557  N ND2 . ASN C  1 12  ? -8.813   53.865  -44.336  1.00 40.61  ? 12  ASN C ND2 1 
ATOM   8558  N N   . TRP C  1 13  ? -11.494  48.442  -44.021  1.00 39.84  ? 13  TRP C N   1 
ATOM   8559  C CA  . TRP C  1 13  ? -12.050  47.273  -44.700  1.00 40.80  ? 13  TRP C CA  1 
ATOM   8560  C C   . TRP C  1 13  ? -13.089  46.576  -43.820  1.00 39.29  ? 13  TRP C C   1 
ATOM   8561  O O   . TRP C  1 13  ? -12.896  46.472  -42.618  1.00 39.45  ? 13  TRP C O   1 
ATOM   8562  C CB  . TRP C  1 13  ? -10.961  46.225  -45.014  1.00 40.72  ? 13  TRP C CB  1 
ATOM   8563  C CG  . TRP C  1 13  ? -10.152  46.435  -46.267  1.00 38.90  ? 13  TRP C CG  1 
ATOM   8564  C CD1 . TRP C  1 13  ? -9.059   47.240  -46.438  1.00 38.26  ? 13  TRP C CD1 1 
ATOM   8565  C CD2 . TRP C  1 13  ? -10.364  45.774  -47.527  1.00 36.17  ? 13  TRP C CD2 1 
ATOM   8566  N NE1 . TRP C  1 13  ? -8.568   47.109  -47.710  1.00 36.71  ? 13  TRP C NE1 1 
ATOM   8567  C CE2 . TRP C  1 13  ? -9.347   46.224  -48.400  1.00 35.09  ? 13  TRP C CE2 1 
ATOM   8568  C CE3 . TRP C  1 13  ? -11.314  44.861  -47.993  1.00 36.01  ? 13  TRP C CE3 1 
ATOM   8569  C CZ2 . TRP C  1 13  ? -9.253   45.789  -49.715  1.00 34.64  ? 13  TRP C CZ2 1 
ATOM   8570  C CZ3 . TRP C  1 13  ? -11.224  44.433  -49.295  1.00 34.88  ? 13  TRP C CZ3 1 
ATOM   8571  C CH2 . TRP C  1 13  ? -10.204  44.890  -50.145  1.00 34.05  ? 13  TRP C CH2 1 
ATOM   8572  N N   . TYR C  1 14  ? -14.134  46.026  -44.447  1.00 37.75  ? 14  TYR C N   1 
ATOM   8573  C CA  . TYR C  1 14  ? -14.929  44.999  -43.809  1.00 37.78  ? 14  TYR C CA  1 
ATOM   8574  C C   . TYR C  1 14  ? -14.091  43.716  -43.755  1.00 36.80  ? 14  TYR C C   1 
ATOM   8575  O O   . TYR C  1 14  ? -13.437  43.321  -44.720  1.00 34.68  ? 14  TYR C O   1 
ATOM   8576  C CB  . TYR C  1 14  ? -16.267  44.730  -44.514  1.00 38.13  ? 14  TYR C CB  1 
ATOM   8577  C CG  . TYR C  1 14  ? -17.348  45.802  -44.472  1.00 38.16  ? 14  TYR C CG  1 
ATOM   8578  C CD1 . TYR C  1 14  ? -17.215  47.001  -45.149  1.00 37.88  ? 14  TYR C CD1 1 
ATOM   8579  C CD2 . TYR C  1 14  ? -18.553  45.563  -43.828  1.00 39.15  ? 14  TYR C CD2 1 
ATOM   8580  C CE1 . TYR C  1 14  ? -18.227  47.945  -45.131  1.00 37.92  ? 14  TYR C CE1 1 
ATOM   8581  C CE2 . TYR C  1 14  ? -19.574  46.492  -43.800  1.00 37.57  ? 14  TYR C CE2 1 
ATOM   8582  C CZ  . TYR C  1 14  ? -19.412  47.690  -44.465  1.00 38.26  ? 14  TYR C CZ  1 
ATOM   8583  O OH  . TYR C  1 14  ? -20.432  48.611  -44.449  1.00 38.63  ? 14  TYR C OH  1 
ATOM   8584  N N   . HIS C  1 15  ? -14.073  43.120  -42.567  1.00 39.10  ? 15  HIS C N   1 
ATOM   8585  C CA  . HIS C  1 15  ? -13.590  41.767  -42.320  1.00 39.94  ? 15  HIS C CA  1 
ATOM   8586  C C   . HIS C  1 15  ? -14.819  40.946  -41.940  1.00 39.61  ? 15  HIS C C   1 
ATOM   8587  O O   . HIS C  1 15  ? -15.611  41.416  -41.123  1.00 41.62  ? 15  HIS C O   1 
ATOM   8588  C CB  . HIS C  1 15  ? -12.604  41.758  -41.143  1.00 40.94  ? 15  HIS C CB  1 
ATOM   8589  C CG  . HIS C  1 15  ? -11.369  42.567  -41.375  1.00 43.49  ? 15  HIS C CG  1 
ATOM   8590  N ND1 . HIS C  1 15  ? -11.381  43.910  -41.684  1.00 42.49  ? 15  HIS C ND1 1 
ATOM   8591  C CD2 . HIS C  1 15  ? -10.077  42.197  -41.403  1.00 44.99  ? 15  HIS C CD2 1 
ATOM   8592  C CE1 . HIS C  1 15  ? -10.141  44.307  -41.890  1.00 42.99  ? 15  HIS C CE1 1 
ATOM   8593  N NE2 . HIS C  1 15  ? -9.336   43.289  -41.737  1.00 42.98  ? 15  HIS C NE2 1 
ATOM   8594  N N   . LEU C  1 16  ? -14.998  39.778  -42.569  1.00 38.01  ? 16  LEU C N   1 
ATOM   8595  C CA  . LEU C  1 16  ? -15.990  38.786  -42.163  1.00 39.08  ? 16  LEU C CA  1 
ATOM   8596  C C   . LEU C  1 16  ? -15.231  37.584  -41.652  1.00 39.42  ? 16  LEU C C   1 
ATOM   8597  O O   . LEU C  1 16  ? -14.490  37.014  -42.437  1.00 38.37  ? 16  LEU C O   1 
ATOM   8598  C CB  . LEU C  1 16  ? -16.921  38.352  -43.297  1.00 38.22  ? 16  LEU C CB  1 
ATOM   8599  C CG  . LEU C  1 16  ? -18.210  39.171  -43.438  1.00 39.66  ? 16  LEU C CG  1 
ATOM   8600  C CD1 . LEU C  1 16  ? -17.923  40.640  -43.310  1.00 38.35  ? 16  LEU C CD1 1 
ATOM   8601  C CD2 . LEU C  1 16  ? -18.978  38.891  -44.727  1.00 39.72  ? 16  LEU C CD2 1 
ATOM   8602  N N   . ASP C  1 17  ? -15.453  37.244  -40.369  1.00 42.23  ? 17  ASP C N   1 
ATOM   8603  C CA  . ASP C  1 17  ? -14.766  36.181  -39.649  1.00 43.12  ? 17  ASP C CA  1 
ATOM   8604  C C   . ASP C  1 17  ? -13.275  36.209  -39.971  1.00 44.22  ? 17  ASP C C   1 
ATOM   8605  O O   . ASP C  1 17  ? -12.741  35.234  -40.506  1.00 44.11  ? 17  ASP C O   1 
ATOM   8606  C CB  . ASP C  1 17  ? -15.347  34.805  -39.970  1.00 43.36  ? 17  ASP C CB  1 
ATOM   8607  C CG  . ASP C  1 17  ? -16.846  34.658  -39.780  1.00 42.74  ? 17  ASP C CG  1 
ATOM   8608  O OD1 . ASP C  1 17  ? -17.380  35.247  -38.809  1.00 42.26  ? 17  ASP C OD1 1 
ATOM   8609  O OD2 . ASP C  1 17  ? -17.457  33.989  -40.626  1.00 41.69  ? 17  ASP C OD2 1 
ATOM   8610  N N   . GLY C  1 18  ? -12.622  37.343  -39.686  1.00 44.94  ? 18  GLY C N   1 
ATOM   8611  C CA  . GLY C  1 18  ? -11.177  37.462  -39.812  1.00 45.30  ? 18  GLY C CA  1 
ATOM   8612  C C   . GLY C  1 18  ? -10.674  37.879  -41.199  1.00 44.71  ? 18  GLY C C   1 
ATOM   8613  O O   . GLY C  1 18  ? -9.566   38.388  -41.280  1.00 47.96  ? 18  GLY C O   1 
ATOM   8614  N N   . GLU C  1 19  ? -11.483  37.725  -42.263  1.00 44.23  ? 19  GLU C N   1 
ATOM   8615  C CA  . GLU C  1 19  ? -11.035  37.803  -43.653  1.00 44.22  ? 19  GLU C CA  1 
ATOM   8616  C C   . GLU C  1 19  ? -11.447  39.117  -44.320  1.00 42.81  ? 19  GLU C C   1 
ATOM   8617  O O   . GLU C  1 19  ? -12.630  39.448  -44.321  1.00 46.57  ? 19  GLU C O   1 
ATOM   8618  C CB  . GLU C  1 19  ? -11.705  36.687  -44.476  1.00 46.52  ? 19  GLU C CB  1 
ATOM   8619  C CG  . GLU C  1 19  ? -11.390  35.263  -44.010  1.00 50.41  ? 19  GLU C CG  1 
ATOM   8620  C CD  . GLU C  1 19  ? -9.892   35.016  -43.991  1.00 56.64  ? 19  GLU C CD  1 
ATOM   8621  O OE1 . GLU C  1 19  ? -9.319   34.976  -45.095  1.00 66.98  ? 19  GLU C OE1 1 
ATOM   8622  O OE2 . GLU C  1 19  ? -9.274   34.946  -42.914  1.00 60.19  ? 19  GLU C OE2 1 
ATOM   8623  N N   . LYS C  1 20  ? -10.529  39.837  -44.984  1.00 38.80  ? 20  LYS C N   1 
ATOM   8624  C CA  . LYS C  1 20  ? -10.968  41.038  -45.695  1.00 38.45  ? 20  LYS C CA  1 
ATOM   8625  C C   . LYS C  1 20  ? -12.025  40.656  -46.728  1.00 37.19  ? 20  LYS C C   1 
ATOM   8626  O O   . LYS C  1 20  ? -11.867  39.682  -47.440  1.00 35.88  ? 20  LYS C O   1 
ATOM   8627  C CB  . LYS C  1 20  ? -9.843   41.820  -46.381  1.00 38.04  ? 20  LYS C CB  1 
ATOM   8628  C CG  . LYS C  1 20  ? -8.869   42.381  -45.387  1.00 39.69  ? 20  LYS C CG  1 
ATOM   8629  C CD  . LYS C  1 20  ? -7.794   43.321  -45.895  1.00 41.93  ? 20  LYS C CD  1 
ATOM   8630  C CE  . LYS C  1 20  ? -6.948   43.702  -44.712  1.00 46.02  ? 20  LYS C CE  1 
ATOM   8631  N NZ  . LYS C  1 20  ? -5.856   44.575  -45.123  1.00 47.05  ? 20  LYS C NZ  1 
ATOM   8632  N N   . TYR C  1 21  ? -13.072  41.469  -46.844  1.00 36.78  ? 21  TYR C N   1 
ATOM   8633  C CA  . TYR C  1 21  ? -14.246  41.110  -47.618  1.00 34.71  ? 21  TYR C CA  1 
ATOM   8634  C C   . TYR C  1 21  ? -14.704  42.317  -48.417  1.00 34.19  ? 21  TYR C C   1 
ATOM   8635  O O   . TYR C  1 21  ? -15.265  43.255  -47.860  1.00 37.00  ? 21  TYR C O   1 
ATOM   8636  C CB  . TYR C  1 21  ? -15.407  40.662  -46.726  1.00 35.43  ? 21  TYR C CB  1 
ATOM   8637  C CG  . TYR C  1 21  ? -16.573  40.031  -47.468  1.00 34.39  ? 21  TYR C CG  1 
ATOM   8638  C CD1 . TYR C  1 21  ? -16.577  38.672  -47.769  1.00 35.02  ? 21  TYR C CD1 1 
ATOM   8639  C CD2 . TYR C  1 21  ? -17.689  40.777  -47.810  1.00 33.95  ? 21  TYR C CD2 1 
ATOM   8640  C CE1 . TYR C  1 21  ? -17.639  38.077  -48.432  1.00 34.36  ? 21  TYR C CE1 1 
ATOM   8641  C CE2 . TYR C  1 21  ? -18.757  40.201  -48.475  1.00 34.69  ? 21  TYR C CE2 1 
ATOM   8642  C CZ  . TYR C  1 21  ? -18.730  38.852  -48.789  1.00 35.09  ? 21  TYR C CZ  1 
ATOM   8643  O OH  . TYR C  1 21  ? -19.785  38.303  -49.454  1.00 36.54  ? 21  TYR C OH  1 
ATOM   8644  N N   . PHE C  1 22  ? -14.462  42.263  -49.724  1.00 32.54  ? 22  PHE C N   1 
ATOM   8645  C CA  . PHE C  1 22  ? -14.889  43.296  -50.620  1.00 32.48  ? 22  PHE C CA  1 
ATOM   8646  C C   . PHE C  1 22  ? -16.358  43.050  -50.941  1.00 32.78  ? 22  PHE C C   1 
ATOM   8647  O O   . PHE C  1 22  ? -16.715  41.995  -51.460  1.00 32.25  ? 22  PHE C O   1 
ATOM   8648  C CB  . PHE C  1 22  ? -13.983  43.246  -51.850  1.00 32.66  ? 22  PHE C CB  1 
ATOM   8649  C CG  . PHE C  1 22  ? -14.175  44.476  -52.715  1.00 31.42  ? 22  PHE C CG  1 
ATOM   8650  C CD1 . PHE C  1 22  ? -15.245  44.572  -53.592  1.00 31.21  ? 22  PHE C CD1 1 
ATOM   8651  C CD2 . PHE C  1 22  ? -13.312  45.556  -52.612  1.00 33.34  ? 22  PHE C CD2 1 
ATOM   8652  C CE1 . PHE C  1 22  ? -15.434  45.713  -54.361  1.00 31.81  ? 22  PHE C CE1 1 
ATOM   8653  C CE2 . PHE C  1 22  ? -13.501  46.698  -53.387  1.00 32.69  ? 22  PHE C CE2 1 
ATOM   8654  C CZ  . PHE C  1 22  ? -14.566  46.784  -54.246  1.00 31.93  ? 22  PHE C CZ  1 
ATOM   8655  N N   . ILE C  1 23  ? -17.197  44.059  -50.703  1.00 32.77  ? 23  ILE C N   1 
ATOM   8656  C CA  . ILE C  1 23  ? -18.617  43.912  -50.974  1.00 32.65  ? 23  ILE C CA  1 
ATOM   8657  C C   . ILE C  1 23  ? -18.892  44.176  -52.455  1.00 30.66  ? 23  ILE C C   1 
ATOM   8658  O O   . ILE C  1 23  ? -18.764  45.302  -52.972  1.00 26.99  ? 23  ILE C O   1 
ATOM   8659  C CB  . ILE C  1 23  ? -19.453  44.827  -50.069  1.00 35.93  ? 23  ILE C CB  1 
ATOM   8660  C CG1 . ILE C  1 23  ? -19.093  44.677  -48.578  1.00 36.71  ? 23  ILE C CG1 1 
ATOM   8661  C CG2 . ILE C  1 23  ? -20.937  44.584  -50.334  1.00 36.35  ? 23  ILE C CG2 1 
ATOM   8662  C CD1 . ILE C  1 23  ? -19.620  45.803  -47.713  1.00 37.74  ? 23  ILE C CD1 1 
ATOM   8663  N N   . LYS C  1 24  ? -19.261  43.069  -53.111  1.00 31.70  ? 24  LYS C N   1 
ATOM   8664  C CA  . LYS C  1 24  ? -19.694  43.029  -54.492  1.00 31.85  ? 24  LYS C CA  1 
ATOM   8665  C C   . LYS C  1 24  ? -21.217  42.950  -54.519  1.00 32.25  ? 24  LYS C C   1 
ATOM   8666  O O   . LYS C  1 24  ? -21.782  41.880  -54.645  1.00 33.49  ? 24  LYS C O   1 
ATOM   8667  C CB  . LYS C  1 24  ? -19.045  41.827  -55.184  1.00 31.85  ? 24  LYS C CB  1 
ATOM   8668  C CG  . LYS C  1 24  ? -17.534  41.875  -55.187  1.00 33.38  ? 24  LYS C CG  1 
ATOM   8669  C CD  . LYS C  1 24  ? -16.900  40.924  -56.194  1.00 33.67  ? 24  LYS C CD  1 
ATOM   8670  C CE  . LYS C  1 24  ? -16.739  39.573  -55.697  1.00 37.98  ? 24  LYS C CE  1 
ATOM   8671  N NZ  . LYS C  1 24  ? -16.425  38.645  -56.800  1.00 42.44  ? 24  LYS C NZ  1 
ATOM   8672  N N   . ALA C  1 25  ? -21.871  44.106  -54.443  1.00 33.33  ? 25  ALA C N   1 
ATOM   8673  C CA  . ALA C  1 25  ? -23.306  44.154  -54.280  1.00 32.75  ? 25  ALA C CA  1 
ATOM   8674  C C   . ALA C  1 25  ? -23.945  44.672  -55.553  1.00 33.52  ? 25  ALA C C   1 
ATOM   8675  O O   . ALA C  1 25  ? -23.255  45.057  -56.503  1.00 35.04  ? 25  ALA C O   1 
ATOM   8676  C CB  . ALA C  1 25  ? -23.657  45.044  -53.109  1.00 35.23  ? 25  ALA C CB  1 
ATOM   8677  N N   . ILE C  1 26  ? -25.277  44.636  -55.546  1.00 33.02  ? 26  ILE C N   1 
ATOM   8678  C CA  . ILE C  1 26  ? -26.085  45.273  -56.562  1.00 31.85  ? 26  ILE C CA  1 
ATOM   8679  C C   . ILE C  1 26  ? -27.343  45.762  -55.874  1.00 30.82  ? 26  ILE C C   1 
ATOM   8680  O O   . ILE C  1 26  ? -27.813  45.126  -54.941  1.00 28.61  ? 26  ILE C O   1 
ATOM   8681  C CB  . ILE C  1 26  ? -26.380  44.319  -57.739  1.00 34.31  ? 26  ILE C CB  1 
ATOM   8682  C CG1 . ILE C  1 26  ? -26.939  45.066  -58.934  1.00 32.42  ? 26  ILE C CG1 1 
ATOM   8683  C CG2 . ILE C  1 26  ? -27.293  43.155  -57.330  1.00 35.21  ? 26  ILE C CG2 1 
ATOM   8684  C CD1 . ILE C  1 26  ? -27.061  44.215  -60.181  1.00 32.94  ? 26  ILE C CD1 1 
ATOM   8685  N N   . GLY C  1 27  ? -27.800  46.955  -56.279  1.00 31.09  ? 27  GLY C N   1 
ATOM   8686  C CA  . GLY C  1 27  ? -29.102  47.461  -55.878  1.00 30.12  ? 27  GLY C CA  1 
ATOM   8687  C C   . GLY C  1 27  ? -30.199  46.516  -56.350  1.00 29.57  ? 27  GLY C C   1 
ATOM   8688  O O   . GLY C  1 27  ? -30.165  46.047  -57.495  1.00 30.52  ? 27  GLY C O   1 
ATOM   8689  N N   . TYR C  1 28  ? -31.135  46.209  -55.454  1.00 28.56  ? 28  TYR C N   1 
ATOM   8690  C CA  . TYR C  1 28  ? -32.164  45.230  -55.733  1.00 28.76  ? 28  TYR C CA  1 
ATOM   8691  C C   . TYR C  1 28  ? -33.468  45.681  -55.090  1.00 30.34  ? 28  TYR C C   1 
ATOM   8692  O O   . TYR C  1 28  ? -33.551  45.789  -53.871  1.00 30.96  ? 28  TYR C O   1 
ATOM   8693  C CB  . TYR C  1 28  ? -31.735  43.875  -55.170  1.00 29.58  ? 28  TYR C CB  1 
ATOM   8694  C CG  . TYR C  1 28  ? -32.825  42.833  -55.305  1.00 29.99  ? 28  TYR C CG  1 
ATOM   8695  C CD1 . TYR C  1 28  ? -33.496  42.681  -56.506  1.00 31.52  ? 28  TYR C CD1 1 
ATOM   8696  C CD2 . TYR C  1 28  ? -33.269  42.086  -54.228  1.00 31.20  ? 28  TYR C CD2 1 
ATOM   8697  C CE1 . TYR C  1 28  ? -34.540  41.772  -56.654  1.00 32.09  ? 28  TYR C CE1 1 
ATOM   8698  C CE2 . TYR C  1 28  ? -34.290  41.142  -54.366  1.00 32.85  ? 28  TYR C CE2 1 
ATOM   8699  C CZ  . TYR C  1 28  ? -34.927  40.976  -55.591  1.00 32.80  ? 28  TYR C CZ  1 
ATOM   8700  O OH  . TYR C  1 28  ? -35.959  40.097  -55.812  1.00 33.82  ? 28  TYR C OH  1 
ATOM   8701  N N   . GLU C  1 29  ? -34.505  45.900  -55.908  1.00 31.97  ? 29  GLU C N   1 
ATOM   8702  C CA  . GLU C  1 29  ? -35.799  46.352  -55.409  1.00 33.14  ? 29  GLU C CA  1 
ATOM   8703  C C   . GLU C  1 29  ? -36.880  45.385  -55.868  1.00 33.95  ? 29  GLU C C   1 
ATOM   8704  O O   . GLU C  1 29  ? -37.282  45.408  -57.026  1.00 34.70  ? 29  GLU C O   1 
ATOM   8705  C CB  . GLU C  1 29  ? -36.040  47.780  -55.906  1.00 33.59  ? 29  GLU C CB  1 
ATOM   8706  C CG  . GLU C  1 29  ? -37.432  48.298  -55.579  1.00 34.75  ? 29  GLU C CG  1 
ATOM   8707  C CD  . GLU C  1 29  ? -37.683  49.764  -55.897  1.00 35.14  ? 29  GLU C CD  1 
ATOM   8708  O OE1 . GLU C  1 29  ? -37.568  50.239  -57.077  1.00 32.59  ? 29  GLU C OE1 1 
ATOM   8709  O OE2 . GLU C  1 29  ? -38.023  50.418  -54.886  1.00 35.16  ? 29  GLU C OE2 1 
ATOM   8710  N N   . ILE C  1 30  ? -37.299  44.493  -54.959  1.00 35.83  ? 30  ILE C N   1 
ATOM   8711  C CA  . ILE C  1 30  ? -38.480  43.663  -55.170  1.00 35.10  ? 30  ILE C CA  1 
ATOM   8712  C C   . ILE C  1 30  ? -39.733  44.541  -55.141  1.00 35.63  ? 30  ILE C C   1 
ATOM   8713  O O   . ILE C  1 30  ? -39.691  45.656  -54.594  1.00 36.83  ? 30  ILE C O   1 
ATOM   8714  C CB  . ILE C  1 30  ? -38.544  42.539  -54.121  1.00 35.31  ? 30  ILE C CB  1 
ATOM   8715  C CG1 . ILE C  1 30  ? -39.548  41.428  -54.500  1.00 34.83  ? 30  ILE C CG1 1 
ATOM   8716  C CG2 . ILE C  1 30  ? -38.863  43.113  -52.751  1.00 37.36  ? 30  ILE C CG2 1 
ATOM   8717  C CD1 . ILE C  1 30  ? -39.335  40.855  -55.891  1.00 33.53  ? 30  ILE C CD1 1 
ATOM   8718  N N   . GLY C  1 31  ? -40.816  44.046  -55.770  1.00 34.57  ? 31  GLY C N   1 
ATOM   8719  C CA  . GLY C  1 31  ? -42.090  44.753  -55.837  1.00 36.18  ? 31  GLY C CA  1 
ATOM   8720  C C   . GLY C  1 31  ? -42.067  45.983  -56.767  1.00 35.91  ? 31  GLY C C   1 
ATOM   8721  O O   . GLY C  1 31  ? -42.849  46.903  -56.587  1.00 35.69  ? 31  GLY C O   1 
ATOM   8722  N N   . ALA C  1 32  ? -41.225  45.955  -57.812  1.00 34.12  ? 32  ALA C N   1 
ATOM   8723  C CA  . ALA C  1 32  ? -41.055  47.044  -58.754  1.00 33.41  ? 32  ALA C CA  1 
ATOM   8724  C C   . ALA C  1 32  ? -41.104  46.548  -60.197  1.00 31.29  ? 32  ALA C C   1 
ATOM   8725  O O   . ALA C  1 32  ? -40.550  47.189  -61.095  1.00 28.87  ? 32  ALA C O   1 
ATOM   8726  C CB  . ALA C  1 32  ? -39.741  47.715  -58.480  1.00 34.15  ? 32  ALA C CB  1 
ATOM   8727  N N   . ARG C  1 33  ? -41.831  45.448  -60.411  1.00 31.09  ? 33  ARG C N   1 
ATOM   8728  C CA  . ARG C  1 33  ? -42.138  44.995  -61.752  1.00 32.03  ? 33  ARG C CA  1 
ATOM   8729  C C   . ARG C  1 33  ? -43.015  46.023  -62.468  1.00 32.62  ? 33  ARG C C   1 
ATOM   8730  O O   . ARG C  1 33  ? -43.629  46.893  -61.839  1.00 33.07  ? 33  ARG C O   1 
ATOM   8731  C CB  . ARG C  1 33  ? -42.903  43.667  -61.738  1.00 34.38  ? 33  ARG C CB  1 
ATOM   8732  C CG  . ARG C  1 33  ? -41.978  42.486  -61.986  1.00 35.08  ? 33  ARG C CG  1 
ATOM   8733  C CD  . ARG C  1 33  ? -40.804  42.371  -61.025  1.00 33.88  ? 33  ARG C CD  1 
ATOM   8734  N NE  . ARG C  1 33  ? -40.091  41.129  -61.335  1.00 32.83  ? 33  ARG C NE  1 
ATOM   8735  C CZ  . ARG C  1 33  ? -39.103  40.655  -60.606  1.00 31.60  ? 33  ARG C CZ  1 
ATOM   8736  N NH1 . ARG C  1 33  ? -38.672  41.328  -59.551  1.00 31.68  ? 33  ARG C NH1 1 
ATOM   8737  N NH2 . ARG C  1 33  ? -38.545  39.509  -60.931  1.00 30.94  ? 33  ARG C NH2 1 
ATOM   8738  N N   . PRO C  1 34  ? -43.145  45.924  -63.811  1.00 31.25  ? 34  PRO C N   1 
ATOM   8739  C CA  . PRO C  1 34  ? -44.114  46.746  -64.524  1.00 32.45  ? 34  PRO C CA  1 
ATOM   8740  C C   . PRO C  1 34  ? -45.471  46.551  -63.878  1.00 33.84  ? 34  PRO C C   1 
ATOM   8741  O O   . PRO C  1 34  ? -45.825  45.443  -63.520  1.00 34.38  ? 34  PRO C O   1 
ATOM   8742  C CB  . PRO C  1 34  ? -44.036  46.244  -65.953  1.00 32.05  ? 34  PRO C CB  1 
ATOM   8743  C CG  . PRO C  1 34  ? -42.613  45.671  -66.035  1.00 30.68  ? 34  PRO C CG  1 
ATOM   8744  C CD  . PRO C  1 34  ? -42.388  45.024  -64.692  1.00 30.35  ? 34  PRO C CD  1 
ATOM   8745  N N   . GLY C  1 35  ? -46.155  47.665  -63.624  1.00 36.05  ? 35  GLY C N   1 
ATOM   8746  C CA  . GLY C  1 35  ? -47.508  47.625  -63.088  1.00 39.02  ? 35  GLY C CA  1 
ATOM   8747  C C   . GLY C  1 35  ? -47.545  47.694  -61.563  1.00 39.60  ? 35  GLY C C   1 
ATOM   8748  O O   . GLY C  1 35  ? -48.628  47.800  -60.984  1.00 41.44  ? 35  GLY C O   1 
ATOM   8749  N N   . GLN C  1 36  ? -46.359  47.640  -60.940  1.00 39.58  ? 36  GLN C N   1 
ATOM   8750  C CA  . GLN C  1 36  ? -46.226  47.669  -59.494  1.00 40.02  ? 36  GLN C CA  1 
ATOM   8751  C C   . GLN C  1 36  ? -45.641  49.006  -59.054  1.00 39.86  ? 36  GLN C C   1 
ATOM   8752  O O   . GLN C  1 36  ? -44.944  49.669  -59.816  1.00 37.91  ? 36  GLN C O   1 
ATOM   8753  C CB  . GLN C  1 36  ? -45.320  46.564  -58.964  1.00 39.96  ? 36  GLN C CB  1 
ATOM   8754  C CG  . GLN C  1 36  ? -45.785  45.149  -59.299  1.00 40.32  ? 36  GLN C CG  1 
ATOM   8755  C CD  . GLN C  1 36  ? -44.968  44.077  -58.601  1.00 40.61  ? 36  GLN C CD  1 
ATOM   8756  O OE1 . GLN C  1 36  ? -43.737  44.100  -58.488  1.00 38.28  ? 36  GLN C OE1 1 
ATOM   8757  N NE2 . GLN C  1 36  ? -45.652  43.066  -58.123  1.00 44.44  ? 36  GLN C NE2 1 
ATOM   8758  N N   . ALA C  1 37  ? -45.939  49.363  -57.799  1.00 41.60  ? 37  ALA C N   1 
ATOM   8759  C CA  . ALA C  1 37  ? -45.355  50.515  -57.134  1.00 42.07  ? 37  ALA C CA  1 
ATOM   8760  C C   . ALA C  1 37  ? -45.089  50.154  -55.678  1.00 42.84  ? 37  ALA C C   1 
ATOM   8761  O O   . ALA C  1 37  ? -46.016  50.095  -54.873  1.00 45.11  ? 37  ALA C O   1 
ATOM   8762  C CB  . ALA C  1 37  ? -46.292  51.696  -57.240  1.00 43.83  ? 37  ALA C CB  1 
ATOM   8763  N N   . PRO C  1 38  ? -43.828  49.879  -55.283  1.00 41.20  ? 38  PRO C N   1 
ATOM   8764  C CA  . PRO C  1 38  ? -43.564  49.348  -53.942  1.00 42.80  ? 38  PRO C CA  1 
ATOM   8765  C C   . PRO C  1 38  ? -43.925  50.253  -52.755  1.00 45.58  ? 38  PRO C C   1 
ATOM   8766  O O   . PRO C  1 38  ? -44.078  49.754  -51.653  1.00 45.45  ? 38  PRO C O   1 
ATOM   8767  C CB  . PRO C  1 38  ? -42.074  49.004  -54.001  1.00 40.30  ? 38  PRO C CB  1 
ATOM   8768  C CG  . PRO C  1 38  ? -41.537  49.953  -55.021  1.00 40.19  ? 38  PRO C CG  1 
ATOM   8769  C CD  . PRO C  1 38  ? -42.617  50.091  -56.073  1.00 39.60  ? 38  PRO C CD  1 
ATOM   8770  N N   . TYR C  1 39  ? -44.110  51.562  -52.982  1.00 47.78  ? 39  TYR C N   1 
ATOM   8771  C CA  . TYR C  1 39  ? -44.424  52.490  -51.902  1.00 50.27  ? 39  TYR C CA  1 
ATOM   8772  C C   . TYR C  1 39  ? -45.906  52.869  -51.918  1.00 52.76  ? 39  TYR C C   1 
ATOM   8773  O O   . TYR C  1 39  ? -46.309  53.700  -51.129  1.00 55.10  ? 39  TYR C O   1 
ATOM   8774  C CB  . TYR C  1 39  ? -43.506  53.725  -51.947  1.00 49.50  ? 39  TYR C CB  1 
ATOM   8775  C CG  . TYR C  1 39  ? -42.029  53.385  -51.755  1.00 48.17  ? 39  TYR C CG  1 
ATOM   8776  C CD1 . TYR C  1 39  ? -41.554  52.871  -50.550  1.00 47.43  ? 39  TYR C CD1 1 
ATOM   8777  C CD2 . TYR C  1 39  ? -41.114  53.542  -52.789  1.00 45.28  ? 39  TYR C CD2 1 
ATOM   8778  C CE1 . TYR C  1 39  ? -40.219  52.538  -50.382  1.00 47.42  ? 39  TYR C CE1 1 
ATOM   8779  C CE2 . TYR C  1 39  ? -39.777  53.211  -52.631  1.00 43.67  ? 39  TYR C CE2 1 
ATOM   8780  C CZ  . TYR C  1 39  ? -39.325  52.706  -51.425  1.00 44.57  ? 39  TYR C CZ  1 
ATOM   8781  O OH  . TYR C  1 39  ? -38.007  52.377  -51.265  1.00 42.48  ? 39  TYR C OH  1 
ATOM   8782  N N   . GLU C  1 40  ? -46.734  52.253  -52.775  1.00 57.91  ? 40  GLU C N   1 
ATOM   8783  C CA  . GLU C  1 40  ? -48.175  52.518  -52.776  1.00 59.91  ? 40  GLU C CA  1 
ATOM   8784  C C   . GLU C  1 40  ? -48.987  51.229  -52.738  1.00 57.37  ? 40  GLU C C   1 
ATOM   8785  O O   . GLU C  1 40  ? -50.018  51.197  -52.101  1.00 57.18  ? 40  GLU C O   1 
ATOM   8786  C CB  . GLU C  1 40  ? -48.609  53.350  -53.977  1.00 62.45  ? 40  GLU C CB  1 
ATOM   8787  C CG  . GLU C  1 40  ? -48.302  54.831  -53.782  1.00 70.23  ? 40  GLU C CG  1 
ATOM   8788  C CD  . GLU C  1 40  ? -48.067  55.507  -55.110  1.00 75.95  ? 40  GLU C CD  1 
ATOM   8789  O OE1 . GLU C  1 40  ? -47.979  54.701  -56.069  1.00 78.57  ? 40  GLU C OE1 1 
ATOM   8790  O OE2 . GLU C  1 40  ? -47.991  56.762  -55.207  1.00 75.05  ? 40  GLU C OE2 1 
ATOM   8791  N N   . ASP C  1 41  ? -48.531  50.176  -53.416  1.00 57.05  ? 41  ASP C N   1 
ATOM   8792  C CA  . ASP C  1 41  ? -49.220  48.897  -53.387  1.00 59.61  ? 41  ASP C CA  1 
ATOM   8793  C C   . ASP C  1 41  ? -49.151  48.274  -51.988  1.00 59.40  ? 41  ASP C C   1 
ATOM   8794  O O   . ASP C  1 41  ? -48.192  48.476  -51.247  1.00 57.08  ? 41  ASP C O   1 
ATOM   8795  C CB  . ASP C  1 41  ? -48.623  47.896  -54.368  1.00 60.65  ? 41  ASP C CB  1 
ATOM   8796  C CG  . ASP C  1 41  ? -48.562  48.278  -55.842  1.00 61.67  ? 41  ASP C CG  1 
ATOM   8797  O OD1 . ASP C  1 41  ? -49.251  49.252  -56.258  1.00 60.42  ? 41  ASP C OD1 1 
ATOM   8798  O OD2 . ASP C  1 41  ? -47.773  47.610  -56.552  1.00 64.37  ? 41  ASP C OD2 1 
ATOM   8799  N N   . GLU C  1 42  ? -50.174  47.480  -51.656  1.00 58.89  ? 42  GLU C N   1 
ATOM   8800  C CA  . GLU C  1 42  ? -50.125  46.576  -50.526  1.00 61.80  ? 42  GLU C CA  1 
ATOM   8801  C C   . GLU C  1 42  ? -48.904  45.659  -50.647  1.00 61.36  ? 42  GLU C C   1 
ATOM   8802  O O   . GLU C  1 42  ? -48.564  45.193  -51.731  1.00 58.55  ? 42  GLU C O   1 
ATOM   8803  C CB  . GLU C  1 42  ? -51.477  45.861  -50.497  1.00 67.19  ? 42  GLU C CB  1 
ATOM   8804  C CG  . GLU C  1 42  ? -51.474  44.570  -49.681  1.00 71.49  ? 42  GLU C CG  1 
ATOM   8805  C CD  . GLU C  1 42  ? -52.821  44.227  -49.074  1.00 74.94  ? 42  GLU C CD  1 
ATOM   8806  O OE1 . GLU C  1 42  ? -53.689  45.128  -49.028  1.00 82.89  ? 42  GLU C OE1 1 
ATOM   8807  O OE2 . GLU C  1 42  ? -52.994  43.073  -48.638  1.00 73.06  ? 42  GLU C OE2 1 
ATOM   8808  N N   . ARG C  1 43  ? -48.249  45.394  -49.515  1.00 62.69  ? 43  ARG C N   1 
ATOM   8809  C CA  . ARG C  1 43  ? -46.954  44.737  -49.503  1.00 65.56  ? 43  ARG C CA  1 
ATOM   8810  C C   . ARG C  1 43  ? -47.133  43.217  -49.579  1.00 59.60  ? 43  ARG C C   1 
ATOM   8811  O O   . ARG C  1 43  ? -47.999  42.654  -48.933  1.00 62.07  ? 43  ARG C O   1 
ATOM   8812  C CB  . ARG C  1 43  ? -46.211  45.169  -48.234  1.00 73.51  ? 43  ARG C CB  1 
ATOM   8813  C CG  . ARG C  1 43  ? -44.742  45.536  -48.425  1.00 77.07  ? 43  ARG C CG  1 
ATOM   8814  C CD  . ARG C  1 43  ? -44.022  45.631  -47.071  1.00 80.54  ? 43  ARG C CD  1 
ATOM   8815  N NE  . ARG C  1 43  ? -43.941  44.270  -46.527  1.00 77.96  ? 43  ARG C NE  1 
ATOM   8816  C CZ  . ARG C  1 43  ? -42.989  43.379  -46.820  1.00 76.86  ? 43  ARG C CZ  1 
ATOM   8817  N NH1 . ARG C  1 43  ? -41.740  43.789  -47.031  1.00 65.85  ? 43  ARG C NH1 1 
ATOM   8818  N NH2 . ARG C  1 43  ? -43.293  42.077  -46.788  1.00 72.43  ? 43  ARG C NH2 1 
ATOM   8819  N N   . LYS C  1 44  ? -46.317  42.564  -50.403  1.00 55.80  ? 44  LYS C N   1 
ATOM   8820  C CA  . LYS C  1 44  ? -46.303  41.117  -50.542  1.00 56.21  ? 44  LYS C CA  1 
ATOM   8821  C C   . LYS C  1 44  ? -44.861  40.604  -50.533  1.00 50.36  ? 44  LYS C C   1 
ATOM   8822  O O   . LYS C  1 44  ? -43.947  41.270  -51.018  1.00 46.61  ? 44  LYS C O   1 
ATOM   8823  C CB  . LYS C  1 44  ? -46.957  40.669  -51.855  1.00 60.79  ? 44  LYS C CB  1 
ATOM   8824  C CG  . LYS C  1 44  ? -48.483  40.668  -51.891  1.00 66.11  ? 44  LYS C CG  1 
ATOM   8825  C CD  . LYS C  1 44  ? -49.081  40.312  -53.251  1.00 69.14  ? 44  LYS C CD  1 
ATOM   8826  C CE  . LYS C  1 44  ? -50.546  40.692  -53.384  1.00 75.64  ? 44  LYS C CE  1 
ATOM   8827  N NZ  . LYS C  1 44  ? -51.438  40.043  -52.409  1.00 77.67  ? 44  LYS C NZ  1 
ATOM   8828  N N   . ASP C  1 45  ? -44.676  39.386  -50.018  1.00 48.20  ? 45  ASP C N   1 
ATOM   8829  C CA  . ASP C  1 45  ? -43.366  38.748  -49.951  1.00 46.70  ? 45  ASP C CA  1 
ATOM   8830  C C   . ASP C  1 45  ? -42.757  38.509  -51.342  1.00 44.66  ? 45  ASP C C   1 
ATOM   8831  O O   . ASP C  1 45  ? -41.559  38.746  -51.536  1.00 41.88  ? 45  ASP C O   1 
ATOM   8832  C CB  . ASP C  1 45  ? -43.447  37.475  -49.126  1.00 47.25  ? 45  ASP C CB  1 
ATOM   8833  C CG  . ASP C  1 45  ? -43.584  37.689  -47.628  1.00 48.56  ? 45  ASP C CG  1 
ATOM   8834  O OD1 . ASP C  1 45  ? -43.235  38.787  -47.166  1.00 51.93  ? 45  ASP C OD1 1 
ATOM   8835  O OD2 . ASP C  1 45  ? -44.053  36.767  -46.943  1.00 50.52  ? 45  ASP C OD2 1 
ATOM   8836  N N   . GLU C  1 46  ? -43.572  38.019  -52.294  1.00 44.48  ? 46  GLU C N   1 
ATOM   8837  C CA  . GLU C  1 46  ? -43.157  37.776  -53.668  1.00 43.33  ? 46  GLU C CA  1 
ATOM   8838  C C   . GLU C  1 46  ? -42.020  36.758  -53.690  1.00 40.63  ? 46  GLU C C   1 
ATOM   8839  O O   . GLU C  1 46  ? -41.054  36.935  -54.408  1.00 38.94  ? 46  GLU C O   1 
ATOM   8840  C CB  . GLU C  1 46  ? -42.719  39.095  -54.311  1.00 44.20  ? 46  GLU C CB  1 
ATOM   8841  C CG  . GLU C  1 46  ? -43.811  40.160  -54.383  1.00 48.29  ? 46  GLU C CG  1 
ATOM   8842  C CD  . GLU C  1 46  ? -44.221  40.455  -55.810  1.00 50.49  ? 46  GLU C CD  1 
ATOM   8843  O OE1 . GLU C  1 46  ? -44.721  39.566  -56.524  1.00 60.76  ? 46  GLU C OE1 1 
ATOM   8844  O OE2 . GLU C  1 46  ? -43.975  41.577  -56.216  1.00 49.24  ? 46  GLU C OE2 1 
ATOM   8845  N N   . LEU C  1 47  ? -42.144  35.688  -52.908  1.00 41.18  ? 47  LEU C N   1 
ATOM   8846  C CA  . LEU C  1 47  ? -41.055  34.751  -52.719  1.00 41.33  ? 47  LEU C CA  1 
ATOM   8847  C C   . LEU C  1 47  ? -40.587  34.149  -54.044  1.00 42.35  ? 47  LEU C C   1 
ATOM   8848  O O   . LEU C  1 47  ? -39.378  34.093  -54.281  1.00 40.06  ? 47  LEU C O   1 
ATOM   8849  C CB  . LEU C  1 47  ? -41.438  33.685  -51.698  1.00 42.78  ? 47  LEU C CB  1 
ATOM   8850  C CG  . LEU C  1 47  ? -41.757  34.260  -50.315  1.00 44.51  ? 47  LEU C CG  1 
ATOM   8851  C CD1 . LEU C  1 47  ? -42.006  33.211  -49.280  1.00 44.27  ? 47  LEU C CD1 1 
ATOM   8852  C CD2 . LEU C  1 47  ? -40.628  35.241  -49.898  1.00 44.54  ? 47  LEU C CD2 1 
ATOM   8853  N N   . GLU C  1 48  ? -41.526  33.724  -54.906  1.00 43.32  ? 48  GLU C N   1 
ATOM   8854  C CA  . GLU C  1 48  ? -41.163  33.084  -56.165  1.00 42.15  ? 48  GLU C CA  1 
ATOM   8855  C C   . GLU C  1 48  ? -40.375  34.037  -57.063  1.00 41.71  ? 48  GLU C C   1 
ATOM   8856  O O   . GLU C  1 48  ? -39.367  33.659  -57.658  1.00 43.24  ? 48  GLU C O   1 
ATOM   8857  C CB  . GLU C  1 48  ? -42.404  32.529  -56.857  1.00 42.60  ? 48  GLU C CB  1 
ATOM   8858  C CG  . GLU C  1 48  ? -43.021  31.403  -56.043  1.00 44.22  ? 48  GLU C CG  1 
ATOM   8859  C CD  . GLU C  1 48  ? -42.038  30.275  -55.784  1.00 44.71  ? 48  GLU C CD  1 
ATOM   8860  O OE1 . GLU C  1 48  ? -41.310  29.910  -56.732  1.00 42.19  ? 48  GLU C OE1 1 
ATOM   8861  O OE2 . GLU C  1 48  ? -42.038  29.724  -54.659  1.00 47.35  ? 48  GLU C OE2 1 
ATOM   8862  N N   . LEU C  1 49  ? -40.809  35.284  -57.168  1.00 40.60  ? 49  LEU C N   1 
ATOM   8863  C CA  . LEU C  1 49  ? -40.059  36.206  -57.992  1.00 40.37  ? 49  LEU C CA  1 
ATOM   8864  C C   . LEU C  1 49  ? -38.699  36.473  -57.356  1.00 40.10  ? 49  LEU C C   1 
ATOM   8865  O O   . LEU C  1 49  ? -37.730  36.717  -58.063  1.00 39.14  ? 49  LEU C O   1 
ATOM   8866  C CB  . LEU C  1 49  ? -40.834  37.506  -58.223  1.00 40.60  ? 49  LEU C CB  1 
ATOM   8867  C CG  . LEU C  1 49  ? -41.968  37.423  -59.242  1.00 40.05  ? 49  LEU C CG  1 
ATOM   8868  C CD1 . LEU C  1 49  ? -42.628  38.769  -59.396  1.00 40.45  ? 49  LEU C CD1 1 
ATOM   8869  C CD2 . LEU C  1 49  ? -41.423  36.915  -60.558  1.00 39.60  ? 49  LEU C CD2 1 
ATOM   8870  N N   . MET C  1 50  ? -38.642  36.462  -56.024  1.00 42.55  ? 50  MET C N   1 
ATOM   8871  C CA  . MET C  1 50  ? -37.399  36.743  -55.322  1.00 42.88  ? 50  MET C CA  1 
ATOM   8872  C C   . MET C  1 50  ? -36.374  35.655  -55.601  1.00 41.61  ? 50  MET C C   1 
ATOM   8873  O O   . MET C  1 50  ? -35.217  35.984  -55.816  1.00 42.06  ? 50  MET C O   1 
ATOM   8874  C CB  . MET C  1 50  ? -37.602  36.883  -53.812  1.00 43.92  ? 50  MET C CB  1 
ATOM   8875  C CG  . MET C  1 50  ? -38.031  38.279  -53.422  1.00 45.37  ? 50  MET C CG  1 
ATOM   8876  S SD  . MET C  1 50  ? -37.929  38.582  -51.649  1.00 46.57  ? 50  MET C SD  1 
ATOM   8877  C CE  . MET C  1 50  ? -36.147  38.659  -51.452  1.00 43.81  ? 50  MET C CE  1 
ATOM   8878  N N   . LYS C  1 51  ? -36.807  34.387  -55.579  1.00 41.78  ? 51  LYS C N   1 
ATOM   8879  C CA  . LYS C  1 51  ? -35.923  33.249  -55.811  1.00 40.55  ? 51  LYS C CA  1 
ATOM   8880  C C   . LYS C  1 51  ? -35.273  33.355  -57.188  1.00 37.29  ? 51  LYS C C   1 
ATOM   8881  O O   . LYS C  1 51  ? -34.078  33.122  -57.334  1.00 36.69  ? 51  LYS C O   1 
ATOM   8882  C CB  . LYS C  1 51  ? -36.626  31.887  -55.760  1.00 40.41  ? 51  LYS C CB  1 
ATOM   8883  C CG  . LYS C  1 51  ? -37.109  31.447  -54.389  1.00 42.97  ? 51  LYS C CG  1 
ATOM   8884  C CD  . LYS C  1 51  ? -38.015  30.208  -54.398  1.00 44.22  ? 51  LYS C CD  1 
ATOM   8885  C CE  . LYS C  1 51  ? -38.698  29.976  -53.081  1.00 46.60  ? 51  LYS C CE  1 
ATOM   8886  N NZ  . LYS C  1 51  ? -39.728  28.936  -53.201  1.00 49.40  ? 51  LYS C NZ  1 
ATOM   8887  N N   . PHE C  1 52  ? -36.096  33.670  -58.188  1.00 34.67  ? 52  PHE C N   1 
ATOM   8888  C CA  . PHE C  1 52  ? -35.622  33.925  -59.534  1.00 33.63  ? 52  PHE C CA  1 
ATOM   8889  C C   . PHE C  1 52  ? -34.519  34.983  -59.517  1.00 31.68  ? 52  PHE C C   1 
ATOM   8890  O O   . PHE C  1 52  ? -33.451  34.752  -60.046  1.00 30.14  ? 52  PHE C O   1 
ATOM   8891  C CB  . PHE C  1 52  ? -36.830  34.316  -60.400  1.00 33.97  ? 52  PHE C CB  1 
ATOM   8892  C CG  . PHE C  1 52  ? -36.473  34.852  -61.780  1.00 32.53  ? 52  PHE C CG  1 
ATOM   8893  C CD1 . PHE C  1 52  ? -36.132  33.978  -62.805  1.00 31.46  ? 52  PHE C CD1 1 
ATOM   8894  C CD2 . PHE C  1 52  ? -36.485  36.221  -62.024  1.00 32.98  ? 52  PHE C CD2 1 
ATOM   8895  C CE1 . PHE C  1 52  ? -35.793  34.454  -64.043  1.00 31.53  ? 52  PHE C CE1 1 
ATOM   8896  C CE2 . PHE C  1 52  ? -36.156  36.712  -63.269  1.00 32.58  ? 52  PHE C CE2 1 
ATOM   8897  C CZ  . PHE C  1 52  ? -35.800  35.829  -64.272  1.00 32.91  ? 52  PHE C CZ  1 
ATOM   8898  N N   . ASP C  1 53  ? -34.792  36.138  -58.899  1.00 33.62  ? 53  ASP C N   1 
ATOM   8899  C CA  . ASP C  1 53  ? -33.870  37.270  -58.863  1.00 32.83  ? 53  ASP C CA  1 
ATOM   8900  C C   . ASP C  1 53  ? -32.533  36.929  -58.180  1.00 31.93  ? 53  ASP C C   1 
ATOM   8901  O O   . ASP C  1 53  ? -31.442  37.247  -58.687  1.00 30.88  ? 53  ASP C O   1 
ATOM   8902  C CB  . ASP C  1 53  ? -34.568  38.437  -58.188  1.00 33.64  ? 53  ASP C CB  1 
ATOM   8903  C CG  . ASP C  1 53  ? -35.763  39.042  -58.930  1.00 33.97  ? 53  ASP C CG  1 
ATOM   8904  O OD1 . ASP C  1 53  ? -35.829  38.960  -60.201  1.00 31.02  ? 53  ASP C OD1 1 
ATOM   8905  O OD2 . ASP C  1 53  ? -36.638  39.567  -58.205  1.00 33.15  ? 53  ASP C OD2 1 
ATOM   8906  N N   . LEU C  1 54  ? -32.617  36.294  -57.009  1.00 31.66  ? 54  LEU C N   1 
ATOM   8907  C CA  . LEU C  1 54  ? -31.444  35.968  -56.211  1.00 32.43  ? 54  LEU C CA  1 
ATOM   8908  C C   . LEU C  1 54  ? -30.519  35.007  -56.959  1.00 33.94  ? 54  LEU C C   1 
ATOM   8909  O O   . LEU C  1 54  ? -29.301  35.222  -56.995  1.00 30.67  ? 54  LEU C O   1 
ATOM   8910  C CB  . LEU C  1 54  ? -31.871  35.420  -54.852  1.00 33.09  ? 54  LEU C CB  1 
ATOM   8911  C CG  . LEU C  1 54  ? -32.544  36.424  -53.903  1.00 33.44  ? 54  LEU C CG  1 
ATOM   8912  C CD1 . LEU C  1 54  ? -32.744  35.854  -52.512  1.00 34.46  ? 54  LEU C CD1 1 
ATOM   8913  C CD2 . LEU C  1 54  ? -31.772  37.726  -53.815  1.00 32.71  ? 54  LEU C CD2 1 
ATOM   8914  N N   . GLU C  1 55  ? -31.102  33.963  -57.577  1.00 35.79  ? 55  GLU C N   1 
ATOM   8915  C CA  . GLU C  1 55  ? -30.343  33.075  -58.454  1.00 37.37  ? 55  GLU C CA  1 
ATOM   8916  C C   . GLU C  1 55  ? -29.658  33.881  -59.568  1.00 35.40  ? 55  GLU C C   1 
ATOM   8917  O O   . GLU C  1 55  ? -28.482  33.671  -59.888  1.00 33.46  ? 55  GLU C O   1 
ATOM   8918  C CB  . GLU C  1 55  ? -31.270  32.024  -59.072  1.00 41.09  ? 55  GLU C CB  1 
ATOM   8919  C CG  . GLU C  1 55  ? -30.565  30.944  -59.897  1.00 41.52  ? 55  GLU C CG  1 
ATOM   8920  C CD  . GLU C  1 55  ? -29.416  30.244  -59.186  1.00 43.89  ? 55  GLU C CD  1 
ATOM   8921  O OE1 . GLU C  1 55  ? -29.568  30.021  -57.967  1.00 44.55  ? 55  GLU C OE1 1 
ATOM   8922  O OE2 . GLU C  1 55  ? -28.387  29.908  -59.835  1.00 41.86  ? 55  GLU C OE2 1 
ATOM   8923  N N   . ASN C  1 56  ? -30.425  34.783  -60.192  1.00 32.31  ? 56  ASN C N   1 
ATOM   8924  C CA  . ASN C  1 56  ? -29.863  35.608  -61.232  1.00 31.79  ? 56  ASN C CA  1 
ATOM   8925  C C   . ASN C  1 56  ? -28.649  36.368  -60.679  1.00 29.65  ? 56  ASN C C   1 
ATOM   8926  O O   . ASN C  1 56  ? -27.611  36.436  -61.313  1.00 25.23  ? 56  ASN C O   1 
ATOM   8927  C CB  . ASN C  1 56  ? -30.922  36.547  -61.797  1.00 33.16  ? 56  ASN C CB  1 
ATOM   8928  C CG  . ASN C  1 56  ? -31.884  35.864  -62.737  1.00 33.08  ? 56  ASN C CG  1 
ATOM   8929  O OD1 . ASN C  1 56  ? -31.546  34.828  -63.303  1.00 32.72  ? 56  ASN C OD1 1 
ATOM   8930  N ND2 . ASN C  1 56  ? -33.049  36.466  -62.966  1.00 32.06  ? 56  ASN C ND2 1 
ATOM   8931  N N   . ILE C  1 57  ? -28.812  36.965  -59.497  1.00 30.88  ? 57  ILE C N   1 
ATOM   8932  C CA  . ILE C  1 57  ? -27.800  37.852  -58.950  1.00 31.81  ? 57  ILE C CA  1 
ATOM   8933  C C   . ILE C  1 57  ? -26.537  37.061  -58.564  1.00 31.85  ? 57  ILE C C   1 
ATOM   8934  O O   . ILE C  1 57  ? -25.416  37.548  -58.723  1.00 29.62  ? 57  ILE C O   1 
ATOM   8935  C CB  . ILE C  1 57  ? -28.423  38.691  -57.815  1.00 32.88  ? 57  ILE C CB  1 
ATOM   8936  C CG1 . ILE C  1 57  ? -29.312  39.784  -58.400  1.00 33.04  ? 57  ILE C CG1 1 
ATOM   8937  C CG2 . ILE C  1 57  ? -27.366  39.315  -56.907  1.00 34.59  ? 57  ILE C CG2 1 
ATOM   8938  C CD1 . ILE C  1 57  ? -30.366  40.304  -57.446  1.00 34.85  ? 57  ILE C CD1 1 
ATOM   8939  N N   . LYS C  1 58  ? -26.704  35.811  -58.113  1.00 32.39  ? 58  LYS C N   1 
ATOM   8940  C CA  . LYS C  1 58  ? -25.564  34.945  -57.849  1.00 33.44  ? 58  LYS C CA  1 
ATOM   8941  C C   . LYS C  1 58  ? -24.807  34.604  -59.131  1.00 31.35  ? 58  LYS C C   1 
ATOM   8942  O O   . LYS C  1 58  ? -23.572  34.668  -59.148  1.00 31.18  ? 58  LYS C O   1 
ATOM   8943  C CB  . LYS C  1 58  ? -25.992  33.661  -57.133  1.00 35.19  ? 58  LYS C CB  1 
ATOM   8944  C CG  . LYS C  1 58  ? -26.113  33.848  -55.638  1.00 37.80  ? 58  LYS C CG  1 
ATOM   8945  C CD  . LYS C  1 58  ? -27.051  32.852  -54.965  1.00 40.88  ? 58  LYS C CD  1 
ATOM   8946  C CE  . LYS C  1 58  ? -26.600  31.431  -54.942  1.00 40.50  ? 58  LYS C CE  1 
ATOM   8947  N NZ  . LYS C  1 58  ? -27.651  30.712  -54.237  1.00 41.05  ? 58  LYS C NZ  1 
ATOM   8948  N N   . GLU C  1 59  ? -25.553  34.276  -60.187  1.00 30.31  ? 59  GLU C N   1 
ATOM   8949  C CA  . GLU C  1 59  ? -24.991  33.936  -61.483  1.00 31.80  ? 59  GLU C CA  1 
ATOM   8950  C C   . GLU C  1 59  ? -24.273  35.141  -62.115  1.00 33.16  ? 59  GLU C C   1 
ATOM   8951  O O   . GLU C  1 59  ? -23.334  34.954  -62.902  1.00 36.98  ? 59  GLU C O   1 
ATOM   8952  C CB  . GLU C  1 59  ? -26.112  33.335  -62.343  1.00 33.70  ? 59  GLU C CB  1 
ATOM   8953  C CG  . GLU C  1 59  ? -26.568  31.923  -61.936  1.00 38.35  ? 59  GLU C CG  1 
ATOM   8954  C CD  . GLU C  1 59  ? -27.691  31.299  -62.788  1.00 42.78  ? 59  GLU C CD  1 
ATOM   8955  O OE1 . GLU C  1 59  ? -28.003  31.902  -63.855  1.00 46.81  ? 59  GLU C OE1 1 
ATOM   8956  O OE2 . GLU C  1 59  ? -28.320  30.267  -62.394  1.00 38.51  ? 59  GLU C OE2 1 
ATOM   8957  N N   . GLY C  1 60  ? -24.707  36.372  -61.795  1.00 29.14  ? 60  GLY C N   1 
ATOM   8958  C CA  . GLY C  1 60  ? -24.090  37.570  -62.335  1.00 30.00  ? 60  GLY C CA  1 
ATOM   8959  C C   . GLY C  1 60  ? -22.807  37.983  -61.595  1.00 29.96  ? 60  GLY C C   1 
ATOM   8960  O O   . GLY C  1 60  ? -22.190  39.000  -61.938  1.00 28.51  ? 60  GLY C O   1 
ATOM   8961  N N   . GLY C  1 61  ? -22.457  37.246  -60.529  1.00 28.96  ? 61  GLY C N   1 
ATOM   8962  C CA  . GLY C  1 61  ? -21.154  37.371  -59.888  1.00 29.18  ? 61  GLY C CA  1 
ATOM   8963  C C   . GLY C  1 61  ? -21.140  38.133  -58.554  1.00 31.08  ? 61  GLY C C   1 
ATOM   8964  O O   . GLY C  1 61  ? -20.050  38.328  -58.005  1.00 30.37  ? 61  GLY C O   1 
ATOM   8965  N N   . TYR C  1 62  ? -22.324  38.554  -58.044  1.00 30.79  ? 62  TYR C N   1 
ATOM   8966  C CA  . TYR C  1 62  ? -22.456  39.409  -56.867  1.00 29.21  ? 62  TYR C CA  1 
ATOM   8967  C C   . TYR C  1 62  ? -22.421  38.543  -55.609  1.00 29.86  ? 62  TYR C C   1 
ATOM   8968  O O   . TYR C  1 62  ? -22.793  37.367  -55.652  1.00 29.41  ? 62  TYR C O   1 
ATOM   8969  C CB  . TYR C  1 62  ? -23.746  40.243  -56.961  1.00 29.52  ? 62  TYR C CB  1 
ATOM   8970  C CG  . TYR C  1 62  ? -23.812  41.116  -58.208  1.00 29.29  ? 62  TYR C CG  1 
ATOM   8971  C CD1 . TYR C  1 62  ? -23.174  42.365  -58.254  1.00 30.02  ? 62  TYR C CD1 1 
ATOM   8972  C CD2 . TYR C  1 62  ? -24.451  40.686  -59.358  1.00 28.83  ? 62  TYR C CD2 1 
ATOM   8973  C CE1 . TYR C  1 62  ? -23.193  43.169  -59.384  1.00 26.76  ? 62  TYR C CE1 1 
ATOM   8974  C CE2 . TYR C  1 62  ? -24.475  41.483  -60.500  1.00 29.38  ? 62  TYR C CE2 1 
ATOM   8975  C CZ  . TYR C  1 62  ? -23.842  42.716  -60.509  1.00 27.64  ? 62  TYR C CZ  1 
ATOM   8976  O OH  . TYR C  1 62  ? -23.804  43.440  -61.653  1.00 29.30  ? 62  TYR C OH  1 
ATOM   8977  N N   . ASN C  1 63  ? -21.952  39.124  -54.486  1.00 29.42  ? 63  ASN C N   1 
ATOM   8978  C CA  . ASN C  1 63  ? -21.944  38.435  -53.204  1.00 29.46  ? 63  ASN C CA  1 
ATOM   8979  C C   . ASN C  1 63  ? -22.947  39.102  -52.243  1.00 29.79  ? 63  ASN C C   1 
ATOM   8980  O O   . ASN C  1 63  ? -23.159  38.586  -51.138  1.00 31.07  ? 63  ASN C O   1 
ATOM   8981  C CB  . ASN C  1 63  ? -20.528  38.329  -52.640  1.00 29.65  ? 63  ASN C CB  1 
ATOM   8982  C CG  . ASN C  1 63  ? -19.952  39.680  -52.259  1.00 31.81  ? 63  ASN C CG  1 
ATOM   8983  O OD1 . ASN C  1 63  ? -20.676  40.685  -52.129  1.00 32.83  ? 63  ASN C OD1 1 
ATOM   8984  N ND2 . ASN C  1 63  ? -18.654  39.727  -52.029  1.00 31.85  ? 63  ASN C ND2 1 
ATOM   8985  N N   . THR C  1 64  ? -23.589  40.209  -52.666  1.00 28.15  ? 64  THR C N   1 
ATOM   8986  C CA  . THR C  1 64  ? -24.409  41.044  -51.780  1.00 28.82  ? 64  THR C CA  1 
ATOM   8987  C C   . THR C  1 64  ? -25.543  41.717  -52.553  1.00 28.35  ? 64  THR C C   1 
ATOM   8988  O O   . THR C  1 64  ? -25.391  42.026  -53.741  1.00 27.29  ? 64  THR C O   1 
ATOM   8989  C CB  . THR C  1 64  ? -23.527  42.118  -51.141  1.00 28.67  ? 64  THR C CB  1 
ATOM   8990  O OG1 . THR C  1 64  ? -22.562  41.464  -50.335  1.00 30.21  ? 64  THR C OG1 1 
ATOM   8991  C CG2 . THR C  1 64  ? -24.253  43.104  -50.245  1.00 29.40  ? 64  THR C CG2 1 
ATOM   8992  N N   . ILE C  1 65  ? -26.661  41.991  -51.854  1.00 28.34  ? 65  ILE C N   1 
ATOM   8993  C CA  . ILE C  1 65  ? -27.702  42.858  -52.378  1.00 27.85  ? 65  ILE C CA  1 
ATOM   8994  C C   . ILE C  1 65  ? -27.855  44.064  -51.463  1.00 30.45  ? 65  ILE C C   1 
ATOM   8995  O O   . ILE C  1 65  ? -27.754  43.950  -50.240  1.00 31.54  ? 65  ILE C O   1 
ATOM   8996  C CB  . ILE C  1 65  ? -29.063  42.159  -52.543  1.00 27.01  ? 65  ILE C CB  1 
ATOM   8997  C CG1 . ILE C  1 65  ? -29.430  41.310  -51.341  1.00 28.48  ? 65  ILE C CG1 1 
ATOM   8998  C CG2 . ILE C  1 65  ? -29.072  41.343  -53.820  1.00 26.51  ? 65  ILE C CG2 1 
ATOM   8999  C CD1 . ILE C  1 65  ? -30.918  41.003  -51.217  1.00 29.09  ? 65  ILE C CD1 1 
ATOM   9000  N N   . ARG C  1 66  ? -28.226  45.198  -52.085  1.00 31.44  ? 66  ARG C N   1 
ATOM   9001  C CA  . ARG C  1 66  ? -28.507  46.427  -51.373  1.00 31.51  ? 66  ARG C CA  1 
ATOM   9002  C C   . ARG C  1 66  ? -29.954  46.819  -51.643  1.00 31.32  ? 66  ARG C C   1 
ATOM   9003  O O   . ARG C  1 66  ? -30.376  46.828  -52.789  1.00 30.48  ? 66  ARG C O   1 
ATOM   9004  C CB  . ARG C  1 66  ? -27.427  47.424  -51.844  1.00 31.46  ? 66  ARG C CB  1 
ATOM   9005  C CG  . ARG C  1 66  ? -27.642  48.876  -51.419  1.00 32.07  ? 66  ARG C CG  1 
ATOM   9006  C CD  . ARG C  1 66  ? -28.604  49.690  -52.266  1.00 31.54  ? 66  ARG C CD  1 
ATOM   9007  N NE  . ARG C  1 66  ? -28.449  51.133  -52.014  1.00 32.74  ? 66  ARG C NE  1 
ATOM   9008  C CZ  . ARG C  1 66  ? -29.264  51.874  -51.271  1.00 32.30  ? 66  ARG C CZ  1 
ATOM   9009  N NH1 . ARG C  1 66  ? -30.207  51.317  -50.554  1.00 34.18  ? 66  ARG C NH1 1 
ATOM   9010  N NH2 . ARG C  1 66  ? -29.086  53.157  -51.169  1.00 32.90  ? 66  ARG C NH2 1 
ATOM   9011  N N   . THR C  1 67  ? -30.685  47.225  -50.599  1.00 34.50  ? 67  THR C N   1 
ATOM   9012  C CA  . THR C  1 67  ? -32.113  47.535  -50.708  1.00 35.31  ? 67  THR C CA  1 
ATOM   9013  C C   . THR C  1 67  ? -32.421  48.902  -50.084  1.00 36.37  ? 67  THR C C   1 
ATOM   9014  O O   . THR C  1 67  ? -31.582  49.476  -49.388  1.00 35.55  ? 67  THR C O   1 
ATOM   9015  C CB  . THR C  1 67  ? -32.946  46.436  -50.044  1.00 34.97  ? 67  THR C CB  1 
ATOM   9016  O OG1 . THR C  1 67  ? -32.687  46.470  -48.649  1.00 33.85  ? 67  THR C OG1 1 
ATOM   9017  C CG2 . THR C  1 67  ? -32.645  45.049  -50.576  1.00 35.31  ? 67  THR C CG2 1 
ATOM   9018  N N   . TRP C  1 68  ? -33.643  49.400  -50.352  1.00 37.22  ? 68  TRP C N   1 
ATOM   9019  C CA  . TRP C  1 68  ? -34.128  50.708  -49.881  1.00 37.78  ? 68  TRP C CA  1 
ATOM   9020  C C   . TRP C  1 68  ? -35.189  50.553  -48.794  1.00 38.82  ? 68  TRP C C   1 
ATOM   9021  O O   . TRP C  1 68  ? -35.378  51.451  -48.002  1.00 39.17  ? 68  TRP C O   1 
ATOM   9022  C CB  . TRP C  1 68  ? -34.668  51.539  -51.058  1.00 35.75  ? 68  TRP C CB  1 
ATOM   9023  C CG  . TRP C  1 68  ? -33.540  52.020  -51.924  1.00 34.53  ? 68  TRP C CG  1 
ATOM   9024  C CD1 . TRP C  1 68  ? -32.880  53.216  -51.810  1.00 33.65  ? 68  TRP C CD1 1 
ATOM   9025  C CD2 . TRP C  1 68  ? -32.846  51.253  -52.933  1.00 33.15  ? 68  TRP C CD2 1 
ATOM   9026  N NE1 . TRP C  1 68  ? -31.849  53.259  -52.709  1.00 32.99  ? 68  TRP C NE1 1 
ATOM   9027  C CE2 . TRP C  1 68  ? -31.785  52.069  -53.392  1.00 32.39  ? 68  TRP C CE2 1 
ATOM   9028  C CE3 . TRP C  1 68  ? -33.006  49.969  -53.482  1.00 33.14  ? 68  TRP C CE3 1 
ATOM   9029  C CZ2 . TRP C  1 68  ? -30.912  51.634  -54.393  1.00 31.70  ? 68  TRP C CZ2 1 
ATOM   9030  C CZ3 . TRP C  1 68  ? -32.119  49.530  -54.443  1.00 30.34  ? 68  TRP C CZ3 1 
ATOM   9031  C CH2 . TRP C  1 68  ? -31.089  50.350  -54.886  1.00 30.50  ? 68  TRP C CH2 1 
ATOM   9032  N N   . SER C  1 69  ? -35.923  49.440  -48.840  1.00 41.43  ? 69  SER C N   1 
ATOM   9033  C CA  . SER C  1 69  ? -37.018  49.178  -47.871  1.00 42.25  ? 69  SER C CA  1 
ATOM   9034  C C   . SER C  1 69  ? -36.806  47.837  -47.155  1.00 41.40  ? 69  SER C C   1 
ATOM   9035  O O   . SER C  1 69  ? -36.354  46.891  -47.805  1.00 38.73  ? 69  SER C O   1 
ATOM   9036  C CB  . SER C  1 69  ? -38.363  49.222  -48.524  1.00 43.41  ? 69  SER C CB  1 
ATOM   9037  O OG  . SER C  1 69  ? -39.392  49.266  -47.549  1.00 45.96  ? 69  SER C OG  1 
ATOM   9038  N N   . GLN C  1 70  ? -37.150  47.778  -45.871  1.00 43.75  ? 70  GLN C N   1 
ATOM   9039  C CA  . GLN C  1 70  ? -36.978  46.568  -45.030  1.00 45.12  ? 70  GLN C CA  1 
ATOM   9040  C C   . GLN C  1 70  ? -37.638  45.339  -45.632  1.00 46.27  ? 70  GLN C C   1 
ATOM   9041  O O   . GLN C  1 70  ? -38.657  45.461  -46.341  1.00 48.47  ? 70  GLN C O   1 
ATOM   9042  C CB  . GLN C  1 70  ? -37.701  46.674  -43.692  1.00 46.42  ? 70  GLN C CB  1 
ATOM   9043  C CG  . GLN C  1 70  ? -37.429  47.954  -42.913  1.00 49.12  ? 70  GLN C CG  1 
ATOM   9044  C CD  . GLN C  1 70  ? -38.290  49.114  -43.353  1.00 47.06  ? 70  GLN C CD  1 
ATOM   9045  O OE1 . GLN C  1 70  ? -37.955  49.829  -44.299  1.00 44.73  ? 70  GLN C OE1 1 
ATOM   9046  N NE2 . GLN C  1 70  ? -39.414  49.304  -42.681  1.00 48.37  ? 70  GLN C NE2 1 
ATOM   9047  N N   . TYR C  1 71  ? -37.085  44.185  -45.297  1.00 44.51  ? 71  TYR C N   1 
ATOM   9048  C CA  . TYR C  1 71  ? -37.710  42.926  -45.749  1.00 42.10  ? 71  TYR C CA  1 
ATOM   9049  C C   . TYR C  1 71  ? -38.494  42.340  -44.616  1.00 42.38  ? 71  TYR C C   1 
ATOM   9050  O O   . TYR C  1 71  ? -38.204  42.668  -43.458  1.00 42.71  ? 71  TYR C O   1 
ATOM   9051  C CB  . TYR C  1 71  ? -36.632  41.908  -46.118  1.00 40.15  ? 71  TYR C CB  1 
ATOM   9052  C CG  . TYR C  1 71  ? -36.053  41.983  -47.519  1.00 37.96  ? 71  TYR C CG  1 
ATOM   9053  C CD1 . TYR C  1 71  ? -36.810  42.436  -48.589  1.00 36.90  ? 71  TYR C CD1 1 
ATOM   9054  C CD2 . TYR C  1 71  ? -34.745  41.589  -47.759  1.00 36.74  ? 71  TYR C CD2 1 
ATOM   9055  C CE1 . TYR C  1 71  ? -36.277  42.497  -49.862  1.00 35.67  ? 71  TYR C CE1 1 
ATOM   9056  C CE2 . TYR C  1 71  ? -34.198  41.653  -49.026  1.00 34.97  ? 71  TYR C CE2 1 
ATOM   9057  C CZ  . TYR C  1 71  ? -34.969  42.106  -50.078  1.00 35.48  ? 71  TYR C CZ  1 
ATOM   9058  O OH  . TYR C  1 71  ? -34.427  42.163  -51.320  1.00 34.79  ? 71  TYR C OH  1 
ATOM   9059  N N   . SER C  1 72  ? -39.500  41.540  -44.935  1.00 42.38  ? 72  SER C N   1 
ATOM   9060  C CA  . SER C  1 72  ? -40.222  40.762  -43.949  1.00 43.97  ? 72  SER C CA  1 
ATOM   9061  C C   . SER C  1 72  ? -39.329  39.604  -43.522  1.00 44.19  ? 72  SER C C   1 
ATOM   9062  O O   . SER C  1 72  ? -38.252  39.415  -44.094  1.00 40.88  ? 72  SER C O   1 
ATOM   9063  C CB  . SER C  1 72  ? -41.535  40.244  -44.510  1.00 44.30  ? 72  SER C CB  1 
ATOM   9064  O OG  . SER C  1 72  ? -41.336  39.135  -45.389  1.00 42.25  ? 72  SER C OG  1 
ATOM   9065  N N   . GLU C  1 73  ? -39.823  38.837  -42.534  1.00 46.53  ? 73  GLU C N   1 
ATOM   9066  C CA  . GLU C  1 73  ? -39.110  37.693  -41.995  1.00 46.53  ? 73  GLU C CA  1 
ATOM   9067  C C   . GLU C  1 73  ? -38.969  36.672  -43.106  1.00 44.62  ? 73  GLU C C   1 
ATOM   9068  O O   . GLU C  1 73  ? -37.852  36.272  -43.406  1.00 44.32  ? 73  GLU C O   1 
ATOM   9069  C CB  . GLU C  1 73  ? -39.745  37.047  -40.766  1.00 49.60  ? 73  GLU C CB  1 
ATOM   9070  C CG  . GLU C  1 73  ? -38.833  35.990  -40.145  1.00 51.34  ? 73  GLU C CG  1 
ATOM   9071  C CD  . GLU C  1 73  ? -39.011  35.683  -38.668  1.00 53.62  ? 73  GLU C CD  1 
ATOM   9072  O OE1 . GLU C  1 73  ? -40.081  36.013  -38.097  1.00 55.03  ? 73  GLU C OE1 1 
ATOM   9073  O OE2 . GLU C  1 73  ? -38.023  35.147  -38.092  1.00 52.74  ? 73  GLU C OE2 1 
ATOM   9074  N N   . ASN C  1 74  ? -40.089  36.320  -43.750  1.00 43.95  ? 74  ASN C N   1 
ATOM   9075  C CA  . ASN C  1 74  ? -40.062  35.317  -44.805  1.00 42.81  ? 74  ASN C CA  1 
ATOM   9076  C C   . ASN C  1 74  ? -39.097  35.727  -45.909  1.00 42.31  ? 74  ASN C C   1 
ATOM   9077  O O   . ASN C  1 74  ? -38.404  34.864  -46.473  1.00 42.79  ? 74  ASN C O   1 
ATOM   9078  C CB  . ASN C  1 74  ? -41.428  35.050  -45.406  1.00 42.13  ? 74  ASN C CB  1 
ATOM   9079  C CG  . ASN C  1 74  ? -42.369  34.487  -44.376  1.00 42.79  ? 74  ASN C CG  1 
ATOM   9080  O OD1 . ASN C  1 74  ? -41.952  33.765  -43.450  1.00 42.62  ? 74  ASN C OD1 1 
ATOM   9081  N ND2 . ASN C  1 74  ? -43.637  34.795  -44.575  1.00 42.24  ? 74  ASN C ND2 1 
ATOM   9082  N N   . GLN C  1 75  ? -39.024  37.035  -46.181  1.00 40.20  ? 75  GLN C N   1 
ATOM   9083  C CA  . GLN C  1 75  ? -38.129  37.498  -47.221  1.00 38.89  ? 75  GLN C CA  1 
ATOM   9084  C C   . GLN C  1 75  ? -36.672  37.306  -46.802  1.00 38.29  ? 75  GLN C C   1 
ATOM   9085  O O   . GLN C  1 75  ? -35.877  36.799  -47.580  1.00 36.80  ? 75  GLN C O   1 
ATOM   9086  C CB  . GLN C  1 75  ? -38.438  38.932  -47.617  1.00 38.80  ? 75  GLN C CB  1 
ATOM   9087  C CG  . GLN C  1 75  ? -39.813  39.111  -48.236  1.00 39.79  ? 75  GLN C CG  1 
ATOM   9088  C CD  . GLN C  1 75  ? -40.048  40.551  -48.608  1.00 39.74  ? 75  GLN C CD  1 
ATOM   9089  O OE1 . GLN C  1 75  ? -39.816  41.468  -47.811  1.00 41.11  ? 75  GLN C OE1 1 
ATOM   9090  N NE2 . GLN C  1 75  ? -40.428  40.769  -49.855  1.00 39.12  ? 75  GLN C NE2 1 
ATOM   9091  N N   . LEU C  1 76  ? -36.334  37.740  -45.586  1.00 39.37  ? 76  LEU C N   1 
ATOM   9092  C CA  . LEU C  1 76  ? -35.027  37.503  -45.011  1.00 39.67  ? 76  LEU C CA  1 
ATOM   9093  C C   . LEU C  1 76  ? -34.679  36.008  -45.012  1.00 42.86  ? 76  LEU C C   1 
ATOM   9094  O O   . LEU C  1 76  ? -33.539  35.668  -45.367  1.00 46.17  ? 76  LEU C O   1 
ATOM   9095  C CB  . LEU C  1 76  ? -34.976  38.053  -43.593  1.00 40.72  ? 76  LEU C CB  1 
ATOM   9096  C CG  . LEU C  1 76  ? -34.725  39.547  -43.429  1.00 40.82  ? 76  LEU C CG  1 
ATOM   9097  C CD1 . LEU C  1 76  ? -34.685  39.818  -41.950  1.00 41.69  ? 76  LEU C CD1 1 
ATOM   9098  C CD2 . LEU C  1 76  ? -33.431  39.982  -44.081  1.00 41.54  ? 76  LEU C CD2 1 
ATOM   9099  N N   . LYS C  1 77  ? -35.612  35.121  -44.586  1.00 42.05  ? 77  LYS C N   1 
ATOM   9100  C CA  . LYS C  1 77  ? -35.316  33.696  -44.518  1.00 42.36  ? 77  LYS C CA  1 
ATOM   9101  C C   . LYS C  1 77  ? -34.725  33.270  -45.850  1.00 40.86  ? 77  LYS C C   1 
ATOM   9102  O O   . LYS C  1 77  ? -33.793  32.494  -45.882  1.00 42.15  ? 77  LYS C O   1 
ATOM   9103  C CB  . LYS C  1 77  ? -36.510  32.760  -44.282  1.00 44.45  ? 77  LYS C CB  1 
ATOM   9104  C CG  . LYS C  1 77  ? -37.057  32.674  -42.852  1.00 46.40  ? 77  LYS C CG  1 
ATOM   9105  C CD  . LYS C  1 77  ? -38.293  31.808  -42.616  1.00 47.52  ? 77  LYS C CD  1 
ATOM   9106  C CE  . LYS C  1 77  ? -38.661  31.722  -41.162  1.00 49.84  ? 77  LYS C CE  1 
ATOM   9107  N NZ  . LYS C  1 77  ? -40.020  31.246  -40.856  1.00 51.58  ? 77  LYS C NZ  1 
ATOM   9108  N N   . LEU C  1 78  ? -35.262  33.828  -46.936  1.00 40.88  ? 78  LEU C N   1 
ATOM   9109  C CA  . LEU C  1 78  ? -34.904  33.446  -48.291  1.00 40.73  ? 78  LEU C CA  1 
ATOM   9110  C C   . LEU C  1 78  ? -33.513  33.943  -48.677  1.00 38.32  ? 78  LEU C C   1 
ATOM   9111  O O   . LEU C  1 78  ? -32.739  33.220  -49.301  1.00 37.84  ? 78  LEU C O   1 
ATOM   9112  C CB  . LEU C  1 78  ? -35.964  34.044  -49.205  1.00 43.00  ? 78  LEU C CB  1 
ATOM   9113  C CG  . LEU C  1 78  ? -35.843  33.636  -50.669  1.00 45.87  ? 78  LEU C CG  1 
ATOM   9114  C CD1 . LEU C  1 78  ? -36.026  32.105  -50.739  1.00 48.46  ? 78  LEU C CD1 1 
ATOM   9115  C CD2 . LEU C  1 78  ? -36.847  34.386  -51.518  1.00 47.22  ? 78  LEU C CD2 1 
ATOM   9116  N N   . VAL C  1 79  ? -33.234  35.202  -48.344  1.00 35.69  ? 79  VAL C N   1 
ATOM   9117  C CA  . VAL C  1 79  ? -31.946  35.807  -48.613  1.00 34.27  ? 79  VAL C CA  1 
ATOM   9118  C C   . VAL C  1 79  ? -30.883  35.040  -47.836  1.00 34.53  ? 79  VAL C C   1 
ATOM   9119  O O   . VAL C  1 79  ? -29.836  34.733  -48.360  1.00 33.66  ? 79  VAL C O   1 
ATOM   9120  C CB  . VAL C  1 79  ? -31.945  37.311  -48.246  1.00 32.98  ? 79  VAL C CB  1 
ATOM   9121  C CG1 . VAL C  1 79  ? -30.561  37.914  -48.427  1.00 31.90  ? 79  VAL C CG1 1 
ATOM   9122  C CG2 . VAL C  1 79  ? -32.983  38.106  -49.026  1.00 31.64  ? 79  VAL C CG2 1 
ATOM   9123  N N   . GLN C  1 80  ? -31.167  34.736  -46.576  1.00 38.32  ? 80  GLN C N   1 
ATOM   9124  C CA  . GLN C  1 80  ? -30.251  33.991  -45.723  1.00 41.22  ? 80  GLN C CA  1 
ATOM   9125  C C   . GLN C  1 80  ? -29.818  32.701  -46.421  1.00 42.62  ? 80  GLN C C   1 
ATOM   9126  O O   . GLN C  1 80  ? -28.634  32.516  -46.660  1.00 42.14  ? 80  GLN C O   1 
ATOM   9127  C CB  . GLN C  1 80  ? -30.958  33.735  -44.390  1.00 42.95  ? 80  GLN C CB  1 
ATOM   9128  C CG  . GLN C  1 80  ? -30.107  33.131  -43.273  1.00 43.72  ? 80  GLN C CG  1 
ATOM   9129  C CD  . GLN C  1 80  ? -29.028  34.054  -42.740  1.00 43.69  ? 80  GLN C CD  1 
ATOM   9130  O OE1 . GLN C  1 80  ? -29.239  35.244  -42.466  1.00 40.98  ? 80  GLN C OE1 1 
ATOM   9131  N NE2 . GLN C  1 80  ? -27.838  33.494  -42.575  1.00 42.48  ? 80  GLN C NE2 1 
ATOM   9132  N N   . GLU C  1 81  ? -30.773  31.828  -46.783  1.00 44.52  ? 81  GLU C N   1 
ATOM   9133  C CA  . GLU C  1 81  ? -30.436  30.531  -47.353  1.00 45.77  ? 81  GLU C CA  1 
ATOM   9134  C C   . GLU C  1 81  ? -29.799  30.668  -48.743  1.00 41.37  ? 81  GLU C C   1 
ATOM   9135  O O   . GLU C  1 81  ? -29.067  29.782  -49.169  1.00 40.50  ? 81  GLU C O   1 
ATOM   9136  C CB  . GLU C  1 81  ? -31.655  29.607  -47.302  1.00 53.98  ? 81  GLU C CB  1 
ATOM   9137  C CG  . GLU C  1 81  ? -32.653  29.816  -48.437  1.00 62.65  ? 81  GLU C CG  1 
ATOM   9138  C CD  . GLU C  1 81  ? -34.075  29.333  -48.159  1.00 75.37  ? 81  GLU C CD  1 
ATOM   9139  O OE1 . GLU C  1 81  ? -34.291  28.773  -47.054  1.00 83.81  ? 81  GLU C OE1 1 
ATOM   9140  O OE2 . GLU C  1 81  ? -34.979  29.551  -49.017  1.00 75.81  ? 81  GLU C OE2 1 
ATOM   9141  N N   . SER C  1 82  ? -30.002  31.804  -49.430  1.00 38.55  ? 82  SER C N   1 
ATOM   9142  C CA  . SER C  1 82  ? -29.408  32.067  -50.739  1.00 35.09  ? 82  SER C CA  1 
ATOM   9143  C C   . SER C  1 82  ? -27.876  32.047  -50.717  1.00 33.77  ? 82  SER C C   1 
ATOM   9144  O O   . SER C  1 82  ? -27.260  31.827  -51.749  1.00 33.03  ? 82  SER C O   1 
ATOM   9145  C CB  . SER C  1 82  ? -29.880  33.436  -51.288  1.00 35.18  ? 82  SER C CB  1 
ATOM   9146  O OG  . SER C  1 82  ? -29.228  34.560  -50.692  1.00 32.35  ? 82  SER C OG  1 
ATOM   9147  N N   . GLY C  1 83  ? -27.268  32.410  -49.579  1.00 34.12  ? 83  GLY C N   1 
ATOM   9148  C CA  . GLY C  1 83  ? -25.842  32.662  -49.492  1.00 33.15  ? 83  GLY C CA  1 
ATOM   9149  C C   . GLY C  1 83  ? -25.489  34.143  -49.648  1.00 32.80  ? 83  GLY C C   1 
ATOM   9150  O O   . GLY C  1 83  ? -24.372  34.519  -49.324  1.00 32.29  ? 83  GLY C O   1 
ATOM   9151  N N   . LEU C  1 84  ? -26.411  34.989  -50.133  1.00 31.98  ? 84  LEU C N   1 
ATOM   9152  C CA  . LEU C  1 84  ? -26.062  36.378  -50.420  1.00 32.11  ? 84  LEU C CA  1 
ATOM   9153  C C   . LEU C  1 84  ? -26.072  37.207  -49.146  1.00 32.31  ? 84  LEU C C   1 
ATOM   9154  O O   . LEU C  1 84  ? -26.930  37.007  -48.301  1.00 32.33  ? 84  LEU C O   1 
ATOM   9155  C CB  . LEU C  1 84  ? -27.030  37.023  -51.404  1.00 31.70  ? 84  LEU C CB  1 
ATOM   9156  C CG  . LEU C  1 84  ? -26.902  36.576  -52.863  1.00 31.67  ? 84  LEU C CG  1 
ATOM   9157  C CD1 . LEU C  1 84  ? -28.208  36.921  -53.566  1.00 31.22  ? 84  LEU C CD1 1 
ATOM   9158  C CD2 . LEU C  1 84  ? -25.692  37.172  -53.585  1.00 30.72  ? 84  LEU C CD2 1 
ATOM   9159  N N   . LYS C  1 85  ? -25.190  38.212  -49.087  1.00 31.62  ? 85  LYS C N   1 
ATOM   9160  C CA  . LYS C  1 85  ? -25.200  39.155  -47.987  1.00 32.85  ? 85  LYS C CA  1 
ATOM   9161  C C   . LYS C  1 85  ? -26.182  40.261  -48.322  1.00 33.49  ? 85  LYS C C   1 
ATOM   9162  O O   . LYS C  1 85  ? -26.542  40.418  -49.485  1.00 35.34  ? 85  LYS C O   1 
ATOM   9163  C CB  . LYS C  1 85  ? -23.842  39.799  -47.696  1.00 33.20  ? 85  LYS C CB  1 
ATOM   9164  C CG  . LYS C  1 85  ? -22.700  38.847  -47.416  1.00 33.64  ? 85  LYS C CG  1 
ATOM   9165  C CD  . LYS C  1 85  ? -23.015  37.705  -46.457  1.00 34.65  ? 85  LYS C CD  1 
ATOM   9166  C CE  . LYS C  1 85  ? -21.892  36.701  -46.386  1.00 34.34  ? 85  LYS C CE  1 
ATOM   9167  N NZ  . LYS C  1 85  ? -22.211  35.567  -45.493  1.00 35.12  ? 85  LYS C NZ  1 
ATOM   9168  N N   . LEU C  1 86  ? -26.565  41.036  -47.303  1.00 34.19  ? 86  LEU C N   1 
ATOM   9169  C CA  . LEU C  1 86  ? -27.612  42.036  -47.421  1.00 34.51  ? 86  LEU C CA  1 
ATOM   9170  C C   . LEU C  1 86  ? -27.181  43.328  -46.735  1.00 34.81  ? 86  LEU C C   1 
ATOM   9171  O O   . LEU C  1 86  ? -26.761  43.347  -45.580  1.00 34.46  ? 86  LEU C O   1 
ATOM   9172  C CB  . LEU C  1 86  ? -28.922  41.532  -46.818  1.00 36.01  ? 86  LEU C CB  1 
ATOM   9173  C CG  . LEU C  1 86  ? -30.063  42.557  -46.747  1.00 37.42  ? 86  LEU C CG  1 
ATOM   9174  C CD1 . LEU C  1 86  ? -30.401  43.132  -48.095  1.00 36.88  ? 86  LEU C CD1 1 
ATOM   9175  C CD2 . LEU C  1 86  ? -31.307  41.913  -46.159  1.00 40.25  ? 86  LEU C CD2 1 
ATOM   9176  N N   . ILE C  1 87  ? -27.282  44.408  -47.496  1.00 34.63  ? 87  ILE C N   1 
ATOM   9177  C CA  . ILE C  1 87  ? -27.236  45.757  -46.973  1.00 34.66  ? 87  ILE C CA  1 
ATOM   9178  C C   . ILE C  1 87  ? -28.685  46.210  -47.002  1.00 35.63  ? 87  ILE C C   1 
ATOM   9179  O O   . ILE C  1 87  ? -29.192  46.446  -48.094  1.00 34.68  ? 87  ILE C O   1 
ATOM   9180  C CB  . ILE C  1 87  ? -26.337  46.608  -47.881  1.00 35.23  ? 87  ILE C CB  1 
ATOM   9181  C CG1 . ILE C  1 87  ? -24.888  46.161  -47.781  1.00 34.89  ? 87  ILE C CG1 1 
ATOM   9182  C CG2 . ILE C  1 87  ? -26.493  48.101  -47.589  1.00 37.39  ? 87  ILE C CG2 1 
ATOM   9183  C CD1 . ILE C  1 87  ? -23.954  46.835  -48.761  1.00 33.63  ? 87  ILE C CD1 1 
ATOM   9184  N N   . MET C  1 88  ? -29.361  46.207  -45.839  1.00 37.30  ? 88  MET C N   1 
ATOM   9185  C CA  . MET C  1 88  ? -30.797  46.479  -45.751  1.00 37.75  ? 88  MET C CA  1 
ATOM   9186  C C   . MET C  1 88  ? -31.048  47.973  -45.496  1.00 37.81  ? 88  MET C C   1 
ATOM   9187  O O   . MET C  1 88  ? -30.534  48.562  -44.543  1.00 35.70  ? 88  MET C O   1 
ATOM   9188  C CB  . MET C  1 88  ? -31.482  45.660  -44.645  1.00 39.81  ? 88  MET C CB  1 
ATOM   9189  C CG  . MET C  1 88  ? -33.009  45.663  -44.736  1.00 41.81  ? 88  MET C CG  1 
ATOM   9190  S SD  . MET C  1 88  ? -33.814  44.301  -43.867  1.00 42.90  ? 88  MET C SD  1 
ATOM   9191  C CE  . MET C  1 88  ? -33.544  44.815  -42.169  1.00 43.89  ? 88  MET C CE  1 
ATOM   9192  N N   . GLY C  1 89  ? -31.782  48.594  -46.416  1.00 37.91  ? 89  GLY C N   1 
ATOM   9193  C CA  . GLY C  1 89  ? -32.237  49.958  -46.223  1.00 41.40  ? 89  GLY C CA  1 
ATOM   9194  C C   . GLY C  1 89  ? -33.513  49.952  -45.387  1.00 43.80  ? 89  GLY C C   1 
ATOM   9195  O O   . GLY C  1 89  ? -34.305  48.996  -45.482  1.00 43.66  ? 89  GLY C O   1 
ATOM   9196  N N   . ILE C  1 90  ? -33.632  50.975  -44.523  1.00 44.29  ? 90  ILE C N   1 
ATOM   9197  C CA  . ILE C  1 90  ? -34.856  51.230  -43.783  1.00 47.21  ? 90  ILE C CA  1 
ATOM   9198  C C   . ILE C  1 90  ? -35.582  52.404  -44.447  1.00 47.49  ? 90  ILE C C   1 
ATOM   9199  O O   . ILE C  1 90  ? -34.956  53.324  -44.977  1.00 43.43  ? 90  ILE C O   1 
ATOM   9200  C CB  . ILE C  1 90  ? -34.578  51.471  -42.283  1.00 51.32  ? 90  ILE C CB  1 
ATOM   9201  C CG1 . ILE C  1 90  ? -33.696  50.369  -41.644  1.00 51.49  ? 90  ILE C CG1 1 
ATOM   9202  C CG2 . ILE C  1 90  ? -35.877  51.636  -41.495  1.00 53.67  ? 90  ILE C CG2 1 
ATOM   9203  C CD1 . ILE C  1 90  ? -34.265  48.968  -41.733  1.00 50.51  ? 90  ILE C CD1 1 
ATOM   9204  N N   . ASP C  1 91  ? -36.922  52.314  -44.430  1.00 51.86  ? 91  ASP C N   1 
ATOM   9205  C CA  . ASP C  1 91  ? -37.833  53.205  -45.135  1.00 52.35  ? 91  ASP C CA  1 
ATOM   9206  C C   . ASP C  1 91  ? -38.201  54.367  -44.225  1.00 53.31  ? 91  ASP C C   1 
ATOM   9207  O O   . ASP C  1 91  ? -39.271  54.371  -43.625  1.00 56.97  ? 91  ASP C O   1 
ATOM   9208  C CB  . ASP C  1 91  ? -39.082  52.433  -45.528  1.00 53.05  ? 91  ASP C CB  1 
ATOM   9209  C CG  . ASP C  1 91  ? -40.104  53.161  -46.392  1.00 56.86  ? 91  ASP C CG  1 
ATOM   9210  O OD1 . ASP C  1 91  ? -39.990  54.420  -46.593  1.00 50.60  ? 91  ASP C OD1 1 
ATOM   9211  O OD2 . ASP C  1 91  ? -41.006  52.425  -46.876  1.00 61.98  ? 91  ASP C OD2 1 
ATOM   9212  N N   . ILE C  1 92  ? -37.278  55.306  -44.062  1.00 51.95  ? 92  ILE C N   1 
ATOM   9213  C CA  . ILE C  1 92  ? -37.541  56.480  -43.247  1.00 56.17  ? 92  ILE C CA  1 
ATOM   9214  C C   . ILE C  1 92  ? -37.744  57.642  -44.224  1.00 55.89  ? 92  ILE C C   1 
ATOM   9215  O O   . ILE C  1 92  ? -36.787  58.051  -44.873  1.00 59.83  ? 92  ILE C O   1 
ATOM   9216  C CB  . ILE C  1 92  ? -36.395  56.736  -42.242  1.00 55.52  ? 92  ILE C CB  1 
ATOM   9217  C CG1 . ILE C  1 92  ? -36.084  55.543  -41.365  1.00 54.19  ? 92  ILE C CG1 1 
ATOM   9218  C CG2 . ILE C  1 92  ? -36.674  57.968  -41.378  1.00 59.20  ? 92  ILE C CG2 1 
ATOM   9219  C CD1 . ILE C  1 92  ? -37.083  55.303  -40.253  1.00 56.57  ? 92  ILE C CD1 1 
ATOM   9220  N N   . LYS C  1 93  ? -38.990  58.108  -44.377  1.00 57.87  ? 93  LYS C N   1 
ATOM   9221  C CA  . LYS C  1 93  ? -39.373  59.046  -45.436  1.00 63.37  ? 93  LYS C CA  1 
ATOM   9222  C C   . LYS C  1 93  ? -38.516  60.322  -45.379  1.00 58.45  ? 93  LYS C C   1 
ATOM   9223  O O   . LYS C  1 93  ? -38.572  61.047  -44.394  1.00 54.05  ? 93  LYS C O   1 
ATOM   9224  C CB  . LYS C  1 93  ? -40.842  59.494  -45.320  1.00 71.02  ? 93  LYS C CB  1 
ATOM   9225  C CG  . LYS C  1 93  ? -41.954  58.452  -45.414  1.00 74.04  ? 93  LYS C CG  1 
ATOM   9226  C CD  . LYS C  1 93  ? -42.175  57.884  -46.814  1.00 76.86  ? 93  LYS C CD  1 
ATOM   9227  C CE  . LYS C  1 93  ? -43.104  56.689  -46.785  1.00 80.07  ? 93  LYS C CE  1 
ATOM   9228  N NZ  . LYS C  1 93  ? -42.773  55.683  -47.802  1.00 76.02  ? 93  LYS C NZ  1 
ATOM   9229  N N   . PRO C  1 94  ? -37.675  60.633  -46.396  1.00 56.25  ? 94  PRO C N   1 
ATOM   9230  C CA  . PRO C  1 94  ? -36.784  61.790  -46.314  1.00 56.93  ? 94  PRO C CA  1 
ATOM   9231  C C   . PRO C  1 94  ? -37.454  63.162  -46.242  1.00 53.57  ? 94  PRO C C   1 
ATOM   9232  O O   . PRO C  1 94  ? -36.800  64.094  -45.830  1.00 52.78  ? 94  PRO C O   1 
ATOM   9233  C CB  . PRO C  1 94  ? -35.878  61.642  -47.590  1.00 55.86  ? 94  PRO C CB  1 
ATOM   9234  C CG  . PRO C  1 94  ? -36.669  60.759  -48.543  1.00 56.09  ? 94  PRO C CG  1 
ATOM   9235  C CD  . PRO C  1 94  ? -37.488  59.865  -47.641  1.00 55.94  ? 94  PRO C CD  1 
ATOM   9236  N N   . GLU C  1 95  ? -38.739  63.271  -46.617  1.00 55.95  ? 95  GLU C N   1 
ATOM   9237  C CA  . GLU C  1 95  ? -39.443  64.546  -46.720  1.00 57.63  ? 95  GLU C CA  1 
ATOM   9238  C C   . GLU C  1 95  ? -40.229  64.851  -45.444  1.00 58.54  ? 95  GLU C C   1 
ATOM   9239  O O   . GLU C  1 95  ? -40.875  65.893  -45.357  1.00 55.32  ? 95  GLU C O   1 
ATOM   9240  C CB  . GLU C  1 95  ? -40.484  64.653  -47.840  1.00 59.32  ? 95  GLU C CB  1 
ATOM   9241  C CG  . GLU C  1 95  ? -40.011  64.135  -49.193  1.00 66.25  ? 95  GLU C CG  1 
ATOM   9242  C CD  . GLU C  1 95  ? -40.067  62.611  -49.358  1.00 76.67  ? 95  GLU C CD  1 
ATOM   9243  O OE1 . GLU C  1 95  ? -40.467  61.886  -48.398  1.00 82.55  ? 95  GLU C OE1 1 
ATOM   9244  O OE2 . GLU C  1 95  ? -39.695  62.131  -50.461  1.00 79.72  ? 95  GLU C OE2 1 
ATOM   9245  N N   . GLU C  1 96  ? -40.203  63.944  -44.464  1.00 56.98  ? 96  GLU C N   1 
ATOM   9246  C CA  . GLU C  1 96  ? -40.919  64.161  -43.216  1.00 58.28  ? 96  GLU C CA  1 
ATOM   9247  C C   . GLU C  1 96  ? -40.090  65.065  -42.295  1.00 56.05  ? 96  GLU C C   1 
ATOM   9248  O O   . GLU C  1 96  ? -38.879  65.191  -42.451  1.00 53.49  ? 96  GLU C O   1 
ATOM   9249  C CB  . GLU C  1 96  ? -41.257  62.806  -42.574  1.00 60.49  ? 96  GLU C CB  1 
ATOM   9250  C CG  . GLU C  1 96  ? -42.394  62.024  -43.240  1.00 61.18  ? 96  GLU C CG  1 
ATOM   9251  C CD  . GLU C  1 96  ? -43.808  62.557  -43.000  1.00 66.11  ? 96  GLU C CD  1 
ATOM   9252  O OE1 . GLU C  1 96  ? -44.306  62.595  -41.857  1.00 64.95  ? 96  GLU C OE1 1 
ATOM   9253  O OE2 . GLU C  1 96  ? -44.435  62.964  -43.994  1.00 71.18  ? 96  GLU C OE2 1 
ATOM   9254  N N   . ASP C  1 97  ? -40.760  65.681  -41.316  1.00 57.11  ? 97  ASP C N   1 
ATOM   9255  C CA  . ASP C  1 97  ? -40.131  66.543  -40.324  1.00 57.19  ? 97  ASP C CA  1 
ATOM   9256  C C   . ASP C  1 97  ? -39.425  65.668  -39.284  1.00 58.94  ? 97  ASP C C   1 
ATOM   9257  O O   . ASP C  1 97  ? -40.065  65.063  -38.421  1.00 59.28  ? 97  ASP C O   1 
ATOM   9258  C CB  . ASP C  1 97  ? -41.163  67.495  -39.738  1.00 56.43  ? 97  ASP C CB  1 
ATOM   9259  C CG  . ASP C  1 97  ? -40.724  68.412  -38.601  1.00 58.36  ? 97  ASP C CG  1 
ATOM   9260  O OD1 . ASP C  1 97  ? -39.508  68.496  -38.278  1.00 56.38  ? 97  ASP C OD1 1 
ATOM   9261  O OD2 . ASP C  1 97  ? -41.628  69.045  -38.018  1.00 62.55  ? 97  ASP C OD2 1 
ATOM   9262  N N   . TYR C  1 98  ? -38.091  65.622  -39.354  1.00 58.24  ? 98  TYR C N   1 
ATOM   9263  C CA  . TYR C  1 98  ? -37.327  64.713  -38.517  1.00 59.61  ? 98  TYR C CA  1 
ATOM   9264  C C   . TYR C  1 98  ? -37.477  65.094  -37.045  1.00 59.84  ? 98  TYR C C   1 
ATOM   9265  O O   . TYR C  1 98  ? -37.152  64.300  -36.162  1.00 60.89  ? 98  TYR C O   1 
ATOM   9266  C CB  . TYR C  1 98  ? -35.840  64.705  -38.900  1.00 59.98  ? 98  TYR C CB  1 
ATOM   9267  C CG  . TYR C  1 98  ? -35.512  64.467  -40.371  1.00 57.56  ? 98  TYR C CG  1 
ATOM   9268  C CD1 . TYR C  1 98  ? -36.293  63.633  -41.168  1.00 56.27  ? 98  TYR C CD1 1 
ATOM   9269  C CD2 . TYR C  1 98  ? -34.416  65.088  -40.967  1.00 57.48  ? 98  TYR C CD2 1 
ATOM   9270  C CE1 . TYR C  1 98  ? -35.999  63.426  -42.509  1.00 54.87  ? 98  TYR C CE1 1 
ATOM   9271  C CE2 . TYR C  1 98  ? -34.107  64.885  -42.306  1.00 55.56  ? 98  TYR C CE2 1 
ATOM   9272  C CZ  . TYR C  1 98  ? -34.908  64.066  -43.087  1.00 55.85  ? 98  TYR C CZ  1 
ATOM   9273  O OH  . TYR C  1 98  ? -34.592  63.856  -44.412  1.00 53.21  ? 98  TYR C OH  1 
ATOM   9274  N N   . GLY C  1 99  ? -37.918  66.321  -36.774  1.00 58.72  ? 99  GLY C N   1 
ATOM   9275  C CA  . GLY C  1 99  ? -37.995  66.789  -35.402  1.00 60.69  ? 99  GLY C CA  1 
ATOM   9276  C C   . GLY C  1 99  ? -39.386  66.623  -34.783  1.00 62.35  ? 99  GLY C C   1 
ATOM   9277  O O   . GLY C  1 99  ? -39.543  66.870  -33.595  1.00 63.34  ? 99  GLY C O   1 
ATOM   9278  N N   . ASP C  1 100 ? -40.402  66.264  -35.583  1.00 63.37  ? 100 ASP C N   1 
ATOM   9279  C CA  . ASP C  1 100 ? -41.750  66.036  -35.067  1.00 68.09  ? 100 ASP C CA  1 
ATOM   9280  C C   . ASP C  1 100 ? -41.768  64.735  -34.256  1.00 73.43  ? 100 ASP C C   1 
ATOM   9281  O O   . ASP C  1 100 ? -41.406  63.656  -34.766  1.00 71.45  ? 100 ASP C O   1 
ATOM   9282  C CB  . ASP C  1 100 ? -42.791  66.007  -36.182  1.00 67.46  ? 100 ASP C CB  1 
ATOM   9283  C CG  . ASP C  1 100 ? -44.197  65.614  -35.753  1.00 69.03  ? 100 ASP C CG  1 
ATOM   9284  O OD1 . ASP C  1 100 ? -44.513  65.806  -34.579  1.00 71.47  ? 100 ASP C OD1 1 
ATOM   9285  O OD2 . ASP C  1 100 ? -44.948  65.068  -36.581  1.00 70.56  ? 100 ASP C OD2 1 
ATOM   9286  N N   . PRO C  1 101 ? -42.176  64.787  -32.965  1.00 77.77  ? 101 PRO C N   1 
ATOM   9287  C CA  . PRO C  1 101 ? -42.084  63.619  -32.084  1.00 77.13  ? 101 PRO C CA  1 
ATOM   9288  C C   . PRO C  1 101 ? -42.878  62.410  -32.564  1.00 77.19  ? 101 PRO C C   1 
ATOM   9289  O O   . PRO C  1 101 ? -42.491  61.280  -32.268  1.00 77.67  ? 101 PRO C O   1 
ATOM   9290  C CB  . PRO C  1 101 ? -42.604  64.140  -30.736  1.00 80.92  ? 101 PRO C CB  1 
ATOM   9291  C CG  . PRO C  1 101 ? -43.466  65.345  -31.096  1.00 83.66  ? 101 PRO C CG  1 
ATOM   9292  C CD  . PRO C  1 101 ? -42.733  65.968  -32.280  1.00 82.21  ? 101 PRO C CD  1 
ATOM   9293  N N   . GLU C  1 102 ? -43.987  62.648  -33.284  1.00 77.18  ? 102 GLU C N   1 
ATOM   9294  C CA  . GLU C  1 102 ? -44.829  61.555  -33.764  1.00 79.32  ? 102 GLU C CA  1 
ATOM   9295  C C   . GLU C  1 102 ? -44.142  60.796  -34.909  1.00 78.20  ? 102 GLU C C   1 
ATOM   9296  O O   . GLU C  1 102 ? -44.355  59.588  -35.077  1.00 73.74  ? 102 GLU C O   1 
ATOM   9297  C CB  . GLU C  1 102 ? -46.222  62.018  -34.196  1.00 79.08  ? 102 GLU C CB  1 
ATOM   9298  C CG  . GLU C  1 102 ? -47.216  60.870  -34.382  1.00 79.87  ? 102 GLU C CG  1 
ATOM   9299  C CD  . GLU C  1 102 ? -48.669  61.320  -34.351  1.00 82.69  ? 102 GLU C CD  1 
ATOM   9300  O OE1 . GLU C  1 102 ? -49.040  61.960  -35.360  1.00 79.51  ? 102 GLU C OE1 1 
ATOM   9301  O OE2 . GLU C  1 102 ? -49.408  61.087  -33.343  1.00 83.83  ? 102 GLU C OE2 1 
ATOM   9302  N N   . PHE C  1 103 ? -43.346  61.523  -35.716  1.00 76.53  ? 103 PHE C N   1 
ATOM   9303  C CA  . PHE C  1 103 ? -42.601  60.920  -36.810  1.00 71.03  ? 103 PHE C CA  1 
ATOM   9304  C C   . PHE C  1 103 ? -41.456  60.072  -36.250  1.00 71.98  ? 103 PHE C C   1 
ATOM   9305  O O   . PHE C  1 103 ? -41.210  58.973  -36.750  1.00 68.12  ? 103 PHE C O   1 
ATOM   9306  C CB  . PHE C  1 103 ? -42.038  61.955  -37.790  1.00 65.48  ? 103 PHE C CB  1 
ATOM   9307  C CG  . PHE C  1 103 ? -41.089  61.334  -38.808  1.00 59.56  ? 103 PHE C CG  1 
ATOM   9308  C CD1 . PHE C  1 103 ? -41.584  60.560  -39.856  1.00 57.04  ? 103 PHE C CD1 1 
ATOM   9309  C CD2 . PHE C  1 103 ? -39.705  61.487  -38.684  1.00 56.75  ? 103 PHE C CD2 1 
ATOM   9310  C CE1 . PHE C  1 103 ? -40.718  59.995  -40.778  1.00 54.77  ? 103 PHE C CE1 1 
ATOM   9311  C CE2 . PHE C  1 103 ? -38.838  60.911  -39.596  1.00 52.84  ? 103 PHE C CE2 1 
ATOM   9312  C CZ  . PHE C  1 103 ? -39.346  60.177  -40.648  1.00 53.37  ? 103 PHE C CZ  1 
ATOM   9313  N N   . VAL C  1 104 ? -40.739  60.612  -35.249  1.00 71.81  ? 104 VAL C N   1 
ATOM   9314  C CA  . VAL C  1 104 ? -39.698  59.866  -34.570  1.00 71.50  ? 104 VAL C CA  1 
ATOM   9315  C C   . VAL C  1 104 ? -40.323  58.566  -34.068  1.00 74.71  ? 104 VAL C C   1 
ATOM   9316  O O   . VAL C  1 104 ? -39.921  57.481  -34.501  1.00 71.53  ? 104 VAL C O   1 
ATOM   9317  C CB  . VAL C  1 104 ? -39.041  60.669  -33.431  1.00 71.35  ? 104 VAL C CB  1 
ATOM   9318  C CG1 . VAL C  1 104 ? -38.069  59.817  -32.628  1.00 73.19  ? 104 VAL C CG1 1 
ATOM   9319  C CG2 . VAL C  1 104 ? -38.315  61.888  -33.968  1.00 71.41  ? 104 VAL C CG2 1 
ATOM   9320  N N   . LYS C  1 105 ? -41.332  58.711  -33.200  1.00 74.20  ? 105 LYS C N   1 
ATOM   9321  C CA  . LYS C  1 105 ? -42.066  57.592  -32.641  1.00 80.03  ? 105 LYS C CA  1 
ATOM   9322  C C   . LYS C  1 105 ? -42.286  56.530  -33.715  1.00 80.48  ? 105 LYS C C   1 
ATOM   9323  O O   . LYS C  1 105 ? -41.655  55.476  -33.668  1.00 83.50  ? 105 LYS C O   1 
ATOM   9324  C CB  . LYS C  1 105 ? -43.400  58.053  -32.024  1.00 86.64  ? 105 LYS C CB  1 
ATOM   9325  C CG  . LYS C  1 105 ? -44.530  57.006  -31.816  1.00 87.59  ? 105 LYS C CG  1 
ATOM   9326  C CD  . LYS C  1 105 ? -45.593  57.365  -30.768  1.00 91.88  ? 105 LYS C CD  1 
ATOM   9327  C CE  . LYS C  1 105 ? -46.715  58.296  -31.153  1.00 93.16  ? 105 LYS C CE  1 
ATOM   9328  N NZ  . LYS C  1 105 ? -47.683  57.576  -31.975  1.00 94.24  ? 105 LYS C NZ  1 
ATOM   9329  N N   . ASP C  1 106 ? -43.167  56.816  -34.685  1.00 78.09  ? 106 ASP C N   1 
ATOM   9330  C CA  . ASP C  1 106 ? -43.635  55.803  -35.627  1.00 75.74  ? 106 ASP C CA  1 
ATOM   9331  C C   . ASP C  1 106 ? -42.467  55.035  -36.276  1.00 69.35  ? 106 ASP C C   1 
ATOM   9332  O O   . ASP C  1 106 ? -42.608  53.825  -36.523  1.00 61.42  ? 106 ASP C O   1 
ATOM   9333  C CB  . ASP C  1 106 ? -44.596  56.409  -36.644  1.00 74.19  ? 106 ASP C CB  1 
ATOM   9334  C CG  . ASP C  1 106 ? -46.004  56.709  -36.145  1.00 74.71  ? 106 ASP C CG  1 
ATOM   9335  O OD1 . ASP C  1 106 ? -46.567  55.863  -35.416  1.00 80.06  ? 106 ASP C OD1 1 
ATOM   9336  O OD2 . ASP C  1 106 ? -46.551  57.753  -36.529  1.00 71.82  ? 106 ASP C OD2 1 
ATOM   9337  N N   . SER C  1 107 ? -41.352  55.774  -36.510  1.00 65.01  ? 107 SER C N   1 
ATOM   9338  C CA  . SER C  1 107 ? -40.099  55.307  -37.091  1.00 63.67  ? 107 SER C CA  1 
ATOM   9339  C C   . SER C  1 107 ? -39.371  54.343  -36.143  1.00 66.21  ? 107 SER C C   1 
ATOM   9340  O O   . SER C  1 107 ? -38.943  53.261  -36.566  1.00 63.97  ? 107 SER C O   1 
ATOM   9341  C CB  . SER C  1 107 ? -39.198  56.494  -37.498  1.00 61.96  ? 107 SER C CB  1 
ATOM   9342  O OG  . SER C  1 107 ? -39.701  57.239  -38.616  1.00 58.16  ? 107 SER C OG  1 
ATOM   9343  N N   . GLU C  1 108 ? -39.241  54.738  -34.866  1.00 67.36  ? 108 GLU C N   1 
ATOM   9344  C CA  . GLU C  1 108 ? -38.647  53.904  -33.829  1.00 68.57  ? 108 GLU C CA  1 
ATOM   9345  C C   . GLU C  1 108 ? -39.393  52.578  -33.684  1.00 69.02  ? 108 GLU C C   1 
ATOM   9346  O O   . GLU C  1 108 ? -38.762  51.540  -33.500  1.00 66.44  ? 108 GLU C O   1 
ATOM   9347  C CB  . GLU C  1 108 ? -38.644  54.579  -32.459  1.00 71.06  ? 108 GLU C CB  1 
ATOM   9348  C CG  . GLU C  1 108 ? -37.757  55.820  -32.383  1.00 71.46  ? 108 GLU C CG  1 
ATOM   9349  C CD  . GLU C  1 108 ? -37.859  56.604  -31.085  1.00 72.27  ? 108 GLU C CD  1 
ATOM   9350  O OE1 . GLU C  1 108 ? -38.990  56.760  -30.558  1.00 72.23  ? 108 GLU C OE1 1 
ATOM   9351  O OE2 . GLU C  1 108 ? -36.801  57.094  -30.629  1.00 72.21  ? 108 GLU C OE2 1 
ATOM   9352  N N   . ILE C  1 109 ? -40.730  52.624  -33.758  1.00 71.36  ? 109 ILE C N   1 
ATOM   9353  C CA  . ILE C  1 109 ? -41.570  51.440  -33.596  1.00 73.15  ? 109 ILE C CA  1 
ATOM   9354  C C   . ILE C  1 109 ? -41.398  50.498  -34.787  1.00 71.02  ? 109 ILE C C   1 
ATOM   9355  O O   . ILE C  1 109 ? -41.338  49.287  -34.614  1.00 72.88  ? 109 ILE C O   1 
ATOM   9356  C CB  . ILE C  1 109 ? -43.055  51.813  -33.440  1.00 74.25  ? 109 ILE C CB  1 
ATOM   9357  C CG1 . ILE C  1 109 ? -43.334  52.537  -32.106  1.00 77.85  ? 109 ILE C CG1 1 
ATOM   9358  C CG2 . ILE C  1 109 ? -43.946  50.579  -33.632  1.00 72.87  ? 109 ILE C CG2 1 
ATOM   9359  C CD1 . ILE C  1 109 ? -44.653  53.301  -32.076  1.00 78.46  ? 109 ILE C CD1 1 
ATOM   9360  N N   . GLU C  1 110 ? -41.401  51.050  -36.003  1.00 68.69  ? 110 GLU C N   1 
ATOM   9361  C CA  . GLU C  1 110 ? -41.170  50.250  -37.193  1.00 63.92  ? 110 GLU C CA  1 
ATOM   9362  C C   . GLU C  1 110 ? -39.768  49.630  -37.128  1.00 62.72  ? 110 GLU C C   1 
ATOM   9363  O O   . GLU C  1 110 ? -39.623  48.454  -37.425  1.00 64.41  ? 110 GLU C O   1 
ATOM   9364  C CB  . GLU C  1 110 ? -41.435  51.060  -38.463  1.00 59.38  ? 110 GLU C CB  1 
ATOM   9365  C CG  . GLU C  1 110 ? -41.325  50.284  -39.773  1.00 57.00  ? 110 GLU C CG  1 
ATOM   9366  C CD  . GLU C  1 110 ? -42.231  49.074  -40.002  1.00 58.00  ? 110 GLU C CD  1 
ATOM   9367  O OE1 . GLU C  1 110 ? -43.066  48.768  -39.137  1.00 58.48  ? 110 GLU C OE1 1 
ATOM   9368  O OE2 . GLU C  1 110 ? -42.102  48.409  -41.065  1.00 56.86  ? 110 GLU C OE2 1 
ATOM   9369  N N   . LEU C  1 111 ? -38.751  50.391  -36.703  1.00 59.33  ? 111 LEU C N   1 
ATOM   9370  C CA  . LEU C  1 111 ? -37.374  49.926  -36.742  1.00 55.68  ? 111 LEU C CA  1 
ATOM   9371  C C   . LEU C  1 111 ? -37.163  48.785  -35.747  1.00 58.24  ? 111 LEU C C   1 
ATOM   9372  O O   . LEU C  1 111 ? -36.597  47.751  -36.083  1.00 59.53  ? 111 LEU C O   1 
ATOM   9373  C CB  . LEU C  1 111 ? -36.419  51.097  -36.497  1.00 53.34  ? 111 LEU C CB  1 
ATOM   9374  C CG  . LEU C  1 111 ? -34.927  50.756  -36.494  1.00 50.94  ? 111 LEU C CG  1 
ATOM   9375  C CD1 . LEU C  1 111 ? -34.464  49.979  -37.698  1.00 48.86  ? 111 LEU C CD1 1 
ATOM   9376  C CD2 . LEU C  1 111 ? -34.139  52.009  -36.407  1.00 50.82  ? 111 LEU C CD2 1 
ATOM   9377  N N   . LYS C  1 112 ? -37.630  48.962  -34.515  1.00 61.71  ? 112 LYS C N   1 
ATOM   9378  C CA  . LYS C  1 112 ? -37.490  47.943  -33.484  1.00 62.27  ? 112 LYS C CA  1 
ATOM   9379  C C   . LYS C  1 112 ? -38.304  46.714  -33.854  1.00 62.22  ? 112 LYS C C   1 
ATOM   9380  O O   . LYS C  1 112 ? -37.932  45.605  -33.486  1.00 65.20  ? 112 LYS C O   1 
ATOM   9381  C CB  . LYS C  1 112 ? -38.002  48.435  -32.125  1.00 64.74  ? 112 LYS C CB  1 
ATOM   9382  C CG  . LYS C  1 112 ? -37.167  49.554  -31.487  1.00 66.09  ? 112 LYS C CG  1 
ATOM   9383  C CD  . LYS C  1 112 ? -37.783  50.207  -30.249  1.00 67.92  ? 112 LYS C CD  1 
ATOM   9384  C CE  . LYS C  1 112 ? -36.760  50.901  -29.393  1.00 69.47  ? 112 LYS C CE  1 
ATOM   9385  N NZ  . LYS C  1 112 ? -37.363  51.506  -28.205  1.00 72.94  ? 112 LYS C NZ  1 
ATOM   9386  N N   . ARG C  1 113 ? -39.447  46.923  -34.516  1.00 60.10  ? 113 ARG C N   1 
ATOM   9387  C CA  . ARG C  1 113 ? -40.247  45.809  -34.986  1.00 59.63  ? 113 ARG C CA  1 
ATOM   9388  C C   . ARG C  1 113 ? -39.367  44.951  -35.886  1.00 58.87  ? 113 ARG C C   1 
ATOM   9389  O O   . ARG C  1 113 ? -39.303  43.734  -35.729  1.00 62.55  ? 113 ARG C O   1 
ATOM   9390  C CB  . ARG C  1 113 ? -41.495  46.246  -35.759  1.00 59.16  ? 113 ARG C CB  1 
ATOM   9391  C CG  . ARG C  1 113 ? -42.468  45.107  -36.031  1.00 60.13  ? 113 ARG C CG  1 
ATOM   9392  C CD  . ARG C  1 113 ? -43.575  45.595  -36.930  1.00 61.67  ? 113 ARG C CD  1 
ATOM   9393  N NE  . ARG C  1 113 ? -43.078  46.052  -38.232  1.00 60.42  ? 113 ARG C NE  1 
ATOM   9394  C CZ  . ARG C  1 113 ? -42.815  45.282  -39.304  1.00 62.81  ? 113 ARG C CZ  1 
ATOM   9395  N NH1 . ARG C  1 113 ? -43.048  43.969  -39.291  1.00 62.91  ? 113 ARG C NH1 1 
ATOM   9396  N NH2 . ARG C  1 113 ? -42.311  45.841  -40.399  1.00 59.63  ? 113 ARG C NH2 1 
ATOM   9397  N N   . VAL C  1 114 ? -38.674  45.618  -36.806  1.00 56.43  ? 114 VAL C N   1 
ATOM   9398  C CA  . VAL C  1 114 ? -37.891  44.949  -37.830  1.00 56.55  ? 114 VAL C CA  1 
ATOM   9399  C C   . VAL C  1 114 ? -36.699  44.230  -37.204  1.00 54.44  ? 114 VAL C C   1 
ATOM   9400  O O   . VAL C  1 114 ? -36.483  43.057  -37.493  1.00 55.98  ? 114 VAL C O   1 
ATOM   9401  C CB  . VAL C  1 114 ? -37.473  45.992  -38.885  1.00 55.17  ? 114 VAL C CB  1 
ATOM   9402  C CG1 . VAL C  1 114 ? -36.324  45.522  -39.768  1.00 53.68  ? 114 VAL C CG1 1 
ATOM   9403  C CG2 . VAL C  1 114 ? -38.681  46.396  -39.724  1.00 55.72  ? 114 VAL C CG2 1 
ATOM   9404  N N   . LEU C  1 115 ? -35.976  44.951  -36.341  1.00 52.75  ? 115 LEU C N   1 
ATOM   9405  C CA  . LEU C  1 115 ? -34.775  44.467  -35.691  1.00 53.04  ? 115 LEU C CA  1 
ATOM   9406  C C   . LEU C  1 115 ? -35.099  43.237  -34.866  1.00 53.93  ? 115 LEU C C   1 
ATOM   9407  O O   . LEU C  1 115 ? -34.211  42.450  -34.535  1.00 53.50  ? 115 LEU C O   1 
ATOM   9408  C CB  . LEU C  1 115 ? -34.201  45.554  -34.785  1.00 54.31  ? 115 LEU C CB  1 
ATOM   9409  C CG  . LEU C  1 115 ? -33.461  46.696  -35.484  1.00 53.97  ? 115 LEU C CG  1 
ATOM   9410  C CD1 . LEU C  1 115 ? -32.938  47.643  -34.424  1.00 56.63  ? 115 LEU C CD1 1 
ATOM   9411  C CD2 . LEU C  1 115 ? -32.337  46.221  -36.358  1.00 51.74  ? 115 LEU C CD2 1 
ATOM   9412  N N   . ASN C  1 116 ? -36.382  43.128  -34.528  1.00 54.67  ? 116 ASN C N   1 
ATOM   9413  C CA  . ASN C  1 116 ? -36.863  42.137  -33.595  1.00 55.82  ? 116 ASN C CA  1 
ATOM   9414  C C   . ASN C  1 116 ? -36.788  40.748  -34.215  1.00 54.14  ? 116 ASN C C   1 
ATOM   9415  O O   . ASN C  1 116 ? -36.591  39.796  -33.477  1.00 56.19  ? 116 ASN C O   1 
ATOM   9416  C CB  . ASN C  1 116 ? -38.289  42.440  -33.164  1.00 57.81  ? 116 ASN C CB  1 
ATOM   9417  C CG  . ASN C  1 116 ? -38.519  42.074  -31.727  1.00 60.16  ? 116 ASN C CG  1 
ATOM   9418  O OD1 . ASN C  1 116 ? -37.695  41.402  -31.094  1.00 59.74  ? 116 ASN C OD1 1 
ATOM   9419  N ND2 . ASN C  1 116 ? -39.640  42.536  -31.204  1.00 63.43  ? 116 ASN C ND2 1 
ATOM   9420  N N   . TYR C  1 117 ? -37.026  40.635  -35.529  1.00 51.80  ? 117 TYR C N   1 
ATOM   9421  C CA  . TYR C  1 117 ? -36.795  39.390  -36.248  1.00 50.61  ? 117 TYR C CA  1 
ATOM   9422  C C   . TYR C  1 117 ? -35.462  39.463  -37.013  1.00 48.68  ? 117 TYR C C   1 
ATOM   9423  O O   . TYR C  1 117 ? -34.796  38.438  -37.194  1.00 46.90  ? 117 TYR C O   1 
ATOM   9424  C CB  . TYR C  1 117 ? -37.994  39.020  -37.130  1.00 50.90  ? 117 TYR C CB  1 
ATOM   9425  C CG  . TYR C  1 117 ? -38.382  40.055  -38.177  1.00 51.99  ? 117 TYR C CG  1 
ATOM   9426  C CD1 . TYR C  1 117 ? -37.747  40.091  -39.413  1.00 50.19  ? 117 TYR C CD1 1 
ATOM   9427  C CD2 . TYR C  1 117 ? -39.362  41.011  -37.929  1.00 54.13  ? 117 TYR C CD2 1 
ATOM   9428  C CE1 . TYR C  1 117 ? -38.058  41.043  -40.366  1.00 50.00  ? 117 TYR C CE1 1 
ATOM   9429  C CE2 . TYR C  1 117 ? -39.700  41.956  -38.887  1.00 53.36  ? 117 TYR C CE2 1 
ATOM   9430  C CZ  . TYR C  1 117 ? -39.047  41.974  -40.107  1.00 51.45  ? 117 TYR C CZ  1 
ATOM   9431  O OH  . TYR C  1 117 ? -39.352  42.887  -41.077  1.00 51.17  ? 117 TYR C OH  1 
ATOM   9432  N N   . ALA C  1 118 ? -35.018  40.671  -37.399  1.00 46.38  ? 118 ALA C N   1 
ATOM   9433  C CA  . ALA C  1 118 ? -33.907  40.789  -38.332  1.00 45.77  ? 118 ALA C CA  1 
ATOM   9434  C C   . ALA C  1 118 ? -32.589  40.309  -37.720  1.00 45.70  ? 118 ALA C C   1 
ATOM   9435  O O   . ALA C  1 118 ? -31.704  39.812  -38.434  1.00 43.81  ? 118 ALA C O   1 
ATOM   9436  C CB  . ALA C  1 118 ? -33.798  42.217  -38.803  1.00 46.04  ? 118 ALA C CB  1 
ATOM   9437  N N   . LYS C  1 119 ? -32.479  40.465  -36.395  1.00 46.69  ? 119 LYS C N   1 
ATOM   9438  C CA  . LYS C  1 119 ? -31.247  40.192  -35.668  1.00 47.51  ? 119 LYS C CA  1 
ATOM   9439  C C   . LYS C  1 119 ? -30.902  38.705  -35.646  1.00 48.25  ? 119 LYS C C   1 
ATOM   9440  O O   . LYS C  1 119 ? -29.837  38.336  -35.156  1.00 48.90  ? 119 LYS C O   1 
ATOM   9441  C CB  . LYS C  1 119 ? -31.376  40.604  -34.196  1.00 48.26  ? 119 LYS C CB  1 
ATOM   9442  C CG  . LYS C  1 119 ? -32.370  39.795  -33.368  1.00 48.75  ? 119 LYS C CG  1 
ATOM   9443  C CD  . LYS C  1 119 ? -32.673  40.437  -32.021  1.00 51.18  ? 119 LYS C CD  1 
ATOM   9444  C CE  . LYS C  1 119 ? -33.759  39.740  -31.270  1.00 53.55  ? 119 LYS C CE  1 
ATOM   9445  N NZ  . LYS C  1 119 ? -34.122  40.456  -30.056  1.00 55.42  ? 119 LYS C NZ  1 
ATOM   9446  N N   . LYS C  1 120 ? -31.824  37.849  -36.088  1.00 48.40  ? 120 LYS C N   1 
ATOM   9447  C CA  . LYS C  1 120 ? -31.543  36.417  -36.157  1.00 49.30  ? 120 LYS C CA  1 
ATOM   9448  C C   . LYS C  1 120 ? -30.851  36.042  -37.471  1.00 46.75  ? 120 LYS C C   1 
ATOM   9449  O O   . LYS C  1 120 ? -30.476  34.891  -37.650  1.00 48.55  ? 120 LYS C O   1 
ATOM   9450  C CB  . LYS C  1 120 ? -32.841  35.616  -36.021  1.00 50.19  ? 120 LYS C CB  1 
ATOM   9451  C CG  . LYS C  1 120 ? -33.631  35.948  -34.775  1.00 53.77  ? 120 LYS C CG  1 
ATOM   9452  C CD  . LYS C  1 120 ? -34.857  35.069  -34.564  1.00 57.01  ? 120 LYS C CD  1 
ATOM   9453  C CE  . LYS C  1 120 ? -35.936  35.200  -35.610  1.00 57.68  ? 120 LYS C CE  1 
ATOM   9454  N NZ  . LYS C  1 120 ? -37.058  34.357  -35.163  1.00 60.82  ? 120 LYS C NZ  1 
ATOM   9455  N N   . TYR C  1 121 ? -30.649  37.016  -38.367  1.00 44.39  ? 121 TYR C N   1 
ATOM   9456  C CA  . TYR C  1 121 ? -30.247  36.740  -39.728  1.00 43.51  ? 121 TYR C CA  1 
ATOM   9457  C C   . TYR C  1 121 ? -28.910  37.434  -39.975  1.00 42.37  ? 121 TYR C C   1 
ATOM   9458  O O   . TYR C  1 121 ? -28.868  38.634  -40.258  1.00 42.68  ? 121 TYR C O   1 
ATOM   9459  C CB  . TYR C  1 121 ? -31.384  37.155  -40.682  1.00 44.61  ? 121 TYR C CB  1 
ATOM   9460  C CG  . TYR C  1 121 ? -32.651  36.342  -40.455  1.00 46.25  ? 121 TYR C CG  1 
ATOM   9461  C CD1 . TYR C  1 121 ? -32.750  35.023  -40.878  1.00 47.04  ? 121 TYR C CD1 1 
ATOM   9462  C CD2 . TYR C  1 121 ? -33.724  36.869  -39.749  1.00 47.18  ? 121 TYR C CD2 1 
ATOM   9463  C CE1 . TYR C  1 121 ? -33.875  34.253  -40.610  1.00 47.98  ? 121 TYR C CE1 1 
ATOM   9464  C CE2 . TYR C  1 121 ? -34.847  36.107  -39.471  1.00 48.58  ? 121 TYR C CE2 1 
ATOM   9465  C CZ  . TYR C  1 121 ? -34.929  34.791  -39.895  1.00 48.96  ? 121 TYR C CZ  1 
ATOM   9466  O OH  . TYR C  1 121 ? -36.043  34.036  -39.597  1.00 49.35  ? 121 TYR C OH  1 
ATOM   9467  N N   . ASP C  1 122 ? -27.830  36.644  -39.983  1.00 41.09  ? 122 ASP C N   1 
ATOM   9468  C CA  . ASP C  1 122 ? -26.484  37.187  -40.017  1.00 40.40  ? 122 ASP C CA  1 
ATOM   9469  C C   . ASP C  1 122 ? -26.065  37.477  -41.448  1.00 39.22  ? 122 ASP C C   1 
ATOM   9470  O O   . ASP C  1 122 ? -24.939  37.902  -41.663  1.00 38.99  ? 122 ASP C O   1 
ATOM   9471  C CB  . ASP C  1 122 ? -25.483  36.299  -39.294  1.00 42.32  ? 122 ASP C CB  1 
ATOM   9472  C CG  . ASP C  1 122 ? -25.102  34.960  -39.927  1.00 41.84  ? 122 ASP C CG  1 
ATOM   9473  O OD1 . ASP C  1 122 ? -25.582  34.645  -41.030  1.00 40.69  ? 122 ASP C OD1 1 
ATOM   9474  O OD2 . ASP C  1 122 ? -24.290  34.241  -39.314  1.00 44.10  ? 122 ASP C OD2 1 
ATOM   9475  N N   . CYS C  1 123 ? -26.967  37.245  -42.415  1.00 39.44  ? 123 CYS C N   1 
ATOM   9476  C CA  . CYS C  1 123 ? -26.735  37.685  -43.784  1.00 38.53  ? 123 CYS C CA  1 
ATOM   9477  C C   . CYS C  1 123 ? -26.715  39.212  -43.897  1.00 37.59  ? 123 CYS C C   1 
ATOM   9478  O O   . CYS C  1 123 ? -26.159  39.732  -44.855  1.00 36.30  ? 123 CYS C O   1 
ATOM   9479  C CB  . CYS C  1 123 ? -27.730  37.081  -44.772  1.00 39.15  ? 123 CYS C CB  1 
ATOM   9480  S SG  . CYS C  1 123 ? -29.446  37.648  -44.603  1.00 40.11  ? 123 CYS C SG  1 
ATOM   9481  N N   . ILE C  1 124 ? -27.325  39.930  -42.943  1.00 39.22  ? 124 ILE C N   1 
ATOM   9482  C CA  . ILE C  1 124 ? -27.341  41.392  -42.943  1.00 38.38  ? 124 ILE C CA  1 
ATOM   9483  C C   . ILE C  1 124 ? -25.985  41.872  -42.448  1.00 37.80  ? 124 ILE C C   1 
ATOM   9484  O O   . ILE C  1 124 ? -25.643  41.597  -41.303  1.00 39.04  ? 124 ILE C O   1 
ATOM   9485  C CB  . ILE C  1 124 ? -28.446  41.957  -42.027  1.00 40.13  ? 124 ILE C CB  1 
ATOM   9486  C CG1 . ILE C  1 124 ? -29.859  41.514  -42.427  1.00 41.08  ? 124 ILE C CG1 1 
ATOM   9487  C CG2 . ILE C  1 124 ? -28.352  43.476  -41.958  1.00 40.46  ? 124 ILE C CG2 1 
ATOM   9488  C CD1 . ILE C  1 124 ? -30.918  41.732  -41.356  1.00 42.09  ? 124 ILE C CD1 1 
ATOM   9489  N N   . ILE C  1 125 ? -25.246  42.594  -43.299  1.00 36.82  ? 125 ILE C N   1 
ATOM   9490  C CA  . ILE C  1 125 ? -23.900  43.026  -42.954  1.00 37.24  ? 125 ILE C CA  1 
ATOM   9491  C C   . ILE C  1 125 ? -23.800  44.542  -42.866  1.00 36.82  ? 125 ILE C C   1 
ATOM   9492  O O   . ILE C  1 125 ? -22.739  45.019  -42.484  1.00 37.10  ? 125 ILE C O   1 
ATOM   9493  C CB  . ILE C  1 125 ? -22.875  42.485  -43.963  1.00 36.48  ? 125 ILE C CB  1 
ATOM   9494  C CG1 . ILE C  1 125 ? -23.150  42.991  -45.376  1.00 36.05  ? 125 ILE C CG1 1 
ATOM   9495  C CG2 . ILE C  1 125 ? -22.807  40.958  -43.888  1.00 37.38  ? 125 ILE C CG2 1 
ATOM   9496  C CD1 . ILE C  1 125 ? -21.932  42.989  -46.294  1.00 35.62  ? 125 ILE C CD1 1 
ATOM   9497  N N   . THR C  1 126 ? -24.854  45.283  -43.266  1.00 37.25  ? 126 THR C N   1 
ATOM   9498  C CA  . THR C  1 126 ? -24.949  46.724  -43.005  1.00 37.48  ? 126 THR C CA  1 
ATOM   9499  C C   . THR C  1 126 ? -26.416  47.153  -42.987  1.00 37.38  ? 126 THR C C   1 
ATOM   9500  O O   . THR C  1 126 ? -27.250  46.620  -43.712  1.00 37.52  ? 126 THR C O   1 
ATOM   9501  C CB  . THR C  1 126 ? -24.173  47.525  -44.049  1.00 37.27  ? 126 THR C CB  1 
ATOM   9502  O OG1 . THR C  1 126 ? -22.795  47.224  -43.890  1.00 38.03  ? 126 THR C OG1 1 
ATOM   9503  C CG2 . THR C  1 126 ? -24.298  49.035  -43.875  1.00 38.53  ? 126 THR C CG2 1 
ATOM   9504  N N   . TYR C  1 127 ? -26.725  48.124  -42.137  1.00 38.80  ? 127 TYR C N   1 
ATOM   9505  C CA  . TYR C  1 127 ? -27.996  48.829  -42.201  1.00 39.56  ? 127 TYR C CA  1 
ATOM   9506  C C   . TYR C  1 127 ? -27.755  50.236  -42.757  1.00 39.87  ? 127 TYR C C   1 
ATOM   9507  O O   . TYR C  1 127 ? -26.757  50.861  -42.412  1.00 38.95  ? 127 TYR C O   1 
ATOM   9508  C CB  . TYR C  1 127 ? -28.649  48.921  -40.817  1.00 40.24  ? 127 TYR C CB  1 
ATOM   9509  C CG  . TYR C  1 127 ? -29.271  47.643  -40.269  1.00 40.85  ? 127 TYR C CG  1 
ATOM   9510  C CD1 . TYR C  1 127 ? -28.517  46.716  -39.561  1.00 41.57  ? 127 TYR C CD1 1 
ATOM   9511  C CD2 . TYR C  1 127 ? -30.631  47.396  -40.391  1.00 41.43  ? 127 TYR C CD2 1 
ATOM   9512  C CE1 . TYR C  1 127 ? -29.078  45.545  -39.063  1.00 42.06  ? 127 TYR C CE1 1 
ATOM   9513  C CE2 . TYR C  1 127 ? -31.206  46.241  -39.881  1.00 42.99  ? 127 TYR C CE2 1 
ATOM   9514  C CZ  . TYR C  1 127 ? -30.430  45.309  -39.214  1.00 41.59  ? 127 TYR C CZ  1 
ATOM   9515  O OH  . TYR C  1 127 ? -30.994  44.185  -38.722  1.00 41.23  ? 127 TYR C OH  1 
ATOM   9516  N N   . LEU C  1 128 ? -28.696  50.704  -43.600  1.00 40.63  ? 128 LEU C N   1 
ATOM   9517  C CA  . LEU C  1 128 ? -28.793  52.074  -44.098  1.00 39.80  ? 128 LEU C CA  1 
ATOM   9518  C C   . LEU C  1 128 ? -30.032  52.772  -43.511  1.00 40.96  ? 128 LEU C C   1 
ATOM   9519  O O   . LEU C  1 128 ? -31.167  52.460  -43.875  1.00 42.18  ? 128 LEU C O   1 
ATOM   9520  C CB  . LEU C  1 128 ? -28.885  52.020  -45.625  1.00 39.38  ? 128 LEU C CB  1 
ATOM   9521  C CG  . LEU C  1 128 ? -27.723  51.389  -46.404  1.00 38.45  ? 128 LEU C CG  1 
ATOM   9522  C CD1 . LEU C  1 128 ? -28.053  51.486  -47.884  1.00 37.16  ? 128 LEU C CD1 1 
ATOM   9523  C CD2 . LEU C  1 128 ? -26.372  52.020  -46.142  1.00 39.13  ? 128 LEU C CD2 1 
ATOM   9524  N N   . VAL C  1 129 ? -29.819  53.730  -42.602  1.00 41.41  ? 129 VAL C N   1 
ATOM   9525  C CA  . VAL C  1 129 ? -30.892  54.250  -41.770  1.00 42.31  ? 129 VAL C CA  1 
ATOM   9526  C C   . VAL C  1 129 ? -31.762  55.260  -42.512  1.00 44.96  ? 129 VAL C C   1 
ATOM   9527  O O   . VAL C  1 129 ? -32.861  55.541  -42.042  1.00 48.53  ? 129 VAL C O   1 
ATOM   9528  C CB  . VAL C  1 129 ? -30.386  54.914  -40.483  1.00 44.17  ? 129 VAL C CB  1 
ATOM   9529  C CG1 . VAL C  1 129 ? -30.002  53.912  -39.423  1.00 45.70  ? 129 VAL C CG1 1 
ATOM   9530  C CG2 . VAL C  1 129 ? -29.236  55.877  -40.727  1.00 44.91  ? 129 VAL C CG2 1 
ATOM   9531  N N   . ILE C  1 130 ? -31.275  55.885  -43.596  1.00 45.18  ? 130 ILE C N   1 
ATOM   9532  C CA  . ILE C  1 130 ? -32.109  56.813  -44.352  1.00 45.25  ? 130 ILE C CA  1 
ATOM   9533  C C   . ILE C  1 130 ? -31.620  56.939  -45.794  1.00 43.55  ? 130 ILE C C   1 
ATOM   9534  O O   . ILE C  1 130 ? -30.445  56.735  -46.098  1.00 42.45  ? 130 ILE C O   1 
ATOM   9535  C CB  . ILE C  1 130 ? -32.216  58.183  -43.643  1.00 46.46  ? 130 ILE C CB  1 
ATOM   9536  C CG1 . ILE C  1 130 ? -33.260  59.081  -44.286  1.00 46.70  ? 130 ILE C CG1 1 
ATOM   9537  C CG2 . ILE C  1 130 ? -30.871  58.882  -43.567  1.00 46.57  ? 130 ILE C CG2 1 
ATOM   9538  C CD1 . ILE C  1 130 ? -33.658  60.275  -43.430  1.00 48.45  ? 130 ILE C CD1 1 
ATOM   9539  N N   . ASN C  1 131 ? -32.562  57.280  -46.681  1.00 44.15  ? 131 ASN C N   1 
ATOM   9540  C CA  . ASN C  1 131 ? -32.279  57.450  -48.094  1.00 42.95  ? 131 ASN C CA  1 
ATOM   9541  C C   . ASN C  1 131 ? -32.439  58.915  -48.544  1.00 41.61  ? 131 ASN C C   1 
ATOM   9542  O O   . ASN C  1 131 ? -33.538  59.410  -48.720  1.00 41.13  ? 131 ASN C O   1 
ATOM   9543  C CB  . ASN C  1 131 ? -33.185  56.552  -48.923  1.00 41.68  ? 131 ASN C CB  1 
ATOM   9544  C CG  . ASN C  1 131 ? -32.763  56.574  -50.365  1.00 41.43  ? 131 ASN C CG  1 
ATOM   9545  O OD1 . ASN C  1 131 ? -33.578  56.798  -51.266  1.00 42.20  ? 131 ASN C OD1 1 
ATOM   9546  N ND2 . ASN C  1 131 ? -31.483  56.334  -50.597  1.00 43.38  ? 131 ASN C ND2 1 
ATOM   9547  N N   . GLU C  1 132 ? -31.318  59.581  -48.787  1.00 41.81  ? 132 GLU C N   1 
ATOM   9548  C CA  . GLU C  1 132 ? -31.245  60.777  -49.616  1.00 43.73  ? 132 GLU C CA  1 
ATOM   9549  C C   . GLU C  1 132 ? -31.956  61.994  -49.007  1.00 43.77  ? 132 GLU C C   1 
ATOM   9550  O O   . GLU C  1 132 ? -32.866  62.572  -49.619  1.00 42.20  ? 132 GLU C O   1 
ATOM   9551  C CB  . GLU C  1 132 ? -31.805  60.419  -50.984  1.00 45.39  ? 132 GLU C CB  1 
ATOM   9552  C CG  . GLU C  1 132 ? -31.157  61.253  -52.076  1.00 46.99  ? 132 GLU C CG  1 
ATOM   9553  C CD  . GLU C  1 132 ? -29.718  60.821  -52.301  1.00 49.61  ? 132 GLU C CD  1 
ATOM   9554  O OE1 . GLU C  1 132 ? -29.542  59.809  -53.054  1.00 44.76  ? 132 GLU C OE1 1 
ATOM   9555  O OE2 . GLU C  1 132 ? -28.805  61.512  -51.720  1.00 51.61  ? 132 GLU C OE2 1 
ATOM   9556  N N   . PRO C  1 133 ? -31.540  62.450  -47.801  1.00 42.78  ? 133 PRO C N   1 
ATOM   9557  C CA  . PRO C  1 133 ? -32.053  63.697  -47.232  1.00 44.35  ? 133 PRO C CA  1 
ATOM   9558  C C   . PRO C  1 133 ? -31.532  64.901  -48.019  1.00 43.91  ? 133 PRO C C   1 
ATOM   9559  O O   . PRO C  1 133 ? -30.324  65.081  -48.202  1.00 42.73  ? 133 PRO C O   1 
ATOM   9560  C CB  . PRO C  1 133 ? -31.537  63.665  -45.792  1.00 44.50  ? 133 PRO C CB  1 
ATOM   9561  C CG  . PRO C  1 133 ? -30.213  62.934  -45.925  1.00 43.86  ? 133 PRO C CG  1 
ATOM   9562  C CD  . PRO C  1 133 ? -30.507  61.838  -46.955  1.00 41.96  ? 133 PRO C CD  1 
ATOM   9563  N N   . GLN C  1 134 ? -32.479  65.703  -48.500  1.00 44.91  ? 134 GLN C N   1 
ATOM   9564  C CA  . GLN C  1 134 ? -32.165  66.848  -49.329  1.00 46.02  ? 134 GLN C CA  1 
ATOM   9565  C C   . GLN C  1 134 ? -31.615  67.971  -48.452  1.00 45.04  ? 134 GLN C C   1 
ATOM   9566  O O   . GLN C  1 134 ? -32.071  68.118  -47.317  1.00 43.09  ? 134 GLN C O   1 
ATOM   9567  C CB  . GLN C  1 134 ? -33.409  67.281  -50.098  1.00 48.29  ? 134 GLN C CB  1 
ATOM   9568  C CG  . GLN C  1 134 ? -33.741  66.407  -51.300  1.00 49.71  ? 134 GLN C CG  1 
ATOM   9569  C CD  . GLN C  1 134 ? -32.819  66.572  -52.489  1.00 55.10  ? 134 GLN C CD  1 
ATOM   9570  O OE1 . GLN C  1 134 ? -32.788  65.672  -53.332  1.00 65.63  ? 134 GLN C OE1 1 
ATOM   9571  N NE2 . GLN C  1 134 ? -32.048  67.659  -52.591  1.00 54.27  ? 134 GLN C NE2 1 
ATOM   9572  N N   . THR C  1 135 ? -30.638  68.710  -49.027  1.00 44.89  ? 135 THR C N   1 
ATOM   9573  C CA  . THR C  1 135 ? -30.007  69.888  -48.444  1.00 47.17  ? 135 THR C CA  1 
ATOM   9574  C C   . THR C  1 135 ? -31.055  70.904  -47.977  1.00 50.32  ? 135 THR C C   1 
ATOM   9575  O O   . THR C  1 135 ? -31.009  71.379  -46.841  1.00 54.55  ? 135 THR C O   1 
ATOM   9576  C CB  . THR C  1 135 ? -29.070  70.580  -49.439  1.00 45.51  ? 135 THR C CB  1 
ATOM   9577  O OG1 . THR C  1 135 ? -28.230  69.684  -50.173  1.00 42.71  ? 135 THR C OG1 1 
ATOM   9578  C CG2 . THR C  1 135 ? -28.231  71.621  -48.719  1.00 46.20  ? 135 THR C CG2 1 
ATOM   9579  N N   . ASP C  1 136 ? -31.990  71.274  -48.858  1.00 49.48  ? 136 ASP C N   1 
ATOM   9580  C CA  . ASP C  1 136 ? -32.933  72.325  -48.500  1.00 50.67  ? 136 ASP C CA  1 
ATOM   9581  C C   . ASP C  1 136 ? -33.868  71.837  -47.381  1.00 51.42  ? 136 ASP C C   1 
ATOM   9582  O O   . ASP C  1 136 ? -34.279  72.612  -46.507  1.00 53.22  ? 136 ASP C O   1 
ATOM   9583  C CB  . ASP C  1 136 ? -33.633  72.915  -49.715  1.00 47.59  ? 136 ASP C CB  1 
ATOM   9584  C CG  . ASP C  1 136 ? -34.581  74.040  -49.341  1.00 49.37  ? 136 ASP C CG  1 
ATOM   9585  O OD1 . ASP C  1 136 ? -34.096  75.151  -49.047  1.00 49.09  ? 136 ASP C OD1 1 
ATOM   9586  O OD2 . ASP C  1 136 ? -35.788  73.774  -49.271  1.00 49.55  ? 136 ASP C OD2 1 
ATOM   9587  N N   . HIS C  1 137 ? -34.189  70.544  -47.406  1.00 48.91  ? 137 HIS C N   1 
ATOM   9588  C CA  . HIS C  1 137 ? -35.103  69.960  -46.436  1.00 49.14  ? 137 HIS C CA  1 
ATOM   9589  C C   . HIS C  1 137 ? -34.466  69.849  -45.054  1.00 47.68  ? 137 HIS C C   1 
ATOM   9590  O O   . HIS C  1 137 ? -35.153  70.043  -44.074  1.00 49.39  ? 137 HIS C O   1 
ATOM   9591  C CB  . HIS C  1 137 ? -35.660  68.613  -46.910  1.00 48.41  ? 137 HIS C CB  1 
ATOM   9592  C CG  . HIS C  1 137 ? -36.657  68.085  -45.942  1.00 51.76  ? 137 HIS C CG  1 
ATOM   9593  N ND1 . HIS C  1 137 ? -36.340  67.117  -45.008  1.00 52.49  ? 137 HIS C ND1 1 
ATOM   9594  C CD2 . HIS C  1 137 ? -37.944  68.422  -45.731  1.00 53.62  ? 137 HIS C CD2 1 
ATOM   9595  C CE1 . HIS C  1 137 ? -37.423  66.867  -44.286  1.00 55.64  ? 137 HIS C CE1 1 
ATOM   9596  N NE2 . HIS C  1 137 ? -38.405  67.661  -44.695  1.00 54.27  ? 137 HIS C NE2 1 
ATOM   9597  N N   . ILE C  1 138 ? -33.167  69.553  -44.966  1.00 47.39  ? 138 ILE C N   1 
ATOM   9598  C CA  . ILE C  1 138 ? -32.466  69.536  -43.687  1.00 46.66  ? 138 ILE C CA  1 
ATOM   9599  C C   . ILE C  1 138 ? -32.371  70.954  -43.128  1.00 47.22  ? 138 ILE C C   1 
ATOM   9600  O O   . ILE C  1 138 ? -32.457  71.124  -41.918  1.00 48.35  ? 138 ILE C O   1 
ATOM   9601  C CB  . ILE C  1 138 ? -31.061  68.913  -43.806  1.00 45.78  ? 138 ILE C CB  1 
ATOM   9602  C CG1 . ILE C  1 138 ? -31.094  67.433  -44.282  1.00 45.89  ? 138 ILE C CG1 1 
ATOM   9603  C CG2 . ILE C  1 138 ? -30.307  69.053  -42.484  1.00 46.18  ? 138 ILE C CG2 1 
ATOM   9604  C CD1 . ILE C  1 138 ? -29.731  66.847  -44.652  1.00 43.90  ? 138 ILE C CD1 1 
ATOM   9605  N N   . HIS C  1 139 ? -32.132  71.970  -43.982  1.00 47.85  ? 139 HIS C N   1 
ATOM   9606  C CA  . HIS C  1 139 ? -32.042  73.355  -43.501  1.00 48.83  ? 139 HIS C CA  1 
ATOM   9607  C C   . HIS C  1 139 ? -33.355  73.738  -42.810  1.00 50.46  ? 139 HIS C C   1 
ATOM   9608  O O   . HIS C  1 139 ? -33.332  74.277  -41.706  1.00 51.79  ? 139 HIS C O   1 
ATOM   9609  C CB  . HIS C  1 139 ? -31.645  74.338  -44.618  1.00 47.65  ? 139 HIS C CB  1 
ATOM   9610  C CG  . HIS C  1 139 ? -31.726  75.788  -44.240  1.00 47.32  ? 139 HIS C CG  1 
ATOM   9611  N ND1 . HIS C  1 139 ? -32.871  76.535  -44.394  1.00 47.93  ? 139 HIS C ND1 1 
ATOM   9612  C CD2 . HIS C  1 139 ? -30.817  76.612  -43.699  1.00 47.34  ? 139 HIS C CD2 1 
ATOM   9613  C CE1 . HIS C  1 139 ? -32.648  77.765  -43.947  1.00 49.56  ? 139 HIS C CE1 1 
ATOM   9614  N NE2 . HIS C  1 139 ? -31.408  77.830  -43.512  1.00 48.99  ? 139 HIS C NE2 1 
ATOM   9615  N N   . SER C  1 140 ? -34.478  73.381  -43.455  1.00 51.24  ? 140 SER C N   1 
ATOM   9616  C CA  . SER C  1 140 ? -35.830  73.737  -43.057  1.00 53.44  ? 140 SER C CA  1 
ATOM   9617  C C   . SER C  1 140 ? -36.298  73.038  -41.776  1.00 54.08  ? 140 SER C C   1 
ATOM   9618  O O   . SER C  1 140 ? -37.105  73.591  -41.050  1.00 55.40  ? 140 SER C O   1 
ATOM   9619  C CB  . SER C  1 140 ? -36.787  73.440  -44.203  1.00 54.71  ? 140 SER C CB  1 
ATOM   9620  O OG  . SER C  1 140 ? -38.116  73.848  -43.884  1.00 56.85  ? 140 SER C OG  1 
ATOM   9621  N N   . VAL C  1 141 ? -35.909  71.789  -41.519  1.00 53.44  ? 141 VAL C N   1 
ATOM   9622  C CA  . VAL C  1 141 ? -36.350  71.137  -40.295  1.00 54.08  ? 141 VAL C CA  1 
ATOM   9623  C C   . VAL C  1 141 ? -35.234  71.206  -39.255  1.00 56.15  ? 141 VAL C C   1 
ATOM   9624  O O   . VAL C  1 141 ? -35.504  70.977  -38.076  1.00 56.54  ? 141 VAL C O   1 
ATOM   9625  C CB  . VAL C  1 141 ? -36.826  69.694  -40.518  1.00 52.91  ? 141 VAL C CB  1 
ATOM   9626  C CG1 . VAL C  1 141 ? -37.951  69.637  -41.548  1.00 52.47  ? 141 VAL C CG1 1 
ATOM   9627  C CG2 . VAL C  1 141 ? -35.675  68.775  -40.900  1.00 51.02  ? 141 VAL C CG2 1 
ATOM   9628  N N   . THR C  1 142 ? -34.001  71.481  -39.724  1.00 57.34  ? 142 THR C N   1 
ATOM   9629  C CA  . THR C  1 142 ? -32.836  71.875  -38.929  1.00 61.06  ? 142 THR C CA  1 
ATOM   9630  C C   . THR C  1 142 ? -31.790  70.756  -38.934  1.00 60.37  ? 142 THR C C   1 
ATOM   9631  O O   . THR C  1 142 ? -32.114  69.569  -38.901  1.00 60.84  ? 142 THR C O   1 
ATOM   9632  C CB  . THR C  1 142 ? -33.163  72.362  -37.505  1.00 66.95  ? 142 THR C CB  1 
ATOM   9633  O OG1 . THR C  1 142 ? -31.928  72.887  -37.012  1.00 68.64  ? 142 THR C OG1 1 
ATOM   9634  C CG2 . THR C  1 142 ? -33.580  71.295  -36.504  1.00 66.09  ? 142 THR C CG2 1 
ATOM   9635  N N   . GLY C  1 143 ? -30.521  71.165  -39.029  1.00 60.40  ? 143 GLY C N   1 
ATOM   9636  C CA  . GLY C  1 143 ? -29.381  70.294  -38.798  1.00 61.44  ? 143 GLY C CA  1 
ATOM   9637  C C   . GLY C  1 143 ? -29.564  69.423  -37.550  1.00 64.03  ? 143 GLY C C   1 
ATOM   9638  O O   . GLY C  1 143 ? -29.323  68.217  -37.590  1.00 62.73  ? 143 GLY C O   1 
ATOM   9639  N N   . LYS C  1 144 ? -29.989  70.047  -36.441  1.00 65.96  ? 144 LYS C N   1 
ATOM   9640  C CA  . LYS C  1 144 ? -30.048  69.397  -35.141  1.00 64.88  ? 144 LYS C CA  1 
ATOM   9641  C C   . LYS C  1 144 ? -31.006  68.207  -35.197  1.00 62.38  ? 144 LYS C C   1 
ATOM   9642  O O   . LYS C  1 144 ? -30.621  67.119  -34.794  1.00 60.52  ? 144 LYS C O   1 
ATOM   9643  C CB  . LYS C  1 144 ? -30.414  70.455  -34.097  1.00 69.79  ? 144 LYS C CB  1 
ATOM   9644  C CG  . LYS C  1 144 ? -30.842  69.967  -32.726  1.00 73.47  ? 144 LYS C CG  1 
ATOM   9645  C CD  . LYS C  1 144 ? -31.455  71.075  -31.873  1.00 78.32  ? 144 LYS C CD  1 
ATOM   9646  C CE  . LYS C  1 144 ? -32.306  70.581  -30.730  1.00 80.11  ? 144 LYS C CE  1 
ATOM   9647  N NZ  . LYS C  1 144 ? -31.707  69.410  -30.090  1.00 79.26  ? 144 LYS C NZ  1 
ATOM   9648  N N   . ALA C  1 145 ? -32.214  68.413  -35.751  1.00 60.60  ? 145 ALA C N   1 
ATOM   9649  C CA  . ALA C  1 145 ? -33.292  67.430  -35.741  1.00 60.26  ? 145 ALA C CA  1 
ATOM   9650  C C   . ALA C  1 145 ? -32.958  66.227  -36.626  1.00 61.01  ? 145 ALA C C   1 
ATOM   9651  O O   . ALA C  1 145 ? -33.512  65.142  -36.418  1.00 57.65  ? 145 ALA C O   1 
ATOM   9652  C CB  . ALA C  1 145 ? -34.588  68.058  -36.191  1.00 59.95  ? 145 ALA C CB  1 
ATOM   9653  N N   . PHE C  1 146 ? -32.118  66.480  -37.649  1.00 59.63  ? 146 PHE C N   1 
ATOM   9654  C CA  . PHE C  1 146 ? -31.513  65.456  -38.477  1.00 55.85  ? 146 PHE C CA  1 
ATOM   9655  C C   . PHE C  1 146 ? -30.508  64.637  -37.658  1.00 55.40  ? 146 PHE C C   1 
ATOM   9656  O O   . PHE C  1 146 ? -30.668  63.425  -37.527  1.00 54.55  ? 146 PHE C O   1 
ATOM   9657  C CB  . PHE C  1 146 ? -30.862  66.066  -39.727  1.00 53.97  ? 146 PHE C CB  1 
ATOM   9658  C CG  . PHE C  1 146 ? -30.088  65.037  -40.553  1.00 51.22  ? 146 PHE C CG  1 
ATOM   9659  C CD1 . PHE C  1 146 ? -30.756  64.079  -41.305  1.00 48.63  ? 146 PHE C CD1 1 
ATOM   9660  C CD2 . PHE C  1 146 ? -28.699  65.000  -40.535  1.00 49.99  ? 146 PHE C CD2 1 
ATOM   9661  C CE1 . PHE C  1 146 ? -30.052  63.102  -41.995  1.00 48.03  ? 146 PHE C CE1 1 
ATOM   9662  C CE2 . PHE C  1 146 ? -28.004  64.035  -41.253  1.00 49.09  ? 146 PHE C CE2 1 
ATOM   9663  C CZ  . PHE C  1 146 ? -28.680  63.086  -41.974  1.00 47.94  ? 146 PHE C CZ  1 
ATOM   9664  N N   . VAL C  1 147 ? -29.468  65.286  -37.127  1.00 54.80  ? 147 VAL C N   1 
ATOM   9665  C CA  . VAL C  1 147 ? -28.400  64.588  -36.429  1.00 54.55  ? 147 VAL C CA  1 
ATOM   9666  C C   . VAL C  1 147 ? -28.940  63.814  -35.224  1.00 57.21  ? 147 VAL C C   1 
ATOM   9667  O O   . VAL C  1 147 ? -28.460  62.720  -34.950  1.00 58.54  ? 147 VAL C O   1 
ATOM   9668  C CB  . VAL C  1 147 ? -27.265  65.527  -35.998  1.00 56.33  ? 147 VAL C CB  1 
ATOM   9669  C CG1 . VAL C  1 147 ? -26.198  64.775  -35.210  1.00 58.31  ? 147 VAL C CG1 1 
ATOM   9670  C CG2 . VAL C  1 147 ? -26.630  66.216  -37.195  1.00 54.94  ? 147 VAL C CG2 1 
ATOM   9671  N N   . ASP C  1 148 ? -29.909  64.392  -34.497  1.00 58.82  ? 148 ASP C N   1 
ATOM   9672  C CA  . ASP C  1 148 ? -30.552  63.766  -33.345  1.00 59.07  ? 148 ASP C CA  1 
ATOM   9673  C C   . ASP C  1 148 ? -31.356  62.520  -33.759  1.00 60.03  ? 148 ASP C C   1 
ATOM   9674  O O   . ASP C  1 148 ? -31.470  61.559  -32.991  1.00 60.53  ? 148 ASP C O   1 
ATOM   9675  C CB  . ASP C  1 148 ? -31.448  64.757  -32.608  1.00 59.38  ? 148 ASP C CB  1 
ATOM   9676  C CG  . ASP C  1 148 ? -30.753  65.805  -31.737  1.00 60.92  ? 148 ASP C CG  1 
ATOM   9677  O OD1 . ASP C  1 148 ? -29.521  65.737  -31.576  1.00 60.00  ? 148 ASP C OD1 1 
ATOM   9678  O OD2 . ASP C  1 148 ? -31.450  66.698  -31.206  1.00 62.34  ? 148 ASP C OD2 1 
ATOM   9679  N N   . LEU C  1 149 ? -31.974  62.562  -34.947  1.00 57.58  ? 149 LEU C N   1 
ATOM   9680  C CA  . LEU C  1 149 ? -32.713  61.434  -35.461  1.00 57.02  ? 149 LEU C CA  1 
ATOM   9681  C C   . LEU C  1 149 ? -31.705  60.330  -35.801  1.00 59.32  ? 149 LEU C C   1 
ATOM   9682  O O   . LEU C  1 149 ? -31.881  59.193  -35.383  1.00 61.49  ? 149 LEU C O   1 
ATOM   9683  C CB  . LEU C  1 149 ? -33.557  61.841  -36.667  1.00 55.38  ? 149 LEU C CB  1 
ATOM   9684  C CG  . LEU C  1 149 ? -34.245  60.679  -37.400  1.00 56.63  ? 149 LEU C CG  1 
ATOM   9685  C CD1 . LEU C  1 149 ? -35.341  60.089  -36.520  1.00 59.07  ? 149 LEU C CD1 1 
ATOM   9686  C CD2 . LEU C  1 149 ? -34.811  61.031  -38.760  1.00 54.36  ? 149 LEU C CD2 1 
ATOM   9687  N N   . MET C  1 150 ? -30.633  60.662  -36.534  1.00 57.64  ? 150 MET C N   1 
ATOM   9688  C CA  . MET C  1 150 ? -29.664  59.663  -36.943  1.00 56.84  ? 150 MET C CA  1 
ATOM   9689  C C   . MET C  1 150 ? -29.163  58.922  -35.710  1.00 58.68  ? 150 MET C C   1 
ATOM   9690  O O   . MET C  1 150 ? -29.250  57.701  -35.680  1.00 59.58  ? 150 MET C O   1 
ATOM   9691  C CB  . MET C  1 150 ? -28.468  60.261  -37.700  1.00 56.95  ? 150 MET C CB  1 
ATOM   9692  C CG  . MET C  1 150 ? -28.793  60.878  -39.050  1.00 54.59  ? 150 MET C CG  1 
ATOM   9693  S SD  . MET C  1 150 ? -29.565  59.737  -40.218  1.00 52.27  ? 150 MET C SD  1 
ATOM   9694  C CE  . MET C  1 150 ? -31.314  59.894  -39.825  1.00 52.27  ? 150 MET C CE  1 
ATOM   9695  N N   . ASN C  1 151 ? -28.667  59.662  -34.705  1.00 59.88  ? 151 ASN C N   1 
ATOM   9696  C CA  . ASN C  1 151 ? -28.118  59.076  -33.492  1.00 60.46  ? 151 ASN C CA  1 
ATOM   9697  C C   . ASN C  1 151 ? -29.129  58.161  -32.800  1.00 62.93  ? 151 ASN C C   1 
ATOM   9698  O O   . ASN C  1 151 ? -28.755  57.160  -32.187  1.00 62.06  ? 151 ASN C O   1 
ATOM   9699  C CB  . ASN C  1 151 ? -27.685  60.140  -32.494  1.00 60.86  ? 151 ASN C CB  1 
ATOM   9700  C CG  . ASN C  1 151 ? -26.402  60.802  -32.906  1.00 60.39  ? 151 ASN C CG  1 
ATOM   9701  O OD1 . ASN C  1 151 ? -26.243  62.018  -32.728  1.00 66.56  ? 151 ASN C OD1 1 
ATOM   9702  N ND2 . ASN C  1 151 ? -25.481  60.028  -33.451  1.00 57.68  ? 151 ASN C ND2 1 
ATOM   9703  N N   . THR C  1 152 ? -30.408  58.537  -32.871  1.00 65.37  ? 152 THR C N   1 
ATOM   9704  C CA  . THR C  1 152 ? -31.474  57.761  -32.260  1.00 68.01  ? 152 THR C CA  1 
ATOM   9705  C C   . THR C  1 152 ? -31.623  56.420  -32.990  1.00 66.07  ? 152 THR C C   1 
ATOM   9706  O O   . THR C  1 152 ? -31.782  55.383  -32.351  1.00 72.47  ? 152 THR C O   1 
ATOM   9707  C CB  . THR C  1 152 ? -32.760  58.593  -32.252  1.00 70.69  ? 152 THR C CB  1 
ATOM   9708  O OG1 . THR C  1 152 ? -32.484  59.708  -31.407  1.00 73.72  ? 152 THR C OG1 1 
ATOM   9709  C CG2 . THR C  1 152 ? -33.969  57.854  -31.704  1.00 73.50  ? 152 THR C CG2 1 
ATOM   9710  N N   . LEU C  1 153 ? -31.581  56.435  -34.321  1.00 61.29  ? 153 LEU C N   1 
ATOM   9711  C CA  . LEU C  1 153 ? -31.786  55.223  -35.100  1.00 61.20  ? 153 LEU C CA  1 
ATOM   9712  C C   . LEU C  1 153 ? -30.528  54.346  -35.047  1.00 59.81  ? 153 LEU C C   1 
ATOM   9713  O O   . LEU C  1 153 ? -30.629  53.121  -34.978  1.00 60.38  ? 153 LEU C O   1 
ATOM   9714  C CB  . LEU C  1 153 ? -32.188  55.576  -36.536  1.00 59.06  ? 153 LEU C CB  1 
ATOM   9715  C CG  . LEU C  1 153 ? -33.399  56.504  -36.706  1.00 58.19  ? 153 LEU C CG  1 
ATOM   9716  C CD1 . LEU C  1 153 ? -33.809  56.649  -38.156  1.00 55.57  ? 153 LEU C CD1 1 
ATOM   9717  C CD2 . LEU C  1 153 ? -34.581  56.011  -35.897  1.00 60.89  ? 153 LEU C CD2 1 
ATOM   9718  N N   . ILE C  1 154 ? -29.343  54.973  -35.076  1.00 56.81  ? 154 ILE C N   1 
ATOM   9719  C CA  . ILE C  1 154 ? -28.082  54.249  -35.020  1.00 55.68  ? 154 ILE C CA  1 
ATOM   9720  C C   . ILE C  1 154 ? -28.011  53.432  -33.730  1.00 58.69  ? 154 ILE C C   1 
ATOM   9721  O O   . ILE C  1 154 ? -27.525  52.309  -33.747  1.00 56.86  ? 154 ILE C O   1 
ATOM   9722  C CB  . ILE C  1 154 ? -26.881  55.203  -35.147  1.00 52.54  ? 154 ILE C CB  1 
ATOM   9723  C CG1 . ILE C  1 154 ? -26.877  55.910  -36.483  1.00 51.50  ? 154 ILE C CG1 1 
ATOM   9724  C CG2 . ILE C  1 154 ? -25.554  54.478  -34.909  1.00 50.99  ? 154 ILE C CG2 1 
ATOM   9725  C CD1 . ILE C  1 154 ? -25.861  57.031  -36.577  1.00 52.09  ? 154 ILE C CD1 1 
ATOM   9726  N N   . ASN C  1 155 ? -28.461  54.030  -32.617  1.00 62.73  ? 155 ASN C N   1 
ATOM   9727  C CA  . ASN C  1 155 ? -28.335  53.431  -31.298  1.00 64.69  ? 155 ASN C CA  1 
ATOM   9728  C C   . ASN C  1 155 ? -29.381  52.345  -31.099  1.00 62.75  ? 155 ASN C C   1 
ATOM   9729  O O   . ASN C  1 155 ? -29.071  51.334  -30.484  1.00 63.02  ? 155 ASN C O   1 
ATOM   9730  C CB  . ASN C  1 155 ? -28.379  54.473  -30.188  1.00 66.55  ? 155 ASN C CB  1 
ATOM   9731  C CG  . ASN C  1 155 ? -27.108  55.284  -30.188  1.00 67.76  ? 155 ASN C CG  1 
ATOM   9732  O OD1 . ASN C  1 155 ? -26.081  54.846  -30.725  1.00 66.38  ? 155 ASN C OD1 1 
ATOM   9733  N ND2 . ASN C  1 155 ? -27.155  56.457  -29.580  1.00 69.73  ? 155 ASN C ND2 1 
ATOM   9734  N N   . ILE C  1 156 ? -30.592  52.547  -31.624  1.00 59.70  ? 156 ILE C N   1 
ATOM   9735  C CA  . ILE C  1 156 ? -31.570  51.479  -31.654  1.00 60.24  ? 156 ILE C CA  1 
ATOM   9736  C C   . ILE C  1 156 ? -30.995  50.254  -32.373  1.00 60.76  ? 156 ILE C C   1 
ATOM   9737  O O   . ILE C  1 156 ? -31.269  49.119  -31.969  1.00 63.57  ? 156 ILE C O   1 
ATOM   9738  C CB  . ILE C  1 156 ? -32.897  51.956  -32.264  1.00 61.25  ? 156 ILE C CB  1 
ATOM   9739  C CG1 . ILE C  1 156 ? -33.655  52.833  -31.269  1.00 64.76  ? 156 ILE C CG1 1 
ATOM   9740  C CG2 . ILE C  1 156 ? -33.762  50.781  -32.720  1.00 61.10  ? 156 ILE C CG2 1 
ATOM   9741  C CD1 . ILE C  1 156 ? -34.917  53.471  -31.825  1.00 65.32  ? 156 ILE C CD1 1 
ATOM   9742  N N   . ILE C  1 157 ? -30.192  50.468  -33.426  1.00 58.98  ? 157 ILE C N   1 
ATOM   9743  C CA  . ILE C  1 157 ? -29.664  49.354  -34.201  1.00 57.36  ? 157 ILE C CA  1 
ATOM   9744  C C   . ILE C  1 157 ? -28.473  48.730  -33.471  1.00 58.82  ? 157 ILE C C   1 
ATOM   9745  O O   . ILE C  1 157 ? -28.417  47.504  -33.348  1.00 58.47  ? 157 ILE C O   1 
ATOM   9746  C CB  . ILE C  1 157 ? -29.339  49.746  -35.653  1.00 54.37  ? 157 ILE C CB  1 
ATOM   9747  C CG1 . ILE C  1 157 ? -30.594  50.112  -36.429  1.00 52.80  ? 157 ILE C CG1 1 
ATOM   9748  C CG2 . ILE C  1 157 ? -28.556  48.639  -36.365  1.00 53.04  ? 157 ILE C CG2 1 
ATOM   9749  C CD1 . ILE C  1 157 ? -30.321  50.897  -37.704  1.00 51.05  ? 157 ILE C CD1 1 
ATOM   9750  N N   . HIS C  1 158 ? -27.601  49.562  -32.936  1.00 57.52  ? 158 HIS C N   1 
ATOM   9751  C CA  . HIS C  1 158 ? -26.403  48.993  -32.284  1.00 58.40  ? 158 HIS C CA  1 
ATOM   9752  C C   . HIS C  1 158 ? -26.848  48.051  -31.162  1.00 59.02  ? 158 HIS C C   1 
ATOM   9753  O O   . HIS C  1 158 ? -26.099  47.117  -30.834  1.00 59.01  ? 158 HIS C O   1 
ATOM   9754  C CB  . HIS C  1 158 ? -25.466  50.121  -31.852  1.00 57.17  ? 158 HIS C CB  1 
ATOM   9755  C CG  . HIS C  1 158 ? -24.697  50.699  -32.987  1.00 54.75  ? 158 HIS C CG  1 
ATOM   9756  N ND1 . HIS C  1 158 ? -23.753  51.686  -32.824  1.00 54.39  ? 158 HIS C ND1 1 
ATOM   9757  C CD2 . HIS C  1 158 ? -24.728  50.426  -34.293  1.00 52.69  ? 158 HIS C CD2 1 
ATOM   9758  C CE1 . HIS C  1 158 ? -23.237  51.988  -34.002  1.00 52.83  ? 158 HIS C CE1 1 
ATOM   9759  N NE2 . HIS C  1 158 ? -23.815  51.235  -34.907  1.00 51.88  ? 158 HIS C NE2 1 
ATOM   9760  N N   . LYS C  1 159 ? -28.043  48.264  -30.619  1.00 60.78  ? 159 LYS C N   1 
ATOM   9761  C CA  . LYS C  1 159 ? -28.491  47.454  -29.459  1.00 65.69  ? 159 LYS C CA  1 
ATOM   9762  C C   . LYS C  1 159 ? -29.447  46.332  -29.896  1.00 62.59  ? 159 LYS C C   1 
ATOM   9763  O O   . LYS C  1 159 ? -29.362  45.246  -29.298  1.00 60.96  ? 159 LYS C O   1 
ATOM   9764  C CB  . LYS C  1 159 ? -29.123  48.387  -28.423  1.00 73.98  ? 159 LYS C CB  1 
ATOM   9765  C CG  . LYS C  1 159 ? -28.125  49.234  -27.652  1.00 85.83  ? 159 LYS C CG  1 
ATOM   9766  C CD  . LYS C  1 159 ? -28.782  50.170  -26.646  1.00 96.56  ? 159 LYS C CD  1 
ATOM   9767  C CE  . LYS C  1 159 ? -29.069  51.525  -27.209  1.00 100.43 ? 159 LYS C CE  1 
ATOM   9768  N NZ  . LYS C  1 159 ? -29.947  52.309  -26.337  1.00 102.96 ? 159 LYS C NZ  1 
ATOM   9769  N N   . GLY C  1 160 ? -30.308  46.581  -30.883  1.00 59.35  ? 160 GLY C N   1 
ATOM   9770  C CA  . GLY C  1 160 ? -31.303  45.582  -31.322  1.00 56.99  ? 160 GLY C CA  1 
ATOM   9771  C C   . GLY C  1 160 ? -30.671  44.503  -32.165  1.00 53.55  ? 160 GLY C C   1 
ATOM   9772  O O   . GLY C  1 160 ? -31.130  43.357  -32.089  1.00 51.88  ? 160 GLY C O   1 
ATOM   9773  N N   . HIS C  1 161 ? -29.692  44.869  -32.977  1.00 50.54  ? 161 HIS C N   1 
ATOM   9774  C CA  . HIS C  1 161 ? -28.941  43.918  -33.776  1.00 48.50  ? 161 HIS C CA  1 
ATOM   9775  C C   . HIS C  1 161 ? -27.449  44.195  -33.593  1.00 48.46  ? 161 HIS C C   1 
ATOM   9776  O O   . HIS C  1 161 ? -26.836  44.835  -34.440  1.00 47.66  ? 161 HIS C O   1 
ATOM   9777  C CB  . HIS C  1 161 ? -29.336  44.028  -35.251  1.00 46.62  ? 161 HIS C CB  1 
ATOM   9778  C CG  . HIS C  1 161 ? -28.907  42.874  -36.102  1.00 45.05  ? 161 HIS C CG  1 
ATOM   9779  N ND1 . HIS C  1 161 ? -29.411  42.669  -37.370  1.00 42.37  ? 161 HIS C ND1 1 
ATOM   9780  C CD2 . HIS C  1 161 ? -28.023  41.867  -35.876  1.00 45.95  ? 161 HIS C CD2 1 
ATOM   9781  C CE1 . HIS C  1 161 ? -28.855  41.570  -37.875  1.00 43.75  ? 161 HIS C CE1 1 
ATOM   9782  N NE2 . HIS C  1 161 ? -28.023  41.042  -36.979  1.00 44.03  ? 161 HIS C NE2 1 
ATOM   9783  N N   . PRO C  1 162 ? -26.815  43.722  -32.488  1.00 50.56  ? 162 PRO C N   1 
ATOM   9784  C CA  . PRO C  1 162 ? -25.385  43.963  -32.245  1.00 50.74  ? 162 PRO C CA  1 
ATOM   9785  C C   . PRO C  1 162 ? -24.467  43.597  -33.406  1.00 50.26  ? 162 PRO C C   1 
ATOM   9786  O O   . PRO C  1 162 ? -24.714  42.634  -34.133  1.00 53.52  ? 162 PRO C O   1 
ATOM   9787  C CB  . PRO C  1 162 ? -25.072  43.091  -30.997  1.00 50.83  ? 162 PRO C CB  1 
ATOM   9788  C CG  . PRO C  1 162 ? -26.400  42.935  -30.299  1.00 51.21  ? 162 PRO C CG  1 
ATOM   9789  C CD  . PRO C  1 162 ? -27.453  42.963  -31.392  1.00 50.34  ? 162 PRO C CD  1 
ATOM   9790  N N   . GLY C  1 163 ? -23.406  44.379  -33.573  1.00 49.05  ? 163 GLY C N   1 
ATOM   9791  C CA  . GLY C  1 163 ? -22.260  43.955  -34.349  1.00 46.55  ? 163 GLY C CA  1 
ATOM   9792  C C   . GLY C  1 163 ? -22.399  44.331  -35.811  1.00 45.72  ? 163 GLY C C   1 
ATOM   9793  O O   . GLY C  1 163 ? -21.465  44.122  -36.575  1.00 47.22  ? 163 GLY C O   1 
ATOM   9794  N N   . ILE C  1 164 ? -23.540  44.909  -36.198  1.00 45.42  ? 164 ILE C N   1 
ATOM   9795  C CA  . ILE C  1 164 ? -23.777  45.244  -37.600  1.00 43.23  ? 164 ILE C CA  1 
ATOM   9796  C C   . ILE C  1 164 ? -23.492  46.728  -37.841  1.00 42.51  ? 164 ILE C C   1 
ATOM   9797  O O   . ILE C  1 164 ? -24.060  47.598  -37.203  1.00 44.51  ? 164 ILE C O   1 
ATOM   9798  C CB  . ILE C  1 164 ? -25.222  44.880  -38.003  1.00 42.70  ? 164 ILE C CB  1 
ATOM   9799  C CG1 . ILE C  1 164 ? -25.620  43.465  -37.572  1.00 43.28  ? 164 ILE C CG1 1 
ATOM   9800  C CG2 . ILE C  1 164 ? -25.451  45.102  -39.491  1.00 41.03  ? 164 ILE C CG2 1 
ATOM   9801  C CD1 . ILE C  1 164 ? -24.733  42.363  -38.112  1.00 41.57  ? 164 ILE C CD1 1 
ATOM   9802  N N   . PRO C  1 165 ? -22.621  47.080  -38.795  1.00 40.85  ? 165 PRO C N   1 
ATOM   9803  C CA  . PRO C  1 165 ? -22.437  48.475  -39.201  1.00 40.52  ? 165 PRO C CA  1 
ATOM   9804  C C   . PRO C  1 165 ? -23.663  49.277  -39.620  1.00 41.65  ? 165 PRO C C   1 
ATOM   9805  O O   . PRO C  1 165 ? -24.513  48.767  -40.350  1.00 42.28  ? 165 PRO C O   1 
ATOM   9806  C CB  . PRO C  1 165 ? -21.507  48.332  -40.397  1.00 38.63  ? 165 PRO C CB  1 
ATOM   9807  C CG  . PRO C  1 165 ? -20.705  47.108  -40.100  1.00 39.27  ? 165 PRO C CG  1 
ATOM   9808  C CD  . PRO C  1 165 ? -21.710  46.153  -39.468  1.00 40.03  ? 165 PRO C CD  1 
ATOM   9809  N N   . VAL C  1 166 ? -23.678  50.575  -39.272  1.00 42.15  ? 166 VAL C N   1 
ATOM   9810  C CA  . VAL C  1 166 ? -24.772  51.449  -39.684  1.00 41.97  ? 166 VAL C CA  1 
ATOM   9811  C C   . VAL C  1 166 ? -24.246  52.656  -40.468  1.00 41.35  ? 166 VAL C C   1 
ATOM   9812  O O   . VAL C  1 166 ? -23.354  53.382  -40.005  1.00 42.90  ? 166 VAL C O   1 
ATOM   9813  C CB  . VAL C  1 166 ? -25.635  51.892  -38.490  1.00 42.58  ? 166 VAL C CB  1 
ATOM   9814  C CG1 . VAL C  1 166 ? -26.730  52.843  -38.948  1.00 42.36  ? 166 VAL C CG1 1 
ATOM   9815  C CG2 . VAL C  1 166 ? -26.251  50.688  -37.753  1.00 43.64  ? 166 VAL C CG2 1 
ATOM   9816  N N   . THR C  1 167 ? -24.798  52.865  -41.672  1.00 38.41  ? 167 THR C N   1 
ATOM   9817  C CA  . THR C  1 167 ? -24.558  54.105  -42.382  1.00 38.01  ? 167 THR C CA  1 
ATOM   9818  C C   . THR C  1 167 ? -25.846  54.529  -43.091  1.00 38.05  ? 167 THR C C   1 
ATOM   9819  O O   . THR C  1 167 ? -26.939  54.127  -42.682  1.00 38.05  ? 167 THR C O   1 
ATOM   9820  C CB  . THR C  1 167 ? -23.320  53.988  -43.273  1.00 36.88  ? 167 THR C CB  1 
ATOM   9821  O OG1 . THR C  1 167 ? -22.995  55.311  -43.714  1.00 35.84  ? 167 THR C OG1 1 
ATOM   9822  C CG2 . THR C  1 167 ? -23.512  53.022  -44.426  1.00 34.97  ? 167 THR C CG2 1 
ATOM   9823  N N   . LEU C  1 168 ? -25.707  55.440  -44.067  1.00 37.26  ? 168 LEU C N   1 
ATOM   9824  C CA  . LEU C  1 168 ? -26.853  56.015  -44.749  1.00 37.26  ? 168 LEU C CA  1 
ATOM   9825  C C   . LEU C  1 168 ? -26.590  56.058  -46.247  1.00 36.22  ? 168 LEU C C   1 
ATOM   9826  O O   . LEU C  1 168 ? -25.473  55.852  -46.702  1.00 36.55  ? 168 LEU C O   1 
ATOM   9827  C CB  . LEU C  1 168 ? -27.146  57.409  -44.196  1.00 38.14  ? 168 LEU C CB  1 
ATOM   9828  C CG  . LEU C  1 168 ? -26.380  58.566  -44.845  1.00 36.99  ? 168 LEU C CG  1 
ATOM   9829  C CD1 . LEU C  1 168 ? -26.865  59.908  -44.323  1.00 38.17  ? 168 LEU C CD1 1 
ATOM   9830  C CD2 . LEU C  1 168 ? -24.903  58.414  -44.624  1.00 36.51  ? 168 LEU C CD2 1 
ATOM   9831  N N   . SER C  1 169 ? -27.651  56.362  -46.993  1.00 36.75  ? 169 SER C N   1 
ATOM   9832  C CA  . SER C  1 169 ? -27.586  56.584  -48.429  1.00 34.88  ? 169 SER C CA  1 
ATOM   9833  C C   . SER C  1 169 ? -27.686  58.089  -48.727  1.00 36.09  ? 169 SER C C   1 
ATOM   9834  O O   . SER C  1 169 ? -28.728  58.707  -48.572  1.00 35.09  ? 169 SER C O   1 
ATOM   9835  C CB  . SER C  1 169 ? -28.688  55.795  -49.060  1.00 34.65  ? 169 SER C CB  1 
ATOM   9836  O OG  . SER C  1 169 ? -28.988  56.236  -50.370  1.00 34.87  ? 169 SER C OG  1 
ATOM   9837  N N   . ALA C  1 170 ? -26.572  58.690  -49.131  1.00 37.38  ? 170 ALA C N   1 
ATOM   9838  C CA  . ALA C  1 170 ? -26.519  60.107  -49.446  1.00 36.75  ? 170 ALA C CA  1 
ATOM   9839  C C   . ALA C  1 170 ? -25.627  60.339  -50.671  1.00 36.80  ? 170 ALA C C   1 
ATOM   9840  O O   . ALA C  1 170 ? -24.471  59.882  -50.726  1.00 33.95  ? 170 ALA C O   1 
ATOM   9841  C CB  . ALA C  1 170 ? -26.033  60.903  -48.253  1.00 37.04  ? 170 ALA C CB  1 
ATOM   9842  N N   . ASN C  1 171 ? -26.181  61.115  -51.617  1.00 35.70  ? 171 ASN C N   1 
ATOM   9843  C CA  . ASN C  1 171 ? -25.548  61.428  -52.877  1.00 36.13  ? 171 ASN C CA  1 
ATOM   9844  C C   . ASN C  1 171 ? -24.393  62.407  -52.634  1.00 37.97  ? 171 ASN C C   1 
ATOM   9845  O O   . ASN C  1 171 ? -24.561  63.410  -51.925  1.00 39.08  ? 171 ASN C O   1 
ATOM   9846  C CB  . ASN C  1 171 ? -26.635  61.938  -53.819  1.00 38.10  ? 171 ASN C CB  1 
ATOM   9847  C CG  . ASN C  1 171 ? -26.170  62.124  -55.241  1.00 39.44  ? 171 ASN C CG  1 
ATOM   9848  O OD1 . ASN C  1 171 ? -25.301  62.959  -55.512  1.00 39.02  ? 171 ASN C OD1 1 
ATOM   9849  N ND2 . ASN C  1 171 ? -26.740  61.353  -56.159  1.00 41.81  ? 171 ASN C ND2 1 
ATOM   9850  N N   . ALA C  1 172 ? -23.235  62.115  -53.256  1.00 36.27  ? 172 ALA C N   1 
ATOM   9851  C CA  . ALA C  1 172 ? -22.008  62.881  -53.071  1.00 35.18  ? 172 ALA C CA  1 
ATOM   9852  C C   . ALA C  1 172 ? -22.147  64.286  -53.651  1.00 35.38  ? 172 ALA C C   1 
ATOM   9853  O O   . ALA C  1 172 ? -21.462  65.212  -53.237  1.00 37.12  ? 172 ALA C O   1 
ATOM   9854  C CB  . ALA C  1 172 ? -20.841  62.156  -53.723  1.00 33.84  ? 172 ALA C CB  1 
ATOM   9855  N N   . MET C  1 173 ? -23.015  64.436  -54.648  1.00 35.93  ? 173 MET C N   1 
ATOM   9856  C CA  . MET C  1 173 ? -23.183  65.704  -55.346  1.00 35.00  ? 173 MET C CA  1 
ATOM   9857  C C   . MET C  1 173 ? -23.975  66.716  -54.519  1.00 34.95  ? 173 MET C C   1 
ATOM   9858  O O   . MET C  1 173 ? -23.820  67.902  -54.783  1.00 35.63  ? 173 MET C O   1 
ATOM   9859  C CB  . MET C  1 173 ? -23.814  65.481  -56.735  1.00 34.12  ? 173 MET C CB  1 
ATOM   9860  C CG  . MET C  1 173 ? -22.878  64.797  -57.744  1.00 32.62  ? 173 MET C CG  1 
ATOM   9861  S SD  . MET C  1 173 ? -21.485  65.805  -58.321  1.00 33.76  ? 173 MET C SD  1 
ATOM   9862  C CE  . MET C  1 173 ? -22.277  67.044  -59.348  1.00 33.62  ? 173 MET C CE  1 
ATOM   9863  N N   . ILE C  1 174 ? -24.800  66.267  -53.544  1.00 36.48  ? 174 ILE C N   1 
ATOM   9864  C CA  . ILE C  1 174 ? -25.610  67.173  -52.728  1.00 37.35  ? 174 ILE C CA  1 
ATOM   9865  C C   . ILE C  1 174 ? -25.266  67.076  -51.240  1.00 38.17  ? 174 ILE C C   1 
ATOM   9866  O O   . ILE C  1 174 ? -25.648  67.967  -50.460  1.00 38.40  ? 174 ILE C O   1 
ATOM   9867  C CB  . ILE C  1 174 ? -27.134  66.973  -52.888  1.00 37.56  ? 174 ILE C CB  1 
ATOM   9868  C CG1 . ILE C  1 174 ? -27.544  65.548  -52.504  1.00 39.37  ? 174 ILE C CG1 1 
ATOM   9869  C CG2 . ILE C  1 174 ? -27.649  67.387  -54.272  1.00 35.49  ? 174 ILE C CG2 1 
ATOM   9870  C CD1 . ILE C  1 174 ? -29.011  65.410  -52.138  1.00 40.35  ? 174 ILE C CD1 1 
ATOM   9871  N N   . SER C  1 175 ? -24.617  65.993  -50.807  1.00 35.82  ? 175 SER C N   1 
ATOM   9872  C CA  . SER C  1 175 ? -24.297  65.909  -49.393  1.00 36.32  ? 175 SER C CA  1 
ATOM   9873  C C   . SER C  1 175 ? -22.797  65.738  -49.188  1.00 35.79  ? 175 SER C C   1 
ATOM   9874  O O   . SER C  1 175 ? -22.342  65.167  -48.205  1.00 35.86  ? 175 SER C O   1 
ATOM   9875  C CB  . SER C  1 175 ? -25.107  64.835  -48.718  1.00 37.36  ? 175 SER C CB  1 
ATOM   9876  O OG  . SER C  1 175 ? -26.503  65.019  -48.925  1.00 37.07  ? 175 SER C OG  1 
ATOM   9877  N N   . ASP C  1 176 ? -22.020  66.277  -50.120  1.00 36.55  ? 176 ASP C N   1 
ATOM   9878  C CA  . ASP C  1 176 ? -20.606  66.527  -49.897  1.00 37.93  ? 176 ASP C CA  1 
ATOM   9879  C C   . ASP C  1 176 ? -20.321  67.224  -48.556  1.00 40.56  ? 176 ASP C C   1 
ATOM   9880  O O   . ASP C  1 176 ? -19.314  66.946  -47.916  1.00 43.38  ? 176 ASP C O   1 
ATOM   9881  C CB  . ASP C  1 176 ? -20.052  67.337  -51.059  1.00 37.85  ? 176 ASP C CB  1 
ATOM   9882  C CG  . ASP C  1 176 ? -20.744  68.652  -51.393  1.00 36.90  ? 176 ASP C CG  1 
ATOM   9883  O OD1 . ASP C  1 176 ? -21.813  68.926  -50.821  1.00 35.36  ? 176 ASP C OD1 1 
ATOM   9884  O OD2 . ASP C  1 176 ? -20.185  69.397  -52.230  1.00 36.15  ? 176 ASP C OD2 1 
ATOM   9885  N N   . TYR C  1 177 ? -21.182  68.155  -48.123  1.00 41.67  ? 177 TYR C N   1 
ATOM   9886  C CA  . TYR C  1 177 ? -20.946  68.956  -46.922  1.00 42.25  ? 177 TYR C CA  1 
ATOM   9887  C C   . TYR C  1 177 ? -21.127  68.126  -45.634  1.00 43.10  ? 177 TYR C C   1 
ATOM   9888  O O   . TYR C  1 177 ? -20.560  68.487  -44.583  1.00 42.45  ? 177 TYR C O   1 
ATOM   9889  C CB  . TYR C  1 177 ? -21.857  70.206  -46.937  1.00 42.09  ? 177 TYR C CB  1 
ATOM   9890  C CG  . TYR C  1 177 ? -23.317  69.869  -46.697  1.00 42.13  ? 177 TYR C CG  1 
ATOM   9891  C CD1 . TYR C  1 177 ? -23.842  69.798  -45.416  1.00 43.34  ? 177 TYR C CD1 1 
ATOM   9892  C CD2 . TYR C  1 177 ? -24.131  69.470  -47.744  1.00 41.99  ? 177 TYR C CD2 1 
ATOM   9893  C CE1 . TYR C  1 177 ? -25.157  69.415  -45.200  1.00 43.97  ? 177 TYR C CE1 1 
ATOM   9894  C CE2 . TYR C  1 177 ? -25.438  69.067  -47.540  1.00 41.87  ? 177 TYR C CE2 1 
ATOM   9895  C CZ  . TYR C  1 177 ? -25.962  69.061  -46.269  1.00 42.38  ? 177 TYR C CZ  1 
ATOM   9896  O OH  . TYR C  1 177 ? -27.258  68.678  -46.128  1.00 43.30  ? 177 TYR C OH  1 
ATOM   9897  N N   . MET C  1 178 ? -21.947  67.049  -45.697  1.00 41.93  ? 178 MET C N   1 
ATOM   9898  C CA  . MET C  1 178 ? -22.501  66.386  -44.508  1.00 43.12  ? 178 MET C CA  1 
ATOM   9899  C C   . MET C  1 178 ? -21.419  65.670  -43.709  1.00 44.23  ? 178 MET C C   1 
ATOM   9900  O O   . MET C  1 178 ? -20.474  65.129  -44.283  1.00 43.86  ? 178 MET C O   1 
ATOM   9901  C CB  . MET C  1 178 ? -23.558  65.345  -44.888  1.00 41.97  ? 178 MET C CB  1 
ATOM   9902  C CG  . MET C  1 178 ? -24.175  64.584  -43.740  1.00 43.14  ? 178 MET C CG  1 
ATOM   9903  S SD  . MET C  1 178 ? -25.516  63.489  -44.269  1.00 44.31  ? 178 MET C SD  1 
ATOM   9904  C CE  . MET C  1 178 ? -26.733  64.610  -44.970  1.00 44.11  ? 178 MET C CE  1 
ATOM   9905  N N   . ASP C  1 179 ? -21.566  65.700  -42.384  1.00 46.61  ? 179 ASP C N   1 
ATOM   9906  C CA  . ASP C  1 179 ? -20.724  64.916  -41.488  1.00 49.70  ? 179 ASP C CA  1 
ATOM   9907  C C   . ASP C  1 179 ? -21.200  63.458  -41.463  1.00 47.20  ? 179 ASP C C   1 
ATOM   9908  O O   . ASP C  1 179 ? -22.349  63.186  -41.173  1.00 45.66  ? 179 ASP C O   1 
ATOM   9909  C CB  . ASP C  1 179 ? -20.737  65.530  -40.096  1.00 51.97  ? 179 ASP C CB  1 
ATOM   9910  C CG  . ASP C  1 179 ? -19.873  64.863  -39.037  1.00 54.15  ? 179 ASP C CG  1 
ATOM   9911  O OD1 . ASP C  1 179 ? -18.966  64.066  -39.389  1.00 51.13  ? 179 ASP C OD1 1 
ATOM   9912  O OD2 . ASP C  1 179 ? -20.138  65.137  -37.855  1.00 58.27  ? 179 ASP C OD2 1 
ATOM   9913  N N   . GLU C  1 180 ? -20.312  62.507  -41.750  1.00 46.69  ? 180 GLU C N   1 
ATOM   9914  C CA  . GLU C  1 180 ? -20.687  61.101  -41.708  1.00 46.48  ? 180 GLU C CA  1 
ATOM   9915  C C   . GLU C  1 180 ? -20.037  60.371  -40.531  1.00 47.60  ? 180 GLU C C   1 
ATOM   9916  O O   . GLU C  1 180 ? -20.241  59.161  -40.370  1.00 47.88  ? 180 GLU C O   1 
ATOM   9917  C CB  . GLU C  1 180 ? -20.318  60.422  -43.024  1.00 46.06  ? 180 GLU C CB  1 
ATOM   9918  C CG  . GLU C  1 180 ? -21.268  60.799  -44.151  1.00 46.49  ? 180 GLU C CG  1 
ATOM   9919  C CD  . GLU C  1 180 ? -21.282  59.848  -45.317  1.00 45.88  ? 180 GLU C CD  1 
ATOM   9920  O OE1 . GLU C  1 180 ? -20.425  58.953  -45.328  1.00 48.27  ? 180 GLU C OE1 1 
ATOM   9921  O OE2 . GLU C  1 180 ? -22.137  60.008  -46.205  1.00 46.56  ? 180 GLU C OE2 1 
ATOM   9922  N N   . SER C  1 181 ? -19.345  61.131  -39.668  1.00 47.69  ? 181 SER C N   1 
ATOM   9923  C CA  . SER C  1 181 ? -18.510  60.594  -38.603  1.00 48.79  ? 181 SER C CA  1 
ATOM   9924  C C   . SER C  1 181 ? -19.346  59.897  -37.522  1.00 50.87  ? 181 SER C C   1 
ATOM   9925  O O   . SER C  1 181 ? -18.802  59.156  -36.705  1.00 51.79  ? 181 SER C O   1 
ATOM   9926  C CB  . SER C  1 181 ? -17.663  61.689  -37.983  1.00 49.54  ? 181 SER C CB  1 
ATOM   9927  O OG  . SER C  1 181 ? -18.472  62.464  -37.112  1.00 49.38  ? 181 SER C OG  1 
ATOM   9928  N N   . ILE C  1 182 ? -20.654  60.170  -37.480  1.00 51.20  ? 182 ILE C N   1 
ATOM   9929  C CA  . ILE C  1 182 ? -21.532  59.526  -36.518  1.00 51.65  ? 182 ILE C CA  1 
ATOM   9930  C C   . ILE C  1 182 ? -21.851  58.104  -36.960  1.00 50.59  ? 182 ILE C C   1 
ATOM   9931  O O   . ILE C  1 182 ? -22.413  57.369  -36.175  1.00 51.05  ? 182 ILE C O   1 
ATOM   9932  C CB  . ILE C  1 182 ? -22.824  60.338  -36.343  1.00 53.57  ? 182 ILE C CB  1 
ATOM   9933  C CG1 . ILE C  1 182 ? -23.627  60.377  -37.653  1.00 52.62  ? 182 ILE C CG1 1 
ATOM   9934  C CG2 . ILE C  1 182 ? -22.491  61.735  -35.801  1.00 54.01  ? 182 ILE C CG2 1 
ATOM   9935  C CD1 . ILE C  1 182 ? -24.937  61.136  -37.562  1.00 53.31  ? 182 ILE C CD1 1 
ATOM   9936  N N   . PHE C  1 183 ? -21.537  57.749  -38.219  1.00 49.23  ? 183 PHE C N   1 
ATOM   9937  C CA  . PHE C  1 183 ? -21.863  56.446  -38.783  1.00 46.57  ? 183 PHE C CA  1 
ATOM   9938  C C   . PHE C  1 183 ? -20.639  55.528  -38.694  1.00 47.18  ? 183 PHE C C   1 
ATOM   9939  O O   . PHE C  1 183 ? -19.520  55.985  -38.487  1.00 48.10  ? 183 PHE C O   1 
ATOM   9940  C CB  . PHE C  1 183 ? -22.328  56.628  -40.232  1.00 43.34  ? 183 PHE C CB  1 
ATOM   9941  C CG  . PHE C  1 183 ? -23.561  57.494  -40.411  1.00 43.12  ? 183 PHE C CG  1 
ATOM   9942  C CD1 . PHE C  1 183 ? -24.827  57.011  -40.090  1.00 43.10  ? 183 PHE C CD1 1 
ATOM   9943  C CD2 . PHE C  1 183 ? -23.450  58.799  -40.896  1.00 42.39  ? 183 PHE C CD2 1 
ATOM   9944  C CE1 . PHE C  1 183 ? -25.944  57.827  -40.225  1.00 43.99  ? 183 PHE C CE1 1 
ATOM   9945  C CE2 . PHE C  1 183 ? -24.576  59.593  -41.059  1.00 41.96  ? 183 PHE C CE2 1 
ATOM   9946  C CZ  . PHE C  1 183 ? -25.817  59.113  -40.711  1.00 42.35  ? 183 PHE C CZ  1 
ATOM   9947  N N   . ASP C  1 184 ? -20.838  54.223  -38.897  1.00 46.97  ? 184 ASP C N   1 
ATOM   9948  C CA  . ASP C  1 184 ? -19.758  53.265  -38.709  1.00 45.18  ? 184 ASP C CA  1 
ATOM   9949  C C   . ASP C  1 184 ? -18.919  53.156  -39.975  1.00 42.71  ? 184 ASP C C   1 
ATOM   9950  O O   . ASP C  1 184 ? -17.752  52.769  -39.904  1.00 43.05  ? 184 ASP C O   1 
ATOM   9951  C CB  . ASP C  1 184 ? -20.286  51.909  -38.309  1.00 44.39  ? 184 ASP C CB  1 
ATOM   9952  C CG  . ASP C  1 184 ? -21.167  51.956  -37.081  1.00 46.81  ? 184 ASP C CG  1 
ATOM   9953  O OD1 . ASP C  1 184 ? -20.691  52.431  -36.036  1.00 48.73  ? 184 ASP C OD1 1 
ATOM   9954  O OD2 . ASP C  1 184 ? -22.323  51.520  -37.192  1.00 50.72  ? 184 ASP C OD2 1 
ATOM   9955  N N   . VAL C  1 185 ? -19.525  53.494  -41.118  1.00 40.21  ? 185 VAL C N   1 
ATOM   9956  C CA  . VAL C  1 185 ? -18.829  53.420  -42.389  1.00 38.94  ? 185 VAL C CA  1 
ATOM   9957  C C   . VAL C  1 185 ? -19.309  54.592  -43.230  1.00 38.03  ? 185 VAL C C   1 
ATOM   9958  O O   . VAL C  1 185 ? -20.436  55.049  -43.067  1.00 37.95  ? 185 VAL C O   1 
ATOM   9959  C CB  . VAL C  1 185 ? -18.989  52.081  -43.151  1.00 39.22  ? 185 VAL C CB  1 
ATOM   9960  C CG1 . VAL C  1 185 ? -19.384  50.913  -42.243  1.00 39.97  ? 185 VAL C CG1 1 
ATOM   9961  C CG2 . VAL C  1 185 ? -19.959  52.165  -44.308  1.00 38.83  ? 185 VAL C CG2 1 
ATOM   9962  N N   . TYR C  1 186 ? -18.412  55.081  -44.092  1.00 38.16  ? 186 TYR C N   1 
ATOM   9963  C CA  . TYR C  1 186 ? -18.681  56.200  -44.970  1.00 37.90  ? 186 TYR C CA  1 
ATOM   9964  C C   . TYR C  1 186 ? -19.344  55.653  -46.226  1.00 38.10  ? 186 TYR C C   1 
ATOM   9965  O O   . TYR C  1 186 ? -18.976  54.578  -46.683  1.00 38.84  ? 186 TYR C O   1 
ATOM   9966  C CB  . TYR C  1 186 ? -17.408  56.968  -45.333  1.00 37.21  ? 186 TYR C CB  1 
ATOM   9967  C CG  . TYR C  1 186 ? -16.697  57.582  -44.140  1.00 38.13  ? 186 TYR C CG  1 
ATOM   9968  C CD1 . TYR C  1 186 ? -17.387  58.360  -43.229  1.00 40.02  ? 186 TYR C CD1 1 
ATOM   9969  C CD2 . TYR C  1 186 ? -15.335  57.391  -43.936  1.00 37.92  ? 186 TYR C CD2 1 
ATOM   9970  C CE1 . TYR C  1 186 ? -16.753  58.925  -42.138  1.00 41.20  ? 186 TYR C CE1 1 
ATOM   9971  C CE2 . TYR C  1 186 ? -14.689  57.940  -42.843  1.00 39.14  ? 186 TYR C CE2 1 
ATOM   9972  C CZ  . TYR C  1 186 ? -15.408  58.695  -41.934  1.00 41.26  ? 186 TYR C CZ  1 
ATOM   9973  O OH  . TYR C  1 186 ? -14.800  59.215  -40.830  1.00 43.25  ? 186 TYR C OH  1 
ATOM   9974  N N   . ALA C  1 187 ? -20.310  56.404  -46.784  1.00 37.60  ? 187 ALA C N   1 
ATOM   9975  C CA  . ALA C  1 187 ? -21.001  55.979  -47.991  1.00 35.56  ? 187 ALA C CA  1 
ATOM   9976  C C   . ALA C  1 187 ? -21.496  57.189  -48.766  1.00 36.23  ? 187 ALA C C   1 
ATOM   9977  O O   . ALA C  1 187 ? -21.891  58.203  -48.185  1.00 38.49  ? 187 ALA C O   1 
ATOM   9978  C CB  . ALA C  1 187 ? -22.145  55.064  -47.661  1.00 34.17  ? 187 ALA C CB  1 
ATOM   9979  N N   . TYR C  1 188 ? -21.502  57.030  -50.088  1.00 34.62  ? 188 TYR C N   1 
ATOM   9980  C CA  . TYR C  1 188 ? -22.166  57.953  -50.980  1.00 33.98  ? 188 TYR C CA  1 
ATOM   9981  C C   . TYR C  1 188 ? -22.848  57.177  -52.099  1.00 32.84  ? 188 TYR C C   1 
ATOM   9982  O O   . TYR C  1 188 ? -22.385  56.103  -52.472  1.00 33.26  ? 188 TYR C O   1 
ATOM   9983  C CB  . TYR C  1 188 ? -21.132  58.927  -51.562  1.00 33.98  ? 188 TYR C CB  1 
ATOM   9984  C CG  . TYR C  1 188 ? -20.528  59.856  -50.518  1.00 36.32  ? 188 TYR C CG  1 
ATOM   9985  C CD1 . TYR C  1 188 ? -21.332  60.766  -49.841  1.00 36.64  ? 188 TYR C CD1 1 
ATOM   9986  C CD2 . TYR C  1 188 ? -19.167  59.833  -50.223  1.00 36.38  ? 188 TYR C CD2 1 
ATOM   9987  C CE1 . TYR C  1 188 ? -20.803  61.624  -48.896  1.00 38.62  ? 188 TYR C CE1 1 
ATOM   9988  C CE2 . TYR C  1 188 ? -18.636  60.668  -49.260  1.00 37.23  ? 188 TYR C CE2 1 
ATOM   9989  C CZ  . TYR C  1 188 ? -19.455  61.573  -48.612  1.00 37.65  ? 188 TYR C CZ  1 
ATOM   9990  O OH  . TYR C  1 188 ? -18.972  62.416  -47.664  1.00 39.63  ? 188 TYR C OH  1 
ATOM   9991  N N   . ASN C  1 189 ? -23.925  57.757  -52.637  1.00 33.01  ? 189 ASN C N   1 
ATOM   9992  C CA  . ASN C  1 189 ? -24.340  57.510  -54.008  1.00 33.27  ? 189 ASN C CA  1 
ATOM   9993  C C   . ASN C  1 189 ? -23.508  58.374  -54.953  1.00 31.77  ? 189 ASN C C   1 
ATOM   9994  O O   . ASN C  1 189 ? -23.429  59.586  -54.775  1.00 36.06  ? 189 ASN C O   1 
ATOM   9995  C CB  . ASN C  1 189 ? -25.828  57.772  -54.214  1.00 34.67  ? 189 ASN C CB  1 
ATOM   9996  C CG  . ASN C  1 189 ? -26.685  57.003  -53.238  1.00 35.63  ? 189 ASN C CG  1 
ATOM   9997  O OD1 . ASN C  1 189 ? -27.651  57.542  -52.680  1.00 37.42  ? 189 ASN C OD1 1 
ATOM   9998  N ND2 . ASN C  1 189 ? -26.322  55.761  -52.978  1.00 34.77  ? 189 ASN C ND2 1 
ATOM   9999  N N   . CYS C  1 190 ? -22.900  57.751  -55.967  1.00 30.03  ? 190 CYS C N   1 
ATOM   10000 C CA  . CYS C  1 190 ? -21.867  58.386  -56.764  1.00 30.63  ? 190 CYS C CA  1 
ATOM   10001 C C   . CYS C  1 190 ? -22.182  58.235  -58.243  1.00 29.26  ? 190 CYS C C   1 
ATOM   10002 O O   . CYS C  1 190 ? -22.251  57.112  -58.751  1.00 31.00  ? 190 CYS C O   1 
ATOM   10003 C CB  . CYS C  1 190 ? -20.501  57.752  -56.516  1.00 32.82  ? 190 CYS C CB  1 
ATOM   10004 S SG  . CYS C  1 190 ? -19.952  57.785  -54.792  1.00 34.48  ? 190 CYS C SG  1 
ATOM   10005 N N   . TYR C  1 191 ? -22.383  59.371  -58.907  1.00 28.30  ? 191 TYR C N   1 
ATOM   10006 C CA  . TYR C  1 191 ? -22.690  59.436  -60.320  1.00 28.16  ? 191 TYR C CA  1 
ATOM   10007 C C   . TYR C  1 191 ? -21.652  60.296  -61.022  1.00 29.12  ? 191 TYR C C   1 
ATOM   10008 O O   . TYR C  1 191 ? -21.253  61.353  -60.535  1.00 30.23  ? 191 TYR C O   1 
ATOM   10009 C CB  . TYR C  1 191 ? -24.112  59.969  -60.500  1.00 28.80  ? 191 TYR C CB  1 
ATOM   10010 C CG  . TYR C  1 191 ? -25.118  58.916  -60.071  1.00 27.92  ? 191 TYR C CG  1 
ATOM   10011 C CD1 . TYR C  1 191 ? -25.427  57.881  -60.940  1.00 29.88  ? 191 TYR C CD1 1 
ATOM   10012 C CD2 . TYR C  1 191 ? -25.629  58.854  -58.788  1.00 26.99  ? 191 TYR C CD2 1 
ATOM   10013 C CE1 . TYR C  1 191 ? -26.281  56.852  -60.590  1.00 28.59  ? 191 TYR C CE1 1 
ATOM   10014 C CE2 . TYR C  1 191 ? -26.481  57.828  -58.419  1.00 28.47  ? 191 TYR C CE2 1 
ATOM   10015 C CZ  . TYR C  1 191 ? -26.819  56.837  -59.329  1.00 28.92  ? 191 TYR C CZ  1 
ATOM   10016 O OH  . TYR C  1 191 ? -27.656  55.801  -59.066  1.00 31.80  ? 191 TYR C OH  1 
ATOM   10017 N N   . ASP C  1 192 ? -21.202  59.783  -62.163  1.00 29.84  ? 192 ASP C N   1 
ATOM   10018 C CA  . ASP C  1 192 ? -20.284  60.495  -63.026  1.00 30.73  ? 192 ASP C CA  1 
ATOM   10019 C C   . ASP C  1 192 ? -21.026  60.991  -64.258  1.00 29.28  ? 192 ASP C C   1 
ATOM   10020 O O   . ASP C  1 192 ? -21.194  60.257  -65.209  1.00 28.41  ? 192 ASP C O   1 
ATOM   10021 C CB  . ASP C  1 192 ? -19.123  59.610  -63.429  1.00 29.95  ? 192 ASP C CB  1 
ATOM   10022 C CG  . ASP C  1 192 ? -18.083  60.338  -64.241  1.00 29.74  ? 192 ASP C CG  1 
ATOM   10023 O OD1 . ASP C  1 192 ? -18.218  61.564  -64.420  1.00 30.05  ? 192 ASP C OD1 1 
ATOM   10024 O OD2 . ASP C  1 192 ? -17.172  59.662  -64.700  1.00 33.69  ? 192 ASP C OD2 1 
ATOM   10025 N N   . HIS C  1 193 ? -21.438  62.255  -64.213  1.00 31.18  ? 193 HIS C N   1 
ATOM   10026 C CA  . HIS C  1 193 ? -22.132  62.926  -65.302  1.00 31.03  ? 193 HIS C CA  1 
ATOM   10027 C C   . HIS C  1 193 ? -21.254  64.035  -65.889  1.00 29.33  ? 193 HIS C C   1 
ATOM   10028 O O   . HIS C  1 193 ? -21.703  64.829  -66.701  1.00 26.53  ? 193 HIS C O   1 
ATOM   10029 C CB  . HIS C  1 193 ? -23.430  63.554  -64.776  1.00 31.03  ? 193 HIS C CB  1 
ATOM   10030 C CG  . HIS C  1 193 ? -24.433  62.579  -64.263  1.00 31.89  ? 193 HIS C CG  1 
ATOM   10031 N ND1 . HIS C  1 193 ? -24.769  61.410  -64.915  1.00 31.50  ? 193 HIS C ND1 1 
ATOM   10032 C CD2 . HIS C  1 193 ? -25.206  62.608  -63.163  1.00 33.52  ? 193 HIS C CD2 1 
ATOM   10033 C CE1 . HIS C  1 193 ? -25.736  60.797  -64.252  1.00 29.65  ? 193 HIS C CE1 1 
ATOM   10034 N NE2 . HIS C  1 193 ? -25.995  61.477  -63.172  1.00 31.53  ? 193 HIS C NE2 1 
ATOM   10035 N N   . ASN C  1 194 ? -20.020  64.112  -65.408  1.00 29.77  ? 194 ASN C N   1 
ATOM   10036 C CA  . ASN C  1 194 ? -19.060  65.083  -65.904  1.00 30.78  ? 194 ASN C CA  1 
ATOM   10037 C C   . ASN C  1 194 ? -19.614  66.515  -65.834  1.00 28.53  ? 194 ASN C C   1 
ATOM   10038 O O   . ASN C  1 194 ? -19.573  67.255  -66.801  1.00 26.21  ? 194 ASN C O   1 
ATOM   10039 C CB  . ASN C  1 194 ? -18.631  64.678  -67.305  1.00 29.99  ? 194 ASN C CB  1 
ATOM   10040 C CG  . ASN C  1 194 ? -17.564  65.595  -67.842  1.00 32.81  ? 194 ASN C CG  1 
ATOM   10041 O OD1 . ASN C  1 194 ? -16.863  66.319  -67.108  1.00 32.29  ? 194 ASN C OD1 1 
ATOM   10042 N ND2 . ASN C  1 194 ? -17.443  65.564  -69.155  1.00 35.23  ? 194 ASN C ND2 1 
ATOM   10043 N N   . GLU C  1 195 ? -20.129  66.898  -64.670  1.00 29.44  ? 195 GLU C N   1 
ATOM   10044 C CA  . GLU C  1 195 ? -20.683  68.227  -64.470  1.00 30.02  ? 195 GLU C CA  1 
ATOM   10045 C C   . GLU C  1 195 ? -20.406  68.648  -63.031  1.00 29.38  ? 195 GLU C C   1 
ATOM   10046 O O   . GLU C  1 195 ? -20.221  67.807  -62.148  1.00 27.50  ? 195 GLU C O   1 
ATOM   10047 C CB  . GLU C  1 195 ? -22.182  68.199  -64.824  1.00 29.04  ? 195 GLU C CB  1 
ATOM   10048 C CG  . GLU C  1 195 ? -23.012  67.388  -63.844  1.00 28.48  ? 195 GLU C CG  1 
ATOM   10049 C CD  . GLU C  1 195 ? -24.476  67.206  -64.180  1.00 29.35  ? 195 GLU C CD  1 
ATOM   10050 O OE1 . GLU C  1 195 ? -24.817  67.960  -65.094  1.00 30.78  ? 195 GLU C OE1 1 
ATOM   10051 O OE2 . GLU C  1 195 ? -25.246  66.403  -63.552  1.00 28.47  ? 195 GLU C OE2 1 
ATOM   10052 N N   . GLY C  1 196 ? -20.440  69.962  -62.789  1.00 30.04  ? 196 GLY C N   1 
ATOM   10053 C CA  . GLY C  1 196 ? -20.123  70.475  -61.470  1.00 30.28  ? 196 GLY C CA  1 
ATOM   10054 C C   . GLY C  1 196 ? -18.833  69.836  -60.931  1.00 29.95  ? 196 GLY C C   1 
ATOM   10055 O O   . GLY C  1 196 ? -17.794  69.866  -61.573  1.00 30.14  ? 196 GLY C O   1 
ATOM   10056 N N   . GLN C  1 197 ? -18.897  69.297  -59.719  1.00 29.53  ? 197 GLN C N   1 
ATOM   10057 C CA  . GLN C  1 197 ? -17.764  68.701  -59.039  1.00 29.05  ? 197 GLN C CA  1 
ATOM   10058 C C   . GLN C  1 197 ? -17.101  67.590  -59.866  1.00 29.65  ? 197 GLN C C   1 
ATOM   10059 O O   . GLN C  1 197 ? -15.895  67.404  -59.743  1.00 28.89  ? 197 GLN C O   1 
ATOM   10060 C CB  . GLN C  1 197 ? -18.271  68.062  -57.743  1.00 29.33  ? 197 GLN C CB  1 
ATOM   10061 C CG  . GLN C  1 197 ? -18.822  69.027  -56.703  1.00 30.58  ? 197 GLN C CG  1 
ATOM   10062 C CD  . GLN C  1 197 ? -20.326  69.112  -56.707  1.00 31.23  ? 197 GLN C CD  1 
ATOM   10063 O OE1 . GLN C  1 197 ? -20.945  69.269  -57.760  1.00 31.10  ? 197 GLN C OE1 1 
ATOM   10064 N NE2 . GLN C  1 197 ? -20.935  68.971  -55.540  1.00 32.59  ? 197 GLN C NE2 1 
ATOM   10065 N N   . THR C  1 198 ? -17.878  66.792  -60.642  1.00 28.71  ? 198 THR C N   1 
ATOM   10066 C CA  . THR C  1 198 ? -17.276  65.740  -61.446  1.00 28.34  ? 198 THR C CA  1 
ATOM   10067 C C   . THR C  1 198 ? -16.665  66.307  -62.733  1.00 28.91  ? 198 THR C C   1 
ATOM   10068 O O   . THR C  1 198 ? -15.863  65.581  -63.332  1.00 28.49  ? 198 THR C O   1 
ATOM   10069 C CB  . THR C  1 198 ? -18.205  64.549  -61.729  1.00 27.81  ? 198 THR C CB  1 
ATOM   10070 O OG1 . THR C  1 198 ? -19.323  64.984  -62.505  1.00 27.75  ? 198 THR C OG1 1 
ATOM   10071 C CG2 . THR C  1 198 ? -18.607  63.804  -60.463  1.00 27.01  ? 198 THR C CG2 1 
ATOM   10072 N N   . ALA C  1 199 ? -16.979  67.571  -63.122  1.00 28.78  ? 199 ALA C N   1 
ATOM   10073 C CA  . ALA C  1 199 ? -16.342  68.235  -64.267  1.00 29.37  ? 199 ALA C CA  1 
ATOM   10074 C C   . ALA C  1 199 ? -15.016  68.869  -63.863  1.00 30.69  ? 199 ALA C C   1 
ATOM   10075 O O   . ALA C  1 199 ? -14.071  68.895  -64.648  1.00 32.44  ? 199 ALA C O   1 
ATOM   10076 C CB  . ALA C  1 199 ? -17.198  69.314  -64.885  1.00 29.08  ? 199 ALA C CB  1 
ATOM   10077 N N   . THR C  1 200 ? -14.911  69.314  -62.619  1.00 31.81  ? 200 THR C N   1 
ATOM   10078 C CA  . THR C  1 200 ? -13.708  70.033  -62.157  1.00 34.02  ? 200 THR C CA  1 
ATOM   10079 C C   . THR C  1 200 ? -12.646  69.085  -61.652  1.00 35.59  ? 200 THR C C   1 
ATOM   10080 O O   . THR C  1 200 ? -11.491  69.240  -62.054  1.00 35.21  ? 200 THR C O   1 
ATOM   10081 C CB  . THR C  1 200 ? -14.136  71.023  -61.075  1.00 33.53  ? 200 THR C CB  1 
ATOM   10082 O OG1 . THR C  1 200 ? -14.836  70.266  -60.097  1.00 31.33  ? 200 THR C OG1 1 
ATOM   10083 C CG2 . THR C  1 200 ? -15.010  72.132  -61.631  1.00 33.96  ? 200 THR C CG2 1 
ATOM   10084 N N   . MET C  1 201 ? -13.019  68.123  -60.813  1.00 35.12  ? 201 MET C N   1 
ATOM   10085 C CA  . MET C  1 201 ? -12.003  67.263  -60.164  1.00 35.48  ? 201 MET C CA  1 
ATOM   10086 C C   . MET C  1 201 ? -11.927  65.879  -60.816  1.00 34.88  ? 201 MET C C   1 
ATOM   10087 O O   . MET C  1 201 ? -10.926  65.193  -60.606  1.00 33.31  ? 201 MET C O   1 
ATOM   10088 C CB  . MET C  1 201 ? -12.358  67.115  -58.685  1.00 35.85  ? 201 MET C CB  1 
ATOM   10089 C CG  . MET C  1 201 ? -12.517  68.426  -57.950  1.00 33.99  ? 201 MET C CG  1 
ATOM   10090 S SD  . MET C  1 201 ? -13.294  68.235  -56.336  1.00 32.42  ? 201 MET C SD  1 
ATOM   10091 C CE  . MET C  1 201 ? -14.841  69.071  -56.696  1.00 33.01  ? 201 MET C CE  1 
ATOM   10092 N N   . GLY C  1 202 ? -12.927  65.521  -61.614  1.00 35.65  ? 202 GLY C N   1 
ATOM   10093 C CA  . GLY C  1 202 ? -13.001  64.157  -62.158  1.00 34.64  ? 202 GLY C CA  1 
ATOM   10094 C C   . GLY C  1 202 ? -13.742  63.280  -61.177  1.00 33.43  ? 202 GLY C C   1 
ATOM   10095 O O   . GLY C  1 202 ? -13.834  63.664  -60.006  1.00 35.51  ? 202 GLY C O   1 
ATOM   10096 N N   . PHE C  1 203 ? -14.269  62.150  -61.632  1.00 32.70  ? 203 PHE C N   1 
ATOM   10097 C CA  . PHE C  1 203 ? -15.063  61.314  -60.744  1.00 30.68  ? 203 PHE C CA  1 
ATOM   10098 C C   . PHE C  1 203 ? -14.168  60.786  -59.632  1.00 30.17  ? 203 PHE C C   1 
ATOM   10099 O O   . PHE C  1 203 ? -14.472  60.972  -58.469  1.00 31.69  ? 203 PHE C O   1 
ATOM   10100 C CB  . PHE C  1 203 ? -15.699  60.163  -61.534  1.00 30.71  ? 203 PHE C CB  1 
ATOM   10101 C CG  . PHE C  1 203 ? -16.808  59.368  -60.849  1.00 28.97  ? 203 PHE C CG  1 
ATOM   10102 C CD1 . PHE C  1 203 ? -17.791  59.991  -60.091  1.00 29.29  ? 203 PHE C CD1 1 
ATOM   10103 C CD2 . PHE C  1 203 ? -16.902  57.991  -61.042  1.00 29.46  ? 203 PHE C CD2 1 
ATOM   10104 C CE1 . PHE C  1 203 ? -18.808  59.246  -59.514  1.00 30.33  ? 203 PHE C CE1 1 
ATOM   10105 C CE2 . PHE C  1 203 ? -17.918  57.251  -60.458  1.00 28.18  ? 203 PHE C CE2 1 
ATOM   10106 C CZ  . PHE C  1 203 ? -18.860  57.875  -59.694  1.00 29.56  ? 203 PHE C CZ  1 
ATOM   10107 N N   . LYS C  1 204 ? -13.038  60.172  -59.991  1.00 29.96  ? 204 LYS C N   1 
ATOM   10108 C CA  . LYS C  1 204 ? -12.208  59.532  -58.976  1.00 31.19  ? 204 LYS C CA  1 
ATOM   10109 C C   . LYS C  1 204 ? -11.775  60.555  -57.932  1.00 30.63  ? 204 LYS C C   1 
ATOM   10110 O O   . LYS C  1 204 ? -11.876  60.297  -56.740  1.00 30.66  ? 204 LYS C O   1 
ATOM   10111 C CB  . LYS C  1 204 ? -10.973  58.806  -59.525  1.00 29.00  ? 204 LYS C CB  1 
ATOM   10112 C CG  . LYS C  1 204 ? -9.853   58.630  -58.528  1.00 29.04  ? 204 LYS C CG  1 
ATOM   10113 C CD  . LYS C  1 204 ? -8.513   58.238  -59.158  1.00 29.80  ? 204 LYS C CD  1 
ATOM   10114 C CE  . LYS C  1 204 ? -7.392   58.190  -58.157  1.00 31.11  ? 204 LYS C CE  1 
ATOM   10115 N NZ  . LYS C  1 204 ? -6.102   58.223  -58.843  1.00 32.36  ? 204 LYS C NZ  1 
ATOM   10116 N N   . ASP C  1 205 ? -11.237  61.688  -58.365  1.00 31.41  ? 205 ASP C N   1 
ATOM   10117 C CA  . ASP C  1 205 ? -10.654  62.614  -57.405  1.00 32.79  ? 205 ASP C CA  1 
ATOM   10118 C C   . ASP C  1 205 ? -11.751  63.309  -56.601  1.00 34.38  ? 205 ASP C C   1 
ATOM   10119 O O   . ASP C  1 205 ? -11.530  63.693  -55.457  1.00 36.27  ? 205 ASP C O   1 
ATOM   10120 C CB  . ASP C  1 205 ? -9.735   63.634  -58.062  1.00 33.85  ? 205 ASP C CB  1 
ATOM   10121 C CG  . ASP C  1 205 ? -8.400   63.124  -58.581  1.00 33.48  ? 205 ASP C CG  1 
ATOM   10122 O OD1 . ASP C  1 205 ? -8.111   61.905  -58.454  1.00 34.50  ? 205 ASP C OD1 1 
ATOM   10123 O OD2 . ASP C  1 205 ? -7.684   63.947  -59.139  1.00 33.58  ? 205 ASP C OD2 1 
ATOM   10124 N N   . TYR C  1 206 ? -12.946  63.469  -57.174  1.00 34.77  ? 206 TYR C N   1 
ATOM   10125 C CA  . TYR C  1 206 ? -14.025  64.081  -56.406  1.00 37.07  ? 206 TYR C CA  1 
ATOM   10126 C C   . TYR C  1 206 ? -14.341  63.217  -55.183  1.00 36.02  ? 206 TYR C C   1 
ATOM   10127 O O   . TYR C  1 206 ? -14.315  63.694  -54.055  1.00 37.40  ? 206 TYR C O   1 
ATOM   10128 C CB  . TYR C  1 206 ? -15.333  64.283  -57.189  1.00 35.14  ? 206 TYR C CB  1 
ATOM   10129 C CG  . TYR C  1 206 ? -16.467  64.882  -56.361  1.00 34.43  ? 206 TYR C CG  1 
ATOM   10130 C CD1 . TYR C  1 206 ? -16.259  65.989  -55.537  1.00 36.12  ? 206 TYR C CD1 1 
ATOM   10131 C CD2 . TYR C  1 206 ? -17.742  64.341  -56.401  1.00 33.51  ? 206 TYR C CD2 1 
ATOM   10132 C CE1 . TYR C  1 206 ? -17.291  66.545  -54.798  1.00 36.46  ? 206 TYR C CE1 1 
ATOM   10133 C CE2 . TYR C  1 206 ? -18.787  64.897  -55.684  1.00 35.14  ? 206 TYR C CE2 1 
ATOM   10134 C CZ  . TYR C  1 206 ? -18.557  65.997  -54.876  1.00 36.61  ? 206 TYR C CZ  1 
ATOM   10135 O OH  . TYR C  1 206 ? -19.562  66.524  -54.132  1.00 37.51  ? 206 TYR C OH  1 
ATOM   10136 N N   . ILE C  1 207 ? -14.664  61.947  -55.426  1.00 34.17  ? 207 ILE C N   1 
ATOM   10137 C CA  . ILE C  1 207 ? -15.014  61.025  -54.349  1.00 35.55  ? 207 ILE C CA  1 
ATOM   10138 C C   . ILE C  1 207 ? -13.819  60.765  -53.417  1.00 34.77  ? 207 ILE C C   1 
ATOM   10139 O O   . ILE C  1 207 ? -13.982  60.690  -52.193  1.00 37.54  ? 207 ILE C O   1 
ATOM   10140 C CB  . ILE C  1 207 ? -15.605  59.729  -54.935  1.00 34.94  ? 207 ILE C CB  1 
ATOM   10141 C CG1 . ILE C  1 207 ? -16.826  60.009  -55.804  1.00 35.88  ? 207 ILE C CG1 1 
ATOM   10142 C CG2 . ILE C  1 207 ? -15.944  58.749  -53.819  1.00 37.13  ? 207 ILE C CG2 1 
ATOM   10143 C CD1 . ILE C  1 207 ? -17.928  60.787  -55.099  1.00 35.72  ? 207 ILE C CD1 1 
ATOM   10144 N N   . LYS C  1 208 ? -12.618  60.623  -53.981  1.00 32.97  ? 208 LYS C N   1 
ATOM   10145 C CA  . LYS C  1 208 ? -11.432  60.447  -53.165  1.00 34.65  ? 208 LYS C CA  1 
ATOM   10146 C C   . LYS C  1 208 ? -11.228  61.626  -52.211  1.00 33.90  ? 208 LYS C C   1 
ATOM   10147 O O   . LYS C  1 208 ? -10.791  61.437  -51.061  1.00 33.02  ? 208 LYS C O   1 
ATOM   10148 C CB  . LYS C  1 208 ? -10.216  60.256  -54.066  1.00 37.61  ? 208 LYS C CB  1 
ATOM   10149 C CG  . LYS C  1 208 ? -8.943   60.017  -53.280  1.00 42.21  ? 208 LYS C CG  1 
ATOM   10150 C CD  . LYS C  1 208 ? -7.794   59.500  -54.134  1.00 47.58  ? 208 LYS C CD  1 
ATOM   10151 C CE  . LYS C  1 208 ? -7.157   60.612  -54.896  1.00 52.46  ? 208 LYS C CE  1 
ATOM   10152 N NZ  . LYS C  1 208 ? -6.361   61.444  -53.992  1.00 56.14  ? 208 LYS C NZ  1 
ATOM   10153 N N   . GLY C  1 209 ? -11.539  62.848  -52.681  1.00 33.09  ? 209 GLY C N   1 
ATOM   10154 C CA  . GLY C  1 209 ? -11.385  64.050  -51.856  1.00 33.71  ? 209 GLY C CA  1 
ATOM   10155 C C   . GLY C  1 209 ? -12.396  64.116  -50.706  1.00 35.04  ? 209 GLY C C   1 
ATOM   10156 O O   . GLY C  1 209 ? -12.078  64.614  -49.643  1.00 34.90  ? 209 GLY C O   1 
ATOM   10157 N N   . LEU C  1 210 ? -13.609  63.573  -50.883  1.00 36.37  ? 210 LEU C N   1 
ATOM   10158 C CA  . LEU C  1 210 ? -14.564  63.494  -49.788  1.00 37.83  ? 210 LEU C CA  1 
ATOM   10159 C C   . LEU C  1 210 ? -14.045  62.518  -48.734  1.00 38.82  ? 210 LEU C C   1 
ATOM   10160 O O   . LEU C  1 210 ? -14.196  62.725  -47.536  1.00 40.29  ? 210 LEU C O   1 
ATOM   10161 C CB  . LEU C  1 210 ? -15.939  63.055  -50.300  1.00 38.04  ? 210 LEU C CB  1 
ATOM   10162 C CG  . LEU C  1 210 ? -16.655  64.017  -51.264  1.00 37.53  ? 210 LEU C CG  1 
ATOM   10163 C CD1 . LEU C  1 210 ? -18.061  63.558  -51.663  1.00 35.61  ? 210 LEU C CD1 1 
ATOM   10164 C CD2 . LEU C  1 210 ? -16.736  65.430  -50.664  1.00 39.10  ? 210 LEU C CD2 1 
ATOM   10165 N N   . ASN C  1 211 ? -13.454  61.422  -49.194  1.00 38.94  ? 211 ASN C N   1 
ATOM   10166 C CA  . ASN C  1 211 ? -12.993  60.347  -48.322  1.00 39.11  ? 211 ASN C CA  1 
ATOM   10167 C C   . ASN C  1 211 ? -11.824  60.880  -47.474  1.00 42.83  ? 211 ASN C C   1 
ATOM   10168 O O   . ASN C  1 211 ? -11.737  60.653  -46.264  1.00 43.18  ? 211 ASN C O   1 
ATOM   10169 C CB  . ASN C  1 211 ? -12.727  59.111  -49.195  1.00 37.56  ? 211 ASN C CB  1 
ATOM   10170 C CG  . ASN C  1 211 ? -12.465  57.841  -48.418  1.00 36.48  ? 211 ASN C CG  1 
ATOM   10171 O OD1 . ASN C  1 211 ? -13.108  57.593  -47.398  1.00 36.25  ? 211 ASN C OD1 1 
ATOM   10172 N ND2 . ASN C  1 211 ? -11.543  57.017  -48.889  1.00 37.70  ? 211 ASN C ND2 1 
ATOM   10173 N N   . GLU C  1 212 ? -10.937  61.660  -48.100  1.00 44.26  ? 212 GLU C N   1 
ATOM   10174 C CA  . GLU C  1 212 ? -9.870   62.343  -47.375  1.00 44.74  ? 212 GLU C CA  1 
ATOM   10175 C C   . GLU C  1 212 ? -10.434  63.273  -46.299  1.00 46.01  ? 212 GLU C C   1 
ATOM   10176 O O   . GLU C  1 212 ? -9.974   63.280  -45.147  1.00 45.78  ? 212 GLU C O   1 
ATOM   10177 C CB  . GLU C  1 212 ? -9.003   63.098  -48.386  1.00 44.73  ? 212 GLU C CB  1 
ATOM   10178 C CG  . GLU C  1 212 ? -8.030   62.179  -49.118  1.00 44.51  ? 212 GLU C CG  1 
ATOM   10179 C CD  . GLU C  1 212 ? -7.452   62.721  -50.389  1.00 45.22  ? 212 GLU C CD  1 
ATOM   10180 O OE1 . GLU C  1 212 ? -7.794   63.855  -50.742  1.00 49.02  ? 212 GLU C OE1 1 
ATOM   10181 O OE2 . GLU C  1 212 ? -6.697   61.972  -51.034  1.00 47.86  ? 212 GLU C OE2 1 
ATOM   10182 N N   . LEU C  1 213 ? -11.453  64.048  -46.682  1.00 46.11  ? 213 LEU C N   1 
ATOM   10183 C CA  . LEU C  1 213 ? -12.080  64.980  -45.760  1.00 48.26  ? 213 LEU C CA  1 
ATOM   10184 C C   . LEU C  1 213 ? -12.758  64.202  -44.632  1.00 46.74  ? 213 LEU C C   1 
ATOM   10185 O O   . LEU C  1 213 ? -12.654  64.584  -43.475  1.00 49.31  ? 213 LEU C O   1 
ATOM   10186 C CB  . LEU C  1 213 ? -13.032  65.912  -46.522  1.00 51.79  ? 213 LEU C CB  1 
ATOM   10187 C CG  . LEU C  1 213 ? -12.375  66.965  -47.437  1.00 52.82  ? 213 LEU C CG  1 
ATOM   10188 C CD1 . LEU C  1 213 ? -13.412  67.732  -48.241  1.00 51.62  ? 213 LEU C CD1 1 
ATOM   10189 C CD2 . LEU C  1 213 ? -11.491  67.955  -46.679  1.00 52.19  ? 213 LEU C CD2 1 
ATOM   10190 N N   . ASN C  1 214 ? -13.378  63.056  -44.947  1.00 45.56  ? 214 ASN C N   1 
ATOM   10191 C CA  . ASN C  1 214 ? -13.983  62.204  -43.924  1.00 43.02  ? 214 ASN C CA  1 
ATOM   10192 C C   . ASN C  1 214 ? -12.943  61.707  -42.914  1.00 42.36  ? 214 ASN C C   1 
ATOM   10193 O O   . ASN C  1 214 ? -13.306  61.413  -41.781  1.00 41.84  ? 214 ASN C O   1 
ATOM   10194 C CB  . ASN C  1 214 ? -14.839  61.112  -44.563  1.00 41.35  ? 214 ASN C CB  1 
ATOM   10195 C CG  . ASN C  1 214 ? -16.108  61.668  -45.174  1.00 40.44  ? 214 ASN C CG  1 
ATOM   10196 O OD1 . ASN C  1 214 ? -16.507  62.792  -44.855  1.00 39.61  ? 214 ASN C OD1 1 
ATOM   10197 N ND2 . ASN C  1 214 ? -16.772  60.911  -46.034  1.00 39.56  ? 214 ASN C ND2 1 
ATOM   10198 N N   . GLY C  1 215 ? -11.654  61.628  -43.296  1.00 43.13  ? 215 GLY C N   1 
ATOM   10199 C CA  . GLY C  1 215 ? -10.583  61.274  -42.369  1.00 43.25  ? 215 GLY C CA  1 
ATOM   10200 C C   . GLY C  1 215 ? -9.955   59.893  -42.611  1.00 43.33  ? 215 GLY C C   1 
ATOM   10201 O O   . GLY C  1 215 ? -9.088   59.487  -41.849  1.00 44.87  ? 215 GLY C O   1 
ATOM   10202 N N   . LEU C  1 216 ? -10.348  59.165  -43.660  1.00 41.44  ? 216 LEU C N   1 
ATOM   10203 C CA  . LEU C  1 216 ? -9.709   57.897  -44.008  1.00 42.88  ? 216 LEU C CA  1 
ATOM   10204 C C   . LEU C  1 216 ? -9.576   57.007  -42.780  1.00 42.65  ? 216 LEU C C   1 
ATOM   10205 O O   . LEU C  1 216 ? -8.558   56.338  -42.596  1.00 41.81  ? 216 LEU C O   1 
ATOM   10206 C CB  . LEU C  1 216 ? -8.318   58.104  -44.596  1.00 45.12  ? 216 LEU C CB  1 
ATOM   10207 C CG  . LEU C  1 216 ? -8.249   58.844  -45.928  1.00 46.68  ? 216 LEU C CG  1 
ATOM   10208 C CD1 . LEU C  1 216 ? -6.778   58.949  -46.313  1.00 46.22  ? 216 LEU C CD1 1 
ATOM   10209 C CD2 . LEU C  1 216 ? -9.094   58.103  -46.968  1.00 45.80  ? 216 LEU C CD2 1 
ATOM   10210 N N   . ASP C  1 217 ? -10.599  57.028  -41.939  1.00 42.35  ? 217 ASP C N   1 
ATOM   10211 C CA  . ASP C  1 217 ? -10.524  56.343  -40.674  1.00 44.53  ? 217 ASP C CA  1 
ATOM   10212 C C   . ASP C  1 217 ? -11.577  55.237  -40.621  1.00 46.42  ? 217 ASP C C   1 
ATOM   10213 O O   . ASP C  1 217 ? -11.594  54.502  -39.646  1.00 47.35  ? 217 ASP C O   1 
ATOM   10214 C CB  . ASP C  1 217 ? -10.601  57.333  -39.526  1.00 45.17  ? 217 ASP C CB  1 
ATOM   10215 C CG  . ASP C  1 217 ? -11.826  58.230  -39.494  1.00 46.13  ? 217 ASP C CG  1 
ATOM   10216 O OD1 . ASP C  1 217 ? -12.485  58.378  -40.529  1.00 44.78  ? 217 ASP C OD1 1 
ATOM   10217 O OD2 . ASP C  1 217 ? -12.106  58.790  -38.424  1.00 51.23  ? 217 ASP C OD2 1 
ATOM   10218 N N   . LYS C  1 218 ? -12.416  55.101  -41.663  1.00 46.24  ? 218 LYS C N   1 
ATOM   10219 C CA  . LYS C  1 218 ? -13.473  54.097  -41.695  1.00 46.16  ? 218 LYS C CA  1 
ATOM   10220 C C   . LYS C  1 218 ? -13.601  53.502  -43.092  1.00 43.18  ? 218 LYS C C   1 
ATOM   10221 O O   . LYS C  1 218 ? -13.263  54.140  -44.076  1.00 41.88  ? 218 LYS C O   1 
ATOM   10222 C CB  . LYS C  1 218 ? -14.851  54.685  -41.373  1.00 48.48  ? 218 LYS C CB  1 
ATOM   10223 C CG  . LYS C  1 218 ? -14.962  55.285  -40.011  1.00 52.25  ? 218 LYS C CG  1 
ATOM   10224 C CD  . LYS C  1 218 ? -16.286  55.984  -39.709  1.00 57.03  ? 218 LYS C CD  1 
ATOM   10225 C CE  . LYS C  1 218 ? -16.331  56.374  -38.229  1.00 58.10  ? 218 LYS C CE  1 
ATOM   10226 N NZ  . LYS C  1 218 ? -17.286  57.453  -38.004  1.00 56.87  ? 218 LYS C NZ  1 
ATOM   10227 N N   . PRO C  1 219 ? -14.145  52.272  -43.239  1.00 43.67  ? 219 PRO C N   1 
ATOM   10228 C CA  . PRO C  1 219 ? -14.392  51.721  -44.565  1.00 41.06  ? 219 PRO C CA  1 
ATOM   10229 C C   . PRO C  1 219 ? -15.312  52.664  -45.318  1.00 37.73  ? 219 PRO C C   1 
ATOM   10230 O O   . PRO C  1 219 ? -16.232  53.208  -44.729  1.00 35.60  ? 219 PRO C O   1 
ATOM   10231 C CB  . PRO C  1 219 ? -15.023  50.347  -44.321  1.00 41.13  ? 219 PRO C CB  1 
ATOM   10232 C CG  . PRO C  1 219 ? -14.607  50.011  -42.898  1.00 42.86  ? 219 PRO C CG  1 
ATOM   10233 C CD  . PRO C  1 219 ? -14.529  51.336  -42.164  1.00 44.56  ? 219 PRO C CD  1 
ATOM   10234 N N   . PHE C  1 220 ? -15.044  52.806  -46.618  1.00 36.65  ? 220 PHE C N   1 
ATOM   10235 C CA  . PHE C  1 220 ? -15.894  53.566  -47.528  1.00 37.91  ? 220 PHE C CA  1 
ATOM   10236 C C   . PHE C  1 220 ? -16.489  52.621  -48.585  1.00 35.36  ? 220 PHE C C   1 
ATOM   10237 O O   . PHE C  1 220 ? -15.764  51.827  -49.186  1.00 34.57  ? 220 PHE C O   1 
ATOM   10238 C CB  . PHE C  1 220 ? -15.087  54.710  -48.168  1.00 36.02  ? 220 PHE C CB  1 
ATOM   10239 C CG  . PHE C  1 220 ? -15.748  55.333  -49.387  1.00 35.87  ? 220 PHE C CG  1 
ATOM   10240 C CD1 . PHE C  1 220 ? -17.028  55.875  -49.307  1.00 35.03  ? 220 PHE C CD1 1 
ATOM   10241 C CD2 . PHE C  1 220 ? -15.111  55.322  -50.630  1.00 36.15  ? 220 PHE C CD2 1 
ATOM   10242 C CE1 . PHE C  1 220 ? -17.635  56.428  -50.424  1.00 34.28  ? 220 PHE C CE1 1 
ATOM   10243 C CE2 . PHE C  1 220 ? -15.741  55.842  -51.758  1.00 34.29  ? 220 PHE C CE2 1 
ATOM   10244 C CZ  . PHE C  1 220 ? -17.006  56.392  -51.647  1.00 34.60  ? 220 PHE C CZ  1 
ATOM   10245 N N   . ILE C  1 221 ? -17.807  52.753  -48.810  1.00 35.72  ? 221 ILE C N   1 
ATOM   10246 C CA  . ILE C  1 221 ? -18.560  51.982  -49.802  1.00 35.59  ? 221 ILE C CA  1 
ATOM   10247 C C   . ILE C  1 221 ? -19.406  52.941  -50.647  1.00 34.75  ? 221 ILE C C   1 
ATOM   10248 O O   . ILE C  1 221 ? -19.695  54.066  -50.210  1.00 33.83  ? 221 ILE C O   1 
ATOM   10249 C CB  . ILE C  1 221 ? -19.454  50.905  -49.138  1.00 34.37  ? 221 ILE C CB  1 
ATOM   10250 C CG1 . ILE C  1 221 ? -20.652  51.540  -48.421  1.00 35.72  ? 221 ILE C CG1 1 
ATOM   10251 C CG2 . ILE C  1 221 ? -18.641  50.000  -48.220  1.00 33.82  ? 221 ILE C CG2 1 
ATOM   10252 C CD1 . ILE C  1 221 ? -21.589  50.561  -47.747  1.00 37.21  ? 221 ILE C CD1 1 
ATOM   10253 N N   . THR C  1 222 ? -19.770  52.482  -51.860  1.00 34.21  ? 222 THR C N   1 
ATOM   10254 C CA  . THR C  1 222 ? -20.724  53.185  -52.714  1.00 35.37  ? 222 THR C CA  1 
ATOM   10255 C C   . THR C  1 222 ? -22.068  52.478  -52.653  1.00 36.08  ? 222 THR C C   1 
ATOM   10256 O O   . THR C  1 222 ? -22.128  51.250  -52.729  1.00 34.91  ? 222 THR C O   1 
ATOM   10257 C CB  . THR C  1 222 ? -20.228  53.270  -54.149  1.00 34.77  ? 222 THR C CB  1 
ATOM   10258 O OG1 . THR C  1 222 ? -20.009  51.924  -54.588  1.00 32.78  ? 222 THR C OG1 1 
ATOM   10259 C CG2 . THR C  1 222 ? -18.989  54.153  -54.224  1.00 35.11  ? 222 THR C CG2 1 
ATOM   10260 N N   . THR C  1 223 ? -23.128  53.270  -52.482  1.00 34.49  ? 223 THR C N   1 
ATOM   10261 C CA  . THR C  1 223 ? -24.454  52.702  -52.309  1.00 34.92  ? 223 THR C CA  1 
ATOM   10262 C C   . THR C  1 223 ? -25.229  52.777  -53.621  1.00 31.68  ? 223 THR C C   1 
ATOM   10263 O O   . THR C  1 223 ? -26.346  52.291  -53.663  1.00 31.27  ? 223 THR C O   1 
ATOM   10264 C CB  . THR C  1 223 ? -25.205  53.344  -51.134  1.00 36.57  ? 223 THR C CB  1 
ATOM   10265 O OG1 . THR C  1 223 ? -25.029  54.756  -51.051  1.00 35.91  ? 223 THR C OG1 1 
ATOM   10266 C CG2 . THR C  1 223 ? -24.737  52.784  -49.804  1.00 37.06  ? 223 THR C CG2 1 
ATOM   10267 N N   . ALA C  1 224 ? -24.607  53.347  -54.665  1.00 29.60  ? 224 ALA C N   1 
ATOM   10268 C CA  . ALA C  1 224 ? -25.167  53.435  -56.005  1.00 28.36  ? 224 ALA C CA  1 
ATOM   10269 C C   . ALA C  1 224 ? -24.206  54.140  -56.967  1.00 28.87  ? 224 ALA C C   1 
ATOM   10270 O O   . ALA C  1 224 ? -23.381  54.965  -56.592  1.00 27.50  ? 224 ALA C O   1 
ATOM   10271 C CB  . ALA C  1 224 ? -26.480  54.151  -56.011  1.00 29.57  ? 224 ALA C CB  1 
ATOM   10272 N N   . PHE C  1 225 ? -24.369  53.791  -58.246  1.00 30.24  ? 225 PHE C N   1 
ATOM   10273 C CA  . PHE C  1 225 ? -23.673  54.366  -59.376  1.00 28.10  ? 225 PHE C CA  1 
ATOM   10274 C C   . PHE C  1 225 ? -24.223  53.645  -60.602  1.00 27.20  ? 225 PHE C C   1 
ATOM   10275 O O   . PHE C  1 225 ? -24.610  52.451  -60.506  1.00 24.84  ? 225 PHE C O   1 
ATOM   10276 C CB  . PHE C  1 225 ? -22.140  54.271  -59.267  1.00 28.11  ? 225 PHE C CB  1 
ATOM   10277 C CG  . PHE C  1 225 ? -21.538  52.872  -59.221  1.00 29.04  ? 225 PHE C CG  1 
ATOM   10278 C CD1 . PHE C  1 225 ? -21.368  52.206  -58.012  1.00 31.29  ? 225 PHE C CD1 1 
ATOM   10279 C CD2 . PHE C  1 225 ? -21.163  52.218  -60.387  1.00 29.66  ? 225 PHE C CD2 1 
ATOM   10280 C CE1 . PHE C  1 225 ? -20.832  50.931  -57.959  1.00 31.19  ? 225 PHE C CE1 1 
ATOM   10281 C CE2 . PHE C  1 225 ? -20.634  50.939  -60.342  1.00 31.61  ? 225 PHE C CE2 1 
ATOM   10282 C CZ  . PHE C  1 225 ? -20.443  50.302  -59.124  1.00 32.16  ? 225 PHE C CZ  1 
ATOM   10283 N N   . GLY C  1 226 ? -24.214  54.379  -61.736  1.00 26.46  ? 226 GLY C N   1 
ATOM   10284 C CA  . GLY C  1 226 ? -24.602  53.815  -63.019  1.00 27.73  ? 226 GLY C CA  1 
ATOM   10285 C C   . GLY C  1 226 ? -25.259  54.817  -63.967  1.00 29.69  ? 226 GLY C C   1 
ATOM   10286 O O   . GLY C  1 226 ? -25.124  56.028  -63.762  1.00 28.57  ? 226 GLY C O   1 
ATOM   10287 N N   . TYR C  1 227 ? -25.967  54.260  -64.985  1.00 27.82  ? 227 TYR C N   1 
ATOM   10288 C CA  . TYR C  1 227 ? -26.445  55.012  -66.135  1.00 26.69  ? 227 TYR C CA  1 
ATOM   10289 C C   . TYR C  1 227 ? -27.787  54.470  -66.609  1.00 27.30  ? 227 TYR C C   1 
ATOM   10290 O O   . TYR C  1 227 ? -28.072  53.285  -66.499  1.00 29.48  ? 227 TYR C O   1 
ATOM   10291 C CB  . TYR C  1 227 ? -25.457  54.987  -67.311  1.00 27.81  ? 227 TYR C CB  1 
ATOM   10292 C CG  . TYR C  1 227 ? -24.161  55.697  -66.969  1.00 26.65  ? 227 TYR C CG  1 
ATOM   10293 C CD1 . TYR C  1 227 ? -24.064  57.083  -67.054  1.00 26.07  ? 227 TYR C CD1 1 
ATOM   10294 C CD2 . TYR C  1 227 ? -23.075  54.993  -66.478  1.00 25.90  ? 227 TYR C CD2 1 
ATOM   10295 C CE1 . TYR C  1 227 ? -22.923  57.767  -66.671  1.00 25.85  ? 227 TYR C CE1 1 
ATOM   10296 C CE2 . TYR C  1 227 ? -21.919  55.660  -66.100  1.00 28.36  ? 227 TYR C CE2 1 
ATOM   10297 C CZ  . TYR C  1 227 ? -21.842  57.045  -66.202  1.00 27.09  ? 227 TYR C CZ  1 
ATOM   10298 O OH  . TYR C  1 227 ? -20.727  57.686  -65.825  1.00 28.14  ? 227 TYR C OH  1 
ATOM   10299 N N   . SER C  1 228 ? -28.588  55.372  -67.166  1.00 27.64  ? 228 SER C N   1 
ATOM   10300 C CA  . SER C  1 228 ? -29.911  55.082  -67.670  1.00 29.38  ? 228 SER C CA  1 
ATOM   10301 C C   . SER C  1 228 ? -29.862  55.029  -69.189  1.00 29.54  ? 228 SER C C   1 
ATOM   10302 O O   . SER C  1 228 ? -29.197  55.875  -69.795  1.00 27.55  ? 228 SER C O   1 
ATOM   10303 C CB  . SER C  1 228 ? -30.915  56.112  -67.225  1.00 30.61  ? 228 SER C CB  1 
ATOM   10304 O OG  . SER C  1 228 ? -32.060  56.150  -68.068  1.00 30.54  ? 228 SER C OG  1 
ATOM   10305 N N   . VAL C  1 229 ? -30.655  54.084  -69.745  1.00 28.40  ? 229 VAL C N   1 
ATOM   10306 C CA  . VAL C  1 229 ? -30.794  53.884  -71.179  1.00 29.46  ? 229 VAL C CA  1 
ATOM   10307 C C   . VAL C  1 229 ? -32.149  54.331  -71.714  1.00 29.28  ? 229 VAL C C   1 
ATOM   10308 O O   . VAL C  1 229 ? -32.579  53.861  -72.773  1.00 27.78  ? 229 VAL C O   1 
ATOM   10309 C CB  . VAL C  1 229 ? -30.484  52.435  -71.550  1.00 30.57  ? 229 VAL C CB  1 
ATOM   10310 C CG1 . VAL C  1 229 ? -29.005  52.228  -71.286  1.00 32.28  ? 229 VAL C CG1 1 
ATOM   10311 C CG2 . VAL C  1 229 ? -31.344  51.417  -70.799  1.00 31.20  ? 229 VAL C CG2 1 
ATOM   10312 N N   . SER C  1 230 ? -32.734  55.345  -71.056  1.00 29.25  ? 230 SER C N   1 
ATOM   10313 C CA  . SER C  1 230 ? -34.010  55.899  -71.482  1.00 29.12  ? 230 SER C CA  1 
ATOM   10314 C C   . SER C  1 230 ? -33.842  56.364  -72.918  1.00 29.02  ? 230 SER C C   1 
ATOM   10315 O O   . SER C  1 230 ? -32.740  56.790  -73.280  1.00 27.49  ? 230 SER C O   1 
ATOM   10316 C CB  . SER C  1 230 ? -34.470  57.012  -70.562  1.00 29.16  ? 230 SER C CB  1 
ATOM   10317 O OG  . SER C  1 230 ? -33.595  58.132  -70.628  1.00 29.39  ? 230 SER C OG  1 
ATOM   10318 N N   . PRO C  1 231 ? -34.852  56.150  -73.789  1.00 28.88  ? 231 PRO C N   1 
ATOM   10319 C CA  . PRO C  1 231 ? -34.818  56.633  -75.165  1.00 30.29  ? 231 PRO C CA  1 
ATOM   10320 C C   . PRO C  1 231 ? -34.473  58.110  -75.313  1.00 32.89  ? 231 PRO C C   1 
ATOM   10321 O O   . PRO C  1 231 ? -33.837  58.485  -76.304  1.00 29.39  ? 231 PRO C O   1 
ATOM   10322 C CB  . PRO C  1 231 ? -36.252  56.345  -75.646  1.00 31.26  ? 231 PRO C CB  1 
ATOM   10323 C CG  . PRO C  1 231 ? -36.573  55.048  -74.926  1.00 30.99  ? 231 PRO C CG  1 
ATOM   10324 C CD  . PRO C  1 231 ? -36.047  55.337  -73.521  1.00 30.82  ? 231 PRO C CD  1 
ATOM   10325 N N   . GLU C  1 232 ? -34.936  58.908  -74.329  1.00 34.99  ? 232 GLU C N   1 
ATOM   10326 C CA  . GLU C  1 232 ? -34.708  60.341  -74.309  1.00 38.85  ? 232 GLU C CA  1 
ATOM   10327 C C   . GLU C  1 232 ? -34.884  60.832  -72.880  1.00 37.47  ? 232 GLU C C   1 
ATOM   10328 O O   . GLU C  1 232 ? -35.086  60.024  -71.964  1.00 33.71  ? 232 GLU C O   1 
ATOM   10329 C CB  . GLU C  1 232 ? -35.644  61.089  -75.273  1.00 42.22  ? 232 GLU C CB  1 
ATOM   10330 C CG  . GLU C  1 232 ? -37.126  60.851  -74.999  1.00 45.59  ? 232 GLU C CG  1 
ATOM   10331 C CD  . GLU C  1 232 ? -38.143  61.439  -75.976  1.00 50.90  ? 232 GLU C CD  1 
ATOM   10332 O OE1 . GLU C  1 232 ? -37.831  62.381  -76.743  1.00 51.03  ? 232 GLU C OE1 1 
ATOM   10333 O OE2 . GLU C  1 232 ? -39.302  60.932  -75.948  1.00 58.11  ? 232 GLU C OE2 1 
ATOM   10334 N N   . GLY C  1 233 ? -34.809  62.161  -72.747  1.00 36.63  ? 233 GLY C N   1 
ATOM   10335 C CA  . GLY C  1 233 ? -34.987  62.828  -71.474  1.00 35.56  ? 233 GLY C CA  1 
ATOM   10336 C C   . GLY C  1 233 ? -33.662  62.905  -70.719  1.00 35.13  ? 233 GLY C C   1 
ATOM   10337 O O   . GLY C  1 233 ? -32.685  62.245  -71.098  1.00 35.72  ? 233 GLY C O   1 
ATOM   10338 N N   . GLY C  1 234 ? -33.713  63.628  -69.591  1.00 34.34  ? 234 GLY C N   1 
ATOM   10339 C CA  . GLY C  1 234 ? -32.590  63.921  -68.723  1.00 33.08  ? 234 GLY C CA  1 
ATOM   10340 C C   . GLY C  1 234 ? -31.807  65.083  -69.307  1.00 33.29  ? 234 GLY C C   1 
ATOM   10341 O O   . GLY C  1 234 ? -32.391  65.964  -69.891  1.00 32.98  ? 234 GLY C O   1 
ATOM   10342 N N   . ASN C  1 235 ? -30.494  65.077  -69.128  1.00 36.92  ? 235 ASN C N   1 
ATOM   10343 C CA  . ASN C  1 235 ? -29.597  65.888  -69.934  1.00 39.76  ? 235 ASN C CA  1 
ATOM   10344 C C   . ASN C  1 235 ? -28.153  65.409  -69.743  1.00 35.92  ? 235 ASN C C   1 
ATOM   10345 O O   . ASN C  1 235 ? -27.784  64.834  -68.719  1.00 34.47  ? 235 ASN C O   1 
ATOM   10346 C CB  . ASN C  1 235 ? -29.724  67.367  -69.607  1.00 47.55  ? 235 ASN C CB  1 
ATOM   10347 C CG  . ASN C  1 235 ? -28.882  67.689  -68.409  1.00 55.35  ? 235 ASN C CG  1 
ATOM   10348 O OD1 . ASN C  1 235 ? -29.202  67.256  -67.294  1.00 56.26  ? 235 ASN C OD1 1 
ATOM   10349 N ND2 . ASN C  1 235 ? -27.783  68.392  -68.652  1.00 62.94  ? 235 ASN C ND2 1 
ATOM   10350 N N   . GLY C  1 236 ? -27.326  65.660  -70.753  1.00 33.75  ? 236 GLY C N   1 
ATOM   10351 C CA  . GLY C  1 236 ? -25.987  65.120  -70.783  1.00 33.64  ? 236 GLY C CA  1 
ATOM   10352 C C   . GLY C  1 236 ? -26.064  63.604  -70.654  1.00 35.78  ? 236 GLY C C   1 
ATOM   10353 O O   . GLY C  1 236 ? -26.909  62.950  -71.289  1.00 34.35  ? 236 GLY C O   1 
ATOM   10354 N N   . GLN C  1 237 ? -25.255  63.095  -69.724  1.00 33.42  ? 237 GLN C N   1 
ATOM   10355 C CA  . GLN C  1 237 ? -25.092  61.672  -69.549  1.00 32.63  ? 237 GLN C CA  1 
ATOM   10356 C C   . GLN C  1 237 ? -26.184  61.129  -68.639  1.00 33.01  ? 237 GLN C C   1 
ATOM   10357 O O   . GLN C  1 237 ? -26.180  59.940  -68.361  1.00 32.41  ? 237 GLN C O   1 
ATOM   10358 C CB  . GLN C  1 237 ? -23.713  61.396  -68.944  1.00 32.09  ? 237 GLN C CB  1 
ATOM   10359 C CG  . GLN C  1 237 ? -22.549  61.406  -69.931  1.00 30.86  ? 237 GLN C CG  1 
ATOM   10360 C CD  . GLN C  1 237 ? -21.270  60.967  -69.246  1.00 31.78  ? 237 GLN C CD  1 
ATOM   10361 O OE1 . GLN C  1 237 ? -21.034  59.777  -68.953  1.00 30.44  ? 237 GLN C OE1 1 
ATOM   10362 N NE2 . GLN C  1 237 ? -20.467  61.962  -68.897  1.00 31.37  ? 237 GLN C NE2 1 
ATOM   10363 N N   . TYR C  1 238 ? -27.040  62.007  -68.102  1.00 33.20  ? 238 TYR C N   1 
ATOM   10364 C CA  . TYR C  1 238 ? -28.147  61.582  -67.252  1.00 31.67  ? 238 TYR C CA  1 
ATOM   10365 C C   . TYR C  1 238 ? -29.387  61.369  -68.124  1.00 33.41  ? 238 TYR C C   1 
ATOM   10366 O O   . TYR C  1 238 ? -29.919  62.302  -68.742  1.00 35.24  ? 238 TYR C O   1 
ATOM   10367 C CB  . TYR C  1 238 ? -28.463  62.589  -66.147  1.00 30.38  ? 238 TYR C CB  1 
ATOM   10368 C CG  . TYR C  1 238 ? -29.696  62.225  -65.339  1.00 31.34  ? 238 TYR C CG  1 
ATOM   10369 C CD1 . TYR C  1 238 ? -29.644  61.198  -64.409  1.00 31.51  ? 238 TYR C CD1 1 
ATOM   10370 C CD2 . TYR C  1 238 ? -30.915  62.878  -65.517  1.00 32.05  ? 238 TYR C CD2 1 
ATOM   10371 C CE1 . TYR C  1 238 ? -30.759  60.852  -63.666  1.00 33.31  ? 238 TYR C CE1 1 
ATOM   10372 C CE2 . TYR C  1 238 ? -32.047  62.528  -64.785  1.00 31.83  ? 238 TYR C CE2 1 
ATOM   10373 C CZ  . TYR C  1 238 ? -31.965  61.521  -63.843  1.00 32.61  ? 238 TYR C CZ  1 
ATOM   10374 O OH  . TYR C  1 238 ? -33.023  61.144  -63.073  1.00 30.36  ? 238 TYR C OH  1 
ATOM   10375 N N   . GLY C  1 239 ? -29.843  60.125  -68.134  1.00 32.47  ? 239 GLY C N   1 
ATOM   10376 C CA  . GLY C  1 239 ? -30.730  59.623  -69.159  1.00 34.28  ? 239 GLY C CA  1 
ATOM   10377 C C   . GLY C  1 239 ? -29.989  59.487  -70.481  1.00 33.51  ? 239 GLY C C   1 
ATOM   10378 O O   . GLY C  1 239 ? -28.823  59.885  -70.576  1.00 32.43  ? 239 GLY C O   1 
ATOM   10379 N N   . SER C  1 240 ? -30.673  58.832  -71.428  1.00 31.75  ? 240 SER C N   1 
ATOM   10380 C CA  . SER C  1 240 ? -30.361  58.884  -72.849  1.00 30.44  ? 240 SER C CA  1 
ATOM   10381 C C   . SER C  1 240 ? -29.053  58.163  -73.251  1.00 27.90  ? 240 SER C C   1 
ATOM   10382 O O   . SER C  1 240 ? -28.568  58.334  -74.359  1.00 27.77  ? 240 SER C O   1 
ATOM   10383 C CB  . SER C  1 240 ? -30.461  60.326  -73.298  1.00 29.94  ? 240 SER C CB  1 
ATOM   10384 O OG  . SER C  1 240 ? -31.830  60.718  -73.153  1.00 30.75  ? 240 SER C OG  1 
ATOM   10385 N N   . ASN C  1 241 ? -28.532  57.243  -72.444  1.00 27.79  ? 241 ASN C N   1 
ATOM   10386 C CA  . ASN C  1 241 ? -27.355  56.463  -72.852  1.00 28.61  ? 241 ASN C CA  1 
ATOM   10387 C C   . ASN C  1 241 ? -27.737  55.320  -73.773  1.00 27.79  ? 241 ASN C C   1 
ATOM   10388 O O   . ASN C  1 241 ? -28.857  54.866  -73.744  1.00 29.80  ? 241 ASN C O   1 
ATOM   10389 C CB  . ASN C  1 241 ? -26.600  55.887  -71.662  1.00 30.13  ? 241 ASN C CB  1 
ATOM   10390 C CG  . ASN C  1 241 ? -26.004  56.991  -70.811  1.00 30.93  ? 241 ASN C CG  1 
ATOM   10391 O OD1 . ASN C  1 241 ? -24.909  57.457  -71.082  1.00 37.36  ? 241 ASN C OD1 1 
ATOM   10392 N ND2 . ASN C  1 241 ? -26.712  57.496  -69.827  1.00 33.39  ? 241 ASN C ND2 1 
ATOM   10393 N N   . THR C  1 242 ? -26.818  54.879  -74.637  1.00 29.69  ? 242 THR C N   1 
ATOM   10394 C CA  . THR C  1 242 ? -26.990  53.630  -75.375  1.00 29.42  ? 242 THR C CA  1 
ATOM   10395 C C   . THR C  1 242 ? -26.729  52.461  -74.426  1.00 28.65  ? 242 THR C C   1 
ATOM   10396 O O   . THR C  1 242 ? -26.146  52.625  -73.360  1.00 28.61  ? 242 THR C O   1 
ATOM   10397 C CB  . THR C  1 242 ? -26.026  53.541  -76.562  1.00 30.05  ? 242 THR C CB  1 
ATOM   10398 O OG1 . THR C  1 242 ? -24.694  53.654  -76.066  1.00 30.44  ? 242 THR C OG1 1 
ATOM   10399 C CG2 . THR C  1 242 ? -26.264  54.591  -77.624  1.00 32.98  ? 242 THR C CG2 1 
ATOM   10400 N N   . LEU C  1 243 ? -27.026  51.253  -74.875  1.00 29.36  ? 243 LEU C N   1 
ATOM   10401 C CA  . LEU C  1 243 ? -26.649  50.071  -74.112  1.00 30.69  ? 243 LEU C CA  1 
ATOM   10402 C C   . LEU C  1 243 ? -25.120  49.957  -73.944  1.00 29.95  ? 243 LEU C C   1 
ATOM   10403 O O   . LEU C  1 243 ? -24.618  49.576  -72.877  1.00 28.94  ? 243 LEU C O   1 
ATOM   10404 C CB  . LEU C  1 243 ? -27.268  48.879  -74.845  1.00 32.13  ? 243 LEU C CB  1 
ATOM   10405 C CG  . LEU C  1 243 ? -28.798  48.772  -74.845  1.00 32.19  ? 243 LEU C CG  1 
ATOM   10406 C CD1 . LEU C  1 243 ? -29.170  47.546  -75.649  1.00 33.83  ? 243 LEU C CD1 1 
ATOM   10407 C CD2 . LEU C  1 243 ? -29.434  48.671  -73.468  1.00 31.64  ? 243 LEU C CD2 1 
ATOM   10408 N N   . LYS C  1 244 ? -24.357  50.304  -74.996  1.00 31.77  ? 244 LYS C N   1 
ATOM   10409 C CA  . LYS C  1 244 ? -22.905  50.335  -74.925  1.00 29.93  ? 244 LYS C CA  1 
ATOM   10410 C C   . LYS C  1 244 ? -22.401  51.364  -73.897  1.00 28.58  ? 244 LYS C C   1 
ATOM   10411 O O   . LYS C  1 244 ? -21.527  51.072  -73.073  1.00 27.16  ? 244 LYS C O   1 
ATOM   10412 C CB  . LYS C  1 244 ? -22.318  50.612  -76.313  1.00 32.55  ? 244 LYS C CB  1 
ATOM   10413 C CG  . LYS C  1 244 ? -20.802  50.326  -76.285  1.00 34.30  ? 244 LYS C CG  1 
ATOM   10414 C CD  . LYS C  1 244 ? -19.943  50.785  -77.461  1.00 38.79  ? 244 LYS C CD  1 
ATOM   10415 C CE  . LYS C  1 244 ? -18.419  50.652  -77.207  1.00 39.18  ? 244 LYS C CE  1 
ATOM   10416 N NZ  . LYS C  1 244 ? -18.053  49.513  -76.334  1.00 39.08  ? 244 LYS C NZ  1 
ATOM   10417 N N   . GLN C  1 245 ? -22.923  52.599  -73.952  1.00 28.06  ? 245 GLN C N   1 
ATOM   10418 C CA  . GLN C  1 245 ? -22.511  53.631  -73.005  1.00 27.42  ? 245 GLN C CA  1 
ATOM   10419 C C   . GLN C  1 245 ? -22.828  53.187  -71.577  1.00 28.27  ? 245 GLN C C   1 
ATOM   10420 O O   . GLN C  1 245 ? -22.040  53.397  -70.658  1.00 25.82  ? 245 GLN C O   1 
ATOM   10421 C CB  . GLN C  1 245 ? -23.176  54.970  -73.311  1.00 27.50  ? 245 GLN C CB  1 
ATOM   10422 C CG  . GLN C  1 245 ? -22.692  55.589  -74.612  1.00 27.43  ? 245 GLN C CG  1 
ATOM   10423 C CD  . GLN C  1 245 ? -23.582  56.708  -75.106  1.00 28.24  ? 245 GLN C CD  1 
ATOM   10424 O OE1 . GLN C  1 245 ? -24.815  56.707  -75.000  1.00 28.04  ? 245 GLN C OE1 1 
ATOM   10425 N NE2 . GLN C  1 245 ? -22.935  57.722  -75.641  1.00 28.42  ? 245 GLN C NE2 1 
ATOM   10426 N N   . GLN C  1 246 ? -24.002  52.567  -71.386  1.00 29.67  ? 246 GLN C N   1 
ATOM   10427 C CA  . GLN C  1 246 ? -24.334  52.049  -70.074  1.00 29.04  ? 246 GLN C CA  1 
ATOM   10428 C C   . GLN C  1 246 ? -23.238  51.070  -69.648  1.00 27.37  ? 246 GLN C C   1 
ATOM   10429 O O   . GLN C  1 246 ? -22.680  51.186  -68.560  1.00 28.11  ? 246 GLN C O   1 
ATOM   10430 C CB  . GLN C  1 246 ? -25.733  51.432  -70.056  1.00 27.99  ? 246 GLN C CB  1 
ATOM   10431 C CG  . GLN C  1 246 ? -26.127  50.940  -68.676  1.00 28.24  ? 246 GLN C CG  1 
ATOM   10432 C CD  . GLN C  1 246 ? -27.407  50.138  -68.679  1.00 29.64  ? 246 GLN C CD  1 
ATOM   10433 O OE1 . GLN C  1 246 ? -27.617  49.249  -69.513  1.00 28.23  ? 246 GLN C OE1 1 
ATOM   10434 N NE2 . GLN C  1 246 ? -28.287  50.477  -67.748  1.00 29.99  ? 246 GLN C NE2 1 
ATOM   10435 N N   . SER C  1 247 ? -22.955  50.084  -70.498  1.00 28.46  ? 247 SER C N   1 
ATOM   10436 C CA  . SER C  1 247 ? -22.049  49.001  -70.138  1.00 27.56  ? 247 SER C CA  1 
ATOM   10437 C C   . SER C  1 247 ? -20.671  49.592  -69.857  1.00 26.34  ? 247 SER C C   1 
ATOM   10438 O O   . SER C  1 247 ? -20.115  49.375  -68.787  1.00 26.83  ? 247 SER C O   1 
ATOM   10439 C CB  . SER C  1 247 ? -21.975  47.925  -71.224  1.00 26.92  ? 247 SER C CB  1 
ATOM   10440 O OG  . SER C  1 247 ? -21.044  46.927  -70.833  1.00 27.18  ? 247 SER C OG  1 
ATOM   10441 N N   . ASP C  1 248 ? -20.146  50.378  -70.802  1.00 24.91  ? 248 ASP C N   1 
ATOM   10442 C CA  . ASP C  1 248 ? -18.823  50.962  -70.617  1.00 26.04  ? 248 ASP C CA  1 
ATOM   10443 C C   . ASP C  1 248 ? -18.810  51.864  -69.379  1.00 26.31  ? 248 ASP C C   1 
ATOM   10444 O O   . ASP C  1 248 ? -17.824  51.886  -68.640  1.00 24.68  ? 248 ASP C O   1 
ATOM   10445 C CB  . ASP C  1 248 ? -18.360  51.724  -71.851  1.00 25.54  ? 248 ASP C CB  1 
ATOM   10446 C CG  . ASP C  1 248 ? -18.175  50.909  -73.117  1.00 24.21  ? 248 ASP C CG  1 
ATOM   10447 O OD1 . ASP C  1 248 ? -18.053  49.664  -73.023  1.00 24.80  ? 248 ASP C OD1 1 
ATOM   10448 O OD2 . ASP C  1 248 ? -18.109  51.538  -74.197  1.00 24.22  ? 248 ASP C OD2 1 
ATOM   10449 N N   . GLY C  1 249 ? -19.927  52.579  -69.140  1.00 27.32  ? 249 GLY C N   1 
ATOM   10450 C CA  . GLY C  1 249 ? -20.036  53.509  -68.016  1.00 26.98  ? 249 GLY C CA  1 
ATOM   10451 C C   . GLY C  1 249 ? -19.879  52.835  -66.648  1.00 26.46  ? 249 GLY C C   1 
ATOM   10452 O O   . GLY C  1 249 ? -19.238  53.376  -65.732  1.00 24.73  ? 249 GLY C O   1 
ATOM   10453 N N   . LEU C  1 250 ? -20.531  51.671  -66.498  1.00 25.59  ? 250 LEU C N   1 
ATOM   10454 C CA  . LEU C  1 250 ? -20.496  50.983  -65.225  1.00 25.42  ? 250 LEU C CA  1 
ATOM   10455 C C   . LEU C  1 250 ? -19.065  50.533  -64.934  1.00 27.56  ? 250 LEU C C   1 
ATOM   10456 O O   . LEU C  1 250 ? -18.643  50.625  -63.800  1.00 30.59  ? 250 LEU C O   1 
ATOM   10457 C CB  . LEU C  1 250 ? -21.482  49.817  -65.234  1.00 25.27  ? 250 LEU C CB  1 
ATOM   10458 C CG  . LEU C  1 250 ? -22.881  50.091  -64.677  1.00 25.18  ? 250 LEU C CG  1 
ATOM   10459 C CD1 . LEU C  1 250 ? -22.845  50.367  -63.196  1.00 24.91  ? 250 LEU C CD1 1 
ATOM   10460 C CD2 . LEU C  1 250 ? -23.559  51.253  -65.406  1.00 26.67  ? 250 LEU C CD2 1 
ATOM   10461 N N   . ILE C  1 251 ? -18.322  50.084  -65.956  1.00 27.51  ? 251 ILE C N   1 
ATOM   10462 C CA  . ILE C  1 251 ? -16.965  49.599  -65.780  1.00 30.25  ? 251 ILE C CA  1 
ATOM   10463 C C   . ILE C  1 251 ? -16.055  50.794  -65.464  1.00 28.79  ? 251 ILE C C   1 
ATOM   10464 O O   . ILE C  1 251 ? -15.165  50.681  -64.617  1.00 27.82  ? 251 ILE C O   1 
ATOM   10465 C CB  . ILE C  1 251 ? -16.476  48.799  -67.023  1.00 33.19  ? 251 ILE C CB  1 
ATOM   10466 C CG1 . ILE C  1 251 ? -17.370  47.609  -67.346  1.00 34.74  ? 251 ILE C CG1 1 
ATOM   10467 C CG2 . ILE C  1 251 ? -15.021  48.337  -66.895  1.00 32.26  ? 251 ILE C CG2 1 
ATOM   10468 C CD1 . ILE C  1 251 ? -17.568  46.649  -66.193  1.00 36.25  ? 251 ILE C CD1 1 
ATOM   10469 N N   . SER C  1 252 ? -16.271  51.921  -66.167  1.00 28.59  ? 252 SER C N   1 
ATOM   10470 C CA  . SER C  1 252 ? -15.555  53.173  -65.915  1.00 27.01  ? 252 SER C CA  1 
ATOM   10471 C C   . SER C  1 252 ? -15.756  53.598  -64.463  1.00 27.67  ? 252 SER C C   1 
ATOM   10472 O O   . SER C  1 252 ? -14.780  53.834  -63.739  1.00 27.10  ? 252 SER C O   1 
ATOM   10473 C CB  . SER C  1 252 ? -15.987  54.269  -66.885  1.00 26.46  ? 252 SER C CB  1 
ATOM   10474 O OG  . SER C  1 252 ? -15.387  55.513  -66.555  1.00 25.85  ? 252 SER C OG  1 
ATOM   10475 N N   . ASN C  1 253 ? -17.026  53.574  -64.000  1.00 26.62  ? 253 ASN C N   1 
ATOM   10476 C CA  . ASN C  1 253 ? -17.311  53.894  -62.609  1.00 26.30  ? 253 ASN C CA  1 
ATOM   10477 C C   . ASN C  1 253 ? -16.636  52.936  -61.627  1.00 26.11  ? 253 ASN C C   1 
ATOM   10478 O O   . ASN C  1 253 ? -16.139  53.364  -60.590  1.00 27.99  ? 253 ASN C O   1 
ATOM   10479 C CB  . ASN C  1 253 ? -18.804  53.869  -62.307  1.00 27.72  ? 253 ASN C CB  1 
ATOM   10480 C CG  . ASN C  1 253 ? -19.557  54.954  -63.034  1.00 27.14  ? 253 ASN C CG  1 
ATOM   10481 O OD1 . ASN C  1 253 ? -18.946  55.812  -63.709  1.00 28.45  ? 253 ASN C OD1 1 
ATOM   10482 N ND2 . ASN C  1 253 ? -20.875  54.912  -62.897  1.00 25.78  ? 253 ASN C ND2 1 
ATOM   10483 N N   . TYR C  1 254 ? -16.647  51.634  -61.915  1.00 26.08  ? 254 TYR C N   1 
ATOM   10484 C CA  . TYR C  1 254 ? -16.197  50.648  -60.938  1.00 26.14  ? 254 TYR C CA  1 
ATOM   10485 C C   . TYR C  1 254 ? -14.710  50.893  -60.662  1.00 26.13  ? 254 TYR C C   1 
ATOM   10486 O O   . TYR C  1 254 ? -14.277  50.939  -59.517  1.00 26.99  ? 254 TYR C O   1 
ATOM   10487 C CB  . TYR C  1 254 ? -16.490  49.210  -61.408  1.00 25.08  ? 254 TYR C CB  1 
ATOM   10488 C CG  . TYR C  1 254 ? -16.838  48.204  -60.317  1.00 24.19  ? 254 TYR C CG  1 
ATOM   10489 C CD1 . TYR C  1 254 ? -15.916  47.837  -59.353  1.00 24.48  ? 254 TYR C CD1 1 
ATOM   10490 C CD2 . TYR C  1 254 ? -18.106  47.605  -60.266  1.00 24.21  ? 254 TYR C CD2 1 
ATOM   10491 C CE1 . TYR C  1 254 ? -16.233  46.910  -58.363  1.00 25.38  ? 254 TYR C CE1 1 
ATOM   10492 C CE2 . TYR C  1 254 ? -18.447  46.706  -59.261  1.00 23.22  ? 254 TYR C CE2 1 
ATOM   10493 C CZ  . TYR C  1 254 ? -17.503  46.340  -58.317  1.00 23.41  ? 254 TYR C CZ  1 
ATOM   10494 O OH  . TYR C  1 254 ? -17.823  45.505  -57.294  1.00 21.92  ? 254 TYR C OH  1 
ATOM   10495 N N   . ARG C  1 255 ? -13.932  51.065  -61.731  1.00 27.11  ? 255 ARG C N   1 
ATOM   10496 C CA  . ARG C  1 255 ? -12.508  51.346  -61.612  1.00 27.58  ? 255 ARG C CA  1 
ATOM   10497 C C   . ARG C  1 255 ? -12.327  52.607  -60.759  1.00 28.52  ? 255 ARG C C   1 
ATOM   10498 O O   . ARG C  1 255 ? -11.643  52.586  -59.725  1.00 26.82  ? 255 ARG C O   1 
ATOM   10499 C CB  . ARG C  1 255 ? -11.949  51.432  -63.041  1.00 27.85  ? 255 ARG C CB  1 
ATOM   10500 C CG  . ARG C  1 255 ? -10.537  51.987  -63.198  1.00 29.65  ? 255 ARG C CG  1 
ATOM   10501 C CD  . ARG C  1 255 ? -9.421   51.004  -62.756  1.00 30.21  ? 255 ARG C CD  1 
ATOM   10502 N NE  . ARG C  1 255 ? -9.093   51.066  -61.328  1.00 29.21  ? 255 ARG C NE  1 
ATOM   10503 C CZ  . ARG C  1 255 ? -9.066   50.030  -60.494  1.00 29.53  ? 255 ARG C CZ  1 
ATOM   10504 N NH1 . ARG C  1 255 ? -9.369   48.803  -60.908  1.00 29.26  ? 255 ARG C NH1 1 
ATOM   10505 N NH2 . ARG C  1 255 ? -8.719   50.224  -59.239  1.00 28.70  ? 255 ARG C NH2 1 
ATOM   10506 N N   . ASP C  1 256 ? -13.001  53.693  -61.182  1.00 29.79  ? 256 ASP C N   1 
ATOM   10507 C CA  . ASP C  1 256 ? -12.779  55.008  -60.603  1.00 29.48  ? 256 ASP C CA  1 
ATOM   10508 C C   . ASP C  1 256 ? -13.123  54.951  -59.125  1.00 29.66  ? 256 ASP C C   1 
ATOM   10509 O O   . ASP C  1 256 ? -12.437  55.547  -58.304  1.00 28.50  ? 256 ASP C O   1 
ATOM   10510 C CB  . ASP C  1 256 ? -13.575  56.117  -61.286  1.00 30.03  ? 256 ASP C CB  1 
ATOM   10511 C CG  . ASP C  1 256 ? -13.193  56.438  -62.716  1.00 29.64  ? 256 ASP C CG  1 
ATOM   10512 O OD1 . ASP C  1 256 ? -12.222  55.844  -63.187  1.00 34.57  ? 256 ASP C OD1 1 
ATOM   10513 O OD2 . ASP C  1 256 ? -13.882  57.250  -63.346  1.00 28.61  ? 256 ASP C OD2 1 
ATOM   10514 N N   . LEU C  1 257 ? -14.169  54.203  -58.753  1.00 29.78  ? 257 LEU C N   1 
ATOM   10515 C CA  . LEU C  1 257 ? -14.592  54.324  -57.366  1.00 29.66  ? 257 LEU C CA  1 
ATOM   10516 C C   . LEU C  1 257 ? -13.685  53.513  -56.458  1.00 30.10  ? 257 LEU C C   1 
ATOM   10517 O O   . LEU C  1 257 ? -13.431  53.932  -55.328  1.00 29.34  ? 257 LEU C O   1 
ATOM   10518 C CB  . LEU C  1 257 ? -16.058  53.953  -57.238  1.00 30.05  ? 257 LEU C CB  1 
ATOM   10519 C CG  . LEU C  1 257 ? -17.003  54.970  -57.882  1.00 28.99  ? 257 LEU C CG  1 
ATOM   10520 C CD1 . LEU C  1 257 ? -18.369  54.287  -58.133  1.00 28.56  ? 257 LEU C CD1 1 
ATOM   10521 C CD2 . LEU C  1 257 ? -17.062  56.216  -57.001  1.00 27.87  ? 257 LEU C CD2 1 
ATOM   10522 N N   . ILE C  1 258 ? -13.177  52.369  -56.955  1.00 30.95  ? 258 ILE C N   1 
ATOM   10523 C CA  . ILE C  1 258 ? -12.146  51.664  -56.209  1.00 31.18  ? 258 ILE C CA  1 
ATOM   10524 C C   . ILE C  1 258 ? -10.949  52.598  -56.007  1.00 30.26  ? 258 ILE C C   1 
ATOM   10525 O O   . ILE C  1 258 ? -10.358  52.640  -54.933  1.00 29.59  ? 258 ILE C O   1 
ATOM   10526 C CB  . ILE C  1 258 ? -11.737  50.355  -56.896  1.00 31.77  ? 258 ILE C CB  1 
ATOM   10527 C CG1 . ILE C  1 258 ? -12.874  49.337  -56.823  1.00 32.93  ? 258 ILE C CG1 1 
ATOM   10528 C CG2 . ILE C  1 258 ? -10.436  49.804  -56.284  1.00 32.13  ? 258 ILE C CG2 1 
ATOM   10529 C CD1 . ILE C  1 258 ? -12.673  48.117  -57.702  1.00 32.84  ? 258 ILE C CD1 1 
ATOM   10530 N N   . ASP C  1 259 ? -10.612  53.353  -57.051  1.00 29.97  ? 259 ASP C N   1 
ATOM   10531 C CA  . ASP C  1 259 ? -9.479   54.273  -57.019  1.00 33.38  ? 259 ASP C CA  1 
ATOM   10532 C C   . ASP C  1 259 ? -9.649   55.365  -55.957  1.00 33.34  ? 259 ASP C C   1 
ATOM   10533 O O   . ASP C  1 259 ? -8.655   55.932  -55.492  1.00 36.74  ? 259 ASP C O   1 
ATOM   10534 C CB  . ASP C  1 259 ? -9.201   54.822  -58.417  1.00 32.69  ? 259 ASP C CB  1 
ATOM   10535 C CG  . ASP C  1 259 ? -8.677   53.758  -59.376  1.00 32.32  ? 259 ASP C CG  1 
ATOM   10536 O OD1 . ASP C  1 259 ? -8.036   52.815  -58.887  1.00 32.58  ? 259 ASP C OD1 1 
ATOM   10537 O OD2 . ASP C  1 259 ? -8.926   53.856  -60.585  1.00 31.18  ? 259 ASP C OD2 1 
ATOM   10538 N N   . ALA C  1 260 ? -10.903  55.643  -55.570  1.00 32.00  ? 260 ALA C N   1 
ATOM   10539 C CA  . ALA C  1 260 ? -11.212  56.619  -54.533  1.00 32.22  ? 260 ALA C CA  1 
ATOM   10540 C C   . ALA C  1 260 ? -11.099  55.980  -53.161  1.00 32.01  ? 260 ALA C C   1 
ATOM   10541 O O   . ALA C  1 260 ? -11.186  56.677  -52.169  1.00 35.60  ? 260 ALA C O   1 
ATOM   10542 C CB  . ALA C  1 260 ? -12.602  57.208  -54.753  1.00 32.05  ? 260 ALA C CB  1 
ATOM   10543 N N   . GLY C  1 261 ? -10.907  54.662  -53.108  1.00 31.73  ? 261 GLY C N   1 
ATOM   10544 C CA  . GLY C  1 261 ? -10.689  53.962  -51.853  1.00 30.53  ? 261 GLY C CA  1 
ATOM   10545 C C   . GLY C  1 261 ? -11.870  53.090  -51.423  1.00 29.60  ? 261 GLY C C   1 
ATOM   10546 O O   . GLY C  1 261 ? -11.885  52.641  -50.291  1.00 30.40  ? 261 GLY C O   1 
ATOM   10547 N N   . ALA C  1 262 ? -12.827  52.823  -52.318  1.00 29.13  ? 262 ALA C N   1 
ATOM   10548 C CA  . ALA C  1 262 ? -14.038  52.082  -51.987  1.00 29.94  ? 262 ALA C CA  1 
ATOM   10549 C C   . ALA C  1 262 ? -13.680  50.607  -51.797  1.00 30.66  ? 262 ALA C C   1 
ATOM   10550 O O   . ALA C  1 262 ? -12.910  50.072  -52.593  1.00 27.18  ? 262 ALA C O   1 
ATOM   10551 C CB  . ALA C  1 262 ? -15.082  52.256  -53.083  1.00 28.48  ? 262 ALA C CB  1 
ATOM   10552 N N   . VAL C  1 263 ? -14.190  50.005  -50.706  1.00 32.84  ? 263 VAL C N   1 
ATOM   10553 C CA  . VAL C  1 263 ? -13.982  48.588  -50.399  1.00 34.14  ? 263 VAL C CA  1 
ATOM   10554 C C   . VAL C  1 263 ? -15.317  47.825  -50.426  1.00 35.21  ? 263 VAL C C   1 
ATOM   10555 O O   . VAL C  1 263 ? -15.418  46.649  -50.041  1.00 32.53  ? 263 VAL C O   1 
ATOM   10556 C CB  . VAL C  1 263 ? -13.279  48.443  -49.037  1.00 35.06  ? 263 VAL C CB  1 
ATOM   10557 C CG1 . VAL C  1 263 ? -11.841  48.955  -49.081  1.00 35.09  ? 263 VAL C CG1 1 
ATOM   10558 C CG2 . VAL C  1 263 ? -14.081  49.097  -47.922  1.00 35.34  ? 263 VAL C CG2 1 
ATOM   10559 N N   . GLY C  1 264 ? -16.361  48.535  -50.871  1.00 36.11  ? 264 GLY C N   1 
ATOM   10560 C CA  . GLY C  1 264 ? -17.631  47.910  -51.171  1.00 37.07  ? 264 GLY C CA  1 
ATOM   10561 C C   . GLY C  1 264 ? -18.342  48.740  -52.226  1.00 37.45  ? 264 GLY C C   1 
ATOM   10562 O O   . GLY C  1 264 ? -18.169  49.960  -52.286  1.00 35.62  ? 264 GLY C O   1 
ATOM   10563 N N   . MET C  1 265 ? -19.079  48.039  -53.094  1.00 38.76  ? 265 MET C N   1 
ATOM   10564 C CA  . MET C  1 265 ? -19.623  48.645  -54.304  1.00 34.64  ? 265 MET C CA  1 
ATOM   10565 C C   . MET C  1 265 ? -21.055  48.174  -54.479  1.00 33.37  ? 265 MET C C   1 
ATOM   10566 O O   . MET C  1 265 ? -21.318  46.974  -54.454  1.00 35.05  ? 265 MET C O   1 
ATOM   10567 C CB  . MET C  1 265 ? -18.767  48.267  -55.518  1.00 32.27  ? 265 MET C CB  1 
ATOM   10568 C CG  . MET C  1 265 ? -17.344  48.798  -55.417  1.00 33.35  ? 265 MET C CG  1 
ATOM   10569 S SD  . MET C  1 265 ? -17.232  50.594  -55.615  1.00 32.20  ? 265 MET C SD  1 
ATOM   10570 C CE  . MET C  1 265 ? -17.297  50.541  -57.407  1.00 31.10  ? 265 MET C CE  1 
ATOM   10571 N N   . CYS C  1 266 ? -21.951  49.138  -54.650  1.00 32.43  ? 266 CYS C N   1 
ATOM   10572 C CA  . CYS C  1 266 ? -23.347  48.855  -54.917  1.00 32.91  ? 266 CYS C CA  1 
ATOM   10573 C C   . CYS C  1 266 ? -23.797  49.478  -56.237  1.00 29.98  ? 266 CYS C C   1 
ATOM   10574 O O   . CYS C  1 266 ? -24.632  50.383  -56.205  1.00 28.00  ? 266 CYS C O   1 
ATOM   10575 C CB  . CYS C  1 266 ? -24.265  49.421  -53.833  1.00 33.57  ? 266 CYS C CB  1 
ATOM   10576 S SG  . CYS C  1 266 ? -23.983  48.682  -52.206  1.00 33.39  ? 266 CYS C SG  1 
ATOM   10577 N N   . PRO C  1 267 ? -23.361  48.941  -57.405  1.00 29.02  ? 267 PRO C N   1 
ATOM   10578 C CA  . PRO C  1 267 ? -23.893  49.347  -58.713  1.00 27.74  ? 267 PRO C CA  1 
ATOM   10579 C C   . PRO C  1 267 ? -25.421  49.326  -58.773  1.00 28.07  ? 267 PRO C C   1 
ATOM   10580 O O   . PRO C  1 267 ? -26.051  48.412  -58.232  1.00 25.44  ? 267 PRO C O   1 
ATOM   10581 C CB  . PRO C  1 267 ? -23.278  48.344  -59.705  1.00 27.83  ? 267 PRO C CB  1 
ATOM   10582 C CG  . PRO C  1 267 ? -22.889  47.168  -58.827  1.00 28.43  ? 267 PRO C CG  1 
ATOM   10583 C CD  . PRO C  1 267 ? -22.394  47.844  -57.539  1.00 29.27  ? 267 PRO C CD  1 
ATOM   10584 N N   . PHE C  1 268 ? -25.959  50.364  -59.451  1.00 29.47  ? 268 PHE C N   1 
ATOM   10585 C CA  . PHE C  1 268 ? -27.372  50.656  -59.567  1.00 29.33  ? 268 PHE C CA  1 
ATOM   10586 C C   . PHE C  1 268 ? -27.834  50.432  -61.000  1.00 28.76  ? 268 PHE C C   1 
ATOM   10587 O O   . PHE C  1 268 ? -27.331  51.110  -61.906  1.00 28.67  ? 268 PHE C O   1 
ATOM   10588 C CB  . PHE C  1 268 ? -27.663  52.120  -59.192  1.00 30.12  ? 268 PHE C CB  1 
ATOM   10589 C CG  . PHE C  1 268 ? -29.151  52.440  -59.086  1.00 29.36  ? 268 PHE C CG  1 
ATOM   10590 C CD1 . PHE C  1 268 ? -29.853  52.211  -57.911  1.00 29.40  ? 268 PHE C CD1 1 
ATOM   10591 C CD2 . PHE C  1 268 ? -29.863  52.912  -60.177  1.00 30.94  ? 268 PHE C CD2 1 
ATOM   10592 C CE1 . PHE C  1 268 ? -31.224  52.422  -57.838  1.00 29.38  ? 268 PHE C CE1 1 
ATOM   10593 C CE2 . PHE C  1 268 ? -31.233  53.164  -60.081  1.00 30.74  ? 268 PHE C CE2 1 
ATOM   10594 C CZ  . PHE C  1 268 ? -31.907  52.890  -58.916  1.00 29.93  ? 268 PHE C CZ  1 
ATOM   10595 N N   . TYR C  1 269 ? -28.752  49.467  -61.220  1.00 29.32  ? 269 TYR C N   1 
ATOM   10596 C CA  . TYR C  1 269 ? -29.173  48.447  -60.249  1.00 28.08  ? 269 TYR C CA  1 
ATOM   10597 C C   . TYR C  1 269 ? -29.716  47.251  -61.034  1.00 27.54  ? 269 TYR C C   1 
ATOM   10598 O O   . TYR C  1 269 ? -29.631  47.232  -62.262  1.00 27.26  ? 269 TYR C O   1 
ATOM   10599 C CB  . TYR C  1 269 ? -30.160  48.995  -59.203  1.00 27.38  ? 269 TYR C CB  1 
ATOM   10600 C CG  . TYR C  1 269 ? -31.559  49.424  -59.633  1.00 28.12  ? 269 TYR C CG  1 
ATOM   10601 C CD1 . TYR C  1 269 ? -31.848  49.828  -60.923  1.00 28.66  ? 269 TYR C CD1 1 
ATOM   10602 C CD2 . TYR C  1 269 ? -32.607  49.479  -58.720  1.00 28.58  ? 269 TYR C CD2 1 
ATOM   10603 C CE1 . TYR C  1 269 ? -33.111  50.269  -61.285  1.00 28.59  ? 269 TYR C CE1 1 
ATOM   10604 C CE2 . TYR C  1 269 ? -33.872  49.932  -59.064  1.00 27.63  ? 269 TYR C CE2 1 
ATOM   10605 C CZ  . TYR C  1 269 ? -34.122  50.328  -60.354  1.00 28.36  ? 269 TYR C CZ  1 
ATOM   10606 O OH  . TYR C  1 269 ? -35.343  50.762  -60.767  1.00 29.34  ? 269 TYR C OH  1 
ATOM   10607 N N   . TYR C  1 270 ? -30.345  46.280  -60.350  1.00 28.58  ? 270 TYR C N   1 
ATOM   10608 C CA  . TYR C  1 270 ? -30.749  45.033  -60.994  1.00 28.16  ? 270 TYR C CA  1 
ATOM   10609 C C   . TYR C  1 270 ? -31.777  45.234  -62.112  1.00 28.35  ? 270 TYR C C   1 
ATOM   10610 O O   . TYR C  1 270 ? -31.531  44.762  -63.218  1.00 28.95  ? 270 TYR C O   1 
ATOM   10611 C CB  . TYR C  1 270 ? -31.234  44.051  -59.931  1.00 30.44  ? 270 TYR C CB  1 
ATOM   10612 C CG  . TYR C  1 270 ? -31.965  42.811  -60.427  1.00 30.40  ? 270 TYR C CG  1 
ATOM   10613 C CD1 . TYR C  1 270 ? -31.301  41.816  -61.119  1.00 31.53  ? 270 TYR C CD1 1 
ATOM   10614 C CD2 . TYR C  1 270 ? -33.297  42.587  -60.105  1.00 32.33  ? 270 TYR C CD2 1 
ATOM   10615 C CE1 . TYR C  1 270 ? -31.948  40.668  -61.548  1.00 30.06  ? 270 TYR C CE1 1 
ATOM   10616 C CE2 . TYR C  1 270 ? -33.954  41.434  -60.508  1.00 33.47  ? 270 TYR C CE2 1 
ATOM   10617 C CZ  . TYR C  1 270 ? -33.273  40.474  -61.230  1.00 30.84  ? 270 TYR C CZ  1 
ATOM   10618 O OH  . TYR C  1 270 ? -33.921  39.367  -61.647  1.00 31.41  ? 270 TYR C OH  1 
ATOM   10619 N N   . ALA C  1 271 ? -32.941  45.864  -61.867  1.00 27.86  ? 271 ALA C N   1 
ATOM   10620 C CA  . ALA C  1 271 ? -33.938  45.919  -62.928  1.00 29.11  ? 271 ALA C CA  1 
ATOM   10621 C C   . ALA C  1 271 ? -34.756  47.212  -62.933  1.00 30.34  ? 271 ALA C C   1 
ATOM   10622 O O   . ALA C  1 271 ? -34.946  47.833  -61.892  1.00 30.81  ? 271 ALA C O   1 
ATOM   10623 C CB  . ALA C  1 271 ? -34.853  44.716  -62.822  1.00 30.32  ? 271 ALA C CB  1 
ATOM   10624 N N   . ASP C  1 272 ? -35.257  47.564  -64.129  1.00 29.83  ? 272 ASP C N   1 
ATOM   10625 C CA  . ASP C  1 272 ? -36.017  48.777  -64.339  1.00 31.42  ? 272 ASP C CA  1 
ATOM   10626 C C   . ASP C  1 272 ? -37.222  48.826  -63.398  1.00 31.23  ? 272 ASP C C   1 
ATOM   10627 O O   . ASP C  1 272 ? -37.872  47.800  -63.119  1.00 30.85  ? 272 ASP C O   1 
ATOM   10628 C CB  . ASP C  1 272 ? -36.533  48.878  -65.766  1.00 33.65  ? 272 ASP C CB  1 
ATOM   10629 C CG  . ASP C  1 272 ? -35.571  49.351  -66.852  1.00 34.62  ? 272 ASP C CG  1 
ATOM   10630 O OD1 . ASP C  1 272 ? -34.392  49.723  -66.533  1.00 33.51  ? 272 ASP C OD1 1 
ATOM   10631 O OD2 . ASP C  1 272 ? -36.029  49.353  -68.025  1.00 33.86  ? 272 ASP C OD2 1 
ATOM   10632 N N   . GLY C  1 273 ? -37.460  50.033  -62.876  1.00 30.04  ? 273 GLY C N   1 
ATOM   10633 C CA  . GLY C  1 273 ? -38.670  50.367  -62.139  1.00 31.30  ? 273 GLY C CA  1 
ATOM   10634 C C   . GLY C  1 273 ? -39.513  51.351  -62.940  1.00 31.24  ? 273 GLY C C   1 
ATOM   10635 O O   . GLY C  1 273 ? -39.128  52.516  -63.073  1.00 31.96  ? 273 GLY C O   1 
ATOM   10636 N N   . TRP C  1 274 ? -40.618  50.866  -63.508  1.00 31.46  ? 274 TRP C N   1 
ATOM   10637 C CA  . TRP C  1 274 ? -41.480  51.677  -64.355  1.00 33.38  ? 274 TRP C CA  1 
ATOM   10638 C C   . TRP C  1 274 ? -42.223  52.727  -63.522  1.00 36.50  ? 274 TRP C C   1 
ATOM   10639 O O   . TRP C  1 274 ? -42.739  53.729  -64.060  1.00 37.17  ? 274 TRP C O   1 
ATOM   10640 C CB  . TRP C  1 274 ? -42.487  50.800  -65.111  1.00 33.85  ? 274 TRP C CB  1 
ATOM   10641 C CG  . TRP C  1 274 ? -41.915  49.945  -66.217  1.00 33.10  ? 274 TRP C CG  1 
ATOM   10642 C CD1 . TRP C  1 274 ? -40.621  49.522  -66.385  1.00 32.56  ? 274 TRP C CD1 1 
ATOM   10643 C CD2 . TRP C  1 274 ? -42.648  49.417  -67.344  1.00 32.85  ? 274 TRP C CD2 1 
ATOM   10644 N NE1 . TRP C  1 274 ? -40.498  48.779  -67.534  1.00 31.24  ? 274 TRP C NE1 1 
ATOM   10645 C CE2 . TRP C  1 274 ? -41.726  48.670  -68.127  1.00 31.77  ? 274 TRP C CE2 1 
ATOM   10646 C CE3 . TRP C  1 274 ? -43.984  49.493  -67.762  1.00 32.79  ? 274 TRP C CE3 1 
ATOM   10647 C CZ2 . TRP C  1 274 ? -42.108  48.018  -69.300  1.00 31.46  ? 274 TRP C CZ2 1 
ATOM   10648 C CZ3 . TRP C  1 274 ? -44.354  48.834  -68.916  1.00 32.64  ? 274 TRP C CZ3 1 
ATOM   10649 C CH2 . TRP C  1 274 ? -43.432  48.119  -69.681  1.00 31.53  ? 274 TRP C CH2 1 
ATOM   10650 N N   . TRP C  1 275 ? -42.287  52.473  -62.206  1.00 37.14  ? 275 TRP C N   1 
ATOM   10651 C CA  . TRP C  1 275 ? -43.024  53.343  -61.300  1.00 39.04  ? 275 TRP C CA  1 
ATOM   10652 C C   . TRP C  1 275 ? -42.280  54.666  -61.124  1.00 37.84  ? 275 TRP C C   1 
ATOM   10653 O O   . TRP C  1 275 ? -42.889  55.670  -60.782  1.00 39.54  ? 275 TRP C O   1 
ATOM   10654 C CB  . TRP C  1 275 ? -43.289  52.658  -59.944  1.00 39.73  ? 275 TRP C CB  1 
ATOM   10655 C CG  . TRP C  1 275 ? -42.068  52.448  -59.076  1.00 39.29  ? 275 TRP C CG  1 
ATOM   10656 C CD1 . TRP C  1 275 ? -41.251  51.367  -59.064  1.00 36.78  ? 275 TRP C CD1 1 
ATOM   10657 C CD2 . TRP C  1 275 ? -41.547  53.362  -58.076  1.00 40.44  ? 275 TRP C CD2 1 
ATOM   10658 N NE1 . TRP C  1 275 ? -40.255  51.546  -58.149  1.00 36.77  ? 275 TRP C NE1 1 
ATOM   10659 C CE2 . TRP C  1 275 ? -40.404  52.748  -57.524  1.00 37.81  ? 275 TRP C CE2 1 
ATOM   10660 C CE3 . TRP C  1 275 ? -41.905  54.647  -57.620  1.00 38.96  ? 275 TRP C CE3 1 
ATOM   10661 C CZ2 . TRP C  1 275 ? -39.627  53.373  -56.540  1.00 38.92  ? 275 TRP C CZ2 1 
ATOM   10662 C CZ3 . TRP C  1 275 ? -41.131  55.266  -56.657  1.00 37.66  ? 275 TRP C CZ3 1 
ATOM   10663 C CH2 . TRP C  1 275 ? -40.011  54.634  -56.117  1.00 38.01  ? 275 TRP C CH2 1 
ATOM   10664 N N   . LYS C  1 276 ? -40.986  54.664  -61.423  1.00 35.63  ? 276 LYS C N   1 
ATOM   10665 C CA  . LYS C  1 276 ? -40.077  55.626  -60.836  1.00 37.11  ? 276 LYS C CA  1 
ATOM   10666 C C   . LYS C  1 276 ? -40.269  57.019  -61.432  1.00 38.35  ? 276 LYS C C   1 
ATOM   10667 O O   . LYS C  1 276 ? -39.846  57.979  -60.826  1.00 42.79  ? 276 LYS C O   1 
ATOM   10668 C CB  . LYS C  1 276 ? -38.633  55.129  -60.952  1.00 34.43  ? 276 LYS C CB  1 
ATOM   10669 C CG  . LYS C  1 276 ? -38.231  54.055  -59.952  1.00 33.30  ? 276 LYS C CG  1 
ATOM   10670 C CD  . LYS C  1 276 ? -36.847  53.461  -60.183  1.00 32.29  ? 276 LYS C CD  1 
ATOM   10671 C CE  . LYS C  1 276 ? -35.686  54.343  -59.900  1.00 31.35  ? 276 LYS C CE  1 
ATOM   10672 N NZ  . LYS C  1 276 ? -35.621  54.704  -58.486  1.00 32.85  ? 276 LYS C NZ  1 
ATOM   10673 N N   . GLY C  1 277 ? -40.908  57.143  -62.590  1.00 40.21  ? 277 GLY C N   1 
ATOM   10674 C CA  . GLY C  1 277 ? -41.175  58.447  -63.170  1.00 41.96  ? 277 GLY C CA  1 
ATOM   10675 C C   . GLY C  1 277 ? -42.672  58.718  -63.332  1.00 43.93  ? 277 GLY C C   1 
ATOM   10676 O O   . GLY C  1 277 ? -43.057  59.517  -64.181  1.00 44.68  ? 277 GLY C O   1 
ATOM   10677 N N   . GLY C  1 278 ? -43.506  58.081  -62.493  1.00 44.66  ? 278 GLY C N   1 
ATOM   10678 C CA  . GLY C  1 278 ? -44.955  58.162  -62.622  1.00 43.44  ? 278 GLY C CA  1 
ATOM   10679 C C   . GLY C  1 278 ? -45.453  57.109  -63.606  1.00 42.96  ? 278 GLY C C   1 
ATOM   10680 O O   . GLY C  1 278 ? -44.687  56.562  -64.406  1.00 46.25  ? 278 GLY C O   1 
ATOM   10681 N N   . GLU C  1 279 ? -46.731  56.809  -63.495  1.00 43.12  ? 279 GLU C N   1 
ATOM   10682 C CA  . GLU C  1 279 ? -47.387  55.789  -64.293  1.00 44.23  ? 279 GLU C CA  1 
ATOM   10683 C C   . GLU C  1 279 ? -46.628  54.474  -64.184  1.00 40.73  ? 279 GLU C C   1 
ATOM   10684 O O   . GLU C  1 279 ? -45.791  54.142  -65.004  1.00 39.06  ? 279 GLU C O   1 
ATOM   10685 C CB  . GLU C  1 279 ? -47.645  56.241  -65.728  1.00 44.38  ? 279 GLU C CB  1 
ATOM   10686 C CG  . GLU C  1 279 ? -48.906  57.095  -65.792  1.00 47.30  ? 279 GLU C CG  1 
ATOM   10687 C CD  . GLU C  1 279 ? -48.786  58.350  -64.940  1.00 48.91  ? 279 GLU C CD  1 
ATOM   10688 O OE1 . GLU C  1 279 ? -47.790  59.093  -65.178  1.00 45.33  ? 279 GLU C OE1 1 
ATOM   10689 O OE2 . GLU C  1 279 ? -49.673  58.577  -64.066  1.00 53.13  ? 279 GLU C OE2 1 
ATOM   10690 N N   . LYS C  1 280 ? -46.981  53.687  -63.181  1.00 42.19  ? 280 LYS C N   1 
ATOM   10691 C CA  . LYS C  1 280 ? -46.307  52.410  -62.945  1.00 40.99  ? 280 LYS C CA  1 
ATOM   10692 C C   . LYS C  1 280 ? -46.572  51.386  -64.051  1.00 39.05  ? 280 LYS C C   1 
ATOM   10693 O O   . LYS C  1 280 ? -45.778  50.461  -64.192  1.00 38.46  ? 280 LYS C O   1 
ATOM   10694 C CB  . LYS C  1 280 ? -46.752  51.874  -61.583  1.00 41.94  ? 280 LYS C CB  1 
ATOM   10695 C CG  . LYS C  1 280 ? -48.220  51.528  -61.537  1.00 43.26  ? 280 LYS C CG  1 
ATOM   10696 C CD  . LYS C  1 280 ? -48.697  51.061  -60.173  1.00 45.48  ? 280 LYS C CD  1 
ATOM   10697 C CE  . LYS C  1 280 ? -50.174  50.843  -60.297  1.00 47.07  ? 280 LYS C CE  1 
ATOM   10698 N NZ  . LYS C  1 280 ? -50.746  50.823  -58.968  1.00 48.36  ? 280 LYS C NZ  1 
ATOM   10699 N N   . SER C  1 281 ? -47.656  51.562  -64.823  1.00 39.28  ? 281 SER C N   1 
ATOM   10700 C CA  . SER C  1 281 ? -48.079  50.645  -65.882  1.00 41.54  ? 281 SER C CA  1 
ATOM   10701 C C   . SER C  1 281 ? -47.570  51.033  -67.272  1.00 42.05  ? 281 SER C C   1 
ATOM   10702 O O   . SER C  1 281 ? -47.821  50.331  -68.259  1.00 42.80  ? 281 SER C O   1 
ATOM   10703 C CB  . SER C  1 281 ? -49.573  50.528  -65.920  1.00 43.67  ? 281 SER C CB  1 
ATOM   10704 O OG  . SER C  1 281 ? -49.999  49.851  -64.754  1.00 44.59  ? 281 SER C OG  1 
ATOM   10705 N N   . ASP C  1 282 ? -46.797  52.113  -67.341  1.00 41.37  ? 282 ASP C N   1 
ATOM   10706 C CA  . ASP C  1 282 ? -46.271  52.564  -68.598  1.00 41.39  ? 282 ASP C CA  1 
ATOM   10707 C C   . ASP C  1 282 ? -44.780  52.819  -68.424  1.00 38.04  ? 282 ASP C C   1 
ATOM   10708 O O   . ASP C  1 282 ? -44.330  53.365  -67.410  1.00 35.50  ? 282 ASP C O   1 
ATOM   10709 C CB  . ASP C  1 282 ? -47.053  53.786  -69.054  1.00 44.66  ? 282 ASP C CB  1 
ATOM   10710 C CG  . ASP C  1 282 ? -46.684  54.253  -70.450  1.00 50.16  ? 282 ASP C CG  1 
ATOM   10711 O OD1 . ASP C  1 282 ? -46.922  53.457  -71.402  1.00 54.21  ? 282 ASP C OD1 1 
ATOM   10712 O OD2 . ASP C  1 282 ? -46.157  55.392  -70.576  1.00 55.32  ? 282 ASP C OD2 1 
ATOM   10713 N N   . HIS C  1 283 ? -44.029  52.483  -69.470  1.00 37.32  ? 283 HIS C N   1 
ATOM   10714 C CA  . HIS C  1 283 ? -42.594  52.728  -69.472  1.00 35.19  ? 283 HIS C CA  1 
ATOM   10715 C C   . HIS C  1 283 ? -42.340  54.005  -70.249  1.00 35.17  ? 283 HIS C C   1 
ATOM   10716 O O   . HIS C  1 283 ? -42.303  54.007  -71.478  1.00 35.01  ? 283 HIS C O   1 
ATOM   10717 C CB  . HIS C  1 283 ? -41.844  51.562  -70.115  1.00 33.26  ? 283 HIS C CB  1 
ATOM   10718 C CG  . HIS C  1 283 ? -40.438  51.428  -69.659  1.00 31.91  ? 283 HIS C CG  1 
ATOM   10719 N ND1 . HIS C  1 283 ? -39.542  50.572  -70.279  1.00 30.48  ? 283 HIS C ND1 1 
ATOM   10720 C CD2 . HIS C  1 283 ? -39.810  51.960  -68.596  1.00 31.01  ? 283 HIS C CD2 1 
ATOM   10721 C CE1 . HIS C  1 283 ? -38.385  50.634  -69.617  1.00 31.13  ? 283 HIS C CE1 1 
ATOM   10722 N NE2 . HIS C  1 283 ? -38.526  51.457  -68.575  1.00 30.60  ? 283 HIS C NE2 1 
ATOM   10723 N N   . SER C  1 284 ? -42.188  55.104  -69.524  1.00 36.79  ? 284 SER C N   1 
ATOM   10724 C CA  . SER C  1 284 ? -42.129  56.391  -70.180  1.00 37.09  ? 284 SER C CA  1 
ATOM   10725 C C   . SER C  1 284 ? -40.793  56.549  -70.922  1.00 36.26  ? 284 SER C C   1 
ATOM   10726 O O   . SER C  1 284 ? -39.717  56.242  -70.398  1.00 33.73  ? 284 SER C O   1 
ATOM   10727 C CB  . SER C  1 284 ? -42.360  57.474  -69.213  1.00 38.12  ? 284 SER C CB  1 
ATOM   10728 O OG  . SER C  1 284 ? -41.984  58.676  -69.867  1.00 40.32  ? 284 SER C OG  1 
ATOM   10729 N N   . LEU C  1 285 ? -40.871  57.030  -72.169  1.00 37.45  ? 285 LEU C N   1 
ATOM   10730 C CA  . LEU C  1 285 ? -39.709  57.128  -73.040  1.00 38.43  ? 285 LEU C CA  1 
ATOM   10731 C C   . LEU C  1 285 ? -38.778  58.239  -72.562  1.00 37.14  ? 285 LEU C C   1 
ATOM   10732 O O   . LEU C  1 285 ? -37.578  58.187  -72.860  1.00 37.46  ? 285 LEU C O   1 
ATOM   10733 C CB  . LEU C  1 285 ? -40.090  57.313  -74.513  1.00 41.94  ? 285 LEU C CB  1 
ATOM   10734 C CG  . LEU C  1 285 ? -41.175  56.365  -75.063  1.00 48.34  ? 285 LEU C CG  1 
ATOM   10735 C CD1 . LEU C  1 285 ? -41.332  56.531  -76.603  1.00 49.32  ? 285 LEU C CD1 1 
ATOM   10736 C CD2 . LEU C  1 285 ? -40.957  54.872  -74.656  1.00 45.28  ? 285 LEU C CD2 1 
ATOM   10737 N N   . ASN C  1 286 ? -39.308  59.217  -71.809  1.00 36.16  ? 286 ASN C N   1 
ATOM   10738 C CA  . ASN C  1 286 ? -38.493  60.356  -71.427  1.00 37.02  ? 286 ASN C CA  1 
ATOM   10739 C C   . ASN C  1 286 ? -38.240  60.465  -69.926  1.00 35.37  ? 286 ASN C C   1 
ATOM   10740 O O   . ASN C  1 286 ? -37.921  61.548  -69.451  1.00 33.94  ? 286 ASN C O   1 
ATOM   10741 C CB  . ASN C  1 286 ? -39.095  61.653  -71.938  1.00 38.97  ? 286 ASN C CB  1 
ATOM   10742 C CG  . ASN C  1 286 ? -40.361  62.028  -71.223  1.00 40.45  ? 286 ASN C CG  1 
ATOM   10743 O OD1 . ASN C  1 286 ? -41.098  61.170  -70.733  1.00 44.02  ? 286 ASN C OD1 1 
ATOM   10744 N ND2 . ASN C  1 286 ? -40.657  63.307  -71.213  1.00 41.57  ? 286 ASN C ND2 1 
ATOM   10745 N N   . GLN C  1 287 ? -38.288  59.347  -69.206  1.00 35.28  ? 287 GLN C N   1 
ATOM   10746 C CA  . GLN C  1 287 ? -38.035  59.343  -67.776  1.00 37.30  ? 287 GLN C CA  1 
ATOM   10747 C C   . GLN C  1 287 ? -36.753  58.566  -67.528  1.00 36.27  ? 287 GLN C C   1 
ATOM   10748 O O   . GLN C  1 287 ? -36.798  57.344  -67.460  1.00 38.23  ? 287 GLN C O   1 
ATOM   10749 C CB  . GLN C  1 287 ? -39.137  58.670  -66.948  1.00 40.25  ? 287 GLN C CB  1 
ATOM   10750 C CG  . GLN C  1 287 ? -40.445  59.463  -66.860  1.00 44.13  ? 287 GLN C CG  1 
ATOM   10751 C CD  . GLN C  1 287 ? -40.274  60.844  -66.250  1.00 44.38  ? 287 GLN C CD  1 
ATOM   10752 O OE1 . GLN C  1 287 ? -39.552  61.033  -65.267  1.00 44.31  ? 287 GLN C OE1 1 
ATOM   10753 N NE2 . GLN C  1 287 ? -40.884  61.838  -66.872  1.00 44.76  ? 287 GLN C NE2 1 
ATOM   10754 N N   . PRO C  1 288 ? -35.590  59.235  -67.357  1.00 35.31  ? 288 PRO C N   1 
ATOM   10755 C CA  . PRO C  1 288 ? -34.337  58.533  -67.050  1.00 34.35  ? 288 PRO C CA  1 
ATOM   10756 C C   . PRO C  1 288 ? -34.467  57.424  -66.003  1.00 34.19  ? 288 PRO C C   1 
ATOM   10757 O O   . PRO C  1 288 ? -33.844  56.369  -66.112  1.00 33.51  ? 288 PRO C O   1 
ATOM   10758 C CB  . PRO C  1 288 ? -33.484  59.692  -66.544  1.00 33.92  ? 288 PRO C CB  1 
ATOM   10759 C CG  . PRO C  1 288 ? -33.909  60.843  -67.423  1.00 36.26  ? 288 PRO C CG  1 
ATOM   10760 C CD  . PRO C  1 288 ? -35.423  60.692  -67.511  1.00 36.70  ? 288 PRO C CD  1 
ATOM   10761 N N   . GLU C  1 289 ? -35.325  57.689  -65.009  1.00 32.64  ? 289 GLU C N   1 
ATOM   10762 C CA  . GLU C  1 289 ? -35.351  56.967  -63.753  1.00 33.23  ? 289 GLU C CA  1 
ATOM   10763 C C   . GLU C  1 289 ? -35.929  55.562  -63.950  1.00 32.65  ? 289 GLU C C   1 
ATOM   10764 O O   . GLU C  1 289 ? -35.737  54.745  -63.054  1.00 31.59  ? 289 GLU C O   1 
ATOM   10765 C CB  . GLU C  1 289 ? -36.136  57.722  -62.669  1.00 32.72  ? 289 GLU C CB  1 
ATOM   10766 C CG  . GLU C  1 289 ? -35.386  58.892  -62.035  1.00 32.70  ? 289 GLU C CG  1 
ATOM   10767 C CD  . GLU C  1 289 ? -34.120  58.557  -61.259  1.00 34.26  ? 289 GLU C CD  1 
ATOM   10768 O OE1 . GLU C  1 289 ? -34.192  57.621  -60.443  1.00 34.98  ? 289 GLU C OE1 1 
ATOM   10769 O OE2 . GLU C  1 289 ? -33.059  59.212  -61.456  1.00 35.61  ? 289 GLU C OE2 1 
ATOM   10770 N N   . GLU C  1 290 ? -36.630  55.320  -65.077  1.00 30.93  ? 290 GLU C N   1 
ATOM   10771 C CA  . GLU C  1 290 ? -37.273  54.050  -65.343  1.00 32.30  ? 290 GLU C CA  1 
ATOM   10772 C C   . GLU C  1 290 ? -36.358  53.097  -66.131  1.00 33.18  ? 290 GLU C C   1 
ATOM   10773 O O   . GLU C  1 290 ? -36.790  51.989  -66.472  1.00 29.87  ? 290 GLU C O   1 
ATOM   10774 C CB  . GLU C  1 290 ? -38.547  54.328  -66.138  1.00 34.71  ? 290 GLU C CB  1 
ATOM   10775 C CG  . GLU C  1 290 ? -39.503  55.285  -65.432  1.00 36.11  ? 290 GLU C CG  1 
ATOM   10776 C CD  . GLU C  1 290 ? -40.908  55.388  -65.984  1.00 37.34  ? 290 GLU C CD  1 
ATOM   10777 O OE1 . GLU C  1 290 ? -41.320  54.528  -66.789  1.00 37.97  ? 290 GLU C OE1 1 
ATOM   10778 O OE2 . GLU C  1 290 ? -41.629  56.319  -65.540  1.00 40.50  ? 290 GLU C OE2 1 
ATOM   10779 N N   . TRP C  1 291 ? -35.115  53.532  -66.458  1.00 32.01  ? 291 TRP C N   1 
ATOM   10780 C CA  . TRP C  1 291 ? -34.286  52.753  -67.371  1.00 31.22  ? 291 TRP C CA  1 
ATOM   10781 C C   . TRP C  1 291 ? -32.877  52.522  -66.822  1.00 28.36  ? 291 TRP C C   1 
ATOM   10782 O O   . TRP C  1 291 ? -31.962  52.356  -67.590  1.00 28.09  ? 291 TRP C O   1 
ATOM   10783 C CB  . TRP C  1 291 ? -34.204  53.420  -68.750  1.00 31.48  ? 291 TRP C CB  1 
ATOM   10784 C CG  . TRP C  1 291 ? -35.517  53.608  -69.461  1.00 32.61  ? 291 TRP C CG  1 
ATOM   10785 C CD1 . TRP C  1 291 ? -36.450  54.582  -69.244  1.00 31.58  ? 291 TRP C CD1 1 
ATOM   10786 C CD2 . TRP C  1 291 ? -36.002  52.833  -70.578  1.00 32.44  ? 291 TRP C CD2 1 
ATOM   10787 N NE1 . TRP C  1 291 ? -37.499  54.438  -70.106  1.00 31.50  ? 291 TRP C NE1 1 
ATOM   10788 C CE2 . TRP C  1 291 ? -37.252  53.396  -70.947  1.00 31.29  ? 291 TRP C CE2 1 
ATOM   10789 C CE3 . TRP C  1 291 ? -35.502  51.729  -71.288  1.00 31.49  ? 291 TRP C CE3 1 
ATOM   10790 C CZ2 . TRP C  1 291 ? -38.020  52.895  -71.994  1.00 32.54  ? 291 TRP C CZ2 1 
ATOM   10791 C CZ3 . TRP C  1 291 ? -36.276  51.219  -72.313  1.00 32.88  ? 291 TRP C CZ3 1 
ATOM   10792 C CH2 . TRP C  1 291 ? -37.508  51.809  -72.671  1.00 33.10  ? 291 TRP C CH2 1 
ATOM   10793 N N   . PHE C  1 292 ? -32.724  52.381  -65.512  1.00 28.31  ? 292 PHE C N   1 
ATOM   10794 C CA  . PHE C  1 292 ? -31.425  52.198  -64.889  1.00 28.22  ? 292 PHE C CA  1 
ATOM   10795 C C   . PHE C  1 292 ? -31.016  50.744  -64.727  1.00 27.90  ? 292 PHE C C   1 
ATOM   10796 O O   . PHE C  1 292 ? -29.918  50.488  -64.243  1.00 27.68  ? 292 PHE C O   1 
ATOM   10797 C CB  . PHE C  1 292 ? -31.447  52.769  -63.476  1.00 28.87  ? 292 PHE C CB  1 
ATOM   10798 C CG  . PHE C  1 292 ? -30.980  54.204  -63.476  1.00 29.32  ? 292 PHE C CG  1 
ATOM   10799 C CD1 . PHE C  1 292 ? -29.631  54.482  -63.436  1.00 30.93  ? 292 PHE C CD1 1 
ATOM   10800 C CD2 . PHE C  1 292 ? -31.886  55.248  -63.558  1.00 28.69  ? 292 PHE C CD2 1 
ATOM   10801 C CE1 . PHE C  1 292 ? -29.195  55.808  -63.478  1.00 31.71  ? 292 PHE C CE1 1 
ATOM   10802 C CE2 . PHE C  1 292 ? -31.454  56.549  -63.540  1.00 31.28  ? 292 PHE C CE2 1 
ATOM   10803 C CZ  . PHE C  1 292 ? -30.108  56.832  -63.539  1.00 31.28  ? 292 PHE C CZ  1 
ATOM   10804 N N   . GLY C  1 293 ? -31.912  49.812  -65.069  1.00 28.11  ? 293 GLY C N   1 
ATOM   10805 C CA  . GLY C  1 293 ? -31.705  48.414  -64.730  1.00 26.59  ? 293 GLY C CA  1 
ATOM   10806 C C   . GLY C  1 293 ? -30.591  47.798  -65.569  1.00 25.64  ? 293 GLY C C   1 
ATOM   10807 O O   . GLY C  1 293 ? -30.357  48.217  -66.699  1.00 23.80  ? 293 GLY C O   1 
ATOM   10808 N N   . PHE C  1 294 ? -29.931  46.781  -65.000  1.00 25.56  ? 294 PHE C N   1 
ATOM   10809 C CA  . PHE C  1 294 ? -29.140  45.872  -65.802  1.00 25.33  ? 294 PHE C CA  1 
ATOM   10810 C C   . PHE C  1 294 ? -30.070  44.893  -66.519  1.00 26.03  ? 294 PHE C C   1 
ATOM   10811 O O   . PHE C  1 294 ? -29.659  44.261  -67.493  1.00 28.10  ? 294 PHE C O   1 
ATOM   10812 C CB  . PHE C  1 294 ? -28.128  45.210  -64.869  1.00 25.13  ? 294 PHE C CB  1 
ATOM   10813 C CG  . PHE C  1 294 ? -27.059  46.085  -64.236  1.00 24.31  ? 294 PHE C CG  1 
ATOM   10814 C CD1 . PHE C  1 294 ? -27.054  47.473  -64.398  1.00 24.82  ? 294 PHE C CD1 1 
ATOM   10815 C CD2 . PHE C  1 294 ? -26.089  45.512  -63.426  1.00 24.55  ? 294 PHE C CD2 1 
ATOM   10816 C CE1 . PHE C  1 294 ? -26.109  48.262  -63.765  1.00 23.61  ? 294 PHE C CE1 1 
ATOM   10817 C CE2 . PHE C  1 294 ? -25.135  46.307  -62.809  1.00 25.40  ? 294 PHE C CE2 1 
ATOM   10818 C CZ  . PHE C  1 294 ? -25.147  47.691  -62.994  1.00 24.28  ? 294 PHE C CZ  1 
ATOM   10819 N N   . TRP C  1 295 ? -31.278  44.676  -65.978  1.00 25.91  ? 295 TRP C N   1 
ATOM   10820 C CA  . TRP C  1 295 ? -32.275  43.851  -66.649  1.00 27.52  ? 295 TRP C CA  1 
ATOM   10821 C C   . TRP C  1 295 ? -33.432  44.749  -67.088  1.00 28.06  ? 295 TRP C C   1 
ATOM   10822 O O   . TRP C  1 295 ? -33.723  45.751  -66.426  1.00 30.90  ? 295 TRP C O   1 
ATOM   10823 C CB  . TRP C  1 295 ? -32.832  42.719  -65.771  1.00 28.26  ? 295 TRP C CB  1 
ATOM   10824 C CG  . TRP C  1 295 ? -31.909  41.561  -65.517  1.00 27.96  ? 295 TRP C CG  1 
ATOM   10825 C CD1 . TRP C  1 295 ? -30.670  41.625  -64.970  1.00 28.47  ? 295 TRP C CD1 1 
ATOM   10826 C CD2 . TRP C  1 295 ? -32.176  40.160  -65.744  1.00 28.77  ? 295 TRP C CD2 1 
ATOM   10827 N NE1 . TRP C  1 295 ? -30.139  40.367  -64.865  1.00 29.46  ? 295 TRP C NE1 1 
ATOM   10828 C CE2 . TRP C  1 295 ? -31.035  39.450  -65.326  1.00 28.71  ? 295 TRP C CE2 1 
ATOM   10829 C CE3 . TRP C  1 295 ? -33.268  39.426  -66.237  1.00 29.26  ? 295 TRP C CE3 1 
ATOM   10830 C CZ2 . TRP C  1 295 ? -30.951  38.055  -65.384  1.00 29.46  ? 295 TRP C CZ2 1 
ATOM   10831 C CZ3 . TRP C  1 295 ? -33.198  38.046  -66.262  1.00 28.84  ? 295 TRP C CZ3 1 
ATOM   10832 C CH2 . TRP C  1 295 ? -32.061  37.369  -65.844  1.00 28.94  ? 295 TRP C CH2 1 
ATOM   10833 N N   . GLY C  1 296 ? -34.068  44.380  -68.202  1.00 27.00  ? 296 GLY C N   1 
ATOM   10834 C CA  . GLY C  1 296 ? -35.147  45.171  -68.763  1.00 28.59  ? 296 GLY C CA  1 
ATOM   10835 C C   . GLY C  1 296 ? -36.340  44.295  -69.113  1.00 29.37  ? 296 GLY C C   1 
ATOM   10836 O O   . GLY C  1 296 ? -36.172  43.132  -69.478  1.00 30.17  ? 296 GLY C O   1 
ATOM   10837 N N   . TYR C  1 297 ? -37.533  44.887  -69.012  1.00 31.10  ? 297 TYR C N   1 
ATOM   10838 C CA  . TYR C  1 297 ? -38.801  44.197  -69.212  1.00 31.02  ? 297 TYR C CA  1 
ATOM   10839 C C   . TYR C  1 297 ? -39.268  44.447  -70.642  1.00 31.09  ? 297 TYR C C   1 
ATOM   10840 O O   . TYR C  1 297 ? -39.180  45.560  -71.163  1.00 32.45  ? 297 TYR C O   1 
ATOM   10841 C CB  . TYR C  1 297 ? -39.783  44.635  -68.118  1.00 31.60  ? 297 TYR C CB  1 
ATOM   10842 C CG  . TYR C  1 297 ? -39.317  44.196  -66.737  1.00 32.52  ? 297 TYR C CG  1 
ATOM   10843 C CD1 . TYR C  1 297 ? -39.328  42.856  -66.343  1.00 33.97  ? 297 TYR C CD1 1 
ATOM   10844 C CD2 . TYR C  1 297 ? -38.754  45.115  -65.854  1.00 34.25  ? 297 TYR C CD2 1 
ATOM   10845 C CE1 . TYR C  1 297 ? -38.846  42.446  -65.097  1.00 33.00  ? 297 TYR C CE1 1 
ATOM   10846 C CE2 . TYR C  1 297 ? -38.263  44.723  -64.616  1.00 34.01  ? 297 TYR C CE2 1 
ATOM   10847 C CZ  . TYR C  1 297 ? -38.296  43.388  -64.238  1.00 33.03  ? 297 TYR C CZ  1 
ATOM   10848 O OH  . TYR C  1 297 ? -37.852  43.076  -62.990  1.00 30.63  ? 297 TYR C OH  1 
ATOM   10849 N N   . SER C  1 298 ? -39.758  43.379  -71.279  1.00 30.95  ? 298 SER C N   1 
ATOM   10850 C CA  . SER C  1 298 ? -40.258  43.454  -72.643  1.00 30.07  ? 298 SER C CA  1 
ATOM   10851 C C   . SER C  1 298 ? -41.533  44.307  -72.711  1.00 30.27  ? 298 SER C C   1 
ATOM   10852 O O   . SER C  1 298 ? -41.727  45.036  -73.673  1.00 30.92  ? 298 SER C O   1 
ATOM   10853 C CB  . SER C  1 298 ? -40.484  42.063  -73.237  1.00 29.40  ? 298 SER C CB  1 
ATOM   10854 O OG  . SER C  1 298 ? -41.698  41.518  -72.761  1.00 28.38  ? 298 SER C OG  1 
ATOM   10855 N N   . ASP C  1 299 ? -42.384  44.243  -71.684  1.00 31.05  ? 299 ASP C N   1 
ATOM   10856 C CA  . ASP C  1 299 ? -43.717  44.835  -71.753  1.00 32.03  ? 299 ASP C CA  1 
ATOM   10857 C C   . ASP C  1 299 ? -44.311  44.860  -70.348  1.00 32.98  ? 299 ASP C C   1 
ATOM   10858 O O   . ASP C  1 299 ? -43.742  44.273  -69.432  1.00 33.16  ? 299 ASP C O   1 
ATOM   10859 C CB  . ASP C  1 299 ? -44.598  44.065  -72.725  1.00 32.69  ? 299 ASP C CB  1 
ATOM   10860 C CG  . ASP C  1 299 ? -44.608  42.557  -72.462  1.00 34.36  ? 299 ASP C CG  1 
ATOM   10861 O OD1 . ASP C  1 299 ? -45.129  42.158  -71.398  1.00 34.79  ? 299 ASP C OD1 1 
ATOM   10862 O OD2 . ASP C  1 299 ? -44.083  41.786  -73.308  1.00 33.18  ? 299 ASP C OD2 1 
ATOM   10863 N N   . LEU C  1 300 ? -45.498  45.464  -70.226  1.00 35.46  ? 300 LEU C N   1 
ATOM   10864 C CA  . LEU C  1 300 ? -46.288  45.535  -69.005  1.00 37.54  ? 300 LEU C CA  1 
ATOM   10865 C C   . LEU C  1 300 ? -46.524  44.189  -68.311  1.00 38.25  ? 300 LEU C C   1 
ATOM   10866 O O   . LEU C  1 300 ? -46.783  44.168  -67.115  1.00 39.23  ? 300 LEU C O   1 
ATOM   10867 C CB  . LEU C  1 300 ? -47.636  46.132  -69.400  1.00 40.83  ? 300 LEU C CB  1 
ATOM   10868 C CG  . LEU C  1 300 ? -48.647  46.343  -68.266  1.00 44.23  ? 300 LEU C CG  1 
ATOM   10869 C CD1 . LEU C  1 300 ? -47.949  46.968  -67.058  1.00 45.44  ? 300 LEU C CD1 1 
ATOM   10870 C CD2 . LEU C  1 300 ? -49.810  47.245  -68.694  1.00 44.49  ? 300 LEU C CD2 1 
ATOM   10871 N N   . ASN C  1 301 ? -46.524  43.068  -69.037  1.00 37.77  ? 301 ASN C N   1 
ATOM   10872 C CA  . ASN C  1 301 ? -46.867  41.798  -68.431  1.00 37.85  ? 301 ASN C CA  1 
ATOM   10873 C C   . ASN C  1 301 ? -45.625  41.018  -67.994  1.00 38.13  ? 301 ASN C C   1 
ATOM   10874 O O   . ASN C  1 301 ? -45.740  39.920  -67.446  1.00 39.69  ? 301 ASN C O   1 
ATOM   10875 C CB  . ASN C  1 301 ? -47.743  41.015  -69.400  1.00 38.82  ? 301 ASN C CB  1 
ATOM   10876 C CG  . ASN C  1 301 ? -49.063  41.716  -69.615  1.00 39.41  ? 301 ASN C CG  1 
ATOM   10877 O OD1 . ASN C  1 301 ? -49.616  42.293  -68.674  1.00 39.09  ? 301 ASN C OD1 1 
ATOM   10878 N ND2 . ASN C  1 301 ? -49.593  41.682  -70.828  1.00 40.26  ? 301 ASN C ND2 1 
ATOM   10879 N N   . ASP C  1 302 ? -44.435  41.572  -68.222  1.00 36.94  ? 302 ASP C N   1 
ATOM   10880 C CA  . ASP C  1 302 ? -43.203  40.816  -68.041  1.00 37.23  ? 302 ASP C CA  1 
ATOM   10881 C C   . ASP C  1 302 ? -42.802  40.871  -66.578  1.00 36.63  ? 302 ASP C C   1 
ATOM   10882 O O   . ASP C  1 302 ? -42.489  41.922  -66.030  1.00 37.60  ? 302 ASP C O   1 
ATOM   10883 C CB  . ASP C  1 302 ? -42.031  41.374  -68.846  1.00 37.11  ? 302 ASP C CB  1 
ATOM   10884 C CG  . ASP C  1 302 ? -40.796  40.490  -68.941  1.00 35.25  ? 302 ASP C CG  1 
ATOM   10885 O OD1 . ASP C  1 302 ? -40.730  39.514  -68.170  1.00 34.68  ? 302 ASP C OD1 1 
ATOM   10886 O OD2 . ASP C  1 302 ? -39.931  40.784  -69.802  1.00 33.55  ? 302 ASP C OD2 1 
ATOM   10887 N N   . LYS C  1 303 ? -42.738  39.711  -65.963  1.00 36.23  ? 303 LYS C N   1 
ATOM   10888 C CA  . LYS C  1 303 ? -42.326  39.648  -64.582  1.00 35.92  ? 303 LYS C CA  1 
ATOM   10889 C C   . LYS C  1 303 ? -40.859  39.234  -64.482  1.00 32.89  ? 303 LYS C C   1 
ATOM   10890 O O   . LYS C  1 303 ? -40.368  39.148  -63.376  1.00 32.49  ? 303 LYS C O   1 
ATOM   10891 C CB  . LYS C  1 303 ? -43.255  38.624  -63.917  1.00 38.50  ? 303 LYS C CB  1 
ATOM   10892 C CG  . LYS C  1 303 ? -44.711  39.034  -63.787  1.00 39.98  ? 303 LYS C CG  1 
ATOM   10893 C CD  . LYS C  1 303 ? -44.943  40.125  -62.745  1.00 40.61  ? 303 LYS C CD  1 
ATOM   10894 C CE  . LYS C  1 303 ? -46.358  40.203  -62.283  1.00 41.69  ? 303 LYS C CE  1 
ATOM   10895 N NZ  . LYS C  1 303 ? -47.050  40.887  -63.364  1.00 42.26  ? 303 LYS C NZ  1 
ATOM   10896 N N   . TYR C  1 304 ? -40.171  38.989  -65.608  1.00 31.51  ? 304 TYR C N   1 
ATOM   10897 C CA  . TYR C  1 304 ? -38.876  38.317  -65.585  1.00 31.15  ? 304 TYR C CA  1 
ATOM   10898 C C   . TYR C  1 304 ? -37.768  39.220  -66.118  1.00 30.69  ? 304 TYR C C   1 
ATOM   10899 O O   . TYR C  1 304 ? -36.810  39.540  -65.406  1.00 30.23  ? 304 TYR C O   1 
ATOM   10900 C CB  . TYR C  1 304 ? -38.997  36.993  -66.348  1.00 31.37  ? 304 TYR C CB  1 
ATOM   10901 C CG  . TYR C  1 304 ? -39.989  36.096  -65.632  1.00 32.92  ? 304 TYR C CG  1 
ATOM   10902 C CD1 . TYR C  1 304 ? -39.657  35.459  -64.434  1.00 33.43  ? 304 TYR C CD1 1 
ATOM   10903 C CD2 . TYR C  1 304 ? -41.312  35.959  -66.092  1.00 35.56  ? 304 TYR C CD2 1 
ATOM   10904 C CE1 . TYR C  1 304 ? -40.582  34.661  -63.758  1.00 33.43  ? 304 TYR C CE1 1 
ATOM   10905 C CE2 . TYR C  1 304 ? -42.241  35.158  -65.432  1.00 35.55  ? 304 TYR C CE2 1 
ATOM   10906 C CZ  . TYR C  1 304 ? -41.871  34.507  -64.261  1.00 35.49  ? 304 TYR C CZ  1 
ATOM   10907 O OH  . TYR C  1 304 ? -42.803  33.750  -63.591  1.00 37.55  ? 304 TYR C OH  1 
ATOM   10908 N N   . GLY C  1 305 ? -37.919  39.640  -67.374  1.00 30.08  ? 305 GLY C N   1 
ATOM   10909 C CA  . GLY C  1 305 ? -36.921  40.480  -68.013  1.00 28.23  ? 305 GLY C CA  1 
ATOM   10910 C C   . GLY C  1 305 ? -35.776  39.640  -68.582  1.00 27.51  ? 305 GLY C C   1 
ATOM   10911 O O   . GLY C  1 305 ? -35.766  38.400  -68.463  1.00 26.74  ? 305 GLY C O   1 
ATOM   10912 N N   . THR C  1 306 ? -34.846  40.349  -69.236  1.00 26.82  ? 306 THR C N   1 
ATOM   10913 C CA  . THR C  1 306 ? -33.628  39.773  -69.782  1.00 26.93  ? 306 THR C CA  1 
ATOM   10914 C C   . THR C  1 306 ? -32.476  40.746  -69.562  1.00 27.27  ? 306 THR C C   1 
ATOM   10915 O O   . THR C  1 306 ? -32.644  41.954  -69.541  1.00 29.28  ? 306 THR C O   1 
ATOM   10916 C CB  . THR C  1 306 ? -33.798  39.418  -71.258  1.00 26.64  ? 306 THR C CB  1 
ATOM   10917 O OG1 . THR C  1 306 ? -33.934  40.639  -71.981  1.00 25.34  ? 306 THR C OG1 1 
ATOM   10918 C CG2 . THR C  1 306 ? -34.962  38.469  -71.532  1.00 26.18  ? 306 THR C CG2 1 
ATOM   10919 N N   . PRO C  1 307 ? -31.259  40.245  -69.319  1.00 28.15  ? 307 PRO C N   1 
ATOM   10920 C CA  . PRO C  1 307 ? -30.126  41.125  -69.036  1.00 27.42  ? 307 PRO C CA  1 
ATOM   10921 C C   . PRO C  1 307 ? -29.689  42.009  -70.201  1.00 26.67  ? 307 PRO C C   1 
ATOM   10922 O O   . PRO C  1 307 ? -29.707  41.598  -71.346  1.00 26.98  ? 307 PRO C O   1 
ATOM   10923 C CB  . PRO C  1 307 ? -29.008  40.126  -68.592  1.00 27.43  ? 307 PRO C CB  1 
ATOM   10924 C CG  . PRO C  1 307 ? -29.417  38.780  -69.213  1.00 27.72  ? 307 PRO C CG  1 
ATOM   10925 C CD  . PRO C  1 307 ? -30.928  38.807  -69.260  1.00 29.01  ? 307 PRO C CD  1 
ATOM   10926 N N   . ARG C  1 308 ? -29.250  43.228  -69.895  1.00 25.83  ? 308 ARG C N   1 
ATOM   10927 C CA  . ARG C  1 308 ? -28.598  44.055  -70.893  1.00 26.02  ? 308 ARG C CA  1 
ATOM   10928 C C   . ARG C  1 308 ? -27.092  43.767  -70.898  1.00 27.11  ? 308 ARG C C   1 
ATOM   10929 O O   . ARG C  1 308 ? -26.568  43.097  -69.984  1.00 26.28  ? 308 ARG C O   1 
ATOM   10930 C CB  . ARG C  1 308 ? -28.925  45.522  -70.595  1.00 26.00  ? 308 ARG C CB  1 
ATOM   10931 C CG  . ARG C  1 308 ? -30.413  45.815  -70.648  1.00 27.13  ? 308 ARG C CG  1 
ATOM   10932 C CD  . ARG C  1 308 ? -30.656  47.237  -70.214  1.00 26.36  ? 308 ARG C CD  1 
ATOM   10933 N NE  . ARG C  1 308 ? -32.055  47.593  -70.422  1.00 26.55  ? 308 ARG C NE  1 
ATOM   10934 C CZ  . ARG C  1 308 ? -32.798  48.419  -69.662  1.00 27.90  ? 308 ARG C CZ  1 
ATOM   10935 N NH1 . ARG C  1 308 ? -32.361  48.865  -68.493  1.00 28.12  ? 308 ARG C NH1 1 
ATOM   10936 N NH2 . ARG C  1 308 ? -34.020  48.762  -70.068  1.00 27.60  ? 308 ARG C NH2 1 
ATOM   10937 N N   . PRO C  1 309 ? -26.353  44.265  -71.934  1.00 27.55  ? 309 PRO C N   1 
ATOM   10938 C CA  . PRO C  1 309 ? -24.915  43.970  -72.077  1.00 26.57  ? 309 PRO C CA  1 
ATOM   10939 C C   . PRO C  1 309 ? -24.097  44.298  -70.836  1.00 27.64  ? 309 PRO C C   1 
ATOM   10940 O O   . PRO C  1 309 ? -23.184  43.544  -70.487  1.00 26.91  ? 309 PRO C O   1 
ATOM   10941 C CB  . PRO C  1 309 ? -24.508  44.746  -73.310  1.00 26.13  ? 309 PRO C CB  1 
ATOM   10942 C CG  . PRO C  1 309 ? -25.809  44.721  -74.144  1.00 27.99  ? 309 PRO C CG  1 
ATOM   10943 C CD  . PRO C  1 309 ? -26.904  44.957  -73.118  1.00 26.96  ? 309 PRO C CD  1 
ATOM   10944 N N   . VAL C  1 310 ? -24.505  45.358  -70.119  1.00 25.88  ? 310 VAL C N   1 
ATOM   10945 C CA  . VAL C  1 310 ? -23.878  45.728  -68.857  1.00 25.36  ? 310 VAL C CA  1 
ATOM   10946 C C   . VAL C  1 310 ? -23.775  44.519  -67.915  1.00 26.92  ? 310 VAL C C   1 
ATOM   10947 O O   . VAL C  1 310 ? -22.789  44.337  -67.205  1.00 28.40  ? 310 VAL C O   1 
ATOM   10948 C CB  . VAL C  1 310 ? -24.616  46.927  -68.218  1.00 25.46  ? 310 VAL C CB  1 
ATOM   10949 C CG1 . VAL C  1 310 ? -26.087  46.673  -67.917  1.00 26.05  ? 310 VAL C CG1 1 
ATOM   10950 C CG2 . VAL C  1 310 ? -23.925  47.402  -66.953  1.00 26.12  ? 310 VAL C CG2 1 
ATOM   10951 N N   . TRP C  1 311 ? -24.807  43.679  -67.883  1.00 27.18  ? 311 TRP C N   1 
ATOM   10952 C CA  . TRP C  1 311 ? -24.811  42.535  -66.983  1.00 28.15  ? 311 TRP C CA  1 
ATOM   10953 C C   . TRP C  1 311 ? -23.571  41.659  -67.149  1.00 25.56  ? 311 TRP C C   1 
ATOM   10954 O O   . TRP C  1 311 ? -22.999  41.211  -66.170  1.00 24.54  ? 311 TRP C O   1 
ATOM   10955 C CB  . TRP C  1 311 ? -26.084  41.728  -67.260  1.00 29.33  ? 311 TRP C CB  1 
ATOM   10956 C CG  . TRP C  1 311 ? -26.312  40.573  -66.344  1.00 28.29  ? 311 TRP C CG  1 
ATOM   10957 C CD1 . TRP C  1 311 ? -26.167  39.261  -66.669  1.00 27.51  ? 311 TRP C CD1 1 
ATOM   10958 C CD2 . TRP C  1 311 ? -26.752  40.621  -64.971  1.00 30.59  ? 311 TRP C CD2 1 
ATOM   10959 N NE1 . TRP C  1 311 ? -26.499  38.483  -65.595  1.00 28.37  ? 311 TRP C NE1 1 
ATOM   10960 C CE2 . TRP C  1 311 ? -26.856  39.277  -64.540  1.00 30.29  ? 311 TRP C CE2 1 
ATOM   10961 C CE3 . TRP C  1 311 ? -27.068  41.644  -64.071  1.00 29.09  ? 311 TRP C CE3 1 
ATOM   10962 C CZ2 . TRP C  1 311 ? -27.267  38.942  -63.259  1.00 29.82  ? 311 TRP C CZ2 1 
ATOM   10963 C CZ3 . TRP C  1 311 ? -27.467  41.305  -62.797  1.00 29.30  ? 311 TRP C CZ3 1 
ATOM   10964 C CH2 . TRP C  1 311 ? -27.585  39.980  -62.409  1.00 29.99  ? 311 TRP C CH2 1 
ATOM   10965 N N   . PHE C  1 312 ? -23.236  41.390  -68.407  1.00 27.25  ? 312 PHE C N   1 
ATOM   10966 C CA  . PHE C  1 312 ? -22.150  40.511  -68.804  1.00 29.48  ? 312 PHE C CA  1 
ATOM   10967 C C   . PHE C  1 312 ? -20.817  41.210  -68.545  1.00 28.66  ? 312 PHE C C   1 
ATOM   10968 O O   . PHE C  1 312 ? -19.891  40.590  -68.008  1.00 27.23  ? 312 PHE C O   1 
ATOM   10969 C CB  . PHE C  1 312 ? -22.444  40.025  -70.231  1.00 29.22  ? 312 PHE C CB  1 
ATOM   10970 C CG  . PHE C  1 312 ? -23.742  39.228  -70.288  1.00 31.21  ? 312 PHE C CG  1 
ATOM   10971 C CD1 . PHE C  1 312 ? -23.805  37.904  -69.824  1.00 34.79  ? 312 PHE C CD1 1 
ATOM   10972 C CD2 . PHE C  1 312 ? -24.916  39.803  -70.756  1.00 31.35  ? 312 PHE C CD2 1 
ATOM   10973 C CE1 . PHE C  1 312 ? -25.024  37.198  -69.820  1.00 34.46  ? 312 PHE C CE1 1 
ATOM   10974 C CE2 . PHE C  1 312 ? -26.119  39.092  -70.768  1.00 31.79  ? 312 PHE C CE2 1 
ATOM   10975 C CZ  . PHE C  1 312 ? -26.184  37.798  -70.280  1.00 31.25  ? 312 PHE C CZ  1 
ATOM   10976 N N   . ALA C  1 313 ? -20.760  42.519  -68.818  1.00 29.30  ? 313 ALA C N   1 
ATOM   10977 C CA  . ALA C  1 313 ? -19.510  43.264  -68.635  1.00 30.69  ? 313 ALA C CA  1 
ATOM   10978 C C   . ALA C  1 313 ? -19.180  43.310  -67.150  1.00 28.84  ? 313 ALA C C   1 
ATOM   10979 O O   . ALA C  1 313 ? -18.030  43.087  -66.782  1.00 28.50  ? 313 ALA C O   1 
ATOM   10980 C CB  . ALA C  1 313 ? -19.548  44.670  -69.258  1.00 31.85  ? 313 ALA C CB  1 
ATOM   10981 N N   . MET C  1 314 ? -20.207  43.542  -66.319  1.00 28.70  ? 314 MET C N   1 
ATOM   10982 C CA  . MET C  1 314 ? -20.050  43.573  -64.864  1.00 28.59  ? 314 MET C CA  1 
ATOM   10983 C C   . MET C  1 314 ? -19.605  42.210  -64.321  1.00 28.47  ? 314 MET C C   1 
ATOM   10984 O O   . MET C  1 314 ? -18.599  42.098  -63.635  1.00 30.52  ? 314 MET C O   1 
ATOM   10985 C CB  . MET C  1 314 ? -21.331  44.050  -64.182  1.00 27.52  ? 314 MET C CB  1 
ATOM   10986 C CG  . MET C  1 314 ? -21.598  45.547  -64.361  1.00 29.24  ? 314 MET C CG  1 
ATOM   10987 S SD  . MET C  1 314 ? -20.447  46.563  -63.414  1.00 31.76  ? 314 MET C SD  1 
ATOM   10988 C CE  . MET C  1 314 ? -21.039  45.972  -61.819  1.00 30.86  ? 314 MET C CE  1 
ATOM   10989 N N   . ARG C  1 315 ? -20.338  41.158  -64.647  1.00 28.26  ? 315 ARG C N   1 
ATOM   10990 C CA  . ARG C  1 315 ? -19.947  39.836  -64.236  1.00 28.22  ? 315 ARG C CA  1 
ATOM   10991 C C   . ARG C  1 315 ? -18.487  39.557  -64.590  1.00 26.85  ? 315 ARG C C   1 
ATOM   10992 O O   . ARG C  1 315 ? -17.740  39.024  -63.774  1.00 25.38  ? 315 ARG C O   1 
ATOM   10993 C CB  . ARG C  1 315 ? -20.811  38.818  -64.982  1.00 29.29  ? 315 ARG C CB  1 
ATOM   10994 C CG  . ARG C  1 315 ? -20.464  37.397  -64.563  1.00 30.47  ? 315 ARG C CG  1 
ATOM   10995 C CD  . ARG C  1 315 ? -21.111  36.403  -65.468  1.00 31.68  ? 315 ARG C CD  1 
ATOM   10996 N NE  . ARG C  1 315 ? -20.609  36.527  -66.844  1.00 34.05  ? 315 ARG C NE  1 
ATOM   10997 C CZ  . ARG C  1 315 ? -21.142  35.882  -67.876  1.00 34.09  ? 315 ARG C CZ  1 
ATOM   10998 N NH1 . ARG C  1 315 ? -22.188  35.084  -67.693  1.00 35.18  ? 315 ARG C NH1 1 
ATOM   10999 N NH2 . ARG C  1 315 ? -20.653  36.064  -69.081  1.00 33.47  ? 315 ARG C NH2 1 
ATOM   11000 N N   . ASP C  1 316 ? -18.100  39.798  -65.841  1.00 27.53  ? 316 ASP C N   1 
ATOM   11001 C CA  . ASP C  1 316 ? -16.728  39.493  -66.242  1.00 29.63  ? 316 ASP C CA  1 
ATOM   11002 C C   . ASP C  1 316 ? -15.747  40.387  -65.501  1.00 28.65  ? 316 ASP C C   1 
ATOM   11003 O O   . ASP C  1 316 ? -14.692  39.905  -65.096  1.00 28.69  ? 316 ASP C O   1 
ATOM   11004 C CB  . ASP C  1 316 ? -16.501  39.614  -67.738  1.00 31.14  ? 316 ASP C CB  1 
ATOM   11005 C CG  . ASP C  1 316 ? -17.242  38.602  -68.603  1.00 33.27  ? 316 ASP C CG  1 
ATOM   11006 O OD1 . ASP C  1 316 ? -17.877  37.650  -68.072  1.00 32.70  ? 316 ASP C OD1 1 
ATOM   11007 O OD2 . ASP C  1 316 ? -17.210  38.810  -69.815  1.00 40.85  ? 316 ASP C OD2 1 
ATOM   11008 N N   . TYR C  1 317 ? -16.131  41.657  -65.271  1.00 25.93  ? 317 TYR C N   1 
ATOM   11009 C CA  . TYR C  1 317 ? -15.258  42.602  -64.599  1.00 26.96  ? 317 TYR C CA  1 
ATOM   11010 C C   . TYR C  1 317 ? -15.040  42.201  -63.144  1.00 28.37  ? 317 TYR C C   1 
ATOM   11011 O O   . TYR C  1 317 ? -13.948  42.386  -62.591  1.00 31.45  ? 317 TYR C O   1 
ATOM   11012 C CB  . TYR C  1 317 ? -15.757  44.051  -64.720  1.00 27.75  ? 317 TYR C CB  1 
ATOM   11013 C CG  . TYR C  1 317 ? -14.785  45.041  -64.124  1.00 25.61  ? 317 TYR C CG  1 
ATOM   11014 C CD1 . TYR C  1 317 ? -13.710  45.528  -64.855  1.00 27.68  ? 317 TYR C CD1 1 
ATOM   11015 C CD2 . TYR C  1 317 ? -14.928  45.479  -62.829  1.00 27.27  ? 317 TYR C CD2 1 
ATOM   11016 C CE1 . TYR C  1 317 ? -12.801  46.439  -64.313  1.00 27.66  ? 317 TYR C CE1 1 
ATOM   11017 C CE2 . TYR C  1 317 ? -14.031  46.399  -62.280  1.00 29.33  ? 317 TYR C CE2 1 
ATOM   11018 C CZ  . TYR C  1 317 ? -12.965  46.882  -63.016  1.00 27.00  ? 317 TYR C CZ  1 
ATOM   11019 O OH  . TYR C  1 317 ? -12.087  47.738  -62.412  1.00 27.33  ? 317 TYR C OH  1 
ATOM   11020 N N   . MET C  1 318 ? -16.044  41.606  -62.511  1.00 27.75  ? 318 MET C N   1 
ATOM   11021 C CA  . MET C  1 318 ? -15.935  41.298  -61.093  1.00 27.45  ? 318 MET C CA  1 
ATOM   11022 C C   . MET C  1 318 ? -15.058  40.080  -60.802  1.00 27.23  ? 318 MET C C   1 
ATOM   11023 O O   . MET C  1 318 ? -14.739  39.827  -59.645  1.00 27.04  ? 318 MET C O   1 
ATOM   11024 C CB  . MET C  1 318 ? -17.329  41.105  -60.493  1.00 29.66  ? 318 MET C CB  1 
ATOM   11025 C CG  . MET C  1 318 ? -18.121  42.405  -60.397  1.00 31.20  ? 318 MET C CG  1 
ATOM   11026 S SD  . MET C  1 318 ? -19.609  42.273  -59.385  1.00 30.10  ? 318 MET C SD  1 
ATOM   11027 C CE  . MET C  1 318 ? -20.602  41.287  -60.521  1.00 31.23  ? 318 MET C CE  1 
ATOM   11028 N N   . LYS C  1 319 ? -14.674  39.290  -61.808  1.00 28.40  ? 319 LYS C N   1 
ATOM   11029 C CA  . LYS C  1 319 ? -13.975  38.049  -61.502  1.00 31.16  ? 319 LYS C CA  1 
ATOM   11030 C C   . LYS C  1 319 ? -12.650  38.292  -60.773  1.00 31.98  ? 319 LYS C C   1 
ATOM   11031 O O   . LYS C  1 319 ? -12.237  37.469  -59.960  1.00 32.57  ? 319 LYS C O   1 
ATOM   11032 C CB  . LYS C  1 319 ? -13.735  37.242  -62.774  1.00 35.08  ? 319 LYS C CB  1 
ATOM   11033 C CG  . LYS C  1 319 ? -15.018  36.630  -63.388  1.00 37.92  ? 319 LYS C CG  1 
ATOM   11034 C CD  . LYS C  1 319 ? -14.646  35.916  -64.690  1.00 42.95  ? 319 LYS C CD  1 
ATOM   11035 C CE  . LYS C  1 319 ? -15.741  35.295  -65.536  1.00 47.34  ? 319 LYS C CE  1 
ATOM   11036 N NZ  . LYS C  1 319 ? -15.208  34.961  -66.871  1.00 47.39  ? 319 LYS C NZ  1 
ATOM   11037 N N   . GLY C  1 320 ? -11.984  39.420  -61.053  1.00 29.73  ? 320 GLY C N   1 
ATOM   11038 C CA  . GLY C  1 320 ? -10.706  39.729  -60.434  1.00 30.16  ? 320 GLY C CA  1 
ATOM   11039 C C   . GLY C  1 320 ? -10.582  41.244  -60.296  1.00 32.44  ? 320 GLY C C   1 
ATOM   11040 O O   . GLY C  1 320 ? -10.569  41.968  -61.308  1.00 31.90  ? 320 GLY C O   1 
ATOM   11041 N N   . LEU C  1 321 ? -10.616  41.728  -59.048  1.00 30.70  ? 321 LEU C N   1 
ATOM   11042 C CA  . LEU C  1 321 ? -10.605  43.157  -58.800  1.00 30.07  ? 321 LEU C CA  1 
ATOM   11043 C C   . LEU C  1 321 ? -9.202   43.613  -58.378  1.00 31.13  ? 321 LEU C C   1 
ATOM   11044 O O   . LEU C  1 321 ? -8.586   42.992  -57.507  1.00 28.64  ? 321 LEU C O   1 
ATOM   11045 C CB  . LEU C  1 321 ? -11.633  43.431  -57.718  1.00 30.19  ? 321 LEU C CB  1 
ATOM   11046 C CG  . LEU C  1 321 ? -13.093  43.275  -58.161  1.00 30.97  ? 321 LEU C CG  1 
ATOM   11047 C CD1 . LEU C  1 321 ? -13.973  43.552  -56.960  1.00 31.77  ? 321 LEU C CD1 1 
ATOM   11048 C CD2 . LEU C  1 321 ? -13.468  44.202  -59.313  1.00 30.60  ? 321 LEU C CD2 1 
ATOM   11049 N N   . ILE C  1 322 ? -8.746   44.734  -58.967  1.00 30.50  ? 322 ILE C N   1 
ATOM   11050 C CA  . ILE C  1 322 ? -7.493   45.370  -58.601  1.00 30.59  ? 322 ILE C CA  1 
ATOM   11051 C C   . ILE C  1 322 ? -7.838   46.534  -57.683  1.00 31.13  ? 322 ILE C C   1 
ATOM   11052 O O   . ILE C  1 322 ? -8.449   47.500  -58.127  1.00 32.32  ? 322 ILE C O   1 
ATOM   11053 C CB  . ILE C  1 322 ? -6.691   45.837  -59.843  1.00 30.50  ? 322 ILE C CB  1 
ATOM   11054 C CG1 . ILE C  1 322 ? -6.591   44.759  -60.938  1.00 30.32  ? 322 ILE C CG1 1 
ATOM   11055 C CG2 . ILE C  1 322 ? -5.304   46.319  -59.435  1.00 30.41  ? 322 ILE C CG2 1 
ATOM   11056 C CD1 . ILE C  1 322 ? -5.964   45.207  -62.257  1.00 29.53  ? 322 ILE C CD1 1 
ATOM   11057 N N   . ILE C  1 323 ? -7.426   46.442  -56.411  1.00 31.62  ? 323 ILE C N   1 
ATOM   11058 C CA  . ILE C  1 323 ? -7.627   47.524  -55.463  1.00 30.97  ? 323 ILE C CA  1 
ATOM   11059 C C   . ILE C  1 323 ? -6.416   48.454  -55.416  1.00 31.23  ? 323 ILE C C   1 
ATOM   11060 O O   . ILE C  1 323 ? -6.588   49.669  -55.252  1.00 32.23  ? 323 ILE C O   1 
ATOM   11061 C CB  . ILE C  1 323 ? -7.971   47.003  -54.062  1.00 31.38  ? 323 ILE C CB  1 
ATOM   11062 C CG1 . ILE C  1 323 ? -9.447   46.593  -53.954  1.00 32.70  ? 323 ILE C CG1 1 
ATOM   11063 C CG2 . ILE C  1 323 ? -7.642   48.051  -53.000  1.00 32.04  ? 323 ILE C CG2 1 
ATOM   11064 C CD1 . ILE C  1 323 ? -9.744   45.198  -54.460  1.00 33.19  ? 323 ILE C CD1 1 
ATOM   11065 N N   . SER C  1 324 ? -5.222   47.859  -55.433  1.00 30.15  ? 324 SER C N   1 
ATOM   11066 C CA  . SER C  1 324 ? -3.965   48.577  -55.505  1.00 30.99  ? 324 SER C CA  1 
ATOM   11067 C C   . SER C  1 324 ? -3.054   47.806  -56.457  1.00 31.91  ? 324 SER C C   1 
ATOM   11068 O O   . SER C  1 324 ? -3.113   46.578  -56.431  1.00 30.30  ? 324 SER C O   1 
ATOM   11069 C CB  . SER C  1 324 ? -3.322   48.738  -54.150  1.00 31.16  ? 324 SER C CB  1 
ATOM   11070 O OG  . SER C  1 324 ? -4.188   49.448  -53.280  1.00 30.16  ? 324 SER C OG  1 
ATOM   11071 N N   . PRO C  1 325 ? -2.244   48.464  -57.335  1.00 32.55  ? 325 PRO C N   1 
ATOM   11072 C CA  . PRO C  1 325 ? -2.180   49.926  -57.430  1.00 32.45  ? 325 PRO C CA  1 
ATOM   11073 C C   . PRO C  1 325 ? -3.443   50.510  -58.047  1.00 31.64  ? 325 PRO C C   1 
ATOM   11074 O O   . PRO C  1 325 ? -4.165   49.807  -58.755  1.00 30.49  ? 325 PRO C O   1 
ATOM   11075 C CB  . PRO C  1 325 ? -0.960   50.212  -58.322  1.00 32.26  ? 325 PRO C CB  1 
ATOM   11076 C CG  . PRO C  1 325 ? -0.777   48.953  -59.136  1.00 32.30  ? 325 PRO C CG  1 
ATOM   11077 C CD  . PRO C  1 325 ? -1.362   47.810  -58.320  1.00 32.97  ? 325 PRO C CD  1 
ATOM   11078 N N   . LYS C  1 326 ? -3.643   51.820  -57.844  1.00 32.23  ? 326 LYS C N   1 
ATOM   11079 C CA  . LYS C  1 326 ? -4.840   52.495  -58.324  1.00 31.73  ? 326 LYS C CA  1 
ATOM   11080 C C   . LYS C  1 326 ? -4.586   53.168  -59.666  1.00 30.16  ? 326 LYS C C   1 
ATOM   11081 O O   . LYS C  1 326 ? -3.516   53.720  -59.888  1.00 28.56  ? 326 LYS C O   1 
ATOM   11082 C CB  . LYS C  1 326 ? -5.294   53.486  -57.247  1.00 33.74  ? 326 LYS C CB  1 
ATOM   11083 C CG  . LYS C  1 326 ? -5.757   52.799  -55.988  1.00 34.42  ? 326 LYS C CG  1 
ATOM   11084 C CD  . LYS C  1 326 ? -6.225   53.702  -54.867  1.00 35.08  ? 326 LYS C CD  1 
ATOM   11085 C CE  . LYS C  1 326 ? -6.990   52.922  -53.857  1.00 35.80  ? 326 LYS C CE  1 
ATOM   11086 N NZ  . LYS C  1 326 ? -6.320   51.669  -53.473  1.00 36.55  ? 326 LYS C NZ  1 
ATOM   11087 N N   . ASN C  1 327 ? -5.615   53.164  -60.526  1.00 30.20  ? 327 ASN C N   1 
ATOM   11088 C CA  . ASN C  1 327 ? -5.544   53.867  -61.794  1.00 32.49  ? 327 ASN C CA  1 
ATOM   11089 C C   . ASN C  1 327 ? -5.389   55.374  -61.548  1.00 31.45  ? 327 ASN C C   1 
ATOM   11090 O O   . ASN C  1 327 ? -6.045   55.943  -60.691  1.00 29.20  ? 327 ASN C O   1 
ATOM   11091 C CB  . ASN C  1 327 ? -6.710   53.500  -62.690  1.00 33.02  ? 327 ASN C CB  1 
ATOM   11092 C CG  . ASN C  1 327 ? -6.577   54.058  -64.089  1.00 33.18  ? 327 ASN C CG  1 
ATOM   11093 O OD1 . ASN C  1 327 ? -5.593   53.792  -64.808  1.00 32.61  ? 327 ASN C OD1 1 
ATOM   11094 N ND2 . ASN C  1 327 ? -7.616   54.765  -64.503  1.00 31.66  ? 327 ASN C ND2 1 
ATOM   11095 N N   . LYS C  1 328 ? -4.400   55.954  -62.244  1.00 33.07  ? 328 LYS C N   1 
ATOM   11096 C CA  . LYS C  1 328 ? -4.062   57.373  -62.215  1.00 33.42  ? 328 LYS C CA  1 
ATOM   11097 C C   . LYS C  1 328 ? -3.421   57.733  -60.882  1.00 31.57  ? 328 LYS C C   1 
ATOM   11098 O O   . LYS C  1 328 ? -3.538   58.856  -60.439  1.00 30.88  ? 328 LYS C O   1 
ATOM   11099 C CB  . LYS C  1 328 ? -5.265   58.273  -62.560  1.00 33.50  ? 328 LYS C CB  1 
ATOM   11100 C CG  . LYS C  1 328 ? -5.904   58.000  -63.925  1.00 33.45  ? 328 LYS C CG  1 
ATOM   11101 C CD  . LYS C  1 328 ? -4.914   58.094  -65.091  1.00 34.70  ? 328 LYS C CD  1 
ATOM   11102 C CE  . LYS C  1 328 ? -5.426   57.696  -66.443  1.00 33.31  ? 328 LYS C CE  1 
ATOM   11103 N NZ  . LYS C  1 328 ? -6.440   58.644  -66.896  1.00 34.79  ? 328 LYS C NZ  1 
ATOM   11104 N N   . SER C  1 329 ? -2.728   56.775  -60.273  1.00 31.30  ? 329 SER C N   1 
ATOM   11105 C CA  . SER C  1 329 ? -1.979   57.009  -59.056  1.00 31.72  ? 329 SER C CA  1 
ATOM   11106 C C   . SER C  1 329 ? -0.549   57.425  -59.396  1.00 32.41  ? 329 SER C C   1 
ATOM   11107 O O   . SER C  1 329 ? -0.013   57.061  -60.442  1.00 31.93  ? 329 SER C O   1 
ATOM   11108 C CB  . SER C  1 329 ? -1.971   55.778  -58.193  1.00 32.34  ? 329 SER C CB  1 
ATOM   11109 O OG  . SER C  1 329 ? -1.437   54.673  -58.913  1.00 31.14  ? 329 SER C OG  1 
ATOM   11110 N N   . ILE C  1 330 ? 0.073    58.174  -58.481  1.00 33.48  ? 330 ILE C N   1 
ATOM   11111 C CA  . ILE C  1 330 ? 1.441    58.651  -58.657  1.00 35.64  ? 330 ILE C CA  1 
ATOM   11112 C C   . ILE C  1 330 ? 2.309    57.965  -57.606  1.00 36.82  ? 330 ILE C C   1 
ATOM   11113 O O   . ILE C  1 330 ? 1.894    57.820  -56.471  1.00 39.15  ? 330 ILE C O   1 
ATOM   11114 C CB  . ILE C  1 330 ? 1.500    60.195  -58.591  1.00 35.93  ? 330 ILE C CB  1 
ATOM   11115 C CG1 . ILE C  1 330 ? 0.532    60.790  -59.620  1.00 35.15  ? 330 ILE C CG1 1 
ATOM   11116 C CG2 . ILE C  1 330 ? 2.932    60.699  -58.773  1.00 37.04  ? 330 ILE C CG2 1 
ATOM   11117 C CD1 . ILE C  1 330 ? 0.368    62.287  -59.570  1.00 36.02  ? 330 ILE C CD1 1 
ATOM   11118 N N   . HIS C  1 331 ? 3.484    57.474  -57.997  1.00 37.35  ? 331 HIS C N   1 
ATOM   11119 C CA  . HIS C  1 331 ? 4.298    56.660  -57.122  1.00 36.99  ? 331 HIS C CA  1 
ATOM   11120 C C   . HIS C  1 331 ? 5.743    57.120  -57.241  1.00 38.61  ? 331 HIS C C   1 
ATOM   11121 O O   . HIS C  1 331 ? 6.266    57.191  -58.348  1.00 39.69  ? 331 HIS C O   1 
ATOM   11122 C CB  . HIS C  1 331 ? 4.170    55.194  -57.547  1.00 36.61  ? 331 HIS C CB  1 
ATOM   11123 C CG  . HIS C  1 331 ? 2.902    54.540  -57.125  1.00 35.03  ? 331 HIS C CG  1 
ATOM   11124 N ND1 . HIS C  1 331 ? 1.760    54.485  -57.902  1.00 34.60  ? 331 HIS C ND1 1 
ATOM   11125 C CD2 . HIS C  1 331 ? 2.619    53.933  -55.988  1.00 34.69  ? 331 HIS C CD2 1 
ATOM   11126 C CE1 . HIS C  1 331 ? 0.807    53.868  -57.226  1.00 33.71  ? 331 HIS C CE1 1 
ATOM   11127 N NE2 . HIS C  1 331 ? 1.320    53.521  -56.067  1.00 35.15  ? 331 HIS C NE2 1 
ATOM   11128 N N   . THR C  1 332 ? 6.394    57.387  -56.107  1.00 40.16  ? 332 THR C N   1 
ATOM   11129 C CA  . THR C  1 332 ? 7.805    57.718  -56.131  1.00 41.22  ? 332 THR C CA  1 
ATOM   11130 C C   . THR C  1 332 ? 8.588    56.608  -55.444  1.00 44.09  ? 332 THR C C   1 
ATOM   11131 O O   . THR C  1 332 ? 9.666    56.804  -54.906  1.00 47.09  ? 332 THR C O   1 
ATOM   11132 C CB  . THR C  1 332 ? 8.048    59.099  -55.528  1.00 41.59  ? 332 THR C CB  1 
ATOM   11133 O OG1 . THR C  1 332 ? 7.496    59.044  -54.220  1.00 42.98  ? 332 THR C OG1 1 
ATOM   11134 C CG2 . THR C  1 332 ? 7.430    60.208  -56.356  1.00 40.21  ? 332 THR C CG2 1 
ATOM   11135 N N   . ASN C  1 333 ? 8.085    55.394  -55.545  1.00 46.39  ? 333 ASN C N   1 
ATOM   11136 C CA  . ASN C  1 333 ? 8.713    54.285  -54.877  1.00 47.54  ? 333 ASN C CA  1 
ATOM   11137 C C   . ASN C  1 333 ? 8.878    53.203  -55.932  1.00 47.10  ? 333 ASN C C   1 
ATOM   11138 O O   . ASN C  1 333 ? 8.022    53.106  -56.795  1.00 45.00  ? 333 ASN C O   1 
ATOM   11139 C CB  . ASN C  1 333 ? 7.878    53.901  -53.666  1.00 49.60  ? 333 ASN C CB  1 
ATOM   11140 C CG  . ASN C  1 333 ? 8.756    53.276  -52.624  1.00 55.59  ? 333 ASN C CG  1 
ATOM   11141 O OD1 . ASN C  1 333 ? 9.105    52.091  -52.738  1.00 57.22  ? 333 ASN C OD1 1 
ATOM   11142 N ND2 . ASN C  1 333 ? 9.173    54.075  -51.648  1.00 61.61  ? 333 ASN C ND2 1 
ATOM   11143 N N   . THR C  1 334 ? 9.965    52.417  -55.872  1.00 47.25  ? 334 THR C N   1 
ATOM   11144 C CA  . THR C  1 334 ? 10.138   51.299  -56.788  1.00 46.35  ? 334 THR C CA  1 
ATOM   11145 C C   . THR C  1 334 ? 9.301    50.096  -56.346  1.00 47.41  ? 334 THR C C   1 
ATOM   11146 O O   . THR C  1 334 ? 9.043    49.228  -57.160  1.00 46.40  ? 334 THR C O   1 
ATOM   11147 C CB  . THR C  1 334 ? 11.602   50.911  -56.957  1.00 46.90  ? 334 THR C CB  1 
ATOM   11148 O OG1 . THR C  1 334 ? 12.023   50.429  -55.685  1.00 47.99  ? 334 THR C OG1 1 
ATOM   11149 C CG2 . THR C  1 334 ? 12.471   52.054  -57.457  1.00 48.53  ? 334 THR C CG2 1 
ATOM   11150 N N   . LYS C  1 335 ? 8.850    50.043  -55.087  1.00 51.09  ? 335 LYS C N   1 
ATOM   11151 C CA  . LYS C  1 335 ? 7.971    48.975  -54.631  1.00 53.26  ? 335 LYS C CA  1 
ATOM   11152 C C   . LYS C  1 335 ? 6.547    49.500  -54.558  1.00 54.15  ? 335 LYS C C   1 
ATOM   11153 O O   . LYS C  1 335 ? 6.296    50.449  -53.828  1.00 64.92  ? 335 LYS C O   1 
ATOM   11154 C CB  . LYS C  1 335 ? 8.368    48.466  -53.245  1.00 57.93  ? 335 LYS C CB  1 
ATOM   11155 C CG  . LYS C  1 335 ? 9.747    47.826  -53.154  1.00 64.30  ? 335 LYS C CG  1 
ATOM   11156 C CD  . LYS C  1 335 ? 9.931    46.575  -54.014  1.00 71.01  ? 335 LYS C CD  1 
ATOM   11157 C CE  . LYS C  1 335 ? 10.992   45.616  -53.524  1.00 73.37  ? 335 LYS C CE  1 
ATOM   11158 N NZ  . LYS C  1 335 ? 12.229   46.319  -53.173  1.00 75.19  ? 335 LYS C NZ  1 
ATOM   11159 N N   . ILE C  1 336 ? 5.646    48.899  -55.341  1.00 51.92  ? 336 ILE C N   1 
ATOM   11160 C CA  . ILE C  1 336 ? 4.259    49.329  -55.433  1.00 51.62  ? 336 ILE C CA  1 
ATOM   11161 C C   . ILE C  1 336 ? 3.403    48.311  -54.686  1.00 48.28  ? 336 ILE C C   1 
ATOM   11162 O O   . ILE C  1 336 ? 3.466    47.136  -55.000  1.00 48.54  ? 336 ILE C O   1 
ATOM   11163 C CB  . ILE C  1 336 ? 3.817    49.474  -56.913  1.00 50.94  ? 336 ILE C CB  1 
ATOM   11164 C CG1 . ILE C  1 336 ? 4.702    50.446  -57.685  1.00 52.47  ? 336 ILE C CG1 1 
ATOM   11165 C CG2 . ILE C  1 336 ? 2.352    49.886  -57.034  1.00 49.77  ? 336 ILE C CG2 1 
ATOM   11166 C CD1 . ILE C  1 336 ? 4.969    51.745  -56.943  1.00 53.19  ? 336 ILE C CD1 1 
ATOM   11167 N N   . PRO C  1 337 ? 2.648    48.705  -53.636  1.00 48.28  ? 337 PRO C N   1 
ATOM   11168 C CA  . PRO C  1 337 ? 1.662    47.810  -53.028  1.00 44.75  ? 337 PRO C CA  1 
ATOM   11169 C C   . PRO C  1 337 ? 0.710    47.192  -54.042  1.00 41.94  ? 337 PRO C C   1 
ATOM   11170 O O   . PRO C  1 337 ? 0.140    47.893  -54.861  1.00 39.72  ? 337 PRO C O   1 
ATOM   11171 C CB  . PRO C  1 337 ? 0.932    48.706  -52.018  1.00 45.66  ? 337 PRO C CB  1 
ATOM   11172 C CG  . PRO C  1 337 ? 1.976    49.753  -51.614  1.00 46.99  ? 337 PRO C CG  1 
ATOM   11173 C CD  . PRO C  1 337 ? 2.795    49.978  -52.893  1.00 47.17  ? 337 PRO C CD  1 
ATOM   11174 N N   . LEU C  1 338 ? 0.555    45.862  -53.978  1.00 40.25  ? 338 LEU C N   1 
ATOM   11175 C CA  . LEU C  1 338 ? -0.440   45.180  -54.788  1.00 41.52  ? 338 LEU C CA  1 
ATOM   11176 C C   . LEU C  1 338 ? -1.528   44.567  -53.897  1.00 39.85  ? 338 LEU C C   1 
ATOM   11177 O O   . LEU C  1 338 ? -1.237   43.849  -52.938  1.00 37.08  ? 338 LEU C O   1 
ATOM   11178 C CB  . LEU C  1 338 ? 0.287    44.148  -55.647  1.00 42.92  ? 338 LEU C CB  1 
ATOM   11179 C CG  . LEU C  1 338 ? -0.564   43.120  -56.392  1.00 42.97  ? 338 LEU C CG  1 
ATOM   11180 C CD1 . LEU C  1 338 ? -1.196   43.711  -57.610  1.00 42.81  ? 338 LEU C CD1 1 
ATOM   11181 C CD2 . LEU C  1 338 ? 0.335    41.941  -56.793  1.00 47.00  ? 338 LEU C CD2 1 
ATOM   11182 N N   . GLU C  1 339 ? -2.793   44.886  -54.221  1.00 38.94  ? 339 GLU C N   1 
ATOM   11183 C CA  . GLU C  1 339 ? -3.948   44.377  -53.495  1.00 37.45  ? 339 GLU C CA  1 
ATOM   11184 C C   . GLU C  1 339 ? -4.956   43.883  -54.521  1.00 35.50  ? 339 GLU C C   1 
ATOM   11185 O O   . GLU C  1 339 ? -5.338   44.660  -55.397  1.00 35.71  ? 339 GLU C O   1 
ATOM   11186 C CB  . GLU C  1 339 ? -4.574   45.454  -52.601  1.00 38.30  ? 339 GLU C CB  1 
ATOM   11187 C CG  . GLU C  1 339 ? -3.801   45.752  -51.317  1.00 40.16  ? 339 GLU C CG  1 
ATOM   11188 C CD  . GLU C  1 339 ? -4.470   46.812  -50.446  1.00 43.17  ? 339 GLU C CD  1 
ATOM   11189 O OE1 . GLU C  1 339 ? -4.507   48.004  -50.865  1.00 42.40  ? 339 GLU C OE1 1 
ATOM   11190 O OE2 . GLU C  1 339 ? -4.968   46.455  -49.344  1.00 42.28  ? 339 GLU C OE2 1 
ATOM   11191 N N   . LEU C  1 340 ? -5.369   42.608  -54.405  1.00 33.58  ? 340 LEU C N   1 
ATOM   11192 C CA  . LEU C  1 340 ? -6.361   42.013  -55.287  1.00 31.06  ? 340 LEU C CA  1 
ATOM   11193 C C   . LEU C  1 340 ? -7.485   41.371  -54.468  1.00 32.02  ? 340 LEU C C   1 
ATOM   11194 O O   . LEU C  1 340 ? -7.269   40.886  -53.348  1.00 32.00  ? 340 LEU C O   1 
ATOM   11195 C CB  . LEU C  1 340 ? -5.716   40.949  -56.166  1.00 31.25  ? 340 LEU C CB  1 
ATOM   11196 C CG  . LEU C  1 340 ? -4.617   41.403  -57.122  1.00 32.02  ? 340 LEU C CG  1 
ATOM   11197 C CD1 . LEU C  1 340 ? -4.026   40.219  -57.872  1.00 30.68  ? 340 LEU C CD1 1 
ATOM   11198 C CD2 . LEU C  1 340 ? -5.131   42.450  -58.116  1.00 32.42  ? 340 LEU C CD2 1 
ATOM   11199 N N   . TYR C  1 341 ? -8.683   41.331  -55.075  1.00 31.30  ? 341 TYR C N   1 
ATOM   11200 C CA  . TYR C  1 341 ? -9.795   40.522  -54.600  1.00 31.31  ? 341 TYR C CA  1 
ATOM   11201 C C   . TYR C  1 341 ? -10.299  39.634  -55.751  1.00 31.20  ? 341 TYR C C   1 
ATOM   11202 O O   . TYR C  1 341 ? -10.993  40.106  -56.646  1.00 30.10  ? 341 TYR C O   1 
ATOM   11203 C CB  . TYR C  1 341 ? -10.956  41.356  -54.039  1.00 31.70  ? 341 TYR C CB  1 
ATOM   11204 C CG  . TYR C  1 341 ? -11.924  40.544  -53.186  1.00 32.38  ? 341 TYR C CG  1 
ATOM   11205 C CD1 . TYR C  1 341 ? -11.683  40.355  -51.822  1.00 33.84  ? 341 TYR C CD1 1 
ATOM   11206 C CD2 . TYR C  1 341 ? -13.027  39.911  -53.748  1.00 32.47  ? 341 TYR C CD2 1 
ATOM   11207 C CE1 . TYR C  1 341 ? -12.539  39.606  -51.034  1.00 34.86  ? 341 TYR C CE1 1 
ATOM   11208 C CE2 . TYR C  1 341 ? -13.882  39.144  -52.971  1.00 33.53  ? 341 TYR C CE2 1 
ATOM   11209 C CZ  . TYR C  1 341 ? -13.639  39.000  -51.615  1.00 34.66  ? 341 TYR C CZ  1 
ATOM   11210 O OH  . TYR C  1 341 ? -14.477  38.257  -50.840  1.00 35.69  ? 341 TYR C OH  1 
ATOM   11211 N N   . ASN C  1 342 ? -9.998   38.328  -55.660  1.00 32.45  ? 342 ASN C N   1 
ATOM   11212 C CA  . ASN C  1 342 ? -10.233  37.344  -56.712  1.00 33.22  ? 342 ASN C CA  1 
ATOM   11213 C C   . ASN C  1 342 ? -11.379  36.382  -56.373  1.00 33.45  ? 342 ASN C C   1 
ATOM   11214 O O   . ASN C  1 342 ? -11.461  35.820  -55.279  1.00 35.68  ? 342 ASN C O   1 
ATOM   11215 C CB  . ASN C  1 342 ? -8.999   36.483  -56.916  1.00 32.39  ? 342 ASN C CB  1 
ATOM   11216 C CG  . ASN C  1 342 ? -7.785   37.304  -57.261  1.00 31.69  ? 342 ASN C CG  1 
ATOM   11217 O OD1 . ASN C  1 342 ? -6.731   37.187  -56.631  1.00 34.10  ? 342 ASN C OD1 1 
ATOM   11218 N ND2 . ASN C  1 342 ? -7.890   38.093  -58.305  1.00 30.97  ? 342 ASN C ND2 1 
ATOM   11219 N N   . ASP C  1 343 ? -12.246  36.135  -57.343  1.00 33.05  ? 343 ASP C N   1 
ATOM   11220 C CA  . ASP C  1 343 ? -13.222  35.074  -57.187  1.00 35.04  ? 343 ASP C CA  1 
ATOM   11221 C C   . ASP C  1 343 ? -12.511  33.725  -57.354  1.00 33.08  ? 343 ASP C C   1 
ATOM   11222 O O   . ASP C  1 343 ? -11.307  33.673  -57.589  1.00 32.56  ? 343 ASP C O   1 
ATOM   11223 C CB  . ASP C  1 343 ? -14.449  35.340  -58.059  1.00 37.48  ? 343 ASP C CB  1 
ATOM   11224 C CG  . ASP C  1 343 ? -14.442  34.847  -59.498  1.00 38.36  ? 343 ASP C CG  1 
ATOM   11225 O OD1 . ASP C  1 343 ? -13.517  34.118  -59.876  1.00 37.98  ? 343 ASP C OD1 1 
ATOM   11226 O OD2 . ASP C  1 343 ? -15.407  35.160  -60.227  1.00 42.90  ? 343 ASP C OD2 1 
ATOM   11227 N N   . LYS C  1 344 ? -13.277  32.631  -57.273  1.00 35.37  ? 344 LYS C N   1 
ATOM   11228 C CA  . LYS C  1 344 ? -12.721  31.295  -57.079  1.00 38.30  ? 344 LYS C CA  1 
ATOM   11229 C C   . LYS C  1 344 ? -12.132  30.768  -58.384  1.00 35.01  ? 344 LYS C C   1 
ATOM   11230 O O   . LYS C  1 344 ? -11.399  29.797  -58.365  1.00 33.26  ? 344 LYS C O   1 
ATOM   11231 C CB  . LYS C  1 344 ? -13.748  30.336  -56.465  1.00 43.61  ? 344 LYS C CB  1 
ATOM   11232 C CG  . LYS C  1 344 ? -14.943  30.014  -57.351  1.00 49.59  ? 344 LYS C CG  1 
ATOM   11233 C CD  . LYS C  1 344 ? -16.257  29.969  -56.579  1.00 60.45  ? 344 LYS C CD  1 
ATOM   11234 C CE  . LYS C  1 344 ? -17.429  29.650  -57.442  1.00 66.38  ? 344 LYS C CE  1 
ATOM   11235 N NZ  . LYS C  1 344 ? -17.188  28.330  -58.048  1.00 66.27  ? 344 LYS C NZ  1 
ATOM   11236 N N   . ASP C  1 345 ? -12.418  31.448  -59.495  1.00 33.38  ? 345 ASP C N   1 
ATOM   11237 C CA  . ASP C  1 345 ? -11.963  31.034  -60.812  1.00 32.91  ? 345 ASP C CA  1 
ATOM   11238 C C   . ASP C  1 345 ? -10.547  31.510  -61.124  1.00 31.21  ? 345 ASP C C   1 
ATOM   11239 O O   . ASP C  1 345 ? -9.934   30.928  -62.005  1.00 30.91  ? 345 ASP C O   1 
ATOM   11240 C CB  . ASP C  1 345 ? -12.930  31.524  -61.882  1.00 32.76  ? 345 ASP C CB  1 
ATOM   11241 C CG  . ASP C  1 345 ? -14.270  30.807  -61.884  1.00 32.39  ? 345 ASP C CG  1 
ATOM   11242 O OD1 . ASP C  1 345 ? -14.319  29.702  -61.341  1.00 31.76  ? 345 ASP C OD1 1 
ATOM   11243 O OD2 . ASP C  1 345 ? -15.221  31.365  -62.415  1.00 31.61  ? 345 ASP C OD2 1 
ATOM   11244 N N   . VAL C  1 346 ? -10.076  32.591  -60.477  1.00 29.36  ? 346 VAL C N   1 
ATOM   11245 C CA  . VAL C  1 346 ? -8.746   33.133  -60.738  1.00 29.87  ? 346 VAL C CA  1 
ATOM   11246 C C   . VAL C  1 346 ? -7.670   32.214  -60.129  1.00 30.51  ? 346 VAL C C   1 
ATOM   11247 O O   . VAL C  1 346 ? -7.607   32.051  -58.905  1.00 30.33  ? 346 VAL C O   1 
ATOM   11248 C CB  . VAL C  1 346 ? -8.621   34.556  -60.138  1.00 28.98  ? 346 VAL C CB  1 
ATOM   11249 C CG1 . VAL C  1 346 ? -7.197   35.103  -60.262  1.00 28.45  ? 346 VAL C CG1 1 
ATOM   11250 C CG2 . VAL C  1 346 ? -9.640   35.535  -60.717  1.00 28.01  ? 346 VAL C CG2 1 
ATOM   11251 N N   . LYS C  1 347 ? -6.766   31.691  -60.962  1.00 31.53  ? 347 LYS C N   1 
ATOM   11252 C CA  . LYS C  1 347 ? -5.734   30.774  -60.491  1.00 33.43  ? 347 LYS C CA  1 
ATOM   11253 C C   . LYS C  1 347 ? -4.342   31.329  -60.693  1.00 34.08  ? 347 LYS C C   1 
ATOM   11254 O O   . LYS C  1 347 ? -3.388   30.786  -60.121  1.00 34.28  ? 347 LYS C O   1 
ATOM   11255 C CB  . LYS C  1 347 ? -5.728   29.426  -61.211  1.00 33.42  ? 347 LYS C CB  1 
ATOM   11256 C CG  . LYS C  1 347 ? -7.054   28.733  -61.003  1.00 36.26  ? 347 LYS C CG  1 
ATOM   11257 C CD  . LYS C  1 347 ? -7.451   28.495  -59.547  1.00 37.66  ? 347 LYS C CD  1 
ATOM   11258 C CE  . LYS C  1 347 ? -8.855   27.941  -59.531  1.00 41.05  ? 347 LYS C CE  1 
ATOM   11259 N NZ  . LYS C  1 347 ? -9.415   27.752  -58.191  1.00 42.21  ? 347 LYS C NZ  1 
ATOM   11260 N N   . LYS C  1 348 ? -4.252   32.405  -61.489  1.00 34.43  ? 348 LYS C N   1 
ATOM   11261 C CA  . LYS C  1 348 ? -2.971   33.034  -61.751  1.00 33.50  ? 348 LYS C CA  1 
ATOM   11262 C C   . LYS C  1 348 ? -3.169   34.506  -62.095  1.00 31.65  ? 348 LYS C C   1 
ATOM   11263 O O   . LYS C  1 348 ? -4.112   34.872  -62.807  1.00 30.35  ? 348 LYS C O   1 
ATOM   11264 C CB  . LYS C  1 348 ? -2.291   32.285  -62.901  1.00 33.70  ? 348 LYS C CB  1 
ATOM   11265 C CG  . LYS C  1 348 ? -0.920   32.867  -63.233  1.00 35.99  ? 348 LYS C CG  1 
ATOM   11266 C CD  . LYS C  1 348 ? -0.041   31.999  -64.131  1.00 36.92  ? 348 LYS C CD  1 
ATOM   11267 C CE  . LYS C  1 348 ? -0.476   32.054  -65.549  1.00 36.22  ? 348 LYS C CE  1 
ATOM   11268 N NZ  . LYS C  1 348 ? 0.520    31.441  -66.430  1.00 36.69  ? 348 LYS C NZ  1 
ATOM   11269 N N   . VAL C  1 349 ? -2.225   35.335  -61.648  1.00 33.13  ? 349 VAL C N   1 
ATOM   11270 C CA  . VAL C  1 349 ? -2.271   36.745  -62.003  1.00 34.24  ? 349 VAL C CA  1 
ATOM   11271 C C   . VAL C  1 349 ? -0.900   37.164  -62.506  1.00 34.63  ? 349 VAL C C   1 
ATOM   11272 O O   . VAL C  1 349 ? 0.102    36.908  -61.836  1.00 35.27  ? 349 VAL C O   1 
ATOM   11273 C CB  . VAL C  1 349 ? -2.770   37.655  -60.878  1.00 33.98  ? 349 VAL C CB  1 
ATOM   11274 C CG1 . VAL C  1 349 ? -2.829   39.099  -61.344  1.00 33.86  ? 349 VAL C CG1 1 
ATOM   11275 C CG2 . VAL C  1 349 ? -4.154   37.206  -60.425  1.00 34.62  ? 349 VAL C CG2 1 
ATOM   11276 N N   . VAL C  1 350 ? -0.906   37.771  -63.705  1.00 32.44  ? 350 VAL C N   1 
ATOM   11277 C CA  . VAL C  1 350 ? 0.309    38.270  -64.318  1.00 32.23  ? 350 VAL C CA  1 
ATOM   11278 C C   . VAL C  1 350 ? 0.142    39.761  -64.569  1.00 29.90  ? 350 VAL C C   1 
ATOM   11279 O O   . VAL C  1 350 ? -0.923   40.188  -64.971  1.00 26.90  ? 350 VAL C O   1 
ATOM   11280 C CB  . VAL C  1 350 ? 0.653    37.521  -65.617  1.00 33.49  ? 350 VAL C CB  1 
ATOM   11281 C CG1 . VAL C  1 350 ? 1.837    38.161  -66.337  1.00 34.36  ? 350 VAL C CG1 1 
ATOM   11282 C CG2 . VAL C  1 350 ? 0.922    36.029  -65.384  1.00 34.12  ? 350 VAL C CG2 1 
ATOM   11283 N N   . VAL C  1 351 ? 1.223    40.514  -64.317  1.00 30.44  ? 351 VAL C N   1 
ATOM   11284 C CA  . VAL C  1 351 ? 1.338    41.924  -64.667  1.00 30.29  ? 351 VAL C CA  1 
ATOM   11285 C C   . VAL C  1 351 ? 2.500    42.087  -65.646  1.00 30.55  ? 351 VAL C C   1 
ATOM   11286 O O   . VAL C  1 351 ? 3.608    41.626  -65.398  1.00 30.84  ? 351 VAL C O   1 
ATOM   11287 C CB  . VAL C  1 351 ? 1.533    42.868  -63.473  1.00 30.84  ? 351 VAL C CB  1 
ATOM   11288 C CG1 . VAL C  1 351 ? 1.506    44.328  -63.898  1.00 31.81  ? 351 VAL C CG1 1 
ATOM   11289 C CG2 . VAL C  1 351 ? 0.489    42.622  -62.405  1.00 30.89  ? 351 VAL C CG2 1 
ATOM   11290 N N   . LYS C  1 352 ? 2.202    42.735  -66.774  1.00 31.19  ? 352 LYS C N   1 
ATOM   11291 C CA  . LYS C  1 352 ? 3.194    43.106  -67.757  1.00 32.58  ? 352 LYS C CA  1 
ATOM   11292 C C   . LYS C  1 352 ? 3.320    44.626  -67.855  1.00 30.94  ? 352 LYS C C   1 
ATOM   11293 O O   . LYS C  1 352 ? 2.386    45.394  -67.607  1.00 31.45  ? 352 LYS C O   1 
ATOM   11294 C CB  . LYS C  1 352 ? 2.818    42.521  -69.112  1.00 35.19  ? 352 LYS C CB  1 
ATOM   11295 C CG  . LYS C  1 352 ? 3.149    41.036  -69.288  1.00 38.35  ? 352 LYS C CG  1 
ATOM   11296 C CD  . LYS C  1 352 ? 2.262    40.427  -70.360  1.00 40.89  ? 352 LYS C CD  1 
ATOM   11297 C CE  . LYS C  1 352 ? 2.517    38.975  -70.507  1.00 47.55  ? 352 LYS C CE  1 
ATOM   11298 N NZ  . LYS C  1 352 ? 1.540    38.332  -71.402  1.00 48.82  ? 352 LYS C NZ  1 
ATOM   11299 N N   . PHE C  1 353 ? 4.523    45.030  -68.228  1.00 29.92  ? 353 PHE C N   1 
ATOM   11300 C CA  . PHE C  1 353 ? 4.795    46.353  -68.736  1.00 29.41  ? 353 PHE C CA  1 
ATOM   11301 C C   . PHE C  1 353 ? 5.558    46.215  -70.053  1.00 29.29  ? 353 PHE C C   1 
ATOM   11302 O O   . PHE C  1 353 ? 6.620    45.594  -70.085  1.00 30.64  ? 353 PHE C O   1 
ATOM   11303 C CB  . PHE C  1 353 ? 5.589    47.126  -67.676  1.00 30.29  ? 353 PHE C CB  1 
ATOM   11304 C CG  . PHE C  1 353 ? 5.879    48.548  -68.141  1.00 30.37  ? 353 PHE C CG  1 
ATOM   11305 C CD1 . PHE C  1 353 ? 4.825    49.395  -68.479  1.00 28.76  ? 353 PHE C CD1 1 
ATOM   11306 C CD2 . PHE C  1 353 ? 7.183    48.959  -68.381  1.00 30.87  ? 353 PHE C CD2 1 
ATOM   11307 C CE1 . PHE C  1 353 ? 5.062    50.661  -68.947  1.00 29.15  ? 353 PHE C CE1 1 
ATOM   11308 C CE2 . PHE C  1 353 ? 7.415    50.232  -68.857  1.00 31.64  ? 353 PHE C CE2 1 
ATOM   11309 C CZ  . PHE C  1 353 ? 6.349    51.081  -69.139  1.00 31.05  ? 353 PHE C CZ  1 
ATOM   11310 N N   . ARG C  1 354 ? 5.044    46.817  -71.132  1.00 28.24  ? 354 ARG C N   1 
ATOM   11311 C CA  . ARG C  1 354 ? 5.690    46.732  -72.432  1.00 29.39  ? 354 ARG C CA  1 
ATOM   11312 C C   . ARG C  1 354 ? 6.019    45.276  -72.752  1.00 30.77  ? 354 ARG C C   1 
ATOM   11313 O O   . ARG C  1 354 ? 7.115    44.983  -73.228  1.00 30.96  ? 354 ARG C O   1 
ATOM   11314 C CB  . ARG C  1 354 ? 6.985    47.565  -72.518  1.00 30.28  ? 354 ARG C CB  1 
ATOM   11315 C CG  . ARG C  1 354 ? 6.722    49.056  -72.399  1.00 29.33  ? 354 ARG C CG  1 
ATOM   11316 C CD  . ARG C  1 354 ? 8.021    49.822  -72.437  1.00 30.29  ? 354 ARG C CD  1 
ATOM   11317 N NE  . ARG C  1 354 ? 7.819    51.254  -72.201  1.00 29.53  ? 354 ARG C NE  1 
ATOM   11318 C CZ  . ARG C  1 354 ? 8.740    52.112  -71.790  1.00 29.78  ? 354 ARG C CZ  1 
ATOM   11319 N NH1 . ARG C  1 354 ? 9.992    51.738  -71.724  1.00 30.73  ? 354 ARG C NH1 1 
ATOM   11320 N NH2 . ARG C  1 354 ? 8.399    53.341  -71.430  1.00 29.30  ? 354 ARG C NH2 1 
ATOM   11321 N N   . ASP C  1 355 ? 5.049    44.377  -72.488  1.00 31.71  ? 355 ASP C N   1 
ATOM   11322 C CA  . ASP C  1 355 ? 5.063    43.001  -72.978  1.00 32.06  ? 355 ASP C CA  1 
ATOM   11323 C C   . ASP C  1 355 ? 6.066    42.123  -72.220  1.00 33.02  ? 355 ASP C C   1 
ATOM   11324 O O   . ASP C  1 355 ? 6.331    40.994  -72.640  1.00 32.86  ? 355 ASP C O   1 
ATOM   11325 C CB  . ASP C  1 355 ? 5.275    42.995  -74.485  1.00 32.19  ? 355 ASP C CB  1 
ATOM   11326 C CG  . ASP C  1 355 ? 4.336    43.927  -75.228  1.00 32.30  ? 355 ASP C CG  1 
ATOM   11327 O OD1 . ASP C  1 355 ? 3.137    43.575  -75.353  1.00 30.53  ? 355 ASP C OD1 1 
ATOM   11328 O OD2 . ASP C  1 355 ? 4.821    45.007  -75.649  1.00 33.31  ? 355 ASP C OD2 1 
ATOM   11329 N N   . LYS C  1 356 ? 6.625    42.662  -71.127  1.00 34.68  ? 356 LYS C N   1 
ATOM   11330 C CA  . LYS C  1 356 ? 7.565    41.972  -70.254  1.00 35.14  ? 356 LYS C CA  1 
ATOM   11331 C C   . LYS C  1 356 ? 6.849    41.743  -68.923  1.00 33.88  ? 356 LYS C C   1 
ATOM   11332 O O   . LYS C  1 356 ? 6.258    42.687  -68.360  1.00 30.95  ? 356 LYS C O   1 
ATOM   11333 C CB  . LYS C  1 356 ? 8.819    42.806  -70.005  1.00 36.76  ? 356 LYS C CB  1 
ATOM   11334 C CG  . LYS C  1 356 ? 10.034   42.107  -69.389  1.00 41.26  ? 356 LYS C CG  1 
ATOM   11335 C CD  . LYS C  1 356 ? 11.113   43.113  -68.950  1.00 44.55  ? 356 LYS C CD  1 
ATOM   11336 C CE  . LYS C  1 356 ? 12.502   42.750  -69.311  1.00 50.12  ? 356 LYS C CE  1 
ATOM   11337 N NZ  . LYS C  1 356 ? 12.898   41.544  -68.577  1.00 54.65  ? 356 LYS C NZ  1 
ATOM   11338 N N   . VAL C  1 357 ? 6.886    40.472  -68.478  1.00 31.86  ? 357 VAL C N   1 
ATOM   11339 C CA  . VAL C  1 357 ? 6.360    40.100  -67.187  1.00 31.13  ? 357 VAL C CA  1 
ATOM   11340 C C   . VAL C  1 357 ? 7.184    40.747  -66.084  1.00 31.85  ? 357 VAL C C   1 
ATOM   11341 O O   . VAL C  1 357 ? 8.357    40.420  -65.948  1.00 32.74  ? 357 VAL C O   1 
ATOM   11342 C CB  . VAL C  1 357 ? 6.350    38.576  -67.001  1.00 31.45  ? 357 VAL C CB  1 
ATOM   11343 C CG1 . VAL C  1 357 ? 6.058    38.221  -65.544  1.00 31.54  ? 357 VAL C CG1 1 
ATOM   11344 C CG2 . VAL C  1 357 ? 5.356    37.907  -67.946  1.00 30.19  ? 357 VAL C CG2 1 
ATOM   11345 N N   . ILE C  1 358 ? 6.528    41.586  -65.260  1.00 30.94  ? 358 ILE C N   1 
ATOM   11346 C CA  . ILE C  1 358 ? 7.149    42.134  -64.063  1.00 31.26  ? 358 ILE C CA  1 
ATOM   11347 C C   . ILE C  1 358 ? 6.584    41.487  -62.794  1.00 31.16  ? 358 ILE C C   1 
ATOM   11348 O O   . ILE C  1 358 ? 7.139    41.696  -61.741  1.00 31.58  ? 358 ILE C O   1 
ATOM   11349 C CB  . ILE C  1 358 ? 7.009    43.675  -63.997  1.00 30.48  ? 358 ILE C CB  1 
ATOM   11350 C CG1 . ILE C  1 358 ? 5.551    44.106  -63.892  1.00 29.16  ? 358 ILE C CG1 1 
ATOM   11351 C CG2 . ILE C  1 358 ? 7.743    44.362  -65.150  1.00 30.60  ? 358 ILE C CG2 1 
ATOM   11352 C CD1 . ILE C  1 358 ? 5.374    45.589  -63.635  1.00 29.96  ? 358 ILE C CD1 1 
ATOM   11353 N N   . TYR C  1 359 ? 5.481    40.738  -62.867  1.00 32.86  ? 359 TYR C N   1 
ATOM   11354 C CA  . TYR C  1 359 ? 4.896    40.095  -61.693  1.00 34.86  ? 359 TYR C CA  1 
ATOM   11355 C C   . TYR C  1 359 ? 4.065    38.893  -62.139  1.00 34.89  ? 359 TYR C C   1 
ATOM   11356 O O   . TYR C  1 359 ? 3.286    39.019  -63.069  1.00 34.29  ? 359 TYR C O   1 
ATOM   11357 C CB  . TYR C  1 359 ? 4.030    41.067  -60.871  1.00 34.60  ? 359 TYR C CB  1 
ATOM   11358 C CG  . TYR C  1 359 ? 3.314    40.451  -59.666  1.00 36.16  ? 359 TYR C CG  1 
ATOM   11359 C CD1 . TYR C  1 359 ? 3.925    40.380  -58.421  1.00 36.68  ? 359 TYR C CD1 1 
ATOM   11360 C CD2 . TYR C  1 359 ? 2.025    39.910  -59.776  1.00 36.92  ? 359 TYR C CD2 1 
ATOM   11361 C CE1 . TYR C  1 359 ? 3.296    39.777  -57.344  1.00 38.91  ? 359 TYR C CE1 1 
ATOM   11362 C CE2 . TYR C  1 359 ? 1.370    39.336  -58.698  1.00 36.96  ? 359 TYR C CE2 1 
ATOM   11363 C CZ  . TYR C  1 359 ? 2.017    39.259  -57.479  1.00 40.42  ? 359 TYR C CZ  1 
ATOM   11364 O OH  . TYR C  1 359 ? 1.399    38.672  -56.410  1.00 44.46  ? 359 TYR C OH  1 
ATOM   11365 N N   . SER C  1 360 ? 4.197    37.768  -61.426  1.00 38.23  ? 360 SER C N   1 
ATOM   11366 C CA  . SER C  1 360 ? 3.508    36.525  -61.736  1.00 41.32  ? 360 SER C CA  1 
ATOM   11367 C C   . SER C  1 360 ? 3.256    35.726  -60.453  1.00 43.31  ? 360 SER C C   1 
ATOM   11368 O O   . SER C  1 360 ? 4.186    35.471  -59.696  1.00 47.92  ? 360 SER C O   1 
ATOM   11369 C CB  . SER C  1 360 ? 4.322    35.710  -62.696  1.00 43.84  ? 360 SER C CB  1 
ATOM   11370 O OG  . SER C  1 360 ? 3.542    34.613  -63.159  1.00 48.51  ? 360 SER C OG  1 
ATOM   11371 N N   . LYS C  1 361 ? 2.012    35.313  -60.204  1.00 41.08  ? 361 LYS C N   1 
ATOM   11372 C CA  . LYS C  1 361 ? 1.688    34.626  -58.960  1.00 42.88  ? 361 LYS C CA  1 
ATOM   11373 C C   . LYS C  1 361 ? 0.540    33.638  -59.167  1.00 39.31  ? 361 LYS C C   1 
ATOM   11374 O O   . LYS C  1 361 ? -0.540   34.053  -59.568  1.00 38.05  ? 361 LYS C O   1 
ATOM   11375 C CB  . LYS C  1 361 ? 1.265    35.597  -57.847  1.00 47.26  ? 361 LYS C CB  1 
ATOM   11376 C CG  . LYS C  1 361 ? 1.302    34.975  -56.443  1.00 51.69  ? 361 LYS C CG  1 
ATOM   11377 C CD  . LYS C  1 361 ? 0.674    35.787  -55.312  1.00 57.77  ? 361 LYS C CD  1 
ATOM   11378 C CE  . LYS C  1 361 ? 0.383    35.005  -54.033  1.00 62.95  ? 361 LYS C CE  1 
ATOM   11379 N NZ  . LYS C  1 361 ? 1.601    34.590  -53.313  1.00 63.68  ? 361 LYS C NZ  1 
ATOM   11380 N N   . ASN C  1 362 ? 0.775    32.347  -58.881  1.00 38.48  ? 362 ASN C N   1 
ATOM   11381 C CA  . ASN C  1 362 ? -0.294   31.358  -58.830  1.00 40.52  ? 362 ASN C CA  1 
ATOM   11382 C C   . ASN C  1 362 ? -1.145   31.664  -57.610  1.00 40.92  ? 362 ASN C C   1 
ATOM   11383 O O   . ASN C  1 362 ? -0.574   31.903  -56.550  1.00 44.64  ? 362 ASN C O   1 
ATOM   11384 C CB  . ASN C  1 362 ? 0.210    29.926  -58.733  1.00 42.04  ? 362 ASN C CB  1 
ATOM   11385 C CG  . ASN C  1 362 ? 1.114    29.579  -59.887  1.00 44.83  ? 362 ASN C CG  1 
ATOM   11386 O OD1 . ASN C  1 362 ? 2.224    29.103  -59.660  1.00 47.95  ? 362 ASN C OD1 1 
ATOM   11387 N ND2 . ASN C  1 362 ? 0.684    29.842  -61.115  1.00 44.90  ? 362 ASN C ND2 1 
ATOM   11388 N N   . ILE C  1 363 ? -2.466   31.744  -57.792  1.00 38.21  ? 363 ILE C N   1 
ATOM   11389 C CA  . ILE C  1 363 ? -3.390   32.032  -56.702  1.00 39.71  ? 363 ILE C CA  1 
ATOM   11390 C C   . ILE C  1 363 ? -3.869   30.716  -56.093  1.00 42.48  ? 363 ILE C C   1 
ATOM   11391 O O   . ILE C  1 363 ? -4.585   29.968  -56.750  1.00 42.91  ? 363 ILE C O   1 
ATOM   11392 C CB  . ILE C  1 363 ? -4.595   32.843  -57.208  1.00 38.22  ? 363 ILE C CB  1 
ATOM   11393 C CG1 . ILE C  1 363 ? -4.160   34.152  -57.926  1.00 37.02  ? 363 ILE C CG1 1 
ATOM   11394 C CG2 . ILE C  1 363 ? -5.593   33.101  -56.082  1.00 38.42  ? 363 ILE C CG2 1 
ATOM   11395 C CD1 . ILE C  1 363 ? -3.342   35.127  -57.099  1.00 35.71  ? 363 ILE C CD1 1 
ATOM   11396 N N   . THR C  1 364 ? -3.498   30.468  -54.832  1.00 49.06  ? 364 THR C N   1 
ATOM   11397 C CA  . THR C  1 364 ? -3.911   29.281  -54.086  1.00 54.38  ? 364 THR C CA  1 
ATOM   11398 C C   . THR C  1 364 ? -5.199   29.566  -53.311  1.00 51.19  ? 364 THR C C   1 
ATOM   11399 O O   . THR C  1 364 ? -5.953   28.655  -53.022  1.00 46.18  ? 364 THR C O   1 
ATOM   11400 C CB  . THR C  1 364 ? -2.804   28.844  -53.119  1.00 57.62  ? 364 THR C CB  1 
ATOM   11401 O OG1 . THR C  1 364 ? -2.691   29.898  -52.161  1.00 59.39  ? 364 THR C OG1 1 
ATOM   11402 C CG2 . THR C  1 364 ? -1.473   28.599  -53.811  1.00 60.30  ? 364 THR C CG2 1 
ATOM   11403 N N   . SER C  1 365 ? -5.443   30.828  -52.951  1.00 52.36  ? 365 SER C N   1 
ATOM   11404 C CA  . SER C  1 365 ? -6.561   31.157  -52.080  1.00 52.71  ? 365 SER C CA  1 
ATOM   11405 C C   . SER C  1 365 ? -7.392   32.278  -52.700  1.00 45.55  ? 365 SER C C   1 
ATOM   11406 O O   . SER C  1 365 ? -6.834   33.245  -53.205  1.00 47.90  ? 365 SER C O   1 
ATOM   11407 C CB  . SER C  1 365 ? -6.032   31.515  -50.722  1.00 55.18  ? 365 SER C CB  1 
ATOM   11408 O OG  . SER C  1 365 ? -7.094   31.982  -49.916  1.00 60.94  ? 365 SER C OG  1 
ATOM   11409 N N   . GLU C  1 366 ? -8.721   32.145  -52.674  1.00 42.64  ? 366 GLU C N   1 
ATOM   11410 C CA  . GLU C  1 366 ? -9.622   33.149  -53.237  1.00 39.61  ? 366 GLU C CA  1 
ATOM   11411 C C   . GLU C  1 366 ? -9.814   34.327  -52.267  1.00 36.17  ? 366 GLU C C   1 
ATOM   11412 O O   . GLU C  1 366 ? -9.464   34.249  -51.103  1.00 36.07  ? 366 GLU C O   1 
ATOM   11413 C CB  . GLU C  1 366 ? -10.983  32.545  -53.603  1.00 39.55  ? 366 GLU C CB  1 
ATOM   11414 C CG  . GLU C  1 366 ? -11.919  32.250  -52.430  1.00 40.99  ? 366 GLU C CG  1 
ATOM   11415 C CD  . GLU C  1 366 ? -13.347  31.868  -52.809  1.00 42.24  ? 366 GLU C CD  1 
ATOM   11416 O OE1 . GLU C  1 366 ? -14.108  32.807  -52.960  1.00 41.80  ? 366 GLU C OE1 1 
ATOM   11417 O OE2 . GLU C  1 366 ? -13.723  30.689  -52.999  1.00 48.08  ? 366 GLU C OE2 1 
ATOM   11418 N N   . GLY C  1 367 ? -10.448  35.398  -52.733  1.00 35.20  ? 367 GLY C N   1 
ATOM   11419 C CA  . GLY C  1 367 ? -10.634  36.604  -51.930  1.00 36.51  ? 367 GLY C CA  1 
ATOM   11420 C C   . GLY C  1 367 ? -9.389   37.513  -51.932  1.00 35.38  ? 367 GLY C C   1 
ATOM   11421 O O   . GLY C  1 367 ? -8.673   37.624  -52.931  1.00 33.19  ? 367 GLY C O   1 
ATOM   11422 N N   . TYR C  1 368 ? -9.134   38.159  -50.785  1.00 34.73  ? 368 TYR C N   1 
ATOM   11423 C CA  . TYR C  1 368 ? -8.100   39.176  -50.664  1.00 34.12  ? 368 TYR C CA  1 
ATOM   11424 C C   . TYR C  1 368 ? -6.708   38.552  -50.687  1.00 35.65  ? 368 TYR C C   1 
ATOM   11425 O O   . TYR C  1 368 ? -6.476   37.559  -50.011  1.00 33.69  ? 368 TYR C O   1 
ATOM   11426 C CB  . TYR C  1 368 ? -8.278   39.883  -49.324  1.00 33.22  ? 368 TYR C CB  1 
ATOM   11427 C CG  . TYR C  1 368 ? -7.271   40.998  -49.144  1.00 32.90  ? 368 TYR C CG  1 
ATOM   11428 C CD1 . TYR C  1 368 ? -7.505   42.279  -49.657  1.00 32.27  ? 368 TYR C CD1 1 
ATOM   11429 C CD2 . TYR C  1 368 ? -6.100   40.776  -48.448  1.00 33.06  ? 368 TYR C CD2 1 
ATOM   11430 C CE1 . TYR C  1 368 ? -6.588   43.302  -49.482  1.00 31.96  ? 368 TYR C CE1 1 
ATOM   11431 C CE2 . TYR C  1 368 ? -5.170   41.787  -48.268  1.00 34.91  ? 368 TYR C CE2 1 
ATOM   11432 C CZ  . TYR C  1 368 ? -5.417   43.051  -48.787  1.00 33.71  ? 368 TYR C CZ  1 
ATOM   11433 O OH  . TYR C  1 368 ? -4.474   44.006  -48.620  1.00 33.08  ? 368 TYR C OH  1 
ATOM   11434 N N   . MET C  1 369 ? -5.784   39.201  -51.409  1.00 37.39  ? 369 MET C N   1 
ATOM   11435 C CA  . MET C  1 369 ? -4.364   38.912  -51.312  1.00 38.51  ? 369 MET C CA  1 
ATOM   11436 C C   . MET C  1 369 ? -3.549   40.185  -51.562  1.00 38.96  ? 369 MET C C   1 
ATOM   11437 O O   . MET C  1 369 ? -3.851   40.983  -52.459  1.00 39.37  ? 369 MET C O   1 
ATOM   11438 C CB  . MET C  1 369 ? -3.933   37.833  -52.305  1.00 41.72  ? 369 MET C CB  1 
ATOM   11439 C CG  . MET C  1 369 ? -4.063   38.237  -53.745  1.00 47.38  ? 369 MET C CG  1 
ATOM   11440 S SD  . MET C  1 369 ? -2.632   37.841  -54.768  1.00 59.30  ? 369 MET C SD  1 
ATOM   11441 C CE  . MET C  1 369 ? -1.304   38.745  -53.965  1.00 55.69  ? 369 MET C CE  1 
ATOM   11442 N N   . ALA C  1 370 ? -2.490   40.361  -50.766  1.00 37.63  ? 370 ALA C N   1 
ATOM   11443 C CA  . ALA C  1 370 ? -1.651   41.546  -50.841  1.00 38.25  ? 370 ALA C CA  1 
ATOM   11444 C C   . ALA C  1 370 ? -0.235   41.104  -51.195  1.00 38.98  ? 370 ALA C C   1 
ATOM   11445 O O   . ALA C  1 370 ? 0.225    40.083  -50.711  1.00 38.73  ? 370 ALA C O   1 
ATOM   11446 C CB  . ALA C  1 370 ? -1.660   42.314  -49.526  1.00 37.80  ? 370 ALA C CB  1 
ATOM   11447 N N   . ASP C  1 371 ? 0.441    41.894  -52.026  1.00 38.19  ? 371 ASP C N   1 
ATOM   11448 C CA  . ASP C  1 371 ? 1.808    41.627  -52.414  1.00 38.98  ? 371 ASP C CA  1 
ATOM   11449 C C   . ASP C  1 371 ? 2.427    42.969  -52.807  1.00 38.17  ? 371 ASP C C   1 
ATOM   11450 O O   . ASP C  1 371 ? 1.929    44.017  -52.391  1.00 36.60  ? 371 ASP C O   1 
ATOM   11451 C CB  . ASP C  1 371 ? 1.820    40.494  -53.438  1.00 38.81  ? 371 ASP C CB  1 
ATOM   11452 C CG  . ASP C  1 371 ? 3.118    39.701  -53.561  1.00 38.40  ? 371 ASP C CG  1 
ATOM   11453 O OD1 . ASP C  1 371 ? 4.130    40.115  -52.993  1.00 36.35  ? 371 ASP C OD1 1 
ATOM   11454 O OD2 . ASP C  1 371 ? 3.107    38.687  -54.274  1.00 42.41  ? 371 ASP C OD2 1 
ATOM   11455 N N   . GLU C  1 372 ? 3.516    42.939  -53.588  1.00 40.28  ? 372 GLU C N   1 
ATOM   11456 C CA  . GLU C  1 372 ? 4.075    44.169  -54.122  1.00 43.04  ? 372 GLU C CA  1 
ATOM   11457 C C   . GLU C  1 372 ? 4.726    43.920  -55.481  1.00 41.71  ? 372 GLU C C   1 
ATOM   11458 O O   . GLU C  1 372 ? 5.214    42.824  -55.735  1.00 41.90  ? 372 GLU C O   1 
ATOM   11459 C CB  . GLU C  1 372 ? 4.988    44.815  -53.084  1.00 46.67  ? 372 GLU C CB  1 
ATOM   11460 C CG  . GLU C  1 372 ? 6.020    43.849  -52.540  1.00 51.10  ? 372 GLU C CG  1 
ATOM   11461 C CD  . GLU C  1 372 ? 7.160    44.605  -51.901  1.00 57.91  ? 372 GLU C CD  1 
ATOM   11462 O OE1 . GLU C  1 372 ? 6.913    45.768  -51.503  1.00 62.09  ? 372 GLU C OE1 1 
ATOM   11463 O OE2 . GLU C  1 372 ? 8.289    44.048  -51.857  1.00 61.29  ? 372 GLU C OE2 1 
ATOM   11464 N N   . LEU C  1 373 ? 4.649    44.942  -56.350  1.00 41.43  ? 373 LEU C N   1 
ATOM   11465 C CA  . LEU C  1 373 ? 5.269    44.955  -57.662  1.00 42.49  ? 373 LEU C CA  1 
ATOM   11466 C C   . LEU C  1 373 ? 6.584    45.670  -57.534  1.00 41.56  ? 373 LEU C C   1 
ATOM   11467 O O   . LEU C  1 373 ? 6.600    46.677  -56.860  1.00 43.93  ? 373 LEU C O   1 
ATOM   11468 C CB  . LEU C  1 373 ? 4.487    45.789  -58.673  1.00 42.82  ? 373 LEU C CB  1 
ATOM   11469 C CG  . LEU C  1 373 ? 3.103    45.281  -59.009  1.00 46.65  ? 373 LEU C CG  1 
ATOM   11470 C CD1 . LEU C  1 373 ? 2.333    46.342  -59.814  1.00 47.16  ? 373 LEU C CD1 1 
ATOM   11471 C CD2 . LEU C  1 373 ? 3.292    43.946  -59.718  1.00 44.22  ? 373 LEU C CD2 1 
ATOM   11472 N N   . THR C  1 374 ? 7.562    45.286  -58.349  1.00 41.88  ? 374 THR C N   1 
ATOM   11473 C CA  . THR C  1 374 ? 8.760    46.082  -58.504  1.00 43.18  ? 374 THR C CA  1 
ATOM   11474 C C   . THR C  1 374 ? 8.762    46.689  -59.900  1.00 44.35  ? 374 THR C C   1 
ATOM   11475 O O   . THR C  1 374 ? 8.555    45.984  -60.881  1.00 46.19  ? 374 THR C O   1 
ATOM   11476 C CB  . THR C  1 374 ? 10.014   45.251  -58.258  1.00 43.37  ? 374 THR C CB  1 
ATOM   11477 O OG1 . THR C  1 374 ? 9.772    44.843  -56.919  1.00 44.09  ? 374 THR C OG1 1 
ATOM   11478 C CG2 . THR C  1 374 ? 11.289   46.074  -58.360  1.00 42.78  ? 374 THR C CG2 1 
ATOM   11479 N N   . ILE C  1 375 ? 9.060    47.990  -59.951  1.00 43.30  ? 375 ILE C N   1 
ATOM   11480 C CA  . ILE C  1 375 ? 9.186    48.736  -61.187  1.00 43.06  ? 375 ILE C CA  1 
ATOM   11481 C C   . ILE C  1 375 ? 10.547   49.428  -61.196  1.00 45.17  ? 375 ILE C C   1 
ATOM   11482 O O   . ILE C  1 375 ? 11.178   49.589  -60.154  1.00 46.49  ? 375 ILE C O   1 
ATOM   11483 C CB  . ILE C  1 375 ? 8.018    49.724  -61.329  1.00 41.20  ? 375 ILE C CB  1 
ATOM   11484 C CG1 . ILE C  1 375 ? 7.984    50.759  -60.198  1.00 39.27  ? 375 ILE C CG1 1 
ATOM   11485 C CG2 . ILE C  1 375 ? 6.682    48.969  -61.454  1.00 39.88  ? 375 ILE C CG2 1 
ATOM   11486 C CD1 . ILE C  1 375 ? 7.060    51.922  -60.498  1.00 38.22  ? 375 ILE C CD1 1 
ATOM   11487 N N   . ASP C  1 376 ? 11.013   49.802  -62.391  1.00 46.90  ? 376 ASP C N   1 
ATOM   11488 C CA  . ASP C  1 376 ? 12.321   50.430  -62.547  1.00 48.95  ? 376 ASP C CA  1 
ATOM   11489 C C   . ASP C  1 376 ? 12.155   51.656  -63.457  1.00 46.50  ? 376 ASP C C   1 
ATOM   11490 O O   . ASP C  1 376 ? 12.674   51.699  -64.558  1.00 47.78  ? 376 ASP C O   1 
ATOM   11491 C CB  . ASP C  1 376 ? 13.332   49.407  -63.044  1.00 49.13  ? 376 ASP C CB  1 
ATOM   11492 C CG  . ASP C  1 376 ? 14.805   49.749  -62.870  1.00 52.93  ? 376 ASP C CG  1 
ATOM   11493 O OD1 . ASP C  1 376 ? 15.133   50.733  -62.161  1.00 53.33  ? 376 ASP C OD1 1 
ATOM   11494 O OD2 . ASP C  1 376 ? 15.630   48.993  -63.425  1.00 56.85  ? 376 ASP C OD2 1 
ATOM   11495 N N   . PRO C  1 377 ? 11.410   52.698  -63.045  1.00 44.15  ? 377 PRO C N   1 
ATOM   11496 C CA  . PRO C  1 377 ? 11.111   53.834  -63.929  1.00 43.59  ? 377 PRO C CA  1 
ATOM   11497 C C   . PRO C  1 377 ? 12.327   54.657  -64.316  1.00 42.40  ? 377 PRO C C   1 
ATOM   11498 O O   . PRO C  1 377 ? 13.257   54.777  -63.519  1.00 42.65  ? 377 PRO C O   1 
ATOM   11499 C CB  . PRO C  1 377 ? 10.110   54.680  -63.132  1.00 42.88  ? 377 PRO C CB  1 
ATOM   11500 C CG  . PRO C  1 377 ? 10.408   54.337  -61.690  1.00 44.66  ? 377 PRO C CG  1 
ATOM   11501 C CD  . PRO C  1 377 ? 10.842   52.863  -61.703  1.00 44.22  ? 377 PRO C CD  1 
ATOM   11502 N N   . VAL C  1 378 ? 12.292   55.197  -65.546  1.00 42.44  ? 378 VAL C N   1 
ATOM   11503 C CA  . VAL C  1 378 ? 13.345   56.069  -66.052  1.00 44.02  ? 378 VAL C CA  1 
ATOM   11504 C C   . VAL C  1 378 ? 12.837   57.514  -66.005  1.00 42.72  ? 378 VAL C C   1 
ATOM   11505 O O   . VAL C  1 378 ? 11.827   57.855  -66.604  1.00 42.40  ? 378 VAL C O   1 
ATOM   11506 C CB  . VAL C  1 378 ? 13.799   55.660  -67.464  1.00 44.96  ? 378 VAL C CB  1 
ATOM   11507 C CG1 . VAL C  1 378 ? 14.847   56.627  -68.004  1.00 46.13  ? 378 VAL C CG1 1 
ATOM   11508 C CG2 . VAL C  1 378 ? 14.324   54.222  -67.484  1.00 46.06  ? 378 VAL C CG2 1 
ATOM   11509 N N   . GLY C  1 379 ? 13.533   58.348  -65.237  1.00 42.48  ? 379 GLY C N   1 
ATOM   11510 C CA  . GLY C  1 379 ? 13.097   59.704  -64.970  1.00 41.21  ? 379 GLY C CA  1 
ATOM   11511 C C   . GLY C  1 379 ? 11.658   59.698  -64.465  1.00 38.32  ? 379 GLY C C   1 
ATOM   11512 O O   . GLY C  1 379 ? 11.314   58.889  -63.612  1.00 37.60  ? 379 GLY C O   1 
ATOM   11513 N N   . ILE C  1 380 ? 10.847   60.596  -65.021  1.00 36.39  ? 380 ILE C N   1 
ATOM   11514 C CA  . ILE C  1 380 ? 9.412    60.523  -64.865  1.00 35.78  ? 380 ILE C CA  1 
ATOM   11515 C C   . ILE C  1 380 ? 8.833    59.709  -66.020  1.00 34.60  ? 380 ILE C C   1 
ATOM   11516 O O   . ILE C  1 380 ? 8.930    60.093  -67.181  1.00 32.66  ? 380 ILE C O   1 
ATOM   11517 C CB  . ILE C  1 380 ? 8.795    61.925  -64.795  1.00 36.12  ? 380 ILE C CB  1 
ATOM   11518 C CG1 . ILE C  1 380 ? 9.625    62.880  -63.913  1.00 37.79  ? 380 ILE C CG1 1 
ATOM   11519 C CG2 . ILE C  1 380 ? 7.343    61.821  -64.348  1.00 34.82  ? 380 ILE C CG2 1 
ATOM   11520 C CD1 . ILE C  1 380 ? 9.109    64.314  -63.894  1.00 37.80  ? 380 ILE C CD1 1 
ATOM   11521 N N   . GLU C  1 381 ? 8.183    58.593  -65.656  1.00 35.58  ? 381 GLU C N   1 
ATOM   11522 C CA  . GLU C  1 381 ? 7.711    57.595  -66.614  1.00 35.80  ? 381 GLU C CA  1 
ATOM   11523 C C   . GLU C  1 381 ? 6.225    57.271  -66.432  1.00 34.82  ? 381 GLU C C   1 
ATOM   11524 O O   . GLU C  1 381 ? 5.838    56.665  -65.432  1.00 35.65  ? 381 GLU C O   1 
ATOM   11525 C CB  . GLU C  1 381 ? 8.512    56.295  -66.443  1.00 35.84  ? 381 GLU C CB  1 
ATOM   11526 C CG  . GLU C  1 381 ? 8.445    55.395  -67.672  1.00 36.00  ? 381 GLU C CG  1 
ATOM   11527 C CD  . GLU C  1 381 ? 9.255    54.117  -67.599  1.00 36.22  ? 381 GLU C CD  1 
ATOM   11528 O OE1 . GLU C  1 381 ? 10.484   54.070  -67.525  1.00 38.10  ? 381 GLU C OE1 1 
ATOM   11529 O OE2 . GLU C  1 381 ? 8.576    53.114  -67.610  1.00 36.56  ? 381 GLU C OE2 1 
ATOM   11530 N N   . ASP C  1 382 ? 5.390    57.602  -67.429  1.00 33.35  ? 382 ASP C N   1 
ATOM   11531 C CA  . ASP C  1 382 ? 4.040    57.054  -67.466  1.00 31.81  ? 382 ASP C CA  1 
ATOM   11532 C C   . ASP C  1 382 ? 4.108    55.551  -67.780  1.00 31.47  ? 382 ASP C C   1 
ATOM   11533 O O   . ASP C  1 382 ? 4.848    55.134  -68.667  1.00 31.14  ? 382 ASP C O   1 
ATOM   11534 C CB  . ASP C  1 382 ? 3.160    57.773  -68.475  1.00 30.62  ? 382 ASP C CB  1 
ATOM   11535 C CG  . ASP C  1 382 ? 3.762    57.887  -69.863  1.00 30.86  ? 382 ASP C CG  1 
ATOM   11536 O OD1 . ASP C  1 382 ? 4.868    58.479  -69.962  1.00 32.32  ? 382 ASP C OD1 1 
ATOM   11537 O OD2 . ASP C  1 382 ? 3.129    57.397  -70.814  1.00 28.46  ? 382 ASP C OD2 1 
ATOM   11538 N N   . MET C  1 383 ? 3.305    54.745  -67.073  1.00 30.79  ? 383 MET C N   1 
ATOM   11539 C CA  . MET C  1 383 ? 3.335    53.303  -67.236  1.00 31.12  ? 383 MET C CA  1 
ATOM   11540 C C   . MET C  1 383 ? 1.913    52.758  -67.257  1.00 29.18  ? 383 MET C C   1 
ATOM   11541 O O   . MET C  1 383 ? 1.161    52.976  -66.326  1.00 27.08  ? 383 MET C O   1 
ATOM   11542 C CB  . MET C  1 383 ? 4.099    52.617  -66.092  1.00 33.37  ? 383 MET C CB  1 
ATOM   11543 C CG  . MET C  1 383 ? 5.489    53.142  -65.869  1.00 35.84  ? 383 MET C CG  1 
ATOM   11544 S SD  . MET C  1 383 ? 6.314    52.339  -64.483  1.00 41.03  ? 383 MET C SD  1 
ATOM   11545 C CE  . MET C  1 383 ? 6.889    50.772  -65.146  1.00 41.86  ? 383 MET C CE  1 
ATOM   11546 N N   . GLU C  1 384 ? 1.555    52.063  -68.341  1.00 30.36  ? 384 GLU C N   1 
ATOM   11547 C CA  . GLU C  1 384 ? 0.318    51.285  -68.394  1.00 30.63  ? 384 GLU C CA  1 
ATOM   11548 C C   . GLU C  1 384 ? 0.633    49.862  -67.924  1.00 29.53  ? 384 GLU C C   1 
ATOM   11549 O O   . GLU C  1 384 ? 1.216    49.099  -68.679  1.00 30.08  ? 384 GLU C O   1 
ATOM   11550 C CB  . GLU C  1 384 ? -0.286   51.262  -69.799  1.00 30.57  ? 384 GLU C CB  1 
ATOM   11551 C CG  . GLU C  1 384 ? -1.642   50.554  -69.892  1.00 30.60  ? 384 GLU C CG  1 
ATOM   11552 C CD  . GLU C  1 384 ? -2.233   50.565  -71.296  1.00 30.14  ? 384 GLU C CD  1 
ATOM   11553 O OE1 . GLU C  1 384 ? -1.558   50.894  -72.298  1.00 30.70  ? 384 GLU C OE1 1 
ATOM   11554 O OE2 . GLU C  1 384 ? -3.434   50.321  -71.375  1.00 31.49  ? 384 GLU C OE2 1 
ATOM   11555 N N   . LEU C  1 385 ? 0.289    49.537  -66.671  1.00 28.78  ? 385 LEU C N   1 
ATOM   11556 C CA  . LEU C  1 385 ? 0.520    48.200  -66.141  1.00 29.83  ? 385 LEU C CA  1 
ATOM   11557 C C   . LEU C  1 385 ? -0.624   47.289  -66.606  1.00 29.81  ? 385 LEU C C   1 
ATOM   11558 O O   . LEU C  1 385 ? -1.777   47.561  -66.272  1.00 28.91  ? 385 LEU C O   1 
ATOM   11559 C CB  . LEU C  1 385 ? 0.631    48.221  -64.615  1.00 29.49  ? 385 LEU C CB  1 
ATOM   11560 C CG  . LEU C  1 385 ? 1.564    49.262  -63.998  1.00 30.71  ? 385 LEU C CG  1 
ATOM   11561 C CD1 . LEU C  1 385 ? 1.438    49.147  -62.513  1.00 31.59  ? 385 LEU C CD1 1 
ATOM   11562 C CD2 . LEU C  1 385 ? 3.008    49.073  -64.411  1.00 31.75  ? 385 LEU C CD2 1 
ATOM   11563 N N   . ALA C  1 386 ? -0.275   46.207  -67.334  1.00 29.95  ? 386 ALA C N   1 
ATOM   11564 C CA  . ALA C  1 386 ? -1.243   45.310  -67.949  1.00 30.97  ? 386 ALA C CA  1 
ATOM   11565 C C   . ALA C  1 386 ? -1.440   44.053  -67.094  1.00 31.92  ? 386 ALA C C   1 
ATOM   11566 O O   . ALA C  1 386 ? -0.566   43.184  -67.036  1.00 31.09  ? 386 ALA C O   1 
ATOM   11567 C CB  . ALA C  1 386 ? -0.783   44.942  -69.346  1.00 30.97  ? 386 ALA C CB  1 
ATOM   11568 N N   . PHE C  1 387 ? -2.598   43.980  -66.425  1.00 30.76  ? 387 PHE C N   1 
ATOM   11569 C CA  . PHE C  1 387 ? -2.918   42.875  -65.547  1.00 30.30  ? 387 PHE C CA  1 
ATOM   11570 C C   . PHE C  1 387 ? -3.645   41.831  -66.376  1.00 32.39  ? 387 PHE C C   1 
ATOM   11571 O O   . PHE C  1 387 ? -4.529   42.189  -67.156  1.00 34.56  ? 387 PHE C O   1 
ATOM   11572 C CB  . PHE C  1 387 ? -3.813   43.312  -64.390  1.00 30.53  ? 387 PHE C CB  1 
ATOM   11573 C CG  . PHE C  1 387 ? -3.088   44.103  -63.310  1.00 32.65  ? 387 PHE C CG  1 
ATOM   11574 C CD1 . PHE C  1 387 ? -2.537   45.352  -63.591  1.00 33.03  ? 387 PHE C CD1 1 
ATOM   11575 C CD2 . PHE C  1 387 ? -2.962   43.594  -62.022  1.00 32.74  ? 387 PHE C CD2 1 
ATOM   11576 C CE1 . PHE C  1 387 ? -1.827   46.039  -62.625  1.00 33.52  ? 387 PHE C CE1 1 
ATOM   11577 C CE2 . PHE C  1 387 ? -2.287   44.294  -61.052  1.00 32.88  ? 387 PHE C CE2 1 
ATOM   11578 C CZ  . PHE C  1 387 ? -1.708   45.508  -61.361  1.00 36.15  ? 387 PHE C CZ  1 
ATOM   11579 N N   . GLU C  1 388 ? -3.263   40.561  -66.184  1.00 31.77  ? 388 GLU C N   1 
ATOM   11580 C CA  . GLU C  1 388 ? -3.935   39.434  -66.798  1.00 31.05  ? 388 GLU C CA  1 
ATOM   11581 C C   . GLU C  1 388 ? -4.354   38.443  -65.714  1.00 30.71  ? 388 GLU C C   1 
ATOM   11582 O O   . GLU C  1 388 ? -3.533   38.050  -64.895  1.00 29.92  ? 388 GLU C O   1 
ATOM   11583 C CB  . GLU C  1 388 ? -2.993   38.727  -67.767  1.00 32.36  ? 388 GLU C CB  1 
ATOM   11584 C CG  . GLU C  1 388 ? -2.480   39.597  -68.911  1.00 33.60  ? 388 GLU C CG  1 
ATOM   11585 C CD  . GLU C  1 388 ? -1.278   39.018  -69.625  1.00 34.36  ? 388 GLU C CD  1 
ATOM   11586 O OE1 . GLU C  1 388 ? -0.674   38.098  -69.073  1.00 32.62  ? 388 GLU C OE1 1 
ATOM   11587 O OE2 . GLU C  1 388 ? -0.925   39.499  -70.724  1.00 38.24  ? 388 GLU C OE2 1 
ATOM   11588 N N   . PHE C  1 389 ? -5.633   38.037  -65.758  1.00 30.96  ? 389 PHE C N   1 
ATOM   11589 C CA  . PHE C  1 389 ? -6.219   37.065  -64.853  1.00 31.21  ? 389 PHE C CA  1 
ATOM   11590 C C   . PHE C  1 389 ? -6.516   35.783  -65.615  1.00 32.19  ? 389 PHE C C   1 
ATOM   11591 O O   . PHE C  1 389 ? -7.186   35.840  -66.631  1.00 33.58  ? 389 PHE C O   1 
ATOM   11592 C CB  . PHE C  1 389 ? -7.525   37.609  -64.279  1.00 29.81  ? 389 PHE C CB  1 
ATOM   11593 C CG  . PHE C  1 389 ? -7.340   38.788  -63.352  1.00 28.79  ? 389 PHE C CG  1 
ATOM   11594 C CD1 . PHE C  1 389 ? -7.163   40.058  -63.872  1.00 30.48  ? 389 PHE C CD1 1 
ATOM   11595 C CD2 . PHE C  1 389 ? -7.341   38.629  -61.981  1.00 29.14  ? 389 PHE C CD2 1 
ATOM   11596 C CE1 . PHE C  1 389 ? -6.992   41.149  -63.040  1.00 29.91  ? 389 PHE C CE1 1 
ATOM   11597 C CE2 . PHE C  1 389 ? -7.177   39.730  -61.150  1.00 29.68  ? 389 PHE C CE2 1 
ATOM   11598 C CZ  . PHE C  1 389 ? -7.003   40.982  -61.679  1.00 29.27  ? 389 PHE C CZ  1 
ATOM   11599 N N   . TYR C  1 390 ? -6.065   34.634  -65.087  1.00 34.87  ? 390 TYR C N   1 
ATOM   11600 C CA  . TYR C  1 390 ? -6.143   33.344  -65.765  1.00 33.68  ? 390 TYR C CA  1 
ATOM   11601 C C   . TYR C  1 390 ? -6.929   32.328  -64.931  1.00 33.89  ? 390 TYR C C   1 
ATOM   11602 O O   . TYR C  1 390 ? -6.784   32.308  -63.713  1.00 31.82  ? 390 TYR C O   1 
ATOM   11603 C CB  . TYR C  1 390 ? -4.734   32.768  -65.895  1.00 35.29  ? 390 TYR C CB  1 
ATOM   11604 C CG  . TYR C  1 390 ? -3.772   33.517  -66.798  1.00 35.47  ? 390 TYR C CG  1 
ATOM   11605 C CD1 . TYR C  1 390 ? -3.157   34.692  -66.392  1.00 36.54  ? 390 TYR C CD1 1 
ATOM   11606 C CD2 . TYR C  1 390 ? -3.444   33.010  -68.043  1.00 39.07  ? 390 TYR C CD2 1 
ATOM   11607 C CE1 . TYR C  1 390 ? -2.287   35.369  -67.226  1.00 37.36  ? 390 TYR C CE1 1 
ATOM   11608 C CE2 . TYR C  1 390 ? -2.541   33.651  -68.871  1.00 41.50  ? 390 TYR C CE2 1 
ATOM   11609 C CZ  . TYR C  1 390 ? -1.979   34.846  -68.468  1.00 40.45  ? 390 TYR C CZ  1 
ATOM   11610 O OH  . TYR C  1 390 ? -1.126   35.465  -69.319  1.00 41.37  ? 390 TYR C OH  1 
ATOM   11611 N N   . ASP C  1 391 ? -7.680   31.445  -65.615  1.00 35.04  ? 391 ASP C N   1 
ATOM   11612 C CA  . ASP C  1 391 ? -8.446   30.372  -64.993  1.00 34.07  ? 391 ASP C CA  1 
ATOM   11613 C C   . ASP C  1 391 ? -7.568   29.123  -64.873  1.00 34.97  ? 391 ASP C C   1 
ATOM   11614 O O   . ASP C  1 391 ? -6.390   29.196  -65.149  1.00 33.63  ? 391 ASP C O   1 
ATOM   11615 C CB  . ASP C  1 391 ? -9.726   30.068  -65.763  1.00 33.11  ? 391 ASP C CB  1 
ATOM   11616 C CG  . ASP C  1 391 ? -9.585   29.473  -67.159  1.00 31.91  ? 391 ASP C CG  1 
ATOM   11617 O OD1 . ASP C  1 391 ? -8.483   29.005  -67.502  1.00 32.32  ? 391 ASP C OD1 1 
ATOM   11618 O OD2 . ASP C  1 391 ? -10.574  29.545  -67.918  1.00 31.50  ? 391 ASP C OD2 1 
ATOM   11619 N N   . SER C  1 392 ? -8.156   27.982  -64.481  1.00 34.70  ? 392 SER C N   1 
ATOM   11620 C CA  . SER C  1 392 ? -7.384   26.771  -64.226  1.00 36.73  ? 392 SER C CA  1 
ATOM   11621 C C   . SER C  1 392 ? -6.930   26.098  -65.517  1.00 36.63  ? 392 SER C C   1 
ATOM   11622 O O   . SER C  1 392 ? -6.088   25.227  -65.458  1.00 34.91  ? 392 SER C O   1 
ATOM   11623 C CB  . SER C  1 392 ? -8.120   25.751  -63.355  1.00 36.66  ? 392 SER C CB  1 
ATOM   11624 O OG  . SER C  1 392 ? -9.370   25.359  -63.898  1.00 34.72  ? 392 SER C OG  1 
ATOM   11625 N N   . ASP C  1 393 ? -7.448   26.521  -66.675  1.00 37.73  ? 393 ASP C N   1 
ATOM   11626 C CA  . ASP C  1 393 ? -6.911   26.034  -67.932  1.00 38.17  ? 393 ASP C CA  1 
ATOM   11627 C C   . ASP C  1 393 ? -5.817   26.960  -68.471  1.00 37.13  ? 393 ASP C C   1 
ATOM   11628 O O   . ASP C  1 393 ? -5.335   26.738  -69.567  1.00 34.82  ? 393 ASP C O   1 
ATOM   11629 C CB  . ASP C  1 393 ? -8.050   25.757  -68.894  1.00 40.30  ? 393 ASP C CB  1 
ATOM   11630 C CG  . ASP C  1 393 ? -8.857   24.526  -68.510  1.00 44.25  ? 393 ASP C CG  1 
ATOM   11631 O OD1 . ASP C  1 393 ? -8.255   23.525  -67.969  1.00 45.71  ? 393 ASP C OD1 1 
ATOM   11632 O OD2 . ASP C  1 393 ? -10.063  24.569  -68.771  1.00 47.38  ? 393 ASP C OD2 1 
ATOM   11633 N N   . ASN C  1 394 ? -5.438   28.011  -67.725  1.00 37.02  ? 394 ASN C N   1 
ATOM   11634 C CA  . ASN C  1 394 ? -4.378   28.912  -68.156  1.00 37.78  ? 394 ASN C CA  1 
ATOM   11635 C C   . ASN C  1 394 ? -4.853   29.758  -69.358  1.00 36.85  ? 394 ASN C C   1 
ATOM   11636 O O   . ASN C  1 394 ? -4.078   30.111  -70.237  1.00 35.05  ? 394 ASN C O   1 
ATOM   11637 C CB  . ASN C  1 394 ? -3.113   28.068  -68.306  1.00 38.98  ? 394 ASN C CB  1 
ATOM   11638 C CG  . ASN C  1 394 ? -1.849   28.884  -68.216  1.00 40.56  ? 394 ASN C CG  1 
ATOM   11639 O OD1 . ASN C  1 394 ? -1.760   29.846  -67.452  1.00 39.25  ? 394 ASN C OD1 1 
ATOM   11640 N ND2 . ASN C  1 394 ? -0.857   28.533  -69.012  1.00 42.17  ? 394 ASN C ND2 1 
ATOM   11641 N N   . LYS C  1 395 ? -6.160   30.031  -69.419  1.00 38.94  ? 395 LYS C N   1 
ATOM   11642 C CA  . LYS C  1 395 ? -6.773   30.950  -70.366  1.00 43.50  ? 395 LYS C CA  1 
ATOM   11643 C C   . LYS C  1 395 ? -7.081   32.267  -69.661  1.00 39.02  ? 395 LYS C C   1 
ATOM   11644 O O   . LYS C  1 395 ? -7.579   32.262  -68.529  1.00 36.93  ? 395 LYS C O   1 
ATOM   11645 C CB  . LYS C  1 395 ? -8.116   30.402  -70.873  1.00 52.59  ? 395 LYS C CB  1 
ATOM   11646 C CG  . LYS C  1 395 ? -8.050   29.193  -71.838  1.00 63.84  ? 395 LYS C CG  1 
ATOM   11647 C CD  . LYS C  1 395 ? -7.203   29.481  -73.086  1.00 74.22  ? 395 LYS C CD  1 
ATOM   11648 C CE  . LYS C  1 395 ? -7.362   28.554  -74.269  1.00 76.08  ? 395 LYS C CE  1 
ATOM   11649 N NZ  . LYS C  1 395 ? -6.957   27.184  -73.948  1.00 73.92  ? 395 LYS C NZ  1 
ATOM   11650 N N   . ILE C  1 396 ? -6.816   33.389  -70.355  1.00 38.10  ? 396 ILE C N   1 
ATOM   11651 C CA  . ILE C  1 396 ? -7.035   34.730  -69.800  1.00 36.30  ? 396 ILE C CA  1 
ATOM   11652 C C   . ILE C  1 396 ? -8.538   34.986  -69.721  1.00 33.35  ? 396 ILE C C   1 
ATOM   11653 O O   . ILE C  1 396 ? -9.246   34.713  -70.673  1.00 35.73  ? 396 ILE C O   1 
ATOM   11654 C CB  . ILE C  1 396 ? -6.229   35.829  -70.544  1.00 36.23  ? 396 ILE C CB  1 
ATOM   11655 C CG1 . ILE C  1 396 ? -4.697   35.653  -70.274  1.00 39.90  ? 396 ILE C CG1 1 
ATOM   11656 C CG2 . ILE C  1 396 ? -6.672   37.231  -70.120  1.00 34.58  ? 396 ILE C CG2 1 
ATOM   11657 C CD1 . ILE C  1 396 ? -3.728   36.375  -71.214  1.00 40.58  ? 396 ILE C CD1 1 
ATOM   11658 N N   . ILE C  1 397 ? -9.038   35.404  -68.555  1.00 31.36  ? 397 ILE C N   1 
ATOM   11659 C CA  . ILE C  1 397 ? -10.471  35.636  -68.411  1.00 31.47  ? 397 ILE C CA  1 
ATOM   11660 C C   . ILE C  1 397 ? -10.766  37.108  -68.187  1.00 29.43  ? 397 ILE C C   1 
ATOM   11661 O O   . ILE C  1 397 ? -11.913  37.505  -68.297  1.00 27.38  ? 397 ILE C O   1 
ATOM   11662 C CB  . ILE C  1 397 ? -11.114  34.775  -67.300  1.00 32.36  ? 397 ILE C CB  1 
ATOM   11663 C CG1 . ILE C  1 397 ? -10.491  35.033  -65.959  1.00 32.84  ? 397 ILE C CG1 1 
ATOM   11664 C CG2 . ILE C  1 397 ? -11.089  33.290  -67.677  1.00 34.49  ? 397 ILE C CG2 1 
ATOM   11665 C CD1 . ILE C  1 397 ? -11.143  34.285  -64.818  1.00 33.81  ? 397 ILE C CD1 1 
ATOM   11666 N N   . LYS C  1 398 ? -9.741   37.900  -67.843  1.00 31.81  ? 398 LYS C N   1 
ATOM   11667 C CA  . LYS C  1 398 ? -9.878   39.349  -67.721  1.00 29.15  ? 398 LYS C CA  1 
ATOM   11668 C C   . LYS C  1 398 ? -8.527   40.004  -68.004  1.00 30.80  ? 398 LYS C C   1 
ATOM   11669 O O   . LYS C  1 398 ? -7.491   39.540  -67.534  1.00 30.73  ? 398 LYS C O   1 
ATOM   11670 C CB  . LYS C  1 398 ? -10.337  39.707  -66.306  1.00 27.60  ? 398 LYS C CB  1 
ATOM   11671 C CG  . LYS C  1 398 ? -10.626  41.176  -66.088  1.00 26.72  ? 398 LYS C CG  1 
ATOM   11672 C CD  . LYS C  1 398 ? -10.922  41.585  -64.654  1.00 25.56  ? 398 LYS C CD  1 
ATOM   11673 C CE  . LYS C  1 398 ? -11.135  43.056  -64.635  1.00 25.19  ? 398 LYS C CE  1 
ATOM   11674 N NZ  . LYS C  1 398 ? -11.471  43.548  -63.297  1.00 24.90  ? 398 LYS C NZ  1 
ATOM   11675 N N   . ASN C  1 399 ? -8.563   41.057  -68.820  1.00 32.32  ? 399 ASN C N   1 
ATOM   11676 C CA  . ASN C  1 399 ? -7.478   42.019  -68.958  1.00 32.64  ? 399 ASN C CA  1 
ATOM   11677 C C   . ASN C  1 399 ? -7.888   43.305  -68.268  1.00 31.69  ? 399 ASN C C   1 
ATOM   11678 O O   . ASN C  1 399 ? -9.047   43.690  -68.400  1.00 33.33  ? 399 ASN C O   1 
ATOM   11679 C CB  . ASN C  1 399 ? -7.225   42.362  -70.420  1.00 33.21  ? 399 ASN C CB  1 
ATOM   11680 C CG  . ASN C  1 399 ? -6.684   41.184  -71.190  1.00 33.93  ? 399 ASN C CG  1 
ATOM   11681 O OD1 . ASN C  1 399 ? -7.339   40.666  -72.102  1.00 33.36  ? 399 ASN C OD1 1 
ATOM   11682 N ND2 . ASN C  1 399 ? -5.485   40.750  -70.837  1.00 35.48  ? 399 ASN C ND2 1 
ATOM   11683 N N   . GLU C  1 400 ? -6.970   43.943  -67.529  1.00 31.65  ? 400 GLU C N   1 
ATOM   11684 C CA  . GLU C  1 400 ? -7.251   45.276  -67.010  1.00 32.06  ? 400 GLU C CA  1 
ATOM   11685 C C   . GLU C  1 400 ? -5.947   46.094  -66.891  1.00 32.90  ? 400 GLU C C   1 
ATOM   11686 O O   . GLU C  1 400 ? -4.927   45.592  -66.447  1.00 34.53  ? 400 GLU C O   1 
ATOM   11687 C CB  . GLU C  1 400 ? -8.091   45.204  -65.734  1.00 31.67  ? 400 GLU C CB  1 
ATOM   11688 C CG  . GLU C  1 400 ? -8.526   46.587  -65.258  1.00 32.83  ? 400 GLU C CG  1 
ATOM   11689 C CD  . GLU C  1 400 ? -9.421   46.692  -64.036  1.00 34.19  ? 400 GLU C CD  1 
ATOM   11690 O OE1 . GLU C  1 400 ? -9.604   45.679  -63.331  1.00 29.87  ? 400 GLU C OE1 1 
ATOM   11691 O OE2 . GLU C  1 400 ? -9.901   47.840  -63.778  1.00 37.45  ? 400 GLU C OE2 1 
ATOM   11692 N N   . SER C  1 401 ? -5.966   47.362  -67.337  1.00 31.53  ? 401 SER C N   1 
ATOM   11693 C CA  . SER C  1 401 ? -4.808   48.241  -67.233  1.00 31.13  ? 401 SER C CA  1 
ATOM   11694 C C   . SER C  1 401 ? -4.919   49.097  -65.970  1.00 31.44  ? 401 SER C C   1 
ATOM   11695 O O   . SER C  1 401 ? -6.018   49.570  -65.609  1.00 30.69  ? 401 SER C O   1 
ATOM   11696 C CB  . SER C  1 401 ? -4.669   49.135  -68.442  1.00 31.92  ? 401 SER C CB  1 
ATOM   11697 O OG  . SER C  1 401 ? -4.313   48.457  -69.635  1.00 32.83  ? 401 SER C OG  1 
ATOM   11698 N N   . ILE C  1 402 ? -3.768   49.297  -65.309  1.00 30.88  ? 402 ILE C N   1 
ATOM   11699 C CA  . ILE C  1 402 ? -3.651   50.318  -64.279  1.00 31.30  ? 402 ILE C CA  1 
ATOM   11700 C C   . ILE C  1 402 ? -2.579   51.325  -64.720  1.00 30.57  ? 402 ILE C C   1 
ATOM   11701 O O   . ILE C  1 402 ? -1.416   50.972  -64.859  1.00 30.42  ? 402 ILE C O   1 
ATOM   11702 C CB  . ILE C  1 402 ? -3.324   49.698  -62.903  1.00 32.91  ? 402 ILE C CB  1 
ATOM   11703 C CG1 . ILE C  1 402 ? -4.336   48.668  -62.425  1.00 32.46  ? 402 ILE C CG1 1 
ATOM   11704 C CG2 . ILE C  1 402 ? -3.148   50.794  -61.852  1.00 34.45  ? 402 ILE C CG2 1 
ATOM   11705 C CD1 . ILE C  1 402 ? -5.718   49.235  -62.121  1.00 32.57  ? 402 ILE C CD1 1 
ATOM   11706 N N   . ASN C  1 403 ? -2.985   52.588  -64.924  1.00 30.95  ? 403 ASN C N   1 
ATOM   11707 C CA  . ASN C  1 403 ? -2.100   53.640  -65.398  1.00 29.28  ? 403 ASN C CA  1 
ATOM   11708 C C   . ASN C  1 403 ? -1.502   54.382  -64.209  1.00 27.81  ? 403 ASN C C   1 
ATOM   11709 O O   . ASN C  1 403 ? -2.217   54.996  -63.412  1.00 26.05  ? 403 ASN C O   1 
ATOM   11710 C CB  . ASN C  1 403 ? -2.837   54.636  -66.301  1.00 29.68  ? 403 ASN C CB  1 
ATOM   11711 C CG  . ASN C  1 403 ? -3.238   54.027  -67.621  1.00 30.21  ? 403 ASN C CG  1 
ATOM   11712 O OD1 . ASN C  1 403 ? -2.405   53.793  -68.489  1.00 32.48  ? 403 ASN C OD1 1 
ATOM   11713 N ND2 . ASN C  1 403 ? -4.501   53.696  -67.786  1.00 31.25  ? 403 ASN C ND2 1 
ATOM   11714 N N   . ILE C  1 404 ? -0.171   54.403  -64.162  1.00 28.02  ? 404 ILE C N   1 
ATOM   11715 C CA  . ILE C  1 404 ? 0.531    55.127  -63.119  1.00 28.54  ? 404 ILE C CA  1 
ATOM   11716 C C   . ILE C  1 404 ? 1.560    56.061  -63.734  1.00 29.23  ? 404 ILE C C   1 
ATOM   11717 O O   . ILE C  1 404 ? 1.912    55.939  -64.910  1.00 28.27  ? 404 ILE C O   1 
ATOM   11718 C CB  . ILE C  1 404 ? 1.183    54.186  -62.097  1.00 29.00  ? 404 ILE C CB  1 
ATOM   11719 C CG1 . ILE C  1 404 ? 2.443    53.516  -62.644  1.00 29.45  ? 404 ILE C CG1 1 
ATOM   11720 C CG2 . ILE C  1 404 ? 0.127    53.171  -61.629  1.00 29.67  ? 404 ILE C CG2 1 
ATOM   11721 C CD1 . ILE C  1 404 ? 3.166    52.623  -61.638  1.00 30.49  ? 404 ILE C CD1 1 
ATOM   11722 N N   . LEU C  1 405 ? 2.005    56.987  -62.873  1.00 29.74  ? 405 LEU C N   1 
ATOM   11723 C CA  . LEU C  1 405 ? 3.093    57.896  -63.154  1.00 30.90  ? 405 LEU C CA  1 
ATOM   11724 C C   . LEU C  1 405 ? 4.174    57.659  -62.104  1.00 31.72  ? 405 LEU C C   1 
ATOM   11725 O O   . LEU C  1 405 ? 3.943    57.815  -60.912  1.00 32.50  ? 405 LEU C O   1 
ATOM   11726 C CB  . LEU C  1 405 ? 2.518    59.318  -63.149  1.00 30.78  ? 405 LEU C CB  1 
ATOM   11727 C CG  . LEU C  1 405 ? 3.464    60.431  -63.593  1.00 32.07  ? 405 LEU C CG  1 
ATOM   11728 C CD1 . LEU C  1 405 ? 4.015    60.138  -64.976  1.00 32.13  ? 405 LEU C CD1 1 
ATOM   11729 C CD2 . LEU C  1 405 ? 2.788    61.815  -63.534  1.00 32.13  ? 405 LEU C CD2 1 
ATOM   11730 N N   . ALA C  1 406 ? 5.374    57.267  -62.532  1.00 32.25  ? 406 ALA C N   1 
ATOM   11731 C CA  . ALA C  1 406 ? 6.334    56.747  -61.571  1.00 33.01  ? 406 ALA C CA  1 
ATOM   11732 C C   . ALA C  1 406 ? 7.685    57.408  -61.765  1.00 33.63  ? 406 ALA C C   1 
ATOM   11733 O O   . ALA C  1 406 ? 8.066    57.812  -62.869  1.00 33.39  ? 406 ALA C O   1 
ATOM   11734 C CB  . ALA C  1 406 ? 6.424    55.227  -61.681  1.00 32.84  ? 406 ALA C CB  1 
ATOM   11735 N N   . SER C  1 407 ? 8.400    57.502  -60.650  1.00 35.08  ? 407 SER C N   1 
ATOM   11736 C CA  . SER C  1 407 ? 9.768    57.980  -60.658  1.00 36.59  ? 407 SER C CA  1 
ATOM   11737 C C   . SER C  1 407 ? 10.472   57.486  -59.404  1.00 37.71  ? 407 SER C C   1 
ATOM   11738 O O   . SER C  1 407 ? 9.828    57.220  -58.404  1.00 37.44  ? 407 SER C O   1 
ATOM   11739 C CB  . SER C  1 407 ? 9.804    59.494  -60.779  1.00 36.40  ? 407 SER C CB  1 
ATOM   11740 O OG  . SER C  1 407 ? 11.139   59.930  -60.619  1.00 36.88  ? 407 SER C OG  1 
ATOM   11741 N N   . LYS C  1 408 ? 11.790   57.328  -59.485  1.00 40.31  ? 408 LYS C N   1 
ATOM   11742 C CA  . LYS C  1 408 ? 12.594   57.008  -58.319  1.00 42.97  ? 408 LYS C CA  1 
ATOM   11743 C C   . LYS C  1 408 ? 12.902   58.277  -57.535  1.00 44.66  ? 408 LYS C C   1 
ATOM   11744 O O   . LYS C  1 408 ? 13.469   58.186  -56.464  1.00 46.45  ? 408 LYS C O   1 
ATOM   11745 C CB  . LYS C  1 408 ? 13.967   56.446  -58.689  1.00 45.50  ? 408 LYS C CB  1 
ATOM   11746 C CG  . LYS C  1 408 ? 13.918   55.095  -59.350  1.00 47.06  ? 408 LYS C CG  1 
ATOM   11747 C CD  . LYS C  1 408 ? 15.247   54.658  -59.934  1.00 50.89  ? 408 LYS C CD  1 
ATOM   11748 C CE  . LYS C  1 408 ? 15.069   53.321  -60.564  1.00 54.22  ? 408 LYS C CE  1 
ATOM   11749 N NZ  . LYS C  1 408 ? 16.210   53.044  -61.442  1.00 58.90  ? 408 LYS C NZ  1 
ATOM   11750 N N   . THR C  1 409 ? 12.594   59.457  -58.083  1.00 44.61  ? 409 THR C N   1 
ATOM   11751 C CA  . THR C  1 409 ? 12.865   60.684  -57.357  1.00 46.53  ? 409 THR C CA  1 
ATOM   11752 C C   . THR C  1 409 ? 11.575   61.501  -57.278  1.00 46.18  ? 409 THR C C   1 
ATOM   11753 O O   . THR C  1 409 ? 10.578   61.200  -57.936  1.00 43.95  ? 409 THR C O   1 
ATOM   11754 C CB  . THR C  1 409 ? 14.068   61.450  -57.929  1.00 47.35  ? 409 THR C CB  1 
ATOM   11755 O OG1 . THR C  1 409 ? 13.832   61.766  -59.288  1.00 46.51  ? 409 THR C OG1 1 
ATOM   11756 C CG2 . THR C  1 409 ? 15.369   60.665  -57.881  1.00 48.34  ? 409 THR C CG2 1 
ATOM   11757 N N   . ALA C  1 410 ? 11.569   62.452  -56.337  1.00 47.53  ? 410 ALA C N   1 
ATOM   11758 C CA  . ALA C  1 410 ? 10.468   63.384  -56.206  1.00 47.62  ? 410 ALA C CA  1 
ATOM   11759 C C   . ALA C  1 410 ? 10.417   64.195  -57.487  1.00 47.02  ? 410 ALA C C   1 
ATOM   11760 O O   . ALA C  1 410 ? 11.432   64.256  -58.178  1.00 48.39  ? 410 ALA C O   1 
ATOM   11761 C CB  . ALA C  1 410 ? 10.685   64.277  -55.010  1.00 49.17  ? 410 ALA C CB  1 
ATOM   11762 N N   . PHE C  1 411 ? 9.247    64.771  -57.794  1.00 45.76  ? 411 PHE C N   1 
ATOM   11763 C CA  . PHE C  1 411 ? 9.136    65.734  -58.883  1.00 44.92  ? 411 PHE C CA  1 
ATOM   11764 C C   . PHE C  1 411 ? 7.985    66.694  -58.600  1.00 44.57  ? 411 PHE C C   1 
ATOM   11765 O O   . PHE C  1 411 ? 7.100    66.381  -57.814  1.00 43.07  ? 411 PHE C O   1 
ATOM   11766 C CB  . PHE C  1 411 ? 9.002    64.978  -60.210  1.00 43.16  ? 411 PHE C CB  1 
ATOM   11767 C CG  . PHE C  1 411 ? 7.873    63.963  -60.284  1.00 41.69  ? 411 PHE C CG  1 
ATOM   11768 C CD1 . PHE C  1 411 ? 8.036    62.672  -59.805  1.00 40.90  ? 411 PHE C CD1 1 
ATOM   11769 C CD2 . PHE C  1 411 ? 6.660    64.295  -60.873  1.00 41.94  ? 411 PHE C CD2 1 
ATOM   11770 C CE1 . PHE C  1 411 ? 6.996    61.751  -59.897  1.00 40.07  ? 411 PHE C CE1 1 
ATOM   11771 C CE2 . PHE C  1 411 ? 5.631    63.358  -60.979  1.00 38.93  ? 411 PHE C CE2 1 
ATOM   11772 C CZ  . PHE C  1 411 ? 5.803    62.094  -60.485  1.00 38.73  ? 411 PHE C CZ  1 
ATOM   11773 N N   . GLU C  1 412 ? 8.019    67.861  -59.251  1.00 45.98  ? 412 GLU C N   1 
ATOM   11774 C CA  . GLU C  1 412 ? 6.952    68.848  -59.132  1.00 47.75  ? 412 GLU C CA  1 
ATOM   11775 C C   . GLU C  1 412 ? 5.848    68.565  -60.149  1.00 43.91  ? 412 GLU C C   1 
ATOM   11776 O O   . GLU C  1 412 ? 6.096    68.396  -61.345  1.00 41.59  ? 412 GLU C O   1 
ATOM   11777 C CB  . GLU C  1 412 ? 7.406    70.297  -59.344  1.00 50.55  ? 412 GLU C CB  1 
ATOM   11778 C CG  . GLU C  1 412 ? 8.523    70.714  -58.399  1.00 56.43  ? 412 GLU C CG  1 
ATOM   11779 C CD  . GLU C  1 412 ? 9.155    72.065  -58.746  1.00 65.80  ? 412 GLU C CD  1 
ATOM   11780 O OE1 . GLU C  1 412 ? 8.840    72.756  -59.763  1.00 65.54  ? 412 GLU C OE1 1 
ATOM   11781 O OE2 . GLU C  1 412 ? 10.012   72.446  -57.925  1.00 72.02  ? 412 GLU C OE2 1 
ATOM   11782 N N   . LEU C  1 413 ? 4.617    68.533  -59.636  1.00 43.56  ? 413 LEU C N   1 
ATOM   11783 C CA  . LEU C  1 413 ? 3.420    68.567  -60.455  1.00 42.98  ? 413 LEU C CA  1 
ATOM   11784 C C   . LEU C  1 413 ? 3.014    70.027  -60.614  1.00 42.49  ? 413 LEU C C   1 
ATOM   11785 O O   . LEU C  1 413 ? 3.430    70.876  -59.837  1.00 43.53  ? 413 LEU C O   1 
ATOM   11786 C CB  . LEU C  1 413 ? 2.270    67.796  -59.812  1.00 42.56  ? 413 LEU C CB  1 
ATOM   11787 C CG  . LEU C  1 413 ? 2.481    66.306  -59.579  1.00 43.40  ? 413 LEU C CG  1 
ATOM   11788 C CD1 . LEU C  1 413 ? 1.393    65.762  -58.676  1.00 43.54  ? 413 LEU C CD1 1 
ATOM   11789 C CD2 . LEU C  1 413 ? 2.503    65.548  -60.891  1.00 43.79  ? 413 LEU C CD2 1 
ATOM   11790 N N   . PRO C  1 414 ? 2.191    70.360  -61.628  1.00 42.04  ? 414 PRO C N   1 
ATOM   11791 C CA  . PRO C  1 414 ? 1.495    71.641  -61.657  1.00 42.87  ? 414 PRO C CA  1 
ATOM   11792 C C   . PRO C  1 414 ? 0.351    71.586  -60.653  1.00 41.13  ? 414 PRO C C   1 
ATOM   11793 O O   . PRO C  1 414 ? -0.167   70.505  -60.376  1.00 41.86  ? 414 PRO C O   1 
ATOM   11794 C CB  . PRO C  1 414 ? 1.057    71.757  -63.125  1.00 42.78  ? 414 PRO C CB  1 
ATOM   11795 C CG  . PRO C  1 414 ? 0.830    70.340  -63.541  1.00 41.85  ? 414 PRO C CG  1 
ATOM   11796 C CD  . PRO C  1 414 ? 1.912    69.548  -62.819  1.00 42.50  ? 414 PRO C CD  1 
ATOM   11797 N N   . GLU C  1 415 ? 0.024    72.754  -60.087  1.00 41.66  ? 415 GLU C N   1 
ATOM   11798 C CA  . GLU C  1 415 ? -0.869   72.880  -58.944  1.00 42.30  ? 415 GLU C CA  1 
ATOM   11799 C C   . GLU C  1 415 ? -1.893   73.972  -59.213  1.00 39.92  ? 415 GLU C C   1 
ATOM   11800 O O   . GLU C  1 415 ? -1.546   75.078  -59.600  1.00 38.57  ? 415 GLU C O   1 
ATOM   11801 C CB  . GLU C  1 415 ? -0.208   73.320  -57.638  1.00 46.20  ? 415 GLU C CB  1 
ATOM   11802 C CG  . GLU C  1 415 ? 0.877    72.377  -57.138  1.00 51.06  ? 415 GLU C CG  1 
ATOM   11803 C CD  . GLU C  1 415 ? 1.763    72.968  -56.046  1.00 59.36  ? 415 GLU C CD  1 
ATOM   11804 O OE1 . GLU C  1 415 ? 2.057    74.196  -56.077  1.00 54.59  ? 415 GLU C OE1 1 
ATOM   11805 O OE2 . GLU C  1 415 ? 2.181    72.154  -55.173  1.00 64.77  ? 415 GLU C OE2 1 
ATOM   11806 N N   . LEU C  1 416 ? -3.152   73.625  -58.973  1.00 39.37  ? 416 LEU C N   1 
ATOM   11807 C CA  . LEU C  1 416 ? -4.272   74.535  -59.083  1.00 39.77  ? 416 LEU C CA  1 
ATOM   11808 C C   . LEU C  1 416 ? -4.840   74.764  -57.684  1.00 39.70  ? 416 LEU C C   1 
ATOM   11809 O O   . LEU C  1 416 ? -5.297   73.820  -57.050  1.00 39.68  ? 416 LEU C O   1 
ATOM   11810 C CB  . LEU C  1 416 ? -5.290   73.874  -60.027  1.00 37.91  ? 416 LEU C CB  1 
ATOM   11811 C CG  . LEU C  1 416 ? -6.507   74.715  -60.435  1.00 37.15  ? 416 LEU C CG  1 
ATOM   11812 C CD1 . LEU C  1 416 ? -7.158   74.126  -61.653  1.00 36.39  ? 416 LEU C CD1 1 
ATOM   11813 C CD2 . LEU C  1 416 ? -7.534   74.831  -59.314  1.00 37.67  ? 416 LEU C CD2 1 
ATOM   11814 N N   . THR C  1 417 ? -4.880   76.023  -57.242  1.00 39.86  ? 417 THR C N   1 
ATOM   11815 C CA  . THR C  1 417 ? -5.513   76.385  -55.980  1.00 39.98  ? 417 THR C CA  1 
ATOM   11816 C C   . THR C  1 417 ? -6.547   77.461  -56.291  1.00 38.53  ? 417 THR C C   1 
ATOM   11817 O O   . THR C  1 417 ? -6.437   78.132  -57.312  1.00 38.05  ? 417 THR C O   1 
ATOM   11818 C CB  . THR C  1 417 ? -4.472   76.813  -54.929  1.00 42.83  ? 417 THR C CB  1 
ATOM   11819 O OG1 . THR C  1 417 ? -3.642   77.864  -55.413  1.00 43.54  ? 417 THR C OG1 1 
ATOM   11820 C CG2 . THR C  1 417 ? -3.525   75.675  -54.555  1.00 43.61  ? 417 THR C CG2 1 
ATOM   11821 N N   . ILE C  1 418 ? -7.561   77.604  -55.434  1.00 38.95  ? 418 ILE C N   1 
ATOM   11822 C CA  . ILE C  1 418 ? -8.575   78.639  -55.628  1.00 41.11  ? 418 ILE C CA  1 
ATOM   11823 C C   . ILE C  1 418 ? -8.717   79.468  -54.352  1.00 42.10  ? 418 ILE C C   1 
ATOM   11824 O O   . ILE C  1 418 ? -8.416   79.017  -53.250  1.00 42.16  ? 418 ILE C O   1 
ATOM   11825 C CB  . ILE C  1 418 ? -9.928   78.069  -56.117  1.00 39.48  ? 418 ILE C CB  1 
ATOM   11826 C CG1 . ILE C  1 418 ? -10.558  77.133  -55.105  1.00 40.90  ? 418 ILE C CG1 1 
ATOM   11827 C CG2 . ILE C  1 418 ? -9.785   77.369  -57.466  1.00 37.42  ? 418 ILE C CG2 1 
ATOM   11828 C CD1 . ILE C  1 418 ? -11.862  76.498  -55.579  1.00 40.49  ? 418 ILE C CD1 1 
ATOM   11829 N N   . GLU C  1 419 ? -9.128   80.717  -54.553  1.00 43.48  ? 419 GLU C N   1 
ATOM   11830 C CA  . GLU C  1 419 ? -9.496   81.646  -53.491  1.00 45.50  ? 419 GLU C CA  1 
ATOM   11831 C C   . GLU C  1 419 ? -10.939  82.076  -53.753  1.00 43.02  ? 419 GLU C C   1 
ATOM   11832 O O   . GLU C  1 419 ? -11.228  82.601  -54.814  1.00 42.99  ? 419 GLU C O   1 
ATOM   11833 C CB  . GLU C  1 419 ? -8.630   82.911  -53.470  1.00 48.93  ? 419 GLU C CB  1 
ATOM   11834 C CG  . GLU C  1 419 ? -7.142   82.667  -53.222  1.00 52.73  ? 419 GLU C CG  1 
ATOM   11835 C CD  . GLU C  1 419 ? -6.418   83.973  -52.947  1.00 60.03  ? 419 GLU C CD  1 
ATOM   11836 O OE1 . GLU C  1 419 ? -6.354   84.917  -53.783  1.00 64.09  ? 419 GLU C OE1 1 
ATOM   11837 O OE2 . GLU C  1 419 ? -5.958   84.066  -51.798  1.00 67.23  ? 419 GLU C OE2 1 
ATOM   11838 N N   . VAL C  1 420 ? -11.848  81.803  -52.816  1.00 42.09  ? 420 VAL C N   1 
ATOM   11839 C CA  . VAL C  1 420 ? -13.275  82.001  -53.015  1.00 40.51  ? 420 VAL C CA  1 
ATOM   11840 C C   . VAL C  1 420 ? -13.732  83.136  -52.099  1.00 40.86  ? 420 VAL C C   1 
ATOM   11841 O O   . VAL C  1 420 ? -13.367  83.183  -50.935  1.00 40.19  ? 420 VAL C O   1 
ATOM   11842 C CB  . VAL C  1 420 ? -14.071  80.705  -52.765  1.00 40.02  ? 420 VAL C CB  1 
ATOM   11843 C CG1 . VAL C  1 420 ? -15.522  80.850  -53.218  1.00 40.22  ? 420 VAL C CG1 1 
ATOM   11844 C CG2 . VAL C  1 420 ? -13.427  79.486  -53.430  1.00 38.18  ? 420 VAL C CG2 1 
ATOM   11845 N N   . THR C  1 421 ? -14.484  84.086  -52.672  1.00 41.39  ? 421 THR C N   1 
ATOM   11846 C CA  . THR C  1 421 ? -15.172  85.132  -51.929  1.00 43.08  ? 421 THR C CA  1 
ATOM   11847 C C   . THR C  1 421 ? -16.675  84.937  -52.098  1.00 43.59  ? 421 THR C C   1 
ATOM   11848 O O   . THR C  1 421 ? -17.120  84.551  -53.178  1.00 42.26  ? 421 THR C O   1 
ATOM   11849 C CB  . THR C  1 421 ? -14.780  86.500  -52.478  1.00 43.74  ? 421 THR C CB  1 
ATOM   11850 O OG1 . THR C  1 421 ? -13.373  86.383  -52.359  1.00 44.63  ? 421 THR C OG1 1 
ATOM   11851 C CG2 . THR C  1 421 ? -15.402  87.657  -51.721  1.00 44.49  ? 421 THR C CG2 1 
ATOM   11852 N N   . PRO C  1 422 ? -17.506  85.149  -51.051  1.00 45.25  ? 422 PRO C N   1 
ATOM   11853 C CA  . PRO C  1 422 ? -17.071  85.067  -49.653  1.00 46.72  ? 422 PRO C CA  1 
ATOM   11854 C C   . PRO C  1 422 ? -16.473  83.714  -49.268  1.00 45.95  ? 422 PRO C C   1 
ATOM   11855 O O   . PRO C  1 422 ? -16.880  82.678  -49.796  1.00 45.12  ? 422 PRO C O   1 
ATOM   11856 C CB  . PRO C  1 422 ? -18.370  85.307  -48.901  1.00 47.72  ? 422 PRO C CB  1 
ATOM   11857 C CG  . PRO C  1 422 ? -19.206  86.100  -49.854  1.00 47.43  ? 422 PRO C CG  1 
ATOM   11858 C CD  . PRO C  1 422 ? -18.925  85.481  -51.191  1.00 45.30  ? 422 PRO C CD  1 
ATOM   11859 N N   . GLU C  1 423 ? -15.548  83.757  -48.306  1.00 48.14  ? 423 GLU C N   1 
ATOM   11860 C CA  . GLU C  1 423 ? -14.603  82.687  -48.020  1.00 49.83  ? 423 GLU C CA  1 
ATOM   11861 C C   . GLU C  1 423 ? -15.185  81.696  -47.013  1.00 50.43  ? 423 GLU C C   1 
ATOM   11862 O O   . GLU C  1 423 ? -14.884  80.518  -47.126  1.00 48.18  ? 423 GLU C O   1 
ATOM   11863 C CB  . GLU C  1 423 ? -13.340  83.358  -47.480  1.00 52.87  ? 423 GLU C CB  1 
ATOM   11864 C CG  . GLU C  1 423 ? -12.150  82.452  -47.167  1.00 53.60  ? 423 GLU C CG  1 
ATOM   11865 C CD  . GLU C  1 423 ? -11.032  83.273  -46.532  1.00 55.96  ? 423 GLU C CD  1 
ATOM   11866 O OE1 . GLU C  1 423 ? -11.069  84.538  -46.461  1.00 54.26  ? 423 GLU C OE1 1 
ATOM   11867 O OE2 . GLU C  1 423 ? -10.094  82.591  -46.090  1.00 58.70  ? 423 GLU C OE2 1 
ATOM   11868 N N   . LYS C  1 424 ? -15.999  82.191  -46.052  1.00 52.81  ? 424 LYS C N   1 
ATOM   11869 C CA  . LYS C  1 424 ? -16.431  81.431  -44.880  1.00 54.81  ? 424 LYS C CA  1 
ATOM   11870 C C   . LYS C  1 424 ? -17.911  81.626  -44.557  1.00 52.74  ? 424 LYS C C   1 
ATOM   11871 O O   . LYS C  1 424 ? -18.503  80.803  -43.868  1.00 52.57  ? 424 LYS C O   1 
ATOM   11872 C CB  . LYS C  1 424 ? -15.660  81.837  -43.616  1.00 60.58  ? 424 LYS C CB  1 
ATOM   11873 C CG  . LYS C  1 424 ? -14.149  81.661  -43.737  1.00 64.99  ? 424 LYS C CG  1 
ATOM   11874 C CD  . LYS C  1 424 ? -13.358  81.793  -42.445  1.00 68.67  ? 424 LYS C CD  1 
ATOM   11875 C CE  . LYS C  1 424 ? -13.052  83.193  -42.102  1.00 72.85  ? 424 LYS C CE  1 
ATOM   11876 N NZ  . LYS C  1 424 ? -12.265  83.179  -40.866  1.00 79.14  ? 424 LYS C NZ  1 
ATOM   11877 N N   . ASP C  1 425 ? -18.518  82.723  -45.015  1.00 51.97  ? 425 ASP C N   1 
ATOM   11878 C CA  . ASP C  1 425 ? -19.882  83.017  -44.614  1.00 50.88  ? 425 ASP C CA  1 
ATOM   11879 C C   . ASP C  1 425 ? -20.617  83.661  -45.777  1.00 49.55  ? 425 ASP C C   1 
ATOM   11880 O O   . ASP C  1 425 ? -20.333  84.813  -46.102  1.00 50.84  ? 425 ASP C O   1 
ATOM   11881 C CB  . ASP C  1 425 ? -19.908  83.838  -43.337  1.00 51.69  ? 425 ASP C CB  1 
ATOM   11882 C CG  . ASP C  1 425 ? -21.303  84.050  -42.771  1.00 52.53  ? 425 ASP C CG  1 
ATOM   11883 O OD1 . ASP C  1 425 ? -22.250  83.597  -43.454  1.00 49.91  ? 425 ASP C OD1 1 
ATOM   11884 O OD2 . ASP C  1 425 ? -21.432  84.731  -41.701  1.00 55.17  ? 425 ASP C OD2 1 
ATOM   11885 N N   . LEU C  1 426 ? -21.554  82.908  -46.379  1.00 47.44  ? 426 LEU C N   1 
ATOM   11886 C CA  . LEU C  1 426 ? -22.302  83.365  -47.543  1.00 47.38  ? 426 LEU C CA  1 
ATOM   11887 C C   . LEU C  1 426 ? -23.177  84.586  -47.225  1.00 49.53  ? 426 LEU C C   1 
ATOM   11888 O O   . LEU C  1 426 ? -23.629  85.260  -48.141  1.00 49.50  ? 426 LEU C O   1 
ATOM   11889 C CB  . LEU C  1 426 ? -23.163  82.256  -48.135  1.00 46.27  ? 426 LEU C CB  1 
ATOM   11890 C CG  . LEU C  1 426 ? -22.422  81.076  -48.764  1.00 44.96  ? 426 LEU C CG  1 
ATOM   11891 C CD1 . LEU C  1 426 ? -23.437  80.064  -49.227  1.00 45.32  ? 426 LEU C CD1 1 
ATOM   11892 C CD2 . LEU C  1 426 ? -21.518  81.453  -49.921  1.00 44.34  ? 426 LEU C CD2 1 
ATOM   11893 N N   . ASN C  1 427 ? -23.438  84.888  -45.948  1.00 50.59  ? 427 ASN C N   1 
ATOM   11894 C CA  . ASN C  1 427 ? -24.179  86.092  -45.630  1.00 52.00  ? 427 ASN C CA  1 
ATOM   11895 C C   . ASN C  1 427 ? -23.365  87.344  -45.949  1.00 53.77  ? 427 ASN C C   1 
ATOM   11896 O O   . ASN C  1 427 ? -23.930  88.436  -45.910  1.00 56.02  ? 427 ASN C O   1 
ATOM   11897 C CB  . ASN C  1 427 ? -24.600  86.175  -44.166  1.00 52.25  ? 427 ASN C CB  1 
ATOM   11898 C CG  . ASN C  1 427 ? -25.791  85.317  -43.832  1.00 50.78  ? 427 ASN C CG  1 
ATOM   11899 O OD1 . ASN C  1 427 ? -25.799  84.682  -42.772  1.00 50.00  ? 427 ASN C OD1 1 
ATOM   11900 N ND2 . ASN C  1 427 ? -26.817  85.334  -44.669  1.00 49.42  ? 427 ASN C ND2 1 
ATOM   11901 N N   . GLU C  1 428 ? -22.059  87.210  -46.223  1.00 54.34  ? 428 GLU C N   1 
ATOM   11902 C CA  . GLU C  1 428 ? -21.210  88.382  -46.428  1.00 56.87  ? 428 GLU C CA  1 
ATOM   11903 C C   . GLU C  1 428 ? -21.365  89.000  -47.823  1.00 55.28  ? 428 GLU C C   1 
ATOM   11904 O O   . GLU C  1 428 ? -20.673  89.955  -48.136  1.00 53.29  ? 428 GLU C O   1 
ATOM   11905 C CB  . GLU C  1 428 ? -19.738  88.045  -46.195  1.00 60.07  ? 428 GLU C CB  1 
ATOM   11906 C CG  . GLU C  1 428 ? -19.455  87.708  -44.733  1.00 65.40  ? 428 GLU C CG  1 
ATOM   11907 C CD  . GLU C  1 428 ? -18.007  87.871  -44.303  1.00 69.91  ? 428 GLU C CD  1 
ATOM   11908 O OE1 . GLU C  1 428 ? -17.247  88.483  -45.099  1.00 73.80  ? 428 GLU C OE1 1 
ATOM   11909 O OE2 . GLU C  1 428 ? -17.645  87.372  -43.203  1.00 70.63  ? 428 GLU C OE2 1 
ATOM   11910 N N   . GLY C  1 429 ? -22.220  88.430  -48.691  1.00 54.02  ? 429 GLY C N   1 
ATOM   11911 C CA  . GLY C  1 429 ? -22.425  88.988  -50.013  1.00 51.96  ? 429 GLY C CA  1 
ATOM   11912 C C   . GLY C  1 429 ? -23.585  88.336  -50.750  1.00 51.02  ? 429 GLY C C   1 
ATOM   11913 O O   . GLY C  1 429 ? -24.012  87.230  -50.408  1.00 53.23  ? 429 GLY C O   1 
ATOM   11914 N N   . LYS C  1 430 ? -24.038  89.023  -51.806  1.00 50.17  ? 430 LYS C N   1 
ATOM   11915 C CA  . LYS C  1 430 ? -24.970  88.481  -52.776  1.00 49.03  ? 430 LYS C CA  1 
ATOM   11916 C C   . LYS C  1 430 ? -24.227  87.911  -53.989  1.00 45.56  ? 430 LYS C C   1 
ATOM   11917 O O   . LYS C  1 430 ? -24.807  87.152  -54.764  1.00 43.76  ? 430 LYS C O   1 
ATOM   11918 C CB  . LYS C  1 430 ? -25.987  89.558  -53.167  1.00 52.32  ? 430 LYS C CB  1 
ATOM   11919 C CG  . LYS C  1 430 ? -27.161  89.704  -52.224  1.00 56.18  ? 430 LYS C CG  1 
ATOM   11920 C CD  . LYS C  1 430 ? -28.091  90.799  -52.739  1.00 63.62  ? 430 LYS C CD  1 
ATOM   11921 C CE  . LYS C  1 430 ? -28.958  91.455  -51.689  1.00 69.79  ? 430 LYS C CE  1 
ATOM   11922 N NZ  . LYS C  1 430 ? -29.749  90.423  -51.007  1.00 75.52  ? 430 LYS C NZ  1 
ATOM   11923 N N   . ILE C  1 431 ? -22.953  88.272  -54.165  1.00 44.04  ? 431 ILE C N   1 
ATOM   11924 C CA  . ILE C  1 431 ? -22.177  87.838  -55.314  1.00 42.39  ? 431 ILE C CA  1 
ATOM   11925 C C   . ILE C  1 431 ? -20.899  87.155  -54.839  1.00 41.64  ? 431 ILE C C   1 
ATOM   11926 O O   . ILE C  1 431 ? -20.323  87.550  -53.841  1.00 40.93  ? 431 ILE C O   1 
ATOM   11927 C CB  . ILE C  1 431 ? -21.869  89.017  -56.250  1.00 42.82  ? 431 ILE C CB  1 
ATOM   11928 C CG1 . ILE C  1 431 ? -23.137  89.677  -56.713  1.00 43.48  ? 431 ILE C CG1 1 
ATOM   11929 C CG2 . ILE C  1 431 ? -21.038  88.558  -57.443  1.00 42.14  ? 431 ILE C CG2 1 
ATOM   11930 C CD1 . ILE C  1 431 ? -22.937  91.063  -57.295  1.00 44.85  ? 431 ILE C CD1 1 
ATOM   11931 N N   . ALA C  1 432 ? -20.499  86.091  -55.551  1.00 41.41  ? 432 ALA C N   1 
ATOM   11932 C CA  . ALA C  1 432 ? -19.307  85.320  -55.222  1.00 41.74  ? 432 ALA C CA  1 
ATOM   11933 C C   . ALA C  1 432 ? -18.296  85.439  -56.356  1.00 42.06  ? 432 ALA C C   1 
ATOM   11934 O O   . ALA C  1 432 ? -18.681  85.747  -57.480  1.00 42.35  ? 432 ALA C O   1 
ATOM   11935 C CB  . ALA C  1 432 ? -19.659  83.863  -55.008  1.00 40.99  ? 432 ALA C CB  1 
ATOM   11936 N N   . SER C  1 433 ? -17.022  85.174  -56.048  1.00 41.93  ? 433 SER C N   1 
ATOM   11937 C CA  . SER C  1 433 ? -16.027  84.940  -57.074  1.00 42.43  ? 433 SER C CA  1 
ATOM   11938 C C   . SER C  1 433 ? -15.165  83.722  -56.745  1.00 40.75  ? 433 SER C C   1 
ATOM   11939 O O   . SER C  1 433 ? -14.963  83.375  -55.592  1.00 38.73  ? 433 SER C O   1 
ATOM   11940 C CB  . SER C  1 433 ? -15.148  86.141  -57.269  1.00 45.68  ? 433 SER C CB  1 
ATOM   11941 O OG  . SER C  1 433 ? -14.290  86.338  -56.151  1.00 48.71  ? 433 SER C OG  1 
ATOM   11942 N N   . ILE C  1 434 ? -14.583  83.148  -57.795  1.00 40.22  ? 434 ILE C N   1 
ATOM   11943 C CA  . ILE C  1 434 ? -13.548  82.141  -57.656  1.00 40.97  ? 434 ILE C CA  1 
ATOM   11944 C C   . ILE C  1 434 ? -12.328  82.624  -58.420  1.00 41.68  ? 434 ILE C C   1 
ATOM   11945 O O   . ILE C  1 434 ? -12.388  82.745  -59.637  1.00 43.47  ? 434 ILE C O   1 
ATOM   11946 C CB  . ILE C  1 434 ? -14.046  80.793  -58.198  1.00 39.18  ? 434 ILE C CB  1 
ATOM   11947 C CG1 . ILE C  1 434 ? -15.200  80.230  -57.320  1.00 39.23  ? 434 ILE C CG1 1 
ATOM   11948 C CG2 . ILE C  1 434 ? -12.867  79.836  -58.334  1.00 39.12  ? 434 ILE C CG2 1 
ATOM   11949 C CD1 . ILE C  1 434 ? -15.964  79.046  -57.918  1.00 39.64  ? 434 ILE C CD1 1 
ATOM   11950 N N   . LYS C  1 435 ? -11.241  82.913  -57.699  1.00 43.47  ? 435 LYS C N   1 
ATOM   11951 C CA  . LYS C  1 435 ? -9.959   83.244  -58.310  1.00 43.31  ? 435 LYS C CA  1 
ATOM   11952 C C   . LYS C  1 435 ? -9.114   81.975  -58.400  1.00 43.14  ? 435 LYS C C   1 
ATOM   11953 O O   . LYS C  1 435 ? -8.695   81.454  -57.372  1.00 44.97  ? 435 LYS C O   1 
ATOM   11954 C CB  . LYS C  1 435 ? -9.274   84.323  -57.469  1.00 44.73  ? 435 LYS C CB  1 
ATOM   11955 C CG  . LYS C  1 435 ? -9.990   85.679  -57.467  1.00 46.44  ? 435 LYS C CG  1 
ATOM   11956 C CD  . LYS C  1 435 ? -9.222   86.882  -56.918  1.00 46.80  ? 435 LYS C CD  1 
ATOM   11957 C CE  . LYS C  1 435 ? -9.122   86.796  -55.448  1.00 47.92  ? 435 LYS C CE  1 
ATOM   11958 N NZ  . LYS C  1 435 ? -8.784   88.106  -54.921  1.00 49.71  ? 435 LYS C NZ  1 
ATOM   11959 N N   . THR C  1 436 ? -8.906   81.462  -59.619  1.00 41.92  ? 436 THR C N   1 
ATOM   11960 C CA  . THR C  1 436 ? -8.088   80.274  -59.834  1.00 42.07  ? 436 THR C CA  1 
ATOM   11961 C C   . THR C  1 436 ? -6.629   80.664  -60.091  1.00 42.06  ? 436 THR C C   1 
ATOM   11962 O O   . THR C  1 436 ? -6.375   81.581  -60.849  1.00 41.81  ? 436 THR C O   1 
ATOM   11963 C CB  . THR C  1 436 ? -8.664   79.511  -61.024  1.00 41.26  ? 436 THR C CB  1 
ATOM   11964 O OG1 . THR C  1 436 ? -10.007  79.233  -60.636  1.00 39.51  ? 436 THR C OG1 1 
ATOM   11965 C CG2 . THR C  1 436 ? -7.857   78.265  -61.344  1.00 41.39  ? 436 THR C CG2 1 
ATOM   11966 N N   . LYS C  1 437 ? -5.682   79.900  -59.531  1.00 42.76  ? 437 LYS C N   1 
ATOM   11967 C CA  . LYS C  1 437 ? -4.258   80.068  -59.799  1.00 43.89  ? 437 LYS C CA  1 
ATOM   11968 C C   . LYS C  1 437 ? -3.621   78.722  -60.171  1.00 42.23  ? 437 LYS C C   1 
ATOM   11969 O O   . LYS C  1 437 ? -3.671   77.780  -59.393  1.00 43.08  ? 437 LYS C O   1 
ATOM   11970 C CB  . LYS C  1 437 ? -3.667   80.684  -58.529  1.00 46.85  ? 437 LYS C CB  1 
ATOM   11971 C CG  . LYS C  1 437 ? -2.171   80.886  -58.504  1.00 49.62  ? 437 LYS C CG  1 
ATOM   11972 C CD  . LYS C  1 437 ? -1.607   81.206  -57.122  1.00 52.53  ? 437 LYS C CD  1 
ATOM   11973 C CE  . LYS C  1 437 ? -0.158   80.796  -57.011  1.00 54.68  ? 437 LYS C CE  1 
ATOM   11974 N NZ  . LYS C  1 437 ? 0.564    81.426  -55.902  1.00 56.66  ? 437 LYS C NZ  1 
ATOM   11975 N N   . ILE C  1 438 ? -3.054   78.619  -61.377  1.00 40.76  ? 438 ILE C N   1 
ATOM   11976 C CA  . ILE C  1 438 ? -2.365   77.416  -61.817  1.00 40.58  ? 438 ILE C CA  1 
ATOM   11977 C C   . ILE C  1 438 ? -0.860   77.687  -61.913  1.00 40.90  ? 438 ILE C C   1 
ATOM   11978 O O   . ILE C  1 438 ? -0.421   78.496  -62.725  1.00 40.77  ? 438 ILE C O   1 
ATOM   11979 C CB  . ILE C  1 438 ? -2.917   76.874  -63.153  1.00 40.10  ? 438 ILE C CB  1 
ATOM   11980 C CG1 . ILE C  1 438 ? -4.425   76.700  -63.145  1.00 39.30  ? 438 ILE C CG1 1 
ATOM   11981 C CG2 . ILE C  1 438 ? -2.255   75.548  -63.534  1.00 39.62  ? 438 ILE C CG2 1 
ATOM   11982 C CD1 . ILE C  1 438 ? -5.029   76.757  -64.532  1.00 38.43  ? 438 ILE C CD1 1 
ATOM   11983 N N   . GLU C  1 439 ? -0.077   76.973  -61.088  1.00 41.42  ? 439 GLU C N   1 
ATOM   11984 C CA  . GLU C  1 439 ? 1.378    76.941  -61.190  1.00 42.62  ? 439 GLU C CA  1 
ATOM   11985 C C   . GLU C  1 439 ? 1.766    75.889  -62.215  1.00 41.67  ? 439 GLU C C   1 
ATOM   11986 O O   . GLU C  1 439 ? 1.440    74.721  -62.011  1.00 43.44  ? 439 GLU C O   1 
ATOM   11987 C CB  . GLU C  1 439 ? 1.985    76.649  -59.822  1.00 44.12  ? 439 GLU C CB  1 
ATOM   11988 C CG  . GLU C  1 439 ? 1.926    77.892  -58.940  1.00 48.15  ? 439 GLU C CG  1 
ATOM   11989 C CD  . GLU C  1 439 ? 2.350    77.727  -57.498  1.00 52.34  ? 439 GLU C CD  1 
ATOM   11990 O OE1 . GLU C  1 439 ? 2.658    76.574  -57.129  1.00 54.53  ? 439 GLU C OE1 1 
ATOM   11991 O OE2 . GLU C  1 439 ? 2.390    78.744  -56.764  1.00 52.61  ? 439 GLU C OE2 1 
ATOM   11992 N N   . THR C  1 440 ? 2.372    76.315  -63.337  1.00 41.83  ? 440 THR C N   1 
ATOM   11993 C CA  . THR C  1 440 ? 2.738    75.399  -64.411  1.00 42.00  ? 440 THR C CA  1 
ATOM   11994 C C   . THR C  1 440 ? 4.010    74.650  -64.020  1.00 41.79  ? 440 THR C C   1 
ATOM   11995 O O   . THR C  1 440 ? 4.700    75.052  -63.100  1.00 39.90  ? 440 THR C O   1 
ATOM   11996 C CB  . THR C  1 440 ? 2.907    76.057  -65.782  1.00 42.22  ? 440 THR C CB  1 
ATOM   11997 O OG1 . THR C  1 440 ? 3.803    77.144  -65.616  1.00 44.68  ? 440 THR C OG1 1 
ATOM   11998 C CG2 . THR C  1 440 ? 1.600    76.558  -66.364  1.00 42.59  ? 440 THR C CG2 1 
ATOM   11999 N N   . SER C  1 441 ? 4.217    73.508  -64.695  1.00 43.07  ? 441 SER C N   1 
ATOM   12000 C CA  . SER C  1 441 ? 5.405    72.682  -64.585  1.00 44.34  ? 441 SER C CA  1 
ATOM   12001 C C   . SER C  1 441 ? 5.874    72.293  -65.982  1.00 45.60  ? 441 SER C C   1 
ATOM   12002 O O   . SER C  1 441 ? 5.096    71.817  -66.800  1.00 43.78  ? 441 SER C O   1 
ATOM   12003 C CB  . SER C  1 441 ? 5.139    71.465  -63.740  1.00 44.02  ? 441 SER C CB  1 
ATOM   12004 O OG  . SER C  1 441 ? 6.349    70.980  -63.185  1.00 44.94  ? 441 SER C OG  1 
ATOM   12005 N N   . GLU C  1 442 ? 7.161    72.506  -66.233  1.00 51.64  ? 442 GLU C N   1 
ATOM   12006 C CA  . GLU C  1 442 ? 7.748    72.412  -67.559  1.00 57.64  ? 442 GLU C CA  1 
ATOM   12007 C C   . GLU C  1 442 ? 7.397    71.074  -68.213  1.00 55.51  ? 442 GLU C C   1 
ATOM   12008 O O   . GLU C  1 442 ? 7.091    71.041  -69.405  1.00 59.64  ? 442 GLU C O   1 
ATOM   12009 C CB  . GLU C  1 442 ? 9.260    72.650  -67.446  1.00 65.78  ? 442 GLU C CB  1 
ATOM   12010 C CG  . GLU C  1 442 ? 9.945    73.058  -68.749  1.00 74.10  ? 442 GLU C CG  1 
ATOM   12011 C CD  . GLU C  1 442 ? 11.358   73.617  -68.561  1.00 84.38  ? 442 GLU C CD  1 
ATOM   12012 O OE1 . GLU C  1 442 ? 11.550   74.757  -68.058  1.00 83.54  ? 442 GLU C OE1 1 
ATOM   12013 O OE2 . GLU C  1 442 ? 12.297   72.880  -68.929  1.00 88.95  ? 442 GLU C OE2 1 
ATOM   12014 N N   . ASN C  1 443 ? 7.431    69.961  -67.470  1.00 50.38  ? 443 ASN C N   1 
ATOM   12015 C CA  . ASN C  1 443 ? 7.284    68.685  -68.151  1.00 48.92  ? 443 ASN C CA  1 
ATOM   12016 C C   . ASN C  1 443 ? 5.820    68.334  -68.444  1.00 48.10  ? 443 ASN C C   1 
ATOM   12017 O O   . ASN C  1 443 ? 5.571    67.369  -69.144  1.00 50.71  ? 443 ASN C O   1 
ATOM   12018 C CB  . ASN C  1 443 ? 7.948    67.568  -67.362  1.00 50.76  ? 443 ASN C CB  1 
ATOM   12019 C CG  . ASN C  1 443 ? 9.382    67.861  -66.978  1.00 50.81  ? 443 ASN C CG  1 
ATOM   12020 O OD1 . ASN C  1 443 ? 10.158   68.369  -67.800  1.00 50.15  ? 443 ASN C OD1 1 
ATOM   12021 N ND2 . ASN C  1 443 ? 9.748    67.536  -65.742  1.00 49.15  ? 443 ASN C ND2 1 
ATOM   12022 N N   . PHE C  1 444 ? 4.843    69.090  -67.919  1.00 45.78  ? 444 PHE C N   1 
ATOM   12023 C CA  . PHE C  1 444 ? 3.449    68.687  -67.925  1.00 42.75  ? 444 PHE C CA  1 
ATOM   12024 C C   . PHE C  1 444 ? 2.610    69.605  -68.822  1.00 43.22  ? 444 PHE C C   1 
ATOM   12025 O O   . PHE C  1 444 ? 2.713    70.820  -68.727  1.00 44.71  ? 444 PHE C O   1 
ATOM   12026 C CB  . PHE C  1 444 ? 2.992    68.701  -66.460  1.00 41.31  ? 444 PHE C CB  1 
ATOM   12027 C CG  . PHE C  1 444 ? 3.554    67.589  -65.586  1.00 39.02  ? 444 PHE C CG  1 
ATOM   12028 C CD1 . PHE C  1 444 ? 4.764    67.749  -64.917  1.00 39.52  ? 444 PHE C CD1 1 
ATOM   12029 C CD2 . PHE C  1 444 ? 2.856    66.401  -65.412  1.00 37.21  ? 444 PHE C CD2 1 
ATOM   12030 C CE1 . PHE C  1 444 ? 5.278    66.731  -64.119  1.00 39.88  ? 444 PHE C CE1 1 
ATOM   12031 C CE2 . PHE C  1 444 ? 3.385    65.378  -64.631  1.00 37.61  ? 444 PHE C CE2 1 
ATOM   12032 C CZ  . PHE C  1 444 ? 4.600    65.537  -63.989  1.00 37.76  ? 444 PHE C CZ  1 
ATOM   12033 N N   . THR C  1 445 ? 1.737    69.019  -69.651  1.00 41.23  ? 445 THR C N   1 
ATOM   12034 C CA  . THR C  1 445 ? 0.955    69.790  -70.597  1.00 41.79  ? 445 THR C CA  1 
ATOM   12035 C C   . THR C  1 445 ? -0.478   69.978  -70.075  1.00 43.83  ? 445 THR C C   1 
ATOM   12036 O O   . THR C  1 445 ? -1.170   69.004  -69.729  1.00 40.87  ? 445 THR C O   1 
ATOM   12037 C CB  . THR C  1 445 ? 0.983    69.108  -71.968  1.00 40.47  ? 445 THR C CB  1 
ATOM   12038 O OG1 . THR C  1 445 ? 2.353    69.072  -72.331  1.00 41.46  ? 445 THR C OG1 1 
ATOM   12039 C CG2 . THR C  1 445 ? 0.278    69.901  -73.058  1.00 39.19  ? 445 THR C CG2 1 
ATOM   12040 N N   . LEU C  1 446 ? -0.943   71.240  -70.089  1.00 42.15  ? 446 LEU C N   1 
ATOM   12041 C CA  . LEU C  1 446 ? -2.313   71.550  -69.726  1.00 42.04  ? 446 LEU C CA  1 
ATOM   12042 C C   . LEU C  1 446 ? -3.202   71.291  -70.924  1.00 42.75  ? 446 LEU C C   1 
ATOM   12043 O O   . LEU C  1 446 ? -2.825   71.594  -72.038  1.00 47.17  ? 446 LEU C O   1 
ATOM   12044 C CB  . LEU C  1 446 ? -2.408   73.002  -69.254  1.00 42.96  ? 446 LEU C CB  1 
ATOM   12045 C CG  . LEU C  1 446 ? -1.523   73.345  -68.047  1.00 43.92  ? 446 LEU C CG  1 
ATOM   12046 C CD1 . LEU C  1 446 ? -1.542   74.822  -67.709  1.00 44.78  ? 446 LEU C CD1 1 
ATOM   12047 C CD2 . LEU C  1 446 ? -1.904   72.540  -66.821  1.00 42.44  ? 446 LEU C CD2 1 
ATOM   12048 N N   . LEU C  1 447 ? -4.399   70.779  -70.685  1.00 44.01  ? 447 LEU C N   1 
ATOM   12049 C CA  . LEU C  1 447 ? -5.242   70.350  -71.775  1.00 52.68  ? 447 LEU C CA  1 
ATOM   12050 C C   . LEU C  1 447 ? -6.524   71.171  -71.795  1.00 61.98  ? 447 LEU C C   1 
ATOM   12051 O O   . LEU C  1 447 ? -7.244   71.195  -70.794  1.00 71.95  ? 447 LEU C O   1 
ATOM   12052 C CB  . LEU C  1 447 ? -5.620   68.875  -71.621  1.00 53.10  ? 447 LEU C CB  1 
ATOM   12053 C CG  . LEU C  1 447 ? -4.602   67.803  -72.018  1.00 53.68  ? 447 LEU C CG  1 
ATOM   12054 C CD1 . LEU C  1 447 ? -5.357   66.465  -72.002  1.00 53.31  ? 447 LEU C CD1 1 
ATOM   12055 C CD2 . LEU C  1 447 ? -3.926   68.007  -73.358  1.00 55.51  ? 447 LEU C CD2 1 
ATOM   12056 N N   . ASP C  1 448 ? -6.873   71.697  -72.979  1.00 64.82  ? 448 ASP C N   1 
ATOM   12057 C CA  . ASP C  1 448 ? -8.224   72.188  -73.255  1.00 63.92  ? 448 ASP C CA  1 
ATOM   12058 C C   . ASP C  1 448 ? -8.542   73.276  -72.229  1.00 53.13  ? 448 ASP C C   1 
ATOM   12059 O O   . ASP C  1 448 ? -7.721   74.154  -72.009  1.00 53.51  ? 448 ASP C O   1 
ATOM   12060 C CB  . ASP C  1 448 ? -9.277   71.072  -73.345  1.00 63.31  ? 448 ASP C CB  1 
ATOM   12061 C CG  . ASP C  1 448 ? -9.066   69.937  -74.354  1.00 67.20  ? 448 ASP C CG  1 
ATOM   12062 O OD1 . ASP C  1 448 ? -8.566   70.215  -75.469  1.00 69.49  ? 448 ASP C OD1 1 
ATOM   12063 O OD2 . ASP C  1 448 ? -9.439   68.764  -74.043  1.00 59.64  ? 448 ASP C OD2 1 
ATOM   12064 N N   . ASP C  1 449 ? -9.688   73.144  -71.555  1.00 52.33  ? 449 ASP C N   1 
ATOM   12065 C CA  . ASP C  1 449 ? -10.290  74.225  -70.789  1.00 56.21  ? 449 ASP C CA  1 
ATOM   12066 C C   . ASP C  1 449 ? -10.224  73.912  -69.288  1.00 47.42  ? 449 ASP C C   1 
ATOM   12067 O O   . ASP C  1 449 ? -10.577  72.812  -68.843  1.00 39.67  ? 449 ASP C O   1 
ATOM   12068 C CB  . ASP C  1 449 ? -11.739  74.519  -71.205  1.00 57.12  ? 449 ASP C CB  1 
ATOM   12069 C CG  . ASP C  1 449 ? -11.956  75.445  -72.397  1.00 60.21  ? 449 ASP C CG  1 
ATOM   12070 O OD1 . ASP C  1 449 ? -10.975  75.757  -73.091  1.00 61.69  ? 449 ASP C OD1 1 
ATOM   12071 O OD2 . ASP C  1 449 ? -13.112  75.860  -72.629  1.00 63.91  ? 449 ASP C OD2 1 
ATOM   12072 N N   . LEU C  1 450 ? -9.825   74.960  -68.545  1.00 43.63  ? 450 LEU C N   1 
ATOM   12073 C CA  . LEU C  1 450 ? -10.201  75.195  -67.155  1.00 42.24  ? 450 LEU C CA  1 
ATOM   12074 C C   . LEU C  1 450 ? -11.729  75.153  -66.973  1.00 40.77  ? 450 LEU C C   1 
ATOM   12075 O O   . LEU C  1 450 ? -12.469  75.770  -67.754  1.00 38.30  ? 450 LEU C O   1 
ATOM   12076 C CB  . LEU C  1 450 ? -9.618   76.569  -66.819  1.00 40.19  ? 450 LEU C CB  1 
ATOM   12077 C CG  . LEU C  1 450 ? -9.853   77.111  -65.411  1.00 39.86  ? 450 LEU C CG  1 
ATOM   12078 C CD1 . LEU C  1 450 ? -9.257   76.162  -64.376  1.00 42.33  ? 450 LEU C CD1 1 
ATOM   12079 C CD2 . LEU C  1 450 ? -9.242   78.500  -65.301  1.00 40.26  ? 450 LEU C CD2 1 
ATOM   12080 N N   . LYS C  1 451 ? -12.196  74.398  -65.961  1.00 38.47  ? 451 LYS C N   1 
ATOM   12081 C CA  . LYS C  1 451 ? -13.616  74.354  -65.619  1.00 40.56  ? 451 LYS C CA  1 
ATOM   12082 C C   . LYS C  1 451 ? -13.798  74.883  -64.199  1.00 38.84  ? 451 LYS C C   1 
ATOM   12083 O O   . LYS C  1 451 ? -12.947  74.650  -63.344  1.00 37.17  ? 451 LYS C O   1 
ATOM   12084 C CB  . LYS C  1 451 ? -14.222  72.968  -65.873  1.00 41.45  ? 451 LYS C CB  1 
ATOM   12085 C CG  . LYS C  1 451 ? -14.061  72.587  -67.334  1.00 44.78  ? 451 LYS C CG  1 
ATOM   12086 C CD  . LYS C  1 451 ? -14.979  71.464  -67.773  1.00 48.96  ? 451 LYS C CD  1 
ATOM   12087 C CE  . LYS C  1 451 ? -14.706  70.960  -69.168  1.00 53.60  ? 451 LYS C CE  1 
ATOM   12088 N NZ  . LYS C  1 451 ? -15.612  69.848  -69.512  1.00 53.76  ? 451 LYS C NZ  1 
ATOM   12089 N N   . ILE C  1 452 ? -14.843  75.710  -64.036  1.00 37.18  ? 452 ILE C N   1 
ATOM   12090 C CA  . ILE C  1 452 ? -15.217  76.327  -62.777  1.00 36.59  ? 452 ILE C CA  1 
ATOM   12091 C C   . ILE C  1 452 ? -16.622  75.856  -62.402  1.00 36.78  ? 452 ILE C C   1 
ATOM   12092 O O   . ILE C  1 452 ? -17.493  75.832  -63.262  1.00 38.17  ? 452 ILE C O   1 
ATOM   12093 C CB  . ILE C  1 452 ? -15.206  77.853  -62.917  1.00 35.83  ? 452 ILE C CB  1 
ATOM   12094 C CG1 . ILE C  1 452 ? -14.066  78.358  -63.787  1.00 35.34  ? 452 ILE C CG1 1 
ATOM   12095 C CG2 . ILE C  1 452 ? -15.215  78.505  -61.537  1.00 36.52  ? 452 ILE C CG2 1 
ATOM   12096 C CD1 . ILE C  1 452 ? -12.704  78.185  -63.164  1.00 35.46  ? 452 ILE C CD1 1 
ATOM   12097 N N   . SER C  1 453 ? -16.855  75.494  -61.135  1.00 36.02  ? 453 SER C N   1 
ATOM   12098 C CA  . SER C  1 453 ? -18.198  75.151  -60.676  1.00 36.39  ? 453 SER C CA  1 
ATOM   12099 C C   . SER C  1 453 ? -18.536  75.890  -59.380  1.00 36.41  ? 453 SER C C   1 
ATOM   12100 O O   . SER C  1 453 ? -17.732  75.919  -58.441  1.00 37.99  ? 453 SER C O   1 
ATOM   12101 C CB  . SER C  1 453 ? -18.366  73.644  -60.519  1.00 35.90  ? 453 SER C CB  1 
ATOM   12102 O OG  . SER C  1 453 ? -19.418  73.354  -59.620  1.00 34.96  ? 453 SER C OG  1 
ATOM   12103 N N   . TYR C  1 454 ? -19.731  76.493  -59.343  1.00 34.83  ? 454 TYR C N   1 
ATOM   12104 C CA  . TYR C  1 454 ? -20.244  77.102  -58.121  1.00 35.71  ? 454 TYR C CA  1 
ATOM   12105 C C   . TYR C  1 454 ? -21.572  76.431  -57.771  1.00 34.79  ? 454 TYR C C   1 
ATOM   12106 O O   . TYR C  1 454 ? -22.655  76.965  -58.003  1.00 36.04  ? 454 TYR C O   1 
ATOM   12107 C CB  . TYR C  1 454 ? -20.380  78.628  -58.218  1.00 35.48  ? 454 TYR C CB  1 
ATOM   12108 C CG  . TYR C  1 454 ? -20.536  79.366  -56.896  1.00 37.10  ? 454 TYR C CG  1 
ATOM   12109 C CD1 . TYR C  1 454 ? -19.431  79.664  -56.103  1.00 37.93  ? 454 TYR C CD1 1 
ATOM   12110 C CD2 . TYR C  1 454 ? -21.775  79.822  -56.448  1.00 37.95  ? 454 TYR C CD2 1 
ATOM   12111 C CE1 . TYR C  1 454 ? -19.552  80.356  -54.903  1.00 39.06  ? 454 TYR C CE1 1 
ATOM   12112 C CE2 . TYR C  1 454 ? -21.901  80.536  -55.260  1.00 39.07  ? 454 TYR C CE2 1 
ATOM   12113 C CZ  . TYR C  1 454 ? -20.789  80.806  -54.475  1.00 39.61  ? 454 TYR C CZ  1 
ATOM   12114 O OH  . TYR C  1 454 ? -20.876  81.524  -53.310  1.00 39.54  ? 454 TYR C OH  1 
ATOM   12115 N N   . ASN C  1 455 ? -21.469  75.273  -57.140  1.00 34.39  ? 455 ASN C N   1 
ATOM   12116 C CA  . ASN C  1 455 ? -22.628  74.408  -57.027  1.00 34.70  ? 455 ASN C CA  1 
ATOM   12117 C C   . ASN C  1 455 ? -23.363  74.739  -55.748  1.00 35.24  ? 455 ASN C C   1 
ATOM   12118 O O   . ASN C  1 455 ? -22.901  74.329  -54.679  1.00 35.38  ? 455 ASN C O   1 
ATOM   12119 C CB  . ASN C  1 455 ? -22.259  72.930  -57.057  1.00 32.81  ? 455 ASN C CB  1 
ATOM   12120 C CG  . ASN C  1 455 ? -23.505  72.092  -56.931  1.00 33.44  ? 455 ASN C CG  1 
ATOM   12121 O OD1 . ASN C  1 455 ? -24.557  72.579  -56.483  1.00 31.89  ? 455 ASN C OD1 1 
ATOM   12122 N ND2 . ASN C  1 455 ? -23.398  70.825  -57.317  1.00 34.41  ? 455 ASN C ND2 1 
ATOM   12123 N N   . THR C  1 456 ? -24.521  75.403  -55.915  1.00 36.27  ? 456 THR C N   1 
ATOM   12124 C CA  . THR C  1 456 ? -25.304  76.002  -54.834  1.00 37.53  ? 456 THR C CA  1 
ATOM   12125 C C   . THR C  1 456 ? -26.352  75.065  -54.191  1.00 37.17  ? 456 THR C C   1 
ATOM   12126 O O   . THR C  1 456 ? -27.043  75.458  -53.248  1.00 37.61  ? 456 THR C O   1 
ATOM   12127 C CB  . THR C  1 456 ? -25.933  77.274  -55.412  1.00 39.13  ? 456 THR C CB  1 
ATOM   12128 O OG1 . THR C  1 456 ? -26.636  77.009  -56.624  1.00 36.85  ? 456 THR C OG1 1 
ATOM   12129 C CG2 . THR C  1 456 ? -24.878  78.319  -55.733  1.00 39.79  ? 456 THR C CG2 1 
ATOM   12130 N N   . HIS C  1 457 ? -26.459  73.810  -54.638  1.00 36.84  ? 457 HIS C N   1 
ATOM   12131 C CA  . HIS C  1 457 ? -27.108  72.769  -53.842  1.00 37.58  ? 457 HIS C CA  1 
ATOM   12132 C C   . HIS C  1 457 ? -28.614  73.018  -53.738  1.00 38.14  ? 457 HIS C C   1 
ATOM   12133 O O   . HIS C  1 457 ? -29.205  72.645  -52.724  1.00 37.31  ? 457 HIS C O   1 
ATOM   12134 C CB  . HIS C  1 457 ? -26.495  72.663  -52.433  1.00 38.87  ? 457 HIS C CB  1 
ATOM   12135 C CG  . HIS C  1 457 ? -25.119  72.057  -52.408  1.00 40.24  ? 457 HIS C CG  1 
ATOM   12136 N ND1 . HIS C  1 457 ? -24.871  70.800  -51.897  1.00 40.31  ? 457 HIS C ND1 1 
ATOM   12137 C CD2 . HIS C  1 457 ? -23.924  72.531  -52.795  1.00 40.28  ? 457 HIS C CD2 1 
ATOM   12138 C CE1 . HIS C  1 457 ? -23.581  70.528  -51.993  1.00 39.27  ? 457 HIS C CE1 1 
ATOM   12139 N NE2 . HIS C  1 457 ? -22.982  71.561  -52.548  1.00 39.64  ? 457 HIS C NE2 1 
ATOM   12140 N N   . LEU C  1 458 ? -29.207  73.679  -54.759  1.00 37.46  ? 458 LEU C N   1 
ATOM   12141 C CA  . LEU C  1 458 ? -30.649  73.872  -54.832  1.00 37.79  ? 458 LEU C CA  1 
ATOM   12142 C C   . LEU C  1 458 ? -31.255  72.632  -55.483  1.00 37.21  ? 458 LEU C C   1 
ATOM   12143 O O   . LEU C  1 458 ? -31.240  72.477  -56.706  1.00 37.22  ? 458 LEU C O   1 
ATOM   12144 C CB  . LEU C  1 458 ? -31.044  75.121  -55.609  1.00 37.71  ? 458 LEU C CB  1 
ATOM   12145 C CG  . LEU C  1 458 ? -30.436  76.457  -55.129  1.00 40.90  ? 458 LEU C CG  1 
ATOM   12146 C CD1 . LEU C  1 458 ? -30.919  77.694  -55.959  1.00 40.37  ? 458 LEU C CD1 1 
ATOM   12147 C CD2 . LEU C  1 458 ? -30.665  76.736  -53.646  1.00 42.42  ? 458 LEU C CD2 1 
ATOM   12148 N N   . GLY C  1 459 ? -31.809  71.755  -54.652  1.00 36.98  ? 459 GLY C N   1 
ATOM   12149 C CA  . GLY C  1 459 ? -32.270  70.459  -55.115  1.00 37.63  ? 459 GLY C CA  1 
ATOM   12150 C C   . GLY C  1 459 ? -31.133  69.683  -55.776  1.00 36.58  ? 459 GLY C C   1 
ATOM   12151 O O   . GLY C  1 459 ? -30.040  69.597  -55.226  1.00 36.74  ? 459 GLY C O   1 
ATOM   12152 N N   . TRP C  1 460 ? -31.409  69.213  -56.990  1.00 35.94  ? 460 TRP C N   1 
ATOM   12153 C CA  . TRP C  1 460 ? -30.448  68.552  -57.850  1.00 36.69  ? 460 TRP C CA  1 
ATOM   12154 C C   . TRP C  1 460 ? -29.756  69.504  -58.845  1.00 37.71  ? 460 TRP C C   1 
ATOM   12155 O O   . TRP C  1 460 ? -28.808  69.082  -59.502  1.00 37.46  ? 460 TRP C O   1 
ATOM   12156 C CB  . TRP C  1 460 ? -31.202  67.457  -58.610  1.00 37.06  ? 460 TRP C CB  1 
ATOM   12157 C CG  . TRP C  1 460 ? -31.785  66.383  -57.724  1.00 38.27  ? 460 TRP C CG  1 
ATOM   12158 C CD1 . TRP C  1 460 ? -33.100  66.197  -57.426  1.00 37.31  ? 460 TRP C CD1 1 
ATOM   12159 C CD2 . TRP C  1 460 ? -31.051  65.342  -57.009  1.00 36.80  ? 460 TRP C CD2 1 
ATOM   12160 N NE1 . TRP C  1 460 ? -33.239  65.085  -56.624  1.00 39.49  ? 460 TRP C NE1 1 
ATOM   12161 C CE2 . TRP C  1 460 ? -32.009  64.559  -56.328  1.00 37.73  ? 460 TRP C CE2 1 
ATOM   12162 C CE3 . TRP C  1 460 ? -29.697  65.018  -56.873  1.00 34.52  ? 460 TRP C CE3 1 
ATOM   12163 C CZ2 . TRP C  1 460 ? -31.653  63.476  -55.527  1.00 39.23  ? 460 TRP C CZ2 1 
ATOM   12164 C CZ3 . TRP C  1 460 ? -29.339  63.966  -56.072  1.00 35.59  ? 460 TRP C CZ3 1 
ATOM   12165 C CH2 . TRP C  1 460 ? -30.304  63.195  -55.426  1.00 38.16  ? 460 TRP C CH2 1 
ATOM   12166 N N   . ALA C  1 461 ? -30.204  70.769  -58.975  1.00 37.55  ? 461 ALA C N   1 
ATOM   12167 C CA  . ALA C  1 461 ? -29.550  71.740  -59.843  1.00 37.91  ? 461 ALA C CA  1 
ATOM   12168 C C   . ALA C  1 461 ? -28.095  71.897  -59.411  1.00 39.24  ? 461 ALA C C   1 
ATOM   12169 O O   . ALA C  1 461 ? -27.835  72.078  -58.226  1.00 42.96  ? 461 ALA C O   1 
ATOM   12170 C CB  . ALA C  1 461 ? -30.282  73.083  -59.780  1.00 38.68  ? 461 ALA C CB  1 
ATOM   12171 N N   . ILE C  1 462 ? -27.150  71.846  -60.358  1.00 38.58  ? 462 ILE C N   1 
ATOM   12172 C CA  . ILE C  1 462 ? -25.725  71.902  -60.035  1.00 38.66  ? 462 ILE C CA  1 
ATOM   12173 C C   . ILE C  1 462 ? -25.210  73.347  -59.977  1.00 38.58  ? 462 ILE C C   1 
ATOM   12174 O O   . ILE C  1 462 ? -24.047  73.572  -59.651  1.00 37.18  ? 462 ILE C O   1 
ATOM   12175 C CB  . ILE C  1 462 ? -24.892  71.069  -61.034  1.00 40.39  ? 462 ILE C CB  1 
ATOM   12176 C CG1 . ILE C  1 462 ? -25.065  71.534  -62.463  1.00 41.55  ? 462 ILE C CG1 1 
ATOM   12177 C CG2 . ILE C  1 462 ? -25.209  69.578  -60.918  1.00 40.29  ? 462 ILE C CG2 1 
ATOM   12178 C CD1 . ILE C  1 462 ? -23.936  71.088  -63.363  1.00 42.18  ? 462 ILE C CD1 1 
ATOM   12179 N N   . GLY C  1 463 ? -26.042  74.330  -60.345  1.00 38.19  ? 463 GLY C N   1 
ATOM   12180 C CA  . GLY C  1 463 ? -25.625  75.723  -60.318  1.00 37.24  ? 463 GLY C CA  1 
ATOM   12181 C C   . GLY C  1 463 ? -24.770  76.095  -61.522  1.00 36.81  ? 463 GLY C C   1 
ATOM   12182 O O   . GLY C  1 463 ? -24.695  75.375  -62.504  1.00 36.36  ? 463 GLY C O   1 
ATOM   12183 N N   . SER C  1 464 ? -24.081  77.227  -61.410  1.00 40.57  ? 464 SER C N   1 
ATOM   12184 C CA  . SER C  1 464 ? -23.324  77.813  -62.509  1.00 40.42  ? 464 SER C CA  1 
ATOM   12185 C C   . SER C  1 464 ? -22.014  77.054  -62.759  1.00 39.87  ? 464 SER C C   1 
ATOM   12186 O O   . SER C  1 464 ? -21.396  76.543  -61.834  1.00 40.32  ? 464 SER C O   1 
ATOM   12187 C CB  . SER C  1 464 ? -23.069  79.275  -62.222  1.00 41.86  ? 464 SER C CB  1 
ATOM   12188 O OG  . SER C  1 464 ? -24.236  80.056  -62.441  1.00 42.43  ? 464 SER C OG  1 
ATOM   12189 N N   . GLN C  1 465 ? -21.618  76.959  -64.033  1.00 40.38  ? 465 GLN C N   1 
ATOM   12190 C CA  . GLN C  1 465 ? -20.324  76.442  -64.447  1.00 41.09  ? 465 GLN C CA  1 
ATOM   12191 C C   . GLN C  1 465 ? -19.721  77.436  -65.428  1.00 40.18  ? 465 GLN C C   1 
ATOM   12192 O O   . GLN C  1 465 ? -20.444  78.237  -65.995  1.00 46.50  ? 465 GLN C O   1 
ATOM   12193 C CB  . GLN C  1 465 ? -20.398  75.128  -65.218  1.00 41.52  ? 465 GLN C CB  1 
ATOM   12194 C CG  . GLN C  1 465 ? -20.943  73.978  -64.399  1.00 46.09  ? 465 GLN C CG  1 
ATOM   12195 C CD  . GLN C  1 465 ? -20.787  72.642  -65.092  1.00 47.60  ? 465 GLN C CD  1 
ATOM   12196 O OE1 . GLN C  1 465 ? -19.693  72.077  -65.179  1.00 46.67  ? 465 GLN C OE1 1 
ATOM   12197 N NE2 . GLN C  1 465 ? -21.903  72.090  -65.547  1.00 51.03  ? 465 GLN C NE2 1 
ATOM   12198 N N   . ALA C  1 466 ? -18.411  77.393  -65.647  1.00 37.97  ? 466 ALA C N   1 
ATOM   12199 C CA  . ALA C  1 466 ? -17.837  78.148  -66.748  1.00 38.06  ? 466 ALA C CA  1 
ATOM   12200 C C   . ALA C  1 466 ? -16.681  77.347  -67.347  1.00 36.56  ? 466 ALA C C   1 
ATOM   12201 O O   . ALA C  1 466 ? -16.055  76.555  -66.656  1.00 39.82  ? 466 ALA C O   1 
ATOM   12202 C CB  . ALA C  1 466 ? -17.452  79.546  -66.270  1.00 36.80  ? 466 ALA C CB  1 
ATOM   12203 N N   . SER C  1 467 ? -16.422  77.524  -68.641  1.00 36.59  ? 467 SER C N   1 
ATOM   12204 C CA  . SER C  1 467 ? -15.220  77.010  -69.267  1.00 36.93  ? 467 SER C CA  1 
ATOM   12205 C C   . SER C  1 467 ? -14.387  78.190  -69.696  1.00 38.35  ? 467 SER C C   1 
ATOM   12206 O O   . SER C  1 467 ? -14.875  79.015  -70.448  1.00 39.86  ? 467 SER C O   1 
ATOM   12207 C CB  . SER C  1 467 ? -15.490  76.159  -70.468  1.00 37.23  ? 467 SER C CB  1 
ATOM   12208 O OG  . SER C  1 467 ? -16.052  74.924  -70.067  1.00 43.39  ? 467 SER C OG  1 
ATOM   12209 N N   . VAL C  1 468 ? -13.126  78.199  -69.270  1.00 40.43  ? 468 VAL C N   1 
ATOM   12210 C CA  . VAL C  1 468 ? -12.228  79.310  -69.497  1.00 41.41  ? 468 VAL C CA  1 
ATOM   12211 C C   . VAL C  1 468 ? -11.071  78.806  -70.346  1.00 39.86  ? 468 VAL C C   1 
ATOM   12212 O O   . VAL C  1 468 ? -10.349  77.928  -69.908  1.00 39.96  ? 468 VAL C O   1 
ATOM   12213 C CB  . VAL C  1 468 ? -11.723  79.923  -68.170  1.00 43.44  ? 468 VAL C CB  1 
ATOM   12214 C CG1 . VAL C  1 468 ? -10.901  81.192  -68.403  1.00 44.27  ? 468 VAL C CG1 1 
ATOM   12215 C CG2 . VAL C  1 468 ? -12.841  80.214  -67.184  1.00 43.28  ? 468 VAL C CG2 1 
ATOM   12216 N N   . SER C  1 469 ? -10.896  79.401  -71.533  1.00 42.44  ? 469 SER C N   1 
ATOM   12217 C CA  . SER C  1 469 ? -9.722   79.189  -72.362  1.00 42.48  ? 469 SER C CA  1 
ATOM   12218 C C   . SER C  1 469 ? -8.526   79.865  -71.711  1.00 44.69  ? 469 SER C C   1 
ATOM   12219 O O   . SER C  1 469 ? -8.614   81.033  -71.319  1.00 42.88  ? 469 SER C O   1 
ATOM   12220 C CB  . SER C  1 469 ? -9.894   79.711  -73.747  1.00 43.19  ? 469 SER C CB  1 
ATOM   12221 O OG  . SER C  1 469 ? -8.759   79.382  -74.538  1.00 43.86  ? 469 SER C OG  1 
ATOM   12222 N N   . ILE C  1 470 ? -7.438   79.083  -71.603  1.00 47.54  ? 470 ILE C N   1 
ATOM   12223 C CA  . ILE C  1 470 ? -6.156   79.528  -71.067  1.00 52.23  ? 470 ILE C CA  1 
ATOM   12224 C C   . ILE C  1 470 ? -5.062   79.417  -72.141  1.00 54.37  ? 470 ILE C C   1 
ATOM   12225 O O   . ILE C  1 470 ? -3.884   79.571  -71.842  1.00 53.72  ? 470 ILE C O   1 
ATOM   12226 C CB  . ILE C  1 470 ? -5.819   78.726  -69.788  1.00 51.95  ? 470 ILE C CB  1 
ATOM   12227 C CG1 . ILE C  1 470 ? -5.739   77.213  -70.027  1.00 50.33  ? 470 ILE C CG1 1 
ATOM   12228 C CG2 . ILE C  1 470 ? -6.786   79.046  -68.652  1.00 51.20  ? 470 ILE C CG2 1 
ATOM   12229 C CD1 . ILE C  1 470 ? -4.324   76.703  -70.204  1.00 50.20  ? 470 ILE C CD1 1 
ATOM   12230 N N   . SER C  1 471 ? -5.463   79.171  -73.397  1.00 58.98  ? 471 SER C N   1 
ATOM   12231 C CA  . SER C  1 471 ? -4.571   79.042  -74.541  1.00 63.04  ? 471 SER C CA  1 
ATOM   12232 C C   . SER C  1 471 ? -3.718   80.307  -74.748  1.00 67.14  ? 471 SER C C   1 
ATOM   12233 O O   . SER C  1 471 ? -2.576   80.211  -75.176  1.00 76.10  ? 471 SER C O   1 
ATOM   12234 C CB  . SER C  1 471 ? -5.387   78.721  -75.777  1.00 62.70  ? 471 SER C CB  1 
ATOM   12235 O OG  . SER C  1 471 ? -6.106   79.883  -76.178  1.00 66.31  ? 471 SER C OG  1 
ATOM   12236 N N   . ASP C  1 472 ? -4.253   81.492  -74.422  1.00 63.80  ? 472 ASP C N   1 
ATOM   12237 C CA  . ASP C  1 472 ? -3.508   82.743  -74.484  1.00 65.88  ? 472 ASP C CA  1 
ATOM   12238 C C   . ASP C  1 472 ? -2.468   82.890  -73.365  1.00 64.66  ? 472 ASP C C   1 
ATOM   12239 O O   . ASP C  1 472 ? -1.832   83.935  -73.280  1.00 61.47  ? 472 ASP C O   1 
ATOM   12240 C CB  . ASP C  1 472 ? -4.434   83.958  -74.452  1.00 68.26  ? 472 ASP C CB  1 
ATOM   12241 C CG  . ASP C  1 472 ? -5.311   84.170  -73.216  1.00 68.69  ? 472 ASP C CG  1 
ATOM   12242 O OD1 . ASP C  1 472 ? -5.606   83.201  -72.478  1.00 68.43  ? 472 ASP C OD1 1 
ATOM   12243 O OD2 . ASP C  1 472 ? -5.712   85.317  -72.987  1.00 67.06  ? 472 ASP C OD2 1 
ATOM   12244 N N   . GLN C  1 473 ? -2.292   81.885  -72.494  1.00 62.85  ? 473 GLN C N   1 
ATOM   12245 C CA  . GLN C  1 473 ? -1.449   82.043  -71.318  1.00 60.82  ? 473 GLN C CA  1 
ATOM   12246 C C   . GLN C  1 473 ? -0.481   80.872  -71.110  1.00 64.50  ? 473 GLN C C   1 
ATOM   12247 O O   . GLN C  1 473 ? 0.225    80.853  -70.100  1.00 68.57  ? 473 GLN C O   1 
ATOM   12248 C CB  . GLN C  1 473 ? -2.334   82.151  -70.075  1.00 57.03  ? 473 GLN C CB  1 
ATOM   12249 C CG  . GLN C  1 473 ? -3.203   83.404  -69.984  1.00 57.13  ? 473 GLN C CG  1 
ATOM   12250 C CD  . GLN C  1 473 ? -3.799   83.623  -68.602  1.00 54.42  ? 473 GLN C CD  1 
ATOM   12251 O OE1 . GLN C  1 473 ? -3.104   83.936  -67.627  1.00 56.78  ? 473 GLN C OE1 1 
ATOM   12252 N NE2 . GLN C  1 473 ? -5.103   83.450  -68.488  1.00 49.28  ? 473 GLN C NE2 1 
ATOM   12253 N N   . LEU C  1 474 ? -0.418   79.908  -72.043  1.00 67.48  ? 474 LEU C N   1 
ATOM   12254 C CA  . LEU C  1 474 ? 0.172    78.595  -71.763  1.00 70.25  ? 474 LEU C CA  1 
ATOM   12255 C C   . LEU C  1 474 ? 1.661    78.703  -71.394  1.00 71.33  ? 474 LEU C C   1 
ATOM   12256 O O   . LEU C  1 474 ? 2.118    77.989  -70.496  1.00 68.96  ? 474 LEU C O   1 
ATOM   12257 C CB  . LEU C  1 474 ? -0.077   77.600  -72.905  1.00 69.82  ? 474 LEU C CB  1 
ATOM   12258 C CG  . LEU C  1 474 ? -1.389   76.795  -72.859  1.00 70.71  ? 474 LEU C CG  1 
ATOM   12259 C CD1 . LEU C  1 474 ? -1.594   75.868  -74.071  1.00 68.45  ? 474 LEU C CD1 1 
ATOM   12260 C CD2 . LEU C  1 474 ? -1.489   75.959  -71.590  1.00 68.04  ? 474 LEU C CD2 1 
ATOM   12261 N N   . ASP C  1 475 ? 2.394    79.626  -72.048  1.00 73.28  ? 475 ASP C N   1 
ATOM   12262 C CA  . ASP C  1 475 ? 3.824    79.849  -71.823  1.00 77.01  ? 475 ASP C CA  1 
ATOM   12263 C C   . ASP C  1 475 ? 4.143    80.355  -70.402  1.00 75.28  ? 475 ASP C C   1 
ATOM   12264 O O   . ASP C  1 475 ? 5.276    80.199  -69.949  1.00 71.74  ? 475 ASP C O   1 
ATOM   12265 C CB  . ASP C  1 475 ? 4.407    80.813  -72.859  1.00 79.54  ? 475 ASP C CB  1 
ATOM   12266 C CG  . ASP C  1 475 ? 3.688    82.156  -72.992  1.00 83.40  ? 475 ASP C CG  1 
ATOM   12267 O OD1 . ASP C  1 475 ? 2.436    82.129  -73.128  1.00 81.93  ? 475 ASP C OD1 1 
ATOM   12268 O OD2 . ASP C  1 475 ? 4.364    83.227  -72.949  1.00 82.19  ? 475 ASP C OD2 1 
ATOM   12269 N N   . LYS C  1 476 ? 3.179    80.991  -69.704  1.00 69.23  ? 476 LYS C N   1 
ATOM   12270 C CA  . LYS C  1 476 ? 3.456    81.684  -68.449  1.00 65.51  ? 476 LYS C CA  1 
ATOM   12271 C C   . LYS C  1 476 ? 3.661    80.678  -67.322  1.00 61.68  ? 476 LYS C C   1 
ATOM   12272 O O   . LYS C  1 476 ? 3.268    79.520  -67.456  1.00 66.99  ? 476 LYS C O   1 
ATOM   12273 C CB  . LYS C  1 476 ? 2.335    82.658  -68.065  1.00 66.12  ? 476 LYS C CB  1 
ATOM   12274 C CG  . LYS C  1 476 ? 1.955    83.662  -69.140  1.00 69.02  ? 476 LYS C CG  1 
ATOM   12275 C CD  . LYS C  1 476 ? 1.226    84.884  -68.603  1.00 73.67  ? 476 LYS C CD  1 
ATOM   12276 C CE  . LYS C  1 476 ? -0.143   84.541  -68.114  1.00 72.45  ? 476 LYS C CE  1 
ATOM   12277 N NZ  . LYS C  1 476 ? -0.605   85.513  -67.119  1.00 74.42  ? 476 LYS C NZ  1 
ATOM   12278 N N   . LYS C  1 477 ? 4.265    81.145  -66.220  1.00 59.33  ? 477 LYS C N   1 
ATOM   12279 C CA  . LYS C  1 477 ? 4.631    80.315  -65.079  1.00 60.42  ? 477 LYS C CA  1 
ATOM   12280 C C   . LYS C  1 477 ? 3.422    80.160  -64.156  1.00 56.84  ? 477 LYS C C   1 
ATOM   12281 O O   . LYS C  1 477 ? 3.219    79.106  -63.530  1.00 56.10  ? 477 LYS C O   1 
ATOM   12282 C CB  . LYS C  1 477 ? 5.886    80.819  -64.342  1.00 66.87  ? 477 LYS C CB  1 
ATOM   12283 C CG  . LYS C  1 477 ? 7.276    80.474  -64.964  1.00 75.92  ? 477 LYS C CG  1 
ATOM   12284 C CD  . LYS C  1 477 ? 7.694    78.989  -64.986  1.00 82.39  ? 477 LYS C CD  1 
ATOM   12285 C CE  . LYS C  1 477 ? 7.208    78.151  -66.177  1.00 81.92  ? 477 LYS C CE  1 
ATOM   12286 N NZ  . LYS C  1 477 ? 6.903    76.733  -65.903  1.00 78.31  ? 477 LYS C NZ  1 
ATOM   12287 N N   . ILE C  1 478 ? 2.611    81.212  -64.107  1.00 52.45  ? 478 ILE C N   1 
ATOM   12288 C CA  . ILE C  1 478 ? 1.414    81.252  -63.289  1.00 51.91  ? 478 ILE C CA  1 
ATOM   12289 C C   . ILE C  1 478 ? 0.268    81.705  -64.184  1.00 50.14  ? 478 ILE C C   1 
ATOM   12290 O O   . ILE C  1 478 ? 0.356    82.755  -64.793  1.00 51.63  ? 478 ILE C O   1 
ATOM   12291 C CB  . ILE C  1 478 ? 1.621    82.201  -62.088  1.00 54.54  ? 478 ILE C CB  1 
ATOM   12292 C CG1 . ILE C  1 478 ? 2.621    81.615  -61.078  1.00 55.24  ? 478 ILE C CG1 1 
ATOM   12293 C CG2 . ILE C  1 478 ? 0.290    82.548  -61.418  1.00 53.47  ? 478 ILE C CG2 1 
ATOM   12294 C CD1 . ILE C  1 478 ? 3.064    82.590  -60.005  1.00 56.95  ? 478 ILE C CD1 1 
ATOM   12295 N N   . ILE C  1 479 ? -0.792   80.907  -64.264  1.00 49.52  ? 479 ILE C N   1 
ATOM   12296 C CA  . ILE C  1 479 ? -1.993   81.249  -65.018  1.00 49.38  ? 479 ILE C CA  1 
ATOM   12297 C C   . ILE C  1 479 ? -3.095   81.610  -64.021  1.00 48.91  ? 479 ILE C C   1 
ATOM   12298 O O   . ILE C  1 479 ? -3.289   80.890  -63.033  1.00 48.80  ? 479 ILE C O   1 
ATOM   12299 C CB  . ILE C  1 479 ? -2.420   80.049  -65.884  1.00 47.81  ? 479 ILE C CB  1 
ATOM   12300 C CG1 . ILE C  1 479 ? -1.336   79.658  -66.906  1.00 48.97  ? 479 ILE C CG1 1 
ATOM   12301 C CG2 . ILE C  1 479 ? -3.765   80.316  -66.553  1.00 47.37  ? 479 ILE C CG2 1 
ATOM   12302 C CD1 . ILE C  1 479 ? -1.536   78.298  -67.560  1.00 46.00  ? 479 ILE C CD1 1 
ATOM   12303 N N   . THR C  1 480 ? -3.816   82.712  -64.252  1.00 45.96  ? 480 THR C N   1 
ATOM   12304 C CA  . THR C  1 480 ? -4.873   83.062  -63.316  1.00 45.11  ? 480 THR C CA  1 
ATOM   12305 C C   . THR C  1 480 ? -6.197   83.173  -64.059  1.00 43.69  ? 480 THR C C   1 
ATOM   12306 O O   . THR C  1 480 ? -6.227   83.165  -65.275  1.00 43.89  ? 480 THR C O   1 
ATOM   12307 C CB  . THR C  1 480 ? -4.512   84.340  -62.563  1.00 46.38  ? 480 THR C CB  1 
ATOM   12308 O OG1 . THR C  1 480 ? -4.530   85.355  -63.555  1.00 46.43  ? 480 THR C OG1 1 
ATOM   12309 C CG2 . THR C  1 480 ? -3.139   84.262  -61.925  1.00 46.94  ? 480 THR C CG2 1 
ATOM   12310 N N   . SER C  1 481 ? -7.286   83.225  -63.298  1.00 44.21  ? 481 SER C N   1 
ATOM   12311 C CA  . SER C  1 481 ? -8.629   83.393  -63.831  1.00 43.77  ? 481 SER C CA  1 
ATOM   12312 C C   . SER C  1 481 ? -9.555   83.915  -62.732  1.00 44.44  ? 481 SER C C   1 
ATOM   12313 O O   . SER C  1 481 ? -9.404   83.562  -61.567  1.00 47.09  ? 481 SER C O   1 
ATOM   12314 C CB  . SER C  1 481 ? -9.162   82.103  -64.373  1.00 42.27  ? 481 SER C CB  1 
ATOM   12315 O OG  . SER C  1 481 ? -10.381  82.389  -65.035  1.00 42.61  ? 481 SER C OG  1 
ATOM   12316 N N   . GLU C  1 482 ? -10.546  84.721  -63.099  1.00 43.64  ? 482 GLU C N   1 
ATOM   12317 C CA  . GLU C  1 482 ? -11.480  85.268  -62.124  1.00 42.52  ? 482 GLU C CA  1 
ATOM   12318 C C   . GLU C  1 482 ? -12.897  85.175  -62.687  1.00 41.94  ? 482 GLU C C   1 
ATOM   12319 O O   . GLU C  1 482 ? -13.203  85.806  -63.691  1.00 40.90  ? 482 GLU C O   1 
ATOM   12320 C CB  . GLU C  1 482 ? -11.112  86.708  -61.773  1.00 41.24  ? 482 GLU C CB  1 
ATOM   12321 C CG  . GLU C  1 482 ? -11.917  87.283  -60.612  1.00 41.29  ? 482 GLU C CG  1 
ATOM   12322 C CD  . GLU C  1 482 ? -11.486  88.692  -60.212  1.00 42.40  ? 482 GLU C CD  1 
ATOM   12323 O OE1 . GLU C  1 482 ? -11.339  89.457  -61.179  1.00 43.53  ? 482 GLU C OE1 1 
ATOM   12324 O OE2 . GLU C  1 482 ? -11.319  89.064  -59.030  1.00 42.00  ? 482 GLU C OE2 1 
ATOM   12325 N N   . ASN C  1 483 ? -13.757  84.411  -62.009  1.00 41.76  ? 483 ASN C N   1 
ATOM   12326 C CA  . ASN C  1 483 ? -15.105  84.176  -62.486  1.00 42.20  ? 483 ASN C CA  1 
ATOM   12327 C C   . ASN C  1 483 ? -16.121  84.532  -61.410  1.00 41.06  ? 483 ASN C C   1 
ATOM   12328 O O   . ASN C  1 483 ? -15.929  84.181  -60.248  1.00 40.84  ? 483 ASN C O   1 
ATOM   12329 C CB  . ASN C  1 483 ? -15.259  82.721  -62.883  1.00 43.73  ? 483 ASN C CB  1 
ATOM   12330 C CG  . ASN C  1 483 ? -14.331  82.408  -64.021  1.00 46.49  ? 483 ASN C CG  1 
ATOM   12331 O OD1 . ASN C  1 483 ? -14.780  82.402  -65.166  1.00 51.45  ? 483 ASN C OD1 1 
ATOM   12332 N ND2 . ASN C  1 483 ? -13.050  82.212  -63.743  1.00 47.64  ? 483 ASN C ND2 1 
ATOM   12333 N N   . PHE C  1 484 ? -17.218  85.185  -61.818  1.00 40.49  ? 484 PHE C N   1 
ATOM   12334 C CA  . PHE C  1 484 ? -18.214  85.674  -60.868  1.00 40.01  ? 484 PHE C CA  1 
ATOM   12335 C C   . PHE C  1 484 ? -19.484  84.816  -60.916  1.00 38.72  ? 484 PHE C C   1 
ATOM   12336 O O   . PHE C  1 484 ? -19.815  84.233  -61.941  1.00 39.23  ? 484 PHE C O   1 
ATOM   12337 C CB  . PHE C  1 484 ? -18.447  87.159  -61.139  1.00 39.29  ? 484 PHE C CB  1 
ATOM   12338 C CG  . PHE C  1 484 ? -17.217  88.024  -60.933  1.00 40.11  ? 484 PHE C CG  1 
ATOM   12339 C CD1 . PHE C  1 484 ? -16.896  88.529  -59.672  1.00 41.63  ? 484 PHE C CD1 1 
ATOM   12340 C CD2 . PHE C  1 484 ? -16.405  88.384  -62.006  1.00 40.11  ? 484 PHE C CD2 1 
ATOM   12341 C CE1 . PHE C  1 484 ? -15.772  89.331  -59.480  1.00 42.40  ? 484 PHE C CE1 1 
ATOM   12342 C CE2 . PHE C  1 484 ? -15.295  89.212  -61.824  1.00 40.96  ? 484 PHE C CE2 1 
ATOM   12343 C CZ  . PHE C  1 484 ? -14.976  89.677  -60.563  1.00 42.25  ? 484 PHE C CZ  1 
ATOM   12344 N N   . PHE C  1 485 ? -20.175  84.709  -59.772  1.00 38.14  ? 485 PHE C N   1 
ATOM   12345 C CA  . PHE C  1 485 ? -21.424  83.966  -59.690  1.00 36.56  ? 485 PHE C CA  1 
ATOM   12346 C C   . PHE C  1 485 ? -22.379  84.643  -58.714  1.00 36.63  ? 485 PHE C C   1 
ATOM   12347 O O   . PHE C  1 485 ? -21.990  85.112  -57.641  1.00 37.51  ? 485 PHE C O   1 
ATOM   12348 C CB  . PHE C  1 485 ? -21.162  82.544  -59.203  1.00 36.00  ? 485 PHE C CB  1 
ATOM   12349 C CG  . PHE C  1 485 ? -20.102  81.819  -60.017  1.00 36.27  ? 485 PHE C CG  1 
ATOM   12350 C CD1 . PHE C  1 485 ? -20.436  81.210  -61.229  1.00 36.22  ? 485 PHE C CD1 1 
ATOM   12351 C CD2 . PHE C  1 485 ? -18.780  81.747  -59.572  1.00 35.99  ? 485 PHE C CD2 1 
ATOM   12352 C CE1 . PHE C  1 485 ? -19.488  80.511  -61.959  1.00 35.23  ? 485 PHE C CE1 1 
ATOM   12353 C CE2 . PHE C  1 485 ? -17.828  81.094  -60.321  1.00 34.96  ? 485 PHE C CE2 1 
ATOM   12354 C CZ  . PHE C  1 485 ? -18.183  80.481  -61.511  1.00 35.81  ? 485 PHE C CZ  1 
ATOM   12355 N N   . ASN C  1 486 ? -23.653  84.666  -59.080  1.00 36.08  ? 486 ASN C N   1 
ATOM   12356 C CA  . ASN C  1 486 ? -24.663  85.129  -58.147  1.00 37.50  ? 486 ASN C CA  1 
ATOM   12357 C C   . ASN C  1 486 ? -24.859  84.058  -57.070  1.00 37.90  ? 486 ASN C C   1 
ATOM   12358 O O   . ASN C  1 486 ? -24.739  82.851  -57.323  1.00 36.18  ? 486 ASN C O   1 
ATOM   12359 C CB  . ASN C  1 486 ? -25.951  85.553  -58.859  1.00 37.26  ? 486 ASN C CB  1 
ATOM   12360 C CG  . ASN C  1 486 ? -25.747  86.830  -59.637  1.00 37.13  ? 486 ASN C CG  1 
ATOM   12361 O OD1 . ASN C  1 486 ? -25.903  86.852  -60.862  1.00 36.48  ? 486 ASN C OD1 1 
ATOM   12362 N ND2 . ASN C  1 486 ? -25.375  87.889  -58.943  1.00 37.90  ? 486 ASN C ND2 1 
ATOM   12363 N N   . ILE C  1 487 ? -25.142  84.544  -55.854  1.00 39.95  ? 487 ILE C N   1 
ATOM   12364 C CA  . ILE C  1 487 ? -25.471  83.684  -54.734  1.00 41.03  ? 487 ILE C CA  1 
ATOM   12365 C C   . ILE C  1 487 ? -26.989  83.696  -54.530  1.00 41.72  ? 487 ILE C C   1 
ATOM   12366 O O   . ILE C  1 487 ? -27.549  84.702  -54.132  1.00 42.48  ? 487 ILE C O   1 
ATOM   12367 C CB  . ILE C  1 487 ? -24.699  84.085  -53.463  1.00 41.73  ? 487 ILE C CB  1 
ATOM   12368 C CG1 . ILE C  1 487 ? -23.191  84.241  -53.722  1.00 41.10  ? 487 ILE C CG1 1 
ATOM   12369 C CG2 . ILE C  1 487 ? -24.957  83.030  -52.392  1.00 42.91  ? 487 ILE C CG2 1 
ATOM   12370 C CD1 . ILE C  1 487 ? -22.384  84.686  -52.516  1.00 41.83  ? 487 ILE C CD1 1 
ATOM   12371 N N   . PRO C  1 488 ? -27.714  82.572  -54.758  1.00 42.00  ? 488 PRO C N   1 
ATOM   12372 C CA  . PRO C  1 488 ? -29.136  82.528  -54.419  1.00 42.42  ? 488 PRO C CA  1 
ATOM   12373 C C   . PRO C  1 488 ? -29.316  82.798  -52.919  1.00 44.30  ? 488 PRO C C   1 
ATOM   12374 O O   . PRO C  1 488 ? -28.552  82.286  -52.093  1.00 44.91  ? 488 PRO C O   1 
ATOM   12375 C CB  . PRO C  1 488 ? -29.577  81.090  -54.867  1.00 40.20  ? 488 PRO C CB  1 
ATOM   12376 C CG  . PRO C  1 488 ? -28.489  80.609  -55.781  1.00 38.66  ? 488 PRO C CG  1 
ATOM   12377 C CD  . PRO C  1 488 ? -27.222  81.283  -55.286  1.00 39.66  ? 488 PRO C CD  1 
ATOM   12378 N N   . ASP C  1 489 ? -30.337  83.600  -52.584  1.00 45.61  ? 489 ASP C N   1 
ATOM   12379 C CA  . ASP C  1 489 ? -30.734  83.864  -51.207  1.00 46.48  ? 489 ASP C CA  1 
ATOM   12380 C C   . ASP C  1 489 ? -31.078  82.578  -50.454  1.00 44.97  ? 489 ASP C C   1 
ATOM   12381 O O   . ASP C  1 489 ? -30.893  82.514  -49.240  1.00 45.34  ? 489 ASP C O   1 
ATOM   12382 C CB  . ASP C  1 489 ? -31.897  84.848  -51.148  1.00 47.59  ? 489 ASP C CB  1 
ATOM   12383 C CG  . ASP C  1 489 ? -31.551  86.281  -51.493  1.00 49.81  ? 489 ASP C CG  1 
ATOM   12384 O OD1 . ASP C  1 489 ? -30.398  86.694  -51.265  1.00 49.88  ? 489 ASP C OD1 1 
ATOM   12385 O OD2 . ASP C  1 489 ? -32.443  86.974  -51.993  1.00 52.89  ? 489 ASP C OD2 1 
ATOM   12386 N N   . ASN C  1 490 ? -31.584  81.560  -51.156  1.00 44.04  ? 490 ASN C N   1 
ATOM   12387 C CA  . ASN C  1 490 ? -31.836  80.274  -50.522  1.00 44.32  ? 490 ASN C CA  1 
ATOM   12388 C C   . ASN C  1 490 ? -30.717  79.260  -50.819  1.00 44.21  ? 490 ASN C C   1 
ATOM   12389 O O   . ASN C  1 490 ? -30.956  78.040  -50.867  1.00 42.65  ? 490 ASN C O   1 
ATOM   12390 C CB  . ASN C  1 490 ? -33.225  79.781  -50.906  1.00 44.96  ? 490 ASN C CB  1 
ATOM   12391 C CG  . ASN C  1 490 ? -33.331  79.406  -52.364  1.00 44.28  ? 490 ASN C CG  1 
ATOM   12392 O OD1 . ASN C  1 490 ? -32.720  80.040  -53.236  1.00 44.85  ? 490 ASN C OD1 1 
ATOM   12393 N ND2 . ASN C  1 490 ? -34.080  78.358  -52.651  1.00 43.53  ? 490 ASN C ND2 1 
ATOM   12394 N N   . CYS C  1 491 ? -29.470  79.750  -50.982  1.00 44.92  ? 491 CYS C N   1 
ATOM   12395 C CA  . CYS C  1 491 ? -28.292  78.885  -50.967  1.00 43.12  ? 491 CYS C CA  1 
ATOM   12396 C C   . CYS C  1 491 ? -27.755  78.852  -49.546  1.00 43.79  ? 491 CYS C C   1 
ATOM   12397 O O   . CYS C  1 491 ? -27.501  79.921  -48.958  1.00 44.51  ? 491 CYS C O   1 
ATOM   12398 C CB  . CYS C  1 491 ? -27.190  79.362  -51.905  1.00 43.66  ? 491 CYS C CB  1 
ATOM   12399 S SG  . CYS C  1 491 ? -25.702  78.328  -51.875  1.00 40.44  ? 491 CYS C SG  1 
ATOM   12400 N N   . TRP C  1 492 ? -27.690  77.622  -49.000  1.00 42.86  ? 492 TRP C N   1 
ATOM   12401 C CA  . TRP C  1 492 ? -27.312  77.359  -47.614  1.00 42.86  ? 492 TRP C CA  1 
ATOM   12402 C C   . TRP C  1 492 ? -25.867  76.872  -47.570  1.00 40.35  ? 492 TRP C C   1 
ATOM   12403 O O   . TRP C  1 492 ? -25.125  77.154  -46.635  1.00 39.77  ? 492 TRP C O   1 
ATOM   12404 C CB  . TRP C  1 492 ? -28.268  76.338  -46.971  1.00 43.92  ? 492 TRP C CB  1 
ATOM   12405 C CG  . TRP C  1 492 ? -29.727  76.616  -47.229  1.00 44.00  ? 492 TRP C CG  1 
ATOM   12406 C CD1 . TRP C  1 492 ? -30.608  75.753  -47.804  1.00 44.14  ? 492 TRP C CD1 1 
ATOM   12407 C CD2 . TRP C  1 492 ? -30.462  77.822  -46.956  1.00 45.23  ? 492 TRP C CD2 1 
ATOM   12408 N NE1 . TRP C  1 492 ? -31.841  76.335  -47.910  1.00 45.46  ? 492 TRP C NE1 1 
ATOM   12409 C CE2 . TRP C  1 492 ? -31.787  77.600  -47.402  1.00 45.47  ? 492 TRP C CE2 1 
ATOM   12410 C CE3 . TRP C  1 492 ? -30.140  79.078  -46.400  1.00 46.75  ? 492 TRP C CE3 1 
ATOM   12411 C CZ2 . TRP C  1 492 ? -32.779  78.581  -47.309  1.00 46.80  ? 492 TRP C CZ2 1 
ATOM   12412 C CZ3 . TRP C  1 492 ? -31.122  80.045  -46.304  1.00 46.45  ? 492 TRP C CZ3 1 
ATOM   12413 C CH2 . TRP C  1 492 ? -32.417  79.807  -46.777  1.00 47.09  ? 492 TRP C CH2 1 
ATOM   12414 N N   . VAL C  1 493 ? -25.480  76.164  -48.626  1.00 38.80  ? 493 VAL C N   1 
ATOM   12415 C CA  . VAL C  1 493 ? -24.118  75.708  -48.758  1.00 38.78  ? 493 VAL C CA  1 
ATOM   12416 C C   . VAL C  1 493 ? -23.760  75.657  -50.236  1.00 37.90  ? 493 VAL C C   1 
ATOM   12417 O O   . VAL C  1 493 ? -24.630  75.415  -51.075  1.00 38.21  ? 493 VAL C O   1 
ATOM   12418 C CB  . VAL C  1 493 ? -23.978  74.323  -48.111  1.00 38.77  ? 493 VAL C CB  1 
ATOM   12419 C CG1 . VAL C  1 493 ? -24.932  73.326  -48.745  1.00 37.96  ? 493 VAL C CG1 1 
ATOM   12420 C CG2 . VAL C  1 493 ? -22.552  73.802  -48.186  1.00 39.04  ? 493 VAL C CG2 1 
ATOM   12421 N N   . VAL C  1 494 ? -22.471  75.871  -50.527  1.00 37.02  ? 494 VAL C N   1 
ATOM   12422 C CA  . VAL C  1 494 ? -21.979  75.828  -51.888  1.00 35.78  ? 494 VAL C CA  1 
ATOM   12423 C C   . VAL C  1 494 ? -20.717  74.974  -51.910  1.00 35.26  ? 494 VAL C C   1 
ATOM   12424 O O   . VAL C  1 494 ? -19.929  75.014  -50.977  1.00 35.07  ? 494 VAL C O   1 
ATOM   12425 C CB  . VAL C  1 494 ? -21.705  77.241  -52.436  1.00 35.91  ? 494 VAL C CB  1 
ATOM   12426 C CG1 . VAL C  1 494 ? -20.652  77.972  -51.622  1.00 37.03  ? 494 VAL C CG1 1 
ATOM   12427 C CG2 . VAL C  1 494 ? -21.267  77.195  -53.890  1.00 35.30  ? 494 VAL C CG2 1 
ATOM   12428 N N   . ASN C  1 495 ? -20.562  74.182  -52.974  1.00 35.21  ? 495 ASN C N   1 
ATOM   12429 C CA  . ASN C  1 495 ? -19.280  73.584  -53.291  1.00 35.58  ? 495 ASN C CA  1 
ATOM   12430 C C   . ASN C  1 495 ? -18.688  74.342  -54.470  1.00 36.08  ? 495 ASN C C   1 
ATOM   12431 O O   . ASN C  1 495 ? -19.189  74.247  -55.598  1.00 36.58  ? 495 ASN C O   1 
ATOM   12432 C CB  . ASN C  1 495 ? -19.396  72.106  -53.637  1.00 34.87  ? 495 ASN C CB  1 
ATOM   12433 C CG  . ASN C  1 495 ? -18.043  71.445  -53.799  1.00 34.76  ? 495 ASN C CG  1 
ATOM   12434 O OD1 . ASN C  1 495 ? -17.114  71.999  -54.393  1.00 34.43  ? 495 ASN C OD1 1 
ATOM   12435 N ND2 . ASN C  1 495 ? -17.936  70.216  -53.329  1.00 35.75  ? 495 ASN C ND2 1 
ATOM   12436 N N   . ALA C  1 496 ? -17.621  75.093  -54.192  1.00 36.50  ? 496 ALA C N   1 
ATOM   12437 C CA  . ALA C  1 496 ? -16.979  75.880  -55.229  1.00 36.43  ? 496 ALA C CA  1 
ATOM   12438 C C   . ALA C  1 496 ? -15.717  75.143  -55.623  1.00 35.93  ? 496 ALA C C   1 
ATOM   12439 O O   . ALA C  1 496 ? -14.893  74.845  -54.764  1.00 35.86  ? 496 ALA C O   1 
ATOM   12440 C CB  . ALA C  1 496 ? -16.689  77.290  -54.746  1.00 37.30  ? 496 ALA C CB  1 
ATOM   12441 N N   . SER C  1 497 ? -15.598  74.839  -56.915  1.00 35.69  ? 497 SER C N   1 
ATOM   12442 C CA  . SER C  1 497 ? -14.452  74.095  -57.378  1.00 35.46  ? 497 SER C CA  1 
ATOM   12443 C C   . SER C  1 497 ? -13.968  74.634  -58.714  1.00 34.61  ? 497 SER C C   1 
ATOM   12444 O O   . SER C  1 497 ? -14.669  75.359  -59.413  1.00 34.96  ? 497 SER C O   1 
ATOM   12445 C CB  . SER C  1 497 ? -14.790  72.625  -57.433  1.00 35.36  ? 497 SER C CB  1 
ATOM   12446 O OG  . SER C  1 497 ? -15.860  72.356  -58.332  1.00 34.73  ? 497 SER C OG  1 
ATOM   12447 N N   . ALA C  1 498 ? -12.728  74.289  -59.034  1.00 34.18  ? 498 ALA C N   1 
ATOM   12448 C CA  . ALA C  1 498 ? -12.198  74.480  -60.371  1.00 34.47  ? 498 ALA C CA  1 
ATOM   12449 C C   . ALA C  1 498 ? -11.149  73.400  -60.653  1.00 34.02  ? 498 ALA C C   1 
ATOM   12450 O O   . ALA C  1 498 ? -10.590  72.829  -59.722  1.00 33.47  ? 498 ALA C O   1 
ATOM   12451 C CB  . ALA C  1 498 ? -11.652  75.888  -60.519  1.00 34.38  ? 498 ALA C CB  1 
ATOM   12452 N N   . GLY C  1 499 ? -10.926  73.109  -61.939  1.00 34.49  ? 499 GLY C N   1 
ATOM   12453 C CA  . GLY C  1 499 ? -10.036  72.034  -62.339  1.00 34.10  ? 499 GLY C CA  1 
ATOM   12454 C C   . GLY C  1 499 ? -9.676   72.031  -63.828  1.00 33.85  ? 499 GLY C C   1 
ATOM   12455 O O   . GLY C  1 499 ? -10.405  72.538  -64.676  1.00 31.71  ? 499 GLY C O   1 
ATOM   12456 N N   . ILE C  1 500 ? -8.526   71.419  -64.143  1.00 34.85  ? 500 ILE C N   1 
ATOM   12457 C CA  . ILE C  1 500 ? -8.055   71.344  -65.512  1.00 33.91  ? 500 ILE C CA  1 
ATOM   12458 C C   . ILE C  1 500 ? -7.333   70.013  -65.721  1.00 33.30  ? 500 ILE C C   1 
ATOM   12459 O O   . ILE C  1 500 ? -6.773   69.472  -64.786  1.00 32.55  ? 500 ILE C O   1 
ATOM   12460 C CB  . ILE C  1 500 ? -7.166   72.554  -65.828  1.00 33.80  ? 500 ILE C CB  1 
ATOM   12461 C CG1 . ILE C  1 500 ? -6.979   72.673  -67.331  1.00 34.60  ? 500 ILE C CG1 1 
ATOM   12462 C CG2 . ILE C  1 500 ? -5.852   72.497  -65.048  1.00 33.44  ? 500 ILE C CG2 1 
ATOM   12463 C CD1 . ILE C  1 500 ? -6.369   73.987  -67.783  1.00 36.41  ? 500 ILE C CD1 1 
ATOM   12464 N N   . SER C  1 501 ? -7.326   69.523  -66.967  1.00 33.63  ? 501 SER C N   1 
ATOM   12465 C CA  . SER C  1 501 ? -6.682   68.265  -67.307  1.00 34.41  ? 501 SER C CA  1 
ATOM   12466 C C   . SER C  1 501 ? -5.184   68.433  -67.581  1.00 35.15  ? 501 SER C C   1 
ATOM   12467 O O   . SER C  1 501 ? -4.763   69.419  -68.190  1.00 38.09  ? 501 SER C O   1 
ATOM   12468 C CB  . SER C  1 501 ? -7.410   67.633  -68.459  1.00 33.04  ? 501 SER C CB  1 
ATOM   12469 O OG  . SER C  1 501 ? -8.671   67.213  -67.978  1.00 32.68  ? 501 SER C OG  1 
ATOM   12470 N N   . VAL C  1 502 ? -4.380   67.463  -67.116  1.00 35.96  ? 502 VAL C N   1 
ATOM   12471 C CA  . VAL C  1 502 ? -2.934   67.462  -67.350  1.00 38.94  ? 502 VAL C CA  1 
ATOM   12472 C C   . VAL C  1 502 ? -2.470   66.146  -67.978  1.00 39.11  ? 502 VAL C C   1 
ATOM   12473 O O   . VAL C  1 502 ? -2.942   65.065  -67.601  1.00 39.51  ? 502 VAL C O   1 
ATOM   12474 C CB  . VAL C  1 502 ? -2.168   67.687  -66.046  1.00 41.37  ? 502 VAL C CB  1 
ATOM   12475 C CG1 . VAL C  1 502 ? -0.670   67.723  -66.302  1.00 44.68  ? 502 VAL C CG1 1 
ATOM   12476 C CG2 . VAL C  1 502 ? -2.608   68.970  -65.352  1.00 43.48  ? 502 VAL C CG2 1 
ATOM   12477 N N   . ARG C  1 503 ? -1.518   66.254  -68.914  1.00 39.85  ? 503 ARG C N   1 
ATOM   12478 C CA  . ARG C  1 503 ? -0.991   65.122  -69.661  1.00 40.77  ? 503 ARG C CA  1 
ATOM   12479 C C   . ARG C  1 503 ? 0.511    65.014  -69.422  1.00 39.01  ? 503 ARG C C   1 
ATOM   12480 O O   . ARG C  1 503 ? 1.206    66.021  -69.482  1.00 38.95  ? 503 ARG C O   1 
ATOM   12481 C CB  . ARG C  1 503 ? -1.274   65.204  -71.166  1.00 44.85  ? 503 ARG C CB  1 
ATOM   12482 C CG  . ARG C  1 503 ? -0.824   63.965  -71.933  1.00 50.99  ? 503 ARG C CG  1 
ATOM   12483 C CD  . ARG C  1 503 ? -0.859   64.097  -73.463  1.00 55.88  ? 503 ARG C CD  1 
ATOM   12484 N NE  . ARG C  1 503 ? -2.226   64.030  -73.998  1.00 64.65  ? 503 ARG C NE  1 
ATOM   12485 C CZ  . ARG C  1 503 ? -3.034   62.955  -74.064  1.00 67.08  ? 503 ARG C CZ  1 
ATOM   12486 N NH1 . ARG C  1 503 ? -2.594   61.725  -73.811  1.00 62.29  ? 503 ARG C NH1 1 
ATOM   12487 N NH2 . ARG C  1 503 ? -4.300   63.123  -74.423  1.00 66.47  ? 503 ARG C NH2 1 
ATOM   12488 N N   . TYR C  1 504 ? 0.973    63.798  -69.080  1.00 36.95  ? 504 TYR C N   1 
ATOM   12489 C CA  . TYR C  1 504 ? 2.372    63.411  -69.203  1.00 35.45  ? 504 TYR C CA  1 
ATOM   12490 C C   . TYR C  1 504 ? 2.412    62.062  -69.937  1.00 34.72  ? 504 TYR C C   1 
ATOM   12491 O O   . TYR C  1 504 ? 2.009    61.044  -69.379  1.00 33.37  ? 504 TYR C O   1 
ATOM   12492 C CB  . TYR C  1 504 ? 3.063    63.328  -67.837  1.00 34.98  ? 504 TYR C CB  1 
ATOM   12493 C CG  . TYR C  1 504 ? 4.561    63.041  -67.929  1.00 35.89  ? 504 TYR C CG  1 
ATOM   12494 C CD1 . TYR C  1 504 ? 5.055    61.786  -68.290  1.00 35.45  ? 504 TYR C CD1 1 
ATOM   12495 C CD2 . TYR C  1 504 ? 5.493    64.033  -67.669  1.00 36.66  ? 504 TYR C CD2 1 
ATOM   12496 C CE1 . TYR C  1 504 ? 6.414    61.551  -68.411  1.00 36.12  ? 504 TYR C CE1 1 
ATOM   12497 C CE2 . TYR C  1 504 ? 6.858    63.814  -67.803  1.00 36.88  ? 504 TYR C CE2 1 
ATOM   12498 C CZ  . TYR C  1 504 ? 7.322    62.570  -68.168  1.00 36.59  ? 504 TYR C CZ  1 
ATOM   12499 O OH  . TYR C  1 504 ? 8.662    62.371  -68.257  1.00 35.73  ? 504 TYR C OH  1 
ATOM   12500 N N   . GLY C  1 505 ? 2.892    62.064  -71.185  1.00 34.07  ? 505 GLY C N   1 
ATOM   12501 C CA  . GLY C  1 505 ? 2.920    60.879  -72.016  1.00 34.05  ? 505 GLY C CA  1 
ATOM   12502 C C   . GLY C  1 505 ? 1.495    60.434  -72.291  1.00 33.98  ? 505 GLY C C   1 
ATOM   12503 O O   . GLY C  1 505 ? 0.707    61.236  -72.750  1.00 34.24  ? 505 GLY C O   1 
ATOM   12504 N N   . LYS C  1 506 ? 1.158    59.190  -71.943  1.00 33.80  ? 506 LYS C N   1 
ATOM   12505 C CA  . LYS C  1 506 ? -0.207   58.689  -72.087  1.00 33.82  ? 506 LYS C CA  1 
ATOM   12506 C C   . LYS C  1 506 ? -1.019   58.826  -70.797  1.00 33.29  ? 506 LYS C C   1 
ATOM   12507 O O   . LYS C  1 506 ? -2.162   58.359  -70.724  1.00 35.26  ? 506 LYS C O   1 
ATOM   12508 C CB  . LYS C  1 506 ? -0.185   57.198  -72.443  1.00 33.50  ? 506 LYS C CB  1 
ATOM   12509 C CG  . LYS C  1 506 ? 0.689    56.801  -73.630  1.00 35.58  ? 506 LYS C CG  1 
ATOM   12510 C CD  . LYS C  1 506 ? 0.729    55.281  -73.780  1.00 36.38  ? 506 LYS C CD  1 
ATOM   12511 C CE  . LYS C  1 506 ? 1.525    54.853  -74.955  1.00 38.60  ? 506 LYS C CE  1 
ATOM   12512 N NZ  . LYS C  1 506 ? 1.533    53.385  -75.053  1.00 40.48  ? 506 LYS C NZ  1 
ATOM   12513 N N   . PHE C  1 507 ? -0.431   59.460  -69.776  1.00 32.65  ? 507 PHE C N   1 
ATOM   12514 C CA  . PHE C  1 507 ? -1.065   59.625  -68.480  1.00 31.29  ? 507 PHE C CA  1 
ATOM   12515 C C   . PHE C  1 507 ? -1.756   60.988  -68.421  1.00 31.92  ? 507 PHE C C   1 
ATOM   12516 O O   . PHE C  1 507 ? -1.111   62.038  -68.512  1.00 33.58  ? 507 PHE C O   1 
ATOM   12517 C CB  . PHE C  1 507 ? 0.036    59.404  -67.438  1.00 31.14  ? 507 PHE C CB  1 
ATOM   12518 C CG  . PHE C  1 507 ? -0.407   59.422  -65.984  1.00 30.17  ? 507 PHE C CG  1 
ATOM   12519 C CD1 . PHE C  1 507 ? -0.552   60.627  -65.304  1.00 29.02  ? 507 PHE C CD1 1 
ATOM   12520 C CD2 . PHE C  1 507 ? -0.687   58.228  -65.315  1.00 30.09  ? 507 PHE C CD2 1 
ATOM   12521 C CE1 . PHE C  1 507 ? -0.962   60.644  -63.991  1.00 29.55  ? 507 PHE C CE1 1 
ATOM   12522 C CE2 . PHE C  1 507 ? -1.048   58.240  -63.978  1.00 29.85  ? 507 PHE C CE2 1 
ATOM   12523 C CZ  . PHE C  1 507 ? -1.204   59.451  -63.323  1.00 30.87  ? 507 PHE C CZ  1 
ATOM   12524 N N   . THR C  1 508 ? -3.082   60.950  -68.279  1.00 32.24  ? 508 THR C N   1 
ATOM   12525 C CA  . THR C  1 508 ? -3.908   62.148  -68.179  1.00 33.87  ? 508 THR C CA  1 
ATOM   12526 C C   . THR C  1 508 ? -4.582   62.106  -66.818  1.00 32.35  ? 508 THR C C   1 
ATOM   12527 O O   . THR C  1 508 ? -4.972   61.031  -66.371  1.00 31.26  ? 508 THR C O   1 
ATOM   12528 C CB  . THR C  1 508 ? -4.954   62.208  -69.287  1.00 34.15  ? 508 THR C CB  1 
ATOM   12529 O OG1 . THR C  1 508 ? -5.503   60.888  -69.264  1.00 39.80  ? 508 THR C OG1 1 
ATOM   12530 C CG2 . THR C  1 508 ? -4.334   62.462  -70.641  1.00 35.42  ? 508 THR C CG2 1 
ATOM   12531 N N   . PHE C  1 509 ? -4.659   63.268  -66.161  1.00 32.07  ? 509 PHE C N   1 
ATOM   12532 C CA  . PHE C  1 509 ? -5.293   63.387  -64.856  1.00 31.94  ? 509 PHE C CA  1 
ATOM   12533 C C   . PHE C  1 509 ? -5.728   64.842  -64.700  1.00 32.21  ? 509 PHE C C   1 
ATOM   12534 O O   . PHE C  1 509 ? -5.537   65.636  -65.602  1.00 32.51  ? 509 PHE C O   1 
ATOM   12535 C CB  . PHE C  1 509 ? -4.355   62.904  -63.735  1.00 30.85  ? 509 PHE C CB  1 
ATOM   12536 C CG  . PHE C  1 509 ? -3.135   63.785  -63.520  1.00 30.47  ? 509 PHE C CG  1 
ATOM   12537 C CD1 . PHE C  1 509 ? -2.140   63.871  -64.489  1.00 30.33  ? 509 PHE C CD1 1 
ATOM   12538 C CD2 . PHE C  1 509 ? -3.002   64.556  -62.375  1.00 30.40  ? 509 PHE C CD2 1 
ATOM   12539 C CE1 . PHE C  1 509 ? -1.028   64.696  -64.308  1.00 31.34  ? 509 PHE C CE1 1 
ATOM   12540 C CE2 . PHE C  1 509 ? -1.884   65.369  -62.203  1.00 31.30  ? 509 PHE C CE2 1 
ATOM   12541 C CZ  . PHE C  1 509 ? -0.899   65.436  -63.167  1.00 31.13  ? 509 PHE C CZ  1 
ATOM   12542 N N   . LYS C  1 510 ? -6.317   65.163  -63.553  1.00 34.68  ? 510 LYS C N   1 
ATOM   12543 C CA  . LYS C  1 510 ? -6.843   66.484  -63.268  1.00 36.88  ? 510 LYS C CA  1 
ATOM   12544 C C   . LYS C  1 510 ? -6.165   67.035  -62.021  1.00 35.99  ? 510 LYS C C   1 
ATOM   12545 O O   . LYS C  1 510 ? -5.841   66.280  -61.098  1.00 33.57  ? 510 LYS C O   1 
ATOM   12546 C CB  . LYS C  1 510 ? -8.358   66.401  -63.047  1.00 40.70  ? 510 LYS C CB  1 
ATOM   12547 C CG  . LYS C  1 510 ? -9.101   66.015  -64.299  1.00 45.50  ? 510 LYS C CG  1 
ATOM   12548 C CD  . LYS C  1 510 ? -10.616  65.999  -64.185  1.00 51.05  ? 510 LYS C CD  1 
ATOM   12549 C CE  . LYS C  1 510 ? -11.264  66.352  -65.483  1.00 52.03  ? 510 LYS C CE  1 
ATOM   12550 N NZ  . LYS C  1 510 ? -11.114  67.792  -65.624  1.00 56.03  ? 510 LYS C NZ  1 
ATOM   12551 N N   . ILE C  1 511 ? -5.941   68.355  -62.031  1.00 35.78  ? 511 ILE C N   1 
ATOM   12552 C CA  . ILE C  1 511 ? -5.569   69.106  -60.835  1.00 36.12  ? 511 ILE C CA  1 
ATOM   12553 C C   . ILE C  1 511 ? -6.724   70.055  -60.546  1.00 36.09  ? 511 ILE C C   1 
ATOM   12554 O O   . ILE C  1 511 ? -7.373   70.541  -61.475  1.00 36.98  ? 511 ILE C O   1 
ATOM   12555 C CB  . ILE C  1 511 ? -4.235   69.856  -60.989  1.00 35.46  ? 511 ILE C CB  1 
ATOM   12556 C CG1 . ILE C  1 511 ? -4.291   70.897  -62.101  1.00 35.96  ? 511 ILE C CG1 1 
ATOM   12557 C CG2 . ILE C  1 511 ? -3.096   68.867  -61.190  1.00 35.97  ? 511 ILE C CG2 1 
ATOM   12558 C CD1 . ILE C  1 511 ? -3.014   71.702  -62.277  1.00 37.98  ? 511 ILE C CD1 1 
ATOM   12559 N N   . HIS C  1 512 ? -6.958   70.338  -59.266  1.00 34.13  ? 512 HIS C N   1 
ATOM   12560 C CA  . HIS C  1 512 ? -8.218   70.931  -58.880  1.00 32.92  ? 512 HIS C CA  1 
ATOM   12561 C C   . HIS C  1 512 ? -8.133   71.353  -57.423  1.00 33.71  ? 512 HIS C C   1 
ATOM   12562 O O   . HIS C  1 512 ? -7.240   70.975  -56.698  1.00 35.07  ? 512 HIS C O   1 
ATOM   12563 C CB  . HIS C  1 512 ? -9.340   69.909  -59.077  1.00 31.65  ? 512 HIS C CB  1 
ATOM   12564 C CG  . HIS C  1 512 ? -8.920   68.558  -58.615  1.00 32.15  ? 512 HIS C CG  1 
ATOM   12565 N ND1 . HIS C  1 512 ? -8.642   68.274  -57.291  1.00 32.62  ? 512 HIS C ND1 1 
ATOM   12566 C CD2 . HIS C  1 512 ? -8.628   67.445  -59.313  1.00 32.57  ? 512 HIS C CD2 1 
ATOM   12567 C CE1 . HIS C  1 512 ? -8.230   67.006  -57.197  1.00 34.12  ? 512 HIS C CE1 1 
ATOM   12568 N NE2 . HIS C  1 512 ? -8.219   66.471  -58.415  1.00 33.14  ? 512 HIS C NE2 1 
ATOM   12569 N N   . ASP C  1 513 ? -9.092   72.164  -57.019  1.00 35.20  ? 513 ASP C N   1 
ATOM   12570 C CA  . ASP C  1 513 ? -9.258   72.568  -55.646  1.00 35.07  ? 513 ASP C CA  1 
ATOM   12571 C C   . ASP C  1 513 ? -10.756  72.751  -55.443  1.00 36.05  ? 513 ASP C C   1 
ATOM   12572 O O   . ASP C  1 513 ? -11.555  72.746  -56.393  1.00 34.76  ? 513 ASP C O   1 
ATOM   12573 C CB  . ASP C  1 513 ? -8.453   73.828  -55.383  1.00 36.62  ? 513 ASP C CB  1 
ATOM   12574 C CG  . ASP C  1 513 ? -8.237   74.209  -53.925  1.00 36.67  ? 513 ASP C CG  1 
ATOM   12575 O OD1 . ASP C  1 513 ? -8.545   73.374  -53.031  1.00 35.44  ? 513 ASP C OD1 1 
ATOM   12576 O OD2 . ASP C  1 513 ? -7.771   75.342  -53.704  1.00 36.71  ? 513 ASP C OD2 1 
ATOM   12577 N N   . GLN C  1 514 ? -11.114  72.904  -54.172  1.00 38.62  ? 514 GLN C N   1 
ATOM   12578 C CA  . GLN C  1 514 ? -12.487  72.746  -53.745  1.00 38.97  ? 514 GLN C CA  1 
ATOM   12579 C C   . GLN C  1 514 ? -12.649  73.461  -52.418  1.00 38.66  ? 514 GLN C C   1 
ATOM   12580 O O   . GLN C  1 514 ? -11.819  73.299  -51.536  1.00 41.25  ? 514 GLN C O   1 
ATOM   12581 C CB  . GLN C  1 514 ? -12.788  71.249  -53.603  1.00 38.52  ? 514 GLN C CB  1 
ATOM   12582 C CG  . GLN C  1 514 ? -14.237  70.972  -53.235  1.00 38.72  ? 514 GLN C CG  1 
ATOM   12583 C CD  . GLN C  1 514 ? -14.471  69.580  -52.711  1.00 39.92  ? 514 GLN C CD  1 
ATOM   12584 O OE1 . GLN C  1 514 ? -13.944  69.198  -51.665  1.00 44.12  ? 514 GLN C OE1 1 
ATOM   12585 N NE2 . GLN C  1 514 ? -15.279  68.812  -53.422  1.00 39.73  ? 514 GLN C NE2 1 
ATOM   12586 N N   . LYS C  1 515 ? -13.712  74.250  -52.296  1.00 38.39  ? 515 LYS C N   1 
ATOM   12587 C CA  . LYS C  1 515 ? -14.096  74.819  -51.014  1.00 38.77  ? 515 LYS C CA  1 
ATOM   12588 C C   . LYS C  1 515 ? -15.578  74.594  -50.789  1.00 39.14  ? 515 LYS C C   1 
ATOM   12589 O O   . LYS C  1 515 ? -16.387  74.857  -51.687  1.00 39.02  ? 515 LYS C O   1 
ATOM   12590 C CB  . LYS C  1 515 ? -13.907  76.332  -50.929  1.00 37.98  ? 515 LYS C CB  1 
ATOM   12591 C CG  . LYS C  1 515 ? -12.507  76.733  -51.229  1.00 37.66  ? 515 LYS C CG  1 
ATOM   12592 C CD  . LYS C  1 515 ? -11.420  76.256  -50.272  1.00 38.01  ? 515 LYS C CD  1 
ATOM   12593 C CE  . LYS C  1 515 ? -10.119  76.734  -50.827  1.00 38.35  ? 515 LYS C CE  1 
ATOM   12594 N NZ  . LYS C  1 515 ? -9.023   76.516  -49.911  1.00 39.82  ? 515 LYS C NZ  1 
ATOM   12595 N N   . ILE C  1 516 ? -15.905  74.137  -49.575  1.00 41.40  ? 516 ILE C N   1 
ATOM   12596 C CA  . ILE C  1 516 ? -17.291  74.022  -49.136  1.00 42.51  ? 516 ILE C CA  1 
ATOM   12597 C C   . ILE C  1 516 ? -17.590  75.166  -48.183  1.00 41.19  ? 516 ILE C C   1 
ATOM   12598 O O   . ILE C  1 516 ? -16.899  75.285  -47.196  1.00 41.23  ? 516 ILE C O   1 
ATOM   12599 C CB  . ILE C  1 516 ? -17.551  72.652  -48.493  1.00 43.73  ? 516 ILE C CB  1 
ATOM   12600 C CG1 . ILE C  1 516 ? -17.150  71.519  -49.452  1.00 41.39  ? 516 ILE C CG1 1 
ATOM   12601 C CG2 . ILE C  1 516 ? -19.017  72.561  -48.036  1.00 45.98  ? 516 ILE C CG2 1 
ATOM   12602 C CD1 . ILE C  1 516 ? -17.070  70.132  -48.829  1.00 40.40  ? 516 ILE C CD1 1 
ATOM   12603 N N   . ILE C  1 517 ? -18.598  75.995  -48.490  1.00 41.59  ? 517 ILE C N   1 
ATOM   12604 C CA  . ILE C  1 517 ? -18.813  77.235  -47.747  1.00 43.90  ? 517 ILE C CA  1 
ATOM   12605 C C   . ILE C  1 517 ? -20.282  77.333  -47.369  1.00 44.50  ? 517 ILE C C   1 
ATOM   12606 O O   . ILE C  1 517 ? -21.125  77.022  -48.201  1.00 44.40  ? 517 ILE C O   1 
ATOM   12607 C CB  . ILE C  1 517 ? -18.335  78.447  -48.580  1.00 44.41  ? 517 ILE C CB  1 
ATOM   12608 C CG1 . ILE C  1 517 ? -16.839  78.369  -48.835  1.00 44.35  ? 517 ILE C CG1 1 
ATOM   12609 C CG2 . ILE C  1 517 ? -18.713  79.800  -47.972  1.00 45.24  ? 517 ILE C CG2 1 
ATOM   12610 C CD1 . ILE C  1 517 ? -16.411  79.087  -50.095  1.00 45.13  ? 517 ILE C CD1 1 
ATOM   12611 N N   . TYR C  1 518 ? -20.546  77.785  -46.130  1.00 47.06  ? 518 TYR C N   1 
ATOM   12612 C CA  . TYR C  1 518 ? -21.867  77.743  -45.520  1.00 48.39  ? 518 TYR C CA  1 
ATOM   12613 C C   . TYR C  1 518 ? -22.377  79.167  -45.336  1.00 49.55  ? 518 TYR C C   1 
ATOM   12614 O O   . TYR C  1 518 ? -21.587  80.100  -45.242  1.00 48.73  ? 518 TYR C O   1 
ATOM   12615 C CB  . TYR C  1 518 ? -21.884  77.044  -44.153  1.00 49.95  ? 518 TYR C CB  1 
ATOM   12616 C CG  . TYR C  1 518 ? -21.459  75.577  -44.110  1.00 50.65  ? 518 TYR C CG  1 
ATOM   12617 C CD1 . TYR C  1 518 ? -22.341  74.551  -44.449  1.00 50.22  ? 518 TYR C CD1 1 
ATOM   12618 C CD2 . TYR C  1 518 ? -20.174  75.213  -43.725  1.00 49.89  ? 518 TYR C CD2 1 
ATOM   12619 C CE1 . TYR C  1 518 ? -21.958  73.217  -44.411  1.00 49.64  ? 518 TYR C CE1 1 
ATOM   12620 C CE2 . TYR C  1 518 ? -19.779  73.889  -43.696  1.00 49.35  ? 518 TYR C CE2 1 
ATOM   12621 C CZ  . TYR C  1 518 ? -20.672  72.877  -44.021  1.00 49.58  ? 518 TYR C CZ  1 
ATOM   12622 O OH  . TYR C  1 518 ? -20.274  71.559  -43.940  1.00 45.56  ? 518 TYR C OH  1 
ATOM   12623 N N   . ARG C  1 519 ? -23.695  79.300  -45.288  1.00 50.68  ? 519 ARG C N   1 
ATOM   12624 C CA  . ARG C  1 519 ? -24.284  80.622  -45.003  1.00 53.97  ? 519 ARG C CA  1 
ATOM   12625 C C   . ARG C  1 519 ? -24.077  80.890  -43.506  1.00 60.26  ? 519 ARG C C   1 
ATOM   12626 O O   . ARG C  1 519 ? -22.952  81.183  -43.110  1.00 60.57  ? 519 ARG C O   1 
ATOM   12627 C CB  . ARG C  1 519 ? -25.742  80.664  -45.455  1.00 51.72  ? 519 ARG C CB  1 
ATOM   12628 C CG  . ARG C  1 519 ? -26.247  82.092  -45.583  1.00 50.43  ? 519 ARG C CG  1 
ATOM   12629 C CD  . ARG C  1 519 ? -27.654  82.187  -46.138  1.00 49.15  ? 519 ARG C CD  1 
ATOM   12630 N NE  . ARG C  1 519 ? -27.691  82.162  -47.604  1.00 48.34  ? 519 ARG C NE  1 
ATOM   12631 C CZ  . ARG C  1 519 ? -27.266  83.120  -48.417  1.00 50.01  ? 519 ARG C CZ  1 
ATOM   12632 N NH1 . ARG C  1 519 ? -26.689  84.205  -47.938  1.00 51.01  ? 519 ARG C NH1 1 
ATOM   12633 N NH2 . ARG C  1 519 ? -27.427  82.991  -49.719  1.00 50.11  ? 519 ARG C NH2 1 
ATOM   12634 N N   . GLY C  1 520 ? -25.079  80.678  -42.672  1.00 63.42  ? 520 GLY C N   1 
ATOM   12635 C CA  . GLY C  1 520 ? -24.872  81.049  -41.264  1.00 66.48  ? 520 GLY C CA  1 
ATOM   12636 C C   . GLY C  1 520 ? -24.200  79.970  -40.450  1.00 65.21  ? 520 GLY C C   1 
ATOM   12637 O O   . GLY C  1 520 ? -23.082  79.573  -40.808  1.00 61.73  ? 520 GLY C O   1 
ATOM   12638 N N   . ASP C  1 521 ? -24.831  79.573  -39.349  1.00 64.10  ? 521 ASP C N   1 
ATOM   12639 C CA  . ASP C  1 521 ? -24.311  78.479  -38.494  1.00 63.85  ? 521 ASP C CA  1 
ATOM   12640 C C   . ASP C  1 521 ? -25.335  77.354  -38.567  1.00 60.64  ? 521 ASP C C   1 
ATOM   12641 O O   . ASP C  1 521 ? -25.349  76.503  -37.667  1.00 62.50  ? 521 ASP C O   1 
ATOM   12642 C CB  . ASP C  1 521 ? -24.079  78.972  -37.078  1.00 65.58  ? 521 ASP C CB  1 
ATOM   12643 C CG  . ASP C  1 521 ? -25.234  79.716  -36.425  1.00 68.09  ? 521 ASP C CG  1 
ATOM   12644 O OD1 . ASP C  1 521 ? -26.340  79.720  -37.002  1.00 66.37  ? 521 ASP C OD1 1 
ATOM   12645 O OD2 . ASP C  1 521 ? -25.013  80.283  -35.337  1.00 69.10  ? 521 ASP C OD2 1 
ATOM   12646 N N   . TRP C  1 522 ? -26.172  77.379  -39.599  1.00 56.66  ? 522 TRP C N   1 
ATOM   12647 C CA  . TRP C  1 522 ? -27.261  76.404  -39.697  1.00 56.05  ? 522 TRP C CA  1 
ATOM   12648 C C   . TRP C  1 522 ? -26.729  74.955  -39.665  1.00 57.17  ? 522 TRP C C   1 
ATOM   12649 O O   . TRP C  1 522 ? -27.431  74.045  -39.224  1.00 53.60  ? 522 TRP C O   1 
ATOM   12650 C CB  . TRP C  1 522 ? -28.117  76.626  -40.965  1.00 53.66  ? 522 TRP C CB  1 
ATOM   12651 C CG  . TRP C  1 522 ? -27.506  76.092  -42.240  1.00 51.53  ? 522 TRP C CG  1 
ATOM   12652 C CD1 . TRP C  1 522 ? -26.615  76.738  -43.042  1.00 50.57  ? 522 TRP C CD1 1 
ATOM   12653 C CD2 . TRP C  1 522 ? -27.673  74.783  -42.834  1.00 52.04  ? 522 TRP C CD2 1 
ATOM   12654 N NE1 . TRP C  1 522 ? -26.219  75.950  -44.084  1.00 47.83  ? 522 TRP C NE1 1 
ATOM   12655 C CE2 . TRP C  1 522 ? -26.851  74.741  -43.982  1.00 49.61  ? 522 TRP C CE2 1 
ATOM   12656 C CE3 . TRP C  1 522 ? -28.423  73.644  -42.511  1.00 52.17  ? 522 TRP C CE3 1 
ATOM   12657 C CZ2 . TRP C  1 522 ? -26.771  73.613  -44.797  1.00 48.34  ? 522 TRP C CZ2 1 
ATOM   12658 C CZ3 . TRP C  1 522 ? -28.341  72.532  -43.318  1.00 50.45  ? 522 TRP C CZ3 1 
ATOM   12659 C CH2 . TRP C  1 522 ? -27.518  72.514  -44.440  1.00 48.83  ? 522 TRP C CH2 1 
ATOM   12660 N N   . ALA C  1 523 ? -25.483  74.769  -40.128  1.00 58.51  ? 523 ALA C N   1 
ATOM   12661 C CA  . ALA C  1 523 ? -24.845  73.475  -40.255  1.00 62.00  ? 523 ALA C CA  1 
ATOM   12662 C C   . ALA C  1 523 ? -23.804  73.212  -39.163  1.00 66.47  ? 523 ALA C C   1 
ATOM   12663 O O   . ALA C  1 523 ? -22.947  72.350  -39.361  1.00 71.33  ? 523 ALA C O   1 
ATOM   12664 C CB  . ALA C  1 523 ? -24.199  73.402  -41.626  1.00 60.65  ? 523 ALA C CB  1 
ATOM   12665 N N   . LYS C  1 524 ? -23.876  73.880  -38.001  1.00 66.86  ? 524 LYS C N   1 
ATOM   12666 C CA  . LYS C  1 524 ? -22.884  73.630  -36.960  1.00 67.63  ? 524 LYS C CA  1 
ATOM   12667 C C   . LYS C  1 524 ? -22.993  72.180  -36.510  1.00 63.81  ? 524 LYS C C   1 
ATOM   12668 O O   . LYS C  1 524 ? -21.973  71.627  -36.126  1.00 62.78  ? 524 LYS C O   1 
ATOM   12669 C CB  . LYS C  1 524 ? -22.853  74.555  -35.731  1.00 74.26  ? 524 LYS C CB  1 
ATOM   12670 C CG  . LYS C  1 524 ? -23.990  74.514  -34.704  1.00 79.75  ? 524 LYS C CG  1 
ATOM   12671 C CD  . LYS C  1 524 ? -23.986  75.759  -33.806  1.00 86.79  ? 524 LYS C CD  1 
ATOM   12672 C CE  . LYS C  1 524 ? -24.900  75.760  -32.594  1.00 89.79  ? 524 LYS C CE  1 
ATOM   12673 N NZ  . LYS C  1 524 ? -26.326  75.736  -32.935  1.00 89.04  ? 524 LYS C NZ  1 
ATOM   12674 N N   . GLU C  1 525 ? -24.183  71.566  -36.629  1.00 61.51  ? 525 GLU C N   1 
ATOM   12675 C CA  . GLU C  1 525 ? -24.352  70.171  -36.224  1.00 62.09  ? 525 GLU C CA  1 
ATOM   12676 C C   . GLU C  1 525 ? -24.056  69.216  -37.388  1.00 60.26  ? 525 GLU C C   1 
ATOM   12677 O O   . GLU C  1 525 ? -23.117  68.422  -37.314  1.00 57.49  ? 525 GLU C O   1 
ATOM   12678 C CB  . GLU C  1 525 ? -25.737  69.837  -35.656  1.00 61.54  ? 525 GLU C CB  1 
ATOM   12679 C CG  . GLU C  1 525 ? -26.171  70.695  -34.470  1.00 62.09  ? 525 GLU C CG  1 
ATOM   12680 C CD  . GLU C  1 525 ? -26.752  72.058  -34.824  1.00 62.00  ? 525 GLU C CD  1 
ATOM   12681 O OE1 . GLU C  1 525 ? -27.320  72.302  -35.917  1.00 58.34  ? 525 GLU C OE1 1 
ATOM   12682 O OE2 . GLU C  1 525 ? -26.590  72.909  -33.940  1.00 64.80  ? 525 GLU C OE2 1 
ATOM   12683 N N   . VAL C  1 526 ? -24.841  69.330  -38.472  1.00 60.03  ? 526 VAL C N   1 
ATOM   12684 C CA  . VAL C  1 526 ? -24.840  68.375  -39.575  1.00 57.58  ? 526 VAL C CA  1 
ATOM   12685 C C   . VAL C  1 526 ? -23.576  68.451  -40.452  1.00 59.51  ? 526 VAL C C   1 
ATOM   12686 O O   . VAL C  1 526 ? -23.193  67.423  -41.045  1.00 61.37  ? 526 VAL C O   1 
ATOM   12687 C CB  . VAL C  1 526 ? -26.120  68.486  -40.433  1.00 57.25  ? 526 VAL C CB  1 
ATOM   12688 C CG1 . VAL C  1 526 ? -26.330  69.855  -41.059  1.00 57.74  ? 526 VAL C CG1 1 
ATOM   12689 C CG2 . VAL C  1 526 ? -26.160  67.425  -41.525  1.00 56.33  ? 526 VAL C CG2 1 
ATOM   12690 N N   . GLY C  1 527 ? -22.910  69.625  -40.532  1.00 56.59  ? 527 GLY C N   1 
ATOM   12691 C CA  . GLY C  1 527 ? -21.804  69.843  -41.463  1.00 53.70  ? 527 GLY C CA  1 
ATOM   12692 C C   . GLY C  1 527 ? -20.464  69.265  -40.995  1.00 54.89  ? 527 GLY C C   1 
ATOM   12693 O O   . GLY C  1 527 ? -20.155  69.238  -39.808  1.00 55.00  ? 527 GLY C O   1 
ATOM   12694 N N   . ARG C  1 528 ? -19.634  68.830  -41.950  1.00 56.03  ? 528 ARG C N   1 
ATOM   12695 C CA  . ARG C  1 528 ? -18.326  68.279  -41.627  1.00 57.05  ? 528 ARG C CA  1 
ATOM   12696 C C   . ARG C  1 528 ? -17.514  69.297  -40.832  1.00 60.67  ? 528 ARG C C   1 
ATOM   12697 O O   . ARG C  1 528 ? -17.573  70.489  -41.120  1.00 59.74  ? 528 ARG C O   1 
ATOM   12698 C CB  . ARG C  1 528 ? -17.541  67.890  -42.887  1.00 54.92  ? 528 ARG C CB  1 
ATOM   12699 C CG  . ARG C  1 528 ? -16.223  67.171  -42.612  1.00 53.61  ? 528 ARG C CG  1 
ATOM   12700 C CD  . ARG C  1 528 ? -15.526  66.759  -43.903  1.00 51.00  ? 528 ARG C CD  1 
ATOM   12701 N NE  . ARG C  1 528 ? -16.286  65.754  -44.658  1.00 47.42  ? 528 ARG C NE  1 
ATOM   12702 C CZ  . ARG C  1 528 ? -16.977  65.945  -45.785  1.00 45.47  ? 528 ARG C CZ  1 
ATOM   12703 N NH1 . ARG C  1 528 ? -17.024  67.129  -46.365  1.00 45.26  ? 528 ARG C NH1 1 
ATOM   12704 N NH2 . ARG C  1 528 ? -17.660  64.950  -46.334  1.00 44.08  ? 528 ARG C NH2 1 
ATOM   12705 N N   . LYS C  1 529 ? -16.728  68.790  -39.873  1.00 65.76  ? 529 LYS C N   1 
ATOM   12706 C CA  . LYS C  1 529 ? -15.827  69.595  -39.058  1.00 72.51  ? 529 LYS C CA  1 
ATOM   12707 C C   . LYS C  1 529 ? -14.362  69.283  -39.434  1.00 70.38  ? 529 LYS C C   1 
ATOM   12708 O O   . LYS C  1 529 ? -14.114  68.150  -39.925  1.00 65.80  ? 529 LYS C O   1 
ATOM   12709 C CB  . LYS C  1 529 ? -16.066  69.336  -37.560  1.00 79.16  ? 529 LYS C CB  1 
ATOM   12710 C CG  . LYS C  1 529 ? -17.097  70.221  -36.821  1.00 83.74  ? 529 LYS C CG  1 
ATOM   12711 C CD  . LYS C  1 529 ? -18.585  69.896  -36.967  1.00 86.77  ? 529 LYS C CD  1 
ATOM   12712 C CE  . LYS C  1 529 ? -19.006  68.528  -36.459  1.00 85.97  ? 529 LYS C CE  1 
ATOM   12713 N NZ  . LYS C  1 529 ? -20.461  68.339  -36.506  1.00 81.79  ? 529 LYS C NZ  1 
ATOM   12714 N N   . SER D  1 3   ? -56.506  -15.080 -38.471  1.00 70.10  ? 3   SER D N   1 
ATOM   12715 C CA  . SER D  1 3   ? -56.693  -13.667 -38.902  1.00 72.02  ? 3   SER D CA  1 
ATOM   12716 C C   . SER D  1 3   ? -56.087  -12.714 -37.862  1.00 66.10  ? 3   SER D C   1 
ATOM   12717 O O   . SER D  1 3   ? -55.890  -13.062 -36.697  1.00 67.14  ? 3   SER D O   1 
ATOM   12718 C CB  . SER D  1 3   ? -58.160  -13.375 -39.193  1.00 73.46  ? 3   SER D CB  1 
ATOM   12719 O OG  . SER D  1 3   ? -58.935  -13.377 -38.002  1.00 70.97  ? 3   SER D OG  1 
ATOM   12720 N N   . LYS D  1 4   ? -55.754  -11.500 -38.298  1.00 57.05  ? 4   LYS D N   1 
ATOM   12721 C CA  . LYS D  1 4   ? -54.922  -10.620 -37.505  1.00 53.30  ? 4   LYS D CA  1 
ATOM   12722 C C   . LYS D  1 4   ? -55.756  -9.863  -36.461  1.00 47.32  ? 4   LYS D C   1 
ATOM   12723 O O   . LYS D  1 4   ? -56.938  -9.620  -36.671  1.00 46.53  ? 4   LYS D O   1 
ATOM   12724 C CB  . LYS D  1 4   ? -54.177  -9.788  -38.553  1.00 56.74  ? 4   LYS D CB  1 
ATOM   12725 C CG  . LYS D  1 4   ? -54.984  -8.676  -39.177  1.00 59.72  ? 4   LYS D CG  1 
ATOM   12726 C CD  . LYS D  1 4   ? -54.426  -8.190  -40.506  1.00 62.93  ? 4   LYS D CD  1 
ATOM   12727 C CE  . LYS D  1 4   ? -54.885  -6.780  -40.784  1.00 68.40  ? 4   LYS D CE  1 
ATOM   12728 N NZ  . LYS D  1 4   ? -56.321  -6.628  -41.039  1.00 66.11  ? 4   LYS D NZ  1 
ATOM   12729 N N   . THR D  1 5   ? -55.126  -9.453  -35.344  1.00 42.79  ? 5   THR D N   1 
ATOM   12730 C CA  . THR D  1 5   ? -55.759  -8.651  -34.300  1.00 40.59  ? 5   THR D CA  1 
ATOM   12731 C C   . THR D  1 5   ? -56.655  -7.556  -34.887  1.00 41.21  ? 5   THR D C   1 
ATOM   12732 O O   . THR D  1 5   ? -56.250  -6.820  -35.764  1.00 40.23  ? 5   THR D O   1 
ATOM   12733 C CB  . THR D  1 5   ? -54.696  -7.997  -33.416  1.00 38.46  ? 5   THR D CB  1 
ATOM   12734 O OG1 . THR D  1 5   ? -53.704  -8.928  -33.007  1.00 36.78  ? 5   THR D OG1 1 
ATOM   12735 C CG2 . THR D  1 5   ? -55.279  -7.421  -32.140  1.00 36.77  ? 5   THR D CG2 1 
ATOM   12736 N N   . LYS D  1 6   ? -57.864  -7.422  -34.346  1.00 45.24  ? 6   LYS D N   1 
ATOM   12737 C CA  . LYS D  1 6   ? -58.769  -6.324  -34.646  1.00 48.33  ? 6   LYS D CA  1 
ATOM   12738 C C   . LYS D  1 6   ? -58.674  -5.277  -33.541  1.00 45.46  ? 6   LYS D C   1 
ATOM   12739 O O   . LYS D  1 6   ? -58.986  -5.554  -32.386  1.00 42.92  ? 6   LYS D O   1 
ATOM   12740 C CB  . LYS D  1 6   ? -60.206  -6.860  -34.725  1.00 57.54  ? 6   LYS D CB  1 
ATOM   12741 C CG  . LYS D  1 6   ? -61.357  -5.844  -34.920  1.00 67.32  ? 6   LYS D CG  1 
ATOM   12742 C CD  . LYS D  1 6   ? -62.729  -6.446  -35.257  1.00 77.30  ? 6   LYS D CD  1 
ATOM   12743 C CE  . LYS D  1 6   ? -63.448  -7.187  -34.148  1.00 88.37  ? 6   LYS D CE  1 
ATOM   12744 N NZ  . LYS D  1 6   ? -64.100  -6.246  -33.237  1.00 92.45  ? 6   LYS D NZ  1 
ATOM   12745 N N   . ILE D  1 7   ? -58.271  -4.057  -33.900  1.00 43.09  ? 7   ILE D N   1 
ATOM   12746 C CA  . ILE D  1 7   ? -58.214  -2.987  -32.920  1.00 40.17  ? 7   ILE D CA  1 
ATOM   12747 C C   . ILE D  1 7   ? -59.412  -2.075  -33.127  1.00 39.20  ? 7   ILE D C   1 
ATOM   12748 O O   . ILE D  1 7   ? -59.605  -1.558  -34.212  1.00 36.19  ? 7   ILE D O   1 
ATOM   12749 C CB  . ILE D  1 7   ? -56.913  -2.176  -33.011  1.00 38.47  ? 7   ILE D CB  1 
ATOM   12750 C CG1 . ILE D  1 7   ? -55.675  -3.047  -32.718  1.00 38.00  ? 7   ILE D CG1 1 
ATOM   12751 C CG2 . ILE D  1 7   ? -56.999  -0.989  -32.062  1.00 37.34  ? 7   ILE D CG2 1 
ATOM   12752 C CD1 . ILE D  1 7   ? -54.329  -2.391  -33.018  1.00 36.56  ? 7   ILE D CD1 1 
ATOM   12753 N N   . GLU D  1 8   ? -60.186  -1.882  -32.057  1.00 40.95  ? 8   GLU D N   1 
ATOM   12754 C CA  . GLU D  1 8   ? -61.311  -0.966  -32.069  1.00 42.83  ? 8   GLU D CA  1 
ATOM   12755 C C   . GLU D  1 8   ? -61.146  0.076   -30.962  1.00 38.81  ? 8   GLU D C   1 
ATOM   12756 O O   . GLU D  1 8   ? -60.799  -0.230  -29.816  1.00 33.73  ? 8   GLU D O   1 
ATOM   12757 C CB  . GLU D  1 8   ? -62.647  -1.700  -31.960  1.00 49.51  ? 8   GLU D CB  1 
ATOM   12758 C CG  . GLU D  1 8   ? -63.849  -0.847  -32.365  1.00 57.87  ? 8   GLU D CG  1 
ATOM   12759 C CD  . GLU D  1 8   ? -65.187  -1.591  -32.425  1.00 65.48  ? 8   GLU D CD  1 
ATOM   12760 O OE1 . GLU D  1 8   ? -65.225  -2.845  -32.305  1.00 64.58  ? 8   GLU D OE1 1 
ATOM   12761 O OE2 . GLU D  1 8   ? -66.204  -0.881  -32.609  1.00 66.08  ? 8   GLU D OE2 1 
ATOM   12762 N N   . LEU D  1 9   ? -61.449  1.321   -31.342  1.00 38.08  ? 9   LEU D N   1 
ATOM   12763 C CA  . LEU D  1 9   ? -61.415  2.434   -30.418  1.00 38.55  ? 9   LEU D CA  1 
ATOM   12764 C C   . LEU D  1 9   ? -62.846  2.873   -30.185  1.00 39.97  ? 9   LEU D C   1 
ATOM   12765 O O   . LEU D  1 9   ? -63.453  3.359   -31.130  1.00 41.03  ? 9   LEU D O   1 
ATOM   12766 C CB  . LEU D  1 9   ? -60.579  3.572   -31.003  1.00 35.92  ? 9   LEU D CB  1 
ATOM   12767 C CG  . LEU D  1 9   ? -59.138  3.227   -31.368  1.00 35.53  ? 9   LEU D CG  1 
ATOM   12768 C CD1 . LEU D  1 9   ? -58.492  4.549   -31.830  1.00 36.50  ? 9   LEU D CD1 1 
ATOM   12769 C CD2 . LEU D  1 9   ? -58.347  2.552   -30.236  1.00 34.24  ? 9   LEU D CD2 1 
ATOM   12770 N N   . LYS D  1 10  ? -63.358  2.680   -28.955  1.00 41.61  ? 10  LYS D N   1 
ATOM   12771 C CA  . LYS D  1 10  ? -64.643  3.246   -28.577  1.00 44.20  ? 10  LYS D CA  1 
ATOM   12772 C C   . LYS D  1 10  ? -64.750  3.288   -27.061  1.00 41.36  ? 10  LYS D C   1 
ATOM   12773 O O   . LYS D  1 10  ? -63.980  2.626   -26.361  1.00 36.56  ? 10  LYS D O   1 
ATOM   12774 C CB  . LYS D  1 10  ? -65.841  2.552   -29.248  1.00 54.86  ? 10  LYS D CB  1 
ATOM   12775 C CG  . LYS D  1 10  ? -66.405  1.241   -28.687  1.00 61.98  ? 10  LYS D CG  1 
ATOM   12776 C CD  . LYS D  1 10  ? -67.710  0.821   -29.381  1.00 67.95  ? 10  LYS D CD  1 
ATOM   12777 C CE  . LYS D  1 10  ? -68.551  -0.187  -28.607  1.00 74.79  ? 10  LYS D CE  1 
ATOM   12778 N NZ  . LYS D  1 10  ? -67.780  -1.367  -28.188  1.00 77.24  ? 10  LYS D NZ  1 
ATOM   12779 N N   . ASP D  1 11  ? -65.686  4.132   -26.587  1.00 38.68  ? 11  ASP D N   1 
ATOM   12780 C CA  . ASP D  1 11  ? -65.840  4.461   -25.176  1.00 36.55  ? 11  ASP D CA  1 
ATOM   12781 C C   . ASP D  1 11  ? -64.501  4.862   -24.563  1.00 34.25  ? 11  ASP D C   1 
ATOM   12782 O O   . ASP D  1 11  ? -64.288  4.635   -23.387  1.00 34.63  ? 11  ASP D O   1 
ATOM   12783 C CB  . ASP D  1 11  ? -66.463  3.317   -24.387  1.00 39.88  ? 11  ASP D CB  1 
ATOM   12784 C CG  . ASP D  1 11  ? -67.633  2.574   -25.032  1.00 42.92  ? 11  ASP D CG  1 
ATOM   12785 O OD1 . ASP D  1 11  ? -68.650  3.239   -25.380  1.00 41.13  ? 11  ASP D OD1 1 
ATOM   12786 O OD2 . ASP D  1 11  ? -67.527  1.317   -25.147  1.00 45.96  ? 11  ASP D OD2 1 
ATOM   12787 N N   . ASN D  1 12  ? -63.585  5.421   -25.362  1.00 35.43  ? 12  ASN D N   1 
ATOM   12788 C CA  . ASN D  1 12  ? -62.296  5.956   -24.899  1.00 35.36  ? 12  ASN D CA  1 
ATOM   12789 C C   . ASN D  1 12  ? -61.322  4.858   -24.423  1.00 33.08  ? 12  ASN D C   1 
ATOM   12790 O O   . ASN D  1 12  ? -60.394  5.116   -23.641  1.00 30.65  ? 12  ASN D O   1 
ATOM   12791 C CB  . ASN D  1 12  ? -62.514  7.095   -23.904  1.00 33.48  ? 12  ASN D CB  1 
ATOM   12792 C CG  . ASN D  1 12  ? -63.280  8.238   -24.524  1.00 36.12  ? 12  ASN D CG  1 
ATOM   12793 O OD1 . ASN D  1 12  ? -63.285  8.432   -25.746  1.00 38.74  ? 12  ASN D OD1 1 
ATOM   12794 N ND2 . ASN D  1 12  ? -63.868  9.077   -23.696  1.00 36.82  ? 12  ASN D ND2 1 
ATOM   12795 N N   . TRP D  1 13  ? -61.502  3.655   -24.976  1.00 31.99  ? 13  TRP D N   1 
ATOM   12796 C CA  . TRP D  1 13  ? -60.664  2.497   -24.723  1.00 31.75  ? 13  TRP D CA  1 
ATOM   12797 C C   . TRP D  1 13  ? -60.205  1.896   -26.046  1.00 32.64  ? 13  TRP D C   1 
ATOM   12798 O O   . TRP D  1 13  ? -60.977  1.821   -26.989  1.00 32.71  ? 13  TRP D O   1 
ATOM   12799 C CB  . TRP D  1 13  ? -61.431  1.412   -23.953  1.00 31.01  ? 13  TRP D CB  1 
ATOM   12800 C CG  . TRP D  1 13  ? -61.510  1.634   -22.471  1.00 31.33  ? 13  TRP D CG  1 
ATOM   12801 C CD1 . TRP D  1 13  ? -62.393  2.427   -21.802  1.00 31.94  ? 13  TRP D CD1 1 
ATOM   12802 C CD2 . TRP D  1 13  ? -60.667  1.044   -21.462  1.00 32.25  ? 13  TRP D CD2 1 
ATOM   12803 N NE1 . TRP D  1 13  ? -62.143  2.381   -20.458  1.00 31.23  ? 13  TRP D NE1 1 
ATOM   12804 C CE2 . TRP D  1 13  ? -61.091  1.552   -20.217  1.00 30.99  ? 13  TRP D CE2 1 
ATOM   12805 C CE3 . TRP D  1 13  ? -59.574  0.172   -21.492  1.00 33.03  ? 13  TRP D CE3 1 
ATOM   12806 C CZ2 . TRP D  1 13  ? -60.487  1.200   -19.018  1.00 31.93  ? 13  TRP D CZ2 1 
ATOM   12807 C CZ3 . TRP D  1 13  ? -58.972  -0.175  -20.300  1.00 32.68  ? 13  TRP D CZ3 1 
ATOM   12808 C CH2 . TRP D  1 13  ? -59.416  0.343   -19.083  1.00 32.01  ? 13  TRP D CH2 1 
ATOM   12809 N N   . TYR D  1 14  ? -58.954  1.430   -26.070  1.00 33.18  ? 14  TYR D N   1 
ATOM   12810 C CA  . TYR D  1 14  ? -58.516  0.440   -27.032  1.00 33.27  ? 14  TYR D CA  1 
ATOM   12811 C C   . TYR D  1 14  ? -59.183  -0.885  -26.697  1.00 33.03  ? 14  TYR D C   1 
ATOM   12812 O O   . TYR D  1 14  ? -59.287  -1.244  -25.539  1.00 32.96  ? 14  TYR D O   1 
ATOM   12813 C CB  . TYR D  1 14  ? -57.013  0.151   -26.983  1.00 32.97  ? 14  TYR D CB  1 
ATOM   12814 C CG  . TYR D  1 14  ? -56.078  1.201   -27.558  1.00 32.24  ? 14  TYR D CG  1 
ATOM   12815 C CD1 . TYR D  1 14  ? -55.972  2.465   -27.005  1.00 31.32  ? 14  TYR D CD1 1 
ATOM   12816 C CD2 . TYR D  1 14  ? -55.220  0.887   -28.595  1.00 33.70  ? 14  TYR D CD2 1 
ATOM   12817 C CE1 . TYR D  1 14  ? -55.045  3.375   -27.479  1.00 30.73  ? 14  TYR D CE1 1 
ATOM   12818 C CE2 . TYR D  1 14  ? -54.300  1.800   -29.089  1.00 32.79  ? 14  TYR D CE2 1 
ATOM   12819 C CZ  . TYR D  1 14  ? -54.221  3.060   -28.543  1.00 31.76  ? 14  TYR D CZ  1 
ATOM   12820 O OH  . TYR D  1 14  ? -53.301  3.963   -29.045  1.00 33.32  ? 14  TYR D OH  1 
ATOM   12821 N N   . HIS D  1 15  ? -59.644  -1.579  -27.734  1.00 34.37  ? 15  HIS D N   1 
ATOM   12822 C CA  . HIS D  1 15  ? -60.115  -2.946  -27.641  1.00 34.97  ? 15  HIS D CA  1 
ATOM   12823 C C   . HIS D  1 15  ? -59.249  -3.793  -28.569  1.00 34.32  ? 15  HIS D C   1 
ATOM   12824 O O   . HIS D  1 15  ? -59.012  -3.417  -29.719  1.00 33.04  ? 15  HIS D O   1 
ATOM   12825 C CB  . HIS D  1 15  ? -61.576  -3.051  -28.087  1.00 36.21  ? 15  HIS D CB  1 
ATOM   12826 C CG  . HIS D  1 15  ? -62.525  -2.223  -27.301  1.00 36.56  ? 15  HIS D CG  1 
ATOM   12827 N ND1 . HIS D  1 15  ? -62.512  -0.854  -27.341  1.00 36.90  ? 15  HIS D ND1 1 
ATOM   12828 C CD2 . HIS D  1 15  ? -63.529  -2.559  -26.473  1.00 37.57  ? 15  HIS D CD2 1 
ATOM   12829 C CE1 . HIS D  1 15  ? -63.474  -0.398  -26.543  1.00 36.51  ? 15  HIS D CE1 1 
ATOM   12830 N NE2 . HIS D  1 15  ? -64.093  -1.408  -26.002  1.00 35.50  ? 15  HIS D NE2 1 
ATOM   12831 N N   . LEU D  1 16  ? -58.734  -4.903  -28.042  1.00 34.97  ? 16  LEU D N   1 
ATOM   12832 C CA  . LEU D  1 16  ? -58.082  -5.909  -28.862  1.00 37.00  ? 16  LEU D CA  1 
ATOM   12833 C C   . LEU D  1 16  ? -59.005  -7.120  -28.961  1.00 36.75  ? 16  LEU D C   1 
ATOM   12834 O O   . LEU D  1 16  ? -59.321  -7.708  -27.939  1.00 35.02  ? 16  LEU D O   1 
ATOM   12835 C CB  . LEU D  1 16  ? -56.718  -6.276  -28.278  1.00 36.44  ? 16  LEU D CB  1 
ATOM   12836 C CG  . LEU D  1 16  ? -55.532  -5.495  -28.856  1.00 38.31  ? 16  LEU D CG  1 
ATOM   12837 C CD1 . LEU D  1 16  ? -55.789  -4.016  -28.809  1.00 36.36  ? 16  LEU D CD1 1 
ATOM   12838 C CD2 . LEU D  1 16  ? -54.206  -5.851  -28.168  1.00 37.54  ? 16  LEU D CD2 1 
ATOM   12839 N N   . ASP D  1 17  ? -59.440  -7.454  -30.184  1.00 39.31  ? 17  ASP D N   1 
ATOM   12840 C CA  . ASP D  1 17  ? -60.278  -8.624  -30.451  1.00 41.08  ? 17  ASP D CA  1 
ATOM   12841 C C   . ASP D  1 17  ? -61.517  -8.589  -29.563  1.00 42.85  ? 17  ASP D C   1 
ATOM   12842 O O   . ASP D  1 17  ? -61.894  -9.609  -29.010  1.00 40.32  ? 17  ASP D O   1 
ATOM   12843 C CB  . ASP D  1 17  ? -59.473  -9.913  -30.342  1.00 40.70  ? 17  ASP D CB  1 
ATOM   12844 C CG  . ASP D  1 17  ? -58.342  -10.006 -31.365  1.00 42.19  ? 17  ASP D CG  1 
ATOM   12845 O OD1 . ASP D  1 17  ? -58.545  -9.529  -32.489  1.00 43.06  ? 17  ASP D OD1 1 
ATOM   12846 O OD2 . ASP D  1 17  ? -57.248  -10.525 -31.050  1.00 42.93  ? 17  ASP D OD2 1 
ATOM   12847 N N   . GLY D  1 18  ? -62.096  -7.381  -29.400  1.00 46.13  ? 18  GLY D N   1 
ATOM   12848 C CA  . GLY D  1 18  ? -63.360  -7.167  -28.705  1.00 45.66  ? 18  GLY D CA  1 
ATOM   12849 C C   . GLY D  1 18  ? -63.232  -6.820  -27.216  1.00 45.39  ? 18  GLY D C   1 
ATOM   12850 O O   . GLY D  1 18  ? -64.212  -6.381  -26.623  1.00 44.20  ? 18  GLY D O   1 
ATOM   12851 N N   . GLU D  1 19  ? -62.063  -7.061  -26.600  1.00 45.18  ? 19  GLU D N   1 
ATOM   12852 C CA  . GLU D  1 19  ? -61.879  -6.873  -25.164  1.00 44.28  ? 19  GLU D CA  1 
ATOM   12853 C C   . GLU D  1 19  ? -61.134  -5.574  -24.855  1.00 40.04  ? 19  GLU D C   1 
ATOM   12854 O O   . GLU D  1 19  ? -60.119  -5.286  -25.477  1.00 40.50  ? 19  GLU D O   1 
ATOM   12855 C CB  . GLU D  1 19  ? -61.031  -8.016  -24.594  1.00 48.07  ? 19  GLU D CB  1 
ATOM   12856 C CG  . GLU D  1 19  ? -61.682  -9.394  -24.731  1.00 53.42  ? 19  GLU D CG  1 
ATOM   12857 C CD  . GLU D  1 19  ? -63.103  -9.386  -24.204  1.00 55.59  ? 19  GLU D CD  1 
ATOM   12858 O OE1 . GLU D  1 19  ? -63.304  -9.048  -23.019  1.00 59.24  ? 19  GLU D OE1 1 
ATOM   12859 O OE2 . GLU D  1 19  ? -64.021  -9.611  -25.013  1.00 66.00  ? 19  GLU D OE2 1 
ATOM   12860 N N   . LYS D  1 20  ? -61.584  -4.844  -23.835  1.00 36.86  ? 20  LYS D N   1 
ATOM   12861 C CA  . LYS D  1 20  ? -60.882  -3.663  -23.370  1.00 36.53  ? 20  LYS D CA  1 
ATOM   12862 C C   . LYS D  1 20  ? -59.460  -4.028  -22.952  1.00 36.00  ? 20  LYS D C   1 
ATOM   12863 O O   . LYS D  1 20  ? -59.247  -4.956  -22.184  1.00 36.81  ? 20  LYS D O   1 
ATOM   12864 C CB  . LYS D  1 20  ? -61.574  -2.940  -22.210  1.00 37.98  ? 20  LYS D CB  1 
ATOM   12865 C CG  . LYS D  1 20  ? -62.748  -2.092  -22.693  1.00 41.66  ? 20  LYS D CG  1 
ATOM   12866 C CD  . LYS D  1 20  ? -63.603  -1.361  -21.662  1.00 42.80  ? 20  LYS D CD  1 
ATOM   12867 C CE  . LYS D  1 20  ? -64.858  -0.840  -22.331  1.00 45.87  ? 20  LYS D CE  1 
ATOM   12868 N NZ  . LYS D  1 20  ? -65.881  -0.444  -21.369  1.00 47.49  ? 20  LYS D NZ  1 
ATOM   12869 N N   . TYR D  1 21  ? -58.488  -3.254  -23.439  1.00 32.94  ? 21  TYR D N   1 
ATOM   12870 C CA  . TYR D  1 21  ? -57.088  -3.559  -23.222  1.00 31.33  ? 21  TYR D CA  1 
ATOM   12871 C C   . TYR D  1 21  ? -56.379  -2.324  -22.676  1.00 31.09  ? 21  TYR D C   1 
ATOM   12872 O O   . TYR D  1 21  ? -56.180  -1.354  -23.404  1.00 30.02  ? 21  TYR D O   1 
ATOM   12873 C CB  . TYR D  1 21  ? -56.554  -3.954  -24.593  1.00 31.45  ? 21  TYR D CB  1 
ATOM   12874 C CG  . TYR D  1 21  ? -55.135  -4.480  -24.542  1.00 30.63  ? 21  TYR D CG  1 
ATOM   12875 C CD1 . TYR D  1 21  ? -54.903  -5.802  -24.207  1.00 30.64  ? 21  TYR D CD1 1 
ATOM   12876 C CD2 . TYR D  1 21  ? -54.048  -3.670  -24.860  1.00 28.51  ? 21  TYR D CD2 1 
ATOM   12877 C CE1 . TYR D  1 21  ? -53.606  -6.290  -24.140  1.00 31.60  ? 21  TYR D CE1 1 
ATOM   12878 C CE2 . TYR D  1 21  ? -52.754  -4.146  -24.795  1.00 28.71  ? 21  TYR D CE2 1 
ATOM   12879 C CZ  . TYR D  1 21  ? -52.534  -5.457  -24.417  1.00 30.22  ? 21  TYR D CZ  1 
ATOM   12880 O OH  . TYR D  1 21  ? -51.273  -5.975  -24.364  1.00 31.77  ? 21  TYR D OH  1 
ATOM   12881 N N   . PHE D  1 22  ? -56.046  -2.365  -21.391  1.00 29.67  ? 22  PHE D N   1 
ATOM   12882 C CA  . PHE D  1 22  ? -55.232  -1.334  -20.785  1.00 30.53  ? 22  PHE D CA  1 
ATOM   12883 C C   . PHE D  1 22  ? -53.780  -1.535  -21.238  1.00 30.31  ? 22  PHE D C   1 
ATOM   12884 O O   . PHE D  1 22  ? -53.197  -2.575  -20.962  1.00 30.76  ? 22  PHE D O   1 
ATOM   12885 C CB  . PHE D  1 22  ? -55.464  -1.381  -19.267  1.00 29.56  ? 22  PHE D CB  1 
ATOM   12886 C CG  . PHE D  1 22  ? -54.868  -0.156  -18.609  1.00 28.62  ? 22  PHE D CG  1 
ATOM   12887 C CD1 . PHE D  1 22  ? -53.498  0.027   -18.559  1.00 27.42  ? 22  PHE D CD1 1 
ATOM   12888 C CD2 . PHE D  1 22  ? -55.687  0.884   -18.201  1.00 30.41  ? 22  PHE D CD2 1 
ATOM   12889 C CE1 . PHE D  1 22  ? -52.973  1.183   -18.038  1.00 27.14  ? 22  PHE D CE1 1 
ATOM   12890 C CE2 . PHE D  1 22  ? -55.148  2.041   -17.664  1.00 27.37  ? 22  PHE D CE2 1 
ATOM   12891 C CZ  . PHE D  1 22  ? -53.799  2.175   -17.581  1.00 27.58  ? 22  PHE D CZ  1 
ATOM   12892 N N   . ILE D  1 23  ? -53.202  -0.560  -21.956  1.00 29.14  ? 23  ILE D N   1 
ATOM   12893 C CA  . ILE D  1 23  ? -51.843  -0.709  -22.444  1.00 29.01  ? 23  ILE D CA  1 
ATOM   12894 C C   . ILE D  1 23  ? -50.865  -0.434  -21.300  1.00 31.04  ? 23  ILE D C   1 
ATOM   12895 O O   . ILE D  1 23  ? -50.759  0.698   -20.804  1.00 32.74  ? 23  ILE D O   1 
ATOM   12896 C CB  . ILE D  1 23  ? -51.579  0.229   -23.629  1.00 29.54  ? 23  ILE D CB  1 
ATOM   12897 C CG1 . ILE D  1 23  ? -52.606  0.081   -24.714  1.00 29.79  ? 23  ILE D CG1 1 
ATOM   12898 C CG2 . ILE D  1 23  ? -50.182  0.015   -24.195  1.00 31.84  ? 23  ILE D CG2 1 
ATOM   12899 C CD1 . ILE D  1 23  ? -52.502  1.159   -25.768  1.00 28.91  ? 23  ILE D CD1 1 
ATOM   12900 N N   . LYS D  1 24  ? -50.103  -1.466  -20.930  1.00 29.94  ? 24  LYS D N   1 
ATOM   12901 C CA  . LYS D  1 24  ? -49.096  -1.362  -19.892  1.00 29.93  ? 24  LYS D CA  1 
ATOM   12902 C C   . LYS D  1 24  ? -47.714  -1.387  -20.531  1.00 29.15  ? 24  LYS D C   1 
ATOM   12903 O O   . LYS D  1 24  ? -47.043  -2.411  -20.511  1.00 31.87  ? 24  LYS D O   1 
ATOM   12904 C CB  . LYS D  1 24  ? -49.248  -2.509  -18.882  1.00 30.16  ? 24  LYS D CB  1 
ATOM   12905 C CG  . LYS D  1 24  ? -50.523  -2.482  -18.050  1.00 31.78  ? 24  LYS D CG  1 
ATOM   12906 C CD  . LYS D  1 24  ? -50.584  -3.472  -16.899  1.00 32.52  ? 24  LYS D CD  1 
ATOM   12907 C CE  . LYS D  1 24  ? -51.003  -4.832  -17.328  1.00 34.22  ? 24  LYS D CE  1 
ATOM   12908 N NZ  . LYS D  1 24  ? -50.710  -5.764  -16.231  1.00 33.93  ? 24  LYS D NZ  1 
ATOM   12909 N N   . ALA D  1 25  ? -47.303  -0.267  -21.116  1.00 29.88  ? 25  ALA D N   1 
ATOM   12910 C CA  . ALA D  1 25  ? -46.062  -0.193  -21.886  1.00 28.58  ? 25  ALA D CA  1 
ATOM   12911 C C   . ALA D  1 25  ? -44.904  0.255   -21.006  1.00 27.87  ? 25  ALA D C   1 
ATOM   12912 O O   . ALA D  1 25  ? -45.074  0.658   -19.856  1.00 30.43  ? 25  ALA D O   1 
ATOM   12913 C CB  . ALA D  1 25  ? -46.200  0.761   -23.060  1.00 26.92  ? 25  ALA D CB  1 
ATOM   12914 N N   . ILE D  1 26  ? -43.707  0.161   -21.569  1.00 26.63  ? 26  ILE D N   1 
ATOM   12915 C CA  . ILE D  1 26  ? -42.564  0.885   -21.046  1.00 25.48  ? 26  ILE D CA  1 
ATOM   12916 C C   . ILE D  1 26  ? -41.809  1.390   -22.258  1.00 25.12  ? 26  ILE D C   1 
ATOM   12917 O O   . ILE D  1 26  ? -41.760  0.713   -23.286  1.00 24.02  ? 26  ILE D O   1 
ATOM   12918 C CB  . ILE D  1 26  ? -41.693  0.026   -20.118  1.00 25.89  ? 26  ILE D CB  1 
ATOM   12919 C CG1 . ILE D  1 26  ? -40.584  0.833   -19.491  1.00 25.10  ? 26  ILE D CG1 1 
ATOM   12920 C CG2 . ILE D  1 26  ? -41.145  -1.212  -20.840  1.00 26.10  ? 26  ILE D CG2 1 
ATOM   12921 C CD1 . ILE D  1 26  ? -39.800  0.045   -18.460  1.00 25.25  ? 26  ILE D CD1 1 
ATOM   12922 N N   . GLY D  1 27  ? -41.334  2.632   -22.167  1.00 25.34  ? 27  GLY D N   1 
ATOM   12923 C CA  . GLY D  1 27  ? -40.437  3.156   -23.184  1.00 26.15  ? 27  GLY D CA  1 
ATOM   12924 C C   . GLY D  1 27  ? -39.205  2.255   -23.265  1.00 27.89  ? 27  GLY D C   1 
ATOM   12925 O O   . GLY D  1 27  ? -38.770  1.712   -22.261  1.00 29.74  ? 27  GLY D O   1 
ATOM   12926 N N   . TYR D  1 28  ? -38.688  2.049   -24.472  1.00 28.19  ? 28  TYR D N   1 
ATOM   12927 C CA  . TYR D  1 28  ? -37.651  1.065   -24.680  1.00 29.60  ? 28  TYR D CA  1 
ATOM   12928 C C   . TYR D  1 28  ? -36.848  1.468   -25.901  1.00 30.69  ? 28  TYR D C   1 
ATOM   12929 O O   . TYR D  1 28  ? -37.380  1.550   -26.996  1.00 32.49  ? 28  TYR D O   1 
ATOM   12930 C CB  . TYR D  1 28  ? -38.271  -0.317  -24.910  1.00 29.83  ? 28  TYR D CB  1 
ATOM   12931 C CG  . TYR D  1 28  ? -37.223  -1.319  -25.343  1.00 30.37  ? 28  TYR D CG  1 
ATOM   12932 C CD1 . TYR D  1 28  ? -36.100  -1.559  -24.558  1.00 29.87  ? 28  TYR D CD1 1 
ATOM   12933 C CD2 . TYR D  1 28  ? -37.321  -1.978  -26.558  1.00 31.45  ? 28  TYR D CD2 1 
ATOM   12934 C CE1 . TYR D  1 28  ? -35.122  -2.457  -24.956  1.00 28.71  ? 28  TYR D CE1 1 
ATOM   12935 C CE2 . TYR D  1 28  ? -36.355  -2.887  -26.961  1.00 31.11  ? 28  TYR D CE2 1 
ATOM   12936 C CZ  . TYR D  1 28  ? -35.244  -3.103  -26.166  1.00 29.27  ? 28  TYR D CZ  1 
ATOM   12937 O OH  . TYR D  1 28  ? -34.289  -3.973  -26.565  1.00 29.14  ? 28  TYR D OH  1 
ATOM   12938 N N   . GLU D  1 29  ? -35.544  1.653   -25.721  1.00 32.59  ? 29  GLU D N   1 
ATOM   12939 C CA  . GLU D  1 29  ? -34.724  2.111   -26.827  1.00 30.96  ? 29  GLU D CA  1 
ATOM   12940 C C   . GLU D  1 29  ? -33.511  1.208   -26.924  1.00 29.85  ? 29  GLU D C   1 
ATOM   12941 O O   . GLU D  1 29  ? -32.564  1.390   -26.184  1.00 31.65  ? 29  GLU D O   1 
ATOM   12942 C CB  . GLU D  1 29  ? -34.271  3.560   -26.607  1.00 30.58  ? 29  GLU D CB  1 
ATOM   12943 C CG  . GLU D  1 29  ? -33.274  4.064   -27.645  1.00 30.37  ? 29  GLU D CG  1 
ATOM   12944 C CD  . GLU D  1 29  ? -32.946  5.543   -27.505  1.00 30.88  ? 29  GLU D CD  1 
ATOM   12945 O OE1 . GLU D  1 29  ? -32.318  5.922   -26.475  1.00 28.17  ? 29  GLU D OE1 1 
ATOM   12946 O OE2 . GLU D  1 29  ? -33.338  6.282   -28.450  1.00 28.25  ? 29  GLU D OE2 1 
ATOM   12947 N N   . ILE D  1 30  ? -33.547  0.287   -27.877  1.00 30.25  ? 30  ILE D N   1 
ATOM   12948 C CA  . ILE D  1 30  ? -32.373  -0.480  -28.250  1.00 30.56  ? 30  ILE D CA  1 
ATOM   12949 C C   . ILE D  1 30  ? -31.341  0.432   -28.919  1.00 30.52  ? 30  ILE D C   1 
ATOM   12950 O O   . ILE D  1 30  ? -31.671  1.494   -29.426  1.00 30.94  ? 30  ILE D O   1 
ATOM   12951 C CB  . ILE D  1 30  ? -32.800  -1.635  -29.154  1.00 30.67  ? 30  ILE D CB  1 
ATOM   12952 C CG1 . ILE D  1 30  ? -31.677  -2.688  -29.316  1.00 33.02  ? 30  ILE D CG1 1 
ATOM   12953 C CG2 . ILE D  1 30  ? -33.319  -1.137  -30.500  1.00 30.36  ? 30  ILE D CG2 1 
ATOM   12954 C CD1 . ILE D  1 30  ? -31.264  -3.396  -28.033  1.00 32.18  ? 30  ILE D CD1 1 
ATOM   12955 N N   . GLY D  1 31  ? -30.078  0.025   -28.873  1.00 31.30  ? 31  GLY D N   1 
ATOM   12956 C CA  . GLY D  1 31  ? -29.003  0.744   -29.540  1.00 32.26  ? 31  GLY D CA  1 
ATOM   12957 C C   . GLY D  1 31  ? -28.459  1.896   -28.689  1.00 32.44  ? 31  GLY D C   1 
ATOM   12958 O O   . GLY D  1 31  ? -27.810  2.791   -29.236  1.00 33.15  ? 31  GLY D O   1 
ATOM   12959 N N   . ALA D  1 32  ? -28.696  1.831   -27.364  1.00 30.92  ? 32  ALA D N   1 
ATOM   12960 C CA  . ALA D  1 32  ? -28.377  2.916   -26.455  1.00 30.83  ? 32  ALA D CA  1 
ATOM   12961 C C   . ALA D  1 32  ? -27.598  2.428   -25.238  1.00 30.57  ? 32  ALA D C   1 
ATOM   12962 O O   . ALA D  1 32  ? -27.672  3.038   -24.167  1.00 30.27  ? 32  ALA D O   1 
ATOM   12963 C CB  . ALA D  1 32  ? -29.642  3.651   -26.034  1.00 30.10  ? 32  ALA D CB  1 
ATOM   12964 N N   . ARG D  1 33  ? -26.823  1.354   -25.410  1.00 32.27  ? 33  ARG D N   1 
ATOM   12965 C CA  . ARG D  1 33  ? -25.950  0.875   -24.349  1.00 32.66  ? 33  ARG D CA  1 
ATOM   12966 C C   . ARG D  1 33  ? -24.866  1.913   -24.084  1.00 34.55  ? 33  ARG D C   1 
ATOM   12967 O O   . ARG D  1 33  ? -24.616  2.786   -24.915  1.00 35.94  ? 33  ARG D O   1 
ATOM   12968 C CB  . ARG D  1 33  ? -25.231  -0.433  -24.721  1.00 33.70  ? 33  ARG D CB  1 
ATOM   12969 C CG  . ARG D  1 33  ? -25.894  -1.653  -24.099  1.00 34.00  ? 33  ARG D CG  1 
ATOM   12970 C CD  . ARG D  1 33  ? -27.426  -1.660  -24.378  1.00 31.97  ? 33  ARG D CD  1 
ATOM   12971 N NE  . ARG D  1 33  ? -27.920  -2.932  -23.846  1.00 32.50  ? 33  ARG D NE  1 
ATOM   12972 C CZ  . ARG D  1 33  ? -29.164  -3.390  -23.869  1.00 30.68  ? 33  ARG D CZ  1 
ATOM   12973 N NH1 . ARG D  1 33  ? -30.137  -2.648  -24.347  1.00 28.94  ? 33  ARG D NH1 1 
ATOM   12974 N NH2 . ARG D  1 33  ? -29.415  -4.589  -23.393  1.00 29.99  ? 33  ARG D NH2 1 
ATOM   12975 N N   . PRO D  1 34  ? -24.142  1.822   -22.947  1.00 34.31  ? 34  PRO D N   1 
ATOM   12976 C CA  . PRO D  1 34  ? -22.935  2.627   -22.759  1.00 37.31  ? 34  PRO D CA  1 
ATOM   12977 C C   . PRO D  1 34  ? -22.050  2.525   -24.000  1.00 40.69  ? 34  PRO D C   1 
ATOM   12978 O O   . PRO D  1 34  ? -21.773  1.426   -24.458  1.00 40.40  ? 34  PRO D O   1 
ATOM   12979 C CB  . PRO D  1 34  ? -22.307  1.993   -21.513  1.00 37.09  ? 34  PRO D CB  1 
ATOM   12980 C CG  . PRO D  1 34  ? -23.507  1.496   -20.734  1.00 34.96  ? 34  PRO D CG  1 
ATOM   12981 C CD  . PRO D  1 34  ? -24.474  1.001   -21.782  1.00 32.93  ? 34  PRO D CD  1 
ATOM   12982 N N   . GLY D  1 35  ? -21.645  3.674   -24.567  1.00 41.82  ? 35  GLY D N   1 
ATOM   12983 C CA  . GLY D  1 35  ? -20.783  3.653   -25.739  1.00 43.06  ? 35  GLY D CA  1 
ATOM   12984 C C   . GLY D  1 35  ? -21.549  3.657   -27.067  1.00 42.43  ? 35  GLY D C   1 
ATOM   12985 O O   . GLY D  1 35  ? -20.902  3.702   -28.107  1.00 45.30  ? 35  GLY D O   1 
ATOM   12986 N N   . GLN D  1 36  ? -22.895  3.620   -27.049  1.00 39.18  ? 36  GLN D N   1 
ATOM   12987 C CA  . GLN D  1 36  ? -23.674  3.590   -28.278  1.00 38.34  ? 36  GLN D CA  1 
ATOM   12988 C C   . GLN D  1 36  ? -24.464  4.883   -28.427  1.00 38.24  ? 36  GLN D C   1 
ATOM   12989 O O   . GLN D  1 36  ? -24.913  5.470   -27.439  1.00 40.32  ? 36  GLN D O   1 
ATOM   12990 C CB  . GLN D  1 36  ? -24.720  2.478   -28.378  1.00 38.04  ? 36  GLN D CB  1 
ATOM   12991 C CG  . GLN D  1 36  ? -24.162  1.070   -28.191  1.00 39.20  ? 36  GLN D CG  1 
ATOM   12992 C CD  . GLN D  1 36  ? -25.171  -0.027  -28.496  1.00 39.49  ? 36  GLN D CD  1 
ATOM   12993 O OE1 . GLN D  1 36  ? -26.243  -0.158  -27.884  1.00 35.71  ? 36  GLN D OE1 1 
ATOM   12994 N NE2 . GLN D  1 36  ? -24.803  -0.862  -29.455  1.00 40.72  ? 36  GLN D NE2 1 
ATOM   12995 N N   . ALA D  1 37  ? -24.736  5.244   -29.679  1.00 38.18  ? 37  ALA D N   1 
ATOM   12996 C CA  . ALA D  1 37  ? -25.635  6.355   -29.961  1.00 39.04  ? 37  ALA D CA  1 
ATOM   12997 C C   . ALA D  1 37  ? -26.584  5.974   -31.096  1.00 39.69  ? 37  ALA D C   1 
ATOM   12998 O O   . ALA D  1 37  ? -26.184  5.940   -32.261  1.00 41.83  ? 37  ALA D O   1 
ATOM   12999 C CB  . ALA D  1 37  ? -24.817  7.577   -30.321  1.00 38.84  ? 37  ALA D CB  1 
ATOM   13000 N N   . PRO D  1 38  ? -27.889  5.742   -30.836  1.00 38.38  ? 38  PRO D N   1 
ATOM   13001 C CA  . PRO D  1 38  ? -28.767  5.226   -31.896  1.00 40.71  ? 38  PRO D CA  1 
ATOM   13002 C C   . PRO D  1 38  ? -29.003  6.098   -33.142  1.00 42.90  ? 38  PRO D C   1 
ATOM   13003 O O   . PRO D  1 38  ? -29.449  5.586   -34.154  1.00 47.78  ? 38  PRO D O   1 
ATOM   13004 C CB  . PRO D  1 38  ? -30.071  4.953   -31.115  1.00 38.56  ? 38  PRO D CB  1 
ATOM   13005 C CG  . PRO D  1 38  ? -30.038  5.989   -30.009  1.00 37.23  ? 38  PRO D CG  1 
ATOM   13006 C CD  . PRO D  1 38  ? -28.580  5.981   -29.561  1.00 36.36  ? 38  PRO D CD  1 
ATOM   13007 N N   . TYR D  1 39  ? -28.764  7.403   -33.080  1.00 44.23  ? 39  TYR D N   1 
ATOM   13008 C CA  . TYR D  1 39  ? -29.142  8.266   -34.234  1.00 44.89  ? 39  TYR D CA  1 
ATOM   13009 C C   . TYR D  1 39  ? -27.905  8.664   -35.026  1.00 46.82  ? 39  TYR D C   1 
ATOM   13010 O O   . TYR D  1 39  ? -28.034  9.200   -36.135  1.00 44.89  ? 39  TYR D O   1 
ATOM   13011 C CB  . TYR D  1 39  ? -29.975  9.463   -33.757  1.00 43.25  ? 39  TYR D CB  1 
ATOM   13012 C CG  . TYR D  1 39  ? -31.336  9.133   -33.161  1.00 42.71  ? 39  TYR D CG  1 
ATOM   13013 C CD1 . TYR D  1 39  ? -32.390  8.716   -33.963  1.00 43.84  ? 39  TYR D CD1 1 
ATOM   13014 C CD2 . TYR D  1 39  ? -31.566  9.252   -31.799  1.00 42.71  ? 39  TYR D CD2 1 
ATOM   13015 C CE1 . TYR D  1 39  ? -33.629  8.415   -33.427  1.00 40.92  ? 39  TYR D CE1 1 
ATOM   13016 C CE2 . TYR D  1 39  ? -32.800  8.952   -31.251  1.00 41.78  ? 39  TYR D CE2 1 
ATOM   13017 C CZ  . TYR D  1 39  ? -33.834  8.535   -32.066  1.00 38.18  ? 39  TYR D CZ  1 
ATOM   13018 O OH  . TYR D  1 39  ? -35.050  8.245   -31.528  1.00 37.35  ? 39  TYR D OH  1 
ATOM   13019 N N   . GLU D  1 40  ? -26.731  8.377   -34.478  1.00 53.28  ? 40  GLU D N   1 
ATOM   13020 C CA  . GLU D  1 40  ? -25.468  8.684   -35.192  1.00 56.24  ? 40  GLU D CA  1 
ATOM   13021 C C   . GLU D  1 40  ? -24.806  7.362   -35.628  1.00 55.50  ? 40  GLU D C   1 
ATOM   13022 O O   . GLU D  1 40  ? -24.149  7.350   -36.676  1.00 54.44  ? 40  GLU D O   1 
ATOM   13023 C CB  . GLU D  1 40  ? -24.644  9.611   -34.294  1.00 58.55  ? 40  GLU D CB  1 
ATOM   13024 C CG  . GLU D  1 40  ? -23.414  8.964   -33.667  1.00 67.45  ? 40  GLU D CG  1 
ATOM   13025 C CD  . GLU D  1 40  ? -22.731  9.831   -32.624  1.00 74.32  ? 40  GLU D CD  1 
ATOM   13026 O OE1 . GLU D  1 40  ? -23.350  10.823  -32.187  1.00 73.31  ? 40  GLU D OE1 1 
ATOM   13027 O OE2 . GLU D  1 40  ? -21.584  9.517   -32.245  1.00 70.60  ? 40  GLU D OE2 1 
ATOM   13028 N N   . ASP D  1 41  ? -24.996  6.286   -34.872  1.00 51.31  ? 41  ASP D N   1 
ATOM   13029 C CA  . ASP D  1 41  ? -24.297  5.017   -35.201  1.00 51.89  ? 41  ASP D CA  1 
ATOM   13030 C C   . ASP D  1 41  ? -25.132  4.239   -36.214  1.00 53.11  ? 41  ASP D C   1 
ATOM   13031 O O   . ASP D  1 41  ? -26.358  4.371   -36.171  1.00 64.40  ? 41  ASP D O   1 
ATOM   13032 C CB  . ASP D  1 41  ? -24.001  4.196   -33.955  1.00 52.33  ? 41  ASP D CB  1 
ATOM   13033 C CG  . ASP D  1 41  ? -23.094  4.832   -32.916  1.00 49.64  ? 41  ASP D CG  1 
ATOM   13034 O OD1 . ASP D  1 41  ? -22.457  5.849   -33.239  1.00 48.06  ? 41  ASP D OD1 1 
ATOM   13035 O OD2 . ASP D  1 41  ? -23.037  4.296   -31.796  1.00 50.51  ? 41  ASP D OD2 1 
ATOM   13036 N N   . GLU D  1 42  ? -24.494  3.474   -37.096  1.00 57.08  ? 42  GLU D N   1 
ATOM   13037 C CA  . GLU D  1 42  ? -25.207  2.635   -38.059  1.00 63.43  ? 42  GLU D CA  1 
ATOM   13038 C C   . GLU D  1 42  ? -26.219  1.740   -37.325  1.00 65.60  ? 42  GLU D C   1 
ATOM   13039 O O   . GLU D  1 42  ? -25.918  1.207   -36.256  1.00 64.80  ? 42  GLU D O   1 
ATOM   13040 C CB  . GLU D  1 42  ? -24.247  1.830   -38.957  1.00 66.57  ? 42  GLU D CB  1 
ATOM   13041 C CG  . GLU D  1 42  ? -23.579  0.605   -38.318  1.00 67.85  ? 42  GLU D CG  1 
ATOM   13042 C CD  . GLU D  1 42  ? -22.609  0.883   -37.171  1.00 74.04  ? 42  GLU D CD  1 
ATOM   13043 O OE1 . GLU D  1 42  ? -22.186  2.062   -36.968  1.00 73.60  ? 42  GLU D OE1 1 
ATOM   13044 O OE2 . GLU D  1 42  ? -22.297  -0.092  -36.447  1.00 79.33  ? 42  GLU D OE2 1 
ATOM   13045 N N   . ARG D  1 43  ? -27.413  1.550   -37.912  1.00 68.07  ? 43  ARG D N   1 
ATOM   13046 C CA  . ARG D  1 43  ? -28.431  0.707   -37.292  1.00 75.04  ? 43  ARG D CA  1 
ATOM   13047 C C   . ARG D  1 43  ? -28.079  -0.779  -37.429  1.00 69.69  ? 43  ARG D C   1 
ATOM   13048 O O   . ARG D  1 43  ? -27.668  -1.278  -38.485  1.00 60.15  ? 43  ARG D O   1 
ATOM   13049 C CB  . ARG D  1 43  ? -29.888  0.960   -37.704  1.00 76.07  ? 43  ARG D CB  1 
ATOM   13050 C CG  . ARG D  1 43  ? -30.282  0.625   -39.133  1.00 79.05  ? 43  ARG D CG  1 
ATOM   13051 C CD  . ARG D  1 43  ? -31.559  1.400   -39.462  1.00 88.97  ? 43  ARG D CD  1 
ATOM   13052 N NE  . ARG D  1 43  ? -31.805  1.584   -40.900  1.00 96.88  ? 43  ARG D NE  1 
ATOM   13053 C CZ  . ARG D  1 43  ? -32.800  2.283   -41.468  1.00 92.48  ? 43  ARG D CZ  1 
ATOM   13054 N NH1 . ARG D  1 43  ? -33.688  2.966   -40.741  1.00 78.27  ? 43  ARG D NH1 1 
ATOM   13055 N NH2 . ARG D  1 43  ? -32.892  2.284   -42.790  1.00 94.19  ? 43  ARG D NH2 1 
ATOM   13056 N N   . LYS D  1 44  ? -28.260  -1.445  -36.284  1.00 65.11  ? 44  LYS D N   1 
ATOM   13057 C CA  . LYS D  1 44  ? -27.894  -2.821  -36.027  1.00 59.94  ? 44  LYS D CA  1 
ATOM   13058 C C   . LYS D  1 44  ? -29.111  -3.484  -35.398  1.00 53.12  ? 44  LYS D C   1 
ATOM   13059 O O   . LYS D  1 44  ? -29.803  -2.863  -34.598  1.00 50.52  ? 44  LYS D O   1 
ATOM   13060 C CB  . LYS D  1 44  ? -26.718  -2.808  -35.050  1.00 65.19  ? 44  LYS D CB  1 
ATOM   13061 C CG  . LYS D  1 44  ? -25.353  -2.478  -35.634  1.00 74.86  ? 44  LYS D CG  1 
ATOM   13062 C CD  . LYS D  1 44  ? -24.176  -2.861  -34.736  1.00 81.92  ? 44  LYS D CD  1 
ATOM   13063 C CE  . LYS D  1 44  ? -23.984  -4.352  -34.505  1.00 83.08  ? 44  LYS D CE  1 
ATOM   13064 N NZ  . LYS D  1 44  ? -23.416  -5.050  -35.662  1.00 82.93  ? 44  LYS D NZ  1 
ATOM   13065 N N   . ASP D  1 45  ? -29.409  -4.728  -35.774  1.00 48.38  ? 45  ASP D N   1 
ATOM   13066 C CA  . ASP D  1 45  ? -30.590  -5.381  -35.232  1.00 44.74  ? 45  ASP D CA  1 
ATOM   13067 C C   . ASP D  1 45  ? -30.459  -5.565  -33.713  1.00 42.54  ? 45  ASP D C   1 
ATOM   13068 O O   . ASP D  1 45  ? -31.437  -5.353  -32.979  1.00 39.25  ? 45  ASP D O   1 
ATOM   13069 C CB  . ASP D  1 45  ? -30.889  -6.643  -36.017  1.00 45.27  ? 45  ASP D CB  1 
ATOM   13070 C CG  . ASP D  1 45  ? -31.503  -6.422  -37.388  1.00 45.04  ? 45  ASP D CG  1 
ATOM   13071 O OD1 . ASP D  1 45  ? -31.997  -5.310  -37.629  1.00 42.84  ? 45  ASP D OD1 1 
ATOM   13072 O OD2 . ASP D  1 45  ? -31.480  -7.378  -38.191  1.00 48.37  ? 45  ASP D OD2 1 
ATOM   13073 N N   . GLU D  1 46  ? -29.244  -5.935  -33.251  1.00 40.57  ? 46  GLU D N   1 
ATOM   13074 C CA  . GLU D  1 46  ? -28.972  -6.155  -31.836  1.00 40.28  ? 46  GLU D CA  1 
ATOM   13075 C C   . GLU D  1 46  ? -29.922  -7.219  -31.282  1.00 37.91  ? 46  GLU D C   1 
ATOM   13076 O O   . GLU D  1 46  ? -30.489  -7.067  -30.201  1.00 39.24  ? 46  GLU D O   1 
ATOM   13077 C CB  . GLU D  1 46  ? -29.137  -4.833  -31.074  1.00 41.25  ? 46  GLU D CB  1 
ATOM   13078 C CG  . GLU D  1 46  ? -28.107  -3.781  -31.469  1.00 43.91  ? 46  GLU D CG  1 
ATOM   13079 C CD  . GLU D  1 46  ? -26.800  -3.965  -30.729  1.00 47.22  ? 46  GLU D CD  1 
ATOM   13080 O OE1 . GLU D  1 46  ? -26.260  -5.084  -30.628  1.00 56.29  ? 46  GLU D OE1 1 
ATOM   13081 O OE2 . GLU D  1 46  ? -26.328  -2.957  -30.223  1.00 52.31  ? 46  GLU D OE2 1 
ATOM   13082 N N   . LEU D  1 47  ? -30.139  -8.277  -32.048  1.00 37.21  ? 47  LEU D N   1 
ATOM   13083 C CA  . LEU D  1 47  ? -31.137  -9.256  -31.688  1.00 36.37  ? 47  LEU D CA  1 
ATOM   13084 C C   . LEU D  1 47  ? -30.801  -9.851  -30.324  1.00 36.68  ? 47  LEU D C   1 
ATOM   13085 O O   . LEU D  1 47  ? -31.684  -9.952  -29.481  1.00 37.21  ? 47  LEU D O   1 
ATOM   13086 C CB  . LEU D  1 47  ? -31.262  -10.314 -32.781  1.00 36.53  ? 47  LEU D CB  1 
ATOM   13087 C CG  . LEU D  1 47  ? -31.766  -9.797  -34.128  1.00 36.58  ? 47  LEU D CG  1 
ATOM   13088 C CD1 . LEU D  1 47  ? -31.867  -10.905 -35.162  1.00 37.17  ? 47  LEU D CD1 1 
ATOM   13089 C CD2 . LEU D  1 47  ? -33.123  -9.086  -33.965  1.00 35.32  ? 47  LEU D CD2 1 
ATOM   13090 N N   . GLU D  1 48  ? -29.545  -10.201 -30.062  1.00 38.77  ? 48  GLU D N   1 
ATOM   13091 C CA  . GLU D  1 48  ? -29.248  -10.923 -28.829  1.00 41.47  ? 48  GLU D CA  1 
ATOM   13092 C C   . GLU D  1 48  ? -29.641  -10.092 -27.604  1.00 38.33  ? 48  GLU D C   1 
ATOM   13093 O O   . GLU D  1 48  ? -30.184  -10.613 -26.634  1.00 37.60  ? 48  GLU D O   1 
ATOM   13094 C CB  . GLU D  1 48  ? -27.787  -11.382 -28.749  1.00 45.46  ? 48  GLU D CB  1 
ATOM   13095 C CG  . GLU D  1 48  ? -27.457  -12.546 -29.683  1.00 52.33  ? 48  GLU D CG  1 
ATOM   13096 C CD  . GLU D  1 48  ? -28.500  -13.672 -29.715  1.00 58.66  ? 48  GLU D CD  1 
ATOM   13097 O OE1 . GLU D  1 48  ? -28.808  -14.252 -28.625  1.00 56.74  ? 48  GLU D OE1 1 
ATOM   13098 O OE2 . GLU D  1 48  ? -29.037  -13.951 -30.833  1.00 57.63  ? 48  GLU D OE2 1 
ATOM   13099 N N   . LEU D  1 49  ? -29.321  -8.800  -27.623  1.00 38.12  ? 49  LEU D N   1 
ATOM   13100 C CA  . LEU D  1 49  ? -29.605  -7.931  -26.494  1.00 37.43  ? 49  LEU D CA  1 
ATOM   13101 C C   . LEU D  1 49  ? -31.107  -7.642  -26.406  1.00 37.96  ? 49  LEU D C   1 
ATOM   13102 O O   . LEU D  1 49  ? -31.601  -7.363  -25.316  1.00 38.16  ? 49  LEU D O   1 
ATOM   13103 C CB  . LEU D  1 49  ? -28.791  -6.647  -26.628  1.00 36.61  ? 49  LEU D CB  1 
ATOM   13104 C CG  . LEU D  1 49  ? -27.288  -6.763  -26.350  1.00 36.80  ? 49  LEU D CG  1 
ATOM   13105 C CD1 . LEU D  1 49  ? -26.635  -5.397  -26.617  1.00 35.95  ? 49  LEU D CD1 1 
ATOM   13106 C CD2 . LEU D  1 49  ? -26.997  -7.214  -24.936  1.00 34.80  ? 49  LEU D CD2 1 
ATOM   13107 N N   . MET D  1 50  ? -31.816  -7.656  -27.546  1.00 38.00  ? 50  MET D N   1 
ATOM   13108 C CA  . MET D  1 50  ? -33.263  -7.472  -27.562  1.00 37.78  ? 50  MET D CA  1 
ATOM   13109 C C   . MET D  1 50  ? -33.930  -8.674  -26.900  1.00 34.83  ? 50  MET D C   1 
ATOM   13110 O O   . MET D  1 50  ? -34.898  -8.531  -26.173  1.00 32.35  ? 50  MET D O   1 
ATOM   13111 C CB  . MET D  1 50  ? -33.822  -7.279  -28.986  1.00 38.81  ? 50  MET D CB  1 
ATOM   13112 C CG  . MET D  1 50  ? -33.672  -5.858  -29.531  1.00 39.75  ? 50  MET D CG  1 
ATOM   13113 S SD  . MET D  1 50  ? -34.610  -5.532  -31.041  1.00 39.46  ? 50  MET D SD  1 
ATOM   13114 C CE  . MET D  1 50  ? -36.292  -5.601  -30.398  1.00 35.28  ? 50  MET D CE  1 
ATOM   13115 N N   . LYS D  1 51  ? -33.399  -9.868  -27.143  1.00 35.63  ? 51  LYS D N   1 
ATOM   13116 C CA  . LYS D  1 51  ? -33.961  -11.050 -26.513  1.00 36.69  ? 51  LYS D CA  1 
ATOM   13117 C C   . LYS D  1 51  ? -33.923  -10.840 -25.015  1.00 34.89  ? 51  LYS D C   1 
ATOM   13118 O O   . LYS D  1 51  ? -34.959  -11.002 -24.367  1.00 35.21  ? 51  LYS D O   1 
ATOM   13119 C CB  . LYS D  1 51  ? -33.227  -12.338 -26.867  1.00 40.32  ? 51  LYS D CB  1 
ATOM   13120 C CG  . LYS D  1 51  ? -33.500  -12.745 -28.297  1.00 46.59  ? 51  LYS D CG  1 
ATOM   13121 C CD  . LYS D  1 51  ? -32.707  -13.934 -28.835  1.00 52.48  ? 51  LYS D CD  1 
ATOM   13122 C CE  . LYS D  1 51  ? -32.999  -14.217 -30.294  1.00 54.89  ? 51  LYS D CE  1 
ATOM   13123 N NZ  . LYS D  1 51  ? -31.985  -15.102 -30.883  1.00 56.13  ? 51  LYS D NZ  1 
ATOM   13124 N N   . PHE D  1 52  ? -32.739  -10.425 -24.519  1.00 32.80  ? 52  PHE D N   1 
ATOM   13125 C CA  . PHE D  1 52  ? -32.518  -10.187 -23.102  1.00 32.60  ? 52  PHE D CA  1 
ATOM   13126 C C   . PHE D  1 52  ? -33.471  -9.114  -22.580  1.00 31.74  ? 52  PHE D C   1 
ATOM   13127 O O   . PHE D  1 52  ? -34.133  -9.325  -21.552  1.00 33.03  ? 52  PHE D O   1 
ATOM   13128 C CB  . PHE D  1 52  ? -31.038  -9.887  -22.849  1.00 33.77  ? 52  PHE D CB  1 
ATOM   13129 C CG  . PHE D  1 52  ? -30.721  -9.352  -21.461  1.00 33.61  ? 52  PHE D CG  1 
ATOM   13130 C CD1 . PHE D  1 52  ? -30.481  -10.212 -20.402  1.00 33.50  ? 52  PHE D CD1 1 
ATOM   13131 C CD2 . PHE D  1 52  ? -30.641  -7.977  -21.235  1.00 34.52  ? 52  PHE D CD2 1 
ATOM   13132 C CE1 . PHE D  1 52  ? -30.205  -9.715  -19.136  1.00 34.43  ? 52  PHE D CE1 1 
ATOM   13133 C CE2 . PHE D  1 52  ? -30.350  -7.477  -19.970  1.00 33.88  ? 52  PHE D CE2 1 
ATOM   13134 C CZ  . PHE D  1 52  ? -30.135  -8.349  -18.923  1.00 35.03  ? 52  PHE D CZ  1 
ATOM   13135 N N   . ASP D  1 53  ? -33.597  -8.001  -23.314  1.00 31.12  ? 53  ASP D N   1 
ATOM   13136 C CA  . ASP D  1 53  ? -34.407  -6.869  -22.863  1.00 30.74  ? 53  ASP D CA  1 
ATOM   13137 C C   . ASP D  1 53  ? -35.897  -7.234  -22.844  1.00 30.89  ? 53  ASP D C   1 
ATOM   13138 O O   . ASP D  1 53  ? -36.617  -6.907  -21.908  1.00 31.33  ? 53  ASP D O   1 
ATOM   13139 C CB  . ASP D  1 53  ? -34.195  -5.625  -23.723  1.00 30.13  ? 53  ASP D CB  1 
ATOM   13140 C CG  . ASP D  1 53  ? -32.806  -4.992  -23.706  1.00 30.74  ? 53  ASP D CG  1 
ATOM   13141 O OD1 . ASP D  1 53  ? -32.033  -5.162  -22.712  1.00 30.32  ? 53  ASP D OD1 1 
ATOM   13142 O OD2 . ASP D  1 53  ? -32.476  -4.375  -24.718  1.00 31.15  ? 53  ASP D OD2 1 
ATOM   13143 N N   . LEU D  1 54  ? -36.385  -7.888  -23.896  1.00 32.32  ? 54  LEU D N   1 
ATOM   13144 C CA  . LEU D  1 54  ? -37.788  -8.265  -23.950  1.00 33.90  ? 54  LEU D CA  1 
ATOM   13145 C C   . LEU D  1 54  ? -38.142  -9.270  -22.844  1.00 34.48  ? 54  LEU D C   1 
ATOM   13146 O O   . LEU D  1 54  ? -39.229  -9.201  -22.273  1.00 33.84  ? 54  LEU D O   1 
ATOM   13147 C CB  . LEU D  1 54  ? -38.078  -8.797  -25.351  1.00 35.33  ? 54  LEU D CB  1 
ATOM   13148 C CG  . LEU D  1 54  ? -38.024  -7.779  -26.492  1.00 36.30  ? 54  LEU D CG  1 
ATOM   13149 C CD1 . LEU D  1 54  ? -38.418  -8.432  -27.786  1.00 36.93  ? 54  LEU D CD1 1 
ATOM   13150 C CD2 . LEU D  1 54  ? -38.927  -6.563  -26.242  1.00 37.47  ? 54  LEU D CD2 1 
ATOM   13151 N N   . GLU D  1 55  ? -37.225  -10.181 -22.507  1.00 34.37  ? 55  GLU D N   1 
ATOM   13152 C CA  . GLU D  1 55  ? -37.514  -11.139 -21.449  1.00 34.88  ? 55  GLU D CA  1 
ATOM   13153 C C   . GLU D  1 55  ? -37.698  -10.368 -20.139  1.00 34.35  ? 55  GLU D C   1 
ATOM   13154 O O   . GLU D  1 55  ? -38.659  -10.610 -19.398  1.00 32.02  ? 55  GLU D O   1 
ATOM   13155 C CB  . GLU D  1 55  ? -36.445  -12.228 -21.396  1.00 35.05  ? 55  GLU D CB  1 
ATOM   13156 C CG  . GLU D  1 55  ? -36.736  -13.374 -20.428  1.00 37.88  ? 55  GLU D CG  1 
ATOM   13157 C CD  . GLU D  1 55  ? -38.183  -13.893 -20.318  1.00 38.95  ? 55  GLU D CD  1 
ATOM   13158 O OE1 . GLU D  1 55  ? -38.907  -14.012 -21.362  1.00 39.81  ? 55  GLU D OE1 1 
ATOM   13159 O OE2 . GLU D  1 55  ? -38.576  -14.171 -19.146  1.00 34.40  ? 55  GLU D OE2 1 
ATOM   13160 N N   . ASN D  1 56  ? -36.818  -9.377  -19.889  1.00 32.45  ? 56  ASN D N   1 
ATOM   13161 C CA  . ASN D  1 56  ? -36.889  -8.622  -18.646  1.00 29.03  ? 56  ASN D CA  1 
ATOM   13162 C C   . ASN D  1 56  ? -38.208  -7.845  -18.545  1.00 28.10  ? 56  ASN D C   1 
ATOM   13163 O O   . ASN D  1 56  ? -38.802  -7.773  -17.470  1.00 26.04  ? 56  ASN D O   1 
ATOM   13164 C CB  . ASN D  1 56  ? -35.716  -7.671  -18.540  1.00 28.91  ? 56  ASN D CB  1 
ATOM   13165 C CG  . ASN D  1 56  ? -34.404  -8.384  -18.367  1.00 30.76  ? 56  ASN D CG  1 
ATOM   13166 O OD1 . ASN D  1 56  ? -34.360  -9.467  -17.779  1.00 30.30  ? 56  ASN D OD1 1 
ATOM   13167 N ND2 . ASN D  1 56  ? -33.322  -7.745  -18.796  1.00 31.33  ? 56  ASN D ND2 1 
ATOM   13168 N N   . ILE D  1 57  ? -38.596  -7.198  -19.658  1.00 28.10  ? 57  ILE D N   1 
ATOM   13169 C CA  . ILE D  1 57  ? -39.762  -6.348  -19.744  1.00 28.74  ? 57  ILE D CA  1 
ATOM   13170 C C   . ILE D  1 57  ? -41.007  -7.185  -19.468  1.00 30.01  ? 57  ILE D C   1 
ATOM   13171 O O   . ILE D  1 57  ? -41.837  -6.819  -18.637  1.00 30.98  ? 57  ILE D O   1 
ATOM   13172 C CB  . ILE D  1 57  ? -39.750  -5.598  -21.092  1.00 30.01  ? 57  ILE D CB  1 
ATOM   13173 C CG1 . ILE D  1 57  ? -38.648  -4.522  -21.093  1.00 31.97  ? 57  ILE D CG1 1 
ATOM   13174 C CG2 . ILE D  1 57  ? -41.087  -4.949  -21.416  1.00 28.51  ? 57  ILE D CG2 1 
ATOM   13175 C CD1 . ILE D  1 57  ? -38.499  -3.785  -22.411  1.00 33.39  ? 57  ILE D CD1 1 
ATOM   13176 N N   . LYS D  1 58  ? -41.107  -8.359  -20.074  1.00 30.40  ? 58  LYS D N   1 
ATOM   13177 C CA  . LYS D  1 58  ? -42.180  -9.271  -19.708  1.00 31.04  ? 58  LYS D CA  1 
ATOM   13178 C C   . LYS D  1 58  ? -42.173  -9.551  -18.208  1.00 30.45  ? 58  LYS D C   1 
ATOM   13179 O O   . LYS D  1 58  ? -43.209  -9.493  -17.543  1.00 27.30  ? 58  LYS D O   1 
ATOM   13180 C CB  . LYS D  1 58  ? -42.060  -10.556 -20.527  1.00 30.93  ? 58  LYS D CB  1 
ATOM   13181 C CG  . LYS D  1 58  ? -42.500  -10.350 -21.956  1.00 32.82  ? 58  LYS D CG  1 
ATOM   13182 C CD  . LYS D  1 58  ? -41.923  -11.373 -22.925  1.00 36.38  ? 58  LYS D CD  1 
ATOM   13183 C CE  . LYS D  1 58  ? -42.451  -12.742 -22.715  1.00 39.53  ? 58  LYS D CE  1 
ATOM   13184 N NZ  . LYS D  1 58  ? -41.798  -13.672 -23.637  1.00 41.27  ? 58  LYS D NZ  1 
ATOM   13185 N N   . GLU D  1 59  ? -40.998  -9.912  -17.690  1.00 32.97  ? 59  GLU D N   1 
ATOM   13186 C CA  . GLU D  1 59  ? -40.880  -10.300 -16.290  1.00 33.29  ? 59  GLU D CA  1 
ATOM   13187 C C   . GLU D  1 59  ? -41.245  -9.110  -15.416  1.00 31.07  ? 59  GLU D C   1 
ATOM   13188 O O   . GLU D  1 59  ? -41.616  -9.280  -14.270  1.00 32.48  ? 59  GLU D O   1 
ATOM   13189 C CB  . GLU D  1 59  ? -39.480  -10.803 -15.925  1.00 34.10  ? 59  GLU D CB  1 
ATOM   13190 C CG  . GLU D  1 59  ? -39.242  -12.272 -16.266  1.00 39.41  ? 59  GLU D CG  1 
ATOM   13191 C CD  . GLU D  1 59  ? -37.775  -12.707 -16.160  1.00 44.46  ? 59  GLU D CD  1 
ATOM   13192 O OE1 . GLU D  1 59  ? -36.943  -11.990 -15.528  1.00 44.57  ? 59  GLU D OE1 1 
ATOM   13193 O OE2 . GLU D  1 59  ? -37.449  -13.742 -16.803  1.00 45.88  ? 59  GLU D OE2 1 
ATOM   13194 N N   . GLY D  1 60  ? -41.071  -7.896  -15.949  1.00 30.26  ? 60  GLY D N   1 
ATOM   13195 C CA  . GLY D  1 60  ? -41.341  -6.685  -15.194  1.00 28.26  ? 60  GLY D CA  1 
ATOM   13196 C C   . GLY D  1 60  ? -42.813  -6.292  -15.185  1.00 26.36  ? 60  GLY D C   1 
ATOM   13197 O O   . GLY D  1 60  ? -43.105  -5.276  -14.577  1.00 24.98  ? 60  GLY D O   1 
ATOM   13198 N N   . GLY D  1 61  ? -43.672  -7.064  -15.886  1.00 27.39  ? 61  GLY D N   1 
ATOM   13199 C CA  . GLY D  1 61  ? -45.136  -7.043  -15.811  1.00 28.03  ? 61  GLY D CA  1 
ATOM   13200 C C   . GLY D  1 61  ? -45.832  -6.269  -16.955  1.00 29.93  ? 61  GLY D C   1 
ATOM   13201 O O   . GLY D  1 61  ? -47.058  -6.108  -16.914  1.00 30.63  ? 61  GLY D O   1 
ATOM   13202 N N   . TYR D  1 62  ? -45.049  -5.775  -17.952  1.00 29.22  ? 62  TYR D N   1 
ATOM   13203 C CA  . TYR D  1 62  ? -45.515  -4.947  -19.051  1.00 27.63  ? 62  TYR D CA  1 
ATOM   13204 C C   . TYR D  1 62  ? -46.086  -5.810  -20.179  1.00 28.95  ? 62  TYR D C   1 
ATOM   13205 O O   . TYR D  1 62  ? -45.770  -6.984  -20.310  1.00 27.36  ? 62  TYR D O   1 
ATOM   13206 C CB  . TYR D  1 62  ? -44.337  -4.090  -19.540  1.00 27.97  ? 62  TYR D CB  1 
ATOM   13207 C CG  . TYR D  1 62  ? -43.681  -3.235  -18.458  1.00 26.42  ? 62  TYR D CG  1 
ATOM   13208 C CD1 . TYR D  1 62  ? -44.190  -1.997  -18.096  1.00 24.91  ? 62  TYR D CD1 1 
ATOM   13209 C CD2 . TYR D  1 62  ? -42.569  -3.695  -17.777  1.00 26.20  ? 62  TYR D CD2 1 
ATOM   13210 C CE1 . TYR D  1 62  ? -43.619  -1.253  -17.079  1.00 24.20  ? 62  TYR D CE1 1 
ATOM   13211 C CE2 . TYR D  1 62  ? -41.951  -2.940  -16.800  1.00 27.06  ? 62  TYR D CE2 1 
ATOM   13212 C CZ  . TYR D  1 62  ? -42.493  -1.718  -16.432  1.00 25.98  ? 62  TYR D CZ  1 
ATOM   13213 O OH  . TYR D  1 62  ? -41.911  -1.043  -15.390  1.00 25.34  ? 62  TYR D OH  1 
ATOM   13214 N N   . ASN D  1 63  ? -46.981  -5.219  -20.985  1.00 29.94  ? 63  ASN D N   1 
ATOM   13215 C CA  . ASN D  1 63  ? -47.590  -5.932  -22.088  1.00 29.63  ? 63  ASN D CA  1 
ATOM   13216 C C   . ASN D  1 63  ? -47.200  -5.261  -23.394  1.00 28.90  ? 63  ASN D C   1 
ATOM   13217 O O   . ASN D  1 63  ? -47.410  -5.848  -24.446  1.00 29.94  ? 63  ASN D O   1 
ATOM   13218 C CB  . ASN D  1 63  ? -49.097  -6.107  -21.913  1.00 31.34  ? 63  ASN D CB  1 
ATOM   13219 C CG  . ASN D  1 63  ? -49.854  -4.800  -21.900  1.00 32.11  ? 63  ASN D CG  1 
ATOM   13220 O OD1 . ASN D  1 63  ? -49.370  -3.801  -22.418  1.00 32.35  ? 63  ASN D OD1 1 
ATOM   13221 N ND2 . ASN D  1 63  ? -51.068  -4.789  -21.376  1.00 34.02  ? 63  ASN D ND2 1 
ATOM   13222 N N   . THR D  1 64  ? -46.520  -4.109  -23.320  1.00 28.67  ? 64  THR D N   1 
ATOM   13223 C CA  . THR D  1 64  ? -46.209  -3.316  -24.502  1.00 28.22  ? 64  THR D CA  1 
ATOM   13224 C C   . THR D  1 64  ? -44.842  -2.641  -24.342  1.00 28.04  ? 64  THR D C   1 
ATOM   13225 O O   . THR D  1 64  ? -44.458  -2.297  -23.217  1.00 26.57  ? 64  THR D O   1 
ATOM   13226 C CB  . THR D  1 64  ? -47.328  -2.292  -24.684  1.00 26.95  ? 64  THR D CB  1 
ATOM   13227 O OG1 . THR D  1 64  ? -48.574  -2.959  -24.834  1.00 28.03  ? 64  THR D OG1 1 
ATOM   13228 C CG2 . THR D  1 64  ? -47.169  -1.452  -25.930  1.00 27.73  ? 64  THR D CG2 1 
ATOM   13229 N N   . ILE D  1 65  ? -44.142  -2.423  -25.476  1.00 27.58  ? 65  ILE D N   1 
ATOM   13230 C CA  . ILE D  1 65  ? -42.977  -1.540  -25.509  1.00 27.40  ? 65  ILE D CA  1 
ATOM   13231 C C   . ILE D  1 65  ? -43.300  -0.349  -26.396  1.00 26.95  ? 65  ILE D C   1 
ATOM   13232 O O   . ILE D  1 65  ? -44.007  -0.511  -27.373  1.00 28.76  ? 65  ILE D O   1 
ATOM   13233 C CB  . ILE D  1 65  ? -41.716  -2.262  -26.009  1.00 26.89  ? 65  ILE D CB  1 
ATOM   13234 C CG1 . ILE D  1 65  ? -41.969  -3.035  -27.270  1.00 27.71  ? 65  ILE D CG1 1 
ATOM   13235 C CG2 . ILE D  1 65  ? -41.117  -3.152  -24.933  1.00 26.89  ? 65  ILE D CG2 1 
ATOM   13236 C CD1 . ILE D  1 65  ? -40.685  -3.464  -27.945  1.00 28.44  ? 65  ILE D CD1 1 
ATOM   13237 N N   . ARG D  1 66  ? -42.816  0.835   -26.012  1.00 27.91  ? 66  ARG D N   1 
ATOM   13238 C CA  . ARG D  1 66  ? -42.954  2.090   -26.756  1.00 26.62  ? 66  ARG D CA  1 
ATOM   13239 C C   . ARG D  1 66  ? -41.577  2.590   -27.231  1.00 26.52  ? 66  ARG D C   1 
ATOM   13240 O O   . ARG D  1 66  ? -40.655  2.734   -26.427  1.00 24.37  ? 66  ARG D O   1 
ATOM   13241 C CB  . ARG D  1 66  ? -43.625  3.120   -25.841  1.00 27.07  ? 66  ARG D CB  1 
ATOM   13242 C CG  . ARG D  1 66  ? -43.738  4.581   -26.290  1.00 27.79  ? 66  ARG D CG  1 
ATOM   13243 C CD  . ARG D  1 66  ? -42.436  5.381   -26.187  1.00 29.79  ? 66  ARG D CD  1 
ATOM   13244 N NE  . ARG D  1 66  ? -42.669  6.831   -26.200  1.00 31.08  ? 66  ARG D NE  1 
ATOM   13245 C CZ  . ARG D  1 66  ? -42.536  7.619   -27.243  1.00 30.71  ? 66  ARG D CZ  1 
ATOM   13246 N NH1 . ARG D  1 66  ? -42.096  7.148   -28.400  1.00 31.15  ? 66  ARG D NH1 1 
ATOM   13247 N NH2 . ARG D  1 66  ? -42.820  8.892   -27.097  1.00 32.42  ? 66  ARG D NH2 1 
ATOM   13248 N N   . THR D  1 67  ? -41.457  2.895   -28.543  1.00 28.41  ? 67  THR D N   1 
ATOM   13249 C CA  . THR D  1 67  ? -40.184  3.243   -29.166  1.00 31.07  ? 67  THR D CA  1 
ATOM   13250 C C   . THR D  1 67  ? -40.258  4.589   -29.880  1.00 32.40  ? 67  THR D C   1 
ATOM   13251 O O   . THR D  1 67  ? -41.327  5.187   -30.032  1.00 31.48  ? 67  THR D O   1 
ATOM   13252 C CB  . THR D  1 67  ? -39.724  2.149   -30.133  1.00 32.40  ? 67  THR D CB  1 
ATOM   13253 O OG1 . THR D  1 67  ? -40.505  2.185   -31.327  1.00 30.84  ? 67  THR D OG1 1 
ATOM   13254 C CG2 . THR D  1 67  ? -39.738  0.782   -29.469  1.00 32.97  ? 67  THR D CG2 1 
ATOM   13255 N N   . TRP D  1 68  ? -39.073  5.070   -30.274  1.00 31.32  ? 68  TRP D N   1 
ATOM   13256 C CA  . TRP D  1 68  ? -38.940  6.395   -30.870  1.00 32.04  ? 68  TRP D CA  1 
ATOM   13257 C C   . TRP D  1 68  ? -38.561  6.259   -32.342  1.00 30.75  ? 68  TRP D C   1 
ATOM   13258 O O   . TRP D  1 68  ? -38.825  7.129   -33.152  1.00 32.75  ? 68  TRP D O   1 
ATOM   13259 C CB  . TRP D  1 68  ? -37.911  7.237   -30.076  1.00 30.68  ? 68  TRP D CB  1 
ATOM   13260 C CG  . TRP D  1 68  ? -38.453  7.711   -28.757  1.00 28.29  ? 68  TRP D CG  1 
ATOM   13261 C CD1 . TRP D  1 68  ? -39.042  8.914   -28.507  1.00 30.03  ? 68  TRP D CD1 1 
ATOM   13262 C CD2 . TRP D  1 68  ? -38.561  6.964   -27.532  1.00 28.64  ? 68  TRP D CD2 1 
ATOM   13263 N NE1 . TRP D  1 68  ? -39.500  8.976   -27.219  1.00 29.45  ? 68  TRP D NE1 1 
ATOM   13264 C CE2 . TRP D  1 68  ? -39.222  7.786   -26.597  1.00 28.52  ? 68  TRP D CE2 1 
ATOM   13265 C CE3 . TRP D  1 68  ? -38.174  5.682   -27.133  1.00 30.03  ? 68  TRP D CE3 1 
ATOM   13266 C CZ2 . TRP D  1 68  ? -39.503  7.364   -25.301  1.00 26.49  ? 68  TRP D CZ2 1 
ATOM   13267 C CZ3 . TRP D  1 68  ? -38.432  5.277   -25.842  1.00 28.01  ? 68  TRP D CZ3 1 
ATOM   13268 C CH2 . TRP D  1 68  ? -39.081  6.109   -24.942  1.00 27.70  ? 68  TRP D CH2 1 
ATOM   13269 N N   . SER D  1 69  ? -37.942  5.144   -32.686  1.00 31.22  ? 69  SER D N   1 
ATOM   13270 C CA  . SER D  1 69  ? -37.377  4.956   -34.008  1.00 30.55  ? 69  SER D CA  1 
ATOM   13271 C C   . SER D  1 69  ? -37.809  3.592   -34.545  1.00 29.92  ? 69  SER D C   1 
ATOM   13272 O O   . SER D  1 69  ? -37.877  2.627   -33.783  1.00 29.14  ? 69  SER D O   1 
ATOM   13273 C CB  . SER D  1 69  ? -35.893  5.076   -33.958  1.00 30.09  ? 69  SER D CB  1 
ATOM   13274 O OG  . SER D  1 69  ? -35.445  5.467   -35.237  1.00 33.64  ? 69  SER D OG  1 
ATOM   13275 N N   . GLN D  1 70  ? -38.030  3.536   -35.863  1.00 29.48  ? 70  GLN D N   1 
ATOM   13276 C CA  . GLN D  1 70  ? -38.586  2.369   -36.505  1.00 30.95  ? 70  GLN D CA  1 
ATOM   13277 C C   . GLN D  1 70  ? -37.622  1.189   -36.423  1.00 32.98  ? 70  GLN D C   1 
ATOM   13278 O O   . GLN D  1 70  ? -36.420  1.339   -36.590  1.00 34.14  ? 70  GLN D O   1 
ATOM   13279 C CB  . GLN D  1 70  ? -38.888  2.632   -37.977  1.00 31.69  ? 70  GLN D CB  1 
ATOM   13280 C CG  . GLN D  1 70  ? -37.765  3.328   -38.738  1.00 32.53  ? 70  GLN D CG  1 
ATOM   13281 C CD  . GLN D  1 70  ? -37.950  4.834   -38.807  1.00 32.64  ? 70  GLN D CD  1 
ATOM   13282 O OE1 . GLN D  1 70  ? -38.336  5.488   -37.834  1.00 30.61  ? 70  GLN D OE1 1 
ATOM   13283 N NE2 . GLN D  1 70  ? -37.697  5.391   -39.981  1.00 34.02  ? 70  GLN D NE2 1 
ATOM   13284 N N   . TYR D  1 71  ? -38.190  -0.005  -36.267  1.00 33.43  ? 71  TYR D N   1 
ATOM   13285 C CA  . TYR D  1 71  ? -37.421  -1.227  -36.270  1.00 32.95  ? 71  TYR D CA  1 
ATOM   13286 C C   . TYR D  1 71  ? -37.271  -1.779  -37.684  1.00 34.44  ? 71  TYR D C   1 
ATOM   13287 O O   . TYR D  1 71  ? -38.072  -1.516  -38.572  1.00 34.66  ? 71  TYR D O   1 
ATOM   13288 C CB  . TYR D  1 71  ? -38.164  -2.289  -35.446  1.00 33.83  ? 71  TYR D CB  1 
ATOM   13289 C CG  . TYR D  1 71  ? -38.090  -2.211  -33.929  1.00 32.73  ? 71  TYR D CG  1 
ATOM   13290 C CD1 . TYR D  1 71  ? -36.943  -1.754  -33.295  1.00 32.29  ? 71  TYR D CD1 1 
ATOM   13291 C CD2 . TYR D  1 71  ? -39.160  -2.630  -33.128  1.00 32.73  ? 71  TYR D CD2 1 
ATOM   13292 C CE1 . TYR D  1 71  ? -36.872  -1.685  -31.915  1.00 32.09  ? 71  TYR D CE1 1 
ATOM   13293 C CE2 . TYR D  1 71  ? -39.083  -2.594  -31.744  1.00 31.44  ? 71  TYR D CE2 1 
ATOM   13294 C CZ  . TYR D  1 71  ? -37.935  -2.108  -31.140  1.00 31.16  ? 71  TYR D CZ  1 
ATOM   13295 O OH  . TYR D  1 71  ? -37.783  -1.977  -29.796  1.00 30.69  ? 71  TYR D OH  1 
ATOM   13296 N N   . SER D  1 72  ? -36.235  -2.602  -37.867  1.00 34.66  ? 72  SER D N   1 
ATOM   13297 C CA  . SER D  1 72  ? -36.103  -3.420  -39.050  1.00 35.68  ? 72  SER D CA  1 
ATOM   13298 C C   . SER D  1 72  ? -37.113  -4.576  -38.982  1.00 36.75  ? 72  SER D C   1 
ATOM   13299 O O   . SER D  1 72  ? -37.758  -4.796  -37.943  1.00 35.89  ? 72  SER D O   1 
ATOM   13300 C CB  . SER D  1 72  ? -34.683  -3.901  -39.186  1.00 35.98  ? 72  SER D CB  1 
ATOM   13301 O OG  . SER D  1 72  ? -34.423  -5.004  -38.327  1.00 35.46  ? 72  SER D OG  1 
ATOM   13302 N N   . GLU D  1 73  ? -37.263  -5.292  -40.115  1.00 38.06  ? 73  GLU D N   1 
ATOM   13303 C CA  . GLU D  1 73  ? -38.200  -6.401  -40.206  1.00 38.96  ? 73  GLU D CA  1 
ATOM   13304 C C   . GLU D  1 73  ? -37.766  -7.509  -39.247  1.00 39.86  ? 73  GLU D C   1 
ATOM   13305 O O   . GLU D  1 73  ? -38.613  -8.140  -38.612  1.00 40.74  ? 73  GLU D O   1 
ATOM   13306 C CB  . GLU D  1 73  ? -38.323  -6.961  -41.623  1.00 40.51  ? 73  GLU D CB  1 
ATOM   13307 C CG  . GLU D  1 73  ? -39.345  -8.099  -41.723  1.00 41.13  ? 73  GLU D CG  1 
ATOM   13308 C CD  . GLU D  1 73  ? -39.779  -8.546  -43.111  1.00 40.96  ? 73  GLU D CD  1 
ATOM   13309 O OE1 . GLU D  1 73  ? -39.067  -8.216  -44.087  1.00 40.98  ? 73  GLU D OE1 1 
ATOM   13310 O OE2 . GLU D  1 73  ? -40.856  -9.195  -43.204  1.00 40.19  ? 73  GLU D OE2 1 
ATOM   13311 N N   . ASN D  1 74  ? -36.449  -7.734  -39.131  1.00 38.74  ? 74  ASN D N   1 
ATOM   13312 C CA  . ASN D  1 74  ? -35.940  -8.751  -38.216  1.00 39.48  ? 74  ASN D CA  1 
ATOM   13313 C C   . ASN D  1 74  ? -36.220  -8.415  -36.760  1.00 37.33  ? 74  ASN D C   1 
ATOM   13314 O O   . ASN D  1 74  ? -36.515  -9.315  -36.000  1.00 37.85  ? 74  ASN D O   1 
ATOM   13315 C CB  . ASN D  1 74  ? -34.449  -8.989  -38.381  1.00 40.08  ? 74  ASN D CB  1 
ATOM   13316 C CG  . ASN D  1 74  ? -34.162  -9.692  -39.678  1.00 40.83  ? 74  ASN D CG  1 
ATOM   13317 O OD1 . ASN D  1 74  ? -35.030  -10.372 -40.258  1.00 41.04  ? 74  ASN D OD1 1 
ATOM   13318 N ND2 . ASN D  1 74  ? -32.951  -9.477  -40.150  1.00 41.36  ? 74  ASN D ND2 1 
ATOM   13319 N N   . GLN D  1 75  ? -36.115  -7.140  -36.379  1.00 35.84  ? 75  GLN D N   1 
ATOM   13320 C CA  . GLN D  1 75  ? -36.454  -6.722  -35.037  1.00 34.45  ? 75  GLN D CA  1 
ATOM   13321 C C   . GLN D  1 75  ? -37.953  -6.956  -34.811  1.00 34.95  ? 75  GLN D C   1 
ATOM   13322 O O   . GLN D  1 75  ? -38.378  -7.392  -33.744  1.00 33.87  ? 75  GLN D O   1 
ATOM   13323 C CB  . GLN D  1 75  ? -36.046  -5.257  -34.838  1.00 34.29  ? 75  GLN D CB  1 
ATOM   13324 C CG  . GLN D  1 75  ? -34.552  -4.979  -34.982  1.00 34.64  ? 75  GLN D CG  1 
ATOM   13325 C CD  . GLN D  1 75  ? -34.154  -3.538  -34.714  1.00 33.39  ? 75  GLN D CD  1 
ATOM   13326 O OE1 . GLN D  1 75  ? -34.742  -2.591  -35.222  1.00 34.49  ? 75  GLN D OE1 1 
ATOM   13327 N NE2 . GLN D  1 75  ? -33.118  -3.327  -33.933  1.00 33.48  ? 75  GLN D NE2 1 
ATOM   13328 N N   . LEU D  1 76  ? -38.784  -6.659  -35.813  1.00 36.48  ? 76  LEU D N   1 
ATOM   13329 C CA  . LEU D  1 76  ? -40.218  -6.857  -35.648  1.00 37.89  ? 76  LEU D CA  1 
ATOM   13330 C C   . LEU D  1 76  ? -40.511  -8.342  -35.445  1.00 39.76  ? 76  LEU D C   1 
ATOM   13331 O O   . LEU D  1 76  ? -41.386  -8.663  -34.643  1.00 41.17  ? 76  LEU D O   1 
ATOM   13332 C CB  . LEU D  1 76  ? -41.072  -6.307  -36.793  1.00 38.78  ? 76  LEU D CB  1 
ATOM   13333 C CG  . LEU D  1 76  ? -41.269  -4.792  -36.830  1.00 39.54  ? 76  LEU D CG  1 
ATOM   13334 C CD1 . LEU D  1 76  ? -42.155  -4.483  -38.005  1.00 41.28  ? 76  LEU D CD1 1 
ATOM   13335 C CD2 . LEU D  1 76  ? -41.886  -4.308  -35.550  1.00 40.13  ? 76  LEU D CD2 1 
ATOM   13336 N N   . LYS D  1 77  ? -39.850  -9.238  -36.205  1.00 40.27  ? 77  LYS D N   1 
ATOM   13337 C CA  . LYS D  1 77  ? -40.122  -10.662 -36.049  1.00 41.59  ? 77  LYS D CA  1 
ATOM   13338 C C   . LYS D  1 77  ? -39.864  -11.079 -34.605  1.00 39.19  ? 77  LYS D C   1 
ATOM   13339 O O   . LYS D  1 77  ? -40.518  -11.984 -34.117  1.00 39.33  ? 77  LYS D O   1 
ATOM   13340 C CB  . LYS D  1 77  ? -39.285  -11.611 -36.919  1.00 43.74  ? 77  LYS D CB  1 
ATOM   13341 C CG  . LYS D  1 77  ? -39.606  -11.543 -38.377  1.00 44.72  ? 77  LYS D CG  1 
ATOM   13342 C CD  . LYS D  1 77  ? -38.729  -12.427 -39.243  1.00 47.47  ? 77  LYS D CD  1 
ATOM   13343 C CE  . LYS D  1 77  ? -39.042  -12.167 -40.686  1.00 49.13  ? 77  LYS D CE  1 
ATOM   13344 N NZ  . LYS D  1 77  ? -38.282  -13.070 -41.546  1.00 52.15  ? 77  LYS D NZ  1 
ATOM   13345 N N   . LEU D  1 78  ? -38.888  -10.436 -33.951  1.00 37.19  ? 78  LEU D N   1 
ATOM   13346 C CA  . LEU D  1 78  ? -38.538  -10.773 -32.586  1.00 36.15  ? 78  LEU D CA  1 
ATOM   13347 C C   . LEU D  1 78  ? -39.655  -10.302 -31.664  1.00 34.60  ? 78  LEU D C   1 
ATOM   13348 O O   . LEU D  1 78  ? -40.134  -11.057 -30.822  1.00 36.41  ? 78  LEU D O   1 
ATOM   13349 C CB  . LEU D  1 78  ? -37.174  -10.204 -32.204  1.00 35.51  ? 78  LEU D CB  1 
ATOM   13350 C CG  . LEU D  1 78  ? -36.666  -10.563 -30.804  1.00 37.87  ? 78  LEU D CG  1 
ATOM   13351 C CD1 . LEU D  1 78  ? -36.701  -12.094 -30.535  1.00 39.07  ? 78  LEU D CD1 1 
ATOM   13352 C CD2 . LEU D  1 78  ? -35.228  -10.067 -30.625  1.00 38.43  ? 78  LEU D CD2 1 
ATOM   13353 N N   . VAL D  1 79  ? -40.079  -9.054  -31.832  1.00 33.54  ? 79  VAL D N   1 
ATOM   13354 C CA  . VAL D  1 79  ? -41.120  -8.515  -30.982  1.00 33.67  ? 79  VAL D CA  1 
ATOM   13355 C C   . VAL D  1 79  ? -42.418  -9.305  -31.166  1.00 35.00  ? 79  VAL D C   1 
ATOM   13356 O O   . VAL D  1 79  ? -43.040  -9.696  -30.181  1.00 37.92  ? 79  VAL D O   1 
ATOM   13357 C CB  . VAL D  1 79  ? -41.296  -7.014  -31.206  1.00 32.56  ? 79  VAL D CB  1 
ATOM   13358 C CG1 . VAL D  1 79  ? -42.301  -6.430  -30.219  1.00 31.96  ? 79  VAL D CG1 1 
ATOM   13359 C CG2 . VAL D  1 79  ? -39.961  -6.314  -31.062  1.00 32.49  ? 79  VAL D CG2 1 
ATOM   13360 N N   . GLN D  1 80  ? -42.762  -9.647  -32.405  1.00 35.47  ? 80  GLN D N   1 
ATOM   13361 C CA  . GLN D  1 80  ? -43.903  -10.508 -32.686  1.00 36.86  ? 80  GLN D CA  1 
ATOM   13362 C C   . GLN D  1 80  ? -43.848  -11.812 -31.871  1.00 38.80  ? 80  GLN D C   1 
ATOM   13363 O O   . GLN D  1 80  ? -44.829  -12.156 -31.219  1.00 37.56  ? 80  GLN D O   1 
ATOM   13364 C CB  . GLN D  1 80  ? -43.989  -10.730 -34.196  1.00 36.23  ? 80  GLN D CB  1 
ATOM   13365 C CG  . GLN D  1 80  ? -45.308  -11.325 -34.684  1.00 37.20  ? 80  GLN D CG  1 
ATOM   13366 C CD  . GLN D  1 80  ? -46.503  -10.392 -34.589  1.00 36.60  ? 80  GLN D CD  1 
ATOM   13367 O OE1 . GLN D  1 80  ? -46.425  -9.184  -34.843  1.00 34.93  ? 80  GLN D OE1 1 
ATOM   13368 N NE2 . GLN D  1 80  ? -47.643  -10.961 -34.216  1.00 36.10  ? 80  GLN D NE2 1 
ATOM   13369 N N   . GLU D  1 81  ? -42.723  -12.540 -31.894  1.00 39.92  ? 81  GLU D N   1 
ATOM   13370 C CA  . GLU D  1 81  ? -42.625  -13.825 -31.210  1.00 42.83  ? 81  GLU D CA  1 
ATOM   13371 C C   . GLU D  1 81  ? -42.593  -13.640 -29.693  1.00 39.51  ? 81  GLU D C   1 
ATOM   13372 O O   . GLU D  1 81  ? -42.945  -14.547 -28.953  1.00 38.17  ? 81  GLU D O   1 
ATOM   13373 C CB  . GLU D  1 81  ? -41.369  -14.636 -31.554  1.00 49.72  ? 81  GLU D CB  1 
ATOM   13374 C CG  . GLU D  1 81  ? -41.341  -15.205 -32.973  1.00 57.74  ? 81  GLU D CG  1 
ATOM   13375 C CD  . GLU D  1 81  ? -39.981  -15.209 -33.694  1.00 66.42  ? 81  GLU D CD  1 
ATOM   13376 O OE1 . GLU D  1 81  ? -38.953  -14.612 -33.215  1.00 65.47  ? 81  GLU D OE1 1 
ATOM   13377 O OE2 . GLU D  1 81  ? -39.968  -15.818 -34.800  1.00 65.26  ? 81  GLU D OE2 1 
ATOM   13378 N N   . SER D  1 82  ? -42.109  -12.482 -29.216  1.00 38.22  ? 82  SER D N   1 
ATOM   13379 C CA  . SER D  1 82  ? -42.034  -12.221 -27.779  1.00 35.33  ? 82  SER D CA  1 
ATOM   13380 C C   . SER D  1 82  ? -43.408  -12.342 -27.099  1.00 33.89  ? 82  SER D C   1 
ATOM   13381 O O   . SER D  1 82  ? -43.475  -12.680 -25.925  1.00 32.24  ? 82  SER D O   1 
ATOM   13382 C CB  . SER D  1 82  ? -41.474  -10.832 -27.523  1.00 35.01  ? 82  SER D CB  1 
ATOM   13383 O OG  . SER D  1 82  ? -42.527  -9.868  -27.614  1.00 33.47  ? 82  SER D OG  1 
ATOM   13384 N N   . GLY D  1 83  ? -44.479  -11.931 -27.803  1.00 33.59  ? 83  GLY D N   1 
ATOM   13385 C CA  . GLY D  1 83  ? -45.798  -11.777 -27.223  1.00 33.75  ? 83  GLY D CA  1 
ATOM   13386 C C   . GLY D  1 83  ? -46.138  -10.319 -26.895  1.00 32.30  ? 83  GLY D C   1 
ATOM   13387 O O   . GLY D  1 83  ? -47.286  -10.000 -26.621  1.00 30.83  ? 83  GLY D O   1 
ATOM   13388 N N   . LEU D  1 84  ? -45.132  -9.445  -26.842  1.00 33.25  ? 84  LEU D N   1 
ATOM   13389 C CA  . LEU D  1 84  ? -45.344  -8.052  -26.438  1.00 32.71  ? 84  LEU D CA  1 
ATOM   13390 C C   . LEU D  1 84  ? -45.985  -7.269  -27.573  1.00 32.05  ? 84  LEU D C   1 
ATOM   13391 O O   . LEU D  1 84  ? -45.620  -7.482  -28.724  1.00 32.02  ? 84  LEU D O   1 
ATOM   13392 C CB  . LEU D  1 84  ? -44.031  -7.384  -26.048  1.00 32.53  ? 84  LEU D CB  1 
ATOM   13393 C CG  . LEU D  1 84  ? -43.467  -7.789  -24.689  1.00 34.86  ? 84  LEU D CG  1 
ATOM   13394 C CD1 . LEU D  1 84  ? -41.980  -7.440  -24.587  1.00 36.76  ? 84  LEU D CD1 1 
ATOM   13395 C CD2 . LEU D  1 84  ? -44.267  -7.138  -23.581  1.00 33.91  ? 84  LEU D CD2 1 
ATOM   13396 N N   . LYS D  1 85  ? -46.871  -6.322  -27.233  1.00 30.62  ? 85  LYS D N   1 
ATOM   13397 C CA  . LYS D  1 85  ? -47.332  -5.362  -28.222  1.00 31.71  ? 85  LYS D CA  1 
ATOM   13398 C C   . LYS D  1 85  ? -46.343  -4.204  -28.352  1.00 30.57  ? 85  LYS D C   1 
ATOM   13399 O O   . LYS D  1 85  ? -45.477  -4.013  -27.499  1.00 29.25  ? 85  LYS D O   1 
ATOM   13400 C CB  . LYS D  1 85  ? -48.702  -4.807  -27.848  1.00 32.92  ? 85  LYS D CB  1 
ATOM   13401 C CG  . LYS D  1 85  ? -49.733  -5.887  -27.568  1.00 34.78  ? 85  LYS D CG  1 
ATOM   13402 C CD  . LYS D  1 85  ? -49.915  -7.022  -28.572  1.00 34.61  ? 85  LYS D CD  1 
ATOM   13403 C CE  . LYS D  1 85  ? -50.972  -8.009  -28.074  1.00 34.38  ? 85  LYS D CE  1 
ATOM   13404 N NZ  . LYS D  1 85  ? -51.132  -9.200  -28.931  1.00 34.18  ? 85  LYS D NZ  1 
ATOM   13405 N N   . LEU D  1 86  ? -46.508  -3.431  -29.434  1.00 31.04  ? 86  LEU D N   1 
ATOM   13406 C CA  . LEU D  1 86  ? -45.577  -2.369  -29.798  1.00 31.44  ? 86  LEU D CA  1 
ATOM   13407 C C   . LEU D  1 86  ? -46.309  -1.090  -30.213  1.00 30.60  ? 86  LEU D C   1 
ATOM   13408 O O   . LEU D  1 86  ? -47.145  -1.093  -31.122  1.00 28.95  ? 86  LEU D O   1 
ATOM   13409 C CB  . LEU D  1 86  ? -44.693  -2.898  -30.926  1.00 31.88  ? 86  LEU D CB  1 
ATOM   13410 C CG  . LEU D  1 86  ? -43.750  -1.893  -31.599  1.00 32.68  ? 86  LEU D CG  1 
ATOM   13411 C CD1 . LEU D  1 86  ? -42.861  -1.101  -30.648  1.00 33.21  ? 86  LEU D CD1 1 
ATOM   13412 C CD2 . LEU D  1 86  ? -42.897  -2.618  -32.626  1.00 32.76  ? 86  LEU D CD2 1 
ATOM   13413 N N   . ILE D  1 87  ? -45.996  -0.008  -29.490  1.00 30.04  ? 87  ILE D N   1 
ATOM   13414 C CA  . ILE D  1 87  ? -46.207  1.349   -29.970  1.00 30.99  ? 87  ILE D CA  1 
ATOM   13415 C C   . ILE D  1 87  ? -44.923  1.806   -30.672  1.00 31.77  ? 87  ILE D C   1 
ATOM   13416 O O   . ILE D  1 87  ? -43.932  2.110   -30.012  1.00 29.16  ? 87  ILE D O   1 
ATOM   13417 C CB  . ILE D  1 87  ? -46.623  2.274   -28.804  1.00 30.22  ? 87  ILE D CB  1 
ATOM   13418 C CG1 . ILE D  1 87  ? -47.933  1.770   -28.217  1.00 30.92  ? 87  ILE D CG1 1 
ATOM   13419 C CG2 . ILE D  1 87  ? -46.739  3.740   -29.246  1.00 29.57  ? 87  ILE D CG2 1 
ATOM   13420 C CD1 . ILE D  1 87  ? -48.371  2.460   -26.948  1.00 30.78  ? 87  ILE D CD1 1 
ATOM   13421 N N   . MET D  1 88  ? -44.940  1.842   -32.012  1.00 32.57  ? 88  MET D N   1 
ATOM   13422 C CA  . MET D  1 88  ? -43.721  2.114   -32.758  1.00 32.79  ? 88  MET D CA  1 
ATOM   13423 C C   . MET D  1 88  ? -43.626  3.599   -33.117  1.00 31.53  ? 88  MET D C   1 
ATOM   13424 O O   . MET D  1 88  ? -44.517  4.140   -33.767  1.00 29.43  ? 88  MET D O   1 
ATOM   13425 C CB  . MET D  1 88  ? -43.617  1.269   -34.037  1.00 33.19  ? 88  MET D CB  1 
ATOM   13426 C CG  . MET D  1 88  ? -42.277  1.420   -34.730  1.00 34.36  ? 88  MET D CG  1 
ATOM   13427 S SD  . MET D  1 88  ? -41.840  0.097   -35.871  1.00 35.86  ? 88  MET D SD  1 
ATOM   13428 C CE  . MET D  1 88  ? -43.164  0.235   -37.073  1.00 34.26  ? 88  MET D CE  1 
ATOM   13429 N N   . GLY D  1 89  ? -42.497  4.215   -32.719  1.00 32.52  ? 89  GLY D N   1 
ATOM   13430 C CA  . GLY D  1 89  ? -42.142  5.576   -33.104  1.00 32.42  ? 89  GLY D CA  1 
ATOM   13431 C C   . GLY D  1 89  ? -41.438  5.582   -34.456  1.00 32.08  ? 89  GLY D C   1 
ATOM   13432 O O   . GLY D  1 89  ? -40.684  4.665   -34.769  1.00 33.49  ? 89  GLY D O   1 
ATOM   13433 N N   . ILE D  1 90  ? -41.754  6.589   -35.263  1.00 31.27  ? 90  ILE D N   1 
ATOM   13434 C CA  . ILE D  1 90  ? -41.137  6.825   -36.557  1.00 33.57  ? 90  ILE D CA  1 
ATOM   13435 C C   . ILE D  1 90  ? -40.252  8.077   -36.444  1.00 33.95  ? 90  ILE D C   1 
ATOM   13436 O O   . ILE D  1 90  ? -40.721  9.065   -35.881  1.00 35.49  ? 90  ILE D O   1 
ATOM   13437 C CB  . ILE D  1 90  ? -42.272  6.999   -37.576  1.00 33.54  ? 90  ILE D CB  1 
ATOM   13438 C CG1 . ILE D  1 90  ? -43.237  5.787   -37.559  1.00 34.02  ? 90  ILE D CG1 1 
ATOM   13439 C CG2 . ILE D  1 90  ? -41.744  7.319   -38.977  1.00 34.67  ? 90  ILE D CG2 1 
ATOM   13440 C CD1 . ILE D  1 90  ? -42.683  4.468   -38.052  1.00 33.33  ? 90  ILE D CD1 1 
ATOM   13441 N N   . ASP D  1 91  ? -38.995  8.032   -36.938  1.00 34.08  ? 91  ASP D N   1 
ATOM   13442 C CA  . ASP D  1 91  ? -38.030  9.125   -36.814  1.00 36.26  ? 91  ASP D CA  1 
ATOM   13443 C C   . ASP D  1 91  ? -38.282  10.254  -37.823  1.00 35.85  ? 91  ASP D C   1 
ATOM   13444 O O   . ASP D  1 91  ? -37.457  10.568  -38.654  1.00 38.78  ? 91  ASP D O   1 
ATOM   13445 C CB  . ASP D  1 91  ? -36.586  8.652   -37.003  1.00 38.91  ? 91  ASP D CB  1 
ATOM   13446 C CG  . ASP D  1 91  ? -35.495  9.736   -36.879  1.00 42.15  ? 91  ASP D CG  1 
ATOM   13447 O OD1 . ASP D  1 91  ? -35.808  10.894  -36.484  1.00 40.79  ? 91  ASP D OD1 1 
ATOM   13448 O OD2 . ASP D  1 91  ? -34.317  9.466   -37.239  1.00 43.23  ? 91  ASP D OD2 1 
ATOM   13449 N N   . ILE D  1 92  ? -39.394  10.955  -37.748  1.00 39.27  ? 92  ILE D N   1 
ATOM   13450 C CA  . ILE D  1 92  ? -39.549  12.175  -38.548  1.00 39.72  ? 92  ILE D CA  1 
ATOM   13451 C C   . ILE D  1 92  ? -38.859  13.329  -37.807  1.00 35.63  ? 92  ILE D C   1 
ATOM   13452 O O   . ILE D  1 92  ? -39.265  13.704  -36.711  1.00 33.35  ? 92  ILE D O   1 
ATOM   13453 C CB  . ILE D  1 92  ? -41.055  12.443  -38.772  1.00 39.76  ? 92  ILE D CB  1 
ATOM   13454 C CG1 . ILE D  1 92  ? -41.775  11.214  -39.378  1.00 38.63  ? 92  ILE D CG1 1 
ATOM   13455 C CG2 . ILE D  1 92  ? -41.284  13.707  -39.607  1.00 41.53  ? 92  ILE D CG2 1 
ATOM   13456 C CD1 . ILE D  1 92  ? -41.214  10.750  -40.712  1.00 38.39  ? 92  ILE D CD1 1 
ATOM   13457 N N   . LYS D  1 93  ? -37.763  13.847  -38.337  1.00 37.83  ? 93  LYS D N   1 
ATOM   13458 C CA  . LYS D  1 93  ? -36.962  14.779  -37.551  1.00 43.11  ? 93  LYS D CA  1 
ATOM   13459 C C   . LYS D  1 93  ? -37.778  16.027  -37.214  1.00 39.23  ? 93  LYS D C   1 
ATOM   13460 O O   . LYS D  1 93  ? -38.216  16.722  -38.127  1.00 36.56  ? 93  LYS D O   1 
ATOM   13461 C CB  . LYS D  1 93  ? -35.654  15.156  -38.250  1.00 51.92  ? 93  LYS D CB  1 
ATOM   13462 C CG  . LYS D  1 93  ? -34.542  14.125  -38.065  1.00 63.78  ? 93  LYS D CG  1 
ATOM   13463 C CD  . LYS D  1 93  ? -33.404  14.294  -39.069  1.00 78.66  ? 93  LYS D CD  1 
ATOM   13464 C CE  . LYS D  1 93  ? -33.752  13.775  -40.453  1.00 84.77  ? 93  LYS D CE  1 
ATOM   13465 N NZ  . LYS D  1 93  ? -32.855  14.306  -41.489  1.00 82.50  ? 93  LYS D NZ  1 
ATOM   13466 N N   . PRO D  1 94  ? -37.987  16.356  -35.912  1.00 37.03  ? 94  PRO D N   1 
ATOM   13467 C CA  . PRO D  1 94  ? -38.776  17.525  -35.514  1.00 38.46  ? 94  PRO D CA  1 
ATOM   13468 C C   . PRO D  1 94  ? -38.266  18.927  -35.845  1.00 39.98  ? 94  PRO D C   1 
ATOM   13469 O O   . PRO D  1 94  ? -39.051  19.874  -35.764  1.00 43.03  ? 94  PRO D O   1 
ATOM   13470 C CB  . PRO D  1 94  ? -38.897  17.339  -33.992  1.00 37.86  ? 94  PRO D CB  1 
ATOM   13471 C CG  . PRO D  1 94  ? -37.705  16.538  -33.578  1.00 36.61  ? 94  PRO D CG  1 
ATOM   13472 C CD  . PRO D  1 94  ? -37.444  15.641  -34.752  1.00 36.85  ? 94  PRO D CD  1 
ATOM   13473 N N   . GLU D  1 95  ? -36.981  19.058  -36.215  1.00 41.18  ? 95  GLU D N   1 
ATOM   13474 C CA  . GLU D  1 95  ? -36.358  20.366  -36.408  1.00 43.71  ? 95  GLU D CA  1 
ATOM   13475 C C   . GLU D  1 95  ? -36.375  20.748  -37.880  1.00 41.15  ? 95  GLU D C   1 
ATOM   13476 O O   . GLU D  1 95  ? -35.984  21.860  -38.220  1.00 38.88  ? 95  GLU D O   1 
ATOM   13477 C CB  . GLU D  1 95  ? -34.884  20.482  -35.999  1.00 47.77  ? 95  GLU D CB  1 
ATOM   13478 C CG  . GLU D  1 95  ? -34.645  20.540  -34.490  1.00 57.07  ? 95  GLU D CG  1 
ATOM   13479 C CD  . GLU D  1 95  ? -34.481  19.186  -33.800  1.00 66.43  ? 95  GLU D CD  1 
ATOM   13480 O OE1 . GLU D  1 95  ? -34.470  18.136  -34.523  1.00 74.75  ? 95  GLU D OE1 1 
ATOM   13481 O OE2 . GLU D  1 95  ? -34.367  19.181  -32.538  1.00 56.08  ? 95  GLU D OE2 1 
ATOM   13482 N N   . GLU D  1 96  ? -36.782  19.817  -38.752  1.00 39.15  ? 96  GLU D N   1 
ATOM   13483 C CA  . GLU D  1 96  ? -36.797  20.085  -40.186  1.00 38.53  ? 96  GLU D CA  1 
ATOM   13484 C C   . GLU D  1 96  ? -37.969  20.995  -40.563  1.00 32.15  ? 96  GLU D C   1 
ATOM   13485 O O   . GLU D  1 96  ? -38.944  21.120  -39.824  1.00 29.01  ? 96  GLU D O   1 
ATOM   13486 C CB  . GLU D  1 96  ? -36.901  18.785  -40.986  1.00 42.19  ? 96  GLU D CB  1 
ATOM   13487 C CG  . GLU D  1 96  ? -35.612  17.973  -41.001  1.00 48.56  ? 96  GLU D CG  1 
ATOM   13488 C CD  . GLU D  1 96  ? -34.491  18.633  -41.776  1.00 53.46  ? 96  GLU D CD  1 
ATOM   13489 O OE1 . GLU D  1 96  ? -34.463  18.630  -43.042  1.00 56.61  ? 96  GLU D OE1 1 
ATOM   13490 O OE2 . GLU D  1 96  ? -33.630  19.152  -41.037  1.00 53.72  ? 96  GLU D OE2 1 
ATOM   13491 N N   . ASP D  1 97  ? -37.869  21.569  -41.762  1.00 30.93  ? 97  ASP D N   1 
ATOM   13492 C CA  . ASP D  1 97  ? -38.932  22.367  -42.344  1.00 32.34  ? 97  ASP D CA  1 
ATOM   13493 C C   . ASP D  1 97  ? -40.057  21.454  -42.873  1.00 33.64  ? 97  ASP D C   1 
ATOM   13494 O O   . ASP D  1 97  ? -39.956  20.895  -43.965  1.00 30.91  ? 97  ASP D O   1 
ATOM   13495 C CB  . ASP D  1 97  ? -38.367  23.295  -43.407  1.00 31.66  ? 97  ASP D CB  1 
ATOM   13496 C CG  . ASP D  1 97  ? -39.407  24.209  -44.038  1.00 31.65  ? 97  ASP D CG  1 
ATOM   13497 O OD1 . ASP D  1 97  ? -40.595  24.111  -43.674  1.00 31.62  ? 97  ASP D OD1 1 
ATOM   13498 O OD2 . ASP D  1 97  ? -39.030  24.971  -44.927  1.00 33.65  ? 97  ASP D OD2 1 
ATOM   13499 N N   . TYR D  1 98  ? -41.159  21.364  -42.115  1.00 34.99  ? 98  TYR D N   1 
ATOM   13500 C CA  . TYR D  1 98  ? -42.272  20.478  -42.438  1.00 34.20  ? 98  TYR D CA  1 
ATOM   13501 C C   . TYR D  1 98  ? -42.927  20.889  -43.751  1.00 34.81  ? 98  TYR D C   1 
ATOM   13502 O O   . TYR D  1 98  ? -43.586  20.075  -44.400  1.00 35.78  ? 98  TYR D O   1 
ATOM   13503 C CB  . TYR D  1 98  ? -43.370  20.556  -41.384  1.00 32.58  ? 98  TYR D CB  1 
ATOM   13504 C CG  . TYR D  1 98  ? -42.923  20.371  -39.949  1.00 31.50  ? 98  TYR D CG  1 
ATOM   13505 C CD1 . TYR D  1 98  ? -41.924  19.469  -39.605  1.00 31.22  ? 98  TYR D CD1 1 
ATOM   13506 C CD2 . TYR D  1 98  ? -43.528  21.096  -38.928  1.00 31.48  ? 98  TYR D CD2 1 
ATOM   13507 C CE1 . TYR D  1 98  ? -41.555  19.277  -38.279  1.00 30.40  ? 98  TYR D CE1 1 
ATOM   13508 C CE2 . TYR D  1 98  ? -43.159  20.919  -37.607  1.00 30.30  ? 98  TYR D CE2 1 
ATOM   13509 C CZ  . TYR D  1 98  ? -42.171  20.008  -37.273  1.00 30.34  ? 98  TYR D CZ  1 
ATOM   13510 O OH  . TYR D  1 98  ? -41.805  19.862  -35.949  1.00 29.03  ? 98  TYR D OH  1 
ATOM   13511 N N   . GLY D  1 99  ? -42.703  22.155  -44.124  1.00 35.35  ? 99  GLY D N   1 
ATOM   13512 C CA  . GLY D  1 99  ? -43.293  22.758  -45.306  1.00 35.40  ? 99  GLY D CA  1 
ATOM   13513 C C   . GLY D  1 99  ? -42.454  22.552  -46.557  1.00 34.61  ? 99  GLY D C   1 
ATOM   13514 O O   . GLY D  1 99  ? -42.927  22.838  -47.649  1.00 38.13  ? 99  GLY D O   1 
ATOM   13515 N N   . ASP D  1 100 ? -41.236  22.030  -46.401  1.00 33.36  ? 100 ASP D N   1 
ATOM   13516 C CA  . ASP D  1 100 ? -40.379  21.727  -47.538  1.00 34.39  ? 100 ASP D CA  1 
ATOM   13517 C C   . ASP D  1 100 ? -40.797  20.400  -48.173  1.00 34.39  ? 100 ASP D C   1 
ATOM   13518 O O   . ASP D  1 100 ? -40.677  19.338  -47.555  1.00 32.40  ? 100 ASP D O   1 
ATOM   13519 C CB  . ASP D  1 100 ? -38.918  21.651  -47.125  1.00 35.88  ? 100 ASP D CB  1 
ATOM   13520 C CG  . ASP D  1 100 ? -37.933  21.349  -48.251  1.00 38.37  ? 100 ASP D CG  1 
ATOM   13521 O OD1 . ASP D  1 100 ? -38.366  21.262  -49.426  1.00 37.24  ? 100 ASP D OD1 1 
ATOM   13522 O OD2 . ASP D  1 100 ? -36.729  21.235  -47.954  1.00 39.93  ? 100 ASP D OD2 1 
ATOM   13523 N N   . PRO D  1 101 ? -41.245  20.408  -49.445  1.00 34.98  ? 101 PRO D N   1 
ATOM   13524 C CA  . PRO D  1 101 ? -41.783  19.216  -50.085  1.00 35.04  ? 101 PRO D CA  1 
ATOM   13525 C C   . PRO D  1 101 ? -40.737  18.112  -50.201  1.00 36.66  ? 101 PRO D C   1 
ATOM   13526 O O   . PRO D  1 101 ? -41.101  16.921  -50.271  1.00 35.23  ? 101 PRO D O   1 
ATOM   13527 C CB  . PRO D  1 101 ? -42.267  19.639  -51.464  1.00 36.59  ? 101 PRO D CB  1 
ATOM   13528 C CG  . PRO D  1 101 ? -42.058  21.140  -51.512  1.00 38.14  ? 101 PRO D CG  1 
ATOM   13529 C CD  . PRO D  1 101 ? -41.160  21.546  -50.366  1.00 37.03  ? 101 PRO D CD  1 
ATOM   13530 N N   . GLU D  1 102 ? -39.454  18.521  -50.280  1.00 36.90  ? 102 GLU D N   1 
ATOM   13531 C CA  . GLU D  1 102 ? -38.356  17.579  -50.293  1.00 37.60  ? 102 GLU D CA  1 
ATOM   13532 C C   . GLU D  1 102 ? -38.434  16.735  -49.022  1.00 36.96  ? 102 GLU D C   1 
ATOM   13533 O O   . GLU D  1 102 ? -38.349  15.505  -49.078  1.00 39.51  ? 102 GLU D O   1 
ATOM   13534 C CB  . GLU D  1 102 ? -36.966  18.194  -50.453  1.00 39.92  ? 102 GLU D CB  1 
ATOM   13535 C CG  . GLU D  1 102 ? -35.927  17.122  -50.766  1.00 42.61  ? 102 GLU D CG  1 
ATOM   13536 C CD  . GLU D  1 102 ? -34.555  17.555  -51.208  1.00 45.96  ? 102 GLU D CD  1 
ATOM   13537 O OE1 . GLU D  1 102 ? -34.441  18.536  -51.931  1.00 48.96  ? 102 GLU D OE1 1 
ATOM   13538 O OE2 . GLU D  1 102 ? -33.599  16.847  -50.890  1.00 50.91  ? 102 GLU D OE2 1 
ATOM   13539 N N   . PHE D  1 103 ? -38.606  17.398  -47.880  1.00 33.62  ? 103 PHE D N   1 
ATOM   13540 C CA  . PHE D  1 103 ? -38.599  16.724  -46.598  1.00 31.51  ? 103 PHE D CA  1 
ATOM   13541 C C   . PHE D  1 103 ? -39.841  15.827  -46.482  1.00 32.06  ? 103 PHE D C   1 
ATOM   13542 O O   . PHE D  1 103 ? -39.802  14.739  -45.872  1.00 30.24  ? 103 PHE D O   1 
ATOM   13543 C CB  . PHE D  1 103 ? -38.495  17.775  -45.489  1.00 29.57  ? 103 PHE D CB  1 
ATOM   13544 C CG  . PHE D  1 103 ? -38.738  17.150  -44.131  1.00 28.36  ? 103 PHE D CG  1 
ATOM   13545 C CD1 . PHE D  1 103 ? -37.776  16.309  -43.568  1.00 27.02  ? 103 PHE D CD1 1 
ATOM   13546 C CD2 . PHE D  1 103 ? -39.976  17.301  -43.487  1.00 27.40  ? 103 PHE D CD2 1 
ATOM   13547 C CE1 . PHE D  1 103 ? -38.014  15.680  -42.358  1.00 25.93  ? 103 PHE D CE1 1 
ATOM   13548 C CE2 . PHE D  1 103 ? -40.227  16.641  -42.287  1.00 26.09  ? 103 PHE D CE2 1 
ATOM   13549 C CZ  . PHE D  1 103 ? -39.232  15.838  -41.728  1.00 26.53  ? 103 PHE D CZ  1 
ATOM   13550 N N   . VAL D  1 104 ? -40.952  16.318  -47.046  1.00 31.12  ? 104 VAL D N   1 
ATOM   13551 C CA  . VAL D  1 104 ? -42.198  15.601  -46.948  1.00 31.04  ? 104 VAL D CA  1 
ATOM   13552 C C   . VAL D  1 104 ? -42.054  14.313  -47.743  1.00 31.67  ? 104 VAL D C   1 
ATOM   13553 O O   . VAL D  1 104 ? -42.530  13.276  -47.324  1.00 32.56  ? 104 VAL D O   1 
ATOM   13554 C CB  . VAL D  1 104 ? -43.405  16.412  -47.443  1.00 31.56  ? 104 VAL D CB  1 
ATOM   13555 C CG1 . VAL D  1 104 ? -44.680  15.588  -47.357  1.00 32.11  ? 104 VAL D CG1 1 
ATOM   13556 C CG2 . VAL D  1 104 ? -43.604  17.698  -46.669  1.00 31.20  ? 104 VAL D CG2 1 
ATOM   13557 N N   . LYS D  1 105 ? -41.422  14.412  -48.906  1.00 32.37  ? 105 LYS D N   1 
ATOM   13558 C CA  . LYS D  1 105 ? -41.218  13.284  -49.786  1.00 32.94  ? 105 LYS D CA  1 
ATOM   13559 C C   . LYS D  1 105 ? -40.294  12.289  -49.106  1.00 34.36  ? 105 LYS D C   1 
ATOM   13560 O O   . LYS D  1 105 ? -40.604  11.095  -49.094  1.00 35.34  ? 105 LYS D O   1 
ATOM   13561 C CB  . LYS D  1 105 ? -40.657  13.773  -51.116  1.00 33.57  ? 105 LYS D CB  1 
ATOM   13562 C CG  . LYS D  1 105 ? -40.497  12.740  -52.201  1.00 35.11  ? 105 LYS D CG  1 
ATOM   13563 C CD  . LYS D  1 105 ? -39.913  13.283  -53.497  1.00 36.47  ? 105 LYS D CD  1 
ATOM   13564 C CE  . LYS D  1 105 ? -39.486  12.227  -54.454  1.00 37.76  ? 105 LYS D CE  1 
ATOM   13565 N NZ  . LYS D  1 105 ? -39.362  12.808  -55.793  1.00 38.84  ? 105 LYS D NZ  1 
ATOM   13566 N N   . ASP D  1 106 ? -39.186  12.771  -48.515  1.00 34.91  ? 106 ASP D N   1 
ATOM   13567 C CA  . ASP D  1 106 ? -38.254  11.856  -47.854  1.00 36.11  ? 106 ASP D CA  1 
ATOM   13568 C C   . ASP D  1 106 ? -38.961  11.100  -46.729  1.00 35.41  ? 106 ASP D C   1 
ATOM   13569 O O   . ASP D  1 106 ? -38.808  9.888   -46.591  1.00 37.61  ? 106 ASP D O   1 
ATOM   13570 C CB  . ASP D  1 106 ? -36.964  12.541  -47.444  1.00 35.37  ? 106 ASP D CB  1 
ATOM   13571 C CG  . ASP D  1 106 ? -36.160  12.992  -48.645  1.00 35.62  ? 106 ASP D CG  1 
ATOM   13572 O OD1 . ASP D  1 106 ? -36.440  12.479  -49.722  1.00 36.19  ? 106 ASP D OD1 1 
ATOM   13573 O OD2 . ASP D  1 106 ? -35.350  13.911  -48.509  1.00 36.90  ? 106 ASP D OD2 1 
ATOM   13574 N N   . SER D  1 107 ? -39.784  11.829  -45.982  1.00 34.00  ? 107 SER D N   1 
ATOM   13575 C CA  . SER D  1 107 ? -40.573  11.255  -44.929  1.00 32.43  ? 107 SER D CA  1 
ATOM   13576 C C   . SER D  1 107 ? -41.516  10.178  -45.490  1.00 34.89  ? 107 SER D C   1 
ATOM   13577 O O   . SER D  1 107 ? -41.507  9.052   -44.986  1.00 34.01  ? 107 SER D O   1 
ATOM   13578 C CB  . SER D  1 107 ? -41.262  12.337  -44.192  1.00 30.69  ? 107 SER D CB  1 
ATOM   13579 O OG  . SER D  1 107 ? -40.328  13.051  -43.388  1.00 30.51  ? 107 SER D OG  1 
ATOM   13580 N N   . GLU D  1 108 ? -42.278  10.492  -46.553  1.00 35.46  ? 108 GLU D N   1 
ATOM   13581 C CA  . GLU D  1 108 ? -43.231  9.543   -47.133  1.00 36.01  ? 108 GLU D CA  1 
ATOM   13582 C C   . GLU D  1 108 ? -42.506  8.279   -47.627  1.00 35.31  ? 108 GLU D C   1 
ATOM   13583 O O   . GLU D  1 108 ? -42.965  7.176   -47.423  1.00 36.05  ? 108 GLU D O   1 
ATOM   13584 C CB  . GLU D  1 108 ? -44.034  10.095  -48.321  1.00 36.30  ? 108 GLU D CB  1 
ATOM   13585 C CG  . GLU D  1 108 ? -44.955  11.269  -47.990  1.00 37.55  ? 108 GLU D CG  1 
ATOM   13586 C CD  . GLU D  1 108 ? -45.871  11.831  -49.083  1.00 37.55  ? 108 GLU D CD  1 
ATOM   13587 O OE1 . GLU D  1 108 ? -45.980  11.180  -50.131  1.00 40.76  ? 108 GLU D OE1 1 
ATOM   13588 O OE2 . GLU D  1 108 ? -46.463  12.931  -48.922  1.00 36.33  ? 108 GLU D OE2 1 
ATOM   13589 N N   . ILE D  1 109 ? -41.402  8.431   -48.342  1.00 34.84  ? 109 ILE D N   1 
ATOM   13590 C CA  . ILE D  1 109 ? -40.702  7.285   -48.886  1.00 36.52  ? 109 ILE D CA  1 
ATOM   13591 C C   . ILE D  1 109 ? -40.307  6.354   -47.738  1.00 36.23  ? 109 ILE D C   1 
ATOM   13592 O O   . ILE D  1 109 ? -40.571  5.157   -47.775  1.00 36.40  ? 109 ILE D O   1 
ATOM   13593 C CB  . ILE D  1 109 ? -39.495  7.763   -49.724  1.00 37.47  ? 109 ILE D CB  1 
ATOM   13594 C CG1 . ILE D  1 109 ? -39.954  8.611   -50.923  1.00 38.06  ? 109 ILE D CG1 1 
ATOM   13595 C CG2 . ILE D  1 109 ? -38.612  6.598   -50.177  1.00 37.56  ? 109 ILE D CG2 1 
ATOM   13596 C CD1 . ILE D  1 109 ? -38.829  9.192   -51.767  1.00 39.13  ? 109 ILE D CD1 1 
ATOM   13597 N N   . GLU D  1 110 ? -39.697  6.933   -46.698  1.00 35.33  ? 110 GLU D N   1 
ATOM   13598 C CA  . GLU D  1 110 ? -39.204  6.155   -45.569  1.00 33.56  ? 110 GLU D CA  1 
ATOM   13599 C C   . GLU D  1 110 ? -40.362  5.514   -44.795  1.00 32.52  ? 110 GLU D C   1 
ATOM   13600 O O   . GLU D  1 110 ? -40.273  4.363   -44.373  1.00 32.28  ? 110 GLU D O   1 
ATOM   13601 C CB  . GLU D  1 110 ? -38.298  7.038   -44.704  1.00 31.16  ? 110 GLU D CB  1 
ATOM   13602 C CG  . GLU D  1 110 ? -37.751  6.354   -43.457  1.00 30.45  ? 110 GLU D CG  1 
ATOM   13603 C CD  . GLU D  1 110 ? -36.998  5.046   -43.681  1.00 32.21  ? 110 GLU D CD  1 
ATOM   13604 O OE1 . GLU D  1 110 ? -36.530  4.716   -44.806  1.00 33.15  ? 110 GLU D OE1 1 
ATOM   13605 O OE2 . GLU D  1 110 ? -36.911  4.312   -42.669  1.00 32.17  ? 110 GLU D OE2 1 
ATOM   13606 N N   . LEU D  1 111 ? -41.436  6.271   -44.569  1.00 31.15  ? 111 LEU D N   1 
ATOM   13607 C CA  . LEU D  1 111 ? -42.585  5.739   -43.860  1.00 31.45  ? 111 LEU D CA  1 
ATOM   13608 C C   . LEU D  1 111 ? -43.164  4.544   -44.634  1.00 32.72  ? 111 LEU D C   1 
ATOM   13609 O O   . LEU D  1 111 ? -43.414  3.498   -44.044  1.00 31.83  ? 111 LEU D O   1 
ATOM   13610 C CB  . LEU D  1 111 ? -43.584  6.871   -43.637  1.00 31.00  ? 111 LEU D CB  1 
ATOM   13611 C CG  . LEU D  1 111 ? -44.854  6.536   -42.858  1.00 30.53  ? 111 LEU D CG  1 
ATOM   13612 C CD1 . LEU D  1 111 ? -44.570  5.948   -41.506  1.00 29.96  ? 111 LEU D CD1 1 
ATOM   13613 C CD2 . LEU D  1 111 ? -45.718  7.775   -42.728  1.00 30.00  ? 111 LEU D CD2 1 
ATOM   13614 N N   . LYS D  1 112 ? -43.291  4.667   -45.955  1.00 33.72  ? 112 LYS D N   1 
ATOM   13615 C CA  . LYS D  1 112 ? -43.806  3.585   -46.769  1.00 37.92  ? 112 LYS D CA  1 
ATOM   13616 C C   . LYS D  1 112 ? -42.866  2.374   -46.769  1.00 39.05  ? 112 LYS D C   1 
ATOM   13617 O O   . LYS D  1 112 ? -43.312  1.224   -46.690  1.00 38.05  ? 112 LYS D O   1 
ATOM   13618 C CB  . LYS D  1 112 ? -44.014  4.047   -48.214  1.00 40.32  ? 112 LYS D CB  1 
ATOM   13619 C CG  . LYS D  1 112 ? -45.170  5.019   -48.411  1.00 41.22  ? 112 LYS D CG  1 
ATOM   13620 C CD  . LYS D  1 112 ? -45.402  5.341   -49.879  1.00 43.60  ? 112 LYS D CD  1 
ATOM   13621 C CE  . LYS D  1 112 ? -46.442  6.396   -49.988  1.00 46.82  ? 112 LYS D CE  1 
ATOM   13622 N NZ  . LYS D  1 112 ? -46.492  6.898   -51.355  1.00 49.85  ? 112 LYS D NZ  1 
ATOM   13623 N N   . ARG D  1 113 ? -41.559  2.625   -46.891  1.00 39.44  ? 113 ARG D N   1 
ATOM   13624 C CA  . ARG D  1 113 ? -40.611  1.529   -46.889  1.00 39.59  ? 113 ARG D CA  1 
ATOM   13625 C C   . ARG D  1 113 ? -40.838  0.700   -45.630  1.00 38.78  ? 113 ARG D C   1 
ATOM   13626 O O   . ARG D  1 113 ? -40.799  -0.516  -45.685  1.00 43.24  ? 113 ARG D O   1 
ATOM   13627 C CB  . ARG D  1 113 ? -39.163  2.018   -46.982  1.00 40.02  ? 113 ARG D CB  1 
ATOM   13628 C CG  . ARG D  1 113 ? -38.120  0.906   -46.901  1.00 39.85  ? 113 ARG D CG  1 
ATOM   13629 C CD  . ARG D  1 113 ? -36.689  1.411   -46.650  1.00 38.94  ? 113 ARG D CD  1 
ATOM   13630 N NE  . ARG D  1 113 ? -36.439  1.856   -45.268  1.00 36.94  ? 113 ARG D NE  1 
ATOM   13631 C CZ  . ARG D  1 113 ? -36.325  1.059   -44.216  1.00 34.83  ? 113 ARG D CZ  1 
ATOM   13632 N NH1 . ARG D  1 113 ? -36.438  -0.237  -44.375  1.00 35.59  ? 113 ARG D NH1 1 
ATOM   13633 N NH2 . ARG D  1 113 ? -36.145  1.547   -43.007  1.00 33.12  ? 113 ARG D NH2 1 
ATOM   13634 N N   . VAL D  1 114 ? -41.116  1.359   -44.512  1.00 36.76  ? 114 VAL D N   1 
ATOM   13635 C CA  . VAL D  1 114 ? -41.341  0.669   -43.255  1.00 37.37  ? 114 VAL D CA  1 
ATOM   13636 C C   . VAL D  1 114 ? -42.661  -0.105  -43.254  1.00 39.87  ? 114 VAL D C   1 
ATOM   13637 O O   . VAL D  1 114 ? -42.703  -1.256  -42.813  1.00 41.02  ? 114 VAL D O   1 
ATOM   13638 C CB  . VAL D  1 114 ? -41.292  1.689   -42.113  1.00 36.73  ? 114 VAL D CB  1 
ATOM   13639 C CG1 . VAL D  1 114 ? -41.707  1.075   -40.777  1.00 36.95  ? 114 VAL D CG1 1 
ATOM   13640 C CG2 . VAL D  1 114 ? -39.904  2.325   -42.016  1.00 37.43  ? 114 VAL D CG2 1 
ATOM   13641 N N   . LEU D  1 115 ? -43.741  0.538   -43.723  1.00 38.96  ? 115 LEU D N   1 
ATOM   13642 C CA  . LEU D  1 115 ? -45.076  -0.036  -43.661  1.00 37.54  ? 115 LEU D CA  1 
ATOM   13643 C C   . LEU D  1 115 ? -45.145  -1.278  -44.539  1.00 37.47  ? 115 LEU D C   1 
ATOM   13644 O O   . LEU D  1 115 ? -45.935  -2.180  -44.307  1.00 37.89  ? 115 LEU D O   1 
ATOM   13645 C CB  . LEU D  1 115 ? -46.130  0.973   -44.105  1.00 36.70  ? 115 LEU D CB  1 
ATOM   13646 C CG  . LEU D  1 115 ? -46.327  2.194   -43.203  1.00 36.29  ? 115 LEU D CG  1 
ATOM   13647 C CD1 . LEU D  1 115 ? -47.177  3.265   -43.884  1.00 35.94  ? 115 LEU D CD1 1 
ATOM   13648 C CD2 . LEU D  1 115 ? -46.974  1.791   -41.894  1.00 36.16  ? 115 LEU D CD2 1 
ATOM   13649 N N   . ASN D  1 116 ? -44.322  -1.309  -45.569  1.00 37.20  ? 116 ASN D N   1 
ATOM   13650 C CA  . ASN D  1 116 ? -44.360  -2.396  -46.524  1.00 38.35  ? 116 ASN D CA  1 
ATOM   13651 C C   . ASN D  1 116 ? -44.095  -3.765  -45.857  1.00 37.69  ? 116 ASN D C   1 
ATOM   13652 O O   . ASN D  1 116 ? -44.645  -4.766  -46.316  1.00 38.64  ? 116 ASN D O   1 
ATOM   13653 C CB  . ASN D  1 116 ? -43.392  -2.084  -47.656  1.00 39.41  ? 116 ASN D CB  1 
ATOM   13654 C CG  . ASN D  1 116 ? -43.536  -3.097  -48.753  1.00 42.74  ? 116 ASN D CG  1 
ATOM   13655 O OD1 . ASN D  1 116 ? -44.643  -3.258  -49.275  1.00 46.33  ? 116 ASN D OD1 1 
ATOM   13656 N ND2 . ASN D  1 116 ? -42.469  -3.819  -49.060  1.00 42.26  ? 116 ASN D ND2 1 
ATOM   13657 N N   . TYR D  1 117 ? -43.218  -3.830  -44.837  1.00 35.29  ? 117 TYR D N   1 
ATOM   13658 C CA  . TYR D  1 117 ? -42.989  -5.053  -44.077  1.00 35.87  ? 117 TYR D CA  1 
ATOM   13659 C C   . TYR D  1 117 ? -43.717  -4.968  -42.730  1.00 35.62  ? 117 TYR D C   1 
ATOM   13660 O O   . TYR D  1 117 ? -44.232  -5.993  -42.241  1.00 34.60  ? 117 TYR D O   1 
ATOM   13661 C CB  . TYR D  1 117 ? -41.514  -5.436  -43.860  1.00 35.64  ? 117 TYR D CB  1 
ATOM   13662 C CG  . TYR D  1 117 ? -40.674  -4.399  -43.131  1.00 35.22  ? 117 TYR D CG  1 
ATOM   13663 C CD1 . TYR D  1 117 ? -40.695  -4.303  -41.757  1.00 34.27  ? 117 TYR D CD1 1 
ATOM   13664 C CD2 . TYR D  1 117 ? -39.875  -3.492  -43.821  1.00 35.91  ? 117 TYR D CD2 1 
ATOM   13665 C CE1 . TYR D  1 117 ? -39.941  -3.350  -41.095  1.00 34.04  ? 117 TYR D CE1 1 
ATOM   13666 C CE2 . TYR D  1 117 ? -39.105  -2.550  -43.172  1.00 34.26  ? 117 TYR D CE2 1 
ATOM   13667 C CZ  . TYR D  1 117 ? -39.132  -2.478  -41.802  1.00 34.51  ? 117 TYR D CZ  1 
ATOM   13668 O OH  . TYR D  1 117 ? -38.425  -1.502  -41.121  1.00 37.33  ? 117 TYR D OH  1 
ATOM   13669 N N   . ALA D  1 118 ? -43.777  -3.750  -42.142  1.00 33.93  ? 118 ALA D N   1 
ATOM   13670 C CA  . ALA D  1 118 ? -44.378  -3.571  -40.828  1.00 34.00  ? 118 ALA D CA  1 
ATOM   13671 C C   . ALA D  1 118 ? -45.837  -4.070  -40.785  1.00 34.74  ? 118 ALA D C   1 
ATOM   13672 O O   . ALA D  1 118 ? -46.305  -4.575  -39.757  1.00 33.19  ? 118 ALA D O   1 
ATOM   13673 C CB  . ALA D  1 118 ? -44.252  -2.125  -40.364  1.00 32.42  ? 118 ALA D CB  1 
ATOM   13674 N N   . LYS D  1 119 ? -46.557  -3.960  -41.906  1.00 36.51  ? 119 LYS D N   1 
ATOM   13675 C CA  . LYS D  1 119 ? -47.976  -4.298  -41.935  1.00 38.63  ? 119 LYS D CA  1 
ATOM   13676 C C   . LYS D  1 119 ? -48.235  -5.788  -41.687  1.00 39.13  ? 119 LYS D C   1 
ATOM   13677 O O   . LYS D  1 119 ? -49.382  -6.172  -41.544  1.00 40.44  ? 119 LYS D O   1 
ATOM   13678 C CB  . LYS D  1 119 ? -48.622  -3.852  -43.254  1.00 38.83  ? 119 LYS D CB  1 
ATOM   13679 C CG  . LYS D  1 119 ? -48.249  -4.662  -44.457  1.00 41.35  ? 119 LYS D CG  1 
ATOM   13680 C CD  . LYS D  1 119 ? -48.703  -4.145  -45.815  1.00 44.06  ? 119 LYS D CD  1 
ATOM   13681 C CE  . LYS D  1 119 ? -48.239  -5.145  -46.835  1.00 48.24  ? 119 LYS D CE  1 
ATOM   13682 N NZ  . LYS D  1 119 ? -48.021  -4.601  -48.179  1.00 51.15  ? 119 LYS D NZ  1 
ATOM   13683 N N   . LYS D  1 120 ? -47.194  -6.629  -41.636  1.00 40.37  ? 120 LYS D N   1 
ATOM   13684 C CA  . LYS D  1 120 ? -47.374  -8.074  -41.489  1.00 40.77  ? 120 LYS D CA  1 
ATOM   13685 C C   . LYS D  1 120 ? -47.282  -8.489  -40.022  1.00 39.50  ? 120 LYS D C   1 
ATOM   13686 O O   . LYS D  1 120 ? -47.576  -9.647  -39.720  1.00 41.97  ? 120 LYS D O   1 
ATOM   13687 C CB  . LYS D  1 120 ? -46.337  -8.873  -42.293  1.00 41.80  ? 120 LYS D CB  1 
ATOM   13688 C CG  . LYS D  1 120 ? -46.319  -8.627  -43.799  1.00 43.88  ? 120 LYS D CG  1 
ATOM   13689 C CD  . LYS D  1 120 ? -45.365  -9.546  -44.548  1.00 46.34  ? 120 LYS D CD  1 
ATOM   13690 C CE  . LYS D  1 120 ? -43.949  -9.172  -44.265  1.00 47.87  ? 120 LYS D CE  1 
ATOM   13691 N NZ  . LYS D  1 120 ? -43.037  -9.979  -45.073  1.00 50.05  ? 120 LYS D NZ  1 
ATOM   13692 N N   . TYR D  1 121 ? -46.903  -7.544  -39.134  1.00 36.01  ? 121 TYR D N   1 
ATOM   13693 C CA  . TYR D  1 121 ? -46.748  -7.801  -37.712  1.00 34.63  ? 121 TYR D CA  1 
ATOM   13694 C C   . TYR D  1 121 ? -47.862  -7.100  -36.925  1.00 33.50  ? 121 TYR D C   1 
ATOM   13695 O O   . TYR D  1 121 ? -47.784  -5.908  -36.667  1.00 34.25  ? 121 TYR D O   1 
ATOM   13696 C CB  . TYR D  1 121 ? -45.288  -7.430  -37.387  1.00 34.48  ? 121 TYR D CB  1 
ATOM   13697 C CG  . TYR D  1 121 ? -44.282  -8.169  -38.257  1.00 35.78  ? 121 TYR D CG  1 
ATOM   13698 C CD1 . TYR D  1 121 ? -43.902  -9.482  -37.981  1.00 38.99  ? 121 TYR D CD1 1 
ATOM   13699 C CD2 . TYR D  1 121 ? -43.797  -7.597  -39.418  1.00 37.08  ? 121 TYR D CD2 1 
ATOM   13700 C CE1 . TYR D  1 121 ? -43.042  -10.187 -38.815  1.00 38.80  ? 121 TYR D CE1 1 
ATOM   13701 C CE2 . TYR D  1 121 ? -42.941  -8.282  -40.265  1.00 38.40  ? 121 TYR D CE2 1 
ATOM   13702 C CZ  . TYR D  1 121 ? -42.568  -9.579  -39.965  1.00 38.87  ? 121 TYR D CZ  1 
ATOM   13703 O OH  . TYR D  1 121 ? -41.723  -10.202 -40.823  1.00 39.82  ? 121 TYR D OH  1 
ATOM   13704 N N   . ASP D  1 122 ? -48.852  -7.853  -36.436  1.00 33.94  ? 122 ASP D N   1 
ATOM   13705 C CA  . ASP D  1 122 ? -50.012  -7.308  -35.735  1.00 33.75  ? 122 ASP D CA  1 
ATOM   13706 C C   . ASP D  1 122 ? -49.702  -7.113  -34.254  1.00 35.63  ? 122 ASP D C   1 
ATOM   13707 O O   . ASP D  1 122 ? -50.575  -6.667  -33.501  1.00 35.18  ? 122 ASP D O   1 
ATOM   13708 C CB  . ASP D  1 122 ? -51.275  -8.139  -35.924  1.00 34.08  ? 122 ASP D CB  1 
ATOM   13709 C CG  . ASP D  1 122 ? -51.272  -9.538  -35.303  1.00 34.54  ? 122 ASP D CG  1 
ATOM   13710 O OD1 . ASP D  1 122 ? -50.278  -9.940  -34.687  1.00 34.15  ? 122 ASP D OD1 1 
ATOM   13711 O OD2 . ASP D  1 122 ? -52.290  -10.224 -35.392  1.00 35.70  ? 122 ASP D OD2 1 
ATOM   13712 N N   . CYS D  1 123 ? -48.456  -7.409  -33.835  1.00 35.83  ? 123 CYS D N   1 
ATOM   13713 C CA  . CYS D  1 123 ? -47.975  -6.893  -32.556  1.00 35.25  ? 123 CYS D CA  1 
ATOM   13714 C C   . CYS D  1 123 ? -47.974  -5.355  -32.497  1.00 35.02  ? 123 CYS D C   1 
ATOM   13715 O O   . CYS D  1 123 ? -47.940  -4.766  -31.415  1.00 36.42  ? 123 CYS D O   1 
ATOM   13716 C CB  . CYS D  1 123 ? -46.596  -7.439  -32.196  1.00 36.13  ? 123 CYS D CB  1 
ATOM   13717 S SG  . CYS D  1 123 ? -45.202  -6.658  -33.048  1.00 37.16  ? 123 CYS D SG  1 
ATOM   13718 N N   . ILE D  1 124 ? -47.966  -4.672  -33.640  1.00 34.49  ? 124 ILE D N   1 
ATOM   13719 C CA  . ILE D  1 124 ? -48.006  -3.222  -33.612  1.00 34.10  ? 124 ILE D CA  1 
ATOM   13720 C C   . ILE D  1 124 ? -49.439  -2.763  -33.343  1.00 34.15  ? 124 ILE D C   1 
ATOM   13721 O O   . ILE D  1 124 ? -50.312  -3.112  -34.134  1.00 35.19  ? 124 ILE D O   1 
ATOM   13722 C CB  . ILE D  1 124 ? -47.484  -2.646  -34.936  1.00 34.59  ? 124 ILE D CB  1 
ATOM   13723 C CG1 . ILE D  1 124 ? -46.032  -3.035  -35.150  1.00 35.14  ? 124 ILE D CG1 1 
ATOM   13724 C CG2 . ILE D  1 124 ? -47.692  -1.131  -34.974  1.00 33.24  ? 124 ILE D CG2 1 
ATOM   13725 C CD1 . ILE D  1 124 ? -45.489  -2.715  -36.524  1.00 35.30  ? 124 ILE D CD1 1 
ATOM   13726 N N   . ILE D  1 125 ? -49.649  -1.961  -32.273  1.00 32.62  ? 125 ILE D N   1 
ATOM   13727 C CA  . ILE D  1 125 ? -50.983  -1.517  -31.877  1.00 32.00  ? 125 ILE D CA  1 
ATOM   13728 C C   . ILE D  1 125 ? -51.135  -0.002  -31.982  1.00 32.32  ? 125 ILE D C   1 
ATOM   13729 O O   . ILE D  1 125 ? -52.256  0.475   -31.869  1.00 33.09  ? 125 ILE D O   1 
ATOM   13730 C CB  . ILE D  1 125 ? -51.385  -2.017  -30.468  1.00 30.34  ? 125 ILE D CB  1 
ATOM   13731 C CG1 . ILE D  1 125 ? -50.433  -1.571  -29.351  1.00 28.56  ? 125 ILE D CG1 1 
ATOM   13732 C CG2 . ILE D  1 125 ? -51.559  -3.537  -30.483  1.00 30.93  ? 125 ILE D CG2 1 
ATOM   13733 C CD1 . ILE D  1 125 ? -50.965  -1.745  -27.930  1.00 26.80  ? 125 ILE D CD1 1 
ATOM   13734 N N   . THR D  1 126 ? -50.037  0.750   -32.144  1.00 31.11  ? 126 THR D N   1 
ATOM   13735 C CA  . THR D  1 126 ? -50.121  2.175   -32.424  1.00 30.93  ? 126 THR D CA  1 
ATOM   13736 C C   . THR D  1 126 ? -48.813  2.635   -33.090  1.00 33.41  ? 126 THR D C   1 
ATOM   13737 O O   . THR D  1 126 ? -47.735  2.058   -32.820  1.00 32.95  ? 126 THR D O   1 
ATOM   13738 C CB  . THR D  1 126 ? -50.376  2.973   -31.145  1.00 29.26  ? 126 THR D CB  1 
ATOM   13739 O OG1 . THR D  1 126 ? -51.643  2.670   -30.587  1.00 28.51  ? 126 THR D OG1 1 
ATOM   13740 C CG2 . THR D  1 126 ? -50.310  4.477   -31.358  1.00 28.47  ? 126 THR D CG2 1 
ATOM   13741 N N   . TYR D  1 127 ? -48.944  3.670   -33.953  1.00 31.53  ? 127 TYR D N   1 
ATOM   13742 C CA  . TYR D  1 127 ? -47.822  4.381   -34.552  1.00 32.13  ? 127 TYR D CA  1 
ATOM   13743 C C   . TYR D  1 127 ? -47.795  5.815   -34.030  1.00 32.06  ? 127 TYR D C   1 
ATOM   13744 O O   . TYR D  1 127 ? -48.833  6.485   -33.968  1.00 33.86  ? 127 TYR D O   1 
ATOM   13745 C CB  . TYR D  1 127 ? -47.899  4.533   -36.077  1.00 32.33  ? 127 TYR D CB  1 
ATOM   13746 C CG  . TYR D  1 127 ? -47.624  3.266   -36.872  1.00 32.04  ? 127 TYR D CG  1 
ATOM   13747 C CD1 . TYR D  1 127 ? -48.641  2.344   -37.121  1.00 30.55  ? 127 TYR D CD1 1 
ATOM   13748 C CD2 . TYR D  1 127 ? -46.353  3.000   -37.376  1.00 31.85  ? 127 TYR D CD2 1 
ATOM   13749 C CE1 . TYR D  1 127 ? -48.408  1.207   -37.871  1.00 31.63  ? 127 TYR D CE1 1 
ATOM   13750 C CE2 . TYR D  1 127 ? -46.091  1.824   -38.070  1.00 33.04  ? 127 TYR D CE2 1 
ATOM   13751 C CZ  . TYR D  1 127 ? -47.124  0.934   -38.325  1.00 33.09  ? 127 TYR D CZ  1 
ATOM   13752 O OH  . TYR D  1 127 ? -46.887  -0.211  -39.029  1.00 34.89  ? 127 TYR D OH  1 
ATOM   13753 N N   . LEU D  1 128 ? -46.598  6.285   -33.711  1.00 30.29  ? 128 LEU D N   1 
ATOM   13754 C CA  . LEU D  1 128 ? -46.382  7.665   -33.321  1.00 29.86  ? 128 LEU D CA  1 
ATOM   13755 C C   . LEU D  1 128 ? -45.607  8.345   -34.424  1.00 30.44  ? 128 LEU D C   1 
ATOM   13756 O O   . LEU D  1 128 ? -44.495  7.933   -34.752  1.00 31.80  ? 128 LEU D O   1 
ATOM   13757 C CB  . LEU D  1 128 ? -45.602  7.772   -32.023  1.00 28.96  ? 128 LEU D CB  1 
ATOM   13758 C CG  . LEU D  1 128 ? -46.209  7.018   -30.861  1.00 28.75  ? 128 LEU D CG  1 
ATOM   13759 C CD1 . LEU D  1 128 ? -45.264  7.155   -29.718  1.00 29.44  ? 128 LEU D CD1 1 
ATOM   13760 C CD2 . LEU D  1 128 ? -47.586  7.526   -30.567  1.00 29.14  ? 128 LEU D CD2 1 
ATOM   13761 N N   . VAL D  1 129 ? -46.201  9.395   -34.989  1.00 30.92  ? 129 VAL D N   1 
ATOM   13762 C CA  . VAL D  1 129 ? -45.756  9.840   -36.294  1.00 30.58  ? 129 VAL D CA  1 
ATOM   13763 C C   . VAL D  1 129 ? -44.707  10.950  -36.182  1.00 31.74  ? 129 VAL D C   1 
ATOM   13764 O O   . VAL D  1 129 ? -44.031  11.254  -37.159  1.00 32.56  ? 129 VAL D O   1 
ATOM   13765 C CB  . VAL D  1 129 ? -46.999  10.225  -37.096  1.00 30.93  ? 129 VAL D CB  1 
ATOM   13766 C CG1 . VAL D  1 129 ? -47.528  11.604  -36.728  1.00 31.65  ? 129 VAL D CG1 1 
ATOM   13767 C CG2 . VAL D  1 129 ? -46.719  10.118  -38.572  1.00 32.37  ? 129 VAL D CG2 1 
ATOM   13768 N N   . ILE D  1 130 ? -44.557  11.555  -35.003  1.00 30.32  ? 130 ILE D N   1 
ATOM   13769 C CA  . ILE D  1 130 ? -43.488  12.503  -34.798  1.00 31.26  ? 130 ILE D CA  1 
ATOM   13770 C C   . ILE D  1 130 ? -43.292  12.677  -33.300  1.00 31.76  ? 130 ILE D C   1 
ATOM   13771 O O   . ILE D  1 130 ? -44.239  12.540  -32.515  1.00 31.77  ? 130 ILE D O   1 
ATOM   13772 C CB  . ILE D  1 130 ? -43.816  13.843  -35.491  1.00 34.56  ? 130 ILE D CB  1 
ATOM   13773 C CG1 . ILE D  1 130 ? -42.626  14.816  -35.473  1.00 33.60  ? 130 ILE D CG1 1 
ATOM   13774 C CG2 . ILE D  1 130 ? -45.073  14.471  -34.871  1.00 34.31  ? 130 ILE D CG2 1 
ATOM   13775 C CD1 . ILE D  1 130 ? -42.826  16.056  -36.333  1.00 33.99  ? 130 ILE D CD1 1 
ATOM   13776 N N   . ASN D  1 131 ? -42.061  13.074  -32.958  1.00 33.41  ? 131 ASN D N   1 
ATOM   13777 C CA  . ASN D  1 131 ? -41.578  13.241  -31.598  1.00 32.09  ? 131 ASN D CA  1 
ATOM   13778 C C   . ASN D  1 131 ? -41.262  14.706  -31.291  1.00 30.48  ? 131 ASN D C   1 
ATOM   13779 O O   . ASN D  1 131 ? -40.177  15.202  -31.584  1.00 32.18  ? 131 ASN D O   1 
ATOM   13780 C CB  . ASN D  1 131 ? -40.327  12.390  -31.382  1.00 30.14  ? 131 ASN D CB  1 
ATOM   13781 C CG  . ASN D  1 131 ? -39.911  12.378  -29.933  1.00 30.78  ? 131 ASN D CG  1 
ATOM   13782 O OD1 . ASN D  1 131 ? -40.747  12.213  -29.045  1.00 35.33  ? 131 ASN D OD1 1 
ATOM   13783 N ND2 . ASN D  1 131 ? -38.636  12.555  -29.647  1.00 33.66  ? 131 ASN D ND2 1 
ATOM   13784 N N   . GLU D  1 132 ? -42.180  15.375  -30.617  1.00 31.49  ? 132 GLU D N   1 
ATOM   13785 C CA  . GLU D  1 132 ? -41.855  16.570  -29.843  1.00 33.48  ? 132 GLU D CA  1 
ATOM   13786 C C   . GLU D  1 132 ? -41.608  17.806  -30.719  1.00 31.73  ? 132 GLU D C   1 
ATOM   13787 O O   . GLU D  1 132 ? -40.591  18.476  -30.600  1.00 32.21  ? 132 GLU D O   1 
ATOM   13788 C CB  . GLU D  1 132 ? -40.617  16.311  -28.969  1.00 33.48  ? 132 GLU D CB  1 
ATOM   13789 C CG  . GLU D  1 132 ? -40.649  17.089  -27.649  1.00 33.65  ? 132 GLU D CG  1 
ATOM   13790 C CD  . GLU D  1 132 ? -41.841  16.672  -26.782  1.00 35.32  ? 132 GLU D CD  1 
ATOM   13791 O OE1 . GLU D  1 132 ? -41.744  15.596  -26.090  1.00 33.24  ? 132 GLU D OE1 1 
ATOM   13792 O OE2 . GLU D  1 132 ? -42.873  17.408  -26.852  1.00 29.73  ? 132 GLU D OE2 1 
ATOM   13793 N N   . PRO D  1 133 ? -42.531  18.190  -31.609  1.00 31.02  ? 133 PRO D N   1 
ATOM   13794 C CA  . PRO D  1 133 ? -42.408  19.464  -32.311  1.00 31.08  ? 133 PRO D CA  1 
ATOM   13795 C C   . PRO D  1 133 ? -42.503  20.610  -31.315  1.00 30.21  ? 133 PRO D C   1 
ATOM   13796 O O   . PRO D  1 133 ? -43.422  20.663  -30.522  1.00 29.45  ? 133 PRO D O   1 
ATOM   13797 C CB  . PRO D  1 133 ? -43.568  19.441  -33.313  1.00 30.84  ? 133 PRO D CB  1 
ATOM   13798 C CG  . PRO D  1 133 ? -44.608  18.578  -32.654  1.00 30.45  ? 133 PRO D CG  1 
ATOM   13799 C CD  . PRO D  1 133 ? -43.773  17.473  -31.945  1.00 31.93  ? 133 PRO D CD  1 
ATOM   13800 N N   . GLN D  1 134 ? -41.510  21.499  -31.347  1.00 33.85  ? 134 GLN D N   1 
ATOM   13801 C CA  . GLN D  1 134 ? -41.430  22.630  -30.438  1.00 33.43  ? 134 GLN D CA  1 
ATOM   13802 C C   . GLN D  1 134 ? -42.307  23.785  -30.907  1.00 28.84  ? 134 GLN D C   1 
ATOM   13803 O O   . GLN D  1 134 ? -42.348  24.088  -32.088  1.00 25.70  ? 134 GLN D O   1 
ATOM   13804 C CB  . GLN D  1 134 ? -39.965  23.077  -30.411  1.00 40.66  ? 134 GLN D CB  1 
ATOM   13805 C CG  . GLN D  1 134 ? -39.058  22.119  -29.645  1.00 44.00  ? 134 GLN D CG  1 
ATOM   13806 C CD  . GLN D  1 134 ? -39.321  22.188  -28.160  1.00 49.82  ? 134 GLN D CD  1 
ATOM   13807 O OE1 . GLN D  1 134 ? -39.967  23.109  -27.615  1.00 49.44  ? 134 GLN D OE1 1 
ATOM   13808 N NE2 . GLN D  1 134 ? -38.836  21.152  -27.512  1.00 50.79  ? 134 GLN D NE2 1 
ATOM   13809 N N   . THR D  1 135 ? -42.922  24.476  -29.943  1.00 27.94  ? 135 THR D N   1 
ATOM   13810 C CA  . THR D  1 135 ? -43.789  25.607  -30.204  1.00 28.98  ? 135 THR D CA  1 
ATOM   13811 C C   . THR D  1 135 ? -43.160  26.583  -31.192  1.00 28.89  ? 135 THR D C   1 
ATOM   13812 O O   . THR D  1 135 ? -43.793  26.988  -32.161  1.00 29.36  ? 135 THR D O   1 
ATOM   13813 C CB  . THR D  1 135 ? -44.102  26.326  -28.889  1.00 29.17  ? 135 THR D CB  1 
ATOM   13814 O OG1 . THR D  1 135 ? -44.369  25.299  -27.932  1.00 27.32  ? 135 THR D OG1 1 
ATOM   13815 C CG2 . THR D  1 135 ? -45.242  27.320  -29.054  1.00 28.50  ? 135 THR D CG2 1 
ATOM   13816 N N   . ASP D  1 136 ? -41.919  27.001  -30.939  1.00 30.52  ? 136 ASP D N   1 
ATOM   13817 C CA  . ASP D  1 136 ? -41.319  28.073  -31.733  1.00 29.86  ? 136 ASP D CA  1 
ATOM   13818 C C   . ASP D  1 136 ? -41.057  27.609  -33.162  1.00 29.58  ? 136 ASP D C   1 
ATOM   13819 O O   . ASP D  1 136 ? -41.189  28.373  -34.109  1.00 32.16  ? 136 ASP D O   1 
ATOM   13820 C CB  . ASP D  1 136 ? -40.018  28.573  -31.141  1.00 30.37  ? 136 ASP D CB  1 
ATOM   13821 C CG  . ASP D  1 136 ? -39.533  29.857  -31.785  1.00 33.11  ? 136 ASP D CG  1 
ATOM   13822 O OD1 . ASP D  1 136 ? -40.155  30.901  -31.460  1.00 31.79  ? 136 ASP D OD1 1 
ATOM   13823 O OD2 . ASP D  1 136 ? -38.550  29.789  -32.594  1.00 32.80  ? 136 ASP D OD2 1 
ATOM   13824 N N   . HIS D  1 137 ? -40.686  26.337  -33.314  1.00 28.42  ? 137 HIS D N   1 
ATOM   13825 C CA  . HIS D  1 137 ? -40.375  25.792  -34.614  1.00 27.92  ? 137 HIS D CA  1 
ATOM   13826 C C   . HIS D  1 137 ? -41.636  25.746  -35.454  1.00 27.36  ? 137 HIS D C   1 
ATOM   13827 O O   . HIS D  1 137 ? -41.629  26.163  -36.613  1.00 29.03  ? 137 HIS D O   1 
ATOM   13828 C CB  . HIS D  1 137 ? -39.687  24.429  -34.468  1.00 28.00  ? 137 HIS D CB  1 
ATOM   13829 C CG  . HIS D  1 137 ? -39.402  23.824  -35.777  1.00 28.07  ? 137 HIS D CG  1 
ATOM   13830 N ND1 . HIS D  1 137 ? -38.508  24.395  -36.653  1.00 29.09  ? 137 HIS D ND1 1 
ATOM   13831 C CD2 . HIS D  1 137 ? -39.903  22.748  -36.387  1.00 29.59  ? 137 HIS D CD2 1 
ATOM   13832 C CE1 . HIS D  1 137 ? -38.455  23.648  -37.754  1.00 30.13  ? 137 HIS D CE1 1 
ATOM   13833 N NE2 . HIS D  1 137 ? -39.278  22.627  -37.607  1.00 29.48  ? 137 HIS D NE2 1 
ATOM   13834 N N   . ILE D  1 138 ? -42.732  25.295  -34.848  1.00 27.59  ? 138 ILE D N   1 
ATOM   13835 C CA  . ILE D  1 138 ? -44.013  25.258  -35.557  1.00 28.43  ? 138 ILE D CA  1 
ATOM   13836 C C   . ILE D  1 138 ? -44.417  26.671  -36.033  1.00 29.13  ? 138 ILE D C   1 
ATOM   13837 O O   . ILE D  1 138 ? -44.793  26.874  -37.200  1.00 32.88  ? 138 ILE D O   1 
ATOM   13838 C CB  . ILE D  1 138 ? -45.101  24.580  -34.703  1.00 27.49  ? 138 ILE D CB  1 
ATOM   13839 C CG1 . ILE D  1 138 ? -44.738  23.112  -34.354  1.00 26.79  ? 138 ILE D CG1 1 
ATOM   13840 C CG2 . ILE D  1 138 ? -46.438  24.673  -35.427  1.00 28.22  ? 138 ILE D CG2 1 
ATOM   13841 C CD1 . ILE D  1 138 ? -45.863  22.290  -33.735  1.00 26.57  ? 138 ILE D CD1 1 
ATOM   13842 N N   . HIS D  1 139 ? -44.335  27.671  -35.150  1.00 28.60  ? 139 HIS D N   1 
ATOM   13843 C CA  . HIS D  1 139 ? -44.636  29.044  -35.525  1.00 29.21  ? 139 HIS D CA  1 
ATOM   13844 C C   . HIS D  1 139 ? -43.779  29.430  -36.720  1.00 28.36  ? 139 HIS D C   1 
ATOM   13845 O O   . HIS D  1 139 ? -44.259  30.068  -37.652  1.00 26.83  ? 139 HIS D O   1 
ATOM   13846 C CB  . HIS D  1 139 ? -44.366  29.991  -34.349  1.00 30.94  ? 139 HIS D CB  1 
ATOM   13847 C CG  . HIS D  1 139 ? -44.582  31.424  -34.666  1.00 32.37  ? 139 HIS D CG  1 
ATOM   13848 N ND1 . HIS D  1 139 ? -43.593  32.253  -35.171  1.00 33.44  ? 139 HIS D ND1 1 
ATOM   13849 C CD2 . HIS D  1 139 ? -45.703  32.171  -34.572  1.00 33.68  ? 139 HIS D CD2 1 
ATOM   13850 C CE1 . HIS D  1 139 ? -44.108  33.477  -35.325  1.00 34.26  ? 139 HIS D CE1 1 
ATOM   13851 N NE2 . HIS D  1 139 ? -45.388  33.452  -34.982  1.00 34.30  ? 139 HIS D NE2 1 
ATOM   13852 N N   . SER D  1 140 ? -42.504  29.015  -36.697  1.00 29.29  ? 140 SER D N   1 
ATOM   13853 C CA  . SER D  1 140 ? -41.550  29.429  -37.722  1.00 30.86  ? 140 SER D CA  1 
ATOM   13854 C C   . SER D  1 140 ? -41.888  28.837  -39.098  1.00 33.16  ? 140 SER D C   1 
ATOM   13855 O O   . SER D  1 140 ? -41.982  29.568  -40.087  1.00 38.14  ? 140 SER D O   1 
ATOM   13856 C CB  . SER D  1 140 ? -40.133  29.131  -37.287  1.00 31.02  ? 140 SER D CB  1 
ATOM   13857 O OG  . SER D  1 140 ? -39.216  29.644  -38.237  1.00 33.41  ? 140 SER D OG  1 
ATOM   13858 N N   . VAL D  1 141 ? -42.138  27.528  -39.182  1.00 32.61  ? 141 VAL D N   1 
ATOM   13859 C CA  . VAL D  1 141 ? -42.468  26.907  -40.462  1.00 32.22  ? 141 VAL D CA  1 
ATOM   13860 C C   . VAL D  1 141 ? -43.973  26.920  -40.776  1.00 31.87  ? 141 VAL D C   1 
ATOM   13861 O O   . VAL D  1 141 ? -44.355  26.402  -41.828  1.00 29.90  ? 141 VAL D O   1 
ATOM   13862 C CB  . VAL D  1 141 ? -41.906  25.465  -40.456  1.00 33.10  ? 141 VAL D CB  1 
ATOM   13863 C CG1 . VAL D  1 141 ? -40.389  25.466  -40.210  1.00 33.34  ? 141 VAL D CG1 1 
ATOM   13864 C CG2 . VAL D  1 141 ? -42.631  24.518  -39.486  1.00 31.20  ? 141 VAL D CG2 1 
ATOM   13865 N N   . THR D  1 142 ? -44.796  27.472  -39.847  1.00 31.21  ? 142 THR D N   1 
ATOM   13866 C CA  . THR D  1 142 ? -46.249  27.656  -39.930  1.00 30.72  ? 142 THR D CA  1 
ATOM   13867 C C   . THR D  1 142 ? -46.962  26.400  -39.421  1.00 32.10  ? 142 THR D C   1 
ATOM   13868 O O   . THR D  1 142 ? -46.546  25.266  -39.685  1.00 30.17  ? 142 THR D O   1 
ATOM   13869 C CB  . THR D  1 142 ? -46.812  28.064  -41.298  1.00 29.83  ? 142 THR D CB  1 
ATOM   13870 O OG1 . THR D  1 142 ? -46.853  26.939  -42.165  1.00 29.36  ? 142 THR D OG1 1 
ATOM   13871 C CG2 . THR D  1 142 ? -46.031  29.177  -41.980  1.00 29.40  ? 142 THR D CG2 1 
ATOM   13872 N N   . GLY D  1 143 ? -48.049  26.639  -38.674  1.00 31.28  ? 143 GLY D N   1 
ATOM   13873 C CA  . GLY D  1 143 ? -48.919  25.571  -38.228  1.00 31.14  ? 143 GLY D CA  1 
ATOM   13874 C C   . GLY D  1 143 ? -49.626  24.866  -39.384  1.00 32.07  ? 143 GLY D C   1 
ATOM   13875 O O   . GLY D  1 143 ? -49.936  23.674  -39.288  1.00 32.12  ? 143 GLY D O   1 
ATOM   13876 N N   . LYS D  1 144 ? -49.916  25.590  -40.469  1.00 31.49  ? 144 LYS D N   1 
ATOM   13877 C CA  . LYS D  1 144 ? -50.429  24.936  -41.656  1.00 33.38  ? 144 LYS D CA  1 
ATOM   13878 C C   . LYS D  1 144 ? -49.512  23.779  -42.059  1.00 33.76  ? 144 LYS D C   1 
ATOM   13879 O O   . LYS D  1 144 ? -49.970  22.651  -42.228  1.00 32.77  ? 144 LYS D O   1 
ATOM   13880 C CB  . LYS D  1 144 ? -50.526  25.861  -42.866  1.00 35.65  ? 144 LYS D CB  1 
ATOM   13881 C CG  . LYS D  1 144 ? -51.490  25.340  -43.916  1.00 37.78  ? 144 LYS D CG  1 
ATOM   13882 C CD  . LYS D  1 144 ? -51.448  26.148  -45.208  1.00 40.99  ? 144 LYS D CD  1 
ATOM   13883 C CE  . LYS D  1 144 ? -52.450  25.679  -46.235  1.00 45.31  ? 144 LYS D CE  1 
ATOM   13884 N NZ  . LYS D  1 144 ? -52.668  24.226  -46.237  1.00 45.27  ? 144 LYS D NZ  1 
ATOM   13885 N N   . ALA D  1 145 ? -48.218  24.086  -42.221  1.00 31.59  ? 145 ALA D N   1 
ATOM   13886 C CA  . ALA D  1 145 ? -47.273  23.148  -42.770  1.00 30.91  ? 145 ALA D CA  1 
ATOM   13887 C C   . ALA D  1 145 ? -47.258  21.899  -41.899  1.00 32.21  ? 145 ALA D C   1 
ATOM   13888 O O   . ALA D  1 145 ? -47.210  20.784  -42.440  1.00 29.98  ? 145 ALA D O   1 
ATOM   13889 C CB  . ALA D  1 145 ? -45.901  23.783  -42.897  1.00 30.68  ? 145 ALA D CB  1 
ATOM   13890 N N   . PHE D  1 146 ? -47.315  22.123  -40.568  1.00 32.66  ? 146 PHE D N   1 
ATOM   13891 C CA  . PHE D  1 146 ? -47.322  21.057  -39.573  1.00 32.54  ? 146 PHE D CA  1 
ATOM   13892 C C   . PHE D  1 146 ? -48.562  20.169  -39.745  1.00 33.26  ? 146 PHE D C   1 
ATOM   13893 O O   . PHE D  1 146 ? -48.463  18.942  -39.816  1.00 36.06  ? 146 PHE D O   1 
ATOM   13894 C CB  . PHE D  1 146 ? -47.224  21.650  -38.160  1.00 31.55  ? 146 PHE D CB  1 
ATOM   13895 C CG  . PHE D  1 146 ? -47.505  20.611  -37.092  1.00 31.87  ? 146 PHE D CG  1 
ATOM   13896 C CD1 . PHE D  1 146 ? -46.538  19.673  -36.748  1.00 31.92  ? 146 PHE D CD1 1 
ATOM   13897 C CD2 . PHE D  1 146 ? -48.757  20.515  -36.494  1.00 31.57  ? 146 PHE D CD2 1 
ATOM   13898 C CE1 . PHE D  1 146 ? -46.811  18.676  -35.831  1.00 30.36  ? 146 PHE D CE1 1 
ATOM   13899 C CE2 . PHE D  1 146 ? -49.006  19.522  -35.564  1.00 31.34  ? 146 PHE D CE2 1 
ATOM   13900 C CZ  . PHE D  1 146 ? -48.036  18.598  -35.250  1.00 30.89  ? 146 PHE D CZ  1 
ATOM   13901 N N   . VAL D  1 147 ? -49.737  20.780  -39.838  1.00 32.64  ? 147 VAL D N   1 
ATOM   13902 C CA  . VAL D  1 147 ? -50.978  20.021  -39.907  1.00 33.04  ? 147 VAL D CA  1 
ATOM   13903 C C   . VAL D  1 147 ? -51.039  19.266  -41.231  1.00 33.48  ? 147 VAL D C   1 
ATOM   13904 O O   . VAL D  1 147 ? -51.475  18.121  -41.285  1.00 33.63  ? 147 VAL D O   1 
ATOM   13905 C CB  . VAL D  1 147 ? -52.185  20.963  -39.731  1.00 32.74  ? 147 VAL D CB  1 
ATOM   13906 C CG1 . VAL D  1 147 ? -53.505  20.298  -40.111  1.00 33.33  ? 147 VAL D CG1 1 
ATOM   13907 C CG2 . VAL D  1 147 ? -52.245  21.508  -38.311  1.00 31.78  ? 147 VAL D CG2 1 
ATOM   13908 N N   . ASP D  1 148 ? -50.620  19.903  -42.322  1.00 33.18  ? 148 ASP D N   1 
ATOM   13909 C CA  . ASP D  1 148 ? -50.560  19.196  -43.596  1.00 32.70  ? 148 ASP D CA  1 
ATOM   13910 C C   . ASP D  1 148 ? -49.650  17.971  -43.492  1.00 31.71  ? 148 ASP D C   1 
ATOM   13911 O O   . ASP D  1 148 ? -49.981  16.914  -44.029  1.00 30.79  ? 148 ASP D O   1 
ATOM   13912 C CB  . ASP D  1 148 ? -50.188  20.112  -44.750  1.00 32.31  ? 148 ASP D CB  1 
ATOM   13913 C CG  . ASP D  1 148 ? -51.266  21.137  -45.077  1.00 33.08  ? 148 ASP D CG  1 
ATOM   13914 O OD1 . ASP D  1 148 ? -52.355  20.992  -44.520  1.00 32.27  ? 148 ASP D OD1 1 
ATOM   13915 O OD2 . ASP D  1 148 ? -50.992  22.096  -45.855  1.00 34.35  ? 148 ASP D OD2 1 
ATOM   13916 N N   . LEU D  1 149 ? -48.495  18.123  -42.830  1.00 31.15  ? 149 LEU D N   1 
ATOM   13917 C CA  . LEU D  1 149 ? -47.550  17.027  -42.717  1.00 31.78  ? 149 LEU D CA  1 
ATOM   13918 C C   . LEU D  1 149 ? -48.228  15.898  -41.922  1.00 32.47  ? 149 LEU D C   1 
ATOM   13919 O O   . LEU D  1 149 ? -48.220  14.752  -42.331  1.00 32.23  ? 149 LEU D O   1 
ATOM   13920 C CB  . LEU D  1 149 ? -46.223  17.437  -42.091  1.00 29.93  ? 149 LEU D CB  1 
ATOM   13921 C CG  . LEU D  1 149 ? -45.209  16.308  -41.840  1.00 30.08  ? 149 LEU D CG  1 
ATOM   13922 C CD1 . LEU D  1 149 ? -44.701  15.762  -43.151  1.00 31.52  ? 149 LEU D CD1 1 
ATOM   13923 C CD2 . LEU D  1 149 ? -43.997  16.740  -40.985  1.00 28.86  ? 149 LEU D CD2 1 
ATOM   13924 N N   . MET D  1 150 ? -48.849  16.238  -40.800  1.00 32.90  ? 150 MET D N   1 
ATOM   13925 C CA  . MET D  1 150 ? -49.448  15.233  -39.956  1.00 32.76  ? 150 MET D CA  1 
ATOM   13926 C C   . MET D  1 150 ? -50.495  14.466  -40.738  1.00 33.51  ? 150 MET D C   1 
ATOM   13927 O O   . MET D  1 150 ? -50.435  13.241  -40.787  1.00 31.77  ? 150 MET D O   1 
ATOM   13928 C CB  . MET D  1 150 ? -50.072  15.861  -38.719  1.00 32.16  ? 150 MET D CB  1 
ATOM   13929 C CG  . MET D  1 150 ? -49.037  16.430  -37.770  1.00 31.67  ? 150 MET D CG  1 
ATOM   13930 S SD  . MET D  1 150 ? -47.876  15.229  -37.102  1.00 31.10  ? 150 MET D SD  1 
ATOM   13931 C CE  . MET D  1 150 ? -46.486  15.485  -38.219  1.00 29.17  ? 150 MET D CE  1 
ATOM   13932 N N   . ASN D  1 151 ? -51.401  15.197  -41.377  1.00 32.95  ? 151 ASN D N   1 
ATOM   13933 C CA  . ASN D  1 151 ? -52.454  14.544  -42.129  1.00 35.05  ? 151 ASN D CA  1 
ATOM   13934 C C   . ASN D  1 151 ? -51.890  13.586  -43.185  1.00 37.04  ? 151 ASN D C   1 
ATOM   13935 O O   . ASN D  1 151 ? -52.445  12.505  -43.429  1.00 35.86  ? 151 ASN D O   1 
ATOM   13936 C CB  . ASN D  1 151 ? -53.388  15.550  -42.793  1.00 34.93  ? 151 ASN D CB  1 
ATOM   13937 C CG  . ASN D  1 151 ? -54.383  16.098  -41.810  1.00 35.80  ? 151 ASN D CG  1 
ATOM   13938 O OD1 . ASN D  1 151 ? -54.745  17.279  -41.865  1.00 38.86  ? 151 ASN D OD1 1 
ATOM   13939 N ND2 . ASN D  1 151 ? -54.815  15.262  -40.885  1.00 37.41  ? 151 ASN D ND2 1 
ATOM   13940 N N   . THR D  1 152 ? -50.846  14.041  -43.883  1.00 36.52  ? 152 THR D N   1 
ATOM   13941 C CA  . THR D  1 152 ? -50.278  13.267  -44.967  1.00 36.14  ? 152 THR D CA  1 
ATOM   13942 C C   . THR D  1 152 ? -49.784  11.943  -44.386  1.00 34.93  ? 152 THR D C   1 
ATOM   13943 O O   . THR D  1 152 ? -50.183  10.893  -44.871  1.00 37.87  ? 152 THR D O   1 
ATOM   13944 C CB  . THR D  1 152 ? -49.204  14.105  -45.655  1.00 36.20  ? 152 THR D CB  1 
ATOM   13945 O OG1 . THR D  1 152 ? -49.863  15.217  -46.256  1.00 37.02  ? 152 THR D OG1 1 
ATOM   13946 C CG2 . THR D  1 152 ? -48.522  13.393  -46.802  1.00 36.39  ? 152 THR D CG2 1 
ATOM   13947 N N   . LEU D  1 153 ? -49.016  11.994  -43.301  1.00 31.93  ? 153 LEU D N   1 
ATOM   13948 C CA  . LEU D  1 153 ? -48.425  10.795  -42.728  1.00 34.57  ? 153 LEU D CA  1 
ATOM   13949 C C   . LEU D  1 153 ? -49.478  9.902   -42.051  1.00 35.48  ? 153 LEU D C   1 
ATOM   13950 O O   . LEU D  1 153 ? -49.352  8.679   -42.046  1.00 35.16  ? 153 LEU D O   1 
ATOM   13951 C CB  . LEU D  1 153 ? -47.351  11.182  -41.719  1.00 33.36  ? 153 LEU D CB  1 
ATOM   13952 C CG  . LEU D  1 153 ? -46.277  12.151  -42.215  1.00 35.74  ? 153 LEU D CG  1 
ATOM   13953 C CD1 . LEU D  1 153 ? -45.225  12.404  -41.128  1.00 35.49  ? 153 LEU D CD1 1 
ATOM   13954 C CD2 . LEU D  1 153 ? -45.646  11.631  -43.504  1.00 37.35  ? 153 LEU D CD2 1 
ATOM   13955 N N   . ILE D  1 154 ? -50.500  10.505  -41.437  1.00 33.83  ? 154 ILE D N   1 
ATOM   13956 C CA  . ILE D  1 154 ? -51.582  9.726   -40.889  1.00 34.82  ? 154 ILE D CA  1 
ATOM   13957 C C   . ILE D  1 154 ? -52.253  8.905   -41.996  1.00 36.26  ? 154 ILE D C   1 
ATOM   13958 O O   . ILE D  1 154 ? -52.563  7.747   -41.762  1.00 35.62  ? 154 ILE D O   1 
ATOM   13959 C CB  . ILE D  1 154 ? -52.595  10.609  -40.140  1.00 33.88  ? 154 ILE D CB  1 
ATOM   13960 C CG1 . ILE D  1 154 ? -51.986  11.214  -38.924  1.00 32.79  ? 154 ILE D CG1 1 
ATOM   13961 C CG2 . ILE D  1 154 ? -53.853  9.808   -39.766  1.00 34.51  ? 154 ILE D CG2 1 
ATOM   13962 C CD1 . ILE D  1 154 ? -52.830  12.325  -38.327  1.00 34.74  ? 154 ILE D CD1 1 
ATOM   13963 N N   . ASN D  1 155 ? -52.520  9.514   -43.161  1.00 37.22  ? 155 ASN D N   1 
ATOM   13964 C CA  . ASN D  1 155 ? -53.262  8.839   -44.212  1.00 40.99  ? 155 ASN D CA  1 
ATOM   13965 C C   . ASN D  1 155 ? -52.388  7.753   -44.838  1.00 39.54  ? 155 ASN D C   1 
ATOM   13966 O O   . ASN D  1 155 ? -52.886  6.683   -45.168  1.00 39.27  ? 155 ASN D O   1 
ATOM   13967 C CB  . ASN D  1 155 ? -53.836  9.784   -45.270  1.00 44.08  ? 155 ASN D CB  1 
ATOM   13968 C CG  . ASN D  1 155 ? -54.870  10.752  -44.718  1.00 53.38  ? 155 ASN D CG  1 
ATOM   13969 O OD1 . ASN D  1 155 ? -55.482  10.517  -43.661  1.00 54.19  ? 155 ASN D OD1 1 
ATOM   13970 N ND2 . ASN D  1 155 ? -55.094  11.862  -45.420  1.00 55.84  ? 155 ASN D ND2 1 
ATOM   13971 N N   . ILE D  1 156 ? -51.102  8.051   -45.034  1.00 36.60  ? 156 ILE D N   1 
ATOM   13972 C CA  . ILE D  1 156 ? -50.154  7.050   -45.493  1.00 36.39  ? 156 ILE D CA  1 
ATOM   13973 C C   . ILE D  1 156 ? -50.181  5.836   -44.567  1.00 35.62  ? 156 ILE D C   1 
ATOM   13974 O O   . ILE D  1 156 ? -50.168  4.718   -45.063  1.00 35.74  ? 156 ILE D O   1 
ATOM   13975 C CB  . ILE D  1 156 ? -48.738  7.629   -45.630  1.00 37.26  ? 156 ILE D CB  1 
ATOM   13976 C CG1 . ILE D  1 156 ? -48.640  8.525   -46.834  1.00 37.26  ? 156 ILE D CG1 1 
ATOM   13977 C CG2 . ILE D  1 156 ? -47.697  6.515   -45.710  1.00 39.08  ? 156 ILE D CG2 1 
ATOM   13978 C CD1 . ILE D  1 156 ? -47.489  9.501   -46.779  1.00 37.16  ? 156 ILE D CD1 1 
ATOM   13979 N N   . ILE D  1 157 ? -50.263  6.041   -43.241  1.00 35.23  ? 157 ILE D N   1 
ATOM   13980 C CA  . ILE D  1 157 ? -50.339  4.918   -42.309  1.00 36.87  ? 157 ILE D CA  1 
ATOM   13981 C C   . ILE D  1 157 ? -51.700  4.205   -42.419  1.00 38.40  ? 157 ILE D C   1 
ATOM   13982 O O   . ILE D  1 157 ? -51.739  2.968   -42.540  1.00 38.55  ? 157 ILE D O   1 
ATOM   13983 C CB  . ILE D  1 157 ? -49.960  5.313   -40.862  1.00 34.68  ? 157 ILE D CB  1 
ATOM   13984 C CG1 . ILE D  1 157 ? -48.473  5.552   -40.694  1.00 33.27  ? 157 ILE D CG1 1 
ATOM   13985 C CG2 . ILE D  1 157 ? -50.397  4.253   -39.848  1.00 35.27  ? 157 ILE D CG2 1 
ATOM   13986 C CD1 . ILE D  1 157 ? -48.139  6.383   -39.463  1.00 32.40  ? 157 ILE D CD1 1 
ATOM   13987 N N   . HIS D  1 158 ? -52.817  4.950   -42.417  1.00 36.09  ? 158 HIS D N   1 
ATOM   13988 C CA  . HIS D  1 158 ? -54.133  4.296   -42.492  1.00 36.43  ? 158 HIS D CA  1 
ATOM   13989 C C   . HIS D  1 158 ? -54.256  3.313   -43.672  1.00 37.33  ? 158 HIS D C   1 
ATOM   13990 O O   . HIS D  1 158 ? -54.929  2.288   -43.538  1.00 38.27  ? 158 HIS D O   1 
ATOM   13991 C CB  . HIS D  1 158 ? -55.289  5.315   -42.441  1.00 33.64  ? 158 HIS D CB  1 
ATOM   13992 C CG  . HIS D  1 158 ? -55.449  5.968   -41.109  1.00 32.31  ? 158 HIS D CG  1 
ATOM   13993 N ND1 . HIS D  1 158 ? -56.267  7.056   -40.887  1.00 31.72  ? 158 HIS D ND1 1 
ATOM   13994 C CD2 . HIS D  1 158 ? -54.915  5.665   -39.905  1.00 31.96  ? 158 HIS D CD2 1 
ATOM   13995 C CE1 . HIS D  1 158 ? -56.225  7.407   -39.612  1.00 31.07  ? 158 HIS D CE1 1 
ATOM   13996 N NE2 . HIS D  1 158 ? -55.410  6.560   -38.984  1.00 32.10  ? 158 HIS D NE2 1 
ATOM   13997 N N   . LYS D  1 159 ? -53.650  3.631   -44.826  1.00 38.73  ? 159 LYS D N   1 
ATOM   13998 C CA  . LYS D  1 159 ? -53.756  2.792   -46.011  1.00 43.57  ? 159 LYS D CA  1 
ATOM   13999 C C   . LYS D  1 159 ? -52.680  1.706   -46.029  1.00 40.40  ? 159 LYS D C   1 
ATOM   14000 O O   . LYS D  1 159 ? -52.941  0.609   -46.508  1.00 38.92  ? 159 LYS D O   1 
ATOM   14001 C CB  . LYS D  1 159 ? -53.714  3.569   -47.334  1.00 50.24  ? 159 LYS D CB  1 
ATOM   14002 C CG  . LYS D  1 159 ? -54.909  4.520   -47.522  1.00 59.74  ? 159 LYS D CG  1 
ATOM   14003 C CD  . LYS D  1 159 ? -56.286  4.004   -47.067  1.00 69.55  ? 159 LYS D CD  1 
ATOM   14004 C CE  . LYS D  1 159 ? -57.348  5.074   -46.843  1.00 72.31  ? 159 LYS D CE  1 
ATOM   14005 N NZ  . LYS D  1 159 ? -57.877  5.560   -48.121  1.00 73.43  ? 159 LYS D NZ  1 
ATOM   14006 N N   . GLY D  1 160 ? -51.492  2.029   -45.511  1.00 38.86  ? 160 GLY D N   1 
ATOM   14007 C CA  . GLY D  1 160 ? -50.319  1.182   -45.606  1.00 38.51  ? 160 GLY D CA  1 
ATOM   14008 C C   . GLY D  1 160 ? -50.302  0.102   -44.523  1.00 39.95  ? 160 GLY D C   1 
ATOM   14009 O O   . GLY D  1 160 ? -49.793  -1.000  -44.769  1.00 42.24  ? 160 GLY D O   1 
ATOM   14010 N N   . HIS D  1 161 ? -50.876  0.411   -43.341  1.00 37.54  ? 161 HIS D N   1 
ATOM   14011 C CA  . HIS D  1 161 ? -51.107  -0.599  -42.316  1.00 35.57  ? 161 HIS D CA  1 
ATOM   14012 C C   . HIS D  1 161 ? -52.498  -0.422  -41.711  1.00 34.65  ? 161 HIS D C   1 
ATOM   14013 O O   . HIS D  1 161 ? -52.640  0.128   -40.634  1.00 33.46  ? 161 HIS D O   1 
ATOM   14014 C CB  . HIS D  1 161 ? -49.967  -0.566  -41.295  1.00 34.56  ? 161 HIS D CB  1 
ATOM   14015 C CG  . HIS D  1 161 ? -49.932  -1.729  -40.351  1.00 33.49  ? 161 HIS D CG  1 
ATOM   14016 N ND1 . HIS D  1 161 ? -48.941  -1.838  -39.396  1.00 31.41  ? 161 HIS D ND1 1 
ATOM   14017 C CD2 . HIS D  1 161 ? -50.763  -2.775  -40.175  1.00 32.67  ? 161 HIS D CD2 1 
ATOM   14018 C CE1 . HIS D  1 161 ? -49.192  -2.918  -38.659  1.00 31.88  ? 161 HIS D CE1 1 
ATOM   14019 N NE2 . HIS D  1 161 ? -50.273  -3.509  -39.126  1.00 32.28  ? 161 HIS D NE2 1 
ATOM   14020 N N   . PRO D  1 162 ? -53.585  -0.932  -42.338  1.00 37.42  ? 162 PRO D N   1 
ATOM   14021 C CA  . PRO D  1 162 ? -54.944  -0.572  -41.900  1.00 37.68  ? 162 PRO D CA  1 
ATOM   14022 C C   . PRO D  1 162 ? -55.328  -1.065  -40.501  1.00 37.75  ? 162 PRO D C   1 
ATOM   14023 O O   . PRO D  1 162 ? -54.996  -2.191  -40.092  1.00 39.05  ? 162 PRO D O   1 
ATOM   14024 C CB  . PRO D  1 162 ? -55.881  -1.154  -42.995  1.00 38.24  ? 162 PRO D CB  1 
ATOM   14025 C CG  . PRO D  1 162 ? -54.941  -1.637  -44.093  1.00 38.82  ? 162 PRO D CG  1 
ATOM   14026 C CD  . PRO D  1 162 ? -53.581  -1.888  -43.461  1.00 37.94  ? 162 PRO D CD  1 
ATOM   14027 N N   . GLY D  1 163 ? -56.055  -0.199  -39.783  1.00 36.93  ? 163 GLY D N   1 
ATOM   14028 C CA  . GLY D  1 163 ? -56.688  -0.574  -38.533  1.00 35.92  ? 163 GLY D CA  1 
ATOM   14029 C C   . GLY D  1 163 ? -55.788  -0.283  -37.343  1.00 36.02  ? 163 GLY D C   1 
ATOM   14030 O O   . GLY D  1 163 ? -56.181  -0.591  -36.221  1.00 38.51  ? 163 GLY D O   1 
ATOM   14031 N N   . ILE D  1 164 ? -54.613  0.338   -37.586  1.00 35.30  ? 164 ILE D N   1 
ATOM   14032 C CA  . ILE D  1 164 ? -53.673  0.683   -36.525  1.00 34.53  ? 164 ILE D CA  1 
ATOM   14033 C C   . ILE D  1 164 ? -53.799  2.169   -36.156  1.00 33.54  ? 164 ILE D C   1 
ATOM   14034 O O   . ILE D  1 164 ? -53.635  3.036   -37.006  1.00 33.68  ? 164 ILE D O   1 
ATOM   14035 C CB  . ILE D  1 164 ? -52.227  0.319   -36.909  1.00 34.30  ? 164 ILE D CB  1 
ATOM   14036 C CG1 . ILE D  1 164 ? -52.068  -1.121  -37.436  1.00 36.75  ? 164 ILE D CG1 1 
ATOM   14037 C CG2 . ILE D  1 164 ? -51.313  0.567   -35.727  1.00 34.26  ? 164 ILE D CG2 1 
ATOM   14038 C CD1 . ILE D  1 164 ? -52.693  -2.216  -36.588  1.00 36.55  ? 164 ILE D CD1 1 
ATOM   14039 N N   . PRO D  1 165 ? -54.146  2.508   -34.891  1.00 32.68  ? 165 PRO D N   1 
ATOM   14040 C CA  . PRO D  1 165 ? -54.168  3.898   -34.419  1.00 31.71  ? 165 PRO D CA  1 
ATOM   14041 C C   . PRO D  1 165 ? -52.889  4.690   -34.635  1.00 31.58  ? 165 PRO D C   1 
ATOM   14042 O O   . PRO D  1 165 ? -51.790  4.153   -34.520  1.00 33.09  ? 165 PRO D O   1 
ATOM   14043 C CB  . PRO D  1 165 ? -54.462  3.724   -32.904  1.00 31.05  ? 165 PRO D CB  1 
ATOM   14044 C CG  . PRO D  1 165 ? -55.348  2.513   -32.859  1.00 33.03  ? 165 PRO D CG  1 
ATOM   14045 C CD  . PRO D  1 165 ? -54.694  1.575   -33.883  1.00 33.40  ? 165 PRO D CD  1 
ATOM   14046 N N   . VAL D  1 166 ? -53.058  5.986   -34.890  1.00 32.11  ? 166 VAL D N   1 
ATOM   14047 C CA  . VAL D  1 166 ? -51.964  6.902   -35.134  1.00 31.03  ? 166 VAL D CA  1 
ATOM   14048 C C   . VAL D  1 166 ? -52.132  8.100   -34.207  1.00 31.55  ? 166 VAL D C   1 
ATOM   14049 O O   . VAL D  1 166 ? -53.183  8.764   -34.189  1.00 30.92  ? 166 VAL D O   1 
ATOM   14050 C CB  . VAL D  1 166 ? -51.931  7.330   -36.612  1.00 31.97  ? 166 VAL D CB  1 
ATOM   14051 C CG1 . VAL D  1 166 ? -50.761  8.272   -36.951  1.00 32.35  ? 166 VAL D CG1 1 
ATOM   14052 C CG2 . VAL D  1 166 ? -51.901  6.126   -37.546  1.00 32.27  ? 166 VAL D CG2 1 
ATOM   14053 N N   . THR D  1 167 ? -51.075  8.373   -33.431  1.00 30.51  ? 167 THR D N   1 
ATOM   14054 C CA  . THR D  1 167 ? -50.997  9.629   -32.704  1.00 29.10  ? 167 THR D CA  1 
ATOM   14055 C C   . THR D  1 167 ? -49.544  10.109  -32.676  1.00 29.25  ? 167 THR D C   1 
ATOM   14056 O O   . THR D  1 167 ? -48.751  9.790   -33.572  1.00 30.39  ? 167 THR D O   1 
ATOM   14057 C CB  . THR D  1 167 ? -51.673  9.436   -31.345  1.00 28.31  ? 167 THR D CB  1 
ATOM   14058 O OG1 . THR D  1 167 ? -51.947  10.734  -30.802  1.00 25.72  ? 167 THR D OG1 1 
ATOM   14059 C CG2 . THR D  1 167 ? -50.888  8.487   -30.449  1.00 27.39  ? 167 THR D CG2 1 
ATOM   14060 N N   . LEU D  1 168 ? -49.206  10.951  -31.694  1.00 28.77  ? 168 LEU D N   1 
ATOM   14061 C CA  . LEU D  1 168 ? -47.898  11.577  -31.693  1.00 27.81  ? 168 LEU D CA  1 
ATOM   14062 C C   . LEU D  1 168 ? -47.329  11.613  -30.279  1.00 28.70  ? 168 LEU D C   1 
ATOM   14063 O O   . LEU D  1 168 ? -48.039  11.432  -29.292  1.00 28.86  ? 168 LEU D O   1 
ATOM   14064 C CB  . LEU D  1 168 ? -47.965  12.979  -32.324  1.00 27.01  ? 168 LEU D CB  1 
ATOM   14065 C CG  . LEU D  1 168 ? -48.276  14.151  -31.398  1.00 26.00  ? 168 LEU D CG  1 
ATOM   14066 C CD1 . LEU D  1 168 ? -48.091  15.410  -32.160  1.00 28.06  ? 168 LEU D CD1 1 
ATOM   14067 C CD2 . LEU D  1 168 ? -49.685  14.075  -30.876  1.00 26.96  ? 168 LEU D CD2 1 
ATOM   14068 N N   . SER D  1 169 ? -46.024  11.905  -30.218  1.00 28.67  ? 169 SER D N   1 
ATOM   14069 C CA  . SER D  1 169 ? -45.326  12.141  -28.973  1.00 27.89  ? 169 SER D CA  1 
ATOM   14070 C C   . SER D  1 169 ? -45.244  13.651  -28.754  1.00 28.73  ? 169 SER D C   1 
ATOM   14071 O O   . SER D  1 169 ? -44.455  14.315  -29.415  1.00 28.48  ? 169 SER D O   1 
ATOM   14072 C CB  . SER D  1 169 ? -43.956  11.490  -29.061  1.00 27.76  ? 169 SER D CB  1 
ATOM   14073 O OG  . SER D  1 169 ? -43.070  11.882  -28.020  1.00 27.66  ? 169 SER D OG  1 
ATOM   14074 N N   . ALA D  1 170 ? -46.072  14.201  -27.858  1.00 29.76  ? 170 ALA D N   1 
ATOM   14075 C CA  . ALA D  1 170 ? -46.074  15.641  -27.600  1.00 28.21  ? 170 ALA D CA  1 
ATOM   14076 C C   . ALA D  1 170 ? -46.168  15.925  -26.109  1.00 28.29  ? 170 ALA D C   1 
ATOM   14077 O O   . ALA D  1 170 ? -47.126  15.506  -25.475  1.00 28.41  ? 170 ALA D O   1 
ATOM   14078 C CB  . ALA D  1 170 ? -47.234  16.287  -28.305  1.00 29.19  ? 170 ALA D CB  1 
ATOM   14079 N N   . ASN D  1 171 ? -45.226  16.729  -25.585  1.00 28.66  ? 171 ASN D N   1 
ATOM   14080 C CA  . ASN D  1 171 ? -45.140  17.028  -24.163  1.00 28.27  ? 171 ASN D CA  1 
ATOM   14081 C C   . ASN D  1 171 ? -46.252  17.987  -23.735  1.00 29.77  ? 171 ASN D C   1 
ATOM   14082 O O   . ASN D  1 171 ? -46.426  19.060  -24.310  1.00 28.99  ? 171 ASN D O   1 
ATOM   14083 C CB  . ASN D  1 171 ? -43.771  17.602  -23.851  1.00 28.18  ? 171 ASN D CB  1 
ATOM   14084 C CG  . ASN D  1 171 ? -43.517  17.781  -22.379  1.00 29.19  ? 171 ASN D CG  1 
ATOM   14085 O OD1 . ASN D  1 171 ? -44.167  18.614  -21.736  1.00 29.42  ? 171 ASN D OD1 1 
ATOM   14086 N ND2 . ASN D  1 171 ? -42.521  17.068  -21.860  1.00 28.24  ? 171 ASN D ND2 1 
ATOM   14087 N N   . ALA D  1 172 ? -47.000  17.592  -22.694  1.00 30.02  ? 172 ALA D N   1 
ATOM   14088 C CA  . ALA D  1 172 ? -48.166  18.345  -22.253  1.00 29.16  ? 172 ALA D CA  1 
ATOM   14089 C C   . ALA D  1 172 ? -47.799  19.771  -21.835  1.00 28.41  ? 172 ALA D C   1 
ATOM   14090 O O   . ALA D  1 172 ? -48.666  20.649  -21.814  1.00 27.06  ? 172 ALA D O   1 
ATOM   14091 C CB  . ALA D  1 172 ? -48.874  17.627  -21.138  1.00 27.44  ? 172 ALA D CB  1 
ATOM   14092 N N   . MET D  1 173 ? -46.533  19.988  -21.466  1.00 27.28  ? 173 MET D N   1 
ATOM   14093 C CA  . MET D  1 173 ? -46.142  21.243  -20.859  1.00 28.07  ? 173 MET D CA  1 
ATOM   14094 C C   . MET D  1 173 ? -45.947  22.308  -21.932  1.00 28.45  ? 173 MET D C   1 
ATOM   14095 O O   . MET D  1 173 ? -46.062  23.513  -21.600  1.00 28.70  ? 173 MET D O   1 
ATOM   14096 C CB  . MET D  1 173 ? -44.903  21.088  -19.965  1.00 29.98  ? 173 MET D CB  1 
ATOM   14097 C CG  . MET D  1 173 ? -45.198  20.431  -18.608  1.00 30.58  ? 173 MET D CG  1 
ATOM   14098 S SD  . MET D  1 173 ? -46.165  21.425  -17.446  1.00 30.63  ? 173 MET D SD  1 
ATOM   14099 C CE  . MET D  1 173 ? -44.991  22.710  -17.009  1.00 29.94  ? 173 MET D CE  1 
ATOM   14100 N N   . ILE D  1 174 ? -45.745  21.869  -23.203  1.00 27.08  ? 174 ILE D N   1 
ATOM   14101 C CA  . ILE D  1 174 ? -45.463  22.791  -24.309  1.00 26.38  ? 174 ILE D CA  1 
ATOM   14102 C C   . ILE D  1 174 ? -46.491  22.704  -25.428  1.00 26.16  ? 174 ILE D C   1 
ATOM   14103 O O   . ILE D  1 174 ? -46.531  23.622  -26.247  1.00 28.62  ? 174 ILE D O   1 
ATOM   14104 C CB  . ILE D  1 174 ? -44.036  22.642  -24.896  1.00 24.93  ? 174 ILE D CB  1 
ATOM   14105 C CG1 . ILE D  1 174 ? -43.786  21.223  -25.487  1.00 26.65  ? 174 ILE D CG1 1 
ATOM   14106 C CG2 . ILE D  1 174 ? -42.999  23.009  -23.851  1.00 23.49  ? 174 ILE D CG2 1 
ATOM   14107 C CD1 . ILE D  1 174 ? -42.557  21.130  -26.381  1.00 26.32  ? 174 ILE D CD1 1 
ATOM   14108 N N   . SER D  1 175 ? -47.304  21.645  -25.471  1.00 26.11  ? 175 SER D N   1 
ATOM   14109 C CA  . SER D  1 175 ? -48.208  21.408  -26.581  1.00 25.69  ? 175 SER D CA  1 
ATOM   14110 C C   . SER D  1 175 ? -49.640  21.220  -26.093  1.00 28.08  ? 175 SER D C   1 
ATOM   14111 O O   . SER D  1 175 ? -50.488  20.698  -26.826  1.00 28.52  ? 175 SER D O   1 
ATOM   14112 C CB  . SER D  1 175 ? -47.746  20.231  -27.382  1.00 27.16  ? 175 SER D CB  1 
ATOM   14113 O OG  . SER D  1 175 ? -46.470  20.483  -27.965  1.00 28.52  ? 175 SER D OG  1 
ATOM   14114 N N   . ASP D  1 176 ? -49.915  21.700  -24.868  1.00 29.29  ? 176 ASP D N   1 
ATOM   14115 C CA  . ASP D  1 176 ? -51.262  21.881  -24.334  1.00 29.22  ? 176 ASP D CA  1 
ATOM   14116 C C   . ASP D  1 176 ? -52.189  22.546  -25.360  1.00 31.25  ? 176 ASP D C   1 
ATOM   14117 O O   . ASP D  1 176 ? -53.388  22.256  -25.415  1.00 35.47  ? 176 ASP D O   1 
ATOM   14118 C CB  . ASP D  1 176 ? -51.198  22.708  -23.055  1.00 30.58  ? 176 ASP D CB  1 
ATOM   14119 C CG  . ASP D  1 176 ? -50.299  23.954  -23.063  1.00 30.25  ? 176 ASP D CG  1 
ATOM   14120 O OD1 . ASP D  1 176 ? -49.550  24.144  -24.025  1.00 30.36  ? 176 ASP D OD1 1 
ATOM   14121 O OD2 . ASP D  1 176 ? -50.340  24.745  -22.101  1.00 30.75  ? 176 ASP D OD2 1 
ATOM   14122 N N   . TYR D  1 177 ? -51.661  23.455  -26.172  1.00 29.67  ? 177 TYR D N   1 
ATOM   14123 C CA  . TYR D  1 177 ? -52.500  24.249  -27.100  1.00 30.51  ? 177 TYR D CA  1 
ATOM   14124 C C   . TYR D  1 177 ? -52.835  23.495  -28.356  1.00 30.78  ? 177 TYR D C   1 
ATOM   14125 O O   . TYR D  1 177 ? -53.758  23.911  -29.066  1.00 30.72  ? 177 TYR D O   1 
ATOM   14126 C CB  . TYR D  1 177 ? -51.668  25.469  -27.503  1.00 29.99  ? 177 TYR D CB  1 
ATOM   14127 C CG  . TYR D  1 177 ? -50.519  25.177  -28.458  1.00 30.67  ? 177 TYR D CG  1 
ATOM   14128 C CD1 . TYR D  1 177 ? -49.283  24.763  -27.981  1.00 30.36  ? 177 TYR D CD1 1 
ATOM   14129 C CD2 . TYR D  1 177 ? -50.672  25.310  -29.831  1.00 30.93  ? 177 TYR D CD2 1 
ATOM   14130 C CE1 . TYR D  1 177 ? -48.237  24.486  -28.841  1.00 29.36  ? 177 TYR D CE1 1 
ATOM   14131 C CE2 . TYR D  1 177 ? -49.635  25.028  -30.702  1.00 31.02  ? 177 TYR D CE2 1 
ATOM   14132 C CZ  . TYR D  1 177 ? -48.413  24.621  -30.204  1.00 30.65  ? 177 TYR D CZ  1 
ATOM   14133 O OH  . TYR D  1 177 ? -47.383  24.351  -31.051  1.00 31.83  ? 177 TYR D OH  1 
ATOM   14134 N N   . MET D  1 178 ? -52.129  22.407  -28.623  1.00 29.84  ? 178 MET D N   1 
ATOM   14135 C CA  . MET D  1 178 ? -52.292  21.742  -29.935  1.00 28.69  ? 178 MET D CA  1 
ATOM   14136 C C   . MET D  1 178 ? -53.626  21.016  -30.101  1.00 28.79  ? 178 MET D C   1 
ATOM   14137 O O   . MET D  1 178 ? -54.109  20.415  -29.134  1.00 28.72  ? 178 MET D O   1 
ATOM   14138 C CB  . MET D  1 178 ? -51.146  20.764  -30.198  1.00 28.73  ? 178 MET D CB  1 
ATOM   14139 C CG  . MET D  1 178 ? -51.082  20.216  -31.595  1.00 30.17  ? 178 MET D CG  1 
ATOM   14140 S SD  . MET D  1 178 ? -49.762  18.994  -31.631  1.00 31.90  ? 178 MET D SD  1 
ATOM   14141 C CE  . MET D  1 178 ? -48.299  20.020  -31.445  1.00 33.16  ? 178 MET D CE  1 
ATOM   14142 N N   . ASP D  1 179 ? -54.193  21.123  -31.297  1.00 30.39  ? 179 ASP D N   1 
ATOM   14143 C CA  . ASP D  1 179 ? -55.392  20.338  -31.655  1.00 32.68  ? 179 ASP D CA  1 
ATOM   14144 C C   . ASP D  1 179 ? -54.915  18.926  -31.995  1.00 30.28  ? 179 ASP D C   1 
ATOM   14145 O O   . ASP D  1 179 ? -54.104  18.766  -32.911  1.00 30.15  ? 179 ASP D O   1 
ATOM   14146 C CB  . ASP D  1 179 ? -56.137  20.978  -32.812  1.00 35.99  ? 179 ASP D CB  1 
ATOM   14147 C CG  . ASP D  1 179 ? -57.350  20.217  -33.318  1.00 39.82  ? 179 ASP D CG  1 
ATOM   14148 O OD1 . ASP D  1 179 ? -58.143  19.759  -32.479  1.00 39.37  ? 179 ASP D OD1 1 
ATOM   14149 O OD2 . ASP D  1 179 ? -57.488  20.097  -34.546  1.00 46.43  ? 179 ASP D OD2 1 
ATOM   14150 N N   . GLU D  1 180 ? -55.399  17.944  -31.253  1.00 30.96  ? 180 GLU D N   1 
ATOM   14151 C CA  . GLU D  1 180 ? -54.978  16.569  -31.480  1.00 29.29  ? 180 GLU D CA  1 
ATOM   14152 C C   . GLU D  1 180 ? -56.084  15.775  -32.174  1.00 29.90  ? 180 GLU D C   1 
ATOM   14153 O O   . GLU D  1 180 ? -55.930  14.563  -32.381  1.00 30.49  ? 180 GLU D O   1 
ATOM   14154 C CB  . GLU D  1 180 ? -54.571  15.883  -30.183  1.00 29.51  ? 180 GLU D CB  1 
ATOM   14155 C CG  . GLU D  1 180 ? -53.193  16.267  -29.646  1.00 28.95  ? 180 GLU D CG  1 
ATOM   14156 C CD  . GLU D  1 180 ? -52.644  15.273  -28.634  1.00 29.83  ? 180 GLU D CD  1 
ATOM   14157 O OE1 . GLU D  1 180 ? -53.271  14.185  -28.370  1.00 29.16  ? 180 GLU D OE1 1 
ATOM   14158 O OE2 . GLU D  1 180 ? -51.545  15.597  -28.125  1.00 27.87  ? 180 GLU D OE2 1 
ATOM   14159 N N   . SER D  1 181 ? -57.141  16.474  -32.617  1.00 28.80  ? 181 SER D N   1 
ATOM   14160 C CA  . SER D  1 181 ? -58.357  15.840  -33.107  1.00 29.64  ? 181 SER D CA  1 
ATOM   14161 C C   . SER D  1 181 ? -58.150  15.156  -34.465  1.00 31.73  ? 181 SER D C   1 
ATOM   14162 O O   . SER D  1 181 ? -58.991  14.357  -34.890  1.00 30.68  ? 181 SER D O   1 
ATOM   14163 C CB  . SER D  1 181 ? -59.498  16.848  -33.161  1.00 29.10  ? 181 SER D CB  1 
ATOM   14164 O OG  . SER D  1 181 ? -59.368  17.672  -34.303  1.00 28.32  ? 181 SER D OG  1 
ATOM   14165 N N   . ILE D  1 182 ? -57.044  15.492  -35.160  1.00 32.92  ? 182 ILE D N   1 
ATOM   14166 C CA  . ILE D  1 182 ? -56.667  14.831  -36.409  1.00 33.88  ? 182 ILE D CA  1 
ATOM   14167 C C   . ILE D  1 182 ? -56.085  13.435  -36.151  1.00 32.82  ? 182 ILE D C   1 
ATOM   14168 O O   . ILE D  1 182 ? -55.976  12.640  -37.071  1.00 32.65  ? 182 ILE D O   1 
ATOM   14169 C CB  . ILE D  1 182 ? -55.660  15.683  -37.205  1.00 35.38  ? 182 ILE D CB  1 
ATOM   14170 C CG1 . ILE D  1 182 ? -54.432  16.045  -36.373  1.00 33.91  ? 182 ILE D CG1 1 
ATOM   14171 C CG2 . ILE D  1 182 ? -56.336  16.925  -37.792  1.00 35.50  ? 182 ILE D CG2 1 
ATOM   14172 C CD1 . ILE D  1 182 ? -53.315  16.660  -37.193  1.00 34.68  ? 182 ILE D CD1 1 
ATOM   14173 N N   . PHE D  1 183 ? -55.649  13.171  -34.919  1.00 32.30  ? 183 PHE D N   1 
ATOM   14174 C CA  . PHE D  1 183 ? -55.087  11.886  -34.556  1.00 32.10  ? 183 PHE D CA  1 
ATOM   14175 C C   . PHE D  1 183 ? -56.223  10.976  -34.125  1.00 31.60  ? 183 PHE D C   1 
ATOM   14176 O O   . PHE D  1 183 ? -57.310  11.443  -33.816  1.00 32.28  ? 183 PHE D O   1 
ATOM   14177 C CB  . PHE D  1 183 ? -54.055  12.043  -33.439  1.00 30.14  ? 183 PHE D CB  1 
ATOM   14178 C CG  . PHE D  1 183 ? -52.908  12.915  -33.887  1.00 31.36  ? 183 PHE D CG  1 
ATOM   14179 C CD1 . PHE D  1 183 ? -51.960  12.443  -34.793  1.00 32.71  ? 183 PHE D CD1 1 
ATOM   14180 C CD2 . PHE D  1 183 ? -52.773  14.224  -33.415  1.00 31.64  ? 183 PHE D CD2 1 
ATOM   14181 C CE1 . PHE D  1 183 ? -50.895  13.264  -35.193  1.00 31.59  ? 183 PHE D CE1 1 
ATOM   14182 C CE2 . PHE D  1 183 ? -51.715  15.019  -33.822  1.00 29.67  ? 183 PHE D CE2 1 
ATOM   14183 C CZ  . PHE D  1 183 ? -50.775  14.534  -34.698  1.00 29.21  ? 183 PHE D CZ  1 
ATOM   14184 N N   . ASP D  1 184 ? -55.950  9.672   -34.134  1.00 32.38  ? 184 ASP D N   1 
ATOM   14185 C CA  . ASP D  1 184 ? -56.936  8.661   -33.751  1.00 31.56  ? 184 ASP D CA  1 
ATOM   14186 C C   . ASP D  1 184 ? -57.003  8.484   -32.234  1.00 29.88  ? 184 ASP D C   1 
ATOM   14187 O O   . ASP D  1 184 ? -58.032  8.088   -31.717  1.00 30.36  ? 184 ASP D O   1 
ATOM   14188 C CB  . ASP D  1 184 ? -56.604  7.297   -34.322  1.00 31.08  ? 184 ASP D CB  1 
ATOM   14189 C CG  . ASP D  1 184 ? -56.432  7.250   -35.825  1.00 32.30  ? 184 ASP D CG  1 
ATOM   14190 O OD1 . ASP D  1 184 ? -57.321  7.773   -36.538  1.00 32.73  ? 184 ASP D OD1 1 
ATOM   14191 O OD2 . ASP D  1 184 ? -55.414  6.662   -36.256  1.00 33.07  ? 184 ASP D OD2 1 
ATOM   14192 N N   . VAL D  1 185 ? -55.891  8.740   -31.538  1.00 28.88  ? 185 VAL D N   1 
ATOM   14193 C CA  . VAL D  1 185 ? -55.838  8.692   -30.085  1.00 28.94  ? 185 VAL D CA  1 
ATOM   14194 C C   . VAL D  1 185 ? -55.233  9.995   -29.559  1.00 27.26  ? 185 VAL D C   1 
ATOM   14195 O O   . VAL D  1 185 ? -54.401  10.604  -30.221  1.00 27.00  ? 185 VAL D O   1 
ATOM   14196 C CB  . VAL D  1 185 ? -55.007  7.434   -29.731  1.00 29.58  ? 185 VAL D CB  1 
ATOM   14197 C CG1 . VAL D  1 185 ? -54.476  7.436   -28.310  1.00 29.16  ? 185 VAL D CG1 1 
ATOM   14198 C CG2 . VAL D  1 185 ? -55.819  6.155   -29.944  1.00 29.74  ? 185 VAL D CG2 1 
ATOM   14199 N N   . TYR D  1 186 ? -55.611  10.402  -28.345  1.00 27.78  ? 186 TYR D N   1 
ATOM   14200 C CA  . TYR D  1 186 ? -54.986  11.560  -27.707  1.00 27.13  ? 186 TYR D CA  1 
ATOM   14201 C C   . TYR D  1 186 ? -53.810  11.066  -26.879  1.00 28.78  ? 186 TYR D C   1 
ATOM   14202 O O   . TYR D  1 186 ? -53.826  9.951   -26.311  1.00 30.85  ? 186 TYR D O   1 
ATOM   14203 C CB  . TYR D  1 186 ? -55.938  12.402  -26.847  1.00 27.27  ? 186 TYR D CB  1 
ATOM   14204 C CG  . TYR D  1 186 ? -57.137  12.998  -27.584  1.00 28.04  ? 186 TYR D CG  1 
ATOM   14205 C CD1 . TYR D  1 186 ? -56.972  13.751  -28.720  1.00 30.22  ? 186 TYR D CD1 1 
ATOM   14206 C CD2 . TYR D  1 186 ? -58.436  12.779  -27.168  1.00 30.08  ? 186 TYR D CD2 1 
ATOM   14207 C CE1 . TYR D  1 186 ? -58.051  14.311  -29.392  1.00 33.65  ? 186 TYR D CE1 1 
ATOM   14208 C CE2 . TYR D  1 186 ? -59.536  13.287  -27.845  1.00 31.23  ? 186 TYR D CE2 1 
ATOM   14209 C CZ  . TYR D  1 186 ? -59.348  14.076  -28.966  1.00 34.01  ? 186 TYR D CZ  1 
ATOM   14210 O OH  . TYR D  1 186 ? -60.404  14.624  -29.667  1.00 33.26  ? 186 TYR D OH  1 
ATOM   14211 N N   . ALA D  1 187 ? -52.761  11.901  -26.822  1.00 27.68  ? 187 ALA D N   1 
ATOM   14212 C CA  . ALA D  1 187 ? -51.526  11.460  -26.188  1.00 26.22  ? 187 ALA D CA  1 
ATOM   14213 C C   . ALA D  1 187 ? -50.682  12.651  -25.765  1.00 25.59  ? 187 ALA D C   1 
ATOM   14214 O O   . ALA D  1 187 ? -50.616  13.635  -26.489  1.00 28.01  ? 187 ALA D O   1 
ATOM   14215 C CB  . ALA D  1 187 ? -50.765  10.540  -27.127  1.00 25.50  ? 187 ALA D CB  1 
ATOM   14216 N N   . TYR D  1 188 ? -50.023  12.530  -24.611  1.00 25.90  ? 188 TYR D N   1 
ATOM   14217 C CA  . TYR D  1 188 ? -49.000  13.478  -24.176  1.00 26.41  ? 188 TYR D CA  1 
ATOM   14218 C C   . TYR D  1 188 ? -47.851  12.771  -23.460  1.00 27.88  ? 188 TYR D C   1 
ATOM   14219 O O   . TYR D  1 188 ? -48.030  11.708  -22.858  1.00 26.55  ? 188 TYR D O   1 
ATOM   14220 C CB  . TYR D  1 188 ? -49.507  14.515  -23.165  1.00 26.47  ? 188 TYR D CB  1 
ATOM   14221 C CG  . TYR D  1 188 ? -50.632  15.368  -23.737  1.00 27.07  ? 188 TYR D CG  1 
ATOM   14222 C CD1 . TYR D  1 188 ? -50.361  16.322  -24.699  1.00 27.16  ? 188 TYR D CD1 1 
ATOM   14223 C CD2 . TYR D  1 188 ? -51.951  15.224  -23.316  1.00 29.00  ? 188 TYR D CD2 1 
ATOM   14224 C CE1 . TYR D  1 188 ? -51.367  17.101  -25.249  1.00 28.39  ? 188 TYR D CE1 1 
ATOM   14225 C CE2 . TYR D  1 188 ? -52.969  16.038  -23.822  1.00 29.49  ? 188 TYR D CE2 1 
ATOM   14226 C CZ  . TYR D  1 188 ? -52.668  16.953  -24.810  1.00 27.49  ? 188 TYR D CZ  1 
ATOM   14227 O OH  . TYR D  1 188 ? -53.608  17.714  -25.380  1.00 26.68  ? 188 TYR D OH  1 
ATOM   14228 N N   . ASN D  1 189 ? -46.670  13.408  -23.512  1.00 28.04  ? 189 ASN D N   1 
ATOM   14229 C CA  . ASN D  1 189 ? -45.631  13.116  -22.540  1.00 28.36  ? 189 ASN D CA  1 
ATOM   14230 C C   . ASN D  1 189 ? -45.932  13.952  -21.311  1.00 27.92  ? 189 ASN D C   1 
ATOM   14231 O O   . ASN D  1 189 ? -46.063  15.156  -21.477  1.00 31.06  ? 189 ASN D O   1 
ATOM   14232 C CB  . ASN D  1 189 ? -44.232  13.440  -23.067  1.00 28.52  ? 189 ASN D CB  1 
ATOM   14233 C CG  . ASN D  1 189 ? -43.889  12.670  -24.313  1.00 27.77  ? 189 ASN D CG  1 
ATOM   14234 O OD1 . ASN D  1 189 ? -43.383  13.265  -25.273  1.00 29.61  ? 189 ASN D OD1 1 
ATOM   14235 N ND2 . ASN D  1 189 ? -44.176  11.373  -24.330  1.00 26.77  ? 189 ASN D ND2 1 
ATOM   14236 N N   . CYS D  1 190 ? -46.041  13.320  -20.129  1.00 27.14  ? 190 CYS D N   1 
ATOM   14237 C CA  . CYS D  1 190 ? -46.536  13.979  -18.931  1.00 28.33  ? 190 CYS D CA  1 
ATOM   14238 C C   . CYS D  1 190 ? -45.537  13.870  -17.792  1.00 29.00  ? 190 CYS D C   1 
ATOM   14239 O O   . CYS D  1 190 ? -45.278  12.760  -17.319  1.00 29.62  ? 190 CYS D O   1 
ATOM   14240 C CB  . CYS D  1 190 ? -47.879  13.409  -18.498  1.00 27.75  ? 190 CYS D CB  1 
ATOM   14241 S SG  . CYS D  1 190 ? -49.089  13.365  -19.843  1.00 28.09  ? 190 CYS D SG  1 
ATOM   14242 N N   . TYR D  1 191 ? -45.018  15.030  -17.358  1.00 26.85  ? 191 TYR D N   1 
ATOM   14243 C CA  . TYR D  1 191 ? -44.068  15.072  -16.264  1.00 28.40  ? 191 TYR D CA  1 
ATOM   14244 C C   . TYR D  1 191 ? -44.616  15.948  -15.140  1.00 27.07  ? 191 TYR D C   1 
ATOM   14245 O O   . TYR D  1 191 ? -45.186  17.020  -15.380  1.00 25.21  ? 191 TYR D O   1 
ATOM   14246 C CB  . TYR D  1 191 ? -42.674  15.596  -16.668  1.00 29.12  ? 191 TYR D CB  1 
ATOM   14247 C CG  . TYR D  1 191 ? -41.942  14.587  -17.506  1.00 26.22  ? 191 TYR D CG  1 
ATOM   14248 C CD1 . TYR D  1 191 ? -41.189  13.580  -16.903  1.00 27.76  ? 191 TYR D CD1 1 
ATOM   14249 C CD2 . TYR D  1 191 ? -42.091  14.564  -18.888  1.00 26.89  ? 191 TYR D CD2 1 
ATOM   14250 C CE1 . TYR D  1 191 ? -40.584  12.573  -17.644  1.00 25.04  ? 191 TYR D CE1 1 
ATOM   14251 C CE2 . TYR D  1 191 ? -41.478  13.565  -19.639  1.00 27.43  ? 191 TYR D CE2 1 
ATOM   14252 C CZ  . TYR D  1 191 ? -40.735  12.569  -19.018  1.00 26.72  ? 191 TYR D CZ  1 
ATOM   14253 O OH  . TYR D  1 191 ? -40.129  11.600  -19.774  1.00 30.92  ? 191 TYR D OH  1 
ATOM   14254 N N   . ASP D  1 192 ? -44.356  15.489  -13.909  1.00 26.80  ? 192 ASP D N   1 
ATOM   14255 C CA  . ASP D  1 192 ? -44.787  16.189  -12.717  1.00 27.99  ? 192 ASP D CA  1 
ATOM   14256 C C   . ASP D  1 192 ? -43.595  16.746  -11.954  1.00 29.47  ? 192 ASP D C   1 
ATOM   14257 O O   . ASP D  1 192 ? -43.046  16.077  -11.084  1.00 28.36  ? 192 ASP D O   1 
ATOM   14258 C CB  . ASP D  1 192 ? -45.531  15.267  -11.782  1.00 27.53  ? 192 ASP D CB  1 
ATOM   14259 C CG  . ASP D  1 192 ? -46.126  15.941  -10.571  1.00 27.71  ? 192 ASP D CG  1 
ATOM   14260 O OD1 . ASP D  1 192 ? -46.013  17.206  -10.472  1.00 30.03  ? 192 ASP D OD1 1 
ATOM   14261 O OD2 . ASP D  1 192 ? -46.620  15.180  -9.719   1.00 26.91  ? 192 ASP D OD2 1 
ATOM   14262 N N   . HIS D  1 193 ? -43.283  18.014  -12.219  1.00 30.03  ? 193 HIS D N   1 
ATOM   14263 C CA  . HIS D  1 193 ? -42.194  18.689  -11.532  1.00 29.69  ? 193 HIS D CA  1 
ATOM   14264 C C   . HIS D  1 193 ? -42.712  19.793  -10.625  1.00 30.69  ? 193 HIS D C   1 
ATOM   14265 O O   . HIS D  1 193 ? -41.911  20.591  -10.140  1.00 31.23  ? 193 HIS D O   1 
ATOM   14266 C CB  . HIS D  1 193 ? -41.260  19.349  -12.533  1.00 29.61  ? 193 HIS D CB  1 
ATOM   14267 C CG  . HIS D  1 193 ? -40.620  18.381  -13.459  1.00 28.78  ? 193 HIS D CG  1 
ATOM   14268 N ND1 . HIS D  1 193 ? -40.616  18.563  -14.820  1.00 26.74  ? 193 HIS D ND1 1 
ATOM   14269 C CD2 . HIS D  1 193 ? -39.974  17.224  -13.211  1.00 29.03  ? 193 HIS D CD2 1 
ATOM   14270 C CE1 . HIS D  1 193 ? -39.944  17.566  -15.373  1.00 29.13  ? 193 HIS D CE1 1 
ATOM   14271 N NE2 . HIS D  1 193 ? -39.546  16.730  -14.419  1.00 28.15  ? 193 HIS D NE2 1 
ATOM   14272 N N   . ASN D  1 194 ? -44.037  19.828  -10.405  1.00 29.36  ? 194 ASN D N   1 
ATOM   14273 C CA  . ASN D  1 194 ? -44.615  20.824  -9.526   1.00 28.22  ? 194 ASN D CA  1 
ATOM   14274 C C   . ASN D  1 194 ? -44.172  22.254  -9.919   1.00 29.78  ? 194 ASN D C   1 
ATOM   14275 O O   . ASN D  1 194 ? -43.669  23.016  -9.087   1.00 29.26  ? 194 ASN D O   1 
ATOM   14276 C CB  . ASN D  1 194 ? -44.215  20.506  -8.096   1.00 26.04  ? 194 ASN D CB  1 
ATOM   14277 C CG  . ASN D  1 194 ? -44.969  21.375  -7.121   1.00 25.48  ? 194 ASN D CG  1 
ATOM   14278 O OD1 . ASN D  1 194 ? -46.091  21.784  -7.400   1.00 26.56  ? 194 ASN D OD1 1 
ATOM   14279 N ND2 . ASN D  1 194 ? -44.414  21.634  -5.962   1.00 24.80  ? 194 ASN D ND2 1 
ATOM   14280 N N   . GLU D  1 195 ? -44.342  22.623  -11.194  1.00 29.04  ? 195 GLU D N   1 
ATOM   14281 C CA  . GLU D  1 195 ? -43.991  23.954  -11.672  1.00 31.18  ? 195 GLU D CA  1 
ATOM   14282 C C   . GLU D  1 195 ? -44.932  24.315  -12.821  1.00 29.67  ? 195 GLU D C   1 
ATOM   14283 O O   . GLU D  1 195 ? -45.483  23.421  -13.460  1.00 28.56  ? 195 GLU D O   1 
ATOM   14284 C CB  . GLU D  1 195 ? -42.527  24.071  -12.120  1.00 30.27  ? 195 GLU D CB  1 
ATOM   14285 C CG  . GLU D  1 195 ? -42.226  23.133  -13.275  1.00 31.27  ? 195 GLU D CG  1 
ATOM   14286 C CD  . GLU D  1 195 ? -40.784  23.021  -13.675  1.00 30.87  ? 195 GLU D CD  1 
ATOM   14287 O OE1 . GLU D  1 195 ? -39.937  23.739  -13.142  1.00 32.58  ? 195 GLU D OE1 1 
ATOM   14288 O OE2 . GLU D  1 195 ? -40.546  22.170  -14.534  1.00 32.03  ? 195 GLU D OE2 1 
ATOM   14289 N N   . GLY D  1 196 ? -45.072  25.622  -13.089  1.00 28.57  ? 196 GLY D N   1 
ATOM   14290 C CA  . GLY D  1 196 ? -46.023  26.115  -14.074  1.00 27.91  ? 196 GLY D CA  1 
ATOM   14291 C C   . GLY D  1 196 ? -47.402  25.473  -13.900  1.00 26.43  ? 196 GLY D C   1 
ATOM   14292 O O   . GLY D  1 196 ? -47.951  25.464  -12.806  1.00 25.59  ? 196 GLY D O   1 
ATOM   14293 N N   . GLN D  1 197 ? -47.913  24.898  -14.988  1.00 26.31  ? 197 GLN D N   1 
ATOM   14294 C CA  . GLN D  1 197 ? -49.198  24.205  -15.008  1.00 28.29  ? 197 GLN D CA  1 
ATOM   14295 C C   . GLN D  1 197 ? -49.334  23.125  -13.924  1.00 26.13  ? 197 GLN D C   1 
ATOM   14296 O O   . GLN D  1 197 ? -50.427  22.922  -13.414  1.00 25.37  ? 197 GLN D O   1 
ATOM   14297 C CB  . GLN D  1 197 ? -49.445  23.572  -16.384  1.00 29.27  ? 197 GLN D CB  1 
ATOM   14298 C CG  . GLN D  1 197 ? -49.520  24.579  -17.532  1.00 28.39  ? 197 GLN D CG  1 
ATOM   14299 C CD  . GLN D  1 197 ? -48.199  24.795  -18.230  1.00 27.87  ? 197 GLN D CD  1 
ATOM   14300 O OE1 . GLN D  1 197 ? -47.191  25.114  -17.600  1.00 28.08  ? 197 GLN D OE1 1 
ATOM   14301 N NE2 . GLN D  1 197 ? -48.184  24.583  -19.535  1.00 26.71  ? 197 GLN D NE2 1 
ATOM   14302 N N   . THR D  1 198 ? -48.251  22.448  -13.523  1.00 24.66  ? 198 THR D N   1 
ATOM   14303 C CA  . THR D  1 198 ? -48.437  21.322  -12.622  1.00 24.73  ? 198 THR D CA  1 
ATOM   14304 C C   . THR D  1 198 ? -48.402  21.810  -11.185  1.00 25.93  ? 198 THR D C   1 
ATOM   14305 O O   . THR D  1 198 ? -48.740  21.042  -10.275  1.00 27.23  ? 198 THR D O   1 
ATOM   14306 C CB  . THR D  1 198 ? -47.431  20.193  -12.843  1.00 23.49  ? 198 THR D CB  1 
ATOM   14307 O OG1 . THR D  1 198 ? -46.100  20.655  -12.627  1.00 22.09  ? 198 THR D OG1 1 
ATOM   14308 C CG2 . THR D  1 198 ? -47.583  19.574  -14.221  1.00 23.52  ? 198 THR D CG2 1 
ATOM   14309 N N   . ALA D  1 199 ? -47.956  23.059  -11.013  1.00 26.18  ? 199 ALA D N   1 
ATOM   14310 C CA  . ALA D  1 199 ? -47.961  23.723  -9.722   1.00 27.07  ? 199 ALA D CA  1 
ATOM   14311 C C   . ALA D  1 199 ? -49.323  24.359  -9.459   1.00 26.60  ? 199 ALA D C   1 
ATOM   14312 O O   . ALA D  1 199 ? -49.772  24.312  -8.327   1.00 28.71  ? 199 ALA D O   1 
ATOM   14313 C CB  . ALA D  1 199 ? -46.845  24.758  -9.650   1.00 28.00  ? 199 ALA D CB  1 
ATOM   14314 N N   . THR D  1 200 ? -49.979  24.939  -10.475  1.00 26.26  ? 200 THR D N   1 
ATOM   14315 C CA  . THR D  1 200 ? -51.270  25.604  -10.268  1.00 28.03  ? 200 THR D CA  1 
ATOM   14316 C C   . THR D  1 200 ? -52.402  24.572  -10.166  1.00 29.96  ? 200 THR D C   1 
ATOM   14317 O O   . THR D  1 200 ? -53.106  24.483  -9.159   1.00 31.36  ? 200 THR D O   1 
ATOM   14318 C CB  . THR D  1 200 ? -51.495  26.588  -11.413  1.00 29.22  ? 200 THR D CB  1 
ATOM   14319 O OG1 . THR D  1 200 ? -51.375  25.891  -12.649  1.00 30.66  ? 200 THR D OG1 1 
ATOM   14320 C CG2 . THR D  1 200 ? -50.437  27.684  -11.455  1.00 29.64  ? 200 THR D CG2 1 
ATOM   14321 N N   . MET D  1 201 ? -52.530  23.727  -11.191  1.00 29.75  ? 201 MET D N   1 
ATOM   14322 C CA  . MET D  1 201 ? -53.650  22.821  -11.317  1.00 30.63  ? 201 MET D CA  1 
ATOM   14323 C C   . MET D  1 201 ? -53.338  21.476  -10.660  1.00 31.41  ? 201 MET D C   1 
ATOM   14324 O O   . MET D  1 201 ? -54.255  20.711  -10.341  1.00 29.20  ? 201 MET D O   1 
ATOM   14325 C CB  . MET D  1 201 ? -53.969  22.633  -12.806  1.00 32.56  ? 201 MET D CB  1 
ATOM   14326 C CG  . MET D  1 201 ? -54.498  23.881  -13.520  1.00 31.90  ? 201 MET D CG  1 
ATOM   14327 S SD  . MET D  1 201 ? -54.583  23.712  -15.311  1.00 30.27  ? 201 MET D SD  1 
ATOM   14328 C CE  . MET D  1 201 ? -52.976  24.485  -15.547  1.00 30.40  ? 201 MET D CE  1 
ATOM   14329 N N   . GLY D  1 202 ? -52.044  21.178  -10.463  1.00 29.77  ? 202 GLY D N   1 
ATOM   14330 C CA  . GLY D  1 202 ? -51.677  19.856  -9.985   1.00 28.38  ? 202 GLY D CA  1 
ATOM   14331 C C   . GLY D  1 202 ? -51.595  18.916  -11.177  1.00 29.43  ? 202 GLY D C   1 
ATOM   14332 O O   . GLY D  1 202 ? -52.134  19.266  -12.235  1.00 29.73  ? 202 GLY D O   1 
ATOM   14333 N N   . PHE D  1 203 ? -50.884  17.776  -11.019  1.00 28.60  ? 203 PHE D N   1 
ATOM   14334 C CA  . PHE D  1 203 ? -50.564  16.902  -12.143  1.00 28.00  ? 203 PHE D CA  1 
ATOM   14335 C C   . PHE D  1 203 ? -51.846  16.279  -12.688  1.00 26.50  ? 203 PHE D C   1 
ATOM   14336 O O   . PHE D  1 203 ? -52.131  16.356  -13.872  1.00 25.92  ? 203 PHE D O   1 
ATOM   14337 C CB  . PHE D  1 203 ? -49.570  15.806  -11.721  1.00 29.55  ? 203 PHE D CB  1 
ATOM   14338 C CG  . PHE D  1 203 ? -48.928  14.956  -12.811  1.00 28.44  ? 203 PHE D CG  1 
ATOM   14339 C CD1 . PHE D  1 203 ? -48.413  15.541  -13.977  1.00 30.05  ? 203 PHE D CD1 1 
ATOM   14340 C CD2 . PHE D  1 203 ? -48.735  13.593  -12.616  1.00 28.76  ? 203 PHE D CD2 1 
ATOM   14341 C CE1 . PHE D  1 203 ? -47.785  14.774  -14.957  1.00 29.57  ? 203 PHE D CE1 1 
ATOM   14342 C CE2 . PHE D  1 203 ? -48.096  12.821  -13.593  1.00 29.43  ? 203 PHE D CE2 1 
ATOM   14343 C CZ  . PHE D  1 203 ? -47.638  13.406  -14.762  1.00 30.08  ? 203 PHE D CZ  1 
ATOM   14344 N N   . LYS D  1 204 ? -52.624  15.623  -11.831  1.00 27.34  ? 204 LYS D N   1 
ATOM   14345 C CA  . LYS D  1 204 ? -53.872  15.026  -12.310  1.00 28.01  ? 204 LYS D CA  1 
ATOM   14346 C C   . LYS D  1 204 ? -54.715  16.062  -13.055  1.00 28.14  ? 204 LYS D C   1 
ATOM   14347 O O   . LYS D  1 204 ? -55.134  15.841  -14.183  1.00 30.56  ? 204 LYS D O   1 
ATOM   14348 C CB  . LYS D  1 204 ? -54.709  14.368  -11.202  1.00 28.01  ? 204 LYS D CB  1 
ATOM   14349 C CG  . LYS D  1 204 ? -56.168  14.016  -11.614  1.00 29.15  ? 204 LYS D CG  1 
ATOM   14350 C CD  . LYS D  1 204 ? -57.083  13.696  -10.434  1.00 28.05  ? 204 LYS D CD  1 
ATOM   14351 C CE  . LYS D  1 204 ? -58.545  13.513  -10.725  1.00 29.00  ? 204 LYS D CE  1 
ATOM   14352 N NZ  . LYS D  1 204 ? -59.329  13.341  -9.487   1.00 28.70  ? 204 LYS D NZ  1 
ATOM   14353 N N   . ASP D  1 205 ? -55.050  17.169  -12.410  1.00 29.20  ? 205 ASP D N   1 
ATOM   14354 C CA  . ASP D  1 205 ? -56.105  18.013  -12.959  1.00 30.89  ? 205 ASP D CA  1 
ATOM   14355 C C   . ASP D  1 205 ? -55.628  18.720  -14.226  1.00 30.12  ? 205 ASP D C   1 
ATOM   14356 O O   . ASP D  1 205 ? -56.421  18.960  -15.121  1.00 30.51  ? 205 ASP D O   1 
ATOM   14357 C CB  . ASP D  1 205 ? -56.685  18.959  -11.914  1.00 32.20  ? 205 ASP D CB  1 
ATOM   14358 C CG  . ASP D  1 205 ? -57.521  18.278  -10.846  1.00 32.83  ? 205 ASP D CG  1 
ATOM   14359 O OD1 . ASP D  1 205 ? -57.705  17.016  -10.966  1.00 31.34  ? 205 ASP D OD1 1 
ATOM   14360 O OD2 . ASP D  1 205 ? -57.967  19.011  -9.928   1.00 31.83  ? 205 ASP D OD2 1 
ATOM   14361 N N   . TYR D  1 206 ? -54.331  19.033  -14.316  1.00 31.53  ? 206 TYR D N   1 
ATOM   14362 C CA  . TYR D  1 206 ? -53.742  19.601  -15.522  1.00 29.89  ? 206 TYR D CA  1 
ATOM   14363 C C   . TYR D  1 206 ? -53.932  18.665  -16.707  1.00 26.57  ? 206 TYR D C   1 
ATOM   14364 O O   . TYR D  1 206 ? -54.458  19.056  -17.739  1.00 26.45  ? 206 TYR D O   1 
ATOM   14365 C CB  . TYR D  1 206 ? -52.230  19.842  -15.406  1.00 30.01  ? 206 TYR D CB  1 
ATOM   14366 C CG  . TYR D  1 206 ? -51.602  20.429  -16.664  1.00 28.54  ? 206 TYR D CG  1 
ATOM   14367 C CD1 . TYR D  1 206 ? -52.234  21.457  -17.354  1.00 28.65  ? 206 TYR D CD1 1 
ATOM   14368 C CD2 . TYR D  1 206 ? -50.413  19.930  -17.184  1.00 27.67  ? 206 TYR D CD2 1 
ATOM   14369 C CE1 . TYR D  1 206 ? -51.689  22.009  -18.503  1.00 28.23  ? 206 TYR D CE1 1 
ATOM   14370 C CE2 . TYR D  1 206 ? -49.840  20.489  -18.319  1.00 29.00  ? 206 TYR D CE2 1 
ATOM   14371 C CZ  . TYR D  1 206 ? -50.484  21.539  -18.979  1.00 29.66  ? 206 TYR D CZ  1 
ATOM   14372 O OH  . TYR D  1 206 ? -49.995  22.134  -20.104  1.00 29.08  ? 206 TYR D OH  1 
ATOM   14373 N N   . ILE D  1 207 ? -53.477  17.429  -16.560  1.00 25.66  ? 207 ILE D N   1 
ATOM   14374 C CA  . ILE D  1 207 ? -53.607  16.479  -17.656  1.00 25.30  ? 207 ILE D CA  1 
ATOM   14375 C C   . ILE D  1 207 ? -55.085  16.204  -17.914  1.00 24.83  ? 207 ILE D C   1 
ATOM   14376 O O   . ILE D  1 207 ? -55.513  16.165  -19.063  1.00 25.86  ? 207 ILE D O   1 
ATOM   14377 C CB  . ILE D  1 207 ? -52.802  15.196  -17.387  1.00 25.44  ? 207 ILE D CB  1 
ATOM   14378 C CG1 . ILE D  1 207 ? -51.311  15.493  -17.180  1.00 26.81  ? 207 ILE D CG1 1 
ATOM   14379 C CG2 . ILE D  1 207 ? -53.025  14.173  -18.503  1.00 26.56  ? 207 ILE D CG2 1 
ATOM   14380 C CD1 . ILE D  1 207 ? -50.665  16.353  -18.276  1.00 26.86  ? 207 ILE D CD1 1 
ATOM   14381 N N   . LYS D  1 208 ? -55.873  16.022  -16.851  1.00 26.52  ? 208 LYS D N   1 
ATOM   14382 C CA  . LYS D  1 208 ? -57.319  15.847  -16.979  1.00 27.80  ? 208 LYS D CA  1 
ATOM   14383 C C   . LYS D  1 208 ? -57.982  17.010  -17.716  1.00 27.44  ? 208 LYS D C   1 
ATOM   14384 O O   . LYS D  1 208 ? -58.940  16.813  -18.468  1.00 27.96  ? 208 LYS D O   1 
ATOM   14385 C CB  . LYS D  1 208 ? -57.927  15.788  -15.587  1.00 30.74  ? 208 LYS D CB  1 
ATOM   14386 C CG  . LYS D  1 208 ? -59.373  15.417  -15.545  1.00 35.22  ? 208 LYS D CG  1 
ATOM   14387 C CD  . LYS D  1 208 ? -59.902  15.288  -14.126  1.00 41.38  ? 208 LYS D CD  1 
ATOM   14388 C CE  . LYS D  1 208 ? -61.393  15.174  -14.187  1.00 50.01  ? 208 LYS D CE  1 
ATOM   14389 N NZ  . LYS D  1 208 ? -61.888  14.826  -12.858  1.00 58.33  ? 208 LYS D NZ  1 
ATOM   14390 N N   . GLY D  1 209 ? -57.506  18.233  -17.467  1.00 26.24  ? 209 GLY D N   1 
ATOM   14391 C CA  . GLY D  1 209 ? -58.095  19.400  -18.097  1.00 26.97  ? 209 GLY D CA  1 
ATOM   14392 C C   . GLY D  1 209 ? -57.899  19.377  -19.603  1.00 27.83  ? 209 GLY D C   1 
ATOM   14393 O O   . GLY D  1 209 ? -58.807  19.767  -20.326  1.00 27.74  ? 209 GLY D O   1 
ATOM   14394 N N   . LEU D  1 210 ? -56.716  18.913  -20.056  1.00 29.64  ? 210 LEU D N   1 
ATOM   14395 C CA  . LEU D  1 210 ? -56.416  18.789  -21.480  1.00 29.38  ? 210 LEU D CA  1 
ATOM   14396 C C   . LEU D  1 210 ? -57.290  17.726  -22.144  1.00 30.54  ? 210 LEU D C   1 
ATOM   14397 O O   . LEU D  1 210 ? -57.829  17.936  -23.225  1.00 30.13  ? 210 LEU D O   1 
ATOM   14398 C CB  . LEU D  1 210 ? -54.927  18.496  -21.649  1.00 28.16  ? 210 LEU D CB  1 
ATOM   14399 C CG  . LEU D  1 210 ? -53.974  19.582  -21.118  1.00 27.24  ? 210 LEU D CG  1 
ATOM   14400 C CD1 . LEU D  1 210 ? -52.500  19.224  -21.349  1.00 26.78  ? 210 LEU D CD1 1 
ATOM   14401 C CD2 . LEU D  1 210 ? -54.273  20.938  -21.708  1.00 26.18  ? 210 LEU D CD2 1 
ATOM   14402 N N   . ASN D  1 211 ? -57.457  16.586  -21.472  1.00 31.46  ? 211 ASN D N   1 
ATOM   14403 C CA  . ASN D  1 211 ? -58.316  15.516  -21.961  1.00 30.08  ? 211 ASN D CA  1 
ATOM   14404 C C   . ASN D  1 211 ? -59.724  16.062  -22.169  1.00 30.14  ? 211 ASN D C   1 
ATOM   14405 O O   . ASN D  1 211 ? -60.331  15.764  -23.188  1.00 31.08  ? 211 ASN D O   1 
ATOM   14406 C CB  . ASN D  1 211 ? -58.331  14.316  -21.010  1.00 30.82  ? 211 ASN D CB  1 
ATOM   14407 C CG  . ASN D  1 211 ? -58.829  13.038  -21.658  1.00 32.50  ? 211 ASN D CG  1 
ATOM   14408 O OD1 . ASN D  1 211 ? -58.573  12.788  -22.844  1.00 29.20  ? 211 ASN D OD1 1 
ATOM   14409 N ND2 . ASN D  1 211 ? -59.575  12.232  -20.909  1.00 34.30  ? 211 ASN D ND2 1 
ATOM   14410 N N   . GLU D  1 212 ? -60.233  16.861  -21.219  1.00 30.28  ? 212 GLU D N   1 
ATOM   14411 C CA  . GLU D  1 212 ? -61.583  17.418  -21.318  1.00 30.76  ? 212 GLU D CA  1 
ATOM   14412 C C   . GLU D  1 212 ? -61.648  18.437  -22.459  1.00 30.20  ? 212 GLU D C   1 
ATOM   14413 O O   . GLU D  1 212 ? -62.575  18.424  -23.268  1.00 29.47  ? 212 GLU D O   1 
ATOM   14414 C CB  . GLU D  1 212 ? -62.047  18.093  -20.030  1.00 32.05  ? 212 GLU D CB  1 
ATOM   14415 C CG  . GLU D  1 212 ? -62.310  17.119  -18.881  1.00 34.21  ? 212 GLU D CG  1 
ATOM   14416 C CD  . GLU D  1 212 ? -62.314  17.756  -17.486  1.00 35.60  ? 212 GLU D CD  1 
ATOM   14417 O OE1 . GLU D  1 212 ? -62.001  18.979  -17.393  1.00 34.53  ? 212 GLU D OE1 1 
ATOM   14418 O OE2 . GLU D  1 212 ? -62.637  17.028  -16.499  1.00 33.28  ? 212 GLU D OE2 1 
ATOM   14419 N N   . LEU D  1 213 ? -60.627  19.282  -22.583  1.00 29.03  ? 213 LEU D N   1 
ATOM   14420 C CA  . LEU D  1 213 ? -60.609  20.244  -23.679  1.00 29.93  ? 213 LEU D CA  1 
ATOM   14421 C C   . LEU D  1 213 ? -60.541  19.521  -25.029  1.00 29.53  ? 213 LEU D C   1 
ATOM   14422 O O   . LEU D  1 213 ? -61.038  20.029  -26.034  1.00 29.02  ? 213 LEU D O   1 
ATOM   14423 C CB  . LEU D  1 213 ? -59.451  21.220  -23.503  1.00 30.20  ? 213 LEU D CB  1 
ATOM   14424 C CG  . LEU D  1 213 ? -59.631  22.291  -22.420  1.00 31.23  ? 213 LEU D CG  1 
ATOM   14425 C CD1 . LEU D  1 213 ? -58.257  22.912  -22.129  1.00 30.03  ? 213 LEU D CD1 1 
ATOM   14426 C CD2 . LEU D  1 213 ? -60.646  23.396  -22.794  1.00 29.70  ? 213 LEU D CD2 1 
ATOM   14427 N N   . ASN D  1 214 ? -59.914  18.330  -25.057  1.00 30.41  ? 214 ASN D N   1 
ATOM   14428 C CA  . ASN D  1 214 ? -59.773  17.562  -26.290  1.00 29.46  ? 214 ASN D CA  1 
ATOM   14429 C C   . ASN D  1 214 ? -61.108  16.924  -26.675  1.00 30.24  ? 214 ASN D C   1 
ATOM   14430 O O   . ASN D  1 214 ? -61.266  16.563  -27.840  1.00 30.19  ? 214 ASN D O   1 
ATOM   14431 C CB  . ASN D  1 214 ? -58.652  16.542  -26.197  1.00 28.62  ? 214 ASN D CB  1 
ATOM   14432 C CG  . ASN D  1 214 ? -57.282  17.184  -26.245  1.00 28.03  ? 214 ASN D CG  1 
ATOM   14433 O OD1 . ASN D  1 214 ? -57.098  18.258  -26.824  1.00 27.21  ? 214 ASN D OD1 1 
ATOM   14434 N ND2 . ASN D  1 214 ? -56.280  16.491  -25.728  1.00 28.48  ? 214 ASN D ND2 1 
ATOM   14435 N N   . GLY D  1 215 ? -62.055  16.824  -25.721  1.00 29.56  ? 215 GLY D N   1 
ATOM   14436 C CA  . GLY D  1 215 ? -63.439  16.495  -26.042  1.00 31.29  ? 215 GLY D CA  1 
ATOM   14437 C C   . GLY D  1 215 ? -63.917  15.144  -25.489  1.00 32.37  ? 215 GLY D C   1 
ATOM   14438 O O   . GLY D  1 215 ? -65.065  14.776  -25.681  1.00 33.81  ? 215 GLY D O   1 
ATOM   14439 N N   . LEU D  1 216 ? -63.051  14.391  -24.802  1.00 33.66  ? 216 LEU D N   1 
ATOM   14440 C CA  . LEU D  1 216 ? -63.407  13.096  -24.224  1.00 33.16  ? 216 LEU D CA  1 
ATOM   14441 C C   . LEU D  1 216 ? -64.085  12.205  -25.267  1.00 32.61  ? 216 LEU D C   1 
ATOM   14442 O O   . LEU D  1 216 ? -64.966  11.421  -24.941  1.00 32.91  ? 216 LEU D O   1 
ATOM   14443 C CB  . LEU D  1 216 ? -64.303  13.280  -22.989  1.00 34.41  ? 216 LEU D CB  1 
ATOM   14444 C CG  . LEU D  1 216 ? -63.759  14.161  -21.851  1.00 31.41  ? 216 LEU D CG  1 
ATOM   14445 C CD1 . LEU D  1 216 ? -64.789  14.378  -20.737  1.00 30.34  ? 216 LEU D CD1 1 
ATOM   14446 C CD2 . LEU D  1 216 ? -62.514  13.505  -21.323  1.00 30.60  ? 216 LEU D CD2 1 
ATOM   14447 N N   . ASP D  1 217 ? -63.623  12.263  -26.514  1.00 33.63  ? 217 ASP D N   1 
ATOM   14448 C CA  . ASP D  1 217 ? -64.197  11.445  -27.571  1.00 34.84  ? 217 ASP D CA  1 
ATOM   14449 C C   . ASP D  1 217 ? -63.181  10.441  -28.137  1.00 35.21  ? 217 ASP D C   1 
ATOM   14450 O O   . ASP D  1 217 ? -63.466  9.776   -29.125  1.00 35.14  ? 217 ASP D O   1 
ATOM   14451 C CB  . ASP D  1 217 ? -64.808  12.339  -28.641  1.00 33.94  ? 217 ASP D CB  1 
ATOM   14452 C CG  . ASP D  1 217 ? -63.839  13.338  -29.243  1.00 35.34  ? 217 ASP D CG  1 
ATOM   14453 O OD1 . ASP D  1 217 ? -62.682  13.345  -28.801  1.00 35.23  ? 217 ASP D OD1 1 
ATOM   14454 O OD2 . ASP D  1 217 ? -64.266  14.155  -30.093  1.00 39.76  ? 217 ASP D OD2 1 
ATOM   14455 N N   . LYS D  1 218 ? -61.973  10.346  -27.567  1.00 36.11  ? 218 LYS D N   1 
ATOM   14456 C CA  . LYS D  1 218 ? -60.992  9.388   -28.055  1.00 35.33  ? 218 LYS D CA  1 
ATOM   14457 C C   . LYS D  1 218 ? -60.248  8.834   -26.861  1.00 32.78  ? 218 LYS D C   1 
ATOM   14458 O O   . LYS D  1 218 ? -60.329  9.435   -25.807  1.00 35.17  ? 218 LYS D O   1 
ATOM   14459 C CB  . LYS D  1 218 ? -59.957  9.950   -29.031  1.00 38.72  ? 218 LYS D CB  1 
ATOM   14460 C CG  . LYS D  1 218 ? -60.576  10.461  -30.311  1.00 43.04  ? 218 LYS D CG  1 
ATOM   14461 C CD  . LYS D  1 218 ? -59.663  11.233  -31.261  1.00 45.75  ? 218 LYS D CD  1 
ATOM   14462 C CE  . LYS D  1 218 ? -60.470  11.559  -32.508  1.00 46.30  ? 218 LYS D CE  1 
ATOM   14463 N NZ  . LYS D  1 218 ? -59.667  12.488  -33.295  1.00 47.89  ? 218 LYS D NZ  1 
ATOM   14464 N N   . PRO D  1 219 ? -59.600  7.653   -26.975  1.00 30.38  ? 219 PRO D N   1 
ATOM   14465 C CA  . PRO D  1 219 ? -58.755  7.127   -25.923  1.00 28.64  ? 219 PRO D CA  1 
ATOM   14466 C C   . PRO D  1 219 ? -57.613  8.085   -25.688  1.00 28.20  ? 219 PRO D C   1 
ATOM   14467 O O   . PRO D  1 219 ? -57.097  8.702   -26.619  1.00 29.67  ? 219 PRO D O   1 
ATOM   14468 C CB  . PRO D  1 219 ? -58.240  5.801   -26.477  1.00 29.64  ? 219 PRO D CB  1 
ATOM   14469 C CG  . PRO D  1 219 ? -59.288  5.386   -27.474  1.00 30.64  ? 219 PRO D CG  1 
ATOM   14470 C CD  . PRO D  1 219 ? -59.729  6.703   -28.091  1.00 31.72  ? 219 PRO D CD  1 
ATOM   14471 N N   . PHE D  1 220 ? -57.185  8.144   -24.434  1.00 27.90  ? 220 PHE D N   1 
ATOM   14472 C CA  . PHE D  1 220 ? -56.025  8.939   -24.075  1.00 27.31  ? 220 PHE D CA  1 
ATOM   14473 C C   . PHE D  1 220 ? -54.977  7.987   -23.501  1.00 26.72  ? 220 PHE D C   1 
ATOM   14474 O O   . PHE D  1 220 ? -55.311  7.207   -22.625  1.00 24.45  ? 220 PHE D O   1 
ATOM   14475 C CB  . PHE D  1 220 ? -56.465  9.990   -23.054  1.00 26.20  ? 220 PHE D CB  1 
ATOM   14476 C CG  . PHE D  1 220 ? -55.325  10.640  -22.305  1.00 28.88  ? 220 PHE D CG  1 
ATOM   14477 C CD1 . PHE D  1 220 ? -54.217  11.135  -22.982  1.00 31.71  ? 220 PHE D CD1 1 
ATOM   14478 C CD2 . PHE D  1 220 ? -55.332  10.729  -20.917  1.00 29.84  ? 220 PHE D CD2 1 
ATOM   14479 C CE1 . PHE D  1 220 ? -53.184  11.770  -22.292  1.00 30.73  ? 220 PHE D CE1 1 
ATOM   14480 C CE2 . PHE D  1 220 ? -54.260  11.296  -20.235  1.00 29.55  ? 220 PHE D CE2 1 
ATOM   14481 C CZ  . PHE D  1 220 ? -53.212  11.849  -20.927  1.00 29.67  ? 220 PHE D CZ  1 
ATOM   14482 N N   . ILE D  1 221 ? -53.722  8.100   -23.971  1.00 26.70  ? 221 ILE D N   1 
ATOM   14483 C CA  . ILE D  1 221 ? -52.606  7.329   -23.432  1.00 26.48  ? 221 ILE D CA  1 
ATOM   14484 C C   . ILE D  1 221 ? -51.489  8.304   -23.081  1.00 26.82  ? 221 ILE D C   1 
ATOM   14485 O O   . ILE D  1 221 ? -51.441  9.378   -23.690  1.00 25.36  ? 221 ILE D O   1 
ATOM   14486 C CB  . ILE D  1 221 ? -52.146  6.281   -24.457  1.00 25.89  ? 221 ILE D CB  1 
ATOM   14487 C CG1 . ILE D  1 221 ? -51.404  6.925   -25.604  1.00 25.99  ? 221 ILE D CG1 1 
ATOM   14488 C CG2 . ILE D  1 221 ? -53.362  5.458   -24.909  1.00 26.13  ? 221 ILE D CG2 1 
ATOM   14489 C CD1 . ILE D  1 221 ? -50.745  5.996   -26.596  1.00 27.57  ? 221 ILE D CD1 1 
ATOM   14490 N N   . THR D  1 222 ? -50.620  7.935   -22.122  1.00 25.53  ? 222 THR D N   1 
ATOM   14491 C CA  . THR D  1 222 ? -49.410  8.721   -21.915  1.00 26.13  ? 222 THR D CA  1 
ATOM   14492 C C   . THR D  1 222 ? -48.221  8.048   -22.597  1.00 28.40  ? 222 THR D C   1 
ATOM   14493 O O   . THR D  1 222 ? -48.074  6.820   -22.551  1.00 28.16  ? 222 THR D O   1 
ATOM   14494 C CB  . THR D  1 222 ? -49.147  8.946   -20.434  1.00 25.81  ? 222 THR D CB  1 
ATOM   14495 O OG1 . THR D  1 222 ? -48.802  7.694   -19.861  1.00 26.25  ? 222 THR D OG1 1 
ATOM   14496 C CG2 . THR D  1 222 ? -50.340  9.522   -19.698  1.00 26.28  ? 222 THR D CG2 1 
ATOM   14497 N N   . THR D  1 223 ? -47.369  8.871   -23.232  1.00 29.40  ? 223 THR D N   1 
ATOM   14498 C CA  . THR D  1 223 ? -46.284  8.327   -24.029  1.00 28.54  ? 223 THR D CA  1 
ATOM   14499 C C   . THR D  1 223 ? -44.946  8.509   -23.308  1.00 28.44  ? 223 THR D C   1 
ATOM   14500 O O   . THR D  1 223 ? -43.901  8.075   -23.816  1.00 26.70  ? 223 THR D O   1 
ATOM   14501 C CB  . THR D  1 223 ? -46.304  8.920   -25.441  1.00 28.44  ? 223 THR D CB  1 
ATOM   14502 O OG1 . THR D  1 223 ? -46.383  10.337  -25.369  1.00 27.02  ? 223 THR D OG1 1 
ATOM   14503 C CG2 . THR D  1 223 ? -47.469  8.387   -26.257  1.00 27.57  ? 223 THR D CG2 1 
ATOM   14504 N N   . ALA D  1 224 ? -45.001  9.098   -22.105  1.00 28.02  ? 224 ALA D N   1 
ATOM   14505 C CA  . ALA D  1 224 ? -43.842  9.191   -21.222  1.00 26.73  ? 224 ALA D CA  1 
ATOM   14506 C C   . ALA D  1 224 ? -44.227  9.835   -19.883  1.00 26.46  ? 224 ALA D C   1 
ATOM   14507 O O   . ALA D  1 224 ? -45.214  10.584  -19.779  1.00 23.87  ? 224 ALA D O   1 
ATOM   14508 C CB  . ALA D  1 224 ? -42.726  9.964   -21.890  1.00 28.90  ? 224 ALA D CB  1 
ATOM   14509 N N   . PHE D  1 225 ? -43.484  9.437   -18.835  1.00 26.64  ? 225 PHE D N   1 
ATOM   14510 C CA  . PHE D  1 225 ? -43.510  10.094  -17.540  1.00 26.76  ? 225 PHE D CA  1 
ATOM   14511 C C   . PHE D  1 225 ? -42.451  9.447   -16.661  1.00 28.63  ? 225 PHE D C   1 
ATOM   14512 O O   . PHE D  1 225 ? -42.273  8.241   -16.755  1.00 33.50  ? 225 PHE D O   1 
ATOM   14513 C CB  . PHE D  1 225 ? -44.867  9.976   -16.856  1.00 25.90  ? 225 PHE D CB  1 
ATOM   14514 C CG  . PHE D  1 225 ? -45.389  8.564   -16.642  1.00 25.96  ? 225 PHE D CG  1 
ATOM   14515 C CD1 . PHE D  1 225 ? -46.099  7.891   -17.631  1.00 25.19  ? 225 PHE D CD1 1 
ATOM   14516 C CD2 . PHE D  1 225 ? -45.237  7.931   -15.420  1.00 27.13  ? 225 PHE D CD2 1 
ATOM   14517 C CE1 . PHE D  1 225 ? -46.586  6.612   -17.413  1.00 24.60  ? 225 PHE D CE1 1 
ATOM   14518 C CE2 . PHE D  1 225 ? -45.743  6.653   -15.210  1.00 25.88  ? 225 PHE D CE2 1 
ATOM   14519 C CZ  . PHE D  1 225 ? -46.438  6.021   -16.198  1.00 24.87  ? 225 PHE D CZ  1 
ATOM   14520 N N   . GLY D  1 226 ? -41.811  10.202  -15.764  1.00 26.53  ? 226 GLY D N   1 
ATOM   14521 C CA  . GLY D  1 226 ? -40.795  9.594   -14.923  1.00 25.95  ? 226 GLY D CA  1 
ATOM   14522 C C   . GLY D  1 226 ? -39.830  10.633  -14.355  1.00 25.82  ? 226 GLY D C   1 
ATOM   14523 O O   . GLY D  1 226 ? -40.090  11.830  -14.474  1.00 24.20  ? 226 GLY D O   1 
ATOM   14524 N N   . TYR D  1 227 ? -38.741  10.130  -13.754  1.00 24.31  ? 227 TYR D N   1 
ATOM   14525 C CA  . TYR D  1 227 ? -37.819  10.872  -12.901  1.00 23.29  ? 227 TYR D CA  1 
ATOM   14526 C C   . TYR D  1 227 ? -36.411  10.345  -13.170  1.00 24.77  ? 227 TYR D C   1 
ATOM   14527 O O   . TYR D  1 227 ? -36.198  9.129   -13.370  1.00 23.44  ? 227 TYR D O   1 
ATOM   14528 C CB  . TYR D  1 227 ? -38.220  10.835  -11.412  1.00 24.43  ? 227 TYR D CB  1 
ATOM   14529 C CG  . TYR D  1 227 ? -39.556  11.531  -11.107  1.00 24.39  ? 227 TYR D CG  1 
ATOM   14530 C CD1 . TYR D  1 227 ? -39.651  12.931  -11.043  1.00 23.71  ? 227 TYR D CD1 1 
ATOM   14531 C CD2 . TYR D  1 227 ? -40.750  10.811  -10.962  1.00 23.00  ? 227 TYR D CD2 1 
ATOM   14532 C CE1 . TYR D  1 227 ? -40.879  13.565  -10.859  1.00 22.86  ? 227 TYR D CE1 1 
ATOM   14533 C CE2 . TYR D  1 227 ? -41.985  11.443  -10.796  1.00 23.49  ? 227 TYR D CE2 1 
ATOM   14534 C CZ  . TYR D  1 227 ? -42.051  12.833  -10.739  1.00 24.68  ? 227 TYR D CZ  1 
ATOM   14535 O OH  . TYR D  1 227 ? -43.252  13.490  -10.545  1.00 27.29  ? 227 TYR D OH  1 
ATOM   14536 N N   . SER D  1 228 ? -35.462  11.299  -13.165  1.00 25.10  ? 228 SER D N   1 
ATOM   14537 C CA  . SER D  1 228 ? -34.036  11.075  -13.393  1.00 24.39  ? 228 SER D CA  1 
ATOM   14538 C C   . SER D  1 228 ? -33.342  11.012  -12.040  1.00 26.34  ? 228 SER D C   1 
ATOM   14539 O O   . SER D  1 228 ? -33.630  11.858  -11.179  1.00 25.67  ? 228 SER D O   1 
ATOM   14540 C CB  . SER D  1 228 ? -33.437  12.197  -14.216  1.00 24.35  ? 228 SER D CB  1 
ATOM   14541 O OG  . SER D  1 228 ? -32.022  12.049  -14.365  1.00 24.49  ? 228 SER D OG  1 
ATOM   14542 N N   . VAL D  1 229 ? -32.401  10.057  -11.876  1.00 26.06  ? 229 VAL D N   1 
ATOM   14543 C CA  . VAL D  1 229 ? -31.649  9.906   -10.632  1.00 26.92  ? 229 VAL D CA  1 
ATOM   14544 C C   . VAL D  1 229 ? -30.173  10.308  -10.821  1.00 27.36  ? 229 VAL D C   1 
ATOM   14545 O O   . VAL D  1 229 ? -29.272  9.812   -10.147  1.00 25.25  ? 229 VAL D O   1 
ATOM   14546 C CB  . VAL D  1 229 ? -31.771  8.465   -10.086  1.00 28.16  ? 229 VAL D CB  1 
ATOM   14547 C CG1 . VAL D  1 229 ? -33.209  8.102   -9.766   1.00 27.32  ? 229 VAL D CG1 1 
ATOM   14548 C CG2 . VAL D  1 229 ? -31.126  7.415   -11.009  1.00 29.01  ? 229 VAL D CG2 1 
ATOM   14549 N N   . SER D  1 230 ? -29.927  11.281  -11.696  1.00 28.22  ? 230 SER D N   1 
ATOM   14550 C CA  . SER D  1 230 ? -28.596  11.826  -11.893  1.00 28.49  ? 230 SER D CA  1 
ATOM   14551 C C   . SER D  1 230 ? -28.008  12.280  -10.564  1.00 28.64  ? 230 SER D C   1 
ATOM   14552 O O   . SER D  1 230 ? -28.724  12.715  -9.670   1.00 28.43  ? 230 SER D O   1 
ATOM   14553 C CB  . SER D  1 230 ? -28.582  12.963  -12.899  1.00 29.09  ? 230 SER D CB  1 
ATOM   14554 O OG  . SER D  1 230 ? -29.440  14.006  -12.482  1.00 30.80  ? 230 SER D OG  1 
ATOM   14555 N N   . PRO D  1 231 ? -26.692  12.073  -10.361  1.00 28.05  ? 231 PRO D N   1 
ATOM   14556 C CA  . PRO D  1 231 ? -26.007  12.532  -9.168   1.00 28.14  ? 231 PRO D CA  1 
ATOM   14557 C C   . PRO D  1 231 ? -26.231  14.005  -8.918   1.00 29.27  ? 231 PRO D C   1 
ATOM   14558 O O   . PRO D  1 231 ? -26.332  14.393  -7.758   1.00 29.36  ? 231 PRO D O   1 
ATOM   14559 C CB  . PRO D  1 231 ? -24.555  12.250  -9.447   1.00 29.59  ? 231 PRO D CB  1 
ATOM   14560 C CG  . PRO D  1 231 ? -24.586  11.075  -10.381  1.00 30.79  ? 231 PRO D CG  1 
ATOM   14561 C CD  . PRO D  1 231 ? -25.852  11.231  -11.212  1.00 29.02  ? 231 PRO D CD  1 
ATOM   14562 N N   . GLU D  1 232 ? -26.246  14.796  -10.001  1.00 31.49  ? 232 GLU D N   1 
ATOM   14563 C CA  . GLU D  1 232 ? -26.484  16.240  -9.913   1.00 34.47  ? 232 GLU D CA  1 
ATOM   14564 C C   . GLU D  1 232 ? -27.062  16.778  -11.227  1.00 31.69  ? 232 GLU D C   1 
ATOM   14565 O O   . GLU D  1 232 ? -27.334  16.019  -12.162  1.00 30.20  ? 232 GLU D O   1 
ATOM   14566 C CB  . GLU D  1 232 ? -25.226  16.967  -9.414   1.00 37.69  ? 232 GLU D CB  1 
ATOM   14567 C CG  . GLU D  1 232 ? -24.024  16.820  -10.338  1.00 42.38  ? 232 GLU D CG  1 
ATOM   14568 C CD  . GLU D  1 232 ? -22.671  17.369  -9.897   1.00 45.17  ? 232 GLU D CD  1 
ATOM   14569 O OE1 . GLU D  1 232 ? -22.493  18.247  -9.013   1.00 49.59  ? 232 GLU D OE1 1 
ATOM   14570 O OE2 . GLU D  1 232 ? -21.747  16.832  -10.507  1.00 46.59  ? 232 GLU D OE2 1 
ATOM   14571 N N   . GLY D  1 233 ? -27.356  18.084  -11.239  1.00 30.33  ? 233 GLY D N   1 
ATOM   14572 C CA  . GLY D  1 233 ? -27.836  18.768  -12.424  1.00 28.92  ? 233 GLY D CA  1 
ATOM   14573 C C   . GLY D  1 233 ? -29.367  18.817  -12.485  1.00 28.29  ? 233 GLY D C   1 
ATOM   14574 O O   . GLY D  1 233 ? -30.045  18.214  -11.652  1.00 29.72  ? 233 GLY D O   1 
ATOM   14575 N N   . GLY D  1 234 ? -29.879  19.512  -13.520  1.00 27.54  ? 234 GLY D N   1 
ATOM   14576 C CA  . GLY D  1 234 ? -31.290  19.786  -13.720  1.00 28.76  ? 234 GLY D CA  1 
ATOM   14577 C C   . GLY D  1 234 ? -31.794  20.892  -12.792  1.00 30.00  ? 234 GLY D C   1 
ATOM   14578 O O   . GLY D  1 234 ? -31.070  21.814  -12.490  1.00 28.65  ? 234 GLY D O   1 
ATOM   14579 N N   . ASN D  1 235 ? -33.076  20.860  -12.422  1.00 31.69  ? 235 ASN D N   1 
ATOM   14580 C CA  A ASN D  1 235 ? -33.638  21.860  -11.522  0.50 31.77  ? 235 ASN D CA  1 
ATOM   14581 C CA  B ASN D  1 235 ? -33.682  21.893  -11.587  0.50 32.11  ? 235 ASN D CA  1 
ATOM   14582 C C   . ASN D  1 235 ? -34.873  21.262  -10.855  1.00 31.24  ? 235 ASN D C   1 
ATOM   14583 O O   . ASN D  1 235 ? -35.717  20.643  -11.515  1.00 27.38  ? 235 ASN D O   1 
ATOM   14584 C CB  A ASN D  1 235 ? -33.960  23.197  -12.202  0.50 31.52  ? 235 ASN D CB  1 
ATOM   14585 C CB  B ASN D  1 235 ? -33.974  23.177  -12.389  0.50 32.12  ? 235 ASN D CB  1 
ATOM   14586 C CG  A ASN D  1 235 ? -34.635  24.162  -11.248  0.50 31.56  ? 235 ASN D CG  1 
ATOM   14587 C CG  B ASN D  1 235 ? -35.169  23.112  -13.317  0.50 32.05  ? 235 ASN D CG  1 
ATOM   14588 O OD1 A ASN D  1 235 ? -34.035  24.637  -10.274  0.50 30.22  ? 235 ASN D OD1 1 
ATOM   14589 O OD1 B ASN D  1 235 ? -35.178  22.362  -14.302  0.50 35.06  ? 235 ASN D OD1 1 
ATOM   14590 N ND2 A ASN D  1 235 ? -35.905  24.437  -11.492  0.50 31.62  ? 235 ASN D ND2 1 
ATOM   14591 N ND2 B ASN D  1 235 ? -36.198  23.900  -13.037  0.50 30.77  ? 235 ASN D ND2 1 
ATOM   14592 N N   . GLY D  1 236 ? -34.938  21.458  -9.528   1.00 31.25  ? 236 GLY D N   1 
ATOM   14593 C CA  . GLY D  1 236 ? -35.972  20.868  -8.688   1.00 31.58  ? 236 GLY D CA  1 
ATOM   14594 C C   . GLY D  1 236 ? -36.029  19.342  -8.872   1.00 32.22  ? 236 GLY D C   1 
ATOM   14595 O O   . GLY D  1 236 ? -35.038  18.604  -8.686   1.00 30.47  ? 236 GLY D O   1 
ATOM   14596 N N   . GLN D  1 237 ? -37.198  18.888  -9.310   1.00 27.92  ? 237 GLN D N   1 
ATOM   14597 C CA  . GLN D  1 237 ? -37.430  17.472  -9.433   1.00 28.33  ? 237 GLN D CA  1 
ATOM   14598 C C   . GLN D  1 237 ? -36.921  16.949  -10.766  1.00 28.75  ? 237 GLN D C   1 
ATOM   14599 O O   . GLN D  1 237 ? -37.082  15.767  -11.043  1.00 28.42  ? 237 GLN D O   1 
ATOM   14600 C CB  . GLN D  1 237 ? -38.932  17.220  -9.347   1.00 28.72  ? 237 GLN D CB  1 
ATOM   14601 C CG  . GLN D  1 237 ? -39.484  17.264  -7.934   1.00 28.45  ? 237 GLN D CG  1 
ATOM   14602 C CD  . GLN D  1 237 ? -40.927  16.811  -7.888   1.00 28.79  ? 237 GLN D CD  1 
ATOM   14603 O OE1 . GLN D  1 237 ? -41.251  15.616  -8.023   1.00 27.16  ? 237 GLN D OE1 1 
ATOM   14604 N NE2 . GLN D  1 237 ? -41.802  17.786  -7.705   1.00 28.20  ? 237 GLN D NE2 1 
ATOM   14605 N N   . TYR D  1 238 ? -36.459  17.852  -11.637  1.00 28.40  ? 238 TYR D N   1 
ATOM   14606 C CA  . TYR D  1 238 ? -35.897  17.472  -12.921  1.00 28.67  ? 238 TYR D CA  1 
ATOM   14607 C C   . TYR D  1 238 ? -34.410  17.233  -12.710  1.00 28.83  ? 238 TYR D C   1 
ATOM   14608 O O   . TYR D  1 238 ? -33.651  18.152  -12.375  1.00 29.66  ? 238 TYR D O   1 
ATOM   14609 C CB  . TYR D  1 238 ? -36.060  18.491  -14.057  1.00 29.77  ? 238 TYR D CB  1 
ATOM   14610 C CG  . TYR D  1 238 ? -35.383  18.085  -15.365  1.00 29.81  ? 238 TYR D CG  1 
ATOM   14611 C CD1 . TYR D  1 238 ? -35.924  17.073  -16.156  1.00 28.28  ? 238 TYR D CD1 1 
ATOM   14612 C CD2 . TYR D  1 238 ? -34.190  18.686  -15.801  1.00 30.35  ? 238 TYR D CD2 1 
ATOM   14613 C CE1 . TYR D  1 238 ? -35.311  16.695  -17.338  1.00 28.22  ? 238 TYR D CE1 1 
ATOM   14614 C CE2 . TYR D  1 238 ? -33.557  18.300  -16.980  1.00 28.68  ? 238 TYR D CE2 1 
ATOM   14615 C CZ  . TYR D  1 238 ? -34.128  17.296  -17.747  1.00 28.80  ? 238 TYR D CZ  1 
ATOM   14616 O OH  . TYR D  1 238 ? -33.581  16.884  -18.925  1.00 29.50  ? 238 TYR D OH  1 
ATOM   14617 N N   . GLY D  1 239 ? -34.012  15.977  -12.911  1.00 28.79  ? 239 GLY D N   1 
ATOM   14618 C CA  . GLY D  1 239 ? -32.716  15.503  -12.450  1.00 29.73  ? 239 GLY D CA  1 
ATOM   14619 C C   . GLY D  1 239 ? -32.680  15.319  -10.939  1.00 27.75  ? 239 GLY D C   1 
ATOM   14620 O O   . GLY D  1 239 ? -33.636  15.663  -10.258  1.00 27.35  ? 239 GLY D O   1 
ATOM   14621 N N   . SER D  1 240 ? -31.591  14.700  -10.470  1.00 29.01  ? 240 SER D N   1 
ATOM   14622 C CA  . SER D  1 240 ? -31.115  14.735  -9.094   1.00 29.50  ? 240 SER D CA  1 
ATOM   14623 C C   . SER D  1 240 ? -32.054  14.059  -8.085   1.00 29.30  ? 240 SER D C   1 
ATOM   14624 O O   . SER D  1 240 ? -31.990  14.378  -6.899   1.00 30.94  ? 240 SER D O   1 
ATOM   14625 C CB  . SER D  1 240 ? -30.769  16.166  -8.695   1.00 30.03  ? 240 SER D CB  1 
ATOM   14626 O OG  . SER D  1 240 ? -29.649  16.644  -9.437   1.00 29.38  ? 240 SER D OG  1 
ATOM   14627 N N   . ASN D  1 241 ? -32.896  13.094  -8.496   1.00 29.53  ? 241 ASN D N   1 
ATOM   14628 C CA  . ASN D  1 241 ? -33.711  12.358  -7.524   1.00 28.87  ? 241 ASN D CA  1 
ATOM   14629 C C   . ASN D  1 241 ? -32.901  11.248  -6.855   1.00 27.17  ? 241 ASN D C   1 
ATOM   14630 O O   . ASN D  1 241 ? -31.951  10.772  -7.452   1.00 25.36  ? 241 ASN D O   1 
ATOM   14631 C CB  . ASN D  1 241 ? -34.953  11.745  -8.152   1.00 30.82  ? 241 ASN D CB  1 
ATOM   14632 C CG  . ASN D  1 241 ? -35.882  12.827  -8.624   1.00 30.01  ? 241 ASN D CG  1 
ATOM   14633 O OD1 . ASN D  1 241 ? -36.772  13.243  -7.902   1.00 29.91  ? 241 ASN D OD1 1 
ATOM   14634 N ND2 . ASN D  1 241 ? -35.639  13.344  -9.805   1.00 32.16  ? 241 ASN D ND2 1 
ATOM   14635 N N   . THR D  1 242 ? -33.278  10.848  -5.626   1.00 28.31  ? 242 THR D N   1 
ATOM   14636 C CA  . THR D  1 242 ? -32.844  9.567   -5.045   1.00 30.25  ? 242 THR D CA  1 
ATOM   14637 C C   . THR D  1 242 ? -33.576  8.411   -5.741   1.00 27.93  ? 242 THR D C   1 
ATOM   14638 O O   . THR D  1 242 ? -34.610  8.616   -6.371   1.00 25.55  ? 242 THR D O   1 
ATOM   14639 C CB  . THR D  1 242 ? -33.109  9.550   -3.538   1.00 31.89  ? 242 THR D CB  1 
ATOM   14640 O OG1 . THR D  1 242 ? -34.536  9.612   -3.364   1.00 28.68  ? 242 THR D OG1 1 
ATOM   14641 C CG2 . THR D  1 242 ? -32.381  10.696  -2.846   1.00 33.91  ? 242 THR D CG2 1 
ATOM   14642 N N   . LEU D  1 243 ? -33.039  7.201   -5.609   1.00 27.60  ? 243 LEU D N   1 
ATOM   14643 C CA  . LEU D  1 243 ? -33.667  5.994   -6.135   1.00 27.37  ? 243 LEU D CA  1 
ATOM   14644 C C   . LEU D  1 243 ? -35.062  5.856   -5.549   1.00 26.75  ? 243 LEU D C   1 
ATOM   14645 O O   . LEU D  1 243 ? -35.993  5.455   -6.238   1.00 26.21  ? 243 LEU D O   1 
ATOM   14646 C CB  . LEU D  1 243 ? -32.856  4.744   -5.802   1.00 30.00  ? 243 LEU D CB  1 
ATOM   14647 C CG  . LEU D  1 243 ? -31.442  4.654   -6.400   1.00 32.54  ? 243 LEU D CG  1 
ATOM   14648 C CD1 . LEU D  1 243 ? -30.744  3.354   -6.028   1.00 32.00  ? 243 LEU D CD1 1 
ATOM   14649 C CD2 . LEU D  1 243 ? -31.471  4.807   -7.909   1.00 33.36  ? 243 LEU D CD2 1 
ATOM   14650 N N   . LYS D  1 244 ? -35.185  6.208   -4.269   1.00 28.04  ? 244 LYS D N   1 
ATOM   14651 C CA  . LYS D  1 244 ? -36.458  6.186   -3.587   1.00 29.46  ? 244 LYS D CA  1 
ATOM   14652 C C   . LYS D  1 244 ? -37.408  7.233   -4.171   1.00 29.40  ? 244 LYS D C   1 
ATOM   14653 O O   . LYS D  1 244 ? -38.595  6.966   -4.344   1.00 34.97  ? 244 LYS D O   1 
ATOM   14654 C CB  . LYS D  1 244 ? -36.274  6.404   -2.083   1.00 32.42  ? 244 LYS D CB  1 
ATOM   14655 C CG  . LYS D  1 244 ? -37.532  6.037   -1.287   1.00 34.97  ? 244 LYS D CG  1 
ATOM   14656 C CD  . LYS D  1 244 ? -37.676  6.704   0.079    1.00 38.55  ? 244 LYS D CD  1 
ATOM   14657 C CE  . LYS D  1 244 ? -39.109  6.652   0.586    1.00 42.95  ? 244 LYS D CE  1 
ATOM   14658 N NZ  . LYS D  1 244 ? -39.768  5.379   0.208    1.00 46.60  ? 244 LYS D NZ  1 
ATOM   14659 N N   . GLN D  1 245 ? -36.929  8.445   -4.432   1.00 26.06  ? 245 GLN D N   1 
ATOM   14660 C CA  . GLN D  1 245 ? -37.808  9.436   -5.017   1.00 25.53  ? 245 GLN D CA  1 
ATOM   14661 C C   . GLN D  1 245 ? -38.259  8.999   -6.413   1.00 25.79  ? 245 GLN D C   1 
ATOM   14662 O O   . GLN D  1 245 ? -39.422  9.228   -6.788   1.00 24.95  ? 245 GLN D O   1 
ATOM   14663 C CB  . GLN D  1 245 ? -37.191  10.837  -5.074   1.00 24.84  ? 245 GLN D CB  1 
ATOM   14664 C CG  . GLN D  1 245 ? -37.035  11.481  -3.708   1.00 24.15  ? 245 GLN D CG  1 
ATOM   14665 C CD  . GLN D  1 245 ? -36.034  12.621  -3.754   1.00 26.57  ? 245 GLN D CD  1 
ATOM   14666 O OE1 . GLN D  1 245 ? -34.939  12.559  -4.333   1.00 25.19  ? 245 GLN D OE1 1 
ATOM   14667 N NE2 . GLN D  1 245 ? -36.456  13.735  -3.188   1.00 27.46  ? 245 GLN D NE2 1 
ATOM   14668 N N   . GLN D  1 246 ? -37.335  8.376   -7.176   1.00 26.18  ? 246 GLN D N   1 
ATOM   14669 C CA  . GLN D  1 246 ? -37.639  7.912   -8.522   1.00 25.67  ? 246 GLN D CA  1 
ATOM   14670 C C   . GLN D  1 246 ? -38.784  6.901   -8.434   1.00 25.65  ? 246 GLN D C   1 
ATOM   14671 O O   . GLN D  1 246 ? -39.777  7.004   -9.142   1.00 23.82  ? 246 GLN D O   1 
ATOM   14672 C CB  . GLN D  1 246 ? -36.386  7.342   -9.189   1.00 25.83  ? 246 GLN D CB  1 
ATOM   14673 C CG  . GLN D  1 246 ? -36.688  6.755   -10.569  1.00 27.52  ? 246 GLN D CG  1 
ATOM   14674 C CD  . GLN D  1 246 ? -35.601  5.877   -11.151  1.00 27.15  ? 246 GLN D CD  1 
ATOM   14675 O OE1 . GLN D  1 246 ? -35.059  4.988   -10.479  1.00 26.95  ? 246 GLN D OE1 1 
ATOM   14676 N NE2 . GLN D  1 246 ? -35.274  6.126   -12.411  1.00 27.13  ? 246 GLN D NE2 1 
ATOM   14677 N N   . SER D  1 247 ? -38.663  5.951   -7.496   1.00 27.55  ? 247 SER D N   1 
ATOM   14678 C CA  . SER D  1 247 ? -39.621  4.863   -7.353   1.00 26.82  ? 247 SER D CA  1 
ATOM   14679 C C   . SER D  1 247 ? -40.987  5.404   -6.925   1.00 27.44  ? 247 SER D C   1 
ATOM   14680 O O   . SER D  1 247 ? -42.023  5.071   -7.517   1.00 26.04  ? 247 SER D O   1 
ATOM   14681 C CB  . SER D  1 247 ? -39.098  3.830   -6.370   1.00 27.17  ? 247 SER D CB  1 
ATOM   14682 O OG  . SER D  1 247 ? -40.027  2.763   -6.229   1.00 29.31  ? 247 SER D OG  1 
ATOM   14683 N N   . ASP D  1 248 ? -40.988  6.190   -5.839   1.00 27.38  ? 248 ASP D N   1 
ATOM   14684 C CA  . ASP D  1 248 ? -42.222  6.705   -5.276   1.00 27.15  ? 248 ASP D CA  1 
ATOM   14685 C C   . ASP D  1 248 ? -42.940  7.583   -6.305   1.00 27.94  ? 248 ASP D C   1 
ATOM   14686 O O   . ASP D  1 248 ? -44.185  7.546   -6.408   1.00 27.76  ? 248 ASP D O   1 
ATOM   14687 C CB  . ASP D  1 248 ? -41.921  7.464   -4.000   1.00 28.79  ? 248 ASP D CB  1 
ATOM   14688 C CG  . ASP D  1 248 ? -41.487  6.587   -2.844   1.00 29.42  ? 248 ASP D CG  1 
ATOM   14689 O OD1 . ASP D  1 248 ? -41.585  5.341   -3.009   1.00 32.00  ? 248 ASP D OD1 1 
ATOM   14690 O OD2 . ASP D  1 248 ? -41.074  7.148   -1.807   1.00 26.08  ? 248 ASP D OD2 1 
ATOM   14691 N N   . GLY D  1 249 ? -42.136  8.343   -7.071   1.00 26.49  ? 249 GLY D N   1 
ATOM   14692 C CA  . GLY D  1 249 ? -42.643  9.246   -8.084   1.00 26.15  ? 249 GLY D CA  1 
ATOM   14693 C C   . GLY D  1 249 ? -43.285  8.535   -9.274   1.00 26.79  ? 249 GLY D C   1 
ATOM   14694 O O   . GLY D  1 249 ? -44.306  8.994   -9.797   1.00 27.94  ? 249 GLY D O   1 
ATOM   14695 N N   . LEU D  1 250 ? -42.662  7.459   -9.763   1.00 26.58  ? 250 LEU D N   1 
ATOM   14696 C CA  . LEU D  1 250 ? -43.300  6.678   -10.810  1.00 26.84  ? 250 LEU D CA  1 
ATOM   14697 C C   . LEU D  1 250 ? -44.702  6.224   -10.387  1.00 25.72  ? 250 LEU D C   1 
ATOM   14698 O O   . LEU D  1 250 ? -45.623  6.327   -11.191  1.00 26.60  ? 250 LEU D O   1 
ATOM   14699 C CB  . LEU D  1 250 ? -42.467  5.495   -11.286  1.00 26.32  ? 250 LEU D CB  1 
ATOM   14700 C CG  . LEU D  1 250 ? -41.576  5.736   -12.501  1.00 26.91  ? 250 LEU D CG  1 
ATOM   14701 C CD1 . LEU D  1 250 ? -42.347  6.065   -13.743  1.00 26.50  ? 250 LEU D CD1 1 
ATOM   14702 C CD2 . LEU D  1 250 ? -40.556  6.829   -12.197  1.00 29.33  ? 250 LEU D CD2 1 
ATOM   14703 N N   . ILE D  1 251 ? -44.863  5.775   -9.138   1.00 25.38  ? 251 ILE D N   1 
ATOM   14704 C CA  . ILE D  1 251 ? -46.127  5.223   -8.659   1.00 27.25  ? 251 ILE D CA  1 
ATOM   14705 C C   . ILE D  1 251 ? -47.135  6.367   -8.510   1.00 26.90  ? 251 ILE D C   1 
ATOM   14706 O O   . ILE D  1 251 ? -48.325  6.197   -8.769   1.00 27.59  ? 251 ILE D O   1 
ATOM   14707 C CB  . ILE D  1 251 ? -45.946  4.431   -7.340   1.00 28.06  ? 251 ILE D CB  1 
ATOM   14708 C CG1 . ILE D  1 251 ? -44.959  3.308   -7.482   1.00 30.43  ? 251 ILE D CG1 1 
ATOM   14709 C CG2 . ILE D  1 251 ? -47.264  3.899   -6.784   1.00 28.47  ? 251 ILE D CG2 1 
ATOM   14710 C CD1 . ILE D  1 251 ? -45.290  2.302   -8.556   1.00 31.77  ? 251 ILE D CD1 1 
ATOM   14711 N N   . SER D  1 252 ? -46.659  7.524   -8.045   1.00 25.60  ? 252 SER D N   1 
ATOM   14712 C CA  . SER D  1 252 ? -47.514  8.687   -7.879   1.00 25.67  ? 252 SER D CA  1 
ATOM   14713 C C   . SER D  1 252 ? -48.045  9.120   -9.256   1.00 25.77  ? 252 SER D C   1 
ATOM   14714 O O   . SER D  1 252 ? -49.257  9.390   -9.428   1.00 22.74  ? 252 SER D O   1 
ATOM   14715 C CB  . SER D  1 252 ? -46.777  9.802   -7.146   1.00 25.98  ? 252 SER D CB  1 
ATOM   14716 O OG  . SER D  1 252 ? -47.379  11.065  -7.397   1.00 26.84  ? 252 SER D OG  1 
ATOM   14717 N N   . ASN D  1 253 ? -47.138  9.135   -10.251  1.00 24.12  ? 253 ASN D N   1 
ATOM   14718 C CA  . ASN D  1 253 ? -47.525  9.540   -11.591  1.00 24.43  ? 253 ASN D CA  1 
ATOM   14719 C C   . ASN D  1 253 ? -48.508  8.517   -12.169  1.00 26.03  ? 253 ASN D C   1 
ATOM   14720 O O   . ASN D  1 253 ? -49.427  8.901   -12.900  1.00 27.45  ? 253 ASN D O   1 
ATOM   14721 C CB  . ASN D  1 253 ? -46.367  9.609   -12.579  1.00 24.66  ? 253 ASN D CB  1 
ATOM   14722 C CG  . ASN D  1 253 ? -45.326  10.641  -12.253  1.00 25.04  ? 253 ASN D CG  1 
ATOM   14723 O OD1 . ASN D  1 253 ? -45.488  11.450  -11.320  1.00 27.38  ? 253 ASN D OD1 1 
ATOM   14724 N ND2 . ASN D  1 253 ? -44.265  10.632  -13.039  1.00 23.73  ? 253 ASN D ND2 1 
ATOM   14725 N N   . TYR D  1 254 ? -48.363  7.225   -11.865  1.00 25.23  ? 254 TYR D N   1 
ATOM   14726 C CA  . TYR D  1 254 ? -49.246  6.190   -12.477  1.00 26.33  ? 254 TYR D CA  1 
ATOM   14727 C C   . TYR D  1 254 ? -50.698  6.402   -12.008  1.00 24.68  ? 254 TYR D C   1 
ATOM   14728 O O   . TYR D  1 254 ? -51.586  6.372   -12.854  1.00 27.16  ? 254 TYR D O   1 
ATOM   14729 C CB  . TYR D  1 254 ? -48.708  4.773   -12.235  1.00 27.18  ? 254 TYR D CB  1 
ATOM   14730 C CG  . TYR D  1 254 ? -48.911  3.781   -13.370  1.00 26.90  ? 254 TYR D CG  1 
ATOM   14731 C CD1 . TYR D  1 254 ? -50.171  3.283   -13.671  1.00 27.60  ? 254 TYR D CD1 1 
ATOM   14732 C CD2 . TYR D  1 254 ? -47.839  3.333   -14.126  1.00 26.31  ? 254 TYR D CD2 1 
ATOM   14733 C CE1 . TYR D  1 254 ? -50.362  2.379   -14.700  1.00 28.55  ? 254 TYR D CE1 1 
ATOM   14734 C CE2 . TYR D  1 254 ? -48.017  2.429   -15.158  1.00 28.37  ? 254 TYR D CE2 1 
ATOM   14735 C CZ  . TYR D  1 254 ? -49.281  1.947   -15.445  1.00 27.65  ? 254 TYR D CZ  1 
ATOM   14736 O OH  . TYR D  1 254 ? -49.464  1.058   -16.461  1.00 24.53  ? 254 TYR D OH  1 
ATOM   14737 N N   . ARG D  1 255 ? -50.907  6.624   -10.717  1.00 23.98  ? 255 ARG D N   1 
ATOM   14738 C CA  . ARG D  1 255 ? -52.254  6.913   -10.173  1.00 24.93  ? 255 ARG D CA  1 
ATOM   14739 C C   . ARG D  1 255 ? -52.816  8.187   -10.816  1.00 24.98  ? 255 ARG D C   1 
ATOM   14740 O O   . ARG D  1 255 ? -53.866  8.106   -11.441  1.00 23.21  ? 255 ARG D O   1 
ATOM   14741 C CB  . ARG D  1 255 ? -52.126  7.047   -8.655   1.00 25.78  ? 255 ARG D CB  1 
ATOM   14742 C CG  . ARG D  1 255 ? -53.329  7.507   -7.848   1.00 27.56  ? 255 ARG D CG  1 
ATOM   14743 C CD  . ARG D  1 255 ? -54.312  6.375   -7.644   1.00 30.47  ? 255 ARG D CD  1 
ATOM   14744 N NE  . ARG D  1 255 ? -55.363  6.399   -8.662   1.00 29.52  ? 255 ARG D NE  1 
ATOM   14745 C CZ  . ARG D  1 255 ? -55.647  5.421   -9.502   1.00 32.44  ? 255 ARG D CZ  1 
ATOM   14746 N NH1 . ARG D  1 255 ? -55.078  4.238   -9.373   1.00 30.73  ? 255 ARG D NH1 1 
ATOM   14747 N NH2 . ARG D  1 255 ? -56.519  5.634   -10.463  1.00 33.20  ? 255 ARG D NH2 1 
ATOM   14748 N N   . ASP D  1 256 ? -52.097  9.293   -10.698  1.00 25.88  ? 256 ASP D N   1 
ATOM   14749 C CA  . ASP D  1 256 ? -52.547  10.607  -11.218  1.00 26.14  ? 256 ASP D CA  1 
ATOM   14750 C C   . ASP D  1 256 ? -52.898  10.510  -12.704  1.00 26.69  ? 256 ASP D C   1 
ATOM   14751 O O   . ASP D  1 256 ? -53.898  11.109  -13.096  1.00 26.00  ? 256 ASP D O   1 
ATOM   14752 C CB  . ASP D  1 256 ? -51.519  11.683  -10.890  1.00 26.52  ? 256 ASP D CB  1 
ATOM   14753 C CG  . ASP D  1 256 ? -51.219  11.927  -9.423   1.00 26.85  ? 256 ASP D CG  1 
ATOM   14754 O OD1 . ASP D  1 256 ? -51.882  11.312  -8.576   1.00 29.37  ? 256 ASP D OD1 1 
ATOM   14755 O OD2 . ASP D  1 256 ? -50.322  12.737  -9.148   1.00 28.49  ? 256 ASP D OD2 1 
ATOM   14756 N N   . LEU D  1 257 ? -52.113  9.783   -13.498  1.00 26.74  ? 257 LEU D N   1 
ATOM   14757 C CA  . LEU D  1 257 ? -52.397  9.788   -14.924  1.00 26.70  ? 257 LEU D CA  1 
ATOM   14758 C C   . LEU D  1 257 ? -53.610  8.911   -15.206  1.00 27.93  ? 257 LEU D C   1 
ATOM   14759 O O   . LEU D  1 257 ? -54.443  9.284   -16.030  1.00 28.24  ? 257 LEU D O   1 
ATOM   14760 C CB  . LEU D  1 257 ? -51.164  9.389   -15.725  1.00 26.87  ? 257 LEU D CB  1 
ATOM   14761 C CG  . LEU D  1 257 ? -49.994  10.383  -15.655  1.00 26.85  ? 257 LEU D CG  1 
ATOM   14762 C CD1 . LEU D  1 257 ? -48.663  9.778   -16.164  1.00 26.18  ? 257 LEU D CD1 1 
ATOM   14763 C CD2 . LEU D  1 257 ? -50.353  11.693  -16.385  1.00 25.36  ? 257 LEU D CD2 1 
ATOM   14764 N N   . ILE D  1 258 ? -53.748  7.771   -14.498  1.00 28.66  ? 258 ILE D N   1 
ATOM   14765 C CA  . ILE D  1 258 ? -54.995  7.009   -14.605  1.00 28.74  ? 258 ILE D CA  1 
ATOM   14766 C C   . ILE D  1 258 ? -56.141  7.954   -14.243  1.00 27.91  ? 258 ILE D C   1 
ATOM   14767 O O   . ILE D  1 258 ? -57.170  7.994   -14.904  1.00 28.77  ? 258 ILE D O   1 
ATOM   14768 C CB  . ILE D  1 258 ? -54.994  5.722   -13.740  1.00 28.44  ? 258 ILE D CB  1 
ATOM   14769 C CG1 . ILE D  1 258 ? -53.957  4.669   -14.248  1.00 29.89  ? 258 ILE D CG1 1 
ATOM   14770 C CG2 . ILE D  1 258 ? -56.377  5.088   -13.677  1.00 27.91  ? 258 ILE D CG2 1 
ATOM   14771 C CD1 . ILE D  1 258 ? -53.835  3.403   -13.406  1.00 28.20  ? 258 ILE D CD1 1 
ATOM   14772 N N   . ASP D  1 259 ? -55.935  8.733   -13.182  1.00 28.26  ? 259 ASP D N   1 
ATOM   14773 C CA  . ASP D  1 259 ? -56.983  9.560   -12.612  1.00 30.64  ? 259 ASP D CA  1 
ATOM   14774 C C   . ASP D  1 259 ? -57.426  10.655  -13.584  1.00 28.59  ? 259 ASP D C   1 
ATOM   14775 O O   . ASP D  1 259 ? -58.494  11.211  -13.405  1.00 27.48  ? 259 ASP D O   1 
ATOM   14776 C CB  . ASP D  1 259 ? -56.571  10.120  -11.264  1.00 31.82  ? 259 ASP D CB  1 
ATOM   14777 C CG  . ASP D  1 259 ? -56.513  9.110   -10.126  1.00 33.40  ? 259 ASP D CG  1 
ATOM   14778 O OD1 . ASP D  1 259 ? -57.373  8.160   -10.097  1.00 32.27  ? 259 ASP D OD1 1 
ATOM   14779 O OD2 . ASP D  1 259 ? -55.650  9.314   -9.246   1.00 31.80  ? 259 ASP D OD2 1 
ATOM   14780 N N   . ALA D  1 260 ? -56.612  10.911  -14.603  1.00 28.85  ? 260 ALA D N   1 
ATOM   14781 C CA  . ALA D  1 260 ? -56.875  11.932  -15.595  1.00 30.79  ? 260 ALA D CA  1 
ATOM   14782 C C   . ALA D  1 260 ? -57.521  11.315  -16.828  1.00 29.55  ? 260 ALA D C   1 
ATOM   14783 O O   . ALA D  1 260 ? -57.828  12.032  -17.773  1.00 28.83  ? 260 ALA D O   1 
ATOM   14784 C CB  . ALA D  1 260 ? -55.574  12.643  -15.945  1.00 32.28  ? 260 ALA D CB  1 
ATOM   14785 N N   . GLY D  1 261 ? -57.748  9.993   -16.799  1.00 28.38  ? 261 GLY D N   1 
ATOM   14786 C CA  . GLY D  1 261 ? -58.485  9.300   -17.854  1.00 27.10  ? 261 GLY D CA  1 
ATOM   14787 C C   . GLY D  1 261 ? -57.597  8.440   -18.771  1.00 27.10  ? 261 GLY D C   1 
ATOM   14788 O O   . GLY D  1 261 ? -58.079  7.938   -19.778  1.00 30.96  ? 261 GLY D O   1 
ATOM   14789 N N   . ALA D  1 262 ? -56.309  8.256   -18.466  1.00 25.31  ? 262 ALA D N   1 
ATOM   14790 C CA  . ALA D  1 262 ? -55.450  7.409   -19.284  1.00 26.04  ? 262 ALA D CA  1 
ATOM   14791 C C   . ALA D  1 262 ? -55.891  5.937   -19.303  1.00 25.81  ? 262 ALA D C   1 
ATOM   14792 O O   . ALA D  1 262 ? -56.229  5.346   -18.287  1.00 24.64  ? 262 ALA D O   1 
ATOM   14793 C CB  . ALA D  1 262 ? -54.019  7.497   -18.783  1.00 26.57  ? 262 ALA D CB  1 
ATOM   14794 N N   . VAL D  1 263 ? -55.849  5.335   -20.488  1.00 26.84  ? 263 VAL D N   1 
ATOM   14795 C CA  . VAL D  1 263 ? -56.187  3.932   -20.664  1.00 28.61  ? 263 VAL D CA  1 
ATOM   14796 C C   . VAL D  1 263 ? -55.008  3.203   -21.276  1.00 27.88  ? 263 VAL D C   1 
ATOM   14797 O O   . VAL D  1 263 ? -55.164  2.082   -21.721  1.00 28.67  ? 263 VAL D O   1 
ATOM   14798 C CB  . VAL D  1 263 ? -57.443  3.730   -21.526  1.00 29.65  ? 263 VAL D CB  1 
ATOM   14799 C CG1 . VAL D  1 263 ? -58.670  4.239   -20.813  1.00 28.74  ? 263 VAL D CG1 1 
ATOM   14800 C CG2 . VAL D  1 263 ? -57.297  4.383   -22.894  1.00 31.65  ? 263 VAL D CG2 1 
ATOM   14801 N N   . GLY D  1 264 ? -53.849  3.865   -21.294  1.00 29.38  ? 264 GLY D N   1 
ATOM   14802 C CA  . GLY D  1 264 ? -52.596  3.335   -21.819  1.00 29.27  ? 264 GLY D CA  1 
ATOM   14803 C C   . GLY D  1 264 ? -51.472  4.144   -21.189  1.00 29.28  ? 264 GLY D C   1 
ATOM   14804 O O   . GLY D  1 264 ? -51.636  5.348   -21.005  1.00 30.03  ? 264 GLY D O   1 
ATOM   14805 N N   . MET D  1 265 ? -50.398  3.487   -20.760  1.00 30.39  ? 265 MET D N   1 
ATOM   14806 C CA  . MET D  1 265 ? -49.341  4.174   -20.030  1.00 29.50  ? 265 MET D CA  1 
ATOM   14807 C C   . MET D  1 265 ? -47.960  3.731   -20.517  1.00 32.13  ? 265 MET D C   1 
ATOM   14808 O O   . MET D  1 265 ? -47.653  2.534   -20.625  1.00 31.47  ? 265 MET D O   1 
ATOM   14809 C CB  . MET D  1 265 ? -49.468  3.869   -18.536  1.00 29.48  ? 265 MET D CB  1 
ATOM   14810 C CG  . MET D  1 265 ? -50.770  4.365   -17.926  1.00 32.04  ? 265 MET D CG  1 
ATOM   14811 S SD  . MET D  1 265 ? -50.857  6.155   -17.635  1.00 29.15  ? 265 MET D SD  1 
ATOM   14812 C CE  . MET D  1 265 ? -49.856  6.093   -16.142  1.00 30.62  ? 265 MET D CE  1 
ATOM   14813 N N   . CYS D  1 266 ? -47.096  4.720   -20.744  1.00 31.59  ? 266 CYS D N   1 
ATOM   14814 C CA  . CYS D  1 266 ? -45.752  4.486   -21.239  1.00 32.60  ? 266 CYS D CA  1 
ATOM   14815 C C   . CYS D  1 266 ? -44.730  5.098   -20.275  1.00 30.80  ? 266 CYS D C   1 
ATOM   14816 O O   . CYS D  1 266 ? -43.988  6.015   -20.614  1.00 27.74  ? 266 CYS D O   1 
ATOM   14817 C CB  . CYS D  1 266 ? -45.562  5.089   -22.636  1.00 33.99  ? 266 CYS D CB  1 
ATOM   14818 S SG  . CYS D  1 266 ? -46.576  4.334   -23.941  1.00 32.07  ? 266 CYS D SG  1 
ATOM   14819 N N   . PRO D  1 267 ? -44.571  4.553   -19.057  1.00 30.41  ? 267 PRO D N   1 
ATOM   14820 C CA  . PRO D  1 267 ? -43.557  5.065   -18.137  1.00 28.73  ? 267 PRO D CA  1 
ATOM   14821 C C   . PRO D  1 267 ? -42.202  5.173   -18.834  1.00 29.38  ? 267 PRO D C   1 
ATOM   14822 O O   . PRO D  1 267 ? -41.841  4.307   -19.625  1.00 30.48  ? 267 PRO D O   1 
ATOM   14823 C CB  . PRO D  1 267 ? -43.560  4.022   -16.965  1.00 29.20  ? 267 PRO D CB  1 
ATOM   14824 C CG  . PRO D  1 267 ? -44.360  2.832   -17.476  1.00 28.65  ? 267 PRO D CG  1 
ATOM   14825 C CD  . PRO D  1 267 ? -45.278  3.371   -18.550  1.00 30.57  ? 267 PRO D CD  1 
ATOM   14826 N N   . PHE D  1 268 ? -41.427  6.209   -18.492  1.00 29.06  ? 268 PHE D N   1 
ATOM   14827 C CA  . PHE D  1 268 ? -40.140  6.450   -19.118  1.00 27.97  ? 268 PHE D CA  1 
ATOM   14828 C C   . PHE D  1 268 ? -39.040  6.126   -18.113  1.00 27.75  ? 268 PHE D C   1 
ATOM   14829 O O   . PHE D  1 268 ? -38.919  6.799   -17.093  1.00 29.52  ? 268 PHE D O   1 
ATOM   14830 C CB  . PHE D  1 268 ? -40.142  7.891   -19.630  1.00 26.80  ? 268 PHE D CB  1 
ATOM   14831 C CG  . PHE D  1 268 ? -38.905  8.229   -20.431  1.00 26.74  ? 268 PHE D CG  1 
ATOM   14832 C CD1 . PHE D  1 268 ? -37.747  8.680   -19.794  1.00 29.98  ? 268 PHE D CD1 1 
ATOM   14833 C CD2 . PHE D  1 268 ? -38.885  8.081   -21.802  1.00 26.87  ? 268 PHE D CD2 1 
ATOM   14834 C CE1 . PHE D  1 268 ? -36.588  8.950   -20.520  1.00 30.23  ? 268 PHE D CE1 1 
ATOM   14835 C CE2 . PHE D  1 268 ? -37.712  8.333   -22.520  1.00 29.96  ? 268 PHE D CE2 1 
ATOM   14836 C CZ  . PHE D  1 268 ? -36.563  8.749   -21.883  1.00 28.79  ? 268 PHE D CZ  1 
ATOM   14837 N N   . TYR D  1 269 ? -38.210  5.103   -18.347  1.00 27.60  ? 269 TYR D N   1 
ATOM   14838 C CA  . TYR D  1 269 ? -38.197  4.148   -19.455  1.00 27.87  ? 269 TYR D CA  1 
ATOM   14839 C C   . TYR D  1 269 ? -37.215  3.051   -19.028  1.00 26.46  ? 269 TYR D C   1 
ATOM   14840 O O   . TYR D  1 269 ? -36.639  3.133   -17.941  1.00 27.08  ? 269 TYR D O   1 
ATOM   14841 C CB  . TYR D  1 269 ? -37.805  4.739   -20.823  1.00 28.86  ? 269 TYR D CB  1 
ATOM   14842 C CG  . TYR D  1 269 ? -36.361  5.211   -21.066  1.00 27.81  ? 269 TYR D CG  1 
ATOM   14843 C CD1 . TYR D  1 269 ? -35.507  5.620   -20.038  1.00 28.07  ? 269 TYR D CD1 1 
ATOM   14844 C CD2 . TYR D  1 269 ? -35.876  5.356   -22.364  1.00 27.50  ? 269 TYR D CD2 1 
ATOM   14845 C CE1 . TYR D  1 269 ? -34.206  6.054   -20.295  1.00 27.07  ? 269 TYR D CE1 1 
ATOM   14846 C CE2 . TYR D  1 269 ? -34.584  5.803   -22.634  1.00 26.78  ? 269 TYR D CE2 1 
ATOM   14847 C CZ  . TYR D  1 269 ? -33.745  6.164   -21.596  1.00 25.93  ? 269 TYR D CZ  1 
ATOM   14848 O OH  . TYR D  1 269 ? -32.467  6.587   -21.863  1.00 27.52  ? 269 TYR D OH  1 
ATOM   14849 N N   . TYR D  1 270 ? -36.981  2.070   -19.899  1.00 28.50  ? 270 TYR D N   1 
ATOM   14850 C CA  . TYR D  1 270 ? -36.299  0.829   -19.552  1.00 27.61  ? 270 TYR D CA  1 
ATOM   14851 C C   . TYR D  1 270 ? -34.900  1.070   -18.984  1.00 28.06  ? 270 TYR D C   1 
ATOM   14852 O O   . TYR D  1 270 ? -34.615  0.624   -17.871  1.00 26.82  ? 270 TYR D O   1 
ATOM   14853 C CB  . TYR D  1 270 ? -36.224  -0.056  -20.793  1.00 28.64  ? 270 TYR D CB  1 
ATOM   14854 C CG  . TYR D  1 270 ? -35.365  -1.313  -20.640  1.00 28.21  ? 270 TYR D CG  1 
ATOM   14855 C CD1 . TYR D  1 270 ? -35.673  -2.259  -19.688  1.00 28.46  ? 270 TYR D CD1 1 
ATOM   14856 C CD2 . TYR D  1 270 ? -34.286  -1.556  -21.470  1.00 29.33  ? 270 TYR D CD2 1 
ATOM   14857 C CE1 . TYR D  1 270 ? -34.938  -3.421  -19.576  1.00 30.51  ? 270 TYR D CE1 1 
ATOM   14858 C CE2 . TYR D  1 270 ? -33.518  -2.701  -21.356  1.00 31.34  ? 270 TYR D CE2 1 
ATOM   14859 C CZ  . TYR D  1 270 ? -33.868  -3.650  -20.418  1.00 31.85  ? 270 TYR D CZ  1 
ATOM   14860 O OH  . TYR D  1 270 ? -33.137  -4.784  -20.231  1.00 34.98  ? 270 TYR D OH  1 
ATOM   14861 N N   . ALA D  1 271 ? -34.008  1.740   -19.735  1.00 27.82  ? 271 ALA D N   1 
ATOM   14862 C CA  . ALA D  1 271 ? -32.619  1.794   -19.282  1.00 28.37  ? 271 ALA D CA  1 
ATOM   14863 C C   . ALA D  1 271 ? -31.931  3.099   -19.694  1.00 27.71  ? 271 ALA D C   1 
ATOM   14864 O O   . ALA D  1 271 ? -32.184  3.669   -20.752  1.00 27.58  ? 271 ALA D O   1 
ATOM   14865 C CB  . ALA D  1 271 ? -31.837  0.578   -19.780  1.00 28.20  ? 271 ALA D CB  1 
ATOM   14866 N N   . ASP D  1 272 ? -30.987  3.507   -18.863  1.00 28.10  ? 272 ASP D N   1 
ATOM   14867 C CA  . ASP D  1 272 ? -30.192  4.699   -19.105  1.00 29.50  ? 272 ASP D CA  1 
ATOM   14868 C C   . ASP D  1 272 ? -29.576  4.698   -20.503  1.00 30.14  ? 272 ASP D C   1 
ATOM   14869 O O   . ASP D  1 272 ? -29.076  3.673   -20.990  1.00 29.84  ? 272 ASP D O   1 
ATOM   14870 C CB  . ASP D  1 272 ? -29.043  4.800   -18.116  1.00 29.23  ? 272 ASP D CB  1 
ATOM   14871 C CG  . ASP D  1 272 ? -29.416  5.238   -16.712  1.00 30.40  ? 272 ASP D CG  1 
ATOM   14872 O OD1 . ASP D  1 272 ? -30.584  5.668   -16.488  1.00 32.10  ? 272 ASP D OD1 1 
ATOM   14873 O OD2 . ASP D  1 272 ? -28.522  5.158   -15.850  1.00 34.28  ? 272 ASP D OD2 1 
ATOM   14874 N N   . GLY D  1 273 ? -29.592  5.888   -21.106  1.00 28.13  ? 273 GLY D N   1 
ATOM   14875 C CA  . GLY D  1 273 ? -28.853  6.145   -22.318  1.00 29.30  ? 273 GLY D CA  1 
ATOM   14876 C C   . GLY D  1 273 ? -27.770  7.198   -22.096  1.00 29.76  ? 273 GLY D C   1 
ATOM   14877 O O   . GLY D  1 273 ? -28.057  8.408   -22.051  1.00 29.94  ? 273 GLY D O   1 
ATOM   14878 N N   . TRP D  1 274 ? -26.511  6.751   -22.088  1.00 29.14  ? 274 TRP D N   1 
ATOM   14879 C CA  . TRP D  1 274 ? -25.412  7.655   -21.807  1.00 29.00  ? 274 TRP D CA  1 
ATOM   14880 C C   . TRP D  1 274 ? -25.267  8.686   -22.934  1.00 30.79  ? 274 TRP D C   1 
ATOM   14881 O O   . TRP D  1 274 ? -24.811  9.804   -22.715  1.00 33.36  ? 274 TRP D O   1 
ATOM   14882 C CB  . TRP D  1 274 ? -24.110  6.880   -21.585  1.00 28.82  ? 274 TRP D CB  1 
ATOM   14883 C CG  . TRP D  1 274 ? -24.063  6.022   -20.344  1.00 28.05  ? 274 TRP D CG  1 
ATOM   14884 C CD1 . TRP D  1 274 ? -25.103  5.608   -19.567  1.00 26.52  ? 274 TRP D CD1 1 
ATOM   14885 C CD2 . TRP D  1 274 ? -22.870  5.411   -19.778  1.00 28.99  ? 274 TRP D CD2 1 
ATOM   14886 N NE1 . TRP D  1 274 ? -24.640  4.839   -18.536  1.00 26.71  ? 274 TRP D NE1 1 
ATOM   14887 C CE2 . TRP D  1 274 ? -23.286  4.666   -18.657  1.00 27.89  ? 274 TRP D CE2 1 
ATOM   14888 C CE3 . TRP D  1 274 ? -21.502  5.444   -20.095  1.00 29.18  ? 274 TRP D CE3 1 
ATOM   14889 C CZ2 . TRP D  1 274 ? -22.379  3.962   -17.865  1.00 29.02  ? 274 TRP D CZ2 1 
ATOM   14890 C CZ3 . TRP D  1 274 ? -20.602  4.755   -19.307  1.00 30.32  ? 274 TRP D CZ3 1 
ATOM   14891 C CH2 . TRP D  1 274 ? -21.038  4.014   -18.211  1.00 30.23  ? 274 TRP D CH2 1 
ATOM   14892 N N   . TRP D  1 275 ? -25.690  8.339   -24.149  1.00 31.48  ? 275 TRP D N   1 
ATOM   14893 C CA  . TRP D  1 275 ? -25.588  9.247   -25.277  1.00 32.50  ? 275 TRP D CA  1 
ATOM   14894 C C   . TRP D  1 275 ? -26.391  10.540  -25.084  1.00 34.92  ? 275 TRP D C   1 
ATOM   14895 O O   . TRP D  1 275 ? -26.150  11.489  -25.814  1.00 33.56  ? 275 TRP D O   1 
ATOM   14896 C CB  . TRP D  1 275 ? -26.057  8.557   -26.557  1.00 32.27  ? 275 TRP D CB  1 
ATOM   14897 C CG  . TRP D  1 275 ? -27.549  8.321   -26.657  1.00 30.58  ? 275 TRP D CG  1 
ATOM   14898 C CD1 . TRP D  1 275 ? -28.248  7.216   -26.266  1.00 29.77  ? 275 TRP D CD1 1 
ATOM   14899 C CD2 . TRP D  1 275 ? -28.510  9.198   -27.269  1.00 30.05  ? 275 TRP D CD2 1 
ATOM   14900 N NE1 . TRP D  1 275 ? -29.567  7.341   -26.579  1.00 29.64  ? 275 TRP D NE1 1 
ATOM   14901 C CE2 . TRP D  1 275 ? -29.761  8.543   -27.202  1.00 29.31  ? 275 TRP D CE2 1 
ATOM   14902 C CE3 . TRP D  1 275 ? -28.431  10.471  -27.852  1.00 30.03  ? 275 TRP D CE3 1 
ATOM   14903 C CZ2 . TRP D  1 275 ? -30.929  9.125   -27.682  1.00 28.53  ? 275 TRP D CZ2 1 
ATOM   14904 C CZ3 . TRP D  1 275 ? -29.580  11.030  -28.370  1.00 30.01  ? 275 TRP D CZ3 1 
ATOM   14905 C CH2 . TRP D  1 275 ? -30.814  10.363  -28.285  1.00 30.06  ? 275 TRP D CH2 1 
ATOM   14906 N N   . LYS D  1 276 ? -27.330  10.578  -24.123  1.00 34.54  ? 276 LYS D N   1 
ATOM   14907 C CA  . LYS D  1 276 ? -28.401  11.551  -24.163  1.00 32.83  ? 276 LYS D CA  1 
ATOM   14908 C C   . LYS D  1 276 ? -27.914  12.933  -23.751  1.00 33.05  ? 276 LYS D C   1 
ATOM   14909 O O   . LYS D  1 276 ? -28.506  13.916  -24.175  1.00 34.88  ? 276 LYS D O   1 
ATOM   14910 C CB  . LYS D  1 276 ? -29.630  11.071  -23.378  1.00 31.50  ? 276 LYS D CB  1 
ATOM   14911 C CG  . LYS D  1 276 ? -30.473  10.014  -24.092  1.00 32.06  ? 276 LYS D CG  1 
ATOM   14912 C CD  . LYS D  1 276 ? -31.485  9.282   -23.220  1.00 31.85  ? 276 LYS D CD  1 
ATOM   14913 C CE  . LYS D  1 276 ? -32.643  10.186  -22.912  1.00 32.70  ? 276 LYS D CE  1 
ATOM   14914 N NZ  . LYS D  1 276 ? -33.434  10.574  -24.102  1.00 32.96  ? 276 LYS D NZ  1 
ATOM   14915 N N   . GLY D  1 277 ? -26.845  13.042  -22.968  1.00 35.58  ? 277 GLY D N   1 
ATOM   14916 C CA  . GLY D  1 277 ? -26.265  14.362  -22.708  1.00 37.78  ? 277 GLY D CA  1 
ATOM   14917 C C   . GLY D  1 277 ? -25.033  14.678  -23.567  1.00 40.86  ? 277 GLY D C   1 
ATOM   14918 O O   . GLY D  1 277 ? -24.248  15.550  -23.230  1.00 41.46  ? 277 GLY D O   1 
ATOM   14919 N N   . GLY D  1 278 ? -24.855  13.995  -24.700  1.00 40.99  ? 278 GLY D N   1 
ATOM   14920 C CA  . GLY D  1 278 ? -23.575  14.012  -25.379  1.00 43.23  ? 278 GLY D CA  1 
ATOM   14921 C C   . GLY D  1 278 ? -22.566  13.143  -24.628  1.00 48.31  ? 278 GLY D C   1 
ATOM   14922 O O   . GLY D  1 278 ? -22.743  12.845  -23.429  1.00 55.18  ? 278 GLY D O   1 
ATOM   14923 N N   . GLU D  1 279 ? -21.524  12.729  -25.366  1.00 44.46  ? 279 GLU D N   1 
ATOM   14924 C CA  . GLU D  1 279 ? -20.471  11.861  -24.858  1.00 44.59  ? 279 GLU D CA  1 
ATOM   14925 C C   . GLU D  1 279 ? -21.046  10.478  -24.496  1.00 41.78  ? 279 GLU D C   1 
ATOM   14926 O O   . GLU D  1 279 ? -21.257  10.188  -23.318  1.00 41.36  ? 279 GLU D O   1 
ATOM   14927 C CB  . GLU D  1 279 ? -19.725  12.463  -23.657  1.00 47.23  ? 279 GLU D CB  1 
ATOM   14928 C CG  . GLU D  1 279 ? -18.951  13.774  -23.847  1.00 52.99  ? 279 GLU D CG  1 
ATOM   14929 C CD  . GLU D  1 279 ? -18.290  14.065  -25.175  1.00 55.03  ? 279 GLU D CD  1 
ATOM   14930 O OE1 . GLU D  1 279 ? -17.427  13.321  -25.694  1.00 61.71  ? 279 GLU D OE1 1 
ATOM   14931 O OE2 . GLU D  1 279 ? -18.724  15.087  -25.718  1.00 63.33  ? 279 GLU D OE2 1 
ATOM   14932 N N   . LYS D  1 280 ? -21.277  9.617   -25.502  1.00 39.21  ? 280 LYS D N   1 
ATOM   14933 C CA  . LYS D  1 280 ? -21.977  8.342   -25.318  1.00 38.64  ? 280 LYS D CA  1 
ATOM   14934 C C   . LYS D  1 280 ? -21.145  7.331   -24.516  1.00 36.77  ? 280 LYS D C   1 
ATOM   14935 O O   . LYS D  1 280 ? -21.701  6.416   -23.952  1.00 35.73  ? 280 LYS D O   1 
ATOM   14936 C CB  . LYS D  1 280 ? -22.341  7.701   -26.662  1.00 38.96  ? 280 LYS D CB  1 
ATOM   14937 C CG  . LYS D  1 280 ? -21.096  7.295   -27.425  1.00 42.61  ? 280 LYS D CG  1 
ATOM   14938 C CD  . LYS D  1 280 ? -21.190  7.223   -28.944  1.00 44.88  ? 280 LYS D CD  1 
ATOM   14939 C CE  . LYS D  1 280 ? -19.858  6.992   -29.609  1.00 45.69  ? 280 LYS D CE  1 
ATOM   14940 N NZ  . LYS D  1 280 ? -20.168  6.589   -30.981  1.00 47.56  ? 280 LYS D NZ  1 
ATOM   14941 N N   . SER D  1 281 ? -19.826  7.506   -24.460  1.00 35.94  ? 281 SER D N   1 
ATOM   14942 C CA  . SER D  1 281 ? -18.940  6.663   -23.680  1.00 37.44  ? 281 SER D CA  1 
ATOM   14943 C C   . SER D  1 281 ? -18.741  7.176   -22.253  1.00 36.63  ? 281 SER D C   1 
ATOM   14944 O O   . SER D  1 281 ? -17.974  6.577   -21.492  1.00 37.79  ? 281 SER D O   1 
ATOM   14945 C CB  . SER D  1 281 ? -17.595  6.531   -24.387  1.00 39.78  ? 281 SER D CB  1 
ATOM   14946 O OG  . SER D  1 281 ? -17.766  5.775   -25.577  1.00 40.10  ? 281 SER D OG  1 
ATOM   14947 N N   . ASP D  1 282 ? -19.417  8.273   -21.890  1.00 36.69  ? 282 ASP D N   1 
ATOM   14948 C CA  . ASP D  1 282 ? -19.288  8.840   -20.557  1.00 38.14  ? 282 ASP D CA  1 
ATOM   14949 C C   . ASP D  1 282 ? -20.659  8.939   -19.893  1.00 36.23  ? 282 ASP D C   1 
ATOM   14950 O O   . ASP D  1 282 ? -21.634  9.389   -20.501  1.00 33.67  ? 282 ASP D O   1 
ATOM   14951 C CB  . ASP D  1 282 ? -18.535  10.161  -20.589  1.00 43.87  ? 282 ASP D CB  1 
ATOM   14952 C CG  . ASP D  1 282 ? -18.201  10.741  -19.224  1.00 46.53  ? 282 ASP D CG  1 
ATOM   14953 O OD1 . ASP D  1 282 ? -17.348  10.117  -18.530  1.00 49.05  ? 282 ASP D OD1 1 
ATOM   14954 O OD2 . ASP D  1 282 ? -18.842  11.778  -18.860  1.00 48.68  ? 282 ASP D OD2 1 
ATOM   14955 N N   . HIS D  1 283 ? -20.728  8.496   -18.629  1.00 36.36  ? 283 HIS D N   1 
ATOM   14956 C CA  . HIS D  1 283 ? -21.942  8.651   -17.846  1.00 34.61  ? 283 HIS D CA  1 
ATOM   14957 C C   . HIS D  1 283 ? -21.820  9.916   -17.004  1.00 34.89  ? 283 HIS D C   1 
ATOM   14958 O O   . HIS D  1 283 ? -21.269  9.877   -15.904  1.00 36.35  ? 283 HIS D O   1 
ATOM   14959 C CB  . HIS D  1 283 ? -22.203  7.427   -16.966  1.00 34.52  ? 283 HIS D CB  1 
ATOM   14960 C CG  . HIS D  1 283 ? -23.651  7.282   -16.602  1.00 32.53  ? 283 HIS D CG  1 
ATOM   14961 N ND1 . HIS D  1 283 ? -24.119  6.444   -15.615  1.00 29.23  ? 283 HIS D ND1 1 
ATOM   14962 C CD2 . HIS D  1 283 ? -24.740  7.882   -17.143  1.00 31.58  ? 283 HIS D CD2 1 
ATOM   14963 C CE1 . HIS D  1 283 ? -25.444  6.545   -15.573  1.00 28.98  ? 283 HIS D CE1 1 
ATOM   14964 N NE2 . HIS D  1 283 ? -25.852  7.385   -16.503  1.00 29.28  ? 283 HIS D NE2 1 
ATOM   14965 N N   . SER D  1 284 ? -22.288  11.031  -17.573  1.00 34.17  ? 284 SER D N   1 
ATOM   14966 C CA  . SER D  1 284 ? -22.099  12.360  -17.011  1.00 34.64  ? 284 SER D CA  1 
ATOM   14967 C C   . SER D  1 284 ? -22.839  12.509  -15.667  1.00 32.83  ? 284 SER D C   1 
ATOM   14968 O O   . SER D  1 284 ? -24.012  12.176  -15.544  1.00 31.65  ? 284 SER D O   1 
ATOM   14969 C CB  . SER D  1 284 ? -22.523  13.393  -18.024  1.00 34.79  ? 284 SER D CB  1 
ATOM   14970 O OG  . SER D  1 284 ? -22.558  14.662  -17.400  1.00 36.16  ? 284 SER D OG  1 
ATOM   14971 N N   . LEU D  1 285 ? -22.139  13.007  -14.632  1.00 32.64  ? 285 LEU D N   1 
ATOM   14972 C CA  . LEU D  1 285 ? -22.722  13.179  -13.312  1.00 32.19  ? 285 LEU D CA  1 
ATOM   14973 C C   . LEU D  1 285 ? -23.848  14.210  -13.346  1.00 33.41  ? 285 LEU D C   1 
ATOM   14974 O O   . LEU D  1 285 ? -24.797  14.053  -12.589  1.00 36.14  ? 285 LEU D O   1 
ATOM   14975 C CB  . LEU D  1 285 ? -21.668  13.548  -12.264  1.00 33.91  ? 285 LEU D CB  1 
ATOM   14976 C CG  . LEU D  1 285 ? -20.474  12.580  -12.107  1.00 35.67  ? 285 LEU D CG  1 
ATOM   14977 C CD1 . LEU D  1 285 ? -19.574  12.962  -10.912  1.00 36.10  ? 285 LEU D CD1 1 
ATOM   14978 C CD2 . LEU D  1 285 ? -20.874  11.112  -12.007  1.00 33.89  ? 285 LEU D CD2 1 
ATOM   14979 N N   . ASN D  1 286 ? -23.813  15.183  -14.276  1.00 32.45  ? 286 ASN D N   1 
ATOM   14980 C CA  . ASN D  1 286 ? -24.722  16.324  -14.217  1.00 34.49  ? 286 ASN D CA  1 
ATOM   14981 C C   . ASN D  1 286 ? -25.679  16.412  -15.410  1.00 33.96  ? 286 ASN D C   1 
ATOM   14982 O O   . ASN D  1 286 ? -26.282  17.475  -15.602  1.00 31.65  ? 286 ASN D O   1 
ATOM   14983 C CB  . ASN D  1 286 ? -23.997  17.659  -14.034  1.00 33.27  ? 286 ASN D CB  1 
ATOM   14984 C CG  . ASN D  1 286 ? -23.164  18.087  -15.216  1.00 35.73  ? 286 ASN D CG  1 
ATOM   14985 O OD1 . ASN D  1 286 ? -22.893  17.350  -16.165  1.00 38.38  ? 286 ASN D OD1 1 
ATOM   14986 N ND2 . ASN D  1 286 ? -22.674  19.302  -15.149  1.00 41.26  ? 286 ASN D ND2 1 
ATOM   14987 N N   . GLN D  1 287 ? -25.869  15.299  -16.135  1.00 32.28  ? 287 GLN D N   1 
ATOM   14988 C CA  . GLN D  1 287 ? -26.844  15.240  -17.216  1.00 32.55  ? 287 GLN D CA  1 
ATOM   14989 C C   . GLN D  1 287 ? -28.053  14.406  -16.817  1.00 31.44  ? 287 GLN D C   1 
ATOM   14990 O O   . GLN D  1 287 ? -28.023  13.184  -16.876  1.00 30.19  ? 287 GLN D O   1 
ATOM   14991 C CB  . GLN D  1 287 ? -26.293  14.628  -18.501  1.00 34.49  ? 287 GLN D CB  1 
ATOM   14992 C CG  . GLN D  1 287 ? -25.206  15.480  -19.155  1.00 37.76  ? 287 GLN D CG  1 
ATOM   14993 C CD  . GLN D  1 287 ? -25.750  16.756  -19.768  1.00 36.84  ? 287 GLN D CD  1 
ATOM   14994 O OE1 . GLN D  1 287 ? -26.873  16.822  -20.288  1.00 36.79  ? 287 GLN D OE1 1 
ATOM   14995 N NE2 . GLN D  1 287 ? -24.949  17.798  -19.687  1.00 37.10  ? 287 GLN D NE2 1 
ATOM   14996 N N   . PRO D  1 288 ? -29.161  15.055  -16.421  1.00 31.01  ? 288 PRO D N   1 
ATOM   14997 C CA  . PRO D  1 288 ? -30.396  14.325  -16.066  1.00 31.54  ? 288 PRO D CA  1 
ATOM   14998 C C   . PRO D  1 288 ? -30.912  13.300  -17.085  1.00 32.06  ? 288 PRO D C   1 
ATOM   14999 O O   . PRO D  1 288 ? -31.388  12.220  -16.720  1.00 32.72  ? 288 PRO D O   1 
ATOM   15000 C CB  . PRO D  1 288 ? -31.407  15.476  -15.840  1.00 28.88  ? 288 PRO D CB  1 
ATOM   15001 C CG  . PRO D  1 288 ? -30.529  16.608  -15.337  1.00 29.73  ? 288 PRO D CG  1 
ATOM   15002 C CD  . PRO D  1 288 ? -29.223  16.506  -16.153  1.00 29.34  ? 288 PRO D CD  1 
ATOM   15003 N N   . GLU D  1 289 ? -30.745  13.620  -18.372  1.00 31.15  ? 289 GLU D N   1 
ATOM   15004 C CA  . GLU D  1 289 ? -31.265  12.797  -19.452  1.00 29.97  ? 289 GLU D CA  1 
ATOM   15005 C C   . GLU D  1 289 ? -30.587  11.414  -19.510  1.00 29.11  ? 289 GLU D C   1 
ATOM   15006 O O   . GLU D  1 289 ? -31.069  10.529  -20.209  1.00 30.88  ? 289 GLU D O   1 
ATOM   15007 C CB  . GLU D  1 289 ? -31.078  13.571  -20.765  1.00 28.98  ? 289 GLU D CB  1 
ATOM   15008 C CG  . GLU D  1 289 ? -32.030  14.742  -20.989  1.00 27.48  ? 289 GLU D CG  1 
ATOM   15009 C CD  . GLU D  1 289 ? -33.467  14.281  -21.059  1.00 29.68  ? 289 GLU D CD  1 
ATOM   15010 O OE1 . GLU D  1 289 ? -33.738  13.263  -21.748  1.00 30.01  ? 289 GLU D OE1 1 
ATOM   15011 O OE2 . GLU D  1 289 ? -34.313  14.913  -20.396  1.00 30.32  ? 289 GLU D OE2 1 
ATOM   15012 N N   . GLU D  1 290 ? -29.441  11.245  -18.847  1.00 27.63  ? 290 GLU D N   1 
ATOM   15013 C CA  . GLU D  1 290 ? -28.654  10.020  -18.904  1.00 27.64  ? 290 GLU D CA  1 
ATOM   15014 C C   . GLU D  1 290 ? -29.020  9.039   -17.776  1.00 27.26  ? 290 GLU D C   1 
ATOM   15015 O O   . GLU D  1 290 ? -28.378  7.993   -17.629  1.00 25.02  ? 290 GLU D O   1 
ATOM   15016 C CB  . GLU D  1 290 ? -27.174  10.408  -18.796  1.00 27.61  ? 290 GLU D CB  1 
ATOM   15017 C CG  . GLU D  1 290 ? -26.521  10.764  -20.124  1.00 28.04  ? 290 GLU D CG  1 
ATOM   15018 C CD  . GLU D  1 290 ? -25.073  11.225  -20.063  1.00 28.04  ? 290 GLU D CD  1 
ATOM   15019 O OE1 . GLU D  1 290 ? -24.174  10.595  -19.479  1.00 25.65  ? 290 GLU D OE1 1 
ATOM   15020 O OE2 . GLU D  1 290 ? -24.860  12.268  -20.710  1.00 31.79  ? 290 GLU D OE2 1 
ATOM   15021 N N   . TRP D  1 291 ? -30.006  9.410   -16.943  1.00 27.36  ? 291 TRP D N   1 
ATOM   15022 C CA  . TRP D  1 291 ? -30.274  8.679   -15.717  1.00 27.49  ? 291 TRP D CA  1 
ATOM   15023 C C   . TRP D  1 291 ? -31.764  8.498   -15.501  1.00 25.72  ? 291 TRP D C   1 
ATOM   15024 O O   . TRP D  1 291 ? -32.210  8.584   -14.368  1.00 26.33  ? 291 TRP D O   1 
ATOM   15025 C CB  . TRP D  1 291 ? -29.661  9.389   -14.495  1.00 29.27  ? 291 TRP D CB  1 
ATOM   15026 C CG  . TRP D  1 291 ? -28.152  9.536   -14.506  1.00 28.65  ? 291 TRP D CG  1 
ATOM   15027 C CD1 . TRP D  1 291 ? -27.455  10.452  -15.217  1.00 27.75  ? 291 TRP D CD1 1 
ATOM   15028 C CD2 . TRP D  1 291 ? -27.165  8.801   -13.754  1.00 27.16  ? 291 TRP D CD2 1 
ATOM   15029 N NE1 . TRP D  1 291 ? -26.121  10.327  -14.980  1.00 27.96  ? 291 TRP D NE1 1 
ATOM   15030 C CE2 . TRP D  1 291 ? -25.909  9.341   -14.074  1.00 27.08  ? 291 TRP D CE2 1 
ATOM   15031 C CE3 . TRP D  1 291 ? -27.208  7.726   -12.863  1.00 27.18  ? 291 TRP D CE3 1 
ATOM   15032 C CZ2 . TRP D  1 291 ? -24.712  8.844   -13.562  1.00 27.44  ? 291 TRP D CZ2 1 
ATOM   15033 C CZ3 . TRP D  1 291 ? -26.021  7.231   -12.347  1.00 26.11  ? 291 TRP D CZ3 1 
ATOM   15034 C CH2 . TRP D  1 291 ? -24.796  7.788   -12.687  1.00 26.44  ? 291 TRP D CH2 1 
ATOM   15035 N N   . PHE D  1 292 ? -32.528  8.228   -16.569  1.00 28.10  ? 292 PHE D N   1 
ATOM   15036 C CA  . PHE D  1 292 ? -33.979  8.058   -16.469  1.00 25.68  ? 292 PHE D CA  1 
ATOM   15037 C C   . PHE D  1 292 ? -34.348  6.581   -16.391  1.00 26.84  ? 292 PHE D C   1 
ATOM   15038 O O   . PHE D  1 292 ? -35.491  6.232   -16.081  1.00 27.51  ? 292 PHE D O   1 
ATOM   15039 C CB  . PHE D  1 292 ? -34.711  8.687   -17.652  1.00 26.73  ? 292 PHE D CB  1 
ATOM   15040 C CG  . PHE D  1 292 ? -35.160  10.134  -17.447  1.00 26.85  ? 292 PHE D CG  1 
ATOM   15041 C CD1 . PHE D  1 292 ? -36.334  10.419  -16.790  1.00 26.50  ? 292 PHE D CD1 1 
ATOM   15042 C CD2 . PHE D  1 292 ? -34.370  11.210  -17.850  1.00 27.83  ? 292 PHE D CD2 1 
ATOM   15043 C CE1 . PHE D  1 292 ? -36.737  11.729  -16.586  1.00 25.58  ? 292 PHE D CE1 1 
ATOM   15044 C CE2 . PHE D  1 292 ? -34.765  12.526  -17.635  1.00 27.30  ? 292 PHE D CE2 1 
ATOM   15045 C CZ  . PHE D  1 292 ? -35.955  12.782  -17.006  1.00 26.82  ? 292 PHE D CZ  1 
ATOM   15046 N N   . GLY D  1 293 ? -33.372  5.697   -16.621  1.00 26.27  ? 293 GLY D N   1 
ATOM   15047 C CA  . GLY D  1 293 ? -33.665  4.282   -16.722  1.00 26.26  ? 293 GLY D CA  1 
ATOM   15048 C C   . GLY D  1 293 ? -34.238  3.661   -15.449  1.00 24.94  ? 293 GLY D C   1 
ATOM   15049 O O   . GLY D  1 293 ? -33.917  4.037   -14.329  1.00 23.58  ? 293 GLY D O   1 
ATOM   15050 N N   . PHE D  1 294 ? -35.078  2.650   -15.648  1.00 24.38  ? 294 PHE D N   1 
ATOM   15051 C CA  . PHE D  1 294 ? -35.417  1.745   -14.561  1.00 24.61  ? 294 PHE D CA  1 
ATOM   15052 C C   . PHE D  1 294 ? -34.257  0.778   -14.345  1.00 25.25  ? 294 PHE D C   1 
ATOM   15053 O O   . PHE D  1 294 ? -34.161  0.204   -13.281  1.00 24.97  ? 294 PHE D O   1 
ATOM   15054 C CB  . PHE D  1 294 ? -36.718  0.982   -14.832  1.00 24.20  ? 294 PHE D CB  1 
ATOM   15055 C CG  . PHE D  1 294 ? -37.989  1.809   -14.855  1.00 23.20  ? 294 PHE D CG  1 
ATOM   15056 C CD1 . PHE D  1 294 ? -37.946  3.197   -14.779  1.00 24.07  ? 294 PHE D CD1 1 
ATOM   15057 C CD2 . PHE D  1 294 ? -39.223  1.185   -15.030  1.00 23.79  ? 294 PHE D CD2 1 
ATOM   15058 C CE1 . PHE D  1 294 ? -39.120  3.954   -14.816  1.00 23.87  ? 294 PHE D CE1 1 
ATOM   15059 C CE2 . PHE D  1 294 ? -40.393  1.940   -15.113  1.00 24.30  ? 294 PHE D CE2 1 
ATOM   15060 C CZ  . PHE D  1 294 ? -40.335  3.326   -14.994  1.00 24.88  ? 294 PHE D CZ  1 
ATOM   15061 N N   . TRP D  1 295 ? -33.363  0.659   -15.342  1.00 26.42  ? 295 TRP D N   1 
ATOM   15062 C CA  . TRP D  1 295 ? -32.152  -0.146  -15.272  1.00 27.07  ? 295 TRP D CA  1 
ATOM   15063 C C   . TRP D  1 295 ? -30.931  0.748   -15.446  1.00 28.56  ? 295 TRP D C   1 
ATOM   15064 O O   . TRP D  1 295 ? -30.965  1.708   -16.229  1.00 30.82  ? 295 TRP D O   1 
ATOM   15065 C CB  . TRP D  1 295 ? -32.170  -1.221  -16.377  1.00 27.51  ? 295 TRP D CB  1 
ATOM   15066 C CG  . TRP D  1 295 ? -33.133  -2.378  -16.157  1.00 27.62  ? 295 TRP D CG  1 
ATOM   15067 C CD1 . TRP D  1 295 ? -34.505  -2.334  -16.009  1.00 27.21  ? 295 TRP D CD1 1 
ATOM   15068 C CD2 . TRP D  1 295 ? -32.769  -3.774  -16.075  1.00 27.02  ? 295 TRP D CD2 1 
ATOM   15069 N NE1 . TRP D  1 295 ? -35.006  -3.592  -15.823  1.00 27.30  ? 295 TRP D NE1 1 
ATOM   15070 C CE2 . TRP D  1 295 ? -33.965  -4.492  -15.841  1.00 27.66  ? 295 TRP D CE2 1 
ATOM   15071 C CE3 . TRP D  1 295 ? -31.560  -4.471  -16.151  1.00 27.48  ? 295 TRP D CE3 1 
ATOM   15072 C CZ2 . TRP D  1 295 ? -33.974  -5.873  -15.700  1.00 27.11  ? 295 TRP D CZ2 1 
ATOM   15073 C CZ3 . TRP D  1 295 ? -31.569  -5.832  -15.981  1.00 27.98  ? 295 TRP D CZ3 1 
ATOM   15074 C CH2 . TRP D  1 295 ? -32.762  -6.525  -15.769  1.00 27.84  ? 295 TRP D CH2 1 
ATOM   15075 N N   . GLY D  1 296 ? -29.859  0.417   -14.714  1.00 28.14  ? 296 GLY D N   1 
ATOM   15076 C CA  . GLY D  1 296 ? -28.633  1.191   -14.735  1.00 28.36  ? 296 GLY D CA  1 
ATOM   15077 C C   . GLY D  1 296 ? -27.426  0.291   -15.001  1.00 29.16  ? 296 GLY D C   1 
ATOM   15078 O O   . GLY D  1 296 ? -27.379  -0.848  -14.522  1.00 28.21  ? 296 GLY D O   1 
ATOM   15079 N N   . TYR D  1 297 ? -26.449  0.846   -15.744  1.00 29.58  ? 297 TYR D N   1 
ATOM   15080 C CA  . TYR D  1 297 ? -25.270  0.126   -16.207  1.00 29.60  ? 297 TYR D CA  1 
ATOM   15081 C C   . TYR D  1 297 ? -24.141  0.461   -15.261  1.00 30.27  ? 297 TYR D C   1 
ATOM   15082 O O   . TYR D  1 297 ? -24.051  1.594   -14.845  1.00 32.30  ? 297 TYR D O   1 
ATOM   15083 C CB  . TYR D  1 297 ? -24.907  0.450   -17.659  1.00 29.95  ? 297 TYR D CB  1 
ATOM   15084 C CG  . TYR D  1 297 ? -26.000  0.024   -18.637  1.00 30.62  ? 297 TYR D CG  1 
ATOM   15085 C CD1 . TYR D  1 297 ? -26.228  -1.319  -18.979  1.00 30.81  ? 297 TYR D CD1 1 
ATOM   15086 C CD2 . TYR D  1 297 ? -26.872  0.983   -19.158  1.00 28.99  ? 297 TYR D CD2 1 
ATOM   15087 C CE1 . TYR D  1 297 ? -27.298  -1.661  -19.805  1.00 30.96  ? 297 TYR D CE1 1 
ATOM   15088 C CE2 . TYR D  1 297 ? -27.907  0.648   -20.001  1.00 28.10  ? 297 TYR D CE2 1 
ATOM   15089 C CZ  . TYR D  1 297 ? -28.131  -0.671  -20.322  1.00 29.42  ? 297 TYR D CZ  1 
ATOM   15090 O OH  . TYR D  1 297 ? -29.176  -0.853  -21.178  1.00 29.51  ? 297 TYR D OH  1 
ATOM   15091 N N   . SER D  1 298 ? -23.317  -0.531  -14.906  1.00 31.67  ? 298 SER D N   1 
ATOM   15092 C CA  . SER D  1 298 ? -22.332  -0.333  -13.859  1.00 33.64  ? 298 SER D CA  1 
ATOM   15093 C C   . SER D  1 298 ? -21.136  0.481   -14.368  1.00 32.71  ? 298 SER D C   1 
ATOM   15094 O O   . SER D  1 298 ? -20.497  1.147   -13.573  1.00 30.85  ? 298 SER D O   1 
ATOM   15095 C CB  . SER D  1 298 ? -21.877  -1.655  -13.223  1.00 33.19  ? 298 SER D CB  1 
ATOM   15096 O OG  . SER D  1 298 ? -21.148  -2.350  -14.193  1.00 34.44  ? 298 SER D OG  1 
ATOM   15097 N N   . ASP D  1 299 ? -20.801  0.323   -15.653  1.00 34.42  ? 299 ASP D N   1 
ATOM   15098 C CA  . ASP D  1 299 ? -19.648  0.949   -16.293  1.00 35.77  ? 299 ASP D CA  1 
ATOM   15099 C C   . ASP D  1 299 ? -19.786  0.774   -17.809  1.00 35.47  ? 299 ASP D C   1 
ATOM   15100 O O   . ASP D  1 299 ? -20.758  0.206   -18.295  1.00 36.39  ? 299 ASP D O   1 
ATOM   15101 C CB  . ASP D  1 299 ? -18.314  0.445   -15.763  1.00 37.30  ? 299 ASP D CB  1 
ATOM   15102 C CG  . ASP D  1 299 ? -18.003  -1.017  -16.034  1.00 40.23  ? 299 ASP D CG  1 
ATOM   15103 O OD1 . ASP D  1 299 ? -18.428  -1.550  -17.077  1.00 40.43  ? 299 ASP D OD1 1 
ATOM   15104 O OD2 . ASP D  1 299 ? -17.312  -1.615  -15.204  1.00 45.65  ? 299 ASP D OD2 1 
ATOM   15105 N N   . LEU D  1 300 ? -18.830  1.315   -18.553  1.00 35.88  ? 300 LEU D N   1 
ATOM   15106 C CA  . LEU D  1 300 ? -18.878  1.351   -20.006  1.00 37.66  ? 300 LEU D CA  1 
ATOM   15107 C C   . LEU D  1 300 ? -18.987  -0.042  -20.642  1.00 39.32  ? 300 LEU D C   1 
ATOM   15108 O O   . LEU D  1 300 ? -19.450  -0.169  -21.764  1.00 39.79  ? 300 LEU D O   1 
ATOM   15109 C CB  . LEU D  1 300 ? -17.612  2.069   -20.486  1.00 36.75  ? 300 LEU D CB  1 
ATOM   15110 C CG  . LEU D  1 300 ? -17.491  2.290   -21.993  1.00 36.86  ? 300 LEU D CG  1 
ATOM   15111 C CD1 . LEU D  1 300 ? -18.649  3.127   -22.535  1.00 36.23  ? 300 LEU D CD1 1 
ATOM   15112 C CD2 . LEU D  1 300 ? -16.164  2.931   -22.315  1.00 37.35  ? 300 LEU D CD2 1 
ATOM   15113 N N   . ASN D  1 301 ? -18.522  -1.095  -19.969  1.00 42.21  ? 301 ASN D N   1 
ATOM   15114 C CA  . ASN D  1 301 ? -18.494  -2.424  -20.572  1.00 43.60  ? 301 ASN D CA  1 
ATOM   15115 C C   . ASN D  1 301 ? -19.748  -3.234  -20.249  1.00 40.90  ? 301 ASN D C   1 
ATOM   15116 O O   . ASN D  1 301 ? -19.841  -4.393  -20.639  1.00 43.01  ? 301 ASN D O   1 
ATOM   15117 C CB  . ASN D  1 301 ? -17.326  -3.258  -20.059  1.00 44.73  ? 301 ASN D CB  1 
ATOM   15118 C CG  . ASN D  1 301 ? -16.023  -2.514  -20.157  1.00 47.05  ? 301 ASN D CG  1 
ATOM   15119 O OD1 . ASN D  1 301 ? -15.343  -2.381  -19.130  1.00 45.78  ? 301 ASN D OD1 1 
ATOM   15120 N ND2 . ASN D  1 301 ? -15.683  -2.040  -21.356  1.00 45.58  ? 301 ASN D ND2 1 
ATOM   15121 N N   . ASP D  1 302 ? -20.680  -2.653  -19.496  1.00 38.56  ? 302 ASP D N   1 
ATOM   15122 C CA  . ASP D  1 302 ? -21.848  -3.392  -19.065  1.00 37.48  ? 302 ASP D CA  1 
ATOM   15123 C C   . ASP D  1 302 ? -22.890  -3.269  -20.170  1.00 38.62  ? 302 ASP D C   1 
ATOM   15124 O O   . ASP D  1 302 ? -23.318  -2.164  -20.498  1.00 38.66  ? 302 ASP D O   1 
ATOM   15125 C CB  . ASP D  1 302 ? -22.293  -2.935  -17.689  1.00 36.61  ? 302 ASP D CB  1 
ATOM   15126 C CG  . ASP D  1 302 ? -23.489  -3.667  -17.119  1.00 36.37  ? 302 ASP D CG  1 
ATOM   15127 O OD1 . ASP D  1 302 ? -23.903  -4.674  -17.745  1.00 38.66  ? 302 ASP D OD1 1 
ATOM   15128 O OD2 . ASP D  1 302 ? -23.997  -3.215  -16.079  1.00 33.85  ? 302 ASP D OD2 1 
ATOM   15129 N N   . LYS D  1 303 ? -23.265  -4.417  -20.744  1.00 39.49  ? 303 LYS D N   1 
ATOM   15130 C CA  . LYS D  1 303 ? -24.259  -4.509  -21.803  1.00 41.05  ? 303 LYS D CA  1 
ATOM   15131 C C   . LYS D  1 303 ? -25.623  -4.863  -21.203  1.00 37.50  ? 303 LYS D C   1 
ATOM   15132 O O   . LYS D  1 303 ? -26.621  -4.806  -21.908  1.00 35.87  ? 303 LYS D O   1 
ATOM   15133 C CB  . LYS D  1 303 ? -23.850  -5.565  -22.844  1.00 47.39  ? 303 LYS D CB  1 
ATOM   15134 C CG  . LYS D  1 303 ? -22.591  -5.269  -23.672  1.00 51.14  ? 303 LYS D CG  1 
ATOM   15135 C CD  . LYS D  1 303 ? -22.820  -4.194  -24.728  1.00 56.75  ? 303 LYS D CD  1 
ATOM   15136 C CE  . LYS D  1 303 ? -21.669  -4.004  -25.696  1.00 60.53  ? 303 LYS D CE  1 
ATOM   15137 N NZ  . LYS D  1 303 ? -20.562  -3.275  -25.078  1.00 60.09  ? 303 LYS D NZ  1 
ATOM   15138 N N   . TYR D  1 304 ? -25.677  -5.171  -19.895  1.00 36.30  ? 304 TYR D N   1 
ATOM   15139 C CA  . TYR D  1 304 ? -26.864  -5.784  -19.295  1.00 35.15  ? 304 TYR D CA  1 
ATOM   15140 C C   . TYR D  1 304 ? -27.526  -4.850  -18.285  1.00 33.75  ? 304 TYR D C   1 
ATOM   15141 O O   . TYR D  1 304 ? -28.735  -4.589  -18.396  1.00 32.03  ? 304 TYR D O   1 
ATOM   15142 C CB  . TYR D  1 304 ? -26.520  -7.153  -18.696  1.00 33.82  ? 304 TYR D CB  1 
ATOM   15143 C CG  . TYR D  1 304 ? -25.944  -8.028  -19.802  1.00 35.26  ? 304 TYR D CG  1 
ATOM   15144 C CD1 . TYR D  1 304 ? -26.735  -8.410  -20.885  1.00 34.99  ? 304 TYR D CD1 1 
ATOM   15145 C CD2 . TYR D  1 304 ? -24.597  -8.393  -19.819  1.00 38.28  ? 304 TYR D CD2 1 
ATOM   15146 C CE1 . TYR D  1 304 ? -26.235  -9.163  -21.933  1.00 36.67  ? 304 TYR D CE1 1 
ATOM   15147 C CE2 . TYR D  1 304 ? -24.069  -9.152  -20.861  1.00 41.08  ? 304 TYR D CE2 1 
ATOM   15148 C CZ  . TYR D  1 304 ? -24.897  -9.549  -21.909  1.00 41.42  ? 304 TYR D CZ  1 
ATOM   15149 O OH  . TYR D  1 304 ? -24.403  -10.296 -22.928  1.00 41.34  ? 304 TYR D OH  1 
ATOM   15150 N N   . GLY D  1 305 ? -26.734  -4.387  -17.301  1.00 33.36  ? 305 GLY D N   1 
ATOM   15151 C CA  . GLY D  1 305 ? -27.217  -3.523  -16.237  1.00 32.37  ? 305 GLY D CA  1 
ATOM   15152 C C   . GLY D  1 305 ? -28.124  -4.280  -15.273  1.00 32.56  ? 305 GLY D C   1 
ATOM   15153 O O   . GLY D  1 305 ? -28.371  -5.471  -15.458  1.00 33.43  ? 305 GLY D O   1 
ATOM   15154 N N   . THR D  1 306 ? -28.594  -3.592  -14.224  1.00 32.10  ? 306 THR D N   1 
ATOM   15155 C CA  . THR D  1 306 ? -29.447  -4.214  -13.226  1.00 31.70  ? 306 THR D CA  1 
ATOM   15156 C C   . THR D  1 306 ? -30.596  -3.256  -12.936  1.00 31.37  ? 306 THR D C   1 
ATOM   15157 O O   . THR D  1 306 ? -30.452  -2.055  -13.129  1.00 31.25  ? 306 THR D O   1 
ATOM   15158 C CB  . THR D  1 306 ? -28.701  -4.587  -11.942  1.00 31.52  ? 306 THR D CB  1 
ATOM   15159 O OG1 . THR D  1 306 ? -28.287  -3.303  -11.488  1.00 31.45  ? 306 THR D OG1 1 
ATOM   15160 C CG2 . THR D  1 306 ? -27.597  -5.625  -12.124  1.00 30.99  ? 306 THR D CG2 1 
ATOM   15161 N N   . PRO D  1 307 ? -31.770  -3.787  -12.491  1.00 30.93  ? 307 PRO D N   1 
ATOM   15162 C CA  . PRO D  1 307 ? -32.900  -2.945  -12.140  1.00 29.42  ? 307 PRO D CA  1 
ATOM   15163 C C   . PRO D  1 307 ? -32.790  -2.132  -10.861  1.00 28.64  ? 307 PRO D C   1 
ATOM   15164 O O   . PRO D  1 307 ? -32.306  -2.616  -9.835   1.00 30.14  ? 307 PRO D O   1 
ATOM   15165 C CB  . PRO D  1 307 ? -34.042  -3.971  -12.081  1.00 29.33  ? 307 PRO D CB  1 
ATOM   15166 C CG  . PRO D  1 307 ? -33.408  -5.210  -11.553  1.00 29.67  ? 307 PRO D CG  1 
ATOM   15167 C CD  . PRO D  1 307 ? -32.137  -5.220  -12.347  1.00 30.21  ? 307 PRO D CD  1 
ATOM   15168 N N   . ARG D  1 308 ? -33.248  -0.891  -10.935  1.00 27.19  ? 308 ARG D N   1 
ATOM   15169 C CA  . ARG D  1 308 ? -33.268  -0.007  -9.748   1.00 26.32  ? 308 ARG D CA  1 
ATOM   15170 C C   . ARG D  1 308 ? -34.609  -0.228  -9.035   1.00 25.65  ? 308 ARG D C   1 
ATOM   15171 O O   . ARG D  1 308 ? -35.502  -0.818  -9.637   1.00 25.45  ? 308 ARG D O   1 
ATOM   15172 C CB  . ARG D  1 308 ? -32.966  1.423   -10.215  1.00 26.83  ? 308 ARG D CB  1 
ATOM   15173 C CG  . ARG D  1 308 ? -31.753  1.631   -11.105  1.00 25.94  ? 308 ARG D CG  1 
ATOM   15174 C CD  . ARG D  1 308 ? -31.920  2.919   -11.879  1.00 26.31  ? 308 ARG D CD  1 
ATOM   15175 N NE  . ARG D  1 308 ? -30.675  3.683   -11.990  1.00 25.11  ? 308 ARG D NE  1 
ATOM   15176 C CZ  . ARG D  1 308 ? -30.302  4.338   -13.073  1.00 25.86  ? 308 ARG D CZ  1 
ATOM   15177 N NH1 . ARG D  1 308 ? -31.196  4.689   -13.974  1.00 25.70  ? 308 ARG D NH1 1 
ATOM   15178 N NH2 . ARG D  1 308 ? -29.034  4.643   -13.250  1.00 27.34  ? 308 ARG D NH2 1 
ATOM   15179 N N   . PRO D  1 309 ? -34.757  0.165   -7.760   1.00 26.24  ? 309 PRO D N   1 
ATOM   15180 C CA  . PRO D  1 309 ? -35.977  -0.124  -7.020   1.00 26.02  ? 309 PRO D CA  1 
ATOM   15181 C C   . PRO D  1 309 ? -37.314  0.195   -7.691   1.00 27.38  ? 309 PRO D C   1 
ATOM   15182 O O   . PRO D  1 309 ? -38.293  -0.507  -7.424   1.00 31.00  ? 309 PRO D O   1 
ATOM   15183 C CB  . PRO D  1 309 ? -35.723  0.707   -5.768   1.00 26.18  ? 309 PRO D CB  1 
ATOM   15184 C CG  . PRO D  1 309 ? -34.238  0.648   -5.579   1.00 27.39  ? 309 PRO D CG  1 
ATOM   15185 C CD  . PRO D  1 309 ? -33.746  0.856   -6.985   1.00 27.40  ? 309 PRO D CD  1 
ATOM   15186 N N   . VAL D  1 310 ? -37.345  1.211   -8.546   1.00 25.77  ? 310 VAL D N   1 
ATOM   15187 C CA  . VAL D  1 310 ? -38.564  1.582   -9.242   1.00 26.32  ? 310 VAL D CA  1 
ATOM   15188 C C   . VAL D  1 310 ? -39.070  0.408   -10.089  1.00 26.88  ? 310 VAL D C   1 
ATOM   15189 O O   . VAL D  1 310 ? -40.261  0.300   -10.322  1.00 26.79  ? 310 VAL D O   1 
ATOM   15190 C CB  . VAL D  1 310 ? -38.330  2.822   -10.116  1.00 24.35  ? 310 VAL D CB  1 
ATOM   15191 C CG1 . VAL D  1 310 ? -37.176  2.639   -11.089  1.00 24.20  ? 310 VAL D CG1 1 
ATOM   15192 C CG2 . VAL D  1 310 ? -39.585  3.207   -10.870  1.00 23.65  ? 310 VAL D CG2 1 
ATOM   15193 N N   . TRP D  1 311 ? -38.155  -0.440  -10.585  1.00 27.18  ? 311 TRP D N   1 
ATOM   15194 C CA  . TRP D  1 311 ? -38.527  -1.584  -11.401  1.00 26.94  ? 311 TRP D CA  1 
ATOM   15195 C C   . TRP D  1 311 ? -39.499  -2.491  -10.669  1.00 26.55  ? 311 TRP D C   1 
ATOM   15196 O O   . TRP D  1 311 ? -40.505  -2.878  -11.250  1.00 28.40  ? 311 TRP D O   1 
ATOM   15197 C CB  . TRP D  1 311 ? -37.290  -2.367  -11.821  1.00 26.60  ? 311 TRP D CB  1 
ATOM   15198 C CG  . TRP D  1 311 ? -37.560  -3.570  -12.678  1.00 26.46  ? 311 TRP D CG  1 
ATOM   15199 C CD1 . TRP D  1 311 ? -37.476  -4.885  -12.295  1.00 25.50  ? 311 TRP D CD1 1 
ATOM   15200 C CD2 . TRP D  1 311 ? -37.836  -3.567  -14.094  1.00 25.19  ? 311 TRP D CD2 1 
ATOM   15201 N NE1 . TRP D  1 311 ? -37.727  -5.692  -13.361  1.00 24.85  ? 311 TRP D NE1 1 
ATOM   15202 C CE2 . TRP D  1 311 ? -37.931  -4.927  -14.480  1.00 25.28  ? 311 TRP D CE2 1 
ATOM   15203 C CE3 . TRP D  1 311 ? -37.979  -2.565  -15.061  1.00 24.47  ? 311 TRP D CE3 1 
ATOM   15204 C CZ2 . TRP D  1 311 ? -38.188  -5.306  -15.790  1.00 24.69  ? 311 TRP D CZ2 1 
ATOM   15205 C CZ3 . TRP D  1 311 ? -38.238  -2.939  -16.362  1.00 24.64  ? 311 TRP D CZ3 1 
ATOM   15206 C CH2 . TRP D  1 311 ? -38.294  -4.298  -16.721  1.00 25.36  ? 311 TRP D CH2 1 
ATOM   15207 N N   . PHE D  1 312 ? -39.202  -2.759  -9.399   1.00 27.44  ? 312 PHE D N   1 
ATOM   15208 C CA  . PHE D  1 312 ? -39.963  -3.697  -8.576   1.00 27.74  ? 312 PHE D CA  1 
ATOM   15209 C C   . PHE D  1 312 ? -41.222  -3.028  -8.021   1.00 27.87  ? 312 PHE D C   1 
ATOM   15210 O O   . PHE D  1 312 ? -42.269  -3.663  -7.937   1.00 26.10  ? 312 PHE D O   1 
ATOM   15211 C CB  . PHE D  1 312 ? -39.029  -4.221  -7.490   1.00 28.44  ? 312 PHE D CB  1 
ATOM   15212 C CG  . PHE D  1 312 ? -37.837  -5.008  -8.034   1.00 29.96  ? 312 PHE D CG  1 
ATOM   15213 C CD1 . PHE D  1 312 ? -37.975  -6.329  -8.456   1.00 30.41  ? 312 PHE D CD1 1 
ATOM   15214 C CD2 . PHE D  1 312 ? -36.578  -4.424  -8.123   1.00 30.88  ? 312 PHE D CD2 1 
ATOM   15215 C CE1 . PHE D  1 312 ? -36.883  -7.040  -8.957   1.00 31.52  ? 312 PHE D CE1 1 
ATOM   15216 C CE2 . PHE D  1 312 ? -35.477  -5.142  -8.593   1.00 32.25  ? 312 PHE D CE2 1 
ATOM   15217 C CZ  . PHE D  1 312 ? -35.634  -6.451  -9.031   1.00 31.12  ? 312 PHE D CZ  1 
ATOM   15218 N N   . ALA D  1 313 ? -41.152  -1.725  -7.680   1.00 27.10  ? 313 ALA D N   1 
ATOM   15219 C CA  . ALA D  1 313 ? -42.349  -1.048  -7.221   1.00 26.48  ? 313 ALA D CA  1 
ATOM   15220 C C   . ALA D  1 313 ? -43.356  -0.983  -8.372   1.00 27.24  ? 313 ALA D C   1 
ATOM   15221 O O   . ALA D  1 313 ? -44.543  -1.137  -8.125   1.00 30.35  ? 313 ALA D O   1 
ATOM   15222 C CB  . ALA D  1 313 ? -42.045  0.313   -6.644   1.00 26.25  ? 313 ALA D CB  1 
ATOM   15223 N N   . MET D  1 314 ? -42.883  -0.788  -9.612   1.00 27.11  ? 314 MET D N   1 
ATOM   15224 C CA  . MET D  1 314 ? -43.758  -0.717  -10.770  1.00 28.09  ? 314 MET D CA  1 
ATOM   15225 C C   . MET D  1 314 ? -44.320  -2.095  -11.107  1.00 28.06  ? 314 MET D C   1 
ATOM   15226 O O   . MET D  1 314 ? -45.482  -2.201  -11.418  1.00 27.42  ? 314 MET D O   1 
ATOM   15227 C CB  . MET D  1 314 ? -43.040  -0.170  -12.005  1.00 28.74  ? 314 MET D CB  1 
ATOM   15228 C CG  . MET D  1 314 ? -42.805  1.317   -11.948  1.00 28.74  ? 314 MET D CG  1 
ATOM   15229 S SD  . MET D  1 314 ? -44.324  2.182   -12.377  1.00 31.77  ? 314 MET D SD  1 
ATOM   15230 C CE  . MET D  1 314 ? -44.375  1.905   -14.146  1.00 32.54  ? 314 MET D CE  1 
ATOM   15231 N N   . ARG D  1 315 ? -43.499  -3.146  -11.073  1.00 29.80  ? 315 ARG D N   1 
ATOM   15232 C CA  . ARG D  1 315 ? -44.009  -4.470  -11.351  1.00 30.95  ? 315 ARG D CA  1 
ATOM   15233 C C   . ARG D  1 315 ? -45.155  -4.797  -10.399  1.00 31.65  ? 315 ARG D C   1 
ATOM   15234 O O   . ARG D  1 315 ? -46.179  -5.343  -10.816  1.00 30.84  ? 315 ARG D O   1 
ATOM   15235 C CB  . ARG D  1 315 ? -42.953  -5.550  -11.149  1.00 31.92  ? 315 ARG D CB  1 
ATOM   15236 C CG  . ARG D  1 315 ? -43.477  -6.952  -11.423  1.00 31.97  ? 315 ARG D CG  1 
ATOM   15237 C CD  . ARG D  1 315 ? -42.438  -7.978  -11.039  1.00 35.75  ? 315 ARG D CD  1 
ATOM   15238 N NE  . ARG D  1 315 ? -42.205  -7.956  -9.591   1.00 39.89  ? 315 ARG D NE  1 
ATOM   15239 C CZ  . ARG D  1 315 ? -41.169  -8.489  -8.960   1.00 39.57  ? 315 ARG D CZ  1 
ATOM   15240 N NH1 . ARG D  1 315 ? -40.314  -9.243  -9.603   1.00 38.81  ? 315 ARG D NH1 1 
ATOM   15241 N NH2 . ARG D  1 315 ? -41.008  -8.265  -7.674   1.00 41.15  ? 315 ARG D NH2 1 
ATOM   15242 N N   . ASP D  1 316 ? -44.941  -4.520  -9.104   1.00 33.20  ? 316 ASP D N   1 
ATOM   15243 C CA  . ASP D  1 316 ? -45.933  -4.864  -8.097   1.00 33.71  ? 316 ASP D CA  1 
ATOM   15244 C C   . ASP D  1 316 ? -47.176  -3.998  -8.293   1.00 30.76  ? 316 ASP D C   1 
ATOM   15245 O O   . ASP D  1 316 ? -48.290  -4.475  -8.143   1.00 29.85  ? 316 ASP D O   1 
ATOM   15246 C CB  . ASP D  1 316 ? -45.386  -4.765  -6.682   1.00 34.19  ? 316 ASP D CB  1 
ATOM   15247 C CG  . ASP D  1 316 ? -44.277  -5.735  -6.311   1.00 34.02  ? 316 ASP D CG  1 
ATOM   15248 O OD1 . ASP D  1 316 ? -43.920  -6.602  -7.145   1.00 34.87  ? 316 ASP D OD1 1 
ATOM   15249 O OD2 . ASP D  1 316 ? -43.734  -5.555  -5.201   1.00 35.30  ? 316 ASP D OD2 1 
ATOM   15250 N N   . TYR D  1 317 ? -46.983  -2.737  -8.680   1.00 28.55  ? 317 TYR D N   1 
ATOM   15251 C CA  . TYR D  1 317 ? -48.110  -1.837  -8.863   1.00 29.12  ? 317 TYR D CA  1 
ATOM   15252 C C   . TYR D  1 317 ? -49.007  -2.307  -10.005  1.00 29.02  ? 317 TYR D C   1 
ATOM   15253 O O   . TYR D  1 317 ? -50.212  -2.214  -9.923   1.00 27.48  ? 317 TYR D O   1 
ATOM   15254 C CB  . TYR D  1 317 ? -47.634  -0.416  -9.168   1.00 27.87  ? 317 TYR D CB  1 
ATOM   15255 C CG  . TYR D  1 317 ? -48.781  0.568   -9.187   1.00 26.87  ? 317 TYR D CG  1 
ATOM   15256 C CD1 . TYR D  1 317 ? -49.326  1.051   -8.001   1.00 26.80  ? 317 TYR D CD1 1 
ATOM   15257 C CD2 . TYR D  1 317 ? -49.317  1.037   -10.386  1.00 27.77  ? 317 TYR D CD2 1 
ATOM   15258 C CE1 . TYR D  1 317 ? -50.390  1.948   -8.005   1.00 26.88  ? 317 TYR D CE1 1 
ATOM   15259 C CE2 . TYR D  1 317 ? -50.384  1.936   -10.388  1.00 28.48  ? 317 TYR D CE2 1 
ATOM   15260 C CZ  . TYR D  1 317 ? -50.919  2.399   -9.194   1.00 25.97  ? 317 TYR D CZ  1 
ATOM   15261 O OH  . TYR D  1 317 ? -51.960  3.285   -9.179   1.00 26.74  ? 317 TYR D OH  1 
ATOM   15262 N N   . MET D  1 318 ? -48.419  -2.845  -11.075  1.00 30.82  ? 318 MET D N   1 
ATOM   15263 C CA  . MET D  1 318 ? -49.177  -3.128  -12.283  1.00 30.72  ? 318 MET D CA  1 
ATOM   15264 C C   . MET D  1 318 ? -50.024  -4.390  -12.177  1.00 30.00  ? 318 MET D C   1 
ATOM   15265 O O   . MET D  1 318 ? -50.784  -4.636  -13.095  1.00 31.06  ? 318 MET D O   1 
ATOM   15266 C CB  . MET D  1 318 ? -48.265  -3.261  -13.502  1.00 29.94  ? 318 MET D CB  1 
ATOM   15267 C CG  . MET D  1 318 ? -47.726  -1.938  -13.975  1.00 28.61  ? 318 MET D CG  1 
ATOM   15268 S SD  . MET D  1 318 ? -46.754  -2.113  -15.476  1.00 29.20  ? 318 MET D SD  1 
ATOM   15269 C CE  . MET D  1 318 ? -45.412  -3.127  -14.837  1.00 27.99  ? 318 MET D CE  1 
ATOM   15270 N N   . LYS D  1 319 ? -49.930  -5.142  -11.080  1.00 31.55  ? 319 LYS D N   1 
ATOM   15271 C CA  . LYS D  1 319 ? -50.656  -6.397  -10.939  1.00 36.36  ? 319 LYS D CA  1 
ATOM   15272 C C   . LYS D  1 319 ? -52.176  -6.185  -10.920  1.00 36.03  ? 319 LYS D C   1 
ATOM   15273 O O   . LYS D  1 319 ? -52.919  -6.992  -11.500  1.00 35.68  ? 319 LYS D O   1 
ATOM   15274 C CB  . LYS D  1 319 ? -50.194  -7.194  -9.709   1.00 40.51  ? 319 LYS D CB  1 
ATOM   15275 C CG  . LYS D  1 319 ? -48.760  -7.784  -9.745   1.00 42.63  ? 319 LYS D CG  1 
ATOM   15276 C CD  . LYS D  1 319 ? -48.360  -8.541  -8.472   1.00 45.49  ? 319 LYS D CD  1 
ATOM   15277 C CE  . LYS D  1 319 ? -46.938  -9.086  -8.394   1.00 50.05  ? 319 LYS D CE  1 
ATOM   15278 N NZ  . LYS D  1 319 ? -46.529  -9.475  -7.030   1.00 47.87  ? 319 LYS D NZ  1 
ATOM   15279 N N   . GLY D  1 320 ? -52.642  -5.128  -10.238  1.00 34.13  ? 320 GLY D N   1 
ATOM   15280 C CA  . GLY D  1 320 ? -54.048  -4.747  -10.300  1.00 34.12  ? 320 GLY D CA  1 
ATOM   15281 C C   . GLY D  1 320 ? -54.226  -3.238  -10.371  1.00 34.21  ? 320 GLY D C   1 
ATOM   15282 O O   . GLY D  1 320 ? -53.865  -2.532  -9.430   1.00 31.89  ? 320 GLY D O   1 
ATOM   15283 N N   . LEU D  1 321 ? -54.801  -2.774  -11.493  1.00 35.11  ? 321 LEU D N   1 
ATOM   15284 C CA  . LEU D  1 321 ? -54.954  -1.349  -11.756  1.00 34.04  ? 321 LEU D CA  1 
ATOM   15285 C C   . LEU D  1 321 ? -56.384  -0.950  -11.446  1.00 31.73  ? 321 LEU D C   1 
ATOM   15286 O O   . LEU D  1 321 ? -57.310  -1.652  -11.846  1.00 34.29  ? 321 LEU D O   1 
ATOM   15287 C CB  . LEU D  1 321 ? -54.552  -0.964  -13.182  1.00 33.33  ? 321 LEU D CB  1 
ATOM   15288 C CG  . LEU D  1 321 ? -53.054  -1.112  -13.509  1.00 33.72  ? 321 LEU D CG  1 
ATOM   15289 C CD1 . LEU D  1 321 ? -52.748  -0.822  -14.966  1.00 34.78  ? 321 LEU D CD1 1 
ATOM   15290 C CD2 . LEU D  1 321 ? -52.141  -0.234  -12.663  1.00 33.19  ? 321 LEU D CD2 1 
ATOM   15291 N N   . ILE D  1 322 ? -56.525  0.162   -10.711  1.00 29.75  ? 322 ILE D N   1 
ATOM   15292 C CA  . ILE D  1 322 ? -57.816  0.756   -10.392  1.00 29.26  ? 322 ILE D CA  1 
ATOM   15293 C C   . ILE D  1 322 ? -57.971  1.946   -11.331  1.00 29.01  ? 322 ILE D C   1 
ATOM   15294 O O   . ILE D  1 322 ? -57.185  2.886   -11.211  1.00 28.87  ? 322 ILE D O   1 
ATOM   15295 C CB  . ILE D  1 322 ? -57.925  1.208   -8.914   1.00 28.17  ? 322 ILE D CB  1 
ATOM   15296 C CG1 . ILE D  1 322 ? -57.531  0.156   -7.913   1.00 28.58  ? 322 ILE D CG1 1 
ATOM   15297 C CG2 . ILE D  1 322 ? -59.320  1.733   -8.570   1.00 27.45  ? 322 ILE D CG2 1 
ATOM   15298 C CD1 . ILE D  1 322 ? -57.088  0.734   -6.571   1.00 28.01  ? 322 ILE D CD1 1 
ATOM   15299 N N   . ILE D  1 323 ? -58.967  1.888   -12.235  1.00 29.02  ? 323 ILE D N   1 
ATOM   15300 C CA  . ILE D  1 323 ? -59.272  2.974   -13.160  1.00 29.64  ? 323 ILE D CA  1 
ATOM   15301 C C   . ILE D  1 323 ? -60.438  3.832   -12.652  1.00 29.84  ? 323 ILE D C   1 
ATOM   15302 O O   . ILE D  1 323 ? -60.467  5.039   -12.876  1.00 29.08  ? 323 ILE D O   1 
ATOM   15303 C CB  . ILE D  1 323 ? -59.546  2.409   -14.568  1.00 30.85  ? 323 ILE D CB  1 
ATOM   15304 C CG1 . ILE D  1 323 ? -58.272  1.907   -15.215  1.00 31.39  ? 323 ILE D CG1 1 
ATOM   15305 C CG2 . ILE D  1 323 ? -60.220  3.443   -15.482  1.00 31.98  ? 323 ILE D CG2 1 
ATOM   15306 C CD1 . ILE D  1 323 ? -57.932  0.482   -14.928  1.00 33.49  ? 323 ILE D CD1 1 
ATOM   15307 N N   . SER D  1 324 ? -61.427  3.194   -12.023  1.00 29.51  ? 324 SER D N   1 
ATOM   15308 C CA  . SER D  1 324 ? -62.474  3.908   -11.323  1.00 31.18  ? 324 SER D CA  1 
ATOM   15309 C C   . SER D  1 324 ? -62.781  3.135   -10.047  1.00 32.17  ? 324 SER D C   1 
ATOM   15310 O O   . SER D  1 324 ? -62.617  1.919   -10.035  1.00 34.91  ? 324 SER D O   1 
ATOM   15311 C CB  . SER D  1 324 ? -63.724  4.073   -12.193  1.00 32.28  ? 324 SER D CB  1 
ATOM   15312 O OG  . SER D  1 324 ? -63.396  4.574   -13.491  1.00 30.81  ? 324 SER D OG  1 
ATOM   15313 N N   . PRO D  1 325 ? -63.172  3.783   -8.921   1.00 30.78  ? 325 PRO D N   1 
ATOM   15314 C CA  . PRO D  1 325 ? -63.185  5.239   -8.807   1.00 29.19  ? 325 PRO D CA  1 
ATOM   15315 C C   . PRO D  1 325 ? -61.792  5.843   -8.864   1.00 29.01  ? 325 PRO D C   1 
ATOM   15316 O O   . PRO D  1 325 ? -60.819  5.145   -8.626   1.00 26.63  ? 325 PRO D O   1 
ATOM   15317 C CB  . PRO D  1 325 ? -63.822  5.447   -7.435   1.00 29.43  ? 325 PRO D CB  1 
ATOM   15318 C CG  . PRO D  1 325 ? -63.446  4.229   -6.685   1.00 29.30  ? 325 PRO D CG  1 
ATOM   15319 C CD  . PRO D  1 325 ? -63.630  3.122   -7.693   1.00 30.06  ? 325 PRO D CD  1 
ATOM   15320 N N   . LYS D  1 326 ? -61.743  7.165   -9.086   1.00 29.54  ? 326 LYS D N   1 
ATOM   15321 C CA  . LYS D  1 326 ? -60.490  7.876   -9.256   1.00 28.95  ? 326 LYS D CA  1 
ATOM   15322 C C   . LYS D  1 326 ? -60.091  8.623   -7.978   1.00 27.49  ? 326 LYS D C   1 
ATOM   15323 O O   . LYS D  1 326 ? -60.911  9.194   -7.263   1.00 25.90  ? 326 LYS D O   1 
ATOM   15324 C CB  . LYS D  1 326 ? -60.628  8.778   -10.482  1.00 31.15  ? 326 LYS D CB  1 
ATOM   15325 C CG  . LYS D  1 326 ? -60.648  8.036   -11.809  1.00 33.21  ? 326 LYS D CG  1 
ATOM   15326 C CD  . LYS D  1 326 ? -60.917  8.952   -13.004  1.00 33.95  ? 326 LYS D CD  1 
ATOM   15327 C CE  . LYS D  1 326 ? -61.015  8.206   -14.304  1.00 35.36  ? 326 LYS D CE  1 
ATOM   15328 N NZ  . LYS D  1 326 ? -61.782  6.957   -14.177  1.00 34.71  ? 326 LYS D NZ  1 
ATOM   15329 N N   . ASN D  1 327 ? -58.783  8.588   -7.693   1.00 27.32  ? 327 ASN D N   1 
ATOM   15330 C CA  . ASN D  1 327 ? -58.202  9.296   -6.566   1.00 27.22  ? 327 ASN D CA  1 
ATOM   15331 C C   . ASN D  1 327 ? -58.483  10.794  -6.711   1.00 27.14  ? 327 ASN D C   1 
ATOM   15332 O O   . ASN D  1 327 ? -58.307  11.338  -7.784   1.00 25.61  ? 327 ASN D O   1 
ATOM   15333 C CB  . ASN D  1 327 ? -56.703  9.049   -6.470   1.00 25.68  ? 327 ASN D CB  1 
ATOM   15334 C CG  . ASN D  1 327 ? -56.138  9.443   -5.125   1.00 26.76  ? 327 ASN D CG  1 
ATOM   15335 O OD1 . ASN D  1 327 ? -56.695  9.093   -4.078   1.00 26.88  ? 327 ASN D OD1 1 
ATOM   15336 N ND2 . ASN D  1 327 ? -55.008  10.136  -5.119   1.00 27.90  ? 327 ASN D ND2 1 
ATOM   15337 N N   . LYS D  1 328 ? -58.908  11.415  -5.613   1.00 27.96  ? 328 LYS D N   1 
ATOM   15338 C CA  . LYS D  1 328 ? -59.300  12.812  -5.551   1.00 30.96  ? 328 LYS D CA  1 
ATOM   15339 C C   . LYS D  1 328 ? -60.487  13.106  -6.471   1.00 31.40  ? 328 LYS D C   1 
ATOM   15340 O O   . LYS D  1 328 ? -60.620  14.220  -6.979   1.00 35.48  ? 328 LYS D O   1 
ATOM   15341 C CB  . LYS D  1 328 ? -58.113  13.741  -5.805   1.00 30.61  ? 328 LYS D CB  1 
ATOM   15342 C CG  . LYS D  1 328 ? -56.908  13.466  -4.930   1.00 31.59  ? 328 LYS D CG  1 
ATOM   15343 C CD  . LYS D  1 328 ? -57.228  13.448  -3.438   1.00 33.79  ? 328 LYS D CD  1 
ATOM   15344 C CE  . LYS D  1 328 ? -56.011  13.103  -2.637   1.00 34.86  ? 328 LYS D CE  1 
ATOM   15345 N NZ  . LYS D  1 328 ? -54.931  14.089  -2.830   1.00 35.39  ? 328 LYS D NZ  1 
ATOM   15346 N N   . SER D  1 329 ? -61.383  12.127  -6.614   1.00 29.84  ? 329 SER D N   1 
ATOM   15347 C CA  . SER D  1 329 ? -62.620  12.317  -7.351   1.00 29.08  ? 329 SER D CA  1 
ATOM   15348 C C   . SER D  1 329 ? -63.701  12.751  -6.382   1.00 29.26  ? 329 SER D C   1 
ATOM   15349 O O   . SER D  1 329 ? -63.671  12.388  -5.195   1.00 29.78  ? 329 SER D O   1 
ATOM   15350 C CB  . SER D  1 329 ? -63.054  11.066  -8.090   1.00 28.87  ? 329 SER D CB  1 
ATOM   15351 O OG  . SER D  1 329 ? -63.391  10.045  -7.157   1.00 27.60  ? 329 SER D OG  1 
ATOM   15352 N N   . ILE D  1 330 ? -64.675  13.486  -6.933   1.00 31.23  ? 330 ILE D N   1 
ATOM   15353 C CA  . ILE D  1 330 ? -65.793  13.999  -6.164   1.00 32.21  ? 330 ILE D CA  1 
ATOM   15354 C C   . ILE D  1 330 ? -67.048  13.338  -6.701   1.00 32.31  ? 330 ILE D C   1 
ATOM   15355 O O   . ILE D  1 330 ? -67.196  13.277  -7.908   1.00 34.34  ? 330 ILE D O   1 
ATOM   15356 C CB  . ILE D  1 330 ? -65.828  15.533  -6.254   1.00 33.80  ? 330 ILE D CB  1 
ATOM   15357 C CG1 . ILE D  1 330 ? -64.604  16.157  -5.532   1.00 33.88  ? 330 ILE D CG1 1 
ATOM   15358 C CG2 . ILE D  1 330 ? -67.154  16.076  -5.719   1.00 34.47  ? 330 ILE D CG2 1 
ATOM   15359 C CD1 . ILE D  1 330 ? -64.431  17.650  -5.753   1.00 35.81  ? 330 ILE D CD1 1 
ATOM   15360 N N   . HIS D  1 331 ? -67.917  12.870  -5.798   1.00 32.35  ? 331 HIS D N   1 
ATOM   15361 C CA  . HIS D  1 331 ? -69.053  12.027  -6.117   1.00 32.59  ? 331 HIS D CA  1 
ATOM   15362 C C   . HIS D  1 331 ? -70.299  12.592  -5.471   1.00 33.69  ? 331 HIS D C   1 
ATOM   15363 O O   . HIS D  1 331 ? -70.241  12.973  -4.318   1.00 33.25  ? 331 HIS D O   1 
ATOM   15364 C CB  . HIS D  1 331 ? -68.804  10.599  -5.616   1.00 32.58  ? 331 HIS D CB  1 
ATOM   15365 C CG  . HIS D  1 331 ? -67.903  9.886   -6.557   1.00 32.79  ? 331 HIS D CG  1 
ATOM   15366 N ND1 . HIS D  1 331 ? -66.520  9.984   -6.512   1.00 32.74  ? 331 HIS D ND1 1 
ATOM   15367 C CD2 . HIS D  1 331 ? -68.213  9.184   -7.660   1.00 32.90  ? 331 HIS D CD2 1 
ATOM   15368 C CE1 . HIS D  1 331 ? -66.022  9.283   -7.530   1.00 32.91  ? 331 HIS D CE1 1 
ATOM   15369 N NE2 . HIS D  1 331 ? -67.033  8.787   -8.236   1.00 32.99  ? 331 HIS D NE2 1 
ATOM   15370 N N   . THR D  1 332 ? -71.404  12.650  -6.223   1.00 37.14  ? 332 THR D N   1 
ATOM   15371 C CA  . THR D  1 332 ? -72.651  13.245  -5.729   1.00 40.09  ? 332 THR D CA  1 
ATOM   15372 C C   . THR D  1 332 ? -73.769  12.210  -5.781   1.00 42.03  ? 332 THR D C   1 
ATOM   15373 O O   . THR D  1 332 ? -74.929  12.539  -5.642   1.00 48.75  ? 332 THR D O   1 
ATOM   15374 C CB  . THR D  1 332 ? -73.003  14.512  -6.515   1.00 40.21  ? 332 THR D CB  1 
ATOM   15375 O OG1 . THR D  1 332 ? -72.912  14.125  -7.880   1.00 39.61  ? 332 THR D OG1 1 
ATOM   15376 C CG2 . THR D  1 332 ? -72.024  15.650  -6.277   1.00 38.80  ? 332 THR D CG2 1 
ATOM   15377 N N   . ASN D  1 333 ? -73.376  10.940  -5.894   1.00 44.93  ? 333 ASN D N   1 
ATOM   15378 C CA  . ASN D  1 333 ? -74.249  9.791   -6.011   1.00 43.34  ? 333 ASN D CA  1 
ATOM   15379 C C   . ASN D  1 333 ? -73.600  8.677   -5.201   1.00 40.43  ? 333 ASN D C   1 
ATOM   15380 O O   . ASN D  1 333 ? -72.409  8.457   -5.363   1.00 41.17  ? 333 ASN D O   1 
ATOM   15381 C CB  . ASN D  1 333 ? -74.392  9.359   -7.467   1.00 45.14  ? 333 ASN D CB  1 
ATOM   15382 C CG  . ASN D  1 333 ? -75.564  8.416   -7.638   1.00 52.94  ? 333 ASN D CG  1 
ATOM   15383 O OD1 . ASN D  1 333 ? -75.453  7.200   -7.404   1.00 52.03  ? 333 ASN D OD1 1 
ATOM   15384 N ND2 . ASN D  1 333 ? -76.719  8.964   -8.000   1.00 55.55  ? 333 ASN D ND2 1 
ATOM   15385 N N   . THR D  1 334 ? -74.367  7.954   -4.383   1.00 39.48  ? 334 THR D N   1 
ATOM   15386 C CA  . THR D  1 334 ? -73.824  6.867   -3.580   1.00 39.43  ? 334 THR D CA  1 
ATOM   15387 C C   . THR D  1 334 ? -73.611  5.567   -4.391   1.00 40.02  ? 334 THR D C   1 
ATOM   15388 O O   . THR D  1 334 ? -73.136  4.587   -3.841   1.00 39.23  ? 334 THR D O   1 
ATOM   15389 C CB  . THR D  1 334 ? -74.719  6.640   -2.364   1.00 39.13  ? 334 THR D CB  1 
ATOM   15390 O OG1 . THR D  1 334 ? -75.934  6.166   -2.902   1.00 39.45  ? 334 THR D OG1 1 
ATOM   15391 C CG2 . THR D  1 334 ? -75.016  7.882   -1.543   1.00 39.85  ? 334 THR D CG2 1 
ATOM   15392 N N   . LYS D  1 335 ? -73.894  5.540   -5.700   1.00 41.43  ? 335 LYS D N   1 
ATOM   15393 C CA  . LYS D  1 335 ? -73.467  4.436   -6.541   1.00 43.30  ? 335 LYS D CA  1 
ATOM   15394 C C   . LYS D  1 335 ? -72.238  4.855   -7.331   1.00 43.14  ? 335 LYS D C   1 
ATOM   15395 O O   . LYS D  1 335 ? -72.349  5.706   -8.211   1.00 45.98  ? 335 LYS D O   1 
ATOM   15396 C CB  . LYS D  1 335 ? -74.493  3.992   -7.585   1.00 47.35  ? 335 LYS D CB  1 
ATOM   15397 C CG  . LYS D  1 335 ? -75.688  3.157   -7.103   1.00 52.35  ? 335 LYS D CG  1 
ATOM   15398 C CD  . LYS D  1 335 ? -75.414  1.666   -6.922   1.00 56.99  ? 335 LYS D CD  1 
ATOM   15399 C CE  . LYS D  1 335 ? -76.647  0.791   -6.742   1.00 56.15  ? 335 LYS D CE  1 
ATOM   15400 N NZ  . LYS D  1 335 ? -77.081  0.720   -5.342   1.00 57.73  ? 335 LYS D NZ  1 
ATOM   15401 N N   . ILE D  1 336 ? -71.114  4.192   -7.042   1.00 41.14  ? 336 ILE D N   1 
ATOM   15402 C CA  . ILE D  1 336 ? -69.795  4.564   -7.534   1.00 43.51  ? 336 ILE D CA  1 
ATOM   15403 C C   . ILE D  1 336 ? -69.364  3.551   -8.579   1.00 41.57  ? 336 ILE D C   1 
ATOM   15404 O O   . ILE D  1 336 ? -69.158  2.400   -8.200   1.00 44.78  ? 336 ILE D O   1 
ATOM   15405 C CB  . ILE D  1 336 ? -68.773  4.592   -6.372   1.00 44.99  ? 336 ILE D CB  1 
ATOM   15406 C CG1 . ILE D  1 336 ? -69.138  5.634   -5.335   1.00 47.53  ? 336 ILE D CG1 1 
ATOM   15407 C CG2 . ILE D  1 336 ? -67.329  4.798   -6.831   1.00 47.13  ? 336 ILE D CG2 1 
ATOM   15408 C CD1 . ILE D  1 336 ? -69.816  6.859   -5.921   1.00 47.72  ? 336 ILE D CD1 1 
ATOM   15409 N N   . PRO D  1 337 ? -69.171  3.931   -9.868   1.00 37.12  ? 337 PRO D N   1 
ATOM   15410 C CA  . PRO D  1 337 ? -68.618  2.997   -10.840  1.00 37.32  ? 337 PRO D CA  1 
ATOM   15411 C C   . PRO D  1 337 ? -67.225  2.533   -10.376  1.00 40.62  ? 337 PRO D C   1 
ATOM   15412 O O   . PRO D  1 337 ? -66.369  3.314   -9.922   1.00 37.89  ? 337 PRO D O   1 
ATOM   15413 C CB  . PRO D  1 337 ? -68.639  3.753   -12.193  1.00 35.37  ? 337 PRO D CB  1 
ATOM   15414 C CG  . PRO D  1 337 ? -69.563  4.947   -11.963  1.00 35.40  ? 337 PRO D CG  1 
ATOM   15415 C CD  . PRO D  1 337 ? -69.482  5.237   -10.471  1.00 36.39  ? 337 PRO D CD  1 
ATOM   15416 N N   . LEU D  1 338 ? -67.039  1.201   -10.427  1.00 39.95  ? 338 LEU D N   1 
ATOM   15417 C CA  . LEU D  1 338 ? -65.751  0.573   -10.210  1.00 38.12  ? 338 LEU D CA  1 
ATOM   15418 C C   . LEU D  1 338 ? -65.256  -0.006  -11.539  1.00 34.54  ? 338 LEU D C   1 
ATOM   15419 O O   . LEU D  1 338 ? -66.023  -0.570  -12.308  1.00 33.65  ? 338 LEU D O   1 
ATOM   15420 C CB  . LEU D  1 338 ? -66.008  -0.471  -9.126   1.00 42.34  ? 338 LEU D CB  1 
ATOM   15421 C CG  . LEU D  1 338 ? -64.886  -1.485  -8.901   1.00 43.80  ? 338 LEU D CG  1 
ATOM   15422 C CD1 . LEU D  1 338 ? -63.710  -0.825  -8.280   1.00 43.16  ? 338 LEU D CD1 1 
ATOM   15423 C CD2 . LEU D  1 338 ? -65.390  -2.588  -8.023   1.00 46.57  ? 338 LEU D CD2 1 
ATOM   15424 N N   . GLU D  1 339 ? -63.982  0.214   -11.851  1.00 32.41  ? 339 GLU D N   1 
ATOM   15425 C CA  . GLU D  1 339 ? -63.383  -0.327  -13.052  1.00 31.89  ? 339 GLU D CA  1 
ATOM   15426 C C   . GLU D  1 339 ? -61.957  -0.731  -12.715  1.00 30.88  ? 339 GLU D C   1 
ATOM   15427 O O   . GLU D  1 339 ? -61.201  0.112   -12.241  1.00 30.73  ? 339 GLU D O   1 
ATOM   15428 C CB  . GLU D  1 339 ? -63.277  0.687   -14.186  1.00 34.22  ? 339 GLU D CB  1 
ATOM   15429 C CG  . GLU D  1 339 ? -64.613  1.218   -14.697  1.00 35.72  ? 339 GLU D CG  1 
ATOM   15430 C CD  . GLU D  1 339 ? -64.443  2.233   -15.818  1.00 37.57  ? 339 GLU D CD  1 
ATOM   15431 O OE1 . GLU D  1 339 ? -64.148  3.424   -15.566  1.00 39.25  ? 339 GLU D OE1 1 
ATOM   15432 O OE2 . GLU D  1 339 ? -64.520  1.779   -16.974  1.00 38.08  ? 339 GLU D OE2 1 
ATOM   15433 N N   . LEU D  1 340 ? -61.624  -2.005  -12.976  1.00 30.10  ? 340 LEU D N   1 
ATOM   15434 C CA  . LEU D  1 340 ? -60.323  -2.572  -12.676  1.00 29.28  ? 340 LEU D CA  1 
ATOM   15435 C C   . LEU D  1 340 ? -59.744  -3.248  -13.917  1.00 29.03  ? 340 LEU D C   1 
ATOM   15436 O O   . LEU D  1 340 ? -60.483  -3.699  -14.771  1.00 28.19  ? 340 LEU D O   1 
ATOM   15437 C CB  . LEU D  1 340 ? -60.470  -3.580  -11.545  1.00 30.42  ? 340 LEU D CB  1 
ATOM   15438 C CG  . LEU D  1 340 ? -61.064  -3.074  -10.229  1.00 29.96  ? 340 LEU D CG  1 
ATOM   15439 C CD1 . LEU D  1 340 ? -61.141  -4.264  -9.292   1.00 29.85  ? 340 LEU D CD1 1 
ATOM   15440 C CD2 . LEU D  1 340 ? -60.270  -1.950  -9.621   1.00 29.11  ? 340 LEU D CD2 1 
ATOM   15441 N N   . TYR D  1 341 ? -58.404  -3.291  -13.997  1.00 30.70  ? 341 TYR D N   1 
ATOM   15442 C CA  . TYR D  1 341 ? -57.679  -4.066  -14.996  1.00 31.61  ? 341 TYR D CA  1 
ATOM   15443 C C   . TYR D  1 341 ? -56.661  -4.932  -14.250  1.00 33.09  ? 341 TYR D C   1 
ATOM   15444 O O   . TYR D  1 341 ? -55.696  -4.421  -13.693  1.00 32.30  ? 341 TYR D O   1 
ATOM   15445 C CB  . TYR D  1 341 ? -56.980  -3.220  -16.064  1.00 31.38  ? 341 TYR D CB  1 
ATOM   15446 C CG  . TYR D  1 341 ? -56.504  -4.006  -17.281  1.00 33.55  ? 341 TYR D CG  1 
ATOM   15447 C CD1 . TYR D  1 341 ? -57.323  -4.205  -18.394  1.00 34.09  ? 341 TYR D CD1 1 
ATOM   15448 C CD2 . TYR D  1 341 ? -55.261  -4.619  -17.289  1.00 34.99  ? 341 TYR D CD2 1 
ATOM   15449 C CE1 . TYR D  1 341 ? -56.916  -4.977  -19.473  1.00 34.29  ? 341 TYR D CE1 1 
ATOM   15450 C CE2 . TYR D  1 341 ? -54.852  -5.414  -18.355  1.00 35.21  ? 341 TYR D CE2 1 
ATOM   15451 C CZ  . TYR D  1 341 ? -55.665  -5.567  -19.464  1.00 34.99  ? 341 TYR D CZ  1 
ATOM   15452 O OH  . TYR D  1 341 ? -55.214  -6.350  -20.498  1.00 34.70  ? 341 TYR D OH  1 
ATOM   15453 N N   . ASN D  1 342 ? -56.964  -6.224  -14.212  1.00 35.57  ? 342 ASN D N   1 
ATOM   15454 C CA  . ASN D  1 342 ? -56.175  -7.135  -13.359  1.00 35.15  ? 342 ASN D CA  1 
ATOM   15455 C C   . ASN D  1 342 ? -55.322  -8.092  -14.180  1.00 37.69  ? 342 ASN D C   1 
ATOM   15456 O O   . ASN D  1 342 ? -55.710  -8.440  -15.299  1.00 42.29  ? 342 ASN D O   1 
ATOM   15457 C CB  . ASN D  1 342 ? -57.125  -7.909  -12.456  1.00 35.93  ? 342 ASN D CB  1 
ATOM   15458 C CG  . ASN D  1 342 ? -57.895  -7.041  -11.495  1.00 34.72  ? 342 ASN D CG  1 
ATOM   15459 O OD1 . ASN D  1 342 ? -59.129  -7.073  -11.484  1.00 37.63  ? 342 ASN D OD1 1 
ATOM   15460 N ND2 . ASN D  1 342 ? -57.194  -6.289  -10.665  1.00 32.07  ? 342 ASN D ND2 1 
ATOM   15461 N N   . ASP D  1 343 ? -54.187  -8.482  -13.618  1.00 38.32  ? 343 ASP D N   1 
ATOM   15462 C CA  . ASP D  1 343 ? -53.333  -9.497  -14.279  1.00 39.56  ? 343 ASP D CA  1 
ATOM   15463 C C   . ASP D  1 343 ? -53.833  -10.890 -13.880  1.00 38.48  ? 343 ASP D C   1 
ATOM   15464 O O   . ASP D  1 343 ? -54.746  -10.971 -13.047  1.00 34.40  ? 343 ASP D O   1 
ATOM   15465 C CB  . ASP D  1 343 ? -51.853  -9.212  -14.050  1.00 39.54  ? 343 ASP D CB  1 
ATOM   15466 C CG  . ASP D  1 343 ? -51.202  -9.715  -12.771  1.00 39.81  ? 343 ASP D CG  1 
ATOM   15467 O OD1 . ASP D  1 343 ? -51.921  -10.034 -11.811  1.00 40.07  ? 343 ASP D OD1 1 
ATOM   15468 O OD2 . ASP D  1 343 ? -49.963  -9.756  -12.747  1.00 42.40  ? 343 ASP D OD2 1 
ATOM   15469 N N   . LYS D  1 344 ? -53.224  -11.932 -14.439  1.00 42.67  ? 344 LYS D N   1 
ATOM   15470 C CA  . LYS D  1 344 ? -53.652  -13.333 -14.219  1.00 45.27  ? 344 LYS D CA  1 
ATOM   15471 C C   . LYS D  1 344 ? -53.487  -13.778 -12.771  1.00 41.28  ? 344 LYS D C   1 
ATOM   15472 O O   . LYS D  1 344 ? -54.040  -14.828 -12.430  1.00 39.49  ? 344 LYS D O   1 
ATOM   15473 C CB  . LYS D  1 344 ? -52.749  -14.208 -15.085  1.00 55.63  ? 344 LYS D CB  1 
ATOM   15474 C CG  . LYS D  1 344 ? -53.475  -15.141 -16.040  1.00 64.15  ? 344 LYS D CG  1 
ATOM   15475 C CD  . LYS D  1 344 ? -52.527  -15.892 -16.966  1.00 70.65  ? 344 LYS D CD  1 
ATOM   15476 C CE  . LYS D  1 344 ? -53.229  -16.578 -18.097  1.00 75.08  ? 344 LYS D CE  1 
ATOM   15477 N NZ  . LYS D  1 344 ? -54.319  -17.438 -17.629  1.00 74.74  ? 344 LYS D NZ  1 
ATOM   15478 N N   . ASP D  1 345 ? -52.781  -13.006 -11.958  1.00 36.09  ? 345 ASP D N   1 
ATOM   15479 C CA  . ASP D  1 345 ? -52.502  -13.463 -10.577  1.00 34.40  ? 345 ASP D CA  1 
ATOM   15480 C C   . ASP D  1 345 ? -53.608  -12.999 -9.629   1.00 33.40  ? 345 ASP D C   1 
ATOM   15481 O O   . ASP D  1 345 ? -53.767  -13.625 -8.580   1.00 34.05  ? 345 ASP D O   1 
ATOM   15482 C CB  . ASP D  1 345 ? -51.094  -13.078 -10.165  1.00 35.13  ? 345 ASP D CB  1 
ATOM   15483 C CG  . ASP D  1 345 ? -49.980  -13.765 -10.933  1.00 34.43  ? 345 ASP D CG  1 
ATOM   15484 O OD1 . ASP D  1 345 ? -50.261  -14.791 -11.576  1.00 35.95  ? 345 ASP D OD1 1 
ATOM   15485 O OD2 . ASP D  1 345 ? -48.846  -13.266 -10.874  1.00 33.56  ? 345 ASP D OD2 1 
ATOM   15486 N N   . VAL D  1 346 ? -54.349  -11.959 -10.001  1.00 31.70  ? 346 VAL D N   1 
ATOM   15487 C CA  . VAL D  1 346 ? -55.436  -11.416 -9.127   1.00 31.42  ? 346 VAL D CA  1 
ATOM   15488 C C   . VAL D  1 346 ? -56.636  -12.380 -9.144   1.00 32.82  ? 346 VAL D C   1 
ATOM   15489 O O   . VAL D  1 346 ? -57.204  -12.603 -10.221  1.00 32.25  ? 346 VAL D O   1 
ATOM   15490 C CB  . VAL D  1 346 ? -55.876  -9.976  -9.462   1.00 31.47  ? 346 VAL D CB  1 
ATOM   15491 C CG1 . VAL D  1 346 ? -56.965  -9.489  -8.517   1.00 31.19  ? 346 VAL D CG1 1 
ATOM   15492 C CG2 . VAL D  1 346 ? -54.698  -9.011  -9.467   1.00 32.22  ? 346 VAL D CG2 1 
ATOM   15493 N N   . LYS D  1 347 ? -56.978  -12.938 -7.983   1.00 35.14  ? 347 LYS D N   1 
ATOM   15494 C CA  . LYS D  1 347 ? -58.154  -13.808 -7.910   1.00 38.80  ? 347 LYS D CA  1 
ATOM   15495 C C   . LYS D  1 347 ? -59.276  -13.225 -7.060   1.00 38.80  ? 347 LYS D C   1 
ATOM   15496 O O   . LYS D  1 347 ? -60.384  -13.753 -7.096   1.00 42.80  ? 347 LYS D O   1 
ATOM   15497 C CB  . LYS D  1 347 ? -57.848  -15.180 -7.299   1.00 39.30  ? 347 LYS D CB  1 
ATOM   15498 C CG  . LYS D  1 347 ? -56.775  -15.901 -8.083   1.00 42.51  ? 347 LYS D CG  1 
ATOM   15499 C CD  . LYS D  1 347 ? -57.008  -16.015 -9.589   1.00 45.58  ? 347 LYS D CD  1 
ATOM   15500 C CE  . LYS D  1 347 ? -55.906  -16.786 -10.294  1.00 49.09  ? 347 LYS D CE  1 
ATOM   15501 N NZ  . LYS D  1 347 ? -56.068  -16.702 -11.750  1.00 48.73  ? 347 LYS D NZ  1 
ATOM   15502 N N   . LYS D  1 348 ? -58.992  -12.166 -6.292   1.00 37.67  ? 348 LYS D N   1 
ATOM   15503 C CA  . LYS D  1 348 ? -60.026  -11.527 -5.497   1.00 37.01  ? 348 LYS D CA  1 
ATOM   15504 C C   . LYS D  1 348 ? -59.642  -10.068 -5.277   1.00 35.32  ? 348 LYS D C   1 
ATOM   15505 O O   . LYS D  1 348 ? -58.457  -9.735  -5.202   1.00 34.19  ? 348 LYS D O   1 
ATOM   15506 C CB  . LYS D  1 348 ? -60.207  -12.263 -4.163   1.00 37.20  ? 348 LYS D CB  1 
ATOM   15507 C CG  . LYS D  1 348 ? -61.296  -11.679 -3.259   1.00 38.12  ? 348 LYS D CG  1 
ATOM   15508 C CD  . LYS D  1 348 ? -61.585  -12.451 -1.979   1.00 38.08  ? 348 LYS D CD  1 
ATOM   15509 C CE  . LYS D  1 348 ? -60.356  -12.660 -1.143   1.00 37.41  ? 348 LYS D CE  1 
ATOM   15510 N NZ  . LYS D  1 348 ? -60.676  -13.354 0.111    1.00 38.19  ? 348 LYS D NZ  1 
ATOM   15511 N N   . VAL D  1 349 ? -60.669  -9.231  -5.133   1.00 34.46  ? 349 VAL D N   1 
ATOM   15512 C CA  . VAL D  1 349 ? -60.515  -7.823  -4.824   1.00 33.74  ? 349 VAL D CA  1 
ATOM   15513 C C   . VAL D  1 349 ? -61.518  -7.434  -3.750   1.00 33.39  ? 349 VAL D C   1 
ATOM   15514 O O   . VAL D  1 349 ? -62.709  -7.677  -3.882   1.00 34.43  ? 349 VAL D O   1 
ATOM   15515 C CB  . VAL D  1 349 ? -60.727  -6.951  -6.063   1.00 35.17  ? 349 VAL D CB  1 
ATOM   15516 C CG1 . VAL D  1 349 ? -60.718  -5.467  -5.694   1.00 34.99  ? 349 VAL D CG1 1 
ATOM   15517 C CG2 . VAL D  1 349 ? -59.656  -7.234  -7.110   1.00 35.53  ? 349 VAL D CG2 1 
ATOM   15518 N N   . VAL D  1 350 ? -61.023  -6.811  -2.692   1.00 32.55  ? 350 VAL D N   1 
ATOM   15519 C CA  . VAL D  1 350 ? -61.885  -6.306  -1.648   1.00 32.11  ? 350 VAL D CA  1 
ATOM   15520 C C   . VAL D  1 350 ? -61.690  -4.791  -1.573   1.00 32.94  ? 350 VAL D C   1 
ATOM   15521 O O   . VAL D  1 350 ? -60.589  -4.285  -1.810   1.00 33.24  ? 350 VAL D O   1 
ATOM   15522 C CB  . VAL D  1 350 ? -61.511  -7.009  -0.340   1.00 33.19  ? 350 VAL D CB  1 
ATOM   15523 C CG1 . VAL D  1 350 ? -62.395  -6.548  0.798    1.00 34.47  ? 350 VAL D CG1 1 
ATOM   15524 C CG2 . VAL D  1 350 ? -61.571  -8.535  -0.449   1.00 34.60  ? 350 VAL D CG2 1 
ATOM   15525 N N   . VAL D  1 351 ? -62.779  -4.060  -1.328   1.00 32.14  ? 351 VAL D N   1 
ATOM   15526 C CA  . VAL D  1 351 ? -62.688  -2.683  -0.902   1.00 31.32  ? 351 VAL D CA  1 
ATOM   15527 C C   . VAL D  1 351 ? -63.195  -2.598  0.528    1.00 31.51  ? 351 VAL D C   1 
ATOM   15528 O O   . VAL D  1 351 ? -64.299  -3.063  0.833    1.00 33.28  ? 351 VAL D O   1 
ATOM   15529 C CB  . VAL D  1 351 ? -63.468  -1.704  -1.804   1.00 32.16  ? 351 VAL D CB  1 
ATOM   15530 C CG1 . VAL D  1 351 ? -63.491  -0.297  -1.222   1.00 31.17  ? 351 VAL D CG1 1 
ATOM   15531 C CG2 . VAL D  1 351 ? -62.909  -1.649  -3.218   1.00 32.80  ? 351 VAL D CG2 1 
ATOM   15532 N N   . LYS D  1 352 ? -62.408  -1.939  1.377    1.00 31.83  ? 352 LYS D N   1 
ATOM   15533 C CA  . LYS D  1 352 ? -62.845  -1.588  2.720    1.00 33.17  ? 352 LYS D CA  1 
ATOM   15534 C C   . LYS D  1 352 ? -62.948  -0.061  2.887    1.00 33.75  ? 352 LYS D C   1 
ATOM   15535 O O   . LYS D  1 352 ? -62.227  0.723   2.247    1.00 33.00  ? 352 LYS D O   1 
ATOM   15536 C CB  . LYS D  1 352 ? -61.888  -2.148  3.771    1.00 34.59  ? 352 LYS D CB  1 
ATOM   15537 C CG  . LYS D  1 352 ? -61.953  -3.648  4.006    1.00 36.40  ? 352 LYS D CG  1 
ATOM   15538 C CD  . LYS D  1 352 ? -60.685  -4.226  4.627    1.00 38.46  ? 352 LYS D CD  1 
ATOM   15539 C CE  . LYS D  1 352 ? -60.855  -5.740  4.580    1.00 41.71  ? 352 LYS D CE  1 
ATOM   15540 N NZ  . LYS D  1 352 ? -59.654  -6.530  4.876    1.00 42.04  ? 352 LYS D NZ  1 
ATOM   15541 N N   . PHE D  1 353 ? -63.849  0.324   3.797    1.00 32.08  ? 353 PHE D N   1 
ATOM   15542 C CA  . PHE D  1 353 ? -63.866  1.627   4.425    1.00 31.35  ? 353 PHE D CA  1 
ATOM   15543 C C   . PHE D  1 353 ? -63.941  1.457   5.938    1.00 30.95  ? 353 PHE D C   1 
ATOM   15544 O O   . PHE D  1 353 ? -64.869  0.821   6.429    1.00 32.49  ? 353 PHE D O   1 
ATOM   15545 C CB  . PHE D  1 353 ? -65.085  2.393   3.897    1.00 31.07  ? 353 PHE D CB  1 
ATOM   15546 C CG  . PHE D  1 353 ? -65.145  3.810   4.415    1.00 30.34  ? 353 PHE D CG  1 
ATOM   15547 C CD1 . PHE D  1 353 ? -64.063  4.664   4.256    1.00 28.81  ? 353 PHE D CD1 1 
ATOM   15548 C CD2 . PHE D  1 353 ? -66.259  4.267   5.112    1.00 31.64  ? 353 PHE D CD2 1 
ATOM   15549 C CE1 . PHE D  1 353 ? -64.100  5.953   4.757    1.00 28.44  ? 353 PHE D CE1 1 
ATOM   15550 C CE2 . PHE D  1 353 ? -66.283  5.565   5.607    1.00 31.06  ? 353 PHE D CE2 1 
ATOM   15551 C CZ  . PHE D  1 353 ? -65.197  6.399   5.429    1.00 29.36  ? 353 PHE D CZ  1 
ATOM   15552 N N   . ARG D  1 354 ? -62.961  2.025   6.650    1.00 30.33  ? 354 ARG D N   1 
ATOM   15553 C CA  . ARG D  1 354 ? -62.893  1.935   8.095    1.00 31.65  ? 354 ARG D CA  1 
ATOM   15554 C C   . ARG D  1 354 ? -62.898  0.469   8.520    1.00 32.33  ? 354 ARG D C   1 
ATOM   15555 O O   . ARG D  1 354 ? -63.552  0.110   9.492    1.00 32.93  ? 354 ARG D O   1 
ATOM   15556 C CB  . ARG D  1 354 ? -64.053  2.725   8.727    1.00 33.34  ? 354 ARG D CB  1 
ATOM   15557 C CG  . ARG D  1 354 ? -63.888  4.227   8.504    1.00 33.34  ? 354 ARG D CG  1 
ATOM   15558 C CD  . ARG D  1 354 ? -64.946  5.069   9.167    1.00 33.24  ? 354 ARG D CD  1 
ATOM   15559 N NE  . ARG D  1 354 ? -64.857  6.486   8.798    1.00 33.27  ? 354 ARG D NE  1 
ATOM   15560 C CZ  . ARG D  1 354 ? -65.860  7.366   8.977    1.00 32.44  ? 354 ARG D CZ  1 
ATOM   15561 N NH1 . ARG D  1 354 ? -66.879  7.055   9.754    1.00 33.53  ? 354 ARG D NH1 1 
ATOM   15562 N NH2 . ARG D  1 354 ? -65.842  8.533   8.371    1.00 31.08  ? 354 ARG D NH2 1 
ATOM   15563 N N   . ASP D  1 355 ? -62.162  -0.373  7.779    1.00 32.09  ? 355 ASP D N   1 
ATOM   15564 C CA  . ASP D  1 355 ? -61.919  -1.747  8.191    1.00 33.27  ? 355 ASP D CA  1 
ATOM   15565 C C   . ASP D  1 355 ? -63.210  -2.557  8.095    1.00 34.63  ? 355 ASP D C   1 
ATOM   15566 O O   . ASP D  1 355 ? -63.338  -3.592  8.721    1.00 33.39  ? 355 ASP D O   1 
ATOM   15567 C CB  . ASP D  1 355 ? -61.376  -1.799  9.606    1.00 32.67  ? 355 ASP D CB  1 
ATOM   15568 C CG  . ASP D  1 355 ? -60.326  -0.738  9.890    1.00 32.93  ? 355 ASP D CG  1 
ATOM   15569 O OD1 . ASP D  1 355 ? -59.211  -0.897  9.372    1.00 31.26  ? 355 ASP D OD1 1 
ATOM   15570 O OD2 . ASP D  1 355 ? -60.647  0.242   10.616   1.00 33.64  ? 355 ASP D OD2 1 
ATOM   15571 N N   . LYS D  1 356 ? -64.180  -2.049  7.328    1.00 35.78  ? 356 LYS D N   1 
ATOM   15572 C CA  . LYS D  1 356 ? -65.349  -2.833  6.980    1.00 35.68  ? 356 LYS D CA  1 
ATOM   15573 C C   . LYS D  1 356 ? -65.397  -3.048  5.473    1.00 33.90  ? 356 LYS D C   1 
ATOM   15574 O O   . LYS D  1 356 ? -65.239  -2.093  4.707    1.00 31.75  ? 356 LYS D O   1 
ATOM   15575 C CB  . LYS D  1 356 ? -66.658  -2.161  7.395    1.00 36.91  ? 356 LYS D CB  1 
ATOM   15576 C CG  . LYS D  1 356 ? -67.859  -3.020  7.022    1.00 38.32  ? 356 LYS D CG  1 
ATOM   15577 C CD  . LYS D  1 356 ? -68.985  -2.954  8.039    1.00 41.66  ? 356 LYS D CD  1 
ATOM   15578 C CE  . LYS D  1 356 ? -69.586  -1.609  8.084    1.00 43.59  ? 356 LYS D CE  1 
ATOM   15579 N NZ  . LYS D  1 356 ? -70.839  -1.780  8.806    1.00 47.36  ? 356 LYS D NZ  1 
ATOM   15580 N N   . VAL D  1 357 ? -65.671  -4.305  5.095    1.00 34.34  ? 357 VAL D N   1 
ATOM   15581 C CA  . VAL D  1 357 ? -65.845  -4.727  3.705    1.00 34.71  ? 357 VAL D CA  1 
ATOM   15582 C C   . VAL D  1 357 ? -67.133  -4.118  3.161    1.00 33.29  ? 357 VAL D C   1 
ATOM   15583 O O   . VAL D  1 357 ? -68.201  -4.423  3.681    1.00 32.79  ? 357 VAL D O   1 
ATOM   15584 C CB  . VAL D  1 357 ? -65.899  -6.268  3.496    1.00 34.32  ? 357 VAL D CB  1 
ATOM   15585 C CG1 . VAL D  1 357 ? -66.110  -6.609  2.031    1.00 33.03  ? 357 VAL D CG1 1 
ATOM   15586 C CG2 . VAL D  1 357 ? -64.652  -6.990  4.009    1.00 33.70  ? 357 VAL D CG2 1 
ATOM   15587 N N   . ILE D  1 358 ? -66.986  -3.296  2.105    1.00 33.22  ? 358 ILE D N   1 
ATOM   15588 C CA  . ILE D  1 358 ? -68.114  -2.756  1.365    1.00 34.53  ? 358 ILE D CA  1 
ATOM   15589 C C   . ILE D  1 358 ? -68.156  -3.281  -0.063   1.00 35.33  ? 358 ILE D C   1 
ATOM   15590 O O   . ILE D  1 358 ? -69.124  -3.024  -0.764   1.00 38.09  ? 358 ILE D O   1 
ATOM   15591 C CB  . ILE D  1 358 ? -68.133  -1.220  1.360    1.00 34.39  ? 358 ILE D CB  1 
ATOM   15592 C CG1 . ILE D  1 358 ? -66.955  -0.624  0.616    1.00 34.89  ? 358 ILE D CG1 1 
ATOM   15593 C CG2 . ILE D  1 358 ? -68.280  -0.699  2.788    1.00 34.54  ? 358 ILE D CG2 1 
ATOM   15594 C CD1 . ILE D  1 358 ? -67.090  0.867   0.337    1.00 35.88  ? 358 ILE D CD1 1 
ATOM   15595 N N   . TYR D  1 359 ? -67.129  -4.006  -0.500   1.00 35.99  ? 359 TYR D N   1 
ATOM   15596 C CA  . TYR D  1 359 ? -67.168  -4.634  -1.801   1.00 35.44  ? 359 TYR D CA  1 
ATOM   15597 C C   . TYR D  1 359 ? -66.179  -5.796  -1.824   1.00 36.57  ? 359 TYR D C   1 
ATOM   15598 O O   . TYR D  1 359 ? -65.083  -5.707  -1.275   1.00 35.22  ? 359 TYR D O   1 
ATOM   15599 C CB  . TYR D  1 359 ? -66.881  -3.605  -2.890   1.00 35.09  ? 359 TYR D CB  1 
ATOM   15600 C CG  . TYR D  1 359 ? -66.810  -4.212  -4.280   1.00 36.19  ? 359 TYR D CG  1 
ATOM   15601 C CD1 . TYR D  1 359 ? -67.960  -4.405  -5.028   1.00 39.09  ? 359 TYR D CD1 1 
ATOM   15602 C CD2 . TYR D  1 359 ? -65.603  -4.600  -4.835   1.00 35.69  ? 359 TYR D CD2 1 
ATOM   15603 C CE1 . TYR D  1 359 ? -67.902  -4.996  -6.278   1.00 42.53  ? 359 TYR D CE1 1 
ATOM   15604 C CE2 . TYR D  1 359 ? -65.526  -5.150  -6.100   1.00 36.55  ? 359 TYR D CE2 1 
ATOM   15605 C CZ  . TYR D  1 359 ? -66.680  -5.362  -6.819   1.00 40.48  ? 359 TYR D CZ  1 
ATOM   15606 O OH  . TYR D  1 359 ? -66.638  -5.949  -8.047   1.00 43.15  ? 359 TYR D OH  1 
ATOM   15607 N N   . SER D  1 360 ? -66.608  -6.869  -2.492   1.00 38.75  ? 360 SER D N   1 
ATOM   15608 C CA  . SER D  1 360 ? -65.863  -8.106  -2.616   1.00 39.68  ? 360 SER D CA  1 
ATOM   15609 C C   . SER D  1 360 ? -66.219  -8.767  -3.944   1.00 41.19  ? 360 SER D C   1 
ATOM   15610 O O   . SER D  1 360 ? -67.401  -8.892  -4.283   1.00 40.94  ? 360 SER D O   1 
ATOM   15611 C CB  . SER D  1 360 ? -66.189  -9.024  -1.493   1.00 39.80  ? 360 SER D CB  1 
ATOM   15612 O OG  . SER D  1 360 ? -65.076  -9.858  -1.292   1.00 39.96  ? 360 SER D OG  1 
ATOM   15613 N N   . LYS D  1 361 ? -65.199  -9.232  -4.663   1.00 40.35  ? 361 LYS D N   1 
ATOM   15614 C CA  . LYS D  1 361 ? -65.442  -10.014 -5.858   1.00 40.67  ? 361 LYS D CA  1 
ATOM   15615 C C   . LYS D  1 361 ? -64.286  -10.974 -6.090   1.00 39.32  ? 361 LYS D C   1 
ATOM   15616 O O   . LYS D  1 361 ? -63.116  -10.582 -6.032   1.00 33.93  ? 361 LYS D O   1 
ATOM   15617 C CB  . LYS D  1 361 ? -65.626  -9.125  -7.093   1.00 44.02  ? 361 LYS D CB  1 
ATOM   15618 C CG  . LYS D  1 361 ? -66.133  -9.893  -8.319   1.00 50.64  ? 361 LYS D CG  1 
ATOM   15619 C CD  . LYS D  1 361 ? -66.865  -9.062  -9.371   1.00 58.49  ? 361 LYS D CD  1 
ATOM   15620 C CE  . LYS D  1 361 ? -67.305  -9.756  -10.645  1.00 61.59  ? 361 LYS D CE  1 
ATOM   15621 N NZ  . LYS D  1 361 ? -68.221  -8.861  -11.371  1.00 66.13  ? 361 LYS D NZ  1 
ATOM   15622 N N   . ASN D  1 362 ? -64.653  -12.240 -6.369   1.00 40.18  ? 362 ASN D N   1 
ATOM   15623 C CA  . ASN D  1 362 ? -63.749  -13.209 -6.965   1.00 39.52  ? 362 ASN D CA  1 
ATOM   15624 C C   . ASN D  1 362 ? -63.558  -12.860 -8.439   1.00 38.64  ? 362 ASN D C   1 
ATOM   15625 O O   . ASN D  1 362 ? -64.519  -12.634 -9.159   1.00 37.95  ? 362 ASN D O   1 
ATOM   15626 C CB  . ASN D  1 362 ? -64.253  -14.636 -6.803   1.00 42.36  ? 362 ASN D CB  1 
ATOM   15627 C CG  . ASN D  1 362 ? -64.469  -14.972 -5.352   1.00 44.56  ? 362 ASN D CG  1 
ATOM   15628 O OD1 . ASN D  1 362 ? -65.547  -15.439 -4.981   1.00 49.93  ? 362 ASN D OD1 1 
ATOM   15629 N ND2 . ASN D  1 362 ? -63.495  -14.687 -4.506   1.00 47.18  ? 362 ASN D ND2 1 
ATOM   15630 N N   . ILE D  1 363 ? -62.300  -12.766 -8.876   1.00 38.48  ? 363 ILE D N   1 
ATOM   15631 C CA  . ILE D  1 363 ? -62.001  -12.523 -10.279  1.00 38.53  ? 363 ILE D CA  1 
ATOM   15632 C C   . ILE D  1 363 ? -61.943  -13.864 -11.030  1.00 39.17  ? 363 ILE D C   1 
ATOM   15633 O O   . ILE D  1 363 ? -61.174  -14.750 -10.688  1.00 39.50  ? 363 ILE D O   1 
ATOM   15634 C CB  . ILE D  1 363 ? -60.696  -11.724 -10.389  1.00 36.70  ? 363 ILE D CB  1 
ATOM   15635 C CG1 . ILE D  1 363 ? -60.707  -10.452 -9.539   1.00 37.05  ? 363 ILE D CG1 1 
ATOM   15636 C CG2 . ILE D  1 363 ? -60.348  -11.444 -11.840  1.00 36.92  ? 363 ILE D CG2 1 
ATOM   15637 C CD1 . ILE D  1 363 ? -61.947  -9.584  -9.703   1.00 39.48  ? 363 ILE D CD1 1 
ATOM   15638 N N   . THR D  1 364 ? -62.805  -14.004 -12.047  1.00 43.38  ? 364 THR D N   1 
ATOM   15639 C CA  . THR D  1 364 ? -62.998  -15.232 -12.818  1.00 45.02  ? 364 THR D CA  1 
ATOM   15640 C C   . THR D  1 364 ? -62.224  -15.137 -14.132  1.00 44.25  ? 364 THR D C   1 
ATOM   15641 O O   . THR D  1 364 ? -62.029  -16.142 -14.808  1.00 47.70  ? 364 THR D O   1 
ATOM   15642 C CB  . THR D  1 364 ? -64.491  -15.443 -13.109  1.00 44.04  ? 364 THR D CB  1 
ATOM   15643 O OG1 . THR D  1 364 ? -64.865  -14.277 -13.826  1.00 46.66  ? 364 THR D OG1 1 
ATOM   15644 C CG2 . THR D  1 364 ? -65.358  -15.509 -11.867  1.00 44.87  ? 364 THR D CG2 1 
ATOM   15645 N N   . SER D  1 365 ? -61.804  -13.914 -14.478  1.00 42.30  ? 365 SER D N   1 
ATOM   15646 C CA  . SER D  1 365 ? -61.239  -13.613 -15.779  1.00 41.94  ? 365 SER D CA  1 
ATOM   15647 C C   . SER D  1 365 ? -60.230  -12.460 -15.635  1.00 39.38  ? 365 SER D C   1 
ATOM   15648 O O   . SER D  1 365 ? -60.472  -11.495 -14.932  1.00 36.52  ? 365 SER D O   1 
ATOM   15649 C CB  . SER D  1 365 ? -62.396  -13.310 -16.696  1.00 43.85  ? 365 SER D CB  1 
ATOM   15650 O OG  . SER D  1 365 ? -61.949  -12.946 -17.983  1.00 46.67  ? 365 SER D OG  1 
ATOM   15651 N N   . GLU D  1 366 ? -59.051  -12.556 -16.246  1.00 38.65  ? 366 GLU D N   1 
ATOM   15652 C CA  . GLU D  1 366 ? -58.098  -11.460 -16.173  1.00 37.60  ? 366 GLU D CA  1 
ATOM   15653 C C   . GLU D  1 366 ? -58.501  -10.312 -17.102  1.00 33.81  ? 366 GLU D C   1 
ATOM   15654 O O   . GLU D  1 366 ? -59.340  -10.453 -17.970  1.00 32.66  ? 366 GLU D O   1 
ATOM   15655 C CB  . GLU D  1 366 ? -56.723  -11.977 -16.570  1.00 39.88  ? 366 GLU D CB  1 
ATOM   15656 C CG  . GLU D  1 366 ? -56.558  -12.206 -18.070  1.00 43.32  ? 366 GLU D CG  1 
ATOM   15657 C CD  . GLU D  1 366 ? -55.112  -12.556 -18.397  1.00 48.25  ? 366 GLU D CD  1 
ATOM   15658 O OE1 . GLU D  1 366 ? -54.208  -11.730 -18.157  1.00 49.50  ? 366 GLU D OE1 1 
ATOM   15659 O OE2 . GLU D  1 366 ? -54.891  -13.691 -18.865  1.00 55.61  ? 366 GLU D OE2 1 
ATOM   15660 N N   . GLY D  1 367 ? -57.855  -9.172  -16.953  1.00 32.25  ? 367 GLY D N   1 
ATOM   15661 C CA  . GLY D  1 367 ? -58.143  -8.018  -17.793  1.00 32.61  ? 367 GLY D CA  1 
ATOM   15662 C C   . GLY D  1 367 ? -59.227  -7.117  -17.192  1.00 32.64  ? 367 GLY D C   1 
ATOM   15663 O O   . GLY D  1 367 ? -59.289  -6.927  -15.990  1.00 33.13  ? 367 GLY D O   1 
ATOM   15664 N N   . TYR D  1 368 ? -60.063  -6.524  -18.045  1.00 33.35  ? 368 TYR D N   1 
ATOM   15665 C CA  . TYR D  1 368 ? -60.947  -5.449  -17.625  1.00 33.96  ? 368 TYR D CA  1 
ATOM   15666 C C   . TYR D  1 368 ? -62.132  -6.039  -16.881  1.00 36.63  ? 368 TYR D C   1 
ATOM   15667 O O   . TYR D  1 368 ? -62.640  -7.069  -17.321  1.00 37.20  ? 368 TYR D O   1 
ATOM   15668 C CB  . TYR D  1 368 ? -61.502  -4.704  -18.840  1.00 33.32  ? 368 TYR D CB  1 
ATOM   15669 C CG  . TYR D  1 368 ? -62.474  -3.585  -18.506  1.00 33.27  ? 368 TYR D CG  1 
ATOM   15670 C CD1 . TYR D  1 368 ? -62.050  -2.288  -18.214  1.00 33.43  ? 368 TYR D CD1 1 
ATOM   15671 C CD2 . TYR D  1 368 ? -63.830  -3.815  -18.517  1.00 34.66  ? 368 TYR D CD2 1 
ATOM   15672 C CE1 . TYR D  1 368 ? -62.959  -1.273  -17.934  1.00 33.05  ? 368 TYR D CE1 1 
ATOM   15673 C CE2 . TYR D  1 368 ? -64.747  -2.810  -18.244  1.00 33.90  ? 368 TYR D CE2 1 
ATOM   15674 C CZ  . TYR D  1 368 ? -64.316  -1.540  -17.939  1.00 32.76  ? 368 TYR D CZ  1 
ATOM   15675 O OH  . TYR D  1 368 ? -65.275  -0.609  -17.662  1.00 31.20  ? 368 TYR D OH  1 
ATOM   15676 N N   . MET D  1 369 ? -62.563  -5.371  -15.801  1.00 37.29  ? 369 MET D N   1 
ATOM   15677 C CA  . MET D  1 369 ? -63.879  -5.626  -15.255  1.00 42.26  ? 369 MET D CA  1 
ATOM   15678 C C   . MET D  1 369 ? -64.504  -4.348  -14.701  1.00 41.18  ? 369 MET D C   1 
ATOM   15679 O O   . MET D  1 369 ? -63.814  -3.542  -14.073  1.00 39.05  ? 369 MET D O   1 
ATOM   15680 C CB  . MET D  1 369 ? -63.844  -6.709  -14.170  1.00 49.62  ? 369 MET D CB  1 
ATOM   15681 C CG  . MET D  1 369 ? -63.122  -6.288  -12.893  1.00 55.67  ? 369 MET D CG  1 
ATOM   15682 S SD  . MET D  1 369 ? -64.071  -6.657  -11.401  1.00 66.53  ? 369 MET D SD  1 
ATOM   15683 C CE  . MET D  1 369 ? -65.713  -6.024  -11.789  1.00 53.13  ? 369 MET D CE  1 
ATOM   15684 N N   . ALA D  1 370 ? -65.834  -4.228  -14.882  1.00 41.37  ? 370 ALA D N   1 
ATOM   15685 C CA  . ALA D  1 370 ? -66.615  -3.076  -14.444  1.00 41.16  ? 370 ALA D CA  1 
ATOM   15686 C C   . ALA D  1 370 ? -67.681  -3.503  -13.441  1.00 41.29  ? 370 ALA D C   1 
ATOM   15687 O O   . ALA D  1 370 ? -68.242  -4.579  -13.580  1.00 45.39  ? 370 ALA D O   1 
ATOM   15688 C CB  . ALA D  1 370 ? -67.253  -2.423  -15.647  1.00 40.49  ? 370 ALA D CB  1 
ATOM   15689 N N   . ASP D  1 371 ? -67.962  -2.664  -12.434  1.00 39.40  ? 371 ASP D N   1 
ATOM   15690 C CA  . ASP D  1 371 ? -68.958  -2.999  -11.427  1.00 38.94  ? 371 ASP D CA  1 
ATOM   15691 C C   . ASP D  1 371 ? -69.326  -1.716  -10.681  1.00 37.22  ? 371 ASP D C   1 
ATOM   15692 O O   . ASP D  1 371 ? -69.119  -0.634  -11.209  1.00 35.38  ? 371 ASP D O   1 
ATOM   15693 C CB  . ASP D  1 371 ? -68.447  -4.168  -10.599  1.00 38.42  ? 371 ASP D CB  1 
ATOM   15694 C CG  . ASP D  1 371 ? -69.434  -5.036  -9.842   1.00 38.20  ? 371 ASP D CG  1 
ATOM   15695 O OD1 . ASP D  1 371 ? -70.642  -4.734  -9.835   1.00 38.58  ? 371 ASP D OD1 1 
ATOM   15696 O OD2 . ASP D  1 371 ? -68.959  -6.025  -9.247   1.00 41.48  ? 371 ASP D OD2 1 
ATOM   15697 N N   . GLU D  1 372 ? -69.958  -1.839  -9.504   1.00 40.54  ? 372 GLU D N   1 
ATOM   15698 C CA  . GLU D  1 372 ? -70.338  -0.690  -8.693   1.00 43.14  ? 372 GLU D CA  1 
ATOM   15699 C C   . GLU D  1 372 ? -70.182  -0.975  -7.205   1.00 41.35  ? 372 GLU D C   1 
ATOM   15700 O O   . GLU D  1 372 ? -70.566  -2.031  -6.748   1.00 41.41  ? 372 GLU D O   1 
ATOM   15701 C CB  . GLU D  1 372 ? -71.802  -0.283  -8.782   1.00 45.65  ? 372 GLU D CB  1 
ATOM   15702 C CG  . GLU D  1 372 ? -72.253  0.082   -10.184  1.00 49.88  ? 372 GLU D CG  1 
ATOM   15703 C CD  . GLU D  1 372 ? -73.722  0.429   -10.088  1.00 58.07  ? 372 GLU D CD  1 
ATOM   15704 O OE1 . GLU D  1 372 ? -74.539  -0.364  -9.551   1.00 58.23  ? 372 GLU D OE1 1 
ATOM   15705 O OE2 . GLU D  1 372 ? -74.031  1.547   -10.530  1.00 68.46  ? 372 GLU D OE2 1 
ATOM   15706 N N   . LEU D  1 373 ? -69.642  0.015   -6.489   1.00 43.75  ? 373 LEU D N   1 
ATOM   15707 C CA  . LEU D  1 373 ? -69.655  0.106   -5.038   1.00 44.11  ? 373 LEU D CA  1 
ATOM   15708 C C   . LEU D  1 373 ? -70.891  0.894   -4.665   1.00 39.77  ? 373 LEU D C   1 
ATOM   15709 O O   . LEU D  1 373 ? -71.168  1.880   -5.324   1.00 41.36  ? 373 LEU D O   1 
ATOM   15710 C CB  . LEU D  1 373 ? -68.502  0.939   -4.454   1.00 44.94  ? 373 LEU D CB  1 
ATOM   15711 C CG  . LEU D  1 373 ? -67.090  0.585   -4.878   1.00 47.20  ? 373 LEU D CG  1 
ATOM   15712 C CD1 . LEU D  1 373 ? -66.165  1.671   -4.384   1.00 49.08  ? 373 LEU D CD1 1 
ATOM   15713 C CD2 . LEU D  1 373 ? -66.750  -0.771  -4.320   1.00 47.87  ? 373 LEU D CD2 1 
ATOM   15714 N N   . THR D  1 374 ? -71.454  0.546   -3.520   1.00 37.86  ? 374 THR D N   1 
ATOM   15715 C CA  . THR D  1 374 ? -72.360  1.379   -2.765   1.00 38.62  ? 374 THR D CA  1 
ATOM   15716 C C   . THR D  1 374 ? -71.633  1.877   -1.517   1.00 38.06  ? 374 THR D C   1 
ATOM   15717 O O   . THR D  1 374 ? -71.023  1.098   -0.788   1.00 40.78  ? 374 THR D O   1 
ATOM   15718 C CB  . THR D  1 374 ? -73.595  0.548   -2.408   1.00 39.75  ? 374 THR D CB  1 
ATOM   15719 O OG1 . THR D  1 374 ? -74.170  0.204   -3.669   1.00 39.95  ? 374 THR D OG1 1 
ATOM   15720 C CG2 . THR D  1 374 ? -74.579  1.324   -1.555   1.00 39.67  ? 374 THR D CG2 1 
ATOM   15721 N N   . ILE D  1 375 ? -71.723  3.183   -1.270   1.00 36.47  ? 375 ILE D N   1 
ATOM   15722 C CA  . ILE D  1 375 ? -71.183  3.821   -0.084   1.00 35.57  ? 375 ILE D CA  1 
ATOM   15723 C C   . ILE D  1 375 ? -72.307  4.539   0.667    1.00 37.06  ? 375 ILE D C   1 
ATOM   15724 O O   . ILE D  1 375 ? -73.405  4.782   0.133    1.00 36.14  ? 375 ILE D O   1 
ATOM   15725 C CB  . ILE D  1 375 ? -70.082  4.805   -0.499   1.00 35.23  ? 375 ILE D CB  1 
ATOM   15726 C CG1 . ILE D  1 375 ? -70.653  5.894   -1.438   1.00 35.04  ? 375 ILE D CG1 1 
ATOM   15727 C CG2 . ILE D  1 375 ? -68.884  4.071   -1.117   1.00 35.23  ? 375 ILE D CG2 1 
ATOM   15728 C CD1 . ILE D  1 375 ? -69.736  7.086   -1.691   1.00 34.13  ? 375 ILE D CD1 1 
ATOM   15729 N N   . ASP D  1 376 ? -72.008  4.894   1.923    1.00 38.68  ? 376 ASP D N   1 
ATOM   15730 C CA  . ASP D  1 376 ? -72.997  5.499   2.801    1.00 40.38  ? 376 ASP D CA  1 
ATOM   15731 C C   . ASP D  1 376 ? -72.421  6.757   3.444    1.00 38.86  ? 376 ASP D C   1 
ATOM   15732 O O   . ASP D  1 376 ? -72.322  6.824   4.655    1.00 40.08  ? 376 ASP D O   1 
ATOM   15733 C CB  . ASP D  1 376 ? -73.498  4.494   3.828    1.00 42.48  ? 376 ASP D CB  1 
ATOM   15734 C CG  . ASP D  1 376 ? -74.848  4.817   4.453    1.00 47.29  ? 376 ASP D CG  1 
ATOM   15735 O OD1 . ASP D  1 376 ? -75.564  5.710   3.930    1.00 53.48  ? 376 ASP D OD1 1 
ATOM   15736 O OD2 . ASP D  1 376 ? -75.192  4.179   5.471    1.00 50.99  ? 376 ASP D OD2 1 
ATOM   15737 N N   . PRO D  1 377 ? -72.041  7.801   2.676    1.00 38.20  ? 377 PRO D N   1 
ATOM   15738 C CA  . PRO D  1 377 ? -71.550  9.057   3.245    1.00 37.43  ? 377 PRO D CA  1 
ATOM   15739 C C   . PRO D  1 377 ? -72.564  9.750   4.138    1.00 38.27  ? 377 PRO D C   1 
ATOM   15740 O O   . PRO D  1 377 ? -73.718  9.885   3.762    1.00 38.75  ? 377 PRO D O   1 
ATOM   15741 C CB  . PRO D  1 377 ? -71.263  9.898   1.990    1.00 37.52  ? 377 PRO D CB  1 
ATOM   15742 C CG  . PRO D  1 377 ? -72.228  9.360   0.974    1.00 37.97  ? 377 PRO D CG  1 
ATOM   15743 C CD  . PRO D  1 377 ? -72.100  7.860   1.209    1.00 38.53  ? 377 PRO D CD  1 
ATOM   15744 N N   . VAL D  1 378 ? -72.118  10.149  5.333    1.00 38.94  ? 378 VAL D N   1 
ATOM   15745 C CA  . VAL D  1 378 ? -72.875  11.055  6.179    1.00 39.66  ? 378 VAL D CA  1 
ATOM   15746 C C   . VAL D  1 378 ? -72.548  12.464  5.698    1.00 39.83  ? 378 VAL D C   1 
ATOM   15747 O O   . VAL D  1 378 ? -71.383  12.855  5.692    1.00 39.90  ? 378 VAL D O   1 
ATOM   15748 C CB  . VAL D  1 378 ? -72.553  10.905  7.680    1.00 40.25  ? 378 VAL D CB  1 
ATOM   15749 C CG1 . VAL D  1 378 ? -73.391  11.848  8.547    1.00 40.14  ? 378 VAL D CG1 1 
ATOM   15750 C CG2 . VAL D  1 378 ? -72.697  9.453   8.149    1.00 39.70  ? 378 VAL D CG2 1 
ATOM   15751 N N   . GLY D  1 379 ? -73.588  13.193  5.297    1.00 40.63  ? 379 GLY D N   1 
ATOM   15752 C CA  . GLY D  1 379 ? -73.463  14.531  4.751    1.00 40.32  ? 379 GLY D CA  1 
ATOM   15753 C C   . GLY D  1 379 ? -72.455  14.548  3.611    1.00 38.65  ? 379 GLY D C   1 
ATOM   15754 O O   . GLY D  1 379 ? -72.609  13.819  2.640    1.00 39.61  ? 379 GLY D O   1 
ATOM   15755 N N   . ILE D  1 380 ? -71.471  15.434  3.749    1.00 35.95  ? 380 ILE D N   1 
ATOM   15756 C CA  . ILE D  1 380 ? -70.328  15.477  2.875    1.00 34.79  ? 380 ILE D CA  1 
ATOM   15757 C C   . ILE D  1 380 ? -69.215  14.761  3.629    1.00 33.93  ? 380 ILE D C   1 
ATOM   15758 O O   . ILE D  1 380 ? -68.908  15.144  4.762    1.00 33.71  ? 380 ILE D O   1 
ATOM   15759 C CB  . ILE D  1 380 ? -69.914  16.924  2.548    1.00 33.58  ? 380 ILE D CB  1 
ATOM   15760 C CG1 . ILE D  1 380 ? -71.050  17.741  1.948    1.00 34.45  ? 380 ILE D CG1 1 
ATOM   15761 C CG2 . ILE D  1 380 ? -68.659  16.919  1.671    1.00 32.35  ? 380 ILE D CG2 1 
ATOM   15762 C CD1 . ILE D  1 380 ? -70.730  19.228  1.766    1.00 33.92  ? 380 ILE D CD1 1 
ATOM   15763 N N   . GLU D  1 381 ? -68.614  13.747  2.989    1.00 33.94  ? 381 GLU D N   1 
ATOM   15764 C CA  . GLU D  1 381 ? -67.701  12.853  3.680    1.00 33.21  ? 381 GLU D CA  1 
ATOM   15765 C C   . GLU D  1 381 ? -66.515  12.485  2.798    1.00 31.45  ? 381 GLU D C   1 
ATOM   15766 O O   . GLU D  1 381 ? -66.642  11.981  1.691    1.00 29.72  ? 381 GLU D O   1 
ATOM   15767 C CB  . GLU D  1 381 ? -68.487  11.642  4.149    1.00 34.99  ? 381 GLU D CB  1 
ATOM   15768 C CG  . GLU D  1 381 ? -67.717  10.814  5.173    1.00 37.11  ? 381 GLU D CG  1 
ATOM   15769 C CD  . GLU D  1 381 ? -68.433  9.544   5.621    1.00 36.92  ? 381 GLU D CD  1 
ATOM   15770 O OE1 . GLU D  1 381 ? -69.558  9.619   6.084    1.00 37.31  ? 381 GLU D OE1 1 
ATOM   15771 O OE2 . GLU D  1 381 ? -67.850  8.469   5.497    1.00 39.48  ? 381 GLU D OE2 1 
ATOM   15772 N N   . ASP D  1 382 ? -65.332  12.786  3.326    1.00 31.51  ? 382 ASP D N   1 
ATOM   15773 C CA  . ASP D  1 382 ? -64.092  12.287  2.768    1.00 30.72  ? 382 ASP D CA  1 
ATOM   15774 C C   . ASP D  1 382 ? -63.911  10.827  3.184    1.00 29.79  ? 382 ASP D C   1 
ATOM   15775 O O   . ASP D  1 382 ? -64.058  10.515  4.373    1.00 29.11  ? 382 ASP D O   1 
ATOM   15776 C CB  . ASP D  1 382 ? -62.937  13.135  3.267    1.00 30.67  ? 382 ASP D CB  1 
ATOM   15777 C CG  . ASP D  1 382 ? -62.802  13.184  4.780    1.00 31.43  ? 382 ASP D CG  1 
ATOM   15778 O OD1 . ASP D  1 382 ? -63.787  13.611  5.447    1.00 29.68  ? 382 ASP D OD1 1 
ATOM   15779 O OD2 . ASP D  1 382 ? -61.699  12.788  5.255    1.00 31.58  ? 382 ASP D OD2 1 
ATOM   15780 N N   . MET D  1 383 ? -63.652  9.972   2.181    1.00 28.46  ? 383 MET D N   1 
ATOM   15781 C CA  . MET D  1 383 ? -63.505  8.529   2.372    1.00 29.74  ? 383 MET D CA  1 
ATOM   15782 C C   . MET D  1 383 ? -62.227  8.032   1.690    1.00 27.32  ? 383 MET D C   1 
ATOM   15783 O O   . MET D  1 383 ? -62.001  8.336   0.513    1.00 24.69  ? 383 MET D O   1 
ATOM   15784 C CB  . MET D  1 383 ? -64.682  7.752   1.773    1.00 29.70  ? 383 MET D CB  1 
ATOM   15785 C CG  . MET D  1 383 ? -65.980  8.377   2.113    1.00 31.57  ? 383 MET D CG  1 
ATOM   15786 S SD  . MET D  1 383 ? -67.442  7.521   1.510    1.00 32.44  ? 383 MET D SD  1 
ATOM   15787 C CE  . MET D  1 383 ? -67.373  5.969   2.419    1.00 32.80  ? 383 MET D CE  1 
ATOM   15788 N N   . GLU D  1 384 ? -61.401  7.314   2.465    1.00 27.98  ? 384 GLU D N   1 
ATOM   15789 C CA  . GLU D  1 384 ? -60.244  6.587   1.952    1.00 28.86  ? 384 GLU D CA  1 
ATOM   15790 C C   . GLU D  1 384 ? -60.674  5.139   1.732    1.00 29.32  ? 384 GLU D C   1 
ATOM   15791 O O   . GLU D  1 384 ? -60.887  4.406   2.702    1.00 30.02  ? 384 GLU D O   1 
ATOM   15792 C CB  . GLU D  1 384 ? -59.036  6.639   2.891    1.00 30.35  ? 384 GLU D CB  1 
ATOM   15793 C CG  . GLU D  1 384 ? -57.801  5.963   2.289    1.00 30.71  ? 384 GLU D CG  1 
ATOM   15794 C CD  . GLU D  1 384 ? -56.522  5.976   3.111    1.00 29.87  ? 384 GLU D CD  1 
ATOM   15795 O OE1 . GLU D  1 384 ? -56.649  6.246   4.322    1.00 27.30  ? 384 GLU D OE1 1 
ATOM   15796 O OE2 . GLU D  1 384 ? -55.406  5.744   2.508    1.00 29.82  ? 384 GLU D OE2 1 
ATOM   15797 N N   . LEU D  1 385 ? -60.951  4.804   0.460    1.00 30.03  ? 385 LEU D N   1 
ATOM   15798 C CA  . LEU D  1 385 ? -61.376  3.465   0.034    1.00 30.65  ? 385 LEU D CA  1 
ATOM   15799 C C   . LEU D  1 385 ? -60.136  2.570   -0.118   1.00 30.02  ? 385 LEU D C   1 
ATOM   15800 O O   . LEU D  1 385 ? -59.245  2.834   -0.934   1.00 29.71  ? 385 LEU D O   1 
ATOM   15801 C CB  . LEU D  1 385 ? -62.125  3.585   -1.290   1.00 30.20  ? 385 LEU D CB  1 
ATOM   15802 C CG  . LEU D  1 385 ? -63.332  4.541   -1.300   1.00 31.82  ? 385 LEU D CG  1 
ATOM   15803 C CD1 . LEU D  1 385 ? -63.962  4.578   -2.684   1.00 32.17  ? 385 LEU D CD1 1 
ATOM   15804 C CD2 . LEU D  1 385 ? -64.375  4.148   -0.268   1.00 32.07  ? 385 LEU D CD2 1 
ATOM   15805 N N   . ALA D  1 386 ? -60.045  1.550   0.723    1.00 29.20  ? 386 ALA D N   1 
ATOM   15806 C CA  . ALA D  1 386 ? -58.857  0.709   0.775    1.00 29.35  ? 386 ALA D CA  1 
ATOM   15807 C C   . ALA D  1 386 ? -59.021  -0.527  -0.121   1.00 28.39  ? 386 ALA D C   1 
ATOM   15808 O O   . ALA D  1 386 ? -59.766  -1.428  0.248    1.00 27.18  ? 386 ALA D O   1 
ATOM   15809 C CB  . ALA D  1 386 ? -58.650  0.310   2.219    1.00 29.84  ? 386 ALA D CB  1 
ATOM   15810 N N   . PHE D  1 387 ? -58.360  -0.541  -1.286   1.00 27.34  ? 387 PHE D N   1 
ATOM   15811 C CA  . PHE D  1 387 ? -58.413  -1.676  -2.205   1.00 26.93  ? 387 PHE D CA  1 
ATOM   15812 C C   . PHE D  1 387 ? -57.358  -2.696  -1.796   1.00 28.12  ? 387 PHE D C   1 
ATOM   15813 O O   . PHE D  1 387 ? -56.239  -2.352  -1.391   1.00 28.32  ? 387 PHE D O   1 
ATOM   15814 C CB  . PHE D  1 387 ? -58.251  -1.304  -3.682   1.00 26.54  ? 387 PHE D CB  1 
ATOM   15815 C CG  . PHE D  1 387 ? -59.446  -0.559  -4.294   1.00 28.27  ? 387 PHE D CG  1 
ATOM   15816 C CD1 . PHE D  1 387 ? -59.809  0.712   -3.854   1.00 25.87  ? 387 PHE D CD1 1 
ATOM   15817 C CD2 . PHE D  1 387 ? -60.224  -1.146  -5.302   1.00 29.03  ? 387 PHE D CD2 1 
ATOM   15818 C CE1 . PHE D  1 387 ? -60.928  1.340   -4.366   1.00 27.53  ? 387 PHE D CE1 1 
ATOM   15819 C CE2 . PHE D  1 387 ? -61.331  -0.492  -5.828   1.00 28.57  ? 387 PHE D CE2 1 
ATOM   15820 C CZ  . PHE D  1 387 ? -61.697  0.742   -5.351   1.00 28.08  ? 387 PHE D CZ  1 
ATOM   15821 N N   . GLU D  1 388 ? -57.758  -3.964  -1.885   1.00 29.47  ? 388 GLU D N   1 
ATOM   15822 C CA  . GLU D  1 388 ? -56.881  -5.092  -1.640   1.00 30.50  ? 388 GLU D CA  1 
ATOM   15823 C C   . GLU D  1 388 ? -57.033  -6.093  -2.780   1.00 31.08  ? 388 GLU D C   1 
ATOM   15824 O O   . GLU D  1 388 ? -58.164  -6.470  -3.139   1.00 32.29  ? 388 GLU D O   1 
ATOM   15825 C CB  . GLU D  1 388 ? -57.267  -5.848  -0.374   1.00 31.48  ? 388 GLU D CB  1 
ATOM   15826 C CG  . GLU D  1 388 ? -56.971  -5.090  0.916    1.00 31.92  ? 388 GLU D CG  1 
ATOM   15827 C CD  . GLU D  1 388 ? -57.701  -5.703  2.100    1.00 33.37  ? 388 GLU D CD  1 
ATOM   15828 O OE1 . GLU D  1 388 ? -58.547  -6.613  1.925    1.00 32.60  ? 388 GLU D OE1 1 
ATOM   15829 O OE2 . GLU D  1 388 ? -57.446  -5.218  3.220    1.00 35.41  ? 388 GLU D OE2 1 
ATOM   15830 N N   . PHE D  1 389 ? -55.872  -6.527  -3.286   1.00 29.21  ? 389 PHE D N   1 
ATOM   15831 C CA  . PHE D  1 389 ? -55.758  -7.498  -4.345   1.00 30.10  ? 389 PHE D CA  1 
ATOM   15832 C C   . PHE D  1 389 ? -55.088  -8.759  -3.783   1.00 32.94  ? 389 PHE D C   1 
ATOM   15833 O O   . PHE D  1 389 ? -54.011  -8.666  -3.181   1.00 31.75  ? 389 PHE D O   1 
ATOM   15834 C CB  . PHE D  1 389 ? -54.948  -6.876  -5.480   1.00 28.19  ? 389 PHE D CB  1 
ATOM   15835 C CG  . PHE D  1 389 ? -55.549  -5.644  -6.136   1.00 27.00  ? 389 PHE D CG  1 
ATOM   15836 C CD1 . PHE D  1 389 ? -56.421  -5.761  -7.218   1.00 27.10  ? 389 PHE D CD1 1 
ATOM   15837 C CD2 . PHE D  1 389 ? -55.189  -4.375  -5.707   1.00 26.36  ? 389 PHE D CD2 1 
ATOM   15838 C CE1 . PHE D  1 389 ? -56.966  -4.647  -7.822   1.00 26.86  ? 389 PHE D CE1 1 
ATOM   15839 C CE2 . PHE D  1 389 ? -55.767  -3.263  -6.280   1.00 25.96  ? 389 PHE D CE2 1 
ATOM   15840 C CZ  . PHE D  1 389 ? -56.637  -3.391  -7.346   1.00 26.79  ? 389 PHE D CZ  1 
ATOM   15841 N N   . TYR D  1 390 ? -55.723  -9.917  -4.050   1.00 32.64  ? 390 TYR D N   1 
ATOM   15842 C CA  . TYR D  1 390 ? -55.349  -11.216 -3.511   1.00 35.03  ? 390 TYR D CA  1 
ATOM   15843 C C   . TYR D  1 390 ? -55.030  -12.212 -4.632   1.00 35.70  ? 390 TYR D C   1 
ATOM   15844 O O   . TYR D  1 390 ? -55.654  -12.197 -5.698   1.00 34.89  ? 390 TYR D O   1 
ATOM   15845 C CB  . TYR D  1 390 ? -56.476  -11.883 -2.715   1.00 35.88  ? 390 TYR D CB  1 
ATOM   15846 C CG  . TYR D  1 390 ? -56.902  -11.158 -1.446   1.00 38.73  ? 390 TYR D CG  1 
ATOM   15847 C CD1 . TYR D  1 390 ? -57.600  -9.942  -1.494   1.00 38.69  ? 390 TYR D CD1 1 
ATOM   15848 C CD2 . TYR D  1 390 ? -56.618  -11.683 -0.189   1.00 40.45  ? 390 TYR D CD2 1 
ATOM   15849 C CE1 . TYR D  1 390 ? -57.995  -9.285  -0.339   1.00 36.79  ? 390 TYR D CE1 1 
ATOM   15850 C CE2 . TYR D  1 390 ? -57.007  -11.027 0.975    1.00 40.77  ? 390 TYR D CE2 1 
ATOM   15851 C CZ  . TYR D  1 390 ? -57.693  -9.823  0.902    1.00 38.24  ? 390 TYR D CZ  1 
ATOM   15852 O OH  . TYR D  1 390 ? -58.067  -9.195  2.059    1.00 37.62  ? 390 TYR D OH  1 
ATOM   15853 N N   . ASP D  1 391 ? -54.104  -13.141 -4.321   1.00 34.90  ? 391 ASP D N   1 
ATOM   15854 C CA  . ASP D  1 391 ? -53.639  -14.164 -5.251   1.00 34.20  ? 391 ASP D CA  1 
ATOM   15855 C C   . ASP D  1 391 ? -54.408  -15.460 -4.999   1.00 35.38  ? 391 ASP D C   1 
ATOM   15856 O O   . ASP D  1 391 ? -55.366  -15.472 -4.243   1.00 33.17  ? 391 ASP D O   1 
ATOM   15857 C CB  . ASP D  1 391 ? -52.125  -14.316 -5.171   1.00 33.94  ? 391 ASP D CB  1 
ATOM   15858 C CG  . ASP D  1 391 ? -51.552  -14.951 -3.909   1.00 35.49  ? 391 ASP D CG  1 
ATOM   15859 O OD1 . ASP D  1 391 ? -52.344  -15.482 -3.089   1.00 35.13  ? 391 ASP D OD1 1 
ATOM   15860 O OD2 . ASP D  1 391 ? -50.302  -14.910 -3.757   1.00 38.37  ? 391 ASP D OD2 1 
ATOM   15861 N N   . SER D  1 392 ? -53.981  -16.557 -5.635   1.00 37.72  ? 392 SER D N   1 
ATOM   15862 C CA  . SER D  1 392 ? -54.759  -17.785 -5.576   1.00 42.23  ? 392 SER D CA  1 
ATOM   15863 C C   . SER D  1 392 ? -54.565  -18.489 -4.230   1.00 43.13  ? 392 SER D C   1 
ATOM   15864 O O   . SER D  1 392 ? -55.353  -19.356 -3.920   1.00 42.92  ? 392 SER D O   1 
ATOM   15865 C CB  . SER D  1 392 ? -54.476  -18.698 -6.749   1.00 42.69  ? 392 SER D CB  1 
ATOM   15866 O OG  . SER D  1 392 ? -53.080  -18.811 -6.980   1.00 43.07  ? 392 SER D OG  1 
ATOM   15867 N N   . ASP D  1 393 ? -53.610  -18.045 -3.389   1.00 45.38  ? 393 ASP D N   1 
ATOM   15868 C CA  . ASP D  1 393 ? -53.477  -18.526 -2.013   1.00 45.19  ? 393 ASP D CA  1 
ATOM   15869 C C   . ASP D  1 393 ? -54.179  -17.629 -0.993   1.00 42.62  ? 393 ASP D C   1 
ATOM   15870 O O   . ASP D  1 393 ? -53.944  -17.751 0.205    1.00 39.51  ? 393 ASP D O   1 
ATOM   15871 C CB  . ASP D  1 393 ? -52.023  -18.587 -1.583   1.00 49.56  ? 393 ASP D CB  1 
ATOM   15872 C CG  . ASP D  1 393 ? -51.310  -19.879 -1.943   1.00 55.81  ? 393 ASP D CG  1 
ATOM   15873 O OD1 . ASP D  1 393 ? -51.971  -20.974 -1.839   1.00 57.23  ? 393 ASP D OD1 1 
ATOM   15874 O OD2 . ASP D  1 393 ? -50.104  -19.764 -2.299   1.00 55.74  ? 393 ASP D OD2 1 
ATOM   15875 N N   . ASN D  1 394 ? -54.984  -16.677 -1.470   1.00 41.90  ? 394 ASN D N   1 
ATOM   15876 C CA  . ASN D  1 394 ? -55.656  -15.738 -0.598   1.00 42.32  ? 394 ASN D CA  1 
ATOM   15877 C C   . ASN D  1 394 ? -54.666  -14.878 0.203    1.00 41.89  ? 394 ASN D C   1 
ATOM   15878 O O   . ASN D  1 394 ? -54.971  -14.498 1.335    1.00 37.95  ? 394 ASN D O   1 
ATOM   15879 C CB  . ASN D  1 394 ? -56.660  -16.474 0.271    1.00 44.06  ? 394 ASN D CB  1 
ATOM   15880 C CG  . ASN D  1 394 ? -57.753  -15.554 0.765    1.00 47.74  ? 394 ASN D CG  1 
ATOM   15881 O OD1 . ASN D  1 394 ? -58.303  -14.747 -0.002   1.00 45.81  ? 394 ASN D OD1 1 
ATOM   15882 N ND2 . ASN D  1 394 ? -58.097  -15.682 2.037    1.00 49.65  ? 394 ASN D ND2 1 
ATOM   15883 N N   . LYS D  1 395 ? -53.520  -14.518 -0.408   1.00 42.63  ? 395 LYS D N   1 
ATOM   15884 C CA  . LYS D  1 395 ? -52.576  -13.576 0.196    1.00 44.60  ? 395 LYS D CA  1 
ATOM   15885 C C   . LYS D  1 395 ? -52.619  -12.231 -0.526   1.00 40.88  ? 395 LYS D C   1 
ATOM   15886 O O   . LYS D  1 395 ? -52.783  -12.178 -1.740   1.00 39.45  ? 395 LYS D O   1 
ATOM   15887 C CB  . LYS D  1 395 ? -51.127  -14.063 0.189    1.00 48.09  ? 395 LYS D CB  1 
ATOM   15888 C CG  . LYS D  1 395 ? -50.899  -15.264 1.061    1.00 55.75  ? 395 LYS D CG  1 
ATOM   15889 C CD  . LYS D  1 395 ? -49.451  -15.717 0.991    1.00 63.40  ? 395 LYS D CD  1 
ATOM   15890 C CE  . LYS D  1 395 ? -49.267  -16.830 1.971    1.00 68.67  ? 395 LYS D CE  1 
ATOM   15891 N NZ  . LYS D  1 395 ? -47.934  -17.413 1.823    1.00 72.53  ? 395 LYS D NZ  1 
ATOM   15892 N N   . ILE D  1 396 ? -52.467  -11.137 0.231    1.00 39.61  ? 396 ILE D N   1 
ATOM   15893 C CA  . ILE D  1 396 ? -52.558  -9.812  -0.352   1.00 37.68  ? 396 ILE D CA  1 
ATOM   15894 C C   . ILE D  1 396 ? -51.272  -9.555  -1.112   1.00 32.79  ? 396 ILE D C   1 
ATOM   15895 O O   . ILE D  1 396 ? -50.221  -9.673  -0.528   1.00 32.86  ? 396 ILE D O   1 
ATOM   15896 C CB  . ILE D  1 396 ? -52.909  -8.750  0.712    1.00 40.31  ? 396 ILE D CB  1 
ATOM   15897 C CG1 . ILE D  1 396 ? -54.408  -8.931  1.124    1.00 45.10  ? 396 ILE D CG1 1 
ATOM   15898 C CG2 . ILE D  1 396 ? -52.654  -7.331  0.200    1.00 39.80  ? 396 ILE D CG2 1 
ATOM   15899 C CD1 . ILE D  1 396 ? -54.864  -8.198  2.385    1.00 47.08  ? 396 ILE D CD1 1 
ATOM   15900 N N   . ILE D  1 397 ? -51.392  -9.263  -2.413   1.00 31.41  ? 397 ILE D N   1 
ATOM   15901 C CA  . ILE D  1 397 ? -50.259  -8.906  -3.255   1.00 32.21  ? 397 ILE D CA  1 
ATOM   15902 C C   . ILE D  1 397 ? -50.231  -7.410  -3.605   1.00 31.30  ? 397 ILE D C   1 
ATOM   15903 O O   . ILE D  1 397 ? -49.234  -6.937  -4.141   1.00 29.64  ? 397 ILE D O   1 
ATOM   15904 C CB  . ILE D  1 397 ? -50.249  -9.773  -4.518   1.00 33.61  ? 397 ILE D CB  1 
ATOM   15905 C CG1 . ILE D  1 397 ? -51.402  -9.402  -5.453   1.00 35.86  ? 397 ILE D CG1 1 
ATOM   15906 C CG2 . ILE D  1 397 ? -50.228  -11.262 -4.126   1.00 34.06  ? 397 ILE D CG2 1 
ATOM   15907 C CD1 . ILE D  1 397 ? -51.698  -10.426 -6.545   1.00 37.20  ? 397 ILE D CD1 1 
ATOM   15908 N N   . LYS D  1 398 ? -51.298  -6.663  -3.294   1.00 30.21  ? 398 LYS D N   1 
ATOM   15909 C CA  . LYS D  1 398 ? -51.309  -5.229  -3.537   1.00 30.89  ? 398 LYS D CA  1 
ATOM   15910 C C   . LYS D  1 398 ? -52.410  -4.577  -2.705   1.00 30.80  ? 398 LYS D C   1 
ATOM   15911 O O   . LYS D  1 398 ? -53.529  -5.081  -2.647   1.00 28.36  ? 398 LYS D O   1 
ATOM   15912 C CB  . LYS D  1 398 ? -51.504  -4.841  -5.003   1.00 31.37  ? 398 LYS D CB  1 
ATOM   15913 C CG  . LYS D  1 398 ? -51.419  -3.327  -5.290   1.00 31.36  ? 398 LYS D CG  1 
ATOM   15914 C CD  . LYS D  1 398 ? -51.790  -2.862  -6.708   1.00 30.94  ? 398 LYS D CD  1 
ATOM   15915 C CE  . LYS D  1 398 ? -51.752  -1.368  -6.862   1.00 29.33  ? 398 LYS D CE  1 
ATOM   15916 N NZ  . LYS D  1 398 ? -51.974  -0.928  -8.239   1.00 27.99  ? 398 LYS D NZ  1 
ATOM   15917 N N   . ASN D  1 399 ? -51.999  -3.524  -1.984   1.00 29.20  ? 399 ASN D N   1 
ATOM   15918 C CA  . ASN D  1 399 ? -52.861  -2.572  -1.320   1.00 28.59  ? 399 ASN D CA  1 
ATOM   15919 C C   . ASN D  1 399 ? -52.762  -1.243  -2.035   1.00 27.36  ? 399 ASN D C   1 
ATOM   15920 O O   . ASN D  1 399 ? -51.658  -0.857  -2.377   1.00 27.01  ? 399 ASN D O   1 
ATOM   15921 C CB  . ASN D  1 399 ? -52.368  -2.225  0.064    1.00 29.10  ? 399 ASN D CB  1 
ATOM   15922 C CG  . ASN D  1 399 ? -52.594  -3.359  1.011    1.00 30.87  ? 399 ASN D CG  1 
ATOM   15923 O OD1 . ASN D  1 399 ? -53.725  -3.596  1.443    1.00 36.05  ? 399 ASN D OD1 1 
ATOM   15924 N ND2 . ASN D  1 399 ? -51.535  -4.037  1.385    1.00 32.28  ? 399 ASN D ND2 1 
ATOM   15925 N N   . GLU D  1 400 ? -53.905  -0.568  -2.242   1.00 27.95  ? 400 GLU D N   1 
ATOM   15926 C CA  . GLU D  1 400 ? -53.929  0.792   -2.771   1.00 25.81  ? 400 GLU D CA  1 
ATOM   15927 C C   . GLU D  1 400 ? -55.204  1.508   -2.304   1.00 27.11  ? 400 GLU D C   1 
ATOM   15928 O O   . GLU D  1 400 ? -56.307  0.946   -2.243   1.00 26.81  ? 400 GLU D O   1 
ATOM   15929 C CB  . GLU D  1 400 ? -53.833  0.727   -4.296   1.00 26.43  ? 400 GLU D CB  1 
ATOM   15930 C CG  . GLU D  1 400 ? -53.650  2.102   -4.947   1.00 27.14  ? 400 GLU D CG  1 
ATOM   15931 C CD  . GLU D  1 400 ? -53.559  2.193   -6.457   1.00 27.62  ? 400 GLU D CD  1 
ATOM   15932 O OE1 . GLU D  1 400 ? -53.842  1.144   -7.108   1.00 27.35  ? 400 GLU D OE1 1 
ATOM   15933 O OE2 . GLU D  1 400 ? -53.187  3.309   -6.964   1.00 27.58  ? 400 GLU D OE2 1 
ATOM   15934 N N   . SER D  1 401 ? -55.053  2.804   -2.033   1.00 26.75  ? 401 SER D N   1 
ATOM   15935 C CA  . SER D  1 401 ? -56.131  3.636   -1.546   1.00 25.78  ? 401 SER D CA  1 
ATOM   15936 C C   . SER D  1 401 ? -56.699  4.527   -2.661   1.00 25.90  ? 401 SER D C   1 
ATOM   15937 O O   . SER D  1 401 ? -55.984  5.013   -3.544   1.00 24.22  ? 401 SER D O   1 
ATOM   15938 C CB  . SER D  1 401 ? -55.633  4.416   -0.386   1.00 26.72  ? 401 SER D CB  1 
ATOM   15939 O OG  . SER D  1 401 ? -55.691  3.628   0.784    1.00 27.59  ? 401 SER D OG  1 
ATOM   15940 N N   . ILE D  1 402 ? -58.024  4.721   -2.635   1.00 25.45  ? 402 ILE D N   1 
ATOM   15941 C CA  . ILE D  1 402 ? -58.648  5.709   -3.494   1.00 26.37  ? 402 ILE D CA  1 
ATOM   15942 C C   . ILE D  1 402 ? -59.354  6.696   -2.575   1.00 26.31  ? 402 ILE D C   1 
ATOM   15943 O O   . ILE D  1 402 ? -60.201  6.285   -1.796   1.00 27.85  ? 402 ILE D O   1 
ATOM   15944 C CB  . ILE D  1 402 ? -59.603  5.038   -4.511   1.00 27.29  ? 402 ILE D CB  1 
ATOM   15945 C CG1 . ILE D  1 402 ? -58.877  4.034   -5.397   1.00 27.77  ? 402 ILE D CG1 1 
ATOM   15946 C CG2 . ILE D  1 402 ? -60.336  6.062   -5.379   1.00 26.97  ? 402 ILE D CG2 1 
ATOM   15947 C CD1 . ILE D  1 402 ? -57.914  4.643   -6.406   1.00 27.36  ? 402 ILE D CD1 1 
ATOM   15948 N N   . ASN D  1 403 ? -58.983  7.975   -2.630   1.00 25.90  ? 403 ASN D N   1 
ATOM   15949 C CA  . ASN D  1 403 ? -59.546  8.971   -1.728   1.00 26.49  ? 403 ASN D CA  1 
ATOM   15950 C C   . ASN D  1 403 ? -60.661  9.700   -2.483   1.00 26.55  ? 403 ASN D C   1 
ATOM   15951 O O   . ASN D  1 403 ? -60.441  10.248  -3.566   1.00 26.18  ? 403 ASN D O   1 
ATOM   15952 C CB  . ASN D  1 403 ? -58.508  9.974   -1.235   1.00 26.59  ? 403 ASN D CB  1 
ATOM   15953 C CG  . ASN D  1 403 ? -57.499  9.388   -0.275   1.00 27.78  ? 403 ASN D CG  1 
ATOM   15954 O OD1 . ASN D  1 403 ? -57.761  9.273   0.923    1.00 28.92  ? 403 ASN D OD1 1 
ATOM   15955 N ND2 . ASN D  1 403 ? -56.333  9.001   -0.778   1.00 28.30  ? 403 ASN D ND2 1 
ATOM   15956 N N   . ILE D  1 404 ? -61.876  9.664   -1.952   1.00 26.37  ? 404 ILE D N   1 
ATOM   15957 C CA  . ILE D  1 404 ? -62.969  10.335  -2.638   1.00 26.94  ? 404 ILE D CA  1 
ATOM   15958 C C   . ILE D  1 404 ? -63.560  11.361  -1.688   1.00 26.60  ? 404 ILE D C   1 
ATOM   15959 O O   . ILE D  1 404 ? -63.374  11.279  -0.489   1.00 25.84  ? 404 ILE D O   1 
ATOM   15960 C CB  . ILE D  1 404 ? -64.035  9.347   -3.157   1.00 28.14  ? 404 ILE D CB  1 
ATOM   15961 C CG1 . ILE D  1 404 ? -64.778  8.630   -2.027   1.00 28.95  ? 404 ILE D CG1 1 
ATOM   15962 C CG2 . ILE D  1 404 ? -63.437  8.348   -4.153   1.00 28.41  ? 404 ILE D CG2 1 
ATOM   15963 C CD1 . ILE D  1 404 ? -66.054  7.935   -2.469   1.00 30.06  ? 404 ILE D CD1 1 
ATOM   15964 N N   . LEU D  1 405 ? -64.265  12.338  -2.247   1.00 27.55  ? 405 LEU D N   1 
ATOM   15965 C CA  . LEU D  1 405 ? -65.111  13.193  -1.439   1.00 28.11  ? 405 LEU D CA  1 
ATOM   15966 C C   . LEU D  1 405 ? -66.551  12.938  -1.859   1.00 29.30  ? 405 LEU D C   1 
ATOM   15967 O O   . LEU D  1 405 ? -66.908  13.232  -2.994   1.00 30.79  ? 405 LEU D O   1 
ATOM   15968 C CB  . LEU D  1 405 ? -64.659  14.640  -1.683   1.00 27.97  ? 405 LEU D CB  1 
ATOM   15969 C CG  . LEU D  1 405 ? -65.500  15.709  -0.976   1.00 28.58  ? 405 LEU D CG  1 
ATOM   15970 C CD1 . LEU D  1 405 ? -65.384  15.499  0.537    1.00 29.18  ? 405 LEU D CD1 1 
ATOM   15971 C CD2 . LEU D  1 405 ? -65.147  17.140  -1.360   1.00 27.69  ? 405 LEU D CD2 1 
ATOM   15972 N N   . ALA D  1 406 ? -67.409  12.455  -0.951   1.00 30.71  ? 406 ALA D N   1 
ATOM   15973 C CA  . ALA D  1 406 ? -68.697  11.945  -1.402   1.00 31.35  ? 406 ALA D CA  1 
ATOM   15974 C C   . ALA D  1 406 ? -69.889  12.525  -0.644   1.00 32.18  ? 406 ALA D C   1 
ATOM   15975 O O   . ALA D  1 406 ? -69.811  12.780  0.546    1.00 32.04  ? 406 ALA D O   1 
ATOM   15976 C CB  . ALA D  1 406 ? -68.671  10.436  -1.309   1.00 31.88  ? 406 ALA D CB  1 
ATOM   15977 N N   . SER D  1 407 ? -71.020  12.647  -1.351   1.00 33.76  ? 407 SER D N   1 
ATOM   15978 C CA  . SER D  1 407 ? -72.295  13.007  -0.749   1.00 36.60  ? 407 SER D CA  1 
ATOM   15979 C C   . SER D  1 407 ? -73.444  12.322  -1.476   1.00 37.86  ? 407 SER D C   1 
ATOM   15980 O O   . SER D  1 407 ? -73.349  12.033  -2.658   1.00 39.73  ? 407 SER D O   1 
ATOM   15981 C CB  . SER D  1 407 ? -72.539  14.498  -0.756   1.00 36.48  ? 407 SER D CB  1 
ATOM   15982 O OG  . SER D  1 407 ? -73.746  14.793  -0.059   1.00 38.05  ? 407 SER D OG  1 
ATOM   15983 N N   . LYS D  1 408 ? -74.561  12.137  -0.789   1.00 39.13  ? 408 LYS D N   1 
ATOM   15984 C CA  . LYS D  1 408 ? -75.724  11.596  -1.470   1.00 42.50  ? 408 LYS D CA  1 
ATOM   15985 C C   . LYS D  1 408 ? -76.244  12.575  -2.520   1.00 43.34  ? 408 LYS D C   1 
ATOM   15986 O O   . LYS D  1 408 ? -77.072  12.187  -3.330   1.00 42.63  ? 408 LYS D O   1 
ATOM   15987 C CB  . LYS D  1 408 ? -76.903  11.307  -0.541   1.00 43.99  ? 408 LYS D CB  1 
ATOM   15988 C CG  . LYS D  1 408 ? -77.518  12.558  0.065    1.00 45.87  ? 408 LYS D CG  1 
ATOM   15989 C CD  . LYS D  1 408 ? -78.629  12.303  1.077    1.00 46.00  ? 408 LYS D CD  1 
ATOM   15990 C CE  . LYS D  1 408 ? -79.205  13.613  1.451    1.00 47.66  ? 408 LYS D CE  1 
ATOM   15991 N NZ  . LYS D  1 408 ? -80.392  13.435  2.287    1.00 50.34  ? 408 LYS D NZ  1 
ATOM   15992 N N   . THR D  1 409 ? -75.779  13.831  -2.521   1.00 43.95  ? 409 THR D N   1 
ATOM   15993 C CA  . THR D  1 409 ? -76.342  14.798  -3.453   1.00 45.86  ? 409 THR D CA  1 
ATOM   15994 C C   . THR D  1 409 ? -75.346  15.921  -3.770   1.00 46.07  ? 409 THR D C   1 
ATOM   15995 O O   . THR D  1 409 ? -74.201  15.907  -3.336   1.00 48.62  ? 409 THR D O   1 
ATOM   15996 C CB  . THR D  1 409 ? -77.664  15.284  -2.855   1.00 46.65  ? 409 THR D CB  1 
ATOM   15997 O OG1 . THR D  1 409 ? -78.386  15.689  -4.010   1.00 48.07  ? 409 THR D OG1 1 
ATOM   15998 C CG2 . THR D  1 409 ? -77.498  16.345  -1.778   1.00 46.54  ? 409 THR D CG2 1 
ATOM   15999 N N   . ALA D  1 410 ? -75.758  16.878  -4.604   1.00 46.56  ? 410 ALA D N   1 
ATOM   16000 C CA  . ALA D  1 410 ? -74.864  17.957  -5.000   1.00 45.03  ? 410 ALA D CA  1 
ATOM   16001 C C   . ALA D  1 410 ? -74.549  18.847  -3.794   1.00 44.52  ? 410 ALA D C   1 
ATOM   16002 O O   . ALA D  1 410 ? -75.390  19.047  -2.927   1.00 43.90  ? 410 ALA D O   1 
ATOM   16003 C CB  . ALA D  1 410 ? -75.478  18.755  -6.119   1.00 44.47  ? 410 ALA D CB  1 
ATOM   16004 N N   . PHE D  1 411 ? -73.306  19.342  -3.719   1.00 43.99  ? 411 PHE D N   1 
ATOM   16005 C CA  . PHE D  1 411 ? -72.923  20.248  -2.651   1.00 43.99  ? 411 PHE D CA  1 
ATOM   16006 C C   . PHE D  1 411 ? -72.071  21.381  -3.224   1.00 43.35  ? 411 PHE D C   1 
ATOM   16007 O O   . PHE D  1 411 ? -71.539  21.286  -4.326   1.00 42.61  ? 411 PHE D O   1 
ATOM   16008 C CB  . PHE D  1 411 ? -72.262  19.443  -1.527   1.00 43.03  ? 411 PHE D CB  1 
ATOM   16009 C CG  . PHE D  1 411 ? -71.024  18.642  -1.918   1.00 42.33  ? 411 PHE D CG  1 
ATOM   16010 C CD1 . PHE D  1 411 ? -71.136  17.317  -2.324   1.00 40.64  ? 411 PHE D CD1 1 
ATOM   16011 C CD2 . PHE D  1 411 ? -69.741  19.192  -1.830   1.00 39.72  ? 411 PHE D CD2 1 
ATOM   16012 C CE1 . PHE D  1 411 ? -70.002  16.582  -2.652   1.00 37.35  ? 411 PHE D CE1 1 
ATOM   16013 C CE2 . PHE D  1 411 ? -68.620  18.440  -2.149   1.00 37.04  ? 411 PHE D CE2 1 
ATOM   16014 C CZ  . PHE D  1 411 ? -68.759  17.151  -2.568   1.00 36.65  ? 411 PHE D CZ  1 
ATOM   16015 N N   . GLU D  1 412 ? -71.974  22.481  -2.478   1.00 43.52  ? 412 GLU D N   1 
ATOM   16016 C CA  . GLU D  1 412 ? -71.165  23.597  -2.923   1.00 44.57  ? 412 GLU D CA  1 
ATOM   16017 C C   . GLU D  1 412 ? -69.704  23.295  -2.622   1.00 40.36  ? 412 GLU D C   1 
ATOM   16018 O O   . GLU D  1 412 ? -69.377  22.791  -1.553   1.00 39.77  ? 412 GLU D O   1 
ATOM   16019 C CB  . GLU D  1 412 ? -71.598  24.915  -2.284   1.00 50.49  ? 412 GLU D CB  1 
ATOM   16020 C CG  . GLU D  1 412 ? -72.886  25.517  -2.859   1.00 57.50  ? 412 GLU D CG  1 
ATOM   16021 C CD  . GLU D  1 412 ? -73.077  26.972  -2.405   1.00 64.19  ? 412 GLU D CD  1 
ATOM   16022 O OE1 . GLU D  1 412 ? -72.198  27.850  -2.700   1.00 66.04  ? 412 GLU D OE1 1 
ATOM   16023 O OE2 . GLU D  1 412 ? -74.089  27.219  -1.702   1.00 62.02  ? 412 GLU D OE2 1 
ATOM   16024 N N   . LEU D  1 413 ? -68.855  23.620  -3.597   1.00 39.26  ? 413 LEU D N   1 
ATOM   16025 C CA  . LEU D  1 413 ? -67.411  23.635  -3.454   1.00 37.31  ? 413 LEU D CA  1 
ATOM   16026 C C   . LEU D  1 413 ? -66.920  25.068  -3.581   1.00 37.42  ? 413 LEU D C   1 
ATOM   16027 O O   . LEU D  1 413 ? -67.527  25.863  -4.286   1.00 35.92  ? 413 LEU D O   1 
ATOM   16028 C CB  . LEU D  1 413 ? -66.817  22.805  -4.588   1.00 37.28  ? 413 LEU D CB  1 
ATOM   16029 C CG  . LEU D  1 413 ? -67.072  21.299  -4.530   1.00 38.74  ? 413 LEU D CG  1 
ATOM   16030 C CD1 . LEU D  1 413 ? -66.955  20.620  -5.901   1.00 39.28  ? 413 LEU D CD1 1 
ATOM   16031 C CD2 . LEU D  1 413 ? -66.101  20.689  -3.537   1.00 38.70  ? 413 LEU D CD2 1 
ATOM   16032 N N   . PRO D  1 414 ? -65.722  25.391  -3.033   1.00 39.19  ? 414 PRO D N   1 
ATOM   16033 C CA  . PRO D  1 414 ? -65.042  26.647  -3.370   1.00 37.50  ? 414 PRO D CA  1 
ATOM   16034 C C   . PRO D  1 414 ? -64.620  26.596  -4.831   1.00 37.28  ? 414 PRO D C   1 
ATOM   16035 O O   . PRO D  1 414 ? -64.352  25.515  -5.350   1.00 36.58  ? 414 PRO D O   1 
ATOM   16036 C CB  . PRO D  1 414 ? -63.850  26.724  -2.440   1.00 37.78  ? 414 PRO D CB  1 
ATOM   16037 C CG  . PRO D  1 414 ? -63.628  25.297  -1.993   1.00 37.77  ? 414 PRO D CG  1 
ATOM   16038 C CD  . PRO D  1 414 ? -64.946  24.535  -2.115   1.00 37.06  ? 414 PRO D CD  1 
ATOM   16039 N N   . GLU D  1 415 ? -64.584  27.766  -5.476   1.00 38.81  ? 415 GLU D N   1 
ATOM   16040 C CA  . GLU D  1 415 ? -64.337  27.884  -6.904   1.00 40.54  ? 415 GLU D CA  1 
ATOM   16041 C C   . GLU D  1 415 ? -63.277  28.957  -7.136   1.00 38.28  ? 415 GLU D C   1 
ATOM   16042 O O   . GLU D  1 415 ? -63.393  30.061  -6.630   1.00 37.22  ? 415 GLU D O   1 
ATOM   16043 C CB  . GLU D  1 415 ? -65.558  28.364  -7.692   1.00 45.73  ? 415 GLU D CB  1 
ATOM   16044 C CG  . GLU D  1 415 ? -66.683  27.339  -7.813   1.00 51.83  ? 415 GLU D CG  1 
ATOM   16045 C CD  . GLU D  1 415 ? -67.941  27.864  -8.491   1.00 55.08  ? 415 GLU D CD  1 
ATOM   16046 O OE1 . GLU D  1 415 ? -68.452  28.943  -8.124   1.00 60.39  ? 415 GLU D OE1 1 
ATOM   16047 O OE2 . GLU D  1 415 ? -68.432  27.160  -9.383   1.00 58.68  ? 415 GLU D OE2 1 
ATOM   16048 N N   . LEU D  1 416 ? -62.263  28.620  -7.931   1.00 35.37  ? 416 LEU D N   1 
ATOM   16049 C CA  . LEU D  1 416 ? -61.299  29.586  -8.399   1.00 34.20  ? 416 LEU D CA  1 
ATOM   16050 C C   . LEU D  1 416 ? -61.530  29.807  -9.889   1.00 32.44  ? 416 LEU D C   1 
ATOM   16051 O O   . LEU D  1 416 ? -61.548  28.838  -10.643  1.00 35.63  ? 416 LEU D O   1 
ATOM   16052 C CB  . LEU D  1 416 ? -59.909  29.023  -8.090   1.00 33.21  ? 416 LEU D CB  1 
ATOM   16053 C CG  . LEU D  1 416 ? -58.740  29.974  -8.359   1.00 33.83  ? 416 LEU D CG  1 
ATOM   16054 C CD1 . LEU D  1 416 ? -57.525  29.594  -7.525   1.00 34.20  ? 416 LEU D CD1 1 
ATOM   16055 C CD2 . LEU D  1 416 ? -58.406  29.997  -9.835   1.00 33.48  ? 416 LEU D CD2 1 
ATOM   16056 N N   . THR D  1 417 ? -61.714  31.065  -10.285  1.00 31.29  ? 417 THR D N   1 
ATOM   16057 C CA  . THR D  1 417 ? -61.718  31.474  -11.683  1.00 31.08  ? 417 THR D CA  1 
ATOM   16058 C C   . THR D  1 417 ? -60.712  32.609  -11.878  1.00 30.79  ? 417 THR D C   1 
ATOM   16059 O O   . THR D  1 417 ? -60.410  33.346  -10.948  1.00 31.53  ? 417 THR D O   1 
ATOM   16060 C CB  . THR D  1 417 ? -63.112  31.885  -12.173  1.00 31.38  ? 417 THR D CB  1 
ATOM   16061 O OG1 . THR D  1 417 ? -63.502  33.028  -11.409  1.00 29.76  ? 417 THR D OG1 1 
ATOM   16062 C CG2 . THR D  1 417 ? -64.093  30.713  -12.113  1.00 31.00  ? 417 THR D CG2 1 
ATOM   16063 N N   . ILE D  1 418 ? -60.196  32.732  -13.108  1.00 30.40  ? 418 ILE D N   1 
ATOM   16064 C CA  . ILE D  1 418 ? -59.365  33.861  -13.488  1.00 30.00  ? 418 ILE D CA  1 
ATOM   16065 C C   . ILE D  1 418 ? -59.936  34.570  -14.712  1.00 30.29  ? 418 ILE D C   1 
ATOM   16066 O O   . ILE D  1 418 ? -60.699  34.002  -15.508  1.00 29.61  ? 418 ILE D O   1 
ATOM   16067 C CB  . ILE D  1 418 ? -57.934  33.385  -13.747  1.00 28.93  ? 418 ILE D CB  1 
ATOM   16068 C CG1 . ILE D  1 418 ? -57.870  32.585  -15.044  1.00 29.08  ? 418 ILE D CG1 1 
ATOM   16069 C CG2 . ILE D  1 418 ? -57.424  32.614  -12.535  1.00 27.77  ? 418 ILE D CG2 1 
ATOM   16070 C CD1 . ILE D  1 418 ? -56.488  32.046  -15.390  1.00 28.36  ? 418 ILE D CD1 1 
ATOM   16071 N N   . GLU D  1 419 ? -59.586  35.855  -14.802  1.00 31.47  ? 419 GLU D N   1 
ATOM   16072 C CA  . GLU D  1 419 ? -59.803  36.676  -15.978  1.00 32.55  ? 419 GLU D CA  1 
ATOM   16073 C C   . GLU D  1 419 ? -58.433  37.201  -16.387  1.00 32.86  ? 419 GLU D C   1 
ATOM   16074 O O   . GLU D  1 419 ? -57.725  37.792  -15.561  1.00 32.90  ? 419 GLU D O   1 
ATOM   16075 C CB  . GLU D  1 419 ? -60.666  37.917  -15.735  1.00 33.84  ? 419 GLU D CB  1 
ATOM   16076 C CG  . GLU D  1 419 ? -62.118  37.660  -15.341  1.00 35.59  ? 419 GLU D CG  1 
ATOM   16077 C CD  . GLU D  1 419 ? -62.765  38.927  -14.758  1.00 39.45  ? 419 GLU D CD  1 
ATOM   16078 O OE1 . GLU D  1 419 ? -62.134  39.704  -14.003  1.00 40.24  ? 419 GLU D OE1 1 
ATOM   16079 O OE2 . GLU D  1 419 ? -63.942  39.147  -15.028  1.00 41.98  ? 419 GLU D OE2 1 
ATOM   16080 N N   . VAL D  1 420 ? -58.070  36.984  -17.651  1.00 31.93  ? 420 VAL D N   1 
ATOM   16081 C CA  . VAL D  1 420 ? -56.725  37.281  -18.114  1.00 30.87  ? 420 VAL D CA  1 
ATOM   16082 C C   . VAL D  1 420 ? -56.769  38.380  -19.172  1.00 30.99  ? 420 VAL D C   1 
ATOM   16083 O O   . VAL D  1 420 ? -57.651  38.407  -20.018  1.00 31.48  ? 420 VAL D O   1 
ATOM   16084 C CB  . VAL D  1 420 ? -56.076  35.999  -18.657  1.00 29.36  ? 420 VAL D CB  1 
ATOM   16085 C CG1 . VAL D  1 420 ? -54.628  36.238  -19.035  1.00 29.39  ? 420 VAL D CG1 1 
ATOM   16086 C CG2 . VAL D  1 420 ? -56.198  34.834  -17.686  1.00 28.83  ? 420 VAL D CG2 1 
ATOM   16087 N N   . THR D  1 421 ? -55.800  39.298  -19.088  1.00 32.25  ? 421 THR D N   1 
ATOM   16088 C CA  . THR D  1 421 ? -55.615  40.399  -20.033  1.00 31.72  ? 421 THR D CA  1 
ATOM   16089 C C   . THR D  1 421 ? -54.216  40.261  -20.639  1.00 31.86  ? 421 THR D C   1 
ATOM   16090 O O   . THR D  1 421 ? -53.270  40.015  -19.898  1.00 30.88  ? 421 THR D O   1 
ATOM   16091 C CB  . THR D  1 421 ? -55.745  41.707  -19.253  1.00 31.52  ? 421 THR D CB  1 
ATOM   16092 O OG1 . THR D  1 421 ? -56.948  41.562  -18.528  1.00 30.90  ? 421 THR D OG1 1 
ATOM   16093 C CG2 . THR D  1 421 ? -55.792  42.949  -20.116  1.00 31.99  ? 421 THR D CG2 1 
ATOM   16094 N N   . PRO D  1 422 ? -54.005  40.374  -21.974  1.00 34.01  ? 422 PRO D N   1 
ATOM   16095 C CA  . PRO D  1 422 ? -55.067  40.340  -22.976  1.00 34.83  ? 422 PRO D CA  1 
ATOM   16096 C C   . PRO D  1 422 ? -55.760  38.990  -22.991  1.00 34.88  ? 422 PRO D C   1 
ATOM   16097 O O   . PRO D  1 422 ? -55.103  37.944  -22.798  1.00 35.21  ? 422 PRO D O   1 
ATOM   16098 C CB  . PRO D  1 422 ? -54.340  40.655  -24.298  1.00 34.85  ? 422 PRO D CB  1 
ATOM   16099 C CG  . PRO D  1 422 ? -53.130  41.432  -23.869  1.00 34.24  ? 422 PRO D CG  1 
ATOM   16100 C CD  . PRO D  1 422 ? -52.714  40.709  -22.597  1.00 35.27  ? 422 PRO D CD  1 
ATOM   16101 N N   . GLU D  1 423 ? -57.086  39.062  -23.197  1.00 34.53  ? 423 GLU D N   1 
ATOM   16102 C CA  . GLU D  1 423 ? -57.999  37.938  -23.064  1.00 34.81  ? 423 GLU D CA  1 
ATOM   16103 C C   . GLU D  1 423 ? -57.903  36.997  -24.268  1.00 34.12  ? 423 GLU D C   1 
ATOM   16104 O O   . GLU D  1 423 ? -58.067  35.786  -24.115  1.00 34.30  ? 423 GLU D O   1 
ATOM   16105 C CB  . GLU D  1 423 ? -59.411  38.495  -22.880  1.00 36.12  ? 423 GLU D CB  1 
ATOM   16106 C CG  . GLU D  1 423 ? -60.446  37.388  -22.702  1.00 38.83  ? 423 GLU D CG  1 
ATOM   16107 C CD  . GLU D  1 423 ? -61.916  37.811  -22.774  1.00 41.42  ? 423 GLU D CD  1 
ATOM   16108 O OE1 . GLU D  1 423 ? -62.270  38.966  -23.046  1.00 39.33  ? 423 GLU D OE1 1 
ATOM   16109 O OE2 . GLU D  1 423 ? -62.732  36.901  -22.552  1.00 46.12  ? 423 GLU D OE2 1 
ATOM   16110 N N   . LYS D  1 424 ? -57.643  37.553  -25.461  1.00 35.51  ? 424 LYS D N   1 
ATOM   16111 C CA  . LYS D  1 424 ? -57.754  36.814  -26.715  1.00 38.66  ? 424 LYS D CA  1 
ATOM   16112 C C   . LYS D  1 424 ? -56.538  36.961  -27.629  1.00 36.58  ? 424 LYS D C   1 
ATOM   16113 O O   . LYS D  1 424 ? -56.202  36.022  -28.357  1.00 36.94  ? 424 LYS D O   1 
ATOM   16114 C CB  . LYS D  1 424 ? -58.988  37.276  -27.500  1.00 43.69  ? 424 LYS D CB  1 
ATOM   16115 C CG  . LYS D  1 424 ? -60.281  36.775  -26.914  1.00 49.26  ? 424 LYS D CG  1 
ATOM   16116 C CD  . LYS D  1 424 ? -61.535  37.318  -27.581  1.00 54.60  ? 424 LYS D CD  1 
ATOM   16117 C CE  . LYS D  1 424 ? -62.668  37.106  -26.631  1.00 57.00  ? 424 LYS D CE  1 
ATOM   16118 N NZ  . LYS D  1 424 ? -63.894  36.931  -27.397  1.00 60.09  ? 424 LYS D NZ  1 
ATOM   16119 N N   . ASP D  1 425 ? -55.892  38.126  -27.645  1.00 35.13  ? 425 ASP D N   1 
ATOM   16120 C CA  . ASP D  1 425 ? -54.797  38.315  -28.583  1.00 34.99  ? 425 ASP D CA  1 
ATOM   16121 C C   . ASP D  1 425 ? -53.601  39.020  -27.927  1.00 33.76  ? 425 ASP D C   1 
ATOM   16122 O O   . ASP D  1 425 ? -53.656  40.203  -27.613  1.00 35.94  ? 425 ASP D O   1 
ATOM   16123 C CB  . ASP D  1 425 ? -55.338  38.989  -29.834  1.00 34.69  ? 425 ASP D CB  1 
ATOM   16124 C CG  . ASP D  1 425 ? -54.289  39.243  -30.904  1.00 35.31  ? 425 ASP D CG  1 
ATOM   16125 O OD1 . ASP D  1 425 ? -53.089  38.987  -30.657  1.00 33.17  ? 425 ASP D OD1 1 
ATOM   16126 O OD2 . ASP D  1 425 ? -54.676  39.704  -31.981  1.00 39.36  ? 425 ASP D OD2 1 
ATOM   16127 N N   . LEU D  1 426 ? -52.461  38.341  -27.835  1.00 32.49  ? 426 LEU D N   1 
ATOM   16128 C CA  . LEU D  1 426 ? -51.309  38.885  -27.130  1.00 32.15  ? 426 LEU D CA  1 
ATOM   16129 C C   . LEU D  1 426 ? -50.728  40.133  -27.798  1.00 33.38  ? 426 LEU D C   1 
ATOM   16130 O O   . LEU D  1 426 ? -49.945  40.831  -27.166  1.00 33.51  ? 426 LEU D O   1 
ATOM   16131 C CB  . LEU D  1 426 ? -50.248  37.804  -26.996  1.00 30.37  ? 426 LEU D CB  1 
ATOM   16132 C CG  . LEU D  1 426 ? -50.676  36.586  -26.178  1.00 28.55  ? 426 LEU D CG  1 
ATOM   16133 C CD1 . LEU D  1 426 ? -49.466  35.668  -26.071  1.00 28.50  ? 426 LEU D CD1 1 
ATOM   16134 C CD2 . LEU D  1 426 ? -51.215  36.918  -24.805  1.00 27.68  ? 426 LEU D CD2 1 
ATOM   16135 N N   . ASN D  1 427 ? -51.128  40.440  -29.043  1.00 34.82  ? 427 ASN D N   1 
ATOM   16136 C CA  . ASN D  1 427 ? -50.667  41.645  -29.732  1.00 35.11  ? 427 ASN D CA  1 
ATOM   16137 C C   . ASN D  1 427 ? -51.277  42.907  -29.134  1.00 38.02  ? 427 ASN D C   1 
ATOM   16138 O O   . ASN D  1 427 ? -50.779  43.983  -29.418  1.00 40.34  ? 427 ASN D O   1 
ATOM   16139 C CB  . ASN D  1 427 ? -50.966  41.682  -31.227  1.00 33.79  ? 427 ASN D CB  1 
ATOM   16140 C CG  . ASN D  1 427 ? -50.109  40.736  -32.031  1.00 34.68  ? 427 ASN D CG  1 
ATOM   16141 O OD1 . ASN D  1 427 ? -50.620  40.060  -32.933  1.00 37.78  ? 427 ASN D OD1 1 
ATOM   16142 N ND2 . ASN D  1 427 ? -48.825  40.654  -31.730  1.00 32.76  ? 427 ASN D ND2 1 
ATOM   16143 N N   . GLU D  1 428 ? -52.364  42.788  -28.353  1.00 40.56  ? 428 GLU D N   1 
ATOM   16144 C CA  . GLU D  1 428 ? -53.041  43.941  -27.780  1.00 39.75  ? 428 GLU D CA  1 
ATOM   16145 C C   . GLU D  1 428 ? -52.310  44.504  -26.569  1.00 38.90  ? 428 GLU D C   1 
ATOM   16146 O O   . GLU D  1 428 ? -52.825  45.383  -25.924  1.00 40.92  ? 428 GLU D O   1 
ATOM   16147 C CB  . GLU D  1 428 ? -54.431  43.562  -27.294  1.00 44.25  ? 428 GLU D CB  1 
ATOM   16148 C CG  . GLU D  1 428 ? -55.289  42.934  -28.389  1.00 49.95  ? 428 GLU D CG  1 
ATOM   16149 C CD  . GLU D  1 428 ? -56.791  43.104  -28.209  1.00 54.52  ? 428 GLU D CD  1 
ATOM   16150 O OE1 . GLU D  1 428 ? -57.226  43.462  -27.088  1.00 54.69  ? 428 GLU D OE1 1 
ATOM   16151 O OE2 . GLU D  1 428 ? -57.520  42.909  -29.206  1.00 56.30  ? 428 GLU D OE2 1 
ATOM   16152 N N   . GLY D  1 429 ? -51.137  43.988  -26.206  1.00 38.88  ? 429 GLY D N   1 
ATOM   16153 C CA  . GLY D  1 429 ? -50.335  44.643  -25.193  1.00 36.88  ? 429 GLY D CA  1 
ATOM   16154 C C   . GLY D  1 429 ? -48.999  43.950  -25.003  1.00 35.84  ? 429 GLY D C   1 
ATOM   16155 O O   . GLY D  1 429 ? -48.826  42.801  -25.417  1.00 35.57  ? 429 GLY D O   1 
ATOM   16156 N N   . LYS D  1 430 ? -48.070  44.688  -24.377  1.00 36.96  ? 430 LYS D N   1 
ATOM   16157 C CA  . LYS D  1 430 ? -46.773  44.181  -23.952  1.00 37.54  ? 430 LYS D CA  1 
ATOM   16158 C C   . LYS D  1 430 ? -46.849  43.547  -22.551  1.00 34.04  ? 430 LYS D C   1 
ATOM   16159 O O   . LYS D  1 430 ? -45.965  42.798  -22.165  1.00 30.09  ? 430 LYS D O   1 
ATOM   16160 C CB  . LYS D  1 430 ? -45.758  45.328  -24.006  1.00 42.30  ? 430 LYS D CB  1 
ATOM   16161 C CG  . LYS D  1 430 ? -45.248  45.681  -25.393  1.00 48.07  ? 430 LYS D CG  1 
ATOM   16162 C CD  . LYS D  1 430 ? -44.093  46.687  -25.367  1.00 59.75  ? 430 LYS D CD  1 
ATOM   16163 C CE  . LYS D  1 430 ? -43.870  47.425  -26.670  1.00 66.89  ? 430 LYS D CE  1 
ATOM   16164 N NZ  . LYS D  1 430 ? -43.788  46.460  -27.777  1.00 74.15  ? 430 LYS D NZ  1 
ATOM   16165 N N   . ILE D  1 431 ? -47.921  43.850  -21.795  1.00 33.10  ? 431 ILE D N   1 
ATOM   16166 C CA  . ILE D  1 431 ? -48.047  43.465  -20.401  1.00 31.81  ? 431 ILE D CA  1 
ATOM   16167 C C   . ILE D  1 431 ? -49.362  42.736  -20.190  1.00 30.47  ? 431 ILE D C   1 
ATOM   16168 O O   . ILE D  1 431 ? -50.388  43.192  -20.670  1.00 30.16  ? 431 ILE D O   1 
ATOM   16169 C CB  . ILE D  1 431 ? -48.005  44.696  -19.484  1.00 33.16  ? 431 ILE D CB  1 
ATOM   16170 C CG1 . ILE D  1 431 ? -46.745  45.503  -19.695  1.00 33.16  ? 431 ILE D CG1 1 
ATOM   16171 C CG2 . ILE D  1 431 ? -48.187  44.248  -18.026  1.00 33.87  ? 431 ILE D CG2 1 
ATOM   16172 C CD1 . ILE D  1 431 ? -46.621  46.696  -18.789  1.00 34.15  ? 431 ILE D CD1 1 
ATOM   16173 N N   . ALA D  1 432 ? -49.319  41.656  -19.405  1.00 29.94  ? 432 ALA D N   1 
ATOM   16174 C CA  . ALA D  1 432 ? -50.505  40.863  -19.115  1.00 29.89  ? 432 ALA D CA  1 
ATOM   16175 C C   . ALA D  1 432 ? -50.859  40.928  -17.639  1.00 29.89  ? 432 ALA D C   1 
ATOM   16176 O O   . ALA D  1 432 ? -49.997  41.187  -16.813  1.00 30.86  ? 432 ALA D O   1 
ATOM   16177 C CB  . ALA D  1 432 ? -50.264  39.420  -19.506  1.00 29.88  ? 432 ALA D CB  1 
ATOM   16178 N N   . SER D  1 433 ? -52.126  40.652  -17.298  1.00 30.74  ? 433 SER D N   1 
ATOM   16179 C CA  . SER D  1 433 ? -52.463  40.375  -15.908  1.00 31.22  ? 433 SER D CA  1 
ATOM   16180 C C   . SER D  1 433 ? -53.352  39.141  -15.800  1.00 32.93  ? 433 SER D C   1 
ATOM   16181 O O   . SER D  1 433 ? -54.079  38.797  -16.729  1.00 33.10  ? 433 SER D O   1 
ATOM   16182 C CB  . SER D  1 433 ? -53.113  41.520  -15.232  1.00 31.03  ? 433 SER D CB  1 
ATOM   16183 O OG  . SER D  1 433 ? -54.458  41.670  -15.633  1.00 31.27  ? 433 SER D OG  1 
ATOM   16184 N N   . ILE D  1 434 ? -53.290  38.513  -14.620  1.00 33.98  ? 434 ILE D N   1 
ATOM   16185 C CA  . ILE D  1 434 ? -54.209  37.466  -14.220  1.00 32.97  ? 434 ILE D CA  1 
ATOM   16186 C C   . ILE D  1 434 ? -54.912  37.934  -12.953  1.00 34.83  ? 434 ILE D C   1 
ATOM   16187 O O   . ILE D  1 434 ? -54.259  38.142  -11.929  1.00 36.60  ? 434 ILE D O   1 
ATOM   16188 C CB  . ILE D  1 434 ? -53.443  36.151  -14.006  1.00 32.36  ? 434 ILE D CB  1 
ATOM   16189 C CG1 . ILE D  1 434 ? -52.769  35.686  -15.275  1.00 31.75  ? 434 ILE D CG1 1 
ATOM   16190 C CG2 . ILE D  1 434 ? -54.356  35.062  -13.442  1.00 33.36  ? 434 ILE D CG2 1 
ATOM   16191 C CD1 . ILE D  1 434 ? -51.741  34.579  -15.049  1.00 33.78  ? 434 ILE D CD1 1 
ATOM   16192 N N   . LYS D  1 435 ? -56.236  38.122  -13.041  1.00 36.38  ? 435 LYS D N   1 
ATOM   16193 C CA  . LYS D  1 435 ? -57.061  38.459  -11.889  1.00 37.53  ? 435 LYS D CA  1 
ATOM   16194 C C   . LYS D  1 435 ? -57.638  37.165  -11.349  1.00 36.32  ? 435 LYS D C   1 
ATOM   16195 O O   . LYS D  1 435 ? -58.257  36.417  -12.096  1.00 36.95  ? 435 LYS D O   1 
ATOM   16196 C CB  . LYS D  1 435 ? -58.169  39.434  -12.301  1.00 39.53  ? 435 LYS D CB  1 
ATOM   16197 C CG  . LYS D  1 435 ? -57.634  40.829  -12.578  1.00 43.70  ? 435 LYS D CG  1 
ATOM   16198 C CD  . LYS D  1 435 ? -58.662  41.951  -12.747  1.00 48.25  ? 435 LYS D CD  1 
ATOM   16199 C CE  . LYS D  1 435 ? -59.295  41.921  -14.115  1.00 52.14  ? 435 LYS D CE  1 
ATOM   16200 N NZ  . LYS D  1 435 ? -59.822  43.242  -14.482  1.00 56.29  ? 435 LYS D NZ  1 
ATOM   16201 N N   . THR D  1 436 ? -57.411  36.876  -10.071  1.00 36.48  ? 436 THR D N   1 
ATOM   16202 C CA  . THR D  1 436 ? -57.898  35.625  -9.504   1.00 36.62  ? 436 THR D CA  1 
ATOM   16203 C C   . THR D  1 436 ? -59.051  35.941  -8.558   1.00 35.25  ? 436 THR D C   1 
ATOM   16204 O O   . THR D  1 436 ? -58.911  36.820  -7.708   1.00 33.15  ? 436 THR D O   1 
ATOM   16205 C CB  . THR D  1 436 ? -56.792  34.856  -8.780   1.00 35.29  ? 436 THR D CB  1 
ATOM   16206 O OG1 . THR D  1 436 ? -55.838  34.586  -9.786   1.00 34.33  ? 436 THR D OG1 1 
ATOM   16207 C CG2 . THR D  1 436 ? -57.261  33.521  -8.225   1.00 35.17  ? 436 THR D CG2 1 
ATOM   16208 N N   . LYS D  1 437 ? -60.150  35.185  -8.728   1.00 34.77  ? 437 LYS D N   1 
ATOM   16209 C CA  . LYS D  1 437 ? -61.291  35.206  -7.830   1.00 35.96  ? 437 LYS D CA  1 
ATOM   16210 C C   . LYS D  1 437 ? -61.486  33.828  -7.205   1.00 34.63  ? 437 LYS D C   1 
ATOM   16211 O O   . LYS D  1 437 ? -61.534  32.809  -7.902   1.00 34.00  ? 437 LYS D O   1 
ATOM   16212 C CB  . LYS D  1 437 ? -62.483  35.636  -8.669   1.00 38.26  ? 437 LYS D CB  1 
ATOM   16213 C CG  . LYS D  1 437 ? -63.758  35.749  -7.879   1.00 42.60  ? 437 LYS D CG  1 
ATOM   16214 C CD  . LYS D  1 437 ? -64.926  36.191  -8.756   1.00 46.39  ? 437 LYS D CD  1 
ATOM   16215 C CE  . LYS D  1 437 ? -66.263  35.894  -8.155   1.00 51.45  ? 437 LYS D CE  1 
ATOM   16216 N NZ  . LYS D  1 437 ? -67.359  36.601  -8.833   1.00 56.61  ? 437 LYS D NZ  1 
ATOM   16217 N N   . ILE D  1 438 ? -61.490  33.786  -5.875   1.00 34.08  ? 438 ILE D N   1 
ATOM   16218 C CA  . ILE D  1 438 ? -61.818  32.574  -5.147   1.00 34.35  ? 438 ILE D CA  1 
ATOM   16219 C C   . ILE D  1 438 ? -63.111  32.795  -4.376   1.00 36.28  ? 438 ILE D C   1 
ATOM   16220 O O   . ILE D  1 438 ? -63.161  33.649  -3.490   1.00 38.63  ? 438 ILE D O   1 
ATOM   16221 C CB  . ILE D  1 438 ? -60.690  32.174  -4.180   1.00 33.65  ? 438 ILE D CB  1 
ATOM   16222 C CG1 . ILE D  1 438 ? -59.344  32.004  -4.889   1.00 33.14  ? 438 ILE D CG1 1 
ATOM   16223 C CG2 . ILE D  1 438 ? -61.089  30.923  -3.394   1.00 32.72  ? 438 ILE D CG2 1 
ATOM   16224 C CD1 . ILE D  1 438 ? -58.175  31.819  -3.938   1.00 32.84  ? 438 ILE D CD1 1 
ATOM   16225 N N   . GLU D  1 439 ? -64.139  32.003  -4.688   1.00 38.55  ? 439 GLU D N   1 
ATOM   16226 C CA  . GLU D  1 439 ? -65.340  31.920  -3.856   1.00 41.02  ? 439 GLU D CA  1 
ATOM   16227 C C   . GLU D  1 439 ? -65.137  30.859  -2.778   1.00 41.36  ? 439 GLU D C   1 
ATOM   16228 O O   . GLU D  1 439 ? -64.928  29.679  -3.093   1.00 41.06  ? 439 GLU D O   1 
ATOM   16229 C CB  . GLU D  1 439 ? -66.573  31.572  -4.684   1.00 44.09  ? 439 GLU D CB  1 
ATOM   16230 C CG  . GLU D  1 439 ? -66.730  32.488  -5.893   1.00 48.95  ? 439 GLU D CG  1 
ATOM   16231 C CD  . GLU D  1 439 ? -68.147  32.847  -6.282   1.00 55.51  ? 439 GLU D CD  1 
ATOM   16232 O OE1 . GLU D  1 439 ? -69.070  32.356  -5.584   1.00 62.30  ? 439 GLU D OE1 1 
ATOM   16233 O OE2 . GLU D  1 439 ? -68.311  33.673  -7.232   1.00 58.92  ? 439 GLU D OE2 1 
ATOM   16234 N N   . THR D  1 440 ? -65.152  31.282  -1.505   1.00 41.86  ? 440 THR D N   1 
ATOM   16235 C CA  . THR D  1 440 ? -64.924  30.349  -0.405   1.00 41.25  ? 440 THR D CA  1 
ATOM   16236 C C   . THR D  1 440 ? -66.207  29.592  -0.078   1.00 42.29  ? 440 THR D C   1 
ATOM   16237 O O   . THR D  1 440 ? -67.309  29.996  -0.448   1.00 41.43  ? 440 THR D O   1 
ATOM   16238 C CB  . THR D  1 440 ? -64.404  31.070  0.839    1.00 41.68  ? 440 THR D CB  1 
ATOM   16239 O OG1 . THR D  1 440 ? -65.335  32.112  1.108    1.00 40.13  ? 440 THR D OG1 1 
ATOM   16240 C CG2 . THR D  1 440 ? -62.996  31.612  0.657    1.00 41.63  ? 440 THR D CG2 1 
ATOM   16241 N N   . SER D  1 441 ? -66.041  28.519  0.691    1.00 42.35  ? 441 SER D N   1 
ATOM   16242 C CA  . SER D  1 441 ? -67.171  27.730  1.140    1.00 44.43  ? 441 SER D CA  1 
ATOM   16243 C C   . SER D  1 441 ? -66.818  27.212  2.528    1.00 45.31  ? 441 SER D C   1 
ATOM   16244 O O   . SER D  1 441 ? -65.700  26.734  2.744    1.00 45.99  ? 441 SER D O   1 
ATOM   16245 C CB  . SER D  1 441 ? -67.451  26.595  0.139    1.00 47.75  ? 441 SER D CB  1 
ATOM   16246 O OG  . SER D  1 441 ? -68.835  26.381  -0.087   1.00 50.85  ? 441 SER D OG  1 
ATOM   16247 N N   . GLU D  1 442 ? -67.761  27.322  3.463    1.00 49.41  ? 442 GLU D N   1 
ATOM   16248 C CA  . GLU D  1 442 ? -67.583  26.803  4.813    1.00 55.70  ? 442 GLU D CA  1 
ATOM   16249 C C   . GLU D  1 442 ? -67.347  25.284  4.775    1.00 58.79  ? 442 GLU D C   1 
ATOM   16250 O O   . GLU D  1 442 ? -67.926  24.535  3.977    1.00 56.97  ? 442 GLU D O   1 
ATOM   16251 C CB  . GLU D  1 442 ? -68.755  27.197  5.722    1.00 62.03  ? 442 GLU D CB  1 
ATOM   16252 C CG  . GLU D  1 442 ? -70.076  26.491  5.416    1.00 64.55  ? 442 GLU D CG  1 
ATOM   16253 C CD  . GLU D  1 442 ? -71.307  27.085  6.097    1.00 74.97  ? 442 GLU D CD  1 
ATOM   16254 O OE1 . GLU D  1 442 ? -71.136  27.965  6.972    1.00 78.71  ? 442 GLU D OE1 1 
ATOM   16255 O OE2 . GLU D  1 442 ? -72.450  26.704  5.731    1.00 75.57  ? 442 GLU D OE2 1 
ATOM   16256 N N   . ASN D  1 443 ? -66.447  24.844  5.657    1.00 57.05  ? 443 ASN D N   1 
ATOM   16257 C CA  . ASN D  1 443 ? -66.102  23.446  5.818    1.00 52.04  ? 443 ASN D CA  1 
ATOM   16258 C C   . ASN D  1 443 ? -64.895  23.135  4.952    1.00 47.85  ? 443 ASN D C   1 
ATOM   16259 O O   . ASN D  1 443 ? -64.188  22.194  5.265    1.00 43.37  ? 443 ASN D O   1 
ATOM   16260 C CB  . ASN D  1 443 ? -67.264  22.492  5.560    1.00 55.22  ? 443 ASN D CB  1 
ATOM   16261 C CG  . ASN D  1 443 ? -68.459  22.806  6.427    1.00 60.80  ? 443 ASN D CG  1 
ATOM   16262 O OD1 . ASN D  1 443 ? -69.588  22.936  5.928    1.00 63.90  ? 443 ASN D OD1 1 
ATOM   16263 N ND2 . ASN D  1 443 ? -68.217  22.968  7.721    1.00 61.57  ? 443 ASN D ND2 1 
ATOM   16264 N N   . PHE D  1 444 ? -64.643  23.927  3.893    1.00 46.04  ? 444 PHE D N   1 
ATOM   16265 C CA  . PHE D  1 444 ? -63.445  23.736  3.085    1.00 39.95  ? 444 PHE D CA  1 
ATOM   16266 C C   . PHE D  1 444 ? -62.414  24.785  3.478    1.00 40.47  ? 444 PHE D C   1 
ATOM   16267 O O   . PHE D  1 444 ? -62.708  25.992  3.490    1.00 41.04  ? 444 PHE D O   1 
ATOM   16268 C CB  . PHE D  1 444 ? -63.733  23.802  1.584    1.00 38.50  ? 444 PHE D CB  1 
ATOM   16269 C CG  . PHE D  1 444 ? -64.648  22.710  1.053    1.00 37.65  ? 444 PHE D CG  1 
ATOM   16270 C CD1 . PHE D  1 444 ? -66.023  22.777  1.236    1.00 39.79  ? 444 PHE D CD1 1 
ATOM   16271 C CD2 . PHE D  1 444 ? -64.131  21.621  0.372    1.00 36.65  ? 444 PHE D CD2 1 
ATOM   16272 C CE1 . PHE D  1 444 ? -66.855  21.790  0.745    1.00 40.00  ? 444 PHE D CE1 1 
ATOM   16273 C CE2 . PHE D  1 444 ? -64.966  20.625  -0.101   1.00 37.08  ? 444 PHE D CE2 1 
ATOM   16274 C CZ  . PHE D  1 444 ? -66.322  20.718  0.073    1.00 38.72  ? 444 PHE D CZ  1 
ATOM   16275 N N   . THR D  1 445 ? -61.203  24.291  3.758    1.00 39.16  ? 445 THR D N   1 
ATOM   16276 C CA  . THR D  1 445 ? -60.084  25.095  4.215    1.00 39.03  ? 445 THR D CA  1 
ATOM   16277 C C   . THR D  1 445 ? -59.110  25.286  3.055    1.00 39.97  ? 445 THR D C   1 
ATOM   16278 O O   . THR D  1 445 ? -58.612  24.310  2.472    1.00 37.79  ? 445 THR D O   1 
ATOM   16279 C CB  . THR D  1 445 ? -59.463  24.375  5.416    1.00 38.49  ? 445 THR D CB  1 
ATOM   16280 O OG1 . THR D  1 445 ? -60.491  24.522  6.387    1.00 38.34  ? 445 THR D OG1 1 
ATOM   16281 C CG2 . THR D  1 445 ? -58.184  25.000  5.954    1.00 38.92  ? 445 THR D CG2 1 
ATOM   16282 N N   . LEU D  1 446 ? -58.812  26.558  2.757    1.00 39.89  ? 446 LEU D N   1 
ATOM   16283 C CA  . LEU D  1 446 ? -57.789  26.884  1.781    1.00 39.87  ? 446 LEU D CA  1 
ATOM   16284 C C   . LEU D  1 446 ? -56.446  26.741  2.476    1.00 42.72  ? 446 LEU D C   1 
ATOM   16285 O O   . LEU D  1 446 ? -56.317  27.152  3.615    1.00 46.59  ? 446 LEU D O   1 
ATOM   16286 C CB  . LEU D  1 446 ? -57.981  28.279  1.193    1.00 39.21  ? 446 LEU D CB  1 
ATOM   16287 C CG  . LEU D  1 446 ? -59.390  28.592  0.673    1.00 39.32  ? 446 LEU D CG  1 
ATOM   16288 C CD1 . LEU D  1 446 ? -59.575  30.059  0.336    1.00 39.33  ? 446 LEU D CD1 1 
ATOM   16289 C CD2 . LEU D  1 446 ? -59.749  27.735  -0.528   1.00 38.34  ? 446 LEU D CD2 1 
ATOM   16290 N N   . LEU D  1 447 ? -55.480  26.117  1.804    1.00 43.66  ? 447 LEU D N   1 
ATOM   16291 C CA  . LEU D  1 447 ? -54.136  25.984  2.333    1.00 51.64  ? 447 LEU D CA  1 
ATOM   16292 C C   . LEU D  1 447 ? -53.151  26.998  1.738    1.00 62.27  ? 447 LEU D C   1 
ATOM   16293 O O   . LEU D  1 447 ? -53.377  27.637  0.706    1.00 70.18  ? 447 LEU D O   1 
ATOM   16294 C CB  . LEU D  1 447 ? -53.676  24.559  2.051    1.00 48.79  ? 447 LEU D CB  1 
ATOM   16295 C CG  . LEU D  1 447 ? -54.517  23.467  2.704    1.00 51.40  ? 447 LEU D CG  1 
ATOM   16296 C CD1 . LEU D  1 447 ? -53.894  22.139  2.374    1.00 51.42  ? 447 LEU D CD1 1 
ATOM   16297 C CD2 . LEU D  1 447 ? -54.641  23.686  4.216    1.00 55.54  ? 447 LEU D CD2 1 
ATOM   16298 N N   . ASP D  1 448 ? -52.037  27.139  2.462    1.00 67.85  ? 448 ASP D N   1 
ATOM   16299 C CA  . ASP D  1 448 ? -50.794  27.710  1.958    1.00 67.05  ? 448 ASP D CA  1 
ATOM   16300 C C   . ASP D  1 448 ? -51.116  28.830  0.973    1.00 54.27  ? 448 ASP D C   1 
ATOM   16301 O O   . ASP D  1 448 ? -52.004  29.617  1.233    1.00 53.44  ? 448 ASP D O   1 
ATOM   16302 C CB  . ASP D  1 448 ? -49.852  26.640  1.395    1.00 63.73  ? 448 ASP D CB  1 
ATOM   16303 C CG  . ASP D  1 448 ? -49.460  25.488  2.316    1.00 60.10  ? 448 ASP D CG  1 
ATOM   16304 O OD1 . ASP D  1 448 ? -49.185  25.732  3.506    1.00 57.46  ? 448 ASP D OD1 1 
ATOM   16305 O OD2 . ASP D  1 448 ? -49.410  24.341  1.824    1.00 58.64  ? 448 ASP D OD2 1 
ATOM   16306 N N   . ASP D  1 449 ? -50.423  28.804  -0.168   1.00 55.57  ? 449 ASP D N   1 
ATOM   16307 C CA  . ASP D  1 449 ? -50.313  29.919  -1.089   1.00 58.31  ? 449 ASP D CA  1 
ATOM   16308 C C   . ASP D  1 449 ? -51.086  29.566  -2.353   1.00 48.52  ? 449 ASP D C   1 
ATOM   16309 O O   . ASP D  1 449 ? -51.065  28.423  -2.800   1.00 38.04  ? 449 ASP D O   1 
ATOM   16310 C CB  . ASP D  1 449 ? -48.876  30.264  -1.484   1.00 57.60  ? 449 ASP D CB  1 
ATOM   16311 C CG  . ASP D  1 449 ? -48.032  31.077  -0.506   1.00 66.74  ? 449 ASP D CG  1 
ATOM   16312 O OD1 . ASP D  1 449 ? -48.457  31.258  0.668    1.00 66.56  ? 449 ASP D OD1 1 
ATOM   16313 O OD2 . ASP D  1 449 ? -46.944  31.543  -0.935   1.00 71.40  ? 449 ASP D OD2 1 
ATOM   16314 N N   . LEU D  1 450 ? -51.792  30.595  -2.837   1.00 45.89  ? 450 LEU D N   1 
ATOM   16315 C CA  . LEU D  1 450 ? -52.233  30.697  -4.208   1.00 40.99  ? 450 LEU D CA  1 
ATOM   16316 C C   . LEU D  1 450 ? -51.007  30.657  -5.112   1.00 36.07  ? 450 LEU D C   1 
ATOM   16317 O O   . LEU D  1 450 ? -50.058  31.394  -4.862   1.00 35.91  ? 450 LEU D O   1 
ATOM   16318 C CB  . LEU D  1 450 ? -52.981  32.031  -4.300   1.00 38.78  ? 450 LEU D CB  1 
ATOM   16319 C CG  . LEU D  1 450 ? -53.503  32.411  -5.688   1.00 38.42  ? 450 LEU D CG  1 
ATOM   16320 C CD1 . LEU D  1 450 ? -54.440  31.343  -6.233   1.00 38.30  ? 450 LEU D CD1 1 
ATOM   16321 C CD2 . LEU D  1 450 ? -54.174  33.762  -5.653   1.00 39.92  ? 450 LEU D CD2 1 
ATOM   16322 N N   . LYS D  1 451 ? -51.051  29.860  -6.180   1.00 33.29  ? 451 LYS D N   1 
ATOM   16323 C CA  . LYS D  1 451 ? -49.989  29.889  -7.174   1.00 34.83  ? 451 LYS D CA  1 
ATOM   16324 C C   . LYS D  1 451 ? -50.498  30.397  -8.518   1.00 33.89  ? 451 LYS D C   1 
ATOM   16325 O O   . LYS D  1 451 ? -51.643  30.122  -8.893   1.00 32.29  ? 451 LYS D O   1 
ATOM   16326 C CB  . LYS D  1 451 ? -49.322  28.523  -7.268   1.00 36.47  ? 451 LYS D CB  1 
ATOM   16327 C CG  . LYS D  1 451 ? -48.612  28.240  -5.956   1.00 42.89  ? 451 LYS D CG  1 
ATOM   16328 C CD  . LYS D  1 451 ? -47.700  27.022  -5.971   1.00 48.66  ? 451 LYS D CD  1 
ATOM   16329 C CE  . LYS D  1 451 ? -47.489  26.458  -4.604   1.00 52.66  ? 451 LYS D CE  1 
ATOM   16330 N NZ  . LYS D  1 451 ? -47.091  25.058  -4.721   1.00 51.96  ? 451 LYS D NZ  1 
ATOM   16331 N N   . ILE D  1 452 ? -49.620  31.159  -9.203   1.00 33.21  ? 452 ILE D N   1 
ATOM   16332 C CA  . ILE D  1 452 ? -49.915  31.789  -10.485  1.00 34.58  ? 452 ILE D CA  1 
ATOM   16333 C C   . ILE D  1 452 ? -48.815  31.455  -11.494  1.00 33.58  ? 452 ILE D C   1 
ATOM   16334 O O   . ILE D  1 452 ? -47.642  31.533  -11.178  1.00 36.59  ? 452 ILE D O   1 
ATOM   16335 C CB  . ILE D  1 452 ? -50.017  33.313  -10.351  1.00 36.11  ? 452 ILE D CB  1 
ATOM   16336 C CG1 . ILE D  1 452 ? -50.763  33.753  -9.090   1.00 37.66  ? 452 ILE D CG1 1 
ATOM   16337 C CG2 . ILE D  1 452 ? -50.576  33.915  -11.638  1.00 36.19  ? 452 ILE D CG2 1 
ATOM   16338 C CD1 . ILE D  1 452 ? -52.255  33.578  -9.126   1.00 38.86  ? 452 ILE D CD1 1 
ATOM   16339 N N   . SER D  1 453 ? -49.202  31.171  -12.737  1.00 31.83  ? 453 SER D N   1 
ATOM   16340 C CA  . SER D  1 453 ? -48.281  30.809  -13.794  1.00 28.83  ? 453 SER D CA  1 
ATOM   16341 C C   . SER D  1 453 ? -48.665  31.567  -15.058  1.00 27.32  ? 453 SER D C   1 
ATOM   16342 O O   . SER D  1 453 ? -49.798  31.464  -15.461  1.00 26.14  ? 453 SER D O   1 
ATOM   16343 C CB  . SER D  1 453 ? -48.326  29.305  -14.049  1.00 28.39  ? 453 SER D CB  1 
ATOM   16344 O OG  . SER D  1 453 ? -47.590  28.950  -15.211  1.00 27.26  ? 453 SER D OG  1 
ATOM   16345 N N   . TYR D  1 454 ? -47.695  32.251  -15.698  1.00 27.49  ? 454 TYR D N   1 
ATOM   16346 C CA  . TYR D  1 454 ? -47.840  32.776  -17.044  1.00 27.70  ? 454 TYR D CA  1 
ATOM   16347 C C   . TYR D  1 454 ? -46.810  32.101  -17.952  1.00 28.68  ? 454 TYR D C   1 
ATOM   16348 O O   . TYR D  1 454 ? -45.752  32.681  -18.225  1.00 28.07  ? 454 TYR D O   1 
ATOM   16349 C CB  . TYR D  1 454 ? -47.723  34.301  -17.010  1.00 27.13  ? 454 TYR D CB  1 
ATOM   16350 C CG  . TYR D  1 454 ? -48.281  34.989  -18.245  1.00 27.15  ? 454 TYR D CG  1 
ATOM   16351 C CD1 . TYR D  1 454 ? -49.653  35.168  -18.416  1.00 27.91  ? 454 TYR D CD1 1 
ATOM   16352 C CD2 . TYR D  1 454 ? -47.450  35.530  -19.212  1.00 27.03  ? 454 TYR D CD2 1 
ATOM   16353 C CE1 . TYR D  1 454 ? -50.183  35.793  -19.541  1.00 27.09  ? 454 TYR D CE1 1 
ATOM   16354 C CE2 . TYR D  1 454 ? -47.963  36.148  -20.345  1.00 26.96  ? 454 TYR D CE2 1 
ATOM   16355 C CZ  . TYR D  1 454 ? -49.333  36.297  -20.510  1.00 27.39  ? 454 TYR D CZ  1 
ATOM   16356 O OH  . TYR D  1 454 ? -49.831  36.969  -21.599  1.00 26.82  ? 454 TYR D OH  1 
ATOM   16357 N N   . ASN D  1 455 ? -47.162  30.902  -18.455  1.00 26.99  ? 455 ASN D N   1 
ATOM   16358 C CA  . ASN D  1 455 ? -46.208  30.073  -19.172  1.00 26.87  ? 455 ASN D CA  1 
ATOM   16359 C C   . ASN D  1 455 ? -46.182  30.424  -20.654  1.00 25.88  ? 455 ASN D C   1 
ATOM   16360 O O   . ASN D  1 455 ? -47.070  30.029  -21.404  1.00 23.66  ? 455 ASN D O   1 
ATOM   16361 C CB  . ASN D  1 455 ? -46.470  28.589  -18.964  1.00 27.72  ? 455 ASN D CB  1 
ATOM   16362 C CG  . ASN D  1 455 ? -45.400  27.725  -19.606  1.00 28.10  ? 455 ASN D CG  1 
ATOM   16363 O OD1 . ASN D  1 455 ? -44.630  28.197  -20.459  1.00 27.59  ? 455 ASN D OD1 1 
ATOM   16364 N ND2 . ASN D  1 455 ? -45.368  26.458  -19.219  1.00 26.34  ? 455 ASN D ND2 1 
ATOM   16365 N N   . THR D  1 456 ? -45.101  31.119  -21.051  1.00 25.81  ? 456 THR D N   1 
ATOM   16366 C CA  . THR D  1 456 ? -44.988  31.827  -22.320  1.00 25.61  ? 456 THR D CA  1 
ATOM   16367 C C   . THR D  1 456 ? -44.456  30.913  -23.427  1.00 26.16  ? 456 THR D C   1 
ATOM   16368 O O   . THR D  1 456 ? -44.400  31.349  -24.596  1.00 26.50  ? 456 THR D O   1 
ATOM   16369 C CB  . THR D  1 456 ? -44.078  33.033  -22.103  1.00 26.99  ? 456 THR D CB  1 
ATOM   16370 O OG1 . THR D  1 456 ? -43.008  32.593  -21.258  1.00 27.78  ? 456 THR D OG1 1 
ATOM   16371 C CG2 . THR D  1 456 ? -44.806  34.202  -21.445  1.00 27.02  ? 456 THR D CG2 1 
ATOM   16372 N N   . HIS D  1 457 ? -44.045  29.679  -23.053  1.00 24.65  ? 457 HIS D N   1 
ATOM   16373 C CA  . HIS D  1 457 ? -43.793  28.596  -24.001  1.00 25.01  ? 457 HIS D CA  1 
ATOM   16374 C C   . HIS D  1 457 ? -42.508  28.813  -24.799  1.00 25.23  ? 457 HIS D C   1 
ATOM   16375 O O   . HIS D  1 457 ? -42.430  28.380  -25.953  1.00 24.74  ? 457 HIS D O   1 
ATOM   16376 C CB  . HIS D  1 457 ? -44.997  28.398  -24.945  1.00 25.06  ? 457 HIS D CB  1 
ATOM   16377 C CG  . HIS D  1 457 ? -46.121  27.633  -24.326  1.00 25.37  ? 457 HIS D CG  1 
ATOM   16378 N ND1 . HIS D  1 457 ? -46.518  26.376  -24.755  1.00 26.97  ? 457 HIS D ND1 1 
ATOM   16379 C CD2 . HIS D  1 457 ? -46.919  27.947  -23.312  1.00 25.82  ? 457 HIS D CD2 1 
ATOM   16380 C CE1 . HIS D  1 457 ? -47.533  25.943  -24.002  1.00 26.38  ? 457 HIS D CE1 1 
ATOM   16381 N NE2 . HIS D  1 457 ? -47.806  26.889  -23.122  1.00 26.82  ? 457 HIS D NE2 1 
ATOM   16382 N N   . LEU D  1 458 ? -41.521  29.506  -24.210  1.00 27.03  ? 458 LEU D N   1 
ATOM   16383 C CA  . LEU D  1 458 ? -40.232  29.738  -24.867  1.00 29.17  ? 458 LEU D CA  1 
ATOM   16384 C C   . LEU D  1 458 ? -39.347  28.494  -24.751  1.00 27.95  ? 458 LEU D C   1 
ATOM   16385 O O   . LEU D  1 458 ? -38.698  28.240  -23.743  1.00 30.08  ? 458 LEU D O   1 
ATOM   16386 C CB  . LEU D  1 458 ? -39.553  30.981  -24.290  1.00 30.09  ? 458 LEU D CB  1 
ATOM   16387 C CG  . LEU D  1 458 ? -40.403  32.269  -24.315  1.00 33.79  ? 458 LEU D CG  1 
ATOM   16388 C CD1 . LEU D  1 458 ? -39.625  33.498  -23.798  1.00 31.67  ? 458 LEU D CD1 1 
ATOM   16389 C CD2 . LEU D  1 458 ? -41.061  32.595  -25.684  1.00 33.64  ? 458 LEU D CD2 1 
ATOM   16390 N N   . GLY D  1 459 ? -39.350  27.651  -25.769  1.00 28.95  ? 459 GLY D N   1 
ATOM   16391 C CA  . GLY D  1 459 ? -38.761  26.334  -25.583  1.00 30.38  ? 459 GLY D CA  1 
ATOM   16392 C C   . GLY D  1 459 ? -39.380  25.640  -24.364  1.00 29.31  ? 459 GLY D C   1 
ATOM   16393 O O   . GLY D  1 459 ? -40.615  25.663  -24.206  1.00 25.49  ? 459 GLY D O   1 
ATOM   16394 N N   . TRP D  1 460 ? -38.490  25.097  -23.499  1.00 29.82  ? 460 TRP D N   1 
ATOM   16395 C CA  . TRP D  1 460 ? -38.847  24.408  -22.258  1.00 28.52  ? 460 TRP D CA  1 
ATOM   16396 C C   . TRP D  1 460 ? -38.950  25.346  -21.068  1.00 28.93  ? 460 TRP D C   1 
ATOM   16397 O O   . TRP D  1 460 ? -39.258  24.883  -19.990  1.00 29.01  ? 460 TRP D O   1 
ATOM   16398 C CB  . TRP D  1 460 ? -37.829  23.319  -21.894  1.00 28.29  ? 460 TRP D CB  1 
ATOM   16399 C CG  . TRP D  1 460 ? -37.703  22.236  -22.931  1.00 27.50  ? 460 TRP D CG  1 
ATOM   16400 C CD1 . TRP D  1 460 ? -36.667  22.031  -23.806  1.00 27.22  ? 460 TRP D CD1 1 
ATOM   16401 C CD2 . TRP D  1 460 ? -38.683  21.223  -23.218  1.00 25.74  ? 460 TRP D CD2 1 
ATOM   16402 N NE1 . TRP D  1 460 ? -36.948  20.961  -24.622  1.00 28.51  ? 460 TRP D NE1 1 
ATOM   16403 C CE2 . TRP D  1 460 ? -38.169  20.437  -24.271  1.00 26.42  ? 460 TRP D CE2 1 
ATOM   16404 C CE3 . TRP D  1 460 ? -39.917  20.884  -22.676  1.00 28.16  ? 460 TRP D CE3 1 
ATOM   16405 C CZ2 . TRP D  1 460 ? -38.854  19.346  -24.776  1.00 27.71  ? 460 TRP D CZ2 1 
ATOM   16406 C CZ3 . TRP D  1 460 ? -40.619  19.820  -23.208  1.00 28.00  ? 460 TRP D CZ3 1 
ATOM   16407 C CH2 . TRP D  1 460 ? -40.082  19.050  -24.227  1.00 27.88  ? 460 TRP D CH2 1 
ATOM   16408 N N   . ALA D  1 461 ? -38.669  26.636  -21.238  1.00 28.60  ? 461 ALA D N   1 
ATOM   16409 C CA  . ALA D  1 461 ? -38.755  27.555  -20.108  1.00 31.38  ? 461 ALA D CA  1 
ATOM   16410 C C   . ALA D  1 461 ? -40.220  27.688  -19.682  1.00 33.49  ? 461 ALA D C   1 
ATOM   16411 O O   . ALA D  1 461 ? -41.111  27.756  -20.535  1.00 33.27  ? 461 ALA D O   1 
ATOM   16412 C CB  . ALA D  1 461 ? -38.123  28.898  -20.478  1.00 29.48  ? 461 ALA D CB  1 
ATOM   16413 N N   . ILE D  1 462 ? -40.470  27.719  -18.370  1.00 33.14  ? 462 ILE D N   1 
ATOM   16414 C CA  . ILE D  1 462 ? -41.851  27.675  -17.898  1.00 35.73  ? 462 ILE D CA  1 
ATOM   16415 C C   . ILE D  1 462 ? -42.432  29.072  -17.694  1.00 33.39  ? 462 ILE D C   1 
ATOM   16416 O O   . ILE D  1 462 ? -43.613  29.173  -17.417  1.00 32.96  ? 462 ILE D O   1 
ATOM   16417 C CB  . ILE D  1 462 ? -41.987  26.850  -16.603  1.00 39.67  ? 462 ILE D CB  1 
ATOM   16418 C CG1 . ILE D  1 462 ? -41.150  27.469  -15.491  1.00 43.44  ? 462 ILE D CG1 1 
ATOM   16419 C CG2 . ILE D  1 462 ? -41.642  25.375  -16.841  1.00 38.25  ? 462 ILE D CG2 1 
ATOM   16420 C CD1 . ILE D  1 462 ? -41.578  27.056  -14.104  1.00 48.62  ? 462 ILE D CD1 1 
ATOM   16421 N N   . GLY D  1 463 ? -41.600  30.126  -17.733  1.00 33.92  ? 463 GLY D N   1 
ATOM   16422 C CA  . GLY D  1 463 ? -42.091  31.489  -17.617  1.00 32.79  ? 463 GLY D CA  1 
ATOM   16423 C C   . GLY D  1 463 ? -42.206  31.909  -16.157  1.00 32.83  ? 463 GLY D C   1 
ATOM   16424 O O   . GLY D  1 463 ? -41.756  31.198  -15.272  1.00 37.16  ? 463 GLY D O   1 
ATOM   16425 N N   . SER D  1 464 ? -42.816  33.069  -15.930  1.00 33.10  ? 464 SER D N   1 
ATOM   16426 C CA  . SER D  1 464 ? -43.020  33.630  -14.609  1.00 34.39  ? 464 SER D CA  1 
ATOM   16427 C C   . SER D  1 464 ? -43.968  32.764  -13.789  1.00 34.40  ? 464 SER D C   1 
ATOM   16428 O O   . SER D  1 464 ? -44.936  32.222  -14.336  1.00 31.45  ? 464 SER D O   1 
ATOM   16429 C CB  . SER D  1 464 ? -43.598  35.001  -14.710  1.00 34.97  ? 464 SER D CB  1 
ATOM   16430 O OG  . SER D  1 464 ? -42.716  35.874  -15.372  1.00 37.33  ? 464 SER D OG  1 
ATOM   16431 N N   . GLN D  1 465 ? -43.679  32.697  -12.471  1.00 35.22  ? 465 GLN D N   1 
ATOM   16432 C CA  . GLN D  1 465 ? -44.602  32.185  -11.473  1.00 34.42  ? 465 GLN D CA  1 
ATOM   16433 C C   . GLN D  1 465 ? -44.718  33.164  -10.317  1.00 35.22  ? 465 GLN D C   1 
ATOM   16434 O O   . GLN D  1 465 ? -43.835  33.989  -10.120  1.00 36.43  ? 465 GLN D O   1 
ATOM   16435 C CB  . GLN D  1 465 ? -44.164  30.852  -10.904  1.00 33.19  ? 465 GLN D CB  1 
ATOM   16436 C CG  . GLN D  1 465 ? -44.035  29.783  -11.975  1.00 33.98  ? 465 GLN D CG  1 
ATOM   16437 C CD  . GLN D  1 465 ? -43.630  28.467  -11.363  1.00 34.89  ? 465 GLN D CD  1 
ATOM   16438 O OE1 . GLN D  1 465 ? -42.454  28.091  -11.354  1.00 39.01  ? 465 GLN D OE1 1 
ATOM   16439 N NE2 . GLN D  1 465 ? -44.590  27.785  -10.771  1.00 34.87  ? 465 GLN D NE2 1 
ATOM   16440 N N   . ALA D  1 466 ? -45.822  33.080  -9.564   1.00 33.41  ? 466 ALA D N   1 
ATOM   16441 C CA  . ALA D  1 466 ? -45.904  33.823  -8.321   1.00 33.61  ? 466 ALA D CA  1 
ATOM   16442 C C   . ALA D  1 466 ? -46.606  32.985  -7.262   1.00 32.22  ? 466 ALA D C   1 
ATOM   16443 O O   . ALA D  1 466 ? -47.477  32.191  -7.575   1.00 32.58  ? 466 ALA D O   1 
ATOM   16444 C CB  . ALA D  1 466 ? -46.583  35.168  -8.547   1.00 34.81  ? 466 ALA D CB  1 
ATOM   16445 N N   . SER D  1 467 ? -46.175  33.173  -6.015   1.00 34.68  ? 467 SER D N   1 
ATOM   16446 C CA  . SER D  1 467 ? -46.813  32.666  -4.809   1.00 37.61  ? 467 SER D CA  1 
ATOM   16447 C C   . SER D  1 467 ? -47.432  33.850  -4.087   1.00 37.69  ? 467 SER D C   1 
ATOM   16448 O O   . SER D  1 467 ? -46.745  34.838  -3.883   1.00 39.49  ? 467 SER D O   1 
ATOM   16449 C CB  . SER D  1 467 ? -45.818  31.972  -3.891   1.00 39.63  ? 467 SER D CB  1 
ATOM   16450 O OG  . SER D  1 467 ? -45.571  30.639  -4.313   1.00 42.57  ? 467 SER D OG  1 
ATOM   16451 N N   . VAL D  1 468 ? -48.719  33.757  -3.752   1.00 36.97  ? 468 VAL D N   1 
ATOM   16452 C CA  . VAL D  1 468 ? -49.427  34.856  -3.127   1.00 37.63  ? 468 VAL D CA  1 
ATOM   16453 C C   . VAL D  1 468 ? -50.057  34.344  -1.831   1.00 38.17  ? 468 VAL D C   1 
ATOM   16454 O O   . VAL D  1 468 ? -50.804  33.361  -1.835   1.00 37.69  ? 468 VAL D O   1 
ATOM   16455 C CB  . VAL D  1 468 ? -50.449  35.458  -4.117   1.00 37.42  ? 468 VAL D CB  1 
ATOM   16456 C CG1 . VAL D  1 468 ? -51.245  36.616  -3.520   1.00 36.45  ? 468 VAL D CG1 1 
ATOM   16457 C CG2 . VAL D  1 468 ? -49.780  35.883  -5.425   1.00 36.14  ? 468 VAL D CG2 1 
ATOM   16458 N N   . SER D  1 469 ? -49.663  34.987  -0.721   1.00 40.98  ? 469 SER D N   1 
ATOM   16459 C CA  . SER D  1 469 ? -50.276  34.816  0.586    1.00 42.86  ? 469 SER D CA  1 
ATOM   16460 C C   . SER D  1 469 ? -51.681  35.401  0.538    1.00 44.30  ? 469 SER D C   1 
ATOM   16461 O O   . SER D  1 469 ? -51.882  36.516  0.069    1.00 43.57  ? 469 SER D O   1 
ATOM   16462 C CB  . SER D  1 469 ? -49.469  35.486  1.693    1.00 43.48  ? 469 SER D CB  1 
ATOM   16463 O OG  . SER D  1 469 ? -49.839  35.022  2.984    1.00 45.01  ? 469 SER D OG  1 
ATOM   16464 N N   . ILE D  1 470 ? -52.638  34.633  1.042    1.00 46.13  ? 470 ILE D N   1 
ATOM   16465 C CA  . ILE D  1 470 ? -53.981  35.141  1.202    1.00 50.56  ? 470 ILE D CA  1 
ATOM   16466 C C   . ILE D  1 470 ? -54.379  35.046  2.671    1.00 53.60  ? 470 ILE D C   1 
ATOM   16467 O O   . ILE D  1 470 ? -55.565  35.135  2.971    1.00 54.52  ? 470 ILE D O   1 
ATOM   16468 C CB  . ILE D  1 470 ? -54.948  34.372  0.290    1.00 49.75  ? 470 ILE D CB  1 
ATOM   16469 C CG1 . ILE D  1 470 ? -55.030  32.924  0.706    1.00 49.03  ? 470 ILE D CG1 1 
ATOM   16470 C CG2 . ILE D  1 470 ? -54.561  34.527  -1.177   1.00 47.55  ? 470 ILE D CG2 1 
ATOM   16471 C CD1 . ILE D  1 470 ? -56.160  32.194  0.030    1.00 53.70  ? 470 ILE D CD1 1 
ATOM   16472 N N   . SER D  1 471 ? -53.381  34.919  3.562    1.00 58.20  ? 471 SER D N   1 
ATOM   16473 C CA  . SER D  1 471 ? -53.559  34.895  5.012    1.00 60.19  ? 471 SER D CA  1 
ATOM   16474 C C   . SER D  1 471 ? -54.438  36.042  5.538    1.00 55.76  ? 471 SER D C   1 
ATOM   16475 O O   . SER D  1 471 ? -55.222  35.843  6.462    1.00 54.80  ? 471 SER D O   1 
ATOM   16476 C CB  . SER D  1 471 ? -52.211  34.853  5.720    1.00 63.89  ? 471 SER D CB  1 
ATOM   16477 O OG  . SER D  1 471 ? -51.790  33.504  5.876    1.00 61.95  ? 471 SER D OG  1 
ATOM   16478 N N   . ASP D  1 472 ? -54.356  37.225  4.928    1.00 55.31  ? 472 ASP D N   1 
ATOM   16479 C CA  . ASP D  1 472 ? -55.079  38.394  5.415    1.00 56.76  ? 472 ASP D CA  1 
ATOM   16480 C C   . ASP D  1 472 ? -56.528  38.449  4.884    1.00 58.91  ? 472 ASP D C   1 
ATOM   16481 O O   . ASP D  1 472 ? -57.202  39.487  5.018    1.00 54.11  ? 472 ASP D O   1 
ATOM   16482 C CB  . ASP D  1 472 ? -54.263  39.639  5.097    1.00 58.78  ? 472 ASP D CB  1 
ATOM   16483 C CG  . ASP D  1 472 ? -54.034  39.959  3.623    1.00 60.37  ? 472 ASP D CG  1 
ATOM   16484 O OD1 . ASP D  1 472 ? -53.806  39.008  2.829    1.00 62.61  ? 472 ASP D OD1 1 
ATOM   16485 O OD2 . ASP D  1 472 ? -54.048  41.159  3.285    1.00 59.34  ? 472 ASP D OD2 1 
ATOM   16486 N N   . GLN D  1 473 ? -57.024  37.330  4.301    1.00 53.86  ? 473 GLN D N   1 
ATOM   16487 C CA  . GLN D  1 473 ? -58.257  37.339  3.522    1.00 52.53  ? 473 GLN D CA  1 
ATOM   16488 C C   . GLN D  1 473 ? -59.157  36.115  3.781    1.00 54.54  ? 473 GLN D C   1 
ATOM   16489 O O   . GLN D  1 473 ? -60.190  35.981  3.123    1.00 52.46  ? 473 GLN D O   1 
ATOM   16490 C CB  . GLN D  1 473 ? -57.943  37.409  2.018    1.00 50.88  ? 473 GLN D CB  1 
ATOM   16491 C CG  . GLN D  1 473 ? -57.575  38.775  1.413    1.00 50.39  ? 473 GLN D CG  1 
ATOM   16492 C CD  . GLN D  1 473 ? -57.603  38.762  -0.113   1.00 47.33  ? 473 GLN D CD  1 
ATOM   16493 O OE1 . GLN D  1 473 ? -58.656  38.824  -0.757   1.00 48.10  ? 473 GLN D OE1 1 
ATOM   16494 N NE2 . GLN D  1 473 ? -56.446  38.637  -0.742   1.00 44.02  ? 473 GLN D NE2 1 
ATOM   16495 N N   . LEU D  1 474 ? -58.820  35.228  4.737    1.00 59.22  ? 474 LEU D N   1 
ATOM   16496 C CA  . LEU D  1 474 ? -59.436  33.902  4.811    1.00 60.16  ? 474 LEU D CA  1 
ATOM   16497 C C   . LEU D  1 474 ? -60.921  33.975  5.187    1.00 63.49  ? 474 LEU D C   1 
ATOM   16498 O O   . LEU D  1 474 ? -61.773  33.249  4.660    1.00 63.01  ? 474 LEU D O   1 
ATOM   16499 C CB  . LEU D  1 474 ? -58.662  33.022  5.795    1.00 62.85  ? 474 LEU D CB  1 
ATOM   16500 C CG  . LEU D  1 474 ? -57.472  32.221  5.239    1.00 64.38  ? 474 LEU D CG  1 
ATOM   16501 C CD1 . LEU D  1 474 ? -57.696  31.692  3.828    1.00 64.28  ? 474 LEU D CD1 1 
ATOM   16502 C CD2 . LEU D  1 474 ? -56.206  33.031  5.293    1.00 65.77  ? 474 LEU D CD2 1 
ATOM   16503 N N   . ASP D  1 475 ? -61.222  34.870  6.119    1.00 65.35  ? 475 ASP D N   1 
ATOM   16504 C CA  . ASP D  1 475 ? -62.564  35.057  6.631    1.00 70.34  ? 475 ASP D CA  1 
ATOM   16505 C C   . ASP D  1 475 ? -63.514  35.584  5.547    1.00 68.18  ? 475 ASP D C   1 
ATOM   16506 O O   . ASP D  1 475 ? -64.715  35.601  5.785    1.00 67.98  ? 475 ASP D O   1 
ATOM   16507 C CB  . ASP D  1 475 ? -62.536  36.030  7.807    1.00 76.74  ? 475 ASP D CB  1 
ATOM   16508 C CG  . ASP D  1 475 ? -61.819  37.352  7.534    1.00 77.03  ? 475 ASP D CG  1 
ATOM   16509 O OD1 . ASP D  1 475 ? -60.896  37.362  6.679    1.00 81.06  ? 475 ASP D OD1 1 
ATOM   16510 O OD2 . ASP D  1 475 ? -62.198  38.373  8.138    1.00 70.13  ? 475 ASP D OD2 1 
ATOM   16511 N N   . LYS D  1 476 ? -63.005  36.068  4.394    1.00 63.81  ? 476 LYS D N   1 
ATOM   16512 C CA  . LYS D  1 476 ? -63.849  36.753  3.417    1.00 57.40  ? 476 LYS D CA  1 
ATOM   16513 C C   . LYS D  1 476 ? -64.531  35.729  2.510    1.00 52.76  ? 476 LYS D C   1 
ATOM   16514 O O   . LYS D  1 476 ? -64.022  34.642  2.264    1.00 46.32  ? 476 LYS D O   1 
ATOM   16515 C CB  . LYS D  1 476 ? -63.125  37.778  2.537    1.00 56.58  ? 476 LYS D CB  1 
ATOM   16516 C CG  . LYS D  1 476 ? -62.420  38.919  3.265    1.00 62.33  ? 476 LYS D CG  1 
ATOM   16517 C CD  . LYS D  1 476 ? -62.099  40.142  2.404    1.00 66.27  ? 476 LYS D CD  1 
ATOM   16518 C CE  . LYS D  1 476 ? -60.956  39.942  1.438    1.00 66.08  ? 476 LYS D CE  1 
ATOM   16519 N NZ  . LYS D  1 476 ? -60.961  40.902  0.324    1.00 66.18  ? 476 LYS D NZ  1 
ATOM   16520 N N   . LYS D  1 477 ? -65.704  36.107  2.006    1.00 53.56  ? 477 LYS D N   1 
ATOM   16521 C CA  . LYS D  1 477 ? -66.489  35.242  1.143    1.00 54.99  ? 477 LYS D CA  1 
ATOM   16522 C C   . LYS D  1 477 ? -65.786  35.117  -0.211   1.00 48.90  ? 477 LYS D C   1 
ATOM   16523 O O   . LYS D  1 477 ? -65.800  34.062  -0.816   1.00 49.33  ? 477 LYS D O   1 
ATOM   16524 C CB  . LYS D  1 477 ? -67.911  35.814  1.070    1.00 61.33  ? 477 LYS D CB  1 
ATOM   16525 C CG  . LYS D  1 477 ? -69.040  34.823  0.786    1.00 74.31  ? 477 LYS D CG  1 
ATOM   16526 C CD  . LYS D  1 477 ? -69.511  33.962  1.966    1.00 84.61  ? 477 LYS D CD  1 
ATOM   16527 C CE  . LYS D  1 477 ? -70.417  32.797  1.611    1.00 90.53  ? 477 LYS D CE  1 
ATOM   16528 N NZ  . LYS D  1 477 ? -69.685  31.736  0.896    1.00 94.25  ? 477 LYS D NZ  1 
ATOM   16529 N N   . ILE D  1 478 ? -65.142  36.200  -0.653   1.00 47.34  ? 478 ILE D N   1 
ATOM   16530 C CA  . ILE D  1 478 ? -64.522  36.327  -1.961   1.00 44.45  ? 478 ILE D CA  1 
ATOM   16531 C C   . ILE D  1 478 ? -63.086  36.823  -1.791   1.00 43.44  ? 478 ILE D C   1 
ATOM   16532 O O   . ILE D  1 478 ? -62.855  37.939  -1.350   1.00 43.44  ? 478 ILE D O   1 
ATOM   16533 C CB  . ILE D  1 478 ? -65.347  37.284  -2.837   1.00 44.63  ? 478 ILE D CB  1 
ATOM   16534 C CG1 . ILE D  1 478 ? -66.777  36.745  -3.022   1.00 46.47  ? 478 ILE D CG1 1 
ATOM   16535 C CG2 . ILE D  1 478 ? -64.658  37.561  -4.175   1.00 43.98  ? 478 ILE D CG2 1 
ATOM   16536 C CD1 . ILE D  1 478 ? -67.610  37.467  -4.067   1.00 46.87  ? 478 ILE D CD1 1 
ATOM   16537 N N   . ILE D  1 479 ? -62.130  35.963  -2.146   1.00 42.73  ? 479 ILE D N   1 
ATOM   16538 C CA  . ILE D  1 479 ? -60.688  36.321  -2.043   1.00 42.54  ? 479 ILE D CA  1 
ATOM   16539 C C   . ILE D  1 479 ? -60.193  36.699  -3.442   1.00 42.09  ? 479 ILE D C   1 
ATOM   16540 O O   . ILE D  1 479 ? -60.503  35.974  -4.391   1.00 43.08  ? 479 ILE D O   1 
ATOM   16541 C CB  . ILE D  1 479 ? -59.894  35.160  -1.423   1.00 42.79  ? 479 ILE D CB  1 
ATOM   16542 C CG1 . ILE D  1 479 ? -60.453  34.793  -0.053   1.00 46.42  ? 479 ILE D CG1 1 
ATOM   16543 C CG2 . ILE D  1 479 ? -58.399  35.469  -1.366   1.00 41.27  ? 479 ILE D CG2 1 
ATOM   16544 C CD1 . ILE D  1 479 ? -59.690  33.691  0.653    1.00 46.15  ? 479 ILE D CD1 1 
ATOM   16545 N N   . THR D  1 480 ? -59.470  37.808  -3.550   1.00 40.94  ? 480 THR D N   1 
ATOM   16546 C CA  . THR D  1 480 ? -59.047  38.280  -4.878   1.00 39.87  ? 480 THR D CA  1 
ATOM   16547 C C   . THR D  1 480 ? -57.552  38.495  -4.939   1.00 39.80  ? 480 THR D C   1 
ATOM   16548 O O   . THR D  1 480 ? -56.943  38.697  -3.881   1.00 41.40  ? 480 THR D O   1 
ATOM   16549 C CB  . THR D  1 480 ? -59.816  39.555  -5.233   1.00 38.77  ? 480 THR D CB  1 
ATOM   16550 O OG1 . THR D  1 480 ? -59.604  40.423  -4.126   1.00 39.95  ? 480 THR D OG1 1 
ATOM   16551 C CG2 . THR D  1 480 ? -61.296  39.303  -5.455   1.00 38.24  ? 480 THR D CG2 1 
ATOM   16552 N N   . SER D  1 481 ? -56.981  38.425  -6.138   1.00 37.93  ? 481 SER D N   1 
ATOM   16553 C CA  . SER D  1 481 ? -55.549  38.748  -6.336   1.00 37.05  ? 481 SER D CA  1 
ATOM   16554 C C   . SER D  1 481 ? -55.362  39.290  -7.747   1.00 34.67  ? 481 SER D C   1 
ATOM   16555 O O   . SER D  1 481 ? -56.142  38.917  -8.627   1.00 32.69  ? 481 SER D O   1 
ATOM   16556 C CB  . SER D  1 481 ? -54.628  37.578  -6.099   1.00 38.64  ? 481 SER D CB  1 
ATOM   16557 O OG  . SER D  1 481 ? -53.290  37.902  -6.442   1.00 39.96  ? 481 SER D OG  1 
ATOM   16558 N N   . GLU D  1 482 ? -54.387  40.169  -7.922   1.00 34.61  ? 482 GLU D N   1 
ATOM   16559 C CA  . GLU D  1 482 ? -54.066  40.614  -9.269   1.00 34.65  ? 482 GLU D CA  1 
ATOM   16560 C C   . GLU D  1 482 ? -52.545  40.587  -9.460   1.00 35.46  ? 482 GLU D C   1 
ATOM   16561 O O   . GLU D  1 482 ? -51.805  41.201  -8.708   1.00 37.95  ? 482 GLU D O   1 
ATOM   16562 C CB  . GLU D  1 482 ? -54.782  41.948  -9.493   1.00 33.93  ? 482 GLU D CB  1 
ATOM   16563 C CG  . GLU D  1 482 ? -54.395  42.637  -10.797  1.00 32.90  ? 482 GLU D CG  1 
ATOM   16564 C CD  . GLU D  1 482 ? -55.071  43.981  -10.958  1.00 33.52  ? 482 GLU D CD  1 
ATOM   16565 O OE1 . GLU D  1 482 ? -55.085  44.747  -9.979   1.00 33.71  ? 482 GLU D OE1 1 
ATOM   16566 O OE2 . GLU D  1 482 ? -55.560  44.259  -12.067  1.00 32.72  ? 482 GLU D OE2 1 
ATOM   16567 N N   . ASN D  1 483 ? -52.093  39.885  -10.489  1.00 35.89  ? 483 ASN D N   1 
ATOM   16568 C CA  . ASN D  1 483 ? -50.677  39.693  -10.738  1.00 37.04  ? 483 ASN D CA  1 
ATOM   16569 C C   . ASN D  1 483 ? -50.346  40.052  -12.189  1.00 35.03  ? 483 ASN D C   1 
ATOM   16570 O O   . ASN D  1 483 ? -51.017  39.587  -13.102  1.00 37.82  ? 483 ASN D O   1 
ATOM   16571 C CB  . ASN D  1 483 ? -50.321  38.252  -10.386  1.00 37.84  ? 483 ASN D CB  1 
ATOM   16572 C CG  . ASN D  1 483 ? -50.520  38.027  -8.906   1.00 40.49  ? 483 ASN D CG  1 
ATOM   16573 O OD1 . ASN D  1 483 ? -49.676  38.446  -8.095   1.00 40.97  ? 483 ASN D OD1 1 
ATOM   16574 N ND2 . ASN D  1 483 ? -51.630  37.400  -8.541   1.00 39.97  ? 483 ASN D ND2 1 
ATOM   16575 N N   . PHE D  1 484 ? -49.243  40.774  -12.394  1.00 32.93  ? 484 PHE D N   1 
ATOM   16576 C CA  . PHE D  1 484 ? -48.846  41.277  -13.703  1.00 32.25  ? 484 PHE D CA  1 
ATOM   16577 C C   . PHE D  1 484 ? -47.595  40.563  -14.220  1.00 33.13  ? 484 PHE D C   1 
ATOM   16578 O O   . PHE D  1 484 ? -46.705  40.171  -13.450  1.00 32.94  ? 484 PHE D O   1 
ATOM   16579 C CB  . PHE D  1 484 ? -48.567  42.770  -13.551  1.00 31.86  ? 484 PHE D CB  1 
ATOM   16580 C CG  . PHE D  1 484 ? -49.769  43.559  -13.049  1.00 32.02  ? 484 PHE D CG  1 
ATOM   16581 C CD1 . PHE D  1 484 ? -50.015  43.704  -11.686  1.00 32.26  ? 484 PHE D CD1 1 
ATOM   16582 C CD2 . PHE D  1 484 ? -50.657  44.154  -13.956  1.00 32.01  ? 484 PHE D CD2 1 
ATOM   16583 C CE1 . PHE D  1 484 ? -51.122  44.441  -11.240  1.00 34.05  ? 484 PHE D CE1 1 
ATOM   16584 C CE2 . PHE D  1 484 ? -51.762  44.869  -13.509  1.00 33.29  ? 484 PHE D CE2 1 
ATOM   16585 C CZ  . PHE D  1 484 ? -51.988  45.027  -12.146  1.00 33.83  ? 484 PHE D CZ  1 
ATOM   16586 N N   . PHE D  1 485 ? -47.528  40.407  -15.549  1.00 33.67  ? 485 PHE D N   1 
ATOM   16587 C CA  . PHE D  1 485 ? -46.413  39.731  -16.185  1.00 33.01  ? 485 PHE D CA  1 
ATOM   16588 C C   . PHE D  1 485 ? -46.096  40.397  -17.502  1.00 33.24  ? 485 PHE D C   1 
ATOM   16589 O O   . PHE D  1 485 ? -47.039  40.750  -18.224  1.00 34.45  ? 485 PHE D O   1 
ATOM   16590 C CB  . PHE D  1 485 ? -46.774  38.294  -16.521  1.00 34.54  ? 485 PHE D CB  1 
ATOM   16591 C CG  . PHE D  1 485 ? -47.246  37.553  -15.292  1.00 33.78  ? 485 PHE D CG  1 
ATOM   16592 C CD1 . PHE D  1 485 ? -46.325  36.962  -14.440  1.00 33.33  ? 485 PHE D CD1 1 
ATOM   16593 C CD2 . PHE D  1 485 ? -48.596  37.515  -14.972  1.00 34.07  ? 485 PHE D CD2 1 
ATOM   16594 C CE1 . PHE D  1 485 ? -46.759  36.286  -13.313  1.00 34.53  ? 485 PHE D CE1 1 
ATOM   16595 C CE2 . PHE D  1 485 ? -49.026  36.828  -13.846  1.00 34.99  ? 485 PHE D CE2 1 
ATOM   16596 C CZ  . PHE D  1 485 ? -48.112  36.222  -13.016  1.00 33.91  ? 485 PHE D CZ  1 
ATOM   16597 N N   . ASN D  1 486 ? -44.784  40.564  -17.773  1.00 32.16  ? 486 ASN D N   1 
ATOM   16598 C CA  . ASN D  1 486 ? -44.309  41.040  -19.068  1.00 30.96  ? 486 ASN D CA  1 
ATOM   16599 C C   . ASN D  1 486 ? -44.531  39.974  -20.140  1.00 31.40  ? 486 ASN D C   1 
ATOM   16600 O O   . ASN D  1 486 ? -44.340  38.762  -19.913  1.00 30.19  ? 486 ASN D O   1 
ATOM   16601 C CB  . ASN D  1 486 ? -42.864  41.478  -18.954  1.00 31.00  ? 486 ASN D CB  1 
ATOM   16602 C CG  . ASN D  1 486 ? -42.791  42.789  -18.212  1.00 32.00  ? 486 ASN D CG  1 
ATOM   16603 O OD1 . ASN D  1 486 ? -42.120  42.881  -17.188  1.00 31.38  ? 486 ASN D OD1 1 
ATOM   16604 N ND2 . ASN D  1 486 ? -43.508  43.802  -18.685  1.00 32.55  ? 486 ASN D ND2 1 
ATOM   16605 N N   . ILE D  1 487 ? -45.041  40.408  -21.297  1.00 31.32  ? 487 ILE D N   1 
ATOM   16606 C CA  . ILE D  1 487 ? -45.264  39.455  -22.376  1.00 31.46  ? 487 ILE D CA  1 
ATOM   16607 C C   . ILE D  1 487 ? -44.072  39.560  -23.322  1.00 31.09  ? 487 ILE D C   1 
ATOM   16608 O O   . ILE D  1 487 ? -43.913  40.583  -23.961  1.00 30.54  ? 487 ILE D O   1 
ATOM   16609 C CB  . ILE D  1 487 ? -46.592  39.670  -23.130  1.00 31.97  ? 487 ILE D CB  1 
ATOM   16610 C CG1 . ILE D  1 487 ? -47.786  39.855  -22.187  1.00 32.05  ? 487 ILE D CG1 1 
ATOM   16611 C CG2 . ILE D  1 487 ? -46.822  38.527  -24.125  1.00 30.63  ? 487 ILE D CG2 1 
ATOM   16612 C CD1 . ILE D  1 487 ? -49.060  40.314  -22.865  1.00 31.45  ? 487 ILE D CD1 1 
ATOM   16613 N N   . PRO D  1 488 ? -43.237  38.501  -23.465  1.00 32.34  ? 488 PRO D N   1 
ATOM   16614 C CA  . PRO D  1 488 ? -42.131  38.518  -24.427  1.00 32.44  ? 488 PRO D CA  1 
ATOM   16615 C C   . PRO D  1 488 ? -42.692  38.678  -25.842  1.00 32.79  ? 488 PRO D C   1 
ATOM   16616 O O   . PRO D  1 488 ? -43.754  38.135  -26.160  1.00 30.80  ? 488 PRO D O   1 
ATOM   16617 C CB  . PRO D  1 488 ? -41.439  37.142  -24.213  1.00 31.81  ? 488 PRO D CB  1 
ATOM   16618 C CG  . PRO D  1 488 ? -41.974  36.638  -22.876  1.00 31.21  ? 488 PRO D CG  1 
ATOM   16619 C CD  . PRO D  1 488 ? -43.369  37.205  -22.769  1.00 30.75  ? 488 PRO D CD  1 
ATOM   16620 N N   . ASP D  1 489 ? -41.949  39.394  -26.697  1.00 33.81  ? 489 ASP D N   1 
ATOM   16621 C CA  . ASP D  1 489 ? -42.357  39.646  -28.075  1.00 34.63  ? 489 ASP D CA  1 
ATOM   16622 C C   . ASP D  1 489 ? -42.303  38.383  -28.927  1.00 33.76  ? 489 ASP D C   1 
ATOM   16623 O O   . ASP D  1 489 ? -42.993  38.306  -29.934  1.00 33.73  ? 489 ASP D O   1 
ATOM   16624 C CB  . ASP D  1 489 ? -41.491  40.691  -28.752  1.00 36.71  ? 489 ASP D CB  1 
ATOM   16625 C CG  . ASP D  1 489 ? -41.486  42.047  -28.071  1.00 40.04  ? 489 ASP D CG  1 
ATOM   16626 O OD1 . ASP D  1 489 ? -42.560  42.463  -27.637  1.00 37.23  ? 489 ASP D OD1 1 
ATOM   16627 O OD2 . ASP D  1 489 ? -40.396  42.671  -28.006  1.00 44.88  ? 489 ASP D OD2 1 
ATOM   16628 N N   . ASN D  1 490 ? -41.513  37.388  -28.516  1.00 33.92  ? 490 ASN D N   1 
ATOM   16629 C CA  . ASN D  1 490 ? -41.533  36.099  -29.179  1.00 35.64  ? 490 ASN D CA  1 
ATOM   16630 C C   . ASN D  1 490 ? -42.360  35.059  -28.393  1.00 33.51  ? 490 ASN D C   1 
ATOM   16631 O O   . ASN D  1 490 ? -42.163  33.853  -28.543  1.00 30.09  ? 490 ASN D O   1 
ATOM   16632 C CB  . ASN D  1 490 ? -40.096  35.731  -29.506  1.00 37.04  ? 490 ASN D CB  1 
ATOM   16633 C CG  . ASN D  1 490 ? -39.341  35.383  -28.255  1.00 40.02  ? 490 ASN D CG  1 
ATOM   16634 O OD1 . ASN D  1 490 ? -39.604  35.952  -27.177  1.00 39.05  ? 490 ASN D OD1 1 
ATOM   16635 N ND2 . ASN D  1 490 ? -38.433  34.425  -28.395  1.00 41.77  ? 490 ASN D ND2 1 
ATOM   16636 N N   . CYS D  1 491 ? -43.313  35.502  -27.557  1.00 32.49  ? 491 CYS D N   1 
ATOM   16637 C CA  . CYS D  1 491 ? -44.294  34.565  -27.022  1.00 31.26  ? 491 CYS D CA  1 
ATOM   16638 C C   . CYS D  1 491 ? -45.457  34.470  -27.992  1.00 30.42  ? 491 CYS D C   1 
ATOM   16639 O O   . CYS D  1 491 ? -46.064  35.508  -28.322  1.00 29.63  ? 491 CYS D O   1 
ATOM   16640 C CB  . CYS D  1 491 ? -44.872  34.972  -25.674  1.00 31.52  ? 491 CYS D CB  1 
ATOM   16641 S SG  . CYS D  1 491 ? -46.288  33.954  -25.181  1.00 30.41  ? 491 CYS D SG  1 
ATOM   16642 N N   . TRP D  1 492 ? -45.730  33.230  -28.439  1.00 27.69  ? 492 TRP D N   1 
ATOM   16643 C CA  . TRP D  1 492 ? -46.721  33.013  -29.476  1.00 28.30  ? 492 TRP D CA  1 
ATOM   16644 C C   . TRP D  1 492 ? -48.004  32.506  -28.852  1.00 27.99  ? 492 TRP D C   1 
ATOM   16645 O O   . TRP D  1 492 ? -49.089  32.685  -29.407  1.00 30.05  ? 492 TRP D O   1 
ATOM   16646 C CB  . TRP D  1 492 ? -46.203  32.027  -30.540  1.00 29.04  ? 492 TRP D CB  1 
ATOM   16647 C CG  . TRP D  1 492 ? -44.806  32.302  -31.041  1.00 28.97  ? 492 TRP D CG  1 
ATOM   16648 C CD1 . TRP D  1 492 ? -43.798  31.393  -31.042  1.00 29.52  ? 492 TRP D CD1 1 
ATOM   16649 C CD2 . TRP D  1 492 ? -44.271  33.501  -31.647  1.00 29.45  ? 492 TRP D CD2 1 
ATOM   16650 N NE1 . TRP D  1 492 ? -42.674  31.942  -31.574  1.00 31.62  ? 492 TRP D NE1 1 
ATOM   16651 C CE2 . TRP D  1 492 ? -42.919  33.229  -31.968  1.00 30.77  ? 492 TRP D CE2 1 
ATOM   16652 C CE3 . TRP D  1 492 ? -44.782  34.771  -31.944  1.00 30.53  ? 492 TRP D CE3 1 
ATOM   16653 C CZ2 . TRP D  1 492 ? -42.066  34.171  -32.561  1.00 30.86  ? 492 TRP D CZ2 1 
ATOM   16654 C CZ3 . TRP D  1 492 ? -43.939  35.722  -32.503  1.00 31.90  ? 492 TRP D CZ3 1 
ATOM   16655 C CH2 . TRP D  1 492 ? -42.596  35.421  -32.816  1.00 32.12  ? 492 TRP D CH2 1 
ATOM   16656 N N   . VAL D  1 493 ? -47.849  31.837  -27.710  1.00 27.63  ? 493 VAL D N   1 
ATOM   16657 C CA  . VAL D  1 493 ? -48.970  31.289  -26.973  1.00 27.59  ? 493 VAL D CA  1 
ATOM   16658 C C   . VAL D  1 493 ? -48.580  31.244  -25.504  1.00 26.59  ? 493 VAL D C   1 
ATOM   16659 O O   . VAL D  1 493 ? -47.422  30.983  -25.168  1.00 26.30  ? 493 VAL D O   1 
ATOM   16660 C CB  . VAL D  1 493 ? -49.349  29.889  -27.493  1.00 28.79  ? 493 VAL D CB  1 
ATOM   16661 C CG1 . VAL D  1 493 ? -48.131  28.954  -27.503  1.00 29.48  ? 493 VAL D CG1 1 
ATOM   16662 C CG2 . VAL D  1 493 ? -50.528  29.275  -26.738  1.00 27.47  ? 493 VAL D CG2 1 
ATOM   16663 N N   . VAL D  1 494 ? -49.574  31.476  -24.648  1.00 25.78  ? 494 VAL D N   1 
ATOM   16664 C CA  . VAL D  1 494 ? -49.395  31.364  -23.218  1.00 25.68  ? 494 VAL D CA  1 
ATOM   16665 C C   . VAL D  1 494 ? -50.501  30.481  -22.644  1.00 26.50  ? 494 VAL D C   1 
ATOM   16666 O O   . VAL D  1 494 ? -51.639  30.450  -23.131  1.00 26.60  ? 494 VAL D O   1 
ATOM   16667 C CB  . VAL D  1 494 ? -49.331  32.744  -22.540  1.00 25.88  ? 494 VAL D CB  1 
ATOM   16668 C CG1 . VAL D  1 494 ? -50.570  33.575  -22.790  1.00 27.23  ? 494 VAL D CG1 1 
ATOM   16669 C CG2 . VAL D  1 494 ? -49.083  32.653  -21.046  1.00 25.99  ? 494 VAL D CG2 1 
ATOM   16670 N N   . ASN D  1 495 ? -50.113  29.745  -21.596  1.00 26.68  ? 495 ASN D N   1 
ATOM   16671 C CA  . ASN D  1 495 ? -51.037  29.067  -20.707  1.00 26.56  ? 495 ASN D CA  1 
ATOM   16672 C C   . ASN D  1 495 ? -51.013  29.813  -19.396  1.00 26.16  ? 495 ASN D C   1 
ATOM   16673 O O   . ASN D  1 495 ? -50.005  29.760  -18.704  1.00 27.01  ? 495 ASN D O   1 
ATOM   16674 C CB  . ASN D  1 495 ? -50.586  27.634  -20.454  1.00 27.28  ? 495 ASN D CB  1 
ATOM   16675 C CG  . ASN D  1 495 ? -51.598  26.884  -19.638  1.00 28.02  ? 495 ASN D CG  1 
ATOM   16676 O OD1 . ASN D  1 495 ? -52.107  27.408  -18.637  1.00 28.85  ? 495 ASN D OD1 1 
ATOM   16677 N ND2 . ASN D  1 495 ? -51.919  25.682  -20.083  1.00 26.92  ? 495 ASN D ND2 1 
ATOM   16678 N N   . ALA D  1 496 ? -52.087  30.541  -19.096  1.00 26.90  ? 496 ALA D N   1 
ATOM   16679 C CA  . ALA D  1 496 ? -52.124  31.374  -17.914  1.00 27.11  ? 496 ALA D CA  1 
ATOM   16680 C C   . ALA D  1 496 ? -53.028  30.658  -16.935  1.00 27.52  ? 496 ALA D C   1 
ATOM   16681 O O   . ALA D  1 496 ? -54.108  30.227  -17.340  1.00 27.91  ? 496 ALA D O   1 
ATOM   16682 C CB  . ALA D  1 496 ? -52.634  32.752  -18.250  1.00 27.96  ? 496 ALA D CB  1 
ATOM   16683 N N   . SER D  1 497 ? -52.549  30.462  -15.703  1.00 27.16  ? 497 SER D N   1 
ATOM   16684 C CA  . SER D  1 497 ? -53.259  29.594  -14.779  1.00 28.45  ? 497 SER D CA  1 
ATOM   16685 C C   . SER D  1 497 ? -53.059  30.055  -13.341  1.00 28.73  ? 497 SER D C   1 
ATOM   16686 O O   . SER D  1 497 ? -52.120  30.788  -13.027  1.00 28.37  ? 497 SER D O   1 
ATOM   16687 C CB  . SER D  1 497 ? -52.870  28.117  -14.969  1.00 28.24  ? 497 SER D CB  1 
ATOM   16688 O OG  . SER D  1 497 ? -51.507  27.844  -14.684  1.00 27.97  ? 497 SER D OG  1 
ATOM   16689 N N   . ALA D  1 498 ? -53.962  29.609  -12.476  1.00 27.98  ? 498 ALA D N   1 
ATOM   16690 C CA  . ALA D  1 498 ? -53.812  29.825  -11.049  1.00 29.13  ? 498 ALA D CA  1 
ATOM   16691 C C   . ALA D  1 498 ? -54.500  28.698  -10.283  1.00 28.80  ? 498 ALA D C   1 
ATOM   16692 O O   . ALA D  1 498 ? -55.469  28.122  -10.760  1.00 28.78  ? 498 ALA D O   1 
ATOM   16693 C CB  . ALA D  1 498 ? -54.420  31.167  -10.704  1.00 30.72  ? 498 ALA D CB  1 
ATOM   16694 N N   . GLY D  1 499 ? -54.046  28.434  -9.061   1.00 29.17  ? 499 GLY D N   1 
ATOM   16695 C CA  . GLY D  1 499 ? -54.594  27.329  -8.289   1.00 29.20  ? 499 GLY D CA  1 
ATOM   16696 C C   . GLY D  1 499 ? -54.195  27.364  -6.815   1.00 29.77  ? 499 GLY D C   1 
ATOM   16697 O O   . GLY D  1 499 ? -53.188  27.973  -6.451   1.00 33.46  ? 499 GLY D O   1 
ATOM   16698 N N   . ILE D  1 500 ? -55.000  26.713  -5.975   1.00 28.41  ? 500 ILE D N   1 
ATOM   16699 C CA  . ILE D  1 500 ? -54.762  26.713  -4.548   1.00 29.85  ? 500 ILE D CA  1 
ATOM   16700 C C   . ILE D  1 500 ? -55.247  25.380  -3.997   1.00 31.38  ? 500 ILE D C   1 
ATOM   16701 O O   . ILE D  1 500 ? -56.203  24.801  -4.531   1.00 32.82  ? 500 ILE D O   1 
ATOM   16702 C CB  . ILE D  1 500 ? -55.429  27.913  -3.852   1.00 30.71  ? 500 ILE D CB  1 
ATOM   16703 C CG1 . ILE D  1 500 ? -54.855  28.120  -2.465   1.00 31.68  ? 500 ILE D CG1 1 
ATOM   16704 C CG2 . ILE D  1 500 ? -56.959  27.812  -3.829   1.00 30.84  ? 500 ILE D CG2 1 
ATOM   16705 C CD1 . ILE D  1 500 ? -55.379  29.363  -1.760   1.00 34.57  ? 500 ILE D CD1 1 
ATOM   16706 N N   . SER D  1 501 ? -54.555  24.897  -2.957   1.00 30.70  ? 501 SER D N   1 
ATOM   16707 C CA  . SER D  1 501 ? -54.905  23.628  -2.341   1.00 31.70  ? 501 SER D CA  1 
ATOM   16708 C C   . SER D  1 501 ? -56.094  23.829  -1.413   1.00 33.90  ? 501 SER D C   1 
ATOM   16709 O O   . SER D  1 501 ? -56.247  24.914  -0.861   1.00 36.60  ? 501 SER D O   1 
ATOM   16710 C CB  . SER D  1 501 ? -53.750  23.037  -1.600   1.00 30.48  ? 501 SER D CB  1 
ATOM   16711 O OG  . SER D  1 501 ? -52.731  22.739  -2.523   1.00 31.27  ? 501 SER D OG  1 
ATOM   16712 N N   . VAL D  1 502 ? -56.917  22.780  -1.262   1.00 34.26  ? 502 VAL D N   1 
ATOM   16713 C CA  . VAL D  1 502 ? -58.105  22.798  -0.424   1.00 36.09  ? 502 VAL D CA  1 
ATOM   16714 C C   . VAL D  1 502 ? -58.179  21.486  0.362    1.00 37.27  ? 502 VAL D C   1 
ATOM   16715 O O   . VAL D  1 502 ? -57.823  20.421  -0.149   1.00 35.51  ? 502 VAL D O   1 
ATOM   16716 C CB  . VAL D  1 502 ? -59.369  22.988  -1.289   1.00 38.63  ? 502 VAL D CB  1 
ATOM   16717 C CG1 . VAL D  1 502 ? -60.647  23.122  -0.458   1.00 39.49  ? 502 VAL D CG1 1 
ATOM   16718 C CG2 . VAL D  1 502 ? -59.248  24.184  -2.222   1.00 38.89  ? 502 VAL D CG2 1 
ATOM   16719 N N   . ARG D  1 503 ? -58.722  21.569  1.584    1.00 39.00  ? 503 ARG D N   1 
ATOM   16720 C CA  . ARG D  1 503 ? -58.819  20.425  2.476    1.00 38.60  ? 503 ARG D CA  1 
ATOM   16721 C C   . ARG D  1 503 ? -60.262  20.252  2.967    1.00 34.84  ? 503 ARG D C   1 
ATOM   16722 O O   . ARG D  1 503 ? -60.895  21.196  3.416    1.00 32.04  ? 503 ARG D O   1 
ATOM   16723 C CB  . ARG D  1 503 ? -57.830  20.576  3.639    1.00 42.02  ? 503 ARG D CB  1 
ATOM   16724 C CG  . ARG D  1 503 ? -57.926  19.485  4.702    1.00 47.71  ? 503 ARG D CG  1 
ATOM   16725 C CD  . ARG D  1 503 ? -56.978  19.678  5.888    1.00 53.12  ? 503 ARG D CD  1 
ATOM   16726 N NE  . ARG D  1 503 ? -55.570  19.642  5.455    1.00 61.18  ? 503 ARG D NE  1 
ATOM   16727 C CZ  . ARG D  1 503 ? -54.856  18.544  5.136    1.00 66.51  ? 503 ARG D CZ  1 
ATOM   16728 N NH1 . ARG D  1 503 ? -55.345  17.313  5.324    1.00 68.87  ? 503 ARG D NH1 1 
ATOM   16729 N NH2 . ARG D  1 503 ? -53.630  18.685  4.644    1.00 64.26  ? 503 ARG D NH2 1 
ATOM   16730 N N   . TYR D  1 504 ? -60.754  19.009  2.907    1.00 31.50  ? 504 TYR D N   1 
ATOM   16731 C CA  . TYR D  1 504 ? -61.931  18.586  3.655    1.00 30.66  ? 504 TYR D CA  1 
ATOM   16732 C C   . TYR D  1 504 ? -61.589  17.267  4.351    1.00 29.36  ? 504 TYR D C   1 
ATOM   16733 O O   . TYR D  1 504 ? -61.395  16.269  3.685    1.00 27.78  ? 504 TYR D O   1 
ATOM   16734 C CB  . TYR D  1 504 ? -63.144  18.456  2.723    1.00 30.70  ? 504 TYR D CB  1 
ATOM   16735 C CG  . TYR D  1 504 ? -64.479  18.248  3.428    1.00 32.19  ? 504 TYR D CG  1 
ATOM   16736 C CD1 . TYR D  1 504 ? -64.857  17.005  3.937    1.00 33.35  ? 504 TYR D CD1 1 
ATOM   16737 C CD2 . TYR D  1 504 ? -65.359  19.296  3.624    1.00 33.93  ? 504 TYR D CD2 1 
ATOM   16738 C CE1 . TYR D  1 504 ? -66.070  16.819  4.585    1.00 34.22  ? 504 TYR D CE1 1 
ATOM   16739 C CE2 . TYR D  1 504 ? -66.581  19.126  4.267    1.00 34.14  ? 504 TYR D CE2 1 
ATOM   16740 C CZ  . TYR D  1 504 ? -66.938  17.884  4.735    1.00 34.24  ? 504 TYR D CZ  1 
ATOM   16741 O OH  . TYR D  1 504 ? -68.125  17.737  5.352    1.00 35.46  ? 504 TYR D OH  1 
ATOM   16742 N N   . GLY D  1 505 ? -61.518  17.285  5.686    1.00 29.84  ? 505 GLY D N   1 
ATOM   16743 C CA  . GLY D  1 505 ? -60.995  16.209  6.488    1.00 30.41  ? 505 GLY D CA  1 
ATOM   16744 C C   . GLY D  1 505 ? -59.608  15.826  5.984    1.00 31.22  ? 505 GLY D C   1 
ATOM   16745 O O   . GLY D  1 505 ? -58.698  16.625  6.069    1.00 32.12  ? 505 GLY D O   1 
ATOM   16746 N N   . LYS D  1 506 ? -59.461  14.606  5.447    1.00 31.83  ? 506 LYS D N   1 
ATOM   16747 C CA  . LYS D  1 506 ? -58.184  14.119  4.950    1.00 30.49  ? 506 LYS D CA  1 
ATOM   16748 C C   . LYS D  1 506 ? -58.094  14.258  3.435    1.00 29.42  ? 506 LYS D C   1 
ATOM   16749 O O   . LYS D  1 506 ? -57.070  13.945  2.844    1.00 30.35  ? 506 LYS D O   1 
ATOM   16750 C CB  . LYS D  1 506 ? -58.047  12.632  5.280    1.00 30.42  ? 506 LYS D CB  1 
ATOM   16751 C CG  . LYS D  1 506 ? -58.198  12.218  6.738    1.00 31.45  ? 506 LYS D CG  1 
ATOM   16752 C CD  . LYS D  1 506 ? -58.040  10.699  6.834    1.00 31.74  ? 506 LYS D CD  1 
ATOM   16753 C CE  . LYS D  1 506 ? -58.287  10.114  8.174    1.00 32.78  ? 506 LYS D CE  1 
ATOM   16754 N NZ  . LYS D  1 506 ? -57.998  8.673   8.164    1.00 33.52  ? 506 LYS D NZ  1 
ATOM   16755 N N   . PHE D  1 507 ? -59.163  14.741  2.805    1.00 29.99  ? 507 PHE D N   1 
ATOM   16756 C CA  . PHE D  1 507 ? -59.191  14.935  1.367    1.00 29.11  ? 507 PHE D CA  1 
ATOM   16757 C C   . PHE D  1 507 ? -58.603  16.293  0.992    1.00 28.58  ? 507 PHE D C   1 
ATOM   16758 O O   . PHE D  1 507 ? -59.141  17.333  1.337    1.00 28.00  ? 507 PHE D O   1 
ATOM   16759 C CB  . PHE D  1 507 ? -60.655  14.826  0.954    1.00 29.22  ? 507 PHE D CB  1 
ATOM   16760 C CG  . PHE D  1 507 ? -60.900  14.805  -0.541   1.00 30.11  ? 507 PHE D CG  1 
ATOM   16761 C CD1 . PHE D  1 507 ? -60.923  15.993  -1.270   1.00 30.67  ? 507 PHE D CD1 1 
ATOM   16762 C CD2 . PHE D  1 507 ? -61.125  13.603  -1.211   1.00 30.02  ? 507 PHE D CD2 1 
ATOM   16763 C CE1 . PHE D  1 507 ? -61.153  15.978  -2.635   1.00 30.26  ? 507 PHE D CE1 1 
ATOM   16764 C CE2 . PHE D  1 507 ? -61.378  13.599  -2.572   1.00 29.48  ? 507 PHE D CE2 1 
ATOM   16765 C CZ  . PHE D  1 507 ? -61.415  14.784  -3.274   1.00 29.97  ? 507 PHE D CZ  1 
ATOM   16766 N N   . THR D  1 508 ? -57.536  16.273  0.204    1.00 30.29  ? 508 THR D N   1 
ATOM   16767 C CA  . THR D  1 508 ? -56.892  17.489  -0.271   1.00 32.63  ? 508 THR D CA  1 
ATOM   16768 C C   . THR D  1 508 ? -56.976  17.464  -1.786   1.00 31.06  ? 508 THR D C   1 
ATOM   16769 O O   . THR D  1 508 ? -56.688  16.438  -2.398   1.00 33.54  ? 508 THR D O   1 
ATOM   16770 C CB  . THR D  1 508 ? -55.429  17.581  0.203    1.00 35.75  ? 508 THR D CB  1 
ATOM   16771 O OG1 . THR D  1 508 ? -54.705  16.435  -0.264   1.00 42.60  ? 508 THR D OG1 1 
ATOM   16772 C CG2 . THR D  1 508 ? -55.266  17.581  1.714    1.00 34.92  ? 508 THR D CG2 1 
ATOM   16773 N N   . PHE D  1 509 ? -57.294  18.602  -2.383   1.00 29.65  ? 509 PHE D N   1 
ATOM   16774 C CA  . PHE D  1 509 ? -57.294  18.710  -3.826   1.00 30.22  ? 509 PHE D CA  1 
ATOM   16775 C C   . PHE D  1 509 ? -56.902  20.130  -4.221   1.00 33.10  ? 509 PHE D C   1 
ATOM   16776 O O   . PHE D  1 509 ? -56.685  20.976  -3.366   1.00 36.47  ? 509 PHE D O   1 
ATOM   16777 C CB  . PHE D  1 509 ? -58.693  18.308  -4.308   1.00 31.19  ? 509 PHE D CB  1 
ATOM   16778 C CG  . PHE D  1 509 ? -59.858  19.158  -3.828   1.00 30.59  ? 509 PHE D CG  1 
ATOM   16779 C CD1 . PHE D  1 509 ? -60.232  19.177  -2.491   1.00 32.41  ? 509 PHE D CD1 1 
ATOM   16780 C CD2 . PHE D  1 509 ? -60.589  19.929  -4.720   1.00 31.12  ? 509 PHE D CD2 1 
ATOM   16781 C CE1 . PHE D  1 509 ? -61.320  19.939  -2.070   1.00 35.51  ? 509 PHE D CE1 1 
ATOM   16782 C CE2 . PHE D  1 509 ? -61.678  20.699  -4.294   1.00 31.85  ? 509 PHE D CE2 1 
ATOM   16783 C CZ  . PHE D  1 509 ? -62.055  20.695  -2.973   1.00 33.78  ? 509 PHE D CZ  1 
ATOM   16784 N N   . LYS D  1 510 ? -56.860  20.417  -5.523   1.00 34.85  ? 510 LYS D N   1 
ATOM   16785 C CA  . LYS D  1 510 ? -56.634  21.787  -5.962   1.00 35.77  ? 510 LYS D CA  1 
ATOM   16786 C C   . LYS D  1 510 ? -57.847  22.312  -6.718   1.00 34.51  ? 510 LYS D C   1 
ATOM   16787 O O   . LYS D  1 510 ? -58.516  21.548  -7.408   1.00 34.10  ? 510 LYS D O   1 
ATOM   16788 C CB  . LYS D  1 510 ? -55.357  21.837  -6.811   1.00 38.17  ? 510 LYS D CB  1 
ATOM   16789 C CG  . LYS D  1 510 ? -54.091  21.547  -6.011   1.00 39.53  ? 510 LYS D CG  1 
ATOM   16790 C CD  . LYS D  1 510 ? -52.793  21.804  -6.759   1.00 43.97  ? 510 LYS D CD  1 
ATOM   16791 C CE  . LYS D  1 510 ? -51.693  22.369  -5.910   1.00 46.38  ? 510 LYS D CE  1 
ATOM   16792 N NZ  . LYS D  1 510 ? -51.986  23.795  -5.779   1.00 47.45  ? 510 LYS D NZ  1 
ATOM   16793 N N   . ILE D  1 511 ? -58.153  23.609  -6.531   1.00 32.39  ? 511 ILE D N   1 
ATOM   16794 C CA  . ILE D  1 511 ? -59.056  24.309  -7.420   1.00 31.25  ? 511 ILE D CA  1 
ATOM   16795 C C   . ILE D  1 511 ? -58.205  25.283  -8.217   1.00 32.75  ? 511 ILE D C   1 
ATOM   16796 O O   . ILE D  1 511 ? -57.213  25.799  -7.707   1.00 34.90  ? 511 ILE D O   1 
ATOM   16797 C CB  . ILE D  1 511 ? -60.213  25.007  -6.678   1.00 31.32  ? 511 ILE D CB  1 
ATOM   16798 C CG1 . ILE D  1 511 ? -59.703  26.102  -5.702   1.00 29.72  ? 511 ILE D CG1 1 
ATOM   16799 C CG2 . ILE D  1 511 ? -61.112  23.950  -6.012   1.00 31.01  ? 511 ILE D CG2 1 
ATOM   16800 C CD1 . ILE D  1 511 ? -60.774  26.761  -4.862   1.00 29.57  ? 511 ILE D CD1 1 
ATOM   16801 N N   . HIS D  1 512 ? -58.616  25.553  -9.454   1.00 32.21  ? 512 HIS D N   1 
ATOM   16802 C CA  . HIS D  1 512 ? -57.725  26.195  -10.397  1.00 32.90  ? 512 HIS D CA  1 
ATOM   16803 C C   . HIS D  1 512 ? -58.551  26.630  -11.598  1.00 33.34  ? 512 HIS D C   1 
ATOM   16804 O O   . HIS D  1 512 ? -59.658  26.132  -11.756  1.00 31.00  ? 512 HIS D O   1 
ATOM   16805 C CB  . HIS D  1 512 ? -56.655  25.190  -10.826  1.00 32.51  ? 512 HIS D CB  1 
ATOM   16806 C CG  . HIS D  1 512 ? -57.224  23.817  -11.017  1.00 35.09  ? 512 HIS D CG  1 
ATOM   16807 N ND1 . HIS D  1 512 ? -58.031  23.470  -12.079  1.00 33.65  ? 512 HIS D ND1 1 
ATOM   16808 C CD2 . HIS D  1 512 ? -57.149  22.727  -10.216  1.00 34.38  ? 512 HIS D CD2 1 
ATOM   16809 C CE1 . HIS D  1 512 ? -58.374  22.205  -11.931  1.00 35.96  ? 512 HIS D CE1 1 
ATOM   16810 N NE2 . HIS D  1 512 ? -57.833  21.736  -10.817  1.00 34.57  ? 512 HIS D NE2 1 
ATOM   16811 N N   . ASP D  1 513 ? -57.982  27.534  -12.416  1.00 33.36  ? 513 ASP D N   1 
ATOM   16812 C CA  . ASP D  1 513 ? -58.519  27.872  -13.737  1.00 32.10  ? 513 ASP D CA  1 
ATOM   16813 C C   . ASP D  1 513 ? -57.345  28.082  -14.706  1.00 30.67  ? 513 ASP D C   1 
ATOM   16814 O O   . ASP D  1 513 ? -56.201  28.187  -14.292  1.00 29.87  ? 513 ASP D O   1 
ATOM   16815 C CB  . ASP D  1 513 ? -59.492  29.035  -13.612  1.00 32.01  ? 513 ASP D CB  1 
ATOM   16816 C CG  . ASP D  1 513 ? -60.456  29.282  -14.764  1.00 32.47  ? 513 ASP D CG  1 
ATOM   16817 O OD1 . ASP D  1 513 ? -60.591  28.409  -15.629  1.00 33.49  ? 513 ASP D OD1 1 
ATOM   16818 O OD2 . ASP D  1 513 ? -61.067  30.367  -14.796  1.00 34.93  ? 513 ASP D OD2 1 
ATOM   16819 N N   . GLN D  1 514 ? -57.634  28.117  -16.008  1.00 30.96  ? 514 GLN D N   1 
ATOM   16820 C CA  . GLN D  1 514 ? -56.624  28.018  -17.047  1.00 30.80  ? 514 GLN D CA  1 
ATOM   16821 C C   . GLN D  1 514 ? -57.177  28.722  -18.274  1.00 31.87  ? 514 GLN D C   1 
ATOM   16822 O O   . GLN D  1 514 ? -58.313  28.501  -18.637  1.00 29.69  ? 514 GLN D O   1 
ATOM   16823 C CB  . GLN D  1 514 ? -56.331  26.557  -17.384  1.00 29.41  ? 514 GLN D CB  1 
ATOM   16824 C CG  . GLN D  1 514 ? -55.312  26.333  -18.498  1.00 29.43  ? 514 GLN D CG  1 
ATOM   16825 C CD  . GLN D  1 514 ? -55.226  24.896  -19.009  1.00 29.12  ? 514 GLN D CD  1 
ATOM   16826 O OE1 . GLN D  1 514 ? -54.235  24.187  -18.803  1.00 27.86  ? 514 GLN D OE1 1 
ATOM   16827 N NE2 . GLN D  1 514 ? -56.250  24.447  -19.726  1.00 28.83  ? 514 GLN D NE2 1 
ATOM   16828 N N   . LYS D  1 515 ? -56.380  29.589  -18.900  1.00 32.31  ? 515 LYS D N   1 
ATOM   16829 C CA  . LYS D  1 515 ? -56.742  30.133  -20.196  1.00 32.02  ? 515 LYS D CA  1 
ATOM   16830 C C   . LYS D  1 515 ? -55.553  29.967  -21.130  1.00 31.83  ? 515 LYS D C   1 
ATOM   16831 O O   . LYS D  1 515 ? -54.432  30.288  -20.728  1.00 33.44  ? 515 LYS D O   1 
ATOM   16832 C CB  . LYS D  1 515 ? -57.011  31.640  -20.164  1.00 32.03  ? 515 LYS D CB  1 
ATOM   16833 C CG  . LYS D  1 515 ? -58.064  32.079  -19.179  1.00 31.82  ? 515 LYS D CG  1 
ATOM   16834 C CD  . LYS D  1 515 ? -59.479  31.657  -19.540  1.00 30.62  ? 515 LYS D CD  1 
ATOM   16835 C CE  . LYS D  1 515 ? -60.348  32.021  -18.398  1.00 30.10  ? 515 LYS D CE  1 
ATOM   16836 N NZ  . LYS D  1 515 ? -61.644  31.409  -18.624  1.00 31.40  ? 515 LYS D NZ  1 
ATOM   16837 N N   . ILE D  1 516 ? -55.824  29.573  -22.382  1.00 30.44  ? 516 ILE D N   1 
ATOM   16838 C CA  . ILE D  1 516 ? -54.773  29.458  -23.376  1.00 30.10  ? 516 ILE D CA  1 
ATOM   16839 C C   . ILE D  1 516 ? -54.979  30.539  -24.426  1.00 29.29  ? 516 ILE D C   1 
ATOM   16840 O O   . ILE D  1 516 ? -56.008  30.608  -25.051  1.00 28.91  ? 516 ILE D O   1 
ATOM   16841 C CB  . ILE D  1 516 ? -54.755  28.036  -23.961  1.00 30.18  ? 516 ILE D CB  1 
ATOM   16842 C CG1 . ILE D  1 516 ? -54.378  27.048  -22.888  1.00 29.96  ? 516 ILE D CG1 1 
ATOM   16843 C CG2 . ILE D  1 516 ? -53.819  27.932  -25.155  1.00 30.86  ? 516 ILE D CG2 1 
ATOM   16844 C CD1 . ILE D  1 516 ? -54.515  25.597  -23.313  1.00 32.48  ? 516 ILE D CD1 1 
ATOM   16845 N N   . ILE D  1 517 ? -53.984  31.396  -24.608  1.00 30.65  ? 517 ILE D N   1 
ATOM   16846 C CA  . ILE D  1 517 ? -54.168  32.604  -25.390  1.00 32.20  ? 517 ILE D CA  1 
ATOM   16847 C C   . ILE D  1 517 ? -53.022  32.744  -26.380  1.00 31.85  ? 517 ILE D C   1 
ATOM   16848 O O   . ILE D  1 517 ? -51.857  32.587  -26.009  1.00 30.26  ? 517 ILE D O   1 
ATOM   16849 C CB  . ILE D  1 517 ? -54.275  33.824  -24.465  1.00 34.15  ? 517 ILE D CB  1 
ATOM   16850 C CG1 . ILE D  1 517 ? -55.394  33.609  -23.427  1.00 37.06  ? 517 ILE D CG1 1 
ATOM   16851 C CG2 . ILE D  1 517 ? -54.484  35.108  -25.270  1.00 35.23  ? 517 ILE D CG2 1 
ATOM   16852 C CD1 . ILE D  1 517 ? -55.420  34.608  -22.271  1.00 39.14  ? 517 ILE D CD1 1 
ATOM   16853 N N   . TYR D  1 518 ? -53.392  33.065  -27.626  1.00 31.21  ? 518 TYR D N   1 
ATOM   16854 C CA  . TYR D  1 518 ? -52.453  33.141  -28.722  1.00 31.19  ? 518 TYR D CA  1 
ATOM   16855 C C   . TYR D  1 518 ? -52.105  34.588  -29.085  1.00 32.56  ? 518 TYR D C   1 
ATOM   16856 O O   . TYR D  1 518 ? -52.879  35.529  -28.840  1.00 32.09  ? 518 TYR D O   1 
ATOM   16857 C CB  . TYR D  1 518 ? -53.127  32.474  -29.912  1.00 30.99  ? 518 TYR D CB  1 
ATOM   16858 C CG  . TYR D  1 518 ? -53.470  31.014  -29.719  1.00 31.61  ? 518 TYR D CG  1 
ATOM   16859 C CD1 . TYR D  1 518 ? -52.480  30.033  -29.687  1.00 31.45  ? 518 TYR D CD1 1 
ATOM   16860 C CD2 . TYR D  1 518 ? -54.795  30.609  -29.658  1.00 32.15  ? 518 TYR D CD2 1 
ATOM   16861 C CE1 . TYR D  1 518 ? -52.807  28.691  -29.566  1.00 29.95  ? 518 TYR D CE1 1 
ATOM   16862 C CE2 . TYR D  1 518 ? -55.129  29.276  -29.516  1.00 32.92  ? 518 TYR D CE2 1 
ATOM   16863 C CZ  . TYR D  1 518 ? -54.134  28.308  -29.477  1.00 30.69  ? 518 TYR D CZ  1 
ATOM   16864 O OH  . TYR D  1 518 ? -54.508  26.999  -29.321  1.00 28.18  ? 518 TYR D OH  1 
ATOM   16865 N N   . ARG D  1 519 ? -50.946  34.734  -29.740  1.00 30.94  ? 519 ARG D N   1 
ATOM   16866 C CA  . ARG D  1 519 ? -50.610  35.962  -30.439  1.00 31.35  ? 519 ARG D CA  1 
ATOM   16867 C C   . ARG D  1 519 ? -51.119  35.887  -31.881  1.00 32.73  ? 519 ARG D C   1 
ATOM   16868 O O   . ARG D  1 519 ? -50.672  35.045  -32.660  1.00 33.13  ? 519 ARG D O   1 
ATOM   16869 C CB  . ARG D  1 519 ? -49.095  36.218  -30.444  1.00 29.62  ? 519 ARG D CB  1 
ATOM   16870 C CG  . ARG D  1 519 ? -48.712  37.543  -31.086  1.00 29.21  ? 519 ARG D CG  1 
ATOM   16871 C CD  . ARG D  1 519 ? -47.194  37.686  -31.197  1.00 28.70  ? 519 ARG D CD  1 
ATOM   16872 N NE  . ARG D  1 519 ? -46.578  37.841  -29.876  1.00 28.74  ? 519 ARG D NE  1 
ATOM   16873 C CZ  . ARG D  1 519 ? -46.663  38.906  -29.092  1.00 29.07  ? 519 ARG D CZ  1 
ATOM   16874 N NH1 . ARG D  1 519 ? -47.210  40.028  -29.504  1.00 28.78  ? 519 ARG D NH1 1 
ATOM   16875 N NH2 . ARG D  1 519 ? -46.156  38.844  -27.883  1.00 29.88  ? 519 ARG D NH2 1 
ATOM   16876 N N   . GLY D  1 520 ? -51.995  36.823  -32.262  1.00 32.34  ? 520 GLY D N   1 
ATOM   16877 C CA  . GLY D  1 520 ? -52.525  36.871  -33.613  1.00 32.15  ? 520 GLY D CA  1 
ATOM   16878 C C   . GLY D  1 520 ? -53.187  35.554  -34.006  1.00 31.30  ? 520 GLY D C   1 
ATOM   16879 O O   . GLY D  1 520 ? -53.722  34.838  -33.166  1.00 29.90  ? 520 GLY D O   1 
ATOM   16880 N N   . ASP D  1 521 ? -53.125  35.248  -35.299  1.00 32.37  ? 521 ASP D N   1 
ATOM   16881 C CA  . ASP D  1 521 ? -53.916  34.175  -35.863  1.00 34.58  ? 521 ASP D CA  1 
ATOM   16882 C C   . ASP D  1 521 ? -53.013  32.993  -36.241  1.00 33.61  ? 521 ASP D C   1 
ATOM   16883 O O   . ASP D  1 521 ? -53.458  32.124  -36.977  1.00 35.70  ? 521 ASP D O   1 
ATOM   16884 C CB  . ASP D  1 521 ? -54.684  34.711  -37.065  1.00 37.92  ? 521 ASP D CB  1 
ATOM   16885 C CG  . ASP D  1 521 ? -53.748  35.089  -38.206  1.00 40.56  ? 521 ASP D CG  1 
ATOM   16886 O OD1 . ASP D  1 521 ? -52.527  34.958  -38.000  1.00 41.60  ? 521 ASP D OD1 1 
ATOM   16887 O OD2 . ASP D  1 521 ? -54.221  35.433  -39.304  1.00 43.99  ? 521 ASP D OD2 1 
ATOM   16888 N N   . TRP D  1 522 ? -51.775  32.918  -35.731  1.00 30.53  ? 522 TRP D N   1 
ATOM   16889 C CA  . TRP D  1 522 ? -50.811  31.963  -36.264  1.00 30.69  ? 522 TRP D CA  1 
ATOM   16890 C C   . TRP D  1 522 ? -51.295  30.528  -36.070  1.00 30.51  ? 522 TRP D C   1 
ATOM   16891 O O   . TRP D  1 522 ? -50.869  29.649  -36.805  1.00 31.91  ? 522 TRP D O   1 
ATOM   16892 C CB  . TRP D  1 522 ? -49.401  32.112  -35.649  1.00 29.91  ? 522 TRP D CB  1 
ATOM   16893 C CG  . TRP D  1 522 ? -49.272  31.554  -34.258  1.00 30.36  ? 522 TRP D CG  1 
ATOM   16894 C CD1 . TRP D  1 522 ? -49.683  32.157  -33.106  1.00 30.65  ? 522 TRP D CD1 1 
ATOM   16895 C CD2 . TRP D  1 522 ? -48.783  30.242  -33.867  1.00 31.92  ? 522 TRP D CD2 1 
ATOM   16896 N NE1 . TRP D  1 522 ? -49.486  31.337  -32.031  1.00 31.03  ? 522 TRP D NE1 1 
ATOM   16897 C CE2 . TRP D  1 522 ? -48.930  30.155  -32.462  1.00 30.49  ? 522 TRP D CE2 1 
ATOM   16898 C CE3 . TRP D  1 522 ? -48.218  29.162  -34.555  1.00 32.09  ? 522 TRP D CE3 1 
ATOM   16899 C CZ2 . TRP D  1 522 ? -48.535  29.035  -31.742  1.00 30.62  ? 522 TRP D CZ2 1 
ATOM   16900 C CZ3 . TRP D  1 522 ? -47.820  28.061  -33.836  1.00 32.24  ? 522 TRP D CZ3 1 
ATOM   16901 C CH2 . TRP D  1 522 ? -47.967  28.001  -32.450  1.00 31.64  ? 522 TRP D CH2 1 
ATOM   16902 N N   . ALA D  1 523 ? -52.100  30.285  -35.032  1.00 30.97  ? 523 ALA D N   1 
ATOM   16903 C CA  . ALA D  1 523 ? -52.509  28.936  -34.667  1.00 31.87  ? 523 ALA D CA  1 
ATOM   16904 C C   . ALA D  1 523 ? -53.898  28.594  -35.187  1.00 32.99  ? 523 ALA D C   1 
ATOM   16905 O O   . ALA D  1 523 ? -54.456  27.612  -34.718  1.00 31.45  ? 523 ALA D O   1 
ATOM   16906 C CB  . ALA D  1 523 ? -52.449  28.753  -33.168  1.00 31.20  ? 523 ALA D CB  1 
ATOM   16907 N N   . LYS D  1 524 ? -54.418  29.368  -36.160  1.00 35.99  ? 524 LYS D N   1 
ATOM   16908 C CA  . LYS D  1 524 ? -55.738  29.095  -36.716  1.00 40.56  ? 524 LYS D CA  1 
ATOM   16909 C C   . LYS D  1 524 ? -55.894  27.619  -37.136  1.00 37.82  ? 524 LYS D C   1 
ATOM   16910 O O   . LYS D  1 524 ? -56.985  27.092  -37.006  1.00 39.80  ? 524 LYS D O   1 
ATOM   16911 C CB  . LYS D  1 524 ? -56.209  30.106  -37.779  1.00 43.58  ? 524 LYS D CB  1 
ATOM   16912 C CG  . LYS D  1 524 ? -55.767  30.024  -39.241  1.00 50.16  ? 524 LYS D CG  1 
ATOM   16913 C CD  . LYS D  1 524 ? -56.284  31.208  -40.083  1.00 58.00  ? 524 LYS D CD  1 
ATOM   16914 C CE  . LYS D  1 524 ? -55.817  31.360  -41.543  1.00 61.04  ? 524 LYS D CE  1 
ATOM   16915 N NZ  . LYS D  1 524 ? -54.360  31.239  -41.746  1.00 60.69  ? 524 LYS D NZ  1 
ATOM   16916 N N   . GLU D  1 525 ? -54.836  26.930  -37.579  1.00 35.33  ? 525 GLU D N   1 
ATOM   16917 C CA  . GLU D  1 525 ? -54.942  25.530  -37.993  1.00 34.68  ? 525 GLU D CA  1 
ATOM   16918 C C   . GLU D  1 525 ? -54.429  24.600  -36.886  1.00 34.67  ? 525 GLU D C   1 
ATOM   16919 O O   . GLU D  1 525 ? -55.105  23.628  -36.560  1.00 34.99  ? 525 GLU D O   1 
ATOM   16920 C CB  . GLU D  1 525 ? -54.224  25.190  -39.304  1.00 33.91  ? 525 GLU D CB  1 
ATOM   16921 C CG  . GLU D  1 525 ? -54.505  26.157  -40.455  1.00 34.10  ? 525 GLU D CG  1 
ATOM   16922 C CD  . GLU D  1 525 ? -53.575  27.361  -40.652  1.00 34.67  ? 525 GLU D CD  1 
ATOM   16923 O OE1 . GLU D  1 525 ? -52.580  27.532  -39.906  1.00 33.67  ? 525 GLU D OE1 1 
ATOM   16924 O OE2 . GLU D  1 525 ? -53.836  28.142  -41.597  1.00 34.37  ? 525 GLU D OE2 1 
ATOM   16925 N N   . VAL D  1 526 ? -53.242  24.875  -36.297  1.00 33.08  ? 526 VAL D N   1 
ATOM   16926 C CA  . VAL D  1 526 ? -52.609  23.917  -35.394  1.00 31.08  ? 526 VAL D CA  1 
ATOM   16927 C C   . VAL D  1 526 ? -53.228  23.959  -33.989  1.00 31.09  ? 526 VAL D C   1 
ATOM   16928 O O   . VAL D  1 526 ? -53.142  22.963  -33.267  1.00 29.68  ? 526 VAL D O   1 
ATOM   16929 C CB  . VAL D  1 526 ? -51.062  24.029  -35.354  1.00 30.87  ? 526 VAL D CB  1 
ATOM   16930 C CG1 . VAL D  1 526 ? -50.556  25.358  -34.814  1.00 30.71  ? 526 VAL D CG1 1 
ATOM   16931 C CG2 . VAL D  1 526 ? -50.426  22.883  -34.579  1.00 30.27  ? 526 VAL D CG2 1 
ATOM   16932 N N   . GLY D  1 527 ? -53.859  25.073  -33.583  1.00 31.30  ? 527 GLY D N   1 
ATOM   16933 C CA  . GLY D  1 527 ? -54.350  25.205  -32.216  1.00 31.21  ? 527 GLY D CA  1 
ATOM   16934 C C   . GLY D  1 527 ? -55.733  24.583  -32.026  1.00 33.06  ? 527 GLY D C   1 
ATOM   16935 O O   . GLY D  1 527 ? -56.496  24.452  -32.968  1.00 34.10  ? 527 GLY D O   1 
ATOM   16936 N N   . ARG D  1 528 ? -56.065  24.190  -30.796  1.00 37.27  ? 528 ARG D N   1 
ATOM   16937 C CA  . ARG D  1 528 ? -57.328  23.515  -30.528  1.00 41.57  ? 528 ARG D CA  1 
ATOM   16938 C C   . ARG D  1 528 ? -58.492  24.485  -30.759  1.00 44.03  ? 528 ARG D C   1 
ATOM   16939 O O   . ARG D  1 528 ? -58.381  25.659  -30.421  1.00 42.00  ? 528 ARG D O   1 
ATOM   16940 C CB  . ARG D  1 528 ? -57.395  22.946  -29.104  1.00 41.26  ? 528 ARG D CB  1 
ATOM   16941 C CG  . ARG D  1 528 ? -58.629  22.078  -28.839  1.00 38.60  ? 528 ARG D CG  1 
ATOM   16942 C CD  . ARG D  1 528 ? -58.765  21.796  -27.339  1.00 36.34  ? 528 ARG D CD  1 
ATOM   16943 N NE  . ARG D  1 528 ? -57.700  20.945  -26.798  1.00 34.95  ? 528 ARG D NE  1 
ATOM   16944 C CZ  . ARG D  1 528 ? -56.564  21.327  -26.192  1.00 36.76  ? 528 ARG D CZ  1 
ATOM   16945 N NH1 . ARG D  1 528 ? -56.336  22.601  -25.932  1.00 36.80  ? 528 ARG D NH1 1 
ATOM   16946 N NH2 . ARG D  1 528 ? -55.646  20.428  -25.841  1.00 34.59  ? 528 ARG D NH2 1 
ATOM   16947 N N   . LYS D  1 529 ? -59.587  23.983  -31.350  1.00 47.64  ? 529 LYS D N   1 
ATOM   16948 C CA  . LYS D  1 529 ? -60.730  24.829  -31.664  1.00 61.01  ? 529 LYS D CA  1 
ATOM   16949 C C   . LYS D  1 529 ? -61.803  24.776  -30.553  1.00 59.76  ? 529 LYS D C   1 
ATOM   16950 O O   . LYS D  1 529 ? -61.974  23.672  -29.942  1.00 56.13  ? 529 LYS D O   1 
ATOM   16951 C CB  . LYS D  1 529 ? -61.360  24.409  -32.997  1.00 69.37  ? 529 LYS D CB  1 
ATOM   16952 C CG  . LYS D  1 529 ? -60.641  24.879  -34.253  1.00 69.18  ? 529 LYS D CG  1 
ATOM   16953 C CD  . LYS D  1 529 ? -59.569  23.905  -34.705  1.00 71.17  ? 529 LYS D CD  1 
ATOM   16954 C CE  . LYS D  1 529 ? -58.848  24.416  -35.910  1.00 69.72  ? 529 LYS D CE  1 
ATOM   16955 N NZ  . LYS D  1 529 ? -57.909  23.377  -36.337  1.00 71.10  ? 529 LYS D NZ  1 
HETATM 16956 C C2  . BGC E  2 .   ? -56.365  14.541  -77.146  1.00 27.05  ? 1   BGC E C2  1 
HETATM 16957 C C3  . BGC E  2 .   ? -55.278  14.955  -78.104  1.00 26.71  ? 1   BGC E C3  1 
HETATM 16958 C C4  . BGC E  2 .   ? -55.234  14.016  -79.264  1.00 26.56  ? 1   BGC E C4  1 
HETATM 16959 C C5  . BGC E  2 .   ? -56.588  13.937  -79.964  1.00 25.61  ? 1   BGC E C5  1 
HETATM 16960 C C6  . BGC E  2 .   ? -56.621  12.945  -81.115  1.00 23.54  ? 1   BGC E C6  1 
HETATM 16961 C C1  . BGC E  2 .   ? -57.698  14.392  -77.896  1.00 27.13  ? 1   BGC E C1  1 
HETATM 16962 O O1  . BGC E  2 .   ? -58.659  13.878  -77.042  1.00 22.97  ? 1   BGC E O1  1 
HETATM 16963 O O2  . BGC E  2 .   ? -56.519  15.452  -76.059  1.00 28.02  ? 1   BGC E O2  1 
HETATM 16964 O O3  . BGC E  2 .   ? -53.977  14.963  -77.500  1.00 30.83  ? 1   BGC E O3  1 
HETATM 16965 O O4  . BGC E  2 .   ? -54.243  14.448  -80.181  1.00 26.23  ? 1   BGC E O4  1 
HETATM 16966 O O5  . BGC E  2 .   ? -57.562  13.523  -79.015  1.00 24.99  ? 1   BGC E O5  1 
HETATM 16967 O O6  . BGC E  2 .   ? -56.349  11.618  -80.677  1.00 24.95  ? 1   BGC E O6  1 
HETATM 16968 C C2  . BGC E  2 .   ? -52.186  15.971  -76.301  1.00 33.35  ? 2   BGC E C2  1 
HETATM 16969 C C3  . BGC E  2 .   ? -51.530  17.342  -75.854  1.00 29.86  ? 2   BGC E C3  1 
HETATM 16970 C C4  . BGC E  2 .   ? -51.488  18.349  -77.002  1.00 29.11  ? 2   BGC E C4  1 
HETATM 16971 C C5  . BGC E  2 .   ? -52.837  18.421  -77.712  1.00 28.50  ? 2   BGC E C5  1 
HETATM 16972 C C6  . BGC E  2 .   ? -52.791  19.333  -78.906  1.00 28.62  ? 2   BGC E C6  1 
HETATM 16973 C C1  . BGC E  2 .   ? -53.484  16.206  -77.079  1.00 29.70  ? 2   BGC E C1  1 
HETATM 16974 O O2  . BGC E  2 .   ? -52.428  15.028  -75.230  1.00 26.78  ? 2   BGC E O2  1 
HETATM 16975 O O3  . BGC E  2 .   ? -50.191  17.134  -75.356  1.00 27.47  ? 2   BGC E O3  1 
HETATM 16976 O O4  . BGC E  2 .   ? -51.181  19.647  -76.507  1.00 27.91  ? 2   BGC E O4  1 
HETATM 16977 O O5  . BGC E  2 .   ? -53.223  17.080  -78.182  1.00 29.67  ? 2   BGC E O5  1 
HETATM 16978 O O6  . BGC E  2 .   ? -51.764  18.946  -79.871  1.00 30.23  ? 2   BGC E O6  1 
HETATM 16979 C C2  . BGC E  2 .   ? -48.731  16.488  -73.561  1.00 36.66  ? 3   BGC E C2  1 
HETATM 16980 C C3  . BGC E  2 .   ? -48.631  16.346  -72.069  1.00 36.96  ? 3   BGC E C3  1 
HETATM 16981 C C4  . BGC E  2 .   ? -49.272  17.548  -71.355  1.00 41.32  ? 3   BGC E C4  1 
HETATM 16982 C C5  . BGC E  2 .   ? -50.693  17.713  -71.824  1.00 39.06  ? 3   BGC E C5  1 
HETATM 16983 C C6  . BGC E  2 .   ? -51.494  18.828  -71.145  1.00 42.35  ? 3   BGC E C6  1 
HETATM 16984 C C1  . BGC E  2 .   ? -50.147  16.839  -73.996  1.00 33.26  ? 3   BGC E C1  1 
HETATM 16985 O O2  . BGC E  2 .   ? -48.274  15.347  -74.269  1.00 38.23  ? 3   BGC E O2  1 
HETATM 16986 O O3  . BGC E  2 .   ? -47.256  16.263  -71.737  1.00 36.79  ? 3   BGC E O3  1 
HETATM 16987 O O4  . BGC E  2 .   ? -49.310  17.391  -69.937  1.00 46.82  ? 3   BGC E O4  1 
HETATM 16988 O O5  . BGC E  2 .   ? -50.621  17.960  -73.247  1.00 37.53  ? 3   BGC E O5  1 
HETATM 16989 O O6  . BGC E  2 .   ? -51.156  20.145  -71.605  1.00 41.06  ? 3   BGC E O6  1 
HETATM 16990 C C2  . BGC F  2 .   ? -8.881   -4.717  -60.761  1.00 27.81  ? 1   BGC F C2  1 
HETATM 16991 C C3  . BGC F  2 .   ? -7.453   -4.253  -61.110  1.00 28.30  ? 1   BGC F C3  1 
HETATM 16992 C C4  . BGC F  2 .   ? -6.879   -5.178  -62.142  1.00 28.46  ? 1   BGC F C4  1 
HETATM 16993 C C5  . BGC F  2 .   ? -7.780   -5.226  -63.355  1.00 30.10  ? 1   BGC F C5  1 
HETATM 16994 C C6  . BGC F  2 .   ? -7.282   -6.207  -64.404  1.00 30.03  ? 1   BGC F C6  1 
HETATM 16995 C C1  . BGC F  2 .   ? -9.760   -4.828  -61.981  1.00 27.17  ? 1   BGC F C1  1 
HETATM 16996 O O1  . BGC F  2 .   ? -11.044  -5.342  -61.590  1.00 25.48  ? 1   BGC F O1  1 
HETATM 16997 O O2  . BGC F  2 .   ? -9.493   -3.845  -59.818  1.00 28.49  ? 1   BGC F O2  1 
HETATM 16998 O O3  . BGC F  2 .   ? -6.630   -4.258  -59.932  1.00 27.36  ? 1   BGC F O3  1 
HETATM 16999 O O4  . BGC F  2 .   ? -5.597   -4.739  -62.547  1.00 28.16  ? 1   BGC F O4  1 
HETATM 17000 O O5  . BGC F  2 .   ? -9.124   -5.627  -62.977  1.00 26.86  ? 1   BGC F O5  1 
HETATM 17001 O O6  . BGC F  2 .   ? -7.047   -7.521  -63.898  1.00 29.28  ? 1   BGC F O6  1 
HETATM 17002 C C2  . BGC F  2 .   ? -5.705   -3.239  -58.020  1.00 27.83  ? 2   BGC F C2  1 
HETATM 17003 C C3  . BGC F  2 .   ? -5.405   -1.919  -57.292  1.00 30.65  ? 2   BGC F C3  1 
HETATM 17004 C C4  . BGC F  2 .   ? -4.829   -0.894  -58.249  1.00 28.20  ? 2   BGC F C4  1 
HETATM 17005 C C5  . BGC F  2 .   ? -5.640   -0.801  -59.511  1.00 28.82  ? 2   BGC F C5  1 
HETATM 17006 C C6  . BGC F  2 .   ? -5.038   0.130   -60.547  1.00 33.49  ? 2   BGC F C6  1 
HETATM 17007 C C1  . BGC F  2 .   ? -6.457   -3.029  -59.314  1.00 29.14  ? 2   BGC F C1  1 
HETATM 17008 O O2  . BGC F  2 .   ? -6.454   -4.056  -57.142  1.00 24.28  ? 2   BGC F O2  1 
HETATM 17009 O O3  . BGC F  2 .   ? -4.486   -2.163  -56.167  1.00 33.46  ? 2   BGC F O3  1 
HETATM 17010 O O4  . BGC F  2 .   ? -4.785   0.387   -57.591  1.00 30.54  ? 2   BGC F O4  1 
HETATM 17011 O O5  . BGC F  2 .   ? -5.737   -2.109  -60.138  1.00 31.21  ? 2   BGC F O5  1 
HETATM 17012 O O6  . BGC F  2 .   ? -3.675   -0.206  -60.872  1.00 30.71  ? 2   BGC F O6  1 
HETATM 17013 C C2  . BGC F  2 .   ? -3.852   -2.692  -53.960  1.00 38.90  ? 3   BGC F C2  1 
HETATM 17014 C C3  . BGC F  2 .   ? -4.347   -2.845  -52.537  1.00 40.92  ? 3   BGC F C3  1 
HETATM 17015 C C4  . BGC F  2 .   ? -5.204   -1.670  -52.118  1.00 44.35  ? 3   BGC F C4  1 
HETATM 17016 C C5  . BGC F  2 .   ? -6.339   -1.441  -53.075  1.00 42.07  ? 3   BGC F C5  1 
HETATM 17017 C C6  . BGC F  2 .   ? -7.069   -0.141  -52.769  1.00 47.97  ? 3   BGC F C6  1 
HETATM 17018 C C1  . BGC F  2 .   ? -5.020   -2.432  -54.902  1.00 35.80  ? 3   BGC F C1  1 
HETATM 17019 O O2  . BGC F  2 .   ? -3.068   -3.794  -54.420  1.00 37.37  ? 3   BGC F O2  1 
HETATM 17020 O O3  . BGC F  2 .   ? -3.233   -2.904  -51.666  1.00 46.20  ? 3   BGC F O3  1 
HETATM 17021 O O4  . BGC F  2 .   ? -5.754   -1.880  -50.836  1.00 50.70  ? 3   BGC F O4  1 
HETATM 17022 O O5  . BGC F  2 .   ? -5.786   -1.329  -54.414  1.00 38.94  ? 3   BGC F O5  1 
HETATM 17023 O O6  . BGC F  2 .   ? -8.486   -0.185  -53.061  1.00 52.46  ? 3   BGC F O6  1 
HETATM 17024 C C2  . BGC G  2 .   ? -31.080  56.623  -55.877  1.00 25.02  ? 1   BGC G C2  1 
HETATM 17025 C C3  . BGC G  2 .   ? -32.244  56.147  -56.643  1.00 27.62  ? 1   BGC G C3  1 
HETATM 17026 C C4  . BGC G  2 .   ? -32.191  56.665  -58.055  1.00 27.27  ? 1   BGC G C4  1 
HETATM 17027 C C5  . BGC G  2 .   ? -30.841  56.315  -58.703  1.00 25.70  ? 1   BGC G C5  1 
HETATM 17028 C C6  . BGC G  2 .   ? -30.629  56.944  -60.059  1.00 27.61  ? 1   BGC G C6  1 
HETATM 17029 C C1  . BGC G  2 .   ? -29.787  56.251  -56.539  1.00 24.84  ? 1   BGC G C1  1 
HETATM 17030 O O1  . BGC G  2 .   ? -28.784  56.772  -55.747  1.00 24.23  ? 1   BGC G O1  1 
HETATM 17031 O O2  . BGC G  2 .   ? -31.119  56.063  -54.579  1.00 26.96  ? 1   BGC G O2  1 
HETATM 17032 O O3  . BGC G  2 .   ? -33.463  56.484  -55.958  1.00 32.47  ? 1   BGC G O3  1 
HETATM 17033 O O4  . BGC G  2 .   ? -33.241  56.028  -58.825  1.00 29.09  ? 1   BGC G O4  1 
HETATM 17034 O O5  . BGC G  2 .   ? -29.752  56.748  -57.874  1.00 26.46  ? 1   BGC G O5  1 
HETATM 17035 O O6  . BGC G  2 .   ? -30.852  58.375  -60.056  1.00 32.85  ? 1   BGC G O6  1 
HETATM 17036 C C2  . BGC G  2 .   ? -35.303  56.023  -54.582  1.00 34.33  ? 2   BGC G C2  1 
HETATM 17037 C C3  . BGC G  2 .   ? -36.123  54.989  -53.797  1.00 36.74  ? 2   BGC G C3  1 
HETATM 17038 C C4  . BGC G  2 .   ? -36.298  53.689  -54.596  1.00 37.06  ? 2   BGC G C4  1 
HETATM 17039 C C5  . BGC G  2 .   ? -34.957  53.232  -55.181  1.00 34.47  ? 2   BGC G C5  1 
HETATM 17040 C C6  . BGC G  2 .   ? -35.094  52.013  -56.051  1.00 31.43  ? 2   BGC G C6  1 
HETATM 17041 C C1  . BGC G  2 .   ? -34.033  55.448  -55.203  1.00 35.63  ? 2   BGC G C1  1 
HETATM 17042 O O2  . BGC G  2 .   ? -34.928  57.055  -53.694  1.00 39.06  ? 2   BGC G O2  1 
HETATM 17043 O O3  . BGC G  2 .   ? -37.417  55.509  -53.414  1.00 37.28  ? 2   BGC G O3  1 
HETATM 17044 O O4  . BGC G  2 .   ? -36.785  52.662  -53.715  1.00 36.21  ? 2   BGC G O4  1 
HETATM 17045 O O5  . BGC G  2 .   ? -34.352  54.283  -55.983  1.00 33.54  ? 2   BGC G O5  1 
HETATM 17046 O O6  . BGC G  2 .   ? -35.849  52.270  -57.211  1.00 32.65  ? 2   BGC G O6  1 
HETATM 17047 C C2  . BGC G  2 .   ? -38.939  56.723  -52.090  1.00 48.79  ? 3   BGC G C2  1 
HETATM 17048 C C3  . BGC G  2 .   ? -39.097  57.465  -50.761  1.00 50.01  ? 3   BGC G C3  1 
HETATM 17049 C C4  . BGC G  2 .   ? -38.666  56.582  -49.599  1.00 52.65  ? 3   BGC G C4  1 
HETATM 17050 C C5  . BGC G  2 .   ? -37.274  56.108  -49.812  1.00 49.24  ? 3   BGC G C5  1 
HETATM 17051 C C6  . BGC G  2 .   ? -36.715  55.311  -48.639  1.00 48.96  ? 3   BGC G C6  1 
HETATM 17052 C C1  . BGC G  2 .   ? -37.533  56.145  -52.178  1.00 41.43  ? 3   BGC G C1  1 
HETATM 17053 O O2  . BGC G  2 .   ? -39.221  57.515  -53.247  1.00 49.25  ? 3   BGC G O2  1 
HETATM 17054 O O3  . BGC G  2 .   ? -40.462  57.807  -50.589  1.00 59.68  ? 3   BGC G O3  1 
HETATM 17055 O O4  . BGC G  2 .   ? -38.666  57.258  -48.371  1.00 64.83  ? 3   BGC G O4  1 
HETATM 17056 O O5  . BGC G  2 .   ? -37.317  55.318  -51.033  1.00 45.90  ? 3   BGC G O5  1 
HETATM 17057 O O6  . BGC G  2 .   ? -36.570  53.910  -48.903  1.00 46.50  ? 3   BGC G O6  1 
HETATM 17058 C C2  . BGC H  2 .   ? -38.775  12.444  -24.195  1.00 22.95  ? 1   BGC H C2  1 
HETATM 17059 C C3  . BGC H  2 .   ? -37.367  11.887  -24.049  1.00 24.62  ? 1   BGC H C3  1 
HETATM 17060 C C4  . BGC H  2 .   ? -36.730  12.418  -22.806  1.00 24.86  ? 1   BGC H C4  1 
HETATM 17061 C C5  . BGC H  2 .   ? -37.597  12.116  -21.605  1.00 27.03  ? 1   BGC H C5  1 
HETATM 17062 C C6  . BGC H  2 .   ? -37.066  12.676  -20.304  1.00 29.63  ? 1   BGC H C6  1 
HETATM 17063 C C1  . BGC H  2 .   ? -39.578  12.151  -22.972  1.00 22.67  ? 1   BGC H C1  1 
HETATM 17064 O O1  . BGC H  2 .   ? -40.899  12.610  -23.075  1.00 23.04  ? 1   BGC H O1  1 
HETATM 17065 O O2  . BGC H  2 .   ? -39.386  11.879  -25.351  1.00 25.39  ? 1   BGC H O2  1 
HETATM 17066 O O3  . BGC H  2 .   ? -36.593  12.206  -25.209  1.00 25.33  ? 1   BGC H O3  1 
HETATM 17067 O O4  . BGC H  2 .   ? -35.471  11.831  -22.655  1.00 26.22  ? 1   BGC H O4  1 
HETATM 17068 O O5  . BGC H  2 .   ? -38.914  12.698  -21.832  1.00 23.80  ? 1   BGC H O5  1 
HETATM 17069 O O6  . BGC H  2 .   ? -37.068  14.118  -20.254  1.00 29.50  ? 1   BGC H O6  1 
HETATM 17070 C C2  . BGC H  2 .   ? -35.671  11.807  -27.339  1.00 29.85  ? 2   BGC H C2  1 
HETATM 17071 C C3  . BGC H  2 .   ? -35.420  10.766  -28.433  1.00 31.43  ? 2   BGC H C3  1 
HETATM 17072 C C4  . BGC H  2 .   ? -34.860  9.488   -27.843  1.00 27.68  ? 2   BGC H C4  1 
HETATM 17073 C C5  . BGC H  2 .   ? -35.700  9.006   -26.717  1.00 28.32  ? 2   BGC H C5  1 
HETATM 17074 C C6  . BGC H  2 .   ? -35.095  7.788   -26.053  1.00 29.81  ? 2   BGC H C6  1 
HETATM 17075 C C1  . BGC H  2 .   ? -36.488  11.228  -26.196  1.00 28.96  ? 2   BGC H C1  1 
HETATM 17076 O O2  . BGC H  2 .   ? -36.329  12.941  -27.899  1.00 29.52  ? 2   BGC H O2  1 
HETATM 17077 O O3  . BGC H  2 .   ? -34.487  11.284  -29.415  1.00 32.71  ? 2   BGC H O3  1 
HETATM 17078 O O4  . BGC H  2 .   ? -34.836  8.500   -28.874  1.00 29.97  ? 2   BGC H O4  1 
HETATM 17079 O O5  . BGC H  2 .   ? -35.852  10.043  -25.702  1.00 31.65  ? 2   BGC H O5  1 
HETATM 17080 O O6  . BGC H  2 .   ? -33.825  8.056   -25.453  1.00 28.33  ? 2   BGC H O6  1 
HETATM 17081 C C2  . BGC H  2 .   ? -33.781  12.577  -31.242  1.00 46.25  ? 3   BGC H C2  1 
HETATM 17082 C C3  . BGC H  2 .   ? -34.197  13.271  -32.501  1.00 45.99  ? 3   BGC H C3  1 
HETATM 17083 C C4  . BGC H  2 .   ? -35.042  12.351  -33.355  1.00 50.22  ? 3   BGC H C4  1 
HETATM 17084 C C5  . BGC H  2 .   ? -36.249  11.927  -32.536  1.00 48.90  ? 3   BGC H C5  1 
HETATM 17085 C C6  . BGC H  2 .   ? -37.304  11.135  -33.305  1.00 54.32  ? 3   BGC H C6  1 
HETATM 17086 C C1  . BGC H  2 .   ? -34.980  11.965  -30.521  1.00 40.76  ? 3   BGC H C1  1 
HETATM 17087 O O2  . BGC H  2 .   ? -33.061  13.487  -30.412  1.00 42.71  ? 3   BGC H O2  1 
HETATM 17088 O O3  . BGC H  2 .   ? -33.011  13.651  -33.157  1.00 54.11  ? 3   BGC H O3  1 
HETATM 17089 O O4  . BGC H  2 .   ? -35.446  13.024  -34.531  1.00 60.31  ? 3   BGC H O4  1 
HETATM 17090 O O5  . BGC H  2 .   ? -35.712  11.138  -31.429  1.00 43.58  ? 3   BGC H O5  1 
HETATM 17091 O O6  . BGC H  2 .   ? -37.297  9.712   -33.094  1.00 57.83  ? 3   BGC H O6  1 
HETATM 17092 C C1  . EDO I  3 .   ? -60.261  9.903   -85.669  1.00 34.61  ? 601 EDO A C1  1 
HETATM 17093 O O1  . EDO I  3 .   ? -60.058  10.249  -84.312  1.00 34.20  ? 601 EDO A O1  1 
HETATM 17094 C C2  . EDO I  3 .   ? -59.019  9.831   -86.502  1.00 36.86  ? 601 EDO A C2  1 
HETATM 17095 O O2  . EDO I  3 .   ? -59.277  9.542   -87.868  1.00 37.14  ? 601 EDO A O2  1 
HETATM 17096 C C2  . BGC J  4 .   ? -57.367  7.456   -79.400  0.75 42.34  ? 602 BGC A C2  1 
HETATM 17097 C C3  . BGC J  4 .   ? -55.993  8.179   -79.417  0.75 41.64  ? 602 BGC A C3  1 
HETATM 17098 C C4  . BGC J  4 .   ? -54.883  7.242   -79.009  0.75 44.60  ? 602 BGC A C4  1 
HETATM 17099 C C5  . BGC J  4 .   ? -54.802  6.125   -80.040  0.75 46.26  ? 602 BGC A C5  1 
HETATM 17100 C C6  . BGC J  4 .   ? -53.702  5.133   -79.690  0.75 42.29  ? 602 BGC A C6  1 
HETATM 17101 C C1  . BGC J  4 .   ? -57.315  6.252   -80.353  0.75 41.74  ? 602 BGC A C1  1 
HETATM 17102 O O1  . BGC J  4 .   ? -58.522  5.521   -80.213  0.75 32.13  ? 602 BGC A O1  1 
HETATM 17103 O O2  . BGC J  4 .   ? -58.524  8.278   -79.671  0.75 34.55  ? 602 BGC A O2  1 
HETATM 17104 O O3  . BGC J  4 .   ? -55.959  9.270   -78.513  0.75 47.20  ? 602 BGC A O3  1 
HETATM 17105 O O4  . BGC J  4 .   ? -53.608  7.927   -78.868  0.75 39.63  ? 602 BGC A O4  1 
HETATM 17106 O O5  . BGC J  4 .   ? -56.127  5.419   -80.122  0.75 50.13  ? 602 BGC A O5  1 
HETATM 17107 O O6  . BGC J  4 .   ? -53.548  4.115   -80.677  0.75 45.24  ? 602 BGC A O6  1 
HETATM 17108 C C1  . GOL K  5 .   ? -69.857  8.992   -90.212  1.00 61.66  ? 603 GOL A C1  1 
HETATM 17109 O O1  . GOL K  5 .   ? -68.859  9.851   -90.759  1.00 48.90  ? 603 GOL A O1  1 
HETATM 17110 C C2  . GOL K  5 .   ? -69.373  8.360   -88.919  1.00 58.12  ? 603 GOL A C2  1 
HETATM 17111 O O2  . GOL K  5 .   ? -68.455  9.258   -88.310  1.00 46.07  ? 603 GOL A O2  1 
HETATM 17112 C C3  . GOL K  5 .   ? -68.698  7.014   -89.080  1.00 55.06  ? 603 GOL A C3  1 
HETATM 17113 O O3  . GOL K  5 .   ? -68.675  6.308   -87.839  1.00 61.93  ? 603 GOL A O3  1 
HETATM 17114 C C1  . EDO L  3 .   ? -31.549  -0.531  -68.145  1.00 44.22  ? 601 EDO B C1  1 
HETATM 17115 O O1  . EDO L  3 .   ? -30.992  -0.720  -69.472  1.00 34.06  ? 601 EDO B O1  1 
HETATM 17116 C C2  . EDO L  3 .   ? -32.888  0.190   -68.088  1.00 48.56  ? 601 EDO B C2  1 
HETATM 17117 O O2  . EDO L  3 .   ? -32.947  1.420   -68.880  1.00 42.67  ? 601 EDO B O2  1 
HETATM 17118 C C2  . BGC M  4 .   ? -8.571   -11.727 -63.035  0.75 43.87  ? 602 BGC B C2  1 
HETATM 17119 C C3  . BGC M  4 .   ? -7.473   -10.854 -62.334  0.75 42.26  ? 602 BGC B C3  1 
HETATM 17120 C C4  . BGC M  4 .   ? -6.445   -11.696 -61.553  0.75 45.59  ? 602 BGC B C4  1 
HETATM 17121 C C5  . BGC M  4 .   ? -5.856   -12.818 -62.441  0.75 45.93  ? 602 BGC B C5  1 
HETATM 17122 C C6  . BGC M  4 .   ? -4.964   -13.763 -61.663  0.75 45.74  ? 602 BGC B C6  1 
HETATM 17123 C C1  . BGC M  4 .   ? -7.915   -12.895 -63.842  0.75 45.99  ? 602 BGC B C1  1 
HETATM 17124 O O1  . BGC M  4 .   ? -8.893   -13.753 -64.354  0.75 34.25  ? 602 BGC B O1  1 
HETATM 17125 O O2  . BGC M  4 .   ? -9.475   -10.984 -63.889  0.75 35.30  ? 602 BGC B O2  1 
HETATM 17126 O O3  . BGC M  4 .   ? -8.082   -9.883  -61.470  0.75 49.88  ? 602 BGC B O3  1 
HETATM 17127 O O4  . BGC M  4 .   ? -5.337   -10.901 -61.026  0.75 38.61  ? 602 BGC B O4  1 
HETATM 17128 O O5  . BGC M  4 .   ? -6.920   -13.637 -63.061  0.75 50.48  ? 602 BGC B O5  1 
HETATM 17129 O O6  . BGC M  4 .   ? -4.677   -14.944 -62.426  0.75 49.41  ? 602 BGC B O6  1 
HETATM 17130 C C1  . GOL N  5 .   ? -26.639  -14.226 -75.487  1.00 47.58  ? 603 GOL B C1  1 
HETATM 17131 O O1  . GOL N  5 .   ? -27.422  -15.156 -74.720  1.00 46.22  ? 603 GOL B O1  1 
HETATM 17132 C C2  . GOL N  5 .   ? -25.183  -14.639 -75.505  1.00 48.01  ? 603 GOL B C2  1 
HETATM 17133 O O2  . GOL N  5 .   ? -24.633  -14.597 -76.838  1.00 47.18  ? 603 GOL B O2  1 
HETATM 17134 C C3  . GOL N  5 .   ? -24.384  -13.855 -74.482  1.00 41.50  ? 603 GOL B C3  1 
HETATM 17135 O O3  . GOL N  5 .   ? -24.705  -14.247 -73.140  1.00 34.91  ? 603 GOL B O3  1 
HETATM 17136 C C1  . EDO O  3 .   ? -7.447   -9.952  -70.507  1.00 42.47  ? 604 EDO B C1  1 
HETATM 17137 O O1  . EDO O  3 .   ? -6.213   -9.765  -71.093  1.00 33.47  ? 604 EDO B O1  1 
HETATM 17138 C C2  . EDO O  3 .   ? -7.630   -9.259  -69.240  1.00 42.64  ? 604 EDO B C2  1 
HETATM 17139 O O2  . EDO O  3 .   ? -8.978   -9.151  -68.887  1.00 37.17  ? 604 EDO B O2  1 
HETATM 17140 C C1  . GOL P  5 .   ? -29.828  -5.500  -93.959  1.00 47.13  ? 605 GOL B C1  1 
HETATM 17141 O O1  . GOL P  5 .   ? -29.433  -4.873  -95.194  1.00 45.79  ? 605 GOL B O1  1 
HETATM 17142 C C2  . GOL P  5 .   ? -29.523  -6.983  -93.867  1.00 44.07  ? 605 GOL B C2  1 
HETATM 17143 O O2  . GOL P  5 .   ? -29.196  -7.345  -92.528  1.00 48.98  ? 605 GOL B O2  1 
HETATM 17144 C C3  . GOL P  5 .   ? -30.643  -7.893  -94.318  1.00 47.12  ? 605 GOL B C3  1 
HETATM 17145 O O3  . GOL P  5 .   ? -30.210  -9.250  -94.488  1.00 40.18  ? 605 GOL B O3  1 
HETATM 17146 C C1  . GOL Q  5 .   ? -4.374   -8.123  -59.600  1.00 62.11  ? 606 GOL B C1  1 
HETATM 17147 O O1  . GOL Q  5 .   ? -5.770   -8.373  -59.383  1.00 52.52  ? 606 GOL B O1  1 
HETATM 17148 C C2  . GOL Q  5 .   ? -3.933   -6.773  -59.060  1.00 61.47  ? 606 GOL B C2  1 
HETATM 17149 O O2  . GOL Q  5 .   ? -3.981   -6.790  -57.636  1.00 64.74  ? 606 GOL B O2  1 
HETATM 17150 C C3  . GOL Q  5 .   ? -2.550   -6.313  -59.489  1.00 60.65  ? 606 GOL B C3  1 
HETATM 17151 O O3  . GOL Q  5 .   ? -2.289   -4.976  -59.037  1.00 51.38  ? 606 GOL B O3  1 
HETATM 17152 C C1  . EDO R  3 .   ? -27.403  58.118  -64.776  1.00 43.31  ? 601 EDO C C1  1 
HETATM 17153 O O1  . EDO R  3 .   ? -26.379  58.234  -63.808  1.00 40.48  ? 601 EDO C O1  1 
HETATM 17154 C C2  . EDO R  3 .   ? -26.997  58.364  -66.170  1.00 39.05  ? 601 EDO C C2  1 
HETATM 17155 O O2  . EDO R  3 .   ? -28.018  58.129  -67.094  1.00 33.86  ? 601 EDO C O2  1 
HETATM 17156 C C1  . PGE S  6 .   ? -37.349  58.441  -58.117  1.00 58.96  ? 602 PGE C C1  1 
HETATM 17157 O O1  . PGE S  6 .   ? -37.783  57.237  -57.462  1.00 52.47  ? 602 PGE C O1  1 
HETATM 17158 C C2  . PGE S  6 .   ? -35.949  58.844  -57.738  1.00 54.21  ? 602 PGE C C2  1 
HETATM 17159 O O2  . PGE S  6 .   ? -35.894  60.230  -57.407  1.00 57.73  ? 602 PGE C O2  1 
HETATM 17160 C C3  . PGE S  6 .   ? -34.728  60.621  -56.674  1.00 55.98  ? 602 PGE C C3  1 
HETATM 17161 C C4  . PGE S  6 .   ? -33.534  60.897  -57.596  1.00 57.38  ? 602 PGE C C4  1 
HETATM 17162 O O4  . PGE S  6 .   ? -31.340  63.341  -60.604  1.00 63.85  ? 602 PGE C O4  1 
HETATM 17163 C C6  . PGE S  6 .   ? -31.765  62.410  -59.607  1.00 63.37  ? 602 PGE C C6  1 
HETATM 17164 C C5  . PGE S  6 .   ? -33.199  62.708  -59.201  1.00 63.30  ? 602 PGE C C5  1 
HETATM 17165 O O3  . PGE S  6 .   ? -33.922  61.527  -58.826  1.00 66.86  ? 602 PGE C O3  1 
HETATM 17166 C C1  . GOL T  5 .   ? -8.481   51.497  -50.053  1.00 51.74  ? 603 GOL C C1  1 
HETATM 17167 O O1  . GOL T  5 .   ? -7.955   50.995  -51.280  1.00 43.74  ? 603 GOL C O1  1 
HETATM 17168 C C2  . GOL T  5 .   ? -7.451   51.471  -48.940  1.00 56.83  ? 603 GOL C C2  1 
HETATM 17169 O O2  . GOL T  5 .   ? -8.063   51.008  -47.731  1.00 54.41  ? 603 GOL C O2  1 
HETATM 17170 C C3  . GOL T  5 .   ? -6.237   50.631  -49.281  1.00 59.89  ? 603 GOL C C3  1 
HETATM 17171 O O3  . GOL T  5 .   ? -6.616   49.293  -49.602  1.00 58.37  ? 603 GOL C O3  1 
HETATM 17172 C C2  . BGC U  4 .   ? -38.683  18.181  -20.029  1.00 59.20  ? 601 BGC D C2  1 
HETATM 17173 C C3  . BGC U  4 .   ? -37.661  17.477  -20.908  1.00 54.12  ? 601 BGC D C3  1 
HETATM 17174 C C4  . BGC U  4 .   ? -36.657  18.484  -21.439  1.00 53.59  ? 601 BGC D C4  1 
HETATM 17175 C C5  . BGC U  4 .   ? -36.012  19.216  -20.275  1.00 61.81  ? 601 BGC D C5  1 
HETATM 17176 C C6  . BGC U  4 .   ? -35.015  20.260  -20.715  1.00 61.50  ? 601 BGC D C6  1 
HETATM 17177 C C1  . BGC U  4 .   ? -37.999  19.008  -18.949  1.00 63.58  ? 601 BGC D C1  1 
HETATM 17178 O O1  . BGC U  4 .   ? -38.931  19.748  -18.239  1.00 42.58  ? 601 BGC D O1  1 
HETATM 17179 O O2  . BGC U  4 .   ? -39.587  17.255  -19.438  1.00 41.72  ? 601 BGC D O2  1 
HETATM 17180 O O3  . BGC U  4 .   ? -38.311  16.788  -21.978  1.00 47.32  ? 601 BGC D O3  1 
HETATM 17181 O O4  . BGC U  4 .   ? -35.637  17.831  -22.180  1.00 51.86  ? 601 BGC D O4  1 
HETATM 17182 O O5  . BGC U  4 .   ? -37.033  19.895  -19.523  1.00 62.05  ? 601 BGC D O5  1 
HETATM 17183 O O6  . BGC U  4 .   ? -34.543  21.021  -19.609  1.00 61.28  ? 601 BGC D O6  1 
HETATM 17184 C C1  . GOL V  5 .   ? -60.109  17.185  -8.441   1.00 45.87  ? 602 GOL D C1  1 
HETATM 17185 O O1  . GOL V  5 .   ? -59.320  16.186  -9.084   1.00 39.90  ? 602 GOL D O1  1 
HETATM 17186 C C2  . GOL V  5 .   ? -60.988  17.885  -9.460   1.00 55.44  ? 602 GOL D C2  1 
HETATM 17187 O O2  . GOL V  5 .   ? -60.778  19.300  -9.427   1.00 52.21  ? 602 GOL D O2  1 
HETATM 17188 C C3  . GOL V  5 .   ? -62.451  17.565  -9.279   1.00 59.73  ? 602 GOL D C3  1 
HETATM 17189 O O3  . GOL V  5 .   ? -62.600  16.301  -8.643   1.00 61.62  ? 602 GOL D O3  1 
HETATM 17190 C C1  . EDO W  3 .   ? -36.636  13.980  -13.956  1.00 37.01  ? 603 EDO D C1  1 
HETATM 17191 O O1  . EDO W  3 .   ? -36.152  13.961  -12.633  1.00 32.84  ? 603 EDO D O1  1 
HETATM 17192 C C2  . EDO W  3 .   ? -38.127  14.141  -14.043  1.00 37.46  ? 603 EDO D C2  1 
HETATM 17193 O O2  . EDO W  3 .   ? -38.579  14.129  -15.381  1.00 37.28  ? 603 EDO D O2  1 
HETATM 17194 C C1  . GOL X  5 .   ? -43.735  15.589  -7.045   1.00 54.86  ? 604 GOL D C1  1 
HETATM 17195 O O1  . GOL X  5 .   ? -44.668  16.677  -7.196   1.00 51.23  ? 604 GOL D O1  1 
HETATM 17196 C C2  . GOL X  5 .   ? -44.294  14.313  -6.443   1.00 49.35  ? 604 GOL D C2  1 
HETATM 17197 O O2  . GOL X  5 .   ? -45.724  14.380  -6.383   1.00 56.62  ? 604 GOL D O2  1 
HETATM 17198 C C3  . GOL X  5 .   ? -43.850  13.065  -7.187   1.00 48.32  ? 604 GOL D C3  1 
HETATM 17199 O O3  . GOL X  5 .   ? -43.507  11.991  -6.300   1.00 44.22  ? 604 GOL D O3  1 
HETATM 17200 C C1  . GOL Y  5 .   ? -45.415  41.567  -10.368  1.00 59.88  ? 605 GOL D C1  1 
HETATM 17201 O O1  . GOL Y  5 .   ? -44.559  42.332  -9.531   1.00 51.21  ? 605 GOL D O1  1 
HETATM 17202 C C2  . GOL Y  5 .   ? -46.455  40.814  -9.554   1.00 58.07  ? 605 GOL D C2  1 
HETATM 17203 O O2  . GOL Y  5 .   ? -47.721  41.440  -9.734   1.00 42.76  ? 605 GOL D O2  1 
HETATM 17204 C C3  . GOL Y  5 .   ? -46.558  39.330  -9.889   1.00 53.12  ? 605 GOL D C3  1 
HETATM 17205 O O3  . GOL Y  5 .   ? -46.921  38.567  -8.738   1.00 58.43  ? 605 GOL D O3  1 
HETATM 17206 C C1  . GOL Z  5 .   ? -48.692  -6.128  -0.980   1.00 64.53  ? 606 GOL D C1  1 
HETATM 17207 O O1  . GOL Z  5 .   ? -48.885  -5.217  0.099    1.00 61.94  ? 606 GOL D O1  1 
HETATM 17208 C C2  . GOL Z  5 .   ? -47.322  -6.770  -0.964   1.00 63.74  ? 606 GOL D C2  1 
HETATM 17209 O O2  . GOL Z  5 .   ? -46.332  -5.787  -0.670   1.00 57.65  ? 606 GOL D O2  1 
HETATM 17210 C C3  . GOL Z  5 .   ? -47.220  -7.922  0.014    1.00 65.09  ? 606 GOL D C3  1 
HETATM 17211 O O3  . GOL Z  5 .   ? -45.899  -8.054  0.527    1.00 66.39  ? 606 GOL D O3  1 
HETATM 17212 C C1  . GOL AA 5 .   ? -58.799  4.178   -38.191  1.00 65.99  ? 607 GOL D C1  1 
HETATM 17213 O O1  . GOL AA 5 .   ? -58.422  4.616   -39.495  1.00 61.23  ? 607 GOL D O1  1 
HETATM 17214 C C2  . GOL AA 5 .   ? -57.654  3.459   -37.507  1.00 65.10  ? 607 GOL D C2  1 
HETATM 17215 O O2  . GOL AA 5 .   ? -57.149  2.433   -38.362  1.00 70.71  ? 607 GOL D O2  1 
HETATM 17216 C C3  . GOL AA 5 .   ? -58.038  2.888   -36.163  1.00 63.13  ? 607 GOL D C3  1 
HETATM 17217 O O3  . GOL AA 5 .   ? -58.374  3.946   -35.272  1.00 63.96  ? 607 GOL D O3  1 
HETATM 17218 O O   . HOH BA 7 .   ? -82.757  23.629  -71.761  1.00 40.16  ? 701 HOH A O   1 
HETATM 17219 O O   . HOH BA 7 .   ? -43.758  14.698  -87.399  1.00 22.42  ? 702 HOH A O   1 
HETATM 17220 O O   . HOH BA 7 .   ? -76.536  -4.679  -85.988  1.00 29.60  ? 703 HOH A O   1 
HETATM 17221 O O   . HOH BA 7 .   ? -58.097  11.702  -75.998  1.00 30.84  ? 704 HOH A O   1 
HETATM 17222 O O   . HOH BA 7 .   ? -58.777  -7.690  -72.873  1.00 31.83  ? 705 HOH A O   1 
HETATM 17223 O O   . HOH BA 7 .   ? -42.163  11.240  -58.477  1.00 35.10  ? 706 HOH A O   1 
HETATM 17224 O O   . HOH BA 7 .   ? -67.264  33.590  -85.047  1.00 32.50  ? 707 HOH A O   1 
HETATM 17225 O O   . HOH BA 7 .   ? -62.445  2.162   -86.415  1.00 20.06  ? 708 HOH A O   1 
HETATM 17226 O O   . HOH BA 7 .   ? -58.663  3.584   -81.710  1.00 35.86  ? 709 HOH A O   1 
HETATM 17227 O O   . HOH BA 7 .   ? -67.016  19.382  -96.650  1.00 34.49  ? 710 HOH A O   1 
HETATM 17228 O O   . HOH BA 7 .   ? -76.986  20.324  -91.735  1.00 30.05  ? 711 HOH A O   1 
HETATM 17229 O O   . HOH BA 7 .   ? -70.035  31.569  -82.844  1.00 28.12  ? 712 HOH A O   1 
HETATM 17230 O O   . HOH BA 7 .   ? -58.270  25.909  -98.403  1.00 36.10  ? 713 HOH A O   1 
HETATM 17231 O O   . HOH BA 7 .   ? -78.364  33.082  -75.670  1.00 28.71  ? 714 HOH A O   1 
HETATM 17232 O O   . HOH BA 7 .   ? -72.171  -17.594 -68.500  1.00 31.25  ? 715 HOH A O   1 
HETATM 17233 O O   . HOH BA 7 .   ? -54.676  1.562   -56.838  1.00 34.61  ? 716 HOH A O   1 
HETATM 17234 O O   . HOH BA 7 .   ? -77.649  21.317  -85.283  1.00 25.62  ? 717 HOH A O   1 
HETATM 17235 O O   . HOH BA 7 .   ? -73.811  -12.498 -75.115  1.00 33.22  ? 718 HOH A O   1 
HETATM 17236 O O   . HOH BA 7 .   ? -66.438  9.155   -66.250  1.00 33.36  ? 719 HOH A O   1 
HETATM 17237 O O   . HOH BA 7 .   ? -81.672  2.411   -77.134  1.00 25.33  ? 720 HOH A O   1 
HETATM 17238 O O   . HOH BA 7 .   ? -77.537  11.359  -83.621  1.00 27.16  ? 721 HOH A O   1 
HETATM 17239 O O   . HOH BA 7 .   ? -59.895  5.284   -55.699  1.00 41.74  ? 722 HOH A O   1 
HETATM 17240 O O   . HOH BA 7 .   ? -81.702  34.540  -77.676  1.00 30.85  ? 723 HOH A O   1 
HETATM 17241 O O   . HOH BA 7 .   ? -64.132  -4.329  -76.573  1.00 26.65  ? 724 HOH A O   1 
HETATM 17242 O O   . HOH BA 7 .   ? -64.959  -0.056  -86.784  1.00 40.40  ? 725 HOH A O   1 
HETATM 17243 O O   . HOH BA 7 .   ? -63.120  15.947  -71.150  1.00 38.46  ? 726 HOH A O   1 
HETATM 17244 O O   . HOH BA 7 .   ? -79.328  4.454   -80.401  1.00 35.95  ? 727 HOH A O   1 
HETATM 17245 O O   . HOH BA 7 .   ? -76.705  34.840  -95.400  1.00 34.72  ? 728 HOH A O   1 
HETATM 17246 O O   . HOH BA 7 .   ? -53.976  28.421  -72.836  1.00 25.21  ? 729 HOH A O   1 
HETATM 17247 O O   . HOH BA 7 .   ? -48.940  8.433   -55.209  1.00 40.22  ? 730 HOH A O   1 
HETATM 17248 O O   . HOH BA 7 .   ? -66.467  9.698   -91.668  1.00 20.49  ? 731 HOH A O   1 
HETATM 17249 O O   . HOH BA 7 .   ? -80.386  35.023  -85.172  1.00 26.70  ? 732 HOH A O   1 
HETATM 17250 O O   . HOH BA 7 .   ? -64.567  8.144   -90.619  1.00 28.40  ? 733 HOH A O   1 
HETATM 17251 O O   . HOH BA 7 .   ? -71.997  13.800  -92.112  1.00 32.58  ? 734 HOH A O   1 
HETATM 17252 O O   . HOH BA 7 .   ? -66.820  -9.728  -65.755  1.00 21.80  ? 735 HOH A O   1 
HETATM 17253 O O   . HOH BA 7 .   ? -77.803  -11.314 -87.134  1.00 31.64  ? 736 HOH A O   1 
HETATM 17254 O O   . HOH BA 7 .   ? -69.636  35.250  -77.518  1.00 28.17  ? 737 HOH A O   1 
HETATM 17255 O O   . HOH BA 7 .   ? -65.288  34.723  -67.243  1.00 25.93  ? 738 HOH A O   1 
HETATM 17256 O O   . HOH BA 7 .   ? -66.496  21.764  -57.762  1.00 29.24  ? 739 HOH A O   1 
HETATM 17257 O O   . HOH BA 7 .   ? -68.496  -10.437 -58.604  1.00 37.24  ? 740 HOH A O   1 
HETATM 17258 O O   . HOH BA 7 .   ? -44.058  25.338  -60.297  1.00 29.69  ? 741 HOH A O   1 
HETATM 17259 O O   . HOH BA 7 .   ? -79.123  37.141  -92.331  1.00 28.15  ? 742 HOH A O   1 
HETATM 17260 O O   . HOH BA 7 .   ? -50.129  24.500  -85.985  1.00 25.14  ? 743 HOH A O   1 
HETATM 17261 O O   . HOH BA 7 .   ? -73.536  32.837  -90.243  1.00 36.81  ? 744 HOH A O   1 
HETATM 17262 O O   . HOH BA 7 .   ? -52.278  13.787  -54.671  1.00 30.49  ? 745 HOH A O   1 
HETATM 17263 O O   . HOH BA 7 .   ? -46.804  28.818  -83.541  1.00 28.74  ? 746 HOH A O   1 
HETATM 17264 O O   . HOH BA 7 .   ? -77.362  16.495  -88.620  1.00 26.91  ? 747 HOH A O   1 
HETATM 17265 O O   . HOH BA 7 .   ? -95.227  15.846  -100.178 1.00 23.75  ? 748 HOH A O   1 
HETATM 17266 O O   . HOH BA 7 .   ? -49.940  8.986   -84.478  1.00 26.79  ? 749 HOH A O   1 
HETATM 17267 O O   . HOH BA 7 .   ? -56.814  4.742   -53.596  1.00 28.70  ? 750 HOH A O   1 
HETATM 17268 O O   . HOH BA 7 .   ? -76.568  0.747   -72.609  1.00 28.32  ? 751 HOH A O   1 
HETATM 17269 O O   . HOH BA 7 .   ? -58.607  0.955   -73.374  1.00 31.43  ? 752 HOH A O   1 
HETATM 17270 O O   . HOH BA 7 .   ? -81.368  21.496  -73.230  1.00 28.85  ? 753 HOH A O   1 
HETATM 17271 O O   . HOH BA 7 .   ? -62.378  42.311  -80.812  1.00 41.21  ? 754 HOH A O   1 
HETATM 17272 O O   . HOH BA 7 .   ? -58.624  6.362   -66.913  1.00 31.20  ? 755 HOH A O   1 
HETATM 17273 O O   . HOH BA 7 .   ? -43.158  12.451  -86.825  1.00 29.55  ? 756 HOH A O   1 
HETATM 17274 O O   . HOH BA 7 .   ? -60.196  5.021   -78.272  1.00 27.10  ? 757 HOH A O   1 
HETATM 17275 O O   . HOH BA 7 .   ? -52.949  7.973   -98.666  1.00 37.89  ? 758 HOH A O   1 
HETATM 17276 O O   . HOH BA 7 .   ? -60.161  6.381   -96.237  1.00 25.71  ? 759 HOH A O   1 
HETATM 17277 O O   . HOH BA 7 .   ? -68.609  2.981   -61.006  1.00 26.32  ? 760 HOH A O   1 
HETATM 17278 O O   . HOH BA 7 .   ? -47.439  21.339  -87.461  1.00 25.25  ? 761 HOH A O   1 
HETATM 17279 O O   . HOH BA 7 .   ? -71.720  13.581  -68.764  1.00 28.75  ? 762 HOH A O   1 
HETATM 17280 O O   . HOH BA 7 .   ? -67.497  -3.505  -59.768  1.00 30.96  ? 763 HOH A O   1 
HETATM 17281 O O   . HOH BA 7 .   ? -47.964  35.374  -61.996  1.00 36.90  ? 764 HOH A O   1 
HETATM 17282 O O   . HOH BA 7 .   ? -50.886  20.818  -82.914  1.00 23.24  ? 765 HOH A O   1 
HETATM 17283 O O   . HOH BA 7 .   ? -90.324  20.316  -98.816  1.00 27.88  ? 766 HOH A O   1 
HETATM 17284 O O   . HOH BA 7 .   ? -85.072  -0.764  -75.229  1.00 30.46  ? 767 HOH A O   1 
HETATM 17285 O O   . HOH BA 7 .   ? -53.902  12.805  -96.657  1.00 29.41  ? 768 HOH A O   1 
HETATM 17286 O O   . HOH BA 7 .   ? -75.424  33.735  -81.273  1.00 34.97  ? 769 HOH A O   1 
HETATM 17287 O O   . HOH BA 7 .   ? -49.519  26.289  -83.758  1.00 23.35  ? 770 HOH A O   1 
HETATM 17288 O O   . HOH BA 7 .   ? -69.157  17.350  -94.657  1.00 35.44  ? 771 HOH A O   1 
HETATM 17289 O O   . HOH BA 7 .   ? -80.901  11.409  -71.136  1.00 36.19  ? 772 HOH A O   1 
HETATM 17290 O O   . HOH BA 7 .   ? -90.145  15.258  -93.702  1.00 34.72  ? 773 HOH A O   1 
HETATM 17291 O O   . HOH BA 7 .   ? -74.107  0.969   -67.229  1.00 32.88  ? 774 HOH A O   1 
HETATM 17292 O O   . HOH BA 7 .   ? -82.134  32.567  -81.832  1.00 27.91  ? 775 HOH A O   1 
HETATM 17293 O O   . HOH BA 7 .   ? -70.483  4.296   -84.053  1.00 36.08  ? 776 HOH A O   1 
HETATM 17294 O O   . HOH BA 7 .   ? -52.479  17.792  -68.306  1.00 31.02  ? 777 HOH A O   1 
HETATM 17295 O O   . HOH BA 7 .   ? -50.164  22.960  -76.057  1.00 22.32  ? 778 HOH A O   1 
HETATM 17296 O O   . HOH BA 7 .   ? -44.245  27.963  -61.315  1.00 31.05  ? 779 HOH A O   1 
HETATM 17297 O O   . HOH BA 7 .   ? -47.545  18.687  -97.961  1.00 22.14  ? 780 HOH A O   1 
HETATM 17298 O O   . HOH BA 7 .   ? -73.972  25.970  -72.217  1.00 24.98  ? 781 HOH A O   1 
HETATM 17299 O O   . HOH BA 7 .   ? -61.490  -8.697  -54.568  1.00 33.21  ? 782 HOH A O   1 
HETATM 17300 O O   . HOH BA 7 .   ? -72.585  -6.262  -63.440  1.00 28.65  ? 783 HOH A O   1 
HETATM 17301 O O   . HOH BA 7 .   ? -88.366  11.497  -94.879  1.00 32.38  ? 784 HOH A O   1 
HETATM 17302 O O   . HOH BA 7 .   ? -78.088  -17.243 -82.785  1.00 33.32  ? 785 HOH A O   1 
HETATM 17303 O O   . HOH BA 7 .   ? -67.872  24.264  -82.105  1.00 24.27  ? 786 HOH A O   1 
HETATM 17304 O O   . HOH BA 7 .   ? -47.837  38.668  -65.793  1.00 27.44  ? 787 HOH A O   1 
HETATM 17305 O O   . HOH BA 7 .   ? -52.500  27.528  -89.157  1.00 29.19  ? 788 HOH A O   1 
HETATM 17306 O O   . HOH BA 7 .   ? -58.549  10.070  -81.660  1.00 26.86  ? 789 HOH A O   1 
HETATM 17307 O O   . HOH BA 7 .   ? -49.884  18.823  -94.764  1.00 24.41  ? 790 HOH A O   1 
HETATM 17308 O O   . HOH BA 7 .   ? -72.789  -13.578 -67.316  1.00 26.76  ? 791 HOH A O   1 
HETATM 17309 O O   . HOH BA 7 .   ? -57.552  -12.663 -64.448  1.00 35.92  ? 792 HOH A O   1 
HETATM 17310 O O   . HOH BA 7 .   ? -55.765  -0.302  -67.179  1.00 31.34  ? 793 HOH A O   1 
HETATM 17311 O O   . HOH BA 7 .   ? -48.954  3.033   -66.056  1.00 27.94  ? 794 HOH A O   1 
HETATM 17312 O O   . HOH BA 7 .   ? -62.792  37.824  -75.319  1.00 25.83  ? 795 HOH A O   1 
HETATM 17313 O O   . HOH BA 7 .   ? -58.428  10.070  -69.068  1.00 32.56  ? 796 HOH A O   1 
HETATM 17314 O O   . HOH BA 7 .   ? -67.240  38.208  -76.621  1.00 35.98  ? 797 HOH A O   1 
HETATM 17315 O O   . HOH BA 7 .   ? -64.683  11.122  -83.766  1.00 22.04  ? 798 HOH A O   1 
HETATM 17316 O O   . HOH BA 7 .   ? -97.561  -11.934 -83.580  1.00 41.74  ? 799 HOH A O   1 
HETATM 17317 O O   . HOH BA 7 .   ? -69.152  33.781  -62.655  1.00 41.90  ? 800 HOH A O   1 
HETATM 17318 O O   . HOH BA 7 .   ? -53.172  27.535  -77.576  1.00 27.36  ? 801 HOH A O   1 
HETATM 17319 O O   . HOH BA 7 .   ? -75.251  28.924  -83.550  1.00 22.90  ? 802 HOH A O   1 
HETATM 17320 O O   . HOH BA 7 .   ? -83.292  7.768   -89.605  1.00 32.00  ? 803 HOH A O   1 
HETATM 17321 O O   . HOH BA 7 .   ? -87.939  17.729  -77.719  1.00 34.69  ? 804 HOH A O   1 
HETATM 17322 O O   . HOH BA 7 .   ? -77.719  18.922  -75.912  1.00 28.39  ? 805 HOH A O   1 
HETATM 17323 O O   . HOH BA 7 .   ? -75.629  16.308  -67.416  1.00 29.21  ? 806 HOH A O   1 
HETATM 17324 O O   . HOH BA 7 .   ? -75.037  34.093  -65.906  1.00 32.05  ? 807 HOH A O   1 
HETATM 17325 O O   . HOH BA 7 .   ? -46.618  20.070  -62.548  1.00 22.85  ? 808 HOH A O   1 
HETATM 17326 O O   . HOH BA 7 .   ? -77.360  -1.547  -66.825  1.00 30.50  ? 809 HOH A O   1 
HETATM 17327 O O   . HOH BA 7 .   ? -62.198  4.339   -80.025  1.00 28.07  ? 810 HOH A O   1 
HETATM 17328 O O   . HOH BA 7 .   ? -59.394  3.266   -76.340  1.00 25.17  ? 811 HOH A O   1 
HETATM 17329 O O   . HOH BA 7 .   ? -51.970  23.240  -83.918  1.00 26.62  ? 812 HOH A O   1 
HETATM 17330 O O   . HOH BA 7 .   ? -65.125  26.277  -89.093  1.00 24.00  ? 813 HOH A O   1 
HETATM 17331 O O   . HOH BA 7 .   ? -63.198  29.107  -60.081  1.00 32.90  ? 814 HOH A O   1 
HETATM 17332 O O   . HOH BA 7 .   ? -56.344  3.106   -55.868  1.00 30.85  ? 815 HOH A O   1 
HETATM 17333 O O   . HOH BA 7 .   ? -67.014  36.371  -70.879  1.00 38.90  ? 816 HOH A O   1 
HETATM 17334 O O   . HOH BA 7 .   ? -57.405  -5.304  -77.090  1.00 34.68  ? 817 HOH A O   1 
HETATM 17335 O O   . HOH BA 7 .   ? -67.119  34.902  -78.345  1.00 24.22  ? 818 HOH A O   1 
HETATM 17336 O O   . HOH BA 7 .   ? -60.622  19.951  -78.823  1.00 28.79  ? 819 HOH A O   1 
HETATM 17337 O O   . HOH BA 7 .   ? -56.924  3.152   -70.234  1.00 52.66  ? 820 HOH A O   1 
HETATM 17338 O O   . HOH BA 7 .   ? -56.184  -3.861  -57.964  1.00 47.94  ? 821 HOH A O   1 
HETATM 17339 O O   . HOH BA 7 .   ? -52.489  16.912  -85.994  1.00 26.30  ? 822 HOH A O   1 
HETATM 17340 O O   . HOH BA 7 .   ? -53.633  -2.166  -66.862  1.00 30.26  ? 823 HOH A O   1 
HETATM 17341 O O   . HOH BA 7 .   ? -70.764  10.300  -85.408  1.00 21.26  ? 824 HOH A O   1 
HETATM 17342 O O   . HOH BA 7 .   ? -62.548  -0.609  -57.149  1.00 35.83  ? 825 HOH A O   1 
HETATM 17343 O O   . HOH BA 7 .   ? -67.882  -2.075  -73.955  1.00 25.41  ? 826 HOH A O   1 
HETATM 17344 O O   . HOH BA 7 .   ? -63.681  36.244  -61.102  1.00 43.63  ? 827 HOH A O   1 
HETATM 17345 O O   . HOH BA 7 .   ? -69.487  11.254  -62.284  1.00 30.73  ? 828 HOH A O   1 
HETATM 17346 O O   . HOH BA 7 .   ? -51.095  7.148   -82.943  1.00 37.65  ? 829 HOH A O   1 
HETATM 17347 O O   . HOH BA 7 .   ? -72.740  4.642   -71.734  1.00 24.07  ? 830 HOH A O   1 
HETATM 17348 O O   . HOH BA 7 .   ? -54.216  2.206   -68.740  1.00 31.45  ? 831 HOH A O   1 
HETATM 17349 O O   . HOH BA 7 .   ? -60.699  16.493  -87.121  1.00 29.58  ? 832 HOH A O   1 
HETATM 17350 O O   . HOH BA 7 .   ? -53.391  -12.002 -67.424  1.00 32.82  ? 833 HOH A O   1 
HETATM 17351 O O   . HOH BA 7 .   ? -65.967  35.907  -64.867  1.00 25.90  ? 834 HOH A O   1 
HETATM 17352 O O   . HOH BA 7 .   ? -65.526  40.090  -72.109  1.00 34.00  ? 835 HOH A O   1 
HETATM 17353 O O   . HOH BA 7 .   ? -79.433  14.582  -88.639  1.00 34.63  ? 836 HOH A O   1 
HETATM 17354 O O   . HOH BA 7 .   ? -44.834  30.695  -94.113  1.00 31.17  ? 837 HOH A O   1 
HETATM 17355 O O   . HOH BA 7 .   ? -83.945  -7.767  -72.217  1.00 35.76  ? 838 HOH A O   1 
HETATM 17356 O O   . HOH BA 7 .   ? -70.818  29.853  -88.362  1.00 32.34  ? 839 HOH A O   1 
HETATM 17357 O O   . HOH BA 7 .   ? -45.717  35.090  -63.680  1.00 34.90  ? 840 HOH A O   1 
HETATM 17358 O O   . HOH BA 7 .   ? -71.780  30.419  -86.212  1.00 31.54  ? 841 HOH A O   1 
HETATM 17359 O O   . HOH BA 7 .   ? -84.856  22.314  -98.044  1.00 30.50  ? 842 HOH A O   1 
HETATM 17360 O O   . HOH BA 7 .   ? -60.882  7.650   -78.292  1.00 24.71  ? 843 HOH A O   1 
HETATM 17361 O O   . HOH BA 7 .   ? -62.041  40.836  -67.811  1.00 28.18  ? 844 HOH A O   1 
HETATM 17362 O O   . HOH BA 7 .   ? -47.804  4.421   -64.131  1.00 27.05  ? 845 HOH A O   1 
HETATM 17363 O O   . HOH BA 7 .   ? -58.091  -1.903  -66.485  1.00 35.84  ? 846 HOH A O   1 
HETATM 17364 O O   . HOH BA 7 .   ? -72.415  21.734  -93.181  1.00 31.25  ? 847 HOH A O   1 
HETATM 17365 O O   . HOH BA 7 .   ? -61.859  17.963  -94.624  1.00 25.62  ? 848 HOH A O   1 
HETATM 17366 O O   . HOH BA 7 .   ? -63.676  36.426  -64.029  1.00 39.89  ? 849 HOH A O   1 
HETATM 17367 O O   . HOH BA 7 .   ? -84.356  20.602  -94.270  1.00 26.87  ? 850 HOH A O   1 
HETATM 17368 O O   . HOH BA 7 .   ? -45.378  20.690  -84.971  1.00 29.51  ? 851 HOH A O   1 
HETATM 17369 O O   . HOH BA 7 .   ? -67.681  10.383  -96.199  1.00 29.99  ? 852 HOH A O   1 
HETATM 17370 O O   . HOH BA 7 .   ? -68.312  -14.259 -59.950  1.00 35.27  ? 853 HOH A O   1 
HETATM 17371 O O   . HOH BA 7 .   ? -64.819  4.914   -80.627  1.00 24.84  ? 854 HOH A O   1 
HETATM 17372 O O   . HOH BA 7 .   ? -59.823  5.668   -92.119  1.00 37.40  ? 855 HOH A O   1 
HETATM 17373 O O   . HOH BA 7 .   ? -50.018  19.896  -92.332  1.00 23.13  ? 856 HOH A O   1 
HETATM 17374 O O   . HOH BA 7 .   ? -56.820  3.846   -90.391  1.00 26.64  ? 857 HOH A O   1 
HETATM 17375 O O   . HOH BA 7 .   ? -64.268  9.880   -99.441  1.00 23.64  ? 858 HOH A O   1 
HETATM 17376 O O   . HOH BA 7 .   ? -47.338  35.953  -68.199  1.00 31.72  ? 859 HOH A O   1 
HETATM 17377 O O   . HOH BA 7 .   ? -75.717  19.684  -70.465  1.00 25.08  ? 860 HOH A O   1 
HETATM 17378 O O   . HOH BA 7 .   ? -57.818  -3.512  -73.262  1.00 30.52  ? 861 HOH A O   1 
HETATM 17379 O O   . HOH BA 7 .   ? -65.667  1.747   -88.808  1.00 28.72  ? 862 HOH A O   1 
HETATM 17380 O O   . HOH BA 7 .   ? -50.607  26.847  -97.688  1.00 26.30  ? 863 HOH A O   1 
HETATM 17381 O O   . HOH BA 7 .   ? -52.197  1.526   -75.192  1.00 31.44  ? 864 HOH A O   1 
HETATM 17382 O O   . HOH BA 7 .   ? -72.517  32.526  -79.576  1.00 21.02  ? 865 HOH A O   1 
HETATM 17383 O O   . HOH BA 7 .   ? -46.892  19.280  -64.968  1.00 35.51  ? 866 HOH A O   1 
HETATM 17384 O O   . HOH BA 7 .   ? -50.865  -0.454  -61.772  1.00 42.37  ? 867 HOH A O   1 
HETATM 17385 O O   . HOH BA 7 .   ? -82.951  18.224  -93.806  1.00 28.01  ? 868 HOH A O   1 
HETATM 17386 O O   . HOH BA 7 .   ? -67.678  1.434   -89.654  1.00 44.62  ? 869 HOH A O   1 
HETATM 17387 O O   . HOH BA 7 .   ? -73.713  8.739   -86.453  1.00 30.25  ? 870 HOH A O   1 
HETATM 17388 O O   . HOH BA 7 .   ? -56.486  23.664  -52.446  1.00 39.68  ? 871 HOH A O   1 
HETATM 17389 O O   . HOH BA 7 .   ? -51.674  9.000   -67.170  1.00 34.79  ? 872 HOH A O   1 
HETATM 17390 O O   . HOH BA 7 .   ? -74.898  7.908   -82.741  1.00 30.57  ? 873 HOH A O   1 
HETATM 17391 O O   . HOH BA 7 .   ? -78.009  7.782   -85.316  1.00 28.22  ? 874 HOH A O   1 
HETATM 17392 O O   . HOH BA 7 .   ? -74.982  28.722  -96.153  1.00 38.88  ? 875 HOH A O   1 
HETATM 17393 O O   . HOH BA 7 .   ? -44.707  37.068  -80.112  1.00 27.28  ? 876 HOH A O   1 
HETATM 17394 O O   . HOH BA 7 .   ? -44.227  19.253  -77.827  1.00 26.06  ? 877 HOH A O   1 
HETATM 17395 O O   . HOH BA 7 .   ? -42.288  35.299  -76.024  1.00 37.74  ? 878 HOH A O   1 
HETATM 17396 O O   . HOH BA 7 .   ? -91.762  -9.890  -81.261  1.00 42.44  ? 879 HOH A O   1 
HETATM 17397 O O   . HOH BA 7 .   ? -87.101  9.132   -89.185  1.00 28.03  ? 880 HOH A O   1 
HETATM 17398 O O   . HOH BA 7 .   ? -60.791  1.986   -74.217  1.00 26.89  ? 881 HOH A O   1 
HETATM 17399 O O   . HOH BA 7 .   ? -55.152  20.086  -69.329  1.00 33.32  ? 882 HOH A O   1 
HETATM 17400 O O   . HOH BA 7 .   ? -75.799  9.048   -55.272  1.00 44.95  ? 883 HOH A O   1 
HETATM 17401 O O   . HOH BA 7 .   ? -54.633  23.723  -83.188  1.00 25.45  ? 884 HOH A O   1 
HETATM 17402 O O   . HOH BA 7 .   ? -43.134  25.895  -79.892  1.00 34.12  ? 885 HOH A O   1 
HETATM 17403 O O   . HOH BA 7 .   ? -76.626  17.214  -69.406  1.00 29.70  ? 886 HOH A O   1 
HETATM 17404 O O   . HOH BA 7 .   ? -77.403  4.803   -73.426  1.00 41.08  ? 887 HOH A O   1 
HETATM 17405 O O   . HOH BA 7 .   ? -46.968  37.411  -70.616  1.00 24.67  ? 888 HOH A O   1 
HETATM 17406 O O   . HOH BA 7 .   ? -88.886  8.716   -91.040  1.00 29.15  ? 889 HOH A O   1 
HETATM 17407 O O   . HOH BA 7 .   ? -91.150  27.211  -96.898  1.00 35.34  ? 890 HOH A O   1 
HETATM 17408 O O   . HOH BA 7 .   ? -85.828  15.259  -78.084  1.00 27.59  ? 891 HOH A O   1 
HETATM 17409 O O   . HOH BA 7 .   ? -50.843  40.895  -76.165  1.00 28.81  ? 892 HOH A O   1 
HETATM 17410 O O   . HOH BA 7 .   ? -51.327  29.757  -96.708  1.00 39.90  ? 893 HOH A O   1 
HETATM 17411 O O   . HOH BA 7 .   ? -65.219  -16.950 -63.471  1.00 43.70  ? 894 HOH A O   1 
HETATM 17412 O O   . HOH BA 7 .   ? -91.915  15.148  -75.748  1.00 43.46  ? 895 HOH A O   1 
HETATM 17413 O O   . HOH BA 7 .   ? -85.173  9.583   -76.669  1.00 30.29  ? 896 HOH A O   1 
HETATM 17414 O O   . HOH BA 7 .   ? -74.942  15.120  -88.639  1.00 34.26  ? 897 HOH A O   1 
HETATM 17415 O O   . HOH BA 7 .   ? -79.684  16.370  -92.142  1.00 25.94  ? 898 HOH A O   1 
HETATM 17416 O O   . HOH BA 7 .   ? -86.409  20.952  -96.234  1.00 23.23  ? 899 HOH A O   1 
HETATM 17417 O O   . HOH BA 7 .   ? -90.071  10.655  -92.477  1.00 27.58  ? 900 HOH A O   1 
HETATM 17418 O O   . HOH BA 7 .   ? -62.857  -15.208 -76.098  1.00 40.39  ? 901 HOH A O   1 
HETATM 17419 O O   . HOH BA 7 .   ? -56.485  19.644  -71.363  1.00 28.82  ? 902 HOH A O   1 
HETATM 17420 O O   . HOH BA 7 .   ? -76.336  5.515   -80.511  1.00 24.23  ? 903 HOH A O   1 
HETATM 17421 O O   . HOH BA 7 .   ? -66.297  7.882   -77.422  1.00 30.37  ? 904 HOH A O   1 
HETATM 17422 O O   . HOH BA 7 .   ? -63.435  8.887   -76.853  1.00 28.20  ? 905 HOH A O   1 
HETATM 17423 O O   . HOH BA 7 .   ? -66.947  6.465   -94.939  1.00 29.64  ? 906 HOH A O   1 
HETATM 17424 O O   . HOH BA 7 .   ? -46.996  30.975  -57.268  1.00 33.36  ? 907 HOH A O   1 
HETATM 17425 O O   . HOH BA 7 .   ? -47.061  17.632  -95.691  1.00 29.50  ? 908 HOH A O   1 
HETATM 17426 O O   . HOH BA 7 .   ? -57.601  -1.658  -79.774  1.00 32.60  ? 909 HOH A O   1 
HETATM 17427 O O   . HOH BA 7 .   ? -76.827  22.311  -64.132  1.00 37.73  ? 910 HOH A O   1 
HETATM 17428 O O   . HOH BA 7 .   ? -90.357  17.325  -95.508  1.00 30.94  ? 911 HOH A O   1 
HETATM 17429 O O   . HOH BA 7 .   ? -71.462  12.421  -60.758  1.00 28.87  ? 912 HOH A O   1 
HETATM 17430 O O   . HOH BA 7 .   ? -75.146  10.964  -87.336  1.00 40.72  ? 913 HOH A O   1 
HETATM 17431 O O   . HOH BA 7 .   ? -92.497  10.179  -93.839  1.00 34.00  ? 914 HOH A O   1 
HETATM 17432 O O   . HOH BA 7 .   ? -64.920  38.261  -73.550  1.00 36.90  ? 915 HOH A O   1 
HETATM 17433 O O   . HOH BA 7 .   ? -62.313  31.170  -93.217  1.00 33.12  ? 916 HOH A O   1 
HETATM 17434 O O   . HOH BA 7 .   ? -74.939  -18.529 -77.064  1.00 32.25  ? 917 HOH A O   1 
HETATM 17435 O O   . HOH BA 7 .   ? -45.741  34.865  -84.374  1.00 42.42  ? 918 HOH A O   1 
HETATM 17436 O O   . HOH BA 7 .   ? -51.785  26.885  -75.468  1.00 29.37  ? 919 HOH A O   1 
HETATM 17437 O O   . HOH BA 7 .   ? -41.416  19.941  -95.879  1.00 32.00  ? 920 HOH A O   1 
HETATM 17438 O O   . HOH BA 7 .   ? -81.046  0.338   -75.303  1.00 27.90  ? 921 HOH A O   1 
HETATM 17439 O O   . HOH BA 7 .   ? -66.584  34.906  -62.766  1.00 34.79  ? 922 HOH A O   1 
HETATM 17440 O O   . HOH BA 7 .   ? -82.690  11.106  -77.131  1.00 16.25  ? 923 HOH A O   1 
HETATM 17441 O O   . HOH BA 7 .   ? -67.438  -17.079 -76.608  1.00 31.10  ? 924 HOH A O   1 
HETATM 17442 O O   . HOH BA 7 .   ? -33.859  33.976  -75.690  1.00 40.27  ? 925 HOH A O   1 
HETATM 17443 O O   . HOH BA 7 .   ? -82.696  -1.692  -74.429  1.00 22.53  ? 926 HOH A O   1 
HETATM 17444 O O   . HOH BA 7 .   ? -74.328  -7.688  -64.706  1.00 29.08  ? 927 HOH A O   1 
HETATM 17445 O O   . HOH BA 7 .   ? -39.417  16.614  -82.498  1.00 32.97  ? 928 HOH A O   1 
HETATM 17446 O O   . HOH BA 7 .   ? -73.252  32.507  -82.181  1.00 33.03  ? 929 HOH A O   1 
HETATM 17447 O O   . HOH BA 7 .   ? -52.498  24.389  -76.126  1.00 27.13  ? 930 HOH A O   1 
HETATM 17448 O O   . HOH BA 7 .   ? -81.510  6.860   -78.910  1.00 26.03  ? 931 HOH A O   1 
HETATM 17449 O O   . HOH BA 7 .   ? -81.772  12.046  -91.994  1.00 26.47  ? 932 HOH A O   1 
HETATM 17450 O O   . HOH BA 7 .   ? -83.942  16.650  -74.682  1.00 33.51  ? 933 HOH A O   1 
HETATM 17451 O O   . HOH BA 7 .   ? -49.886  -3.269  -66.025  1.00 30.25  ? 934 HOH A O   1 
HETATM 17452 O O   . HOH BA 7 .   ? -55.246  34.458  -57.564  1.00 40.64  ? 935 HOH A O   1 
HETATM 17453 O O   . HOH BA 7 .   ? -90.412  15.289  -97.427  1.00 40.16  ? 936 HOH A O   1 
HETATM 17454 O O   . HOH BA 7 .   ? -79.483  19.352  -73.997  1.00 28.02  ? 937 HOH A O   1 
HETATM 17455 O O   . HOH BA 7 .   ? -49.679  3.563   -87.444  1.00 36.27  ? 938 HOH A O   1 
HETATM 17456 O O   . HOH BA 7 .   ? -79.476  10.119  -88.716  1.00 37.27  ? 939 HOH A O   1 
HETATM 17457 O O   . HOH BA 7 .   ? -72.897  -6.961  -88.262  1.00 31.63  ? 940 HOH A O   1 
HETATM 17458 O O   . HOH BA 7 .   ? -49.896  14.267  -78.891  1.00 40.07  ? 941 HOH A O   1 
HETATM 17459 O O   . HOH BA 7 .   ? -57.908  -3.561  -56.469  1.00 38.23  ? 942 HOH A O   1 
HETATM 17460 O O   . HOH BA 7 .   ? -81.434  32.758  -72.834  1.00 33.78  ? 943 HOH A O   1 
HETATM 17461 O O   . HOH BA 7 .   ? -60.782  -13.371 -74.797  1.00 32.45  ? 944 HOH A O   1 
HETATM 17462 O O   . HOH BA 7 .   ? -77.817  18.981  -95.136  1.00 31.45  ? 945 HOH A O   1 
HETATM 17463 O O   . HOH BA 7 .   ? -53.497  32.807  -57.028  1.00 36.49  ? 946 HOH A O   1 
HETATM 17464 O O   . HOH BA 7 .   ? -75.474  33.349  -93.537  1.00 35.14  ? 947 HOH A O   1 
HETATM 17465 O O   . HOH BA 7 .   ? -93.929  -8.411  -79.893  1.00 35.79  ? 948 HOH A O   1 
HETATM 17466 O O   . HOH BA 7 .   ? -46.374  32.901  -68.583  1.00 34.15  ? 949 HOH A O   1 
HETATM 17467 O O   . HOH BA 7 .   ? -67.866  8.971   -93.931  1.00 28.57  ? 950 HOH A O   1 
HETATM 17468 O O   . HOH BA 7 .   ? -66.312  1.778   -56.678  1.00 36.49  ? 951 HOH A O   1 
HETATM 17469 O O   . HOH BA 7 .   ? -51.565  11.939  -78.484  1.00 29.95  ? 952 HOH A O   1 
HETATM 17470 O O   . HOH BA 7 .   ? -51.759  2.784   -70.058  1.00 36.29  ? 953 HOH A O   1 
HETATM 17471 O O   . HOH BA 7 .   ? -74.822  22.308  -92.422  1.00 36.58  ? 954 HOH A O   1 
HETATM 17472 O O   . HOH BA 7 .   ? -52.433  -1.792  -69.434  1.00 37.32  ? 955 HOH A O   1 
HETATM 17473 O O   . HOH BA 7 .   ? -80.267  17.858  -94.489  1.00 24.66  ? 956 HOH A O   1 
HETATM 17474 O O   . HOH BA 7 .   ? -88.576  19.124  -96.716  1.00 28.20  ? 957 HOH A O   1 
HETATM 17475 O O   . HOH BA 7 .   ? -77.459  8.537   -83.282  1.00 21.95  ? 958 HOH A O   1 
HETATM 17476 O O   . HOH BA 7 .   ? -50.936  0.430   -69.833  1.00 32.96  ? 959 HOH A O   1 
HETATM 17477 O O   . HOH BA 7 .   ? -56.356  -5.345  -74.760  1.00 34.51  ? 960 HOH A O   1 
HETATM 17478 O O   . HOH BA 7 .   ? -45.029  31.508  -58.775  1.00 39.40  ? 961 HOH A O   1 
HETATM 17479 O O   . HOH BA 7 .   ? -53.708  12.490  -74.909  1.00 31.37  ? 962 HOH A O   1 
HETATM 17480 O O   . HOH BA 7 .   ? -68.875  27.395  -61.173  1.00 37.21  ? 963 HOH A O   1 
HETATM 17481 O O   . HOH BA 7 .   ? -44.638  12.426  -78.705  1.00 38.70  ? 964 HOH A O   1 
HETATM 17482 O O   . HOH BA 7 .   ? -74.469  14.370  -91.134  1.00 33.78  ? 965 HOH A O   1 
HETATM 17483 O O   . HOH BA 7 .   ? -79.771  13.703  -91.084  1.00 31.37  ? 966 HOH A O   1 
HETATM 17484 O O   . HOH BA 7 .   ? -78.441  5.793   -82.258  1.00 33.23  ? 967 HOH A O   1 
HETATM 17485 O O   . HOH BA 7 .   ? -44.051  18.039  -96.202  1.00 27.88  ? 968 HOH A O   1 
HETATM 17486 O O   . HOH BA 7 .   ? -77.107  17.318  -91.130  1.00 25.47  ? 969 HOH A O   1 
HETATM 17487 O O   . HOH BA 7 .   ? -66.647  36.202  -81.840  1.00 38.58  ? 970 HOH A O   1 
HETATM 17488 O O   . HOH BA 7 .   ? -55.021  14.558  -97.843  1.00 32.81  ? 971 HOH A O   1 
HETATM 17489 O O   . HOH BA 7 .   ? -80.824  7.884   -91.176  1.00 30.70  ? 972 HOH A O   1 
HETATM 17490 O O   . HOH BA 7 .   ? -66.675  9.363   -98.512  1.00 27.32  ? 973 HOH A O   1 
HETATM 17491 O O   . HOH BA 7 .   ? -45.364  15.383  -74.750  1.00 45.12  ? 974 HOH A O   1 
HETATM 17492 O O   . HOH BA 7 .   ? -48.908  14.547  -76.768  1.00 34.72  ? 975 HOH A O   1 
HETATM 17493 O O   . HOH CA 7 .   ? -21.912  -31.109 -80.154  1.00 33.62  ? 701 HOH B O   1 
HETATM 17494 O O   . HOH CA 7 .   ? 7.317    -4.506  -63.614  1.00 20.48  ? 702 HOH B O   1 
HETATM 17495 O O   . HOH CA 7 .   ? -4.662   -13.820 -75.038  1.00 37.75  ? 703 HOH B O   1 
HETATM 17496 O O   . HOH CA 7 .   ? -15.510  -23.611 -64.113  1.00 29.00  ? 704 HOH B O   1 
HETATM 17497 O O   . HOH CA 7 .   ? 3.918    5.613   -76.273  1.00 33.61  ? 705 HOH B O   1 
HETATM 17498 O O   . HOH CA 7 .   ? -20.096  -21.490 -63.584  1.00 42.55  ? 706 HOH B O   1 
HETATM 17499 O O   . HOH CA 7 .   ? -11.736  -15.568 -54.472  1.00 45.17  ? 707 HOH B O   1 
HETATM 17500 O O   . HOH CA 7 .   ? -31.990  -12.952 -91.422  1.00 34.10  ? 708 HOH B O   1 
HETATM 17501 O O   . HOH CA 7 .   ? -6.659   -0.375  -29.161  1.00 40.21  ? 709 HOH B O   1 
HETATM 17502 O O   . HOH CA 7 .   ? -7.485   -16.325 -47.800  1.00 36.45  ? 710 HOH B O   1 
HETATM 17503 O O   . HOH CA 7 .   ? -19.104  -16.397 -42.141  1.00 35.17  ? 711 HOH B O   1 
HETATM 17504 O O   . HOH CA 7 .   ? 5.857    7.906   -75.864  1.00 26.99  ? 712 HOH B O   1 
HETATM 17505 O O   . HOH CA 7 .   ? -27.067  -16.531 -52.401  1.00 37.66  ? 713 HOH B O   1 
HETATM 17506 O O   . HOH CA 7 .   ? -23.638  -28.044 -42.969  1.00 39.80  ? 714 HOH B O   1 
HETATM 17507 O O   . HOH CA 7 .   ? -17.655  -15.043 -73.702  1.00 32.79  ? 715 HOH B O   1 
HETATM 17508 O O   . HOH CA 7 .   ? -29.068  -0.307  -64.348  1.00 24.91  ? 716 HOH B O   1 
HETATM 17509 O O   . HOH CA 7 .   ? -11.002  -7.613  -60.450  1.00 32.81  ? 717 HOH B O   1 
HETATM 17510 O O   . HOH CA 7 .   ? -18.603  21.268  -54.940  1.00 26.04  ? 718 HOH B O   1 
HETATM 17511 O O   . HOH CA 7 .   ? -0.020   8.630   -69.597  1.00 31.38  ? 719 HOH B O   1 
HETATM 17512 O O   . HOH CA 7 .   ? -40.478  -5.023  -77.056  1.00 38.21  ? 720 HOH B O   1 
HETATM 17513 O O   . HOH CA 7 .   ? -9.869   -1.245  -50.889  1.00 38.89  ? 721 HOH B O   1 
HETATM 17514 O O   . HOH CA 7 .   ? -44.781  -12.286 -86.042  1.00 40.77  ? 722 HOH B O   1 
HETATM 17515 O O   . HOH CA 7 .   ? -22.930  -10.426 -55.935  1.00 30.81  ? 723 HOH B O   1 
HETATM 17516 O O   . HOH CA 7 .   ? -9.269   16.055  -43.208  1.00 38.49  ? 724 HOH B O   1 
HETATM 17517 O O   . HOH CA 7 .   ? -12.305  -18.267 -58.576  1.00 26.14  ? 725 HOH B O   1 
HETATM 17518 O O   . HOH CA 7 .   ? -1.355   -2.051  -66.353  1.00 24.85  ? 726 HOH B O   1 
HETATM 17519 O O   . HOH CA 7 .   ? 2.236    10.053  -61.629  1.00 32.17  ? 727 HOH B O   1 
HETATM 17520 O O   . HOH CA 7 .   ? -19.281  3.219   -86.646  1.00 33.54  ? 728 HOH B O   1 
HETATM 17521 O O   . HOH CA 7 .   ? -30.043  -10.526 -86.006  1.00 32.27  ? 729 HOH B O   1 
HETATM 17522 O O   . HOH CA 7 .   ? -1.549   1.836   -63.292  1.00 26.93  ? 730 HOH B O   1 
HETATM 17523 O O   . HOH CA 7 .   ? -15.270  14.160  -72.579  1.00 29.78  ? 731 HOH B O   1 
HETATM 17524 O O   . HOH CA 7 .   ? -9.606   -17.240 -71.859  1.00 28.95  ? 732 HOH B O   1 
HETATM 17525 O O   . HOH CA 7 .   ? -24.098  1.759   -78.098  1.00 22.04  ? 733 HOH B O   1 
HETATM 17526 O O   . HOH CA 7 .   ? -21.434  16.817  -59.972  1.00 25.62  ? 734 HOH B O   1 
HETATM 17527 O O   . HOH CA 7 .   ? -27.138  1.616   -48.863  1.00 37.95  ? 735 HOH B O   1 
HETATM 17528 O O   . HOH CA 7 .   ? -24.209  -12.189 -78.671  1.00 34.10  ? 736 HOH B O   1 
HETATM 17529 O O   . HOH CA 7 .   ? -38.013  -7.532  -96.495  1.00 24.99  ? 737 HOH B O   1 
HETATM 17530 O O   . HOH CA 7 .   ? -26.681  15.513  -79.067  1.00 26.71  ? 738 HOH B O   1 
HETATM 17531 O O   . HOH CA 7 .   ? -26.038  -37.385 -60.588  1.00 42.00  ? 739 HOH B O   1 
HETATM 17532 O O   . HOH CA 7 .   ? -14.606  -9.427  -54.466  1.00 23.65  ? 740 HOH B O   1 
HETATM 17533 O O   . HOH CA 7 .   ? -6.256   8.616   -40.873  1.00 40.64  ? 741 HOH B O   1 
HETATM 17534 O O   . HOH CA 7 .   ? -18.144  13.278  -80.574  1.00 31.47  ? 742 HOH B O   1 
HETATM 17535 O O   . HOH CA 7 .   ? -11.626  -22.729 -57.938  1.00 24.35  ? 743 HOH B O   1 
HETATM 17536 O O   . HOH CA 7 .   ? -22.533  17.720  -84.901  1.00 26.78  ? 744 HOH B O   1 
HETATM 17537 O O   . HOH CA 7 .   ? -33.841  10.343  -92.144  1.00 38.90  ? 745 HOH B O   1 
HETATM 17538 O O   . HOH CA 7 .   ? -31.859  -21.820 -61.717  1.00 39.83  ? 746 HOH B O   1 
HETATM 17539 O O   . HOH CA 7 .   ? -5.025   -9.637  -83.798  1.00 26.63  ? 747 HOH B O   1 
HETATM 17540 O O   . HOH CA 7 .   ? -27.644  16.898  -65.455  1.00 37.92  ? 748 HOH B O   1 
HETATM 17541 O O   . HOH CA 7 .   ? -11.268  6.910   -75.473  1.00 25.96  ? 749 HOH B O   1 
HETATM 17542 O O   . HOH CA 7 .   ? -16.535  10.183  -77.501  1.00 32.57  ? 750 HOH B O   1 
HETATM 17543 O O   . HOH CA 7 .   ? -32.500  -21.899 -67.472  1.00 40.61  ? 751 HOH B O   1 
HETATM 17544 O O   . HOH CA 7 .   ? -4.193   3.724   -56.794  1.00 33.87  ? 752 HOH B O   1 
HETATM 17545 O O   . HOH CA 7 .   ? -30.274  2.620   -54.144  1.00 41.32  ? 753 HOH B O   1 
HETATM 17546 O O   . HOH CA 7 .   ? -8.074   -2.883  -71.418  1.00 25.61  ? 754 HOH B O   1 
HETATM 17547 O O   . HOH CA 7 .   ? -30.019  -7.185  -53.705  1.00 35.81  ? 755 HOH B O   1 
HETATM 17548 O O   . HOH CA 7 .   ? -34.895  -27.907 -69.327  1.00 36.27  ? 756 HOH B O   1 
HETATM 17549 O O   . HOH CA 7 .   ? -28.384  -0.842  -69.769  1.00 25.64  ? 757 HOH B O   1 
HETATM 17550 O O   . HOH CA 7 .   ? -26.937  -33.339 -59.886  1.00 41.38  ? 758 HOH B O   1 
HETATM 17551 O O   . HOH CA 7 .   ? 0.409    5.433   -65.402  1.00 22.83  ? 759 HOH B O   1 
HETATM 17552 O O   . HOH CA 7 .   ? -29.575  13.231  -70.006  1.00 27.59  ? 760 HOH B O   1 
HETATM 17553 O O   . HOH CA 7 .   ? -15.676  -12.927 -52.664  1.00 31.41  ? 761 HOH B O   1 
HETATM 17554 O O   . HOH CA 7 .   ? -26.266  -6.075  -60.743  1.00 25.26  ? 762 HOH B O   1 
HETATM 17555 O O   . HOH CA 7 .   ? -15.688  -5.409  -81.303  1.00 38.82  ? 763 HOH B O   1 
HETATM 17556 O O   . HOH CA 7 .   ? -18.637  15.509  -86.293  1.00 31.53  ? 764 HOH B O   1 
HETATM 17557 O O   . HOH CA 7 .   ? -28.409  -19.058 -66.362  1.00 26.43  ? 765 HOH B O   1 
HETATM 17558 O O   . HOH CA 7 .   ? -21.896  -14.550 -43.537  1.00 29.01  ? 766 HOH B O   1 
HETATM 17559 O O   . HOH CA 7 .   ? -17.625  -9.159  -74.655  1.00 25.48  ? 767 HOH B O   1 
HETATM 17560 O O   . HOH CA 7 .   ? -22.304  12.813  -70.682  1.00 31.93  ? 768 HOH B O   1 
HETATM 17561 O O   . HOH CA 7 .   ? -31.194  -17.670 -72.780  1.00 28.33  ? 769 HOH B O   1 
HETATM 17562 O O   . HOH CA 7 .   ? -4.457   -5.129  -47.661  1.00 43.95  ? 770 HOH B O   1 
HETATM 17563 O O   . HOH CA 7 .   ? -13.120  -8.163  -70.528  1.00 24.93  ? 771 HOH B O   1 
HETATM 17564 O O   . HOH CA 7 .   ? -24.546  -8.301  -76.619  1.00 20.70  ? 772 HOH B O   1 
HETATM 17565 O O   . HOH CA 7 .   ? -27.402  -37.929 -83.311  1.00 47.27  ? 773 HOH B O   1 
HETATM 17566 O O   . HOH CA 7 .   ? -26.472  -23.145 -50.637  1.00 32.14  ? 774 HOH B O   1 
HETATM 17567 O O   . HOH CA 7 .   ? -32.164  -4.030  -99.700  1.00 30.82  ? 775 HOH B O   1 
HETATM 17568 O O   . HOH CA 7 .   ? -7.915   -16.081 -65.203  1.00 34.21  ? 776 HOH B O   1 
HETATM 17569 O O   . HOH CA 7 .   ? -27.635  -8.621  -53.963  1.00 28.44  ? 777 HOH B O   1 
HETATM 17570 O O   . HOH CA 7 .   ? 3.869    0.906   -71.272  1.00 23.86  ? 778 HOH B O   1 
HETATM 17571 O O   . HOH CA 7 .   ? -8.461   -22.214 -47.693  1.00 33.88  ? 779 HOH B O   1 
HETATM 17572 O O   . HOH CA 7 .   ? -20.304  -14.784 -40.154  1.00 31.47  ? 780 HOH B O   1 
HETATM 17573 O O   . HOH CA 7 .   ? -30.723  -4.363  -91.425  1.00 27.46  ? 781 HOH B O   1 
HETATM 17574 O O   . HOH CA 7 .   ? -22.020  15.078  -56.360  1.00 27.61  ? 782 HOH B O   1 
HETATM 17575 O O   . HOH CA 7 .   ? -18.783  10.183  -92.279  1.00 35.22  ? 783 HOH B O   1 
HETATM 17576 O O   . HOH CA 7 .   ? -26.380  1.290   -91.578  1.00 27.29  ? 784 HOH B O   1 
HETATM 17577 O O   . HOH CA 7 .   ? -12.040  -2.004  -82.227  1.00 32.18  ? 785 HOH B O   1 
HETATM 17578 O O   . HOH CA 7 .   ? -26.794  6.024   -64.873  1.00 34.01  ? 786 HOH B O   1 
HETATM 17579 O O   . HOH CA 7 .   ? -15.274  -10.368 -63.980  1.00 27.12  ? 787 HOH B O   1 
HETATM 17580 O O   . HOH CA 7 .   ? -13.758  -0.545  -33.534  1.00 39.77  ? 788 HOH B O   1 
HETATM 17581 O O   . HOH CA 7 .   ? -35.785  -3.490  -98.169  1.00 17.11  ? 789 HOH B O   1 
HETATM 17582 O O   . HOH CA 7 .   ? -22.921  9.269   -75.459  1.00 26.40  ? 790 HOH B O   1 
HETATM 17583 O O   . HOH CA 7 .   ? -18.231  15.457  -66.645  1.00 29.21  ? 791 HOH B O   1 
HETATM 17584 O O   . HOH CA 7 .   ? -9.488   -11.205 -76.716  1.00 28.34  ? 792 HOH B O   1 
HETATM 17585 O O   . HOH CA 7 .   ? -9.289   9.107   -55.937  1.00 26.83  ? 793 HOH B O   1 
HETATM 17586 O O   . HOH CA 7 .   ? -11.891  1.082   -53.072  1.00 46.26  ? 794 HOH B O   1 
HETATM 17587 O O   . HOH CA 7 .   ? -29.614  -12.878 -74.276  1.00 26.66  ? 795 HOH B O   1 
HETATM 17588 O O   . HOH CA 7 .   ? -15.737  18.508  -62.126  1.00 30.63  ? 796 HOH B O   1 
HETATM 17589 O O   . HOH CA 7 .   ? -36.828  3.045   -59.376  1.00 32.85  ? 797 HOH B O   1 
HETATM 17590 O O   . HOH CA 7 .   ? -10.949  -21.329 -50.541  1.00 27.03  ? 798 HOH B O   1 
HETATM 17591 O O   . HOH CA 7 .   ? 4.233    1.960   -62.457  1.00 37.35  ? 799 HOH B O   1 
HETATM 17592 O O   . HOH CA 7 .   ? -5.897   16.937  -48.545  1.00 37.08  ? 800 HOH B O   1 
HETATM 17593 O O   . HOH CA 7 .   ? -7.908   0.646   -43.400  1.00 32.36  ? 801 HOH B O   1 
HETATM 17594 O O   . HOH CA 7 .   ? -28.637  0.590   -95.995  1.00 32.77  ? 802 HOH B O   1 
HETATM 17595 O O   . HOH CA 7 .   ? -23.497  16.366  -54.697  1.00 28.16  ? 803 HOH B O   1 
HETATM 17596 O O   . HOH CA 7 .   ? -14.836  -21.237 -52.363  1.00 28.00  ? 804 HOH B O   1 
HETATM 17597 O O   . HOH CA 7 .   ? -16.947  4.802   -70.614  1.00 25.12  ? 805 HOH B O   1 
HETATM 17598 O O   . HOH CA 7 .   ? -23.611  9.582   -49.141  1.00 24.23  ? 806 HOH B O   1 
HETATM 17599 O O   . HOH CA 7 .   ? -2.989   11.675  -52.736  1.00 48.30  ? 807 HOH B O   1 
HETATM 17600 O O   . HOH CA 7 .   ? -15.626  2.147   -82.271  1.00 29.62  ? 808 HOH B O   1 
HETATM 17601 O O   . HOH CA 7 .   ? -24.422  -32.108 -67.466  1.00 28.88  ? 809 HOH B O   1 
HETATM 17602 O O   . HOH CA 7 .   ? -13.935  -17.300 -60.506  1.00 27.50  ? 810 HOH B O   1 
HETATM 17603 O O   . HOH CA 7 .   ? -8.479   -9.244  -65.757  1.00 37.06  ? 811 HOH B O   1 
HETATM 17604 O O   . HOH CA 7 .   ? 2.417    -6.645  -76.963  1.00 42.92  ? 812 HOH B O   1 
HETATM 17605 O O   . HOH CA 7 .   ? -34.594  -10.613 -74.277  1.00 27.36  ? 813 HOH B O   1 
HETATM 17606 O O   . HOH CA 7 .   ? -17.655  -3.602  -58.509  1.00 28.60  ? 814 HOH B O   1 
HETATM 17607 O O   . HOH CA 7 .   ? -30.531  -3.408  -61.392  1.00 30.38  ? 815 HOH B O   1 
HETATM 17608 O O   . HOH CA 7 .   ? -21.778  -3.258  -80.881  1.00 25.40  ? 816 HOH B O   1 
HETATM 17609 O O   . HOH CA 7 .   ? -1.871   4.055   -64.661  1.00 33.34  ? 817 HOH B O   1 
HETATM 17610 O O   . HOH CA 7 .   ? -8.054   -27.248 -52.611  1.00 34.04  ? 818 HOH B O   1 
HETATM 17611 O O   . HOH CA 7 .   ? -2.782   -15.292 -72.283  1.00 31.51  ? 819 HOH B O   1 
HETATM 17612 O O   . HOH CA 7 .   ? -14.456  -14.332 -67.772  1.00 25.22  ? 820 HOH B O   1 
HETATM 17613 O O   . HOH CA 7 .   ? -20.684  15.755  -67.081  1.00 33.12  ? 821 HOH B O   1 
HETATM 17614 O O   . HOH CA 7 .   ? -18.840  1.859   -90.308  1.00 32.31  ? 822 HOH B O   1 
HETATM 17615 O O   . HOH CA 7 .   ? -2.837   3.902   -81.469  1.00 29.15  ? 823 HOH B O   1 
HETATM 17616 O O   . HOH CA 7 .   ? 2.123    0.386   -55.388  1.00 39.42  ? 824 HOH B O   1 
HETATM 17617 O O   . HOH CA 7 .   ? -28.535  -15.247 -67.218  1.00 39.44  ? 825 HOH B O   1 
HETATM 17618 O O   . HOH CA 7 .   ? -21.948  -2.522  -38.494  1.00 41.23  ? 826 HOH B O   1 
HETATM 17619 O O   . HOH CA 7 .   ? -18.840  12.015  -72.247  1.00 34.43  ? 827 HOH B O   1 
HETATM 17620 O O   . HOH CA 7 .   ? -6.074   8.508   -59.605  1.00 26.31  ? 828 HOH B O   1 
HETATM 17621 O O   . HOH CA 7 .   ? 3.845    6.615   -56.724  1.00 33.13  ? 829 HOH B O   1 
HETATM 17622 O O   . HOH CA 7 .   ? -30.094  12.711  -77.033  1.00 28.61  ? 830 HOH B O   1 
HETATM 17623 O O   . HOH CA 7 .   ? 8.174    -1.584  -72.228  1.00 31.30  ? 831 HOH B O   1 
HETATM 17624 O O   . HOH CA 7 .   ? -24.302  -7.548  -86.109  1.00 27.51  ? 832 HOH B O   1 
HETATM 17625 O O   . HOH CA 7 .   ? 9.149    11.837  -70.411  1.00 31.57  ? 833 HOH B O   1 
HETATM 17626 O O   . HOH CA 7 .   ? -25.880  -15.045 -63.864  1.00 23.99  ? 834 HOH B O   1 
HETATM 17627 O O   . HOH CA 7 .   ? -22.755  -29.349 -55.697  1.00 32.61  ? 835 HOH B O   1 
HETATM 17628 O O   . HOH CA 7 .   ? -37.120  -37.358 -78.184  1.00 41.78  ? 836 HOH B O   1 
HETATM 17629 O O   . HOH CA 7 .   ? -9.843   -9.000  -82.841  1.00 24.49  ? 837 HOH B O   1 
HETATM 17630 O O   . HOH CA 7 .   ? -23.425  16.630  -50.019  1.00 30.45  ? 838 HOH B O   1 
HETATM 17631 O O   . HOH CA 7 .   ? -5.501   -1.146  -78.585  1.00 21.24  ? 839 HOH B O   1 
HETATM 17632 O O   . HOH CA 7 .   ? 0.424    -9.870  -64.314  1.00 27.04  ? 840 HOH B O   1 
HETATM 17633 O O   . HOH CA 7 .   ? -34.421  -4.583  -76.015  1.00 24.24  ? 841 HOH B O   1 
HETATM 17634 O O   . HOH CA 7 .   ? -20.256  0.472   -83.112  1.00 24.65  ? 842 HOH B O   1 
HETATM 17635 O O   . HOH CA 7 .   ? -30.853  -6.482  -69.704  1.00 39.75  ? 843 HOH B O   1 
HETATM 17636 O O   . HOH CA 7 .   ? -12.410  -11.531 -63.702  1.00 28.23  ? 844 HOH B O   1 
HETATM 17637 O O   . HOH CA 7 .   ? -11.590  -14.240 -63.758  1.00 27.79  ? 845 HOH B O   1 
HETATM 17638 O O   . HOH CA 7 .   ? -2.065   17.348  -50.797  1.00 37.41  ? 846 HOH B O   1 
HETATM 17639 O O   . HOH CA 7 .   ? -24.888  -14.971 -87.450  1.00 36.74  ? 847 HOH B O   1 
HETATM 17640 O O   . HOH CA 7 .   ? -9.137   -24.298 -61.332  1.00 32.81  ? 848 HOH B O   1 
HETATM 17641 O O   . HOH CA 7 .   ? -24.136  -20.290 -46.234  1.00 34.26  ? 849 HOH B O   1 
HETATM 17642 O O   . HOH CA 7 .   ? -10.025  -4.998  -57.857  1.00 27.06  ? 850 HOH B O   1 
HETATM 17643 O O   . HOH CA 7 .   ? -37.561  -3.279  -93.864  1.00 32.85  ? 851 HOH B O   1 
HETATM 17644 O O   . HOH CA 7 .   ? -10.640  -16.819 -52.352  1.00 30.58  ? 852 HOH B O   1 
HETATM 17645 O O   . HOH CA 7 .   ? 3.785    2.437   -65.559  1.00 29.17  ? 853 HOH B O   1 
HETATM 17646 O O   . HOH CA 7 .   ? -17.285  -34.271 -67.125  1.00 31.48  ? 854 HOH B O   1 
HETATM 17647 O O   . HOH CA 7 .   ? 0.144    7.354   -63.362  1.00 26.79  ? 855 HOH B O   1 
HETATM 17648 O O   . HOH CA 7 .   ? -29.944  -27.856 -58.447  1.00 39.98  ? 856 HOH B O   1 
HETATM 17649 O O   . HOH CA 7 .   ? -6.441   5.158   -58.020  1.00 29.89  ? 857 HOH B O   1 
HETATM 17650 O O   . HOH CA 7 .   ? 12.776   1.171   -69.930  1.00 43.65  ? 858 HOH B O   1 
HETATM 17651 O O   . HOH CA 7 .   ? -11.861  0.710   -64.198  1.00 21.92  ? 859 HOH B O   1 
HETATM 17652 O O   . HOH CA 7 .   ? -23.712  -4.988  -81.815  1.00 23.16  ? 860 HOH B O   1 
HETATM 17653 O O   . HOH CA 7 .   ? 2.226    16.599  -53.023  1.00 36.23  ? 861 HOH B O   1 
HETATM 17654 O O   . HOH CA 7 .   ? -12.532  -15.071 -65.980  1.00 26.39  ? 862 HOH B O   1 
HETATM 17655 O O   . HOH CA 7 .   ? -8.918   0.112   -83.123  1.00 33.87  ? 863 HOH B O   1 
HETATM 17656 O O   . HOH CA 7 .   ? -10.766  -9.628  -78.291  1.00 25.47  ? 864 HOH B O   1 
HETATM 17657 O O   . HOH CA 7 .   ? -31.385  8.688   -54.656  1.00 36.73  ? 865 HOH B O   1 
HETATM 17658 O O   . HOH CA 7 .   ? -17.534  -11.796 -65.869  1.00 41.31  ? 866 HOH B O   1 
HETATM 17659 O O   . HOH CA 7 .   ? -22.115  -11.613 -74.589  1.00 27.15  ? 867 HOH B O   1 
HETATM 17660 O O   . HOH CA 7 .   ? -5.034   21.968  -56.964  1.00 37.02  ? 868 HOH B O   1 
HETATM 17661 O O   . HOH CA 7 .   ? -30.868  -11.065 -88.595  1.00 31.66  ? 869 HOH B O   1 
HETATM 17662 O O   . HOH CA 7 .   ? -24.317  -1.515  -88.107  1.00 35.11  ? 870 HOH B O   1 
HETATM 17663 O O   . HOH CA 7 .   ? -30.894  10.389  -93.846  1.00 33.04  ? 871 HOH B O   1 
HETATM 17664 O O   . HOH CA 7 .   ? -12.841  -19.692 -51.433  1.00 34.30  ? 872 HOH B O   1 
HETATM 17665 O O   . HOH CA 7 .   ? -36.054  3.958   -96.495  1.00 22.54  ? 873 HOH B O   1 
HETATM 17666 O O   . HOH CA 7 .   ? -21.599  15.867  -74.897  1.00 38.09  ? 874 HOH B O   1 
HETATM 17667 O O   . HOH CA 7 .   ? -36.804  11.438  -73.928  1.00 27.84  ? 875 HOH B O   1 
HETATM 17668 O O   . HOH CA 7 .   ? -19.934  -4.782  -79.631  1.00 32.41  ? 876 HOH B O   1 
HETATM 17669 O O   . HOH CA 7 .   ? -29.856  -28.677 -83.140  1.00 36.32  ? 877 HOH B O   1 
HETATM 17670 O O   . HOH CA 7 .   ? -31.014  14.135  -59.987  1.00 30.89  ? 878 HOH B O   1 
HETATM 17671 O O   . HOH CA 7 .   ? -8.628   20.311  -68.344  1.00 37.18  ? 879 HOH B O   1 
HETATM 17672 O O   . HOH CA 7 .   ? -31.343  -9.178  -90.299  1.00 33.37  ? 880 HOH B O   1 
HETATM 17673 O O   . HOH CA 7 .   ? -6.112   7.603   -57.127  1.00 31.63  ? 881 HOH B O   1 
HETATM 17674 O O   . HOH CA 7 .   ? -22.385  -24.213 -78.179  1.00 31.40  ? 882 HOH B O   1 
HETATM 17675 O O   . HOH CA 7 .   ? -22.330  -3.228  -84.999  1.00 25.68  ? 883 HOH B O   1 
HETATM 17676 O O   . HOH CA 7 .   ? -29.026  -26.040 -56.667  1.00 33.18  ? 884 HOH B O   1 
HETATM 17677 O O   . HOH CA 7 .   ? -11.713  -15.788 -61.562  1.00 25.73  ? 885 HOH B O   1 
HETATM 17678 O O   . HOH CA 7 .   ? -33.363  2.512   -59.000  1.00 32.28  ? 886 HOH B O   1 
HETATM 17679 O O   . HOH CA 7 .   ? -21.917  17.071  -52.634  1.00 38.66  ? 887 HOH B O   1 
HETATM 17680 O O   . HOH CA 7 .   ? -13.189  -32.809 -60.690  1.00 36.21  ? 888 HOH B O   1 
HETATM 17681 O O   . HOH CA 7 .   ? -33.546  -27.025 -80.370  1.00 37.63  ? 889 HOH B O   1 
HETATM 17682 O O   . HOH CA 7 .   ? -27.757  -30.371 -50.185  1.00 27.55  ? 890 HOH B O   1 
HETATM 17683 O O   . HOH CA 7 .   ? -41.307  -18.196 -88.338  1.00 38.70  ? 891 HOH B O   1 
HETATM 17684 O O   . HOH CA 7 .   ? -33.530  12.475  -68.451  1.00 35.03  ? 892 HOH B O   1 
HETATM 17685 O O   . HOH CA 7 .   ? -25.054  -7.129  -62.703  1.00 34.95  ? 893 HOH B O   1 
HETATM 17686 O O   . HOH CA 7 .   ? -30.634  -2.457  -63.669  1.00 23.31  ? 894 HOH B O   1 
HETATM 17687 O O   . HOH CA 7 .   ? -23.250  18.315  -64.229  1.00 35.95  ? 895 HOH B O   1 
HETATM 17688 O O   . HOH CA 7 .   ? -25.643  0.847   -89.232  1.00 29.52  ? 896 HOH B O   1 
HETATM 17689 O O   . HOH CA 7 .   ? -39.355  7.916   -87.203  1.00 30.32  ? 897 HOH B O   1 
HETATM 17690 O O   . HOH CA 7 .   ? 10.489   -9.387  -68.601  1.00 36.07  ? 898 HOH B O   1 
HETATM 17691 O O   . HOH CA 7 .   ? -22.118  9.984   -94.234  1.00 39.10  ? 899 HOH B O   1 
HETATM 17692 O O   . HOH CA 7 .   ? -20.444  -8.000  -78.534  1.00 39.64  ? 900 HOH B O   1 
HETATM 17693 O O   . HOH CA 7 .   ? -32.041  -8.736  -73.279  1.00 15.46  ? 901 HOH B O   1 
HETATM 17694 O O   . HOH CA 7 .   ? -4.560   4.318   -65.089  1.00 41.75  ? 902 HOH B O   1 
HETATM 17695 O O   . HOH CA 7 .   ? -36.255  -2.465  -76.144  1.00 30.46  ? 903 HOH B O   1 
HETATM 17696 O O   . HOH CA 7 .   ? 11.478   -2.478  -69.276  1.00 32.75  ? 904 HOH B O   1 
HETATM 17697 O O   . HOH CA 7 .   ? -6.280   15.818  -43.619  1.00 37.49  ? 905 HOH B O   1 
HETATM 17698 O O   . HOH CA 7 .   ? -21.622  12.895  -73.090  1.00 28.93  ? 906 HOH B O   1 
HETATM 17699 O O   . HOH CA 7 .   ? -31.156  -19.424 -70.739  1.00 24.45  ? 907 HOH B O   1 
HETATM 17700 O O   . HOH CA 7 .   ? 3.987    16.315  -57.040  1.00 29.78  ? 908 HOH B O   1 
HETATM 17701 O O   . HOH CA 7 .   ? -29.974  -2.372  -93.091  1.00 27.31  ? 909 HOH B O   1 
HETATM 17702 O O   . HOH CA 7 .   ? 3.310    15.958  -61.814  1.00 33.64  ? 910 HOH B O   1 
HETATM 17703 O O   . HOH CA 7 .   ? 2.203    18.401  -57.542  1.00 32.39  ? 911 HOH B O   1 
HETATM 17704 O O   . HOH CA 7 .   ? -11.756  0.358   -55.687  1.00 40.02  ? 912 HOH B O   1 
HETATM 17705 O O   . HOH CA 7 .   ? -4.341   18.513  -50.115  1.00 32.79  ? 913 HOH B O   1 
HETATM 17706 O O   . HOH CA 7 .   ? -32.492  -9.761  -92.421  1.00 32.93  ? 914 HOH B O   1 
HETATM 17707 O O   . HOH CA 7 .   ? -14.197  -11.648 -76.414  1.00 31.78  ? 915 HOH B O   1 
HETATM 17708 O O   . HOH CA 7 .   ? -6.790   19.545  -67.073  1.00 36.16  ? 916 HOH B O   1 
HETATM 17709 O O   . HOH CA 7 .   ? -32.837  -21.759 -70.457  1.00 30.82  ? 917 HOH B O   1 
HETATM 17710 O O   . HOH CA 7 .   ? -27.168  4.933   -43.540  1.00 32.86  ? 918 HOH B O   1 
HETATM 17711 O O   . HOH CA 7 .   ? -6.813   11.989  -77.990  1.00 38.78  ? 919 HOH B O   1 
HETATM 17712 O O   . HOH CA 7 .   ? -31.280  -13.908 -73.248  1.00 43.46  ? 920 HOH B O   1 
HETATM 17713 O O   . HOH CA 7 .   ? -17.737  -36.499 -65.892  1.00 33.72  ? 921 HOH B O   1 
HETATM 17714 O O   . HOH CA 7 .   ? -40.766  -15.557 -76.170  1.00 39.54  ? 922 HOH B O   1 
HETATM 17715 O O   . HOH CA 7 .   ? -18.071  13.653  -75.780  1.00 30.05  ? 923 HOH B O   1 
HETATM 17716 O O   . HOH CA 7 .   ? -24.331  -11.186 -76.414  1.00 22.86  ? 924 HOH B O   1 
HETATM 17717 O O   . HOH CA 7 .   ? -28.136  -0.628  -93.486  1.00 36.49  ? 925 HOH B O   1 
HETATM 17718 O O   . HOH CA 7 .   ? -27.712  7.676   -52.895  1.00 40.45  ? 926 HOH B O   1 
HETATM 17719 O O   . HOH CA 7 .   ? -9.653   -24.460 -58.630  1.00 33.77  ? 927 HOH B O   1 
HETATM 17720 O O   . HOH CA 7 .   ? -26.454  -19.052 -46.924  1.00 32.64  ? 928 HOH B O   1 
HETATM 17721 O O   . HOH CA 7 .   ? -27.328  8.334   -50.473  1.00 36.85  ? 929 HOH B O   1 
HETATM 17722 O O   . HOH CA 7 .   ? -13.627  -9.699  -77.705  1.00 26.56  ? 930 HOH B O   1 
HETATM 17723 O O   . HOH CA 7 .   ? -7.062   -18.423 -51.627  1.00 32.61  ? 931 HOH B O   1 
HETATM 17724 O O   . HOH CA 7 .   ? -19.409  -1.349  -87.257  1.00 34.01  ? 932 HOH B O   1 
HETATM 17725 O O   . HOH CA 7 .   ? -27.812  -16.540 -65.124  1.00 28.86  ? 933 HOH B O   1 
HETATM 17726 O O   . HOH CA 7 .   ? -7.140   -7.968  -55.246  1.00 35.94  ? 934 HOH B O   1 
HETATM 17727 O O   . HOH CA 7 .   ? -20.732  -2.257  -83.064  1.00 28.11  ? 935 HOH B O   1 
HETATM 17728 O O   . HOH CA 7 .   ? 2.157    -4.620  -78.246  1.00 29.73  ? 936 HOH B O   1 
HETATM 17729 O O   . HOH CA 7 .   ? -21.719  -2.164  -87.497  1.00 29.43  ? 937 HOH B O   1 
HETATM 17730 O O   . HOH CA 7 .   ? -22.887  -6.037  -84.284  1.00 28.21  ? 938 HOH B O   1 
HETATM 17731 O O   . HOH CA 7 .   ? -26.913  -33.459 -50.720  1.00 34.90  ? 939 HOH B O   1 
HETATM 17732 O O   . HOH CA 7 .   ? -7.857   -9.679  -84.301  1.00 32.27  ? 940 HOH B O   1 
HETATM 17733 O O   . HOH CA 7 .   ? 10.906   -1.172  -71.426  1.00 31.86  ? 941 HOH B O   1 
HETATM 17734 O O   . HOH CA 7 .   ? -33.589  -17.875 -73.760  1.00 37.05  ? 942 HOH B O   1 
HETATM 17735 O O   . HOH DA 7 .   ? -43.702  54.862  -65.838  1.00 28.34  ? 701 HOH C O   1 
HETATM 17736 O O   . HOH DA 7 .   ? -13.395  58.123  -65.479  1.00 29.58  ? 702 HOH C O   1 
HETATM 17737 O O   . HOH DA 7 .   ? -28.957  59.520  -55.320  1.00 30.63  ? 703 HOH C O   1 
HETATM 17738 O O   . HOH DA 7 .   ? -9.581   69.221  -55.300  1.00 34.75  ? 704 HOH C O   1 
HETATM 17739 O O   . HOH DA 7 .   ? -20.468  64.024  -46.663  1.00 35.52  ? 705 HOH C O   1 
HETATM 17740 O O   . HOH DA 7 .   ? 6.080    59.456  -71.825  1.00 39.38  ? 706 HOH C O   1 
HETATM 17741 O O   . HOH DA 7 .   ? -29.132  64.002  -61.454  1.00 34.96  ? 707 HOH C O   1 
HETATM 17742 O O   . HOH DA 7 .   ? -26.955  51.566  -64.321  1.00 25.45  ? 708 HOH C O   1 
HETATM 17743 O O   . HOH DA 7 .   ? -26.999  34.274  -47.319  1.00 29.23  ? 709 HOH C O   1 
HETATM 17744 O O   . HOH DA 7 .   ? -16.165  56.809  -64.567  1.00 20.90  ? 710 HOH C O   1 
HETATM 17745 O O   . HOH DA 7 .   ? -27.440  70.598  -56.248  1.00 26.69  ? 711 HOH C O   1 
HETATM 17746 O O   . HOH DA 7 .   ? -25.474  40.266  -33.817  1.00 39.90  ? 712 HOH C O   1 
HETATM 17747 O O   . HOH DA 7 .   ? -11.602  70.225  -65.985  1.00 39.22  ? 713 HOH C O   1 
HETATM 17748 O O   . HOH DA 7 .   ? -37.198  49.555  -59.465  1.00 30.45  ? 714 HOH C O   1 
HETATM 17749 O O   . HOH DA 7 .   ? -23.900  39.676  -40.190  1.00 30.62  ? 715 HOH C O   1 
HETATM 17750 O O   . HOH DA 7 .   ? -9.013   23.181  -65.134  1.00 37.97  ? 716 HOH C O   1 
HETATM 17751 O O   . HOH DA 7 .   ? -5.871   60.930  -59.116  1.00 26.52  ? 717 HOH C O   1 
HETATM 17752 O O   . HOH DA 7 .   ? -15.787  33.799  -62.826  1.00 32.90  ? 718 HOH C O   1 
HETATM 17753 O O   . HOH DA 7 .   ? -18.204  72.209  -57.345  1.00 29.42  ? 719 HOH C O   1 
HETATM 17754 O O   . HOH DA 7 .   ? -3.322   58.907  -72.925  1.00 39.21  ? 720 HOH C O   1 
HETATM 17755 O O   . HOH DA 7 .   ? -23.567  34.186  -65.735  1.00 36.16  ? 721 HOH C O   1 
HETATM 17756 O O   . HOH DA 7 .   ? -8.619   58.732  -65.546  1.00 30.09  ? 722 HOH C O   1 
HETATM 17757 O O   . HOH DA 7 .   ? -10.638  37.675  -48.479  1.00 25.79  ? 723 HOH C O   1 
HETATM 17758 O O   . HOH DA 7 .   ? -37.928  47.746  -68.687  1.00 33.28  ? 724 HOH C O   1 
HETATM 17759 O O   . HOH DA 7 .   ? -36.441  41.707  -71.610  1.00 27.62  ? 725 HOH C O   1 
HETATM 17760 O O   . HOH DA 7 .   ? -21.405  63.606  -61.786  1.00 29.88  ? 726 HOH C O   1 
HETATM 17761 O O   . HOH DA 7 .   ? -9.150   70.234  -69.336  1.00 35.45  ? 727 HOH C O   1 
HETATM 17762 O O   . HOH DA 7 .   ? 5.417    39.335  -74.406  1.00 25.76  ? 728 HOH C O   1 
HETATM 17763 O O   . HOH DA 7 .   ? -33.015  53.703  -46.650  1.00 40.55  ? 729 HOH C O   1 
HETATM 17764 O O   . HOH DA 7 .   ? -21.726  74.117  -60.987  1.00 29.47  ? 730 HOH C O   1 
HETATM 17765 O O   . HOH DA 7 .   ? -41.873  42.112  -57.638  1.00 30.27  ? 731 HOH C O   1 
HETATM 17766 O O   . HOH DA 7 .   ? -29.426  69.508  -52.475  1.00 52.08  ? 732 HOH C O   1 
HETATM 17767 O O   . HOH DA 7 .   ? 13.057   57.304  -62.495  1.00 34.05  ? 733 HOH C O   1 
HETATM 17768 O O   . HOH DA 7 .   ? -36.326  40.947  -63.260  1.00 27.36  ? 734 HOH C O   1 
HETATM 17769 O O   . HOH DA 7 .   ? -11.623  81.203  -61.608  1.00 25.75  ? 735 HOH C O   1 
HETATM 17770 O O   . HOH DA 7 .   ? -13.012  88.476  -56.955  1.00 30.42  ? 736 HOH C O   1 
HETATM 17771 O O   . HOH DA 7 .   ? -7.607   76.424  -73.308  1.00 34.19  ? 737 HOH C O   1 
HETATM 17772 O O   . HOH DA 7 .   ? -18.573  47.465  -71.524  1.00 25.15  ? 738 HOH C O   1 
HETATM 17773 O O   . HOH DA 7 .   ? -10.354  49.647  -65.635  1.00 26.63  ? 739 HOH C O   1 
HETATM 17774 O O   . HOH DA 7 .   ? -16.092  62.927  -65.159  1.00 37.08  ? 740 HOH C O   1 
HETATM 17775 O O   . HOH DA 7 .   ? -10.461  28.466  -62.771  1.00 38.71  ? 741 HOH C O   1 
HETATM 17776 O O   . HOH DA 7 .   ? -23.874  65.120  -68.171  1.00 28.81  ? 742 HOH C O   1 
HETATM 17777 O O   . HOH DA 7 .   ? -12.525  85.040  -54.678  1.00 34.35  ? 743 HOH C O   1 
HETATM 17778 O O   . HOH DA 7 .   ? -44.942  46.517  -55.020  1.00 35.45  ? 744 HOH C O   1 
HETATM 17779 O O   . HOH DA 7 .   ? -41.886  39.602  -41.068  1.00 38.75  ? 745 HOH C O   1 
HETATM 17780 O O   . HOH DA 7 .   ? -6.923   35.726  -54.119  1.00 27.66  ? 746 HOH C O   1 
HETATM 17781 O O   . HOH DA 7 .   ? -4.607   66.320  -58.757  1.00 37.29  ? 747 HOH C O   1 
HETATM 17782 O O   . HOH DA 7 .   ? -18.645  58.661  -68.685  1.00 33.62  ? 748 HOH C O   1 
HETATM 17783 O O   . HOH DA 7 .   ? -10.570  45.928  -60.871  1.00 30.23  ? 749 HOH C O   1 
HETATM 17784 O O   . HOH DA 7 .   ? -9.091   32.454  -56.739  1.00 31.97  ? 750 HOH C O   1 
HETATM 17785 O O   . HOH DA 7 .   ? -34.683  44.838  -47.577  1.00 44.75  ? 751 HOH C O   1 
HETATM 17786 O O   . HOH DA 7 .   ? -17.498  37.596  -58.996  1.00 25.01  ? 752 HOH C O   1 
HETATM 17787 O O   . HOH DA 7 .   ? -15.827  43.500  -68.225  1.00 34.21  ? 753 HOH C O   1 
HETATM 17788 O O   . HOH DA 7 .   ? -37.096  60.175  -64.683  1.00 27.01  ? 754 HOH C O   1 
HETATM 17789 O O   . HOH DA 7 .   ? -9.682   55.900  -62.371  1.00 35.37  ? 755 HOH C O   1 
HETATM 17790 O O   . HOH DA 7 .   ? -27.436  78.617  -58.601  1.00 32.14  ? 756 HOH C O   1 
HETATM 17791 O O   . HOH DA 7 .   ? -36.339  46.852  -59.834  1.00 32.34  ? 757 HOH C O   1 
HETATM 17792 O O   . HOH DA 7 .   ? -30.238  73.874  -50.584  1.00 34.94  ? 758 HOH C O   1 
HETATM 17793 O O   . HOH DA 7 .   ? -13.630  39.415  -57.244  1.00 29.87  ? 759 HOH C O   1 
HETATM 17794 O O   . HOH DA 7 .   ? -22.506  57.041  -62.883  1.00 29.78  ? 760 HOH C O   1 
HETATM 17795 O O   . HOH DA 7 .   ? -28.279  63.059  -49.373  1.00 40.90  ? 761 HOH C O   1 
HETATM 17796 O O   . HOH DA 7 .   ? -25.172  47.217  -34.789  1.00 43.87  ? 762 HOH C O   1 
HETATM 17797 O O   . HOH DA 7 .   ? -21.140  45.363  -73.017  1.00 31.93  ? 763 HOH C O   1 
HETATM 17798 O O   . HOH DA 7 .   ? 1.932    41.492  -74.146  1.00 17.48  ? 764 HOH C O   1 
HETATM 17799 O O   . HOH DA 7 .   ? -35.173  52.122  -63.301  1.00 27.09  ? 765 HOH C O   1 
HETATM 17800 O O   . HOH DA 7 .   ? -15.544  51.023  -69.799  1.00 26.64  ? 766 HOH C O   1 
HETATM 17801 O O   . HOH DA 7 .   ? -40.447  47.249  -74.541  1.00 27.22  ? 767 HOH C O   1 
HETATM 17802 O O   . HOH DA 7 .   ? -29.604  63.007  -71.483  1.00 31.56  ? 768 HOH C O   1 
HETATM 17803 O O   . HOH DA 7 .   ? -14.766  45.850  -47.263  1.00 32.46  ? 769 HOH C O   1 
HETATM 17804 O O   . HOH DA 7 .   ? -10.192  50.872  -52.887  1.00 31.45  ? 770 HOH C O   1 
HETATM 17805 O O   . HOH DA 7 .   ? -24.317  64.891  -61.504  1.00 26.83  ? 771 HOH C O   1 
HETATM 17806 O O   . HOH DA 7 .   ? -27.294  50.563  -55.722  1.00 35.00  ? 772 HOH C O   1 
HETATM 17807 O O   . HOH DA 7 .   ? 10.382   51.102  -67.826  1.00 37.20  ? 773 HOH C O   1 
HETATM 17808 O O   . HOH DA 7 .   ? -42.601  49.560  -61.186  1.00 29.06  ? 774 HOH C O   1 
HETATM 17809 O O   . HOH DA 7 .   ? -23.653  41.162  -63.533  1.00 30.19  ? 775 HOH C O   1 
HETATM 17810 O O   . HOH DA 7 .   ? -23.096  53.910  -78.250  1.00 23.04  ? 776 HOH C O   1 
HETATM 17811 O O   . HOH DA 7 .   ? -23.537  61.504  -56.984  1.00 31.12  ? 777 HOH C O   1 
HETATM 17812 O O   . HOH DA 7 .   ? -38.291  39.494  -71.551  1.00 26.61  ? 778 HOH C O   1 
HETATM 17813 O O   . HOH DA 7 .   ? -19.848  35.578  -49.575  1.00 30.31  ? 779 HOH C O   1 
HETATM 17814 O O   . HOH DA 7 .   ? -8.103   51.164  -66.366  1.00 23.39  ? 780 HOH C O   1 
HETATM 17815 O O   . HOH DA 7 .   ? -22.388  35.993  -50.494  1.00 27.61  ? 781 HOH C O   1 
HETATM 17816 O O   . HOH DA 7 .   ? -51.556  43.906  -69.729  1.00 38.68  ? 782 HOH C O   1 
HETATM 17817 O O   . HOH DA 7 .   ? -20.537  41.770  -35.533  1.00 40.46  ? 783 HOH C O   1 
HETATM 17818 O O   . HOH DA 7 .   ? -18.491  82.287  -52.200  1.00 31.82  ? 784 HOH C O   1 
HETATM 17819 O O   . HOH DA 7 .   ? -21.829  35.247  -57.101  1.00 28.73  ? 785 HOH C O   1 
HETATM 17820 O O   . HOH DA 7 .   ? 1.026    51.336  -73.107  1.00 30.97  ? 786 HOH C O   1 
HETATM 17821 O O   . HOH DA 7 .   ? 13.751   62.911  -54.735  1.00 34.51  ? 787 HOH C O   1 
HETATM 17822 O O   . HOH DA 7 .   ? -38.185  45.123  -61.189  1.00 34.16  ? 788 HOH C O   1 
HETATM 17823 O O   . HOH DA 7 .   ? -40.550  47.962  -63.740  1.00 19.65  ? 789 HOH C O   1 
HETATM 17824 O O   . HOH DA 7 .   ? -35.640  44.381  -52.413  1.00 29.10  ? 790 HOH C O   1 
HETATM 17825 O O   . HOH DA 7 .   ? -4.997   45.869  -70.286  1.00 26.87  ? 791 HOH C O   1 
HETATM 17826 O O   . HOH DA 7 .   ? -28.190  75.214  -50.754  1.00 32.36  ? 792 HOH C O   1 
HETATM 17827 O O   . HOH DA 7 .   ? -25.512  68.926  -56.709  1.00 26.35  ? 793 HOH C O   1 
HETATM 17828 O O   . HOH DA 7 .   ? -19.439  53.842  -74.935  1.00 20.35  ? 794 HOH C O   1 
HETATM 17829 O O   . HOH DA 7 .   ? -15.634  58.616  -47.878  1.00 41.62  ? 795 HOH C O   1 
HETATM 17830 O O   . HOH DA 7 .   ? -11.117  45.217  -67.376  1.00 25.81  ? 796 HOH C O   1 
HETATM 17831 O O   . HOH DA 7 .   ? 1.778    55.056  -70.211  1.00 27.83  ? 797 HOH C O   1 
HETATM 17832 O O   . HOH DA 7 .   ? -38.070  49.607  -52.237  1.00 29.07  ? 798 HOH C O   1 
HETATM 17833 O O   . HOH DA 7 .   ? -12.332  59.552  -63.140  1.00 32.49  ? 799 HOH C O   1 
HETATM 17834 O O   . HOH DA 7 .   ? 15.985   57.651  -64.115  1.00 32.42  ? 800 HOH C O   1 
HETATM 17835 O O   . HOH DA 7 .   ? -18.027  47.828  -78.552  1.00 40.67  ? 801 HOH C O   1 
HETATM 17836 O O   . HOH DA 7 .   ? -43.787  53.185  -55.234  1.00 40.15  ? 802 HOH C O   1 
HETATM 17837 O O   . HOH DA 7 .   ? 6.237    55.085  -71.108  1.00 33.42  ? 803 HOH C O   1 
HETATM 17838 O O   . HOH DA 7 .   ? -47.451  57.550  -69.349  1.00 32.27  ? 804 HOH C O   1 
HETATM 17839 O O   . HOH DA 7 .   ? -16.752  37.401  -52.229  1.00 28.24  ? 805 HOH C O   1 
HETATM 17840 O O   . HOH DA 7 .   ? -33.758  53.033  -75.179  1.00 38.79  ? 806 HOH C O   1 
HETATM 17841 O O   . HOH DA 7 .   ? -14.058  66.255  -52.927  1.00 34.75  ? 807 HOH C O   1 
HETATM 17842 O O   . HOH DA 7 .   ? -10.975  41.621  -70.160  1.00 28.71  ? 808 HOH C O   1 
HETATM 17843 O O   . HOH DA 7 .   ? -18.954  37.457  -55.560  1.00 33.37  ? 809 HOH C O   1 
HETATM 17844 O O   . HOH DA 7 .   ? -20.449  55.710  -70.918  1.00 26.94  ? 810 HOH C O   1 
HETATM 17845 O O   . HOH DA 7 .   ? -28.149  74.716  -57.260  1.00 41.31  ? 811 HOH C O   1 
HETATM 17846 O O   . HOH DA 7 .   ? -20.528  44.721  -57.482  1.00 26.84  ? 812 HOH C O   1 
HETATM 17847 O O   . HOH DA 7 .   ? 11.154   49.309  -72.573  1.00 30.67  ? 813 HOH C O   1 
HETATM 17848 O O   . HOH DA 7 .   ? 9.257    46.266  -69.321  1.00 34.44  ? 814 HOH C O   1 
HETATM 17849 O O   . HOH DA 7 .   ? -39.073  43.994  -58.695  1.00 19.81  ? 815 HOH C O   1 
HETATM 17850 O O   . HOH DA 7 .   ? -32.400  75.639  -51.265  1.00 33.29  ? 816 HOH C O   1 
HETATM 17851 O O   . HOH DA 7 .   ? -18.256  37.565  -61.402  1.00 30.44  ? 817 HOH C O   1 
HETATM 17852 O O   . HOH DA 7 .   ? -23.182  40.664  -35.484  1.00 32.62  ? 818 HOH C O   1 
HETATM 17853 O O   . HOH DA 7 .   ? -28.292  75.253  -61.809  1.00 36.33  ? 819 HOH C O   1 
HETATM 17854 O O   . HOH DA 7 .   ? -40.466  49.336  -72.665  1.00 33.08  ? 820 HOH C O   1 
HETATM 17855 O O   . HOH DA 7 .   ? -26.130  47.666  -71.349  1.00 26.74  ? 821 HOH C O   1 
HETATM 17856 O O   . HOH DA 7 .   ? -12.444  51.948  -47.588  1.00 34.55  ? 822 HOH C O   1 
HETATM 17857 O O   . HOH DA 7 .   ? 0.031    50.741  -54.970  1.00 36.24  ? 823 HOH C O   1 
HETATM 17858 O O   . HOH DA 7 .   ? -44.731  39.420  -70.700  1.00 23.61  ? 824 HOH C O   1 
HETATM 17859 O O   . HOH DA 7 .   ? 2.293    47.754  -70.956  1.00 34.01  ? 825 HOH C O   1 
HETATM 17860 O O   . HOH DA 7 .   ? 2.514    52.445  -71.006  1.00 32.35  ? 826 HOH C O   1 
HETATM 17861 O O   . HOH DA 7 .   ? -31.235  53.368  -48.849  1.00 37.34  ? 827 HOH C O   1 
HETATM 17862 O O   . HOH DA 7 .   ? -14.509  67.963  -67.644  1.00 44.91  ? 828 HOH C O   1 
HETATM 17863 O O   . HOH DA 7 .   ? -1.698   59.010  -56.366  1.00 31.06  ? 829 HOH C O   1 
HETATM 17864 O O   . HOH DA 7 .   ? -36.887  45.858  -50.453  1.00 23.73  ? 830 HOH C O   1 
HETATM 17865 O O   . HOH DA 7 .   ? 8.613    38.660  -69.933  1.00 25.51  ? 831 HOH C O   1 
HETATM 17866 O O   . HOH DA 7 .   ? -1.898   42.162  -71.315  1.00 24.67  ? 832 HOH C O   1 
HETATM 17867 O O   . HOH DA 7 .   ? -23.157  76.349  -40.846  1.00 41.75  ? 833 HOH C O   1 
HETATM 17868 O O   . HOH DA 7 .   ? -3.837   43.263  -69.765  1.00 18.32  ? 834 HOH C O   1 
HETATM 17869 O O   . HOH DA 7 .   ? -10.466  62.422  -61.379  1.00 31.43  ? 835 HOH C O   1 
HETATM 17870 O O   . HOH DA 7 .   ? -5.295   68.645  -57.573  1.00 31.76  ? 836 HOH C O   1 
HETATM 17871 O O   . HOH DA 7 .   ? 9.575    48.951  -64.785  1.00 40.96  ? 837 HOH C O   1 
HETATM 17872 O O   . HOH DA 7 .   ? -46.454  37.547  -52.577  1.00 32.38  ? 838 HOH C O   1 
HETATM 17873 O O   . HOH DA 7 .   ? -35.806  48.001  -51.788  1.00 25.99  ? 839 HOH C O   1 
HETATM 17874 O O   . HOH DA 7 .   ? -3.529   40.562  -73.039  1.00 36.47  ? 840 HOH C O   1 
HETATM 17875 O O   . HOH DA 7 .   ? -26.988  67.111  -58.255  1.00 25.24  ? 841 HOH C O   1 
HETATM 17876 O O   . HOH DA 7 .   ? 6.396    37.991  -59.443  1.00 30.40  ? 842 HOH C O   1 
HETATM 17877 O O   . HOH DA 7 .   ? -28.902  34.421  -65.164  1.00 38.20  ? 843 HOH C O   1 
HETATM 17878 O O   . HOH DA 7 .   ? -18.075  77.872  -44.230  1.00 38.63  ? 844 HOH C O   1 
HETATM 17879 O O   . HOH DA 7 .   ? -44.197  37.369  -67.230  1.00 23.06  ? 845 HOH C O   1 
HETATM 17880 O O   . HOH DA 7 .   ? -14.160  39.780  -38.660  1.00 43.29  ? 846 HOH C O   1 
HETATM 17881 O O   . HOH DA 7 .   ? -1.905   53.149  -55.776  1.00 30.26  ? 847 HOH C O   1 
HETATM 17882 O O   . HOH DA 7 .   ? -24.456  33.439  -43.555  1.00 33.44  ? 848 HOH C O   1 
HETATM 17883 O O   . HOH DA 7 .   ? -13.760  61.528  -64.541  1.00 40.33  ? 849 HOH C O   1 
HETATM 17884 O O   . HOH DA 7 .   ? -12.372  70.902  -49.717  1.00 36.92  ? 850 HOH C O   1 
HETATM 17885 O O   . HOH DA 7 .   ? 2.785    46.892  -74.396  1.00 34.65  ? 851 HOH C O   1 
HETATM 17886 O O   . HOH DA 7 .   ? -4.452   57.807  -56.314  1.00 24.46  ? 852 HOH C O   1 
HETATM 17887 O O   . HOH DA 7 .   ? -12.701  51.151  -66.359  1.00 32.56  ? 853 HOH C O   1 
HETATM 17888 O O   . HOH DA 7 .   ? -8.250   48.281  -69.199  1.00 27.49  ? 854 HOH C O   1 
HETATM 17889 O O   . HOH DA 7 .   ? 2.151    45.294  -71.936  1.00 29.45  ? 855 HOH C O   1 
HETATM 17890 O O   . HOH DA 7 .   ? -15.894  36.489  -54.636  1.00 30.07  ? 856 HOH C O   1 
HETATM 17891 O O   . HOH DA 7 .   ? -5.724   52.013  -70.147  1.00 36.41  ? 857 HOH C O   1 
HETATM 17892 O O   . HOH DA 7 .   ? -28.292  65.878  -63.250  1.00 36.50  ? 858 HOH C O   1 
HETATM 17893 O O   . HOH DA 7 .   ? -33.721  46.461  -58.877  1.00 30.71  ? 859 HOH C O   1 
HETATM 17894 O O   . HOH DA 7 .   ? -43.894  35.828  -56.783  1.00 29.69  ? 860 HOH C O   1 
HETATM 17895 O O   . HOH DA 7 .   ? 4.970    52.746  -72.234  1.00 39.80  ? 861 HOH C O   1 
HETATM 17896 O O   . HOH DA 7 .   ? -10.373  29.357  -52.872  1.00 36.96  ? 862 HOH C O   1 
HETATM 17897 O O   . HOH DA 7 .   ? -42.037  41.843  -35.586  1.00 37.19  ? 863 HOH C O   1 
HETATM 17898 O O   . HOH DA 7 .   ? -28.594  59.232  -61.442  1.00 26.32  ? 864 HOH C O   1 
HETATM 17899 O O   . HOH DA 7 .   ? -30.302  66.155  -62.396  1.00 37.10  ? 865 HOH C O   1 
HETATM 17900 O O   . HOH DA 7 .   ? -18.823  33.754  -65.514  1.00 36.24  ? 866 HOH C O   1 
HETATM 17901 O O   . HOH DA 7 .   ? -46.457  36.673  -65.994  1.00 26.47  ? 867 HOH C O   1 
HETATM 17902 O O   . HOH DA 7 .   ? -8.367   61.835  -62.172  1.00 34.79  ? 868 HOH C O   1 
HETATM 17903 O O   . HOH DA 7 .   ? -9.659   58.574  -63.155  1.00 30.02  ? 869 HOH C O   1 
HETATM 17904 O O   . HOH DA 7 .   ? -30.543  60.204  -57.826  1.00 32.75  ? 870 HOH C O   1 
HETATM 17905 O O   . HOH DA 7 .   ? -18.240  56.337  -68.916  1.00 31.18  ? 871 HOH C O   1 
HETATM 17906 O O   . HOH DA 7 .   ? -29.321  76.124  -59.669  1.00 25.01  ? 872 HOH C O   1 
HETATM 17907 O O   . HOH DA 7 .   ? -7.582   46.122  -70.931  1.00 25.72  ? 873 HOH C O   1 
HETATM 17908 O O   . HOH DA 7 .   ? -10.811  48.006  -67.527  1.00 34.23  ? 874 HOH C O   1 
HETATM 17909 O O   . HOH DA 7 .   ? 0.504    43.355  -72.485  1.00 27.40  ? 875 HOH C O   1 
HETATM 17910 O O   . HOH DA 7 .   ? -4.020   62.377  -58.763  1.00 40.13  ? 876 HOH C O   1 
HETATM 17911 O O   . HOH DA 7 .   ? -32.829  50.776  -75.223  1.00 34.29  ? 877 HOH C O   1 
HETATM 17912 O O   . HOH DA 7 .   ? -43.366  30.240  -60.108  1.00 39.00  ? 878 HOH C O   1 
HETATM 17913 O O   . HOH DA 7 .   ? -18.917  41.738  -33.514  1.00 46.76  ? 879 HOH C O   1 
HETATM 17914 O O   . HOH DA 7 .   ? -7.967   51.244  -68.747  1.00 33.36  ? 880 HOH C O   1 
HETATM 17915 O O   . HOH DA 7 .   ? -13.162  51.304  -68.757  1.00 28.41  ? 881 HOH C O   1 
HETATM 17916 O O   . HOH DA 7 .   ? -19.910  48.156  -35.878  1.00 42.69  ? 882 HOH C O   1 
HETATM 17917 O O   . HOH DA 7 .   ? -18.611  34.895  -62.918  1.00 43.72  ? 883 HOH C O   1 
HETATM 17918 O O   . HOH DA 7 .   ? -20.518  54.093  -77.246  1.00 32.78  ? 884 HOH C O   1 
HETATM 17919 O O   . HOH DA 7 .   ? 10.711   46.603  -71.404  1.00 23.29  ? 885 HOH C O   1 
HETATM 17920 O O   . HOH DA 7 .   ? -25.966  64.900  -59.432  1.00 29.01  ? 886 HOH C O   1 
HETATM 17921 O O   . HOH DA 7 .   ? -19.206  55.999  -73.307  1.00 37.79  ? 887 HOH C O   1 
HETATM 17922 O O   . HOH DA 7 .   ? -32.065  76.242  -60.029  1.00 35.72  ? 888 HOH C O   1 
HETATM 17923 O O   . HOH EA 7 .   ? -22.868  10.878  -21.694  1.00 22.07  ? 701 HOH D O   1 
HETATM 17924 O O   . HOH EA 7 .   ? -34.048  5.555   -30.487  1.00 29.63  ? 702 HOH D O   1 
HETATM 17925 O O   . HOH EA 7 .   ? -60.870  21.567  -8.864   1.00 35.04  ? 703 HOH D O   1 
HETATM 17926 O O   . HOH EA 7 .   ? -47.457  12.506  -9.273   1.00 25.52  ? 704 HOH D O   1 
HETATM 17927 O O   . HOH EA 7 .   ? -38.111  36.542  -25.398  1.00 34.84  ? 705 HOH D O   1 
HETATM 17928 O O   . HOH EA 7 .   ? -64.497  24.227  -7.366   1.00 27.53  ? 706 HOH D O   1 
HETATM 17929 O O   . HOH EA 7 .   ? -41.917  3.380   -4.362   1.00 25.26  ? 707 HOH D O   1 
HETATM 17930 O O   . HOH EA 7 .   ? -56.854  26.805  -28.755  1.00 35.95  ? 708 HOH D O   1 
HETATM 17931 O O   . HOH EA 7 .   ? -47.941  23.267  -6.111   1.00 36.31  ? 709 HOH D O   1 
HETATM 17932 O O   . HOH EA 7 .   ? -51.418  -8.394  -24.159  1.00 35.46  ? 710 HOH D O   1 
HETATM 17933 O O   . HOH EA 7 .   ? -30.090  -3.228  -19.910  1.00 30.33  ? 711 HOH D O   1 
HETATM 17934 O O   . HOH EA 7 .   ? -37.487  26.557  -36.129  1.00 31.60  ? 712 HOH D O   1 
HETATM 17935 O O   . HOH EA 7 .   ? -59.871  -7.030  -21.038  1.00 32.38  ? 713 HOH D O   1 
HETATM 17936 O O   . HOH EA 7 .   ? -55.346  44.058  -14.502  1.00 33.91  ? 714 HOH D O   1 
HETATM 17937 O O   . HOH EA 7 .   ? -40.687  31.606  -29.166  1.00 25.46  ? 715 HOH D O   1 
HETATM 17938 O O   . HOH EA 7 .   ? -51.824  27.112  -37.604  1.00 34.83  ? 716 HOH D O   1 
HETATM 17939 O O   . HOH EA 7 .   ? -52.900  19.379  -27.054  1.00 22.64  ? 717 HOH D O   1 
HETATM 17940 O O   . HOH EA 7 .   ? -47.811  13.490  -50.910  1.00 37.55  ? 718 HOH D O   1 
HETATM 17941 O O   . HOH EA 7 .   ? -45.298  7.059   -4.261   1.00 29.06  ? 719 HOH D O   1 
HETATM 17942 O O   . HOH EA 7 .   ? -49.475  13.582  -6.986   1.00 32.50  ? 720 HOH D O   1 
HETATM 17943 O O   . HOH EA 7 .   ? -46.138  20.425  -44.640  1.00 35.60  ? 721 HOH D O   1 
HETATM 17944 O O   . HOH EA 7 .   ? -54.009  1.289   -9.573   1.00 26.28  ? 722 HOH D O   1 
HETATM 17945 O O   . HOH EA 7 .   ? -48.545  -10.577 -10.881  1.00 42.88  ? 723 HOH D O   1 
HETATM 17946 O O   . HOH EA 7 .   ? -39.941  14.011  -26.749  1.00 30.58  ? 724 HOH D O   1 
HETATM 17947 O O   . HOH EA 7 .   ? -42.248  26.241  -22.404  1.00 20.05  ? 725 HOH D O   1 
HETATM 17948 O O   . HOH EA 7 .   ? -38.099  7.486   -14.830  1.00 25.35  ? 726 HOH D O   1 
HETATM 17949 O O   . HOH EA 7 .   ? -54.302  11.257  -7.910   1.00 21.34  ? 727 HOH D O   1 
HETATM 17950 O O   . HOH EA 7 .   ? -33.142  2.463   -31.218  1.00 29.84  ? 728 HOH D O   1 
HETATM 17951 O O   . HOH EA 7 .   ? -64.354  10.330  6.862    1.00 30.28  ? 729 HOH D O   1 
HETATM 17952 O O   . HOH EA 7 .   ? -35.684  16.113  -24.018  1.00 33.52  ? 730 HOH D O   1 
HETATM 17953 O O   . HOH EA 7 .   ? -42.065  34.391  -19.768  1.00 30.90  ? 731 HOH D O   1 
HETATM 17954 O O   . HOH EA 7 .   ? -62.380  0.218   12.444   1.00 24.93  ? 732 HOH D O   1 
HETATM 17955 O O   . HOH EA 7 .   ? -71.533  9.858   -3.454   1.00 42.41  ? 733 HOH D O   1 
HETATM 17956 O O   . HOH EA 7 .   ? -29.230  16.158  -19.598  1.00 18.76  ? 734 HOH D O   1 
HETATM 17957 O O   . HOH EA 7 .   ? -40.997  15.277  -23.679  1.00 30.99  ? 735 HOH D O   1 
HETATM 17958 O O   . HOH EA 7 .   ? -51.502  45.277  -21.623  1.00 32.82  ? 736 HOH D O   1 
HETATM 17959 O O   . HOH EA 7 .   ? -44.679  18.855  -28.767  1.00 30.66  ? 737 HOH D O   1 
HETATM 17960 O O   . HOH EA 7 .   ? -60.361  7.632   -32.661  1.00 40.10  ? 738 HOH D O   1 
HETATM 17961 O O   . HOH EA 7 .   ? -38.509  15.317  -18.158  1.00 28.12  ? 739 HOH D O   1 
HETATM 17962 O O   . HOH EA 7 .   ? -39.952  -2.146  -47.472  1.00 38.51  ? 740 HOH D O   1 
HETATM 17963 O O   . HOH EA 7 .   ? -51.826  5.016   -5.619   1.00 27.18  ? 741 HOH D O   1 
HETATM 17964 O O   . HOH EA 7 .   ? -49.775  27.910  -16.578  1.00 25.44  ? 742 HOH D O   1 
HETATM 17965 O O   . HOH EA 7 .   ? -25.818  5.389   -25.036  1.00 29.99  ? 743 HOH D O   1 
HETATM 17966 O O   . HOH EA 7 .   ? -47.167  41.819  -27.119  1.00 38.33  ? 744 HOH D O   1 
HETATM 17967 O O   . HOH EA 7 .   ? -45.644  -8.760  -18.451  1.00 31.66  ? 745 HOH D O   1 
HETATM 17968 O O   . HOH EA 7 .   ? -39.440  0.620   -33.336  1.00 35.32  ? 746 HOH D O   1 
HETATM 17969 O O   . HOH EA 7 .   ? -45.062  29.834  -15.378  1.00 38.93  ? 747 HOH D O   1 
HETATM 17970 O O   . HOH EA 7 .   ? -65.797  0.318   10.764   1.00 27.71  ? 748 HOH D O   1 
HETATM 17971 O O   . HOH EA 7 .   ? -20.377  1.763   -35.140  1.00 45.35  ? 749 HOH D O   1 
HETATM 17972 O O   . HOH EA 7 .   ? -53.237  40.670  -33.910  1.00 31.65  ? 750 HOH D O   1 
HETATM 17973 O O   . HOH EA 7 .   ? -39.837  12.184  -34.684  1.00 26.37  ? 751 HOH D O   1 
HETATM 17974 O O   . HOH EA 7 .   ? -43.770  37.372  -17.794  1.00 35.32  ? 752 HOH D O   1 
HETATM 17975 O O   . HOH EA 7 .   ? -31.625  5.357   -23.995  1.00 31.42  ? 753 HOH D O   1 
HETATM 17976 O O   . HOH EA 7 .   ? -41.472  -3.101  -13.657  1.00 31.65  ? 754 HOH D O   1 
HETATM 17977 O O   . HOH EA 7 .   ? -48.809  -7.021  -18.613  1.00 42.35  ? 755 HOH D O   1 
HETATM 17978 O O   . HOH EA 7 .   ? -21.734  14.029  -27.619  1.00 36.78  ? 756 HOH D O   1 
HETATM 17979 O O   . HOH EA 7 .   ? -53.940  36.788  -9.718   1.00 27.41  ? 757 HOH D O   1 
HETATM 17980 O O   . HOH EA 7 .   ? -31.491  7.908   -19.828  1.00 25.01  ? 758 HOH D O   1 
HETATM 17981 O O   . HOH EA 7 .   ? -32.959  14.249  -4.042   1.00 26.80  ? 759 HOH D O   1 
HETATM 17982 O O   . HOH EA 7 .   ? -48.945  -10.054 -30.094  1.00 36.85  ? 760 HOH D O   1 
HETATM 17983 O O   . HOH EA 7 .   ? -46.705  30.938  -38.007  1.00 29.52  ? 761 HOH D O   1 
HETATM 17984 O O   . HOH EA 7 .   ? -48.358  -8.286  -24.605  1.00 27.58  ? 762 HOH D O   1 
HETATM 17985 O O   . HOH EA 7 .   ? -53.733  14.361  -5.145   1.00 27.54  ? 763 HOH D O   1 
HETATM 17986 O O   . HOH EA 7 .   ? -62.871  35.362  -12.422  1.00 36.00  ? 764 HOH D O   1 
HETATM 17987 O O   . HOH EA 7 .   ? -58.211  6.325   -16.648  1.00 31.32  ? 765 HOH D O   1 
HETATM 17988 O O   . HOH EA 7 .   ? -41.371  30.552  -21.531  1.00 30.54  ? 766 HOH D O   1 
HETATM 17989 O O   . HOH EA 7 .   ? -52.383  -4.980  -34.407  1.00 32.38  ? 767 HOH D O   1 
HETATM 17990 O O   . HOH EA 7 .   ? -35.583  3.578   -8.315   1.00 21.64  ? 768 HOH D O   1 
HETATM 17991 O O   . HOH EA 7 .   ? -71.115  11.680  -8.659   1.00 34.06  ? 769 HOH D O   1 
HETATM 17992 O O   . HOH EA 7 .   ? -26.088  -2.355  -12.783  1.00 26.09  ? 770 HOH D O   1 
HETATM 17993 O O   . HOH EA 7 .   ? -56.355  33.401  -28.088  1.00 27.55  ? 771 HOH D O   1 
HETATM 17994 O O   . HOH EA 7 .   ? -37.410  31.418  -34.332  1.00 39.47  ? 772 HOH D O   1 
HETATM 17995 O O   . HOH EA 7 .   ? -60.597  3.245   5.066    1.00 32.05  ? 773 HOH D O   1 
HETATM 17996 O O   . HOH EA 7 .   ? -43.063  12.827  -13.918  1.00 24.82  ? 774 HOH D O   1 
HETATM 17997 O O   . HOH EA 7 .   ? -44.381  19.474  -14.767  1.00 20.99  ? 775 HOH D O   1 
HETATM 17998 O O   . HOH EA 7 .   ? -64.263  7.894   -14.296  1.00 35.23  ? 776 HOH D O   1 
HETATM 17999 O O   . HOH EA 7 .   ? -66.542  -8.811  -25.246  1.00 40.59  ? 777 HOH D O   1 
HETATM 18000 O O   . HOH EA 7 .   ? -32.499  18.762  -10.061  1.00 30.63  ? 778 HOH D O   1 
HETATM 18001 O O   . HOH EA 7 .   ? -61.243  -4.857  -31.168  1.00 33.42  ? 779 HOH D O   1 
HETATM 18002 O O   . HOH EA 7 .   ? -64.351  14.543  -9.599   1.00 28.03  ? 780 HOH D O   1 
HETATM 18003 O O   . HOH EA 7 .   ? -60.566  11.578  -24.246  1.00 36.31  ? 781 HOH D O   1 
HETATM 18004 O O   . HOH EA 7 .   ? -52.933  20.321  -34.727  1.00 31.11  ? 782 HOH D O   1 
HETATM 18005 O O   . HOH EA 7 .   ? -45.627  -0.641  -5.743   1.00 32.60  ? 783 HOH D O   1 
HETATM 18006 O O   . HOH EA 7 .   ? -48.052  15.814  -7.563   1.00 34.25  ? 784 HOH D O   1 
HETATM 18007 O O   . HOH EA 7 .   ? -51.879  -7.604  -31.372  1.00 31.48  ? 785 HOH D O   1 
HETATM 18008 O O   . HOH EA 7 .   ? -35.923  5.979   -47.079  1.00 29.88  ? 786 HOH D O   1 
HETATM 18009 O O   . HOH EA 7 .   ? -52.408  37.591  -21.274  1.00 24.01  ? 787 HOH D O   1 
HETATM 18010 O O   . HOH EA 7 .   ? -47.718  12.286  -26.776  1.00 26.89  ? 788 HOH D O   1 
HETATM 18011 O O   . HOH EA 7 .   ? -34.927  9.766   -0.719   1.00 17.99  ? 789 HOH D O   1 
HETATM 18012 O O   . HOH EA 7 .   ? -49.845  4.095   -47.648  1.00 38.08  ? 790 HOH D O   1 
HETATM 18013 O O   . HOH EA 7 .   ? -42.000  20.432  -16.150  1.00 29.81  ? 791 HOH D O   1 
HETATM 18014 O O   . HOH EA 7 .   ? -44.956  41.499  -26.253  1.00 27.14  ? 792 HOH D O   1 
HETATM 18015 O O   . HOH EA 7 .   ? -41.073  3.992   -50.138  1.00 40.70  ? 793 HOH D O   1 
HETATM 18016 O O   . HOH EA 7 .   ? -46.646  -6.988  -12.889  1.00 29.33  ? 794 HOH D O   1 
HETATM 18017 O O   . HOH EA 7 .   ? -36.285  0.223   -29.390  1.00 25.83  ? 795 HOH D O   1 
HETATM 18018 O O   . HOH EA 7 .   ? -41.414  20.735  -18.583  1.00 24.31  ? 796 HOH D O   1 
HETATM 18019 O O   . HOH EA 7 .   ? -47.074  0.537   -17.596  1.00 28.18  ? 797 HOH D O   1 
HETATM 18020 O O   . HOH EA 7 .   ? -61.903  12.975  -10.895  1.00 13.71  ? 798 HOH D O   1 
HETATM 18021 O O   . HOH EA 7 .   ? -29.787  1.275   -22.721  1.00 22.57  ? 799 HOH D O   1 
HETATM 18022 O O   . HOH EA 7 .   ? -66.240  5.986   -10.279  1.00 33.62  ? 800 HOH D O   1 
HETATM 18023 O O   . HOH EA 7 .   ? -58.041  24.580  -14.540  1.00 28.94  ? 801 HOH D O   1 
HETATM 18024 O O   . HOH EA 7 .   ? -26.303  3.652   -16.200  1.00 25.77  ? 802 HOH D O   1 
HETATM 18025 O O   . HOH EA 7 .   ? -60.126  17.596  -30.065  1.00 34.23  ? 803 HOH D O   1 
HETATM 18026 O O   . HOH EA 7 .   ? -39.429  13.795  -7.188   1.00 26.51  ? 804 HOH D O   1 
HETATM 18027 O O   . HOH EA 7 .   ? -38.524  33.068  -31.496  1.00 34.37  ? 805 HOH D O   1 
HETATM 18028 O O   . HOH EA 7 .   ? -53.800  6.569   -3.967   1.00 27.66  ? 806 HOH D O   1 
HETATM 18029 O O   . HOH EA 7 .   ? -36.498  8.653   -47.312  1.00 31.48  ? 807 HOH D O   1 
HETATM 18030 O O   . HOH EA 7 .   ? -39.089  20.718  -9.999   1.00 22.88  ? 808 HOH D O   1 
HETATM 18031 O O   . HOH EA 7 .   ? -58.440  20.729  -14.664  1.00 30.47  ? 809 HOH D O   1 
HETATM 18032 O O   . HOH EA 7 .   ? -53.071  -4.892  -14.555  1.00 27.90  ? 810 HOH D O   1 
HETATM 18033 O O   . HOH EA 7 .   ? -28.072  -2.169  -28.099  1.00 28.81  ? 811 HOH D O   1 
HETATM 18034 O O   . HOH EA 7 .   ? -43.925  34.703  -18.104  1.00 38.84  ? 812 HOH D O   1 
HETATM 18035 O O   . HOH EA 7 .   ? -60.838  10.329  4.442    1.00 28.28  ? 813 HOH D O   1 
HETATM 18036 O O   . HOH EA 7 .   ? -53.922  2.445   -39.656  1.00 33.94  ? 814 HOH D O   1 
HETATM 18037 O O   . HOH EA 7 .   ? -58.202  41.548  -23.018  1.00 30.58  ? 815 HOH D O   1 
HETATM 18038 O O   . HOH EA 7 .   ? -52.544  -16.026 -8.135   1.00 39.73  ? 816 HOH D O   1 
HETATM 18039 O O   . HOH EA 7 .   ? -41.259  20.170  -6.480   1.00 32.52  ? 817 HOH D O   1 
HETATM 18040 O O   . HOH EA 7 .   ? -56.873  40.421  -16.043  1.00 33.97  ? 818 HOH D O   1 
HETATM 18041 O O   . HOH EA 7 .   ? -42.196  18.063  -19.268  1.00 25.17  ? 819 HOH D O   1 
HETATM 18042 O O   . HOH EA 7 .   ? -56.375  13.827  -24.113  1.00 34.09  ? 820 HOH D O   1 
HETATM 18043 O O   . HOH EA 7 .   ? -40.666  26.766  -28.509  1.00 36.24  ? 821 HOH D O   1 
HETATM 18044 O O   . HOH EA 7 .   ? -57.267  40.235  -26.549  1.00 30.00  ? 822 HOH D O   1 
HETATM 18045 O O   . HOH EA 7 .   ? -60.562  10.022  -22.206  1.00 27.25  ? 823 HOH D O   1 
HETATM 18046 O O   . HOH EA 7 .   ? -51.560  31.915  2.671    1.00 38.20  ? 824 HOH D O   1 
HETATM 18047 O O   . HOH EA 7 .   ? -58.568  6.681   6.242    1.00 28.85  ? 825 HOH D O   1 
HETATM 18048 O O   . HOH EA 7 .   ? -24.619  -4.553  -13.756  1.00 27.14  ? 826 HOH D O   1 
HETATM 18049 O O   . HOH EA 7 .   ? -56.662  -2.580  3.197    1.00 29.62  ? 827 HOH D O   1 
HETATM 18050 O O   . HOH EA 7 .   ? -55.718  -1.409  1.143    1.00 21.36  ? 828 HOH D O   1 
HETATM 18051 O O   . HOH EA 7 .   ? -40.660  11.619  -6.211   1.00 23.96  ? 829 HOH D O   1 
HETATM 18052 O O   . HOH EA 7 .   ? -58.746  -3.174  7.895    1.00 24.16  ? 830 HOH D O   1 
HETATM 18053 O O   . HOH EA 7 .   ? -57.217  -3.142  -36.311  1.00 29.88  ? 831 HOH D O   1 
HETATM 18054 O O   . HOH EA 7 .   ? -50.215  28.666  -40.749  1.00 27.03  ? 832 HOH D O   1 
HETATM 18055 O O   . HOH EA 7 .   ? -62.889  14.301  -16.833  1.00 41.59  ? 833 HOH D O   1 
HETATM 18056 O O   . HOH EA 7 .   ? -61.941  21.542  -18.414  1.00 42.30  ? 834 HOH D O   1 
HETATM 18057 O O   . HOH EA 7 .   ? -39.317  21.082  -33.295  1.00 29.62  ? 835 HOH D O   1 
HETATM 18058 O O   . HOH EA 7 .   ? -51.224  10.826  -47.432  1.00 38.80  ? 836 HOH D O   1 
HETATM 18059 O O   . HOH EA 7 .   ? -33.065  -2.466  -7.180   1.00 34.03  ? 837 HOH D O   1 
HETATM 18060 O O   . HOH EA 7 .   ? -44.653  30.821  -27.300  1.00 29.40  ? 838 HOH D O   1 
HETATM 18061 O O   . HOH EA 7 .   ? -55.446  -3.995  -38.039  1.00 31.67  ? 839 HOH D O   1 
HETATM 18062 O O   . HOH EA 7 .   ? -59.583  35.492  -19.431  1.00 26.12  ? 840 HOH D O   1 
HETATM 18063 O O   . HOH EA 7 .   ? -41.990  6.275   -22.519  1.00 28.96  ? 841 HOH D O   1 
HETATM 18064 O O   . HOH EA 7 .   ? -54.277  7.490   0.671    1.00 27.68  ? 842 HOH D O   1 
HETATM 18065 O O   . HOH EA 7 .   ? -55.154  35.727  -30.960  1.00 38.17  ? 843 HOH D O   1 
HETATM 18066 O O   . HOH EA 7 .   ? -18.143  9.405   -25.591  1.00 45.23  ? 844 HOH D O   1 
HETATM 18067 O O   . HOH EA 7 .   ? -59.139  7.308   -22.273  1.00 20.63  ? 845 HOH D O   1 
HETATM 18068 O O   . HOH EA 7 .   ? -26.284  3.979   -21.939  1.00 33.79  ? 846 HOH D O   1 
HETATM 18069 O O   . HOH EA 7 .   ? -51.915  15.091  -9.190   1.00 27.65  ? 847 HOH D O   1 
HETATM 18070 O O   . HOH EA 7 .   ? -38.946  1.037   -4.327   1.00 27.10  ? 848 HOH D O   1 
HETATM 18071 O O   . HOH EA 7 .   ? -54.600  1.067   1.007    1.00 26.86  ? 849 HOH D O   1 
HETATM 18072 O O   . HOH EA 7 .   ? -21.998  5.229   -14.243  1.00 22.54  ? 850 HOH D O   1 
HETATM 18073 O O   . HOH EA 7 .   ? -48.742  29.450  -38.625  1.00 24.77  ? 851 HOH D O   1 
HETATM 18074 O O   . HOH EA 7 .   ? -57.085  1.276   -23.808  1.00 36.79  ? 852 HOH D O   1 
HETATM 18075 O O   . HOH EA 7 .   ? -66.254  -6.278  7.010    1.00 30.68  ? 853 HOH D O   1 
HETATM 18076 O O   . HOH EA 7 .   ? -27.917  9.065   -30.973  1.00 40.84  ? 854 HOH D O   1 
HETATM 18077 O O   . HOH EA 7 .   ? -36.349  -4.745  -42.722  1.00 32.45  ? 855 HOH D O   1 
HETATM 18078 O O   . HOH EA 7 .   ? -47.479  18.990  -8.800   1.00 34.93  ? 856 HOH D O   1 
HETATM 18079 O O   . HOH EA 7 .   ? -39.617  9.569   -1.871   1.00 23.12  ? 857 HOH D O   1 
HETATM 18080 O O   . HOH EA 7 .   ? -55.613  21.758  -18.340  1.00 22.65  ? 858 HOH D O   1 
HETATM 18081 O O   . HOH EA 7 .   ? -48.609  -6.741  -14.603  1.00 35.40  ? 859 HOH D O   1 
HETATM 18082 O O   . HOH EA 7 .   ? -41.833  25.037  -26.694  1.00 38.30  ? 860 HOH D O   1 
HETATM 18083 O O   . HOH EA 7 .   ? -52.501  -7.136  -20.231  1.00 29.48  ? 861 HOH D O   1 
HETATM 18084 O O   . HOH EA 7 .   ? -59.855  28.645  4.383    1.00 30.80  ? 862 HOH D O   1 
HETATM 18085 O O   . HOH EA 7 .   ? -43.657  24.771  -20.748  1.00 27.81  ? 863 HOH D O   1 
HETATM 18086 O O   . HOH EA 7 .   ? -40.779  31.838  -35.352  1.00 33.14  ? 864 HOH D O   1 
HETATM 18087 O O   . HOH EA 7 .   ? -32.096  12.515  -25.714  1.00 28.72  ? 865 HOH D O   1 
HETATM 18088 O O   . HOH EA 7 .   ? -45.498  22.677  -29.518  1.00 25.07  ? 866 HOH D O   1 
HETATM 18089 O O   . HOH EA 7 .   ? -41.942  9.063   -30.521  1.00 39.79  ? 867 HOH D O   1 
HETATM 18090 O O   . HOH EA 7 .   ? -26.929  -7.732  -29.767  1.00 32.32  ? 868 HOH D O   1 
HETATM 18091 O O   . HOH EA 7 .   ? -60.362  -8.763  -14.071  1.00 24.38  ? 869 HOH D O   1 
HETATM 18092 O O   . HOH EA 7 .   ? -64.223  8.356   -9.890   1.00 28.04  ? 870 HOH D O   1 
HETATM 18093 O O   . HOH EA 7 .   ? -53.886  -5.436  -36.610  1.00 37.33  ? 871 HOH D O   1 
HETATM 18094 O O   . HOH EA 7 .   ? -37.363  27.356  -33.550  1.00 29.19  ? 872 HOH D O   1 
HETATM 18095 O O   . HOH EA 7 .   ? -45.189  17.175  -19.470  1.00 24.91  ? 873 HOH D O   1 
HETATM 18096 O O   . HOH EA 7 .   ? -61.074  7.796   5.280    1.00 29.52  ? 874 HOH D O   1 
HETATM 18097 O O   . HOH EA 7 .   ? -46.391  -10.008 -29.872  1.00 34.10  ? 875 HOH D O   1 
HETATM 18098 O O   . HOH EA 7 .   ? -37.700  21.559  -16.365  1.00 33.75  ? 876 HOH D O   1 
HETATM 18099 O O   . HOH EA 7 .   ? -42.424  29.543  -28.592  1.00 32.07  ? 877 HOH D O   1 
HETATM 18100 O O   . HOH EA 7 .   ? -58.664  29.041  -22.658  1.00 36.72  ? 878 HOH D O   1 
HETATM 18101 O O   . HOH EA 7 .   ? -50.484  1.035   -4.239   1.00 36.22  ? 879 HOH D O   1 
HETATM 18102 O O   . HOH EA 7 .   ? -41.416  22.954  -20.213  1.00 24.67  ? 880 HOH D O   1 
HETATM 18103 O O   . HOH EA 7 .   ? -21.365  -6.802  -20.068  1.00 26.95  ? 881 HOH D O   1 
HETATM 18104 O O   . HOH EA 7 .   ? -62.765  26.146  -9.379   1.00 35.27  ? 882 HOH D O   1 
HETATM 18105 O O   . HOH EA 7 .   ? -39.686  40.959  -25.739  1.00 38.72  ? 883 HOH D O   1 
HETATM 18106 O O   . HOH EA 7 .   ? -49.854  -11.254 -27.210  1.00 39.10  ? 884 HOH D O   1 
HETATM 18107 O O   . HOH EA 7 .   ? -37.925  21.566  -13.373  1.00 54.80  ? 885 HOH D O   1 
HETATM 18108 O O   . HOH EA 7 .   ? -43.980  8.344   -51.749  1.00 41.06  ? 886 HOH D O   1 
HETATM 18109 O O   . HOH EA 7 .   ? -32.041  2.620   -23.582  1.00 30.40  ? 887 HOH D O   1 
HETATM 18110 O O   . HOH EA 7 .   ? -60.262  0.524   5.743    1.00 26.51  ? 888 HOH D O   1 
HETATM 18111 O O   . HOH EA 7 .   ? -30.055  0.216   -25.241  1.00 26.54  ? 889 HOH D O   1 
HETATM 18112 O O   . HOH EA 7 .   ? -53.942  31.918  -33.142  1.00 42.40  ? 890 HOH D O   1 
HETATM 18113 O O   . HOH EA 7 .   ? -58.389  26.210  -20.676  1.00 31.86  ? 891 HOH D O   1 
HETATM 18114 O O   . HOH EA 7 .   ? -63.423  6.514   -28.084  1.00 36.45  ? 892 HOH D O   1 
HETATM 18115 O O   . HOH EA 7 .   ? -62.499  7.825   7.665    1.00 41.73  ? 893 HOH D O   1 
HETATM 18116 O O   . HOH EA 7 .   ? -61.083  23.936  -10.420  1.00 28.97  ? 894 HOH D O   1 
HETATM 18117 O O   . HOH EA 7 .   ? -61.068  37.106  -11.583  1.00 31.38  ? 895 HOH D O   1 
HETATM 18118 O O   . HOH EA 7 .   ? -38.820  31.091  -17.669  1.00 30.91  ? 896 HOH D O   1 
HETATM 18119 O O   . HOH EA 7 .   ? -55.254  20.513  -36.418  1.00 36.20  ? 897 HOH D O   1 
HETATM 18120 O O   . HOH EA 7 .   ? -47.464  35.468  -34.433  1.00 41.94  ? 898 HOH D O   1 
HETATM 18121 O O   . HOH EA 7 .   ? -58.735  34.440  -21.579  1.00 29.12  ? 899 HOH D O   1 
HETATM 18122 O O   . HOH EA 7 .   ? -44.697  10.704  -3.929   1.00 41.81  ? 900 HOH D O   1 
HETATM 18123 O O   . HOH EA 7 .   ? -18.515  7.395   -17.013  1.00 27.01  ? 901 HOH D O   1 
HETATM 18124 O O   . HOH EA 7 .   ? -60.928  -9.105  4.156    1.00 31.16  ? 902 HOH D O   1 
HETATM 18125 O O   . HOH EA 7 .   ? -42.559  39.321  -16.257  1.00 35.87  ? 903 HOH D O   1 
HETATM 18126 O O   . HOH EA 7 .   ? -52.414  3.869   -1.189   1.00 25.93  ? 904 HOH D O   1 
HETATM 18127 O O   . HOH EA 7 .   ? -63.176  27.942  1.256    1.00 40.17  ? 905 HOH D O   1 
HETATM 18128 O O   . HOH EA 7 .   ? -52.017  25.770  -1.666   1.00 26.96  ? 906 HOH D O   1 
HETATM 18129 O O   . HOH EA 7 .   ? -19.370  13.887  -15.316  1.00 34.64  ? 907 HOH D O   1 
HETATM 18130 O O   . HOH EA 7 .   ? -52.975  41.549  -5.672   1.00 36.16  ? 908 HOH D O   1 
HETATM 18131 O O   . HOH EA 7 .   ? -40.860  33.394  -11.744  1.00 36.34  ? 909 HOH D O   1 
HETATM 18132 O O   . HOH EA 7 .   ? -67.042  5.889   -28.596  1.00 36.72  ? 910 HOH D O   1 
HETATM 18133 O O   . HOH EA 7 .   ? -54.364  17.864  -9.394   1.00 22.76  ? 911 HOH D O   1 
HETATM 18134 O O   . HOH EA 7 .   ? -55.086  14.555  -21.562  1.00 33.19  ? 912 HOH D O   1 
HETATM 18135 O O   . HOH EA 7 .   ? -56.072  18.029  -7.813   1.00 44.59  ? 913 HOH D O   1 
HETATM 18136 O O   . HOH EA 7 .   ? -71.864  17.312  6.063    1.00 39.61  ? 914 HOH D O   1 
HETATM 18137 O O   . HOH EA 7 .   ? -52.320  16.938  -46.025  1.00 32.94  ? 915 HOH D O   1 
HETATM 18138 O O   . HOH EA 7 .   ? -27.019  -9.412  -31.516  1.00 35.63  ? 916 HOH D O   1 
HETATM 18139 O O   . HOH EA 7 .   ? -36.324  3.823   -30.089  1.00 28.67  ? 917 HOH D O   1 
HETATM 18140 O O   . HOH EA 7 .   ? -49.751  7.060   -6.245   1.00 36.21  ? 918 HOH D O   1 
HETATM 18141 O O   . HOH EA 7 .   ? -35.507  25.512  -23.860  1.00 36.98  ? 919 HOH D O   1 
HETATM 18142 O O   . HOH EA 7 .   ? -49.023  -2.895  -1.901   1.00 24.67  ? 920 HOH D O   1 
HETATM 18143 O O   . HOH EA 7 .   ? -34.441  -6.756  -41.218  1.00 37.43  ? 921 HOH D O   1 
HETATM 18144 O O   . HOH EA 7 .   ? -53.373  11.131  -2.702   1.00 39.66  ? 922 HOH D O   1 
HETATM 18145 O O   . HOH EA 7 .   ? -48.149  47.792  -24.624  1.00 41.42  ? 923 HOH D O   1 
HETATM 18146 O O   . HOH EA 7 .   ? -21.481  10.795  -28.389  1.00 34.21  ? 924 HOH D O   1 
HETATM 18147 O O   . HOH EA 7 .   ? -34.611  2.333   -22.804  1.00 20.15  ? 925 HOH D O   1 
HETATM 18148 O O   . HOH EA 7 .   ? -56.865  18.897  -40.211  1.00 27.53  ? 926 HOH D O   1 
HETATM 18149 O O   . HOH EA 7 .   ? -52.129  -11.710 3.302    1.00 35.42  ? 927 HOH D O   1 
HETATM 18150 O O   . HOH EA 7 .   ? -50.070  17.241  -8.031   1.00 31.78  ? 928 HOH D O   1 
HETATM 18151 O O   . HOH EA 7 .   ? -27.950  -6.082  -38.210  1.00 39.98  ? 929 HOH D O   1 
HETATM 18152 O O   . HOH EA 7 .   ? -52.203  -7.894  -18.007  1.00 35.65  ? 930 HOH D O   1 
HETATM 18153 O O   . HOH EA 7 .   ? -35.837  1.709   -31.559  1.00 33.11  ? 931 HOH D O   1 
HETATM 18154 O O   . HOH EA 7 .   ? -63.969  -11.146 -12.922  1.00 31.26  ? 932 HOH D O   1 
HETATM 18155 O O   . HOH EA 7 .   ? -47.288  17.669  -17.809  1.00 40.36  ? 933 HOH D O   1 
HETATM 18156 O O   . HOH EA 7 .   ? -41.925  9.594   -32.872  1.00 45.96  ? 934 HOH D O   1 
HETATM 18157 O O   . HOH EA 7 .   ? -37.940  25.572  -31.628  1.00 27.12  ? 935 HOH D O   1 
HETATM 18158 O O   . HOH EA 7 .   ? -36.529  32.602  -26.388  1.00 41.64  ? 936 HOH D O   1 
HETATM 18159 O O   . HOH EA 7 .   ? -43.609  25.832  -7.308   1.00 38.67  ? 937 HOH D O   1 
HETATM 18160 O O   . HOH EA 7 .   ? -45.432  9.345   -53.395  1.00 36.53  ? 938 HOH D O   1 
HETATM 18161 O O   . HOH EA 7 .   ? -60.964  6.451   -17.560  1.00 27.81  ? 939 HOH D O   1 
HETATM 18162 O O   . HOH EA 7 .   ? -57.038  20.541  -38.315  1.00 36.45  ? 940 HOH D O   1 
HETATM 18163 O O   . HOH EA 7 .   ? -54.154  13.804  -7.384   1.00 21.97  ? 941 HOH D O   1 
HETATM 18164 O O   . HOH EA 7 .   ? -59.083  28.864  -28.888  1.00 48.15  ? 942 HOH D O   1 
HETATM 18165 O O   . HOH EA 7 .   ? -38.255  30.686  -27.753  1.00 29.71  ? 943 HOH D O   1 
HETATM 18166 O O   . HOH EA 7 .   ? -39.352  31.996  -20.148  1.00 26.64  ? 944 HOH D O   1 
HETATM 18167 O O   . HOH EA 7 .   ? -63.028  5.676   -18.608  1.00 30.50  ? 945 HOH D O   1 
HETATM 18168 O O   . HOH EA 7 .   ? -46.073  -9.549  -12.526  1.00 42.28  ? 946 HOH D O   1 
HETATM 18169 O O   . HOH EA 7 .   ? -51.776  1.816   0.543    1.00 29.04  ? 947 HOH D O   1 
HETATM 18170 O O   . HOH EA 7 .   ? -37.994  26.128  -29.328  1.00 32.92  ? 948 HOH D O   1 
HETATM 18171 O O   . HOH EA 7 .   ? -57.609  22.627  -16.414  1.00 28.95  ? 949 HOH D O   1 
HETATM 18172 O O   . HOH EA 7 .   ? -67.626  1.556   9.259    1.00 29.46  ? 950 HOH D O   1 
HETATM 18173 O O   . HOH EA 7 .   ? -49.476  1.324   0.252    1.00 38.82  ? 951 HOH D O   1 
HETATM 18174 O O   . HOH EA 7 .   ? -43.175  10.469  -52.997  1.00 31.68  ? 952 HOH D O   1 
HETATM 18175 O O   . HOH EA 7 .   ? -53.206  12.371  0.448    1.00 36.62  ? 953 HOH D O   1 
HETATM 18176 O O   . HOH EA 7 .   ? -37.581  15.022  -26.516  1.00 31.91  ? 954 HOH D O   1 
HETATM 18177 O O   . HOH EA 7 .   ? -50.665  3.568   -3.695   1.00 30.59  ? 955 HOH D O   1 
HETATM 18178 O O   . HOH EA 7 .   ? -51.575  -9.230  -21.742  1.00 40.22  ? 956 HOH D O   1 
HETATM 18179 O O   . HOH EA 7 .   ? -56.357  30.978  -32.796  1.00 35.49  ? 957 HOH D O   1 
HETATM 18180 O O   . HOH EA 7 .   ? -52.828  6.735   -1.347   1.00 26.05  ? 958 HOH D O   1 
HETATM 18181 O O   . HOH EA 7 .   ? -36.772  22.665  -32.853  1.00 34.47  ? 959 HOH D O   1 
HETATM 18182 O O   . HOH EA 7 .   ? -63.992  10.579  -11.416  1.00 32.88  ? 960 HOH D O   1 
HETATM 18183 O O   . HOH EA 7 .   ? -37.556  9.839   -0.202   1.00 30.94  ? 961 HOH D O   1 
HETATM 18184 O O   . HOH EA 7 .   ? -36.895  17.143  -28.069  1.00 38.61  ? 962 HOH D O   1 
HETATM 18185 O O   . HOH EA 7 .   ? -19.023  5.546   -15.270  1.00 33.71  ? 963 HOH D O   1 
HETATM 18186 O O   . HOH EA 7 .   ? -34.463  16.360  -28.363  1.00 37.54  ? 964 HOH D 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   . SER A 3   ? 0.9729 0.7130 1.0469 0.0240  0.0251  -0.0910 3   SER A N   
2     C CA  . SER A 3   ? 0.9661 0.7182 1.0525 0.0306  0.0321  -0.0890 3   SER A CA  
3     C C   . SER A 3   ? 0.8593 0.6299 0.9560 0.0274  0.0332  -0.0810 3   SER A C   
4     O O   . SER A 3   ? 0.9848 0.7623 1.0949 0.0281  0.0323  -0.0752 3   SER A O   
5     C CB  . SER A 3   ? 0.9474 0.6915 1.0431 0.0346  0.0296  -0.0885 3   SER A CB  
6     O OG  . SER A 3   ? 0.9020 0.6589 1.0114 0.0397  0.0342  -0.0847 3   SER A OG  
7     N N   . LYS A 4   ? 0.7269 0.5045 0.8162 0.0241  0.0352  -0.0808 4   LYS A N   
8     C CA  . LYS A 4   ? 0.7018 0.4941 0.7989 0.0198  0.0344  -0.0735 4   LYS A CA  
9     C C   . LYS A 4   ? 0.5832 0.3906 0.6856 0.0236  0.0425  -0.0724 4   LYS A C   
10    O O   . LYS A 4   ? 0.5784 0.3852 0.6754 0.0283  0.0489  -0.0778 4   LYS A O   
11    C CB  . LYS A 4   ? 0.7801 0.5697 0.8670 0.0128  0.0295  -0.0730 4   LYS A CB  
12    C CG  . LYS A 4   ? 0.8247 0.6126 0.8959 0.0127  0.0332  -0.0777 4   LYS A CG  
13    C CD  . LYS A 4   ? 0.8888 0.6697 0.9485 0.0060  0.0261  -0.0779 4   LYS A CD  
14    C CE  . LYS A 4   ? 0.9666 0.7418 1.0075 0.0062  0.0294  -0.0834 4   LYS A CE  
15    N NZ  . LYS A 4   ? 0.9167 0.7049 0.9582 0.0083  0.0378  -0.0819 4   LYS A NZ  
16    N N   . THR A 5   ? 0.4773 0.2978 0.5903 0.0214  0.0419  -0.0655 5   THR A N   
17    C CA  . THR A 5   ? 0.4678 0.3032 0.5884 0.0241  0.0481  -0.0632 5   THR A CA  
18    C C   . THR A 5   ? 0.4916 0.3301 0.6012 0.0233  0.0533  -0.0666 5   THR A C   
19    O O   . THR A 5   ? 0.4907 0.3266 0.5906 0.0181  0.0503  -0.0660 5   THR A O   
20    C CB  . THR A 5   ? 0.4473 0.2935 0.5781 0.0203  0.0448  -0.0555 5   THR A CB  
21    O OG1 . THR A 5   ? 0.4111 0.2526 0.5494 0.0199  0.0398  -0.0523 5   THR A OG1 
22    C CG2 . THR A 5   ? 0.4301 0.2913 0.5703 0.0230  0.0499  -0.0527 5   THR A CG2 
23    N N   . LYS A 6   ? 0.4988 0.3428 0.6099 0.0285  0.0612  -0.0699 6   LYS A N   
24    C CA  . LYS A 6   ? 0.5503 0.3995 0.6525 0.0275  0.0674  -0.0719 6   LYS A CA  
25    C C   . LYS A 6   ? 0.4824 0.3475 0.5945 0.0254  0.0690  -0.0657 6   LYS A C   
26    O O   . LYS A 6   ? 0.4287 0.3035 0.5553 0.0287  0.0708  -0.0632 6   LYS A O   
27    C CB  . LYS A 6   ? 0.6428 0.4900 0.7422 0.0339  0.0755  -0.0789 6   LYS A CB  
28    C CG  . LYS A 6   ? 0.7594 0.6134 0.8511 0.0336  0.0842  -0.0811 6   LYS A CG  
29    C CD  . LYS A 6   ? 0.8926 0.7436 0.9789 0.0396  0.0930  -0.0889 6   LYS A CD  
30    C CE  . LYS A 6   ? 0.9967 0.8518 1.0986 0.0477  0.0966  -0.0915 6   LYS A CE  
31    N NZ  . LYS A 6   ? 0.9371 0.8100 1.0574 0.0502  0.1009  -0.0877 6   LYS A NZ  
32    N N   . ILE A 7   ? 0.4528 0.3195 0.5567 0.0197  0.0675  -0.0632 7   ILE A N   
33    C CA  . ILE A 7   ? 0.4305 0.3106 0.5418 0.0173  0.0687  -0.0577 7   ILE A CA  
34    C C   . ILE A 7   ? 0.4426 0.3268 0.5458 0.0168  0.0763  -0.0599 7   ILE A C   
35    O O   . ILE A 7   ? 0.4403 0.3161 0.5274 0.0139  0.0761  -0.0622 7   ILE A O   
36    C CB  . ILE A 7   ? 0.4227 0.3024 0.5322 0.0113  0.0613  -0.0527 7   ILE A CB  
37    C CG1 . ILE A 7   ? 0.4192 0.2956 0.5368 0.0109  0.0543  -0.0501 7   ILE A CG1 
38    C CG2 . ILE A 7   ? 0.3904 0.2826 0.5057 0.0090  0.0631  -0.0479 7   ILE A CG2 
39    C CD1 . ILE A 7   ? 0.4080 0.2828 0.5234 0.0053  0.0472  -0.0463 7   ILE A CD1 
40    N N   . GLU A 8   ? 0.4643 0.3613 0.5785 0.0193  0.0823  -0.0586 8   GLU A N   
41    C CA  . GLU A 8   ? 0.5043 0.4073 0.6131 0.0181  0.0902  -0.0596 8   GLU A CA  
42    C C   . GLU A 8   ? 0.4499 0.3660 0.5690 0.0153  0.0903  -0.0537 8   GLU A C   
43    O O   . GLU A 8   ? 0.4077 0.3325 0.5427 0.0177  0.0891  -0.0511 8   GLU A O   
44    C CB  . GLU A 8   ? 0.5590 0.4660 0.6717 0.0238  0.0995  -0.0648 8   GLU A CB  
45    C CG  . GLU A 8   ? 0.6784 0.5717 0.7775 0.0266  0.1012  -0.0718 8   GLU A CG  
46    C CD  . GLU A 8   ? 0.7617 0.6573 0.8707 0.0344  0.1070  -0.0770 8   GLU A CD  
47    O OE1 . GLU A 8   ? 0.7306 0.6250 0.8511 0.0384  0.1026  -0.0767 8   GLU A OE1 
48    O OE2 . GLU A 8   ? 0.8142 0.7132 0.9193 0.0365  0.1162  -0.0810 8   GLU A OE2 
49    N N   . LEU A 9   ? 0.4576 0.3742 0.5667 0.0103  0.0917  -0.0518 9   LEU A N   
50    C CA  . LEU A 9   ? 0.4334 0.3610 0.5502 0.0071  0.0922  -0.0465 9   LEU A CA  
51    C C   . LEU A 9   ? 0.4276 0.3638 0.5461 0.0077  0.1022  -0.0480 9   LEU A C   
52    O O   . LEU A 9   ? 0.4428 0.3739 0.5467 0.0058  0.1071  -0.0504 9   LEU A O   
53    C CB  . LEU A 9   ? 0.4221 0.3435 0.5268 0.0010  0.0865  -0.0431 9   LEU A CB  
54    C CG  . LEU A 9   ? 0.4213 0.3338 0.5232 0.0001  0.0771  -0.0422 9   LEU A CG  
55    C CD1 . LEU A 9   ? 0.4321 0.3408 0.5250 -0.0055 0.0716  -0.0385 9   LEU A CD1 
56    C CD2 . LEU A 9   ? 0.3979 0.3159 0.5161 0.0025  0.0728  -0.0398 9   LEU A CD2 
57    N N   . LYS A 10  ? 0.4422 0.3914 0.5781 0.0102  0.1053  -0.0467 10  LYS A N   
58    C CA  . LYS A 10  ? 0.4735 0.4330 0.6136 0.0095  0.1143  -0.0469 10  LYS A CA  
59    C C   . LYS A 10  ? 0.4276 0.4015 0.5884 0.0106  0.1139  -0.0435 10  LYS A C   
60    O O   . LYS A 10  ? 0.3737 0.3489 0.5452 0.0136  0.1078  -0.0423 10  LYS A O   
61    C CB  . LYS A 10  ? 0.5701 0.5288 0.7063 0.0137  0.1237  -0.0532 10  LYS A CB  
62    C CG  . LYS A 10  ? 0.6683 0.6307 0.8187 0.0214  0.1253  -0.0573 10  LYS A CG  
63    C CD  . LYS A 10  ? 0.7661 0.7286 0.9131 0.0258  0.1357  -0.0640 10  LYS A CD  
64    C CE  . LYS A 10  ? 0.8177 0.7913 0.9664 0.0234  0.1463  -0.0639 10  LYS A CE  
65    N NZ  . LYS A 10  ? 0.8148 0.7921 0.9677 0.0297  0.1562  -0.0705 10  LYS A NZ  
66    N N   . ASP A 11  ? 0.4054 0.3894 0.5708 0.0077  0.1200  -0.0418 11  ASP A N   
67    C CA  . ASP A 11  ? 0.3966 0.3937 0.5797 0.0070  0.1188  -0.0380 11  ASP A CA  
68    C C   . ASP A 11  ? 0.3590 0.3532 0.5427 0.0041  0.1088  -0.0331 11  ASP A C   
69    O O   . ASP A 11  ? 0.3360 0.3374 0.5341 0.0059  0.1048  -0.0311 11  ASP A O   
70    C CB  . ASP A 11  ? 0.4350 0.4410 0.6360 0.0138  0.1211  -0.0408 11  ASP A CB  
71    C CG  . ASP A 11  ? 0.4988 0.5061 0.6983 0.0177  0.1310  -0.0466 11  ASP A CG  
72    O OD1 . ASP A 11  ? 0.5116 0.5233 0.7068 0.0143  0.1391  -0.0469 11  ASP A OD1 
73    O OD2 . ASP A 11  ? 0.6213 0.6241 0.8227 0.0240  0.1307  -0.0509 11  ASP A OD2 
74    N N   . ASN A 12  ? 0.3588 0.3421 0.5268 0.0002  0.1045  -0.0317 12  ASN A N   
75    C CA  . ASN A 12  ? 0.3791 0.3586 0.5465 -0.0021 0.0954  -0.0277 12  ASN A CA  
76    C C   . ASN A 12  ? 0.3504 0.3291 0.5268 0.0026  0.0895  -0.0280 12  ASN A C   
77    O O   . ASN A 12  ? 0.3289 0.3092 0.5107 0.0017  0.0833  -0.0247 12  ASN A O   
78    C CB  . ASN A 12  ? 0.3951 0.3820 0.5683 -0.0065 0.0944  -0.0232 12  ASN A CB  
79    C CG  . ASN A 12  ? 0.4252 0.4127 0.5899 -0.0113 0.1010  -0.0225 12  ASN A CG  
80    O OD1 . ASN A 12  ? 0.4751 0.4534 0.6235 -0.0133 0.1029  -0.0238 12  ASN A OD1 
81    N ND2 . ASN A 12  ? 0.4082 0.4062 0.5832 -0.0135 0.1045  -0.0204 12  ASN A ND2 
82    N N   . TRP A 13  ? 0.3477 0.3229 0.5246 0.0074  0.0912  -0.0321 13  TRP A N   
83    C CA  . TRP A 13  ? 0.3668 0.3382 0.5487 0.0111  0.0853  -0.0321 13  TRP A CA  
84    C C   . TRP A 13  ? 0.3535 0.3118 0.5228 0.0116  0.0832  -0.0350 13  TRP A C   
85    O O   . TRP A 13  ? 0.3628 0.3161 0.5227 0.0121  0.0880  -0.0389 13  TRP A O   
86    C CB  . TRP A 13  ? 0.3716 0.3501 0.5679 0.0171  0.0879  -0.0342 13  TRP A CB  
87    C CG  . TRP A 13  ? 0.3439 0.3337 0.5550 0.0175  0.0860  -0.0308 13  TRP A CG  
88    C CD1 . TRP A 13  ? 0.3380 0.3388 0.5570 0.0158  0.0899  -0.0297 13  TRP A CD1 
89    C CD2 . TRP A 13  ? 0.3372 0.3278 0.5565 0.0198  0.0794  -0.0283 13  TRP A CD2 
90    N NE1 . TRP A 13  ? 0.3392 0.3474 0.5709 0.0168  0.0854  -0.0268 13  TRP A NE1 
91    C CE2 . TRP A 13  ? 0.3241 0.3261 0.5556 0.0194  0.0791  -0.0259 13  TRP A CE2 
92    C CE3 . TRP A 13  ? 0.3409 0.3236 0.5583 0.0219  0.0739  -0.0277 13  TRP A CE3 
93    C CZ2 . TRP A 13  ? 0.3113 0.3162 0.5514 0.0212  0.0732  -0.0231 13  TRP A CZ2 
94    C CZ3 . TRP A 13  ? 0.3323 0.3182 0.5586 0.0237  0.0689  -0.0247 13  TRP A CZ3 
95    C CH2 . TRP A 13  ? 0.3113 0.3080 0.5481 0.0234  0.0684  -0.0226 13  TRP A CH2 
96    N N   . TYR A 14  ? 0.3464 0.2992 0.5161 0.0118  0.0763  -0.0333 14  TYR A N   
97    C CA  . TYR A 14  ? 0.3407 0.2822 0.5033 0.0136  0.0743  -0.0365 14  TYR A CA  
98    C C   . TYR A 14  ? 0.3365 0.2790 0.5075 0.0198  0.0771  -0.0397 14  TYR A C   
99    O O   . TYR A 14  ? 0.3135 0.2634 0.4974 0.0226  0.0762  -0.0377 14  TYR A O   
100   C CB  . TYR A 14  ? 0.3365 0.2723 0.4992 0.0122  0.0666  -0.0338 14  TYR A CB  
101   C CG  . TYR A 14  ? 0.3347 0.2668 0.4894 0.0068  0.0619  -0.0312 14  TYR A CG  
102   C CD1 . TYR A 14  ? 0.3359 0.2749 0.4927 0.0038  0.0612  -0.0275 14  TYR A CD1 
103   C CD2 . TYR A 14  ? 0.3390 0.2608 0.4854 0.0051  0.0575  -0.0322 14  TYR A CD2 
104   C CE1 . TYR A 14  ? 0.3190 0.2546 0.4697 -0.0004 0.0564  -0.0251 14  TYR A CE1 
105   C CE2 . TYR A 14  ? 0.3501 0.2694 0.4913 0.0006  0.0525  -0.0297 14  TYR A CE2 
106   C CZ  . TYR A 14  ? 0.3338 0.2600 0.4772 -0.0019 0.0520  -0.0261 14  TYR A CZ  
107   O OH  . TYR A 14  ? 0.3310 0.2544 0.4698 -0.0057 0.0468  -0.0238 14  TYR A OH  
108   N N   . HIS A 15  ? 0.3739 0.3077 0.5369 0.0220  0.0797  -0.0447 15  HIS A N   
109   C CA  . HIS A 15  ? 0.3812 0.3124 0.5503 0.0282  0.0811  -0.0482 15  HIS A CA  
110   C C   . HIS A 15  ? 0.3856 0.3024 0.5465 0.0282  0.0758  -0.0500 15  HIS A C   
111   O O   . HIS A 15  ? 0.3867 0.2946 0.5340 0.0251  0.0752  -0.0521 15  HIS A O   
112   C CB  . HIS A 15  ? 0.3940 0.3275 0.5611 0.0314  0.0898  -0.0536 15  HIS A CB  
113   C CG  . HIS A 15  ? 0.4092 0.3569 0.5852 0.0314  0.0960  -0.0525 15  HIS A CG  
114   N ND1 . HIS A 15  ? 0.3803 0.3334 0.5516 0.0259  0.0982  -0.0498 15  HIS A ND1 
115   C CD2 . HIS A 15  ? 0.3971 0.3547 0.5871 0.0366  0.1009  -0.0543 15  HIS A CD2 
116   C CE1 . HIS A 15  ? 0.3476 0.3133 0.5297 0.0272  0.1044  -0.0499 15  HIS A CE1 
117   N NE2 . HIS A 15  ? 0.3503 0.3196 0.5445 0.0338  0.1061  -0.0526 15  HIS A NE2 
118   N N   . LEU A 16  ? 0.3895 0.3033 0.5584 0.0313  0.0717  -0.0489 16  LEU A N   
119   C CA  . LEU A 16  ? 0.3903 0.2904 0.5532 0.0317  0.0673  -0.0508 16  LEU A CA  
120   C C   . LEU A 16  ? 0.3952 0.2914 0.5623 0.0387  0.0705  -0.0557 16  LEU A C   
121   O O   . LEU A 16  ? 0.3781 0.2804 0.5578 0.0430  0.0706  -0.0541 16  LEU A O   
122   C CB  . LEU A 16  ? 0.3751 0.2731 0.5431 0.0296  0.0601  -0.0456 16  LEU A CB  
123   C CG  . LEU A 16  ? 0.3918 0.2955 0.5596 0.0239  0.0568  -0.0404 16  LEU A CG  
124   C CD1 . LEU A 16  ? 0.3967 0.2960 0.5681 0.0222  0.0507  -0.0364 16  LEU A CD1 
125   C CD2 . LEU A 16  ? 0.4128 0.3135 0.5687 0.0190  0.0568  -0.0416 16  LEU A CD2 
126   N N   . ASP A 17  ? 0.4136 0.2995 0.5698 0.0400  0.0729  -0.0617 17  ASP A N   
127   C CA  . ASP A 17  ? 0.4432 0.3233 0.6020 0.0470  0.0757  -0.0672 17  ASP A CA  
128   C C   . ASP A 17  ? 0.4311 0.3248 0.6024 0.0523  0.0825  -0.0682 17  ASP A C   
129   O O   . ASP A 17  ? 0.4204 0.3150 0.6027 0.0585  0.0825  -0.0692 17  ASP A O   
130   C CB  . ASP A 17  ? 0.4497 0.3190 0.6120 0.0489  0.0690  -0.0661 17  ASP A CB  
131   C CG  . ASP A 17  ? 0.4715 0.3273 0.6229 0.0435  0.0625  -0.0656 17  ASP A CG  
132   O OD1 . ASP A 17  ? 0.5037 0.3519 0.6417 0.0414  0.0636  -0.0700 17  ASP A OD1 
133   O OD2 . ASP A 17  ? 0.4636 0.3170 0.6197 0.0411  0.0562  -0.0606 17  ASP A OD2 
134   N N   . GLY A 18  ? 0.4473 0.3513 0.6169 0.0498  0.0882  -0.0680 18  GLY A N   
135   C CA  . GLY A 18  ? 0.4554 0.3728 0.6363 0.0540  0.0956  -0.0695 18  GLY A CA  
136   C C   . GLY A 18  ? 0.4611 0.3925 0.6577 0.0535  0.0932  -0.0634 18  GLY A C   
137   O O   . GLY A 18  ? 0.4709 0.4153 0.6770 0.0550  0.0990  -0.0637 18  GLY A O   
138   N N   . GLU A 19  ? 0.4569 0.3858 0.6562 0.0511  0.0851  -0.0579 19  GLU A N   
139   C CA  . GLU A 19  ? 0.4411 0.3808 0.6540 0.0512  0.0818  -0.0524 19  GLU A CA  
140   C C   . GLU A 19  ? 0.4352 0.3808 0.6444 0.0441  0.0801  -0.0476 19  GLU A C   
141   O O   . GLU A 19  ? 0.3755 0.3136 0.5740 0.0391  0.0764  -0.0458 19  GLU A O   
142   C CB  . GLU A 19  ? 0.5076 0.4400 0.7239 0.0526  0.0740  -0.0491 19  GLU A CB  
143   C CG  . GLU A 19  ? 0.5754 0.5002 0.7965 0.0598  0.0732  -0.0524 19  GLU A CG  
144   C CD  . GLU A 19  ? 0.6378 0.5732 0.8730 0.0665  0.0778  -0.0551 19  GLU A CD  
145   O OE1 . GLU A 19  ? 0.6229 0.5705 0.8705 0.0674  0.0768  -0.0516 19  GLU A OE1 
146   O OE2 . GLU A 19  ? 0.7448 0.6761 0.9781 0.0709  0.0829  -0.0613 19  GLU A OE2 
147   N N   . LYS A 20  ? 0.4057 0.3649 0.6248 0.0436  0.0823  -0.0453 20  LYS A N   
148   C CA  . LYS A 20  ? 0.3952 0.3593 0.6118 0.0373  0.0799  -0.0405 20  LYS A CA  
149   C C   . LYS A 20  ? 0.3563 0.3156 0.5730 0.0359  0.0719  -0.0360 20  LYS A C   
150   O O   . LYS A 20  ? 0.3351 0.2937 0.5597 0.0400  0.0687  -0.0350 20  LYS A O   
151   C CB  . LYS A 20  ? 0.4138 0.3926 0.6418 0.0368  0.0829  -0.0387 20  LYS A CB  
152   C CG  . LYS A 20  ? 0.4454 0.4301 0.6732 0.0371  0.0917  -0.0426 20  LYS A CG  
153   C CD  . LYS A 20  ? 0.4675 0.4659 0.7042 0.0343  0.0946  -0.0401 20  LYS A CD  
154   C CE  . LYS A 20  ? 0.5145 0.5184 0.7508 0.0344  0.1041  -0.0438 20  LYS A CE  
155   N NZ  . LYS A 20  ? 0.5478 0.5657 0.7951 0.0316  0.1068  -0.0412 20  LYS A NZ  
156   N N   . TYR A 21  ? 0.3146 0.2708 0.5228 0.0302  0.0690  -0.0333 21  TYR A N   
157   C CA  . TYR A 21  ? 0.3040 0.2546 0.5103 0.0283  0.0625  -0.0297 21  TYR A CA  
158   C C   . TYR A 21  ? 0.3039 0.2596 0.5090 0.0233  0.0601  -0.0256 21  TYR A C   
159   O O   . TYR A 21  ? 0.2874 0.2404 0.4838 0.0191  0.0603  -0.0257 21  TYR A O   
160   C CB  . TYR A 21  ? 0.3213 0.2591 0.5171 0.0272  0.0610  -0.0320 21  TYR A CB  
161   C CG  . TYR A 21  ? 0.3311 0.2624 0.5261 0.0255  0.0549  -0.0286 21  TYR A CG  
162   C CD1 . TYR A 21  ? 0.3132 0.2442 0.5039 0.0203  0.0516  -0.0255 21  TYR A CD1 
163   C CD2 . TYR A 21  ? 0.3308 0.2565 0.5300 0.0292  0.0526  -0.0284 21  TYR A CD2 
164   C CE1 . TYR A 21  ? 0.3095 0.2354 0.5004 0.0187  0.0469  -0.0225 21  TYR A CE1 
165   C CE2 . TYR A 21  ? 0.3328 0.2526 0.5312 0.0271  0.0477  -0.0250 21  TYR A CE2 
166   C CZ  . TYR A 21  ? 0.3284 0.2489 0.5229 0.0218  0.0452  -0.0221 21  TYR A CZ  
167   O OH  . TYR A 21  ? 0.3284 0.2439 0.5233 0.0199  0.0412  -0.0188 21  TYR A OH  
168   N N   . PHE A 22  ? 0.2894 0.2518 0.5031 0.0242  0.0574  -0.0221 22  PHE A N   
169   C CA  . PHE A 22  ? 0.2759 0.2420 0.4889 0.0203  0.0545  -0.0184 22  PHE A CA  
170   C C   . PHE A 22  ? 0.2893 0.2476 0.4965 0.0180  0.0502  -0.0164 22  PHE A C   
171   O O   . PHE A 22  ? 0.2658 0.2202 0.4753 0.0201  0.0477  -0.0151 22  PHE A O   
172   C CB  . PHE A 22  ? 0.2591 0.2335 0.4817 0.0220  0.0525  -0.0157 22  PHE A CB  
173   C CG  . PHE A 22  ? 0.2451 0.2244 0.4669 0.0180  0.0508  -0.0129 22  PHE A CG  
174   C CD1 . PHE A 22  ? 0.2421 0.2181 0.4599 0.0157  0.0468  -0.0101 22  PHE A CD1 
175   C CD2 . PHE A 22  ? 0.2474 0.2345 0.4726 0.0164  0.0533  -0.0132 22  PHE A CD2 
176   C CE1 . PHE A 22  ? 0.2586 0.2383 0.4755 0.0126  0.0452  -0.0082 22  PHE A CE1 
177   C CE2 . PHE A 22  ? 0.2588 0.2489 0.4828 0.0127  0.0513  -0.0109 22  PHE A CE2 
178   C CZ  . PHE A 22  ? 0.2474 0.2336 0.4671 0.0111  0.0471  -0.0086 22  PHE A CZ  
179   N N   . ILE A 23  ? 0.2898 0.2464 0.4902 0.0136  0.0494  -0.0158 23  ILE A N   
180   C CA  . ILE A 23  ? 0.2943 0.2450 0.4908 0.0112  0.0456  -0.0140 23  ILE A CA  
181   C C   . ILE A 23  ? 0.2984 0.2541 0.4994 0.0106  0.0429  -0.0101 23  ILE A C   
182   O O   . ILE A 23  ? 0.3274 0.2883 0.5287 0.0086  0.0426  -0.0090 23  ILE A O   
183   C CB  . ILE A 23  ? 0.3003 0.2471 0.4885 0.0072  0.0451  -0.0151 23  ILE A CB  
184   C CG1 . ILE A 23  ? 0.3115 0.2524 0.4931 0.0079  0.0480  -0.0193 23  ILE A CG1 
185   C CG2 . ILE A 23  ? 0.2946 0.2369 0.4811 0.0046  0.0408  -0.0132 23  ILE A CG2 
186   C CD1 . ILE A 23  ? 0.3257 0.2637 0.4979 0.0041  0.0479  -0.0204 23  ILE A CD1 
187   N N   . LYS A 24  ? 0.3040 0.2571 0.5077 0.0122  0.0409  -0.0082 24  LYS A N   
188   C CA  . LYS A 24  ? 0.3113 0.2671 0.5173 0.0116  0.0385  -0.0046 24  LYS A CA  
189   C C   . LYS A 24  ? 0.3289 0.2803 0.5319 0.0085  0.0366  -0.0031 24  LYS A C   
190   O O   . LYS A 24  ? 0.3460 0.2934 0.5496 0.0087  0.0354  -0.0012 24  LYS A O   
191   C CB  . LYS A 24  ? 0.3276 0.2834 0.5380 0.0154  0.0377  -0.0032 24  LYS A CB  
192   C CG  . LYS A 24  ? 0.3275 0.2889 0.5430 0.0186  0.0392  -0.0047 24  LYS A CG  
193   C CD  . LYS A 24  ? 0.3408 0.3032 0.5611 0.0222  0.0369  -0.0026 24  LYS A CD  
194   C CE  . LYS A 24  ? 0.3675 0.3225 0.5879 0.0249  0.0361  -0.0025 24  LYS A CE  
195   N NZ  . LYS A 24  ? 0.3851 0.3398 0.6089 0.0283  0.0331  0.0003  24  LYS A NZ  
196   N N   . ALA A 25  ? 0.3190 0.2716 0.5193 0.0055  0.0362  -0.0036 25  ALA A N   
197   C CA  . ALA A 25  ? 0.3085 0.2580 0.5077 0.0026  0.0342  -0.0025 25  ALA A CA  
198   C C   . ALA A 25  ? 0.3106 0.2649 0.5124 0.0018  0.0333  0.0004  25  ALA A C   
199   O O   . ALA A 25  ? 0.3055 0.2646 0.5088 0.0034  0.0338  0.0014  25  ALA A O   
200   C CB  . ALA A 25  ? 0.3208 0.2680 0.5156 0.0000  0.0334  -0.0047 25  ALA A CB  
201   N N   . ILE A 26  ? 0.2982 0.2510 0.5008 -0.0007 0.0320  0.0015  26  ILE A N   
202   C CA  . ILE A 26  ? 0.2774 0.2349 0.4826 -0.0017 0.0316  0.0035  26  ILE A CA  
203   C C   . ILE A 26  ? 0.2932 0.2496 0.4995 -0.0047 0.0296  0.0029  26  ILE A C   
204   O O   . ILE A 26  ? 0.2880 0.2393 0.4938 -0.0063 0.0284  0.0021  26  ILE A O   
205   C CB  . ILE A 26  ? 0.2730 0.2311 0.4802 -0.0010 0.0326  0.0065  26  ILE A CB  
206   C CG1 . ILE A 26  ? 0.2510 0.2145 0.4599 -0.0014 0.0331  0.0079  26  ILE A CG1 
207   C CG2 . ILE A 26  ? 0.2780 0.2307 0.4864 -0.0029 0.0323  0.0076  26  ILE A CG2 
208   C CD1 . ILE A 26  ? 0.2542 0.2184 0.4631 -0.0007 0.0348  0.0109  26  ILE A CD1 
209   N N   . GLY A 27  ? 0.2924 0.2532 0.5004 -0.0054 0.0287  0.0031  27  GLY A N   
210   C CA  . GLY A 27  ? 0.3028 0.2634 0.5134 -0.0079 0.0262  0.0028  27  GLY A CA  
211   C C   . GLY A 27  ? 0.2752 0.2366 0.4915 -0.0094 0.0268  0.0049  27  GLY A C   
212   O O   . GLY A 27  ? 0.2791 0.2438 0.4974 -0.0083 0.0294  0.0069  27  GLY A O   
213   N N   . TYR A 28  ? 0.2650 0.2233 0.4834 -0.0121 0.0244  0.0044  28  TYR A N   
214   C CA  . TYR A 28  ? 0.2949 0.2536 0.5192 -0.0142 0.0250  0.0066  28  TYR A CA  
215   C C   . TYR A 28  ? 0.2752 0.2354 0.5057 -0.0173 0.0215  0.0061  28  TYR A C   
216   O O   . TYR A 28  ? 0.2833 0.2383 0.5110 -0.0188 0.0179  0.0041  28  TYR A O   
217   C CB  . TYR A 28  ? 0.2752 0.2265 0.4964 -0.0146 0.0255  0.0068  28  TYR A CB  
218   C CG  . TYR A 28  ? 0.2946 0.2448 0.5217 -0.0179 0.0256  0.0092  28  TYR A CG  
219   C CD1 . TYR A 28  ? 0.2911 0.2469 0.5234 -0.0184 0.0287  0.0125  28  TYR A CD1 
220   C CD2 . TYR A 28  ? 0.3132 0.2563 0.5404 -0.0207 0.0226  0.0082  28  TYR A CD2 
221   C CE1 . TYR A 28  ? 0.2987 0.2536 0.5366 -0.0220 0.0294  0.0151  28  TYR A CE1 
222   C CE2 . TYR A 28  ? 0.2945 0.2365 0.5278 -0.0243 0.0224  0.0106  28  TYR A CE2 
223   C CZ  . TYR A 28  ? 0.2943 0.2425 0.5334 -0.0251 0.0260  0.0143  28  TYR A CZ  
224   O OH  . TYR A 28  ? 0.3512 0.2987 0.5969 -0.0293 0.0264  0.0171  28  TYR A OH  
225   N N   . GLU A 29  ? 0.2660 0.2331 0.5049 -0.0181 0.0226  0.0079  29  GLU A N   
226   C CA  . GLU A 29  ? 0.2809 0.2506 0.5281 -0.0209 0.0191  0.0076  29  GLU A CA  
227   C C   . GLU A 29  ? 0.2726 0.2451 0.5288 -0.0240 0.0211  0.0103  29  GLU A C   
228   O O   . GLU A 29  ? 0.2698 0.2492 0.5312 -0.0234 0.0255  0.0124  29  GLU A O   
229   C CB  . GLU A 29  ? 0.2652 0.2418 0.5166 -0.0191 0.0181  0.0069  29  GLU A CB  
230   C CG  . GLU A 29  ? 0.2762 0.2565 0.5377 -0.0214 0.0136  0.0065  29  GLU A CG  
231   C CD  . GLU A 29  ? 0.2682 0.2536 0.5330 -0.0190 0.0115  0.0054  29  GLU A CD  
232   O OE1 . GLU A 29  ? 0.2492 0.2408 0.5172 -0.0163 0.0156  0.0060  29  GLU A OE1 
233   O OE2 . GLU A 29  ? 0.2291 0.2113 0.4925 -0.0196 0.0055  0.0039  29  GLU A OE2 
234   N N   . ILE A 30  ? 0.2682 0.2352 0.5258 -0.0276 0.0180  0.0102  30  ILE A N   
235   C CA  . ILE A 30  ? 0.2658 0.2355 0.5336 -0.0316 0.0187  0.0127  30  ILE A CA  
236   C C   . ILE A 30  ? 0.2832 0.2612 0.5630 -0.0331 0.0159  0.0123  30  ILE A C   
237   O O   . ILE A 30  ? 0.2807 0.2586 0.5594 -0.0320 0.0111  0.0098  30  ILE A O   
238   C CB  . ILE A 30  ? 0.2707 0.2305 0.5360 -0.0351 0.0155  0.0124  30  ILE A CB  
239   C CG1 . ILE A 30  ? 0.2674 0.2284 0.5420 -0.0397 0.0173  0.0158  30  ILE A CG1 
240   C CG2 . ILE A 30  ? 0.2731 0.2288 0.5377 -0.0367 0.0083  0.0091  30  ILE A CG2 
241   C CD1 . ILE A 30  ? 0.2693 0.2322 0.5428 -0.0389 0.0241  0.0196  30  ILE A CD1 
242   N N   . GLY A 31  ? 0.3023 0.2876 0.5938 -0.0357 0.0190  0.0150  31  GLY A N   
243   C CA  . GLY A 31  ? 0.2976 0.2924 0.6037 -0.0373 0.0169  0.0149  31  GLY A CA  
244   C C   . GLY A 31  ? 0.2908 0.2950 0.6005 -0.0330 0.0203  0.0144  31  GLY A C   
245   O O   . GLY A 31  ? 0.3167 0.3279 0.6369 -0.0327 0.0171  0.0132  31  GLY A O   
246   N N   . ALA A 32  ? 0.2668 0.2710 0.5681 -0.0296 0.0262  0.0151  32  ALA A N   
247   C CA  . ALA A 32  ? 0.2599 0.2709 0.5619 -0.0251 0.0293  0.0141  32  ALA A CA  
248   C C   . ALA A 32  ? 0.2625 0.2790 0.5653 -0.0243 0.0377  0.0165  32  ALA A C   
249   O O   . ALA A 32  ? 0.2518 0.2703 0.5494 -0.0202 0.0410  0.0157  32  ALA A O   
250   C CB  . ALA A 32  ? 0.2515 0.2562 0.5404 -0.0213 0.0269  0.0118  32  ALA A CB  
251   N N   . ARG A 33  ? 0.2760 0.2944 0.5851 -0.0284 0.0412  0.0196  33  ARG A N   
252   C CA  . ARG A 33  ? 0.2771 0.3014 0.5880 -0.0284 0.0495  0.0223  33  ARG A CA  
253   C C   . ARG A 33  ? 0.2888 0.3251 0.6114 -0.0260 0.0521  0.0207  33  ARG A C   
254   O O   . ARG A 33  ? 0.2978 0.3378 0.6296 -0.0255 0.0468  0.0183  33  ARG A O   
255   C CB  . ARG A 33  ? 0.3013 0.3258 0.6185 -0.0342 0.0523  0.0263  33  ARG A CB  
256   C CG  . ARG A 33  ? 0.2838 0.2987 0.5882 -0.0354 0.0549  0.0294  33  ARG A CG  
257   C CD  . ARG A 33  ? 0.2843 0.2882 0.5763 -0.0331 0.0492  0.0272  33  ARG A CD  
258   N NE  . ARG A 33  ? 0.3128 0.3076 0.5939 -0.0337 0.0511  0.0300  33  ARG A NE  
259   C CZ  . ARG A 33  ? 0.3260 0.3104 0.5985 -0.0332 0.0469  0.0292  33  ARG A CZ  
260   N NH1 . ARG A 33  ? 0.3176 0.2988 0.5883 -0.0317 0.0411  0.0254  33  ARG A NH1 
261   N NH2 . ARG A 33  ? 0.3686 0.3454 0.6337 -0.0341 0.0487  0.0323  33  ARG A NH2 
262   N N   . PRO A 34  ? 0.2940 0.3358 0.6154 -0.0240 0.0600  0.0217  34  PRO A N   
263   C CA  . PRO A 34  ? 0.3141 0.3679 0.6478 -0.0216 0.0636  0.0200  34  PRO A CA  
264   C C   . PRO A 34  ? 0.2987 0.3603 0.6513 -0.0260 0.0618  0.0210  34  PRO A C   
265   O O   . PRO A 34  ? 0.3258 0.3845 0.6804 -0.0315 0.0616  0.0241  34  PRO A O   
266   C CB  . PRO A 34  ? 0.3046 0.3615 0.6327 -0.0205 0.0734  0.0219  34  PRO A CB  
267   C CG  . PRO A 34  ? 0.2954 0.3402 0.6044 -0.0202 0.0729  0.0235  34  PRO A CG  
268   C CD  . PRO A 34  ? 0.2789 0.3153 0.5866 -0.0236 0.0655  0.0242  34  PRO A CD  
269   N N   . GLY A 35  ? 0.3014 0.3714 0.6674 -0.0237 0.0589  0.0182  35  GLY A N   
270   C CA  . GLY A 35  ? 0.2852 0.3638 0.6712 -0.0276 0.0562  0.0188  35  GLY A CA  
271   C C   . GLY A 35  ? 0.2764 0.3477 0.6630 -0.0306 0.0454  0.0181  35  GLY A C   
272   O O   . GLY A 35  ? 0.2609 0.3381 0.6633 -0.0339 0.0413  0.0183  35  GLY A O   
273   N N   . GLN A 36  ? 0.2914 0.3500 0.6609 -0.0293 0.0404  0.0170  36  GLN A N   
274   C CA  . GLN A 36  ? 0.2685 0.3189 0.6358 -0.0320 0.0308  0.0161  36  GLN A CA  
275   C C   . GLN A 36  ? 0.2624 0.3083 0.6223 -0.0274 0.0243  0.0127  36  GLN A C   
276   O O   . GLN A 36  ? 0.2955 0.3393 0.6452 -0.0228 0.0271  0.0115  36  GLN A O   
277   C CB  . GLN A 36  ? 0.2500 0.2882 0.6032 -0.0350 0.0306  0.0178  36  GLN A CB  
278   C CG  . GLN A 36  ? 0.2361 0.2757 0.5932 -0.0399 0.0367  0.0218  36  GLN A CG  
279   C CD  . GLN A 36  ? 0.2281 0.2545 0.5732 -0.0430 0.0342  0.0231  36  GLN A CD  
280   O OE1 . GLN A 36  ? 0.2548 0.2719 0.5843 -0.0401 0.0331  0.0219  36  GLN A OE1 
281   N NE2 . GLN A 36  ? 0.2269 0.2518 0.5792 -0.0490 0.0331  0.0254  36  GLN A NE2 
282   N N   . ALA A 37  ? 0.2622 0.3050 0.6255 -0.0289 0.0151  0.0113  37  ALA A N   
283   C CA  . ALA A 37  ? 0.2722 0.3081 0.6258 -0.0257 0.0083  0.0087  37  ALA A CA  
284   C C   . ALA A 37  ? 0.2886 0.3136 0.6343 -0.0294 0.0006  0.0082  37  ALA A C   
285   O O   . ALA A 37  ? 0.3162 0.3426 0.6719 -0.0329 -0.0056 0.0082  37  ALA A O   
286   C CB  . ALA A 37  ? 0.2817 0.3261 0.6489 -0.0227 0.0043  0.0071  37  ALA A CB  
287   N N   . PRO A 38  ? 0.2812 0.2951 0.6090 -0.0288 0.0007  0.0077  38  PRO A N   
288   C CA  . PRO A 38  ? 0.2950 0.2982 0.6144 -0.0324 -0.0051 0.0070  38  PRO A CA  
289   C C   . PRO A 38  ? 0.3021 0.3016 0.6216 -0.0332 -0.0151 0.0051  38  PRO A C   
290   O O   . PRO A 38  ? 0.2956 0.2884 0.6130 -0.0371 -0.0205 0.0045  38  PRO A O   
291   C CB  . PRO A 38  ? 0.3127 0.3068 0.6139 -0.0302 -0.0017 0.0065  38  PRO A CB  
292   C CG  . PRO A 38  ? 0.2969 0.2961 0.5964 -0.0252 0.0023  0.0062  38  PRO A CG  
293   C CD  . PRO A 38  ? 0.2856 0.2970 0.6011 -0.0248 0.0063  0.0075  38  PRO A CD  
294   N N   . TYR A 39  ? 0.3187 0.3215 0.6403 -0.0296 -0.0180 0.0041  39  TYR A N   
295   C CA  . TYR A 39  ? 0.3528 0.3514 0.6736 -0.0301 -0.0281 0.0027  39  TYR A CA  
296   C C   . TYR A 39  ? 0.3586 0.3668 0.6997 -0.0315 -0.0333 0.0030  39  TYR A C   
297   O O   . TYR A 39  ? 0.3474 0.3522 0.6891 -0.0323 -0.0428 0.0020  39  TYR A O   
298   C CB  . TYR A 39  ? 0.3285 0.3231 0.6386 -0.0258 -0.0297 0.0017  39  TYR A CB  
299   C CG  . TYR A 39  ? 0.3283 0.3133 0.6191 -0.0252 -0.0258 0.0012  39  TYR A CG  
300   C CD1 . TYR A 39  ? 0.3460 0.3202 0.6242 -0.0281 -0.0290 0.0003  39  TYR A CD1 
301   C CD2 . TYR A 39  ? 0.3296 0.3166 0.6156 -0.0218 -0.0185 0.0016  39  TYR A CD2 
302   C CE1 . TYR A 39  ? 0.3693 0.3361 0.6320 -0.0273 -0.0246 -0.0003 39  TYR A CE1 
303   C CE2 . TYR A 39  ? 0.3176 0.2971 0.5883 -0.0213 -0.0149 0.0012  39  TYR A CE2 
304   C CZ  . TYR A 39  ? 0.3424 0.3122 0.6020 -0.0240 -0.0177 0.0003  39  TYR A CZ  
305   O OH  . TYR A 39  ? 0.3067 0.2702 0.5527 -0.0232 -0.0138 -0.0003 39  TYR A OH  
306   N N   . GLU A 40  ? 0.4030 0.4232 0.7609 -0.0321 -0.0276 0.0044  40  GLU A N   
307   C CA  . GLU A 40  ? 0.4400 0.4712 0.8194 -0.0330 -0.0321 0.0046  40  GLU A CA  
308   C C   . GLU A 40  ? 0.4439 0.4804 0.8364 -0.0387 -0.0302 0.0063  40  GLU A C   
309   O O   . GLU A 40  ? 0.4446 0.4866 0.8527 -0.0417 -0.0368 0.0063  40  GLU A O   
310   C CB  . GLU A 40  ? 0.4317 0.4757 0.8246 -0.0281 -0.0270 0.0045  40  GLU A CB  
311   C CG  . GLU A 40  ? 0.5143 0.5544 0.8979 -0.0223 -0.0290 0.0029  40  GLU A CG  
312   C CD  . GLU A 40  ? 0.6229 0.6748 1.0184 -0.0172 -0.0222 0.0025  40  GLU A CD  
313   O OE1 . GLU A 40  ? 0.6303 0.6937 1.0410 -0.0183 -0.0157 0.0034  40  GLU A OE1 
314   O OE2 . GLU A 40  ? 0.7826 0.8320 1.1719 -0.0122 -0.0229 0.0012  40  GLU A OE2 
315   N N   . ASP A 41  ? 0.4441 0.4794 0.8312 -0.0403 -0.0213 0.0079  41  ASP A N   
316   C CA  . ASP A 41  ? 0.4692 0.5089 0.8676 -0.0459 -0.0181 0.0102  41  ASP A CA  
317   C C   . ASP A 41  ? 0.4762 0.5051 0.8695 -0.0514 -0.0266 0.0096  41  ASP A C   
318   O O   . ASP A 41  ? 0.4740 0.4899 0.8490 -0.0505 -0.0309 0.0078  41  ASP A O   
319   C CB  . ASP A 41  ? 0.4637 0.5030 0.8548 -0.0457 -0.0069 0.0123  41  ASP A CB  
320   C CG  . ASP A 41  ? 0.4886 0.5396 0.8867 -0.0414 0.0023  0.0130  41  ASP A CG  
321   O OD1 . ASP A 41  ? 0.4569 0.5190 0.8704 -0.0390 0.0009  0.0120  41  ASP A OD1 
322   O OD2 . ASP A 41  ? 0.4546 0.5033 0.8426 -0.0402 0.0105  0.0144  41  ASP A OD2 
323   N N   . GLU A 42  ? 0.4465 0.4807 0.8559 -0.0571 -0.0286 0.0111  42  GLU A N   
324   C CA  . GLU A 42  ? 0.4877 0.5111 0.8921 -0.0630 -0.0346 0.0109  42  GLU A CA  
325   C C   . GLU A 42  ? 0.4352 0.4458 0.8189 -0.0625 -0.0291 0.0111  42  GLU A C   
326   O O   . GLU A 42  ? 0.3808 0.3948 0.7629 -0.0610 -0.0192 0.0133  42  GLU A O   
327   C CB  . GLU A 42  ? 0.5339 0.5656 0.9592 -0.0697 -0.0349 0.0132  42  GLU A CB  
328   C CG  . GLU A 42  ? 0.6707 0.6925 1.0952 -0.0756 -0.0459 0.0119  42  GLU A CG  
329   C CD  . GLU A 42  ? 0.8093 0.8380 1.2546 -0.0833 -0.0477 0.0142  42  GLU A CD  
330   O OE1 . GLU A 42  ? 0.8110 0.8364 1.2558 -0.0877 -0.0418 0.0168  42  GLU A OE1 
331   O OE2 . GLU A 42  ? 0.7796 0.8169 1.2424 -0.0850 -0.0554 0.0135  42  GLU A OE2 
332   N N   . ARG A 43  ? 0.4200 0.4159 0.7874 -0.0633 -0.0357 0.0086  43  ARG A N   
333   C CA  . ARG A 43  ? 0.4169 0.4006 0.7641 -0.0615 -0.0313 0.0080  43  ARG A CA  
334   C C   . ARG A 43  ? 0.3668 0.3463 0.7160 -0.0663 -0.0276 0.0102  43  ARG A C   
335   O O   . ARG A 43  ? 0.3520 0.3287 0.7085 -0.0718 -0.0334 0.0102  43  ARG A O   
336   C CB  . ARG A 43  ? 0.4536 0.4232 0.7827 -0.0604 -0.0387 0.0043  43  ARG A CB  
337   C CG  . ARG A 43  ? 0.5214 0.4836 0.8314 -0.0556 -0.0329 0.0033  43  ARG A CG  
338   C CD  . ARG A 43  ? 0.5531 0.4992 0.8444 -0.0560 -0.0374 0.0000  43  ARG A CD  
339   N NE  . ARG A 43  ? 0.5947 0.5335 0.8887 -0.0615 -0.0418 -0.0005 43  ARG A NE  
340   C CZ  . ARG A 43  ? 0.5556 0.4878 0.8465 -0.0634 -0.0379 0.0003  43  ARG A CZ  
341   N NH1 . ARG A 43  ? 0.5156 0.4468 0.7991 -0.0598 -0.0295 0.0015  43  ARG A NH1 
342   N NH2 . ARG A 43  ? 0.4739 0.3996 0.7687 -0.0689 -0.0433 -0.0002 43  ARG A NH2 
343   N N   . LYS A 44  ? 0.3480 0.3274 0.6912 -0.0642 -0.0183 0.0124  44  LYS A N   
344   C CA  . LYS A 44  ? 0.3835 0.3576 0.7257 -0.0677 -0.0139 0.0150  44  LYS A CA  
345   C C   . LYS A 44  ? 0.3553 0.3173 0.6776 -0.0640 -0.0108 0.0138  44  LYS A C   
346   O O   . LYS A 44  ? 0.3601 0.3232 0.6734 -0.0585 -0.0084 0.0125  44  LYS A O   
347   C CB  . LYS A 44  ? 0.3952 0.3815 0.7488 -0.0681 -0.0045 0.0194  44  LYS A CB  
348   C CG  . LYS A 44  ? 0.4145 0.4142 0.7899 -0.0722 -0.0053 0.0211  44  LYS A CG  
349   C CD  . LYS A 44  ? 0.4469 0.4591 0.8336 -0.0729 0.0048  0.0253  44  LYS A CD  
350   C CE  . LYS A 44  ? 0.5087 0.5352 0.9187 -0.0763 0.0025  0.0259  44  LYS A CE  
351   N NZ  . LYS A 44  ? 0.5383 0.5789 0.9628 -0.0778 0.0122  0.0296  44  LYS A NZ  
352   N N   . ASP A 45  ? 0.3687 0.3200 0.6855 -0.0669 -0.0106 0.0147  45  ASP A N   
353   C CA  . ASP A 45  ? 0.3740 0.3132 0.6735 -0.0634 -0.0086 0.0132  45  ASP A CA  
354   C C   . ASP A 45  ? 0.3588 0.3023 0.6557 -0.0601 0.0006  0.0166  45  ASP A C   
355   O O   . ASP A 45  ? 0.3626 0.3018 0.6471 -0.0550 0.0030  0.0152  45  ASP A O   
356   C CB  . ASP A 45  ? 0.4037 0.3285 0.6983 -0.0673 -0.0130 0.0122  45  ASP A CB  
357   C CG  . ASP A 45  ? 0.4156 0.3311 0.7034 -0.0683 -0.0221 0.0071  45  ASP A CG  
358   O OD1 . ASP A 45  ? 0.4338 0.3516 0.7162 -0.0648 -0.0244 0.0043  45  ASP A OD1 
359   O OD2 . ASP A 45  ? 0.4172 0.3224 0.7045 -0.0726 -0.0270 0.0061  45  ASP A OD2 
360   N N   . GLU A 46  ? 0.3399 0.2919 0.6486 -0.0632 0.0055  0.0211  46  GLU A N   
361   C CA  . GLU A 46  ? 0.3375 0.2946 0.6441 -0.0605 0.0140  0.0246  46  GLU A CA  
362   C C   . GLU A 46  ? 0.3404 0.2853 0.6333 -0.0585 0.0161  0.0254  46  GLU A C   
363   O O   . GLU A 46  ? 0.3298 0.2756 0.6144 -0.0535 0.0206  0.0259  46  GLU A O   
364   C CB  . GLU A 46  ? 0.3615 0.3270 0.6654 -0.0546 0.0162  0.0226  46  GLU A CB  
365   C CG  . GLU A 46  ? 0.3932 0.3705 0.7104 -0.0553 0.0138  0.0215  46  GLU A CG  
366   C CD  . GLU A 46  ? 0.4194 0.4102 0.7489 -0.0559 0.0206  0.0248  46  GLU A CD  
367   O OE1 . GLU A 46  ? 0.4930 0.4889 0.8343 -0.0608 0.0233  0.0280  46  GLU A OE1 
368   O OE2 . GLU A 46  ? 0.5527 0.5493 0.8794 -0.0510 0.0236  0.0237  46  GLU A OE2 
369   N N   . LEU A 47  ? 0.3197 0.2531 0.6107 -0.0622 0.0125  0.0255  47  LEU A N   
370   C CA  . LEU A 47  ? 0.3339 0.2541 0.6120 -0.0597 0.0127  0.0252  47  LEU A CA  
371   C C   . LEU A 47  ? 0.3513 0.2721 0.6261 -0.0583 0.0196  0.0300  47  LEU A C   
372   O O   . LEU A 47  ? 0.3403 0.2548 0.6041 -0.0534 0.0209  0.0294  47  LEU A O   
373   C CB  . LEU A 47  ? 0.3373 0.2448 0.6155 -0.0645 0.0071  0.0243  47  LEU A CB  
374   C CG  . LEU A 47  ? 0.3502 0.2533 0.6276 -0.0655 -0.0007 0.0189  47  LEU A CG  
375   C CD1 . LEU A 47  ? 0.3855 0.2751 0.6628 -0.0706 -0.0063 0.0181  47  LEU A CD1 
376   C CD2 . LEU A 47  ? 0.3383 0.2373 0.6025 -0.0591 -0.0018 0.0139  47  LEU A CD2 
377   N N   . GLU A 48  ? 0.3947 0.3224 0.6789 -0.0627 0.0238  0.0350  48  GLU A N   
378   C CA  . GLU A 48  ? 0.4316 0.3591 0.7116 -0.0621 0.0302  0.0402  48  GLU A CA  
379   C C   . GLU A 48  ? 0.4172 0.3516 0.6904 -0.0554 0.0341  0.0390  48  GLU A C   
380   O O   . GLU A 48  ? 0.4478 0.3764 0.7104 -0.0515 0.0359  0.0400  48  GLU A O   
381   C CB  . GLU A 48  ? 0.4733 0.4071 0.7640 -0.0686 0.0348  0.0458  48  GLU A CB  
382   C CG  . GLU A 48  ? 0.5872 0.5124 0.8841 -0.0759 0.0312  0.0479  48  GLU A CG  
383   C CD  . GLU A 48  ? 0.7033 0.6104 0.9891 -0.0755 0.0275  0.0482  48  GLU A CD  
384   O OE1 . GLU A 48  ? 0.6601 0.5612 0.9354 -0.0721 0.0307  0.0509  48  GLU A OE1 
385   O OE2 . GLU A 48  ? 0.7763 0.6744 1.0637 -0.0783 0.0209  0.0454  48  GLU A OE2 
386   N N   . LEU A 49  ? 0.3603 0.3065 0.6397 -0.0539 0.0346  0.0366  49  LEU A N   
387   C CA  . LEU A 49  ? 0.3729 0.3252 0.6462 -0.0480 0.0380  0.0354  49  LEU A CA  
388   C C   . LEU A 49  ? 0.3271 0.2720 0.5892 -0.0427 0.0344  0.0313  49  LEU A C   
389   O O   . LEU A 49  ? 0.3151 0.2601 0.5692 -0.0382 0.0370  0.0315  49  LEU A O   
390   C CB  . LEU A 49  ? 0.3616 0.3277 0.6446 -0.0475 0.0394  0.0339  49  LEU A CB  
391   C CG  . LEU A 49  ? 0.3598 0.3353 0.6539 -0.0517 0.0451  0.0380  49  LEU A CG  
392   C CD1 . LEU A 49  ? 0.3414 0.3306 0.6470 -0.0509 0.0458  0.0358  49  LEU A CD1 
393   C CD2 . LEU A 49  ? 0.3631 0.3382 0.6489 -0.0502 0.0521  0.0420  49  LEU A CD2 
394   N N   . MET A 50  ? 0.3223 0.2609 0.5838 -0.0434 0.0286  0.0276  50  MET A N   
395   C CA  . MET A 50  ? 0.3571 0.2882 0.6081 -0.0388 0.0260  0.0238  50  MET A CA  
396   C C   . MET A 50  ? 0.3536 0.2751 0.5965 -0.0368 0.0273  0.0257  50  MET A C   
397   O O   . MET A 50  ? 0.3896 0.3098 0.6250 -0.0318 0.0281  0.0242  50  MET A O   
398   C CB  . MET A 50  ? 0.3677 0.2923 0.6181 -0.0403 0.0198  0.0195  50  MET A CB  
399   C CG  . MET A 50  ? 0.3605 0.2931 0.6162 -0.0409 0.0171  0.0168  50  MET A CG  
400   S SD  . MET A 50  ? 0.3628 0.2868 0.6127 -0.0412 0.0098  0.0112  50  MET A SD  
401   C CE  . MET A 50  ? 0.3384 0.2560 0.5742 -0.0349 0.0118  0.0084  50  MET A CE  
402   N N   . LYS A 51  ? 0.3922 0.3067 0.6369 -0.0408 0.0272  0.0291  51  LYS A N   
403   C CA  . LYS A 51  ? 0.4095 0.3138 0.6467 -0.0388 0.0277  0.0312  51  LYS A CA  
404   C C   . LYS A 51  ? 0.3961 0.3058 0.6288 -0.0351 0.0323  0.0341  51  LYS A C   
405   O O   . LYS A 51  ? 0.4091 0.3142 0.6344 -0.0302 0.0320  0.0333  51  LYS A O   
406   C CB  . LYS A 51  ? 0.4251 0.3207 0.6645 -0.0439 0.0274  0.0357  51  LYS A CB  
407   C CG  . LYS A 51  ? 0.4860 0.3701 0.7256 -0.0464 0.0219  0.0328  51  LYS A CG  
408   C CD  . LYS A 51  ? 0.5446 0.4231 0.7907 -0.0538 0.0207  0.0366  51  LYS A CD  
409   C CE  . LYS A 51  ? 0.5706 0.4442 0.8211 -0.0576 0.0148  0.0326  51  LYS A CE  
410   N NZ  . LYS A 51  ? 0.5951 0.4660 0.8543 -0.0656 0.0139  0.0368  51  LYS A NZ  
411   N N   . PHE A 52  ? 0.3700 0.2892 0.6076 -0.0375 0.0365  0.0374  52  PHE A N   
412   C CA  . PHE A 52  ? 0.3470 0.2712 0.5796 -0.0345 0.0410  0.0401  52  PHE A CA  
413   C C   . PHE A 52  ? 0.3592 0.2876 0.5873 -0.0286 0.0400  0.0358  52  PHE A C   
414   O O   . PHE A 52  ? 0.3724 0.2977 0.5930 -0.0245 0.0403  0.0363  52  PHE A O   
415   C CB  . PHE A 52  ? 0.3315 0.2658 0.5711 -0.0383 0.0459  0.0432  52  PHE A CB  
416   C CG  . PHE A 52  ? 0.3241 0.2659 0.5591 -0.0350 0.0507  0.0445  52  PHE A CG  
417   C CD1 . PHE A 52  ? 0.3311 0.2686 0.5578 -0.0346 0.0539  0.0492  52  PHE A CD1 
418   C CD2 . PHE A 52  ? 0.3023 0.2543 0.5405 -0.0325 0.0515  0.0410  52  PHE A CD2 
419   C CE1 . PHE A 52  ? 0.3417 0.2850 0.5628 -0.0316 0.0578  0.0500  52  PHE A CE1 
420   C CE2 . PHE A 52  ? 0.3112 0.2690 0.5445 -0.0294 0.0556  0.0416  52  PHE A CE2 
421   C CZ  . PHE A 52  ? 0.3347 0.2880 0.5591 -0.0290 0.0587  0.0460  52  PHE A CZ  
422   N N   . ASP A 53  ? 0.3364 0.2709 0.5693 -0.0284 0.0383  0.0316  53  ASP A N   
423   C CA  . ASP A 53  ? 0.3372 0.2761 0.5667 -0.0237 0.0376  0.0277  53  ASP A CA  
424   C C   . ASP A 53  ? 0.3310 0.2617 0.5538 -0.0202 0.0347  0.0251  53  ASP A C   
425   O O   . ASP A 53  ? 0.3257 0.2575 0.5436 -0.0160 0.0354  0.0246  53  ASP A O   
426   C CB  . ASP A 53  ? 0.3230 0.2689 0.5589 -0.0249 0.0359  0.0245  53  ASP A CB  
427   C CG  . ASP A 53  ? 0.3070 0.2629 0.5509 -0.0272 0.0389  0.0262  53  ASP A CG  
428   O OD1 . ASP A 53  ? 0.2720 0.2318 0.5145 -0.0265 0.0434  0.0292  53  ASP A OD1 
429   O OD2 . ASP A 53  ? 0.3072 0.2668 0.5588 -0.0296 0.0364  0.0244  53  ASP A OD2 
430   N N   . LEU A 54  ? 0.3238 0.2466 0.5470 -0.0217 0.0314  0.0232  54  LEU A N   
431   C CA  . LEU A 54  ? 0.3391 0.2547 0.5565 -0.0179 0.0294  0.0200  54  LEU A CA  
432   C C   . LEU A 54  ? 0.3448 0.2557 0.5576 -0.0146 0.0304  0.0227  54  LEU A C   
433   O O   . LEU A 54  ? 0.3377 0.2486 0.5469 -0.0099 0.0303  0.0206  54  LEU A O   
434   C CB  . LEU A 54  ? 0.3474 0.2542 0.5651 -0.0203 0.0258  0.0173  54  LEU A CB  
435   C CG  . LEU A 54  ? 0.3524 0.2624 0.5726 -0.0226 0.0234  0.0137  54  LEU A CG  
436   C CD1 . LEU A 54  ? 0.3632 0.2626 0.5813 -0.0243 0.0195  0.0106  54  LEU A CD1 
437   C CD2 . LEU A 54  ? 0.3502 0.2667 0.5673 -0.0191 0.0239  0.0104  54  LEU A CD2 
438   N N   . GLU A 55  ? 0.3253 0.2327 0.5385 -0.0172 0.0316  0.0276  55  GLU A N   
439   C CA  . GLU A 55  ? 0.3407 0.2433 0.5489 -0.0145 0.0322  0.0312  55  GLU A CA  
440   C C   . GLU A 55  ? 0.3547 0.2655 0.5600 -0.0110 0.0342  0.0318  55  GLU A C   
441   O O   . GLU A 55  ? 0.3498 0.2586 0.5512 -0.0064 0.0331  0.0313  55  GLU A O   
442   C CB  . GLU A 55  ? 0.3524 0.2498 0.5609 -0.0191 0.0334  0.0369  55  GLU A CB  
443   C CG  . GLU A 55  ? 0.4043 0.2933 0.6065 -0.0165 0.0327  0.0409  55  GLU A CG  
444   C CD  . GLU A 55  ? 0.4291 0.3090 0.6289 -0.0118 0.0289  0.0379  55  GLU A CD  
445   O OE1 . GLU A 55  ? 0.4217 0.2960 0.6240 -0.0124 0.0266  0.0340  55  GLU A OE1 
446   O OE2 . GLU A 55  ? 0.3960 0.2746 0.5916 -0.0073 0.0282  0.0392  55  GLU A OE2 
447   N N   . ASN A 56  ? 0.3597 0.2797 0.5673 -0.0130 0.0370  0.0325  56  ASN A N   
448   C CA  . ASN A 56  ? 0.3553 0.2825 0.5597 -0.0100 0.0387  0.0326  56  ASN A CA  
449   C C   . ASN A 56  ? 0.3570 0.2864 0.5605 -0.0056 0.0366  0.0280  56  ASN A C   
450   O O   . ASN A 56  ? 0.3941 0.3240 0.5938 -0.0019 0.0360  0.0283  56  ASN A O   
451   C CB  . ASN A 56  ? 0.3557 0.2924 0.5636 -0.0124 0.0419  0.0328  56  ASN A CB  
452   C CG  . ASN A 56  ? 0.3743 0.3109 0.5827 -0.0163 0.0454  0.0378  56  ASN A CG  
453   O OD1 . ASN A 56  ? 0.3851 0.3155 0.5880 -0.0164 0.0461  0.0419  56  ASN A OD1 
454   N ND2 . ASN A 56  ? 0.3960 0.3399 0.6110 -0.0194 0.0479  0.0376  56  ASN A ND2 
455   N N   . ILE A 57  ? 0.3435 0.2743 0.5506 -0.0064 0.0354  0.0240  57  ILE A N   
456   C CA  . ILE A 57  ? 0.3392 0.2729 0.5457 -0.0032 0.0342  0.0197  57  ILE A CA  
457   C C   . ILE A 57  ? 0.3952 0.3230 0.5995 0.0006  0.0326  0.0186  57  ILE A C   
458   O O   . ILE A 57  ? 0.4077 0.3390 0.6113 0.0040  0.0324  0.0167  57  ILE A O   
459   C CB  . ILE A 57  ? 0.2937 0.2286 0.5031 -0.0056 0.0332  0.0162  57  ILE A CB  
460   C CG1 . ILE A 57  ? 0.2847 0.2272 0.4976 -0.0080 0.0344  0.0169  57  ILE A CG1 
461   C CG2 . ILE A 57  ? 0.3004 0.2360 0.5080 -0.0028 0.0322  0.0120  57  ILE A CG2 
462   C CD1 . ILE A 57  ? 0.2943 0.2378 0.5107 -0.0108 0.0325  0.0144  57  ILE A CD1 
463   N N   . LYS A 58  ? 0.3721 0.2908 0.5759 0.0000  0.0315  0.0199  58  LYS A N   
464   C CA  . LYS A 58  ? 0.3636 0.2762 0.5660 0.0041  0.0299  0.0190  58  LYS A CA  
465   C C   . LYS A 58  ? 0.3563 0.2701 0.5564 0.0072  0.0295  0.0224  58  LYS A C   
466   O O   . LYS A 58  ? 0.3327 0.2482 0.5334 0.0115  0.0285  0.0206  58  LYS A O   
467   C CB  . LYS A 58  ? 0.3715 0.2730 0.5737 0.0028  0.0283  0.0194  58  LYS A CB  
468   C CG  . LYS A 58  ? 0.3725 0.2708 0.5755 0.0012  0.0276  0.0147  58  LYS A CG  
469   C CD  . LYS A 58  ? 0.3933 0.2808 0.5963 -0.0020 0.0257  0.0158  58  LYS A CD  
470   C CE  . LYS A 58  ? 0.4220 0.2995 0.6233 0.0015  0.0240  0.0164  58  LYS A CE  
471   N NZ  . LYS A 58  ? 0.4488 0.3155 0.6500 -0.0023 0.0220  0.0168  58  LYS A NZ  
472   N N   . GLU A 59  ? 0.3464 0.2594 0.5439 0.0047  0.0304  0.0272  59  GLU A N   
473   C CA  . GLU A 59  ? 0.3398 0.2537 0.5331 0.0070  0.0299  0.0307  59  GLU A CA  
474   C C   . GLU A 59  ? 0.3380 0.2617 0.5311 0.0088  0.0305  0.0288  59  GLU A C   
475   O O   . GLU A 59  ? 0.3514 0.2759 0.5414 0.0116  0.0290  0.0304  59  GLU A O   
476   C CB  . GLU A 59  ? 0.3658 0.2762 0.5552 0.0032  0.0316  0.0362  59  GLU A CB  
477   C CG  . GLU A 59  ? 0.4147 0.3134 0.6031 0.0020  0.0300  0.0393  59  GLU A CG  
478   C CD  . GLU A 59  ? 0.4525 0.3481 0.6379 -0.0030 0.0324  0.0449  59  GLU A CD  
479   O OE1 . GLU A 59  ? 0.4778 0.3771 0.6581 -0.0030 0.0343  0.0478  59  GLU A OE1 
480   O OE2 . GLU A 59  ? 0.4553 0.3449 0.6431 -0.0070 0.0327  0.0463  59  GLU A OE2 
481   N N   . GLY A 60  ? 0.3221 0.2527 0.5184 0.0072  0.0321  0.0255  60  GLY A N   
482   C CA  . GLY A 60  ? 0.3053 0.2440 0.5015 0.0088  0.0323  0.0235  60  GLY A CA  
483   C C   . GLY A 60  ? 0.3121 0.2531 0.5114 0.0121  0.0307  0.0199  60  GLY A C   
484   O O   . GLY A 60  ? 0.3328 0.2799 0.5324 0.0134  0.0303  0.0184  60  GLY A O   
485   N N   . GLY A 61  ? 0.2794 0.2155 0.4810 0.0132  0.0301  0.0180  61  GLY A N   
486   C CA  . GLY A 61  ? 0.2571 0.1946 0.4620 0.0170  0.0292  0.0149  61  GLY A CA  
487   C C   . GLY A 61  ? 0.2535 0.1928 0.4605 0.0161  0.0309  0.0104  61  GLY A C   
488   O O   . GLY A 61  ? 0.2503 0.1918 0.4601 0.0188  0.0312  0.0075  61  GLY A O   
489   N N   . TYR A 62  ? 0.2581 0.1968 0.4637 0.0121  0.0319  0.0100  62  TYR A N   
490   C CA  . TYR A 62  ? 0.2599 0.1997 0.4656 0.0107  0.0329  0.0061  62  TYR A CA  
491   C C   . TYR A 62  ? 0.2623 0.1944 0.4674 0.0117  0.0328  0.0036  62  TYR A C   
492   O O   . TYR A 62  ? 0.2859 0.2110 0.4908 0.0121  0.0317  0.0054  62  TYR A O   
493   C CB  . TYR A 62  ? 0.2640 0.2060 0.4689 0.0065  0.0330  0.0068  62  TYR A CB  
494   C CG  . TYR A 62  ? 0.2763 0.2251 0.4815 0.0061  0.0333  0.0089  62  TYR A CG  
495   C CD1 . TYR A 62  ? 0.2657 0.2205 0.4711 0.0068  0.0335  0.0071  62  TYR A CD1 
496   C CD2 . TYR A 62  ? 0.3002 0.2488 0.5047 0.0053  0.0336  0.0124  62  TYR A CD2 
497   C CE1 . TYR A 62  ? 0.2647 0.2246 0.4697 0.0068  0.0334  0.0085  62  TYR A CE1 
498   C CE2 . TYR A 62  ? 0.3251 0.2793 0.5287 0.0055  0.0341  0.0137  62  TYR A CE2 
499   C CZ  . TYR A 62  ? 0.2928 0.2523 0.4967 0.0064  0.0337  0.0115  62  TYR A CZ  
500   O OH  . TYR A 62  ? 0.2857 0.2496 0.4883 0.0068  0.0338  0.0123  62  TYR A OH  
501   N N   . ASN A 63  ? 0.2601 0.1925 0.4643 0.0120  0.0340  -0.0004 63  ASN A N   
502   C CA  . ASN A 63  ? 0.2739 0.1984 0.4762 0.0129  0.0342  -0.0036 63  ASN A CA  
503   C C   . ASN A 63  ? 0.2803 0.2019 0.4784 0.0089  0.0337  -0.0057 63  ASN A C   
504   O O   . ASN A 63  ? 0.2905 0.2047 0.4856 0.0090  0.0334  -0.0087 63  ASN A O   
505   C CB  . ASN A 63  ? 0.2729 0.1986 0.4768 0.0175  0.0362  -0.0070 63  ASN A CB  
506   C CG  . ASN A 63  ? 0.2825 0.2162 0.4862 0.0171  0.0387  -0.0092 63  ASN A CG  
507   O OD1 . ASN A 63  ? 0.2868 0.2224 0.4873 0.0134  0.0386  -0.0092 63  ASN A OD1 
508   N ND2 . ASN A 63  ? 0.2909 0.2290 0.4982 0.0208  0.0410  -0.0113 63  ASN A ND2 
509   N N   . THR A 64  ? 0.2924 0.2197 0.4905 0.0057  0.0333  -0.0043 64  THR A N   
510   C CA  . THR A 64  ? 0.2849 0.2106 0.4794 0.0022  0.0321  -0.0062 64  THR A CA  
511   C C   . THR A 64  ? 0.2854 0.2157 0.4825 -0.0011 0.0306  -0.0032 64  THR A C   
512   O O   . THR A 64  ? 0.3018 0.2386 0.5017 -0.0002 0.0315  -0.0009 64  THR A O   
513   C CB  . THR A 64  ? 0.2711 0.2002 0.4621 0.0030  0.0340  -0.0092 64  THR A CB  
514   O OG1 . THR A 64  ? 0.2551 0.1812 0.4448 0.0064  0.0364  -0.0122 64  THR A OG1 
515   C CG2 . THR A 64  ? 0.2683 0.1948 0.4540 -0.0005 0.0323  -0.0109 64  THR A CG2 
516   N N   . ILE A 65  ? 0.2910 0.2183 0.4873 -0.0046 0.0282  -0.0038 65  ILE A N   
517   C CA  . ILE A 65  ? 0.2846 0.2172 0.4840 -0.0074 0.0267  -0.0019 65  ILE A CA  
518   C C   . ILE A 65  ? 0.2728 0.2055 0.4681 -0.0089 0.0249  -0.0044 65  ILE A C   
519   O O   . ILE A 65  ? 0.2719 0.1985 0.4612 -0.0090 0.0243  -0.0075 65  ILE A O   
520   C CB  . ILE A 65  ? 0.3071 0.2378 0.5113 -0.0106 0.0249  0.0003  65  ILE A CB  
521   C CG1 . ILE A 65  ? 0.3271 0.2484 0.5286 -0.0126 0.0222  -0.0020 65  ILE A CG1 
522   C CG2 . ILE A 65  ? 0.3057 0.2379 0.5134 -0.0095 0.0270  0.0039  65  ILE A CG2 
523   C CD1 . ILE A 65  ? 0.3352 0.2552 0.5424 -0.0169 0.0196  0.0000  65  ILE A CD1 
524   N N   . ARG A 66  ? 0.2644 0.2031 0.4623 -0.0100 0.0239  -0.0031 66  ARG A N   
525   C CA  . ARG A 66  ? 0.2657 0.2043 0.4598 -0.0115 0.0215  -0.0046 66  ARG A CA  
526   C C   . ARG A 66  ? 0.2547 0.1962 0.4546 -0.0140 0.0182  -0.0031 66  ARG A C   
527   O O   . ARG A 66  ? 0.2346 0.1821 0.4411 -0.0135 0.0194  -0.0008 66  ARG A O   
528   C CB  . ARG A 66  ? 0.2749 0.2184 0.4670 -0.0096 0.0236  -0.0045 66  ARG A CB  
529   C CG  . ARG A 66  ? 0.2864 0.2305 0.4750 -0.0111 0.0213  -0.0050 66  ARG A CG  
530   C CD  . ARG A 66  ? 0.2966 0.2452 0.4910 -0.0120 0.0186  -0.0032 66  ARG A CD  
531   N NE  . ARG A 66  ? 0.3254 0.2747 0.5162 -0.0123 0.0170  -0.0032 66  ARG A NE  
532   C CZ  . ARG A 66  ? 0.3569 0.3037 0.5454 -0.0141 0.0127  -0.0035 66  ARG A CZ  
533   N NH1 . ARG A 66  ? 0.3467 0.2899 0.5358 -0.0161 0.0089  -0.0041 66  ARG A NH1 
534   N NH2 . ARG A 66  ? 0.3497 0.2969 0.5351 -0.0141 0.0116  -0.0030 66  ARG A NH2 
535   N N   . THR A 67  ? 0.2721 0.2093 0.4695 -0.0165 0.0140  -0.0046 67  THR A N   
536   C CA  . THR A 67  ? 0.2744 0.2140 0.4789 -0.0190 0.0100  -0.0034 67  THR A CA  
537   C C   . THR A 67  ? 0.2696 0.2087 0.4708 -0.0199 0.0057  -0.0043 67  THR A C   
538   O O   . THR A 67  ? 0.2798 0.2150 0.4715 -0.0193 0.0059  -0.0059 67  THR A O   
539   C CB  . THR A 67  ? 0.2815 0.2154 0.4877 -0.0218 0.0073  -0.0041 67  THR A CB  
540   O OG1 . THR A 67  ? 0.2551 0.1807 0.4511 -0.0226 0.0045  -0.0071 67  THR A OG1 
541   C CG2 . THR A 67  ? 0.2935 0.2254 0.5013 -0.0210 0.0110  -0.0031 67  THR A CG2 
542   N N   . TRP A 68  ? 0.2639 0.2067 0.4730 -0.0215 0.0019  -0.0033 68  TRP A N   
543   C CA  . TRP A 68  ? 0.2823 0.2249 0.4897 -0.0220 -0.0030 -0.0036 68  TRP A CA  
544   C C   . TRP A 68  ? 0.2976 0.2352 0.5051 -0.0252 -0.0097 -0.0047 68  TRP A C   
545   O O   . TRP A 68  ? 0.3525 0.2856 0.5532 -0.0260 -0.0146 -0.0056 68  TRP A O   
546   C CB  . TRP A 68  ? 0.2668 0.2183 0.4841 -0.0204 -0.0027 -0.0018 68  TRP A CB  
547   C CG  . TRP A 68  ? 0.2621 0.2164 0.4762 -0.0175 0.0019  -0.0013 68  TRP A CG  
548   C CD1 . TRP A 68  ? 0.2939 0.2469 0.5021 -0.0165 0.0008  -0.0015 68  TRP A CD1 
549   C CD2 . TRP A 68  ? 0.2729 0.2310 0.4889 -0.0156 0.0078  -0.0004 68  TRP A CD2 
550   N NE1 . TRP A 68  ? 0.3171 0.2732 0.5242 -0.0142 0.0056  -0.0010 68  TRP A NE1 
551   C CE2 . TRP A 68  ? 0.2817 0.2409 0.4933 -0.0135 0.0098  -0.0004 68  TRP A CE2 
552   C CE3 . TRP A 68  ? 0.2883 0.2482 0.5090 -0.0158 0.0112  0.0006  68  TRP A CE3 
553   C CZ2 . TRP A 68  ? 0.2734 0.2359 0.4853 -0.0114 0.0146  0.0003  68  TRP A CZ2 
554   C CZ3 . TRP A 68  ? 0.3046 0.2675 0.5251 -0.0135 0.0161  0.0017  68  TRP A CZ3 
555   C CH2 . TRP A 68  ? 0.3196 0.2839 0.5357 -0.0112 0.0175  0.0013  68  TRP A CH2 
556   N N   . SER A 69  ? 0.3168 0.2540 0.5304 -0.0271 -0.0100 -0.0046 69  SER A N   
557   C CA  . SER A 69  ? 0.3197 0.2538 0.5371 -0.0306 -0.0166 -0.0053 69  SER A CA  
558   C C   . SER A 69  ? 0.3227 0.2486 0.5352 -0.0325 -0.0162 -0.0069 69  SER A C   
559   O O   . SER A 69  ? 0.3237 0.2510 0.5390 -0.0317 -0.0109 -0.0059 69  SER A O   
560   C CB  . SER A 69  ? 0.3282 0.2722 0.5624 -0.0315 -0.0171 -0.0030 69  SER A CB  
561   O OG  . SER A 69  ? 0.3640 0.3074 0.6038 -0.0343 -0.0249 -0.0035 69  SER A OG  
562   N N   . GLN A 70  ? 0.3296 0.2468 0.5351 -0.0350 -0.0224 -0.0093 70  GLN A N   
563   C CA  . GLN A 70  ? 0.3533 0.2607 0.5522 -0.0367 -0.0229 -0.0116 70  GLN A CA  
564   C C   . GLN A 70  ? 0.3441 0.2538 0.5552 -0.0390 -0.0219 -0.0099 70  GLN A C   
565   O O   . GLN A 70  ? 0.3228 0.2385 0.5469 -0.0417 -0.0252 -0.0080 70  GLN A O   
566   C CB  . GLN A 70  ? 0.3627 0.2602 0.5529 -0.0396 -0.0310 -0.0146 70  GLN A CB  
567   C CG  . GLN A 70  ? 0.3475 0.2491 0.5483 -0.0427 -0.0392 -0.0134 70  GLN A CG  
568   C CD  . GLN A 70  ? 0.3352 0.2388 0.5320 -0.0414 -0.0428 -0.0129 70  GLN A CD  
569   O OE1 . GLN A 70  ? 0.3086 0.2171 0.5037 -0.0382 -0.0377 -0.0116 70  GLN A OE1 
570   N NE2 . GLN A 70  ? 0.3451 0.2434 0.5385 -0.0440 -0.0520 -0.0141 70  GLN A NE2 
571   N N   . TYR A 71  ? 0.3406 0.2445 0.5472 -0.0381 -0.0178 -0.0107 71  TYR A N   
572   C CA  . TYR A 71  ? 0.3283 0.2316 0.5441 -0.0408 -0.0174 -0.0090 71  TYR A CA  
573   C C   . TYR A 71  ? 0.3134 0.2072 0.5278 -0.0452 -0.0247 -0.0114 71  TYR A C   
574   O O   . TYR A 71  ? 0.3435 0.2283 0.5454 -0.0450 -0.0285 -0.0151 71  TYR A O   
575   C CB  . TYR A 71  ? 0.3236 0.2226 0.5346 -0.0381 -0.0112 -0.0089 71  TYR A CB  
576   C CG  . TYR A 71  ? 0.3124 0.2209 0.5285 -0.0349 -0.0043 -0.0056 71  TYR A CG  
577   C CD1 . TYR A 71  ? 0.2956 0.2154 0.5232 -0.0357 -0.0031 -0.0022 71  TYR A CD1 
578   C CD2 . TYR A 71  ? 0.3053 0.2110 0.5145 -0.0309 0.0008  -0.0061 71  TYR A CD2 
579   C CE1 . TYR A 71  ? 0.2822 0.2094 0.5126 -0.0328 0.0029  0.0005  71  TYR A CE1 
580   C CE2 . TYR A 71  ? 0.3041 0.2177 0.5169 -0.0281 0.0062  -0.0032 71  TYR A CE2 
581   C CZ  . TYR A 71  ? 0.2934 0.2172 0.5159 -0.0292 0.0071  0.0000  71  TYR A CZ  
582   O OH  . TYR A 71  ? 0.3279 0.2579 0.5521 -0.0263 0.0122  0.0024  71  TYR A OH  
583   N N   . SER A 72  ? 0.2799 0.1756 0.5066 -0.0493 -0.0266 -0.0091 72  SER A N   
584   C CA  . SER A 72  ? 0.3029 0.1884 0.5288 -0.0538 -0.0331 -0.0112 72  SER A CA  
585   C C   . SER A 72  ? 0.3195 0.1925 0.5347 -0.0523 -0.0304 -0.0135 72  SER A C   
586   O O   . SER A 72  ? 0.3234 0.1979 0.5353 -0.0481 -0.0234 -0.0126 72  SER A O   
587   C CB  . SER A 72  ? 0.2993 0.1911 0.5429 -0.0590 -0.0351 -0.0077 72  SER A CB  
588   O OG  . SER A 72  ? 0.2827 0.1763 0.5315 -0.0589 -0.0282 -0.0043 72  SER A OG  
589   N N   . GLU A 73  ? 0.3475 0.2082 0.5579 -0.0555 -0.0362 -0.0166 73  GLU A N   
590   C CA  . GLU A 73  ? 0.3696 0.2176 0.5704 -0.0537 -0.0340 -0.0192 73  GLU A CA  
591   C C   . GLU A 73  ? 0.3783 0.2294 0.5886 -0.0538 -0.0284 -0.0147 73  GLU A C   
592   O O   . GLU A 73  ? 0.3924 0.2405 0.5971 -0.0494 -0.0228 -0.0148 73  GLU A O   
593   C CB  . GLU A 73  ? 0.3861 0.2195 0.5803 -0.0574 -0.0418 -0.0235 73  GLU A CB  
594   C CG  . GLU A 73  ? 0.3912 0.2105 0.5736 -0.0543 -0.0392 -0.0271 73  GLU A CG  
595   C CD  . GLU A 73  ? 0.4134 0.2165 0.5836 -0.0561 -0.0459 -0.0331 73  GLU A CD  
596   O OE1 . GLU A 73  ? 0.4090 0.2098 0.5787 -0.0604 -0.0539 -0.0347 73  GLU A OE1 
597   O OE2 . GLU A 73  ? 0.4570 0.2490 0.6177 -0.0526 -0.0431 -0.0365 73  GLU A OE2 
598   N N   . ASN A 74  ? 0.3925 0.2499 0.6176 -0.0589 -0.0300 -0.0105 74  ASN A N   
599   C CA  . ASN A 74  ? 0.4013 0.2625 0.6354 -0.0598 -0.0247 -0.0053 74  ASN A CA  
600   C C   . ASN A 74  ? 0.3581 0.2281 0.5903 -0.0540 -0.0166 -0.0031 74  ASN A C   
601   O O   . ASN A 74  ? 0.3506 0.2171 0.5801 -0.0515 -0.0121 -0.0014 74  ASN A O   
602   C CB  . ASN A 74  ? 0.4099 0.2804 0.6611 -0.0660 -0.0264 -0.0009 74  ASN A CB  
603   C CG  . ASN A 74  ? 0.4470 0.3082 0.7031 -0.0726 -0.0328 -0.0012 74  ASN A CG  
604   O OD1 . ASN A 74  ? 0.4538 0.2997 0.7003 -0.0726 -0.0351 -0.0041 74  ASN A OD1 
605   N ND2 . ASN A 74  ? 0.4268 0.2971 0.6985 -0.0784 -0.0358 0.0016  74  ASN A ND2 
606   N N   . GLN A 75  ? 0.3634 0.2447 0.5978 -0.0521 -0.0153 -0.0027 75  GLN A N   
607   C CA  . GLN A 75  ? 0.3740 0.2632 0.6066 -0.0470 -0.0084 -0.0009 75  GLN A CA  
608   C C   . GLN A 75  ? 0.3891 0.2702 0.6079 -0.0417 -0.0062 -0.0044 75  GLN A C   
609   O O   . GLN A 75  ? 0.4050 0.2872 0.6223 -0.0381 -0.0010 -0.0026 75  GLN A O   
610   C CB  . GLN A 75  ? 0.3585 0.2601 0.5954 -0.0459 -0.0083 -0.0004 75  GLN A CB  
611   C CG  . GLN A 75  ? 0.3614 0.2741 0.6139 -0.0498 -0.0083 0.0035  75  GLN A CG  
612   C CD  . GLN A 75  ? 0.3681 0.2914 0.6253 -0.0486 -0.0097 0.0031  75  GLN A CD  
613   O OE1 . GLN A 75  ? 0.3570 0.2773 0.6086 -0.0482 -0.0149 -0.0001 75  GLN A OE1 
614   N NE2 . GLN A 75  ? 0.3683 0.3033 0.6350 -0.0478 -0.0049 0.0065  75  GLN A NE2 
615   N N   . LEU A 76  ? 0.4129 0.2865 0.6219 -0.0410 -0.0100 -0.0094 76  LEU A N   
616   C CA  . LEU A 76  ? 0.4302 0.2970 0.6267 -0.0359 -0.0073 -0.0131 76  LEU A CA  
617   C C   . LEU A 76  ? 0.4022 0.2600 0.5974 -0.0345 -0.0052 -0.0130 76  LEU A C   
618   O O   . LEU A 76  ? 0.3951 0.2535 0.5869 -0.0296 -0.0004 -0.0130 76  LEU A O   
619   C CB  . LEU A 76  ? 0.4441 0.3023 0.6292 -0.0362 -0.0117 -0.0186 76  LEU A CB  
620   C CG  . LEU A 76  ? 0.4601 0.3225 0.6370 -0.0331 -0.0100 -0.0207 76  LEU A CG  
621   C CD1 . LEU A 76  ? 0.4669 0.3164 0.6300 -0.0332 -0.0135 -0.0264 76  LEU A CD1 
622   C CD2 . LEU A 76  ? 0.4556 0.3241 0.6306 -0.0278 -0.0028 -0.0199 76  LEU A CD2 
623   N N   . LYS A 77  ? 0.3820 0.2316 0.5803 -0.0388 -0.0094 -0.0127 77  LYS A N   
624   C CA  . LYS A 77  ? 0.4145 0.2524 0.6100 -0.0377 -0.0089 -0.0133 77  LYS A CA  
625   C C   . LYS A 77  ? 0.3917 0.2351 0.5927 -0.0353 -0.0034 -0.0081 77  LYS A C   
626   O O   . LYS A 77  ? 0.3816 0.2186 0.5779 -0.0308 -0.0009 -0.0089 77  LYS A O   
627   C CB  . LYS A 77  ? 0.4708 0.2993 0.6700 -0.0439 -0.0151 -0.0133 77  LYS A CB  
628   C CG  . LYS A 77  ? 0.4950 0.3082 0.6907 -0.0437 -0.0163 -0.0144 77  LYS A CG  
629   C CD  . LYS A 77  ? 0.5587 0.3611 0.7547 -0.0498 -0.0239 -0.0168 77  LYS A CD  
630   C CE  . LYS A 77  ? 0.6040 0.3913 0.7995 -0.0516 -0.0263 -0.0166 77  LYS A CE  
631   N NZ  . LYS A 77  ? 0.6100 0.3900 0.7965 -0.0442 -0.0223 -0.0194 77  LYS A NZ  
632   N N   . LEU A 78  ? 0.3630 0.2181 0.5737 -0.0381 -0.0018 -0.0030 78  LEU A N   
633   C CA  . LEU A 78  ? 0.3787 0.2398 0.5936 -0.0363 0.0033  0.0022  78  LEU A CA  
634   C C   . LEU A 78  ? 0.3725 0.2382 0.5817 -0.0296 0.0076  0.0009  78  LEU A C   
635   O O   . LEU A 78  ? 0.3799 0.2435 0.5876 -0.0262 0.0104  0.0028  78  LEU A O   
636   C CB  . LEU A 78  ? 0.3893 0.2626 0.6147 -0.0404 0.0046  0.0069  78  LEU A CB  
637   C CG  . LEU A 78  ? 0.4225 0.3010 0.6519 -0.0399 0.0097  0.0128  78  LEU A CG  
638   C CD1 . LEU A 78  ? 0.4372 0.3047 0.6674 -0.0430 0.0087  0.0158  78  LEU A CD1 
639   C CD2 . LEU A 78  ? 0.4444 0.3366 0.6833 -0.0430 0.0119  0.0162  78  LEU A CD2 
640   N N   . VAL A 79  ? 0.3811 0.2531 0.5872 -0.0279 0.0077  -0.0022 79  VAL A N   
641   C CA  . VAL A 79  ? 0.3574 0.2342 0.5588 -0.0222 0.0116  -0.0036 79  VAL A CA  
642   C C   . VAL A 79  ? 0.3565 0.2229 0.5504 -0.0181 0.0120  -0.0075 79  VAL A C   
643   O O   . VAL A 79  ? 0.3386 0.2063 0.5315 -0.0133 0.0153  -0.0070 79  VAL A O   
644   C CB  . VAL A 79  ? 0.3515 0.2359 0.5507 -0.0218 0.0114  -0.0058 79  VAL A CB  
645   C CG1 . VAL A 79  ? 0.3420 0.2311 0.5368 -0.0165 0.0155  -0.0071 79  VAL A CG1 
646   C CG2 . VAL A 79  ? 0.3554 0.2501 0.5628 -0.0252 0.0108  -0.0024 79  VAL A CG2 
647   N N   . GLN A 80  ? 0.3621 0.2183 0.5510 -0.0198 0.0083  -0.0117 80  GLN A N   
648   C CA  . GLN A 80  ? 0.3994 0.2451 0.5808 -0.0156 0.0088  -0.0164 80  GLN A CA  
649   C C   . GLN A 80  ? 0.4037 0.2446 0.5886 -0.0133 0.0101  -0.0133 80  GLN A C   
650   O O   . GLN A 80  ? 0.3983 0.2394 0.5815 -0.0077 0.0132  -0.0144 80  GLN A O   
651   C CB  . GLN A 80  ? 0.4213 0.2553 0.5960 -0.0184 0.0041  -0.0213 80  GLN A CB  
652   C CG  . GLN A 80  ? 0.4055 0.2272 0.5714 -0.0139 0.0047  -0.0271 80  GLN A CG  
653   C CD  . GLN A 80  ? 0.4151 0.2411 0.5736 -0.0092 0.0089  -0.0314 80  GLN A CD  
654   O OE1 . GLN A 80  ? 0.4190 0.2533 0.5759 -0.0107 0.0093  -0.0311 80  GLN A OE1 
655   N NE2 . GLN A 80  ? 0.4193 0.2405 0.5742 -0.0034 0.0123  -0.0349 80  GLN A NE2 
656   N N   . GLU A 81  ? 0.4092 0.2471 0.5997 -0.0178 0.0078  -0.0089 81  GLU A N   
657   C CA  . GLU A 81  ? 0.4217 0.2516 0.6139 -0.0165 0.0079  -0.0059 81  GLU A CA  
658   C C   . GLU A 81  ? 0.4075 0.2467 0.6033 -0.0136 0.0118  -0.0009 81  GLU A C   
659   O O   . GLU A 81  ? 0.4137 0.2471 0.6094 -0.0106 0.0122  0.0012  81  GLU A O   
660   C CB  . GLU A 81  ? 0.4582 0.2801 0.6541 -0.0232 0.0039  -0.0033 81  GLU A CB  
661   C CG  . GLU A 81  ? 0.5231 0.3337 0.7139 -0.0253 -0.0008 -0.0091 81  GLU A CG  
662   C CD  . GLU A 81  ? 0.6098 0.4105 0.8041 -0.0323 -0.0059 -0.0075 81  GLU A CD  
663   O OE1 . GLU A 81  ? 0.5736 0.3765 0.7757 -0.0369 -0.0058 -0.0012 81  GLU A OE1 
664   O OE2 . GLU A 81  ? 0.5937 0.3835 0.7820 -0.0331 -0.0102 -0.0132 81  GLU A OE2 
665   N N   . SER A 82  ? 0.3513 0.2042 0.5495 -0.0138 0.0143  0.0004  82  SER A N   
666   C CA  . SER A 82  ? 0.3186 0.1803 0.5192 -0.0112 0.0177  0.0046  82  SER A CA  
667   C C   . SER A 82  ? 0.3332 0.1952 0.5306 -0.0042 0.0196  0.0018  82  SER A C   
668   O O   . SER A 82  ? 0.3331 0.1981 0.5319 -0.0013 0.0210  0.0052  82  SER A O   
669   C CB  . SER A 82  ? 0.3114 0.1862 0.5150 -0.0133 0.0193  0.0060  82  SER A CB  
670   O OG  . SER A 82  ? 0.2914 0.1716 0.4919 -0.0102 0.0204  0.0017  82  SER A OG  
671   N N   . GLY A 83  ? 0.3257 0.1854 0.5191 -0.0016 0.0197  -0.0042 83  GLY A N   
672   C CA  . GLY A 83  ? 0.3380 0.2005 0.5299 0.0047  0.0223  -0.0072 83  GLY A CA  
673   C C   . GLY A 83  ? 0.3591 0.2343 0.5511 0.0052  0.0249  -0.0081 83  GLY A C   
674   O O   . GLY A 83  ? 0.3551 0.2333 0.5456 0.0093  0.0273  -0.0116 83  GLY A O   
675   N N   . LEU A 84  ? 0.3486 0.2313 0.5428 0.0009  0.0246  -0.0051 84  LEU A N   
676   C CA  . LEU A 84  ? 0.3050 0.1985 0.4991 0.0012  0.0266  -0.0058 84  LEU A CA  
677   C C   . LEU A 84  ? 0.3043 0.1957 0.4929 0.0004  0.0263  -0.0108 84  LEU A C   
678   O O   . LEU A 84  ? 0.2929 0.1759 0.4785 -0.0022 0.0237  -0.0127 84  LEU A O   
679   C CB  . LEU A 84  ? 0.2895 0.1905 0.4873 -0.0026 0.0262  -0.0017 84  LEU A CB  
680   C CG  . LEU A 84  ? 0.2926 0.1970 0.4941 -0.0018 0.0272  0.0034  84  LEU A CG  
681   C CD1 . LEU A 84  ? 0.2935 0.2026 0.4985 -0.0063 0.0269  0.0067  84  LEU A CD1 
682   C CD2 . LEU A 84  ? 0.2908 0.2025 0.4926 0.0023  0.0293  0.0036  84  LEU A CD2 
683   N N   . LYS A 85  ? 0.2828 0.1814 0.4697 0.0021  0.0288  -0.0125 85  LYS A N   
684   C CA  . LYS A 85  ? 0.2789 0.1764 0.4593 0.0007  0.0288  -0.0163 85  LYS A CA  
685   C C   . LYS A 85  ? 0.2954 0.1984 0.4770 -0.0035 0.0266  -0.0141 85  LYS A C   
686   O O   . LYS A 85  ? 0.2792 0.1885 0.4669 -0.0045 0.0264  -0.0101 85  LYS A O   
687   C CB  . LYS A 85  ? 0.2803 0.1827 0.4586 0.0043  0.0329  -0.0188 85  LYS A CB  
688   C CG  . LYS A 85  ? 0.2916 0.1913 0.4716 0.0095  0.0355  -0.0209 85  LYS A CG  
689   C CD  . LYS A 85  ? 0.3014 0.1888 0.4765 0.0105  0.0345  -0.0248 85  LYS A CD  
690   C CE  . LYS A 85  ? 0.3202 0.2048 0.4990 0.0161  0.0364  -0.0261 85  LYS A CE  
691   N NZ  . LYS A 85  ? 0.3426 0.2146 0.5158 0.0174  0.0356  -0.0307 85  LYS A NZ  
692   N N   . LEU A 86  ? 0.3044 0.2044 0.4796 -0.0058 0.0248  -0.0168 86  LEU A N   
693   C CA  . LEU A 86  ? 0.3072 0.2111 0.4839 -0.0097 0.0217  -0.0150 86  LEU A CA  
694   C C   . LEU A 86  ? 0.3152 0.2209 0.4848 -0.0098 0.0223  -0.0170 86  LEU A C   
695   O O   . LEU A 86  ? 0.3446 0.2442 0.5055 -0.0092 0.0230  -0.0207 86  LEU A O   
696   C CB  . LEU A 86  ? 0.2916 0.1887 0.4687 -0.0136 0.0168  -0.0152 86  LEU A CB  
697   C CG  . LEU A 86  ? 0.2991 0.1991 0.4775 -0.0174 0.0125  -0.0143 86  LEU A CG  
698   C CD1 . LEU A 86  ? 0.2879 0.1987 0.4753 -0.0176 0.0136  -0.0101 86  LEU A CD1 
699   C CD2 . LEU A 86  ? 0.3007 0.1943 0.4807 -0.0215 0.0072  -0.0148 86  LEU A CD2 
700   N N   . ILE A 87  ? 0.3168 0.2307 0.4898 -0.0106 0.0221  -0.0144 87  ILE A N   
701   C CA  . ILE A 87  ? 0.3035 0.2180 0.4700 -0.0120 0.0211  -0.0153 87  ILE A CA  
702   C C   . ILE A 87  ? 0.2972 0.2118 0.4665 -0.0155 0.0155  -0.0138 87  ILE A C   
703   O O   . ILE A 87  ? 0.2850 0.2064 0.4628 -0.0158 0.0150  -0.0108 87  ILE A O   
704   C CB  . ILE A 87  ? 0.2768 0.1995 0.4452 -0.0103 0.0245  -0.0137 87  ILE A CB  
705   C CG1 . ILE A 87  ? 0.2789 0.2025 0.4463 -0.0069 0.0297  -0.0153 87  ILE A CG1 
706   C CG2 . ILE A 87  ? 0.2980 0.2209 0.4604 -0.0123 0.0227  -0.0137 87  ILE A CG2 
707   C CD1 . ILE A 87  ? 0.2781 0.2105 0.4498 -0.0054 0.0325  -0.0134 87  ILE A CD1 
708   N N   . MET A 88  ? 0.3100 0.2168 0.4725 -0.0179 0.0114  -0.0161 88  MET A N   
709   C CA  . MET A 88  ? 0.3247 0.2310 0.4918 -0.0213 0.0053  -0.0150 88  MET A CA  
710   C C   . MET A 88  ? 0.3155 0.2228 0.4783 -0.0228 0.0016  -0.0146 88  MET A C   
711   O O   . MET A 88  ? 0.3005 0.2011 0.4514 -0.0234 0.0003  -0.0169 88  MET A O   
712   C CB  . MET A 88  ? 0.3387 0.2351 0.5017 -0.0235 0.0014  -0.0177 88  MET A CB  
713   C CG  . MET A 88  ? 0.3372 0.2341 0.5073 -0.0273 -0.0054 -0.0163 88  MET A CG  
714   S SD  . MET A 88  ? 0.3561 0.2436 0.5274 -0.0303 -0.0094 -0.0181 88  MET A SD  
715   C CE  . MET A 88  ? 0.3737 0.2486 0.5263 -0.0305 -0.0122 -0.0233 88  MET A CE  
716   N N   . GLY A 89  ? 0.3085 0.2234 0.4809 -0.0233 -0.0004 -0.0117 89  GLY A N   
717   C CA  . GLY A 89  ? 0.3211 0.2367 0.4914 -0.0245 -0.0050 -0.0110 89  GLY A CA  
718   C C   . GLY A 89  ? 0.3376 0.2487 0.5090 -0.0277 -0.0127 -0.0117 89  GLY A C   
719   O O   . GLY A 89  ? 0.3077 0.2192 0.4872 -0.0291 -0.0141 -0.0115 89  GLY A O   
720   N N   . ILE A 90  ? 0.3436 0.2499 0.5062 -0.0289 -0.0176 -0.0123 90  ILE A N   
721   C CA  . ILE A 90  ? 0.3611 0.2631 0.5241 -0.0319 -0.0262 -0.0128 90  ILE A CA  
722   C C   . ILE A 90  ? 0.3591 0.2681 0.5312 -0.0316 -0.0304 -0.0102 90  ILE A C   
723   O O   . ILE A 90  ? 0.3487 0.2604 0.5182 -0.0297 -0.0281 -0.0088 90  ILE A O   
724   C CB  . ILE A 90  ? 0.4001 0.2897 0.5447 -0.0335 -0.0296 -0.0157 90  ILE A CB  
725   C CG1 . ILE A 90  ? 0.3953 0.2783 0.5309 -0.0328 -0.0242 -0.0188 90  ILE A CG1 
726   C CG2 . ILE A 90  ? 0.3970 0.2811 0.5411 -0.0367 -0.0398 -0.0164 90  ILE A CG2 
727   C CD1 . ILE A 90  ? 0.3939 0.2751 0.5370 -0.0341 -0.0256 -0.0201 90  ILE A CD1 
728   N N   . ASP A 91  ? 0.3586 0.2711 0.5429 -0.0334 -0.0361 -0.0095 91  ASP A N   
729   C CA  . ASP A 91  ? 0.3812 0.3014 0.5773 -0.0327 -0.0402 -0.0073 91  ASP A CA  
730   C C   . ASP A 91  ? 0.3905 0.3036 0.5773 -0.0338 -0.0488 -0.0076 91  ASP A C   
731   O O   . ASP A 91  ? 0.4203 0.3305 0.6098 -0.0362 -0.0570 -0.0082 91  ASP A O   
732   C CB  . ASP A 91  ? 0.3726 0.3006 0.5871 -0.0341 -0.0423 -0.0064 91  ASP A CB  
733   C CG  . ASP A 91  ? 0.4009 0.3389 0.6309 -0.0328 -0.0453 -0.0045 91  ASP A CG  
734   O OD1 . ASP A 91  ? 0.3519 0.2907 0.5791 -0.0304 -0.0464 -0.0038 91  ASP A OD1 
735   O OD2 . ASP A 91  ? 0.4801 0.4254 0.7258 -0.0342 -0.0463 -0.0038 91  ASP A OD2 
736   N N   . ILE A 92  ? 0.3826 0.2919 0.5574 -0.0323 -0.0472 -0.0070 92  ILE A N   
737   C CA  . ILE A 92  ? 0.4098 0.3115 0.5740 -0.0333 -0.0549 -0.0066 92  ILE A CA  
738   C C   . ILE A 92  ? 0.4179 0.3266 0.5915 -0.0307 -0.0560 -0.0040 92  ILE A C   
739   O O   . ILE A 92  ? 0.3977 0.3081 0.5677 -0.0288 -0.0500 -0.0031 92  ILE A O   
740   C CB  . ILE A 92  ? 0.4130 0.3039 0.5552 -0.0341 -0.0521 -0.0078 92  ILE A CB  
741   C CG1 . ILE A 92  ? 0.3971 0.2812 0.5305 -0.0359 -0.0500 -0.0110 92  ILE A CG1 
742   C CG2 . ILE A 92  ? 0.4372 0.3190 0.5661 -0.0355 -0.0599 -0.0067 92  ILE A CG2 
743   C CD1 . ILE A 92  ? 0.4231 0.3002 0.5543 -0.0389 -0.0594 -0.0126 92  ILE A CD1 
744   N N   . LYS A 93  ? 0.4224 0.3358 0.6096 -0.0305 -0.0634 -0.0032 93  LYS A N   
745   C CA  . LYS A 93  ? 0.4673 0.3884 0.6666 -0.0274 -0.0645 -0.0013 93  LYS A CA  
746   C C   . LYS A 93  ? 0.4297 0.3441 0.6153 -0.0262 -0.0648 0.0001  93  LYS A C   
747   O O   . LYS A 93  ? 0.3991 0.3035 0.5717 -0.0279 -0.0717 0.0007  93  LYS A O   
748   C CB  . LYS A 93  ? 0.5429 0.4671 0.7551 -0.0274 -0.0747 -0.0008 93  LYS A CB  
749   C CG  . LYS A 93  ? 0.6345 0.5682 0.8658 -0.0284 -0.0754 -0.0015 93  LYS A CG  
750   C CD  . LYS A 93  ? 0.7475 0.6941 0.9948 -0.0260 -0.0664 -0.0011 93  LYS A CD  
751   C CE  . LYS A 93  ? 0.7705 0.7258 1.0351 -0.0279 -0.0657 -0.0014 93  LYS A CE  
752   N NZ  . LYS A 93  ? 0.7352 0.7011 1.0109 -0.0260 -0.0557 -0.0009 93  LYS A NZ  
753   N N   . PRO A 94  ? 0.4312 0.3503 0.6191 -0.0236 -0.0578 0.0010  94  PRO A N   
754   C CA  . PRO A 94  ? 0.4672 0.3798 0.6427 -0.0231 -0.0579 0.0026  94  PRO A CA  
755   C C   . PRO A 94  ? 0.4489 0.3581 0.6257 -0.0219 -0.0668 0.0044  94  PRO A C   
756   O O   . PRO A 94  ? 0.4816 0.3823 0.6449 -0.0226 -0.0685 0.0061  94  PRO A O   
757   C CB  . PRO A 94  ? 0.4764 0.3963 0.6573 -0.0207 -0.0485 0.0026  94  PRO A CB  
758   C CG  . PRO A 94  ? 0.4873 0.4186 0.6863 -0.0189 -0.0455 0.0016  94  PRO A CG  
759   C CD  . PRO A 94  ? 0.4361 0.3663 0.6378 -0.0214 -0.0500 0.0005  94  PRO A CD  
760   N N   . GLU A 95  ? 0.4590 0.3750 0.6526 -0.0199 -0.0721 0.0043  95  GLU A N   
761   C CA  . GLU A 95  ? 0.4854 0.3998 0.6837 -0.0175 -0.0804 0.0059  95  GLU A CA  
762   C C   . GLU A 95  ? 0.4572 0.3635 0.6498 -0.0198 -0.0919 0.0065  95  GLU A C   
763   O O   . GLU A 95  ? 0.4167 0.3184 0.6091 -0.0184 -0.1006 0.0081  95  GLU A O   
764   C CB  . GLU A 95  ? 0.5134 0.4406 0.7335 -0.0132 -0.0780 0.0051  95  GLU A CB  
765   C CG  . GLU A 95  ? 0.6551 0.5929 0.8926 -0.0134 -0.0777 0.0036  95  GLU A CG  
766   C CD  . GLU A 95  ? 0.7156 0.6568 0.9516 -0.0159 -0.0693 0.0023  95  GLU A CD  
767   O OE1 . GLU A 95  ? 0.6894 0.6330 0.9224 -0.0149 -0.0602 0.0021  95  GLU A OE1 
768   O OE2 . GLU A 95  ? 0.8094 0.7502 1.0472 -0.0189 -0.0723 0.0015  95  GLU A OE2 
769   N N   . GLU A 96  ? 0.4716 0.3746 0.6575 -0.0234 -0.0926 0.0051  96  GLU A N   
770   C CA  . GLU A 96  ? 0.4573 0.3511 0.6349 -0.0260 -0.1037 0.0053  96  GLU A CA  
771   C C   . GLU A 96  ? 0.4383 0.3170 0.5909 -0.0281 -0.1066 0.0072  96  GLU A C   
772   O O   . GLU A 96  ? 0.4262 0.3016 0.5668 -0.0285 -0.0984 0.0078  96  GLU A O   
773   C CB  . GLU A 96  ? 0.4926 0.3864 0.6693 -0.0293 -0.1030 0.0029  96  GLU A CB  
774   C CG  . GLU A 96  ? 0.5584 0.4657 0.7596 -0.0285 -0.1027 0.0016  96  GLU A CG  
775   C CD  . GLU A 96  ? 0.5954 0.5062 0.8114 -0.0275 -0.1144 0.0024  96  GLU A CD  
776   O OE1 . GLU A 96  ? 0.5797 0.4829 0.7892 -0.0304 -0.1242 0.0020  96  GLU A OE1 
777   O OE2 . GLU A 96  ? 0.6825 0.6033 0.9160 -0.0237 -0.1140 0.0031  96  GLU A OE2 
778   N N   . ASP A 97  ? 0.4158 0.2852 0.5606 -0.0296 -0.1185 0.0082  97  ASP A N   
779   C CA  . ASP A 97  ? 0.4340 0.2877 0.5536 -0.0322 -0.1226 0.0101  97  ASP A CA  
780   C C   . ASP A 97  ? 0.4461 0.2923 0.5471 -0.0362 -0.1181 0.0079  97  ASP A C   
781   O O   . ASP A 97  ? 0.4062 0.2477 0.5033 -0.0384 -0.1251 0.0061  97  ASP A O   
782   C CB  . ASP A 97  ? 0.4637 0.3102 0.5820 -0.0321 -0.1376 0.0121  97  ASP A CB  
783   C CG  . ASP A 97  ? 0.4865 0.3158 0.5783 -0.0345 -0.1430 0.0151  97  ASP A CG  
784   O OD1 . ASP A 97  ? 0.4510 0.2740 0.5244 -0.0368 -0.1343 0.0155  97  ASP A OD1 
785   O OD2 . ASP A 97  ? 0.5394 0.3619 0.6295 -0.0342 -0.1560 0.0172  97  ASP A OD2 
786   N N   . TYR A 98  ? 0.4712 0.3148 0.5592 -0.0370 -0.1073 0.0080  98  TYR A N   
787   C CA  . TYR A 98  ? 0.4862 0.3230 0.5562 -0.0400 -0.1011 0.0057  98  TYR A CA  
788   C C   . TYR A 98  ? 0.4975 0.3184 0.5444 -0.0434 -0.1098 0.0059  98  TYR A C   
789   O O   . TYR A 98  ? 0.5007 0.3153 0.5338 -0.0458 -0.1072 0.0030  98  TYR A O   
790   C CB  . TYR A 98  ? 0.5022 0.3399 0.5645 -0.0398 -0.0893 0.0067  98  TYR A CB  
791   C CG  . TYR A 98  ? 0.4790 0.3304 0.5607 -0.0366 -0.0813 0.0069  98  TYR A CG  
792   C CD1 . TYR A 98  ? 0.4615 0.3246 0.5634 -0.0345 -0.0794 0.0047  98  TYR A CD1 
793   C CD2 . TYR A 98  ? 0.4654 0.3174 0.5445 -0.0359 -0.0759 0.0093  98  TYR A CD2 
794   C CE1 . TYR A 98  ? 0.4385 0.3131 0.5558 -0.0316 -0.0721 0.0048  98  TYR A CE1 
795   C CE2 . TYR A 98  ? 0.4366 0.3000 0.5318 -0.0330 -0.0692 0.0091  98  TYR A CE2 
796   C CZ  . TYR A 98  ? 0.4268 0.3014 0.5405 -0.0307 -0.0672 0.0068  98  TYR A CZ  
797   O OH  . TYR A 98  ? 0.4258 0.3109 0.5536 -0.0279 -0.0605 0.0066  98  TYR A OH  
798   N N   . GLY A 99  ? 0.4952 0.3090 0.5371 -0.0435 -0.1202 0.0093  99  GLY A N   
799   C CA  . GLY A 99  ? 0.5030 0.3005 0.5212 -0.0466 -0.1293 0.0103  99  GLY A CA  
800   C C   . GLY A 99  ? 0.5092 0.3047 0.5337 -0.0472 -0.1429 0.0089  99  GLY A C   
801   O O   . GLY A 99  ? 0.5317 0.3133 0.5360 -0.0500 -0.1513 0.0090  99  GLY A O   
802   N N   . ASP A 100 ? 0.4828 0.2921 0.5346 -0.0447 -0.1447 0.0075  100 ASP A N   
803   C CA  . ASP A 100 ? 0.4922 0.3021 0.5543 -0.0453 -0.1574 0.0062  100 ASP A CA  
804   C C   . ASP A 100 ? 0.4801 0.2851 0.5327 -0.0487 -0.1563 0.0019  100 ASP A C   
805   O O   . ASP A 100 ? 0.4384 0.2518 0.5002 -0.0484 -0.1463 -0.0008 100 ASP A O   
806   C CB  . ASP A 100 ? 0.4729 0.3003 0.5679 -0.0418 -0.1579 0.0062  100 ASP A CB  
807   C CG  . ASP A 100 ? 0.4810 0.3125 0.5925 -0.0423 -0.1703 0.0051  100 ASP A CG  
808   O OD1 . ASP A 100 ? 0.4985 0.3213 0.5986 -0.0459 -0.1767 0.0029  100 ASP A OD1 
809   O OD2 . ASP A 100 ? 0.4833 0.3266 0.6192 -0.0390 -0.1739 0.0063  100 ASP A OD2 
810   N N   . PRO A 101 ? 0.4978 0.2888 0.5322 -0.0518 -0.1672 0.0010  101 PRO A N   
811   C CA  . PRO A 101 ? 0.5180 0.3018 0.5400 -0.0550 -0.1662 -0.0036 101 PRO A CA  
812   C C   . PRO A 101 ? 0.5033 0.2985 0.5486 -0.0553 -0.1658 -0.0069 101 PRO A C   
813   O O   . PRO A 101 ? 0.5111 0.3033 0.5497 -0.0570 -0.1601 -0.0108 101 PRO A O   
814   C CB  . PRO A 101 ? 0.5391 0.3058 0.5392 -0.0580 -0.1810 -0.0033 101 PRO A CB  
815   C CG  . PRO A 101 ? 0.5421 0.3056 0.5396 -0.0564 -0.1879 0.0020  101 PRO A CG  
816   C CD  . PRO A 101 ? 0.5141 0.2953 0.5403 -0.0523 -0.1821 0.0042  101 PRO A CD  
817   N N   . GLU A 102 ? 0.4825 0.2905 0.5552 -0.0534 -0.1718 -0.0052 102 GLU A N   
818   C CA  . GLU A 102 ? 0.4647 0.2854 0.5630 -0.0538 -0.1717 -0.0073 102 GLU A CA  
819   C C   . GLU A 102 ? 0.4487 0.2811 0.5583 -0.0517 -0.1558 -0.0079 102 GLU A C   
820   O O   . GLU A 102 ? 0.4562 0.2919 0.5718 -0.0532 -0.1505 -0.0107 102 GLU A O   
821   C CB  . GLU A 102 ? 0.4530 0.2848 0.5775 -0.0522 -0.1821 -0.0050 102 GLU A CB  
822   C CG  . GLU A 102 ? 0.4777 0.2998 0.5964 -0.0547 -0.1998 -0.0050 102 GLU A CG  
823   C CD  . GLU A 102 ? 0.4766 0.3095 0.6213 -0.0526 -0.2108 -0.0027 102 GLU A CD  
824   O OE1 . GLU A 102 ? 0.4838 0.3298 0.6470 -0.0486 -0.2042 -0.0008 102 GLU A OE1 
825   O OE2 . GLU A 102 ? 0.4971 0.3257 0.6443 -0.0545 -0.2258 -0.0029 102 GLU A OE2 
826   N N   . PHE A 103 ? 0.4388 0.2770 0.5517 -0.0483 -0.1489 -0.0050 103 PHE A N   
827   C CA  . PHE A 103 ? 0.4179 0.2660 0.5388 -0.0461 -0.1341 -0.0053 103 PHE A CA  
828   C C   . PHE A 103 ? 0.4319 0.2712 0.5321 -0.0478 -0.1251 -0.0080 103 PHE A C   
829   O O   . PHE A 103 ? 0.4573 0.3031 0.5659 -0.0475 -0.1164 -0.0098 103 PHE A O   
830   C CB  . PHE A 103 ? 0.3934 0.2466 0.5175 -0.0425 -0.1293 -0.0020 103 PHE A CB  
831   C CG  . PHE A 103 ? 0.3683 0.2311 0.4998 -0.0405 -0.1148 -0.0025 103 PHE A CG  
832   C CD1 . PHE A 103 ? 0.3506 0.2276 0.5060 -0.0390 -0.1107 -0.0030 103 PHE A CD1 
833   C CD2 . PHE A 103 ? 0.3785 0.2359 0.4927 -0.0404 -0.1054 -0.0024 103 PHE A CD2 
834   C CE1 . PHE A 103 ? 0.3320 0.2167 0.4925 -0.0374 -0.0982 -0.0034 103 PHE A CE1 
835   C CE2 . PHE A 103 ? 0.3563 0.2223 0.4776 -0.0386 -0.0931 -0.0030 103 PHE A CE2 
836   C CZ  . PHE A 103 ? 0.3364 0.2154 0.4800 -0.0371 -0.0899 -0.0035 103 PHE A CZ  
837   N N   . VAL A 104 ? 0.4518 0.2765 0.5255 -0.0494 -0.1270 -0.0081 104 VAL A N   
838   C CA  . VAL A 104 ? 0.4827 0.2990 0.5360 -0.0505 -0.1180 -0.0108 104 VAL A CA  
839   C C   . VAL A 104 ? 0.4920 0.3050 0.5457 -0.0528 -0.1197 -0.0152 104 VAL A C   
840   O O   . VAL A 104 ? 0.4689 0.2849 0.5248 -0.0522 -0.1101 -0.0177 104 VAL A O   
841   C CB  . VAL A 104 ? 0.5149 0.3160 0.5394 -0.0521 -0.1203 -0.0097 104 VAL A CB  
842   C CG1 . VAL A 104 ? 0.5313 0.3229 0.5334 -0.0534 -0.1115 -0.0132 104 VAL A CG1 
843   C CG2 . VAL A 104 ? 0.5147 0.3185 0.5384 -0.0502 -0.1170 -0.0052 104 VAL A CG2 
844   N N   . LYS A 105 ? 0.5111 0.3177 0.5636 -0.0553 -0.1328 -0.0161 105 LYS A N   
845   C CA  . LYS A 105 ? 0.5253 0.3271 0.5775 -0.0580 -0.1367 -0.0202 105 LYS A CA  
846   C C   . LYS A 105 ? 0.5097 0.3258 0.5886 -0.0573 -0.1314 -0.0207 105 LYS A C   
847   O O   . LYS A 105 ? 0.5172 0.3305 0.5937 -0.0583 -0.1263 -0.0240 105 LYS A O   
848   C CB  . LYS A 105 ? 0.5658 0.3589 0.6133 -0.0608 -0.1534 -0.0202 105 LYS A CB  
849   C CG  . LYS A 105 ? 0.5972 0.3853 0.6473 -0.0644 -0.1612 -0.0242 105 LYS A CG  
850   C CD  . LYS A 105 ? 0.6497 0.4242 0.6772 -0.0659 -0.1560 -0.0292 105 LYS A CD  
851   C CE  . LYS A 105 ? 0.7263 0.4845 0.7211 -0.0663 -0.1567 -0.0302 105 LYS A CE  
852   N NZ  . LYS A 105 ? 0.7776 0.5219 0.7530 -0.0683 -0.1557 -0.0360 105 LYS A NZ  
853   N N   . ASP A 106 ? 0.5086 0.3395 0.6121 -0.0555 -0.1320 -0.0174 106 ASP A N   
854   C CA  . ASP A 106 ? 0.4804 0.3245 0.6083 -0.0554 -0.1271 -0.0175 106 ASP A CA  
855   C C   . ASP A 106 ? 0.4710 0.3185 0.5964 -0.0531 -0.1122 -0.0182 106 ASP A C   
856   O O   . ASP A 106 ? 0.4614 0.3120 0.5949 -0.0539 -0.1071 -0.0198 106 ASP A O   
857   C CB  . ASP A 106 ? 0.4611 0.3202 0.6148 -0.0536 -0.1303 -0.0141 106 ASP A CB  
858   C CG  . ASP A 106 ? 0.4785 0.3383 0.6432 -0.0558 -0.1451 -0.0136 106 ASP A CG  
859   O OD1 . ASP A 106 ? 0.5113 0.3602 0.6657 -0.0594 -0.1540 -0.0160 106 ASP A OD1 
860   O OD2 . ASP A 106 ? 0.4962 0.3671 0.6794 -0.0537 -0.1480 -0.0110 106 ASP A OD2 
861   N N   . SER A 107 ? 0.4477 0.2939 0.5615 -0.0505 -0.1059 -0.0167 107 SER A N   
862   C CA  . SER A 107 ? 0.4551 0.3051 0.5667 -0.0482 -0.0925 -0.0170 107 SER A CA  
863   C C   . SER A 107 ? 0.4787 0.3173 0.5728 -0.0495 -0.0887 -0.0212 107 SER A C   
864   O O   . SER A 107 ? 0.4788 0.3208 0.5780 -0.0485 -0.0804 -0.0227 107 SER A O   
865   C CB  . SER A 107 ? 0.4603 0.3116 0.5647 -0.0456 -0.0877 -0.0144 107 SER A CB  
866   O OG  . SER A 107 ? 0.4478 0.3091 0.5690 -0.0439 -0.0912 -0.0110 107 SER A OG  
867   N N   . GLU A 108 ? 0.5081 0.3326 0.5812 -0.0516 -0.0952 -0.0233 108 GLU A N   
868   C CA  . GLU A 108 ? 0.5342 0.3465 0.5886 -0.0526 -0.0921 -0.0279 108 GLU A CA  
869   C C   . GLU A 108 ? 0.5226 0.3337 0.5867 -0.0546 -0.0954 -0.0309 108 GLU A C   
870   O O   . GLU A 108 ? 0.5131 0.3217 0.5743 -0.0537 -0.0880 -0.0338 108 GLU A O   
871   C CB  . GLU A 108 ? 0.5720 0.3684 0.6006 -0.0547 -0.0992 -0.0296 108 GLU A CB  
872   C CG  . GLU A 108 ? 0.5698 0.3637 0.5833 -0.0535 -0.0955 -0.0269 108 GLU A CG  
873   C CD  . GLU A 108 ? 0.5883 0.3661 0.5763 -0.0561 -0.1040 -0.0278 108 GLU A CD  
874   O OE1 . GLU A 108 ? 0.6003 0.3736 0.5898 -0.0584 -0.1170 -0.0277 108 GLU A OE1 
875   O OE2 . GLU A 108 ? 0.6340 0.4036 0.6002 -0.0560 -0.0980 -0.0287 108 GLU A OE2 
876   N N   . ILE A 109 ? 0.5162 0.3289 0.5923 -0.0574 -0.1069 -0.0300 109 ILE A N   
877   C CA  . ILE A 109 ? 0.5165 0.3284 0.6035 -0.0601 -0.1109 -0.0324 109 ILE A CA  
878   C C   . ILE A 109 ? 0.4899 0.3142 0.5962 -0.0583 -0.1007 -0.0309 109 ILE A C   
879   O O   . ILE A 109 ? 0.5313 0.3515 0.6373 -0.0589 -0.0970 -0.0336 109 ILE A O   
880   C CB  . ILE A 109 ? 0.5265 0.3404 0.6264 -0.0636 -0.1248 -0.0311 109 ILE A CB  
881   C CG1 . ILE A 109 ? 0.5592 0.3582 0.6378 -0.0658 -0.1364 -0.0331 109 ILE A CG1 
882   C CG2 . ILE A 109 ? 0.5291 0.3456 0.6458 -0.0668 -0.1277 -0.0325 109 ILE A CG2 
883   C CD1 . ILE A 109 ? 0.5625 0.3651 0.6542 -0.0682 -0.1508 -0.0308 109 ILE A CD1 
884   N N   . GLU A 110 ? 0.4661 0.3045 0.5879 -0.0559 -0.0962 -0.0267 110 GLU A N   
885   C CA  . GLU A 110 ? 0.4292 0.2793 0.5687 -0.0543 -0.0872 -0.0250 110 GLU A CA  
886   C C   . GLU A 110 ? 0.4247 0.2702 0.5516 -0.0516 -0.0762 -0.0271 110 GLU A C   
887   O O   . GLU A 110 ? 0.4143 0.2585 0.5452 -0.0520 -0.0723 -0.0286 110 GLU A O   
888   C CB  . GLU A 110 ? 0.3878 0.2533 0.5459 -0.0523 -0.0857 -0.0206 110 GLU A CB  
889   C CG  . GLU A 110 ? 0.3770 0.2545 0.5524 -0.0508 -0.0764 -0.0185 110 GLU A CG  
890   C CD  . GLU A 110 ? 0.3916 0.2704 0.5795 -0.0539 -0.0768 -0.0191 110 GLU A CD  
891   O OE1 . GLU A 110 ? 0.4014 0.2756 0.5923 -0.0579 -0.0861 -0.0204 110 GLU A OE1 
892   O OE2 . GLU A 110 ? 0.3738 0.2578 0.5686 -0.0526 -0.0681 -0.0180 110 GLU A OE2 
893   N N   . LEU A 111 ? 0.4336 0.2759 0.5451 -0.0491 -0.0715 -0.0272 111 LEU A N   
894   C CA  . LEU A 111 ? 0.4320 0.2715 0.5335 -0.0463 -0.0610 -0.0292 111 LEU A CA  
895   C C   . LEU A 111 ? 0.4306 0.2574 0.5208 -0.0476 -0.0617 -0.0342 111 LEU A C   
896   O O   . LEU A 111 ? 0.4112 0.2385 0.5040 -0.0457 -0.0543 -0.0356 111 LEU A O   
897   C CB  . LEU A 111 ? 0.4563 0.2931 0.5419 -0.0445 -0.0573 -0.0288 111 LEU A CB  
898   C CG  . LEU A 111 ? 0.4723 0.3086 0.5492 -0.0414 -0.0458 -0.0304 111 LEU A CG  
899   C CD1 . LEU A 111 ? 0.4572 0.3034 0.5503 -0.0389 -0.0382 -0.0293 111 LEU A CD1 
900   C CD2 . LEU A 111 ? 0.4748 0.3135 0.5433 -0.0401 -0.0420 -0.0280 111 LEU A CD2 
901   N N   . LYS A 112 ? 0.4517 0.2666 0.5293 -0.0506 -0.0709 -0.0369 112 LYS A N   
902   C CA  . LYS A 112 ? 0.4873 0.2887 0.5525 -0.0516 -0.0720 -0.0423 112 LYS A CA  
903   C C   . LYS A 112 ? 0.4856 0.2893 0.5678 -0.0534 -0.0737 -0.0425 112 LYS A C   
904   O O   . LYS A 112 ? 0.4694 0.2654 0.5467 -0.0527 -0.0700 -0.0460 112 LYS A O   
905   C CB  . LYS A 112 ? 0.5204 0.3076 0.5668 -0.0546 -0.0821 -0.0454 112 LYS A CB  
906   C CG  . LYS A 112 ? 0.5632 0.3416 0.5847 -0.0528 -0.0779 -0.0475 112 LYS A CG  
907   C CD  . LYS A 112 ? 0.6299 0.3937 0.6314 -0.0560 -0.0886 -0.0500 112 LYS A CD  
908   C CE  . LYS A 112 ? 0.6899 0.4484 0.6699 -0.0551 -0.0859 -0.0495 112 LYS A CE  
909   N NZ  . LYS A 112 ? 0.7290 0.4754 0.6932 -0.0586 -0.0985 -0.0503 112 LYS A NZ  
910   N N   . ARG A 113 ? 0.4846 0.2985 0.5868 -0.0559 -0.0791 -0.0386 113 ARG A N   
911   C CA  . ARG A 113 ? 0.4900 0.3072 0.6096 -0.0583 -0.0804 -0.0378 113 ARG A CA  
912   C C   . ARG A 113 ? 0.4661 0.2892 0.5926 -0.0549 -0.0689 -0.0367 113 ARG A C   
913   O O   . ARG A 113 ? 0.4554 0.2722 0.5826 -0.0555 -0.0672 -0.0387 113 ARG A O   
914   C CB  . ARG A 113 ? 0.4872 0.3171 0.6283 -0.0609 -0.0863 -0.0334 113 ARG A CB  
915   C CG  . ARG A 113 ? 0.4904 0.3227 0.6490 -0.0651 -0.0899 -0.0326 113 ARG A CG  
916   C CD  . ARG A 113 ? 0.4552 0.3028 0.6361 -0.0667 -0.0937 -0.0280 113 ARG A CD  
917   N NE  . ARG A 113 ? 0.4063 0.2677 0.5974 -0.0629 -0.0837 -0.0242 113 ARG A NE  
918   C CZ  . ARG A 113 ? 0.3976 0.2648 0.5980 -0.0619 -0.0751 -0.0223 113 ARG A CZ  
919   N NH1 . ARG A 113 ? 0.4223 0.2836 0.6254 -0.0647 -0.0749 -0.0233 113 ARG A NH1 
920   N NH2 . ARG A 113 ? 0.3720 0.2505 0.5789 -0.0582 -0.0669 -0.0192 113 ARG A NH2 
921   N N   . VAL A 114 ? 0.4228 0.2567 0.5531 -0.0514 -0.0615 -0.0335 114 VAL A N   
922   C CA  . VAL A 114 ? 0.4169 0.2571 0.5529 -0.0478 -0.0510 -0.0321 114 VAL A CA  
923   C C   . VAL A 114 ? 0.4193 0.2480 0.5391 -0.0452 -0.0459 -0.0367 114 VAL A C   
924   O O   . VAL A 114 ? 0.4172 0.2433 0.5413 -0.0445 -0.0425 -0.0375 114 VAL A O   
925   C CB  . VAL A 114 ? 0.4237 0.2763 0.5646 -0.0447 -0.0454 -0.0284 114 VAL A CB  
926   C CG1 . VAL A 114 ? 0.4239 0.2820 0.5691 -0.0409 -0.0352 -0.0272 114 VAL A CG1 
927   C CG2 . VAL A 114 ? 0.4115 0.2757 0.5695 -0.0465 -0.0498 -0.0242 114 VAL A CG2 
928   N N   . LEU A 115 ? 0.4217 0.2430 0.5228 -0.0438 -0.0454 -0.0398 115 LEU A N   
929   C CA  . LEU A 115 ? 0.4304 0.2430 0.5169 -0.0405 -0.0388 -0.0442 115 LEU A CA  
930   C C   . LEU A 115 ? 0.4729 0.2726 0.5553 -0.0418 -0.0423 -0.0486 115 LEU A C   
931   O O   . LEU A 115 ? 0.4684 0.2635 0.5473 -0.0386 -0.0361 -0.0514 115 LEU A O   
932   C CB  . LEU A 115 ? 0.4468 0.2532 0.5135 -0.0398 -0.0385 -0.0466 115 LEU A CB  
933   C CG  . LEU A 115 ? 0.4729 0.2902 0.5414 -0.0381 -0.0340 -0.0426 115 LEU A CG  
934   C CD1 . LEU A 115 ? 0.4948 0.3046 0.5425 -0.0384 -0.0344 -0.0445 115 LEU A CD1 
935   C CD2 . LEU A 115 ? 0.4694 0.2957 0.5457 -0.0339 -0.0235 -0.0413 115 LEU A CD2 
936   N N   . ASN A 116 ? 0.4700 0.2638 0.5536 -0.0466 -0.0525 -0.0493 116 ASN A N   
937   C CA  . ASN A 116 ? 0.5002 0.2795 0.5771 -0.0487 -0.0576 -0.0540 116 ASN A CA  
938   C C   . ASN A 116 ? 0.4863 0.2660 0.5754 -0.0478 -0.0535 -0.0534 116 ASN A C   
939   O O   . ASN A 116 ? 0.4702 0.2372 0.5509 -0.0469 -0.0533 -0.0581 116 ASN A O   
940   C CB  . ASN A 116 ? 0.5503 0.3253 0.6291 -0.0545 -0.0702 -0.0540 116 ASN A CB  
941   C CG  . ASN A 116 ? 0.6312 0.3887 0.6986 -0.0566 -0.0759 -0.0599 116 ASN A CG  
942   O OD1 . ASN A 116 ? 0.7534 0.4989 0.8008 -0.0539 -0.0730 -0.0654 116 ASN A OD1 
943   N ND2 . ASN A 116 ? 0.6442 0.4000 0.7245 -0.0613 -0.0831 -0.0591 116 ASN A ND2 
944   N N   . TYR A 117 ? 0.4654 0.2592 0.5733 -0.0476 -0.0499 -0.0477 117 TYR A N   
945   C CA  . TYR A 117 ? 0.4448 0.2397 0.5631 -0.0462 -0.0449 -0.0462 117 TYR A CA  
946   C C   . TYR A 117 ? 0.4344 0.2381 0.5540 -0.0404 -0.0343 -0.0444 117 TYR A C   
947   O O   . TYR A 117 ? 0.4220 0.2218 0.5418 -0.0372 -0.0293 -0.0455 117 TYR A O   
948   C CB  . TYR A 117 ? 0.4256 0.2287 0.5639 -0.0509 -0.0486 -0.0409 117 TYR A CB  
949   C CG  . TYR A 117 ? 0.3993 0.2195 0.5507 -0.0512 -0.0473 -0.0354 117 TYR A CG  
950   C CD1 . TYR A 117 ? 0.3765 0.2082 0.5357 -0.0477 -0.0389 -0.0315 117 TYR A CD1 
951   C CD2 . TYR A 117 ? 0.3772 0.2018 0.5343 -0.0553 -0.0550 -0.0340 117 TYR A CD2 
952   C CE1 . TYR A 117 ? 0.3515 0.1976 0.5220 -0.0479 -0.0377 -0.0270 117 TYR A CE1 
953   C CE2 . TYR A 117 ? 0.3508 0.1906 0.5209 -0.0553 -0.0539 -0.0293 117 TYR A CE2 
954   C CZ  . TYR A 117 ? 0.3406 0.1908 0.5170 -0.0516 -0.0451 -0.0259 117 TYR A CZ  
955   O OH  . TYR A 117 ? 0.3373 0.2013 0.5251 -0.0513 -0.0440 -0.0219 117 TYR A OH  
956   N N   . ALA A 118 ? 0.4105 0.2255 0.5314 -0.0390 -0.0314 -0.0416 118 ALA A N   
957   C CA  . ALA A 118 ? 0.4029 0.2272 0.5273 -0.0342 -0.0222 -0.0394 118 ALA A CA  
958   C C   . ALA A 118 ? 0.4310 0.2476 0.5421 -0.0295 -0.0163 -0.0443 118 ALA A C   
959   O O   . ALA A 118 ? 0.4726 0.2947 0.5880 -0.0254 -0.0092 -0.0431 118 ALA A O   
960   C CB  . ALA A 118 ? 0.3827 0.2189 0.5096 -0.0338 -0.0208 -0.0360 118 ALA A CB  
961   N N   . LYS A 119 ? 0.4624 0.2669 0.5573 -0.0298 -0.0189 -0.0497 119 LYS A N   
962   C CA  . LYS A 119 ? 0.4897 0.2873 0.5709 -0.0252 -0.0127 -0.0548 119 LYS A CA  
963   C C   . LYS A 119 ? 0.4893 0.2795 0.5734 -0.0223 -0.0102 -0.0575 119 LYS A C   
964   O O   . LYS A 119 ? 0.4857 0.2716 0.5617 -0.0175 -0.0041 -0.0617 119 LYS A O   
965   C CB  . LYS A 119 ? 0.5242 0.3091 0.5859 -0.0268 -0.0167 -0.0603 119 LYS A CB  
966   C CG  . LYS A 119 ? 0.5452 0.3154 0.6023 -0.0300 -0.0248 -0.0641 119 LYS A CG  
967   C CD  . LYS A 119 ? 0.5802 0.3373 0.6170 -0.0322 -0.0303 -0.0692 119 LYS A CD  
968   C CE  . LYS A 119 ? 0.6319 0.3751 0.6662 -0.0357 -0.0390 -0.0728 119 LYS A CE  
969   N NZ  . LYS A 119 ? 0.6729 0.4045 0.6891 -0.0388 -0.0466 -0.0767 119 LYS A NZ  
970   N N   . LYS A 120 ? 0.4804 0.2688 0.5757 -0.0252 -0.0150 -0.0550 120 LYS A N   
971   C CA  . LYS A 120 ? 0.4935 0.2743 0.5926 -0.0229 -0.0136 -0.0565 120 LYS A CA  
972   C C   . LYS A 120 ? 0.4794 0.2714 0.5914 -0.0192 -0.0070 -0.0518 120 LYS A C   
973   O O   . LYS A 120 ? 0.4496 0.2364 0.5640 -0.0157 -0.0044 -0.0529 120 LYS A O   
974   C CB  . LYS A 120 ? 0.5317 0.3060 0.6379 -0.0287 -0.0218 -0.0549 120 LYS A CB  
975   C CG  . LYS A 120 ? 0.5746 0.3364 0.6691 -0.0329 -0.0301 -0.0595 120 LYS A CG  
976   C CD  . LYS A 120 ? 0.5995 0.3526 0.7011 -0.0383 -0.0379 -0.0590 120 LYS A CD  
977   C CE  . LYS A 120 ? 0.6158 0.3820 0.7354 -0.0432 -0.0407 -0.0517 120 LYS A CE  
978   N NZ  . LYS A 120 ? 0.6296 0.3881 0.7567 -0.0492 -0.0483 -0.0509 120 LYS A NZ  
979   N N   . TYR A 121 ? 0.4384 0.2451 0.5580 -0.0197 -0.0046 -0.0468 121 TYR A N   
980   C CA  . TYR A 121 ? 0.4173 0.2345 0.5495 -0.0173 0.0000  -0.0417 121 TYR A CA  
981   C C   . TYR A 121 ? 0.4237 0.2494 0.5534 -0.0122 0.0073  -0.0423 121 TYR A C   
982   O O   . TYR A 121 ? 0.4052 0.2401 0.5344 -0.0131 0.0084  -0.0405 121 TYR A O   
983   C CB  . TYR A 121 ? 0.4035 0.2303 0.5474 -0.0222 -0.0035 -0.0357 121 TYR A CB  
984   C CG  . TYR A 121 ? 0.4000 0.2193 0.5487 -0.0275 -0.0102 -0.0349 121 TYR A CG  
985   C CD1 . TYR A 121 ? 0.4254 0.2413 0.5820 -0.0278 -0.0099 -0.0323 121 TYR A CD1 
986   C CD2 . TYR A 121 ? 0.4003 0.2150 0.5453 -0.0322 -0.0171 -0.0368 121 TYR A CD2 
987   C CE1 . TYR A 121 ? 0.4230 0.2314 0.5842 -0.0331 -0.0158 -0.0315 121 TYR A CE1 
988   C CE2 . TYR A 121 ? 0.4246 0.2324 0.5749 -0.0374 -0.0236 -0.0362 121 TYR A CE2 
989   C CZ  . TYR A 121 ? 0.4196 0.2247 0.5784 -0.0381 -0.0226 -0.0334 121 TYR A CZ  
990   O OH  . TYR A 121 ? 0.4392 0.2380 0.6042 -0.0437 -0.0285 -0.0322 121 TYR A OH  
991   N N   . ASP A 122 ? 0.4176 0.2403 0.5468 -0.0068 0.0121  -0.0446 122 ASP A N   
992   C CA  . ASP A 122 ? 0.4238 0.2539 0.5510 -0.0019 0.0191  -0.0459 122 ASP A CA  
993   C C   . ASP A 122 ? 0.3891 0.2333 0.5281 -0.0007 0.0221  -0.0402 122 ASP A C   
994   O O   . ASP A 122 ? 0.4205 0.2721 0.5598 0.0029  0.0275  -0.0407 122 ASP A O   
995   C CB  . ASP A 122 ? 0.4371 0.2591 0.5586 0.0037  0.0232  -0.0517 122 ASP A CB  
996   C CG  . ASP A 122 ? 0.4477 0.2666 0.5777 0.0076  0.0239  -0.0508 122 ASP A CG  
997   O OD1 . ASP A 122 ? 0.4506 0.2744 0.5910 0.0061  0.0220  -0.0450 122 ASP A OD1 
998   O OD2 . ASP A 122 ? 0.4982 0.3089 0.6239 0.0123  0.0263  -0.0559 122 ASP A OD2 
999   N N   . CYS A 123 ? 0.3572 0.2053 0.5056 -0.0037 0.0189  -0.0349 123 CYS A N   
1000  C CA  . CYS A 123 ? 0.3408 0.2018 0.4983 -0.0031 0.0213  -0.0298 123 CYS A CA  
1001  C C   . CYS A 123 ? 0.3464 0.2161 0.5016 -0.0049 0.0220  -0.0289 123 CYS A C   
1002  O O   . CYS A 123 ? 0.3610 0.2411 0.5215 -0.0034 0.0249  -0.0260 123 CYS A O   
1003  C CB  . CYS A 123 ? 0.3412 0.2039 0.5079 -0.0061 0.0183  -0.0245 123 CYS A CB  
1004  S SG  . CYS A 123 ? 0.3577 0.2207 0.5263 -0.0132 0.0124  -0.0226 123 CYS A SG  
1005  N N   . ILE A 124 ? 0.3433 0.2082 0.4903 -0.0082 0.0187  -0.0314 124 ILE A N   
1006  C CA  . ILE A 124 ? 0.3446 0.2160 0.4879 -0.0098 0.0189  -0.0306 124 ILE A CA  
1007  C C   . ILE A 124 ? 0.3341 0.2078 0.4709 -0.0063 0.0248  -0.0333 124 ILE A C   
1008  O O   . ILE A 124 ? 0.3361 0.2018 0.4632 -0.0049 0.0264  -0.0381 124 ILE A O   
1009  C CB  . ILE A 124 ? 0.3441 0.2091 0.4802 -0.0143 0.0128  -0.0321 124 ILE A CB  
1010  C CG1 . ILE A 124 ? 0.3314 0.1962 0.4767 -0.0182 0.0071  -0.0291 124 ILE A CG1 
1011  C CG2 . ILE A 124 ? 0.3380 0.2089 0.4697 -0.0156 0.0129  -0.0309 124 ILE A CG2 
1012  C CD1 . ILE A 124 ? 0.3418 0.1993 0.4815 -0.0225 0.0000  -0.0309 124 ILE A CD1 
1013  N N   . ILE A 125 ? 0.3481 0.2326 0.4897 -0.0053 0.0281  -0.0304 125 ILE A N   
1014  C CA  . ILE A 125 ? 0.3528 0.2412 0.4904 -0.0025 0.0341  -0.0324 125 ILE A CA  
1015  C C   . ILE A 125 ? 0.3431 0.2364 0.4761 -0.0051 0.0343  -0.0308 125 ILE A C   
1016  O O   . ILE A 125 ? 0.3746 0.2714 0.5040 -0.0038 0.0393  -0.0320 125 ILE A O   
1017  C CB  . ILE A 125 ? 0.3459 0.2421 0.4939 0.0017  0.0384  -0.0308 125 ILE A CB  
1018  C CG1 . ILE A 125 ? 0.3489 0.2544 0.5066 0.0006  0.0367  -0.0255 125 ILE A CG1 
1019  C CG2 . ILE A 125 ? 0.3518 0.2413 0.5025 0.0049  0.0385  -0.0328 125 ILE A CG2 
1020  C CD1 . ILE A 125 ? 0.3416 0.2562 0.5073 0.0041  0.0407  -0.0239 125 ILE A CD1 
1021  N N   . THR A 126 ? 0.3203 0.2144 0.4542 -0.0088 0.0289  -0.0280 126 THR A N   
1022  C CA  . THR A 126 ? 0.3194 0.2154 0.4472 -0.0114 0.0278  -0.0268 126 THR A CA  
1023  C C   . THR A 126 ? 0.3258 0.2191 0.4543 -0.0150 0.0203  -0.0251 126 THR A C   
1024  O O   . THR A 126 ? 0.2966 0.1917 0.4346 -0.0154 0.0175  -0.0233 126 THR A O   
1025  C CB  . THR A 126 ? 0.3048 0.2115 0.4394 -0.0103 0.0314  -0.0237 126 THR A CB  
1026  O OG1 . THR A 126 ? 0.3121 0.2207 0.4440 -0.0078 0.0380  -0.0258 126 THR A OG1 
1027  C CG2 . THR A 126 ? 0.3004 0.2089 0.4306 -0.0133 0.0291  -0.0215 126 THR A CG2 
1028  N N   . TYR A 127 ? 0.3328 0.2214 0.4509 -0.0177 0.0170  -0.0256 127 TYR A N   
1029  C CA  . TYR A 127 ? 0.3320 0.2200 0.4518 -0.0209 0.0097  -0.0235 127 TYR A CA  
1030  C C   . TYR A 127 ? 0.3318 0.2258 0.4521 -0.0216 0.0097  -0.0203 127 TYR A C   
1031  O O   . TYR A 127 ? 0.3224 0.2157 0.4341 -0.0214 0.0135  -0.0208 127 TYR A O   
1032  C CB  . TYR A 127 ? 0.3561 0.2326 0.4628 -0.0236 0.0043  -0.0264 127 TYR A CB  
1033  C CG  . TYR A 127 ? 0.3483 0.2172 0.4548 -0.0240 0.0016  -0.0293 127 TYR A CG  
1034  C CD1 . TYR A 127 ? 0.3520 0.2209 0.4674 -0.0265 -0.0051 -0.0280 127 TYR A CD1 
1035  C CD2 . TYR A 127 ? 0.3638 0.2255 0.4620 -0.0220 0.0058  -0.0337 127 TYR A CD2 
1036  C CE1 . TYR A 127 ? 0.3617 0.2231 0.4775 -0.0274 -0.0079 -0.0304 127 TYR A CE1 
1037  C CE2 . TYR A 127 ? 0.3559 0.2096 0.4542 -0.0223 0.0030  -0.0365 127 TYR A CE2 
1038  C CZ  . TYR A 127 ? 0.3557 0.2092 0.4629 -0.0253 -0.0040 -0.0346 127 TYR A CZ  
1039  O OH  . TYR A 127 ? 0.3762 0.2214 0.4841 -0.0264 -0.0072 -0.0370 127 TYR A OH  
1040  N N   . LEU A 128 ? 0.3524 0.2520 0.4829 -0.0224 0.0054  -0.0172 128 LEU A N   
1041  C CA  . LEU A 128 ? 0.3536 0.2574 0.4852 -0.0232 0.0035  -0.0144 128 LEU A CA  
1042  C C   . LEU A 128 ? 0.3672 0.2663 0.4964 -0.0258 -0.0050 -0.0139 128 LEU A C   
1043  O O   . LEU A 128 ? 0.3842 0.2852 0.5230 -0.0265 -0.0092 -0.0134 128 LEU A O   
1044  C CB  . LEU A 128 ? 0.3595 0.2735 0.5053 -0.0213 0.0053  -0.0116 128 LEU A CB  
1045  C CG  . LEU A 128 ? 0.3548 0.2740 0.5046 -0.0186 0.0124  -0.0118 128 LEU A CG  
1046  C CD1 . LEU A 128 ? 0.3467 0.2746 0.5090 -0.0171 0.0129  -0.0091 128 LEU A CD1 
1047  C CD2 . LEU A 128 ? 0.3515 0.2705 0.4934 -0.0181 0.0173  -0.0124 128 LEU A CD2 
1048  N N   . VAL A 129 ? 0.3723 0.2654 0.4889 -0.0275 -0.0074 -0.0138 129 VAL A N   
1049  C CA  . VAL A 129 ? 0.3810 0.2668 0.4912 -0.0301 -0.0159 -0.0139 129 VAL A CA  
1050  C C   . VAL A 129 ? 0.3869 0.2773 0.5054 -0.0303 -0.0217 -0.0107 129 VAL A C   
1051  O O   . VAL A 129 ? 0.3987 0.2851 0.5164 -0.0320 -0.0299 -0.0105 129 VAL A O   
1052  C CB  . VAL A 129 ? 0.4024 0.2773 0.4924 -0.0319 -0.0166 -0.0156 129 VAL A CB  
1053  C CG1 . VAL A 129 ? 0.4127 0.2808 0.4946 -0.0318 -0.0138 -0.0199 129 VAL A CG1 
1054  C CG2 . VAL A 129 ? 0.4007 0.2764 0.4828 -0.0318 -0.0114 -0.0139 129 VAL A CG2 
1055  N N   . ILE A 130 ? 0.3767 0.2751 0.5033 -0.0284 -0.0180 -0.0084 130 ILE A N   
1056  C CA  . ILE A 130 ? 0.3768 0.2798 0.5131 -0.0279 -0.0233 -0.0058 130 ILE A CA  
1057  C C   . ILE A 130 ? 0.3706 0.2831 0.5175 -0.0253 -0.0177 -0.0043 130 ILE A C   
1058  O O   . ILE A 130 ? 0.3675 0.2813 0.5107 -0.0245 -0.0110 -0.0046 130 ILE A O   
1059  C CB  . ILE A 130 ? 0.3660 0.2616 0.4912 -0.0295 -0.0293 -0.0043 130 ILE A CB  
1060  C CG1 . ILE A 130 ? 0.3777 0.2773 0.5140 -0.0286 -0.0360 -0.0022 130 ILE A CG1 
1061  C CG2 . ILE A 130 ? 0.3808 0.2743 0.4954 -0.0298 -0.0238 -0.0033 130 ILE A CG2 
1062  C CD1 . ILE A 130 ? 0.3994 0.2902 0.5253 -0.0302 -0.0443 -0.0007 130 ILE A CD1 
1063  N N   . ASN A 131 ? 0.3695 0.2885 0.5296 -0.0239 -0.0207 -0.0029 131 ASN A N   
1064  C CA  . ASN A 131 ? 0.3806 0.3080 0.5506 -0.0213 -0.0164 -0.0018 131 ASN A CA  
1065  C C   . ASN A 131 ? 0.3844 0.3116 0.5552 -0.0205 -0.0205 0.0000  131 ASN A C   
1066  O O   . ASN A 131 ? 0.3753 0.3039 0.5536 -0.0199 -0.0264 0.0005  131 ASN A O   
1067  C CB  . ASN A 131 ? 0.3683 0.3035 0.5527 -0.0201 -0.0151 -0.0020 131 ASN A CB  
1068  C CG  . ASN A 131 ? 0.4046 0.3477 0.5972 -0.0173 -0.0100 -0.0012 131 ASN A CG  
1069  O OD1 . ASN A 131 ? 0.4612 0.4049 0.6495 -0.0165 -0.0047 -0.0012 131 ASN A OD1 
1070  N ND2 . ASN A 131 ? 0.3995 0.3492 0.6043 -0.0158 -0.0114 -0.0005 131 ASN A ND2 
1071  N N   . GLU A 132 ? 0.3867 0.3119 0.5502 -0.0205 -0.0175 0.0009  132 GLU A N   
1072  C CA  . GLU A 132 ? 0.3959 0.3230 0.5634 -0.0189 -0.0189 0.0024  132 GLU A CA  
1073  C C   . GLU A 132 ? 0.3851 0.3058 0.5487 -0.0196 -0.0272 0.0038  132 GLU A C   
1074  O O   . GLU A 132 ? 0.4140 0.3379 0.5877 -0.0175 -0.0315 0.0042  132 GLU A O   
1075  C CB  . GLU A 132 ? 0.4068 0.3434 0.5896 -0.0158 -0.0171 0.0019  132 GLU A CB  
1076  C CG  . GLU A 132 ? 0.3965 0.3365 0.5830 -0.0135 -0.0147 0.0024  132 GLU A CG  
1077  C CD  . GLU A 132 ? 0.4492 0.3890 0.6290 -0.0144 -0.0086 0.0024  132 GLU A CD  
1078  O OE1 . GLU A 132 ? 0.4852 0.4185 0.6544 -0.0167 -0.0095 0.0035  132 GLU A OE1 
1079  O OE2 . GLU A 132 ? 0.3825 0.3281 0.5672 -0.0131 -0.0033 0.0016  132 GLU A OE2 
1080  N N   . PRO A 133 ? 0.3914 0.3026 0.5403 -0.0225 -0.0297 0.0047  133 PRO A N   
1081  C CA  . PRO A 133 ? 0.4275 0.3312 0.5708 -0.0234 -0.0380 0.0066  133 PRO A CA  
1082  C C   . PRO A 133 ? 0.4421 0.3449 0.5855 -0.0223 -0.0379 0.0086  133 PRO A C   
1083  O O   . PRO A 133 ? 0.4018 0.3046 0.5401 -0.0234 -0.0320 0.0091  133 PRO A O   
1084  C CB  . PRO A 133 ? 0.4053 0.2990 0.5304 -0.0271 -0.0388 0.0068  133 PRO A CB  
1085  C CG  . PRO A 133 ? 0.3908 0.2871 0.5114 -0.0279 -0.0290 0.0058  133 PRO A CG  
1086  C CD  . PRO A 133 ? 0.3992 0.3062 0.5354 -0.0250 -0.0247 0.0039  133 PRO A CD  
1087  N N   . GLN A 134 ? 0.4418 0.3443 0.5926 -0.0202 -0.0449 0.0095  134 GLN A N   
1088  C CA  . GLN A 134 ? 0.4386 0.3398 0.5916 -0.0185 -0.0461 0.0110  134 GLN A CA  
1089  C C   . GLN A 134 ? 0.4500 0.3389 0.5868 -0.0218 -0.0500 0.0140  134 GLN A C   
1090  O O   . GLN A 134 ? 0.4941 0.3755 0.6218 -0.0237 -0.0560 0.0151  134 GLN A O   
1091  C CB  . GLN A 134 ? 0.4427 0.3480 0.6103 -0.0144 -0.0521 0.0104  134 GLN A CB  
1092  C CG  . GLN A 134 ? 0.4451 0.3627 0.6289 -0.0109 -0.0469 0.0078  134 GLN A CG  
1093  C CD  . GLN A 134 ? 0.4813 0.4020 0.6662 -0.0096 -0.0403 0.0074  134 GLN A CD  
1094  O OE1 . GLN A 134 ? 0.5362 0.4511 0.7153 -0.0099 -0.0414 0.0087  134 GLN A OE1 
1095  N NE2 . GLN A 134 ? 0.5014 0.4303 0.6921 -0.0089 -0.0334 0.0056  134 GLN A NE2 
1096  N N   . THR A 135 ? 0.4399 0.3266 0.5732 -0.0224 -0.0472 0.0155  135 THR A N   
1097  C CA  . THR A 135 ? 0.4146 0.2896 0.5330 -0.0259 -0.0502 0.0190  135 THR A CA  
1098  C C   . THR A 135 ? 0.4206 0.2868 0.5359 -0.0253 -0.0612 0.0210  135 THR A C   
1099  O O   . THR A 135 ? 0.4508 0.3073 0.5511 -0.0287 -0.0648 0.0232  135 THR A O   
1100  C CB  . THR A 135 ? 0.4135 0.2884 0.5333 -0.0261 -0.0469 0.0202  135 THR A CB  
1101  O OG1 . THR A 135 ? 0.4157 0.2994 0.5396 -0.0264 -0.0376 0.0181  135 THR A OG1 
1102  C CG2 . THR A 135 ? 0.4329 0.2959 0.5371 -0.0306 -0.0488 0.0242  135 THR A CG2 
1103  N N   . ASP A 136 ? 0.4153 0.2843 0.5440 -0.0208 -0.0668 0.0204  136 ASP A N   
1104  C CA  . ASP A 136 ? 0.4125 0.2729 0.5394 -0.0197 -0.0779 0.0226  136 ASP A CA  
1105  C C   . ASP A 136 ? 0.4253 0.2838 0.5486 -0.0208 -0.0835 0.0222  136 ASP A C   
1106  O O   . ASP A 136 ? 0.4411 0.2882 0.5523 -0.0228 -0.0916 0.0250  136 ASP A O   
1107  C CB  . ASP A 136 ? 0.4040 0.2691 0.5478 -0.0140 -0.0818 0.0212  136 ASP A CB  
1108  C CG  . ASP A 136 ? 0.4334 0.2903 0.5783 -0.0117 -0.0937 0.0232  136 ASP A CG  
1109  O OD1 . ASP A 136 ? 0.4360 0.2815 0.5715 -0.0128 -0.0981 0.0264  136 ASP A OD1 
1110  O OD2 . ASP A 136 ? 0.4656 0.3278 0.6217 -0.0089 -0.0990 0.0216  136 ASP A OD2 
1111  N N   . HIS A 137 ? 0.4033 0.2722 0.5367 -0.0197 -0.0796 0.0190  137 HIS A N   
1112  C CA  . HIS A 137 ? 0.4117 0.2797 0.5437 -0.0208 -0.0849 0.0181  137 HIS A CA  
1113  C C   . HIS A 137 ? 0.4229 0.2795 0.5324 -0.0260 -0.0850 0.0198  137 HIS A C   
1114  O O   . HIS A 137 ? 0.4637 0.3114 0.5640 -0.0275 -0.0938 0.0212  137 HIS A O   
1115  C CB  . HIS A 137 ? 0.3981 0.2790 0.5447 -0.0192 -0.0795 0.0145  137 HIS A CB  
1116  C CG  . HIS A 137 ? 0.4108 0.2908 0.5569 -0.0208 -0.0848 0.0134  137 HIS A CG  
1117  N ND1 . HIS A 137 ? 0.4015 0.2802 0.5547 -0.0194 -0.0956 0.0139  137 HIS A ND1 
1118  C CD2 . HIS A 137 ? 0.4264 0.3055 0.5649 -0.0239 -0.0816 0.0118  137 HIS A CD2 
1119  C CE1 . HIS A 137 ? 0.4355 0.3130 0.5861 -0.0218 -0.0990 0.0127  137 HIS A CE1 
1120  N NE2 . HIS A 137 ? 0.4212 0.2986 0.5626 -0.0245 -0.0905 0.0112  137 HIS A NE2 
1121  N N   . ILE A 138 ? 0.4221 0.2794 0.5229 -0.0285 -0.0750 0.0194  138 ILE A N   
1122  C CA  . ILE A 138 ? 0.4345 0.2818 0.5136 -0.0333 -0.0729 0.0207  138 ILE A CA  
1123  C C   . ILE A 138 ? 0.4767 0.3106 0.5413 -0.0355 -0.0799 0.0251  138 ILE A C   
1124  O O   . ILE A 138 ? 0.5159 0.3388 0.5634 -0.0385 -0.0849 0.0266  138 ILE A O   
1125  C CB  . ILE A 138 ? 0.4135 0.2654 0.4890 -0.0350 -0.0604 0.0197  138 ILE A CB  
1126  C CG1 . ILE A 138 ? 0.4099 0.2734 0.4976 -0.0331 -0.0539 0.0157  138 ILE A CG1 
1127  C CG2 . ILE A 138 ? 0.4289 0.2707 0.4822 -0.0398 -0.0575 0.0211  138 ILE A CG2 
1128  C CD1 . ILE A 138 ? 0.4179 0.2856 0.5022 -0.0345 -0.0426 0.0146  138 ILE A CD1 
1129  N N   . HIS A 139 ? 0.4333 0.2669 0.5033 -0.0341 -0.0802 0.0273  139 HIS A N   
1130  C CA  . HIS A 139 ? 0.4528 0.2728 0.5100 -0.0359 -0.0877 0.0319  139 HIS A CA  
1131  C C   . HIS A 139 ? 0.4758 0.2890 0.5317 -0.0346 -0.1007 0.0328  139 HIS A C   
1132  O O   . HIS A 139 ? 0.4818 0.2814 0.5193 -0.0378 -0.1070 0.0361  139 HIS A O   
1133  C CB  . HIS A 139 ? 0.4416 0.2621 0.5076 -0.0338 -0.0878 0.0335  139 HIS A CB  
1134  C CG  . HIS A 139 ? 0.4601 0.2654 0.5126 -0.0359 -0.0960 0.0386  139 HIS A CG  
1135  N ND1 . HIS A 139 ? 0.4530 0.2520 0.5092 -0.0328 -0.1083 0.0401  139 HIS A ND1 
1136  C CD2 . HIS A 139 ? 0.4705 0.2651 0.5051 -0.0411 -0.0935 0.0427  139 HIS A CD2 
1137  C CE1 . HIS A 139 ? 0.4796 0.2638 0.5198 -0.0360 -0.1134 0.0451  139 HIS A CE1 
1138  N NE2 . HIS A 139 ? 0.4805 0.2620 0.5076 -0.0412 -0.1042 0.0469  139 HIS A NE2 
1139  N N   . SER A 140 ? 0.4622 0.2852 0.5381 -0.0299 -0.1047 0.0299  140 SER A N   
1140  C CA  . SER A 140 ? 0.4740 0.2930 0.5539 -0.0278 -0.1176 0.0305  140 SER A CA  
1141  C C   . SER A 140 ? 0.4926 0.3064 0.5601 -0.0311 -0.1214 0.0297  140 SER A C   
1142  O O   . SER A 140 ? 0.5333 0.3362 0.5907 -0.0321 -0.1323 0.0321  140 SER A O   
1143  C CB  . SER A 140 ? 0.4512 0.2836 0.5574 -0.0221 -0.1193 0.0275  140 SER A CB  
1144  O OG  . SER A 140 ? 0.4672 0.2969 0.5787 -0.0202 -0.1318 0.0280  140 SER A OG  
1145  N N   . VAL A 141 ? 0.4820 0.3024 0.5491 -0.0327 -0.1132 0.0264  141 VAL A N   
1146  C CA  . VAL A 141 ? 0.4914 0.3060 0.5471 -0.0354 -0.1177 0.0251  141 VAL A CA  
1147  C C   . VAL A 141 ? 0.5188 0.3220 0.5478 -0.0405 -0.1124 0.0264  141 VAL A C   
1148  O O   . VAL A 141 ? 0.5167 0.3125 0.5317 -0.0431 -0.1158 0.0254  141 VAL A O   
1149  C CB  . VAL A 141 ? 0.4708 0.2975 0.5412 -0.0343 -0.1137 0.0204  141 VAL A CB  
1150  C CG1 . VAL A 141 ? 0.4432 0.2819 0.5402 -0.0296 -0.1183 0.0192  141 VAL A CG1 
1151  C CG2 . VAL A 141 ? 0.4587 0.2925 0.5286 -0.0351 -0.0993 0.0181  141 VAL A CG2 
1152  N N   . THR A 142 ? 0.5356 0.3378 0.5585 -0.0418 -0.1040 0.0285  142 THR A N   
1153  C CA  . THR A 142 ? 0.5376 0.3304 0.5370 -0.0466 -0.0973 0.0303  142 THR A CA  
1154  C C   . THR A 142 ? 0.5360 0.3373 0.5363 -0.0474 -0.0841 0.0265  142 THR A C   
1155  O O   . THR A 142 ? 0.5330 0.3423 0.5435 -0.0457 -0.0826 0.0223  142 THR A O   
1156  C CB  . THR A 142 ? 0.5485 0.3248 0.5231 -0.0503 -0.1052 0.0326  142 THR A CB  
1157  O OG1 . THR A 142 ? 0.5377 0.3150 0.5095 -0.0507 -0.1057 0.0284  142 THR A OG1 
1158  C CG2 . THR A 142 ? 0.5349 0.3019 0.5086 -0.0492 -0.1199 0.0365  142 THR A CG2 
1159  N N   . GLY A 143 ? 0.5458 0.3459 0.5368 -0.0501 -0.0747 0.0281  143 GLY A N   
1160  C CA  . GLY A 143 ? 0.5706 0.3781 0.5614 -0.0509 -0.0619 0.0250  143 GLY A CA  
1161  C C   . GLY A 143 ? 0.5969 0.3979 0.5711 -0.0531 -0.0608 0.0223  143 GLY A C   
1162  O O   . GLY A 143 ? 0.5632 0.3714 0.5423 -0.0520 -0.0536 0.0181  143 GLY A O   
1163  N N   . LYS A 144 ? 0.6125 0.3990 0.5663 -0.0560 -0.0683 0.0247  144 LYS A N   
1164  C CA  . LYS A 144 ? 0.6659 0.4444 0.6014 -0.0581 -0.0681 0.0219  144 LYS A CA  
1165  C C   . LYS A 144 ? 0.6487 0.4327 0.5978 -0.0552 -0.0737 0.0174  144 LYS A C   
1166  O O   . LYS A 144 ? 0.6480 0.4341 0.5947 -0.0551 -0.0679 0.0129  144 LYS A O   
1167  C CB  . LYS A 144 ? 0.7275 0.4883 0.6362 -0.0622 -0.0750 0.0256  144 LYS A CB  
1168  C CG  . LYS A 144 ? 0.7899 0.5411 0.6769 -0.0645 -0.0742 0.0222  144 LYS A CG  
1169  C CD  . LYS A 144 ? 0.8523 0.5859 0.7079 -0.0692 -0.0765 0.0257  144 LYS A CD  
1170  C CE  . LYS A 144 ? 0.8603 0.5812 0.6971 -0.0705 -0.0852 0.0232  144 LYS A CE  
1171  N NZ  . LYS A 144 ? 0.8450 0.5721 0.6867 -0.0687 -0.0791 0.0163  144 LYS A NZ  
1172  N N   . ALA A 145 ? 0.6062 0.3928 0.5704 -0.0527 -0.0845 0.0184  145 ALA A N   
1173  C CA  . ALA A 145 ? 0.5896 0.3825 0.5685 -0.0504 -0.0895 0.0146  145 ALA A CA  
1174  C C   . ALA A 145 ? 0.5749 0.3815 0.5696 -0.0482 -0.0782 0.0108  145 ALA A C   
1175  O O   . ALA A 145 ? 0.5380 0.3458 0.5329 -0.0482 -0.0764 0.0068  145 ALA A O   
1176  C CB  . ALA A 145 ? 0.5715 0.3679 0.5676 -0.0477 -0.1009 0.0165  145 ALA A CB  
1177  N N   . PHE A 146 ? 0.5666 0.3825 0.5735 -0.0465 -0.0710 0.0124  146 PHE A N   
1178  C CA  . PHE A 146 ? 0.5176 0.3461 0.5390 -0.0444 -0.0605 0.0096  146 PHE A CA  
1179  C C   . PHE A 146 ? 0.5043 0.3301 0.5120 -0.0462 -0.0511 0.0066  146 PHE A C   
1180  O O   . PHE A 146 ? 0.4691 0.2994 0.4829 -0.0449 -0.0480 0.0026  146 PHE A O   
1181  C CB  . PHE A 146 ? 0.4946 0.3308 0.5268 -0.0429 -0.0550 0.0121  146 PHE A CB  
1182  C CG  . PHE A 146 ? 0.4732 0.3217 0.5186 -0.0409 -0.0445 0.0093  146 PHE A CG  
1183  C CD1 . PHE A 146 ? 0.4553 0.3130 0.5182 -0.0380 -0.0450 0.0067  146 PHE A CD1 
1184  C CD2 . PHE A 146 ? 0.4531 0.3034 0.4928 -0.0421 -0.0343 0.0095  146 PHE A CD2 
1185  C CE1 . PHE A 146 ? 0.4335 0.3009 0.5066 -0.0362 -0.0359 0.0045  146 PHE A CE1 
1186  C CE2 . PHE A 146 ? 0.4446 0.3055 0.4961 -0.0400 -0.0257 0.0070  146 PHE A CE2 
1187  C CZ  . PHE A 146 ? 0.4200 0.2890 0.4876 -0.0370 -0.0267 0.0046  146 PHE A CZ  
1188  N N   . VAL A 147 ? 0.4877 0.3063 0.4774 -0.0490 -0.0464 0.0085  147 VAL A N   
1189  C CA  . VAL A 147 ? 0.5119 0.3292 0.4897 -0.0503 -0.0360 0.0057  147 VAL A CA  
1190  C C   . VAL A 147 ? 0.5285 0.3372 0.4936 -0.0510 -0.0394 0.0017  147 VAL A C   
1191  O O   . VAL A 147 ? 0.5001 0.3118 0.4659 -0.0499 -0.0325 -0.0025 147 VAL A O   
1192  C CB  . VAL A 147 ? 0.5168 0.3287 0.4790 -0.0536 -0.0300 0.0092  147 VAL A CB  
1193  C CG1 . VAL A 147 ? 0.5317 0.3407 0.4784 -0.0552 -0.0195 0.0064  147 VAL A CG1 
1194  C CG2 . VAL A 147 ? 0.4863 0.3083 0.4635 -0.0527 -0.0250 0.0120  147 VAL A CG2 
1195  N N   . ASP A 148 ? 0.5603 0.3580 0.5141 -0.0528 -0.0507 0.0028  148 ASP A N   
1196  C CA  . ASP A 148 ? 0.5739 0.3625 0.5154 -0.0537 -0.0557 -0.0010 148 ASP A CA  
1197  C C   . ASP A 148 ? 0.5669 0.3639 0.5275 -0.0511 -0.0573 -0.0049 148 ASP A C   
1198  O O   . ASP A 148 ? 0.5747 0.3674 0.5286 -0.0513 -0.0561 -0.0095 148 ASP A O   
1199  C CB  . ASP A 148 ? 0.6109 0.3871 0.5394 -0.0560 -0.0692 0.0017  148 ASP A CB  
1200  C CG  . ASP A 148 ? 0.6691 0.4326 0.5715 -0.0595 -0.0682 0.0051  148 ASP A CG  
1201  O OD1 . ASP A 148 ? 0.6891 0.4534 0.5825 -0.0605 -0.0559 0.0046  148 ASP A OD1 
1202  O OD2 . ASP A 148 ? 0.7042 0.4571 0.5958 -0.0613 -0.0796 0.0083  148 ASP A OD2 
1203  N N   . LEU A 149 ? 0.5435 0.3514 0.5274 -0.0488 -0.0606 -0.0032 149 LEU A N   
1204  C CA  . LEU A 149 ? 0.5311 0.3473 0.5338 -0.0468 -0.0620 -0.0062 149 LEU A CA  
1205  C C   . LEU A 149 ? 0.5317 0.3552 0.5398 -0.0450 -0.0495 -0.0091 149 LEU A C   
1206  O O   . LEU A 149 ? 0.4959 0.3181 0.5041 -0.0447 -0.0482 -0.0132 149 LEU A O   
1207  C CB  . LEU A 149 ? 0.5130 0.3390 0.5382 -0.0447 -0.0679 -0.0034 149 LEU A CB  
1208  C CG  . LEU A 149 ? 0.4958 0.3327 0.5432 -0.0428 -0.0678 -0.0056 149 LEU A CG  
1209  C CD1 . LEU A 149 ? 0.5157 0.3458 0.5595 -0.0446 -0.0761 -0.0085 149 LEU A CD1 
1210  C CD2 . LEU A 149 ? 0.4568 0.3049 0.5262 -0.0403 -0.0708 -0.0030 149 LEU A CD2 
1211  N N   . MET A 150 ? 0.5228 0.3534 0.5354 -0.0439 -0.0407 -0.0071 150 MET A N   
1212  C CA  . MET A 150 ? 0.4929 0.3307 0.5109 -0.0420 -0.0293 -0.0096 150 MET A CA  
1213  C C   . MET A 150 ? 0.5142 0.3430 0.5142 -0.0430 -0.0249 -0.0138 150 MET A C   
1214  O O   . MET A 150 ? 0.5010 0.3316 0.5064 -0.0414 -0.0222 -0.0176 150 MET A O   
1215  C CB  . MET A 150 ? 0.4782 0.3233 0.5004 -0.0413 -0.0212 -0.0069 150 MET A CB  
1216  C CG  . MET A 150 ? 0.4693 0.3231 0.5092 -0.0398 -0.0246 -0.0034 150 MET A CG  
1217  S SD  . MET A 150 ? 0.4747 0.3406 0.5392 -0.0364 -0.0249 -0.0050 150 MET A SD  
1218  C CE  . MET A 150 ? 0.4725 0.3340 0.5405 -0.0372 -0.0380 -0.0048 150 MET A CE  
1219  N N   . ASN A 151 ? 0.5348 0.3530 0.5128 -0.0457 -0.0247 -0.0132 151 ASN A N   
1220  C CA  . ASN A 151 ? 0.5701 0.3790 0.5292 -0.0465 -0.0201 -0.0175 151 ASN A CA  
1221  C C   . ASN A 151 ? 0.5837 0.3863 0.5420 -0.0462 -0.0274 -0.0218 151 ASN A C   
1222  O O   . ASN A 151 ? 0.5832 0.3859 0.5421 -0.0445 -0.0220 -0.0264 151 ASN A O   
1223  C CB  . ASN A 151 ? 0.5729 0.3709 0.5073 -0.0497 -0.0189 -0.0158 151 ASN A CB  
1224  C CG  . ASN A 151 ? 0.5705 0.3751 0.5054 -0.0501 -0.0085 -0.0129 151 ASN A CG  
1225  O OD1 . ASN A 151 ? 0.6325 0.4327 0.5579 -0.0529 -0.0103 -0.0083 151 ASN A OD1 
1226  N ND2 . ASN A 151 ? 0.5244 0.3390 0.4701 -0.0476 0.0022  -0.0150 151 ASN A ND2 
1227  N N   . THR A 152 ? 0.5681 0.3659 0.5270 -0.0479 -0.0399 -0.0203 152 THR A N   
1228  C CA  . THR A 152 ? 0.5633 0.3551 0.5223 -0.0484 -0.0480 -0.0239 152 THR A CA  
1229  C C   . THR A 152 ? 0.5163 0.3176 0.4949 -0.0458 -0.0434 -0.0267 152 THR A C   
1230  O O   . THR A 152 ? 0.5250 0.3205 0.4982 -0.0455 -0.0422 -0.0314 152 THR A O   
1231  C CB  . THR A 152 ? 0.5818 0.3721 0.5467 -0.0500 -0.0618 -0.0207 152 THR A CB  
1232  O OG1 . THR A 152 ? 0.6181 0.3973 0.5613 -0.0525 -0.0656 -0.0184 152 THR A OG1 
1233  C CG2 . THR A 152 ? 0.5714 0.3569 0.5397 -0.0512 -0.0716 -0.0239 152 THR A CG2 
1234  N N   . LEU A 153 ? 0.4708 0.2857 0.4712 -0.0438 -0.0409 -0.0237 153 LEU A N   
1235  C CA  . LEU A 153 ? 0.4462 0.2696 0.4652 -0.0416 -0.0376 -0.0254 153 LEU A CA  
1236  C C   . LEU A 153 ? 0.4586 0.2841 0.4752 -0.0392 -0.0256 -0.0283 153 LEU A C   
1237  O O   . LEU A 153 ? 0.4569 0.2830 0.4801 -0.0377 -0.0236 -0.0314 153 LEU A O   
1238  C CB  . LEU A 153 ? 0.4189 0.2556 0.4600 -0.0403 -0.0385 -0.0212 153 LEU A CB  
1239  C CG  . LEU A 153 ? 0.4296 0.2661 0.4759 -0.0419 -0.0499 -0.0182 153 LEU A CG  
1240  C CD1 . LEU A 153 ? 0.4139 0.2639 0.4831 -0.0400 -0.0497 -0.0151 153 LEU A CD1 
1241  C CD2 . LEU A 153 ? 0.4539 0.2825 0.4973 -0.0442 -0.0597 -0.0207 153 LEU A CD2 
1242  N N   . ILE A 154 ? 0.4530 0.2801 0.4615 -0.0387 -0.0179 -0.0270 154 ILE A N   
1243  C CA  . ILE A 154 ? 0.4676 0.2976 0.4746 -0.0362 -0.0066 -0.0297 154 ILE A CA  
1244  C C   . ILE A 154 ? 0.4958 0.3138 0.4865 -0.0362 -0.0057 -0.0354 154 ILE A C   
1245  O O   . ILE A 154 ? 0.4755 0.2949 0.4711 -0.0335 -0.0002 -0.0390 154 ILE A O   
1246  C CB  . ILE A 154 ? 0.4476 0.2813 0.4487 -0.0364 0.0012  -0.0272 154 ILE A CB  
1247  C CG1 . ILE A 154 ? 0.4370 0.2828 0.4558 -0.0356 0.0015  -0.0225 154 ILE A CG1 
1248  C CG2 . ILE A 154 ? 0.4427 0.2775 0.4390 -0.0341 0.0126  -0.0309 154 ILE A CG2 
1249  C CD1 . ILE A 154 ? 0.4526 0.3000 0.4647 -0.0372 0.0056  -0.0190 154 ILE A CD1 
1250  N N   . ASN A 155 ? 0.5214 0.3272 0.4924 -0.0392 -0.0115 -0.0361 155 ASN A N   
1251  C CA  . ASN A 155 ? 0.5825 0.3752 0.5337 -0.0395 -0.0107 -0.0417 155 ASN A CA  
1252  C C   . ASN A 155 ? 0.5691 0.3573 0.5269 -0.0391 -0.0172 -0.0454 155 ASN A C   
1253  O O   . ASN A 155 ? 0.6188 0.4004 0.5689 -0.0375 -0.0133 -0.0508 155 ASN A O   
1254  C CB  . ASN A 155 ? 0.6192 0.3993 0.5457 -0.0430 -0.0152 -0.0412 155 ASN A CB  
1255  C CG  . ASN A 155 ? 0.6534 0.4360 0.5700 -0.0434 -0.0058 -0.0387 155 ASN A CG  
1256  O OD1 . ASN A 155 ? 0.6566 0.4492 0.5826 -0.0409 0.0050  -0.0387 155 ASN A OD1 
1257  N ND2 . ASN A 155 ? 0.6604 0.4338 0.5580 -0.0468 -0.0099 -0.0362 155 ASN A ND2 
1258  N N   . ILE A 156 ? 0.5420 0.3337 0.5139 -0.0408 -0.0271 -0.0425 156 ILE A N   
1259  C CA  . ILE A 156 ? 0.5226 0.3110 0.5027 -0.0413 -0.0339 -0.0452 156 ILE A CA  
1260  C C   . ILE A 156 ? 0.5139 0.3101 0.5098 -0.0379 -0.0260 -0.0466 156 ILE A C   
1261  O O   . ILE A 156 ? 0.4924 0.2820 0.4873 -0.0373 -0.0267 -0.0509 156 ILE A O   
1262  C CB  . ILE A 156 ? 0.5158 0.3085 0.5096 -0.0439 -0.0452 -0.0411 156 ILE A CB  
1263  C CG1 . ILE A 156 ? 0.5397 0.3207 0.5166 -0.0473 -0.0557 -0.0412 156 ILE A CG1 
1264  C CG2 . ILE A 156 ? 0.5119 0.3084 0.5243 -0.0441 -0.0492 -0.0419 156 ILE A CG2 
1265  C CD1 . ILE A 156 ? 0.5425 0.3295 0.5332 -0.0492 -0.0661 -0.0364 156 ILE A CD1 
1266  N N   . ILE A 157 ? 0.4971 0.3066 0.5066 -0.0356 -0.0187 -0.0430 157 ILE A N   
1267  C CA  . ILE A 157 ? 0.4782 0.2948 0.5017 -0.0322 -0.0115 -0.0440 157 ILE A CA  
1268  C C   . ILE A 157 ? 0.5088 0.3199 0.5203 -0.0292 -0.0025 -0.0491 157 ILE A C   
1269  O O   . ILE A 157 ? 0.4985 0.3067 0.5143 -0.0270 -0.0006 -0.0525 157 ILE A O   
1270  C CB  . ILE A 157 ? 0.4319 0.2636 0.4731 -0.0306 -0.0074 -0.0389 157 ILE A CB  
1271  C CG1 . ILE A 157 ? 0.4231 0.2606 0.4790 -0.0327 -0.0154 -0.0349 157 ILE A CG1 
1272  C CG2 . ILE A 157 ? 0.4208 0.2588 0.4731 -0.0268 0.0006  -0.0400 157 ILE A CG2 
1273  C CD1 . ILE A 157 ? 0.4046 0.2552 0.4737 -0.0314 -0.0122 -0.0301 157 ILE A CD1 
1274  N N   . HIS A 158 ? 0.5207 0.3302 0.5178 -0.0290 0.0032  -0.0495 158 HIS A N   
1275  C CA  . HIS A 158 ? 0.5476 0.3525 0.5331 -0.0261 0.0124  -0.0545 158 HIS A CA  
1276  C C   . HIS A 158 ? 0.6001 0.3901 0.5726 -0.0260 0.0088  -0.0609 158 HIS A C   
1277  O O   . HIS A 158 ? 0.6092 0.3969 0.5817 -0.0223 0.0150  -0.0655 158 HIS A O   
1278  C CB  . HIS A 158 ? 0.5384 0.3428 0.5085 -0.0271 0.0186  -0.0538 158 HIS A CB  
1279  C CG  . HIS A 158 ? 0.5106 0.3288 0.4922 -0.0265 0.0245  -0.0488 158 HIS A CG  
1280  N ND1 . HIS A 158 ? 0.4859 0.3168 0.4890 -0.0238 0.0277  -0.0466 158 HIS A ND1 
1281  C CD2 . HIS A 158 ? 0.4866 0.3070 0.4602 -0.0286 0.0277  -0.0456 158 HIS A CD2 
1282  C CE1 . HIS A 158 ? 0.4528 0.2931 0.4607 -0.0243 0.0322  -0.0425 158 HIS A CE1 
1283  N NE2 . HIS A 158 ? 0.4599 0.2940 0.4505 -0.0273 0.0324  -0.0418 158 HIS A NE2 
1284  N N   . LYS A 159 ? 0.6284 0.4077 0.5897 -0.0299 -0.0014 -0.0614 159 LYS A N   
1285  C CA  . LYS A 159 ? 0.6891 0.4535 0.6381 -0.0304 -0.0063 -0.0675 159 LYS A CA  
1286  C C   . LYS A 159 ? 0.6358 0.4009 0.6022 -0.0304 -0.0121 -0.0678 159 LYS A C   
1287  O O   . LYS A 159 ? 0.6216 0.3785 0.5850 -0.0283 -0.0108 -0.0731 159 LYS A O   
1288  C CB  . LYS A 159 ? 0.8113 0.5633 0.7403 -0.0348 -0.0156 -0.0681 159 LYS A CB  
1289  C CG  . LYS A 159 ? 0.9736 0.7194 0.8790 -0.0348 -0.0091 -0.0698 159 LYS A CG  
1290  C CD  . LYS A 159 ? 1.0809 0.8136 0.9641 -0.0392 -0.0184 -0.0697 159 LYS A CD  
1291  C CE  . LYS A 159 ? 1.1083 0.8399 0.9734 -0.0398 -0.0112 -0.0681 159 LYS A CE  
1292  N NZ  . LYS A 159 ? 1.1078 0.8401 0.9704 -0.0438 -0.0196 -0.0618 159 LYS A NZ  
1293  N N   . GLY A 160 ? 0.6051 0.3795 0.5896 -0.0326 -0.0183 -0.0622 160 GLY A N   
1294  C CA  . GLY A 160 ? 0.5835 0.3582 0.5837 -0.0337 -0.0245 -0.0619 160 GLY A CA  
1295  C C   . GLY A 160 ? 0.5600 0.3421 0.5762 -0.0298 -0.0170 -0.0617 160 GLY A C   
1296  O O   . GLY A 160 ? 0.6190 0.3963 0.6419 -0.0300 -0.0200 -0.0635 160 GLY A O   
1297  N N   . HIS A 161 ? 0.4934 0.2870 0.5161 -0.0266 -0.0079 -0.0591 161 HIS A N   
1298  C CA  . HIS A 161 ? 0.4570 0.2576 0.4936 -0.0225 -0.0010 -0.0587 161 HIS A CA  
1299  C C   . HIS A 161 ? 0.4622 0.2671 0.4932 -0.0183 0.0098  -0.0603 161 HIS A C   
1300  O O   . HIS A 161 ? 0.4309 0.2480 0.4699 -0.0175 0.0142  -0.0561 161 HIS A O   
1301  C CB  . HIS A 161 ? 0.4266 0.2403 0.4843 -0.0234 -0.0026 -0.0524 161 HIS A CB  
1302  C CG  . HIS A 161 ? 0.4123 0.2302 0.4829 -0.0199 0.0022  -0.0521 161 HIS A CG  
1303  N ND1 . HIS A 161 ? 0.3873 0.2154 0.4758 -0.0202 0.0016  -0.0469 161 HIS A ND1 
1304  C CD2 . HIS A 161 ? 0.4088 0.2214 0.4764 -0.0157 0.0076  -0.0563 161 HIS A CD2 
1305  C CE1 . HIS A 161 ? 0.3941 0.2226 0.4892 -0.0166 0.0062  -0.0476 161 HIS A CE1 
1306  N NE2 . HIS A 161 ? 0.4104 0.2297 0.4937 -0.0136 0.0098  -0.0533 161 HIS A NE2 
1307  N N   . PRO A 162 ? 0.5004 0.2953 0.5173 -0.0156 0.0142  -0.0666 162 PRO A N   
1308  C CA  . PRO A 162 ? 0.5065 0.3050 0.5156 -0.0124 0.0245  -0.0686 162 PRO A CA  
1309  C C   . PRO A 162 ? 0.4920 0.3032 0.5178 -0.0078 0.0324  -0.0667 162 PRO A C   
1310  O O   . PRO A 162 ? 0.5132 0.3255 0.5518 -0.0056 0.0315  -0.0666 162 PRO A O   
1311  C CB  . PRO A 162 ? 0.5264 0.3101 0.5170 -0.0105 0.0266  -0.0764 162 PRO A CB  
1312  C CG  . PRO A 162 ? 0.5362 0.3074 0.5222 -0.0141 0.0154  -0.0780 162 PRO A CG  
1313  C CD  . PRO A 162 ? 0.5059 0.2854 0.5133 -0.0159 0.0096  -0.0724 162 PRO A CD  
1314  N N   . GLY A 163 ? 0.4808 0.3011 0.5059 -0.0069 0.0397  -0.0650 163 GLY A N   
1315  C CA  . GLY A 163 ? 0.4606 0.2926 0.4992 -0.0025 0.0479  -0.0641 163 GLY A CA  
1316  C C   . GLY A 163 ? 0.4442 0.2887 0.5008 -0.0035 0.0453  -0.0574 163 GLY A C   
1317  O O   . GLY A 163 ? 0.4767 0.3308 0.5458 0.0000  0.0505  -0.0561 163 GLY A O   
1318  N N   . ILE A 164 ? 0.4066 0.2509 0.4649 -0.0079 0.0372  -0.0534 164 ILE A N   
1319  C CA  . ILE A 164 ? 0.3863 0.2418 0.4610 -0.0087 0.0350  -0.0475 164 ILE A CA  
1320  C C   . ILE A 164 ? 0.4076 0.2703 0.4802 -0.0111 0.0361  -0.0437 164 ILE A C   
1321  O O   . ILE A 164 ? 0.4349 0.2919 0.4960 -0.0147 0.0319  -0.0434 164 ILE A O   
1322  C CB  . ILE A 164 ? 0.3868 0.2394 0.4677 -0.0117 0.0260  -0.0452 164 ILE A CB  
1323  C CG1 . ILE A 164 ? 0.4106 0.2529 0.4912 -0.0108 0.0230  -0.0488 164 ILE A CG1 
1324  C CG2 . ILE A 164 ? 0.3597 0.2243 0.4571 -0.0118 0.0253  -0.0396 164 ILE A CG2 
1325  C CD1 . ILE A 164 ? 0.4127 0.2572 0.5026 -0.0059 0.0281  -0.0500 164 ILE A CD1 
1326  N N   . PRO A 165 ? 0.3982 0.2727 0.4814 -0.0095 0.0410  -0.0407 165 PRO A N   
1327  C CA  . PRO A 165 ? 0.3909 0.2713 0.4727 -0.0122 0.0412  -0.0369 165 PRO A CA  
1328  C C   . PRO A 165 ? 0.3954 0.2759 0.4801 -0.0157 0.0328  -0.0329 165 PRO A C   
1329  O O   . PRO A 165 ? 0.3860 0.2678 0.4808 -0.0156 0.0283  -0.0316 165 PRO A O   
1330  C CB  . PRO A 165 ? 0.3792 0.2718 0.4748 -0.0092 0.0471  -0.0350 165 PRO A CB  
1331  C CG  . PRO A 165 ? 0.3888 0.2799 0.4857 -0.0049 0.0526  -0.0393 165 PRO A CG  
1332  C CD  . PRO A 165 ? 0.3912 0.2727 0.4865 -0.0049 0.0466  -0.0413 165 PRO A CD  
1333  N N   . VAL A 166 ? 0.4064 0.2857 0.4823 -0.0188 0.0311  -0.0309 166 VAL A N   
1334  C CA  . VAL A 166 ? 0.4014 0.2808 0.4794 -0.0218 0.0234  -0.0272 166 VAL A CA  
1335  C C   . VAL A 166 ? 0.3879 0.2750 0.4693 -0.0227 0.0254  -0.0232 166 VAL A C   
1336  O O   . VAL A 166 ? 0.3974 0.2842 0.4703 -0.0234 0.0307  -0.0233 166 VAL A O   
1337  C CB  . VAL A 166 ? 0.4230 0.2905 0.4846 -0.0249 0.0176  -0.0288 166 VAL A CB  
1338  C CG1 . VAL A 166 ? 0.4253 0.2924 0.4896 -0.0277 0.0086  -0.0253 166 VAL A CG1 
1339  C CG2 . VAL A 166 ? 0.4351 0.2937 0.4916 -0.0241 0.0160  -0.0335 166 VAL A CG2 
1340  N N   . THR A 167 ? 0.3630 0.2566 0.4568 -0.0227 0.0215  -0.0197 167 THR A N   
1341  C CA  . THR A 167 ? 0.3527 0.2516 0.4491 -0.0238 0.0217  -0.0160 167 THR A CA  
1342  C C   . THR A 167 ? 0.3391 0.2396 0.4432 -0.0247 0.0140  -0.0133 167 THR A C   
1343  O O   . THR A 167 ? 0.3173 0.2128 0.4200 -0.0256 0.0081  -0.0142 167 THR A O   
1344  C CB  . THR A 167 ? 0.3302 0.2388 0.4362 -0.0215 0.0286  -0.0154 167 THR A CB  
1345  O OG1 . THR A 167 ? 0.3209 0.2332 0.4280 -0.0231 0.0284  -0.0120 167 THR A OG1 
1346  C CG2 . THR A 167 ? 0.3223 0.2375 0.4432 -0.0187 0.0284  -0.0151 167 THR A CG2 
1347  N N   . LEU A 168 ? 0.3323 0.2393 0.4441 -0.0245 0.0137  -0.0102 168 LEU A N   
1348  C CA  . LEU A 168 ? 0.3471 0.2559 0.4666 -0.0247 0.0070  -0.0080 168 LEU A CA  
1349  C C   . LEU A 168 ? 0.3362 0.2546 0.4693 -0.0225 0.0091  -0.0062 168 LEU A C   
1350  O O   . LEU A 168 ? 0.3393 0.2622 0.4745 -0.0214 0.0148  -0.0061 168 LEU A O   
1351  C CB  . LEU A 168 ? 0.3671 0.2694 0.4769 -0.0273 0.0014  -0.0062 168 LEU A CB  
1352  C CG  . LEU A 168 ? 0.3779 0.2828 0.4882 -0.0278 0.0022  -0.0032 168 LEU A CG  
1353  C CD1 . LEU A 168 ? 0.3901 0.2870 0.4906 -0.0303 -0.0046 -0.0010 168 LEU A CD1 
1354  C CD2 . LEU A 168 ? 0.3838 0.2905 0.4892 -0.0282 0.0102  -0.0034 168 LEU A CD2 
1355  N N   . SER A 169 ? 0.3391 0.2605 0.4812 -0.0220 0.0043  -0.0048 169 SER A N   
1356  C CA  . SER A 169 ? 0.3052 0.2346 0.4590 -0.0199 0.0053  -0.0033 169 SER A CA  
1357  C C   . SER A 169 ? 0.3437 0.2720 0.4956 -0.0206 0.0019  -0.0012 169 SER A C   
1358  O O   . SER A 169 ? 0.3741 0.2993 0.5258 -0.0213 -0.0042 -0.0004 169 SER A O   
1359  C CB  . SER A 169 ? 0.2942 0.2271 0.4584 -0.0189 0.0028  -0.0035 169 SER A CB  
1360  O OG  . SER A 169 ? 0.2771 0.2167 0.4519 -0.0170 0.0025  -0.0021 169 SER A OG  
1361  N N   . ALA A 170 ? 0.3515 0.2817 0.5019 -0.0206 0.0055  -0.0002 170 ALA A N   
1362  C CA  . ALA A 170 ? 0.3420 0.2693 0.4889 -0.0218 0.0022  0.0018  170 ALA A CA  
1363  C C   . ALA A 170 ? 0.3094 0.2425 0.4630 -0.0204 0.0051  0.0026  170 ALA A C   
1364  O O   . ALA A 170 ? 0.3083 0.2449 0.4626 -0.0203 0.0104  0.0021  170 ALA A O   
1365  C CB  . ALA A 170 ? 0.3592 0.2789 0.4920 -0.0250 0.0026  0.0025  170 ALA A CB  
1366  N N   . ASN A 171 ? 0.3122 0.2463 0.4717 -0.0190 0.0012  0.0036  171 ASN A N   
1367  C CA  . ASN A 171 ? 0.3388 0.2776 0.5043 -0.0175 0.0031  0.0039  171 ASN A CA  
1368  C C   . ASN A 171 ? 0.3285 0.2637 0.4869 -0.0202 0.0042  0.0054  171 ASN A C   
1369  O O   . ASN A 171 ? 0.3573 0.2856 0.5081 -0.0225 0.0007  0.0070  171 ASN A O   
1370  C CB  . ASN A 171 ? 0.3506 0.2911 0.5240 -0.0149 -0.0010 0.0038  171 ASN A CB  
1371  C CG  . ASN A 171 ? 0.3652 0.3095 0.5434 -0.0131 0.0008  0.0036  171 ASN A CG  
1372  O OD1 . ASN A 171 ? 0.3790 0.3206 0.5532 -0.0147 0.0008  0.0046  171 ASN A OD1 
1373  N ND2 . ASN A 171 ? 0.3553 0.3055 0.5415 -0.0101 0.0025  0.0023  171 ASN A ND2 
1374  N N   . ALA A 172 ? 0.3003 0.2404 0.4617 -0.0201 0.0088  0.0051  172 ALA A N   
1375  C CA  . ALA A 172 ? 0.3041 0.2427 0.4610 -0.0231 0.0109  0.0066  172 ALA A CA  
1376  C C   . ALA A 172 ? 0.3004 0.2347 0.4569 -0.0239 0.0064  0.0083  172 ALA A C   
1377  O O   . ALA A 172 ? 0.3438 0.2738 0.4943 -0.0274 0.0064  0.0103  172 ALA A O   
1378  C CB  . ALA A 172 ? 0.2807 0.2267 0.4436 -0.0223 0.0161  0.0056  172 ALA A CB  
1379  N N   . MET A 173 ? 0.3048 0.2403 0.4679 -0.0207 0.0028  0.0074  173 MET A N   
1380  C CA  . MET A 173 ? 0.3035 0.2344 0.4667 -0.0207 -0.0016 0.0085  173 MET A CA  
1381  C C   . MET A 173 ? 0.3117 0.2338 0.4681 -0.0222 -0.0072 0.0104  173 MET A C   
1382  O O   . MET A 173 ? 0.3107 0.2267 0.4636 -0.0239 -0.0103 0.0122  173 MET A O   
1383  C CB  . MET A 173 ? 0.2875 0.2223 0.4595 -0.0163 -0.0032 0.0065  173 MET A CB  
1384  C CG  . MET A 173 ? 0.2912 0.2325 0.4680 -0.0153 0.0008  0.0051  173 MET A CG  
1385  S SD  . MET A 173 ? 0.3320 0.2705 0.5062 -0.0189 0.0009  0.0065  173 MET A SD  
1386  C CE  . MET A 173 ? 0.2893 0.2223 0.4654 -0.0163 -0.0050 0.0056  173 MET A CE  
1387  N N   . ILE A 174 ? 0.3200 0.2407 0.4737 -0.0219 -0.0087 0.0101  174 ILE A N   
1388  C CA  . ILE A 174 ? 0.3118 0.2240 0.4591 -0.0230 -0.0151 0.0119  174 ILE A CA  
1389  C C   . ILE A 174 ? 0.3339 0.2404 0.4687 -0.0270 -0.0141 0.0135  174 ILE A C   
1390  O O   . ILE A 174 ? 0.3323 0.2299 0.4585 -0.0288 -0.0194 0.0157  174 ILE A O   
1391  C CB  . ILE A 174 ? 0.3047 0.2189 0.4597 -0.0192 -0.0196 0.0105  174 ILE A CB  
1392  C CG1 . ILE A 174 ? 0.2931 0.2137 0.4518 -0.0183 -0.0160 0.0085  174 ILE A CG1 
1393  C CG2 . ILE A 174 ? 0.3021 0.2194 0.4673 -0.0153 -0.0215 0.0093  174 ILE A CG2 
1394  C CD1 . ILE A 174 ? 0.2996 0.2206 0.4633 -0.0165 -0.0211 0.0077  174 ILE A CD1 
1395  N N   . SER A 175 ? 0.3473 0.2584 0.4805 -0.0280 -0.0077 0.0121  175 SER A N   
1396  C CA  . SER A 175 ? 0.3587 0.2646 0.4795 -0.0313 -0.0060 0.0128  175 SER A CA  
1397  C C   . SER A 175 ? 0.3539 0.2619 0.4704 -0.0342 0.0016  0.0132  175 SER A C   
1398  O O   . SER A 175 ? 0.3600 0.2667 0.4684 -0.0361 0.0057  0.0126  175 SER A O   
1399  C CB  . SER A 175 ? 0.3758 0.2835 0.4977 -0.0296 -0.0061 0.0103  175 SER A CB  
1400  O OG  . SER A 175 ? 0.3690 0.2755 0.4961 -0.0273 -0.0132 0.0101  175 SER A OG  
1401  N N   . ASP A 176 ? 0.3525 0.2632 0.4739 -0.0349 0.0031  0.0144  176 ASP A N   
1402  C CA  . ASP A 176 ? 0.3470 0.2591 0.4648 -0.0386 0.0091  0.0157  176 ASP A CA  
1403  C C   . ASP A 176 ? 0.3414 0.2449 0.4440 -0.0433 0.0099  0.0182  176 ASP A C   
1404  O O   . ASP A 176 ? 0.3446 0.2506 0.4433 -0.0459 0.0169  0.0182  176 ASP A O   
1405  C CB  . ASP A 176 ? 0.3567 0.2703 0.4811 -0.0393 0.0080  0.0171  176 ASP A CB  
1406  C CG  . ASP A 176 ? 0.3624 0.2679 0.4850 -0.0392 0.0002  0.0191  176 ASP A CG  
1407  O OD1 . ASP A 176 ? 0.3747 0.2743 0.4925 -0.0381 -0.0049 0.0194  176 ASP A OD1 
1408  O OD2 . ASP A 176 ? 0.3614 0.2665 0.4883 -0.0400 -0.0012 0.0201  176 ASP A OD2 
1409  N N   . TYR A 177 ? 0.3410 0.2344 0.4350 -0.0445 0.0030  0.0205  177 TYR A N   
1410  C CA  . TYR A 177 ? 0.3547 0.2381 0.4322 -0.0492 0.0028  0.0236  177 TYR A CA  
1411  C C   . TYR A 177 ? 0.3833 0.2641 0.4501 -0.0495 0.0051  0.0218  177 TYR A C   
1412  O O   . TYR A 177 ? 0.4118 0.2856 0.4638 -0.0537 0.0076  0.0238  177 TYR A O   
1413  C CB  . TYR A 177 ? 0.3701 0.2427 0.4419 -0.0498 -0.0067 0.0267  177 TYR A CB  
1414  C CG  . TYR A 177 ? 0.3669 0.2377 0.4410 -0.0457 -0.0138 0.0248  177 TYR A CG  
1415  C CD1 . TYR A 177 ? 0.3886 0.2522 0.4502 -0.0469 -0.0166 0.0249  177 TYR A CD1 
1416  C CD2 . TYR A 177 ? 0.3714 0.2484 0.4605 -0.0409 -0.0173 0.0227  177 TYR A CD2 
1417  C CE1 . TYR A 177 ? 0.4082 0.2710 0.4733 -0.0436 -0.0233 0.0231  177 TYR A CE1 
1418  C CE2 . TYR A 177 ? 0.3736 0.2505 0.4666 -0.0375 -0.0232 0.0209  177 TYR A CE2 
1419  C CZ  . TYR A 177 ? 0.3871 0.2572 0.4689 -0.0390 -0.0264 0.0212  177 TYR A CZ  
1420  O OH  . TYR A 177 ? 0.3806 0.2511 0.4673 -0.0361 -0.0325 0.0195  177 TYR A OH  
1421  N N   . MET A 178 ? 0.3653 0.2508 0.4388 -0.0455 0.0044  0.0181  178 MET A N   
1422  C CA  . MET A 178 ? 0.4117 0.2923 0.4750 -0.0455 0.0037  0.0163  178 MET A CA  
1423  C C   . MET A 178 ? 0.4127 0.2955 0.4689 -0.0471 0.0132  0.0144  178 MET A C   
1424  O O   . MET A 178 ? 0.4377 0.3302 0.5043 -0.0456 0.0198  0.0126  178 MET A O   
1425  C CB  . MET A 178 ? 0.4180 0.3039 0.4927 -0.0409 0.0006  0.0129  178 MET A CB  
1426  C CG  . MET A 178 ? 0.4264 0.3080 0.4930 -0.0406 -0.0004 0.0103  178 MET A CG  
1427  S SD  . MET A 178 ? 0.4445 0.3312 0.5255 -0.0363 -0.0060 0.0076  178 MET A SD  
1428  C CE  . MET A 178 ? 0.4242 0.3075 0.5103 -0.0354 -0.0166 0.0103  178 MET A CE  
1429  N N   . ASP A 179 ? 0.4155 0.2891 0.4543 -0.0498 0.0134  0.0146  179 ASP A N   
1430  C CA  . ASP A 179 ? 0.4795 0.3544 0.5108 -0.0505 0.0220  0.0118  179 ASP A CA  
1431  C C   . ASP A 179 ? 0.4587 0.3384 0.4981 -0.0461 0.0225  0.0070  179 ASP A C   
1432  O O   . ASP A 179 ? 0.4435 0.3181 0.4808 -0.0448 0.0153  0.0059  179 ASP A O   
1433  C CB  . ASP A 179 ? 0.5195 0.3820 0.5283 -0.0541 0.0216  0.0127  179 ASP A CB  
1434  C CG  . ASP A 179 ? 0.5739 0.4378 0.5739 -0.0552 0.0324  0.0100  179 ASP A CG  
1435  O OD1 . ASP A 179 ? 0.5731 0.4398 0.5708 -0.0583 0.0399  0.0122  179 ASP A OD1 
1436  O OD2 . ASP A 179 ? 0.6409 0.5036 0.6376 -0.0528 0.0334  0.0057  179 ASP A OD2 
1437  N N   . GLU A 180 ? 0.4259 0.3153 0.4751 -0.0439 0.0305  0.0043  180 GLU A N   
1438  C CA  . GLU A 180 ? 0.4424 0.3354 0.4984 -0.0399 0.0314  0.0000  180 GLU A CA  
1439  C C   . GLU A 180 ? 0.4513 0.3424 0.4975 -0.0398 0.0390  -0.0036 180 GLU A C   
1440  O O   . GLU A 180 ? 0.4498 0.3443 0.5022 -0.0364 0.0414  -0.0074 180 GLU A O   
1441  C CB  . GLU A 180 ? 0.4301 0.3348 0.5057 -0.0365 0.0332  -0.0007 180 GLU A CB  
1442  C CG  . GLU A 180 ? 0.4044 0.3110 0.4908 -0.0349 0.0255  0.0010  180 GLU A CG  
1443  C CD  . GLU A 180 ? 0.4235 0.3401 0.5262 -0.0311 0.0276  -0.0005 180 GLU A CD  
1444  O OE1 . GLU A 180 ? 0.4239 0.3450 0.5292 -0.0296 0.0341  -0.0029 180 GLU A OE1 
1445  O OE2 . GLU A 180 ? 0.4021 0.3217 0.5146 -0.0294 0.0229  0.0005  180 GLU A OE2 
1446  N N   . SER A 181 ? 0.4556 0.3402 0.4855 -0.0435 0.0426  -0.0025 181 SER A N   
1447  C CA  . SER A 181 ? 0.4666 0.3511 0.4883 -0.0434 0.0519  -0.0058 181 SER A CA  
1448  C C   . SER A 181 ? 0.4740 0.3487 0.4827 -0.0423 0.0491  -0.0099 181 SER A C   
1449  O O   . SER A 181 ? 0.4623 0.3367 0.4661 -0.0406 0.0561  -0.0140 181 SER A O   
1450  C CB  . SER A 181 ? 0.4699 0.3521 0.4795 -0.0480 0.0581  -0.0031 181 SER A CB  
1451  O OG  . SER A 181 ? 0.5023 0.3713 0.4930 -0.0515 0.0519  -0.0008 181 SER A OG  
1452  N N   . ILE A 182 ? 0.4974 0.3640 0.5012 -0.0429 0.0387  -0.0088 182 ILE A N   
1453  C CA  . ILE A 182 ? 0.4871 0.3441 0.4800 -0.0421 0.0345  -0.0126 182 ILE A CA  
1454  C C   . ILE A 182 ? 0.4718 0.3345 0.4794 -0.0376 0.0346  -0.0166 182 ILE A C   
1455  O O   . ILE A 182 ? 0.4910 0.3471 0.4910 -0.0365 0.0340  -0.0209 182 ILE A O   
1456  C CB  . ILE A 182 ? 0.4921 0.3394 0.4770 -0.0444 0.0226  -0.0100 182 ILE A CB  
1457  C CG1 . ILE A 182 ? 0.4832 0.3377 0.4879 -0.0425 0.0154  -0.0078 182 ILE A CG1 
1458  C CG2 . ILE A 182 ? 0.5090 0.3486 0.4770 -0.0489 0.0222  -0.0058 182 ILE A CG2 
1459  C CD1 . ILE A 182 ? 0.5070 0.3546 0.5076 -0.0445 0.0042  -0.0044 182 ILE A CD1 
1460  N N   . PHE A 183 ? 0.4583 0.3322 0.4858 -0.0354 0.0350  -0.0151 183 PHE A N   
1461  C CA  . PHE A 183 ? 0.4381 0.3173 0.4797 -0.0314 0.0350  -0.0180 183 PHE A CA  
1462  C C   . PHE A 183 ? 0.4274 0.3124 0.4728 -0.0286 0.0450  -0.0213 183 PHE A C   
1463  O O   . PHE A 183 ? 0.4149 0.3022 0.4553 -0.0298 0.0522  -0.0208 183 PHE A O   
1464  C CB  . PHE A 183 ? 0.4212 0.3092 0.4808 -0.0302 0.0309  -0.0148 183 PHE A CB  
1465  C CG  . PHE A 183 ? 0.4250 0.3084 0.4831 -0.0323 0.0212  -0.0119 183 PHE A CG  
1466  C CD1 . PHE A 183 ? 0.4254 0.3038 0.4836 -0.0320 0.0138  -0.0133 183 PHE A CD1 
1467  C CD2 . PHE A 183 ? 0.4477 0.3320 0.5053 -0.0344 0.0191  -0.0077 183 PHE A CD2 
1468  C CE1 . PHE A 183 ? 0.4207 0.2959 0.4793 -0.0336 0.0047  -0.0107 183 PHE A CE1 
1469  C CE2 . PHE A 183 ? 0.4485 0.3286 0.5057 -0.0357 0.0099  -0.0052 183 PHE A CE2 
1470  C CZ  . PHE A 183 ? 0.4329 0.3089 0.4911 -0.0351 0.0028  -0.0067 183 PHE A CZ  
1471  N N   . ASP A 184 ? 0.4308 0.3180 0.4854 -0.0249 0.0455  -0.0244 184 ASP A N   
1472  C CA  . ASP A 184 ? 0.4259 0.3176 0.4844 -0.0215 0.0542  -0.0281 184 ASP A CA  
1473  C C   . ASP A 184 ? 0.4176 0.3224 0.4941 -0.0194 0.0580  -0.0259 184 ASP A C   
1474  O O   . ASP A 184 ? 0.4208 0.3316 0.5021 -0.0170 0.0656  -0.0279 184 ASP A O   
1475  C CB  . ASP A 184 ? 0.4007 0.2869 0.4595 -0.0184 0.0527  -0.0326 184 ASP A CB  
1476  C CG  . ASP A 184 ? 0.4300 0.3024 0.4709 -0.0206 0.0481  -0.0352 184 ASP A CG  
1477  O OD1 . ASP A 184 ? 0.4268 0.2942 0.4521 -0.0227 0.0517  -0.0359 184 ASP A OD1 
1478  O OD2 . ASP A 184 ? 0.4328 0.2998 0.4754 -0.0206 0.0407  -0.0361 184 ASP A OD2 
1479  N N   . VAL A 185 ? 0.4101 0.3193 0.4971 -0.0199 0.0522  -0.0222 185 VAL A N   
1480  C CA  . VAL A 185 ? 0.4022 0.3228 0.5047 -0.0183 0.0545  -0.0200 185 VAL A CA  
1481  C C   . VAL A 185 ? 0.3708 0.2931 0.4758 -0.0211 0.0493  -0.0155 185 VAL A C   
1482  O O   . VAL A 185 ? 0.3532 0.2689 0.4518 -0.0232 0.0429  -0.0143 185 VAL A O   
1483  C CB  . VAL A 185 ? 0.4234 0.3485 0.5393 -0.0140 0.0541  -0.0214 185 VAL A CB  
1484  C CG1 . VAL A 185 ? 0.4297 0.3493 0.5416 -0.0111 0.0566  -0.0261 185 VAL A CG1 
1485  C CG2 . VAL A 185 ? 0.4348 0.3599 0.5574 -0.0142 0.0468  -0.0189 185 VAL A CG2 
1486  N N   . TYR A 186 ? 0.3707 0.3017 0.4850 -0.0211 0.0521  -0.0133 186 TYR A N   
1487  C CA  . TYR A 186 ? 0.3636 0.2963 0.4808 -0.0235 0.0478  -0.0093 186 TYR A CA  
1488  C C   . TYR A 186 ? 0.3509 0.2885 0.4811 -0.0207 0.0439  -0.0087 186 TYR A C   
1489  O O   . TYR A 186 ? 0.3978 0.3403 0.5363 -0.0175 0.0466  -0.0104 186 TYR A O   
1490  C CB  . TYR A 186 ? 0.3581 0.2965 0.4775 -0.0257 0.0524  -0.0072 186 TYR A CB  
1491  C CG  . TYR A 186 ? 0.3525 0.2873 0.4594 -0.0289 0.0580  -0.0075 186 TYR A CG  
1492  C CD1 . TYR A 186 ? 0.3782 0.3026 0.4693 -0.0321 0.0550  -0.0065 186 TYR A CD1 
1493  C CD2 . TYR A 186 ? 0.3442 0.2860 0.4550 -0.0286 0.0664  -0.0087 186 TYR A CD2 
1494  C CE1 . TYR A 186 ? 0.4129 0.3333 0.4908 -0.0352 0.0606  -0.0066 186 TYR A CE1 
1495  C CE2 . TYR A 186 ? 0.3515 0.2905 0.4507 -0.0316 0.0727  -0.0090 186 TYR A CE2 
1496  C CZ  . TYR A 186 ? 0.3814 0.3093 0.4632 -0.0350 0.0699  -0.0078 186 TYR A CZ  
1497  O OH  . TYR A 186 ? 0.3798 0.3039 0.4480 -0.0382 0.0762  -0.0079 186 TYR A OH  
1498  N N   . ALA A 187 ? 0.3351 0.2709 0.4664 -0.0218 0.0376  -0.0064 187 ALA A N   
1499  C CA  . ALA A 187 ? 0.3328 0.2724 0.4748 -0.0193 0.0339  -0.0058 187 ALA A CA  
1500  C C   . ALA A 187 ? 0.3325 0.2724 0.4768 -0.0206 0.0290  -0.0030 187 ALA A C   
1501  O O   . ALA A 187 ? 0.3541 0.2880 0.4905 -0.0231 0.0254  -0.0018 187 ALA A O   
1502  C CB  . ALA A 187 ? 0.3372 0.2721 0.4777 -0.0183 0.0309  -0.0076 187 ALA A CB  
1503  N N   . TYR A 188 ? 0.2979 0.2439 0.4524 -0.0187 0.0283  -0.0022 188 TYR A N   
1504  C CA  . TYR A 188 ? 0.3135 0.2595 0.4712 -0.0188 0.0235  -0.0003 188 TYR A CA  
1505  C C   . TYR A 188 ? 0.3166 0.2677 0.4843 -0.0158 0.0226  -0.0006 188 TYR A C   
1506  O O   . TYR A 188 ? 0.3444 0.2999 0.5169 -0.0139 0.0259  -0.0014 188 TYR A O   
1507  C CB  . TYR A 188 ? 0.3042 0.2515 0.4620 -0.0205 0.0237  0.0015  188 TYR A CB  
1508  C CG  . TYR A 188 ? 0.3061 0.2486 0.4540 -0.0242 0.0252  0.0026  188 TYR A CG  
1509  C CD1 . TYR A 188 ? 0.3108 0.2454 0.4499 -0.0264 0.0207  0.0040  188 TYR A CD1 
1510  C CD2 . TYR A 188 ? 0.3055 0.2514 0.4528 -0.0255 0.0311  0.0024  188 TYR A CD2 
1511  C CE1 . TYR A 188 ? 0.3308 0.2601 0.4591 -0.0302 0.0221  0.0054  188 TYR A CE1 
1512  C CE2 . TYR A 188 ? 0.3233 0.2650 0.4610 -0.0294 0.0333  0.0037  188 TYR A CE2 
1513  C CZ  . TYR A 188 ? 0.3319 0.2647 0.4592 -0.0318 0.0289  0.0053  188 TYR A CZ  
1514  O OH  . TYR A 188 ? 0.3505 0.2783 0.4668 -0.0359 0.0311  0.0070  188 TYR A OH  
1515  N N   . ASN A 189 ? 0.3183 0.2685 0.4888 -0.0152 0.0181  0.0001  189 ASN A N   
1516  C CA  . ASN A 189 ? 0.3352 0.2904 0.5142 -0.0127 0.0175  0.0003  189 ASN A CA  
1517  C C   . ASN A 189 ? 0.3032 0.2604 0.4835 -0.0127 0.0176  0.0011  189 ASN A C   
1518  O O   . ASN A 189 ? 0.3115 0.2651 0.4881 -0.0143 0.0150  0.0021  189 ASN A O   
1519  C CB  . ASN A 189 ? 0.3115 0.2659 0.4940 -0.0119 0.0132  0.0005  189 ASN A CB  
1520  C CG  . ASN A 189 ? 0.3239 0.2756 0.5052 -0.0128 0.0120  -0.0002 189 ASN A CG  
1521  O OD1 . ASN A 189 ? 0.3414 0.2935 0.5225 -0.0125 0.0150  -0.0011 189 ASN A OD1 
1522  N ND2 . ASN A 189 ? 0.3439 0.2921 0.5241 -0.0138 0.0071  0.0000  189 ASN A ND2 
1523  N N   . CYS A 190 ? 0.2798 0.2421 0.4651 -0.0108 0.0200  0.0008  190 CYS A N   
1524  C CA  . CYS A 190 ? 0.2708 0.2350 0.4571 -0.0112 0.0204  0.0013  190 CYS A CA  
1525  C C   . CYS A 190 ? 0.2530 0.2202 0.4443 -0.0085 0.0192  0.0009  190 CYS A C   
1526  O O   . CYS A 190 ? 0.2630 0.2336 0.4575 -0.0064 0.0211  0.0005  190 CYS A O   
1527  C CB  . CYS A 190 ? 0.2744 0.2420 0.4615 -0.0117 0.0243  0.0010  190 CYS A CB  
1528  S SG  . CYS A 190 ? 0.3069 0.2713 0.4872 -0.0145 0.0272  0.0009  190 CYS A SG  
1529  N N   . TYR A 191 ? 0.2519 0.2172 0.4432 -0.0085 0.0162  0.0010  191 TYR A N   
1530  C CA  . TYR A 191 ? 0.2536 0.2209 0.4482 -0.0058 0.0153  0.0002  191 TYR A CA  
1531  C C   . TYR A 191 ? 0.2673 0.2335 0.4612 -0.0066 0.0136  0.0001  191 TYR A C   
1532  O O   . TYR A 191 ? 0.2764 0.2386 0.4675 -0.0091 0.0116  0.0009  191 TYR A O   
1533  C CB  . TYR A 191 ? 0.2685 0.2343 0.4648 -0.0041 0.0130  -0.0003 191 TYR A CB  
1534  C CG  . TYR A 191 ? 0.2508 0.2188 0.4497 -0.0032 0.0146  -0.0003 191 TYR A CG  
1535  C CD1 . TYR A 191 ? 0.2653 0.2374 0.4672 -0.0010 0.0173  -0.0006 191 TYR A CD1 
1536  C CD2 . TYR A 191 ? 0.2299 0.1955 0.4277 -0.0048 0.0132  0.0002  191 TYR A CD2 
1537  C CE1 . TYR A 191 ? 0.2536 0.2275 0.4582 -0.0008 0.0189  -0.0002 191 TYR A CE1 
1538  C CE2 . TYR A 191 ? 0.2545 0.2219 0.4552 -0.0044 0.0144  0.0002  191 TYR A CE2 
1539  C CZ  . TYR A 191 ? 0.2513 0.2229 0.4558 -0.0025 0.0173  0.0001  191 TYR A CZ  
1540  O OH  . TYR A 191 ? 0.2785 0.2517 0.4863 -0.0026 0.0185  0.0004  191 TYR A OH  
1541  N N   . ASP A 192 ? 0.2581 0.2272 0.4539 -0.0046 0.0141  -0.0008 192 ASP A N   
1542  C CA  . ASP A 192 ? 0.2765 0.2448 0.4720 -0.0054 0.0121  -0.0012 192 ASP A CA  
1543  C C   . ASP A 192 ? 0.2674 0.2334 0.4623 -0.0027 0.0098  -0.0029 192 ASP A C   
1544  O O   . ASP A 192 ? 0.2637 0.2321 0.4589 -0.0001 0.0107  -0.0040 192 ASP A O   
1545  C CB  . ASP A 192 ? 0.2959 0.2687 0.4935 -0.0054 0.0137  -0.0011 192 ASP A CB  
1546  C CG  . ASP A 192 ? 0.3104 0.2828 0.5086 -0.0067 0.0111  -0.0016 192 ASP A CG  
1547  O OD1 . ASP A 192 ? 0.3193 0.2871 0.5157 -0.0078 0.0081  -0.0020 192 ASP A OD1 
1548  O OD2 . ASP A 192 ? 0.3113 0.2878 0.5121 -0.0064 0.0116  -0.0016 192 ASP A OD2 
1549  N N   . HIS A 193 ? 0.2531 0.2141 0.4467 -0.0031 0.0067  -0.0032 193 HIS A N   
1550  C CA  . HIS A 193 ? 0.2688 0.2270 0.4621 0.0000  0.0046  -0.0054 193 HIS A CA  
1551  C C   . HIS A 193 ? 0.2805 0.2337 0.4717 -0.0014 0.0009  -0.0062 193 HIS A C   
1552  O O   . HIS A 193 ? 0.3088 0.2581 0.4990 0.0011  -0.0015 -0.0083 193 HIS A O   
1553  C CB  . HIS A 193 ? 0.2818 0.2378 0.4765 0.0016  0.0033  -0.0056 193 HIS A CB  
1554  C CG  . HIS A 193 ? 0.3056 0.2661 0.5032 0.0026  0.0062  -0.0050 193 HIS A CG  
1555  N ND1 . HIS A 193 ? 0.3190 0.2847 0.5184 0.0046  0.0099  -0.0054 193 HIS A ND1 
1556  C CD2 . HIS A 193 ? 0.3064 0.2659 0.5051 0.0015  0.0053  -0.0038 193 HIS A CD2 
1557  C CE1 . HIS A 193 ? 0.2975 0.2654 0.4998 0.0045  0.0112  -0.0045 193 HIS A CE1 
1558  N NE2 . HIS A 193 ? 0.3145 0.2789 0.5165 0.0027  0.0083  -0.0037 193 HIS A NE2 
1559  N N   . ASN A 194 ? 0.2719 0.2252 0.4628 -0.0055 0.0005  -0.0045 194 ASN A N   
1560  C CA  . ASN A 194 ? 0.2767 0.2259 0.4666 -0.0079 -0.0030 -0.0047 194 ASN A CA  
1561  C C   . ASN A 194 ? 0.2816 0.2224 0.4692 -0.0081 -0.0069 -0.0050 194 ASN A C   
1562  O O   . ASN A 194 ? 0.2607 0.1970 0.4470 -0.0059 -0.0100 -0.0074 194 ASN A O   
1563  C CB  . ASN A 194 ? 0.2976 0.2485 0.4874 -0.0060 -0.0038 -0.0070 194 ASN A CB  
1564  C CG  . ASN A 194 ? 0.3248 0.2717 0.5142 -0.0091 -0.0080 -0.0074 194 ASN A CG  
1565  O OD1 . ASN A 194 ? 0.3202 0.2655 0.5108 -0.0137 -0.0088 -0.0052 194 ASN A OD1 
1566  N ND2 . ASN A 194 ? 0.3296 0.2745 0.5168 -0.0069 -0.0105 -0.0101 194 ASN A ND2 
1567  N N   . GLU A 195 ? 0.2761 0.2146 0.4627 -0.0103 -0.0070 -0.0026 195 GLU A N   
1568  C CA  . GLU A 195 ? 0.2879 0.2183 0.4722 -0.0103 -0.0110 -0.0021 195 GLU A CA  
1569  C C   . GLU A 195 ? 0.2935 0.2217 0.4748 -0.0148 -0.0106 0.0015  195 GLU A C   
1570  O O   . GLU A 195 ? 0.2884 0.2221 0.4700 -0.0162 -0.0067 0.0027  195 GLU A O   
1571  C CB  . GLU A 195 ? 0.2696 0.1997 0.4557 -0.0050 -0.0117 -0.0042 195 GLU A CB  
1572  C CG  . GLU A 195 ? 0.2648 0.2010 0.4530 -0.0040 -0.0083 -0.0033 195 GLU A CG  
1573  C CD  . GLU A 195 ? 0.2643 0.2017 0.4562 0.0007  -0.0088 -0.0050 195 GLU A CD  
1574  O OE1 . GLU A 195 ? 0.2523 0.1858 0.4451 0.0038  -0.0114 -0.0072 195 GLU A OE1 
1575  O OE2 . GLU A 195 ? 0.2620 0.2042 0.4563 0.0012  -0.0064 -0.0043 195 GLU A OE2 
1576  N N   . GLY A 196 ? 0.3216 0.2411 0.4995 -0.0171 -0.0148 0.0031  196 GLY A N   
1577  C CA  . GLY A 196 ? 0.3275 0.2430 0.5005 -0.0221 -0.0148 0.0069  196 GLY A CA  
1578  C C   . GLY A 196 ? 0.3345 0.2562 0.5079 -0.0265 -0.0099 0.0085  196 GLY A C   
1579  O O   . GLY A 196 ? 0.3170 0.2410 0.4933 -0.0285 -0.0093 0.0081  196 GLY A O   
1580  N N   . GLN A 197 ? 0.3529 0.2774 0.5238 -0.0277 -0.0064 0.0099  197 GLN A N   
1581  C CA  . GLN A 197 ? 0.3219 0.2522 0.4930 -0.0315 -0.0011 0.0113  197 GLN A CA  
1582  C C   . GLN A 197 ? 0.2980 0.2374 0.4764 -0.0295 0.0018  0.0090  197 GLN A C   
1583  O O   . GLN A 197 ? 0.2896 0.2330 0.4708 -0.0330 0.0043  0.0099  197 GLN A O   
1584  C CB  . GLN A 197 ? 0.3116 0.2429 0.4781 -0.0318 0.0022  0.0122  197 GLN A CB  
1585  C CG  . GLN A 197 ? 0.3141 0.2358 0.4716 -0.0347 -0.0007 0.0150  197 GLN A CG  
1586  C CD  . GLN A 197 ? 0.3015 0.2190 0.4581 -0.0306 -0.0055 0.0141  197 GLN A CD  
1587  O OE1 . GLN A 197 ? 0.2859 0.2032 0.4475 -0.0268 -0.0088 0.0121  197 GLN A OE1 
1588  N NE2 . GLN A 197 ? 0.3065 0.2217 0.4573 -0.0311 -0.0053 0.0150  197 GLN A NE2 
1589  N N   . THR A 198 ? 0.2803 0.2231 0.4621 -0.0244 0.0014  0.0063  198 THR A N   
1590  C CA  . THR A 198 ? 0.2974 0.2482 0.4848 -0.0225 0.0039  0.0046  198 THR A CA  
1591  C C   . THR A 198 ? 0.2891 0.2387 0.4790 -0.0228 0.0006  0.0035  198 THR A C   
1592  O O   . THR A 198 ? 0.2869 0.2424 0.4811 -0.0225 0.0018  0.0026  198 THR A O   
1593  C CB  . THR A 198 ? 0.2904 0.2452 0.4795 -0.0175 0.0054  0.0026  198 THR A CB  
1594  O OG1 . THR A 198 ? 0.3539 0.3044 0.5421 -0.0143 0.0020  0.0011  198 THR A OG1 
1595  C CG2 . THR A 198 ? 0.2781 0.2340 0.4653 -0.0174 0.0083  0.0034  198 THR A CG2 
1596  N N   . ALA A 199 ? 0.2829 0.2244 0.4699 -0.0231 -0.0040 0.0033  199 ALA A N   
1597  C CA  . ALA A 199 ? 0.3001 0.2387 0.4884 -0.0239 -0.0078 0.0020  199 ALA A CA  
1598  C C   . ALA A 199 ? 0.2914 0.2294 0.4811 -0.0303 -0.0081 0.0046  199 ALA A C   
1599  O O   . ALA A 199 ? 0.3031 0.2429 0.4965 -0.0318 -0.0098 0.0037  199 ALA A O   
1600  C CB  . ALA A 199 ? 0.3104 0.2399 0.4953 -0.0214 -0.0128 0.0004  199 ALA A CB  
1601  N N   . THR A 200 ? 0.2893 0.2246 0.4758 -0.0343 -0.0064 0.0077  200 THR A N   
1602  C CA  . THR A 200 ? 0.3062 0.2404 0.4935 -0.0410 -0.0060 0.0107  200 THR A CA  
1603  C C   . THR A 200 ? 0.3106 0.2560 0.5040 -0.0429 -0.0003 0.0112  200 THR A C   
1604  O O   . THR A 200 ? 0.3217 0.2715 0.5214 -0.0461 -0.0004 0.0115  200 THR A O   
1605  C CB  . THR A 200 ? 0.3232 0.2492 0.5030 -0.0445 -0.0063 0.0141  200 THR A CB  
1606  O OG1 . THR A 200 ? 0.3079 0.2362 0.4841 -0.0422 -0.0028 0.0143  200 THR A OG1 
1607  C CG2 . THR A 200 ? 0.3456 0.2597 0.5209 -0.0435 -0.0129 0.0140  200 THR A CG2 
1608  N N   . MET A 201 ? 0.2978 0.2478 0.4898 -0.0408 0.0045  0.0112  201 MET A N   
1609  C CA  . MET A 201 ? 0.2981 0.2575 0.4948 -0.0424 0.0105  0.0118  201 MET A CA  
1610  C C   . MET A 201 ? 0.2799 0.2478 0.4836 -0.0378 0.0113  0.0091  201 MET A C   
1611  O O   . MET A 201 ? 0.2653 0.2417 0.4761 -0.0389 0.0146  0.0092  201 MET A O   
1612  C CB  . MET A 201 ? 0.3203 0.2784 0.5105 -0.0430 0.0149  0.0132  201 MET A CB  
1613  C CG  . MET A 201 ? 0.3265 0.2774 0.5099 -0.0489 0.0150  0.0168  201 MET A CG  
1614  S SD  . MET A 201 ? 0.3439 0.2895 0.5157 -0.0496 0.0181  0.0184  201 MET A SD  
1615  C CE  . MET A 201 ? 0.3657 0.3011 0.5318 -0.0455 0.0105  0.0176  201 MET A CE  
1616  N N   . GLY A 202 ? 0.2757 0.2411 0.4775 -0.0328 0.0082  0.0069  202 GLY A N   
1617  C CA  . GLY A 202 ? 0.2509 0.2226 0.4566 -0.0281 0.0094  0.0048  202 GLY A CA  
1618  C C   . GLY A 202 ? 0.2476 0.2215 0.4512 -0.0260 0.0139  0.0049  202 GLY A C   
1619  O O   . GLY A 202 ? 0.2575 0.2294 0.4574 -0.0287 0.0165  0.0064  202 GLY A O   
1620  N N   . PHE A 203 ? 0.2637 0.2408 0.4685 -0.0214 0.0146  0.0033  203 PHE A N   
1621  C CA  . PHE A 203 ? 0.2564 0.2337 0.4586 -0.0193 0.0178  0.0031  203 PHE A CA  
1622  C C   . PHE A 203 ? 0.2599 0.2423 0.4646 -0.0209 0.0228  0.0037  203 PHE A C   
1623  O O   . PHE A 203 ? 0.2763 0.2562 0.4764 -0.0225 0.0254  0.0044  203 PHE A O   
1624  C CB  . PHE A 203 ? 0.2752 0.2543 0.4786 -0.0146 0.0172  0.0016  203 PHE A CB  
1625  C CG  . PHE A 203 ? 0.2513 0.2295 0.4521 -0.0123 0.0194  0.0014  203 PHE A CG  
1626  C CD1 . PHE A 203 ? 0.2392 0.2124 0.4352 -0.0134 0.0190  0.0019  203 PHE A CD1 
1627  C CD2 . PHE A 203 ? 0.2542 0.2360 0.4575 -0.0092 0.0212  0.0008  203 PHE A CD2 
1628  C CE1 . PHE A 203 ? 0.2538 0.2263 0.4483 -0.0115 0.0202  0.0015  203 PHE A CE1 
1629  C CE2 . PHE A 203 ? 0.2394 0.2199 0.4408 -0.0076 0.0228  0.0006  203 PHE A CE2 
1630  C CZ  . PHE A 203 ? 0.2422 0.2183 0.4396 -0.0089 0.0223  0.0009  203 PHE A CZ  
1631  N N   . LYS A 204 ? 0.2719 0.2613 0.4840 -0.0202 0.0240  0.0032  204 LYS A N   
1632  C CA  . LYS A 204 ? 0.2741 0.2693 0.4904 -0.0214 0.0291  0.0034  204 LYS A CA  
1633  C C   . LYS A 204 ? 0.3018 0.2949 0.5144 -0.0264 0.0318  0.0050  204 LYS A C   
1634  O O   . LYS A 204 ? 0.3455 0.3375 0.5537 -0.0268 0.0360  0.0049  204 LYS A O   
1635  C CB  . LYS A 204 ? 0.2461 0.2495 0.4727 -0.0211 0.0289  0.0030  204 LYS A CB  
1636  C CG  . LYS A 204 ? 0.2484 0.2591 0.4813 -0.0221 0.0346  0.0030  204 LYS A CG  
1637  C CD  . LYS A 204 ? 0.2402 0.2598 0.4852 -0.0231 0.0340  0.0030  204 LYS A CD  
1638  C CE  . LYS A 204 ? 0.2352 0.2623 0.4869 -0.0248 0.0404  0.0030  204 LYS A CE  
1639  N NZ  . LYS A 204 ? 0.2337 0.2705 0.4991 -0.0260 0.0395  0.0032  204 LYS A NZ  
1640  N N   . ASP A 205 ? 0.3299 0.3217 0.5435 -0.0305 0.0295  0.0064  205 ASP A N   
1641  C CA  . ASP A 205 ? 0.3078 0.2983 0.5186 -0.0359 0.0327  0.0085  205 ASP A CA  
1642  C C   . ASP A 205 ? 0.2914 0.2723 0.4902 -0.0369 0.0322  0.0096  205 ASP A C   
1643  O O   . ASP A 205 ? 0.3011 0.2805 0.4946 -0.0401 0.0364  0.0109  205 ASP A O   
1644  C CB  . ASP A 205 ? 0.3092 0.3011 0.5254 -0.0404 0.0304  0.0101  205 ASP A CB  
1645  C CG  . ASP A 205 ? 0.3228 0.3256 0.5518 -0.0406 0.0321  0.0094  205 ASP A CG  
1646  O OD1 . ASP A 205 ? 0.3153 0.3241 0.5487 -0.0364 0.0348  0.0076  205 ASP A OD1 
1647  O OD2 . ASP A 205 ? 0.3532 0.3583 0.5881 -0.0450 0.0306  0.0108  205 ASP A OD2 
1648  N N   . TYR A 206 ? 0.2968 0.2715 0.4912 -0.0341 0.0274  0.0089  206 TYR A N   
1649  C CA  . TYR A 206 ? 0.3050 0.2710 0.4893 -0.0349 0.0260  0.0100  206 TYR A CA  
1650  C C   . TYR A 206 ? 0.3108 0.2777 0.4910 -0.0336 0.0305  0.0091  206 TYR A C   
1651  O O   . TYR A 206 ? 0.3282 0.2912 0.5006 -0.0367 0.0330  0.0105  206 TYR A O   
1652  C CB  . TYR A 206 ? 0.2997 0.2602 0.4823 -0.0317 0.0200  0.0092  206 TYR A CB  
1653  C CG  . TYR A 206 ? 0.2892 0.2413 0.4628 -0.0320 0.0177  0.0102  206 TYR A CG  
1654  C CD1 . TYR A 206 ? 0.3035 0.2492 0.4696 -0.0366 0.0175  0.0128  206 TYR A CD1 
1655  C CD2 . TYR A 206 ? 0.3022 0.2531 0.4753 -0.0279 0.0157  0.0087  206 TYR A CD2 
1656  C CE1 . TYR A 206 ? 0.3286 0.2662 0.4862 -0.0367 0.0145  0.0139  206 TYR A CE1 
1657  C CE2 . TYR A 206 ? 0.3386 0.2825 0.5048 -0.0281 0.0129  0.0095  206 TYR A CE2 
1658  C CZ  . TYR A 206 ? 0.3625 0.2994 0.5208 -0.0324 0.0118  0.0121  206 TYR A CZ  
1659  O OH  . TYR A 206 ? 0.3976 0.3270 0.5487 -0.0325 0.0079  0.0131  206 TYR A OH  
1660  N N   . ILE A 207 ? 0.3237 0.2952 0.5083 -0.0292 0.0316  0.0069  207 ILE A N   
1661  C CA  . ILE A 207 ? 0.3080 0.2789 0.4885 -0.0275 0.0348  0.0056  207 ILE A CA  
1662  C C   . ILE A 207 ? 0.3139 0.2891 0.4947 -0.0297 0.0413  0.0055  207 ILE A C   
1663  O O   . ILE A 207 ? 0.3373 0.3088 0.5101 -0.0308 0.0443  0.0052  207 ILE A O   
1664  C CB  . ILE A 207 ? 0.3091 0.2831 0.4946 -0.0225 0.0341  0.0036  207 ILE A CB  
1665  C CG1 . ILE A 207 ? 0.2944 0.2649 0.4799 -0.0207 0.0286  0.0037  207 ILE A CG1 
1666  C CG2 . ILE A 207 ? 0.3121 0.2847 0.4936 -0.0210 0.0371  0.0020  207 ILE A CG2 
1667  C CD1 . ILE A 207 ? 0.3101 0.2730 0.4879 -0.0217 0.0255  0.0044  207 ILE A CD1 
1668  N N   . LYS A 208 ? 0.3369 0.3198 0.5268 -0.0305 0.0435  0.0056  208 LYS A N   
1669  C CA  . LYS A 208 ? 0.3516 0.3402 0.5441 -0.0325 0.0503  0.0055  208 LYS A CA  
1670  C C   . LYS A 208 ? 0.3590 0.3423 0.5420 -0.0382 0.0526  0.0079  208 LYS A C   
1671  O O   . LYS A 208 ? 0.3508 0.3344 0.5288 -0.0395 0.0586  0.0074  208 LYS A O   
1672  C CB  . LYS A 208 ? 0.3529 0.3512 0.5588 -0.0326 0.0509  0.0055  208 LYS A CB  
1673  C CG  . LYS A 208 ? 0.3902 0.3967 0.6022 -0.0351 0.0580  0.0055  208 LYS A CG  
1674  C CD  . LYS A 208 ? 0.4046 0.4215 0.6320 -0.0343 0.0572  0.0051  208 LYS A CD  
1675  C CE  . LYS A 208 ? 0.4779 0.5038 0.7136 -0.0380 0.0634  0.0058  208 LYS A CE  
1676  N NZ  . LYS A 208 ? 0.4785 0.5030 0.7143 -0.0445 0.0618  0.0090  208 LYS A NZ  
1677  N N   . GLY A 209 ? 0.3701 0.3480 0.5503 -0.0414 0.0477  0.0104  209 GLY A N   
1678  C CA  . GLY A 209 ? 0.3717 0.3429 0.5419 -0.0469 0.0487  0.0134  209 GLY A CA  
1679  C C   . GLY A 209 ? 0.3746 0.3376 0.5311 -0.0465 0.0495  0.0130  209 GLY A C   
1680  O O   . GLY A 209 ? 0.3889 0.3492 0.5366 -0.0502 0.0542  0.0143  209 GLY A O   
1681  N N   . LEU A 210 ? 0.3334 0.2928 0.4881 -0.0421 0.0449  0.0113  210 LEU A N   
1682  C CA  . LEU A 210 ? 0.3404 0.2918 0.4829 -0.0417 0.0442  0.0108  210 LEU A CA  
1683  C C   . LEU A 210 ? 0.3505 0.3049 0.4904 -0.0406 0.0512  0.0083  210 LEU A C   
1684  O O   . LEU A 210 ? 0.3784 0.3263 0.5058 -0.0423 0.0529  0.0083  210 LEU A O   
1685  C CB  . LEU A 210 ? 0.3295 0.2777 0.4733 -0.0376 0.0377  0.0095  210 LEU A CB  
1686  C CG  . LEU A 210 ? 0.3060 0.2497 0.4508 -0.0381 0.0307  0.0115  210 LEU A CG  
1687  C CD1 . LEU A 210 ? 0.3020 0.2423 0.4468 -0.0343 0.0252  0.0102  210 LEU A CD1 
1688  C CD2 . LEU A 210 ? 0.2979 0.2334 0.4325 -0.0431 0.0292  0.0149  210 LEU A CD2 
1689  N N   . ASN A 211 ? 0.3589 0.3228 0.5102 -0.0374 0.0547  0.0059  211 ASN A N   
1690  C CA  . ASN A 211 ? 0.3561 0.3237 0.5073 -0.0355 0.0615  0.0031  211 ASN A CA  
1691  C C   . ASN A 211 ? 0.3768 0.3470 0.5246 -0.0398 0.0690  0.0041  211 ASN A C   
1692  O O   . ASN A 211 ? 0.3829 0.3508 0.5220 -0.0401 0.0745  0.0025  211 ASN A O   
1693  C CB  . ASN A 211 ? 0.3458 0.3223 0.5112 -0.0306 0.0618  0.0008  211 ASN A CB  
1694  C CG  . ASN A 211 ? 0.3537 0.3315 0.5189 -0.0268 0.0664  -0.0028 211 ASN A CG  
1695  O OD1 . ASN A 211 ? 0.3451 0.3152 0.4993 -0.0264 0.0663  -0.0042 211 ASN A OD1 
1696  N ND2 . ASN A 211 ? 0.3432 0.3303 0.5205 -0.0240 0.0699  -0.0044 211 ASN A ND2 
1697  N N   . GLU A 212 ? 0.3540 0.3288 0.5085 -0.0435 0.0693  0.0069  212 GLU A N   
1698  C CA  . GLU A 212 ? 0.3625 0.3397 0.5141 -0.0486 0.0764  0.0087  212 GLU A CA  
1699  C C   . GLU A 212 ? 0.3567 0.3219 0.4895 -0.0529 0.0761  0.0111  212 GLU A C   
1700  O O   . GLU A 212 ? 0.3607 0.3250 0.4848 -0.0552 0.0833  0.0108  212 GLU A O   
1701  C CB  . GLU A 212 ? 0.3626 0.3473 0.5266 -0.0520 0.0761  0.0113  212 GLU A CB  
1702  C CG  . GLU A 212 ? 0.3704 0.3680 0.5525 -0.0479 0.0779  0.0087  212 GLU A CG  
1703  C CD  . GLU A 212 ? 0.4049 0.4082 0.5995 -0.0503 0.0741  0.0108  212 GLU A CD  
1704  O OE1 . GLU A 212 ? 0.4517 0.4483 0.6405 -0.0550 0.0704  0.0141  212 GLU A OE1 
1705  O OE2 . GLU A 212 ? 0.4051 0.4183 0.6143 -0.0473 0.0740  0.0091  212 GLU A OE2 
1706  N N   . LEU A 213 ? 0.3924 0.3483 0.5186 -0.0540 0.0678  0.0135  213 LEU A N   
1707  C CA  . LEU A 213 ? 0.4008 0.3441 0.5088 -0.0579 0.0658  0.0161  213 LEU A CA  
1708  C C   . LEU A 213 ? 0.3897 0.3274 0.4857 -0.0553 0.0675  0.0131  213 LEU A C   
1709  O O   . LEU A 213 ? 0.3884 0.3193 0.4690 -0.0586 0.0711  0.0141  213 LEU A O   
1710  C CB  . LEU A 213 ? 0.4104 0.3458 0.5169 -0.0582 0.0556  0.0187  213 LEU A CB  
1711  C CG  . LEU A 213 ? 0.4430 0.3796 0.5566 -0.0619 0.0531  0.0222  213 LEU A CG  
1712  C CD1 . LEU A 213 ? 0.4186 0.3469 0.5307 -0.0605 0.0430  0.0235  213 LEU A CD1 
1713  C CD2 . LEU A 213 ? 0.4361 0.3699 0.5425 -0.0692 0.0578  0.0264  213 LEU A CD2 
1714  N N   . ASN A 214 ? 0.3953 0.3356 0.4979 -0.0496 0.0650  0.0094  214 ASN A N   
1715  C CA  . ASN A 214 ? 0.4003 0.3362 0.4939 -0.0468 0.0665  0.0058  214 ASN A CA  
1716  C C   . ASN A 214 ? 0.4252 0.3652 0.5153 -0.0474 0.0771  0.0036  214 ASN A C   
1717  O O   . ASN A 214 ? 0.4612 0.3940 0.5374 -0.0472 0.0790  0.0015  214 ASN A O   
1718  C CB  . ASN A 214 ? 0.3714 0.3096 0.4743 -0.0411 0.0618  0.0029  214 ASN A CB  
1719  C CG  . ASN A 214 ? 0.3749 0.3074 0.4776 -0.0407 0.0520  0.0047  214 ASN A CG  
1720  O OD1 . ASN A 214 ? 0.3773 0.3006 0.4686 -0.0437 0.0477  0.0072  214 ASN A OD1 
1721  N ND2 . ASN A 214 ? 0.3723 0.3096 0.4872 -0.0367 0.0485  0.0035  214 ASN A ND2 
1722  N N   . GLY A 215 ? 0.4166 0.3681 0.5193 -0.0480 0.0837  0.0037  215 GLY A N   
1723  C CA  . GLY A 215 ? 0.4198 0.3765 0.5206 -0.0490 0.0947  0.0019  215 GLY A CA  
1724  C C   . GLY A 215 ? 0.4367 0.4045 0.5521 -0.0433 0.1001  -0.0028 215 GLY A C   
1725  O O   . GLY A 215 ? 0.4679 0.4405 0.5828 -0.0431 0.1095  -0.0051 215 GLY A O   
1726  N N   . LEU A 216 ? 0.4379 0.4093 0.5656 -0.0384 0.0945  -0.0044 216 LEU A N   
1727  C CA  . LEU A 216 ? 0.3958 0.3775 0.5387 -0.0330 0.0982  -0.0079 216 LEU A CA  
1728  C C   . LEU A 216 ? 0.3872 0.3664 0.5228 -0.0297 0.1047  -0.0127 216 LEU A C   
1729  O O   . LEU A 216 ? 0.3744 0.3627 0.5205 -0.0266 0.1113  -0.0155 216 LEU A O   
1730  C CB  . LEU A 216 ? 0.4138 0.4086 0.5721 -0.0349 0.1031  -0.0063 216 LEU A CB  
1731  C CG  . LEU A 216 ? 0.3995 0.3971 0.5667 -0.0378 0.0964  -0.0022 216 LEU A CG  
1732  C CD1 . LEU A 216 ? 0.3974 0.4082 0.5806 -0.0397 0.1010  -0.0011 216 LEU A CD1 
1733  C CD2 . LEU A 216 ? 0.3918 0.3882 0.5654 -0.0332 0.0879  -0.0030 216 LEU A CD2 
1734  N N   . ASP A 217 ? 0.3958 0.3625 0.5146 -0.0298 0.1018  -0.0140 217 ASP A N   
1735  C CA  . ASP A 217 ? 0.4083 0.3698 0.5159 -0.0275 0.1076  -0.0186 217 ASP A CA  
1736  C C   . ASP A 217 ? 0.4178 0.3705 0.5208 -0.0234 0.1012  -0.0217 217 ASP A C   
1737  O O   . ASP A 217 ? 0.4386 0.3846 0.5308 -0.0215 0.1042  -0.0258 217 ASP A O   
1738  C CB  . ASP A 217 ? 0.4236 0.3768 0.5114 -0.0329 0.1112  -0.0172 217 ASP A CB  
1739  C CG  . ASP A 217 ? 0.4323 0.3741 0.5073 -0.0370 0.1021  -0.0132 217 ASP A CG  
1740  O OD1 . ASP A 217 ? 0.4150 0.3577 0.4986 -0.0366 0.0939  -0.0108 217 ASP A OD1 
1741  O OD2 . ASP A 217 ? 0.4885 0.4205 0.5446 -0.0404 0.1032  -0.0127 217 ASP A OD2 
1742  N N   . LYS A 218 ? 0.4379 0.3907 0.5491 -0.0222 0.0926  -0.0198 218 LYS A N   
1743  C CA  . LYS A 218 ? 0.4453 0.3922 0.5565 -0.0183 0.0870  -0.0223 218 LYS A CA  
1744  C C   . LYS A 218 ? 0.4022 0.3567 0.5311 -0.0152 0.0826  -0.0210 218 LYS A C   
1745  O O   . LYS A 218 ? 0.3977 0.3589 0.5354 -0.0168 0.0811  -0.0177 218 LYS A O   
1746  C CB  . LYS A 218 ? 0.4570 0.3922 0.5548 -0.0211 0.0792  -0.0209 218 LYS A CB  
1747  C CG  . LYS A 218 ? 0.5106 0.4364 0.5887 -0.0245 0.0818  -0.0217 218 LYS A CG  
1748  C CD  . LYS A 218 ? 0.5557 0.4705 0.6210 -0.0279 0.0731  -0.0193 218 LYS A CD  
1749  C CE  . LYS A 218 ? 0.5903 0.4947 0.6348 -0.0299 0.0764  -0.0217 218 LYS A CE  
1750  N NZ  . LYS A 218 ? 0.5969 0.4906 0.6282 -0.0335 0.0680  -0.0190 218 LYS A NZ  
1751  N N   . PRO A 219 ? 0.3957 0.3483 0.5292 -0.0108 0.0799  -0.0235 219 PRO A N   
1752  C CA  . PRO A 219 ? 0.3692 0.3268 0.5163 -0.0085 0.0748  -0.0216 219 PRO A CA  
1753  C C   . PRO A 219 ? 0.3513 0.3062 0.4963 -0.0119 0.0677  -0.0177 219 PRO A C   
1754  O O   . PRO A 219 ? 0.3388 0.2856 0.4718 -0.0149 0.0648  -0.0171 219 PRO A O   
1755  C CB  . PRO A 219 ? 0.3794 0.3316 0.5269 -0.0043 0.0729  -0.0248 219 PRO A CB  
1756  C CG  . PRO A 219 ? 0.3879 0.3349 0.5254 -0.0033 0.0788  -0.0293 219 PRO A CG  
1757  C CD  . PRO A 219 ? 0.4046 0.3486 0.5292 -0.0083 0.0811  -0.0280 219 PRO A CD  
1758  N N   . PHE A 220 ? 0.3305 0.2924 0.4873 -0.0112 0.0649  -0.0152 220 PHE A N   
1759  C CA  . PHE A 220 ? 0.2897 0.2508 0.4476 -0.0133 0.0586  -0.0118 220 PHE A CA  
1760  C C   . PHE A 220 ? 0.2908 0.2532 0.4571 -0.0100 0.0544  -0.0116 220 PHE A C   
1761  O O   . PHE A 220 ? 0.2966 0.2650 0.4724 -0.0069 0.0561  -0.0122 220 PHE A O   
1762  C CB  . PHE A 220 ? 0.2824 0.2505 0.4464 -0.0155 0.0597  -0.0092 220 PHE A CB  
1763  C CG  . PHE A 220 ? 0.2679 0.2361 0.4354 -0.0164 0.0533  -0.0064 220 PHE A CG  
1764  C CD1 . PHE A 220 ? 0.2626 0.2236 0.4232 -0.0176 0.0481  -0.0054 220 PHE A CD1 
1765  C CD2 . PHE A 220 ? 0.2667 0.2423 0.4449 -0.0156 0.0525  -0.0050 220 PHE A CD2 
1766  C CE1 . PHE A 220 ? 0.2722 0.2337 0.4368 -0.0178 0.0429  -0.0034 220 PHE A CE1 
1767  C CE2 . PHE A 220 ? 0.2506 0.2257 0.4311 -0.0161 0.0471  -0.0030 220 PHE A CE2 
1768  C CZ  . PHE A 220 ? 0.2605 0.2288 0.4345 -0.0170 0.0427  -0.0023 220 PHE A CZ  
1769  N N   . ILE A 221 ? 0.2883 0.2454 0.4513 -0.0108 0.0489  -0.0106 221 ILE A N   
1770  C CA  . ILE A 221 ? 0.3039 0.2624 0.4742 -0.0084 0.0454  -0.0099 221 ILE A CA  
1771  C C   . ILE A 221 ? 0.3044 0.2631 0.4758 -0.0101 0.0406  -0.0072 221 ILE A C   
1772  O O   . ILE A 221 ? 0.3016 0.2570 0.4668 -0.0130 0.0388  -0.0062 221 ILE A O   
1773  C CB  . ILE A 221 ? 0.3138 0.2662 0.4814 -0.0070 0.0443  -0.0118 221 ILE A CB  
1774  C CG1 . ILE A 221 ? 0.3338 0.2787 0.4927 -0.0098 0.0403  -0.0118 221 ILE A CG1 
1775  C CG2 . ILE A 221 ? 0.3230 0.2743 0.4891 -0.0047 0.0492  -0.0150 221 ILE A CG2 
1776  C CD1 . ILE A 221 ? 0.3663 0.3050 0.5234 -0.0090 0.0382  -0.0136 221 ILE A CD1 
1777  N N   . THR A 222 ? 0.3053 0.2674 0.4842 -0.0081 0.0385  -0.0061 222 THR A N   
1778  C CA  . THR A 222 ? 0.3091 0.2711 0.4896 -0.0088 0.0343  -0.0043 222 THR A CA  
1779  C C   . THR A 222 ? 0.2994 0.2581 0.4803 -0.0082 0.0318  -0.0045 222 THR A C   
1780  O O   . THR A 222 ? 0.2475 0.2064 0.4315 -0.0062 0.0331  -0.0051 222 THR A O   
1781  C CB  . THR A 222 ? 0.2930 0.2611 0.4805 -0.0073 0.0340  -0.0030 222 THR A CB  
1782  O OG1 . THR A 222 ? 0.2889 0.2590 0.4812 -0.0045 0.0350  -0.0033 222 THR A OG1 
1783  C CG2 . THR A 222 ? 0.2880 0.2598 0.4766 -0.0083 0.0364  -0.0029 222 THR A CG2 
1784  N N   . THR A 223 ? 0.2911 0.2469 0.4697 -0.0100 0.0280  -0.0038 223 THR A N   
1785  C CA  . THR A 223 ? 0.2870 0.2402 0.4671 -0.0101 0.0252  -0.0039 223 THR A CA  
1786  C C   . THR A 223 ? 0.2775 0.2351 0.4648 -0.0090 0.0235  -0.0023 223 THR A C   
1787  O O   . THR A 223 ? 0.2663 0.2236 0.4571 -0.0091 0.0217  -0.0019 223 THR A O   
1788  C CB  . THR A 223 ? 0.3149 0.2621 0.4880 -0.0126 0.0219  -0.0044 223 THR A CB  
1789  O OG1 . THR A 223 ? 0.2956 0.2428 0.4660 -0.0139 0.0202  -0.0032 223 THR A OG1 
1790  C CG2 . THR A 223 ? 0.3277 0.2698 0.4930 -0.0133 0.0242  -0.0066 223 THR A CG2 
1791  N N   . ALA A 224 ? 0.2624 0.2242 0.4522 -0.0079 0.0245  -0.0014 224 ALA A N   
1792  C CA  . ALA A 224 ? 0.2739 0.2394 0.4692 -0.0065 0.0235  -0.0004 224 ALA A CA  
1793  C C   . ALA A 224 ? 0.2920 0.2605 0.4879 -0.0055 0.0240  0.0000  224 ALA A C   
1794  O O   . ALA A 224 ? 0.3015 0.2688 0.4942 -0.0069 0.0236  -0.0001 224 ALA A O   
1795  C CB  . ALA A 224 ? 0.2695 0.2339 0.4664 -0.0073 0.0199  -0.0002 224 ALA A CB  
1796  N N   . PHE A 225 ? 0.2951 0.2671 0.4948 -0.0035 0.0248  0.0005  225 PHE A N   
1797  C CA  . PHE A 225 ? 0.2875 0.2617 0.4877 -0.0024 0.0243  0.0006  225 PHE A CA  
1798  C C   . PHE A 225 ? 0.2857 0.2625 0.4885 -0.0002 0.0252  0.0010  225 PHE A C   
1799  O O   . PHE A 225 ? 0.2564 0.2335 0.4604 0.0004  0.0269  0.0017  225 PHE A O   
1800  C CB  . PHE A 225 ? 0.2906 0.2660 0.4899 -0.0027 0.0256  0.0004  225 PHE A CB  
1801  C CG  . PHE A 225 ? 0.2757 0.2528 0.4767 -0.0012 0.0280  0.0006  225 PHE A CG  
1802  C CD1 . PHE A 225 ? 0.2927 0.2679 0.4926 -0.0018 0.0297  0.0000  225 PHE A CD1 
1803  C CD2 . PHE A 225 ? 0.2660 0.2455 0.4688 0.0008  0.0281  0.0011  225 PHE A CD2 
1804  C CE1 . PHE A 225 ? 0.2868 0.2628 0.4886 0.0001  0.0315  0.0000  225 PHE A CE1 
1805  C CE2 . PHE A 225 ? 0.2864 0.2667 0.4907 0.0025  0.0295  0.0015  225 PHE A CE2 
1806  C CZ  . PHE A 225 ? 0.2756 0.2542 0.4800 0.0022  0.0312  0.0009  225 PHE A CZ  
1807  N N   . GLY A 226 ? 0.2682 0.2461 0.4710 0.0010  0.0242  0.0006  226 GLY A N   
1808  C CA  . GLY A 226 ? 0.2754 0.2554 0.4788 0.0031  0.0256  0.0010  226 GLY A CA  
1809  C C   . GLY A 226 ? 0.2883 0.2687 0.4920 0.0045  0.0247  -0.0001 226 GLY A C   
1810  O O   . GLY A 226 ? 0.2965 0.2751 0.5001 0.0040  0.0223  -0.0010 226 GLY A O   
1811  N N   . TYR A 227 ? 0.3076 0.2898 0.5114 0.0064  0.0268  0.0001  227 TYR A N   
1812  C CA  . TYR A 227 ? 0.2674 0.2502 0.4706 0.0085  0.0269  -0.0015 227 TYR A CA  
1813  C C   . TYR A 227 ? 0.2618 0.2475 0.4680 0.0096  0.0302  -0.0011 227 TYR A C   
1814  O O   . TYR A 227 ? 0.2653 0.2523 0.4720 0.0089  0.0328  0.0008  227 TYR A O   
1815  C CB  . TYR A 227 ? 0.2573 0.2390 0.4550 0.0099  0.0264  -0.0021 227 TYR A CB  
1816  C CG  . TYR A 227 ? 0.2482 0.2278 0.4447 0.0084  0.0230  -0.0025 227 TYR A CG  
1817  C CD1 . TYR A 227 ? 0.2454 0.2227 0.4418 0.0082  0.0202  -0.0041 227 TYR A CD1 
1818  C CD2 . TYR A 227 ? 0.2595 0.2396 0.4558 0.0072  0.0228  -0.0013 227 TYR A CD2 
1819  C CE1 . TYR A 227 ? 0.2832 0.2587 0.4789 0.0062  0.0175  -0.0042 227 TYR A CE1 
1820  C CE2 . TYR A 227 ? 0.2568 0.2363 0.4534 0.0055  0.0204  -0.0016 227 TYR A CE2 
1821  C CZ  . TYR A 227 ? 0.2573 0.2345 0.4535 0.0047  0.0179  -0.0029 227 TYR A CZ  
1822  O OH  . TYR A 227 ? 0.2145 0.1909 0.4111 0.0024  0.0158  -0.0028 227 TYR A OH  
1823  N N   . SER A 228 ? 0.2562 0.2432 0.4648 0.0114  0.0303  -0.0029 228 SER A N   
1824  C CA  . SER A 228 ? 0.2534 0.2445 0.4668 0.0127  0.0338  -0.0030 228 SER A CA  
1825  C C   . SER A 228 ? 0.2576 0.2491 0.4658 0.0154  0.0369  -0.0042 228 SER A C   
1826  O O   . SER A 228 ? 0.2420 0.2306 0.4457 0.0172  0.0348  -0.0066 228 SER A O   
1827  C CB  . SER A 228 ? 0.2711 0.2636 0.4917 0.0134  0.0317  -0.0045 228 SER A CB  
1828  O OG  . SER A 228 ? 0.2678 0.2655 0.4944 0.0152  0.0354  -0.0052 228 SER A OG  
1829  N N   . VAL A 229 ? 0.2437 0.2386 0.4526 0.0155  0.0418  -0.0028 229 VAL A N   
1830  C CA  . VAL A 229 ? 0.2638 0.2587 0.4661 0.0179  0.0455  -0.0038 229 VAL A CA  
1831  C C   . VAL A 229 ? 0.2811 0.2811 0.4894 0.0201  0.0497  -0.0056 229 VAL A C   
1832  O O   . VAL A 229 ? 0.2719 0.2741 0.4770 0.0212  0.0552  -0.0054 229 VAL A O   
1833  C CB  . VAL A 229 ? 0.2586 0.2521 0.4541 0.0166  0.0480  -0.0007 229 VAL A CB  
1834  C CG1 . VAL A 229 ? 0.2553 0.2444 0.4461 0.0155  0.0433  0.0002  229 VAL A CG1 
1835  C CG2 . VAL A 229 ? 0.2695 0.2666 0.4708 0.0142  0.0519  0.0024  229 VAL A CG2 
1836  N N   . SER A 230 ? 0.2812 0.2828 0.4979 0.0210  0.0470  -0.0076 230 SER A N   
1837  C CA  . SER A 230 ? 0.2914 0.2987 0.5162 0.0236  0.0505  -0.0096 230 SER A CA  
1838  C C   . SER A 230 ? 0.2941 0.3001 0.5113 0.0275  0.0539  -0.0128 230 SER A C   
1839  O O   . SER A 230 ? 0.3082 0.3080 0.5159 0.0286  0.0509  -0.0144 230 SER A O   
1840  C CB  . SER A 230 ? 0.3079 0.3159 0.5423 0.0243  0.0457  -0.0112 230 SER A CB  
1841  O OG  . SER A 230 ? 0.2739 0.2758 0.5032 0.0264  0.0409  -0.0139 230 SER A OG  
1842  N N   . PRO A 231 ? 0.3036 0.3153 0.5240 0.0295  0.0606  -0.0137 231 PRO A N   
1843  C CA  . PRO A 231 ? 0.3184 0.3284 0.5311 0.0338  0.0639  -0.0176 231 PRO A CA  
1844  C C   . PRO A 231 ? 0.3035 0.3090 0.5162 0.0375  0.0589  -0.0221 231 PRO A C   
1845  O O   . PRO A 231 ? 0.2941 0.2936 0.4959 0.0398  0.0582  -0.0250 231 PRO A O   
1846  C CB  . PRO A 231 ? 0.3260 0.3450 0.5471 0.0350  0.0722  -0.0177 231 PRO A CB  
1847  C CG  . PRO A 231 ? 0.3343 0.3572 0.5602 0.0298  0.0738  -0.0124 231 PRO A CG  
1848  C CD  . PRO A 231 ? 0.3218 0.3416 0.5526 0.0274  0.0657  -0.0111 231 PRO A CD  
1849  N N   . GLU A 232 ? 0.2953 0.3029 0.5199 0.0379  0.0550  -0.0227 232 GLU A N   
1850  C CA  . GLU A 232 ? 0.3193 0.3211 0.5441 0.0405  0.0489  -0.0261 232 GLU A CA  
1851  C C   . GLU A 232 ? 0.3002 0.3025 0.5349 0.0382  0.0429  -0.0241 232 GLU A C   
1852  O O   . GLU A 232 ? 0.2736 0.2793 0.5124 0.0343  0.0429  -0.0203 232 GLU A O   
1853  C CB  . GLU A 232 ? 0.3456 0.3495 0.5730 0.0464  0.0528  -0.0310 232 GLU A CB  
1854  C CG  . GLU A 232 ? 0.3761 0.3907 0.6188 0.0477  0.0578  -0.0309 232 GLU A CG  
1855  C CD  . GLU A 232 ? 0.4088 0.4273 0.6569 0.0539  0.0625  -0.0359 232 GLU A CD  
1856  O OE1 . GLU A 232 ? 0.4310 0.4449 0.6808 0.0582  0.0583  -0.0400 232 GLU A OE1 
1857  O OE2 . GLU A 232 ? 0.4352 0.4622 0.6874 0.0543  0.0708  -0.0355 232 GLU A OE2 
1858  N N   . GLY A 233 ? 0.2945 0.2924 0.5319 0.0408  0.0375  -0.0267 233 GLY A N   
1859  C CA  . GLY A 233 ? 0.2696 0.2662 0.5145 0.0391  0.0309  -0.0251 233 GLY A CA  
1860  C C   . GLY A 233 ? 0.2687 0.2571 0.5046 0.0352  0.0253  -0.0230 233 GLY A C   
1861  O O   . GLY A 233 ? 0.2564 0.2417 0.4823 0.0336  0.0264  -0.0225 233 GLY A O   
1862  N N   . GLY A 234 ? 0.2613 0.2468 0.5012 0.0335  0.0193  -0.0215 234 GLY A N   
1863  C CA  . GLY A 234 ? 0.2795 0.2581 0.5121 0.0295  0.0144  -0.0193 234 GLY A CA  
1864  C C   . GLY A 234 ? 0.3143 0.2840 0.5405 0.0310  0.0100  -0.0215 234 GLY A C   
1865  O O   . GLY A 234 ? 0.2992 0.2668 0.5288 0.0351  0.0084  -0.0244 234 GLY A O   
1866  N N   . ASN A 235 ? 0.3656 0.3303 0.5834 0.0274  0.0081  -0.0200 235 ASN A N   
1867  C CA  . ASN A 235 ? 0.3864 0.3425 0.5980 0.0273  0.0036  -0.0213 235 ASN A CA  
1868  C C   . ASN A 235 ? 0.3463 0.3007 0.5503 0.0231  0.0038  -0.0195 235 ASN A C   
1869  O O   . ASN A 235 ? 0.3546 0.3113 0.5586 0.0193  0.0042  -0.0163 235 ASN A O   
1870  C CB  . ASN A 235 ? 0.4296 0.3800 0.6438 0.0264  -0.0025 -0.0201 235 ASN A CB  
1871  C CG  . ASN A 235 ? 0.5928 0.5334 0.8010 0.0260  -0.0072 -0.0213 235 ASN A CG  
1872  O OD1 . ASN A 235 ? 0.6156 0.5527 0.8233 0.0302  -0.0079 -0.0251 235 ASN A OD1 
1873  N ND2 . ASN A 235 ? 0.6306 0.5667 0.8343 0.0210  -0.0103 -0.0183 235 ASN A ND2 
1874  N N   . GLY A 236 ? 0.3243 0.2751 0.5220 0.0241  0.0035  -0.0218 236 GLY A N   
1875  C CA  . GLY A 236 ? 0.3346 0.2847 0.5266 0.0207  0.0033  -0.0204 236 GLY A CA  
1876  C C   . GLY A 236 ? 0.3733 0.3308 0.5658 0.0196  0.0081  -0.0183 236 GLY A C   
1877  O O   . GLY A 236 ? 0.3519 0.3138 0.5451 0.0223  0.0125  -0.0192 236 GLY A O   
1878  N N   . GLN A 237 ? 0.3364 0.2951 0.5287 0.0155  0.0075  -0.0152 237 GLN A N   
1879  C CA  . GLN A 237 ? 0.3381 0.3026 0.5309 0.0147  0.0115  -0.0132 237 GLN A CA  
1880  C C   . GLN A 237 ? 0.3150 0.2837 0.5136 0.0145  0.0139  -0.0116 237 GLN A C   
1881  O O   . GLN A 237 ? 0.2937 0.2663 0.4930 0.0136  0.0169  -0.0098 237 GLN A O   
1882  C CB  . GLN A 237 ? 0.3284 0.2930 0.5195 0.0110  0.0103  -0.0111 237 GLN A CB  
1883  C CG  . GLN A 237 ? 0.3302 0.2919 0.5166 0.0108  0.0078  -0.0125 237 GLN A CG  
1884  C CD  . GLN A 237 ? 0.3339 0.2974 0.5213 0.0072  0.0070  -0.0102 237 GLN A CD  
1885  O OE1 . GLN A 237 ? 0.3640 0.3318 0.5525 0.0068  0.0095  -0.0085 237 GLN A OE1 
1886  N NE2 . GLN A 237 ? 0.3149 0.2751 0.5027 0.0044  0.0035  -0.0101 237 GLN A NE2 
1887  N N   . TYR A 238 ? 0.3242 0.2916 0.5271 0.0152  0.0119  -0.0120 238 TYR A N   
1888  C CA  . TYR A 238 ? 0.3324 0.3040 0.5415 0.0150  0.0135  -0.0107 238 TYR A CA  
1889  C C   . TYR A 238 ? 0.3519 0.3280 0.5651 0.0187  0.0171  -0.0125 238 TYR A C   
1890  O O   . TYR A 238 ? 0.3690 0.3437 0.5844 0.0219  0.0160  -0.0150 238 TYR A O   
1891  C CB  . TYR A 238 ? 0.3219 0.2900 0.5338 0.0139  0.0090  -0.0100 238 TYR A CB  
1892  C CG  . TYR A 238 ? 0.2752 0.2474 0.4941 0.0139  0.0095  -0.0090 238 TYR A CG  
1893  C CD1 . TYR A 238 ? 0.2745 0.2490 0.4936 0.0109  0.0109  -0.0068 238 TYR A CD1 
1894  C CD2 . TYR A 238 ? 0.2754 0.2490 0.5013 0.0169  0.0081  -0.0105 238 TYR A CD2 
1895  C CE1 . TYR A 238 ? 0.2798 0.2575 0.5053 0.0105  0.0107  -0.0060 238 TYR A CE1 
1896  C CE2 . TYR A 238 ? 0.2917 0.2698 0.5253 0.0167  0.0080  -0.0096 238 TYR A CE2 
1897  C CZ  . TYR A 238 ? 0.2804 0.2603 0.5135 0.0132  0.0091  -0.0073 238 TYR A CZ  
1898  O OH  . TYR A 238 ? 0.2955 0.2791 0.5362 0.0125  0.0083  -0.0065 238 TYR A OH  
1899  N N   . GLY A 239 ? 0.3276 0.3088 0.5419 0.0183  0.0217  -0.0112 239 GLY A N   
1900  C CA  . GLY A 239 ? 0.3149 0.3009 0.5317 0.0213  0.0265  -0.0125 239 GLY A CA  
1901  C C   . GLY A 239 ? 0.3316 0.3153 0.5398 0.0232  0.0284  -0.0142 239 GLY A C   
1902  O O   . GLY A 239 ? 0.3027 0.2812 0.5046 0.0224  0.0250  -0.0147 239 GLY A O   
1903  N N   . SER A 240 ? 0.3107 0.2984 0.5185 0.0253  0.0339  -0.0148 240 SER A N   
1904  C CA  . SER A 240 ? 0.3088 0.2943 0.5083 0.0281  0.0362  -0.0173 240 SER A CA  
1905  C C   . SER A 240 ? 0.3057 0.2870 0.4949 0.0264  0.0346  -0.0162 240 SER A C   
1906  O O   . SER A 240 ? 0.3131 0.2903 0.4940 0.0283  0.0339  -0.0185 240 SER A O   
1907  C CB  . SER A 240 ? 0.3206 0.3024 0.5207 0.0316  0.0334  -0.0215 240 SER A CB  
1908  O OG  . SER A 240 ? 0.3062 0.2929 0.5166 0.0339  0.0354  -0.0227 240 SER A OG  
1909  N N   . ASN A 241 ? 0.3239 0.3062 0.5136 0.0231  0.0339  -0.0126 241 ASN A N   
1910  C CA  . ASN A 241 ? 0.2923 0.2717 0.4737 0.0220  0.0327  -0.0114 241 ASN A CA  
1911  C C   . ASN A 241 ? 0.2931 0.2740 0.4688 0.0230  0.0377  -0.0102 241 ASN A C   
1912  O O   . ASN A 241 ? 0.2909 0.2761 0.4710 0.0229  0.0424  -0.0089 241 ASN A O   
1913  C CB  . ASN A 241 ? 0.2965 0.2763 0.4809 0.0186  0.0303  -0.0084 241 ASN A CB  
1914  C CG  . ASN A 241 ? 0.2848 0.2623 0.4724 0.0172  0.0256  -0.0093 241 ASN A CG  
1915  O OD1 . ASN A 241 ? 0.3450 0.3197 0.5293 0.0161  0.0221  -0.0095 241 ASN A OD1 
1916  N ND2 . ASN A 241 ? 0.2752 0.2538 0.4693 0.0167  0.0252  -0.0093 241 ASN A ND2 
1917  N N   . THR A 242 ? 0.3046 0.2817 0.4704 0.0234  0.0363  -0.0102 242 THR A N   
1918  C CA  . THR A 242 ? 0.2944 0.2717 0.4532 0.0235  0.0401  -0.0079 242 THR A CA  
1919  C C   . THR A 242 ? 0.2963 0.2751 0.4591 0.0207  0.0398  -0.0036 242 THR A C   
1920  O O   . THR A 242 ? 0.2903 0.2694 0.4590 0.0190  0.0362  -0.0031 242 THR A O   
1921  C CB  . THR A 242 ? 0.3071 0.2789 0.4533 0.0249  0.0375  -0.0090 242 THR A CB  
1922  O OG1 . THR A 242 ? 0.2748 0.2446 0.4219 0.0232  0.0313  -0.0082 242 THR A OG1 
1923  C CG2 . THR A 242 ? 0.3333 0.3022 0.4736 0.0279  0.0378  -0.0137 242 THR A CG2 
1924  N N   . LEU A 243 ? 0.3221 0.3008 0.4801 0.0203  0.0433  -0.0006 243 LEU A N   
1925  C CA  . LEU A 243 ? 0.3292 0.3078 0.4895 0.0181  0.0428  0.0034  243 LEU A CA  
1926  C C   . LEU A 243 ? 0.3152 0.2906 0.4727 0.0179  0.0369  0.0037  243 LEU A C   
1927  O O   . LEU A 243 ? 0.3077 0.2838 0.4709 0.0164  0.0350  0.0053  243 LEU A O   
1928  C CB  . LEU A 243 ? 0.3380 0.3157 0.4918 0.0178  0.0476  0.0065  243 LEU A CB  
1929  C CG  . LEU A 243 ? 0.3575 0.3397 0.5163 0.0171  0.0542  0.0072  243 LEU A CG  
1930  C CD1 . LEU A 243 ? 0.3779 0.3578 0.5283 0.0162  0.0582  0.0111  243 LEU A CD1 
1931  C CD2 . LEU A 243 ? 0.3550 0.3414 0.5269 0.0148  0.0547  0.0081  243 LEU A CD2 
1932  N N   . LYS A 244 ? 0.3277 0.2998 0.4767 0.0195  0.0340  0.0019  244 LYS A N   
1933  C CA  . LYS A 244 ? 0.3455 0.3155 0.4933 0.0194  0.0279  0.0019  244 LYS A CA  
1934  C C   . LYS A 244 ? 0.3515 0.3236 0.5083 0.0181  0.0248  -0.0001 244 LYS A C   
1935  O O   . LYS A 244 ? 0.3937 0.3669 0.5553 0.0170  0.0219  0.0011  244 LYS A O   
1936  C CB  . LYS A 244 ? 0.4081 0.3738 0.5449 0.0211  0.0247  0.0001  244 LYS A CB  
1937  C CG  . LYS A 244 ? 0.4853 0.4495 0.6219 0.0207  0.0181  0.0008  244 LYS A CG  
1938  C CD  . LYS A 244 ? 0.6067 0.5663 0.7333 0.0220  0.0133  -0.0016 244 LYS A CD  
1939  C CE  . LYS A 244 ? 0.6466 0.6067 0.7775 0.0211  0.0061  -0.0015 244 LYS A CE  
1940  N NZ  . LYS A 244 ? 0.6400 0.6033 0.7787 0.0204  0.0056  0.0019  244 LYS A NZ  
1941  N N   . GLN A 245 ? 0.3217 0.2943 0.4806 0.0185  0.0254  -0.0031 245 GLN A N   
1942  C CA  . GLN A 245 ? 0.3144 0.2881 0.4807 0.0170  0.0227  -0.0045 245 GLN A CA  
1943  C C   . GLN A 245 ? 0.3050 0.2819 0.4795 0.0151  0.0243  -0.0023 245 GLN A C   
1944  O O   . GLN A 245 ? 0.2760 0.2536 0.4552 0.0134  0.0219  -0.0021 245 GLN A O   
1945  C CB  . GLN A 245 ? 0.3059 0.2786 0.4727 0.0182  0.0231  -0.0077 245 GLN A CB  
1946  C CG  . GLN A 245 ? 0.3147 0.2829 0.4740 0.0197  0.0198  -0.0108 245 GLN A CG  
1947  C CD  . GLN A 245 ? 0.3201 0.2861 0.4786 0.0217  0.0203  -0.0144 245 GLN A CD  
1948  O OE1 . GLN A 245 ? 0.3036 0.2715 0.4637 0.0235  0.0248  -0.0151 245 GLN A OE1 
1949  N NE2 . GLN A 245 ? 0.3562 0.3180 0.5129 0.0215  0.0155  -0.0169 245 GLN A NE2 
1950  N N   . GLN A 246 ? 0.3037 0.2822 0.4796 0.0152  0.0287  -0.0008 246 GLN A N   
1951  C CA  . GLN A 246 ? 0.2886 0.2692 0.4715 0.0133  0.0300  0.0010  246 GLN A CA  
1952  C C   . GLN A 246 ? 0.2784 0.2584 0.4614 0.0126  0.0284  0.0031  246 GLN A C   
1953  O O   . GLN A 246 ? 0.2865 0.2673 0.4744 0.0111  0.0273  0.0032  246 GLN A O   
1954  C CB  . GLN A 246 ? 0.2945 0.2769 0.4792 0.0133  0.0345  0.0023  246 GLN A CB  
1955  C CG  . GLN A 246 ? 0.2996 0.2832 0.4909 0.0111  0.0352  0.0041  246 GLN A CG  
1956  C CD  . GLN A 246 ? 0.2943 0.2798 0.4882 0.0104  0.0394  0.0058  246 GLN A CD  
1957  O OE1 . GLN A 246 ? 0.2951 0.2800 0.4843 0.0110  0.0422  0.0075  246 GLN A OE1 
1958  N NE2 . GLN A 246 ? 0.2840 0.2714 0.4850 0.0088  0.0397  0.0057  246 GLN A NE2 
1959  N N   . SER A 247 ? 0.2815 0.2598 0.4587 0.0138  0.0284  0.0047  247 SER A N   
1960  C CA  . SER A 247 ? 0.3045 0.2820 0.4823 0.0138  0.0268  0.0068  247 SER A CA  
1961  C C   . SER A 247 ? 0.3060 0.2846 0.4865 0.0136  0.0225  0.0054  247 SER A C   
1962  O O   . SER A 247 ? 0.3198 0.2999 0.5061 0.0128  0.0221  0.0057  247 SER A O   
1963  C CB  . SER A 247 ? 0.3139 0.2885 0.4842 0.0151  0.0272  0.0092  247 SER A CB  
1964  O OG  . SER A 247 ? 0.3383 0.3116 0.5095 0.0156  0.0250  0.0113  247 SER A OG  
1965  N N   . ASP A 248 ? 0.3159 0.2937 0.4926 0.0142  0.0197  0.0035  248 ASP A N   
1966  C CA  . ASP A 248 ? 0.3050 0.2843 0.4854 0.0135  0.0156  0.0023  248 ASP A CA  
1967  C C   . ASP A 248 ? 0.2893 0.2707 0.4765 0.0113  0.0163  0.0012  248 ASP A C   
1968  O O   . ASP A 248 ? 0.2937 0.2776 0.4863 0.0102  0.0150  0.0014  248 ASP A O   
1969  C CB  . ASP A 248 ? 0.2990 0.2761 0.4739 0.0141  0.0118  0.0004  248 ASP A CB  
1970  C CG  . ASP A 248 ? 0.2958 0.2699 0.4621 0.0161  0.0098  0.0013  248 ASP A CG  
1971  O OD1 . ASP A 248 ? 0.2899 0.2638 0.4554 0.0170  0.0104  0.0039  248 ASP A OD1 
1972  O OD2 . ASP A 248 ? 0.3235 0.2945 0.4828 0.0168  0.0075  -0.0008 248 ASP A OD2 
1973  N N   . GLY A 249 ? 0.2819 0.2625 0.4689 0.0107  0.0185  0.0003  249 GLY A N   
1974  C CA  . GLY A 249 ? 0.2836 0.2652 0.4756 0.0086  0.0189  -0.0004 249 GLY A CA  
1975  C C   . GLY A 249 ? 0.3108 0.2939 0.5072 0.0074  0.0209  0.0010  249 GLY A C   
1976  O O   . GLY A 249 ? 0.3228 0.3071 0.5226 0.0056  0.0205  0.0007  249 GLY A O   
1977  N N   . LEU A 250 ? 0.2927 0.2754 0.4886 0.0083  0.0234  0.0024  250 LEU A N   
1978  C CA  . LEU A 250 ? 0.2753 0.2585 0.4747 0.0076  0.0251  0.0032  250 LEU A CA  
1979  C C   . LEU A 250 ? 0.2832 0.2682 0.4854 0.0080  0.0239  0.0034  250 LEU A C   
1980  O O   . LEU A 250 ? 0.2796 0.2657 0.4851 0.0070  0.0250  0.0029  250 LEU A O   
1981  C CB  . LEU A 250 ? 0.2897 0.2713 0.4880 0.0083  0.0274  0.0049  250 LEU A CB  
1982  C CG  . LEU A 250 ? 0.2788 0.2597 0.4783 0.0070  0.0291  0.0047  250 LEU A CG  
1983  C CD1 . LEU A 250 ? 0.2922 0.2727 0.4943 0.0051  0.0289  0.0037  250 LEU A CD1 
1984  C CD2 . LEU A 250 ? 0.2634 0.2451 0.4619 0.0072  0.0289  0.0037  250 LEU A CD2 
1985  N N   . ILE A 251 ? 0.2827 0.2684 0.4837 0.0096  0.0216  0.0039  251 ILE A N   
1986  C CA  . ILE A 251 ? 0.3026 0.2910 0.5082 0.0104  0.0201  0.0041  251 ILE A CA  
1987  C C   . ILE A 251 ? 0.2666 0.2584 0.4765 0.0084  0.0190  0.0026  251 ILE A C   
1988  O O   . ILE A 251 ? 0.2621 0.2570 0.4776 0.0078  0.0201  0.0023  251 ILE A O   
1989  C CB  . ILE A 251 ? 0.3533 0.3409 0.5562 0.0128  0.0171  0.0053  251 ILE A CB  
1990  C CG1 . ILE A 251 ? 0.3725 0.3561 0.5702 0.0142  0.0187  0.0074  251 ILE A CG1 
1991  C CG2 . ILE A 251 ? 0.3512 0.3424 0.5608 0.0140  0.0149  0.0055  251 ILE A CG2 
1992  C CD1 . ILE A 251 ? 0.3613 0.3438 0.5621 0.0145  0.0213  0.0083  251 ILE A CD1 
1993  N N   . SER A 252 ? 0.2744 0.2653 0.4817 0.0071  0.0170  0.0017  252 SER A N   
1994  C CA  . SER A 252 ? 0.2532 0.2459 0.4637 0.0044  0.0160  0.0007  252 SER A CA  
1995  C C   . SER A 252 ? 0.2531 0.2457 0.4651 0.0023  0.0194  0.0006  252 SER A C   
1996  O O   . SER A 252 ? 0.2465 0.2423 0.4631 0.0004  0.0204  0.0005  252 SER A O   
1997  C CB  . SER A 252 ? 0.2629 0.2526 0.4690 0.0037  0.0132  -0.0003 252 SER A CB  
1998  O OG  . SER A 252 ? 0.3087 0.2990 0.5175 0.0006  0.0119  -0.0010 252 SER A OG  
1999  N N   . ASN A 253 ? 0.2516 0.2409 0.4598 0.0024  0.0211  0.0007  253 ASN A N   
2000  C CA  . ASN A 253 ? 0.2361 0.2242 0.4441 0.0005  0.0235  0.0006  253 ASN A CA  
2001  C C   . ASN A 253 ? 0.2633 0.2537 0.4747 0.0010  0.0263  0.0006  253 ASN A C   
2002  O O   . ASN A 253 ? 0.3129 0.3042 0.5254 -0.0009 0.0282  0.0002  253 ASN A O   
2003  C CB  . ASN A 253 ? 0.2475 0.2321 0.4521 0.0009  0.0242  0.0007  253 ASN A CB  
2004  C CG  . ASN A 253 ? 0.2381 0.2204 0.4402 0.0007  0.0222  0.0002  253 ASN A CG  
2005  O OD1 . ASN A 253 ? 0.2190 0.1995 0.4200 0.0011  0.0227  0.0002  253 ASN A OD1 
2006  N ND2 . ASN A 253 ? 0.2225 0.2047 0.4242 0.0002  0.0198  -0.0004 253 ASN A ND2 
2007  N N   . TYR A 254 ? 0.2411 0.2322 0.4539 0.0038  0.0265  0.0011  254 TYR A N   
2008  C CA  . TYR A 254 ? 0.2385 0.2303 0.4540 0.0049  0.0291  0.0008  254 TYR A CA  
2009  C C   . TYR A 254 ? 0.2252 0.2223 0.4468 0.0044  0.0300  0.0001  254 TYR A C   
2010  O O   . TYR A 254 ? 0.2138 0.2118 0.4367 0.0037  0.0332  -0.0009 254 TYR A O   
2011  C CB  . TYR A 254 ? 0.2313 0.2215 0.4468 0.0080  0.0287  0.0018  254 TYR A CB  
2012  C CG  . TYR A 254 ? 0.2259 0.2132 0.4414 0.0089  0.0312  0.0014  254 TYR A CG  
2013  C CD1 . TYR A 254 ? 0.2428 0.2320 0.4624 0.0100  0.0332  0.0001  254 TYR A CD1 
2014  C CD2 . TYR A 254 ? 0.2443 0.2269 0.4559 0.0086  0.0316  0.0021  254 TYR A CD2 
2015  C CE1 . TYR A 254 ? 0.2504 0.2359 0.4693 0.0112  0.0353  -0.0008 254 TYR A CE1 
2016  C CE2 . TYR A 254 ? 0.2582 0.2372 0.4696 0.0092  0.0333  0.0016  254 TYR A CE2 
2017  C CZ  . TYR A 254 ? 0.2568 0.2366 0.4712 0.0107  0.0350  0.0000  254 TYR A CZ  
2018  O OH  . TYR A 254 ? 0.2655 0.2406 0.4788 0.0114  0.0365  -0.0011 254 TYR A OH  
2019  N N   . ARG A 255 ? 0.2341 0.2348 0.4595 0.0050  0.0271  0.0005  255 ARG A N   
2020  C CA  . ARG A 255 ? 0.2489 0.2559 0.4819 0.0041  0.0271  0.0000  255 ARG A CA  
2021  C C   . ARG A 255 ? 0.2577 0.2654 0.4901 -0.0001 0.0293  -0.0004 255 ARG A C   
2022  O O   . ARG A 255 ? 0.2168 0.2284 0.4536 -0.0010 0.0330  -0.0010 255 ARG A O   
2023  C CB  . ARG A 255 ? 0.2655 0.2745 0.5006 0.0047  0.0221  0.0006  255 ARG A CB  
2024  C CG  . ARG A 255 ? 0.2589 0.2746 0.5027 0.0030  0.0207  0.0004  255 ARG A CG  
2025  C CD  . ARG A 255 ? 0.2545 0.2762 0.5077 0.0059  0.0218  0.0001  255 ARG A CD  
2026  N NE  . ARG A 255 ? 0.2402 0.2648 0.4970 0.0049  0.0277  -0.0009 255 ARG A NE  
2027  C CZ  . ARG A 255 ? 0.2545 0.2797 0.5136 0.0078  0.0311  -0.0018 255 ARG A CZ  
2028  N NH1 . ARG A 255 ? 0.2789 0.3026 0.5391 0.0121  0.0289  -0.0015 255 ARG A NH1 
2029  N NH2 . ARG A 255 ? 0.2572 0.2842 0.5175 0.0064  0.0367  -0.0031 255 ARG A NH2 
2030  N N   . ASP A 256 ? 0.2722 0.2757 0.4987 -0.0023 0.0274  0.0000  256 ASP A N   
2031  C CA  . ASP A 256 ? 0.2692 0.2721 0.4943 -0.0065 0.0284  0.0002  256 ASP A CA  
2032  C C   . ASP A 256 ? 0.2551 0.2563 0.4770 -0.0076 0.0329  -0.0001 256 ASP A C   
2033  O O   . ASP A 256 ? 0.2603 0.2636 0.4834 -0.0106 0.0358  0.0000  256 ASP A O   
2034  C CB  . ASP A 256 ? 0.2787 0.2760 0.4978 -0.0078 0.0250  0.0006  256 ASP A CB  
2035  C CG  . ASP A 256 ? 0.3066 0.3049 0.5278 -0.0079 0.0206  0.0005  256 ASP A CG  
2036  O OD1 . ASP A 256 ? 0.3001 0.3035 0.5275 -0.0069 0.0198  0.0004  256 ASP A OD1 
2037  O OD2 . ASP A 256 ? 0.3462 0.3398 0.5628 -0.0087 0.0177  0.0003  256 ASP A OD2 
2038  N N   . LEU A 257 ? 0.2402 0.2370 0.4573 -0.0057 0.0336  -0.0005 257 LEU A N   
2039  C CA  . LEU A 257 ? 0.2519 0.2453 0.4639 -0.0070 0.0368  -0.0011 257 LEU A CA  
2040  C C   . LEU A 257 ? 0.2557 0.2530 0.4718 -0.0056 0.0412  -0.0024 257 LEU A C   
2041  O O   . LEU A 257 ? 0.2748 0.2715 0.4880 -0.0074 0.0449  -0.0031 257 LEU A O   
2042  C CB  . LEU A 257 ? 0.2541 0.2418 0.4607 -0.0056 0.0353  -0.0012 257 LEU A CB  
2043  C CG  . LEU A 257 ? 0.2550 0.2390 0.4579 -0.0068 0.0317  -0.0003 257 LEU A CG  
2044  C CD1 . LEU A 257 ? 0.2372 0.2181 0.4382 -0.0050 0.0301  -0.0002 257 LEU A CD1 
2045  C CD2 . LEU A 257 ? 0.2659 0.2465 0.4637 -0.0105 0.0318  0.0002  257 LEU A CD2 
2046  N N   . ILE A 258 ? 0.2688 0.2698 0.4914 -0.0020 0.0408  -0.0028 258 ILE A N   
2047  C CA  . ILE A 258 ? 0.2627 0.2684 0.4912 -0.0002 0.0448  -0.0042 258 ILE A CA  
2048  C C   . ILE A 258 ? 0.2574 0.2695 0.4910 -0.0033 0.0471  -0.0041 258 ILE A C   
2049  O O   . ILE A 258 ? 0.2684 0.2828 0.5028 -0.0040 0.0524  -0.0053 258 ILE A O   
2050  C CB  . ILE A 258 ? 0.2750 0.2836 0.5106 0.0043  0.0430  -0.0044 258 ILE A CB  
2051  C CG1 . ILE A 258 ? 0.3005 0.3022 0.5307 0.0068  0.0417  -0.0043 258 ILE A CG1 
2052  C CG2 . ILE A 258 ? 0.2786 0.2935 0.5228 0.0066  0.0469  -0.0061 258 ILE A CG2 
2053  C CD1 . ILE A 258 ? 0.2963 0.2987 0.5312 0.0110  0.0391  -0.0036 258 ILE A CD1 
2054  N N   . ASP A 259 ? 0.2574 0.2719 0.4940 -0.0053 0.0434  -0.0026 259 ASP A N   
2055  C CA  . ASP A 259 ? 0.2749 0.2957 0.5177 -0.0088 0.0450  -0.0020 259 ASP A CA  
2056  C C   . ASP A 259 ? 0.2692 0.2864 0.5045 -0.0134 0.0485  -0.0014 259 ASP A C   
2057  O O   . ASP A 259 ? 0.2813 0.3038 0.5212 -0.0165 0.0521  -0.0010 259 ASP A O   
2058  C CB  . ASP A 259 ? 0.2641 0.2869 0.5112 -0.0103 0.0396  -0.0007 259 ASP A CB  
2059  C CG  . ASP A 259 ? 0.2666 0.2931 0.5206 -0.0063 0.0357  -0.0010 259 ASP A CG  
2060  O OD1 . ASP A 259 ? 0.2657 0.2972 0.5267 -0.0031 0.0382  -0.0020 259 ASP A OD1 
2061  O OD2 . ASP A 259 ? 0.2546 0.2784 0.5064 -0.0061 0.0303  -0.0003 259 ASP A OD2 
2062  N N   . ALA A 260 ? 0.2469 0.2555 0.4713 -0.0138 0.0475  -0.0013 260 ALA A N   
2063  C CA  . ALA A 260 ? 0.2750 0.2786 0.4904 -0.0179 0.0500  -0.0005 260 ALA A CA  
2064  C C   . ALA A 260 ? 0.2833 0.2858 0.4941 -0.0172 0.0558  -0.0023 260 ALA A C   
2065  O O   . ALA A 260 ? 0.3341 0.3320 0.5360 -0.0205 0.0581  -0.0017 260 ALA A O   
2066  C CB  . ALA A 260 ? 0.2880 0.2829 0.4944 -0.0187 0.0451  0.0005  260 ALA A CB  
2067  N N   . GLY A 261 ? 0.2775 0.2832 0.4935 -0.0128 0.0579  -0.0044 261 GLY A N   
2068  C CA  . GLY A 261 ? 0.2924 0.2969 0.5048 -0.0113 0.0634  -0.0069 261 GLY A CA  
2069  C C   . GLY A 261 ? 0.2942 0.2911 0.4999 -0.0082 0.0615  -0.0084 261 GLY A C   
2070  O O   . GLY A 261 ? 0.3266 0.3205 0.5274 -0.0070 0.0654  -0.0108 261 GLY A O   
2071  N N   . ALA A 262 ? 0.2903 0.2837 0.4954 -0.0070 0.0558  -0.0073 262 ALA A N   
2072  C CA  . ALA A 262 ? 0.2887 0.2752 0.4883 -0.0048 0.0541  -0.0084 262 ALA A CA  
2073  C C   . ALA A 262 ? 0.2906 0.2790 0.4958 -0.0004 0.0566  -0.0106 262 ALA A C   
2074  O O   . ALA A 262 ? 0.3035 0.2983 0.5183 0.0020  0.0563  -0.0103 262 ALA A O   
2075  C CB  . ALA A 262 ? 0.2712 0.2551 0.4709 -0.0044 0.0484  -0.0066 262 ALA A CB  
2076  N N   . VAL A 263 ? 0.3150 0.2972 0.5139 0.0008  0.0584  -0.0129 263 VAL A N   
2077  C CA  . VAL A 263 ? 0.2979 0.2792 0.5007 0.0053  0.0597  -0.0152 263 VAL A CA  
2078  C C   . VAL A 263 ? 0.3203 0.2933 0.5182 0.0060  0.0557  -0.0150 263 VAL A C   
2079  O O   . VAL A 263 ? 0.3118 0.2806 0.5095 0.0089  0.0564  -0.0171 263 VAL A O   
2080  C CB  . VAL A 263 ? 0.3214 0.3024 0.5215 0.0064  0.0660  -0.0187 263 VAL A CB  
2081  C CG1 . VAL A 263 ? 0.3707 0.3618 0.5789 0.0061  0.0706  -0.0188 263 VAL A CG1 
2082  C CG2 . VAL A 263 ? 0.3092 0.2820 0.4956 0.0032  0.0670  -0.0199 263 VAL A CG2 
2083  N N   . GLY A 264 ? 0.3013 0.2720 0.4957 0.0032  0.0516  -0.0127 264 GLY A N   
2084  C CA  . GLY A 264 ? 0.3164 0.2812 0.5085 0.0033  0.0478  -0.0120 264 GLY A CA  
2085  C C   . GLY A 264 ? 0.3085 0.2750 0.5015 0.0013  0.0440  -0.0090 264 GLY A C   
2086  O O   . GLY A 264 ? 0.2989 0.2674 0.4899 -0.0012 0.0438  -0.0082 264 GLY A O   
2087  N N   . MET A 265 ? 0.2945 0.2601 0.4905 0.0025  0.0413  -0.0075 265 MET A N   
2088  C CA  . MET A 265 ? 0.2781 0.2463 0.4761 0.0016  0.0384  -0.0050 265 MET A CA  
2089  C C   . MET A 265 ? 0.2718 0.2359 0.4688 0.0009  0.0361  -0.0040 265 MET A C   
2090  O O   . MET A 265 ? 0.2497 0.2108 0.4478 0.0023  0.0362  -0.0040 265 MET A O   
2091  C CB  . MET A 265 ? 0.2712 0.2449 0.4752 0.0039  0.0384  -0.0038 265 MET A CB  
2092  C CG  . MET A 265 ? 0.2796 0.2585 0.4865 0.0040  0.0404  -0.0046 265 MET A CG  
2093  S SD  . MET A 265 ? 0.2664 0.2476 0.4712 0.0003  0.0393  -0.0037 265 MET A SD  
2094  C CE  . MET A 265 ? 0.2374 0.2219 0.4463 0.0018  0.0359  -0.0018 265 MET A CE  
2095  N N   . CYS A 266 ? 0.2752 0.2392 0.4708 -0.0013 0.0338  -0.0031 266 CYS A N   
2096  C CA  . CYS A 266 ? 0.2713 0.2332 0.4679 -0.0022 0.0318  -0.0020 266 CYS A CA  
2097  C C   . CYS A 266 ? 0.2481 0.2143 0.4476 -0.0019 0.0306  -0.0003 266 CYS A C   
2098  O O   . CYS A 266 ? 0.2399 0.2064 0.4392 -0.0034 0.0287  -0.0001 266 CYS A O   
2099  C CB  . CYS A 266 ? 0.2762 0.2337 0.4691 -0.0048 0.0297  -0.0030 266 CYS A CB  
2100  S SG  . CYS A 266 ? 0.3182 0.2691 0.5045 -0.0053 0.0308  -0.0059 266 CYS A SG  
2101  N N   . PRO A 267 ? 0.2524 0.2216 0.4545 0.0001  0.0314  0.0010  267 PRO A N   
2102  C CA  . PRO A 267 ? 0.2516 0.2239 0.4552 0.0005  0.0306  0.0023  267 PRO A CA  
2103  C C   . PRO A 267 ? 0.2665 0.2380 0.4717 -0.0009 0.0298  0.0028  267 PRO A C   
2104  O O   . PRO A 267 ? 0.3064 0.2753 0.5126 -0.0018 0.0300  0.0032  267 PRO A O   
2105  C CB  . PRO A 267 ? 0.2526 0.2261 0.4571 0.0027  0.0316  0.0037  267 PRO A CB  
2106  C CG  . PRO A 267 ? 0.2690 0.2392 0.4736 0.0034  0.0325  0.0036  267 PRO A CG  
2107  C CD  . PRO A 267 ? 0.2709 0.2397 0.4741 0.0023  0.0328  0.0013  267 PRO A CD  
2108  N N   . PHE A 268 ? 0.2612 0.2352 0.4675 -0.0010 0.0287  0.0028  268 PHE A N   
2109  C CA  . PHE A 268 ? 0.2601 0.2351 0.4700 -0.0018 0.0280  0.0032  268 PHE A CA  
2110  C C   . PHE A 268 ? 0.2711 0.2496 0.4831 -0.0003 0.0300  0.0044  268 PHE A C   
2111  O O   . PHE A 268 ? 0.2661 0.2464 0.4766 0.0013  0.0300  0.0039  268 PHE A O   
2112  C CB  . PHE A 268 ? 0.2532 0.2283 0.4634 -0.0025 0.0253  0.0021  268 PHE A CB  
2113  C CG  . PHE A 268 ? 0.2421 0.2188 0.4577 -0.0032 0.0238  0.0023  268 PHE A CG  
2114  C CD1 . PHE A 268 ? 0.2459 0.2268 0.4657 -0.0016 0.0248  0.0024  268 PHE A CD1 
2115  C CD2 . PHE A 268 ? 0.2434 0.2175 0.4600 -0.0054 0.0214  0.0020  268 PHE A CD2 
2116  C CE1 . PHE A 268 ? 0.2653 0.2489 0.4920 -0.0021 0.0236  0.0024  268 PHE A CE1 
2117  C CE2 . PHE A 268 ? 0.2455 0.2218 0.4687 -0.0062 0.0194  0.0021  268 PHE A CE2 
2118  C CZ  . PHE A 268 ? 0.2625 0.2442 0.4916 -0.0044 0.0206  0.0024  268 PHE A CZ  
2119  N N   . TYR A 269 ? 0.2686 0.2475 0.4832 -0.0009 0.0319  0.0060  269 TYR A N   
2120  C CA  . TYR A 269 ? 0.2724 0.2484 0.4888 -0.0029 0.0318  0.0067  269 TYR A CA  
2121  C C   . TYR A 269 ? 0.2498 0.2266 0.4679 -0.0032 0.0346  0.0092  269 TYR A C   
2122  O O   . TYR A 269 ? 0.2765 0.2560 0.4934 -0.0017 0.0367  0.0101  269 TYR A O   
2123  C CB  . TYR A 269 ? 0.2853 0.2610 0.5056 -0.0052 0.0292  0.0058  269 TYR A CB  
2124  C CG  . TYR A 269 ? 0.2825 0.2631 0.5100 -0.0058 0.0293  0.0063  269 TYR A CG  
2125  C CD1 . TYR A 269 ? 0.2786 0.2639 0.5079 -0.0039 0.0319  0.0067  269 TYR A CD1 
2126  C CD2 . TYR A 269 ? 0.2986 0.2790 0.5314 -0.0081 0.0266  0.0059  269 TYR A CD2 
2127  C CE1 . TYR A 269 ? 0.2827 0.2731 0.5196 -0.0040 0.0324  0.0067  269 TYR A CE1 
2128  C CE2 . TYR A 269 ? 0.2748 0.2607 0.5160 -0.0085 0.0264  0.0062  269 TYR A CE2 
2129  C CZ  . TYR A 269 ? 0.2818 0.2732 0.5256 -0.0062 0.0297  0.0065  269 TYR A CZ  
2130  O OH  . TYR A 269 ? 0.2615 0.2592 0.5147 -0.0060 0.0303  0.0064  269 TYR A OH  
2131  N N   . TYR A 270 ? 0.2626 0.2369 0.4835 -0.0055 0.0347  0.0103  270 TYR A N   
2132  C CA  . TYR A 270 ? 0.2686 0.2418 0.4897 -0.0062 0.0374  0.0133  270 TYR A CA  
2133  C C   . TYR A 270 ? 0.2892 0.2681 0.5137 -0.0065 0.0406  0.0149  270 TYR A C   
2134  O O   . TYR A 270 ? 0.2877 0.2665 0.5083 -0.0054 0.0434  0.0170  270 TYR A O   
2135  C CB  . TYR A 270 ? 0.2772 0.2459 0.5010 -0.0092 0.0362  0.0140  270 TYR A CB  
2136  C CG  . TYR A 270 ? 0.2627 0.2298 0.4882 -0.0112 0.0388  0.0175  270 TYR A CG  
2137  C CD1 . TYR A 270 ? 0.2619 0.2251 0.4819 -0.0098 0.0403  0.0199  270 TYR A CD1 
2138  C CD2 . TYR A 270 ? 0.2611 0.2301 0.4938 -0.0148 0.0391  0.0188  270 TYR A CD2 
2139  C CE1 . TYR A 270 ? 0.2656 0.2262 0.4860 -0.0120 0.0425  0.0236  270 TYR A CE1 
2140  C CE2 . TYR A 270 ? 0.2689 0.2361 0.5033 -0.0174 0.0417  0.0224  270 TYR A CE2 
2141  C CZ  . TYR A 270 ? 0.2598 0.2224 0.4873 -0.0160 0.0435  0.0250  270 TYR A CZ  
2142  O OH  . TYR A 270 ? 0.2600 0.2198 0.4881 -0.0189 0.0459  0.0291  270 TYR A OH  
2143  N N   . ALA A 271 ? 0.2742 0.2578 0.5060 -0.0078 0.0403  0.0141  271 ALA A N   
2144  C CA  . ALA A 271 ? 0.2737 0.2633 0.5102 -0.0081 0.0443  0.0155  271 ALA A CA  
2145  C C   . ALA A 271 ? 0.2479 0.2438 0.4922 -0.0076 0.0432  0.0133  271 ALA A C   
2146  O O   . ALA A 271 ? 0.2407 0.2361 0.4893 -0.0088 0.0391  0.0118  271 ALA A O   
2147  C CB  . ALA A 271 ? 0.2747 0.2636 0.5150 -0.0116 0.0467  0.0187  271 ALA A CB  
2148  N N   . ASP A 272 ? 0.2437 0.2450 0.4895 -0.0057 0.0470  0.0132  272 ASP A N   
2149  C CA  . ASP A 272 ? 0.2545 0.2623 0.5084 -0.0044 0.0466  0.0110  272 ASP A CA  
2150  C C   . ASP A 272 ? 0.2407 0.2522 0.5066 -0.0074 0.0448  0.0114  272 ASP A C   
2151  O O   . ASP A 272 ? 0.2638 0.2758 0.5341 -0.0109 0.0466  0.0139  272 ASP A O   
2152  C CB  . ASP A 272 ? 0.2602 0.2736 0.5149 -0.0022 0.0525  0.0111  272 ASP A CB  
2153  C CG  . ASP A 272 ? 0.2440 0.2543 0.4873 0.0012  0.0536  0.0100  272 ASP A CG  
2154  O OD1 . ASP A 272 ? 0.2244 0.2296 0.4615 0.0022  0.0494  0.0088  272 ASP A OD1 
2155  O OD2 . ASP A 272 ? 0.2684 0.2817 0.5093 0.0028  0.0588  0.0102  272 ASP A OD2 
2156  N N   . GLY A 273 ? 0.2292 0.2426 0.5002 -0.0061 0.0405  0.0089  273 GLY A N   
2157  C CA  . GLY A 273 ? 0.2455 0.2630 0.5287 -0.0082 0.0373  0.0086  273 GLY A CA  
2158  C C   . GLY A 273 ? 0.2548 0.2806 0.5476 -0.0053 0.0386  0.0069  273 GLY A C   
2159  O O   . GLY A 273 ? 0.2737 0.2984 0.5647 -0.0022 0.0352  0.0045  273 GLY A O   
2160  N N   . TRP A 274 ? 0.2351 0.2690 0.5373 -0.0060 0.0441  0.0081  274 TRP A N   
2161  C CA  . TRP A 274 ? 0.2325 0.2750 0.5445 -0.0026 0.0465  0.0062  274 TRP A CA  
2162  C C   . TRP A 274 ? 0.2512 0.2961 0.5740 -0.0020 0.0393  0.0043  274 TRP A C   
2163  O O   . TRP A 274 ? 0.2806 0.3297 0.6090 0.0021  0.0387  0.0018  274 TRP A O   
2164  C CB  . TRP A 274 ? 0.2181 0.2696 0.5398 -0.0043 0.0541  0.0081  274 TRP A CB  
2165  C CG  . TRP A 274 ? 0.2054 0.2545 0.5157 -0.0044 0.0614  0.0101  274 TRP A CG  
2166  C CD1 . TRP A 274 ? 0.1965 0.2364 0.4906 -0.0039 0.0610  0.0108  274 TRP A CD1 
2167  C CD2 . TRP A 274 ? 0.2034 0.2600 0.5181 -0.0049 0.0703  0.0116  274 TRP A CD2 
2168  N NE1 . TRP A 274 ? 0.1958 0.2363 0.4834 -0.0039 0.0683  0.0127  274 TRP A NE1 
2169  C CE2 . TRP A 274 ? 0.2013 0.2515 0.5003 -0.0047 0.0744  0.0134  274 TRP A CE2 
2170  C CE3 . TRP A 274 ? 0.2090 0.2773 0.5396 -0.0054 0.0753  0.0117  274 TRP A CE3 
2171  C CZ2 . TRP A 274 ? 0.2271 0.2814 0.5242 -0.0052 0.0832  0.0154  274 TRP A CZ2 
2172  C CZ3 . TRP A 274 ? 0.2105 0.2838 0.5400 -0.0058 0.0850  0.0134  274 TRP A CZ3 
2173  C CH2 . TRP A 274 ? 0.2285 0.2943 0.5405 -0.0058 0.0888  0.0154  274 TRP A CH2 
2174  N N   . TRP A 275 ? 0.2562 0.2980 0.5818 -0.0059 0.0336  0.0054  275 TRP A N   
2175  C CA  . TRP A 275 ? 0.2442 0.2874 0.5791 -0.0060 0.0258  0.0040  275 TRP A CA  
2176  C C   . TRP A 275 ? 0.2491 0.2863 0.5761 -0.0022 0.0206  0.0017  275 TRP A C   
2177  O O   . TRP A 275 ? 0.2172 0.2564 0.5523 -0.0007 0.0148  0.0004  275 TRP A O   
2178  C CB  . TRP A 275 ? 0.2530 0.2910 0.5876 -0.0112 0.0204  0.0055  275 TRP A CB  
2179  C CG  . TRP A 275 ? 0.2476 0.2735 0.5654 -0.0123 0.0170  0.0054  275 TRP A CG  
2180  C CD1 . TRP A 275 ? 0.2493 0.2692 0.5567 -0.0143 0.0203  0.0069  275 TRP A CD1 
2181  C CD2 . TRP A 275 ? 0.2335 0.2519 0.5439 -0.0116 0.0094  0.0039  275 TRP A CD2 
2182  N NE1 . TRP A 275 ? 0.2334 0.2435 0.5283 -0.0146 0.0159  0.0060  275 TRP A NE1 
2183  C CE2 . TRP A 275 ? 0.2346 0.2435 0.5305 -0.0133 0.0095  0.0043  275 TRP A CE2 
2184  C CE3 . TRP A 275 ? 0.2247 0.2432 0.5391 -0.0098 0.0027  0.0024  275 TRP A CE3 
2185  C CZ2 . TRP A 275 ? 0.2278 0.2282 0.5131 -0.0134 0.0039  0.0032  275 TRP A CZ2 
2186  C CZ3 . TRP A 275 ? 0.2108 0.2197 0.5134 -0.0101 -0.0034 0.0017  275 TRP A CZ3 
2187  C CH2 . TRP A 275 ? 0.2293 0.2297 0.5177 -0.0120 -0.0023 0.0020  275 TRP A CH2 
2188  N N   . LYS A 276 ? 0.2716 0.3014 0.5832 -0.0008 0.0222  0.0014  276 LYS A N   
2189  C CA  . LYS A 276 ? 0.2607 0.2823 0.5625 0.0007  0.0163  0.0001  276 LYS A CA  
2190  C C   . LYS A 276 ? 0.2844 0.3084 0.5900 0.0055  0.0151  -0.0021 276 LYS A C   
2191  O O   . LYS A 276 ? 0.3053 0.3236 0.6068 0.0065  0.0089  -0.0029 276 LYS A O   
2192  C CB  . LYS A 276 ? 0.2516 0.2654 0.5376 0.0001  0.0183  0.0007  276 LYS A CB  
2193  C CG  . LYS A 276 ? 0.2620 0.2712 0.5431 -0.0042 0.0179  0.0024  276 LYS A CG  
2194  C CD  . LYS A 276 ? 0.2535 0.2570 0.5217 -0.0042 0.0211  0.0030  276 LYS A CD  
2195  C CE  . LYS A 276 ? 0.2341 0.2318 0.4924 -0.0026 0.0184  0.0018  276 LYS A CE  
2196  N NZ  . LYS A 276 ? 0.2416 0.2331 0.4956 -0.0050 0.0129  0.0016  276 LYS A NZ  
2197  N N   . GLY A 277 ? 0.2910 0.3227 0.6038 0.0085  0.0211  -0.0031 277 GLY A N   
2198  C CA  . GLY A 277 ? 0.3121 0.3458 0.6293 0.0136  0.0200  -0.0058 277 GLY A CA  
2199  C C   . GLY A 277 ? 0.3280 0.3706 0.6637 0.0152  0.0176  -0.0067 277 GLY A C   
2200  O O   . GLY A 277 ? 0.3333 0.3781 0.6743 0.0200  0.0170  -0.0092 277 GLY A O   
2201  N N   . GLY A 278 ? 0.3641 0.4118 0.7101 0.0113  0.0163  -0.0049 278 GLY A N   
2202  C CA  . GLY A 278 ? 0.3244 0.3800 0.6888 0.0123  0.0119  -0.0056 278 GLY A CA  
2203  C C   . GLY A 278 ? 0.3313 0.3992 0.7120 0.0099  0.0174  -0.0045 278 GLY A C   
2204  O O   . GLY A 278 ? 0.3250 0.3986 0.7206 0.0083  0.0123  -0.0041 278 GLY A O   
2205  N N   . GLU A 279 ? 0.3135 0.3860 0.6924 0.0100  0.0276  -0.0040 279 GLU A N   
2206  C CA  . GLU A 279 ? 0.3069 0.3914 0.7010 0.0076  0.0341  -0.0026 279 GLU A CA  
2207  C C   . GLU A 279 ? 0.3000 0.3813 0.6838 0.0027  0.0402  0.0005  279 GLU A C   
2208  O O   . GLU A 279 ? 0.3105 0.3901 0.6837 0.0043  0.0474  0.0005  279 GLU A O   
2209  C CB  . GLU A 279 ? 0.3104 0.4057 0.7152 0.0128  0.0417  -0.0051 279 GLU A CB  
2210  C CG  . GLU A 279 ? 0.3323 0.4406 0.7519 0.0099  0.0503  -0.0033 279 GLU A CG  
2211  C CD  . GLU A 279 ? 0.3851 0.4995 0.8212 0.0044  0.0455  -0.0010 279 GLU A CD  
2212  O OE1 . GLU A 279 ? 0.4482 0.5654 0.8970 0.0057  0.0371  -0.0024 279 GLU A OE1 
2213  O OE2 . GLU A 279 ? 0.4513 0.5674 0.8882 -0.0015 0.0499  0.0023  279 GLU A OE2 
2214  N N   . LYS A 280 ? 0.2940 0.3744 0.6816 -0.0032 0.0371  0.0031  280 LYS A N   
2215  C CA  . LYS A 280 ? 0.2735 0.3477 0.6497 -0.0078 0.0407  0.0061  280 LYS A CA  
2216  C C   . LYS A 280 ? 0.2604 0.3416 0.6392 -0.0091 0.0518  0.0082  280 LYS A C   
2217  O O   . LYS A 280 ? 0.2506 0.3256 0.6171 -0.0117 0.0555  0.0107  280 LYS A O   
2218  C CB  . LYS A 280 ? 0.2911 0.3629 0.6731 -0.0136 0.0339  0.0078  280 LYS A CB  
2219  C CG  . LYS A 280 ? 0.2850 0.3693 0.6893 -0.0162 0.0345  0.0087  280 LYS A CG  
2220  C CD  . LYS A 280 ? 0.3190 0.4001 0.7291 -0.0214 0.0257  0.0096  280 LYS A CD  
2221  C CE  . LYS A 280 ? 0.3544 0.4489 0.7878 -0.0247 0.0269  0.0108  280 LYS A CE  
2222  N NZ  . LYS A 280 ? 0.3889 0.4803 0.8286 -0.0277 0.0154  0.0103  280 LYS A NZ  
2223  N N   . SER A 281 ? 0.2612 0.3553 0.6560 -0.0073 0.0570  0.0073  281 SER A N   
2224  C CA  . SER A 281 ? 0.2868 0.3887 0.6854 -0.0090 0.0682  0.0095  281 SER A CA  
2225  C C   . SER A 281 ? 0.2816 0.3833 0.6689 -0.0038 0.0762  0.0078  281 SER A C   
2226  O O   . SER A 281 ? 0.2588 0.3657 0.6459 -0.0047 0.0861  0.0094  281 SER A O   
2227  C CB  . SER A 281 ? 0.2919 0.4089 0.7148 -0.0104 0.0707  0.0096  281 SER A CB  
2228  O OG  . SER A 281 ? 0.3264 0.4429 0.7579 -0.0170 0.0650  0.0123  281 SER A OG  
2229  N N   . ASP A 282 ? 0.2907 0.3863 0.6692 0.0016  0.0715  0.0043  282 ASP A N   
2230  C CA  . ASP A 282 ? 0.3313 0.4259 0.6998 0.0072  0.0770  0.0015  282 ASP A CA  
2231  C C   . ASP A 282 ? 0.2953 0.3759 0.6429 0.0081  0.0724  0.0013  282 ASP A C   
2232  O O   . ASP A 282 ? 0.2767 0.3503 0.6214 0.0068  0.0637  0.0014  282 ASP A O   
2233  C CB  . ASP A 282 ? 0.4054 0.5079 0.7873 0.0131  0.0761  -0.0028 282 ASP A CB  
2234  C CG  . ASP A 282 ? 0.5176 0.6176 0.8888 0.0195  0.0807  -0.0065 282 ASP A CG  
2235  O OD1 . ASP A 282 ? 0.5927 0.6991 0.9642 0.0207  0.0910  -0.0069 282 ASP A OD1 
2236  O OD2 . ASP A 282 ? 0.6022 0.6931 0.9635 0.0227  0.0742  -0.0089 282 ASP A OD2 
2237  N N   . HIS A 283 ? 0.2883 0.3649 0.6212 0.0099  0.0784  0.0012  283 HIS A N   
2238  C CA  . HIS A 283 ? 0.2881 0.3526 0.6026 0.0111  0.0743  0.0007  283 HIS A CA  
2239  C C   . HIS A 283 ? 0.2834 0.3470 0.5940 0.0174  0.0742  -0.0039 283 HIS A C   
2240  O O   . HIS A 283 ? 0.2832 0.3482 0.5877 0.0202  0.0812  -0.0053 283 HIS A O   
2241  C CB  . HIS A 283 ? 0.2639 0.3230 0.5640 0.0083  0.0791  0.0040  283 HIS A CB  
2242  C CG  . HIS A 283 ? 0.2565 0.3042 0.5417 0.0078  0.0733  0.0046  283 HIS A CG  
2243  N ND1 . HIS A 283 ? 0.2602 0.3015 0.5301 0.0074  0.0761  0.0064  283 HIS A ND1 
2244  C CD2 . HIS A 283 ? 0.2376 0.2794 0.5210 0.0077  0.0652  0.0036  283 HIS A CD2 
2245  C CE1 . HIS A 283 ? 0.2502 0.2830 0.5112 0.0074  0.0697  0.0062  283 HIS A CE1 
2246  N NE2 . HIS A 283 ? 0.2333 0.2663 0.5019 0.0074  0.0635  0.0046  283 HIS A NE2 
2247  N N   . SER A 284 ? 0.2789 0.3400 0.5937 0.0196  0.0663  -0.0063 284 SER A N   
2248  C CA  . SER A 284 ? 0.2674 0.3279 0.5820 0.0257  0.0652  -0.0108 284 SER A CA  
2249  C C   . SER A 284 ? 0.2516 0.3024 0.5472 0.0277  0.0655  -0.0121 284 SER A C   
2250  O O   . SER A 284 ? 0.2553 0.2978 0.5399 0.0251  0.0612  -0.0104 284 SER A O   
2251  C CB  . SER A 284 ? 0.2644 0.3237 0.5878 0.0268  0.0561  -0.0122 284 SER A CB  
2252  O OG  . SER A 284 ? 0.2964 0.3500 0.6139 0.0318  0.0530  -0.0158 284 SER A OG  
2253  N N   . LEU A 285 ? 0.2654 0.3172 0.5569 0.0323  0.0707  -0.0155 285 LEU A N   
2254  C CA  . LEU A 285 ? 0.2694 0.3124 0.5433 0.0342  0.0708  -0.0171 285 LEU A CA  
2255  C C   . LEU A 285 ? 0.2633 0.2971 0.5318 0.0354  0.0617  -0.0188 285 LEU A C   
2256  O O   . LEU A 285 ? 0.2649 0.2907 0.5194 0.0350  0.0598  -0.0188 285 LEU A O   
2257  C CB  . LEU A 285 ? 0.2895 0.3355 0.5609 0.0393  0.0782  -0.0210 285 LEU A CB  
2258  C CG  . LEU A 285 ? 0.3231 0.3788 0.5999 0.0383  0.0886  -0.0195 285 LEU A CG  
2259  C CD1 . LEU A 285 ? 0.3339 0.3918 0.6058 0.0436  0.0965  -0.0239 285 LEU A CD1 
2260  C CD2 . LEU A 285 ? 0.3175 0.3710 0.5851 0.0326  0.0912  -0.0142 285 LEU A CD2 
2261  N N   . ASN A 286 ? 0.2656 0.3006 0.5451 0.0364  0.0558  -0.0198 286 ASN A N   
2262  C CA  . ASN A 286 ? 0.2706 0.2967 0.5449 0.0380  0.0480  -0.0216 286 ASN A CA  
2263  C C   . ASN A 286 ? 0.2485 0.2717 0.5263 0.0343  0.0403  -0.0189 286 ASN A C   
2264  O O   . ASN A 286 ? 0.2489 0.2662 0.5259 0.0357  0.0338  -0.0202 286 ASN A O   
2265  C CB  . ASN A 286 ? 0.2908 0.3176 0.5716 0.0441  0.0471  -0.0262 286 ASN A CB  
2266  C CG  . ASN A 286 ? 0.3058 0.3406 0.6050 0.0454  0.0453  -0.0264 286 ASN A CG  
2267  O OD1 . ASN A 286 ? 0.3060 0.3476 0.6144 0.0418  0.0460  -0.0234 286 ASN A OD1 
2268  N ND2 . ASN A 286 ? 0.3423 0.3755 0.6471 0.0505  0.0416  -0.0300 286 ASN A ND2 
2269  N N   . GLN A 287 ? 0.2672 0.2928 0.5464 0.0295  0.0411  -0.0152 287 GLN A N   
2270  C CA  . GLN A 287 ? 0.2658 0.2876 0.5455 0.0257  0.0345  -0.0127 287 GLN A CA  
2271  C C   . GLN A 287 ? 0.2612 0.2766 0.5277 0.0221  0.0343  -0.0105 287 GLN A C   
2272  O O   . GLN A 287 ? 0.2768 0.2945 0.5424 0.0191  0.0379  -0.0080 287 GLN A O   
2273  C CB  . GLN A 287 ? 0.2676 0.2972 0.5603 0.0231  0.0352  -0.0107 287 GLN A CB  
2274  C CG  . GLN A 287 ? 0.2668 0.3029 0.5749 0.0263  0.0333  -0.0127 287 GLN A CG  
2275  C CD  . GLN A 287 ? 0.2659 0.2954 0.5738 0.0275  0.0241  -0.0136 287 GLN A CD  
2276  O OE1 . GLN A 287 ? 0.2869 0.3084 0.5856 0.0244  0.0191  -0.0119 287 GLN A OE1 
2277  N NE2 . GLN A 287 ? 0.2394 0.2719 0.5573 0.0321  0.0221  -0.0163 287 GLN A NE2 
2278  N N   . PRO A 288 ? 0.2433 0.2506 0.5001 0.0222  0.0301  -0.0110 288 PRO A N   
2279  C CA  . PRO A 288 ? 0.2505 0.2530 0.4968 0.0191  0.0300  -0.0090 288 PRO A CA  
2280  C C   . PRO A 288 ? 0.2473 0.2510 0.4957 0.0149  0.0298  -0.0060 288 PRO A C   
2281  O O   . PRO A 288 ? 0.2720 0.2751 0.5150 0.0131  0.0328  -0.0043 288 PRO A O   
2282  C CB  . PRO A 288 ? 0.2468 0.2420 0.4875 0.0192  0.0241  -0.0099 288 PRO A CB  
2283  C CG  . PRO A 288 ? 0.2454 0.2406 0.4890 0.0237  0.0237  -0.0132 288 PRO A CG  
2284  C CD  . PRO A 288 ? 0.2481 0.2507 0.5044 0.0250  0.0251  -0.0135 288 PRO A CD  
2285  N N   . GLU A 289 ? 0.2403 0.2456 0.4970 0.0136  0.0263  -0.0055 289 GLU A N   
2286  C CA  . GLU A 289 ? 0.2611 0.2652 0.5185 0.0096  0.0243  -0.0033 289 GLU A CA  
2287  C C   . GLU A 289 ? 0.2549 0.2639 0.5163 0.0076  0.0293  -0.0014 289 GLU A C   
2288  O O   . GLU A 289 ? 0.2574 0.2645 0.5181 0.0043  0.0282  0.0003  289 GLU A O   
2289  C CB  . GLU A 289 ? 0.2442 0.2477 0.5082 0.0088  0.0181  -0.0035 289 GLU A CB  
2290  C CG  . GLU A 289 ? 0.2764 0.2723 0.5331 0.0089  0.0124  -0.0040 289 GLU A CG  
2291  C CD  . GLU A 289 ? 0.2814 0.2710 0.5271 0.0059  0.0119  -0.0027 289 GLU A CD  
2292  O OE1 . GLU A 289 ? 0.2931 0.2829 0.5388 0.0031  0.0126  -0.0014 289 GLU A OE1 
2293  O OE2 . GLU A 289 ? 0.2646 0.2492 0.5023 0.0061  0.0106  -0.0031 289 GLU A OE2 
2294  N N   . GLU A 290 ? 0.2477 0.2627 0.5133 0.0096  0.0349  -0.0018 290 GLU A N   
2295  C CA  . GLU A 290 ? 0.2479 0.2679 0.5182 0.0075  0.0401  0.0003  290 GLU A CA  
2296  C C   . GLU A 290 ? 0.2574 0.2747 0.5172 0.0073  0.0448  0.0017  290 GLU A C   
2297  O O   . GLU A 290 ? 0.2646 0.2851 0.5263 0.0056  0.0497  0.0039  290 GLU A O   
2298  C CB  . GLU A 290 ? 0.2574 0.2862 0.5390 0.0097  0.0441  -0.0009 290 GLU A CB  
2299  C CG  . GLU A 290 ? 0.2600 0.2929 0.5549 0.0097  0.0393  -0.0018 290 GLU A CG  
2300  C CD  . GLU A 290 ? 0.2718 0.3153 0.5810 0.0116  0.0437  -0.0028 290 GLU A CD  
2301  O OE1 . GLU A 290 ? 0.2873 0.3364 0.5993 0.0106  0.0510  -0.0014 290 GLU A OE1 
2302  O OE2 . GLU A 290 ? 0.3111 0.3571 0.6296 0.0138  0.0392  -0.0047 290 GLU A OE2 
2303  N N   . TRP A 291 ? 0.2684 0.2797 0.5173 0.0087  0.0430  0.0008  291 TRP A N   
2304  C CA  . TRP A 291 ? 0.2424 0.2511 0.4812 0.0093  0.0464  0.0018  291 TRP A CA  
2305  C C   . TRP A 291 ? 0.2480 0.2500 0.4784 0.0083  0.0425  0.0023  291 TRP A C   
2306  O O   . TRP A 291 ? 0.2561 0.2552 0.4783 0.0099  0.0427  0.0017  291 TRP A O   
2307  C CB  . TRP A 291 ? 0.2458 0.2554 0.4808 0.0133  0.0488  -0.0008 291 TRP A CB  
2308  C CG  . TRP A 291 ? 0.2328 0.2496 0.4758 0.0150  0.0537  -0.0019 291 TRP A CG  
2309  C CD1 . TRP A 291 ? 0.2279 0.2494 0.4818 0.0169  0.0526  -0.0041 291 TRP A CD1 
2310  C CD2 . TRP A 291 ? 0.2395 0.2598 0.4802 0.0153  0.0610  -0.0008 291 TRP A CD2 
2311  N NE1 . TRP A 291 ? 0.2197 0.2484 0.4795 0.0185  0.0590  -0.0047 291 TRP A NE1 
2312  C CE2 . TRP A 291 ? 0.2359 0.2638 0.4872 0.0174  0.0646  -0.0026 291 TRP A CE2 
2313  C CE3 . TRP A 291 ? 0.2599 0.2773 0.4906 0.0140  0.0646  0.0019  291 TRP A CE3 
2314  C CZ2 . TRP A 291 ? 0.2633 0.2965 0.5150 0.0179  0.0726  -0.0021 291 TRP A CZ2 
2315  C CZ3 . TRP A 291 ? 0.2674 0.2890 0.4974 0.0143  0.0720  0.0028  291 TRP A CZ3 
2316  C CH2 . TRP A 291 ? 0.2764 0.3060 0.5167 0.0161  0.0764  0.0008  291 TRP A CH2 
2317  N N   . PHE A 292 ? 0.2482 0.2478 0.4808 0.0058  0.0389  0.0030  292 PHE A N   
2318  C CA  . PHE A 292 ? 0.2675 0.2618 0.4930 0.0050  0.0363  0.0033  292 PHE A CA  
2319  C C   . PHE A 292 ? 0.2514 0.2436 0.4737 0.0034  0.0383  0.0058  292 PHE A C   
2320  O O   . PHE A 292 ? 0.2496 0.2380 0.4669 0.0031  0.0367  0.0061  292 PHE A O   
2321  C CB  . PHE A 292 ? 0.2990 0.2905 0.5261 0.0033  0.0317  0.0026  292 PHE A CB  
2322  C CG  . PHE A 292 ? 0.3016 0.2915 0.5270 0.0047  0.0283  0.0006  292 PHE A CG  
2323  C CD1 . PHE A 292 ? 0.3123 0.2987 0.5310 0.0049  0.0269  0.0002  292 PHE A CD1 
2324  C CD2 . PHE A 292 ? 0.3348 0.3268 0.5661 0.0058  0.0264  -0.0007 292 PHE A CD2 
2325  C CE1 . PHE A 292 ? 0.3107 0.2950 0.5278 0.0057  0.0239  -0.0013 292 PHE A CE1 
2326  C CE2 . PHE A 292 ? 0.3327 0.3220 0.5619 0.0072  0.0231  -0.0022 292 PHE A CE2 
2327  C CZ  . PHE A 292 ? 0.3112 0.2962 0.5329 0.0068  0.0219  -0.0024 292 PHE A CZ  
2328  N N   . GLY A 293 ? 0.2394 0.2340 0.4651 0.0022  0.0417  0.0078  293 GLY A N   
2329  C CA  . GLY A 293 ? 0.2453 0.2365 0.4686 0.0003  0.0428  0.0104  293 GLY A CA  
2330  C C   . GLY A 293 ? 0.2290 0.2170 0.4435 0.0019  0.0438  0.0115  293 GLY A C   
2331  O O   . GLY A 293 ? 0.2103 0.1994 0.4202 0.0041  0.0452  0.0110  293 GLY A O   
2332  N N   . PHE A 294 ? 0.2409 0.2244 0.4528 0.0010  0.0426  0.0130  294 PHE A N   
2333  C CA  . PHE A 294 ? 0.2372 0.2176 0.4423 0.0022  0.0435  0.0150  294 PHE A CA  
2334  C C   . PHE A 294 ? 0.2424 0.2227 0.4465 0.0009  0.0475  0.0183  294 PHE A C   
2335  O O   . PHE A 294 ? 0.2731 0.2510 0.4700 0.0021  0.0486  0.0203  294 PHE A O   
2336  C CB  . PHE A 294 ? 0.2581 0.2338 0.4618 0.0022  0.0409  0.0153  294 PHE A CB  
2337  C CG  . PHE A 294 ? 0.2382 0.2141 0.4416 0.0035  0.0379  0.0125  294 PHE A CG  
2338  C CD1 . PHE A 294 ? 0.2320 0.2111 0.4362 0.0041  0.0369  0.0102  294 PHE A CD1 
2339  C CD2 . PHE A 294 ? 0.2390 0.2116 0.4417 0.0040  0.0362  0.0123  294 PHE A CD2 
2340  C CE1 . PHE A 294 ? 0.2305 0.2094 0.4343 0.0045  0.0344  0.0082  294 PHE A CE1 
2341  C CE2 . PHE A 294 ? 0.2250 0.1985 0.4279 0.0048  0.0343  0.0100  294 PHE A CE2 
2342  C CZ  . PHE A 294 ? 0.2378 0.2143 0.4411 0.0047  0.0335  0.0081  294 PHE A CZ  
2343  N N   . TRP A 295 ? 0.2296 0.2127 0.4409 -0.0017 0.0495  0.0190  295 TRP A N   
2344  C CA  . TRP A 295 ? 0.2387 0.2231 0.4510 -0.0037 0.0541  0.0222  295 TRP A CA  
2345  C C   . TRP A 295 ? 0.2459 0.2380 0.4652 -0.0039 0.0571  0.0208  295 TRP A C   
2346  O O   . TRP A 295 ? 0.2686 0.2640 0.4953 -0.0040 0.0548  0.0182  295 TRP A O   
2347  C CB  . TRP A 295 ? 0.2421 0.2232 0.4590 -0.0074 0.0537  0.0247  295 TRP A CB  
2348  C CG  . TRP A 295 ? 0.2444 0.2173 0.4550 -0.0072 0.0516  0.0267  295 TRP A CG  
2349  C CD1 . TRP A 295 ? 0.2547 0.2239 0.4614 -0.0047 0.0477  0.0249  295 TRP A CD1 
2350  C CD2 . TRP A 295 ? 0.2410 0.2085 0.4489 -0.0095 0.0532  0.0311  295 TRP A CD2 
2351  N NE1 . TRP A 295 ? 0.2813 0.2435 0.4838 -0.0047 0.0468  0.0275  295 TRP A NE1 
2352  C CE2 . TRP A 295 ? 0.2497 0.2100 0.4524 -0.0077 0.0498  0.0314  295 TRP A CE2 
2353  C CE3 . TRP A 295 ? 0.2444 0.2125 0.4542 -0.0130 0.0574  0.0349  295 TRP A CE3 
2354  C CZ2 . TRP A 295 ? 0.2530 0.2057 0.4518 -0.0089 0.0497  0.0353  295 TRP A CZ2 
2355  C CZ3 . TRP A 295 ? 0.2598 0.2202 0.4650 -0.0148 0.0577  0.0392  295 TRP A CZ3 
2356  C CH2 . TRP A 295 ? 0.2553 0.2075 0.4549 -0.0126 0.0535  0.0394  295 TRP A CH2 
2357  N N   . GLY A 296 ? 0.2593 0.2542 0.4763 -0.0038 0.0625  0.0224  296 GLY A N   
2358  C CA  . GLY A 296 ? 0.2573 0.2603 0.4821 -0.0037 0.0664  0.0212  296 GLY A CA  
2359  C C   . GLY A 296 ? 0.2589 0.2649 0.4878 -0.0072 0.0723  0.0250  296 GLY A C   
2360  O O   . GLY A 296 ? 0.2649 0.2657 0.4860 -0.0088 0.0745  0.0288  296 GLY A O   
2361  N N   . TYR A 297 ? 0.2650 0.2793 0.5061 -0.0082 0.0750  0.0239  297 TYR A N   
2362  C CA  . TYR A 297 ? 0.2840 0.3037 0.5332 -0.0121 0.0808  0.0271  297 TYR A CA  
2363  C C   . TYR A 297 ? 0.2918 0.3177 0.5389 -0.0099 0.0886  0.0267  297 TYR A C   
2364  O O   . TYR A 297 ? 0.2914 0.3208 0.5387 -0.0056 0.0884  0.0225  297 TYR A O   
2365  C CB  . TYR A 297 ? 0.2598 0.2854 0.5256 -0.0148 0.0781  0.0261  297 TYR A CB  
2366  C CG  . TYR A 297 ? 0.2431 0.2615 0.5090 -0.0167 0.0705  0.0261  297 TYR A CG  
2367  C CD1 . TYR A 297 ? 0.2614 0.2739 0.5260 -0.0210 0.0701  0.0298  297 TYR A CD1 
2368  C CD2 . TYR A 297 ? 0.2268 0.2436 0.4932 -0.0143 0.0641  0.0224  297 TYR A CD2 
2369  C CE1 . TYR A 297 ? 0.2491 0.2543 0.5126 -0.0223 0.0636  0.0292  297 TYR A CE1 
2370  C CE2 . TYR A 297 ? 0.2303 0.2402 0.4952 -0.0159 0.0581  0.0221  297 TYR A CE2 
2371  C CZ  . TYR A 297 ? 0.2322 0.2363 0.4956 -0.0197 0.0579  0.0252  297 TYR A CZ  
2372  O OH  . TYR A 297 ? 0.2233 0.2202 0.4848 -0.0210 0.0523  0.0245  297 TYR A OH  
2373  N N   . SER A 298 ? 0.2975 0.3239 0.5416 -0.0129 0.0953  0.0309  298 SER A N   
2374  C CA  . SER A 298 ? 0.3209 0.3518 0.5597 -0.0110 0.1036  0.0308  298 SER A CA  
2375  C C   . SER A 298 ? 0.3232 0.3669 0.5785 -0.0105 0.1082  0.0282  298 SER A C   
2376  O O   . SER A 298 ? 0.3291 0.3773 0.5824 -0.0063 0.1123  0.0248  298 SER A O   
2377  C CB  . SER A 298 ? 0.3388 0.3658 0.5684 -0.0148 0.1096  0.0365  298 SER A CB  
2378  O OG  . SER A 298 ? 0.3702 0.4031 0.6139 -0.0202 0.1130  0.0398  298 SER A OG  
2379  N N   . ASP A 299 ? 0.3284 0.3778 0.6001 -0.0147 0.1072  0.0297  299 ASP A N   
2380  C CA  . ASP A 299 ? 0.3197 0.3822 0.6096 -0.0147 0.1113  0.0278  299 ASP A CA  
2381  C C   . ASP A 299 ? 0.3164 0.3816 0.6227 -0.0188 0.1052  0.0285  299 ASP A C   
2382  O O   . ASP A 299 ? 0.3075 0.3638 0.6090 -0.0210 0.0983  0.0298  299 ASP A O   
2383  C CB  . ASP A 299 ? 0.3315 0.4008 0.6220 -0.0166 0.1228  0.0305  299 ASP A CB  
2384  C CG  . ASP A 299 ? 0.3681 0.4358 0.6604 -0.0239 0.1261  0.0371  299 ASP A CG  
2385  O OD1 . ASP A 299 ? 0.3890 0.4527 0.6870 -0.0278 0.1195  0.0389  299 ASP A OD1 
2386  O OD2 . ASP A 299 ? 0.4029 0.4729 0.6901 -0.0259 0.1354  0.0403  299 ASP A OD2 
2387  N N   . LEU A 300 ? 0.3245 0.4021 0.6500 -0.0194 0.1075  0.0272  300 LEU A N   
2388  C CA  . LEU A 300 ? 0.3094 0.3905 0.6516 -0.0227 0.1006  0.0270  300 LEU A CA  
2389  C C   . LEU A 300 ? 0.3140 0.3900 0.6571 -0.0300 0.0995  0.0321  300 LEU A C   
2390  O O   . LEU A 300 ? 0.3278 0.4019 0.6789 -0.0328 0.0919  0.0319  300 LEU A O   
2391  C CB  . LEU A 300 ? 0.2882 0.3847 0.6519 -0.0220 0.1042  0.0251  300 LEU A CB  
2392  C CG  . LEU A 300 ? 0.2592 0.3611 0.6425 -0.0256 0.0971  0.0250  300 LEU A CG  
2393  C CD1 . LEU A 300 ? 0.2399 0.3333 0.6187 -0.0233 0.0853  0.0219  300 LEU A CD1 
2394  C CD2 . LEU A 300 ? 0.2520 0.3703 0.6575 -0.0240 0.1008  0.0228  300 LEU A CD2 
2395  N N   . ASN A 301 ? 0.3163 0.3904 0.6519 -0.0333 0.1072  0.0367  301 ASN A N   
2396  C CA  . ASN A 301 ? 0.3075 0.3772 0.6450 -0.0406 0.1073  0.0421  301 ASN A CA  
2397  C C   . ASN A 301 ? 0.3156 0.3693 0.6344 -0.0410 0.1025  0.0441  301 ASN A C   
2398  O O   . ASN A 301 ? 0.3244 0.3715 0.6426 -0.0465 0.1011  0.0482  301 ASN A O   
2399  C CB  . ASN A 301 ? 0.3025 0.3787 0.6427 -0.0446 0.1186  0.0467  301 ASN A CB  
2400  C CG  . ASN A 301 ? 0.3146 0.4078 0.6767 -0.0449 0.1233  0.0449  301 ASN A CG  
2401  O OD1 . ASN A 301 ? 0.3127 0.4145 0.6756 -0.0428 0.1329  0.0445  301 ASN A OD1 
2402  N ND2 . ASN A 301 ? 0.3060 0.4043 0.6862 -0.0473 0.1166  0.0435  301 ASN A ND2 
2403  N N   . ASP A 302 ? 0.3083 0.3558 0.6124 -0.0351 0.1001  0.0413  302 ASP A N   
2404  C CA  . ASP A 302 ? 0.3067 0.3404 0.5944 -0.0347 0.0957  0.0428  302 ASP A CA  
2405  C C   . ASP A 302 ? 0.3345 0.3632 0.6265 -0.0351 0.0860  0.0404  302 ASP A C   
2406  O O   . ASP A 302 ? 0.3091 0.3407 0.6046 -0.0314 0.0816  0.0358  302 ASP A O   
2407  C CB  . ASP A 302 ? 0.3093 0.3392 0.5811 -0.0286 0.0967  0.0406  302 ASP A CB  
2408  C CG  . ASP A 302 ? 0.2873 0.3039 0.5425 -0.0278 0.0927  0.0424  302 ASP A CG  
2409  O OD1 . ASP A 302 ? 0.2852 0.2953 0.5408 -0.0319 0.0901  0.0457  302 ASP A OD1 
2410  O OD2 . ASP A 302 ? 0.2894 0.3025 0.5322 -0.0232 0.0922  0.0406  302 ASP A OD2 
2411  N N   . LYS A 303 ? 0.3630 0.3833 0.6537 -0.0397 0.0829  0.0435  303 LYS A N   
2412  C CA  . LYS A 303 ? 0.3953 0.4093 0.6884 -0.0404 0.0741  0.0413  303 LYS A CA  
2413  C C   . LYS A 303 ? 0.3644 0.3658 0.6416 -0.0375 0.0699  0.0409  303 LYS A C   
2414  O O   . LYS A 303 ? 0.3770 0.3722 0.6540 -0.0377 0.0632  0.0388  303 LYS A O   
2415  C CB  . LYS A 303 ? 0.5013 0.5125 0.8033 -0.0474 0.0723  0.0444  303 LYS A CB  
2416  C CG  . LYS A 303 ? 0.5601 0.5832 0.8802 -0.0521 0.0761  0.0460  303 LYS A CG  
2417  C CD  . LYS A 303 ? 0.6059 0.6377 0.9407 -0.0512 0.0711  0.0416  303 LYS A CD  
2418  C CE  . LYS A 303 ? 0.6256 0.6707 0.9794 -0.0554 0.0757  0.0433  303 LYS A CE  
2419  N NZ  . LYS A 303 ? 0.6013 0.6554 0.9677 -0.0527 0.0711  0.0387  303 LYS A NZ  
2420  N N   . TYR A 304 ? 0.3469 0.3448 0.6111 -0.0347 0.0737  0.0426  304 TYR A N   
2421  C CA  . TYR A 304 ? 0.3285 0.3149 0.5789 -0.0325 0.0703  0.0433  304 TYR A CA  
2422  C C   . TYR A 304 ? 0.3138 0.3007 0.5550 -0.0264 0.0695  0.0401  304 TYR A C   
2423  O O   . TYR A 304 ? 0.3263 0.3081 0.5631 -0.0236 0.0641  0.0374  304 TYR A O   
2424  C CB  . TYR A 304 ? 0.3498 0.3293 0.5922 -0.0353 0.0741  0.0492  304 TYR A CB  
2425  C CG  . TYR A 304 ? 0.3600 0.3373 0.6113 -0.0419 0.0741  0.0526  304 TYR A CG  
2426  C CD1 . TYR A 304 ? 0.3819 0.3507 0.6348 -0.0434 0.0675  0.0517  304 TYR A CD1 
2427  C CD2 . TYR A 304 ? 0.3869 0.3708 0.6457 -0.0467 0.0806  0.0564  304 TYR A CD2 
2428  C CE1 . TYR A 304 ? 0.3801 0.3458 0.6410 -0.0496 0.0666  0.0544  304 TYR A CE1 
2429  C CE2 . TYR A 304 ? 0.4154 0.3976 0.6839 -0.0533 0.0800  0.0594  304 TYR A CE2 
2430  C CZ  . TYR A 304 ? 0.4045 0.3770 0.6737 -0.0548 0.0726  0.0584  304 TYR A CZ  
2431  O OH  . TYR A 304 ? 0.3976 0.3674 0.6761 -0.0613 0.0710  0.0608  304 TYR A OH  
2432  N N   . GLY A 305 ? 0.3113 0.3037 0.5489 -0.0245 0.0751  0.0405  305 GLY A N   
2433  C CA  . GLY A 305 ? 0.3304 0.3229 0.5590 -0.0190 0.0742  0.0374  305 GLY A CA  
2434  C C   . GLY A 305 ? 0.3281 0.3112 0.5420 -0.0171 0.0729  0.0396  305 GLY A C   
2435  O O   . GLY A 305 ? 0.3235 0.2996 0.5339 -0.0198 0.0728  0.0438  305 GLY A O   
2436  N N   . THR A 306 ? 0.3110 0.2940 0.5164 -0.0126 0.0720  0.0372  306 THR A N   
2437  C CA  . THR A 306 ? 0.3045 0.2793 0.4971 -0.0102 0.0692  0.0386  306 THR A CA  
2438  C C   . THR A 306 ? 0.2922 0.2669 0.4833 -0.0061 0.0639  0.0341  306 THR A C   
2439  O O   . THR A 306 ? 0.2776 0.2584 0.4735 -0.0045 0.0639  0.0302  306 THR A O   
2440  C CB  . THR A 306 ? 0.3183 0.2920 0.4996 -0.0095 0.0742  0.0413  306 THR A CB  
2441  O OG1 . THR A 306 ? 0.3290 0.3097 0.5105 -0.0068 0.0765  0.0374  306 THR A OG1 
2442  C CG2 . THR A 306 ? 0.3211 0.2951 0.5034 -0.0141 0.0804  0.0463  306 THR A CG2 
2443  N N   . PRO A 307 ? 0.2878 0.2558 0.4726 -0.0042 0.0594  0.0346  307 PRO A N   
2444  C CA  . PRO A 307 ? 0.2807 0.2491 0.4646 -0.0008 0.0547  0.0306  307 PRO A CA  
2445  C C   . PRO A 307 ? 0.2922 0.2625 0.4684 0.0022  0.0553  0.0290  307 PRO A C   
2446  O O   . PRO A 307 ? 0.3093 0.2768 0.4763 0.0026  0.0576  0.0316  307 PRO A O   
2447  C CB  . PRO A 307 ? 0.2786 0.2396 0.4590 0.0001  0.0506  0.0324  307 PRO A CB  
2448  C CG  . PRO A 307 ? 0.2881 0.2436 0.4610 -0.0013 0.0530  0.0376  307 PRO A CG  
2449  C CD  . PRO A 307 ? 0.2912 0.2509 0.4694 -0.0052 0.0585  0.0391  307 PRO A CD  
2450  N N   . ARG A 308 ? 0.2984 0.2725 0.4778 0.0041  0.0530  0.0247  308 ARG A N   
2451  C CA  . ARG A 308 ? 0.2987 0.2737 0.4716 0.0070  0.0522  0.0223  308 ARG A CA  
2452  C C   . ARG A 308 ? 0.2926 0.2634 0.4605 0.0090  0.0469  0.0221  308 ARG A C   
2453  O O   . ARG A 308 ? 0.3109 0.2793 0.4822 0.0085  0.0443  0.0231  308 ARG A O   
2454  C CB  . ARG A 308 ? 0.3134 0.2935 0.4933 0.0078  0.0513  0.0180  308 ARG A CB  
2455  C CG  . ARG A 308 ? 0.3416 0.3271 0.5276 0.0066  0.0562  0.0176  308 ARG A CG  
2456  C CD  . ARG A 308 ? 0.3419 0.3318 0.5369 0.0070  0.0546  0.0140  308 ARG A CD  
2457  N NE  . ARG A 308 ? 0.3173 0.3130 0.5185 0.0067  0.0592  0.0134  308 ARG A NE  
2458  C CZ  . ARG A 308 ? 0.3057 0.3060 0.5170 0.0064  0.0584  0.0114  308 ARG A CZ  
2459  N NH1 . ARG A 308 ? 0.3089 0.3077 0.5240 0.0059  0.0533  0.0100  308 ARG A NH1 
2460  N NH2 . ARG A 308 ? 0.3214 0.3277 0.5389 0.0068  0.0628  0.0107  308 ARG A NH2 
2461  N N   . PRO A 309 ? 0.2880 0.2580 0.4486 0.0114  0.0448  0.0205  309 PRO A N   
2462  C CA  . PRO A 309 ? 0.2941 0.2607 0.4512 0.0131  0.0394  0.0207  309 PRO A CA  
2463  C C   . PRO A 309 ? 0.2946 0.2627 0.4603 0.0131  0.0357  0.0190  309 PRO A C   
2464  O O   . PRO A 309 ? 0.3308 0.2963 0.4967 0.0140  0.0325  0.0203  309 PRO A O   
2465  C CB  . PRO A 309 ? 0.2950 0.2616 0.4447 0.0150  0.0379  0.0182  309 PRO A CB  
2466  C CG  . PRO A 309 ? 0.3101 0.2771 0.4543 0.0147  0.0437  0.0188  309 PRO A CG  
2467  C CD  . PRO A 309 ? 0.3023 0.2740 0.4573 0.0126  0.0475  0.0186  309 PRO A CD  
2468  N N   . VAL A 310 ? 0.2924 0.2644 0.4652 0.0121  0.0366  0.0162  310 VAL A N   
2469  C CA  . VAL A 310 ? 0.2933 0.2668 0.4733 0.0117  0.0341  0.0145  310 VAL A CA  
2470  C C   . VAL A 310 ? 0.2872 0.2580 0.4704 0.0110  0.0341  0.0165  310 VAL A C   
2471  O O   . VAL A 310 ? 0.2869 0.2574 0.4731 0.0119  0.0316  0.0157  310 VAL A O   
2472  C CB  . VAL A 310 ? 0.2865 0.2635 0.4719 0.0105  0.0352  0.0118  310 VAL A CB  
2473  C CG1 . VAL A 310 ? 0.2861 0.2644 0.4748 0.0088  0.0388  0.0127  310 VAL A CG1 
2474  C CG2 . VAL A 310 ? 0.2781 0.2561 0.4689 0.0098  0.0328  0.0100  310 VAL A CG2 
2475  N N   . TRP A 311 ? 0.2754 0.2443 0.4583 0.0095  0.0370  0.0190  311 TRP A N   
2476  C CA  . TRP A 311 ? 0.2801 0.2452 0.4657 0.0087  0.0368  0.0208  311 TRP A CA  
2477  C C   . TRP A 311 ? 0.2690 0.2302 0.4518 0.0111  0.0336  0.0222  311 TRP A C   
2478  O O   . TRP A 311 ? 0.2499 0.2096 0.4369 0.0118  0.0321  0.0214  311 TRP A O   
2479  C CB  . TRP A 311 ? 0.2733 0.2361 0.4574 0.0064  0.0403  0.0240  311 TRP A CB  
2480  C CG  . TRP A 311 ? 0.2846 0.2425 0.4713 0.0050  0.0401  0.0261  311 TRP A CG  
2481  C CD1 . TRP A 311 ? 0.3094 0.2611 0.4916 0.0050  0.0399  0.0299  311 TRP A CD1 
2482  C CD2 . TRP A 311 ? 0.3073 0.2646 0.5006 0.0031  0.0399  0.0245  311 TRP A CD2 
2483  N NE1 . TRP A 311 ? 0.3210 0.2683 0.5072 0.0033  0.0396  0.0307  311 TRP A NE1 
2484  C CE2 . TRP A 311 ? 0.3244 0.2750 0.5172 0.0021  0.0396  0.0273  311 TRP A CE2 
2485  C CE3 . TRP A 311 ? 0.3085 0.2695 0.5073 0.0021  0.0395  0.0211  311 TRP A CE3 
2486  C CZ2 . TRP A 311 ? 0.3038 0.2513 0.5014 0.0002  0.0389  0.0263  311 TRP A CZ2 
2487  C CZ3 . TRP A 311 ? 0.3079 0.2659 0.5107 0.0002  0.0387  0.0203  311 TRP A CZ3 
2488  C CH2 . TRP A 311 ? 0.3211 0.2725 0.5234 -0.0007 0.0385  0.0226  311 TRP A CH2 
2489  N N   . PHE A 312 ? 0.2809 0.2404 0.4563 0.0124  0.0327  0.0242  312 PHE A N   
2490  C CA  . PHE A 312 ? 0.2955 0.2509 0.4674 0.0149  0.0290  0.0262  312 PHE A CA  
2491  C C   . PHE A 312 ? 0.2968 0.2560 0.4728 0.0171  0.0251  0.0232  312 PHE A C   
2492  O O   . PHE A 312 ? 0.3079 0.2659 0.4874 0.0191  0.0222  0.0234  312 PHE A O   
2493  C CB  . PHE A 312 ? 0.2861 0.2378 0.4473 0.0152  0.0292  0.0294  312 PHE A CB  
2494  C CG  . PHE A 312 ? 0.2882 0.2362 0.4460 0.0126  0.0335  0.0331  312 PHE A CG  
2495  C CD1 . PHE A 312 ? 0.3235 0.2652 0.4814 0.0121  0.0329  0.0365  312 PHE A CD1 
2496  C CD2 . PHE A 312 ? 0.2857 0.2368 0.4415 0.0104  0.0384  0.0329  312 PHE A CD2 
2497  C CE1 . PHE A 312 ? 0.3225 0.2606 0.4780 0.0089  0.0369  0.0402  312 PHE A CE1 
2498  C CE2 . PHE A 312 ? 0.2922 0.2411 0.4466 0.0076  0.0429  0.0363  312 PHE A CE2 
2499  C CZ  . PHE A 312 ? 0.3143 0.2566 0.4685 0.0064  0.0421  0.0401  312 PHE A CZ  
2500  N N   . ALA A 313 ? 0.3072 0.2712 0.4839 0.0166  0.0253  0.0203  313 ALA A N   
2501  C CA  . ALA A 313 ? 0.2850 0.2529 0.4661 0.0179  0.0219  0.0176  313 ALA A CA  
2502  C C   . ALA A 313 ? 0.2789 0.2491 0.4689 0.0175  0.0226  0.0158  313 ALA A C   
2503  O O   . ALA A 313 ? 0.2571 0.2290 0.4520 0.0192  0.0202  0.0151  313 ALA A O   
2504  C CB  . ALA A 313 ? 0.2746 0.2457 0.4537 0.0171  0.0217  0.0152  313 ALA A CB  
2505  N N   . MET A 314 ? 0.2600 0.2299 0.4518 0.0154  0.0260  0.0152  314 MET A N   
2506  C CA  . MET A 314 ? 0.2742 0.2450 0.4722 0.0149  0.0270  0.0134  314 MET A CA  
2507  C C   . MET A 314 ? 0.2771 0.2438 0.4768 0.0167  0.0264  0.0146  314 MET A C   
2508  O O   . MET A 314 ? 0.2609 0.2291 0.4657 0.0181  0.0259  0.0128  314 MET A O   
2509  C CB  . MET A 314 ? 0.2970 0.2675 0.4955 0.0121  0.0298  0.0125  314 MET A CB  
2510  C CG  . MET A 314 ? 0.3198 0.2944 0.5184 0.0108  0.0299  0.0104  314 MET A CG  
2511  S SD  . MET A 314 ? 0.3234 0.3010 0.5266 0.0104  0.0292  0.0076  314 MET A SD  
2512  C CE  . MET A 314 ? 0.2977 0.2721 0.5026 0.0091  0.0312  0.0069  314 MET A CE  
2513  N N   . ARG A 315 ? 0.2680 0.2294 0.4638 0.0166  0.0268  0.0177  315 ARG A N   
2514  C CA  . ARG A 315 ? 0.2856 0.2417 0.4825 0.0185  0.0256  0.0192  315 ARG A CA  
2515  C C   . ARG A 315 ? 0.2883 0.2461 0.4880 0.0221  0.0220  0.0189  315 ARG A C   
2516  O O   . ARG A 315 ? 0.2661 0.2236 0.4713 0.0243  0.0215  0.0174  315 ARG A O   
2517  C CB  . ARG A 315 ? 0.2860 0.2355 0.4770 0.0176  0.0260  0.0234  315 ARG A CB  
2518  C CG  . ARG A 315 ? 0.3058 0.2482 0.4976 0.0195  0.0243  0.0252  315 ARG A CG  
2519  C CD  . ARG A 315 ? 0.3266 0.2618 0.5113 0.0186  0.0240  0.0302  315 ARG A CD  
2520  N NE  . ARG A 315 ? 0.3758 0.3124 0.5544 0.0200  0.0218  0.0321  315 ARG A NE  
2521  C CZ  . ARG A 315 ? 0.3817 0.3136 0.5515 0.0193  0.0217  0.0364  315 ARG A CZ  
2522  N NH1 . ARG A 315 ? 0.3927 0.3183 0.5594 0.0168  0.0239  0.0398  315 ARG A NH1 
2523  N NH2 . ARG A 315 ? 0.3892 0.3224 0.5528 0.0207  0.0193  0.0372  315 ARG A NH2 
2524  N N   . ASP A 316 ? 0.3141 0.2739 0.5101 0.0229  0.0195  0.0200  316 ASP A N   
2525  C CA  . ASP A 316 ? 0.3381 0.2998 0.5371 0.0262  0.0151  0.0201  316 ASP A CA  
2526  C C   . ASP A 316 ? 0.3134 0.2825 0.5218 0.0268  0.0152  0.0163  316 ASP A C   
2527  O O   . ASP A 316 ? 0.3131 0.2838 0.5285 0.0297  0.0134  0.0156  316 ASP A O   
2528  C CB  . ASP A 316 ? 0.3618 0.3227 0.5531 0.0264  0.0119  0.0222  316 ASP A CB  
2529  C CG  . ASP A 316 ? 0.4308 0.3838 0.6120 0.0263  0.0115  0.0265  316 ASP A CG  
2530  O OD1 . ASP A 316 ? 0.4247 0.3719 0.6056 0.0262  0.0130  0.0287  316 ASP A OD1 
2531  O OD2 . ASP A 316 ? 0.4863 0.4384 0.6593 0.0261  0.0098  0.0278  316 ASP A OD2 
2532  N N   . TYR A 317 ? 0.2826 0.2561 0.4913 0.0240  0.0175  0.0140  317 TYR A N   
2533  C CA  . TYR A 317 ? 0.2582 0.2384 0.4743 0.0234  0.0184  0.0109  317 TYR A CA  
2534  C C   . TYR A 317 ? 0.2666 0.2466 0.4883 0.0243  0.0213  0.0091  317 TYR A C   
2535  O O   . TYR A 317 ? 0.2918 0.2768 0.5211 0.0257  0.0215  0.0072  317 TYR A O   
2536  C CB  . TYR A 317 ? 0.2424 0.2250 0.4559 0.0200  0.0202  0.0094  317 TYR A CB  
2537  C CG  . TYR A 317 ? 0.2379 0.2268 0.4581 0.0189  0.0207  0.0069  317 TYR A CG  
2538  C CD1 . TYR A 317 ? 0.2621 0.2556 0.4857 0.0192  0.0174  0.0065  317 TYR A CD1 
2539  C CD2 . TYR A 317 ? 0.2380 0.2279 0.4606 0.0174  0.0244  0.0050  317 TYR A CD2 
2540  C CE1 . TYR A 317 ? 0.2582 0.2578 0.4887 0.0177  0.0181  0.0046  317 TYR A CE1 
2541  C CE2 . TYR A 317 ? 0.2573 0.2527 0.4852 0.0160  0.0254  0.0031  317 TYR A CE2 
2542  C CZ  . TYR A 317 ? 0.2614 0.2621 0.4939 0.0160  0.0225  0.0030  317 TYR A CZ  
2543  O OH  . TYR A 317 ? 0.2307 0.2370 0.4689 0.0139  0.0240  0.0015  317 TYR A OH  
2544  N N   . MET A 318 ? 0.2604 0.2346 0.4785 0.0234  0.0237  0.0095  318 MET A N   
2545  C CA  . MET A 318 ? 0.2602 0.2329 0.4817 0.0240  0.0265  0.0072  318 MET A CA  
2546  C C   . MET A 318 ? 0.2674 0.2376 0.4935 0.0283  0.0252  0.0073  318 MET A C   
2547  O O   . MET A 318 ? 0.2665 0.2353 0.4957 0.0295  0.0275  0.0048  318 MET A O   
2548  C CB  . MET A 318 ? 0.2560 0.2228 0.4724 0.0214  0.0287  0.0075  318 MET A CB  
2549  C CG  . MET A 318 ? 0.2577 0.2272 0.4719 0.0178  0.0305  0.0062  318 MET A CG  
2550  S SD  . MET A 318 ? 0.2935 0.2566 0.5039 0.0150  0.0322  0.0061  318 MET A SD  
2551  C CE  . MET A 318 ? 0.2702 0.2286 0.4770 0.0146  0.0310  0.0104  318 MET A CE  
2552  N N   . LYS A 319 ? 0.2772 0.2464 0.5036 0.0309  0.0212  0.0099  319 LYS A N   
2553  C CA  . LYS A 319 ? 0.3187 0.2846 0.5497 0.0353  0.0192  0.0102  319 LYS A CA  
2554  C C   . LYS A 319 ? 0.3179 0.2911 0.5594 0.0381  0.0204  0.0066  319 LYS A C   
2555  O O   . LYS A 319 ? 0.3069 0.2776 0.5530 0.0415  0.0213  0.0050  319 LYS A O   
2556  C CB  . LYS A 319 ? 0.3734 0.3361 0.6014 0.0374  0.0140  0.0142  319 LYS A CB  
2557  C CG  . LYS A 319 ? 0.4214 0.3754 0.6388 0.0351  0.0136  0.0181  319 LYS A CG  
2558  C CD  . LYS A 319 ? 0.4948 0.4434 0.7089 0.0380  0.0084  0.0221  319 LYS A CD  
2559  C CE  . LYS A 319 ? 0.5725 0.5126 0.7756 0.0357  0.0082  0.0266  319 LYS A CE  
2560  N NZ  . LYS A 319 ? 0.5987 0.5378 0.7954 0.0366  0.0037  0.0299  319 LYS A NZ  
2561  N N   . GLY A 320 ? 0.2982 0.2803 0.5438 0.0365  0.0207  0.0054  320 GLY A N   
2562  C CA  . GLY A 320 ? 0.2807 0.2711 0.5371 0.0385  0.0226  0.0023  320 GLY A CA  
2563  C C   . GLY A 320 ? 0.2728 0.2705 0.5301 0.0343  0.0252  0.0007  320 GLY A C   
2564  O O   . GLY A 320 ? 0.2686 0.2696 0.5251 0.0324  0.0221  0.0022  320 GLY A O   
2565  N N   . LEU A 321 ? 0.2591 0.2582 0.5169 0.0328  0.0306  -0.0021 321 LEU A N   
2566  C CA  . LEU A 321 ? 0.2501 0.2538 0.5064 0.0283  0.0333  -0.0032 321 LEU A CA  
2567  C C   . LEU A 321 ? 0.2756 0.2892 0.5429 0.0290  0.0358  -0.0053 321 LEU A C   
2568  O O   . LEU A 321 ? 0.2577 0.2733 0.5318 0.0326  0.0384  -0.0075 321 LEU A O   
2569  C CB  . LEU A 321 ? 0.2521 0.2496 0.5001 0.0259  0.0372  -0.0045 321 LEU A CB  
2570  C CG  . LEU A 321 ? 0.2554 0.2452 0.4938 0.0239  0.0352  -0.0023 321 LEU A CG  
2571  C CD1 . LEU A 321 ? 0.2576 0.2426 0.4900 0.0216  0.0387  -0.0042 321 LEU A CD1 
2572  C CD2 . LEU A 321 ? 0.2496 0.2414 0.4849 0.0210  0.0324  -0.0002 321 LEU A CD2 
2573  N N   . ILE A 322 ? 0.2611 0.2808 0.5308 0.0256  0.0346  -0.0046 322 ILE A N   
2574  C CA  . ILE A 322 ? 0.2379 0.2676 0.5179 0.0245  0.0372  -0.0060 322 ILE A CA  
2575  C C   . ILE A 322 ? 0.2406 0.2701 0.5149 0.0197  0.0424  -0.0071 322 ILE A C   
2576  O O   . ILE A 322 ? 0.2568 0.2838 0.5244 0.0157  0.0405  -0.0056 322 ILE A O   
2577  C CB  . ILE A 322 ? 0.2295 0.2656 0.5162 0.0235  0.0319  -0.0044 322 ILE A CB  
2578  C CG1 . ILE A 322 ? 0.2392 0.2732 0.5278 0.0277  0.0255  -0.0027 322 ILE A CG1 
2579  C CG2 . ILE A 322 ? 0.2263 0.2737 0.5260 0.0223  0.0349  -0.0058 322 ILE A CG2 
2580  C CD1 . ILE A 322 ? 0.2382 0.2749 0.5283 0.0263  0.0189  -0.0009 322 ILE A CD1 
2581  N N   . ILE A 323 ? 0.2351 0.2669 0.5120 0.0204  0.0486  -0.0096 323 ILE A N   
2582  C CA  . ILE A 323 ? 0.2548 0.2861 0.5258 0.0161  0.0538  -0.0106 323 ILE A CA  
2583  C C   . ILE A 323 ? 0.2633 0.3053 0.5442 0.0134  0.0565  -0.0107 323 ILE A C   
2584  O O   . ILE A 323 ? 0.2907 0.3324 0.5667 0.0082  0.0574  -0.0095 323 ILE A O   
2585  C CB  . ILE A 323 ? 0.2920 0.3179 0.5570 0.0178  0.0592  -0.0134 323 ILE A CB  
2586  C CG1 . ILE A 323 ? 0.3023 0.3169 0.5556 0.0180  0.0564  -0.0129 323 ILE A CG1 
2587  C CG2 . ILE A 323 ? 0.3194 0.3469 0.5800 0.0136  0.0654  -0.0146 323 ILE A CG2 
2588  C CD1 . ILE A 323 ? 0.3175 0.3285 0.5730 0.0223  0.0517  -0.0118 323 ILE A CD1 
2589  N N   . SER A 324 ? 0.2482 0.2995 0.5432 0.0167  0.0579  -0.0119 324 SER A N   
2590  C CA  . SER A 324 ? 0.2471 0.3100 0.5543 0.0140  0.0596  -0.0116 324 SER A CA  
2591  C C   . SER A 324 ? 0.2599 0.3307 0.5821 0.0178  0.0543  -0.0111 324 SER A C   
2592  O O   . SER A 324 ? 0.2784 0.3477 0.6041 0.0236  0.0526  -0.0122 324 SER A O   
2593  C CB  . SER A 324 ? 0.2514 0.3203 0.5628 0.0133  0.0688  -0.0140 324 SER A CB  
2594  O OG  . SER A 324 ? 0.2697 0.3297 0.5657 0.0110  0.0733  -0.0149 324 SER A OG  
2595  N N   . PRO A 325 ? 0.2451 0.3237 0.5764 0.0146  0.0508  -0.0095 325 PRO A N   
2596  C CA  . PRO A 325 ? 0.2444 0.3242 0.5725 0.0075  0.0521  -0.0080 325 PRO A CA  
2597  C C   . PRO A 325 ? 0.2502 0.3186 0.5628 0.0051  0.0471  -0.0062 325 PRO A C   
2598  O O   . PRO A 325 ? 0.2287 0.2904 0.5354 0.0086  0.0423  -0.0058 325 PRO A O   
2599  C CB  . PRO A 325 ? 0.2473 0.3384 0.5916 0.0060  0.0482  -0.0071 325 PRO A CB  
2600  C CG  . PRO A 325 ? 0.2472 0.3378 0.5963 0.0118  0.0406  -0.0069 325 PRO A CG  
2601  C CD  . PRO A 325 ? 0.2504 0.3353 0.5945 0.0177  0.0439  -0.0087 325 PRO A CD  
2602  N N   . LYS A 326 ? 0.2538 0.3202 0.5602 -0.0009 0.0485  -0.0050 326 LYS A N   
2603  C CA  . LYS A 326 ? 0.2533 0.3090 0.5453 -0.0031 0.0447  -0.0036 326 LYS A CA  
2604  C C   . LYS A 326 ? 0.2480 0.3046 0.5427 -0.0056 0.0376  -0.0020 326 LYS A C   
2605  O O   . LYS A 326 ? 0.2306 0.2957 0.5369 -0.0081 0.0367  -0.0016 326 LYS A O   
2606  C CB  . LYS A 326 ? 0.2628 0.3139 0.5450 -0.0074 0.0502  -0.0034 326 LYS A CB  
2607  C CG  . LYS A 326 ? 0.2607 0.3077 0.5363 -0.0047 0.0557  -0.0053 326 LYS A CG  
2608  C CD  . LYS A 326 ? 0.2683 0.3118 0.5348 -0.0090 0.0615  -0.0052 326 LYS A CD  
2609  C CE  . LYS A 326 ? 0.2958 0.3316 0.5518 -0.0064 0.0643  -0.0070 326 LYS A CE  
2610  N NZ  . LYS A 326 ? 0.3196 0.3602 0.5827 -0.0018 0.0690  -0.0098 326 LYS A NZ  
2611  N N   . ASN A 327 ? 0.2330 0.2809 0.5173 -0.0050 0.0327  -0.0013 327 ASN A N   
2612  C CA  . ASN A 327 ? 0.2481 0.2948 0.5323 -0.0071 0.0259  -0.0003 327 ASN A CA  
2613  C C   . ASN A 327 ? 0.2381 0.2843 0.5209 -0.0134 0.0272  0.0006  327 ASN A C   
2614  O O   . ASN A 327 ? 0.2312 0.2720 0.5051 -0.0155 0.0311  0.0009  327 ASN A O   
2615  C CB  . ASN A 327 ? 0.2465 0.2843 0.5197 -0.0043 0.0213  -0.0001 327 ASN A CB  
2616  C CG  . ASN A 327 ? 0.2533 0.2891 0.5251 -0.0055 0.0142  0.0003  327 ASN A CG  
2617  O OD1 . ASN A 327 ? 0.2458 0.2871 0.5262 -0.0050 0.0099  0.0003  327 ASN A OD1 
2618  N ND2 . ASN A 327 ? 0.2889 0.3165 0.5496 -0.0066 0.0125  0.0004  327 ASN A ND2 
2619  N N   . LYS A 328 ? 0.2221 0.2732 0.5132 -0.0164 0.0232  0.0011  328 LYS A N   
2620  C CA  . LYS A 328 ? 0.2518 0.3022 0.5429 -0.0229 0.0232  0.0023  328 LYS A CA  
2621  C C   . LYS A 328 ? 0.2458 0.3021 0.5418 -0.0261 0.0314  0.0029  328 LYS A C   
2622  O O   . LYS A 328 ? 0.2236 0.2757 0.5135 -0.0310 0.0339  0.0043  328 LYS A O   
2623  C CB  . LYS A 328 ? 0.2722 0.3108 0.5490 -0.0245 0.0204  0.0028  328 LYS A CB  
2624  C CG  . LYS A 328 ? 0.2972 0.3298 0.5678 -0.0210 0.0134  0.0019  328 LYS A CG  
2625  C CD  . LYS A 328 ? 0.3262 0.3620 0.6042 -0.0222 0.0066  0.0016  328 LYS A CD  
2626  C CE  . LYS A 328 ? 0.3069 0.3369 0.5780 -0.0187 0.0000  0.0005  328 LYS A CE  
2627  N NZ  . LYS A 328 ? 0.2975 0.3174 0.5566 -0.0198 -0.0014 0.0002  328 LYS A NZ  
2628  N N   . SER A 329 ? 0.2495 0.3155 0.5567 -0.0234 0.0354  0.0019  329 SER A N   
2629  C CA  . SER A 329 ? 0.2560 0.3286 0.5684 -0.0259 0.0441  0.0020  329 SER A CA  
2630  C C   . SER A 329 ? 0.2941 0.3785 0.6233 -0.0299 0.0441  0.0028  329 SER A C   
2631  O O   . SER A 329 ? 0.3032 0.3926 0.6426 -0.0286 0.0377  0.0025  329 SER A O   
2632  C CB  . SER A 329 ? 0.2360 0.3113 0.5497 -0.0201 0.0495  -0.0002 329 SER A CB  
2633  O OG  . SER A 329 ? 0.2103 0.2927 0.5362 -0.0150 0.0460  -0.0014 329 SER A OG  
2634  N N   . ILE A 330 ? 0.3239 0.4130 0.6561 -0.0350 0.0516  0.0038  330 ILE A N   
2635  C CA  . ILE A 330 ? 0.3284 0.4296 0.6775 -0.0397 0.0527  0.0049  330 ILE A CA  
2636  C C   . ILE A 330 ? 0.3352 0.4489 0.6968 -0.0374 0.0617  0.0033  330 ILE A C   
2637  O O   . ILE A 330 ? 0.3259 0.4369 0.6790 -0.0363 0.0695  0.0025  330 ILE A O   
2638  C CB  . ILE A 330 ? 0.3475 0.4434 0.6900 -0.0482 0.0538  0.0079  330 ILE A CB  
2639  C CG1 . ILE A 330 ? 0.3548 0.4386 0.6867 -0.0494 0.0441  0.0087  330 ILE A CG1 
2640  C CG2 . ILE A 330 ? 0.3399 0.4486 0.6998 -0.0545 0.0569  0.0095  330 ILE A CG2 
2641  C CD1 . ILE A 330 ? 0.3921 0.4640 0.7086 -0.0546 0.0450  0.0110  330 ILE A CD1 
2642  N N   . HIS A 331 ? 0.3408 0.4682 0.7229 -0.0364 0.0604  0.0027  331 HIS A N   
2643  C CA  . HIS A 331 ? 0.3367 0.4773 0.7334 -0.0330 0.0683  0.0007  331 HIS A CA  
2644  C C   . HIS A 331 ? 0.3417 0.4978 0.7593 -0.0385 0.0709  0.0019  331 HIS A C   
2645  O O   . HIS A 331 ? 0.3274 0.4863 0.7540 -0.0418 0.0627  0.0034  331 HIS A O   
2646  C CB  . HIS A 331 ? 0.3252 0.4676 0.7276 -0.0238 0.0639  -0.0020 331 HIS A CB  
2647  C CG  . HIS A 331 ? 0.3217 0.4500 0.7044 -0.0190 0.0639  -0.0031 331 HIS A CG  
2648  N ND1 . HIS A 331 ? 0.3193 0.4462 0.6964 -0.0153 0.0723  -0.0054 331 HIS A ND1 
2649  C CD2 . HIS A 331 ? 0.3260 0.4411 0.6931 -0.0182 0.0571  -0.0024 331 HIS A CD2 
2650  C CE1 . HIS A 331 ? 0.3273 0.4405 0.6866 -0.0127 0.0699  -0.0057 331 HIS A CE1 
2651  N NE2 . HIS A 331 ? 0.3214 0.4279 0.6751 -0.0142 0.0609  -0.0039 331 HIS A NE2 
2652  N N   . THR A 332 ? 0.3675 0.5330 0.7921 -0.0399 0.0825  0.0013  332 THR A N   
2653  C CA  . THR A 332 ? 0.3806 0.5620 0.8257 -0.0455 0.0870  0.0026  332 THR A CA  
2654  C C   . THR A 332 ? 0.4223 0.6187 0.8850 -0.0395 0.0948  -0.0007 332 THR A C   
2655  O O   . THR A 332 ? 0.6067 0.8169 1.0842 -0.0430 0.1035  -0.0005 332 THR A O   
2656  C CB  . THR A 332 ? 0.3676 0.5455 0.8032 -0.0549 0.0945  0.0057  332 THR A CB  
2657  O OG1 . THR A 332 ? 0.4154 0.5852 0.8335 -0.0519 0.1029  0.0042  332 THR A OG1 
2658  C CG2 . THR A 332 ? 0.3519 0.5152 0.7721 -0.0610 0.0866  0.0090  332 THR A CG2 
2659  N N   . ASN A 333 ? 0.4704 0.6646 0.9330 -0.0301 0.0910  -0.0037 333 ASN A N   
2660  C CA  . ASN A 333 ? 0.4709 0.6777 0.9501 -0.0228 0.0966  -0.0073 333 ASN A CA  
2661  C C   . ASN A 333 ? 0.4604 0.6704 0.9523 -0.0165 0.0846  -0.0081 333 ASN A C   
2662  O O   . ASN A 333 ? 0.5655 0.7652 1.0479 -0.0173 0.0736  -0.0064 333 ASN A O   
2663  C CB  . ASN A 333 ? 0.5398 0.7372 1.0018 -0.0176 0.1047  -0.0101 333 ASN A CB  
2664  C CG  . ASN A 333 ? 0.6543 0.8645 1.1298 -0.0130 0.1163  -0.0138 333 ASN A CG  
2665  O OD1 . ASN A 333 ? 0.6048 0.8264 1.1003 -0.0064 0.1145  -0.0162 333 ASN A OD1 
2666  N ND2 . ASN A 333 ? 0.7225 0.9304 1.1866 -0.0159 0.1283  -0.0145 333 ASN A ND2 
2667  N N   . THR A 334 ? 0.3994 0.6235 0.9129 -0.0102 0.0864  -0.0108 334 THR A N   
2668  C CA  . THR A 334 ? 0.3686 0.5937 0.8916 -0.0027 0.0753  -0.0118 334 THR A CA  
2669  C C   . THR A 334 ? 0.3657 0.5792 0.8743 0.0060  0.0763  -0.0144 334 THR A C   
2670  O O   . THR A 334 ? 0.3307 0.5397 0.8399 0.0122  0.0669  -0.0148 334 THR A O   
2671  C CB  . THR A 334 ? 0.3980 0.6439 0.9527 0.0000  0.0752  -0.0131 334 THR A CB  
2672  O OG1 . THR A 334 ? 0.4041 0.6600 0.9678 0.0032  0.0887  -0.0162 334 THR A OG1 
2673  C CG2 . THR A 334 ? 0.4122 0.6707 0.9838 -0.0089 0.0733  -0.0104 334 THR A CG2 
2674  N N   . LYS A 335 ? 0.3811 0.5894 0.8768 0.0063  0.0875  -0.0162 335 LYS A N   
2675  C CA  . LYS A 335 ? 0.3803 0.5767 0.8614 0.0137  0.0890  -0.0189 335 LYS A CA  
2676  C C   . LYS A 335 ? 0.3695 0.5475 0.8226 0.0097  0.0878  -0.0171 335 LYS A C   
2677  O O   . LYS A 335 ? 0.3858 0.5617 0.8293 0.0030  0.0945  -0.0160 335 LYS A O   
2678  C CB  . LYS A 335 ? 0.4544 0.6568 0.9396 0.0175  0.1023  -0.0229 335 LYS A CB  
2679  C CG  . LYS A 335 ? 0.4685 0.6905 0.9830 0.0224  0.1058  -0.0256 335 LYS A CG  
2680  C CD  . LYS A 335 ? 0.4986 0.7226 1.0265 0.0311  0.0954  -0.0265 335 LYS A CD  
2681  C CE  . LYS A 335 ? 0.5648 0.8084 1.1220 0.0365  0.0998  -0.0295 335 LYS A CE  
2682  N NZ  . LYS A 335 ? 0.5820 0.8263 1.1513 0.0456  0.0897  -0.0305 335 LYS A NZ  
2683  N N   . ILE A 336 ? 0.3527 0.5182 0.7943 0.0140  0.0791  -0.0167 336 ILE A N   
2684  C CA  . ILE A 336 ? 0.3673 0.5158 0.7846 0.0113  0.0757  -0.0150 336 ILE A CA  
2685  C C   . ILE A 336 ? 0.3510 0.4890 0.7561 0.0178  0.0783  -0.0176 336 ILE A C   
2686  O O   . ILE A 336 ? 0.3272 0.4648 0.7385 0.0250  0.0740  -0.0190 336 ILE A O   
2687  C CB  . ILE A 336 ? 0.3946 0.5381 0.8098 0.0103  0.0629  -0.0121 336 ILE A CB  
2688  C CG1 . ILE A 336 ? 0.4382 0.5910 0.8652 0.0037  0.0595  -0.0098 336 ILE A CG1 
2689  C CG2 . ILE A 336 ? 0.4148 0.5413 0.8065 0.0088  0.0591  -0.0107 336 ILE A CG2 
2690  C CD1 . ILE A 336 ? 0.4478 0.6030 0.8715 -0.0042 0.0677  -0.0088 336 ILE A CD1 
2691  N N   . PRO A 337 ? 0.3198 0.4485 0.7075 0.0156  0.0851  -0.0185 337 PRO A N   
2692  C CA  . PRO A 337 ? 0.2981 0.4150 0.6728 0.0210  0.0859  -0.0208 337 PRO A CA  
2693  C C   . PRO A 337 ? 0.2854 0.3919 0.6523 0.0234  0.0752  -0.0188 337 PRO A C   
2694  O O   . PRO A 337 ? 0.2557 0.3586 0.6168 0.0189  0.0691  -0.0157 337 PRO A O   
2695  C CB  . PRO A 337 ? 0.3002 0.4087 0.6566 0.0165  0.0932  -0.0213 337 PRO A CB  
2696  C CG  . PRO A 337 ? 0.3223 0.4419 0.6866 0.0103  0.0998  -0.0203 337 PRO A CG  
2697  C CD  . PRO A 337 ? 0.3075 0.4373 0.6884 0.0081  0.0927  -0.0176 337 PRO A CD  
2698  N N   . LEU A 338 ? 0.2857 0.3881 0.6540 0.0307  0.0732  -0.0206 338 LEU A N   
2699  C CA  . LEU A 338 ? 0.2973 0.3881 0.6560 0.0334  0.0648  -0.0190 338 LEU A CA  
2700  C C   . LEU A 338 ? 0.2942 0.3722 0.6373 0.0354  0.0682  -0.0209 338 LEU A C   
2701  O O   . LEU A 338 ? 0.2666 0.3450 0.6125 0.0397  0.0740  -0.0244 338 LEU A O   
2702  C CB  . LEU A 338 ? 0.3291 0.4250 0.7026 0.0399  0.0587  -0.0190 338 LEU A CB  
2703  C CG  . LEU A 338 ? 0.3410 0.4250 0.7056 0.0436  0.0505  -0.0172 338 LEU A CG  
2704  C CD1 . LEU A 338 ? 0.3393 0.4187 0.6952 0.0391  0.0431  -0.0134 338 LEU A CD1 
2705  C CD2 . LEU A 338 ? 0.3791 0.4670 0.7579 0.0510  0.0457  -0.0177 338 LEU A CD2 
2706  N N   . GLU A 339 ? 0.3307 0.3971 0.6577 0.0324  0.0643  -0.0187 339 GLU A N   
2707  C CA  . GLU A 339 ? 0.3184 0.3722 0.6308 0.0336  0.0661  -0.0200 339 GLU A CA  
2708  C C   . GLU A 339 ? 0.3234 0.3675 0.6276 0.0343  0.0581  -0.0172 339 GLU A C   
2709  O O   . GLU A 339 ? 0.3127 0.3552 0.6113 0.0300  0.0541  -0.0143 339 GLU A O   
2710  C CB  . GLU A 339 ? 0.3244 0.3742 0.6239 0.0279  0.0714  -0.0205 339 GLU A CB  
2711  C CG  . GLU A 339 ? 0.3361 0.3928 0.6396 0.0273  0.0808  -0.0236 339 GLU A CG  
2712  C CD  . GLU A 339 ? 0.3633 0.4131 0.6510 0.0222  0.0857  -0.0241 339 GLU A CD  
2713  O OE1 . GLU A 339 ? 0.3782 0.4287 0.6615 0.0162  0.0848  -0.0213 339 GLU A OE1 
2714  O OE2 . GLU A 339 ? 0.3726 0.4153 0.6516 0.0243  0.0898  -0.0272 339 GLU A OE2 
2715  N N   . LEU A 340 ? 0.3154 0.3525 0.6183 0.0395  0.0564  -0.0181 340 LEU A N   
2716  C CA  . LEU A 340 ? 0.3101 0.3379 0.6056 0.0402  0.0495  -0.0152 340 LEU A CA  
2717  C C   . LEU A 340 ? 0.3018 0.3173 0.5855 0.0410  0.0510  -0.0164 340 LEU A C   
2718  O O   . LEU A 340 ? 0.3438 0.3575 0.6279 0.0436  0.0559  -0.0199 340 LEU A O   
2719  C CB  . LEU A 340 ? 0.3065 0.3368 0.6123 0.0455  0.0437  -0.0139 340 LEU A CB  
2720  C CG  . LEU A 340 ? 0.3134 0.3552 0.6314 0.0449  0.0401  -0.0124 340 LEU A CG  
2721  C CD1 . LEU A 340 ? 0.3213 0.3624 0.6468 0.0508  0.0333  -0.0109 340 LEU A CD1 
2722  C CD2 . LEU A 340 ? 0.3116 0.3532 0.6223 0.0389  0.0369  -0.0095 340 LEU A CD2 
2723  N N   . TYR A 341 ? 0.3004 0.3077 0.5742 0.0388  0.0467  -0.0135 341 TYR A N   
2724  C CA  . TYR A 341 ? 0.3034 0.2988 0.5673 0.0393  0.0466  -0.0138 341 TYR A CA  
2725  C C   . TYR A 341 ? 0.2999 0.2896 0.5623 0.0410  0.0403  -0.0101 341 TYR A C   
2726  O O   . TYR A 341 ? 0.2855 0.2738 0.5422 0.0376  0.0372  -0.0070 341 TYR A O   
2727  C CB  . TYR A 341 ? 0.3043 0.2945 0.5563 0.0339  0.0487  -0.0140 341 TYR A CB  
2728  C CG  . TYR A 341 ? 0.3049 0.2840 0.5492 0.0348  0.0495  -0.0156 341 TYR A CG  
2729  C CD1 . TYR A 341 ? 0.3023 0.2791 0.5464 0.0371  0.0541  -0.0200 341 TYR A CD1 
2730  C CD2 . TYR A 341 ? 0.3135 0.2842 0.5508 0.0331  0.0458  -0.0130 341 TYR A CD2 
2731  C CE1 . TYR A 341 ? 0.3074 0.2732 0.5441 0.0378  0.0543  -0.0219 341 TYR A CE1 
2732  C CE2 . TYR A 341 ? 0.3268 0.2873 0.5579 0.0333  0.0461  -0.0145 341 TYR A CE2 
2733  C CZ  . TYR A 341 ? 0.3320 0.2896 0.5626 0.0357  0.0499  -0.0190 341 TYR A CZ  
2734  O OH  . TYR A 341 ? 0.3099 0.2564 0.5339 0.0359  0.0497  -0.0209 341 TYR A OH  
2735  N N   . ASN A 342 ? 0.3118 0.2979 0.5790 0.0464  0.0385  -0.0106 342 ASN A N   
2736  C CA  . ASN A 342 ? 0.3172 0.2980 0.5838 0.0486  0.0324  -0.0068 342 ASN A CA  
2737  C C   . ASN A 342 ? 0.3218 0.2897 0.5791 0.0483  0.0316  -0.0058 342 ASN A C   
2738  O O   . ASN A 342 ? 0.3634 0.3259 0.6195 0.0498  0.0346  -0.0090 342 ASN A O   
2739  C CB  . ASN A 342 ? 0.3013 0.2857 0.5796 0.0549  0.0297  -0.0073 342 ASN A CB  
2740  C CG  . ASN A 342 ? 0.2989 0.2969 0.5883 0.0551  0.0298  -0.0080 342 ASN A CG  
2741  O OD1 . ASN A 342 ? 0.2952 0.2969 0.5822 0.0514  0.0271  -0.0055 342 ASN A OD1 
2742  N ND2 . ASN A 342 ? 0.2966 0.3022 0.5982 0.0590  0.0329  -0.0115 342 ASN A ND2 
2743  N N   . ASP A 343 ? 0.3450 0.3073 0.5960 0.0465  0.0274  -0.0014 343 ASP A N   
2744  C CA  . ASP A 343 ? 0.3821 0.3321 0.6262 0.0464  0.0262  0.0001  343 ASP A CA  
2745  C C   . ASP A 343 ? 0.3547 0.3000 0.6039 0.0524  0.0225  0.0010  343 ASP A C   
2746  O O   . ASP A 343 ? 0.3418 0.2941 0.5997 0.0561  0.0206  0.0007  343 ASP A O   
2747  C CB  . ASP A 343 ? 0.3795 0.3255 0.6144 0.0415  0.0247  0.0042  343 ASP A CB  
2748  C CG  . ASP A 343 ? 0.4011 0.3455 0.6338 0.0422  0.0198  0.0092  343 ASP A CG  
2749  O OD1 . ASP A 343 ? 0.4384 0.3833 0.6766 0.0469  0.0163  0.0099  343 ASP A OD1 
2750  O OD2 . ASP A 343 ? 0.4375 0.3806 0.6630 0.0382  0.0196  0.0121  343 ASP A OD2 
2751  N N   . LYS A 344 ? 0.4172 0.3504 0.6613 0.0528  0.0208  0.0026  344 LYS A N   
2752  C CA  . LYS A 344 ? 0.4853 0.4115 0.7339 0.0589  0.0177  0.0027  344 LYS A CA  
2753  C C   . LYS A 344 ? 0.4401 0.3663 0.6903 0.0614  0.0114  0.0076  344 LYS A C   
2754  O O   . LYS A 344 ? 0.4472 0.3695 0.7031 0.0672  0.0079  0.0077  344 LYS A O   
2755  C CB  . LYS A 344 ? 0.5769 0.4889 0.8193 0.0583  0.0177  0.0026  344 LYS A CB  
2756  C CG  . LYS A 344 ? 0.7381 0.6417 0.9707 0.0534  0.0153  0.0082  344 LYS A CG  
2757  C CD  . LYS A 344 ? 0.9141 0.8073 1.1403 0.0496  0.0171  0.0073  344 LYS A CD  
2758  C CE  . LYS A 344 ? 0.9535 0.8396 1.1716 0.0444  0.0152  0.0133  344 LYS A CE  
2759  N NZ  . LYS A 344 ? 0.9044 0.7991 1.1196 0.0406  0.0158  0.0165  344 LYS A NZ  
2760  N N   . ASP A 345 ? 0.4026 0.3339 0.6484 0.0576  0.0099  0.0110  345 ASP A N   
2761  C CA  . ASP A 345 ? 0.4064 0.3371 0.6511 0.0593  0.0037  0.0157  345 ASP A CA  
2762  C C   . ASP A 345 ? 0.3988 0.3414 0.6542 0.0627  0.0013  0.0141  345 ASP A C   
2763  O O   . ASP A 345 ? 0.3695 0.3112 0.6264 0.0658  -0.0050 0.0172  345 ASP A O   
2764  C CB  . ASP A 345 ? 0.4215 0.3498 0.6545 0.0537  0.0033  0.0201  345 ASP A CB  
2765  C CG  . ASP A 345 ? 0.4457 0.3617 0.6692 0.0506  0.0042  0.0232  345 ASP A CG  
2766  O OD1 . ASP A 345 ? 0.5000 0.4066 0.7245 0.0535  0.0026  0.0236  345 ASP A OD1 
2767  O OD2 . ASP A 345 ? 0.4435 0.3596 0.6593 0.0454  0.0063  0.0252  345 ASP A OD2 
2768  N N   . VAL A 346 ? 0.3814 0.3348 0.6442 0.0619  0.0060  0.0095  346 VAL A N   
2769  C CA  . VAL A 346 ? 0.3537 0.3195 0.6282 0.0643  0.0045  0.0078  346 VAL A CA  
2770  C C   . VAL A 346 ? 0.3861 0.3532 0.6733 0.0713  0.0037  0.0051  346 VAL A C   
2771  O O   . VAL A 346 ? 0.3952 0.3611 0.6852 0.0728  0.0090  0.0010  346 VAL A O   
2772  C CB  . VAL A 346 ? 0.3497 0.3259 0.6269 0.0603  0.0105  0.0042  346 VAL A CB  
2773  C CG1 . VAL A 346 ? 0.3336 0.3230 0.6250 0.0626  0.0096  0.0022  346 VAL A CG1 
2774  C CG2 . VAL A 346 ? 0.3470 0.3225 0.6129 0.0538  0.0111  0.0065  346 VAL A CG2 
2775  N N   . LYS A 347 ? 0.3856 0.3545 0.6798 0.0758  -0.0032 0.0073  347 LYS A N   
2776  C CA  . LYS A 347 ? 0.3913 0.3619 0.6991 0.0832  -0.0049 0.0049  347 LYS A CA  
2777  C C   . LYS A 347 ? 0.3875 0.3737 0.7115 0.0855  -0.0065 0.0030  347 LYS A C   
2778  O O   . LYS A 347 ? 0.3909 0.3818 0.7293 0.0919  -0.0071 0.0003  347 LYS A O   
2779  C CB  . LYS A 347 ? 0.4244 0.3839 0.7300 0.0879  -0.0132 0.0092  347 LYS A CB  
2780  C CG  . LYS A 347 ? 0.4534 0.3961 0.7442 0.0861  -0.0131 0.0121  347 LYS A CG  
2781  C CD  . LYS A 347 ? 0.4645 0.4023 0.7548 0.0863  -0.0061 0.0076  347 LYS A CD  
2782  C CE  . LYS A 347 ? 0.5028 0.4252 0.7783 0.0827  -0.0064 0.0110  347 LYS A CE  
2783  N NZ  . LYS A 347 ? 0.5272 0.4439 0.8022 0.0831  -0.0007 0.0064  347 LYS A NZ  
2784  N N   . LYS A 348 ? 0.3719 0.3658 0.6939 0.0806  -0.0077 0.0045  348 LYS A N   
2785  C CA  . LYS A 348 ? 0.3629 0.3721 0.7006 0.0816  -0.0093 0.0028  348 LYS A CA  
2786  C C   . LYS A 348 ? 0.3261 0.3422 0.6592 0.0744  -0.0067 0.0028  348 LYS A C   
2787  O O   . LYS A 348 ? 0.3049 0.3142 0.6232 0.0699  -0.0083 0.0058  348 LYS A O   
2788  C CB  . LYS A 348 ? 0.3706 0.3803 0.7148 0.0860  -0.0199 0.0061  348 LYS A CB  
2789  C CG  . LYS A 348 ? 0.3805 0.4062 0.7441 0.0879  -0.0223 0.0041  348 LYS A CG  
2790  C CD  . LYS A 348 ? 0.4037 0.4298 0.7746 0.0927  -0.0338 0.0072  348 LYS A CD  
2791  C CE  . LYS A 348 ? 0.4454 0.4643 0.8008 0.0887  -0.0415 0.0121  348 LYS A CE  
2792  N NZ  . LYS A 348 ? 0.4757 0.4962 0.8382 0.0927  -0.0532 0.0149  348 LYS A NZ  
2793  N N   . VAL A 349 ? 0.3370 0.3668 0.6833 0.0735  -0.0025 -0.0006 349 VAL A N   
2794  C CA  . VAL A 349 ? 0.3333 0.3705 0.6778 0.0670  -0.0009 -0.0006 349 VAL A CA  
2795  C C   . VAL A 349 ? 0.3340 0.3852 0.6958 0.0679  -0.0049 -0.0011 349 VAL A C   
2796  O O   . VAL A 349 ? 0.3225 0.3836 0.7015 0.0717  -0.0023 -0.0040 349 VAL A O   
2797  C CB  . VAL A 349 ? 0.3440 0.3833 0.6856 0.0633  0.0093  -0.0039 349 VAL A CB  
2798  C CG1 . VAL A 349 ? 0.3494 0.3960 0.6898 0.0566  0.0106  -0.0037 349 VAL A CG1 
2799  C CG2 . VAL A 349 ? 0.3426 0.3681 0.6679 0.0622  0.0122  -0.0033 349 VAL A CG2 
2800  N N   . VAL A 350 ? 0.3108 0.3627 0.6678 0.0640  -0.0111 0.0015  350 VAL A N   
2801  C CA  . VAL A 350 ? 0.2943 0.3590 0.6664 0.0633  -0.0158 0.0012  350 VAL A CA  
2802  C C   . VAL A 350 ? 0.2717 0.3410 0.6398 0.0558  -0.0129 0.0008  350 VAL A C   
2803  O O   . VAL A 350 ? 0.2610 0.3213 0.6119 0.0518  -0.0120 0.0021  350 VAL A O   
2804  C CB  . VAL A 350 ? 0.2969 0.3576 0.6677 0.0662  -0.0277 0.0046  350 VAL A CB  
2805  C CG1 . VAL A 350 ? 0.3096 0.3826 0.6949 0.0648  -0.0341 0.0044  350 VAL A CG1 
2806  C CG2 . VAL A 350 ? 0.2985 0.3543 0.6741 0.0738  -0.0312 0.0053  350 VAL A CG2 
2807  N N   . VAL A 351 ? 0.2676 0.3510 0.6527 0.0540  -0.0116 -0.0011 351 VAL A N   
2808  C CA  . VAL A 351 ? 0.2372 0.3258 0.6214 0.0469  -0.0107 -0.0012 351 VAL A CA  
2809  C C   . VAL A 351 ? 0.2321 0.3300 0.6303 0.0465  -0.0195 -0.0004 351 VAL A C   
2810  O O   . VAL A 351 ? 0.2047 0.3137 0.6226 0.0502  -0.0210 -0.0015 351 VAL A O   
2811  C CB  . VAL A 351 ? 0.2312 0.3272 0.6207 0.0431  0.0001  -0.0038 351 VAL A CB  
2812  C CG1 . VAL A 351 ? 0.2332 0.3321 0.6198 0.0354  0.0001  -0.0032 351 VAL A CG1 
2813  C CG2 . VAL A 351 ? 0.2337 0.3203 0.6097 0.0437  0.0081  -0.0048 351 VAL A CG2 
2814  N N   . LYS A 352 ? 0.2381 0.3317 0.6262 0.0419  -0.0253 0.0012  352 LYS A N   
2815  C CA  . LYS A 352 ? 0.2641 0.3644 0.6624 0.0408  -0.0350 0.0020  352 LYS A CA  
2816  C C   . LYS A 352 ? 0.2424 0.3471 0.6412 0.0331  -0.0338 0.0013  352 LYS A C   
2817  O O   . LYS A 352 ? 0.2524 0.3497 0.6362 0.0290  -0.0290 0.0013  352 LYS A O   
2818  C CB  . LYS A 352 ? 0.3103 0.3987 0.6938 0.0429  -0.0454 0.0046  352 LYS A CB  
2819  C CG  . LYS A 352 ? 0.3269 0.4137 0.7159 0.0503  -0.0521 0.0060  352 LYS A CG  
2820  C CD  . LYS A 352 ? 0.3689 0.4399 0.7361 0.0517  -0.0587 0.0090  352 LYS A CD  
2821  C CE  . LYS A 352 ? 0.4244 0.4929 0.7966 0.0590  -0.0650 0.0108  352 LYS A CE  
2822  N NZ  . LYS A 352 ? 0.4742 0.5268 0.8252 0.0608  -0.0702 0.0142  352 LYS A NZ  
2823  N N   . PHE A 353 ? 0.2216 0.3383 0.6385 0.0312  -0.0386 0.0009  353 PHE A N   
2824  C CA  . PHE A 353 ? 0.2095 0.3293 0.6274 0.0239  -0.0405 0.0007  353 PHE A CA  
2825  C C   . PHE A 353 ? 0.2179 0.3390 0.6408 0.0241  -0.0539 0.0017  353 PHE A C   
2826  O O   . PHE A 353 ? 0.2474 0.3782 0.6886 0.0277  -0.0588 0.0016  353 PHE A O   
2827  C CB  . PHE A 353 ? 0.2033 0.3371 0.6389 0.0198  -0.0317 -0.0007 353 PHE A CB  
2828  C CG  . PHE A 353 ? 0.1977 0.3344 0.6351 0.0115  -0.0336 -0.0006 353 PHE A CG  
2829  C CD1 . PHE A 353 ? 0.1875 0.3116 0.6044 0.0071  -0.0337 -0.0001 353 PHE A CD1 
2830  C CD2 . PHE A 353 ? 0.1901 0.3415 0.6501 0.0083  -0.0364 -0.0008 353 PHE A CD2 
2831  C CE1 . PHE A 353 ? 0.1977 0.3227 0.6156 -0.0001 -0.0367 0.0000  353 PHE A CE1 
2832  C CE2 . PHE A 353 ? 0.1892 0.3417 0.6503 0.0005  -0.0394 -0.0005 353 PHE A CE2 
2833  C CZ  . PHE A 353 ? 0.1955 0.3342 0.6351 -0.0037 -0.0395 -0.0001 353 PHE A CZ  
2834  N N   . ARG A 354 ? 0.2236 0.3346 0.6303 0.0205  -0.0602 0.0023  354 ARG A N   
2835  C CA  . ARG A 354 ? 0.2408 0.3514 0.6497 0.0201  -0.0734 0.0028  354 ARG A CA  
2836  C C   . ARG A 354 ? 0.2537 0.3632 0.6655 0.0275  -0.0808 0.0042  354 ARG A C   
2837  O O   . ARG A 354 ? 0.2594 0.3768 0.6865 0.0288  -0.0901 0.0044  354 ARG A O   
2838  C CB  . ARG A 354 ? 0.2462 0.3713 0.6775 0.0151  -0.0763 0.0019  354 ARG A CB  
2839  C CG  . ARG A 354 ? 0.2483 0.3719 0.6743 0.0070  -0.0714 0.0011  354 ARG A CG  
2840  C CD  . ARG A 354 ? 0.2309 0.3679 0.6786 0.0012  -0.0750 0.0006  354 ARG A CD  
2841  N NE  . ARG A 354 ? 0.2263 0.3618 0.6700 -0.0066 -0.0694 0.0002  354 ARG A NE  
2842  C CZ  . ARG A 354 ? 0.2163 0.3631 0.6779 -0.0130 -0.0691 0.0001  354 ARG A CZ  
2843  N NH1 . ARG A 354 ? 0.2227 0.3839 0.7082 -0.0126 -0.0742 0.0001  354 ARG A NH1 
2844  N NH2 . ARG A 354 ? 0.2131 0.3572 0.6698 -0.0200 -0.0634 0.0002  354 ARG A NH2 
2845  N N   . ASP A 355 ? 0.2543 0.3536 0.6513 0.0323  -0.0768 0.0053  355 ASP A N   
2846  C CA  . ASP A 355 ? 0.2659 0.3591 0.6587 0.0389  -0.0843 0.0072  355 ASP A CA  
2847  C C   . ASP A 355 ? 0.2647 0.3700 0.6811 0.0444  -0.0838 0.0069  355 ASP A C   
2848  O O   . ASP A 355 ? 0.2767 0.3783 0.6934 0.0503  -0.0913 0.0086  355 ASP A O   
2849  C CB  . ASP A 355 ? 0.2772 0.3635 0.6606 0.0383  -0.0978 0.0085  355 ASP A CB  
2850  C CG  . ASP A 355 ? 0.3039 0.3784 0.6644 0.0333  -0.0974 0.0081  355 ASP A CG  
2851  O OD1 . ASP A 355 ? 0.3097 0.3725 0.6503 0.0343  -0.0915 0.0090  355 ASP A OD1 
2852  O OD2 . ASP A 355 ? 0.3030 0.3808 0.6670 0.0280  -0.1020 0.0067  355 ASP A OD2 
2853  N N   . LYS A 356 ? 0.2648 0.3832 0.6990 0.0427  -0.0744 0.0047  356 LYS A N   
2854  C CA  . LYS A 356 ? 0.2718 0.4029 0.7294 0.0480  -0.0717 0.0036  356 LYS A CA  
2855  C C   . LYS A 356 ? 0.2527 0.3823 0.7073 0.0502  -0.0582 0.0022  356 LYS A C   
2856  O O   . LYS A 356 ? 0.2551 0.3834 0.7019 0.0453  -0.0486 0.0011  356 LYS A O   
2857  C CB  . LYS A 356 ? 0.2810 0.4304 0.7643 0.0443  -0.0727 0.0021  356 LYS A CB  
2858  C CG  . LYS A 356 ? 0.2996 0.4655 0.8097 0.0481  -0.0662 0.0001  356 LYS A CG  
2859  C CD  . LYS A 356 ? 0.3468 0.5305 0.8817 0.0434  -0.0689 -0.0008 356 LYS A CD  
2860  C CE  . LYS A 356 ? 0.3883 0.5874 0.9418 0.0413  -0.0555 -0.0032 356 LYS A CE  
2861  N NZ  . LYS A 356 ? 0.4019 0.6179 0.9848 0.0469  -0.0556 -0.0047 356 LYS A NZ  
2862  N N   . VAL A 357 ? 0.2409 0.3698 0.7013 0.0578  -0.0582 0.0022  357 VAL A N   
2863  C CA  . VAL A 357 ? 0.2290 0.3561 0.6879 0.0609  -0.0467 0.0005  357 VAL A CA  
2864  C C   . VAL A 357 ? 0.2198 0.3633 0.6986 0.0587  -0.0368 -0.0027 357 VAL A C   
2865  O O   . VAL A 357 ? 0.2020 0.3601 0.7046 0.0608  -0.0395 -0.0037 357 VAL A O   
2866  C CB  . VAL A 357 ? 0.2210 0.3434 0.6833 0.0700  -0.0501 0.0010  357 VAL A CB  
2867  C CG1 . VAL A 357 ? 0.2131 0.3354 0.6773 0.0734  -0.0382 -0.0017 357 VAL A CG1 
2868  C CG2 . VAL A 357 ? 0.2261 0.3306 0.6659 0.0717  -0.0584 0.0047  357 VAL A CG2 
2869  N N   . ILE A 358 ? 0.2399 0.3808 0.7087 0.0545  -0.0254 -0.0040 358 ILE A N   
2870  C CA  . ILE A 358 ? 0.2631 0.4171 0.7468 0.0527  -0.0140 -0.0070 358 ILE A CA  
2871  C C   . ILE A 358 ? 0.2498 0.3988 0.7280 0.0573  -0.0040 -0.0092 358 ILE A C   
2872  O O   . ILE A 358 ? 0.2467 0.4065 0.7391 0.0586  0.0049  -0.0121 358 ILE A O   
2873  C CB  . ILE A 358 ? 0.2712 0.4283 0.7506 0.0433  -0.0093 -0.0068 358 ILE A CB  
2874  C CG1 . ILE A 358 ? 0.2932 0.4349 0.7463 0.0397  -0.0054 -0.0059 358 ILE A CG1 
2875  C CG2 . ILE A 358 ? 0.2647 0.4279 0.7525 0.0389  -0.0194 -0.0051 358 ILE A CG2 
2876  C CD1 . ILE A 358 ? 0.3101 0.4547 0.7597 0.0313  0.0014  -0.0061 358 ILE A CD1 
2877  N N   . TYR A 359 ? 0.2469 0.3795 0.7047 0.0596  -0.0051 -0.0081 359 TYR A N   
2878  C CA  . TYR A 359 ? 0.2385 0.3649 0.6904 0.0637  0.0032  -0.0103 359 TYR A CA  
2879  C C   . TYR A 359 ? 0.2538 0.3653 0.6930 0.0691  -0.0036 -0.0082 359 TYR A C   
2880  O O   . TYR A 359 ? 0.2669 0.3680 0.6899 0.0662  -0.0098 -0.0051 359 TYR A O   
2881  C CB  . TYR A 359 ? 0.2253 0.3468 0.6621 0.0575  0.0128  -0.0112 359 TYR A CB  
2882  C CG  . TYR A 359 ? 0.2522 0.3667 0.6819 0.0613  0.0212  -0.0138 359 TYR A CG  
2883  C CD1 . TYR A 359 ? 0.2749 0.3730 0.6858 0.0630  0.0193  -0.0125 359 TYR A CD1 
2884  C CD2 . TYR A 359 ? 0.2685 0.3925 0.7107 0.0636  0.0307  -0.0177 359 TYR A CD2 
2885  C CE1 . TYR A 359 ? 0.2695 0.3603 0.6739 0.0664  0.0259  -0.0151 359 TYR A CE1 
2886  C CE2 . TYR A 359 ? 0.2875 0.4039 0.7223 0.0674  0.0377  -0.0206 359 TYR A CE2 
2887  C CZ  . TYR A 359 ? 0.2917 0.3912 0.7076 0.0687  0.0349  -0.0193 359 TYR A CZ  
2888  O OH  . TYR A 359 ? 0.2791 0.3704 0.6879 0.0722  0.0410  -0.0223 359 TYR A OH  
2889  N N   . SER A 360 ? 0.2437 0.3538 0.6898 0.0766  -0.0017 -0.0102 360 SER A N   
2890  C CA  . SER A 360 ? 0.2660 0.3613 0.7008 0.0819  -0.0070 -0.0083 360 SER A CA  
2891  C C   . SER A 360 ? 0.2931 0.3837 0.7278 0.0870  0.0010  -0.0117 360 SER A C   
2892  O O   . SER A 360 ? 0.3109 0.4122 0.7630 0.0911  0.0062  -0.0155 360 SER A O   
2893  C CB  . SER A 360 ? 0.2675 0.3647 0.7133 0.0873  -0.0186 -0.0061 360 SER A CB  
2894  O OG  . SER A 360 ? 0.2664 0.3475 0.6943 0.0883  -0.0264 -0.0021 360 SER A OG  
2895  N N   . LYS A 361 ? 0.3137 0.3881 0.7291 0.0868  0.0021  -0.0107 361 LYS A N   
2896  C CA  . LYS A 361 ? 0.3516 0.4201 0.7661 0.0916  0.0086  -0.0141 361 LYS A CA  
2897  C C   . LYS A 361 ? 0.3481 0.3976 0.7442 0.0928  0.0046  -0.0112 361 LYS A C   
2898  O O   . LYS A 361 ? 0.3647 0.4056 0.7433 0.0870  0.0036  -0.0083 361 LYS A O   
2899  C CB  . LYS A 361 ? 0.4164 0.4892 0.8279 0.0874  0.0207  -0.0180 361 LYS A CB  
2900  C CG  . LYS A 361 ? 0.5193 0.5878 0.9315 0.0925  0.0285  -0.0228 361 LYS A CG  
2901  C CD  . LYS A 361 ? 0.6088 0.6788 1.0139 0.0879  0.0401  -0.0264 361 LYS A CD  
2902  C CE  . LYS A 361 ? 0.6297 0.6907 1.0284 0.0918  0.0471  -0.0310 361 LYS A CE  
2903  N NZ  . LYS A 361 ? 0.6192 0.6908 1.0353 0.0981  0.0536  -0.0363 361 LYS A NZ  
2904  N N   . ASN A 362 ? 0.3572 0.4006 0.7582 0.1003  0.0026  -0.0123 362 ASN A N   
2905  C CA  . ASN A 362 ? 0.3714 0.3968 0.7573 0.1020  0.0009  -0.0107 362 ASN A CA  
2906  C C   . ASN A 362 ? 0.3550 0.3750 0.7308 0.0992  0.0110  -0.0144 362 ASN A C   
2907  O O   . ASN A 362 ? 0.3477 0.3748 0.7328 0.1016  0.0186  -0.0196 362 ASN A O   
2908  C CB  . ASN A 362 ? 0.4158 0.4363 0.8115 0.1111  -0.0049 -0.0108 362 ASN A CB  
2909  C CG  . ASN A 362 ? 0.4458 0.4702 0.8496 0.1136  -0.0162 -0.0066 362 ASN A CG  
2910  O OD1 . ASN A 362 ? 0.5335 0.5691 0.9574 0.1194  -0.0187 -0.0085 362 ASN A OD1 
2911  N ND2 . ASN A 362 ? 0.4529 0.4690 0.8417 0.1092  -0.0229 -0.0010 362 ASN A ND2 
2912  N N   . ILE A 363 ? 0.3676 0.3757 0.7243 0.0937  0.0109  -0.0116 363 ILE A N   
2913  C CA  . ILE A 363 ? 0.3932 0.3936 0.7378 0.0905  0.0184  -0.0142 363 ILE A CA  
2914  C C   . ILE A 363 ? 0.4304 0.4153 0.7692 0.0950  0.0165  -0.0144 363 ILE A C   
2915  O O   . ILE A 363 ? 0.4319 0.4058 0.7618 0.0945  0.0099  -0.0096 363 ILE A O   
2916  C CB  . ILE A 363 ? 0.3847 0.3807 0.7131 0.0822  0.0183  -0.0108 363 ILE A CB  
2917  C CG1 . ILE A 363 ? 0.4305 0.4390 0.7628 0.0776  0.0178  -0.0095 363 ILE A CG1 
2918  C CG2 . ILE A 363 ? 0.3877 0.3771 0.7050 0.0786  0.0256  -0.0137 363 ILE A CG2 
2919  C CD1 . ILE A 363 ? 0.4507 0.4736 0.7959 0.0775  0.0247  -0.0140 363 ILE A CD1 
2920  N N   . THR A 364 ? 0.4616 0.4445 0.8037 0.0988  0.0227  -0.0199 364 THR A N   
2921  C CA  . THR A 364 ? 0.5505 0.5176 0.8870 0.1030  0.0208  -0.0206 364 THR A CA  
2922  C C   . THR A 364 ? 0.5517 0.5076 0.8717 0.0977  0.0253  -0.0218 364 THR A C   
2923  O O   . THR A 364 ? 0.5900 0.5307 0.9021 0.0988  0.0225  -0.0208 364 THR A O   
2924  C CB  . THR A 364 ? 0.5519 0.5217 0.9030 0.1121  0.0230  -0.0260 364 THR A CB  
2925  O OG1 . THR A 364 ? 0.5574 0.5424 0.9175 0.1114  0.0313  -0.0309 364 THR A OG1 
2926  C CG2 . THR A 364 ? 0.5505 0.5238 0.9156 0.1187  0.0147  -0.0234 364 THR A CG2 
2927  N N   . SER A 365 ? 0.5090 0.4721 0.8246 0.0919  0.0319  -0.0239 365 SER A N   
2928  C CA  . SER A 365 ? 0.5056 0.4593 0.8061 0.0864  0.0356  -0.0249 365 SER A CA  
2929  C C   . SER A 365 ? 0.4442 0.4040 0.7373 0.0783  0.0370  -0.0223 365 SER A C   
2930  O O   . SER A 365 ? 0.3611 0.3342 0.6610 0.0767  0.0394  -0.0227 365 SER A O   
2931  C CB  . SER A 365 ? 0.5702 0.5222 0.8702 0.0887  0.0431  -0.0319 365 SER A CB  
2932  O OG  . SER A 365 ? 0.5814 0.5488 0.8914 0.0895  0.0492  -0.0354 365 SER A OG  
2933  N N   . GLU A 366 ? 0.4061 0.3553 0.6856 0.0732  0.0358  -0.0199 366 GLU A N   
2934  C CA  . GLU A 366 ? 0.4149 0.3671 0.6862 0.0658  0.0363  -0.0172 366 GLU A CA  
2935  C C   . GLU A 366 ? 0.3877 0.3452 0.6564 0.0627  0.0433  -0.0215 366 GLU A C   
2936  O O   . GLU A 366 ? 0.3986 0.3571 0.6710 0.0662  0.0481  -0.0266 366 GLU A O   
2937  C CB  . GLU A 366 ? 0.4527 0.3918 0.7123 0.0622  0.0329  -0.0137 366 GLU A CB  
2938  C CG  . GLU A 366 ? 0.4637 0.3924 0.7153 0.0609  0.0359  -0.0172 366 GLU A CG  
2939  C CD  . GLU A 366 ? 0.5086 0.4265 0.7504 0.0562  0.0325  -0.0131 366 GLU A CD  
2940  O OE1 . GLU A 366 ? 0.5468 0.4682 0.7834 0.0505  0.0328  -0.0107 366 GLU A OE1 
2941  O OE2 . GLU A 366 ? 0.5479 0.4540 0.7876 0.0582  0.0296  -0.0122 366 GLU A OE2 
2942  N N   . GLY A 367 ? 0.3393 0.3002 0.6015 0.0563  0.0440  -0.0195 367 GLY A N   
2943  C CA  . GLY A 367 ? 0.3296 0.2942 0.5874 0.0526  0.0498  -0.0227 367 GLY A CA  
2944  C C   . GLY A 367 ? 0.3122 0.2910 0.5790 0.0525  0.0532  -0.0236 367 GLY A C   
2945  O O   . GLY A 367 ? 0.2830 0.2695 0.5580 0.0533  0.0498  -0.0208 367 GLY A O   
2946  N N   . TYR A 368 ? 0.3103 0.2919 0.5746 0.0511  0.0597  -0.0276 368 TYR A N   
2947  C CA  . TYR A 368 ? 0.3073 0.3019 0.5789 0.0497  0.0640  -0.0284 368 TYR A CA  
2948  C C   . TYR A 368 ? 0.3228 0.3263 0.6103 0.0559  0.0652  -0.0303 368 TYR A C   
2949  O O   . TYR A 368 ? 0.2968 0.2957 0.5874 0.0616  0.0661  -0.0333 368 TYR A O   
2950  C CB  . TYR A 368 ? 0.3057 0.2987 0.5684 0.0467  0.0710  -0.0321 368 TYR A CB  
2951  C CG  . TYR A 368 ? 0.3078 0.3135 0.5767 0.0446  0.0767  -0.0330 368 TYR A CG  
2952  C CD1 . TYR A 368 ? 0.3126 0.3229 0.5787 0.0384  0.0758  -0.0297 368 TYR A CD1 
2953  C CD2 . TYR A 368 ? 0.3277 0.3405 0.6057 0.0486  0.0831  -0.0370 368 TYR A CD2 
2954  C CE1 . TYR A 368 ? 0.3224 0.3435 0.5941 0.0358  0.0809  -0.0301 368 TYR A CE1 
2955  C CE2 . TYR A 368 ? 0.3561 0.3810 0.6408 0.0462  0.0888  -0.0375 368 TYR A CE2 
2956  C CZ  . TYR A 368 ? 0.3382 0.3669 0.6194 0.0395  0.0876  -0.0338 368 TYR A CZ  
2957  O OH  . TYR A 368 ? 0.3635 0.4037 0.6515 0.0368  0.0934  -0.0340 368 TYR A OH  
2958  N N   . MET A 369 ? 0.3417 0.3580 0.6400 0.0547  0.0647  -0.0284 369 MET A N   
2959  C CA  . MET A 369 ? 0.3619 0.3900 0.6768 0.0594  0.0679  -0.0310 369 MET A CA  
2960  C C   . MET A 369 ? 0.3491 0.3906 0.6706 0.0546  0.0714  -0.0302 369 MET A C   
2961  O O   . MET A 369 ? 0.3390 0.3818 0.6566 0.0493  0.0677  -0.0264 369 MET A O   
2962  C CB  . MET A 369 ? 0.3963 0.4259 0.7229 0.0652  0.0608  -0.0291 369 MET A CB  
2963  C CG  . MET A 369 ? 0.4799 0.5106 0.8060 0.0621  0.0527  -0.0236 369 MET A CG  
2964  S SD  . MET A 369 ? 0.6078 0.6501 0.9534 0.0666  0.0462  -0.0218 369 MET A SD  
2965  C CE  . MET A 369 ? 0.5472 0.6056 0.9096 0.0682  0.0552  -0.0265 369 MET A CE  
2966  N N   . ALA A 370 ? 0.3235 0.3750 0.6555 0.0568  0.0787  -0.0338 370 ALA A N   
2967  C CA  . ALA A 370 ? 0.3362 0.4019 0.6780 0.0529  0.0826  -0.0332 370 ALA A CA  
2968  C C   . ALA A 370 ? 0.3234 0.4025 0.6874 0.0582  0.0818  -0.0341 370 ALA A C   
2969  O O   . ALA A 370 ? 0.3491 0.4273 0.7202 0.0653  0.0824  -0.0371 370 ALA A O   
2970  C CB  . ALA A 370 ? 0.3515 0.4183 0.6862 0.0498  0.0929  -0.0365 370 ALA A CB  
2971  N N   . ASP A 371 ? 0.3208 0.4125 0.6964 0.0545  0.0805  -0.0317 371 ASP A N   
2972  C CA  . ASP A 371 ? 0.3093 0.4161 0.7079 0.0584  0.0799  -0.0325 371 ASP A CA  
2973  C C   . ASP A 371 ? 0.3058 0.4244 0.7113 0.0511  0.0812  -0.0301 371 ASP A C   
2974  O O   . ASP A 371 ? 0.2985 0.4127 0.6903 0.0442  0.0842  -0.0287 371 ASP A O   
2975  C CB  . ASP A 371 ? 0.2990 0.4025 0.7038 0.0638  0.0691  -0.0304 371 ASP A CB  
2976  C CG  . ASP A 371 ? 0.2724 0.3879 0.7004 0.0709  0.0675  -0.0321 371 ASP A CG  
2977  O OD1 . ASP A 371 ? 0.2544 0.3834 0.6969 0.0714  0.0751  -0.0350 371 ASP A OD1 
2978  O OD2 . ASP A 371 ? 0.2726 0.3838 0.7043 0.0758  0.0585  -0.0305 371 ASP A OD2 
2979  N N   . GLU A 372 ? 0.3423 0.4752 0.7687 0.0522  0.0782  -0.0293 372 GLU A N   
2980  C CA  . GLU A 372 ? 0.3803 0.5228 0.8126 0.0446  0.0775  -0.0264 372 GLU A CA  
2981  C C   . GLU A 372 ? 0.3386 0.4866 0.7836 0.0454  0.0660  -0.0234 372 GLU A C   
2982  O O   . GLU A 372 ? 0.3037 0.4543 0.7603 0.0524  0.0609  -0.0242 372 GLU A O   
2983  C CB  . GLU A 372 ? 0.4059 0.5618 0.8488 0.0416  0.0890  -0.0286 372 GLU A CB  
2984  C CG  . GLU A 372 ? 0.4377 0.6075 0.9032 0.0485  0.0938  -0.0324 372 GLU A CG  
2985  C CD  . GLU A 372 ? 0.4797 0.6635 0.9554 0.0451  0.1066  -0.0345 372 GLU A CD  
2986  O OE1 . GLU A 372 ? 0.4286 0.6082 0.8896 0.0376  0.1126  -0.0333 372 GLU A OE1 
2987  O OE2 . GLU A 372 ? 0.4055 0.6043 0.9039 0.0500  0.1106  -0.0373 372 GLU A OE2 
2988  N N   . LEU A 373 ? 0.3386 0.4860 0.7786 0.0382  0.0611  -0.0200 373 LEU A N   
2989  C CA  . LEU A 373 ? 0.3485 0.5016 0.7997 0.0374  0.0506  -0.0173 373 LEU A CA  
2990  C C   . LEU A 373 ? 0.3016 0.4729 0.7743 0.0339  0.0541  -0.0176 373 LEU A C   
2991  O O   . LEU A 373 ? 0.3278 0.5025 0.7981 0.0279  0.0625  -0.0178 373 LEU A O   
2992  C CB  . LEU A 373 ? 0.3493 0.4925 0.7848 0.0316  0.0431  -0.0138 373 LEU A CB  
2993  C CG  . LEU A 373 ? 0.3769 0.5030 0.7916 0.0338  0.0386  -0.0127 373 LEU A CG  
2994  C CD1 . LEU A 373 ? 0.3816 0.5006 0.7832 0.0275  0.0331  -0.0098 373 LEU A CD1 
2995  C CD2 . LEU A 373 ? 0.4398 0.5636 0.8598 0.0413  0.0307  -0.0124 373 LEU A CD2 
2996  N N   . THR A 374 ? 0.2905 0.4724 0.7832 0.0369  0.0469  -0.0173 374 THR A N   
2997  C CA  . THR A 374 ? 0.3036 0.5026 0.8176 0.0325  0.0474  -0.0168 374 THR A CA  
2998  C C   . THR A 374 ? 0.3223 0.5185 0.8339 0.0275  0.0354  -0.0133 374 THR A C   
2999  O O   . THR A 374 ? 0.3452 0.5351 0.8540 0.0316  0.0246  -0.0122 374 THR A O   
3000  C CB  . THR A 374 ? 0.3033 0.5171 0.8434 0.0398  0.0473  -0.0192 374 THR A CB  
3001  O OG1 . THR A 374 ? 0.3349 0.5479 0.8721 0.0441  0.0591  -0.0227 374 THR A OG1 
3002  C CG2 . THR A 374 ? 0.2895 0.5228 0.8547 0.0352  0.0478  -0.0187 374 THR A CG2 
3003  N N   . ILE A 375 ? 0.3403 0.5397 0.8510 0.0186  0.0375  -0.0117 375 ILE A N   
3004  C CA  . ILE A 375 ? 0.3380 0.5352 0.8471 0.0131  0.0268  -0.0089 375 ILE A CA  
3005  C C   . ILE A 375 ? 0.3265 0.5416 0.8600 0.0079  0.0275  -0.0085 375 ILE A C   
3006  O O   . ILE A 375 ? 0.2983 0.5251 0.8441 0.0065  0.0385  -0.0098 375 ILE A O   
3007  C CB  . ILE A 375 ? 0.3179 0.5004 0.8026 0.0067  0.0274  -0.0071 375 ILE A CB  
3008  C CG1 . ILE A 375 ? 0.3246 0.5099 0.8064 0.0006  0.0397  -0.0072 375 ILE A CG1 
3009  C CG2 . ILE A 375 ? 0.3148 0.4800 0.7768 0.0114  0.0246  -0.0071 375 ILE A CG2 
3010  C CD1 . ILE A 375 ? 0.3284 0.5002 0.7885 -0.0060 0.0393  -0.0052 375 ILE A CD1 
3011  N N   . ASP A 376 ? 0.3533 0.5700 0.8929 0.0046  0.0160  -0.0067 376 ASP A N   
3012  C CA  . ASP A 376 ? 0.4073 0.6412 0.9710 -0.0010 0.0158  -0.0061 376 ASP A CA  
3013  C C   . ASP A 376 ? 0.4226 0.6505 0.9785 -0.0102 0.0089  -0.0036 376 ASP A C   
3014  O O   . ASP A 376 ? 0.4307 0.6620 0.9965 -0.0116 -0.0028 -0.0028 376 ASP A O   
3015  C CB  . ASP A 376 ? 0.4136 0.6610 1.0022 0.0055  0.0091  -0.0072 376 ASP A CB  
3016  C CG  . ASP A 376 ? 0.4609 0.7286 1.0788 0.0004  0.0090  -0.0069 376 ASP A CG  
3017  O OD1 . ASP A 376 ? 0.4900 0.7690 1.1184 -0.0035 0.0217  -0.0075 376 ASP A OD1 
3018  O OD2 . ASP A 376 ? 0.4794 0.7513 1.1090 0.0001  -0.0038 -0.0060 376 ASP A OD2 
3019  N N   . PRO A 377 ? 0.3533 0.5723 0.8921 -0.0169 0.0156  -0.0024 377 PRO A N   
3020  C CA  . PRO A 377 ? 0.3270 0.5388 0.8575 -0.0252 0.0091  -0.0003 377 PRO A CA  
3021  C C   . PRO A 377 ? 0.3124 0.5391 0.8660 -0.0330 0.0073  0.0010  377 PRO A C   
3022  O O   . PRO A 377 ? 0.2784 0.5204 0.8504 -0.0353 0.0168  0.0009  377 PRO A O   
3023  C CB  . PRO A 377 ? 0.2871 0.4874 0.7960 -0.0287 0.0189  0.0004  377 PRO A CB  
3024  C CG  . PRO A 377 ? 0.2924 0.5042 0.8119 -0.0272 0.0326  -0.0008 377 PRO A CG  
3025  C CD  . PRO A 377 ? 0.3185 0.5346 0.8466 -0.0170 0.0296  -0.0031 377 PRO A CD  
3026  N N   . VAL A 378 ? 0.3158 0.5380 0.8688 -0.0371 -0.0052 0.0020  378 VAL A N   
3027  C CA  . VAL A 378 ? 0.3332 0.5658 0.9044 -0.0459 -0.0088 0.0035  378 VAL A CA  
3028  C C   . VAL A 378 ? 0.3043 0.5252 0.8589 -0.0549 -0.0063 0.0055  378 VAL A C   
3029  O O   . VAL A 378 ? 0.3260 0.5294 0.8583 -0.0549 -0.0128 0.0056  378 VAL A O   
3030  C CB  . VAL A 378 ? 0.3740 0.6071 0.9532 -0.0443 -0.0251 0.0031  378 VAL A CB  
3031  C CG1 . VAL A 378 ? 0.4185 0.6636 1.0196 -0.0532 -0.0304 0.0043  378 VAL A CG1 
3032  C CG2 . VAL A 378 ? 0.3806 0.6218 0.9720 -0.0342 -0.0286 0.0013  378 VAL A CG2 
3033  N N   . GLY A 379 ? 0.2786 0.5090 0.8438 -0.0622 0.0038  0.0072  379 GLY A N   
3034  C CA  . GLY A 379 ? 0.2682 0.4884 0.8190 -0.0710 0.0081  0.0096  379 GLY A CA  
3035  C C   . GLY A 379 ? 0.2877 0.4903 0.8096 -0.0671 0.0129  0.0092  379 GLY A C   
3036  O O   . GLY A 379 ? 0.2978 0.5024 0.8161 -0.0611 0.0217  0.0079  379 GLY A O   
3037  N N   . ILE A 380 ? 0.3123 0.4977 0.8141 -0.0705 0.0069  0.0101  380 ILE A N   
3038  C CA  . ILE A 380 ? 0.2854 0.4537 0.7604 -0.0662 0.0089  0.0095  380 ILE A CA  
3039  C C   . ILE A 380 ? 0.2570 0.4166 0.7233 -0.0594 -0.0026 0.0074  380 ILE A C   
3040  O O   . ILE A 380 ? 0.2378 0.3933 0.7047 -0.0623 -0.0134 0.0074  380 ILE A O   
3041  C CB  . ILE A 380 ? 0.3082 0.4628 0.7664 -0.0735 0.0100  0.0117  380 ILE A CB  
3042  C CG1 . ILE A 380 ? 0.3343 0.4973 0.8016 -0.0816 0.0205  0.0144  380 ILE A CG1 
3043  C CG2 . ILE A 380 ? 0.3097 0.4476 0.7419 -0.0687 0.0119  0.0109  380 ILE A CG2 
3044  C CD1 . ILE A 380 ? 0.3683 0.5194 0.8241 -0.0906 0.0193  0.0173  380 ILE A CD1 
3045  N N   . GLU A 381 ? 0.2419 0.3993 0.7007 -0.0506 0.0000  0.0057  381 GLU A N   
3046  C CA  . GLU A 381 ? 0.2342 0.3859 0.6872 -0.0434 -0.0096 0.0040  381 GLU A CA  
3047  C C   . GLU A 381 ? 0.2206 0.3573 0.6496 -0.0385 -0.0071 0.0034  381 GLU A C   
3048  O O   . GLU A 381 ? 0.2368 0.3744 0.6622 -0.0352 0.0021  0.0031  381 GLU A O   
3049  C CB  . GLU A 381 ? 0.2278 0.3926 0.6988 -0.0368 -0.0109 0.0028  381 GLU A CB  
3050  C CG  . GLU A 381 ? 0.2361 0.3974 0.7065 -0.0322 -0.0242 0.0019  381 GLU A CG  
3051  C CD  . GLU A 381 ? 0.2552 0.4298 0.7452 -0.0258 -0.0264 0.0010  381 GLU A CD  
3052  O OE1 . GLU A 381 ? 0.2529 0.4440 0.7655 -0.0274 -0.0211 0.0010  381 GLU A OE1 
3053  O OE2 . GLU A 381 ? 0.2566 0.4253 0.7398 -0.0191 -0.0336 0.0004  381 GLU A OE2 
3054  N N   . ASP A 382 ? 0.2232 0.3461 0.6360 -0.0384 -0.0152 0.0031  382 ASP A N   
3055  C CA  . ASP A 382 ? 0.2193 0.3291 0.6113 -0.0328 -0.0148 0.0023  382 ASP A CA  
3056  C C   . ASP A 382 ? 0.2203 0.3325 0.6151 -0.0248 -0.0188 0.0013  382 ASP A C   
3057  O O   . ASP A 382 ? 0.2193 0.3368 0.6246 -0.0237 -0.0272 0.0010  382 ASP A O   
3058  C CB  . ASP A 382 ? 0.2089 0.3044 0.5841 -0.0349 -0.0217 0.0020  382 ASP A CB  
3059  C CG  . ASP A 382 ? 0.2030 0.2981 0.5827 -0.0362 -0.0336 0.0013  382 ASP A CG  
3060  O OD1 . ASP A 382 ? 0.2303 0.3339 0.6255 -0.0416 -0.0363 0.0019  382 ASP A OD1 
3061  O OD2 . ASP A 382 ? 0.2004 0.2862 0.5674 -0.0320 -0.0401 0.0002  382 ASP A OD2 
3062  N N   . MET A 383 ? 0.2258 0.3338 0.6114 -0.0193 -0.0130 0.0009  383 MET A N   
3063  C CA  . MET A 383 ? 0.2367 0.3472 0.6260 -0.0118 -0.0156 0.0003  383 MET A CA  
3064  C C   . MET A 383 ? 0.2185 0.3159 0.5876 -0.0072 -0.0145 0.0001  383 MET A C   
3065  O O   . MET A 383 ? 0.2130 0.3068 0.5744 -0.0073 -0.0062 0.0001  383 MET A O   
3066  C CB  . MET A 383 ? 0.2410 0.3644 0.6469 -0.0093 -0.0077 -0.0002 383 MET A CB  
3067  C CG  . MET A 383 ? 0.2483 0.3874 0.6774 -0.0131 -0.0076 -0.0001 383 MET A CG  
3068  S SD  . MET A 383 ? 0.2687 0.4229 0.7168 -0.0091 0.0029  -0.0014 383 MET A SD  
3069  C CE  . MET A 383 ? 0.2923 0.4489 0.7484 0.0005  -0.0050 -0.0023 383 MET A CE  
3070  N N   . GLU A 384 ? 0.2306 0.3208 0.5911 -0.0034 -0.0227 0.0002  384 GLU A N   
3071  C CA  . GLU A 384 ? 0.2353 0.3148 0.5794 0.0014  -0.0213 0.0004  384 GLU A CA  
3072  C C   . GLU A 384 ? 0.2318 0.3159 0.5837 0.0078  -0.0198 0.0005  384 GLU A C   
3073  O O   . GLU A 384 ? 0.2308 0.3173 0.5889 0.0114  -0.0271 0.0010  384 GLU A O   
3074  C CB  . GLU A 384 ? 0.2502 0.3188 0.5794 0.0023  -0.0297 0.0006  384 GLU A CB  
3075  C CG  . GLU A 384 ? 0.2558 0.3129 0.5667 0.0058  -0.0273 0.0011  384 GLU A CG  
3076  C CD  . GLU A 384 ? 0.2719 0.3183 0.5669 0.0070  -0.0343 0.0012  384 GLU A CD  
3077  O OE1 . GLU A 384 ? 0.2553 0.3020 0.5520 0.0058  -0.0427 0.0008  384 GLU A OE1 
3078  O OE2 . GLU A 384 ? 0.3049 0.3424 0.5852 0.0088  -0.0312 0.0016  384 GLU A OE2 
3079  N N   . LEU A 385 ? 0.2380 0.3224 0.5890 0.0094  -0.0106 0.0001  385 LEU A N   
3080  C CA  . LEU A 385 ? 0.2528 0.3401 0.6102 0.0156  -0.0082 -0.0003 385 LEU A CA  
3081  C C   . LEU A 385 ? 0.2467 0.3216 0.5880 0.0199  -0.0108 0.0008  385 LEU A C   
3082  O O   . LEU A 385 ? 0.2223 0.2886 0.5494 0.0191  -0.0064 0.0009  385 LEU A O   
3083  C CB  . LEU A 385 ? 0.2559 0.3485 0.6192 0.0156  0.0025  -0.0017 385 LEU A CB  
3084  C CG  . LEU A 385 ? 0.2775 0.3826 0.6563 0.0110  0.0070  -0.0025 385 LEU A CG  
3085  C CD1 . LEU A 385 ? 0.2786 0.3877 0.6603 0.0112  0.0183  -0.0040 385 LEU A CD1 
3086  C CD2 . LEU A 385 ? 0.2877 0.4053 0.6872 0.0127  0.0013  -0.0026 385 LEU A CD2 
3087  N N   . ALA A 386 ? 0.2695 0.3440 0.6138 0.0244  -0.0183 0.0017  386 ALA A N   
3088  C CA  . ALA A 386 ? 0.2695 0.3325 0.5991 0.0281  -0.0218 0.0034  386 ALA A CA  
3089  C C   . ALA A 386 ? 0.2482 0.3099 0.5805 0.0336  -0.0179 0.0034  386 ALA A C   
3090  O O   . ALA A 386 ? 0.2182 0.2853 0.5630 0.0380  -0.0213 0.0034  386 ALA A O   
3091  C CB  . ALA A 386 ? 0.2878 0.3500 0.6179 0.0294  -0.0328 0.0047  386 ALA A CB  
3092  N N   . PHE A 387 ? 0.2593 0.3132 0.5798 0.0334  -0.0113 0.0033  387 PHE A N   
3093  C CA  . PHE A 387 ? 0.2656 0.3156 0.5856 0.0380  -0.0074 0.0031  387 PHE A CA  
3094  C C   . PHE A 387 ? 0.2863 0.3251 0.5938 0.0411  -0.0128 0.0059  387 PHE A C   
3095  O O   . PHE A 387 ? 0.3200 0.3517 0.6138 0.0386  -0.0153 0.0074  387 PHE A O   
3096  C CB  . PHE A 387 ? 0.2517 0.2984 0.5648 0.0356  0.0017  0.0017  387 PHE A CB  
3097  C CG  . PHE A 387 ? 0.2470 0.3037 0.5714 0.0334  0.0085  -0.0009 387 PHE A CG  
3098  C CD1 . PHE A 387 ? 0.2455 0.3092 0.5747 0.0284  0.0084  -0.0012 387 PHE A CD1 
3099  C CD2 . PHE A 387 ? 0.2604 0.3192 0.5906 0.0363  0.0150  -0.0031 387 PHE A CD2 
3100  C CE1 . PHE A 387 ? 0.2360 0.3088 0.5754 0.0260  0.0149  -0.0031 387 PHE A CE1 
3101  C CE2 . PHE A 387 ? 0.2626 0.3306 0.6022 0.0342  0.0218  -0.0054 387 PHE A CE2 
3102  C CZ  . PHE A 387 ? 0.2474 0.3226 0.5917 0.0289  0.0219  -0.0052 387 PHE A CZ  
3103  N N   . GLU A 388 ? 0.3174 0.3546 0.6301 0.0466  -0.0143 0.0065  388 GLU A N   
3104  C CA  . GLU A 388 ? 0.3079 0.3341 0.6099 0.0498  -0.0193 0.0095  388 GLU A CA  
3105  C C   . GLU A 388 ? 0.3069 0.3282 0.6096 0.0535  -0.0145 0.0090  388 GLU A C   
3106  O O   . GLU A 388 ? 0.3014 0.3292 0.6186 0.0573  -0.0130 0.0069  388 GLU A O   
3107  C CB  . GLU A 388 ? 0.3107 0.3386 0.6194 0.0537  -0.0291 0.0114  388 GLU A CB  
3108  C CG  . GLU A 388 ? 0.3296 0.3639 0.6414 0.0505  -0.0349 0.0112  388 GLU A CG  
3109  C CD  . GLU A 388 ? 0.3259 0.3628 0.6458 0.0542  -0.0454 0.0127  388 GLU A CD  
3110  O OE1 . GLU A 388 ? 0.3320 0.3710 0.6629 0.0596  -0.0468 0.0128  388 GLU A OE1 
3111  O OE2 . GLU A 388 ? 0.3308 0.3671 0.6459 0.0520  -0.0524 0.0137  388 GLU A OE2 
3112  N N   . PHE A 389 ? 0.2960 0.3060 0.5837 0.0524  -0.0123 0.0108  389 PHE A N   
3113  C CA  . PHE A 389 ? 0.2994 0.3021 0.5852 0.0553  -0.0089 0.0107  389 PHE A CA  
3114  C C   . PHE A 389 ? 0.3075 0.2997 0.5856 0.0585  -0.0152 0.0148  389 PHE A C   
3115  O O   . PHE A 389 ? 0.3021 0.2883 0.5674 0.0561  -0.0184 0.0179  389 PHE A O   
3116  C CB  . PHE A 389 ? 0.2928 0.2903 0.5678 0.0510  -0.0019 0.0099  389 PHE A CB  
3117  C CG  . PHE A 389 ? 0.2546 0.2606 0.5347 0.0476  0.0044  0.0064  389 PHE A CG  
3118  C CD1 . PHE A 389 ? 0.2706 0.2819 0.5494 0.0434  0.0037  0.0063  389 PHE A CD1 
3119  C CD2 . PHE A 389 ? 0.2556 0.2631 0.5407 0.0485  0.0107  0.0032  389 PHE A CD2 
3120  C CE1 . PHE A 389 ? 0.2828 0.3006 0.5652 0.0398  0.0092  0.0036  389 PHE A CE1 
3121  C CE2 . PHE A 389 ? 0.2612 0.2754 0.5491 0.0450  0.0165  0.0004  389 PHE A CE2 
3122  C CZ  . PHE A 389 ? 0.2850 0.3043 0.5717 0.0405  0.0157  0.0008  389 PHE A CZ  
3123  N N   . TYR A 390 ? 0.3147 0.3044 0.6002 0.0640  -0.0169 0.0147  390 TYR A N   
3124  C CA  . TYR A 390 ? 0.3434 0.3226 0.6228 0.0675  -0.0237 0.0189  390 TYR A CA  
3125  C C   . TYR A 390 ? 0.3365 0.3047 0.6108 0.0691  -0.0201 0.0193  390 TYR A C   
3126  O O   . TYR A 390 ? 0.3266 0.2971 0.6072 0.0699  -0.0140 0.0155  390 TYR A O   
3127  C CB  . TYR A 390 ? 0.3663 0.3510 0.6604 0.0736  -0.0305 0.0187  390 TYR A CB  
3128  C CG  . TYR A 390 ? 0.3882 0.3830 0.6892 0.0728  -0.0363 0.0187  390 TYR A CG  
3129  C CD1 . TYR A 390 ? 0.3967 0.4053 0.7096 0.0704  -0.0323 0.0148  390 TYR A CD1 
3130  C CD2 . TYR A 390 ? 0.4282 0.4184 0.7241 0.0745  -0.0462 0.0226  390 TYR A CD2 
3131  C CE1 . TYR A 390 ? 0.3705 0.3882 0.6908 0.0693  -0.0382 0.0147  390 TYR A CE1 
3132  C CE2 . TYR A 390 ? 0.4635 0.4625 0.7662 0.0738  -0.0525 0.0223  390 TYR A CE2 
3133  C CZ  . TYR A 390 ? 0.4128 0.4256 0.7279 0.0710  -0.0485 0.0183  390 TYR A CZ  
3134  O OH  . TYR A 390 ? 0.3867 0.4070 0.7080 0.0699  -0.0555 0.0183  390 TYR A OH  
3135  N N   . ASP A 391 ? 0.3725 0.3283 0.6352 0.0696  -0.0243 0.0241  391 ASP A N   
3136  C CA  . ASP A 391 ? 0.3807 0.3245 0.6382 0.0708  -0.0221 0.0252  391 ASP A CA  
3137  C C   . ASP A 391 ? 0.3704 0.3094 0.6356 0.0778  -0.0284 0.0263  391 ASP A C   
3138  O O   . ASP A 391 ? 0.3514 0.2979 0.6272 0.0817  -0.0337 0.0258  391 ASP A O   
3139  C CB  . ASP A 391 ? 0.3662 0.2990 0.6060 0.0660  -0.0217 0.0299  391 ASP A CB  
3140  C CG  . ASP A 391 ? 0.3693 0.2959 0.5999 0.0668  -0.0295 0.0354  391 ASP A CG  
3141  O OD1 . ASP A 391 ? 0.3745 0.3020 0.6125 0.0720  -0.0365 0.0362  391 ASP A OD1 
3142  O OD2 . ASP A 391 ? 0.3933 0.3150 0.6098 0.0622  -0.0285 0.0387  391 ASP A OD2 
3143  N N   . SER A 392 ? 0.4082 0.3342 0.6681 0.0794  -0.0283 0.0281  392 SER A N   
3144  C CA  . SER A 392 ? 0.4357 0.3560 0.7039 0.0866  -0.0333 0.0283  392 SER A CA  
3145  C C   . SER A 392 ? 0.4470 0.3630 0.7128 0.0898  -0.0436 0.0336  392 SER A C   
3146  O O   . SER A 392 ? 0.4565 0.3699 0.7317 0.0966  -0.0491 0.0336  392 SER A O   
3147  C CB  . SER A 392 ? 0.4531 0.3588 0.7147 0.0868  -0.0311 0.0292  392 SER A CB  
3148  O OG  . SER A 392 ? 0.4624 0.3567 0.7068 0.0816  -0.0323 0.0352  392 SER A OG  
3149  N N   . ASP A 393 ? 0.4663 0.3807 0.7189 0.0851  -0.0462 0.0379  393 ASP A N   
3150  C CA  . ASP A 393 ? 0.4876 0.3983 0.7359 0.0875  -0.0563 0.0427  393 ASP A CA  
3151  C C   . ASP A 393 ? 0.4561 0.3815 0.7141 0.0881  -0.0599 0.0404  393 ASP A C   
3152  O O   . ASP A 393 ? 0.4306 0.3538 0.6833 0.0890  -0.0684 0.0441  393 ASP A O   
3153  C CB  . ASP A 393 ? 0.5282 0.4268 0.7548 0.0824  -0.0575 0.0490  393 ASP A CB  
3154  C CG  . ASP A 393 ? 0.5562 0.4394 0.7730 0.0812  -0.0550 0.0524  393 ASP A CG  
3155  O OD1 . ASP A 393 ? 0.5779 0.4539 0.8011 0.0864  -0.0582 0.0527  393 ASP A OD1 
3156  O OD2 . ASP A 393 ? 0.6167 0.4951 0.8198 0.0751  -0.0500 0.0548  393 ASP A OD2 
3157  N N   . ASN A 394 ? 0.4517 0.3913 0.7228 0.0872  -0.0539 0.0345  394 ASN A N   
3158  C CA  . ASN A 394 ? 0.4666 0.4206 0.7487 0.0873  -0.0569 0.0322  394 ASN A CA  
3159  C C   . ASN A 394 ? 0.4534 0.4069 0.7206 0.0812  -0.0584 0.0345  394 ASN A C   
3160  O O   . ASN A 394 ? 0.4268 0.3857 0.6967 0.0816  -0.0655 0.0352  394 ASN A O   
3161  C CB  . ASN A 394 ? 0.4844 0.4413 0.7806 0.0945  -0.0664 0.0328  394 ASN A CB  
3162  C CG  . ASN A 394 ? 0.5000 0.4750 0.8159 0.0955  -0.0669 0.0284  394 ASN A CG  
3163  O OD1 . ASN A 394 ? 0.4676 0.4528 0.7914 0.0930  -0.0582 0.0237  394 ASN A OD1 
3164  N ND2 . ASN A 394 ? 0.5173 0.4968 0.8420 0.0991  -0.0771 0.0298  394 ASN A ND2 
3165  N N   . LYS A 395 ? 0.4586 0.4057 0.7107 0.0758  -0.0519 0.0356  395 LYS A N   
3166  C CA  . LYS A 395 ? 0.5188 0.4659 0.7572 0.0702  -0.0513 0.0369  395 LYS A CA  
3167  C C   . LYS A 395 ? 0.4655 0.4215 0.7065 0.0653  -0.0423 0.0325  395 LYS A C   
3168  O O   . LYS A 395 ? 0.4734 0.4279 0.7143 0.0638  -0.0347 0.0308  395 LYS A O   
3169  C CB  . LYS A 395 ? 0.6033 0.5357 0.8214 0.0677  -0.0508 0.0421  395 LYS A CB  
3170  C CG  . LYS A 395 ? 0.7083 0.6301 0.9184 0.0711  -0.0604 0.0476  395 LYS A CG  
3171  C CD  . LYS A 395 ? 0.8345 0.7420 1.0239 0.0677  -0.0586 0.0530  395 LYS A CD  
3172  C CE  . LYS A 395 ? 0.9374 0.8325 1.1178 0.0710  -0.0677 0.0590  395 LYS A CE  
3173  N NZ  . LYS A 395 ? 0.9696 0.8509 1.1324 0.0675  -0.0640 0.0641  395 LYS A NZ  
3174  N N   . ILE A 396 ? 0.4194 0.3831 0.6606 0.0626  -0.0438 0.0310  396 ILE A N   
3175  C CA  . ILE A 396 ? 0.4105 0.3827 0.6550 0.0582  -0.0365 0.0270  396 ILE A CA  
3176  C C   . ILE A 396 ? 0.4053 0.3700 0.6348 0.0538  -0.0300 0.0282  396 ILE A C   
3177  O O   . ILE A 396 ? 0.4195 0.3764 0.6344 0.0523  -0.0322 0.0315  396 ILE A O   
3178  C CB  . ILE A 396 ? 0.4042 0.3849 0.6520 0.0563  -0.0410 0.0255  396 ILE A CB  
3179  C CG1 . ILE A 396 ? 0.4620 0.4526 0.7290 0.0604  -0.0465 0.0238  396 ILE A CG1 
3180  C CG2 . ILE A 396 ? 0.3776 0.3646 0.6254 0.0513  -0.0342 0.0222  396 ILE A CG2 
3181  C CD1 . ILE A 396 ? 0.4519 0.4515 0.7249 0.0583  -0.0517 0.0223  396 ILE A CD1 
3182  N N   . ILE A 397 ? 0.3911 0.3583 0.6244 0.0519  -0.0220 0.0254  397 ILE A N   
3183  C CA  . ILE A 397 ? 0.4013 0.3629 0.6232 0.0478  -0.0159 0.0261  397 ILE A CA  
3184  C C   . ILE A 397 ? 0.3774 0.3468 0.6009 0.0437  -0.0110 0.0226  397 ILE A C   
3185  O O   . ILE A 397 ? 0.3894 0.3555 0.6035 0.0401  -0.0070 0.0231  397 ILE A O   
3186  C CB  . ILE A 397 ? 0.4407 0.3961 0.6635 0.0487  -0.0116 0.0262  397 ILE A CB  
3187  C CG1 . ILE A 397 ? 0.4546 0.4172 0.6921 0.0510  -0.0086 0.0218  397 ILE A CG1 
3188  C CG2 . ILE A 397 ? 0.4905 0.4350 0.7076 0.0517  -0.0164 0.0308  397 ILE A CG2 
3189  C CD1 . ILE A 397 ? 0.4561 0.4125 0.6944 0.0518  -0.0043 0.0209  397 ILE A CD1 
3190  N N   . LYS A 398 ? 0.3377 0.3172 0.5734 0.0441  -0.0113 0.0193  398 LYS A N   
3191  C CA  . LYS A 398 ? 0.3094 0.2953 0.5456 0.0399  -0.0079 0.0166  398 LYS A CA  
3192  C C   . LYS A 398 ? 0.3310 0.3267 0.5782 0.0402  -0.0116 0.0146  398 LYS A C   
3193  O O   . LYS A 398 ? 0.3331 0.3343 0.5930 0.0434  -0.0134 0.0137  398 LYS A O   
3194  C CB  . LYS A 398 ? 0.2784 0.2660 0.5178 0.0380  -0.0003 0.0140  398 LYS A CB  
3195  C CG  . LYS A 398 ? 0.2731 0.2658 0.5120 0.0337  0.0031  0.0117  398 LYS A CG  
3196  C CD  . LYS A 398 ? 0.2655 0.2596 0.5074 0.0321  0.0097  0.0092  398 LYS A CD  
3197  C CE  . LYS A 398 ? 0.2484 0.2481 0.4916 0.0282  0.0121  0.0071  398 LYS A CE  
3198  N NZ  . LYS A 398 ? 0.2357 0.2356 0.4791 0.0261  0.0179  0.0050  398 LYS A NZ  
3199  N N   . ASN A 399 ? 0.3325 0.3303 0.5751 0.0367  -0.0126 0.0139  399 ASN A N   
3200  C CA  . ASN A 399 ? 0.3064 0.3132 0.5586 0.0352  -0.0152 0.0119  399 ASN A CA  
3201  C C   . ASN A 399 ? 0.3025 0.3127 0.5548 0.0308  -0.0093 0.0095  399 ASN A C   
3202  O O   . ASN A 399 ? 0.2769 0.2816 0.5182 0.0285  -0.0063 0.0097  399 ASN A O   
3203  C CB  . ASN A 399 ? 0.3104 0.3156 0.5564 0.0345  -0.0226 0.0129  399 ASN A CB  
3204  C CG  . ASN A 399 ? 0.3424 0.3448 0.5885 0.0386  -0.0304 0.0153  399 ASN A CG  
3205  O OD1 . ASN A 399 ? 0.3545 0.3635 0.6145 0.0413  -0.0340 0.0149  399 ASN A OD1 
3206  N ND2 . ASN A 399 ? 0.3500 0.3428 0.5807 0.0391  -0.0331 0.0180  399 ASN A ND2 
3207  N N   . GLU A 400 ? 0.2787 0.2981 0.5438 0.0295  -0.0078 0.0073  400 GLU A N   
3208  C CA  . GLU A 400 ? 0.2750 0.2971 0.5398 0.0251  -0.0031 0.0055  400 GLU A CA  
3209  C C   . GLU A 400 ? 0.2719 0.3042 0.5504 0.0233  -0.0044 0.0040  400 GLU A C   
3210  O O   . GLU A 400 ? 0.2406 0.2798 0.5319 0.0258  -0.0045 0.0035  400 GLU A O   
3211  C CB  . GLU A 400 ? 0.3013 0.3219 0.5649 0.0244  0.0046  0.0045  400 GLU A CB  
3212  C CG  . GLU A 400 ? 0.2955 0.3168 0.5561 0.0197  0.0087  0.0031  400 GLU A CG  
3213  C CD  . GLU A 400 ? 0.3037 0.3210 0.5592 0.0190  0.0150  0.0025  400 GLU A CD  
3214  O OE1 . GLU A 400 ? 0.2744 0.2892 0.5305 0.0221  0.0169  0.0026  400 GLU A OE1 
3215  O OE2 . GLU A 400 ? 0.2941 0.3100 0.5448 0.0154  0.0174  0.0019  400 GLU A OE2 
3216  N N   . SER A 401 ? 0.2396 0.2722 0.5150 0.0190  -0.0057 0.0035  401 SER A N   
3217  C CA  . SER A 401 ? 0.2368 0.2784 0.5242 0.0160  -0.0067 0.0024  401 SER A CA  
3218  C C   . SER A 401 ? 0.2245 0.2687 0.5140 0.0128  0.0013  0.0012  401 SER A C   
3219  O O   . SER A 401 ? 0.2313 0.2688 0.5101 0.0117  0.0051  0.0012  401 SER A O   
3220  C CB  . SER A 401 ? 0.2613 0.3007 0.5441 0.0130  -0.0130 0.0023  401 SER A CB  
3221  O OG  . SER A 401 ? 0.2740 0.3129 0.5575 0.0157  -0.0211 0.0032  401 SER A OG  
3222  N N   . ILE A 402 ? 0.2308 0.2849 0.5344 0.0112  0.0035  0.0004  402 ILE A N   
3223  C CA  . ILE A 402 ? 0.2216 0.2793 0.5279 0.0069  0.0101  -0.0004 402 ILE A CA  
3224  C C   . ILE A 402 ? 0.2277 0.2931 0.5447 0.0025  0.0071  -0.0003 402 ILE A C   
3225  O O   . ILE A 402 ? 0.2166 0.2912 0.5480 0.0037  0.0045  -0.0005 402 ILE A O   
3226  C CB  . ILE A 402 ? 0.2143 0.2771 0.5281 0.0094  0.0173  -0.0016 402 ILE A CB  
3227  C CG1 . ILE A 402 ? 0.2197 0.2743 0.5237 0.0136  0.0197  -0.0017 402 ILE A CG1 
3228  C CG2 . ILE A 402 ? 0.2107 0.2778 0.5272 0.0047  0.0245  -0.0022 402 ILE A CG2 
3229  C CD1 . ILE A 402 ? 0.2252 0.2707 0.5145 0.0110  0.0230  -0.0016 402 ILE A CD1 
3230  N N   . ASN A 403 ? 0.2437 0.3052 0.5541 -0.0026 0.0070  0.0000  403 ASN A N   
3231  C CA  . ASN A 403 ? 0.2538 0.3208 0.5729 -0.0075 0.0036  0.0002  403 ASN A CA  
3232  C C   . ASN A 403 ? 0.2399 0.3140 0.5672 -0.0120 0.0110  0.0004  403 ASN A C   
3233  O O   . ASN A 403 ? 0.2503 0.3189 0.5682 -0.0143 0.0163  0.0007  403 ASN A O   
3234  C CB  . ASN A 403 ? 0.2602 0.3180 0.5677 -0.0107 -0.0013 0.0004  403 ASN A CB  
3235  C CG  . ASN A 403 ? 0.2575 0.3086 0.5563 -0.0068 -0.0083 0.0002  403 ASN A CG  
3236  O OD1 . ASN A 403 ? 0.2511 0.3048 0.5552 -0.0064 -0.0155 0.0000  403 ASN A OD1 
3237  N ND2 . ASN A 403 ? 0.2838 0.3260 0.5687 -0.0042 -0.0064 0.0002  403 ASN A ND2 
3238  N N   . ILE A 404 ? 0.2176 0.3036 0.5621 -0.0136 0.0111  0.0004  404 ILE A N   
3239  C CA  . ILE A 404 ? 0.2248 0.3181 0.5773 -0.0181 0.0189  0.0007  404 ILE A CA  
3240  C C   . ILE A 404 ? 0.2267 0.3262 0.5900 -0.0244 0.0151  0.0018  404 ILE A C   
3241  O O   . ILE A 404 ? 0.2350 0.3366 0.6047 -0.0238 0.0065  0.0017  404 ILE A O   
3242  C CB  . ILE A 404 ? 0.2187 0.3224 0.5835 -0.0141 0.0255  -0.0005 404 ILE A CB  
3243  C CG1 . ILE A 404 ? 0.2177 0.3329 0.6013 -0.0114 0.0207  -0.0010 404 ILE A CG1 
3244  C CG2 . ILE A 404 ? 0.2160 0.3125 0.5700 -0.0081 0.0287  -0.0016 404 ILE A CG2 
3245  C CD1 . ILE A 404 ? 0.2107 0.3376 0.6090 -0.0080 0.0282  -0.0024 404 ILE A CD1 
3246  N N   . LEU A 405 ? 0.2210 0.3235 0.5867 -0.0305 0.0215  0.0029  405 LEU A N   
3247  C CA  . LEU A 405 ? 0.2124 0.3229 0.5916 -0.0372 0.0198  0.0042  405 LEU A CA  
3248  C C   . LEU A 405 ? 0.2008 0.3260 0.5968 -0.0382 0.0285  0.0042  405 LEU A C   
3249  O O   . LEU A 405 ? 0.2186 0.3431 0.6089 -0.0388 0.0378  0.0043  405 LEU A O   
3250  C CB  . LEU A 405 ? 0.2272 0.3275 0.5941 -0.0438 0.0196  0.0059  405 LEU A CB  
3251  C CG  . LEU A 405 ? 0.2367 0.3414 0.6142 -0.0517 0.0160  0.0076  405 LEU A CG  
3252  C CD1 . LEU A 405 ? 0.2444 0.3496 0.6281 -0.0506 0.0045  0.0066  405 LEU A CD1 
3253  C CD2 . LEU A 405 ? 0.2324 0.3262 0.5976 -0.0585 0.0167  0.0096  405 LEU A CD2 
3254  N N   . ALA A 406 ? 0.1870 0.3259 0.6039 -0.0379 0.0257  0.0038  406 ALA A N   
3255  C CA  . ALA A 406 ? 0.1873 0.3411 0.6214 -0.0364 0.0342  0.0030  406 ALA A CA  
3256  C C   . ALA A 406 ? 0.2041 0.3726 0.6601 -0.0428 0.0343  0.0042  406 ALA A C   
3257  O O   . ALA A 406 ? 0.2090 0.3794 0.6731 -0.0451 0.0245  0.0048  406 ALA A O   
3258  C CB  . ALA A 406 ? 0.1838 0.3417 0.6246 -0.0273 0.0316  0.0007  406 ALA A CB  
3259  N N   . SER A 407 ? 0.2145 0.3945 0.6815 -0.0448 0.0455  0.0042  407 SER A N   
3260  C CA  . SER A 407 ? 0.2289 0.4259 0.7199 -0.0503 0.0478  0.0053  407 SER A CA  
3261  C C   . SER A 407 ? 0.2386 0.4491 0.7421 -0.0471 0.0604  0.0036  407 SER A C   
3262  O O   . SER A 407 ? 0.2455 0.4495 0.7346 -0.0441 0.0686  0.0025  407 SER A O   
3263  C CB  . SER A 407 ? 0.2368 0.4299 0.7233 -0.0612 0.0493  0.0086  407 SER A CB  
3264  O OG  . SER A 407 ? 0.2255 0.4349 0.7353 -0.0677 0.0520  0.0101  407 SER A OG  
3265  N N   . LYS A 408 ? 0.2678 0.4970 0.7980 -0.0480 0.0619  0.0032  408 LYS A N   
3266  C CA  . LYS A 408 ? 0.3070 0.5508 0.8513 -0.0458 0.0749  0.0015  408 LYS A CA  
3267  C C   . LYS A 408 ? 0.3406 0.5865 0.8812 -0.0549 0.0868  0.0039  408 LYS A C   
3268  O O   . LYS A 408 ? 0.3669 0.6231 0.9150 -0.0537 0.0994  0.0025  408 LYS A O   
3269  C CB  . LYS A 408 ? 0.3241 0.5890 0.9010 -0.0443 0.0725  0.0005  408 LYS A CB  
3270  C CG  . LYS A 408 ? 0.3491 0.6132 0.9321 -0.0358 0.0597  -0.0013 408 LYS A CG  
3271  C CD  . LYS A 408 ? 0.3754 0.6594 0.9908 -0.0348 0.0545  -0.0019 408 LYS A CD  
3272  C CE  . LYS A 408 ? 0.4070 0.6883 1.0249 -0.0250 0.0434  -0.0039 408 LYS A CE  
3273  N NZ  . LYS A 408 ? 0.4217 0.7206 1.0699 -0.0236 0.0359  -0.0043 408 LYS A NZ  
3274  N N   . THR A 409 ? 0.3639 0.6002 0.8935 -0.0638 0.0829  0.0075  409 THR A N   
3275  C CA  . THR A 409 ? 0.3707 0.6086 0.8977 -0.0735 0.0928  0.0107  409 THR A CA  
3276  C C   . THR A 409 ? 0.3969 0.6134 0.8951 -0.0779 0.0900  0.0132  409 THR A C   
3277  O O   . THR A 409 ? 0.4277 0.6320 0.9160 -0.0771 0.0780  0.0135  409 THR A O   
3278  C CB  . THR A 409 ? 0.3779 0.6316 0.9307 -0.0815 0.0908  0.0130  409 THR A CB  
3279  O OG1 . THR A 409 ? 0.3366 0.5861 0.8935 -0.0821 0.0752  0.0134  409 THR A OG1 
3280  C CG2 . THR A 409 ? 0.3837 0.6609 0.9666 -0.0779 0.0968  0.0107  409 THR A CG2 
3281  N N   . ALA A 410 ? 0.4004 0.6119 0.8845 -0.0819 0.1013  0.0148  410 ALA A N   
3282  C CA  . ALA A 410 ? 0.3925 0.5856 0.8519 -0.0877 0.1001  0.0179  410 ALA A CA  
3283  C C   . ALA A 410 ? 0.4009 0.5885 0.8626 -0.0947 0.0887  0.0210  410 ALA A C   
3284  O O   . ALA A 410 ? 0.4045 0.6051 0.8878 -0.1002 0.0873  0.0224  410 ALA A O   
3285  C CB  . ALA A 410 ? 0.3893 0.5846 0.8434 -0.0945 0.1140  0.0205  410 ALA A CB  
3286  N N   . PHE A 411 ? 0.3653 0.5336 0.8052 -0.0948 0.0808  0.0218  411 PHE A N   
3287  C CA  . PHE A 411 ? 0.3704 0.5312 0.8102 -0.1007 0.0696  0.0240  411 PHE A CA  
3288  C C   . PHE A 411 ? 0.3892 0.5289 0.8028 -0.1034 0.0669  0.0262  411 PHE A C   
3289  O O   . PHE A 411 ? 0.3603 0.4910 0.7561 -0.0993 0.0714  0.0254  411 PHE A O   
3290  C CB  . PHE A 411 ? 0.3349 0.4965 0.7825 -0.0947 0.0568  0.0211  411 PHE A CB  
3291  C CG  . PHE A 411 ? 0.3099 0.4609 0.7414 -0.0847 0.0530  0.0179  411 PHE A CG  
3292  C CD1 . PHE A 411 ? 0.3135 0.4462 0.7241 -0.0839 0.0459  0.0181  411 PHE A CD1 
3293  C CD2 . PHE A 411 ? 0.2925 0.4518 0.7298 -0.0762 0.0571  0.0148  411 PHE A CD2 
3294  C CE1 . PHE A 411 ? 0.3003 0.4244 0.6973 -0.0752 0.0432  0.0154  411 PHE A CE1 
3295  C CE2 . PHE A 411 ? 0.2742 0.4237 0.6971 -0.0677 0.0539  0.0123  411 PHE A CE2 
3296  C CZ  . PHE A 411 ? 0.2913 0.4237 0.6944 -0.0675 0.0472  0.0127  411 PHE A CZ  
3297  N N   . GLU A 412 ? 0.4676 0.5996 0.8801 -0.1103 0.0589  0.0287  412 GLU A N   
3298  C CA  . GLU A 412 ? 0.5179 0.6305 0.9084 -0.1139 0.0557  0.0312  412 GLU A CA  
3299  C C   . GLU A 412 ? 0.4161 0.5157 0.7935 -0.1065 0.0454  0.0282  412 GLU A C   
3300  O O   . GLU A 412 ? 0.4022 0.5042 0.7885 -0.1043 0.0362  0.0261  412 GLU A O   
3301  C CB  . GLU A 412 ? 0.6285 0.7366 1.0234 -0.1241 0.0501  0.0348  412 GLU A CB  
3302  C CG  . GLU A 412 ? 0.7788 0.8983 1.1865 -0.1338 0.0597  0.0389  412 GLU A CG  
3303  C CD  . GLU A 412 ? 0.8654 0.9800 1.2578 -0.1365 0.0717  0.0419  412 GLU A CD  
3304  O OE1 . GLU A 412 ? 0.7721 0.8864 1.1545 -0.1295 0.0781  0.0396  412 GLU A OE1 
3305  O OE2 . GLU A 412 ? 0.8603 0.9712 1.2510 -0.1465 0.0744  0.0468  412 GLU A OE2 
3306  N N   . LEU A 413 ? 0.4173 0.5030 0.7734 -0.1035 0.0468  0.0282  413 LEU A N   
3307  C CA  . LEU A 413 ? 0.3942 0.4651 0.7358 -0.0984 0.0374  0.0263  413 LEU A CA  
3308  C C   . LEU A 413 ? 0.3577 0.4133 0.6874 -0.1049 0.0325  0.0293  413 LEU A C   
3309  O O   . LEU A 413 ? 0.3513 0.4042 0.6771 -0.1120 0.0380  0.0332  413 LEU A O   
3310  C CB  . LEU A 413 ? 0.3956 0.4612 0.7227 -0.0906 0.0413  0.0242  413 LEU A CB  
3311  C CG  . LEU A 413 ? 0.3790 0.4568 0.7156 -0.0830 0.0448  0.0208  413 LEU A CG  
3312  C CD1 . LEU A 413 ? 0.3729 0.4457 0.6953 -0.0778 0.0511  0.0197  413 LEU A CD1 
3313  C CD2 . LEU A 413 ? 0.3816 0.4597 0.7230 -0.0772 0.0349  0.0178  413 LEU A CD2 
3314  N N   . PRO A 414 ? 0.3706 0.4144 0.6925 -0.1024 0.0223  0.0276  414 PRO A N   
3315  C CA  . PRO A 414 ? 0.3663 0.3932 0.6740 -0.1066 0.0179  0.0299  414 PRO A CA  
3316  C C   . PRO A 414 ? 0.3555 0.3737 0.6457 -0.1032 0.0231  0.0306  414 PRO A C   
3317  O O   . PRO A 414 ? 0.3654 0.3870 0.6526 -0.0958 0.0259  0.0279  414 PRO A O   
3318  C CB  . PRO A 414 ? 0.3710 0.3903 0.6767 -0.1027 0.0066  0.0266  414 PRO A CB  
3319  C CG  . PRO A 414 ? 0.3650 0.3922 0.6738 -0.0937 0.0067  0.0226  414 PRO A CG  
3320  C CD  . PRO A 414 ? 0.3646 0.4097 0.6897 -0.0951 0.0145  0.0233  414 PRO A CD  
3321  N N   . GLU A 415 ? 0.3835 0.3899 0.6623 -0.1089 0.0237  0.0344  415 GLU A N   
3322  C CA  . GLU A 415 ? 0.4025 0.4013 0.6656 -0.1078 0.0292  0.0361  415 GLU A CA  
3323  C C   . GLU A 415 ? 0.3878 0.3678 0.6354 -0.1081 0.0220  0.0373  415 GLU A C   
3324  O O   . GLU A 415 ? 0.3981 0.3706 0.6462 -0.1142 0.0170  0.0397  415 GLU A O   
3325  C CB  . GLU A 415 ? 0.4748 0.4784 0.7389 -0.1156 0.0388  0.0406  415 GLU A CB  
3326  C CG  . GLU A 415 ? 0.5607 0.5648 0.8138 -0.1123 0.0474  0.0406  415 GLU A CG  
3327  C CD  . GLU A 415 ? 0.6378 0.6473 0.8905 -0.1192 0.0583  0.0444  415 GLU A CD  
3328  O OE1 . GLU A 415 ? 0.6676 0.6906 0.9375 -0.1236 0.0620  0.0451  415 GLU A OE1 
3329  O OE2 . GLU A 415 ? 0.5725 0.5736 0.8086 -0.1199 0.0629  0.0464  415 GLU A OE2 
3330  N N   . LEU A 416 ? 0.3426 0.3154 0.5772 -0.1016 0.0217  0.0357  416 LEU A N   
3331  C CA  . LEU A 416 ? 0.3412 0.2969 0.5614 -0.1008 0.0155  0.0367  416 LEU A CA  
3332  C C   . LEU A 416 ? 0.3550 0.3045 0.5613 -0.1021 0.0209  0.0398  416 LEU A C   
3333  O O   . LEU A 416 ? 0.3498 0.3038 0.5526 -0.0969 0.0254  0.0379  416 LEU A O   
3334  C CB  . LEU A 416 ? 0.3280 0.2801 0.5458 -0.0920 0.0089  0.0320  416 LEU A CB  
3335  C CG  . LEU A 416 ? 0.3383 0.2736 0.5443 -0.0903 0.0014  0.0321  416 LEU A CG  
3336  C CD1 . LEU A 416 ? 0.3429 0.2771 0.5511 -0.0831 -0.0050 0.0271  416 LEU A CD1 
3337  C CD2 . LEU A 416 ? 0.3417 0.2694 0.5343 -0.0879 0.0033  0.0335  416 LEU A CD2 
3338  N N   . THR A 417 ? 0.3817 0.3195 0.5791 -0.1088 0.0195  0.0446  417 THR A N   
3339  C CA  . THR A 417 ? 0.4088 0.3371 0.5901 -0.1098 0.0224  0.0478  417 THR A CA  
3340  C C   . THR A 417 ? 0.4114 0.3215 0.5809 -0.1092 0.0132  0.0492  417 THR A C   
3341  O O   . THR A 417 ? 0.4077 0.3109 0.5806 -0.1112 0.0062  0.0496  417 THR A O   
3342  C CB  . THR A 417 ? 0.4240 0.3552 0.6037 -0.1188 0.0308  0.0529  417 THR A CB  
3343  O OG1 . THR A 417 ? 0.4104 0.3382 0.5959 -0.1266 0.0276  0.0562  417 THR A OG1 
3344  C CG2 . THR A 417 ? 0.4382 0.3881 0.6301 -0.1183 0.0403  0.0508  417 THR A CG2 
3345  N N   . ILE A 418 ? 0.3892 0.2909 0.5448 -0.1061 0.0130  0.0500  418 ILE A N   
3346  C CA  . ILE A 418 ? 0.3936 0.2781 0.5382 -0.1054 0.0046  0.0519  418 ILE A CA  
3347  C C   . ILE A 418 ? 0.4021 0.2766 0.5314 -0.1112 0.0072  0.0577  418 ILE A C   
3348  O O   . ILE A 418 ? 0.3932 0.2737 0.5178 -0.1123 0.0152  0.0586  418 ILE A O   
3349  C CB  . ILE A 418 ? 0.3830 0.2652 0.5255 -0.0956 -0.0006 0.0471  418 ILE A CB  
3350  C CG1 . ILE A 418 ? 0.3856 0.2717 0.5211 -0.0919 0.0044  0.0463  418 ILE A CG1 
3351  C CG2 . ILE A 418 ? 0.3613 0.2527 0.5172 -0.0902 -0.0028 0.0416  418 ILE A CG2 
3352  C CD1 . ILE A 418 ? 0.3866 0.2722 0.5221 -0.0828 0.0000  0.0418  418 ILE A CD1 
3353  N N   . GLU A 419 ? 0.4293 0.2876 0.5503 -0.1144 0.0001  0.0615  419 GLU A N   
3354  C CA  . GLU A 419 ? 0.4655 0.3100 0.5691 -0.1183 -0.0005 0.0670  419 GLU A CA  
3355  C C   . GLU A 419 ? 0.4521 0.2837 0.5488 -0.1116 -0.0106 0.0656  419 GLU A C   
3356  O O   . GLU A 419 ? 0.4378 0.2632 0.5399 -0.1096 -0.0182 0.0641  419 GLU A O   
3357  C CB  . GLU A 419 ? 0.4952 0.3292 0.5939 -0.1285 -0.0014 0.0738  419 GLU A CB  
3358  C CG  . GLU A 419 ? 0.5481 0.3937 0.6522 -0.1368 0.0093  0.0766  419 GLU A CG  
3359  C CD  . GLU A 419 ? 0.5965 0.4346 0.7018 -0.1469 0.0078  0.0823  419 GLU A CD  
3360  O OE1 . GLU A 419 ? 0.6994 0.5203 0.7976 -0.1485 -0.0012 0.0852  419 GLU A OE1 
3361  O OE2 . GLU A 419 ? 0.5749 0.4245 0.6895 -0.1534 0.0157  0.0839  419 GLU A OE2 
3362  N N   . VAL A 420 ? 0.4590 0.2861 0.5437 -0.1085 -0.0106 0.0662  420 VAL A N   
3363  C CA  . VAL A 420 ? 0.4600 0.2774 0.5399 -0.1014 -0.0196 0.0644  420 VAL A CA  
3364  C C   . VAL A 420 ? 0.4862 0.2858 0.5486 -0.1054 -0.0243 0.0707  420 VAL A C   
3365  O O   . VAL A 420 ? 0.4736 0.2714 0.5246 -0.1115 -0.0186 0.0751  420 VAL A O   
3366  C CB  . VAL A 420 ? 0.4588 0.2867 0.5417 -0.0935 -0.0172 0.0591  420 VAL A CB  
3367  C CG1 . VAL A 420 ? 0.4799 0.2991 0.5588 -0.0864 -0.0260 0.0575  420 VAL A CG1 
3368  C CG2 . VAL A 420 ? 0.4405 0.2839 0.5398 -0.0894 -0.0137 0.0534  420 VAL A CG2 
3369  N N   . THR A 421 ? 0.5036 0.2900 0.5642 -0.1018 -0.0350 0.0709  421 THR A N   
3370  C CA  . THR A 421 ? 0.5152 0.2831 0.5601 -0.1039 -0.0421 0.0764  421 THR A CA  
3371  C C   . THR A 421 ? 0.4929 0.2564 0.5379 -0.0944 -0.0506 0.0730  421 THR A C   
3372  O O   . THR A 421 ? 0.4583 0.2276 0.5162 -0.0874 -0.0536 0.0674  421 THR A O   
3373  C CB  . THR A 421 ? 0.5400 0.2945 0.5841 -0.1092 -0.0477 0.0806  421 THR A CB  
3374  O OG1 . THR A 421 ? 0.5431 0.3046 0.5899 -0.1179 -0.0391 0.0832  421 THR A OG1 
3375  C CG2 . THR A 421 ? 0.5688 0.3027 0.5961 -0.1121 -0.0554 0.0871  421 THR A CG2 
3376  N N   . PRO A 422 ? 0.5023 0.2573 0.5339 -0.0936 -0.0541 0.0758  422 PRO A N   
3377  C CA  . PRO A 422 ? 0.5273 0.2807 0.5434 -0.0999 -0.0480 0.0803  422 PRO A CA  
3378  C C   . PRO A 422 ? 0.5181 0.2898 0.5403 -0.1006 -0.0360 0.0768  422 PRO A C   
3379  O O   . PRO A 422 ? 0.5195 0.3037 0.5535 -0.0938 -0.0346 0.0706  422 PRO A O   
3380  C CB  . PRO A 422 ? 0.5189 0.2641 0.5245 -0.0952 -0.0551 0.0808  422 PRO A CB  
3381  C CG  . PRO A 422 ? 0.5183 0.2537 0.5302 -0.0897 -0.0667 0.0799  422 PRO A CG  
3382  C CD  . PRO A 422 ? 0.4983 0.2458 0.5297 -0.0858 -0.0643 0.0740  422 PRO A CD  
3383  N N   . GLU A 423 ? 0.5642 0.3366 0.5777 -0.1088 -0.0277 0.0810  423 GLU A N   
3384  C CA  . GLU A 423 ? 0.5842 0.3729 0.6026 -0.1105 -0.0157 0.0784  423 GLU A CA  
3385  C C   . GLU A 423 ? 0.5718 0.3646 0.5828 -0.1063 -0.0130 0.0756  423 GLU A C   
3386  O O   . GLU A 423 ? 0.5782 0.3862 0.5994 -0.1028 -0.0065 0.0704  423 GLU A O   
3387  C CB  . GLU A 423 ? 0.6291 0.4159 0.6397 -0.1209 -0.0078 0.0843  423 GLU A CB  
3388  C CG  . GLU A 423 ? 0.7013 0.5058 0.7187 -0.1225 0.0052  0.0815  423 GLU A CG  
3389  C CD  . GLU A 423 ? 0.7372 0.5432 0.7513 -0.1327 0.0142  0.0867  423 GLU A CD  
3390  O OE1 . GLU A 423 ? 0.7086 0.5011 0.7150 -0.1390 0.0100  0.0928  423 GLU A OE1 
3391  O OE2 . GLU A 423 ? 0.7339 0.5543 0.7532 -0.1341 0.0254  0.0846  423 GLU A OE2 
3392  N N   . LYS A 424 ? 0.5992 0.3784 0.5927 -0.1066 -0.0185 0.0788  424 LYS A N   
3393  C CA  . LYS A 424 ? 0.6595 0.4409 0.6424 -0.1049 -0.0150 0.0770  424 LYS A CA  
3394  C C   . LYS A 424 ? 0.6366 0.4082 0.6124 -0.0992 -0.0260 0.0763  424 LYS A C   
3395  O O   . LYS A 424 ? 0.6346 0.4107 0.6073 -0.0955 -0.0246 0.0728  424 LYS A O   
3396  C CB  . LYS A 424 ? 0.7604 0.5370 0.7251 -0.1133 -0.0067 0.0820  424 LYS A CB  
3397  C CG  . LYS A 424 ? 0.8433 0.6335 0.8159 -0.1186 0.0068  0.0818  424 LYS A CG  
3398  C CD  . LYS A 424 ? 0.8731 0.6796 0.8516 -0.1157 0.0173  0.0760  424 LYS A CD  
3399  C CE  . LYS A 424 ? 0.9158 0.7329 0.8976 -0.1220 0.0306  0.0772  424 LYS A CE  
3400  N NZ  . LYS A 424 ? 0.8898 0.6971 0.8510 -0.1304 0.0363  0.0833  424 LYS A NZ  
3401  N N   . ASP A 425 ? 0.5851 0.3435 0.5590 -0.0983 -0.0369 0.0794  425 ASP A N   
3402  C CA  . ASP A 425 ? 0.5839 0.3323 0.5512 -0.0934 -0.0481 0.0795  425 ASP A CA  
3403  C C   . ASP A 425 ? 0.5608 0.3044 0.5405 -0.0883 -0.0585 0.0788  425 ASP A C   
3404  O O   . ASP A 425 ? 0.5554 0.2864 0.5303 -0.0917 -0.0636 0.0836  425 ASP A O   
3405  C CB  . ASP A 425 ? 0.6134 0.3454 0.5557 -0.0990 -0.0508 0.0859  425 ASP A CB  
3406  C CG  . ASP A 425 ? 0.6156 0.3363 0.5481 -0.0948 -0.0626 0.0866  425 ASP A CG  
3407  O OD1 . ASP A 425 ? 0.5894 0.3142 0.5358 -0.0872 -0.0700 0.0823  425 ASP A OD1 
3408  O OD2 . ASP A 425 ? 0.6463 0.3536 0.5568 -0.0995 -0.0646 0.0916  425 ASP A OD2 
3409  N N   . LEU A 426 ? 0.5374 0.2905 0.5323 -0.0800 -0.0616 0.0727  426 LEU A N   
3410  C CA  . LEU A 426 ? 0.5482 0.2991 0.5564 -0.0739 -0.0704 0.0707  426 LEU A CA  
3411  C C   . LEU A 426 ? 0.5678 0.3002 0.5655 -0.0734 -0.0828 0.0754  426 LEU A C   
3412  O O   . LEU A 426 ? 0.5876 0.3146 0.5939 -0.0698 -0.0901 0.0750  426 LEU A O   
3413  C CB  . LEU A 426 ? 0.5352 0.2999 0.5599 -0.0654 -0.0708 0.0636  426 LEU A CB  
3414  C CG  . LEU A 426 ? 0.5508 0.3333 0.5871 -0.0649 -0.0598 0.0587  426 LEU A CG  
3415  C CD1 . LEU A 426 ? 0.5491 0.3429 0.6001 -0.0568 -0.0612 0.0526  426 LEU A CD1 
3416  C CD2 . LEU A 426 ? 0.5493 0.3356 0.5940 -0.0675 -0.0552 0.0585  426 LEU A CD2 
3417  N N   . ASN A 427 ? 0.5775 0.2998 0.5568 -0.0766 -0.0859 0.0796  427 ASN A N   
3418  C CA  . ASN A 427 ? 0.6200 0.3241 0.5890 -0.0758 -0.0986 0.0843  427 ASN A CA  
3419  C C   . ASN A 427 ? 0.6271 0.3164 0.5880 -0.0818 -0.1010 0.0906  427 ASN A C   
3420  O O   . ASN A 427 ? 0.6052 0.2786 0.5597 -0.0808 -0.1123 0.0946  427 ASN A O   
3421  C CB  . ASN A 427 ? 0.6565 0.3512 0.6050 -0.0785 -0.1021 0.0878  427 ASN A CB  
3422  C CG  . ASN A 427 ? 0.6456 0.3467 0.6005 -0.0715 -0.1075 0.0831  427 ASN A CG  
3423  O OD1 . ASN A 427 ? 0.6261 0.3323 0.5985 -0.0639 -0.1139 0.0792  427 ASN A OD1 
3424  N ND2 . ASN A 427 ? 0.6483 0.3497 0.5895 -0.0740 -0.1046 0.0832  427 ASN A ND2 
3425  N N   . GLU A 428 ? 0.6475 0.3418 0.6085 -0.0883 -0.0907 0.0918  428 GLU A N   
3426  C CA  . GLU A 428 ? 0.7213 0.4017 0.6727 -0.0958 -0.0916 0.0986  428 GLU A CA  
3427  C C   . GLU A 428 ? 0.6742 0.3510 0.6403 -0.0923 -0.0979 0.0971  428 GLU A C   
3428  O O   . GLU A 428 ? 0.6581 0.3220 0.6179 -0.0979 -0.1003 0.1025  428 GLU A O   
3429  C CB  . GLU A 428 ? 0.7911 0.4791 0.7381 -0.1045 -0.0779 0.1005  428 GLU A CB  
3430  C CG  . GLU A 428 ? 0.8768 0.5626 0.8036 -0.1101 -0.0717 0.1039  428 GLU A CG  
3431  C CD  . GLU A 428 ? 0.9544 0.6504 0.8796 -0.1179 -0.0570 0.1049  428 GLU A CD  
3432  O OE1 . GLU A 428 ? 0.9605 0.6632 0.9002 -0.1196 -0.0533 0.1039  428 GLU A OE1 
3433  O OE2 . GLU A 428 ? 0.9346 0.6326 0.8456 -0.1219 -0.0490 0.1062  428 GLU A OE2 
3434  N N   . GLY A 429 ? 0.6462 0.3336 0.6313 -0.0831 -0.1005 0.0899  429 GLY A N   
3435  C CA  . GLY A 429 ? 0.6288 0.3111 0.6263 -0.0785 -0.1077 0.0878  429 GLY A CA  
3436  C C   . GLY A 429 ? 0.5965 0.2919 0.6135 -0.0680 -0.1094 0.0795  429 GLY A C   
3437  O O   . GLY A 429 ? 0.6247 0.3356 0.6479 -0.0651 -0.1033 0.0751  429 GLY A O   
3438  N N   . LYS A 430 ? 0.5771 0.2665 0.6043 -0.0624 -0.1169 0.0772  430 LYS A N   
3439  C CA  . LYS A 430 ? 0.5870 0.2873 0.6318 -0.0521 -0.1190 0.0696  430 LYS A CA  
3440  C C   . LYS A 430 ? 0.5383 0.2514 0.5967 -0.0512 -0.1112 0.0640  430 LYS A C   
3441  O O   . LYS A 430 ? 0.5012 0.2272 0.5737 -0.0439 -0.1092 0.0573  430 LYS A O   
3442  C CB  . LYS A 430 ? 0.6648 0.3523 0.7136 -0.0451 -0.1317 0.0694  430 LYS A CB  
3443  C CG  . LYS A 430 ? 0.7517 0.4263 0.7874 -0.0456 -0.1407 0.0749  430 LYS A CG  
3444  C CD  . LYS A 430 ? 0.8818 0.5541 0.9271 -0.0356 -0.1514 0.0721  430 LYS A CD  
3445  C CE  . LYS A 430 ? 0.9682 0.6481 1.0102 -0.0345 -0.1517 0.0720  430 LYS A CE  
3446  N NZ  . LYS A 430 ? 1.0546 0.7314 1.1043 -0.0262 -0.1631 0.0707  430 LYS A NZ  
3447  N N   . ILE A 431 ? 0.5199 0.2297 0.5735 -0.0591 -0.1066 0.0671  431 ILE A N   
3448  C CA  . ILE A 431 ? 0.4838 0.2032 0.5490 -0.0590 -0.1008 0.0625  431 ILE A CA  
3449  C C   . ILE A 431 ? 0.4709 0.2013 0.5334 -0.0667 -0.0897 0.0640  431 ILE A C   
3450  O O   . ILE A 431 ? 0.4728 0.1964 0.5224 -0.0750 -0.0876 0.0704  431 ILE A O   
3451  C CB  . ILE A 431 ? 0.4964 0.2010 0.5616 -0.0607 -0.1071 0.0640  431 ILE A CB  
3452  C CG1 . ILE A 431 ? 0.5012 0.1957 0.5713 -0.0519 -0.1178 0.0614  431 ILE A CG1 
3453  C CG2 . ILE A 431 ? 0.4901 0.2043 0.5653 -0.0623 -0.1009 0.0598  431 ILE A CG2 
3454  C CD1 . ILE A 431 ? 0.5222 0.1974 0.5885 -0.0542 -0.1257 0.0642  431 ILE A CD1 
3455  N N   . ALA A 432 ? 0.4467 0.1937 0.5214 -0.0640 -0.0827 0.0581  432 ALA A N   
3456  C CA  . ALA A 432 ? 0.4518 0.2105 0.5267 -0.0704 -0.0724 0.0589  432 ALA A CA  
3457  C C   . ALA A 432 ? 0.4402 0.2013 0.5230 -0.0737 -0.0701 0.0574  432 ALA A C   
3458  O O   . ALA A 432 ? 0.4381 0.1944 0.5278 -0.0695 -0.0757 0.0541  432 ALA A O   
3459  C CB  . ALA A 432 ? 0.4398 0.2155 0.5206 -0.0658 -0.0658 0.0543  432 ALA A CB  
3460  N N   . SER A 433 ? 0.4349 0.2028 0.5164 -0.0815 -0.0621 0.0600  433 SER A N   
3461  C CA  . SER A 433 ? 0.4391 0.2144 0.5309 -0.0842 -0.0586 0.0577  433 SER A CA  
3462  C C   . SER A 433 ? 0.4300 0.2236 0.5275 -0.0865 -0.0480 0.0561  433 SER A C   
3463  O O   . SER A 433 ? 0.4174 0.2144 0.5075 -0.0901 -0.0421 0.0593  433 SER A O   
3464  C CB  . SER A 433 ? 0.4360 0.1988 0.5237 -0.0926 -0.0615 0.0628  433 SER A CB  
3465  O OG  . SER A 433 ? 0.4373 0.2004 0.5168 -0.1019 -0.0551 0.0690  433 SER A OG  
3466  N N   . ILE A 434 ? 0.4331 0.2370 0.5430 -0.0846 -0.0459 0.0514  434 ILE A N   
3467  C CA  . ILE A 434 ? 0.4230 0.2432 0.5403 -0.0875 -0.0370 0.0502  434 ILE A CA  
3468  C C   . ILE A 434 ? 0.4380 0.2583 0.5624 -0.0937 -0.0373 0.0510  434 ILE A C   
3469  O O   . ILE A 434 ? 0.4422 0.2620 0.5740 -0.0903 -0.0418 0.0468  434 ILE A O   
3470  C CB  . ILE A 434 ? 0.3924 0.2266 0.5186 -0.0793 -0.0342 0.0437  434 ILE A CB  
3471  C CG1 . ILE A 434 ? 0.4075 0.2430 0.5281 -0.0741 -0.0334 0.0430  434 ILE A CG1 
3472  C CG2 . ILE A 434 ? 0.3880 0.2377 0.5231 -0.0823 -0.0264 0.0425  434 ILE A CG2 
3473  C CD1 . ILE A 434 ? 0.3997 0.2487 0.5287 -0.0667 -0.0302 0.0372  434 ILE A CD1 
3474  N N   . LYS A 435 ? 0.4597 0.2816 0.5820 -0.1028 -0.0318 0.0561  435 LYS A N   
3475  C CA  . LYS A 435 ? 0.4729 0.2981 0.6039 -0.1098 -0.0307 0.0572  435 LYS A CA  
3476  C C   . LYS A 435 ? 0.4677 0.3130 0.6105 -0.1094 -0.0226 0.0541  435 LYS A C   
3477  O O   . LYS A 435 ? 0.4629 0.3171 0.6038 -0.1113 -0.0143 0.0558  435 LYS A O   
3478  C CB  . LYS A 435 ? 0.5045 0.3205 0.6270 -0.1202 -0.0289 0.0650  435 LYS A CB  
3479  C CG  . LYS A 435 ? 0.5783 0.3731 0.6914 -0.1223 -0.0383 0.0686  435 LYS A CG  
3480  C CD  . LYS A 435 ? 0.6249 0.4089 0.7286 -0.1333 -0.0370 0.0770  435 LYS A CD  
3481  C CE  . LYS A 435 ? 0.6720 0.4572 0.7635 -0.1351 -0.0304 0.0810  435 LYS A CE  
3482  N NZ  . LYS A 435 ? 0.7474 0.5145 0.8239 -0.1423 -0.0334 0.0888  435 LYS A NZ  
3483  N N   . THR A 436 ? 0.4438 0.2957 0.5984 -0.1064 -0.0252 0.0492  436 THR A N   
3484  C CA  . THR A 436 ? 0.4122 0.2825 0.5788 -0.1055 -0.0189 0.0461  436 THR A CA  
3485  C C   . THR A 436 ? 0.4325 0.3074 0.6086 -0.1144 -0.0174 0.0487  436 THR A C   
3486  O O   . THR A 436 ? 0.4031 0.2676 0.5797 -0.1184 -0.0240 0.0499  436 THR A O   
3487  C CB  . THR A 436 ? 0.3809 0.2557 0.5537 -0.0967 -0.0229 0.0394  436 THR A CB  
3488  O OG1 . THR A 436 ? 0.3661 0.2383 0.5320 -0.0887 -0.0237 0.0370  436 THR A OG1 
3489  C CG2 . THR A 436 ? 0.3699 0.2624 0.5551 -0.0956 -0.0178 0.0364  436 THR A CG2 
3490  N N   . LYS A 437 ? 0.4307 0.3217 0.6156 -0.1169 -0.0090 0.0490  437 LYS A N   
3491  C CA  . LYS A 437 ? 0.4594 0.3586 0.6564 -0.1250 -0.0065 0.0511  437 LYS A CA  
3492  C C   . LYS A 437 ? 0.4194 0.3376 0.6306 -0.1212 -0.0022 0.0468  437 LYS A C   
3493  O O   . LYS A 437 ? 0.3973 0.3252 0.6081 -0.1175 0.0049  0.0458  437 LYS A O   
3494  C CB  . LYS A 437 ? 0.5213 0.4195 0.7132 -0.1342 0.0007  0.0578  437 LYS A CB  
3495  C CG  . LYS A 437 ? 0.5820 0.4912 0.7878 -0.1432 0.0053  0.0605  437 LYS A CG  
3496  C CD  . LYS A 437 ? 0.6322 0.5425 0.8321 -0.1513 0.0148  0.0668  437 LYS A CD  
3497  C CE  . LYS A 437 ? 0.6702 0.5976 0.8869 -0.1581 0.0224  0.0682  437 LYS A CE  
3498  N NZ  . LYS A 437 ? 0.6736 0.6030 0.8843 -0.1657 0.0329  0.0740  437 LYS A NZ  
3499  N N   . ILE A 438 ? 0.4022 0.3242 0.6248 -0.1215 -0.0076 0.0439  438 ILE A N   
3500  C CA  . ILE A 438 ? 0.3843 0.3231 0.6211 -0.1184 -0.0054 0.0402  438 ILE A CA  
3501  C C   . ILE A 438 ? 0.4151 0.3634 0.6665 -0.1274 -0.0032 0.0429  438 ILE A C   
3502  O O   . ILE A 438 ? 0.4344 0.3758 0.6894 -0.1330 -0.0099 0.0439  438 ILE A O   
3503  C CB  . ILE A 438 ? 0.3733 0.3098 0.6117 -0.1110 -0.0137 0.0344  438 ILE A CB  
3504  C CG1 . ILE A 438 ? 0.3552 0.2820 0.5804 -0.1025 -0.0161 0.0318  438 ILE A CG1 
3505  C CG2 . ILE A 438 ? 0.3697 0.3233 0.6218 -0.1076 -0.0114 0.0310  438 ILE A CG2 
3506  C CD1 . ILE A 438 ? 0.3414 0.2639 0.5663 -0.0959 -0.0239 0.0263  438 ILE A CD1 
3507  N N   . GLU A 439 ? 0.4251 0.3890 0.6849 -0.1289 0.0064  0.0440  439 GLU A N   
3508  C CA  . GLU A 439 ? 0.4470 0.4250 0.7247 -0.1358 0.0097  0.0456  439 GLU A CA  
3509  C C   . GLU A 439 ? 0.3973 0.3872 0.6885 -0.1297 0.0058  0.0403  439 GLU A C   
3510  O O   . GLU A 439 ? 0.3703 0.3698 0.6635 -0.1227 0.0102  0.0375  439 GLU A O   
3511  C CB  . GLU A 439 ? 0.5266 0.5166 0.8080 -0.1395 0.0222  0.0488  439 GLU A CB  
3512  C CG  . GLU A 439 ? 0.6496 0.6305 0.9214 -0.1487 0.0267  0.0553  439 GLU A CG  
3513  C CD  . GLU A 439 ? 0.7947 0.7905 1.0749 -0.1543 0.0394  0.0584  439 GLU A CD  
3514  O OE1 . GLU A 439 ? 0.7621 0.7754 1.0626 -0.1559 0.0423  0.0570  439 GLU A OE1 
3515  O OE2 . GLU A 439 ? 0.8343 0.8237 1.1002 -0.1569 0.0461  0.0621  439 GLU A OE2 
3516  N N   . THR A 440 ? 0.3869 0.3748 0.6864 -0.1327 -0.0030 0.0391  440 THR A N   
3517  C CA  . THR A 440 ? 0.3589 0.3559 0.6695 -0.1275 -0.0083 0.0343  440 THR A CA  
3518  C C   . THR A 440 ? 0.3570 0.3744 0.6882 -0.1310 -0.0026 0.0352  440 THR A C   
3519  O O   . THR A 440 ? 0.3609 0.3852 0.6991 -0.1385 0.0050  0.0394  440 THR A O   
3520  C CB  . THR A 440 ? 0.3538 0.3400 0.6644 -0.1293 -0.0205 0.0323  440 THR A CB  
3521  O OG1 . THR A 440 ? 0.3474 0.3335 0.6674 -0.1402 -0.0220 0.0361  440 THR A OG1 
3522  C CG2 . THR A 440 ? 0.3608 0.3277 0.6524 -0.1246 -0.0262 0.0306  440 THR A CG2 
3523  N N   . SER A 441 ? 0.3630 0.3891 0.7036 -0.1252 -0.0071 0.0310  441 SER A N   
3524  C CA  . SER A 441 ? 0.3731 0.4186 0.7343 -0.1256 -0.0046 0.0302  441 SER A CA  
3525  C C   . SER A 441 ? 0.3649 0.4100 0.7316 -0.1221 -0.0162 0.0261  441 SER A C   
3526  O O   . SER A 441 ? 0.3403 0.3784 0.6960 -0.1138 -0.0208 0.0224  441 SER A O   
3527  C CB  . SER A 441 ? 0.3901 0.4457 0.7510 -0.1183 0.0046  0.0289  441 SER A CB  
3528  O OG  . SER A 441 ? 0.4055 0.4794 0.7850 -0.1216 0.0124  0.0304  441 SER A OG  
3529  N N   . GLU A 442 ? 0.3915 0.4441 0.7752 -0.1287 -0.0211 0.0268  442 GLU A N   
3530  C CA  . GLU A 442 ? 0.3957 0.4486 0.7854 -0.1260 -0.0327 0.0229  442 GLU A CA  
3531  C C   . GLU A 442 ? 0.3903 0.4567 0.7874 -0.1172 -0.0307 0.0200  442 GLU A C   
3532  O O   . GLU A 442 ? 0.4204 0.4992 0.8244 -0.1155 -0.0206 0.0213  442 GLU A O   
3533  C CB  . GLU A 442 ? 0.4244 0.4813 0.8304 -0.1365 -0.0382 0.0250  442 GLU A CB  
3534  C CG  . GLU A 442 ? 0.4191 0.4948 0.8454 -0.1430 -0.0285 0.0288  442 GLU A CG  
3535  C CD  . GLU A 442 ? 0.4184 0.4985 0.8617 -0.1544 -0.0329 0.0315  442 GLU A CD  
3536  O OE1 . GLU A 442 ? 0.4664 0.5321 0.9007 -0.1614 -0.0357 0.0340  442 GLU A OE1 
3537  O OE2 . GLU A 442 ? 0.3951 0.4933 0.8611 -0.1564 -0.0330 0.0314  442 GLU A OE2 
3538  N N   . ASN A 443 ? 0.3481 0.4103 0.7413 -0.1112 -0.0404 0.0160  443 ASN A N   
3539  C CA  . ASN A 443 ? 0.3321 0.4029 0.7279 -0.1021 -0.0401 0.0132  443 ASN A CA  
3540  C C   . ASN A 443 ? 0.3228 0.3838 0.6984 -0.0941 -0.0354 0.0120  443 ASN A C   
3541  O O   . ASN A 443 ? 0.3260 0.3886 0.6982 -0.0861 -0.0371 0.0094  443 ASN A O   
3542  C CB  . ASN A 443 ? 0.3511 0.4430 0.7692 -0.1026 -0.0337 0.0146  443 ASN A CB  
3543  C CG  . ASN A 443 ? 0.3686 0.4711 0.8084 -0.1102 -0.0395 0.0155  443 ASN A CG  
3544  O OD1 . ASN A 443 ? 0.3930 0.5088 0.8500 -0.1166 -0.0326 0.0185  443 ASN A OD1 
3545  N ND2 . ASN A 443 ? 0.3720 0.4686 0.8112 -0.1099 -0.0523 0.0130  443 ASN A ND2 
3546  N N   . PHE A 444 ? 0.3251 0.3757 0.6876 -0.0965 -0.0301 0.0140  444 PHE A N   
3547  C CA  . PHE A 444 ? 0.3427 0.3827 0.6861 -0.0895 -0.0271 0.0127  444 PHE A CA  
3548  C C   . PHE A 444 ? 0.3727 0.3944 0.7003 -0.0899 -0.0347 0.0113  444 PHE A C   
3549  O O   . PHE A 444 ? 0.4021 0.4158 0.7266 -0.0964 -0.0351 0.0135  444 PHE A O   
3550  C CB  . PHE A 444 ? 0.3097 0.3510 0.6482 -0.0903 -0.0157 0.0155  444 PHE A CB  
3551  C CG  . PHE A 444 ? 0.2986 0.3560 0.6489 -0.0882 -0.0066 0.0162  444 PHE A CG  
3552  C CD1 . PHE A 444 ? 0.3017 0.3729 0.6700 -0.0944 -0.0022 0.0185  444 PHE A CD1 
3553  C CD2 . PHE A 444 ? 0.2892 0.3477 0.6325 -0.0800 -0.0022 0.0144  444 PHE A CD2 
3554  C CE1 . PHE A 444 ? 0.2846 0.3704 0.6636 -0.0918 0.0066  0.0185  444 PHE A CE1 
3555  C CE2 . PHE A 444 ? 0.2742 0.3463 0.6279 -0.0778 0.0058  0.0146  444 PHE A CE2 
3556  C CZ  . PHE A 444 ? 0.2636 0.3493 0.6348 -0.0833 0.0104  0.0164  444 PHE A CZ  
3557  N N   . THR A 445 ? 0.4037 0.4183 0.7206 -0.0825 -0.0400 0.0076  445 THR A N   
3558  C CA  . THR A 445 ? 0.3954 0.3932 0.6975 -0.0815 -0.0468 0.0054  445 THR A CA  
3559  C C   . THR A 445 ? 0.3885 0.3771 0.6751 -0.0772 -0.0414 0.0056  445 THR A C   
3560  O O   . THR A 445 ? 0.3797 0.3719 0.6621 -0.0707 -0.0365 0.0048  445 THR A O   
3561  C CB  . THR A 445 ? 0.3961 0.3914 0.6948 -0.0762 -0.0553 0.0011  445 THR A CB  
3562  O OG1 . THR A 445 ? 0.3554 0.3602 0.6697 -0.0803 -0.0606 0.0012  445 THR A OG1 
3563  C CG2 . THR A 445 ? 0.3935 0.3716 0.6782 -0.0757 -0.0627 -0.0018 445 THR A CG2 
3564  N N   . LEU A 446 ? 0.3857 0.3617 0.6642 -0.0809 -0.0431 0.0066  446 LEU A N   
3565  C CA  . LEU A 446 ? 0.3892 0.3544 0.6529 -0.0767 -0.0405 0.0063  446 LEU A CA  
3566  C C   . LEU A 446 ? 0.3835 0.3391 0.6365 -0.0700 -0.0470 0.0015  446 LEU A C   
3567  O O   . LEU A 446 ? 0.3757 0.3259 0.6289 -0.0716 -0.0548 -0.0008 446 LEU A O   
3568  C CB  . LEU A 446 ? 0.4042 0.3598 0.6646 -0.0836 -0.0404 0.0097  446 LEU A CB  
3569  C CG  . LEU A 446 ? 0.3925 0.3571 0.6626 -0.0912 -0.0336 0.0147  446 LEU A CG  
3570  C CD1 . LEU A 446 ? 0.4342 0.3864 0.6977 -0.0976 -0.0341 0.0182  446 LEU A CD1 
3571  C CD2 . LEU A 446 ? 0.3840 0.3585 0.6545 -0.0877 -0.0241 0.0159  446 LEU A CD2 
3572  N N   . LEU A 447 ? 0.4105 0.3650 0.6548 -0.0627 -0.0433 0.0000  447 LEU A N   
3573  C CA  . LEU A 447 ? 0.4431 0.3910 0.6777 -0.0557 -0.0474 -0.0044 447 LEU A CA  
3574  C C   . LEU A 447 ? 0.5094 0.4453 0.7321 -0.0526 -0.0467 -0.0053 447 LEU A C   
3575  O O   . LEU A 447 ? 0.4818 0.4194 0.7022 -0.0510 -0.0405 -0.0032 447 LEU A O   
3576  C CB  . LEU A 447 ? 0.4627 0.4202 0.6980 -0.0496 -0.0432 -0.0052 447 LEU A CB  
3577  C CG  . LEU A 447 ? 0.4856 0.4553 0.7322 -0.0504 -0.0443 -0.0049 447 LEU A CG  
3578  C CD1 . LEU A 447 ? 0.4557 0.4316 0.7001 -0.0435 -0.0405 -0.0057 447 LEU A CD1 
3579  C CD2 . LEU A 447 ? 0.5190 0.4841 0.7659 -0.0520 -0.0537 -0.0077 447 LEU A CD2 
3580  N N   . ASP A 448 ? 0.6061 0.5301 0.8212 -0.0510 -0.0532 -0.0087 448 ASP A N   
3581  C CA  . ASP A 448 ? 0.6231 0.5361 0.8274 -0.0462 -0.0532 -0.0108 448 ASP A CA  
3582  C C   . ASP A 448 ? 0.5092 0.4165 0.7130 -0.0503 -0.0513 -0.0070 448 ASP A C   
3583  O O   . ASP A 448 ? 0.4986 0.4052 0.7077 -0.0576 -0.0527 -0.0040 448 ASP A O   
3584  C CB  . ASP A 448 ? 0.6577 0.5753 0.8571 -0.0384 -0.0483 -0.0125 448 ASP A CB  
3585  C CG  . ASP A 448 ? 0.6802 0.6012 0.8773 -0.0340 -0.0504 -0.0161 448 ASP A CG  
3586  O OD1 . ASP A 448 ? 0.6646 0.5774 0.8568 -0.0334 -0.0569 -0.0197 448 ASP A OD1 
3587  O OD2 . ASP A 448 ? 0.6861 0.6170 0.8857 -0.0312 -0.0459 -0.0151 448 ASP A OD2 
3588  N N   . ASP A 449 ? 0.4946 0.3987 0.6923 -0.0458 -0.0479 -0.0070 449 ASP A N   
3589  C CA  . ASP A 449 ? 0.5211 0.4157 0.7151 -0.0481 -0.0483 -0.0044 449 ASP A CA  
3590  C C   . ASP A 449 ? 0.4516 0.3535 0.6483 -0.0509 -0.0416 0.0004  449 ASP A C   
3591  O O   . ASP A 449 ? 0.4178 0.3295 0.6160 -0.0476 -0.0361 0.0005  449 ASP A O   
3592  C CB  . ASP A 449 ? 0.5456 0.4306 0.7312 -0.0411 -0.0501 -0.0078 449 ASP A CB  
3593  C CG  . ASP A 449 ? 0.5768 0.4497 0.7577 -0.0392 -0.0573 -0.0124 449 ASP A CG  
3594  O OD1 . ASP A 449 ? 0.5805 0.4497 0.7637 -0.0445 -0.0623 -0.0125 449 ASP A OD1 
3595  O OD2 . ASP A 449 ? 0.6142 0.4814 0.7893 -0.0324 -0.0579 -0.0160 449 ASP A OD2 
3596  N N   . LEU A 450 ? 0.4247 0.3207 0.6211 -0.0574 -0.0423 0.0045  450 LEU A N   
3597  C CA  . LEU A 450 ? 0.4124 0.3101 0.6069 -0.0597 -0.0369 0.0089  450 LEU A CA  
3598  C C   . LEU A 450 ? 0.4066 0.2992 0.5938 -0.0528 -0.0365 0.0075  450 LEU A C   
3599  O O   . LEU A 450 ? 0.4265 0.3081 0.6088 -0.0497 -0.0417 0.0053  450 LEU A O   
3600  C CB  . LEU A 450 ? 0.3812 0.2703 0.5747 -0.0678 -0.0391 0.0133  450 LEU A CB  
3601  C CG  . LEU A 450 ? 0.3765 0.2640 0.5653 -0.0712 -0.0346 0.0184  450 LEU A CG  
3602  C CD1 . LEU A 450 ? 0.3622 0.2646 0.5563 -0.0730 -0.0262 0.0203  450 LEU A CD1 
3603  C CD2 . LEU A 450 ? 0.3879 0.2641 0.5739 -0.0792 -0.0378 0.0229  450 LEU A CD2 
3604  N N   . LYS A 451 ? 0.3694 0.2699 0.5563 -0.0506 -0.0305 0.0087  451 LYS A N   
3605  C CA  . LYS A 451 ? 0.4058 0.3024 0.5870 -0.0450 -0.0302 0.0079  451 LYS A CA  
3606  C C   . LYS A 451 ? 0.3643 0.2574 0.5409 -0.0487 -0.0281 0.0126  451 LYS A C   
3607  O O   . LYS A 451 ? 0.3583 0.2573 0.5365 -0.0538 -0.0234 0.0158  451 LYS A O   
3608  C CB  . LYS A 451 ? 0.4305 0.3371 0.6141 -0.0387 -0.0263 0.0048  451 LYS A CB  
3609  C CG  . LYS A 451 ? 0.5029 0.4105 0.6884 -0.0349 -0.0292 0.0003  451 LYS A CG  
3610  C CD  . LYS A 451 ? 0.5509 0.4658 0.7369 -0.0283 -0.0259 -0.0026 451 LYS A CD  
3611  C CE  . LYS A 451 ? 0.5681 0.4858 0.7555 -0.0261 -0.0277 -0.0061 451 LYS A CE  
3612  N NZ  . LYS A 451 ? 0.5595 0.4846 0.7469 -0.0207 -0.0236 -0.0077 451 LYS A NZ  
3613  N N   . ILE A 452 ? 0.3440 0.2267 0.5145 -0.0462 -0.0318 0.0129  452 ILE A N   
3614  C CA  . ILE A 452 ? 0.3456 0.2222 0.5097 -0.0493 -0.0315 0.0174  452 ILE A CA  
3615  C C   . ILE A 452 ? 0.3198 0.1971 0.4816 -0.0428 -0.0313 0.0159  452 ILE A C   
3616  O O   . ILE A 452 ? 0.3142 0.1905 0.4781 -0.0366 -0.0340 0.0120  452 ILE A O   
3617  C CB  . ILE A 452 ? 0.3756 0.2373 0.5347 -0.0531 -0.0378 0.0201  452 ILE A CB  
3618  C CG1 . ILE A 452 ? 0.3982 0.2576 0.5610 -0.0587 -0.0400 0.0204  452 ILE A CG1 
3619  C CG2 . ILE A 452 ? 0.3787 0.2343 0.5297 -0.0578 -0.0369 0.0256  452 ILE A CG2 
3620  C CD1 . ILE A 452 ? 0.4034 0.2713 0.5697 -0.0663 -0.0344 0.0239  452 ILE A CD1 
3621  N N   . SER A 453 ? 0.3174 0.1970 0.4751 -0.0444 -0.0277 0.0187  453 SER A N   
3622  C CA  . SER A 453 ? 0.3148 0.1950 0.4707 -0.0392 -0.0280 0.0177  453 SER A CA  
3623  C C   . SER A 453 ? 0.3409 0.2127 0.4880 -0.0426 -0.0296 0.0222  453 SER A C   
3624  O O   . SER A 453 ? 0.3639 0.2362 0.5065 -0.0486 -0.0260 0.0257  453 SER A O   
3625  C CB  . SER A 453 ? 0.3030 0.1958 0.4630 -0.0364 -0.0220 0.0156  453 SER A CB  
3626  O OG  . SER A 453 ? 0.2901 0.1828 0.4476 -0.0331 -0.0223 0.0156  453 SER A OG  
3627  N N   . TYR A 454 ? 0.3519 0.2159 0.4964 -0.0388 -0.0353 0.0220  454 TYR A N   
3628  C CA  . TYR A 454 ? 0.3641 0.2198 0.4995 -0.0409 -0.0380 0.0260  454 TYR A CA  
3629  C C   . TYR A 454 ? 0.3545 0.2145 0.4922 -0.0350 -0.0387 0.0237  454 TYR A C   
3630  O O   . TYR A 454 ? 0.3276 0.1823 0.4671 -0.0304 -0.0447 0.0226  454 TYR A O   
3631  C CB  . TYR A 454 ? 0.3816 0.2222 0.5121 -0.0426 -0.0456 0.0286  454 TYR A CB  
3632  C CG  . TYR A 454 ? 0.4016 0.2316 0.5202 -0.0471 -0.0484 0.0342  454 TYR A CG  
3633  C CD1 . TYR A 454 ? 0.4136 0.2419 0.5245 -0.0551 -0.0441 0.0387  454 TYR A CD1 
3634  C CD2 . TYR A 454 ? 0.3966 0.2185 0.5115 -0.0434 -0.0551 0.0351  454 TYR A CD2 
3635  C CE1 . TYR A 454 ? 0.4356 0.2536 0.5336 -0.0595 -0.0461 0.0440  454 TYR A CE1 
3636  C CE2 . TYR A 454 ? 0.4094 0.2206 0.5118 -0.0477 -0.0582 0.0404  454 TYR A CE2 
3637  C CZ  . TYR A 454 ? 0.4183 0.2271 0.5113 -0.0559 -0.0536 0.0450  454 TYR A CZ  
3638  O OH  . TYR A 454 ? 0.4056 0.2032 0.4843 -0.0608 -0.0559 0.0506  454 TYR A OH  
3639  N N   . ASN A 455 ? 0.3505 0.2204 0.4889 -0.0351 -0.0327 0.0229  455 ASN A N   
3640  C CA  . ASN A 455 ? 0.3230 0.1988 0.4657 -0.0297 -0.0328 0.0202  455 ASN A CA  
3641  C C   . ASN A 455 ? 0.3436 0.2120 0.4782 -0.0308 -0.0369 0.0231  455 ASN A C   
3642  O O   . ASN A 455 ? 0.3687 0.2363 0.4950 -0.0351 -0.0339 0.0256  455 ASN A O   
3643  C CB  . ASN A 455 ? 0.3086 0.1971 0.4564 -0.0289 -0.0255 0.0178  455 ASN A CB  
3644  C CG  . ASN A 455 ? 0.3024 0.1967 0.4557 -0.0236 -0.0257 0.0150  455 ASN A CG  
3645  O OD1 . ASN A 455 ? 0.2958 0.1852 0.4483 -0.0214 -0.0310 0.0155  455 ASN A OD1 
3646  N ND2 . ASN A 455 ? 0.2715 0.1760 0.4309 -0.0216 -0.0204 0.0124  455 ASN A ND2 
3647  N N   . THR A 456 ? 0.3518 0.2140 0.4883 -0.0268 -0.0441 0.0228  456 THR A N   
3648  C CA  . THR A 456 ? 0.3547 0.2075 0.4830 -0.0277 -0.0502 0.0259  456 THR A CA  
3649  C C   . THR A 456 ? 0.3422 0.2014 0.4729 -0.0250 -0.0500 0.0243  456 THR A C   
3650  O O   . THR A 456 ? 0.3279 0.1804 0.4520 -0.0257 -0.0552 0.0265  456 THR A O   
3651  C CB  . THR A 456 ? 0.3643 0.2073 0.4948 -0.0245 -0.0587 0.0263  456 THR A CB  
3652  O OG1 . THR A 456 ? 0.3524 0.2026 0.4959 -0.0180 -0.0585 0.0214  456 THR A OG1 
3653  C CG2 . THR A 456 ? 0.3787 0.2112 0.5025 -0.0290 -0.0604 0.0294  456 THR A CG2 
3654  N N   . HIS A 457 ? 0.3506 0.2222 0.4906 -0.0222 -0.0443 0.0205  457 HIS A N   
3655  C CA  . HIS A 457 ? 0.3510 0.2293 0.4927 -0.0210 -0.0424 0.0192  457 HIS A CA  
3656  C C   . HIS A 457 ? 0.3530 0.2303 0.5005 -0.0167 -0.0494 0.0183  457 HIS A C   
3657  O O   . HIS A 457 ? 0.3498 0.2267 0.4939 -0.0175 -0.0513 0.0189  457 HIS A O   
3658  C CB  . HIS A 457 ? 0.3769 0.2514 0.5056 -0.0265 -0.0400 0.0219  457 HIS A CB  
3659  C CG  . HIS A 457 ? 0.3666 0.2464 0.4928 -0.0300 -0.0315 0.0218  457 HIS A CG  
3660  N ND1 . HIS A 457 ? 0.3671 0.2534 0.4922 -0.0306 -0.0260 0.0203  457 HIS A ND1 
3661  C CD2 . HIS A 457 ? 0.3516 0.2307 0.4757 -0.0333 -0.0279 0.0231  457 HIS A CD2 
3662  C CE1 . HIS A 457 ? 0.3538 0.2438 0.4772 -0.0337 -0.0191 0.0205  457 HIS A CE1 
3663  N NE2 . HIS A 457 ? 0.3427 0.2290 0.4660 -0.0355 -0.0202 0.0223  457 HIS A NE2 
3664  N N   . LEU A 458 ? 0.3686 0.2457 0.5252 -0.0119 -0.0532 0.0166  458 LEU A N   
3665  C CA  . LEU A 458 ? 0.3657 0.2430 0.5304 -0.0072 -0.0597 0.0155  458 LEU A CA  
3666  C C   . LEU A 458 ? 0.3546 0.2454 0.5319 -0.0036 -0.0549 0.0117  458 LEU A C   
3667  O O   . LEU A 458 ? 0.3606 0.2577 0.5470 0.0001  -0.0516 0.0087  458 LEU A O   
3668  C CB  . LEU A 458 ? 0.3925 0.2634 0.5617 -0.0034 -0.0658 0.0152  458 LEU A CB  
3669  C CG  . LEU A 458 ? 0.4100 0.2660 0.5671 -0.0070 -0.0713 0.0193  458 LEU A CG  
3670  C CD1 . LEU A 458 ? 0.4064 0.2557 0.5696 -0.0019 -0.0784 0.0185  458 LEU A CD1 
3671  C CD2 . LEU A 458 ? 0.4272 0.2747 0.5717 -0.0113 -0.0758 0.0236  458 LEU A CD2 
3672  N N   . GLY A 459 ? 0.3595 0.2543 0.5365 -0.0050 -0.0544 0.0119  459 GLY A N   
3673  C CA  . GLY A 459 ? 0.3412 0.2481 0.5285 -0.0029 -0.0491 0.0090  459 GLY A CA  
3674  C C   . GLY A 459 ? 0.3449 0.2572 0.5313 -0.0039 -0.0405 0.0077  459 GLY A C   
3675  O O   . GLY A 459 ? 0.3498 0.2586 0.5261 -0.0081 -0.0374 0.0093  459 GLY A O   
3676  N N   . TRP A 460 ? 0.3516 0.2724 0.5488 0.0001  -0.0367 0.0047  460 TRP A N   
3677  C CA  . TRP A 460 ? 0.3351 0.2611 0.5321 -0.0002 -0.0294 0.0033  460 TRP A CA  
3678  C C   . TRP A 460 ? 0.3147 0.2361 0.5095 0.0006  -0.0298 0.0029  460 TRP A C   
3679  O O   . TRP A 460 ? 0.2989 0.2232 0.4924 -0.0001 -0.0249 0.0020  460 TRP A O   
3680  C CB  . TRP A 460 ? 0.3155 0.2521 0.5232 0.0032  -0.0249 0.0007  460 TRP A CB  
3681  C CG  . TRP A 460 ? 0.3461 0.2872 0.5554 0.0015  -0.0234 0.0012  460 TRP A CG  
3682  C CD1 . TRP A 460 ? 0.3450 0.2903 0.5630 0.0031  -0.0259 0.0006  460 TRP A CD1 
3683  C CD2 . TRP A 460 ? 0.3489 0.2905 0.5514 -0.0023 -0.0194 0.0021  460 TRP A CD2 
3684  N NE1 . TRP A 460 ? 0.3543 0.3021 0.5709 0.0004  -0.0239 0.0012  460 TRP A NE1 
3685  C CE2 . TRP A 460 ? 0.3562 0.3015 0.5630 -0.0027 -0.0198 0.0020  460 TRP A CE2 
3686  C CE3 . TRP A 460 ? 0.3159 0.2557 0.5102 -0.0052 -0.0155 0.0029  460 TRP A CE3 
3687  C CZ2 . TRP A 460 ? 0.3429 0.2887 0.5449 -0.0057 -0.0167 0.0024  460 TRP A CZ2 
3688  C CZ3 . TRP A 460 ? 0.3429 0.2842 0.5333 -0.0077 -0.0120 0.0033  460 TRP A CZ3 
3689  C CH2 . TRP A 460 ? 0.3374 0.2811 0.5310 -0.0079 -0.0126 0.0029  460 TRP A CH2 
3690  N N   . ALA A 461 ? 0.3043 0.2180 0.4988 0.0022  -0.0362 0.0034  461 ALA A N   
3691  C CA  . ALA A 461 ? 0.3064 0.2151 0.5000 0.0035  -0.0372 0.0024  461 ALA A CA  
3692  C C   . ALA A 461 ? 0.3215 0.2249 0.5048 -0.0021 -0.0355 0.0048  461 ALA A C   
3693  O O   . ALA A 461 ? 0.3327 0.2312 0.5080 -0.0065 -0.0368 0.0081  461 ALA A O   
3694  C CB  . ALA A 461 ? 0.3034 0.2045 0.4995 0.0067  -0.0448 0.0024  461 ALA A CB  
3695  N N   . ILE A 462 ? 0.3573 0.2613 0.5409 -0.0019 -0.0329 0.0032  462 ILE A N   
3696  C CA  . ILE A 462 ? 0.3593 0.2611 0.5362 -0.0071 -0.0304 0.0050  462 ILE A CA  
3697  C C   . ILE A 462 ? 0.3459 0.2357 0.5158 -0.0105 -0.0356 0.0080  462 ILE A C   
3698  O O   . ILE A 462 ? 0.3611 0.2487 0.5249 -0.0160 -0.0338 0.0106  462 ILE A O   
3699  C CB  . ILE A 462 ? 0.3731 0.2805 0.5538 -0.0053 -0.0265 0.0020  462 ILE A CB  
3700  C CG1 . ILE A 462 ? 0.4034 0.3217 0.5889 -0.0033 -0.0209 0.0002  462 ILE A CG1 
3701  C CG2 . ILE A 462 ? 0.4313 0.3366 0.6074 -0.0104 -0.0250 0.0035  462 ILE A CG2 
3702  C CD1 . ILE A 462 ? 0.3882 0.3101 0.5704 -0.0072 -0.0174 0.0026  462 ILE A CD1 
3703  N N   . GLY A 463 ? 0.3571 0.2393 0.5284 -0.0073 -0.0419 0.0075  463 GLY A N   
3704  C CA  . GLY A 463 ? 0.3419 0.2113 0.5069 -0.0101 -0.0475 0.0101  463 GLY A CA  
3705  C C   . GLY A 463 ? 0.3553 0.2226 0.5217 -0.0099 -0.0471 0.0079  463 GLY A C   
3706  O O   . GLY A 463 ? 0.3775 0.2531 0.5492 -0.0072 -0.0429 0.0043  463 GLY A O   
3707  N N   . SER A 464 ? 0.3872 0.2430 0.5480 -0.0134 -0.0516 0.0104  464 SER A N   
3708  C CA  . SER A 464 ? 0.3973 0.2487 0.5582 -0.0145 -0.0525 0.0088  464 SER A CA  
3709  C C   . SER A 464 ? 0.3978 0.2570 0.5587 -0.0192 -0.0465 0.0090  464 SER A C   
3710  O O   . SER A 464 ? 0.3917 0.2543 0.5490 -0.0245 -0.0428 0.0124  464 SER A O   
3711  C CB  . SER A 464 ? 0.4199 0.2562 0.5742 -0.0183 -0.0590 0.0125  464 SER A CB  
3712  O OG  . SER A 464 ? 0.4770 0.3052 0.6318 -0.0135 -0.0656 0.0123  464 SER A OG  
3713  N N   . GLN A 465 ? 0.4084 0.2690 0.5727 -0.0173 -0.0461 0.0052  465 GLN A N   
3714  C CA  . GLN A 465 ? 0.4073 0.2729 0.5722 -0.0217 -0.0427 0.0052  465 GLN A CA  
3715  C C   . GLN A 465 ? 0.4201 0.2760 0.5840 -0.0231 -0.0476 0.0039  465 GLN A C   
3716  O O   . GLN A 465 ? 0.4047 0.2507 0.5676 -0.0196 -0.0531 0.0022  465 GLN A O   
3717  C CB  . GLN A 465 ? 0.3831 0.2607 0.5531 -0.0176 -0.0377 0.0013  465 GLN A CB  
3718  C CG  . GLN A 465 ? 0.4306 0.3173 0.6025 -0.0154 -0.0333 0.0017  465 GLN A CG  
3719  C CD  . GLN A 465 ? 0.4175 0.3156 0.5937 -0.0126 -0.0280 -0.0012 465 GLN A CD  
3720  O OE1 . GLN A 465 ? 0.4475 0.3494 0.6267 -0.0070 -0.0269 -0.0042 465 GLN A OE1 
3721  N NE2 . GLN A 465 ? 0.3738 0.2773 0.5504 -0.0166 -0.0249 -0.0002 465 GLN A NE2 
3722  N N   . ALA A 466 ? 0.3968 0.2556 0.5615 -0.0282 -0.0460 0.0045  466 ALA A N   
3723  C CA  . ALA A 466 ? 0.4129 0.2630 0.5772 -0.0297 -0.0509 0.0028  466 ALA A CA  
3724  C C   . ALA A 466 ? 0.3931 0.2519 0.5611 -0.0328 -0.0480 0.0017  466 ALA A C   
3725  O O   . ALA A 466 ? 0.3806 0.2489 0.5506 -0.0364 -0.0428 0.0044  466 ALA A O   
3726  C CB  . ALA A 466 ? 0.4118 0.2489 0.5713 -0.0356 -0.0556 0.0074  466 ALA A CB  
3727  N N   . SER A 467 ? 0.4006 0.2561 0.5692 -0.0306 -0.0513 -0.0027 467 SER A N   
3728  C CA  . SER A 467 ? 0.4242 0.2852 0.5961 -0.0340 -0.0509 -0.0039 467 SER A CA  
3729  C C   . SER A 467 ? 0.4268 0.2765 0.5975 -0.0399 -0.0569 -0.0026 467 SER A C   
3730  O O   . SER A 467 ? 0.4721 0.3101 0.6393 -0.0370 -0.0623 -0.0054 467 SER A O   
3731  C CB  . SER A 467 ? 0.4264 0.2902 0.5983 -0.0278 -0.0512 -0.0097 467 SER A CB  
3732  O OG  . SER A 467 ? 0.4578 0.3341 0.6319 -0.0243 -0.0452 -0.0103 467 SER A OG  
3733  N N   . VAL A 468 ? 0.4557 0.3097 0.6303 -0.0477 -0.0558 0.0009  468 VAL A N   
3734  C CA  . VAL A 468 ? 0.4503 0.2944 0.6249 -0.0545 -0.0613 0.0026  468 VAL A CA  
3735  C C   . VAL A 468 ? 0.4854 0.3366 0.6661 -0.0576 -0.0621 0.0007  468 VAL A C   
3736  O O   . VAL A 468 ? 0.4676 0.3323 0.6545 -0.0604 -0.0569 0.0027  468 VAL A O   
3737  C CB  . VAL A 468 ? 0.4299 0.2712 0.6039 -0.0625 -0.0597 0.0095  468 VAL A CB  
3738  C CG1 . VAL A 468 ? 0.4509 0.2798 0.6245 -0.0696 -0.0660 0.0114  468 VAL A CG1 
3739  C CG2 . VAL A 468 ? 0.4211 0.2569 0.5887 -0.0594 -0.0587 0.0118  468 VAL A CG2 
3740  N N   . SER A 469 ? 0.5312 0.3727 0.7102 -0.0571 -0.0691 -0.0033 469 SER A N   
3741  C CA  . SER A 469 ? 0.5475 0.3925 0.7318 -0.0613 -0.0722 -0.0049 469 SER A CA  
3742  C C   . SER A 469 ? 0.5345 0.3804 0.7249 -0.0719 -0.0724 0.0009  469 SER A C   
3743  O O   . SER A 469 ? 0.5141 0.3486 0.7013 -0.0762 -0.0748 0.0043  469 SER A O   
3744  C CB  . SER A 469 ? 0.5590 0.3913 0.7384 -0.0586 -0.0803 -0.0106 469 SER A CB  
3745  O OG  . SER A 469 ? 0.5447 0.3820 0.7290 -0.0618 -0.0835 -0.0126 469 SER A OG  
3746  N N   . ILE A 470 ? 0.5583 0.4175 0.7579 -0.0760 -0.0700 0.0020  470 ILE A N   
3747  C CA  . ILE A 470 ? 0.5754 0.4373 0.7830 -0.0864 -0.0700 0.0068  470 ILE A CA  
3748  C C   . ILE A 470 ? 0.5654 0.4282 0.7798 -0.0899 -0.0765 0.0040  470 ILE A C   
3749  O O   . ILE A 470 ? 0.6027 0.4718 0.8269 -0.0982 -0.0761 0.0076  470 ILE A O   
3750  C CB  . ILE A 470 ? 0.5390 0.4170 0.7537 -0.0891 -0.0608 0.0113  470 ILE A CB  
3751  C CG1 . ILE A 470 ? 0.5426 0.4352 0.7618 -0.0831 -0.0573 0.0080  470 ILE A CG1 
3752  C CG2 . ILE A 470 ? 0.5234 0.3976 0.7306 -0.0882 -0.0556 0.0150  470 ILE A CG2 
3753  C CD1 . ILE A 470 ? 0.5304 0.4395 0.7598 -0.0869 -0.0497 0.0116  470 ILE A CD1 
3754  N N   . SER A 471 ? 0.6008 0.4573 0.8101 -0.0840 -0.0825 -0.0022 471 SER A N   
3755  C CA  . SER A 471 ? 0.6192 0.4741 0.8327 -0.0871 -0.0902 -0.0055 471 SER A CA  
3756  C C   . SER A 471 ? 0.5992 0.4463 0.8180 -0.0975 -0.0953 -0.0020 471 SER A C   
3757  O O   . SER A 471 ? 0.6476 0.5030 0.8776 -0.1042 -0.0972 -0.0007 471 SER A O   
3758  C CB  . SER A 471 ? 0.6363 0.4797 0.8392 -0.0795 -0.0963 -0.0126 471 SER A CB  
3759  O OG  . SER A 471 ? 0.6810 0.5340 0.8810 -0.0711 -0.0919 -0.0156 471 SER A OG  
3760  N N   . ASP A 472 ? 0.5863 0.4177 0.7976 -0.0990 -0.0976 -0.0005 472 ASP A N   
3761  C CA  . ASP A 472 ? 0.6268 0.4469 0.8406 -0.1086 -0.1032 0.0028  472 ASP A CA  
3762  C C   . ASP A 472 ? 0.6311 0.4627 0.8563 -0.1189 -0.0973 0.0104  472 ASP A C   
3763  O O   . ASP A 472 ? 0.6392 0.4630 0.8676 -0.1282 -0.1008 0.0143  472 ASP A O   
3764  C CB  . ASP A 472 ? 0.6107 0.4106 0.8126 -0.1063 -0.1069 0.0027  472 ASP A CB  
3765  C CG  . ASP A 472 ? 0.6735 0.4734 0.8691 -0.1022 -0.1000 0.0061  472 ASP A CG  
3766  O OD1 . ASP A 472 ? 0.7234 0.5353 0.9184 -0.0951 -0.0935 0.0046  472 ASP A OD1 
3767  O OD2 . ASP A 472 ? 0.7093 0.4963 0.9000 -0.1058 -0.1015 0.0102  472 ASP A OD2 
3768  N N   . GLN A 473 ? 0.5953 0.4449 0.8265 -0.1175 -0.0882 0.0127  473 GLN A N   
3769  C CA  . GLN A 473 ? 0.5845 0.4445 0.8244 -0.1259 -0.0808 0.0198  473 GLN A CA  
3770  C C   . GLN A 473 ? 0.5744 0.4564 0.8282 -0.1265 -0.0753 0.0198  473 GLN A C   
3771  O O   . GLN A 473 ? 0.5267 0.4198 0.7883 -0.1322 -0.0675 0.0250  473 GLN A O   
3772  C CB  . GLN A 473 ? 0.5953 0.4548 0.8268 -0.1233 -0.0727 0.0236  473 GLN A CB  
3773  C CG  . GLN A 473 ? 0.5954 0.4351 0.8145 -0.1244 -0.0759 0.0262  473 GLN A CG  
3774  C CD  . GLN A 473 ? 0.5503 0.3915 0.7628 -0.1240 -0.0678 0.0311  473 GLN A CD  
3775  O OE1 . GLN A 473 ? 0.5521 0.3963 0.7669 -0.1322 -0.0626 0.0375  473 GLN A OE1 
3776  N NE2 . GLN A 473 ? 0.4966 0.3356 0.7004 -0.1143 -0.0667 0.0281  473 GLN A NE2 
3777  N N   . LEU A 474 ? 0.5830 0.4710 0.8396 -0.1206 -0.0791 0.0142  474 LEU A N   
3778  C CA  . LEU A 474 ? 0.6239 0.5320 0.8917 -0.1184 -0.0739 0.0137  474 LEU A CA  
3779  C C   . LEU A 474 ? 0.6386 0.5597 0.9243 -0.1283 -0.0723 0.0177  474 LEU A C   
3780  O O   . LEU A 474 ? 0.5726 0.5109 0.8683 -0.1282 -0.0645 0.0196  474 LEU A O   
3781  C CB  . LEU A 474 ? 0.6371 0.5472 0.9028 -0.1103 -0.0792 0.0072  474 LEU A CB  
3782  C CG  . LEU A 474 ? 0.6714 0.5776 0.9236 -0.0994 -0.0764 0.0038  474 LEU A CG  
3783  C CD1 . LEU A 474 ? 0.6779 0.5857 0.9275 -0.0924 -0.0816 -0.0021 474 LEU A CD1 
3784  C CD2 . LEU A 474 ? 0.6230 0.5412 0.8768 -0.0967 -0.0656 0.0070  474 LEU A CD2 
3785  N N   . ASP A 475 ? 0.6269 0.5396 0.9168 -0.1368 -0.0794 0.0188  475 ASP A N   
3786  C CA  . ASP A 475 ? 0.6878 0.6118 0.9958 -0.1470 -0.0792 0.0224  475 ASP A CA  
3787  C C   . ASP A 475 ? 0.6727 0.5996 0.9841 -0.1554 -0.0704 0.0297  475 ASP A C   
3788  O O   . ASP A 475 ? 0.7166 0.6539 1.0437 -0.1644 -0.0686 0.0333  475 ASP A O   
3789  C CB  . ASP A 475 ? 0.7533 0.6668 1.0648 -0.1531 -0.0912 0.0205  475 ASP A CB  
3790  C CG  . ASP A 475 ? 0.8005 0.7199 1.1185 -0.1494 -0.0995 0.0148  475 ASP A CG  
3791  O OD1 . ASP A 475 ? 0.6903 0.6219 1.0096 -0.1413 -0.0960 0.0121  475 ASP A OD1 
3792  O OD2 . ASP A 475 ? 0.7761 0.6874 1.0976 -0.1549 -0.1097 0.0131  475 ASP A OD2 
3793  N N   . LYS A 476 ? 0.6179 0.5355 0.9149 -0.1530 -0.0650 0.0322  476 LYS A N   
3794  C CA  . LYS A 476 ? 0.5995 0.5186 0.8972 -0.1608 -0.0564 0.0393  476 LYS A CA  
3795  C C   . LYS A 476 ? 0.5608 0.4993 0.8652 -0.1585 -0.0444 0.0409  476 LYS A C   
3796  O O   . LYS A 476 ? 0.5620 0.5074 0.8639 -0.1489 -0.0422 0.0369  476 LYS A O   
3797  C CB  . LYS A 476 ? 0.6222 0.5219 0.9007 -0.1594 -0.0567 0.0415  476 LYS A CB  
3798  C CG  . LYS A 476 ? 0.6874 0.5658 0.9585 -0.1627 -0.0676 0.0410  476 LYS A CG  
3799  C CD  . LYS A 476 ? 0.7328 0.5918 0.9848 -0.1578 -0.0696 0.0413  476 LYS A CD  
3800  C CE  . LYS A 476 ? 0.7520 0.6050 0.9966 -0.1638 -0.0633 0.0488  476 LYS A CE  
3801  N NZ  . LYS A 476 ? 0.7305 0.5740 0.9590 -0.1555 -0.0619 0.0482  476 LYS A NZ  
3802  N N   . LYS A 477 ? 0.5560 0.5027 0.8682 -0.1673 -0.0362 0.0469  477 LYS A N   
3803  C CA  . LYS A 477 ? 0.5183 0.4819 0.8356 -0.1658 -0.0239 0.0486  477 LYS A CA  
3804  C C   . LYS A 477 ? 0.4950 0.4500 0.7931 -0.1593 -0.0186 0.0492  477 LYS A C   
3805  O O   . LYS A 477 ? 0.4472 0.4122 0.7444 -0.1518 -0.0124 0.0469  477 LYS A O   
3806  C CB  . LYS A 477 ? 0.5263 0.4995 0.8568 -0.1779 -0.0171 0.0548  477 LYS A CB  
3807  C CG  . LYS A 477 ? 0.5537 0.5427 0.8884 -0.1783 -0.0029 0.0575  477 LYS A CG  
3808  C CD  . LYS A 477 ? 0.5474 0.5565 0.8953 -0.1707 0.0012  0.0530  477 LYS A CD  
3809  C CE  . LYS A 477 ? 0.5422 0.5643 0.8914 -0.1698 0.0152  0.0550  477 LYS A CE  
3810  N NZ  . LYS A 477 ? 0.5173 0.5541 0.8753 -0.1602 0.0169  0.0497  477 LYS A NZ  
3811  N N   . ILE A 478 ? 0.4891 0.4253 0.7723 -0.1624 -0.0216 0.0523  478 ILE A N   
3812  C CA  . ILE A 478 ? 0.4783 0.4047 0.7433 -0.1572 -0.0180 0.0534  478 ILE A CA  
3813  C C   . ILE A 478 ? 0.4587 0.3666 0.7108 -0.1509 -0.0283 0.0499  478 ILE A C   
3814  O O   . ILE A 478 ? 0.4855 0.3800 0.7356 -0.1553 -0.0363 0.0507  478 ILE A O   
3815  C CB  . ILE A 478 ? 0.4865 0.4075 0.7445 -0.1662 -0.0112 0.0609  478 ILE A CB  
3816  C CG1 . ILE A 478 ? 0.4914 0.4322 0.7635 -0.1724 0.0001  0.0639  478 ILE A CG1 
3817  C CG2 . ILE A 478 ? 0.4916 0.4019 0.7301 -0.1606 -0.0086 0.0619  478 ILE A CG2 
3818  C CD1 . ILE A 478 ? 0.5122 0.4490 0.7782 -0.1826 0.0077  0.0716  478 ILE A CD1 
3819  N N   . ILE A 479 ? 0.4471 0.3554 0.6917 -0.1403 -0.0280 0.0456  479 ILE A N   
3820  C CA  . ILE A 479 ? 0.4638 0.3570 0.6974 -0.1330 -0.0366 0.0415  479 ILE A CA  
3821  C C   . ILE A 479 ? 0.4575 0.3409 0.6755 -0.1293 -0.0339 0.0436  479 ILE A C   
3822  O O   . ILE A 479 ? 0.4425 0.3354 0.6588 -0.1259 -0.0260 0.0440  479 ILE A O   
3823  C CB  . ILE A 479 ? 0.4379 0.3399 0.6759 -0.1235 -0.0387 0.0347  479 ILE A CB  
3824  C CG1 . ILE A 479 ? 0.4306 0.3402 0.6828 -0.1268 -0.0435 0.0323  479 ILE A CG1 
3825  C CG2 . ILE A 479 ? 0.4534 0.3419 0.6788 -0.1147 -0.0447 0.0305  479 ILE A CG2 
3826  C CD1 . ILE A 479 ? 0.4090 0.3249 0.6639 -0.1180 -0.0470 0.0258  479 ILE A CD1 
3827  N N   . THR A 480 ? 0.4380 0.3023 0.6452 -0.1296 -0.0408 0.0447  480 THR A N   
3828  C CA  . THR A 480 ? 0.4418 0.2955 0.6346 -0.1269 -0.0396 0.0473  480 THR A CA  
3829  C C   . THR A 480 ? 0.4478 0.2898 0.6327 -0.1173 -0.0470 0.0423  480 THR A C   
3830  O O   . THR A 480 ? 0.4462 0.2840 0.6342 -0.1141 -0.0539 0.0376  480 THR A O   
3831  C CB  . THR A 480 ? 0.4770 0.3185 0.6632 -0.1367 -0.0397 0.0547  480 THR A CB  
3832  O OG1 . THR A 480 ? 0.5007 0.3266 0.6861 -0.1400 -0.0493 0.0547  480 THR A OG1 
3833  C CG2 . THR A 480 ? 0.4752 0.3295 0.6695 -0.1463 -0.0310 0.0596  480 THR A CG2 
3834  N N   . SER A 481 ? 0.4544 0.2916 0.6289 -0.1124 -0.0454 0.0433  481 SER A N   
3835  C CA  . SER A 481 ? 0.4377 0.2630 0.6047 -0.1040 -0.0521 0.0396  481 SER A CA  
3836  C C   . SER A 481 ? 0.4425 0.2595 0.5979 -0.1035 -0.0508 0.0439  481 SER A C   
3837  O O   . SER A 481 ? 0.4554 0.2799 0.6087 -0.1069 -0.0435 0.0477  481 SER A O   
3838  C CB  . SER A 481 ? 0.4270 0.2625 0.5982 -0.0944 -0.0511 0.0329  481 SER A CB  
3839  O OG  . SER A 481 ? 0.4409 0.2670 0.6052 -0.0860 -0.0557 0.0298  481 SER A OG  
3840  N N   . GLU A 482 ? 0.4545 0.2556 0.6022 -0.0995 -0.0583 0.0433  482 GLU A N   
3841  C CA  . GLU A 482 ? 0.4547 0.2467 0.5913 -0.0980 -0.0590 0.0470  482 GLU A CA  
3842  C C   . GLU A 482 ? 0.4390 0.2261 0.5738 -0.0870 -0.0643 0.0417  482 GLU A C   
3843  O O   . GLU A 482 ? 0.4469 0.2240 0.5827 -0.0837 -0.0715 0.0384  482 GLU A O   
3844  C CB  . GLU A 482 ? 0.4486 0.2247 0.5783 -0.1071 -0.0629 0.0537  482 GLU A CB  
3845  C CG  . GLU A 482 ? 0.4622 0.2264 0.5786 -0.1072 -0.0645 0.0589  482 GLU A CG  
3846  C CD  . GLU A 482 ? 0.4847 0.2301 0.5924 -0.1152 -0.0698 0.0657  482 GLU A CD  
3847  O OE1 . GLU A 482 ? 0.5173 0.2518 0.6278 -0.1165 -0.0769 0.0646  482 GLU A OE1 
3848  O OE2 . GLU A 482 ? 0.4772 0.2176 0.5743 -0.1200 -0.0672 0.0721  482 GLU A OE2 
3849  N N   . ASN A 483 ? 0.4021 0.1958 0.5344 -0.0813 -0.0609 0.0408  483 ASN A N   
3850  C CA  . ASN A 483 ? 0.4233 0.2148 0.5560 -0.0711 -0.0650 0.0357  483 ASN A CA  
3851  C C   . ASN A 483 ? 0.4246 0.2094 0.5487 -0.0691 -0.0666 0.0391  483 ASN A C   
3852  O O   . ASN A 483 ? 0.4459 0.2350 0.5650 -0.0732 -0.0615 0.0433  483 ASN A O   
3853  C CB  . ASN A 483 ? 0.4496 0.2577 0.5907 -0.0648 -0.0600 0.0297  483 ASN A CB  
3854  C CG  . ASN A 483 ? 0.4793 0.2925 0.6279 -0.0666 -0.0598 0.0264  483 ASN A CG  
3855  O OD1 . ASN A 483 ? 0.4882 0.2964 0.6389 -0.0618 -0.0648 0.0216  483 ASN A OD1 
3856  N ND2 . ASN A 483 ? 0.4791 0.3013 0.6317 -0.0737 -0.0547 0.0289  483 ASN A ND2 
3857  N N   . PHE A 484 ? 0.4328 0.2063 0.5548 -0.0627 -0.0741 0.0373  484 PHE A N   
3858  C CA  . PHE A 484 ? 0.4305 0.1950 0.5444 -0.0610 -0.0780 0.0409  484 PHE A CA  
3859  C C   . PHE A 484 ? 0.4260 0.1979 0.5445 -0.0510 -0.0783 0.0360  484 PHE A C   
3860  O O   . PHE A 484 ? 0.4367 0.2141 0.5634 -0.0443 -0.0785 0.0297  484 PHE A O   
3861  C CB  . PHE A 484 ? 0.4380 0.1820 0.5463 -0.0624 -0.0875 0.0437  484 PHE A CB  
3862  C CG  . PHE A 484 ? 0.4459 0.1808 0.5492 -0.0731 -0.0878 0.0493  484 PHE A CG  
3863  C CD1 . PHE A 484 ? 0.4540 0.1821 0.5463 -0.0809 -0.0867 0.0572  484 PHE A CD1 
3864  C CD2 . PHE A 484 ? 0.4517 0.1846 0.5607 -0.0756 -0.0893 0.0470  484 PHE A CD2 
3865  C CE1 . PHE A 484 ? 0.4642 0.1851 0.5526 -0.0913 -0.0860 0.0627  484 PHE A CE1 
3866  C CE2 . PHE A 484 ? 0.4626 0.1875 0.5682 -0.0860 -0.0897 0.0524  484 PHE A CE2 
3867  C CZ  . PHE A 484 ? 0.4736 0.1926 0.5692 -0.0939 -0.0879 0.0604  484 PHE A CZ  
3868  N N   . PHE A 485 ? 0.4271 0.1990 0.5400 -0.0503 -0.0781 0.0389  485 PHE A N   
3869  C CA  . PHE A 485 ? 0.4073 0.1867 0.5249 -0.0421 -0.0783 0.0351  485 PHE A CA  
3870  C C   . PHE A 485 ? 0.4203 0.1888 0.5303 -0.0409 -0.0849 0.0390  485 PHE A C   
3871  O O   . PHE A 485 ? 0.4314 0.1930 0.5302 -0.0477 -0.0850 0.0452  485 PHE A O   
3872  C CB  . PHE A 485 ? 0.4099 0.2062 0.5300 -0.0432 -0.0691 0.0340  485 PHE A CB  
3873  C CG  . PHE A 485 ? 0.4009 0.2082 0.5287 -0.0440 -0.0632 0.0304  485 PHE A CG  
3874  C CD1 . PHE A 485 ? 0.4041 0.2183 0.5411 -0.0369 -0.0629 0.0241  485 PHE A CD1 
3875  C CD2 . PHE A 485 ? 0.4173 0.2275 0.5430 -0.0520 -0.0582 0.0334  485 PHE A CD2 
3876  C CE1 . PHE A 485 ? 0.4085 0.2316 0.5513 -0.0378 -0.0584 0.0210  485 PHE A CE1 
3877  C CE2 . PHE A 485 ? 0.4146 0.2348 0.5480 -0.0526 -0.0538 0.0301  485 PHE A CE2 
3878  C CZ  . PHE A 485 ? 0.4024 0.2284 0.5437 -0.0455 -0.0544 0.0240  485 PHE A CZ  
3879  N N   . ASN A 486 ? 0.4069 0.1738 0.5230 -0.0322 -0.0906 0.0354  486 ASN A N   
3880  C CA  . ASN A 486 ? 0.4187 0.1768 0.5297 -0.0301 -0.0977 0.0386  486 ASN A CA  
3881  C C   . ASN A 486 ? 0.4162 0.1855 0.5253 -0.0307 -0.0928 0.0392  486 ASN A C   
3882  O O   . ASN A 486 ? 0.4088 0.1932 0.5261 -0.0281 -0.0860 0.0349  486 ASN A O   
3883  C CB  . ASN A 486 ? 0.4181 0.1715 0.5376 -0.0207 -0.1054 0.0345  486 ASN A CB  
3884  C CG  . ASN A 486 ? 0.4187 0.1567 0.5368 -0.0207 -0.1118 0.0349  486 ASN A CG  
3885  O OD1 . ASN A 486 ? 0.4056 0.1458 0.5319 -0.0163 -0.1111 0.0294  486 ASN A OD1 
3886  N ND2 . ASN A 486 ? 0.4475 0.1690 0.5542 -0.0262 -0.1179 0.0413  486 ASN A ND2 
3887  N N   . ILE A 487 ? 0.4433 0.2045 0.5406 -0.0347 -0.0959 0.0448  487 ILE A N   
3888  C CA  . ILE A 487 ? 0.4442 0.2144 0.5383 -0.0355 -0.0919 0.0453  487 ILE A CA  
3889  C C   . ILE A 487 ? 0.4354 0.2052 0.5347 -0.0282 -0.0992 0.0436  487 ILE A C   
3890  O O   . ILE A 487 ? 0.4539 0.2100 0.5478 -0.0273 -0.1086 0.0469  487 ILE A O   
3891  C CB  . ILE A 487 ? 0.4610 0.2238 0.5380 -0.0444 -0.0899 0.0519  487 ILE A CB  
3892  C CG1 . ILE A 487 ? 0.4601 0.2232 0.5332 -0.0520 -0.0829 0.0541  487 ILE A CG1 
3893  C CG2 . ILE A 487 ? 0.4580 0.2298 0.5312 -0.0448 -0.0855 0.0515  487 ILE A CG2 
3894  C CD1 . ILE A 487 ? 0.4736 0.2269 0.5294 -0.0608 -0.0816 0.0612  487 ILE A CD1 
3895  N N   . PRO A 488 ? 0.4344 0.2187 0.5447 -0.0229 -0.0957 0.0386  488 PRO A N   
3896  C CA  . PRO A 488 ? 0.4353 0.2207 0.5516 -0.0168 -0.1025 0.0373  488 PRO A CA  
3897  C C   . PRO A 488 ? 0.4579 0.2358 0.5603 -0.0211 -0.1066 0.0424  488 PRO A C   
3898  O O   . PRO A 488 ? 0.4456 0.2248 0.5372 -0.0274 -0.1007 0.0448  488 PRO A O   
3899  C CB  . PRO A 488 ? 0.4172 0.2207 0.5473 -0.0121 -0.0958 0.0315  488 PRO A CB  
3900  C CG  . PRO A 488 ? 0.4225 0.2331 0.5544 -0.0146 -0.0866 0.0293  488 PRO A CG  
3901  C CD  . PRO A 488 ? 0.4262 0.2265 0.5440 -0.0229 -0.0855 0.0345  488 PRO A CD  
3902  N N   . ASP A 489 ? 0.4961 0.2651 0.5982 -0.0175 -0.1172 0.0441  489 ASP A N   
3903  C CA  . ASP A 489 ? 0.5258 0.2862 0.6144 -0.0208 -0.1231 0.0488  489 ASP A CA  
3904  C C   . ASP A 489 ? 0.5143 0.2869 0.6032 -0.0217 -0.1178 0.0467  489 ASP A C   
3905  O O   . ASP A 489 ? 0.5135 0.2802 0.5872 -0.0267 -0.1187 0.0504  489 ASP A O   
3906  C CB  . ASP A 489 ? 0.5391 0.2907 0.6323 -0.0150 -0.1360 0.0496  489 ASP A CB  
3907  C CG  . ASP A 489 ? 0.5870 0.3222 0.6756 -0.0150 -0.1431 0.0529  489 ASP A CG  
3908  O OD1 . ASP A 489 ? 0.5837 0.3116 0.6610 -0.0215 -0.1388 0.0562  489 ASP A OD1 
3909  O OD2 . ASP A 489 ? 0.6155 0.3451 0.7121 -0.0085 -0.1530 0.0523  489 ASP A OD2 
3910  N N   . ASN A 490 ? 0.4761 0.2649 0.5818 -0.0167 -0.1125 0.0409  490 ASN A N   
3911  C CA  . ASN A 490 ? 0.4547 0.2549 0.5626 -0.0170 -0.1081 0.0386  490 ASN A CA  
3912  C C   . ASN A 490 ? 0.4232 0.2331 0.5296 -0.0209 -0.0957 0.0369  490 ASN A C   
3913  O O   . ASN A 490 ? 0.3951 0.2167 0.5073 -0.0200 -0.0903 0.0337  490 ASN A O   
3914  C CB  . ASN A 490 ? 0.4364 0.2472 0.5631 -0.0096 -0.1115 0.0341  490 ASN A CB  
3915  C CG  . ASN A 490 ? 0.4203 0.2417 0.5634 -0.0045 -0.1061 0.0293  490 ASN A CG  
3916  O OD1 . ASN A 490 ? 0.4115 0.2286 0.5535 -0.0048 -0.1039 0.0293  490 ASN A OD1 
3917  N ND2 . ASN A 490 ? 0.4121 0.2468 0.5703 0.0001  -0.1041 0.0251  490 ASN A ND2 
3918  N N   . CYS A 491 ? 0.4401 0.2449 0.5392 -0.0252 -0.0914 0.0390  491 CYS A N   
3919  C CA  . CYS A 491 ? 0.4301 0.2422 0.5252 -0.0299 -0.0805 0.0385  491 CYS A CA  
3920  C C   . CYS A 491 ? 0.4420 0.2473 0.5192 -0.0361 -0.0797 0.0425  491 CYS A C   
3921  O O   . CYS A 491 ? 0.4492 0.2406 0.5125 -0.0402 -0.0842 0.0475  491 CYS A O   
3922  C CB  . CYS A 491 ? 0.4347 0.2447 0.5298 -0.0325 -0.0765 0.0393  491 CYS A CB  
3923  S SG  . CYS A 491 ? 0.4307 0.2512 0.5235 -0.0380 -0.0635 0.0385  491 CYS A SG  
3924  N N   . TRP A 492 ? 0.4135 0.2278 0.4902 -0.0367 -0.0738 0.0402  492 TRP A N   
3925  C CA  . TRP A 492 ? 0.4266 0.2352 0.4860 -0.0422 -0.0717 0.0429  492 TRP A CA  
3926  C C   . TRP A 492 ? 0.4410 0.2549 0.4961 -0.0470 -0.0603 0.0430  492 TRP A C   
3927  O O   . TRP A 492 ? 0.4793 0.2861 0.5184 -0.0529 -0.0574 0.0465  492 TRP A O   
3928  C CB  . TRP A 492 ? 0.4264 0.2399 0.4872 -0.0398 -0.0736 0.0402  492 TRP A CB  
3929  C CG  . TRP A 492 ? 0.4209 0.2341 0.4926 -0.0340 -0.0837 0.0389  492 TRP A CG  
3930  C CD1 . TRP A 492 ? 0.4202 0.2455 0.5084 -0.0289 -0.0834 0.0344  492 TRP A CD1 
3931  C CD2 . TRP A 492 ? 0.4449 0.2461 0.5130 -0.0327 -0.0953 0.0421  492 TRP A CD2 
3932  N NE1 . TRP A 492 ? 0.4268 0.2496 0.5231 -0.0245 -0.0935 0.0343  492 TRP A NE1 
3933  C CE2 . TRP A 492 ? 0.4470 0.2549 0.5314 -0.0264 -0.1013 0.0389  492 TRP A CE2 
3934  C CE3 . TRP A 492 ? 0.4867 0.2719 0.5399 -0.0361 -0.1013 0.0475  492 TRP A CE3 
3935  C CZ2 . TRP A 492 ? 0.4484 0.2484 0.5357 -0.0230 -0.1132 0.0406  492 TRP A CZ2 
3936  C CZ3 . TRP A 492 ? 0.4933 0.2695 0.5482 -0.0327 -0.1136 0.0494  492 TRP A CZ3 
3937  C CH2 . TRP A 492 ? 0.4776 0.2614 0.5496 -0.0261 -0.1196 0.0459  492 TRP A CH2 
3938  N N   . VAL A 493 ? 0.4127 0.2392 0.4823 -0.0445 -0.0539 0.0392  493 VAL A N   
3939  C CA  . VAL A 493 ? 0.4106 0.2436 0.4794 -0.0484 -0.0437 0.0390  493 VAL A CA  
3940  C C   . VAL A 493 ? 0.3866 0.2269 0.4701 -0.0458 -0.0417 0.0367  493 VAL A C   
3941  O O   . VAL A 493 ? 0.3635 0.2081 0.4589 -0.0401 -0.0453 0.0336  493 VAL A O   
3942  C CB  . VAL A 493 ? 0.4030 0.2455 0.4715 -0.0485 -0.0361 0.0360  493 VAL A CB  
3943  C CG1 . VAL A 493 ? 0.3789 0.2306 0.4607 -0.0423 -0.0377 0.0314  493 VAL A CG1 
3944  C CG2 . VAL A 493 ? 0.3909 0.2417 0.4619 -0.0515 -0.0258 0.0353  493 VAL A CG2 
3945  N N   . VAL A 494 ? 0.3878 0.2291 0.4699 -0.0503 -0.0359 0.0382  494 VAL A N   
3946  C CA  . VAL A 494 ? 0.3798 0.2281 0.4746 -0.0486 -0.0336 0.0359  494 VAL A CA  
3947  C C   . VAL A 494 ? 0.3585 0.2167 0.4557 -0.0519 -0.0239 0.0351  494 VAL A C   
3948  O O   . VAL A 494 ? 0.3692 0.2252 0.4570 -0.0575 -0.0194 0.0380  494 VAL A O   
3949  C CB  . VAL A 494 ? 0.3939 0.2316 0.4873 -0.0504 -0.0394 0.0388  494 VAL A CB  
3950  C CG1 . VAL A 494 ? 0.4035 0.2330 0.4847 -0.0584 -0.0371 0.0441  494 VAL A CG1 
3951  C CG2 . VAL A 494 ? 0.3927 0.2366 0.4990 -0.0477 -0.0384 0.0355  494 VAL A CG2 
3952  N N   . ASN A 495 ? 0.3629 0.2317 0.4729 -0.0482 -0.0210 0.0311  495 ASN A N   
3953  C CA  . ASN A 495 ? 0.3481 0.2264 0.4638 -0.0505 -0.0135 0.0301  495 ASN A CA  
3954  C C   . ASN A 495 ? 0.3504 0.2267 0.4721 -0.0514 -0.0162 0.0304  495 ASN A C   
3955  O O   . ASN A 495 ? 0.3436 0.2226 0.4740 -0.0466 -0.0191 0.0272  495 ASN A O   
3956  C CB  . ASN A 495 ? 0.3242 0.2150 0.4491 -0.0460 -0.0090 0.0257  495 ASN A CB  
3957  C CG  . ASN A 495 ? 0.3392 0.2394 0.4700 -0.0482 -0.0020 0.0249  495 ASN A CG  
3958  O OD1 . ASN A 495 ? 0.3640 0.2635 0.4980 -0.0511 -0.0024 0.0262  495 ASN A OD1 
3959  N ND2 . ASN A 495 ? 0.3106 0.2195 0.4436 -0.0470 0.0039  0.0229  495 ASN A ND2 
3960  N N   . ALA A 496 ? 0.3744 0.2458 0.4910 -0.0579 -0.0148 0.0342  496 ALA A N   
3961  C CA  . ALA A 496 ? 0.3708 0.2399 0.4927 -0.0601 -0.0170 0.0347  496 ALA A CA  
3962  C C   . ALA A 496 ? 0.3430 0.2242 0.4736 -0.0623 -0.0102 0.0333  496 ALA A C   
3963  O O   . ALA A 496 ? 0.3361 0.2214 0.4636 -0.0668 -0.0037 0.0353  496 ALA A O   
3964  C CB  . ALA A 496 ? 0.3983 0.2548 0.5103 -0.0665 -0.0199 0.0401  496 ALA A CB  
3965  N N   . SER A 497 ? 0.3187 0.2052 0.4597 -0.0589 -0.0117 0.0297  497 SER A N   
3966  C CA  . SER A 497 ? 0.3206 0.2188 0.4708 -0.0602 -0.0065 0.0281  497 SER A CA  
3967  C C   . SER A 497 ? 0.3229 0.2201 0.4803 -0.0604 -0.0106 0.0265  497 SER A C   
3968  O O   . SER A 497 ? 0.3126 0.2011 0.4689 -0.0579 -0.0173 0.0255  497 SER A O   
3969  C CB  . SER A 497 ? 0.3139 0.2231 0.4692 -0.0548 -0.0024 0.0244  497 SER A CB  
3970  O OG  . SER A 497 ? 0.3172 0.2273 0.4775 -0.0485 -0.0064 0.0206  497 SER A OG  
3971  N N   . ALA A 498 ? 0.3196 0.2260 0.4849 -0.0634 -0.0068 0.0262  498 ALA A N   
3972  C CA  . ALA A 498 ? 0.3352 0.2418 0.5078 -0.0638 -0.0108 0.0244  498 ALA A CA  
3973  C C   . ALA A 498 ? 0.3393 0.2599 0.5222 -0.0639 -0.0062 0.0225  498 ALA A C   
3974  O O   . ALA A 498 ? 0.3320 0.2608 0.5167 -0.0661 0.0005  0.0239  498 ALA A O   
3975  C CB  . ALA A 498 ? 0.3473 0.2443 0.5173 -0.0709 -0.0141 0.0281  498 ALA A CB  
3976  N N   . GLY A 499 ? 0.3314 0.2542 0.5207 -0.0614 -0.0100 0.0192  499 GLY A N   
3977  C CA  . GLY A 499 ? 0.3257 0.2612 0.5246 -0.0608 -0.0068 0.0174  499 GLY A CA  
3978  C C   . GLY A 499 ? 0.3129 0.2482 0.5169 -0.0591 -0.0125 0.0143  499 GLY A C   
3979  O O   . GLY A 499 ? 0.3172 0.2434 0.5165 -0.0562 -0.0179 0.0123  499 GLY A O   
3980  N N   . ILE A 500 ? 0.3188 0.2640 0.5325 -0.0610 -0.0113 0.0137  500 ILE A N   
3981  C CA  . ILE A 500 ? 0.3198 0.2653 0.5381 -0.0597 -0.0170 0.0107  500 ILE A CA  
3982  C C   . ILE A 500 ? 0.3192 0.2781 0.5463 -0.0572 -0.0142 0.0091  500 ILE A C   
3983  O O   . ILE A 500 ? 0.3310 0.2993 0.5635 -0.0589 -0.0082 0.0109  500 ILE A O   
3984  C CB  . ILE A 500 ? 0.3389 0.2791 0.5604 -0.0669 -0.0215 0.0124  500 ILE A CB  
3985  C CG1 . ILE A 500 ? 0.3504 0.2863 0.5730 -0.0652 -0.0292 0.0087  500 ILE A CG1 
3986  C CG2 . ILE A 500 ? 0.3479 0.2984 0.5798 -0.0738 -0.0170 0.0157  500 ILE A CG2 
3987  C CD1 . ILE A 500 ? 0.3550 0.2848 0.5809 -0.0726 -0.0343 0.0103  500 ILE A CD1 
3988  N N   . SER A 501 ? 0.3267 0.2857 0.5544 -0.0529 -0.0189 0.0056  501 SER A N   
3989  C CA  . SER A 501 ? 0.3258 0.2958 0.5613 -0.0505 -0.0182 0.0041  501 SER A CA  
3990  C C   . SER A 501 ? 0.3451 0.3211 0.5920 -0.0562 -0.0209 0.0050  501 SER A C   
3991  O O   . SER A 501 ? 0.3400 0.3091 0.5868 -0.0607 -0.0262 0.0052  501 SER A O   
3992  C CB  . SER A 501 ? 0.3108 0.2776 0.5407 -0.0438 -0.0219 0.0004  501 SER A CB  
3993  O OG  . SER A 501 ? 0.3243 0.2897 0.5474 -0.0389 -0.0178 0.0001  501 SER A OG  
3994  N N   . VAL A 502 ? 0.3261 0.3150 0.5834 -0.0559 -0.0174 0.0055  502 VAL A N   
3995  C CA  . VAL A 502 ? 0.3328 0.3308 0.6039 -0.0610 -0.0189 0.0065  502 VAL A CA  
3996  C C   . VAL A 502 ? 0.3545 0.3620 0.6331 -0.0563 -0.0207 0.0045  502 VAL A C   
3997  O O   . VAL A 502 ? 0.3428 0.3528 0.6178 -0.0502 -0.0174 0.0035  502 VAL A O   
3998  C CB  . VAL A 502 ? 0.3363 0.3418 0.6143 -0.0661 -0.0109 0.0101  502 VAL A CB  
3999  C CG1 . VAL A 502 ? 0.3380 0.3544 0.6326 -0.0720 -0.0116 0.0114  502 VAL A CG1 
4000  C CG2 . VAL A 502 ? 0.3343 0.3291 0.6023 -0.0700 -0.0090 0.0126  502 VAL A CG2 
4001  N N   . ARG A 503 ? 0.3762 0.3891 0.6657 -0.0596 -0.0261 0.0041  503 ARG A N   
4002  C CA  . ARG A 503 ? 0.3867 0.4076 0.6836 -0.0556 -0.0297 0.0024  503 ARG A CA  
4003  C C   . ARG A 503 ? 0.3751 0.4094 0.6911 -0.0607 -0.0297 0.0039  503 ARG A C   
4004  O O   . ARG A 503 ? 0.4073 0.4409 0.7292 -0.0677 -0.0323 0.0052  503 ARG A O   
4005  C CB  . ARG A 503 ? 0.4339 0.4456 0.7227 -0.0533 -0.0394 -0.0007 503 ARG A CB  
4006  C CG  . ARG A 503 ? 0.5207 0.5374 0.8120 -0.0481 -0.0439 -0.0026 503 ARG A CG  
4007  C CD  . ARG A 503 ? 0.5894 0.5979 0.8741 -0.0473 -0.0544 -0.0056 503 ARG A CD  
4008  N NE  . ARG A 503 ? 0.6947 0.6917 0.9614 -0.0416 -0.0548 -0.0080 503 ARG A NE  
4009  C CZ  . ARG A 503 ? 0.8106 0.8085 1.0707 -0.0353 -0.0504 -0.0081 503 ARG A CZ  
4010  N NH1 . ARG A 503 ? 0.8763 0.8845 1.1449 -0.0328 -0.0486 -0.0069 503 ARG A NH1 
4011  N NH2 . ARG A 503 ? 0.7489 0.7373 0.9945 -0.0315 -0.0482 -0.0095 503 ARG A NH2 
4012  N N   . TYR A 504 ? 0.3338 0.3800 0.6598 -0.0569 -0.0270 0.0038  504 TYR A N   
4013  C CA  . TYR A 504 ? 0.3126 0.3727 0.6583 -0.0598 -0.0287 0.0045  504 TYR A CA  
4014  C C   . TYR A 504 ? 0.3083 0.3724 0.6564 -0.0528 -0.0337 0.0025  504 TYR A C   
4015  O O   . TYR A 504 ? 0.3050 0.3725 0.6514 -0.0469 -0.0286 0.0023  504 TYR A O   
4016  C CB  . TYR A 504 ? 0.3200 0.3917 0.6769 -0.0623 -0.0182 0.0068  504 TYR A CB  
4017  C CG  . TYR A 504 ? 0.3257 0.4130 0.7054 -0.0664 -0.0188 0.0077  504 TYR A CG  
4018  C CD1 . TYR A 504 ? 0.3341 0.4328 0.7267 -0.0615 -0.0208 0.0065  504 TYR A CD1 
4019  C CD2 . TYR A 504 ? 0.3444 0.4348 0.7332 -0.0753 -0.0179 0.0100  504 TYR A CD2 
4020  C CE1 . TYR A 504 ? 0.3134 0.4271 0.7285 -0.0650 -0.0221 0.0071  504 TYR A CE1 
4021  C CE2 . TYR A 504 ? 0.3309 0.4364 0.7421 -0.0794 -0.0185 0.0109  504 TYR A CE2 
4022  C CZ  . TYR A 504 ? 0.3221 0.4399 0.7471 -0.0741 -0.0206 0.0093  504 TYR A CZ  
4023  O OH  . TYR A 504 ? 0.3512 0.4849 0.8000 -0.0779 -0.0216 0.0100  504 TYR A OH  
4024  N N   . GLY A 505 ? 0.2759 0.3389 0.6273 -0.0537 -0.0441 0.0010  505 GLY A N   
4025  C CA  . GLY A 505 ? 0.2736 0.3373 0.6235 -0.0473 -0.0505 -0.0007 505 GLY A CA  
4026  C C   . GLY A 505 ? 0.2805 0.3321 0.6097 -0.0410 -0.0490 -0.0020 505 GLY A C   
4027  O O   . GLY A 505 ? 0.2884 0.3277 0.6034 -0.0419 -0.0511 -0.0031 505 GLY A O   
4028  N N   . LYS A 506 ? 0.2839 0.3390 0.6119 -0.0347 -0.0449 -0.0018 506 LYS A N   
4029  C CA  . LYS A 506 ? 0.2755 0.3205 0.5855 -0.0291 -0.0431 -0.0026 506 LYS A CA  
4030  C C   . LYS A 506 ? 0.2832 0.3274 0.5887 -0.0285 -0.0326 -0.0015 506 LYS A C   
4031  O O   . LYS A 506 ? 0.3264 0.3631 0.6186 -0.0246 -0.0300 -0.0020 506 LYS A O   
4032  C CB  . LYS A 506 ? 0.2925 0.3403 0.6029 -0.0227 -0.0461 -0.0028 506 LYS A CB  
4033  C CG  . LYS A 506 ? 0.3105 0.3596 0.6252 -0.0223 -0.0571 -0.0037 506 LYS A CG  
4034  C CD  . LYS A 506 ? 0.3282 0.3773 0.6392 -0.0154 -0.0593 -0.0034 506 LYS A CD  
4035  C CE  . LYS A 506 ? 0.3360 0.3881 0.6534 -0.0142 -0.0700 -0.0037 506 LYS A CE  
4036  N NZ  . LYS A 506 ? 0.3463 0.3993 0.6619 -0.0076 -0.0708 -0.0026 506 LYS A NZ  
4037  N N   . PHE A 507 ? 0.3022 0.3545 0.6191 -0.0326 -0.0265 0.0000  507 PHE A N   
4038  C CA  . PHE A 507 ? 0.2963 0.3475 0.6087 -0.0330 -0.0170 0.0011  507 PHE A CA  
4039  C C   . PHE A 507 ? 0.3030 0.3435 0.6040 -0.0372 -0.0168 0.0014  507 PHE A C   
4040  O O   . PHE A 507 ? 0.2946 0.3355 0.6009 -0.0434 -0.0183 0.0023  507 PHE A O   
4041  C CB  . PHE A 507 ? 0.2715 0.3360 0.6006 -0.0359 -0.0110 0.0025  507 PHE A CB  
4042  C CG  . PHE A 507 ? 0.2570 0.3219 0.5823 -0.0359 -0.0007 0.0034  507 PHE A CG  
4043  C CD1 . PHE A 507 ? 0.2422 0.3027 0.5625 -0.0416 0.0033  0.0049  507 PHE A CD1 
4044  C CD2 . PHE A 507 ? 0.2476 0.3167 0.5742 -0.0304 0.0044  0.0028  507 PHE A CD2 
4045  C CE1 . PHE A 507 ? 0.2427 0.3031 0.5586 -0.0417 0.0122  0.0057  507 PHE A CE1 
4046  C CE2 . PHE A 507 ? 0.2416 0.3106 0.5643 -0.0305 0.0134  0.0033  507 PHE A CE2 
4047  C CZ  . PHE A 507 ? 0.2398 0.3045 0.5568 -0.0362 0.0172  0.0047  507 PHE A CZ  
4048  N N   . THR A 508 ? 0.3112 0.3423 0.5975 -0.0337 -0.0148 0.0008  508 THR A N   
4049  C CA  . THR A 508 ? 0.3282 0.3487 0.6033 -0.0362 -0.0143 0.0009  508 THR A CA  
4050  C C   . THR A 508 ? 0.3114 0.3312 0.5819 -0.0358 -0.0060 0.0023  508 THR A C   
4051  O O   . THR A 508 ? 0.2912 0.3136 0.5603 -0.0313 -0.0020 0.0020  508 THR A O   
4052  C CB  . THR A 508 ? 0.3445 0.3541 0.6063 -0.0324 -0.0193 -0.0013 508 THR A CB  
4053  O OG1 . THR A 508 ? 0.3911 0.4022 0.6488 -0.0265 -0.0160 -0.0016 508 THR A OG1 
4054  C CG2 . THR A 508 ? 0.3545 0.3624 0.6170 -0.0323 -0.0280 -0.0031 508 THR A CG2 
4055  N N   . PHE A 509 ? 0.3185 0.3335 0.5859 -0.0408 -0.0040 0.0038  509 PHE A N   
4056  C CA  . PHE A 509 ? 0.2991 0.3128 0.5616 -0.0413 0.0031  0.0053  509 PHE A CA  
4057  C C   . PHE A 509 ? 0.3246 0.3281 0.5788 -0.0455 0.0017  0.0065  509 PHE A C   
4058  O O   . PHE A 509 ? 0.3393 0.3370 0.5921 -0.0474 -0.0044 0.0060  509 PHE A O   
4059  C CB  . PHE A 509 ? 0.2997 0.3246 0.5731 -0.0437 0.0096  0.0067  509 PHE A CB  
4060  C CG  . PHE A 509 ? 0.2599 0.2902 0.5437 -0.0508 0.0096  0.0086  509 PHE A CG  
4061  C CD1 . PHE A 509 ? 0.2652 0.3011 0.5600 -0.0522 0.0039  0.0079  509 PHE A CD1 
4062  C CD2 . PHE A 509 ? 0.2566 0.2865 0.5391 -0.0562 0.0155  0.0111  509 PHE A CD2 
4063  C CE1 . PHE A 509 ? 0.2719 0.3133 0.5775 -0.0593 0.0040  0.0098  509 PHE A CE1 
4064  C CE2 . PHE A 509 ? 0.2764 0.3114 0.5687 -0.0633 0.0160  0.0132  509 PHE A CE2 
4065  C CZ  . PHE A 509 ? 0.2724 0.3134 0.5769 -0.0650 0.0103  0.0126  509 PHE A CZ  
4066  N N   . LYS A 510 ? 0.3588 0.3594 0.6070 -0.0467 0.0070  0.0082  510 LYS A N   
4067  C CA  . LYS A 510 ? 0.3531 0.3434 0.5932 -0.0506 0.0055  0.0099  510 LYS A CA  
4068  C C   . LYS A 510 ? 0.3288 0.3217 0.5707 -0.0567 0.0113  0.0131  510 LYS A C   
4069  O O   . LYS A 510 ? 0.3019 0.3028 0.5475 -0.0563 0.0179  0.0135  510 LYS A O   
4070  C CB  . LYS A 510 ? 0.3841 0.3655 0.6124 -0.0462 0.0050  0.0090  510 LYS A CB  
4071  C CG  . LYS A 510 ? 0.4462 0.4224 0.6707 -0.0414 -0.0008 0.0061  510 LYS A CG  
4072  C CD  . LYS A 510 ? 0.4928 0.4613 0.7076 -0.0375 -0.0008 0.0054  510 LYS A CD  
4073  C CE  . LYS A 510 ? 0.5423 0.5072 0.7537 -0.0323 -0.0050 0.0024  510 LYS A CE  
4074  N NZ  . LYS A 510 ? 0.5778 0.5359 0.7882 -0.0345 -0.0109 0.0015  510 LYS A NZ  
4075  N N   . ILE A 511 ? 0.2803 0.2658 0.5193 -0.0625 0.0087  0.0154  511 ILE A N   
4076  C CA  . ILE A 511 ? 0.2809 0.2654 0.5178 -0.0688 0.0138  0.0191  511 ILE A CA  
4077  C C   . ILE A 511 ? 0.2830 0.2531 0.5059 -0.0690 0.0110  0.0204  511 ILE A C   
4078  O O   . ILE A 511 ? 0.2785 0.2403 0.4973 -0.0665 0.0043  0.0188  511 ILE A O   
4079  C CB  . ILE A 511 ? 0.2989 0.2877 0.5461 -0.0763 0.0131  0.0213  511 ILE A CB  
4080  C CG1 . ILE A 511 ? 0.2979 0.2773 0.5440 -0.0785 0.0041  0.0209  511 ILE A CG1 
4081  C CG2 . ILE A 511 ? 0.2882 0.2926 0.5508 -0.0754 0.0159  0.0198  511 ILE A CG2 
4082  C CD1 . ILE A 511 ? 0.3210 0.3032 0.5767 -0.0868 0.0029  0.0235  511 ILE A CD1 
4083  N N   . HIS A 512 ? 0.2899 0.2572 0.5052 -0.0717 0.0162  0.0232  512 HIS A N   
4084  C CA  . HIS A 512 ? 0.3032 0.2586 0.5052 -0.0697 0.0140  0.0238  512 HIS A CA  
4085  C C   . HIS A 512 ? 0.3091 0.2621 0.5033 -0.0743 0.0199  0.0275  512 HIS A C   
4086  O O   . HIS A 512 ? 0.3054 0.2675 0.5046 -0.0774 0.0268  0.0285  512 HIS A O   
4087  C CB  . HIS A 512 ? 0.3008 0.2580 0.5008 -0.0615 0.0136  0.0202  512 HIS A CB  
4088  C CG  . HIS A 512 ? 0.3122 0.2812 0.5183 -0.0591 0.0201  0.0187  512 HIS A CG  
4089  N ND1 . HIS A 512 ? 0.3036 0.2755 0.5062 -0.0609 0.0271  0.0202  512 HIS A ND1 
4090  C CD2 . HIS A 512 ? 0.3204 0.2990 0.5361 -0.0554 0.0204  0.0161  512 HIS A CD2 
4091  C CE1 . HIS A 512 ? 0.3101 0.2927 0.5204 -0.0578 0.0316  0.0180  512 HIS A CE1 
4092  N NE2 . HIS A 512 ? 0.3148 0.3016 0.5333 -0.0544 0.0274  0.0157  512 HIS A NE2 
4093  N N   . ASP A 513 ? 0.3239 0.2645 0.5055 -0.0746 0.0169  0.0293  513 ASP A N   
4094  C CA  . ASP A 513 ? 0.3328 0.2686 0.5035 -0.0782 0.0215  0.0327  513 ASP A CA  
4095  C C   . ASP A 513 ? 0.3439 0.2688 0.5030 -0.0741 0.0167  0.0323  513 ASP A C   
4096  O O   . ASP A 513 ? 0.3335 0.2536 0.4936 -0.0697 0.0099  0.0303  513 ASP A O   
4097  C CB  . ASP A 513 ? 0.3593 0.2896 0.5273 -0.0869 0.0220  0.0376  513 ASP A CB  
4098  C CG  . ASP A 513 ? 0.3748 0.3032 0.5328 -0.0922 0.0290  0.0414  513 ASP A CG  
4099  O OD1 . ASP A 513 ? 0.3420 0.2750 0.4961 -0.0893 0.0345  0.0399  513 ASP A OD1 
4100  O OD2 . ASP A 513 ? 0.4275 0.3494 0.5814 -0.0996 0.0290  0.0460  513 ASP A OD2 
4101  N N   . GLN A 514 ? 0.3697 0.2907 0.5178 -0.0755 0.0202  0.0343  514 GLN A N   
4102  C CA  . GLN A 514 ? 0.3712 0.2851 0.5103 -0.0708 0.0167  0.0333  514 GLN A CA  
4103  C C   . GLN A 514 ? 0.3827 0.2869 0.5067 -0.0753 0.0179  0.0374  514 GLN A C   
4104  O O   . GLN A 514 ? 0.3756 0.2834 0.4959 -0.0796 0.0253  0.0390  514 GLN A O   
4105  C CB  . GLN A 514 ? 0.3458 0.2692 0.4892 -0.0650 0.0205  0.0291  514 GLN A CB  
4106  C CG  . GLN A 514 ? 0.3356 0.2531 0.4711 -0.0604 0.0171  0.0278  514 GLN A CG  
4107  C CD  . GLN A 514 ? 0.3123 0.2384 0.4516 -0.0556 0.0212  0.0241  514 GLN A CD  
4108  O OE1 . GLN A 514 ? 0.2936 0.2234 0.4397 -0.0503 0.0187  0.0211  514 GLN A OE1 
4109  N NE2 . GLN A 514 ? 0.3128 0.2416 0.4471 -0.0574 0.0278  0.0243  514 GLN A NE2 
4110  N N   . LYS A 515 ? 0.3903 0.2821 0.5055 -0.0740 0.0105  0.0388  515 LYS A N   
4111  C CA  . LYS A 515 ? 0.4044 0.2854 0.5037 -0.0773 0.0099  0.0425  515 LYS A CA  
4112  C C   . LYS A 515 ? 0.3863 0.2621 0.4807 -0.0713 0.0040  0.0405  515 LYS A C   
4113  O O   . LYS A 515 ? 0.3580 0.2316 0.4582 -0.0666 -0.0028 0.0386  515 LYS A O   
4114  C CB  . LYS A 515 ? 0.4227 0.2918 0.5154 -0.0835 0.0059  0.0478  515 LYS A CB  
4115  C CG  . LYS A 515 ? 0.4515 0.3257 0.5507 -0.0900 0.0109  0.0500  515 LYS A CG  
4116  C CD  . LYS A 515 ? 0.4602 0.3401 0.5546 -0.0957 0.0212  0.0522  515 LYS A CD  
4117  C CE  . LYS A 515 ? 0.4653 0.3528 0.5702 -0.1018 0.0260  0.0539  515 LYS A CE  
4118  N NZ  . LYS A 515 ? 0.4525 0.3508 0.5590 -0.1056 0.0373  0.0544  515 LYS A NZ  
4119  N N   . ILE A 516 ? 0.3911 0.2648 0.4746 -0.0719 0.0069  0.0409  516 ILE A N   
4120  C CA  . ILE A 516 ? 0.4010 0.2691 0.4785 -0.0675 0.0012  0.0396  516 ILE A CA  
4121  C C   . ILE A 516 ? 0.4082 0.2616 0.4686 -0.0719 -0.0029 0.0446  516 ILE A C   
4122  O O   . ILE A 516 ? 0.3878 0.2387 0.4374 -0.0775 0.0028  0.0475  516 ILE A O   
4123  C CB  . ILE A 516 ? 0.4262 0.3027 0.5045 -0.0644 0.0066  0.0358  516 ILE A CB  
4124  C CG1 . ILE A 516 ? 0.4155 0.3057 0.5107 -0.0602 0.0101  0.0315  516 ILE A CG1 
4125  C CG2 . ILE A 516 ? 0.4488 0.3190 0.5206 -0.0607 0.0004  0.0347  516 ILE A CG2 
4126  C CD1 . ILE A 516 ? 0.4123 0.3106 0.5097 -0.0568 0.0153  0.0276  516 ILE A CD1 
4127  N N   . ILE A 517 ? 0.4170 0.2605 0.4755 -0.0696 -0.0127 0.0459  517 ILE A N   
4128  C CA  . ILE A 517 ? 0.4314 0.2596 0.4744 -0.0740 -0.0178 0.0513  517 ILE A CA  
4129  C C   . ILE A 517 ? 0.4434 0.2638 0.4817 -0.0695 -0.0271 0.0508  517 ILE A C   
4130  O O   . ILE A 517 ? 0.4540 0.2769 0.5040 -0.0636 -0.0329 0.0479  517 ILE A O   
4131  C CB  . ILE A 517 ? 0.4250 0.2464 0.4705 -0.0773 -0.0214 0.0547  517 ILE A CB  
4132  C CG1 . ILE A 517 ? 0.4194 0.2489 0.4709 -0.0823 -0.0129 0.0554  517 ILE A CG1 
4133  C CG2 . ILE A 517 ? 0.4407 0.2448 0.4696 -0.0817 -0.0276 0.0608  517 ILE A CG2 
4134  C CD1 . ILE A 517 ? 0.4261 0.2509 0.4846 -0.0841 -0.0174 0.0571  517 ILE A CD1 
4135  N N   . TYR A 518 ? 0.4615 0.2720 0.4822 -0.0727 -0.0286 0.0539  518 TYR A N   
4136  C CA  . TYR A 518 ? 0.4759 0.2792 0.4907 -0.0691 -0.0374 0.0536  518 TYR A CA  
4137  C C   . TYR A 518 ? 0.5128 0.2997 0.5176 -0.0707 -0.0476 0.0588  518 TYR A C   
4138  O O   . TYR A 518 ? 0.4989 0.2767 0.4930 -0.0767 -0.0465 0.0639  518 TYR A O   
4139  C CB  . TYR A 518 ? 0.4822 0.2839 0.4821 -0.0713 -0.0334 0.0534  518 TYR A CB  
4140  C CG  . TYR A 518 ? 0.4658 0.2822 0.4741 -0.0693 -0.0239 0.0481  518 TYR A CG  
4141  C CD1 . TYR A 518 ? 0.4384 0.2621 0.4567 -0.0634 -0.0262 0.0432  518 TYR A CD1 
4142  C CD2 . TYR A 518 ? 0.4646 0.2874 0.4713 -0.0735 -0.0127 0.0482  518 TYR A CD2 
4143  C CE1 . TYR A 518 ? 0.4381 0.2737 0.4634 -0.0616 -0.0181 0.0388  518 TYR A CE1 
4144  C CE2 . TYR A 518 ? 0.4674 0.3031 0.4825 -0.0711 -0.0046 0.0435  518 TYR A CE2 
4145  C CZ  . TYR A 518 ? 0.4566 0.2979 0.4800 -0.0652 -0.0075 0.0388  518 TYR A CZ  
4146  O OH  . TYR A 518 ? 0.4539 0.3065 0.4847 -0.0629 0.0000  0.0344  518 TYR A OH  
4147  N N   . ARG A 519 ? 0.5426 0.3257 0.5509 -0.0653 -0.0576 0.0575  519 ARG A N   
4148  C CA  . ARG A 519 ? 0.5835 0.3506 0.5821 -0.0658 -0.0686 0.0621  519 ARG A CA  
4149  C C   . ARG A 519 ? 0.6636 0.4191 0.6390 -0.0708 -0.0697 0.0662  519 ARG A C   
4150  O O   . ARG A 519 ? 0.7356 0.4797 0.6954 -0.0772 -0.0690 0.0719  519 ARG A O   
4151  C CB  . ARG A 519 ? 0.5500 0.3172 0.5608 -0.0582 -0.0792 0.0595  519 ARG A CB  
4152  C CG  . ARG A 519 ? 0.5468 0.2965 0.5478 -0.0587 -0.0912 0.0647  519 ARG A CG  
4153  C CD  . ARG A 519 ? 0.5326 0.2818 0.5467 -0.0510 -0.1023 0.0625  519 ARG A CD  
4154  N NE  . ARG A 519 ? 0.5057 0.2630 0.5394 -0.0460 -0.1013 0.0588  519 ARG A NE  
4155  C CZ  . ARG A 519 ? 0.5030 0.2532 0.5377 -0.0471 -0.1028 0.0610  519 ARG A CZ  
4156  N NH1 . ARG A 519 ? 0.5165 0.2501 0.5349 -0.0525 -0.1072 0.0674  519 ARG A NH1 
4157  N NH2 . ARG A 519 ? 0.4979 0.2570 0.5493 -0.0430 -0.0999 0.0567  519 ARG A NH2 
4158  N N   . GLY A 520 ? 0.7150 0.4723 0.6869 -0.0683 -0.0720 0.0636  520 GLY A N   
4159  C CA  . GLY A 520 ? 0.7956 0.5388 0.7436 -0.0728 -0.0755 0.0677  520 GLY A CA  
4160  C C   . GLY A 520 ? 0.7361 0.4812 0.6695 -0.0786 -0.0636 0.0680  520 GLY A C   
4161  O O   . GLY A 520 ? 0.6584 0.4116 0.5966 -0.0815 -0.0528 0.0676  520 GLY A O   
4162  N N   . ASP A 521 ? 0.7505 0.4873 0.6659 -0.0801 -0.0665 0.0686  521 ASP A N   
4163  C CA  . ASP A 521 ? 0.7613 0.5036 0.6682 -0.0817 -0.0572 0.0652  521 ASP A CA  
4164  C C   . ASP A 521 ? 0.6837 0.4346 0.6028 -0.0753 -0.0612 0.0590  521 ASP A C   
4165  O O   . ASP A 521 ? 0.7634 0.5121 0.6706 -0.0760 -0.0600 0.0568  521 ASP A O   
4166  C CB  . ASP A 521 ? 0.8280 0.5543 0.7053 -0.0878 -0.0576 0.0698  521 ASP A CB  
4167  C CG  . ASP A 521 ? 0.9229 0.6340 0.7858 -0.0868 -0.0719 0.0722  521 ASP A CG  
4168  O OD1 . ASP A 521 ? 0.8803 0.5925 0.7573 -0.0812 -0.0830 0.0707  521 ASP A OD1 
4169  O OD2 . ASP A 521 ? 1.0280 0.7259 0.8651 -0.0916 -0.0721 0.0753  521 ASP A OD2 
4170  N N   . TRP A 522 ? 0.6059 0.3658 0.5477 -0.0694 -0.0661 0.0561  522 TRP A N   
4171  C CA  . TRP A 522 ? 0.5947 0.3617 0.5481 -0.0640 -0.0708 0.0511  522 TRP A CA  
4172  C C   . TRP A 522 ? 0.5933 0.3730 0.5521 -0.0634 -0.0596 0.0457  522 TRP A C   
4173  O O   . TRP A 522 ? 0.6154 0.3977 0.5750 -0.0612 -0.0615 0.0419  522 TRP A O   
4174  C CB  . TRP A 522 ? 0.5734 0.3473 0.5499 -0.0580 -0.0778 0.0495  522 TRP A CB  
4175  C CG  . TRP A 522 ? 0.5700 0.3587 0.5661 -0.0556 -0.0690 0.0464  522 TRP A CG  
4176  C CD1 . TRP A 522 ? 0.5747 0.3641 0.5750 -0.0571 -0.0652 0.0486  522 TRP A CD1 
4177  C CD2 . TRP A 522 ? 0.5972 0.4014 0.6101 -0.0517 -0.0632 0.0407  522 TRP A CD2 
4178  N NE1 . TRP A 522 ? 0.5614 0.3653 0.5793 -0.0543 -0.0578 0.0446  522 TRP A NE1 
4179  C CE2 . TRP A 522 ? 0.5644 0.3775 0.5901 -0.0509 -0.0563 0.0399  522 TRP A CE2 
4180  C CE3 . TRP A 522 ? 0.5859 0.3967 0.6041 -0.0490 -0.0633 0.0364  522 TRP A CE3 
4181  C CZ2 . TRP A 522 ? 0.5482 0.3759 0.5904 -0.0475 -0.0498 0.0353  522 TRP A CZ2 
4182  C CZ3 . TRP A 522 ? 0.5466 0.3718 0.5818 -0.0458 -0.0567 0.0320  522 TRP A CZ3 
4183  C CH2 . TRP A 522 ? 0.5519 0.3853 0.5985 -0.0449 -0.0500 0.0316  522 TRP A CH2 
4184  N N   . ALA A 523 ? 0.5806 0.3679 0.5435 -0.0654 -0.0484 0.0455  523 ALA A N   
4185  C CA  . ALA A 523 ? 0.5859 0.3863 0.5574 -0.0641 -0.0378 0.0406  523 ALA A CA  
4186  C C   . ALA A 523 ? 0.6250 0.4221 0.5782 -0.0689 -0.0282 0.0409  523 ALA A C   
4187  O O   . ALA A 523 ? 0.6135 0.4210 0.5730 -0.0687 -0.0177 0.0378  523 ALA A O   
4188  C CB  . ALA A 523 ? 0.5866 0.3989 0.5774 -0.0623 -0.0324 0.0397  523 ALA A CB  
4189  N N   . LYS A 524 ? 0.6691 0.4515 0.5996 -0.0731 -0.0320 0.0446  524 LYS A N   
4190  C CA  . LYS A 524 ? 0.6927 0.4708 0.6034 -0.0774 -0.0231 0.0444  524 LYS A CA  
4191  C C   . LYS A 524 ? 0.6577 0.4444 0.5731 -0.0741 -0.0174 0.0376  524 LYS A C   
4192  O O   . LYS A 524 ? 0.6000 0.3931 0.5137 -0.0754 -0.0055 0.0356  524 LYS A O   
4193  C CB  . LYS A 524 ? 0.7429 0.5026 0.6275 -0.0811 -0.0306 0.0485  524 LYS A CB  
4194  C CG  . LYS A 524 ? 0.8601 0.6141 0.7219 -0.0861 -0.0207 0.0488  524 LYS A CG  
4195  C CD  . LYS A 524 ? 0.9500 0.6849 0.7831 -0.0898 -0.0281 0.0523  524 LYS A CD  
4196  C CE  . LYS A 524 ? 0.9864 0.7155 0.7967 -0.0957 -0.0166 0.0541  524 LYS A CE  
4197  N NZ  . LYS A 524 ? 1.0193 0.7287 0.8001 -0.0995 -0.0241 0.0581  524 LYS A NZ  
4198  N N   . GLU A 525 ? 0.6125 0.3998 0.5347 -0.0698 -0.0258 0.0343  525 GLU A N   
4199  C CA  . GLU A 525 ? 0.6169 0.4104 0.5420 -0.0671 -0.0213 0.0281  525 GLU A CA  
4200  C C   . GLU A 525 ? 0.5545 0.3648 0.5050 -0.0630 -0.0155 0.0247  525 GLU A C   
4201  O O   . GLU A 525 ? 0.5488 0.3666 0.5020 -0.0625 -0.0052 0.0214  525 GLU A O   
4202  C CB  . GLU A 525 ? 0.6107 0.3969 0.5299 -0.0653 -0.0317 0.0257  525 GLU A CB  
4203  C CG  . GLU A 525 ? 0.6341 0.4027 0.5265 -0.0692 -0.0384 0.0287  525 GLU A CG  
4204  C CD  . GLU A 525 ? 0.6710 0.4309 0.5613 -0.0702 -0.0499 0.0346  525 GLU A CD  
4205  O OE1 . GLU A 525 ? 0.6140 0.3809 0.5250 -0.0669 -0.0556 0.0353  525 GLU A OE1 
4206  O OE2 . GLU A 525 ? 0.6915 0.4368 0.5581 -0.0744 -0.0530 0.0384  525 GLU A OE2 
4207  N N   . VAL A 526 ? 0.5265 0.3425 0.4954 -0.0598 -0.0219 0.0254  526 VAL A N   
4208  C CA  . VAL A 526 ? 0.5064 0.3368 0.4977 -0.0554 -0.0181 0.0217  526 VAL A CA  
4209  C C   . VAL A 526 ? 0.4865 0.3263 0.4879 -0.0560 -0.0092 0.0227  526 VAL A C   
4210  O O   . VAL A 526 ? 0.4526 0.3038 0.4683 -0.0531 -0.0035 0.0195  526 VAL A O   
4211  C CB  . VAL A 526 ? 0.5105 0.3435 0.5170 -0.0515 -0.0283 0.0215  526 VAL A CB  
4212  C CG1 . VAL A 526 ? 0.5232 0.3519 0.5319 -0.0521 -0.0347 0.0261  526 VAL A CG1 
4213  C CG2 . VAL A 526 ? 0.4812 0.3281 0.5090 -0.0472 -0.0245 0.0179  526 VAL A CG2 
4214  N N   . GLY A 527 ? 0.4959 0.3306 0.4905 -0.0597 -0.0088 0.0273  527 GLY A N   
4215  C CA  . GLY A 527 ? 0.4740 0.3170 0.4789 -0.0608 -0.0016 0.0285  527 GLY A CA  
4216  C C   . GLY A 527 ? 0.4819 0.3309 0.4833 -0.0626 0.0105  0.0265  527 GLY A C   
4217  O O   . GLY A 527 ? 0.4943 0.3368 0.4791 -0.0649 0.0136  0.0260  527 GLY A O   
4218  N N   . ARG A 528 ? 0.5038 0.3650 0.5209 -0.0614 0.0171  0.0253  528 ARG A N   
4219  C CA  . ARG A 528 ? 0.5620 0.4310 0.5799 -0.0625 0.0287  0.0232  528 ARG A CA  
4220  C C   . ARG A 528 ? 0.6230 0.4859 0.6254 -0.0687 0.0343  0.0270  528 ARG A C   
4221  O O   . ARG A 528 ? 0.6089 0.4680 0.6102 -0.0723 0.0318  0.0317  528 ARG A O   
4222  C CB  . ARG A 528 ? 0.5578 0.4400 0.5955 -0.0609 0.0331  0.0225  528 ARG A CB  
4223  C CG  . ARG A 528 ? 0.5488 0.4406 0.5903 -0.0615 0.0446  0.0204  528 ARG A CG  
4224  C CD  . ARG A 528 ? 0.5248 0.4291 0.5863 -0.0601 0.0472  0.0200  528 ARG A CD  
4225  N NE  . ARG A 528 ? 0.4869 0.3975 0.5622 -0.0542 0.0435  0.0166  528 ARG A NE  
4226  C CZ  . ARG A 528 ? 0.4699 0.3807 0.5541 -0.0521 0.0362  0.0173  528 ARG A CZ  
4227  N NH1 . ARG A 528 ? 0.4866 0.3914 0.5681 -0.0549 0.0311  0.0210  528 ARG A NH1 
4228  N NH2 . ARG A 528 ? 0.4674 0.3838 0.5626 -0.0470 0.0340  0.0142  528 ARG A NH2 
4229  N N   . LYS A 529 ? 0.7037 0.5658 0.6945 -0.0698 0.0422  0.0248  529 LYS A N   
4230  C CA  . LYS A 529 ? 0.8418 0.7005 0.8190 -0.0758 0.0501  0.0280  529 LYS A CA  
4231  C C   . LYS A 529 ? 0.7759 0.6492 0.7669 -0.0756 0.0617  0.0259  529 LYS A C   
4232  O O   . LYS A 529 ? 0.7863 0.6681 0.7868 -0.0709 0.0655  0.0208  529 LYS A O   
4233  C CB  . LYS A 529 ? 0.9841 0.8312 0.9367 -0.0780 0.0522  0.0275  529 LYS A CB  
4234  C CG  . LYS A 529 ? 1.1209 0.9516 1.0559 -0.0802 0.0411  0.0313  529 LYS A CG  
4235  C CD  . LYS A 529 ? 1.2168 1.0444 1.1553 -0.0751 0.0305  0.0280  529 LYS A CD  
4236  C CE  . LYS A 529 ? 1.1918 1.0180 1.1221 -0.0724 0.0334  0.0223  529 LYS A CE  
4237  N NZ  . LYS A 529 ? 1.1593 0.9836 1.0956 -0.0680 0.0231  0.0195  529 LYS A NZ  
4238  N N   . LEU A 530 ? 0.7795 0.6553 0.7720 -0.0808 0.0665  0.0301  530 LEU A N   
4239  C CA  . LEU A 530 ? 0.8763 0.7667 0.8839 -0.0813 0.0768  0.0288  530 LEU A CA  
4240  C C   . LEU A 530 ? 0.9014 0.7924 0.8962 -0.0844 0.0889  0.0280  530 LEU A C   
4241  O O   . LEU A 530 ? 0.8517 0.7298 0.8237 -0.0882 0.0889  0.0304  530 LEU A O   
4242  C CB  . LEU A 530 ? 0.9146 0.8086 0.9334 -0.0854 0.0751  0.0336  530 LEU A CB  
4243  C CG  . LEU A 530 ? 0.8722 0.7708 0.9093 -0.0814 0.0664  0.0329  530 LEU A CG  
4244  C CD1 . LEU A 530 ? 0.8625 0.7741 0.9165 -0.0748 0.0692  0.0271  530 LEU A CD1 
4245  C CD2 . LEU A 530 ? 0.7679 0.6541 0.7978 -0.0798 0.0540  0.0346  530 LEU A CD2 
4246  N N   . LYS B 4   ? 0.7658 0.5053 0.8147 0.0714  0.0608  -0.0397 4   LYS B N   
4247  C CA  . LYS B 4   ? 0.7563 0.5144 0.8202 0.0624  0.0553  -0.0359 4   LYS B CA  
4248  C C   . LYS B 4   ? 0.6269 0.4081 0.7088 0.0688  0.0566  -0.0302 4   LYS B C   
4249  O O   . LYS B 4   ? 0.5831 0.3694 0.6672 0.0797  0.0616  -0.0294 4   LYS B O   
4250  C CB  . LYS B 4   ? 0.8207 0.5820 0.8794 0.0546  0.0532  -0.0394 4   LYS B CB  
4251  C CG  . LYS B 4   ? 0.8563 0.6310 0.9167 0.0606  0.0577  -0.0399 4   LYS B CG  
4252  C CD  . LYS B 4   ? 0.9028 0.6701 0.9491 0.0562  0.0576  -0.0450 4   LYS B CD  
4253  C CE  . LYS B 4   ? 0.9092 0.6957 0.9618 0.0582  0.0602  -0.0436 4   LYS B CE  
4254  N NZ  . LYS B 4   ? 0.9246 0.7209 0.9832 0.0698  0.0672  -0.0418 4   LYS B NZ  
4255  N N   . THR B 5   ? 0.5594 0.3545 0.6543 0.0617  0.0518  -0.0265 5   THR B N   
4256  C CA  . THR B 5   ? 0.5069 0.3248 0.6188 0.0648  0.0517  -0.0215 5   THR B CA  
4257  C C   . THR B 5   ? 0.4757 0.3096 0.5923 0.0686  0.0551  -0.0219 5   THR B C   
4258  O O   . THR B 5   ? 0.4672 0.3021 0.5794 0.0630  0.0543  -0.0243 5   THR B O   
4259  C CB  . THR B 5   ? 0.4845 0.3121 0.6061 0.0547  0.0459  -0.0190 5   THR B CB  
4260  O OG1 . THR B 5   ? 0.4661 0.2778 0.5819 0.0513  0.0437  -0.0190 5   THR B OG1 
4261  C CG2 . THR B 5   ? 0.4578 0.3072 0.5959 0.0568  0.0452  -0.0142 5   THR B CG2 
4262  N N   . LYS B 6   ? 0.4908 0.3374 0.6161 0.0778  0.0588  -0.0192 6   LYS B N   
4263  C CA  . LYS B 6   ? 0.4933 0.3592 0.6266 0.0807  0.0621  -0.0183 6   LYS B CA  
4264  C C   . LYS B 6   ? 0.4697 0.3556 0.6188 0.0746  0.0581  -0.0141 6   LYS B C   
4265  O O   . LYS B 6   ? 0.4364 0.3288 0.5948 0.0759  0.0559  -0.0107 6   LYS B O   
4266  C CB  . LYS B 6   ? 0.5376 0.4078 0.6728 0.0936  0.0680  -0.0177 6   LYS B CB  
4267  C CG  . LYS B 6   ? 0.5960 0.4828 0.7358 0.0970  0.0731  -0.0180 6   LYS B CG  
4268  C CD  . LYS B 6   ? 0.6792 0.5767 0.8257 0.1097  0.0786  -0.0164 6   LYS B CD  
4269  C CE  . LYS B 6   ? 0.7235 0.6456 0.8815 0.1104  0.0823  -0.0147 6   LYS B CE  
4270  N NZ  . LYS B 6   ? 0.7546 0.6852 0.9158 0.1233  0.0890  -0.0146 6   LYS B NZ  
4271  N N   . ILE B 7   ? 0.4627 0.3562 0.6131 0.0674  0.0568  -0.0146 7   ILE B N   
4272  C CA  . ILE B 7   ? 0.4256 0.3364 0.5894 0.0617  0.0534  -0.0111 7   ILE B CA  
4273  C C   . ILE B 7   ? 0.4052 0.3338 0.5769 0.0652  0.0576  -0.0095 7   ILE B C   
4274  O O   . ILE B 7   ? 0.4046 0.3324 0.5696 0.0659  0.0613  -0.0116 7   ILE B O   
4275  C CB  . ILE B 7   ? 0.4070 0.3147 0.5679 0.0515  0.0487  -0.0119 7   ILE B CB  
4276  C CG1 . ILE B 7   ? 0.4275 0.3191 0.5813 0.0475  0.0449  -0.0136 7   ILE B CG1 
4277  C CG2 . ILE B 7   ? 0.4031 0.3274 0.5772 0.0465  0.0457  -0.0083 7   ILE B CG2 
4278  C CD1 . ILE B 7   ? 0.4340 0.3246 0.5868 0.0379  0.0397  -0.0141 7   ILE B CD1 
4279  N N   . GLU B 8   ? 0.4025 0.3474 0.5880 0.0666  0.0569  -0.0059 8   GLU B N   
4280  C CA  . GLU B 8   ? 0.4102 0.3738 0.6046 0.0685  0.0607  -0.0041 8   GLU B CA  
4281  C C   . GLU B 8   ? 0.3893 0.3679 0.5961 0.0615  0.0569  -0.0009 8   GLU B C   
4282  O O   . GLU B 8   ? 0.3788 0.3600 0.5922 0.0603  0.0528  0.0011  8   GLU B O   
4283  C CB  . GLU B 8   ? 0.4089 0.3769 0.6061 0.0796  0.0652  -0.0038 8   GLU B CB  
4284  C CG  . GLU B 8   ? 0.4770 0.4671 0.6854 0.0820  0.0693  -0.0018 8   GLU B CG  
4285  C CD  . GLU B 8   ? 0.5492 0.5457 0.7594 0.0937  0.0754  -0.0021 8   GLU B CD  
4286  O OE1 . GLU B 8   ? 0.6566 0.6380 0.8577 0.1017  0.0771  -0.0041 8   GLU B OE1 
4287  O OE2 . GLU B 8   ? 0.5197 0.5368 0.7406 0.0943  0.0787  -0.0003 8   GLU B OE2 
4288  N N   . LEU B 9   ? 0.3727 0.3603 0.5814 0.0568  0.0585  -0.0003 9   LEU B N   
4289  C CA  . LEU B 9   ? 0.3544 0.3544 0.5730 0.0498  0.0554  0.0025  9   LEU B CA  
4290  C C   . LEU B 9   ? 0.3358 0.3557 0.5661 0.0523  0.0589  0.0048  9   LEU B C   
4291  O O   . LEU B 9   ? 0.3132 0.3393 0.5424 0.0541  0.0643  0.0044  9   LEU B O   
4292  C CB  . LEU B 9   ? 0.3651 0.3601 0.5770 0.0424  0.0546  0.0019  9   LEU B CB  
4293  C CG  . LEU B 9   ? 0.3824 0.3597 0.5832 0.0394  0.0508  -0.0004 9   LEU B CG  
4294  C CD1 . LEU B 9   ? 0.3702 0.3461 0.5663 0.0327  0.0497  -0.0001 9   LEU B CD1 
4295  C CD2 . LEU B 9   ? 0.3560 0.3274 0.5595 0.0375  0.0453  -0.0001 9   LEU B CD2 
4296  N N   . LYS B 10  ? 0.3457 0.3765 0.5872 0.0519  0.0559  0.0071  10  LYS B N   
4297  C CA  . LYS B 10  ? 0.3761 0.4271 0.6296 0.0548  0.0586  0.0091  10  LYS B CA  
4298  C C   . LYS B 10  ? 0.3515 0.4119 0.6153 0.0510  0.0532  0.0115  10  LYS B C   
4299  O O   . LYS B 10  ? 0.2953 0.3463 0.5568 0.0510  0.0487  0.0114  10  LYS B O   
4300  C CB  . LYS B 10  ? 0.4421 0.4933 0.6942 0.0661  0.0630  0.0082  10  LYS B CB  
4301  C CG  . LYS B 10  ? 0.4965 0.5680 0.7613 0.0724  0.0652  0.0103  10  LYS B CG  
4302  C CD  . LYS B 10  ? 0.5872 0.6758 0.8580 0.0730  0.0716  0.0107  10  LYS B CD  
4303  C CE  . LYS B 10  ? 0.6547 0.7617 0.9371 0.0825  0.0740  0.0123  10  LYS B CE  
4304  N NZ  . LYS B 10  ? 0.6686 0.8006 0.9644 0.0788  0.0769  0.0144  10  LYS B NZ  
4305  N N   . ASP B 11  ? 0.3465 0.4250 0.6208 0.0470  0.0540  0.0133  11  ASP B N   
4306  C CA  . ASP B 11  ? 0.3192 0.4082 0.6031 0.0423  0.0493  0.0152  11  ASP B CA  
4307  C C   . ASP B 11  ? 0.2880 0.3634 0.5661 0.0353  0.0443  0.0147  11  ASP B C   
4308  O O   . ASP B 11  ? 0.2849 0.3606 0.5662 0.0341  0.0397  0.0154  11  ASP B O   
4309  C CB  . ASP B 11  ? 0.3451 0.4409 0.6351 0.0497  0.0470  0.0163  11  ASP B CB  
4310  C CG  . ASP B 11  ? 0.3981 0.5082 0.6947 0.0585  0.0516  0.0170  11  ASP B CG  
4311  O OD1 . ASP B 11  ? 0.4378 0.5635 0.7417 0.0554  0.0549  0.0178  11  ASP B OD1 
4312  O OD2 . ASP B 11  ? 0.4760 0.5804 0.7695 0.0684  0.0523  0.0168  11  ASP B OD2 
4313  N N   . ASN B 12  ? 0.3047 0.3678 0.5737 0.0316  0.0454  0.0134  12  ASN B N   
4314  C CA  . ASN B 12  ? 0.2954 0.3456 0.5585 0.0257  0.0412  0.0129  12  ASN B CA  
4315  C C   . ASN B 12  ? 0.2708 0.3102 0.5304 0.0290  0.0377  0.0120  12  ASN B C   
4316  O O   . ASN B 12  ? 0.2555 0.2905 0.5151 0.0247  0.0335  0.0122  12  ASN B O   
4317  C CB  . ASN B 12  ? 0.2715 0.3285 0.5405 0.0179  0.0383  0.0143  12  ASN B CB  
4318  C CG  . ASN B 12  ? 0.2694 0.3365 0.5415 0.0139  0.0422  0.0154  12  ASN B CG  
4319  O OD1 . ASN B 12  ? 0.2836 0.3477 0.5501 0.0151  0.0465  0.0150  12  ASN B OD1 
4320  N ND2 . ASN B 12  ? 0.2836 0.3631 0.5643 0.0090  0.0411  0.0168  12  ASN B ND2 
4321  N N   . TRP B 13  ? 0.2875 0.3218 0.5434 0.0365  0.0397  0.0111  13  TRP B N   
4322  C CA  . TRP B 13  ? 0.2857 0.3070 0.5361 0.0393  0.0371  0.0103  13  TRP B CA  
4323  C C   . TRP B 13  ? 0.2872 0.2945 0.5269 0.0425  0.0397  0.0080  13  TRP B C   
4324  O O   . TRP B 13  ? 0.2860 0.2955 0.5237 0.0470  0.0443  0.0072  13  TRP B O   
4325  C CB  . TRP B 13  ? 0.2992 0.3263 0.5547 0.0459  0.0365  0.0118  13  TRP B CB  
4326  C CG  . TRP B 13  ? 0.3181 0.3537 0.5809 0.0429  0.0322  0.0137  13  TRP B CG  
4327  C CD1 . TRP B 13  ? 0.2864 0.3383 0.5587 0.0401  0.0313  0.0151  13  TRP B CD1 
4328  C CD2 . TRP B 13  ? 0.3278 0.3555 0.5882 0.0423  0.0283  0.0142  13  TRP B CD2 
4329  N NE1 . TRP B 13  ? 0.2967 0.3504 0.5718 0.0379  0.0268  0.0161  13  TRP B NE1 
4330  C CE2 . TRP B 13  ? 0.3085 0.3478 0.5764 0.0394  0.0252  0.0157  13  TRP B CE2 
4331  C CE3 . TRP B 13  ? 0.3409 0.3529 0.5932 0.0433  0.0274  0.0134  13  TRP B CE3 
4332  C CZ2 . TRP B 13  ? 0.3099 0.3454 0.5768 0.0383  0.0214  0.0165  13  TRP B CZ2 
4333  C CZ3 . TRP B 13  ? 0.3602 0.3691 0.6123 0.0418  0.0239  0.0145  13  TRP B CZ3 
4334  C CH2 . TRP B 13  ? 0.3350 0.3555 0.5940 0.0396  0.0211  0.0160  13  TRP B CH2 
4335  N N   . TYR B 14  ? 0.2828 0.2761 0.5158 0.0408  0.0369  0.0069  14  TYR B N   
4336  C CA  . TYR B 14  ? 0.2804 0.2592 0.5030 0.0443  0.0388  0.0046  14  TYR B CA  
4337  C C   . TYR B 14  ? 0.2892 0.2663 0.5121 0.0525  0.0402  0.0052  14  TYR B C   
4338  O O   . TYR B 14  ? 0.2882 0.2685 0.5160 0.0535  0.0377  0.0073  14  TYR B O   
4339  C CB  . TYR B 14  ? 0.2746 0.2390 0.4900 0.0398  0.0354  0.0031  14  TYR B CB  
4340  C CG  . TYR B 14  ? 0.2829 0.2446 0.4947 0.0331  0.0338  0.0019  14  TYR B CG  
4341  C CD1 . TYR B 14  ? 0.2690 0.2400 0.4873 0.0281  0.0318  0.0035  14  TYR B CD1 
4342  C CD2 . TYR B 14  ? 0.2957 0.2444 0.4972 0.0315  0.0335  -0.0007 14  TYR B CD2 
4343  C CE1 . TYR B 14  ? 0.2684 0.2360 0.4830 0.0227  0.0299  0.0029  14  TYR B CE1 
4344  C CE2 . TYR B 14  ? 0.3011 0.2479 0.4994 0.0256  0.0312  -0.0015 14  TYR B CE2 
4345  C CZ  . TYR B 14  ? 0.2721 0.2284 0.4771 0.0217  0.0294  0.0006  14  TYR B CZ  
4346  O OH  . TYR B 14  ? 0.2631 0.2174 0.4649 0.0169  0.0269  0.0003  14  TYR B OH  
4347  N N   . HIS B 15  ? 0.2978 0.2695 0.5145 0.0587  0.0445  0.0035  15  HIS B N   
4348  C CA  . HIS B 15  ? 0.3203 0.2844 0.5334 0.0671  0.0460  0.0036  15  HIS B CA  
4349  C C   . HIS B 15  ? 0.3435 0.2858 0.5425 0.0668  0.0465  0.0005  15  HIS B C   
4350  O O   . HIS B 15  ? 0.3267 0.2634 0.5184 0.0648  0.0485  -0.0023 15  HIS B O   
4351  C CB  . HIS B 15  ? 0.3170 0.2918 0.5341 0.0759  0.0510  0.0040  15  HIS B CB  
4352  C CG  . HIS B 15  ? 0.3150 0.3121 0.5461 0.0752  0.0505  0.0068  15  HIS B CG  
4353  N ND1 . HIS B 15  ? 0.3158 0.3237 0.5522 0.0675  0.0500  0.0071  15  HIS B ND1 
4354  C CD2 . HIS B 15  ? 0.3154 0.3256 0.5558 0.0811  0.0501  0.0095  15  HIS B CD2 
4355  C CE1 . HIS B 15  ? 0.3087 0.3354 0.5574 0.0680  0.0494  0.0097  15  HIS B CE1 
4356  N NE2 . HIS B 15  ? 0.3011 0.3304 0.5527 0.0762  0.0492  0.0111  15  HIS B NE2 
4357  N N   . LEU B 16  ? 0.3683 0.2983 0.5629 0.0684  0.0446  0.0011  16  LEU B N   
4358  C CA  . LEU B 16  ? 0.4078 0.3161 0.5886 0.0691  0.0456  -0.0018 16  LEU B CA  
4359  C C   . LEU B 16  ? 0.4152 0.3172 0.5927 0.0800  0.0487  -0.0010 16  LEU B C   
4360  O O   . LEU B 16  ? 0.3876 0.2923 0.5697 0.0831  0.0469  0.0023  16  LEU B O   
4361  C CB  . LEU B 16  ? 0.4229 0.3201 0.6001 0.0614  0.0413  -0.0017 16  LEU B CB  
4362  C CG  . LEU B 16  ? 0.4476 0.3440 0.6232 0.0514  0.0385  -0.0038 16  LEU B CG  
4363  C CD1 . LEU B 16  ? 0.4543 0.3689 0.6397 0.0488  0.0380  -0.0026 16  LEU B CD1 
4364  C CD2 . LEU B 16  ? 0.4358 0.3260 0.6112 0.0441  0.0344  -0.0030 16  LEU B CD2 
4365  N N   . ASP B 17  ? 0.4504 0.3440 0.6192 0.0861  0.0533  -0.0040 17  ASP B N   
4366  C CA  . ASP B 17  ? 0.4823 0.3660 0.6452 0.0973  0.0567  -0.0039 17  ASP B CA  
4367  C C   . ASP B 17  ? 0.4911 0.3944 0.6674 0.1051  0.0571  0.0003  17  ASP B C   
4368  O O   . ASP B 17  ? 0.4882 0.3863 0.6637 0.1118  0.0565  0.0029  17  ASP B O   
4369  C CB  . ASP B 17  ? 0.4940 0.3545 0.6457 0.0962  0.0548  -0.0041 17  ASP B CB  
4370  C CG  . ASP B 17  ? 0.5366 0.3754 0.6731 0.0902  0.0550  -0.0088 17  ASP B CG  
4371  O OD1 . ASP B 17  ? 0.5396 0.3773 0.6707 0.0903  0.0579  -0.0126 17  ASP B OD1 
4372  O OD2 . ASP B 17  ? 0.5454 0.3684 0.6750 0.0850  0.0523  -0.0088 17  ASP B OD2 
4373  N N   . GLY B 18  ? 0.4749 0.4006 0.6630 0.1035  0.0578  0.0012  18  GLY B N   
4374  C CA  . GLY B 18  ? 0.4812 0.4282 0.6829 0.1103  0.0583  0.0048  18  GLY B CA  
4375  C C   . GLY B 18  ? 0.4804 0.4398 0.6929 0.1050  0.0527  0.0086  18  GLY B C   
4376  O O   . GLY B 18  ? 0.5471 0.5265 0.7717 0.1085  0.0522  0.0113  18  GLY B O   
4377  N N   . GLU B 19  ? 0.4469 0.3954 0.6551 0.0965  0.0485  0.0086  19  GLU B N   
4378  C CA  . GLU B 19  ? 0.4366 0.3934 0.6524 0.0925  0.0435  0.0119  19  GLU B CA  
4379  C C   . GLU B 19  ? 0.3818 0.3475 0.6031 0.0813  0.0409  0.0112  19  GLU B C   
4380  O O   . GLU B 19  ? 0.3874 0.3423 0.6020 0.0746  0.0406  0.0087  19  GLU B O   
4381  C CB  . GLU B 19  ? 0.5046 0.4431 0.7117 0.0914  0.0408  0.0130  19  GLU B CB  
4382  C CG  . GLU B 19  ? 0.5853 0.5081 0.7830 0.1016  0.0433  0.0136  19  GLU B CG  
4383  C CD  . GLU B 19  ? 0.6674 0.6039 0.8725 0.1131  0.0444  0.0166  19  GLU B CD  
4384  O OE1 . GLU B 19  ? 0.7206 0.6698 0.9340 0.1130  0.0407  0.0201  19  GLU B OE1 
4385  O OE2 . GLU B 19  ? 0.7428 0.6786 0.9459 0.1221  0.0488  0.0153  19  GLU B OE2 
4386  N N   . LYS B 20  ? 0.3393 0.3240 0.5723 0.0792  0.0387  0.0134  20  LYS B N   
4387  C CA  . LYS B 20  ? 0.3145 0.3052 0.5518 0.0690  0.0358  0.0131  20  LYS B CA  
4388  C C   . LYS B 20  ? 0.3208 0.2964 0.5512 0.0634  0.0328  0.0127  20  LYS B C   
4389  O O   . LYS B 20  ? 0.3082 0.2770 0.5358 0.0663  0.0313  0.0145  20  LYS B O   
4390  C CB  . LYS B 20  ? 0.3213 0.3316 0.5707 0.0676  0.0332  0.0157  20  LYS B CB  
4391  C CG  . LYS B 20  ? 0.3473 0.3753 0.6052 0.0687  0.0359  0.0157  20  LYS B CG  
4392  C CD  . LYS B 20  ? 0.3544 0.4030 0.6246 0.0672  0.0334  0.0180  20  LYS B CD  
4393  C CE  . LYS B 20  ? 0.4187 0.4830 0.6962 0.0694  0.0375  0.0179  20  LYS B CE  
4394  N NZ  . LYS B 20  ? 0.4620 0.5477 0.7517 0.0719  0.0361  0.0203  20  LYS B NZ  
4395  N N   . TYR B 21  ? 0.3039 0.2752 0.5318 0.0555  0.0320  0.0107  21  TYR B N   
4396  C CA  . TYR B 21  ? 0.3029 0.2610 0.5247 0.0501  0.0296  0.0100  21  TYR B CA  
4397  C C   . TYR B 21  ? 0.3019 0.2665 0.5284 0.0418  0.0268  0.0098  21  TYR B C   
4398  O O   . TYR B 21  ? 0.2782 0.2440 0.5042 0.0382  0.0274  0.0081  21  TYR B O   
4399  C CB  . TYR B 21  ? 0.3076 0.2501 0.5189 0.0500  0.0317  0.0070  21  TYR B CB  
4400  C CG  . TYR B 21  ? 0.3049 0.2335 0.5096 0.0444  0.0295  0.0061  21  TYR B CG  
4401  C CD1 . TYR B 21  ? 0.3205 0.2356 0.5184 0.0471  0.0298  0.0068  21  TYR B CD1 
4402  C CD2 . TYR B 21  ? 0.2903 0.2190 0.4952 0.0365  0.0274  0.0047  21  TYR B CD2 
4403  C CE1 . TYR B 21  ? 0.3031 0.2060 0.4953 0.0410  0.0281  0.0061  21  TYR B CE1 
4404  C CE2 . TYR B 21  ? 0.2978 0.2160 0.4979 0.0312  0.0254  0.0039  21  TYR B CE2 
4405  C CZ  . TYR B 21  ? 0.3059 0.2117 0.5001 0.0330  0.0259  0.0046  21  TYR B CZ  
4406  O OH  . TYR B 21  ? 0.3117 0.2083 0.5019 0.0267  0.0242  0.0040  21  TYR B OH  
4407  N N   . PHE B 22  ? 0.3041 0.2718 0.5342 0.0393  0.0239  0.0115  22  PHE B N   
4408  C CA  . PHE B 22  ? 0.3034 0.2756 0.5373 0.0323  0.0214  0.0113  22  PHE B CA  
4409  C C   . PHE B 22  ? 0.3109 0.2716 0.5390 0.0277  0.0205  0.0098  22  PHE B C   
4410  O O   . PHE B 22  ? 0.3102 0.2622 0.5342 0.0277  0.0201  0.0102  22  PHE B O   
4411  C CB  . PHE B 22  ? 0.2918 0.2712 0.5307 0.0318  0.0190  0.0134  22  PHE B CB  
4412  C CG  . PHE B 22  ? 0.3051 0.2907 0.5482 0.0257  0.0169  0.0129  22  PHE B CG  
4413  C CD1 . PHE B 22  ? 0.3131 0.2929 0.5542 0.0211  0.0156  0.0121  22  PHE B CD1 
4414  C CD2 . PHE B 22  ? 0.2719 0.2692 0.5212 0.0246  0.0164  0.0132  22  PHE B CD2 
4415  C CE1 . PHE B 22  ? 0.3126 0.2970 0.5571 0.0167  0.0140  0.0116  22  PHE B CE1 
4416  C CE2 . PHE B 22  ? 0.2606 0.2610 0.5124 0.0193  0.0147  0.0127  22  PHE B CE2 
4417  C CZ  . PHE B 22  ? 0.2832 0.2769 0.5324 0.0160  0.0135  0.0119  22  PHE B CZ  
4418  N N   . ILE B 23  ? 0.3209 0.2820 0.5487 0.0235  0.0200  0.0081  23  ILE B N   
4419  C CA  . ILE B 23  ? 0.3375 0.2901 0.5609 0.0190  0.0187  0.0066  23  ILE B CA  
4420  C C   . ILE B 23  ? 0.3281 0.2837 0.5556 0.0149  0.0162  0.0075  23  ILE B C   
4421  O O   . ILE B 23  ? 0.2886 0.2517 0.5209 0.0126  0.0149  0.0078  23  ILE B O   
4422  C CB  . ILE B 23  ? 0.3448 0.2972 0.5658 0.0166  0.0187  0.0047  23  ILE B CB  
4423  C CG1 . ILE B 23  ? 0.3425 0.2915 0.5585 0.0208  0.0219  0.0035  23  ILE B CG1 
4424  C CG2 . ILE B 23  ? 0.3758 0.3217 0.5935 0.0116  0.0165  0.0033  23  ILE B CG2 
4425  C CD1 . ILE B 23  ? 0.3560 0.3060 0.5691 0.0189  0.0224  0.0022  23  ILE B CD1 
4426  N N   . LYS B 24  ? 0.3231 0.2721 0.5481 0.0141  0.0160  0.0081  24  LYS B N   
4427  C CA  . LYS B 24  ? 0.3198 0.2710 0.5478 0.0103  0.0144  0.0088  24  LYS B CA  
4428  C C   . LYS B 24  ? 0.3084 0.2549 0.5344 0.0053  0.0133  0.0073  24  LYS B C   
4429  O O   . LYS B 24  ? 0.3023 0.2416 0.5249 0.0032  0.0136  0.0074  24  LYS B O   
4430  C CB  . LYS B 24  ? 0.3346 0.2827 0.5610 0.0123  0.0151  0.0110  24  LYS B CB  
4431  C CG  . LYS B 24  ? 0.3476 0.3017 0.5763 0.0173  0.0155  0.0127  24  LYS B CG  
4432  C CD  . LYS B 24  ? 0.3619 0.3146 0.5892 0.0188  0.0153  0.0151  24  LYS B CD  
4433  C CE  . LYS B 24  ? 0.3628 0.3050 0.5835 0.0225  0.0168  0.0165  24  LYS B CE  
4434  N NZ  . LYS B 24  ? 0.3822 0.3216 0.6003 0.0226  0.0166  0.0191  24  LYS B NZ  
4435  N N   . ALA B 25  ? 0.2998 0.2505 0.5279 0.0033  0.0119  0.0060  25  ALA B N   
4436  C CA  . ALA B 25  ? 0.2788 0.2269 0.5054 -0.0011 0.0102  0.0044  25  ALA B CA  
4437  C C   . ALA B 25  ? 0.2771 0.2321 0.5099 -0.0041 0.0086  0.0050  25  ALA B C   
4438  O O   . ALA B 25  ? 0.2623 0.2228 0.4993 -0.0028 0.0090  0.0064  25  ALA B O   
4439  C CB  . ALA B 25  ? 0.2889 0.2373 0.5132 -0.0011 0.0093  0.0030  25  ALA B CB  
4440  N N   . ILE B 26  ? 0.2765 0.2307 0.5091 -0.0082 0.0068  0.0039  26  ILE B N   
4441  C CA  . ILE B 26  ? 0.2646 0.2268 0.5035 -0.0107 0.0049  0.0041  26  ILE B CA  
4442  C C   . ILE B 26  ? 0.2445 0.2071 0.4820 -0.0132 0.0021  0.0025  26  ILE B C   
4443  O O   . ILE B 26  ? 0.2667 0.2222 0.4983 -0.0154 0.0017  0.0010  26  ILE B O   
4444  C CB  . ILE B 26  ? 0.2751 0.2386 0.5168 -0.0138 0.0059  0.0049  26  ILE B CB  
4445  C CG1 . ILE B 26  ? 0.2874 0.2611 0.5367 -0.0152 0.0046  0.0051  26  ILE B CG1 
4446  C CG2 . ILE B 26  ? 0.3103 0.2658 0.5471 -0.0182 0.0058  0.0039  26  ILE B CG2 
4447  C CD1 . ILE B 26  ? 0.2923 0.2692 0.5451 -0.0180 0.0063  0.0061  26  ILE B CD1 
4448  N N   . GLY B 27  ? 0.2403 0.2103 0.4822 -0.0126 0.0000  0.0028  27  GLY B N   
4449  C CA  . GLY B 27  ? 0.2264 0.1986 0.4679 -0.0149 -0.0035 0.0017  27  GLY B CA  
4450  C C   . GLY B 27  ? 0.2160 0.1902 0.4599 -0.0200 -0.0048 0.0009  27  GLY B C   
4451  O O   . GLY B 27  ? 0.2283 0.2067 0.4775 -0.0211 -0.0033 0.0018  27  GLY B O   
4452  N N   . TYR B 28  ? 0.2254 0.1968 0.4652 -0.0236 -0.0075 -0.0008 28  TYR B N   
4453  C CA  . TYR B 28  ? 0.2483 0.2209 0.4898 -0.0298 -0.0087 -0.0018 28  TYR B CA  
4454  C C   . TYR B 28  ? 0.2506 0.2267 0.4910 -0.0329 -0.0136 -0.0034 28  TYR B C   
4455  O O   . TYR B 28  ? 0.2508 0.2191 0.4825 -0.0327 -0.0147 -0.0049 28  TYR B O   
4456  C CB  . TYR B 28  ? 0.2568 0.2165 0.4905 -0.0324 -0.0062 -0.0028 28  TYR B CB  
4457  C CG  . TYR B 28  ? 0.2764 0.2348 0.5097 -0.0401 -0.0078 -0.0042 28  TYR B CG  
4458  C CD1 . TYR B 28  ? 0.2751 0.2446 0.5179 -0.0440 -0.0084 -0.0031 28  TYR B CD1 
4459  C CD2 . TYR B 28  ? 0.3071 0.2537 0.5306 -0.0438 -0.0089 -0.0068 28  TYR B CD2 
4460  C CE1 . TYR B 28  ? 0.2689 0.2384 0.5121 -0.0521 -0.0098 -0.0043 28  TYR B CE1 
4461  C CE2 . TYR B 28  ? 0.3193 0.2642 0.5421 -0.0520 -0.0106 -0.0083 28  TYR B CE2 
4462  C CZ  . TYR B 28  ? 0.2998 0.2569 0.5329 -0.0566 -0.0112 -0.0069 28  TYR B CZ  
4463  O OH  . TYR B 28  ? 0.3309 0.2873 0.5637 -0.0656 -0.0131 -0.0084 28  TYR B OH  
4464  N N   . GLU B 29  ? 0.2603 0.2486 0.5093 -0.0358 -0.0164 -0.0029 29  GLU B N   
4465  C CA  . GLU B 29  ? 0.2698 0.2639 0.5190 -0.0387 -0.0219 -0.0041 29  GLU B CA  
4466  C C   . GLU B 29  ? 0.2767 0.2761 0.5303 -0.0468 -0.0238 -0.0053 29  GLU B C   
4467  O O   . GLU B 29  ? 0.2636 0.2763 0.5284 -0.0478 -0.0238 -0.0039 29  GLU B O   
4468  C CB  . GLU B 29  ? 0.2753 0.2817 0.5321 -0.0337 -0.0244 -0.0022 29  GLU B CB  
4469  C CG  . GLU B 29  ? 0.2934 0.3066 0.5499 -0.0354 -0.0307 -0.0029 29  GLU B CG  
4470  C CD  . GLU B 29  ? 0.2827 0.3042 0.5433 -0.0288 -0.0333 -0.0007 29  GLU B CD  
4471  O OE1 . GLU B 29  ? 0.2556 0.2883 0.5268 -0.0260 -0.0329 0.0010  29  GLU B OE1 
4472  O OE2 . GLU B 29  ? 0.2751 0.2905 0.5272 -0.0262 -0.0354 -0.0005 29  GLU B OE2 
4473  N N   . ILE B 30  ? 0.2745 0.2636 0.5190 -0.0526 -0.0251 -0.0079 30  ILE B N   
4474  C CA  . ILE B 30  ? 0.3090 0.3026 0.5563 -0.0618 -0.0280 -0.0095 30  ILE B CA  
4475  C C   . ILE B 30  ? 0.3247 0.3342 0.5790 -0.0626 -0.0343 -0.0095 30  ILE B C   
4476  O O   . ILE B 30  ? 0.3511 0.3620 0.6027 -0.0572 -0.0370 -0.0091 30  ILE B O   
4477  C CB  . ILE B 30  ? 0.3223 0.2987 0.5562 -0.0678 -0.0282 -0.0128 30  ILE B CB  
4478  C CG1 . ILE B 30  ? 0.3396 0.3187 0.5764 -0.0787 -0.0300 -0.0142 30  ILE B CG1 
4479  C CG2 . ILE B 30  ? 0.3116 0.2821 0.5351 -0.0662 -0.0321 -0.0151 30  ILE B CG2 
4480  C CD1 . ILE B 30  ? 0.3344 0.3185 0.5802 -0.0814 -0.0257 -0.0118 30  ILE B CD1 
4481  N N   . GLY B 31  ? 0.3564 0.3787 0.6202 -0.0693 -0.0365 -0.0096 31  GLY B N   
4482  C CA  . GLY B 31  ? 0.3570 0.3947 0.6271 -0.0718 -0.0435 -0.0100 31  GLY B CA  
4483  C C   . GLY B 31  ? 0.3447 0.3997 0.6272 -0.0640 -0.0443 -0.0070 31  GLY B C   
4484  O O   . GLY B 31  ? 0.3368 0.4026 0.6224 -0.0619 -0.0502 -0.0066 31  GLY B O   
4485  N N   . ALA B 32  ? 0.3305 0.3878 0.6197 -0.0599 -0.0385 -0.0048 32  ALA B N   
4486  C CA  . ALA B 32  ? 0.3146 0.3850 0.6142 -0.0517 -0.0378 -0.0021 32  ALA B CA  
4487  C C   . ALA B 32  ? 0.3017 0.3832 0.6132 -0.0531 -0.0333 -0.0008 32  ALA B C   
4488  O O   . ALA B 32  ? 0.3435 0.4278 0.6594 -0.0461 -0.0295 0.0010  32  ALA B O   
4489  C CB  . ALA B 32  ? 0.2770 0.3353 0.5690 -0.0430 -0.0348 -0.0010 32  ALA B CB  
4490  N N   . ARG B 33  ? 0.2821 0.3687 0.5977 -0.0627 -0.0333 -0.0017 33  ARG B N   
4491  C CA  . ARG B 33  ? 0.2763 0.3776 0.6047 -0.0651 -0.0297 -0.0003 33  ARG B CA  
4492  C C   . ARG B 33  ? 0.2718 0.3954 0.6140 -0.0600 -0.0331 0.0010  33  ARG B C   
4493  O O   . ARG B 33  ? 0.2738 0.4014 0.6153 -0.0570 -0.0392 0.0007  33  ARG B O   
4494  C CB  . ARG B 33  ? 0.2720 0.3758 0.6024 -0.0778 -0.0301 -0.0016 33  ARG B CB  
4495  C CG  . ARG B 33  ? 0.2823 0.3699 0.6050 -0.0824 -0.0237 -0.0014 33  ARG B CG  
4496  C CD  . ARG B 33  ? 0.2903 0.3541 0.5971 -0.0782 -0.0221 -0.0023 33  ARG B CD  
4497  N NE  . ARG B 33  ? 0.3137 0.3642 0.6145 -0.0820 -0.0162 -0.0016 33  ARG B NE  
4498  C CZ  . ARG B 33  ? 0.3342 0.3636 0.6217 -0.0803 -0.0136 -0.0020 33  ARG B CZ  
4499  N NH1 . ARG B 33  ? 0.3294 0.3475 0.6074 -0.0746 -0.0155 -0.0033 33  ARG B NH1 
4500  N NH2 . ARG B 33  ? 0.3390 0.3592 0.6226 -0.0842 -0.0087 -0.0008 33  ARG B NH2 
4501  N N   . PRO B 34  ? 0.2611 0.4006 0.6163 -0.0590 -0.0293 0.0026  34  PRO B N   
4502  C CA  . PRO B 34  ? 0.2648 0.4279 0.6347 -0.0551 -0.0326 0.0037  34  PRO B CA  
4503  C C   . PRO B 34  ? 0.2893 0.4635 0.6631 -0.0633 -0.0400 0.0024  34  PRO B C   
4504  O O   . PRO B 34  ? 0.2967 0.4663 0.6674 -0.0747 -0.0401 0.0008  34  PRO B O   
4505  C CB  . PRO B 34  ? 0.2485 0.4245 0.6299 -0.0556 -0.0259 0.0051  34  PRO B CB  
4506  C CG  . PRO B 34  ? 0.2438 0.3999 0.6143 -0.0547 -0.0192 0.0052  34  PRO B CG  
4507  C CD  . PRO B 34  ? 0.2488 0.3846 0.6049 -0.0612 -0.0216 0.0035  34  PRO B CD  
4508  N N   . GLY B 35  ? 0.2989 0.4863 0.6784 -0.0573 -0.0463 0.0031  35  GLY B N   
4509  C CA  . GLY B 35  ? 0.3182 0.5175 0.7012 -0.0639 -0.0547 0.0020  35  GLY B CA  
4510  C C   . GLY B 35  ? 0.3150 0.4957 0.6811 -0.0658 -0.0601 0.0000  35  GLY B C   
4511  O O   . GLY B 35  ? 0.3330 0.5214 0.6993 -0.0706 -0.0677 -0.0012 35  GLY B O   
4512  N N   . GLN B 36  ? 0.3017 0.4589 0.6533 -0.0619 -0.0563 -0.0004 36  GLN B N   
4513  C CA  . GLN B 36  ? 0.3128 0.4516 0.6479 -0.0643 -0.0599 -0.0024 36  GLN B CA  
4514  C C   . GLN B 36  ? 0.3244 0.4531 0.6514 -0.0528 -0.0599 -0.0009 36  GLN B C   
4515  O O   . GLN B 36  ? 0.3296 0.4563 0.6592 -0.0449 -0.0547 0.0011  36  GLN B O   
4516  C CB  . GLN B 36  ? 0.3139 0.4308 0.6365 -0.0707 -0.0549 -0.0046 36  GLN B CB  
4517  C CG  . GLN B 36  ? 0.3065 0.4269 0.6344 -0.0820 -0.0523 -0.0057 36  GLN B CG  
4518  C CD  . GLN B 36  ? 0.3032 0.3995 0.6157 -0.0885 -0.0493 -0.0081 36  GLN B CD  
4519  O OE1 . GLN B 36  ? 0.2768 0.3561 0.5802 -0.0835 -0.0442 -0.0077 36  GLN B OE1 
4520  N NE2 . GLN B 36  ? 0.3301 0.4246 0.6395 -0.0999 -0.0526 -0.0107 36  GLN B NE2 
4521  N N   . ALA B 37  ? 0.3423 0.4641 0.6586 -0.0526 -0.0657 -0.0018 37  ALA B N   
4522  C CA  . ALA B 37  ? 0.3775 0.4869 0.6830 -0.0438 -0.0659 -0.0005 37  ALA B CA  
4523  C C   . ALA B 37  ? 0.3733 0.4639 0.6616 -0.0488 -0.0672 -0.0033 37  ALA B C   
4524  O O   . ALA B 37  ? 0.3528 0.4454 0.6363 -0.0542 -0.0734 -0.0051 37  ALA B O   
4525  C CB  . ALA B 37  ? 0.3899 0.5135 0.7009 -0.0368 -0.0723 0.0020  37  ALA B CB  
4526  N N   . PRO B 38  ? 0.3935 0.4655 0.6716 -0.0472 -0.0612 -0.0039 38  PRO B N   
4527  C CA  . PRO B 38  ? 0.4376 0.4923 0.7001 -0.0521 -0.0614 -0.0069 38  PRO B CA  
4528  C C   . PRO B 38  ? 0.4723 0.5229 0.7234 -0.0500 -0.0671 -0.0072 38  PRO B C   
4529  O O   . PRO B 38  ? 0.4672 0.5084 0.7069 -0.0558 -0.0694 -0.0104 38  PRO B O   
4530  C CB  . PRO B 38  ? 0.4319 0.4712 0.6887 -0.0484 -0.0536 -0.0065 38  PRO B CB  
4531  C CG  . PRO B 38  ? 0.4317 0.4785 0.6972 -0.0396 -0.0512 -0.0030 38  PRO B CG  
4532  C CD  . PRO B 38  ? 0.3896 0.4569 0.6704 -0.0403 -0.0543 -0.0018 38  PRO B CD  
4533  N N   . TYR B 39  ? 0.5006 0.5578 0.7541 -0.0418 -0.0695 -0.0040 39  TYR B N   
4534  C CA  . TYR B 39  ? 0.4818 0.5337 0.7231 -0.0390 -0.0744 -0.0035 39  TYR B CA  
4535  C C   . TYR B 39  ? 0.4671 0.5345 0.7124 -0.0417 -0.0837 -0.0035 39  TYR B C   
4536  O O   . TYR B 39  ? 0.4619 0.5247 0.6953 -0.0415 -0.0886 -0.0039 39  TYR B O   
4537  C CB  . TYR B 39  ? 0.4578 0.5043 0.6958 -0.0292 -0.0718 0.0001  39  TYR B CB  
4538  C CG  . TYR B 39  ? 0.4455 0.4762 0.6773 -0.0277 -0.0636 -0.0004 39  TYR B CG  
4539  C CD1 . TYR B 39  ? 0.4417 0.4569 0.6589 -0.0302 -0.0614 -0.0027 39  TYR B CD1 
4540  C CD2 . TYR B 39  ? 0.4355 0.4677 0.6765 -0.0237 -0.0580 0.0013  39  TYR B CD2 
4541  C CE1 . TYR B 39  ? 0.4673 0.4704 0.6806 -0.0286 -0.0540 -0.0031 39  TYR B CE1 
4542  C CE2 . TYR B 39  ? 0.4261 0.4459 0.6626 -0.0228 -0.0510 0.0009  39  TYR B CE2 
4543  C CZ  . TYR B 39  ? 0.4276 0.4335 0.6508 -0.0250 -0.0491 -0.0012 39  TYR B CZ  
4544  O OH  . TYR B 39  ? 0.3900 0.3862 0.6106 -0.0232 -0.0425 -0.0012 39  TYR B OH  
4545  N N   . GLU B 40  ? 0.4999 0.5859 0.7611 -0.0442 -0.0861 -0.0031 40  GLU B N   
4546  C CA  . GLU B 40  ? 0.5739 0.6778 0.8410 -0.0463 -0.0953 -0.0028 40  GLU B CA  
4547  C C   . GLU B 40  ? 0.5651 0.6746 0.8348 -0.0588 -0.0983 -0.0068 40  GLU B C   
4548  O O   . GLU B 40  ? 0.5602 0.6777 0.8276 -0.0637 -0.1065 -0.0082 40  GLU B O   
4549  C CB  . GLU B 40  ? 0.6016 0.7275 0.8870 -0.0400 -0.0972 0.0008  40  GLU B CB  
4550  C CG  . GLU B 40  ? 0.6378 0.7609 0.9240 -0.0274 -0.0944 0.0050  40  GLU B CG  
4551  C CD  . GLU B 40  ? 0.6533 0.7967 0.9586 -0.0217 -0.0940 0.0077  40  GLU B CD  
4552  O OE1 . GLU B 40  ? 0.6392 0.7998 0.9576 -0.0280 -0.0957 0.0063  40  GLU B OE1 
4553  O OE2 . GLU B 40  ? 0.6595 0.8018 0.9670 -0.0114 -0.0916 0.0109  40  GLU B OE2 
4554  N N   . ASP B 41  ? 0.5778 0.6836 0.8526 -0.0640 -0.0918 -0.0084 41  ASP B N   
4555  C CA  . ASP B 41  ? 0.6305 0.7397 0.9083 -0.0764 -0.0931 -0.0118 41  ASP B CA  
4556  C C   . ASP B 41  ? 0.6716 0.7627 0.9305 -0.0838 -0.0957 -0.0162 41  ASP B C   
4557  O O   . ASP B 41  ? 0.6758 0.7474 0.9196 -0.0797 -0.0924 -0.0169 41  ASP B O   
4558  C CB  . ASP B 41  ? 0.6029 0.7094 0.8886 -0.0787 -0.0845 -0.0116 41  ASP B CB  
4559  C CG  . ASP B 41  ? 0.5879 0.7160 0.8939 -0.0753 -0.0826 -0.0085 41  ASP B CG  
4560  O OD1 . ASP B 41  ? 0.5446 0.6926 0.8611 -0.0709 -0.0882 -0.0063 41  ASP B OD1 
4561  O OD2 . ASP B 41  ? 0.5161 0.6413 0.8271 -0.0766 -0.0754 -0.0081 41  ASP B OD2 
4562  N N   . GLU B 42  ? 0.6694 0.7674 0.9293 -0.0951 -0.1015 -0.0194 42  GLU B N   
4563  C CA  . GLU B 42  ? 0.7169 0.7958 0.9595 -0.1042 -0.1024 -0.0245 42  GLU B CA  
4564  C C   . GLU B 42  ? 0.6865 0.7438 0.9219 -0.1037 -0.0925 -0.0254 42  GLU B C   
4565  O O   . GLU B 42  ? 0.6036 0.6653 0.8505 -0.1037 -0.0868 -0.0236 42  GLU B O   
4566  C CB  . GLU B 42  ? 0.7895 0.8817 1.0389 -0.1175 -0.1088 -0.0273 42  GLU B CB  
4567  C CG  . GLU B 42  ? 0.8575 0.9300 1.0895 -0.1289 -0.1102 -0.0331 42  GLU B CG  
4568  C CD  . GLU B 42  ? 0.9469 1.0289 1.1883 -0.1430 -0.1122 -0.0354 42  GLU B CD  
4569  O OE1 . GLU B 42  ? 0.9350 1.0414 1.1892 -0.1472 -0.1199 -0.0347 42  GLU B OE1 
4570  O OE2 . GLU B 42  ? 0.9784 1.0445 1.2152 -0.1495 -0.1061 -0.0374 42  GLU B OE2 
4571  N N   . ARG B 43  ? 0.6913 0.7258 0.9075 -0.1026 -0.0904 -0.0281 43  ARG B N   
4572  C CA  . ARG B 43  ? 0.7612 0.7765 0.9707 -0.0993 -0.0811 -0.0283 43  ARG B CA  
4573  C C   . ARG B 43  ? 0.6646 0.6700 0.8718 -0.1101 -0.0786 -0.0316 43  ARG B C   
4574  O O   . ARG B 43  ? 0.6080 0.6072 0.8058 -0.1195 -0.0833 -0.0359 43  ARG B O   
4575  C CB  . ARG B 43  ? 0.8978 0.8954 1.0893 -0.0927 -0.0795 -0.0294 43  ARG B CB  
4576  C CG  . ARG B 43  ? 0.9793 0.9647 1.1681 -0.0838 -0.0706 -0.0273 43  ARG B CG  
4577  C CD  . ARG B 43  ? 1.1327 1.0981 1.3123 -0.0874 -0.0643 -0.0303 43  ARG B CD  
4578  N NE  . ARG B 43  ? 1.1644 1.1135 1.3265 -0.0940 -0.0666 -0.0357 43  ARG B NE  
4579  C CZ  . ARG B 43  ? 1.0718 1.0065 1.2266 -0.1018 -0.0648 -0.0394 43  ARG B CZ  
4580  N NH1 . ARG B 43  ? 1.0561 0.9876 1.2179 -0.1029 -0.0592 -0.0380 43  ARG B NH1 
4581  N NH2 . ARG B 43  ? 0.9522 0.8740 1.0913 -0.1083 -0.0682 -0.0445 43  ARG B NH2 
4582  N N   . LYS B 44  ? 0.6056 0.6093 0.8208 -0.1091 -0.0715 -0.0296 44  LYS B N   
4583  C CA  . LYS B 44  ? 0.6021 0.5947 0.8147 -0.1186 -0.0682 -0.0318 44  LYS B CA  
4584  C C   . LYS B 44  ? 0.5633 0.5365 0.7687 -0.1126 -0.0592 -0.0310 44  LYS B C   
4585  O O   . LYS B 44  ? 0.4737 0.4492 0.6833 -0.1022 -0.0552 -0.0276 44  LYS B O   
4586  C CB  . LYS B 44  ? 0.6152 0.6281 0.8459 -0.1260 -0.0695 -0.0300 44  LYS B CB  
4587  C CG  . LYS B 44  ? 0.7056 0.7382 0.9437 -0.1336 -0.0788 -0.0313 44  LYS B CG  
4588  C CD  . LYS B 44  ? 0.8188 0.8650 1.0693 -0.1462 -0.0802 -0.0316 44  LYS B CD  
4589  C CE  . LYS B 44  ? 0.8817 0.9391 1.1482 -0.1437 -0.0734 -0.0274 44  LYS B CE  
4590  N NZ  . LYS B 44  ? 0.8266 0.9043 1.1075 -0.1323 -0.0735 -0.0232 44  LYS B NZ  
4591  N N   . ASP B 45  ? 0.5311 0.4844 0.7248 -0.1194 -0.0565 -0.0341 45  ASP B N   
4592  C CA  . ASP B 45  ? 0.4968 0.4300 0.6818 -0.1142 -0.0487 -0.0337 45  ASP B CA  
4593  C C   . ASP B 45  ? 0.4557 0.3966 0.6542 -0.1122 -0.0433 -0.0293 45  ASP B C   
4594  O O   . ASP B 45  ? 0.4464 0.3828 0.6449 -0.1029 -0.0379 -0.0268 45  ASP B O   
4595  C CB  . ASP B 45  ? 0.5167 0.4255 0.6845 -0.1217 -0.0478 -0.0383 45  ASP B CB  
4596  C CG  . ASP B 45  ? 0.5076 0.3999 0.6567 -0.1194 -0.0496 -0.0427 45  ASP B CG  
4597  O OD1 . ASP B 45  ? 0.5164 0.4119 0.6635 -0.1099 -0.0494 -0.0417 45  ASP B OD1 
4598  O OD2 . ASP B 45  ? 0.4999 0.3758 0.6358 -0.1274 -0.0509 -0.0472 45  ASP B OD2 
4599  N N   . GLU B 46  ? 0.4633 0.4156 0.6726 -0.1213 -0.0444 -0.0285 46  GLU B N   
4600  C CA  . GLU B 46  ? 0.4558 0.4184 0.6784 -0.1198 -0.0395 -0.0242 46  GLU B CA  
4601  C C   . GLU B 46  ? 0.4386 0.3807 0.6526 -0.1180 -0.0322 -0.0233 46  GLU B C   
4602  O O   . GLU B 46  ? 0.4280 0.3728 0.6476 -0.1106 -0.0272 -0.0197 46  GLU B O   
4603  C CB  . GLU B 46  ? 0.4516 0.4319 0.6861 -0.1090 -0.0393 -0.0208 46  GLU B CB  
4604  C CG  . GLU B 46  ? 0.4759 0.4781 0.7207 -0.1103 -0.0464 -0.0208 46  GLU B CG  
4605  C CD  . GLU B 46  ? 0.4986 0.5242 0.7626 -0.1111 -0.0458 -0.0176 46  GLU B CD  
4606  O OE1 . GLU B 46  ? 0.6062 0.6362 0.8766 -0.1195 -0.0437 -0.0171 46  GLU B OE1 
4607  O OE2 . GLU B 46  ? 0.5440 0.5829 0.8160 -0.1026 -0.0470 -0.0154 46  GLU B OE2 
4608  N N   . LEU B 47  ? 0.4355 0.3570 0.6357 -0.1253 -0.0317 -0.0264 47  LEU B N   
4609  C CA  . LEU B 47  ? 0.4419 0.3405 0.6305 -0.1217 -0.0254 -0.0258 47  LEU B CA  
4610  C C   . LEU B 47  ? 0.4399 0.3424 0.6371 -0.1235 -0.0204 -0.0216 47  LEU B C   
4611  O O   . LEU B 47  ? 0.4357 0.3297 0.6300 -0.1156 -0.0151 -0.0191 47  LEU B O   
4612  C CB  . LEU B 47  ? 0.4664 0.3407 0.6371 -0.1289 -0.0263 -0.0304 47  LEU B CB  
4613  C CG  . LEU B 47  ? 0.4638 0.3314 0.6232 -0.1258 -0.0303 -0.0348 47  LEU B CG  
4614  C CD1 . LEU B 47  ? 0.4857 0.3285 0.6269 -0.1333 -0.0308 -0.0396 47  LEU B CD1 
4615  C CD2 . LEU B 47  ? 0.4606 0.3250 0.6166 -0.1114 -0.0270 -0.0335 47  LEU B CD2 
4616  N N   . GLU B 48  ? 0.4657 0.3823 0.6736 -0.1337 -0.0220 -0.0208 48  GLU B N   
4617  C CA  . GLU B 48  ? 0.4849 0.4047 0.6997 -0.1369 -0.0169 -0.0169 48  GLU B CA  
4618  C C   . GLU B 48  ? 0.4393 0.3741 0.6654 -0.1258 -0.0137 -0.0129 48  GLU B C   
4619  O O   . GLU B 48  ? 0.4221 0.3488 0.6458 -0.1217 -0.0082 -0.0099 48  GLU B O   
4620  C CB  . GLU B 48  ? 0.5235 0.4570 0.7483 -0.1507 -0.0186 -0.0167 48  GLU B CB  
4621  C CG  . GLU B 48  ? 0.6055 0.5211 0.8180 -0.1639 -0.0206 -0.0203 48  GLU B CG  
4622  C CD  . GLU B 48  ? 0.6888 0.5712 0.8813 -0.1621 -0.0164 -0.0212 48  GLU B CD  
4623  O OE1 . GLU B 48  ? 0.7312 0.6048 0.9219 -0.1599 -0.0103 -0.0174 48  GLU B OE1 
4624  O OE2 . GLU B 48  ? 0.7126 0.5774 0.8905 -0.1621 -0.0192 -0.0256 48  GLU B OE2 
4625  N N   . LEU B 49  ? 0.4264 0.3816 0.6636 -0.1208 -0.0174 -0.0128 49  LEU B N   
4626  C CA  . LEU B 49  ? 0.4103 0.3787 0.6573 -0.1103 -0.0148 -0.0095 49  LEU B CA  
4627  C C   . LEU B 49  ? 0.3783 0.3314 0.6150 -0.0995 -0.0122 -0.0093 49  LEU B C   
4628  O O   . LEU B 49  ? 0.3611 0.3156 0.6007 -0.0923 -0.0081 -0.0064 49  LEU B O   
4629  C CB  . LEU B 49  ? 0.3901 0.3827 0.6507 -0.1076 -0.0195 -0.0095 49  LEU B CB  
4630  C CG  . LEU B 49  ? 0.3840 0.3975 0.6588 -0.1165 -0.0215 -0.0089 49  LEU B CG  
4631  C CD1 . LEU B 49  ? 0.3469 0.3844 0.6350 -0.1126 -0.0265 -0.0087 49  LEU B CD1 
4632  C CD2 . LEU B 49  ? 0.3880 0.4062 0.6697 -0.1186 -0.0151 -0.0055 49  LEU B CD2 
4633  N N   . MET B 50  ? 0.4043 0.3430 0.6287 -0.0983 -0.0145 -0.0125 50  MET B N   
4634  C CA  . MET B 50  ? 0.3859 0.3115 0.6013 -0.0882 -0.0118 -0.0123 50  MET B CA  
4635  C C   . MET B 50  ? 0.3770 0.2862 0.5851 -0.0869 -0.0061 -0.0103 50  MET B C   
4636  O O   . MET B 50  ? 0.3505 0.2581 0.5585 -0.0779 -0.0028 -0.0081 50  MET B O   
4637  C CB  . MET B 50  ? 0.4110 0.3246 0.6141 -0.0872 -0.0148 -0.0162 50  MET B CB  
4638  C CG  . MET B 50  ? 0.3918 0.3187 0.5995 -0.0826 -0.0190 -0.0168 50  MET B CG  
4639  S SD  . MET B 50  ? 0.4125 0.3232 0.6036 -0.0794 -0.0207 -0.0209 50  MET B SD  
4640  C CE  . MET B 50  ? 0.4243 0.3277 0.6130 -0.0674 -0.0143 -0.0182 50  MET B CE  
4641  N N   . LYS B 51  ? 0.4000 0.2970 0.6017 -0.0959 -0.0051 -0.0110 51  LYS B N   
4642  C CA  . LYS B 51  ? 0.4318 0.3122 0.6258 -0.0953 0.0001  -0.0087 51  LYS B CA  
4643  C C   . LYS B 51  ? 0.3960 0.2887 0.6002 -0.0919 0.0037  -0.0041 51  LYS B C   
4644  O O   . LYS B 51  ? 0.3909 0.2755 0.5908 -0.0847 0.0074  -0.0016 51  LYS B O   
4645  C CB  . LYS B 51  ? 0.4863 0.3524 0.6725 -0.1073 0.0004  -0.0099 51  LYS B CB  
4646  C CG  . LYS B 51  ? 0.5390 0.3841 0.7095 -0.1099 -0.0016 -0.0145 51  LYS B CG  
4647  C CD  . LYS B 51  ? 0.5878 0.4210 0.7515 -0.1239 -0.0026 -0.0165 51  LYS B CD  
4648  C CE  . LYS B 51  ? 0.6376 0.4476 0.7839 -0.1251 -0.0041 -0.0213 51  LYS B CE  
4649  N NZ  . LYS B 51  ? 0.6850 0.4927 0.8288 -0.1400 -0.0080 -0.0246 51  LYS B NZ  
4650  N N   . PHE B 52  ? 0.3820 0.2943 0.5994 -0.0975 0.0025  -0.0031 52  PHE B N   
4651  C CA  . PHE B 52  ? 0.3650 0.2905 0.5923 -0.0945 0.0060  0.0008  52  PHE B CA  
4652  C C   . PHE B 52  ? 0.3359 0.2667 0.5657 -0.0823 0.0065  0.0017  52  PHE B C   
4653  O O   . PHE B 52  ? 0.3107 0.2373 0.5384 -0.0769 0.0103  0.0045  52  PHE B O   
4654  C CB  . PHE B 52  ? 0.3695 0.3171 0.6112 -0.1016 0.0040  0.0008  52  PHE B CB  
4655  C CG  . PHE B 52  ? 0.3622 0.3273 0.6158 -0.0977 0.0071  0.0040  52  PHE B CG  
4656  C CD1 . PHE B 52  ? 0.3860 0.3500 0.6401 -0.1017 0.0122  0.0071  52  PHE B CD1 
4657  C CD2 . PHE B 52  ? 0.3396 0.3221 0.6034 -0.0906 0.0050  0.0037  52  PHE B CD2 
4658  C CE1 . PHE B 52  ? 0.3952 0.3751 0.6592 -0.0982 0.0153  0.0097  52  PHE B CE1 
4659  C CE2 . PHE B 52  ? 0.3368 0.3344 0.6107 -0.0870 0.0080  0.0061  52  PHE B CE2 
4660  C CZ  . PHE B 52  ? 0.3685 0.3651 0.6425 -0.0906 0.0132  0.0090  52  PHE B CZ  
4661  N N   . ASP B 53  ? 0.3288 0.2683 0.5623 -0.0785 0.0024  -0.0006 53  ASP B N   
4662  C CA  . ASP B 53  ? 0.3364 0.2821 0.5729 -0.0681 0.0024  0.0001  53  ASP B CA  
4663  C C   . ASP B 53  ? 0.3490 0.2783 0.5747 -0.0612 0.0050  0.0006  53  ASP B C   
4664  O O   . ASP B 53  ? 0.3526 0.2844 0.5803 -0.0545 0.0074  0.0029  53  ASP B O   
4665  C CB  . ASP B 53  ? 0.3116 0.2662 0.5514 -0.0661 -0.0024 -0.0022 53  ASP B CB  
4666  C CG  . ASP B 53  ? 0.2985 0.2728 0.5508 -0.0701 -0.0056 -0.0023 53  ASP B CG  
4667  O OD1 . ASP B 53  ? 0.2691 0.2540 0.5302 -0.0722 -0.0033 -0.0002 53  ASP B OD1 
4668  O OD2 . ASP B 53  ? 0.2871 0.2663 0.5401 -0.0708 -0.0103 -0.0043 53  ASP B OD2 
4669  N N   . LEU B 54  ? 0.3747 0.2877 0.5891 -0.0626 0.0043  -0.0017 54  LEU B N   
4670  C CA  . LEU B 54  ? 0.4103 0.3092 0.6151 -0.0551 0.0067  -0.0014 54  LEU B CA  
4671  C C   . LEU B 54  ? 0.4030 0.2933 0.6043 -0.0537 0.0109  0.0019  54  LEU B C   
4672  O O   . LEU B 54  ? 0.4183 0.3076 0.6187 -0.0456 0.0129  0.0038  54  LEU B O   
4673  C CB  . LEU B 54  ? 0.4527 0.3356 0.6454 -0.0563 0.0055  -0.0049 54  LEU B CB  
4674  C CG  . LEU B 54  ? 0.4513 0.3400 0.6443 -0.0566 0.0014  -0.0082 54  LEU B CG  
4675  C CD1 . LEU B 54  ? 0.5105 0.3801 0.6892 -0.0579 0.0012  -0.0117 54  LEU B CD1 
4676  C CD2 . LEU B 54  ? 0.4159 0.3149 0.6138 -0.0482 0.0010  -0.0075 54  LEU B CD2 
4677  N N   . GLU B 55  ? 0.3948 0.2799 0.5944 -0.0617 0.0122  0.0029  55  GLU B N   
4678  C CA  . GLU B 55  ? 0.4061 0.2850 0.6030 -0.0609 0.0161  0.0068  55  GLU B CA  
4679  C C   . GLU B 55  ? 0.3993 0.2946 0.6061 -0.0559 0.0174  0.0095  55  GLU B C   
4680  O O   . GLU B 55  ? 0.4472 0.3379 0.6505 -0.0498 0.0198  0.0122  55  GLU B O   
4681  C CB  . GLU B 55  ? 0.4261 0.2991 0.6207 -0.0719 0.0173  0.0075  55  GLU B CB  
4682  C CG  . GLU B 55  ? 0.4796 0.3410 0.6675 -0.0717 0.0217  0.0117  55  GLU B CG  
4683  C CD  . GLU B 55  ? 0.5261 0.3691 0.7019 -0.0629 0.0233  0.0129  55  GLU B CD  
4684  O OE1 . GLU B 55  ? 0.5349 0.3642 0.7020 -0.0611 0.0221  0.0099  55  GLU B OE1 
4685  O OE2 . GLU B 55  ? 0.5043 0.3473 0.6793 -0.0576 0.0259  0.0167  55  GLU B OE2 
4686  N N   . ASN B 56  ? 0.3473 0.2613 0.5660 -0.0580 0.0157  0.0088  56  ASN B N   
4687  C CA  . ASN B 56  ? 0.3294 0.2569 0.5559 -0.0531 0.0171  0.0110  56  ASN B CA  
4688  C C   . ASN B 56  ? 0.3107 0.2377 0.5356 -0.0434 0.0165  0.0108  56  ASN B C   
4689  O O   . ASN B 56  ? 0.2990 0.2286 0.5246 -0.0384 0.0184  0.0130  56  ASN B O   
4690  C CB  . ASN B 56  ? 0.3234 0.2704 0.5625 -0.0555 0.0155  0.0101  56  ASN B CB  
4691  C CG  . ASN B 56  ? 0.3387 0.2913 0.5824 -0.0649 0.0165  0.0107  56  ASN B CG  
4692  O OD1 . ASN B 56  ? 0.3552 0.3002 0.5944 -0.0690 0.0199  0.0131  56  ASN B OD1 
4693  N ND2 . ASN B 56  ? 0.3324 0.2985 0.5851 -0.0687 0.0135  0.0088  56  ASN B ND2 
4694  N N   . ILE B 57  ? 0.3059 0.2311 0.5293 -0.0413 0.0137  0.0081  57  ILE B N   
4695  C CA  . ILE B 57  ? 0.3108 0.2384 0.5344 -0.0332 0.0130  0.0077  57  ILE B CA  
4696  C C   . ILE B 57  ? 0.3365 0.2520 0.5518 -0.0277 0.0153  0.0094  57  ILE B C   
4697  O O   . ILE B 57  ? 0.2950 0.2150 0.5122 -0.0215 0.0159  0.0106  57  ILE B O   
4698  C CB  . ILE B 57  ? 0.3096 0.2385 0.5331 -0.0333 0.0098  0.0046  57  ILE B CB  
4699  C CG1 . ILE B 57  ? 0.3027 0.2472 0.5362 -0.0359 0.0073  0.0040  57  ILE B CG1 
4700  C CG2 . ILE B 57  ? 0.3119 0.2385 0.5323 -0.0259 0.0098  0.0041  57  ILE B CG2 
4701  C CD1 . ILE B 57  ? 0.3010 0.2479 0.5343 -0.0366 0.0036  0.0014  57  ILE B CD1 
4702  N N   . LYS B 58  ? 0.3485 0.2488 0.5549 -0.0304 0.0166  0.0096  58  LYS B N   
4703  C CA  . LYS B 58  ? 0.3822 0.2701 0.5803 -0.0248 0.0188  0.0116  58  LYS B CA  
4704  C C   . LYS B 58  ? 0.3857 0.2772 0.5855 -0.0235 0.0208  0.0155  58  LYS B C   
4705  O O   . LYS B 58  ? 0.3723 0.2644 0.5709 -0.0163 0.0214  0.0172  58  LYS B O   
4706  C CB  . LYS B 58  ? 0.4087 0.2774 0.5956 -0.0281 0.0198  0.0109  58  LYS B CB  
4707  C CG  . LYS B 58  ? 0.4144 0.2759 0.5961 -0.0269 0.0184  0.0071  58  LYS B CG  
4708  C CD  . LYS B 58  ? 0.4552 0.2991 0.6266 -0.0334 0.0186  0.0051  58  LYS B CD  
4709  C CE  . LYS B 58  ? 0.4787 0.3022 0.6380 -0.0304 0.0215  0.0069  58  LYS B CE  
4710  N NZ  . LYS B 58  ? 0.4849 0.2912 0.6342 -0.0378 0.0214  0.0044  58  LYS B NZ  
4711  N N   . GLU B 59  ? 0.3718 0.2673 0.5746 -0.0304 0.0218  0.0166  59  GLU B N   
4712  C CA  . GLU B 59  ? 0.3556 0.2547 0.5592 -0.0301 0.0241  0.0201  59  GLU B CA  
4713  C C   . GLU B 59  ? 0.3471 0.2613 0.5585 -0.0249 0.0234  0.0202  59  GLU B C   
4714  O O   . GLU B 59  ? 0.3560 0.2715 0.5656 -0.0214 0.0247  0.0228  59  GLU B O   
4715  C CB  . GLU B 59  ? 0.3707 0.2709 0.5759 -0.0393 0.0259  0.0210  59  GLU B CB  
4716  C CG  . GLU B 59  ? 0.4298 0.3109 0.6243 -0.0441 0.0273  0.0219  59  GLU B CG  
4717  C CD  . GLU B 59  ? 0.4841 0.3649 0.6795 -0.0548 0.0292  0.0228  59  GLU B CD  
4718  O OE1 . GLU B 59  ? 0.4970 0.3934 0.7016 -0.0579 0.0301  0.0234  59  GLU B OE1 
4719  O OE2 . GLU B 59  ? 0.5355 0.4007 0.7225 -0.0605 0.0299  0.0228  59  GLU B OE2 
4720  N N   . GLY B 60  ? 0.3351 0.2601 0.5541 -0.0245 0.0210  0.0174  60  GLY B N   
4721  C CA  . GLY B 60  ? 0.3232 0.2605 0.5486 -0.0199 0.0202  0.0170  60  GLY B CA  
4722  C C   . GLY B 60  ? 0.3081 0.2436 0.5311 -0.0128 0.0190  0.0169  60  GLY B C   
4723  O O   . GLY B 60  ? 0.2764 0.2211 0.5041 -0.0097 0.0181  0.0165  60  GLY B O   
4724  N N   . GLY B 61  ? 0.3125 0.2362 0.5283 -0.0103 0.0193  0.0172  61  GLY B N   
4725  C CA  . GLY B 61  ? 0.3058 0.2283 0.5193 -0.0031 0.0189  0.0179  61  GLY B CA  
4726  C C   . GLY B 61  ? 0.3282 0.2529 0.5436 -0.0005 0.0175  0.0153  61  GLY B C   
4727  O O   . GLY B 61  ? 0.3755 0.3028 0.5912 0.0052  0.0172  0.0157  61  GLY B O   
4728  N N   . TYR B 62  ? 0.3379 0.2621 0.5544 -0.0047 0.0165  0.0127  62  TYR B N   
4729  C CA  . TYR B 62  ? 0.3083 0.2340 0.5253 -0.0030 0.0153  0.0102  62  TYR B CA  
4730  C C   . TYR B 62  ? 0.3159 0.2286 0.5245 -0.0006 0.0165  0.0094  62  TYR B C   
4731  O O   . TYR B 62  ? 0.3170 0.2181 0.5191 -0.0027 0.0176  0.0099  62  TYR B O   
4732  C CB  . TYR B 62  ? 0.2868 0.2180 0.5081 -0.0085 0.0134  0.0082  62  TYR B CB  
4733  C CG  . TYR B 62  ? 0.2740 0.2173 0.5032 -0.0095 0.0127  0.0091  62  TYR B CG  
4734  C CD1 . TYR B 62  ? 0.2819 0.2336 0.5156 -0.0064 0.0118  0.0088  62  TYR B CD1 
4735  C CD2 . TYR B 62  ? 0.2709 0.2170 0.5028 -0.0136 0.0134  0.0101  62  TYR B CD2 
4736  C CE1 . TYR B 62  ? 0.2701 0.2308 0.5097 -0.0068 0.0114  0.0092  62  TYR B CE1 
4737  C CE2 . TYR B 62  ? 0.2814 0.2379 0.5199 -0.0136 0.0133  0.0105  62  TYR B CE2 
4738  C CZ  . TYR B 62  ? 0.2718 0.2350 0.5138 -0.0100 0.0122  0.0100  62  TYR B CZ  
4739  O OH  . TYR B 62  ? 0.2916 0.2631 0.5386 -0.0095 0.0123  0.0102  62  TYR B OH  
4740  N N   . ASN B 63  ? 0.3000 0.2140 0.5079 0.0038  0.0166  0.0080  63  ASN B N   
4741  C CA  . ASN B 63  ? 0.3195 0.2215 0.5190 0.0067  0.0181  0.0065  63  ASN B CA  
4742  C C   . ASN B 63  ? 0.3186 0.2200 0.5163 0.0037  0.0169  0.0032  63  ASN B C   
4743  O O   . ASN B 63  ? 0.3391 0.2295 0.5286 0.0049  0.0180  0.0011  63  ASN B O   
4744  C CB  . ASN B 63  ? 0.3188 0.2220 0.5178 0.0151  0.0199  0.0080  63  ASN B CB  
4745  C CG  . ASN B 63  ? 0.3189 0.2361 0.5251 0.0179  0.0195  0.0079  63  ASN B CG  
4746  O OD1 . ASN B 63  ? 0.2874 0.2113 0.4973 0.0145  0.0181  0.0064  63  ASN B OD1 
4747  N ND2 . ASN B 63  ? 0.2988 0.2206 0.5070 0.0243  0.0206  0.0096  63  ASN B ND2 
4748  N N   . THR B 64  ? 0.2977 0.2101 0.5021 0.0002  0.0147  0.0027  64  THR B N   
4749  C CA  . THR B 64  ? 0.2790 0.1929 0.4820 -0.0019 0.0131  0.0002  64  THR B CA  
4750  C C   . THR B 64  ? 0.2678 0.1892 0.4764 -0.0078 0.0101  -0.0001 64  THR B C   
4751  O O   . THR B 64  ? 0.2598 0.1898 0.4757 -0.0084 0.0096  0.0018  64  THR B O   
4752  C CB  . THR B 64  ? 0.2636 0.1855 0.4695 0.0027  0.0138  0.0005  64  THR B CB  
4753  O OG1 . THR B 64  ? 0.2788 0.1954 0.4806 0.0086  0.0168  0.0007  64  THR B OG1 
4754  C CG2 . THR B 64  ? 0.2644 0.1866 0.4673 0.0008  0.0125  -0.0018 64  THR B CG2 
4755  N N   . ILE B 65  ? 0.2688 0.1878 0.4739 -0.0117 0.0079  -0.0025 65  ILE B N   
4756  C CA  . ILE B 65  ? 0.2640 0.1926 0.4750 -0.0157 0.0045  -0.0027 65  ILE B CA  
4757  C C   . ILE B 65  ? 0.2678 0.1998 0.4773 -0.0138 0.0032  -0.0036 65  ILE B C   
4758  O O   . ILE B 65  ? 0.2870 0.2118 0.4887 -0.0118 0.0044  -0.0052 65  ILE B O   
4759  C CB  . ILE B 65  ? 0.2661 0.1911 0.4751 -0.0227 0.0022  -0.0044 65  ILE B CB  
4760  C CG1 . ILE B 65  ? 0.2719 0.1837 0.4696 -0.0241 0.0021  -0.0074 65  ILE B CG1 
4761  C CG2 . ILE B 65  ? 0.2744 0.1993 0.4872 -0.0257 0.0035  -0.0027 65  ILE B CG2 
4762  C CD1 . ILE B 65  ? 0.2849 0.1934 0.4798 -0.0321 -0.0010 -0.0096 65  ILE B CD1 
4763  N N   . ARG B 66  ? 0.2665 0.2088 0.4826 -0.0145 0.0007  -0.0026 66  ARG B N   
4764  C CA  . ARG B 66  ? 0.2694 0.2144 0.4834 -0.0132 -0.0010 -0.0029 66  ARG B CA  
4765  C C   . ARG B 66  ? 0.2743 0.2240 0.4898 -0.0173 -0.0055 -0.0037 66  ARG B C   
4766  O O   . ARG B 66  ? 0.2729 0.2301 0.4962 -0.0192 -0.0071 -0.0027 66  ARG B O   
4767  C CB  . ARG B 66  ? 0.2761 0.2279 0.4956 -0.0093 0.0004  -0.0006 66  ARG B CB  
4768  C CG  . ARG B 66  ? 0.2714 0.2270 0.4903 -0.0082 -0.0012 0.0001  66  ARG B CG  
4769  C CD  . ARG B 66  ? 0.2974 0.2601 0.5218 -0.0096 -0.0049 0.0010  66  ARG B CD  
4770  N NE  . ARG B 66  ? 0.3209 0.2860 0.5451 -0.0072 -0.0054 0.0026  66  ARG B NE  
4771  C CZ  . ARG B 66  ? 0.3274 0.2916 0.5467 -0.0073 -0.0078 0.0028  66  ARG B CZ  
4772  N NH1 . ARG B 66  ? 0.3482 0.3095 0.5618 -0.0097 -0.0102 0.0011  66  ARG B NH1 
4773  N NH2 . ARG B 66  ? 0.3537 0.3191 0.5728 -0.0052 -0.0081 0.0048  66  ARG B NH2 
4774  N N   . THR B 67  ? 0.2834 0.2298 0.4917 -0.0182 -0.0077 -0.0052 67  THR B N   
4775  C CA  . THR B 67  ? 0.3012 0.2526 0.5106 -0.0222 -0.0127 -0.0060 67  THR B CA  
4776  C C   . THR B 67  ? 0.3107 0.2650 0.5169 -0.0199 -0.0152 -0.0051 67  THR B C   
4777  O O   . THR B 67  ? 0.2886 0.2392 0.4902 -0.0163 -0.0125 -0.0044 67  THR B O   
4778  C CB  . THR B 67  ? 0.3083 0.2514 0.5100 -0.0272 -0.0141 -0.0091 67  THR B CB  
4779  O OG1 . THR B 67  ? 0.3039 0.2382 0.4943 -0.0251 -0.0129 -0.0107 67  THR B OG1 
4780  C CG2 . THR B 67  ? 0.3196 0.2567 0.5221 -0.0292 -0.0111 -0.0096 67  THR B CG2 
4781  N N   . TRP B 68  ? 0.3051 0.2657 0.5132 -0.0225 -0.0204 -0.0052 68  TRP B N   
4782  C CA  . TRP B 68  ? 0.3430 0.3069 0.5483 -0.0203 -0.0236 -0.0038 68  TRP B CA  
4783  C C   . TRP B 68  ? 0.3722 0.3321 0.5674 -0.0236 -0.0277 -0.0061 68  TRP B C   
4784  O O   . TRP B 68  ? 0.4233 0.3821 0.6118 -0.0216 -0.0294 -0.0052 68  TRP B O   
4785  C CB  . TRP B 68  ? 0.3071 0.2828 0.5231 -0.0188 -0.0267 -0.0013 68  TRP B CB  
4786  C CG  . TRP B 68  ? 0.2881 0.2659 0.5109 -0.0146 -0.0229 0.0009  68  TRP B CG  
4787  C CD1 . TRP B 68  ? 0.2873 0.2643 0.5089 -0.0104 -0.0219 0.0032  68  TRP B CD1 
4788  C CD2 . TRP B 68  ? 0.3002 0.2797 0.5302 -0.0148 -0.0194 0.0009  68  TRP B CD2 
4789  N NE1 . TRP B 68  ? 0.2732 0.2515 0.5011 -0.0082 -0.0184 0.0043  68  TRP B NE1 
4790  C CE2 . TRP B 68  ? 0.2706 0.2507 0.5034 -0.0106 -0.0167 0.0030  68  TRP B CE2 
4791  C CE3 . TRP B 68  ? 0.3018 0.2817 0.5352 -0.0185 -0.0182 -0.0004 68  TRP B CE3 
4792  C CZ2 . TRP B 68  ? 0.2625 0.2440 0.5011 -0.0097 -0.0133 0.0034  68  TRP B CZ2 
4793  C CZ3 . TRP B 68  ? 0.2805 0.2615 0.5195 -0.0172 -0.0144 0.0004  68  TRP B CZ3 
4794  C CH2 . TRP B 68  ? 0.2605 0.2425 0.5019 -0.0127 -0.0121 0.0022  68  TRP B CH2 
4795  N N   . SER B 69  ? 0.3725 0.3302 0.5659 -0.0291 -0.0295 -0.0091 69  SER B N   
4796  C CA  . SER B 69  ? 0.3554 0.3076 0.5375 -0.0328 -0.0333 -0.0120 69  SER B CA  
4797  C C   . SER B 69  ? 0.3447 0.2851 0.5194 -0.0370 -0.0310 -0.0158 69  SER B C   
4798  O O   . SER B 69  ? 0.3374 0.2771 0.5179 -0.0391 -0.0288 -0.0161 69  SER B O   
4799  C CB  . SER B 69  ? 0.3394 0.3020 0.5254 -0.0364 -0.0406 -0.0119 69  SER B CB  
4800  O OG  . SER B 69  ? 0.3481 0.3204 0.5474 -0.0390 -0.0411 -0.0112 69  SER B OG  
4801  N N   . GLN B 70  ? 0.3723 0.3035 0.5332 -0.0384 -0.0323 -0.0187 70  GLN B N   
4802  C CA  . GLN B 70  ? 0.4035 0.3197 0.5531 -0.0405 -0.0292 -0.0226 70  GLN B CA  
4803  C C   . GLN B 70  ? 0.3983 0.3130 0.5504 -0.0481 -0.0318 -0.0250 70  GLN B C   
4804  O O   . GLN B 70  ? 0.4222 0.3460 0.5786 -0.0533 -0.0378 -0.0252 70  GLN B O   
4805  C CB  . GLN B 70  ? 0.4060 0.3136 0.5395 -0.0408 -0.0308 -0.0254 70  GLN B CB  
4806  C CG  . GLN B 70  ? 0.4082 0.3239 0.5403 -0.0450 -0.0389 -0.0257 70  GLN B CG  
4807  C CD  . GLN B 70  ? 0.3861 0.3098 0.5191 -0.0398 -0.0403 -0.0219 70  GLN B CD  
4808  O OE1 . GLN B 70  ? 0.3563 0.2863 0.4987 -0.0348 -0.0374 -0.0180 70  GLN B OE1 
4809  N NE2 . GLN B 70  ? 0.3994 0.3211 0.5208 -0.0409 -0.0446 -0.0231 70  GLN B NE2 
4810  N N   . TYR B 71  ? 0.4057 0.3088 0.5546 -0.0487 -0.0272 -0.0265 71  TYR B N   
4811  C CA  . TYR B 71  ? 0.4005 0.2975 0.5480 -0.0566 -0.0287 -0.0292 71  TYR B CA  
4812  C C   . TYR B 71  ? 0.4069 0.2900 0.5379 -0.0615 -0.0311 -0.0344 71  TYR B C   
4813  O O   . TYR B 71  ? 0.4307 0.3041 0.5492 -0.0574 -0.0292 -0.0363 71  TYR B O   
4814  C CB  . TYR B 71  ? 0.4008 0.2885 0.5496 -0.0548 -0.0226 -0.0285 71  TYR B CB  
4815  C CG  . TYR B 71  ? 0.3754 0.2750 0.5396 -0.0525 -0.0205 -0.0241 71  TYR B CG  
4816  C CD1 . TYR B 71  ? 0.3763 0.2923 0.5536 -0.0560 -0.0243 -0.0220 71  TYR B CD1 
4817  C CD2 . TYR B 71  ? 0.3654 0.2598 0.5307 -0.0465 -0.0147 -0.0222 71  TYR B CD2 
4818  C CE1 . TYR B 71  ? 0.3479 0.2734 0.5378 -0.0536 -0.0218 -0.0184 71  TYR B CE1 
4819  C CE2 . TYR B 71  ? 0.3423 0.2463 0.5200 -0.0445 -0.0128 -0.0185 71  TYR B CE2 
4820  C CZ  . TYR B 71  ? 0.3234 0.2423 0.5129 -0.0481 -0.0161 -0.0167 71  TYR B CZ  
4821  O OH  . TYR B 71  ? 0.3116 0.2378 0.5112 -0.0455 -0.0133 -0.0134 71  TYR B OH  
4822  N N   . SER B 72  ? 0.4051 0.2875 0.5360 -0.0709 -0.0355 -0.0368 72  SER B N   
4823  C CA  . SER B 72  ? 0.4397 0.3058 0.5544 -0.0772 -0.0373 -0.0423 72  SER B CA  
4824  C C   . SER B 72  ? 0.4666 0.3119 0.5716 -0.0748 -0.0305 -0.0441 72  SER B C   
4825  O O   . SER B 72  ? 0.4581 0.3037 0.5708 -0.0701 -0.0254 -0.0408 72  SER B O   
4826  C CB  . SER B 72  ? 0.4330 0.3053 0.5519 -0.0887 -0.0437 -0.0440 72  SER B CB  
4827  O OG  . SER B 72  ? 0.4296 0.3018 0.5577 -0.0922 -0.0407 -0.0422 72  SER B OG  
4828  N N   . GLU B 73  ? 0.4744 0.3010 0.5616 -0.0777 -0.0305 -0.0494 73  GLU B N   
4829  C CA  . GLU B 73  ? 0.5043 0.3097 0.5811 -0.0751 -0.0244 -0.0513 73  GLU B CA  
4830  C C   . GLU B 73  ? 0.5228 0.3264 0.6079 -0.0804 -0.0232 -0.0494 73  GLU B C   
4831  O O   . GLU B 73  ? 0.5359 0.3320 0.6221 -0.0747 -0.0173 -0.0472 73  GLU B O   
4832  C CB  . GLU B 73  ? 0.5332 0.3175 0.5888 -0.0790 -0.0253 -0.0579 73  GLU B CB  
4833  C CG  . GLU B 73  ? 0.5353 0.2972 0.5792 -0.0729 -0.0179 -0.0596 73  GLU B CG  
4834  C CD  . GLU B 73  ? 0.5716 0.3124 0.5932 -0.0724 -0.0168 -0.0660 73  GLU B CD  
4835  O OE1 . GLU B 73  ? 0.5784 0.3213 0.5920 -0.0770 -0.0220 -0.0694 73  GLU B OE1 
4836  O OE2 . GLU B 73  ? 0.5774 0.2998 0.5899 -0.0664 -0.0105 -0.0672 73  GLU B OE2 
4837  N N   . ASN B 74  ? 0.5188 0.3294 0.6091 -0.0917 -0.0288 -0.0502 74  ASN B N   
4838  C CA  . ASN B 74  ? 0.4947 0.3035 0.5921 -0.0983 -0.0276 -0.0484 74  ASN B CA  
4839  C C   . ASN B 74  ? 0.4594 0.2821 0.5728 -0.0912 -0.0236 -0.0423 74  ASN B C   
4840  O O   . ASN B 74  ? 0.4470 0.2607 0.5610 -0.0903 -0.0190 -0.0403 74  ASN B O   
4841  C CB  . ASN B 74  ? 0.4910 0.3109 0.5949 -0.1114 -0.0344 -0.0496 74  ASN B CB  
4842  C CG  . ASN B 74  ? 0.5136 0.3160 0.6002 -0.1208 -0.0380 -0.0559 74  ASN B CG  
4843  O OD1 . ASN B 74  ? 0.5326 0.3120 0.6016 -0.1173 -0.0347 -0.0596 74  ASN B OD1 
4844  N ND2 . ASN B 74  ? 0.5168 0.3301 0.6082 -0.1325 -0.0449 -0.0576 74  ASN B ND2 
4845  N N   . GLN B 75  ? 0.4291 0.2725 0.5545 -0.0863 -0.0256 -0.0394 75  GLN B N   
4846  C CA  . GLN B 75  ? 0.4368 0.2930 0.5766 -0.0798 -0.0222 -0.0340 75  GLN B CA  
4847  C C   . GLN B 75  ? 0.4411 0.2854 0.5749 -0.0695 -0.0156 -0.0329 75  GLN B C   
4848  O O   . GLN B 75  ? 0.4194 0.2628 0.5586 -0.0666 -0.0116 -0.0298 75  GLN B O   
4849  C CB  . GLN B 75  ? 0.4494 0.3286 0.6025 -0.0769 -0.0257 -0.0313 75  GLN B CB  
4850  C CG  . GLN B 75  ? 0.4572 0.3520 0.6197 -0.0860 -0.0320 -0.0315 75  GLN B CG  
4851  C CD  . GLN B 75  ? 0.4520 0.3667 0.6247 -0.0817 -0.0358 -0.0291 75  GLN B CD  
4852  O OE1 . GLN B 75  ? 0.4302 0.3432 0.5962 -0.0761 -0.0366 -0.0297 75  GLN B OE1 
4853  N NE2 . GLN B 75  ? 0.4392 0.3724 0.6277 -0.0840 -0.0376 -0.0262 75  GLN B NE2 
4854  N N   . LEU B 76  ? 0.4743 0.3100 0.5967 -0.0638 -0.0145 -0.0355 76  LEU B N   
4855  C CA  . LEU B 76  ? 0.4724 0.2972 0.5886 -0.0541 -0.0083 -0.0349 76  LEU B CA  
4856  C C   . LEU B 76  ? 0.4858 0.2909 0.5936 -0.0550 -0.0045 -0.0358 76  LEU B C   
4857  O O   . LEU B 76  ? 0.5120 0.3141 0.6218 -0.0473 0.0004  -0.0331 76  LEU B O   
4858  C CB  . LEU B 76  ? 0.4842 0.3025 0.5883 -0.0489 -0.0074 -0.0380 76  LEU B CB  
4859  C CG  . LEU B 76  ? 0.5016 0.3368 0.6130 -0.0437 -0.0083 -0.0356 76  LEU B CG  
4860  C CD1 . LEU B 76  ? 0.5209 0.3468 0.6184 -0.0384 -0.0059 -0.0386 76  LEU B CD1 
4861  C CD2 . LEU B 76  ? 0.4777 0.3250 0.6027 -0.0369 -0.0050 -0.0305 76  LEU B CD2 
4862  N N   . LYS B 77  ? 0.4649 0.2562 0.5629 -0.0640 -0.0067 -0.0395 77  LYS B N   
4863  C CA  . LYS B 77  ? 0.4993 0.2692 0.5877 -0.0650 -0.0030 -0.0403 77  LYS B CA  
4864  C C   . LYS B 77  ? 0.4949 0.2719 0.5956 -0.0648 -0.0008 -0.0349 77  LYS B C   
4865  O O   . LYS B 77  ? 0.4935 0.2594 0.5907 -0.0587 0.0039  -0.0329 77  LYS B O   
4866  C CB  . LYS B 77  ? 0.5045 0.2573 0.5802 -0.0764 -0.0059 -0.0450 77  LYS B CB  
4867  C CG  . LYS B 77  ? 0.5290 0.2649 0.5863 -0.0752 -0.0062 -0.0511 77  LYS B CG  
4868  C CD  . LYS B 77  ? 0.5550 0.2737 0.5984 -0.0874 -0.0098 -0.0566 77  LYS B CD  
4869  C CE  . LYS B 77  ? 0.5682 0.2714 0.5929 -0.0855 -0.0101 -0.0628 77  LYS B CE  
4870  N NZ  . LYS B 77  ? 0.5859 0.2805 0.6003 -0.0987 -0.0160 -0.0682 77  LYS B NZ  
4871  N N   . LEU B 78  ? 0.4975 0.2942 0.6127 -0.0708 -0.0043 -0.0325 78  LEU B N   
4872  C CA  . LEU B 78  ? 0.4957 0.3003 0.6222 -0.0718 -0.0024 -0.0277 78  LEU B CA  
4873  C C   . LEU B 78  ? 0.4612 0.2728 0.5943 -0.0601 0.0016  -0.0237 78  LEU B C   
4874  O O   . LEU B 78  ? 0.4554 0.2599 0.5880 -0.0570 0.0054  -0.0207 78  LEU B O   
4875  C CB  . LEU B 78  ? 0.5152 0.3409 0.6558 -0.0799 -0.0070 -0.0266 78  LEU B CB  
4876  C CG  . LEU B 78  ? 0.5266 0.3600 0.6777 -0.0843 -0.0054 -0.0225 78  LEU B CG  
4877  C CD1 . LEU B 78  ? 0.5853 0.3981 0.7261 -0.0913 -0.0030 -0.0230 78  LEU B CD1 
4878  C CD2 . LEU B 78  ? 0.5423 0.3970 0.7064 -0.0919 -0.0101 -0.0224 78  LEU B CD2 
4879  N N   . VAL B 79  ? 0.4472 0.2723 0.5856 -0.0542 0.0004  -0.0236 79  VAL B N   
4880  C CA  . VAL B 79  ? 0.4197 0.2534 0.5648 -0.0439 0.0035  -0.0203 79  VAL B CA  
4881  C C   . VAL B 79  ? 0.4188 0.2351 0.5530 -0.0362 0.0083  -0.0206 79  VAL B C   
4882  O O   . VAL B 79  ? 0.4213 0.2379 0.5591 -0.0306 0.0114  -0.0172 79  VAL B O   
4883  C CB  . VAL B 79  ? 0.4069 0.2555 0.5576 -0.0396 0.0017  -0.0203 79  VAL B CB  
4884  C CG1 . VAL B 79  ? 0.3779 0.2356 0.5362 -0.0306 0.0048  -0.0168 79  VAL B CG1 
4885  C CG2 . VAL B 79  ? 0.4215 0.2863 0.5819 -0.0461 -0.0033 -0.0201 79  VAL B CG2 
4886  N N   . GLN B 80  ? 0.4327 0.2343 0.5535 -0.0355 0.0087  -0.0249 80  GLN B N   
4887  C CA  . GLN B 80  ? 0.4708 0.2552 0.5805 -0.0275 0.0134  -0.0256 80  GLN B CA  
4888  C C   . GLN B 80  ? 0.4814 0.2531 0.5884 -0.0281 0.0158  -0.0231 80  GLN B C   
4889  O O   . GLN B 80  ? 0.4759 0.2435 0.5823 -0.0191 0.0196  -0.0205 80  GLN B O   
4890  C CB  . GLN B 80  ? 0.4966 0.2633 0.5898 -0.0290 0.0133  -0.0313 80  GLN B CB  
4891  C CG  . GLN B 80  ? 0.4984 0.2483 0.5798 -0.0188 0.0186  -0.0326 80  GLN B CG  
4892  C CD  . GLN B 80  ? 0.4918 0.2550 0.5791 -0.0083 0.0213  -0.0311 80  GLN B CD  
4893  O OE1 . GLN B 80  ? 0.5125 0.2916 0.6064 -0.0092 0.0192  -0.0312 80  GLN B OE1 
4894  N NE2 . GLN B 80  ? 0.4980 0.2559 0.5837 0.0018  0.0260  -0.0293 80  GLN B NE2 
4895  N N   . GLU B 81  ? 0.4832 0.2482 0.5880 -0.0388 0.0136  -0.0237 81  GLU B N   
4896  C CA  . GLU B 81  ? 0.4938 0.2426 0.5928 -0.0409 0.0160  -0.0217 81  GLU B CA  
4897  C C   . GLU B 81  ? 0.4598 0.2224 0.5715 -0.0386 0.0172  -0.0158 81  GLU B C   
4898  O O   . GLU B 81  ? 0.4428 0.1942 0.5503 -0.0358 0.0201  -0.0128 81  GLU B O   
4899  C CB  . GLU B 81  ? 0.5114 0.2512 0.6056 -0.0548 0.0132  -0.0239 81  GLU B CB  
4900  C CG  . GLU B 81  ? 0.5405 0.2642 0.6201 -0.0596 0.0114  -0.0302 81  GLU B CG  
4901  C CD  . GLU B 81  ? 0.5745 0.3004 0.6549 -0.0748 0.0066  -0.0327 81  GLU B CD  
4902  O OE1 . GLU B 81  ? 0.5842 0.3267 0.6780 -0.0817 0.0046  -0.0297 81  GLU B OE1 
4903  O OE2 . GLU B 81  ? 0.6063 0.3174 0.6736 -0.0801 0.0047  -0.0381 81  GLU B OE2 
4904  N N   . SER B 82  ? 0.4329 0.2191 0.5593 -0.0397 0.0148  -0.0142 82  SER B N   
4905  C CA  . SER B 82  ? 0.4104 0.2108 0.5488 -0.0383 0.0156  -0.0093 82  SER B CA  
4906  C C   . SER B 82  ? 0.4060 0.2070 0.5452 -0.0265 0.0188  -0.0062 82  SER B C   
4907  O O   . SER B 82  ? 0.3746 0.1803 0.5190 -0.0253 0.0200  -0.0020 82  SER B O   
4908  C CB  . SER B 82  ? 0.3973 0.2213 0.5498 -0.0411 0.0124  -0.0090 82  SER B CB  
4909  O OG  . SER B 82  ? 0.3951 0.2289 0.5514 -0.0327 0.0124  -0.0092 82  SER B OG  
4910  N N   . GLY B 83  ? 0.4118 0.2104 0.5468 -0.0182 0.0199  -0.0081 83  GLY B N   
4911  C CA  . GLY B 83  ? 0.3978 0.2007 0.5353 -0.0069 0.0225  -0.0056 83  GLY B CA  
4912  C C   . GLY B 83  ? 0.4044 0.2298 0.5546 -0.0041 0.0211  -0.0048 83  GLY B C   
4913  O O   . GLY B 83  ? 0.3851 0.2162 0.5377 0.0044  0.0228  -0.0038 83  GLY B O   
4914  N N   . LEU B 84  ? 0.4143 0.2527 0.5729 -0.0113 0.0180  -0.0051 84  LEU B N   
4915  C CA  . LEU B 84  ? 0.3920 0.2497 0.5616 -0.0093 0.0165  -0.0043 84  LEU B CA  
4916  C C   . LEU B 84  ? 0.3950 0.2532 0.5610 -0.0057 0.0166  -0.0072 84  LEU B C   
4917  O O   . LEU B 84  ? 0.3925 0.2397 0.5492 -0.0084 0.0162  -0.0106 84  LEU B O   
4918  C CB  . LEU B 84  ? 0.3730 0.2424 0.5509 -0.0172 0.0133  -0.0043 84  LEU B CB  
4919  C CG  . LEU B 84  ? 0.4013 0.2753 0.5853 -0.0205 0.0136  -0.0011 84  LEU B CG  
4920  C CD1 . LEU B 84  ? 0.3780 0.2619 0.5691 -0.0290 0.0107  -0.0016 84  LEU B CD1 
4921  C CD2 . LEU B 84  ? 0.3726 0.2575 0.5640 -0.0141 0.0148  0.0020  84  LEU B CD2 
4922  N N   . LYS B 85  ? 0.3748 0.2458 0.5477 -0.0001 0.0173  -0.0058 85  LYS B N   
4923  C CA  . LYS B 85  ? 0.3595 0.2339 0.5304 0.0022  0.0174  -0.0079 85  LYS B CA  
4924  C C   . LYS B 85  ? 0.3674 0.2519 0.5435 -0.0039 0.0136  -0.0086 85  LYS B C   
4925  O O   . LYS B 85  ? 0.3489 0.2405 0.5324 -0.0082 0.0115  -0.0069 85  LYS B O   
4926  C CB  . LYS B 85  ? 0.3591 0.2426 0.5348 0.0099  0.0200  -0.0061 85  LYS B CB  
4927  C CG  . LYS B 85  ? 0.3827 0.2604 0.5562 0.0172  0.0233  -0.0046 85  LYS B CG  
4928  C CD  . LYS B 85  ? 0.3968 0.2561 0.5572 0.0198  0.0257  -0.0073 85  LYS B CD  
4929  C CE  . LYS B 85  ? 0.3939 0.2459 0.5515 0.0276  0.0287  -0.0053 85  LYS B CE  
4930  N NZ  . LYS B 85  ? 0.3981 0.2326 0.5427 0.0314  0.0315  -0.0084 85  LYS B NZ  
4931  N N   . LEU B 86  ? 0.3638 0.2494 0.5359 -0.0034 0.0131  -0.0107 86  LEU B N   
4932  C CA  . LEU B 86  ? 0.3453 0.2387 0.5201 -0.0083 0.0092  -0.0113 86  LEU B CA  
4933  C C   . LEU B 86  ? 0.3318 0.2332 0.5079 -0.0046 0.0099  -0.0108 86  LEU B C   
4934  O O   . LEU B 86  ? 0.3223 0.2183 0.4910 -0.0009 0.0127  -0.0123 86  LEU B O   
4935  C CB  . LEU B 86  ? 0.3601 0.2430 0.5252 -0.0138 0.0069  -0.0150 86  LEU B CB  
4936  C CG  . LEU B 86  ? 0.3555 0.2456 0.5215 -0.0188 0.0021  -0.0160 86  LEU B CG  
4937  C CD1 . LEU B 86  ? 0.3267 0.2309 0.5051 -0.0218 -0.0011 -0.0134 86  LEU B CD1 
4938  C CD2 . LEU B 86  ? 0.3720 0.2510 0.5280 -0.0251 -0.0005 -0.0199 86  LEU B CD2 
4939  N N   . ILE B 87  ? 0.2896 0.2034 0.4747 -0.0056 0.0079  -0.0085 87  ILE B N   
4940  C CA  . ILE B 87  ? 0.3022 0.2224 0.4875 -0.0045 0.0073  -0.0079 87  ILE B CA  
4941  C C   . ILE B 87  ? 0.3018 0.2230 0.4850 -0.0095 0.0025  -0.0091 87  ILE B C   
4942  O O   . ILE B 87  ? 0.2967 0.2250 0.4875 -0.0123 -0.0005 -0.0077 87  ILE B O   
4943  C CB  . ILE B 87  ? 0.3094 0.2408 0.5049 -0.0024 0.0079  -0.0046 87  ILE B CB  
4944  C CG1 . ILE B 87  ? 0.3101 0.2421 0.5078 0.0025  0.0120  -0.0035 87  ILE B CG1 
4945  C CG2 . ILE B 87  ? 0.3281 0.2650 0.5235 -0.0022 0.0069  -0.0036 87  ILE B CG2 
4946  C CD1 . ILE B 87  ? 0.3024 0.2441 0.5098 0.0035  0.0121  -0.0008 87  ILE B CD1 
4947  N N   . MET B 88  ? 0.3083 0.2231 0.4810 -0.0105 0.0017  -0.0115 88  MET B N   
4948  C CA  . MET B 88  ? 0.3301 0.2450 0.4994 -0.0156 -0.0034 -0.0131 88  MET B CA  
4949  C C   . MET B 88  ? 0.3533 0.2749 0.5222 -0.0148 -0.0057 -0.0115 88  MET B C   
4950  O O   . MET B 88  ? 0.3609 0.2800 0.5231 -0.0119 -0.0033 -0.0115 88  MET B O   
4951  C CB  . MET B 88  ? 0.3467 0.2488 0.5029 -0.0180 -0.0037 -0.0172 88  MET B CB  
4952  C CG  . MET B 88  ? 0.3776 0.2805 0.5302 -0.0240 -0.0097 -0.0191 88  MET B CG  
4953  S SD  . MET B 88  ? 0.4190 0.3065 0.5584 -0.0298 -0.0112 -0.0244 88  MET B SD  
4954  C CE  . MET B 88  ? 0.4363 0.3116 0.5598 -0.0246 -0.0067 -0.0271 88  MET B CE  
4955  N N   . GLY B 89  ? 0.3689 0.2992 0.5449 -0.0172 -0.0103 -0.0099 89  GLY B N   
4956  C CA  . GLY B 89  ? 0.3653 0.3008 0.5402 -0.0163 -0.0132 -0.0080 89  GLY B CA  
4957  C C   . GLY B 89  ? 0.3532 0.2854 0.5184 -0.0197 -0.0178 -0.0103 89  GLY B C   
4958  O O   . GLY B 89  ? 0.3740 0.3044 0.5384 -0.0242 -0.0207 -0.0128 89  GLY B O   
4959  N N   . ILE B 90  ? 0.3394 0.2699 0.4962 -0.0179 -0.0182 -0.0095 90  ILE B N   
4960  C CA  . ILE B 90  ? 0.3636 0.2917 0.5102 -0.0206 -0.0231 -0.0112 90  ILE B CA  
4961  C C   . ILE B 90  ? 0.3806 0.3182 0.5324 -0.0202 -0.0285 -0.0079 90  ILE B C   
4962  O O   . ILE B 90  ? 0.4098 0.3516 0.5669 -0.0165 -0.0269 -0.0043 90  ILE B O   
4963  C CB  . ILE B 90  ? 0.3764 0.2955 0.5085 -0.0187 -0.0196 -0.0124 90  ILE B CB  
4964  C CG1 . ILE B 90  ? 0.4128 0.3230 0.5409 -0.0173 -0.0134 -0.0153 90  ILE B CG1 
4965  C CG2 . ILE B 90  ? 0.3822 0.2978 0.5017 -0.0218 -0.0250 -0.0146 90  ILE B CG2 
4966  C CD1 . ILE B 90  ? 0.4092 0.3124 0.5344 -0.0215 -0.0150 -0.0195 90  ILE B CD1 
4967  N N   . ASP B 91  ? 0.3973 0.3381 0.5469 -0.0238 -0.0351 -0.0092 91  ASP B N   
4968  C CA  . ASP B 91  ? 0.4515 0.4028 0.6073 -0.0230 -0.0411 -0.0062 91  ASP B CA  
4969  C C   . ASP B 91  ? 0.4698 0.4184 0.6140 -0.0208 -0.0436 -0.0043 91  ASP B C   
4970  O O   . ASP B 91  ? 0.4882 0.4396 0.6272 -0.0228 -0.0501 -0.0048 91  ASP B O   
4971  C CB  . ASP B 91  ? 0.4948 0.4528 0.6552 -0.0284 -0.0472 -0.0085 91  ASP B CB  
4972  C CG  . ASP B 91  ? 0.5781 0.5496 0.7473 -0.0272 -0.0538 -0.0056 91  ASP B CG  
4973  O OD1 . ASP B 91  ? 0.5594 0.5334 0.7303 -0.0216 -0.0535 -0.0016 91  ASP B OD1 
4974  O OD2 . ASP B 91  ? 0.6429 0.6220 0.8168 -0.0320 -0.0591 -0.0074 91  ASP B OD2 
4975  N N   . ILE B 92  ? 0.4658 0.4090 0.6051 -0.0170 -0.0384 -0.0021 92  ILE B N   
4976  C CA  . ILE B 92  ? 0.5035 0.4440 0.6320 -0.0148 -0.0402 0.0007  92  ILE B CA  
4977  C C   . ILE B 92  ? 0.5023 0.4509 0.6400 -0.0114 -0.0439 0.0052  92  ILE B C   
4978  O O   . ILE B 92  ? 0.5418 0.4923 0.6888 -0.0089 -0.0402 0.0074  92  ILE B O   
4979  C CB  . ILE B 92  ? 0.5407 0.4727 0.6610 -0.0127 -0.0327 0.0014  92  ILE B CB  
4980  C CG1 . ILE B 92  ? 0.5534 0.4775 0.6652 -0.0148 -0.0286 -0.0035 92  ILE B CG1 
4981  C CG2 . ILE B 92  ? 0.5876 0.5162 0.6965 -0.0106 -0.0336 0.0049  92  ILE B CG2 
4982  C CD1 . ILE B 92  ? 0.5634 0.4828 0.6619 -0.0181 -0.0335 -0.0069 92  ILE B CD1 
4983  N N   . LYS B 93  ? 0.5651 0.5189 0.7008 -0.0115 -0.0515 0.0063  93  LYS B N   
4984  C CA  . LYS B 93  ? 0.6089 0.5712 0.7536 -0.0076 -0.0559 0.0104  93  LYS B CA  
4985  C C   . LYS B 93  ? 0.5724 0.5289 0.7142 -0.0028 -0.0520 0.0150  93  LYS B C   
4986  O O   . LYS B 93  ? 0.6369 0.5858 0.7652 -0.0020 -0.0515 0.0169  93  LYS B O   
4987  C CB  . LYS B 93  ? 0.7437 0.7114 0.8829 -0.0081 -0.0648 0.0109  93  LYS B CB  
4988  C CG  . LYS B 93  ? 0.8536 0.8323 1.0012 -0.0125 -0.0707 0.0076  93  LYS B CG  
4989  C CD  . LYS B 93  ? 0.9240 0.9175 1.0872 -0.0094 -0.0755 0.0101  93  LYS B CD  
4990  C CE  . LYS B 93  ? 0.9563 0.9626 1.1291 -0.0145 -0.0810 0.0071  93  LYS B CE  
4991  N NZ  . LYS B 93  ? 1.0103 1.0165 1.1918 -0.0189 -0.0756 0.0038  93  LYS B NZ  
4992  N N   . PRO B 94  ? 0.5139 0.4728 0.6672 -0.0001 -0.0487 0.0168  94  PRO B N   
4993  C CA  . PRO B 94  ? 0.5292 0.4811 0.6793 0.0034  -0.0448 0.0208  94  PRO B CA  
4994  C C   . PRO B 94  ? 0.5321 0.4809 0.6749 0.0076  -0.0488 0.0258  94  PRO B C   
4995  O O   . PRO B 94  ? 0.4664 0.4064 0.6020 0.0088  -0.0450 0.0288  94  PRO B O   
4996  C CB  . PRO B 94  ? 0.5099 0.4660 0.6745 0.0050  -0.0415 0.0208  94  PRO B CB  
4997  C CG  . PRO B 94  ? 0.5230 0.4901 0.6987 0.0038  -0.0454 0.0182  94  PRO B CG  
4998  C CD  . PRO B 94  ? 0.5106 0.4777 0.6791 -0.0009 -0.0479 0.0148  94  PRO B CD  
4999  N N   . GLU B 95  ? 0.5419 0.4983 0.6868 0.0098  -0.0565 0.0267  95  GLU B N   
5000  C CA  . GLU B 95  ? 0.5575 0.5115 0.6965 0.0151  -0.0610 0.0318  95  GLU B CA  
5001  C C   . GLU B 95  ? 0.5355 0.4846 0.6577 0.0139  -0.0648 0.0329  95  GLU B C   
5002  O O   . GLU B 95  ? 0.4955 0.4411 0.6096 0.0181  -0.0689 0.0375  95  GLU B O   
5003  C CB  . GLU B 95  ? 0.5912 0.5571 0.7422 0.0197  -0.0672 0.0331  95  GLU B CB  
5004  C CG  . GLU B 95  ? 0.6644 0.6334 0.8298 0.0223  -0.0633 0.0329  95  GLU B CG  
5005  C CD  . GLU B 95  ? 0.8154 0.7936 0.9938 0.0179  -0.0609 0.0280  95  GLU B CD  
5006  O OE1 . GLU B 95  ? 0.7628 0.7481 0.9420 0.0135  -0.0643 0.0249  95  GLU B OE1 
5007  O OE2 . GLU B 95  ? 0.7977 0.7749 0.9842 0.0186  -0.0557 0.0273  95  GLU B OE2 
5008  N N   . GLU B 96  ? 0.5168 0.4642 0.6325 0.0084  -0.0631 0.0287  96  GLU B N   
5009  C CA  . GLU B 96  ? 0.5473 0.4898 0.6460 0.0069  -0.0665 0.0290  96  GLU B CA  
5010  C C   . GLU B 96  ? 0.5078 0.4371 0.5921 0.0076  -0.0609 0.0324  96  GLU B C   
5011  O O   . GLU B 96  ? 0.5162 0.4407 0.6043 0.0075  -0.0536 0.0332  96  GLU B O   
5012  C CB  . GLU B 96  ? 0.5940 0.5382 0.6899 0.0010  -0.0667 0.0228  96  GLU B CB  
5013  C CG  . GLU B 96  ? 0.6275 0.5845 0.7334 -0.0008 -0.0743 0.0200  96  GLU B CG  
5014  C CD  . GLU B 96  ? 0.6691 0.6321 0.7703 0.0019  -0.0840 0.0231  96  GLU B CD  
5015  O OE1 . GLU B 96  ? 0.7359 0.6950 0.8216 -0.0001 -0.0880 0.0224  96  GLU B OE1 
5016  O OE2 . GLU B 96  ? 0.6610 0.6327 0.7740 0.0066  -0.0873 0.0263  96  GLU B OE2 
5017  N N   . ASP B 97  ? 0.4827 0.4067 0.5503 0.0079  -0.0644 0.0345  97  ASP B N   
5018  C CA  . ASP B 97  ? 0.4863 0.3981 0.5386 0.0080  -0.0592 0.0381  97  ASP B CA  
5019  C C   . ASP B 97  ? 0.4681 0.3756 0.5142 0.0032  -0.0519 0.0335  97  ASP B C   
5020  O O   . ASP B 97  ? 0.4632 0.3695 0.4983 0.0007  -0.0539 0.0303  97  ASP B O   
5021  C CB  . ASP B 97  ? 0.4947 0.4021 0.5307 0.0106  -0.0657 0.0425  97  ASP B CB  
5022  C CG  . ASP B 97  ? 0.5192 0.4133 0.5372 0.0100  -0.0600 0.0464  97  ASP B CG  
5023  O OD1 . ASP B 97  ? 0.5101 0.3994 0.5294 0.0074  -0.0507 0.0457  97  ASP B OD1 
5024  O OD2 . ASP B 97  ? 0.5631 0.4524 0.5655 0.0117  -0.0648 0.0500  97  ASP B OD2 
5025  N N   . TYR B 98  ? 0.4520 0.3567 0.5044 0.0023  -0.0434 0.0335  98  TYR B N   
5026  C CA  . TYR B 98  ? 0.4689 0.3712 0.5186 -0.0011 -0.0357 0.0294  98  TYR B CA  
5027  C C   . TYR B 98  ? 0.4795 0.3735 0.5089 -0.0024 -0.0331 0.0304  98  TYR B C   
5028  O O   . TYR B 98  ? 0.5055 0.3977 0.5293 -0.0046 -0.0286 0.0261  98  TYR B O   
5029  C CB  . TYR B 98  ? 0.4690 0.3711 0.5292 -0.0014 -0.0277 0.0305  98  TYR B CB  
5030  C CG  . TYR B 98  ? 0.4559 0.3648 0.5348 0.0000  -0.0292 0.0301  98  TYR B CG  
5031  C CD1 . TYR B 98  ? 0.4621 0.3789 0.5509 0.0001  -0.0344 0.0265  98  TYR B CD1 
5032  C CD2 . TYR B 98  ? 0.4326 0.3399 0.5188 0.0007  -0.0249 0.0331  98  TYR B CD2 
5033  C CE1 . TYR B 98  ? 0.4556 0.3789 0.5608 0.0014  -0.0350 0.0262  98  TYR B CE1 
5034  C CE2 . TYR B 98  ? 0.4284 0.3413 0.5302 0.0021  -0.0260 0.0325  98  TYR B CE2 
5035  C CZ  . TYR B 98  ? 0.4342 0.3554 0.5456 0.0028  -0.0309 0.0291  98  TYR B CZ  
5036  O OH  . TYR B 98  ? 0.3998 0.3270 0.5263 0.0041  -0.0314 0.0283  98  TYR B OH  
5037  N N   . GLY B 99  ? 0.5063 0.3945 0.5247 -0.0005 -0.0354 0.0362  99  GLY B N   
5038  C CA  . GLY B 99  ? 0.5105 0.3900 0.5085 -0.0016 -0.0324 0.0382  99  GLY B CA  
5039  C C   . GLY B 99  ? 0.5276 0.4062 0.5113 -0.0014 -0.0403 0.0369  99  GLY B C   
5040  O O   . GLY B 99  ? 0.5406 0.4122 0.5059 -0.0025 -0.0382 0.0375  99  GLY B O   
5041  N N   . ASP B 100 ? 0.5477 0.4341 0.5399 -0.0005 -0.0492 0.0347  100 ASP B N   
5042  C CA  . ASP B 100 ? 0.5852 0.4727 0.5656 -0.0013 -0.0577 0.0326  100 ASP B CA  
5043  C C   . ASP B 100 ? 0.5543 0.4402 0.5288 -0.0055 -0.0543 0.0251  100 ASP B C   
5044  O O   . ASP B 100 ? 0.5319 0.4226 0.5198 -0.0073 -0.0523 0.0203  100 ASP B O   
5045  C CB  . ASP B 100 ? 0.6170 0.5154 0.6100 0.0005  -0.0680 0.0327  100 ASP B CB  
5046  C CG  . ASP B 100 ? 0.6654 0.5676 0.6486 -0.0008 -0.0782 0.0305  100 ASP B CG  
5047  O OD1 . ASP B 100 ? 0.6545 0.5496 0.6188 -0.0033 -0.0778 0.0284  100 ASP B OD1 
5048  O OD2 . ASP B 100 ? 0.7690 0.6821 0.7641 0.0006  -0.0864 0.0308  100 ASP B OD2 
5049  N N   . PRO B 101 ? 0.5588 0.4366 0.5120 -0.0070 -0.0530 0.0241  101 PRO B N   
5050  C CA  . PRO B 101 ? 0.5776 0.4514 0.5231 -0.0102 -0.0485 0.0169  101 PRO B CA  
5051  C C   . PRO B 101 ? 0.5995 0.4780 0.5496 -0.0134 -0.0555 0.0103  101 PRO B C   
5052  O O   . PRO B 101 ? 0.6247 0.5003 0.5751 -0.0157 -0.0506 0.0042  101 PRO B O   
5053  C CB  . PRO B 101 ? 0.5869 0.4509 0.5072 -0.0106 -0.0462 0.0179  101 PRO B CB  
5054  C CG  . PRO B 101 ? 0.5938 0.4562 0.5080 -0.0076 -0.0498 0.0264  101 PRO B CG  
5055  C CD  . PRO B 101 ? 0.5636 0.4342 0.4985 -0.0051 -0.0542 0.0301  101 PRO B CD  
5056  N N   . GLU B 102 ? 0.6090 0.4948 0.5626 -0.0134 -0.0665 0.0117  102 GLU B N   
5057  C CA  . GLU B 102 ? 0.6132 0.5055 0.5732 -0.0173 -0.0738 0.0060  102 GLU B CA  
5058  C C   . GLU B 102 ? 0.5475 0.4467 0.5306 -0.0178 -0.0706 0.0041  102 GLU B C   
5059  O O   . GLU B 102 ? 0.5707 0.4695 0.5573 -0.0217 -0.0699 -0.0020 102 GLU B O   
5060  C CB  . GLU B 102 ? 0.6585 0.5595 0.6180 -0.0173 -0.0867 0.0082  102 GLU B CB  
5061  C CG  . GLU B 102 ? 0.7114 0.6179 0.6725 -0.0231 -0.0943 0.0015  102 GLU B CG  
5062  C CD  . GLU B 102 ? 0.7711 0.6666 0.7114 -0.0282 -0.0937 -0.0054 102 GLU B CD  
5063  O OE1 . GLU B 102 ? 0.8181 0.7059 0.7369 -0.0274 -0.0949 -0.0041 102 GLU B OE1 
5064  O OE2 . GLU B 102 ? 0.7271 0.6213 0.6720 -0.0330 -0.0925 -0.0120 102 GLU B OE2 
5065  N N   . PHE B 103 ? 0.5243 0.4285 0.5218 -0.0138 -0.0684 0.0094  103 PHE B N   
5066  C CA  . PHE B 103 ? 0.5060 0.4162 0.5243 -0.0138 -0.0645 0.0083  103 PHE B CA  
5067  C C   . PHE B 103 ? 0.5406 0.4434 0.5578 -0.0151 -0.0542 0.0043  103 PHE B C   
5068  O O   . PHE B 103 ? 0.5565 0.4618 0.5845 -0.0173 -0.0527 0.0000  103 PHE B O   
5069  C CB  . PHE B 103 ? 0.4780 0.3927 0.5083 -0.0090 -0.0639 0.0148  103 PHE B CB  
5070  C CG  . PHE B 103 ? 0.4617 0.3821 0.5121 -0.0089 -0.0595 0.0135  103 PHE B CG  
5071  C CD1 . PHE B 103 ? 0.4503 0.3803 0.5145 -0.0109 -0.0645 0.0106  103 PHE B CD1 
5072  C CD2 . PHE B 103 ? 0.4572 0.3731 0.5116 -0.0076 -0.0503 0.0148  103 PHE B CD2 
5073  C CE1 . PHE B 103 ? 0.4366 0.3710 0.5175 -0.0111 -0.0602 0.0093  103 PHE B CE1 
5074  C CE2 . PHE B 103 ? 0.4502 0.3711 0.5217 -0.0076 -0.0466 0.0134  103 PHE B CE2 
5075  C CZ  . PHE B 103 ? 0.4443 0.3739 0.5286 -0.0091 -0.0515 0.0108  103 PHE B CZ  
5076  N N   . VAL B 104 ? 0.5251 0.4193 0.5296 -0.0136 -0.0469 0.0058  104 VAL B N   
5077  C CA  . VAL B 104 ? 0.5130 0.4016 0.5164 -0.0140 -0.0371 0.0022  104 VAL B CA  
5078  C C   . VAL B 104 ? 0.5412 0.4250 0.5365 -0.0175 -0.0386 -0.0052 104 VAL B C   
5079  O O   . VAL B 104 ? 0.5200 0.4040 0.5245 -0.0187 -0.0358 -0.0093 104 VAL B O   
5080  C CB  . VAL B 104 ? 0.5210 0.4030 0.5121 -0.0120 -0.0291 0.0054  104 VAL B CB  
5081  C CG1 . VAL B 104 ? 0.5195 0.3972 0.5091 -0.0118 -0.0191 0.0013  104 VAL B CG1 
5082  C CG2 . VAL B 104 ? 0.5006 0.3856 0.4999 -0.0095 -0.0269 0.0125  104 VAL B CG2 
5083  N N   . LYS B 105 ? 0.5862 0.4650 0.5633 -0.0193 -0.0436 -0.0069 105 LYS B N   
5084  C CA  . LYS B 105 ? 0.5949 0.4676 0.5617 -0.0234 -0.0464 -0.0141 105 LYS B CA  
5085  C C   . LYS B 105 ? 0.5536 0.4327 0.5364 -0.0268 -0.0513 -0.0173 105 LYS B C   
5086  O O   . LYS B 105 ? 0.5342 0.4078 0.5179 -0.0286 -0.0473 -0.0225 105 LYS B O   
5087  C CB  . LYS B 105 ? 0.6280 0.4974 0.5754 -0.0254 -0.0541 -0.0145 105 LYS B CB  
5088  C CG  . LYS B 105 ? 0.6562 0.5174 0.5897 -0.0302 -0.0568 -0.0225 105 LYS B CG  
5089  C CD  . LYS B 105 ? 0.7087 0.5672 0.6225 -0.0328 -0.0655 -0.0233 105 LYS B CD  
5090  C CE  . LYS B 105 ? 0.7175 0.5661 0.6150 -0.0382 -0.0683 -0.0317 105 LYS B CE  
5091  N NZ  . LYS B 105 ? 0.7541 0.5990 0.6296 -0.0396 -0.0750 -0.0317 105 LYS B NZ  
5092  N N   . ASP B 106 ? 0.5393 0.4300 0.5349 -0.0275 -0.0595 -0.0142 106 ASP B N   
5093  C CA  . ASP B 106 ? 0.5462 0.4438 0.5560 -0.0316 -0.0642 -0.0173 106 ASP B CA  
5094  C C   . ASP B 106 ? 0.5104 0.4084 0.5356 -0.0302 -0.0565 -0.0177 106 ASP B C   
5095  O O   . ASP B 106 ? 0.5129 0.4093 0.5433 -0.0338 -0.0562 -0.0221 106 ASP B O   
5096  C CB  . ASP B 106 ? 0.5668 0.4786 0.5884 -0.0321 -0.0740 -0.0137 106 ASP B CB  
5097  C CG  . ASP B 106 ? 0.5889 0.5022 0.5963 -0.0337 -0.0834 -0.0133 106 ASP B CG  
5098  O OD1 . ASP B 106 ? 0.5997 0.5027 0.5882 -0.0367 -0.0836 -0.0177 106 ASP B OD1 
5099  O OD2 . ASP B 106 ? 0.5915 0.5155 0.6054 -0.0311 -0.0901 -0.0083 106 ASP B OD2 
5100  N N   . SER B 107 ? 0.4997 0.3994 0.5314 -0.0251 -0.0503 -0.0129 107 SER B N   
5101  C CA  . SER B 107 ? 0.4695 0.3703 0.5153 -0.0233 -0.0431 -0.0128 107 SER B CA  
5102  C C   . SER B 107 ? 0.4871 0.3769 0.5246 -0.0238 -0.0360 -0.0180 107 SER B C   
5103  O O   . SER B 107 ? 0.4618 0.3512 0.5088 -0.0246 -0.0331 -0.0204 107 SER B O   
5104  C CB  . SER B 107 ? 0.4509 0.3554 0.5038 -0.0186 -0.0386 -0.0068 107 SER B CB  
5105  O OG  . SER B 107 ? 0.4329 0.3471 0.4966 -0.0174 -0.0447 -0.0024 107 SER B OG  
5106  N N   . GLU B 108 ? 0.5180 0.3987 0.5370 -0.0230 -0.0330 -0.0196 108 GLU B N   
5107  C CA  . GLU B 108 ? 0.5330 0.4027 0.5421 -0.0220 -0.0253 -0.0243 108 GLU B CA  
5108  C C   . GLU B 108 ? 0.5377 0.3997 0.5407 -0.0267 -0.0288 -0.0311 108 GLU B C   
5109  O O   . GLU B 108 ? 0.5195 0.3742 0.5230 -0.0260 -0.0233 -0.0348 108 GLU B O   
5110  C CB  . GLU B 108 ? 0.5576 0.4200 0.5474 -0.0198 -0.0211 -0.0242 108 GLU B CB  
5111  C CG  . GLU B 108 ? 0.5865 0.4542 0.5805 -0.0157 -0.0156 -0.0179 108 GLU B CG  
5112  C CD  . GLU B 108 ? 0.6436 0.5051 0.6185 -0.0141 -0.0114 -0.0170 108 GLU B CD  
5113  O OE1 . GLU B 108 ? 0.7216 0.5783 0.6812 -0.0164 -0.0171 -0.0186 108 GLU B OE1 
5114  O OE2 . GLU B 108 ? 0.6851 0.5472 0.6602 -0.0110 -0.0029 -0.0145 108 GLU B OE2 
5115  N N   . ILE B 109 ? 0.5327 0.3959 0.5291 -0.0315 -0.0381 -0.0325 109 ILE B N   
5116  C CA  . ILE B 109 ? 0.5246 0.3807 0.5141 -0.0377 -0.0429 -0.0389 109 ILE B CA  
5117  C C   . ILE B 109 ? 0.5034 0.3643 0.5111 -0.0402 -0.0436 -0.0394 109 ILE B C   
5118  O O   . ILE B 109 ? 0.5316 0.3826 0.5360 -0.0428 -0.0413 -0.0444 109 ILE B O   
5119  C CB  . ILE B 109 ? 0.5412 0.4013 0.5220 -0.0422 -0.0534 -0.0391 109 ILE B CB  
5120  C CG1 . ILE B 109 ? 0.5528 0.4044 0.5112 -0.0403 -0.0521 -0.0397 109 ILE B CG1 
5121  C CG2 . ILE B 109 ? 0.5435 0.4015 0.5235 -0.0503 -0.0604 -0.0447 109 ILE B CG2 
5122  C CD1 . ILE B 109 ? 0.5655 0.4214 0.5140 -0.0440 -0.0629 -0.0393 109 ILE B CD1 
5123  N N   . GLU B 110 ? 0.4749 0.3500 0.5010 -0.0388 -0.0457 -0.0340 110 GLU B N   
5124  C CA  . GLU B 110 ? 0.4542 0.3359 0.4982 -0.0411 -0.0466 -0.0337 110 GLU B CA  
5125  C C   . GLU B 110 ? 0.4379 0.3134 0.4871 -0.0372 -0.0371 -0.0341 110 GLU B C   
5126  O O   . GLU B 110 ? 0.4212 0.2915 0.4738 -0.0400 -0.0358 -0.0372 110 GLU B O   
5127  C CB  . GLU B 110 ? 0.4391 0.3376 0.4994 -0.0403 -0.0518 -0.0282 110 GLU B CB  
5128  C CG  . GLU B 110 ? 0.4474 0.3543 0.5265 -0.0427 -0.0527 -0.0277 110 GLU B CG  
5129  C CD  . GLU B 110 ? 0.4910 0.3940 0.5692 -0.0506 -0.0560 -0.0328 110 GLU B CD  
5130  O OE1 . GLU B 110 ? 0.5315 0.4280 0.5960 -0.0558 -0.0608 -0.0371 110 GLU B OE1 
5131  O OE2 . GLU B 110 ? 0.4842 0.3899 0.5752 -0.0518 -0.0536 -0.0325 110 GLU B OE2 
5132  N N   . LEU B 111 ? 0.4195 0.2958 0.4692 -0.0308 -0.0306 -0.0308 111 LEU B N   
5133  C CA  . LEU B 111 ? 0.4252 0.2973 0.4800 -0.0266 -0.0220 -0.0309 111 LEU B CA  
5134  C C   . LEU B 111 ? 0.4368 0.2932 0.4769 -0.0268 -0.0179 -0.0369 111 LEU B C   
5135  O O   . LEU B 111 ? 0.4380 0.2891 0.4825 -0.0261 -0.0142 -0.0387 111 LEU B O   
5136  C CB  . LEU B 111 ? 0.4371 0.3141 0.4944 -0.0207 -0.0164 -0.0263 111 LEU B CB  
5137  C CG  . LEU B 111 ? 0.4232 0.3000 0.4883 -0.0158 -0.0079 -0.0253 111 LEU B CG  
5138  C CD1 . LEU B 111 ? 0.4231 0.3061 0.5050 -0.0166 -0.0089 -0.0240 111 LEU B CD1 
5139  C CD2 . LEU B 111 ? 0.4305 0.3136 0.4971 -0.0120 -0.0040 -0.0206 111 LEU B CD2 
5140  N N   . LYS B 112 ? 0.4663 0.3142 0.4880 -0.0276 -0.0186 -0.0400 112 LYS B N   
5141  C CA  . LYS B 112 ? 0.5022 0.3337 0.5084 -0.0272 -0.0144 -0.0461 112 LYS B CA  
5142  C C   . LYS B 112 ? 0.5112 0.3351 0.5176 -0.0335 -0.0186 -0.0505 112 LYS B C   
5143  O O   . LYS B 112 ? 0.4911 0.3036 0.4947 -0.0318 -0.0135 -0.0537 112 LYS B O   
5144  C CB  . LYS B 112 ? 0.5375 0.3612 0.5225 -0.0272 -0.0147 -0.0488 112 LYS B CB  
5145  C CG  . LYS B 112 ? 0.5568 0.3821 0.5378 -0.0202 -0.0066 -0.0460 112 LYS B CG  
5146  C CD  . LYS B 112 ? 0.6046 0.4207 0.5629 -0.0193 -0.0048 -0.0489 112 LYS B CD  
5147  C CE  . LYS B 112 ? 0.6233 0.4458 0.5819 -0.0134 0.0026  -0.0443 112 LYS B CE  
5148  N NZ  . LYS B 112 ? 0.6577 0.4754 0.5964 -0.0137 0.0023  -0.0450 112 LYS B NZ  
5149  N N   . ARG B 113 ? 0.5377 0.3684 0.5477 -0.0406 -0.0278 -0.0504 113 ARG B N   
5150  C CA  . ARG B 113 ? 0.5541 0.3792 0.5644 -0.0483 -0.0325 -0.0545 113 ARG B CA  
5151  C C   . ARG B 113 ? 0.5370 0.3632 0.5627 -0.0472 -0.0285 -0.0527 113 ARG B C   
5152  O O   . ARG B 113 ? 0.5189 0.3319 0.5395 -0.0501 -0.0268 -0.0567 113 ARG B O   
5153  C CB  . ARG B 113 ? 0.5537 0.3911 0.5690 -0.0555 -0.0430 -0.0535 113 ARG B CB  
5154  C CG  . ARG B 113 ? 0.5695 0.4033 0.5863 -0.0649 -0.0483 -0.0574 113 ARG B CG  
5155  C CD  . ARG B 113 ? 0.5805 0.4322 0.6090 -0.0709 -0.0580 -0.0550 113 ARG B CD  
5156  N NE  . ARG B 113 ? 0.5609 0.4292 0.6113 -0.0673 -0.0570 -0.0488 113 ARG B NE  
5157  C CZ  . ARG B 113 ? 0.5473 0.4195 0.6122 -0.0695 -0.0553 -0.0477 113 ARG B CZ  
5158  N NH1 . ARG B 113 ? 0.5784 0.4388 0.6388 -0.0759 -0.0548 -0.0520 113 ARG B NH1 
5159  N NH2 . ARG B 113 ? 0.5076 0.3946 0.5907 -0.0656 -0.0543 -0.0422 113 ARG B NH2 
5160  N N   . VAL B 114 ? 0.5145 0.3553 0.5576 -0.0430 -0.0268 -0.0468 114 VAL B N   
5161  C CA  . VAL B 114 ? 0.5154 0.3585 0.5728 -0.0411 -0.0228 -0.0446 114 VAL B CA  
5162  C C   . VAL B 114 ? 0.5230 0.3526 0.5731 -0.0348 -0.0141 -0.0464 114 VAL B C   
5163  O O   . VAL B 114 ? 0.5350 0.3542 0.5844 -0.0359 -0.0118 -0.0486 114 VAL B O   
5164  C CB  . VAL B 114 ? 0.4896 0.3504 0.5653 -0.0375 -0.0227 -0.0382 114 VAL B CB  
5165  C CG1 . VAL B 114 ? 0.4897 0.3520 0.5783 -0.0350 -0.0182 -0.0360 114 VAL B CG1 
5166  C CG2 . VAL B 114 ? 0.5020 0.3766 0.5866 -0.0426 -0.0310 -0.0361 114 VAL B CG2 
5167  N N   . LEU B 115 ? 0.4949 0.3249 0.5396 -0.0280 -0.0092 -0.0454 115 LEU B N   
5168  C CA  . LEU B 115 ? 0.4837 0.3048 0.5240 -0.0207 -0.0005 -0.0464 115 LEU B CA  
5169  C C   . LEU B 115 ? 0.5034 0.3043 0.5276 -0.0225 0.0007  -0.0528 115 LEU B C   
5170  O O   . LEU B 115 ? 0.5058 0.2975 0.5297 -0.0183 0.0061  -0.0538 115 LEU B O   
5171  C CB  . LEU B 115 ? 0.4699 0.2954 0.5058 -0.0144 0.0045  -0.0446 115 LEU B CB  
5172  C CG  . LEU B 115 ? 0.4692 0.3125 0.5205 -0.0124 0.0041  -0.0382 115 LEU B CG  
5173  C CD1 . LEU B 115 ? 0.4892 0.3360 0.5343 -0.0079 0.0087  -0.0365 115 LEU B CD1 
5174  C CD2 . LEU B 115 ? 0.4364 0.2872 0.5047 -0.0093 0.0072  -0.0347 115 LEU B CD2 
5175  N N   . ASN B 116 ? 0.5251 0.3189 0.5359 -0.0289 -0.0047 -0.0569 116 ASN B N   
5176  C CA  . ASN B 116 ? 0.5598 0.3325 0.5519 -0.0309 -0.0036 -0.0637 116 ASN B CA  
5177  C C   . ASN B 116 ? 0.5663 0.3287 0.5624 -0.0332 -0.0027 -0.0650 116 ASN B C   
5178  O O   . ASN B 116 ? 0.5856 0.3295 0.5690 -0.0301 0.0021  -0.0691 116 ASN B O   
5179  C CB  . ASN B 116 ? 0.5956 0.3644 0.5741 -0.0389 -0.0111 -0.0677 116 ASN B CB  
5180  C CG  . ASN B 116 ? 0.6383 0.3835 0.5941 -0.0400 -0.0090 -0.0752 116 ASN B CG  
5181  O OD1 . ASN B 116 ? 0.6772 0.4138 0.6207 -0.0327 -0.0023 -0.0773 116 ASN B OD1 
5182  N ND2 . ASN B 116 ? 0.6485 0.3828 0.5984 -0.0490 -0.0142 -0.0795 116 ASN B ND2 
5183  N N   . TYR B 117 ? 0.5430 0.3166 0.5558 -0.0381 -0.0068 -0.0613 117 TYR B N   
5184  C CA  . TYR B 117 ? 0.5322 0.2972 0.5497 -0.0405 -0.0057 -0.0615 117 TYR B CA  
5185  C C   . TYR B 117 ? 0.5091 0.2851 0.5438 -0.0334 -0.0010 -0.0556 117 TYR B C   
5186  O O   . TYR B 117 ? 0.5257 0.2915 0.5606 -0.0304 0.0033  -0.0555 117 TYR B O   
5187  C CB  . TYR B 117 ? 0.5299 0.2978 0.5516 -0.0526 -0.0137 -0.0625 117 TYR B CB  
5188  C CG  . TYR B 117 ? 0.4919 0.2839 0.5317 -0.0559 -0.0193 -0.0575 117 TYR B CG  
5189  C CD1 . TYR B 117 ? 0.4685 0.2732 0.5267 -0.0533 -0.0175 -0.0521 117 TYR B CD1 
5190  C CD2 . TYR B 117 ? 0.4941 0.2956 0.5319 -0.0609 -0.0264 -0.0583 117 TYR B CD2 
5191  C CE1 . TYR B 117 ? 0.4554 0.2810 0.5294 -0.0552 -0.0220 -0.0478 117 TYR B CE1 
5192  C CE2 . TYR B 117 ? 0.4838 0.3069 0.5378 -0.0622 -0.0311 -0.0535 117 TYR B CE2 
5193  C CZ  . TYR B 117 ? 0.4614 0.2961 0.5335 -0.0592 -0.0286 -0.0484 117 TYR B CZ  
5194  O OH  . TYR B 117 ? 0.4286 0.2831 0.5160 -0.0597 -0.0327 -0.0441 117 TYR B OH  
5195  N N   . ALA B 118 ? 0.4609 0.2568 0.5093 -0.0308 -0.0019 -0.0507 118 ALA B N   
5196  C CA  . ALA B 118 ? 0.4309 0.2377 0.4951 -0.0249 0.0019  -0.0455 118 ALA B CA  
5197  C C   . ALA B 118 ? 0.4295 0.2278 0.4890 -0.0152 0.0100  -0.0457 118 ALA B C   
5198  O O   . ALA B 118 ? 0.4090 0.2079 0.4769 -0.0113 0.0131  -0.0431 118 ALA B O   
5199  C CB  . ALA B 118 ? 0.4025 0.2294 0.4790 -0.0238 -0.0002 -0.0409 118 ALA B CB  
5200  N N   . LYS B 119 ? 0.4446 0.2360 0.4910 -0.0107 0.0135  -0.0487 119 LYS B N   
5201  C CA  . LYS B 119 ? 0.4761 0.2627 0.5198 -0.0005 0.0215  -0.0486 119 LYS B CA  
5202  C C   . LYS B 119 ? 0.5223 0.2907 0.5596 0.0017  0.0244  -0.0510 119 LYS B C   
5203  O O   . LYS B 119 ? 0.5543 0.3189 0.5908 0.0109  0.0308  -0.0505 119 LYS B O   
5204  C CB  . LYS B 119 ? 0.4984 0.2796 0.5271 0.0032  0.0248  -0.0521 119 LYS B CB  
5205  C CG  . LYS B 119 ? 0.5457 0.3049 0.5536 -0.0004 0.0238  -0.0590 119 LYS B CG  
5206  C CD  . LYS B 119 ? 0.5682 0.3198 0.5583 0.0024  0.0268  -0.0633 119 LYS B CD  
5207  C CE  . LYS B 119 ? 0.5999 0.3320 0.5717 -0.0048 0.0227  -0.0698 119 LYS B CE  
5208  N NZ  . LYS B 119 ? 0.6238 0.3444 0.5749 -0.0027 0.0253  -0.0751 119 LYS B NZ  
5209  N N   . LYS B 120 ? 0.5092 0.2663 0.5421 -0.0064 0.0200  -0.0532 120 LYS B N   
5210  C CA  . LYS B 120 ? 0.5413 0.2800 0.5680 -0.0045 0.0229  -0.0548 120 LYS B CA  
5211  C C   . LYS B 120 ? 0.5156 0.2624 0.5582 -0.0041 0.0227  -0.0494 120 LYS B C   
5212  O O   . LYS B 120 ? 0.5060 0.2390 0.5450 -0.0014 0.0255  -0.0493 120 LYS B O   
5213  C CB  . LYS B 120 ? 0.5681 0.2874 0.5802 -0.0141 0.0189  -0.0601 120 LYS B CB  
5214  C CG  . LYS B 120 ? 0.6046 0.3098 0.5966 -0.0141 0.0195  -0.0665 120 LYS B CG  
5215  C CD  . LYS B 120 ? 0.6588 0.3456 0.6365 -0.0250 0.0147  -0.0721 120 LYS B CD  
5216  C CE  . LYS B 120 ? 0.6537 0.3543 0.6426 -0.0370 0.0065  -0.0702 120 LYS B CE  
5217  N NZ  . LYS B 120 ? 0.6971 0.3810 0.6727 -0.0483 0.0018  -0.0756 120 LYS B NZ  
5218  N N   . TYR B 121 ? 0.4843 0.2527 0.5436 -0.0063 0.0197  -0.0448 121 TYR B N   
5219  C CA  . TYR B 121 ? 0.4708 0.2469 0.5440 -0.0073 0.0190  -0.0402 121 TYR B CA  
5220  C C   . TYR B 121 ? 0.4712 0.2633 0.5570 0.0014  0.0225  -0.0355 121 TYR B C   
5221  O O   . TYR B 121 ? 0.4885 0.2984 0.5847 0.0007  0.0207  -0.0330 121 TYR B O   
5222  C CB  . TYR B 121 ? 0.4563 0.2411 0.5367 -0.0185 0.0123  -0.0395 121 TYR B CB  
5223  C CG  . TYR B 121 ? 0.4566 0.2254 0.5241 -0.0277 0.0088  -0.0444 121 TYR B CG  
5224  C CD1 . TYR B 121 ? 0.4665 0.2327 0.5238 -0.0319 0.0055  -0.0486 121 TYR B CD1 
5225  C CD2 . TYR B 121 ? 0.4749 0.2302 0.5393 -0.0325 0.0087  -0.0447 121 TYR B CD2 
5226  C CE1 . TYR B 121 ? 0.4854 0.2369 0.5304 -0.0408 0.0020  -0.0535 121 TYR B CE1 
5227  C CE2 . TYR B 121 ? 0.4933 0.2329 0.5453 -0.0418 0.0056  -0.0494 121 TYR B CE2 
5228  C CZ  . TYR B 121 ? 0.4955 0.2335 0.5380 -0.0462 0.0020  -0.0540 121 TYR B CZ  
5229  O OH  . TYR B 121 ? 0.5396 0.2626 0.5698 -0.0560 -0.0015 -0.0589 121 TYR B OH  
5230  N N   . ASP B 122 ? 0.4772 0.2627 0.5624 0.0095  0.0273  -0.0342 122 ASP B N   
5231  C CA  . ASP B 122 ? 0.4636 0.2643 0.5604 0.0179  0.0307  -0.0301 122 ASP B CA  
5232  C C   . ASP B 122 ? 0.4326 0.2478 0.5451 0.0154  0.0281  -0.0252 122 ASP B C   
5233  O O   . ASP B 122 ? 0.4274 0.2558 0.5502 0.0211  0.0300  -0.0217 122 ASP B O   
5234  C CB  . ASP B 122 ? 0.4666 0.2576 0.5572 0.0285  0.0366  -0.0306 122 ASP B CB  
5235  C CG  . ASP B 122 ? 0.4722 0.2490 0.5598 0.0307  0.0376  -0.0294 122 ASP B CG  
5236  O OD1 . ASP B 122 ? 0.4266 0.2008 0.5168 0.0230  0.0339  -0.0282 122 ASP B OD1 
5237  O OD2 . ASP B 122 ? 0.5253 0.2941 0.6079 0.0407  0.0425  -0.0296 122 ASP B OD2 
5238  N N   . CYS B 123 ? 0.4069 0.2203 0.5217 0.0068  0.0238  -0.0248 123 CYS B N   
5239  C CA  . CYS B 123 ? 0.3939 0.2229 0.5234 0.0042  0.0214  -0.0205 123 CYS B CA  
5240  C C   . CYS B 123 ? 0.3772 0.2241 0.5154 0.0033  0.0195  -0.0194 123 CYS B C   
5241  O O   . CYS B 123 ? 0.3741 0.2349 0.5244 0.0032  0.0184  -0.0159 123 CYS B O   
5242  C CB  . CYS B 123 ? 0.3897 0.2153 0.5205 -0.0051 0.0177  -0.0204 123 CYS B CB  
5243  S SG  . CYS B 123 ? 0.3926 0.2198 0.5200 -0.0153 0.0122  -0.0240 123 CYS B SG  
5244  N N   . ILE B 124 ? 0.3859 0.2318 0.5171 0.0026  0.0191  -0.0222 124 ILE B N   
5245  C CA  . ILE B 124 ? 0.3800 0.2411 0.5179 0.0025  0.0178  -0.0207 124 ILE B CA  
5246  C C   . ILE B 124 ? 0.3751 0.2433 0.5167 0.0107  0.0225  -0.0188 124 ILE B C   
5247  O O   . ILE B 124 ? 0.4125 0.2730 0.5454 0.0159  0.0266  -0.0209 124 ILE B O   
5248  C CB  . ILE B 124 ? 0.4177 0.2750 0.5458 -0.0014 0.0153  -0.0241 124 ILE B CB  
5249  C CG1 . ILE B 124 ? 0.4464 0.2995 0.5724 -0.0102 0.0099  -0.0259 124 ILE B CG1 
5250  C CG2 . ILE B 124 ? 0.4136 0.2845 0.5465 -0.0006 0.0146  -0.0221 124 ILE B CG2 
5251  C CD1 . ILE B 124 ? 0.4673 0.3131 0.5805 -0.0140 0.0073  -0.0300 124 ILE B CD1 
5252  N N   . ILE B 125 ? 0.3411 0.2240 0.4953 0.0115  0.0221  -0.0150 125 ILE B N   
5253  C CA  . ILE B 125 ? 0.3447 0.2374 0.5049 0.0179  0.0259  -0.0128 125 ILE B CA  
5254  C C   . ILE B 125 ? 0.3317 0.2371 0.4973 0.0162  0.0251  -0.0110 125 ILE B C   
5255  O O   . ILE B 125 ? 0.2907 0.2046 0.4606 0.0203  0.0284  -0.0094 125 ILE B O   
5256  C CB  . ILE B 125 ? 0.3310 0.2287 0.5005 0.0208  0.0266  -0.0097 125 ILE B CB  
5257  C CG1 . ILE B 125 ? 0.3303 0.2355 0.5089 0.0155  0.0225  -0.0074 125 ILE B CG1 
5258  C CG2 . ILE B 125 ? 0.3435 0.2274 0.5063 0.0243  0.0285  -0.0108 125 ILE B CG2 
5259  C CD1 . ILE B 125 ? 0.3296 0.2432 0.5178 0.0186  0.0231  -0.0042 125 ILE B CD1 
5260  N N   . THR B 126 ? 0.3409 0.2481 0.5065 0.0103  0.0207  -0.0112 126 THR B N   
5261  C CA  . THR B 126 ? 0.3232 0.2386 0.4900 0.0091  0.0201  -0.0098 126 THR B CA  
5262  C C   . THR B 126 ? 0.3370 0.2494 0.4988 0.0036  0.0152  -0.0111 126 THR B C   
5263  O O   . THR B 126 ? 0.3349 0.2449 0.4984 -0.0002 0.0114  -0.0118 126 THR B O   
5264  C CB  . THR B 126 ? 0.3290 0.2566 0.5081 0.0091  0.0196  -0.0062 126 THR B CB  
5265  O OG1 . THR B 126 ? 0.3265 0.2592 0.5104 0.0140  0.0238  -0.0049 126 THR B OG1 
5266  C CG2 . THR B 126 ? 0.3382 0.2719 0.5179 0.0067  0.0180  -0.0045 126 THR B CG2 
5267  N N   . TYR B 127 ? 0.3328 0.2464 0.4888 0.0032  0.0152  -0.0111 127 TYR B N   
5268  C CA  . TYR B 127 ? 0.3333 0.2467 0.4853 -0.0012 0.0101  -0.0114 127 TYR B CA  
5269  C C   . TYR B 127 ? 0.3416 0.2648 0.5005 -0.0017 0.0087  -0.0076 127 TYR B C   
5270  O O   . TYR B 127 ? 0.3396 0.2665 0.4993 0.0009  0.0126  -0.0058 127 TYR B O   
5271  C CB  . TYR B 127 ? 0.3327 0.2389 0.4705 -0.0014 0.0106  -0.0138 127 TYR B CB  
5272  C CG  . TYR B 127 ? 0.3413 0.2352 0.4691 -0.0024 0.0105  -0.0183 127 TYR B CG  
5273  C CD1 . TYR B 127 ? 0.3444 0.2345 0.4694 -0.0079 0.0048  -0.0203 127 TYR B CD1 
5274  C CD2 . TYR B 127 ? 0.3389 0.2251 0.4604 0.0021  0.0162  -0.0206 127 TYR B CD2 
5275  C CE1 . TYR B 127 ? 0.3616 0.2390 0.4763 -0.0099 0.0045  -0.0247 127 TYR B CE1 
5276  C CE2 . TYR B 127 ? 0.3564 0.2289 0.4671 0.0012  0.0162  -0.0249 127 TYR B CE2 
5277  C CZ  . TYR B 127 ? 0.3571 0.2245 0.4639 -0.0053 0.0103  -0.0271 127 TYR B CZ  
5278  O OH  . TYR B 127 ? 0.3902 0.2429 0.4858 -0.0071 0.0102  -0.0315 127 TYR B OH  
5279  N N   . LEU B 128 ? 0.3276 0.2543 0.4905 -0.0049 0.0032  -0.0066 128 LEU B N   
5280  C CA  . LEU B 128 ? 0.3395 0.2731 0.5070 -0.0051 0.0013  -0.0032 128 LEU B CA  
5281  C C   . LEU B 128 ? 0.3531 0.2843 0.5114 -0.0070 -0.0028 -0.0034 128 LEU B C   
5282  O O   . LEU B 128 ? 0.3913 0.3223 0.5490 -0.0097 -0.0078 -0.0048 128 LEU B O   
5283  C CB  . LEU B 128 ? 0.3422 0.2827 0.5217 -0.0058 -0.0014 -0.0013 128 LEU B CB  
5284  C CG  . LEU B 128 ? 0.3499 0.2926 0.5379 -0.0045 0.0015  -0.0012 128 LEU B CG  
5285  C CD1 . LEU B 128 ? 0.3497 0.2987 0.5476 -0.0055 -0.0014 0.0003  128 LEU B CD1 
5286  C CD2 . LEU B 128 ? 0.3494 0.2939 0.5388 -0.0015 0.0066  0.0001  128 LEU B CD2 
5287  N N   . VAL B 129 ? 0.3334 0.2635 0.4848 -0.0057 -0.0008 -0.0018 129 VAL B N   
5288  C CA  . VAL B 129 ? 0.3654 0.2910 0.5045 -0.0070 -0.0035 -0.0025 129 VAL B CA  
5289  C C   . VAL B 129 ? 0.3714 0.3010 0.5122 -0.0079 -0.0093 0.0006  129 VAL B C   
5290  O O   . VAL B 129 ? 0.3728 0.3002 0.5050 -0.0092 -0.0137 0.0001  129 VAL B O   
5291  C CB  . VAL B 129 ? 0.3993 0.3214 0.5293 -0.0051 0.0024  -0.0021 129 VAL B CB  
5292  C CG1 . VAL B 129 ? 0.4183 0.3442 0.5501 -0.0045 0.0037  0.0025  129 VAL B CG1 
5293  C CG2 . VAL B 129 ? 0.4349 0.3491 0.5491 -0.0059 0.0017  -0.0050 129 VAL B CG2 
5294  N N   . ILE B 130 ? 0.3704 0.3057 0.5219 -0.0068 -0.0096 0.0037  130 ILE B N   
5295  C CA  . ILE B 130 ? 0.3953 0.3343 0.5496 -0.0066 -0.0153 0.0063  130 ILE B CA  
5296  C C   . ILE B 130 ? 0.3880 0.3330 0.5560 -0.0055 -0.0152 0.0078  130 ILE B C   
5297  O O   . ILE B 130 ? 0.3840 0.3297 0.5575 -0.0048 -0.0105 0.0079  130 ILE B O   
5298  C CB  . ILE B 130 ? 0.4272 0.3628 0.5720 -0.0055 -0.0156 0.0097  130 ILE B CB  
5299  C CG1 . ILE B 130 ? 0.4604 0.3983 0.6044 -0.0047 -0.0226 0.0119  130 ILE B CG1 
5300  C CG2 . ILE B 130 ? 0.4254 0.3607 0.5736 -0.0043 -0.0105 0.0127  130 ILE B CG2 
5301  C CD1 . ILE B 130 ? 0.4618 0.3943 0.5933 -0.0037 -0.0235 0.0153  130 ILE B CD1 
5302  N N   . ASN B 131 ? 0.3709 0.3207 0.5439 -0.0051 -0.0205 0.0088  131 ASN B N   
5303  C CA  . ASN B 131 ? 0.3685 0.3240 0.5535 -0.0035 -0.0210 0.0102  131 ASN B CA  
5304  C C   . ASN B 131 ? 0.3709 0.3263 0.5554 -0.0005 -0.0233 0.0140  131 ASN B C   
5305  O O   . ASN B 131 ? 0.3574 0.3154 0.5408 0.0008  -0.0286 0.0152  131 ASN B O   
5306  C CB  . ASN B 131 ? 0.3768 0.3388 0.5694 -0.0051 -0.0245 0.0081  131 ASN B CB  
5307  C CG  . ASN B 131 ? 0.3917 0.3597 0.5964 -0.0036 -0.0237 0.0088  131 ASN B CG  
5308  O OD1 . ASN B 131 ? 0.4355 0.4022 0.6439 -0.0033 -0.0192 0.0086  131 ASN B OD1 
5309  N ND2 . ASN B 131 ? 0.4158 0.3908 0.6265 -0.0023 -0.0280 0.0098  131 ASN B ND2 
5310  N N   . GLU B 132 ? 0.3863 0.3383 0.5715 0.0006  -0.0194 0.0160  132 GLU B N   
5311  C CA  . GLU B 132 ? 0.3922 0.3434 0.5801 0.0036  -0.0206 0.0191  132 GLU B CA  
5312  C C   . GLU B 132 ? 0.3955 0.3411 0.5732 0.0053  -0.0234 0.0225  132 GLU B C   
5313  O O   . GLU B 132 ? 0.4313 0.3783 0.6103 0.0086  -0.0278 0.0244  132 GLU B O   
5314  C CB  . GLU B 132 ? 0.3903 0.3492 0.5890 0.0054  -0.0237 0.0181  132 GLU B CB  
5315  C CG  . GLU B 132 ? 0.3902 0.3481 0.5942 0.0083  -0.0224 0.0199  132 GLU B CG  
5316  C CD  . GLU B 132 ? 0.3862 0.3418 0.5929 0.0064  -0.0170 0.0188  132 GLU B CD  
5317  O OE1 . GLU B 132 ? 0.3736 0.3345 0.5883 0.0056  -0.0157 0.0165  132 GLU B OE1 
5318  O OE2 . GLU B 132 ? 0.3908 0.3396 0.5913 0.0052  -0.0142 0.0204  132 GLU B OE2 
5319  N N   . PRO B 133 ? 0.3744 0.3133 0.5416 0.0036  -0.0206 0.0237  133 PRO B N   
5320  C CA  . PRO B 133 ? 0.3869 0.3190 0.5435 0.0051  -0.0226 0.0277  133 PRO B CA  
5321  C C   . PRO B 133 ? 0.4109 0.3380 0.5697 0.0072  -0.0215 0.0308  133 PRO B C   
5322  O O   . PRO B 133 ? 0.3634 0.2886 0.5257 0.0053  -0.0167 0.0305  133 PRO B O   
5323  C CB  . PRO B 133 ? 0.3944 0.3216 0.5408 0.0021  -0.0181 0.0276  133 PRO B CB  
5324  C CG  . PRO B 133 ? 0.3795 0.3096 0.5337 -0.0001 -0.0124 0.0252  133 PRO B CG  
5325  C CD  . PRO B 133 ? 0.3866 0.3242 0.5519 0.0006  -0.0149 0.0219  133 PRO B CD  
5326  N N   . GLN B 134 ? 0.4246 0.3502 0.5818 0.0115  -0.0265 0.0335  134 GLN B N   
5327  C CA  . GLN B 134 ? 0.4629 0.3817 0.6202 0.0146  -0.0264 0.0367  134 GLN B CA  
5328  C C   . GLN B 134 ? 0.4401 0.3467 0.5844 0.0130  -0.0238 0.0407  134 GLN B C   
5329  O O   . GLN B 134 ? 0.4670 0.3705 0.6005 0.0123  -0.0250 0.0425  134 GLN B O   
5330  C CB  . GLN B 134 ? 0.5433 0.4655 0.7027 0.0206  -0.0329 0.0383  134 GLN B CB  
5331  C CG  . GLN B 134 ? 0.5503 0.4847 0.7239 0.0225  -0.0350 0.0350  134 GLN B CG  
5332  C CD  . GLN B 134 ? 0.6484 0.5812 0.8300 0.0238  -0.0315 0.0341  134 GLN B CD  
5333  O OE1 . GLN B 134 ? 0.6947 0.6168 0.8715 0.0247  -0.0291 0.0364  134 GLN B OE1 
5334  N NE2 . GLN B 134 ? 0.7410 0.6840 0.9342 0.0233  -0.0310 0.0307  134 GLN B NE2 
5335  N N   . THR B 135 ? 0.4426 0.3418 0.5873 0.0121  -0.0202 0.0420  135 THR B N   
5336  C CA  . THR B 135 ? 0.4432 0.3300 0.5762 0.0095  -0.0172 0.0460  135 THR B CA  
5337  C C   . THR B 135 ? 0.4580 0.3369 0.5785 0.0132  -0.0215 0.0507  135 THR B C   
5338  O O   . THR B 135 ? 0.4736 0.3477 0.5825 0.0105  -0.0200 0.0530  135 THR B O   
5339  C CB  . THR B 135 ? 0.4402 0.3192 0.5758 0.0088  -0.0145 0.0468  135 THR B CB  
5340  O OG1 . THR B 135 ? 0.4307 0.3187 0.5787 0.0066  -0.0120 0.0423  135 THR B OG1 
5341  C CG2 . THR B 135 ? 0.4603 0.3282 0.5856 0.0036  -0.0100 0.0501  135 THR B CG2 
5342  N N   . ASP B 136 ? 0.4586 0.3365 0.5808 0.0198  -0.0267 0.0522  136 ASP B N   
5343  C CA  . ASP B 136 ? 0.4764 0.3456 0.5863 0.0242  -0.0311 0.0573  136 ASP B CA  
5344  C C   . ASP B 136 ? 0.4793 0.3551 0.5830 0.0237  -0.0345 0.0572  136 ASP B C   
5345  O O   . ASP B 136 ? 0.5025 0.3698 0.5918 0.0239  -0.0357 0.0614  136 ASP B O   
5346  C CB  . ASP B 136 ? 0.4740 0.3425 0.5883 0.0325  -0.0361 0.0589  136 ASP B CB  
5347  C CG  . ASP B 136 ? 0.4944 0.3532 0.5956 0.0382  -0.0410 0.0648  136 ASP B CG  
5348  O OD1 . ASP B 136 ? 0.5042 0.3462 0.5948 0.0387  -0.0389 0.0691  136 ASP B OD1 
5349  O OD2 . ASP B 136 ? 0.4864 0.3541 0.5876 0.0418  -0.0470 0.0651  136 ASP B OD2 
5350  N N   . HIS B 137 ? 0.4524 0.3421 0.5660 0.0225  -0.0360 0.0523  137 HIS B N   
5351  C CA  . HIS B 137 ? 0.4361 0.3320 0.5443 0.0213  -0.0393 0.0510  137 HIS B CA  
5352  C C   . HIS B 137 ? 0.4276 0.3173 0.5240 0.0156  -0.0339 0.0514  137 HIS B C   
5353  O O   . HIS B 137 ? 0.4385 0.3233 0.5211 0.0157  -0.0360 0.0540  137 HIS B O   
5354  C CB  . HIS B 137 ? 0.4110 0.3213 0.5323 0.0203  -0.0412 0.0455  137 HIS B CB  
5355  C CG  . HIS B 137 ? 0.4368 0.3519 0.5512 0.0190  -0.0455 0.0442  137 HIS B CG  
5356  N ND1 . HIS B 137 ? 0.4666 0.3804 0.5717 0.0226  -0.0521 0.0476  137 HIS B ND1 
5357  C CD2 . HIS B 137 ? 0.4245 0.3445 0.5386 0.0144  -0.0442 0.0398  137 HIS B CD2 
5358  C CE1 . HIS B 137 ? 0.4835 0.4017 0.5829 0.0197  -0.0549 0.0450  137 HIS B CE1 
5359  N NE2 . HIS B 137 ? 0.4398 0.3609 0.5440 0.0147  -0.0499 0.0402  137 HIS B NE2 
5360  N N   . ILE B 138 ? 0.4042 0.2943 0.5059 0.0110  -0.0270 0.0490  138 ILE B N   
5361  C CA  . ILE B 138 ? 0.4043 0.2905 0.4970 0.0059  -0.0209 0.0491  138 ILE B CA  
5362  C C   . ILE B 138 ? 0.4567 0.3298 0.5344 0.0055  -0.0194 0.0551  138 ILE B C   
5363  O O   . ILE B 138 ? 0.4708 0.3403 0.5356 0.0033  -0.0177 0.0566  138 ILE B O   
5364  C CB  . ILE B 138 ? 0.3834 0.2736 0.4863 0.0018  -0.0142 0.0461  138 ILE B CB  
5365  C CG1 . ILE B 138 ? 0.3627 0.2643 0.4791 0.0021  -0.0151 0.0406  138 ILE B CG1 
5366  C CG2 . ILE B 138 ? 0.4043 0.2920 0.4984 -0.0028 -0.0077 0.0466  138 ILE B CG2 
5367  C CD1 . ILE B 138 ? 0.3516 0.2575 0.4776 -0.0012 -0.0090 0.0379  138 ILE B CD1 
5368  N N   . HIS B 139 ? 0.4570 0.3219 0.5355 0.0074  -0.0198 0.0586  139 HIS B N   
5369  C CA  . HIS B 139 ? 0.4837 0.3339 0.5474 0.0072  -0.0188 0.0649  139 HIS B CA  
5370  C C   . HIS B 139 ? 0.5033 0.3504 0.5537 0.0111  -0.0247 0.0681  139 HIS B C   
5371  O O   . HIS B 139 ? 0.5279 0.3664 0.5629 0.0088  -0.0226 0.0719  139 HIS B O   
5372  C CB  . HIS B 139 ? 0.4902 0.3309 0.5570 0.0098  -0.0194 0.0676  139 HIS B CB  
5373  C CG  . HIS B 139 ? 0.4870 0.3104 0.5381 0.0094  -0.0182 0.0741  139 HIS B CG  
5374  N ND1 . HIS B 139 ? 0.4876 0.3028 0.5286 0.0160  -0.0244 0.0788  139 HIS B ND1 
5375  C CD2 . HIS B 139 ? 0.4933 0.3057 0.5366 0.0032  -0.0120 0.0772  139 HIS B CD2 
5376  C CE1 . HIS B 139 ? 0.5034 0.3014 0.5301 0.0141  -0.0217 0.0847  139 HIS B CE1 
5377  N NE2 . HIS B 139 ? 0.5112 0.3073 0.5391 0.0060  -0.0141 0.0838  139 HIS B NE2 
5378  N N   . SER B 140 ? 0.5082 0.3631 0.5645 0.0168  -0.0322 0.0666  140 SER B N   
5379  C CA  . SER B 140 ? 0.5269 0.3799 0.5715 0.0212  -0.0393 0.0699  140 SER B CA  
5380  C C   . SER B 140 ? 0.5203 0.3771 0.5549 0.0176  -0.0391 0.0679  140 SER B C   
5381  O O   . SER B 140 ? 0.5340 0.3836 0.5521 0.0185  -0.0413 0.0720  140 SER B O   
5382  C CB  . SER B 140 ? 0.5247 0.3874 0.5804 0.0280  -0.0474 0.0686  140 SER B CB  
5383  O OG  . SER B 140 ? 0.5689 0.4318 0.6142 0.0324  -0.0550 0.0718  140 SER B OG  
5384  N N   . VAL B 141 ? 0.4954 0.3628 0.5392 0.0138  -0.0364 0.0617  141 VAL B N   
5385  C CA  . VAL B 141 ? 0.4797 0.3501 0.5143 0.0106  -0.0358 0.0588  141 VAL B CA  
5386  C C   . VAL B 141 ? 0.4938 0.3585 0.5207 0.0052  -0.0264 0.0590  141 VAL B C   
5387  O O   . VAL B 141 ? 0.4942 0.3579 0.5089 0.0031  -0.0249 0.0580  141 VAL B O   
5388  C CB  . VAL B 141 ? 0.4682 0.3517 0.5154 0.0099  -0.0384 0.0520  141 VAL B CB  
5389  C CG1 . VAL B 141 ? 0.4683 0.3593 0.5237 0.0148  -0.0475 0.0521  141 VAL B CG1 
5390  C CG2 . VAL B 141 ? 0.4339 0.3227 0.4957 0.0069  -0.0319 0.0477  141 VAL B CG2 
5391  N N   . THR B 142 ? 0.5175 0.3789 0.5512 0.0030  -0.0202 0.0604  142 THR B N   
5392  C CA  . THR B 142 ? 0.4932 0.3500 0.5218 -0.0024 -0.0110 0.0618  142 THR B CA  
5393  C C   . THR B 142 ? 0.4889 0.3562 0.5313 -0.0054 -0.0056 0.0559  142 THR B C   
5394  O O   . THR B 142 ? 0.4780 0.3536 0.5256 -0.0044 -0.0078 0.0508  142 THR B O   
5395  C CB  . THR B 142 ? 0.4978 0.3481 0.5070 -0.0046 -0.0080 0.0645  142 THR B CB  
5396  O OG1 . THR B 142 ? 0.4806 0.3380 0.4872 -0.0049 -0.0082 0.0594  142 THR B OG1 
5397  C CG2 . THR B 142 ? 0.5128 0.3516 0.5060 -0.0015 -0.0133 0.0710  142 THR B CG2 
5398  N N   . GLY B 143 ? 0.4762 0.3427 0.5242 -0.0092 0.0012  0.0569  143 GLY B N   
5399  C CA  . GLY B 143 ? 0.4464 0.3226 0.5063 -0.0121 0.0071  0.0523  143 GLY B CA  
5400  C C   . GLY B 143 ? 0.4653 0.3454 0.5177 -0.0132 0.0109  0.0495  143 GLY B C   
5401  O O   . GLY B 143 ? 0.4739 0.3623 0.5345 -0.0125 0.0117  0.0443  143 GLY B O   
5402  N N   . LYS B 144 ? 0.4970 0.3700 0.5325 -0.0144 0.0129  0.0529  144 LYS B N   
5403  C CA  . LYS B 144 ? 0.5344 0.4098 0.5605 -0.0150 0.0168  0.0502  144 LYS B CA  
5404  C C   . LYS B 144 ? 0.5359 0.4152 0.5629 -0.0116 0.0108  0.0449  144 LYS B C   
5405  O O   . LYS B 144 ? 0.4944 0.3795 0.5250 -0.0117 0.0142  0.0398  144 LYS B O   
5406  C CB  . LYS B 144 ? 0.5693 0.4353 0.5752 -0.0166 0.0191  0.0551  144 LYS B CB  
5407  C CG  . LYS B 144 ? 0.5997 0.4676 0.5944 -0.0173 0.0245  0.0523  144 LYS B CG  
5408  C CD  . LYS B 144 ? 0.6460 0.5046 0.6203 -0.0193 0.0278  0.0577  144 LYS B CD  
5409  C CE  . LYS B 144 ? 0.6869 0.5452 0.6462 -0.0187 0.0309  0.0547  144 LYS B CE  
5410  N NZ  . LYS B 144 ? 0.6894 0.5577 0.6591 -0.0184 0.0368  0.0484  144 LYS B NZ  
5411  N N   . ALA B 145 ? 0.4963 0.3726 0.5205 -0.0087 0.0019  0.0459  145 ALA B N   
5412  C CA  . ALA B 145 ? 0.4895 0.3696 0.5133 -0.0068 -0.0040 0.0410  145 ALA B CA  
5413  C C   . ALA B 145 ? 0.4560 0.3450 0.4980 -0.0066 -0.0036 0.0358  145 ALA B C   
5414  O O   . ALA B 145 ? 0.4499 0.3420 0.4921 -0.0066 -0.0041 0.0306  145 ALA B O   
5415  C CB  . ALA B 145 ? 0.4952 0.3726 0.5143 -0.0038 -0.0138 0.0436  145 ALA B CB  
5416  N N   . PHE B 146 ? 0.4479 0.3396 0.5039 -0.0064 -0.0030 0.0374  146 PHE B N   
5417  C CA  . PHE B 146 ? 0.4351 0.3347 0.5078 -0.0062 -0.0025 0.0332  146 PHE B CA  
5418  C C   . PHE B 146 ? 0.4562 0.3595 0.5310 -0.0079 0.0054  0.0298  146 PHE B C   
5419  O O   . PHE B 146 ? 0.4858 0.3931 0.5653 -0.0073 0.0054  0.0249  146 PHE B O   
5420  C CB  . PHE B 146 ? 0.4230 0.3241 0.5084 -0.0059 -0.0028 0.0356  146 PHE B CB  
5421  C CG  . PHE B 146 ? 0.4002 0.3092 0.5018 -0.0060 -0.0009 0.0317  146 PHE B CG  
5422  C CD1 . PHE B 146 ? 0.3776 0.2918 0.4873 -0.0044 -0.0058 0.0281  146 PHE B CD1 
5423  C CD2 . PHE B 146 ? 0.3878 0.2997 0.4965 -0.0082 0.0057  0.0317  146 PHE B CD2 
5424  C CE1 . PHE B 146 ? 0.3472 0.2677 0.4704 -0.0045 -0.0040 0.0250  146 PHE B CE1 
5425  C CE2 . PHE B 146 ? 0.3556 0.2747 0.4780 -0.0080 0.0069  0.0284  146 PHE B CE2 
5426  C CZ  . PHE B 146 ? 0.3374 0.2600 0.4667 -0.0060 0.0021  0.0253  146 PHE B CZ  
5427  N N   . VAL B 147 ? 0.4380 0.3399 0.5094 -0.0100 0.0124  0.0326  147 VAL B N   
5428  C CA  . VAL B 147 ? 0.4386 0.3459 0.5133 -0.0110 0.0202  0.0299  147 VAL B CA  
5429  C C   . VAL B 147 ? 0.4290 0.3344 0.4924 -0.0096 0.0214  0.0258  147 VAL B C   
5430  O O   . VAL B 147 ? 0.3963 0.3060 0.4652 -0.0083 0.0245  0.0214  147 VAL B O   
5431  C CB  . VAL B 147 ? 0.4275 0.3347 0.5001 -0.0141 0.0274  0.0340  147 VAL B CB  
5432  C CG1 . VAL B 147 ? 0.4194 0.3332 0.4931 -0.0146 0.0360  0.0316  147 VAL B CG1 
5433  C CG2 . VAL B 147 ? 0.4249 0.3337 0.5097 -0.0160 0.0267  0.0367  147 VAL B CG2 
5434  N N   . ASP B 148 ? 0.4506 0.3489 0.4973 -0.0098 0.0194  0.0275  148 ASP B N   
5435  C CA  . ASP B 148 ? 0.4942 0.3888 0.5269 -0.0089 0.0203  0.0239  148 ASP B CA  
5436  C C   . ASP B 148 ? 0.4953 0.3910 0.5326 -0.0075 0.0146  0.0183  148 ASP B C   
5437  O O   . ASP B 148 ? 0.4691 0.3642 0.5032 -0.0065 0.0177  0.0134  148 ASP B O   
5438  C CB  . ASP B 148 ? 0.5024 0.3890 0.5161 -0.0095 0.0176  0.0271  148 ASP B CB  
5439  C CG  . ASP B 148 ? 0.5278 0.4115 0.5322 -0.0115 0.0247  0.0321  148 ASP B CG  
5440  O OD1 . ASP B 148 ? 0.5112 0.4004 0.5240 -0.0128 0.0325  0.0327  148 ASP B OD1 
5441  O OD2 . ASP B 148 ? 0.5772 0.4535 0.5659 -0.0120 0.0222  0.0358  148 ASP B OD2 
5442  N N   . LEU B 149 ? 0.4734 0.3705 0.5183 -0.0073 0.0066  0.0193  149 LEU B N   
5443  C CA  . LEU B 149 ? 0.4779 0.3768 0.5284 -0.0070 0.0009  0.0147  149 LEU B CA  
5444  C C   . LEU B 149 ? 0.4519 0.3557 0.5159 -0.0064 0.0055  0.0112  149 LEU B C   
5445  O O   . LEU B 149 ? 0.4554 0.3578 0.5182 -0.0061 0.0056  0.0062  149 LEU B O   
5446  C CB  . LEU B 149 ? 0.4963 0.3979 0.5540 -0.0067 -0.0078 0.0169  149 LEU B CB  
5447  C CG  . LEU B 149 ? 0.5008 0.4060 0.5659 -0.0072 -0.0136 0.0124  149 LEU B CG  
5448  C CD1 . LEU B 149 ? 0.5132 0.4135 0.5639 -0.0087 -0.0163 0.0080  149 LEU B CD1 
5449  C CD2 . LEU B 149 ? 0.5008 0.4109 0.5750 -0.0064 -0.0211 0.0150  149 LEU B CD2 
5450  N N   . MET B 150 ? 0.4382 0.3471 0.5146 -0.0062 0.0090  0.0139  150 MET B N   
5451  C CA  . MET B 150 ? 0.4303 0.3444 0.5197 -0.0053 0.0128  0.0112  150 MET B CA  
5452  C C   . MET B 150 ? 0.4393 0.3519 0.5220 -0.0039 0.0198  0.0079  150 MET B C   
5453  O O   . MET B 150 ? 0.4287 0.3406 0.5136 -0.0026 0.0202  0.0035  150 MET B O   
5454  C CB  . MET B 150 ? 0.4156 0.3354 0.5177 -0.0058 0.0153  0.0148  150 MET B CB  
5455  C CG  . MET B 150 ? 0.4119 0.3330 0.5223 -0.0060 0.0090  0.0170  150 MET B CG  
5456  S SD  . MET B 150 ? 0.4339 0.3583 0.5547 -0.0052 0.0033  0.0131  150 MET B SD  
5457  C CE  . MET B 150 ? 0.4666 0.3868 0.5764 -0.0056 -0.0047 0.0131  150 MET B CE  
5458  N N   . ASN B 151 ? 0.4525 0.3643 0.5264 -0.0041 0.0256  0.0100  151 ASN B N   
5459  C CA  . ASN B 151 ? 0.4853 0.3971 0.5538 -0.0021 0.0333  0.0072  151 ASN B CA  
5460  C C   . ASN B 151 ? 0.5063 0.4099 0.5619 -0.0008 0.0313  0.0019  151 ASN B C   
5461  O O   . ASN B 151 ? 0.5226 0.4250 0.5771 0.0019  0.0359  -0.0022 151 ASN B O   
5462  C CB  . ASN B 151 ? 0.4792 0.3922 0.5399 -0.0030 0.0401  0.0106  151 ASN B CB  
5463  C CG  . ASN B 151 ? 0.4826 0.4048 0.5568 -0.0044 0.0447  0.0144  151 ASN B CG  
5464  O OD1 . ASN B 151 ? 0.4812 0.4103 0.5702 -0.0032 0.0454  0.0132  151 ASN B OD1 
5465  N ND2 . ASN B 151 ? 0.4669 0.3890 0.5355 -0.0072 0.0478  0.0190  151 ASN B ND2 
5466  N N   . THR B 152 ? 0.4943 0.3918 0.5392 -0.0028 0.0244  0.0020  152 THR B N   
5467  C CA  . THR B 152 ? 0.5233 0.4123 0.5541 -0.0028 0.0217  -0.0030 152 THR B CA  
5468  C C   . THR B 152 ? 0.5109 0.3992 0.5504 -0.0024 0.0189  -0.0076 152 THR B C   
5469  O O   . THR B 152 ? 0.5211 0.4031 0.5533 -0.0010 0.0216  -0.0127 152 THR B O   
5470  C CB  . THR B 152 ? 0.5419 0.4268 0.5616 -0.0053 0.0138  -0.0012 152 THR B CB  
5471  O OG1 . THR B 152 ? 0.5885 0.4724 0.5983 -0.0052 0.0186  0.0028  152 THR B OG1 
5472  C CG2 . THR B 152 ? 0.5383 0.4152 0.5441 -0.0064 0.0092  -0.0066 152 THR B CG2 
5473  N N   . LEU B 153 ? 0.4724 0.3666 0.5271 -0.0036 0.0140  -0.0057 153 LEU B N   
5474  C CA  . LEU B 153 ? 0.4640 0.3576 0.5267 -0.0043 0.0104  -0.0092 153 LEU B CA  
5475  C C   . LEU B 153 ? 0.4622 0.3575 0.5336 -0.0011 0.0172  -0.0110 153 LEU B C   
5476  O O   . LEU B 153 ? 0.4590 0.3486 0.5288 -0.0005 0.0172  -0.0153 153 LEU B O   
5477  C CB  . LEU B 153 ? 0.4519 0.3521 0.5272 -0.0063 0.0035  -0.0062 153 LEU B CB  
5478  C CG  . LEU B 153 ? 0.4516 0.3514 0.5201 -0.0085 -0.0042 -0.0043 153 LEU B CG  
5479  C CD1 . LEU B 153 ? 0.4415 0.3489 0.5246 -0.0093 -0.0099 -0.0016 153 LEU B CD1 
5480  C CD2 . LEU B 153 ? 0.4821 0.3753 0.5381 -0.0109 -0.0090 -0.0088 153 LEU B CD2 
5481  N N   . ILE B 154 ? 0.4195 0.3227 0.5007 0.0007  0.0221  -0.0072 154 ILE B N   
5482  C CA  . ILE B 154 ? 0.4131 0.3201 0.5024 0.0043  0.0288  -0.0082 154 ILE B CA  
5483  C C   . ILE B 154 ? 0.4199 0.3196 0.4964 0.0076  0.0344  -0.0124 154 ILE B C   
5484  O O   . ILE B 154 ? 0.4133 0.3098 0.4919 0.0106  0.0368  -0.0156 154 ILE B O   
5485  C CB  . ILE B 154 ? 0.3773 0.2943 0.4761 0.0048  0.0333  -0.0035 154 ILE B CB  
5486  C CG1 . ILE B 154 ? 0.3781 0.3010 0.4897 0.0023  0.0285  0.0000  154 ILE B CG1 
5487  C CG2 . ILE B 154 ? 0.3621 0.2845 0.4676 0.0090  0.0407  -0.0045 154 ILE B CG2 
5488  C CD1 . ILE B 154 ? 0.3825 0.3114 0.4978 0.0007  0.0310  0.0048  154 ILE B CD1 
5489  N N   . ASN B 155 ? 0.4349 0.3314 0.4977 0.0073  0.0369  -0.0122 155 ASN B N   
5490  C CA  . ASN B 155 ? 0.4921 0.3814 0.5414 0.0107  0.0428  -0.0164 155 ASN B CA  
5491  C C   . ASN B 155 ? 0.5080 0.3848 0.5479 0.0102  0.0386  -0.0222 155 ASN B C   
5492  O O   . ASN B 155 ? 0.5174 0.3876 0.5524 0.0142  0.0432  -0.0263 155 ASN B O   
5493  C CB  . ASN B 155 ? 0.5234 0.4114 0.5586 0.0099  0.0459  -0.0148 155 ASN B CB  
5494  C CG  . ASN B 155 ? 0.5970 0.4777 0.6179 0.0141  0.0528  -0.0194 155 ASN B CG  
5495  O OD1 . ASN B 155 ? 0.6690 0.5540 0.6960 0.0191  0.0601  -0.0204 155 ASN B OD1 
5496  N ND2 . ASN B 155 ? 0.6206 0.4904 0.6225 0.0125  0.0504  -0.0225 155 ASN B ND2 
5497  N N   . ILE B 156 ? 0.4965 0.3695 0.5332 0.0053  0.0300  -0.0225 156 ILE B N   
5498  C CA  . ILE B 156 ? 0.4926 0.3542 0.5202 0.0033  0.0256  -0.0279 156 ILE B CA  
5499  C C   . ILE B 156 ? 0.4739 0.3344 0.5129 0.0049  0.0263  -0.0297 156 ILE B C   
5500  O O   . ILE B 156 ? 0.4589 0.3078 0.4892 0.0061  0.0277  -0.0348 156 ILE B O   
5501  C CB  . ILE B 156 ? 0.4907 0.3521 0.5149 -0.0026 0.0158  -0.0272 156 ILE B CB  
5502  C CG1 . ILE B 156 ? 0.5246 0.3807 0.5300 -0.0039 0.0148  -0.0278 156 ILE B CG1 
5503  C CG2 . ILE B 156 ? 0.4905 0.3456 0.5150 -0.0065 0.0095  -0.0313 156 ILE B CG2 
5504  C CD1 . ILE B 156 ? 0.5271 0.3878 0.5322 -0.0082 0.0058  -0.0245 156 ILE B CD1 
5505  N N   . ILE B 157 ? 0.4199 0.2914 0.4771 0.0052  0.0257  -0.0255 157 ILE B N   
5506  C CA  . ILE B 157 ? 0.4382 0.3087 0.5057 0.0066  0.0261  -0.0266 157 ILE B CA  
5507  C C   . ILE B 157 ? 0.4617 0.3304 0.5288 0.0135  0.0346  -0.0280 157 ILE B C   
5508  O O   . ILE B 157 ? 0.4939 0.3537 0.5589 0.0157  0.0358  -0.0313 157 ILE B O   
5509  C CB  . ILE B 157 ? 0.4309 0.3131 0.5168 0.0049  0.0227  -0.0221 157 ILE B CB  
5510  C CG1 . ILE B 157 ? 0.4443 0.3285 0.5317 -0.0010 0.0142  -0.0211 157 ILE B CG1 
5511  C CG2 . ILE B 157 ? 0.4282 0.3094 0.5236 0.0071  0.0242  -0.0229 157 ILE B CG2 
5512  C CD1 . ILE B 157 ? 0.4128 0.3090 0.5150 -0.0020 0.0118  -0.0161 157 ILE B CD1 
5513  N N   . HIS B 158 ? 0.4462 0.3231 0.5150 0.0170  0.0406  -0.0255 158 HIS B N   
5514  C CA  . HIS B 158 ? 0.4400 0.3182 0.5102 0.0241  0.0487  -0.0264 158 HIS B CA  
5515  C C   . HIS B 158 ? 0.4850 0.3481 0.5375 0.0274  0.0522  -0.0322 158 HIS B C   
5516  O O   . HIS B 158 ? 0.4786 0.3374 0.5312 0.0336  0.0571  -0.0344 158 HIS B O   
5517  C CB  . HIS B 158 ? 0.4149 0.3064 0.4906 0.0261  0.0544  -0.0225 158 HIS B CB  
5518  C CG  . HIS B 158 ? 0.3785 0.2844 0.4721 0.0242  0.0530  -0.0173 158 HIS B CG  
5519  N ND1 . HIS B 158 ? 0.3763 0.2934 0.4742 0.0234  0.0565  -0.0133 158 HIS B ND1 
5520  C CD2 . HIS B 158 ? 0.3603 0.2706 0.4672 0.0229  0.0488  -0.0155 158 HIS B CD2 
5521  C CE1 . HIS B 158 ? 0.3615 0.2889 0.4750 0.0216  0.0544  -0.0096 158 HIS B CE1 
5522  N NE2 . HIS B 158 ? 0.3463 0.2698 0.4652 0.0215  0.0497  -0.0109 158 HIS B NE2 
5523  N N   . LYS B 159 ? 0.5161 0.3706 0.5526 0.0237  0.0495  -0.0348 159 LYS B N   
5524  C CA  . LYS B 159 ? 0.5593 0.3980 0.5770 0.0263  0.0526  -0.0408 159 LYS B CA  
5525  C C   . LYS B 159 ? 0.5545 0.3786 0.5667 0.0230  0.0469  -0.0452 159 LYS B C   
5526  O O   . LYS B 159 ? 0.6072 0.4177 0.6094 0.0270  0.0506  -0.0499 159 LYS B O   
5527  C CB  . LYS B 159 ? 0.6340 0.4685 0.6343 0.0239  0.0527  -0.0423 159 LYS B CB  
5528  C CG  . LYS B 159 ? 0.7266 0.5716 0.7273 0.0281  0.0609  -0.0393 159 LYS B CG  
5529  C CD  . LYS B 159 ? 0.8615 0.7016 0.8430 0.0270  0.0630  -0.0406 159 LYS B CD  
5530  C CE  . LYS B 159 ? 0.9140 0.7683 0.9003 0.0275  0.0683  -0.0351 159 LYS B CE  
5531  N NZ  . LYS B 159 ? 0.8790 0.7478 0.8829 0.0321  0.0751  -0.0316 159 LYS B NZ  
5532  N N   . GLY B 160 ? 0.5278 0.3547 0.5466 0.0157  0.0384  -0.0435 160 GLY B N   
5533  C CA  . GLY B 160 ? 0.5155 0.3300 0.5286 0.0104  0.0321  -0.0474 160 GLY B CA  
5534  C C   . GLY B 160 ? 0.5059 0.3188 0.5308 0.0119  0.0325  -0.0468 160 GLY B C   
5535  O O   . GLY B 160 ? 0.5416 0.3393 0.5584 0.0108  0.0316  -0.0511 160 GLY B O   
5536  N N   . HIS B 161 ? 0.4603 0.2880 0.5035 0.0142  0.0336  -0.0415 161 HIS B N   
5537  C CA  . HIS B 161 ? 0.4286 0.2560 0.4828 0.0168  0.0347  -0.0403 161 HIS B CA  
5538  C C   . HIS B 161 ? 0.4138 0.2521 0.4779 0.0249  0.0417  -0.0370 161 HIS B C   
5539  O O   . HIS B 161 ? 0.3925 0.2456 0.4720 0.0247  0.0409  -0.0323 161 HIS B O   
5540  C CB  . HIS B 161 ? 0.4024 0.2364 0.4689 0.0100  0.0276  -0.0375 161 HIS B CB  
5541  C CG  . HIS B 161 ? 0.4025 0.2320 0.4760 0.0111  0.0279  -0.0372 161 HIS B CG  
5542  N ND1 . HIS B 161 ? 0.3886 0.2221 0.4720 0.0054  0.0225  -0.0352 161 HIS B ND1 
5543  C CD2 . HIS B 161 ? 0.4083 0.2297 0.4801 0.0178  0.0331  -0.0381 161 HIS B CD2 
5544  C CE1 . HIS B 161 ? 0.3944 0.2217 0.4811 0.0080  0.0246  -0.0349 161 HIS B CE1 
5545  N NE2 . HIS B 161 ? 0.3910 0.2106 0.4706 0.0156  0.0307  -0.0366 161 HIS B NE2 
5546  N N   . PRO B 162 ? 0.4369 0.2686 0.4926 0.0324  0.0488  -0.0396 162 PRO B N   
5547  C CA  . PRO B 162 ? 0.4304 0.2751 0.4956 0.0401  0.0556  -0.0366 162 PRO B CA  
5548  C C   . PRO B 162 ? 0.4236 0.2775 0.5060 0.0426  0.0552  -0.0327 162 PRO B C   
5549  O O   . PRO B 162 ? 0.4501 0.2945 0.5327 0.0427  0.0530  -0.0337 162 PRO B O   
5550  C CB  . PRO B 162 ? 0.4521 0.2850 0.5037 0.0479  0.0627  -0.0411 162 PRO B CB  
5551  C CG  . PRO B 162 ? 0.4718 0.2875 0.5041 0.0427  0.0595  -0.0463 162 PRO B CG  
5552  C CD  . PRO B 162 ? 0.4653 0.2773 0.5016 0.0339  0.0507  -0.0458 162 PRO B CD  
5553  N N   . GLY B 163 ? 0.4111 0.2834 0.5073 0.0441  0.0572  -0.0282 163 GLY B N   
5554  C CA  . GLY B 163 ? 0.3979 0.2801 0.5092 0.0482  0.0581  -0.0248 163 GLY B CA  
5555  C C   . GLY B 163 ? 0.4031 0.2919 0.5261 0.0417  0.0515  -0.0215 163 GLY B C   
5556  O O   . GLY B 163 ? 0.4453 0.3423 0.5803 0.0443  0.0515  -0.0186 163 GLY B O   
5557  N N   . ILE B 164 ? 0.3842 0.2696 0.5035 0.0339  0.0459  -0.0220 164 ILE B N   
5558  C CA  . ILE B 164 ? 0.3645 0.2554 0.4941 0.0281  0.0399  -0.0193 164 ILE B CA  
5559  C C   . ILE B 164 ? 0.3638 0.2692 0.5017 0.0250  0.0388  -0.0156 164 ILE B C   
5560  O O   . ILE B 164 ? 0.3669 0.2716 0.4977 0.0221  0.0381  -0.0161 164 ILE B O   
5561  C CB  . ILE B 164 ? 0.3503 0.2301 0.4724 0.0216  0.0341  -0.0218 164 ILE B CB  
5562  C CG1 . ILE B 164 ? 0.3768 0.2395 0.4877 0.0233  0.0353  -0.0259 164 ILE B CG1 
5563  C CG2 . ILE B 164 ? 0.3342 0.2210 0.4682 0.0169  0.0290  -0.0189 164 ILE B CG2 
5564  C CD1 . ILE B 164 ? 0.3722 0.2325 0.4892 0.0279  0.0371  -0.0247 164 ILE B CD1 
5565  N N   . PRO B 165 ? 0.3626 0.2801 0.5144 0.0257  0.0387  -0.0120 165 PRO B N   
5566  C CA  . PRO B 165 ? 0.3590 0.2884 0.5182 0.0223  0.0377  -0.0086 165 PRO B CA  
5567  C C   . PRO B 165 ? 0.3780 0.3045 0.5341 0.0160  0.0320  -0.0084 165 PRO B C   
5568  O O   . PRO B 165 ? 0.3995 0.3200 0.5549 0.0134  0.0276  -0.0096 165 PRO B O   
5569  C CB  . PRO B 165 ? 0.3462 0.2851 0.5193 0.0232  0.0370  -0.0058 165 PRO B CB  
5570  C CG  . PRO B 165 ? 0.3593 0.2953 0.5323 0.0298  0.0405  -0.0071 165 PRO B CG  
5571  C CD  . PRO B 165 ? 0.3520 0.2718 0.5119 0.0300  0.0400  -0.0110 165 PRO B CD  
5572  N N   . VAL B 166 ? 0.3667 0.2975 0.5206 0.0139  0.0323  -0.0066 166 VAL B N   
5573  C CA  . VAL B 166 ? 0.3721 0.3017 0.5236 0.0089  0.0269  -0.0055 166 VAL B CA  
5574  C C   . VAL B 166 ? 0.3420 0.2812 0.5032 0.0070  0.0261  -0.0014 166 VAL B C   
5575  O O   . VAL B 166 ? 0.3411 0.2869 0.5056 0.0083  0.0305  0.0004  166 VAL B O   
5576  C CB  . VAL B 166 ? 0.4028 0.3265 0.5401 0.0085  0.0282  -0.0069 166 VAL B CB  
5577  C CG1 . VAL B 166 ? 0.4066 0.3281 0.5389 0.0041  0.0223  -0.0059 166 VAL B CG1 
5578  C CG2 . VAL B 166 ? 0.4063 0.3197 0.5330 0.0110  0.0303  -0.0115 166 VAL B CG2 
5579  N N   . THR B 167 ? 0.3304 0.2703 0.4959 0.0040  0.0207  -0.0002 167 THR B N   
5580  C CA  . THR B 167 ? 0.3164 0.2623 0.4885 0.0020  0.0193  0.0034  167 THR B CA  
5581  C C   . THR B 167 ? 0.3255 0.2686 0.4960 -0.0005 0.0131  0.0038  167 THR B C   
5582  O O   . THR B 167 ? 0.3494 0.2869 0.5117 -0.0012 0.0106  0.0018  167 THR B O   
5583  C CB  . THR B 167 ? 0.2967 0.2497 0.4809 0.0028  0.0205  0.0045  167 THR B CB  
5584  O OG1 . THR B 167 ? 0.2888 0.2457 0.4765 0.0006  0.0199  0.0076  167 THR B OG1 
5585  C CG2 . THR B 167 ? 0.2903 0.2425 0.4802 0.0029  0.0172  0.0033  167 THR B CG2 
5586  N N   . LEU B 168 ? 0.3196 0.2666 0.4973 -0.0016 0.0106  0.0063  168 LEU B N   
5587  C CA  . LEU B 168 ? 0.3360 0.2818 0.5132 -0.0030 0.0050  0.0072  168 LEU B CA  
5588  C C   . LEU B 168 ? 0.3201 0.2704 0.5081 -0.0030 0.0028  0.0082  168 LEU B C   
5589  O O   . LEU B 168 ? 0.3091 0.2629 0.5040 -0.0025 0.0055  0.0087  168 LEU B O   
5590  C CB  . LEU B 168 ? 0.3209 0.2641 0.4904 -0.0036 0.0043  0.0100  168 LEU B CB  
5591  C CG  . LEU B 168 ? 0.3199 0.2649 0.4941 -0.0040 0.0051  0.0134  168 LEU B CG  
5592  C CD1 . LEU B 168 ? 0.3242 0.2644 0.4891 -0.0046 0.0038  0.0165  168 LEU B CD1 
5593  C CD2 . LEU B 168 ? 0.3108 0.2597 0.4898 -0.0044 0.0107  0.0138  168 LEU B CD2 
5594  N N   . SER B 169 ? 0.3392 0.2900 0.5285 -0.0034 -0.0022 0.0086  169 SER B N   
5595  C CA  . SER B 169 ? 0.3240 0.2788 0.5224 -0.0028 -0.0042 0.0096  169 SER B CA  
5596  C C   . SER B 169 ? 0.3537 0.3071 0.5508 -0.0020 -0.0053 0.0128  169 SER B C   
5597  O O   . SER B 169 ? 0.3735 0.3249 0.5655 -0.0015 -0.0088 0.0141  169 SER B O   
5598  C CB  . SER B 169 ? 0.3340 0.2913 0.5355 -0.0035 -0.0084 0.0081  169 SER B CB  
5599  O OG  . SER B 169 ? 0.3638 0.3258 0.5734 -0.0025 -0.0107 0.0091  169 SER B OG  
5600  N N   . ALA B 170 ? 0.3532 0.3069 0.5538 -0.0021 -0.0024 0.0140  170 ALA B N   
5601  C CA  . ALA B 170 ? 0.3413 0.2911 0.5389 -0.0020 -0.0026 0.0170  170 ALA B CA  
5602  C C   . ALA B 170 ? 0.3282 0.2793 0.5332 -0.0016 -0.0021 0.0173  170 ALA B C   
5603  O O   . ALA B 170 ? 0.3270 0.2811 0.5366 -0.0029 0.0009  0.0163  170 ALA B O   
5604  C CB  . ALA B 170 ? 0.3353 0.2821 0.5262 -0.0038 0.0012  0.0184  170 ALA B CB  
5605  N N   . ASN B 171 ? 0.3188 0.2679 0.5248 0.0004  -0.0052 0.0185  171 ASN B N   
5606  C CA  . ASN B 171 ? 0.3207 0.2697 0.5322 0.0013  -0.0048 0.0184  171 ASN B CA  
5607  C C   . ASN B 171 ? 0.3097 0.2534 0.5182 -0.0012 -0.0020 0.0198  171 ASN B C   
5608  O O   . ASN B 171 ? 0.3239 0.2612 0.5251 -0.0019 -0.0019 0.0223  171 ASN B O   
5609  C CB  . ASN B 171 ? 0.3354 0.2831 0.5479 0.0050  -0.0085 0.0193  171 ASN B CB  
5610  C CG  . ASN B 171 ? 0.3412 0.2896 0.5597 0.0065  -0.0079 0.0183  171 ASN B CG  
5611  O OD1 . ASN B 171 ? 0.3834 0.3262 0.5999 0.0053  -0.0059 0.0188  171 ASN B OD1 
5612  N ND2 . ASN B 171 ? 0.3293 0.2844 0.5547 0.0087  -0.0093 0.0167  171 ASN B ND2 
5613  N N   . ALA B 172 ? 0.3102 0.2566 0.5241 -0.0028 0.0002  0.0184  172 ALA B N   
5614  C CA  . ALA B 172 ? 0.2921 0.2355 0.5043 -0.0064 0.0029  0.0193  172 ALA B CA  
5615  C C   . ALA B 172 ? 0.3116 0.2450 0.5189 -0.0061 0.0018  0.0211  172 ALA B C   
5616  O O   . ALA B 172 ? 0.3281 0.2562 0.5311 -0.0098 0.0037  0.0227  172 ALA B O   
5617  C CB  . ALA B 172 ? 0.2748 0.2243 0.4940 -0.0079 0.0045  0.0171  172 ALA B CB  
5618  N N   . MET B 173 ? 0.3133 0.2442 0.5214 -0.0018 -0.0010 0.0209  173 MET B N   
5619  C CA  . MET B 173 ? 0.3170 0.2372 0.5201 -0.0004 -0.0020 0.0224  173 MET B CA  
5620  C C   . MET B 173 ? 0.3129 0.2249 0.5067 0.0003  -0.0031 0.0260  173 MET B C   
5621  O O   . MET B 173 ? 0.3254 0.2263 0.5126 -0.0003 -0.0027 0.0281  173 MET B O   
5622  C CB  . MET B 173 ? 0.3053 0.2264 0.5127 0.0049  -0.0040 0.0209  173 MET B CB  
5623  C CG  . MET B 173 ? 0.3031 0.2288 0.5168 0.0037  -0.0024 0.0178  173 MET B CG  
5624  S SD  . MET B 173 ? 0.3435 0.2594 0.5528 -0.0007 -0.0004 0.0172  173 MET B SD  
5625  C CE  . MET B 173 ? 0.3477 0.2510 0.5514 0.0052  -0.0021 0.0181  173 MET B CE  
5626  N N   . ILE B 174 ? 0.3257 0.2421 0.5178 0.0012  -0.0043 0.0269  174 ILE B N   
5627  C CA  . ILE B 174 ? 0.3357 0.2447 0.5181 0.0023  -0.0058 0.0305  174 ILE B CA  
5628  C C   . ILE B 174 ? 0.3612 0.2712 0.5381 -0.0020 -0.0032 0.0316  174 ILE B C   
5629  O O   . ILE B 174 ? 0.3838 0.2862 0.5510 -0.0024 -0.0034 0.0349  174 ILE B O   
5630  C CB  . ILE B 174 ? 0.3546 0.2673 0.5379 0.0080  -0.0105 0.0308  174 ILE B CB  
5631  C CG1 . ILE B 174 ? 0.3621 0.2867 0.5517 0.0074  -0.0111 0.0279  174 ILE B CG1 
5632  C CG2 . ILE B 174 ? 0.3547 0.2656 0.5423 0.0132  -0.0127 0.0304  174 ILE B CG2 
5633  C CD1 . ILE B 174 ? 0.3814 0.3100 0.5699 0.0109  -0.0159 0.0284  174 ILE B CD1 
5634  N N   . SER B 175 ? 0.3681 0.2874 0.5507 -0.0046 -0.0006 0.0290  175 SER B N   
5635  C CA  . SER B 175 ? 0.3695 0.2909 0.5476 -0.0078 0.0024  0.0296  175 SER B CA  
5636  C C   . SER B 175 ? 0.3544 0.2797 0.5364 -0.0126 0.0072  0.0289  175 SER B C   
5637  O O   . SER B 175 ? 0.3578 0.2873 0.5382 -0.0148 0.0105  0.0289  175 SER B O   
5638  C CB  . SER B 175 ? 0.3838 0.3119 0.5631 -0.0057 0.0009  0.0275  175 SER B CB  
5639  O OG  . SER B 175 ? 0.3882 0.3125 0.5619 -0.0024 -0.0036 0.0290  175 SER B OG  
5640  N N   . ASP B 176 ? 0.3503 0.2732 0.5361 -0.0144 0.0076  0.0286  176 ASP B N   
5641  C CA  . ASP B 176 ? 0.3313 0.2559 0.5192 -0.0200 0.0113  0.0288  176 ASP B CA  
5642  C C   . ASP B 176 ? 0.3367 0.2588 0.5173 -0.0242 0.0149  0.0318  176 ASP B C   
5643  O O   . ASP B 176 ? 0.3131 0.2429 0.4974 -0.0281 0.0186  0.0315  176 ASP B O   
5644  C CB  . ASP B 176 ? 0.3305 0.2479 0.5191 -0.0214 0.0102  0.0287  176 ASP B CB  
5645  C CG  . ASP B 176 ? 0.3463 0.2491 0.5255 -0.0201 0.0083  0.0316  176 ASP B CG  
5646  O OD1 . ASP B 176 ? 0.3542 0.2531 0.5270 -0.0170 0.0068  0.0338  176 ASP B OD1 
5647  O OD2 . ASP B 176 ? 0.3518 0.2466 0.5296 -0.0221 0.0082  0.0316  176 ASP B OD2 
5648  N N   . TYR B 177 ? 0.3703 0.2820 0.5404 -0.0235 0.0139  0.0351  177 TYR B N   
5649  C CA  . TYR B 177 ? 0.3894 0.2974 0.5511 -0.0280 0.0177  0.0384  177 TYR B CA  
5650  C C   . TYR B 177 ? 0.3906 0.3068 0.5507 -0.0273 0.0204  0.0379  177 TYR B C   
5651  O O   . TYR B 177 ? 0.3750 0.2914 0.5299 -0.0313 0.0248  0.0401  177 TYR B O   
5652  C CB  . TYR B 177 ? 0.4125 0.3057 0.5616 -0.0268 0.0156  0.0425  177 TYR B CB  
5653  C CG  . TYR B 177 ? 0.4082 0.3005 0.5529 -0.0203 0.0114  0.0426  177 TYR B CG  
5654  C CD1 . TYR B 177 ? 0.4221 0.3144 0.5712 -0.0146 0.0063  0.0409  177 TYR B CD1 
5655  C CD2 . TYR B 177 ? 0.4156 0.3078 0.5515 -0.0202 0.0125  0.0443  177 TYR B CD2 
5656  C CE1 . TYR B 177 ? 0.3906 0.2841 0.5369 -0.0095 0.0021  0.0409  177 TYR B CE1 
5657  C CE2 . TYR B 177 ? 0.4319 0.3239 0.5635 -0.0150 0.0080  0.0441  177 TYR B CE2 
5658  C CZ  . TYR B 177 ? 0.4097 0.3028 0.5470 -0.0098 0.0027  0.0424  177 TYR B CZ  
5659  O OH  . TYR B 177 ? 0.4332 0.3281 0.5673 -0.0054 -0.0020 0.0421  177 TYR B OH  
5660  N N   . MET B 178 ? 0.4013 0.3235 0.5650 -0.0224 0.0180  0.0350  178 MET B N   
5661  C CA  . MET B 178 ? 0.3990 0.3245 0.5575 -0.0208 0.0195  0.0344  178 MET B CA  
5662  C C   . MET B 178 ? 0.4005 0.3368 0.5646 -0.0229 0.0250  0.0327  178 MET B C   
5663  O O   . MET B 178 ? 0.3957 0.3400 0.5705 -0.0232 0.0257  0.0305  178 MET B O   
5664  C CB  . MET B 178 ? 0.4041 0.3313 0.5643 -0.0156 0.0148  0.0317  178 MET B CB  
5665  C CG  . MET B 178 ? 0.3988 0.3282 0.5530 -0.0139 0.0157  0.0302  178 MET B CG  
5666  S SD  . MET B 178 ? 0.4156 0.3472 0.5730 -0.0095 0.0099  0.0266  178 MET B SD  
5667  C CE  . MET B 178 ? 0.4266 0.3503 0.5781 -0.0073 0.0035  0.0296  178 MET B CE  
5668  N N   . ASP B 179 ? 0.3909 0.3274 0.5469 -0.0237 0.0288  0.0339  179 ASP B N   
5669  C CA  . ASP B 179 ? 0.3866 0.3333 0.5460 -0.0239 0.0342  0.0321  179 ASP B CA  
5670  C C   . ASP B 179 ? 0.3571 0.3072 0.5186 -0.0186 0.0326  0.0280  179 ASP B C   
5671  O O   . ASP B 179 ? 0.3599 0.3049 0.5123 -0.0162 0.0310  0.0273  179 ASP B O   
5672  C CB  . ASP B 179 ? 0.4023 0.3470 0.5508 -0.0261 0.0392  0.0346  179 ASP B CB  
5673  C CG  . ASP B 179 ? 0.4687 0.4250 0.6214 -0.0260 0.0459  0.0331  179 ASP B CG  
5674  O OD1 . ASP B 179 ? 0.4688 0.4350 0.6335 -0.0245 0.0465  0.0304  179 ASP B OD1 
5675  O OD2 . ASP B 179 ? 0.5942 0.5500 0.7381 -0.0273 0.0506  0.0347  179 ASP B OD2 
5676  N N   . GLU B 180 ? 0.3464 0.3054 0.5193 -0.0172 0.0334  0.0254  180 GLU B N   
5677  C CA  . GLU B 180 ? 0.3258 0.2874 0.5012 -0.0126 0.0324  0.0217  180 GLU B CA  
5678  C C   . GLU B 180 ? 0.3281 0.2973 0.5044 -0.0109 0.0385  0.0202  180 GLU B C   
5679  O O   . GLU B 180 ? 0.3404 0.3116 0.5190 -0.0069 0.0387  0.0172  180 GLU B O   
5680  C CB  . GLU B 180 ? 0.3163 0.2816 0.5029 -0.0114 0.0291  0.0199  180 GLU B CB  
5681  C CG  . GLU B 180 ? 0.3367 0.2952 0.5229 -0.0112 0.0231  0.0203  180 GLU B CG  
5682  C CD  . GLU B 180 ? 0.3416 0.3029 0.5365 -0.0090 0.0201  0.0179  180 GLU B CD  
5683  O OE1 . GLU B 180 ? 0.3204 0.2882 0.5210 -0.0075 0.0224  0.0161  180 GLU B OE1 
5684  O OE2 . GLU B 180 ? 0.3111 0.2685 0.5068 -0.0085 0.0156  0.0180  180 GLU B OE2 
5685  N N   . SER B 181 ? 0.3218 0.2947 0.4957 -0.0137 0.0437  0.0225  181 SER B N   
5686  C CA  . SER B 181 ? 0.3371 0.3196 0.5138 -0.0117 0.0501  0.0213  181 SER B CA  
5687  C C   . SER B 181 ? 0.3503 0.3273 0.5159 -0.0075 0.0517  0.0189  181 SER B C   
5688  O O   . SER B 181 ? 0.3909 0.3740 0.5580 -0.0040 0.0566  0.0170  181 SER B O   
5689  C CB  . SER B 181 ? 0.3177 0.3080 0.4966 -0.0166 0.0557  0.0245  181 SER B CB  
5690  O OG  . SER B 181 ? 0.3299 0.3126 0.4954 -0.0186 0.0578  0.0266  181 SER B OG  
5691  N N   . ILE B 182 ? 0.3696 0.3351 0.5243 -0.0075 0.0475  0.0187  182 ILE B N   
5692  C CA  . ILE B 182 ? 0.3599 0.3190 0.5028 -0.0041 0.0482  0.0159  182 ILE B CA  
5693  C C   . ILE B 182 ? 0.3519 0.3092 0.4983 0.0000  0.0452  0.0117  182 ILE B C   
5694  O O   . ILE B 182 ? 0.3511 0.3036 0.4891 0.0031  0.0467  0.0086  182 ILE B O   
5695  C CB  . ILE B 182 ? 0.3750 0.3234 0.5044 -0.0061 0.0442  0.0174  182 ILE B CB  
5696  C CG1 . ILE B 182 ? 0.3851 0.3289 0.5183 -0.0069 0.0360  0.0178  182 ILE B CG1 
5697  C CG2 . ILE B 182 ? 0.3861 0.3343 0.5092 -0.0101 0.0480  0.0218  182 ILE B CG2 
5698  C CD1 . ILE B 182 ? 0.3888 0.3236 0.5104 -0.0084 0.0313  0.0200  182 ILE B CD1 
5699  N N   . PHE B 183 ? 0.3362 0.2963 0.4939 -0.0002 0.0413  0.0116  183 PHE B N   
5700  C CA  . PHE B 183 ? 0.3590 0.3168 0.5200 0.0030  0.0385  0.0083  183 PHE B CA  
5701  C C   . PHE B 183 ? 0.3613 0.3271 0.5312 0.0067  0.0428  0.0070  183 PHE B C   
5702  O O   . PHE B 183 ? 0.3762 0.3517 0.5527 0.0064  0.0470  0.0089  183 PHE B O   
5703  C CB  . PHE B 183 ? 0.3374 0.2936 0.5048 0.0011  0.0320  0.0089  183 PHE B CB  
5704  C CG  . PHE B 183 ? 0.3589 0.3087 0.5190 -0.0017 0.0274  0.0106  183 PHE B CG  
5705  C CD1 . PHE B 183 ? 0.3719 0.3143 0.5222 -0.0013 0.0241  0.0087  183 PHE B CD1 
5706  C CD2 . PHE B 183 ? 0.3524 0.3033 0.5157 -0.0045 0.0258  0.0141  183 PHE B CD2 
5707  C CE1 . PHE B 183 ? 0.3832 0.3210 0.5274 -0.0032 0.0193  0.0105  183 PHE B CE1 
5708  C CE2 . PHE B 183 ? 0.3864 0.3311 0.5429 -0.0059 0.0214  0.0159  183 PHE B CE2 
5709  C CZ  . PHE B 183 ? 0.3795 0.3184 0.5270 -0.0050 0.0180  0.0142  183 PHE B CZ  
5710  N N   . ASP B 184 ? 0.3385 0.3004 0.5090 0.0101  0.0414  0.0041  184 ASP B N   
5711  C CA  . ASP B 184 ? 0.3469 0.3149 0.5242 0.0148  0.0452  0.0030  184 ASP B CA  
5712  C C   . ASP B 184 ? 0.3372 0.3130 0.5278 0.0139  0.0427  0.0048  184 ASP B C   
5713  O O   . ASP B 184 ? 0.3462 0.3308 0.5448 0.0170  0.0457  0.0052  184 ASP B O   
5714  C CB  . ASP B 184 ? 0.3361 0.2948 0.5067 0.0192  0.0454  -0.0007 184 ASP B CB  
5715  C CG  . ASP B 184 ? 0.3568 0.3066 0.5126 0.0200  0.0476  -0.0032 184 ASP B CG  
5716  O OD1 . ASP B 184 ? 0.3715 0.3260 0.5241 0.0201  0.0524  -0.0020 184 ASP B OD1 
5717  O OD2 . ASP B 184 ? 0.3834 0.3219 0.5307 0.0197  0.0445  -0.0061 184 ASP B OD2 
5718  N N   . VAL B 185 ? 0.3422 0.3148 0.5349 0.0102  0.0372  0.0057  185 VAL B N   
5719  C CA  . VAL B 185 ? 0.3305 0.3092 0.5343 0.0093  0.0348  0.0070  185 VAL B CA  
5720  C C   . VAL B 185 ? 0.3198 0.2971 0.5245 0.0044  0.0309  0.0090  185 VAL B C   
5721  O O   . VAL B 185 ? 0.3005 0.2704 0.4978 0.0027  0.0283  0.0088  185 VAL B O   
5722  C CB  . VAL B 185 ? 0.3465 0.3222 0.5535 0.0121  0.0324  0.0054  185 VAL B CB  
5723  C CG1 . VAL B 185 ? 0.3484 0.3195 0.5503 0.0173  0.0354  0.0030  185 VAL B CG1 
5724  C CG2 . VAL B 185 ? 0.3534 0.3218 0.5583 0.0094  0.0271  0.0048  185 VAL B CG2 
5725  N N   . TYR B 186 ? 0.2988 0.2833 0.5123 0.0024  0.0304  0.0107  186 TYR B N   
5726  C CA  . TYR B 186 ? 0.2851 0.2678 0.4996 -0.0018 0.0273  0.0125  186 TYR B CA  
5727  C C   . TYR B 186 ? 0.2996 0.2782 0.5163 -0.0012 0.0227  0.0115  186 TYR B C   
5728  O O   . TYR B 186 ? 0.3249 0.3059 0.5464 0.0011  0.0223  0.0103  186 TYR B O   
5729  C CB  . TYR B 186 ? 0.2736 0.2646 0.4953 -0.0047 0.0290  0.0143  186 TYR B CB  
5730  C CG  . TYR B 186 ? 0.2836 0.2800 0.5037 -0.0064 0.0340  0.0158  186 TYR B CG  
5731  C CD1 . TYR B 186 ? 0.2833 0.2737 0.4940 -0.0080 0.0354  0.0169  186 TYR B CD1 
5732  C CD2 . TYR B 186 ? 0.2892 0.2978 0.5175 -0.0065 0.0372  0.0163  186 TYR B CD2 
5733  C CE1 . TYR B 186 ? 0.2851 0.2806 0.4940 -0.0100 0.0406  0.0185  186 TYR B CE1 
5734  C CE2 . TYR B 186 ? 0.2807 0.2961 0.5087 -0.0083 0.0422  0.0177  186 TYR B CE2 
5735  C CZ  . TYR B 186 ? 0.2907 0.2992 0.5088 -0.0102 0.0443  0.0188  186 TYR B CZ  
5736  O OH  . TYR B 186 ? 0.2799 0.2952 0.4971 -0.0122 0.0499  0.0204  186 TYR B OH  
5737  N N   . ALA B 187 ? 0.3175 0.2902 0.5308 -0.0030 0.0192  0.0121  187 ALA B N   
5738  C CA  . ALA B 187 ? 0.3187 0.2889 0.5346 -0.0024 0.0152  0.0112  187 ALA B CA  
5739  C C   . ALA B 187 ? 0.2991 0.2661 0.5144 -0.0042 0.0122  0.0127  187 ALA B C   
5740  O O   . ALA B 187 ? 0.2913 0.2545 0.5006 -0.0055 0.0122  0.0143  187 ALA B O   
5741  C CB  . ALA B 187 ? 0.3194 0.2849 0.5303 -0.0008 0.0139  0.0092  187 ALA B CB  
5742  N N   . TYR B 188 ? 0.2965 0.2644 0.5173 -0.0039 0.0099  0.0123  188 TYR B N   
5743  C CA  . TYR B 188 ? 0.3148 0.2792 0.5354 -0.0042 0.0068  0.0132  188 TYR B CA  
5744  C C   . TYR B 188 ? 0.3251 0.2909 0.5502 -0.0026 0.0042  0.0118  188 TYR B C   
5745  O O   . TYR B 188 ? 0.3077 0.2769 0.5373 -0.0021 0.0050  0.0106  188 TYR B O   
5746  C CB  . TYR B 188 ? 0.3219 0.2860 0.5443 -0.0062 0.0077  0.0145  188 TYR B CB  
5747  C CG  . TYR B 188 ? 0.2941 0.2572 0.5124 -0.0089 0.0104  0.0163  188 TYR B CG  
5748  C CD1 . TYR B 188 ? 0.2991 0.2564 0.5096 -0.0093 0.0101  0.0181  188 TYR B CD1 
5749  C CD2 . TYR B 188 ? 0.3303 0.2988 0.5523 -0.0112 0.0133  0.0164  188 TYR B CD2 
5750  C CE1 . TYR B 188 ? 0.3318 0.2879 0.5379 -0.0122 0.0131  0.0201  188 TYR B CE1 
5751  C CE2 . TYR B 188 ? 0.3450 0.3138 0.5639 -0.0144 0.0163  0.0183  188 TYR B CE2 
5752  C CZ  . TYR B 188 ? 0.3308 0.2930 0.5414 -0.0150 0.0165  0.0201  188 TYR B CZ  
5753  O OH  . TYR B 188 ? 0.3388 0.3008 0.5455 -0.0185 0.0198  0.0222  188 TYR B OH  
5754  N N   . ASN B 189 ? 0.3458 0.3092 0.5699 -0.0017 0.0011  0.0124  189 ASN B N   
5755  C CA  . ASN B 189 ? 0.3196 0.2851 0.5491 -0.0002 -0.0009 0.0118  189 ASN B CA  
5756  C C   . ASN B 189 ? 0.3060 0.2700 0.5374 -0.0002 -0.0002 0.0123  189 ASN B C   
5757  O O   . ASN B 189 ? 0.3382 0.2972 0.5658 -0.0004 -0.0004 0.0139  189 ASN B O   
5758  C CB  . ASN B 189 ? 0.3298 0.2950 0.5579 0.0013  -0.0045 0.0122  189 ASN B CB  
5759  C CG  . ASN B 189 ? 0.3455 0.3114 0.5705 0.0003  -0.0057 0.0112  189 ASN B CG  
5760  O OD1 . ASN B 189 ? 0.4221 0.3861 0.6421 0.0006  -0.0081 0.0121  189 ASN B OD1 
5761  N ND2 . ASN B 189 ? 0.3060 0.2739 0.5332 -0.0008 -0.0043 0.0094  189 ASN B ND2 
5762  N N   . CYS B 190 ? 0.2908 0.2581 0.5272 -0.0001 0.0008  0.0111  190 CYS B N   
5763  C CA  . CYS B 190 ? 0.2823 0.2482 0.5196 -0.0010 0.0018  0.0109  190 CYS B CA  
5764  C C   . CYS B 190 ? 0.2896 0.2562 0.5302 0.0011  0.0010  0.0099  190 CYS B C   
5765  O O   . CYS B 190 ? 0.2737 0.2450 0.5181 0.0016  0.0013  0.0088  190 CYS B O   
5766  C CB  . CYS B 190 ? 0.2658 0.2359 0.5051 -0.0029 0.0040  0.0103  190 CYS B CB  
5767  S SG  . CYS B 190 ? 0.2937 0.2646 0.5300 -0.0049 0.0060  0.0115  190 CYS B SG  
5768  N N   . TYR B 191 ? 0.2611 0.2226 0.4997 0.0027  0.0000  0.0102  191 TYR B N   
5769  C CA  . TYR B 191 ? 0.2635 0.2259 0.5050 0.0055  -0.0002 0.0090  191 TYR B CA  
5770  C C   . TYR B 191 ? 0.2771 0.2332 0.5155 0.0047  0.0008  0.0082  191 TYR B C   
5771  O O   . TYR B 191 ? 0.2968 0.2462 0.5305 0.0029  0.0007  0.0092  191 TYR B O   
5772  C CB  . TYR B 191 ? 0.2833 0.2462 0.5259 0.0094  -0.0022 0.0097  191 TYR B CB  
5773  C CG  . TYR B 191 ? 0.2582 0.2287 0.5049 0.0096  -0.0035 0.0098  191 TYR B CG  
5774  C CD1 . TYR B 191 ? 0.2466 0.2240 0.4990 0.0100  -0.0028 0.0085  191 TYR B CD1 
5775  C CD2 . TYR B 191 ? 0.2709 0.2411 0.5148 0.0083  -0.0050 0.0109  191 TYR B CD2 
5776  C CE1 . TYR B 191 ? 0.2559 0.2393 0.5115 0.0088  -0.0039 0.0085  191 TYR B CE1 
5777  C CE2 . TYR B 191 ? 0.2624 0.2382 0.5089 0.0075  -0.0063 0.0105  191 TYR B CE2 
5778  C CZ  . TYR B 191 ? 0.2718 0.2542 0.5243 0.0075  -0.0058 0.0093  191 TYR B CZ  
5779  O OH  . TYR B 191 ? 0.2883 0.2754 0.5429 0.0056  -0.0072 0.0088  191 TYR B OH  
5780  N N   . ASP B 192 ? 0.2804 0.2385 0.5209 0.0056  0.0017  0.0063  192 ASP B N   
5781  C CA  . ASP B 192 ? 0.3023 0.2545 0.5394 0.0046  0.0025  0.0048  192 ASP B CA  
5782  C C   . ASP B 192 ? 0.3083 0.2570 0.5447 0.0093  0.0026  0.0037  192 ASP B C   
5783  O O   . ASP B 192 ? 0.3163 0.2697 0.5556 0.0112  0.0037  0.0021  192 ASP B O   
5784  C CB  . ASP B 192 ? 0.3139 0.2706 0.5522 0.0016  0.0034  0.0034  192 ASP B CB  
5785  C CG  . ASP B 192 ? 0.3281 0.2788 0.5619 -0.0001 0.0037  0.0013  192 ASP B CG  
5786  O OD1 . ASP B 192 ? 0.3619 0.3031 0.5910 0.0003  0.0034  0.0011  192 ASP B OD1 
5787  O OD2 . ASP B 192 ? 0.3265 0.2812 0.5609 -0.0019 0.0040  0.0000  192 ASP B OD2 
5788  N N   . HIS B 193 ? 0.3077 0.2479 0.5399 0.0115  0.0018  0.0046  193 HIS B N   
5789  C CA  . HIS B 193 ? 0.3152 0.2508 0.5461 0.0172  0.0021  0.0037  193 HIS B CA  
5790  C C   . HIS B 193 ? 0.3321 0.2540 0.5548 0.0164  0.0027  0.0023  193 HIS B C   
5791  O O   . HIS B 193 ? 0.3016 0.2167 0.5214 0.0217  0.0032  0.0014  193 HIS B O   
5792  C CB  . HIS B 193 ? 0.3009 0.2363 0.5327 0.0216  0.0002  0.0061  193 HIS B CB  
5793  C CG  . HIS B 193 ? 0.2910 0.2385 0.5299 0.0221  -0.0010 0.0072  193 HIS B CG  
5794  N ND1 . HIS B 193 ? 0.2835 0.2317 0.5217 0.0216  -0.0032 0.0096  193 HIS B ND1 
5795  C CD2 . HIS B 193 ? 0.2924 0.2511 0.5384 0.0226  -0.0002 0.0062  193 HIS B CD2 
5796  C CE1 . HIS B 193 ? 0.3009 0.2600 0.5454 0.0217  -0.0041 0.0097  193 HIS B CE1 
5797  N NE2 . HIS B 193 ? 0.2949 0.2604 0.5444 0.0221  -0.0023 0.0078  193 HIS B NE2 
5798  N N   . ASN B 194 ? 0.3139 0.2322 0.5331 0.0099  0.0028  0.0019  194 ASN B N   
5799  C CA  . ASN B 194 ? 0.3221 0.2280 0.5335 0.0073  0.0034  0.0000  194 ASN B CA  
5800  C C   . ASN B 194 ? 0.3280 0.2195 0.5323 0.0106  0.0029  0.0013  194 ASN B C   
5801  O O   . ASN B 194 ? 0.3482 0.2299 0.5474 0.0145  0.0037  -0.0006 194 ASN B O   
5802  C CB  . ASN B 194 ? 0.3290 0.2356 0.5397 0.0086  0.0046  -0.0036 194 ASN B CB  
5803  C CG  . ASN B 194 ? 0.3504 0.2444 0.5523 0.0046  0.0048  -0.0063 194 ASN B CG  
5804  O OD1 . ASN B 194 ? 0.3606 0.2496 0.5590 -0.0018 0.0040  -0.0056 194 ASN B OD1 
5805  N ND2 . ASN B 194 ? 0.3761 0.2642 0.5737 0.0083  0.0061  -0.0094 194 ASN B ND2 
5806  N N   . GLU B 195 ? 0.3329 0.2227 0.5362 0.0091  0.0019  0.0047  195 GLU B N   
5807  C CA  . GLU B 195 ? 0.3593 0.2356 0.5553 0.0120  0.0011  0.0070  195 GLU B CA  
5808  C C   . GLU B 195 ? 0.3599 0.2353 0.5537 0.0062  0.0007  0.0103  195 GLU B C   
5809  O O   . GLU B 195 ? 0.3369 0.2246 0.5367 0.0033  0.0006  0.0110  195 GLU B O   
5810  C CB  . GLU B 195 ? 0.3580 0.2369 0.5568 0.0211  0.0000  0.0084  195 GLU B CB  
5811  C CG  . GLU B 195 ? 0.3635 0.2572 0.5702 0.0215  -0.0015 0.0106  195 GLU B CG  
5812  C CD  . GLU B 195 ? 0.3584 0.2590 0.5702 0.0296  -0.0031 0.0116  195 GLU B CD  
5813  O OE1 . GLU B 195 ? 0.3762 0.2726 0.5872 0.0361  -0.0027 0.0106  195 GLU B OE1 
5814  O OE2 . GLU B 195 ? 0.3538 0.2639 0.5700 0.0291  -0.0048 0.0134  195 GLU B OE2 
5815  N N   . GLY B 196 ? 0.3860 0.2457 0.5703 0.0046  0.0007  0.0122  196 GLY B N   
5816  C CA  . GLY B 196 ? 0.3627 0.2196 0.5432 -0.0012 0.0009  0.0155  196 GLY B CA  
5817  C C   . GLY B 196 ? 0.3402 0.2061 0.5249 -0.0098 0.0023  0.0142  196 GLY B C   
5818  O O   . GLY B 196 ? 0.3420 0.2060 0.5262 -0.0137 0.0029  0.0112  196 GLY B O   
5819  N N   . GLN B 197 ? 0.3415 0.2179 0.5303 -0.0121 0.0026  0.0162  197 GLN B N   
5820  C CA  . GLN B 197 ? 0.3397 0.2267 0.5334 -0.0190 0.0040  0.0156  197 GLN B CA  
5821  C C   . GLN B 197 ? 0.3306 0.2274 0.5313 -0.0190 0.0038  0.0118  197 GLN B C   
5822  O O   . GLN B 197 ? 0.3320 0.2336 0.5348 -0.0253 0.0045  0.0106  197 GLN B O   
5823  C CB  . GLN B 197 ? 0.3373 0.2347 0.5346 -0.0186 0.0044  0.0179  197 GLN B CB  
5824  C CG  . GLN B 197 ? 0.3327 0.2217 0.5223 -0.0196 0.0049  0.0219  197 GLN B CG  
5825  C CD  . GLN B 197 ? 0.3486 0.2333 0.5353 -0.0120 0.0026  0.0236  197 GLN B CD  
5826  O OE1 . GLN B 197 ? 0.3762 0.2541 0.5613 -0.0069 0.0010  0.0228  197 GLN B OE1 
5827  N NE2 . GLN B 197 ? 0.3414 0.2300 0.5267 -0.0110 0.0024  0.0261  197 GLN B NE2 
5828  N N   . THR B 198 ? 0.3139 0.2153 0.5186 -0.0124 0.0028  0.0102  198 THR B N   
5829  C CA  . THR B 198 ? 0.3015 0.2129 0.5123 -0.0124 0.0029  0.0073  198 THR B CA  
5830  C C   . THR B 198 ? 0.3364 0.2394 0.5429 -0.0130 0.0028  0.0042  198 THR B C   
5831  O O   . THR B 198 ? 0.3625 0.2720 0.5719 -0.0146 0.0028  0.0017  198 THR B O   
5832  C CB  . THR B 198 ? 0.2998 0.2210 0.5170 -0.0066 0.0024  0.0071  198 THR B CB  
5833  O OG1 . THR B 198 ? 0.2903 0.2065 0.5061 -0.0002 0.0017  0.0072  198 THR B OG1 
5834  C CG2 . THR B 198 ? 0.2867 0.2165 0.5077 -0.0071 0.0025  0.0093  198 THR B CG2 
5835  N N   . ALA B 199 ? 0.3415 0.2293 0.5401 -0.0113 0.0028  0.0043  199 ALA B N   
5836  C CA  . ALA B 199 ? 0.3643 0.2405 0.5561 -0.0126 0.0029  0.0011  199 ALA B CA  
5837  C C   . ALA B 199 ? 0.3811 0.2520 0.5685 -0.0223 0.0030  0.0007  199 ALA B C   
5838  O O   . ALA B 199 ? 0.3748 0.2436 0.5598 -0.0261 0.0027  -0.0026 199 ALA B O   
5839  C CB  . ALA B 199 ? 0.3692 0.2297 0.5535 -0.0063 0.0030  0.0014  199 ALA B CB  
5840  N N   . THR B 200 ? 0.3677 0.2365 0.5538 -0.0265 0.0034  0.0042  200 THR B N   
5841  C CA  . THR B 200 ? 0.3915 0.2556 0.5738 -0.0363 0.0038  0.0043  200 THR B CA  
5842  C C   . THR B 200 ? 0.3868 0.2693 0.5781 -0.0418 0.0037  0.0037  200 THR B C   
5843  O O   . THR B 200 ? 0.3935 0.2773 0.5845 -0.0477 0.0029  0.0010  200 THR B O   
5844  C CB  . THR B 200 ? 0.3966 0.2506 0.5728 -0.0386 0.0048  0.0084  200 THR B CB  
5845  O OG1 . THR B 200 ? 0.3563 0.2220 0.5386 -0.0354 0.0053  0.0115  200 THR B OG1 
5846  C CG2 . THR B 200 ? 0.4125 0.2464 0.5784 -0.0330 0.0046  0.0090  200 THR B CG2 
5847  N N   . MET B 201 ? 0.3620 0.2586 0.5611 -0.0395 0.0043  0.0059  201 MET B N   
5848  C CA  . MET B 201 ? 0.3603 0.2737 0.5677 -0.0440 0.0044  0.0058  201 MET B CA  
5849  C C   . MET B 201 ? 0.3332 0.2582 0.5471 -0.0395 0.0033  0.0036  201 MET B C   
5850  O O   . MET B 201 ? 0.3169 0.2546 0.5368 -0.0425 0.0029  0.0030  201 MET B O   
5851  C CB  . MET B 201 ? 0.3537 0.2752 0.5650 -0.0440 0.0062  0.0094  201 MET B CB  
5852  C CG  . MET B 201 ? 0.3502 0.2632 0.5557 -0.0502 0.0078  0.0120  201 MET B CG  
5853  S SD  . MET B 201 ? 0.3677 0.2840 0.5732 -0.0479 0.0101  0.0163  201 MET B SD  
5854  C CE  . MET B 201 ? 0.3758 0.2760 0.5733 -0.0397 0.0084  0.0169  201 MET B CE  
5855  N N   . GLY B 202 ? 0.3314 0.2522 0.5439 -0.0322 0.0029  0.0025  202 GLY B N   
5856  C CA  . GLY B 202 ? 0.2909 0.2219 0.5089 -0.0277 0.0024  0.0011  202 GLY B CA  
5857  C C   . GLY B 202 ? 0.2819 0.2236 0.5064 -0.0247 0.0031  0.0035  202 GLY B C   
5858  O O   . GLY B 202 ? 0.2938 0.2368 0.5188 -0.0269 0.0041  0.0059  202 GLY B O   
5859  N N   . PHE B 203 ? 0.2827 0.2317 0.5115 -0.0200 0.0030  0.0029  203 PHE B N   
5860  C CA  . PHE B 203 ? 0.2696 0.2249 0.5025 -0.0164 0.0036  0.0048  203 PHE B CA  
5861  C C   . PHE B 203 ? 0.2669 0.2325 0.5045 -0.0191 0.0043  0.0060  203 PHE B C   
5862  O O   . PHE B 203 ? 0.2811 0.2480 0.5191 -0.0192 0.0053  0.0079  203 PHE B O   
5863  C CB  . PHE B 203 ? 0.2591 0.2179 0.4947 -0.0114 0.0034  0.0038  203 PHE B CB  
5864  C CG  . PHE B 203 ? 0.2527 0.2160 0.4915 -0.0080 0.0038  0.0053  203 PHE B CG  
5865  C CD1 . PHE B 203 ? 0.2649 0.2244 0.5020 -0.0070 0.0037  0.0070  203 PHE B CD1 
5866  C CD2 . PHE B 203 ? 0.2649 0.2353 0.5077 -0.0060 0.0040  0.0050  203 PHE B CD2 
5867  C CE1 . PHE B 203 ? 0.2879 0.2512 0.5273 -0.0043 0.0035  0.0079  203 PHE B CE1 
5868  C CE2 . PHE B 203 ? 0.2344 0.2074 0.4792 -0.0036 0.0042  0.0060  203 PHE B CE2 
5869  C CZ  . PHE B 203 ? 0.2399 0.2097 0.4832 -0.0030 0.0038  0.0072  203 PHE B CZ  
5870  N N   . LYS B 204 ? 0.2831 0.2562 0.5237 -0.0207 0.0037  0.0049  204 LYS B N   
5871  C CA  . LYS B 204 ? 0.2803 0.2643 0.5259 -0.0227 0.0043  0.0061  204 LYS B CA  
5872  C C   . LYS B 204 ? 0.2875 0.2707 0.5324 -0.0276 0.0055  0.0075  204 LYS B C   
5873  O O   . LYS B 204 ? 0.2834 0.2704 0.5299 -0.0270 0.0074  0.0093  204 LYS B O   
5874  C CB  . LYS B 204 ? 0.2569 0.2483 0.5050 -0.0246 0.0027  0.0047  204 LYS B CB  
5875  C CG  . LYS B 204 ? 0.2480 0.2522 0.5022 -0.0263 0.0031  0.0061  204 LYS B CG  
5876  C CD  . LYS B 204 ? 0.2375 0.2499 0.4942 -0.0295 0.0008  0.0049  204 LYS B CD  
5877  C CE  . LYS B 204 ? 0.2388 0.2642 0.5020 -0.0323 0.0012  0.0063  204 LYS B CE  
5878  N NZ  . LYS B 204 ? 0.2507 0.2841 0.5160 -0.0361 -0.0019 0.0051  204 LYS B NZ  
5879  N N   . ASP B 205 ? 0.3147 0.2926 0.5563 -0.0330 0.0047  0.0066  205 ASP B N   
5880  C CA  . ASP B 205 ? 0.3112 0.2891 0.5522 -0.0391 0.0061  0.0081  205 ASP B CA  
5881  C C   . ASP B 205 ? 0.2996 0.2690 0.5360 -0.0378 0.0079  0.0103  205 ASP B C   
5882  O O   . ASP B 205 ? 0.2991 0.2721 0.5363 -0.0406 0.0101  0.0124  205 ASP B O   
5883  C CB  . ASP B 205 ? 0.3319 0.3049 0.5697 -0.0459 0.0046  0.0064  205 ASP B CB  
5884  C CG  . ASP B 205 ? 0.3259 0.3113 0.5692 -0.0495 0.0028  0.0049  205 ASP B CG  
5885  O OD1 . ASP B 205 ? 0.2877 0.2849 0.5371 -0.0452 0.0024  0.0052  205 ASP B OD1 
5886  O OD2 . ASP B 205 ? 0.3411 0.3234 0.5818 -0.0565 0.0014  0.0034  205 ASP B OD2 
5887  N N   . TYR B 206 ? 0.3037 0.2625 0.5352 -0.0333 0.0072  0.0101  206 TYR B N   
5888  C CA  . TYR B 206 ? 0.3308 0.2829 0.5579 -0.0317 0.0083  0.0126  206 TYR B CA  
5889  C C   . TYR B 206 ? 0.3063 0.2678 0.5371 -0.0291 0.0099  0.0140  206 TYR B C   
5890  O O   . TYR B 206 ? 0.2956 0.2573 0.5244 -0.0314 0.0120  0.0161  206 TYR B O   
5891  C CB  . TYR B 206 ? 0.3341 0.2758 0.5566 -0.0263 0.0068  0.0123  206 TYR B CB  
5892  C CG  . TYR B 206 ? 0.3262 0.2616 0.5438 -0.0241 0.0072  0.0150  206 TYR B CG  
5893  C CD1 . TYR B 206 ? 0.3281 0.2575 0.5402 -0.0285 0.0087  0.0175  206 TYR B CD1 
5894  C CD2 . TYR B 206 ? 0.3227 0.2588 0.5409 -0.0180 0.0059  0.0151  206 TYR B CD2 
5895  C CE1 . TYR B 206 ? 0.3462 0.2695 0.5527 -0.0261 0.0087  0.0202  206 TYR B CE1 
5896  C CE2 . TYR B 206 ? 0.3203 0.2513 0.5337 -0.0158 0.0055  0.0175  206 TYR B CE2 
5897  C CZ  . TYR B 206 ? 0.3401 0.2644 0.5472 -0.0196 0.0068  0.0200  206 TYR B CZ  
5898  O OH  . TYR B 206 ? 0.3575 0.2769 0.5589 -0.0169 0.0061  0.0225  206 TYR B OH  
5899  N N   . ILE B 207 ? 0.3026 0.2710 0.5380 -0.0245 0.0093  0.0128  207 ILE B N   
5900  C CA  . ILE B 207 ? 0.3090 0.2840 0.5467 -0.0215 0.0107  0.0135  207 ILE B CA  
5901  C C   . ILE B 207 ? 0.2892 0.2750 0.5315 -0.0241 0.0129  0.0141  207 ILE B C   
5902  O O   . ILE B 207 ? 0.2737 0.2626 0.5155 -0.0235 0.0153  0.0154  207 ILE B O   
5903  C CB  . ILE B 207 ? 0.3074 0.2847 0.5478 -0.0164 0.0093  0.0121  207 ILE B CB  
5904  C CG1 . ILE B 207 ? 0.3367 0.3054 0.5737 -0.0136 0.0073  0.0116  207 ILE B CG1 
5905  C CG2 . ILE B 207 ? 0.2939 0.2763 0.5357 -0.0135 0.0107  0.0125  207 ILE B CG2 
5906  C CD1 . ILE B 207 ? 0.3516 0.3131 0.5830 -0.0133 0.0072  0.0134  207 ILE B CD1 
5907  N N   . LYS B 208 ? 0.3083 0.3003 0.5550 -0.0270 0.0122  0.0132  208 LYS B N   
5908  C CA  . LYS B 208 ? 0.3231 0.3272 0.5754 -0.0298 0.0141  0.0139  208 LYS B CA  
5909  C C   . LYS B 208 ? 0.3268 0.3291 0.5764 -0.0353 0.0166  0.0158  208 LYS B C   
5910  O O   . LYS B 208 ? 0.3581 0.3696 0.6109 -0.0360 0.0196  0.0170  208 LYS B O   
5911  C CB  . LYS B 208 ? 0.3589 0.3701 0.6159 -0.0332 0.0121  0.0126  208 LYS B CB  
5912  C CG  . LYS B 208 ? 0.3723 0.3986 0.6366 -0.0363 0.0136  0.0135  208 LYS B CG  
5913  C CD  . LYS B 208 ? 0.3773 0.4139 0.6475 -0.0364 0.0109  0.0122  208 LYS B CD  
5914  C CE  . LYS B 208 ? 0.4331 0.4658 0.7012 -0.0434 0.0084  0.0109  208 LYS B CE  
5915  N NZ  . LYS B 208 ? 0.5169 0.5598 0.7899 -0.0504 0.0098  0.0119  208 LYS B NZ  
5916  N N   . GLY B 209 ? 0.3236 0.3140 0.5669 -0.0392 0.0156  0.0161  209 GLY B N   
5917  C CA  . GLY B 209 ? 0.3117 0.2980 0.5509 -0.0450 0.0181  0.0184  209 GLY B CA  
5918  C C   . GLY B 209 ? 0.3063 0.2912 0.5416 -0.0419 0.0208  0.0204  209 GLY B C   
5919  O O   . GLY B 209 ? 0.3424 0.3323 0.5778 -0.0455 0.0242  0.0223  209 GLY B O   
5920  N N   . LEU B 210 ? 0.2901 0.2683 0.5216 -0.0357 0.0193  0.0200  210 LEU B N   
5921  C CA  . LEU B 210 ? 0.3070 0.2833 0.5338 -0.0326 0.0211  0.0214  210 LEU B CA  
5922  C C   . LEU B 210 ? 0.2936 0.2827 0.5257 -0.0305 0.0241  0.0210  210 LEU B C   
5923  O O   . LEU B 210 ? 0.3046 0.2955 0.5336 -0.0312 0.0276  0.0226  210 LEU B O   
5924  C CB  . LEU B 210 ? 0.3296 0.2978 0.5524 -0.0269 0.0181  0.0206  210 LEU B CB  
5925  C CG  . LEU B 210 ? 0.3150 0.2702 0.5319 -0.0270 0.0153  0.0213  210 LEU B CG  
5926  C CD1 . LEU B 210 ? 0.3078 0.2592 0.5226 -0.0211 0.0127  0.0207  210 LEU B CD1 
5927  C CD2 . LEU B 210 ? 0.3147 0.2610 0.5238 -0.0313 0.0168  0.0242  210 LEU B CD2 
5928  N N   . ASN B 211 ? 0.2890 0.2866 0.5284 -0.0275 0.0231  0.0191  211 ASN B N   
5929  C CA  . ASN B 211 ? 0.2854 0.2954 0.5305 -0.0250 0.0260  0.0188  211 ASN B CA  
5930  C C   . ASN B 211 ? 0.3113 0.3316 0.5606 -0.0302 0.0295  0.0203  211 ASN B C   
5931  O O   . ASN B 211 ? 0.3326 0.3598 0.5825 -0.0288 0.0336  0.0211  211 ASN B O   
5932  C CB  . ASN B 211 ? 0.2931 0.3087 0.5445 -0.0211 0.0236  0.0169  211 ASN B CB  
5933  C CG  . ASN B 211 ? 0.2939 0.3160 0.5476 -0.0152 0.0257  0.0163  211 ASN B CG  
5934  O OD1 . ASN B 211 ? 0.2834 0.3014 0.5320 -0.0127 0.0278  0.0163  211 ASN B OD1 
5935  N ND2 . ASN B 211 ? 0.2999 0.3316 0.5608 -0.0130 0.0251  0.0157  211 ASN B ND2 
5936  N N   . GLU B 212 ? 0.3246 0.3462 0.5764 -0.0366 0.0284  0.0207  212 GLU B N   
5937  C CA  . GLU B 212 ? 0.3368 0.3690 0.5931 -0.0429 0.0317  0.0223  212 GLU B CA  
5938  C C   . GLU B 212 ? 0.3365 0.3624 0.5850 -0.0457 0.0356  0.0248  212 GLU B C   
5939  O O   . GLU B 212 ? 0.3741 0.4103 0.6253 -0.0463 0.0402  0.0260  212 GLU B O   
5940  C CB  . GLU B 212 ? 0.3494 0.3835 0.6093 -0.0503 0.0293  0.0220  212 GLU B CB  
5941  C CG  . GLU B 212 ? 0.3581 0.4030 0.6266 -0.0478 0.0261  0.0199  212 GLU B CG  
5942  C CD  . GLU B 212 ? 0.3879 0.4295 0.6568 -0.0532 0.0220  0.0184  212 GLU B CD  
5943  O OE1 . GLU B 212 ? 0.4633 0.4932 0.7257 -0.0592 0.0217  0.0189  212 GLU B OE1 
5944  O OE2 . GLU B 212 ? 0.4073 0.4566 0.6817 -0.0513 0.0191  0.0168  212 GLU B OE2 
5945  N N   . LEU B 213 ? 0.3359 0.3454 0.5745 -0.0467 0.0340  0.0256  213 LEU B N   
5946  C CA  . LEU B 213 ? 0.3416 0.3438 0.5714 -0.0494 0.0373  0.0284  213 LEU B CA  
5947  C C   . LEU B 213 ? 0.3410 0.3461 0.5679 -0.0431 0.0401  0.0283  213 LEU B C   
5948  O O   . LEU B 213 ? 0.3209 0.3278 0.5437 -0.0450 0.0447  0.0303  213 LEU B O   
5949  C CB  . LEU B 213 ? 0.3470 0.3304 0.5665 -0.0504 0.0341  0.0295  213 LEU B CB  
5950  C CG  . LEU B 213 ? 0.3373 0.3132 0.5558 -0.0574 0.0322  0.0299  213 LEU B CG  
5951  C CD1 . LEU B 213 ? 0.3265 0.2840 0.5360 -0.0547 0.0282  0.0300  213 LEU B CD1 
5952  C CD2 . LEU B 213 ? 0.3196 0.2954 0.5353 -0.0664 0.0362  0.0329  213 LEU B CD2 
5953  N N   . ASN B 214 ? 0.3211 0.3252 0.5489 -0.0358 0.0374  0.0259  214 ASN B N   
5954  C CA  . ASN B 214 ? 0.3085 0.3143 0.5333 -0.0298 0.0396  0.0250  214 ASN B CA  
5955  C C   . ASN B 214 ? 0.3317 0.3527 0.5632 -0.0289 0.0448  0.0249  214 ASN B C   
5956  O O   . ASN B 214 ? 0.3062 0.3275 0.5326 -0.0258 0.0485  0.0248  214 ASN B O   
5957  C CB  . ASN B 214 ? 0.2903 0.2914 0.5151 -0.0235 0.0355  0.0224  214 ASN B CB  
5958  C CG  . ASN B 214 ? 0.3003 0.2872 0.5165 -0.0231 0.0316  0.0228  214 ASN B CG  
5959  O OD1 . ASN B 214 ? 0.3280 0.3074 0.5360 -0.0256 0.0325  0.0250  214 ASN B OD1 
5960  N ND2 . ASN B 214 ? 0.2848 0.2682 0.5027 -0.0196 0.0275  0.0209  214 ASN B ND2 
5961  N N   . GLY B 215 ? 0.3432 0.3772 0.5858 -0.0315 0.0451  0.0248  215 GLY B N   
5962  C CA  . GLY B 215 ? 0.3225 0.3736 0.5731 -0.0317 0.0501  0.0253  215 GLY B CA  
5963  C C   . GLY B 215 ? 0.3406 0.4037 0.6009 -0.0251 0.0495  0.0233  215 GLY B C   
5964  O O   . GLY B 215 ? 0.3297 0.4076 0.5968 -0.0231 0.0538  0.0236  215 GLY B O   
5965  N N   . LEU B 216 ? 0.3423 0.3991 0.6028 -0.0211 0.0445  0.0214  216 LEU B N   
5966  C CA  . LEU B 216 ? 0.3248 0.3909 0.5935 -0.0154 0.0430  0.0200  216 LEU B CA  
5967  C C   . LEU B 216 ? 0.2983 0.3714 0.5680 -0.0080 0.0477  0.0195  216 LEU B C   
5968  O O   . LEU B 216 ? 0.2698 0.3556 0.5482 -0.0039 0.0483  0.0193  216 LEU B O   
5969  C CB  . LEU B 216 ? 0.3304 0.4106 0.6100 -0.0199 0.0414  0.0207  216 LEU B CB  
5970  C CG  . LEU B 216 ? 0.3601 0.4327 0.6387 -0.0256 0.0361  0.0203  216 LEU B CG  
5971  C CD1 . LEU B 216 ? 0.3463 0.4339 0.6352 -0.0303 0.0345  0.0206  216 LEU B CD1 
5972  C CD2 . LEU B 216 ? 0.3578 0.4195 0.6325 -0.0202 0.0320  0.0186  216 LEU B CD2 
5973  N N   . ASP B 217 ? 0.3013 0.3649 0.5612 -0.0057 0.0505  0.0190  217 ASP B N   
5974  C CA  . ASP B 217 ? 0.3187 0.3871 0.5773 0.0008  0.0559  0.0183  217 ASP B CA  
5975  C C   . ASP B 217 ? 0.3171 0.3715 0.5667 0.0074  0.0546  0.0158  217 ASP B C   
5976  O O   . ASP B 217 ? 0.3536 0.4076 0.5990 0.0129  0.0589  0.0146  217 ASP B O   
5977  C CB  . ASP B 217 ? 0.3305 0.4013 0.5846 -0.0030 0.0616  0.0198  217 ASP B CB  
5978  C CG  . ASP B 217 ? 0.3508 0.4059 0.5928 -0.0082 0.0601  0.0206  217 ASP B CG  
5979  O OD1 . ASP B 217 ? 0.3204 0.3650 0.5600 -0.0105 0.0543  0.0204  217 ASP B OD1 
5980  O OD2 . ASP B 217 ? 0.3576 0.4110 0.5924 -0.0095 0.0647  0.0215  217 ASP B OD2 
5981  N N   . LYS B 218 ? 0.3187 0.3618 0.5652 0.0068  0.0490  0.0149  218 LYS B N   
5982  C CA  . LYS B 218 ? 0.3303 0.3606 0.5690 0.0118  0.0473  0.0126  218 LYS B CA  
5983  C C   . LYS B 218 ? 0.3020 0.3282 0.5441 0.0118  0.0417  0.0122  218 LYS B C   
5984  O O   . LYS B 218 ? 0.2558 0.2855 0.5031 0.0072  0.0388  0.0134  218 LYS B O   
5985  C CB  . LYS B 218 ? 0.3802 0.3967 0.6070 0.0093  0.0464  0.0120  218 LYS B CB  
5986  C CG  . LYS B 218 ? 0.4220 0.4400 0.6430 0.0072  0.0512  0.0130  218 LYS B CG  
5987  C CD  . LYS B 218 ? 0.4415 0.4465 0.6495 0.0051  0.0502  0.0127  218 LYS B CD  
5988  C CE  . LYS B 218 ? 0.4650 0.4722 0.6662 0.0058  0.0565  0.0130  218 LYS B CE  
5989  N NZ  . LYS B 218 ? 0.4823 0.4783 0.6710 0.0027  0.0552  0.0135  218 LYS B NZ  
5990  N N   . PRO B 219 ? 0.3074 0.3255 0.5459 0.0166  0.0403  0.0104  219 PRO B N   
5991  C CA  . PRO B 219 ? 0.2987 0.3119 0.5391 0.0161  0.0354  0.0101  219 PRO B CA  
5992  C C   . PRO B 219 ? 0.2951 0.3019 0.5326 0.0102  0.0319  0.0105  219 PRO B C   
5993  O O   . PRO B 219 ? 0.2910 0.2924 0.5219 0.0080  0.0326  0.0104  219 PRO B O   
5994  C CB  . PRO B 219 ? 0.3075 0.3105 0.5414 0.0211  0.0355  0.0081  219 PRO B CB  
5995  C CG  . PRO B 219 ? 0.3195 0.3257 0.5513 0.0264  0.0408  0.0074  219 PRO B CG  
5996  C CD  . PRO B 219 ? 0.3218 0.3342 0.5534 0.0225  0.0436  0.0084  219 PRO B CD  
5997  N N   . PHE B 220 ? 0.3150 0.3223 0.5569 0.0080  0.0282  0.0110  220 PHE B N   
5998  C CA  . PHE B 220 ? 0.2834 0.2840 0.5229 0.0039  0.0248  0.0111  220 PHE B CA  
5999  C C   . PHE B 220 ? 0.2780 0.2726 0.5169 0.0055  0.0217  0.0100  220 PHE B C   
6000  O O   . PHE B 220 ? 0.2710 0.2693 0.5143 0.0076  0.0212  0.0100  220 PHE B O   
6001  C CB  . PHE B 220 ? 0.2695 0.2759 0.5142 -0.0005 0.0237  0.0125  220 PHE B CB  
6002  C CG  . PHE B 220 ? 0.2511 0.2507 0.4942 -0.0034 0.0201  0.0125  220 PHE B CG  
6003  C CD1 . PHE B 220 ? 0.2545 0.2456 0.4913 -0.0043 0.0189  0.0125  220 PHE B CD1 
6004  C CD2 . PHE B 220 ? 0.2507 0.2525 0.4984 -0.0045 0.0177  0.0123  220 PHE B CD2 
6005  C CE1 . PHE B 220 ? 0.2577 0.2434 0.4937 -0.0057 0.0157  0.0125  220 PHE B CE1 
6006  C CE2 . PHE B 220 ? 0.2434 0.2388 0.4893 -0.0062 0.0149  0.0120  220 PHE B CE2 
6007  C CZ  . PHE B 220 ? 0.2406 0.2284 0.4813 -0.0065 0.0140  0.0122  220 PHE B CZ  
6008  N N   . ILE B 221 ? 0.2808 0.2671 0.5144 0.0044  0.0197  0.0092  221 ILE B N   
6009  C CA  . ILE B 221 ? 0.2720 0.2539 0.5059 0.0047  0.0168  0.0084  221 ILE B CA  
6010  C C   . ILE B 221 ? 0.2771 0.2563 0.5107 0.0018  0.0138  0.0088  221 ILE B C   
6011  O O   . ILE B 221 ? 0.2823 0.2600 0.5129 0.0000  0.0137  0.0095  221 ILE B O   
6012  C CB  . ILE B 221 ? 0.2606 0.2356 0.4890 0.0066  0.0170  0.0067  221 ILE B CB  
6013  C CG1 . ILE B 221 ? 0.2650 0.2347 0.4868 0.0048  0.0161  0.0061  221 ILE B CG1 
6014  C CG2 . ILE B 221 ? 0.2843 0.2600 0.5117 0.0107  0.0203  0.0062  221 ILE B CG2 
6015  C CD1 . ILE B 221 ? 0.2983 0.2605 0.5132 0.0059  0.0161  0.0040  221 ILE B CD1 
6016  N N   . THR B 222 ? 0.2574 0.2357 0.4938 0.0017  0.0116  0.0083  222 THR B N   
6017  C CA  . THR B 222 ? 0.2809 0.2568 0.5172 0.0002  0.0089  0.0084  222 THR B CA  
6018  C C   . THR B 222 ? 0.2897 0.2619 0.5236 0.0003  0.0073  0.0072  222 THR B C   
6019  O O   . THR B 222 ? 0.2940 0.2652 0.5281 0.0011  0.0080  0.0065  222 THR B O   
6020  C CB  . THR B 222 ? 0.2644 0.2430 0.5056 -0.0002 0.0079  0.0086  222 THR B CB  
6021  O OG1 . THR B 222 ? 0.2631 0.2422 0.5063 0.0009  0.0078  0.0080  222 THR B OG1 
6022  C CG2 . THR B 222 ? 0.2672 0.2500 0.5108 -0.0009 0.0092  0.0093  222 THR B CG2 
6023  N N   . THR B 223 ? 0.3047 0.2748 0.5361 -0.0007 0.0050  0.0073  223 THR B N   
6024  C CA  . THR B 223 ? 0.3067 0.2744 0.5357 -0.0015 0.0029  0.0062  223 THR B CA  
6025  C C   . THR B 223 ? 0.3181 0.2887 0.5517 -0.0020 0.0001  0.0064  223 THR B C   
6026  O O   . THR B 223 ? 0.3133 0.2841 0.5466 -0.0033 -0.0021 0.0056  223 THR B O   
6027  C CB  . THR B 223 ? 0.3112 0.2756 0.5331 -0.0019 0.0022  0.0062  223 THR B CB  
6028  O OG1 . THR B 223 ? 0.2615 0.2265 0.4832 -0.0018 0.0015  0.0080  223 THR B OG1 
6029  C CG2 . THR B 223 ? 0.3361 0.2977 0.5529 -0.0011 0.0055  0.0055  223 THR B CG2 
6030  N N   . ALA B 224 ? 0.2959 0.2692 0.5340 -0.0012 0.0004  0.0073  224 ALA B N   
6031  C CA  . ALA B 224 ? 0.2858 0.2625 0.5288 -0.0007 -0.0011 0.0073  224 ALA B CA  
6032  C C   . ALA B 224 ? 0.2831 0.2607 0.5288 0.0004  0.0001  0.0079  224 ALA B C   
6033  O O   . ALA B 224 ? 0.3098 0.2850 0.5530 0.0004  0.0009  0.0086  224 ALA B O   
6034  C CB  . ALA B 224 ? 0.3049 0.2823 0.5473 -0.0002 -0.0043 0.0078  224 ALA B CB  
6035  N N   . PHE B 225 ? 0.2556 0.2363 0.5056 0.0010  0.0003  0.0074  225 PHE B N   
6036  C CA  . PHE B 225 ? 0.2384 0.2194 0.4902 0.0022  0.0012  0.0073  225 PHE B CA  
6037  C C   . PHE B 225 ? 0.2521 0.2375 0.5083 0.0028  0.0015  0.0067  225 PHE B C   
6038  O O   . PHE B 225 ? 0.2678 0.2555 0.5255 0.0014  0.0018  0.0065  225 PHE B O   
6039  C CB  . PHE B 225 ? 0.2412 0.2212 0.4916 0.0013  0.0030  0.0073  225 PHE B CB  
6040  C CG  . PHE B 225 ? 0.2440 0.2259 0.4952 0.0008  0.0044  0.0071  225 PHE B CG  
6041  C CD1 . PHE B 225 ? 0.2417 0.2257 0.4948 0.0011  0.0052  0.0067  225 PHE B CD1 
6042  C CD2 . PHE B 225 ? 0.2563 0.2373 0.5055 0.0004  0.0051  0.0074  225 PHE B CD2 
6043  C CE1 . PHE B 225 ? 0.2401 0.2247 0.4928 0.0010  0.0064  0.0071  225 PHE B CE1 
6044  C CE2 . PHE B 225 ? 0.2462 0.2276 0.4954 0.0008  0.0063  0.0074  225 PHE B CE2 
6045  C CZ  . PHE B 225 ? 0.2357 0.2187 0.4865 0.0011  0.0068  0.0075  225 PHE B CZ  
6046  N N   . GLY B 226 ? 0.2583 0.2443 0.5160 0.0048  0.0018  0.0064  226 GLY B N   
6047  C CA  . GLY B 226 ? 0.2518 0.2428 0.5137 0.0057  0.0029  0.0058  226 GLY B CA  
6048  C C   . GLY B 226 ? 0.2673 0.2599 0.5315 0.0092  0.0024  0.0055  226 GLY B C   
6049  O O   . GLY B 226 ? 0.2945 0.2823 0.5558 0.0110  0.0012  0.0058  226 GLY B O   
6050  N N   . TYR B 227 ? 0.2459 0.2452 0.5151 0.0101  0.0036  0.0051  227 TYR B N   
6051  C CA  . TYR B 227 ? 0.2255 0.2278 0.4976 0.0143  0.0044  0.0045  227 TYR B CA  
6052  C C   . TYR B 227 ? 0.2348 0.2477 0.5145 0.0146  0.0042  0.0049  227 TYR B C   
6053  O O   . TYR B 227 ? 0.2326 0.2502 0.5149 0.0107  0.0050  0.0051  227 TYR B O   
6054  C CB  . TYR B 227 ? 0.2229 0.2226 0.4923 0.0151  0.0074  0.0032  227 TYR B CB  
6055  C CG  . TYR B 227 ? 0.2435 0.2336 0.5060 0.0145  0.0070  0.0027  227 TYR B CG  
6056  C CD1 . TYR B 227 ? 0.2531 0.2367 0.5124 0.0173  0.0060  0.0024  227 TYR B CD1 
6057  C CD2 . TYR B 227 ? 0.2624 0.2503 0.5218 0.0111  0.0074  0.0026  227 TYR B CD2 
6058  C CE1 . TYR B 227 ? 0.2669 0.2419 0.5200 0.0155  0.0056  0.0020  227 TYR B CE1 
6059  C CE2 . TYR B 227 ? 0.2556 0.2369 0.5100 0.0098  0.0068  0.0023  227 TYR B CE2 
6060  C CZ  . TYR B 227 ? 0.2625 0.2374 0.5138 0.0114  0.0059  0.0019  227 TYR B CZ  
6061  O OH  . TYR B 227 ? 0.3054 0.2737 0.5517 0.0091  0.0054  0.0015  227 TYR B OH  
6062  N N   . SER B 228 ? 0.2334 0.2500 0.5165 0.0194  0.0034  0.0050  228 SER B N   
6063  C CA  . SER B 228 ? 0.2220 0.2508 0.5137 0.0208  0.0027  0.0054  228 SER B CA  
6064  C C   . SER B 228 ? 0.2241 0.2588 0.5198 0.0240  0.0067  0.0043  228 SER B C   
6065  O O   . SER B 228 ? 0.2200 0.2483 0.5115 0.0284  0.0084  0.0033  228 SER B O   
6066  C CB  . SER B 228 ? 0.2300 0.2600 0.5231 0.0253  -0.0009 0.0064  228 SER B CB  
6067  O OG  . SER B 228 ? 0.2472 0.2911 0.5499 0.0279  -0.0014 0.0068  228 SER B OG  
6068  N N   . VAL B 229 ? 0.2037 0.2504 0.5070 0.0216  0.0083  0.0046  229 VAL B N   
6069  C CA  . VAL B 229 ? 0.1987 0.2523 0.5058 0.0244  0.0128  0.0037  229 VAL B CA  
6070  C C   . VAL B 229 ? 0.2008 0.2685 0.5182 0.0289  0.0123  0.0042  229 VAL B C   
6071  O O   . VAL B 229 ? 0.1879 0.2670 0.5121 0.0294  0.0159  0.0039  229 VAL B O   
6072  C CB  . VAL B 229 ? 0.1971 0.2535 0.5043 0.0187  0.0165  0.0037  229 VAL B CB  
6073  C CG1 . VAL B 229 ? 0.1891 0.2323 0.4864 0.0158  0.0168  0.0035  229 VAL B CG1 
6074  C CG2 . VAL B 229 ? 0.2029 0.2697 0.5175 0.0127  0.0154  0.0050  229 VAL B CG2 
6075  N N   . SER B 230 ? 0.2247 0.2915 0.5428 0.0331  0.0080  0.0049  230 SER B N   
6076  C CA  . SER B 230 ? 0.2602 0.3406 0.5880 0.0385  0.0066  0.0057  230 SER B CA  
6077  C C   . SER B 230 ? 0.2816 0.3664 0.6123 0.0455  0.0117  0.0044  230 SER B C   
6078  O O   . SER B 230 ? 0.2995 0.3719 0.6217 0.0482  0.0145  0.0029  230 SER B O   
6079  C CB  . SER B 230 ? 0.2799 0.3546 0.6047 0.0428  0.0012  0.0069  230 SER B CB  
6080  O OG  . SER B 230 ? 0.3123 0.3728 0.6285 0.0488  0.0023  0.0063  230 SER B OG  
6081  N N   . PRO B 231 ? 0.2663 0.3693 0.6089 0.0483  0.0132  0.0048  231 PRO B N   
6082  C CA  . PRO B 231 ? 0.2710 0.3792 0.6167 0.0565  0.0182  0.0035  231 PRO B CA  
6083  C C   . PRO B 231 ? 0.2843 0.3796 0.6228 0.0662  0.0175  0.0028  231 PRO B C   
6084  O O   . PRO B 231 ? 0.2586 0.3480 0.5925 0.0715  0.0222  0.0007  231 PRO B O   
6085  C CB  . PRO B 231 ? 0.2597 0.3920 0.6214 0.0582  0.0180  0.0047  231 PRO B CB  
6086  C CG  . PRO B 231 ? 0.2596 0.3991 0.6257 0.0471  0.0149  0.0060  231 PRO B CG  
6087  C CD  . PRO B 231 ? 0.2768 0.3970 0.6306 0.0429  0.0107  0.0062  231 PRO B CD  
6088  N N   . GLU B 232 ? 0.3202 0.4112 0.6574 0.0683  0.0116  0.0045  232 GLU B N   
6089  C CA  . GLU B 232 ? 0.3317 0.4082 0.6607 0.0768  0.0101  0.0045  232 GLU B CA  
6090  C C   . GLU B 232 ? 0.3356 0.4046 0.6602 0.0747  0.0034  0.0068  232 GLU B C   
6091  O O   . GLU B 232 ? 0.3185 0.3917 0.6449 0.0664  0.0004  0.0078  232 GLU B O   
6092  C CB  . GLU B 232 ? 0.3512 0.4380 0.6877 0.0881  0.0122  0.0044  232 GLU B CB  
6093  C CG  . GLU B 232 ? 0.3801 0.4873 0.7302 0.0899  0.0077  0.0069  232 GLU B CG  
6094  C CD  . GLU B 232 ? 0.4209 0.5472 0.7837 0.0993  0.0102  0.0071  232 GLU B CD  
6095  O OE1 . GLU B 232 ? 0.5087 0.6518 0.8815 0.0966  0.0146  0.0062  232 GLU B OE1 
6096  O OE2 . GLU B 232 ? 0.4352 0.5592 0.7977 0.1093  0.0074  0.0084  232 GLU B OE2 
6097  N N   . GLY B 233 ? 0.3235 0.3793 0.6406 0.0821  0.0016  0.0076  233 GLY B N   
6098  C CA  . GLY B 233 ? 0.3024 0.3490 0.6133 0.0815  -0.0041 0.0100  233 GLY B CA  
6099  C C   . GLY B 233 ? 0.2917 0.3190 0.5897 0.0747  -0.0039 0.0094  233 GLY B C   
6100  O O   . GLY B 233 ? 0.3033 0.3255 0.5978 0.0700  0.0000  0.0071  233 GLY B O   
6101  N N   . GLY B 234 ? 0.3078 0.3259 0.5992 0.0740  -0.0084 0.0118  234 GLY B N   
6102  C CA  . GLY B 234 ? 0.3179 0.3184 0.5973 0.0683  -0.0085 0.0118  234 GLY B CA  
6103  C C   . GLY B 234 ? 0.3197 0.3022 0.5891 0.0731  -0.0060 0.0108  234 GLY B C   
6104  O O   . GLY B 234 ? 0.3027 0.2831 0.5721 0.0820  -0.0060 0.0113  234 GLY B O   
6105  N N   . ASN B 235 ? 0.3585 0.3280 0.6193 0.0670  -0.0041 0.0094  235 ASN B N   
6106  C CA  . ASN B 235 ? 0.4011 0.3532 0.6520 0.0698  -0.0016 0.0078  235 ASN B CA  
6107  C C   . ASN B 235 ? 0.3757 0.3217 0.6217 0.0612  0.0009  0.0054  235 ASN B C   
6108  O O   . ASN B 235 ? 0.3697 0.3185 0.6161 0.0538  -0.0005 0.0063  235 ASN B O   
6109  C CB  . ASN B 235 ? 0.4581 0.3953 0.7001 0.0740  -0.0043 0.0106  235 ASN B CB  
6110  C CG  . ASN B 235 ? 0.5661 0.4892 0.7981 0.0661  -0.0050 0.0113  235 ASN B CG  
6111  O OD1 . ASN B 235 ? 0.6540 0.5821 0.8872 0.0599  -0.0070 0.0130  235 ASN B OD1 
6112  N ND2 . ASN B 235 ? 0.6373 0.5428 0.8591 0.0659  -0.0029 0.0099  235 ASN B ND2 
6113  N N   . GLY B 236 ? 0.3483 0.2877 0.5902 0.0627  0.0045  0.0022  236 GLY B N   
6114  C CA  . GLY B 236 ? 0.3358 0.2708 0.5734 0.0556  0.0067  -0.0004 236 GLY B CA  
6115  C C   . GLY B 236 ? 0.3491 0.2996 0.5949 0.0501  0.0072  -0.0005 236 GLY B C   
6116  O O   . GLY B 236 ? 0.3185 0.2829 0.5731 0.0529  0.0084  -0.0006 236 GLY B O   
6117  N N   . GLN B 237 ? 0.3106 0.2584 0.5533 0.0423  0.0064  -0.0003 237 GLN B N   
6118  C CA  . GLN B 237 ? 0.3155 0.2749 0.5641 0.0370  0.0067  -0.0002 237 GLN B CA  
6119  C C   . GLN B 237 ? 0.2993 0.2686 0.5547 0.0362  0.0041  0.0025  237 GLN B C   
6120  O O   . GLN B 237 ? 0.2775 0.2556 0.5375 0.0322  0.0044  0.0026  237 GLN B O   
6121  C CB  . GLN B 237 ? 0.3049 0.2585 0.5481 0.0300  0.0066  -0.0008 237 GLN B CB  
6122  C CG  . GLN B 237 ? 0.3019 0.2486 0.5391 0.0290  0.0089  -0.0038 237 GLN B CG  
6123  C CD  . GLN B 237 ? 0.3168 0.2618 0.5508 0.0219  0.0083  -0.0041 237 GLN B CD  
6124  O OE1 . GLN B 237 ? 0.3485 0.3022 0.5867 0.0187  0.0083  -0.0034 237 GLN B OE1 
6125  N NE2 . GLN B 237 ? 0.3237 0.2575 0.5505 0.0194  0.0076  -0.0049 237 GLN B NE2 
6126  N N   . TYR B 238 ? 0.3053 0.2722 0.5602 0.0398  0.0013  0.0046  238 TYR B N   
6127  C CA  . TYR B 238 ? 0.2835 0.2604 0.5445 0.0394  -0.0016 0.0067  238 TYR B CA  
6128  C C   . TYR B 238 ? 0.2737 0.2632 0.5437 0.0447  -0.0014 0.0067  238 TYR B C   
6129  O O   . TYR B 238 ? 0.3136 0.3017 0.5838 0.0518  -0.0020 0.0072  238 TYR B O   
6130  C CB  . TYR B 238 ? 0.2986 0.2685 0.5546 0.0404  -0.0051 0.0094  238 TYR B CB  
6131  C CG  . TYR B 238 ? 0.3130 0.2933 0.5743 0.0403  -0.0087 0.0113  238 TYR B CG  
6132  C CD1 . TYR B 238 ? 0.2976 0.2826 0.5601 0.0339  -0.0095 0.0114  238 TYR B CD1 
6133  C CD2 . TYR B 238 ? 0.3367 0.3219 0.6014 0.0466  -0.0115 0.0130  238 TYR B CD2 
6134  C CE1 . TYR B 238 ? 0.3038 0.2969 0.5697 0.0331  -0.0130 0.0127  238 TYR B CE1 
6135  C CE2 . TYR B 238 ? 0.3084 0.3036 0.5775 0.0459  -0.0154 0.0146  238 TYR B CE2 
6136  C CZ  . TYR B 238 ? 0.3146 0.3132 0.5839 0.0388  -0.0162 0.0143  238 TYR B CZ  
6137  O OH  . TYR B 238 ? 0.3625 0.3696 0.6347 0.0374  -0.0202 0.0154  238 TYR B OH  
6138  N N   . GLY B 239 ? 0.2449 0.2470 0.5223 0.0412  -0.0005 0.0062  239 GLY B N   
6139  C CA  . GLY B 239 ? 0.2493 0.2654 0.5363 0.0446  0.0008  0.0058  239 GLY B CA  
6140  C C   . GLY B 239 ? 0.2580 0.2736 0.5446 0.0466  0.0058  0.0034  239 GLY B C   
6141  O O   . GLY B 239 ? 0.2326 0.2358 0.5107 0.0459  0.0074  0.0020  239 GLY B O   
6142  N N   . SER B 240 ? 0.2656 0.2954 0.5612 0.0483  0.0081  0.0030  240 SER B N   
6143  C CA  . SER B 240 ? 0.2804 0.3120 0.5767 0.0530  0.0130  0.0009  240 SER B CA  
6144  C C   . SER B 240 ? 0.2864 0.3114 0.5761 0.0483  0.0165  -0.0010 240 SER B C   
6145  O O   . SER B 240 ? 0.2800 0.3026 0.5668 0.0520  0.0205  -0.0031 240 SER B O   
6146  C CB  . SER B 240 ? 0.2829 0.3060 0.5750 0.0620  0.0132  0.0002  240 SER B CB  
6147  O OG  . SER B 240 ? 0.2701 0.3018 0.5693 0.0679  0.0102  0.0022  240 SER B OG  
6148  N N   . ASN B 241 ? 0.2922 0.3158 0.5800 0.0406  0.0154  -0.0003 241 ASN B N   
6149  C CA  . ASN B 241 ? 0.2870 0.3057 0.5689 0.0364  0.0183  -0.0017 241 ASN B CA  
6150  C C   . ASN B 241 ? 0.2501 0.2805 0.5376 0.0350  0.0223  -0.0018 241 ASN B C   
6151  O O   . ASN B 241 ? 0.2279 0.2708 0.5246 0.0345  0.0222  -0.0005 241 ASN B O   
6152  C CB  . ASN B 241 ? 0.3189 0.3313 0.5963 0.0298  0.0158  -0.0007 241 ASN B CB  
6153  C CG  . ASN B 241 ? 0.3146 0.3150 0.5854 0.0303  0.0128  -0.0006 241 ASN B CG  
6154  O OD1 . ASN B 241 ? 0.3402 0.3310 0.6036 0.0298  0.0135  -0.0021 241 ASN B OD1 
6155  N ND2 . ASN B 241 ? 0.3273 0.3281 0.6003 0.0309  0.0094  0.0010  241 ASN B ND2 
6156  N N   . THR B 242 ? 0.2373 0.2638 0.5189 0.0344  0.0259  -0.0034 242 THR B N   
6157  C CA  . THR B 242 ? 0.2433 0.2785 0.5276 0.0314  0.0298  -0.0030 242 THR B CA  
6158  C C   . THR B 242 ? 0.2552 0.2895 0.5389 0.0240  0.0278  -0.0010 242 THR B C   
6159  O O   . THR B 242 ? 0.2311 0.2572 0.5108 0.0219  0.0240  -0.0005 242 THR B O   
6160  C CB  . THR B 242 ? 0.2585 0.2878 0.5345 0.0333  0.0338  -0.0053 242 THR B CB  
6161  O OG1 . THR B 242 ? 0.2814 0.2984 0.5476 0.0302  0.0317  -0.0060 242 THR B OG1 
6162  C CG2 . THR B 242 ? 0.2586 0.2854 0.5331 0.0411  0.0358  -0.0078 242 THR B CG2 
6163  N N   . LEU B 243 ? 0.2528 0.2949 0.5398 0.0201  0.0306  0.0003  243 LEU B N   
6164  C CA  . LEU B 243 ? 0.2532 0.2926 0.5380 0.0136  0.0294  0.0021  243 LEU B CA  
6165  C C   . LEU B 243 ? 0.2613 0.2893 0.5358 0.0127  0.0289  0.0016  243 LEU B C   
6166  O O   . LEU B 243 ? 0.2584 0.2806 0.5298 0.0096  0.0261  0.0027  243 LEU B O   
6167  C CB  . LEU B 243 ? 0.2494 0.2978 0.5384 0.0096  0.0332  0.0037  243 LEU B CB  
6168  C CG  . LEU B 243 ? 0.2457 0.3081 0.5464 0.0090  0.0336  0.0044  243 LEU B CG  
6169  C CD1 . LEU B 243 ? 0.2369 0.3082 0.5410 0.0047  0.0385  0.0058  243 LEU B CD1 
6170  C CD2 . LEU B 243 ? 0.2426 0.3053 0.5472 0.0054  0.0286  0.0054  243 LEU B CD2 
6171  N N   . LYS B 244 ? 0.2920 0.3170 0.5607 0.0156  0.0317  -0.0001 244 LYS B N   
6172  C CA  . LYS B 244 ? 0.3212 0.3368 0.5801 0.0146  0.0308  -0.0007 244 LYS B CA  
6173  C C   . LYS B 244 ? 0.3149 0.3227 0.5714 0.0153  0.0265  -0.0017 244 LYS B C   
6174  O O   . LYS B 244 ? 0.3454 0.3481 0.5977 0.0126  0.0241  -0.0010 244 LYS B O   
6175  C CB  . LYS B 244 ? 0.3730 0.3869 0.6253 0.0171  0.0345  -0.0028 244 LYS B CB  
6176  C CG  . LYS B 244 ? 0.3928 0.3987 0.6346 0.0154  0.0334  -0.0033 244 LYS B CG  
6177  C CD  . LYS B 244 ? 0.4326 0.4336 0.6669 0.0189  0.0353  -0.0069 244 LYS B CD  
6178  C CE  . LYS B 244 ? 0.4239 0.4178 0.6470 0.0174  0.0343  -0.0082 244 LYS B CE  
6179  N NZ  . LYS B 244 ? 0.4362 0.4275 0.6586 0.0137  0.0297  -0.0062 244 LYS B NZ  
6180  N N   . GLN B 245 ? 0.2881 0.2954 0.5474 0.0191  0.0256  -0.0030 245 GLN B N   
6181  C CA  . GLN B 245 ? 0.2720 0.2715 0.5288 0.0194  0.0219  -0.0035 245 GLN B CA  
6182  C C   . GLN B 245 ? 0.2731 0.2740 0.5337 0.0161  0.0188  -0.0012 245 GLN B C   
6183  O O   . GLN B 245 ? 0.2803 0.2753 0.5373 0.0142  0.0163  -0.0010 245 GLN B O   
6184  C CB  . GLN B 245 ? 0.2790 0.2766 0.5373 0.0246  0.0217  -0.0048 245 GLN B CB  
6185  C CG  . GLN B 245 ? 0.2848 0.2759 0.5364 0.0284  0.0241  -0.0078 245 GLN B CG  
6186  C CD  . GLN B 245 ? 0.2740 0.2652 0.5282 0.0350  0.0250  -0.0088 245 GLN B CD  
6187  O OE1 . GLN B 245 ? 0.2720 0.2714 0.5345 0.0373  0.0245  -0.0071 245 GLN B OE1 
6188  N NE2 . GLN B 245 ? 0.3054 0.2871 0.5522 0.0386  0.0264  -0.0116 245 GLN B NE2 
6189  N N   . GLN B 246 ? 0.2493 0.2582 0.5169 0.0153  0.0191  0.0003  246 GLN B N   
6190  C CA  . GLN B 246 ? 0.2582 0.2675 0.5281 0.0120  0.0163  0.0020  246 GLN B CA  
6191  C C   . GLN B 246 ? 0.2770 0.2820 0.5420 0.0084  0.0163  0.0028  246 GLN B C   
6192  O O   . GLN B 246 ? 0.3103 0.3106 0.5727 0.0072  0.0140  0.0032  246 GLN B O   
6193  C CB  . GLN B 246 ? 0.2504 0.2689 0.5279 0.0107  0.0166  0.0031  246 GLN B CB  
6194  C CG  . GLN B 246 ? 0.2376 0.2553 0.5161 0.0071  0.0137  0.0044  246 GLN B CG  
6195  C CD  . GLN B 246 ? 0.2247 0.2510 0.5098 0.0041  0.0139  0.0052  246 GLN B CD  
6196  O OE1 . GLN B 246 ? 0.2331 0.2646 0.5206 0.0023  0.0169  0.0056  246 GLN B OE1 
6197  N NE2 . GLN B 246 ? 0.2239 0.2519 0.5117 0.0031  0.0105  0.0056  246 GLN B NE2 
6198  N N   . SER B 247 ? 0.2973 0.3043 0.5606 0.0074  0.0191  0.0032  247 SER B N   
6199  C CA  . SER B 247 ? 0.3080 0.3114 0.5666 0.0047  0.0191  0.0045  247 SER B CA  
6200  C C   . SER B 247 ? 0.2880 0.2857 0.5408 0.0055  0.0175  0.0035  247 SER B C   
6201  O O   . SER B 247 ? 0.2400 0.2351 0.4913 0.0043  0.0156  0.0045  247 SER B O   
6202  C CB  . SER B 247 ? 0.3093 0.3154 0.5664 0.0035  0.0226  0.0055  247 SER B CB  
6203  O OG  . SER B 247 ? 0.3418 0.3435 0.5938 0.0016  0.0221  0.0072  247 SER B OG  
6204  N N   . ASP B 248 ? 0.2913 0.2874 0.5408 0.0076  0.0183  0.0015  248 ASP B N   
6205  C CA  . ASP B 248 ? 0.2890 0.2801 0.5331 0.0073  0.0163  0.0003  248 ASP B CA  
6206  C C   . ASP B 248 ? 0.2746 0.2629 0.5204 0.0066  0.0135  0.0004  248 ASP B C   
6207  O O   . ASP B 248 ? 0.2637 0.2508 0.5077 0.0049  0.0116  0.0009  248 ASP B O   
6208  C CB  . ASP B 248 ? 0.2928 0.2808 0.5320 0.0092  0.0176  -0.0024 248 ASP B CB  
6209  C CG  . ASP B 248 ? 0.2846 0.2746 0.5197 0.0095  0.0205  -0.0025 248 ASP B CG  
6210  O OD1 . ASP B 248 ? 0.2972 0.2898 0.5321 0.0078  0.0210  -0.0001 248 ASP B OD1 
6211  O OD2 . ASP B 248 ? 0.2813 0.2696 0.5128 0.0116  0.0224  -0.0049 248 ASP B OD2 
6212  N N   . GLY B 249 ? 0.2522 0.2409 0.5019 0.0081  0.0132  0.0002  249 GLY B N   
6213  C CA  . GLY B 249 ? 0.2619 0.2475 0.5124 0.0076  0.0108  0.0006  249 GLY B CA  
6214  C C   . GLY B 249 ? 0.2716 0.2586 0.5237 0.0053  0.0096  0.0025  249 GLY B C   
6215  O O   . GLY B 249 ? 0.2918 0.2765 0.5423 0.0040  0.0081  0.0027  249 GLY B O   
6216  N N   . LEU B 250 ? 0.2674 0.2580 0.5224 0.0048  0.0103  0.0037  250 LEU B N   
6217  C CA  . LEU B 250 ? 0.2563 0.2466 0.5115 0.0031  0.0094  0.0051  250 LEU B CA  
6218  C C   . LEU B 250 ? 0.2596 0.2488 0.5116 0.0026  0.0092  0.0055  250 LEU B C   
6219  O O   . LEU B 250 ? 0.2831 0.2715 0.5347 0.0021  0.0082  0.0061  250 LEU B O   
6220  C CB  . LEU B 250 ? 0.2718 0.2645 0.5294 0.0020  0.0104  0.0061  250 LEU B CB  
6221  C CG  . LEU B 250 ? 0.2662 0.2605 0.5273 0.0014  0.0092  0.0061  250 LEU B CG  
6222  C CD1 . LEU B 250 ? 0.2896 0.2805 0.5488 0.0011  0.0074  0.0063  250 LEU B CD1 
6223  C CD2 . LEU B 250 ? 0.2765 0.2736 0.5405 0.0036  0.0089  0.0052  250 LEU B CD2 
6224  N N   . ILE B 251 ? 0.2710 0.2608 0.5205 0.0029  0.0102  0.0053  251 ILE B N   
6225  C CA  . ILE B 251 ? 0.2711 0.2613 0.5178 0.0026  0.0094  0.0060  251 ILE B CA  
6226  C C   . ILE B 251 ? 0.2685 0.2584 0.5143 0.0018  0.0077  0.0049  251 ILE B C   
6227  O O   . ILE B 251 ? 0.2665 0.2585 0.5123 0.0014  0.0065  0.0056  251 ILE B O   
6228  C CB  . ILE B 251 ? 0.3072 0.2980 0.5504 0.0031  0.0108  0.0063  251 ILE B CB  
6229  C CG1 . ILE B 251 ? 0.3472 0.3380 0.5913 0.0028  0.0130  0.0078  251 ILE B CG1 
6230  C CG2 . ILE B 251 ? 0.3129 0.3047 0.5527 0.0033  0.0094  0.0072  251 ILE B CG2 
6231  C CD1 . ILE B 251 ? 0.3523 0.3413 0.5975 0.0024  0.0127  0.0095  251 ILE B CD1 
6232  N N   . SER B 252 ? 0.2836 0.2711 0.5286 0.0016  0.0076  0.0030  252 SER B N   
6233  C CA  . SER B 252 ? 0.2935 0.2791 0.5370 -0.0001 0.0061  0.0018  252 SER B CA  
6234  C C   . SER B 252 ? 0.2799 0.2655 0.5261 -0.0011 0.0054  0.0030  252 SER B C   
6235  O O   . SER B 252 ? 0.2302 0.2175 0.4765 -0.0030 0.0044  0.0032  252 SER B O   
6236  C CB  . SER B 252 ? 0.3111 0.2917 0.5516 0.0003  0.0065  -0.0004 252 SER B CB  
6237  O OG  . SER B 252 ? 0.3621 0.3387 0.6014 -0.0018 0.0052  -0.0010 252 SER B OG  
6238  N N   . ASN B 253 ? 0.2727 0.2572 0.5209 0.0002  0.0060  0.0036  253 ASN B N   
6239  C CA  . ASN B 253 ? 0.2570 0.2410 0.5064 -0.0004 0.0055  0.0047  253 ASN B CA  
6240  C C   . ASN B 253 ? 0.2413 0.2289 0.4919 -0.0006 0.0057  0.0059  253 ASN B C   
6241  O O   . ASN B 253 ? 0.2501 0.2386 0.5010 -0.0017 0.0056  0.0065  253 ASN B O   
6242  C CB  . ASN B 253 ? 0.2652 0.2480 0.5161 0.0009  0.0056  0.0051  253 ASN B CB  
6243  C CG  . ASN B 253 ? 0.2959 0.2755 0.5463 0.0023  0.0052  0.0043  253 ASN B CG  
6244  O OD1 . ASN B 253 ? 0.3266 0.3028 0.5746 0.0023  0.0052  0.0032  253 ASN B OD1 
6245  N ND2 . ASN B 253 ? 0.2833 0.2637 0.5357 0.0037  0.0048  0.0049  253 ASN B ND2 
6246  N N   . TYR B 254 ? 0.2394 0.2288 0.4903 0.0007  0.0064  0.0066  254 TYR B N   
6247  C CA  . TYR B 254 ? 0.2346 0.2259 0.4859 0.0017  0.0068  0.0079  254 TYR B CA  
6248  C C   . TYR B 254 ? 0.2394 0.2354 0.4915 0.0013  0.0061  0.0082  254 TYR B C   
6249  O O   . TYR B 254 ? 0.2350 0.2338 0.4885 0.0019  0.0065  0.0090  254 TYR B O   
6250  C CB  . TYR B 254 ? 0.2365 0.2270 0.4868 0.0032  0.0076  0.0088  254 TYR B CB  
6251  C CG  . TYR B 254 ? 0.2558 0.2440 0.5054 0.0044  0.0084  0.0097  254 TYR B CG  
6252  C CD1 . TYR B 254 ? 0.2803 0.2703 0.5298 0.0064  0.0087  0.0106  254 TYR B CD1 
6253  C CD2 . TYR B 254 ? 0.2738 0.2581 0.5225 0.0038  0.0091  0.0096  254 TYR B CD2 
6254  C CE1 . TYR B 254 ? 0.2943 0.2805 0.5418 0.0083  0.0098  0.0112  254 TYR B CE1 
6255  C CE2 . TYR B 254 ? 0.2979 0.2781 0.5445 0.0046  0.0099  0.0102  254 TYR B CE2 
6256  C CZ  . TYR B 254 ? 0.2834 0.2637 0.5288 0.0072  0.0104  0.0109  254 TYR B CZ  
6257  O OH  . TYR B 254 ? 0.2530 0.2278 0.4952 0.0087  0.0114  0.0110  254 TYR B OH  
6258  N N   . ARG B 255 ? 0.2453 0.2429 0.4963 0.0004  0.0050  0.0075  255 ARG B N   
6259  C CA  . ARG B 255 ? 0.2617 0.2649 0.5137 -0.0009 0.0036  0.0075  255 ARG B CA  
6260  C C   . ARG B 255 ? 0.2682 0.2723 0.5219 -0.0039 0.0034  0.0070  255 ARG B C   
6261  O O   . ARG B 255 ? 0.2372 0.2473 0.4938 -0.0044 0.0034  0.0079  255 ARG B O   
6262  C CB  . ARG B 255 ? 0.2826 0.2853 0.5314 -0.0018 0.0024  0.0063  255 ARG B CB  
6263  C CG  . ARG B 255 ? 0.3154 0.3229 0.5639 -0.0045 0.0001  0.0055  255 ARG B CG  
6264  C CD  . ARG B 255 ? 0.3248 0.3407 0.5757 -0.0027 -0.0012 0.0073  255 ARG B CD  
6265  N NE  . ARG B 255 ? 0.3210 0.3424 0.5770 -0.0022 -0.0006 0.0086  255 ARG B NE  
6266  C CZ  . ARG B 255 ? 0.3327 0.3581 0.5911 0.0018  0.0001  0.0107  255 ARG B CZ  
6267  N NH1 . ARG B 255 ? 0.3298 0.3524 0.5855 0.0057  0.0005  0.0120  255 ARG B NH1 
6268  N NH2 . ARG B 255 ? 0.3199 0.3513 0.5829 0.0019  0.0009  0.0114  255 ARG B NH2 
6269  N N   . ASP B 256 ? 0.2689 0.2669 0.5203 -0.0058 0.0035  0.0057  256 ASP B N   
6270  C CA  . ASP B 256 ? 0.2564 0.2529 0.5078 -0.0091 0.0034  0.0055  256 ASP B CA  
6271  C C   . ASP B 256 ? 0.2620 0.2605 0.5155 -0.0086 0.0049  0.0070  256 ASP B C   
6272  O O   . ASP B 256 ? 0.2517 0.2540 0.5068 -0.0113 0.0053  0.0076  256 ASP B O   
6273  C CB  . ASP B 256 ? 0.2516 0.2392 0.4994 -0.0095 0.0035  0.0043  256 ASP B CB  
6274  C CG  . ASP B 256 ? 0.2612 0.2448 0.5055 -0.0105 0.0026  0.0022  256 ASP B CG  
6275  O OD1 . ASP B 256 ? 0.2639 0.2519 0.5080 -0.0118 0.0014  0.0015  256 ASP B OD1 
6276  O OD2 . ASP B 256 ? 0.2950 0.2710 0.5363 -0.0096 0.0029  0.0013  256 ASP B OD2 
6277  N N   . LEU B 257 ? 0.2620 0.2580 0.5151 -0.0055 0.0058  0.0076  257 LEU B N   
6278  C CA  . LEU B 257 ? 0.2568 0.2528 0.5100 -0.0049 0.0072  0.0086  257 LEU B CA  
6279  C C   . LEU B 257 ? 0.2703 0.2738 0.5265 -0.0035 0.0083  0.0095  257 LEU B C   
6280  O O   . LEU B 257 ? 0.2896 0.2957 0.5464 -0.0043 0.0098  0.0102  257 LEU B O   
6281  C CB  . LEU B 257 ? 0.2610 0.2519 0.5123 -0.0027 0.0073  0.0085  257 LEU B CB  
6282  C CG  . LEU B 257 ? 0.2923 0.2773 0.5414 -0.0035 0.0064  0.0081  257 LEU B CG  
6283  C CD1 . LEU B 257 ? 0.2900 0.2726 0.5388 -0.0015 0.0059  0.0079  257 LEU B CD1 
6284  C CD2 . LEU B 257 ? 0.2875 0.2700 0.5344 -0.0056 0.0067  0.0089  257 LEU B CD2 
6285  N N   . ILE B 258 ? 0.2465 0.2534 0.5040 -0.0011 0.0078  0.0097  258 ILE B N   
6286  C CA  . ILE B 258 ? 0.2410 0.2558 0.5018 0.0011  0.0085  0.0108  258 ILE B CA  
6287  C C   . ILE B 258 ? 0.2447 0.2679 0.5092 -0.0023 0.0079  0.0109  258 ILE B C   
6288  O O   . ILE B 258 ? 0.2310 0.2618 0.4991 -0.0018 0.0093  0.0118  258 ILE B O   
6289  C CB  . ILE B 258 ? 0.2393 0.2549 0.4997 0.0046  0.0076  0.0113  258 ILE B CB  
6290  C CG1 . ILE B 258 ? 0.2587 0.2664 0.5156 0.0074  0.0088  0.0115  258 ILE B CG1 
6291  C CG2 . ILE B 258 ? 0.2562 0.2815 0.5205 0.0072  0.0074  0.0126  258 ILE B CG2 
6292  C CD1 . ILE B 258 ? 0.2674 0.2734 0.5225 0.0097  0.0080  0.0123  258 ILE B CD1 
6293  N N   . ASP B 259 ? 0.2263 0.2484 0.4900 -0.0059 0.0058  0.0099  259 ASP B N   
6294  C CA  . ASP B 259 ? 0.2367 0.2652 0.5030 -0.0107 0.0048  0.0096  259 ASP B CA  
6295  C C   . ASP B 259 ? 0.2294 0.2570 0.4960 -0.0143 0.0068  0.0101  259 ASP B C   
6296  O O   . ASP B 259 ? 0.2194 0.2547 0.4895 -0.0182 0.0068  0.0104  259 ASP B O   
6297  C CB  . ASP B 259 ? 0.2427 0.2668 0.5058 -0.0141 0.0023  0.0079  259 ASP B CB  
6298  C CG  . ASP B 259 ? 0.2335 0.2601 0.4959 -0.0115 0.0003  0.0076  259 ASP B CG  
6299  O OD1 . ASP B 259 ? 0.2189 0.2545 0.4849 -0.0089 -0.0003 0.0089  259 ASP B OD1 
6300  O OD2 . ASP B 259 ? 0.2349 0.2545 0.4926 -0.0121 -0.0006 0.0061  259 ASP B OD2 
6301  N N   . ALA B 260 ? 0.2386 0.2576 0.5013 -0.0130 0.0083  0.0102  260 ALA B N   
6302  C CA  . ALA B 260 ? 0.2442 0.2615 0.5057 -0.0157 0.0105  0.0111  260 ALA B CA  
6303  C C   . ALA B 260 ? 0.2669 0.2907 0.5309 -0.0128 0.0133  0.0123  260 ALA B C   
6304  O O   . ALA B 260 ? 0.2999 0.3228 0.5621 -0.0145 0.0157  0.0132  260 ALA B O   
6305  C CB  . ALA B 260 ? 0.2407 0.2460 0.4963 -0.0153 0.0103  0.0109  260 ALA B CB  
6306  N N   . GLY B 261 ? 0.3007 0.3302 0.5676 -0.0079 0.0135  0.0124  261 GLY B N   
6307  C CA  . GLY B 261 ? 0.2753 0.3102 0.5440 -0.0041 0.0165  0.0132  261 GLY B CA  
6308  C C   . GLY B 261 ? 0.2567 0.2830 0.5204 0.0008  0.0175  0.0127  261 GLY B C   
6309  O O   . GLY B 261 ? 0.3158 0.3444 0.5792 0.0043  0.0203  0.0129  261 GLY B O   
6310  N N   . ALA B 262 ? 0.2525 0.2694 0.5122 0.0010  0.0155  0.0119  262 ALA B N   
6311  C CA  . ALA B 262 ? 0.2428 0.2517 0.4978 0.0043  0.0162  0.0112  262 ALA B CA  
6312  C C   . ALA B 262 ? 0.2444 0.2546 0.5001 0.0094  0.0169  0.0113  262 ALA B C   
6313  O O   . ALA B 262 ? 0.2296 0.2439 0.4883 0.0106  0.0154  0.0119  262 ALA B O   
6314  C CB  . ALA B 262 ? 0.2449 0.2457 0.4969 0.0028  0.0139  0.0105  262 ALA B CB  
6315  N N   . VAL B 263 ? 0.2725 0.2780 0.5242 0.0126  0.0190  0.0108  263 VAL B N   
6316  C CA  . VAL B 263 ? 0.2803 0.2837 0.5307 0.0180  0.0200  0.0109  263 VAL B CA  
6317  C C   . VAL B 263 ? 0.2865 0.2777 0.5301 0.0184  0.0198  0.0096  263 VAL B C   
6318  O O   . VAL B 263 ? 0.2936 0.2792 0.5334 0.0225  0.0212  0.0093  263 VAL B O   
6319  C CB  . VAL B 263 ? 0.2904 0.2999 0.5421 0.0222  0.0234  0.0111  263 VAL B CB  
6320  C CG1 . VAL B 263 ? 0.3018 0.3257 0.5618 0.0218  0.0233  0.0126  263 VAL B CG1 
6321  C CG2 . VAL B 263 ? 0.3017 0.3075 0.5488 0.0208  0.0259  0.0101  263 VAL B CG2 
6322  N N   . GLY B 264 ? 0.2587 0.2457 0.5006 0.0140  0.0179  0.0089  264 GLY B N   
6323  C CA  . GLY B 264 ? 0.2584 0.2359 0.4952 0.0128  0.0169  0.0077  264 GLY B CA  
6324  C C   . GLY B 264 ? 0.2721 0.2496 0.5106 0.0087  0.0142  0.0077  264 GLY B C   
6325  O O   . GLY B 264 ? 0.2294 0.2107 0.4698 0.0066  0.0136  0.0081  264 GLY B O   
6326  N N   . MET B 265 ? 0.2779 0.2513 0.5158 0.0077  0.0128  0.0074  265 MET B N   
6327  C CA  . MET B 265 ? 0.2766 0.2516 0.5173 0.0050  0.0107  0.0075  265 MET B CA  
6328  C C   . MET B 265 ? 0.2816 0.2517 0.5201 0.0030  0.0094  0.0066  265 MET B C   
6329  O O   . MET B 265 ? 0.2683 0.2339 0.5046 0.0031  0.0100  0.0063  265 MET B O   
6330  C CB  . MET B 265 ? 0.2899 0.2685 0.5340 0.0056  0.0105  0.0085  265 MET B CB  
6331  C CG  . MET B 265 ? 0.2992 0.2841 0.5460 0.0068  0.0110  0.0093  265 MET B CG  
6332  S SD  . MET B 265 ? 0.3023 0.2903 0.5511 0.0038  0.0099  0.0090  265 MET B SD  
6333  C CE  . MET B 265 ? 0.3129 0.3013 0.5634 0.0026  0.0083  0.0087  265 MET B CE  
6334  N N   . CYS B 266 ? 0.2630 0.2342 0.5022 0.0010  0.0076  0.0062  266 CYS B N   
6335  C CA  . CYS B 266 ? 0.2661 0.2355 0.5048 -0.0013 0.0057  0.0054  266 CYS B CA  
6336  C C   . CYS B 266 ? 0.2691 0.2433 0.5129 -0.0021 0.0043  0.0058  266 CYS B C   
6337  O O   . CYS B 266 ? 0.2455 0.2214 0.4901 -0.0026 0.0024  0.0058  266 CYS B O   
6338  C CB  . CYS B 266 ? 0.2659 0.2326 0.5002 -0.0022 0.0044  0.0045  266 CYS B CB  
6339  S SG  . CYS B 266 ? 0.2632 0.2232 0.4900 -0.0007 0.0067  0.0033  266 CYS B SG  
6340  N N   . PRO B 267 ? 0.2799 0.2563 0.5268 -0.0019 0.0053  0.0063  267 PRO B N   
6341  C CA  . PRO B 267 ? 0.2725 0.2534 0.5239 -0.0024 0.0045  0.0064  267 PRO B CA  
6342  C C   . PRO B 267 ? 0.2910 0.2739 0.5442 -0.0042 0.0025  0.0059  267 PRO B C   
6343  O O   . PRO B 267 ? 0.3072 0.2876 0.5582 -0.0065 0.0019  0.0053  267 PRO B O   
6344  C CB  . PRO B 267 ? 0.2586 0.2400 0.5109 -0.0024 0.0064  0.0070  267 PRO B CB  
6345  C CG  . PRO B 267 ? 0.2607 0.2366 0.5089 -0.0026 0.0074  0.0072  267 PRO B CG  
6346  C CD  . PRO B 267 ? 0.2626 0.2371 0.5083 -0.0009 0.0072  0.0069  267 PRO B CD  
6347  N N   . PHE B 268 ? 0.2787 0.2661 0.5355 -0.0031 0.0012  0.0060  268 PHE B N   
6348  C CA  . PHE B 268 ? 0.2899 0.2817 0.5497 -0.0040 -0.0012 0.0058  268 PHE B CA  
6349  C C   . PHE B 268 ? 0.2690 0.2676 0.5351 -0.0041 -0.0004 0.0059  268 PHE B C   
6350  O O   . PHE B 268 ? 0.2669 0.2674 0.5350 -0.0012 0.0006  0.0061  268 PHE B O   
6351  C CB  . PHE B 268 ? 0.2952 0.2868 0.5539 -0.0016 -0.0034 0.0063  268 PHE B CB  
6352  C CG  . PHE B 268 ? 0.3062 0.3024 0.5671 -0.0021 -0.0068 0.0063  268 PHE B CG  
6353  C CD1 . PHE B 268 ? 0.3322 0.3362 0.5998 -0.0003 -0.0077 0.0066  268 PHE B CD1 
6354  C CD2 . PHE B 268 ? 0.2951 0.2889 0.5517 -0.0042 -0.0091 0.0058  268 PHE B CD2 
6355  C CE1 . PHE B 268 ? 0.3205 0.3308 0.5912 -0.0006 -0.0114 0.0068  268 PHE B CE1 
6356  C CE2 . PHE B 268 ? 0.3273 0.3263 0.5859 -0.0051 -0.0129 0.0058  268 PHE B CE2 
6357  C CZ  . PHE B 268 ? 0.3136 0.3216 0.5798 -0.0032 -0.0142 0.0064  268 PHE B CZ  
6358  N N   . TYR B 269 ? 0.2518 0.2538 0.5207 -0.0075 -0.0004 0.0056  269 TYR B N   
6359  C CA  . TYR B 269 ? 0.2690 0.2670 0.5344 -0.0116 -0.0013 0.0050  269 TYR B CA  
6360  C C   . TYR B 269 ? 0.2542 0.2562 0.5235 -0.0159 -0.0001 0.0051  269 TYR B C   
6361  O O   . TYR B 269 ? 0.2474 0.2561 0.5221 -0.0152 0.0017  0.0057  269 TYR B O   
6362  C CB  . TYR B 269 ? 0.2791 0.2773 0.5427 -0.0127 -0.0051 0.0043  269 TYR B CB  
6363  C CG  . TYR B 269 ? 0.2673 0.2754 0.5374 -0.0136 -0.0083 0.0043  269 TYR B CG  
6364  C CD1 . TYR B 269 ? 0.2636 0.2811 0.5416 -0.0115 -0.0076 0.0050  269 TYR B CD1 
6365  C CD2 . TYR B 269 ? 0.3064 0.3150 0.5742 -0.0159 -0.0122 0.0035  269 TYR B CD2 
6366  C CE1 . TYR B 269 ? 0.2529 0.2812 0.5378 -0.0115 -0.0106 0.0052  269 TYR B CE1 
6367  C CE2 . TYR B 269 ? 0.2973 0.3164 0.5714 -0.0165 -0.0159 0.0036  269 TYR B CE2 
6368  C CZ  . TYR B 269 ? 0.2623 0.2920 0.5456 -0.0139 -0.0151 0.0046  269 TYR B CZ  
6369  O OH  . TYR B 269 ? 0.2655 0.3070 0.5559 -0.0134 -0.0187 0.0050  269 TYR B OH  
6370  N N   . TYR B 270 ? 0.2704 0.2682 0.5366 -0.0206 -0.0009 0.0043  270 TYR B N   
6371  C CA  . TYR B 270 ? 0.2497 0.2485 0.5177 -0.0258 0.0007  0.0045  270 TYR B CA  
6372  C C   . TYR B 270 ? 0.2379 0.2501 0.5157 -0.0274 0.0007  0.0050  270 TYR B C   
6373  O O   . TYR B 270 ? 0.2129 0.2284 0.4936 -0.0278 0.0041  0.0061  270 TYR B O   
6374  C CB  . TYR B 270 ? 0.2537 0.2456 0.5163 -0.0308 -0.0014 0.0031  270 TYR B CB  
6375  C CG  . TYR B 270 ? 0.2559 0.2476 0.5197 -0.0377 -0.0001 0.0032  270 TYR B CG  
6376  C CD1 . TYR B 270 ? 0.2731 0.2606 0.5354 -0.0384 0.0040  0.0048  270 TYR B CD1 
6377  C CD2 . TYR B 270 ? 0.2465 0.2426 0.5127 -0.0440 -0.0031 0.0019  270 TYR B CD2 
6378  C CE1 . TYR B 270 ? 0.2833 0.2697 0.5460 -0.0453 0.0056  0.0054  270 TYR B CE1 
6379  C CE2 . TYR B 270 ? 0.2635 0.2596 0.5310 -0.0514 -0.0018 0.0021  270 TYR B CE2 
6380  C CZ  . TYR B 270 ? 0.2650 0.2559 0.5306 -0.0522 0.0028  0.0040  270 TYR B CZ  
6381  O OH  . TYR B 270 ? 0.2552 0.2455 0.5216 -0.0602 0.0045  0.0046  270 TYR B OH  
6382  N N   . ALA B 271 ? 0.2521 0.2729 0.5349 -0.0284 -0.0031 0.0043  271 ALA B N   
6383  C CA  . ALA B 271 ? 0.2492 0.2846 0.5424 -0.0305 -0.0034 0.0047  271 ALA B CA  
6384  C C   . ALA B 271 ? 0.2355 0.2812 0.5346 -0.0262 -0.0072 0.0047  271 ALA B C   
6385  O O   . ALA B 271 ? 0.2408 0.2826 0.5355 -0.0251 -0.0110 0.0040  271 ALA B O   
6386  C CB  . ALA B 271 ? 0.2573 0.2937 0.5511 -0.0391 -0.0046 0.0040  271 ALA B CB  
6387  N N   . ASP B 272 ? 0.2471 0.3061 0.5559 -0.0240 -0.0061 0.0054  272 ASP B N   
6388  C CA  . ASP B 272 ? 0.2566 0.3271 0.5724 -0.0195 -0.0096 0.0057  272 ASP B CA  
6389  C C   . ASP B 272 ? 0.2537 0.3288 0.5704 -0.0235 -0.0155 0.0050  272 ASP B C   
6390  O O   . ASP B 272 ? 0.2716 0.3487 0.5893 -0.0314 -0.0163 0.0042  272 ASP B O   
6391  C CB  . ASP B 272 ? 0.2478 0.3343 0.5753 -0.0179 -0.0073 0.0064  272 ASP B CB  
6392  C CG  . ASP B 272 ? 0.2640 0.3489 0.5914 -0.0113 -0.0025 0.0069  272 ASP B CG  
6393  O OD1 . ASP B 272 ? 0.2762 0.3480 0.5949 -0.0075 -0.0020 0.0067  272 ASP B OD1 
6394  O OD2 . ASP B 272 ? 0.2323 0.3290 0.5680 -0.0106 0.0008  0.0072  272 ASP B OD2 
6395  N N   . GLY B 273 ? 0.2347 0.3108 0.5504 -0.0182 -0.0196 0.0054  273 GLY B N   
6396  C CA  . GLY B 273 ? 0.2332 0.3163 0.5505 -0.0206 -0.0259 0.0051  273 GLY B CA  
6397  C C   . GLY B 273 ? 0.2205 0.3190 0.5476 -0.0143 -0.0288 0.0065  273 GLY B C   
6398  O O   . GLY B 273 ? 0.2227 0.3172 0.5464 -0.0070 -0.0302 0.0076  273 GLY B O   
6399  N N   . TRP B 274 ? 0.2142 0.3305 0.5533 -0.0175 -0.0301 0.0066  274 TRP B N   
6400  C CA  . TRP B 274 ? 0.2199 0.3533 0.5701 -0.0109 -0.0323 0.0080  274 TRP B CA  
6401  C C   . TRP B 274 ? 0.2385 0.3727 0.5855 -0.0069 -0.0395 0.0089  274 TRP B C   
6402  O O   . TRP B 274 ? 0.2456 0.3890 0.5986 0.0014  -0.0414 0.0106  274 TRP B O   
6403  C CB  . TRP B 274 ? 0.2126 0.3665 0.5770 -0.0166 -0.0323 0.0079  274 TRP B CB  
6404  C CG  . TRP B 274 ? 0.1932 0.3486 0.5618 -0.0190 -0.0248 0.0077  274 TRP B CG  
6405  C CD1 . TRP B 274 ? 0.2065 0.3459 0.5663 -0.0186 -0.0191 0.0074  274 TRP B CD1 
6406  C CD2 . TRP B 274 ? 0.1884 0.3633 0.5709 -0.0227 -0.0222 0.0081  274 TRP B CD2 
6407  N NE1 . TRP B 274 ? 0.2081 0.3548 0.5745 -0.0214 -0.0132 0.0076  274 TRP B NE1 
6408  C CE2 . TRP B 274 ? 0.1874 0.3555 0.5675 -0.0242 -0.0147 0.0081  274 TRP B CE2 
6409  C CE3 . TRP B 274 ? 0.1872 0.3856 0.5841 -0.0249 -0.0256 0.0086  274 TRP B CE3 
6410  C CZ2 . TRP B 274 ? 0.1901 0.3729 0.5808 -0.0281 -0.0099 0.0086  274 TRP B CZ2 
6411  C CZ3 . TRP B 274 ? 0.1827 0.3971 0.5915 -0.0289 -0.0208 0.0090  274 TRP B CZ3 
6412  C CH2 . TRP B 274 ? 0.1832 0.3893 0.5884 -0.0309 -0.0128 0.0090  274 TRP B CH2 
6413  N N   . TRP B 275 ? 0.2522 0.3766 0.5892 -0.0124 -0.0434 0.0078  275 TRP B N   
6414  C CA  . TRP B 275 ? 0.2528 0.3777 0.5852 -0.0096 -0.0505 0.0086  275 TRP B CA  
6415  C C   . TRP B 275 ? 0.2659 0.3784 0.5900 -0.0002 -0.0496 0.0105  275 TRP B C   
6416  O O   . TRP B 275 ? 0.2975 0.4122 0.6197 0.0052  -0.0546 0.0123  275 TRP B O   
6417  C CB  . TRP B 275 ? 0.2405 0.3573 0.5629 -0.0181 -0.0544 0.0066  275 TRP B CB  
6418  C CG  . TRP B 275 ? 0.2735 0.3682 0.5814 -0.0193 -0.0505 0.0055  275 TRP B CG  
6419  C CD1 . TRP B 275 ? 0.2705 0.3555 0.5750 -0.0246 -0.0452 0.0038  275 TRP B CD1 
6420  C CD2 . TRP B 275 ? 0.2709 0.3512 0.5660 -0.0148 -0.0515 0.0062  275 TRP B CD2 
6421  N NE1 . TRP B 275 ? 0.2704 0.3376 0.5622 -0.0232 -0.0429 0.0033  275 TRP B NE1 
6422  C CE2 . TRP B 275 ? 0.2797 0.3439 0.5655 -0.0177 -0.0465 0.0047  275 TRP B CE2 
6423  C CE3 . TRP B 275 ? 0.2928 0.3724 0.5831 -0.0087 -0.0560 0.0083  275 TRP B CE3 
6424  C CZ2 . TRP B 275 ? 0.3062 0.3553 0.5793 -0.0151 -0.0456 0.0050  275 TRP B CZ2 
6425  C CZ3 . TRP B 275 ? 0.2888 0.3520 0.5655 -0.0065 -0.0549 0.0087  275 TRP B CZ3 
6426  C CH2 . TRP B 275 ? 0.3086 0.3576 0.5774 -0.0098 -0.0497 0.0070  275 TRP B CH2 
6427  N N   . LYS B 276 ? 0.2870 0.3860 0.6056 0.0013  -0.0434 0.0102  276 LYS B N   
6428  C CA  . LYS B 276 ? 0.3005 0.3840 0.6083 0.0072  -0.0424 0.0114  276 LYS B CA  
6429  C C   . LYS B 276 ? 0.3099 0.3978 0.6209 0.0171  -0.0443 0.0140  276 LYS B C   
6430  O O   . LYS B 276 ? 0.3509 0.4284 0.6526 0.0212  -0.0463 0.0156  276 LYS B O   
6431  C CB  . LYS B 276 ? 0.2748 0.3452 0.5774 0.0058  -0.0357 0.0104  276 LYS B CB  
6432  C CG  . LYS B 276 ? 0.2900 0.3523 0.5857 -0.0025 -0.0350 0.0083  276 LYS B CG  
6433  C CD  . LYS B 276 ? 0.2993 0.3509 0.5911 -0.0039 -0.0288 0.0074  276 LYS B CD  
6434  C CE  . LYS B 276 ? 0.3102 0.3500 0.5945 0.0014  -0.0268 0.0085  276 LYS B CE  
6435  N NZ  . LYS B 276 ? 0.3324 0.3616 0.6057 0.0000  -0.0287 0.0084  276 LYS B NZ  
6436  N N   . GLY B 277 ? 0.3040 0.4064 0.6274 0.0212  -0.0434 0.0145  277 GLY B N   
6437  C CA  . GLY B 277 ? 0.3322 0.4379 0.6580 0.0315  -0.0452 0.0169  277 GLY B CA  
6438  C C   . GLY B 277 ? 0.3447 0.4684 0.6791 0.0339  -0.0521 0.0184  277 GLY B C   
6439  O O   . GLY B 277 ? 0.3576 0.4896 0.6985 0.0430  -0.0531 0.0203  277 GLY B O   
6440  N N   . GLY B 278 ? 0.3426 0.4723 0.6767 0.0259  -0.0570 0.0174  278 GLY B N   
6441  C CA  . GLY B 278 ? 0.3648 0.5145 0.7085 0.0261  -0.0640 0.0184  278 GLY B CA  
6442  C C   . GLY B 278 ? 0.3874 0.5581 0.7480 0.0224  -0.0620 0.0171  278 GLY B C   
6443  O O   . GLY B 278 ? 0.4510 0.6215 0.8165 0.0232  -0.0549 0.0163  278 GLY B O   
6444  N N   . GLU B 279 ? 0.3695 0.5588 0.7388 0.0178  -0.0682 0.0170  279 GLU B N   
6445  C CA  . GLU B 279 ? 0.3988 0.6095 0.7842 0.0118  -0.0671 0.0158  279 GLU B CA  
6446  C C   . GLU B 279 ? 0.3817 0.5831 0.7641 0.0015  -0.0606 0.0131  279 GLU B C   
6447  O O   . GLU B 279 ? 0.4059 0.6062 0.7922 0.0032  -0.0532 0.0128  279 GLU B O   
6448  C CB  . GLU B 279 ? 0.4502 0.6787 0.8505 0.0217  -0.0645 0.0176  279 GLU B CB  
6449  C CG  . GLU B 279 ? 0.5281 0.7705 0.9340 0.0312  -0.0721 0.0205  279 GLU B CG  
6450  C CD  . GLU B 279 ? 0.6325 0.8813 1.0461 0.0454  -0.0687 0.0226  279 GLU B CD  
6451  O OE1 . GLU B 279 ? 0.6117 0.8783 1.0403 0.0470  -0.0643 0.0223  279 GLU B OE1 
6452  O OE2 . GLU B 279 ? 0.7580 0.9924 1.1614 0.0551  -0.0702 0.0247  279 GLU B OE2 
6453  N N   . LYS B 280 ? 0.3685 0.5635 0.7437 -0.0092 -0.0636 0.0110  280 LYS B N   
6454  C CA  . LYS B 280 ? 0.3446 0.5300 0.7159 -0.0193 -0.0583 0.0086  280 LYS B CA  
6455  C C   . LYS B 280 ? 0.3043 0.5067 0.6904 -0.0247 -0.0540 0.0083  280 LYS B C   
6456  O O   . LYS B 280 ? 0.2771 0.4703 0.6601 -0.0307 -0.0480 0.0071  280 LYS B O   
6457  C CB  . LYS B 280 ? 0.3710 0.5493 0.7328 -0.0291 -0.0639 0.0065  280 LYS B CB  
6458  C CG  . LYS B 280 ? 0.3694 0.5683 0.7407 -0.0359 -0.0714 0.0058  280 LYS B CG  
6459  C CD  . LYS B 280 ? 0.3964 0.5829 0.7542 -0.0449 -0.0765 0.0032  280 LYS B CD  
6460  C CE  . LYS B 280 ? 0.4121 0.6141 0.7763 -0.0557 -0.0830 0.0013  280 LYS B CE  
6461  N NZ  . LYS B 280 ? 0.4508 0.6713 0.8220 -0.0502 -0.0914 0.0032  280 LYS B NZ  
6462  N N   . SER B 281 ? 0.2747 0.5024 0.6770 -0.0228 -0.0568 0.0094  281 SER B N   
6463  C CA  . SER B 281 ? 0.2677 0.5141 0.6849 -0.0290 -0.0529 0.0092  281 SER B CA  
6464  C C   . SER B 281 ? 0.2607 0.5134 0.6860 -0.0194 -0.0456 0.0107  281 SER B C   
6465  O O   . SER B 281 ? 0.2678 0.5366 0.7056 -0.0226 -0.0410 0.0109  281 SER B O   
6466  C CB  . SER B 281 ? 0.2642 0.5369 0.6954 -0.0340 -0.0602 0.0094  281 SER B CB  
6467  O OG  . SER B 281 ? 0.2641 0.5302 0.6867 -0.0445 -0.0668 0.0074  281 SER B OG  
6468  N N   . ASP B 282 ? 0.2723 0.5110 0.6893 -0.0080 -0.0440 0.0117  282 ASP B N   
6469  C CA  . ASP B 282 ? 0.2848 0.5266 0.7070 0.0022  -0.0376 0.0127  282 ASP B CA  
6470  C C   . ASP B 282 ? 0.2626 0.4783 0.6697 0.0052  -0.0321 0.0121  282 ASP B C   
6471  O O   . ASP B 282 ? 0.2370 0.4339 0.6305 0.0053  -0.0349 0.0118  282 ASP B O   
6472  C CB  . ASP B 282 ? 0.3328 0.5856 0.7612 0.0150  -0.0417 0.0147  282 ASP B CB  
6473  C CG  . ASP B 282 ? 0.3945 0.6564 0.8318 0.0253  -0.0351 0.0155  282 ASP B CG  
6474  O OD1 . ASP B 282 ? 0.4593 0.7456 0.9130 0.0243  -0.0335 0.0158  282 ASP B OD1 
6475  O OD2 . ASP B 282 ? 0.4229 0.6673 0.8505 0.0337  -0.0315 0.0155  282 ASP B OD2 
6476  N N   . HIS B 283 ? 0.2477 0.4637 0.6577 0.0072  -0.0242 0.0118  283 HIS B N   
6477  C CA  . HIS B 283 ? 0.2467 0.4407 0.6440 0.0103  -0.0189 0.0111  283 HIS B CA  
6478  C C   . HIS B 283 ? 0.2602 0.4538 0.6583 0.0237  -0.0169 0.0119  283 HIS B C   
6479  O O   . HIS B 283 ? 0.2540 0.4569 0.6595 0.0280  -0.0113 0.0117  283 HIS B O   
6480  C CB  . HIS B 283 ? 0.2210 0.4118 0.6174 0.0030  -0.0118 0.0102  283 HIS B CB  
6481  C CG  . HIS B 283 ? 0.1933 0.3599 0.5744 0.0021  -0.0091 0.0094  283 HIS B CG  
6482  N ND1 . HIS B 283 ? 0.1744 0.3338 0.5515 -0.0007 -0.0024 0.0089  283 HIS B ND1 
6483  C CD2 . HIS B 283 ? 0.1899 0.3388 0.5588 0.0035  -0.0124 0.0092  283 HIS B CD2 
6484  C CE1 . HIS B 283 ? 0.1826 0.3214 0.5463 -0.0005 -0.0021 0.0083  283 HIS B CE1 
6485  N NE2 . HIS B 283 ? 0.1822 0.3145 0.5410 0.0021  -0.0078 0.0085  283 HIS B NE2 
6486  N N   . SER B 284 ? 0.2762 0.4593 0.6667 0.0301  -0.0216 0.0128  284 SER B N   
6487  C CA  . SER B 284 ? 0.3023 0.4843 0.6931 0.0429  -0.0210 0.0137  284 SER B CA  
6488  C C   . SER B 284 ? 0.2921 0.4595 0.6754 0.0464  -0.0135 0.0124  284 SER B C   
6489  O O   . SER B 284 ? 0.2463 0.3958 0.6181 0.0415  -0.0117 0.0114  284 SER B O   
6490  C CB  . SER B 284 ? 0.3553 0.5263 0.7371 0.0476  -0.0275 0.0153  284 SER B CB  
6491  O OG  . SER B 284 ? 0.3821 0.5406 0.7574 0.0583  -0.0254 0.0159  284 SER B OG  
6492  N N   . LEU B 285 ? 0.2979 0.4734 0.6878 0.0553  -0.0094 0.0123  285 LEU B N   
6493  C CA  . LEU B 285 ? 0.3126 0.4756 0.6955 0.0592  -0.0024 0.0106  285 LEU B CA  
6494  C C   . LEU B 285 ? 0.3028 0.4416 0.6705 0.0638  -0.0036 0.0105  285 LEU B C   
6495  O O   . LEU B 285 ? 0.2694 0.3937 0.6280 0.0630  0.0010  0.0088  285 LEU B O   
6496  C CB  . LEU B 285 ? 0.3268 0.5052 0.7203 0.0681  0.0024  0.0103  285 LEU B CB  
6497  C CG  . LEU B 285 ? 0.3418 0.5461 0.7514 0.0629  0.0044  0.0105  285 LEU B CG  
6498  C CD1 . LEU B 285 ? 0.3121 0.5300 0.7308 0.0727  0.0105  0.0100  285 LEU B CD1 
6499  C CD2 . LEU B 285 ? 0.2919 0.4943 0.6994 0.0493  0.0074  0.0097  285 LEU B CD2 
6500  N N   . ASN B 286 ? 0.3041 0.4387 0.6687 0.0678  -0.0098 0.0124  286 ASN B N   
6501  C CA  . ASN B 286 ? 0.3333 0.4458 0.6841 0.0729  -0.0105 0.0126  286 ASN B CA  
6502  C C   . ASN B 286 ? 0.3019 0.4022 0.6431 0.0668  -0.0157 0.0138  286 ASN B C   
6503  O O   . ASN B 286 ? 0.3342 0.4193 0.6655 0.0711  -0.0177 0.0150  286 ASN B O   
6504  C CB  . ASN B 286 ? 0.3435 0.4567 0.6959 0.0861  -0.0115 0.0139  286 ASN B CB  
6505  C CG  . ASN B 286 ? 0.3702 0.4953 0.7288 0.0899  -0.0187 0.0169  286 ASN B CG  
6506  O OD1 . ASN B 286 ? 0.4046 0.5423 0.7694 0.0826  -0.0228 0.0176  286 ASN B OD1 
6507  N ND2 . ASN B 286 ? 0.3927 0.5131 0.7489 0.1012  -0.0207 0.0187  286 ASN B ND2 
6508  N N   . GLN B 287 ? 0.2876 0.3927 0.6305 0.0566  -0.0171 0.0134  287 GLN B N   
6509  C CA  . GLN B 287 ? 0.2892 0.3822 0.6222 0.0507  -0.0209 0.0140  287 GLN B CA  
6510  C C   . GLN B 287 ? 0.3005 0.3815 0.6262 0.0433  -0.0168 0.0122  287 GLN B C   
6511  O O   . GLN B 287 ? 0.3212 0.4077 0.6500 0.0354  -0.0159 0.0112  287 GLN B O   
6512  C CB  . GLN B 287 ? 0.3104 0.4148 0.6480 0.0451  -0.0267 0.0148  287 GLN B CB  
6513  C CG  . GLN B 287 ? 0.3249 0.4415 0.6690 0.0524  -0.0323 0.0171  287 GLN B CG  
6514  C CD  . GLN B 287 ? 0.3345 0.4365 0.6674 0.0586  -0.0360 0.0193  287 GLN B CD  
6515  O OE1 . GLN B 287 ? 0.3389 0.4235 0.6594 0.0550  -0.0358 0.0193  287 GLN B OE1 
6516  N NE2 . GLN B 287 ? 0.3219 0.4317 0.6595 0.0680  -0.0393 0.0215  287 GLN B NE2 
6517  N N   . PRO B 288 ? 0.2978 0.3612 0.6128 0.0454  -0.0148 0.0119  288 PRO B N   
6518  C CA  . PRO B 288 ? 0.2943 0.3463 0.6019 0.0391  -0.0116 0.0104  288 PRO B CA  
6519  C C   . PRO B 288 ? 0.2634 0.3163 0.5697 0.0305  -0.0135 0.0103  288 PRO B C   
6520  O O   . PRO B 288 ? 0.2594 0.3105 0.5649 0.0251  -0.0103 0.0091  288 PRO B O   
6521  C CB  . PRO B 288 ? 0.2961 0.3311 0.5927 0.0424  -0.0120 0.0111  288 PRO B CB  
6522  C CG  . PRO B 288 ? 0.3162 0.3524 0.6151 0.0519  -0.0119 0.0117  288 PRO B CG  
6523  C CD  . PRO B 288 ? 0.3150 0.3683 0.6240 0.0538  -0.0159 0.0132  288 PRO B CD  
6524  N N   . GLU B 289 ? 0.2595 0.3138 0.5646 0.0299  -0.0186 0.0116  289 GLU B N   
6525  C CA  . GLU B 289 ? 0.2768 0.3285 0.5777 0.0226  -0.0209 0.0113  289 GLU B CA  
6526  C C   . GLU B 289 ? 0.2585 0.3212 0.5668 0.0162  -0.0202 0.0101  289 GLU B C   
6527  O O   . GLU B 289 ? 0.2536 0.3108 0.5572 0.0097  -0.0200 0.0091  289 GLU B O   
6528  C CB  . GLU B 289 ? 0.2874 0.3376 0.5839 0.0243  -0.0266 0.0130  289 GLU B CB  
6529  C CG  . GLU B 289 ? 0.2998 0.3344 0.5855 0.0279  -0.0264 0.0143  289 GLU B CG  
6530  C CD  . GLU B 289 ? 0.3268 0.3490 0.6040 0.0229  -0.0234 0.0133  289 GLU B CD  
6531  O OE1 . GLU B 289 ? 0.3145 0.3382 0.5910 0.0168  -0.0238 0.0121  289 GLU B OE1 
6532  O OE2 . GLU B 289 ? 0.3351 0.3464 0.6064 0.0248  -0.0208 0.0136  289 GLU B OE2 
6533  N N   . GLU B 290 ? 0.2408 0.3180 0.5600 0.0182  -0.0193 0.0101  290 GLU B N   
6534  C CA  . GLU B 290 ? 0.2347 0.3242 0.5622 0.0117  -0.0186 0.0093  290 GLU B CA  
6535  C C   . GLU B 290 ? 0.2182 0.3055 0.5461 0.0088  -0.0123 0.0083  290 GLU B C   
6536  O O   . GLU B 290 ? 0.2372 0.3330 0.5709 0.0028  -0.0109 0.0079  290 GLU B O   
6537  C CB  . GLU B 290 ? 0.2536 0.3624 0.5938 0.0154  -0.0207 0.0101  290 GLU B CB  
6538  C CG  . GLU B 290 ? 0.2669 0.3806 0.6074 0.0169  -0.0280 0.0113  290 GLU B CG  
6539  C CD  . GLU B 290 ? 0.2791 0.4139 0.6331 0.0205  -0.0309 0.0124  290 GLU B CD  
6540  O OE1 . GLU B 290 ? 0.2874 0.4368 0.6523 0.0173  -0.0282 0.0118  290 GLU B OE1 
6541  O OE2 . GLU B 290 ? 0.2604 0.3974 0.6137 0.0259  -0.0363 0.0140  290 GLU B OE2 
6542  N N   . TRP B 291 ? 0.2099 0.2854 0.5310 0.0122  -0.0088 0.0080  291 TRP B N   
6543  C CA  . TRP B 291 ? 0.1950 0.2686 0.5158 0.0106  -0.0031 0.0072  291 TRP B CA  
6544  C C   . TRP B 291 ? 0.1973 0.2549 0.5073 0.0089  -0.0015 0.0067  291 TRP B C   
6545  O O   . TRP B 291 ? 0.2023 0.2550 0.5093 0.0112  0.0022  0.0062  291 TRP B O   
6546  C CB  . TRP B 291 ? 0.1937 0.2729 0.5191 0.0177  0.0003  0.0070  291 TRP B CB  
6547  C CG  . TRP B 291 ? 0.1971 0.2944 0.5347 0.0203  -0.0004 0.0075  291 TRP B CG  
6548  C CD1 . TRP B 291 ? 0.1966 0.3008 0.5386 0.0250  -0.0051 0.0085  291 TRP B CD1 
6549  C CD2 . TRP B 291 ? 0.1931 0.3053 0.5405 0.0187  0.0035  0.0074  291 TRP B CD2 
6550  N NE1 . TRP B 291 ? 0.2103 0.3336 0.5650 0.0266  -0.0046 0.0089  291 TRP B NE1 
6551  C CE2 . TRP B 291 ? 0.1870 0.3158 0.5455 0.0226  0.0009  0.0082  291 TRP B CE2 
6552  C CE3 . TRP B 291 ? 0.1913 0.3049 0.5390 0.0141  0.0090  0.0070  291 TRP B CE3 
6553  C CZ2 . TRP B 291 ? 0.1756 0.3233 0.5464 0.0220  0.0039  0.0084  291 TRP B CZ2 
6554  C CZ3 . TRP B 291 ? 0.1752 0.3059 0.5338 0.0132  0.0123  0.0073  291 TRP B CZ3 
6555  C CH2 . TRP B 291 ? 0.1787 0.3270 0.5493 0.0171  0.0099  0.0079  291 TRP B CH2 
6556  N N   . PHE B 292 ? 0.2148 0.2648 0.5188 0.0049  -0.0042 0.0068  292 PHE B N   
6557  C CA  . PHE B 292 ? 0.2203 0.2570 0.5152 0.0039  -0.0027 0.0065  292 PHE B CA  
6558  C C   . PHE B 292 ? 0.2271 0.2607 0.5198 -0.0018 -0.0004 0.0062  292 PHE B C   
6559  O O   . PHE B 292 ? 0.2226 0.2467 0.5085 -0.0023 0.0012  0.0061  292 PHE B O   
6560  C CB  . PHE B 292 ? 0.2517 0.2809 0.5403 0.0038  -0.0063 0.0068  292 PHE B CB  
6561  C CG  . PHE B 292 ? 0.2570 0.2804 0.5419 0.0093  -0.0069 0.0073  292 PHE B CG  
6562  C CD1 . PHE B 292 ? 0.2777 0.2917 0.5566 0.0100  -0.0045 0.0071  292 PHE B CD1 
6563  C CD2 . PHE B 292 ? 0.2736 0.3008 0.5607 0.0136  -0.0100 0.0083  292 PHE B CD2 
6564  C CE1 . PHE B 292 ? 0.2986 0.3062 0.5735 0.0139  -0.0050 0.0075  292 PHE B CE1 
6565  C CE2 . PHE B 292 ? 0.2947 0.3144 0.5771 0.0184  -0.0104 0.0090  292 PHE B CE2 
6566  C CZ  . PHE B 292 ? 0.2980 0.3073 0.5740 0.0180  -0.0078 0.0086  292 PHE B CZ  
6567  N N   . GLY B 293 ? 0.2420 0.2836 0.5401 -0.0063 -0.0004 0.0062  293 GLY B N   
6568  C CA  . GLY B 293 ? 0.2411 0.2775 0.5356 -0.0123 0.0011  0.0061  293 GLY B CA  
6569  C C   . GLY B 293 ? 0.2277 0.2604 0.5198 -0.0122 0.0058  0.0066  293 GLY B C   
6570  O O   . GLY B 293 ? 0.2237 0.2624 0.5197 -0.0093 0.0083  0.0068  293 GLY B O   
6571  N N   . PHE B 294 ? 0.2250 0.2477 0.5101 -0.0150 0.0068  0.0069  294 PHE B N   
6572  C CA  . PHE B 294 ? 0.2328 0.2524 0.5153 -0.0163 0.0108  0.0078  294 PHE B CA  
6573  C C   . PHE B 294 ? 0.2535 0.2802 0.5410 -0.0215 0.0128  0.0085  294 PHE B C   
6574  O O   . PHE B 294 ? 0.2785 0.3058 0.5653 -0.0222 0.0167  0.0096  294 PHE B O   
6575  C CB  . PHE B 294 ? 0.2233 0.2306 0.4971 -0.0171 0.0110  0.0082  294 PHE B CB  
6576  C CG  . PHE B 294 ? 0.2180 0.2198 0.4875 -0.0123 0.0101  0.0078  294 PHE B CG  
6577  C CD1 . PHE B 294 ? 0.2094 0.2152 0.4816 -0.0084 0.0088  0.0071  294 PHE B CD1 
6578  C CD2 . PHE B 294 ? 0.2252 0.2180 0.4880 -0.0118 0.0104  0.0083  294 PHE B CD2 
6579  C CE1 . PHE B 294 ? 0.2138 0.2145 0.4820 -0.0053 0.0080  0.0069  294 PHE B CE1 
6580  C CE2 . PHE B 294 ? 0.2417 0.2315 0.5017 -0.0082 0.0096  0.0080  294 PHE B CE2 
6581  C CZ  . PHE B 294 ? 0.2357 0.2295 0.4985 -0.0055 0.0084  0.0073  294 PHE B CZ  
6582  N N   . TRP B 295 ? 0.2774 0.3093 0.5693 -0.0258 0.0102  0.0080  295 TRP B N   
6583  C CA  . TRP B 295 ? 0.2832 0.3241 0.5814 -0.0318 0.0118  0.0086  295 TRP B CA  
6584  C C   . TRP B 295 ? 0.2688 0.3257 0.5778 -0.0302 0.0099  0.0081  295 TRP B C   
6585  O O   . TRP B 295 ? 0.3028 0.3608 0.6126 -0.0266 0.0059  0.0072  295 TRP B O   
6586  C CB  . TRP B 295 ? 0.2682 0.3022 0.5624 -0.0394 0.0102  0.0083  295 TRP B CB  
6587  C CG  . TRP B 295 ? 0.2783 0.2973 0.5625 -0.0415 0.0129  0.0093  295 TRP B CG  
6588  C CD1 . TRP B 295 ? 0.2955 0.3028 0.5714 -0.0366 0.0134  0.0096  295 TRP B CD1 
6589  C CD2 . TRP B 295 ? 0.2601 0.2742 0.5415 -0.0488 0.0154  0.0105  295 TRP B CD2 
6590  N NE1 . TRP B 295 ? 0.2814 0.2771 0.5495 -0.0395 0.0158  0.0109  295 TRP B NE1 
6591  C CE2 . TRP B 295 ? 0.2631 0.2616 0.5338 -0.0471 0.0172  0.0116  295 TRP B CE2 
6592  C CE3 . TRP B 295 ? 0.2630 0.2845 0.5499 -0.0568 0.0164  0.0110  295 TRP B CE3 
6593  C CZ2 . TRP B 295 ? 0.2762 0.2644 0.5404 -0.0525 0.0199  0.0133  295 TRP B CZ2 
6594  C CZ3 . TRP B 295 ? 0.2840 0.2954 0.5646 -0.0633 0.0193  0.0125  295 TRP B CZ3 
6595  C CH2 . TRP B 295 ? 0.2803 0.2744 0.5491 -0.0608 0.0211  0.0137  295 TRP B CH2 
6596  N N   . GLY B 296 ? 0.2629 0.3323 0.5801 -0.0325 0.0128  0.0088  296 GLY B N   
6597  C CA  . GLY B 296 ? 0.2382 0.3251 0.5672 -0.0307 0.0112  0.0085  296 GLY B CA  
6598  C C   . GLY B 296 ? 0.2310 0.3304 0.5685 -0.0391 0.0117  0.0090  296 GLY B C   
6599  O O   . GLY B 296 ? 0.2155 0.3116 0.5506 -0.0452 0.0155  0.0100  296 GLY B O   
6600  N N   . TYR B 297 ? 0.2304 0.3451 0.5782 -0.0391 0.0078  0.0086  297 TYR B N   
6601  C CA  . TYR B 297 ? 0.2206 0.3494 0.5778 -0.0478 0.0072  0.0088  297 TYR B CA  
6602  C C   . TYR B 297 ? 0.2118 0.3617 0.5825 -0.0446 0.0107  0.0097  297 TYR B C   
6603  O O   . TYR B 297 ? 0.2024 0.3591 0.5775 -0.0351 0.0103  0.0096  297 TYR B O   
6604  C CB  . TYR B 297 ? 0.2265 0.3590 0.5857 -0.0510 -0.0002 0.0076  297 TYR B CB  
6605  C CG  . TYR B 297 ? 0.2478 0.3597 0.5931 -0.0534 -0.0034 0.0064  297 TYR B CG  
6606  C CD1 . TYR B 297 ? 0.2703 0.3710 0.6085 -0.0629 -0.0025 0.0060  297 TYR B CD1 
6607  C CD2 . TYR B 297 ? 0.2452 0.3480 0.5837 -0.0461 -0.0066 0.0057  297 TYR B CD2 
6608  C CE1 . TYR B 297 ? 0.2622 0.3440 0.5875 -0.0642 -0.0049 0.0046  297 TYR B CE1 
6609  C CE2 . TYR B 297 ? 0.2409 0.3261 0.5671 -0.0480 -0.0088 0.0046  297 TYR B CE2 
6610  C CZ  . TYR B 297 ? 0.2560 0.3309 0.5757 -0.0566 -0.0079 0.0039  297 TYR B CZ  
6611  O OH  . TYR B 297 ? 0.2640 0.3214 0.5713 -0.0573 -0.0096 0.0026  297 TYR B OH  
6612  N N   . SER B 298 ? 0.2096 0.3692 0.5866 -0.0528 0.0145  0.0107  298 SER B N   
6613  C CA  . SER B 298 ? 0.1995 0.3785 0.5885 -0.0506 0.0197  0.0117  298 SER B CA  
6614  C C   . SER B 298 ? 0.1997 0.4012 0.6037 -0.0477 0.0153  0.0114  298 SER B C   
6615  O O   . SER B 298 ? 0.1897 0.4053 0.6025 -0.0395 0.0180  0.0117  298 SER B O   
6616  C CB  . SER B 298 ? 0.2053 0.3886 0.5965 -0.0610 0.0251  0.0132  298 SER B CB  
6617  O OG  . SER B 298 ? 0.2081 0.3980 0.6045 -0.0718 0.0210  0.0130  298 SER B OG  
6618  N N   . ASP B 299 ? 0.2165 0.4218 0.6232 -0.0547 0.0087  0.0107  299 ASP B N   
6619  C CA  . ASP B 299 ? 0.2143 0.4423 0.6354 -0.0529 0.0036  0.0106  299 ASP B CA  
6620  C C   . ASP B 299 ? 0.2317 0.4549 0.6490 -0.0595 -0.0048 0.0093  299 ASP B C   
6621  O O   . ASP B 299 ? 0.2556 0.4579 0.6594 -0.0650 -0.0058 0.0084  299 ASP B O   
6622  C CB  . ASP B 299 ? 0.2109 0.4639 0.6481 -0.0572 0.0080  0.0118  299 ASP B CB  
6623  C CG  . ASP B 299 ? 0.2377 0.4928 0.6763 -0.0727 0.0097  0.0122  299 ASP B CG  
6624  O OD1 . ASP B 299 ? 0.2318 0.4702 0.6598 -0.0812 0.0060  0.0112  299 ASP B OD1 
6625  O OD2 . ASP B 299 ? 0.2802 0.5552 0.7315 -0.0765 0.0147  0.0135  299 ASP B OD2 
6626  N N   . LEU B 300 ? 0.2451 0.4882 0.6743 -0.0587 -0.0109 0.0092  300 LEU B N   
6627  C CA  . LEU B 300 ? 0.2504 0.4910 0.6761 -0.0638 -0.0197 0.0079  300 LEU B CA  
6628  C C   . LEU B 300 ? 0.2544 0.4854 0.6737 -0.0790 -0.0203 0.0066  300 LEU B C   
6629  O O   . LEU B 300 ? 0.2411 0.4597 0.6506 -0.0829 -0.0261 0.0049  300 LEU B O   
6630  C CB  . LEU B 300 ? 0.2331 0.5015 0.6752 -0.0616 -0.0256 0.0084  300 LEU B CB  
6631  C CG  . LEU B 300 ? 0.2166 0.4855 0.6558 -0.0670 -0.0355 0.0070  300 LEU B CG  
6632  C CD1 . LEU B 300 ? 0.2138 0.4567 0.6348 -0.0613 -0.0384 0.0061  300 LEU B CD1 
6633  C CD2 . LEU B 300 ? 0.2042 0.5015 0.6598 -0.0625 -0.0416 0.0080  300 LEU B CD2 
6634  N N   . ASN B 301 ? 0.2666 0.5038 0.6913 -0.0875 -0.0143 0.0075  301 ASN B N   
6635  C CA  . ASN B 301 ? 0.2834 0.5120 0.7026 -0.1026 -0.0146 0.0065  301 ASN B CA  
6636  C C   . ASN B 301 ? 0.2915 0.4910 0.6932 -0.1045 -0.0093 0.0065  301 ASN B C   
6637  O O   . ASN B 301 ? 0.2907 0.4792 0.6857 -0.1162 -0.0086 0.0060  301 ASN B O   
6638  C CB  . ASN B 301 ? 0.2877 0.5387 0.7222 -0.1120 -0.0108 0.0078  301 ASN B CB  
6639  C CG  . ASN B 301 ? 0.3132 0.5924 0.7643 -0.1140 -0.0175 0.0074  301 ASN B CG  
6640  O OD1 . ASN B 301 ? 0.3408 0.6459 0.8088 -0.1098 -0.0152 0.0090  301 ASN B OD1 
6641  N ND2 . ASN B 301 ? 0.3482 0.6233 0.7945 -0.1197 -0.0261 0.0052  301 ASN B ND2 
6642  N N   . ASP B 302 ? 0.2705 0.4574 0.6646 -0.0932 -0.0057 0.0073  302 ASP B N   
6643  C CA  . ASP B 302 ? 0.2898 0.4514 0.6684 -0.0942 -0.0011 0.0076  302 ASP B CA  
6644  C C   . ASP B 302 ? 0.2985 0.4390 0.6626 -0.0933 -0.0063 0.0055  302 ASP B C   
6645  O O   . ASP B 302 ? 0.2836 0.4223 0.6455 -0.0845 -0.0101 0.0047  302 ASP B O   
6646  C CB  . ASP B 302 ? 0.2993 0.4597 0.6775 -0.0844 0.0057  0.0093  302 ASP B CB  
6647  C CG  . ASP B 302 ? 0.2878 0.4238 0.6506 -0.0838 0.0104  0.0101  302 ASP B CG  
6648  O OD1 . ASP B 302 ? 0.2962 0.4154 0.6484 -0.0910 0.0089  0.0094  302 ASP B OD1 
6649  O OD2 . ASP B 302 ? 0.2435 0.3776 0.6046 -0.0762 0.0154  0.0113  302 ASP B OD2 
6650  N N   . LYS B 303 ? 0.3160 0.4391 0.6692 -0.1025 -0.0062 0.0046  303 LYS B N   
6651  C CA  . LYS B 303 ? 0.3263 0.4290 0.6651 -0.1018 -0.0103 0.0024  303 LYS B CA  
6652  C C   . LYS B 303 ? 0.2800 0.3598 0.6050 -0.0967 -0.0055 0.0032  303 LYS B C   
6653  O O   . LYS B 303 ? 0.2522 0.3140 0.5647 -0.0953 -0.0076 0.0016  303 LYS B O   
6654  C CB  . LYS B 303 ? 0.4081 0.5051 0.7426 -0.1152 -0.0137 0.0003  303 LYS B CB  
6655  C CG  . LYS B 303 ? 0.4650 0.5841 0.8122 -0.1226 -0.0195 -0.0008 303 LYS B CG  
6656  C CD  . LYS B 303 ? 0.5288 0.6544 0.8769 -0.1176 -0.0275 -0.0027 303 LYS B CD  
6657  C CE  . LYS B 303 ? 0.5883 0.7395 0.9513 -0.1247 -0.0330 -0.0032 303 LYS B CE  
6658  N NZ  . LYS B 303 ? 0.6289 0.7878 0.9930 -0.1181 -0.0406 -0.0043 303 LYS B NZ  
6659  N N   . TYR B 304 ? 0.2739 0.3549 0.6010 -0.0942 0.0010  0.0057  304 TYR B N   
6660  C CA  . TYR B 304 ? 0.2969 0.3570 0.6110 -0.0921 0.0056  0.0069  304 TYR B CA  
6661  C C   . TYR B 304 ? 0.2813 0.3425 0.5958 -0.0802 0.0083  0.0081  304 TYR B C   
6662  O O   . TYR B 304 ? 0.2890 0.3365 0.5942 -0.0738 0.0075  0.0075  304 TYR B O   
6663  C CB  . TYR B 304 ? 0.3140 0.3693 0.6259 -0.1014 0.0107  0.0088  304 TYR B CB  
6664  C CG  . TYR B 304 ? 0.3311 0.3808 0.6400 -0.1139 0.0078  0.0072  304 TYR B CG  
6665  C CD1 . TYR B 304 ? 0.3295 0.3562 0.6235 -0.1159 0.0057  0.0054  304 TYR B CD1 
6666  C CD2 . TYR B 304 ? 0.3486 0.4168 0.6695 -0.1235 0.0067  0.0071  304 TYR B CD2 
6667  C CE1 . TYR B 304 ? 0.3387 0.3588 0.6285 -0.1273 0.0027  0.0034  304 TYR B CE1 
6668  C CE2 . TYR B 304 ? 0.3638 0.4269 0.6816 -0.1358 0.0035  0.0053  304 TYR B CE2 
6669  C CZ  . TYR B 304 ? 0.3563 0.3943 0.6578 -0.1376 0.0014  0.0032  304 TYR B CZ  
6670  O OH  . TYR B 304 ? 0.3901 0.4214 0.6872 -0.1496 -0.0018 0.0010  304 TYR B OH  
6671  N N   . GLY B 305 ? 0.2552 0.3333 0.5805 -0.0776 0.0115  0.0095  305 GLY B N   
6672  C CA  . GLY B 305 ? 0.2407 0.3206 0.5665 -0.0671 0.0141  0.0103  305 GLY B CA  
6673  C C   . GLY B 305 ? 0.2447 0.3113 0.5611 -0.0659 0.0197  0.0121  305 GLY B C   
6674  O O   . GLY B 305 ? 0.2487 0.3038 0.5579 -0.0730 0.0214  0.0131  305 GLY B O   
6675  N N   . THR B 306 ? 0.2374 0.3045 0.5530 -0.0570 0.0220  0.0125  306 THR B N   
6676  C CA  . THR B 306 ? 0.2336 0.2893 0.5401 -0.0548 0.0266  0.0143  306 THR B CA  
6677  C C   . THR B 306 ? 0.2312 0.2792 0.5319 -0.0454 0.0252  0.0134  306 THR B C   
6678  O O   . THR B 306 ? 0.2201 0.2747 0.5257 -0.0401 0.0222  0.0118  306 THR B O   
6679  C CB  . THR B 306 ? 0.2312 0.2981 0.5430 -0.0559 0.0326  0.0160  306 THR B CB  
6680  O OG1 . THR B 306 ? 0.1943 0.2760 0.5150 -0.0487 0.0331  0.0149  306 THR B OG1 
6681  C CG2 . THR B 306 ? 0.2306 0.3045 0.5476 -0.0666 0.0345  0.0173  306 THR B CG2 
6682  N N   . PRO B 307 ? 0.2457 0.2796 0.5358 -0.0434 0.0270  0.0145  307 PRO B N   
6683  C CA  . PRO B 307 ? 0.2406 0.2676 0.5253 -0.0356 0.0256  0.0137  307 PRO B CA  
6684  C C   . PRO B 307 ? 0.2522 0.2871 0.5399 -0.0298 0.0281  0.0135  307 PRO B C   
6685  O O   . PRO B 307 ? 0.2730 0.3118 0.5609 -0.0310 0.0325  0.0148  307 PRO B O   
6686  C CB  . PRO B 307 ? 0.2475 0.2587 0.5208 -0.0363 0.0267  0.0153  307 PRO B CB  
6687  C CG  . PRO B 307 ? 0.2479 0.2581 0.5197 -0.0433 0.0307  0.0177  307 PRO B CG  
6688  C CD  . PRO B 307 ? 0.2552 0.2783 0.5374 -0.0489 0.0301  0.0168  307 PRO B CD  
6689  N N   . ARG B 308 ? 0.2454 0.2815 0.5343 -0.0236 0.0255  0.0118  308 ARG B N   
6690  C CA  . ARG B 308 ? 0.2538 0.2929 0.5426 -0.0175 0.0275  0.0111  308 ARG B CA  
6691  C C   . ARG B 308 ? 0.2351 0.2628 0.5136 -0.0153 0.0285  0.0117  308 ARG B C   
6692  O O   . ARG B 308 ? 0.2237 0.2417 0.4962 -0.0172 0.0269  0.0127  308 ARG B O   
6693  C CB  . ARG B 308 ? 0.2392 0.2819 0.5323 -0.0124 0.0240  0.0092  308 ARG B CB  
6694  C CG  . ARG B 308 ? 0.2399 0.2960 0.5437 -0.0133 0.0230  0.0089  308 ARG B CG  
6695  C CD  . ARG B 308 ? 0.2387 0.2958 0.5449 -0.0086 0.0185  0.0076  308 ARG B CD  
6696  N NE  . ARG B 308 ? 0.2283 0.3000 0.5452 -0.0080 0.0175  0.0075  308 ARG B NE  
6697  C CZ  . ARG B 308 ? 0.2392 0.3149 0.5601 -0.0071 0.0127  0.0072  308 ARG B CZ  
6698  N NH1 . ARG B 308 ? 0.2729 0.3382 0.5873 -0.0063 0.0090  0.0069  308 ARG B NH1 
6699  N NH2 . ARG B 308 ? 0.2328 0.3235 0.5641 -0.0064 0.0118  0.0073  308 ARG B NH2 
6700  N N   . PRO B 309 ? 0.2275 0.2562 0.5034 -0.0113 0.0309  0.0112  309 PRO B N   
6701  C CA  . PRO B 309 ? 0.2439 0.2635 0.5102 -0.0093 0.0313  0.0117  309 PRO B CA  
6702  C C   . PRO B 309 ? 0.2697 0.2808 0.5320 -0.0079 0.0271  0.0113  309 PRO B C   
6703  O O   . PRO B 309 ? 0.3057 0.3094 0.5612 -0.0084 0.0269  0.0128  309 PRO B O   
6704  C CB  . PRO B 309 ? 0.2408 0.2641 0.5065 -0.0048 0.0333  0.0099  309 PRO B CB  
6705  C CG  . PRO B 309 ? 0.2542 0.2889 0.5276 -0.0058 0.0369  0.0099  309 PRO B CG  
6706  C CD  . PRO B 309 ? 0.2391 0.2782 0.5206 -0.0084 0.0338  0.0100  309 PRO B CD  
6707  N N   . VAL B 310 ? 0.2516 0.2642 0.5180 -0.0060 0.0241  0.0097  310 VAL B N   
6708  C CA  . VAL B 310 ? 0.2637 0.2695 0.5269 -0.0049 0.0207  0.0094  310 VAL B CA  
6709  C C   . VAL B 310 ? 0.2647 0.2641 0.5245 -0.0079 0.0199  0.0110  310 VAL B C   
6710  O O   . VAL B 310 ? 0.2519 0.2453 0.5070 -0.0064 0.0186  0.0114  310 VAL B O   
6711  C CB  . VAL B 310 ? 0.2542 0.2627 0.5221 -0.0032 0.0179  0.0079  310 VAL B CB  
6712  C CG1 . VAL B 310 ? 0.2713 0.2859 0.5457 -0.0059 0.0173  0.0080  310 VAL B CG1 
6713  C CG2 . VAL B 310 ? 0.2481 0.2502 0.5125 -0.0024 0.0150  0.0077  310 VAL B CG2 
6714  N N   . TRP B 311 ? 0.2443 0.2452 0.5066 -0.0121 0.0209  0.0118  311 TRP B N   
6715  C CA  . TRP B 311 ? 0.2507 0.2437 0.5088 -0.0151 0.0205  0.0130  311 TRP B CA  
6716  C C   . TRP B 311 ? 0.2494 0.2348 0.4997 -0.0140 0.0220  0.0150  311 TRP B C   
6717  O O   . TRP B 311 ? 0.2541 0.2316 0.4997 -0.0129 0.0207  0.0155  311 TRP B O   
6718  C CB  . TRP B 311 ? 0.2666 0.2627 0.5281 -0.0209 0.0218  0.0136  311 TRP B CB  
6719  C CG  . TRP B 311 ? 0.2855 0.2715 0.5416 -0.0249 0.0217  0.0146  311 TRP B CG  
6720  C CD1 . TRP B 311 ? 0.2807 0.2600 0.5314 -0.0282 0.0244  0.0169  311 TRP B CD1 
6721  C CD2 . TRP B 311 ? 0.2940 0.2742 0.5484 -0.0261 0.0187  0.0133  311 TRP B CD2 
6722  N NE1 . TRP B 311 ? 0.2869 0.2563 0.5330 -0.0314 0.0234  0.0169  311 TRP B NE1 
6723  C CE2 . TRP B 311 ? 0.2883 0.2580 0.5363 -0.0301 0.0200  0.0145  311 TRP B CE2 
6724  C CE3 . TRP B 311 ? 0.2993 0.2813 0.5559 -0.0241 0.0154  0.0112  311 TRP B CE3 
6725  C CZ2 . TRP B 311 ? 0.2965 0.2575 0.5404 -0.0322 0.0181  0.0133  311 TRP B CZ2 
6726  C CZ3 . TRP B 311 ? 0.3141 0.2884 0.5666 -0.0262 0.0136  0.0102  311 TRP B CZ3 
6727  C CH2 . TRP B 311 ? 0.3172 0.2812 0.5636 -0.0303 0.0149  0.0109  311 TRP B CH2 
6728  N N   . PHE B 312 ? 0.2719 0.2599 0.5208 -0.0139 0.0248  0.0161  312 PHE B N   
6729  C CA  . PHE B 312 ? 0.2991 0.2808 0.5400 -0.0128 0.0263  0.0185  312 PHE B CA  
6730  C C   . PHE B 312 ? 0.3037 0.2844 0.5415 -0.0078 0.0241  0.0179  312 PHE B C   
6731  O O   . PHE B 312 ? 0.3148 0.2893 0.5467 -0.0060 0.0233  0.0196  312 PHE B O   
6732  C CB  . PHE B 312 ? 0.3033 0.2887 0.5432 -0.0149 0.0302  0.0198  312 PHE B CB  
6733  C CG  . PHE B 312 ? 0.3133 0.2999 0.5563 -0.0209 0.0325  0.0209  312 PHE B CG  
6734  C CD1 . PHE B 312 ? 0.3346 0.3111 0.5716 -0.0244 0.0334  0.0234  312 PHE B CD1 
6735  C CD2 . PHE B 312 ? 0.3208 0.3183 0.5726 -0.0231 0.0337  0.0194  312 PHE B CD2 
6736  C CE1 . PHE B 312 ? 0.3446 0.3216 0.5841 -0.0312 0.0353  0.0242  312 PHE B CE1 
6737  C CE2 . PHE B 312 ? 0.3452 0.3455 0.6007 -0.0295 0.0356  0.0204  312 PHE B CE2 
6738  C CZ  . PHE B 312 ? 0.3237 0.3134 0.5729 -0.0342 0.0364  0.0227  312 PHE B CZ  
6739  N N   . ALA B 313 ? 0.3033 0.2900 0.5448 -0.0057 0.0231  0.0155  313 ALA B N   
6740  C CA  . ALA B 313 ? 0.2929 0.2790 0.5317 -0.0022 0.0209  0.0147  313 ALA B CA  
6741  C C   . ALA B 313 ? 0.3002 0.2828 0.5394 -0.0011 0.0182  0.0148  313 ALA B C   
6742  O O   . ALA B 313 ? 0.3248 0.3051 0.5602 0.0012  0.0169  0.0159  313 ALA B O   
6743  C CB  . ALA B 313 ? 0.2837 0.2749 0.5256 -0.0007 0.0205  0.0121  313 ALA B CB  
6744  N N   . MET B 314 ? 0.2954 0.2782 0.5389 -0.0026 0.0175  0.0138  314 MET B N   
6745  C CA  . MET B 314 ? 0.3134 0.2928 0.5568 -0.0016 0.0155  0.0135  314 MET B CA  
6746  C C   . MET B 314 ? 0.3203 0.2924 0.5585 -0.0011 0.0161  0.0156  314 MET B C   
6747  O O   . MET B 314 ? 0.2822 0.2523 0.5183 0.0020  0.0150  0.0161  314 MET B O   
6748  C CB  . MET B 314 ? 0.3340 0.3145 0.5816 -0.0037 0.0147  0.0121  314 MET B CB  
6749  C CG  . MET B 314 ? 0.3397 0.3257 0.5916 -0.0027 0.0134  0.0102  314 MET B CG  
6750  S SD  . MET B 314 ? 0.3314 0.3163 0.5821 -0.0001 0.0114  0.0096  314 MET B SD  
6751  C CE  . MET B 314 ? 0.3353 0.3162 0.5855 -0.0011 0.0105  0.0094  314 MET B CE  
6752  N N   . ARG B 315 ? 0.3347 0.3027 0.5707 -0.0040 0.0180  0.0169  315 ARG B N   
6753  C CA  . ARG B 315 ? 0.3553 0.3141 0.5847 -0.0034 0.0189  0.0193  315 ARG B CA  
6754  C C   . ARG B 315 ? 0.3475 0.3060 0.5727 0.0010  0.0184  0.0212  315 ARG B C   
6755  O O   . ARG B 315 ? 0.3326 0.2868 0.5547 0.0045  0.0175  0.0222  315 ARG B O   
6756  C CB  . ARG B 315 ? 0.3461 0.3003 0.5728 -0.0080 0.0215  0.0209  315 ARG B CB  
6757  C CG  . ARG B 315 ? 0.3507 0.2926 0.5689 -0.0073 0.0225  0.0237  315 ARG B CG  
6758  C CD  . ARG B 315 ? 0.3481 0.2852 0.5630 -0.0127 0.0254  0.0257  315 ARG B CD  
6759  N NE  . ARG B 315 ? 0.3787 0.3216 0.5930 -0.0123 0.0271  0.0273  315 ARG B NE  
6760  C CZ  . ARG B 315 ? 0.3751 0.3190 0.5885 -0.0170 0.0303  0.0289  315 ARG B CZ  
6761  N NH1 . ARG B 315 ? 0.3800 0.3193 0.5934 -0.0230 0.0319  0.0293  315 ARG B NH1 
6762  N NH2 . ARG B 315 ? 0.3777 0.3272 0.5899 -0.0161 0.0320  0.0299  315 ARG B NH2 
6763  N N   . ASP B 316 ? 0.3356 0.2993 0.5605 0.0010  0.0190  0.0216  316 ASP B N   
6764  C CA  . ASP B 316 ? 0.3325 0.2964 0.5526 0.0045  0.0181  0.0235  316 ASP B CA  
6765  C C   . ASP B 316 ? 0.3063 0.2753 0.5294 0.0078  0.0152  0.0221  316 ASP B C   
6766  O O   . ASP B 316 ? 0.3083 0.2767 0.5285 0.0116  0.0137  0.0238  316 ASP B O   
6767  C CB  . ASP B 316 ? 0.3558 0.3231 0.5734 0.0032  0.0196  0.0238  316 ASP B CB  
6768  C CG  . ASP B 316 ? 0.3600 0.3229 0.5737 -0.0001 0.0231  0.0260  316 ASP B CG  
6769  O OD1 . ASP B 316 ? 0.3419 0.2974 0.5536 -0.0019 0.0242  0.0276  316 ASP B OD1 
6770  O OD2 . ASP B 316 ? 0.3812 0.3479 0.5933 -0.0013 0.0250  0.0259  316 ASP B OD2 
6771  N N   . TYR B 317 ? 0.2753 0.2494 0.5043 0.0066  0.0144  0.0192  317 TYR B N   
6772  C CA  . TYR B 317 ? 0.2708 0.2500 0.5028 0.0086  0.0119  0.0180  317 TYR B CA  
6773  C C   . TYR B 317 ? 0.2721 0.2486 0.5041 0.0114  0.0114  0.0189  317 TYR B C   
6774  O O   . TYR B 317 ? 0.2661 0.2468 0.4990 0.0143  0.0097  0.0194  317 TYR B O   
6775  C CB  . TYR B 317 ? 0.2567 0.2399 0.4938 0.0065  0.0115  0.0151  317 TYR B CB  
6776  C CG  . TYR B 317 ? 0.2291 0.2172 0.4688 0.0075  0.0093  0.0139  317 TYR B CG  
6777  C CD1 . TYR B 317 ? 0.2391 0.2312 0.4776 0.0073  0.0079  0.0132  317 TYR B CD1 
6778  C CD2 . TYR B 317 ? 0.2098 0.1984 0.4525 0.0079  0.0089  0.0134  317 TYR B CD2 
6779  C CE1 . TYR B 317 ? 0.2224 0.2194 0.4635 0.0071  0.0058  0.0122  317 TYR B CE1 
6780  C CE2 . TYR B 317 ? 0.2149 0.2087 0.4602 0.0081  0.0073  0.0127  317 TYR B CE2 
6781  C CZ  . TYR B 317 ? 0.2079 0.2060 0.4527 0.0073  0.0057  0.0121  317 TYR B CZ  
6782  O OH  . TYR B 317 ? 0.2065 0.2101 0.4540 0.0064  0.0041  0.0114  317 TYR B OH  
6783  N N   . MET B 318 ? 0.2958 0.2659 0.5270 0.0104  0.0128  0.0189  318 MET B N   
6784  C CA  . MET B 318 ? 0.3054 0.2720 0.5363 0.0129  0.0128  0.0189  318 MET B CA  
6785  C C   . MET B 318 ? 0.2883 0.2497 0.5140 0.0175  0.0131  0.0217  318 MET B C   
6786  O O   . MET B 318 ? 0.2696 0.2285 0.4947 0.0210  0.0133  0.0218  318 MET B O   
6787  C CB  . MET B 318 ? 0.3105 0.2708 0.5409 0.0099  0.0140  0.0175  318 MET B CB  
6788  C CG  . MET B 318 ? 0.2997 0.2651 0.5352 0.0073  0.0132  0.0149  318 MET B CG  
6789  S SD  . MET B 318 ? 0.3288 0.2878 0.5631 0.0040  0.0135  0.0132  318 MET B SD  
6790  C CE  . MET B 318 ? 0.3402 0.2956 0.5730 -0.0003 0.0148  0.0143  318 MET B CE  
6791  N N   . LYS B 319 ? 0.2974 0.2569 0.5188 0.0180  0.0132  0.0241  319 LYS B N   
6792  C CA  . LYS B 319 ? 0.3568 0.3093 0.5721 0.0227  0.0135  0.0272  319 LYS B CA  
6793  C C   . LYS B 319 ? 0.3721 0.3317 0.5901 0.0286  0.0115  0.0278  319 LYS B C   
6794  O O   . LYS B 319 ? 0.3712 0.3256 0.5863 0.0337  0.0120  0.0294  319 LYS B O   
6795  C CB  . LYS B 319 ? 0.4012 0.3498 0.6103 0.0221  0.0140  0.0301  319 LYS B CB  
6796  C CG  . LYS B 319 ? 0.4386 0.3796 0.6447 0.0163  0.0167  0.0302  319 LYS B CG  
6797  C CD  . LYS B 319 ? 0.5156 0.4515 0.7140 0.0160  0.0178  0.0337  319 LYS B CD  
6798  C CE  . LYS B 319 ? 0.5915 0.5242 0.7884 0.0095  0.0208  0.0339  319 LYS B CE  
6799  N NZ  . LYS B 319 ? 0.5863 0.5197 0.7776 0.0091  0.0218  0.0365  319 LYS B NZ  
6800  N N   . GLY B 320 ? 0.3312 0.3029 0.5549 0.0277  0.0094  0.0264  320 GLY B N   
6801  C CA  . GLY B 320 ? 0.3236 0.3051 0.5519 0.0318  0.0074  0.0267  320 GLY B CA  
6802  C C   . GLY B 320 ? 0.3058 0.2976 0.5412 0.0280  0.0063  0.0237  320 GLY B C   
6803  O O   . GLY B 320 ? 0.3148 0.3102 0.5508 0.0242  0.0051  0.0226  320 GLY B O   
6804  N N   . LEU B 321 ? 0.2862 0.2815 0.5262 0.0290  0.0070  0.0225  321 LEU B N   
6805  C CA  . LEU B 321 ? 0.2656 0.2685 0.5113 0.0251  0.0064  0.0200  321 LEU B CA  
6806  C C   . LEU B 321 ? 0.2860 0.3015 0.5370 0.0271  0.0045  0.0206  321 LEU B C   
6807  O O   . LEU B 321 ? 0.2840 0.3026 0.5363 0.0326  0.0049  0.0223  321 LEU B O   
6808  C CB  . LEU B 321 ? 0.2642 0.2626 0.5107 0.0241  0.0087  0.0184  321 LEU B CB  
6809  C CG  . LEU B 321 ? 0.2462 0.2342 0.4887 0.0211  0.0100  0.0174  321 LEU B CG  
6810  C CD1 . LEU B 321 ? 0.2662 0.2509 0.5089 0.0209  0.0117  0.0160  321 LEU B CD1 
6811  C CD2 . LEU B 321 ? 0.2267 0.2161 0.4702 0.0163  0.0091  0.0162  321 LEU B CD2 
6812  N N   . ILE B 322 ? 0.2814 0.3040 0.5356 0.0226  0.0026  0.0192  322 ILE B N   
6813  C CA  . ILE B 322 ? 0.2650 0.3006 0.5252 0.0222  0.0007  0.0191  322 ILE B CA  
6814  C C   . ILE B 322 ? 0.2500 0.2876 0.5144 0.0185  0.0024  0.0173  322 ILE B C   
6815  O O   . ILE B 322 ? 0.2320 0.2648 0.4950 0.0136  0.0027  0.0154  322 ILE B O   
6816  C CB  . ILE B 322 ? 0.2756 0.3163 0.5350 0.0189  -0.0027 0.0186  322 ILE B CB  
6817  C CG1 . ILE B 322 ? 0.2861 0.3223 0.5393 0.0219  -0.0040 0.0205  322 ILE B CG1 
6818  C CG2 . ILE B 322 ? 0.2633 0.3187 0.5294 0.0179  -0.0053 0.0187  322 ILE B CG2 
6819  C CD1 . ILE B 322 ? 0.2969 0.3345 0.5466 0.0179  -0.0067 0.0193  322 ILE B CD1 
6820  N N   . ILE B 323 ? 0.2539 0.2984 0.5229 0.0216  0.0039  0.0180  323 ILE B N   
6821  C CA  . ILE B 323 ? 0.2411 0.2890 0.5138 0.0187  0.0060  0.0169  323 ILE B CA  
6822  C C   . ILE B 323 ? 0.2366 0.2989 0.5162 0.0153  0.0041  0.0169  323 ILE B C   
6823  O O   . ILE B 323 ? 0.2231 0.2871 0.5045 0.0094  0.0045  0.0156  323 ILE B O   
6824  C CB  . ILE B 323 ? 0.2395 0.2857 0.5122 0.0241  0.0094  0.0175  323 ILE B CB  
6825  C CG1 . ILE B 323 ? 0.2581 0.2891 0.5237 0.0251  0.0112  0.0167  323 ILE B CG1 
6826  C CG2 . ILE B 323 ? 0.2367 0.2899 0.5139 0.0218  0.0118  0.0168  323 ILE B CG2 
6827  C CD1 . ILE B 323 ? 0.2760 0.2992 0.5366 0.0289  0.0104  0.0180  323 ILE B CD1 
6828  N N   . SER B 324 ? 0.2302 0.3033 0.5137 0.0190  0.0021  0.0185  324 SER B N   
6829  C CA  . SER B 324 ? 0.2537 0.3417 0.5440 0.0150  -0.0004 0.0185  324 SER B CA  
6830  C C   . SER B 324 ? 0.2642 0.3571 0.5537 0.0172  -0.0048 0.0196  324 SER B C   
6831  O O   . SER B 324 ? 0.2778 0.3668 0.5641 0.0242  -0.0047 0.0215  324 SER B O   
6832  C CB  . SER B 324 ? 0.2619 0.3639 0.5608 0.0171  0.0019  0.0195  324 SER B CB  
6833  O OG  . SER B 324 ? 0.2549 0.3510 0.5527 0.0166  0.0064  0.0188  324 SER B OG  
6834  N N   . PRO B 325 ? 0.2343 0.3342 0.5251 0.0112  -0.0086 0.0185  325 PRO B N   
6835  C CA  . PRO B 325 ? 0.2282 0.3288 0.5205 0.0023  -0.0087 0.0162  325 PRO B CA  
6836  C C   . PRO B 325 ? 0.2338 0.3171 0.5181 -0.0013 -0.0072 0.0141  325 PRO B C   
6837  O O   . PRO B 325 ? 0.2204 0.2935 0.4983 0.0018  -0.0072 0.0141  325 PRO B O   
6838  C CB  . PRO B 325 ? 0.2367 0.3479 0.5308 -0.0020 -0.0138 0.0156  325 PRO B CB  
6839  C CG  . PRO B 325 ? 0.2364 0.3445 0.5251 0.0038  -0.0164 0.0169  325 PRO B CG  
6840  C CD  . PRO B 325 ? 0.2378 0.3444 0.5276 0.0129  -0.0134 0.0196  325 PRO B CD  
6841  N N   . LYS B 326 ? 0.2317 0.3128 0.5165 -0.0079 -0.0061 0.0124  326 LYS B N   
6842  C CA  . LYS B 326 ? 0.2367 0.3025 0.5148 -0.0108 -0.0046 0.0106  326 LYS B CA  
6843  C C   . LYS B 326 ? 0.2525 0.3131 0.5256 -0.0163 -0.0075 0.0082  326 LYS B C   
6844  O O   . LYS B 326 ? 0.2397 0.3078 0.5147 -0.0216 -0.0103 0.0073  326 LYS B O   
6845  C CB  . LYS B 326 ? 0.2339 0.2993 0.5147 -0.0138 -0.0015 0.0108  326 LYS B CB  
6846  C CG  . LYS B 326 ? 0.2351 0.3016 0.5181 -0.0081 0.0020  0.0125  326 LYS B CG  
6847  C CD  . LYS B 326 ? 0.2337 0.3026 0.5194 -0.0107 0.0053  0.0129  326 LYS B CD  
6848  C CE  . LYS B 326 ? 0.2452 0.3105 0.5297 -0.0048 0.0088  0.0138  326 LYS B CE  
6849  N NZ  . LYS B 326 ? 0.2325 0.3039 0.5197 0.0026  0.0091  0.0151  326 LYS B NZ  
6850  N N   . ASN B 327 ? 0.2312 0.2786 0.4975 -0.0155 -0.0067 0.0070  327 ASN B N   
6851  C CA  . ASN B 327 ? 0.2467 0.2873 0.5069 -0.0196 -0.0087 0.0044  327 ASN B CA  
6852  C C   . ASN B 327 ? 0.2317 0.2696 0.4919 -0.0267 -0.0086 0.0028  327 ASN B C   
6853  O O   . ASN B 327 ? 0.2178 0.2537 0.4801 -0.0273 -0.0060 0.0038  327 ASN B O   
6854  C CB  . ASN B 327 ? 0.2467 0.2757 0.5007 -0.0161 -0.0072 0.0037  327 ASN B CB  
6855  C CG  . ASN B 327 ? 0.2416 0.2636 0.4885 -0.0188 -0.0088 0.0008  327 ASN B CG  
6856  O OD1 . ASN B 327 ? 0.2330 0.2594 0.4775 -0.0200 -0.0117 0.0000  327 ASN B OD1 
6857  N ND2 . ASN B 327 ? 0.2672 0.2779 0.5099 -0.0190 -0.0068 -0.0007 327 ASN B ND2 
6858  N N   . LYS B 328 ? 0.2417 0.2792 0.4987 -0.0322 -0.0114 0.0005  328 LYS B N   
6859  C CA  . LYS B 328 ? 0.2936 0.3287 0.5501 -0.0401 -0.0118 -0.0010 328 LYS B CA  
6860  C C   . LYS B 328 ? 0.2949 0.3429 0.5602 -0.0431 -0.0110 0.0012  328 LYS B C   
6861  O O   . LYS B 328 ? 0.3160 0.3601 0.5813 -0.0481 -0.0093 0.0012  328 LYS B O   
6862  C CB  . LYS B 328 ? 0.2916 0.3099 0.5415 -0.0410 -0.0093 -0.0022 328 LYS B CB  
6863  C CG  . LYS B 328 ? 0.3135 0.3204 0.5556 -0.0371 -0.0094 -0.0042 328 LYS B CG  
6864  C CD  . LYS B 328 ? 0.3559 0.3639 0.5932 -0.0392 -0.0127 -0.0068 328 LYS B CD  
6865  C CE  . LYS B 328 ? 0.3737 0.3721 0.6034 -0.0349 -0.0120 -0.0087 328 LYS B CE  
6866  N NZ  . LYS B 328 ? 0.3877 0.3706 0.6105 -0.0359 -0.0103 -0.0111 328 LYS B NZ  
6867  N N   . SER B 329 ? 0.2913 0.3547 0.5639 -0.0399 -0.0122 0.0030  329 SER B N   
6868  C CA  . SER B 329 ? 0.2824 0.3605 0.5643 -0.0422 -0.0112 0.0050  329 SER B CA  
6869  C C   . SER B 329 ? 0.2765 0.3665 0.5619 -0.0496 -0.0153 0.0038  329 SER B C   
6870  O O   . SER B 329 ? 0.2737 0.3640 0.5554 -0.0502 -0.0194 0.0021  329 SER B O   
6871  C CB  . SER B 329 ? 0.2822 0.3709 0.5706 -0.0339 -0.0097 0.0078  329 SER B CB  
6872  O OG  . SER B 329 ? 0.2507 0.3455 0.5392 -0.0292 -0.0130 0.0081  329 SER B OG  
6873  N N   . ILE B 330 ? 0.2981 0.3979 0.5904 -0.0555 -0.0141 0.0047  330 ILE B N   
6874  C CA  . ILE B 330 ? 0.3310 0.4429 0.6276 -0.0644 -0.0178 0.0035  330 ILE B CA  
6875  C C   . ILE B 330 ? 0.3085 0.4446 0.6184 -0.0623 -0.0179 0.0062  330 ILE B C   
6876  O O   . ILE B 330 ? 0.2925 0.4338 0.6080 -0.0590 -0.0134 0.0086  330 ILE B O   
6877  C CB  . ILE B 330 ? 0.3503 0.4516 0.6425 -0.0749 -0.0163 0.0021  330 ILE B CB  
6878  C CG1 . ILE B 330 ? 0.3872 0.4644 0.6660 -0.0749 -0.0164 -0.0006 330 ILE B CG1 
6879  C CG2 . ILE B 330 ? 0.3627 0.4770 0.6599 -0.0856 -0.0200 0.0009  330 ILE B CG2 
6880  C CD1 . ILE B 330 ? 0.4125 0.4752 0.6844 -0.0843 -0.0154 -0.0022 330 ILE B CD1 
6881  N N   . HIS B 331 ? 0.3221 0.4730 0.6364 -0.0630 -0.0231 0.0059  331 HIS B N   
6882  C CA  . HIS B 331 ? 0.3136 0.4884 0.6407 -0.0584 -0.0238 0.0086  331 HIS B CA  
6883  C C   . HIS B 331 ? 0.3136 0.5065 0.6479 -0.0680 -0.0287 0.0077  331 HIS B C   
6884  O O   . HIS B 331 ? 0.3327 0.5216 0.6607 -0.0730 -0.0339 0.0050  331 HIS B O   
6885  C CB  . HIS B 331 ? 0.2937 0.4703 0.6195 -0.0468 -0.0258 0.0101  331 HIS B CB  
6886  C CG  . HIS B 331 ? 0.2988 0.4601 0.6191 -0.0381 -0.0209 0.0112  331 HIS B CG  
6887  N ND1 . HIS B 331 ? 0.2959 0.4637 0.6227 -0.0310 -0.0165 0.0139  331 HIS B ND1 
6888  C CD2 . HIS B 331 ? 0.2788 0.4191 0.5880 -0.0360 -0.0196 0.0099  331 HIS B CD2 
6889  C CE1 . HIS B 331 ? 0.3031 0.4534 0.6221 -0.0251 -0.0131 0.0140  331 HIS B CE1 
6890  N NE2 . HIS B 331 ? 0.2895 0.4240 0.5986 -0.0282 -0.0150 0.0117  331 HIS B NE2 
6891  N N   . THR B 332 ? 0.3176 0.5308 0.6649 -0.0702 -0.0267 0.0098  332 THR B N   
6892  C CA  . THR B 332 ? 0.3252 0.5595 0.6820 -0.0798 -0.0309 0.0093  332 THR B CA  
6893  C C   . THR B 332 ? 0.3236 0.5856 0.6948 -0.0719 -0.0324 0.0124  332 THR B C   
6894  O O   . THR B 332 ? 0.3893 0.6742 0.7734 -0.0774 -0.0329 0.0134  332 THR B O   
6895  C CB  . THR B 332 ? 0.3119 0.5461 0.6715 -0.0919 -0.0271 0.0089  332 THR B CB  
6896  O OG1 . THR B 332 ? 0.3290 0.5699 0.6959 -0.0858 -0.0203 0.0120  332 THR B OG1 
6897  C CG2 . THR B 332 ? 0.3105 0.5159 0.6553 -0.0984 -0.0253 0.0063  332 THR B CG2 
6898  N N   . ASN B 333 ? 0.3554 0.6152 0.7238 -0.0593 -0.0338 0.0138  333 ASN B N   
6899  C CA  . ASN B 333 ? 0.3628 0.6447 0.7425 -0.0490 -0.0350 0.0170  333 ASN B CA  
6900  C C   . ASN B 333 ? 0.3453 0.6210 0.7171 -0.0404 -0.0402 0.0173  333 ASN B C   
6901  O O   . ASN B 333 ? 0.3995 0.6512 0.7575 -0.0390 -0.0396 0.0158  333 ASN B O   
6902  C CB  . ASN B 333 ? 0.3906 0.6717 0.7744 -0.0398 -0.0272 0.0195  333 ASN B CB  
6903  C CG  . ASN B 333 ? 0.4541 0.7621 0.8526 -0.0312 -0.0273 0.0228  333 ASN B CG  
6904  O OD1 . ASN B 333 ? 0.5260 0.8401 0.9250 -0.0218 -0.0315 0.0244  333 ASN B OD1 
6905  N ND2 . ASN B 333 ? 0.5246 0.8500 0.9352 -0.0345 -0.0229 0.0238  333 ASN B ND2 
6906  N N   . THR B 334 ? 0.3042 0.6014 0.6844 -0.0344 -0.0451 0.0196  334 THR B N   
6907  C CA  . THR B 334 ? 0.2944 0.5867 0.6669 -0.0255 -0.0499 0.0208  334 THR B CA  
6908  C C   . THR B 334 ? 0.2961 0.5770 0.6648 -0.0112 -0.0450 0.0236  334 THR B C   
6909  O O   . THR B 334 ? 0.2542 0.5249 0.6137 -0.0040 -0.0476 0.0246  334 THR B O   
6910  C CB  . THR B 334 ? 0.3005 0.6195 0.6825 -0.0238 -0.0575 0.0226  334 THR B CB  
6911  O OG1 . THR B 334 ? 0.2876 0.6280 0.6852 -0.0171 -0.0542 0.0257  334 THR B OG1 
6912  C CG2 . THR B 334 ? 0.3146 0.6438 0.6985 -0.0385 -0.0637 0.0194  334 THR B CG2 
6913  N N   . LYS B 335 ? 0.3276 0.6091 0.7023 -0.0076 -0.0379 0.0247  335 LYS B N   
6914  C CA  . LYS B 335 ? 0.3410 0.6122 0.7125 0.0053  -0.0330 0.0271  335 LYS B CA  
6915  C C   . LYS B 335 ? 0.3319 0.5781 0.6935 0.0029  -0.0269 0.0251  335 LYS B C   
6916  O O   . LYS B 335 ? 0.4126 0.6591 0.7777 -0.0039 -0.0227 0.0238  335 LYS B O   
6917  C CB  . LYS B 335 ? 0.3815 0.6729 0.7670 0.0127  -0.0291 0.0297  335 LYS B CB  
6918  C CG  . LYS B 335 ? 0.4476 0.7661 0.8446 0.0183  -0.0347 0.0325  335 LYS B CG  
6919  C CD  . LYS B 335 ? 0.5112 0.8244 0.9007 0.0287  -0.0398 0.0348  335 LYS B CD  
6920  C CE  . LYS B 335 ? 0.5249 0.8668 0.9271 0.0361  -0.0449 0.0381  335 LYS B CE  
6921  N NZ  . LYS B 335 ? 0.5122 0.8492 0.9060 0.0442  -0.0511 0.0405  335 LYS B NZ  
6922  N N   . ILE B 336 ? 0.3207 0.5461 0.6700 0.0082  -0.0266 0.0251  336 ILE B N   
6923  C CA  . ILE B 336 ? 0.3243 0.5257 0.6633 0.0057  -0.0221 0.0231  336 ILE B CA  
6924  C C   . ILE B 336 ? 0.2791 0.4711 0.6155 0.0167  -0.0171 0.0250  336 ILE B C   
6925  O O   . ILE B 336 ? 0.2588 0.4464 0.5906 0.0252  -0.0188 0.0270  336 ILE B O   
6926  C CB  . ILE B 336 ? 0.3624 0.5475 0.6891 0.0017  -0.0257 0.0211  336 ILE B CB  
6927  C CG1 . ILE B 336 ? 0.4317 0.6259 0.7596 -0.0084 -0.0314 0.0190  336 ILE B CG1 
6928  C CG2 . ILE B 336 ? 0.3464 0.5084 0.6634 -0.0009 -0.0215 0.0191  336 ILE B CG2 
6929  C CD1 . ILE B 336 ? 0.4606 0.6618 0.7952 -0.0189 -0.0298 0.0171  336 ILE B CD1 
6930  N N   . PRO B 337 ? 0.2560 0.4435 0.5939 0.0170  -0.0110 0.0246  337 PRO B N   
6931  C CA  . PRO B 337 ? 0.2672 0.4419 0.5999 0.0263  -0.0064 0.0257  337 PRO B CA  
6932  C C   . PRO B 337 ? 0.2829 0.4362 0.6030 0.0277  -0.0076 0.0251  337 PRO B C   
6933  O O   . PRO B 337 ? 0.2582 0.4021 0.5726 0.0202  -0.0093 0.0231  337 PRO B O   
6934  C CB  . PRO B 337 ? 0.2463 0.4181 0.5807 0.0231  -0.0004 0.0244  337 PRO B CB  
6935  C CG  . PRO B 337 ? 0.2455 0.4369 0.5905 0.0151  -0.0013 0.0241  337 PRO B CG  
6936  C CD  . PRO B 337 ? 0.2502 0.4443 0.5940 0.0085  -0.0080 0.0233  337 PRO B CD  
6937  N N   . LEU B 338 ? 0.3070 0.4538 0.6230 0.0376  -0.0068 0.0272  338 LEU B N   
6938  C CA  . LEU B 338 ? 0.3035 0.4301 0.6078 0.0395  -0.0068 0.0271  338 LEU B CA  
6939  C C   . LEU B 338 ? 0.2760 0.3892 0.5760 0.0448  -0.0014 0.0271  338 LEU B C   
6940  O O   . LEU B 338 ? 0.2599 0.3784 0.5635 0.0523  0.0011  0.0285  338 LEU B O   
6941  C CB  . LEU B 338 ? 0.3234 0.4517 0.6245 0.0454  -0.0111 0.0298  338 LEU B CB  
6942  C CG  . LEU B 338 ? 0.3859 0.4941 0.6747 0.0466  -0.0110 0.0301  338 LEU B CG  
6943  C CD1 . LEU B 338 ? 0.3801 0.4820 0.6643 0.0372  -0.0127 0.0275  338 LEU B CD1 
6944  C CD2 . LEU B 338 ? 0.3961 0.5032 0.6801 0.0547  -0.0139 0.0337  338 LEU B CD2 
6945  N N   . GLU B 339 ? 0.2604 0.3568 0.5527 0.0404  0.0004  0.0252  339 GLU B N   
6946  C CA  . GLU B 339 ? 0.2571 0.3391 0.5437 0.0439  0.0048  0.0247  339 GLU B CA  
6947  C C   . GLU B 339 ? 0.2556 0.3203 0.5325 0.0424  0.0041  0.0244  339 GLU B C   
6948  O O   . GLU B 339 ? 0.2473 0.3084 0.5223 0.0354  0.0028  0.0227  339 GLU B O   
6949  C CB  . GLU B 339 ? 0.2631 0.3453 0.5521 0.0392  0.0084  0.0226  339 GLU B CB  
6950  C CG  . GLU B 339 ? 0.2679 0.3668 0.5662 0.0416  0.0104  0.0232  339 GLU B CG  
6951  C CD  . GLU B 339 ? 0.2709 0.3684 0.5698 0.0377  0.0147  0.0215  339 GLU B CD  
6952  O OE1 . GLU B 339 ? 0.3244 0.4230 0.6244 0.0293  0.0136  0.0203  339 GLU B OE1 
6953  O OE2 . GLU B 339 ? 0.2743 0.3689 0.5718 0.0429  0.0190  0.0213  339 GLU B OE2 
6954  N N   . LEU B 340 ? 0.2717 0.3262 0.5425 0.0490  0.0051  0.0261  340 LEU B N   
6955  C CA  . LEU B 340 ? 0.2806 0.3188 0.5423 0.0473  0.0052  0.0260  340 LEU B CA  
6956  C C   . LEU B 340 ? 0.2749 0.2984 0.5307 0.0498  0.0090  0.0254  340 LEU B C   
6957  O O   . LEU B 340 ? 0.3051 0.3292 0.5619 0.0556  0.0114  0.0256  340 LEU B O   
6958  C CB  . LEU B 340 ? 0.3058 0.3433 0.5636 0.0514  0.0023  0.0290  340 LEU B CB  
6959  C CG  . LEU B 340 ? 0.3030 0.3533 0.5643 0.0485  -0.0022 0.0295  340 LEU B CG  
6960  C CD1 . LEU B 340 ? 0.3074 0.3553 0.5631 0.0538  -0.0048 0.0328  340 LEU B CD1 
6961  C CD2 . LEU B 340 ? 0.2812 0.3291 0.5411 0.0398  -0.0031 0.0269  340 LEU B CD2 
6962  N N   . TYR B 341 ? 0.2693 0.2799 0.5190 0.0454  0.0096  0.0243  341 TYR B N   
6963  C CA  . TYR B 341 ? 0.2780 0.2738 0.5210 0.0471  0.0125  0.0237  341 TYR B CA  
6964  C C   . TYR B 341 ? 0.2846 0.2685 0.5202 0.0456  0.0119  0.0251  341 TYR B C   
6965  O O   . TYR B 341 ? 0.3092 0.2913 0.5442 0.0395  0.0112  0.0241  341 TYR B O   
6966  C CB  . TYR B 341 ? 0.2874 0.2800 0.5308 0.0423  0.0145  0.0207  341 TYR B CB  
6967  C CG  . TYR B 341 ? 0.3067 0.2849 0.5430 0.0443  0.0173  0.0197  341 TYR B CG  
6968  C CD1 . TYR B 341 ? 0.3171 0.2822 0.5469 0.0405  0.0173  0.0193  341 TYR B CD1 
6969  C CD2 . TYR B 341 ? 0.2986 0.2759 0.5341 0.0498  0.0199  0.0191  341 TYR B CD2 
6970  C CE1 . TYR B 341 ? 0.3383 0.2897 0.5610 0.0413  0.0195  0.0181  341 TYR B CE1 
6971  C CE2 . TYR B 341 ? 0.3316 0.2941 0.5591 0.0513  0.0223  0.0177  341 TYR B CE2 
6972  C CZ  . TYR B 341 ? 0.3633 0.3123 0.5841 0.0468  0.0219  0.0171  341 TYR B CZ  
6973  O OH  . TYR B 341 ? 0.3614 0.2951 0.5736 0.0470  0.0238  0.0154  341 TYR B OH  
6974  N N   . ASN B 342 ? 0.2978 0.2740 0.5279 0.0517  0.0124  0.0276  342 ASN B N   
6975  C CA  . ASN B 342 ? 0.3166 0.2833 0.5394 0.0512  0.0117  0.0300  342 ASN B CA  
6976  C C   . ASN B 342 ? 0.3491 0.2979 0.5638 0.0501  0.0145  0.0296  342 ASN B C   
6977  O O   . ASN B 342 ? 0.3683 0.3105 0.5806 0.0541  0.0165  0.0287  342 ASN B O   
6978  C CB  . ASN B 342 ? 0.3077 0.2774 0.5288 0.0587  0.0099  0.0339  342 ASN B CB  
6979  C CG  . ASN B 342 ? 0.3012 0.2888 0.5297 0.0584  0.0063  0.0343  342 ASN B CG  
6980  O OD1 . ASN B 342 ? 0.2726 0.2645 0.5023 0.0521  0.0047  0.0332  342 ASN B OD1 
6981  N ND2 . ASN B 342 ? 0.3121 0.3102 0.5452 0.0653  0.0050  0.0358  342 ASN B ND2 
6982  N N   . ASP B 343 ? 0.3689 0.3097 0.5788 0.0448  0.0146  0.0302  343 ASP B N   
6983  C CA  . ASP B 343 ? 0.4017 0.3251 0.6032 0.0430  0.0169  0.0304  343 ASP B CA  
6984  C C   . ASP B 343 ? 0.4382 0.3513 0.6313 0.0493  0.0172  0.0344  343 ASP B C   
6985  O O   . ASP B 343 ? 0.4502 0.3716 0.6450 0.0548  0.0152  0.0370  343 ASP B O   
6986  C CB  . ASP B 343 ? 0.4229 0.3443 0.6244 0.0340  0.0173  0.0290  343 ASP B CB  
6987  C CG  . ASP B 343 ? 0.4294 0.3488 0.6273 0.0311  0.0172  0.0317  343 ASP B CG  
6988  O OD1 . ASP B 343 ? 0.4175 0.3347 0.6106 0.0361  0.0165  0.0353  343 ASP B OD1 
6989  O OD2 . ASP B 343 ? 0.4135 0.3334 0.6128 0.0240  0.0180  0.0304  343 ASP B OD2 
6990  N N   . LYS B 344 ? 0.4823 0.3773 0.6660 0.0483  0.0194  0.0352  344 LYS B N   
6991  C CA  . LYS B 344 ? 0.5306 0.4128 0.7050 0.0555  0.0200  0.0391  344 LYS B CA  
6992  C C   . LYS B 344 ? 0.4642 0.3460 0.6343 0.0550  0.0187  0.0435  344 LYS B C   
6993  O O   . LYS B 344 ? 0.4404 0.3155 0.6038 0.0621  0.0183  0.0475  344 LYS B O   
6994  C CB  . LYS B 344 ? 0.6556 0.5161 0.8198 0.0544  0.0229  0.0384  344 LYS B CB  
6995  C CG  . LYS B 344 ? 0.7812 0.6321 0.9410 0.0440  0.0242  0.0379  344 LYS B CG  
6996  C CD  . LYS B 344 ? 0.9643 0.7926 1.1131 0.0420  0.0267  0.0371  344 LYS B CD  
6997  C CE  . LYS B 344 ? 1.0034 0.8236 1.1484 0.0310  0.0279  0.0372  344 LYS B CE  
6998  N NZ  . LYS B 344 ? 0.9571 0.7936 1.1128 0.0230  0.0268  0.0344  344 LYS B NZ  
6999  N N   . ASP B 345 ? 0.4281 0.3179 0.6018 0.0475  0.0181  0.0428  345 ASP B N   
7000  C CA  . ASP B 345 ? 0.4080 0.2981 0.5770 0.0469  0.0172  0.0467  345 ASP B CA  
7001  C C   . ASP B 345 ? 0.3871 0.2928 0.5608 0.0523  0.0137  0.0481  345 ASP B C   
7002  O O   . ASP B 345 ? 0.4052 0.3101 0.5731 0.0538  0.0125  0.0518  345 ASP B O   
7003  C CB  . ASP B 345 ? 0.4219 0.3149 0.5927 0.0372  0.0184  0.0452  345 ASP B CB  
7004  C CG  . ASP B 345 ? 0.4324 0.3104 0.5976 0.0306  0.0217  0.0449  345 ASP B CG  
7005  O OD1 . ASP B 345 ? 0.4130 0.2744 0.5691 0.0333  0.0231  0.0470  345 ASP B OD1 
7006  O OD2 . ASP B 345 ? 0.4216 0.3049 0.5915 0.0228  0.0227  0.0425  345 ASP B OD2 
7007  N N   . VAL B 346 ? 0.3686 0.2890 0.5524 0.0542  0.0119  0.0452  346 VAL B N   
7008  C CA  . VAL B 346 ? 0.3500 0.2864 0.5389 0.0583  0.0081  0.0463  346 VAL B CA  
7009  C C   . VAL B 346 ? 0.3476 0.2826 0.5335 0.0688  0.0067  0.0500  346 VAL B C   
7010  O O   . VAL B 346 ? 0.3384 0.2715 0.5266 0.0737  0.0080  0.0490  346 VAL B O   
7011  C CB  . VAL B 346 ? 0.3340 0.2861 0.5347 0.0561  0.0070  0.0421  346 VAL B CB  
7012  C CG1 . VAL B 346 ? 0.3446 0.3136 0.5510 0.0596  0.0030  0.0430  346 VAL B CG1 
7013  C CG2 . VAL B 346 ? 0.3556 0.3098 0.5596 0.0469  0.0081  0.0386  346 VAL B CG2 
7014  N N   . LYS B 347 ? 0.3651 0.3030 0.5465 0.0724  0.0038  0.0540  347 LYS B N   
7015  C CA  . LYS B 347 ? 0.4158 0.3542 0.5943 0.0832  0.0015  0.0582  347 LYS B CA  
7016  C C   . LYS B 347 ? 0.4126 0.3717 0.5981 0.0865  -0.0036 0.0591  347 LYS B C   
7017  O O   . LYS B 347 ? 0.3988 0.3627 0.5845 0.0960  -0.0061 0.0623  347 LYS B O   
7018  C CB  . LYS B 347 ? 0.4647 0.3857 0.6288 0.0859  0.0021  0.0635  347 LYS B CB  
7019  C CG  . LYS B 347 ? 0.4987 0.3978 0.6543 0.0820  0.0069  0.0633  347 LYS B CG  
7020  C CD  . LYS B 347 ? 0.5484 0.4394 0.7051 0.0869  0.0094  0.0614  347 LYS B CD  
7021  C CE  . LYS B 347 ? 0.6231 0.4931 0.7714 0.0807  0.0137  0.0605  347 LYS B CE  
7022  N NZ  . LYS B 347 ? 0.6886 0.5470 0.8347 0.0854  0.0162  0.0587  347 LYS B NZ  
7023  N N   . LYS B 348 ? 0.3815 0.3528 0.5725 0.0787  -0.0054 0.0561  348 LYS B N   
7024  C CA  . LYS B 348 ? 0.3777 0.3686 0.5754 0.0800  -0.0105 0.0561  348 LYS B CA  
7025  C C   . LYS B 348 ? 0.3554 0.3571 0.5611 0.0706  -0.0107 0.0509  348 LYS B C   
7026  O O   . LYS B 348 ? 0.3105 0.3048 0.5134 0.0632  -0.0082 0.0486  348 LYS B O   
7027  C CB  . LYS B 348 ? 0.3993 0.3891 0.5874 0.0828  -0.0141 0.0606  348 LYS B CB  
7028  C CG  . LYS B 348 ? 0.4262 0.4367 0.6205 0.0852  -0.0204 0.0611  348 LYS B CG  
7029  C CD  . LYS B 348 ? 0.4418 0.4524 0.6263 0.0896  -0.0248 0.0660  348 LYS B CD  
7030  C CE  . LYS B 348 ? 0.4684 0.4683 0.6419 0.0823  -0.0234 0.0658  348 LYS B CE  
7031  N NZ  . LYS B 348 ? 0.4964 0.4987 0.6601 0.0848  -0.0281 0.0697  348 LYS B NZ  
7032  N N   . VAL B 349 ? 0.3414 0.3612 0.5577 0.0713  -0.0138 0.0492  349 VAL B N   
7033  C CA  . VAL B 349 ? 0.3225 0.3528 0.5454 0.0629  -0.0149 0.0449  349 VAL B CA  
7034  C C   . VAL B 349 ? 0.3393 0.3859 0.5649 0.0633  -0.0208 0.0456  349 VAL B C   
7035  O O   . VAL B 349 ? 0.3060 0.3641 0.5367 0.0700  -0.0237 0.0480  349 VAL B O   
7036  C CB  . VAL B 349 ? 0.3125 0.3480 0.5455 0.0611  -0.0123 0.0415  349 VAL B CB  
7037  C CG1 . VAL B 349 ? 0.3007 0.3460 0.5399 0.0526  -0.0135 0.0374  349 VAL B CG1 
7038  C CG2 . VAL B 349 ? 0.3273 0.3460 0.5561 0.0604  -0.0070 0.0407  349 VAL B CG2 
7039  N N   . VAL B 350 ? 0.3321 0.3795 0.5539 0.0562  -0.0225 0.0435  350 VAL B N   
7040  C CA  . VAL B 350 ? 0.3199 0.3821 0.5435 0.0544  -0.0284 0.0430  350 VAL B CA  
7041  C C   . VAL B 350 ? 0.3078 0.3765 0.5374 0.0452  -0.0285 0.0377  350 VAL B C   
7042  O O   . VAL B 350 ? 0.2817 0.3400 0.5090 0.0400  -0.0246 0.0349  350 VAL B O   
7043  C CB  . VAL B 350 ? 0.3199 0.3752 0.5304 0.0551  -0.0306 0.0456  350 VAL B CB  
7044  C CG1 . VAL B 350 ? 0.3167 0.3858 0.5268 0.0523  -0.0371 0.0446  350 VAL B CG1 
7045  C CG2 . VAL B 350 ? 0.3400 0.3872 0.5435 0.0644  -0.0304 0.0515  350 VAL B CG2 
7046  N N   . VAL B 351 ? 0.2961 0.3821 0.5337 0.0434  -0.0331 0.0365  351 VAL B N   
7047  C CA  . VAL B 351 ? 0.2826 0.3741 0.5239 0.0342  -0.0342 0.0317  351 VAL B CA  
7048  C C   . VAL B 351 ? 0.3014 0.4016 0.5384 0.0312  -0.0405 0.0311  351 VAL B C   
7049  O O   . VAL B 351 ? 0.3450 0.4594 0.5860 0.0348  -0.0454 0.0335  351 VAL B O   
7050  C CB  . VAL B 351 ? 0.2744 0.3773 0.5288 0.0319  -0.0333 0.0299  351 VAL B CB  
7051  C CG1 . VAL B 351 ? 0.2722 0.3758 0.5283 0.0218  -0.0334 0.0250  351 VAL B CG1 
7052  C CG2 . VAL B 351 ? 0.2773 0.3726 0.5351 0.0358  -0.0275 0.0307  351 VAL B CG2 
7053  N N   . LYS B 352 ? 0.3019 0.3944 0.5312 0.0243  -0.0404 0.0276  352 LYS B N   
7054  C CA  . LYS B 352 ? 0.2933 0.3922 0.5170 0.0201  -0.0462 0.0259  352 LYS B CA  
7055  C C   . LYS B 352 ? 0.2641 0.3663 0.4912 0.0105  -0.0472 0.0204  352 LYS B C   
7056  O O   . LYS B 352 ? 0.2517 0.3461 0.4811 0.0066  -0.0428 0.0176  352 LYS B O   
7057  C CB  . LYS B 352 ? 0.3253 0.4105 0.5341 0.0207  -0.0451 0.0263  352 LYS B CB  
7058  C CG  . LYS B 352 ? 0.3696 0.4538 0.5719 0.0287  -0.0467 0.0319  352 LYS B CG  
7059  C CD  . LYS B 352 ? 0.4238 0.4914 0.6124 0.0296  -0.0430 0.0330  352 LYS B CD  
7060  C CE  . LYS B 352 ? 0.4580 0.5246 0.6398 0.0375  -0.0451 0.0391  352 LYS B CE  
7061  N NZ  . LYS B 352 ? 0.4778 0.5273 0.6487 0.0389  -0.0396 0.0412  352 LYS B NZ  
7062  N N   . PHE B 353 ? 0.2570 0.3701 0.4829 0.0066  -0.0535 0.0190  353 PHE B N   
7063  C CA  . PHE B 353 ? 0.2659 0.3803 0.4918 -0.0033 -0.0554 0.0136  353 PHE B CA  
7064  C C   . PHE B 353 ? 0.2720 0.3868 0.4859 -0.0057 -0.0610 0.0122  353 PHE B C   
7065  O O   . PHE B 353 ? 0.2682 0.3960 0.4830 -0.0024 -0.0668 0.0151  353 PHE B O   
7066  C CB  . PHE B 353 ? 0.2564 0.3874 0.4963 -0.0078 -0.0578 0.0127  353 PHE B CB  
7067  C CG  . PHE B 353 ? 0.2538 0.3833 0.4920 -0.0189 -0.0596 0.0072  353 PHE B CG  
7068  C CD1 . PHE B 353 ? 0.2584 0.3709 0.4914 -0.0231 -0.0546 0.0035  353 PHE B CD1 
7069  C CD2 . PHE B 353 ? 0.2601 0.4044 0.5009 -0.0250 -0.0665 0.0055  353 PHE B CD2 
7070  C CE1 . PHE B 353 ? 0.2579 0.3664 0.4875 -0.0328 -0.0561 -0.0015 353 PHE B CE1 
7071  C CE2 . PHE B 353 ? 0.2657 0.4062 0.5032 -0.0358 -0.0681 0.0002  353 PHE B CE2 
7072  C CZ  . PHE B 353 ? 0.2634 0.3849 0.4945 -0.0394 -0.0628 -0.0033 353 PHE B CZ  
7073  N N   . ARG B 354 ? 0.2679 0.3684 0.4705 -0.0105 -0.0591 0.0080  354 ARG B N   
7074  C CA  . ARG B 354 ? 0.2914 0.3895 0.4802 -0.0130 -0.0635 0.0059  354 ARG B CA  
7075  C C   . ARG B 354 ? 0.3028 0.4019 0.4845 -0.0047 -0.0651 0.0112  354 ARG B C   
7076  O O   . ARG B 354 ? 0.3085 0.4156 0.4841 -0.0048 -0.0717 0.0119  354 ARG B O   
7077  C CB  . ARG B 354 ? 0.3060 0.4170 0.4968 -0.0209 -0.0709 0.0026  354 ARG B CB  
7078  C CG  . ARG B 354 ? 0.3070 0.4123 0.5004 -0.0301 -0.0691 -0.0031 354 ARG B CG  
7079  C CD  . ARG B 354 ? 0.3167 0.4341 0.5114 -0.0390 -0.0765 -0.0065 354 ARG B CD  
7080  N NE  . ARG B 354 ? 0.3135 0.4247 0.5121 -0.0476 -0.0740 -0.0110 354 ARG B NE  
7081  C CZ  . ARG B 354 ? 0.2936 0.4163 0.4987 -0.0564 -0.0787 -0.0133 354 ARG B CZ  
7082  N NH1 . ARG B 354 ? 0.3051 0.4451 0.5119 -0.0583 -0.0866 -0.0125 354 ARG B NH1 
7083  N NH2 . ARG B 354 ? 0.2809 0.3980 0.4904 -0.0633 -0.0758 -0.0162 354 ARG B NH2 
7084  N N   . ASP B 355 ? 0.3129 0.4031 0.4948 0.0020  -0.0592 0.0149  355 ASP B N   
7085  C CA  . ASP B 355 ? 0.3411 0.4272 0.5138 0.0094  -0.0592 0.0200  355 ASP B CA  
7086  C C   . ASP B 355 ? 0.3340 0.4354 0.5132 0.0156  -0.0649 0.0252  355 ASP B C   
7087  O O   . ASP B 355 ? 0.3327 0.4322 0.5036 0.0219  -0.0665 0.0299  355 ASP B O   
7088  C CB  . ASP B 355 ? 0.3537 0.4315 0.5094 0.0069  -0.0604 0.0179  355 ASP B CB  
7089  C CG  . ASP B 355 ? 0.3548 0.4195 0.5049 0.0009  -0.0553 0.0121  355 ASP B CG  
7090  O OD1 . ASP B 355 ? 0.3394 0.3930 0.4893 0.0031  -0.0483 0.0128  355 ASP B OD1 
7091  O OD2 . ASP B 355 ? 0.3730 0.4392 0.5197 -0.0059 -0.0586 0.0068  355 ASP B OD2 
7092  N N   . LYS B 356 ? 0.3303 0.4463 0.5243 0.0144  -0.0673 0.0248  356 LYS B N   
7093  C CA  . LYS B 356 ? 0.3503 0.4824 0.5528 0.0213  -0.0719 0.0297  356 LYS B CA  
7094  C C   . LYS B 356 ? 0.3167 0.4486 0.5313 0.0268  -0.0664 0.0323  356 LYS B C   
7095  O O   . LYS B 356 ? 0.2909 0.4210 0.5135 0.0222  -0.0623 0.0290  356 LYS B O   
7096  C CB  . LYS B 356 ? 0.3743 0.5273 0.5848 0.0161  -0.0797 0.0276  356 LYS B CB  
7097  C CG  . LYS B 356 ? 0.3883 0.5609 0.6089 0.0235  -0.0849 0.0326  356 LYS B CG  
7098  C CD  . LYS B 356 ? 0.4503 0.6458 0.6823 0.0170  -0.0918 0.0302  356 LYS B CD  
7099  C CE  . LYS B 356 ? 0.5079 0.7068 0.7290 0.0105  -0.0993 0.0274  356 LYS B CE  
7100  N NZ  . LYS B 356 ? 0.5581 0.7823 0.7900 0.0061  -0.1076 0.0266  356 LYS B NZ  
7101  N N   . VAL B 357 ? 0.3061 0.4396 0.5210 0.0370  -0.0668 0.0381  357 VAL B N   
7102  C CA  . VAL B 357 ? 0.2875 0.4209 0.5125 0.0433  -0.0621 0.0407  357 VAL B CA  
7103  C C   . VAL B 357 ? 0.2699 0.4249 0.5113 0.0422  -0.0651 0.0398  357 VAL B C   
7104  O O   . VAL B 357 ? 0.2467 0.4190 0.4919 0.0443  -0.0719 0.0415  357 VAL B O   
7105  C CB  . VAL B 357 ? 0.2952 0.4221 0.5138 0.0547  -0.0618 0.0471  357 VAL B CB  
7106  C CG1 . VAL B 357 ? 0.2880 0.4178 0.5173 0.0626  -0.0584 0.0499  357 VAL B CG1 
7107  C CG2 . VAL B 357 ? 0.2965 0.4014 0.4998 0.0548  -0.0574 0.0482  357 VAL B CG2 
7108  N N   . ILE B 358 ? 0.2792 0.4333 0.5302 0.0391  -0.0599 0.0372  358 ILE B N   
7109  C CA  . ILE B 358 ? 0.2871 0.4604 0.5542 0.0385  -0.0608 0.0368  358 ILE B CA  
7110  C C   . ILE B 358 ? 0.2807 0.4511 0.5543 0.0470  -0.0551 0.0395  358 ILE B C   
7111  O O   . ILE B 358 ? 0.2820 0.4691 0.5686 0.0496  -0.0554 0.0404  358 ILE B O   
7112  C CB  . ILE B 358 ? 0.2797 0.4557 0.5520 0.0265  -0.0599 0.0312  358 ILE B CB  
7113  C CG1 . ILE B 358 ? 0.2978 0.4552 0.5673 0.0236  -0.0523 0.0288  358 ILE B CG1 
7114  C CG2 . ILE B 358 ? 0.2816 0.4589 0.5460 0.0182  -0.0657 0.0280  358 ILE B CG2 
7115  C CD1 . ILE B 358 ? 0.3116 0.4717 0.5877 0.0135  -0.0507 0.0243  358 ILE B CD1 
7116  N N   . TYR B 359 ? 0.2896 0.4392 0.5541 0.0508  -0.0497 0.0407  359 TYR B N   
7117  C CA  . TYR B 359 ? 0.3166 0.4610 0.5847 0.0592  -0.0447 0.0432  359 TYR B CA  
7118  C C   . TYR B 359 ? 0.3467 0.4699 0.6015 0.0650  -0.0418 0.0462  359 TYR B C   
7119  O O   . TYR B 359 ? 0.3185 0.4271 0.5631 0.0599  -0.0403 0.0446  359 TYR B O   
7120  C CB  . TYR B 359 ? 0.3150 0.4568 0.5904 0.0539  -0.0390 0.0396  359 TYR B CB  
7121  C CG  . TYR B 359 ? 0.3116 0.4464 0.5894 0.0618  -0.0333 0.0413  359 TYR B CG  
7122  C CD1 . TYR B 359 ? 0.2870 0.3996 0.5550 0.0634  -0.0284 0.0416  359 TYR B CD1 
7123  C CD2 . TYR B 359 ? 0.2831 0.4335 0.5725 0.0676  -0.0328 0.0427  359 TYR B CD2 
7124  C CE1 . TYR B 359 ? 0.2820 0.3872 0.5511 0.0701  -0.0236 0.0427  359 TYR B CE1 
7125  C CE2 . TYR B 359 ? 0.2708 0.4138 0.5611 0.0752  -0.0274 0.0439  359 TYR B CE2 
7126  C CZ  . TYR B 359 ? 0.2909 0.4104 0.5703 0.0762  -0.0230 0.0438  359 TYR B CZ  
7127  O OH  . TYR B 359 ? 0.3102 0.4214 0.5895 0.0830  -0.0180 0.0444  359 TYR B OH  
7128  N N   . SER B 360 ? 0.3571 0.4789 0.6121 0.0759  -0.0409 0.0505  360 SER B N   
7129  C CA  . SER B 360 ? 0.3636 0.4654 0.6058 0.0822  -0.0384 0.0541  360 SER B CA  
7130  C C   . SER B 360 ? 0.3726 0.4703 0.6179 0.0924  -0.0346 0.0567  360 SER B C   
7131  O O   . SER B 360 ? 0.4217 0.5333 0.6738 0.1008  -0.0374 0.0595  360 SER B O   
7132  C CB  . SER B 360 ? 0.3644 0.4674 0.5975 0.0856  -0.0440 0.0579  360 SER B CB  
7133  O OG  . SER B 360 ? 0.4139 0.4954 0.6333 0.0895  -0.0409 0.0611  360 SER B OG  
7134  N N   . LYS B 361 ? 0.3745 0.4536 0.6152 0.0917  -0.0284 0.0556  361 LYS B N   
7135  C CA  . LYS B 361 ? 0.4191 0.4906 0.6606 0.1004  -0.0241 0.0572  361 LYS B CA  
7136  C C   . LYS B 361 ? 0.3839 0.4291 0.6114 0.1014  -0.0200 0.0587  361 LYS B C   
7137  O O   . LYS B 361 ? 0.3463 0.3806 0.5690 0.0928  -0.0176 0.0562  361 LYS B O   
7138  C CB  . LYS B 361 ? 0.4481 0.5259 0.7004 0.0970  -0.0201 0.0529  361 LYS B CB  
7139  C CG  . LYS B 361 ? 0.4743 0.5450 0.7277 0.1054  -0.0151 0.0534  361 LYS B CG  
7140  C CD  . LYS B 361 ? 0.5385 0.6223 0.7979 0.1177  -0.0168 0.0570  361 LYS B CD  
7141  C CE  . LYS B 361 ? 0.5640 0.6360 0.8205 0.1281  -0.0118 0.0580  361 LYS B CE  
7142  N NZ  . LYS B 361 ? 0.5641 0.6369 0.8268 0.1236  -0.0066 0.0535  361 LYS B NZ  
7143  N N   . ASN B 362 ? 0.4010 0.4364 0.6219 0.1120  -0.0195 0.0632  362 ASN B N   
7144  C CA  . ASN B 362 ? 0.4024 0.4121 0.6111 0.1138  -0.0147 0.0646  362 ASN B CA  
7145  C C   . ASN B 362 ? 0.4050 0.4088 0.6181 0.1134  -0.0092 0.0609  362 ASN B C   
7146  O O   . ASN B 362 ? 0.3969 0.4120 0.6189 0.1199  -0.0088 0.0604  362 ASN B O   
7147  C CB  . ASN B 362 ? 0.4088 0.4092 0.6086 0.1258  -0.0159 0.0705  362 ASN B CB  
7148  C CG  . ASN B 362 ? 0.4310 0.4328 0.6228 0.1263  -0.0210 0.0748  362 ASN B CG  
7149  O OD1 . ASN B 362 ? 0.4561 0.4583 0.6448 0.1169  -0.0221 0.0733  362 ASN B OD1 
7150  N ND2 . ASN B 362 ? 0.4805 0.4829 0.6681 0.1377  -0.0242 0.0802  362 ASN B ND2 
7151  N N   . ILE B 363 ? 0.4064 0.3938 0.6138 0.1056  -0.0052 0.0582  363 ILE B N   
7152  C CA  . ILE B 363 ? 0.4138 0.3931 0.6230 0.1045  -0.0002 0.0547  363 ILE B CA  
7153  C C   . ILE B 363 ? 0.4747 0.4310 0.6720 0.1113  0.0031  0.0570  363 ILE B C   
7154  O O   . ILE B 363 ? 0.5038 0.4426 0.6898 0.1079  0.0040  0.0588  363 ILE B O   
7155  C CB  . ILE B 363 ? 0.3990 0.3746 0.6090 0.0923  0.0017  0.0503  363 ILE B CB  
7156  C CG1 . ILE B 363 ? 0.3732 0.3667 0.5912 0.0850  -0.0017 0.0484  363 ILE B CG1 
7157  C CG2 . ILE B 363 ? 0.3928 0.3634 0.6056 0.0908  0.0060  0.0464  363 ILE B CG2 
7158  C CD1 . ILE B 363 ? 0.3649 0.3798 0.5957 0.0869  -0.0035 0.0469  363 ILE B CD1 
7159  N N   . THR B 364 ? 0.5351 0.4909 0.7346 0.1203  0.0053  0.0568  364 THR B N   
7160  C CA  . THR B 364 ? 0.6233 0.5563 0.8112 0.1276  0.0088  0.0585  364 THR B CA  
7161  C C   . THR B 364 ? 0.6239 0.5449 0.8101 0.1234  0.0138  0.0535  364 THR B C   
7162  O O   . THR B 364 ? 0.6768 0.5764 0.8522 0.1271  0.0170  0.0537  364 THR B O   
7163  C CB  . THR B 364 ? 0.6490 0.5882 0.8388 0.1425  0.0078  0.0619  364 THR B CB  
7164  O OG1 . THR B 364 ? 0.6345 0.5951 0.8385 0.1447  0.0083  0.0589  364 THR B OG1 
7165  C CG2 . THR B 364 ? 0.6701 0.6182 0.8591 0.1475  0.0024  0.0674  364 THR B CG2 
7166  N N   . SER B 365 ? 0.6417 0.5759 0.8377 0.1156  0.0143  0.0491  365 SER B N   
7167  C CA  . SER B 365 ? 0.5605 0.4880 0.7565 0.1125  0.0184  0.0444  365 SER B CA  
7168  C C   . SER B 365 ? 0.4921 0.4261 0.6932 0.0996  0.0177  0.0409  365 SER B C   
7169  O O   . SER B 365 ? 0.4452 0.3981 0.6560 0.0962  0.0149  0.0408  365 SER B O   
7170  C CB  . SER B 365 ? 0.5695 0.5114 0.7743 0.1206  0.0199  0.0431  365 SER B CB  
7171  O OG  . SER B 365 ? 0.6024 0.5366 0.8054 0.1189  0.0241  0.0387  365 SER B OG  
7172  N N   . GLU B 366 ? 0.4639 0.3820 0.6581 0.0924  0.0200  0.0384  366 GLU B N   
7173  C CA  . GLU B 366 ? 0.4429 0.3668 0.6418 0.0811  0.0193  0.0354  366 GLU B CA  
7174  C C   . GLU B 366 ? 0.3910 0.3270 0.5985 0.0797  0.0206  0.0316  366 GLU B C   
7175  O O   . GLU B 366 ? 0.3903 0.3281 0.5989 0.0871  0.0226  0.0310  366 GLU B O   
7176  C CB  . GLU B 366 ? 0.4786 0.3831 0.6681 0.0741  0.0211  0.0341  366 GLU B CB  
7177  C CG  . GLU B 366 ? 0.5401 0.4310 0.7238 0.0760  0.0245  0.0311  366 GLU B CG  
7178  C CD  . GLU B 366 ? 0.6184 0.4906 0.7928 0.0682  0.0258  0.0295  366 GLU B CD  
7179  O OE1 . GLU B 366 ? 0.5757 0.4528 0.7541 0.0587  0.0249  0.0274  366 GLU B OE1 
7180  O OE2 . GLU B 366 ? 0.6523 0.5050 0.8156 0.0719  0.0277  0.0306  366 GLU B OE2 
7181  N N   . GLY B 367 ? 0.3406 0.2840 0.5533 0.0705  0.0196  0.0291  367 GLY B N   
7182  C CA  . GLY B 367 ? 0.3287 0.2819 0.5482 0.0678  0.0208  0.0258  367 GLY B CA  
7183  C C   . GLY B 367 ? 0.3156 0.2905 0.5464 0.0694  0.0190  0.0265  367 GLY B C   
7184  O O   . GLY B 367 ? 0.3101 0.2937 0.5444 0.0685  0.0159  0.0285  367 GLY B O   
7185  N N   . TYR B 368 ? 0.3054 0.2886 0.5412 0.0717  0.0212  0.0247  368 TYR B N   
7186  C CA  . TYR B 368 ? 0.3125 0.3165 0.5595 0.0711  0.0200  0.0250  368 TYR B CA  
7187  C C   . TYR B 368 ? 0.3251 0.3398 0.5763 0.0790  0.0180  0.0283  368 TYR B C   
7188  O O   . TYR B 368 ? 0.3074 0.3162 0.5548 0.0880  0.0197  0.0298  368 TYR B O   
7189  C CB  . TYR B 368 ? 0.3164 0.3263 0.5670 0.0719  0.0236  0.0226  368 TYR B CB  
7190  C CG  . TYR B 368 ? 0.3011 0.3327 0.5635 0.0698  0.0228  0.0228  368 TYR B CG  
7191  C CD1 . TYR B 368 ? 0.2819 0.3191 0.5480 0.0604  0.0211  0.0216  368 TYR B CD1 
7192  C CD2 . TYR B 368 ? 0.2857 0.3322 0.5555 0.0772  0.0238  0.0244  368 TYR B CD2 
7193  C CE1 . TYR B 368 ? 0.2928 0.3482 0.5688 0.0575  0.0205  0.0218  368 TYR B CE1 
7194  C CE2 . TYR B 368 ? 0.2729 0.3400 0.5538 0.0743  0.0231  0.0247  368 TYR B CE2 
7195  C CZ  . TYR B 368 ? 0.2875 0.3582 0.5711 0.0640  0.0214  0.0233  368 TYR B CZ  
7196  O OH  . TYR B 368 ? 0.2705 0.3599 0.5642 0.0600  0.0206  0.0236  368 TYR B OH  
7197  N N   . MET B 369 ? 0.3410 0.3713 0.5998 0.0758  0.0143  0.0295  369 MET B N   
7198  C CA  . MET B 369 ? 0.3615 0.4087 0.6278 0.0826  0.0124  0.0320  369 MET B CA  
7199  C C   . MET B 369 ? 0.3396 0.4071 0.6171 0.0762  0.0103  0.0311  369 MET B C   
7200  O O   . MET B 369 ? 0.3252 0.3913 0.6025 0.0668  0.0091  0.0292  369 MET B O   
7201  C CB  . MET B 369 ? 0.3921 0.4363 0.6540 0.0869  0.0086  0.0356  369 MET B CB  
7202  C CG  . MET B 369 ? 0.4488 0.4888 0.7070 0.0784  0.0054  0.0354  369 MET B CG  
7203  S SD  . MET B 369 ? 0.5670 0.6204 0.8277 0.0798  -0.0008 0.0386  369 MET B SD  
7204  C CE  . MET B 369 ? 0.4266 0.5060 0.7011 0.0853  -0.0025 0.0397  369 MET B CE  
7205  N N   . ALA B 370 ? 0.3169 0.4030 0.6040 0.0816  0.0100  0.0325  370 ALA B N   
7206  C CA  . ALA B 370 ? 0.2975 0.4048 0.5959 0.0758  0.0079  0.0319  370 ALA B CA  
7207  C C   . ALA B 370 ? 0.3046 0.4289 0.6096 0.0810  0.0033  0.0350  370 ALA B C   
7208  O O   . ALA B 370 ? 0.3237 0.4470 0.6270 0.0915  0.0032  0.0377  370 ALA B O   
7209  C CB  . ALA B 370 ? 0.2725 0.3894 0.5780 0.0756  0.0126  0.0303  370 ALA B CB  
7210  N N   . ASP B 371 ? 0.3068 0.4457 0.6184 0.0735  -0.0009 0.0346  371 ASP B N   
7211  C CA  . ASP B 371 ? 0.3040 0.4601 0.6217 0.0768  -0.0063 0.0373  371 ASP B CA  
7212  C C   . ASP B 371 ? 0.2792 0.4507 0.6048 0.0657  -0.0095 0.0354  371 ASP B C   
7213  O O   . ASP B 371 ? 0.2740 0.4435 0.6012 0.0580  -0.0063 0.0327  371 ASP B O   
7214  C CB  . ASP B 371 ? 0.3251 0.4680 0.6321 0.0807  -0.0099 0.0395  371 ASP B CB  
7215  C CG  . ASP B 371 ? 0.3110 0.4682 0.6218 0.0887  -0.0150 0.0434  371 ASP B CG  
7216  O OD1 . ASP B 371 ? 0.3041 0.4839 0.6273 0.0900  -0.0163 0.0438  371 ASP B OD1 
7217  O OD2 . ASP B 371 ? 0.3061 0.4518 0.6072 0.0936  -0.0174 0.0460  371 ASP B OD2 
7218  N N   . GLU B 372 ? 0.3080 0.4932 0.6372 0.0645  -0.0157 0.0367  372 GLU B N   
7219  C CA  . GLU B 372 ? 0.3395 0.5359 0.6737 0.0527  -0.0192 0.0345  372 GLU B CA  
7220  C C   . GLU B 372 ? 0.3338 0.5325 0.6635 0.0503  -0.0264 0.0352  372 GLU B C   
7221  O O   . GLU B 372 ? 0.3643 0.5691 0.6937 0.0585  -0.0300 0.0383  372 GLU B O   
7222  C CB  . GLU B 372 ? 0.3430 0.5638 0.6923 0.0505  -0.0183 0.0344  372 GLU B CB  
7223  C CG  . GLU B 372 ? 0.3654 0.6096 0.7248 0.0580  -0.0224 0.0375  372 GLU B CG  
7224  C CD  . GLU B 372 ? 0.3927 0.6636 0.7686 0.0555  -0.0212 0.0376  372 GLU B CD  
7225  O OE1 . GLU B 372 ? 0.3830 0.6547 0.7627 0.0481  -0.0164 0.0354  372 GLU B OE1 
7226  O OE2 . GLU B 372 ? 0.3909 0.6830 0.7759 0.0614  -0.0254 0.0402  372 GLU B OE2 
7227  N N   . LEU B 373 ? 0.3320 0.5249 0.6574 0.0392  -0.0283 0.0321  373 LEU B N   
7228  C CA  . LEU B 373 ? 0.3425 0.5383 0.6634 0.0346  -0.0350 0.0317  373 LEU B CA  
7229  C C   . LEU B 373 ? 0.3028 0.5231 0.6355 0.0286  -0.0394 0.0310  373 LEU B C   
7230  O O   . LEU B 373 ? 0.3061 0.5341 0.6471 0.0226  -0.0366 0.0293  373 LEU B O   
7231  C CB  . LEU B 373 ? 0.3655 0.5434 0.6758 0.0255  -0.0347 0.0282  373 LEU B CB  
7232  C CG  . LEU B 373 ? 0.3961 0.5504 0.6961 0.0283  -0.0297 0.0279  373 LEU B CG  
7233  C CD1 . LEU B 373 ? 0.4160 0.5574 0.7097 0.0187  -0.0287 0.0240  373 LEU B CD1 
7234  C CD2 . LEU B 373 ? 0.4593 0.6051 0.7503 0.0361  -0.0314 0.0309  373 LEU B CD2 
7235  N N   . THR B 374 ? 0.3033 0.5343 0.6354 0.0293  -0.0464 0.0322  374 THR B N   
7236  C CA  . THR B 374 ? 0.3128 0.5655 0.6537 0.0215  -0.0522 0.0310  374 THR B CA  
7237  C C   . THR B 374 ? 0.3375 0.5796 0.6672 0.0118  -0.0565 0.0277  374 THR B C   
7238  O O   . THR B 374 ? 0.3456 0.5766 0.6638 0.0157  -0.0591 0.0286  374 THR B O   
7239  C CB  . THR B 374 ? 0.3330 0.6071 0.6816 0.0307  -0.0574 0.0351  374 THR B CB  
7240  O OG1 . THR B 374 ? 0.3464 0.6259 0.7033 0.0409  -0.0521 0.0379  374 THR B OG1 
7241  C CG2 . THR B 374 ? 0.3353 0.6356 0.6950 0.0227  -0.0639 0.0341  374 THR B CG2 
7242  N N   . ILE B 375 ? 0.3449 0.5890 0.6770 -0.0007 -0.0568 0.0238  375 ILE B N   
7243  C CA  . ILE B 375 ? 0.3442 0.5806 0.6665 -0.0106 -0.0613 0.0200  375 ILE B CA  
7244  C C   . ILE B 375 ? 0.3519 0.6114 0.6833 -0.0193 -0.0679 0.0187  375 ILE B C   
7245  O O   . ILE B 375 ? 0.3446 0.6247 0.6910 -0.0196 -0.0674 0.0203  375 ILE B O   
7246  C CB  . ILE B 375 ? 0.3636 0.5789 0.6787 -0.0182 -0.0560 0.0163  375 ILE B CB  
7247  C CG1 . ILE B 375 ? 0.3454 0.5682 0.6713 -0.0251 -0.0522 0.0152  375 ILE B CG1 
7248  C CG2 . ILE B 375 ? 0.3821 0.5756 0.6881 -0.0103 -0.0503 0.0174  375 ILE B CG2 
7249  C CD1 . ILE B 375 ? 0.3550 0.5578 0.6731 -0.0337 -0.0483 0.0114  375 ILE B CD1 
7250  N N   . ASP B 376 ? 0.3600 0.6165 0.6823 -0.0266 -0.0740 0.0158  376 ASP B N   
7251  C CA  . ASP B 376 ? 0.3763 0.6523 0.7051 -0.0370 -0.0809 0.0137  376 ASP B CA  
7252  C C   . ASP B 376 ? 0.3578 0.6165 0.6745 -0.0497 -0.0819 0.0080  376 ASP B C   
7253  O O   . ASP B 376 ? 0.3989 0.6499 0.7031 -0.0517 -0.0867 0.0058  376 ASP B O   
7254  C CB  . ASP B 376 ? 0.3844 0.6784 0.7142 -0.0321 -0.0895 0.0161  376 ASP B CB  
7255  C CG  . ASP B 376 ? 0.4084 0.7299 0.7497 -0.0409 -0.0971 0.0151  376 ASP B CG  
7256  O OD1 . ASP B 376 ? 0.3978 0.7301 0.7507 -0.0499 -0.0950 0.0136  376 ASP B OD1 
7257  O OD2 . ASP B 376 ? 0.4484 0.7818 0.7873 -0.0391 -0.1053 0.0161  376 ASP B OD2 
7258  N N   . PRO B 377 ? 0.3163 0.5658 0.6346 -0.0578 -0.0766 0.0054  377 PRO B N   
7259  C CA  . PRO B 377 ? 0.3149 0.5445 0.6206 -0.0686 -0.0766 0.0001  377 PRO B CA  
7260  C C   . PRO B 377 ? 0.3230 0.5649 0.6315 -0.0826 -0.0828 -0.0034 377 PRO B C   
7261  O O   . PRO B 377 ? 0.3150 0.5798 0.6386 -0.0865 -0.0843 -0.0018 377 PRO B O   
7262  C CB  . PRO B 377 ? 0.3169 0.5331 0.6246 -0.0688 -0.0680 0.0002  377 PRO B CB  
7263  C CG  . PRO B 377 ? 0.3099 0.5488 0.6356 -0.0670 -0.0660 0.0038  377 PRO B CG  
7264  C CD  . PRO B 377 ? 0.3087 0.5661 0.6404 -0.0566 -0.0703 0.0076  377 PRO B CD  
7265  N N   . VAL B 378 ? 0.3442 0.5716 0.6379 -0.0897 -0.0866 -0.0081 378 VAL B N   
7266  C CA  . VAL B 378 ? 0.3801 0.6153 0.6732 -0.1040 -0.0930 -0.0123 378 VAL B CA  
7267  C C   . VAL B 378 ? 0.3813 0.5983 0.6699 -0.1149 -0.0883 -0.0161 378 VAL B C   
7268  O O   . VAL B 378 ? 0.3947 0.5857 0.6706 -0.1125 -0.0834 -0.0180 378 VAL B O   
7269  C CB  . VAL B 378 ? 0.4244 0.6535 0.7021 -0.1060 -0.1003 -0.0158 378 VAL B CB  
7270  C CG1 . VAL B 378 ? 0.4491 0.6914 0.7283 -0.1207 -0.1083 -0.0196 378 VAL B CG1 
7271  C CG2 . VAL B 378 ? 0.4300 0.6689 0.7070 -0.0931 -0.1038 -0.0116 378 VAL B CG2 
7272  N N   . GLY B 379 ? 0.3889 0.6201 0.6882 -0.1266 -0.0896 -0.0168 379 GLY B N   
7273  C CA  . GLY B 379 ? 0.3835 0.5997 0.6806 -0.1371 -0.0846 -0.0193 379 GLY B CA  
7274  C C   . GLY B 379 ? 0.3894 0.5887 0.6853 -0.1280 -0.0754 -0.0167 379 GLY B C   
7275  O O   . GLY B 379 ? 0.4278 0.6396 0.7351 -0.1185 -0.0719 -0.0120 379 GLY B O   
7276  N N   . ILE B 380 ? 0.3743 0.5449 0.6555 -0.1303 -0.0718 -0.0200 380 ILE B N   
7277  C CA  . ILE B 380 ? 0.3409 0.4937 0.6187 -0.1214 -0.0640 -0.0181 380 ILE B CA  
7278  C C   . ILE B 380 ? 0.3267 0.4640 0.5912 -0.1121 -0.0645 -0.0194 380 ILE B C   
7279  O O   . ILE B 380 ? 0.3700 0.4958 0.6217 -0.1169 -0.0682 -0.0239 380 ILE B O   
7280  C CB  . ILE B 380 ? 0.3561 0.4882 0.6272 -0.1299 -0.0595 -0.0204 380 ILE B CB  
7281  C CG1 . ILE B 380 ? 0.3715 0.5187 0.6548 -0.1414 -0.0589 -0.0191 380 ILE B CG1 
7282  C CG2 . ILE B 380 ? 0.3448 0.4587 0.6116 -0.1201 -0.0522 -0.0185 380 ILE B CG2 
7283  C CD1 . ILE B 380 ? 0.3647 0.4912 0.6391 -0.1534 -0.0564 -0.0220 380 ILE B CD1 
7284  N N   . GLU B 381 ? 0.2916 0.4292 0.5588 -0.0992 -0.0608 -0.0157 381 GLU B N   
7285  C CA  . GLU B 381 ? 0.2946 0.4229 0.5513 -0.0904 -0.0618 -0.0161 381 GLU B CA  
7286  C C   . GLU B 381 ? 0.2737 0.3869 0.5280 -0.0808 -0.0546 -0.0140 381 GLU B C   
7287  O O   . GLU B 381 ? 0.2631 0.3848 0.5276 -0.0743 -0.0512 -0.0099 381 GLU B O   
7288  C CB  . GLU B 381 ? 0.2935 0.4439 0.5571 -0.0849 -0.0672 -0.0131 381 GLU B CB  
7289  C CG  . GLU B 381 ? 0.3074 0.4500 0.5587 -0.0779 -0.0696 -0.0136 381 GLU B CG  
7290  C CD  . GLU B 381 ? 0.3276 0.4900 0.5839 -0.0712 -0.0749 -0.0100 381 GLU B CD  
7291  O OE1 . GLU B 381 ? 0.3359 0.5193 0.6013 -0.0758 -0.0806 -0.0094 381 GLU B OE1 
7292  O OE2 . GLU B 381 ? 0.3627 0.5197 0.6134 -0.0613 -0.0737 -0.0076 381 GLU B OE2 
7293  N N   . ASP B 382 ? 0.2695 0.3606 0.5104 -0.0799 -0.0523 -0.0171 382 ASP B N   
7294  C CA  . ASP B 382 ? 0.2537 0.3325 0.4917 -0.0702 -0.0466 -0.0152 382 ASP B CA  
7295  C C   . ASP B 382 ? 0.2431 0.3299 0.4812 -0.0608 -0.0482 -0.0123 382 ASP B C   
7296  O O   . ASP B 382 ? 0.2358 0.3267 0.4679 -0.0618 -0.0531 -0.0137 382 ASP B O   
7297  C CB  . ASP B 382 ? 0.2707 0.3262 0.4946 -0.0710 -0.0442 -0.0192 382 ASP B CB  
7298  C CG  . ASP B 382 ? 0.2816 0.3313 0.4928 -0.0749 -0.0487 -0.0237 382 ASP B CG  
7299  O OD1 . ASP B 382 ? 0.2697 0.3265 0.4810 -0.0839 -0.0537 -0.0260 382 ASP B OD1 
7300  O OD2 . ASP B 382 ? 0.2703 0.3083 0.4711 -0.0692 -0.0470 -0.0250 382 ASP B OD2 
7301  N N   . MET B 383 ? 0.2443 0.3315 0.4874 -0.0519 -0.0439 -0.0084 383 MET B N   
7302  C CA  . MET B 383 ? 0.2445 0.3375 0.4870 -0.0430 -0.0450 -0.0052 383 MET B CA  
7303  C C   . MET B 383 ? 0.2266 0.3071 0.4665 -0.0352 -0.0391 -0.0034 383 MET B C   
7304  O O   . MET B 383 ? 0.2178 0.2966 0.4642 -0.0336 -0.0349 -0.0019 383 MET B O   
7305  C CB  . MET B 383 ? 0.2487 0.3627 0.5039 -0.0397 -0.0473 -0.0011 383 MET B CB  
7306  C CG  . MET B 383 ? 0.2655 0.3968 0.5268 -0.0472 -0.0532 -0.0022 383 MET B CG  
7307  S SD  . MET B 383 ? 0.2718 0.4297 0.5496 -0.0417 -0.0552 0.0029  383 MET B SD  
7308  C CE  . MET B 383 ? 0.3013 0.4624 0.5736 -0.0306 -0.0586 0.0064  383 MET B CE  
7309  N N   . GLU B 384 ? 0.2359 0.3079 0.4660 -0.0309 -0.0388 -0.0035 384 GLU B N   
7310  C CA  . GLU B 384 ? 0.2257 0.2885 0.4541 -0.0236 -0.0338 -0.0013 384 GLU B CA  
7311  C C   . GLU B 384 ? 0.2234 0.2957 0.4555 -0.0162 -0.0349 0.0035  384 GLU B C   
7312  O O   . GLU B 384 ? 0.2264 0.3014 0.4523 -0.0140 -0.0382 0.0044  384 GLU B O   
7313  C CB  . GLU B 384 ? 0.2417 0.2901 0.4577 -0.0233 -0.0321 -0.0039 384 GLU B CB  
7314  C CG  . GLU B 384 ? 0.2439 0.2829 0.4589 -0.0172 -0.0265 -0.0020 384 GLU B CG  
7315  C CD  . GLU B 384 ? 0.2582 0.2851 0.4623 -0.0162 -0.0240 -0.0041 384 GLU B CD  
7316  O OE1 . GLU B 384 ? 0.2622 0.2882 0.4579 -0.0191 -0.0270 -0.0068 384 GLU B OE1 
7317  O OE2 . GLU B 384 ? 0.2782 0.2973 0.4823 -0.0128 -0.0190 -0.0034 384 GLU B OE2 
7318  N N   . LEU B 385 ? 0.2189 0.2959 0.4603 -0.0123 -0.0323 0.0064  385 LEU B N   
7319  C CA  . LEU B 385 ? 0.2231 0.3074 0.4677 -0.0046 -0.0328 0.0109  385 LEU B CA  
7320  C C   . LEU B 385 ? 0.2322 0.3028 0.4698 0.0007  -0.0287 0.0125  385 LEU B C   
7321  O O   . LEU B 385 ? 0.2183 0.2795 0.4566 0.0005  -0.0241 0.0117  385 LEU B O   
7322  C CB  . LEU B 385 ? 0.2122 0.3063 0.4687 -0.0022 -0.0313 0.0131  385 LEU B CB  
7323  C CG  . LEU B 385 ? 0.2171 0.3250 0.4824 -0.0085 -0.0339 0.0116  385 LEU B CG  
7324  C CD1 . LEU B 385 ? 0.2029 0.3190 0.4793 -0.0057 -0.0308 0.0137  385 LEU B CD1 
7325  C CD2 . LEU B 385 ? 0.2217 0.3436 0.4875 -0.0098 -0.0404 0.0119  385 LEU B CD2 
7326  N N   . ALA B 386 ? 0.2394 0.3090 0.4696 0.0048  -0.0306 0.0148  386 ALA B N   
7327  C CA  . ALA B 386 ? 0.2578 0.3146 0.4804 0.0086  -0.0268 0.0163  386 ALA B CA  
7328  C C   . ALA B 386 ? 0.2651 0.3221 0.4903 0.0160  -0.0252 0.0210  386 ALA B C   
7329  O O   . ALA B 386 ? 0.2347 0.2985 0.4589 0.0206  -0.0286 0.0243  386 ALA B O   
7330  C CB  . ALA B 386 ? 0.2703 0.3235 0.4813 0.0079  -0.0289 0.0158  386 ALA B CB  
7331  N N   . PHE B 387 ? 0.2736 0.3227 0.5017 0.0171  -0.0203 0.0212  387 PHE B N   
7332  C CA  . PHE B 387 ? 0.2623 0.3087 0.4921 0.0235  -0.0182 0.0248  387 PHE B CA  
7333  C C   . PHE B 387 ? 0.2749 0.3089 0.4950 0.0258  -0.0157 0.0270  387 PHE B C   
7334  O O   . PHE B 387 ? 0.2712 0.2970 0.4873 0.0221  -0.0128 0.0250  387 PHE B O   
7335  C CB  . PHE B 387 ? 0.2406 0.2846 0.4775 0.0231  -0.0144 0.0238  387 PHE B CB  
7336  C CG  . PHE B 387 ? 0.2542 0.3110 0.5010 0.0226  -0.0161 0.0231  387 PHE B CG  
7337  C CD1 . PHE B 387 ? 0.2730 0.3366 0.5233 0.0161  -0.0181 0.0200  387 PHE B CD1 
7338  C CD2 . PHE B 387 ? 0.2811 0.3423 0.5333 0.0283  -0.0150 0.0254  387 PHE B CD2 
7339  C CE1 . PHE B 387 ? 0.2873 0.3633 0.5469 0.0148  -0.0192 0.0196  387 PHE B CE1 
7340  C CE2 . PHE B 387 ? 0.2708 0.3451 0.5326 0.0277  -0.0158 0.0249  387 PHE B CE2 
7341  C CZ  . PHE B 387 ? 0.2667 0.3489 0.5325 0.0207  -0.0179 0.0222  387 PHE B CZ  
7342  N N   . GLU B 388 ? 0.2887 0.3217 0.5057 0.0321  -0.0165 0.0313  388 GLU B N   
7343  C CA  . GLU B 388 ? 0.3110 0.3316 0.5184 0.0346  -0.0140 0.0344  388 GLU B CA  
7344  C C   . GLU B 388 ? 0.3098 0.3237 0.5182 0.0402  -0.0115 0.0375  388 GLU B C   
7345  O O   . GLU B 388 ? 0.3058 0.3260 0.5173 0.0460  -0.0139 0.0398  388 GLU B O   
7346  C CB  . GLU B 388 ? 0.3138 0.3370 0.5129 0.0373  -0.0179 0.0373  388 GLU B CB  
7347  C CG  . GLU B 388 ? 0.3148 0.3423 0.5104 0.0316  -0.0202 0.0339  388 GLU B CG  
7348  C CD  . GLU B 388 ? 0.3377 0.3695 0.5251 0.0339  -0.0249 0.0363  388 GLU B CD  
7349  O OE1 . GLU B 388 ? 0.3372 0.3698 0.5221 0.0404  -0.0270 0.0411  388 GLU B OE1 
7350  O OE2 . GLU B 388 ? 0.3617 0.3959 0.5451 0.0290  -0.0267 0.0330  388 GLU B OE2 
7351  N N   . PHE B 389 ? 0.3022 0.3038 0.5079 0.0384  -0.0068 0.0373  389 PHE B N   
7352  C CA  . PHE B 389 ? 0.3267 0.3187 0.5308 0.0428  -0.0042 0.0399  389 PHE B CA  
7353  C C   . PHE B 389 ? 0.3195 0.2991 0.5121 0.0444  -0.0028 0.0439  389 PHE B C   
7354  O O   . PHE B 389 ? 0.3137 0.2886 0.5014 0.0395  -0.0008 0.0433  389 PHE B O   
7355  C CB  . PHE B 389 ? 0.3237 0.3105 0.5327 0.0392  -0.0005 0.0369  389 PHE B CB  
7356  C CG  . PHE B 389 ? 0.2979 0.2955 0.5171 0.0372  -0.0014 0.0333  389 PHE B CG  
7357  C CD1 . PHE B 389 ? 0.3123 0.3163 0.5346 0.0316  -0.0024 0.0300  389 PHE B CD1 
7358  C CD2 . PHE B 389 ? 0.2904 0.2906 0.5149 0.0410  -0.0009 0.0332  389 PHE B CD2 
7359  C CE1 . PHE B 389 ? 0.2997 0.3122 0.5303 0.0293  -0.0032 0.0271  389 PHE B CE1 
7360  C CE2 . PHE B 389 ? 0.2832 0.2931 0.5163 0.0388  -0.0013 0.0303  389 PHE B CE2 
7361  C CZ  . PHE B 389 ? 0.3013 0.3169 0.5373 0.0327  -0.0025 0.0275  389 PHE B CZ  
7362  N N   . TYR B 390 ? 0.3336 0.3080 0.5216 0.0514  -0.0035 0.0481  390 TYR B N   
7363  C CA  . TYR B 390 ? 0.3664 0.3276 0.5421 0.0532  -0.0022 0.0527  390 TYR B CA  
7364  C C   . TYR B 390 ? 0.3494 0.2948 0.5210 0.0557  0.0015  0.0546  390 TYR B C   
7365  O O   . TYR B 390 ? 0.3376 0.2834 0.5143 0.0600  0.0016  0.0540  390 TYR B O   
7366  C CB  . TYR B 390 ? 0.3861 0.3516 0.5562 0.0600  -0.0067 0.0571  390 TYR B CB  
7367  C CG  . TYR B 390 ? 0.4295 0.4088 0.6005 0.0576  -0.0110 0.0556  390 TYR B CG  
7368  C CD1 . TYR B 390 ? 0.4079 0.4038 0.5895 0.0575  -0.0147 0.0525  390 TYR B CD1 
7369  C CD2 . TYR B 390 ? 0.4663 0.4418 0.6267 0.0550  -0.0112 0.0573  390 TYR B CD2 
7370  C CE1 . TYR B 390 ? 0.4234 0.4307 0.6049 0.0545  -0.0189 0.0509  390 TYR B CE1 
7371  C CE2 . TYR B 390 ? 0.4665 0.4533 0.6260 0.0528  -0.0153 0.0556  390 TYR B CE2 
7372  C CZ  . TYR B 390 ? 0.4579 0.4604 0.6280 0.0524  -0.0194 0.0523  390 TYR B CZ  
7373  O OH  . TYR B 390 ? 0.4527 0.4653 0.6213 0.0492  -0.0236 0.0501  390 TYR B OH  
7374  N N   . ASP B 391 ? 0.3573 0.2884 0.5191 0.0528  0.0046  0.0571  391 ASP B N   
7375  C CA  . ASP B 391 ? 0.3914 0.3049 0.5468 0.0542  0.0080  0.0593  391 ASP B CA  
7376  C C   . ASP B 391 ? 0.4221 0.3267 0.5675 0.0628  0.0064  0.0652  391 ASP B C   
7377  O O   . ASP B 391 ? 0.4466 0.3612 0.5921 0.0681  0.0022  0.0672  391 ASP B O   
7378  C CB  . ASP B 391 ? 0.3916 0.2947 0.5425 0.0455  0.0124  0.0588  391 ASP B CB  
7379  C CG  . ASP B 391 ? 0.3780 0.2765 0.5189 0.0426  0.0135  0.0624  391 ASP B CG  
7380  O OD1 . ASP B 391 ? 0.3822 0.2807 0.5159 0.0482  0.0109  0.0665  391 ASP B OD1 
7381  O OD2 . ASP B 391 ? 0.3778 0.2728 0.5179 0.0348  0.0172  0.0612  391 ASP B OD2 
7382  N N   . SER B 392 ? 0.4632 0.3484 0.5995 0.0642  0.0095  0.0680  392 SER B N   
7383  C CA  . SER B 392 ? 0.4678 0.3416 0.5937 0.0734  0.0083  0.0738  392 SER B CA  
7384  C C   . SER B 392 ? 0.4615 0.3305 0.5754 0.0733  0.0074  0.0792  392 SER B C   
7385  O O   . SER B 392 ? 0.4687 0.3317 0.5741 0.0819  0.0051  0.0845  392 SER B O   
7386  C CB  . SER B 392 ? 0.5015 0.3541 0.6204 0.0747  0.0121  0.0747  392 SER B CB  
7387  O OG  . SER B 392 ? 0.5330 0.3722 0.6454 0.0649  0.0163  0.0747  392 SER B OG  
7388  N N   . ASP B 393 ? 0.4532 0.3250 0.5659 0.0641  0.0092  0.0780  393 ASP B N   
7389  C CA  . ASP B 393 ? 0.4790 0.3487 0.5805 0.0637  0.0085  0.0825  393 ASP B CA  
7390  C C   . ASP B 393 ? 0.4534 0.3437 0.5605 0.0649  0.0035  0.0807  393 ASP B C   
7391  O O   . ASP B 393 ? 0.4387 0.3310 0.5381 0.0630  0.0027  0.0828  393 ASP B O   
7392  C CB  . ASP B 393 ? 0.5332 0.3917 0.6277 0.0539  0.0140  0.0831  393 ASP B CB  
7393  C CG  . ASP B 393 ? 0.5781 0.4151 0.6655 0.0517  0.0185  0.0852  393 ASP B CG  
7394  O OD1 . ASP B 393 ? 0.6148 0.4374 0.6926 0.0593  0.0177  0.0901  393 ASP B OD1 
7395  O OD2 . ASP B 393 ? 0.5424 0.3768 0.6340 0.0427  0.0226  0.0819  393 ASP B OD2 
7396  N N   . ASN B 394 ? 0.4594 0.3649 0.5796 0.0677  0.0003  0.0767  394 ASN B N   
7397  C CA  . ASN B 394 ? 0.4698 0.3945 0.5960 0.0684  -0.0047 0.0746  394 ASN B CA  
7398  C C   . ASN B 394 ? 0.4613 0.3920 0.5883 0.0591  -0.0031 0.0708  394 ASN B C   
7399  O O   . ASN B 394 ? 0.4426 0.3825 0.5666 0.0588  -0.0065 0.0708  394 ASN B O   
7400  C CB  . ASN B 394 ? 0.4920 0.4184 0.6096 0.0767  -0.0097 0.0803  394 ASN B CB  
7401  C CG  . ASN B 394 ? 0.5274 0.4754 0.6546 0.0793  -0.0159 0.0778  394 ASN B CG  
7402  O OD1 . ASN B 394 ? 0.5407 0.4991 0.6809 0.0808  -0.0169 0.0745  394 ASN B OD1 
7403  N ND2 . ASN B 394 ? 0.5527 0.5078 0.6737 0.0784  -0.0198 0.0790  394 ASN B ND2 
7404  N N   . LYS B 395 ? 0.4552 0.3808 0.5861 0.0520  0.0020  0.0675  395 LYS B N   
7405  C CA  . LYS B 395 ? 0.4899 0.4217 0.6236 0.0440  0.0041  0.0633  395 LYS B CA  
7406  C C   . LYS B 395 ? 0.4449 0.3880 0.5931 0.0413  0.0034  0.0572  395 LYS B C   
7407  O O   . LYS B 395 ? 0.4062 0.3476 0.5612 0.0430  0.0040  0.0561  395 LYS B O   
7408  C CB  . LYS B 395 ? 0.5106 0.4299 0.6384 0.0377  0.0102  0.0643  395 LYS B CB  
7409  C CG  . LYS B 395 ? 0.6141 0.5232 0.7266 0.0383  0.0116  0.0701  395 LYS B CG  
7410  C CD  . LYS B 395 ? 0.7195 0.6150 0.8274 0.0322  0.0180  0.0717  395 LYS B CD  
7411  C CE  . LYS B 395 ? 0.7870 0.6699 0.8791 0.0320  0.0204  0.0780  395 LYS B CE  
7412  N NZ  . LYS B 395 ? 0.8748 0.7439 0.9589 0.0387  0.0188  0.0833  395 LYS B NZ  
7413  N N   . ILE B 396 ? 0.4483 0.4022 0.6002 0.0373  0.0023  0.0532  396 ILE B N   
7414  C CA  . ILE B 396 ? 0.4523 0.4160 0.6166 0.0345  0.0017  0.0477  396 ILE B CA  
7415  C C   . ILE B 396 ? 0.4416 0.3994 0.6098 0.0291  0.0068  0.0453  396 ILE B C   
7416  O O   . ILE B 396 ? 0.4796 0.4332 0.6430 0.0249  0.0102  0.0455  396 ILE B O   
7417  C CB  . ILE B 396 ? 0.4471 0.4223 0.6127 0.0322  -0.0015 0.0442  396 ILE B CB  
7418  C CG1 . ILE B 396 ? 0.5183 0.5024 0.6837 0.0372  -0.0075 0.0459  396 ILE B CG1 
7419  C CG2 . ILE B 396 ? 0.4393 0.4210 0.6155 0.0278  -0.0008 0.0386  396 ILE B CG2 
7420  C CD1 . ILE B 396 ? 0.5634 0.5587 0.7295 0.0345  -0.0115 0.0424  396 ILE B CD1 
7421  N N   . ILE B 397 ? 0.4260 0.3844 0.6029 0.0292  0.0072  0.0432  397 ILE B N   
7422  C CA  . ILE B 397 ? 0.4101 0.3647 0.5916 0.0241  0.0110  0.0407  397 ILE B CA  
7423  C C   . ILE B 397 ? 0.3806 0.3449 0.5723 0.0215  0.0101  0.0357  397 ILE B C   
7424  O O   . ILE B 397 ? 0.3512 0.3142 0.5470 0.0175  0.0127  0.0334  397 ILE B O   
7425  C CB  . ILE B 397 ? 0.3944 0.3385 0.5753 0.0256  0.0128  0.0424  397 ILE B CB  
7426  C CG1 . ILE B 397 ? 0.3999 0.3478 0.5856 0.0313  0.0099  0.0422  397 ILE B CG1 
7427  C CG2 . ILE B 397 ? 0.4148 0.3463 0.5843 0.0264  0.0148  0.0474  397 ILE B CG2 
7428  C CD1 . ILE B 397 ? 0.4360 0.3727 0.6202 0.0336  0.0117  0.0433  397 ILE B CD1 
7429  N N   . LYS B 398 ? 0.3821 0.3559 0.5776 0.0237  0.0063  0.0342  398 LYS B N   
7430  C CA  . LYS B 398 ? 0.3503 0.3320 0.5537 0.0207  0.0054  0.0298  398 LYS B CA  
7431  C C   . LYS B 398 ? 0.3751 0.3663 0.5789 0.0215  0.0012  0.0287  398 LYS B C   
7432  O O   . LYS B 398 ? 0.3678 0.3629 0.5707 0.0256  -0.0019 0.0310  398 LYS B O   
7433  C CB  . LYS B 398 ? 0.3238 0.3060 0.5349 0.0212  0.0057  0.0284  398 LYS B CB  
7434  C CG  . LYS B 398 ? 0.3177 0.3061 0.5360 0.0179  0.0052  0.0243  398 LYS B CG  
7435  C CD  . LYS B 398 ? 0.3011 0.2903 0.5260 0.0181  0.0056  0.0229  398 LYS B CD  
7436  C CE  . LYS B 398 ? 0.3008 0.2968 0.5314 0.0155  0.0043  0.0197  398 LYS B CE  
7437  N NZ  . LYS B 398 ? 0.3057 0.3015 0.5413 0.0159  0.0051  0.0190  398 LYS B NZ  
7438  N N   . ASN B 399 ? 0.3793 0.3742 0.5844 0.0176  0.0011  0.0250  399 ASN B N   
7439  C CA  . ASN B 399 ? 0.3585 0.3616 0.5651 0.0165  -0.0027 0.0226  399 ASN B CA  
7440  C C   . ASN B 399 ? 0.3411 0.3472 0.5560 0.0136  -0.0025 0.0191  399 ASN B C   
7441  O O   . ASN B 399 ? 0.3567 0.3581 0.5736 0.0118  0.0007  0.0177  399 ASN B O   
7442  C CB  . ASN B 399 ? 0.3501 0.3525 0.5491 0.0142  -0.0029 0.0210  399 ASN B CB  
7443  C CG  . ASN B 399 ? 0.3620 0.3620 0.5514 0.0168  -0.0037 0.0246  399 ASN B CG  
7444  O OD1 . ASN B 399 ? 0.3541 0.3481 0.5368 0.0160  -0.0003 0.0253  399 ASN B OD1 
7445  N ND2 . ASN B 399 ? 0.3933 0.3989 0.5817 0.0199  -0.0081 0.0269  399 ASN B ND2 
7446  N N   . GLU B 400 ? 0.3195 0.3337 0.5390 0.0130  -0.0059 0.0179  400 GLU B N   
7447  C CA  . GLU B 400 ? 0.2826 0.2990 0.5084 0.0095  -0.0058 0.0147  400 GLU B CA  
7448  C C   . GLU B 400 ? 0.2649 0.2905 0.4931 0.0073  -0.0100 0.0134  400 GLU B C   
7449  O O   . GLU B 400 ? 0.2740 0.3072 0.5037 0.0098  -0.0129 0.0155  400 GLU B O   
7450  C CB  . GLU B 400 ? 0.2824 0.2977 0.5146 0.0108  -0.0037 0.0155  400 GLU B CB  
7451  C CG  . GLU B 400 ? 0.2932 0.3085 0.5302 0.0072  -0.0029 0.0126  400 GLU B CG  
7452  C CD  . GLU B 400 ? 0.3137 0.3272 0.5557 0.0082  -0.0007 0.0132  400 GLU B CD  
7453  O OE1 . GLU B 400 ? 0.2528 0.2652 0.4949 0.0120  0.0001  0.0156  400 GLU B OE1 
7454  O OE2 . GLU B 400 ? 0.3073 0.3193 0.5518 0.0054  0.0001  0.0111  400 GLU B OE2 
7455  N N   . SER B 401 ? 0.2459 0.2709 0.4747 0.0026  -0.0104 0.0098  401 SER B N   
7456  C CA  . SER B 401 ? 0.2405 0.2734 0.4712 -0.0010 -0.0143 0.0081  401 SER B CA  
7457  C C   . SER B 401 ? 0.2204 0.2572 0.4595 -0.0031 -0.0137 0.0077  401 SER B C   
7458  O O   . SER B 401 ? 0.2185 0.2490 0.4594 -0.0030 -0.0104 0.0073  401 SER B O   
7459  C CB  . SER B 401 ? 0.2477 0.2759 0.4716 -0.0055 -0.0153 0.0043  401 SER B CB  
7460  O OG  . SER B 401 ? 0.2490 0.2753 0.4643 -0.0040 -0.0164 0.0046  401 SER B OG  
7461  N N   . ILE B 402 ? 0.2147 0.2627 0.4589 -0.0049 -0.0169 0.0080  402 ILE B N   
7462  C CA  . ILE B 402 ? 0.2151 0.2674 0.4663 -0.0085 -0.0163 0.0072  402 ILE B CA  
7463  C C   . ILE B 402 ? 0.2148 0.2717 0.4653 -0.0154 -0.0200 0.0045  402 ILE B C   
7464  O O   . ILE B 402 ? 0.2293 0.2966 0.4807 -0.0159 -0.0240 0.0050  402 ILE B O   
7465  C CB  . ILE B 402 ? 0.2246 0.2875 0.4841 -0.0046 -0.0160 0.0102  402 ILE B CB  
7466  C CG1 . ILE B 402 ? 0.2244 0.2805 0.4832 0.0018  -0.0124 0.0125  402 ILE B CG1 
7467  C CG2 . ILE B 402 ? 0.2308 0.2998 0.4976 -0.0090 -0.0151 0.0095  402 ILE B CG2 
7468  C CD1 . ILE B 402 ? 0.2223 0.2695 0.4815 0.0004  -0.0085 0.0113  402 ILE B CD1 
7469  N N   . ASN B 403 ? 0.2014 0.2507 0.4501 -0.0207 -0.0187 0.0017  403 ASN B N   
7470  C CA  . ASN B 403 ? 0.2184 0.2693 0.4650 -0.0281 -0.0220 -0.0012 403 ASN B CA  
7471  C C   . ASN B 403 ? 0.2164 0.2776 0.4719 -0.0327 -0.0224 -0.0005 403 ASN B C   
7472  O O   . ASN B 403 ? 0.2203 0.2771 0.4785 -0.0335 -0.0191 -0.0001 403 ASN B O   
7473  C CB  . ASN B 403 ? 0.2276 0.2631 0.4661 -0.0316 -0.0204 -0.0048 403 ASN B CB  
7474  C CG  . ASN B 403 ? 0.2337 0.2613 0.4632 -0.0279 -0.0202 -0.0059 403 ASN B CG  
7475  O OD1 . ASN B 403 ? 0.2724 0.3037 0.4972 -0.0291 -0.0236 -0.0070 403 ASN B OD1 
7476  N ND2 . ASN B 403 ? 0.2220 0.2411 0.4498 -0.0233 -0.0162 -0.0053 403 ASN B ND2 
7477  N N   . ILE B 404 ? 0.2124 0.2873 0.4718 -0.0363 -0.0267 -0.0005 404 ILE B N   
7478  C CA  . ILE B 404 ? 0.2248 0.3111 0.4931 -0.0418 -0.0270 0.0000  404 ILE B CA  
7479  C C   . ILE B 404 ? 0.2500 0.3380 0.5154 -0.0517 -0.0313 -0.0033 404 ILE B C   
7480  O O   . ILE B 404 ? 0.2625 0.3469 0.5201 -0.0527 -0.0347 -0.0055 404 ILE B O   
7481  C CB  . ILE B 404 ? 0.2160 0.3212 0.4950 -0.0369 -0.0278 0.0036  404 ILE B CB  
7482  C CG1 . ILE B 404 ? 0.2202 0.3382 0.4998 -0.0362 -0.0337 0.0039  404 ILE B CG1 
7483  C CG2 . ILE B 404 ? 0.2125 0.3139 0.4927 -0.0273 -0.0237 0.0065  404 ILE B CG2 
7484  C CD1 . ILE B 404 ? 0.2159 0.3543 0.5070 -0.0312 -0.0349 0.0075  404 ILE B CD1 
7485  N N   . LEU B 405 ? 0.2390 0.3324 0.5102 -0.0592 -0.0308 -0.0036 405 LEU B N   
7486  C CA  . LEU B 405 ? 0.2621 0.3610 0.5331 -0.0696 -0.0350 -0.0062 405 LEU B CA  
7487  C C   . LEU B 405 ? 0.2569 0.3801 0.5420 -0.0714 -0.0366 -0.0035 405 LEU B C   
7488  O O   . LEU B 405 ? 0.2563 0.3845 0.5491 -0.0704 -0.0325 -0.0011 405 LEU B O   
7489  C CB  . LEU B 405 ? 0.2787 0.3612 0.5438 -0.0774 -0.0324 -0.0085 405 LEU B CB  
7490  C CG  . LEU B 405 ? 0.3018 0.3844 0.5640 -0.0898 -0.0362 -0.0119 405 LEU B CG  
7491  C CD1 . LEU B 405 ? 0.3319 0.4071 0.5831 -0.0906 -0.0406 -0.0157 405 LEU B CD1 
7492  C CD2 . LEU B 405 ? 0.3203 0.3868 0.5776 -0.0972 -0.0328 -0.0131 405 LEU B CD2 
7493  N N   . ALA B 406 ? 0.2491 0.3877 0.5373 -0.0737 -0.0425 -0.0039 406 ALA B N   
7494  C CA  . ALA B 406 ? 0.2461 0.4102 0.5488 -0.0724 -0.0440 -0.0008 406 ALA B CA  
7495  C C   . ALA B 406 ? 0.2551 0.4348 0.5626 -0.0834 -0.0499 -0.0027 406 ALA B C   
7496  O O   . ALA B 406 ? 0.2541 0.4290 0.5530 -0.0882 -0.0550 -0.0059 406 ALA B O   
7497  C CB  . ALA B 406 ? 0.2381 0.4105 0.5428 -0.0606 -0.0457 0.0021  406 ALA B CB  
7498  N N   . SER B 407 ? 0.2609 0.4611 0.5826 -0.0866 -0.0491 -0.0004 407 SER B N   
7499  C CA  . SER B 407 ? 0.2872 0.5088 0.6171 -0.0958 -0.0550 -0.0013 407 SER B CA  
7500  C C   . SER B 407 ? 0.2855 0.5360 0.6334 -0.0911 -0.0546 0.0029  407 SER B C   
7501  O O   . SER B 407 ? 0.2864 0.5382 0.6400 -0.0835 -0.0485 0.0059  407 SER B O   
7502  C CB  . SER B 407 ? 0.2961 0.5104 0.6234 -0.1108 -0.0545 -0.0044 407 SER B CB  
7503  O OG  . SER B 407 ? 0.3016 0.5360 0.6358 -0.1208 -0.0610 -0.0057 407 SER B OG  
7504  N N   . LYS B 408 ? 0.3342 0.6087 0.6911 -0.0960 -0.0611 0.0029  408 LYS B N   
7505  C CA  . LYS B 408 ? 0.3817 0.6863 0.7570 -0.0915 -0.0610 0.0067  408 LYS B CA  
7506  C C   . LYS B 408 ? 0.4088 0.7217 0.7944 -0.0998 -0.0552 0.0075  408 LYS B C   
7507  O O   . LYS B 408 ? 0.3764 0.7071 0.7753 -0.0931 -0.0511 0.0111  408 LYS B O   
7508  C CB  . LYS B 408 ? 0.4162 0.7457 0.7987 -0.0944 -0.0701 0.0067  408 LYS B CB  
7509  C CG  . LYS B 408 ? 0.4484 0.7796 0.8265 -0.0813 -0.0747 0.0085  408 LYS B CG  
7510  C CD  . LYS B 408 ? 0.4835 0.8366 0.8658 -0.0844 -0.0849 0.0082  408 LYS B CD  
7511  C CE  . LYS B 408 ? 0.5444 0.8931 0.9182 -0.0715 -0.0889 0.0101  408 LYS B CE  
7512  N NZ  . LYS B 408 ? 0.5686 0.9247 0.9367 -0.0769 -0.0989 0.0080  408 LYS B NZ  
7513  N N   . THR B 409 ? 0.4348 0.7333 0.8132 -0.1138 -0.0546 0.0042  409 THR B N   
7514  C CA  . THR B 409 ? 0.4495 0.7528 0.8352 -0.1238 -0.0492 0.0049  409 THR B CA  
7515  C C   . THR B 409 ? 0.4665 0.7375 0.8375 -0.1279 -0.0437 0.0030  409 THR B C   
7516  O O   . THR B 409 ? 0.4805 0.7275 0.8366 -0.1249 -0.0451 0.0006  409 THR B O   
7517  C CB  . THR B 409 ? 0.4526 0.7754 0.8464 -0.1392 -0.0548 0.0031  409 THR B CB  
7518  O OG1 . THR B 409 ? 0.4325 0.7351 0.8107 -0.1471 -0.0602 -0.0016 409 THR B OG1 
7519  C CG2 . THR B 409 ? 0.4489 0.8068 0.8589 -0.1352 -0.0605 0.0052  409 THR B CG2 
7520  N N   . ALA B 410 ? 0.4910 0.7626 0.8665 -0.1351 -0.0377 0.0043  410 ALA B N   
7521  C CA  . ALA B 410 ? 0.4715 0.7143 0.8340 -0.1395 -0.0324 0.0033  410 ALA B CA  
7522  C C   . ALA B 410 ? 0.4414 0.6652 0.7907 -0.1516 -0.0371 -0.0012 410 ALA B C   
7523  O O   . ALA B 410 ? 0.4351 0.6717 0.7876 -0.1599 -0.0436 -0.0034 410 ALA B O   
7524  C CB  . ALA B 410 ? 0.4675 0.7180 0.8381 -0.1457 -0.0256 0.0061  410 ALA B CB  
7525  N N   . PHE B 411 ? 0.4162 0.6092 0.7500 -0.1516 -0.0339 -0.0027 411 PHE B N   
7526  C CA  . PHE B 411 ? 0.4046 0.5755 0.7237 -0.1612 -0.0374 -0.0073 411 PHE B CA  
7527  C C   . PHE B 411 ? 0.4099 0.5521 0.7168 -0.1630 -0.0315 -0.0072 411 PHE B C   
7528  O O   . PHE B 411 ? 0.3701 0.5060 0.6768 -0.1534 -0.0260 -0.0043 411 PHE B O   
7529  C CB  . PHE B 411 ? 0.3837 0.5460 0.6932 -0.1545 -0.0430 -0.0105 411 PHE B CB  
7530  C CG  . PHE B 411 ? 0.3803 0.5308 0.6846 -0.1385 -0.0400 -0.0091 411 PHE B CG  
7531  C CD1 . PHE B 411 ? 0.3516 0.5200 0.6656 -0.1265 -0.0402 -0.0060 411 PHE B CD1 
7532  C CD2 . PHE B 411 ? 0.3751 0.4964 0.6644 -0.1354 -0.0371 -0.0108 411 PHE B CD2 
7533  C CE1 . PHE B 411 ? 0.3535 0.5105 0.6623 -0.1132 -0.0375 -0.0048 411 PHE B CE1 
7534  C CE2 . PHE B 411 ? 0.3689 0.4812 0.6544 -0.1218 -0.0346 -0.0096 411 PHE B CE2 
7535  C CZ  . PHE B 411 ? 0.3546 0.4844 0.6497 -0.1112 -0.0347 -0.0066 411 PHE B CZ  
7536  N N   . GLU B 412 ? 0.4499 0.5743 0.7457 -0.1752 -0.0332 -0.0105 412 GLU B N   
7537  C CA  . GLU B 412 ? 0.5132 0.6086 0.7959 -0.1779 -0.0284 -0.0106 412 GLU B CA  
7538  C C   . GLU B 412 ? 0.4841 0.5553 0.7529 -0.1667 -0.0283 -0.0126 412 GLU B C   
7539  O O   . GLU B 412 ? 0.4790 0.5449 0.7408 -0.1655 -0.0331 -0.0165 412 GLU B O   
7540  C CB  . GLU B 412 ? 0.5637 0.6465 0.8380 -0.1948 -0.0305 -0.0137 412 GLU B CB  
7541  C CG  . GLU B 412 ? 0.6149 0.7147 0.9004 -0.2077 -0.0282 -0.0109 412 GLU B CG  
7542  C CD  . GLU B 412 ? 0.6859 0.7692 0.9611 -0.2252 -0.0298 -0.0140 412 GLU B CD  
7543  O OE1 . GLU B 412 ? 0.7081 0.7589 0.9655 -0.2254 -0.0289 -0.0163 412 GLU B OE1 
7544  O OE2 . GLU B 412 ? 0.6622 0.7652 0.9473 -0.2385 -0.0320 -0.0140 412 GLU B OE2 
7545  N N   . LEU B 413 ? 0.4968 0.5539 0.7616 -0.1592 -0.0225 -0.0099 413 LEU B N   
7546  C CA  . LEU B 413 ? 0.4774 0.5092 0.7287 -0.1501 -0.0213 -0.0114 413 LEU B CA  
7547  C C   . LEU B 413 ? 0.4690 0.4731 0.7065 -0.1572 -0.0188 -0.0124 413 LEU B C   
7548  O O   . LEU B 413 ? 0.4511 0.4553 0.6904 -0.1663 -0.0161 -0.0101 413 LEU B O   
7549  C CB  . LEU B 413 ? 0.4385 0.4740 0.6949 -0.1369 -0.0169 -0.0076 413 LEU B CB  
7550  C CG  . LEU B 413 ? 0.4399 0.4972 0.7073 -0.1270 -0.0184 -0.0063 413 LEU B CG  
7551  C CD1 . LEU B 413 ? 0.4119 0.4703 0.6831 -0.1159 -0.0135 -0.0026 413 LEU B CD1 
7552  C CD2 . LEU B 413 ? 0.4842 0.5352 0.7447 -0.1216 -0.0227 -0.0098 413 LEU B CD2 
7553  N N   . PRO B 414 ? 0.4854 0.4643 0.7086 -0.1522 -0.0189 -0.0151 414 PRO B N   
7554  C CA  . PRO B 414 ? 0.5026 0.4547 0.7132 -0.1549 -0.0155 -0.0147 414 PRO B CA  
7555  C C   . PRO B 414 ? 0.4912 0.4432 0.7055 -0.1471 -0.0102 -0.0095 414 PRO B C   
7556  O O   . PRO B 414 ? 0.4708 0.4369 0.6937 -0.1367 -0.0092 -0.0075 414 PRO B O   
7557  C CB  . PRO B 414 ? 0.5210 0.4508 0.7174 -0.1494 -0.0173 -0.0191 414 PRO B CB  
7558  C CG  . PRO B 414 ? 0.5255 0.4709 0.7284 -0.1392 -0.0197 -0.0202 414 PRO B CG  
7559  C CD  . PRO B 414 ? 0.4984 0.4736 0.7166 -0.1436 -0.0220 -0.0185 414 PRO B CD  
7560  N N   . GLU B 415 ? 0.4931 0.4288 0.7002 -0.1530 -0.0068 -0.0073 415 GLU B N   
7561  C CA  . GLU B 415 ? 0.4875 0.4224 0.6965 -0.1480 -0.0019 -0.0022 415 GLU B CA  
7562  C C   . GLU B 415 ? 0.4936 0.3981 0.6870 -0.1461 0.0002  -0.0015 415 GLU B C   
7563  O O   . GLU B 415 ? 0.5138 0.3989 0.6960 -0.1551 -0.0003 -0.0032 415 GLU B O   
7564  C CB  . GLU B 415 ? 0.5329 0.4818 0.7501 -0.1575 0.0013  0.0018  415 GLU B CB  
7565  C CG  . GLU B 415 ? 0.5761 0.5549 0.8086 -0.1636 -0.0007 0.0013  415 GLU B CG  
7566  C CD  . GLU B 415 ? 0.6277 0.6199 0.8680 -0.1728 0.0035  0.0054  415 GLU B CD  
7567  O OE1 . GLU B 415 ? 0.7339 0.7269 0.9755 -0.1659 0.0080  0.0093  415 GLU B OE1 
7568  O OE2 . GLU B 415 ? 0.6671 0.6687 0.9118 -0.1863 0.0024  0.0049  415 GLU B OE2 
7569  N N   . LEU B 416 ? 0.4676 0.3681 0.6602 -0.1344 0.0027  0.0012  416 LEU B N   
7570  C CA  . LEU B 416 ? 0.4612 0.3365 0.6410 -0.1300 0.0048  0.0029  416 LEU B CA  
7571  C C   . LEU B 416 ? 0.4403 0.3205 0.6231 -0.1296 0.0089  0.0086  416 LEU B C   
7572  O O   . LEU B 416 ? 0.4147 0.3137 0.6079 -0.1231 0.0100  0.0104  416 LEU B O   
7573  C CB  . LEU B 416 ? 0.4510 0.3185 0.6273 -0.1164 0.0034  0.0009  416 LEU B CB  
7574  C CG  . LEU B 416 ? 0.4581 0.2997 0.6211 -0.1101 0.0048  0.0021  416 LEU B CG  
7575  C CD1 . LEU B 416 ? 0.4643 0.2984 0.6236 -0.0989 0.0030  -0.0014 416 LEU B CD1 
7576  C CD2 . LEU B 416 ? 0.4305 0.2738 0.5950 -0.1050 0.0078  0.0075  416 LEU B CD2 
7577  N N   . THR B 417 ? 0.4540 0.3164 0.6267 -0.1368 0.0113  0.0113  417 THR B N   
7578  C CA  . THR B 417 ? 0.4534 0.3149 0.6247 -0.1365 0.0155  0.0169  417 THR B CA  
7579  C C   . THR B 417 ? 0.4576 0.2890 0.6124 -0.1334 0.0161  0.0186  417 THR B C   
7580  O O   . THR B 417 ? 0.4683 0.2805 0.6132 -0.1361 0.0142  0.0156  417 THR B O   
7581  C CB  . THR B 417 ? 0.4703 0.3432 0.6466 -0.1502 0.0184  0.0194  417 THR B CB  
7582  O OG1 . THR B 417 ? 0.4926 0.3507 0.6608 -0.1626 0.0172  0.0175  417 THR B OG1 
7583  C CG2 . THR B 417 ? 0.4626 0.3675 0.6565 -0.1512 0.0179  0.0183  417 THR B CG2 
7584  N N   . ILE B 418 ? 0.4607 0.2884 0.6123 -0.1271 0.0187  0.0233  418 ILE B N   
7585  C CA  . ILE B 418 ? 0.4830 0.2834 0.6190 -0.1236 0.0194  0.0261  418 ILE B CA  
7586  C C   . ILE B 418 ? 0.5108 0.3081 0.6421 -0.1303 0.0236  0.0320  418 ILE B C   
7587  O O   . ILE B 418 ? 0.5302 0.3491 0.6718 -0.1326 0.0260  0.0339  418 ILE B O   
7588  C CB  . ILE B 418 ? 0.4485 0.2456 0.5834 -0.1080 0.0177  0.0261  418 ILE B CB  
7589  C CG1 . ILE B 418 ? 0.4471 0.2648 0.5918 -0.1017 0.0191  0.0288  418 ILE B CG1 
7590  C CG2 . ILE B 418 ? 0.4311 0.2292 0.5690 -0.1022 0.0142  0.0204  418 ILE B CG2 
7591  C CD1 . ILE B 418 ? 0.4435 0.2619 0.5894 -0.0873 0.0170  0.0283  418 ILE B CD1 
7592  N N   . GLU B 419 ? 0.5497 0.3198 0.6650 -0.1327 0.0246  0.0350  419 GLU B N   
7593  C CA  . GLU B 419 ? 0.5726 0.3341 0.6794 -0.1352 0.0284  0.0415  419 GLU B CA  
7594  C C   . GLU B 419 ? 0.5795 0.3200 0.6740 -0.1228 0.0269  0.0440  419 GLU B C   
7595  O O   . GLU B 419 ? 0.5972 0.3181 0.6832 -0.1187 0.0243  0.0416  419 GLU B O   
7596  C CB  . GLU B 419 ? 0.6132 0.3586 0.7100 -0.1504 0.0310  0.0437  419 GLU B CB  
7597  C CG  . GLU B 419 ? 0.6311 0.3964 0.7398 -0.1644 0.0321  0.0412  419 GLU B CG  
7598  C CD  . GLU B 419 ? 0.6953 0.4419 0.7930 -0.1803 0.0342  0.0429  419 GLU B CD  
7599  O OE1 . GLU B 419 ? 0.6953 0.4171 0.7810 -0.1828 0.0318  0.0403  419 GLU B OE1 
7600  O OE2 . GLU B 419 ? 0.7572 0.5134 0.8576 -0.1906 0.0386  0.0469  419 GLU B OE2 
7601  N N   . VAL B 420 ? 0.5590 0.3043 0.6525 -0.1164 0.0284  0.0485  420 VAL B N   
7602  C CA  . VAL B 420 ? 0.5334 0.2650 0.6182 -0.1030 0.0261  0.0508  420 VAL B CA  
7603  C C   . VAL B 420 ? 0.5435 0.2566 0.6129 -0.1053 0.0287  0.0579  420 VAL B C   
7604  O O   . VAL B 420 ? 0.5487 0.2700 0.6186 -0.1132 0.0327  0.0614  420 VAL B O   
7605  C CB  . VAL B 420 ? 0.4988 0.2524 0.5953 -0.0921 0.0245  0.0497  420 VAL B CB  
7606  C CG1 . VAL B 420 ? 0.5022 0.2439 0.5915 -0.0786 0.0215  0.0514  420 VAL B CG1 
7607  C CG2 . VAL B 420 ? 0.4773 0.2504 0.5890 -0.0905 0.0225  0.0435  420 VAL B CG2 
7608  N N   . THR B 421 ? 0.5560 0.2440 0.6113 -0.0978 0.0266  0.0601  421 THR B N   
7609  C CA  . THR B 421 ? 0.5691 0.2375 0.6081 -0.0975 0.0282  0.0672  421 THR B CA  
7610  C C   . THR B 421 ? 0.5714 0.2363 0.6066 -0.0816 0.0246  0.0694  421 THR B C   
7611  O O   . THR B 421 ? 0.5405 0.2039 0.5790 -0.0713 0.0208  0.0658  421 THR B O   
7612  C CB  . THR B 421 ? 0.6004 0.2382 0.6239 -0.1042 0.0289  0.0683  421 THR B CB  
7613  O OG1 . THR B 421 ? 0.5878 0.2336 0.6183 -0.1184 0.0311  0.0647  421 THR B OG1 
7614  C CG2 . THR B 421 ? 0.6259 0.2418 0.6312 -0.1070 0.0314  0.0763  421 THR B CG2 
7615  N N   . PRO B 422 ? 0.5991 0.2642 0.6276 -0.0788 0.0256  0.0753  422 PRO B N   
7616  C CA  . PRO B 422 ? 0.6021 0.2773 0.6305 -0.0892 0.0305  0.0789  422 PRO B CA  
7617  C C   . PRO B 422 ? 0.5796 0.2861 0.6271 -0.0928 0.0320  0.0742  422 PRO B C   
7618  O O   . PRO B 422 ? 0.5784 0.3003 0.6375 -0.0839 0.0287  0.0699  422 PRO B O   
7619  C CB  . PRO B 422 ? 0.6111 0.2816 0.6293 -0.0808 0.0295  0.0847  422 PRO B CB  
7620  C CG  . PRO B 422 ? 0.6283 0.2745 0.6346 -0.0703 0.0250  0.0864  422 PRO B CG  
7621  C CD  . PRO B 422 ? 0.6109 0.2658 0.6306 -0.0653 0.0219  0.0789  422 PRO B CD  
7622  N N   . GLU B 423 ? 0.5970 0.3123 0.6472 -0.1056 0.0372  0.0754  423 GLU B N   
7623  C CA  . GLU B 423 ? 0.5888 0.3324 0.6569 -0.1110 0.0392  0.0712  423 GLU B CA  
7624  C C   . GLU B 423 ? 0.5520 0.3169 0.6276 -0.1038 0.0399  0.0714  423 GLU B C   
7625  O O   . GLU B 423 ? 0.4970 0.2830 0.5878 -0.1007 0.0387  0.0666  423 GLU B O   
7626  C CB  . GLU B 423 ? 0.6144 0.3615 0.6833 -0.1270 0.0447  0.0728  423 GLU B CB  
7627  C CG  . GLU B 423 ? 0.6024 0.3793 0.6909 -0.1319 0.0462  0.0682  423 GLU B CG  
7628  C CD  . GLU B 423 ? 0.6232 0.4099 0.7155 -0.1472 0.0518  0.0698  423 GLU B CD  
7629  O OE1 . GLU B 423 ? 0.6496 0.4186 0.7296 -0.1569 0.0548  0.0741  423 GLU B OE1 
7630  O OE2 . GLU B 423 ? 0.6166 0.4302 0.7252 -0.1491 0.0533  0.0669  423 GLU B OE2 
7631  N N   . LYS B 424 ? 0.5744 0.3320 0.6382 -0.1011 0.0414  0.0769  424 LYS B N   
7632  C CA  . LYS B 424 ? 0.5944 0.3699 0.6618 -0.0977 0.0437  0.0779  424 LYS B CA  
7633  C C   . LYS B 424 ? 0.5636 0.3301 0.6201 -0.0866 0.0403  0.0810  424 LYS B C   
7634  O O   . LYS B 424 ? 0.5430 0.3244 0.6043 -0.0802 0.0396  0.0797  424 LYS B O   
7635  C CB  . LYS B 424 ? 0.6499 0.4285 0.7126 -0.1090 0.0508  0.0823  424 LYS B CB  
7636  C CG  . LYS B 424 ? 0.7168 0.5144 0.7940 -0.1198 0.0550  0.0793  424 LYS B CG  
7637  C CD  . LYS B 424 ? 0.7812 0.5853 0.8558 -0.1310 0.0627  0.0835  424 LYS B CD  
7638  C CE  . LYS B 424 ? 0.8151 0.6366 0.9042 -0.1423 0.0660  0.0807  424 LYS B CE  
7639  N NZ  . LYS B 424 ? 0.8772 0.6971 0.9603 -0.1554 0.0730  0.0858  424 LYS B NZ  
7640  N N   . ASP B 425 ? 0.5613 0.3030 0.6018 -0.0846 0.0383  0.0855  425 ASP B N   
7641  C CA  . ASP B 425 ? 0.5539 0.2871 0.5827 -0.0748 0.0351  0.0894  425 ASP B CA  
7642  C C   . ASP B 425 ? 0.5714 0.2842 0.5930 -0.0668 0.0295  0.0901  425 ASP B C   
7643  O O   . ASP B 425 ? 0.5988 0.2897 0.6091 -0.0714 0.0305  0.0933  425 ASP B O   
7644  C CB  . ASP B 425 ? 0.5632 0.2874 0.5764 -0.0804 0.0397  0.0963  425 ASP B CB  
7645  C CG  . ASP B 425 ? 0.5744 0.2907 0.5742 -0.0707 0.0362  0.1007  425 ASP B CG  
7646  O OD1 . ASP B 425 ? 0.5780 0.2939 0.5805 -0.0596 0.0296  0.0986  425 ASP B OD1 
7647  O OD2 . ASP B 425 ? 0.5915 0.3035 0.5787 -0.0743 0.0399  0.1060  425 ASP B OD2 
7648  N N   . LEU B 426 ? 0.5524 0.2716 0.5792 -0.0548 0.0237  0.0876  426 LEU B N   
7649  C CA  . LEU B 426 ? 0.5809 0.2846 0.6038 -0.0457 0.0184  0.0875  426 LEU B CA  
7650  C C   . LEU B 426 ? 0.5992 0.2790 0.6019 -0.0418 0.0169  0.0950  426 LEU B C   
7651  O O   . LEU B 426 ? 0.5957 0.2586 0.5925 -0.0350 0.0134  0.0958  426 LEU B O   
7652  C CB  . LEU B 426 ? 0.5594 0.2780 0.5946 -0.0344 0.0130  0.0828  426 LEU B CB  
7653  C CG  . LEU B 426 ? 0.5471 0.2874 0.6014 -0.0369 0.0138  0.0756  426 LEU B CG  
7654  C CD1 . LEU B 426 ? 0.5228 0.2778 0.5881 -0.0263 0.0088  0.0718  426 LEU B CD1 
7655  C CD2 . LEU B 426 ? 0.5548 0.2877 0.6128 -0.0428 0.0155  0.0725  426 LEU B CD2 
7656  N N   . ASN B 427 ? 0.6122 0.2898 0.6037 -0.0459 0.0199  0.1004  427 ASN B N   
7657  C CA  . ASN B 427 ? 0.6598 0.3146 0.6308 -0.0422 0.0184  0.1080  427 ASN B CA  
7658  C C   . ASN B 427 ? 0.6849 0.3145 0.6430 -0.0511 0.0224  0.1120  427 ASN B C   
7659  O O   . ASN B 427 ? 0.7025 0.3105 0.6420 -0.0490 0.0218  0.1189  427 ASN B O   
7660  C CB  . ASN B 427 ? 0.6517 0.3113 0.6128 -0.0427 0.0198  0.1128  427 ASN B CB  
7661  C CG  . ASN B 427 ? 0.6335 0.3103 0.6010 -0.0321 0.0142  0.1106  427 ASN B CG  
7662  O OD1 . ASN B 427 ? 0.6079 0.2834 0.5787 -0.0213 0.0078  0.1093  427 ASN B OD1 
7663  N ND2 . ASN B 427 ? 0.6111 0.3046 0.5806 -0.0351 0.0168  0.1098  427 ASN B ND2 
7664  N N   . GLU B 428 ? 0.7109 0.3436 0.6779 -0.0616 0.0264  0.1079  428 GLU B N   
7665  C CA  . GLU B 428 ? 0.7433 0.3529 0.6988 -0.0722 0.0304  0.1109  428 GLU B CA  
7666  C C   . GLU B 428 ? 0.7403 0.3278 0.6907 -0.0655 0.0263  0.1096  428 GLU B C   
7667  O O   . GLU B 428 ? 0.7831 0.3447 0.7196 -0.0715 0.0283  0.1129  428 GLU B O   
7668  C CB  . GLU B 428 ? 0.7793 0.3993 0.7452 -0.0874 0.0360  0.1072  428 GLU B CB  
7669  C CG  . GLU B 428 ? 0.8258 0.4713 0.8009 -0.0952 0.0411  0.1068  428 GLU B CG  
7670  C CD  . GLU B 428 ? 0.8917 0.5320 0.8529 -0.1023 0.0466  0.1141  428 GLU B CD  
7671  O OE1 . GLU B 428 ? 0.9917 0.6056 0.9331 -0.1025 0.0468  0.1208  428 GLU B OE1 
7672  O OE2 . GLU B 428 ? 0.8588 0.5217 0.8287 -0.1075 0.0511  0.1131  428 GLU B OE2 
7673  N N   . GLY B 429 ? 0.7123 0.3088 0.6732 -0.0533 0.0209  0.1049  429 GLY B N   
7674  C CA  . GLY B 429 ? 0.7247 0.2993 0.6789 -0.0450 0.0172  0.1043  429 GLY B CA  
7675  C C   . GLY B 429 ? 0.6954 0.2824 0.6602 -0.0294 0.0112  0.1007  429 GLY B C   
7676  O O   . GLY B 429 ? 0.6767 0.2905 0.6567 -0.0268 0.0098  0.0970  429 GLY B O   
7677  N N   . LYS B 430 ? 0.7076 0.2741 0.6641 -0.0193 0.0078  0.1017  430 LYS B N   
7678  C CA  . LYS B 430 ? 0.7102 0.2862 0.6761 -0.0043 0.0024  0.0984  430 LYS B CA  
7679  C C   . LYS B 430 ? 0.6601 0.2417 0.6388 -0.0048 0.0028  0.0903  430 LYS B C   
7680  O O   . LYS B 430 ? 0.6244 0.2207 0.6155 0.0054  -0.0006 0.0861  430 LYS B O   
7681  C CB  . LYS B 430 ? 0.7949 0.3467 0.7448 0.0082  -0.0014 0.1044  430 LYS B CB  
7682  C CG  . LYS B 430 ? 0.8714 0.4221 0.8104 0.0129  -0.0039 0.1121  430 LYS B CG  
7683  C CD  . LYS B 430 ? 0.9910 0.5166 0.9137 0.0261  -0.0080 0.1182  430 LYS B CD  
7684  C CE  . LYS B 430 ? 1.0321 0.5569 0.9436 0.0326  -0.0117 0.1260  430 LYS B CE  
7685  N NZ  . LYS B 430 ? 1.0315 0.5894 0.9592 0.0361  -0.0151 0.1229  430 LYS B NZ  
7686  N N   . ILE B 431 ? 0.6491 0.2195 0.6246 -0.0172 0.0071  0.0881  431 ILE B N   
7687  C CA  . ILE B 431 ? 0.6247 0.1972 0.6093 -0.0195 0.0078  0.0805  431 ILE B CA  
7688  C C   . ILE B 431 ? 0.5953 0.1874 0.5920 -0.0340 0.0114  0.0765  431 ILE B C   
7689  O O   . ILE B 431 ? 0.5934 0.1831 0.5846 -0.0458 0.0150  0.0799  431 ILE B O   
7690  C CB  . ILE B 431 ? 0.6492 0.1877 0.6175 -0.0206 0.0089  0.0810  431 ILE B CB  
7691  C CG1 . ILE B 431 ? 0.6814 0.1997 0.6373 -0.0050 0.0054  0.0854  431 ILE B CG1 
7692  C CG2 . ILE B 431 ? 0.6382 0.1786 0.6147 -0.0236 0.0096  0.0728  431 ILE B CG2 
7693  C CD1 . ILE B 431 ? 0.7166 0.1972 0.6533 -0.0049 0.0067  0.0869  431 ILE B CD1 
7694  N N   . ALA B 432 ? 0.5734 0.1842 0.5859 -0.0331 0.0106  0.0694  432 ALA B N   
7695  C CA  . ALA B 432 ? 0.5606 0.1907 0.5854 -0.0454 0.0133  0.0651  432 ALA B CA  
7696  C C   . ALA B 432 ? 0.5670 0.1887 0.5927 -0.0508 0.0140  0.0592  432 ALA B C   
7697  O O   . ALA B 432 ? 0.5782 0.1836 0.5979 -0.0428 0.0121  0.0572  432 ALA B O   
7698  C CB  . ALA B 432 ? 0.5333 0.1945 0.5759 -0.0404 0.0117  0.0621  432 ALA B CB  
7699  N N   . SER B 433 ? 0.5737 0.2062 0.6061 -0.0644 0.0166  0.0566  433 SER B N   
7700  C CA  . SER B 433 ? 0.5934 0.2248 0.6298 -0.0699 0.0165  0.0499  433 SER B CA  
7701  C C   . SER B 433 ? 0.5778 0.2398 0.6322 -0.0767 0.0172  0.0459  433 SER B C   
7702  O O   . SER B 433 ? 0.5803 0.2602 0.6418 -0.0804 0.0188  0.0486  433 SER B O   
7703  C CB  . SER B 433 ? 0.6150 0.2199 0.6367 -0.0813 0.0186  0.0506  433 SER B CB  
7704  O OG  . SER B 433 ? 0.6166 0.2312 0.6415 -0.0966 0.0218  0.0523  433 SER B OG  
7705  N N   . ILE B 434 ? 0.5906 0.2582 0.6519 -0.0775 0.0158  0.0394  434 ILE B N   
7706  C CA  . ILE B 434 ? 0.5576 0.2506 0.6339 -0.0853 0.0162  0.0354  434 ILE B CA  
7707  C C   . ILE B 434 ? 0.5720 0.2543 0.6442 -0.0957 0.0162  0.0308  434 ILE B C   
7708  O O   . ILE B 434 ? 0.5677 0.2366 0.6346 -0.0908 0.0144  0.0266  434 ILE B O   
7709  C CB  . ILE B 434 ? 0.5215 0.2365 0.6120 -0.0750 0.0139  0.0317  434 ILE B CB  
7710  C CG1 . ILE B 434 ? 0.5017 0.2291 0.5971 -0.0655 0.0135  0.0355  434 ILE B CG1 
7711  C CG2 . ILE B 434 ? 0.5182 0.2562 0.6223 -0.0829 0.0140  0.0276  434 ILE B CG2 
7712  C CD1 . ILE B 434 ? 0.4680 0.2125 0.5751 -0.0548 0.0111  0.0321  434 ILE B CD1 
7713  N N   . LYS B 435 ? 0.5836 0.2720 0.6579 -0.1103 0.0183  0.0316  435 LYS B N   
7714  C CA  . LYS B 435 ? 0.5836 0.2662 0.6558 -0.1227 0.0180  0.0273  435 LYS B CA  
7715  C C   . LYS B 435 ? 0.5700 0.2827 0.6597 -0.1253 0.0165  0.0228  435 LYS B C   
7716  O O   . LYS B 435 ? 0.5606 0.2969 0.6623 -0.1286 0.0180  0.0249  435 LYS B O   
7717  C CB  . LYS B 435 ? 0.6135 0.2857 0.6779 -0.1374 0.0211  0.0314  435 LYS B CB  
7718  C CG  . LYS B 435 ? 0.6815 0.3183 0.7255 -0.1361 0.0220  0.0348  435 LYS B CG  
7719  C CD  . LYS B 435 ? 0.7268 0.3502 0.7614 -0.1525 0.0253  0.0386  435 LYS B CD  
7720  C CE  . LYS B 435 ? 0.7465 0.3875 0.7876 -0.1557 0.0287  0.0447  435 LYS B CE  
7721  N NZ  . LYS B 435 ? 0.8160 0.4396 0.8450 -0.1701 0.0324  0.0493  435 LYS B NZ  
7722  N N   . THR B 436 ? 0.5742 0.2855 0.6647 -0.1220 0.0137  0.0168  436 THR B N   
7723  C CA  . THR B 436 ? 0.5459 0.2832 0.6512 -0.1236 0.0118  0.0124  436 THR B CA  
7724  C C   . THR B 436 ? 0.5648 0.3010 0.6688 -0.1391 0.0110  0.0092  436 THR B C   
7725  O O   . THR B 436 ? 0.5897 0.3003 0.6794 -0.1447 0.0107  0.0074  436 THR B O   
7726  C CB  . THR B 436 ? 0.5296 0.2669 0.6361 -0.1109 0.0093  0.0080  436 THR B CB  
7727  O OG1 . THR B 436 ? 0.5178 0.2594 0.6272 -0.0988 0.0101  0.0119  436 THR B OG1 
7728  C CG2 . THR B 436 ? 0.5016 0.2635 0.6215 -0.1121 0.0071  0.0036  436 THR B CG2 
7729  N N   . LYS B 437 ? 0.5449 0.3093 0.6639 -0.1456 0.0107  0.0086  437 LYS B N   
7730  C CA  . LYS B 437 ? 0.5680 0.3395 0.6900 -0.1600 0.0090  0.0052  437 LYS B CA  
7731  C C   . LYS B 437 ? 0.5428 0.3409 0.6791 -0.1568 0.0059  0.0011  437 LYS B C   
7732  O O   . LYS B 437 ? 0.4971 0.3200 0.6474 -0.1522 0.0066  0.0033  437 LYS B O   
7733  C CB  . LYS B 437 ? 0.6028 0.3825 0.7286 -0.1721 0.0124  0.0101  437 LYS B CB  
7734  C CG  . LYS B 437 ? 0.6486 0.4395 0.7797 -0.1883 0.0110  0.0075  437 LYS B CG  
7735  C CD  . LYS B 437 ? 0.6997 0.4988 0.8346 -0.2011 0.0149  0.0125  437 LYS B CD  
7736  C CE  . LYS B 437 ? 0.7584 0.5762 0.9030 -0.2158 0.0128  0.0095  437 LYS B CE  
7737  N NZ  . LYS B 437 ? 0.8105 0.6412 0.9615 -0.2285 0.0168  0.0141  437 LYS B NZ  
7738  N N   . ILE B 438 ? 0.5513 0.3427 0.6828 -0.1591 0.0023  -0.0048 438 ILE B N   
7739  C CA  . ILE B 438 ? 0.5590 0.3737 0.7021 -0.1580 -0.0011 -0.0087 438 ILE B CA  
7740  C C   . ILE B 438 ? 0.6059 0.4275 0.7506 -0.1736 -0.0039 -0.0119 438 ILE B C   
7741  O O   . ILE B 438 ? 0.6531 0.4542 0.7849 -0.1807 -0.0058 -0.0161 438 ILE B O   
7742  C CB  . ILE B 438 ? 0.5599 0.3658 0.6974 -0.1463 -0.0032 -0.0131 438 ILE B CB  
7743  C CG1 . ILE B 438 ? 0.5395 0.3385 0.6754 -0.1313 -0.0008 -0.0102 438 ILE B CG1 
7744  C CG2 . ILE B 438 ? 0.5382 0.3692 0.6874 -0.1449 -0.0066 -0.0163 438 ILE B CG2 
7745  C CD1 . ILE B 438 ? 0.5430 0.3310 0.6722 -0.1203 -0.0021 -0.0144 438 ILE B CD1 
7746  N N   . GLU B 439 ? 0.6016 0.4534 0.7626 -0.1783 -0.0044 -0.0102 439 GLU B N   
7747  C CA  . GLU B 439 ? 0.5952 0.4620 0.7622 -0.1917 -0.0079 -0.0132 439 GLU B CA  
7748  C C   . GLU B 439 ? 0.5485 0.4278 0.7197 -0.1856 -0.0127 -0.0179 439 GLU B C   
7749  O O   . GLU B 439 ? 0.5291 0.4267 0.7108 -0.1745 -0.0127 -0.0165 439 GLU B O   
7750  C CB  . GLU B 439 ? 0.6285 0.5229 0.8116 -0.1983 -0.0059 -0.0087 439 GLU B CB  
7751  C CG  . GLU B 439 ? 0.6782 0.5604 0.8559 -0.2081 -0.0013 -0.0044 439 GLU B CG  
7752  C CD  . GLU B 439 ? 0.6986 0.6082 0.8918 -0.2158 0.0015  -0.0001 439 GLU B CD  
7753  O OE1 . GLU B 439 ? 0.7157 0.6545 0.9251 -0.2097 0.0013  0.0010  439 GLU B OE1 
7754  O OE2 . GLU B 439 ? 0.7346 0.6346 0.9226 -0.2284 0.0042  0.0022  439 GLU B OE2 
7755  N N   . THR B 440 ? 0.5410 0.4084 0.7024 -0.1929 -0.0167 -0.0236 440 THR B N   
7756  C CA  . THR B 440 ? 0.5284 0.4019 0.6894 -0.1869 -0.0211 -0.0284 440 THR B CA  
7757  C C   . THR B 440 ? 0.5243 0.4287 0.6997 -0.1946 -0.0253 -0.0291 440 THR B C   
7758  O O   . THR B 440 ? 0.4797 0.3960 0.6624 -0.2069 -0.0253 -0.0272 440 THR B O   
7759  C CB  . THR B 440 ? 0.5298 0.3742 0.6717 -0.1900 -0.0232 -0.0345 440 THR B CB  
7760  O OG1 . THR B 440 ? 0.5311 0.3681 0.6681 -0.2072 -0.0244 -0.0358 440 THR B OG1 
7761  C CG2 . THR B 440 ? 0.5328 0.3480 0.6611 -0.1798 -0.0192 -0.0340 440 THR B CG2 
7762  N N   . SER B 441 ? 0.5490 0.4667 0.7284 -0.1869 -0.0289 -0.0315 441 SER B N   
7763  C CA  . SER B 441 ? 0.5868 0.5329 0.7784 -0.1931 -0.0339 -0.0324 441 SER B CA  
7764  C C   . SER B 441 ? 0.6270 0.5694 0.8102 -0.1909 -0.0392 -0.0382 441 SER B C   
7765  O O   . SER B 441 ? 0.6255 0.5539 0.7999 -0.1794 -0.0381 -0.0399 441 SER B O   
7766  C CB  . SER B 441 ? 0.5698 0.5450 0.7800 -0.1851 -0.0322 -0.0272 441 SER B CB  
7767  O OG  . SER B 441 ? 0.5795 0.5829 0.8025 -0.1923 -0.0367 -0.0273 441 SER B OG  
7768  N N   . GLU B 442 ? 0.6943 0.6501 0.8801 -0.2025 -0.0450 -0.0412 442 GLU B N   
7769  C CA  . GLU B 442 ? 0.7756 0.7191 0.9474 -0.2061 -0.0502 -0.0480 442 GLU B CA  
7770  C C   . GLU B 442 ? 0.7390 0.6884 0.9104 -0.1913 -0.0514 -0.0487 442 GLU B C   
7771  O O   . GLU B 442 ? 0.7473 0.6762 0.9032 -0.1870 -0.0519 -0.0533 442 GLU B O   
7772  C CB  . GLU B 442 ? 0.8729 0.8321 1.0488 -0.2223 -0.0566 -0.0507 442 GLU B CB  
7773  C CG  . GLU B 442 ? 0.9515 0.8929 1.1095 -0.2292 -0.0619 -0.0584 442 GLU B CG  
7774  C CD  . GLU B 442 ? 1.0259 0.9896 1.1904 -0.2432 -0.0697 -0.0609 442 GLU B CD  
7775  O OE1 . GLU B 442 ? 1.0538 1.0181 1.2199 -0.2595 -0.0709 -0.0615 442 GLU B OE1 
7776  O OE2 . GLU B 442 ? 0.9863 0.9686 1.1552 -0.2375 -0.0746 -0.0618 442 GLU B OE2 
7777  N N   . ASN B 443 ? 0.6856 0.6615 0.8733 -0.1831 -0.0513 -0.0441 443 ASN B N   
7778  C CA  . ASN B 443 ? 0.7176 0.7021 0.9055 -0.1713 -0.0534 -0.0446 443 ASN B CA  
7779  C C   . ASN B 443 ? 0.6754 0.6450 0.8584 -0.1563 -0.0477 -0.0429 443 ASN B C   
7780  O O   . ASN B 443 ? 0.6532 0.6247 0.8334 -0.1465 -0.0485 -0.0437 443 ASN B O   
7781  C CB  . ASN B 443 ? 0.8005 0.8194 1.0066 -0.1701 -0.0567 -0.0408 443 ASN B CB  
7782  C CG  . ASN B 443 ? 0.8208 0.8561 1.0325 -0.1852 -0.0625 -0.0425 443 ASN B CG  
7783  O OD1 . ASN B 443 ? 0.7228 0.7827 0.9513 -0.1886 -0.0627 -0.0385 443 ASN B OD1 
7784  N ND2 . ASN B 443 ? 0.7862 0.8092 0.9845 -0.1944 -0.0674 -0.0485 443 ASN B ND2 
7785  N N   . PHE B 444 ? 0.6044 0.5593 0.7862 -0.1548 -0.0420 -0.0405 444 PHE B N   
7786  C CA  . PHE B 444 ? 0.5142 0.4587 0.6943 -0.1412 -0.0368 -0.0381 444 PHE B CA  
7787  C C   . PHE B 444 ? 0.5201 0.4333 0.6827 -0.1398 -0.0344 -0.0419 444 PHE B C   
7788  O O   . PHE B 444 ? 0.5290 0.4262 0.6836 -0.1494 -0.0342 -0.0437 444 PHE B O   
7789  C CB  . PHE B 444 ? 0.4860 0.4391 0.6780 -0.1395 -0.0325 -0.0322 444 PHE B CB  
7790  C CG  . PHE B 444 ? 0.4467 0.4304 0.6558 -0.1383 -0.0341 -0.0285 444 PHE B CG  
7791  C CD1 . PHE B 444 ? 0.4566 0.4581 0.6742 -0.1496 -0.0374 -0.0283 444 PHE B CD1 
7792  C CD2 . PHE B 444 ? 0.4366 0.4313 0.6529 -0.1257 -0.0325 -0.0255 444 PHE B CD2 
7793  C CE1 . PHE B 444 ? 0.4284 0.4584 0.6618 -0.1472 -0.0388 -0.0250 444 PHE B CE1 
7794  C CE2 . PHE B 444 ? 0.4212 0.4423 0.6519 -0.1236 -0.0340 -0.0224 444 PHE B CE2 
7795  C CZ  . PHE B 444 ? 0.4224 0.4613 0.6617 -0.1339 -0.0372 -0.0221 444 PHE B CZ  
7796  N N   . THR B 445 ? 0.5104 0.4153 0.6677 -0.1276 -0.0322 -0.0426 445 THR B N   
7797  C CA  . THR B 445 ? 0.5559 0.4330 0.6980 -0.1234 -0.0293 -0.0458 445 THR B CA  
7798  C C   . THR B 445 ? 0.5702 0.4407 0.7158 -0.1142 -0.0240 -0.0414 445 THR B C   
7799  O O   . THR B 445 ? 0.5186 0.4035 0.6744 -0.1053 -0.0224 -0.0377 445 THR B O   
7800  C CB  . THR B 445 ? 0.5543 0.4279 0.6880 -0.1161 -0.0304 -0.0499 445 THR B CB  
7801  O OG1 . THR B 445 ? 0.5717 0.4503 0.7013 -0.1267 -0.0359 -0.0539 445 THR B OG1 
7802  C CG2 . THR B 445 ? 0.5827 0.4287 0.7008 -0.1105 -0.0270 -0.0536 445 THR B CG2 
7803  N N   . LEU B 446 ? 0.6237 0.4710 0.7594 -0.1165 -0.0215 -0.0420 446 LEU B N   
7804  C CA  . LEU B 446 ? 0.6355 0.4718 0.7707 -0.1075 -0.0169 -0.0385 446 LEU B CA  
7805  C C   . LEU B 446 ? 0.6341 0.4551 0.7593 -0.0966 -0.0150 -0.0417 446 LEU B C   
7806  O O   . LEU B 446 ? 0.6582 0.4621 0.7698 -0.0990 -0.0159 -0.0470 446 LEU B O   
7807  C CB  . LEU B 446 ? 0.6599 0.4774 0.7878 -0.1156 -0.0155 -0.0375 446 LEU B CB  
7808  C CG  . LEU B 446 ? 0.6384 0.4695 0.7756 -0.1271 -0.0163 -0.0340 446 LEU B CG  
7809  C CD1 . LEU B 446 ? 0.6527 0.4607 0.7798 -0.1337 -0.0141 -0.0328 446 LEU B CD1 
7810  C CD2 . LEU B 446 ? 0.6329 0.4874 0.7863 -0.1215 -0.0147 -0.0284 446 LEU B CD2 
7811  N N   . LEU B 447 ? 0.6428 0.4689 0.7742 -0.0848 -0.0120 -0.0384 447 LEU B N   
7812  C CA  . LEU B 447 ? 0.7785 0.5959 0.9038 -0.0736 -0.0099 -0.0408 447 LEU B CA  
7813  C C   . LEU B 447 ? 0.9441 0.7416 1.0629 -0.0671 -0.0064 -0.0395 447 LEU B C   
7814  O O   . LEU B 447 ? 1.1530 0.9488 1.2754 -0.0685 -0.0054 -0.0352 447 LEU B O   
7815  C CB  . LEU B 447 ? 0.7227 0.5612 0.8600 -0.0651 -0.0092 -0.0382 447 LEU B CB  
7816  C CG  . LEU B 447 ? 0.7146 0.5721 0.8573 -0.0689 -0.0125 -0.0392 447 LEU B CG  
7817  C CD1 . LEU B 447 ? 0.7448 0.6190 0.8976 -0.0596 -0.0111 -0.0362 447 LEU B CD1 
7818  C CD2 . LEU B 447 ? 0.7258 0.5740 0.8559 -0.0723 -0.0146 -0.0454 447 LEU B CD2 
7819  N N   . ASP B 448 ? 0.9836 0.7661 1.0921 -0.0595 -0.0045 -0.0433 448 ASP B N   
7820  C CA  . ASP B 448 ? 1.0118 0.7823 1.1176 -0.0484 -0.0010 -0.0417 448 ASP B CA  
7821  C C   . ASP B 448 ? 0.8407 0.5985 0.9443 -0.0517 -0.0005 -0.0379 448 ASP B C   
7822  O O   . ASP B 448 ? 0.8627 0.6045 0.9562 -0.0608 -0.0016 -0.0398 448 ASP B O   
7823  C CB  . ASP B 448 ? 1.0260 0.8151 1.1445 -0.0379 0.0006  -0.0384 448 ASP B CB  
7824  C CG  . ASP B 448 ? 0.9683 0.7699 1.0892 -0.0333 0.0010  -0.0411 448 ASP B CG  
7825  O OD1 . ASP B 448 ? 0.8496 0.6395 0.9592 -0.0317 0.0017  -0.0464 448 ASP B OD1 
7826  O OD2 . ASP B 448 ? 0.9262 0.7483 1.0596 -0.0307 0.0008  -0.0379 448 ASP B OD2 
7827  N N   . ASP B 449 ? 0.7970 0.5636 0.9101 -0.0453 0.0008  -0.0324 449 ASP B N   
7828  C CA  . ASP B 449 ? 0.8277 0.5807 0.9373 -0.0444 0.0020  -0.0283 449 ASP B CA  
7829  C C   . ASP B 449 ? 0.7129 0.4820 0.8339 -0.0492 0.0014  -0.0227 449 ASP B C   
7830  O O   . ASP B 449 ? 0.6268 0.4171 0.7604 -0.0455 0.0013  -0.0205 449 ASP B O   
7831  C CB  . ASP B 449 ? 0.8273 0.5705 0.9341 -0.0308 0.0044  -0.0271 449 ASP B CB  
7832  C CG  . ASP B 449 ? 0.8667 0.5841 0.9578 -0.0263 0.0058  -0.0315 449 ASP B CG  
7833  O OD1 . ASP B 449 ? 0.8042 0.5085 0.8847 -0.0347 0.0049  -0.0360 449 ASP B OD1 
7834  O OD2 . ASP B 449 ? 0.8875 0.5985 0.9771 -0.0142 0.0078  -0.0307 449 ASP B OD2 
7835  N N   . LEU B 450 ? 0.6694 0.4261 0.7843 -0.0578 0.0013  -0.0208 450 LEU B N   
7836  C CA  . LEU B 450 ? 0.6055 0.3686 0.7263 -0.0604 0.0019  -0.0149 450 LEU B CA  
7837  C C   . LEU B 450 ? 0.5826 0.3437 0.7049 -0.0481 0.0033  -0.0112 450 LEU B C   
7838  O O   . LEU B 450 ? 0.6110 0.3532 0.7236 -0.0410 0.0042  -0.0120 450 LEU B O   
7839  C CB  . LEU B 450 ? 0.6151 0.3589 0.7249 -0.0711 0.0021  -0.0143 450 LEU B CB  
7840  C CG  . LEU B 450 ? 0.6419 0.3880 0.7545 -0.0752 0.0034  -0.0081 450 LEU B CG  
7841  C CD1 . LEU B 450 ? 0.6023 0.3763 0.7301 -0.0797 0.0030  -0.0059 450 LEU B CD1 
7842  C CD2 . LEU B 450 ? 0.7209 0.4454 0.8209 -0.0865 0.0039  -0.0078 450 LEU B CD2 
7843  N N   . LYS B 451 ? 0.5191 0.2999 0.6535 -0.0456 0.0034  -0.0074 451 LYS B N   
7844  C CA  . LYS B 451 ? 0.5181 0.2998 0.6549 -0.0356 0.0041  -0.0034 451 LYS B CA  
7845  C C   . LYS B 451 ? 0.4996 0.2813 0.6366 -0.0400 0.0046  0.0020  451 LYS B C   
7846  O O   . LYS B 451 ? 0.4628 0.2552 0.6047 -0.0490 0.0048  0.0030  451 LYS B O   
7847  C CB  . LYS B 451 ? 0.5395 0.3428 0.6888 -0.0285 0.0037  -0.0040 451 LYS B CB  
7848  C CG  . LYS B 451 ? 0.5959 0.3984 0.7439 -0.0237 0.0038  -0.0090 451 LYS B CG  
7849  C CD  . LYS B 451 ? 0.6609 0.4727 0.8156 -0.0122 0.0043  -0.0084 451 LYS B CD  
7850  C CE  . LYS B 451 ? 0.7053 0.5155 0.8578 -0.0069 0.0052  -0.0131 451 LYS B CE  
7851  N NZ  . LYS B 451 ? 0.6760 0.5010 0.8342 -0.0124 0.0045  -0.0154 451 LYS B NZ  
7852  N N   . ILE B 452 ? 0.4855 0.2547 0.6164 -0.0332 0.0050  0.0056  452 ILE B N   
7853  C CA  . ILE B 452 ? 0.4780 0.2430 0.6057 -0.0365 0.0057  0.0110  452 ILE B CA  
7854  C C   . ILE B 452 ? 0.4677 0.2404 0.5999 -0.0261 0.0050  0.0145  452 ILE B C   
7855  O O   . ILE B 452 ? 0.4929 0.2617 0.6244 -0.0160 0.0042  0.0135  452 ILE B O   
7856  C CB  . ILE B 452 ? 0.5214 0.2585 0.6333 -0.0391 0.0064  0.0124  452 ILE B CB  
7857  C CG1 . ILE B 452 ? 0.5490 0.2729 0.6536 -0.0461 0.0065  0.0073  452 ILE B CG1 
7858  C CG2 . ILE B 452 ? 0.5286 0.2616 0.6364 -0.0462 0.0076  0.0179  452 ILE B CG2 
7859  C CD1 . ILE B 452 ? 0.5476 0.2800 0.6556 -0.0606 0.0068  0.0063  452 ILE B CD1 
7860  N N   . SER B 453 ? 0.4563 0.2397 0.5929 -0.0283 0.0053  0.0184  453 SER B N   
7861  C CA  . SER B 453 ? 0.4386 0.2301 0.5793 -0.0194 0.0041  0.0214  453 SER B CA  
7862  C C   . SER B 453 ? 0.4449 0.2312 0.5795 -0.0222 0.0047  0.0268  453 SER B C   
7863  O O   . SER B 453 ? 0.4208 0.2122 0.5564 -0.0314 0.0065  0.0279  453 SER B O   
7864  C CB  . SER B 453 ? 0.4318 0.2467 0.5859 -0.0179 0.0037  0.0197  453 SER B CB  
7865  O OG  . SER B 453 ? 0.4205 0.2426 0.5774 -0.0112 0.0024  0.0227  453 SER B OG  
7866  N N   . TYR B 454 ? 0.4657 0.2422 0.5939 -0.0140 0.0033  0.0303  454 TYR B N   
7867  C CA  . TYR B 454 ? 0.4615 0.2332 0.5829 -0.0150 0.0034  0.0359  454 TYR B CA  
7868  C C   . TYR B 454 ? 0.4383 0.2231 0.5656 -0.0059 0.0009  0.0374  454 TYR B C   
7869  O O   . TYR B 454 ? 0.4371 0.2140 0.5597 0.0029  -0.0015 0.0396  454 TYR B O   
7870  C CB  . TYR B 454 ? 0.4656 0.2107 0.5711 -0.0155 0.0038  0.0392  454 TYR B CB  
7871  C CG  . TYR B 454 ? 0.4678 0.2052 0.5639 -0.0201 0.0050  0.0452  454 TYR B CG  
7872  C CD1 . TYR B 454 ? 0.4751 0.2135 0.5697 -0.0325 0.0083  0.0463  454 TYR B CD1 
7873  C CD2 . TYR B 454 ? 0.4746 0.2035 0.5627 -0.0122 0.0030  0.0501  454 TYR B CD2 
7874  C CE1 . TYR B 454 ? 0.4966 0.2278 0.5819 -0.0369 0.0101  0.0519  454 TYR B CE1 
7875  C CE2 . TYR B 454 ? 0.4886 0.2096 0.5666 -0.0163 0.0042  0.0558  454 TYR B CE2 
7876  C CZ  . TYR B 454 ? 0.5056 0.2275 0.5820 -0.0288 0.0080  0.0568  454 TYR B CZ  
7877  O OH  . TYR B 454 ? 0.5162 0.2305 0.5820 -0.0328 0.0098  0.0626  454 TYR B OH  
7878  N N   . ASN B 455 ? 0.4262 0.2313 0.5640 -0.0081 0.0012  0.0361  455 ASN B N   
7879  C CA  . ASN B 455 ? 0.4115 0.2302 0.5562 -0.0005 -0.0014 0.0363  455 ASN B CA  
7880  C C   . ASN B 455 ? 0.4052 0.2223 0.5432 -0.0001 -0.0023 0.0412  455 ASN B C   
7881  O O   . ASN B 455 ? 0.4028 0.2273 0.5416 -0.0061 -0.0003 0.0421  455 ASN B O   
7882  C CB  . ASN B 455 ? 0.4047 0.2436 0.5625 -0.0021 -0.0010 0.0324  455 ASN B CB  
7883  C CG  . ASN B 455 ? 0.4039 0.2550 0.5681 0.0052  -0.0038 0.0324  455 ASN B CG  
7884  O OD1 . ASN B 455 ? 0.4206 0.2673 0.5795 0.0103  -0.0062 0.0357  455 ASN B OD1 
7885  N ND2 . ASN B 455 ? 0.3776 0.2437 0.5525 0.0054  -0.0037 0.0289  455 ASN B ND2 
7886  N N   . THR B 456 ? 0.4128 0.2213 0.5445 0.0078  -0.0053 0.0443  456 THR B N   
7887  C CA  . THR B 456 ? 0.4109 0.2129 0.5325 0.0085  -0.0064 0.0496  456 THR B CA  
7888  C C   . THR B 456 ? 0.3927 0.2112 0.5200 0.0121  -0.0091 0.0497  456 THR B C   
7889  O O   . THR B 456 ? 0.4036 0.2185 0.5226 0.0134  -0.0107 0.0538  456 THR B O   
7890  C CB  . THR B 456 ? 0.4208 0.2039 0.5316 0.0158  -0.0087 0.0531  456 THR B CB  
7891  O OG1 . THR B 456 ? 0.3948 0.1848 0.5141 0.0248  -0.0115 0.0502  456 THR B OG1 
7892  C CG2 . THR B 456 ? 0.4348 0.1974 0.5360 0.0105  -0.0056 0.0537  456 THR B CG2 
7893  N N   . HIS B 457 ? 0.3884 0.2238 0.5287 0.0134  -0.0097 0.0453  457 HIS B N   
7894  C CA  . HIS B 457 ? 0.3814 0.2324 0.5272 0.0144  -0.0116 0.0447  457 HIS B CA  
7895  C C   . HIS B 457 ? 0.4041 0.2560 0.5470 0.0223  -0.0168 0.0474  457 HIS B C   
7896  O O   . HIS B 457 ? 0.4384 0.2973 0.5796 0.0217  -0.0184 0.0484  457 HIS B O   
7897  C CB  . HIS B 457 ? 0.3682 0.2209 0.5094 0.0069  -0.0085 0.0460  457 HIS B CB  
7898  C CG  . HIS B 457 ? 0.3772 0.2374 0.5257 -0.0002 -0.0043 0.0426  457 HIS B CG  
7899  N ND1 . HIS B 457 ? 0.3616 0.2146 0.5101 -0.0047 -0.0015 0.0417  457 HIS B ND1 
7900  C CD2 . HIS B 457 ? 0.3484 0.2229 0.5045 -0.0032 -0.0026 0.0398  457 HIS B CD2 
7901  C CE1 . HIS B 457 ? 0.3606 0.2248 0.5170 -0.0100 0.0014  0.0386  457 HIS B CE1 
7902  N NE2 . HIS B 457 ? 0.3429 0.2198 0.5040 -0.0088 0.0009  0.0376  457 HIS B NE2 
7903  N N   . LEU B 458 ? 0.4228 0.2675 0.5644 0.0298  -0.0194 0.0486  458 LEU B N   
7904  C CA  . LEU B 458 ? 0.4372 0.2858 0.5785 0.0383  -0.0248 0.0509  458 LEU B CA  
7905  C C   . LEU B 458 ? 0.4292 0.2975 0.5851 0.0410  -0.0270 0.0469  458 LEU B C   
7906  O O   . LEU B 458 ? 0.4134 0.2853 0.5776 0.0451  -0.0267 0.0444  458 LEU B O   
7907  C CB  . LEU B 458 ? 0.4349 0.2689 0.5699 0.0462  -0.0265 0.0538  458 LEU B CB  
7908  C CG  . LEU B 458 ? 0.4509 0.2625 0.5703 0.0433  -0.0242 0.0580  458 LEU B CG  
7909  C CD1 . LEU B 458 ? 0.4694 0.2663 0.5822 0.0528  -0.0265 0.0609  458 LEU B CD1 
7910  C CD2 . LEU B 458 ? 0.4453 0.2535 0.5538 0.0389  -0.0246 0.0622  458 LEU B CD2 
7911  N N   . GLY B 459 ? 0.4101 0.2905 0.5685 0.0383  -0.0288 0.0463  459 GLY B N   
7912  C CA  . GLY B 459 ? 0.3937 0.2919 0.5655 0.0386  -0.0301 0.0423  459 GLY B CA  
7913  C C   . GLY B 459 ? 0.3811 0.2821 0.5612 0.0351  -0.0255 0.0381  459 GLY B C   
7914  O O   . GLY B 459 ? 0.3899 0.2857 0.5671 0.0287  -0.0214 0.0373  459 GLY B O   
7915  N N   . TRP B 460 ? 0.3822 0.2915 0.5726 0.0395  -0.0263 0.0357  460 TRP B N   
7916  C CA  . TRP B 460 ? 0.3836 0.2969 0.5818 0.0368  -0.0224 0.0317  460 TRP B CA  
7917  C C   . TRP B 460 ? 0.3638 0.2645 0.5587 0.0394  -0.0200 0.0316  460 TRP B C   
7918  O O   . TRP B 460 ? 0.3319 0.2331 0.5306 0.0365  -0.0167 0.0284  460 TRP B O   
7919  C CB  . TRP B 460 ? 0.3740 0.3038 0.5847 0.0389  -0.0237 0.0290  460 TRP B CB  
7920  C CG  . TRP B 460 ? 0.3905 0.3314 0.6043 0.0350  -0.0257 0.0282  460 TRP B CG  
7921  C CD1 . TRP B 460 ? 0.3827 0.3329 0.5992 0.0376  -0.0304 0.0292  460 TRP B CD1 
7922  C CD2 . TRP B 460 ? 0.4018 0.3455 0.6160 0.0278  -0.0230 0.0261  460 TRP B CD2 
7923  N NE1 . TRP B 460 ? 0.3982 0.3552 0.6156 0.0320  -0.0308 0.0276  460 TRP B NE1 
7924  C CE2 . TRP B 460 ? 0.4021 0.3551 0.6182 0.0265  -0.0261 0.0257  460 TRP B CE2 
7925  C CE3 . TRP B 460 ? 0.4061 0.3457 0.6193 0.0227  -0.0185 0.0245  460 TRP B CE3 
7926  C CZ2 . TRP B 460 ? 0.4369 0.3931 0.6530 0.0207  -0.0244 0.0236  460 TRP B CZ2 
7927  C CZ3 . TRP B 460 ? 0.3811 0.3257 0.5953 0.0176  -0.0170 0.0229  460 TRP B CZ3 
7928  C CH2 . TRP B 460 ? 0.4110 0.3630 0.6263 0.0168  -0.0197 0.0224  460 TRP B CH2 
7929  N N   . ALA B 461 ? 0.3777 0.2659 0.5641 0.0445  -0.0217 0.0349  461 ALA B N   
7930  C CA  . ALA B 461 ? 0.4050 0.2788 0.5866 0.0473  -0.0195 0.0346  461 ALA B CA  
7931  C C   . ALA B 461 ? 0.4324 0.2959 0.6081 0.0385  -0.0154 0.0336  461 ALA B C   
7932  O O   . ALA B 461 ? 0.4272 0.2879 0.5973 0.0324  -0.0148 0.0356  461 ALA B O   
7933  C CB  . ALA B 461 ? 0.4257 0.2865 0.5981 0.0548  -0.0222 0.0389  461 ALA B CB  
7934  N N   . ILE B 462 ? 0.4530 0.3109 0.6296 0.0383  -0.0128 0.0306  462 ILE B N   
7935  C CA  . ILE B 462 ? 0.4672 0.3197 0.6414 0.0298  -0.0092 0.0284  462 ILE B CA  
7936  C C   . ILE B 462 ? 0.4548 0.2865 0.6158 0.0269  -0.0081 0.0310  462 ILE B C   
7937  O O   . ILE B 462 ? 0.4253 0.2527 0.5830 0.0182  -0.0056 0.0306  462 ILE B O   
7938  C CB  . ILE B 462 ? 0.5084 0.3652 0.6893 0.0312  -0.0075 0.0237  462 ILE B CB  
7939  C CG1 . ILE B 462 ? 0.5288 0.4056 0.7217 0.0304  -0.0077 0.0215  462 ILE B CG1 
7940  C CG2 . ILE B 462 ? 0.5325 0.3793 0.7085 0.0243  -0.0045 0.0213  462 ILE B CG2 
7941  C CD1 . ILE B 462 ? 0.5376 0.4217 0.7322 0.0223  -0.0068 0.0217  462 ILE B CD1 
7942  N N   . GLY B 463 ? 0.4521 0.2710 0.6056 0.0343  -0.0099 0.0338  463 GLY B N   
7943  C CA  . GLY B 463 ? 0.4675 0.2639 0.6070 0.0320  -0.0088 0.0365  463 GLY B CA  
7944  C C   . GLY B 463 ? 0.4868 0.2712 0.6234 0.0314  -0.0064 0.0327  463 GLY B C   
7945  O O   . GLY B 463 ? 0.4822 0.2760 0.6271 0.0339  -0.0058 0.0284  463 GLY B O   
7946  N N   . SER B 464 ? 0.5426 0.3055 0.6663 0.0274  -0.0049 0.0343  464 SER B N   
7947  C CA  . SER B 464 ? 0.5422 0.2899 0.6603 0.0269  -0.0030 0.0307  464 SER B CA  
7948  C C   . SER B 464 ? 0.5152 0.2729 0.6402 0.0180  -0.0009 0.0256  464 SER B C   
7949  O O   . SER B 464 ? 0.4817 0.2509 0.6115 0.0094  -0.0002 0.0261  464 SER B O   
7950  C CB  . SER B 464 ? 0.5731 0.2952 0.6752 0.0235  -0.0021 0.0340  464 SER B CB  
7951  O OG  . SER B 464 ? 0.6189 0.3307 0.7144 0.0343  -0.0044 0.0382  464 SER B OG  
7952  N N   . GLN B 465 ? 0.5167 0.2701 0.6419 0.0208  0.0001  0.0209  465 GLN B N   
7953  C CA  . GLN B 465 ? 0.5340 0.2907 0.6615 0.0124  0.0018  0.0160  465 GLN B CA  
7954  C C   . GLN B 465 ? 0.5390 0.2719 0.6539 0.0118  0.0031  0.0132  465 GLN B C   
7955  O O   . GLN B 465 ? 0.5710 0.2893 0.6787 0.0210  0.0029  0.0140  465 GLN B O   
7956  C CB  . GLN B 465 ? 0.5088 0.2856 0.6489 0.0158  0.0019  0.0120  465 GLN B CB  
7957  C CG  . GLN B 465 ? 0.5484 0.3479 0.7007 0.0164  0.0007  0.0140  465 GLN B CG  
7958  C CD  . GLN B 465 ? 0.5647 0.3830 0.7285 0.0166  0.0012  0.0101  465 GLN B CD  
7959  O OE1 . GLN B 465 ? 0.6189 0.4482 0.7900 0.0243  0.0006  0.0097  465 GLN B OE1 
7960  N NE2 . GLN B 465 ? 0.5156 0.3380 0.6809 0.0082  0.0022  0.0074  465 GLN B NE2 
7961  N N   . ALA B 466 ? 0.5272 0.2565 0.6395 0.0013  0.0043  0.0099  466 ALA B N   
7962  C CA  . ALA B 466 ? 0.5422 0.2511 0.6433 0.0003  0.0053  0.0056  466 ALA B CA  
7963  C C   . ALA B 466 ? 0.5600 0.2796 0.6662 -0.0069 0.0057  0.0000  466 ALA B C   
7964  O O   . ALA B 466 ? 0.5372 0.2746 0.6525 -0.0148 0.0053  0.0004  466 ALA B O   
7965  C CB  . ALA B 466 ? 0.5637 0.2485 0.6504 -0.0071 0.0059  0.0081  466 ALA B CB  
7966  N N   . SER B 467 ? 0.5722 0.2811 0.6722 -0.0030 0.0066  -0.0051 467 SER B N   
7967  C CA  . SER B 467 ? 0.5714 0.2835 0.6712 -0.0102 0.0067  -0.0108 467 SER B CA  
7968  C C   . SER B 467 ? 0.6000 0.2855 0.6837 -0.0176 0.0071  -0.0134 467 SER B C   
7969  O O   . SER B 467 ? 0.6384 0.3025 0.7107 -0.0104 0.0082  -0.0145 467 SER B O   
7970  C CB  . SER B 467 ? 0.5909 0.3106 0.6944 -0.0011 0.0076  -0.0151 467 SER B CB  
7971  O OG  . SER B 467 ? 0.6071 0.3539 0.7259 0.0000  0.0071  -0.0143 467 SER B OG  
7972  N N   . VAL B 468 ? 0.6108 0.2981 0.6938 -0.0316 0.0062  -0.0142 468 VAL B N   
7973  C CA  . VAL B 468 ? 0.6314 0.2945 0.6996 -0.0412 0.0063  -0.0168 468 VAL B CA  
7974  C C   . VAL B 468 ? 0.6097 0.2782 0.6776 -0.0483 0.0052  -0.0234 468 VAL B C   
7975  O O   . VAL B 468 ? 0.5988 0.2907 0.6785 -0.0546 0.0038  -0.0236 468 VAL B O   
7976  C CB  . VAL B 468 ? 0.6357 0.2948 0.7019 -0.0531 0.0061  -0.0121 468 VAL B CB  
7977  C CG1 . VAL B 468 ? 0.6449 0.2770 0.6948 -0.0637 0.0063  -0.0146 468 VAL B CG1 
7978  C CG2 . VAL B 468 ? 0.6272 0.2840 0.6942 -0.0465 0.0070  -0.0051 468 VAL B CG2 
7979  N N   . SER B 469 ? 0.6334 0.2796 0.6870 -0.0466 0.0058  -0.0287 469 SER B N   
7980  C CA  . SER B 469 ? 0.6796 0.3246 0.7282 -0.0540 0.0045  -0.0355 469 SER B CA  
7981  C C   . SER B 469 ? 0.7078 0.3446 0.7505 -0.0711 0.0028  -0.0361 469 SER B C   
7982  O O   . SER B 469 ? 0.7195 0.3337 0.7511 -0.0753 0.0036  -0.0341 469 SER B O   
7983  C CB  . SER B 469 ? 0.7093 0.3320 0.7434 -0.0464 0.0061  -0.0413 469 SER B CB  
7984  O OG  . SER B 469 ? 0.7318 0.3539 0.7603 -0.0549 0.0045  -0.0479 469 SER B OG  
7985  N N   . ILE B 470 ? 0.7381 0.3932 0.7878 -0.0807 0.0003  -0.0389 470 ILE B N   
7986  C CA  . ILE B 470 ? 0.7649 0.4185 0.8122 -0.0978 -0.0018 -0.0396 470 ILE B CA  
7987  C C   . ILE B 470 ? 0.8071 0.4561 0.8463 -0.1049 -0.0043 -0.0472 470 ILE B C   
7988  O O   . ILE B 470 ? 0.8396 0.4922 0.8787 -0.1196 -0.0069 -0.0486 470 ILE B O   
7989  C CB  . ILE B 470 ? 0.7859 0.4703 0.8517 -0.1036 -0.0030 -0.0349 470 ILE B CB  
7990  C CG1 . ILE B 470 ? 0.7877 0.4999 0.8663 -0.1003 -0.0049 -0.0371 470 ILE B CG1 
7991  C CG2 . ILE B 470 ? 0.7962 0.4847 0.8687 -0.0965 -0.0005 -0.0276 470 ILE B CG2 
7992  C CD1 . ILE B 470 ? 0.7561 0.4973 0.8511 -0.1077 -0.0066 -0.0337 470 ILE B CD1 
7993  N N   . SER B 471 ? 0.8757 0.5189 0.9088 -0.0945 -0.0036 -0.0520 471 SER B N   
7994  C CA  . SER B 471 ? 0.9223 0.5573 0.9445 -0.0996 -0.0056 -0.0598 471 SER B CA  
7995  C C   . SER B 471 ? 0.9378 0.5460 0.9434 -0.1134 -0.0068 -0.0631 471 SER B C   
7996  O O   . SER B 471 ? 0.9497 0.5615 0.9523 -0.1256 -0.0104 -0.0676 471 SER B O   
7997  C CB  . SER B 471 ? 0.9612 0.5861 0.9755 -0.0848 -0.0029 -0.0638 471 SER B CB  
7998  O OG  . SER B 471 ? 1.0064 0.6025 1.0080 -0.0773 0.0003  -0.0632 471 SER B OG  
7999  N N   . ASP B 472 ? 0.9132 0.4953 0.9083 -0.1122 -0.0043 -0.0605 472 ASP B N   
8000  C CA  . ASP B 472 ? 0.9624 0.5155 0.9402 -0.1251 -0.0050 -0.0633 472 ASP B CA  
8001  C C   . ASP B 472 ? 0.9963 0.5622 0.9817 -0.1438 -0.0077 -0.0606 472 ASP B C   
8002  O O   . ASP B 472 ? 1.0325 0.5764 1.0046 -0.1570 -0.0085 -0.0627 472 ASP B O   
8003  C CB  . ASP B 472 ? 0.9606 0.4813 0.9243 -0.1173 -0.0013 -0.0607 472 ASP B CB  
8004  C CG  . ASP B 472 ? 0.9388 0.4648 0.9115 -0.1132 0.0008  -0.0516 472 ASP B CG  
8005  O OD1 . ASP B 472 ? 0.8955 0.4511 0.8868 -0.1074 0.0008  -0.0471 472 ASP B OD1 
8006  O OD2 . ASP B 472 ? 0.9946 0.4932 0.9543 -0.1152 0.0025  -0.0490 472 ASP B OD2 
8007  N N   . GLN B 473 ? 0.9553 0.5563 0.9616 -0.1454 -0.0090 -0.0561 473 GLN B N   
8008  C CA  . GLN B 473 ? 0.8881 0.5052 0.9045 -0.1610 -0.0107 -0.0525 473 GLN B CA  
8009  C C   . GLN B 473 ? 0.8768 0.5305 0.9106 -0.1659 -0.0144 -0.0533 473 GLN B C   
8010  O O   . GLN B 473 ? 0.8310 0.5035 0.8767 -0.1765 -0.0154 -0.0496 473 GLN B O   
8011  C CB  . GLN B 473 ? 0.8686 0.4951 0.8959 -0.1563 -0.0075 -0.0438 473 GLN B CB  
8012  C CG  . GLN B 473 ? 0.8809 0.4759 0.8940 -0.1528 -0.0040 -0.0403 473 GLN B CG  
8013  C CD  . GLN B 473 ? 0.8340 0.4407 0.8577 -0.1513 -0.0015 -0.0317 473 GLN B CD  
8014  O OE1 . GLN B 473 ? 0.7873 0.4046 0.8174 -0.1642 -0.0015 -0.0283 473 GLN B OE1 
8015  N NE2 . GLN B 473 ? 0.8074 0.4131 0.8331 -0.1353 0.0007  -0.0281 473 GLN B NE2 
8016  N N   . LEU B 474 ? 0.8820 0.5461 0.9174 -0.1583 -0.0162 -0.0579 474 LEU B N   
8017  C CA  . LEU B 474 ? 0.8811 0.5803 0.9336 -0.1589 -0.0193 -0.0574 474 LEU B CA  
8018  C C   . LEU B 474 ? 0.8829 0.5934 0.9382 -0.1770 -0.0240 -0.0597 474 LEU B C   
8019  O O   . LEU B 474 ? 0.8083 0.5493 0.8807 -0.1806 -0.0260 -0.0566 474 LEU B O   
8020  C CB  . LEU B 474 ? 0.8935 0.5988 0.9447 -0.1475 -0.0202 -0.0617 474 LEU B CB  
8021  C CG  . LEU B 474 ? 0.9183 0.6284 0.9756 -0.1294 -0.0164 -0.0584 474 LEU B CG  
8022  C CD1 . LEU B 474 ? 0.8791 0.6019 0.9384 -0.1203 -0.0173 -0.0619 474 LEU B CD1 
8023  C CD2 . LEU B 474 ? 0.8856 0.6168 0.9605 -0.1265 -0.0147 -0.0506 474 LEU B CD2 
8024  N N   . ASP B 475 ? 0.9824 0.6680 1.0207 -0.1880 -0.0256 -0.0649 475 ASP B N   
8025  C CA  . ASP B 475 ? 1.0404 0.7337 1.0792 -0.2067 -0.0303 -0.0678 475 ASP B CA  
8026  C C   . ASP B 475 ? 0.9864 0.6926 1.0373 -0.2184 -0.0294 -0.0616 475 ASP B C   
8027  O O   . ASP B 475 ? 0.9333 0.6610 0.9939 -0.2313 -0.0334 -0.0621 475 ASP B O   
8028  C CB  . ASP B 475 ? 1.0954 0.7567 1.1113 -0.2152 -0.0323 -0.0757 475 ASP B CB  
8029  C CG  . ASP B 475 ? 1.1907 0.8123 1.1879 -0.2152 -0.0281 -0.0758 475 ASP B CG  
8030  O OD1 . ASP B 475 ? 1.1574 0.7748 1.1588 -0.2070 -0.0234 -0.0693 475 ASP B OD1 
8031  O OD2 . ASP B 475 ? 1.1131 0.7068 1.0906 -0.2232 -0.0296 -0.0825 475 ASP B OD2 
8032  N N   . LYS B 476 ? 0.9524 0.6476 1.0033 -0.2138 -0.0243 -0.0557 476 LYS B N   
8033  C CA  . LYS B 476 ? 0.9196 0.6196 0.9769 -0.2265 -0.0227 -0.0504 476 LYS B CA  
8034  C C   . LYS B 476 ? 0.8256 0.5658 0.9070 -0.2261 -0.0229 -0.0451 476 LYS B C   
8035  O O   . LYS B 476 ? 0.7827 0.5418 0.8749 -0.2126 -0.0228 -0.0437 476 LYS B O   
8036  C CB  . LYS B 476 ? 0.9632 0.6354 1.0098 -0.2215 -0.0172 -0.0458 476 LYS B CB  
8037  C CG  . LYS B 476 ? 1.0613 0.6912 1.0831 -0.2250 -0.0167 -0.0505 476 LYS B CG  
8038  C CD  . LYS B 476 ? 1.1022 0.7038 1.1125 -0.2243 -0.0119 -0.0454 476 LYS B CD  
8039  C CE  . LYS B 476 ? 1.0633 0.6614 1.0750 -0.2043 -0.0082 -0.0411 476 LYS B CE  
8040  N NZ  . LYS B 476 ? 1.0776 0.6588 1.0837 -0.2046 -0.0041 -0.0342 476 LYS B NZ  
8041  N N   . LYS B 477 ? 0.7905 0.5427 0.8799 -0.2410 -0.0227 -0.0419 477 LYS B N   
8042  C CA  . LYS B 477 ? 0.7656 0.5549 0.8774 -0.2414 -0.0223 -0.0367 477 LYS B CA  
8043  C C   . LYS B 477 ? 0.7084 0.4988 0.8255 -0.2290 -0.0166 -0.0299 477 LYS B C   
8044  O O   . LYS B 477 ? 0.6246 0.4428 0.7583 -0.2209 -0.0160 -0.0266 477 LYS B O   
8045  C CB  . LYS B 477 ? 0.8098 0.6127 0.9293 -0.2607 -0.0228 -0.0349 477 LYS B CB  
8046  C CG  . LYS B 477 ? 0.9225 0.7407 1.0457 -0.2742 -0.0294 -0.0403 477 LYS B CG  
8047  C CD  . LYS B 477 ? 1.0535 0.8866 1.1856 -0.2939 -0.0295 -0.0381 477 LYS B CD  
8048  C CE  . LYS B 477 ? 1.1311 0.9666 1.2597 -0.3110 -0.0360 -0.0443 477 LYS B CE  
8049  N NZ  . LYS B 477 ? 1.1720 1.0285 1.3076 -0.3036 -0.0421 -0.0484 477 LYS B NZ  
8050  N N   . ILE B 478 ? 0.6798 0.4389 0.7819 -0.2279 -0.0127 -0.0279 478 ILE B N   
8051  C CA  . ILE B 478 ? 0.6381 0.3931 0.7415 -0.2172 -0.0076 -0.0214 478 ILE B CA  
8052  C C   . ILE B 478 ? 0.6383 0.3613 0.7249 -0.2046 -0.0062 -0.0227 478 ILE B C   
8053  O O   . ILE B 478 ? 0.6657 0.3581 0.7346 -0.2097 -0.0062 -0.0254 478 ILE B O   
8054  C CB  . ILE B 478 ? 0.6451 0.3969 0.7485 -0.2297 -0.0039 -0.0159 478 ILE B CB  
8055  C CG1 . ILE B 478 ? 0.6324 0.4186 0.7541 -0.2421 -0.0050 -0.0146 478 ILE B CG1 
8056  C CG2 . ILE B 478 ? 0.6457 0.3911 0.7482 -0.2181 0.0011  -0.0093 478 ILE B CG2 
8057  C CD1 . ILE B 478 ? 0.6476 0.4364 0.7721 -0.2540 -0.0004 -0.0086 478 ILE B CD1 
8058  N N   . ILE B 479 ? 0.6262 0.3563 0.7184 -0.1880 -0.0046 -0.0202 479 ILE B N   
8059  C CA  . ILE B 479 ? 0.6304 0.3358 0.7098 -0.1741 -0.0033 -0.0212 479 ILE B CA  
8060  C C   . ILE B 479 ? 0.6278 0.3295 0.7082 -0.1657 0.0007  -0.0141 479 ILE B C   
8061  O O   . ILE B 479 ? 0.6005 0.3273 0.6959 -0.1609 0.0017  -0.0102 479 ILE B O   
8062  C CB  . ILE B 479 ? 0.6108 0.3291 0.6960 -0.1613 -0.0055 -0.0251 479 ILE B CB  
8063  C CG1 . ILE B 479 ? 0.6184 0.3398 0.7010 -0.1692 -0.0098 -0.0322 479 ILE B CG1 
8064  C CG2 . ILE B 479 ? 0.6314 0.3288 0.7064 -0.1456 -0.0036 -0.0254 479 ILE B CG2 
8065  C CD1 . ILE B 479 ? 0.5936 0.3336 0.6842 -0.1587 -0.0120 -0.0353 479 ILE B CD1 
8066  N N   . THR B 480 ? 0.6364 0.3064 0.7003 -0.1635 0.0029  -0.0125 480 THR B N   
8067  C CA  . THR B 480 ? 0.6186 0.2828 0.6811 -0.1573 0.0063  -0.0054 480 THR B CA  
8068  C C   . THR B 480 ? 0.6123 0.2570 0.6653 -0.1405 0.0069  -0.0052 480 THR B C   
8069  O O   . THR B 480 ? 0.6310 0.2573 0.6733 -0.1363 0.0057  -0.0103 480 THR B O   
8070  C CB  . THR B 480 ? 0.6243 0.2703 0.6766 -0.1709 0.0087  -0.0015 480 THR B CB  
8071  O OG1 . THR B 480 ? 0.6323 0.2438 0.6652 -0.1720 0.0081  -0.0051 480 THR B OG1 
8072  C CG2 . THR B 480 ? 0.6275 0.2940 0.6900 -0.1883 0.0083  -0.0016 480 THR B CG2 
8073  N N   . SER B 481 ? 0.6090 0.2589 0.6661 -0.1307 0.0087  0.0005  481 SER B N   
8074  C CA  . SER B 481 ? 0.6258 0.2596 0.6752 -0.1149 0.0092  0.0016  481 SER B CA  
8075  C C   . SER B 481 ? 0.6200 0.2499 0.6675 -0.1116 0.0114  0.0094  481 SER B C   
8076  O O   . SER B 481 ? 0.6283 0.2773 0.6855 -0.1177 0.0126  0.0131  481 SER B O   
8077  C CB  . SER B 481 ? 0.6312 0.2846 0.6922 -0.1018 0.0077  -0.0011 481 SER B CB  
8078  O OG  . SER B 481 ? 0.6671 0.3041 0.7202 -0.0871 0.0082  -0.0001 481 SER B OG  
8079  N N   . GLU B 482 ? 0.6364 0.2416 0.6707 -0.1017 0.0120  0.0116  482 GLU B N   
8080  C CA  . GLU B 482 ? 0.6277 0.2259 0.6574 -0.0975 0.0137  0.0191  482 GLU B CA  
8081  C C   . GLU B 482 ? 0.6293 0.2216 0.6569 -0.0789 0.0126  0.0200  482 GLU B C   
8082  O O   . GLU B 482 ? 0.6484 0.2204 0.6659 -0.0723 0.0120  0.0166  482 GLU B O   
8083  C CB  . GLU B 482 ? 0.6479 0.2148 0.6592 -0.1070 0.0155  0.0222  482 GLU B CB  
8084  C CG  . GLU B 482 ? 0.6512 0.2100 0.6561 -0.1040 0.0173  0.0306  482 GLU B CG  
8085  C CD  . GLU B 482 ? 0.6669 0.1966 0.6541 -0.1160 0.0197  0.0344  482 GLU B CD  
8086  O OE1 . GLU B 482 ? 0.6896 0.1924 0.6630 -0.1185 0.0194  0.0309  482 GLU B OE1 
8087  O OE2 . GLU B 482 ? 0.6636 0.1965 0.6499 -0.1230 0.0221  0.0406  482 GLU B OE2 
8088  N N   . ASN B 483 ? 0.6099 0.2194 0.6465 -0.0709 0.0124  0.0245  483 ASN B N   
8089  C CA  . ASN B 483 ? 0.6157 0.2266 0.6542 -0.0538 0.0109  0.0251  483 ASN B CA  
8090  C C   . ASN B 483 ? 0.6112 0.2217 0.6473 -0.0484 0.0110  0.0326  483 ASN B C   
8091  O O   . ASN B 483 ? 0.6228 0.2519 0.6672 -0.0537 0.0117  0.0356  483 ASN B O   
8092  C CB  . ASN B 483 ? 0.5991 0.2392 0.6551 -0.0485 0.0095  0.0209  483 ASN B CB  
8093  C CG  . ASN B 483 ? 0.6295 0.2681 0.6859 -0.0511 0.0090  0.0136  483 ASN B CG  
8094  O OD1 . ASN B 483 ? 0.6935 0.3237 0.7466 -0.0406 0.0085  0.0103  483 ASN B OD1 
8095  N ND2 . ASN B 483 ? 0.6254 0.2723 0.6856 -0.0647 0.0093  0.0109  483 ASN B ND2 
8096  N N   . PHE B 484 ? 0.6340 0.2242 0.6589 -0.0370 0.0102  0.0356  484 PHE B N   
8097  C CA  . PHE B 484 ? 0.6257 0.2119 0.6453 -0.0320 0.0098  0.0431  484 PHE B CA  
8098  C C   . PHE B 484 ? 0.6022 0.2066 0.6322 -0.0170 0.0071  0.0440  484 PHE B C   
8099  O O   . PHE B 484 ? 0.5926 0.2022 0.6285 -0.0076 0.0058  0.0396  484 PHE B O   
8100  C CB  . PHE B 484 ? 0.6426 0.1923 0.6413 -0.0302 0.0104  0.0463  484 PHE B CB  
8101  C CG  . PHE B 484 ? 0.6625 0.1933 0.6500 -0.0466 0.0131  0.0460  484 PHE B CG  
8102  C CD1 . PHE B 484 ? 0.6691 0.1994 0.6527 -0.0583 0.0153  0.0515  484 PHE B CD1 
8103  C CD2 . PHE B 484 ? 0.6850 0.1968 0.6645 -0.0503 0.0136  0.0404  484 PHE B CD2 
8104  C CE1 . PHE B 484 ? 0.6873 0.2011 0.6612 -0.0742 0.0179  0.0514  484 PHE B CE1 
8105  C CE2 . PHE B 484 ? 0.6956 0.1887 0.6640 -0.0662 0.0158  0.0401  484 PHE B CE2 
8106  C CZ  . PHE B 484 ? 0.7017 0.1963 0.6678 -0.0783 0.0179  0.0457  484 PHE B CZ  
8107  N N   . PHE B 485 ? 0.5983 0.2127 0.6302 -0.0151 0.0063  0.0496  485 PHE B N   
8108  C CA  . PHE B 485 ? 0.5882 0.2205 0.6298 -0.0023 0.0033  0.0506  485 PHE B CA  
8109  C C   . PHE B 485 ? 0.6029 0.2280 0.6353 0.0017  0.0021  0.0583  485 PHE B C   
8110  O O   . PHE B 485 ? 0.6068 0.2274 0.6327 -0.0084 0.0042  0.0621  485 PHE B O   
8111  C CB  . PHE B 485 ? 0.5806 0.2449 0.6403 -0.0059 0.0033  0.0475  485 PHE B CB  
8112  C CG  . PHE B 485 ? 0.5916 0.2650 0.6603 -0.0111 0.0044  0.0405  485 PHE B CG  
8113  C CD1 . PHE B 485 ? 0.5984 0.2786 0.6744 -0.0019 0.0031  0.0358  485 PHE B CD1 
8114  C CD2 . PHE B 485 ? 0.5978 0.2740 0.6678 -0.0252 0.0069  0.0387  485 PHE B CD2 
8115  C CE1 . PHE B 485 ? 0.5830 0.2719 0.6663 -0.0066 0.0040  0.0296  485 PHE B CE1 
8116  C CE2 . PHE B 485 ? 0.5839 0.2693 0.6618 -0.0296 0.0073  0.0324  485 PHE B CE2 
8117  C CZ  . PHE B 485 ? 0.5644 0.2552 0.6482 -0.0203 0.0058  0.0279  485 PHE B CZ  
8118  N N   . ASN B 486 ? 0.6062 0.2312 0.6383 0.0162  -0.0014 0.0604  486 ASN B N   
8119  C CA  . ASN B 486 ? 0.6178 0.2382 0.6417 0.0216  -0.0036 0.0677  486 ASN B CA  
8120  C C   . ASN B 486 ? 0.5846 0.2329 0.6206 0.0191  -0.0046 0.0682  486 ASN B C   
8121  O O   . ASN B 486 ? 0.5534 0.2241 0.6051 0.0201  -0.0052 0.0632  486 ASN B O   
8122  C CB  . ASN B 486 ? 0.6331 0.2437 0.6524 0.0380  -0.0073 0.0700  486 ASN B CB  
8123  C CG  . ASN B 486 ? 0.6748 0.2517 0.6769 0.0403  -0.0060 0.0712  486 ASN B CG  
8124  O OD1 . ASN B 486 ? 0.7014 0.2721 0.7049 0.0481  -0.0061 0.0671  486 ASN B OD1 
8125  N ND2 . ASN B 486 ? 0.6908 0.2446 0.6758 0.0338  -0.0044 0.0769  486 ASN B ND2 
8126  N N   . ILE B 487 ? 0.5945 0.2399 0.6220 0.0149  -0.0043 0.0741  487 ILE B N   
8127  C CA  . ILE B 487 ? 0.5741 0.2432 0.6105 0.0119  -0.0047 0.0746  487 ILE B CA  
8128  C C   . ILE B 487 ? 0.5720 0.2450 0.6058 0.0236  -0.0097 0.0788  487 ILE B C   
8129  O O   . ILE B 487 ? 0.5932 0.2486 0.6118 0.0265  -0.0108 0.0851  487 ILE B O   
8130  C CB  . ILE B 487 ? 0.5748 0.2407 0.6040 -0.0014 -0.0004 0.0777  487 ILE B CB  
8131  C CG1 . ILE B 487 ? 0.5673 0.2309 0.5995 -0.0138 0.0041  0.0738  487 ILE B CG1 
8132  C CG2 . ILE B 487 ? 0.5610 0.2499 0.5977 -0.0029 -0.0008 0.0782  487 ILE B CG2 
8133  C CD1 . ILE B 487 ? 0.5769 0.2366 0.6017 -0.0269 0.0087  0.0776  487 ILE B CD1 
8134  N N   . PRO B 488 ? 0.5479 0.2438 0.5958 0.0304  -0.0131 0.0758  488 PRO B N   
8135  C CA  . PRO B 488 ? 0.5510 0.2519 0.5968 0.0408  -0.0184 0.0797  488 PRO B CA  
8136  C C   . PRO B 488 ? 0.5805 0.2804 0.6160 0.0356  -0.0183 0.0851  488 PRO B C   
8137  O O   . PRO B 488 ? 0.5810 0.2885 0.6183 0.0250  -0.0144 0.0839  488 PRO B O   
8138  C CB  . PRO B 488 ? 0.5138 0.2413 0.5784 0.0456  -0.0211 0.0744  488 PRO B CB  
8139  C CG  . PRO B 488 ? 0.5035 0.2354 0.5784 0.0405  -0.0173 0.0680  488 PRO B CG  
8140  C CD  . PRO B 488 ? 0.5309 0.2483 0.5967 0.0284  -0.0122 0.0688  488 PRO B CD  
8141  N N   . ASP B 489 ? 0.6235 0.3138 0.6473 0.0436  -0.0224 0.0911  489 ASP B N   
8142  C CA  . ASP B 489 ? 0.6333 0.3225 0.6458 0.0405  -0.0230 0.0965  489 ASP B CA  
8143  C C   . ASP B 489 ? 0.6157 0.3309 0.6399 0.0362  -0.0232 0.0928  489 ASP B C   
8144  O O   . ASP B 489 ? 0.6365 0.3527 0.6543 0.0280  -0.0201 0.0946  489 ASP B O   
8145  C CB  . ASP B 489 ? 0.6450 0.3225 0.6449 0.0518  -0.0287 0.1031  489 ASP B CB  
8146  C CG  . ASP B 489 ? 0.6932 0.3396 0.6757 0.0537  -0.0273 0.1084  489 ASP B CG  
8147  O OD1 . ASP B 489 ? 0.6926 0.3258 0.6709 0.0438  -0.0214 0.1075  489 ASP B OD1 
8148  O OD2 . ASP B 489 ? 0.6933 0.3288 0.6666 0.0651  -0.0322 0.1135  489 ASP B OD2 
8149  N N   . ASN B 490 ? 0.5853 0.3204 0.6258 0.0415  -0.0265 0.0877  490 ASN B N   
8150  C CA  . ASN B 490 ? 0.5615 0.3197 0.6121 0.0389  -0.0276 0.0842  490 ASN B CA  
8151  C C   . ASN B 490 ? 0.5269 0.2984 0.5920 0.0312  -0.0230 0.0776  490 ASN B C   
8152  O O   . ASN B 490 ? 0.5161 0.3068 0.5929 0.0314  -0.0244 0.0735  490 ASN B O   
8153  C CB  . ASN B 490 ? 0.5450 0.3171 0.6033 0.0493  -0.0347 0.0836  490 ASN B CB  
8154  C CG  . ASN B 490 ? 0.5505 0.3283 0.6226 0.0553  -0.0356 0.0794  490 ASN B CG  
8155  O OD1 . ASN B 490 ? 0.5565 0.3192 0.6257 0.0565  -0.0329 0.0795  490 ASN B OD1 
8156  N ND2 . ASN B 490 ? 0.5178 0.3168 0.6043 0.0588  -0.0390 0.0755  490 ASN B ND2 
8157  N N   . CYS B 491 ? 0.5336 0.2946 0.5976 0.0246  -0.0177 0.0765  491 CYS B N   
8158  C CA  . CYS B 491 ? 0.5044 0.2762 0.5790 0.0158  -0.0130 0.0713  491 CYS B CA  
8159  C C   . CYS B 491 ? 0.5102 0.2841 0.5787 0.0068  -0.0090 0.0732  491 CYS B C   
8160  O O   . CYS B 491 ? 0.5311 0.2892 0.5862 0.0024  -0.0064 0.0779  491 CYS B O   
8161  C CB  . CYS B 491 ? 0.5158 0.2746 0.5897 0.0112  -0.0092 0.0699  491 CYS B CB  
8162  S SG  . CYS B 491 ? 0.4869 0.2602 0.5737 0.0004  -0.0040 0.0640  491 CYS B SG  
8163  N N   . TRP B 492 ? 0.4873 0.2803 0.5652 0.0045  -0.0084 0.0697  492 TRP B N   
8164  C CA  . TRP B 492 ? 0.4880 0.2851 0.5606 -0.0025 -0.0046 0.0710  492 TRP B CA  
8165  C C   . TRP B 492 ? 0.4757 0.2796 0.5567 -0.0115 0.0014  0.0676  492 TRP B C   
8166  O O   . TRP B 492 ? 0.4722 0.2751 0.5479 -0.0191 0.0064  0.0694  492 TRP B O   
8167  C CB  . TRP B 492 ? 0.4909 0.3029 0.5664 0.0011  -0.0077 0.0694  492 TRP B CB  
8168  C CG  . TRP B 492 ? 0.4653 0.2747 0.5357 0.0102  -0.0147 0.0719  492 TRP B CG  
8169  C CD1 . TRP B 492 ? 0.4546 0.2777 0.5350 0.0161  -0.0197 0.0686  492 TRP B CD1 
8170  C CD2 . TRP B 492 ? 0.4728 0.2668 0.5278 0.0145  -0.0177 0.0783  492 TRP B CD2 
8171  N NE1 . TRP B 492 ? 0.4634 0.2823 0.5367 0.0237  -0.0259 0.0723  492 TRP B NE1 
8172  C CE2 . TRP B 492 ? 0.4857 0.2866 0.5433 0.0234  -0.0250 0.0783  492 TRP B CE2 
8173  C CE3 . TRP B 492 ? 0.5046 0.2796 0.5438 0.0116  -0.0151 0.0842  492 TRP B CE3 
8174  C CZ2 . TRP B 492 ? 0.5005 0.2906 0.5457 0.0304  -0.0300 0.0840  492 TRP B CZ2 
8175  C CZ3 . TRP B 492 ? 0.5138 0.2760 0.5395 0.0184  -0.0198 0.0900  492 TRP B CZ3 
8176  C CH2 . TRP B 492 ? 0.5226 0.2927 0.5514 0.0280  -0.0273 0.0899  492 TRP B CH2 
8177  N N   . VAL B 493 ? 0.4602 0.2717 0.5544 -0.0105 0.0008  0.0627  493 VAL B N   
8178  C CA  . VAL B 493 ? 0.4463 0.2651 0.5493 -0.0182 0.0055  0.0593  493 VAL B CA  
8179  C C   . VAL B 493 ? 0.4240 0.2404 0.5347 -0.0160 0.0040  0.0559  493 VAL B C   
8180  O O   . VAL B 493 ? 0.4094 0.2277 0.5241 -0.0080 -0.0003 0.0545  493 VAL B O   
8181  C CB  . VAL B 493 ? 0.4286 0.2671 0.5416 -0.0197 0.0071  0.0557  493 VAL B CB  
8182  C CG1 . VAL B 493 ? 0.4083 0.2572 0.5293 -0.0121 0.0023  0.0525  493 VAL B CG1 
8183  C CG2 . VAL B 493 ? 0.4252 0.2728 0.5484 -0.0266 0.0113  0.0522  493 VAL B CG2 
8184  N N   . VAL B 494 ? 0.4207 0.2336 0.5333 -0.0235 0.0075  0.0546  494 VAL B N   
8185  C CA  . VAL B 494 ? 0.4100 0.2214 0.5294 -0.0229 0.0067  0.0507  494 VAL B CA  
8186  C C   . VAL B 494 ? 0.3990 0.2253 0.5299 -0.0297 0.0096  0.0465  494 VAL B C   
8187  O O   . VAL B 494 ? 0.3911 0.2225 0.5220 -0.0372 0.0133  0.0476  494 VAL B O   
8188  C CB  . VAL B 494 ? 0.4216 0.2107 0.5300 -0.0248 0.0071  0.0529  494 VAL B CB  
8189  C CG1 . VAL B 494 ? 0.4491 0.2311 0.5512 -0.0363 0.0117  0.0552  494 VAL B CG1 
8190  C CG2 . VAL B 494 ? 0.4197 0.2059 0.5335 -0.0222 0.0057  0.0485  494 VAL B CG2 
8191  N N   . ASN B 495 ? 0.3847 0.2186 0.5255 -0.0264 0.0079  0.0420  495 ASN B N   
8192  C CA  . ASN B 495 ? 0.3830 0.2261 0.5327 -0.0323 0.0098  0.0382  495 ASN B CA  
8193  C C   . ASN B 495 ? 0.3789 0.2079 0.5247 -0.0343 0.0094  0.0366  495 ASN B C   
8194  O O   . ASN B 495 ? 0.3563 0.1804 0.5026 -0.0277 0.0069  0.0346  495 ASN B O   
8195  C CB  . ASN B 495 ? 0.3608 0.2210 0.5228 -0.0279 0.0084  0.0342  495 ASN B CB  
8196  C CG  . ASN B 495 ? 0.3538 0.2254 0.5247 -0.0338 0.0102  0.0309  495 ASN B CG  
8197  O OD1 . ASN B 495 ? 0.3560 0.2215 0.5256 -0.0392 0.0110  0.0298  495 ASN B OD1 
8198  N ND2 . ASN B 495 ? 0.3633 0.2513 0.5432 -0.0326 0.0107  0.0292  495 ASN B ND2 
8199  N N   . ALA B 496 ? 0.3881 0.2115 0.5304 -0.0439 0.0120  0.0372  496 ALA B N   
8200  C CA  . ALA B 496 ? 0.3994 0.2076 0.5362 -0.0474 0.0118  0.0356  496 ALA B CA  
8201  C C   . ALA B 496 ? 0.3905 0.2113 0.5370 -0.0539 0.0125  0.0312  496 ALA B C   
8202  O O   . ALA B 496 ? 0.4036 0.2372 0.5557 -0.0608 0.0148  0.0317  496 ALA B O   
8203  C CB  . ALA B 496 ? 0.4129 0.2024 0.5366 -0.0537 0.0138  0.0398  496 ALA B CB  
8204  N N   . SER B 497 ? 0.4022 0.2206 0.5507 -0.0508 0.0105  0.0270  497 SER B N   
8205  C CA  . SER B 497 ? 0.3998 0.2309 0.5572 -0.0556 0.0104  0.0227  497 SER B CA  
8206  C C   . SER B 497 ? 0.4299 0.2475 0.5820 -0.0560 0.0089  0.0188  497 SER B C   
8207  O O   . SER B 497 ? 0.4473 0.2477 0.5907 -0.0502 0.0081  0.0189  497 SER B O   
8208  C CB  . SER B 497 ? 0.3632 0.2144 0.5324 -0.0496 0.0095  0.0209  497 SER B CB  
8209  O OG  . SER B 497 ? 0.3450 0.1919 0.5134 -0.0396 0.0074  0.0199  497 SER B OG  
8210  N N   . ALA B 498 ? 0.4481 0.2738 0.6052 -0.0631 0.0087  0.0153  498 ALA B N   
8211  C CA  . ALA B 498 ? 0.4496 0.2657 0.6024 -0.0647 0.0073  0.0107  498 ALA B CA  
8212  C C   . ALA B 498 ? 0.4329 0.2686 0.5964 -0.0679 0.0061  0.0072  498 ALA B C   
8213  O O   . ALA B 498 ? 0.4530 0.3050 0.6247 -0.0732 0.0069  0.0085  498 ALA B O   
8214  C CB  . ALA B 498 ? 0.4585 0.2558 0.6003 -0.0744 0.0080  0.0110  498 ALA B CB  
8215  N N   . GLY B 499 ? 0.4330 0.2673 0.5961 -0.0640 0.0044  0.0028  499 GLY B N   
8216  C CA  . GLY B 499 ? 0.4092 0.2599 0.5803 -0.0669 0.0029  -0.0006 499 GLY B CA  
8217  C C   . GLY B 499 ? 0.4149 0.2557 0.5796 -0.0657 0.0014  -0.0057 499 GLY B C   
8218  O O   . GLY B 499 ? 0.4124 0.2357 0.5681 -0.0602 0.0017  -0.0068 499 GLY B O   
8219  N N   . ILE B 500 ? 0.4268 0.2798 0.5963 -0.0703 -0.0004 -0.0087 500 ILE B N   
8220  C CA  . ILE B 500 ? 0.4526 0.2986 0.6159 -0.0702 -0.0021 -0.0139 500 ILE B CA  
8221  C C   . ILE B 500 ? 0.4606 0.3277 0.6332 -0.0706 -0.0041 -0.0155 500 ILE B C   
8222  O O   . ILE B 500 ? 0.4789 0.3626 0.6605 -0.0759 -0.0047 -0.0135 500 ILE B O   
8223  C CB  . ILE B 500 ? 0.4508 0.2788 0.6026 -0.0802 -0.0029 -0.0165 500 ILE B CB  
8224  C CG1 . ILE B 500 ? 0.4870 0.3012 0.6285 -0.0778 -0.0040 -0.0222 500 ILE B CG1 
8225  C CG2 . ILE B 500 ? 0.4296 0.2702 0.5869 -0.0929 -0.0045 -0.0163 500 ILE B CG2 
8226  C CD1 . ILE B 500 ? 0.5164 0.3104 0.6448 -0.0879 -0.0049 -0.0255 500 ILE B CD1 
8227  N N   . SER B 501 ? 0.4431 0.3093 0.6130 -0.0648 -0.0048 -0.0190 501 SER B N   
8228  C CA  . SER B 501 ? 0.4284 0.3115 0.6044 -0.0651 -0.0069 -0.0208 501 SER B CA  
8229  C C   . SER B 501 ? 0.4433 0.3275 0.6160 -0.0759 -0.0100 -0.0239 501 SER B C   
8230  O O   . SER B 501 ? 0.4503 0.3177 0.6130 -0.0824 -0.0104 -0.0263 501 SER B O   
8231  C CB  . SER B 501 ? 0.4354 0.3166 0.6087 -0.0562 -0.0062 -0.0231 501 SER B CB  
8232  O OG  . SER B 501 ? 0.4470 0.3288 0.6244 -0.0472 -0.0037 -0.0200 501 SER B OG  
8233  N N   . VAL B 502 ? 0.4038 0.3081 0.5852 -0.0779 -0.0124 -0.0236 502 VAL B N   
8234  C CA  . VAL B 502 ? 0.4323 0.3438 0.6135 -0.0880 -0.0161 -0.0261 502 VAL B CA  
8235  C C   . VAL B 502 ? 0.4346 0.3612 0.6195 -0.0844 -0.0188 -0.0274 502 VAL B C   
8236  O O   . VAL B 502 ? 0.4185 0.3581 0.6119 -0.0770 -0.0178 -0.0244 502 VAL B O   
8237  C CB  . VAL B 502 ? 0.4403 0.3654 0.6314 -0.0957 -0.0164 -0.0226 502 VAL B CB  
8238  C CG1 . VAL B 502 ? 0.4734 0.4065 0.6650 -0.1073 -0.0205 -0.0251 502 VAL B CG1 
8239  C CG2 . VAL B 502 ? 0.4792 0.3906 0.6671 -0.0980 -0.0131 -0.0201 502 VAL B CG2 
8240  N N   . ARG B 503 ? 0.4448 0.3693 0.6226 -0.0901 -0.0224 -0.0317 503 ARG B N   
8241  C CA  . ARG B 503 ? 0.4505 0.3881 0.6298 -0.0873 -0.0254 -0.0329 503 ARG B CA  
8242  C C   . ARG B 503 ? 0.4223 0.3749 0.6059 -0.0971 -0.0305 -0.0337 503 ARG B C   
8243  O O   . ARG B 503 ? 0.4090 0.3541 0.5872 -0.1074 -0.0325 -0.0365 503 ARG B O   
8244  C CB  . ARG B 503 ? 0.5251 0.4479 0.6907 -0.0839 -0.0255 -0.0378 503 ARG B CB  
8245  C CG  . ARG B 503 ? 0.5551 0.4895 0.7199 -0.0808 -0.0283 -0.0389 503 ARG B CG  
8246  C CD  . ARG B 503 ? 0.6321 0.5503 0.7811 -0.0794 -0.0283 -0.0445 503 ARG B CD  
8247  N NE  . ARG B 503 ? 0.6897 0.5954 0.8349 -0.0696 -0.0229 -0.0444 503 ARG B NE  
8248  C CZ  . ARG B 503 ? 0.7130 0.6265 0.8639 -0.0600 -0.0200 -0.0413 503 ARG B CZ  
8249  N NH1 . ARG B 503 ? 0.7223 0.6534 0.8802 -0.0580 -0.0220 -0.0386 503 ARG B NH1 
8250  N NH2 . ARG B 503 ? 0.6845 0.5876 0.8337 -0.0524 -0.0153 -0.0410 503 ARG B NH2 
8251  N N   . TYR B 504 ? 0.3815 0.3553 0.5747 -0.0937 -0.0327 -0.0313 504 TYR B N   
8252  C CA  . TYR B 504 ? 0.3439 0.3335 0.5399 -0.1003 -0.0385 -0.0325 504 TYR B CA  
8253  C C   . TYR B 504 ? 0.3379 0.3344 0.5320 -0.0920 -0.0401 -0.0324 504 TYR B C   
8254  O O   . TYR B 504 ? 0.3434 0.3493 0.5454 -0.0834 -0.0380 -0.0283 504 TYR B O   
8255  C CB  . TYR B 504 ? 0.3222 0.3332 0.5336 -0.1047 -0.0396 -0.0285 504 TYR B CB  
8256  C CG  . TYR B 504 ? 0.3226 0.3518 0.5384 -0.1125 -0.0460 -0.0296 504 TYR B CG  
8257  C CD1 . TYR B 504 ? 0.3167 0.3628 0.5369 -0.1071 -0.0496 -0.0283 504 TYR B CD1 
8258  C CD2 . TYR B 504 ? 0.3405 0.3693 0.5551 -0.1258 -0.0488 -0.0322 504 TYR B CD2 
8259  C CE1 . TYR B 504 ? 0.3235 0.3868 0.5473 -0.1139 -0.0562 -0.0293 504 TYR B CE1 
8260  C CE2 . TYR B 504 ? 0.3345 0.3810 0.5534 -0.1336 -0.0552 -0.0335 504 TYR B CE2 
8261  C CZ  . TYR B 504 ? 0.3303 0.3951 0.5542 -0.1274 -0.0592 -0.0320 504 TYR B CZ  
8262  O OH  . TYR B 504 ? 0.3237 0.4079 0.5525 -0.1350 -0.0662 -0.0331 504 TYR B OH  
8263  N N   . GLY B 505 ? 0.3369 0.3267 0.5191 -0.0944 -0.0434 -0.0369 505 GLY B N   
8264  C CA  . GLY B 505 ? 0.3373 0.3311 0.5151 -0.0869 -0.0446 -0.0369 505 GLY B CA  
8265  C C   . GLY B 505 ? 0.3383 0.3223 0.5145 -0.0760 -0.0385 -0.0351 505 GLY B C   
8266  O O   . GLY B 505 ? 0.3399 0.3061 0.5088 -0.0748 -0.0348 -0.0374 505 GLY B O   
8267  N N   . LYS B 506 ? 0.3455 0.3417 0.5293 -0.0681 -0.0376 -0.0308 506 LYS B N   
8268  C CA  . LYS B 506 ? 0.3355 0.3248 0.5193 -0.0587 -0.0321 -0.0287 506 LYS B CA  
8269  C C   . LYS B 506 ? 0.3247 0.3163 0.5195 -0.0563 -0.0285 -0.0249 506 LYS B C   
8270  O O   . LYS B 506 ? 0.3554 0.3419 0.5512 -0.0492 -0.0242 -0.0232 506 LYS B O   
8271  C CB  . LYS B 506 ? 0.3335 0.3324 0.5177 -0.0518 -0.0327 -0.0261 506 LYS B CB  
8272  C CG  . LYS B 506 ? 0.3577 0.3551 0.5300 -0.0529 -0.0362 -0.0292 506 LYS B CG  
8273  C CD  . LYS B 506 ? 0.3800 0.3875 0.5537 -0.0459 -0.0366 -0.0253 506 LYS B CD  
8274  C CE  . LYS B 506 ? 0.3947 0.4050 0.5580 -0.0473 -0.0412 -0.0272 506 LYS B CE  
8275  N NZ  . LYS B 506 ? 0.3820 0.3971 0.5442 -0.0396 -0.0401 -0.0232 506 LYS B NZ  
8276  N N   . PHE B 507 ? 0.3206 0.3193 0.5230 -0.0627 -0.0300 -0.0238 507 PHE B N   
8277  C CA  . PHE B 507 ? 0.3106 0.3132 0.5232 -0.0608 -0.0267 -0.0200 507 PHE B CA  
8278  C C   . PHE B 507 ? 0.3458 0.3326 0.5545 -0.0643 -0.0238 -0.0214 507 PHE B C   
8279  O O   . PHE B 507 ? 0.3693 0.3530 0.5761 -0.0730 -0.0255 -0.0233 507 PHE B O   
8280  C CB  . PHE B 507 ? 0.2928 0.3140 0.5159 -0.0657 -0.0299 -0.0179 507 PHE B CB  
8281  C CG  . PHE B 507 ? 0.2738 0.3022 0.5078 -0.0641 -0.0267 -0.0139 507 PHE B CG  
8282  C CD1 . PHE B 507 ? 0.2687 0.2915 0.5038 -0.0704 -0.0249 -0.0140 507 PHE B CD1 
8283  C CD2 . PHE B 507 ? 0.2552 0.2949 0.4971 -0.0563 -0.0254 -0.0100 507 PHE B CD2 
8284  C CE1 . PHE B 507 ? 0.2604 0.2896 0.5044 -0.0689 -0.0217 -0.0104 507 PHE B CE1 
8285  C CE2 . PHE B 507 ? 0.2443 0.2899 0.4950 -0.0548 -0.0223 -0.0069 507 PHE B CE2 
8286  C CZ  . PHE B 507 ? 0.2523 0.2931 0.5040 -0.0610 -0.0204 -0.0071 507 PHE B CZ  
8287  N N   . THR B 508 ? 0.3528 0.3298 0.5603 -0.0576 -0.0196 -0.0204 508 THR B N   
8288  C CA  . THR B 508 ? 0.3973 0.3588 0.6007 -0.0590 -0.0168 -0.0210 508 THR B CA  
8289  C C   . THR B 508 ? 0.3823 0.3492 0.5949 -0.0565 -0.0141 -0.0166 508 THR B C   
8290  O O   . THR B 508 ? 0.3935 0.3691 0.6123 -0.0501 -0.0128 -0.0139 508 THR B O   
8291  C CB  . THR B 508 ? 0.4406 0.3871 0.6350 -0.0525 -0.0142 -0.0233 508 THR B CB  
8292  O OG1 . THR B 508 ? 0.4688 0.4233 0.6682 -0.0444 -0.0125 -0.0209 508 THR B OG1 
8293  C CG2 . THR B 508 ? 0.4581 0.3965 0.6413 -0.0547 -0.0162 -0.0281 508 THR B CG2 
8294  N N   . PHE B 509 ? 0.3884 0.3489 0.6006 -0.0618 -0.0130 -0.0160 509 PHE B N   
8295  C CA  . PHE B 509 ? 0.3794 0.3435 0.5984 -0.0600 -0.0103 -0.0120 509 PHE B CA  
8296  C C   . PHE B 509 ? 0.4047 0.3524 0.6173 -0.0636 -0.0085 -0.0120 509 PHE B C   
8297  O O   . PHE B 509 ? 0.4385 0.3721 0.6417 -0.0672 -0.0093 -0.0152 509 PHE B O   
8298  C CB  . PHE B 509 ? 0.3755 0.3580 0.6044 -0.0645 -0.0116 -0.0098 509 PHE B CB  
8299  C CG  . PHE B 509 ? 0.3600 0.3440 0.5881 -0.0755 -0.0137 -0.0113 509 PHE B CG  
8300  C CD1 . PHE B 509 ? 0.3852 0.3709 0.6096 -0.0804 -0.0177 -0.0147 509 PHE B CD1 
8301  C CD2 . PHE B 509 ? 0.3658 0.3504 0.5969 -0.0815 -0.0119 -0.0091 509 PHE B CD2 
8302  C CE1 . PHE B 509 ? 0.3859 0.3747 0.6104 -0.0915 -0.0201 -0.0162 509 PHE B CE1 
8303  C CE2 . PHE B 509 ? 0.3887 0.3763 0.6201 -0.0927 -0.0138 -0.0103 509 PHE B CE2 
8304  C CZ  . PHE B 509 ? 0.3822 0.3722 0.6106 -0.0979 -0.0181 -0.0139 509 PHE B CZ  
8305  N N   . LYS B 510 ? 0.3991 0.3478 0.6157 -0.0628 -0.0060 -0.0085 510 LYS B N   
8306  C CA  . LYS B 510 ? 0.4222 0.3549 0.6320 -0.0657 -0.0043 -0.0078 510 LYS B CA  
8307  C C   . LYS B 510 ? 0.3771 0.3165 0.5912 -0.0740 -0.0035 -0.0053 510 LYS B C   
8308  O O   . LYS B 510 ? 0.3313 0.2866 0.5546 -0.0731 -0.0026 -0.0027 510 LYS B O   
8309  C CB  . LYS B 510 ? 0.4636 0.3888 0.6719 -0.0567 -0.0020 -0.0058 510 LYS B CB  
8310  C CG  . LYS B 510 ? 0.5165 0.4343 0.7200 -0.0497 -0.0024 -0.0086 510 LYS B CG  
8311  C CD  . LYS B 510 ? 0.5598 0.4717 0.7625 -0.0407 -0.0006 -0.0072 510 LYS B CD  
8312  C CE  . LYS B 510 ? 0.6008 0.4958 0.7959 -0.0407 0.0005  -0.0063 510 LYS B CE  
8313  N NZ  . LYS B 510 ? 0.6798 0.5583 0.8647 -0.0410 0.0001  -0.0097 510 LYS B NZ  
8314  N N   . ILE B 511 ? 0.3936 0.3201 0.6004 -0.0822 -0.0036 -0.0061 511 ILE B N   
8315  C CA  . ILE B 511 ? 0.3927 0.3198 0.6007 -0.0896 -0.0016 -0.0031 511 ILE B CA  
8316  C C   . ILE B 511 ? 0.4001 0.3082 0.5995 -0.0862 0.0009  -0.0009 511 ILE B C   
8317  O O   . ILE B 511 ? 0.4158 0.3071 0.6063 -0.0818 0.0004  -0.0028 511 ILE B O   
8318  C CB  . ILE B 511 ? 0.4086 0.3347 0.6144 -0.1024 -0.0033 -0.0050 511 ILE B CB  
8319  C CG1 . ILE B 511 ? 0.4086 0.3098 0.5999 -0.1054 -0.0045 -0.0087 511 ILE B CG1 
8320  C CG2 . ILE B 511 ? 0.3809 0.3291 0.5967 -0.1054 -0.0063 -0.0066 511 ILE B CG2 
8321  C CD1 . ILE B 511 ? 0.4142 0.3105 0.6012 -0.1192 -0.0061 -0.0106 511 ILE B CD1 
8322  N N   . HIS B 512 ? 0.3884 0.2991 0.5899 -0.0886 0.0037  0.0032  512 HIS B N   
8323  C CA  . HIS B 512 ? 0.3678 0.2661 0.5635 -0.0832 0.0059  0.0064  512 HIS B CA  
8324  C C   . HIS B 512 ? 0.3472 0.2515 0.5454 -0.0886 0.0090  0.0106  512 HIS B C   
8325  O O   . HIS B 512 ? 0.3216 0.2432 0.5286 -0.0943 0.0097  0.0111  512 HIS B O   
8326  C CB  . HIS B 512 ? 0.3662 0.2700 0.5658 -0.0712 0.0057  0.0066  512 HIS B CB  
8327  C CG  . HIS B 512 ? 0.3573 0.2836 0.5690 -0.0691 0.0055  0.0066  512 HIS B CG  
8328  N ND1 . HIS B 512 ? 0.3297 0.2696 0.5482 -0.0711 0.0077  0.0095  512 HIS B ND1 
8329  C CD2 . HIS B 512 ? 0.3515 0.2880 0.5685 -0.0656 0.0036  0.0041  512 HIS B CD2 
8330  C CE1 . HIS B 512 ? 0.3327 0.2897 0.5605 -0.0678 0.0070  0.0087  512 HIS B CE1 
8331  N NE2 . HIS B 512 ? 0.3323 0.2875 0.5592 -0.0648 0.0043  0.0056  512 HIS B NE2 
8332  N N   . ASP B 513 ? 0.3542 0.2439 0.5442 -0.0863 0.0109  0.0138  513 ASP B N   
8333  C CA  . ASP B 513 ? 0.3547 0.2471 0.5445 -0.0898 0.0142  0.0182  513 ASP B CA  
8334  C C   . ASP B 513 ? 0.3629 0.2437 0.5457 -0.0809 0.0148  0.0210  513 ASP B C   
8335  O O   . ASP B 513 ? 0.3458 0.2138 0.5229 -0.0741 0.0127  0.0196  513 ASP B O   
8336  C CB  . ASP B 513 ? 0.4003 0.2824 0.5835 -0.1019 0.0157  0.0195  513 ASP B CB  
8337  C CG  . ASP B 513 ? 0.3950 0.2859 0.5808 -0.1084 0.0198  0.0237  513 ASP B CG  
8338  O OD1 . ASP B 513 ? 0.3547 0.2607 0.5477 -0.1029 0.0215  0.0254  513 ASP B OD1 
8339  O OD2 . ASP B 513 ? 0.4030 0.2839 0.5825 -0.1189 0.0214  0.0253  513 ASP B OD2 
8340  N N   . GLN B 514 ? 0.3851 0.2716 0.5686 -0.0810 0.0176  0.0248  514 GLN B N   
8341  C CA  . GLN B 514 ? 0.3903 0.2717 0.5695 -0.0722 0.0177  0.0272  514 GLN B CA  
8342  C C   . GLN B 514 ? 0.3889 0.2685 0.5631 -0.0765 0.0213  0.0319  514 GLN B C   
8343  O O   . GLN B 514 ? 0.3890 0.2824 0.5695 -0.0829 0.0242  0.0326  514 GLN B O   
8344  C CB  . GLN B 514 ? 0.3746 0.2735 0.5639 -0.0645 0.0170  0.0257  514 GLN B CB  
8345  C CG  . GLN B 514 ? 0.3670 0.2626 0.5529 -0.0556 0.0163  0.0275  514 GLN B CG  
8346  C CD  . GLN B 514 ? 0.3532 0.2660 0.5481 -0.0505 0.0165  0.0263  514 GLN B CD  
8347  O OE1 . GLN B 514 ? 0.3501 0.2742 0.5489 -0.0531 0.0193  0.0275  514 GLN B OE1 
8348  N NE2 . GLN B 514 ? 0.3347 0.2495 0.5329 -0.0432 0.0138  0.0241  514 GLN B NE2 
8349  N N   . LYS B 515 ? 0.4035 0.2666 0.5665 -0.0729 0.0212  0.0351  515 LYS B N   
8350  C CA  . LYS B 515 ? 0.4177 0.2774 0.5737 -0.0753 0.0244  0.0399  515 LYS B CA  
8351  C C   . LYS B 515 ? 0.4414 0.2962 0.5921 -0.0651 0.0225  0.0418  515 LYS B C   
8352  O O   . LYS B 515 ? 0.4749 0.3180 0.6211 -0.0585 0.0191  0.0411  515 LYS B O   
8353  C CB  . LYS B 515 ? 0.4450 0.2844 0.5886 -0.0828 0.0257  0.0429  515 LYS B CB  
8354  C CG  . LYS B 515 ? 0.4633 0.3032 0.6098 -0.0938 0.0267  0.0410  515 LYS B CG  
8355  C CD  . LYS B 515 ? 0.4661 0.3246 0.6209 -0.1029 0.0308  0.0420  515 LYS B CD  
8356  C CE  . LYS B 515 ? 0.4653 0.3251 0.6238 -0.1136 0.0305  0.0395  515 LYS B CE  
8357  N NZ  . LYS B 515 ? 0.4559 0.3383 0.6259 -0.1211 0.0338  0.0397  515 LYS B NZ  
8358  N N   . ILE B 516 ? 0.4148 0.2793 0.5661 -0.0639 0.0248  0.0439  516 ILE B N   
8359  C CA  . ILE B 516 ? 0.4035 0.2638 0.5487 -0.0557 0.0230  0.0459  516 ILE B CA  
8360  C C   . ILE B 516 ? 0.3986 0.2471 0.5307 -0.0594 0.0257  0.0513  516 ILE B C   
8361  O O   . ILE B 516 ? 0.3878 0.2423 0.5199 -0.0666 0.0303  0.0530  516 ILE B O   
8362  C CB  . ILE B 516 ? 0.3767 0.2553 0.5310 -0.0507 0.0230  0.0435  516 ILE B CB  
8363  C CG1 . ILE B 516 ? 0.3763 0.2636 0.5416 -0.0465 0.0200  0.0388  516 ILE B CG1 
8364  C CG2 . ILE B 516 ? 0.3676 0.2426 0.5145 -0.0440 0.0214  0.0457  516 ILE B CG2 
8365  C CD1 . ILE B 516 ? 0.3735 0.2790 0.5488 -0.0439 0.0209  0.0362  516 ILE B CD1 
8366  N N   . ILE B 517 ? 0.4332 0.2647 0.5539 -0.0544 0.0229  0.0542  517 ILE B N   
8367  C CA  . ILE B 517 ? 0.4441 0.2601 0.5500 -0.0579 0.0250  0.0599  517 ILE B CA  
8368  C C   . ILE B 517 ? 0.4608 0.2703 0.5576 -0.0491 0.0218  0.0629  517 ILE B C   
8369  O O   . ILE B 517 ? 0.4568 0.2632 0.5547 -0.0405 0.0169  0.0615  517 ILE B O   
8370  C CB  . ILE B 517 ? 0.4558 0.2518 0.5538 -0.0625 0.0249  0.0613  517 ILE B CB  
8371  C CG1 . ILE B 517 ? 0.4586 0.2615 0.5660 -0.0710 0.0268  0.0577  517 ILE B CG1 
8372  C CG2 . ILE B 517 ? 0.4818 0.2613 0.5640 -0.0674 0.0277  0.0677  517 ILE B CG2 
8373  C CD1 . ILE B 517 ? 0.4902 0.2724 0.5897 -0.0752 0.0260  0.0579  517 ILE B CD1 
8374  N N   . TYR B 518 ? 0.4822 0.2898 0.5694 -0.0515 0.0246  0.0672  518 TYR B N   
8375  C CA  . TYR B 518 ? 0.4649 0.2700 0.5435 -0.0441 0.0218  0.0698  518 TYR B CA  
8376  C C   . TYR B 518 ? 0.4954 0.2781 0.5562 -0.0438 0.0210  0.0762  518 TYR B C   
8377  O O   . TYR B 518 ? 0.5004 0.2718 0.5542 -0.0519 0.0250  0.0793  518 TYR B O   
8378  C CB  . TYR B 518 ? 0.4655 0.2843 0.5446 -0.0473 0.0261  0.0700  518 TYR B CB  
8379  C CG  . TYR B 518 ? 0.4686 0.3085 0.5637 -0.0461 0.0267  0.0641  518 TYR B CG  
8380  C CD1 . TYR B 518 ? 0.4438 0.2911 0.5442 -0.0379 0.0219  0.0609  518 TYR B CD1 
8381  C CD2 . TYR B 518 ? 0.4537 0.3060 0.5581 -0.0533 0.0319  0.0621  518 TYR B CD2 
8382  C CE1 . TYR B 518 ? 0.4472 0.3114 0.5606 -0.0368 0.0225  0.0559  518 TYR B CE1 
8383  C CE2 . TYR B 518 ? 0.4477 0.3179 0.5657 -0.0512 0.0321  0.0572  518 TYR B CE2 
8384  C CZ  . TYR B 518 ? 0.4463 0.3214 0.5681 -0.0430 0.0276  0.0542  518 TYR B CZ  
8385  O OH  . TYR B 518 ? 0.4311 0.3216 0.5647 -0.0405 0.0277  0.0496  518 TYR B OH  
8386  N N   . ARG B 519 ? 0.4972 0.2740 0.5507 -0.0347 0.0159  0.0783  519 ARG B N   
8387  C CA  . ARG B 519 ? 0.5164 0.2742 0.5516 -0.0335 0.0152  0.0851  519 ARG B CA  
8388  C C   . ARG B 519 ? 0.5422 0.3049 0.5689 -0.0370 0.0186  0.0881  519 ARG B C   
8389  O O   . ARG B 519 ? 0.5479 0.3207 0.5749 -0.0314 0.0159  0.0870  519 ARG B O   
8390  C CB  . ARG B 519 ? 0.5043 0.2544 0.5351 -0.0219 0.0078  0.0865  519 ARG B CB  
8391  C CG  . ARG B 519 ? 0.5127 0.2401 0.5239 -0.0195 0.0064  0.0939  519 ARG B CG  
8392  C CD  . ARG B 519 ? 0.5068 0.2318 0.5158 -0.0069 -0.0013 0.0951  519 ARG B CD  
8393  N NE  . ARG B 519 ? 0.5033 0.2248 0.5212 -0.0018 -0.0039 0.0919  519 ARG B NE  
8394  C CZ  . ARG B 519 ? 0.5033 0.2041 0.5138 -0.0021 -0.0030 0.0941  519 ARG B CZ  
8395  N NH1 . ARG B 519 ? 0.5150 0.1961 0.5091 -0.0073 0.0000  0.0999  519 ARG B NH1 
8396  N NH2 . ARG B 519 ? 0.4963 0.1956 0.5154 0.0023  -0.0047 0.0902  519 ARG B NH2 
8397  N N   . GLY B 520 ? 0.5693 0.3242 0.5873 -0.0464 0.0248  0.0920  520 GLY B N   
8398  C CA  . GLY B 520 ? 0.5735 0.3296 0.5801 -0.0496 0.0288  0.0959  520 GLY B CA  
8399  C C   . GLY B 520 ? 0.5477 0.3273 0.5661 -0.0506 0.0316  0.0908  520 GLY B C   
8400  O O   . GLY B 520 ? 0.5206 0.3132 0.5548 -0.0535 0.0334  0.0858  520 GLY B O   
8401  N N   . ASP B 521 ? 0.5624 0.3464 0.5727 -0.0472 0.0313  0.0919  521 ASP B N   
8402  C CA  . ASP B 521 ? 0.5901 0.3928 0.6073 -0.0493 0.0358  0.0881  521 ASP B CA  
8403  C C   . ASP B 521 ? 0.5419 0.3561 0.5654 -0.0407 0.0303  0.0832  521 ASP B C   
8404  O O   . ASP B 521 ? 0.5095 0.3363 0.5353 -0.0409 0.0332  0.0802  521 ASP B O   
8405  C CB  . ASP B 521 ? 0.6291 0.4284 0.6318 -0.0549 0.0425  0.0928  521 ASP B CB  
8406  C CG  . ASP B 521 ? 0.7049 0.4927 0.6880 -0.0498 0.0390  0.0974  521 ASP B CG  
8407  O OD1 . ASP B 521 ? 0.7236 0.5098 0.7060 -0.0411 0.0310  0.0961  521 ASP B OD1 
8408  O OD2 . ASP B 521 ? 0.7986 0.5793 0.7671 -0.0548 0.0444  0.1025  521 ASP B OD2 
8409  N N   . TRP B 522 ? 0.5195 0.3297 0.5462 -0.0335 0.0225  0.0821  522 TRP B N   
8410  C CA  . TRP B 522 ? 0.5160 0.3351 0.5461 -0.0260 0.0167  0.0784  522 TRP B CA  
8411  C C   . TRP B 522 ? 0.5040 0.3414 0.5496 -0.0270 0.0192  0.0717  522 TRP B C   
8412  O O   . TRP B 522 ? 0.5146 0.3600 0.5600 -0.0235 0.0172  0.0687  522 TRP B O   
8413  C CB  . TRP B 522 ? 0.5007 0.3146 0.5338 -0.0184 0.0084  0.0784  522 TRP B CB  
8414  C CG  . TRP B 522 ? 0.4803 0.3008 0.5308 -0.0178 0.0075  0.0738  522 TRP B CG  
8415  C CD1 . TRP B 522 ? 0.4972 0.3094 0.5510 -0.0205 0.0091  0.0748  522 TRP B CD1 
8416  C CD2 . TRP B 522 ? 0.4687 0.3043 0.5343 -0.0145 0.0049  0.0677  522 TRP B CD2 
8417  N NE1 . TRP B 522 ? 0.4808 0.3025 0.5506 -0.0190 0.0078  0.0696  522 TRP B NE1 
8418  C CE2 . TRP B 522 ? 0.4617 0.2978 0.5391 -0.0153 0.0053  0.0654  522 TRP B CE2 
8419  C CE3 . TRP B 522 ? 0.4580 0.3056 0.5276 -0.0113 0.0023  0.0639  522 TRP B CE3 
8420  C CZ2 . TRP B 522 ? 0.4469 0.2956 0.5395 -0.0128 0.0034  0.0599  522 TRP B CZ2 
8421  C CZ3 . TRP B 522 ? 0.4455 0.3048 0.5303 -0.0092 0.0005  0.0585  522 TRP B CZ3 
8422  C CH2 . TRP B 522 ? 0.4382 0.2982 0.5344 -0.0098 0.0011  0.0567  522 TRP B CH2 
8423  N N   . ALA B 523 ? 0.4982 0.3413 0.5561 -0.0318 0.0234  0.0695  523 ALA B N   
8424  C CA  . ALA B 523 ? 0.5073 0.3668 0.5804 -0.0318 0.0251  0.0636  523 ALA B CA  
8425  C C   . ALA B 523 ? 0.5331 0.4022 0.6074 -0.0374 0.0332  0.0629  523 ALA B C   
8426  O O   . ALA B 523 ? 0.5475 0.4298 0.6353 -0.0383 0.0357  0.0586  523 ALA B O   
8427  C CB  . ALA B 523 ? 0.4648 0.3263 0.5517 -0.0320 0.0232  0.0611  523 ALA B CB  
8428  N N   . LYS B 524 ? 0.5441 0.4079 0.6047 -0.0406 0.0376  0.0669  524 LYS B N   
8429  C CA  . LYS B 524 ? 0.5860 0.4604 0.6488 -0.0457 0.0460  0.0663  524 LYS B CA  
8430  C C   . LYS B 524 ? 0.5736 0.4623 0.6442 -0.0413 0.0467  0.0605  524 LYS B C   
8431  O O   . LYS B 524 ? 0.5528 0.4544 0.6342 -0.0436 0.0520  0.0578  524 LYS B O   
8432  C CB  . LYS B 524 ? 0.6440 0.5108 0.6900 -0.0499 0.0513  0.0717  524 LYS B CB  
8433  C CG  . LYS B 524 ? 0.7482 0.6058 0.7767 -0.0452 0.0480  0.0737  524 LYS B CG  
8434  C CD  . LYS B 524 ? 0.8770 0.7256 0.8876 -0.0500 0.0536  0.0798  524 LYS B CD  
8435  C CE  . LYS B 524 ? 0.9367 0.7766 0.9283 -0.0455 0.0504  0.0819  524 LYS B CE  
8436  N NZ  . LYS B 524 ? 0.9304 0.7624 0.9195 -0.0386 0.0401  0.0818  524 LYS B NZ  
8437  N N   . GLU B 525 ? 0.5549 0.4412 0.6202 -0.0351 0.0412  0.0583  525 GLU B N   
8438  C CA  . GLU B 525 ? 0.5099 0.4068 0.5808 -0.0311 0.0415  0.0527  525 GLU B CA  
8439  C C   . GLU B 525 ? 0.4775 0.3811 0.5650 -0.0284 0.0372  0.0485  525 GLU B C   
8440  O O   . GLU B 525 ? 0.4440 0.3587 0.5427 -0.0283 0.0405  0.0449  525 GLU B O   
8441  C CB  . GLU B 525 ? 0.5291 0.4208 0.5861 -0.0268 0.0379  0.0519  525 GLU B CB  
8442  C CG  . GLU B 525 ? 0.5301 0.4152 0.5688 -0.0290 0.0423  0.0557  525 GLU B CG  
8443  C CD  . GLU B 525 ? 0.5666 0.4372 0.5915 -0.0292 0.0376  0.0616  525 GLU B CD  
8444  O OE1 . GLU B 525 ? 0.5475 0.4128 0.5761 -0.0266 0.0304  0.0626  525 GLU B OE1 
8445  O OE2 . GLU B 525 ? 0.5743 0.4388 0.5838 -0.0315 0.0416  0.0655  525 GLU B OE2 
8446  N N   . VAL B 526 ? 0.4771 0.3742 0.5661 -0.0257 0.0300  0.0490  526 VAL B N   
8447  C CA  . VAL B 526 ? 0.4494 0.3527 0.5520 -0.0225 0.0257  0.0448  526 VAL B CA  
8448  C C   . VAL B 526 ? 0.4205 0.3285 0.5365 -0.0255 0.0276  0.0443  526 VAL B C   
8449  O O   . VAL B 526 ? 0.3623 0.2781 0.4903 -0.0235 0.0262  0.0405  526 VAL B O   
8450  C CB  . VAL B 526 ? 0.4551 0.3519 0.5548 -0.0180 0.0175  0.0452  526 VAL B CB  
8451  C CG1 . VAL B 526 ? 0.4592 0.3456 0.5557 -0.0187 0.0151  0.0497  526 VAL B CG1 
8452  C CG2 . VAL B 526 ? 0.4489 0.3535 0.5618 -0.0147 0.0137  0.0405  526 VAL B CG2 
8453  N N   . GLY B 527 ? 0.4235 0.3261 0.5367 -0.0305 0.0305  0.0482  527 GLY B N   
8454  C CA  . GLY B 527 ? 0.4160 0.3214 0.5404 -0.0341 0.0315  0.0477  527 GLY B CA  
8455  C C   . GLY B 527 ? 0.4118 0.3310 0.5461 -0.0378 0.0376  0.0458  527 GLY B C   
8456  O O   . GLY B 527 ? 0.3840 0.3079 0.5140 -0.0395 0.0429  0.0466  527 GLY B O   
8457  N N   . ARG B 528 ? 0.4386 0.3646 0.5859 -0.0389 0.0368  0.0433  528 ARG B N   
8458  C CA  . ARG B 528 ? 0.4921 0.4325 0.6501 -0.0420 0.0417  0.0416  528 ARG B CA  
8459  C C   . ARG B 528 ? 0.5338 0.4744 0.6878 -0.0496 0.0475  0.0454  528 ARG B C   
8460  O O   . ARG B 528 ? 0.4603 0.3893 0.6076 -0.0540 0.0467  0.0487  528 ARG B O   
8461  C CB  . ARG B 528 ? 0.5102 0.4567 0.6812 -0.0426 0.0392  0.0390  528 ARG B CB  
8462  C CG  . ARG B 528 ? 0.4630 0.4267 0.6465 -0.0432 0.0428  0.0365  528 ARG B CG  
8463  C CD  . ARG B 528 ? 0.4324 0.4010 0.6271 -0.0447 0.0399  0.0345  528 ARG B CD  
8464  N NE  . ARG B 528 ? 0.4004 0.3677 0.5987 -0.0384 0.0350  0.0314  528 ARG B NE  
8465  C CZ  . ARG B 528 ? 0.3993 0.3557 0.5942 -0.0363 0.0301  0.0311  528 ARG B CZ  
8466  N NH1 . ARG B 528 ? 0.4132 0.3579 0.6015 -0.0398 0.0290  0.0336  528 ARG B NH1 
8467  N NH2 . ARG B 528 ? 0.3653 0.3220 0.5629 -0.0305 0.0265  0.0286  528 ARG B NH2 
8468  N N   . LYS B 529 ? 0.6515 0.6053 0.8095 -0.0509 0.0535  0.0449  529 LYS B N   
8469  C CA  . LYS B 529 ? 0.6878 0.6452 0.8434 -0.0584 0.0601  0.0483  529 LYS B CA  
8470  C C   . LYS B 529 ? 0.7217 0.6912 0.8914 -0.0645 0.0617  0.0477  529 LYS B C   
8471  O O   . LYS B 529 ? 0.6628 0.6452 0.8450 -0.0607 0.0606  0.0439  529 LYS B O   
8472  C CB  . LYS B 529 ? 0.7094 0.6760 0.8617 -0.0563 0.0665  0.0482  529 LYS B CB  
8473  C CG  . LYS B 529 ? 0.7832 0.7372 0.9181 -0.0538 0.0667  0.0504  529 LYS B CG  
8474  C CD  . LYS B 529 ? 0.8476 0.7992 0.9792 -0.0451 0.0626  0.0466  529 LYS B CD  
8475  C CE  . LYS B 529 ? 0.8661 0.8040 0.9801 -0.0429 0.0607  0.0487  529 LYS B CE  
8476  N NZ  . LYS B 529 ? 0.7622 0.6962 0.8751 -0.0359 0.0541  0.0452  529 LYS B NZ  
8477  N N   . SER C 3   ? 1.0734 0.6390 0.8270 0.0408  0.0644  0.1651  3   SER C N   
8478  C CA  . SER C 3   ? 1.0930 0.6549 0.8236 0.0424  0.0546  0.1559  3   SER C CA  
8479  C C   . SER C 3   ? 1.0675 0.6494 0.8233 0.0402  0.0561  0.1454  3   SER C C   
8480  O O   . SER C 3   ? 1.0644 0.6655 0.8562 0.0372  0.0515  0.1417  3   SER C O   
8481  C CB  . SER C 3   ? 1.0875 0.6458 0.8101 0.0429  0.0329  0.1535  3   SER C CB  
8482  O OG  . SER C 3   ? 1.0538 0.6029 0.7472 0.0446  0.0243  0.1471  3   SER C OG  
8483  N N   . LYS C 4   ? 1.0063 0.5827 0.7419 0.0420  0.0624  0.1405  4   LYS C N   
8484  C CA  . LYS C 4   ? 0.9598 0.5534 0.7172 0.0403  0.0656  0.1315  4   LYS C CA  
8485  C C   . LYS C 4   ? 0.8689 0.4668 0.6218 0.0396  0.0486  0.1209  4   LYS C C   
8486  O O   . LYS C 4   ? 0.8472 0.4301 0.5701 0.0412  0.0384  0.1200  4   LYS C O   
8487  C CB  . LYS C 4   ? 1.0372 0.6248 0.7827 0.0427  0.0854  0.1331  4   LYS C CB  
8488  C CG  . LYS C 4   ? 1.1029 0.6708 0.8062 0.0465  0.0879  0.1300  4   LYS C CG  
8489  C CD  . LYS C 4   ? 1.1752 0.7284 0.8575 0.0503  0.1098  0.1376  4   LYS C CD  
8490  C CE  . LYS C 4   ? 1.2128 0.7500 0.8605 0.0543  0.1166  0.1329  4   LYS C CE  
8491  N NZ  . LYS C 4   ? 1.2498 0.7722 0.8648 0.0550  0.0995  0.1267  4   LYS C NZ  
8492  N N   . THR C 5   ? 0.8073 0.4257 0.5907 0.0369  0.0461  0.1133  5   THR C N   
8493  C CA  . THR C 5   ? 0.8056 0.4327 0.5937 0.0353  0.0315  0.1033  5   THR C CA  
8494  C C   . THR C 5   ? 0.8041 0.4145 0.5559 0.0373  0.0281  0.0992  5   THR C C   
8495  O O   . THR C 5   ? 0.7767 0.3765 0.5096 0.0396  0.0411  0.0997  5   THR C O   
8496  C CB  . THR C 5   ? 0.7624 0.4109 0.5835 0.0328  0.0358  0.0972  5   THR C CB  
8497  O OG1 . THR C 5   ? 0.7432 0.4030 0.5930 0.0311  0.0387  0.1018  5   THR C OG1 
8498  C CG2 . THR C 5   ? 0.7285 0.3889 0.5606 0.0306  0.0212  0.0878  5   THR C CG2 
8499  N N   . LYS C 6   ? 0.8161 0.4237 0.5586 0.0365  0.0101  0.0953  6   LYS C N   
8500  C CA  . LYS C 6   ? 0.8427 0.4365 0.5549 0.0372  0.0023  0.0899  6   LYS C CA  
8501  C C   . LYS C 6   ? 0.7980 0.4078 0.5303 0.0342  -0.0048 0.0801  6   LYS C C   
8502  O O   . LYS C 6   ? 0.7427 0.3688 0.5006 0.0316  -0.0164 0.0771  6   LYS C O   
8503  C CB  . LYS C 6   ? 0.8998 0.4815 0.5924 0.0378  -0.0142 0.0927  6   LYS C CB  
8504  C CG  . LYS C 6   ? 0.9710 0.5373 0.6316 0.0380  -0.0260 0.0872  6   LYS C CG  
8505  C CD  . LYS C 6   ? 1.0287 0.5864 0.6757 0.0381  -0.0451 0.0897  6   LYS C CD  
8506  C CE  . LYS C 6   ? 1.0951 0.6320 0.7030 0.0387  -0.0549 0.0859  6   LYS C CE  
8507  N NZ  . LYS C 6   ? 1.1375 0.6588 0.7219 0.0404  -0.0677 0.0920  6   LYS C NZ  
8508  N N   . ILE C 7   ? 0.8214 0.4259 0.5415 0.0350  0.0032  0.0753  7   ILE C N   
8509  C CA  . ILE C 7   ? 0.7923 0.4087 0.5268 0.0323  -0.0026 0.0664  7   ILE C CA  
8510  C C   . ILE C 7   ? 0.8538 0.4543 0.5584 0.0319  -0.0149 0.0610  7   ILE C C   
8511  O O   . ILE C 7   ? 0.8626 0.4418 0.5329 0.0347  -0.0095 0.0614  7   ILE C O   
8512  C CB  . ILE C 7   ? 0.7593 0.3819 0.5048 0.0332  0.0140  0.0646  7   ILE C CB  
8513  C CG1 . ILE C 7   ? 0.7445 0.3804 0.5168 0.0335  0.0261  0.0706  7   ILE C CG1 
8514  C CG2 . ILE C 7   ? 0.7311 0.3670 0.4939 0.0302  0.0079  0.0560  7   ILE C CG2 
8515  C CD1 . ILE C 7   ? 0.7456 0.3911 0.5346 0.0340  0.0406  0.0688  7   ILE C CD1 
8516  N N   . GLU C 8   ? 0.8937 0.5050 0.6127 0.0283  -0.0312 0.0557  8   GLU C N   
8517  C CA  . GLU C 8   ? 0.9218 0.5205 0.6177 0.0269  -0.0454 0.0505  8   GLU C CA  
8518  C C   . GLU C 8   ? 0.8560 0.4693 0.5731 0.0230  -0.0512 0.0425  8   GLU C C   
8519  O O   . GLU C 8   ? 0.8073 0.4423 0.5578 0.0204  -0.0559 0.0414  8   GLU C O   
8520  C CB  . GLU C 8   ? 1.0016 0.5973 0.6931 0.0267  -0.0607 0.0546  8   GLU C CB  
8521  C CG  . GLU C 8   ? 1.1143 0.6921 0.7754 0.0258  -0.0770 0.0518  8   GLU C CG  
8522  C CD  . GLU C 8   ? 1.2051 0.7749 0.8547 0.0272  -0.0887 0.0582  8   GLU C CD  
8523  O OE1 . GLU C 8   ? 1.1658 0.7395 0.8248 0.0294  -0.0827 0.0655  8   GLU C OE1 
8524  O OE2 . GLU C 8   ? 1.2912 0.8498 0.9217 0.0259  -0.1050 0.0557  8   GLU C OE2 
8525  N N   . LEU C 9   ? 0.8657 0.4660 0.5620 0.0227  -0.0506 0.0368  9   LEU C N   
8526  C CA  . LEU C 9   ? 0.8108 0.4219 0.5235 0.0189  -0.0559 0.0296  9   LEU C CA  
8527  C C   . LEU C 9   ? 0.8308 0.4342 0.5311 0.0155  -0.0757 0.0255  9   LEU C C   
8528  O O   . LEU C 9   ? 0.8849 0.4655 0.5504 0.0167  -0.0800 0.0244  9   LEU C O   
8529  C CB  . LEU C 9   ? 0.8236 0.4243 0.5225 0.0211  -0.0417 0.0263  9   LEU C CB  
8530  C CG  . LEU C 9   ? 0.8101 0.4154 0.5177 0.0251  -0.0216 0.0312  9   LEU C CG  
8531  C CD1 . LEU C 9   ? 0.8513 0.4483 0.5489 0.0272  -0.0090 0.0273  9   LEU C CD1 
8532  C CD2 . LEU C 9   ? 0.7399 0.3717 0.4882 0.0233  -0.0194 0.0335  9   LEU C CD2 
8533  N N   . LYS C 10  ? 0.8152 0.4376 0.5441 0.0113  -0.0878 0.0235  10  LYS C N   
8534  C CA  . LYS C 10  ? 0.8259 0.4446 0.5492 0.0078  -0.1077 0.0211  10  LYS C CA  
8535  C C   . LYS C 10  ? 0.7933 0.4369 0.5546 0.0033  -0.1152 0.0185  10  LYS C C   
8536  O O   . LYS C 10  ? 0.8008 0.4636 0.5903 0.0040  -0.1081 0.0209  10  LYS C O   
8537  C CB  . LYS C 10  ? 0.9106 0.5227 0.6228 0.0100  -0.1160 0.0272  10  LYS C CB  
8538  C CG  . LYS C 10  ? 0.9705 0.5773 0.6750 0.0070  -0.1377 0.0258  10  LYS C CG  
8539  C CD  . LYS C 10  ? 1.0731 0.6721 0.7654 0.0099  -0.1455 0.0326  10  LYS C CD  
8540  C CE  . LYS C 10  ? 1.1325 0.7291 0.8221 0.0069  -0.1682 0.0317  10  LYS C CE  
8541  N NZ  . LYS C 10  ? 1.1623 0.7436 0.8295 0.0036  -0.1763 0.0249  10  LYS C NZ  
8542  N N   . ASP C 11  ? 0.8241 0.4666 0.5855 -0.0012 -0.1285 0.0135  11  ASP C N   
8543  C CA  . ASP C 11  ? 0.7897 0.4544 0.5853 -0.0059 -0.1349 0.0109  11  ASP C CA  
8544  C C   . ASP C 11  ? 0.7383 0.4163 0.5535 -0.0057 -0.1196 0.0092  11  ASP C C   
8545  O O   . ASP C 11  ? 0.7094 0.4094 0.5566 -0.0076 -0.1195 0.0093  11  ASP C O   
8546  C CB  . ASP C 11  ? 0.8324 0.5140 0.6524 -0.0062 -0.1447 0.0147  11  ASP C CB  
8547  C CG  . ASP C 11  ? 0.9084 0.5772 0.7099 -0.0058 -0.1605 0.0173  11  ASP C CG  
8548  O OD1 . ASP C 11  ? 0.9693 0.6231 0.7504 -0.0086 -0.1716 0.0138  11  ASP C OD1 
8549  O OD2 . ASP C 11  ? 1.0024 0.6754 0.8095 -0.0027 -0.1621 0.0227  11  ASP C OD2 
8550  N N   . ASN C 12  ? 0.7431 0.4072 0.5386 -0.0032 -0.1067 0.0078  12  ASN C N   
8551  C CA  . ASN C 12  ? 0.7061 0.3803 0.5172 -0.0024 -0.0920 0.0067  12  ASN C CA  
8552  C C   . ASN C 12  ? 0.6684 0.3612 0.5044 0.0000  -0.0824 0.0113  12  ASN C C   
8553  O O   . ASN C 12  ? 0.6037 0.3120 0.4625 -0.0007 -0.0752 0.0104  12  ASN C O   
8554  C CB  . ASN C 12  ? 0.6832 0.3668 0.5108 -0.0075 -0.0975 0.0019  12  ASN C CB  
8555  C CG  . ASN C 12  ? 0.6927 0.3565 0.4958 -0.0102 -0.1063 -0.0030 12  ASN C CG  
8556  O OD1 . ASN C 12  ? 0.7200 0.3610 0.4906 -0.0075 -0.1039 -0.0040 12  ASN C OD1 
8557  N ND2 . ASN C 12  ? 0.6843 0.3560 0.5025 -0.0157 -0.1158 -0.0063 12  ASN C ND2 
8558  N N   . TRP C 13  ? 0.6647 0.3543 0.4948 0.0031  -0.0822 0.0163  13  TRP C N   
8559  C CA  . TRP C 13  ? 0.6647 0.3691 0.5162 0.0053  -0.0741 0.0207  13  TRP C CA  
8560  C C   . TRP C 13  ? 0.6567 0.3473 0.4889 0.0099  -0.0634 0.0257  13  TRP C C   
8561  O O   . TRP C 13  ? 0.6741 0.3462 0.4785 0.0114  -0.0675 0.0274  13  TRP C O   
8562  C CB  . TRP C 13  ? 0.6531 0.3705 0.5235 0.0043  -0.0856 0.0228  13  TRP C CB  
8563  C CG  . TRP C 13  ? 0.6129 0.3514 0.5136 0.0008  -0.0914 0.0197  13  TRP C CG  
8564  C CD1 . TRP C 13  ? 0.6019 0.3441 0.5077 -0.0033 -0.1028 0.0160  13  TRP C CD1 
8565  C CD2 . TRP C 13  ? 0.5619 0.3206 0.4920 0.0011  -0.0857 0.0204  13  TRP C CD2 
8566  N NE1 . TRP C 13  ? 0.5649 0.3287 0.5014 -0.0052 -0.1037 0.0148  13  TRP C NE1 
8567  C CE2 . TRP C 13  ? 0.5364 0.3100 0.4869 -0.0024 -0.0935 0.0171  13  TRP C CE2 
8568  C CE3 . TRP C 13  ? 0.5542 0.3191 0.4948 0.0039  -0.0751 0.0234  13  TRP C CE3 
8569  C CZ2 . TRP C 13  ? 0.5146 0.3082 0.4934 -0.0027 -0.0903 0.0165  13  TRP C CZ2 
8570  C CZ3 . TRP C 13  ? 0.5240 0.3083 0.4927 0.0032  -0.0731 0.0223  13  TRP C CZ3 
8571  C CH2 . TRP C 13  ? 0.5031 0.3012 0.4895 0.0002  -0.0804 0.0189  13  TRP C CH2 
8572  N N   . TYR C 14  ? 0.6287 0.3290 0.4767 0.0118  -0.0504 0.0286  14  TYR C N   
8573  C CA  . TYR C 14  ? 0.6345 0.3273 0.4737 0.0154  -0.0418 0.0348  14  TYR C CA  
8574  C C   . TYR C 14  ? 0.6173 0.3155 0.4657 0.0153  -0.0519 0.0385  14  TYR C C   
8575  O O   . TYR C 14  ? 0.5758 0.2915 0.4504 0.0134  -0.0584 0.0370  14  TYR C O   
8576  C CB  . TYR C 14  ? 0.6300 0.3324 0.4865 0.0170  -0.0262 0.0371  14  TYR C CB  
8577  C CG  . TYR C 14  ? 0.6350 0.3315 0.4833 0.0185  -0.0135 0.0352  14  TYR C CG  
8578  C CD1 . TYR C 14  ? 0.6274 0.3294 0.4825 0.0164  -0.0149 0.0295  14  TYR C CD1 
8579  C CD2 . TYR C 14  ? 0.6548 0.3414 0.4914 0.0221  0.0008  0.0398  14  TYR C CD2 
8580  C CE1 . TYR C 14  ? 0.6318 0.3283 0.4808 0.0184  -0.0032 0.0282  14  TYR C CE1 
8581  C CE2 . TYR C 14  ? 0.6380 0.3200 0.4694 0.0242  0.0133  0.0385  14  TYR C CE2 
8582  C CZ  . TYR C 14  ? 0.6429 0.3299 0.4807 0.0225  0.0110  0.0325  14  TYR C CZ  
8583  O OH  . TYR C 14  ? 0.6506 0.3329 0.4843 0.0250  0.0233  0.0314  14  TYR C OH  
8584  N N   . HIS C 15  ? 0.6598 0.3414 0.4844 0.0178  -0.0533 0.0432  15  HIS C N   
8585  C CA  . HIS C 15  ? 0.6685 0.3512 0.4980 0.0190  -0.0595 0.0486  15  HIS C CA  
8586  C C   . HIS C 15  ? 0.6681 0.3444 0.4926 0.0220  -0.0450 0.0552  15  HIS C C   
8587  O O   . HIS C 15  ? 0.7069 0.3676 0.5070 0.0241  -0.0354 0.0567  15  HIS C O   
8588  C CB  . HIS C 15  ? 0.6954 0.3617 0.4985 0.0194  -0.0732 0.0498  15  HIS C CB  
8589  C CG  . HIS C 15  ? 0.7246 0.3958 0.5319 0.0160  -0.0884 0.0439  15  HIS C CG  
8590  N ND1 . HIS C 15  ? 0.7126 0.3842 0.5177 0.0134  -0.0878 0.0375  15  HIS C ND1 
8591  C CD2 . HIS C 15  ? 0.7384 0.4157 0.5552 0.0146  -0.1046 0.0438  15  HIS C CD2 
8592  C CE1 . HIS C 15  ? 0.7140 0.3918 0.5274 0.0101  -0.1029 0.0339  15  HIS C CE1 
8593  N NE2 . HIS C 15  ? 0.7099 0.3919 0.5312 0.0108  -0.1131 0.0376  15  HIS C NE2 
8594  N N   . LEU C 16  ? 0.6358 0.3242 0.4842 0.0223  -0.0429 0.0588  16  LEU C N   
8595  C CA  . LEU C 16  ? 0.6522 0.3345 0.4982 0.0246  -0.0316 0.0662  16  LEU C CA  
8596  C C   . LEU C 16  ? 0.6591 0.3364 0.5023 0.0258  -0.0412 0.0714  16  LEU C C   
8597  O O   . LEU C 16  ? 0.6333 0.3245 0.5002 0.0247  -0.0500 0.0698  16  LEU C O   
8598  C CB  . LEU C 16  ? 0.6256 0.3245 0.5020 0.0237  -0.0212 0.0664  16  LEU C CB  
8599  C CG  . LEU C 16  ? 0.6443 0.3431 0.5195 0.0240  -0.0061 0.0656  16  LEU C CG  
8600  C CD1 . LEU C 16  ? 0.6341 0.3283 0.4945 0.0235  -0.0084 0.0593  16  LEU C CD1 
8601  C CD2 . LEU C 16  ? 0.6279 0.3454 0.5358 0.0224  0.0008  0.0645  16  LEU C CD2 
8602  N N   . ASP C 17  ? 0.7111 0.3683 0.5252 0.0284  -0.0389 0.0777  17  ASP C N   
8603  C CA  . ASP C 17  ? 0.7286 0.3766 0.5333 0.0301  -0.0482 0.0838  17  ASP C CA  
8604  C C   . ASP C 17  ? 0.7364 0.3926 0.5511 0.0288  -0.0670 0.0797  17  ASP C C   
8605  O O   . ASP C 17  ? 0.7240 0.3907 0.5612 0.0290  -0.0734 0.0813  17  ASP C O   
8606  C CB  . ASP C 17  ? 0.7235 0.3766 0.5474 0.0309  -0.0413 0.0904  17  ASP C CB  
8607  C CG  . ASP C 17  ? 0.7182 0.3664 0.5392 0.0316  -0.0224 0.0953  17  ASP C CG  
8608  O OD1 . ASP C 17  ? 0.7273 0.3592 0.5190 0.0333  -0.0144 0.0975  17  ASP C OD1 
8609  O OD2 . ASP C 17  ? 0.6915 0.3525 0.5402 0.0304  -0.0158 0.0965  17  ASP C OD2 
8610  N N   . GLY C 18  ? 0.7519 0.4038 0.5519 0.0275  -0.0755 0.0741  18  GLY C N   
8611  C CA  . GLY C 18  ? 0.7520 0.4100 0.5590 0.0261  -0.0939 0.0708  18  GLY C CA  
8612  C C   . GLY C 18  ? 0.7255 0.4069 0.5664 0.0231  -0.0974 0.0638  18  GLY C C   
8613  O O   . GLY C 18  ? 0.7640 0.4499 0.6084 0.0213  -0.1108 0.0600  18  GLY C O   
8614  N N   . GLU C 19  ? 0.7069 0.4024 0.5713 0.0225  -0.0855 0.0623  19  GLU C N   
8615  C CA  . GLU C 19  ? 0.6882 0.4061 0.5859 0.0204  -0.0879 0.0570  19  GLU C CA  
8616  C C   . GLU C 19  ? 0.6667 0.3915 0.5683 0.0177  -0.0818 0.0506  19  GLU C C   
8617  O O   . GLU C 19  ? 0.7178 0.4385 0.6131 0.0181  -0.0686 0.0511  19  GLU C O   
8618  C CB  . GLU C 19  ? 0.7059 0.4344 0.6273 0.0216  -0.0793 0.0595  19  GLU C CB  
8619  C CG  . GLU C 19  ? 0.7565 0.4796 0.6793 0.0243  -0.0839 0.0660  19  GLU C CG  
8620  C CD  . GLU C 19  ? 0.8311 0.5593 0.7617 0.0249  -0.1004 0.0650  19  GLU C CD  
8621  O OE1 . GLU C 19  ? 0.9472 0.6932 0.9045 0.0240  -0.1037 0.0604  19  GLU C OE1 
8622  O OE2 . GLU C 19  ? 0.8873 0.6022 0.7975 0.0261  -0.1100 0.0685  19  GLU C OE2 
8623  N N   . LYS C 20  ? 0.6075 0.3441 0.5224 0.0150  -0.0903 0.0450  20  LYS C N   
8624  C CA  . LYS C 20  ? 0.5993 0.3424 0.5192 0.0125  -0.0839 0.0396  20  LYS C CA  
8625  C C   . LYS C 20  ? 0.5727 0.3277 0.5125 0.0130  -0.0710 0.0396  20  LYS C C   
8626  O O   . LYS C 20  ? 0.5452 0.3118 0.5063 0.0137  -0.0716 0.0406  20  LYS C O   
8627  C CB  . LYS C 20  ? 0.5851 0.3407 0.5197 0.0092  -0.0940 0.0342  20  LYS C CB  
8628  C CG  . LYS C 20  ? 0.6163 0.3601 0.5318 0.0079  -0.1073 0.0336  20  LYS C CG  
8629  C CD  . LYS C 20  ? 0.6373 0.3910 0.5649 0.0038  -0.1173 0.0286  20  LYS C CD  
8630  C CE  . LYS C 20  ? 0.7013 0.4402 0.6071 0.0027  -0.1312 0.0288  20  LYS C CE  
8631  N NZ  . LYS C 20  ? 0.7070 0.4550 0.6256 -0.0018 -0.1420 0.0246  20  LYS C NZ  
8632  N N   . TYR C 21  ? 0.5706 0.3226 0.5042 0.0126  -0.0600 0.0382  21  TYR C N   
8633  C CA  . TYR C 21  ? 0.5365 0.2969 0.4855 0.0133  -0.0476 0.0392  21  TYR C CA  
8634  C C   . TYR C 21  ? 0.5252 0.2930 0.4810 0.0114  -0.0421 0.0344  21  TYR C C   
8635  O O   . TYR C 21  ? 0.5702 0.3272 0.5085 0.0118  -0.0366 0.0338  21  TYR C O   
8636  C CB  . TYR C 21  ? 0.5555 0.3021 0.4886 0.0158  -0.0367 0.0449  21  TYR C CB  
8637  C CG  . TYR C 21  ? 0.5329 0.2886 0.4852 0.0162  -0.0255 0.0471  21  TYR C CG  
8638  C CD1 . TYR C 21  ? 0.5340 0.2950 0.5016 0.0168  -0.0264 0.0504  21  TYR C CD1 
8639  C CD2 . TYR C 21  ? 0.5257 0.2836 0.4806 0.0161  -0.0143 0.0461  21  TYR C CD2 
8640  C CE1 . TYR C 21  ? 0.5172 0.2858 0.5026 0.0166  -0.0172 0.0522  21  TYR C CE1 
8641  C CE2 . TYR C 21  ? 0.5260 0.2925 0.4996 0.0161  -0.0052 0.0483  21  TYR C CE2 
8642  C CZ  . TYR C 21  ? 0.5243 0.2960 0.5130 0.0161  -0.0070 0.0512  21  TYR C CZ  
8643  O OH  . TYR C 21  ? 0.5337 0.3134 0.5413 0.0155  0.0010  0.0530  21  TYR C OH  
8644  N N   . PHE C 22  ? 0.4901 0.2755 0.4707 0.0097  -0.0435 0.0312  22  PHE C N   
8645  C CA  . PHE C 22  ? 0.4837 0.2774 0.4730 0.0081  -0.0387 0.0274  22  PHE C CA  
8646  C C   . PHE C 22  ? 0.4848 0.2802 0.4804 0.0094  -0.0262 0.0297  22  PHE C C   
8647  O O   . PHE C 22  ? 0.4704 0.2734 0.4815 0.0100  -0.0240 0.0316  22  PHE C O   
8648  C CB  . PHE C 22  ? 0.4728 0.2838 0.4844 0.0060  -0.0454 0.0237  22  PHE C CB  
8649  C CG  . PHE C 22  ? 0.4525 0.2708 0.4704 0.0038  -0.0425 0.0198  22  PHE C CG  
8650  C CD1 . PHE C 22  ? 0.4437 0.2694 0.4729 0.0041  -0.0337 0.0195  22  PHE C CD1 
8651  C CD2 . PHE C 22  ? 0.4794 0.2960 0.4913 0.0014  -0.0490 0.0168  22  PHE C CD2 
8652  C CE1 . PHE C 22  ? 0.4479 0.2792 0.4817 0.0024  -0.0313 0.0166  22  PHE C CE1 
8653  C CE2 . PHE C 22  ? 0.4676 0.2897 0.4847 -0.0006 -0.0461 0.0138  22  PHE C CE2 
8654  C CZ  . PHE C 22  ? 0.4522 0.2813 0.4795 0.0001  -0.0372 0.0139  22  PHE C CZ  
8655  N N   . ILE C 23  ? 0.4902 0.2792 0.4757 0.0099  -0.0183 0.0293  23  ILE C N   
8656  C CA  . ILE C 23  ? 0.4854 0.2766 0.4785 0.0113  -0.0064 0.0319  23  ILE C CA  
8657  C C   . ILE C 23  ? 0.4467 0.2549 0.4632 0.0096  -0.0055 0.0288  23  ILE C C   
8658  O O   . ILE C 23  ? 0.3988 0.2105 0.4162 0.0084  -0.0062 0.0253  23  ILE C O   
8659  C CB  . ILE C 23  ? 0.5382 0.3153 0.5115 0.0134  0.0027  0.0331  23  ILE C CB  
8660  C CG1 . ILE C 23  ? 0.5636 0.3219 0.5092 0.0152  0.0011  0.0356  23  ILE C CG1 
8661  C CG2 . ILE C 23  ? 0.5385 0.3195 0.5231 0.0150  0.0153  0.0366  23  ILE C CG2 
8662  C CD1 . ILE C 23  ? 0.5897 0.3323 0.5119 0.0172  0.0081  0.0349  23  ILE C CD1 
8663  N N   . LYS C 24  ? 0.4508 0.2684 0.4852 0.0096  -0.0044 0.0304  24  LYS C N   
8664  C CA  . LYS C 24  ? 0.4405 0.2731 0.4965 0.0083  -0.0032 0.0283  24  LYS C CA  
8665  C C   . LYS C 24  ? 0.4434 0.2760 0.5058 0.0094  0.0073  0.0317  24  LYS C C   
8666  O O   . LYS C 24  ? 0.4545 0.2899 0.5278 0.0094  0.0096  0.0345  24  LYS C O   
8667  C CB  . LYS C 24  ? 0.4326 0.2741 0.5033 0.0075  -0.0097 0.0272  24  LYS C CB  
8668  C CG  . LYS C 24  ? 0.4525 0.2956 0.5201 0.0068  -0.0196 0.0242  24  LYS C CG  
8669  C CD  . LYS C 24  ? 0.4465 0.3012 0.5317 0.0065  -0.0250 0.0218  24  LYS C CD  
8670  C CE  . LYS C 24  ? 0.5020 0.3523 0.5887 0.0080  -0.0271 0.0247  24  LYS C CE  
8671  N NZ  . LYS C 24  ? 0.5488 0.4099 0.6538 0.0081  -0.0302 0.0219  24  LYS C NZ  
8672  N N   . ALA C 25  ? 0.4597 0.2898 0.5169 0.0101  0.0133  0.0314  25  ALA C N   
8673  C CA  . ALA C 25  ? 0.4509 0.2801 0.5133 0.0118  0.0239  0.0353  25  ALA C CA  
8674  C C   . ALA C 25  ? 0.4502 0.2924 0.5309 0.0108  0.0250  0.0334  25  ALA C C   
8675  O O   . ALA C 25  ? 0.4649 0.3153 0.5513 0.0091  0.0180  0.0292  25  ALA C O   
8676  C CB  . ALA C 25  ? 0.4941 0.3088 0.5356 0.0144  0.0312  0.0370  25  ALA C CB  
8677  N N   . ILE C 26  ? 0.4401 0.2841 0.5305 0.0121  0.0338  0.0372  26  ILE C N   
8678  C CA  . ILE C 26  ? 0.4166 0.2710 0.5226 0.0120  0.0358  0.0364  26  ILE C CA  
8679  C C   . ILE C 26  ? 0.4055 0.2547 0.5109 0.0150  0.0476  0.0409  26  ILE C C   
8680  O O   . ILE C 26  ? 0.3811 0.2234 0.4824 0.0163  0.0543  0.0453  26  ILE C O   
8681  C CB  . ILE C 26  ? 0.4358 0.3036 0.5641 0.0096  0.0311  0.0360  26  ILE C CB  
8682  C CG1 . ILE C 26  ? 0.4038 0.2823 0.5457 0.0091  0.0300  0.0343  26  ILE C CG1 
8683  C CG2 . ILE C 26  ? 0.4437 0.3113 0.5827 0.0095  0.0363  0.0410  26  ILE C CG2 
8684  C CD1 . ILE C 26  ? 0.4004 0.2907 0.5604 0.0066  0.0235  0.0325  26  ILE C CD1 
8685  N N   . GLY C 27  ? 0.4074 0.2589 0.5151 0.0164  0.0504  0.0398  27  GLY C N   
8686  C CA  . GLY C 27  ? 0.3940 0.2437 0.5066 0.0197  0.0617  0.0439  27  GLY C CA  
8687  C C   . GLY C 27  ? 0.3752 0.2359 0.5124 0.0187  0.0648  0.0483  27  GLY C C   
8688  O O   . GLY C 27  ? 0.3777 0.2504 0.5315 0.0158  0.0570  0.0466  27  GLY C O   
8689  N N   . TYR C 28  ? 0.3635 0.2195 0.5023 0.0211  0.0759  0.0539  28  TYR C N   
8690  C CA  . TYR C 28  ? 0.3550 0.2203 0.5174 0.0197  0.0792  0.0588  28  TYR C CA  
8691  C C   . TYR C 28  ? 0.3733 0.2371 0.5424 0.0235  0.0934  0.0645  28  TYR C C   
8692  O O   . TYR C 28  ? 0.3909 0.2422 0.5431 0.0266  0.1032  0.0673  28  TYR C O   
8693  C CB  . TYR C 28  ? 0.3684 0.2289 0.5266 0.0175  0.0777  0.0608  28  TYR C CB  
8694  C CG  . TYR C 28  ? 0.3630 0.2312 0.5452 0.0158  0.0820  0.0665  28  TYR C CG  
8695  C CD1 . TYR C 28  ? 0.3688 0.2517 0.5771 0.0134  0.0772  0.0661  28  TYR C CD1 
8696  C CD2 . TYR C 28  ? 0.3818 0.2424 0.5611 0.0165  0.0914  0.0728  28  TYR C CD2 
8697  C CE1 . TYR C 28  ? 0.3656 0.2557 0.5979 0.0112  0.0804  0.0713  28  TYR C CE1 
8698  C CE2 . TYR C 28  ? 0.3922 0.2602 0.5957 0.0143  0.0955  0.0786  28  TYR C CE2 
8699  C CZ  . TYR C 28  ? 0.3774 0.2605 0.6085 0.0114  0.0896  0.0776  28  TYR C CZ  
8700  O OH  . TYR C 28  ? 0.3788 0.2699 0.6361 0.0087  0.0922  0.0830  28  TYR C OH  
8701  N N   . GLU C 29  ? 0.3812 0.2580 0.5756 0.0236  0.0946  0.0666  29  GLU C N   
8702  C CA  . GLU C 29  ? 0.3919 0.2697 0.5974 0.0275  0.1082  0.0724  29  GLU C CA  
8703  C C   . GLU C 29  ? 0.3873 0.2784 0.6242 0.0249  0.1094  0.0779  29  GLU C C   
8704  O O   . GLU C 29  ? 0.3851 0.2895 0.6436 0.0227  0.1017  0.0769  29  GLU C O   
8705  C CB  . GLU C 29  ? 0.3965 0.2766 0.6030 0.0309  0.1086  0.0700  29  GLU C CB  
8706  C CG  . GLU C 29  ? 0.4047 0.2883 0.6274 0.0355  0.1219  0.0758  29  GLU C CG  
8707  C CD  . GLU C 29  ? 0.4102 0.2933 0.6317 0.0399  0.1238  0.0739  29  GLU C CD  
8708  O OE1 . GLU C 29  ? 0.3713 0.2637 0.6032 0.0383  0.1134  0.0709  29  GLU C OE1 
8709  O OE2 . GLU C 29  ? 0.4183 0.2904 0.6272 0.0453  0.1367  0.0756  29  GLU C OE2 
8710  N N   . ILE C 30  ? 0.4121 0.2988 0.6506 0.0247  0.1184  0.0837  30  ILE C N   
8711  C CA  . ILE C 30  ? 0.3888 0.2868 0.6581 0.0225  0.1226  0.0902  30  ILE C CA  
8712  C C   . ILE C 30  ? 0.3872 0.2922 0.6743 0.0268  0.1334  0.0947  30  ILE C C   
8713  O O   . ILE C 30  ? 0.4106 0.3075 0.6812 0.0322  0.1413  0.0937  30  ILE C O   
8714  C CB  . ILE C 30  ? 0.3958 0.2856 0.6601 0.0213  0.1305  0.0959  30  ILE C CB  
8715  C CG1 . ILE C 30  ? 0.3746 0.2765 0.6724 0.0170  0.1310  0.1020  30  ILE C CG1 
8716  C CG2 . ILE C 30  ? 0.4321 0.3093 0.6780 0.0271  0.1475  0.1003  30  ILE C CG2 
8717  C CD1 . ILE C 30  ? 0.3482 0.2616 0.6641 0.0114  0.1142  0.0973  30  ILE C CD1 
8718  N N   . GLY C 31  ? 0.3573 0.2773 0.6789 0.0243  0.1329  0.0994  31  GLY C N   
8719  C CA  . GLY C 31  ? 0.3667 0.2962 0.7116 0.0281  0.1422  0.1046  31  GLY C CA  
8720  C C   . GLY C 31  ? 0.3606 0.2959 0.7079 0.0306  0.1350  0.0999  31  GLY C C   
8721  O O   . GLY C 31  ? 0.3542 0.2920 0.7100 0.0358  0.1442  0.1029  31  GLY C O   
8722  N N   . ALA C 32  ? 0.3390 0.2769 0.6806 0.0268  0.1185  0.0931  32  ALA C N   
8723  C CA  . ALA C 32  ? 0.3287 0.2710 0.6697 0.0285  0.1103  0.0887  32  ALA C CA  
8724  C C   . ALA C 32  ? 0.2911 0.2466 0.6511 0.0232  0.0940  0.0862  32  ALA C C   
8725  O O   . ALA C 32  ? 0.2624 0.2193 0.6150 0.0229  0.0837  0.0810  32  ALA C O   
8726  C CB  . ALA C 32  ? 0.3541 0.2826 0.6607 0.0300  0.1075  0.0820  32  ALA C CB  
8727  N N   . ARG C 33  ? 0.2772 0.2419 0.6622 0.0190  0.0922  0.0903  33  ARG C N   
8728  C CA  . ARG C 33  ? 0.2777 0.2551 0.6840 0.0143  0.0775  0.0886  33  ARG C CA  
8729  C C   . ARG C 33  ? 0.2754 0.2635 0.7004 0.0174  0.0757  0.0908  33  ARG C C   
8730  O O   . ARG C 33  ? 0.2802 0.2676 0.7088 0.0231  0.0878  0.0951  33  ARG C O   
8731  C CB  . ARG C 33  ? 0.2964 0.2811 0.7285 0.0093  0.0769  0.0934  33  ARG C CB  
8732  C CG  . ARG C 33  ? 0.3109 0.2903 0.7318 0.0038  0.0671  0.0884  33  ARG C CG  
8733  C CD  . ARG C 33  ? 0.3115 0.2755 0.7001 0.0053  0.0727  0.0857  33  ARG C CD  
8734  N NE  . ARG C 33  ? 0.3008 0.2616 0.6851 0.0001  0.0632  0.0819  33  ARG C NE  
8735  C CZ  . ARG C 33  ? 0.2967 0.2456 0.6582 0.0001  0.0653  0.0800  33  ARG C CZ  
8736  N NH1 . ARG C 33  ? 0.3087 0.2472 0.6478 0.0046  0.0756  0.0810  33  ARG C NH1 
8737  N NH2 . ARG C 33  ? 0.2894 0.2360 0.6501 -0.0042 0.0567  0.0770  33  ARG C NH2 
8738  N N   . PRO C 34  ? 0.2506 0.2484 0.6884 0.0140  0.0604  0.0882  34  PRO C N   
8739  C CA  . PRO C 34  ? 0.2547 0.2638 0.7145 0.0165  0.0574  0.0914  34  PRO C CA  
8740  C C   . PRO C 34  ? 0.2593 0.2769 0.7495 0.0182  0.0688  0.1002  34  PRO C C   
8741  O O   . PRO C 34  ? 0.2608 0.2810 0.7647 0.0141  0.0711  0.1033  34  PRO C O   
8742  C CB  . PRO C 34  ? 0.2441 0.2611 0.7125 0.0112  0.0387  0.0875  34  PRO C CB  
8743  C CG  . PRO C 34  ? 0.2402 0.2464 0.6793 0.0080  0.0329  0.0799  34  PRO C CG  
8744  C CD  . PRO C 34  ? 0.2414 0.2391 0.6727 0.0081  0.0456  0.0821  34  PRO C CD  
8745  N N   . GLY C 35  ? 0.2835 0.3040 0.7821 0.0245  0.0776  0.1044  35  GLY C N   
8746  C CA  . GLY C 35  ? 0.3073 0.3376 0.8378 0.0271  0.0892  0.1132  35  GLY C CA  
8747  C C   . GLY C 35  ? 0.3218 0.3420 0.8408 0.0316  0.1099  0.1168  35  GLY C C   
8748  O O   . GLY C 35  ? 0.3349 0.3619 0.8776 0.0350  0.1229  0.1245  35  GLY C O   
8749  N N   . GLN C 36  ? 0.3390 0.3431 0.8218 0.0316  0.1127  0.1115  36  GLN C N   
8750  C CA  . GLN C 36  ? 0.3545 0.3461 0.8198 0.0356  0.1307  0.1139  36  GLN C CA  
8751  C C   . GLN C 36  ? 0.3664 0.3450 0.8030 0.0424  0.1369  0.1100  36  GLN C C   
8752  O O   . GLN C 36  ? 0.3470 0.3234 0.7699 0.0423  0.1257  0.1040  36  GLN C O   
8753  C CB  . GLN C 36  ? 0.3640 0.3454 0.8087 0.0308  0.1294  0.1113  36  GLN C CB  
8754  C CG  . GLN C 36  ? 0.3570 0.3480 0.8268 0.0237  0.1235  0.1148  36  GLN C CG  
8755  C CD  . GLN C 36  ? 0.3712 0.3507 0.8211 0.0200  0.1249  0.1135  36  GLN C CD  
8756  O OE1 . GLN C 36  ? 0.3561 0.3237 0.7748 0.0196  0.1198  0.1070  36  GLN C OE1 
8757  N NE2 . GLN C 36  ? 0.4121 0.3953 0.8813 0.0169  0.1316  0.1202  36  GLN C NE2 
8758  N N   . ALA C 37  ? 0.3947 0.3640 0.8219 0.0482  0.1553  0.1135  37  ALA C N   
8759  C CA  . ALA C 37  ? 0.4163 0.3696 0.8125 0.0546  0.1631  0.1096  37  ALA C CA  
8760  C C   . ALA C 37  ? 0.4390 0.3770 0.8119 0.0567  0.1782  0.1110  37  ALA C C   
8761  O O   . ALA C 37  ? 0.4634 0.4024 0.8482 0.0609  0.1947  0.1178  37  ALA C O   
8762  C CB  . ALA C 37  ? 0.4315 0.3898 0.8440 0.0619  0.1708  0.1128  37  ALA C CB  
8763  N N   . PRO C 38  ? 0.4342 0.3578 0.7734 0.0541  0.1733  0.1053  38  PRO C N   
8764  C CA  . PRO C 38  ? 0.4665 0.3759 0.7837 0.0553  0.1857  0.1072  38  PRO C CA  
8765  C C   . PRO C 38  ? 0.5121 0.4077 0.8120 0.0638  0.2045  0.1090  38  PRO C C   
8766  O O   . PRO C 38  ? 0.5173 0.4037 0.8059 0.0654  0.2175  0.1130  38  PRO C O   
8767  C CB  . PRO C 38  ? 0.4485 0.3471 0.7357 0.0507  0.1728  0.0999  38  PRO C CB  
8768  C CG  . PRO C 38  ? 0.4474 0.3486 0.7311 0.0506  0.1600  0.0934  38  PRO C CG  
8769  C CD  . PRO C 38  ? 0.4210 0.3414 0.7421 0.0503  0.1564  0.0971  38  PRO C CD  
8770  N N   . TYR C 39  ? 0.5413 0.4349 0.8393 0.0694  0.2064  0.1064  39  TYR C N   
8771  C CA  . TYR C 39  ? 0.5837 0.4626 0.8636 0.0780  0.2240  0.1070  39  TYR C CA  
8772  C C   . TYR C 39  ? 0.6001 0.4913 0.9133 0.0839  0.2377  0.1144  39  TYR C C   
8773  O O   . TYR C 39  ? 0.6368 0.5174 0.9394 0.0920  0.2531  0.1151  39  TYR C O   
8774  C CB  . TYR C 39  ? 0.5889 0.4529 0.8388 0.0809  0.2181  0.0985  39  TYR C CB  
8775  C CG  . TYR C 39  ? 0.5877 0.4386 0.8040 0.0756  0.2064  0.0917  39  TYR C CG  
8776  C CD1 . TYR C 39  ? 0.5930 0.4279 0.7811 0.0760  0.2139  0.0917  39  TYR C CD1 
8777  C CD2 . TYR C 39  ? 0.5505 0.4057 0.7643 0.0704  0.1879  0.0858  39  TYR C CD2 
8778  C CE1 . TYR C 39  ? 0.6058 0.4299 0.7659 0.0713  0.2024  0.0860  39  TYR C CE1 
8779  C CE2 . TYR C 39  ? 0.5426 0.3875 0.7292 0.0657  0.1775  0.0801  39  TYR C CE2 
8780  C CZ  . TYR C 39  ? 0.5678 0.3974 0.7282 0.0662  0.1843  0.0802  39  TYR C CZ  
8781  O OH  . TYR C 39  ? 0.5528 0.3730 0.6881 0.0618  0.1733  0.0749  39  TYR C OH  
8782  N N   . GLU C 40  ? 0.6446 0.5575 0.9983 0.0802  0.2325  0.1199  40  GLU C N   
8783  C CA  . GLU C 40  ? 0.6535 0.5800 1.0429 0.0854  0.2452  0.1279  40  GLU C CA  
8784  C C   . GLU C 40  ? 0.6056 0.5471 1.0268 0.0807  0.2491  0.1364  40  GLU C C   
8785  O O   . GLU C 40  ? 0.5956 0.5416 1.0353 0.0854  0.2667  0.1440  40  GLU C O   
8786  C CB  . GLU C 40  ? 0.6727 0.6129 1.0871 0.0869  0.2347  0.1271  40  GLU C CB  
8787  C CG  . GLU C 40  ? 0.7837 0.7097 1.1752 0.0946  0.2386  0.1218  40  GLU C CG  
8788  C CD  . GLU C 40  ? 0.8501 0.7843 1.2513 0.0929  0.2208  0.1180  40  GLU C CD  
8789  O OE1 . GLU C 40  ? 0.8727 0.8210 1.2915 0.0851  0.2053  0.1185  40  GLU C OE1 
8790  O OE2 . GLU C 40  ? 0.8446 0.7710 1.2360 0.0989  0.2221  0.1149  40  GLU C OE2 
8791  N N   . ASP C 41  ? 0.5969 0.5459 1.0249 0.0715  0.2332  0.1351  41  ASP C N   
8792  C CA  . ASP C 41  ? 0.6155 0.5770 1.0724 0.0660  0.2355  0.1427  41  ASP C CA  
8793  C C   . ASP C 41  ? 0.6239 0.5718 1.0611 0.0674  0.2528  0.1469  41  ASP C C   
8794  O O   . ASP C 41  ? 0.6148 0.5429 1.0111 0.0692  0.2553  0.1419  41  ASP C O   
8795  C CB  . ASP C 41  ? 0.6242 0.5930 1.0874 0.0561  0.2144  0.1393  41  ASP C CB  
8796  C CG  . ASP C 41  ? 0.6274 0.6089 1.1068 0.0532  0.1948  0.1348  41  ASP C CG  
8797  O OD1 . ASP C 41  ? 0.6032 0.5927 1.0998 0.0583  0.1965  0.1363  41  ASP C OD1 
8798  O OD2 . ASP C 41  ? 0.6638 0.6457 1.1361 0.0462  0.1780  0.1297  41  ASP C OD2 
8799  N N   . GLU C 42  ? 0.6039 0.5626 1.0712 0.0660  0.2639  0.1566  42  GLU C N   
8800  C CA  . GLU C 42  ? 0.6486 0.5971 1.1025 0.0649  0.2772  0.1619  42  GLU C CA  
8801  C C   . GLU C 42  ? 0.6544 0.5934 1.0836 0.0573  0.2620  0.1564  42  GLU C C   
8802  O O   . GLU C 42  ? 0.6113 0.5600 1.0534 0.0504  0.2427  0.1526  42  GLU C O   
8803  C CB  . GLU C 42  ? 0.6956 0.6620 1.1952 0.0630  0.2876  0.1733  42  GLU C CB  
8804  C CG  . GLU C 42  ? 0.7530 0.7139 1.2492 0.0583  0.2960  0.1799  42  GLU C CG  
8805  C CD  . GLU C 42  ? 0.7820 0.7535 1.3117 0.0604  0.3168  0.1924  42  GLU C CD  
8806  O OE1 . GLU C 42  ? 0.8739 0.8533 1.4221 0.0676  0.3285  0.1956  42  GLU C OE1 
8807  O OE2 . GLU C 42  ? 0.7556 0.7271 1.2932 0.0550  0.3217  0.1993  42  GLU C OE2 
8808  N N   . ARG C 43  ? 0.6898 0.6093 1.0826 0.0589  0.2711  0.1562  43  ARG C N   
8809  C CA  . ARG C 43  ? 0.7400 0.6476 1.1033 0.0535  0.2574  0.1503  43  ARG C CA  
8810  C C   . ARG C 43  ? 0.6559 0.5701 1.0386 0.0456  0.2539  0.1562  43  ARG C C   
8811  O O   . ARG C 43  ? 0.6807 0.5978 1.0799 0.0458  0.2690  0.1658  43  ARG C O   
8812  C CB  . ARG C 43  ? 0.8646 0.7479 1.1807 0.0591  0.2681  0.1478  43  ARG C CB  
8813  C CG  . ARG C 43  ? 0.9262 0.7962 1.2060 0.0578  0.2522  0.1371  43  ARG C CG  
8814  C CD  . ARG C 43  ? 0.9934 0.8390 1.2278 0.0617  0.2615  0.1361  43  ARG C CD  
8815  N NE  . ARG C 43  ? 0.9623 0.8045 1.1954 0.0572  0.2639  0.1423  43  ARG C NE  
8816  C CZ  . ARG C 43  ? 0.9519 0.7919 1.1767 0.0507  0.2484  0.1393  43  ARG C CZ  
8817  N NH1 . ARG C 43  ? 0.8246 0.6553 1.0220 0.0500  0.2342  0.1301  43  ARG C NH1 
8818  N NH2 . ARG C 43  ? 0.8880 0.7334 1.1306 0.0453  0.2488  0.1462  43  ARG C NH2 
8819  N N   . LYS C 44  ? 0.6073 0.5239 0.9888 0.0386  0.2340  0.1506  44  LYS C N   
8820  C CA  . LYS C 44  ? 0.6064 0.5267 1.0024 0.0308  0.2280  0.1545  44  LYS C CA  
8821  C C   . LYS C 44  ? 0.5478 0.4545 0.9112 0.0275  0.2144  0.1473  44  LYS C C   
8822  O O   . LYS C 44  ? 0.5083 0.4109 0.8519 0.0285  0.2026  0.1382  44  LYS C O   
8823  C CB  . LYS C 44  ? 0.6433 0.5846 1.0819 0.0246  0.2147  0.1550  44  LYS C CB  
8824  C CG  . LYS C 44  ? 0.6911 0.6488 1.1721 0.0252  0.2263  0.1645  44  LYS C CG  
8825  C CD  . LYS C 44  ? 0.7092 0.6871 1.2307 0.0189  0.2105  0.1640  44  LYS C CD  
8826  C CE  . LYS C 44  ? 0.7719 0.7673 1.3349 0.0211  0.2205  0.1722  44  LYS C CE  
8827  N NZ  . LYS C 44  ? 0.7910 0.7881 1.3720 0.0209  0.2397  0.1839  44  LYS C NZ  
8828  N N   . ASP C 45  ? 0.5235 0.4239 0.8840 0.0233  0.2158  0.1520  45  ASP C N   
8829  C CA  . ASP C 45  ? 0.5178 0.4058 0.8508 0.0202  0.2036  0.1466  45  ASP C CA  
8830  C C   . ASP C 45  ? 0.4852 0.3827 0.8290 0.0148  0.1816  0.1381  45  ASP C C   
8831  O O   . ASP C 45  ? 0.4613 0.3507 0.7791 0.0152  0.1705  0.1300  45  ASP C O   
8832  C CB  . ASP C 45  ? 0.5279 0.4079 0.8595 0.0170  0.2106  0.1546  45  ASP C CB  
8833  C CG  . ASP C 45  ? 0.5585 0.4226 0.8639 0.0228  0.2304  0.1612  45  ASP C CG  
8834  O OD1 . ASP C 45  ? 0.6134 0.4681 0.8917 0.0292  0.2354  0.1570  45  ASP C OD1 
8835  O OD2 . ASP C 45  ? 0.5823 0.4429 0.8942 0.0209  0.2407  0.1705  45  ASP C OD2 
8836  N N   . GLU C 46  ? 0.4646 0.3788 0.8466 0.0099  0.1753  0.1401  46  GLU C N   
8837  C CA  . GLU C 46  ? 0.4429 0.3665 0.8369 0.0050  0.1553  0.1325  46  GLU C CA  
8838  C C   . GLU C 46  ? 0.4181 0.3315 0.7943 0.0010  0.1443  0.1284  46  GLU C C   
8839  O O   . GLU C 46  ? 0.4015 0.3137 0.7643 0.0002  0.1303  0.1196  46  GLU C O   
8840  C CB  . GLU C 46  ? 0.4571 0.3831 0.8391 0.0089  0.1485  0.1244  46  GLU C CB  
8841  C CG  . GLU C 46  ? 0.4995 0.4354 0.8998 0.0134  0.1580  0.1280  46  GLU C CG  
8842  C CD  . GLU C 46  ? 0.5132 0.4655 0.9397 0.0108  0.1443  0.1243  46  GLU C CD  
8843  O OE1 . GLU C 46  ? 0.6305 0.5934 1.0847 0.0048  0.1359  0.1261  46  GLU C OE1 
8844  O OE2 . GLU C 46  ? 0.5003 0.4534 0.9172 0.0147  0.1411  0.1194  46  GLU C OE2 
8845  N N   . LEU C 47  ? 0.4273 0.3335 0.8040 -0.0014 0.1510  0.1353  47  LEU C N   
8846  C CA  . LEU C 47  ? 0.4396 0.3339 0.7969 -0.0040 0.1427  0.1325  47  LEU C CA  
8847  C C   . LEU C 47  ? 0.4459 0.3474 0.8159 -0.0094 0.1233  0.1249  47  LEU C C   
8848  O O   . LEU C 47  ? 0.4266 0.3210 0.7746 -0.0090 0.1129  0.1175  47  LEU C O   
8849  C CB  . LEU C 47  ? 0.4598 0.3459 0.8196 -0.0059 0.1538  0.1425  47  LEU C CB  
8850  C CG  . LEU C 47  ? 0.4916 0.3676 0.8321 0.0001  0.1735  0.1496  47  LEU C CG  
8851  C CD1 . LEU C 47  ? 0.4926 0.3585 0.8308 -0.0015 0.1845  0.1596  47  LEU C CD1 
8852  C CD2 . LEU C 47  ? 0.5095 0.3731 0.8097 0.0059  0.1715  0.1423  47  LEU C CD2 
8853  N N   . GLU C 48  ? 0.4420 0.3571 0.8470 -0.0142 0.1185  0.1265  48  GLU C N   
8854  C CA  . GLU C 48  ? 0.4214 0.3420 0.8380 -0.0193 0.1004  0.1192  48  GLU C CA  
8855  C C   . GLU C 48  ? 0.4198 0.3435 0.8215 -0.0167 0.0892  0.1089  48  GLU C C   
8856  O O   . GLU C 48  ? 0.4446 0.3643 0.8339 -0.0182 0.0767  0.1013  48  GLU C O   
8857  C CB  . GLU C 48  ? 0.4093 0.3434 0.8659 -0.0249 0.0974  0.1233  48  GLU C CB  
8858  C CG  . GLU C 48  ? 0.4263 0.3562 0.8978 -0.0287 0.1068  0.1332  48  GLU C CG  
8859  C CD  . GLU C 48  ? 0.4427 0.3586 0.8973 -0.0310 0.1008  0.1312  48  GLU C CD  
8860  O OE1 . GLU C 48  ? 0.4123 0.3277 0.8631 -0.0333 0.0850  0.1222  48  GLU C OE1 
8861  O OE2 . GLU C 48  ? 0.4824 0.3879 0.9287 -0.0305 0.1121  0.1390  48  GLU C OE2 
8862  N N   . LEU C 49  ? 0.4032 0.3336 0.8059 -0.0127 0.0940  0.1088  49  LEU C N   
8863  C CA  . LEU C 49  ? 0.4043 0.3369 0.7925 -0.0105 0.0840  0.0998  49  LEU C CA  
8864  C C   . LEU C 49  ? 0.4177 0.3364 0.7697 -0.0071 0.0843  0.0954  49  LEU C C   
8865  O O   . LEU C 49  ? 0.4102 0.3282 0.7488 -0.0070 0.0732  0.0874  49  LEU C O   
8866  C CB  . LEU C 49  ? 0.4010 0.3429 0.7986 -0.0067 0.0891  0.1010  49  LEU C CB  
8867  C CG  . LEU C 49  ? 0.3770 0.3349 0.8100 -0.0101 0.0830  0.1027  49  LEU C CG  
8868  C CD1 . LEU C 49  ? 0.3770 0.3430 0.8168 -0.0054 0.0882  0.1041  49  LEU C CD1 
8869  C CD2 . LEU C 49  ? 0.3692 0.3307 0.8047 -0.0146 0.0644  0.0946  49  LEU C CD2 
8870  N N   . MET C 50  ? 0.4575 0.3653 0.7937 -0.0041 0.0972  0.1010  50  MET C N   
8871  C CA  . MET C 50  ? 0.4778 0.3718 0.7795 -0.0008 0.0973  0.0975  50  MET C CA  
8872  C C   . MET C 50  ? 0.4660 0.3546 0.7605 -0.0041 0.0858  0.0934  50  MET C C   
8873  O O   . MET C 50  ? 0.4799 0.3641 0.7543 -0.0027 0.0779  0.0866  50  MET C O   
8874  C CB  . MET C 50  ? 0.5006 0.3825 0.7855 0.0030  0.1131  0.1047  50  MET C CB  
8875  C CG  . MET C 50  ? 0.5217 0.4036 0.7986 0.0084  0.1233  0.1053  50  MET C CG  
8876  S SD  . MET C 50  ? 0.5533 0.4168 0.7994 0.0139  0.1402  0.1110  50  MET C SD  
8877  C CE  . MET C 50  ? 0.5350 0.3850 0.7448 0.0145  0.1281  0.1030  50  MET C CE  
8878  N N   . LYS C 51  ? 0.4624 0.3511 0.7739 -0.0083 0.0852  0.0978  51  LYS C N   
8879  C CA  . LYS C 51  ? 0.4504 0.3330 0.7571 -0.0112 0.0751  0.0945  51  LYS C CA  
8880  C C   . LYS C 51  ? 0.4059 0.2957 0.7154 -0.0127 0.0598  0.0846  51  LYS C C   
8881  O O   . LYS C 51  ? 0.4058 0.2898 0.6986 -0.0119 0.0520  0.0789  51  LYS C O   
8882  C CB  . LYS C 51  ? 0.4412 0.3238 0.7703 -0.0161 0.0759  0.1005  51  LYS C CB  
8883  C CG  . LYS C 51  ? 0.4780 0.3513 0.8034 -0.0153 0.0903  0.1110  51  LYS C CG  
8884  C CD  . LYS C 51  ? 0.4841 0.3593 0.8369 -0.0208 0.0923  0.1180  51  LYS C CD  
8885  C CE  . LYS C 51  ? 0.5170 0.3852 0.8686 -0.0198 0.1091  0.1296  51  LYS C CE  
8886  N NZ  . LYS C 51  ? 0.5402 0.4131 0.9235 -0.0257 0.1116  0.1368  51  LYS C NZ  
8887  N N   . PHE C 52  ? 0.3611 0.2636 0.6925 -0.0148 0.0560  0.0829  52  PHE C N   
8888  C CA  . PHE C 52  ? 0.3451 0.2546 0.6782 -0.0158 0.0427  0.0740  52  PHE C CA  
8889  C C   . PHE C 52  ? 0.3301 0.2365 0.6373 -0.0116 0.0410  0.0683  52  PHE C C   
8890  O O   . PHE C 52  ? 0.3150 0.2191 0.6110 -0.0117 0.0319  0.0616  52  PHE C O   
8891  C CB  . PHE C 52  ? 0.3362 0.2592 0.6951 -0.0179 0.0408  0.0749  52  PHE C CB  
8892  C CG  . PHE C 52  ? 0.3156 0.2462 0.6741 -0.0182 0.0285  0.0664  52  PHE C CG  
8893  C CD1 . PHE C 52  ? 0.2999 0.2313 0.6641 -0.0218 0.0158  0.0603  52  PHE C CD1 
8894  C CD2 . PHE C 52  ? 0.3220 0.2575 0.6734 -0.0147 0.0301  0.0649  52  PHE C CD2 
8895  C CE1 . PHE C 52  ? 0.2999 0.2370 0.6612 -0.0218 0.0054  0.0529  52  PHE C CE1 
8896  C CE2 . PHE C 52  ? 0.3154 0.2570 0.6652 -0.0150 0.0194  0.0579  52  PHE C CE2 
8897  C CZ  . PHE C 52  ? 0.3180 0.2604 0.6720 -0.0185 0.0073  0.0520  52  PHE C CZ  
8898  N N   . ASP C 53  ? 0.3577 0.2637 0.6561 -0.0078 0.0503  0.0711  53  ASP C N   
8899  C CA  . ASP C 53  ? 0.3563 0.2592 0.6319 -0.0041 0.0491  0.0663  53  ASP C CA  
8900  C C   . ASP C 53  ? 0.3569 0.2481 0.6081 -0.0028 0.0470  0.0640  53  ASP C C   
8901  O O   . ASP C 53  ? 0.3479 0.2389 0.5866 -0.0022 0.0389  0.0574  53  ASP C O   
8902  C CB  . ASP C 53  ? 0.3677 0.2704 0.6400 -0.0004 0.0606  0.0706  53  ASP C CB  
8903  C CG  . ASP C 53  ? 0.3600 0.2753 0.6555 -0.0006 0.0618  0.0723  53  ASP C CG  
8904  O OD1 . ASP C 53  ? 0.3152 0.2398 0.6237 -0.0033 0.0509  0.0679  53  ASP C OD1 
8905  O OD2 . ASP C 53  ? 0.3482 0.2633 0.6482 0.0020  0.0737  0.0782  53  ASP C OD2 
8906  N N   . LEU C 54  ? 0.3589 0.2404 0.6036 -0.0023 0.0545  0.0700  54  LEU C N   
8907  C CA  . LEU C 54  ? 0.3804 0.2498 0.6018 -0.0007 0.0529  0.0692  54  LEU C CA  
8908  C C   . LEU C 54  ? 0.3984 0.2687 0.6224 -0.0029 0.0408  0.0638  54  LEU C C   
8909  O O   . LEU C 54  ? 0.3635 0.2304 0.5714 -0.0014 0.0345  0.0589  54  LEU C O   
8910  C CB  . LEU C 54  ? 0.3945 0.2532 0.6096 0.0003  0.0637  0.0777  54  LEU C CB  
8911  C CG  . LEU C 54  ? 0.4038 0.2581 0.6088 0.0039  0.0771  0.0825  54  LEU C CG  
8912  C CD1 . LEU C 54  ? 0.4251 0.2664 0.6178 0.0053  0.0874  0.0905  54  LEU C CD1 
8913  C CD2 . LEU C 54  ? 0.4027 0.2538 0.5861 0.0072  0.0752  0.0770  54  LEU C CD2 
8914  N N   . GLU C 55  ? 0.4133 0.2882 0.6586 -0.0065 0.0374  0.0645  55  GLU C N   
8915  C CA  . GLU C 55  ? 0.4314 0.3074 0.6810 -0.0084 0.0259  0.0585  55  GLU C CA  
8916  C C   . GLU C 55  ? 0.4053 0.2890 0.6506 -0.0075 0.0178  0.0500  55  GLU C C   
8917  O O   . GLU C 55  ? 0.3848 0.2665 0.6201 -0.0065 0.0107  0.0445  55  GLU C O   
8918  C CB  . GLU C 55  ? 0.4688 0.3490 0.7432 -0.0127 0.0233  0.0599  55  GLU C CB  
8919  C CG  . GLU C 55  ? 0.4734 0.3522 0.7520 -0.0145 0.0123  0.0538  55  GLU C CG  
8920  C CD  . GLU C 55  ? 0.5124 0.3800 0.7754 -0.0124 0.0107  0.0539  55  GLU C CD  
8921  O OE1 . GLU C 55  ? 0.5259 0.3850 0.7819 -0.0115 0.0184  0.0614  55  GLU C OE1 
8922  O OE2 . GLU C 55  ? 0.4884 0.3557 0.7465 -0.0114 0.0021  0.0470  55  GLU C OE2 
8923  N N   . ASN C 56  ? 0.3602 0.2530 0.6143 -0.0079 0.0190  0.0493  56  ASN C N   
8924  C CA  . ASN C 56  ? 0.3528 0.2525 0.6025 -0.0072 0.0123  0.0423  56  ASN C CA  
8925  C C   . ASN C 56  ? 0.3352 0.2294 0.5618 -0.0040 0.0127  0.0401  56  ASN C C   
8926  O O   . ASN C 56  ? 0.2810 0.1769 0.5008 -0.0036 0.0056  0.0342  56  ASN C O   
8927  C CB  . ASN C 56  ? 0.3633 0.2722 0.6246 -0.0075 0.0144  0.0433  56  ASN C CB  
8928  C CG  . ASN C 56  ? 0.3520 0.2684 0.6364 -0.0111 0.0094  0.0431  56  ASN C CG  
8929  O OD1 . ASN C 56  ? 0.3463 0.2615 0.6353 -0.0133 0.0020  0.0394  56  ASN C OD1 
8930  N ND2 . ASN C 56  ? 0.3318 0.2557 0.6307 -0.0116 0.0126  0.0465  56  ASN C ND2 
8931  N N   . ILE C 57  ? 0.3569 0.2445 0.5721 -0.0018 0.0213  0.0450  57  ILE C N   
8932  C CA  . ILE C 57  ? 0.3776 0.2596 0.5713 0.0008  0.0215  0.0430  57  ILE C CA  
8933  C C   . ILE C 57  ? 0.3841 0.2593 0.5667 0.0012  0.0159  0.0412  57  ILE C C   
8934  O O   . ILE C 57  ? 0.3597 0.2348 0.5309 0.0022  0.0108  0.0368  57  ILE C O   
8935  C CB  . ILE C 57  ? 0.3967 0.2722 0.5805 0.0031  0.0322  0.0484  57  ILE C CB  
8936  C CG1 . ILE C 57  ? 0.3930 0.2765 0.5858 0.0037  0.0356  0.0482  57  ILE C CG1 
8937  C CG2 . ILE C 57  ? 0.4300 0.2954 0.5890 0.0055  0.0323  0.0473  57  ILE C CG2 
8938  C CD1 . ILE C 57  ? 0.4177 0.2968 0.6097 0.0059  0.0479  0.0545  57  ILE C CD1 
8939  N N   . LYS C 58  ? 0.3910 0.2610 0.5786 0.0003  0.0165  0.0447  58  LYS C N   
8940  C CA  . LYS C 58  ? 0.4088 0.2728 0.5889 0.0010  0.0105  0.0432  58  LYS C CA  
8941  C C   . LYS C 58  ? 0.3772 0.2488 0.5650 0.0002  0.0010  0.0358  58  LYS C C   
8942  O O   . LYS C 58  ? 0.3785 0.2491 0.5569 0.0018  -0.0043 0.0323  58  LYS C O   
8943  C CB  . LYS C 58  ? 0.4320 0.2881 0.6170 0.0002  0.0134  0.0491  58  LYS C CB  
8944  C CG  . LYS C 58  ? 0.4744 0.3190 0.6429 0.0021  0.0212  0.0560  58  LYS C CG  
8945  C CD  . LYS C 58  ? 0.5127 0.3512 0.6892 0.0008  0.0281  0.0639  58  LYS C CD  
8946  C CE  . LYS C 58  ? 0.5080 0.3412 0.6896 -0.0001 0.0228  0.0649  58  LYS C CE  
8947  N NZ  . LYS C 58  ? 0.5144 0.3418 0.7034 -0.0017 0.0313  0.0734  58  LYS C NZ  
8948  N N   . GLU C 59  ? 0.3559 0.2351 0.5606 -0.0020 -0.0010 0.0336  59  GLU C N   
8949  C CA  . GLU C 59  ? 0.3704 0.2560 0.5817 -0.0026 -0.0092 0.0263  59  GLU C CA  
8950  C C   . GLU C 59  ? 0.3883 0.2804 0.5911 -0.0014 -0.0116 0.0214  59  GLU C C   
8951  O O   . GLU C 59  ? 0.4360 0.3315 0.6377 -0.0006 -0.0175 0.0157  59  GLU C O   
8952  C CB  . GLU C 59  ? 0.3867 0.2771 0.6166 -0.0056 -0.0107 0.0258  59  GLU C CB  
8953  C CG  . GLU C 59  ? 0.4444 0.3281 0.6846 -0.0074 -0.0105 0.0293  59  GLU C CG  
8954  C CD  . GLU C 59  ? 0.4924 0.3804 0.7525 -0.0111 -0.0132 0.0286  59  GLU C CD  
8955  O OE1 . GLU C 59  ? 0.5391 0.4356 0.8040 -0.0119 -0.0169 0.0242  59  GLU C OE1 
8956  O OE2 . GLU C 59  ? 0.4363 0.3192 0.7075 -0.0134 -0.0119 0.0328  59  GLU C OE2 
8957  N N   . GLY C 60  ? 0.3387 0.2324 0.5359 -0.0010 -0.0066 0.0237  60  GLY C N   
8958  C CA  . GLY C 60  ? 0.3506 0.2494 0.5399 -0.0002 -0.0085 0.0200  60  GLY C CA  
8959  C C   . GLY C 60  ? 0.3570 0.2508 0.5306 0.0016  -0.0096 0.0194  60  GLY C C   
8960  O O   . GLY C 60  ? 0.3397 0.2370 0.5067 0.0019  -0.0111 0.0166  60  GLY C O   
8961  N N   . GLY C 61  ? 0.3492 0.2343 0.5168 0.0026  -0.0090 0.0225  61  GLY C N   
8962  C CA  . GLY C 61  ? 0.3577 0.2383 0.5126 0.0041  -0.0124 0.0218  61  GLY C CA  
8963  C C   . GLY C 61  ? 0.3905 0.2617 0.5289 0.0051  -0.0083 0.0259  61  GLY C C   
8964  O O   . GLY C 61  ? 0.3865 0.2537 0.5138 0.0061  -0.0123 0.0252  61  GLY C O   
8965  N N   . TYR C 62  ? 0.3885 0.2561 0.5254 0.0051  -0.0005 0.0300  62  TYR C N   
8966  C CA  . TYR C 62  ? 0.3773 0.2353 0.4971 0.0064  0.0048  0.0333  62  TYR C CA  
8967  C C   . TYR C 62  ? 0.3928 0.2389 0.5029 0.0076  0.0069  0.0385  62  TYR C C   
8968  O O   . TYR C 62  ? 0.3838 0.2297 0.5040 0.0071  0.0074  0.0410  62  TYR C O   
8969  C CB  . TYR C 62  ? 0.3794 0.2392 0.5031 0.0066  0.0130  0.0353  62  TYR C CB  
8970  C CG  . TYR C 62  ? 0.3698 0.2406 0.5025 0.0055  0.0105  0.0309  62  TYR C CG  
8971  C CD1 . TYR C 62  ? 0.3829 0.2531 0.5047 0.0059  0.0088  0.0280  62  TYR C CD1 
8972  C CD2 . TYR C 62  ? 0.3545 0.2355 0.5054 0.0040  0.0090  0.0296  62  TYR C CD2 
8973  C CE1 . TYR C 62  ? 0.3362 0.2154 0.4650 0.0050  0.0066  0.0246  62  TYR C CE1 
8974  C CE2 . TYR C 62  ? 0.3564 0.2464 0.5133 0.0033  0.0062  0.0259  62  TYR C CE2 
8975  C CZ  . TYR C 62  ? 0.3384 0.2276 0.4841 0.0038  0.0054  0.0237  62  TYR C CZ  
8976  O OH  . TYR C 62  ? 0.3549 0.2524 0.5060 0.0030  0.0026  0.0206  62  TYR C OH  
8977  N N   . ASN C 63  ? 0.3978 0.2329 0.4872 0.0092  0.0078  0.0401  63  ASN C N   
8978  C CA  . ASN C 63  ? 0.4070 0.2291 0.4831 0.0106  0.0102  0.0455  63  ASN C CA  
8979  C C   . ASN C 63  ? 0.4187 0.2312 0.4818 0.0122  0.0212  0.0500  63  ASN C C   
8980  O O   . ASN C 63  ? 0.4431 0.2437 0.4937 0.0136  0.0257  0.0554  63  ASN C O   
8981  C CB  . ASN C 63  ? 0.4162 0.2321 0.4781 0.0114  0.0011  0.0441  63  ASN C CB  
8982  C CG  . ASN C 63  ? 0.4507 0.2622 0.4958 0.0117  -0.0011 0.0411  63  ASN C CG  
8983  O OD1 . ASN C 63  ? 0.4663 0.2756 0.5055 0.0120  0.0058  0.0410  63  ASN C OD1 
8984  N ND2 . ASN C 63  ? 0.4544 0.2640 0.4918 0.0116  -0.0107 0.0389  63  ASN C ND2 
8985  N N   . THR C 64  ? 0.3954 0.2126 0.4615 0.0123  0.0262  0.0480  64  THR C N   
8986  C CA  . THR C 64  ? 0.4116 0.2194 0.4639 0.0145  0.0367  0.0511  64  THR C CA  
8987  C C   . THR C 64  ? 0.3970 0.2145 0.4655 0.0145  0.0436  0.0508  64  THR C C   
8988  O O   . THR C 64  ? 0.3747 0.2043 0.4577 0.0127  0.0381  0.0464  64  THR C O   
8989  C CB  . THR C 64  ? 0.4209 0.2188 0.4495 0.0157  0.0330  0.0477  64  THR C CB  
8990  O OG1 . THR C 64  ? 0.4487 0.2369 0.4622 0.0159  0.0265  0.0489  64  THR C OG1 
8991  C CG2 . THR C 64  ? 0.4399 0.2261 0.4511 0.0185  0.0434  0.0495  64  THR C CG2 
8992  N N   . ILE C 65  ? 0.3999 0.2117 0.4653 0.0167  0.0558  0.0556  65  ILE C N   
8993  C CA  . ILE C 65  ? 0.3872 0.2061 0.4647 0.0177  0.0628  0.0556  65  ILE C CA  
8994  C C   . ILE C 65  ? 0.4316 0.2380 0.4874 0.0213  0.0703  0.0555  65  ILE C C   
8995  O O   . ILE C 65  ? 0.4573 0.2491 0.4919 0.0235  0.0754  0.0583  65  ILE C O   
8996  C CB  . ILE C 65  ? 0.3671 0.1929 0.4664 0.0174  0.0715  0.0614  65  ILE C CB  
8997  C CG1 . ILE C 65  ? 0.3922 0.2071 0.4826 0.0186  0.0798  0.0683  65  ILE C CG1 
8998  C CG2 . ILE C 65  ? 0.3476 0.1879 0.4717 0.0137  0.0630  0.0595  65  ILE C CG2 
8999  C CD1 . ILE C 65  ? 0.3924 0.2118 0.5011 0.0192  0.0923  0.0751  65  ILE C CD1 
9000  N N   . ARG C 66  ? 0.4402 0.2522 0.5022 0.0222  0.0718  0.0526  66  ARG C N   
9001  C CA  . ARG C 66  ? 0.4507 0.2515 0.4952 0.0259  0.0796  0.0519  66  ARG C CA  
9002  C C   . ARG C 66  ? 0.4401 0.2476 0.5023 0.0283  0.0910  0.0556  66  ARG C C   
9003  O O   . ARG C 66  ? 0.4166 0.2391 0.5025 0.0266  0.0877  0.0550  66  ARG C O   
9004  C CB  . ARG C 66  ? 0.4535 0.2534 0.4884 0.0245  0.0694  0.0451  66  ARG C CB  
9005  C CG  . ARG C 66  ? 0.4697 0.2594 0.4896 0.0277  0.0750  0.0428  66  ARG C CG  
9006  C CD  . ARG C 66  ? 0.4535 0.2529 0.4918 0.0292  0.0801  0.0430  66  ARG C CD  
9007  N NE  . ARG C 66  ? 0.4773 0.2664 0.5002 0.0316  0.0818  0.0393  66  ARG C NE  
9008  C CZ  . ARG C 66  ? 0.4785 0.2570 0.4918 0.0365  0.0936  0.0408  66  ARG C CZ  
9009  N NH1 . ARG C 66  ? 0.5030 0.2785 0.5174 0.0397  0.1055  0.0461  66  ARG C NH1 
9010  N NH2 . ARG C 66  ? 0.4933 0.2626 0.4942 0.0384  0.0940  0.0369  66  ARG C NH2 
9011  N N   . THR C 67  ? 0.4883 0.2845 0.5381 0.0327  0.1041  0.0591  67  THR C N   
9012  C CA  . THR C 67  ? 0.4904 0.2929 0.5582 0.0358  0.1166  0.0635  67  THR C CA  
9013  C C   . THR C 67  ? 0.5136 0.3041 0.5643 0.0411  0.1257  0.0619  67  THR C C   
9014  O O   . THR C 67  ? 0.5178 0.2929 0.5401 0.0422  0.1232  0.0578  67  THR C O   
9015  C CB  . THR C 67  ? 0.4837 0.2858 0.5591 0.0363  0.1270  0.0712  67  THR C CB  
9016  O OG1 . THR C 67  ? 0.4859 0.2689 0.5311 0.0395  0.1344  0.0729  67  THR C OG1 
9017  C CG2 . THR C 67  ? 0.4797 0.2912 0.5707 0.0312  0.1182  0.0728  67  THR C CG2 
9018  N N   . TRP C 68  ? 0.5157 0.3134 0.5849 0.0444  0.1359  0.0651  68  TRP C N   
9019  C CA  . TRP C 68  ? 0.5299 0.3178 0.5878 0.0502  0.1460  0.0639  68  TRP C CA  
9020  C C   . TRP C 68  ? 0.5469 0.3270 0.6011 0.0555  0.1644  0.0702  68  TRP C C   
9021  O O   . TRP C 68  ? 0.5629 0.3283 0.5970 0.0609  0.1740  0.0689  68  TRP C O   
9022  C CB  . TRP C 68  ? 0.4916 0.2932 0.5734 0.0507  0.1434  0.0625  68  TRP C CB  
9023  C CG  . TRP C 68  ? 0.4769 0.2809 0.5541 0.0467  0.1277  0.0559  68  TRP C CG  
9024  C CD1 . TRP C 68  ? 0.4761 0.2687 0.5338 0.0481  0.1244  0.0503  68  TRP C CD1 
9025  C CD2 . TRP C 68  ? 0.4509 0.2677 0.5407 0.0406  0.1135  0.0541  68  TRP C CD2 
9026  N NE1 . TRP C 68  ? 0.4651 0.2640 0.5244 0.0431  0.1096  0.0458  68  TRP C NE1 
9027  C CE2 . TRP C 68  ? 0.4466 0.2599 0.5243 0.0387  0.1030  0.0478  68  TRP C CE2 
9028  C CE3 . TRP C 68  ? 0.4399 0.2698 0.5495 0.0367  0.1090  0.0569  68  TRP C CE3 
9029  C CZ2 . TRP C 68  ? 0.4318 0.2554 0.5172 0.0335  0.0893  0.0448  68  TRP C CZ2 
9030  C CZ3 . TRP C 68  ? 0.3997 0.2381 0.5149 0.0317  0.0949  0.0532  68  TRP C CZ3 
9031  C CH2 . TRP C 68  ? 0.4067 0.2423 0.5099 0.0303  0.0858  0.0473  68  TRP C CH2 
9032  N N   . SER C 69  ? 0.5712 0.3599 0.6429 0.0538  0.1693  0.0769  69  SER C N   
9033  C CA  . SER C 69  ? 0.5814 0.3669 0.6571 0.0583  0.1877  0.0843  69  SER C CA  
9034  C C   . SER C 69  ? 0.5732 0.3554 0.6445 0.0555  0.1899  0.0898  69  SER C C   
9035  O O   . SER C 69  ? 0.5310 0.3235 0.6170 0.0497  0.1786  0.0901  69  SER C O   
9036  C CB  . SER C 69  ? 0.5773 0.3814 0.6908 0.0593  0.1935  0.0887  69  SER C CB  
9037  O OG  . SER C 69  ? 0.6091 0.4101 0.7271 0.0646  0.2130  0.0957  69  SER C OG  
9038  N N   . GLN C 70  ? 0.6147 0.3818 0.6658 0.0601  0.2052  0.0943  70  GLN C N   
9039  C CA  . GLN C 70  ? 0.6383 0.3977 0.6785 0.0586  0.2098  0.1002  70  GLN C CA  
9040  C C   . GLN C 70  ? 0.6346 0.4123 0.7110 0.0536  0.2085  0.1067  70  GLN C C   
9041  O O   . GLN C 70  ? 0.6465 0.4396 0.7554 0.0540  0.2150  0.1106  70  GLN C O   
9042  C CB  . GLN C 70  ? 0.6631 0.4103 0.6905 0.0648  0.2316  0.1071  70  GLN C CB  
9043  C CG  . GLN C 70  ? 0.7165 0.4426 0.7071 0.0715  0.2390  0.1024  70  GLN C CG  
9044  C CD  . GLN C 70  ? 0.6849 0.4159 0.6874 0.0764  0.2455  0.0993  70  GLN C CD  
9045  O OE1 . GLN C 70  ? 0.6513 0.3883 0.6599 0.0747  0.2327  0.0923  70  GLN C OE1 
9046  N NE2 . GLN C 70  ? 0.7024 0.4291 0.7062 0.0830  0.2661  0.1045  70  GLN C NE2 
9047  N N   . TYR C 71  ? 0.6158 0.3899 0.6853 0.0493  0.2014  0.1086  71  TYR C N   
9048  C CA  . TYR C 71  ? 0.5715 0.3579 0.6700 0.0449  0.2027  0.1159  71  TYR C CA  
9049  C C   . TYR C 71  ? 0.5805 0.3575 0.6723 0.0480  0.2218  0.1255  71  TYR C C   
9050  O O   . TYR C 71  ? 0.6026 0.3604 0.6598 0.0528  0.2305  0.1259  71  TYR C O   
9051  C CB  . TYR C 71  ? 0.5474 0.3342 0.6440 0.0390  0.1866  0.1139  71  TYR C CB  
9052  C CG  . TYR C 71  ? 0.5097 0.3102 0.6224 0.0349  0.1687  0.1061  71  TYR C CG  
9053  C CD1 . TYR C 71  ? 0.4813 0.2984 0.6223 0.0345  0.1674  0.1043  71  TYR C CD1 
9054  C CD2 . TYR C 71  ? 0.5002 0.2967 0.5990 0.0317  0.1531  0.1007  71  TYR C CD2 
9055  C CE1 . TYR C 71  ? 0.4579 0.2863 0.6111 0.0308  0.1513  0.0975  71  TYR C CE1 
9056  C CE2 . TYR C 71  ? 0.4693 0.2778 0.5817 0.0283  0.1379  0.0938  71  TYR C CE2 
9057  C CZ  . TYR C 71  ? 0.4617 0.2858 0.6004 0.0277  0.1372  0.0923  71  TYR C CZ  
9058  O OH  . TYR C 71  ? 0.4465 0.2806 0.5947 0.0245  0.1224  0.0855  71  TYR C OH  
9059  N N   . SER C 72  ? 0.5647 0.3553 0.6901 0.0450  0.2276  0.1333  72  SER C N   
9060  C CA  . SER C 72  ? 0.5869 0.3713 0.7122 0.0460  0.2441  0.1439  72  SER C CA  
9061  C C   . SER C 72  ? 0.5991 0.3728 0.7069 0.0420  0.2358  0.1457  72  SER C C   
9062  O O   . SER C 72  ? 0.5594 0.3333 0.6607 0.0386  0.2175  0.1387  72  SER C O   
9063  C CB  . SER C 72  ? 0.5694 0.3734 0.7403 0.0432  0.2516  0.1515  72  SER C CB  
9064  O OG  . SER C 72  ? 0.5314 0.3470 0.7270 0.0355  0.2372  0.1517  72  SER C OG  
9065  N N   . GLU C 73  ? 0.6336 0.3985 0.7357 0.0427  0.2499  0.1557  73  GLU C N   
9066  C CA  . GLU C 73  ? 0.6431 0.3963 0.7286 0.0396  0.2445  0.1594  73  GLU C CA  
9067  C C   . GLU C 73  ? 0.6027 0.3715 0.7211 0.0320  0.2294  0.1587  73  GLU C C   
9068  O O   . GLU C 73  ? 0.6040 0.3689 0.7110 0.0293  0.2129  0.1532  73  GLU C O   
9069  C CB  . GLU C 73  ? 0.6895 0.4307 0.7643 0.0416  0.2634  0.1713  73  GLU C CB  
9070  C CG  . GLU C 73  ? 0.7246 0.4505 0.7756 0.0392  0.2560  0.1744  73  GLU C CG  
9071  C CD  . GLU C 73  ? 0.7709 0.4761 0.7903 0.0432  0.2725  0.1838  73  GLU C CD  
9072  O OE1 . GLU C 73  ? 0.7878 0.4923 0.8107 0.0471  0.2934  0.1906  73  GLU C OE1 
9073  O OE2 . GLU C 73  ? 0.7749 0.4641 0.7648 0.0428  0.2639  0.1839  73  GLU C OE2 
9074  N N   . ASN C 74  ? 0.5748 0.3611 0.7341 0.0289  0.2346  0.1636  74  ASN C N   
9075  C CA  . ASN C 74  ? 0.5452 0.3451 0.7361 0.0215  0.2208  0.1630  74  ASN C CA  
9076  C C   . ASN C 74  ? 0.5371 0.3435 0.7271 0.0198  0.2003  0.1509  74  ASN C C   
9077  O O   . ASN C 74  ? 0.5409 0.3489 0.7361 0.0151  0.1857  0.1479  74  ASN C O   
9078  C CB  . ASN C 74  ? 0.5156 0.3341 0.7511 0.0184  0.2278  0.1690  74  ASN C CB  
9079  C CG  . ASN C 74  ? 0.5238 0.3373 0.7645 0.0192  0.2480  0.1819  74  ASN C CG  
9080  O OD1 . ASN C 74  ? 0.5347 0.3323 0.7525 0.0192  0.2522  0.1873  74  ASN C OD1 
9081  N ND2 . ASN C 74  ? 0.5018 0.3294 0.7738 0.0197  0.2600  0.1872  74  ASN C ND2 
9082  N N   . GLN C 75  ? 0.5120 0.3212 0.6943 0.0238  0.1999  0.1441  75  GLN C N   
9083  C CA  . GLN C 75  ? 0.4937 0.3091 0.6749 0.0223  0.1819  0.1333  75  GLN C CA  
9084  C C   . GLN C 75  ? 0.5024 0.3028 0.6498 0.0225  0.1711  0.1284  75  GLN C C   
9085  O O   . GLN C 75  ? 0.4802 0.2852 0.6329 0.0187  0.1554  0.1230  75  GLN C O   
9086  C CB  . GLN C 75  ? 0.4902 0.3116 0.6726 0.0263  0.1843  0.1282  75  GLN C CB  
9087  C CG  . GLN C 75  ? 0.4842 0.3230 0.7045 0.0257  0.1916  0.1324  75  GLN C CG  
9088  C CD  . GLN C 75  ? 0.4822 0.3257 0.7020 0.0303  0.1933  0.1273  75  GLN C CD  
9089  O OE1 . GLN C 75  ? 0.5131 0.3436 0.7052 0.0360  0.2015  0.1257  75  GLN C OE1 
9090  N NE2 . GLN C 75  ? 0.4591 0.3197 0.7076 0.0277  0.1843  0.1242  75  GLN C NE2 
9091  N N   . LEU C 76  ? 0.5333 0.3161 0.6463 0.0273  0.1795  0.1300  76  LEU C N   
9092  C CA  . LEU C 76  ? 0.5532 0.3205 0.6336 0.0277  0.1702  0.1269  76  LEU C CA  
9093  C C   . LEU C 76  ? 0.5916 0.3575 0.6795 0.0233  0.1635  0.1313  76  LEU C C   
9094  O O   . LEU C 76  ? 0.6366 0.4008 0.7167 0.0214  0.1481  0.1258  76  LEU C O   
9095  C CB  . LEU C 76  ? 0.5853 0.3327 0.6290 0.0334  0.1825  0.1300  76  LEU C CB  
9096  C CG  . LEU C 76  ? 0.5957 0.3371 0.6181 0.0381  0.1837  0.1228  76  LEU C CG  
9097  C CD1 . LEU C 76  ? 0.6267 0.3460 0.6112 0.0433  0.1957  0.1267  76  LEU C CD1 
9098  C CD2 . LEU C 76  ? 0.6074 0.3501 0.6206 0.0363  0.1647  0.1127  76  LEU C CD2 
9099  N N   . LYS C 77  ? 0.5764 0.3423 0.6789 0.0218  0.1752  0.1414  77  LYS C N   
9100  C CA  . LYS C 77  ? 0.5793 0.3419 0.6881 0.0178  0.1696  0.1462  77  LYS C CA  
9101  C C   . LYS C 77  ? 0.5490 0.3244 0.6790 0.0132  0.1513  0.1384  77  LYS C C   
9102  O O   . LYS C 77  ? 0.5698 0.3395 0.6921 0.0115  0.1401  0.1369  77  LYS C O   
9103  C CB  . LYS C 77  ? 0.5964 0.3626 0.7299 0.0150  0.1823  0.1573  77  LYS C CB  
9104  C CG  . LYS C 77  ? 0.6329 0.3841 0.7461 0.0186  0.2013  0.1679  77  LYS C CG  
9105  C CD  . LYS C 77  ? 0.6366 0.3925 0.7766 0.0157  0.2154  0.1798  77  LYS C CD  
9106  C CE  . LYS C 77  ? 0.6801 0.4189 0.7946 0.0198  0.2340  0.1901  77  LYS C CE  
9107  N NZ  . LYS C 77  ? 0.6917 0.4363 0.8319 0.0182  0.2523  0.2019  77  LYS C NZ  
9108  N N   . LEU C 78  ? 0.5352 0.3274 0.6906 0.0117  0.1486  0.1336  78  LEU C N   
9109  C CA  . LEU C 78  ? 0.5215 0.3267 0.6992 0.0073  0.1330  0.1266  78  LEU C CA  
9110  C C   . LEU C 78  ? 0.4984 0.3011 0.6563 0.0086  0.1186  0.1167  78  LEU C C   
9111  O O   . LEU C 78  ? 0.4902 0.2948 0.6529 0.0059  0.1056  0.1125  78  LEU C O   
9112  C CB  . LEU C 78  ? 0.5349 0.3572 0.7418 0.0061  0.1358  0.1253  78  LEU C CB  
9113  C CG  . LEU C 78  ? 0.5580 0.3944 0.7903 0.0014  0.1209  0.1188  78  LEU C CG  
9114  C CD1 . LEU C 78  ? 0.5856 0.4208 0.8349 -0.0036 0.1180  0.1237  78  LEU C CD1 
9115  C CD2 . LEU C 78  ? 0.5615 0.4138 0.8190 0.0009  0.1229  0.1175  78  LEU C CD2 
9116  N N   . VAL C 79  ? 0.4734 0.2721 0.6106 0.0128  0.1213  0.1128  79  VAL C N   
9117  C CA  . VAL C 79  ? 0.4627 0.2586 0.5808 0.0140  0.1090  0.1041  79  VAL C CA  
9118  C C   . VAL C 79  ? 0.4782 0.2599 0.5738 0.0144  0.1031  0.1055  79  VAL C C   
9119  O O   . VAL C 79  ? 0.4670 0.2505 0.5614 0.0130  0.0897  0.1000  79  VAL C O   
9120  C CB  . VAL C 79  ? 0.4540 0.2459 0.5533 0.0182  0.1144  0.1007  79  VAL C CB  
9121  C CG1 . VAL C 79  ? 0.4483 0.2363 0.5276 0.0189  0.1016  0.0924  79  VAL C CG1 
9122  C CG2 . VAL C 79  ? 0.4248 0.2306 0.5468 0.0184  0.1198  0.0996  79  VAL C CG2 
9123  N N   . GLN C 80  ? 0.5367 0.3043 0.6148 0.0165  0.1137  0.1134  80  GLN C N   
9124  C CA  . GLN C 80  ? 0.5860 0.3387 0.6414 0.0173  0.1088  0.1163  80  GLN C CA  
9125  C C   . GLN C 80  ? 0.5955 0.3537 0.6701 0.0134  0.0978  0.1159  80  GLN C C   
9126  O O   . GLN C 80  ? 0.5927 0.3493 0.6593 0.0134  0.0846  0.1107  80  GLN C O   
9127  C CB  . GLN C 80  ? 0.6181 0.3564 0.6573 0.0197  0.1244  0.1265  80  GLN C CB  
9128  C CG  . GLN C 80  ? 0.6442 0.3637 0.6533 0.0215  0.1214  0.1307  80  GLN C CG  
9129  C CD  . GLN C 80  ? 0.6585 0.3671 0.6344 0.0249  0.1141  0.1247  80  GLN C CD  
9130  O OE1 . GLN C 80  ? 0.6300 0.3356 0.5915 0.0278  0.1200  0.1215  80  GLN C OE1 
9131  N NE2 . GLN C 80  ? 0.6494 0.3514 0.6131 0.0246  0.1006  0.1232  80  GLN C NE2 
9132  N N   . GLU C 81  ? 0.6084 0.3733 0.7097 0.0101  0.1029  0.1212  81  GLU C N   
9133  C CA  . GLU C 81  ? 0.6177 0.3852 0.7361 0.0066  0.0934  0.1214  81  GLU C CA  
9134  C C   . GLU C 81  ? 0.5525 0.3333 0.6861 0.0047  0.0791  0.1108  81  GLU C C   
9135  O O   . GLU C 81  ? 0.5398 0.3201 0.6788 0.0033  0.0685  0.1083  81  GLU C O   
9136  C CB  . GLU C 81  ? 0.7131 0.4828 0.8552 0.0032  0.1029  0.1301  81  GLU C CB  
9137  C CG  . GLU C 81  ? 0.8060 0.5934 0.9811 -0.0003 0.1039  0.1274  81  GLU C CG  
9138  C CD  . GLU C 81  ? 0.9589 0.7492 1.1557 -0.0029 0.1173  0.1371  81  GLU C CD  
9139  O OE1 . GLU C 81  ? 1.0737 0.8515 1.2592 -0.0021 0.1270  0.1466  81  GLU C OE1 
9140  O OE2 . GLU C 81  ? 0.9503 0.7553 1.1750 -0.0057 0.1183  0.1358  81  GLU C OE2 
9141  N N   . SER C 82  ? 0.5115 0.3031 0.6501 0.0052  0.0788  0.1046  82  SER C N   
9142  C CA  . SER C 82  ? 0.4598 0.2635 0.6100 0.0038  0.0664  0.0949  82  SER C CA  
9143  C C   . SER C 82  ? 0.4507 0.2492 0.5830 0.0055  0.0545  0.0892  82  SER C C   
9144  O O   . SER C 82  ? 0.4350 0.2417 0.5781 0.0042  0.0440  0.0824  82  SER C O   
9145  C CB  . SER C 82  ? 0.4563 0.2701 0.6102 0.0047  0.0694  0.0904  82  SER C CB  
9146  O OG  . SER C 82  ? 0.4314 0.2384 0.5594 0.0083  0.0701  0.0877  82  SER C OG  
9147  N N   . GLY C 83  ? 0.4686 0.2542 0.5734 0.0087  0.0563  0.0916  83  GLY C N   
9148  C CA  . GLY C 83  ? 0.4634 0.2451 0.5510 0.0105  0.0453  0.0863  83  GLY C CA  
9149  C C   . GLY C 83  ? 0.4618 0.2469 0.5376 0.0121  0.0441  0.0802  83  GLY C C   
9150  O O   . GLY C 83  ? 0.4628 0.2427 0.5211 0.0136  0.0365  0.0769  83  GLY C O   
9151  N N   . LEU C 84  ? 0.4454 0.2388 0.5311 0.0116  0.0509  0.0788  84  LEU C N   
9152  C CA  . LEU C 84  ? 0.4488 0.2456 0.5257 0.0128  0.0490  0.0727  84  LEU C CA  
9153  C C   . LEU C 84  ? 0.4653 0.2479 0.5144 0.0160  0.0560  0.0753  84  LEU C C   
9154  O O   . LEU C 84  ? 0.4701 0.2447 0.5134 0.0174  0.0674  0.0821  84  LEU C O   
9155  C CB  . LEU C 84  ? 0.4324 0.2426 0.5295 0.0116  0.0532  0.0704  84  LEU C CB  
9156  C CG  . LEU C 84  ? 0.4192 0.2439 0.5402 0.0086  0.0444  0.0653  84  LEU C CG  
9157  C CD1 . LEU C 84  ? 0.4030 0.2384 0.5448 0.0074  0.0506  0.0663  84  LEU C CD1 
9158  C CD2 . LEU C 84  ? 0.4072 0.2370 0.5231 0.0086  0.0335  0.0574  84  LEU C CD2 
9159  N N   . LYS C 85  ? 0.4628 0.2427 0.4958 0.0171  0.0499  0.0697  85  LYS C N   
9160  C CA  . LYS C 85  ? 0.4922 0.2580 0.4979 0.0200  0.0557  0.0706  85  LYS C CA  
9161  C C   . LYS C 85  ? 0.4965 0.2674 0.5085 0.0211  0.0650  0.0692  85  LYS C C   
9162  O O   . LYS C 85  ? 0.5072 0.2930 0.5425 0.0192  0.0633  0.0663  85  LYS C O   
9163  C CB  . LYS C 85  ? 0.5057 0.2648 0.4909 0.0204  0.0445  0.0652  85  LYS C CB  
9164  C CG  . LYS C 85  ? 0.5145 0.2696 0.4941 0.0198  0.0333  0.0658  85  LYS C CG  
9165  C CD  . LYS C 85  ? 0.5338 0.2776 0.5050 0.0210  0.0380  0.0739  85  LYS C CD  
9166  C CE  . LYS C 85  ? 0.5305 0.2727 0.5015 0.0204  0.0258  0.0744  85  LYS C CE  
9167  N NZ  . LYS C 85  ? 0.5467 0.2775 0.5102 0.0216  0.0303  0.0828  85  LYS C NZ  
9168  N N   . LEU C 86  ? 0.5172 0.2747 0.5070 0.0244  0.0743  0.0711  86  LEU C N   
9169  C CA  . LEU C 86  ? 0.5189 0.2790 0.5133 0.0265  0.0854  0.0710  86  LEU C CA  
9170  C C   . LEU C 86  ? 0.5366 0.2831 0.5029 0.0293  0.0860  0.0668  86  LEU C C   
9171  O O   . LEU C 86  ? 0.5473 0.2766 0.4852 0.0314  0.0870  0.0682  86  LEU C O   
9172  C CB  . LEU C 86  ? 0.5370 0.2943 0.5370 0.0284  0.1011  0.0792  86  LEU C CB  
9173  C CG  . LEU C 86  ? 0.5533 0.3116 0.5569 0.0317  0.1146  0.0801  86  LEU C CG  
9174  C CD1 . LEU C 86  ? 0.5318 0.3077 0.5619 0.0300  0.1107  0.0758  86  LEU C CD1 
9175  C CD2 . LEU C 86  ? 0.5867 0.3437 0.5988 0.0333  0.1302  0.0891  86  LEU C CD2 
9176  N N   . ILE C 87  ? 0.5290 0.2830 0.5037 0.0293  0.0848  0.0617  87  ILE C N   
9177  C CA  . ILE C 87  ? 0.5404 0.2826 0.4937 0.0323  0.0883  0.0580  87  ILE C CA  
9178  C C   . ILE C 87  ? 0.5478 0.2932 0.5127 0.0356  0.1038  0.0615  87  ILE C C   
9179  O O   . ILE C 87  ? 0.5219 0.2830 0.5127 0.0343  0.1034  0.0604  87  ILE C O   
9180  C CB  . ILE C 87  ? 0.5439 0.2931 0.5015 0.0297  0.0760  0.0505  87  ILE C CB  
9181  C CG1 . ILE C 87  ? 0.5439 0.2904 0.4914 0.0267  0.0614  0.0476  87  ILE C CG1 
9182  C CG2 . ILE C 87  ? 0.5797 0.3191 0.5218 0.0325  0.0804  0.0466  87  ILE C CG2 
9183  C CD1 . ILE C 87  ? 0.5222 0.2779 0.4778 0.0236  0.0494  0.0411  87  ILE C CD1 
9184  N N   . MET C 88  ? 0.5795 0.3109 0.5269 0.0397  0.1173  0.0662  88  MET C N   
9185  C CA  . MET C 88  ? 0.5798 0.3144 0.5400 0.0434  0.1339  0.0709  88  MET C CA  
9186  C C   . MET C 88  ? 0.5884 0.3139 0.5342 0.0478  0.1402  0.0666  88  MET C C   
9187  O O   . MET C 88  ? 0.5790 0.2852 0.4921 0.0504  0.1409  0.0637  88  MET C O   
9188  C CB  . MET C 88  ? 0.6123 0.3372 0.5630 0.0460  0.1475  0.0791  88  MET C CB  
9189  C CG  . MET C 88  ? 0.6271 0.3608 0.6007 0.0487  0.1642  0.0854  88  MET C CG  
9190  S SD  . MET C 88  ? 0.6410 0.3712 0.6179 0.0491  0.1778  0.0966  88  MET C SD  
9191  C CE  . MET C 88  ? 0.6796 0.3808 0.6072 0.0551  0.1881  0.0973  88  MET C CE  
9192  N N   . GLY C 89  ? 0.5769 0.3161 0.5475 0.0485  0.1433  0.0658  89  GLY C N   
9193  C CA  . GLY C 89  ? 0.6266 0.3582 0.5883 0.0533  0.1513  0.0628  89  GLY C CA  
9194  C C   . GLY C 89  ? 0.6592 0.3849 0.6200 0.0592  0.1714  0.0692  89  GLY C C   
9195  O O   . GLY C 89  ? 0.6467 0.3832 0.6290 0.0584  0.1783  0.0763  89  GLY C O   
9196  N N   . ILE C 90  ? 0.6805 0.3878 0.6146 0.0648  0.1804  0.0666  90  ILE C N   
9197  C CA  . ILE C 90  ? 0.7200 0.4212 0.6526 0.0716  0.2010  0.0717  90  ILE C CA  
9198  C C   . ILE C 90  ? 0.7151 0.4235 0.6656 0.0753  0.2061  0.0694  90  ILE C C   
9199  O O   . ILE C 90  ? 0.6659 0.3726 0.6116 0.0743  0.1957  0.0624  90  ILE C O   
9200  C CB  . ILE C 90  ? 0.7957 0.4696 0.6845 0.0762  0.2093  0.0709  90  ILE C CB  
9201  C CG1 . ILE C 90  ? 0.8075 0.4729 0.6760 0.0724  0.2013  0.0728  90  ILE C CG1 
9202  C CG2 . ILE C 90  ? 0.8281 0.4958 0.7154 0.0837  0.2327  0.0769  90  ILE C CG2 
9203  C CD1 . ILE C 90  ? 0.7832 0.4616 0.6745 0.0698  0.2062  0.0819  90  ILE C CD1 
9204  N N   . ASP C 91  ? 0.7600 0.4773 0.7330 0.0795  0.2221  0.0761  91  ASP C N   
9205  C CA  . ASP C 91  ? 0.7541 0.4825 0.7525 0.0832  0.2281  0.0762  91  ASP C CA  
9206  C C   . ASP C 91  ? 0.7811 0.4898 0.7548 0.0917  0.2424  0.0737  91  ASP C C   
9207  O O   . ASP C 91  ? 0.8263 0.5333 0.8050 0.0978  0.2612  0.0793  91  ASP C O   
9208  C CB  . ASP C 91  ? 0.7433 0.4918 0.7803 0.0832  0.2377  0.0852  91  ASP C CB  
9209  C CG  . ASP C 91  ? 0.7752 0.5396 0.8457 0.0864  0.2422  0.0868  91  ASP C CG  
9210  O OD1 . ASP C 91  ? 0.7007 0.4586 0.7632 0.0902  0.2411  0.0812  91  ASP C OD1 
9211  O OD2 . ASP C 91  ? 0.8220 0.6053 0.9275 0.0847  0.2459  0.0939  91  ASP C OD2 
9212  N N   . ILE C 92  ? 0.7786 0.4711 0.7241 0.0921  0.2339  0.0652  92  ILE C N   
9213  C CA  . ILE C 92  ? 0.8476 0.5191 0.7675 0.1000  0.2458  0.0614  92  ILE C CA  
9214  C C   . ILE C 92  ? 0.8353 0.5145 0.7739 0.1015  0.2413  0.0574  92  ILE C C   
9215  O O   . ILE C 92  ? 0.8862 0.5658 0.8211 0.0965  0.2245  0.0514  92  ILE C O   
9216  C CB  . ILE C 92  ? 0.8642 0.5089 0.7364 0.0995  0.2397  0.0547  92  ILE C CB  
9217  C CG1 . ILE C 92  ? 0.8558 0.4935 0.7095 0.0974  0.2413  0.0589  92  ILE C CG1 
9218  C CG2 . ILE C 92  ? 0.9285 0.5491 0.7717 0.1079  0.2520  0.0499  92  ILE C CG2 
9219  C CD1 . ILE C 92  ? 0.8935 0.5204 0.7354 0.1048  0.2641  0.0651  92  ILE C CD1 
9220  N N   . LYS C 93  ? 0.8503 0.5369 0.8114 0.1081  0.2561  0.0615  93  LYS C N   
9221  C CA  . LYS C 93  ? 0.9077 0.6059 0.8942 0.1095  0.2522  0.0599  93  LYS C CA  
9222  C C   . LYS C 93  ? 0.8609 0.5400 0.8201 0.1105  0.2441  0.0505  93  LYS C C   
9223  O O   . LYS C 93  ? 0.8225 0.4787 0.7526 0.1169  0.2545  0.0469  93  LYS C O   
9224  C CB  . LYS C 93  ? 0.9953 0.6991 1.0040 0.1184  0.2717  0.0655  93  LYS C CB  
9225  C CG  . LYS C 93  ? 1.0156 0.7396 1.0580 0.1187  0.2825  0.0756  93  LYS C CG  
9226  C CD  . LYS C 93  ? 1.0279 0.7802 1.1122 0.1120  0.2693  0.0794  93  LYS C CD  
9227  C CE  . LYS C 93  ? 1.0529 0.8227 1.1665 0.1107  0.2780  0.0890  93  LYS C CE  
9228  N NZ  . LYS C 93  ? 0.9874 0.7768 1.1243 0.1013  0.2613  0.0907  93  LYS C NZ  
9229  N N   . PRO C 94  ? 0.8281 0.5146 0.7945 0.1041  0.2254  0.0462  94  PRO C N   
9230  C CA  . PRO C 94  ? 0.8515 0.5194 0.7921 0.1039  0.2170  0.0377  94  PRO C CA  
9231  C C   . PRO C 94  ? 0.8128 0.4700 0.7525 0.1121  0.2271  0.0353  94  PRO C C   
9232  O O   . PRO C 94  ? 0.8192 0.4553 0.7310 0.1131  0.2236  0.0281  94  PRO C O   
9233  C CB  . PRO C 94  ? 0.8273 0.5112 0.7840 0.0948  0.1961  0.0358  94  PRO C CB  
9234  C CG  . PRO C 94  ? 0.8075 0.5193 0.8044 0.0927  0.1962  0.0433  94  PRO C CG  
9235  C CD  . PRO C 94  ? 0.8054 0.5171 0.8029 0.0964  0.2116  0.0492  94  PRO C CD  
9236  N N   . GLU C 95  ? 0.8281 0.4993 0.7983 0.1179  0.2393  0.0415  95  GLU C N   
9237  C CA  . GLU C 95  ? 0.8498 0.5142 0.8257 0.1261  0.2482  0.0402  95  GLU C CA  
9238  C C   . GLU C 95  ? 0.8737 0.5197 0.8309 0.1363  0.2702  0.0406  95  GLU C C   
9239  O O   . GLU C 95  ? 0.8349 0.4727 0.7944 0.1445  0.2804  0.0394  95  GLU C O   
9240  C CB  . GLU C 95  ? 0.8479 0.5371 0.8688 0.1282  0.2499  0.0467  95  GLU C CB  
9241  C CG  . GLU C 95  ? 0.9199 0.6317 0.9655 0.1189  0.2309  0.0484  95  GLU C CG  
9242  C CD  . GLU C 95  ? 1.0405 0.7706 1.1018 0.1127  0.2278  0.0539  95  GLU C CD  
9243  O OE1 . GLU C 95  ? 1.1189 0.8449 1.1726 0.1152  0.2404  0.0571  95  GLU C OE1 
9244  O OE2 . GLU C 95  ? 1.0668 0.8148 1.1473 0.1054  0.2128  0.0549  95  GLU C OE2 
9245  N N   . GLU C 96  ? 0.8622 0.5016 0.8013 0.1362  0.2781  0.0426  96  GLU C N   
9246  C CA  . GLU C 96  ? 0.8915 0.5126 0.8101 0.1460  0.3000  0.0433  96  GLU C CA  
9247  C C   . GLU C 96  ? 0.8907 0.4782 0.7608 0.1485  0.2986  0.0333  96  GLU C C   
9248  O O   . GLU C 96  ? 0.8673 0.4468 0.7184 0.1412  0.2806  0.0270  96  GLU C O   
9249  C CB  . GLU C 96  ? 0.9171 0.5448 0.8365 0.1447  0.3092  0.0505  96  GLU C CB  
9250  C CG  . GLU C 96  ? 0.8999 0.5575 0.8672 0.1448  0.3165  0.0610  96  GLU C CG  
9251  C CD  . GLU C 96  ? 0.9546 0.6153 0.9419 0.1557  0.3386  0.0660  96  GLU C CD  
9252  O OE1 . GLU C 96  ? 0.9520 0.5968 0.9190 0.1634  0.3584  0.0674  96  GLU C OE1 
9253  O OE2 . GLU C 96  ? 1.0004 0.6796 1.0245 0.1569  0.3362  0.0689  96  GLU C OE2 
9254  N N   . ASP C 97  ? 0.9173 0.4849 0.7677 0.1589  0.3182  0.0319  97  ASP C N   
9255  C CA  . ASP C 97  ? 0.9460 0.4789 0.7482 0.1626  0.3195  0.0223  97  ASP C CA  
9256  C C   . ASP C 97  ? 0.9853 0.5035 0.7506 0.1590  0.3178  0.0212  97  ASP C C   
9257  O O   . ASP C 97  ? 0.9941 0.5080 0.7502 0.1642  0.3351  0.0262  97  ASP C O   
9258  C CB  . ASP C 97  ? 0.9432 0.4611 0.7398 0.1757  0.3415  0.0213  97  ASP C CB  
9259  C CG  . ASP C 97  ? 0.9977 0.4770 0.7429 0.1815  0.3467  0.0113  97  ASP C CG  
9260  O OD1 . ASP C 97  ? 0.9896 0.4513 0.7010 0.1749  0.3306  0.0038  97  ASP C OD1 
9261  O OD2 . ASP C 97  ? 1.0571 0.5235 0.7961 0.1931  0.3673  0.0110  97  ASP C OD2 
9262  N N   . TYR C 98  ? 0.9863 0.4963 0.7303 0.1502  0.2969  0.0150  98  TYR C N   
9263  C CA  . TYR C 98  ? 1.0174 0.5167 0.7307 0.1456  0.2916  0.0147  98  TYR C CA  
9264  C C   . TYR C 98  ? 1.0472 0.5132 0.7133 0.1539  0.3066  0.0105  98  TYR C C   
9265  O O   . TYR C 98  ? 1.0730 0.5284 0.7120 0.1527  0.3081  0.0120  98  TYR C O   
9266  C CB  . TYR C 98  ? 1.0270 0.5238 0.7283 0.1350  0.2657  0.0085  98  TYR C CB  
9267  C CG  . TYR C 98  ? 0.9729 0.4990 0.7150 0.1266  0.2494  0.0110  98  TYR C CG  
9268  C CD1 . TYR C 98  ? 0.9326 0.4885 0.7167 0.1255  0.2539  0.0201  98  TYR C CD1 
9269  C CD2 . TYR C 98  ? 0.9740 0.4974 0.7125 0.1198  0.2296  0.0043  98  TYR C CD2 
9270  C CE1 . TYR C 98  ? 0.8952 0.4760 0.7137 0.1183  0.2391  0.0219  98  TYR C CE1 
9271  C CE2 . TYR C 98  ? 0.9296 0.4786 0.7030 0.1126  0.2157  0.0066  98  TYR C CE2 
9272  C CZ  . TYR C 98  ? 0.9107 0.4880 0.7233 0.1121  0.2205  0.0152  98  TYR C CZ  
9273  O OH  . TYR C 98  ? 0.8588 0.4598 0.7031 0.1051  0.2066  0.0171  98  TYR C OH  
9274  N N   . GLY C 99  ? 1.0432 0.4910 0.6971 0.1623  0.3168  0.0049  99  GLY C N   
9275  C CA  . GLY C 99  ? 1.0958 0.5090 0.7013 0.1705  0.3301  -0.0006 99  GLY C CA  
9276  C C   . GLY C 99  ? 1.1152 0.5282 0.7258 0.1819  0.3592  0.0061  99  GLY C C   
9277  O O   . GLY C 99  ? 1.1507 0.5356 0.7204 0.1894  0.3730  0.0027  99  GLY C O   
9278  N N   . ASP C 100 ? 1.1015 0.5447 0.7616 0.1837  0.3687  0.0154  100 ASP C N   
9279  C CA  . ASP C 100 ? 1.1563 0.6032 0.8277 0.1940  0.3964  0.0231  100 ASP C CA  
9280  C C   . ASP C 100 ? 1.2291 0.6758 0.8853 0.1920  0.4038  0.0301  100 ASP C C   
9281  O O   . ASP C 100 ? 1.1901 0.6581 0.8666 0.1826  0.3914  0.0359  100 ASP C O   
9282  C CB  . ASP C 100 ? 1.1174 0.5976 0.8481 0.1956  0.4022  0.0313  100 ASP C CB  
9283  C CG  . ASP C 100 ? 1.1273 0.6172 0.8783 0.2048  0.4299  0.0410  100 ASP C CG  
9284  O OD1 . ASP C 100 ? 1.1777 0.6435 0.8942 0.2135  0.4487  0.0395  100 ASP C OD1 
9285  O OD2 . ASP C 100 ? 1.1196 0.6411 0.9202 0.2030  0.4321  0.0502  100 ASP C OD2 
9286  N N   . PRO C 101 ? 1.3047 0.7265 0.9236 0.2010  0.4243  0.0299  101 PRO C N   
9287  C CA  . PRO C 101 ? 1.3058 0.7224 0.9025 0.1993  0.4308  0.0362  101 PRO C CA  
9288  C C   . PRO C 101 ? 1.2802 0.7298 0.9230 0.1963  0.4388  0.0498  101 PRO C C   
9289  O O   . PRO C 101 ? 1.2876 0.7407 0.9228 0.1900  0.4339  0.0551  101 PRO C O   
9290  C CB  . PRO C 101 ? 1.3792 0.7636 0.9320 0.2116  0.4550  0.0334  101 PRO C CB  
9291  C CG  . PRO C 101 ? 1.4071 0.7918 0.9797 0.2214  0.4684  0.0303  101 PRO C CG  
9292  C CD  . PRO C 101 ? 1.3777 0.7737 0.9720 0.2135  0.4427  0.0237  101 PRO C CD  
9293  N N   . GLU C 102 ? 1.2563 0.7293 0.9467 0.2007  0.4507  0.0556  102 GLU C N   
9294  C CA  . GLU C 102 ? 1.2573 0.7620 0.9946 0.1979  0.4585  0.0685  102 GLU C CA  
9295  C C   . GLU C 102 ? 1.2244 0.7547 0.9922 0.1847  0.4326  0.0703  102 GLU C C   
9296  O O   . GLU C 102 ? 1.1541 0.7032 0.9442 0.1791  0.4327  0.0795  102 GLU C O   
9297  C CB  . GLU C 102 ? 1.2336 0.7565 1.0145 0.2064  0.4779  0.0745  102 GLU C CB  
9298  C CG  . GLU C 102 ? 1.2200 0.7709 1.0436 0.2050  0.4908  0.0886  102 GLU C CG  
9299  C CD  . GLU C 102 ? 1.2414 0.8031 1.0973 0.2160  0.5165  0.0951  102 GLU C CD  
9300  O OE1 . GLU C 102 ? 1.1828 0.7620 1.0760 0.2168  0.5103  0.0941  102 GLU C OE1 
9301  O OE2 . GLU C 102 ? 1.2632 0.8153 1.1067 0.2241  0.5425  0.1010  102 GLU C OE2 
9302  N N   . PHE C 103 ? 1.2025 0.7333 0.9721 0.1800  0.4114  0.0616  103 PHE C N   
9303  C CA  . PHE C 103 ? 1.1172 0.6697 0.9117 0.1681  0.3867  0.0620  103 PHE C CA  
9304  C C   . PHE C 103 ? 1.1447 0.6850 0.9052 0.1605  0.3732  0.0603  103 PHE C C   
9305  O O   . PHE C 103 ? 1.0823 0.6419 0.8640 0.1522  0.3628  0.0658  103 PHE C O   
9306  C CB  . PHE C 103 ? 1.0431 0.5981 0.8468 0.1653  0.3687  0.0536  103 PHE C CB  
9307  C CG  . PHE C 103 ? 0.9563 0.5296 0.7773 0.1530  0.3430  0.0530  103 PHE C CG  
9308  C CD1 . PHE C 103 ? 0.8976 0.5030 0.7666 0.1479  0.3387  0.0608  103 PHE C CD1 
9309  C CD2 . PHE C 103 ? 0.9365 0.4943 0.7254 0.1466  0.3235  0.0447  103 PHE C CD2 
9310  C CE1 . PHE C 103 ? 0.8591 0.4798 0.7420 0.1373  0.3162  0.0597  103 PHE C CE1 
9311  C CE2 . PHE C 103 ? 0.8761 0.4506 0.6811 0.1360  0.3014  0.0443  103 PHE C CE2 
9312  C CZ  . PHE C 103 ? 0.8570 0.4625 0.7081 0.1316  0.2982  0.0515  103 PHE C CZ  
9313  N N   . VAL C 104 ? 1.1707 0.6787 0.8789 0.1633  0.3723  0.0522  104 VAL C N   
9314  C CA  . VAL C 104 ? 1.1836 0.6771 0.8560 0.1574  0.3608  0.0508  104 VAL C CA  
9315  C C   . VAL C 104 ? 1.2187 0.7210 0.8989 0.1576  0.3748  0.0624  104 VAL C C   
9316  O O   . VAL C 104 ? 1.1672 0.6861 0.8645 0.1491  0.3626  0.0674  104 VAL C O   
9317  C CB  . VAL C 104 ? 1.2140 0.6694 0.8276 0.1620  0.3610  0.0411  104 VAL C CB  
9318  C CG1 . VAL C 104 ? 1.2548 0.6950 0.8310 0.1568  0.3505  0.0411  104 VAL C CG1 
9319  C CG2 . VAL C 104 ? 1.2197 0.6667 0.8270 0.1602  0.3446  0.0298  104 VAL C CG2 
9320  N N   . LYS C 105 ? 1.2195 0.7109 0.8889 0.1675  0.4009  0.0667  105 LYS C N   
9321  C CA  . LYS C 105 ? 1.2887 0.7867 0.9652 0.1689  0.4182  0.0785  105 LYS C CA  
9322  C C   . LYS C 105 ? 1.2653 0.7983 0.9941 0.1602  0.4092  0.0870  105 LYS C C   
9323  O O   . LYS C 105 ? 1.3039 0.8402 1.0283 0.1526  0.3977  0.0904  105 LYS C O   
9324  C CB  . LYS C 105 ? 1.3733 0.8660 1.0525 0.1809  0.4490  0.0831  105 LYS C CB  
9325  C CG  . LYS C 105 ? 1.3697 0.8800 1.0782 0.1826  0.4700  0.0975  105 LYS C CG  
9326  C CD  . LYS C 105 ? 1.4344 0.9296 1.1269 0.1951  0.5022  0.1017  105 LYS C CD  
9327  C CE  . LYS C 105 ? 1.4366 0.9423 1.1609 0.2042  0.5191  0.1022  105 LYS C CE  
9328  N NZ  . LYS C 105 ? 1.4176 0.9594 1.2038 0.2011  0.5248  0.1138  105 LYS C NZ  
9329  N N   . ASP C 106 ? 1.2105 0.7685 0.9881 0.1614  0.4137  0.0902  106 ASP C N   
9330  C CA  . ASP C 106 ? 1.1527 0.7434 0.9816 0.1545  0.4092  0.0992  106 ASP C CA  
9331  C C   . ASP C 106 ? 1.0683 0.6674 0.8993 0.1427  0.3823  0.0968  106 ASP C C   
9332  O O   . ASP C 106 ? 0.9549 0.5704 0.8085 0.1367  0.3800  0.1049  106 ASP C O   
9333  C CB  . ASP C 106 ? 1.1092 0.7233 0.9865 0.1573  0.4136  0.1010  106 ASP C CB  
9334  C CG  . ASP C 106 ? 1.1099 0.7261 1.0025 0.1677  0.4423  0.1080  106 ASP C CG  
9335  O OD1 . ASP C 106 ? 1.1781 0.7941 1.0699 0.1692  0.4590  0.1172  106 ASP C OD1 
9336  O OD2 . ASP C 106 ? 1.0671 0.6865 0.9752 0.1741  0.4479  0.1049  106 ASP C OD2 
9337  N N   . SER C 107 ? 1.0251 0.6122 0.8326 0.1400  0.3634  0.0859  107 SER C N   
9338  C CA  . SER C 107 ? 1.0076 0.5993 0.8121 0.1300  0.3375  0.0815  107 SER C CA  
9339  C C   . SER C 107 ? 1.0565 0.6325 0.8266 0.1269  0.3341  0.0838  107 SER C C   
9340  O O   . SER C 107 ? 1.0185 0.6082 0.8039 0.1191  0.3221  0.0877  107 SER C O   
9341  C CB  . SER C 107 ? 0.9947 0.5762 0.7833 0.1291  0.3213  0.0697  107 SER C CB  
9342  O OG  . SER C 107 ? 0.9284 0.5280 0.7533 0.1298  0.3191  0.0682  107 SER C OG  
9343  N N   . GLU C 108 ? 1.0965 0.6432 0.8195 0.1332  0.3447  0.0812  108 GLU C N   
9344  C CA  . GLU C 108 ? 1.1303 0.6588 0.8161 0.1317  0.3437  0.0839  108 GLU C CA  
9345  C C   . GLU C 108 ? 1.1238 0.6666 0.8321 0.1302  0.3559  0.0969  108 GLU C C   
9346  O O   . GLU C 108 ? 1.0938 0.6362 0.7944 0.1243  0.3459  0.1005  108 GLU C O   
9347  C CB  . GLU C 108 ? 1.1910 0.6854 0.8235 0.1402  0.3571  0.0801  108 GLU C CB  
9348  C CG  . GLU C 108 ? 1.2131 0.6874 0.8145 0.1411  0.3437  0.0668  108 GLU C CG  
9349  C CD  . GLU C 108 ? 1.2523 0.6919 0.8017 0.1502  0.3577  0.0619  108 GLU C CD  
9350  O OE1 . GLU C 108 ? 1.2533 0.6886 0.8025 0.1590  0.3832  0.0669  108 GLU C OE1 
9351  O OE2 . GLU C 108 ? 1.2725 0.6892 0.7821 0.1486  0.3428  0.0528  108 GLU C OE2 
9352  N N   . ILE C 109 ? 1.1399 0.6949 0.8767 0.1356  0.3775  0.1040  109 ILE C N   
9353  C CA  . ILE C 109 ? 1.1498 0.7185 0.9109 0.1345  0.3914  0.1169  109 ILE C CA  
9354  C C   . ILE C 109 ? 1.0984 0.6958 0.9042 0.1245  0.3746  0.1205  109 ILE C C   
9355  O O   . ILE C 109 ? 1.1186 0.7206 0.9299 0.1197  0.3736  0.1282  109 ILE C O   
9356  C CB  . ILE C 109 ? 1.1534 0.7298 0.9380 0.1427  0.4184  0.1235  109 ILE C CB  
9357  C CG1 . ILE C 109 ? 1.2246 0.7708 0.9626 0.1535  0.4393  0.1217  109 ILE C CG1 
9358  C CG2 . ILE C 109 ? 1.1154 0.7136 0.9396 0.1393  0.4290  0.1370  109 ILE C CG2 
9359  C CD1 . ILE C 109 ? 1.2231 0.7752 0.9827 0.1631  0.4637  0.1245  109 ILE C CD1 
9360  N N   . GLU C 110 ? 1.0516 0.6680 0.8903 0.1217  0.3626  0.1154  110 GLU C N   
9361  C CA  . GLU C 110 ? 0.9696 0.6116 0.8475 0.1125  0.3453  0.1172  110 GLU C CA  
9362  C C   . GLU C 110 ? 0.9655 0.5987 0.8188 0.1055  0.3240  0.1131  110 GLU C C   
9363  O O   . GLU C 110 ? 0.9773 0.6221 0.8480 0.0991  0.3171  0.1187  110 GLU C O   
9364  C CB  . GLU C 110 ? 0.8939 0.5553 0.8070 0.1118  0.3371  0.1123  110 GLU C CB  
9365  C CG  . GLU C 110 ? 0.8408 0.5291 0.7960 0.1028  0.3204  0.1141  110 GLU C CG  
9366  C CD  . GLU C 110 ? 0.8346 0.5422 0.8269 0.0995  0.3282  0.1254  110 GLU C CD  
9367  O OE1 . GLU C 110 ? 0.8432 0.5457 0.8333 0.1040  0.3489  0.1335  110 GLU C OE1 
9368  O OE2 . GLU C 110 ? 0.8029 0.5306 0.8271 0.0920  0.3136  0.1261  110 GLU C OE2 
9369  N N   . LEU C 111 ? 0.9428 0.5551 0.7563 0.1068  0.3140  0.1037  111 LEU C N   
9370  C CA  . LEU C 111 ? 0.9052 0.5112 0.6992 0.1002  0.2921  0.0992  111 LEU C CA  
9371  C C   . LEU C 111 ? 0.9495 0.5430 0.7202 0.0992  0.2962  0.1065  111 LEU C C   
9372  O O   . LEU C 111 ? 0.9595 0.5617 0.7407 0.0926  0.2832  0.1092  111 LEU C O   
9373  C CB  . LEU C 111 ? 0.8938 0.4804 0.6526 0.1019  0.2812  0.0877  111 LEU C CB  
9374  C CG  . LEU C 111 ? 0.8729 0.4521 0.6106 0.0954  0.2580  0.0824  111 LEU C CG  
9375  C CD1 . LEU C 111 ? 0.8262 0.4301 0.6001 0.0871  0.2409  0.0832  111 LEU C CD1 
9376  C CD2 . LEU C 111 ? 0.8854 0.4490 0.5968 0.0967  0.2479  0.0713  111 LEU C CD2 
9377  N N   . LYS C 112 ? 1.0112 0.5836 0.7498 0.1063  0.3148  0.1098  112 LYS C N   
9378  C CA  . LYS C 112 ? 1.0317 0.5898 0.7446 0.1062  0.3205  0.1175  112 LYS C CA  
9379  C C   . LYS C 112 ? 1.0110 0.5899 0.7634 0.1026  0.3286  0.1293  112 LYS C C   
9380  O O   . LYS C 112 ? 1.0523 0.6277 0.7972 0.0988  0.3244  0.1354  112 LYS C O   
9381  C CB  . LYS C 112 ? 1.0853 0.6171 0.7572 0.1153  0.3420  0.1194  112 LYS C CB  
9382  C CG  . LYS C 112 ? 1.1278 0.6324 0.7511 0.1192  0.3348  0.1081  112 LYS C CG  
9383  C CD  . LYS C 112 ? 1.1728 0.6512 0.7566 0.1293  0.3574  0.1085  112 LYS C CD  
9384  C CE  . LYS C 112 ? 1.2218 0.6687 0.7492 0.1315  0.3471  0.0989  112 LYS C CE  
9385  N NZ  . LYS C 112 ? 1.2880 0.7082 0.7752 0.1415  0.3693  0.0988  112 LYS C NZ  
9386  N N   . ARG C 113 ? 0.9636 0.5629 0.7571 0.1041  0.3408  0.1329  113 ARG C N   
9387  C CA  . ARG C 113 ? 0.9364 0.5573 0.7721 0.0999  0.3469  0.1435  113 ARG C CA  
9388  C C   . ARG C 113 ? 0.9161 0.5505 0.7703 0.0905  0.3229  0.1416  113 ARG C C   
9389  O O   . ARG C 113 ? 0.9597 0.5965 0.8202 0.0861  0.3214  0.1492  113 ARG C O   
9390  C CB  . ARG C 113 ? 0.9077 0.5510 0.7891 0.1020  0.3587  0.1461  113 ARG C CB  
9391  C CG  . ARG C 113 ? 0.8996 0.5625 0.8223 0.0982  0.3684  0.1583  113 ARG C CG  
9392  C CD  . ARG C 113 ? 0.8955 0.5822 0.8655 0.0995  0.3755  0.1597  113 ARG C CD  
9393  N NE  . ARG C 113 ? 0.8673 0.5694 0.8588 0.0951  0.3542  0.1507  113 ARG C NE  
9394  C CZ  . ARG C 113 ? 0.8807 0.6020 0.9036 0.0866  0.3367  0.1508  113 ARG C CZ  
9395  N NH1 . ARG C 113 ? 0.8736 0.6024 0.9144 0.0811  0.3373  0.1594  113 ARG C NH1 
9396  N NH2 . ARG C 113 ? 0.8327 0.5646 0.8683 0.0837  0.3187  0.1420  113 ARG C NH2 
9397  N N   . VAL C 114 ? 0.8801 0.5222 0.7417 0.0878  0.3046  0.1315  114 VAL C N   
9398  C CA  . VAL C 114 ? 0.8694 0.5267 0.7525 0.0795  0.2825  0.1286  114 VAL C CA  
9399  C C   . VAL C 114 ? 0.8588 0.5002 0.7093 0.0766  0.2699  0.1281  114 VAL C C   
9400  O O   . VAL C 114 ? 0.8702 0.5200 0.7367 0.0711  0.2624  0.1330  114 VAL C O   
9401  C CB  . VAL C 114 ? 0.8445 0.5118 0.7397 0.0784  0.2686  0.1181  114 VAL C CB  
9402  C CG1 . VAL C 114 ? 0.8199 0.4964 0.7234 0.0710  0.2443  0.1127  114 VAL C CG1 
9403  C CG2 . VAL C 114 ? 0.8306 0.5189 0.7676 0.0798  0.2780  0.1204  114 VAL C CG2 
9404  N N   . LEU C 115 ? 0.8602 0.4781 0.6659 0.0805  0.2677  0.1223  115 LEU C N   
9405  C CA  . LEU C 115 ? 0.8812 0.4820 0.6523 0.0784  0.2543  0.1209  115 LEU C CA  
9406  C C   . LEU C 115 ? 0.8975 0.4909 0.6608 0.0783  0.2642  0.1323  115 LEU C C   
9407  O O   . LEU C 115 ? 0.9004 0.4855 0.6470 0.0751  0.2521  0.1337  115 LEU C O   
9408  C CB  . LEU C 115 ? 0.9216 0.4967 0.6452 0.0835  0.2539  0.1135  115 LEU C CB  
9409  C CG  . LEU C 115 ? 0.9166 0.4941 0.6397 0.0823  0.2386  0.1014  115 LEU C CG  
9410  C CD1 . LEU C 115 ? 0.9765 0.5254 0.6497 0.0873  0.2390  0.0950  115 LEU C CD1 
9411  C CD2 . LEU C 115 ? 0.8791 0.4692 0.6174 0.0749  0.2147  0.0973  115 LEU C CD2 
9412  N N   . ASN C 116 ? 0.9019 0.4980 0.6773 0.0820  0.2868  0.1405  116 ASN C N   
9413  C CA  . ASN C 116 ? 0.9232 0.5097 0.6879 0.0831  0.3012  0.1523  116 ASN C CA  
9414  C C   . ASN C 116 ? 0.8858 0.4885 0.6829 0.0757  0.2923  0.1589  116 ASN C C   
9415  O O   . ASN C 116 ? 0.9211 0.5122 0.7016 0.0748  0.2943  0.1667  116 ASN C O   
9416  C CB  . ASN C 116 ? 0.9449 0.5325 0.7190 0.0890  0.3284  0.1594  116 ASN C CB  
9417  C CG  . ASN C 116 ? 0.9956 0.5593 0.7309 0.0939  0.3454  0.1677  116 ASN C CG  
9418  O OD1 . ASN C 116 ? 1.0054 0.5534 0.7110 0.0921  0.3365  0.1699  116 ASN C OD1 
9419  N ND2 . ASN C 116 ? 1.0383 0.5987 0.7731 0.1005  0.3702  0.1725  116 ASN C ND2 
9420  N N   . TYR C 117 ? 0.8324 0.4607 0.6751 0.0708  0.2839  0.1564  117 TYR C N   
9421  C CA  . TYR C 117 ? 0.8026 0.4454 0.6750 0.0635  0.2719  0.1602  117 TYR C CA  
9422  C C   . TYR C 117 ? 0.7775 0.4242 0.6479 0.0592  0.2461  0.1500  117 TYR C C   
9423  O O   . TYR C 117 ? 0.7531 0.4011 0.6277 0.0546  0.2335  0.1519  117 TYR C O   
9424  C CB  . TYR C 117 ? 0.7810 0.4483 0.7047 0.0605  0.2803  0.1656  117 TYR C CB  
9425  C CG  . TYR C 117 ? 0.7801 0.4649 0.7302 0.0610  0.2776  0.1579  117 TYR C CG  
9426  C CD1 . TYR C 117 ? 0.7454 0.4452 0.7164 0.0560  0.2573  0.1498  117 TYR C CD1 
9427  C CD2 . TYR C 117 ? 0.8061 0.4915 0.7591 0.0670  0.2954  0.1588  117 TYR C CD2 
9428  C CE1 . TYR C 117 ? 0.7309 0.4454 0.7236 0.0565  0.2541  0.1432  117 TYR C CE1 
9429  C CE2 . TYR C 117 ? 0.7833 0.4841 0.7602 0.0678  0.2922  0.1522  117 TYR C CE2 
9430  C CZ  . TYR C 117 ? 0.7478 0.4629 0.7440 0.0624  0.2712  0.1446  117 TYR C CZ  
9431  O OH  . TYR C 117 ? 0.7320 0.4616 0.7507 0.0630  0.2673  0.1385  117 TYR C OH  
9432  N N   . ALA C 118 ? 0.7510 0.3980 0.6132 0.0611  0.2386  0.1395  118 ALA C N   
9433  C CA  . ALA C 118 ? 0.7380 0.3936 0.6074 0.0566  0.2158  0.1303  118 ALA C CA  
9434  C C   . ALA C 118 ? 0.7532 0.3927 0.5906 0.0554  0.2014  0.1288  118 ALA C C   
9435  O O   . ALA C 118 ? 0.7223 0.3705 0.5717 0.0507  0.1835  0.1250  118 ALA C O   
9436  C CB  . ALA C 118 ? 0.7413 0.3995 0.6085 0.0590  0.2129  0.1205  118 ALA C CB  
9437  N N   . LYS C 119 ? 0.7872 0.4031 0.5837 0.0600  0.2095  0.1318  119 LYS C N   
9438  C CA  . LYS C 119 ? 0.8155 0.4132 0.5763 0.0598  0.1960  0.1301  119 LYS C CA  
9439  C C   . LYS C 119 ? 0.8211 0.4210 0.5912 0.0558  0.1891  0.1376  119 LYS C C   
9440  O O   . LYS C 119 ? 0.8415 0.4289 0.5874 0.0552  0.1759  0.1369  119 LYS C O   
9441  C CB  . LYS C 119 ? 0.8499 0.4203 0.5636 0.0659  0.2081  0.1330  119 LYS C CB  
9442  C CG  . LYS C 119 ? 0.8599 0.4229 0.5694 0.0683  0.2284  0.1456  119 LYS C CG  
9443  C CD  . LYS C 119 ? 0.9146 0.4516 0.5784 0.0754  0.2437  0.1473  119 LYS C CD  
9444  C CE  . LYS C 119 ? 0.9471 0.4783 0.6094 0.0781  0.2665  0.1601  119 LYS C CE  
9445  N NZ  . LYS C 119 ? 0.9932 0.5001 0.6122 0.0856  0.2830  0.1610  119 LYS C NZ  
9446  N N   . LYS C 120 ? 0.8070 0.4211 0.6109 0.0534  0.1985  0.1453  120 LYS C N   
9447  C CA  . LYS C 120 ? 0.8136 0.4300 0.6297 0.0493  0.1919  0.1522  120 LYS C CA  
9448  C C   . LYS C 120 ? 0.7644 0.3999 0.6119 0.0439  0.1728  0.1457  120 LYS C C   
9449  O O   . LYS C 120 ? 0.7827 0.4206 0.6413 0.0406  0.1648  0.1497  120 LYS C O   
9450  C CB  . LYS C 120 ? 0.8154 0.4374 0.6542 0.0486  0.2103  0.1637  120 LYS C CB  
9451  C CG  . LYS C 120 ? 0.8758 0.4805 0.6867 0.0543  0.2319  0.1710  120 LYS C CG  
9452  C CD  . LYS C 120 ? 0.9077 0.5173 0.7410 0.0532  0.2505  0.1837  120 LYS C CD  
9453  C CE  . LYS C 120 ? 0.8921 0.5263 0.7734 0.0506  0.2577  0.1837  120 LYS C CE  
9454  N NZ  . LYS C 120 ? 0.9260 0.5614 0.8233 0.0499  0.2765  0.1971  120 LYS C NZ  
9455  N N   . TYR C 121 ? 0.7262 0.3740 0.5862 0.0433  0.1656  0.1358  121 TYR C N   
9456  C CA  . TYR C 121 ? 0.6973 0.3653 0.5906 0.0385  0.1512  0.1300  121 TYR C CA  
9457  C C   . TYR C 121 ? 0.6890 0.3546 0.5664 0.0383  0.1336  0.1199  121 TYR C C   
9458  O O   . TYR C 121 ? 0.6934 0.3613 0.5667 0.0398  0.1331  0.1127  121 TYR C O   
9459  C CB  . TYR C 121 ? 0.6930 0.3802 0.6216 0.0374  0.1601  0.1290  121 TYR C CB  
9460  C CG  . TYR C 121 ? 0.7061 0.3969 0.6543 0.0367  0.1762  0.1398  121 TYR C CG  
9461  C CD1 . TYR C 121 ? 0.7055 0.4039 0.6780 0.0321  0.1720  0.1449  121 TYR C CD1 
9462  C CD2 . TYR C 121 ? 0.7219 0.4072 0.6634 0.0408  0.1960  0.1451  121 TYR C CD2 
9463  C CE1 . TYR C 121 ? 0.7107 0.4114 0.7011 0.0309  0.1865  0.1553  121 TYR C CE1 
9464  C CE2 . TYR C 121 ? 0.7326 0.4210 0.6923 0.0401  0.2114  0.1557  121 TYR C CE2 
9465  C CZ  . TYR C 121 ? 0.7265 0.4227 0.7111 0.0348  0.2065  0.1611  121 TYR C CZ  
9466  O OH  . TYR C 121 ? 0.7242 0.4232 0.7278 0.0335  0.2217  0.1722  121 TYR C OH  
9467  N N   . ASP C 122 ? 0.6752 0.3381 0.5481 0.0362  0.1187  0.1195  122 ASP C N   
9468  C CA  . ASP C 122 ? 0.6736 0.3323 0.5292 0.0362  0.1020  0.1115  122 ASP C CA  
9469  C C   . ASP C 122 ? 0.6420 0.3211 0.5269 0.0328  0.0906  0.1032  122 ASP C C   
9470  O O   . ASP C 122 ? 0.6417 0.3209 0.5188 0.0320  0.0765  0.0965  122 ASP C O   
9471  C CB  . ASP C 122 ? 0.7088 0.3545 0.5448 0.0363  0.0913  0.1151  122 ASP C CB  
9472  C CG  . ASP C 122 ? 0.6910 0.3467 0.5520 0.0330  0.0822  0.1179  122 ASP C CG  
9473  O OD1 . ASP C 122 ? 0.6591 0.3327 0.5544 0.0301  0.0831  0.1164  122 ASP C OD1 
9474  O OD2 . ASP C 122 ? 0.7285 0.3732 0.5739 0.0336  0.0734  0.1212  122 ASP C OD2 
9475  N N   . CYS C 123 ? 0.6279 0.3241 0.5464 0.0306  0.0966  0.1039  123 CYS C N   
9476  C CA  . CYS C 123 ? 0.6017 0.3164 0.5456 0.0279  0.0880  0.0960  123 CYS C CA  
9477  C C   . CYS C 123 ? 0.5934 0.3078 0.5270 0.0297  0.0892  0.0892  123 CYS C C   
9478  O O   . CYS C 123 ? 0.5694 0.2950 0.5149 0.0278  0.0794  0.0820  123 CYS C O   
9479  C CB  . CYS C 123 ? 0.5918 0.3235 0.5723 0.0251  0.0931  0.0984  123 CYS C CB  
9480  S SG  . CYS C 123 ? 0.5993 0.3342 0.5904 0.0271  0.1134  0.1034  123 CYS C SG  
9481  N N   . ILE C 124 ? 0.6258 0.3268 0.5373 0.0335  0.1017  0.0915  124 ILE C N   
9482  C CA  . ILE C 124 ? 0.6203 0.3182 0.5198 0.0357  0.1036  0.0852  124 ILE C CA  
9483  C C   . ILE C 124 ? 0.6265 0.3119 0.4978 0.0358  0.0902  0.0797  124 ILE C C   
9484  O O   . ILE C 124 ? 0.6577 0.3253 0.5002 0.0378  0.0906  0.0830  124 ILE C O   
9485  C CB  . ILE C 124 ? 0.6517 0.3377 0.5355 0.0405  0.1223  0.0895  124 ILE C CB  
9486  C CG1 . ILE C 124 ? 0.6496 0.3482 0.5629 0.0405  0.1366  0.0959  124 ILE C CG1 
9487  C CG2 . ILE C 124 ? 0.6631 0.3429 0.5314 0.0431  0.1233  0.0824  124 ILE C CG2 
9488  C CD1 . ILE C 124 ? 0.6716 0.3577 0.5698 0.0454  0.1566  0.1025  124 ILE C CD1 
9489  N N   . ILE C 125 ? 0.6082 0.3028 0.4878 0.0336  0.0787  0.0718  125 ILE C N   
9490  C CA  . ILE C 125 ? 0.6238 0.3092 0.4820 0.0327  0.0644  0.0665  125 ILE C CA  
9491  C C   . ILE C 125 ? 0.6257 0.3044 0.4690 0.0340  0.0647  0.0599  125 ILE C C   
9492  O O   . ILE C 125 ? 0.6388 0.3081 0.4627 0.0332  0.0533  0.0554  125 ILE C O   
9493  C CB  . ILE C 125 ? 0.6019 0.3027 0.4816 0.0286  0.0488  0.0631  125 ILE C CB  
9494  C CG1 . ILE C 125 ? 0.5802 0.3005 0.4892 0.0264  0.0481  0.0585  125 ILE C CG1 
9495  C CG2 . ILE C 125 ? 0.6091 0.3125 0.4987 0.0278  0.0469  0.0693  125 ILE C CG2 
9496  C CD1 . ILE C 125 ? 0.5665 0.2986 0.4885 0.0229  0.0326  0.0528  125 ILE C CD1 
9497  N N   . THR C 126 ? 0.6257 0.3096 0.4800 0.0358  0.0766  0.0592  126 THR C N   
9498  C CA  . THR C 126 ? 0.6376 0.3115 0.4749 0.0381  0.0799  0.0539  126 THR C CA  
9499  C C   . THR C 126 ? 0.6333 0.3084 0.4784 0.0420  0.0982  0.0569  126 THR C C   
9500  O O   . THR C 126 ? 0.6201 0.3112 0.4942 0.0414  0.1046  0.0608  126 THR C O   
9501  C CB  . THR C 126 ? 0.6268 0.3118 0.4775 0.0346  0.0676  0.0465  126 THR C CB  
9502  O OG1 . THR C 126 ? 0.6407 0.3226 0.4817 0.0315  0.0516  0.0439  126 THR C OG1 
9503  C CG2 . THR C 126 ? 0.6511 0.3260 0.4870 0.0366  0.0707  0.0410  126 THR C CG2 
9504  N N   . TYR C 127 ? 0.6660 0.3234 0.4847 0.0463  0.1066  0.0550  127 TYR C N   
9505  C CA  . TYR C 127 ? 0.6727 0.3312 0.4991 0.0506  0.1230  0.0562  127 TYR C CA  
9506  C C   . TYR C 127 ? 0.6765 0.3352 0.5033 0.0507  0.1185  0.0484  127 TYR C C   
9507  O O   . TYR C 127 ? 0.6765 0.3227 0.4806 0.0495  0.1079  0.0425  127 TYR C O   
9508  C CB  . TYR C 127 ? 0.6985 0.3357 0.4947 0.0565  0.1385  0.0600  127 TYR C CB  
9509  C CG  . TYR C 127 ? 0.7053 0.3426 0.5043 0.0575  0.1485  0.0695  127 TYR C CG  
9510  C CD1 . TYR C 127 ? 0.7241 0.3514 0.5039 0.0559  0.1412  0.0724  127 TYR C CD1 
9511  C CD2 . TYR C 127 ? 0.7026 0.3489 0.5227 0.0602  0.1658  0.0760  127 TYR C CD2 
9512  C CE1 . TYR C 127 ? 0.7297 0.3563 0.5120 0.0565  0.1504  0.0817  127 TYR C CE1 
9513  C CE2 . TYR C 127 ? 0.7212 0.3674 0.5449 0.0606  0.1754  0.0851  127 TYR C CE2 
9514  C CZ  . TYR C 127 ? 0.7134 0.3492 0.5175 0.0587  0.1679  0.0881  127 TYR C CZ  
9515  O OH  . TYR C 127 ? 0.7080 0.3429 0.5157 0.0590  0.1774  0.0975  127 TYR C OH  
9516  N N   . LEU C 128 ? 0.6727 0.3453 0.5259 0.0520  0.1264  0.0490  128 LEU C N   
9517  C CA  . LEU C 128 ? 0.6614 0.3337 0.5170 0.0533  0.1262  0.0432  128 LEU C CA  
9518  C C   . LEU C 128 ? 0.6815 0.3443 0.5305 0.0604  0.1452  0.0452  128 LEU C C   
9519  O O   . LEU C 128 ? 0.6845 0.3601 0.5582 0.0626  0.1568  0.0507  128 LEU C O   
9520  C CB  . LEU C 128 ? 0.6355 0.3323 0.5283 0.0495  0.1195  0.0428  128 LEU C CB  
9521  C CG  . LEU C 128 ? 0.6162 0.3249 0.5199 0.0429  0.1020  0.0405  128 LEU C CG  
9522  C CD1 . LEU C 128 ? 0.5811 0.3118 0.5190 0.0404  0.0986  0.0402  128 LEU C CD1 
9523  C CD2 . LEU C 128 ? 0.6360 0.3332 0.5174 0.0403  0.0886  0.0340  128 LEU C CD2 
9524  N N   . VAL C 129 ? 0.7057 0.3459 0.5217 0.0643  0.1484  0.0406  129 VAL C N   
9525  C CA  . VAL C 129 ? 0.7263 0.3529 0.5286 0.0719  0.1676  0.0426  129 VAL C CA  
9526  C C   . VAL C 129 ? 0.7495 0.3849 0.5738 0.0753  0.1754  0.0413  129 VAL C C   
9527  O O   . VAL C 129 ? 0.7965 0.4270 0.6204 0.0819  0.1932  0.0445  129 VAL C O   
9528  C CB  . VAL C 129 ? 0.7752 0.3718 0.5313 0.0754  0.1688  0.0376  129 VAL C CB  
9529  C CG1 . VAL C 129 ? 0.8073 0.3913 0.5377 0.0751  0.1686  0.0413  129 VAL C CG1 
9530  C CG2 . VAL C 129 ? 0.7919 0.3802 0.5344 0.0718  0.1522  0.0285  129 VAL C CG2 
9531  N N   . ILE C 130 ? 0.7430 0.3894 0.5841 0.0715  0.1630  0.0366  130 ILE C N   
9532  C CA  . ILE C 130 ? 0.7338 0.3888 0.5968 0.0747  0.1696  0.0362  130 ILE C CA  
9533  C C   . ILE C 130 ? 0.6963 0.3713 0.5870 0.0687  0.1548  0.0342  130 ILE C C   
9534  O O   . ILE C 130 ? 0.6837 0.3601 0.5691 0.0626  0.1391  0.0306  130 ILE C O   
9535  C CB  . ILE C 130 ? 0.7657 0.3977 0.6017 0.0807  0.1767  0.0305  130 ILE C CB  
9536  C CG1 . ILE C 130 ? 0.7585 0.3984 0.6175 0.0857  0.1864  0.0314  130 ILE C CG1 
9537  C CG2 . ILE C 130 ? 0.7797 0.3978 0.5920 0.0764  0.1605  0.0222  130 ILE C CG2 
9538  C CD1 . ILE C 130 ? 0.7971 0.4133 0.6305 0.0935  0.1984  0.0272  130 ILE C CD1 
9539  N N   . ASN C 131 ? 0.6888 0.3794 0.6094 0.0707  0.1604  0.0369  131 ASN C N   
9540  C CA  . ASN C 131 ? 0.6585 0.3678 0.6055 0.0660  0.1483  0.0358  131 ASN C CA  
9541  C C   . ASN C 131 ? 0.6427 0.3473 0.5909 0.0688  0.1486  0.0319  131 ASN C C   
9542  O O   . ASN C 131 ? 0.6303 0.3387 0.5935 0.0743  0.1597  0.0347  131 ASN C O   
9543  C CB  . ASN C 131 ? 0.6226 0.3554 0.6055 0.0650  0.1514  0.0425  131 ASN C CB  
9544  C CG  . ASN C 131 ? 0.6058 0.3566 0.6118 0.0595  0.1374  0.0411  131 ASN C CG  
9545  O OD1 . ASN C 131 ? 0.6017 0.3672 0.6345 0.0606  0.1393  0.0438  131 ASN C OD1 
9546  N ND2 . ASN C 131 ? 0.6342 0.3841 0.6300 0.0537  0.1233  0.0370  131 ASN C ND2 
9547  N N   . GLU C 132 ? 0.6520 0.3495 0.5870 0.0648  0.1358  0.0257  132 GLU C N   
9548  C CA  . GLU C 132 ? 0.6731 0.3719 0.6165 0.0648  0.1312  0.0227  132 GLU C CA  
9549  C C   . GLU C 132 ? 0.6837 0.3650 0.6145 0.0724  0.1434  0.0208  132 GLU C C   
9550  O O   . GLU C 132 ? 0.6542 0.3435 0.6056 0.0765  0.1497  0.0233  132 GLU C O   
9551  C CB  . GLU C 132 ? 0.6734 0.3976 0.6534 0.0628  0.1284  0.0273  132 GLU C CB  
9552  C CG  . GLU C 132 ? 0.6895 0.4188 0.6771 0.0589  0.1165  0.0241  132 GLU C CG  
9553  C CD  . GLU C 132 ? 0.7251 0.4558 0.7039 0.0512  0.1015  0.0206  132 GLU C CD  
9554  O OE1 . GLU C 132 ? 0.6517 0.4005 0.6485 0.0469  0.0951  0.0232  132 GLU C OE1 
9555  O OE2 . GLU C 132 ? 0.7643 0.4777 0.7188 0.0497  0.0964  0.0152  132 GLU C OE2 
9556  N N   . PRO C 133 ? 0.6910 0.3474 0.5872 0.0749  0.1465  0.0160  133 PRO C N   
9557  C CA  . PRO C 133 ? 0.7225 0.3593 0.6032 0.0820  0.1567  0.0126  133 PRO C CA  
9558  C C   . PRO C 133 ? 0.7167 0.3508 0.6009 0.0796  0.1469  0.0081  133 PRO C C   
9559  O O   . PRO C 133 ? 0.7066 0.3366 0.5803 0.0728  0.1323  0.0037  133 PRO C O   
9560  C CB  . PRO C 133 ? 0.7465 0.3575 0.5869 0.0835  0.1592  0.0082  133 PRO C CB  
9561  C CG  . PRO C 133 ? 0.7390 0.3543 0.5730 0.0746  0.1419  0.0065  133 PRO C CG  
9562  C CD  . PRO C 133 ? 0.6934 0.3380 0.5628 0.0709  0.1391  0.0131  133 PRO C CD  
9563  N N   . GLN C 134 ? 0.7226 0.3599 0.6237 0.0853  0.1552  0.0100  134 GLN C N   
9564  C CA  . GLN C 134 ? 0.7349 0.3709 0.6428 0.0837  0.1475  0.0072  134 GLN C CA  
9565  C C   . GLN C 134 ? 0.7434 0.3497 0.6180 0.0856  0.1472  -0.0006 134 GLN C C   
9566  O O   . GLN C 134 ? 0.7323 0.3200 0.5848 0.0921  0.1593  -0.0026 134 GLN C O   
9567  C CB  . GLN C 134 ? 0.7494 0.3985 0.6868 0.0897  0.1564  0.0124  134 GLN C CB  
9568  C CG  . GLN C 134 ? 0.7460 0.4247 0.7182 0.0858  0.1511  0.0190  134 GLN C CG  
9569  C CD  . GLN C 134 ? 0.8071 0.4968 0.7896 0.0778  0.1345  0.0180  134 GLN C CD  
9570  O OE1 . GLN C 134 ? 0.9264 0.6375 0.9297 0.0733  0.1280  0.0219  134 GLN C OE1 
9571  N NE2 . GLN C 134 ? 0.8060 0.4816 0.7744 0.0757  0.1274  0.0130  134 GLN C NE2 
9572  N N   . THR C 135 ? 0.7437 0.3462 0.6157 0.0795  0.1334  -0.0047 135 THR C N   
9573  C CA  . THR C 135 ? 0.7906 0.3662 0.6353 0.0796  0.1298  -0.0122 135 THR C CA  
9574  C C   . THR C 135 ? 0.8382 0.3970 0.6765 0.0898  0.1448  -0.0136 135 THR C C   
9575  O O   . THR C 135 ? 0.9110 0.4436 0.7182 0.0940  0.1505  -0.0193 135 THR C O   
9576  C CB  . THR C 135 ? 0.7651 0.3449 0.6191 0.0720  0.1146  -0.0140 135 THR C CB  
9577  O OG1 . THR C 135 ? 0.7181 0.3184 0.5862 0.0632  0.1019  -0.0115 135 THR C OG1 
9578  C CG2 . THR C 135 ? 0.7934 0.3448 0.6174 0.0701  0.1085  -0.0223 135 THR C CG2 
9579  N N   . ASP C 136 ? 0.8135 0.3863 0.6803 0.0942  0.1509  -0.0086 136 ASP C N   
9580  C CA  . ASP C 136 ? 0.8350 0.3920 0.6980 0.1041  0.1644  -0.0098 136 ASP C CA  
9581  C C   . ASP C 136 ? 0.8509 0.4004 0.7024 0.1129  0.1824  -0.0087 136 ASP C C   
9582  O O   . ASP C 136 ? 0.8887 0.4144 0.7189 0.1208  0.1937  -0.0131 136 ASP C O   
9583  C CB  . ASP C 136 ? 0.7798 0.3525 0.6758 0.1066  0.1651  -0.0046 136 ASP C CB  
9584  C CG  . ASP C 136 ? 0.8091 0.3648 0.7020 0.1175  0.1789  -0.0060 136 ASP C CG  
9585  O OD1 . ASP C 136 ? 0.8201 0.3521 0.6927 0.1180  0.1759  -0.0125 136 ASP C OD1 
9586  O OD2 . ASP C 136 ? 0.8023 0.3677 0.7125 0.1255  0.1931  -0.0007 136 ASP C OD2 
9587  N N   . HIS C 137 ? 0.8080 0.3771 0.6732 0.1115  0.1854  -0.0029 137 HIS C N   
9588  C CA  . HIS C 137 ? 0.8145 0.3798 0.6727 0.1191  0.2030  -0.0001 137 HIS C CA  
9589  C C   . HIS C 137 ? 0.8193 0.3580 0.6342 0.1193  0.2046  -0.0065 137 HIS C C   
9590  O O   . HIS C 137 ? 0.8523 0.3747 0.6497 0.1279  0.2207  -0.0075 137 HIS C O   
9591  C CB  . HIS C 137 ? 0.7860 0.3800 0.6735 0.1170  0.2054  0.0085  137 HIS C CB  
9592  C CG  . HIS C 137 ? 0.8312 0.4216 0.7140 0.1249  0.2246  0.0122  137 HIS C CG  
9593  N ND1 . HIS C 137 ? 0.8496 0.4337 0.7110 0.1231  0.2272  0.0123  137 HIS C ND1 
9594  C CD2 . HIS C 137 ? 0.8500 0.4412 0.7462 0.1349  0.2428  0.0160  137 HIS C CD2 
9595  C CE1 . HIS C 137 ? 0.8901 0.4718 0.7521 0.1315  0.2468  0.0165  137 HIS C CE1 
9596  N NE2 . HIS C 137 ? 0.8642 0.4502 0.7475 0.1389  0.2569  0.0186  137 HIS C NE2 
9597  N N   . ILE C 138 ? 0.8230 0.3570 0.6205 0.1102  0.1881  -0.0107 138 ILE C N   
9598  C CA  . ILE C 138 ? 0.8369 0.3443 0.5919 0.1098  0.1867  -0.0172 138 ILE C CA  
9599  C C   . ILE C 138 ? 0.8630 0.3401 0.5912 0.1146  0.1893  -0.0255 138 ILE C C   
9600  O O   . ILE C 138 ? 0.8971 0.3489 0.5909 0.1199  0.1978  -0.0301 138 ILE C O   
9601  C CB  . ILE C 138 ? 0.8272 0.3385 0.5737 0.0987  0.1669  -0.0194 138 ILE C CB  
9602  C CG1 . ILE C 138 ? 0.8116 0.3505 0.5816 0.0941  0.1641  -0.0117 138 ILE C CG1 
9603  C CG2 . ILE C 138 ? 0.8574 0.3388 0.5585 0.0983  0.1636  -0.0266 138 ILE C CG2 
9604  C CD1 . ILE C 138 ? 0.7837 0.3309 0.5532 0.0833  0.1442  -0.0132 138 ILE C CD1 
9605  N N   . HIS C 139 ? 0.8663 0.3439 0.6079 0.1125  0.1813  -0.0278 139 HIS C N   
9606  C CA  . HIS C 139 ? 0.8967 0.3445 0.6142 0.1168  0.1831  -0.0359 139 HIS C CA  
9607  C C   . HIS C 139 ? 0.9235 0.3590 0.6347 0.1300  0.2059  -0.0353 139 HIS C C   
9608  O O   . HIS C 139 ? 0.9625 0.3677 0.6374 0.1354  0.2126  -0.0424 139 HIS C O   
9609  C CB  . HIS C 139 ? 0.8736 0.3262 0.6105 0.1123  0.1716  -0.0369 139 HIS C CB  
9610  C CG  . HIS C 139 ? 0.8857 0.3090 0.6032 0.1176  0.1749  -0.0442 139 HIS C CG  
9611  N ND1 . HIS C 139 ? 0.8904 0.3104 0.6203 0.1279  0.1899  -0.0425 139 HIS C ND1 
9612  C CD2 . HIS C 139 ? 0.9052 0.3009 0.5925 0.1140  0.1652  -0.0533 139 HIS C CD2 
9613  C CE1 . HIS C 139 ? 0.9287 0.3190 0.6351 0.1308  0.1896  -0.0506 139 HIS C CE1 
9614  N NE2 . HIS C 139 ? 0.9356 0.3103 0.6155 0.1222  0.1745  -0.0574 139 HIS C NE2 
9615  N N   . SER C 140 ? 0.9135 0.3730 0.6601 0.1351  0.2173  -0.0268 140 SER C N   
9616  C CA  . SER C 140 ? 0.9413 0.3959 0.6933 0.1478  0.2393  -0.0244 140 SER C CA  
9617  C C   . SER C 140 ? 0.9614 0.4046 0.6888 0.1540  0.2553  -0.0240 140 SER C C   
9618  O O   . SER C 140 ? 0.9883 0.4141 0.7024 0.1649  0.2731  -0.0258 140 SER C O   
9619  C CB  . SER C 140 ? 0.9304 0.4174 0.7309 0.1497  0.2437  -0.0146 140 SER C CB  
9620  O OG  . SER C 140 ? 0.9552 0.4393 0.7653 0.1622  0.2648  -0.0117 140 SER C OG  
9621  N N   . VAL C 141 ? 0.9509 0.4050 0.6745 0.1481  0.2509  -0.0206 141 VAL C N   
9622  C CA  . VAL C 141 ? 0.9713 0.4135 0.6702 0.1540  0.2665  -0.0195 141 VAL C CA  
9623  C C   . VAL C 141 ? 1.0236 0.4365 0.6734 0.1502  0.2571  -0.0281 141 VAL C C   
9624  O O   . VAL C 141 ? 1.0455 0.4390 0.6637 0.1562  0.2698  -0.0296 141 VAL C O   
9625  C CB  . VAL C 141 ? 0.9385 0.4087 0.6630 0.1516  0.2711  -0.0093 141 VAL C CB  
9626  C CG1 . VAL C 141 ? 0.9070 0.4059 0.6807 0.1551  0.2792  -0.0008 141 VAL C CG1 
9627  C CG2 . VAL C 141 ? 0.9101 0.3928 0.6355 0.1393  0.2506  -0.0087 141 VAL C CG2 
9628  N N   . THR C 142 ? 1.0408 0.4519 0.6859 0.1401  0.2348  -0.0332 142 THR C N   
9629  C CA  . THR C 142 ? 1.1117 0.4942 0.7140 0.1356  0.2218  -0.0428 142 THR C CA  
9630  C C   . THR C 142 ? 1.1004 0.4941 0.6992 0.1250  0.2052  -0.0409 142 THR C C   
9631  O O   . THR C 142 ? 1.0964 0.5080 0.7073 0.1245  0.2103  -0.0334 142 THR C O   
9632  C CB  . THR C 142 ? 1.2135 0.5602 0.7701 0.1449  0.2360  -0.0493 142 THR C CB  
9633  O OG1 . THR C 142 ? 1.2551 0.5764 0.7764 0.1387  0.2185  -0.0590 142 THR C OG1 
9634  C CG2 . THR C 142 ? 1.2100 0.5536 0.7474 0.1491  0.2492  -0.0449 142 THR C CG2 
9635  N N   . GLY C 143 ? 1.1088 0.4926 0.6936 0.1164  0.1848  -0.0474 143 GLY C N   
9636  C CA  . GLY C 143 ? 1.1249 0.5118 0.6979 0.1071  0.1681  -0.0477 143 GLY C CA  
9637  C C   . GLY C 143 ? 1.1725 0.5463 0.7142 0.1111  0.1769  -0.0464 143 GLY C C   
9638  O O   . GLY C 143 ? 1.1476 0.5381 0.6979 0.1068  0.1729  -0.0404 143 GLY C O   
9639  N N   . LYS C 144 ? 1.2197 0.5624 0.7240 0.1196  0.1893  -0.0519 144 LYS C N   
9640  C CA  . LYS C 144 ? 1.2250 0.5489 0.6912 0.1235  0.1969  -0.0520 144 LYS C CA  
9641  C C   . LYS C 144 ? 1.1785 0.5250 0.6666 0.1274  0.2131  -0.0408 144 LYS C C   
9642  O O   . LYS C 144 ? 1.1564 0.5074 0.6358 0.1238  0.2086  -0.0367 144 LYS C O   
9643  C CB  . LYS C 144 ? 1.3137 0.6000 0.7382 0.1327  0.2085  -0.0605 144 LYS C CB  
9644  C CG  . LYS C 144 ? 1.3812 0.6453 0.7650 0.1403  0.2235  -0.0602 144 LYS C CG  
9645  C CD  . LYS C 144 ? 1.4656 0.6956 0.8147 0.1512  0.2393  -0.0681 144 LYS C CD  
9646  C CE  . LYS C 144 ? 1.5031 0.7178 0.8231 0.1615  0.2621  -0.0649 144 LYS C CE  
9647  N NZ  . LYS C 144 ? 1.4994 0.7136 0.7983 0.1565  0.2545  -0.0611 144 LYS C NZ  
9648  N N   . ALA C 145 ? 1.1405 0.5023 0.6597 0.1343  0.2304  -0.0357 145 ALA C N   
9649  C CA  . ALA C 145 ? 1.1226 0.5036 0.6632 0.1392  0.2485  -0.0253 145 ALA C CA  
9650  C C   . ALA C 145 ? 1.1093 0.5234 0.6852 0.1301  0.2369  -0.0174 145 ALA C C   
9651  O O   . ALA C 145 ? 1.0593 0.4862 0.6449 0.1315  0.2470  -0.0092 145 ALA C O   
9652  C CB  . ALA C 145 ? 1.1067 0.4964 0.6746 0.1481  0.2674  -0.0223 145 ALA C CB  
9653  N N   . PHE C 146 ? 1.0805 0.5082 0.6769 0.1214  0.2171  -0.0199 146 PHE C N   
9654  C CA  . PHE C 146 ? 1.0145 0.4692 0.6382 0.1120  0.2024  -0.0148 146 PHE C CA  
9655  C C   . PHE C 146 ? 1.0226 0.4662 0.6161 0.1068  0.1910  -0.0159 146 PHE C C   
9656  O O   . PHE C 146 ? 1.0050 0.4613 0.6061 0.1055  0.1939  -0.0088 146 PHE C O   
9657  C CB  . PHE C 146 ? 0.9773 0.4463 0.6269 0.1049  0.1856  -0.0176 146 PHE C CB  
9658  C CG  . PHE C 146 ? 0.9260 0.4205 0.5998 0.0950  0.1694  -0.0135 146 PHE C CG  
9659  C CD1 . PHE C 146 ? 0.8715 0.3945 0.5815 0.0944  0.1746  -0.0048 146 PHE C CD1 
9660  C CD2 . PHE C 146 ? 0.9167 0.4059 0.5767 0.0866  0.1492  -0.0183 146 PHE C CD2 
9661  C CE1 . PHE C 146 ? 0.8506 0.3945 0.5798 0.0861  0.1607  -0.0016 146 PHE C CE1 
9662  C CE2 . PHE C 146 ? 0.8906 0.4025 0.5723 0.0786  0.1358  -0.0145 146 PHE C CE2 
9663  C CZ  . PHE C 146 ? 0.8559 0.3944 0.5711 0.0785  0.1418  -0.0064 146 PHE C CZ  
9664  N N   . VAL C 147 ? 1.0338 0.4540 0.5943 0.1035  0.1773  -0.0246 147 VAL C N   
9665  C CA  . VAL C 147 ? 1.0430 0.4531 0.5766 0.0979  0.1632  -0.0260 147 VAL C CA  
9666  C C   . VAL C 147 ? 1.0907 0.4870 0.5959 0.1041  0.1777  -0.0219 147 VAL C C   
9667  O O   . VAL C 147 ? 1.1072 0.5090 0.6080 0.1001  0.1708  -0.0175 147 VAL C O   
9668  C CB  . VAL C 147 ? 1.0844 0.4695 0.5865 0.0939  0.1463  -0.0364 147 VAL C CB  
9669  C CG1 . VAL C 147 ? 1.1224 0.4969 0.5963 0.0886  0.1316  -0.0373 147 VAL C CG1 
9670  C CG2 . VAL C 147 ? 1.0524 0.4520 0.5832 0.0867  0.1313  -0.0395 147 VAL C CG2 
9671  N N   . ASP C 148 ? 1.1242 0.5015 0.6093 0.1141  0.1978  -0.0232 148 ASP C N   
9672  C CA  . ASP C 148 ? 1.1413 0.5041 0.5988 0.1211  0.2149  -0.0189 148 ASP C CA  
9673  C C   . ASP C 148 ? 1.1326 0.5237 0.6246 0.1215  0.2264  -0.0069 148 ASP C C   
9674  O O   . ASP C 148 ? 1.1460 0.5324 0.6213 0.1228  0.2327  -0.0012 148 ASP C O   
9675  C CB  . ASP C 148 ? 1.1619 0.4998 0.5943 0.1322  0.2352  -0.0233 148 ASP C CB  
9676  C CG  . ASP C 148 ? 1.2102 0.5108 0.5936 0.1337  0.2275  -0.0351 148 ASP C CG  
9677  O OD1 . ASP C 148 ? 1.2074 0.4995 0.5726 0.1257  0.2055  -0.0399 148 ASP C OD1 
9678  O OD2 . ASP C 148 ? 1.2420 0.5213 0.6053 0.1429  0.2434  -0.0397 148 ASP C OD2 
9679  N N   . LEU C 149 ? 1.0762 0.4955 0.6159 0.1207  0.2299  -0.0027 149 LEU C N   
9680  C CA  . LEU C 149 ? 1.0478 0.4950 0.6238 0.1201  0.2385  0.0081  149 LEU C CA  
9681  C C   . LEU C 149 ? 1.0694 0.5307 0.6537 0.1103  0.2194  0.0109  149 LEU C C   
9682  O O   . LEU C 149 ? 1.0959 0.5616 0.6787 0.1100  0.2243  0.0181  149 LEU C O   
9683  C CB  . LEU C 149 ? 1.0031 0.4751 0.6259 0.1214  0.2445  0.0109  149 LEU C CB  
9684  C CG  . LEU C 149 ? 0.9941 0.4977 0.6599 0.1191  0.2495  0.0215  149 LEU C CG  
9685  C CD1 . LEU C 149 ? 1.0286 0.5278 0.6880 0.1266  0.2729  0.0291  149 LEU C CD1 
9686  C CD2 . LEU C 149 ? 0.9410 0.4708 0.6537 0.1181  0.2486  0.0235  149 LEU C CD2 
9687  N N   . MET C 150 ? 1.0434 0.5109 0.6359 0.1026  0.1979  0.0054  150 MET C N   
9688  C CA  . MET C 150 ? 1.0247 0.5069 0.6282 0.0938  0.1800  0.0078  150 MET C CA  
9689  C C   . MET C 150 ? 1.0670 0.5300 0.6324 0.0939  0.1780  0.0091  150 MET C C   
9690  O O   . MET C 150 ? 1.0709 0.5460 0.6469 0.0920  0.1792  0.0167  150 MET C O   
9691  C CB  . MET C 150 ? 1.0223 0.5087 0.6327 0.0860  0.1578  0.0008  150 MET C CB  
9692  C CG  . MET C 150 ? 0.9724 0.4800 0.6218 0.0844  0.1565  0.0004  150 MET C CG  
9693  S SD  . MET C 150 ? 0.9137 0.4582 0.6141 0.0824  0.1615  0.0104  150 MET C SD  
9694  C CE  . MET C 150 ? 0.9118 0.4550 0.6191 0.0929  0.1890  0.0159  150 MET C CE  
9695  N N   . ASN C 151 ? 1.1073 0.5396 0.6283 0.0963  0.1750  0.0018  151 ASN C N   
9696  C CA  . ASN C 151 ? 1.1355 0.5463 0.6155 0.0966  0.1712  0.0022  151 ASN C CA  
9697  C C   . ASN C 151 ? 1.1691 0.5786 0.6431 0.1027  0.1919  0.0115  151 ASN C C   
9698  O O   . ASN C 151 ? 1.1650 0.5700 0.6230 0.1010  0.1881  0.0164  151 ASN C O   
9699  C CB  . ASN C 151 ? 1.1683 0.5440 0.6001 0.0997  0.1682  -0.0074 151 ASN C CB  
9700  C CG  . ASN C 151 ? 1.1639 0.5368 0.5939 0.0920  0.1439  -0.0158 151 ASN C CG  
9701  O OD1 . ASN C 151 ? 1.2543 0.6085 0.6662 0.0935  0.1417  -0.0246 151 ASN C OD1 
9702  N ND2 . ASN C 151 ? 1.1171 0.5081 0.5663 0.0838  0.1260  -0.0133 151 ASN C ND2 
9703  N N   . THR C 152 ? 1.1948 0.6074 0.6814 0.1100  0.2139  0.0142  152 THR C N   
9704  C CA  . THR C 152 ? 1.2289 0.6416 0.7137 0.1161  0.2358  0.0235  152 THR C CA  
9705  C C   . THR C 152 ? 1.1810 0.6238 0.7056 0.1107  0.2334  0.0334  152 THR C C   
9706  O O   . THR C 152 ? 1.2664 0.7064 0.7807 0.1112  0.2395  0.0410  152 THR C O   
9707  C CB  . THR C 152 ? 1.2608 0.6714 0.7537 0.1252  0.2589  0.0235  152 THR C CB  
9708  O OG1 . THR C 152 ? 1.3248 0.7029 0.7733 0.1301  0.2600  0.0139  152 THR C OG1 
9709  C CG2 . THR C 152 ? 1.2940 0.7075 0.7910 0.1317  0.2838  0.0338  152 THR C CG2 
9710  N N   . LEU C 153 ? 1.0964 0.5667 0.6655 0.1055  0.2244  0.0334  153 LEU C N   
9711  C CA  . LEU C 153 ? 1.0728 0.5712 0.6811 0.1005  0.2222  0.0419  153 LEU C CA  
9712  C C   . LEU C 153 ? 1.0580 0.5571 0.6573 0.0930  0.2017  0.0420  153 LEU C C   
9713  O O   . LEU C 153 ? 1.0587 0.5672 0.6682 0.0908  0.2029  0.0500  153 LEU C O   
9714  C CB  . LEU C 153 ? 1.0208 0.5465 0.6767 0.0980  0.2197  0.0415  153 LEU C CB  
9715  C CG  . LEU C 153 ? 1.0049 0.5320 0.6740 0.1054  0.2382  0.0414  153 LEU C CG  
9716  C CD1 . LEU C 153 ? 0.9458 0.5018 0.6638 0.1024  0.2344  0.0427  153 LEU C CD1 
9717  C CD2 . LEU C 153 ? 1.0419 0.5646 0.7070 0.1125  0.2623  0.0496  153 LEU C CD2 
9718  N N   . ILE C 154 ? 1.0293 0.5183 0.6109 0.0890  0.1827  0.0334  154 ILE C N   
9719  C CA  . ILE C 154 ? 1.0175 0.5069 0.5912 0.0823  0.1622  0.0329  154 ILE C CA  
9720  C C   . ILE C 154 ? 1.0740 0.5439 0.6121 0.0849  0.1668  0.0380  154 ILE C C   
9721  O O   . ILE C 154 ? 1.0461 0.5239 0.5905 0.0808  0.1582  0.0433  154 ILE C O   
9722  C CB  . ILE C 154 ? 0.9860 0.4654 0.5447 0.0781  0.1425  0.0227  154 ILE C CB  
9723  C CG1 . ILE C 154 ? 0.9539 0.4537 0.5490 0.0749  0.1371  0.0188  154 ILE C CG1 
9724  C CG2 . ILE C 154 ? 0.9710 0.4482 0.5180 0.0719  0.1218  0.0224  154 ILE C CG2 
9725  C CD1 . ILE C 154 ? 0.9701 0.4584 0.5507 0.0714  0.1211  0.0089  154 ILE C CD1 
9726  N N   . ASN C 155 ? 1.1471 0.5902 0.6462 0.0919  0.1800  0.0362  155 ASN C N   
9727  C CA  . ASN C 155 ? 1.1936 0.6134 0.6511 0.0949  0.1840  0.0401  155 ASN C CA  
9728  C C   . ASN C 155 ? 1.1612 0.5904 0.6328 0.0980  0.2031  0.0520  155 ASN C C   
9729  O O   . ASN C 155 ? 1.1717 0.5947 0.6279 0.0968  0.2004  0.0582  155 ASN C O   
9730  C CB  . ASN C 155 ? 1.2449 0.6309 0.6529 0.1012  0.1905  0.0331  155 ASN C CB  
9731  C CG  . ASN C 155 ? 1.2708 0.6443 0.6594 0.0966  0.1674  0.0224  155 ASN C CG  
9732  O OD1 . ASN C 155 ? 1.2439 0.6303 0.6479 0.0890  0.1465  0.0217  155 ASN C OD1 
9733  N ND2 . ASN C 155 ? 1.3153 0.6635 0.6706 0.1011  0.1709  0.0140  155 ASN C ND2 
9734  N N   . ILE C 156 ? 1.1074 0.5516 0.6091 0.1016  0.2216  0.0554  156 ILE C N   
9735  C CA  . ILE C 156 ? 1.1018 0.5603 0.6269 0.1029  0.2379  0.0670  156 ILE C CA  
9736  C C   . ILE C 156 ? 1.0913 0.5714 0.6460 0.0949  0.2227  0.0721  156 ILE C C   
9737  O O   . ILE C 156 ? 1.1262 0.6076 0.6815 0.0946  0.2291  0.0815  156 ILE C O   
9738  C CB  . ILE C 156 ? 1.0979 0.5724 0.6570 0.1072  0.2572  0.0693  156 ILE C CB  
9739  C CG1 . ILE C 156 ? 1.1612 0.6117 0.6875 0.1169  0.2780  0.0675  156 ILE C CG1 
9740  C CG2 . ILE C 156 ? 1.0750 0.5732 0.6734 0.1055  0.2677  0.0808  156 ILE C CG2 
9741  C CD1 . ILE C 156 ? 1.1531 0.6176 0.7114 0.1221  0.2966  0.0688  156 ILE C CD1 
9742  N N   . ILE C 157 ? 1.0554 0.5516 0.6339 0.0886  0.2031  0.0661  157 ILE C N   
9743  C CA  . ILE C 157 ? 1.0179 0.5353 0.6263 0.0815  0.1893  0.0701  157 ILE C CA  
9744  C C   . ILE C 157 ? 1.0516 0.5539 0.6294 0.0787  0.1733  0.0702  157 ILE C C   
9745  O O   . ILE C 157 ? 1.0431 0.5507 0.6279 0.0766  0.1723  0.0781  157 ILE C O   
9746  C CB  . ILE C 157 ? 0.9590 0.5005 0.6062 0.0763  0.1764  0.0646  157 ILE C CB  
9747  C CG1 . ILE C 157 ? 0.9217 0.4809 0.6038 0.0788  0.1916  0.0667  157 ILE C CG1 
9748  C CG2 . ILE C 157 ? 0.9283 0.4876 0.5993 0.0693  0.1598  0.0671  157 ILE C CG2 
9749  C CD1 . ILE C 157 ? 0.8844 0.4607 0.5945 0.0754  0.1807  0.0598  157 ILE C CD1 
9750  N N   . HIS C 158 ? 1.0531 0.5357 0.5967 0.0788  0.1610  0.0619  158 HIS C N   
9751  C CA  . HIS C 158 ? 1.0787 0.5468 0.5934 0.0763  0.1448  0.0621  158 HIS C CA  
9752  C C   . HIS C 158 ? 1.1000 0.5530 0.5894 0.0802  0.1572  0.0718  158 HIS C C   
9753  O O   . HIS C 158 ? 1.1005 0.5541 0.5875 0.0771  0.1469  0.0769  158 HIS C O   
9754  C CB  . HIS C 158 ? 1.0814 0.5290 0.5619 0.0757  0.1298  0.0518  158 HIS C CB  
9755  C CG  . HIS C 158 ? 1.0365 0.5004 0.5431 0.0699  0.1125  0.0439  158 HIS C CG  
9756  N ND1 . HIS C 158 ? 1.0441 0.4933 0.5290 0.0688  0.1005  0.0340  158 HIS C ND1 
9757  C CD2 . HIS C 158 ? 0.9861 0.4784 0.5375 0.0649  0.1055  0.0443  158 HIS C CD2 
9758  C CE1 . HIS C 158 ? 1.0072 0.4762 0.5238 0.0632  0.0874  0.0294  158 HIS C CE1 
9759  N NE2 . HIS C 158 ? 0.9731 0.4683 0.5295 0.0610  0.0903  0.0355  158 HIS C NE2 
9760  N N   . LYS C 159 ? 1.1324 0.5724 0.6045 0.0870  0.1799  0.0749  159 LYS C N   
9761  C CA  . LYS C 159 ? 1.2100 0.6327 0.6532 0.0909  0.1925  0.0841  159 LYS C CA  
9762  C C   . LYS C 159 ? 1.1513 0.5949 0.6317 0.0899  0.2056  0.0957  159 LYS C C   
9763  O O   . LYS C 159 ? 1.1367 0.5738 0.6055 0.0895  0.2068  0.1045  159 LYS C O   
9764  C CB  . LYS C 159 ? 1.3396 0.7335 0.7379 0.0990  0.2095  0.0819  159 LYS C CB  
9765  C CG  . LYS C 159 ? 1.4818 0.8820 0.8971 0.1047  0.2331  0.0817  159 LYS C CG  
9766  C CD  . LYS C 159 ? 1.6075 1.0179 1.0433 0.1080  0.2576  0.0938  159 LYS C CD  
9767  C CE  . LYS C 159 ? 1.6413 1.0663 1.1082 0.1119  0.2759  0.0930  159 LYS C CE  
9768  N NZ  . LYS C 159 ? 1.6517 1.0999 1.1605 0.1109  0.2903  0.1042  159 LYS C NZ  
9769  N N   . GLY C 160 ? 1.0872 0.5555 0.6124 0.0890  0.2140  0.0958  160 GLY C N   
9770  C CA  . GLY C 160 ? 1.0390 0.5262 0.6003 0.0885  0.2291  0.1063  160 GLY C CA  
9771  C C   . GLY C 160 ? 0.9754 0.4854 0.5737 0.0810  0.2141  0.1097  160 GLY C C   
9772  O O   . GLY C 160 ? 0.9459 0.4637 0.5615 0.0798  0.2223  0.1198  160 GLY C O   
9773  N N   . HIS C 161 ? 0.9292 0.4500 0.5411 0.0762  0.1932  0.1013  161 HIS C N   
9774  C CA  . HIS C 161 ? 0.8888 0.4267 0.5273 0.0696  0.1758  0.1024  161 HIS C CA  
9775  C C   . HIS C 161 ? 0.8996 0.4271 0.5143 0.0671  0.1530  0.0950  161 HIS C C   
9776  O O   . HIS C 161 ? 0.8808 0.4193 0.5106 0.0639  0.1398  0.0867  161 HIS C O   
9777  C CB  . HIS C 161 ? 0.8389 0.4057 0.5269 0.0660  0.1739  0.0998  161 HIS C CB  
9778  C CG  . HIS C 161 ? 0.8021 0.3877 0.5219 0.0600  0.1615  0.1028  161 HIS C CG  
9779  N ND1 . HIS C 161 ? 0.7449 0.3558 0.5093 0.0567  0.1616  0.1026  161 HIS C ND1 
9780  C CD2 . HIS C 161 ? 0.8168 0.3990 0.5300 0.0571  0.1486  0.1058  161 HIS C CD2 
9781  C CE1 . HIS C 161 ? 0.7528 0.3742 0.5354 0.0520  0.1497  0.1050  161 HIS C CE1 
9782  N NE2 . HIS C 161 ? 0.7717 0.3763 0.5249 0.0523  0.1421  0.1073  161 HIS C NE2 
9783  N N   . PRO C 162 ? 0.9459 0.4520 0.5233 0.0683  0.1476  0.0982  162 PRO C N   
9784  C CA  . PRO C 162 ? 0.9590 0.4549 0.5139 0.0658  0.1251  0.0917  162 PRO C CA  
9785  C C   . PRO C 162 ? 0.9339 0.4522 0.5234 0.0596  0.1055  0.0881  162 PRO C C   
9786  O O   . PRO C 162 ? 0.9576 0.4948 0.5810 0.0568  0.1063  0.0933  162 PRO C O   
9787  C CB  . PRO C 162 ? 0.9794 0.4536 0.4982 0.0679  0.1242  0.0994  162 PRO C CB  
9788  C CG  . PRO C 162 ? 0.9913 0.4559 0.4986 0.0732  0.1498  0.1074  162 PRO C CG  
9789  C CD  . PRO C 162 ? 0.9561 0.4463 0.5104 0.0722  0.1629  0.1086  162 PRO C CD  
9790  N N   . GLY C 163 ? 0.9225 0.4380 0.5030 0.0573  0.0883  0.0791  163 GLY C N   
9791  C CA  . GLY C 163 ? 0.8785 0.4092 0.4811 0.0519  0.0677  0.0763  163 GLY C CA  
9792  C C   . GLY C 163 ? 0.8452 0.4019 0.4902 0.0485  0.0662  0.0714  163 GLY C C   
9793  O O   . GLY C 163 ? 0.8527 0.4235 0.5179 0.0442  0.0503  0.0681  163 GLY C O   
9794  N N   . ILE C 164 ? 0.8348 0.3979 0.4929 0.0506  0.0825  0.0709  164 ILE C N   
9795  C CA  . ILE C 164 ? 0.7858 0.3732 0.4837 0.0477  0.0818  0.0670  164 ILE C CA  
9796  C C   . ILE C 164 ? 0.7805 0.3642 0.4707 0.0476  0.0777  0.0577  164 ILE C C   
9797  O O   . ILE C 164 ? 0.8184 0.3866 0.4860 0.0517  0.0884  0.0557  164 ILE C O   
9798  C CB  . ILE C 164 ? 0.7668 0.3661 0.4895 0.0496  0.1008  0.0731  164 ILE C CB  
9799  C CG1 . ILE C 164 ? 0.7732 0.3720 0.4992 0.0499  0.1071  0.0831  164 ILE C CG1 
9800  C CG2 . ILE C 164 ? 0.7235 0.3481 0.4874 0.0463  0.0984  0.0696  164 ILE C CG2 
9801  C CD1 . ILE C 164 ? 0.7417 0.3521 0.4859 0.0454  0.0916  0.0846  164 ILE C CD1 
9802  N N   . PRO C 165 ? 0.7483 0.3459 0.4578 0.0431  0.0628  0.0516  165 PRO C N   
9803  C CA  . PRO C 165 ? 0.7448 0.3415 0.4531 0.0424  0.0598  0.0434  165 PRO C CA  
9804  C C   . PRO C 165 ? 0.7536 0.3549 0.4738 0.0456  0.0760  0.0426  165 PRO C C   
9805  O O   . PRO C 165 ? 0.7461 0.3646 0.4957 0.0457  0.0850  0.0470  165 PRO C O   
9806  C CB  . PRO C 165 ? 0.7040 0.3216 0.4420 0.0368  0.0442  0.0401  165 PRO C CB  
9807  C CG  . PRO C 165 ? 0.7123 0.3308 0.4490 0.0349  0.0336  0.0441  165 PRO C CG  
9808  C CD  . PRO C 165 ? 0.7255 0.3385 0.4568 0.0385  0.0481  0.0526  165 PRO C CD  
9809  N N   . VAL C 166 ? 0.7716 0.3584 0.4715 0.0477  0.0778  0.0364  166 VAL C N   
9810  C CA  . VAL C 166 ? 0.7643 0.3548 0.4756 0.0511  0.0922  0.0352  166 VAL C CA  
9811  C C   . VAL C 166 ? 0.7522 0.3470 0.4720 0.0483  0.0829  0.0272  166 VAL C C   
9812  O O   . VAL C 166 ? 0.7848 0.3643 0.4809 0.0469  0.0721  0.0211  166 VAL C O   
9813  C CB  . VAL C 166 ? 0.7901 0.3577 0.4699 0.0580  0.1089  0.0364  166 VAL C CB  
9814  C CG1 . VAL C 166 ? 0.7812 0.3532 0.4750 0.0620  0.1234  0.0349  166 VAL C CG1 
9815  C CG2 . VAL C 166 ? 0.8069 0.3710 0.4802 0.0608  0.1202  0.0455  166 VAL C CG2 
9816  N N   . THR C 167 ? 0.6966 0.3120 0.4508 0.0473  0.0865  0.0275  167 THR C N   
9817  C CA  . THR C 167 ? 0.6881 0.3062 0.4497 0.0458  0.0816  0.0211  167 THR C CA  
9818  C C   . THR C 167 ? 0.6768 0.3065 0.4624 0.0493  0.0959  0.0232  167 THR C C   
9819  O O   . THR C 167 ? 0.6767 0.3054 0.4636 0.0540  0.1112  0.0286  167 THR C O   
9820  C CB  . THR C 167 ? 0.6637 0.2958 0.4418 0.0389  0.0631  0.0180  167 THR C CB  
9821  O OG1 . THR C 167 ? 0.6517 0.2807 0.4295 0.0375  0.0583  0.0117  167 THR C OG1 
9822  C CG2 . THR C 167 ? 0.6187 0.2768 0.4333 0.0361  0.0619  0.0223  167 THR C CG2 
9823  N N   . LEU C 168 ? 0.6583 0.2970 0.4605 0.0473  0.0910  0.0191  168 LEU C N   
9824  C CA  . LEU C 168 ? 0.6480 0.2963 0.4716 0.0507  0.1027  0.0206  168 LEU C CA  
9825  C C   . LEU C 168 ? 0.6161 0.2874 0.4726 0.0459  0.0935  0.0201  168 LEU C C   
9826  O O   . LEU C 168 ? 0.6172 0.2946 0.4770 0.0403  0.0790  0.0175  168 LEU C O   
9827  C CB  . LEU C 168 ? 0.6729 0.3013 0.4751 0.0554  0.1093  0.0157  168 LEU C CB  
9828  C CG  . LEU C 168 ? 0.6581 0.2853 0.4618 0.0519  0.0978  0.0091  168 LEU C CG  
9829  C CD1 . LEU C 168 ? 0.6861 0.2933 0.4710 0.0573  0.1065  0.0048  168 LEU C CD1 
9830  C CD2 . LEU C 168 ? 0.6589 0.2804 0.4479 0.0457  0.0804  0.0051  168 LEU C CD2 
9831  N N   . SER C 169 ? 0.6108 0.2943 0.4910 0.0486  0.1025  0.0226  169 SER C N   
9832  C CA  . SER C 169 ? 0.5709 0.2742 0.4803 0.0451  0.0956  0.0222  169 SER C CA  
9833  C C   . SER C 169 ? 0.5896 0.2857 0.4959 0.0469  0.0965  0.0180  169 SER C C   
9834  O O   . SER C 169 ? 0.5776 0.2695 0.4861 0.0526  0.1087  0.0193  169 SER C O   
9835  C CB  . SER C 169 ? 0.5522 0.2739 0.4904 0.0464  0.1035  0.0284  169 SER C CB  
9836  O OG  . SER C 169 ? 0.5408 0.2788 0.5051 0.0451  0.1003  0.0284  169 SER C OG  
9837  N N   . ALA C 170 ? 0.6082 0.3024 0.5097 0.0422  0.0835  0.0131  170 ALA C N   
9838  C CA  . ALA C 170 ? 0.6038 0.2903 0.5022 0.0429  0.0826  0.0091  170 ALA C CA  
9839  C C   . ALA C 170 ? 0.5940 0.2947 0.5094 0.0364  0.0692  0.0075  170 ALA C C   
9840  O O   . ALA C 170 ? 0.5583 0.2616 0.4701 0.0309  0.0574  0.0056  170 ALA C O   
9841  C CB  . ALA C 170 ? 0.6277 0.2877 0.4919 0.0445  0.0822  0.0037  170 ALA C CB  
9842  N N   . ASN C 171 ? 0.5717 0.2802 0.5045 0.0376  0.0716  0.0083  171 ASN C N   
9843  C CA  . ASN C 171 ? 0.5669 0.2889 0.5168 0.0324  0.0615  0.0078  171 ASN C CA  
9844  C C   . ASN C 171 ? 0.6008 0.3086 0.5334 0.0285  0.0523  0.0023  171 ASN C C   
9845  O O   . ASN C 171 ? 0.6273 0.3157 0.5419 0.0315  0.0563  -0.0008 171 ASN C O   
9846  C CB  . ASN C 171 ? 0.5812 0.3137 0.5526 0.0358  0.0680  0.0111  171 ASN C CB  
9847  C CG  . ASN C 171 ? 0.5865 0.3350 0.5771 0.0311  0.0590  0.0119  171 ASN C CG  
9848  O OD1 . ASN C 171 ? 0.5851 0.3280 0.5696 0.0275  0.0516  0.0088  171 ASN C OD1 
9849  N ND2 . ASN C 171 ? 0.6025 0.3702 0.6158 0.0310  0.0594  0.0160  171 ASN C ND2 
9850  N N   . ALA C 172 ? 0.5736 0.2914 0.5131 0.0218  0.0401  0.0013  172 ALA C N   
9851  C CA  . ALA C 172 ? 0.5675 0.2747 0.4944 0.0168  0.0297  -0.0032 172 ALA C CA  
9852  C C   . ALA C 172 ? 0.5707 0.2726 0.5010 0.0167  0.0302  -0.0044 172 ALA C C   
9853  O O   . ALA C 172 ? 0.6027 0.2892 0.5184 0.0142  0.0249  -0.0086 172 ALA C O   
9854  C CB  . ALA C 172 ? 0.5415 0.2641 0.4802 0.0102  0.0182  -0.0029 172 ALA C CB  
9855  N N   . MET C 173 ? 0.5668 0.2815 0.5170 0.0192  0.0358  -0.0006 173 MET C N   
9856  C CA  . MET C 173 ? 0.5540 0.2656 0.5101 0.0193  0.0361  -0.0006 173 MET C CA  
9857  C C   . MET C 173 ? 0.5656 0.2561 0.5062 0.0255  0.0450  -0.0028 173 MET C C   
9858  O O   . MET C 173 ? 0.5781 0.2592 0.5164 0.0248  0.0433  -0.0044 173 MET C O   
9859  C CB  . MET C 173 ? 0.5272 0.2598 0.5094 0.0199  0.0378  0.0045  173 MET C CB  
9860  C CG  . MET C 173 ? 0.4974 0.2485 0.4936 0.0134  0.0283  0.0058  173 MET C CG  
9861  S SD  . MET C 173 ? 0.5134 0.2613 0.5081 0.0060  0.0177  0.0037  173 MET C SD  
9862  C CE  . MET C 173 ? 0.5079 0.2561 0.5136 0.0086  0.0218  0.0070  173 MET C CE  
9863  N N   . ILE C 174 ? 0.5911 0.2739 0.5212 0.0316  0.0548  -0.0027 174 ILE C N   
9864  C CA  . ILE C 174 ? 0.6138 0.2764 0.5287 0.0385  0.0651  -0.0048 174 ILE C CA  
9865  C C   . ILE C 174 ? 0.6417 0.2825 0.5259 0.0398  0.0663  -0.0095 174 ILE C C   
9866  O O   . ILE C 174 ? 0.6582 0.2774 0.5235 0.0447  0.0729  -0.0131 174 ILE C O   
9867  C CB  . ILE C 174 ? 0.6089 0.2794 0.5388 0.0464  0.0789  0.0001  174 ILE C CB  
9868  C CG1 . ILE C 174 ? 0.6268 0.3082 0.5608 0.0476  0.0836  0.0034  174 ILE C CG1 
9869  C CG2 . ILE C 174 ? 0.5682 0.2551 0.5250 0.0466  0.0783  0.0045  174 ILE C CG2 
9870  C CD1 . ILE C 174 ? 0.6368 0.3187 0.5775 0.0560  0.0991  0.0072  174 ILE C CD1 
9871  N N   . SER C 175 ? 0.6127 0.2578 0.4905 0.0362  0.0608  -0.0096 175 SER C N   
9872  C CA  . SER C 175 ? 0.6366 0.2601 0.4834 0.0376  0.0612  -0.0138 175 SER C CA  
9873  C C   . SER C 175 ? 0.6344 0.2547 0.4707 0.0297  0.0454  -0.0173 175 SER C C   
9874  O O   . SER C 175 ? 0.6454 0.2556 0.4616 0.0291  0.0423  -0.0191 175 SER C O   
9875  C CB  . SER C 175 ? 0.6502 0.2760 0.4934 0.0428  0.0718  -0.0102 175 SER C CB  
9876  O OG  . SER C 175 ? 0.6408 0.2709 0.4968 0.0500  0.0865  -0.0064 175 SER C OG  
9877  N N   . ASP C 176 ? 0.6366 0.2651 0.4869 0.0236  0.0354  -0.0181 176 ASP C N   
9878  C CA  . ASP C 176 ? 0.6598 0.2814 0.5001 0.0161  0.0207  -0.0222 176 ASP C CA  
9879  C C   . ASP C 176 ? 0.7143 0.3060 0.5206 0.0173  0.0187  -0.0286 176 ASP C C   
9880  O O   . ASP C 176 ? 0.7573 0.3417 0.5492 0.0127  0.0078  -0.0315 176 ASP C O   
9881  C CB  . ASP C 176 ? 0.6494 0.2802 0.5084 0.0107  0.0137  -0.0219 176 ASP C CB  
9882  C CG  . ASP C 176 ? 0.6405 0.2611 0.5005 0.0140  0.0202  -0.0227 176 ASP C CG  
9883  O OD1 . ASP C 176 ? 0.6285 0.2372 0.4780 0.0216  0.0319  -0.0232 176 ASP C OD1 
9884  O OD2 . ASP C 176 ? 0.6257 0.2504 0.4976 0.0090  0.0137  -0.0226 176 ASP C OD2 
9885  N N   . TYR C 177 ? 0.7390 0.3125 0.5319 0.0235  0.0288  -0.0311 177 TYR C N   
9886  C CA  . TYR C 177 ? 0.7678 0.3105 0.5269 0.0249  0.0272  -0.0380 177 TYR C CA  
9887  C C   . TYR C 177 ? 0.7915 0.3219 0.5242 0.0289  0.0312  -0.0389 177 TYR C C   
9888  O O   . TYR C 177 ? 0.8014 0.3079 0.5037 0.0279  0.0250  -0.0448 177 TYR C O   
9889  C CB  . TYR C 177 ? 0.7724 0.2998 0.5268 0.0310  0.0379  -0.0403 177 TYR C CB  
9890  C CG  . TYR C 177 ? 0.7720 0.3010 0.5278 0.0410  0.0563  -0.0367 177 TYR C CG  
9891  C CD1 . TYR C 177 ? 0.8043 0.3119 0.5307 0.0477  0.0658  -0.0396 177 TYR C CD1 
9892  C CD2 . TYR C 177 ? 0.7516 0.3051 0.5388 0.0434  0.0638  -0.0299 177 TYR C CD2 
9893  C CE1 . TYR C 177 ? 0.8098 0.3209 0.5400 0.0566  0.0833  -0.0355 177 TYR C CE1 
9894  C CE2 . TYR C 177 ? 0.7471 0.3045 0.5391 0.0518  0.0798  -0.0259 177 TYR C CE2 
9895  C CZ  . TYR C 177 ? 0.7698 0.3064 0.5343 0.0585  0.0902  -0.0286 177 TYR C CZ  
9896  O OH  . TYR C 177 ? 0.7767 0.3190 0.5494 0.0667  0.1067  -0.0239 177 TYR C OH  
9897  N N   . MET C 178 ? 0.7681 0.3134 0.5115 0.0334  0.0417  -0.0331 178 MET C N   
9898  C CA  . MET C 178 ? 0.7955 0.3280 0.5149 0.0394  0.0510  -0.0326 178 MET C CA  
9899  C C   . MET C 178 ? 0.8186 0.3441 0.5181 0.0347  0.0383  -0.0344 178 MET C C   
9900  O O   . MET C 178 ? 0.8030 0.3449 0.5188 0.0276  0.0253  -0.0328 178 MET C O   
9901  C CB  . MET C 178 ? 0.7671 0.3200 0.5076 0.0440  0.0639  -0.0250 178 MET C CB  
9902  C CG  . MET C 178 ? 0.7927 0.3347 0.5117 0.0500  0.0748  -0.0231 178 MET C CG  
9903  S SD  . MET C 178 ? 0.7896 0.3560 0.5380 0.0550  0.0906  -0.0138 178 MET C SD  
9904  C CE  . MET C 178 ? 0.7799 0.3491 0.5469 0.0612  0.1038  -0.0132 178 MET C CE  
9905  N N   . ASP C 179 ? 0.8689 0.3694 0.5328 0.0390  0.0422  -0.0377 179 ASP C N   
9906  C CA  . ASP C 179 ? 0.9181 0.4103 0.5600 0.0360  0.0319  -0.0384 179 ASP C CA  
9907  C C   . ASP C 179 ? 0.8773 0.3862 0.5299 0.0384  0.0390  -0.0307 179 ASP C C   
9908  O O   . ASP C 179 ? 0.8590 0.3665 0.5093 0.0456  0.0558  -0.0273 179 ASP C O   
9909  C CB  . ASP C 179 ? 0.9733 0.4308 0.5706 0.0400  0.0334  -0.0447 179 ASP C CB  
9910  C CG  . ASP C 179 ? 1.0150 0.4589 0.5836 0.0374  0.0218  -0.0461 179 ASP C CG  
9911  O OD1 . ASP C 179 ? 0.9660 0.4267 0.5499 0.0310  0.0083  -0.0432 179 ASP C OD1 
9912  O OD2 . ASP C 179 ? 1.0891 0.5054 0.6195 0.0424  0.0268  -0.0499 179 ASP C OD2 
9913  N N   . GLU C 180 ? 0.8615 0.3860 0.5266 0.0325  0.0265  -0.0279 180 GLU C N   
9914  C CA  . GLU C 180 ? 0.8508 0.3896 0.5256 0.0344  0.0321  -0.0208 180 GLU C CA  
9915  C C   . GLU C 180 ? 0.8797 0.4036 0.5252 0.0339  0.0245  -0.0208 180 GLU C C   
9916  O O   . GLU C 180 ? 0.8787 0.4117 0.5289 0.0351  0.0278  -0.0148 180 GLU C O   
9917  C CB  . GLU C 180 ? 0.8221 0.3917 0.5362 0.0292  0.0256  -0.0167 180 GLU C CB  
9918  C CG  . GLU C 180 ? 0.8123 0.3986 0.5556 0.0313  0.0363  -0.0143 180 GLU C CG  
9919  C CD  . GLU C 180 ? 0.7830 0.3985 0.5617 0.0284  0.0347  -0.0090 180 GLU C CD  
9920  O OE1 . GLU C 180 ? 0.8093 0.4329 0.5918 0.0243  0.0243  -0.0076 180 GLU C OE1 
9921  O OE2 . GLU C 180 ? 0.7793 0.4087 0.5812 0.0304  0.0434  -0.0064 180 GLU C OE2 
9922  N N   . SER C 181 ? 0.8996 0.3988 0.5134 0.0325  0.0150  -0.0274 181 SER C N   
9923  C CA  . SER C 181 ? 0.9283 0.4122 0.5134 0.0308  0.0034  -0.0283 181 SER C CA  
9924  C C   . SER C 181 ? 0.9683 0.4378 0.5266 0.0381  0.0170  -0.0244 181 SER C C   
9925  O O   . SER C 181 ? 0.9898 0.4504 0.5275 0.0374  0.0093  -0.0227 181 SER C O   
9926  C CB  . SER C 181 ? 0.9548 0.4147 0.5126 0.0275  -0.0100 -0.0368 181 SER C CB  
9927  O OG  . SER C 181 ? 0.9728 0.4055 0.4977 0.0343  0.0023  -0.0409 181 SER C OG  
9928  N N   . ILE C 182 ? 0.9739 0.4401 0.5314 0.0451  0.0373  -0.0228 182 ILE C N   
9929  C CA  . ILE C 182 ? 0.9911 0.4453 0.5262 0.0522  0.0527  -0.0183 182 ILE C CA  
9930  C C   . ILE C 182 ? 0.9609 0.4389 0.5224 0.0518  0.0572  -0.0090 182 ILE C C   
9931  O O   . ILE C 182 ? 0.9749 0.4448 0.5199 0.0564  0.0678  -0.0040 182 ILE C O   
9932  C CB  . ILE C 182 ? 1.0213 0.4647 0.5493 0.0602  0.0736  -0.0196 182 ILE C CB  
9933  C CG1 . ILE C 182 ? 0.9851 0.4562 0.5580 0.0606  0.0831  -0.0157 182 ILE C CG1 
9934  C CG2 . ILE C 182 ? 1.0461 0.4622 0.5438 0.0610  0.0690  -0.0294 182 ILE C CG2 
9935  C CD1 . ILE C 182 ? 0.9968 0.4605 0.5683 0.0687  0.1036  -0.0160 182 ILE C CD1 
9936  N N   . PHE C 183 ? 0.9209 0.4270 0.5227 0.0466  0.0502  -0.0068 183 PHE C N   
9937  C CA  . PHE C 183 ? 0.8701 0.3995 0.5000 0.0459  0.0540  0.0013  183 PHE C CA  
9938  C C   . PHE C 183 ? 0.8758 0.4107 0.5062 0.0404  0.0362  0.0027  183 PHE C C   
9939  O O   . PHE C 183 ? 0.8944 0.4209 0.5123 0.0361  0.0199  -0.0025 183 PHE C O   
9940  C CB  . PHE C 183 ? 0.8062 0.3619 0.4785 0.0442  0.0577  0.0025  183 PHE C CB  
9941  C CG  . PHE C 183 ? 0.8030 0.3558 0.4795 0.0499  0.0748  0.0018  183 PHE C CG  
9942  C CD1 . PHE C 183 ? 0.8018 0.3554 0.4804 0.0561  0.0935  0.0077  183 PHE C CD1 
9943  C CD2 . PHE C 183 ? 0.7938 0.3432 0.4734 0.0491  0.0721  -0.0043 183 PHE C CD2 
9944  C CE1 . PHE C 183 ? 0.8121 0.3634 0.4959 0.0618  0.1091  0.0073  183 PHE C CE1 
9945  C CE2 . PHE C 183 ? 0.7877 0.3344 0.4722 0.0549  0.0875  -0.0046 183 PHE C CE2 
9946  C CZ  . PHE C 183 ? 0.7916 0.3394 0.4782 0.0614  0.1059  0.0011  183 PHE C CZ  
9947  N N   . ASP C 184 ? 0.8626 0.4123 0.5096 0.0403  0.0388  0.0100  184 ASP C N   
9948  C CA  . ASP C 184 ? 0.8390 0.3923 0.4851 0.0363  0.0234  0.0121  184 ASP C CA  
9949  C C   . ASP C 184 ? 0.7880 0.3656 0.4693 0.0301  0.0102  0.0106  184 ASP C C   
9950  O O   . ASP C 184 ? 0.7916 0.3713 0.4726 0.0260  -0.0060 0.0099  184 ASP C O   
9951  C CB  . ASP C 184 ? 0.8280 0.3842 0.4746 0.0391  0.0316  0.0205  184 ASP C CB  
9952  C CG  . ASP C 184 ? 0.8777 0.4107 0.4903 0.0455  0.0467  0.0231  184 ASP C CG  
9953  O OD1 . ASP C 184 ? 0.9227 0.4314 0.4976 0.0467  0.0412  0.0195  184 ASP C OD1 
9954  O OD2 . ASP C 184 ? 0.9210 0.4606 0.5454 0.0493  0.0638  0.0287  184 ASP C OD2 
9955  N N   . VAL C 185 ? 0.7402 0.3359 0.4516 0.0297  0.0175  0.0104  185 VAL C N   
9956  C CA  . VAL C 185 ? 0.7055 0.3241 0.4497 0.0243  0.0071  0.0092  185 VAL C CA  
9957  C C   . VAL C 185 ? 0.6875 0.3117 0.4456 0.0241  0.0126  0.0054  185 VAL C C   
9958  O O   . VAL C 185 ? 0.6901 0.3081 0.4435 0.0289  0.0272  0.0061  185 VAL C O   
9959  C CB  . VAL C 185 ? 0.6919 0.3328 0.4654 0.0234  0.0084  0.0151  185 VAL C CB  
9960  C CG1 . VAL C 185 ? 0.7086 0.3417 0.4684 0.0267  0.0141  0.0213  185 VAL C CG1 
9961  C CG2 . VAL C 185 ? 0.6709 0.3302 0.4743 0.0242  0.0191  0.0166  185 VAL C CG2 
9962  N N   . TYR C 186 ? 0.6798 0.3152 0.4547 0.0188  0.0008  0.0019  186 TYR C N   
9963  C CA  . TYR C 186 ? 0.6698 0.3111 0.4589 0.0178  0.0036  -0.0014 186 TYR C CA  
9964  C C   . TYR C 186 ? 0.6529 0.3186 0.4761 0.0180  0.0104  0.0026  186 TYR C C   
9965  O O   . TYR C 186 ? 0.6516 0.3326 0.4916 0.0159  0.0057  0.0057  186 TYR C O   
9966  C CB  . TYR C 186 ? 0.6600 0.3020 0.4519 0.0117  -0.0119 -0.0064 186 TYR C CB  
9967  C CG  . TYR C 186 ? 0.6908 0.3082 0.4497 0.0107  -0.0208 -0.0110 186 TYR C CG  
9968  C CD1 . TYR C 186 ? 0.7322 0.3260 0.4625 0.0151  -0.0124 -0.0139 186 TYR C CD1 
9969  C CD2 . TYR C 186 ? 0.6889 0.3064 0.4456 0.0053  -0.0379 -0.0127 186 TYR C CD2 
9970  C CE1 . TYR C 186 ? 0.7659 0.3355 0.4638 0.0142  -0.0211 -0.0187 186 TYR C CE1 
9971  C CE2 . TYR C 186 ? 0.7221 0.3166 0.4485 0.0041  -0.0475 -0.0171 186 TYR C CE2 
9972  C CZ  . TYR C 186 ? 0.7674 0.3372 0.4630 0.0085  -0.0393 -0.0203 186 TYR C CZ  
9973  O OH  . TYR C 186 ? 0.8117 0.3569 0.4746 0.0074  -0.0491 -0.0250 186 TYR C OH  
9974  N N   . ALA C 187 ? 0.6422 0.3110 0.4753 0.0206  0.0208  0.0024  187 ALA C N   
9975  C CA  . ALA C 187 ? 0.5986 0.2894 0.4629 0.0208  0.0266  0.0060  187 ALA C CA  
9976  C C   . ALA C 187 ? 0.6028 0.2962 0.4774 0.0214  0.0309  0.0040  187 ALA C C   
9977  O O   . ALA C 187 ? 0.6428 0.3195 0.5002 0.0244  0.0364  0.0013  187 ALA C O   
9978  C CB  . ALA C 187 ? 0.5792 0.2724 0.4467 0.0253  0.0392  0.0115  187 ALA C CB  
9979  N N   . TYR C 188 ? 0.5663 0.2805 0.4688 0.0188  0.0285  0.0054  188 TYR C N   
9980  C CA  . TYR C 188 ? 0.5513 0.2715 0.4681 0.0199  0.0336  0.0052  188 TYR C CA  
9981  C C   . TYR C 188 ? 0.5202 0.2623 0.4655 0.0201  0.0371  0.0095  188 TYR C C   
9982  O O   . TYR C 188 ? 0.5177 0.2721 0.4739 0.0174  0.0316  0.0110  188 TYR C O   
9983  C CB  . TYR C 188 ? 0.5508 0.2711 0.4693 0.0150  0.0231  0.0012  188 TYR C CB  
9984  C CG  . TYR C 188 ? 0.5971 0.2945 0.4882 0.0144  0.0190  -0.0036 188 TYR C CG  
9985  C CD1 . TYR C 188 ? 0.6128 0.2923 0.4872 0.0193  0.0282  -0.0053 188 TYR C CD1 
9986  C CD2 . TYR C 188 ? 0.6019 0.2955 0.4847 0.0091  0.0057  -0.0065 188 TYR C CD2 
9987  C CE1 . TYR C 188 ? 0.6543 0.3111 0.5022 0.0188  0.0241  -0.0104 188 TYR C CE1 
9988  C CE2 . TYR C 188 ? 0.6283 0.3002 0.4859 0.0082  0.0008  -0.0112 188 TYR C CE2 
9989  C CZ  . TYR C 188 ? 0.6461 0.2990 0.4854 0.0130  0.0098  -0.0134 188 TYR C CZ  
9990  O OH  . TYR C 188 ? 0.6878 0.3174 0.5004 0.0123  0.0050  -0.0186 188 TYR C OH  
9991  N N   . ASN C 189 ? 0.5170 0.2632 0.4741 0.0234  0.0457  0.0112  189 ASN C N   
9992  C CA  . ASN C 189 ? 0.5044 0.2708 0.4887 0.0222  0.0451  0.0138  189 ASN C CA  
9993  C C   . ASN C 189 ? 0.4820 0.2531 0.4720 0.0181  0.0363  0.0111  189 ASN C C   
9994  O O   . ASN C 189 ? 0.5434 0.3030 0.5236 0.0187  0.0368  0.0087  189 ASN C O   
9995  C CB  . ASN C 189 ? 0.5172 0.2868 0.5132 0.0274  0.0568  0.0173  189 ASN C CB  
9996  C CG  . ASN C 189 ? 0.5328 0.2973 0.5236 0.0316  0.0671  0.0206  189 ASN C CG  
9997  O OD1 . ASN C 189 ? 0.5600 0.3158 0.5460 0.0369  0.0782  0.0220  189 ASN C OD1 
9998  N ND2 . ASN C 189 ? 0.5204 0.2892 0.5114 0.0295  0.0639  0.0221  189 ASN C ND2 
9999  N N   . CYS C 190 ? 0.4492 0.2367 0.4551 0.0140  0.0288  0.0115  190 CYS C N   
10000 C CA  . CYS C 190 ? 0.4540 0.2459 0.4637 0.0093  0.0199  0.0092  190 CYS C CA  
10001 C C   . CYS C 190 ? 0.4233 0.2334 0.4551 0.0083  0.0191  0.0115  190 CYS C C   
10002 O O   . CYS C 190 ? 0.4370 0.2600 0.4809 0.0076  0.0177  0.0130  190 CYS C O   
10003 C CB  . CYS C 190 ? 0.4829 0.2763 0.4879 0.0048  0.0103  0.0072  190 CYS C CB  
10004 S SG  . CYS C 190 ? 0.5200 0.2923 0.4975 0.0053  0.0082  0.0045  190 CYS C SG  
10005 N N   . TYR C 191 ? 0.4100 0.2195 0.4455 0.0083  0.0197  0.0117  191 TYR C N   
10006 C CA  . TYR C 191 ? 0.3975 0.2218 0.4508 0.0075  0.0186  0.0139  191 TYR C CA  
10007 C C   . TYR C 191 ? 0.4094 0.2346 0.4625 0.0030  0.0120  0.0126  191 TYR C C   
10008 O O   . TYR C 191 ? 0.4316 0.2438 0.4734 0.0021  0.0112  0.0108  191 TYR C O   
10009 C CB  . TYR C 191 ? 0.4036 0.2270 0.4636 0.0125  0.0265  0.0169  191 TYR C CB  
10010 C CG  . TYR C 191 ? 0.3890 0.2166 0.4553 0.0160  0.0326  0.0192  191 TYR C CG  
10011 C CD1 . TYR C 191 ? 0.4029 0.2464 0.4858 0.0150  0.0304  0.0211  191 TYR C CD1 
10012 C CD2 . TYR C 191 ? 0.3852 0.2003 0.4398 0.0197  0.0400  0.0192  191 TYR C CD2 
10013 C CE1 . TYR C 191 ? 0.3826 0.2305 0.4730 0.0173  0.0352  0.0235  191 TYR C CE1 
10014 C CE2 . TYR C 191 ? 0.4002 0.2199 0.4618 0.0222  0.0458  0.0220  191 TYR C CE2 
10015 C CZ  . TYR C 191 ? 0.3940 0.2304 0.4746 0.0208  0.0432  0.0243  191 TYR C CZ  
10016 O OH  . TYR C 191 ? 0.4255 0.2672 0.5156 0.0226  0.0481  0.0273  191 TYR C OH  
10017 N N   . ASP C 192 ? 0.4093 0.2495 0.4749 0.0002  0.0075  0.0134  192 ASP C N   
10018 C CA  . ASP C 192 ? 0.4184 0.2624 0.4867 -0.0040 0.0024  0.0133  192 ASP C CA  
10019 C C   . ASP C 192 ? 0.3940 0.2456 0.4729 -0.0026 0.0043  0.0165  192 ASP C C   
10020 O O   . ASP C 192 ? 0.3750 0.2399 0.4645 -0.0027 0.0031  0.0178  192 ASP C O   
10021 C CB  . ASP C 192 ? 0.4033 0.2580 0.4766 -0.0079 -0.0036 0.0120  192 ASP C CB  
10022 C CG  . ASP C 192 ? 0.3982 0.2569 0.4747 -0.0125 -0.0079 0.0121  192 ASP C CG  
10023 O OD1 . ASP C 192 ? 0.4056 0.2571 0.4791 -0.0130 -0.0068 0.0132  192 ASP C OD1 
10024 O OD2 . ASP C 192 ? 0.4429 0.3117 0.5253 -0.0152 -0.0118 0.0115  192 ASP C OD2 
10025 N N   . HIS C 193 ? 0.4226 0.2645 0.4976 -0.0013 0.0069  0.0176  193 HIS C N   
10026 C CA  . HIS C 193 ? 0.4163 0.2628 0.4998 0.0003  0.0083  0.0212  193 HIS C CA  
10027 C C   . HIS C 193 ? 0.3968 0.2399 0.4777 -0.0038 0.0048  0.0219  193 HIS C C   
10028 O O   . HIS C 193 ? 0.3597 0.2034 0.4449 -0.0028 0.0056  0.0251  193 HIS C O   
10029 C CB  . HIS C 193 ? 0.4197 0.2570 0.5022 0.0060  0.0149  0.0228  193 HIS C CB  
10030 C CG  . HIS C 193 ? 0.4278 0.2687 0.5151 0.0101  0.0196  0.0233  193 HIS C CG  
10031 N ND1 . HIS C 193 ? 0.4140 0.2697 0.5132 0.0100  0.0180  0.0245  193 HIS C ND1 
10032 C CD2 . HIS C 193 ? 0.4533 0.2847 0.5355 0.0145  0.0263  0.0229  193 HIS C CD2 
10033 C CE1 . HIS C 193 ? 0.3894 0.2449 0.4923 0.0138  0.0233  0.0254  193 HIS C CE1 
10034 N NE2 . HIS C 193 ? 0.4214 0.2626 0.5138 0.0167  0.0289  0.0246  193 HIS C NE2 
10035 N N   . ASN C 194 ? 0.4060 0.2449 0.4802 -0.0083 0.0008  0.0191  194 ASN C N   
10036 C CA  . ASN C 194 ? 0.4199 0.2563 0.4933 -0.0131 -0.0026 0.0199  194 ASN C CA  
10037 C C   . ASN C 194 ? 0.3975 0.2202 0.4663 -0.0115 0.0000  0.0216  194 ASN C C   
10038 O O   . ASN C 194 ? 0.3658 0.1907 0.4393 -0.0128 -0.0004 0.0250  194 ASN C O   
10039 C CB  . ASN C 194 ? 0.4010 0.2535 0.4848 -0.0156 -0.0047 0.0226  194 ASN C CB  
10040 C CG  . ASN C 194 ? 0.4370 0.2883 0.5212 -0.0210 -0.0075 0.0241  194 ASN C CG  
10041 O OD1 . ASN C 194 ? 0.4361 0.2763 0.5143 -0.0243 -0.0097 0.0224  194 ASN C OD1 
10042 N ND2 . ASN C 194 ? 0.4617 0.3240 0.5528 -0.0220 -0.0075 0.0276  194 ASN C ND2 
10043 N N   . GLU C 195 ? 0.4173 0.2251 0.4762 -0.0083 0.0031  0.0191  195 GLU C N   
10044 C CA  . GLU C 195 ? 0.4315 0.2242 0.4851 -0.0058 0.0062  0.0199  195 GLU C CA  
10045 C C   . GLU C 195 ? 0.4350 0.2088 0.4727 -0.0058 0.0064  0.0150  195 GLU C C   
10046 O O   . GLU C 195 ? 0.4136 0.1865 0.4447 -0.0055 0.0059  0.0119  195 GLU C O   
10047 C CB  . GLU C 195 ? 0.4154 0.2116 0.4763 0.0011  0.0123  0.0232  195 GLU C CB  
10048 C CG  . GLU C 195 ? 0.4098 0.2044 0.4679 0.0062  0.0175  0.0213  195 GLU C CG  
10049 C CD  . GLU C 195 ? 0.4152 0.2159 0.4841 0.0127  0.0234  0.0249  195 GLU C CD  
10050 O OE1 . GLU C 195 ? 0.4303 0.2329 0.5062 0.0135  0.0229  0.0285  195 GLU C OE1 
10051 O OE2 . GLU C 195 ? 0.4028 0.2057 0.4734 0.0166  0.0283  0.0245  195 GLU C OE2 
10052 N N   . GLY C 196 ? 0.4512 0.2086 0.4817 -0.0057 0.0070  0.0145  196 GLY C N   
10053 C CA  . GLY C 196 ? 0.4667 0.2038 0.4799 -0.0060 0.0063  0.0092  196 GLY C CA  
10054 C C   . GLY C 196 ? 0.4637 0.2026 0.4717 -0.0122 -0.0012 0.0058  196 GLY C C   
10055 O O   . GLY C 196 ? 0.4606 0.2081 0.4763 -0.0186 -0.0075 0.0070  196 GLY C O   
10056 N N   . GLN C 197 ? 0.4657 0.1959 0.4603 -0.0101 -0.0006 0.0017  197 GLN C N   
10057 C CA  . GLN C 197 ? 0.4622 0.1917 0.4499 -0.0151 -0.0082 -0.0016 197 GLN C CA  
10058 C C   . GLN C 197 ? 0.4569 0.2093 0.4605 -0.0186 -0.0122 0.0010  197 GLN C C   
10059 O O   . GLN C 197 ? 0.4459 0.2011 0.4505 -0.0245 -0.0201 -0.0004 197 GLN C O   
10060 C CB  . GLN C 197 ? 0.4745 0.1938 0.4462 -0.0103 -0.0047 -0.0048 197 GLN C CB  
10061 C CG  . GLN C 197 ? 0.5053 0.1996 0.4571 -0.0063 -0.0005 -0.0086 197 GLN C CG  
10062 C CD  . GLN C 197 ? 0.5136 0.2062 0.4667 0.0021  0.0114  -0.0065 197 GLN C CD  
10063 O OE1 . GLN C 197 ? 0.5024 0.2070 0.4722 0.0040  0.0151  -0.0021 197 GLN C OE1 
10064 N NE2 . GLN C 197 ? 0.5415 0.2196 0.4774 0.0075  0.0175  -0.0092 197 GLN C NE2 
10065 N N   . THR C 198 ? 0.4355 0.2038 0.4514 -0.0149 -0.0071 0.0045  198 THR C N   
10066 C CA  . THR C 198 ? 0.4196 0.2080 0.4492 -0.0178 -0.0105 0.0063  198 THR C CA  
10067 C C   . THR C 198 ? 0.4194 0.2177 0.4614 -0.0223 -0.0131 0.0095  198 THR C C   
10068 O O   . THR C 198 ? 0.4060 0.2189 0.4576 -0.0256 -0.0167 0.0103  198 THR C O   
10069 C CB  . THR C 198 ? 0.4062 0.2071 0.4433 -0.0129 -0.0055 0.0082  198 THR C CB  
10070 O OG1 . THR C 198 ? 0.4020 0.2060 0.4463 -0.0090 0.0002  0.0115  198 THR C OG1 
10071 C CG2 . THR C 198 ? 0.4025 0.1956 0.4283 -0.0094 -0.0032 0.0058  198 THR C CG2 
10072 N N   . ALA C 199 ? 0.4209 0.2106 0.4621 -0.0223 -0.0113 0.0112  199 ALA C N   
10073 C CA  . ALA C 199 ? 0.4229 0.2194 0.4738 -0.0270 -0.0135 0.0147  199 ALA C CA  
10074 C C   . ALA C 199 ? 0.4428 0.2320 0.4910 -0.0342 -0.0202 0.0128  199 ALA C C   
10075 O O   . ALA C 199 ? 0.4581 0.2579 0.5166 -0.0394 -0.0234 0.0152  199 ALA C O   
10076 C CB  . ALA C 199 ? 0.4208 0.2111 0.4728 -0.0243 -0.0092 0.0182  199 ALA C CB  
10077 N N   . THR C 200 ? 0.4679 0.2385 0.5022 -0.0343 -0.0224 0.0086  200 THR C N   
10078 C CA  . THR C 200 ? 0.5000 0.2613 0.5312 -0.0413 -0.0299 0.0065  200 THR C CA  
10079 C C   . THR C 200 ? 0.5164 0.2862 0.5497 -0.0448 -0.0364 0.0042  200 THR C C   
10080 O O   . THR C 200 ? 0.5060 0.2829 0.5490 -0.0514 -0.0422 0.0052  200 THR C O   
10081 C CB  . THR C 200 ? 0.5078 0.2440 0.5220 -0.0402 -0.0303 0.0026  200 THR C CB  
10082 O OG1 . THR C 200 ? 0.4860 0.2167 0.4876 -0.0349 -0.0282 -0.0011 200 THR C OG1 
10083 C CG2 . THR C 200 ? 0.5162 0.2439 0.5303 -0.0368 -0.0242 0.0052  200 THR C CG2 
10084 N N   . MET C 201 ? 0.5135 0.2824 0.5385 -0.0403 -0.0354 0.0015  201 MET C N   
10085 C CA  . MET C 201 ? 0.5174 0.2896 0.5409 -0.0432 -0.0426 -0.0011 201 MET C CA  
10086 C C   . MET C 201 ? 0.4977 0.2921 0.5355 -0.0422 -0.0416 0.0013  201 MET C C   
10087 O O   . MET C 201 ? 0.4734 0.2754 0.5166 -0.0455 -0.0479 0.0005  201 MET C O   
10088 C CB  . MET C 201 ? 0.5351 0.2893 0.5377 -0.0395 -0.0432 -0.0056 201 MET C CB  
10089 C CG  . MET C 201 ? 0.5249 0.2553 0.5113 -0.0418 -0.0472 -0.0095 201 MET C CG  
10090 S SD  . MET C 201 ? 0.5220 0.2297 0.4803 -0.0359 -0.0453 -0.0147 201 MET C SD  
10091 C CE  . MET C 201 ? 0.5315 0.2334 0.4894 -0.0292 -0.0326 -0.0127 201 MET C CE  
10092 N N   . GLY C 202 ? 0.5017 0.3064 0.5464 -0.0376 -0.0341 0.0042  202 GLY C N   
10093 C CA  . GLY C 202 ? 0.4801 0.3020 0.5343 -0.0353 -0.0324 0.0054  202 GLY C CA  
10094 C C   . GLY C 202 ? 0.4702 0.2862 0.5138 -0.0304 -0.0308 0.0031  202 GLY C C   
10095 O O   . GLY C 202 ? 0.5069 0.3068 0.5354 -0.0300 -0.0328 0.0002  202 GLY C O   
10096 N N   . PHE C 203 ? 0.4545 0.2827 0.5051 -0.0267 -0.0269 0.0044  203 PHE C N   
10097 C CA  . PHE C 203 ? 0.4336 0.2566 0.4756 -0.0219 -0.0238 0.0033  203 PHE C CA  
10098 C C   . PHE C 203 ? 0.4318 0.2490 0.4653 -0.0238 -0.0305 0.0007  203 PHE C C   
10099 O O   . PHE C 203 ? 0.4618 0.2633 0.4790 -0.0219 -0.0303 -0.0012 203 PHE C O   
10100 C CB  . PHE C 203 ? 0.4249 0.2632 0.4786 -0.0187 -0.0198 0.0054  203 PHE C CB  
10101 C CG  . PHE C 203 ? 0.4059 0.2404 0.4543 -0.0135 -0.0145 0.0055  203 PHE C CG  
10102 C CD1 . PHE C 203 ? 0.4185 0.2389 0.4555 -0.0098 -0.0089 0.0054  203 PHE C CD1 
10103 C CD2 . PHE C 203 ? 0.4060 0.2513 0.4620 -0.0120 -0.0144 0.0062  203 PHE C CD2 
10104 C CE1 . PHE C 203 ? 0.4333 0.2515 0.4674 -0.0052 -0.0030 0.0064  203 PHE C CE1 
10105 C CE2 . PHE C 203 ? 0.3917 0.2341 0.4447 -0.0078 -0.0093 0.0070  203 PHE C CE2 
10106 C CZ  . PHE C 203 ? 0.4171 0.2465 0.4596 -0.0045 -0.0034 0.0074  203 PHE C CZ  
10107 N N   . LYS C 204 ? 0.4217 0.2509 0.4658 -0.0273 -0.0366 0.0008  204 LYS C N   
10108 C CA  . LYS C 204 ? 0.4406 0.2660 0.4786 -0.0286 -0.0438 -0.0010 204 LYS C CA  
10109 C C   . LYS C 204 ? 0.4448 0.2518 0.4672 -0.0314 -0.0493 -0.0036 204 LYS C C   
10110 O O   . LYS C 204 ? 0.4549 0.2489 0.4611 -0.0297 -0.0515 -0.0055 204 LYS C O   
10111 C CB  . LYS C 204 ? 0.4022 0.2436 0.4561 -0.0319 -0.0498 -0.0003 204 LYS C CB  
10112 C CG  . LYS C 204 ? 0.4060 0.2421 0.4552 -0.0349 -0.0597 -0.0020 204 LYS C CG  
10113 C CD  . LYS C 204 ? 0.4039 0.2563 0.4721 -0.0388 -0.0656 -0.0010 204 LYS C CD  
10114 C CE  . LYS C 204 ? 0.4234 0.2703 0.4883 -0.0422 -0.0768 -0.0024 204 LYS C CE  
10115 N NZ  . LYS C 204 ? 0.4274 0.2894 0.5128 -0.0468 -0.0818 -0.0010 204 LYS C NZ  
10116 N N   . ASP C 205 ? 0.4540 0.2592 0.4804 -0.0360 -0.0520 -0.0038 205 ASP C N   
10117 C CA  . ASP C 205 ? 0.4816 0.2696 0.4946 -0.0397 -0.0592 -0.0068 205 ASP C CA  
10118 C C   . ASP C 205 ? 0.5157 0.2829 0.5077 -0.0356 -0.0537 -0.0089 205 ASP C C   
10119 O O   . ASP C 205 ? 0.5517 0.3010 0.5254 -0.0363 -0.0587 -0.0123 205 ASP C O   
10120 C CB  . ASP C 205 ? 0.4902 0.2813 0.5145 -0.0464 -0.0640 -0.0061 205 ASP C CB  
10121 C CG  . ASP C 205 ? 0.4734 0.2819 0.5168 -0.0513 -0.0708 -0.0044 205 ASP C CG  
10122 O OD1 . ASP C 205 ? 0.4812 0.2999 0.5298 -0.0494 -0.0726 -0.0040 205 ASP C OD1 
10123 O OD2 . ASP C 205 ? 0.4700 0.2818 0.5239 -0.0568 -0.0736 -0.0032 205 ASP C OD2 
10124 N N   . TYR C 206 ? 0.5193 0.2883 0.5134 -0.0309 -0.0436 -0.0071 206 TYR C N   
10125 C CA  . TYR C 206 ? 0.5608 0.3110 0.5367 -0.0262 -0.0371 -0.0089 206 TYR C CA  
10126 C C   . TYR C 206 ? 0.5560 0.2972 0.5154 -0.0222 -0.0364 -0.0105 206 TYR C C   
10127 O O   . TYR C 206 ? 0.5872 0.3084 0.5255 -0.0216 -0.0385 -0.0139 206 TYR C O   
10128 C CB  . TYR C 206 ? 0.5323 0.2875 0.5154 -0.0211 -0.0262 -0.0060 206 TYR C CB  
10129 C CG  . TYR C 206 ? 0.5353 0.2718 0.5013 -0.0154 -0.0185 -0.0076 206 TYR C CG  
10130 C CD1 . TYR C 206 ? 0.5699 0.2846 0.5180 -0.0164 -0.0210 -0.0115 206 TYR C CD1 
10131 C CD2 . TYR C 206 ? 0.5217 0.2618 0.4897 -0.0089 -0.0086 -0.0054 206 TYR C CD2 
10132 C CE1 . TYR C 206 ? 0.5854 0.2825 0.5175 -0.0105 -0.0129 -0.0133 206 TYR C CE1 
10133 C CE2 . TYR C 206 ? 0.5521 0.2763 0.5065 -0.0032 -0.0003 -0.0064 206 TYR C CE2 
10134 C CZ  . TYR C 206 ? 0.5842 0.2866 0.5199 -0.0036 -0.0020 -0.0105 206 TYR C CZ  
10135 O OH  . TYR C 206 ? 0.6062 0.2919 0.5273 0.0026  0.0069  -0.0120 206 TYR C OH  
10136 N N   . ILE C 207 ? 0.5250 0.2800 0.4932 -0.0194 -0.0332 -0.0079 207 ILE C N   
10137 C CA  . ILE C 207 ? 0.5496 0.2974 0.5038 -0.0156 -0.0315 -0.0083 207 ILE C CA  
10138 C C   . ILE C 207 ? 0.5460 0.2861 0.4889 -0.0193 -0.0430 -0.0107 207 ILE C C   
10139 O O   . ILE C 207 ? 0.5942 0.3172 0.5150 -0.0170 -0.0435 -0.0126 207 ILE C O   
10140 C CB  . ILE C 207 ? 0.5313 0.2961 0.5002 -0.0125 -0.0260 -0.0047 207 ILE C CB  
10141 C CG1 . ILE C 207 ? 0.5374 0.3089 0.5171 -0.0089 -0.0159 -0.0023 207 ILE C CG1 
10142 C CG2 . ILE C 207 ? 0.5663 0.3234 0.5213 -0.0088 -0.0241 -0.0043 207 ILE C CG2 
10143 C CD1 . ILE C 207 ? 0.5460 0.3006 0.5106 -0.0041 -0.0073 -0.0030 207 ILE C CD1 
10144 N N   . LYS C 208 ? 0.5140 0.2667 0.4719 -0.0248 -0.0522 -0.0104 208 LYS C N   
10145 C CA  . LYS C 208 ? 0.5398 0.2867 0.4902 -0.0286 -0.0643 -0.0124 208 LYS C CA  
10146 C C   . LYS C 208 ? 0.5453 0.2690 0.4739 -0.0307 -0.0693 -0.0166 208 LYS C C   
10147 O O   . LYS C 208 ? 0.5449 0.2548 0.4550 -0.0311 -0.0768 -0.0188 208 LYS C O   
10148 C CB  . LYS C 208 ? 0.5631 0.3288 0.5371 -0.0341 -0.0721 -0.0110 208 LYS C CB  
10149 C CG  . LYS C 208 ? 0.6237 0.3861 0.5941 -0.0382 -0.0856 -0.0124 208 LYS C CG  
10150 C CD  . LYS C 208 ? 0.6758 0.4598 0.6723 -0.0422 -0.0917 -0.0102 208 LYS C CD  
10151 C CE  . LYS C 208 ? 0.7316 0.5202 0.7413 -0.0482 -0.0943 -0.0103 208 LYS C CE  
10152 N NZ  . LYS C 208 ? 0.7870 0.5605 0.7857 -0.0533 -0.1057 -0.0133 208 LYS C NZ  
10153 N N   . GLY C 209 ? 0.5365 0.2546 0.4662 -0.0320 -0.0658 -0.0177 209 GLY C N   
10154 C CA  . GLY C 209 ? 0.5590 0.2537 0.4683 -0.0339 -0.0702 -0.0222 209 GLY C CA  
10155 C C   . GLY C 209 ? 0.5925 0.2654 0.4734 -0.0275 -0.0633 -0.0247 209 GLY C C   
10156 O O   . GLY C 209 ? 0.6054 0.2573 0.4633 -0.0285 -0.0695 -0.0290 209 GLY C O   
10157 N N   . LEU C 210 ? 0.6074 0.2850 0.4895 -0.0208 -0.0504 -0.0220 210 LEU C N   
10158 C CA  . LEU C 210 ? 0.6405 0.2995 0.4974 -0.0143 -0.0424 -0.0235 210 LEU C CA  
10159 C C   . LEU C 210 ? 0.6601 0.3132 0.5014 -0.0142 -0.0491 -0.0239 210 LEU C C   
10160 O O   . LEU C 210 ? 0.6956 0.3266 0.5086 -0.0117 -0.0494 -0.0269 210 LEU C O   
10161 C CB  . LEU C 210 ? 0.6367 0.3053 0.5035 -0.0078 -0.0274 -0.0196 210 LEU C CB  
10162 C CG  . LEU C 210 ? 0.6244 0.2970 0.5044 -0.0066 -0.0198 -0.0187 210 LEU C CG  
10163 C CD1 . LEU C 210 ? 0.5940 0.2754 0.4836 0.0001  -0.0059 -0.0147 210 LEU C CD1 
10164 C CD2 . LEU C 210 ? 0.6589 0.3074 0.5193 -0.0062 -0.0197 -0.0235 210 LEU C CD2 
10165 N N   . ASN C 211 ? 0.6492 0.3217 0.5085 -0.0163 -0.0541 -0.0205 211 ASN C N   
10166 C CA  . ASN C 211 ? 0.6560 0.3258 0.5042 -0.0157 -0.0603 -0.0196 211 ASN C CA  
10167 C C   . ASN C 211 ? 0.7136 0.3682 0.5453 -0.0207 -0.0754 -0.0238 211 ASN C C   
10168 O O   . ASN C 211 ? 0.7328 0.3696 0.5383 -0.0190 -0.0793 -0.0254 211 ASN C O   
10169 C CB  . ASN C 211 ? 0.6190 0.3143 0.4938 -0.0163 -0.0608 -0.0150 211 ASN C CB  
10170 C CG  . ASN C 211 ? 0.6082 0.3027 0.4749 -0.0144 -0.0646 -0.0128 211 ASN C CG  
10171 O OD1 . ASN C 211 ? 0.6184 0.2969 0.4618 -0.0100 -0.0596 -0.0126 211 ASN C OD1 
10172 N ND2 . ASN C 211 ? 0.6119 0.3232 0.4974 -0.0174 -0.0729 -0.0108 211 ASN C ND2 
10173 N N   . GLU C 212 ? 0.7249 0.3855 0.5712 -0.0271 -0.0841 -0.0255 212 GLU C N   
10174 C CA  . GLU C 212 ? 0.7403 0.3862 0.5733 -0.0327 -0.0990 -0.0297 212 GLU C CA  
10175 C C   . GLU C 212 ? 0.7779 0.3936 0.5769 -0.0301 -0.0967 -0.0349 212 GLU C C   
10176 O O   . GLU C 212 ? 0.7895 0.3865 0.5633 -0.0308 -0.1062 -0.0380 212 GLU C O   
10177 C CB  . GLU C 212 ? 0.7275 0.3863 0.5856 -0.0400 -0.1057 -0.0298 212 GLU C CB  
10178 C CG  . GLU C 212 ? 0.7068 0.3911 0.5932 -0.0435 -0.1125 -0.0259 212 GLU C CG  
10179 C CD  . GLU C 212 ? 0.7002 0.4024 0.6155 -0.0490 -0.1135 -0.0242 212 GLU C CD  
10180 O OE1 . GLU C 212 ? 0.7513 0.4460 0.6653 -0.0504 -0.1095 -0.0258 212 GLU C OE1 
10181 O OE2 . GLU C 212 ? 0.7188 0.4421 0.6576 -0.0512 -0.1174 -0.0210 212 GLU C OE2 
10182 N N   . LEU C 213 ? 0.7813 0.3918 0.5790 -0.0266 -0.0841 -0.0357 213 LEU C N   
10183 C CA  . LEU C 213 ? 0.8283 0.4102 0.5950 -0.0232 -0.0797 -0.0408 213 LEU C CA  
10184 C C   . LEU C 213 ? 0.8226 0.3910 0.5623 -0.0163 -0.0733 -0.0404 213 LEU C C   
10185 O O   . LEU C 213 ? 0.8742 0.4172 0.5820 -0.0153 -0.0776 -0.0450 213 LEU C O   
10186 C CB  . LEU C 213 ? 0.8701 0.4521 0.6456 -0.0204 -0.0670 -0.0408 213 LEU C CB  
10187 C CG  . LEU C 213 ? 0.8749 0.4625 0.6695 -0.0272 -0.0735 -0.0419 213 LEU C CG  
10188 C CD1 . LEU C 213 ? 0.8558 0.4452 0.6602 -0.0235 -0.0603 -0.0407 213 LEU C CD1 
10189 C CD2 . LEU C 213 ? 0.8806 0.4458 0.6566 -0.0329 -0.0871 -0.0482 213 LEU C CD2 
10190 N N   . ASN C 214 ? 0.7981 0.3830 0.5501 -0.0120 -0.0639 -0.0348 214 ASN C N   
10191 C CA  . ASN C 214 ? 0.7771 0.3512 0.5061 -0.0059 -0.0575 -0.0332 214 ASN C CA  
10192 C C   . ASN C 214 ? 0.7789 0.3421 0.4883 -0.0088 -0.0727 -0.0346 214 ASN C C   
10193 O O   . ASN C 214 ? 0.7888 0.3330 0.4680 -0.0044 -0.0698 -0.0352 214 ASN C O   
10194 C CB  . ASN C 214 ? 0.7422 0.3370 0.4918 -0.0016 -0.0451 -0.0267 214 ASN C CB  
10195 C CG  . ASN C 214 ? 0.7266 0.3244 0.4855 0.0031  -0.0289 -0.0258 214 ASN C CG  
10196 O OD1 . ASN C 214 ? 0.7272 0.3072 0.4706 0.0051  -0.0246 -0.0299 214 ASN C OD1 
10197 N ND2 . ASN C 214 ? 0.7001 0.3192 0.4838 0.0053  -0.0201 -0.0205 214 ASN C ND2 
10198 N N   . GLY C 215 ? 0.7792 0.3541 0.5054 -0.0161 -0.0888 -0.0348 215 GLY C N   
10199 C CA  . GLY C 215 ? 0.7896 0.3544 0.4993 -0.0194 -0.1054 -0.0362 215 GLY C CA  
10200 C C   . GLY C 215 ? 0.7773 0.3628 0.5061 -0.0205 -0.1118 -0.0306 215 GLY C C   
10201 O O   . GLY C 215 ? 0.8031 0.3817 0.5200 -0.0227 -0.1258 -0.0309 215 GLY C O   
10202 N N   . LEU C 216 ? 0.7354 0.3455 0.4936 -0.0189 -0.1027 -0.0257 216 LEU C N   
10203 C CA  . LEU C 216 ? 0.7400 0.3702 0.5190 -0.0200 -0.1087 -0.0209 216 LEU C CA  
10204 C C   . LEU C 216 ? 0.7500 0.3666 0.5040 -0.0170 -0.1139 -0.0190 216 LEU C C   
10205 O O   . LEU C 216 ? 0.7350 0.3581 0.4957 -0.0196 -0.1273 -0.0173 216 LEU C O   
10206 C CB  . LEU C 216 ? 0.7558 0.4003 0.5582 -0.0273 -0.1241 -0.0217 216 LEU C CB  
10207 C CG  . LEU C 216 ? 0.7605 0.4218 0.5914 -0.0310 -0.1203 -0.0222 216 LEU C CG  
10208 C CD1 . LEU C 216 ? 0.7433 0.4174 0.5953 -0.0382 -0.1360 -0.0224 216 LEU C CD1 
10209 C CD2 . LEU C 216 ? 0.7353 0.4167 0.5880 -0.0270 -0.1060 -0.0179 216 LEU C CD2 
10210 N N   . ASP C 217 ? 0.7622 0.3594 0.4874 -0.0112 -0.1030 -0.0192 217 ASP C N   
10211 C CA  . ASP C 217 ? 0.8054 0.3854 0.5011 -0.0082 -0.1072 -0.0176 217 ASP C CA  
10212 C C   . ASP C 217 ? 0.8276 0.4125 0.5237 -0.0019 -0.0920 -0.0115 217 ASP C C   
10213 O O   . ASP C 217 ? 0.8509 0.4234 0.5247 0.0011  -0.0936 -0.0087 217 ASP C O   
10214 C CB  . ASP C 217 ? 0.8371 0.3860 0.4930 -0.0075 -0.1103 -0.0233 217 ASP C CB  
10215 C CG  . ASP C 217 ? 0.8582 0.3942 0.5005 -0.0031 -0.0933 -0.0263 217 ASP C CG  
10216 O OD1 . ASP C 217 ? 0.8269 0.3796 0.4948 -0.0022 -0.0816 -0.0248 217 ASP C OD1 
10217 O OD2 . ASP C 217 ? 0.9442 0.4528 0.5496 -0.0004 -0.0922 -0.0302 217 ASP C OD2 
10218 N N   . LYS C 218 ? 0.8109 0.4136 0.5325 -0.0001 -0.0781 -0.0093 218 LYS C N   
10219 C CA  . LYS C 218 ? 0.8067 0.4151 0.5322 0.0053  -0.0635 -0.0035 218 LYS C CA  
10220 C C   . LYS C 218 ? 0.7460 0.3831 0.5114 0.0040  -0.0595 -0.0004 218 LYS C C   
10221 O O   . LYS C 218 ? 0.7181 0.3682 0.5048 0.0003  -0.0624 -0.0031 218 LYS C O   
10222 C CB  . LYS C 218 ? 0.8459 0.4411 0.5551 0.0106  -0.0457 -0.0041 218 LYS C CB  
10223 C CG  . LYS C 218 ? 0.9177 0.4827 0.5849 0.0133  -0.0458 -0.0074 218 LYS C CG  
10224 C CD  . LYS C 218 ? 0.9879 0.5394 0.6397 0.0191  -0.0274 -0.0086 218 LYS C CD  
10225 C CE  . LYS C 218 ? 1.0275 0.5471 0.6331 0.0224  -0.0276 -0.0115 218 LYS C CE  
10226 N NZ  . LYS C 218 ? 1.0221 0.5264 0.6123 0.0269  -0.0137 -0.0154 218 LYS C NZ  
10227 N N   . PRO C 219 ? 0.7454 0.3923 0.5214 0.0070  -0.0521 0.0053  219 PRO C N   
10228 C CA  . PRO C 219 ? 0.6922 0.3642 0.5036 0.0061  -0.0475 0.0076  219 PRO C CA  
10229 C C   . PRO C 219 ? 0.6454 0.3218 0.4666 0.0069  -0.0361 0.0055  219 PRO C C   
10230 O O   . PRO C 219 ? 0.6293 0.2911 0.4321 0.0106  -0.0256 0.0051  219 PRO C O   
10231 C CB  . PRO C 219 ? 0.6913 0.3664 0.5050 0.0098  -0.0401 0.0139  219 PRO C CB  
10232 C CG  . PRO C 219 ? 0.7306 0.3851 0.5127 0.0114  -0.0463 0.0153  219 PRO C CG  
10233 C CD  . PRO C 219 ? 0.7682 0.4022 0.5226 0.0111  -0.0482 0.0100  219 PRO C CD  
10234 N N   . PHE C 220 ? 0.6152 0.3118 0.4655 0.0038  -0.0381 0.0046  220 PHE C N   
10235 C CA  . PHE C 220 ? 0.6241 0.3282 0.4882 0.0045  -0.0283 0.0036  220 PHE C CA  
10236 C C   . PHE C 220 ? 0.5756 0.3006 0.4673 0.0055  -0.0217 0.0074  220 PHE C C   
10237 O O   . PHE C 220 ? 0.5549 0.2945 0.4641 0.0031  -0.0289 0.0084  220 PHE C O   
10238 C CB  . PHE C 220 ? 0.5964 0.3040 0.4682 -0.0003 -0.0365 -0.0009 220 PHE C CB  
10239 C CG  . PHE C 220 ? 0.5834 0.3037 0.4756 -0.0004 -0.0287 -0.0011 220 PHE C CG  
10240 C CD1 . PHE C 220 ? 0.5772 0.2904 0.4636 0.0039  -0.0158 -0.0006 220 PHE C CD1 
10241 C CD2 . PHE C 220 ? 0.5721 0.3117 0.4897 -0.0043 -0.0340 -0.0012 220 PHE C CD2 
10242 C CE1 . PHE C 220 ? 0.5575 0.2823 0.4628 0.0040  -0.0098 -0.0003 220 PHE C CE1 
10243 C CE2 . PHE C 220 ? 0.5392 0.2898 0.4738 -0.0042 -0.0273 -0.0009 220 PHE C CE2 
10244 C CZ  . PHE C 220 ? 0.5476 0.2908 0.4762 -0.0001 -0.0157 -0.0004 220 PHE C CZ  
10245 N N   . ILE C 221 ? 0.5786 0.3044 0.4742 0.0090  -0.0083 0.0093  221 ILE C N   
10246 C CA  . ILE C 221 ? 0.5625 0.3063 0.4833 0.0100  -0.0016 0.0127  221 ILE C CA  
10247 C C   . ILE C 221 ? 0.5461 0.2956 0.4785 0.0108  0.0061  0.0117  221 ILE C C   
10248 O O   . ILE C 221 ? 0.5437 0.2801 0.4616 0.0122  0.0097  0.0094  221 ILE C O   
10249 C CB  . ILE C 221 ? 0.5499 0.2898 0.4662 0.0138  0.0073  0.0177  221 ILE C CB  
10250 C CG1 . ILE C 221 ? 0.5766 0.3028 0.4777 0.0183  0.0206  0.0188  221 ILE C CG1 
10251 C CG2 . ILE C 221 ? 0.5502 0.2823 0.4524 0.0134  -0.0003 0.0192  221 ILE C CG2 
10252 C CD1 . ILE C 221 ? 0.5982 0.3204 0.4953 0.0219  0.0310  0.0244  221 ILE C CD1 
10253 N N   . THR C 222 ? 0.5245 0.2927 0.4825 0.0100  0.0078  0.0133  222 THR C N   
10254 C CA  . THR C 222 ? 0.5325 0.3077 0.5037 0.0113  0.0152  0.0136  222 THR C CA  
10255 C C   . THR C 222 ? 0.5376 0.3163 0.5171 0.0151  0.0263  0.0181  222 THR C C   
10256 O O   . THR C 222 ? 0.5173 0.3034 0.5058 0.0148  0.0257  0.0207  222 THR C O   
10257 C CB  . THR C 222 ? 0.5118 0.3046 0.5045 0.0078  0.0091  0.0123  222 THR C CB  
10258 O OG1 . THR C 222 ? 0.4779 0.2831 0.4844 0.0068  0.0060  0.0141  222 THR C OG1 
10259 C CG2 . THR C 222 ? 0.5194 0.3087 0.5057 0.0040  -0.0003 0.0085  222 THR C CG2 
10260 N N   . THR C 223 ? 0.5202 0.2932 0.4971 0.0186  0.0362  0.0189  223 THR C N   
10261 C CA  . THR C 223 ? 0.5221 0.2976 0.5072 0.0223  0.0477  0.0236  223 THR C CA  
10262 C C   . THR C 223 ? 0.4664 0.2591 0.4782 0.0221  0.0498  0.0251  223 THR C C   
10263 O O   . THR C 223 ? 0.4555 0.2534 0.4794 0.0245  0.0581  0.0292  223 THR C O   
10264 C CB  . THR C 223 ? 0.5555 0.3133 0.5208 0.0272  0.0589  0.0245  223 THR C CB  
10265 O OG1 . THR C 223 ? 0.5545 0.3020 0.5079 0.0281  0.0586  0.0204  223 THR C OG1 
10266 C CG2 . THR C 223 ? 0.5751 0.3174 0.5157 0.0280  0.0586  0.0250  223 THR C CG2 
10267 N N   . ALA C 224 ? 0.4343 0.2355 0.4548 0.0190  0.0419  0.0221  224 ALA C N   
10268 C CA  . ALA C 224 ? 0.4057 0.2227 0.4492 0.0184  0.0416  0.0232  224 ALA C CA  
10269 C C   . ALA C 224 ? 0.4093 0.2319 0.4558 0.0147  0.0325  0.0197  224 ALA C C   
10270 O O   . ALA C 224 ? 0.3999 0.2128 0.4321 0.0134  0.0286  0.0167  224 ALA C O   
10271 C CB  . ALA C 224 ? 0.4195 0.2351 0.4689 0.0226  0.0516  0.0257  224 ALA C CB  
10272 N N   . PHE C 225 ? 0.4149 0.2532 0.4807 0.0131  0.0292  0.0204  225 PHE C N   
10273 C CA  . PHE C 225 ? 0.3831 0.2293 0.4552 0.0100  0.0223  0.0183  225 PHE C CA  
10274 C C   . PHE C 225 ? 0.3597 0.2218 0.4518 0.0095  0.0209  0.0199  225 PHE C C   
10275 O O   . PHE C 225 ? 0.3258 0.1928 0.4254 0.0098  0.0219  0.0213  225 PHE C O   
10276 C CB  . PHE C 225 ? 0.3865 0.2312 0.4502 0.0062  0.0137  0.0150  225 PHE C CB  
10277 C CG  . PHE C 225 ? 0.3950 0.2459 0.4626 0.0047  0.0092  0.0147  225 PHE C CG  
10278 C CD1 . PHE C 225 ? 0.4303 0.2720 0.4865 0.0057  0.0100  0.0152  225 PHE C CD1 
10279 C CD2 . PHE C 225 ? 0.3933 0.2584 0.4753 0.0026  0.0044  0.0140  225 PHE C CD2 
10280 C CE1 . PHE C 225 ? 0.4261 0.2727 0.4864 0.0046  0.0058  0.0154  225 PHE C CE1 
10281 C CE2 . PHE C 225 ? 0.4151 0.2849 0.5010 0.0018  0.0007  0.0136  225 PHE C CE2 
10282 C CZ  . PHE C 225 ? 0.4286 0.2893 0.5042 0.0027  0.0011  0.0144  225 PHE C CZ  
10283 N N   . GLY C 226 ? 0.3456 0.2146 0.4452 0.0085  0.0182  0.0196  226 GLY C N   
10284 C CA  . GLY C 226 ? 0.3515 0.2346 0.4674 0.0076  0.0152  0.0204  226 GLY C CA  
10285 C C   . GLY C 226 ? 0.3726 0.2598 0.4958 0.0086  0.0158  0.0222  226 GLY C C   
10286 O O   . GLY C 226 ? 0.3636 0.2430 0.4789 0.0093  0.0174  0.0221  226 GLY C O   
10287 N N   . TYR C 227 ? 0.3401 0.2387 0.4780 0.0087  0.0139  0.0236  227 TYR C N   
10288 C CA  . TYR C 227 ? 0.3214 0.2259 0.4668 0.0091  0.0118  0.0253  227 TYR C CA  
10289 C C   . TYR C 227 ? 0.3210 0.2337 0.4828 0.0110  0.0127  0.0282  227 TYR C C   
10290 O O   . TYR C 227 ? 0.3446 0.2619 0.5137 0.0104  0.0121  0.0281  227 TYR C O   
10291 C CB  . TYR C 227 ? 0.3337 0.2450 0.4778 0.0058  0.0048  0.0231  227 TYR C CB  
10292 C CG  . TYR C 227 ? 0.3257 0.2302 0.4568 0.0036  0.0037  0.0210  227 TYR C CG  
10293 C CD1 . TYR C 227 ? 0.3222 0.2206 0.4478 0.0038  0.0049  0.0222  227 TYR C CD1 
10294 C CD2 . TYR C 227 ? 0.3183 0.2220 0.4437 0.0014  0.0015  0.0180  227 TYR C CD2 
10295 C CE1 . TYR C 227 ? 0.3253 0.2167 0.4403 0.0013  0.0036  0.0204  227 TYR C CE1 
10296 C CE2 . TYR C 227 ? 0.3547 0.2525 0.4701 -0.0009 -0.0002 0.0164  227 TYR C CE2 
10297 C CZ  . TYR C 227 ? 0.3424 0.2341 0.4528 -0.0012 0.0008  0.0175  227 TYR C CZ  
10298 O OH  . TYR C 227 ? 0.3605 0.2462 0.4624 -0.0041 -0.0014 0.0159  227 TYR C OH  
10299 N N   . SER C 228 ? 0.3225 0.2369 0.4908 0.0131  0.0134  0.0311  228 SER C N   
10300 C CA  . SER C 228 ? 0.3360 0.2586 0.5216 0.0150  0.0133  0.0345  228 SER C CA  
10301 C C   . SER C 228 ? 0.3332 0.2650 0.5240 0.0131  0.0048  0.0343  228 SER C C   
10302 O O   . SER C 228 ? 0.3116 0.2415 0.4937 0.0123  0.0021  0.0337  228 SER C O   
10303 C CB  . SER C 228 ? 0.3515 0.2697 0.5420 0.0194  0.0199  0.0384  228 SER C CB  
10304 O OG  . SER C 228 ? 0.3416 0.2692 0.5498 0.0210  0.0174  0.0421  228 SER C OG  
10305 N N   . VAL C 229 ? 0.3111 0.2519 0.5162 0.0126  0.0011  0.0352  229 VAL C N   
10306 C CA  . VAL C 229 ? 0.3201 0.2691 0.5302 0.0110  -0.0076 0.0349  229 VAL C CA  
10307 C C   . VAL C 229 ? 0.3107 0.2653 0.5363 0.0135  -0.0094 0.0396  229 VAL C C   
10308 O O   . VAL C 229 ? 0.2867 0.2487 0.5200 0.0122  -0.0173 0.0396  229 VAL C O   
10309 C CB  . VAL C 229 ? 0.3318 0.2857 0.5441 0.0080  -0.0127 0.0312  229 VAL C CB  
10310 C CG1 . VAL C 229 ? 0.3602 0.3095 0.5569 0.0060  -0.0122 0.0269  229 VAL C CG1 
10311 C CG2 . VAL C 229 ? 0.3344 0.2904 0.5606 0.0082  -0.0099 0.0325  229 VAL C CG2 
10312 N N   . SER C 230 ? 0.3108 0.2609 0.5395 0.0172  -0.0027 0.0433  230 SER C N   
10313 C CA  . SER C 230 ? 0.3022 0.2574 0.5469 0.0203  -0.0037 0.0483  230 SER C CA  
10314 C C   . SER C 230 ? 0.3007 0.2597 0.5421 0.0193  -0.0131 0.0488  230 SER C C   
10315 O O   . SER C 230 ? 0.2885 0.2428 0.5131 0.0176  -0.0146 0.0463  230 SER C O   
10316 C CB  . SER C 230 ? 0.3049 0.2528 0.5503 0.0250  0.0057  0.0516  230 SER C CB  
10317 O OG  . SER C 230 ? 0.3163 0.2554 0.5449 0.0253  0.0064  0.0505  230 SER C OG  
10318 N N   . PRO C 231 ? 0.2910 0.2587 0.5476 0.0198  -0.0202 0.0517  231 PRO C N   
10319 C CA  . PRO C 231 ? 0.3093 0.2797 0.5618 0.0194  -0.0295 0.0529  231 PRO C CA  
10320 C C   . PRO C 231 ? 0.3481 0.3115 0.5902 0.0218  -0.0270 0.0556  231 PRO C C   
10321 O O   . PRO C 231 ? 0.3083 0.2705 0.5379 0.0203  -0.0326 0.0552  231 PRO C O   
10322 C CB  . PRO C 231 ? 0.3109 0.2907 0.5859 0.0208  -0.0354 0.0570  231 PRO C CB  
10323 C CG  . PRO C 231 ? 0.3024 0.2861 0.5889 0.0188  -0.0329 0.0550  231 PRO C CG  
10324 C CD  . PRO C 231 ? 0.3057 0.2811 0.5843 0.0203  -0.0203 0.0541  231 PRO C CD  
10325 N N   . GLU C 232 ? 0.3745 0.3329 0.6221 0.0257  -0.0183 0.0585  232 GLU C N   
10326 C CA  . GLU C 232 ? 0.4289 0.3789 0.6682 0.0285  -0.0151 0.0611  232 GLU C CA  
10327 C C   . GLU C 232 ? 0.4139 0.3557 0.6541 0.0318  -0.0035 0.0613  232 GLU C C   
10328 O O   . GLU C 232 ? 0.3642 0.3071 0.6095 0.0317  0.0018  0.0595  232 GLU C O   
10329 C CB  . GLU C 232 ? 0.4667 0.4209 0.7167 0.0316  -0.0213 0.0670  232 GLU C CB  
10330 C CG  . GLU C 232 ? 0.4983 0.4604 0.7734 0.0354  -0.0205 0.0712  232 GLU C CG  
10331 C CD  . GLU C 232 ? 0.5589 0.5270 0.8479 0.0385  -0.0283 0.0774  232 GLU C CD  
10332 O OE1 . GLU C 232 ? 0.5654 0.5290 0.8443 0.0393  -0.0325 0.0797  232 GLU C OE1 
10333 O OE2 . GLU C 232 ? 0.6395 0.6172 0.9513 0.0401  -0.0304 0.0803  232 GLU C OE2 
10334 N N   . GLY C 233 ? 0.4083 0.3411 0.6425 0.0349  0.0000  0.0636  233 GLY C N   
10335 C CA  . GLY C 233 ? 0.3986 0.3212 0.6311 0.0388  0.0108  0.0636  233 GLY C CA  
10336 C C   . GLY C 233 ? 0.4039 0.3156 0.6153 0.0356  0.0146  0.0583  233 GLY C C   
10337 O O   . GLY C 233 ? 0.4137 0.3280 0.6156 0.0305  0.0097  0.0548  233 GLY C O   
10338 N N   . GLY C 234 ? 0.3998 0.2995 0.6054 0.0390  0.0236  0.0577  234 GLY C N   
10339 C CA  . GLY C 234 ? 0.3946 0.2815 0.5806 0.0367  0.0274  0.0531  234 GLY C CA  
10340 C C   . GLY C 234 ? 0.4037 0.2828 0.5783 0.0350  0.0237  0.0534  234 GLY C C   
10341 O O   . GLY C 234 ? 0.3980 0.2763 0.5790 0.0382  0.0227  0.0576  234 GLY C O   
10342 N N   . ASN C 235 ? 0.4567 0.3302 0.6158 0.0301  0.0218  0.0493  235 ASN C N   
10343 C CA  . ASN C 235 ? 0.4968 0.3668 0.6472 0.0267  0.0168  0.0500  235 ASN C CA  
10344 C C   . ASN C 235 ? 0.4527 0.3216 0.5904 0.0205  0.0142  0.0453  235 ASN C C   
10345 O O   . ASN C 235 ? 0.4374 0.3028 0.5695 0.0196  0.0171  0.0414  235 ASN C O   
10346 C CB  . ASN C 235 ? 0.6019 0.4575 0.7471 0.0296  0.0205  0.0516  235 ASN C CB  
10347 C CG  . ASN C 235 ? 0.7106 0.5519 0.8407 0.0279  0.0245  0.0467  235 ASN C CG  
10348 O OD1 . ASN C 235 ? 0.7242 0.5612 0.8522 0.0303  0.0302  0.0440  235 ASN C OD1 
10349 N ND2 . ASN C 235 ? 0.8126 0.6469 0.9321 0.0234  0.0212  0.0457  235 ASN C ND2 
10350 N N   . GLY C 236 ? 0.4254 0.2977 0.5591 0.0164  0.0088  0.0462  236 GLY C N   
10351 C CA  . GLY C 236 ? 0.4260 0.3006 0.5515 0.0107  0.0060  0.0426  236 GLY C CA  
10352 C C   . GLY C 236 ? 0.4480 0.3331 0.5784 0.0101  0.0049  0.0398  236 GLY C C   
10353 O O   . GLY C 236 ? 0.4233 0.3182 0.5637 0.0120  0.0029  0.0416  236 GLY C O   
10354 N N   . GLN C 237 ? 0.4216 0.3032 0.5451 0.0078  0.0061  0.0356  237 GLN C N   
10355 C CA  . GLN C 237 ? 0.4078 0.2977 0.5343 0.0066  0.0048  0.0328  237 GLN C CA  
10356 C C   . GLN C 237 ? 0.4112 0.2997 0.5433 0.0107  0.0094  0.0329  237 GLN C C   
10357 O O   . GLN C 237 ? 0.4008 0.2947 0.5359 0.0101  0.0090  0.0310  237 GLN C O   
10358 C CB  . GLN C 237 ? 0.4052 0.2917 0.5223 0.0025  0.0035  0.0288  237 GLN C CB  
10359 C CG  . GLN C 237 ? 0.3882 0.2810 0.5034 -0.0019 -0.0009 0.0285  237 GLN C CG  
10360 C CD  . GLN C 237 ? 0.4022 0.2935 0.5118 -0.0055 -0.0024 0.0248  237 GLN C CD  
10361 O OE1 . GLN C 237 ? 0.3827 0.2794 0.4942 -0.0057 -0.0034 0.0222  237 GLN C OE1 
10362 N NE2 . GLN C 237 ? 0.4021 0.2850 0.5050 -0.0082 -0.0027 0.0246  237 GLN C NE2 
10363 N N   . TYR C 238 ? 0.4160 0.2963 0.5490 0.0148  0.0145  0.0350  238 TYR C N   
10364 C CA  . TYR C 238 ? 0.3949 0.2740 0.5343 0.0191  0.0205  0.0359  238 TYR C CA  
10365 C C   . TYR C 238 ? 0.4076 0.2976 0.5642 0.0220  0.0194  0.0401  238 TYR C C   
10366 O O   . TYR C 238 ? 0.4293 0.3188 0.5907 0.0243  0.0187  0.0435  238 TYR C O   
10367 C CB  . TYR C 238 ? 0.3863 0.2503 0.5178 0.0229  0.0278  0.0358  238 TYR C CB  
10368 C CG  . TYR C 238 ? 0.3961 0.2595 0.5354 0.0281  0.0356  0.0375  238 TYR C CG  
10369 C CD1 . TYR C 238 ? 0.3994 0.2622 0.5355 0.0278  0.0389  0.0356  238 TYR C CD1 
10370 C CD2 . TYR C 238 ? 0.4010 0.2649 0.5519 0.0334  0.0400  0.0416  238 TYR C CD2 
10371 C CE1 . TYR C 238 ? 0.4200 0.2823 0.5634 0.0323  0.0471  0.0379  238 TYR C CE1 
10372 C CE2 . TYR C 238 ? 0.3949 0.2594 0.5551 0.0382  0.0481  0.0437  238 TYR C CE2 
10373 C CZ  . TYR C 238 ? 0.4065 0.2700 0.5626 0.0376  0.0521  0.0419  238 TYR C CZ  
10374 O OH  . TYR C 238 ? 0.3751 0.2388 0.5396 0.0421  0.0612  0.0444  238 TYR C OH  
10375 N N   . GLY C 239 ? 0.3894 0.2887 0.5556 0.0217  0.0186  0.0399  239 GLY C N   
10376 C CA  . GLY C 239 ? 0.4029 0.3146 0.5851 0.0222  0.0141  0.0429  239 GLY C CA  
10377 C C   . GLY C 239 ? 0.3921 0.3104 0.5708 0.0184  0.0054  0.0419  239 GLY C C   
10378 O O   . GLY C 239 ? 0.3844 0.2979 0.5500 0.0156  0.0041  0.0396  239 GLY C O   
10379 N N   . SER C 240 ? 0.3623 0.2914 0.5529 0.0182  -0.0002 0.0434  240 SER C N   
10380 C CA  . SER C 240 ? 0.3445 0.2794 0.5328 0.0161  -0.0082 0.0438  240 SER C CA  
10381 C C   . SER C 240 ? 0.3154 0.2521 0.4924 0.0117  -0.0117 0.0392  240 SER C C   
10382 O O   . SER C 240 ? 0.3147 0.2543 0.4859 0.0100  -0.0167 0.0392  240 SER C O   
10383 C CB  . SER C 240 ? 0.3410 0.2708 0.5258 0.0181  -0.0082 0.0476  240 SER C CB  
10384 O OG  . SER C 240 ? 0.3459 0.2772 0.5453 0.0226  -0.0064 0.0521  240 SER C OG  
10385 N N   . ASN C 241 ? 0.3151 0.2511 0.4898 0.0101  -0.0093 0.0354  241 ASN C N   
10386 C CA  . ASN C 241 ? 0.3272 0.2660 0.4939 0.0066  -0.0126 0.0311  241 ASN C CA  
10387 C C   . ASN C 241 ? 0.3116 0.2592 0.4850 0.0057  -0.0187 0.0296  241 ASN C C   
10388 O O   . ASN C 241 ? 0.3318 0.2831 0.5174 0.0071  -0.0199 0.0313  241 ASN C O   
10389 C CB  . ASN C 241 ? 0.3495 0.2839 0.5112 0.0054  -0.0088 0.0279  241 ASN C CB  
10390 C CG  . ASN C 241 ? 0.3662 0.2906 0.5182 0.0055  -0.0043 0.0283  241 ASN C CG  
10391 O OD1 . ASN C 241 ? 0.4512 0.3738 0.5945 0.0031  -0.0056 0.0270  241 ASN C OD1 
10392 N ND2 . ASN C 241 ? 0.3993 0.3168 0.5527 0.0083  0.0011  0.0301  241 ASN C ND2 
10393 N N   . THR C 242 ? 0.3373 0.2880 0.5029 0.0034  -0.0226 0.0265  242 THR C N   
10394 C CA  . THR C 242 ? 0.3305 0.2874 0.4998 0.0024  -0.0281 0.0235  242 THR C CA  
10395 C C   . THR C 242 ? 0.3197 0.2761 0.4925 0.0016  -0.0259 0.0202  242 THR C C   
10396 O O   . THR C 242 ? 0.3222 0.2737 0.4912 0.0015  -0.0208 0.0198  242 THR C O   
10397 C CB  . THR C 242 ? 0.3415 0.3007 0.4996 0.0008  -0.0316 0.0210  242 THR C CB  
10398 O OG1 . THR C 242 ? 0.3500 0.3065 0.4999 -0.0007 -0.0274 0.0188  242 THR C OG1 
10399 C CG2 . THR C 242 ? 0.3803 0.3396 0.5332 0.0014  -0.0343 0.0246  242 THR C CG2 
10400 N N   . LEU C 243 ? 0.3256 0.2861 0.5038 0.0008  -0.0303 0.0174  243 LEU C N   
10401 C CA  . LEU C 243 ? 0.3420 0.3015 0.5225 0.0000  -0.0289 0.0142  243 LEU C CA  
10402 C C   . LEU C 243 ? 0.3371 0.2946 0.5063 -0.0011 -0.0270 0.0108  243 LEU C C   
10403 O O   . LEU C 243 ? 0.3258 0.2798 0.4942 -0.0012 -0.0235 0.0099  243 LEU C O   
10404 C CB  . LEU C 243 ? 0.3563 0.3200 0.5444 -0.0009 -0.0351 0.0117  243 LEU C CB  
10405 C CG  . LEU C 243 ? 0.3510 0.3177 0.5545 -0.0004 -0.0375 0.0152  243 LEU C CG  
10406 C CD1 . LEU C 243 ? 0.3688 0.3387 0.5779 -0.0021 -0.0450 0.0117  243 LEU C CD1 
10407 C CD2 . LEU C 243 ? 0.3413 0.3059 0.5550 0.0005  -0.0310 0.0186  243 LEU C CD2 
10408 N N   . LYS C 244 ? 0.3624 0.3220 0.5228 -0.0017 -0.0291 0.0092  244 LYS C N   
10409 C CA  . LYS C 244 ? 0.3420 0.3011 0.4940 -0.0026 -0.0269 0.0068  244 LYS C CA  
10410 C C   . LYS C 244 ? 0.3277 0.2820 0.4763 -0.0030 -0.0222 0.0093  244 LYS C C   
10411 O O   . LYS C 244 ? 0.3110 0.2632 0.4577 -0.0037 -0.0203 0.0077  244 LYS C O   
10412 C CB  . LYS C 244 ? 0.3768 0.3393 0.5207 -0.0030 -0.0290 0.0056  244 LYS C CB  
10413 C CG  . LYS C 244 ? 0.4003 0.3641 0.5388 -0.0038 -0.0265 0.0025  244 LYS C CG  
10414 C CD  . LYS C 244 ? 0.4591 0.4260 0.5889 -0.0043 -0.0258 0.0022  244 LYS C CD  
10415 C CE  . LYS C 244 ? 0.4638 0.4328 0.5920 -0.0051 -0.0222 0.0003  244 LYS C CE  
10416 N NZ  . LYS C 244 ? 0.4606 0.4294 0.5947 -0.0045 -0.0224 -0.0031 244 LYS C NZ  
10417 N N   . GLN C 245 ? 0.3223 0.2741 0.4697 -0.0026 -0.0209 0.0133  245 GLN C N   
10418 C CA  . GLN C 245 ? 0.3177 0.2632 0.4610 -0.0030 -0.0169 0.0153  245 GLN C CA  
10419 C C   . GLN C 245 ? 0.3292 0.2696 0.4752 -0.0021 -0.0140 0.0151  245 GLN C C   
10420 O O   . GLN C 245 ? 0.3017 0.2370 0.4424 -0.0030 -0.0120 0.0143  245 GLN C O   
10421 C CB  . GLN C 245 ? 0.3200 0.2625 0.4623 -0.0020 -0.0159 0.0196  245 GLN C CB  
10422 C CG  . GLN C 245 ? 0.3199 0.2655 0.4567 -0.0032 -0.0180 0.0207  245 GLN C CG  
10423 C CD  . GLN C 245 ? 0.3307 0.2742 0.4682 -0.0017 -0.0185 0.0254  245 GLN C CD  
10424 O OE1 . GLN C 245 ? 0.3256 0.2691 0.4705 0.0007  -0.0193 0.0275  245 GLN C OE1 
10425 N NE2 . GLN C 245 ? 0.3360 0.2774 0.4665 -0.0030 -0.0178 0.0277  245 GLN C NE2 
10426 N N   . GLN C 246 ? 0.3437 0.2853 0.4982 -0.0004 -0.0140 0.0160  246 GLN C N   
10427 C CA  . GLN C 246 ? 0.3366 0.2734 0.4933 0.0005  -0.0104 0.0163  246 GLN C CA  
10428 C C   . GLN C 246 ? 0.3169 0.2534 0.4698 -0.0009 -0.0117 0.0128  246 GLN C C   
10429 O O   . GLN C 246 ? 0.3304 0.2605 0.4772 -0.0010 -0.0093 0.0126  246 GLN C O   
10430 C CB  . GLN C 246 ? 0.3184 0.2580 0.4871 0.0020  -0.0101 0.0183  246 GLN C CB  
10431 C CG  . GLN C 246 ? 0.3228 0.2569 0.4933 0.0032  -0.0050 0.0195  246 GLN C CG  
10432 C CD  . GLN C 246 ? 0.3344 0.2725 0.5192 0.0040  -0.0046 0.0216  246 GLN C CD  
10433 O OE1 . GLN C 246 ? 0.3120 0.2564 0.5043 0.0026  -0.0098 0.0200  246 GLN C OE1 
10434 N NE2 . GLN C 246 ? 0.3389 0.2730 0.5277 0.0062  0.0018  0.0252  246 GLN C NE2 
10435 N N   . SER C 247 ? 0.3275 0.2702 0.4838 -0.0016 -0.0156 0.0100  247 SER C N   
10436 C CA  . SER C 247 ? 0.3163 0.2592 0.4716 -0.0023 -0.0169 0.0068  247 SER C CA  
10437 C C   . SER C 247 ? 0.3041 0.2454 0.4514 -0.0035 -0.0165 0.0058  247 SER C C   
10438 O O   . SER C 247 ? 0.3129 0.2494 0.4570 -0.0036 -0.0157 0.0055  247 SER C O   
10439 C CB  . SER C 247 ? 0.3047 0.2537 0.4643 -0.0024 -0.0210 0.0034  247 SER C CB  
10440 O OG  . SER C 247 ? 0.3083 0.2569 0.4674 -0.0025 -0.0218 0.0005  247 SER C OG  
10441 N N   . ASP C 248 ? 0.2858 0.2306 0.4299 -0.0045 -0.0173 0.0057  248 ASP C N   
10442 C CA  . ASP C 248 ? 0.3020 0.2464 0.4410 -0.0062 -0.0171 0.0051  248 ASP C CA  
10443 C C   . ASP C 248 ? 0.3101 0.2457 0.4438 -0.0067 -0.0151 0.0072  248 ASP C C   
10444 O O   . ASP C 248 ? 0.2914 0.2243 0.4219 -0.0080 -0.0159 0.0063  248 ASP C O   
10445 C CB  . ASP C 248 ? 0.2948 0.2441 0.4316 -0.0074 -0.0173 0.0056  248 ASP C CB  
10446 C CG  . ASP C 248 ? 0.2749 0.2315 0.4133 -0.0067 -0.0190 0.0030  248 ASP C CG  
10447 O OD1 . ASP C 248 ? 0.2805 0.2390 0.4225 -0.0057 -0.0204 -0.0001 248 ASP C OD1 
10448 O OD2 . ASP C 248 ? 0.2752 0.2348 0.4103 -0.0072 -0.0188 0.0041  248 ASP C OD2 
10449 N N   . GLY C 249 ? 0.3247 0.2556 0.4578 -0.0055 -0.0126 0.0099  249 GLY C N   
10450 C CA  . GLY C 249 ? 0.3260 0.2468 0.4524 -0.0053 -0.0100 0.0115  249 GLY C CA  
10451 C C   . GLY C 249 ? 0.3228 0.2371 0.4454 -0.0047 -0.0093 0.0106  249 GLY C C   
10452 O O   . GLY C 249 ? 0.3063 0.2127 0.4205 -0.0057 -0.0095 0.0102  249 GLY C O   
10453 N N   . LEU C 250 ? 0.3092 0.2258 0.4373 -0.0031 -0.0088 0.0105  250 LEU C N   
10454 C CA  . LEU C 250 ? 0.3106 0.2204 0.4346 -0.0022 -0.0076 0.0105  250 LEU C CA  
10455 C C   . LEU C 250 ? 0.3387 0.2491 0.4593 -0.0040 -0.0120 0.0081  250 LEU C C   
10456 O O   . LEU C 250 ? 0.3828 0.2848 0.4948 -0.0040 -0.0123 0.0083  250 LEU C O   
10457 C CB  . LEU C 250 ? 0.3050 0.2177 0.4375 -0.0006 -0.0061 0.0115  250 LEU C CB  
10458 C CG  . LEU C 250 ? 0.3046 0.2128 0.4392 0.0016  -0.0003 0.0148  250 LEU C CG  
10459 C CD1 . LEU C 250 ? 0.3091 0.2052 0.4321 0.0029  0.0037  0.0160  250 LEU C CD1 
10460 C CD2 . LEU C 250 ? 0.3219 0.2321 0.4594 0.0023  0.0011  0.0163  250 LEU C CD2 
10461 N N   . ILE C 251 ? 0.3329 0.2526 0.4597 -0.0051 -0.0153 0.0061  251 ILE C N   
10462 C CA  . ILE C 251 ? 0.3668 0.2889 0.4936 -0.0063 -0.0191 0.0041  251 ILE C CA  
10463 C C   . ILE C 251 ? 0.3515 0.2702 0.4722 -0.0087 -0.0206 0.0043  251 ILE C C   
10464 O O   . ILE C 251 ? 0.3417 0.2566 0.4587 -0.0097 -0.0238 0.0037  251 ILE C O   
10465 C CB  . ILE C 251 ? 0.3975 0.3306 0.5330 -0.0062 -0.0210 0.0017  251 ILE C CB  
10466 C CG1 . ILE C 251 ? 0.4146 0.3496 0.5559 -0.0043 -0.0206 0.0010  251 ILE C CG1 
10467 C CG2 . ILE C 251 ? 0.3838 0.3205 0.5215 -0.0069 -0.0244 -0.0001 251 ILE C CG2 
10468 C CD1 . ILE C 251 ? 0.4360 0.3648 0.5766 -0.0030 -0.0207 0.0017  251 ILE C CD1 
10469 N N   . SER C 252 ? 0.3488 0.2686 0.4689 -0.0098 -0.0190 0.0053  252 SER C N   
10470 C CA  . SER C 252 ? 0.3319 0.2473 0.4469 -0.0126 -0.0201 0.0058  252 SER C CA  
10471 C C   . SER C 252 ? 0.3485 0.2504 0.4525 -0.0123 -0.0201 0.0061  252 SER C C   
10472 O O   . SER C 252 ? 0.3442 0.2417 0.4437 -0.0144 -0.0241 0.0053  252 SER C O   
10473 C CB  . SER C 252 ? 0.3241 0.2412 0.4398 -0.0133 -0.0177 0.0075  252 SER C CB  
10474 O OG  . SER C 252 ? 0.3203 0.2311 0.4308 -0.0161 -0.0187 0.0082  252 SER C OG  
10475 N N   . ASN C 253 ? 0.3386 0.2341 0.4387 -0.0094 -0.0158 0.0074  253 ASN C N   
10476 C CA  . ASN C 253 ? 0.3432 0.2249 0.4311 -0.0083 -0.0144 0.0076  253 ASN C CA  
10477 C C   . ASN C 253 ? 0.3435 0.2219 0.4268 -0.0083 -0.0180 0.0067  253 ASN C C   
10478 O O   . ASN C 253 ? 0.3747 0.2423 0.4463 -0.0092 -0.0205 0.0060  253 ASN C O   
10479 C CB  . ASN C 253 ? 0.3632 0.2402 0.4498 -0.0047 -0.0078 0.0096  253 ASN C CB  
10480 C CG  . ASN C 253 ? 0.3547 0.2322 0.4442 -0.0041 -0.0045 0.0110  253 ASN C CG  
10481 O OD1 . ASN C 253 ? 0.3703 0.2501 0.4607 -0.0065 -0.0069 0.0107  253 ASN C OD1 
10482 N ND2 . ASN C 253 ? 0.3372 0.2129 0.4292 -0.0007 0.0012  0.0131  253 ASN C ND2 
10483 N N   . TYR C 254 ? 0.3377 0.2238 0.4292 -0.0072 -0.0187 0.0066  254 TYR C N   
10484 C CA  . TYR C 254 ? 0.3414 0.2232 0.4285 -0.0065 -0.0216 0.0066  254 TYR C CA  
10485 C C   . TYR C 254 ? 0.3419 0.2238 0.4270 -0.0092 -0.0288 0.0050  254 TYR C C   
10486 O O   . TYR C 254 ? 0.3598 0.2318 0.4339 -0.0095 -0.0321 0.0050  254 TYR C O   
10487 C CB  . TYR C 254 ? 0.3218 0.2117 0.4195 -0.0048 -0.0211 0.0068  254 TYR C CB  
10488 C CG  . TYR C 254 ? 0.3148 0.1972 0.4071 -0.0027 -0.0203 0.0085  254 TYR C CG  
10489 C CD1 . TYR C 254 ? 0.3230 0.1994 0.4075 -0.0030 -0.0252 0.0084  254 TYR C CD1 
10490 C CD2 . TYR C 254 ? 0.3143 0.1957 0.4099 -0.0006 -0.0146 0.0106  254 TYR C CD2 
10491 C CE1 . TYR C 254 ? 0.3392 0.2077 0.4174 -0.0010 -0.0244 0.0106  254 TYR C CE1 
10492 C CE2 . TYR C 254 ? 0.3059 0.1799 0.3964 0.0011  -0.0129 0.0129  254 TYR C CE2 
10493 C CZ  . TYR C 254 ? 0.3137 0.1809 0.3947 0.0010  -0.0177 0.0130  254 TYR C CZ  
10494 O OH  . TYR C 254 ? 0.3001 0.1587 0.3741 0.0028  -0.0160 0.0159  254 TYR C OH  
10495 N N   . ARG C 255 ? 0.3469 0.2402 0.4429 -0.0113 -0.0311 0.0039  255 ARG C N   
10496 C CA  . ARG C 255 ? 0.3512 0.2471 0.4494 -0.0143 -0.0376 0.0029  255 ARG C CA  
10497 C C   . ARG C 255 ? 0.3714 0.2550 0.4572 -0.0167 -0.0397 0.0028  255 ARG C C   
10498 O O   . ARG C 255 ? 0.3550 0.2310 0.4330 -0.0178 -0.0455 0.0023  255 ARG C O   
10499 C CB  . ARG C 255 ? 0.3453 0.2556 0.4574 -0.0158 -0.0370 0.0024  255 ARG C CB  
10500 C CG  . ARG C 255 ? 0.3642 0.2797 0.4825 -0.0195 -0.0419 0.0020  255 ARG C CG  
10501 C CD  . ARG C 255 ? 0.3675 0.2878 0.4925 -0.0192 -0.0478 0.0015  255 ARG C CD  
10502 N NE  . ARG C 255 ? 0.3621 0.2709 0.4768 -0.0199 -0.0539 0.0017  255 ARG C NE  
10503 C CZ  . ARG C 255 ? 0.3688 0.2734 0.4798 -0.0174 -0.0569 0.0019  255 ARG C CZ  
10504 N NH1 . ARG C 255 ? 0.3610 0.2717 0.4790 -0.0140 -0.0544 0.0018  255 ARG C NH1 
10505 N NH2 . ARG C 255 ? 0.3658 0.2591 0.4654 -0.0183 -0.0630 0.0022  255 ARG C NH2 
10506 N N   . ASP C 256 ? 0.3895 0.2700 0.4724 -0.0172 -0.0353 0.0032  256 ASP C N   
10507 C CA  . ASP C 256 ? 0.3928 0.2618 0.4654 -0.0198 -0.0372 0.0027  256 ASP C CA  
10508 C C   . ASP C 256 ? 0.4063 0.2592 0.4615 -0.0180 -0.0380 0.0021  256 ASP C C   
10509 O O   . ASP C 256 ? 0.3982 0.2411 0.4436 -0.0204 -0.0437 0.0007  256 ASP C O   
10510 C CB  . ASP C 256 ? 0.4005 0.2677 0.4727 -0.0197 -0.0317 0.0035  256 ASP C CB  
10511 C CG  . ASP C 256 ? 0.3867 0.2671 0.4724 -0.0219 -0.0311 0.0045  256 ASP C CG  
10512 O OD1 . ASP C 256 ? 0.4420 0.3335 0.5378 -0.0236 -0.0344 0.0042  256 ASP C OD1 
10513 O OD2 . ASP C 256 ? 0.3739 0.2534 0.4598 -0.0215 -0.0269 0.0058  256 ASP C OD2 
10514 N N   . LEU C 257 ? 0.4102 0.2600 0.4612 -0.0139 -0.0326 0.0032  257 LEU C N   
10515 C CA  . LEU C 257 ? 0.4207 0.2535 0.4528 -0.0119 -0.0315 0.0030  257 LEU C CA  
10516 C C   . LEU C 257 ? 0.4294 0.2586 0.4555 -0.0125 -0.0389 0.0026  257 LEU C C   
10517 O O   . LEU C 257 ? 0.4306 0.2450 0.4393 -0.0129 -0.0424 0.0016  257 LEU C O   
10518 C CB  . LEU C 257 ? 0.4273 0.2572 0.4572 -0.0074 -0.0221 0.0049  257 LEU C CB  
10519 C CG  . LEU C 257 ? 0.4130 0.2428 0.4458 -0.0064 -0.0155 0.0054  257 LEU C CG  
10520 C CD1 . LEU C 257 ? 0.4036 0.2380 0.4435 -0.0024 -0.0072 0.0081  257 LEU C CD1 
10521 C CD2 . LEU C 257 ? 0.4105 0.2228 0.4257 -0.0063 -0.0147 0.0038  257 LEU C CD2 
10522 N N   . ILE C 258 ? 0.4314 0.2735 0.4712 -0.0124 -0.0418 0.0034  258 ILE C N   
10523 C CA  . ILE C 258 ? 0.4358 0.2762 0.4727 -0.0132 -0.0502 0.0034  258 ILE C CA  
10524 C C   . ILE C 258 ? 0.4254 0.2634 0.4607 -0.0176 -0.0589 0.0015  258 ILE C C   
10525 O O   . ILE C 258 ? 0.4247 0.2520 0.4475 -0.0186 -0.0661 0.0010  258 ILE C O   
10526 C CB  . ILE C 258 ? 0.4326 0.2877 0.4867 -0.0121 -0.0517 0.0043  258 ILE C CB  
10527 C CG1 . ILE C 258 ? 0.4478 0.3020 0.5014 -0.0082 -0.0447 0.0062  258 ILE C CG1 
10528 C CG2 . ILE C 258 ? 0.4368 0.2923 0.4918 -0.0132 -0.0618 0.0043  258 ILE C CG2 
10529 C CD1 . ILE C 258 ? 0.4361 0.3043 0.5073 -0.0070 -0.0449 0.0065  258 ILE C CD1 
10530 N N   . ASP C 259 ? 0.4144 0.2621 0.4622 -0.0206 -0.0584 0.0008  259 ASP C N   
10531 C CA  . ASP C 259 ? 0.4569 0.3042 0.5071 -0.0255 -0.0662 -0.0004 259 ASP C CA  
10532 C C   . ASP C 259 ? 0.4699 0.2975 0.4993 -0.0270 -0.0687 -0.0022 259 ASP C C   
10533 O O   . ASP C 259 ? 0.5153 0.3383 0.5423 -0.0311 -0.0778 -0.0035 259 ASP C O   
10534 C CB  . ASP C 259 ? 0.4376 0.2991 0.5052 -0.0281 -0.0633 -0.0001 259 ASP C CB  
10535 C CG  . ASP C 259 ? 0.4204 0.3004 0.5074 -0.0272 -0.0629 0.0009  259 ASP C CG  
10536 O OD1 . ASP C 259 ? 0.4218 0.3043 0.5118 -0.0262 -0.0683 0.0011  259 ASP C OD1 
10537 O OD2 . ASP C 259 ? 0.3987 0.2894 0.4965 -0.0270 -0.0572 0.0015  259 ASP C OD2 
10538 N N   . ALA C 260 ? 0.4616 0.2775 0.4766 -0.0235 -0.0607 -0.0023 260 ALA C N   
10539 C CA  . ALA C 260 ? 0.4787 0.2740 0.4715 -0.0236 -0.0613 -0.0044 260 ALA C CA  
10540 C C   . ALA C 260 ? 0.4868 0.2687 0.4608 -0.0216 -0.0657 -0.0047 260 ALA C C   
10541 O O   . ALA C 260 ? 0.5455 0.3087 0.4982 -0.0217 -0.0678 -0.0069 260 ALA C O   
10542 C CB  . ALA C 260 ? 0.4806 0.2698 0.4675 -0.0201 -0.0499 -0.0041 260 ALA C CB  
10543 N N   . GLY C 261 ? 0.4781 0.2685 0.4588 -0.0197 -0.0672 -0.0025 261 GLY C N   
10544 C CA  . GLY C 261 ? 0.4725 0.2511 0.4363 -0.0179 -0.0723 -0.0019 261 GLY C CA  
10545 C C   . GLY C 261 ? 0.4653 0.2390 0.4202 -0.0124 -0.0627 0.0007  261 GLY C C   
10546 O O   . GLY C 261 ? 0.4861 0.2466 0.4224 -0.0105 -0.0650 0.0015  261 GLY C O   
10547 N N   . ALA C 262 ? 0.4515 0.2357 0.4197 -0.0101 -0.0524 0.0022  262 ALA C N   
10548 C CA  . ALA C 262 ? 0.4647 0.2452 0.4275 -0.0054 -0.0424 0.0050  262 ALA C CA  
10549 C C   . ALA C 262 ? 0.4699 0.2563 0.4386 -0.0042 -0.0459 0.0078  262 ALA C C   
10550 O O   . ALA C 262 ? 0.4147 0.2160 0.4022 -0.0060 -0.0513 0.0076  262 ALA C O   
10551 C CB  . ALA C 262 ? 0.4375 0.2287 0.4158 -0.0041 -0.0324 0.0059  262 ALA C CB  
10552 N N   . VAL C 263 ? 0.5076 0.2810 0.4591 -0.0010 -0.0428 0.0103  263 VAL C N   
10553 C CA  . VAL C 263 ? 0.5221 0.2983 0.4768 0.0006  -0.0453 0.0136  263 VAL C CA  
10554 C C   . VAL C 263 ? 0.5345 0.3111 0.4920 0.0042  -0.0333 0.0173  263 VAL C C   
10555 O O   . VAL C 263 ? 0.5008 0.2765 0.4585 0.0060  -0.0329 0.0209  263 VAL C O   
10556 C CB  . VAL C 263 ? 0.5468 0.3068 0.4786 0.0009  -0.0537 0.0143  263 VAL C CB  
10557 C CG1 . VAL C 263 ? 0.5453 0.3079 0.4799 -0.0032 -0.0676 0.0112  263 VAL C CG1 
10558 C CG2 . VAL C 263 ? 0.5668 0.3058 0.4702 0.0033  -0.0471 0.0144  263 VAL C CG2 
10559 N N   . GLY C 264 ? 0.5446 0.3223 0.5051 0.0051  -0.0235 0.0168  264 GLY C N   
10560 C CA  . GLY C 264 ? 0.5521 0.3344 0.5221 0.0077  -0.0126 0.0201  264 GLY C CA  
10561 C C   . GLY C 264 ? 0.5491 0.3408 0.5330 0.0073  -0.0067 0.0185  264 GLY C C   
10562 O O   . GLY C 264 ? 0.5295 0.3170 0.5070 0.0062  -0.0076 0.0155  264 GLY C O   
10563 N N   . MET C 265 ? 0.5550 0.3594 0.5585 0.0078  -0.0019 0.0204  265 MET C N   
10564 C CA  . MET C 265 ? 0.4934 0.3094 0.5132 0.0071  0.0013  0.0190  265 MET C CA  
10565 C C   . MET C 265 ? 0.4729 0.2923 0.5026 0.0095  0.0112  0.0226  265 MET C C   
10566 O O   . MET C 265 ? 0.4903 0.3134 0.5279 0.0098  0.0121  0.0252  265 MET C O   
10567 C CB  . MET C 265 ? 0.4523 0.2839 0.4899 0.0043  -0.0065 0.0166  265 MET C CB  
10568 C CG  . MET C 265 ? 0.4684 0.2988 0.5000 0.0016  -0.0159 0.0136  265 MET C CG  
10569 S SD  . MET C 265 ? 0.4577 0.2834 0.4823 -0.0001 -0.0158 0.0108  265 MET C SD  
10570 C CE  . MET C 265 ? 0.4292 0.2746 0.4778 -0.0017 -0.0157 0.0099  265 MET C CE  
10571 N N   . CYS C 266 ? 0.4613 0.2794 0.4916 0.0110  0.0183  0.0228  266 CYS C N   
10572 C CA  . CYS C 266 ? 0.4614 0.2845 0.5045 0.0131  0.0275  0.0263  266 CYS C CA  
10573 C C   . CYS C 266 ? 0.4144 0.2499 0.4748 0.0123  0.0274  0.0251  266 CYS C C   
10574 O O   . CYS C 266 ? 0.3903 0.2230 0.4505 0.0145  0.0340  0.0260  266 CYS C O   
10575 C CB  . CYS C 266 ? 0.4790 0.2885 0.5081 0.0169  0.0382  0.0288  266 CYS C CB  
10576 S SG  . CYS C 266 ? 0.4900 0.2828 0.4958 0.0186  0.0404  0.0315  266 CYS C SG  
10577 N N   . PRO C 267 ? 0.3925 0.2417 0.4684 0.0097  0.0205  0.0234  267 PRO C N   
10578 C CA  . PRO C 267 ? 0.3670 0.2281 0.4591 0.0090  0.0202  0.0229  267 PRO C CA  
10579 C C   . PRO C 267 ? 0.3665 0.2302 0.4699 0.0115  0.0285  0.0267  267 PRO C C   
10580 O O   . PRO C 267 ? 0.3323 0.1948 0.4396 0.0124  0.0330  0.0299  267 PRO C O   
10581 C CB  . PRO C 267 ? 0.3600 0.2329 0.4645 0.0065  0.0128  0.0210  267 PRO C CB  
10582 C CG  . PRO C 267 ? 0.3711 0.2387 0.4704 0.0066  0.0118  0.0221  267 PRO C CG  
10583 C CD  . PRO C 267 ? 0.3935 0.2468 0.4719 0.0076  0.0131  0.0222  267 PRO C CD  
10584 N N   . PHE C 268 ? 0.3810 0.2484 0.4902 0.0123  0.0302  0.0267  268 PHE C N   
10585 C CA  . PHE C 268 ? 0.3744 0.2446 0.4953 0.0150  0.0376  0.0303  268 PHE C CA  
10586 C C   . PHE C 268 ? 0.3556 0.2406 0.4964 0.0135  0.0330  0.0304  268 PHE C C   
10587 O O   . PHE C 268 ? 0.3531 0.2422 0.4939 0.0122  0.0275  0.0280  268 PHE C O   
10588 C CB  . PHE C 268 ? 0.3904 0.2520 0.5019 0.0179  0.0429  0.0303  268 PHE C CB  
10589 C CG  . PHE C 268 ? 0.3764 0.2396 0.4995 0.0218  0.0523  0.0346  268 PHE C CG  
10590 C CD1 . PHE C 268 ? 0.3814 0.2363 0.4996 0.0251  0.0625  0.0377  268 PHE C CD1 
10591 C CD2 . PHE C 268 ? 0.3872 0.2608 0.5274 0.0223  0.0510  0.0359  268 PHE C CD2 
10592 C CE1 . PHE C 268 ? 0.3754 0.2335 0.5074 0.0287  0.0717  0.0421  268 PHE C CE1 
10593 C CE2 . PHE C 268 ? 0.3793 0.2557 0.5330 0.0260  0.0591  0.0402  268 PHE C CE2 
10594 C CZ  . PHE C 268 ? 0.3724 0.2417 0.5232 0.0292  0.0697  0.0434  268 PHE C CZ  
10595 N N   . TYR C 269 ? 0.3549 0.2472 0.5120 0.0134  0.0346  0.0333  269 TYR C N   
10596 C CA  . TYR C 269 ? 0.3402 0.2284 0.4982 0.0140  0.0401  0.0364  269 TYR C CA  
10597 C C   . TYR C 269 ? 0.3230 0.2223 0.5011 0.0116  0.0363  0.0375  269 TYR C C   
10598 O O   . TYR C 269 ? 0.3132 0.2218 0.5007 0.0097  0.0289  0.0351  269 TYR C O   
10599 C CB  . TYR C 269 ? 0.3348 0.2154 0.4901 0.0180  0.0519  0.0406  269 TYR C CB  
10600 C CG  . TYR C 269 ? 0.3352 0.2234 0.5096 0.0202  0.0574  0.0445  269 TYR C CG  
10601 C CD1 . TYR C 269 ? 0.3338 0.2329 0.5223 0.0192  0.0513  0.0436  269 TYR C CD1 
10602 C CD2 . TYR C 269 ? 0.3412 0.2253 0.5193 0.0237  0.0692  0.0494  269 TYR C CD2 
10603 C CE1 . TYR C 269 ? 0.3245 0.2306 0.5311 0.0216  0.0555  0.0475  269 TYR C CE1 
10604 C CE2 . TYR C 269 ? 0.3203 0.2119 0.5174 0.0263  0.0746  0.0533  269 TYR C CE2 
10605 C CZ  . TYR C 269 ? 0.3209 0.2237 0.5329 0.0251  0.0671  0.0523  269 TYR C CZ  
10606 O OH  . TYR C 269 ? 0.3238 0.2348 0.5561 0.0276  0.0708  0.0564  269 TYR C OH  
10607 N N   . TYR C 270 ? 0.3345 0.2323 0.5192 0.0117  0.0414  0.0413  270 TYR C N   
10608 C CA  . TYR C 270 ? 0.3203 0.2266 0.5229 0.0088  0.0369  0.0420  270 TYR C CA  
10609 C C   . TYR C 270 ? 0.3117 0.2298 0.5354 0.0082  0.0343  0.0430  270 TYR C C   
10610 O O   . TYR C 270 ? 0.3146 0.2399 0.5456 0.0055  0.0252  0.0397  270 TYR C O   
10611 C CB  . TYR C 270 ? 0.3502 0.2511 0.5551 0.0090  0.0439  0.0468  270 TYR C CB  
10612 C CG  . TYR C 270 ? 0.3399 0.2485 0.5665 0.0060  0.0415  0.0490  270 TYR C CG  
10613 C CD1 . TYR C 270 ? 0.3524 0.2637 0.5819 0.0030  0.0320  0.0451  270 TYR C CD1 
10614 C CD2 . TYR C 270 ? 0.3574 0.2694 0.6015 0.0064  0.0492  0.0551  270 TYR C CD2 
10615 C CE1 . TYR C 270 ? 0.3257 0.2423 0.5741 0.0000  0.0291  0.0466  270 TYR C CE1 
10616 C CE2 . TYR C 270 ? 0.3629 0.2812 0.6275 0.0031  0.0465  0.0573  270 TYR C CE2 
10617 C CZ  . TYR C 270 ? 0.3285 0.2485 0.5947 -0.0002 0.0360  0.0528  270 TYR C CZ  
10618 O OH  . TYR C 270 ? 0.3275 0.2524 0.6135 -0.0037 0.0326  0.0544  270 TYR C OH  
10619 N N   . ALA C 271 ? 0.3013 0.2217 0.5356 0.0106  0.0419  0.0476  271 ALA C N   
10620 C CA  . ALA C 271 ? 0.3057 0.2380 0.5622 0.0098  0.0380  0.0491  271 ALA C CA  
10621 C C   . ALA C 271 ? 0.3189 0.2532 0.5807 0.0136  0.0437  0.0521  271 ALA C C   
10622 O O   . ALA C 271 ? 0.3304 0.2568 0.5835 0.0172  0.0540  0.0546  271 ALA C O   
10623 C CB  . ALA C 271 ? 0.3126 0.2500 0.5895 0.0075  0.0393  0.0530  271 ALA C CB  
10624 N N   . ASP C 272 ? 0.3044 0.2487 0.5803 0.0129  0.0367  0.0518  272 ASP C N   
10625 C CA  . ASP C 272 ? 0.3213 0.2685 0.6042 0.0165  0.0401  0.0546  272 ASP C CA  
10626 C C   . ASP C 272 ? 0.3140 0.2616 0.6111 0.0198  0.0523  0.0611  272 ASP C C   
10627 O O   . ASP C 272 ? 0.3025 0.2545 0.6153 0.0179  0.0547  0.0645  272 ASP C O   
10628 C CB  . ASP C 272 ? 0.3402 0.2990 0.6395 0.0149  0.0297  0.0544  272 ASP C CB  
10629 C CG  . ASP C 272 ? 0.3569 0.3158 0.6427 0.0135  0.0195  0.0492  272 ASP C CG  
10630 O OD1 . ASP C 272 ? 0.3530 0.3034 0.6170 0.0136  0.0203  0.0455  272 ASP C OD1 
10631 O OD2 . ASP C 272 ? 0.3404 0.3080 0.6381 0.0122  0.0107  0.0492  272 ASP C OD2 
10632 N N   . GLY C 273 ? 0.3029 0.2450 0.5935 0.0248  0.0606  0.0627  273 GLY C N   
10633 C CA  . GLY C 273 ? 0.3137 0.2569 0.6186 0.0292  0.0730  0.0689  273 GLY C CA  
10634 C C   . GLY C 273 ? 0.3045 0.2562 0.6263 0.0322  0.0711  0.0713  273 GLY C C   
10635 O O   . GLY C 273 ? 0.3200 0.2657 0.6287 0.0352  0.0710  0.0692  273 GLY C O   
10636 N N   . TRP C 274 ? 0.2930 0.2582 0.6441 0.0311  0.0684  0.0758  274 TRP C N   
10637 C CA  . TRP C 274 ? 0.3078 0.2826 0.6780 0.0337  0.0646  0.0787  274 TRP C CA  
10638 C C   . TRP C 274 ? 0.3472 0.3181 0.7214 0.0410  0.0789  0.0831  274 TRP C C   
10639 O O   . TRP C 274 ? 0.3513 0.3261 0.7349 0.0448  0.0774  0.0851  274 TRP C O   
10640 C CB  . TRP C 274 ? 0.2980 0.2883 0.6998 0.0302  0.0573  0.0825  274 TRP C CB  
10641 C CG  . TRP C 274 ? 0.2876 0.2824 0.6877 0.0238  0.0414  0.0778  274 TRP C CG  
10642 C CD1 . TRP C 274 ? 0.2914 0.2785 0.6672 0.0203  0.0354  0.0713  274 TRP C CD1 
10643 C CD2 . TRP C 274 ? 0.2722 0.2800 0.6961 0.0202  0.0291  0.0792  274 TRP C CD2 
10644 N NE1 . TRP C 274 ? 0.2704 0.2642 0.6524 0.0154  0.0213  0.0683  274 TRP C NE1 
10645 C CE2 . TRP C 274 ? 0.2636 0.2695 0.6740 0.0149  0.0168  0.0729  274 TRP C CE2 
10646 C CE3 . TRP C 274 ? 0.2565 0.2772 0.7122 0.0211  0.0269  0.0852  274 TRP C CE3 
10647 C CZ2 . TRP C 274 ? 0.2518 0.2667 0.6769 0.0106  0.0026  0.0718  274 TRP C CZ2 
10648 C CZ3 . TRP C 274 ? 0.2462 0.2765 0.7176 0.0162  0.0118  0.0844  274 TRP C CZ3 
10649 C CH2 . TRP C 274 ? 0.2387 0.2655 0.6938 0.0111  -0.0002 0.0775  274 TRP C CH2 
10650 N N   . TRP C 275 ? 0.3607 0.3233 0.7271 0.0433  0.0928  0.0848  275 TRP C N   
10651 C CA  . TRP C 275 ? 0.3855 0.3432 0.7546 0.0506  0.1083  0.0889  275 TRP C CA  
10652 C C   . TRP C 275 ? 0.3837 0.3274 0.7265 0.0547  0.1099  0.0844  275 TRP C C   
10653 O O   . TRP C 275 ? 0.4051 0.3457 0.7517 0.0613  0.1190  0.0868  275 TRP C O   
10654 C CB  . TRP C 275 ? 0.3975 0.3489 0.7632 0.0519  0.1233  0.0921  275 TRP C CB  
10655 C CG  . TRP C 275 ? 0.4093 0.3438 0.7398 0.0506  0.1256  0.0870  275 TRP C CG  
10656 C CD1 . TRP C 275 ? 0.3816 0.3142 0.7016 0.0447  0.1186  0.0842  275 TRP C CD1 
10657 C CD2 . TRP C 275 ? 0.4395 0.3562 0.7410 0.0557  0.1354  0.0842  275 TRP C CD2 
10658 N NE1 . TRP C 275 ? 0.3978 0.3137 0.6855 0.0456  0.1227  0.0802  275 TRP C NE1 
10659 C CE2 . TRP C 275 ? 0.4187 0.3242 0.6937 0.0520  0.1325  0.0799  275 TRP C CE2 
10660 C CE3 . TRP C 275 ? 0.4257 0.3340 0.7206 0.0630  0.1453  0.0845  275 TRP C CE3 
10661 C CZ2 . TRP C 275 ? 0.4499 0.3366 0.6924 0.0550  0.1385  0.0761  275 TRP C CZ2 
10662 C CZ3 . TRP C 275 ? 0.4268 0.3155 0.6884 0.0659  0.1516  0.0801  275 TRP C CZ3 
10663 C CH2 . TRP C 275 ? 0.4435 0.3216 0.6792 0.0618  0.1479  0.0760  275 TRP C CH2 
10664 N N   . LYS C 276 ? 0.3664 0.3026 0.6848 0.0507  0.1004  0.0780  276 LYS C N   
10665 C CA  . LYS C 276 ? 0.4006 0.3201 0.6892 0.0533  0.1039  0.0734  276 LYS C CA  
10666 C C   . LYS C 276 ? 0.4163 0.3345 0.7065 0.0575  0.1020  0.0733  276 LYS C C   
10667 O O   . LYS C 276 ? 0.4839 0.3877 0.7540 0.0611  0.1077  0.0707  276 LYS C O   
10668 C CB  . LYS C 276 ? 0.3767 0.2898 0.6418 0.0475  0.0943  0.0672  276 LYS C CB  
10669 C CG  . LYS C 276 ? 0.3681 0.2751 0.6218 0.0453  0.0992  0.0667  276 LYS C CG  
10670 C CD  . LYS C 276 ? 0.3627 0.2660 0.5980 0.0395  0.0886  0.0611  276 LYS C CD  
10671 C CE  . LYS C 276 ? 0.3645 0.2543 0.5724 0.0399  0.0864  0.0558  276 LYS C CE  
10672 N NZ  . LYS C 276 ? 0.3953 0.2692 0.5837 0.0438  0.0979  0.0557  276 LYS C NZ  
10673 N N   . GLY C 277 ? 0.4274 0.3595 0.7407 0.0570  0.0937  0.0762  277 GLY C N   
10674 C CA  . GLY C 277 ? 0.4489 0.3800 0.7654 0.0613  0.0918  0.0772  277 GLY C CA  
10675 C C   . GLY C 277 ? 0.4596 0.4020 0.8075 0.0666  0.0972  0.0842  277 GLY C C   
10676 O O   . GLY C 277 ? 0.4638 0.4111 0.8227 0.0690  0.0914  0.0863  277 GLY C O   
10677 N N   . GLY C 278 ? 0.4626 0.4090 0.8251 0.0687  0.1087  0.0883  278 GLY C N   
10678 C CA  . GLY C 278 ? 0.4314 0.3910 0.8281 0.0732  0.1140  0.0956  278 GLY C CA  
10679 C C   . GLY C 278 ? 0.4102 0.3884 0.8335 0.0672  0.1017  0.0986  278 GLY C C   
10680 O O   . GLY C 278 ? 0.4542 0.4346 0.8686 0.0606  0.0878  0.0945  278 GLY C O   
10681 N N   . GLU C 279 ? 0.3972 0.3883 0.8530 0.0697  0.1075  0.1055  279 GLU C N   
10682 C CA  . GLU C 279 ? 0.3956 0.4043 0.8805 0.0642  0.0971  0.1090  279 GLU C CA  
10683 C C   . GLU C 279 ? 0.3560 0.3629 0.8286 0.0563  0.0920  0.1050  279 GLU C C   
10684 O O   . GLU C 279 ? 0.3396 0.3456 0.7988 0.0508  0.0779  0.0999  279 GLU C O   
10685 C CB  . GLU C 279 ? 0.3895 0.4085 0.8882 0.0633  0.0805  0.1098  279 GLU C CB  
10686 C CG  . GLU C 279 ? 0.4138 0.4417 0.9417 0.0707  0.0860  0.1170  279 GLU C CG  
10687 C CD  . GLU C 279 ? 0.4444 0.4580 0.9559 0.0792  0.1007  0.1165  279 GLU C CD  
10688 O OE1 . GLU C 279 ? 0.4131 0.4138 0.8956 0.0794  0.0961  0.1110  279 GLU C OE1 
10689 O OE2 . GLU C 279 ? 0.4918 0.5071 1.0197 0.0857  0.1167  0.1215  279 GLU C OE2 
10690 N N   . LYS C 280 ? 0.3726 0.3791 0.8513 0.0560  0.1040  0.1080  280 LYS C N   
10691 C CA  . LYS C 280 ? 0.3620 0.3656 0.8296 0.0490  0.1007  0.1049  280 LYS C CA  
10692 C C   . LYS C 280 ? 0.3258 0.3433 0.8147 0.0417  0.0847  0.1052  280 LYS C C   
10693 O O   . LYS C 280 ? 0.3239 0.3378 0.7994 0.0358  0.0775  0.1008  280 LYS C O   
10694 C CB  . LYS C 280 ? 0.3743 0.3741 0.8450 0.0510  0.1185  0.1094  280 LYS C CB  
10695 C CG  . LYS C 280 ? 0.3724 0.3878 0.8836 0.0522  0.1247  0.1181  280 LYS C CG  
10696 C CD  . LYS C 280 ? 0.4008 0.4122 0.9150 0.0547  0.1442  0.1234  280 LYS C CD  
10697 C CE  . LYS C 280 ? 0.4002 0.4295 0.9586 0.0559  0.1493  0.1324  280 LYS C CE  
10698 N NZ  . LYS C 280 ? 0.4172 0.4421 0.9783 0.0610  0.1716  0.1382  280 LYS C NZ  
10699 N N   . SER C 281 ? 0.3129 0.3454 0.8341 0.0424  0.0787  0.1101  281 SER C N   
10700 C CA  . SER C 281 ? 0.3294 0.3753 0.8736 0.0357  0.0630  0.1108  281 SER C CA  
10701 C C   . SER C 281 ? 0.3386 0.3858 0.8733 0.0335  0.0444  0.1059  281 SER C C   
10702 O O   . SER C 281 ? 0.3402 0.3966 0.8892 0.0280  0.0295  0.1053  281 SER C O   
10703 C CB  . SER C 281 ? 0.3370 0.3989 0.9232 0.0370  0.0660  0.1194  281 SER C CB  
10704 O OG  . SER C 281 ? 0.3455 0.4071 0.9416 0.0371  0.0815  0.1239  281 SER C OG  
10705 N N   . ASP C 282 ? 0.3420 0.3790 0.8507 0.0374  0.0453  0.1022  282 ASP C N   
10706 C CA  . ASP C 282 ? 0.3460 0.3831 0.8434 0.0358  0.0296  0.0982  282 ASP C CA  
10707 C C   . ASP C 282 ? 0.3216 0.3435 0.7803 0.0349  0.0301  0.0909  282 ASP C C   
10708 O O   . ASP C 282 ? 0.2990 0.3098 0.7402 0.0388  0.0428  0.0900  282 ASP C O   
10709 C CB  . ASP C 282 ? 0.3808 0.4233 0.8929 0.0418  0.0287  0.1030  282 ASP C CB  
10710 C CG  . ASP C 282 ? 0.4529 0.4967 0.9564 0.0402  0.0118  0.1003  282 ASP C CG  
10711 O OD1 . ASP C 282 ? 0.4974 0.5500 1.0123 0.0348  -0.0027 0.0997  282 ASP C OD1 
10712 O OD2 . ASP C 282 ? 0.5272 0.5625 1.0120 0.0442  0.0131  0.0990  282 ASP C OD2 
10713 N N   . HIS C 283 ? 0.3168 0.3385 0.7626 0.0301  0.0157  0.0857  283 HIS C N   
10714 C CA  . HIS C 283 ? 0.3052 0.3145 0.7172 0.0290  0.0146  0.0791  283 HIS C CA  
10715 C C   . HIS C 283 ? 0.3092 0.3160 0.7110 0.0320  0.0094  0.0788  283 HIS C C   
10716 O O   . HIS C 283 ? 0.3053 0.3170 0.7080 0.0297  -0.0040 0.0778  283 HIS C O   
10717 C CB  . HIS C 283 ? 0.2838 0.2935 0.6865 0.0223  0.0036  0.0735  283 HIS C CB  
10718 C CG  . HIS C 283 ? 0.2805 0.2783 0.6537 0.0208  0.0067  0.0675  283 HIS C CG  
10719 N ND1 . HIS C 283 ? 0.2671 0.2635 0.6276 0.0159  -0.0025 0.0618  283 HIS C ND1 
10720 C CD2 . HIS C 283 ? 0.2787 0.2657 0.6340 0.0237  0.0179  0.0666  283 HIS C CD2 
10721 C CE1 . HIS C 283 ? 0.2866 0.2726 0.6236 0.0159  0.0029  0.0579  283 HIS C CE1 
10722 N NE2 . HIS C 283 ? 0.2832 0.2632 0.6163 0.0203  0.0149  0.0606  283 HIS C NE2 
10723 N N   . SER C 284 ? 0.3360 0.3341 0.7275 0.0373  0.0200  0.0799  284 SER C N   
10724 C CA  . SER C 284 ? 0.3426 0.3381 0.7284 0.0409  0.0162  0.0810  284 SER C CA  
10725 C C   . SER C 284 ? 0.3434 0.3320 0.7021 0.0372  0.0075  0.0752  284 SER C C   
10726 O O   . SER C 284 ? 0.3212 0.3013 0.6591 0.0347  0.0109  0.0703  284 SER C O   
10727 C CB  . SER C 284 ? 0.3594 0.3466 0.7422 0.0475  0.0297  0.0834  284 SER C CB  
10728 O OG  . SER C 284 ? 0.3930 0.3748 0.7642 0.0498  0.0252  0.0832  284 SER C OG  
10729 N N   . LEU C 285 ? 0.3568 0.3495 0.7166 0.0368  -0.0038 0.0763  285 LEU C N   
10730 C CA  . LEU C 285 ? 0.3785 0.3664 0.7151 0.0333  -0.0124 0.0717  285 LEU C CA  
10731 C C   . LEU C 285 ? 0.3738 0.3488 0.6883 0.0354  -0.0053 0.0700  285 LEU C C   
10732 O O   . LEU C 285 ? 0.3869 0.3563 0.6803 0.0320  -0.0084 0.0654  285 LEU C O   
10733 C CB  . LEU C 285 ? 0.4186 0.4137 0.7610 0.0324  -0.0263 0.0738  285 LEU C CB  
10734 C CG  . LEU C 285 ? 0.4873 0.4951 0.8543 0.0305  -0.0352 0.0760  285 LEU C CG  
10735 C CD1 . LEU C 285 ? 0.4986 0.5110 0.8644 0.0291  -0.0508 0.0769  285 LEU C CD1 
10736 C CD2 . LEU C 285 ? 0.4470 0.4572 0.8162 0.0255  -0.0349 0.0717  285 LEU C CD2 
10737 N N   . ASN C 286 ? 0.3614 0.3315 0.6811 0.0411  0.0042  0.0735  286 ASN C N   
10738 C CA  . ASN C 286 ? 0.3834 0.3403 0.6828 0.0430  0.0097  0.0720  286 ASN C CA  
10739 C C   . ASN C 286 ? 0.3690 0.3154 0.6596 0.0452  0.0230  0.0699  286 ASN C C   
10740 O O   . ASN C 286 ? 0.3586 0.2934 0.6374 0.0483  0.0289  0.0696  286 ASN C O   
10741 C CB  . ASN C 286 ? 0.4064 0.3618 0.7124 0.0480  0.0084  0.0770  286 ASN C CB  
10742 C CG  . ASN C 286 ? 0.4174 0.3751 0.7445 0.0545  0.0173  0.0819  286 ASN C CG  
10743 O OD1 . ASN C 286 ? 0.4543 0.4199 0.7984 0.0547  0.0210  0.0832  286 ASN C OD1 
10744 N ND2 . ASN C 286 ? 0.4336 0.3847 0.7611 0.0599  0.0206  0.0851  286 ASN C ND2 
10745 N N   . GLN C 287 ? 0.3658 0.3148 0.6597 0.0432  0.0271  0.0681  287 GLN C N   
10746 C CA  . GLN C 287 ? 0.3985 0.3370 0.6819 0.0450  0.0392  0.0663  287 GLN C CA  
10747 C C   . GLN C 287 ? 0.3935 0.3273 0.6573 0.0395  0.0366  0.0605  287 GLN C C   
10748 O O   . GLN C 287 ? 0.4141 0.3543 0.6840 0.0363  0.0348  0.0596  287 GLN C O   
10749 C CB  . GLN C 287 ? 0.4277 0.3715 0.7300 0.0477  0.0482  0.0698  287 GLN C CB  
10750 C CG  . GLN C 287 ? 0.4688 0.4163 0.7918 0.0544  0.0544  0.0758  287 GLN C CG  
10751 C CD  . GLN C 287 ? 0.4813 0.4145 0.7905 0.0601  0.0629  0.0754  287 GLN C CD  
10752 O OE1 . GLN C 287 ? 0.4921 0.4115 0.7798 0.0604  0.0702  0.0715  287 GLN C OE1 
10753 N NE2 . GLN C 287 ? 0.4817 0.4170 0.8019 0.0644  0.0608  0.0791  287 GLN C NE2 
10754 N N   . PRO C 288 ? 0.3927 0.3152 0.6338 0.0383  0.0364  0.0566  288 PRO C N   
10755 C CA  . PRO C 288 ? 0.3877 0.3060 0.6115 0.0334  0.0340  0.0514  288 PRO C CA  
10756 C C   . PRO C 288 ? 0.3855 0.3031 0.6104 0.0329  0.0400  0.0507  288 PRO C C   
10757 O O   . PRO C 288 ? 0.3769 0.2978 0.5983 0.0286  0.0354  0.0479  288 PRO C O   
10758 C CB  . PRO C 288 ? 0.3937 0.2976 0.5975 0.0344  0.0372  0.0490  288 PRO C CB  
10759 C CG  . PRO C 288 ? 0.4211 0.3260 0.6307 0.0369  0.0343  0.0522  288 PRO C CG  
10760 C CD  . PRO C 288 ? 0.4160 0.3297 0.6488 0.0412  0.0375  0.0574  288 PRO C CD  
10761 N N   . GLU C 289 ? 0.3656 0.2787 0.5956 0.0377  0.0508  0.0536  289 GLU C N   
10762 C CA  . GLU C 289 ? 0.3768 0.2842 0.6015 0.0382  0.0593  0.0532  289 GLU C CA  
10763 C C   . GLU C 289 ? 0.3595 0.2789 0.6020 0.0356  0.0573  0.0553  289 GLU C C   
10764 O O   . GLU C 289 ? 0.3494 0.2647 0.5861 0.0346  0.0621  0.0548  289 GLU C O   
10765 C CB  . GLU C 289 ? 0.3737 0.2720 0.5976 0.0447  0.0726  0.0558  289 GLU C CB  
10766 C CG  . GLU C 289 ? 0.3871 0.2684 0.5870 0.0468  0.0762  0.0523  289 GLU C CG  
10767 C CD  . GLU C 289 ? 0.4189 0.2888 0.5940 0.0434  0.0750  0.0473  289 GLU C CD  
10768 O OE1 . GLU C 289 ? 0.4293 0.2978 0.6018 0.0430  0.0798  0.0477  289 GLU C OE1 
10769 O OE2 . GLU C 289 ? 0.4438 0.3063 0.6028 0.0410  0.0692  0.0433  289 GLU C OE2 
10770 N N   . GLU C 290 ? 0.3263 0.2592 0.5896 0.0345  0.0501  0.0578  290 GLU C N   
10771 C CA  . GLU C 290 ? 0.3335 0.2776 0.6160 0.0318  0.0472  0.0599  290 GLU C CA  
10772 C C   . GLU C 290 ? 0.3455 0.2933 0.6218 0.0258  0.0357  0.0554  290 GLU C C   
10773 O O   . GLU C 290 ? 0.2959 0.2521 0.5869 0.0229  0.0315  0.0562  290 GLU C O   
10774 C CB  . GLU C 290 ? 0.3514 0.3075 0.6599 0.0338  0.0444  0.0648  290 GLU C CB  
10775 C CG  . GLU C 290 ? 0.3670 0.3205 0.6845 0.0404  0.0560  0.0696  290 GLU C CG  
10776 C CD  . GLU C 290 ? 0.3679 0.3346 0.7160 0.0429  0.0551  0.0757  290 GLU C CD  
10777 O OE1 . GLU C 290 ? 0.3662 0.3447 0.7316 0.0389  0.0458  0.0768  290 GLU C OE1 
10778 O OE2 . GLU C 290 ? 0.4064 0.3709 0.7617 0.0490  0.0641  0.0794  290 GLU C OE2 
10779 N N   . TRP C 291 ? 0.3395 0.2813 0.5954 0.0241  0.0308  0.0507  291 TRP C N   
10780 C CA  . TRP C 291 ? 0.3295 0.2757 0.5808 0.0193  0.0203  0.0465  291 TRP C CA  
10781 C C   . TRP C 291 ? 0.3035 0.2409 0.5333 0.0172  0.0206  0.0418  291 TRP C C   
10782 O O   . TRP C 291 ? 0.3021 0.2412 0.5239 0.0144  0.0131  0.0382  291 TRP C O   
10783 C CB  . TRP C 291 ? 0.3309 0.2823 0.5830 0.0187  0.0113  0.0461  291 TRP C CB  
10784 C CG  . TRP C 291 ? 0.3349 0.2958 0.6084 0.0204  0.0081  0.0506  291 TRP C CG  
10785 C CD1 . TRP C 291 ? 0.3184 0.2795 0.6020 0.0250  0.0133  0.0554  291 TRP C CD1 
10786 C CD2 . TRP C 291 ? 0.3248 0.2960 0.6118 0.0176  -0.0022 0.0506  291 TRP C CD2 
10787 N NE1 . TRP C 291 ? 0.3068 0.2788 0.6112 0.0252  0.0069  0.0589  291 TRP C NE1 
10788 C CE2 . TRP C 291 ? 0.3016 0.2795 0.6077 0.0205  -0.0031 0.0560  291 TRP C CE2 
10789 C CE3 . TRP C 291 ? 0.3125 0.2872 0.5969 0.0132  -0.0108 0.0464  291 TRP C CE3 
10790 C CZ2 . TRP C 291 ? 0.3085 0.2966 0.6312 0.0187  -0.0133 0.0574  291 TRP C CZ2 
10791 C CZ3 . TRP C 291 ? 0.3221 0.3057 0.6216 0.0115  -0.0203 0.0473  291 TRP C CZ3 
10792 C CH2 . TRP C 291 ? 0.3164 0.3068 0.6345 0.0140  -0.0221 0.0527  291 TRP C CH2 
10793 N N   . PHE C 292 ? 0.3084 0.2373 0.5300 0.0186  0.0288  0.0421  292 PHE C N   
10794 C CA  . PHE C 292 ? 0.3168 0.2369 0.5185 0.0168  0.0286  0.0382  292 PHE C CA  
10795 C C   . PHE C 292 ? 0.3116 0.2338 0.5145 0.0138  0.0257  0.0365  292 PHE C C   
10796 O O   . PHE C 292 ? 0.3159 0.2319 0.5040 0.0124  0.0245  0.0334  292 PHE C O   
10797 C CB  . PHE C 292 ? 0.3334 0.2410 0.5227 0.0200  0.0385  0.0393  292 PHE C CB  
10798 C CG  . PHE C 292 ? 0.3459 0.2458 0.5223 0.0217  0.0391  0.0379  292 PHE C CG  
10799 C CD1 . PHE C 292 ? 0.3739 0.2678 0.5333 0.0191  0.0345  0.0337  292 PHE C CD1 
10800 C CD2 . PHE C 292 ? 0.3361 0.2351 0.5191 0.0256  0.0439  0.0408  292 PHE C CD2 
10801 C CE1 . PHE C 292 ? 0.3899 0.2764 0.5387 0.0199  0.0345  0.0326  292 PHE C CE1 
10802 C CE2 . PHE C 292 ? 0.3756 0.2661 0.5466 0.0270  0.0444  0.0395  292 PHE C CE2 
10803 C CZ  . PHE C 292 ? 0.3834 0.2677 0.5375 0.0238  0.0394  0.0354  292 PHE C CZ  
10804 N N   . GLY C 293 ? 0.3056 0.2360 0.5265 0.0128  0.0244  0.0387  293 GLY C N   
10805 C CA  . GLY C 293 ? 0.2855 0.2161 0.5088 0.0104  0.0233  0.0380  293 GLY C CA  
10806 C C   . GLY C 293 ? 0.2747 0.2078 0.4918 0.0072  0.0138  0.0327  293 GLY C C   
10807 O O   . GLY C 293 ? 0.2494 0.1879 0.4669 0.0063  0.0073  0.0305  293 GLY C O   
10808 N N   . PHE C 294 ? 0.2769 0.2060 0.4883 0.0057  0.0134  0.0311  294 PHE C N   
10809 C CA  . PHE C 294 ? 0.2728 0.2056 0.4839 0.0031  0.0052  0.0267  294 PHE C CA  
10810 C C   . PHE C 294 ? 0.2732 0.2132 0.5027 0.0012  0.0011  0.0274  294 PHE C C   
10811 O O   . PHE C 294 ? 0.2976 0.2415 0.5286 -0.0008 -0.0066 0.0233  294 PHE C O   
10812 C CB  . PHE C 294 ? 0.2769 0.2020 0.4760 0.0028  0.0063  0.0253  294 PHE C CB  
10813 C CG  . PHE C 294 ? 0.2750 0.1929 0.4558 0.0038  0.0079  0.0238  294 PHE C CG  
10814 C CD1 . PHE C 294 ? 0.2838 0.2007 0.4587 0.0050  0.0095  0.0240  294 PHE C CD1 
10815 C CD2 . PHE C 294 ? 0.2837 0.1950 0.4539 0.0036  0.0075  0.0226  294 PHE C CD2 
10816 C CE1 . PHE C 294 ? 0.2764 0.1856 0.4352 0.0055  0.0105  0.0226  294 PHE C CE1 
10817 C CE2 . PHE C 294 ? 0.3021 0.2066 0.4564 0.0042  0.0079  0.0214  294 PHE C CE2 
10818 C CZ  . PHE C 294 ? 0.2902 0.1935 0.4390 0.0049  0.0093  0.0212  294 PHE C CZ  
10819 N N   . TRP C 295 ? 0.2666 0.2078 0.5099 0.0017  0.0064  0.0324  295 TRP C N   
10820 C CA  . TRP C 295 ? 0.2778 0.2265 0.5413 -0.0005 0.0021  0.0336  295 TRP C CA  
10821 C C   . TRP C 295 ? 0.2779 0.2334 0.5548 0.0009  0.0030  0.0373  295 TRP C C   
10822 O O   . TRP C 295 ? 0.3158 0.2687 0.5895 0.0040  0.0108  0.0406  295 TRP C O   
10823 C CB  . TRP C 295 ? 0.2845 0.2308 0.5584 -0.0018 0.0067  0.0372  295 TRP C CB  
10824 C CG  . TRP C 295 ? 0.2852 0.2259 0.5513 -0.0035 0.0038  0.0341  295 TRP C CG  
10825 C CD1 . TRP C 295 ? 0.3005 0.2338 0.5475 -0.0024 0.0048  0.0315  295 TRP C CD1 
10826 C CD2 . TRP C 295 ? 0.2912 0.2326 0.5694 -0.0066 -0.0005 0.0336  295 TRP C CD2 
10827 N NE1 . TRP C 295 ? 0.3142 0.2441 0.5609 -0.0041 0.0015  0.0295  295 TRP C NE1 
10828 C CE2 . TRP C 295 ? 0.2973 0.2314 0.5623 -0.0067 -0.0016 0.0306  295 TRP C CE2 
10829 C CE3 . TRP C 295 ? 0.2883 0.2355 0.5881 -0.0095 -0.0039 0.0354  295 TRP C CE3 
10830 C CZ2 . TRP C 295 ? 0.3054 0.2370 0.5771 -0.0091 -0.0054 0.0295  295 TRP C CZ2 
10831 C CZ3 . TRP C 295 ? 0.2817 0.2260 0.5881 -0.0125 -0.0078 0.0342  295 TRP C CZ3 
10832 C CH2 . TRP C 295 ? 0.2903 0.2266 0.5825 -0.0121 -0.0083 0.0312  295 TRP C CH2 
10833 N N   . GLY C 296 ? 0.2570 0.2205 0.5484 -0.0013 -0.0054 0.0365  296 GLY C N   
10834 C CA  . GLY C 296 ? 0.2698 0.2408 0.5755 -0.0001 -0.0067 0.0401  296 GLY C CA  
10835 C C   . GLY C 296 ? 0.2689 0.2475 0.5995 -0.0028 -0.0108 0.0428  296 GLY C C   
10836 O O   . GLY C 296 ? 0.2780 0.2565 0.6120 -0.0063 -0.0172 0.0397  296 GLY C O   
10837 N N   . TYR C 297 ? 0.2827 0.2677 0.6314 -0.0010 -0.0074 0.0486  297 TYR C N   
10838 C CA  . TYR C 297 ? 0.2696 0.2630 0.6460 -0.0035 -0.0102 0.0527  297 TYR C CA  
10839 C C   . TYR C 297 ? 0.2648 0.2662 0.6502 -0.0048 -0.0233 0.0512  297 TYR C C   
10840 O O   . TYR C 297 ? 0.2841 0.2867 0.6623 -0.0020 -0.0252 0.0512  297 TYR C O   
10841 C CB  . TYR C 297 ? 0.2713 0.2668 0.6627 -0.0003 0.0028  0.0604  297 TYR C CB  
10842 C CG  . TYR C 297 ? 0.2896 0.2759 0.6700 0.0005  0.0147  0.0617  297 TYR C CG  
10843 C CD1 . TYR C 297 ? 0.3065 0.2909 0.6933 -0.0033 0.0149  0.0621  297 TYR C CD1 
10844 C CD2 . TYR C 297 ? 0.3209 0.2987 0.6817 0.0049  0.0247  0.0620  297 TYR C CD2 
10845 C CE1 . TYR C 297 ? 0.3016 0.2764 0.6760 -0.0024 0.0250  0.0636  297 TYR C CE1 
10846 C CE2 . TYR C 297 ? 0.3256 0.2937 0.6731 0.0057  0.0343  0.0628  297 TYR C CE2 
10847 C CZ  . TYR C 297 ? 0.3115 0.2781 0.6653 0.0022  0.0345  0.0638  297 TYR C CZ  
10848 O OH  . TYR C 297 ? 0.2892 0.2456 0.6289 0.0034  0.0441  0.0655  297 TYR C OH  
10849 N N   . SER C 298 ? 0.2565 0.2623 0.6571 -0.0094 -0.0329 0.0499  298 SER C N   
10850 C CA  . SER C 298 ? 0.2404 0.2528 0.6493 -0.0112 -0.0469 0.0483  298 SER C CA  
10851 C C   . SER C 298 ? 0.2320 0.2543 0.6638 -0.0089 -0.0460 0.0554  298 SER C C   
10852 O O   . SER C 298 ? 0.2394 0.2655 0.6700 -0.0076 -0.0544 0.0551  298 SER C O   
10853 C CB  . SER C 298 ? 0.2282 0.2415 0.6474 -0.0169 -0.0577 0.0447  298 SER C CB  
10854 O OG  . SER C 298 ? 0.2030 0.2231 0.6521 -0.0192 -0.0557 0.0508  298 SER C OG  
10855 N N   . ASP C 299 ? 0.2339 0.2601 0.6859 -0.0078 -0.0353 0.0622  299 ASP C N   
10856 C CA  . ASP C 299 ? 0.2333 0.2705 0.7130 -0.0059 -0.0347 0.0694  299 ASP C CA  
10857 C C   . ASP C 299 ? 0.2404 0.2786 0.7343 -0.0034 -0.0179 0.0763  299 ASP C C   
10858 O O   . ASP C 299 ? 0.2489 0.2792 0.7316 -0.0041 -0.0091 0.0753  299 ASP C O   
10859 C CB  . ASP C 299 ? 0.2307 0.2769 0.7344 -0.0110 -0.0494 0.0698  299 ASP C CB  
10860 C CG  . ASP C 299 ? 0.2497 0.2939 0.7618 -0.0169 -0.0514 0.0680  299 ASP C CG  
10861 O OD1 . ASP C 299 ? 0.2491 0.2951 0.7775 -0.0172 -0.0399 0.0735  299 ASP C OD1 
10862 O OD2 . ASP C 299 ? 0.2397 0.2797 0.7413 -0.0211 -0.0638 0.0610  299 ASP C OD2 
10863 N N   . LEU C 300 ? 0.2599 0.3080 0.7796 -0.0006 -0.0140 0.0835  300 LEU C N   
10864 C CA  . LEU C 300 ? 0.2791 0.3302 0.8170 0.0023  0.0022  0.0911  300 LEU C CA  
10865 C C   . LEU C 300 ? 0.2841 0.3349 0.8345 -0.0025 0.0069  0.0932  300 LEU C C   
10866 O O   . LEU C 300 ? 0.2960 0.3445 0.8501 0.0000  0.0229  0.0982  300 LEU C O   
10867 C CB  . LEU C 300 ? 0.3052 0.3703 0.8758 0.0046  0.0001  0.0981  300 LEU C CB  
10868 C CG  . LEU C 300 ? 0.3384 0.4092 0.9331 0.0085  0.0174  0.1069  300 LEU C CG  
10869 C CD1 . LEU C 300 ? 0.3669 0.4247 0.9349 0.0142  0.0350  0.1064  300 LEU C CD1 
10870 C CD2 . LEU C 300 ? 0.3278 0.4116 0.9510 0.0127  0.0159  0.1133  300 LEU C CD2 
10871 N N   . ASN C 301 ? 0.2747 0.3276 0.8329 -0.0093 -0.0064 0.0899  301 ASN C N   
10872 C CA  . ASN C 301 ? 0.2704 0.3235 0.8443 -0.0142 -0.0025 0.0928  301 ASN C CA  
10873 C C   . ASN C 301 ? 0.2881 0.3272 0.8335 -0.0161 -0.0007 0.0869  301 ASN C C   
10874 O O   . ASN C 301 ? 0.3059 0.3425 0.8597 -0.0201 0.0027  0.0888  301 ASN C O   
10875 C CB  . ASN C 301 ? 0.2693 0.3328 0.8726 -0.0205 -0.0178 0.0935  301 ASN C CB  
10876 C CG  . ASN C 301 ? 0.2610 0.3394 0.8971 -0.0183 -0.0177 0.1011  301 ASN C CG  
10877 O OD1 . ASN C 301 ? 0.2520 0.3340 0.8993 -0.0135 -0.0018 0.1082  301 ASN C OD1 
10878 N ND2 . ASN C 301 ? 0.2637 0.3506 0.9154 -0.0215 -0.0352 0.0997  301 ASN C ND2 
10879 N N   . ASP C 302 ? 0.2868 0.3170 0.7996 -0.0134 -0.0028 0.0801  302 ASP C N   
10880 C CA  . ASP C 302 ? 0.3029 0.3212 0.7903 -0.0155 -0.0043 0.0738  302 ASP C CA  
10881 C C   . ASP C 302 ? 0.3028 0.3123 0.7768 -0.0123 0.0124  0.0771  302 ASP C C   
10882 O O   . ASP C 302 ? 0.3215 0.3270 0.7801 -0.0069 0.0214  0.0778  302 ASP C O   
10883 C CB  . ASP C 302 ? 0.3129 0.3254 0.7716 -0.0139 -0.0127 0.0656  302 ASP C CB  
10884 C CG  . ASP C 302 ? 0.3001 0.3025 0.7368 -0.0165 -0.0173 0.0585  302 ASP C CG  
10885 O OD1 . ASP C 302 ? 0.2934 0.2911 0.7332 -0.0187 -0.0121 0.0600  302 ASP C OD1 
10886 O OD2 . ASP C 302 ? 0.2859 0.2855 0.7035 -0.0160 -0.0257 0.0517  302 ASP C OD2 
10887 N N   . LYS C 303 ? 0.2980 0.3028 0.7755 -0.0157 0.0157  0.0785  303 LYS C N   
10888 C CA  . LYS C 303 ? 0.3023 0.2974 0.7651 -0.0130 0.0305  0.0817  303 LYS C CA  
10889 C C   . LYS C 303 ? 0.2781 0.2610 0.7105 -0.0133 0.0268  0.0747  303 LYS C C   
10890 O O   . LYS C 303 ? 0.2814 0.2549 0.6981 -0.0112 0.0370  0.0766  303 LYS C O   
10891 C CB  . LYS C 303 ? 0.3258 0.3237 0.8134 -0.0165 0.0372  0.0892  303 LYS C CB  
10892 C CG  . LYS C 303 ? 0.3297 0.3401 0.8493 -0.0155 0.0439  0.0975  303 LYS C CG  
10893 C CD  . LYS C 303 ? 0.3410 0.3492 0.8529 -0.0084 0.0612  0.1026  303 LYS C CD  
10894 C CE  . LYS C 303 ? 0.3403 0.3590 0.8848 -0.0076 0.0720  0.1123  303 LYS C CE  
10895 N NZ  . LYS C 303 ? 0.3362 0.3682 0.9012 -0.0071 0.0622  0.1120  303 LYS C NZ  
10896 N N   . TYR C 304 ? 0.2635 0.2463 0.6876 -0.0157 0.0126  0.0669  304 TYR C N   
10897 C CA  . TYR C 304 ? 0.2697 0.2423 0.6713 -0.0167 0.0084  0.0607  304 TYR C CA  
10898 C C   . TYR C 304 ? 0.2733 0.2430 0.6500 -0.0137 0.0040  0.0541  304 TYR C C   
10899 O O   . TYR C 304 ? 0.2776 0.2388 0.6321 -0.0109 0.0097  0.0527  304 TYR C O   
10900 C CB  . TYR C 304 ? 0.2680 0.2415 0.6824 -0.0224 -0.0030 0.0575  304 TYR C CB  
10901 C CG  . TYR C 304 ? 0.2793 0.2542 0.7174 -0.0257 0.0031  0.0650  304 TYR C CG  
10902 C CD1 . TYR C 304 ? 0.2913 0.2570 0.7219 -0.0254 0.0130  0.0687  304 TYR C CD1 
10903 C CD2 . TYR C 304 ? 0.2988 0.2847 0.7677 -0.0289 -0.0002 0.0693  304 TYR C CD2 
10904 C CE1 . TYR C 304 ? 0.2836 0.2505 0.7360 -0.0284 0.0198  0.0765  304 TYR C CE1 
10905 C CE2 . TYR C 304 ? 0.2899 0.2779 0.7829 -0.0322 0.0060  0.0768  304 TYR C CE2 
10906 C CZ  . TYR C 304 ? 0.2953 0.2735 0.7795 -0.0320 0.0166  0.0806  304 TYR C CZ  
10907 O OH  . TYR C 304 ? 0.3130 0.2931 0.8208 -0.0353 0.0239  0.0889  304 TYR C OH  
10908 N N   . GLY C 305 ? 0.2619 0.2384 0.6426 -0.0145 -0.0065 0.0503  305 GLY C N   
10909 C CA  . GLY C 305 ? 0.2464 0.2208 0.6053 -0.0121 -0.0111 0.0445  305 GLY C CA  
10910 C C   . GLY C 305 ? 0.2441 0.2129 0.5883 -0.0141 -0.0193 0.0369  305 GLY C C   
10911 O O   . GLY C 305 ? 0.2333 0.1990 0.5838 -0.0172 -0.0218 0.0360  305 GLY C O   
10912 N N   . THR C 306 ? 0.2419 0.2095 0.5676 -0.0123 -0.0233 0.0318  306 THR C N   
10913 C CA  . THR C 306 ? 0.2503 0.2131 0.5600 -0.0130 -0.0295 0.0246  306 THR C CA  
10914 C C   . THR C 306 ? 0.2631 0.2222 0.5509 -0.0098 -0.0256 0.0226  306 THR C C   
10915 O O   . THR C 306 ? 0.2889 0.2503 0.5733 -0.0075 -0.0224 0.0249  306 THR C O   
10916 C CB  . THR C 306 ? 0.2441 0.2108 0.5575 -0.0153 -0.0418 0.0195  306 THR C CB  
10917 O OG1 . THR C 306 ? 0.2274 0.1990 0.5363 -0.0135 -0.0442 0.0196  306 THR C OG1 
10918 C CG2 . THR C 306 ? 0.2294 0.1996 0.5657 -0.0192 -0.0474 0.0211  306 THR C CG2 
10919 N N   . PRO C 307 ? 0.2810 0.2340 0.5544 -0.0094 -0.0256 0.0186  307 PRO C N   
10920 C CA  . PRO C 307 ? 0.2791 0.2289 0.5337 -0.0069 -0.0222 0.0170  307 PRO C CA  
10921 C C   . PRO C 307 ? 0.2711 0.2250 0.5172 -0.0062 -0.0273 0.0134  307 PRO C C   
10922 O O   . PRO C 307 ? 0.2734 0.2303 0.5213 -0.0075 -0.0350 0.0095  307 PRO C O   
10923 C CB  . PRO C 307 ? 0.2843 0.2278 0.5301 -0.0070 -0.0226 0.0137  307 PRO C CB  
10924 C CG  . PRO C 307 ? 0.2838 0.2279 0.5414 -0.0097 -0.0291 0.0111  307 PRO C CG  
10925 C CD  . PRO C 307 ? 0.2925 0.2412 0.5685 -0.0114 -0.0289 0.0158  307 PRO C CD  
10926 N N   . ARG C 308 ? 0.2644 0.2172 0.4999 -0.0041 -0.0229 0.0148  308 ARG C N   
10927 C CA  . ARG C 308 ? 0.2694 0.2246 0.4945 -0.0036 -0.0266 0.0118  308 ARG C CA  
10928 C C   . ARG C 308 ? 0.2889 0.2409 0.5001 -0.0034 -0.0272 0.0073  308 ARG C C   
10929 O O   . ARG C 308 ? 0.2807 0.2281 0.4897 -0.0033 -0.0244 0.0071  308 ARG C O   
10930 C CB  . ARG C 308 ? 0.2701 0.2254 0.4925 -0.0017 -0.0219 0.0159  308 ARG C CB  
10931 C CG  . ARG C 308 ? 0.2777 0.2372 0.5158 -0.0012 -0.0212 0.0206  308 ARG C CG  
10932 C CD  . ARG C 308 ? 0.2697 0.2275 0.5043 0.0014  -0.0154 0.0245  308 ARG C CD  
10933 N NE  . ARG C 308 ? 0.2649 0.2280 0.5160 0.0024  -0.0153 0.0291  308 ARG C NE  
10934 C CZ  . ARG C 308 ? 0.2805 0.2424 0.5371 0.0052  -0.0078 0.0340  308 ARG C CZ  
10935 N NH1 . ARG C 308 ? 0.2895 0.2435 0.5355 0.0071  0.0007  0.0349  308 ARG C NH1 
10936 N NH2 . ARG C 308 ? 0.2690 0.2373 0.5423 0.0063  -0.0091 0.0380  308 ARG C NH2 
10937 N N   . PRO C 309 ? 0.2967 0.2513 0.4988 -0.0033 -0.0306 0.0040  309 PRO C N   
10938 C CA  . PRO C 309 ? 0.2883 0.2416 0.4798 -0.0030 -0.0311 -0.0003 309 PRO C CA  
10939 C C   . PRO C 309 ? 0.3054 0.2542 0.4905 -0.0023 -0.0258 0.0013  309 PRO C C   
10940 O O   . PRO C 309 ? 0.2979 0.2446 0.4801 -0.0021 -0.0262 -0.0011 309 PRO C O   
10941 C CB  . PRO C 309 ? 0.2840 0.2410 0.4677 -0.0029 -0.0337 -0.0021 309 PRO C CB  
10942 C CG  . PRO C 309 ? 0.3039 0.2641 0.4956 -0.0035 -0.0385 -0.0011 309 PRO C CG  
10943 C CD  . PRO C 309 ? 0.2875 0.2467 0.4901 -0.0034 -0.0349 0.0042  309 PRO C CD  
10944 N N   . VAL C 310 ? 0.2845 0.2308 0.4678 -0.0018 -0.0214 0.0055  310 VAL C N   
10945 C CA  . VAL C 310 ? 0.2825 0.2228 0.4584 -0.0012 -0.0170 0.0071  310 VAL C CA  
10946 C C   . VAL C 310 ? 0.3029 0.2389 0.4812 -0.0011 -0.0161 0.0072  310 VAL C C   
10947 O O   . VAL C 310 ? 0.3253 0.2573 0.4964 -0.0008 -0.0157 0.0064  310 VAL C O   
10948 C CB  . VAL C 310 ? 0.2853 0.2222 0.4598 -0.0001 -0.0120 0.0114  310 VAL C CB  
10949 C CG1 . VAL C 310 ? 0.2889 0.2261 0.4748 0.0006  -0.0092 0.0151  310 VAL C CG1 
10950 C CG2 . VAL C 310 ? 0.2999 0.2288 0.4637 0.0004  -0.0081 0.0124  310 VAL C CG2 
10951 N N   . TRP C 311 ? 0.3024 0.2390 0.4914 -0.0014 -0.0161 0.0086  311 TRP C N   
10952 C CA  . TRP C 311 ? 0.3154 0.2471 0.5070 -0.0014 -0.0148 0.0096  311 TRP C CA  
10953 C C   . TRP C 311 ? 0.2842 0.2152 0.4717 -0.0014 -0.0188 0.0054  311 TRP C C   
10954 O O   . TRP C 311 ? 0.2747 0.2000 0.4575 -0.0007 -0.0175 0.0064  311 TRP C O   
10955 C CB  . TRP C 311 ? 0.3246 0.2586 0.5310 -0.0026 -0.0156 0.0113  311 TRP C CB  
10956 C CG  . TRP C 311 ? 0.3117 0.2404 0.5228 -0.0029 -0.0135 0.0135  311 TRP C CG  
10957 C CD1 . TRP C 311 ? 0.3000 0.2280 0.5173 -0.0041 -0.0178 0.0110  311 TRP C CD1 
10958 C CD2 . TRP C 311 ? 0.3435 0.2659 0.5530 -0.0021 -0.0063 0.0190  311 TRP C CD2 
10959 N NE1 . TRP C 311 ? 0.3117 0.2337 0.5324 -0.0043 -0.0140 0.0150  311 TRP C NE1 
10960 C CE2 . TRP C 311 ? 0.3389 0.2574 0.5544 -0.0030 -0.0067 0.0201  311 TRP C CE2 
10961 C CE3 . TRP C 311 ? 0.3280 0.2465 0.5306 -0.0004 0.0007  0.0229  311 TRP C CE3 
10962 C CZ2 . TRP C 311 ? 0.3356 0.2472 0.5501 -0.0025 -0.0002 0.0255  311 TRP C CZ2 
10963 C CZ3 . TRP C 311 ? 0.3338 0.2450 0.5345 0.0004  0.0074  0.0277  311 TRP C CZ3 
10964 C CH2 . TRP C 311 ? 0.3416 0.2497 0.5482 -0.0007 0.0071  0.0293  311 TRP C CH2 
10965 N N   . PHE C 312 ? 0.3032 0.2395 0.4926 -0.0018 -0.0236 0.0009  312 PHE C N   
10966 C CA  . PHE C 312 ? 0.3321 0.2687 0.5196 -0.0012 -0.0271 -0.0037 312 PHE C CA  
10967 C C   . PHE C 312 ? 0.3247 0.2617 0.5026 -0.0003 -0.0263 -0.0045 312 PHE C C   
10968 O O   . PHE C 312 ? 0.3079 0.2425 0.4840 0.0007  -0.0271 -0.0054 312 PHE C O   
10969 C CB  . PHE C 312 ? 0.3257 0.2667 0.5176 -0.0017 -0.0318 -0.0081 312 PHE C CB  
10970 C CG  . PHE C 312 ? 0.3476 0.2873 0.5508 -0.0032 -0.0336 -0.0069 312 PHE C CG  
10971 C CD1 . PHE C 312 ? 0.3925 0.3274 0.6019 -0.0035 -0.0347 -0.0074 312 PHE C CD1 
10972 C CD2 . PHE C 312 ? 0.3462 0.2894 0.5554 -0.0044 -0.0344 -0.0047 312 PHE C CD2 
10973 C CE1 . PHE C 312 ? 0.3847 0.3184 0.6063 -0.0055 -0.0362 -0.0056 312 PHE C CE1 
10974 C CE2 . PHE C 312 ? 0.3476 0.2906 0.5698 -0.0062 -0.0363 -0.0031 312 PHE C CE2 
10975 C CZ  . PHE C 312 ? 0.3401 0.2783 0.5688 -0.0070 -0.0371 -0.0034 312 PHE C CZ  
10976 N N   . ALA C 313 ? 0.3336 0.2733 0.5064 -0.0007 -0.0248 -0.0034 313 ALA C N   
10977 C CA  . ALA C 313 ? 0.3535 0.2940 0.5187 -0.0006 -0.0243 -0.0040 313 ALA C CA  
10978 C C   . ALA C 313 ? 0.3339 0.2674 0.4945 -0.0004 -0.0227 -0.0012 313 ALA C C   
10979 O O   . ALA C 313 ? 0.3306 0.2636 0.4885 0.0000  -0.0244 -0.0023 313 ALA C O   
10980 C CB  . ALA C 313 ? 0.3686 0.3122 0.5295 -0.0015 -0.0232 -0.0031 313 ALA C CB  
10981 N N   . MET C 314 ? 0.3342 0.2622 0.4941 -0.0004 -0.0193 0.0026  314 MET C N   
10982 C CA  . MET C 314 ? 0.3380 0.2574 0.4907 0.0002  -0.0172 0.0055  314 MET C CA  
10983 C C   . MET C 314 ? 0.3368 0.2531 0.4915 0.0010  -0.0194 0.0052  314 MET C C   
10984 O O   . MET C 314 ? 0.3660 0.2789 0.5148 0.0015  -0.0214 0.0052  314 MET C O   
10985 C CB  . MET C 314 ? 0.3266 0.2408 0.4783 0.0006  -0.0118 0.0096  314 MET C CB  
10986 C CG  . MET C 314 ? 0.3500 0.2643 0.4969 0.0004  -0.0094 0.0105  314 MET C CG  
10987 S SD  . MET C 314 ? 0.3894 0.2962 0.5212 0.0001  -0.0098 0.0102  314 MET C SD  
10988 C CE  . MET C 314 ? 0.3840 0.2793 0.5090 0.0018  -0.0054 0.0139  314 MET C CE  
10989 N N   . ARG C 315 ? 0.3310 0.2482 0.4947 0.0011  -0.0195 0.0052  315 ARG C N   
10990 C CA  . ARG C 315 ? 0.3306 0.2443 0.4971 0.0019  -0.0217 0.0050  315 ARG C CA  
10991 C C   . ARG C 315 ? 0.3126 0.2296 0.4780 0.0029  -0.0261 0.0012  315 ARG C C   
10992 O O   . ARG C 315 ? 0.2965 0.2089 0.4588 0.0040  -0.0280 0.0022  315 ARG C O   
10993 C CB  . ARG C 315 ? 0.3396 0.2556 0.5178 0.0013  -0.0227 0.0037  315 ARG C CB  
10994 C CG  . ARG C 315 ? 0.3549 0.2660 0.5367 0.0022  -0.0248 0.0037  315 ARG C CG  
10995 C CD  . ARG C 315 ? 0.3659 0.2789 0.5590 0.0014  -0.0272 0.0010  315 ARG C CD  
10996 N NE  . ARG C 315 ? 0.3932 0.3131 0.5874 0.0017  -0.0308 -0.0050 315 ARG C NE  
10997 C CZ  . ARG C 315 ? 0.3906 0.3126 0.5921 0.0009  -0.0338 -0.0087 315 ARG C CZ  
10998 N NH1 . ARG C 315 ? 0.4027 0.3210 0.6131 -0.0008 -0.0342 -0.0067 315 ARG C NH1 
10999 N NH2 . ARG C 315 ? 0.3817 0.3089 0.5812 0.0016  -0.0364 -0.0140 315 ARG C NH2 
11000 N N   . ASP C 316 ? 0.3174 0.2423 0.4862 0.0028  -0.0279 -0.0029 316 ASP C N   
11001 C CA  . ASP C 316 ? 0.3423 0.2715 0.5121 0.0041  -0.0310 -0.0064 316 ASP C CA  
11002 C C   . ASP C 316 ? 0.3323 0.2609 0.4952 0.0037  -0.0315 -0.0047 316 ASP C C   
11003 O O   . ASP C 316 ? 0.3325 0.2610 0.4965 0.0050  -0.0344 -0.0051 316 ASP C O   
11004 C CB  . ASP C 316 ? 0.3576 0.2949 0.5307 0.0042  -0.0316 -0.0109 316 ASP C CB  
11005 C CG  . ASP C 316 ? 0.3826 0.3199 0.5617 0.0047  -0.0328 -0.0140 316 ASP C CG  
11006 O OD1 . ASP C 316 ? 0.3759 0.3075 0.5592 0.0047  -0.0334 -0.0127 316 ASP C OD1 
11007 O OD2 . ASP C 316 ? 0.4769 0.4194 0.6559 0.0047  -0.0332 -0.0175 316 ASP C OD2 
11008 N N   . TYR C 317 ? 0.3004 0.2279 0.4569 0.0020  -0.0293 -0.0026 317 TYR C N   
11009 C CA  . TYR C 317 ? 0.3163 0.2421 0.4659 0.0011  -0.0304 -0.0014 317 TYR C CA  
11010 C C   . TYR C 317 ? 0.3394 0.2560 0.4826 0.0018  -0.0321 0.0015  317 TYR C C   
11011 O O   . TYR C 317 ? 0.3797 0.2954 0.5199 0.0017  -0.0359 0.0016  317 TYR C O   
11012 C CB  . TYR C 317 ? 0.3285 0.2537 0.4723 -0.0007 -0.0276 -0.0001 317 TYR C CB  
11013 C CG  . TYR C 317 ? 0.3043 0.2274 0.4414 -0.0022 -0.0297 0.0005  317 TYR C CG  
11014 C CD1 . TYR C 317 ? 0.3265 0.2575 0.4678 -0.0035 -0.0316 -0.0013 317 TYR C CD1 
11015 C CD2 . TYR C 317 ? 0.3322 0.2450 0.4589 -0.0025 -0.0297 0.0029  317 TYR C CD2 
11016 C CE1 . TYR C 317 ? 0.3282 0.2575 0.4653 -0.0056 -0.0343 -0.0006 317 TYR C CE1 
11017 C CE2 . TYR C 317 ? 0.3615 0.2712 0.4816 -0.0043 -0.0328 0.0030  317 TYR C CE2 
11018 C CZ  . TYR C 317 ? 0.3271 0.2453 0.4535 -0.0061 -0.0355 0.0014  317 TYR C CZ  
11019 O OH  . TYR C 317 ? 0.3341 0.2489 0.4554 -0.0085 -0.0393 0.0017  317 TYR C OH  
11020 N N   . MET C 318 ? 0.3346 0.2441 0.4758 0.0026  -0.0295 0.0041  318 MET C N   
11021 C CA  . MET C 318 ? 0.3372 0.2364 0.4694 0.0034  -0.0303 0.0074  318 MET C CA  
11022 C C   . MET C 318 ? 0.3333 0.2318 0.4695 0.0051  -0.0351 0.0073  318 MET C C   
11023 O O   . MET C 318 ? 0.3365 0.2265 0.4644 0.0058  -0.0372 0.0102  318 MET C O   
11024 C CB  . MET C 318 ? 0.3687 0.2605 0.4977 0.0037  -0.0246 0.0111  318 MET C CB  
11025 C CG  . MET C 318 ? 0.3911 0.2808 0.5137 0.0028  -0.0197 0.0122  318 MET C CG  
11026 S SD  . MET C 318 ? 0.3820 0.2619 0.4996 0.0038  -0.0119 0.0174  318 MET C SD  
11027 C CE  . MET C 318 ? 0.3871 0.2758 0.5236 0.0034  -0.0106 0.0169  318 MET C CE  
11028 N N   . LYS C 319 ? 0.3415 0.2479 0.4895 0.0061  -0.0369 0.0040  319 LYS C N   
11029 C CA  . LYS C 319 ? 0.3755 0.2801 0.5282 0.0083  -0.0408 0.0041  319 LYS C CA  
11030 C C   . LYS C 319 ? 0.3875 0.2914 0.5364 0.0089  -0.0464 0.0050  319 LYS C C   
11031 O O   . LYS C 319 ? 0.3973 0.2953 0.5449 0.0107  -0.0499 0.0073  319 LYS C O   
11032 C CB  . LYS C 319 ? 0.4183 0.3309 0.5836 0.0097  -0.0414 -0.0004 319 LYS C CB  
11033 C CG  . LYS C 319 ? 0.4531 0.3645 0.6233 0.0092  -0.0382 -0.0013 319 LYS C CG  
11034 C CD  . LYS C 319 ? 0.5112 0.4294 0.6911 0.0107  -0.0395 -0.0068 319 LYS C CD  
11035 C CE  . LYS C 319 ? 0.5652 0.4829 0.7506 0.0100  -0.0381 -0.0091 319 LYS C CE  
11036 N NZ  . LYS C 319 ? 0.5619 0.4862 0.7524 0.0116  -0.0393 -0.0152 319 LYS C NZ  
11037 N N   . GLY C 320 ? 0.3574 0.2671 0.5052 0.0072  -0.0476 0.0034  320 GLY C N   
11038 C CA  . GLY C 320 ? 0.3632 0.2733 0.5095 0.0071  -0.0537 0.0042  320 GLY C CA  
11039 C C   . GLY C 320 ? 0.3945 0.3047 0.5333 0.0039  -0.0536 0.0042  320 GLY C C   
11040 O O   . GLY C 320 ? 0.3832 0.3017 0.5271 0.0024  -0.0508 0.0018  320 GLY C O   
11041 N N   . LEU C 321 ? 0.3808 0.2800 0.5056 0.0030  -0.0561 0.0069  321 LEU C N   
11042 C CA  . LEU C 321 ? 0.3769 0.2731 0.4924 0.0000  -0.0561 0.0067  321 LEU C CA  
11043 C C   . LEU C 321 ? 0.3893 0.2874 0.5059 -0.0016 -0.0644 0.0065  321 LEU C C   
11044 O O   . LEU C 321 ? 0.3603 0.2536 0.4742 -0.0004 -0.0707 0.0083  321 LEU C O   
11045 C CB  . LEU C 321 ? 0.3891 0.2708 0.4872 0.0003  -0.0528 0.0093  321 LEU C CB  
11046 C CG  . LEU C 321 ? 0.3989 0.2799 0.4978 0.0012  -0.0441 0.0099  321 LEU C CG  
11047 C CD1 . LEU C 321 ? 0.4196 0.2861 0.5014 0.0018  -0.0403 0.0130  321 LEU C CD1 
11048 C CD2 . LEU C 321 ? 0.3893 0.2787 0.4946 -0.0005 -0.0401 0.0075  321 LEU C CD2 
11049 N N   . ILE C 322 ? 0.3780 0.2824 0.4985 -0.0047 -0.0646 0.0048  322 ILE C N   
11050 C CA  . ILE C 322 ? 0.3777 0.2841 0.5005 -0.0073 -0.0723 0.0047  322 ILE C CA  
11051 C C   . ILE C 322 ? 0.3951 0.2880 0.4997 -0.0100 -0.0738 0.0052  322 ILE C C   
11052 O O   . ILE C 322 ? 0.4117 0.3036 0.5126 -0.0118 -0.0685 0.0042  322 ILE C O   
11053 C CB  . ILE C 322 ? 0.3657 0.2875 0.5056 -0.0093 -0.0714 0.0029  322 ILE C CB  
11054 C CG1 . ILE C 322 ? 0.3544 0.2882 0.5096 -0.0060 -0.0674 0.0016  322 ILE C CG1 
11055 C CG2 . ILE C 322 ? 0.3613 0.2867 0.5076 -0.0121 -0.0801 0.0035  322 ILE C CG2 
11056 C CD1 . ILE C 322 ? 0.3347 0.2829 0.5042 -0.0073 -0.0641 0.0000  322 ILE C CD1 
11057 N N   . ILE C 323 ? 0.4090 0.2909 0.5016 -0.0101 -0.0811 0.0066  323 ILE C N   
11058 C CA  . ILE C 323 ? 0.4119 0.2793 0.4853 -0.0125 -0.0835 0.0064  323 ILE C CA  
11059 C C   . ILE C 323 ? 0.4126 0.2830 0.4909 -0.0169 -0.0922 0.0052  323 ILE C C   
11060 O O   . ILE C 323 ? 0.4310 0.2940 0.4998 -0.0200 -0.0920 0.0038  323 ILE C O   
11061 C CB  . ILE C 323 ? 0.4294 0.2803 0.4827 -0.0101 -0.0863 0.0085  323 ILE C CB  
11062 C CG1 . ILE C 323 ? 0.4516 0.2954 0.4954 -0.0069 -0.0757 0.0099  323 ILE C CG1 
11063 C CG2 . ILE C 323 ? 0.4490 0.2851 0.4831 -0.0129 -0.0930 0.0076  323 ILE C CG2 
11064 C CD1 . ILE C 323 ? 0.4507 0.3028 0.5074 -0.0037 -0.0722 0.0115  323 ILE C CD1 
11065 N N   . SER C 324 ? 0.3911 0.2707 0.4835 -0.0172 -0.1003 0.0059  324 SER C N   
11066 C CA  . SER C 324 ? 0.3960 0.2821 0.4992 -0.0216 -0.1088 0.0054  324 SER C CA  
11067 C C   . SER C 324 ? 0.3924 0.2981 0.5221 -0.0204 -0.1093 0.0060  324 SER C C   
11068 O O   . SER C 324 ? 0.3696 0.2780 0.5036 -0.0160 -0.1086 0.0071  324 SER C O   
11069 C CB  . SER C 324 ? 0.4067 0.2803 0.4968 -0.0232 -0.1212 0.0061  324 SER C CB  
11070 O OG  . SER C 324 ? 0.4094 0.2636 0.4730 -0.0237 -0.1196 0.0051  324 SER C OG  
11071 N N   . PRO C 325 ? 0.3900 0.3092 0.5377 -0.0238 -0.1093 0.0055  325 PRO C N   
11072 C CA  . PRO C 325 ? 0.3912 0.3068 0.5349 -0.0293 -0.1098 0.0045  325 PRO C CA  
11073 C C   . PRO C 325 ? 0.3858 0.2970 0.5195 -0.0289 -0.0987 0.0033  325 PRO C C   
11074 O O   . PRO C 325 ? 0.3685 0.2849 0.5051 -0.0251 -0.0903 0.0032  325 PRO C O   
11075 C CB  . PRO C 325 ? 0.3742 0.3080 0.5436 -0.0325 -0.1115 0.0053  325 PRO C CB  
11076 C CG  . PRO C 325 ? 0.3645 0.3125 0.5502 -0.0274 -0.1063 0.0057  325 PRO C CG  
11077 C CD  . PRO C 325 ? 0.3805 0.3188 0.5536 -0.0224 -0.1080 0.0060  325 PRO C CD  
11078 N N   . LYS C 326 ? 0.3996 0.3017 0.5233 -0.0331 -0.0992 0.0024  326 LYS C N   
11079 C CA  . LYS C 326 ? 0.3984 0.2949 0.5122 -0.0326 -0.0896 0.0016  326 LYS C CA  
11080 C C   . LYS C 326 ? 0.3691 0.2785 0.4983 -0.0353 -0.0842 0.0020  326 LYS C C   
11081 O O   . LYS C 326 ? 0.3423 0.2588 0.4840 -0.0397 -0.0890 0.0027  326 LYS C O   
11082 C CB  . LYS C 326 ? 0.4379 0.3145 0.5294 -0.0346 -0.0927 0.0004  326 LYS C CB  
11083 C CG  . LYS C 326 ? 0.4575 0.3200 0.5303 -0.0311 -0.0955 0.0003  326 LYS C CG  
11084 C CD  . LYS C 326 ? 0.4812 0.3224 0.5292 -0.0322 -0.0978 -0.0013 326 LYS C CD  
11085 C CE  . LYS C 326 ? 0.5009 0.3293 0.5299 -0.0275 -0.0961 -0.0006 326 LYS C CE  
11086 N NZ  . LYS C 326 ? 0.5067 0.3404 0.5415 -0.0256 -0.1026 0.0012  326 LYS C NZ  
11087 N N   . ASN C 327 ? 0.3692 0.2810 0.4970 -0.0328 -0.0743 0.0020  327 ASN C N   
11088 C CA  . ASN C 327 ? 0.3916 0.3131 0.5299 -0.0350 -0.0686 0.0027  327 ASN C CA  
11089 C C   . ASN C 327 ? 0.3833 0.2959 0.5157 -0.0401 -0.0710 0.0029  327 ASN C C   
11090 O O   . ASN C 327 ? 0.3658 0.2626 0.4811 -0.0402 -0.0721 0.0019  327 ASN C O   
11091 C CB  . ASN C 327 ? 0.3978 0.3224 0.5343 -0.0311 -0.0591 0.0026  327 ASN C CB  
11092 C CG  . ASN C 327 ? 0.3928 0.3283 0.5396 -0.0327 -0.0534 0.0038  327 ASN C CG  
11093 O OD1 . ASN C 327 ? 0.3761 0.3249 0.5380 -0.0337 -0.0534 0.0044  327 ASN C OD1 
11094 N ND2 . ASN C 327 ? 0.3781 0.3080 0.5166 -0.0323 -0.0480 0.0042  327 ASN C ND2 
11095 N N   . LYS C 328 ? 0.3953 0.3183 0.5429 -0.0445 -0.0721 0.0044  328 LYS C N   
11096 C CA  . LYS C 328 ? 0.4020 0.3190 0.5487 -0.0503 -0.0745 0.0051  328 LYS C CA  
11097 C C   . LYS C 328 ? 0.3847 0.2902 0.5245 -0.0538 -0.0858 0.0037  328 LYS C C   
11098 O O   . LYS C 328 ? 0.3836 0.2761 0.5136 -0.0575 -0.0885 0.0030  328 LYS C O   
11099 C CB  . LYS C 328 ? 0.4106 0.3176 0.5445 -0.0496 -0.0675 0.0051  328 LYS C CB  
11100 C CG  . LYS C 328 ? 0.4044 0.3223 0.5443 -0.0465 -0.0576 0.0067  328 LYS C CG  
11101 C CD  . LYS C 328 ? 0.4085 0.3429 0.5671 -0.0493 -0.0553 0.0092  328 LYS C CD  
11102 C CE  . LYS C 328 ? 0.3860 0.3309 0.5489 -0.0460 -0.0464 0.0104  328 LYS C CE  
11103 N NZ  . LYS C 328 ? 0.4107 0.3475 0.5636 -0.0460 -0.0415 0.0116  328 LYS C NZ  
11104 N N   . SER C 329 ? 0.3782 0.2879 0.5231 -0.0526 -0.0926 0.0034  329 SER C N   
11105 C CA  . SER C 329 ? 0.3884 0.2886 0.5282 -0.0560 -0.1050 0.0024  329 SER C CA  
11106 C C   . SER C 329 ? 0.3854 0.2982 0.5478 -0.0621 -0.1115 0.0043  329 SER C C   
11107 O O   . SER C 329 ? 0.3663 0.2974 0.5495 -0.0619 -0.1065 0.0066  329 SER C O   
11108 C CB  . SER C 329 ? 0.3990 0.2968 0.5327 -0.0516 -0.1098 0.0018  329 SER C CB  
11109 O OG  . SER C 329 ? 0.3712 0.2875 0.5247 -0.0487 -0.1075 0.0034  329 SER C OG  
11110 N N   . ILE C 330 ? 0.4039 0.3062 0.5618 -0.0675 -0.1227 0.0034  330 ILE C N   
11111 C CA  . ILE C 330 ? 0.4204 0.3332 0.6005 -0.0742 -0.1305 0.0054  330 ILE C CA  
11112 C C   . ILE C 330 ? 0.4345 0.3471 0.6176 -0.0745 -0.1441 0.0050  330 ILE C C   
11113 O O   . ILE C 330 ? 0.4771 0.3726 0.6379 -0.0728 -0.1506 0.0025  330 ILE C O   
11114 C CB  . ILE C 330 ? 0.4294 0.3308 0.6048 -0.0813 -0.1332 0.0049  330 ILE C CB  
11115 C CG1 . ILE C 330 ? 0.4213 0.3221 0.5922 -0.0799 -0.1195 0.0057  330 ILE C CG1 
11116 C CG2 . ILE C 330 ? 0.4312 0.3441 0.6319 -0.0890 -0.1414 0.0074  330 ILE C CG2 
11117 C CD1 . ILE C 330 ? 0.4394 0.3264 0.6027 -0.0856 -0.1205 0.0051  330 ILE C CD1 
11118 N N   . HIS C 331 ? 0.4256 0.3573 0.6360 -0.0759 -0.1479 0.0078  331 HIS C N   
11119 C CA  . HIS C 331 ? 0.4184 0.3526 0.6347 -0.0750 -0.1603 0.0082  331 HIS C CA  
11120 C C   . HIS C 331 ? 0.4251 0.3726 0.6694 -0.0820 -0.1696 0.0109  331 HIS C C   
11121 O O   . HIS C 331 ? 0.4242 0.3905 0.6934 -0.0833 -0.1620 0.0139  331 HIS C O   
11122 C CB  . HIS C 331 ? 0.4065 0.3535 0.6309 -0.0671 -0.1538 0.0094  331 HIS C CB  
11123 C CG  . HIS C 331 ? 0.3997 0.3331 0.5981 -0.0606 -0.1484 0.0072  331 HIS C CG  
11124 N ND1 . HIS C 331 ? 0.3976 0.3301 0.5871 -0.0569 -0.1344 0.0063  331 HIS C ND1 
11125 C CD2 . HIS C 331 ? 0.4060 0.3261 0.5860 -0.0575 -0.1556 0.0061  331 HIS C CD2 
11126 C CE1 . HIS C 331 ? 0.3979 0.3173 0.5657 -0.0519 -0.1331 0.0048  331 HIS C CE1 
11127 N NE2 . HIS C 331 ? 0.4208 0.3325 0.5822 -0.0521 -0.1453 0.0048  331 HIS C NE2 
11128 N N   . THR C 332 ? 0.4491 0.3871 0.6897 -0.0863 -0.1861 0.0101  332 THR C N   
11129 C CA  . THR C 332 ? 0.4483 0.3999 0.7181 -0.0929 -0.1967 0.0130  332 THR C CA  
11130 C C   . THR C 332 ? 0.4787 0.4375 0.7590 -0.0897 -0.2083 0.0144  332 THR C C   
11131 O O   . THR C 332 ? 0.5101 0.4730 0.8061 -0.0949 -0.2230 0.0159  332 THR C O   
11132 C CB  . THR C 332 ? 0.4608 0.3969 0.7224 -0.1020 -0.2074 0.0112  332 THR C CB  
11133 O OG1 . THR C 332 ? 0.4973 0.4094 0.7262 -0.1003 -0.2172 0.0071  332 THR C OG1 
11134 C CG2 . THR C 332 ? 0.4462 0.3780 0.7034 -0.1053 -0.1955 0.0108  332 THR C CG2 
11135 N N   . ASN C 333 ? 0.5086 0.4707 0.7832 -0.0811 -0.2015 0.0144  333 ASN C N   
11136 C CA  . ASN C 333 ? 0.5190 0.4861 0.8011 -0.0771 -0.2118 0.0160  333 ASN C CA  
11137 C C   . ASN C 333 ? 0.4987 0.4874 0.8036 -0.0705 -0.1996 0.0184  333 ASN C C   
11138 O O   . ASN C 333 ? 0.4738 0.4639 0.7721 -0.0670 -0.1841 0.0174  333 ASN C O   
11139 C CB  . ASN C 333 ? 0.5649 0.5085 0.8111 -0.0733 -0.2179 0.0132  333 ASN C CB  
11140 C CG  . ASN C 333 ? 0.6398 0.5823 0.8901 -0.0729 -0.2357 0.0149  333 ASN C CG  
11141 O OD1 . ASN C 333 ? 0.6516 0.6063 0.9161 -0.0670 -0.2354 0.0175  333 ASN C OD1 
11142 N ND2 . ASN C 333 ? 0.7242 0.6528 0.9638 -0.0793 -0.2516 0.0135  333 ASN C ND2 
11143 N N   . THR C 334 ? 0.4863 0.4911 0.8177 -0.0686 -0.2068 0.0216  334 THR C N   
11144 C CA  . THR C 334 ? 0.4620 0.4854 0.8135 -0.0613 -0.1956 0.0234  334 THR C CA  
11145 C C   . THR C 334 ? 0.4859 0.4989 0.8163 -0.0528 -0.1934 0.0218  334 THR C C   
11146 O O   . THR C 334 ? 0.4673 0.4902 0.8054 -0.0464 -0.1815 0.0219  334 THR C O   
11147 C CB  . THR C 334 ? 0.4489 0.4943 0.8388 -0.0618 -0.2026 0.0275  334 THR C CB  
11148 O OG1 . THR C 334 ? 0.4671 0.5043 0.8518 -0.0611 -0.2203 0.0282  334 THR C OG1 
11149 C CG2 . THR C 334 ? 0.4572 0.5149 0.8718 -0.0705 -0.2038 0.0298  334 THR C CG2 
11150 N N   . LYS C 335 ? 0.5486 0.5410 0.8516 -0.0527 -0.2043 0.0205  335 LYS C N   
11151 C CA  . LYS C 335 ? 0.5872 0.5680 0.8684 -0.0453 -0.2014 0.0196  335 LYS C CA  
11152 C C   . LYS C 335 ? 0.6155 0.5778 0.8643 -0.0454 -0.1923 0.0162  335 LYS C C   
11153 O O   . LYS C 335 ? 0.7638 0.7100 0.9928 -0.0504 -0.1988 0.0145  335 LYS C O   
11154 C CB  . LYS C 335 ? 0.6538 0.6231 0.9243 -0.0442 -0.2185 0.0211  335 LYS C CB  
11155 C CG  . LYS C 335 ? 0.7181 0.7046 1.0203 -0.0430 -0.2296 0.0249  335 LYS C CG  
11156 C CD  . LYS C 335 ? 0.7899 0.7937 1.1142 -0.0351 -0.2194 0.0266  335 LYS C CD  
11157 C CE  . LYS C 335 ? 0.8098 0.8230 1.1551 -0.0312 -0.2318 0.0305  335 LYS C CE  
11158 N NZ  . LYS C 335 ? 0.8224 0.8448 1.1895 -0.0377 -0.2465 0.0328  335 LYS C NZ  
11159 N N   . ILE C 336 ? 0.5878 0.5525 0.8324 -0.0400 -0.1774 0.0152  336 ILE C N   
11160 C CA  . ILE C 336 ? 0.5976 0.5478 0.8160 -0.0396 -0.1672 0.0125  336 ILE C CA  
11161 C C   . ILE C 336 ? 0.5671 0.5037 0.7638 -0.0335 -0.1667 0.0124  336 ILE C C   
11162 O O   . ILE C 336 ? 0.5642 0.5090 0.7712 -0.0279 -0.1634 0.0136  336 ILE C O   
11163 C CB  . ILE C 336 ? 0.5809 0.5438 0.8107 -0.0386 -0.1512 0.0116  336 ILE C CB  
11164 C CG1 . ILE C 336 ? 0.5883 0.5651 0.8403 -0.0446 -0.1507 0.0126  336 ILE C CG1 
11165 C CG2 . ILE C 336 ? 0.5791 0.5280 0.7838 -0.0378 -0.1412 0.0092  336 ILE C CG2 
11166 C CD1 . ILE C 336 ? 0.6041 0.5696 0.8472 -0.0522 -0.1607 0.0121  336 ILE C CD1 
11167 N N   . PRO C 337 ? 0.5843 0.4993 0.7507 -0.0344 -0.1703 0.0112  337 PRO C N   
11168 C CA  . PRO C 337 ? 0.5513 0.4530 0.6961 -0.0287 -0.1667 0.0116  337 PRO C CA  
11169 C C   . PRO C 337 ? 0.5122 0.4205 0.6608 -0.0243 -0.1512 0.0109  337 PRO C C   
11170 O O   . PRO C 337 ? 0.4829 0.3941 0.6321 -0.0261 -0.1415 0.0091  337 PRO C O   
11171 C CB  . PRO C 337 ? 0.5810 0.4598 0.6939 -0.0313 -0.1693 0.0098  337 PRO C CB  
11172 C CG  . PRO C 337 ? 0.5966 0.4745 0.7141 -0.0381 -0.1824 0.0090  337 PRO C CG  
11173 C CD  . PRO C 337 ? 0.5798 0.4812 0.7314 -0.0407 -0.1790 0.0096  337 PRO C CD  
11174 N N   . LEU C 338 ? 0.4893 0.3994 0.6407 -0.0185 -0.1496 0.0126  338 LEU C N   
11175 C CA  . LEU C 338 ? 0.5041 0.4174 0.6561 -0.0143 -0.1363 0.0118  338 LEU C CA  
11176 C C   . LEU C 338 ? 0.4969 0.3926 0.6245 -0.0109 -0.1341 0.0130  338 LEU C C   
11177 O O   . LEU C 338 ? 0.4669 0.3548 0.5873 -0.0086 -0.1421 0.0155  338 LEU C O   
11178 C CB  . LEU C 338 ? 0.5071 0.4381 0.6855 -0.0105 -0.1347 0.0125  338 LEU C CB  
11179 C CG  . LEU C 338 ? 0.5061 0.4398 0.6867 -0.0054 -0.1237 0.0117  338 LEU C CG  
11180 C CD1 . LEU C 338 ? 0.5007 0.4413 0.6847 -0.0069 -0.1120 0.0089  338 LEU C CD1 
11181 C CD2 . LEU C 338 ? 0.5456 0.4919 0.7484 -0.0008 -0.1259 0.0126  338 LEU C CD2 
11182 N N   . GLU C 339 ? 0.4915 0.3811 0.6069 -0.0106 -0.1230 0.0115  339 GLU C N   
11183 C CA  . GLU C 339 ? 0.4848 0.3591 0.5791 -0.0076 -0.1184 0.0129  339 GLU C CA  
11184 C C   . GLU C 339 ? 0.4556 0.3363 0.5569 -0.0051 -0.1058 0.0119  339 GLU C C   
11185 O O   . GLU C 339 ? 0.4547 0.3414 0.5606 -0.0072 -0.0991 0.0096  339 GLU C O   
11186 C CB  . GLU C 339 ? 0.5100 0.3668 0.5785 -0.0102 -0.1186 0.0122  339 GLU C CB  
11187 C CG  . GLU C 339 ? 0.5424 0.3870 0.5963 -0.0119 -0.1318 0.0132  339 GLU C CG  
11188 C CD  . GLU C 339 ? 0.5964 0.4217 0.6223 -0.0139 -0.1311 0.0118  339 GLU C CD  
11189 O OE1 . GLU C 339 ? 0.5859 0.4122 0.6127 -0.0178 -0.1291 0.0089  339 GLU C OE1 
11190 O OE2 . GLU C 339 ? 0.5985 0.4069 0.6010 -0.0115 -0.1319 0.0137  339 GLU C OE2 
11191 N N   . LEU C 340 ? 0.4317 0.3105 0.5338 -0.0009 -0.1033 0.0139  340 LEU C N   
11192 C CA  . LEU C 340 ? 0.3961 0.2795 0.5044 0.0013  -0.0927 0.0130  340 LEU C CA  
11193 C C   . LEU C 340 ? 0.4187 0.2876 0.5103 0.0037  -0.0885 0.0159  340 LEU C C   
11194 O O   . LEU C 340 ? 0.4259 0.2839 0.5059 0.0052  -0.0943 0.0191  340 LEU C O   
11195 C CB  . LEU C 340 ? 0.3867 0.2837 0.5169 0.0042  -0.0931 0.0122  340 LEU C CB  
11196 C CG  . LEU C 340 ? 0.3846 0.2979 0.5342 0.0027  -0.0951 0.0098  340 LEU C CG  
11197 C CD1 . LEU C 340 ? 0.3573 0.2819 0.5266 0.0067  -0.0946 0.0091  340 LEU C CD1 
11198 C CD2 . LEU C 340 ? 0.3873 0.3064 0.5381 -0.0003 -0.0874 0.0071  340 LEU C CD2 
11199 N N   . TYR C 341 ? 0.4094 0.2789 0.5012 0.0041  -0.0784 0.0151  341 TYR C N   
11200 C CA  . TYR C 341 ? 0.4155 0.2754 0.4988 0.0064  -0.0726 0.0180  341 TYR C CA  
11201 C C   . TYR C 341 ? 0.4051 0.2749 0.5054 0.0080  -0.0668 0.0165  341 TYR C C   
11202 O O   . TYR C 341 ? 0.3875 0.2632 0.4929 0.0068  -0.0603 0.0142  341 TYR C O   
11203 C CB  . TYR C 341 ? 0.4302 0.2788 0.4956 0.0054  -0.0657 0.0190  341 TYR C CB  
11204 C CG  . TYR C 341 ? 0.4468 0.2830 0.5006 0.0077  -0.0607 0.0234  341 TYR C CG  
11205 C CD1 . TYR C 341 ? 0.4764 0.2981 0.5114 0.0088  -0.0651 0.0270  341 TYR C CD1 
11206 C CD2 . TYR C 341 ? 0.4441 0.2833 0.5064 0.0087  -0.0523 0.0243  341 TYR C CD2 
11207 C CE1 . TYR C 341 ? 0.4968 0.3068 0.5208 0.0109  -0.0598 0.0317  341 TYR C CE1 
11208 C CE2 . TYR C 341 ? 0.4639 0.2924 0.5177 0.0104  -0.0474 0.0289  341 TYR C CE2 
11209 C CZ  . TYR C 341 ? 0.4895 0.3034 0.5239 0.0116  -0.0506 0.0329  341 TYR C CZ  
11210 O OH  . TYR C 341 ? 0.5092 0.3122 0.5346 0.0133  -0.0449 0.0381  341 TYR C OH  
11211 N N   . ASN C 342 ? 0.4185 0.2882 0.5262 0.0109  -0.0695 0.0181  342 ASN C N   
11212 C CA  . ASN C 342 ? 0.4200 0.2980 0.5442 0.0127  -0.0661 0.0161  342 ASN C CA  
11213 C C   . ASN C 342 ? 0.4271 0.2962 0.5478 0.0140  -0.0610 0.0192  342 ASN C C   
11214 O O   . ASN C 342 ? 0.4624 0.3201 0.5730 0.0153  -0.0629 0.0238  342 ASN C O   
11215 C CB  . ASN C 342 ? 0.4030 0.2873 0.5404 0.0153  -0.0729 0.0154  342 ASN C CB  
11216 C CG  . ASN C 342 ? 0.3883 0.2829 0.5328 0.0141  -0.0779 0.0130  342 ASN C CG  
11217 O OD1 . ASN C 342 ? 0.4184 0.3128 0.5643 0.0150  -0.0861 0.0148  342 ASN C OD1 
11218 N ND2 . ASN C 342 ? 0.3739 0.2782 0.5246 0.0121  -0.0735 0.0094  342 ASN C ND2 
11219 N N   . ASP C 343 ? 0.4173 0.2915 0.5470 0.0135  -0.0549 0.0170  343 ASP C N   
11220 C CA  . ASP C 343 ? 0.4440 0.3117 0.5756 0.0144  -0.0509 0.0196  343 ASP C CA  
11221 C C   . ASP C 343 ? 0.4154 0.2838 0.5578 0.0174  -0.0556 0.0193  343 ASP C C   
11222 O O   . ASP C 343 ? 0.4046 0.2791 0.5532 0.0190  -0.0613 0.0172  343 ASP C O   
11223 C CB  . ASP C 343 ? 0.4716 0.3436 0.6087 0.0125  -0.0438 0.0177  343 ASP C CB  
11224 C CG  . ASP C 343 ? 0.4741 0.3564 0.6269 0.0128  -0.0437 0.0125  343 ASP C CG  
11225 O OD1 . ASP C 343 ? 0.4655 0.3513 0.6264 0.0150  -0.0480 0.0101  343 ASP C OD1 
11226 O OD2 . ASP C 343 ? 0.5292 0.4151 0.6858 0.0110  -0.0392 0.0108  343 ASP C OD2 
11227 N N   . LYS C 344 ? 0.4452 0.3073 0.5912 0.0181  -0.0529 0.0216  344 LYS C N   
11228 C CA  . LYS C 344 ? 0.4815 0.3395 0.6343 0.0212  -0.0573 0.0230  344 LYS C CA  
11229 C C   . LYS C 344 ? 0.4308 0.2991 0.6002 0.0230  -0.0590 0.0167  344 LYS C C   
11230 O O   . LYS C 344 ? 0.4067 0.2736 0.5834 0.0263  -0.0633 0.0166  344 LYS C O   
11231 C CB  . LYS C 344 ? 0.5534 0.3997 0.7038 0.0209  -0.0536 0.0283  344 LYS C CB  
11232 C CG  . LYS C 344 ? 0.6250 0.4740 0.7853 0.0188  -0.0478 0.0260  344 LYS C CG  
11233 C CD  . LYS C 344 ? 0.7678 0.6077 0.9213 0.0165  -0.0412 0.0322  344 LYS C CD  
11234 C CE  . LYS C 344 ? 0.8377 0.6810 1.0034 0.0140  -0.0365 0.0303  344 LYS C CE  
11235 N NZ  . LYS C 344 ? 0.8323 0.6745 1.0110 0.0153  -0.0402 0.0278  344 LYS C NZ  
11236 N N   . ASP C 345 ? 0.4054 0.2833 0.5796 0.0212  -0.0557 0.0115  345 ASP C N   
11237 C CA  . ASP C 345 ? 0.3921 0.2791 0.5794 0.0230  -0.0561 0.0051  345 ASP C CA  
11238 C C   . ASP C 345 ? 0.3658 0.2624 0.5576 0.0250  -0.0598 0.0023  345 ASP C C   
11239 O O   . ASP C 345 ? 0.3565 0.2589 0.5591 0.0278  -0.0603 -0.0021 345 ASP C O   
11240 C CB  . ASP C 345 ? 0.3878 0.2800 0.5770 0.0203  -0.0512 0.0011  345 ASP C CB  
11241 C CG  . ASP C 345 ? 0.3849 0.2699 0.5760 0.0185  -0.0482 0.0027  345 ASP C CG  
11242 O OD1 . ASP C 345 ? 0.3789 0.2554 0.5724 0.0200  -0.0498 0.0054  345 ASP C OD1 
11243 O OD2 . ASP C 345 ? 0.3741 0.2620 0.5649 0.0158  -0.0447 0.0015  345 ASP C OD2 
11244 N N   . VAL C 346 ? 0.3445 0.2428 0.5284 0.0233  -0.0617 0.0047  346 VAL C N   
11245 C CA  . VAL C 346 ? 0.3456 0.2539 0.5356 0.0243  -0.0654 0.0028  346 VAL C CA  
11246 C C   . VAL C 346 ? 0.3520 0.2585 0.5487 0.0284  -0.0719 0.0050  346 VAL C C   
11247 O O   . VAL C 346 ? 0.3558 0.2529 0.5438 0.0285  -0.0763 0.0102  346 VAL C O   
11248 C CB  . VAL C 346 ? 0.3377 0.2465 0.5171 0.0208  -0.0665 0.0049  346 VAL C CB  
11249 C CG1 . VAL C 346 ? 0.3250 0.2437 0.5121 0.0212  -0.0713 0.0039  346 VAL C CG1 
11250 C CG2 . VAL C 346 ? 0.3267 0.2373 0.5002 0.0173  -0.0602 0.0032  346 VAL C CG2 
11251 N N   . LYS C 347 ? 0.3571 0.2724 0.5684 0.0319  -0.0726 0.0012  347 LYS C N   
11252 C CA  . LYS C 347 ? 0.3785 0.2930 0.5989 0.0365  -0.0786 0.0031  347 LYS C CA  
11253 C C   . LYS C 347 ? 0.3788 0.3059 0.6102 0.0376  -0.0822 0.0022  347 LYS C C   
11254 O O   . LYS C 347 ? 0.3786 0.3061 0.6178 0.0411  -0.0886 0.0048  347 LYS C O   
11255 C CB  . LYS C 347 ? 0.3749 0.2882 0.6065 0.0411  -0.0766 -0.0003 347 LYS C CB  
11256 C CG  . LYS C 347 ? 0.4178 0.3185 0.6414 0.0397  -0.0739 0.0010  347 LYS C CG  
11257 C CD  . LYS C 347 ? 0.4436 0.3314 0.6559 0.0387  -0.0776 0.0084  347 LYS C CD  
11258 C CE  . LYS C 347 ? 0.4918 0.3693 0.6985 0.0366  -0.0730 0.0095  347 LYS C CE  
11259 N NZ  . LYS C 347 ? 0.5150 0.3795 0.7093 0.0352  -0.0743 0.0170  347 LYS C NZ  
11260 N N   . LYS C 348 ? 0.3794 0.3168 0.6121 0.0347  -0.0781 -0.0010 348 LYS C N   
11261 C CA  . LYS C 348 ? 0.3593 0.3097 0.6038 0.0350  -0.0805 -0.0015 348 LYS C CA  
11262 C C   . LYS C 348 ? 0.3360 0.2921 0.5744 0.0297  -0.0774 -0.0024 348 LYS C C   
11263 O O   . LYS C 348 ? 0.3221 0.2774 0.5535 0.0275  -0.0709 -0.0051 348 LYS C O   
11264 C CB  . LYS C 348 ? 0.3529 0.3130 0.6145 0.0401  -0.0764 -0.0061 348 LYS C CB  
11265 C CG  . LYS C 348 ? 0.3716 0.3469 0.6488 0.0408  -0.0777 -0.0062 348 LYS C CG  
11266 C CD  . LYS C 348 ? 0.3741 0.3586 0.6699 0.0472  -0.0742 -0.0096 348 LYS C CD  
11267 C CE  . LYS C 348 ? 0.3642 0.3530 0.6590 0.0478  -0.0643 -0.0156 348 LYS C CE  
11268 N NZ  . LYS C 348 ? 0.3610 0.3599 0.6731 0.0540  -0.0599 -0.0190 348 LYS C NZ  
11269 N N   . VAL C 349 ? 0.3513 0.3136 0.5939 0.0275  -0.0826 -0.0002 349 VAL C N   
11270 C CA  . VAL C 349 ? 0.3648 0.3325 0.6035 0.0224  -0.0801 -0.0009 349 VAL C CA  
11271 C C   . VAL C 349 ? 0.3587 0.3416 0.6156 0.0226  -0.0813 -0.0012 349 VAL C C   
11272 O O   . VAL C 349 ? 0.3625 0.3484 0.6293 0.0240  -0.0890 0.0015  349 VAL C O   
11273 C CB  . VAL C 349 ? 0.3708 0.3280 0.5921 0.0177  -0.0845 0.0024  349 VAL C CB  
11274 C CG1 . VAL C 349 ? 0.3686 0.3309 0.5869 0.0127  -0.0814 0.0013  349 VAL C CG1 
11275 C CG2 . VAL C 349 ? 0.3891 0.3322 0.5941 0.0179  -0.0816 0.0032  349 VAL C CG2 
11276 N N   . VAL C 350 ? 0.3263 0.3187 0.5877 0.0213  -0.0735 -0.0043 350 VAL C N   
11277 C CA  . VAL C 350 ? 0.3126 0.3203 0.5915 0.0210  -0.0724 -0.0043 350 VAL C CA  
11278 C C   . VAL C 350 ? 0.2844 0.2946 0.5572 0.0147  -0.0702 -0.0037 350 VAL C C   
11279 O O   . VAL C 350 ? 0.2529 0.2574 0.5119 0.0127  -0.0650 -0.0053 350 VAL C O   
11280 C CB  . VAL C 350 ? 0.3211 0.3384 0.6127 0.0262  -0.0641 -0.0082 350 VAL C CB  
11281 C CG1 . VAL C 350 ? 0.3208 0.3545 0.6301 0.0256  -0.0607 -0.0078 350 VAL C CG1 
11282 C CG2 . VAL C 350 ? 0.3275 0.3419 0.6269 0.0329  -0.0664 -0.0090 350 VAL C CG2 
11283 N N   . VAL C 351 ? 0.2844 0.3033 0.5690 0.0117  -0.0747 -0.0012 351 VAL C N   
11284 C CA  . VAL C 351 ? 0.2813 0.3046 0.5649 0.0057  -0.0726 -0.0003 351 VAL C CA  
11285 C C   . VAL C 351 ? 0.2713 0.3123 0.5770 0.0065  -0.0677 -0.0002 351 VAL C C   
11286 O O   . VAL C 351 ? 0.2659 0.3158 0.5902 0.0087  -0.0719 0.0014  351 VAL C O   
11287 C CB  . VAL C 351 ? 0.2927 0.3092 0.5697 0.0001  -0.0824 0.0027  351 VAL C CB  
11288 C CG1 . VAL C 351 ? 0.3050 0.3241 0.5796 -0.0061 -0.0794 0.0033  351 VAL C CG1 
11289 C CG2 . VAL C 351 ? 0.3065 0.3054 0.5618 0.0002  -0.0868 0.0030  351 VAL C CG2 
11290 N N   . LYS C 352 ? 0.2787 0.3244 0.5820 0.0048  -0.0582 -0.0016 352 LYS C N   
11291 C CA  . LYS C 352 ? 0.2850 0.3466 0.6064 0.0046  -0.0517 -0.0009 352 LYS C CA  
11292 C C   . LYS C 352 ? 0.2639 0.3276 0.5841 -0.0028 -0.0515 0.0018  352 LYS C C   
11293 O O   . LYS C 352 ? 0.2801 0.3328 0.5822 -0.0068 -0.0524 0.0018  352 LYS C O   
11294 C CB  . LYS C 352 ? 0.3175 0.3827 0.6367 0.0095  -0.0401 -0.0047 352 LYS C CB  
11295 C CG  . LYS C 352 ? 0.3538 0.4214 0.6821 0.0173  -0.0387 -0.0075 352 LYS C CG  
11296 C CD  . LYS C 352 ? 0.3917 0.4546 0.7075 0.0213  -0.0298 -0.0124 352 LYS C CD  
11297 C CE  . LYS C 352 ? 0.4736 0.5364 0.7966 0.0289  -0.0287 -0.0156 352 LYS C CE  
11298 N NZ  . LYS C 352 ? 0.4970 0.5522 0.8056 0.0323  -0.0224 -0.0209 352 LYS C NZ  
11299 N N   . PHE C 353 ? 0.2392 0.3174 0.5804 -0.0044 -0.0499 0.0044  353 PHE C N   
11300 C CA  . PHE C 353 ? 0.2298 0.3134 0.5743 -0.0107 -0.0461 0.0071  353 PHE C CA  
11301 C C   . PHE C 353 ? 0.2174 0.3169 0.5784 -0.0079 -0.0344 0.0075  353 PHE C C   
11302 O O   . PHE C 353 ? 0.2232 0.3349 0.6060 -0.0045 -0.0342 0.0085  353 PHE C O   
11303 C CB  . PHE C 353 ? 0.2370 0.3217 0.5920 -0.0168 -0.0575 0.0108  353 PHE C CB  
11304 C CG  . PHE C 353 ? 0.2352 0.3242 0.5943 -0.0241 -0.0543 0.0139  353 PHE C CG  
11305 C CD1 . PHE C 353 ? 0.2254 0.3037 0.5638 -0.0272 -0.0501 0.0132  353 PHE C CD1 
11306 C CD2 . PHE C 353 ? 0.2277 0.3323 0.6128 -0.0271 -0.0541 0.0177  353 PHE C CD2 
11307 C CE1 . PHE C 353 ? 0.2282 0.3095 0.5699 -0.0335 -0.0468 0.0162  353 PHE C CE1 
11308 C CE2 . PHE C 353 ? 0.2350 0.3430 0.6240 -0.0339 -0.0504 0.0209  353 PHE C CE2 
11309 C CZ  . PHE C 353 ? 0.2392 0.3348 0.6057 -0.0370 -0.0469 0.0201  353 PHE C CZ  
11310 N N   . ARG C 354 ? 0.2076 0.3070 0.5585 -0.0092 -0.0243 0.0072  354 ARG C N   
11311 C CA  . ARG C 354 ? 0.2136 0.3265 0.5763 -0.0064 -0.0119 0.0077  354 ARG C CA  
11312 C C   . ARG C 354 ? 0.2268 0.3447 0.5975 0.0024  -0.0081 0.0041  354 ARG C C   
11313 O O   . ARG C 354 ? 0.2173 0.3497 0.6092 0.0053  -0.0023 0.0054  354 ARG C O   
11314 C CB  . ARG C 354 ? 0.2119 0.3395 0.5989 -0.0113 -0.0108 0.0131  354 ARG C CB  
11315 C CG  . ARG C 354 ? 0.2039 0.3266 0.5839 -0.0200 -0.0129 0.0167  354 ARG C CG  
11316 C CD  . ARG C 354 ? 0.2025 0.3397 0.6085 -0.0253 -0.0127 0.0223  354 ARG C CD  
11317 N NE  . ARG C 354 ? 0.1969 0.3278 0.5971 -0.0342 -0.0162 0.0257  354 ARG C NE  
11318 C CZ  . ARG C 354 ? 0.1915 0.3293 0.6108 -0.0412 -0.0215 0.0304  354 ARG C CZ  
11319 N NH1 . ARG C 354 ? 0.1886 0.3425 0.6366 -0.0405 -0.0221 0.0330  354 ARG C NH1 
11320 N NH2 . ARG C 354 ? 0.1916 0.3197 0.6019 -0.0490 -0.0264 0.0324  354 ARG C NH2 
11321 N N   . ASP C 355 ? 0.2483 0.3540 0.6025 0.0066  -0.0110 -0.0004 355 ASP C N   
11322 C CA  . ASP C 355 ? 0.2520 0.3585 0.6077 0.0150  -0.0062 -0.0050 355 ASP C CA  
11323 C C   . ASP C 355 ? 0.2547 0.3681 0.6319 0.0191  -0.0122 -0.0041 355 ASP C C   
11324 O O   . ASP C 355 ? 0.2497 0.3658 0.6331 0.0266  -0.0077 -0.0074 355 ASP C O   
11325 C CB  . ASP C 355 ? 0.2511 0.3652 0.6067 0.0183  0.0079  -0.0066 355 ASP C CB  
11326 C CG  . ASP C 355 ? 0.2617 0.3691 0.5964 0.0142  0.0129  -0.0066 355 ASP C CG  
11327 O OD1 . ASP C 355 ? 0.2505 0.3452 0.5645 0.0155  0.0117  -0.0104 355 ASP C OD1 
11328 O OD2 . ASP C 355 ? 0.2700 0.3850 0.6106 0.0095  0.0175  -0.0022 355 ASP C OD2 
11329 N N   . LYS C 356 ? 0.2712 0.3869 0.6594 0.0142  -0.0227 0.0003  356 LYS C N   
11330 C CA  . LYS C 356 ? 0.2683 0.3900 0.6767 0.0170  -0.0311 0.0021  356 LYS C CA  
11331 C C   . LYS C 356 ? 0.2625 0.3687 0.6560 0.0153  -0.0442 0.0020  356 LYS C C   
11332 O O   . LYS C 356 ? 0.2332 0.3304 0.6121 0.0087  -0.0496 0.0034  356 LYS C O   
11333 C CB  . LYS C 356 ? 0.2758 0.4121 0.7089 0.0121  -0.0344 0.0076  356 LYS C CB  
11334 C CG  . LYS C 356 ? 0.3199 0.4674 0.7805 0.0158  -0.0412 0.0101  356 LYS C CG  
11335 C CD  . LYS C 356 ? 0.3499 0.5097 0.8331 0.0088  -0.0476 0.0159  356 LYS C CD  
11336 C CE  . LYS C 356 ? 0.4021 0.5822 0.9199 0.0126  -0.0439 0.0188  356 LYS C CE  
11337 N NZ  . LYS C 356 ? 0.4558 0.6360 0.9845 0.0193  -0.0522 0.0184  356 LYS C NZ  
11338 N N   . VAL C 357 ? 0.2373 0.3398 0.6335 0.0218  -0.0481 0.0003  357 VAL C N   
11339 C CA  . VAL C 357 ? 0.2366 0.3253 0.6209 0.0211  -0.0600 0.0010  357 VAL C CA  
11340 C C   . VAL C 357 ? 0.2409 0.3329 0.6364 0.0161  -0.0724 0.0059  357 VAL C C   
11341 O O   . VAL C 357 ? 0.2399 0.3443 0.6597 0.0185  -0.0757 0.0083  357 VAL C O   
11342 C CB  . VAL C 357 ? 0.2409 0.3256 0.6283 0.0293  -0.0613 -0.0011 357 VAL C CB  
11343 C CG1 . VAL C 357 ? 0.2493 0.3213 0.6276 0.0285  -0.0745 0.0012  357 VAL C CG1 
11344 C CG2 . VAL C 357 ? 0.2324 0.3099 0.6049 0.0335  -0.0513 -0.0065 357 VAL C CG2 
11345 N N   . ILE C 358 ? 0.2396 0.3194 0.6166 0.0097  -0.0796 0.0070  358 ILE C N   
11346 C CA  . ILE C 358 ? 0.2425 0.3209 0.6243 0.0049  -0.0933 0.0109  358 ILE C CA  
11347 C C   . ILE C 358 ? 0.2523 0.3143 0.6172 0.0066  -0.1037 0.0112  358 ILE C C   
11348 O O   . ILE C 358 ? 0.2575 0.3171 0.6253 0.0040  -0.1162 0.0142  358 ILE C O   
11349 C CB  . ILE C 358 ? 0.2358 0.3120 0.6102 -0.0039 -0.0945 0.0122  358 ILE C CB  
11350 C CG1 . ILE C 358 ? 0.2349 0.2941 0.5792 -0.0061 -0.0915 0.0097  358 ILE C CG1 
11351 C CG2 . ILE C 358 ? 0.2252 0.3184 0.6190 -0.0062 -0.0852 0.0133  358 ILE C CG2 
11352 C CD1 . ILE C 358 ? 0.2496 0.3037 0.5849 -0.0143 -0.0943 0.0110  358 ILE C CD1 
11353 N N   . TYR C 359 ? 0.2838 0.3341 0.6305 0.0105  -0.0991 0.0084  359 TYR C N   
11354 C CA  . TYR C 359 ? 0.3201 0.3544 0.6501 0.0121  -0.1075 0.0093  359 TYR C CA  
11355 C C   . TYR C 359 ? 0.3249 0.3531 0.6475 0.0184  -0.1002 0.0064  359 TYR C C   
11356 O O   . TYR C 359 ? 0.3201 0.3477 0.6350 0.0184  -0.0899 0.0032  359 TYR C O   
11357 C CB  . TYR C 359 ? 0.3302 0.3493 0.6353 0.0060  -0.1118 0.0099  359 TYR C CB  
11358 C CG  . TYR C 359 ? 0.3626 0.3638 0.6473 0.0077  -0.1187 0.0111  359 TYR C CG  
11359 C CD1 . TYR C 359 ? 0.3715 0.3671 0.6549 0.0069  -0.1321 0.0145  359 TYR C CD1 
11360 C CD2 . TYR C 359 ? 0.3820 0.3718 0.6491 0.0101  -0.1118 0.0092  359 TYR C CD2 
11361 C CE1 . TYR C 359 ? 0.4119 0.3908 0.6757 0.0089  -0.1376 0.0161  359 TYR C CE1 
11362 C CE2 . TYR C 359 ? 0.3936 0.3676 0.6430 0.0116  -0.1168 0.0110  359 TYR C CE2 
11363 C CZ  . TYR C 359 ? 0.4402 0.4084 0.6871 0.0112  -0.1293 0.0146  359 TYR C CZ  
11364 O OH  . TYR C 359 ? 0.5031 0.4550 0.7313 0.0129  -0.1338 0.0169  359 TYR C OH  
11365 N N   . SER C 360 ? 0.3689 0.3912 0.6927 0.0233  -0.1064 0.0079  360 SER C N   
11366 C CA  . SER C 360 ? 0.4119 0.4274 0.7307 0.0292  -0.1011 0.0056  360 SER C CA  
11367 C C   . SER C 360 ? 0.4453 0.4467 0.7537 0.0313  -0.1106 0.0088  360 SER C C   
11368 O O   . SER C 360 ? 0.4994 0.5032 0.8182 0.0327  -0.1206 0.0124  360 SER C O   
11369 C CB  . SER C 360 ? 0.4319 0.4607 0.7733 0.0355  -0.0954 0.0035  360 SER C CB  
11370 O OG  . SER C 360 ? 0.4958 0.5168 0.8305 0.0405  -0.0893 0.0001  360 SER C OG  
11371 N N   . LYS C 361 ? 0.4285 0.4152 0.7171 0.0315  -0.1076 0.0080  361 LYS C N   
11372 C CA  . LYS C 361 ? 0.4604 0.4323 0.7366 0.0331  -0.1155 0.0118  361 LYS C CA  
11373 C C   . LYS C 361 ? 0.4223 0.3832 0.6881 0.0360  -0.1091 0.0103  361 LYS C C   
11374 O O   . LYS C 361 ? 0.4121 0.3684 0.6651 0.0331  -0.1018 0.0080  361 LYS C O   
11375 C CB  . LYS C 361 ? 0.5266 0.4872 0.7819 0.0273  -0.1218 0.0147  361 LYS C CB  
11376 C CG  . LYS C 361 ? 0.5911 0.5379 0.8350 0.0290  -0.1321 0.0197  361 LYS C CG  
11377 C CD  . LYS C 361 ? 0.6817 0.6134 0.8997 0.0243  -0.1367 0.0221  361 LYS C CD  
11378 C CE  . LYS C 361 ? 0.7584 0.6733 0.9600 0.0267  -0.1436 0.0269  361 LYS C CE  
11379 N NZ  . LYS C 361 ? 0.7638 0.6807 0.9751 0.0291  -0.1568 0.0308  361 LYS C NZ  
11380 N N   . ASN C 362 ? 0.4110 0.3676 0.6833 0.0417  -0.1121 0.0119  362 ASN C N   
11381 C CA  . ASN C 362 ? 0.4447 0.3884 0.7067 0.0439  -0.1081 0.0116  362 ASN C CA  
11382 C C   . ASN C 362 ? 0.4626 0.3906 0.7015 0.0403  -0.1118 0.0160  362 ASN C C   
11383 O O   . ASN C 362 ? 0.5125 0.4367 0.7467 0.0395  -0.1212 0.0204  362 ASN C O   
11384 C CB  . ASN C 362 ? 0.4605 0.4019 0.7348 0.0508  -0.1111 0.0128  362 ASN C CB  
11385 C CG  . ASN C 362 ? 0.4832 0.4395 0.7804 0.0554  -0.1069 0.0084  362 ASN C CG  
11386 O OD1 . ASN C 362 ? 0.5152 0.4777 0.8289 0.0599  -0.1127 0.0104  362 ASN C OD1 
11387 N ND2 . ASN C 362 ? 0.4817 0.4440 0.7802 0.0546  -0.0969 0.0025  362 ASN C ND2 
11388 N N   . ILE C 363 ? 0.4357 0.3555 0.6606 0.0378  -0.1044 0.0147  363 ILE C N   
11389 C CA  . ILE C 363 ? 0.4670 0.3719 0.6698 0.0347  -0.1055 0.0188  363 ILE C CA  
11390 C C   . ILE C 363 ? 0.5080 0.3998 0.7064 0.0381  -0.1065 0.0225  363 ILE C C   
11391 O O   . ILE C 363 ? 0.5127 0.4027 0.7151 0.0395  -0.1000 0.0203  363 ILE C O   
11392 C CB  . ILE C 363 ? 0.4521 0.3558 0.6443 0.0304  -0.0966 0.0160  363 ILE C CB  
11393 C CG1 . ILE C 363 ? 0.4311 0.3473 0.6281 0.0270  -0.0949 0.0124  363 ILE C CG1 
11394 C CG2 . ILE C 363 ? 0.4671 0.3553 0.6372 0.0278  -0.0962 0.0204  363 ILE C CG2 
11395 C CD1 . ILE C 363 ? 0.4159 0.3327 0.6081 0.0242  -0.1029 0.0149  363 ILE C CD1 
11396 N N   . THR C 364 ? 0.5976 0.4797 0.7868 0.0391  -0.1149 0.0284  364 THR C N   
11397 C CA  . THR C 364 ? 0.6719 0.5399 0.8546 0.0421  -0.1166 0.0334  364 THR C CA  
11398 C C   . THR C 364 ? 0.6439 0.4974 0.8036 0.0387  -0.1118 0.0369  364 THR C C   
11399 O O   . THR C 364 ? 0.5856 0.4284 0.7407 0.0399  -0.1085 0.0401  364 THR C O   
11400 C CB  . THR C 364 ? 0.7135 0.5780 0.8976 0.0455  -0.1286 0.0386  364 THR C CB  
11401 O OG1 . THR C 364 ? 0.7437 0.6030 0.9099 0.0417  -0.1342 0.0413  364 THR C OG1 
11402 C CG2 . THR C 364 ? 0.7341 0.6140 0.9431 0.0493  -0.1333 0.0358  364 THR C CG2 
11403 N N   . SER C 365 ? 0.6638 0.5164 0.8092 0.0344  -0.1112 0.0365  365 SER C N   
11404 C CA  . SER C 365 ? 0.6806 0.5189 0.8032 0.0319  -0.1068 0.0403  365 SER C CA  
11405 C C   . SER C 365 ? 0.5896 0.4328 0.7083 0.0277  -0.0982 0.0360  365 SER C C   
11406 O O   . SER C 365 ? 0.6141 0.4677 0.7380 0.0257  -0.0998 0.0320  365 SER C O   
11407 C CB  . SER C 365 ? 0.7216 0.5491 0.8259 0.0318  -0.1158 0.0452  365 SER C CB  
11408 O OG  . SER C 365 ? 0.8071 0.6208 0.8876 0.0295  -0.1102 0.0482  365 SER C OG  
11409 N N   . GLU C 366 ? 0.5578 0.3938 0.6686 0.0264  -0.0891 0.0373  366 GLU C N   
11410 C CA  . GLU C 366 ? 0.5190 0.3592 0.6268 0.0229  -0.0808 0.0339  366 GLU C CA  
11411 C C   . GLU C 366 ? 0.4856 0.3171 0.5717 0.0206  -0.0812 0.0358  366 GLU C C   
11412 O O   . GLU C 366 ? 0.4932 0.3133 0.5640 0.0215  -0.0868 0.0401  366 GLU C O   
11413 C CB  . GLU C 366 ? 0.5185 0.3553 0.6288 0.0225  -0.0714 0.0348  366 GLU C CB  
11414 C CG  . GLU C 366 ? 0.5479 0.3688 0.6409 0.0223  -0.0671 0.0414  366 GLU C CG  
11415 C CD  . GLU C 366 ? 0.5627 0.3820 0.6602 0.0209  -0.0571 0.0425  366 GLU C CD  
11416 O OE1 . GLU C 366 ? 0.5583 0.3793 0.6508 0.0186  -0.0509 0.0412  366 GLU C OE1 
11417 O OE2 . GLU C 366 ? 0.6344 0.4511 0.7414 0.0219  -0.0555 0.0444  366 GLU C OE2 
11418 N N   . GLY C 367 ? 0.4730 0.3083 0.5563 0.0177  -0.0749 0.0326  367 GLY C N   
11419 C CA  . GLY C 367 ? 0.4990 0.3260 0.5624 0.0156  -0.0747 0.0333  367 GLY C CA  
11420 C C   . GLY C 367 ? 0.4826 0.3152 0.5467 0.0140  -0.0838 0.0303  367 GLY C C   
11421 O O   . GLY C 367 ? 0.4438 0.2908 0.5263 0.0135  -0.0862 0.0265  367 GLY C O   
11422 N N   . TYR C 368 ? 0.4852 0.3057 0.5287 0.0132  -0.0888 0.0322  368 TYR C N   
11423 C CA  . TYR C 368 ? 0.4770 0.3005 0.5189 0.0107  -0.0976 0.0295  368 TYR C CA  
11424 C C   . TYR C 368 ? 0.4891 0.3202 0.5451 0.0120  -0.1091 0.0301  368 TYR C C   
11425 O O   . TYR C 368 ? 0.4677 0.2920 0.5202 0.0150  -0.1138 0.0343  368 TYR C O   
11426 C CB  . TYR C 368 ? 0.4812 0.2865 0.4944 0.0098  -0.1004 0.0315  368 TYR C CB  
11427 C CG  . TYR C 368 ? 0.4777 0.2843 0.4881 0.0066  -0.1101 0.0285  368 TYR C CG  
11428 C CD1 . TYR C 368 ? 0.4686 0.2786 0.4788 0.0033  -0.1061 0.0243  368 TYR C CD1 
11429 C CD2 . TYR C 368 ? 0.4814 0.2852 0.4895 0.0067  -0.1237 0.0301  368 TYR C CD2 
11430 C CE1 . TYR C 368 ? 0.4653 0.2756 0.4735 -0.0002 -0.1153 0.0217  368 TYR C CE1 
11431 C CE2 . TYR C 368 ? 0.5048 0.3098 0.5118 0.0032  -0.1336 0.0275  368 TYR C CE2 
11432 C CZ  . TYR C 368 ? 0.4885 0.2965 0.4956 -0.0005 -0.1291 0.0232  368 TYR C CZ  
11433 O OH  . TYR C 368 ? 0.4801 0.2891 0.4877 -0.0045 -0.1392 0.0208  368 TYR C OH  
11434 N N   . MET C 369 ? 0.5014 0.3461 0.5731 0.0098  -0.1136 0.0265  369 MET C N   
11435 C CA  . MET C 369 ? 0.5087 0.3609 0.5937 0.0105  -0.1255 0.0271  369 MET C CA  
11436 C C   . MET C 369 ? 0.5101 0.3699 0.6005 0.0061  -0.1309 0.0239  369 MET C C   
11437 O O   . MET C 369 ? 0.5104 0.3782 0.6073 0.0035  -0.1239 0.0204  369 MET C O   
11438 C CB  . MET C 369 ? 0.5360 0.4027 0.6467 0.0138  -0.1237 0.0264  369 MET C CB  
11439 C CG  . MET C 369 ? 0.5968 0.4788 0.7248 0.0125  -0.1155 0.0217  369 MET C CG  
11440 S SD  . MET C 369 ? 0.7305 0.6330 0.8896 0.0143  -0.1196 0.0196  369 MET C SD  
11441 C CE  . MET C 369 ? 0.6841 0.5881 0.8438 0.0111  -0.1334 0.0211  369 MET C CE  
11442 N N   . ALA C 370 ? 0.4948 0.3519 0.5830 0.0051  -0.1441 0.0256  370 ALA C N   
11443 C CA  . ALA C 370 ? 0.4992 0.3618 0.5923 0.0004  -0.1511 0.0232  370 ALA C CA  
11444 C C   . ALA C 370 ? 0.4943 0.3727 0.6141 0.0011  -0.1604 0.0240  370 ALA C C   
11445 O O   . ALA C 370 ? 0.4903 0.3674 0.6137 0.0049  -0.1670 0.0274  370 ALA C O   
11446 C CB  . ALA C 370 ? 0.5087 0.3528 0.5745 -0.0023 -0.1595 0.0239  370 ALA C CB  
11447 N N   . ASP C 371 ? 0.4730 0.3663 0.6117 -0.0024 -0.1605 0.0214  371 ASP C N   
11448 C CA  . ASP C 371 ? 0.4682 0.3782 0.6345 -0.0020 -0.1682 0.0223  371 ASP C CA  
11449 C C   . ASP C 371 ? 0.4521 0.3704 0.6278 -0.0083 -0.1707 0.0201  371 ASP C C   
11450 O O   . ASP C 371 ? 0.4426 0.3493 0.5990 -0.0126 -0.1709 0.0185  371 ASP C O   
11451 C CB  . ASP C 371 ? 0.4547 0.3780 0.6420 0.0033  -0.1597 0.0221  371 ASP C CB  
11452 C CG  . ASP C 371 ? 0.4362 0.3731 0.6497 0.0067  -0.1676 0.0243  371 ASP C CG  
11453 O OD1 . ASP C 371 ? 0.4070 0.3467 0.6274 0.0042  -0.1800 0.0261  371 ASP C OD1 
11454 O OD2 . ASP C 371 ? 0.4796 0.4244 0.7075 0.0118  -0.1611 0.0239  371 ASP C OD2 
11455 N N   . GLU C 372 ? 0.4623 0.4002 0.6679 -0.0087 -0.1724 0.0202  372 GLU C N   
11456 C CA  . GLU C 372 ? 0.4901 0.4376 0.7077 -0.0148 -0.1729 0.0187  372 GLU C CA  
11457 C C   . GLU C 372 ? 0.4552 0.4254 0.7043 -0.0133 -0.1651 0.0182  372 GLU C C   
11458 O O   . GLU C 372 ? 0.4489 0.4284 0.7146 -0.0080 -0.1650 0.0196  372 GLU C O   
11459 C CB  . GLU C 372 ? 0.5383 0.4807 0.7540 -0.0196 -0.1896 0.0202  372 GLU C CB  
11460 C CG  . GLU C 372 ? 0.5875 0.5357 0.8184 -0.0161 -0.2018 0.0239  372 GLU C CG  
11461 C CD  . GLU C 372 ? 0.6700 0.6204 0.9098 -0.0218 -0.2180 0.0253  372 GLU C CD  
11462 O OE1 . GLU C 372 ? 0.7322 0.6716 0.9553 -0.0279 -0.2214 0.0232  372 GLU C OE1 
11463 O OE2 . GLU C 372 ? 0.7001 0.6637 0.9650 -0.0200 -0.2271 0.0283  372 GLU C OE2 
11464 N N   . LEU C 373 ? 0.4473 0.4246 0.7021 -0.0178 -0.1575 0.0163  373 LEU C N   
11465 C CA  . LEU C 373 ? 0.4449 0.4427 0.7267 -0.0174 -0.1492 0.0160  373 LEU C CA  
11466 C C   . LEU C 373 ? 0.4223 0.4313 0.7254 -0.0225 -0.1587 0.0182  373 LEU C C   
11467 O O   . LEU C 373 ? 0.4594 0.4588 0.7510 -0.0286 -0.1665 0.0181  373 LEU C O   
11468 C CB  . LEU C 373 ? 0.4507 0.4496 0.7265 -0.0200 -0.1363 0.0135  373 LEU C CB  
11469 C CG  . LEU C 373 ? 0.5086 0.4982 0.7656 -0.0160 -0.1257 0.0112  373 LEU C CG  
11470 C CD1 . LEU C 373 ? 0.5183 0.5067 0.7669 -0.0196 -0.1158 0.0093  373 LEU C CD1 
11471 C CD2 . LEU C 373 ? 0.4693 0.4695 0.7414 -0.0091 -0.1199 0.0108  373 LEU C CD2 
11472 N N   . THR C 374 ? 0.4095 0.4387 0.7429 -0.0205 -0.1556 0.0196  374 THR C N   
11473 C CA  . THR C 374 ? 0.4132 0.4563 0.7711 -0.0260 -0.1613 0.0219  374 THR C CA  
11474 C C   . THR C 374 ? 0.4195 0.4757 0.7899 -0.0279 -0.1468 0.0212  374 THR C C   
11475 O O   . THR C 374 ? 0.4377 0.5024 0.8149 -0.0223 -0.1345 0.0200  374 THR C O   
11476 C CB  . THR C 374 ? 0.4017 0.4588 0.7875 -0.0226 -0.1700 0.0252  374 THR C CB  
11477 O OG1 . THR C 374 ? 0.4229 0.4633 0.7891 -0.0215 -0.1833 0.0258  374 THR C OG1 
11478 C CG2 . THR C 374 ? 0.3796 0.4521 0.7936 -0.0288 -0.1768 0.0282  374 THR C CG2 
11479 N N   . ILE C 375 ? 0.4048 0.4620 0.7784 -0.0359 -0.1492 0.0220  375 ILE C N   
11480 C CA  . ILE C 375 ? 0.3937 0.4628 0.7797 -0.0389 -0.1369 0.0224  375 ILE C CA  
11481 C C   . ILE C 375 ? 0.4057 0.4896 0.8211 -0.0451 -0.1438 0.0262  375 ILE C C   
11482 O O   . ILE C 375 ? 0.4219 0.5027 0.8420 -0.0485 -0.1594 0.0278  375 ILE C O   
11483 C CB  . ILE C 375 ? 0.3841 0.4381 0.7432 -0.0429 -0.1312 0.0201  375 ILE C CB  
11484 C CG1 . ILE C 375 ? 0.3696 0.4082 0.7143 -0.0501 -0.1443 0.0200  375 ILE C CG1 
11485 C CG2 . ILE C 375 ? 0.3795 0.4217 0.7141 -0.0365 -0.1232 0.0168  375 ILE C CG2 
11486 C CD1 . ILE C 375 ? 0.3668 0.3936 0.6918 -0.0546 -0.1378 0.0183  375 ILE C CD1 
11487 N N   . ASP C 376 ? 0.4153 0.5157 0.8511 -0.0464 -0.1321 0.0280  376 ASP C N   
11488 C CA  . ASP C 376 ? 0.4250 0.5420 0.8927 -0.0522 -0.1363 0.0324  376 ASP C CA  
11489 C C   . ASP C 376 ? 0.3931 0.5125 0.8612 -0.0586 -0.1259 0.0335  376 ASP C C   
11490 O O   . ASP C 376 ? 0.3968 0.5331 0.8856 -0.0579 -0.1139 0.0360  376 ASP C O   
11491 C CB  . ASP C 376 ? 0.4095 0.5479 0.9091 -0.0460 -0.1324 0.0348  376 ASP C CB  
11492 C CG  . ASP C 376 ? 0.4394 0.5958 0.9761 -0.0507 -0.1408 0.0399  376 ASP C CG  
11493 O OD1 . ASP C 376 ? 0.4458 0.5969 0.9838 -0.0596 -0.1534 0.0414  376 ASP C OD1 
11494 O OD2 . ASP C 376 ? 0.4731 0.6486 1.0382 -0.0453 -0.1351 0.0422  376 ASP C OD2 
11495 N N   . PRO C 377 ? 0.3771 0.4789 0.8214 -0.0647 -0.1296 0.0319  377 PRO C N   
11496 C CA  . PRO C 377 ? 0.3710 0.4727 0.8125 -0.0700 -0.1193 0.0330  377 PRO C CA  
11497 C C   . PRO C 377 ? 0.3400 0.4577 0.8131 -0.0775 -0.1201 0.0382  377 PRO C C   
11498 O O   . PRO C 377 ? 0.3359 0.4579 0.8268 -0.0818 -0.1340 0.0402  377 PRO C O   
11499 C CB  . PRO C 377 ? 0.3807 0.4582 0.7904 -0.0743 -0.1261 0.0300  377 PRO C CB  
11500 C CG  . PRO C 377 ? 0.4080 0.4762 0.8128 -0.0749 -0.1440 0.0287  377 PRO C CG  
11501 C CD  . PRO C 377 ? 0.3937 0.4742 0.8124 -0.0666 -0.1437 0.0291  377 PRO C CD  
11502 N N   . VAL C 378 ? 0.3357 0.4618 0.8151 -0.0789 -0.1051 0.0406  378 VAL C N   
11503 C CA  . VAL C 378 ? 0.3411 0.4820 0.8496 -0.0865 -0.1031 0.0462  378 VAL C CA  
11504 C C   . VAL C 378 ? 0.3347 0.4608 0.8277 -0.0951 -0.1045 0.0466  378 VAL C C   
11505 O O   . VAL C 378 ? 0.3416 0.4577 0.8118 -0.0936 -0.0944 0.0451  378 VAL C O   
11506 C CB  . VAL C 378 ? 0.3395 0.5009 0.8680 -0.0820 -0.0849 0.0495  378 VAL C CB  
11507 C CG1 . VAL C 378 ? 0.3393 0.5158 0.8978 -0.0902 -0.0814 0.0561  378 VAL C CG1 
11508 C CG2 . VAL C 378 ? 0.3436 0.5187 0.8880 -0.0729 -0.0836 0.0487  378 VAL C CG2 
11509 N N   . GLY C 379 ? 0.3284 0.4521 0.8336 -0.1042 -0.1182 0.0486  379 GLY C N   
11510 C CA  . GLY C 379 ? 0.3230 0.4298 0.8129 -0.1126 -0.1226 0.0483  379 GLY C CA  
11511 C C   . GLY C 379 ? 0.3082 0.3907 0.7572 -0.1087 -0.1237 0.0423  379 GLY C C   
11512 O O   . GLY C 379 ? 0.3064 0.3808 0.7412 -0.1037 -0.1316 0.0383  379 GLY C O   
11513 N N   . ILE C 380 ? 0.2932 0.3647 0.7248 -0.1111 -0.1152 0.0423  380 ILE C N   
11514 C CA  . ILE C 380 ? 0.3035 0.3561 0.6998 -0.1060 -0.1116 0.0375  380 ILE C CA  
11515 C C   . ILE C 380 ? 0.2868 0.3488 0.6790 -0.0975 -0.0950 0.0376  380 ILE C C   
11516 O O   . ILE C 380 ? 0.2563 0.3277 0.6571 -0.0984 -0.0826 0.0413  380 ILE C O   
11517 C CB  . ILE C 380 ? 0.3196 0.3541 0.6988 -0.1124 -0.1122 0.0372  380 ILE C CB  
11518 C CG1 . ILE C 380 ? 0.3393 0.3674 0.7290 -0.1224 -0.1274 0.0380  380 ILE C CG1 
11519 C CG2 . ILE C 380 ? 0.3220 0.3356 0.6655 -0.1070 -0.1112 0.0319  380 ILE C CG2 
11520 C CD1 . ILE C 380 ? 0.3504 0.3604 0.7256 -0.1291 -0.1277 0.0379  380 ILE C CD1 
11521 N N   . GLU C 381 ? 0.3058 0.3634 0.6828 -0.0894 -0.0955 0.0334  381 GLU C N   
11522 C CA  . GLU C 381 ? 0.3066 0.3730 0.6808 -0.0809 -0.0823 0.0326  381 GLU C CA  
11523 C C   . GLU C 381 ? 0.3103 0.3599 0.6528 -0.0753 -0.0796 0.0280  381 GLU C C   
11524 O O   . GLU C 381 ? 0.3284 0.3680 0.6580 -0.0723 -0.0879 0.0246  381 GLU C O   
11525 C CB  . GLU C 381 ? 0.2960 0.3770 0.6889 -0.0755 -0.0848 0.0324  381 GLU C CB  
11526 C CG  . GLU C 381 ? 0.2914 0.3860 0.6903 -0.0680 -0.0700 0.0326  381 GLU C CG  
11527 C CD  . GLU C 381 ? 0.2828 0.3919 0.7015 -0.0621 -0.0711 0.0324  381 GLU C CD  
11528 O OE1 . GLU C 381 ? 0.2922 0.4163 0.7392 -0.0643 -0.0745 0.0358  381 GLU C OE1 
11529 O OE2 . GLU C 381 ? 0.2931 0.3977 0.6982 -0.0547 -0.0684 0.0287  381 GLU C OE2 
11530 N N   . ASP C 382 ? 0.2965 0.3437 0.6270 -0.0736 -0.0678 0.0283  382 ASP C N   
11531 C CA  . ASP C 382 ? 0.2889 0.3250 0.5948 -0.0672 -0.0637 0.0245  382 ASP C CA  
11532 C C   . ASP C 382 ? 0.2794 0.3258 0.5906 -0.0593 -0.0596 0.0225  382 ASP C C   
11533 O O   . ASP C 382 ? 0.2638 0.3265 0.5930 -0.0575 -0.0524 0.0245  382 ASP C O   
11534 C CB  . ASP C 382 ? 0.2795 0.3111 0.5727 -0.0674 -0.0532 0.0256  382 ASP C CB  
11535 C CG  . ASP C 382 ? 0.2721 0.3196 0.5807 -0.0677 -0.0418 0.0296  382 ASP C CG  
11536 O OD1 . ASP C 382 ? 0.2808 0.3376 0.6096 -0.0735 -0.0430 0.0336  382 ASP C OD1 
11537 O OD2 . ASP C 382 ? 0.2437 0.2938 0.5439 -0.0624 -0.0321 0.0288  382 ASP C OD2 
11538 N N   . MET C 383 ? 0.2796 0.3157 0.5746 -0.0543 -0.0635 0.0187  383 MET C N   
11539 C CA  . MET C 383 ? 0.2800 0.3233 0.5792 -0.0470 -0.0611 0.0166  383 MET C CA  
11540 C C   . MET C 383 ? 0.2670 0.2986 0.5433 -0.0418 -0.0575 0.0131  383 MET C C   
11541 O O   . MET C 383 ? 0.2510 0.2677 0.5104 -0.0426 -0.0633 0.0116  383 MET C O   
11542 C CB  . MET C 383 ? 0.3049 0.3494 0.6136 -0.0463 -0.0727 0.0162  383 MET C CB  
11543 C CG  . MET C 383 ? 0.3246 0.3799 0.6571 -0.0519 -0.0791 0.0197  383 MET C CG  
11544 S SD  . MET C 383 ? 0.3872 0.4426 0.7293 -0.0508 -0.0945 0.0195  383 MET C SD  
11545 C CE  . MET C 383 ? 0.3854 0.4581 0.7468 -0.0421 -0.0881 0.0193  383 MET C CE  
11546 N N   . GLU C 384 ? 0.2797 0.3180 0.5559 -0.0367 -0.0477 0.0119  384 GLU C N   
11547 C CA  . GLU C 384 ? 0.2917 0.3213 0.5507 -0.0314 -0.0450 0.0085  384 GLU C CA  
11548 C C   . GLU C 384 ? 0.2747 0.3073 0.5400 -0.0260 -0.0485 0.0065  384 GLU C C   
11549 O O   . GLU C 384 ? 0.2734 0.3178 0.5515 -0.0222 -0.0434 0.0059  384 GLU C O   
11550 C CB  . GLU C 384 ? 0.2914 0.3248 0.5452 -0.0289 -0.0340 0.0079  384 GLU C CB  
11551 C CG  . GLU C 384 ? 0.3006 0.3248 0.5374 -0.0242 -0.0320 0.0046  384 GLU C CG  
11552 C CD  . GLU C 384 ? 0.2957 0.3229 0.5265 -0.0221 -0.0226 0.0039  384 GLU C CD  
11553 O OE1 . GLU C 384 ? 0.2967 0.3340 0.5357 -0.0228 -0.0162 0.0057  384 GLU C OE1 
11554 O OE2 . GLU C 384 ? 0.3203 0.3391 0.5372 -0.0199 -0.0219 0.0020  384 GLU C OE2 
11555 N N   . LEU C 385 ? 0.2719 0.2935 0.5281 -0.0256 -0.0571 0.0056  385 LEU C N   
11556 C CA  . LEU C 385 ? 0.2834 0.3058 0.5440 -0.0205 -0.0611 0.0042  385 LEU C CA  
11557 C C   . LEU C 385 ? 0.2889 0.3061 0.5376 -0.0152 -0.0550 0.0013  385 LEU C C   
11558 O O   . LEU C 385 ? 0.2873 0.2924 0.5186 -0.0158 -0.0548 0.0006  385 LEU C O   
11559 C CB  . LEU C 385 ? 0.2848 0.2966 0.5389 -0.0222 -0.0727 0.0051  385 LEU C CB  
11560 C CG  . LEU C 385 ? 0.2975 0.3103 0.5591 -0.0286 -0.0808 0.0075  385 LEU C CG  
11561 C CD1 . LEU C 385 ? 0.3174 0.3164 0.5665 -0.0292 -0.0919 0.0075  385 LEU C CD1 
11562 C CD2 . LEU C 385 ? 0.2958 0.3261 0.5842 -0.0290 -0.0820 0.0096  385 LEU C CD2 
11563 N N   . ALA C 386 ? 0.2842 0.3104 0.5433 -0.0100 -0.0505 -0.0005 386 ALA C N   
11564 C CA  . ALA C 386 ? 0.3014 0.3239 0.5516 -0.0052 -0.0448 -0.0037 386 ALA C CA  
11565 C C   . ALA C 386 ? 0.3161 0.3321 0.5648 -0.0010 -0.0501 -0.0048 386 ALA C C   
11566 O O   . ALA C 386 ? 0.2987 0.3214 0.5611 0.0026  -0.0519 -0.0051 386 ALA C O   
11567 C CB  . ALA C 386 ? 0.2941 0.3285 0.5542 -0.0020 -0.0361 -0.0054 386 ALA C CB  
11568 N N   . PHE C 387 ? 0.3112 0.3139 0.5435 -0.0014 -0.0522 -0.0050 387 PHE C N   
11569 C CA  . PHE C 387 ? 0.3095 0.3039 0.5379 0.0020  -0.0568 -0.0052 387 PHE C CA  
11570 C C   . PHE C 387 ? 0.3366 0.3304 0.5636 0.0064  -0.0510 -0.0085 387 PHE C C   
11571 O O   . PHE C 387 ? 0.3671 0.3596 0.5863 0.0055  -0.0454 -0.0101 387 PHE C O   
11572 C CB  . PHE C 387 ? 0.3229 0.3029 0.5343 -0.0005 -0.0609 -0.0034 387 PHE C CB  
11573 C CG  . PHE C 387 ? 0.3511 0.3280 0.5613 -0.0043 -0.0690 -0.0007 387 PHE C CG  
11574 C CD1 . PHE C 387 ? 0.3528 0.3350 0.5670 -0.0090 -0.0691 0.0001  387 PHE C CD1 
11575 C CD2 . PHE C 387 ? 0.3572 0.3251 0.5617 -0.0033 -0.0768 0.0010  387 PHE C CD2 
11576 C CE1 . PHE C 387 ? 0.3602 0.3392 0.5741 -0.0127 -0.0776 0.0021  387 PHE C CE1 
11577 C CE2 . PHE C 387 ? 0.3611 0.3252 0.5631 -0.0067 -0.0852 0.0031  387 PHE C CE2 
11578 C CZ  . PHE C 387 ? 0.3989 0.3686 0.6062 -0.0116 -0.0859 0.0034  387 PHE C CZ  
11579 N N   . GLU C 388 ? 0.3261 0.3203 0.5607 0.0110  -0.0530 -0.0095 388 GLU C N   
11580 C CA  . GLU C 388 ? 0.3184 0.3097 0.5515 0.0152  -0.0491 -0.0128 388 GLU C CA  
11581 C C   . GLU C 388 ? 0.3193 0.2996 0.5480 0.0173  -0.0543 -0.0114 388 GLU C C   
11582 O O   . GLU C 388 ? 0.3071 0.2875 0.5424 0.0188  -0.0603 -0.0091 388 GLU C O   
11583 C CB  . GLU C 388 ? 0.3266 0.3285 0.5743 0.0198  -0.0453 -0.0157 388 GLU C CB  
11584 C CG  . GLU C 388 ? 0.3369 0.3501 0.5894 0.0183  -0.0389 -0.0167 388 GLU C CG  
11585 C CD  . GLU C 388 ? 0.3371 0.3620 0.6062 0.0228  -0.0352 -0.0185 388 GLU C CD  
11586 O OE1 . GLU C 388 ? 0.3117 0.3369 0.5907 0.0267  -0.0391 -0.0182 388 GLU C OE1 
11587 O OE2 . GLU C 388 ? 0.3824 0.4159 0.6545 0.0228  -0.0280 -0.0197 388 GLU C OE2 
11588 N N   . PHE C 389 ? 0.3289 0.3001 0.5473 0.0174  -0.0521 -0.0124 389 PHE C N   
11589 C CA  . PHE C 389 ? 0.3374 0.2975 0.5511 0.0191  -0.0554 -0.0108 389 PHE C CA  
11590 C C   . PHE C 389 ? 0.3484 0.3075 0.5674 0.0232  -0.0526 -0.0145 389 PHE C C   
11591 O O   . PHE C 389 ? 0.3662 0.3267 0.5828 0.0228  -0.0478 -0.0180 389 PHE C O   
11592 C CB  . PHE C 389 ? 0.3278 0.2780 0.5269 0.0157  -0.0543 -0.0086 389 PHE C CB  
11593 C CG  . PHE C 389 ? 0.3186 0.2659 0.5094 0.0120  -0.0574 -0.0052 389 PHE C CG  
11594 C CD1 . PHE C 389 ? 0.3382 0.2916 0.5281 0.0088  -0.0553 -0.0058 389 PHE C CD1 
11595 C CD2 . PHE C 389 ? 0.3290 0.2664 0.5119 0.0119  -0.0625 -0.0014 389 PHE C CD2 
11596 C CE1 . PHE C 389 ? 0.3349 0.2844 0.5170 0.0053  -0.0585 -0.0032 389 PHE C CE1 
11597 C CE2 . PHE C 389 ? 0.3404 0.2736 0.5137 0.0086  -0.0657 0.0010  389 PHE C CE2 
11598 C CZ  . PHE C 389 ? 0.3332 0.2723 0.5066 0.0052  -0.0638 -0.0002 389 PHE C CZ  
11599 N N   . TYR C 390 ? 0.3814 0.3368 0.6066 0.0270  -0.0563 -0.0138 390 TYR C N   
11600 C CA  . TYR C 390 ? 0.3648 0.3185 0.5965 0.0315  -0.0544 -0.0177 390 TYR C CA  
11601 C C   . TYR C 390 ? 0.3732 0.3138 0.6005 0.0323  -0.0572 -0.0153 390 TYR C C   
11602 O O   . TYR C 390 ? 0.3502 0.2849 0.5739 0.0317  -0.0620 -0.0103 390 TYR C O   
11603 C CB  . TYR C 390 ? 0.3778 0.3390 0.6242 0.0363  -0.0562 -0.0186 390 TYR C CB  
11604 C CG  . TYR C 390 ? 0.3725 0.3478 0.6274 0.0367  -0.0525 -0.0208 390 TYR C CG  
11605 C CD1 . TYR C 390 ? 0.3832 0.3655 0.6395 0.0331  -0.0545 -0.0174 390 TYR C CD1 
11606 C CD2 . TYR C 390 ? 0.4139 0.3949 0.6756 0.0407  -0.0467 -0.0262 390 TYR C CD2 
11607 C CE1 . TYR C 390 ? 0.3863 0.3816 0.6516 0.0330  -0.0505 -0.0188 390 TYR C CE1 
11608 C CE2 . TYR C 390 ? 0.4377 0.4316 0.7074 0.0413  -0.0421 -0.0277 390 TYR C CE2 
11609 C CZ  . TYR C 390 ? 0.4211 0.4226 0.6932 0.0372  -0.0438 -0.0236 390 TYR C CZ  
11610 O OH  . TYR C 390 ? 0.4256 0.4399 0.7065 0.0374  -0.0385 -0.0246 390 TYR C OH  
11611 N N   . ASP C 391 ? 0.3893 0.3250 0.6171 0.0337  -0.0546 -0.0190 391 ASP C N   
11612 C CA  . ASP C 391 ? 0.3817 0.3051 0.6076 0.0343  -0.0565 -0.0170 391 ASP C CA  
11613 C C   . ASP C 391 ? 0.3904 0.3115 0.6267 0.0399  -0.0595 -0.0178 391 ASP C C   
11614 O O   . ASP C 391 ? 0.3677 0.2974 0.6126 0.0431  -0.0601 -0.0192 391 ASP C O   
11615 C CB  . ASP C 391 ? 0.3722 0.2911 0.5947 0.0323  -0.0531 -0.0203 391 ASP C CB  
11616 C CG  . ASP C 391 ? 0.3541 0.2761 0.5822 0.0352  -0.0507 -0.0278 391 ASP C CG  
11617 O OD1 . ASP C 391 ? 0.3553 0.2815 0.5913 0.0399  -0.0508 -0.0306 391 ASP C OD1 
11618 O OD2 . ASP C 391 ? 0.3509 0.2712 0.5749 0.0328  -0.0486 -0.0309 391 ASP C OD2 
11619 N N   . SER C 392 ? 0.3908 0.3004 0.6272 0.0411  -0.0610 -0.0165 392 SER C N   
11620 C CA  . SER C 392 ? 0.4149 0.3202 0.6607 0.0466  -0.0644 -0.0164 392 SER C CA  
11621 C C   . SER C 392 ? 0.4092 0.3183 0.6643 0.0511  -0.0614 -0.0241 392 SER C C   
11622 O O   . SER C 392 ? 0.3846 0.2926 0.6493 0.0566  -0.0634 -0.0248 392 SER C O   
11623 C CB  . SER C 392 ? 0.4198 0.3103 0.6628 0.0464  -0.0669 -0.0119 392 SER C CB  
11624 O OG  . SER C 392 ? 0.3983 0.2824 0.6386 0.0436  -0.0638 -0.0146 392 SER C OG  
11625 N N   . ASP C 393 ? 0.4229 0.3362 0.6745 0.0493  -0.0568 -0.0299 393 ASP C N   
11626 C CA  . ASP C 393 ? 0.4251 0.3423 0.6828 0.0539  -0.0533 -0.0376 393 ASP C CA  
11627 C C   . ASP C 393 ? 0.4056 0.3377 0.6676 0.0554  -0.0501 -0.0390 393 ASP C C   
11628 O O   . ASP C 393 ? 0.3737 0.3103 0.6392 0.0593  -0.0458 -0.0452 393 ASP C O   
11629 C CB  . ASP C 393 ? 0.4564 0.3675 0.7074 0.0516  -0.0510 -0.0432 393 ASP C CB  
11630 C CG  . ASP C 393 ? 0.5110 0.4075 0.7630 0.0515  -0.0542 -0.0428 393 ASP C CG  
11631 O OD1 . ASP C 393 ? 0.5289 0.4194 0.7886 0.0560  -0.0568 -0.0413 393 ASP C OD1 
11632 O OD2 . ASP C 393 ? 0.5542 0.4456 0.8004 0.0470  -0.0541 -0.0437 393 ASP C OD2 
11633 N N   . ASN C 394 ? 0.4022 0.3413 0.6632 0.0524  -0.0519 -0.0334 394 ASN C N   
11634 C CA  . ASN C 394 ? 0.4050 0.3583 0.6720 0.0531  -0.0493 -0.0339 394 ASN C CA  
11635 C C   . ASN C 394 ? 0.3940 0.3529 0.6533 0.0503  -0.0432 -0.0382 394 ASN C C   
11636 O O   . ASN C 394 ? 0.3662 0.3351 0.6304 0.0525  -0.0383 -0.0412 394 ASN C O   
11637 C CB  . ASN C 394 ? 0.4137 0.3715 0.6960 0.0603  -0.0493 -0.0355 394 ASN C CB  
11638 C CG  . ASN C 394 ? 0.4252 0.3976 0.7183 0.0609  -0.0491 -0.0329 394 ASN C CG  
11639 O OD1 . ASN C 394 ? 0.4084 0.3842 0.6988 0.0562  -0.0528 -0.0277 394 ASN C OD1 
11640 N ND2 . ASN C 394 ? 0.4385 0.4195 0.7442 0.0666  -0.0445 -0.0366 394 ASN C ND2 
11641 N N   . LYS C 395 ? 0.4267 0.3787 0.6742 0.0456  -0.0432 -0.0383 395 LYS C N   
11642 C CA  . LYS C 395 ? 0.4861 0.4421 0.7247 0.0422  -0.0390 -0.0408 395 LYS C CA  
11643 C C   . LYS C 395 ? 0.4303 0.3893 0.6630 0.0365  -0.0403 -0.0351 395 LYS C C   
11644 O O   . LYS C 395 ? 0.4071 0.3593 0.6367 0.0341  -0.0442 -0.0304 395 LYS C O   
11645 C CB  . LYS C 395 ? 0.6071 0.5533 0.8377 0.0406  -0.0391 -0.0443 395 LYS C CB  
11646 C CG  . LYS C 395 ? 0.7506 0.6917 0.9833 0.0454  -0.0377 -0.0516 395 LYS C CG  
11647 C CD  . LYS C 395 ? 0.8792 0.8290 1.1119 0.0489  -0.0318 -0.0570 395 LYS C CD  
11648 C CE  . LYS C 395 ? 0.9060 0.8496 1.1349 0.0529  -0.0295 -0.0654 395 LYS C CE  
11649 N NZ  . LYS C 395 ? 0.8784 0.8144 1.1158 0.0582  -0.0314 -0.0676 395 LYS C NZ  
11650 N N   . ILE C 396 ? 0.4164 0.3845 0.6466 0.0345  -0.0365 -0.0357 396 ILE C N   
11651 C CA  . ILE C 396 ? 0.3946 0.3654 0.6193 0.0293  -0.0373 -0.0309 396 ILE C CA  
11652 C C   . ILE C 396 ? 0.3635 0.3264 0.5774 0.0256  -0.0376 -0.0301 396 ILE C C   
11653 O O   . ILE C 396 ? 0.3956 0.3566 0.6055 0.0258  -0.0355 -0.0341 396 ILE C O   
11654 C CB  . ILE C 396 ? 0.3891 0.3716 0.6159 0.0283  -0.0331 -0.0311 396 ILE C CB  
11655 C CG1 . ILE C 396 ? 0.4279 0.4191 0.6689 0.0314  -0.0338 -0.0300 396 ILE C CG1 
11656 C CG2 . ILE C 396 ? 0.3705 0.3535 0.5898 0.0227  -0.0338 -0.0269 396 ILE C CG2 
11657 C CD1 . ILE C 396 ? 0.4301 0.4340 0.6775 0.0318  -0.0281 -0.0309 396 ILE C CD1 
11658 N N   . ILE C 397 ? 0.3416 0.2990 0.5509 0.0225  -0.0405 -0.0251 397 ILE C N   
11659 C CA  . ILE C 397 ? 0.3480 0.2985 0.5491 0.0193  -0.0401 -0.0238 397 ILE C CA  
11660 C C   . ILE C 397 ? 0.3237 0.2766 0.5179 0.0153  -0.0388 -0.0206 397 ILE C C   
11661 O O   . ILE C 397 ? 0.3007 0.2502 0.4892 0.0129  -0.0375 -0.0198 397 ILE C O   
11662 C CB  . ILE C 397 ? 0.3631 0.3031 0.5635 0.0194  -0.0430 -0.0206 397 ILE C CB  
11663 C CG1 . ILE C 397 ? 0.3705 0.3079 0.5693 0.0191  -0.0461 -0.0157 397 ILE C CG1 
11664 C CG2 . ILE C 397 ? 0.3892 0.3251 0.5961 0.0229  -0.0440 -0.0242 397 ILE C CG2 
11665 C CD1 . ILE C 397 ? 0.3876 0.3138 0.5832 0.0191  -0.0481 -0.0116 397 ILE C CD1 
11666 N N   . LYS C 398 ? 0.3515 0.3099 0.5472 0.0146  -0.0396 -0.0187 398 LYS C N   
11667 C CA  . LYS C 398 ? 0.3193 0.2796 0.5088 0.0108  -0.0385 -0.0162 398 LYS C CA  
11668 C C   . LYS C 398 ? 0.3350 0.3048 0.5306 0.0105  -0.0384 -0.0162 398 LYS C C   
11669 O O   . LYS C 398 ? 0.3307 0.3030 0.5340 0.0124  -0.0414 -0.0157 398 LYS C O   
11670 C CB  . LYS C 398 ? 0.3051 0.2564 0.4873 0.0088  -0.0411 -0.0118 398 LYS C CB  
11671 C CG  . LYS C 398 ? 0.2966 0.2473 0.4711 0.0052  -0.0399 -0.0095 398 LYS C CG  
11672 C CD  . LYS C 398 ? 0.2883 0.2292 0.4537 0.0037  -0.0422 -0.0057 398 LYS C CD  
11673 C CE  . LYS C 398 ? 0.2861 0.2264 0.4446 0.0005  -0.0407 -0.0044 398 LYS C CE  
11674 N NZ  . LYS C 398 ? 0.2898 0.2192 0.4371 -0.0007 -0.0422 -0.0014 398 LYS C NZ  
11675 N N   . ASN C 399 ? 0.3533 0.3284 0.5464 0.0083  -0.0350 -0.0165 399 ASN C N   
11676 C CA  . ASN C 399 ? 0.3532 0.3362 0.5510 0.0063  -0.0345 -0.0150 399 ASN C CA  
11677 C C   . ASN C 399 ? 0.3455 0.3236 0.5351 0.0020  -0.0359 -0.0116 399 ASN C C   
11678 O O   . ASN C 399 ? 0.3709 0.3436 0.5518 0.0008  -0.0340 -0.0112 399 ASN C O   
11679 C CB  . ASN C 399 ? 0.3569 0.3484 0.5566 0.0067  -0.0289 -0.0173 399 ASN C CB  
11680 C CG  . ASN C 399 ? 0.3619 0.3582 0.5689 0.0115  -0.0266 -0.0213 399 ASN C CG  
11681 O OD1 . ASN C 399 ? 0.3568 0.3514 0.5591 0.0134  -0.0238 -0.0248 399 ASN C OD1 
11682 N ND2 . ASN C 399 ? 0.3758 0.3778 0.5945 0.0135  -0.0280 -0.0209 399 ASN C ND2 
11683 N N   . GLU C 400 ? 0.3434 0.3230 0.5362 -0.0003 -0.0395 -0.0092 400 GLU C N   
11684 C CA  . GLU C 400 ? 0.3530 0.3276 0.5377 -0.0046 -0.0406 -0.0066 400 GLU C CA  
11685 C C   . GLU C 400 ? 0.3587 0.3399 0.5514 -0.0076 -0.0431 -0.0049 400 GLU C C   
11686 O O   . GLU C 400 ? 0.3748 0.3602 0.5770 -0.0067 -0.0473 -0.0046 400 GLU C O   
11687 C CB  . GLU C 400 ? 0.3561 0.3177 0.5295 -0.0048 -0.0437 -0.0050 400 GLU C CB  
11688 C CG  . GLU C 400 ? 0.3765 0.3312 0.5398 -0.0085 -0.0437 -0.0031 400 GLU C CG  
11689 C CD  . GLU C 400 ? 0.4026 0.3437 0.5527 -0.0085 -0.0451 -0.0015 400 GLU C CD  
11690 O OE1 . GLU C 400 ? 0.3501 0.2864 0.4984 -0.0061 -0.0470 -0.0012 400 GLU C OE1 
11691 O OE2 . GLU C 400 ? 0.4489 0.3838 0.5903 -0.0109 -0.0439 -0.0005 400 GLU C OE2 
11692 N N   . SER C 401 ? 0.3417 0.3243 0.5320 -0.0113 -0.0407 -0.0036 401 SER C N   
11693 C CA  . SER C 401 ? 0.3320 0.3202 0.5305 -0.0151 -0.0431 -0.0016 401 SER C CA  
11694 C C   . SER C 401 ? 0.3427 0.3198 0.5321 -0.0188 -0.0492 0.0001  401 SER C C   
11695 O O   . SER C 401 ? 0.3415 0.3077 0.5170 -0.0193 -0.0482 0.0002  401 SER C O   
11696 C CB  . SER C 401 ? 0.3386 0.3340 0.5400 -0.0173 -0.0370 -0.0007 401 SER C CB  
11697 O OG  . SER C 401 ? 0.3439 0.3499 0.5535 -0.0142 -0.0313 -0.0023 401 SER C OG  
11698 N N   . ILE C 402 ? 0.3319 0.3116 0.5296 -0.0212 -0.0558 0.0013  402 ILE C N   
11699 C CA  . ILE C 402 ? 0.3433 0.3131 0.5330 -0.0256 -0.0620 0.0026  402 ILE C CA  
11700 C C   . ILE C 402 ? 0.3271 0.3053 0.5292 -0.0307 -0.0631 0.0044  402 ILE C C   
11701 O O   . ILE C 402 ? 0.3158 0.3053 0.5347 -0.0310 -0.0657 0.0052  402 ILE C O   
11702 C CB  . ILE C 402 ? 0.3675 0.3297 0.5531 -0.0246 -0.0710 0.0027  402 ILE C CB  
11703 C CG1 . ILE C 402 ? 0.3685 0.3222 0.5426 -0.0199 -0.0695 0.0017  402 ILE C CG1 
11704 C CG2 . ILE C 402 ? 0.3942 0.3449 0.5696 -0.0294 -0.0781 0.0034  402 ILE C CG2 
11705 C CD1 . ILE C 402 ? 0.3804 0.3210 0.5362 -0.0201 -0.0655 0.0014  402 ILE C CD1 
11706 N N   . ASN C 403 ? 0.3363 0.3088 0.5311 -0.0346 -0.0609 0.0053  403 ASN C N   
11707 C CA  . ASN C 403 ? 0.3092 0.2883 0.5151 -0.0400 -0.0610 0.0075  403 ASN C CA  
11708 C C   . ASN C 403 ? 0.2941 0.2646 0.4980 -0.0450 -0.0712 0.0080  403 ASN C C   
11709 O O   . ASN C 403 ? 0.2828 0.2376 0.4695 -0.0462 -0.0740 0.0070  403 ASN C O   
11710 C CB  . ASN C 403 ? 0.3173 0.2940 0.5165 -0.0416 -0.0536 0.0086  403 ASN C CB  
11711 C CG  . ASN C 403 ? 0.3198 0.3061 0.5220 -0.0376 -0.0444 0.0084  403 ASN C CG  
11712 O OD1 . ASN C 403 ? 0.3394 0.3391 0.5557 -0.0375 -0.0406 0.0095  403 ASN C OD1 
11713 N ND2 . ASN C 403 ? 0.3394 0.3191 0.5287 -0.0339 -0.0408 0.0068  403 ASN C ND2 
11714 N N   . ILE C 404 ? 0.2871 0.2680 0.5093 -0.0481 -0.0763 0.0096  404 ILE C N   
11715 C CA  . ILE C 404 ? 0.2959 0.2698 0.5186 -0.0536 -0.0873 0.0101  404 ILE C CA  
11716 C C   . ILE C 404 ? 0.2950 0.2792 0.5364 -0.0599 -0.0873 0.0131  404 ILE C C   
11717 O O   . ILE C 404 ? 0.2730 0.2719 0.5291 -0.0592 -0.0789 0.0151  404 ILE C O   
11718 C CB  . ILE C 404 ? 0.3003 0.2746 0.5270 -0.0517 -0.0974 0.0095  404 ILE C CB  
11719 C CG1 . ILE C 404 ? 0.2904 0.2845 0.5442 -0.0511 -0.0979 0.0116  404 ILE C CG1 
11720 C CG2 . ILE C 404 ? 0.3177 0.2827 0.5270 -0.0452 -0.0954 0.0073  404 ILE C CG2 
11721 C CD1 . ILE C 404 ? 0.3012 0.2962 0.5611 -0.0492 -0.1089 0.0116  404 ILE C CD1 
11722 N N   . LEU C 405 ? 0.3053 0.2802 0.5445 -0.0660 -0.0971 0.0132  405 LEU C N   
11723 C CA  . LEU C 405 ? 0.3111 0.2938 0.5691 -0.0733 -0.1002 0.0162  405 LEU C CA  
11724 C C   . LEU C 405 ? 0.3175 0.3016 0.5863 -0.0762 -0.1144 0.0163  405 LEU C C   
11725 O O   . LEU C 405 ? 0.3382 0.3061 0.5903 -0.0773 -0.1245 0.0138  405 LEU C O   
11726 C CB  . LEU C 405 ? 0.3189 0.2871 0.5634 -0.0783 -0.0992 0.0162  405 LEU C CB  
11727 C CG  . LEU C 405 ? 0.3271 0.3016 0.5897 -0.0865 -0.1006 0.0198  405 LEU C CG  
11728 C CD1 . LEU C 405 ? 0.3135 0.3092 0.5980 -0.0857 -0.0898 0.0238  405 LEU C CD1 
11729 C CD2 . LEU C 405 ? 0.3388 0.2962 0.5858 -0.0909 -0.0998 0.0194  405 LEU C CD2 
11730 N N   . ALA C 406 ? 0.3085 0.3118 0.6052 -0.0774 -0.1154 0.0193  406 ALA C N   
11731 C CA  . ALA C 406 ? 0.3133 0.3197 0.6213 -0.0783 -0.1290 0.0195  406 ALA C CA  
11732 C C   . ALA C 406 ? 0.3071 0.3268 0.6438 -0.0858 -0.1344 0.0233  406 ALA C C   
11733 O O   . ALA C 406 ? 0.2936 0.3270 0.6480 -0.0880 -0.1247 0.0266  406 ALA C O   
11734 C CB  . ALA C 406 ? 0.3053 0.3223 0.6200 -0.0702 -0.1264 0.0191  406 ALA C CB  
11735 N N   . SER C 407 ? 0.3256 0.3407 0.6663 -0.0897 -0.1504 0.0230  407 SER C N   
11736 C CA  . SER C 407 ? 0.3303 0.3588 0.7012 -0.0969 -0.1584 0.0268  407 SER C CA  
11737 C C   . SER C 407 ? 0.3441 0.3699 0.7188 -0.0975 -0.1765 0.0261  407 SER C C   
11738 O O   . SER C 407 ? 0.3557 0.3632 0.7036 -0.0948 -0.1840 0.0225  407 SER C O   
11739 C CB  . SER C 407 ? 0.3310 0.3513 0.7007 -0.1061 -0.1597 0.0276  407 SER C CB  
11740 O OG  . SER C 407 ? 0.3233 0.3553 0.7226 -0.1137 -0.1697 0.0312  407 SER C OG  
11741 N N   . LYS C 408 ? 0.3595 0.4040 0.7679 -0.1006 -0.1830 0.0301  408 LYS C N   
11742 C CA  . LYS C 408 ? 0.3915 0.4343 0.8069 -0.1024 -0.2022 0.0302  408 LYS C CA  
11743 C C   . LYS C 408 ? 0.4195 0.4480 0.8295 -0.1128 -0.2168 0.0292  408 LYS C C   
11744 O O   . LYS C 408 ? 0.4440 0.4667 0.8542 -0.1154 -0.2347 0.0287  408 LYS C O   
11745 C CB  . LYS C 408 ? 0.4006 0.4700 0.8583 -0.1024 -0.2048 0.0353  408 LYS C CB  
11746 C CG  . LYS C 408 ? 0.4121 0.4965 0.8795 -0.0921 -0.1931 0.0362  408 LYS C CG  
11747 C CD  . LYS C 408 ? 0.4368 0.5489 0.9481 -0.0917 -0.1917 0.0414  408 LYS C CD  
11748 C CE  . LYS C 408 ? 0.4736 0.5969 0.9895 -0.0807 -0.1796 0.0412  408 LYS C CE  
11749 N NZ  . LYS C 408 ? 0.5100 0.6605 1.0672 -0.0797 -0.1723 0.0461  408 LYS C NZ  
11750 N N   . THR C 409 ? 0.4218 0.4449 0.8283 -0.1189 -0.2099 0.0293  409 THR C N   
11751 C CA  . THR C 409 ? 0.4532 0.4610 0.8538 -0.1288 -0.2237 0.0279  409 THR C CA  
11752 C C   . THR C 409 ? 0.4690 0.4523 0.8332 -0.1290 -0.2172 0.0235  409 THR C C   
11753 O O   . THR C 409 ? 0.4462 0.4282 0.7956 -0.1224 -0.2015 0.0225  409 THR C O   
11754 C CB  . THR C 409 ? 0.4449 0.4704 0.8840 -0.1382 -0.2259 0.0332  409 THR C CB  
11755 O OG1 . THR C 409 ? 0.4267 0.4641 0.8765 -0.1377 -0.2065 0.0365  409 THR C OG1 
11756 C CG2 . THR C 409 ? 0.4369 0.4863 0.9135 -0.1379 -0.2337 0.0377  409 THR C CG2 
11757 N N   . ALA C 410 ? 0.4986 0.4609 0.8465 -0.1359 -0.2310 0.0202  410 ALA C N   
11758 C CA  . ALA C 410 ? 0.5183 0.4566 0.8343 -0.1369 -0.2261 0.0160  410 ALA C CA  
11759 C C   . ALA C 410 ? 0.5022 0.4503 0.8341 -0.1406 -0.2117 0.0198  410 ALA C C   
11760 O O   . ALA C 410 ? 0.5007 0.4703 0.8675 -0.1451 -0.2104 0.0251  410 ALA C O   
11761 C CB  . ALA C 410 ? 0.5510 0.4663 0.8508 -0.1443 -0.2444 0.0119  410 ALA C CB  
11762 N N   . PHE C 411 ? 0.4998 0.4325 0.8066 -0.1384 -0.2008 0.0174  411 PHE C N   
11763 C CA  . PHE C 411 ? 0.4844 0.4212 0.8014 -0.1428 -0.1891 0.0208  411 PHE C CA  
11764 C C   . PHE C 411 ? 0.4996 0.4097 0.7841 -0.1429 -0.1863 0.0165  411 PHE C C   
11765 O O   . PHE C 411 ? 0.4964 0.3890 0.7509 -0.1372 -0.1882 0.0114  411 PHE C O   
11766 C CB  . PHE C 411 ? 0.4493 0.4088 0.7818 -0.1365 -0.1713 0.0252  411 PHE C CB  
11767 C CG  . PHE C 411 ? 0.4392 0.3956 0.7491 -0.1254 -0.1618 0.0223  411 PHE C CG  
11768 C CD1 . PHE C 411 ? 0.4267 0.3900 0.7374 -0.1191 -0.1659 0.0210  411 PHE C CD1 
11769 C CD2 . PHE C 411 ? 0.4523 0.3993 0.7420 -0.1215 -0.1488 0.0213  411 PHE C CD2 
11770 C CE1 . PHE C 411 ? 0.4236 0.3838 0.7149 -0.1096 -0.1571 0.0186  411 PHE C CE1 
11771 C CE2 . PHE C 411 ? 0.4207 0.3659 0.6924 -0.1119 -0.1404 0.0189  411 PHE C CE2 
11772 C CZ  . PHE C 411 ? 0.4158 0.3674 0.6883 -0.1063 -0.1445 0.0175  411 PHE C CZ  
11773 N N   . GLU C 412 ? 0.5161 0.4234 0.8077 -0.1493 -0.1815 0.0191  412 GLU C N   
11774 C CA  . GLU C 412 ? 0.5557 0.4389 0.8198 -0.1492 -0.1774 0.0158  412 GLU C CA  
11775 C C   . GLU C 412 ? 0.5087 0.3965 0.7633 -0.1412 -0.1588 0.0175  412 GLU C C   
11776 O O   . GLU C 412 ? 0.4660 0.3734 0.7408 -0.1408 -0.1475 0.0230  412 GLU C O   
11777 C CB  . GLU C 412 ? 0.5905 0.4656 0.8644 -0.1597 -0.1810 0.0178  412 GLU C CB  
11778 C CG  . GLU C 412 ? 0.6631 0.5329 0.9482 -0.1691 -0.2006 0.0163  412 GLU C CG  
11779 C CD  . GLU C 412 ? 0.7773 0.6434 1.0796 -0.1806 -0.2040 0.0196  412 GLU C CD  
11780 O OE1 . GLU C 412 ? 0.7714 0.6397 1.0793 -0.1821 -0.1912 0.0239  412 GLU C OE1 
11781 O OE2 . GLU C 412 ? 0.8555 0.7154 1.1657 -0.1887 -0.2212 0.0178  412 GLU C OE2 
11782 N N   . LEU C 413 ? 0.5212 0.3897 0.7442 -0.1348 -0.1559 0.0125  413 LEU C N   
11783 C CA  . LEU C 413 ? 0.5186 0.3855 0.7290 -0.1282 -0.1404 0.0134  413 LEU C CA  
11784 C C   . LEU C 413 ? 0.5212 0.3704 0.7228 -0.1330 -0.1387 0.0135  413 LEU C C   
11785 O O   . LEU C 413 ? 0.5410 0.3745 0.7385 -0.1397 -0.1501 0.0109  413 LEU C O   
11786 C CB  . LEU C 413 ? 0.5260 0.3818 0.7092 -0.1188 -0.1378 0.0086  413 LEU C CB  
11787 C CG  . LEU C 413 ? 0.5305 0.4003 0.7182 -0.1130 -0.1390 0.0082  413 LEU C CG  
11788 C CD1 . LEU C 413 ? 0.5475 0.4010 0.7058 -0.1055 -0.1388 0.0032  413 LEU C CD1 
11789 C CD2 . LEU C 413 ? 0.5214 0.4149 0.7275 -0.1090 -0.1264 0.0128  413 LEU C CD2 
11790 N N   . PRO C 414 ? 0.5161 0.3667 0.7143 -0.1296 -0.1250 0.0165  414 PRO C N   
11791 C CA  . PRO C 414 ? 0.5383 0.3685 0.7220 -0.1315 -0.1226 0.0158  414 PRO C CA  
11792 C C   . PRO C 414 ? 0.5342 0.3421 0.6864 -0.1249 -0.1239 0.0090  414 PRO C C   
11793 O O   . PRO C 414 ? 0.5450 0.3574 0.6879 -0.1174 -0.1212 0.0068  414 PRO C O   
11794 C CB  . PRO C 414 ? 0.5299 0.3729 0.7225 -0.1290 -0.1077 0.0220  414 PRO C CB  
11795 C CG  . PRO C 414 ? 0.5109 0.3725 0.7067 -0.1213 -0.1011 0.0225  414 PRO C CG  
11796 C CD  . PRO C 414 ? 0.5117 0.3831 0.7201 -0.1238 -0.1117 0.0208  414 PRO C CD  
11797 N N   . GLU C 415 ? 0.5541 0.3378 0.6909 -0.1279 -0.1281 0.0058  415 GLU C N   
11798 C CA  . GLU C 415 ? 0.5805 0.3398 0.6870 -0.1230 -0.1310 -0.0012 415 GLU C CA  
11799 C C   . GLU C 415 ? 0.5611 0.3023 0.6533 -0.1208 -0.1233 -0.0015 415 GLU C C   
11800 O O   . GLU C 415 ? 0.5435 0.2783 0.6436 -0.1273 -0.1246 0.0007  415 GLU C O   
11801 C CB  . GLU C 415 ? 0.6396 0.3801 0.7356 -0.1288 -0.1469 -0.0069 415 GLU C CB  
11802 C CG  . GLU C 415 ? 0.6924 0.4467 0.8009 -0.1316 -0.1580 -0.0071 415 GLU C CG  
11803 C CD  . GLU C 415 ? 0.8044 0.5426 0.9085 -0.1398 -0.1757 -0.0115 415 GLU C CD  
11804 O OE1 . GLU C 415 ? 0.7475 0.4727 0.8540 -0.1472 -0.1802 -0.0119 415 GLU C OE1 
11805 O OE2 . GLU C 415 ? 0.8744 0.6134 0.9732 -0.1387 -0.1856 -0.0143 415 GLU C OE2 
11806 N N   . LEU C 416 ? 0.5637 0.2967 0.6357 -0.1114 -0.1154 -0.0042 416 LEU C N   
11807 C CA  . LEU C 416 ? 0.5798 0.2949 0.6364 -0.1074 -0.1077 -0.0051 416 LEU C CA  
11808 C C   . LEU C 416 ? 0.5974 0.2859 0.6251 -0.1038 -0.1123 -0.0130 416 LEU C C   
11809 O O   . LEU C 416 ? 0.6013 0.2901 0.6163 -0.0975 -0.1112 -0.0159 416 LEU C O   
11810 C CB  . LEU C 416 ? 0.5503 0.2802 0.6098 -0.0990 -0.0940 -0.0011 416 LEU C CB  
11811 C CG  . LEU C 416 ? 0.5484 0.2655 0.5975 -0.0939 -0.0845 -0.0001 416 LEU C CG  
11812 C CD1 . LEU C 416 ? 0.5288 0.2655 0.5885 -0.0885 -0.0734 0.0056  416 LEU C CD1 
11813 C CD2 . LEU C 416 ? 0.5712 0.2659 0.5940 -0.0870 -0.0832 -0.0065 416 LEU C CD2 
11814 N N   . THR C 417 ? 0.6111 0.2757 0.6275 -0.1073 -0.1164 -0.0162 417 THR C N   
11815 C CA  . THR C 417 ? 0.6320 0.2685 0.6184 -0.1032 -0.1190 -0.0240 417 THR C CA  
11816 C C   . THR C 417 ? 0.6225 0.2422 0.5993 -0.0991 -0.1098 -0.0240 417 THR C C   
11817 O O   . THR C 417 ? 0.6088 0.2349 0.6021 -0.1026 -0.1061 -0.0186 417 THR C O   
11818 C CB  . THR C 417 ? 0.6761 0.2963 0.6547 -0.1113 -0.1354 -0.0295 417 THR C CB  
11819 O OG1 . THR C 417 ? 0.6805 0.2985 0.6754 -0.1212 -0.1416 -0.0272 417 THR C OG1 
11820 C CG2 . THR C 417 ? 0.6775 0.3144 0.6652 -0.1141 -0.1448 -0.0293 417 THR C CG2 
11821 N N   . ILE C 418 ? 0.6436 0.2422 0.5942 -0.0913 -0.1054 -0.0296 418 ILE C N   
11822 C CA  . ILE C 418 ? 0.6800 0.2611 0.6210 -0.0865 -0.0967 -0.0301 418 ILE C CA  
11823 C C   . ILE C 418 ? 0.7131 0.2602 0.6261 -0.0861 -0.1022 -0.0389 418 ILE C C   
11824 O O   . ILE C 418 ? 0.7231 0.2603 0.6186 -0.0861 -0.1096 -0.0447 418 ILE C O   
11825 C CB  . ILE C 418 ? 0.6563 0.2474 0.5965 -0.0755 -0.0818 -0.0269 418 ILE C CB  
11826 C CG1 . ILE C 418 ? 0.6823 0.2688 0.6028 -0.0678 -0.0789 -0.0315 418 ILE C CG1 
11827 C CG2 . ILE C 418 ? 0.6109 0.2333 0.5775 -0.0764 -0.0768 -0.0186 418 ILE C CG2 
11828 C CD1 . ILE C 418 ? 0.6726 0.2707 0.5952 -0.0577 -0.0648 -0.0279 418 ILE C CD1 
11829 N N   . GLU C 419 ? 0.7382 0.2668 0.6470 -0.0859 -0.0991 -0.0395 419 GLU C N   
11830 C CA  . GLU C 419 ? 0.7845 0.2784 0.6657 -0.0837 -0.1014 -0.0479 419 GLU C CA  
11831 C C   . GLU C 419 ? 0.7586 0.2438 0.6321 -0.0729 -0.0862 -0.0470 419 GLU C C   
11832 O O   . GLU C 419 ? 0.7498 0.2429 0.6405 -0.0729 -0.0802 -0.0407 419 GLU C O   
11833 C CB  . GLU C 419 ? 0.8330 0.3091 0.7171 -0.0939 -0.1122 -0.0499 419 GLU C CB  
11834 C CG  . GLU C 419 ? 0.8751 0.3585 0.7698 -0.1057 -0.1285 -0.0506 419 GLU C CG  
11835 C CD  . GLU C 419 ? 0.9761 0.4360 0.8686 -0.1152 -0.1399 -0.0543 419 GLU C CD  
11836 O OE1 . GLU C 419 ? 1.0231 0.4813 0.9307 -0.1194 -0.1375 -0.0497 419 GLU C OE1 
11837 O OE2 . GLU C 419 ? 1.0806 0.5206 0.9531 -0.1183 -0.1517 -0.0624 419 GLU C OE2 
11838 N N   . VAL C 420 ? 0.7599 0.2303 0.6089 -0.0634 -0.0797 -0.0525 420 VAL C N   
11839 C CA  . VAL C 420 ? 0.7431 0.2091 0.5870 -0.0520 -0.0644 -0.0512 420 VAL C CA  
11840 C C   . VAL C 420 ? 0.7686 0.1978 0.5860 -0.0482 -0.0633 -0.0592 420 VAL C C   
11841 O O   . VAL C 420 ? 0.7752 0.1837 0.5683 -0.0494 -0.0705 -0.0673 420 VAL C O   
11842 C CB  . VAL C 420 ? 0.7332 0.2142 0.5731 -0.0432 -0.0553 -0.0499 420 VAL C CB  
11843 C CG1 . VAL C 420 ? 0.7340 0.2170 0.5770 -0.0323 -0.0395 -0.0465 420 VAL C CG1 
11844 C CG2 . VAL C 420 ? 0.6918 0.2054 0.5533 -0.0478 -0.0590 -0.0440 420 VAL C CG2 
11845 N N   . THR C 421 ? 0.7764 0.1972 0.5990 -0.0438 -0.0550 -0.0568 421 THR C N   
11846 C CA  . THR C 421 ? 0.8168 0.2040 0.6161 -0.0374 -0.0503 -0.0638 421 THR C CA  
11847 C C   . THR C 421 ? 0.8221 0.2131 0.6211 -0.0239 -0.0331 -0.0610 421 THR C C   
11848 O O   . THR C 421 ? 0.7888 0.2051 0.6116 -0.0218 -0.0266 -0.0524 421 THR C O   
11849 C CB  . THR C 421 ? 0.8273 0.1999 0.6349 -0.0436 -0.0552 -0.0628 421 THR C CB  
11850 O OG1 . THR C 421 ? 0.8357 0.2120 0.6481 -0.0564 -0.0709 -0.0641 421 THR C OG1 
11851 C CG2 . THR C 421 ? 0.8571 0.1927 0.6406 -0.0375 -0.0513 -0.0706 421 THR C CG2 
11852 N N   . PRO C 422 ? 0.8600 0.2270 0.6325 -0.0144 -0.0251 -0.0680 422 PRO C N   
11853 C CA  . PRO C 422 ? 0.8971 0.2402 0.6379 -0.0153 -0.0316 -0.0781 422 PRO C CA  
11854 C C   . PRO C 422 ? 0.8818 0.2432 0.6208 -0.0190 -0.0378 -0.0777 422 PRO C C   
11855 O O   . PRO C 422 ? 0.8566 0.2458 0.6121 -0.0158 -0.0311 -0.0710 422 PRO C O   
11856 C CB  . PRO C 422 ? 0.9237 0.2466 0.6426 -0.0016 -0.0166 -0.0826 422 PRO C CB  
11857 C CG  . PRO C 422 ? 0.9128 0.2384 0.6508 0.0038  -0.0068 -0.0770 422 PRO C CG  
11858 C CD  . PRO C 422 ? 0.8622 0.2244 0.6346 -0.0017 -0.0091 -0.0663 422 PRO C CD  
11859 N N   . GLU C 423 ? 0.9225 0.2662 0.6403 -0.0254 -0.0508 -0.0851 423 GLU C N   
11860 C CA  . GLU C 423 ? 0.9382 0.2976 0.6575 -0.0323 -0.0619 -0.0846 423 GLU C CA  
11861 C C   . GLU C 423 ? 0.9547 0.3108 0.6506 -0.0240 -0.0551 -0.0876 423 GLU C C   
11862 O O   . GLU C 423 ? 0.9152 0.2946 0.6210 -0.0256 -0.0573 -0.0834 423 GLU C O   
11863 C CB  . GLU C 423 ? 0.9869 0.3267 0.6953 -0.0433 -0.0802 -0.0911 423 GLU C CB  
11864 C CG  . GLU C 423 ? 0.9905 0.3439 0.7020 -0.0522 -0.0952 -0.0910 423 GLU C CG  
11865 C CD  . GLU C 423 ? 1.0327 0.3622 0.7312 -0.0624 -0.1134 -0.0982 423 GLU C CD  
11866 O OE1 . GLU C 423 ? 1.0223 0.3267 0.7128 -0.0641 -0.1153 -0.1028 423 GLU C OE1 
11867 O OE2 . GLU C 423 ? 1.0656 0.4020 0.7627 -0.0688 -0.1265 -0.0992 423 GLU C OE2 
11868 N N   . LYS C 424 ? 1.0048 0.3317 0.6701 -0.0150 -0.0466 -0.0946 424 LYS C N   
11869 C CA  . LYS C 424 ? 1.0435 0.3596 0.6795 -0.0079 -0.0413 -0.0988 424 LYS C CA  
11870 C C   . LYS C 424 ? 1.0255 0.3300 0.6486 0.0061  -0.0212 -0.0997 424 LYS C C   
11871 O O   . LYS C 424 ? 1.0284 0.3330 0.6359 0.0134  -0.0122 -0.0999 424 LYS C O   
11872 C CB  . LYS C 424 ? 1.1393 0.4230 0.7395 -0.0120 -0.0546 -0.1092 424 LYS C CB  
11873 C CG  . LYS C 424 ? 1.1888 0.4811 0.7993 -0.0258 -0.0760 -0.1092 424 LYS C CG  
11874 C CD  . LYS C 424 ? 1.2564 0.5206 0.8321 -0.0302 -0.0909 -0.1186 424 LYS C CD  
11875 C CE  . LYS C 424 ? 1.3257 0.5571 0.8850 -0.0339 -0.0988 -0.1270 424 LYS C CE  
11876 N NZ  . LYS C 424 ? 1.4250 0.6312 0.9508 -0.0384 -0.1146 -0.1358 424 LYS C NZ  
11877 N N   . ASP C 425 ? 1.0172 0.3108 0.6465 0.0101  -0.0137 -0.1000 425 ASP C N   
11878 C CA  . ASP C 425 ? 1.0125 0.2922 0.6286 0.0236  0.0051  -0.1016 425 ASP C CA  
11879 C C   . ASP C 425 ? 0.9819 0.2734 0.6272 0.0273  0.0143  -0.0952 425 ASP C C   
11880 O O   . ASP C 425 ? 1.0025 0.2789 0.6503 0.0239  0.0091  -0.0976 425 ASP C O   
11881 C CB  . ASP C 425 ? 1.0507 0.2882 0.6252 0.0274  0.0048  -0.1132 425 ASP C CB  
11882 C CG  . ASP C 425 ? 1.0721 0.2939 0.6298 0.0424  0.0255  -0.1154 425 ASP C CG  
11883 O OD1 . ASP C 425 ? 1.0227 0.2685 0.6051 0.0492  0.0394  -0.1071 425 ASP C OD1 
11884 O OD2 . ASP C 425 ? 1.1298 0.3153 0.6510 0.0471  0.0275  -0.1253 425 ASP C OD2 
11885 N N   . LEU C 426 ? 0.9393 0.2571 0.6062 0.0342  0.0273  -0.0870 426 LEU C N   
11886 C CA  . LEU C 426 ? 0.9237 0.2564 0.6203 0.0380  0.0355  -0.0797 426 LEU C CA  
11887 C C   . LEU C 426 ? 0.9642 0.2692 0.6485 0.0476  0.0464  -0.0841 426 LEU C C   
11888 O O   . LEU C 426 ? 0.9547 0.2655 0.6606 0.0497  0.0502  -0.0792 426 LEU C O   
11889 C CB  . LEU C 426 ? 0.8910 0.2559 0.6110 0.0436  0.0465  -0.0708 426 LEU C CB  
11890 C CG  . LEU C 426 ? 0.8575 0.2538 0.5971 0.0349  0.0372  -0.0648 426 LEU C CG  
11891 C CD1 . LEU C 426 ? 0.8466 0.2695 0.6059 0.0418  0.0493  -0.0572 426 LEU C CD1 
11892 C CD2 . LEU C 426 ? 0.8369 0.2474 0.6003 0.0244  0.0248  -0.0606 426 LEU C CD2 
11893 N N   . ASN C 427 ? 0.9996 0.2738 0.6488 0.0538  0.0516  -0.0932 427 ASN C N   
11894 C CA  . ASN C 427 ? 1.0313 0.2769 0.6676 0.0628  0.0614  -0.0982 427 ASN C CA  
11895 C C   . ASN C 427 ? 1.0604 0.2866 0.6959 0.0548  0.0484  -0.1022 427 ASN C C   
11896 O O   . ASN C 427 ? 1.0979 0.3022 0.7283 0.0614  0.0553  -0.1053 427 ASN C O   
11897 C CB  . ASN C 427 ? 1.0584 0.2728 0.6542 0.0715  0.0703  -0.1078 427 ASN C CB  
11898 C CG  . ASN C 427 ? 1.0354 0.2621 0.6321 0.0834  0.0891  -0.1038 427 ASN C CG  
11899 O OD1 . ASN C 427 ? 1.0381 0.2546 0.6072 0.0862  0.0925  -0.1082 427 ASN C OD1 
11900 N ND2 . ASN C 427 ? 1.0015 0.2479 0.6282 0.0907  0.1016  -0.0956 427 ASN C ND2 
11901 N N   . GLU C 428 ? 1.0636 0.2968 0.7042 0.0409  0.0302  -0.1022 428 GLU C N   
11902 C CA  . GLU C 428 ? 1.1028 0.3161 0.7417 0.0322  0.0171  -0.1063 428 GLU C CA  
11903 C C   . GLU C 428 ? 1.0659 0.2951 0.7394 0.0300  0.0177  -0.0974 428 GLU C C   
11904 O O   . GLU C 428 ? 1.0442 0.2599 0.7208 0.0223  0.0074  -0.0990 428 GLU C O   
11905 C CB  . GLU C 428 ? 1.1446 0.3596 0.7781 0.0179  -0.0027 -0.1091 428 GLU C CB  
11906 C CG  . GLU C 428 ? 1.2332 0.4244 0.8272 0.0190  -0.0065 -0.1193 428 GLU C CG  
11907 C CD  . GLU C 428 ? 1.2983 0.4776 0.8804 0.0054  -0.0280 -0.1252 428 GLU C CD  
11908 O OE1 . GLU C 428 ? 1.3387 0.5232 0.9423 -0.0047 -0.0391 -0.1223 428 GLU C OE1 
11909 O OE2 . GLU C 428 ? 1.3217 0.4875 0.8745 0.0049  -0.0336 -0.1320 428 GLU C OE2 
11910 N N   . GLY C 429 ? 1.0314 0.2897 0.7315 0.0362  0.0288  -0.0876 429 GLY C N   
11911 C CA  . GLY C 429 ? 0.9901 0.2631 0.7211 0.0349  0.0295  -0.0787 429 GLY C CA  
11912 C C   . GLY C 429 ? 0.9609 0.2618 0.7157 0.0441  0.0431  -0.0694 429 GLY C C   
11913 O O   . GLY C 429 ? 0.9841 0.3008 0.7375 0.0485  0.0496  -0.0682 429 GLY C O   
11914 N N   . LYS C 430 ? 0.9403 0.2477 0.7181 0.0463  0.0461  -0.0623 430 LYS C N   
11915 C CA  . LYS C 430 ? 0.9068 0.2437 0.7125 0.0525  0.0550  -0.0519 430 LYS C CA  
11916 C C   . LYS C 430 ? 0.8439 0.2119 0.6752 0.0418  0.0450  -0.0432 430 LYS C C   
11917 O O   . LYS C 430 ? 0.8046 0.2008 0.6573 0.0449  0.0498  -0.0351 430 LYS C O   
11918 C CB  . LYS C 430 ? 0.9497 0.2743 0.7640 0.0624  0.0646  -0.0492 430 LYS C CB  
11919 C CG  . LYS C 430 ? 1.0092 0.3168 0.8084 0.0768  0.0803  -0.0542 430 LYS C CG  
11920 C CD  . LYS C 430 ? 1.1027 0.4000 0.9145 0.0862  0.0885  -0.0505 430 LYS C CD  
11921 C CE  . LYS C 430 ? 1.1978 0.4652 0.9887 0.0992  0.1019  -0.0582 430 LYS C CE  
11922 N NZ  . LYS C 430 ? 1.2682 0.5469 1.0543 0.1077  0.1144  -0.0589 430 LYS C NZ  
11923 N N   . ILE C 431 ? 0.8270 0.1898 0.6565 0.0295  0.0312  -0.0448 431 ILE C N   
11924 C CA  . ILE C 431 ? 0.7893 0.1793 0.6421 0.0194  0.0223  -0.0367 431 ILE C CA  
11925 C C   . ILE C 431 ? 0.7812 0.1757 0.6253 0.0084  0.0105  -0.0409 431 ILE C C   
11926 O O   . ILE C 431 ? 0.7877 0.1578 0.6095 0.0051  0.0045  -0.0497 431 ILE C O   
11927 C CB  . ILE C 431 ? 0.7926 0.1757 0.6585 0.0146  0.0177  -0.0317 431 ILE C CB  
11928 C CG1 . ILE C 431 ? 0.7995 0.1782 0.6744 0.0260  0.0287  -0.0271 431 ILE C CG1 
11929 C CG2 . ILE C 431 ? 0.7671 0.1781 0.6558 0.0043  0.0095  -0.0231 431 ILE C CG2 
11930 C CD1 . ILE C 431 ? 0.8209 0.1818 0.7011 0.0232  0.0251  -0.0244 431 ILE C CD1 
11931 N N   . ALA C 432 ? 0.7618 0.1877 0.6238 0.0033  0.0071  -0.0347 432 ALA C N   
11932 C CA  . ALA C 432 ? 0.7643 0.1991 0.6227 -0.0066 -0.0038 -0.0373 432 ALA C CA  
11933 C C   . ALA C 432 ? 0.7552 0.2073 0.6356 -0.0178 -0.0131 -0.0305 432 ALA C C   
11934 O O   . ALA C 432 ? 0.7487 0.2127 0.6478 -0.0165 -0.0093 -0.0226 432 ALA C O   
11935 C CB  . ALA C 432 ? 0.7470 0.2037 0.6069 -0.0027 0.0007  -0.0361 432 ALA C CB  
11936 N N   . SER C 433 ? 0.7540 0.2074 0.6318 -0.0283 -0.0250 -0.0334 433 SER C N   
11937 C CA  . SER C 433 ? 0.7454 0.2212 0.6455 -0.0385 -0.0324 -0.0266 433 SER C CA  
11938 C C   . SER C 433 ? 0.7178 0.2112 0.6191 -0.0441 -0.0395 -0.0281 433 SER C C   
11939 O O   . SER C 433 ? 0.7027 0.1840 0.5848 -0.0436 -0.0432 -0.0356 433 SER C O   
11940 C CB  . SER C 433 ? 0.7911 0.2507 0.6938 -0.0478 -0.0412 -0.0269 433 SER C CB  
11941 O OG  . SER C 433 ? 0.8417 0.2819 0.7271 -0.0541 -0.0517 -0.0356 433 SER C OG  
11942 N N   . ILE C 434 ? 0.6945 0.2153 0.6184 -0.0498 -0.0419 -0.0208 434 ILE C N   
11943 C CA  . ILE C 434 ? 0.6963 0.2344 0.6260 -0.0567 -0.0500 -0.0212 434 ILE C CA  
11944 C C   . ILE C 434 ? 0.6968 0.2425 0.6445 -0.0683 -0.0585 -0.0167 434 ILE C C   
11945 O O   . ILE C 434 ? 0.7080 0.2695 0.6742 -0.0694 -0.0544 -0.0087 434 ILE C O   
11946 C CB  . ILE C 434 ? 0.6606 0.2268 0.6012 -0.0514 -0.0432 -0.0165 434 ILE C CB  
11947 C CG1 . ILE C 434 ? 0.6694 0.2283 0.5927 -0.0405 -0.0349 -0.0209 434 ILE C CG1 
11948 C CG2 . ILE C 434 ? 0.6492 0.2359 0.6011 -0.0592 -0.0515 -0.0153 434 ILE C CG2 
11949 C CD1 . ILE C 434 ? 0.6624 0.2465 0.5974 -0.0342 -0.0268 -0.0159 434 ILE C CD1 
11950 N N   . LYS C 435 ? 0.7252 0.2592 0.6672 -0.0769 -0.0702 -0.0217 435 LYS C N   
11951 C CA  . LYS C 435 ? 0.7137 0.2570 0.6748 -0.0889 -0.0790 -0.0175 435 LYS C CA  
11952 C C   . LYS C 435 ? 0.6988 0.2681 0.6723 -0.0930 -0.0839 -0.0159 435 LYS C C   
11953 O O   . LYS C 435 ? 0.7277 0.2916 0.6894 -0.0941 -0.0914 -0.0221 435 LYS C O   
11954 C CB  . LYS C 435 ? 0.7448 0.2600 0.6946 -0.0962 -0.0899 -0.0239 435 LYS C CB  
11955 C CG  . LYS C 435 ? 0.7789 0.2672 0.7185 -0.0931 -0.0856 -0.0253 435 LYS C CG  
11956 C CD  . LYS C 435 ? 0.7946 0.2560 0.7277 -0.1021 -0.0967 -0.0302 435 LYS C CD  
11957 C CE  . LYS C 435 ? 0.8251 0.2639 0.7316 -0.1011 -0.1043 -0.0413 435 LYS C CE  
11958 N NZ  . LYS C 435 ? 0.8622 0.2690 0.7575 -0.1066 -0.1123 -0.0470 435 LYS C NZ  
11959 N N   . THR C 436 ? 0.6668 0.2632 0.6627 -0.0944 -0.0794 -0.0075 436 THR C N   
11960 C CA  . THR C 436 ? 0.6556 0.2776 0.6655 -0.0979 -0.0830 -0.0054 436 THR C CA  
11961 C C   . THR C 436 ? 0.6475 0.2753 0.6752 -0.1102 -0.0929 -0.0029 436 THR C C   
11962 O O   . THR C 436 ? 0.6412 0.2670 0.6804 -0.1153 -0.0918 0.0022  436 THR C O   
11963 C CB  . THR C 436 ? 0.6325 0.2795 0.6558 -0.0924 -0.0724 0.0017  436 THR C CB  
11964 O OG1 . THR C 436 ? 0.6182 0.2576 0.6255 -0.0816 -0.0645 -0.0011 436 THR C OG1 
11965 C CG2 . THR C 436 ? 0.6203 0.2938 0.6586 -0.0952 -0.0749 0.0040  436 THR C CG2 
11966 N N   . LYS C 437 ? 0.6520 0.2889 0.6840 -0.1148 -0.1020 -0.0054 437 LYS C N   
11967 C CA  . LYS C 437 ? 0.6557 0.3032 0.7089 -0.1262 -0.1112 -0.0023 437 LYS C CA  
11968 C C   . LYS C 437 ? 0.6191 0.2962 0.6892 -0.1265 -0.1113 0.0009  437 LYS C C   
11969 O O   . LYS C 437 ? 0.6324 0.3116 0.6928 -0.1226 -0.1147 -0.0037 437 LYS C O   
11970 C CB  . LYS C 437 ? 0.7056 0.3289 0.7456 -0.1323 -0.1251 -0.0100 437 LYS C CB  
11971 C CG  . LYS C 437 ? 0.7315 0.3620 0.7918 -0.1447 -0.1376 -0.0084 437 LYS C CG  
11972 C CD  . LYS C 437 ? 0.7809 0.3891 0.8259 -0.1498 -0.1532 -0.0170 437 LYS C CD  
11973 C CE  . LYS C 437 ? 0.7953 0.4198 0.8625 -0.1596 -0.1658 -0.0152 437 LYS C CE  
11974 N NZ  . LYS C 437 ? 0.8307 0.4332 0.8888 -0.1676 -0.1829 -0.0220 437 LYS C NZ  
11975 N N   . ILE C 438 ? 0.5849 0.2842 0.6796 -0.1305 -0.1068 0.0089  438 ILE C N   
11976 C CA  . ILE C 438 ? 0.5673 0.2945 0.6799 -0.1310 -0.1063 0.0122  438 ILE C CA  
11977 C C   . ILE C 438 ? 0.5605 0.2970 0.6964 -0.1424 -0.1155 0.0152  438 ILE C C   
11978 O O   . ILE C 438 ? 0.5528 0.2922 0.7041 -0.1488 -0.1131 0.0212  438 ILE C O   
11979 C CB  . ILE C 438 ? 0.5514 0.2990 0.6733 -0.1252 -0.0928 0.0189  438 ILE C CB  
11980 C CG1 . ILE C 438 ? 0.5507 0.2898 0.6529 -0.1146 -0.0841 0.0169  438 ILE C CG1 
11981 C CG2 . ILE C 438 ? 0.5309 0.3056 0.6689 -0.1246 -0.0920 0.0212  438 ILE C CG2 
11982 C CD1 . ILE C 438 ? 0.5331 0.2844 0.6428 -0.1109 -0.0723 0.0241  438 ILE C CD1 
11983 N N   . GLU C 439 ? 0.5644 0.3060 0.7035 -0.1449 -0.1260 0.0114  439 GLU C N   
11984 C CA  . GLU C 439 ? 0.5660 0.3221 0.7313 -0.1547 -0.1347 0.0147  439 GLU C CA  
11985 C C   . GLU C 439 ? 0.5364 0.3237 0.7233 -0.1523 -0.1262 0.0210  439 GLU C C   
11986 O O   . GLU C 439 ? 0.5576 0.3545 0.7385 -0.1450 -0.1241 0.0187  439 GLU C O   
11987 C CB  . GLU C 439 ? 0.5906 0.3372 0.7485 -0.1578 -0.1505 0.0078  439 GLU C CB  
11988 C CG  . GLU C 439 ? 0.6575 0.3733 0.7988 -0.1631 -0.1604 0.0022  439 GLU C CG  
11989 C CD  . GLU C 439 ? 0.7206 0.4210 0.8472 -0.1654 -0.1766 -0.0057 439 GLU C CD  
11990 O OE1 . GLU C 439 ? 0.7430 0.4571 0.8720 -0.1623 -0.1803 -0.0066 439 GLU C OE1 
11991 O OE2 . GLU C 439 ? 0.7373 0.4116 0.8500 -0.1703 -0.1858 -0.0108 439 GLU C OE2 
11992 N N   . THR C 440 ? 0.5258 0.3276 0.7361 -0.1579 -0.1203 0.0289  440 THR C N   
11993 C CA  . THR C 440 ? 0.5119 0.3423 0.7417 -0.1554 -0.1107 0.0350  440 THR C CA  
11994 C C   . THR C 440 ? 0.4963 0.3439 0.7476 -0.1599 -0.1197 0.0351  440 THR C C   
11995 O O   . THR C 440 ? 0.4745 0.3126 0.7290 -0.1668 -0.1333 0.0320  440 THR C O   
11996 C CB  . THR C 440 ? 0.5063 0.3462 0.7515 -0.1589 -0.0998 0.0439  440 THR C CB  
11997 O OG1 . THR C 440 ? 0.5350 0.3678 0.7947 -0.1701 -0.1074 0.0465  440 THR C OG1 
11998 C CG2 . THR C 440 ? 0.5215 0.3493 0.7474 -0.1526 -0.0895 0.0451  440 THR C CG2 
11999 N N   . SER C 441 ? 0.5005 0.3720 0.7641 -0.1549 -0.1121 0.0380  441 SER C N   
12000 C CA  . SER C 441 ? 0.5015 0.3938 0.7893 -0.1576 -0.1175 0.0395  441 SER C CA  
12001 C C   . SER C 441 ? 0.5015 0.4192 0.8120 -0.1570 -0.1042 0.0473  441 SER C C   
12002 O O   . SER C 441 ? 0.4796 0.4030 0.7809 -0.1493 -0.0919 0.0487  441 SER C O   
12003 C CB  . SER C 441 ? 0.5011 0.3945 0.7768 -0.1503 -0.1227 0.0335  441 SER C CB  
12004 O OG  . SER C 441 ? 0.5022 0.4073 0.7982 -0.1548 -0.1339 0.0334  441 SER C OG  
12005 N N   . GLU C 442 ? 0.5631 0.4956 0.9033 -0.1651 -0.1072 0.0525  442 GLU C N   
12006 C CA  . GLU C 442 ? 0.6240 0.5786 0.9875 -0.1664 -0.0943 0.0608  442 GLU C CA  
12007 C C   . GLU C 442 ? 0.5922 0.5637 0.9531 -0.1559 -0.0834 0.0606  442 GLU C C   
12008 O O   . GLU C 442 ? 0.6417 0.6217 1.0026 -0.1526 -0.0693 0.0653  442 GLU C O   
12009 C CB  . GLU C 442 ? 0.7108 0.6797 1.1088 -0.1763 -0.1014 0.0654  442 GLU C CB  
12010 C CG  . GLU C 442 ? 0.8019 0.7885 1.2249 -0.1809 -0.0885 0.0753  442 GLU C CG  
12011 C CD  . GLU C 442 ? 0.9173 0.9139 1.3747 -0.1926 -0.0964 0.0803  442 GLU C CD  
12012 O OE1 . GLU C 442 ? 0.9116 0.8921 1.3704 -0.2020 -0.1060 0.0805  442 GLU C OE1 
12013 O OE2 . GLU C 442 ? 0.9580 0.9791 1.4425 -0.1924 -0.0928 0.0842  442 GLU C OE2 
12014 N N   . ASN C 443 ? 0.5269 0.5027 0.8847 -0.1505 -0.0899 0.0551  443 ASN C N   
12015 C CA  . ASN C 443 ? 0.5018 0.4951 0.8617 -0.1416 -0.0798 0.0554  443 ASN C CA  
12016 C C   . ASN C 443 ? 0.5047 0.4876 0.8353 -0.1324 -0.0720 0.0519  443 ASN C C   
12017 O O   . ASN C 443 ? 0.5338 0.5292 0.8638 -0.1251 -0.0627 0.0522  443 ASN C O   
12018 C CB  . ASN C 443 ? 0.5179 0.5217 0.8889 -0.1391 -0.0889 0.0520  443 ASN C CB  
12019 C CG  . ASN C 443 ? 0.5049 0.5194 0.9063 -0.1480 -0.0986 0.0552  443 ASN C CG  
12020 O OD1 . ASN C 443 ? 0.4842 0.5119 0.9093 -0.1537 -0.0920 0.0621  443 ASN C OD1 
12021 N ND2 . ASN C 443 ? 0.4856 0.4948 0.8871 -0.1494 -0.1141 0.0507  443 ASN C ND2 
12022 N N   . PHE C 444 ? 0.4908 0.4509 0.7976 -0.1324 -0.0755 0.0486  444 PHE C N   
12023 C CA  . PHE C 444 ? 0.4648 0.4145 0.7451 -0.1237 -0.0707 0.0445  444 PHE C CA  
12024 C C   . PHE C 444 ? 0.4774 0.4185 0.7463 -0.1233 -0.0612 0.0482  444 PHE C C   
12025 O O   . PHE C 444 ? 0.5002 0.4293 0.7692 -0.1299 -0.0639 0.0503  444 PHE C O   
12026 C CB  . PHE C 444 ? 0.4591 0.3896 0.7210 -0.1229 -0.0827 0.0375  444 PHE C CB  
12027 C CG  . PHE C 444 ? 0.4259 0.3636 0.6933 -0.1208 -0.0915 0.0337  444 PHE C CG  
12028 C CD1 . PHE C 444 ? 0.4251 0.3665 0.7100 -0.1279 -0.1032 0.0340  444 PHE C CD1 
12029 C CD2 . PHE C 444 ? 0.4063 0.3462 0.6614 -0.1119 -0.0888 0.0301  444 PHE C CD2 
12030 C CE1 . PHE C 444 ? 0.4259 0.3736 0.7158 -0.1257 -0.1119 0.0310  444 PHE C CE1 
12031 C CE2 . PHE C 444 ? 0.4076 0.3536 0.6677 -0.1098 -0.0968 0.0272  444 PHE C CE2 
12032 C CZ  . PHE C 444 ? 0.4025 0.3525 0.6798 -0.1165 -0.1084 0.0278  444 PHE C CZ  
12033 N N   . THR C 445 ? 0.4541 0.4000 0.7124 -0.1155 -0.0509 0.0486  445 THR C N   
12034 C CA  . THR C 445 ? 0.4667 0.4062 0.7150 -0.1145 -0.0420 0.0527  445 THR C CA  
12035 C C   . THR C 445 ? 0.5074 0.4278 0.7303 -0.1089 -0.0434 0.0481  445 THR C C   
12036 O O   . THR C 445 ? 0.4734 0.3942 0.6854 -0.1018 -0.0435 0.0433  445 THR C O   
12037 C CB  . THR C 445 ? 0.4421 0.3995 0.6960 -0.1101 -0.0299 0.0569  445 THR C CB  
12038 O OG1 . THR C 445 ? 0.4411 0.4147 0.7196 -0.1157 -0.0285 0.0613  445 THR C OG1 
12039 C CG2 . THR C 445 ? 0.4310 0.3830 0.6752 -0.1093 -0.0210 0.0622  445 THR C CG2 
12040 N N   . LEU C 446 ? 0.4943 0.3984 0.7088 -0.1120 -0.0436 0.0500  446 LEU C N   
12041 C CA  . LEU C 446 ? 0.5061 0.3926 0.6985 -0.1065 -0.0433 0.0467  446 LEU C CA  
12042 C C   . LEU C 446 ? 0.5152 0.4079 0.7011 -0.1002 -0.0329 0.0502  446 LEU C C   
12043 O O   . LEU C 446 ? 0.5654 0.4671 0.7598 -0.1025 -0.0263 0.0565  446 LEU C O   
12044 C CB  . LEU C 446 ? 0.5266 0.3924 0.7134 -0.1120 -0.0478 0.0472  446 LEU C CB  
12045 C CG  . LEU C 446 ? 0.5398 0.3972 0.7316 -0.1189 -0.0595 0.0433  446 LEU C CG  
12046 C CD1 . LEU C 446 ? 0.5592 0.3957 0.7464 -0.1249 -0.0638 0.0439  446 LEU C CD1 
12047 C CD2 . LEU C 446 ? 0.5278 0.3785 0.7063 -0.1141 -0.0662 0.0354  446 LEU C CD2 
12048 N N   . LEU C 447 ? 0.5383 0.4253 0.7086 -0.0925 -0.0316 0.0463  447 LEU C N   
12049 C CA  . LEU C 447 ? 0.6475 0.5417 0.8123 -0.0862 -0.0234 0.0489  447 LEU C CA  
12050 C C   . LEU C 447 ? 0.7757 0.6536 0.9256 -0.0827 -0.0219 0.0495  447 LEU C C   
12051 O O   . LEU C 447 ? 0.9099 0.7750 1.0490 -0.0796 -0.0256 0.0446  447 LEU C O   
12052 C CB  . LEU C 447 ? 0.6505 0.5547 0.8124 -0.0796 -0.0229 0.0443  447 LEU C CB  
12053 C CG  . LEU C 447 ? 0.6467 0.5703 0.8226 -0.0801 -0.0214 0.0444  447 LEU C CG  
12054 C CD1 . LEU C 447 ? 0.6424 0.5717 0.8113 -0.0724 -0.0200 0.0401  447 LEU C CD1 
12055 C CD2 . LEU C 447 ? 0.6621 0.5984 0.8484 -0.0827 -0.0141 0.0508  447 LEU C CD2 
12056 N N   . ASP C 448 ? 0.8115 0.6911 0.9603 -0.0820 -0.0156 0.0557  448 ASP C N   
12057 C CA  . ASP C 448 ? 0.8080 0.6766 0.9441 -0.0766 -0.0131 0.0570  448 ASP C CA  
12058 C C   . ASP C 448 ? 0.6805 0.5282 0.8099 -0.0784 -0.0178 0.0548  448 ASP C C   
12059 O O   . ASP C 448 ? 0.6856 0.5267 0.8208 -0.0854 -0.0206 0.0566  448 ASP C O   
12060 C CB  . ASP C 448 ? 0.8008 0.6753 0.9294 -0.0683 -0.0114 0.0536  448 ASP C CB  
12061 C CG  . ASP C 448 ? 0.8425 0.7356 0.9752 -0.0658 -0.0071 0.0547  448 ASP C CG  
12062 O OD1 . ASP C 448 ? 0.8676 0.7680 1.0045 -0.0682 -0.0026 0.0604  448 ASP C OD1 
12063 O OD2 . ASP C 448 ? 0.7453 0.6447 0.8762 -0.0611 -0.0080 0.0499  448 ASP C OD2 
12064 N N   . ASP C 449 ? 0.6776 0.5151 0.7954 -0.0721 -0.0186 0.0505  449 ASP C N   
12065 C CA  . ASP C 449 ? 0.7369 0.5532 0.8456 -0.0716 -0.0208 0.0489  449 ASP C CA  
12066 C C   . ASP C 449 ? 0.6310 0.4377 0.7331 -0.0712 -0.0263 0.0410  449 ASP C C   
12067 O O   . ASP C 449 ? 0.5317 0.3449 0.6306 -0.0666 -0.0263 0.0369  449 ASP C O   
12068 C CB  . ASP C 449 ? 0.7533 0.5632 0.8536 -0.0641 -0.0164 0.0509  449 ASP C CB  
12069 C CG  . ASP C 449 ? 0.7924 0.6007 0.8945 -0.0648 -0.0127 0.0589  449 ASP C CG  
12070 O OD1 . ASP C 449 ? 0.8064 0.6210 0.9164 -0.0711 -0.0120 0.0637  449 ASP C OD1 
12071 O OD2 . ASP C 449 ? 0.8439 0.6446 0.9398 -0.0590 -0.0104 0.0608  449 ASP C OD2 
12072 N N   . LEU C 450 ? 0.5898 0.3793 0.6886 -0.0760 -0.0309 0.0393  450 LEU C N   
12073 C CA  . LEU C 450 ? 0.5828 0.3537 0.6684 -0.0741 -0.0350 0.0325  450 LEU C CA  
12074 C C   . LEU C 450 ? 0.5707 0.3335 0.6446 -0.0647 -0.0296 0.0310  450 LEU C C   
12075 O O   . LEU C 450 ? 0.5402 0.3005 0.6144 -0.0617 -0.0249 0.0357  450 LEU C O   
12076 C CB  . LEU C 450 ? 0.5630 0.3161 0.6478 -0.0810 -0.0396 0.0327  450 LEU C CB  
12077 C CG  . LEU C 450 ? 0.5718 0.3013 0.6413 -0.0804 -0.0446 0.0255  450 LEU C CG  
12078 C CD1 . LEU C 450 ? 0.6032 0.3359 0.6693 -0.0816 -0.0509 0.0194  450 LEU C CD1 
12079 C CD2 . LEU C 450 ? 0.5822 0.2947 0.6528 -0.0878 -0.0491 0.0265  450 LEU C CD2 
12080 N N   . LYS C 451 ? 0.5459 0.3054 0.6104 -0.0600 -0.0303 0.0251  451 LYS C N   
12081 C CA  . LYS C 451 ? 0.5785 0.3297 0.6328 -0.0512 -0.0250 0.0235  451 LYS C CA  
12082 C C   . LYS C 451 ? 0.5696 0.2981 0.6082 -0.0501 -0.0275 0.0170  451 LYS C C   
12083 O O   . LYS C 451 ? 0.5513 0.2756 0.5855 -0.0544 -0.0338 0.0126  451 LYS C O   
12084 C CB  . LYS C 451 ? 0.5831 0.3513 0.6406 -0.0456 -0.0213 0.0235  451 LYS C CB  
12085 C CG  . LYS C 451 ? 0.6144 0.4022 0.6849 -0.0466 -0.0190 0.0295  451 LYS C CG  
12086 C CD  . LYS C 451 ? 0.6620 0.4633 0.7349 -0.0401 -0.0149 0.0301  451 LYS C CD  
12087 C CE  . LYS C 451 ? 0.7112 0.5310 0.7945 -0.0413 -0.0134 0.0350  451 LYS C CE  
12088 N NZ  . LYS C 451 ? 0.7089 0.5401 0.7938 -0.0353 -0.0106 0.0347  451 LYS C NZ  
12089 N N   . ILE C 452 ? 0.5563 0.2694 0.5869 -0.0446 -0.0227 0.0170  452 ILE C N   
12090 C CA  . ILE C 452 ? 0.5625 0.2516 0.5762 -0.0419 -0.0231 0.0110  452 ILE C CA  
12091 C C   . ILE C 452 ? 0.5676 0.2552 0.5746 -0.0318 -0.0151 0.0098  452 ILE C C   
12092 O O   . ILE C 452 ? 0.5793 0.2759 0.5950 -0.0270 -0.0094 0.0147  452 ILE C O   
12093 C CB  . ILE C 452 ? 0.5600 0.2303 0.5710 -0.0441 -0.0237 0.0121  452 ILE C CB  
12094 C CG1 . ILE C 452 ? 0.5473 0.2243 0.5712 -0.0534 -0.0288 0.0168  452 ILE C CG1 
12095 C CG2 . ILE C 452 ? 0.5839 0.2276 0.5759 -0.0435 -0.0263 0.0045  452 ILE C CG2 
12096 C CD1 . ILE C 452 ? 0.5490 0.2254 0.5731 -0.0621 -0.0379 0.0131  452 ILE C CD1 
12097 N N   . SER C 453 ? 0.5668 0.2429 0.5588 -0.0285 -0.0147 0.0036  453 SER C N   
12098 C CA  . SER C 453 ? 0.5748 0.2474 0.5603 -0.0189 -0.0061 0.0027  453 SER C CA  
12099 C C   . SER C 453 ? 0.5910 0.2365 0.5558 -0.0154 -0.0042 -0.0036 453 SER C C   
12100 O O   . SER C 453 ? 0.6196 0.2529 0.5708 -0.0196 -0.0106 -0.0091 453 SER C O   
12101 C CB  . SER C 453 ? 0.5618 0.2516 0.5506 -0.0167 -0.0046 0.0025  453 SER C CB  
12102 O OG  . SER C 453 ? 0.5566 0.2374 0.5343 -0.0087 0.0026  -0.0001 453 SER C OG  
12103 N N   . TYR C 454 ? 0.5752 0.2109 0.5374 -0.0074 0.0043  -0.0028 454 TYR C N   
12104 C CA  . TYR C 454 ? 0.6017 0.2118 0.5434 -0.0021 0.0085  -0.0088 454 TYR C CA  
12105 C C   . TYR C 454 ? 0.5887 0.2032 0.5298 0.0079  0.0195  -0.0080 454 TYR C C   
12106 O O   . TYR C 454 ? 0.6044 0.2150 0.5499 0.0152  0.0278  -0.0056 454 TYR C O   
12107 C CB  . TYR C 454 ? 0.6070 0.1963 0.5445 -0.0016 0.0091  -0.0094 454 TYR C CB  
12108 C CG  . TYR C 454 ? 0.6459 0.2049 0.5589 0.0018  0.0108  -0.0173 454 TYR C CG  
12109 C CD1 . TYR C 454 ? 0.6670 0.2100 0.5642 -0.0054 0.0012  -0.0236 454 TYR C CD1 
12110 C CD2 . TYR C 454 ? 0.6637 0.2090 0.5691 0.0121  0.0217  -0.0186 454 TYR C CD2 
12111 C CE1 . TYR C 454 ? 0.6995 0.2128 0.5717 -0.0024 0.0021  -0.0314 454 TYR C CE1 
12112 C CE2 . TYR C 454 ? 0.6958 0.2117 0.5769 0.0156  0.0239  -0.0263 454 TYR C CE2 
12113 C CZ  . TYR C 454 ? 0.7143 0.2132 0.5773 0.0083  0.0139  -0.0330 454 TYR C CZ  
12114 O OH  . TYR C 454 ? 0.7325 0.2006 0.5692 0.0114  0.0150  -0.0412 454 TYR C OH  
12115 N N   . ASN C 455 ? 0.5832 0.2048 0.5187 0.0082  0.0196  -0.0100 455 ASN C N   
12116 C CA  . ASN C 455 ? 0.5819 0.2140 0.5224 0.0161  0.0293  -0.0076 455 ASN C CA  
12117 C C   . ASN C 455 ? 0.6030 0.2129 0.5230 0.0236  0.0378  -0.0125 455 ASN C C   
12118 O O   . ASN C 455 ? 0.6146 0.2139 0.5157 0.0224  0.0357  -0.0175 455 ASN C O   
12119 C CB  . ASN C 455 ? 0.5495 0.2011 0.4958 0.0133  0.0263  -0.0064 455 ASN C CB  
12120 C CG  . ASN C 455 ? 0.5522 0.2134 0.5048 0.0211  0.0366  -0.0036 455 ASN C CG  
12121 O OD1 . ASN C 455 ? 0.5379 0.1880 0.4858 0.0288  0.0462  -0.0039 455 ASN C OD1 
12122 N ND2 . ASN C 455 ? 0.5539 0.2356 0.5179 0.0191  0.0347  -0.0009 455 ASN C ND2 
12123 N N   . THR C 456 ? 0.6162 0.2207 0.5412 0.0316  0.0475  -0.0103 456 THR C N   
12124 C CA  . THR C 456 ? 0.6460 0.2273 0.5528 0.0399  0.0574  -0.0147 456 THR C CA  
12125 C C   . THR C 456 ? 0.6399 0.2267 0.5456 0.0478  0.0690  -0.0135 456 THR C C   
12126 O O   . THR C 456 ? 0.6568 0.2252 0.5470 0.0554  0.0789  -0.0169 456 THR C O   
12127 C CB  . THR C 456 ? 0.6664 0.2391 0.5814 0.0443  0.0615  -0.0126 456 THR C CB  
12128 O OG1 . THR C 456 ? 0.6208 0.2166 0.5627 0.0464  0.0638  -0.0046 456 THR C OG1 
12129 C CG2 . THR C 456 ? 0.6805 0.2407 0.5907 0.0366  0.0510  -0.0148 456 THR C CG2 
12130 N N   . HIS C 457 ? 0.6227 0.2336 0.5436 0.0462  0.0684  -0.0091 457 HIS C N   
12131 C CA  . HIS C 457 ? 0.6324 0.2469 0.5485 0.0511  0.0770  -0.0087 457 HIS C CA  
12132 C C   . HIS C 457 ? 0.6369 0.2507 0.5617 0.0617  0.0917  -0.0056 457 HIS C C   
12133 O O   . HIS C 457 ? 0.6334 0.2386 0.5457 0.0675  0.1017  -0.0071 457 HIS C O   
12134 C CB  . HIS C 457 ? 0.6664 0.2593 0.5513 0.0503  0.0759  -0.0157 457 HIS C CB  
12135 C CG  . HIS C 457 ? 0.6840 0.2818 0.5632 0.0407  0.0622  -0.0178 457 HIS C CG  
12136 N ND1 . HIS C 457 ? 0.6839 0.2895 0.5582 0.0392  0.0610  -0.0174 457 HIS C ND1 
12137 C CD2 . HIS C 457 ? 0.6854 0.2813 0.5638 0.0323  0.0494  -0.0200 457 HIS C CD2 
12138 C CE1 . HIS C 457 ? 0.6707 0.2794 0.5420 0.0307  0.0478  -0.0193 457 HIS C CE1 
12139 N NE2 . HIS C 457 ? 0.6760 0.2796 0.5505 0.0262  0.0407  -0.0208 457 HIS C NE2 
12140 N N   . LEU C 458 ? 0.6187 0.2406 0.5641 0.0641  0.0929  -0.0011 458 LEU C N   
12141 C CA  . LEU C 458 ? 0.6170 0.2424 0.5766 0.0739  0.1057  0.0031  458 LEU C CA  
12142 C C   . LEU C 458 ? 0.5921 0.2454 0.5762 0.0738  0.1070  0.0097  458 LEU C C   
12143 O O   . LEU C 458 ? 0.5789 0.2509 0.5843 0.0704  0.1002  0.0145  458 LEU C O   
12144 C CB  . LEU C 458 ? 0.6136 0.2347 0.5847 0.0770  0.1058  0.0054  458 LEU C CB  
12145 C CG  . LEU C 458 ? 0.6705 0.2634 0.6199 0.0765  0.1034  -0.0009 458 LEU C CG  
12146 C CD1 . LEU C 458 ? 0.6606 0.2496 0.6236 0.0802  0.1040  0.0025  458 LEU C CD1 
12147 C CD2 . LEU C 458 ? 0.7074 0.2747 0.6296 0.0826  0.1130  -0.0077 458 LEU C CD2 
12148 N N   . GLY C 459 ? 0.5899 0.2449 0.5702 0.0777  0.1160  0.0100  459 GLY C N   
12149 C CA  . GLY C 459 ? 0.5831 0.2626 0.5841 0.0765  0.1165  0.0154  459 GLY C CA  
12150 C C   . GLY C 459 ? 0.5645 0.2575 0.5680 0.0665  0.1024  0.0152  459 GLY C C   
12151 O O   . GLY C 459 ? 0.5767 0.2592 0.5599 0.0613  0.0960  0.0102  459 GLY C O   
12152 N N   . TRP C 460 ? 0.5405 0.2559 0.5691 0.0643  0.0976  0.0205  460 TRP C N   
12153 C CA  . TRP C 460 ? 0.5430 0.2731 0.5778 0.0557  0.0851  0.0209  460 TRP C CA  
12154 C C   . TRP C 460 ? 0.5554 0.2848 0.5927 0.0514  0.0758  0.0209  460 TRP C C   
12155 O O   . TRP C 460 ? 0.5483 0.2874 0.5877 0.0442  0.0659  0.0207  460 TRP C O   
12156 C CB  . TRP C 460 ? 0.5316 0.2854 0.5910 0.0560  0.0854  0.0265  460 TRP C CB  
12157 C CG  . TRP C 460 ? 0.5462 0.3026 0.6052 0.0589  0.0937  0.0273  460 TRP C CG  
12158 C CD1 . TRP C 460 ? 0.5285 0.2889 0.6004 0.0658  0.1049  0.0313  460 TRP C CD1 
12159 C CD2 . TRP C 460 ? 0.5325 0.2876 0.5781 0.0548  0.0913  0.0246  460 TRP C CD2 
12160 N NE1 . TRP C 460 ? 0.5569 0.3191 0.6246 0.0658  0.1100  0.0316  460 TRP C NE1 
12161 C CE2 . TRP C 460 ? 0.5416 0.2997 0.5922 0.0594  0.1018  0.0275  460 TRP C CE2 
12162 C CE3 . TRP C 460 ? 0.5096 0.2613 0.5405 0.0479  0.0816  0.0206  460 TRP C CE3 
12163 C CZ2 . TRP C 460 ? 0.5647 0.3214 0.6046 0.0573  0.1027  0.0265  460 TRP C CZ2 
12164 C CZ3 . TRP C 460 ? 0.5270 0.2775 0.5476 0.0462  0.0819  0.0194  460 TRP C CZ3 
12165 C CH2 . TRP C 460 ? 0.5574 0.3103 0.5821 0.0508  0.0922  0.0224  460 TRP C CH2 
12166 N N   . ALA C 461 ? 0.5570 0.2752 0.5945 0.0558  0.0792  0.0215  461 ALA C N   
12167 C CA  . ALA C 461 ? 0.5623 0.2775 0.6008 0.0517  0.0711  0.0219  461 ALA C CA  
12168 C C   . ALA C 461 ? 0.5893 0.2931 0.6083 0.0441  0.0632  0.0164  461 ALA C C   
12169 O O   . ALA C 461 ? 0.6490 0.3350 0.6481 0.0452  0.0662  0.0111  461 ALA C O   
12170 C CB  . ALA C 461 ? 0.5768 0.2773 0.6154 0.0585  0.0773  0.0228  461 ALA C CB  
12171 N N   . ILE C 462 ? 0.5758 0.2896 0.6006 0.0366  0.0531  0.0176  462 ILE C N   
12172 C CA  . ILE C 462 ? 0.5840 0.2905 0.5946 0.0288  0.0448  0.0131  462 ILE C CA  
12173 C C   . ILE C 462 ? 0.5926 0.2799 0.5932 0.0269  0.0420  0.0110  462 ILE C C   
12174 O O   . ILE C 462 ? 0.5814 0.2604 0.5707 0.0203  0.0348  0.0072  462 ILE C O   
12175 C CB  . ILE C 462 ? 0.5953 0.3222 0.6173 0.0216  0.0362  0.0155  462 ILE C CB  
12176 C CG1 . ILE C 462 ? 0.6008 0.3390 0.6389 0.0206  0.0335  0.0211  462 ILE C CG1 
12177 C CG2 . ILE C 462 ? 0.5865 0.3291 0.6152 0.0226  0.0378  0.0163  462 ILE C CG2 
12178 C CD1 . ILE C 462 ? 0.6024 0.3542 0.6460 0.0127  0.0249  0.0222  462 ILE C CD1 
12179 N N   . GLY C 463 ? 0.5879 0.2687 0.5944 0.0322  0.0468  0.0138  463 GLY C N   
12180 C CA  . GLY C 463 ? 0.5851 0.2467 0.5831 0.0307  0.0444  0.0121  463 GLY C CA  
12181 C C   . GLY C 463 ? 0.5735 0.2439 0.5812 0.0232  0.0356  0.0159  463 GLY C C   
12182 O O   . GLY C 463 ? 0.5559 0.2475 0.5780 0.0206  0.0326  0.0204  463 GLY C O   
12183 N N   . SER C 464 ? 0.6299 0.2829 0.6288 0.0193  0.0316  0.0138  464 SER C N   
12184 C CA  . SER C 464 ? 0.6234 0.2812 0.6309 0.0125  0.0247  0.0181  464 SER C CA  
12185 C C   . SER C 464 ? 0.6118 0.2825 0.6207 0.0031  0.0165  0.0174  464 SER C C   
12186 O O   . SER C 464 ? 0.6224 0.2889 0.6205 0.0002  0.0139  0.0118  464 SER C O   
12187 C CB  . SER C 464 ? 0.6529 0.2864 0.6510 0.0116  0.0237  0.0161  464 SER C CB  
12188 O OG  . SER C 464 ? 0.6613 0.2869 0.6639 0.0200  0.0306  0.0192  464 SER C OG  
12189 N N   . GLN C 465 ? 0.6082 0.2951 0.6308 -0.0013 0.0128  0.0233  465 GLN C N   
12190 C CA  . GLN C 465 ? 0.6120 0.3109 0.6383 -0.0103 0.0057  0.0235  465 GLN C CA  
12191 C C   . GLN C 465 ? 0.5989 0.2961 0.6315 -0.0157 0.0022  0.0285  465 GLN C C   
12192 O O   . GLN C 465 ? 0.6795 0.3716 0.7158 -0.0118 0.0053  0.0329  465 GLN C O   
12193 C CB  . GLN C 465 ? 0.6053 0.3293 0.6432 -0.0102 0.0056  0.0266  465 GLN C CB  
12194 C CG  . GLN C 465 ? 0.6625 0.3915 0.6970 -0.0057 0.0087  0.0228  465 GLN C CG  
12195 C CD  . GLN C 465 ? 0.6705 0.4226 0.7154 -0.0071 0.0072  0.0249  465 GLN C CD  
12196 O OE1 . GLN C 465 ? 0.6557 0.4159 0.7016 -0.0131 0.0021  0.0236  465 GLN C OE1 
12197 N NE2 . GLN C 465 ? 0.7077 0.4704 0.7610 -0.0012 0.0115  0.0278  465 GLN C NE2 
12198 N N   . ALA C 466 ? 0.5688 0.2705 0.6035 -0.0246 -0.0040 0.0285  466 ALA C N   
12199 C CA  . ALA C 466 ? 0.5661 0.2706 0.6093 -0.0300 -0.0062 0.0347  466 ALA C CA  
12200 C C   . ALA C 466 ? 0.5379 0.2615 0.5897 -0.0373 -0.0103 0.0364  466 ALA C C   
12201 O O   . ALA C 466 ? 0.5785 0.3065 0.6279 -0.0399 -0.0134 0.0315  466 ALA C O   
12202 C CB  . ALA C 466 ? 0.5604 0.2413 0.5965 -0.0334 -0.0086 0.0332  466 ALA C CB  
12203 N N   . SER C 467 ? 0.5314 0.2662 0.5928 -0.0400 -0.0099 0.0434  467 SER C N   
12204 C CA  . SER C 467 ? 0.5277 0.2782 0.5975 -0.0473 -0.0128 0.0456  467 SER C CA  
12205 C C   . SER C 467 ? 0.5473 0.2894 0.6206 -0.0546 -0.0149 0.0499  467 SER C C   
12206 O O   . SER C 467 ? 0.5678 0.3046 0.6420 -0.0530 -0.0123 0.0557  467 SER C O   
12207 C CB  . SER C 467 ? 0.5221 0.2933 0.5993 -0.0450 -0.0099 0.0504  467 SER C CB  
12208 O OG  . SER C 467 ? 0.5973 0.3780 0.6732 -0.0398 -0.0089 0.0462  467 SER C OG  
12209 N N   . VAL C 468 ? 0.5725 0.3147 0.6490 -0.0626 -0.0197 0.0476  468 VAL C N   
12210 C CA  . VAL C 468 ? 0.5863 0.3195 0.6674 -0.0707 -0.0225 0.0510  468 VAL C CA  
12211 C C   . VAL C 468 ? 0.5557 0.3086 0.6501 -0.0775 -0.0228 0.0555  468 VAL C C   
12212 O O   . VAL C 468 ? 0.5522 0.3156 0.6506 -0.0801 -0.0259 0.0516  468 VAL C O   
12213 C CB  . VAL C 468 ? 0.6210 0.3344 0.6951 -0.0750 -0.0288 0.0442  468 VAL C CB  
12214 C CG1 . VAL C 468 ? 0.6337 0.3352 0.7132 -0.0836 -0.0320 0.0479  468 VAL C CG1 
12215 C CG2 . VAL C 468 ? 0.6304 0.3247 0.6894 -0.0673 -0.0275 0.0383  468 VAL C CG2 
12216 N N   . SER C 469 ? 0.5850 0.3419 0.6858 -0.0801 -0.0194 0.0639  469 SER C N   
12217 C CA  . SER C 469 ? 0.5759 0.3486 0.6894 -0.0872 -0.0186 0.0691  469 SER C CA  
12218 C C   . SER C 469 ? 0.6043 0.3687 0.7248 -0.0969 -0.0243 0.0678  469 SER C C   
12219 O O   . SER C 469 ? 0.5893 0.3338 0.7061 -0.0996 -0.0269 0.0679  469 SER C O   
12220 C CB  . SER C 469 ? 0.5827 0.3595 0.6988 -0.0872 -0.0130 0.0787  469 SER C CB  
12221 O OG  . SER C 469 ? 0.5818 0.3752 0.7096 -0.0934 -0.0107 0.0836  469 SER C OG  
12222 N N   . ILE C 470 ? 0.6316 0.4117 0.7630 -0.1019 -0.0267 0.0664  470 ILE C N   
12223 C CA  . ILE C 470 ? 0.6884 0.4655 0.8305 -0.1118 -0.0329 0.0656  470 ILE C CA  
12224 C C   . ILE C 470 ? 0.7034 0.4992 0.8633 -0.1182 -0.0290 0.0734  470 ILE C C   
12225 O O   . ILE C 470 ? 0.6894 0.4889 0.8629 -0.1266 -0.0335 0.0738  470 ILE C O   
12226 C CB  . ILE C 470 ? 0.6856 0.4631 0.8254 -0.1117 -0.0404 0.0565  470 ILE C CB  
12227 C CG1 . ILE C 470 ? 0.6562 0.4560 0.8000 -0.1072 -0.0377 0.0550  470 ILE C CG1 
12228 C CG2 . ILE C 470 ? 0.6895 0.4451 0.8108 -0.1065 -0.0438 0.0491  470 ILE C CG2 
12229 C CD1 . ILE C 470 ? 0.6425 0.4599 0.8048 -0.1142 -0.0400 0.0568  470 ILE C CD1 
12230 N N   . SER C 471 ? 0.7581 0.5654 0.9177 -0.1142 -0.0205 0.0800  471 SER C N   
12231 C CA  . SER C 471 ? 0.7992 0.6237 0.9725 -0.1188 -0.0145 0.0879  471 SER C CA  
12232 C C   . SER C 471 ? 0.8501 0.6664 1.0346 -0.1287 -0.0152 0.0946  471 SER C C   
12233 O O   . SER C 471 ? 0.9535 0.7834 1.1546 -0.1355 -0.0131 0.0991  471 SER C O   
12234 C CB  . SER C 471 ? 0.7951 0.6273 0.9601 -0.1117 -0.0061 0.0932  471 SER C CB  
12235 O OG  . SER C 471 ? 0.8490 0.6648 1.0058 -0.1110 -0.0044 0.0985  471 SER C OG  
12236 N N   . ASP C 472 ? 0.8179 0.6118 0.9944 -0.1298 -0.0180 0.0951  472 ASP C N   
12237 C CA  . ASP C 472 ? 0.8446 0.6274 1.0312 -0.1396 -0.0199 0.1007  472 ASP C CA  
12238 C C   . ASP C 472 ? 0.8266 0.6055 1.0246 -0.1482 -0.0296 0.0952  472 ASP C C   
12239 O O   . ASP C 472 ? 0.7867 0.5549 0.9939 -0.1571 -0.0328 0.0988  472 ASP C O   
12240 C CB  . ASP C 472 ? 0.8872 0.6455 1.0611 -0.1375 -0.0204 0.1025  472 ASP C CB  
12241 C CG  . ASP C 472 ? 0.9045 0.6423 1.0633 -0.1324 -0.0270 0.0928  472 ASP C CG  
12242 O OD1 . ASP C 472 ? 0.9015 0.6446 1.0541 -0.1273 -0.0298 0.0845  472 ASP C OD1 
12243 O OD2 . ASP C 472 ? 0.8932 0.6090 1.0459 -0.1334 -0.0290 0.0936  472 ASP C OD2 
12244 N N   . GLN C 473 ? 0.8013 0.5878 0.9989 -0.1460 -0.0351 0.0867  473 GLN C N   
12245 C CA  . GLN C 473 ? 0.7754 0.5551 0.9802 -0.1533 -0.0461 0.0807  473 GLN C CA  
12246 C C   . GLN C 473 ? 0.8096 0.6119 1.0293 -0.1552 -0.0486 0.0785  473 GLN C C   
12247 O O   . GLN C 473 ? 0.8604 0.6589 1.0861 -0.1606 -0.0589 0.0732  473 GLN C O   
12248 C CB  . GLN C 473 ? 0.7414 0.4998 0.9258 -0.1480 -0.0532 0.0707  473 GLN C CB  
12249 C CG  . GLN C 473 ? 0.7560 0.4883 0.9265 -0.1465 -0.0528 0.0711  473 GLN C CG  
12250 C CD  . GLN C 473 ? 0.7353 0.4449 0.8876 -0.1431 -0.0606 0.0607  473 GLN C CD  
12251 O OE1 . GLN C 473 ? 0.7683 0.4670 0.9220 -0.1498 -0.0706 0.0553  473 GLN C OE1 
12252 N NE2 . GLN C 473 ? 0.6787 0.3804 0.8133 -0.1327 -0.0560 0.0576  473 GLN C NE2 
12253 N N   . LEU C 474 ? 0.8379 0.6627 1.0632 -0.1508 -0.0398 0.0823  474 LEU C N   
12254 C CA  . LEU C 474 ? 0.8634 0.7079 1.0977 -0.1490 -0.0415 0.0785  474 LEU C CA  
12255 C C   . LEU C 474 ? 0.8661 0.7195 1.1245 -0.1594 -0.0481 0.0798  474 LEU C C   
12256 O O   . LEU C 474 ? 0.8331 0.6913 1.0957 -0.1597 -0.0563 0.0736  474 LEU C O   
12257 C CB  . LEU C 474 ? 0.8510 0.7160 1.0857 -0.1421 -0.0303 0.0822  474 LEU C CB  
12258 C CG  . LEU C 474 ? 0.8699 0.7329 1.0840 -0.1307 -0.0277 0.0770  474 LEU C CG  
12259 C CD1 . LEU C 474 ? 0.8348 0.7168 1.0491 -0.1246 -0.0173 0.0808  474 LEU C CD1 
12260 C CD2 . LEU C 474 ? 0.8386 0.6996 1.0472 -0.1276 -0.0362 0.0675  474 LEU C CD2 
12261 N N   . ASP C 475 ? 0.8850 0.7397 1.1595 -0.1680 -0.0452 0.0882  475 ASP C N   
12262 C CA  . ASP C 475 ? 0.9204 0.7843 1.2214 -0.1788 -0.0507 0.0910  475 ASP C CA  
12263 C C   . ASP C 475 ? 0.9046 0.7509 1.2049 -0.1850 -0.0667 0.0837  475 ASP C C   
12264 O O   . ASP C 475 ? 0.8496 0.7054 1.1707 -0.1924 -0.0744 0.0834  475 ASP C O   
12265 C CB  . ASP C 475 ? 0.9460 0.8131 1.2631 -0.1867 -0.0431 0.1023  475 ASP C CB  
12266 C CG  . ASP C 475 ? 1.0078 0.8500 1.3110 -0.1886 -0.0428 0.1050  475 ASP C CG  
12267 O OD1 . ASP C 475 ? 1.0008 0.8320 1.2802 -0.1796 -0.0391 0.1025  475 ASP C OD1 
12268 O OD2 . ASP C 475 ? 0.9907 0.8244 1.3077 -0.1991 -0.0464 0.1097  475 ASP C OD2 
12269 N N   . LYS C 476 ? 0.8444 0.6647 1.1212 -0.1822 -0.0718 0.0778  476 LYS C N   
12270 C CA  . LYS C 476 ? 0.8055 0.6050 1.0787 -0.1887 -0.0863 0.0712  476 LYS C CA  
12271 C C   . LYS C 476 ? 0.7572 0.5602 1.0260 -0.1859 -0.0964 0.0622  476 LYS C C   
12272 O O   . LYS C 476 ? 0.8218 0.6386 1.0849 -0.1772 -0.0913 0.0602  476 LYS C O   
12273 C CB  . LYS C 476 ? 0.8314 0.6011 1.0795 -0.1855 -0.0874 0.0675  476 LYS C CB  
12274 C CG  . LYS C 476 ? 0.8701 0.6333 1.1189 -0.1868 -0.0778 0.0763  476 LYS C CG  
12275 C CD  . LYS C 476 ? 0.9456 0.6771 1.1765 -0.1872 -0.0821 0.0729  476 LYS C CD  
12276 C CE  . LYS C 476 ? 0.9436 0.6625 1.1468 -0.1751 -0.0803 0.0655  476 LYS C CE  
12277 N NZ  . LYS C 476 ? 0.9847 0.6722 1.1709 -0.1759 -0.0882 0.0585  476 LYS C NZ  
12278 N N   . LYS C 477 ? 0.7314 0.5207 1.0023 -0.1933 -0.1110 0.0569  477 LYS C N   
12279 C CA  . LYS C 477 ? 0.7455 0.5365 1.0135 -0.1924 -0.1229 0.0490  477 LYS C CA  
12280 C C   . LYS C 477 ? 0.7188 0.4881 0.9528 -0.1834 -0.1254 0.0396  477 LYS C C   
12281 O O   . LYS C 477 ? 0.7110 0.4853 0.9354 -0.1770 -0.1283 0.0341  477 LYS C O   
12282 C CB  . LYS C 477 ? 0.8223 0.6099 1.1085 -0.2047 -0.1384 0.0479  477 LYS C CB  
12283 C CG  . LYS C 477 ? 0.9148 0.7309 1.2390 -0.2125 -0.1381 0.0559  477 LYS C CG  
12284 C CD  . LYS C 477 ? 0.9843 0.8266 1.3195 -0.2069 -0.1367 0.0555  477 LYS C CD  
12285 C CE  . LYS C 477 ? 0.9712 0.8340 1.3073 -0.1977 -0.1189 0.0606  477 LYS C CE  
12286 N NZ  . LYS C 477 ? 0.9243 0.7991 1.2522 -0.1879 -0.1178 0.0560  477 LYS C NZ  
12287 N N   . ILE C 478 ? 0.6770 0.4222 0.8936 -0.1826 -0.1234 0.0384  478 ILE C N   
12288 C CA  . ILE C 478 ? 0.6883 0.4110 0.8733 -0.1740 -0.1241 0.0302  478 ILE C CA  
12289 C C   . ILE C 478 ? 0.6709 0.3884 0.8457 -0.1672 -0.1105 0.0343  478 ILE C C   
12290 O O   . ILE C 478 ? 0.6899 0.4001 0.8716 -0.1723 -0.1077 0.0398  478 ILE C O   
12291 C CB  . ILE C 478 ? 0.7354 0.4290 0.9077 -0.1801 -0.1381 0.0228  478 ILE C CB  
12292 C CG1 . ILE C 478 ? 0.7410 0.4387 0.9192 -0.1853 -0.1530 0.0177  478 ILE C CG1 
12293 C CG2 . ILE C 478 ? 0.7417 0.4087 0.8811 -0.1712 -0.1357 0.0156  478 ILE C CG2 
12294 C CD1 . ILE C 478 ? 0.7745 0.4453 0.9442 -0.1936 -0.1685 0.0112  478 ILE C CD1 
12295 N N   . ILE C 479 ? 0.6669 0.3884 0.8262 -0.1559 -0.1026 0.0322  479 ILE C N   
12296 C CA  . ILE C 479 ? 0.6706 0.3869 0.8188 -0.1483 -0.0908 0.0355  479 ILE C CA  
12297 C C   . ILE C 479 ? 0.6825 0.3725 0.8034 -0.1414 -0.0926 0.0273  479 ILE C C   
12298 O O   . ILE C 479 ? 0.6866 0.3731 0.7945 -0.1373 -0.0973 0.0200  479 ILE C O   
12299 C CB  . ILE C 479 ? 0.6411 0.3821 0.7933 -0.1404 -0.0805 0.0391  479 ILE C CB  
12300 C CG1 . ILE C 479 ? 0.6384 0.4054 0.8166 -0.1462 -0.0772 0.0470  479 ILE C CG1 
12301 C CG2 . ILE C 479 ? 0.6418 0.3769 0.7811 -0.1317 -0.0700 0.0417  479 ILE C CG2 
12302 C CD1 . ILE C 479 ? 0.5916 0.3828 0.7736 -0.1391 -0.0694 0.0487  479 ILE C CD1 
12303 N N   . THR C 480 ? 0.6545 0.3254 0.7663 -0.1399 -0.0886 0.0288  480 THR C N   
12304 C CA  . THR C 480 ? 0.6606 0.3065 0.7470 -0.1327 -0.0891 0.0211  480 THR C CA  
12305 C C   . THR C 480 ? 0.6452 0.2906 0.7242 -0.1228 -0.0769 0.0248  480 THR C C   
12306 O O   . THR C 480 ? 0.6382 0.2991 0.7304 -0.1229 -0.0698 0.0333  480 THR C O   
12307 C CB  . THR C 480 ? 0.6884 0.3060 0.7678 -0.1396 -0.0982 0.0168  480 THR C CB  
12308 O OG1 . THR C 480 ? 0.6866 0.3009 0.7766 -0.1432 -0.0932 0.0247  480 THR C OG1 
12309 C CG2 . THR C 480 ? 0.6914 0.3109 0.7812 -0.1504 -0.1115 0.0140  480 THR C CG2 
12310 N N   . SER C 481 ? 0.6645 0.2927 0.7224 -0.1141 -0.0747 0.0185  481 SER C N   
12311 C CA  . SER C 481 ? 0.6623 0.2876 0.7129 -0.1042 -0.0642 0.0212  481 SER C CA  
12312 C C   . SER C 481 ? 0.6876 0.2854 0.7153 -0.0974 -0.0641 0.0133  481 SER C C   
12313 O O   . SER C 481 ? 0.7289 0.3171 0.7432 -0.0970 -0.0698 0.0051  481 SER C O   
12314 C CB  . SER C 481 ? 0.6340 0.2835 0.6884 -0.0970 -0.0572 0.0237  481 SER C CB  
12315 O OG  . SER C 481 ? 0.6401 0.2877 0.6910 -0.0887 -0.0481 0.0277  481 SER C OG  
12316 N N   . GLU C 482 ? 0.6835 0.2685 0.7060 -0.0914 -0.0573 0.0157  482 GLU C N   
12317 C CA  . GLU C 482 ? 0.6852 0.2439 0.6867 -0.0840 -0.0555 0.0085  482 GLU C CA  
12318 C C   . GLU C 482 ? 0.6769 0.2396 0.6770 -0.0725 -0.0441 0.0123  482 GLU C C   
12319 O O   . GLU C 482 ? 0.6599 0.2245 0.6695 -0.0720 -0.0400 0.0198  482 GLU C O   
12320 C CB  . GLU C 482 ? 0.6801 0.2107 0.6762 -0.0898 -0.0610 0.0062  482 GLU C CB  
12321 C CG  . GLU C 482 ? 0.6987 0.1992 0.6708 -0.0827 -0.0600 -0.0028 482 GLU C CG  
12322 C CD  . GLU C 482 ? 0.7250 0.1956 0.6905 -0.0889 -0.0666 -0.0062 482 GLU C CD  
12323 O OE1 . GLU C 482 ? 0.7342 0.2058 0.7139 -0.0928 -0.0652 0.0016  482 GLU C OE1 
12324 O OE2 . GLU C 482 ? 0.7343 0.1804 0.6810 -0.0898 -0.0729 -0.0158 482 GLU C OE2 
12325 N N   . ASN C 483 ? 0.6783 0.2417 0.6666 -0.0635 -0.0396 0.0074  483 ASN C N   
12326 C CA  . ASN C 483 ? 0.6815 0.2513 0.6706 -0.0526 -0.0293 0.0109  483 ASN C CA  
12327 C C   . ASN C 483 ? 0.6810 0.2278 0.6511 -0.0434 -0.0246 0.0038  483 ASN C C   
12328 O O   . ASN C 483 ? 0.6868 0.2234 0.6416 -0.0431 -0.0275 -0.0042 483 ASN C O   
12329 C CB  . ASN C 483 ? 0.6887 0.2867 0.6861 -0.0499 -0.0265 0.0133  483 ASN C CB  
12330 C CG  . ASN C 483 ? 0.7104 0.3303 0.7258 -0.0578 -0.0295 0.0204  483 ASN C CG  
12331 O OD1 . ASN C 483 ? 0.7653 0.3981 0.7914 -0.0553 -0.0246 0.0279  483 ASN C OD1 
12332 N ND2 . ASN C 483 ? 0.7225 0.3460 0.7416 -0.0671 -0.0374 0.0184  483 ASN C ND2 
12333 N N   . PHE C 484 ? 0.6759 0.2153 0.6470 -0.0354 -0.0170 0.0072  484 PHE C N   
12334 C CA  . PHE C 484 ? 0.6831 0.1994 0.6376 -0.0260 -0.0111 0.0011  484 PHE C CA  
12335 C C   . PHE C 484 ? 0.6614 0.1915 0.6182 -0.0148 -0.0013 0.0028  484 PHE C C   
12336 O O   . PHE C 484 ? 0.6546 0.2083 0.6275 -0.0134 0.0014  0.0101  484 PHE C O   
12337 C CB  . PHE C 484 ? 0.6816 0.1756 0.6355 -0.0253 -0.0103 0.0030  484 PHE C CB  
12338 C CG  . PHE C 484 ? 0.6987 0.1761 0.6493 -0.0366 -0.0203 0.0005  484 PHE C CG  
12339 C CD1 . PHE C 484 ? 0.7338 0.1838 0.6642 -0.0381 -0.0248 -0.0096 484 PHE C CD1 
12340 C CD2 . PHE C 484 ? 0.6896 0.1775 0.6570 -0.0458 -0.0250 0.0083  484 PHE C CD2 
12341 C CE1 . PHE C 484 ? 0.7493 0.1837 0.6779 -0.0491 -0.0351 -0.0120 484 PHE C CE1 
12342 C CE2 . PHE C 484 ? 0.7056 0.1783 0.6724 -0.0566 -0.0341 0.0066  484 PHE C CE2 
12343 C CZ  . PHE C 484 ? 0.7370 0.1833 0.6851 -0.0585 -0.0396 -0.0037 484 PHE C CZ  
12344 N N   . PHE C 485 ? 0.6646 0.1798 0.6047 -0.0071 0.0041  -0.0043 485 PHE C N   
12345 C CA  . PHE C 485 ? 0.6401 0.1663 0.5827 0.0036  0.0141  -0.0030 485 PHE C CA  
12346 C C   . PHE C 485 ? 0.6548 0.1556 0.5814 0.0135  0.0224  -0.0086 485 PHE C C   
12347 O O   . PHE C 485 ? 0.6809 0.1573 0.5868 0.0123  0.0200  -0.0169 485 PHE C O   
12348 C CB  . PHE C 485 ? 0.6285 0.1711 0.5681 0.0024  0.0131  -0.0056 485 PHE C CB  
12349 C CG  . PHE C 485 ? 0.6195 0.1855 0.5730 -0.0073 0.0049  -0.0014 485 PHE C CG  
12350 C CD1 . PHE C 485 ? 0.6038 0.1956 0.5768 -0.0065 0.0071  0.0066  485 PHE C CD1 
12351 C CD2 . PHE C 485 ? 0.6196 0.1815 0.5665 -0.0171 -0.0050 -0.0055 485 PHE C CD2 
12352 C CE1 . PHE C 485 ? 0.5805 0.1930 0.5649 -0.0145 0.0008  0.0100  485 PHE C CE1 
12353 C CE2 . PHE C 485 ? 0.5944 0.1782 0.5555 -0.0252 -0.0113 -0.0015 485 PHE C CE2 
12354 C CZ  . PHE C 485 ? 0.5910 0.1996 0.5702 -0.0236 -0.0078 0.0062  485 PHE C CZ  
12355 N N   . ASN C 486 ? 0.6427 0.1493 0.5789 0.0236  0.0321  -0.0042 486 ASN C N   
12356 C CA  . ASN C 486 ? 0.6720 0.1579 0.5949 0.0345  0.0421  -0.0091 486 ASN C CA  
12357 C C   . ASN C 486 ? 0.6808 0.1692 0.5902 0.0377  0.0465  -0.0147 486 ASN C C   
12358 O O   . ASN C 486 ? 0.6481 0.1604 0.5662 0.0353  0.0452  -0.0119 486 ASN C O   
12359 C CB  . ASN C 486 ? 0.6617 0.1528 0.6010 0.0444  0.0510  -0.0023 486 ASN C CB  
12360 C CG  . ASN C 486 ? 0.6616 0.1414 0.6077 0.0421  0.0470  0.0018  486 ASN C CG  
12361 O OD1 . ASN C 486 ? 0.6410 0.1382 0.6067 0.0409  0.0451  0.0107  486 ASN C OD1 
12362 N ND2 . ASN C 486 ? 0.6870 0.1368 0.6161 0.0411  0.0454  -0.0047 486 ASN C ND2 
12363 N N   . ILE C 487 ? 0.7233 0.1848 0.6098 0.0433  0.0518  -0.0228 487 ILE C N   
12364 C CA  . ILE C 487 ? 0.7432 0.2022 0.6135 0.0481  0.0580  -0.0281 487 ILE C CA  
12365 C C   . ILE C 487 ? 0.7505 0.2091 0.6254 0.0617  0.0735  -0.0261 487 ILE C C   
12366 O O   . ILE C 487 ? 0.7708 0.2066 0.6368 0.0689  0.0802  -0.0292 487 ILE C O   
12367 C CB  . ILE C 487 ? 0.7722 0.2020 0.6114 0.0447  0.0530  -0.0386 487 ILE C CB  
12368 C CG1 . ILE C 487 ? 0.7647 0.1942 0.6029 0.0309  0.0368  -0.0400 487 ILE C CG1 
12369 C CG2 . ILE C 487 ? 0.7925 0.2229 0.6150 0.0488  0.0586  -0.0427 487 ILE C CG2 
12370 C CD1 . ILE C 487 ? 0.7935 0.1939 0.6020 0.0267  0.0297  -0.0504 487 ILE C CD1 
12371 N N   . PRO C 488 ? 0.7410 0.2243 0.6305 0.0659  0.0801  -0.0209 488 PRO C N   
12372 C CA  . PRO C 488 ? 0.7450 0.2278 0.6390 0.0787  0.0953  -0.0193 488 PRO C CA  
12373 C C   . PRO C 488 ? 0.7885 0.2427 0.6520 0.0847  0.1034  -0.0284 488 PRO C C   
12374 O O   . PRO C 488 ? 0.8058 0.2525 0.6481 0.0797  0.0987  -0.0343 488 PRO C O   
12375 C CB  . PRO C 488 ? 0.6997 0.2147 0.6131 0.0788  0.0976  -0.0128 488 PRO C CB  
12376 C CG  . PRO C 488 ? 0.6705 0.2040 0.5943 0.0669  0.0836  -0.0097 488 PRO C CG  
12377 C CD  . PRO C 488 ? 0.6977 0.2093 0.5998 0.0589  0.0736  -0.0167 488 PRO C CD  
12378 N N   . ASP C 489 ? 0.8110 0.2494 0.6725 0.0960  0.1157  -0.0294 489 ASP C N   
12379 C CA  . ASP C 489 ? 0.8404 0.2519 0.6737 0.1041  0.1266  -0.0375 489 ASP C CA  
12380 C C   . ASP C 489 ? 0.8200 0.2424 0.6464 0.1068  0.1343  -0.0376 489 ASP C C   
12381 O O   . ASP C 489 ? 0.8419 0.2429 0.6381 0.1089  0.1381  -0.0452 489 ASP C O   
12382 C CB  . ASP C 489 ? 0.8574 0.2550 0.6959 0.1168  0.1401  -0.0369 489 ASP C CB  
12383 C CG  . ASP C 489 ? 0.8939 0.2696 0.7290 0.1157  0.1343  -0.0395 489 ASP C CG  
12384 O OD1 . ASP C 489 ? 0.9065 0.2657 0.7232 0.1063  0.1221  -0.0455 489 ASP C OD1 
12385 O OD2 . ASP C 489 ? 0.9273 0.3027 0.7795 0.1240  0.1417  -0.0351 489 ASP C OD2 
12386 N N   . ASN C 490 ? 0.7886 0.2428 0.6418 0.1069  0.1364  -0.0292 490 ASN C N   
12387 C CA  . ASN C 490 ? 0.7897 0.2557 0.6385 0.1081  0.1425  -0.0284 490 ASN C CA  
12388 C C   . ASN C 490 ? 0.7824 0.2653 0.6320 0.0960  0.1282  -0.0276 490 ASN C C   
12389 O O   . ASN C 490 ? 0.7521 0.2562 0.6121 0.0953  0.1305  -0.0233 490 ASN C O   
12390 C CB  . ASN C 490 ? 0.7817 0.2688 0.6579 0.1172  0.1559  -0.0204 490 ASN C CB  
12391 C CG  . ASN C 490 ? 0.7511 0.2690 0.6624 0.1126  0.1481  -0.0114 490 ASN C CG  
12392 O OD1 . ASN C 490 ? 0.7555 0.2744 0.6742 0.1066  0.1368  -0.0103 490 ASN C OD1 
12393 N ND2 . ASN C 490 ? 0.7262 0.2689 0.6587 0.1149  0.1537  -0.0049 490 ASN C ND2 
12394 N N   . CYS C 491 ? 0.7983 0.2714 0.6372 0.0863  0.1136  -0.0317 491 CYS C N   
12395 C CA  . CYS C 491 ? 0.7740 0.2570 0.6075 0.0755  0.1005  -0.0328 491 CYS C CA  
12396 C C   . CYS C 491 ? 0.8031 0.2604 0.6002 0.0751  0.0998  -0.0417 491 CYS C C   
12397 O O   . CYS C 491 ? 0.8291 0.2577 0.6044 0.0762  0.0988  -0.0487 491 CYS C O   
12398 C CB  . CYS C 491 ? 0.7758 0.2639 0.6191 0.0648  0.0850  -0.0319 491 CYS C CB  
12399 S SG  . CYS C 491 ? 0.7324 0.2329 0.5711 0.0519  0.0693  -0.0332 491 CYS C SG  
12400 N N   . TRP C 492 ? 0.7902 0.2573 0.5810 0.0743  0.1012  -0.0410 492 TRP C N   
12401 C CA  . TRP C 492 ? 0.8091 0.2544 0.5650 0.0750  0.1017  -0.0481 492 TRP C CA  
12402 C C   . TRP C 492 ? 0.7788 0.2274 0.5270 0.0631  0.0840  -0.0505 492 TRP C C   
12403 O O   . TRP C 492 ? 0.7889 0.2142 0.5077 0.0602  0.0772  -0.0579 492 TRP C O   
12404 C CB  . TRP C 492 ? 0.8210 0.2735 0.5742 0.0828  0.1163  -0.0450 492 TRP C CB  
12405 C CG  . TRP C 492 ? 0.8144 0.2724 0.5850 0.0939  0.1335  -0.0404 492 TRP C CG  
12406 C CD1 . TRP C 492 ? 0.7978 0.2827 0.5964 0.0972  0.1416  -0.0320 492 TRP C CD1 
12407 C CD2 . TRP C 492 ? 0.8396 0.2762 0.6028 0.1029  0.1441  -0.0436 492 TRP C CD2 
12408 N NE1 . TRP C 492 ? 0.8110 0.2943 0.6217 0.1075  0.1562  -0.0294 492 TRP C NE1 
12409 C CE2 . TRP C 492 ? 0.8280 0.2820 0.6176 0.1116  0.1586  -0.0362 492 TRP C CE2 
12410 C CE3 . TRP C 492 ? 0.8780 0.2824 0.6159 0.1046  0.1426  -0.0519 492 TRP C CE3 
12411 C CZ2 . TRP C 492 ? 0.8482 0.2894 0.6406 0.1223  0.1717  -0.0367 492 TRP C CZ2 
12412 C CZ3 . TRP C 492 ? 0.8785 0.2689 0.6175 0.1152  0.1559  -0.0528 492 TRP C CZ3 
12413 C CH2 . TRP C 492 ? 0.8710 0.2802 0.6378 0.1240  0.1703  -0.0451 492 TRP C CH2 
12414 N N   . VAL C 493 ? 0.7403 0.2179 0.5160 0.0565  0.0764  -0.0441 493 VAL C N   
12415 C CA  . VAL C 493 ? 0.7381 0.2225 0.5127 0.0454  0.0601  -0.0453 493 VAL C CA  
12416 C C   . VAL C 493 ? 0.7075 0.2178 0.5148 0.0391  0.0528  -0.0390 493 VAL C C   
12417 O O   . VAL C 493 ? 0.6972 0.2265 0.5283 0.0432  0.0605  -0.0325 493 VAL C O   
12418 C CB  . VAL C 493 ? 0.7377 0.2311 0.5042 0.0450  0.0602  -0.0443 493 VAL C CB  
12419 C CG1 . VAL C 493 ? 0.7100 0.2303 0.5019 0.0494  0.0702  -0.0363 493 VAL C CG1 
12420 C CG2 . VAL C 493 ? 0.7390 0.2395 0.5047 0.0342  0.0432  -0.0455 493 VAL C CG2 
12421 N N   . VAL C 494 ? 0.6959 0.2067 0.5039 0.0289  0.0378  -0.0408 494 VAL C N   
12422 C CA  . VAL C 494 ? 0.6632 0.1970 0.4994 0.0222  0.0306  -0.0351 494 VAL C CA  
12423 C C   . VAL C 494 ? 0.6518 0.1979 0.4900 0.0130  0.0177  -0.0353 494 VAL C C   
12424 O O   . VAL C 494 ? 0.6617 0.1919 0.4789 0.0092  0.0099  -0.0410 494 VAL C O   
12425 C CB  . VAL C 494 ? 0.6676 0.1893 0.5075 0.0193  0.0266  -0.0360 494 VAL C CB  
12426 C CG1 . VAL C 494 ? 0.6976 0.1943 0.5149 0.0131  0.0158  -0.0436 494 VAL C CG1 
12427 C CG2 . VAL C 494 ? 0.6424 0.1880 0.5108 0.0130  0.0207  -0.0292 494 VAL C CG2 
12428 N N   . ASN C 495 ? 0.6333 0.2077 0.4967 0.0097  0.0156  -0.0290 495 ASN C N   
12429 C CA  . ASN C 495 ? 0.6310 0.2189 0.5021 0.0005  0.0031  -0.0283 495 ASN C CA  
12430 C C   . ASN C 495 ? 0.6283 0.2245 0.5182 -0.0059 -0.0029 -0.0252 495 ASN C C   
12431 O O   . ASN C 495 ? 0.6216 0.2356 0.5324 -0.0044 0.0016  -0.0192 495 ASN C O   
12432 C CB  . ASN C 495 ? 0.6091 0.2218 0.4940 0.0010  0.0047  -0.0239 495 ASN C CB  
12433 C CG  . ASN C 495 ? 0.6017 0.2265 0.4926 -0.0076 -0.0078 -0.0239 495 ASN C CG  
12434 O OD1 . ASN C 495 ? 0.5934 0.2212 0.4935 -0.0148 -0.0164 -0.0236 495 ASN C OD1 
12435 N ND2 . ASN C 495 ? 0.6125 0.2455 0.5003 -0.0068 -0.0085 -0.0236 495 ASN C ND2 
12436 N N   . ALA C 496 ? 0.6407 0.2234 0.5228 -0.0132 -0.0133 -0.0290 496 ALA C N   
12437 C CA  . ALA C 496 ? 0.6324 0.2208 0.5311 -0.0200 -0.0190 -0.0259 496 ALA C CA  
12438 C C   . ALA C 496 ? 0.6156 0.2225 0.5271 -0.0287 -0.0294 -0.0240 496 ALA C C   
12439 O O   . ALA C 496 ? 0.6210 0.2209 0.5208 -0.0329 -0.0379 -0.0284 496 ALA C O   
12440 C CB  . ALA C 496 ? 0.6573 0.2183 0.5418 -0.0225 -0.0230 -0.0307 496 ALA C CB  
12441 N N   . SER C 497 ? 0.5968 0.2272 0.5320 -0.0310 -0.0284 -0.0175 497 SER C N   
12442 C CA  . SER C 497 ? 0.5828 0.2325 0.5321 -0.0383 -0.0365 -0.0153 497 SER C CA  
12443 C C   . SER C 497 ? 0.5609 0.2233 0.5307 -0.0438 -0.0380 -0.0096 497 SER C C   
12444 O O   . SER C 497 ? 0.5643 0.2247 0.5392 -0.0409 -0.0319 -0.0062 497 SER C O   
12445 C CB  . SER C 497 ? 0.5735 0.2419 0.5279 -0.0343 -0.0329 -0.0135 497 SER C CB  
12446 O OG  . SER C 497 ? 0.5573 0.2388 0.5234 -0.0285 -0.0233 -0.0086 497 SER C OG  
12447 N N   . ALA C 498 ? 0.5473 0.2225 0.5289 -0.0517 -0.0461 -0.0083 498 ALA C N   
12448 C CA  . ALA C 498 ? 0.5383 0.2306 0.5408 -0.0566 -0.0463 -0.0020 498 ALA C CA  
12449 C C   . ALA C 498 ? 0.5210 0.2346 0.5370 -0.0614 -0.0516 -0.0005 498 ALA C C   
12450 O O   . ALA C 498 ? 0.5173 0.2282 0.5264 -0.0630 -0.0581 -0.0047 498 ALA C O   
12451 C CB  . ALA C 498 ? 0.5416 0.2195 0.5451 -0.0630 -0.0506 -0.0016 498 ALA C CB  
12452 N N   . GLY C 499 ? 0.5140 0.2481 0.5484 -0.0630 -0.0486 0.0054  499 GLY C N   
12453 C CA  . GLY C 499 ? 0.4973 0.2529 0.5456 -0.0661 -0.0516 0.0071  499 GLY C CA  
12454 C C   . GLY C 499 ? 0.4814 0.2560 0.5485 -0.0688 -0.0479 0.0138  499 GLY C C   
12455 O O   . GLY C 499 ? 0.4537 0.2287 0.5225 -0.0661 -0.0415 0.0177  499 GLY C O   
12456 N N   . ILE C 500 ? 0.4840 0.2748 0.5652 -0.0738 -0.0519 0.0152  500 ILE C N   
12457 C CA  . ILE C 500 ? 0.4605 0.2695 0.5585 -0.0764 -0.0480 0.0214  500 ILE C CA  
12458 C C   . ILE C 500 ? 0.4422 0.2715 0.5517 -0.0765 -0.0491 0.0213  500 ILE C C   
12459 O O   . ILE C 500 ? 0.4334 0.2618 0.5416 -0.0778 -0.0557 0.0174  500 ILE C O   
12460 C CB  . ILE C 500 ? 0.4579 0.2618 0.5644 -0.0848 -0.0511 0.0246  500 ILE C CB  
12461 C CG1 . ILE C 500 ? 0.4584 0.2777 0.5784 -0.0862 -0.0445 0.0319  500 ILE C CG1 
12462 C CG2 . ILE C 500 ? 0.4510 0.2551 0.5646 -0.0921 -0.0610 0.0221  500 ILE C CG2 
12463 C CD1 . ILE C 500 ? 0.4813 0.2938 0.6085 -0.0936 -0.0453 0.0366  500 ILE C CD1 
12464 N N   . SER C 501 ? 0.4370 0.2838 0.5570 -0.0751 -0.0429 0.0257  501 SER C N   
12465 C CA  . SER C 501 ? 0.4367 0.3028 0.5679 -0.0744 -0.0427 0.0258  501 SER C CA  
12466 C C   . SER C 501 ? 0.4368 0.3134 0.5854 -0.0819 -0.0461 0.0284  501 SER C C   
12467 O O   . SER C 501 ? 0.4720 0.3477 0.6275 -0.0871 -0.0446 0.0328  501 SER C O   
12468 C CB  . SER C 501 ? 0.4150 0.2930 0.5473 -0.0689 -0.0346 0.0284  501 SER C CB  
12469 O OG  . SER C 501 ? 0.4172 0.2877 0.5366 -0.0622 -0.0329 0.0253  501 SER C OG  
12470 N N   . VAL C 502 ? 0.4409 0.3277 0.5978 -0.0825 -0.0508 0.0261  502 VAL C N   
12471 C CA  . VAL C 502 ? 0.4679 0.3673 0.6444 -0.0890 -0.0540 0.0287  502 VAL C CA  
12472 C C   . VAL C 502 ? 0.4589 0.3793 0.6477 -0.0857 -0.0501 0.0295  502 VAL C C   
12473 O O   . VAL C 502 ? 0.4655 0.3879 0.6478 -0.0798 -0.0505 0.0259  502 VAL C O   
12474 C CB  . VAL C 502 ? 0.5014 0.3919 0.6787 -0.0940 -0.0657 0.0253  502 VAL C CB  
12475 C CG1 . VAL C 502 ? 0.5306 0.4355 0.7315 -0.1011 -0.0694 0.0285  502 VAL C CG1 
12476 C CG2 . VAL C 502 ? 0.5403 0.4079 0.7036 -0.0971 -0.0699 0.0235  502 VAL C CG2 
12477 N N   . ARG C 503 ? 0.4574 0.3926 0.6642 -0.0895 -0.0462 0.0343  503 ARG C N   
12478 C CA  . ARG C 503 ? 0.4581 0.4133 0.6776 -0.0864 -0.0411 0.0354  503 ARG C CA  
12479 C C   . ARG C 503 ? 0.4245 0.3915 0.6661 -0.0920 -0.0460 0.0370  503 ARG C C   
12480 O O   . ARG C 503 ? 0.4208 0.3865 0.6727 -0.0993 -0.0479 0.0406  503 ARG C O   
12481 C CB  . ARG C 503 ? 0.5066 0.4705 0.7269 -0.0843 -0.0297 0.0400  503 ARG C CB  
12482 C CG  . ARG C 503 ? 0.5749 0.5574 0.8051 -0.0799 -0.0238 0.0400  503 ARG C CG  
12483 C CD  . ARG C 503 ? 0.6333 0.6249 0.8649 -0.0787 -0.0126 0.0449  503 ARG C CD  
12484 N NE  . ARG C 503 ? 0.7533 0.7372 0.9657 -0.0731 -0.0085 0.0440  503 ARG C NE  
12485 C CZ  . ARG C 503 ? 0.7870 0.7720 0.9899 -0.0661 -0.0075 0.0398  503 ARG C CZ  
12486 N NH1 . ARG C 503 ? 0.7208 0.7154 0.9307 -0.0629 -0.0087 0.0361  503 ARG C NH1 
12487 N NH2 . ARG C 503 ? 0.7873 0.7638 0.9745 -0.0624 -0.0055 0.0395  503 ARG C NH2 
12488 N N   . TYR C 504 ? 0.3923 0.3699 0.6415 -0.0886 -0.0486 0.0344  504 TYR C N   
12489 C CA  . TYR C 504 ? 0.3595 0.3542 0.6334 -0.0918 -0.0502 0.0367  504 TYR C CA  
12490 C C   . TYR C 504 ? 0.3432 0.3535 0.6223 -0.0845 -0.0427 0.0360  504 TYR C C   
12491 O O   . TYR C 504 ? 0.3291 0.3378 0.6008 -0.0790 -0.0458 0.0316  504 TYR C O   
12492 C CB  . TYR C 504 ? 0.3530 0.3433 0.6327 -0.0954 -0.0639 0.0340  504 TYR C CB  
12493 C CG  . TYR C 504 ? 0.3488 0.3573 0.6574 -0.0993 -0.0667 0.0371  504 TYR C CG  
12494 C CD1 . TYR C 504 ? 0.3331 0.3589 0.6549 -0.0940 -0.0630 0.0370  504 TYR C CD1 
12495 C CD2 . TYR C 504 ? 0.3533 0.3620 0.6777 -0.1084 -0.0731 0.0403  504 TYR C CD2 
12496 C CE1 . TYR C 504 ? 0.3263 0.3695 0.6764 -0.0971 -0.0647 0.0402  504 TYR C CE1 
12497 C CE2 . TYR C 504 ? 0.3402 0.3670 0.6939 -0.1123 -0.0752 0.0439  504 TYR C CE2 
12498 C CZ  . TYR C 504 ? 0.3262 0.3707 0.6933 -0.1063 -0.0708 0.0439  504 TYR C CZ  
12499 O OH  . TYR C 504 ? 0.2991 0.3617 0.6967 -0.1097 -0.0728 0.0476  504 TYR C OH  
12500 N N   . GLY C 505 ? 0.3263 0.3507 0.6175 -0.0846 -0.0324 0.0404  505 GLY C N   
12501 C CA  . GLY C 505 ? 0.3205 0.3583 0.6150 -0.0776 -0.0240 0.0396  505 GLY C CA  
12502 C C   . GLY C 505 ? 0.3307 0.3589 0.6015 -0.0710 -0.0204 0.0360  505 GLY C C   
12503 O O   . GLY C 505 ? 0.3413 0.3605 0.5990 -0.0718 -0.0168 0.0378  505 GLY C O   
12504 N N   . LYS C 506 ? 0.3294 0.3590 0.5958 -0.0647 -0.0222 0.0314  506 LYS C N   
12505 C CA  . LYS C 506 ? 0.3395 0.3602 0.5855 -0.0587 -0.0201 0.0279  506 LYS C CA  
12506 C C   . LYS C 506 ? 0.3428 0.3474 0.5748 -0.0587 -0.0289 0.0245  506 LYS C C   
12507 O O   . LYS C 506 ? 0.3753 0.3724 0.5921 -0.0539 -0.0279 0.0217  506 LYS C O   
12508 C CB  . LYS C 506 ? 0.3314 0.3614 0.5799 -0.0517 -0.0168 0.0246  506 LYS C CB  
12509 C CG  . LYS C 506 ? 0.3478 0.3940 0.6101 -0.0502 -0.0076 0.0267  506 LYS C CG  
12510 C CD  . LYS C 506 ? 0.3549 0.4079 0.6194 -0.0430 -0.0058 0.0225  506 LYS C CD  
12511 C CE  . LYS C 506 ? 0.3744 0.4420 0.6503 -0.0405 0.0042  0.0240  506 LYS C CE  
12512 N NZ  . LYS C 506 ? 0.3961 0.4683 0.6734 -0.0333 0.0055  0.0193  506 LYS C NZ  
12513 N N   . PHE C 507 ? 0.3349 0.3339 0.5716 -0.0641 -0.0374 0.0249  507 PHE C N   
12514 C CA  . PHE C 507 ? 0.3278 0.3106 0.5503 -0.0642 -0.0457 0.0216  507 PHE C CA  
12515 C C   . PHE C 507 ? 0.3448 0.3131 0.5548 -0.0677 -0.0454 0.0229  507 PHE C C   
12516 O O   . PHE C 507 ? 0.3637 0.3310 0.5813 -0.0740 -0.0469 0.0260  507 PHE C O   
12517 C CB  . PHE C 507 ? 0.3213 0.3063 0.5554 -0.0674 -0.0558 0.0208  507 PHE C CB  
12518 C CG  . PHE C 507 ? 0.3196 0.2882 0.5387 -0.0673 -0.0654 0.0173  507 PHE C CG  
12519 C CD1 . PHE C 507 ? 0.3132 0.2665 0.5228 -0.0724 -0.0709 0.0170  507 PHE C CD1 
12520 C CD2 . PHE C 507 ? 0.3209 0.2882 0.5341 -0.0620 -0.0686 0.0142  507 PHE C CD2 
12521 C CE1 . PHE C 507 ? 0.3308 0.2678 0.5241 -0.0719 -0.0788 0.0135  507 PHE C CE1 
12522 C CE2 . PHE C 507 ? 0.3281 0.2799 0.5262 -0.0618 -0.0768 0.0114  507 PHE C CE2 
12523 C CZ  . PHE C 507 ? 0.3497 0.2862 0.5370 -0.0666 -0.0816 0.0109  507 PHE C CZ  
12524 N N   . THR C 508 ? 0.3587 0.3157 0.5506 -0.0634 -0.0433 0.0208  508 THR C N   
12525 C CA  . THR C 508 ? 0.3886 0.3308 0.5675 -0.0651 -0.0425 0.0217  508 THR C CA  
12526 C C   . THR C 508 ? 0.3797 0.3058 0.5434 -0.0633 -0.0486 0.0176  508 THR C C   
12527 O O   . THR C 508 ? 0.3672 0.2941 0.5262 -0.0585 -0.0493 0.0148  508 THR C O   
12528 C CB  . THR C 508 ? 0.3942 0.3374 0.5659 -0.0611 -0.0338 0.0234  508 THR C CB  
12529 O OG1 . THR C 508 ? 0.4653 0.4133 0.6336 -0.0548 -0.0324 0.0203  508 THR C OG1 
12530 C CG2 . THR C 508 ? 0.4023 0.3584 0.5852 -0.0631 -0.0273 0.0279  508 THR C CG2 
12531 N N   . PHE C 509 ? 0.3839 0.2949 0.5398 -0.0673 -0.0527 0.0173  509 PHE C N   
12532 C CA  . PHE C 509 ? 0.3936 0.2871 0.5326 -0.0656 -0.0577 0.0134  509 PHE C CA  
12533 C C   . PHE C 509 ? 0.4057 0.2829 0.5350 -0.0685 -0.0576 0.0139  509 PHE C C   
12534 O O   . PHE C 509 ? 0.4059 0.2866 0.5426 -0.0717 -0.0540 0.0176  509 PHE C O   
12535 C CB  . PHE C 509 ? 0.3795 0.2718 0.5208 -0.0679 -0.0676 0.0108  509 PHE C CB  
12536 C CG  . PHE C 509 ? 0.3714 0.2631 0.5234 -0.0760 -0.0751 0.0120  509 PHE C CG  
12537 C CD1 . PHE C 509 ? 0.3568 0.2653 0.5302 -0.0800 -0.0731 0.0160  509 PHE C CD1 
12538 C CD2 . PHE C 509 ? 0.3802 0.2540 0.5208 -0.0796 -0.0837 0.0092  509 PHE C CD2 
12539 C CE1 . PHE C 509 ? 0.3654 0.2740 0.5511 -0.0880 -0.0798 0.0177  509 PHE C CE1 
12540 C CE2 . PHE C 509 ? 0.3882 0.2612 0.5399 -0.0877 -0.0914 0.0103  509 PHE C CE2 
12541 C CZ  . PHE C 509 ? 0.3721 0.2631 0.5475 -0.0921 -0.0896 0.0148  509 PHE C CZ  
12542 N N   . LYS C 510 ? 0.4487 0.3077 0.5610 -0.0671 -0.0611 0.0103  510 LYS C N   
12543 C CA  . LYS C 510 ? 0.4866 0.3275 0.5874 -0.0686 -0.0608 0.0098  510 LYS C CA  
12544 C C   . LYS C 510 ? 0.4828 0.3086 0.5760 -0.0734 -0.0710 0.0062  510 LYS C C   
12545 O O   . LYS C 510 ? 0.4543 0.2786 0.5427 -0.0725 -0.0771 0.0032  510 LYS C O   
12546 C CB  . LYS C 510 ? 0.5435 0.3744 0.6286 -0.0613 -0.0543 0.0083  510 LYS C CB  
12547 C CG  . LYS C 510 ? 0.5977 0.4415 0.6896 -0.0571 -0.0456 0.0118  510 LYS C CG  
12548 C CD  . LYS C 510 ? 0.6746 0.5103 0.7548 -0.0503 -0.0393 0.0112  510 LYS C CD  
12549 C CE  . LYS C 510 ? 0.6827 0.5253 0.7688 -0.0484 -0.0326 0.0155  510 LYS C CE  
12550 N NZ  . LYS C 510 ? 0.7378 0.5691 0.8220 -0.0522 -0.0332 0.0173  510 LYS C NZ  
12551 N N   . ILE C 511 ? 0.4845 0.2986 0.5765 -0.0785 -0.0733 0.0068  511 ILE C N   
12552 C CA  . ILE C 511 ? 0.4994 0.2936 0.5794 -0.0826 -0.0826 0.0026  511 ILE C CA  
12553 C C   . ILE C 511 ? 0.5122 0.2855 0.5736 -0.0791 -0.0778 0.0006  511 ILE C C   
12554 O O   . ILE C 511 ? 0.5215 0.2972 0.5865 -0.0772 -0.0697 0.0041  511 ILE C O   
12555 C CB  . ILE C 511 ? 0.4851 0.2818 0.5804 -0.0923 -0.0906 0.0044  511 ILE C CB  
12556 C CG1 . ILE C 511 ? 0.4876 0.2859 0.5927 -0.0956 -0.0846 0.0092  511 ILE C CG1 
12557 C CG2 . ILE C 511 ? 0.4781 0.2958 0.5929 -0.0950 -0.0951 0.0062  511 ILE C CG2 
12558 C CD1 . ILE C 511 ? 0.5071 0.3074 0.6286 -0.1057 -0.0916 0.0117  511 ILE C CD1 
12559 N N   . HIS C 512 ? 0.5010 0.2534 0.5424 -0.0781 -0.0829 -0.0048 512 HIS C N   
12560 C CA  . HIS C 512 ? 0.4983 0.2320 0.5205 -0.0722 -0.0764 -0.0072 512 HIS C CA  
12561 C C   . HIS C 512 ? 0.5239 0.2331 0.5238 -0.0729 -0.0840 -0.0137 512 HIS C C   
12562 O O   . HIS C 512 ? 0.5420 0.2502 0.5401 -0.0768 -0.0940 -0.0162 512 HIS C O   
12563 C CB  . HIS C 512 ? 0.4804 0.2229 0.4993 -0.0634 -0.0669 -0.0062 512 HIS C CB  
12564 C CG  . HIS C 512 ? 0.4827 0.2360 0.5030 -0.0622 -0.0706 -0.0073 512 HIS C CG  
12565 N ND1 . HIS C 512 ? 0.4983 0.2385 0.5026 -0.0622 -0.0779 -0.0119 512 HIS C ND1 
12566 C CD2 . HIS C 512 ? 0.4752 0.2507 0.5114 -0.0614 -0.0690 -0.0042 512 HIS C CD2 
12567 C CE1 . HIS C 512 ? 0.5104 0.2648 0.5213 -0.0612 -0.0804 -0.0111 512 HIS C CE1 
12568 N NE2 . HIS C 512 ? 0.4841 0.2601 0.5148 -0.0606 -0.0749 -0.0067 512 HIS C NE2 
12569 N N   . ASP C 513 ? 0.5553 0.2442 0.5378 -0.0687 -0.0789 -0.0163 513 ASP C N   
12570 C CA  . ASP C 513 ? 0.5709 0.2339 0.5277 -0.0674 -0.0835 -0.0230 513 ASP C CA  
12571 C C   . ASP C 513 ? 0.5924 0.2436 0.5338 -0.0580 -0.0715 -0.0241 513 ASP C C   
12572 O O   . ASP C 513 ? 0.5687 0.2309 0.5212 -0.0539 -0.0616 -0.0196 513 ASP C O   
12573 C CB  . ASP C 513 ? 0.5968 0.2433 0.5513 -0.0754 -0.0930 -0.0256 513 ASP C CB  
12574 C CG  . ASP C 513 ? 0.6150 0.2347 0.5434 -0.0764 -0.1020 -0.0332 513 ASP C CG  
12575 O OD1 . ASP C 513 ? 0.6066 0.2219 0.5182 -0.0714 -0.1020 -0.0362 513 ASP C OD1 
12576 O OD2 . ASP C 513 ? 0.6227 0.2254 0.5469 -0.0823 -0.1089 -0.0360 513 ASP C OD2 
12577 N N   . GLN C 514 ? 0.6411 0.2696 0.5567 -0.0546 -0.0726 -0.0300 514 GLN C N   
12578 C CA  . GLN C 514 ? 0.6538 0.2729 0.5539 -0.0448 -0.0609 -0.0312 514 GLN C CA  
12579 C C   . GLN C 514 ? 0.6702 0.2582 0.5405 -0.0430 -0.0634 -0.0385 514 GLN C C   
12580 O O   . GLN C 514 ? 0.7105 0.2889 0.5680 -0.0472 -0.0743 -0.0426 514 GLN C O   
12581 C CB  . GLN C 514 ? 0.6420 0.2772 0.5442 -0.0403 -0.0572 -0.0292 514 GLN C CB  
12582 C CG  . GLN C 514 ? 0.6506 0.2796 0.5408 -0.0303 -0.0441 -0.0292 514 GLN C CG  
12583 C CD  . GLN C 514 ? 0.6645 0.3019 0.5502 -0.0263 -0.0419 -0.0285 514 GLN C CD  
12584 O OE1 . GLN C 514 ? 0.7269 0.3539 0.5956 -0.0275 -0.0488 -0.0320 514 GLN C OE1 
12585 N NE2 . GLN C 514 ? 0.6512 0.3067 0.5515 -0.0217 -0.0328 -0.0237 514 GLN C NE2 
12586 N N   . LYS C 515 ? 0.6758 0.2478 0.5350 -0.0367 -0.0537 -0.0400 515 LYS C N   
12587 C CA  . LYS C 515 ? 0.7011 0.2427 0.5292 -0.0327 -0.0529 -0.0471 515 LYS C CA  
12588 C C   . LYS C 515 ? 0.7100 0.2477 0.5292 -0.0214 -0.0370 -0.0464 515 LYS C C   
12589 O O   . LYS C 515 ? 0.6999 0.2475 0.5351 -0.0175 -0.0275 -0.0419 515 LYS C O   
12590 C CB  . LYS C 515 ? 0.7014 0.2199 0.5216 -0.0358 -0.0565 -0.0512 515 LYS C CB  
12591 C CG  . LYS C 515 ? 0.6924 0.2140 0.5243 -0.0474 -0.0714 -0.0513 515 LYS C CG  
12592 C CD  . LYS C 515 ? 0.7029 0.2187 0.5224 -0.0533 -0.0858 -0.0557 515 LYS C CD  
12593 C CE  . LYS C 515 ? 0.6984 0.2216 0.5373 -0.0648 -0.0988 -0.0542 515 LYS C CE  
12594 N NZ  . LYS C 515 ? 0.7232 0.2382 0.5515 -0.0714 -0.1145 -0.0587 515 LYS C NZ  
12595 N N   . ILE C 516 ? 0.7521 0.2750 0.5458 -0.0165 -0.0346 -0.0507 516 ILE C N   
12596 C CA  . ILE C 516 ? 0.7729 0.2878 0.5545 -0.0056 -0.0191 -0.0508 516 ILE C CA  
12597 C C   . ILE C 516 ? 0.7772 0.2580 0.5300 -0.0021 -0.0170 -0.0582 516 ILE C C   
12598 O O   . ILE C 516 ? 0.7919 0.2537 0.5209 -0.0053 -0.0262 -0.0642 516 ILE C O   
12599 C CB  . ILE C 516 ? 0.7885 0.3111 0.5620 -0.0017 -0.0155 -0.0494 516 ILE C CB  
12600 C CG1 . ILE C 516 ? 0.7385 0.2935 0.5404 -0.0057 -0.0189 -0.0427 516 ILE C CG1 
12601 C CG2 . ILE C 516 ? 0.8232 0.3379 0.5860 0.0094  0.0018  -0.0488 516 ILE C CG2 
12602 C CD1 . ILE C 516 ? 0.7257 0.2882 0.5209 -0.0042 -0.0193 -0.0414 516 ILE C CD1 
12603 N N   . ILE C 517 ? 0.7840 0.2571 0.5392 0.0045  -0.0054 -0.0577 517 ILE C N   
12604 C CA  . ILE C 517 ? 0.8325 0.2727 0.5629 0.0074  -0.0038 -0.0649 517 ILE C CA  
12605 C C   . ILE C 517 ? 0.8461 0.2774 0.5673 0.0199  0.0145  -0.0649 517 ILE C C   
12606 O O   . ILE C 517 ? 0.8302 0.2818 0.5748 0.0245  0.0245  -0.0581 517 ILE C O   
12607 C CB  . ILE C 517 ? 0.8354 0.2719 0.5802 0.0013  -0.0105 -0.0648 517 ILE C CB  
12608 C CG1 . ILE C 517 ? 0.8293 0.2733 0.5826 -0.0112 -0.0282 -0.0650 517 ILE C CG1 
12609 C CG2 . ILE C 517 ? 0.8646 0.2673 0.5872 0.0054  -0.0072 -0.0718 517 ILE C CG2 
12610 C CD1 . ILE C 517 ? 0.8262 0.2821 0.6065 -0.0177 -0.0326 -0.0603 517 ILE C CD1 
12611 N N   . TYR C 518 ? 0.9001 0.3007 0.5873 0.0251  0.0183  -0.0724 518 TYR C N   
12612 C CA  . TYR C 518 ? 0.9249 0.3151 0.5987 0.0374  0.0363  -0.0730 518 TYR C CA  
12613 C C   . TYR C 518 ? 0.9525 0.3160 0.6143 0.0428  0.0425  -0.0782 518 TYR C C   
12614 O O   . TYR C 518 ? 0.9516 0.2966 0.6035 0.0367  0.0311  -0.0838 518 TYR C O   
12615 C CB  . TYR C 518 ? 0.9609 0.3356 0.6015 0.0410  0.0387  -0.0773 518 TYR C CB  
12616 C CG  . TYR C 518 ? 0.9600 0.3570 0.6074 0.0372  0.0338  -0.0726 518 TYR C CG  
12617 C CD1 . TYR C 518 ? 0.9410 0.3611 0.6062 0.0426  0.0461  -0.0651 518 TYR C CD1 
12618 C CD2 . TYR C 518 ? 0.9548 0.3493 0.5916 0.0281  0.0166  -0.0755 518 TYR C CD2 
12619 C CE1 . TYR C 518 ? 0.9252 0.3642 0.5966 0.0393  0.0416  -0.0609 518 TYR C CE1 
12620 C CE2 . TYR C 518 ? 0.9390 0.3532 0.5827 0.0251  0.0121  -0.0710 518 TYR C CE2 
12621 C CZ  . TYR C 518 ? 0.9294 0.3650 0.5893 0.0308  0.0248  -0.0639 518 TYR C CZ  
12622 O OH  . TYR C 518 ? 0.8709 0.3238 0.5362 0.0279  0.0202  -0.0597 518 TYR C OH  
12623 N N   . ARG C 519 ? 0.9673 0.3282 0.6299 0.0543  0.0606  -0.0764 519 ARG C N   
12624 C CA  . ARG C 519 ? 1.0217 0.3566 0.6724 0.0616  0.0690  -0.0812 519 ARG C CA  
12625 C C   . ARG C 519 ? 1.1278 0.4273 0.7345 0.0668  0.0729  -0.0909 519 ARG C C   
12626 O O   . ARG C 519 ? 1.1491 0.4203 0.7321 0.0631  0.0634  -0.0994 519 ARG C O   
12627 C CB  . ARG C 519 ? 0.9801 0.3296 0.6555 0.0717  0.0862  -0.0743 519 ARG C CB  
12628 C CG  . ARG C 519 ? 0.9753 0.2990 0.6416 0.0802  0.0958  -0.0787 519 ARG C CG  
12629 C CD  . ARG C 519 ? 0.9453 0.2843 0.6380 0.0904  0.1120  -0.0714 519 ARG C CD  
12630 N NE  . ARG C 519 ? 0.9136 0.2793 0.6437 0.0852  0.1055  -0.0631 519 ARG C NE  
12631 C CZ  . ARG C 519 ? 0.9341 0.2929 0.6731 0.0809  0.0975  -0.0634 519 ARG C CZ  
12632 N NH1 . ARG C 519 ? 0.9658 0.2916 0.6806 0.0808  0.0941  -0.0718 519 ARG C NH1 
12633 N NH2 . ARG C 519 ? 0.9163 0.2998 0.6879 0.0771  0.0932  -0.0551 519 ARG C NH2 
12634 N N   . GLY C 520 ? 1.1723 0.4710 0.7665 0.0762  0.0879  -0.0899 520 GLY C N   
12635 C CA  . GLY C 520 ? 1.2374 0.4996 0.7888 0.0831  0.0945  -0.0992 520 GLY C CA  
12636 C C   . GLY C 520 ? 1.2352 0.4858 0.7567 0.0759  0.0806  -0.1044 520 GLY C C   
12637 O O   . GLY C 520 ? 1.1844 0.4457 0.7154 0.0641  0.0621  -0.1038 520 GLY C O   
12638 N N   . ASP C 521 ? 1.2395 0.4697 0.7262 0.0835  0.0906  -0.1086 521 ASP C N   
12639 C CA  . ASP C 521 ? 1.2420 0.4743 0.7095 0.0799  0.0842  -0.1083 521 ASP C CA  
12640 C C   . ASP C 521 ? 1.1886 0.4445 0.6709 0.0871  0.1012  -0.0992 521 ASP C C   
12641 O O   . ASP C 521 ? 1.2224 0.4719 0.6804 0.0890  0.1037  -0.0994 521 ASP C O   
12642 C CB  . ASP C 521 ? 1.2950 0.4864 0.7105 0.0822  0.0812  -0.1192 521 ASP C CB  
12643 C CG  . ASP C 521 ? 1.3433 0.5096 0.7343 0.0963  0.1030  -0.1234 521 ASP C CG  
12644 O OD1 . ASP C 521 ? 1.3070 0.4918 0.7231 0.1046  0.1215  -0.1161 521 ASP C OD1 
12645 O OD2 . ASP C 521 ? 1.3830 0.5115 0.7311 0.0988  0.1011  -0.1338 521 ASP C OD2 
12646 N N   . TRP C 522 ? 1.1165 0.3986 0.6377 0.0909  0.1122  -0.0912 522 TRP C N   
12647 C CA  . TRP C 522 ? 1.0958 0.3995 0.6342 0.0983  0.1295  -0.0826 522 TRP C CA  
12648 C C   . TRP C 522 ? 1.1010 0.4261 0.6451 0.0919  0.1219  -0.0770 522 TRP C C   
12649 O O   . TRP C 522 ? 1.0542 0.3865 0.5960 0.0976  0.1348  -0.0722 522 TRP C O   
12650 C CB  . TRP C 522 ? 1.0421 0.3718 0.6248 0.1014  0.1380  -0.0750 522 TRP C CB  
12651 C CG  . TRP C 522 ? 0.9918 0.3544 0.6116 0.0913  0.1241  -0.0684 522 TRP C CG  
12652 C CD1 . TRP C 522 ? 0.9744 0.3402 0.6069 0.0824  0.1082  -0.0700 522 TRP C CD1 
12653 C CD2 . TRP C 522 ? 0.9781 0.3740 0.6252 0.0886  0.1247  -0.0594 522 TRP C CD2 
12654 N NE1 . TRP C 522 ? 0.9183 0.3163 0.5828 0.0750  0.0995  -0.0629 522 TRP C NE1 
12655 C CE2 . TRP C 522 ? 0.9316 0.3482 0.6053 0.0786  0.1090  -0.0566 522 TRP C CE2 
12656 C CE3 . TRP C 522 ? 0.9738 0.3831 0.6254 0.0936  0.1369  -0.0534 522 TRP C CE3 
12657 C CZ2 . TRP C 522 ? 0.8950 0.3440 0.5977 0.0740  0.1053  -0.0488 522 TRP C CZ2 
12658 C CZ3 . TRP C 522 ? 0.9313 0.3727 0.6128 0.0885  0.1325  -0.0456 522 TRP C CZ3 
12659 C CH2 . TRP C 522 ? 0.8963 0.3567 0.6021 0.0790  0.1167  -0.0437 522 TRP C CH2 
12660 N N   . ALA C 523 ? 1.1121 0.4467 0.6641 0.0802  0.1011  -0.0776 523 ALA C N   
12661 C CA  . ALA C 523 ? 1.1460 0.5021 0.7075 0.0733  0.0915  -0.0725 523 ALA C CA  
12662 C C   . ALA C 523 ? 1.2221 0.5572 0.7465 0.0685  0.0781  -0.0785 523 ALA C C   
12663 O O   . ALA C 523 ? 1.2753 0.6264 0.8085 0.0606  0.0648  -0.0755 523 ALA C O   
12664 C CB  . ALA C 523 ? 1.1067 0.4909 0.7067 0.0640  0.0784  -0.0681 523 ALA C CB  
12665 N N   . LYS C 524 ? 1.2527 0.5523 0.7353 0.0734  0.0814  -0.0868 524 LYS C N   
12666 C CA  . LYS C 524 ? 1.2816 0.5605 0.7277 0.0687  0.0673  -0.0925 524 LYS C CA  
12667 C C   . LYS C 524 ? 1.2302 0.5219 0.6723 0.0699  0.0709  -0.0859 524 LYS C C   
12668 O O   . LYS C 524 ? 1.2218 0.5120 0.6516 0.0629  0.0547  -0.0869 524 LYS C O   
12669 C CB  . LYS C 524 ? 1.3961 0.6320 0.7933 0.0732  0.0682  -0.1032 524 LYS C CB  
12670 C CG  . LYS C 524 ? 1.4831 0.6978 0.8490 0.0861  0.0903  -0.1045 524 LYS C CG  
12671 C CD  . LYS C 524 ? 1.6005 0.7729 0.9243 0.0906  0.0912  -0.1163 524 LYS C CD  
12672 C CE  . LYS C 524 ? 1.6611 0.8062 0.9444 0.1030  0.1110  -0.1194 524 LYS C CE  
12673 N NZ  . LYS C 524 ? 1.6402 0.7980 0.9447 0.1140  0.1367  -0.1134 524 LYS C NZ  
12674 N N   . GLU C 525 ? 1.1918 0.4977 0.6477 0.0781  0.0910  -0.0788 525 GLU C N   
12675 C CA  . GLU C 525 ? 1.1958 0.5139 0.6495 0.0792  0.0956  -0.0718 525 GLU C CA  
12676 C C   . GLU C 525 ? 1.1450 0.5017 0.6431 0.0723  0.0883  -0.0633 525 GLU C C   
12677 O O   . GLU C 525 ? 1.1074 0.4719 0.6048 0.0652  0.0735  -0.0618 525 GLU C O   
12678 C CB  . GLU C 525 ? 1.1931 0.5069 0.6382 0.0909  0.1208  -0.0677 525 GLU C CB  
12679 C CG  . GLU C 525 ? 1.2280 0.5034 0.6278 0.0996  0.1318  -0.0756 525 GLU C CG  
12680 C CD  . GLU C 525 ? 1.2287 0.4930 0.6340 0.1048  0.1402  -0.0808 525 GLU C CD  
12681 O OE1 . GLU C 525 ? 1.1614 0.4484 0.6068 0.1056  0.1460  -0.0762 525 GLU C OE1 
12682 O OE2 . GLU C 525 ? 1.2888 0.5185 0.6547 0.1081  0.1400  -0.0901 525 GLU C OE2 
12683 N N   . VAL C 526 ? 1.1217 0.5015 0.6577 0.0744  0.0979  -0.0581 526 VAL C N   
12684 C CA  . VAL C 526 ? 1.0649 0.4806 0.6422 0.0699  0.0951  -0.0497 526 VAL C CA  
12685 C C   . VAL C 526 ? 1.0781 0.5082 0.6748 0.0588  0.0738  -0.0508 526 VAL C C   
12686 O O   . VAL C 526 ? 1.0857 0.5405 0.7055 0.0538  0.0672  -0.0451 526 VAL C O   
12687 C CB  . VAL C 526 ? 1.0434 0.4781 0.6537 0.0760  0.1117  -0.0439 526 VAL C CB  
12688 C CG1 . VAL C 526 ? 1.0482 0.4773 0.6685 0.0773  0.1125  -0.0478 526 VAL C CG1 
12689 C CG2 . VAL C 526 ? 1.0067 0.4769 0.6568 0.0715  0.1087  -0.0355 526 VAL C CG2 
12690 N N   . GLY C 527 ? 1.0491 0.4639 0.6372 0.0549  0.0633  -0.0579 527 GLY C N   
12691 C CA  . GLY C 527 ? 1.0003 0.4294 0.6105 0.0447  0.0453  -0.0584 527 GLY C CA  
12692 C C   . GLY C 527 ? 1.0205 0.4474 0.6178 0.0366  0.0266  -0.0603 527 GLY C C   
12693 O O   . GLY C 527 ? 1.0418 0.4447 0.6032 0.0378  0.0230  -0.0649 527 GLY C O   
12694 N N   . ARG C 528 ? 1.0169 0.4685 0.6435 0.0285  0.0142  -0.0568 528 ARG C N   
12695 C CA  . ARG C 528 ? 1.0315 0.4843 0.6518 0.0207  -0.0041 -0.0580 528 ARG C CA  
12696 C C   . ARG C 528 ? 1.0970 0.5206 0.6877 0.0169  -0.0168 -0.0667 528 ARG C C   
12697 O O   . ARG C 528 ? 1.0885 0.5014 0.6799 0.0162  -0.0168 -0.0710 528 ARG C O   
12698 C CB  . ARG C 528 ? 0.9817 0.4647 0.6402 0.0127  -0.0147 -0.0536 528 ARG C CB  
12699 C CG  . ARG C 528 ? 0.9639 0.4521 0.6209 0.0053  -0.0326 -0.0535 528 ARG C CG  
12700 C CD  . ARG C 528 ? 0.9076 0.4265 0.6035 -0.0015 -0.0404 -0.0489 528 ARG C CD  
12701 N NE  . ARG C 528 ? 0.8459 0.3897 0.5662 0.0022  -0.0291 -0.0418 528 ARG C NE  
12702 C CZ  . ARG C 528 ? 0.8067 0.3676 0.5534 0.0038  -0.0198 -0.0382 528 ARG C CZ  
12703 N NH1 . ARG C 528 ? 0.8028 0.3599 0.5568 0.0022  -0.0196 -0.0405 528 ARG C NH1 
12704 N NH2 . ARG C 528 ? 0.7760 0.3572 0.5418 0.0071  -0.0108 -0.0322 528 ARG C NH2 
12705 N N   . LYS C 529 ? 1.1736 0.5851 0.7398 0.0142  -0.0287 -0.0690 529 LYS C N   
12706 C CA  . LYS C 529 ? 1.2777 0.6621 0.8151 0.0095  -0.0440 -0.0773 529 LYS C CA  
12707 C C   . LYS C 529 ? 1.2399 0.6390 0.7952 -0.0014 -0.0658 -0.0764 529 LYS C C   
12708 O O   . LYS C 529 ? 1.1654 0.5907 0.7440 -0.0031 -0.0675 -0.0696 529 LYS C O   
12709 C CB  . LYS C 529 ? 1.3870 0.7425 0.8781 0.0152  -0.0415 -0.0810 529 LYS C CB  
12710 C CG  . LYS C 529 ? 1.4657 0.7913 0.9248 0.0242  -0.0261 -0.0867 529 LYS C CG  
12711 C CD  . LYS C 529 ? 1.4995 0.8324 0.9650 0.0347  -0.0012 -0.0816 529 LYS C CD  
12712 C CE  . LYS C 529 ? 1.4888 0.8300 0.9476 0.0392  0.0070  -0.0749 529 LYS C CE  
12713 N NZ  . LYS C 529 ? 1.4329 0.7782 0.8965 0.0492  0.0313  -0.0705 529 LYS C NZ  
12714 N N   . SER D 3   ? 1.0478 0.6501 0.9657 -0.1150 -0.1273 -0.0803 3   SER D N   
12715 C CA  . SER D 3   ? 1.0608 0.6868 0.9888 -0.1131 -0.1279 -0.0774 3   SER D CA  
12716 C C   . SER D 3   ? 0.9693 0.6205 0.9217 -0.1032 -0.1190 -0.0726 3   SER D C   
12717 O O   . SER D 3   ? 0.9765 0.6323 0.9424 -0.1009 -0.1151 -0.0697 3   SER D O   
12718 C CB  . SER D 3   ? 1.0729 0.7108 1.0074 -0.1264 -0.1404 -0.0733 3   SER D CB  
12719 O OG  . SER D 3   ? 1.0272 0.6834 0.9858 -0.1318 -0.1432 -0.0663 3   SER D OG  
12720 N N   . LYS D 4   ? 0.8481 0.5146 0.8050 -0.0974 -0.1158 -0.0717 4   LYS D N   
12721 C CA  . LYS D 4   ? 0.7884 0.4737 0.7630 -0.0868 -0.1063 -0.0687 4   LYS D CA  
12722 C C   . LYS D 4   ? 0.6946 0.4072 0.6962 -0.0904 -0.1092 -0.0611 4   LYS D C   
12723 O O   . LYS D 4   ? 0.6797 0.4013 0.6867 -0.0996 -0.1181 -0.0579 4   LYS D O   
12724 C CB  . LYS D 4   ? 0.8357 0.5209 0.7993 -0.0797 -0.1018 -0.0717 4   LYS D CB  
12725 C CG  . LYS D 4   ? 0.8664 0.5678 0.8349 -0.0844 -0.1081 -0.0685 4   LYS D CG  
12726 C CD  . LYS D 4   ? 0.9160 0.6092 0.8657 -0.0803 -0.1060 -0.0725 4   LYS D CD  
12727 C CE  . LYS D 4   ? 0.9740 0.6893 0.9354 -0.0808 -0.1087 -0.0678 4   LYS D CE  
12728 N NZ  . LYS D 4   ? 0.9410 0.6640 0.9067 -0.0919 -0.1207 -0.0643 4   LYS D NZ  
12729 N N   . THR D 5   ? 0.6269 0.3534 0.6457 -0.0828 -0.1014 -0.0580 5   THR D N   
12730 C CA  . THR D 5   ? 0.5822 0.3342 0.6258 -0.0843 -0.1023 -0.0513 5   THR D CA  
12731 C C   . THR D 5   ? 0.5824 0.3509 0.6325 -0.0885 -0.1083 -0.0482 5   THR D C   
12732 O O   . THR D 5   ? 0.5723 0.3413 0.6148 -0.0845 -0.1068 -0.0501 5   THR D O   
12733 C CB  . THR D 5   ? 0.5470 0.3110 0.6032 -0.0735 -0.0924 -0.0498 5   THR D CB  
12734 O OG1 . THR D 5   ? 0.5331 0.2820 0.5823 -0.0679 -0.0862 -0.0527 5   THR D OG1 
12735 C CG2 . THR D 5   ? 0.5103 0.2967 0.5902 -0.0747 -0.0924 -0.0434 5   THR D CG2 
12736 N N   . LYS D 6   ? 0.6235 0.4066 0.6887 -0.0962 -0.1147 -0.0428 6   LYS D N   
12737 C CA  . LYS D 6   ? 0.6524 0.4551 0.7287 -0.0993 -0.1199 -0.0384 6   LYS D CA  
12738 C C   . LYS D 6   ? 0.6010 0.4267 0.6996 -0.0931 -0.1141 -0.0334 6   LYS D C   
12739 O O   . LYS D 6   ? 0.5615 0.3953 0.6740 -0.0944 -0.1129 -0.0300 6   LYS D O   
12740 C CB  . LYS D 6   ? 0.7669 0.5723 0.8469 -0.1117 -0.1306 -0.0350 6   LYS D CB  
12741 C CG  . LYS D 6   ? 0.8785 0.7062 0.9730 -0.1159 -0.1371 -0.0291 6   LYS D CG  
12742 C CD  . LYS D 6   ? 1.0043 0.8331 1.0997 -0.1290 -0.1487 -0.0262 6   LYS D CD  
12743 C CE  . LYS D 6   ? 1.1378 0.9726 1.2473 -0.1355 -0.1505 -0.0218 6   LYS D CE  
12744 N NZ  . LYS D 6   ? 1.1718 1.0344 1.3067 -0.1335 -0.1488 -0.0146 6   LYS D NZ  
12745 N N   . ILE D 7   ? 0.5667 0.4024 0.6680 -0.0867 -0.1108 -0.0330 7   ILE D N   
12746 C CA  . ILE D 7   ? 0.5163 0.3726 0.6373 -0.0811 -0.1059 -0.0286 7   ILE D CA  
12747 C C   . ILE D 7   ? 0.4942 0.3683 0.6270 -0.0851 -0.1121 -0.0235 7   ILE D C   
12748 O O   . ILE D 7   ? 0.4589 0.3322 0.5839 -0.0860 -0.1160 -0.0240 7   ILE D O   
12749 C CB  . ILE D 7   ? 0.4956 0.3520 0.6139 -0.0709 -0.0973 -0.0309 7   ILE D CB  
12750 C CG1 . ILE D 7   ? 0.4980 0.3390 0.6069 -0.0659 -0.0905 -0.0353 7   ILE D CG1 
12751 C CG2 . ILE D 7   ? 0.4681 0.3451 0.6057 -0.0663 -0.0935 -0.0264 7   ILE D CG2 
12752 C CD1 . ILE D 7   ? 0.4820 0.3213 0.5858 -0.0566 -0.0825 -0.0379 7   ILE D CD1 
12753 N N   . GLU D 8   ? 0.5046 0.3950 0.6562 -0.0869 -0.1125 -0.0182 8   GLU D N   
12754 C CA  . GLU D 8   ? 0.5172 0.4270 0.6832 -0.0892 -0.1172 -0.0126 8   GLU D CA  
12755 C C   . GLU D 8   ? 0.4549 0.3817 0.6381 -0.0819 -0.1102 -0.0092 8   GLU D C   
12756 O O   . GLU D 8   ? 0.3876 0.3162 0.5779 -0.0795 -0.1048 -0.0088 8   GLU D O   
12757 C CB  . GLU D 8   ? 0.5980 0.5127 0.7706 -0.0996 -0.1255 -0.0087 8   GLU D CB  
12758 C CG  . GLU D 8   ? 0.6939 0.6267 0.8780 -0.1027 -0.1321 -0.0031 8   GLU D CG  
12759 C CD  . GLU D 8   ? 0.7864 0.7247 0.9767 -0.1140 -0.1415 0.0011  8   GLU D CD  
12760 O OE1 . GLU D 8   ? 0.7818 0.7071 0.9647 -0.1208 -0.1439 -0.0009 8   GLU D OE1 
12761 O OE2 . GLU D 8   ? 0.7840 0.7399 0.9867 -0.1160 -0.1464 0.0067  8   GLU D OE2 
12762 N N   . LEU D 9   ? 0.4395 0.3784 0.6288 -0.0785 -0.1110 -0.0066 9   LEU D N   
12763 C CA  . LEU D 9   ? 0.4353 0.3896 0.6398 -0.0718 -0.1053 -0.0034 9   LEU D CA  
12764 C C   . LEU D 9   ? 0.4419 0.4145 0.6623 -0.0753 -0.1103 0.0030  9   LEU D C   
12765 O O   . LEU D 9   ? 0.4543 0.4309 0.6735 -0.0773 -0.1162 0.0049  9   LEU D O   
12766 C CB  . LEU D 9   ? 0.4044 0.3573 0.6032 -0.0645 -0.1015 -0.0052 9   LEU D CB  
12767 C CG  . LEU D 9   ? 0.4101 0.3465 0.5934 -0.0607 -0.0963 -0.0111 9   LEU D CG  
12768 C CD1 . LEU D 9   ? 0.4221 0.3613 0.6037 -0.0540 -0.0926 -0.0113 9   LEU D CD1 
12769 C CD2 . LEU D 9   ? 0.3945 0.3265 0.5800 -0.0581 -0.0899 -0.0130 9   LEU D CD2 
12770 N N   . LYS D 10  ? 0.4542 0.4377 0.6892 -0.0760 -0.1078 0.0065  10  LYS D N   
12771 C CA  . LYS D 10  ? 0.4745 0.4778 0.7270 -0.0773 -0.1106 0.0131  10  LYS D CA  
12772 C C   . LYS D 10  ? 0.4307 0.4441 0.6968 -0.0744 -0.1040 0.0156  10  LYS D C   
12773 O O   . LYS D 10  ? 0.3744 0.3788 0.6360 -0.0736 -0.0993 0.0126  10  LYS D O   
12774 C CB  . LYS D 10  ? 0.6078 0.6147 0.8620 -0.0873 -0.1205 0.0164  10  LYS D CB  
12775 C CG  . LYS D 10  ? 0.6973 0.7030 0.9549 -0.0959 -0.1233 0.0179  10  LYS D CG  
12776 C CD  . LYS D 10  ? 0.7689 0.7819 1.0310 -0.1059 -0.1339 0.0224  10  LYS D CD  
12777 C CE  . LYS D 10  ? 0.8501 0.8693 1.1224 -0.1142 -0.1362 0.0264  10  LYS D CE  
12778 N NZ  . LYS D 10  ? 0.8911 0.8918 1.1519 -0.1168 -0.1334 0.0218  10  LYS D NZ  
12779 N N   . ASP D 11  ? 0.3851 0.4173 0.6674 -0.0721 -0.1035 0.0212  11  ASP D N   
12780 C CA  . ASP D 11  ? 0.3499 0.3934 0.6453 -0.0677 -0.0965 0.0238  11  ASP D CA  
12781 C C   . ASP D 11  ? 0.3262 0.3605 0.6146 -0.0601 -0.0883 0.0191  11  ASP D C   
12782 O O   . ASP D 11  ? 0.3289 0.3652 0.6218 -0.0584 -0.0828 0.0194  11  ASP D O   
12783 C CB  . ASP D 11  ? 0.3886 0.4357 0.6907 -0.0746 -0.0974 0.0266  11  ASP D CB  
12784 C CG  . ASP D 11  ? 0.4240 0.4765 0.7303 -0.0846 -0.1065 0.0306  11  ASP D CG  
12785 O OD1 . ASP D 11  ? 0.3923 0.4604 0.7100 -0.0849 -0.1103 0.0357  11  ASP D OD1 
12786 O OD2 . ASP D 11  ? 0.4689 0.5098 0.7674 -0.0922 -0.1098 0.0289  11  ASP D OD2 
12787 N N   . ASN D 12  ? 0.3482 0.3725 0.6253 -0.0561 -0.0877 0.0150  12  ASN D N   
12788 C CA  . ASN D 12  ? 0.3517 0.3687 0.6229 -0.0490 -0.0805 0.0110  12  ASN D CA  
12789 C C   . ASN D 12  ? 0.3300 0.3341 0.5926 -0.0504 -0.0775 0.0071  12  ASN D C   
12790 O O   . ASN D 12  ? 0.3006 0.3019 0.5621 -0.0453 -0.0713 0.0050  12  ASN D O   
12791 C CB  . ASN D 12  ? 0.3201 0.3493 0.6028 -0.0424 -0.0749 0.0136  12  ASN D CB  
12792 C CG  . ASN D 12  ? 0.3481 0.3872 0.6371 -0.0397 -0.0775 0.0169  12  ASN D CG  
12793 O OD1 . ASN D 12  ? 0.3849 0.4197 0.6672 -0.0411 -0.0824 0.0164  12  ASN D OD1 
12794 N ND2 . ASN D 12  ? 0.3489 0.4004 0.6498 -0.0350 -0.0738 0.0204  12  ASN D ND2 
12795 N N   . TRP D 13  ? 0.3215 0.3168 0.5771 -0.0572 -0.0825 0.0061  13  TRP D N   
12796 C CA  . TRP D 13  ? 0.3262 0.3075 0.5725 -0.0589 -0.0807 0.0025  13  TRP D CA  
12797 C C   . TRP D 13  ? 0.3480 0.3136 0.5785 -0.0618 -0.0849 -0.0016 13  TRP D C   
12798 O O   . TRP D 13  ? 0.3494 0.3156 0.5777 -0.0667 -0.0915 -0.0005 13  TRP D O   
12799 C CB  . TRP D 13  ? 0.3139 0.2978 0.5664 -0.0653 -0.0825 0.0055  13  TRP D CB  
12800 C CG  . TRP D 13  ? 0.3108 0.3049 0.5746 -0.0622 -0.0767 0.0083  13  TRP D CG  
12801 C CD1 . TRP D 13  ? 0.3082 0.3193 0.5860 -0.0605 -0.0751 0.0129  13  TRP D CD1 
12802 C CD2 . TRP D 13  ? 0.3256 0.3131 0.5866 -0.0600 -0.0715 0.0068  13  TRP D CD2 
12803 N NE1 . TRP D 13  ? 0.2964 0.3112 0.5792 -0.0576 -0.0691 0.0140  13  TRP D NE1 
12804 C CE2 . TRP D 13  ? 0.3012 0.3020 0.5741 -0.0575 -0.0671 0.0105  13  TRP D CE2 
12805 C CE3 . TRP D 13  ? 0.3447 0.3163 0.5942 -0.0595 -0.0700 0.0029  13  TRP D CE3 
12806 C CZ2 . TRP D 13  ? 0.3138 0.3126 0.5869 -0.0551 -0.0619 0.0103  13  TRP D CZ2 
12807 C CZ3 . TRP D 13  ? 0.3402 0.3105 0.5911 -0.0568 -0.0649 0.0031  13  TRP D CZ3 
12808 C CH2 . TRP D 13  ? 0.3234 0.3071 0.5856 -0.0549 -0.0611 0.0068  13  TRP D CH2 
12809 N N   . TYR D 14  ? 0.3630 0.3150 0.5826 -0.0586 -0.0809 -0.0061 14  TYR D N   
12810 C CA  . TYR D 14  ? 0.3752 0.3098 0.5791 -0.0618 -0.0838 -0.0102 14  TYR D CA  
12811 C C   . TYR D 14  ? 0.3738 0.3033 0.5777 -0.0693 -0.0877 -0.0091 14  TYR D C   
12812 O O   . TYR D 14  ? 0.3687 0.3027 0.5809 -0.0695 -0.0849 -0.0068 14  TYR D O   
12813 C CB  . TYR D 14  ? 0.3789 0.3009 0.5727 -0.0560 -0.0777 -0.0148 14  TYR D CB  
12814 C CG  . TYR D 14  ? 0.3712 0.2932 0.5606 -0.0494 -0.0739 -0.0169 14  TYR D CG  
12815 C CD1 . TYR D 14  ? 0.3518 0.2867 0.5514 -0.0445 -0.0703 -0.0147 14  TYR D CD1 
12816 C CD2 . TYR D 14  ? 0.3993 0.3074 0.5736 -0.0477 -0.0731 -0.0213 14  TYR D CD2 
12817 C CE1 . TYR D 14  ? 0.3461 0.2801 0.5415 -0.0390 -0.0667 -0.0165 14  TYR D CE1 
12818 C CE2 . TYR D 14  ? 0.3891 0.2973 0.5596 -0.0418 -0.0690 -0.0229 14  TYR D CE2 
12819 C CZ  . TYR D 14  ? 0.3680 0.2893 0.5493 -0.0378 -0.0661 -0.0203 14  TYR D CZ  
12820 O OH  . TYR D 14  ? 0.3892 0.3102 0.5665 -0.0328 -0.0622 -0.0216 14  TYR D OH  
12821 N N   . HIS D 15  ? 0.3976 0.3171 0.5913 -0.0759 -0.0944 -0.0105 15  HIS D N   
12822 C CA  . HIS D 15  ? 0.4099 0.3195 0.5994 -0.0837 -0.0986 -0.0105 15  HIS D CA  
12823 C C   . HIS D 15  ? 0.4160 0.3028 0.5851 -0.0836 -0.0990 -0.0166 15  HIS D C   
12824 O O   . HIS D 15  ? 0.4054 0.2864 0.5637 -0.0825 -0.1009 -0.0195 15  HIS D O   
12825 C CB  . HIS D 15  ? 0.4209 0.3387 0.6160 -0.0928 -0.1074 -0.0065 15  HIS D CB  
12826 C CG  . HIS D 15  ? 0.4111 0.3519 0.6263 -0.0927 -0.1071 -0.0002 15  HIS D CG  
12827 N ND1 . HIS D 15  ? 0.4084 0.3625 0.6312 -0.0862 -0.1045 0.0013  15  HIS D ND1 
12828 C CD2 . HIS D 15  ? 0.4154 0.3680 0.6442 -0.0980 -0.1089 0.0051  15  HIS D CD2 
12829 C CE1 . HIS D 15  ? 0.3913 0.3641 0.6316 -0.0871 -0.1044 0.0071  15  HIS D CE1 
12830 N NE2 . HIS D 15  ? 0.3771 0.3500 0.6215 -0.0941 -0.1068 0.0096  15  HIS D NE2 
12831 N N   . LEU D 16  ? 0.4305 0.3042 0.5940 -0.0840 -0.0966 -0.0184 16  LEU D N   
12832 C CA  . LEU D 16  ? 0.4705 0.3210 0.6145 -0.0847 -0.0975 -0.0240 16  LEU D CA  
12833 C C   . LEU D 16  ? 0.4721 0.3127 0.6116 -0.0953 -0.1047 -0.0232 16  LEU D C   
12834 O O   . LEU D 16  ? 0.4466 0.2897 0.5944 -0.0981 -0.1041 -0.0200 16  LEU D O   
12835 C CB  . LEU D 16  ? 0.4679 0.3091 0.6075 -0.0765 -0.0893 -0.0268 16  LEU D CB  
12836 C CG  . LEU D 16  ? 0.4942 0.3338 0.6274 -0.0673 -0.0835 -0.0303 16  LEU D CG  
12837 C CD1 . LEU D 16  ? 0.4590 0.3183 0.6042 -0.0646 -0.0827 -0.0274 16  LEU D CD1 
12838 C CD2 . LEU D 16  ? 0.4871 0.3205 0.6189 -0.0592 -0.0756 -0.0321 16  LEU D CD2 
12839 N N   . ASP D 17  ? 0.5127 0.3422 0.6387 -0.1013 -0.1116 -0.0258 17  ASP D N   
12840 C CA  . ASP D 17  ? 0.5415 0.3589 0.6605 -0.1123 -0.1195 -0.0257 17  ASP D CA  
12841 C C   . ASP D 17  ? 0.5513 0.3872 0.6897 -0.1196 -0.1234 -0.0185 17  ASP D C   
12842 O O   . ASP D 17  ? 0.5213 0.3504 0.6604 -0.1260 -0.1255 -0.0169 17  ASP D O   
12843 C CB  . ASP D 17  ? 0.5499 0.3427 0.6538 -0.1113 -0.1167 -0.0302 17  ASP D CB  
12844 C CG  . ASP D 17  ? 0.5818 0.3558 0.6653 -0.1045 -0.1131 -0.0373 17  ASP D CG  
12845 O OD1 . ASP D 17  ? 0.5961 0.3689 0.6709 -0.1060 -0.1170 -0.0394 17  ASP D OD1 
12846 O OD2 . ASP D 17  ? 0.5978 0.3591 0.6743 -0.0973 -0.1062 -0.0404 17  ASP D OD2 
12847 N N   . GLY D 18  ? 0.5797 0.4390 0.7341 -0.1179 -0.1236 -0.0140 18  GLY D N   
12848 C CA  . GLY D 18  ? 0.5604 0.4402 0.7342 -0.1242 -0.1272 -0.0068 18  GLY D CA  
12849 C C   . GLY D 18  ? 0.5464 0.4411 0.7371 -0.1188 -0.1197 -0.0027 18  GLY D C   
12850 O O   . GLY D 18  ? 0.5190 0.4336 0.7270 -0.1217 -0.1210 0.0034  18  GLY D O   
12851 N N   . GLU D 19  ? 0.5485 0.4337 0.7342 -0.1113 -0.1120 -0.0058 19  GLU D N   
12852 C CA  . GLU D 19  ? 0.5290 0.4254 0.7281 -0.1069 -0.1052 -0.0023 19  GLU D CA  
12853 C C   . GLU D 19  ? 0.4696 0.3773 0.6746 -0.0961 -0.0982 -0.0030 19  GLU D C   
12854 O O   . GLU D 19  ? 0.4821 0.3803 0.6762 -0.0899 -0.0954 -0.0078 19  GLU D O   
12855 C CB  . GLU D 19  ? 0.5860 0.4645 0.7759 -0.1056 -0.1015 -0.0047 19  GLU D CB  
12856 C CG  . GLU D 19  ? 0.6605 0.5252 0.8439 -0.1163 -0.1078 -0.0039 19  GLU D CG  
12857 C CD  . GLU D 19  ? 0.6768 0.5590 0.8763 -0.1252 -0.1123 0.0032  19  GLU D CD  
12858 O OE1 . GLU D 19  ? 0.7130 0.6106 0.9270 -0.1228 -0.1075 0.0079  19  GLU D OE1 
12859 O OE2 . GLU D 19  ? 0.8092 0.6913 1.0071 -0.1341 -0.1204 0.0042  19  GLU D OE2 
12860 N N   . LYS D 20  ? 0.4174 0.3443 0.6388 -0.0938 -0.0948 0.0018  20  LYS D N   
12861 C CA  . LYS D 20  ? 0.4082 0.3447 0.6350 -0.0841 -0.0880 0.0013  20  LYS D CA  
12862 C C   . LYS D 20  ? 0.4088 0.3324 0.6268 -0.0775 -0.0819 -0.0027 20  LYS D C   
12863 O O   . LYS D 20  ? 0.4216 0.3385 0.6386 -0.0789 -0.0802 -0.0020 20  LYS D O   
12864 C CB  . LYS D 20  ? 0.4139 0.3709 0.6583 -0.0825 -0.0848 0.0068  20  LYS D CB  
12865 C CG  . LYS D 20  ? 0.4516 0.4248 0.7063 -0.0850 -0.0891 0.0105  20  LYS D CG  
12866 C CD  . LYS D 20  ? 0.4532 0.4474 0.7256 -0.0835 -0.0861 0.0163  20  LYS D CD  
12867 C CE  . LYS D 20  ? 0.4844 0.4925 0.7660 -0.0875 -0.0919 0.0203  20  LYS D CE  
12868 N NZ  . LYS D 20  ? 0.4924 0.5205 0.7916 -0.0877 -0.0897 0.0267  20  LYS D NZ  
12869 N N   . TYR D 21  ? 0.3726 0.2938 0.5851 -0.0702 -0.0784 -0.0063 21  TYR D N   
12870 C CA  . TYR D 21  ? 0.3588 0.2686 0.5630 -0.0638 -0.0730 -0.0100 21  TYR D CA  
12871 C C   . TYR D 21  ? 0.3499 0.2707 0.5607 -0.0558 -0.0671 -0.0099 21  TYR D C   
12872 O O   . TYR D 21  ? 0.3355 0.2599 0.5451 -0.0527 -0.0669 -0.0113 21  TYR D O   
12873 C CB  . TYR D 21  ? 0.3710 0.2645 0.5592 -0.0639 -0.0753 -0.0150 21  TYR D CB  
12874 C CG  . TYR D 21  ? 0.3685 0.2483 0.5469 -0.0576 -0.0700 -0.0189 21  TYR D CG  
12875 C CD1 . TYR D 21  ? 0.3755 0.2412 0.5475 -0.0595 -0.0701 -0.0196 21  TYR D CD1 
12876 C CD2 . TYR D 21  ? 0.3422 0.2231 0.5179 -0.0499 -0.0652 -0.0214 21  TYR D CD2 
12877 C CE1 . TYR D 21  ? 0.3942 0.2481 0.5582 -0.0530 -0.0651 -0.0227 21  TYR D CE1 
12878 C CE2 . TYR D 21  ? 0.3507 0.2210 0.5191 -0.0439 -0.0602 -0.0242 21  TYR D CE2 
12879 C CZ  . TYR D 21  ? 0.3761 0.2333 0.5389 -0.0451 -0.0601 -0.0248 21  TYR D CZ  
12880 O OH  . TYR D 21  ? 0.4015 0.2483 0.5575 -0.0386 -0.0552 -0.0273 21  TYR D OH  
12881 N N   . PHE D 22  ? 0.3280 0.2538 0.5456 -0.0530 -0.0627 -0.0079 22  PHE D N   
12882 C CA  . PHE D 22  ? 0.3347 0.2684 0.5568 -0.0457 -0.0573 -0.0081 22  PHE D CA  
12883 C C   . PHE D 22  ? 0.3392 0.2611 0.5511 -0.0403 -0.0541 -0.0123 22  PHE D C   
12884 O O   . PHE D 22  ? 0.3503 0.2617 0.5568 -0.0399 -0.0530 -0.0132 22  PHE D O   
12885 C CB  . PHE D 22  ? 0.3164 0.2588 0.5480 -0.0454 -0.0543 -0.0045 22  PHE D CB  
12886 C CG  . PHE D 22  ? 0.2994 0.2515 0.5363 -0.0391 -0.0496 -0.0044 22  PHE D CG  
12887 C CD1 . PHE D 22  ? 0.2877 0.2345 0.5195 -0.0334 -0.0460 -0.0071 22  PHE D CD1 
12888 C CD2 . PHE D 22  ? 0.3143 0.2804 0.5607 -0.0387 -0.0490 -0.0018 22  PHE D CD2 
12889 C CE1 . PHE D 22  ? 0.2801 0.2350 0.5161 -0.0286 -0.0425 -0.0072 22  PHE D CE1 
12890 C CE2 . PHE D 22  ? 0.2726 0.2454 0.5221 -0.0332 -0.0450 -0.0022 22  PHE D CE2 
12891 C CZ  . PHE D 22  ? 0.2789 0.2459 0.5231 -0.0286 -0.0421 -0.0049 22  PHE D CZ  
12892 N N   . ILE D 23  ? 0.3246 0.2484 0.5341 -0.0362 -0.0526 -0.0145 23  ILE D N   
12893 C CA  . ILE D 23  ? 0.3290 0.2434 0.5299 -0.0310 -0.0492 -0.0179 23  ILE D CA  
12894 C C   . ILE D 23  ? 0.3513 0.2707 0.5575 -0.0258 -0.0441 -0.0170 23  ILE D C   
12895 O O   . ILE D 23  ? 0.3667 0.2972 0.5801 -0.0233 -0.0421 -0.0158 23  ILE D O   
12896 C CB  . ILE D 23  ? 0.3371 0.2520 0.5333 -0.0290 -0.0493 -0.0201 23  ILE D CB  
12897 C CG1 . ILE D 23  ? 0.3431 0.2546 0.5343 -0.0344 -0.0550 -0.0205 23  ILE D CG1 
12898 C CG2 . ILE D 23  ? 0.3723 0.2779 0.5595 -0.0238 -0.0454 -0.0234 23  ILE D CG2 
12899 C CD1 . ILE D 23  ? 0.3321 0.2464 0.5201 -0.0326 -0.0555 -0.0216 23  ILE D CD1 
12900 N N   . LYS D 24  ? 0.3418 0.2522 0.5438 -0.0239 -0.0422 -0.0177 24  LYS D N   
12901 C CA  . LYS D 24  ? 0.3389 0.2530 0.5451 -0.0190 -0.0380 -0.0166 24  LYS D CA  
12902 C C   . LYS D 24  ? 0.3332 0.2413 0.5333 -0.0133 -0.0347 -0.0193 24  LYS D C   
12903 O O   . LYS D 24  ? 0.3726 0.2709 0.5675 -0.0110 -0.0332 -0.0201 24  LYS D O   
12904 C CB  . LYS D 24  ? 0.3430 0.2528 0.5503 -0.0207 -0.0383 -0.0144 24  LYS D CB  
12905 C CG  . LYS D 24  ? 0.3584 0.2760 0.5730 -0.0260 -0.0406 -0.0109 24  LYS D CG  
12906 C CD  . LYS D 24  ? 0.3682 0.2831 0.5845 -0.0273 -0.0401 -0.0080 24  LYS D CD  
12907 C CE  . LYS D 24  ? 0.3965 0.2977 0.6059 -0.0316 -0.0431 -0.0083 24  LYS D CE  
12908 N NZ  . LYS D 24  ? 0.3941 0.2910 0.6039 -0.0312 -0.0418 -0.0055 24  LYS D NZ  
12909 N N   . ALA D 25  ? 0.3402 0.2541 0.5409 -0.0110 -0.0332 -0.0204 25  ALA D N   
12910 C CA  . ALA D 25  ? 0.3271 0.2366 0.5223 -0.0060 -0.0298 -0.0227 25  ALA D CA  
12911 C C   . ALA D 25  ? 0.3133 0.2306 0.5151 -0.0013 -0.0259 -0.0211 25  ALA D C   
12912 O O   . ALA D 25  ? 0.3403 0.2661 0.5499 -0.0020 -0.0261 -0.0187 25  ALA D O   
12913 C CB  . ALA D 25  ? 0.3067 0.2178 0.4984 -0.0064 -0.0302 -0.0243 25  ALA D CB  
12914 N N   . ILE D 26  ? 0.2999 0.2140 0.4980 0.0035  -0.0224 -0.0224 26  ILE D N   
12915 C CA  . ILE D 26  ? 0.2800 0.2035 0.4847 0.0074  -0.0191 -0.0209 26  ILE D CA  
12916 C C   . ILE D 26  ? 0.2772 0.1999 0.4775 0.0102  -0.0163 -0.0227 26  ILE D C   
12917 O O   . ILE D 26  ? 0.2697 0.1821 0.4608 0.0113  -0.0155 -0.0251 26  ILE D O   
12918 C CB  . ILE D 26  ? 0.2844 0.2072 0.4920 0.0111  -0.0173 -0.0191 26  ILE D CB  
12919 C CG1 . ILE D 26  ? 0.2681 0.2022 0.4835 0.0141  -0.0149 -0.0171 26  ILE D CG1 
12920 C CG2 . ILE D 26  ? 0.2940 0.2042 0.4935 0.0148  -0.0151 -0.0209 26  ILE D CG2 
12921 C CD1 . ILE D 26  ? 0.2684 0.2034 0.4876 0.0174  -0.0139 -0.0146 26  ILE D CD1 
12922 N N   . GLY D 27  ? 0.2748 0.2075 0.4806 0.0106  -0.0150 -0.0216 27  GLY D N   
12923 C CA  . GLY D 27  ? 0.2857 0.2193 0.4886 0.0134  -0.0116 -0.0224 27  GLY D CA  
12924 C C   . GLY D 27  ? 0.3091 0.2397 0.5109 0.0190  -0.0074 -0.0223 27  GLY D C   
12925 O O   . GLY D 27  ? 0.3301 0.2630 0.5371 0.0209  -0.0071 -0.0205 27  GLY D O   
12926 N N   . TYR D 28  ? 0.3174 0.2422 0.5116 0.0220  -0.0042 -0.0241 28  TYR D N   
12927 C CA  . TYR D 28  ? 0.3376 0.2577 0.5292 0.0280  0.0002  -0.0243 28  TYR D CA  
12928 C C   . TYR D 28  ? 0.3530 0.2732 0.5398 0.0313  0.0050  -0.0252 28  TYR D C   
12929 O O   . TYR D 28  ? 0.3817 0.2943 0.5584 0.0297  0.0047  -0.0279 28  TYR D O   
12930 C CB  . TYR D 28  ? 0.3489 0.2536 0.5309 0.0282  -0.0011 -0.0269 28  TYR D CB  
12931 C CG  . TYR D 28  ? 0.3599 0.2571 0.5369 0.0354  0.0041  -0.0277 28  TYR D CG  
12932 C CD1 . TYR D 28  ? 0.3480 0.2527 0.5340 0.0406  0.0072  -0.0246 28  TYR D CD1 
12933 C CD2 . TYR D 28  ? 0.3829 0.2659 0.5460 0.0372  0.0060  -0.0314 28  TYR D CD2 
12934 C CE1 . TYR D 28  ? 0.3366 0.2352 0.5189 0.0481  0.0124  -0.0250 28  TYR D CE1 
12935 C CE2 . TYR D 28  ? 0.3829 0.2584 0.5408 0.0446  0.0115  -0.0323 28  TYR D CE2 
12936 C CZ  . TYR D 28  ? 0.3533 0.2372 0.5215 0.0504  0.0149  -0.0289 28  TYR D CZ  
12937 O OH  . TYR D 28  ? 0.3553 0.2325 0.5192 0.0584  0.0207  -0.0295 28  TYR D OH  
12938 N N   . GLU D 29  ? 0.3718 0.3008 0.5656 0.0359  0.0096  -0.0228 29  GLU D N   
12939 C CA  . GLU D 29  ? 0.3515 0.2828 0.5420 0.0389  0.0147  -0.0229 29  GLU D CA  
12940 C C   . GLU D 29  ? 0.3373 0.2680 0.5287 0.0467  0.0206  -0.0221 29  GLU D C   
12941 O O   . GLU D 29  ? 0.3524 0.2949 0.5554 0.0492  0.0224  -0.0184 29  GLU D O   
12942 C CB  . GLU D 29  ? 0.3385 0.2845 0.5387 0.0362  0.0148  -0.0199 29  GLU D CB  
12943 C CG  . GLU D 29  ? 0.3349 0.2854 0.5337 0.0392  0.0207  -0.0189 29  GLU D CG  
12944 C CD  . GLU D 29  ? 0.3344 0.2975 0.5414 0.0352  0.0201  -0.0159 29  GLU D CD  
12945 O OE1 . GLU D 29  ? 0.2922 0.2667 0.5114 0.0346  0.0194  -0.0127 29  GLU D OE1 
12946 O OE2 . GLU D 29  ? 0.3042 0.2647 0.5045 0.0326  0.0202  -0.0169 29  GLU D OE2 
12947 N N   . ILE D 30  ? 0.3512 0.2681 0.5299 0.0505  0.0237  -0.0254 30  ILE D N   
12948 C CA  . ILE D 30  ? 0.3561 0.2715 0.5337 0.0589  0.0307  -0.0249 30  ILE D CA  
12949 C C   . ILE D 30  ? 0.3501 0.2776 0.5321 0.0613  0.0363  -0.0226 30  ILE D C   
12950 O O   . ILE D 30  ? 0.3544 0.2860 0.5351 0.0564  0.0351  -0.0226 30  ILE D O   
12951 C CB  . ILE D 30  ? 0.3700 0.2651 0.5304 0.0618  0.0322  -0.0297 30  ILE D CB  
12952 C CG1 . ILE D 30  ? 0.4016 0.2923 0.5605 0.0717  0.0393  -0.0294 30  ILE D CG1 
12953 C CG2 . ILE D 30  ? 0.3728 0.2609 0.5199 0.0588  0.0326  -0.0330 30  ILE D CG2 
12954 C CD1 . ILE D 30  ? 0.3861 0.2806 0.5559 0.0751  0.0383  -0.0263 30  ILE D CD1 
12955 N N   . GLY D 31  ? 0.3557 0.2896 0.5439 0.0687  0.0426  -0.0200 31  GLY D N   
12956 C CA  . GLY D 31  ? 0.3624 0.3082 0.5552 0.0716  0.0489  -0.0173 31  GLY D CA  
12957 C C   . GLY D 31  ? 0.3522 0.3181 0.5622 0.0676  0.0468  -0.0121 31  GLY D C   
12958 O O   . GLY D 31  ? 0.3564 0.3326 0.5703 0.0669  0.0504  -0.0096 31  GLY D O   
12959 N N   . ALA D 32  ? 0.3282 0.2987 0.5477 0.0649  0.0411  -0.0103 32  ALA D N   
12960 C CA  . ALA D 32  ? 0.3170 0.3037 0.5505 0.0598  0.0376  -0.0062 32  ALA D CA  
12961 C C   . ALA D 32  ? 0.3062 0.3026 0.5526 0.0630  0.0368  -0.0022 32  ALA D C   
12962 O O   . ALA D 32  ? 0.2964 0.3017 0.5519 0.0580  0.0316  0.0001  32  ALA D O   
12963 C CB  . ALA D 32  ? 0.3101 0.2930 0.5407 0.0514  0.0304  -0.0082 32  ALA D CB  
12964 N N   . ARG D 33  ? 0.3282 0.3230 0.5751 0.0716  0.0419  -0.0013 33  ARG D N   
12965 C CA  . ARG D 33  ? 0.3252 0.3306 0.5851 0.0756  0.0416  0.0033  33  ARG D CA  
12966 C C   . ARG D 33  ? 0.3372 0.3636 0.6121 0.0738  0.0425  0.0088  33  ARG D C   
12967 O O   . ARG D 33  ? 0.3532 0.3848 0.6277 0.0715  0.0455  0.0091  33  ARG D O   
12968 C CB  . ARG D 33  ? 0.3409 0.3408 0.5987 0.0864  0.0480  0.0037  33  ARG D CB  
12969 C CG  . ARG D 33  ? 0.3518 0.3369 0.6033 0.0886  0.0448  0.0016  33  ARG D CG  
12970 C CD  . ARG D 33  ? 0.3366 0.3046 0.5735 0.0819  0.0401  -0.0042 33  ARG D CD  
12971 N NE  . ARG D 33  ? 0.3499 0.3038 0.5811 0.0846  0.0380  -0.0057 33  ARG D NE  
12972 C CZ  . ARG D 33  ? 0.3360 0.2738 0.5557 0.0804  0.0339  -0.0098 33  ARG D CZ  
12973 N NH1 . ARG D 33  ? 0.3174 0.2518 0.5305 0.0730  0.0308  -0.0130 33  ARG D NH1 
12974 N NH2 . ARG D 33  ? 0.3328 0.2585 0.5483 0.0835  0.0327  -0.0103 33  ARG D NH2 
12975 N N   . PRO D 34  ? 0.3253 0.3646 0.6138 0.0747  0.0399  0.0137  34  PRO D N   
12976 C CA  . PRO D 34  ? 0.3514 0.4114 0.6550 0.0738  0.0413  0.0196  34  PRO D CA  
12977 C C   . PRO D 34  ? 0.3925 0.4570 0.6966 0.0803  0.0504  0.0208  34  PRO D C   
12978 O O   . PRO D 34  ? 0.3924 0.4501 0.6924 0.0893  0.0559  0.0200  34  PRO D O   
12979 C CB  . PRO D 34  ? 0.3417 0.4105 0.6569 0.0771  0.0382  0.0241  34  PRO D CB  
12980 C CG  . PRO D 34  ? 0.3226 0.3768 0.6289 0.0741  0.0321  0.0204  34  PRO D CG  
12981 C CD  . PRO D 34  ? 0.3087 0.3436 0.5987 0.0757  0.0351  0.0142  34  PRO D CD  
12982 N N   . GLY D 35  ? 0.4019 0.4770 0.7102 0.0757  0.0523  0.0228  35  GLY D N   
12983 C CA  . GLY D 35  ? 0.4155 0.4962 0.7244 0.0814  0.0614  0.0245  35  GLY D CA  
12984 C C   . GLY D 35  ? 0.4189 0.4832 0.7099 0.0817  0.0654  0.0188  35  GLY D C   
12985 O O   . GLY D 35  ? 0.4545 0.5225 0.7441 0.0861  0.0733  0.0199  35  GLY D O   
12986 N N   . GLN D 36  ? 0.3879 0.4352 0.6656 0.0771  0.0602  0.0131  36  GLN D N   
12987 C CA  . GLN D 36  ? 0.3884 0.4199 0.6486 0.0769  0.0629  0.0078  36  GLN D CA  
12988 C C   . GLN D 36  ? 0.3884 0.4192 0.6452 0.0670  0.0578  0.0066  36  GLN D C   
12989 O O   . GLN D 36  ? 0.4117 0.4460 0.6743 0.0604  0.0506  0.0073  36  GLN D O   
12990 C CB  . GLN D 36  ? 0.3965 0.4069 0.6418 0.0795  0.0610  0.0019  36  GLN D CB  
12991 C CG  . GLN D 36  ? 0.4126 0.4185 0.6583 0.0894  0.0651  0.0021  36  GLN D CG  
12992 C CD  . GLN D 36  ? 0.4297 0.4125 0.6583 0.0916  0.0639  -0.0040 36  GLN D CD  
12993 O OE1 . GLN D 36  ? 0.3862 0.3600 0.6107 0.0861  0.0567  -0.0066 36  GLN D OE1 
12994 N NE2 . GLN D 36  ? 0.4519 0.4248 0.6704 0.0998  0.0713  -0.0063 36  GLN D NE2 
12995 N N   . ALA D 37  ? 0.3939 0.4178 0.6391 0.0663  0.0616  0.0043  37  ALA D N   
12996 C CA  . ALA D 37  ? 0.4081 0.4279 0.6472 0.0578  0.0569  0.0027  37  ALA D CA  
12997 C C   . ALA D 37  ? 0.4288 0.4305 0.6487 0.0587  0.0579  -0.0028 37  ALA D C   
12998 O O   . ALA D 37  ? 0.4593 0.4587 0.6713 0.0621  0.0646  -0.0031 37  ALA D O   
12999 C CB  . ALA D 37  ? 0.3981 0.4324 0.6454 0.0542  0.0596  0.0074  37  ALA D CB  
13000 N N   . PRO D 38  ? 0.4194 0.4080 0.6308 0.0550  0.0514  -0.0071 38  PRO D N   
13001 C CA  . PRO D 38  ? 0.4609 0.4321 0.6539 0.0559  0.0518  -0.0122 38  PRO D CA  
13002 C C   . PRO D 38  ? 0.4929 0.4613 0.6758 0.0528  0.0537  -0.0127 38  PRO D C   
13003 O O   . PRO D 38  ? 0.5645 0.5194 0.7316 0.0548  0.0556  -0.0165 38  PRO D O   
13004 C CB  . PRO D 38  ? 0.4375 0.3997 0.6280 0.0513  0.0434  -0.0152 38  PRO D CB  
13005 C CG  . PRO D 38  ? 0.4114 0.3868 0.6163 0.0457  0.0386  -0.0116 38  PRO D CG  
13006 C CD  . PRO D 38  ? 0.3909 0.3812 0.6094 0.0498  0.0434  -0.0070 38  PRO D CD  
13007 N N   . TYR D 39  ? 0.5035 0.4831 0.6940 0.0478  0.0529  -0.0090 39  TYR D N   
13008 C CA  . TYR D 39  ? 0.5164 0.4923 0.6969 0.0442  0.0536  -0.0092 39  TYR D CA  
13009 C C   . TYR D 39  ? 0.5367 0.5224 0.7197 0.0471  0.0620  -0.0053 39  TYR D C   
13010 O O   . TYR D 39  ? 0.5171 0.4987 0.6897 0.0457  0.0645  -0.0053 39  TYR D O   
13011 C CB  . TYR D 39  ? 0.4940 0.4717 0.6774 0.0360  0.0465  -0.0081 39  TYR D CB  
13012 C CG  . TYR D 39  ? 0.4916 0.4597 0.6714 0.0330  0.0386  -0.0118 39  TYR D CG  
13013 C CD1 . TYR D 39  ? 0.5158 0.4693 0.6805 0.0331  0.0365  -0.0161 39  TYR D CD1 
13014 C CD2 . TYR D 39  ? 0.4858 0.4596 0.6772 0.0300  0.0333  -0.0108 39  TYR D CD2 
13015 C CE1 . TYR D 39  ? 0.4819 0.4280 0.6447 0.0302  0.0294  -0.0189 39  TYR D CE1 
13016 C CE2 . TYR D 39  ? 0.4775 0.4436 0.6663 0.0276  0.0268  -0.0137 39  TYR D CE2 
13017 C CZ  . TYR D 39  ? 0.4409 0.3937 0.6161 0.0276  0.0249  -0.0176 39  TYR D CZ  
13018 O OH  . TYR D 39  ? 0.4323 0.3797 0.6070 0.0247  0.0185  -0.0197 39  TYR D OH  
13019 N N   . GLU D 40  ? 0.6094 0.6086 0.8062 0.0509  0.0666  -0.0015 40  GLU D N   
13020 C CA  . GLU D 40  ? 0.6429 0.6519 0.8421 0.0546  0.0756  0.0024  40  GLU D CA  
13021 C C   . GLU D 40  ? 0.6366 0.6414 0.8308 0.0647  0.0832  0.0006  40  GLU D C   
13022 O O   . GLU D 40  ? 0.6261 0.6300 0.8124 0.0691  0.0913  0.0011  40  GLU D O   
13023 C CB  . GLU D 40  ? 0.6598 0.6879 0.8770 0.0499  0.0753  0.0089  40  GLU D CB  
13024 C CG  . GLU D 40  ? 0.7630 0.8025 0.9974 0.0504  0.0721  0.0114  40  GLU D CG  
13025 C CD  . GLU D 40  ? 0.8370 0.8966 1.0900 0.0464  0.0722  0.0182  40  GLU D CD  
13026 O OE1 . GLU D 40  ? 0.8225 0.8840 1.0788 0.0380  0.0661  0.0193  40  GLU D OE1 
13027 O OE2 . GLU D 40  ? 0.7816 0.8549 1.0460 0.0515  0.0780  0.0224  40  GLU D OE2 
13028 N N   . ASP D 41  ? 0.5839 0.5846 0.7812 0.0689  0.0811  -0.0015 41  ASP D N   
13029 C CA  . ASP D 41  ? 0.5940 0.5902 0.7871 0.0791  0.0886  -0.0029 41  ASP D CA  
13030 C C   . ASP D 41  ? 0.6245 0.5990 0.7944 0.0815  0.0900  -0.0094 41  ASP D C   
13031 O O   . ASP D 41  ? 0.7746 0.7375 0.9349 0.0754  0.0828  -0.0130 41  ASP D O   
13032 C CB  . ASP D 41  ? 0.5974 0.5925 0.7983 0.0828  0.0854  -0.0035 41  ASP D CB  
13033 C CG  . ASP D 41  ? 0.5494 0.5644 0.7725 0.0823  0.0839  0.0025  41  ASP D CG  
13034 O OD1 . ASP D 41  ? 0.5200 0.5516 0.7543 0.0801  0.0866  0.0078  41  ASP D OD1 
13035 O OD2 . ASP D 41  ? 0.5590 0.5723 0.7877 0.0834  0.0793  0.0020  41  ASP D OD2 
13036 N N   . GLU D 42  ? 0.6798 0.6484 0.8406 0.0905  0.0990  -0.0108 42  GLU D N   
13037 C CA  . GLU D 42  ? 0.7756 0.7216 0.9129 0.0934  0.1004  -0.0175 42  GLU D CA  
13038 C C   . GLU D 42  ? 0.8094 0.7408 0.9422 0.0920  0.0924  -0.0221 42  GLU D C   
13039 O O   . GLU D 42  ? 0.7934 0.7300 0.9388 0.0947  0.0908  -0.0205 42  GLU D O   
13040 C CB  . GLU D 42  ? 0.8194 0.7616 0.9482 0.1044  0.1122  -0.0182 42  GLU D CB  
13041 C CG  . GLU D 42  ? 0.8336 0.7752 0.9691 0.1141  0.1162  -0.0181 42  GLU D CG  
13042 C CD  . GLU D 42  ? 0.8955 0.8604 1.0573 0.1155  0.1165  -0.0111 42  GLU D CD  
13043 O OE1 . GLU D 42  ? 0.8789 0.8627 1.0548 0.1099  0.1157  -0.0056 42  GLU D OE1 
13044 O OE2 . GLU D 42  ? 0.9609 0.9244 1.1288 0.1219  0.1170  -0.0110 42  GLU D OE2 
13045 N N   . ARG D 43  ? 0.8530 0.7660 0.9674 0.0877  0.0873  -0.0276 43  ARG D N   
13046 C CA  . ARG D 43  ? 0.9476 0.8464 1.0571 0.0855  0.0797  -0.0318 43  ARG D CA  
13047 C C   . ARG D 43  ? 0.8877 0.7722 0.9878 0.0946  0.0848  -0.0353 43  ARG D C   
13048 O O   . ARG D 43  ? 0.7753 0.6496 0.8605 0.1009  0.0923  -0.0380 43  ARG D O   
13049 C CB  . ARG D 43  ? 0.9697 0.8553 1.0654 0.0770  0.0712  -0.0359 43  ARG D CB  
13050 C CG  . ARG D 43  ? 1.0213 0.8892 1.0929 0.0779  0.0736  -0.0408 43  ARG D CG  
13051 C CD  . ARG D 43  ? 1.1506 1.0144 1.2153 0.0682  0.0648  -0.0421 43  ARG D CD  
13052 N NE  . ARG D 43  ? 1.2613 1.1141 1.3055 0.0675  0.0670  -0.0448 43  ARG D NE  
13053 C CZ  . ARG D 43  ? 1.2098 1.0587 1.2454 0.0600  0.0605  -0.0456 43  ARG D CZ  
13054 N NH1 . ARG D 43  ? 1.0240 0.8795 1.0703 0.0525  0.0515  -0.0437 43  ARG D NH1 
13055 N NH2 . ARG D 43  ? 1.2419 1.0797 1.2574 0.0606  0.0632  -0.0481 43  ARG D NH2 
13056 N N   . LYS D 44  ? 0.8269 0.7107 0.9361 0.0951  0.0803  -0.0350 44  LYS D N   
13057 C CA  . LYS D 44  ? 0.7665 0.6390 0.8719 0.1034  0.0838  -0.0370 44  LYS D CA  
13058 C C   . LYS D 44  ? 0.6868 0.5447 0.7868 0.0980  0.0746  -0.0405 44  LYS D C   
13059 O O   . LYS D 44  ? 0.6479 0.5137 0.7578 0.0899  0.0666  -0.0387 44  LYS D O   
13060 C CB  . LYS D 44  ? 0.8193 0.7111 0.9466 0.1092  0.0876  -0.0308 44  LYS D CB  
13061 C CG  . LYS D 44  ? 0.9350 0.8408 1.0686 0.1167  0.0982  -0.0269 44  LYS D CG  
13062 C CD  . LYS D 44  ? 1.0129 0.9341 1.1658 0.1244  0.1024  -0.0214 44  LYS D CD  
13063 C CE  . LYS D 44  ? 1.0345 0.9409 1.1814 0.1339  0.1053  -0.0237 44  LYS D CE  
13064 N NZ  . LYS D 44  ? 1.0414 0.9361 1.1734 0.1440  0.1158  -0.0267 44  LYS D NZ  
13065 N N   . ASP D 45  ? 0.6396 0.4756 0.7231 0.1020  0.0756  -0.0456 45  ASP D N   
13066 C CA  . ASP D 45  ? 0.6001 0.4217 0.6779 0.0961  0.0668  -0.0487 45  ASP D CA  
13067 C C   . ASP D 45  ? 0.5623 0.3948 0.6592 0.0958  0.0630  -0.0443 45  ASP D C   
13068 O O   . ASP D 45  ? 0.5187 0.3522 0.6203 0.0876  0.0543  -0.0440 45  ASP D O   
13069 C CB  . ASP D 45  ? 0.6233 0.4182 0.6784 0.0999  0.0687  -0.0550 45  ASP D CB  
13070 C CG  . ASP D 45  ? 0.6321 0.4135 0.6658 0.0961  0.0683  -0.0600 45  ASP D CG  
13071 O OD1 . ASP D 45  ? 0.5997 0.3914 0.6365 0.0887  0.0642  -0.0586 45  ASP D OD1 
13072 O OD2 . ASP D 45  ? 0.6881 0.4481 0.7018 0.1008  0.0720  -0.0652 45  ASP D OD2 
13073 N N   . GLU D 46  ? 0.5307 0.3722 0.6387 0.1050  0.0695  -0.0407 46  GLU D N   
13074 C CA  . GLU D 46  ? 0.5175 0.3696 0.6431 0.1058  0.0664  -0.0361 46  GLU D CA  
13075 C C   . GLU D 46  ? 0.4964 0.3301 0.6141 0.1031  0.0602  -0.0391 46  GLU D C   
13076 O O   . GLU D 46  ? 0.5079 0.3474 0.6355 0.0971  0.0532  -0.0368 46  GLU D O   
13077 C CB  . GLU D 46  ? 0.5170 0.3906 0.6596 0.0978  0.0611  -0.0317 46  GLU D CB  
13078 C CG  . GLU D 46  ? 0.5408 0.4339 0.6936 0.0999  0.0669  -0.0278 46  GLU D CG  
13079 C CD  . GLU D 46  ? 0.5718 0.4807 0.7417 0.1075  0.0715  -0.0221 46  GLU D CD  
13080 O OE1 . GLU D 46  ? 0.6898 0.5912 0.8578 0.1164  0.0759  -0.0221 46  GLU D OE1 
13081 O OE2 . GLU D 46  ? 0.6244 0.5534 0.8099 0.1042  0.0704  -0.0173 46  GLU D OE2 
13082 N N   . LEU D 47  ? 0.5015 0.3121 0.6002 0.1070  0.0627  -0.0443 47  LEU D N   
13083 C CA  . LEU D 47  ? 0.5007 0.2917 0.5896 0.1031  0.0564  -0.0475 47  LEU D CA  
13084 C C   . LEU D 47  ? 0.4983 0.2943 0.6011 0.1062  0.0548  -0.0430 47  LEU D C   
13085 O O   . LEU D 47  ? 0.5042 0.2989 0.6107 0.0988  0.0471  -0.0423 47  LEU D O   
13086 C CB  . LEU D 47  ? 0.5195 0.2837 0.5847 0.1075  0.0602  -0.0538 47  LEU D CB  
13087 C CG  . LEU D 47  ? 0.5281 0.2849 0.5767 0.1032  0.0603  -0.0586 47  LEU D CG  
13088 C CD1 . LEU D 47  ? 0.5534 0.2819 0.5769 0.1076  0.0638  -0.0652 47  LEU D CD1 
13089 C CD2 . LEU D 47  ? 0.5109 0.2707 0.5603 0.0899  0.0500  -0.0591 47  LEU D CD2 
13090 N N   . GLU D 48  ? 0.5195 0.3227 0.6310 0.1168  0.0618  -0.0396 48  GLU D N   
13091 C CA  . GLU D 48  ? 0.5495 0.3544 0.6717 0.1204  0.0601  -0.0355 48  GLU D CA  
13092 C C   . GLU D 48  ? 0.4976 0.3215 0.6372 0.1120  0.0527  -0.0308 48  GLU D C   
13093 O O   . GLU D 48  ? 0.4890 0.3083 0.6313 0.1087  0.0471  -0.0294 48  GLU D O   
13094 C CB  . GLU D 48  ? 0.5950 0.4068 0.7253 0.1337  0.0688  -0.0318 48  GLU D CB  
13095 C CG  . GLU D 48  ? 0.6959 0.4842 0.8081 0.1435  0.0760  -0.0364 48  GLU D CG  
13096 C CD  . GLU D 48  ? 0.7919 0.5511 0.8857 0.1401  0.0712  -0.0416 48  GLU D CD  
13097 O OE1 . GLU D 48  ? 0.7666 0.5228 0.8664 0.1384  0.0659  -0.0389 48  GLU D OE1 
13098 O OE2 . GLU D 48  ? 0.7924 0.5319 0.8655 0.1385  0.0722  -0.0482 48  GLU D OE2 
13099 N N   . LEU D 49  ? 0.4840 0.3291 0.6351 0.1088  0.0529  -0.0281 49  LEU D N   
13100 C CA  . LEU D 49  ? 0.4641 0.3271 0.6309 0.1014  0.0465  -0.0239 49  LEU D CA  
13101 C C   . LEU D 49  ? 0.4758 0.3311 0.6355 0.0901  0.0385  -0.0270 49  LEU D C   
13102 O O   . LEU D 49  ? 0.4727 0.3357 0.6416 0.0844  0.0326  -0.0244 49  LEU D O   
13103 C CB  . LEU D 49  ? 0.4418 0.3276 0.6215 0.1013  0.0494  -0.0204 49  LEU D CB  
13104 C CG  . LEU D 49  ? 0.4350 0.3353 0.6279 0.1109  0.0557  -0.0152 49  LEU D CG  
13105 C CD1 . LEU D 49  ? 0.4133 0.3351 0.6174 0.1086  0.0579  -0.0121 49  LEU D CD1 
13106 C CD2 . LEU D 49  ? 0.4032 0.3104 0.6087 0.1125  0.0521  -0.0103 49  LEU D CD2 
13107 N N   . MET D 50  ? 0.4861 0.3276 0.6301 0.0870  0.0385  -0.0324 50  MET D N   
13108 C CA  . MET D 50  ? 0.4882 0.3220 0.6252 0.0767  0.0309  -0.0352 50  MET D CA  
13109 C C   . MET D 50  ? 0.4577 0.2759 0.5897 0.0753  0.0268  -0.0359 50  MET D C   
13110 O O   . MET D 50  ? 0.4246 0.2445 0.5602 0.0674  0.0201  -0.0350 50  MET D O   
13111 C CB  . MET D 50  ? 0.5106 0.3328 0.6312 0.0739  0.0314  -0.0405 50  MET D CB  
13112 C CG  . MET D 50  ? 0.5157 0.3534 0.6411 0.0710  0.0325  -0.0395 50  MET D CG  
13113 S SD  . MET D 50  ? 0.5227 0.3476 0.6291 0.0654  0.0306  -0.0450 50  MET D SD  
13114 C CE  . MET D 50  ? 0.4714 0.2913 0.5776 0.0542  0.0198  -0.0457 50  MET D CE  
13115 N N   . LYS D 51  ? 0.4758 0.2786 0.5992 0.0830  0.0310  -0.0374 51  LYS D N   
13116 C CA  . LYS D 51  ? 0.4964 0.2831 0.6145 0.0819  0.0273  -0.0377 51  LYS D CA  
13117 C C   . LYS D 51  ? 0.4629 0.2646 0.5980 0.0799  0.0237  -0.0319 51  LYS D C   
13118 O O   . LYS D 51  ? 0.4682 0.2664 0.6034 0.0721  0.0172  -0.0315 51  LYS D O   
13119 C CB  . LYS D 51  ? 0.5518 0.3204 0.6598 0.0920  0.0331  -0.0394 51  LYS D CB  
13120 C CG  . LYS D 51  ? 0.6449 0.3932 0.7320 0.0928  0.0357  -0.0460 51  LYS D CG  
13121 C CD  . LYS D 51  ? 0.7301 0.4590 0.8048 0.1040  0.0427  -0.0485 51  LYS D CD  
13122 C CE  . LYS D 51  ? 0.7748 0.4837 0.8272 0.1041  0.0452  -0.0556 51  LYS D CE  
13123 N NZ  . LYS D 51  ? 0.7986 0.4934 0.8408 0.1169  0.0542  -0.0577 51  LYS D NZ  
13124 N N   . PHE D 52  ? 0.4260 0.2451 0.5751 0.0865  0.0277  -0.0274 52  PHE D N   
13125 C CA  . PHE D 52  ? 0.4132 0.2475 0.5781 0.0854  0.0246  -0.0216 52  PHE D CA  
13126 C C   . PHE D 52  ? 0.3962 0.2424 0.5674 0.0748  0.0183  -0.0209 52  PHE D C   
13127 O O   . PHE D 52  ? 0.4112 0.2576 0.5862 0.0698  0.0132  -0.0188 52  PHE D O   
13128 C CB  . PHE D 52  ? 0.4180 0.2690 0.5959 0.0942  0.0300  -0.0171 52  PHE D CB  
13129 C CG  . PHE D 52  ? 0.4040 0.2742 0.5987 0.0922  0.0264  -0.0111 52  PHE D CG  
13130 C CD1 . PHE D 52  ? 0.4020 0.2697 0.6011 0.0955  0.0247  -0.0072 52  PHE D CD1 
13131 C CD2 . PHE D 52  ? 0.4056 0.2954 0.6107 0.0869  0.0246  -0.0094 52  PHE D CD2 
13132 C CE1 . PHE D 52  ? 0.4035 0.2883 0.6166 0.0933  0.0211  -0.0018 52  PHE D CE1 
13133 C CE2 . PHE D 52  ? 0.3875 0.2935 0.6064 0.0848  0.0210  -0.0043 52  PHE D CE2 
13134 C CZ  . PHE D 52  ? 0.4015 0.3053 0.6242 0.0879  0.0192  -0.0005 52  PHE D CZ  
13135 N N   . ASP D 53  ? 0.3854 0.2403 0.5569 0.0713  0.0188  -0.0228 53  ASP D N   
13136 C CA  . ASP D 53  ? 0.3743 0.2413 0.5524 0.0623  0.0136  -0.0219 53  ASP D CA  
13137 C C   . ASP D 53  ? 0.3832 0.2378 0.5527 0.0543  0.0078  -0.0246 53  ASP D C   
13138 O O   . ASP D 53  ? 0.3844 0.2456 0.5604 0.0483  0.0030  -0.0225 53  ASP D O   
13139 C CB  . ASP D 53  ? 0.3627 0.2401 0.5421 0.0609  0.0156  -0.0231 53  ASP D CB  
13140 C CG  . ASP D 53  ? 0.3615 0.2550 0.5516 0.0667  0.0207  -0.0198 53  ASP D CG  
13141 O OD1 . ASP D 53  ? 0.3492 0.2523 0.5504 0.0704  0.0211  -0.0154 53  ASP D OD1 
13142 O OD2 . ASP D 53  ? 0.3668 0.2630 0.5538 0.0677  0.0243  -0.0213 53  ASP D OD2 
13143 N N   . LEU D 54  ? 0.4121 0.2490 0.5668 0.0538  0.0081  -0.0291 54  LEU D N   
13144 C CA  . LEU D 54  ? 0.4385 0.2641 0.5855 0.0456  0.0023  -0.0314 54  LEU D CA  
13145 C C   . LEU D 54  ? 0.4475 0.2662 0.5963 0.0444  -0.0007 -0.0289 54  LEU D C   
13146 O O   . LEU D 54  ? 0.4383 0.2581 0.5892 0.0367  -0.0061 -0.0279 54  LEU D O   
13147 C CB  . LEU D 54  ? 0.4685 0.2758 0.5982 0.0457  0.0033  -0.0368 54  LEU D CB  
13148 C CG  . LEU D 54  ? 0.4801 0.2929 0.6060 0.0449  0.0050  -0.0393 54  LEU D CG  
13149 C CD1 . LEU D 54  ? 0.5012 0.2939 0.6080 0.0443  0.0051  -0.0447 54  LEU D CD1 
13150 C CD2 . LEU D 54  ? 0.4876 0.3146 0.6215 0.0367  -0.0001 -0.0378 54  LEU D CD2 
13151 N N   . GLU D 55  ? 0.4483 0.2607 0.5969 0.0522  0.0029  -0.0273 55  GLU D N   
13152 C CA  . GLU D 55  ? 0.4567 0.2621 0.6067 0.0513  0.0002  -0.0245 55  GLU D CA  
13153 C C   . GLU D 55  ? 0.4387 0.2631 0.6034 0.0473  -0.0029 -0.0196 55  GLU D C   
13154 O O   . GLU D 55  ? 0.4095 0.2320 0.5751 0.0407  -0.0076 -0.0180 55  GLU D O   
13155 C CB  . GLU D 55  ? 0.4634 0.2582 0.6102 0.0613  0.0049  -0.0235 55  GLU D CB  
13156 C CG  . GLU D 55  ? 0.5033 0.2869 0.6489 0.0609  0.0022  -0.0206 55  GLU D CG  
13157 C CD  . GLU D 55  ? 0.5239 0.2944 0.6616 0.0508  -0.0038 -0.0221 55  GLU D CD  
13158 O OE1 . GLU D 55  ? 0.5429 0.3010 0.6687 0.0462  -0.0053 -0.0270 55  GLU D OE1 
13159 O OE2 . GLU D 55  ? 0.4632 0.2367 0.6071 0.0473  -0.0071 -0.0178 55  GLU D OE2 
13160 N N   . ASN D 56  ? 0.4048 0.2475 0.5805 0.0508  -0.0005 -0.0173 56  ASN D N   
13161 C CA  . ASN D 56  ? 0.3517 0.2115 0.5399 0.0475  -0.0032 -0.0131 56  ASN D CA  
13162 C C   . ASN D 56  ? 0.3382 0.2025 0.5269 0.0379  -0.0078 -0.0142 56  ASN D C   
13163 O O   . ASN D 56  ? 0.3087 0.1782 0.5026 0.0335  -0.0112 -0.0114 56  ASN D O   
13164 C CB  . ASN D 56  ? 0.3408 0.2181 0.5394 0.0521  -0.0001 -0.0109 56  ASN D CB  
13165 C CG  . ASN D 56  ? 0.3633 0.2403 0.5650 0.0615  0.0040  -0.0082 56  ASN D CG  
13166 O OD1 . ASN D 56  ? 0.3613 0.2289 0.5609 0.0642  0.0034  -0.0062 56  ASN D OD1 
13167 N ND2 . ASN D 56  ? 0.3646 0.2532 0.5724 0.0666  0.0080  -0.0074 56  ASN D ND2 
13168 N N   . ILE D 57  ? 0.3401 0.2038 0.5240 0.0354  -0.0076 -0.0180 57  ILE D N   
13169 C CA  . ILE D 57  ? 0.3460 0.2152 0.5309 0.0275  -0.0115 -0.0190 57  ILE D CA  
13170 C C   . ILE D 57  ? 0.3674 0.2256 0.5472 0.0213  -0.0158 -0.0192 57  ILE D C   
13171 O O   . ILE D 57  ? 0.3752 0.2409 0.5609 0.0158  -0.0190 -0.0169 57  ILE D O   
13172 C CB  . ILE D 57  ? 0.3636 0.2330 0.5434 0.0273  -0.0100 -0.0226 57  ILE D CB  
13173 C CG1 . ILE D 57  ? 0.3808 0.2652 0.5689 0.0315  -0.0064 -0.0212 57  ILE D CG1 
13174 C CG2 . ILE D 57  ? 0.3446 0.2157 0.5230 0.0194  -0.0144 -0.0240 57  ILE D CG2 
13175 C CD1 . ILE D 57  ? 0.4002 0.2851 0.5832 0.0318  -0.0043 -0.0241 57  ILE D CD1 
13176 N N   . LYS D 58  ? 0.3820 0.2221 0.5508 0.0223  -0.0156 -0.0214 58  LYS D N   
13177 C CA  . LYS D 58  ? 0.3953 0.2244 0.5597 0.0162  -0.0198 -0.0209 58  LYS D CA  
13178 C C   . LYS D 58  ? 0.3829 0.2182 0.5558 0.0158  -0.0208 -0.0159 58  LYS D C   
13179 O O   . LYS D 58  ? 0.3406 0.1795 0.5170 0.0091  -0.0243 -0.0138 58  LYS D O   
13180 C CB  . LYS D 58  ? 0.4059 0.2128 0.5564 0.0184  -0.0190 -0.0241 58  LYS D CB  
13181 C CG  . LYS D 58  ? 0.4360 0.2350 0.5759 0.0158  -0.0199 -0.0291 58  LYS D CG  
13182 C CD  . LYS D 58  ? 0.4929 0.2713 0.6180 0.0210  -0.0169 -0.0331 58  LYS D CD  
13183 C CE  . LYS D 58  ? 0.5423 0.3011 0.6585 0.0181  -0.0197 -0.0333 58  LYS D CE  
13184 N NZ  . LYS D 58  ? 0.5763 0.3143 0.6774 0.0243  -0.0162 -0.0375 58  LYS D NZ  
13185 N N   . GLU D 59  ? 0.4136 0.2498 0.5895 0.0233  -0.0175 -0.0137 59  GLU D N   
13186 C CA  . GLU D 59  ? 0.4141 0.2544 0.5964 0.0236  -0.0184 -0.0087 59  GLU D CA  
13187 C C   . GLU D 59  ? 0.3762 0.2354 0.5690 0.0196  -0.0200 -0.0062 59  GLU D C   
13188 O O   . GLU D 59  ? 0.3914 0.2545 0.5883 0.0169  -0.0219 -0.0025 59  GLU D O   
13189 C CB  . GLU D 59  ? 0.4238 0.2636 0.6084 0.0329  -0.0148 -0.0063 59  GLU D CB  
13190 C CG  . GLU D 59  ? 0.5013 0.3201 0.6759 0.0370  -0.0136 -0.0070 59  GLU D CG  
13191 C CD  . GLU D 59  ? 0.5646 0.3833 0.7415 0.0478  -0.0092 -0.0051 59  GLU D CD  
13192 O OE1 . GLU D 59  ? 0.5565 0.3925 0.7444 0.0514  -0.0080 -0.0018 59  GLU D OE1 
13193 O OE2 . GLU D 59  ? 0.5916 0.3925 0.7590 0.0528  -0.0069 -0.0071 59  GLU D OE2 
13194 N N   . GLY D 60  ? 0.3609 0.2315 0.5574 0.0197  -0.0190 -0.0082 60  GLY D N   
13195 C CA  . GLY D 60  ? 0.3270 0.2143 0.5324 0.0166  -0.0202 -0.0064 60  GLY D CA  
13196 C C   . GLY D 60  ? 0.3023 0.1914 0.5076 0.0087  -0.0234 -0.0071 60  GLY D C   
13197 O O   . GLY D 60  ? 0.2785 0.1803 0.4903 0.0064  -0.0240 -0.0058 60  GLY D O   
13198 N N   . GLY D 61  ? 0.3221 0.1985 0.5200 0.0048  -0.0254 -0.0090 61  GLY D N   
13199 C CA  . GLY D 61  ? 0.3301 0.2067 0.5281 -0.0031 -0.0290 -0.0085 61  GLY D CA  
13200 C C   . GLY D 61  ? 0.3541 0.2329 0.5502 -0.0065 -0.0305 -0.0118 61  GLY D C   
13201 O O   . GLY D 61  ? 0.3614 0.2431 0.5594 -0.0129 -0.0336 -0.0111 61  GLY D O   
13202 N N   . TYR D 62  ? 0.3463 0.2245 0.5392 -0.0022 -0.0283 -0.0150 62  TYR D N   
13203 C CA  . TYR D 62  ? 0.3262 0.2069 0.5169 -0.0045 -0.0294 -0.0178 62  TYR D CA  
13204 C C   . TYR D 62  ? 0.3517 0.2169 0.5312 -0.0076 -0.0319 -0.0209 62  TYR D C   
13205 O O   . TYR D 62  ? 0.3389 0.1899 0.5109 -0.0061 -0.0314 -0.0218 62  TYR D O   
13206 C CB  . TYR D 62  ? 0.3281 0.2147 0.5199 0.0015  -0.0256 -0.0193 62  TYR D CB  
13207 C CG  . TYR D 62  ? 0.3003 0.2012 0.5022 0.0042  -0.0237 -0.0164 62  TYR D CG  
13208 C CD1 . TYR D 62  ? 0.2748 0.1882 0.4834 0.0015  -0.0247 -0.0155 62  TYR D CD1 
13209 C CD2 . TYR D 62  ? 0.2966 0.1979 0.5009 0.0093  -0.0211 -0.0146 62  TYR D CD2 
13210 C CE1 . TYR D 62  ? 0.2596 0.1841 0.4757 0.0033  -0.0234 -0.0133 62  TYR D CE1 
13211 C CE2 . TYR D 62  ? 0.3006 0.2144 0.5133 0.0111  -0.0201 -0.0120 62  TYR D CE2 
13212 C CZ  . TYR D 62  ? 0.2814 0.2063 0.4994 0.0078  -0.0213 -0.0116 62  TYR D CZ  
13213 O OH  . TYR D 62  ? 0.2675 0.2030 0.4923 0.0091  -0.0207 -0.0092 62  TYR D OH  
13214 N N   . ASN D 63  ? 0.3640 0.2316 0.5420 -0.0123 -0.0349 -0.0224 63  ASN D N   
13215 C CA  . ASN D 63  ? 0.3684 0.2220 0.5353 -0.0163 -0.0381 -0.0253 63  ASN D CA  
13216 C C   . ASN D 63  ? 0.3618 0.2141 0.5220 -0.0139 -0.0370 -0.0288 63  ASN D C   
13217 O O   . ASN D 63  ? 0.3834 0.2223 0.5317 -0.0156 -0.0388 -0.0320 63  ASN D O   
13218 C CB  . ASN D 63  ? 0.3887 0.2440 0.5582 -0.0250 -0.0437 -0.0234 63  ASN D CB  
13219 C CG  . ASN D 63  ? 0.3899 0.2616 0.5684 -0.0276 -0.0454 -0.0218 63  ASN D CG  
13220 O OD1 . ASN D 63  ? 0.3907 0.2687 0.5699 -0.0240 -0.0434 -0.0232 63  ASN D OD1 
13221 N ND2 . ASN D 63  ? 0.4095 0.2882 0.5950 -0.0338 -0.0490 -0.0187 63  ASN D ND2 
13222 N N   . THR D 64  ? 0.3527 0.2174 0.5193 -0.0096 -0.0337 -0.0282 64  THR D N   
13223 C CA  . THR D 64  ? 0.3484 0.2139 0.5099 -0.0078 -0.0325 -0.0307 64  THR D CA  
13224 C C   . THR D 64  ? 0.3421 0.2152 0.5080 -0.0007 -0.0268 -0.0303 64  THR D C   
13225 O O   . THR D 64  ? 0.3167 0.1999 0.4928 0.0011  -0.0253 -0.0274 64  THR D O   
13226 C CB  . THR D 64  ? 0.3272 0.2030 0.4938 -0.0131 -0.0366 -0.0294 64  THR D CB  
13227 O OG1 . THR D 64  ? 0.3438 0.2139 0.5074 -0.0199 -0.0421 -0.0293 64  THR D OG1 
13228 C CG2 . THR D 64  ? 0.3388 0.2151 0.4996 -0.0121 -0.0362 -0.0315 64  THR D CG2 
13229 N N   . ILE D 65  ? 0.3404 0.2091 0.4983 0.0028  -0.0239 -0.0329 65  ILE D N   
13230 C CA  . ILE D 65  ? 0.3333 0.2115 0.4962 0.0082  -0.0190 -0.0321 65  ILE D CA  
13231 C C   . ILE D 65  ? 0.3262 0.2101 0.4877 0.0061  -0.0199 -0.0327 65  ILE D C   
13232 O O   . ILE D 65  ? 0.3550 0.2308 0.5070 0.0029  -0.0227 -0.0349 65  ILE D O   
13233 C CB  . ILE D 65  ? 0.3318 0.2018 0.4880 0.0151  -0.0135 -0.0338 65  ILE D CB  
13234 C CG1 . ILE D 65  ? 0.3531 0.2064 0.4934 0.0148  -0.0138 -0.0378 65  ILE D CG1 
13235 C CG2 . ILE D 65  ? 0.3306 0.1993 0.4918 0.0187  -0.0117 -0.0319 65  ILE D CG2 
13236 C CD1 . ILE D 65  ? 0.3668 0.2136 0.5001 0.0225  -0.0072 -0.0396 65  ILE D CD1 
13237 N N   . ARG D 66  ? 0.3310 0.2280 0.5016 0.0075  -0.0180 -0.0305 66  ARG D N   
13238 C CA  . ARG D 66  ? 0.3127 0.2157 0.4831 0.0063  -0.0182 -0.0303 66  ARG D CA  
13239 C C   . ARG D 66  ? 0.3104 0.2169 0.4804 0.0113  -0.0125 -0.0302 66  ARG D C   
13240 O O   . ARG D 66  ? 0.2778 0.1918 0.4562 0.0145  -0.0095 -0.0282 66  ARG D O   
13241 C CB  . ARG D 66  ? 0.3107 0.2256 0.4921 0.0031  -0.0210 -0.0276 66  ARG D CB  
13242 C CG  . ARG D 66  ? 0.3165 0.2391 0.5003 0.0022  -0.0212 -0.0266 66  ARG D CG  
13243 C CD  . ARG D 66  ? 0.3380 0.2676 0.5261 0.0058  -0.0166 -0.0254 66  ARG D CD  
13244 N NE  . ARG D 66  ? 0.3504 0.2877 0.5430 0.0041  -0.0175 -0.0238 66  ARG D NE  
13245 C CZ  . ARG D 66  ? 0.3474 0.2843 0.5353 0.0040  -0.0167 -0.0238 66  ARG D CZ  
13246 N NH1 . ARG D 66  ? 0.3585 0.2883 0.5366 0.0056  -0.0146 -0.0255 66  ARG D NH1 
13247 N NH2 . ARG D 66  ? 0.3655 0.3085 0.5579 0.0024  -0.0179 -0.0221 66  ARG D NH2 
13248 N N   . THR D 67  ? 0.3390 0.2409 0.4996 0.0118  -0.0112 -0.0319 67  THR D N   
13249 C CA  . THR D 67  ? 0.3725 0.2767 0.5313 0.0165  -0.0052 -0.0317 67  THR D CA  
13250 C C   . THR D 67  ? 0.3875 0.2976 0.5459 0.0146  -0.0053 -0.0306 67  THR D C   
13251 O O   . THR D 67  ? 0.3757 0.2866 0.5337 0.0102  -0.0101 -0.0303 67  THR D O   
13252 C CB  . THR D 67  ? 0.3981 0.2891 0.5437 0.0203  -0.0018 -0.0349 67  THR D CB  
13253 O OG1 . THR D 67  ? 0.3858 0.2676 0.5185 0.0173  -0.0045 -0.0374 67  THR D OG1 
13254 C CG2 . THR D 67  ? 0.4083 0.2911 0.5531 0.0221  -0.0021 -0.0360 67  THR D CG2 
13255 N N   . TRP D 68  ? 0.3719 0.2869 0.5313 0.0182  0.0002  -0.0294 68  TRP D N   
13256 C CA  . TRP D 68  ? 0.3787 0.2999 0.5387 0.0167  0.0009  -0.0277 68  TRP D CA  
13257 C C   . TRP D 68  ? 0.3694 0.2831 0.5160 0.0187  0.0045  -0.0293 68  TRP D C   
13258 O O   . TRP D 68  ? 0.3962 0.3102 0.5380 0.0166  0.0038  -0.0286 68  TRP D O   
13259 C CB  . TRP D 68  ? 0.3529 0.2870 0.5256 0.0178  0.0039  -0.0243 68  TRP D CB  
13260 C CG  . TRP D 68  ? 0.3168 0.2578 0.5005 0.0148  -0.0003 -0.0227 68  TRP D CG  
13261 C CD1 . TRP D 68  ? 0.3358 0.2817 0.5237 0.0111  -0.0035 -0.0212 68  TRP D CD1 
13262 C CD2 . TRP D 68  ? 0.3186 0.2609 0.5088 0.0153  -0.0019 -0.0226 68  TRP D CD2 
13263 N NE1 . TRP D 68  ? 0.3242 0.2744 0.5204 0.0095  -0.0065 -0.0204 68  TRP D NE1 
13264 C CE2 . TRP D 68  ? 0.3124 0.2608 0.5102 0.0117  -0.0057 -0.0212 68  TRP D CE2 
13265 C CE3 . TRP D 68  ? 0.3377 0.2759 0.5275 0.0185  -0.0004 -0.0235 68  TRP D CE3 
13266 C CZ2 . TRP D 68  ? 0.2838 0.2347 0.4882 0.0111  -0.0079 -0.0206 68  TRP D CZ2 
13267 C CZ3 . TRP D 68  ? 0.3088 0.2497 0.5059 0.0178  -0.0028 -0.0226 68  TRP D CZ3 
13268 C CH2 . TRP D 68  ? 0.3003 0.2477 0.5044 0.0140  -0.0065 -0.0212 68  TRP D CH2 
13269 N N   . SER D 69  ? 0.3800 0.2862 0.5198 0.0232  0.0087  -0.0315 69  SER D N   
13270 C CA  . SER D 69  ? 0.3782 0.2775 0.5050 0.0264  0.0137  -0.0331 69  SER D CA  
13271 C C   . SER D 69  ? 0.3805 0.2634 0.4930 0.0278  0.0130  -0.0376 69  SER D C   
13272 O O   . SER D 69  ? 0.3709 0.2499 0.4863 0.0291  0.0120  -0.0386 69  SER D O   
13273 C CB  . SER D 69  ? 0.3675 0.2751 0.5006 0.0319  0.0214  -0.0308 69  SER D CB  
13274 O OG  . SER D 69  ? 0.4167 0.3220 0.5396 0.0334  0.0260  -0.0310 69  SER D OG  
13275 N N   . GLN D 70  ? 0.3836 0.2564 0.4800 0.0275  0.0136  -0.0400 70  GLN D N   
13276 C CA  . GLN D 70  ? 0.4135 0.2689 0.4936 0.0274  0.0118  -0.0446 70  GLN D CA  
13277 C C   . GLN D 70  ? 0.4428 0.2909 0.5192 0.0345  0.0183  -0.0467 70  GLN D C   
13278 O O   . GLN D 70  ? 0.4547 0.3086 0.5340 0.0405  0.0260  -0.0452 70  GLN D O   
13279 C CB  . GLN D 70  ? 0.4317 0.2782 0.4942 0.0259  0.0117  -0.0467 70  GLN D CB  
13280 C CG  . GLN D 70  ? 0.4412 0.2933 0.5013 0.0302  0.0196  -0.0449 70  GLN D CG  
13281 C CD  . GLN D 70  ? 0.4358 0.3005 0.5038 0.0263  0.0175  -0.0407 70  GLN D CD  
13282 O OE1 . GLN D 70  ? 0.4015 0.2769 0.4845 0.0230  0.0134  -0.0378 70  GLN D OE1 
13283 N NE2 . GLN D 70  ? 0.4577 0.3203 0.5145 0.0266  0.0205  -0.0403 70  GLN D NE2 
13284 N N   . TYR D 71  ? 0.4558 0.2899 0.5245 0.0339  0.0152  -0.0501 71  TYR D N   
13285 C CA  . TYR D 71  ? 0.4553 0.2788 0.5178 0.0408  0.0208  -0.0525 71  TYR D CA  
13286 C C   . TYR D 71  ? 0.4873 0.2938 0.5275 0.0436  0.0244  -0.0571 71  TYR D C   
13287 O O   . TYR D 71  ? 0.4968 0.2960 0.5242 0.0385  0.0201  -0.0592 71  TYR D O   
13288 C CB  . TYR D 71  ? 0.4693 0.2835 0.5325 0.0382  0.0154  -0.0541 71  TYR D CB  
13289 C CG  . TYR D 71  ? 0.4446 0.2716 0.5274 0.0378  0.0136  -0.0502 71  TYR D CG  
13290 C CD1 . TYR D 71  ? 0.4293 0.2711 0.5264 0.0431  0.0191  -0.0464 71  TYR D CD1 
13291 C CD2 . TYR D 71  ? 0.4443 0.2684 0.5308 0.0320  0.0063  -0.0501 71  TYR D CD2 
13292 C CE1 . TYR D 71  ? 0.4176 0.2704 0.5311 0.0425  0.0171  -0.0430 71  TYR D CE1 
13293 C CE2 . TYR D 71  ? 0.4190 0.2539 0.5218 0.0318  0.0050  -0.0466 71  TYR D CE2 
13294 C CZ  . TYR D 71  ? 0.4064 0.2553 0.5221 0.0371  0.0103  -0.0432 71  TYR D CZ  
13295 O OH  . TYR D 71  ? 0.3916 0.2518 0.5227 0.0369  0.0089  -0.0396 71  TYR D OH  
13296 N N   . SER D 72  ? 0.4941 0.2938 0.5291 0.0521  0.0325  -0.0587 72  SER D N   
13297 C CA  . SER D 72  ? 0.5213 0.3011 0.5334 0.0557  0.0362  -0.0639 72  SER D CA  
13298 C C   . SER D 72  ? 0.5455 0.3053 0.5453 0.0515  0.0295  -0.0684 72  SER D C   
13299 O O   . SER D 72  ? 0.5299 0.2928 0.5408 0.0470  0.0232  -0.0669 72  SER D O   
13300 C CB  . SER D 72  ? 0.5250 0.3050 0.5371 0.0667  0.0473  -0.0637 72  SER D CB  
13301 O OG  . SER D 72  ? 0.5190 0.2927 0.5357 0.0711  0.0482  -0.0642 72  SER D OG  
13302 N N   . GLU D 73  ? 0.5772 0.3159 0.5531 0.0526  0.0307  -0.0739 73  GLU D N   
13303 C CA  . GLU D 73  ? 0.6005 0.3178 0.5619 0.0480  0.0241  -0.0786 73  GLU D CA  
13304 C C   . GLU D 73  ? 0.6120 0.3230 0.5794 0.0533  0.0266  -0.0787 73  GLU D C   
13305 O O   . GLU D 73  ? 0.6251 0.3288 0.5938 0.0476  0.0194  -0.0793 73  GLU D O   
13306 C CB  . GLU D 73  ? 0.6372 0.3318 0.5701 0.0486  0.0255  -0.0848 73  GLU D CB  
13307 C CG  . GLU D 73  ? 0.6579 0.3295 0.5752 0.0425  0.0176  -0.0897 73  GLU D CG  
13308 C CD  . GLU D 73  ? 0.6733 0.3219 0.5612 0.0399  0.0158  -0.0960 73  GLU D CD  
13309 O OE1 . GLU D 73  ? 0.6782 0.3247 0.5541 0.0455  0.0231  -0.0975 73  GLU D OE1 
13310 O OE2 . GLU D 73  ? 0.6721 0.3055 0.5493 0.0316  0.0066  -0.0990 73  GLU D OE2 
13311 N N   . ASN D 74  ? 0.5952 0.3098 0.5669 0.0640  0.0367  -0.0776 74  ASN D N   
13312 C CA  . ASN D 74  ? 0.6041 0.3137 0.5823 0.0701  0.0395  -0.0771 74  ASN D CA  
13313 C C   . ASN D 74  ? 0.5632 0.2902 0.5651 0.0661  0.0343  -0.0716 74  ASN D C   
13314 O O   . ASN D 74  ? 0.5720 0.2903 0.5756 0.0655  0.0312  -0.0718 74  ASN D O   
13315 C CB  . ASN D 74  ? 0.6101 0.3226 0.5900 0.0830  0.0514  -0.0762 74  ASN D CB  
13316 C CG  . ASN D 74  ? 0.6358 0.3258 0.5898 0.0885  0.0574  -0.0823 74  ASN D CG  
13317 O OD1 . ASN D 74  ? 0.6528 0.3202 0.5864 0.0835  0.0522  -0.0878 74  ASN D OD1 
13318 N ND2 . ASN D 74  ? 0.6400 0.3369 0.5948 0.0985  0.0682  -0.0811 74  ASN D ND2 
13319 N N   . GLN D 75  ? 0.5307 0.2811 0.5498 0.0635  0.0335  -0.0669 75  GLN D N   
13320 C CA  . GLN D 75  ? 0.5008 0.2673 0.5406 0.0591  0.0283  -0.0621 75  GLN D CA  
13321 C C   . GLN D 75  ? 0.5112 0.2696 0.5470 0.0487  0.0180  -0.0636 75  GLN D C   
13322 O O   . GLN D 75  ? 0.4942 0.2536 0.5391 0.0459  0.0137  -0.0617 75  GLN D O   
13323 C CB  . GLN D 75  ? 0.4854 0.2761 0.5413 0.0581  0.0297  -0.0574 75  GLN D CB  
13324 C CG  . GLN D 75  ? 0.4840 0.2855 0.5465 0.0675  0.0396  -0.0549 75  GLN D CG  
13325 C CD  . GLN D 75  ? 0.4551 0.2798 0.5338 0.0656  0.0403  -0.0500 75  GLN D CD  
13326 O OE1 . GLN D 75  ? 0.4683 0.2973 0.5448 0.0595  0.0369  -0.0500 75  GLN D OE1 
13327 N NE2 . GLN D 75  ? 0.4457 0.2857 0.5408 0.0706  0.0446  -0.0456 75  GLN D NE2 
13328 N N   . LEU D 76  ? 0.5376 0.2884 0.5598 0.0425  0.0137  -0.0666 76  LEU D N   
13329 C CA  . LEU D 76  ? 0.5585 0.3033 0.5779 0.0324  0.0037  -0.0675 76  LEU D CA  
13330 C C   . LEU D 76  ? 0.5928 0.3163 0.6014 0.0322  0.0017  -0.0708 76  LEU D C   
13331 O O   . LEU D 76  ? 0.6084 0.3321 0.6237 0.0257  -0.0050 -0.0692 76  LEU D O   
13332 C CB  . LEU D 76  ? 0.5755 0.3160 0.5820 0.0257  -0.0013 -0.0699 76  LEU D CB  
13333 C CG  . LEU D 76  ? 0.5743 0.3354 0.5927 0.0225  -0.0029 -0.0660 76  LEU D CG  
13334 C CD1 . LEU D 76  ? 0.6039 0.3574 0.6072 0.0162  -0.0084 -0.0684 76  LEU D CD1 
13335 C CD2 . LEU D 76  ? 0.5696 0.3466 0.6084 0.0178  -0.0081 -0.0614 76  LEU D CD2 
13336 N N   . LYS D 77  ? 0.6115 0.3160 0.6027 0.0388  0.0074  -0.0752 77  LYS D N   
13337 C CA  . LYS D 77  ? 0.6396 0.3215 0.6190 0.0387  0.0056  -0.0785 77  LYS D CA  
13338 C C   . LYS D 77  ? 0.6010 0.2903 0.5978 0.0410  0.0059  -0.0742 77  LYS D C   
13339 O O   . LYS D 77  ? 0.6080 0.2848 0.6017 0.0366  0.0009  -0.0749 77  LYS D O   
13340 C CB  . LYS D 77  ? 0.6810 0.3409 0.6401 0.0476  0.0131  -0.0837 77  LYS D CB  
13341 C CG  . LYS D 77  ? 0.7058 0.3512 0.6420 0.0451  0.0124  -0.0891 77  LYS D CG  
13342 C CD  . LYS D 77  ? 0.7549 0.3786 0.6702 0.0548  0.0210  -0.0945 77  LYS D CD  
13343 C CE  . LYS D 77  ? 0.7872 0.3994 0.6802 0.0519  0.0203  -0.0993 77  LYS D CE  
13344 N NZ  . LYS D 77  ? 0.8408 0.4296 0.7111 0.0610  0.0284  -0.1051 77  LYS D NZ  
13345 N N   . LEU D 78  ? 0.5632 0.2724 0.5776 0.0477  0.0117  -0.0698 78  LEU D N   
13346 C CA  . LEU D 78  ? 0.5419 0.2591 0.5725 0.0505  0.0122  -0.0654 78  LEU D CA  
13347 C C   . LEU D 78  ? 0.5139 0.2430 0.5576 0.0404  0.0036  -0.0619 78  LEU D C   
13348 O O   . LEU D 78  ? 0.5379 0.2611 0.5845 0.0374  -0.0002 -0.0606 78  LEU D O   
13349 C CB  . LEU D 78  ? 0.5230 0.2582 0.5680 0.0599  0.0202  -0.0615 78  LEU D CB  
13350 C CG  . LEU D 78  ? 0.5445 0.2885 0.6058 0.0638  0.0210  -0.0566 78  LEU D CG  
13351 C CD1 . LEU D 78  ? 0.5705 0.2922 0.6219 0.0669  0.0210  -0.0585 78  LEU D CD1 
13352 C CD2 . LEU D 78  ? 0.5419 0.3025 0.6155 0.0735  0.0292  -0.0531 78  LEU D CD2 
13353 N N   . VAL D 79  ? 0.4925 0.2380 0.5437 0.0353  0.0009  -0.0603 79  VAL D N   
13354 C CA  . VAL D 79  ? 0.4857 0.2437 0.5497 0.0267  -0.0063 -0.0569 79  VAL D CA  
13355 C C   . VAL D 79  ? 0.5114 0.2536 0.5648 0.0179  -0.0141 -0.0593 79  VAL D C   
13356 O O   . VAL D 79  ? 0.5452 0.2890 0.6066 0.0133  -0.0183 -0.0567 79  VAL D O   
13357 C CB  . VAL D 79  ? 0.4624 0.2394 0.5353 0.0238  -0.0073 -0.0549 79  VAL D CB  
13358 C CG1 . VAL D 79  ? 0.4455 0.2362 0.5327 0.0163  -0.0138 -0.0511 79  VAL D CG1 
13359 C CG2 . VAL D 79  ? 0.4536 0.2447 0.5360 0.0319  0.0003  -0.0525 79  VAL D CG2 
13360 N N   . GLN D 80  ? 0.5291 0.2549 0.5637 0.0157  -0.0156 -0.0641 80  GLN D N   
13361 C CA  . GLN D 80  ? 0.5564 0.2650 0.5789 0.0072  -0.0230 -0.0667 80  GLN D CA  
13362 C C   . GLN D 80  ? 0.5860 0.2808 0.6074 0.0081  -0.0232 -0.0665 80  GLN D C   
13363 O O   . GLN D 80  ? 0.5687 0.2632 0.5950 0.0001  -0.0297 -0.0644 80  GLN D O   
13364 C CB  . GLN D 80  ? 0.5618 0.2529 0.5618 0.0065  -0.0233 -0.0725 80  GLN D CB  
13365 C CG  . GLN D 80  ? 0.5833 0.2595 0.5706 -0.0044 -0.0327 -0.0751 80  GLN D CG  
13366 C CD  . GLN D 80  ? 0.5666 0.2594 0.5646 -0.0141 -0.0407 -0.0718 80  GLN D CD  
13367 O OE1 . GLN D 80  ? 0.5373 0.2470 0.5428 -0.0132 -0.0397 -0.0699 80  GLN D OE1 
13368 N NE2 . GLN D 80  ? 0.5616 0.2496 0.5605 -0.0236 -0.0488 -0.0708 80  GLN D NE2 
13369 N N   . GLU D 81  ? 0.6060 0.2896 0.6212 0.0179  -0.0159 -0.0681 81  GLU D N   
13370 C CA  . GLU D 81  ? 0.6490 0.3170 0.6612 0.0196  -0.0158 -0.0679 81  GLU D CA  
13371 C C   . GLU D 81  ? 0.5941 0.2795 0.6275 0.0195  -0.0165 -0.0616 81  GLU D C   
13372 O O   . GLU D 81  ? 0.5802 0.2561 0.6139 0.0169  -0.0192 -0.0601 81  GLU D O   
13373 C CB  . GLU D 81  ? 0.7450 0.3976 0.7466 0.0316  -0.0073 -0.0707 81  GLU D CB  
13374 C CG  . GLU D 81  ? 0.8630 0.4915 0.8394 0.0328  -0.0059 -0.0777 81  GLU D CG  
13375 C CD  . GLU D 81  ? 0.9768 0.6014 0.9456 0.0458  0.0046  -0.0803 81  GLU D CD  
13376 O OE1 . GLU D 81  ? 0.9531 0.5968 0.9375 0.0541  0.0113  -0.0763 81  GLU D OE1 
13377 O OE2 . GLU D 81  ? 0.9772 0.5791 0.9232 0.0472  0.0061  -0.0864 81  GLU D OE2 
13378 N N   . SER D 82  ? 0.5640 0.2737 0.6143 0.0225  -0.0137 -0.0578 82  SER D N   
13379 C CA  . SER D 82  ? 0.5156 0.2420 0.5849 0.0225  -0.0142 -0.0520 82  SER D CA  
13380 C C   . SER D 82  ? 0.4950 0.2234 0.5694 0.0115  -0.0222 -0.0496 82  SER D C   
13381 O O   . SER D 82  ? 0.4694 0.2022 0.5535 0.0110  -0.0231 -0.0456 82  SER D O   
13382 C CB  . SER D 82  ? 0.4982 0.2494 0.5826 0.0255  -0.0112 -0.0490 82  SER D CB  
13383 O OG  . SER D 82  ? 0.4731 0.2361 0.5626 0.0168  -0.0167 -0.0482 82  SER D OG  
13384 N N   . GLY D 83  ? 0.4928 0.2210 0.5622 0.0030  -0.0279 -0.0515 83  GLY D N   
13385 C CA  . GLY D 83  ? 0.4899 0.2253 0.5670 -0.0074 -0.0351 -0.0486 83  GLY D CA  
13386 C C   . GLY D 83  ? 0.4581 0.2185 0.5506 -0.0096 -0.0362 -0.0453 83  GLY D C   
13387 O O   . GLY D 83  ? 0.4348 0.2030 0.5336 -0.0178 -0.0419 -0.0432 83  GLY D O   
13388 N N   . LEU D 84  ? 0.4635 0.2367 0.5630 -0.0022 -0.0305 -0.0446 84  LEU D N   
13389 C CA  . LEU D 84  ? 0.4445 0.2400 0.5583 -0.0036 -0.0310 -0.0415 84  LEU D CA  
13390 C C   . LEU D 84  ? 0.4372 0.2349 0.5455 -0.0079 -0.0341 -0.0437 84  LEU D C   
13391 O O   . LEU D 84  ? 0.4453 0.2312 0.5399 -0.0056 -0.0325 -0.0477 84  LEU D O   
13392 C CB  . LEU D 84  ? 0.4353 0.2429 0.5577 0.0049  -0.0245 -0.0399 84  LEU D CB  
13393 C CG  . LEU D 84  ? 0.4597 0.2723 0.5923 0.0086  -0.0223 -0.0362 84  LEU D CG  
13394 C CD1 . LEU D 84  ? 0.4799 0.2997 0.6172 0.0178  -0.0156 -0.0354 84  LEU D CD1 
13395 C CD2 . LEU D 84  ? 0.4381 0.2661 0.5842 0.0031  -0.0259 -0.0321 84  LEU D CD2 
13396 N N   . LYS D 85  ? 0.4105 0.2234 0.5294 -0.0132 -0.0380 -0.0409 85  LYS D N   
13397 C CA  . LYS D 85  ? 0.4235 0.2417 0.5396 -0.0159 -0.0403 -0.0420 85  LYS D CA  
13398 C C   . LYS D 85  ? 0.4032 0.2335 0.5248 -0.0095 -0.0349 -0.0414 85  LYS D C   
13399 O O   . LYS D 85  ? 0.3808 0.2189 0.5115 -0.0043 -0.0303 -0.0394 85  LYS D O   
13400 C CB  . LYS D 85  ? 0.4318 0.2615 0.5574 -0.0236 -0.0465 -0.0389 85  LYS D CB  
13401 C CG  . LYS D 85  ? 0.4591 0.2800 0.5823 -0.0309 -0.0521 -0.0383 85  LYS D CG  
13402 C CD  . LYS D 85  ? 0.4702 0.2694 0.5754 -0.0340 -0.0551 -0.0425 85  LYS D CD  
13403 C CE  . LYS D 85  ? 0.4693 0.2620 0.5750 -0.0423 -0.0609 -0.0409 85  LYS D CE  
13404 N NZ  . LYS D 85  ? 0.4805 0.2501 0.5681 -0.0459 -0.0641 -0.0450 85  LYS D NZ  
13405 N N   . LEU D 86  ? 0.4105 0.2422 0.5264 -0.0104 -0.0358 -0.0428 86  LEU D N   
13406 C CA  . LEU D 86  ? 0.4118 0.2525 0.5302 -0.0051 -0.0307 -0.0425 86  LEU D CA  
13407 C C   . LEU D 86  ? 0.3961 0.2479 0.5186 -0.0088 -0.0342 -0.0409 86  LEU D C   
13408 O O   . LEU D 86  ? 0.3800 0.2262 0.4939 -0.0135 -0.0389 -0.0422 86  LEU D O   
13409 C CB  . LEU D 86  ? 0.4272 0.2540 0.5300 -0.0002 -0.0263 -0.0465 86  LEU D CB  
13410 C CG  . LEU D 86  ? 0.4352 0.2691 0.5375 0.0047  -0.0210 -0.0464 86  LEU D CG  
13411 C CD1 . LEU D 86  ? 0.4313 0.2813 0.5492 0.0091  -0.0165 -0.0428 86  LEU D CD1 
13412 C CD2 . LEU D 86  ? 0.4464 0.2656 0.5328 0.0100  -0.0159 -0.0503 86  LEU D CD2 
13413 N N   . ILE D 87  ? 0.3795 0.2466 0.5152 -0.0068 -0.0320 -0.0377 87  ILE D N   
13414 C CA  . ILE D 87  ? 0.3872 0.2641 0.5260 -0.0076 -0.0327 -0.0363 87  ILE D CA  
13415 C C   . ILE D 87  ? 0.3990 0.2753 0.5327 -0.0020 -0.0266 -0.0374 87  ILE D C   
13416 O O   . ILE D 87  ? 0.3609 0.2444 0.5026 0.0023  -0.0218 -0.0359 87  ILE D O   
13417 C CB  . ILE D 87  ? 0.3672 0.2593 0.5218 -0.0088 -0.0338 -0.0325 87  ILE D CB  
13418 C CG1 . ILE D 87  ? 0.3743 0.2671 0.5333 -0.0143 -0.0394 -0.0313 87  ILE D CG1 
13419 C CG2 . ILE D 87  ? 0.3548 0.2560 0.5126 -0.0088 -0.0341 -0.0309 87  ILE D CG2 
13420 C CD1 . ILE D 87  ? 0.3632 0.2695 0.5367 -0.0150 -0.0398 -0.0278 87  ILE D CD1 
13421 N N   . MET D 88  ? 0.4163 0.2845 0.5367 -0.0023 -0.0268 -0.0396 88  MET D N   
13422 C CA  . MET D 88  ? 0.4217 0.2882 0.5359 0.0031  -0.0204 -0.0406 88  MET D CA  
13423 C C   . MET D 88  ? 0.4007 0.2779 0.5192 0.0028  -0.0198 -0.0381 88  MET D C   
13424 O O   . MET D 88  ? 0.3756 0.2526 0.4900 -0.0012 -0.0245 -0.0377 88  MET D O   
13425 C CB  . MET D 88  ? 0.4387 0.2887 0.5338 0.0038  -0.0196 -0.0448 88  MET D CB  
13426 C CG  . MET D 88  ? 0.4560 0.3045 0.5449 0.0103  -0.0116 -0.0457 88  MET D CG  
13427 S SD  . MET D 88  ? 0.4893 0.3168 0.5563 0.0138  -0.0082 -0.0511 88  MET D SD  
13428 C CE  . MET D 88  ? 0.4775 0.2953 0.5289 0.0064  -0.0161 -0.0532 88  MET D CE  
13429 N N   . GLY D 89  ? 0.4076 0.2937 0.5341 0.0070  -0.0141 -0.0362 89  GLY D N   
13430 C CA  . GLY D 89  ? 0.4024 0.2972 0.5321 0.0073  -0.0123 -0.0338 89  GLY D CA  
13431 C C   . GLY D 89  ? 0.4048 0.2930 0.5211 0.0099  -0.0079 -0.0352 89  GLY D C   
13432 O O   . GLY D 89  ? 0.4275 0.3083 0.5368 0.0140  -0.0033 -0.0375 89  GLY D O   
13433 N N   . ILE D 90  ? 0.3953 0.2853 0.5075 0.0078  -0.0094 -0.0339 90  ILE D N   
13434 C CA  . ILE D 90  ? 0.4302 0.3154 0.5300 0.0098  -0.0052 -0.0345 90  ILE D CA  
13435 C C   . ILE D 90  ? 0.4282 0.3251 0.5368 0.0112  -0.0007 -0.0306 90  ILE D C   
13436 O O   . ILE D 90  ? 0.4416 0.3467 0.5601 0.0084  -0.0042 -0.0279 90  ILE D O   
13437 C CB  . ILE D 90  ? 0.4363 0.3141 0.5238 0.0054  -0.0113 -0.0354 90  ILE D CB  
13438 C CG1 . ILE D 90  ? 0.4484 0.3155 0.5288 0.0026  -0.0168 -0.0388 90  ILE D CG1 
13439 C CG2 . ILE D 90  ? 0.4575 0.3297 0.5302 0.0070  -0.0075 -0.0358 90  ILE D CG2 
13440 C CD1 . ILE D 90  ? 0.4487 0.3021 0.5156 0.0058  -0.0131 -0.0431 90  ILE D CD1 
13441 N N   . ASP D 91  ? 0.4306 0.3282 0.5359 0.0156  0.0069  -0.0304 91  ASP D N   
13442 C CA  . ASP D 91  ? 0.4515 0.3605 0.5658 0.0166  0.0115  -0.0264 91  ASP D CA  
13443 C C   . ASP D 91  ? 0.4487 0.3576 0.5560 0.0139  0.0106  -0.0242 91  ASP D C   
13444 O O   . ASP D 91  ? 0.4875 0.3969 0.5890 0.0159  0.0163  -0.0230 91  ASP D O   
13445 C CB  . ASP D 91  ? 0.4842 0.3955 0.5986 0.0222  0.0202  -0.0262 91  ASP D CB  
13446 C CG  . ASP D 91  ? 0.5175 0.4418 0.6421 0.0227  0.0251  -0.0216 91  ASP D CG  
13447 O OD1 . ASP D 91  ? 0.4955 0.4265 0.6279 0.0185  0.0216  -0.0187 91  ASP D OD1 
13448 O OD2 . ASP D 91  ? 0.5303 0.4577 0.6545 0.0271  0.0327  -0.0207 91  ASP D OD2 
13449 N N   . ILE D 92  ? 0.4914 0.4005 0.6000 0.0096  0.0039  -0.0232 92  ILE D N   
13450 C CA  . ILE D 92  ? 0.4981 0.4085 0.6025 0.0073  0.0031  -0.0201 92  ILE D CA  
13451 C C   . ILE D 92  ? 0.4379 0.3596 0.5564 0.0067  0.0054  -0.0160 92  ILE D C   
13452 O O   . ILE D 92  ? 0.4033 0.3304 0.5336 0.0051  0.0018  -0.0152 92  ILE D O   
13453 C CB  . ILE D 92  ? 0.5013 0.4075 0.6018 0.0034  -0.0054 -0.0202 92  ILE D CB  
13454 C CG1 . ILE D 92  ? 0.4951 0.3901 0.5824 0.0029  -0.0087 -0.0244 92  ILE D CG1 
13455 C CG2 . ILE D 92  ? 0.5251 0.4318 0.6209 0.0014  -0.0067 -0.0167 92  ILE D CG2 
13456 C CD1 . ILE D 92  ? 0.5011 0.3867 0.5706 0.0049  -0.0044 -0.0263 92  ILE D CD1 
13457 N N   . LYS D 93  ? 0.4649 0.3902 0.5822 0.0080  0.0116  -0.0136 93  LYS D N   
13458 C CA  . LYS D 93  ? 0.5237 0.4595 0.6548 0.0070  0.0139  -0.0099 93  LYS D CA  
13459 C C   . LYS D 93  ? 0.4725 0.4098 0.6083 0.0030  0.0083  -0.0074 93  LYS D C   
13460 O O   . LYS D 93  ? 0.4428 0.3759 0.5703 0.0014  0.0067  -0.0057 93  LYS D O   
13461 C CB  . LYS D 93  ? 0.6343 0.5746 0.7637 0.0085  0.0216  -0.0070 93  LYS D CB  
13462 C CG  . LYS D 93  ? 0.7823 0.7263 0.9147 0.0131  0.0282  -0.0082 93  LYS D CG  
13463 C CD  . LYS D 93  ? 0.9715 0.9184 1.0986 0.0154  0.0364  -0.0057 93  LYS D CD  
13464 C CE  . LYS D 93  ? 1.0592 0.9946 1.1669 0.0173  0.0382  -0.0082 93  LYS D CE  
13465 N NZ  . LYS D 93  ? 1.0317 0.9697 1.1333 0.0181  0.0454  -0.0049 93  LYS D NZ  
13466 N N   . PRO D 94  ? 0.4385 0.3812 0.5871 0.0017  0.0053  -0.0070 94  PRO D N   
13467 C CA  . PRO D 94  ? 0.4551 0.3982 0.6081 -0.0012 0.0004  -0.0050 94  PRO D CA  
13468 C C   . PRO D 94  ? 0.4733 0.4184 0.6272 -0.0036 0.0020  -0.0008 94  PRO D C   
13469 O O   . PRO D 94  ? 0.5126 0.4553 0.6670 -0.0054 -0.0021 0.0008  94  PRO D O   
13470 C CB  . PRO D 94  ? 0.4416 0.3898 0.6069 -0.0014 -0.0016 -0.0061 94  PRO D CB  
13471 C CG  . PRO D 94  ? 0.4226 0.3758 0.5927 0.0008  0.0033  -0.0069 94  PRO D CG  
13472 C CD  . PRO D 94  ? 0.4309 0.3792 0.5898 0.0034  0.0068  -0.0084 94  PRO D CD  
13473 N N   . GLU D 95  ? 0.4870 0.4362 0.6413 -0.0034 0.0081  0.0013  95  GLU D N   
13474 C CA  . GLU D 95  ? 0.5174 0.4692 0.6740 -0.0063 0.0099  0.0057  95  GLU D CA  
13475 C C   . GLU D 95  ? 0.4910 0.4376 0.6349 -0.0067 0.0118  0.0079  95  GLU D C   
13476 O O   . GLU D 95  ? 0.4622 0.4093 0.6059 -0.0094 0.0130  0.0120  95  GLU D O   
13477 C CB  . GLU D 95  ? 0.5628 0.5239 0.7284 -0.0070 0.0153  0.0080  95  GLU D CB  
13478 C CG  . GLU D 95  ? 0.6741 0.6412 0.8529 -0.0082 0.0133  0.0074  95  GLU D CG  
13479 C CD  . GLU D 95  ? 0.7900 0.7607 0.9734 -0.0047 0.0140  0.0040  95  GLU D CD  
13480 O OE1 . GLU D 95  ? 0.8987 0.8667 1.0749 -0.0011 0.0167  0.0020  95  GLU D OE1 
13481 O OE2 . GLU D 95  ? 0.6541 0.6293 0.8474 -0.0056 0.0119  0.0035  95  GLU D OE2 
13482 N N   . GLU D 96  ? 0.4712 0.4123 0.6038 -0.0041 0.0121  0.0053  96  GLU D N   
13483 C CA  . GLU D 96  ? 0.4700 0.4055 0.5885 -0.0043 0.0140  0.0072  96  GLU D CA  
13484 C C   . GLU D 96  ? 0.3929 0.3222 0.5063 -0.0066 0.0075  0.0090  96  GLU D C   
13485 O O   . GLU D 96  ? 0.3516 0.2800 0.4706 -0.0070 0.0016  0.0078  96  GLU D O   
13486 C CB  . GLU D 96  ? 0.5222 0.4523 0.6286 -0.0010 0.0159  0.0034  96  GLU D CB  
13487 C CG  . GLU D 96  ? 0.6006 0.5356 0.7088 0.0022  0.0239  0.0025  96  GLU D CG  
13488 C CD  . GLU D 96  ? 0.6621 0.6013 0.7678 0.0018  0.0310  0.0069  96  GLU D CD  
13489 O OE1 . GLU D 96  ? 0.7089 0.6423 0.7998 0.0025  0.0338  0.0075  96  GLU D OE1 
13490 O OE2 . GLU D 96  ? 0.6577 0.6064 0.7768 0.0005  0.0336  0.0098  96  GLU D OE2 
13491 N N   . ASP D 97  ? 0.3827 0.3078 0.4848 -0.0075 0.0090  0.0121  97  ASP D N   
13492 C CA  . ASP D 97  ? 0.4050 0.3237 0.5001 -0.0091 0.0032  0.0145  97  ASP D CA  
13493 C C   . ASP D 97  ? 0.4268 0.3393 0.5118 -0.0077 -0.0019 0.0110  97  ASP D C   
13494 O O   . ASP D 97  ? 0.3986 0.3061 0.4695 -0.0069 -0.0001 0.0100  97  ASP D O   
13495 C CB  . ASP D 97  ? 0.4000 0.3163 0.4864 -0.0108 0.0067  0.0195  97  ASP D CB  
13496 C CG  . ASP D 97  ? 0.4046 0.3142 0.4837 -0.0122 0.0007  0.0228  97  ASP D CG  
13497 O OD1 . ASP D 97  ? 0.4042 0.3117 0.4854 -0.0116 -0.0062 0.0211  97  ASP D OD1 
13498 O OD2 . ASP D 97  ? 0.4336 0.3403 0.5046 -0.0137 0.0030  0.0272  97  ASP D OD2 
13499 N N   . TYR D 98  ? 0.4416 0.3543 0.5335 -0.0078 -0.0085 0.0093  98  TYR D N   
13500 C CA  . TYR D 98  ? 0.4354 0.3437 0.5205 -0.0073 -0.0142 0.0063  98  TYR D CA  
13501 C C   . TYR D 98  ? 0.4500 0.3518 0.5207 -0.0084 -0.0179 0.0088  98  TYR D C   
13502 O O   . TYR D 98  ? 0.4674 0.3642 0.5277 -0.0086 -0.0215 0.0064  98  TYR D O   
13503 C CB  . TYR D 98  ? 0.4100 0.3213 0.5066 -0.0075 -0.0205 0.0055  98  TYR D CB  
13504 C CG  . TYR D 98  ? 0.3892 0.3069 0.5007 -0.0068 -0.0182 0.0037  98  TYR D CG  
13505 C CD1 . TYR D 98  ? 0.3841 0.3043 0.4976 -0.0056 -0.0128 0.0008  98  TYR D CD1 
13506 C CD2 . TYR D 98  ? 0.3839 0.3051 0.5070 -0.0070 -0.0215 0.0049  98  TYR D CD2 
13507 C CE1 . TYR D 98  ? 0.3674 0.2936 0.4940 -0.0050 -0.0114 -0.0006 98  TYR D CE1 
13508 C CE2 . TYR D 98  ? 0.3631 0.2896 0.4984 -0.0066 -0.0198 0.0032  98  TYR D CE2 
13509 C CZ  . TYR D 98  ? 0.3621 0.2913 0.4993 -0.0058 -0.0150 0.0006  98  TYR D CZ  
13510 O OH  . TYR D 98  ? 0.3399 0.2745 0.4888 -0.0055 -0.0138 -0.0008 98  TYR D OH  
13511 N N   . GLY D 99  ? 0.4573 0.3586 0.5271 -0.0094 -0.0171 0.0139  99  GLY D N   
13512 C CA  . GLY D 99  ? 0.4641 0.3595 0.5212 -0.0105 -0.0207 0.0175  99  GLY D CA  
13513 C C   . GLY D 99  ? 0.4610 0.3519 0.5021 -0.0106 -0.0152 0.0182  99  GLY D C   
13514 O O   . GLY D 99  ? 0.5120 0.3971 0.5396 -0.0115 -0.0183 0.0206  99  GLY D O   
13515 N N   . ASP D 100 ? 0.4438 0.3375 0.4862 -0.0095 -0.0072 0.0162  100 ASP D N   
13516 C CA  . ASP D 100 ? 0.4630 0.3530 0.4905 -0.0089 -0.0007 0.0165  100 ASP D CA  
13517 C C   . ASP D 100 ? 0.4700 0.3532 0.4834 -0.0076 -0.0022 0.0112  100 ASP D C   
13518 O O   . ASP D 100 ? 0.4428 0.3272 0.4609 -0.0059 -0.0010 0.0063  100 ASP D O   
13519 C CB  . ASP D 100 ? 0.4771 0.3739 0.5124 -0.0078 0.0088  0.0167  100 ASP D CB  
13520 C CG  . ASP D 100 ? 0.5141 0.4086 0.5353 -0.0065 0.0170  0.0174  100 ASP D CG  
13521 O OD1 . ASP D 100 ? 0.5084 0.3948 0.5117 -0.0067 0.0155  0.0177  100 ASP D OD1 
13522 O OD2 . ASP D 100 ? 0.5292 0.4306 0.5574 -0.0052 0.0250  0.0180  100 ASP D OD2 
13523 N N   . PRO D 101 ? 0.4864 0.3615 0.4812 -0.0085 -0.0047 0.0122  101 PRO D N   
13524 C CA  . PRO D 101 ? 0.4950 0.3617 0.4746 -0.0081 -0.0076 0.0071  101 PRO D CA  
13525 C C   . PRO D 101 ? 0.5181 0.3828 0.4919 -0.0049 0.0011  0.0025  101 PRO D C   
13526 O O   . PRO D 101 ? 0.5046 0.3629 0.4709 -0.0041 -0.0009 -0.0031 101 PRO D O   
13527 C CB  . PRO D 101 ? 0.5238 0.3826 0.4840 -0.0099 -0.0111 0.0100  101 PRO D CB  
13528 C CG  . PRO D 101 ? 0.5398 0.4030 0.5062 -0.0111 -0.0103 0.0172  101 PRO D CG  
13529 C CD  . PRO D 101 ? 0.5161 0.3888 0.5021 -0.0101 -0.0043 0.0182  101 PRO D CD  
13530 N N   . GLU D 102 ? 0.5185 0.3883 0.4952 -0.0032 0.0107  0.0051  102 GLU D N   
13531 C CA  . GLU D 102 ? 0.5281 0.3982 0.5023 0.0007  0.0199  0.0016  102 GLU D CA  
13532 C C   . GLU D 102 ? 0.5136 0.3878 0.5029 0.0023  0.0185  -0.0028 102 GLU D C   
13533 O O   . GLU D 102 ? 0.5501 0.4185 0.5325 0.0049  0.0203  -0.0081 102 GLU D O   
13534 C CB  . GLU D 102 ? 0.5535 0.4312 0.5320 0.0021  0.0303  0.0059  102 GLU D CB  
13535 C CG  . GLU D 102 ? 0.5903 0.4668 0.5619 0.0071  0.0401  0.0023  102 GLU D CG  
13536 C CD  . GLU D 102 ? 0.6302 0.5137 0.6023 0.0090  0.0513  0.0065  102 GLU D CD  
13537 O OE1 . GLU D 102 ? 0.6702 0.5539 0.6362 0.0064  0.0524  0.0117  102 GLU D OE1 
13538 O OE2 . GLU D 102 ? 0.6894 0.5779 0.6671 0.0133  0.0591  0.0046  102 GLU D OE2 
13539 N N   . PHE D 103 ? 0.4618 0.3449 0.4707 0.0006  0.0154  -0.0004 103 PHE D N   
13540 C CA  . PHE D 103 ? 0.4284 0.3165 0.4525 0.0019  0.0145  -0.0036 103 PHE D CA  
13541 C C   . PHE D 103 ? 0.4395 0.3202 0.4586 0.0010  0.0063  -0.0082 103 PHE D C   
13542 O O   . PHE D 103 ? 0.4156 0.2952 0.4382 0.0028  0.0068  -0.0126 103 PHE D O   
13543 C CB  . PHE D 103 ? 0.3937 0.2922 0.4376 0.0000  0.0131  0.0003  103 PHE D CB  
13544 C CG  . PHE D 103 ? 0.3720 0.2749 0.4306 0.0008  0.0105  -0.0029 103 PHE D CG  
13545 C CD1 . PHE D 103 ? 0.3516 0.2586 0.4165 0.0040  0.0166  -0.0052 103 PHE D CD1 
13546 C CD2 . PHE D 103 ? 0.3579 0.2604 0.4228 -0.0014 0.0019  -0.0035 103 PHE D CD2 
13547 C CE1 . PHE D 103 ? 0.3327 0.2429 0.4096 0.0047  0.0140  -0.0079 103 PHE D CE1 
13548 C CE2 . PHE D 103 ? 0.3362 0.2422 0.4130 -0.0007 -0.0002 -0.0064 103 PHE D CE2 
13549 C CZ  . PHE D 103 ? 0.3387 0.2482 0.4211 0.0022  0.0058  -0.0086 103 PHE D CZ  
13550 N N   . VAL D 104 ? 0.4315 0.3078 0.4433 -0.0022 -0.0014 -0.0066 104 VAL D N   
13551 C CA  . VAL D 104 ? 0.4333 0.3043 0.4418 -0.0041 -0.0100 -0.0099 104 VAL D CA  
13552 C C   . VAL D 104 ? 0.4511 0.3108 0.4413 -0.0027 -0.0081 -0.0152 104 VAL D C   
13553 O O   . VAL D 104 ? 0.4637 0.3194 0.4542 -0.0030 -0.0114 -0.0195 104 VAL D O   
13554 C CB  . VAL D 104 ? 0.4416 0.3111 0.4463 -0.0076 -0.0189 -0.0064 104 VAL D CB  
13555 C CG1 . VAL D 104 ? 0.4508 0.3161 0.4529 -0.0100 -0.0280 -0.0095 104 VAL D CG1 
13556 C CG2 . VAL D 104 ? 0.4284 0.3071 0.4499 -0.0084 -0.0208 -0.0014 104 VAL D CG2 
13557 N N   . LYS D 105 ? 0.4675 0.3214 0.4411 -0.0015 -0.0028 -0.0146 105 LYS D N   
13558 C CA  . LYS D 105 ? 0.4855 0.3271 0.4389 0.0002  -0.0001 -0.0197 105 LYS D CA  
13559 C C   . LYS D 105 ? 0.5012 0.3436 0.4608 0.0048  0.0075  -0.0236 105 LYS D C   
13560 O O   . LYS D 105 ? 0.5193 0.3524 0.4711 0.0054  0.0057  -0.0290 105 LYS D O   
13561 C CB  . LYS D 105 ? 0.5012 0.3378 0.4366 0.0010  0.0051  -0.0174 105 LYS D CB  
13562 C CG  . LYS D 105 ? 0.5338 0.3559 0.4444 0.0028  0.0079  -0.0225 105 LYS D CG  
13563 C CD  . LYS D 105 ? 0.5585 0.3763 0.4510 0.0037  0.0138  -0.0198 105 LYS D CD  
13564 C CE  . LYS D 105 ? 0.5874 0.3912 0.4560 0.0069  0.0193  -0.0253 105 LYS D CE  
13565 N NZ  . LYS D 105 ? 0.6099 0.4079 0.4580 0.0060  0.0214  -0.0225 105 LYS D NZ  
13566 N N   . ASP D 106 ? 0.4997 0.3530 0.4736 0.0077  0.0154  -0.0207 106 ASP D N   
13567 C CA  . ASP D 106 ? 0.5118 0.3673 0.4928 0.0126  0.0225  -0.0237 106 ASP D CA  
13568 C C   . ASP D 106 ? 0.4993 0.3547 0.4913 0.0115  0.0163  -0.0269 106 ASP D C   
13569 O O   . ASP D 106 ? 0.5313 0.3794 0.5183 0.0143  0.0182  -0.0317 106 ASP D O   
13570 C CB  . ASP D 106 ? 0.4934 0.3619 0.4884 0.0152  0.0313  -0.0194 106 ASP D CB  
13571 C CG  . ASP D 106 ? 0.5015 0.3686 0.4831 0.0169  0.0390  -0.0168 106 ASP D CG  
13572 O OD1 . ASP D 106 ? 0.5200 0.3747 0.4805 0.0175  0.0391  -0.0198 106 ASP D OD1 
13573 O OD2 . ASP D 106 ? 0.5107 0.3887 0.5026 0.0168  0.0441  -0.0117 106 ASP D OD2 
13574 N N   . SER D 107 ? 0.4744 0.3370 0.4802 0.0075  0.0089  -0.0242 107 SER D N   
13575 C CA  . SER D 107 ? 0.4508 0.3143 0.4672 0.0059  0.0026  -0.0264 107 SER D CA  
13576 C C   . SER D 107 ? 0.4917 0.3416 0.4924 0.0039  -0.0033 -0.0312 107 SER D C   
13577 O O   . SER D 107 ? 0.4819 0.3270 0.4832 0.0053  -0.0031 -0.0352 107 SER D O   
13578 C CB  . SER D 107 ? 0.4204 0.2937 0.4521 0.0025  -0.0033 -0.0223 107 SER D CB  
13579 O OG  . SER D 107 ? 0.4091 0.2937 0.4565 0.0042  0.0021  -0.0191 107 SER D OG  
13580 N N   . GLU D 108 ? 0.5061 0.3493 0.4921 0.0006  -0.0087 -0.0306 108 GLU D N   
13581 C CA  . GLU D 108 ? 0.5224 0.3527 0.4929 -0.0025 -0.0156 -0.0348 108 GLU D CA  
13582 C C   . GLU D 108 ? 0.5234 0.3405 0.4778 0.0013  -0.0093 -0.0405 108 GLU D C   
13583 O O   . GLU D 108 ? 0.5373 0.3454 0.4869 0.0002  -0.0127 -0.0449 108 GLU D O   
13584 C CB  . GLU D 108 ? 0.5331 0.3579 0.4881 -0.0065 -0.0219 -0.0331 108 GLU D CB  
13585 C CG  . GLU D 108 ? 0.5411 0.3765 0.5092 -0.0101 -0.0294 -0.0276 108 GLU D CG  
13586 C CD  . GLU D 108 ? 0.5468 0.3781 0.5018 -0.0142 -0.0371 -0.0250 108 GLU D CD  
13587 O OE1 . GLU D 108 ? 0.5987 0.4175 0.5323 -0.0154 -0.0384 -0.0283 108 GLU D OE1 
13588 O OE2 . GLU D 108 ? 0.5251 0.3651 0.4901 -0.0159 -0.0418 -0.0198 108 GLU D OE2 
13589 N N   . ILE D 109 ? 0.5212 0.3364 0.4662 0.0058  0.0000  -0.0404 109 ILE D N   
13590 C CA  . ILE D 109 ? 0.5523 0.3544 0.4808 0.0103  0.0068  -0.0457 109 ILE D CA  
13591 C C   . ILE D 109 ? 0.5438 0.3474 0.4853 0.0137  0.0096  -0.0483 109 ILE D C   
13592 O O   . ILE D 109 ? 0.5537 0.3442 0.4850 0.0141  0.0080  -0.0535 109 ILE D O   
13593 C CB  . ILE D 109 ? 0.5667 0.3703 0.4868 0.0152  0.0175  -0.0438 109 ILE D CB  
13594 C CG1 . ILE D 109 ? 0.5805 0.3806 0.4851 0.0115  0.0142  -0.0413 109 ILE D CG1 
13595 C CG2 . ILE D 109 ? 0.5768 0.3684 0.4821 0.0216  0.0265  -0.0490 109 ILE D CG2 
13596 C CD1 . ILE D 109 ? 0.5960 0.3984 0.4924 0.0155  0.0246  -0.0385 109 ILE D CD1 
13597 N N   . GLU D 110 ? 0.5197 0.3390 0.4835 0.0158  0.0133  -0.0444 110 GLU D N   
13598 C CA  . GLU D 110 ? 0.4918 0.3143 0.4689 0.0194  0.0164  -0.0459 110 GLU D CA  
13599 C C   . GLU D 110 ? 0.4782 0.2970 0.4606 0.0148  0.0070  -0.0481 110 GLU D C   
13600 O O   . GLU D 110 ? 0.4783 0.2892 0.4590 0.0170  0.0078  -0.0518 110 GLU D O   
13601 C CB  . GLU D 110 ? 0.4483 0.2888 0.4470 0.0217  0.0217  -0.0408 110 GLU D CB  
13602 C CG  . GLU D 110 ? 0.4322 0.2782 0.4465 0.0253  0.0245  -0.0415 110 GLU D CG  
13603 C CD  . GLU D 110 ? 0.4613 0.2968 0.4657 0.0318  0.0315  -0.0458 110 GLU D CD  
13604 O OE1 . GLU D 110 ? 0.4824 0.3082 0.4689 0.0353  0.0372  -0.0480 110 GLU D OE1 
13605 O OE2 . GLU D 110 ? 0.4570 0.2935 0.4717 0.0336  0.0310  -0.0469 110 GLU D OE2 
13606 N N   . LEU D 111 ? 0.4564 0.2812 0.4459 0.0088  -0.0017 -0.0453 111 LEU D N   
13607 C CA  . LEU D 111 ? 0.4589 0.2819 0.4542 0.0042  -0.0105 -0.0466 111 LEU D CA  
13608 C C   . LEU D 111 ? 0.4880 0.2925 0.4627 0.0020  -0.0144 -0.0520 111 LEU D C   
13609 O O   . LEU D 111 ? 0.4785 0.2766 0.4544 0.0016  -0.0164 -0.0550 111 LEU D O   
13610 C CB  . LEU D 111 ? 0.4462 0.2797 0.4519 -0.0010 -0.0182 -0.0421 111 LEU D CB  
13611 C CG  . LEU D 111 ? 0.4366 0.2720 0.4514 -0.0061 -0.0274 -0.0421 111 LEU D CG  
13612 C CD1 . LEU D 111 ? 0.4227 0.2629 0.4527 -0.0042 -0.0252 -0.0427 111 LEU D CD1 
13613 C CD2 . LEU D 111 ? 0.4228 0.2693 0.4478 -0.0097 -0.0335 -0.0372 111 LEU D CD2 
13614 N N   . LYS D 112 ? 0.5106 0.3055 0.4652 0.0009  -0.0152 -0.0533 112 LYS D N   
13615 C CA  . LYS D 112 ? 0.5774 0.3533 0.5100 -0.0016 -0.0191 -0.0587 112 LYS D CA  
13616 C C   . LYS D 112 ? 0.5991 0.3624 0.5222 0.0046  -0.0110 -0.0638 112 LYS D C   
13617 O O   . LYS D 112 ? 0.5939 0.3434 0.5083 0.0027  -0.0146 -0.0683 112 LYS D O   
13618 C CB  . LYS D 112 ? 0.6173 0.3857 0.5291 -0.0036 -0.0207 -0.0589 112 LYS D CB  
13619 C CG  . LYS D 112 ? 0.6244 0.4009 0.5409 -0.0102 -0.0308 -0.0545 112 LYS D CG  
13620 C CD  . LYS D 112 ? 0.6652 0.4325 0.5589 -0.0124 -0.0331 -0.0548 112 LYS D CD  
13621 C CE  . LYS D 112 ? 0.7002 0.4776 0.6013 -0.0179 -0.0423 -0.0494 112 LYS D CE  
13622 N NZ  . LYS D 112 ? 0.7476 0.5183 0.6284 -0.0191 -0.0435 -0.0485 112 LYS D NZ  
13623 N N   . ARG D 113 ? 0.6022 0.3698 0.5266 0.0120  0.0001  -0.0630 113 ARG D N   
13624 C CA  . ARG D 113 ? 0.6103 0.3672 0.5269 0.0190  0.0086  -0.0672 113 ARG D CA  
13625 C C   . ARG D 113 ? 0.5953 0.3526 0.5257 0.0188  0.0059  -0.0683 113 ARG D C   
13626 O O   . ARG D 113 ? 0.6609 0.4023 0.5799 0.0206  0.0068  -0.0731 113 ARG D O   
13627 C CB  . ARG D 113 ? 0.6106 0.3772 0.5328 0.0270  0.0208  -0.0647 113 ARG D CB  
13628 C CG  . ARG D 113 ? 0.6132 0.3709 0.5300 0.0355  0.0304  -0.0684 113 ARG D CG  
13629 C CD  . ARG D 113 ? 0.5923 0.3650 0.5223 0.0432  0.0419  -0.0644 113 ARG D CD  
13630 N NE  . ARG D 113 ? 0.5516 0.3428 0.5092 0.0431  0.0412  -0.0598 113 ARG D NE  
13631 C CZ  . ARG D 113 ? 0.5211 0.3125 0.4897 0.0454  0.0408  -0.0607 113 ARG D CZ  
13632 N NH1 . ARG D 113 ? 0.5413 0.3147 0.4962 0.0480  0.0412  -0.0660 113 ARG D NH1 
13633 N NH2 . ARG D 113 ? 0.4860 0.2941 0.4782 0.0447  0.0396  -0.0564 113 ARG D NH2 
13634 N N   . VAL D 114 ? 0.5562 0.3305 0.5101 0.0164  0.0025  -0.0637 114 VAL D N   
13635 C CA  . VAL D 114 ? 0.5585 0.3349 0.5265 0.0159  0.0001  -0.0639 114 VAL D CA  
13636 C C   . VAL D 114 ? 0.5967 0.3611 0.5569 0.0086  -0.0102 -0.0668 114 VAL D C   
13637 O O   . VAL D 114 ? 0.6159 0.3695 0.5733 0.0094  -0.0105 -0.0699 114 VAL D O   
13638 C CB  . VAL D 114 ? 0.5347 0.3325 0.5283 0.0151  -0.0007 -0.0581 114 VAL D CB  
13639 C CG1 . VAL D 114 ? 0.5318 0.3325 0.5398 0.0135  -0.0045 -0.0578 114 VAL D CG1 
13640 C CG2 . VAL D 114 ? 0.5368 0.3462 0.5390 0.0219  0.0093  -0.0552 114 VAL D CG2 
13641 N N   . LEU D 115 ? 0.5854 0.3522 0.5428 0.0015  -0.0187 -0.0652 115 LEU D N   
13642 C CA  . LEU D 115 ? 0.5711 0.3305 0.5247 -0.0065 -0.0293 -0.0667 115 LEU D CA  
13643 C C   . LEU D 115 ? 0.5865 0.3221 0.5150 -0.0072 -0.0301 -0.0730 115 LEU D C   
13644 O O   . LEU D 115 ? 0.5966 0.3220 0.5211 -0.0124 -0.0368 -0.0754 115 LEU D O   
13645 C CB  . LEU D 115 ? 0.5571 0.3249 0.5125 -0.0132 -0.0378 -0.0632 115 LEU D CB  
13646 C CG  . LEU D 115 ? 0.5365 0.3262 0.5160 -0.0136 -0.0387 -0.0570 115 LEU D CG  
13647 C CD1 . LEU D 115 ? 0.5304 0.3267 0.5085 -0.0183 -0.0454 -0.0536 115 LEU D CD1 
13648 C CD2 . LEU D 115 ? 0.5270 0.3233 0.5238 -0.0165 -0.0430 -0.0557 115 LEU D CD2 
13649 N N   . ASN D 116 ? 0.5922 0.3182 0.5029 -0.0021 -0.0232 -0.0758 116 ASN D N   
13650 C CA  . ASN D 116 ? 0.6238 0.3256 0.5077 -0.0024 -0.0235 -0.0823 116 ASN D CA  
13651 C C   . ASN D 116 ? 0.6204 0.3088 0.5028 0.0003  -0.0212 -0.0862 116 ASN D C   
13652 O O   . ASN D 116 ? 0.6453 0.3136 0.5094 -0.0037 -0.0261 -0.0911 116 ASN D O   
13653 C CB  . ASN D 116 ? 0.6448 0.3410 0.5117 0.0040  -0.0146 -0.0840 116 ASN D CB  
13654 C CG  . ASN D 116 ? 0.7058 0.3759 0.5422 0.0031  -0.0155 -0.0909 116 ASN D CG  
13655 O OD1 . ASN D 116 ? 0.7582 0.4195 0.5827 -0.0055 -0.0260 -0.0924 116 ASN D OD1 
13656 N ND2 . ASN D 116 ? 0.7081 0.3655 0.5320 0.0117  -0.0052 -0.0950 116 ASN D ND2 
13657 N N   . TYR D 117 ? 0.5807 0.2792 0.4808 0.0072  -0.0138 -0.0841 117 TYR D N   
13658 C CA  . TYR D 117 ? 0.5912 0.2790 0.4927 0.0099  -0.0120 -0.0867 117 TYR D CA  
13659 C C   . TYR D 117 ? 0.5758 0.2770 0.5004 0.0047  -0.0186 -0.0826 117 TYR D C   
13660 O O   . TYR D 117 ? 0.5673 0.2572 0.4900 0.0014  -0.0229 -0.0846 117 TYR D O   
13661 C CB  . TYR D 117 ? 0.5880 0.2748 0.4912 0.0216  0.0006  -0.0875 117 TYR D CB  
13662 C CG  . TYR D 117 ? 0.5666 0.2781 0.4934 0.0267  0.0069  -0.0815 117 TYR D CG  
13663 C CD1 . TYR D 117 ? 0.5420 0.2677 0.4921 0.0264  0.0054  -0.0776 117 TYR D CD1 
13664 C CD2 . TYR D 117 ? 0.5729 0.2933 0.4982 0.0312  0.0139  -0.0797 117 TYR D CD2 
13665 C CE1 . TYR D 117 ? 0.5252 0.2725 0.4957 0.0302  0.0104  -0.0723 117 TYR D CE1 
13666 C CE2 . TYR D 117 ? 0.5377 0.2800 0.4841 0.0350  0.0191  -0.0743 117 TYR D CE2 
13667 C CZ  . TYR D 117 ? 0.5290 0.2844 0.4978 0.0344  0.0171  -0.0707 117 TYR D CZ  
13668 O OH  . TYR D 117 ? 0.5508 0.3275 0.5401 0.0371  0.0212  -0.0653 117 TYR D OH  
13669 N N   . ALA D 118 ? 0.5398 0.2642 0.4853 0.0038  -0.0192 -0.0768 118 ALA D N   
13670 C CA  . ALA D 118 ? 0.5287 0.2671 0.4963 -0.0001 -0.0241 -0.0727 118 ALA D CA  
13671 C C   . ALA D 118 ? 0.5415 0.2730 0.5056 -0.0102 -0.0354 -0.0734 118 ALA D C   
13672 O O   . ALA D 118 ? 0.5171 0.2510 0.4928 -0.0131 -0.0388 -0.0720 118 ALA D O   
13673 C CB  . ALA D 118 ? 0.4942 0.2561 0.4813 0.0004  -0.0230 -0.0670 118 ALA D CB  
13674 N N   . LYS D 119 ? 0.5721 0.2951 0.5200 -0.0158 -0.0414 -0.0754 119 LYS D N   
13675 C CA  . LYS D 119 ? 0.6009 0.3201 0.5469 -0.0261 -0.0529 -0.0752 119 LYS D CA  
13676 C C   . LYS D 119 ? 0.6168 0.3167 0.5532 -0.0289 -0.0555 -0.0792 119 LYS D C   
13677 O O   . LYS D 119 ? 0.6340 0.3315 0.5710 -0.0379 -0.0649 -0.0786 119 LYS D O   
13678 C CB  . LYS D 119 ? 0.6104 0.3247 0.5401 -0.0314 -0.0591 -0.0763 119 LYS D CB  
13679 C CG  . LYS D 119 ? 0.6600 0.3500 0.5609 -0.0302 -0.0573 -0.0828 119 LYS D CG  
13680 C CD  . LYS D 119 ? 0.7020 0.3871 0.5850 -0.0343 -0.0622 -0.0837 119 LYS D CD  
13681 C CE  . LYS D 119 ? 0.7736 0.4322 0.6271 -0.0323 -0.0593 -0.0910 119 LYS D CE  
13682 N NZ  . LYS D 119 ? 0.8189 0.4718 0.6527 -0.0313 -0.0580 -0.0926 119 LYS D NZ  
13683 N N   . LYS D 120 ? 0.6400 0.3262 0.5677 -0.0214 -0.0474 -0.0830 120 LYS D N   
13684 C CA  . LYS D 120 ? 0.6562 0.3209 0.5720 -0.0234 -0.0494 -0.0872 120 LYS D CA  
13685 C C   . LYS D 120 ? 0.6310 0.3034 0.5665 -0.0221 -0.0480 -0.0840 120 LYS D C   
13686 O O   . LYS D 120 ? 0.6698 0.3262 0.5988 -0.0250 -0.0508 -0.0862 120 LYS D O   
13687 C CB  . LYS D 120 ? 0.6843 0.3267 0.5774 -0.0155 -0.0413 -0.0933 120 LYS D CB  
13688 C CG  . LYS D 120 ? 0.7223 0.3533 0.5918 -0.0160 -0.0415 -0.0973 120 LYS D CG  
13689 C CD  . LYS D 120 ? 0.7694 0.3763 0.6149 -0.0081 -0.0333 -0.1039 120 LYS D CD  
13690 C CE  . LYS D 120 ? 0.7822 0.3994 0.6372 0.0044  -0.0204 -0.1023 120 LYS D CE  
13691 N NZ  . LYS D 120 ? 0.8249 0.4201 0.6567 0.0128  -0.0118 -0.1083 120 LYS D NZ  
13692 N N   . TYR D 121 ? 0.5714 0.2672 0.5298 -0.0182 -0.0442 -0.0787 121 TYR D N   
13693 C CA  . TYR D 121 ? 0.5444 0.2495 0.5218 -0.0164 -0.0425 -0.0752 121 TYR D CA  
13694 C C   . TYR D 121 ? 0.5174 0.2415 0.5139 -0.0242 -0.0499 -0.0699 121 TYR D C   
13695 O O   . TYR D 121 ? 0.5157 0.2594 0.5263 -0.0227 -0.0486 -0.0661 121 TYR D O   
13696 C CB  . TYR D 121 ? 0.5374 0.2507 0.5222 -0.0050 -0.0315 -0.0742 121 TYR D CB  
13697 C CG  . TYR D 121 ? 0.5668 0.2609 0.5318 0.0027  -0.0242 -0.0794 121 TYR D CG  
13698 C CD1 . TYR D 121 ? 0.6162 0.2921 0.5730 0.0063  -0.0215 -0.0824 121 TYR D CD1 
13699 C CD2 . TYR D 121 ? 0.5878 0.2803 0.5406 0.0061  -0.0201 -0.0815 121 TYR D CD2 
13700 C CE1 . TYR D 121 ? 0.6268 0.2835 0.5641 0.0138  -0.0146 -0.0874 121 TYR D CE1 
13701 C CE2 . TYR D 121 ? 0.6171 0.2914 0.5504 0.0132  -0.0131 -0.0864 121 TYR D CE2 
13702 C CZ  . TYR D 121 ? 0.6317 0.2881 0.5572 0.0173  -0.0102 -0.0896 121 TYR D CZ  
13703 O OH  . TYR D 121 ? 0.6562 0.2947 0.5622 0.0251  -0.0027 -0.0945 121 TYR D OH  
13704 N N   . ASP D 122 ? 0.5242 0.2429 0.5224 -0.0320 -0.0570 -0.0692 122 ASP D N   
13705 C CA  . ASP D 122 ? 0.5104 0.2463 0.5258 -0.0396 -0.0641 -0.0641 122 ASP D CA  
13706 C C   . ASP D 122 ? 0.5221 0.2731 0.5585 -0.0361 -0.0602 -0.0597 122 ASP D C   
13707 O O   . ASP D 122 ? 0.5062 0.2722 0.5582 -0.0412 -0.0646 -0.0553 122 ASP D O   
13708 C CB  . ASP D 122 ? 0.5204 0.2456 0.5289 -0.0505 -0.0739 -0.0648 122 ASP D CB  
13709 C CG  . ASP D 122 ? 0.5330 0.2421 0.5373 -0.0522 -0.0742 -0.0662 122 ASP D CG  
13710 O OD1 . ASP D 122 ? 0.5285 0.2340 0.5351 -0.0444 -0.0668 -0.0667 122 ASP D OD1 
13711 O OD2 . ASP D 122 ? 0.5520 0.2527 0.5516 -0.0617 -0.0823 -0.0663 122 ASP D OD2 
13712 N N   . CYS D 123 ? 0.5255 0.2733 0.5626 -0.0272 -0.0519 -0.0607 123 CYS D N   
13713 C CA  . CYS D 123 ? 0.5058 0.2710 0.5626 -0.0227 -0.0475 -0.0563 123 CYS D CA  
13714 C C   . CYS D 123 ? 0.4915 0.2780 0.5612 -0.0216 -0.0466 -0.0530 123 CYS D C   
13715 O O   . CYS D 123 ? 0.4981 0.3007 0.5849 -0.0204 -0.0453 -0.0490 123 CYS D O   
13716 C CB  . CYS D 123 ? 0.5195 0.2785 0.5748 -0.0131 -0.0391 -0.0576 123 CYS D CB  
13717 S SG  . CYS D 123 ? 0.5330 0.2955 0.5834 -0.0034 -0.0304 -0.0594 123 CYS D SG  
13718 N N   . ILE D 124 ? 0.4878 0.2741 0.5487 -0.0216 -0.0470 -0.0547 124 ILE D N   
13719 C CA  . ILE D 124 ? 0.4728 0.2776 0.5451 -0.0208 -0.0465 -0.0514 124 ILE D CA  
13720 C C   . ILE D 124 ? 0.4671 0.2821 0.5485 -0.0288 -0.0546 -0.0481 124 ILE D C   
13721 O O   . ILE D 124 ? 0.4863 0.2931 0.5576 -0.0350 -0.0610 -0.0495 124 ILE D O   
13722 C CB  . ILE D 124 ? 0.4847 0.2855 0.5441 -0.0178 -0.0439 -0.0537 124 ILE D CB  
13723 C CG1 . ILE D 124 ? 0.4965 0.2898 0.5489 -0.0092 -0.0349 -0.0563 124 ILE D CG1 
13724 C CG2 . ILE D 124 ? 0.4581 0.2766 0.5283 -0.0182 -0.0446 -0.0500 124 ILE D CG2 
13725 C CD1 . ILE D 124 ? 0.5061 0.2922 0.5428 -0.0062 -0.0317 -0.0591 124 ILE D CD1 
13726 N N   . ILE D 125 ? 0.4356 0.2684 0.5355 -0.0284 -0.0541 -0.0437 125 ILE D N   
13727 C CA  . ILE D 125 ? 0.4203 0.2645 0.5310 -0.0349 -0.0607 -0.0401 125 ILE D CA  
13728 C C   . ILE D 125 ? 0.4161 0.2759 0.5358 -0.0334 -0.0604 -0.0371 125 ILE D C   
13729 O O   . ILE D 125 ? 0.4202 0.2895 0.5477 -0.0381 -0.0658 -0.0341 125 ILE D O   
13730 C CB  . ILE D 125 ? 0.3930 0.2430 0.5167 -0.0368 -0.0612 -0.0372 125 ILE D CB  
13731 C CG1 . ILE D 125 ? 0.3635 0.2230 0.4987 -0.0303 -0.0544 -0.0355 125 ILE D CG1 
13732 C CG2 . ILE D 125 ? 0.4092 0.2425 0.5232 -0.0404 -0.0635 -0.0396 125 ILE D CG2 
13733 C CD1 . ILE D 125 ? 0.3334 0.2022 0.4826 -0.0323 -0.0551 -0.0319 125 ILE D CD1 
13734 N N   . THR D 126 ? 0.3998 0.2628 0.5194 -0.0270 -0.0542 -0.0376 126 THR D N   
13735 C CA  . THR D 126 ? 0.3917 0.2665 0.5169 -0.0258 -0.0540 -0.0351 126 THR D CA  
13736 C C   . THR D 126 ? 0.4266 0.2982 0.5444 -0.0198 -0.0476 -0.0369 126 THR D C   
13737 O O   . THR D 126 ? 0.4233 0.2897 0.5388 -0.0153 -0.0419 -0.0388 126 THR D O   
13738 C CB  . THR D 126 ? 0.3594 0.2498 0.5026 -0.0249 -0.0531 -0.0312 126 THR D CB  
13739 O OG1 . THR D 126 ? 0.3457 0.2410 0.4965 -0.0302 -0.0586 -0.0290 126 THR D OG1 
13740 C CG2 . THR D 126 ? 0.3441 0.2450 0.4928 -0.0227 -0.0521 -0.0289 126 THR D CG2 
13741 N N   . TYR D 127 ? 0.4027 0.2779 0.5173 -0.0199 -0.0486 -0.0358 127 TYR D N   
13742 C CA  . TYR D 127 ? 0.4118 0.2873 0.5217 -0.0150 -0.0427 -0.0362 127 TYR D CA  
13743 C C   . TYR D 127 ? 0.4018 0.2916 0.5249 -0.0137 -0.0416 -0.0323 127 TYR D C   
13744 O O   . TYR D 127 ? 0.4203 0.3170 0.5493 -0.0168 -0.0467 -0.0297 127 TYR D O   
13745 C CB  . TYR D 127 ? 0.4226 0.2895 0.5162 -0.0161 -0.0443 -0.0378 127 TYR D CB  
13746 C CG  . TYR D 127 ? 0.4304 0.2803 0.5064 -0.0162 -0.0437 -0.0425 127 TYR D CG  
13747 C CD1 . TYR D 127 ? 0.4170 0.2579 0.4857 -0.0219 -0.0506 -0.0443 127 TYR D CD1 
13748 C CD2 . TYR D 127 ? 0.4336 0.2764 0.5002 -0.0105 -0.0362 -0.0450 127 TYR D CD2 
13749 C CE1 . TYR D 127 ? 0.4425 0.2658 0.4934 -0.0221 -0.0504 -0.0490 127 TYR D CE1 
13750 C CE2 . TYR D 127 ? 0.4599 0.2858 0.5095 -0.0098 -0.0351 -0.0496 127 TYR D CE2 
13751 C CZ  . TYR D 127 ? 0.4670 0.2823 0.5081 -0.0157 -0.0423 -0.0518 127 TYR D CZ  
13752 O OH  . TYR D 127 ? 0.5021 0.2987 0.5248 -0.0152 -0.0414 -0.0567 127 TYR D OH  
13753 N N   . LEU D 128 ? 0.3765 0.2705 0.5037 -0.0090 -0.0350 -0.0319 128 LEU D N   
13754 C CA  . LEU D 128 ? 0.3640 0.2692 0.5012 -0.0077 -0.0334 -0.0286 128 LEU D CA  
13755 C C   . LEU D 128 ? 0.3751 0.2780 0.5036 -0.0056 -0.0299 -0.0285 128 LEU D C   
13756 O O   . LEU D 128 ? 0.3956 0.2943 0.5184 -0.0022 -0.0243 -0.0301 128 LEU D O   
13757 C CB  . LEU D 128 ? 0.3462 0.2587 0.4955 -0.0049 -0.0291 -0.0277 128 LEU D CB  
13758 C CG  . LEU D 128 ? 0.3403 0.2546 0.4976 -0.0064 -0.0316 -0.0277 128 LEU D CG  
13759 C CD1 . LEU D 128 ? 0.3436 0.2644 0.5105 -0.0033 -0.0271 -0.0267 128 LEU D CD1 
13760 C CD2 . LEU D 128 ? 0.3412 0.2612 0.5047 -0.0101 -0.0373 -0.0255 128 LEU D CD2 
13761 N N   . VAL D 129 ? 0.3803 0.2863 0.5080 -0.0074 -0.0330 -0.0261 129 VAL D N   
13762 C CA  . VAL D 129 ? 0.3817 0.2829 0.4972 -0.0067 -0.0312 -0.0261 129 VAL D CA  
13763 C C   . VAL D 129 ? 0.3924 0.3002 0.5132 -0.0039 -0.0256 -0.0236 129 VAL D C   
13764 O O   . VAL D 129 ? 0.4070 0.3115 0.5186 -0.0026 -0.0221 -0.0234 129 VAL D O   
13765 C CB  . VAL D 129 ? 0.3887 0.2881 0.4985 -0.0104 -0.0383 -0.0247 129 VAL D CB  
13766 C CG1 . VAL D 129 ? 0.3910 0.3001 0.5115 -0.0109 -0.0406 -0.0205 129 VAL D CG1 
13767 C CG2 . VAL D 129 ? 0.4158 0.3059 0.5081 -0.0105 -0.0377 -0.0261 129 VAL D CG2 
13768 N N   . ILE D 130 ? 0.3667 0.2835 0.5018 -0.0033 -0.0246 -0.0216 130 ILE D N   
13769 C CA  . ILE D 130 ? 0.3749 0.2974 0.5153 -0.0014 -0.0196 -0.0195 130 ILE D CA  
13770 C C   . ILE D 130 ? 0.3739 0.3042 0.5286 -0.0009 -0.0189 -0.0187 130 ILE D C   
13771 O O   . ILE D 130 ? 0.3712 0.3036 0.5322 -0.0024 -0.0230 -0.0187 130 ILE D O   
13772 C CB  . ILE D 130 ? 0.4171 0.3408 0.5552 -0.0028 -0.0213 -0.0163 130 ILE D CB  
13773 C CG1 . ILE D 130 ? 0.4024 0.3305 0.5438 -0.0016 -0.0159 -0.0138 130 ILE D CG1 
13774 C CG2 . ILE D 130 ? 0.4099 0.3376 0.5560 -0.0047 -0.0271 -0.0145 130 ILE D CG2 
13775 C CD1 . ILE D 130 ? 0.4093 0.3363 0.5459 -0.0029 -0.0169 -0.0106 130 ILE D CD1 
13776 N N   . ASN D 131 ? 0.3917 0.3266 0.5512 0.0008  -0.0137 -0.0176 131 ASN D N   
13777 C CA  . ASN D 131 ? 0.3685 0.3105 0.5401 0.0013  -0.0124 -0.0168 131 ASN D CA  
13778 C C   . ASN D 131 ? 0.3444 0.2918 0.5221 0.0001  -0.0118 -0.0139 131 ASN D C   
13779 O O   . ASN D 131 ? 0.3649 0.3148 0.5428 0.0006  -0.0077 -0.0123 131 ASN D O   
13780 C CB  . ASN D 131 ? 0.3430 0.2863 0.5159 0.0042  -0.0072 -0.0178 131 ASN D CB  
13781 C CG  . ASN D 131 ? 0.3449 0.2952 0.5295 0.0045  -0.0068 -0.0171 131 ASN D CG  
13782 O OD1 . ASN D 131 ? 0.4007 0.3517 0.5900 0.0033  -0.0105 -0.0176 131 ASN D OD1 
13783 N ND2 . ASN D 131 ? 0.3777 0.3338 0.5675 0.0060  -0.0026 -0.0156 131 ASN D ND2 
13784 N N   . GLU D 132 ? 0.3548 0.3039 0.5377 -0.0013 -0.0157 -0.0130 132 GLU D N   
13785 C CA  . GLU D 132 ? 0.3761 0.3296 0.5663 -0.0023 -0.0152 -0.0110 132 GLU D CA  
13786 C C   . GLU D 132 ? 0.3559 0.3077 0.5420 -0.0033 -0.0145 -0.0084 132 GLU D C   
13787 O O   . GLU D 132 ? 0.3603 0.3147 0.5490 -0.0042 -0.0115 -0.0067 132 GLU D O   
13788 C CB  . GLU D 132 ? 0.3722 0.3309 0.5690 -0.0017 -0.0117 -0.0111 132 GLU D CB  
13789 C CG  . GLU D 132 ? 0.3703 0.3328 0.5754 -0.0030 -0.0131 -0.0103 132 GLU D CG  
13790 C CD  . GLU D 132 ? 0.3906 0.3528 0.5986 -0.0026 -0.0165 -0.0118 132 GLU D CD  
13791 O OE1 . GLU D 132 ? 0.3627 0.3267 0.5735 -0.0017 -0.0163 -0.0132 132 GLU D OE1 
13792 O OE2 . GLU D 132 ? 0.3207 0.2810 0.5281 -0.0031 -0.0193 -0.0112 132 GLU D OE2 
13793 N N   . PRO D 133 ? 0.3504 0.2979 0.5302 -0.0037 -0.0174 -0.0075 133 PRO D N   
13794 C CA  . PRO D 133 ? 0.3531 0.2984 0.5294 -0.0048 -0.0172 -0.0045 133 PRO D CA  
13795 C C   . PRO D 133 ? 0.3390 0.2859 0.5228 -0.0056 -0.0181 -0.0031 133 PRO D C   
13796 O O   . PRO D 133 ? 0.3276 0.2753 0.5161 -0.0049 -0.0211 -0.0039 133 PRO D O   
13797 C CB  . PRO D 133 ? 0.3541 0.2949 0.5228 -0.0047 -0.0213 -0.0040 133 PRO D CB  
13798 C CG  . PRO D 133 ? 0.3473 0.2896 0.5201 -0.0042 -0.0249 -0.0062 133 PRO D CG  
13799 C CD  . PRO D 133 ? 0.3641 0.3088 0.5403 -0.0036 -0.0216 -0.0089 133 PRO D CD  
13800 N N   . GLN D 134 ? 0.3848 0.3320 0.5694 -0.0071 -0.0153 -0.0010 134 GLN D N   
13801 C CA  . GLN D 134 ? 0.3777 0.3247 0.5677 -0.0084 -0.0160 0.0001  134 GLN D CA  
13802 C C   . GLN D 134 ? 0.3228 0.2640 0.5092 -0.0083 -0.0187 0.0024  134 GLN D C   
13803 O O   . GLN D 134 ? 0.2864 0.2244 0.4659 -0.0085 -0.0187 0.0046  134 GLN D O   
13804 C CB  . GLN D 134 ? 0.4678 0.4174 0.6597 -0.0109 -0.0122 0.0018  134 GLN D CB  
13805 C CG  . GLN D 134 ? 0.5059 0.4622 0.7038 -0.0108 -0.0098 0.0001  134 GLN D CG  
13806 C CD  . GLN D 134 ? 0.5767 0.5347 0.7815 -0.0110 -0.0120 -0.0016 134 GLN D CD  
13807 O OE1 . GLN D 134 ? 0.5730 0.5270 0.7783 -0.0116 -0.0144 -0.0015 134 GLN D OE1 
13808 N NE2 . GLN D 134 ? 0.5857 0.5490 0.7949 -0.0102 -0.0108 -0.0033 134 GLN D NE2 
13809 N N   . THR D 135 ? 0.3104 0.2500 0.5012 -0.0077 -0.0208 0.0021  135 THR D N   
13810 C CA  . THR D 135 ? 0.3262 0.2601 0.5147 -0.0066 -0.0232 0.0044  135 THR D CA  
13811 C C   . THR D 135 ? 0.3288 0.2577 0.5114 -0.0086 -0.0220 0.0078  135 THR D C   
13812 O O   . THR D 135 ? 0.3379 0.2629 0.5149 -0.0076 -0.0238 0.0103  135 THR D O   
13813 C CB  . THR D 135 ? 0.3275 0.2595 0.5212 -0.0059 -0.0239 0.0034  135 THR D CB  
13814 O OG1 . THR D 135 ? 0.3004 0.2382 0.4995 -0.0048 -0.0240 0.0003  135 THR D OG1 
13815 C CG2 . THR D 135 ? 0.3214 0.2479 0.5136 -0.0031 -0.0264 0.0053  135 THR D CG2 
13816 N N   . ASP D 136 ? 0.3489 0.2780 0.5326 -0.0118 -0.0190 0.0085  136 ASP D N   
13817 C CA  . ASP D 136 ? 0.3440 0.2679 0.5227 -0.0144 -0.0178 0.0123  136 ASP D CA  
13818 C C   . ASP D 136 ? 0.3424 0.2674 0.5142 -0.0146 -0.0162 0.0142  136 ASP D C   
13819 O O   . ASP D 136 ? 0.3791 0.2987 0.5443 -0.0151 -0.0166 0.0177  136 ASP D O   
13820 C CB  . ASP D 136 ? 0.3489 0.2740 0.5312 -0.0186 -0.0153 0.0130  136 ASP D CB  
13821 C CG  . ASP D 136 ? 0.3874 0.3058 0.5650 -0.0219 -0.0145 0.0172  136 ASP D CG  
13822 O OD1 . ASP D 136 ? 0.3740 0.2839 0.5500 -0.0215 -0.0169 0.0180  136 ASP D OD1 
13823 O OD2 . ASP D 136 ? 0.3831 0.3046 0.5586 -0.0246 -0.0113 0.0198  136 ASP D OD2 
13824 N N   . HIS D 137 ? 0.3254 0.2566 0.4977 -0.0138 -0.0143 0.0119  137 HIS D N   
13825 C CA  . HIS D 137 ? 0.3215 0.2531 0.4861 -0.0136 -0.0121 0.0130  137 HIS D CA  
13826 C C   . HIS D 137 ? 0.3184 0.2453 0.4758 -0.0115 -0.0161 0.0136  137 HIS D C   
13827 O O   . HIS D 137 ? 0.3438 0.2667 0.4926 -0.0120 -0.0158 0.0165  137 HIS D O   
13828 C CB  . HIS D 137 ? 0.3196 0.2577 0.4863 -0.0127 -0.0090 0.0101  137 HIS D CB  
13829 C CG  . HIS D 137 ? 0.3240 0.2613 0.4814 -0.0119 -0.0064 0.0106  137 HIS D CG  
13830 N ND1 . HIS D 137 ? 0.3386 0.2754 0.4911 -0.0138 -0.0024 0.0141  137 HIS D ND1 
13831 C CD2 . HIS D 137 ? 0.3458 0.2817 0.4968 -0.0097 -0.0071 0.0082  137 HIS D CD2 
13832 C CE1 . HIS D 137 ? 0.3555 0.2909 0.4985 -0.0122 -0.0004 0.0135  137 HIS D CE1 
13833 N NE2 . HIS D 137 ? 0.3481 0.2824 0.4897 -0.0098 -0.0033 0.0097  137 HIS D NE2 
13834 N N   . ILE D 138 ? 0.3198 0.2476 0.4810 -0.0092 -0.0199 0.0112  138 ILE D N   
13835 C CA  . ILE D 138 ? 0.3330 0.2579 0.4891 -0.0074 -0.0245 0.0121  138 ILE D CA  
13836 C C   . ILE D 138 ? 0.3451 0.2639 0.4979 -0.0074 -0.0265 0.0164  138 ILE D C   
13837 O O   . ILE D 138 ? 0.3965 0.3118 0.5408 -0.0073 -0.0283 0.0191  138 ILE D O   
13838 C CB  . ILE D 138 ? 0.3178 0.2462 0.4806 -0.0054 -0.0281 0.0093  138 ILE D CB  
13839 C CG1 . ILE D 138 ? 0.3068 0.2396 0.4713 -0.0055 -0.0264 0.0053  138 ILE D CG1 
13840 C CG2 . ILE D 138 ? 0.3289 0.2555 0.4879 -0.0039 -0.0333 0.0111  138 ILE D CG2 
13841 C CD1 . ILE D 138 ? 0.3014 0.2373 0.4708 -0.0042 -0.0301 0.0031  138 ILE D CD1 
13842 N N   . HIS D 139 ? 0.3371 0.2538 0.4957 -0.0075 -0.0262 0.0173  139 HIS D N   
13843 C CA  . HIS D 139 ? 0.3483 0.2577 0.5036 -0.0073 -0.0277 0.0215  139 HIS D CA  
13844 C C   . HIS D 139 ? 0.3417 0.2477 0.4881 -0.0100 -0.0252 0.0249  139 HIS D C   
13845 O O   . HIS D 139 ? 0.3264 0.2271 0.4659 -0.0094 -0.0273 0.0287  139 HIS D O   
13846 C CB  . HIS D 139 ? 0.3693 0.2754 0.5307 -0.0078 -0.0267 0.0212  139 HIS D CB  
13847 C CG  . HIS D 139 ? 0.3919 0.2887 0.5494 -0.0076 -0.0279 0.0253  139 HIS D CG  
13848 N ND1 . HIS D 139 ? 0.4087 0.3002 0.5615 -0.0114 -0.0255 0.0285  139 HIS D ND1 
13849 C CD2 . HIS D 139 ? 0.4101 0.3018 0.5679 -0.0038 -0.0312 0.0270  139 HIS D CD2 
13850 C CE1 . HIS D 139 ? 0.4233 0.3054 0.5730 -0.0101 -0.0274 0.0318  139 HIS D CE1 
13851 N NE2 . HIS D 139 ? 0.4228 0.3049 0.5755 -0.0051 -0.0308 0.0310  139 HIS D NE2 
13852 N N   . SER D 140 ? 0.3521 0.2618 0.4990 -0.0129 -0.0205 0.0239  140 SER D N   
13853 C CA  . SER D 140 ? 0.3750 0.2826 0.5147 -0.0158 -0.0170 0.0275  140 SER D CA  
13854 C C   . SER D 140 ? 0.4082 0.3149 0.5370 -0.0147 -0.0175 0.0285  140 SER D C   
13855 O O   . SER D 140 ? 0.4758 0.3770 0.5962 -0.0154 -0.0181 0.0328  140 SER D O   
13856 C CB  . SER D 140 ? 0.3735 0.2869 0.5180 -0.0188 -0.0118 0.0266  140 SER D CB  
13857 O OG  . SER D 140 ? 0.4064 0.3184 0.5448 -0.0217 -0.0080 0.0308  140 SER D OG  
13858 N N   . VAL D 141 ? 0.4000 0.3112 0.5280 -0.0130 -0.0178 0.0247  141 VAL D N   
13859 C CA  . VAL D 141 ? 0.3996 0.3087 0.5158 -0.0122 -0.0187 0.0250  141 VAL D CA  
13860 C C   . VAL D 141 ? 0.3971 0.3034 0.5103 -0.0102 -0.0257 0.0255  141 VAL D C   
13861 O O   . VAL D 141 ? 0.3763 0.2804 0.4791 -0.0100 -0.0276 0.0257  141 VAL D O   
13862 C CB  . VAL D 141 ? 0.4096 0.3233 0.5249 -0.0116 -0.0153 0.0205  141 VAL D CB  
13863 C CG1 . VAL D 141 ? 0.4098 0.3279 0.5289 -0.0132 -0.0083 0.0209  141 VAL D CG1 
13864 C CG2 . VAL D 141 ? 0.3817 0.2991 0.5048 -0.0098 -0.0185 0.0160  141 VAL D CG2 
13865 N N   . THR D 142 ? 0.3856 0.2922 0.5080 -0.0087 -0.0294 0.0257  142 THR D N   
13866 C CA  . THR D 142 ? 0.3794 0.2852 0.5027 -0.0063 -0.0359 0.0270  142 THR D CA  
13867 C C   . THR D 142 ? 0.3932 0.3048 0.5215 -0.0052 -0.0385 0.0226  142 THR D C   
13868 O O   . THR D 142 ? 0.3696 0.2830 0.4939 -0.0063 -0.0368 0.0194  142 THR D O   
13869 C CB  . THR D 142 ? 0.3734 0.2744 0.4853 -0.0062 -0.0395 0.0313  142 THR D CB  
13870 O OG1 . THR D 142 ? 0.3704 0.2722 0.4730 -0.0072 -0.0403 0.0292  142 THR D OG1 
13871 C CG2 . THR D 142 ? 0.3724 0.2672 0.4773 -0.0078 -0.0365 0.0359  142 THR D CG2 
13872 N N   . GLY D 143 ? 0.3792 0.2933 0.5161 -0.0029 -0.0425 0.0229  143 GLY D N   
13873 C CA  . GLY D 143 ? 0.3737 0.2936 0.5158 -0.0021 -0.0458 0.0199  143 GLY D CA  
13874 C C   . GLY D 143 ? 0.3886 0.3080 0.5218 -0.0031 -0.0506 0.0205  143 GLY D C   
13875 O O   . GLY D 143 ? 0.3881 0.3106 0.5216 -0.0042 -0.0523 0.0172  143 GLY D O   
13876 N N   . LYS D 144 ? 0.3855 0.3006 0.5102 -0.0031 -0.0534 0.0248  144 LYS D N   
13877 C CA  . LYS D 144 ? 0.4136 0.3273 0.5274 -0.0047 -0.0579 0.0253  144 LYS D CA  
13878 C C   . LYS D 144 ? 0.4221 0.3335 0.5269 -0.0070 -0.0541 0.0209  144 LYS D C   
13879 O O   . LYS D 144 ? 0.4103 0.3227 0.5123 -0.0084 -0.0570 0.0179  144 LYS D O   
13880 C CB  . LYS D 144 ? 0.4478 0.3558 0.5508 -0.0047 -0.0601 0.0306  144 LYS D CB  
13881 C CG  . LYS D 144 ? 0.4779 0.3857 0.5720 -0.0059 -0.0673 0.0320  144 LYS D CG  
13882 C CD  . LYS D 144 ? 0.5250 0.4265 0.6060 -0.0063 -0.0691 0.0371  144 LYS D CD  
13883 C CE  . LYS D 144 ? 0.5828 0.4843 0.6546 -0.0079 -0.0772 0.0388  144 LYS D CE  
13884 N NZ  . LYS D 144 ? 0.5826 0.4858 0.6516 -0.0105 -0.0792 0.0335  144 LYS D NZ  
13885 N N   . ALA D 145 ? 0.3972 0.3053 0.4977 -0.0075 -0.0474 0.0207  145 ALA D N   
13886 C CA  . ALA D 145 ? 0.3927 0.2982 0.4835 -0.0089 -0.0429 0.0174  145 ALA D CA  
13887 C C   . ALA D 145 ? 0.4057 0.3150 0.5032 -0.0088 -0.0421 0.0121  145 ALA D C   
13888 O O   . ALA D 145 ? 0.3814 0.2878 0.4700 -0.0097 -0.0423 0.0088  145 ALA D O   
13889 C CB  . ALA D 145 ? 0.3910 0.2949 0.4798 -0.0092 -0.0355 0.0189  145 ALA D CB  
13890 N N   . PHE D 146 ? 0.4047 0.3193 0.5168 -0.0077 -0.0412 0.0114  146 PHE D N   
13891 C CA  . PHE D 146 ? 0.3993 0.3179 0.5192 -0.0074 -0.0404 0.0070  146 PHE D CA  
13892 C C   . PHE D 146 ? 0.4086 0.3278 0.5272 -0.0084 -0.0470 0.0056  146 PHE D C   
13893 O O   . PHE D 146 ? 0.4460 0.3636 0.5606 -0.0094 -0.0468 0.0018  146 PHE D O   
13894 C CB  . PHE D 146 ? 0.3802 0.3039 0.5147 -0.0062 -0.0387 0.0072  146 PHE D CB  
13895 C CG  . PHE D 146 ? 0.3799 0.3081 0.5228 -0.0060 -0.0392 0.0035  146 PHE D CG  
13896 C CD1 . PHE D 146 ? 0.3805 0.3090 0.5233 -0.0061 -0.0346 0.0000  146 PHE D CD1 
13897 C CD2 . PHE D 146 ? 0.3723 0.3044 0.5229 -0.0055 -0.0441 0.0038  146 PHE D CD2 
13898 C CE1 . PHE D 146 ? 0.3576 0.2891 0.5069 -0.0060 -0.0353 -0.0030 146 PHE D CE1 
13899 C CE2 . PHE D 146 ? 0.3658 0.3017 0.5233 -0.0057 -0.0443 0.0008  146 PHE D CE2 
13900 C CZ  . PHE D 146 ? 0.3608 0.2958 0.5171 -0.0061 -0.0401 -0.0027 146 PHE D CZ  
13901 N N   . VAL D 147 ? 0.3988 0.3203 0.5209 -0.0082 -0.0529 0.0089  147 VAL D N   
13902 C CA  . VAL D 147 ? 0.4027 0.3268 0.5261 -0.0096 -0.0597 0.0084  147 VAL D CA  
13903 C C   . VAL D 147 ? 0.4157 0.3333 0.5230 -0.0122 -0.0626 0.0072  147 VAL D C   
13904 O O   . VAL D 147 ? 0.4189 0.3355 0.5235 -0.0144 -0.0656 0.0042  147 VAL D O   
13905 C CB  . VAL D 147 ? 0.3942 0.3235 0.5261 -0.0081 -0.0651 0.0130  147 VAL D CB  
13906 C CG1 . VAL D 147 ? 0.4006 0.3333 0.5324 -0.0102 -0.0730 0.0139  147 VAL D CG1 
13907 C CG2 . VAL D 147 ? 0.3752 0.3101 0.5221 -0.0054 -0.0623 0.0132  147 VAL D CG2 
13908 N N   . ASP D 148 ? 0.4176 0.3298 0.5132 -0.0122 -0.0617 0.0096  148 ASP D N   
13909 C CA  . ASP D 148 ? 0.4199 0.3246 0.4980 -0.0145 -0.0636 0.0081  148 ASP D CA  
13910 C C   . ASP D 148 ? 0.4107 0.3110 0.4830 -0.0149 -0.0583 0.0023  148 ASP D C   
13911 O O   . ASP D 148 ? 0.4042 0.2992 0.4665 -0.0171 -0.0615 -0.0007 148 ASP D O   
13912 C CB  . ASP D 148 ? 0.4207 0.3204 0.4866 -0.0143 -0.0628 0.0118  148 ASP D CB  
13913 C CG  . ASP D 148 ? 0.4285 0.3310 0.4972 -0.0140 -0.0697 0.0176  148 ASP D CG  
13914 O OD1 . ASP D 148 ? 0.4128 0.3214 0.4920 -0.0142 -0.0754 0.0184  148 ASP D OD1 
13915 O OD2 . ASP D 148 ? 0.4484 0.3472 0.5096 -0.0134 -0.0689 0.0217  148 ASP D OD2 
13916 N N   . LEU D 149 ? 0.4012 0.3030 0.4793 -0.0127 -0.0504 0.0011  149 LEU D N   
13917 C CA  . LEU D 149 ? 0.4119 0.3102 0.4855 -0.0121 -0.0447 -0.0037 149 LEU D CA  
13918 C C   . LEU D 149 ? 0.4180 0.3177 0.4981 -0.0132 -0.0483 -0.0072 149 LEU D C   
13919 O O   . LEU D 149 ? 0.4203 0.3135 0.4907 -0.0144 -0.0489 -0.0110 149 LEU D O   
13920 C CB  . LEU D 149 ? 0.3850 0.2866 0.4657 -0.0096 -0.0363 -0.0036 149 LEU D CB  
13921 C CG  . LEU D 149 ? 0.3882 0.2878 0.4669 -0.0081 -0.0301 -0.0080 149 LEU D CG  
13922 C CD1 . LEU D 149 ? 0.4156 0.3064 0.4757 -0.0078 -0.0273 -0.0097 149 LEU D CD1 
13923 C CD2 . LEU D 149 ? 0.3670 0.2729 0.4568 -0.0060 -0.0229 -0.0072 149 LEU D CD2 
13924 N N   . MET D 150 ? 0.4155 0.3232 0.5114 -0.0130 -0.0507 -0.0057 150 MET D N   
13925 C CA  . MET D 150 ? 0.4104 0.3204 0.5137 -0.0142 -0.0534 -0.0084 150 MET D CA  
13926 C C   . MET D 150 ? 0.4245 0.3301 0.5186 -0.0178 -0.0608 -0.0092 150 MET D C   
13927 O O   . MET D 150 ? 0.4064 0.3063 0.4945 -0.0194 -0.0611 -0.0132 150 MET D O   
13928 C CB  . MET D 150 ? 0.3939 0.3135 0.5147 -0.0133 -0.0549 -0.0060 150 MET D CB  
13929 C CG  . MET D 150 ? 0.3835 0.3067 0.5132 -0.0105 -0.0481 -0.0060 150 MET D CG  
13930 S SD  . MET D 150 ? 0.3767 0.2980 0.5070 -0.0095 -0.0418 -0.0106 150 MET D SD  
13931 C CE  . MET D 150 ? 0.3585 0.2739 0.4760 -0.0081 -0.0355 -0.0108 150 MET D CE  
13932 N N   . ASN D 151 ? 0.4173 0.3248 0.5097 -0.0191 -0.0668 -0.0054 151 ASN D N   
13933 C CA  . ASN D 151 ? 0.4476 0.3521 0.5320 -0.0232 -0.0750 -0.0056 151 ASN D CA  
13934 C C   . ASN D 151 ? 0.4838 0.3756 0.5480 -0.0249 -0.0740 -0.0098 151 ASN D C   
13935 O O   . ASN D 151 ? 0.4728 0.3595 0.5304 -0.0286 -0.0788 -0.0126 151 ASN D O   
13936 C CB  . ASN D 151 ? 0.4448 0.3532 0.5291 -0.0239 -0.0815 -0.0002 151 ASN D CB  
13937 C CG  . ASN D 151 ? 0.4456 0.3659 0.5488 -0.0231 -0.0850 0.0035  151 ASN D CG  
13938 O OD1 . ASN D 151 ? 0.4808 0.4061 0.5897 -0.0208 -0.0863 0.0083  151 ASN D OD1 
13939 N ND2 . ASN D 151 ? 0.4613 0.3858 0.5741 -0.0245 -0.0860 0.0015  151 ASN D ND2 
13940 N N   . THR D 152 ? 0.4824 0.3690 0.5362 -0.0225 -0.0680 -0.0099 152 THR D N   
13941 C CA  . THR D 152 ? 0.4885 0.3628 0.5218 -0.0233 -0.0661 -0.0137 152 THR D CA  
13942 C C   . THR D 152 ? 0.4750 0.3443 0.5080 -0.0228 -0.0624 -0.0192 152 THR D C   
13943 O O   . THR D 152 ? 0.5192 0.3794 0.5403 -0.0259 -0.0663 -0.0227 152 THR D O   
13944 C CB  . THR D 152 ? 0.4927 0.3647 0.5180 -0.0202 -0.0592 -0.0120 152 THR D CB  
13945 O OG1 . THR D 152 ? 0.5025 0.3774 0.5266 -0.0213 -0.0643 -0.0067 152 THR D OG1 
13946 C CG2 . THR D 152 ? 0.5067 0.3661 0.5100 -0.0201 -0.0558 -0.0156 152 THR D CG2 
13947 N N   . LEU D 153 ? 0.4306 0.3056 0.4768 -0.0195 -0.0558 -0.0197 153 LEU D N   
13948 C CA  . LEU D 153 ? 0.4656 0.3360 0.5119 -0.0182 -0.0516 -0.0244 153 LEU D CA  
13949 C C   . LEU D 153 ? 0.4748 0.3458 0.5275 -0.0219 -0.0581 -0.0259 153 LEU D C   
13950 O O   . LEU D 153 ? 0.4761 0.3382 0.5215 -0.0227 -0.0578 -0.0301 153 LEU D O   
13951 C CB  . LEU D 153 ? 0.4433 0.3211 0.5030 -0.0139 -0.0435 -0.0238 153 LEU D CB  
13952 C CG  . LEU D 153 ? 0.4738 0.3534 0.5306 -0.0108 -0.0368 -0.0215 153 LEU D CG  
13953 C CD1 . LEU D 153 ? 0.4634 0.3507 0.5343 -0.0074 -0.0297 -0.0209 153 LEU D CD1 
13954 C CD2 . LEU D 153 ? 0.5048 0.3731 0.5412 -0.0098 -0.0332 -0.0241 153 LEU D CD2 
13955 N N   . ILE D 154 ? 0.4458 0.3271 0.5126 -0.0239 -0.0637 -0.0221 154 ILE D N   
13956 C CA  . ILE D 154 ? 0.4557 0.3387 0.5287 -0.0279 -0.0703 -0.0226 154 ILE D CA  
13957 C C   . ILE D 154 ? 0.4831 0.3555 0.5392 -0.0329 -0.0772 -0.0248 154 ILE D C   
13958 O O   . ILE D 154 ? 0.4778 0.3443 0.5313 -0.0360 -0.0797 -0.0278 154 ILE D O   
13959 C CB  . ILE D 154 ? 0.4332 0.3301 0.5240 -0.0287 -0.0747 -0.0176 154 ILE D CB  
13960 C CG1 . ILE D 154 ? 0.4116 0.3169 0.5175 -0.0244 -0.0684 -0.0165 154 ILE D CG1 
13961 C CG2 . ILE D 154 ? 0.4384 0.3381 0.5348 -0.0337 -0.0823 -0.0174 154 ILE D CG2 
13962 C CD1 . ILE D 154 ? 0.4271 0.3446 0.5481 -0.0238 -0.0713 -0.0116 154 ILE D CD1 
13963 N N   . ASN D 155 ? 0.4998 0.3696 0.5447 -0.0342 -0.0808 -0.0229 155 ASN D N   
13964 C CA  . ASN D 155 ? 0.5561 0.4164 0.5848 -0.0396 -0.0886 -0.0245 155 ASN D CA  
13965 C C   . ASN D 155 ? 0.5500 0.3935 0.5589 -0.0390 -0.0842 -0.0307 155 ASN D C   
13966 O O   . ASN D 155 ? 0.5534 0.3869 0.5518 -0.0437 -0.0893 -0.0340 155 ASN D O   
13967 C CB  . ASN D 155 ? 0.5969 0.4592 0.6186 -0.0412 -0.0943 -0.0204 155 ASN D CB  
13968 C CG  . ASN D 155 ? 0.7033 0.5813 0.7438 -0.0417 -0.0997 -0.0141 155 ASN D CG  
13969 O OD1 . ASN D 155 ? 0.7049 0.5918 0.7620 -0.0428 -0.1016 -0.0130 155 ASN D OD1 
13970 N ND2 . ASN D 155 ? 0.7339 0.6155 0.7720 -0.0407 -0.1021 -0.0096 155 ASN D ND2 
13971 N N   . ILE D 156 ? 0.5156 0.3558 0.5192 -0.0334 -0.0747 -0.0321 156 ILE D N   
13972 C CA  . ILE D 156 ? 0.5234 0.3489 0.5103 -0.0312 -0.0686 -0.0378 156 ILE D CA  
13973 C C   . ILE D 156 ? 0.5131 0.3348 0.5057 -0.0318 -0.0682 -0.0414 156 ILE D C   
13974 O O   . ILE D 156 ? 0.5248 0.3316 0.5015 -0.0337 -0.0693 -0.0462 156 ILE D O   
13975 C CB  . ILE D 156 ? 0.5345 0.3612 0.5201 -0.0245 -0.0577 -0.0376 156 ILE D CB  
13976 C CG1 . ILE D 156 ? 0.5394 0.3643 0.5122 -0.0244 -0.0579 -0.0352 156 ILE D CG1 
13977 C CG2 . ILE D 156 ? 0.5652 0.3798 0.5398 -0.0206 -0.0500 -0.0432 156 ILE D CG2 
13978 C CD1 . ILE D 156 ? 0.5339 0.3657 0.5121 -0.0190 -0.0486 -0.0324 156 ILE D CD1 
13979 N N   . ILE D 157 ? 0.4968 0.3308 0.5109 -0.0306 -0.0669 -0.0390 157 ILE D N   
13980 C CA  . ILE D 157 ? 0.5166 0.3475 0.5367 -0.0315 -0.0668 -0.0417 157 ILE D CA  
13981 C C   . ILE D 157 ? 0.5382 0.3653 0.5557 -0.0393 -0.0773 -0.0420 157 ILE D C   
13982 O O   . ILE D 157 ? 0.5481 0.3618 0.5549 -0.0417 -0.0786 -0.0464 157 ILE D O   
13983 C CB  . ILE D 157 ? 0.4771 0.3215 0.5192 -0.0279 -0.0620 -0.0392 157 ILE D CB  
13984 C CG1 . ILE D 157 ? 0.4589 0.3036 0.5015 -0.0209 -0.0516 -0.0401 157 ILE D CG1 
13985 C CG2 . ILE D 157 ? 0.4824 0.3255 0.5323 -0.0303 -0.0642 -0.0406 157 ILE D CG2 
13986 C CD1 . ILE D 157 ? 0.4360 0.2958 0.4994 -0.0180 -0.0480 -0.0365 157 ILE D CD1 
13987 N N   . HIS D 158 ? 0.5019 0.3404 0.5288 -0.0433 -0.0848 -0.0374 158 HIS D N   
13988 C CA  . HIS D 158 ? 0.5068 0.3441 0.5333 -0.0512 -0.0951 -0.0369 158 HIS D CA  
13989 C C   . HIS D 158 ? 0.5327 0.3510 0.5347 -0.0557 -0.0996 -0.0416 158 HIS D C   
13990 O O   . HIS D 158 ? 0.5478 0.3593 0.5469 -0.0617 -0.1055 -0.0435 158 HIS D O   
13991 C CB  . HIS D 158 ? 0.4617 0.3148 0.5016 -0.0541 -0.1024 -0.0306 158 HIS D CB  
13992 C CG  . HIS D 158 ? 0.4313 0.3011 0.4952 -0.0511 -0.0995 -0.0266 158 HIS D CG  
13993 N ND1 . HIS D 158 ? 0.4140 0.2990 0.4920 -0.0511 -0.1032 -0.0208 158 HIS D ND1 
13994 C CD2 . HIS D 158 ? 0.4220 0.2950 0.4974 -0.0479 -0.0933 -0.0276 158 HIS D CD2 
13995 C CE1 . HIS D 158 ? 0.3958 0.2921 0.4924 -0.0480 -0.0991 -0.0188 158 HIS D CE1 
13996 N NE2 . HIS D 158 ? 0.4117 0.3011 0.5069 -0.0463 -0.0933 -0.0228 158 HIS D NE2 
13997 N N   . LYS D 159 ? 0.5594 0.3688 0.5433 -0.0534 -0.0971 -0.0435 159 LYS D N   
13998 C CA  . LYS D 159 ? 0.6355 0.4260 0.5940 -0.0574 -0.1011 -0.0482 159 LYS D CA  
13999 C C   . LYS D 159 ? 0.6057 0.3789 0.5504 -0.0534 -0.0931 -0.0547 159 LYS D C   
14000 O O   . LYS D 159 ? 0.5981 0.3545 0.5260 -0.0577 -0.0971 -0.0594 159 LYS D O   
14001 C CB  . LYS D 159 ? 0.7263 0.5138 0.6689 -0.0573 -0.1029 -0.0471 159 LYS D CB  
14002 C CG  . LYS D 159 ? 0.8384 0.6403 0.7911 -0.0619 -0.1125 -0.0406 159 LYS D CG  
14003 C CD  . LYS D 159 ? 0.9573 0.7650 0.9204 -0.0700 -0.1235 -0.0385 159 LYS D CD  
14004 C CE  . LYS D 159 ? 0.9795 0.8070 0.9610 -0.0720 -0.1304 -0.0309 159 LYS D CE  
14005 N NZ  . LYS D 159 ? 0.9993 0.8243 0.9665 -0.0754 -0.1381 -0.0288 159 LYS D NZ  
14006 N N   . GLY D 160 ? 0.5824 0.3598 0.5343 -0.0452 -0.0822 -0.0549 160 GLY D N   
14007 C CA  . GLY D 160 ? 0.5868 0.3499 0.5265 -0.0395 -0.0731 -0.0603 160 GLY D CA  
14008 C C   . GLY D 160 ? 0.6034 0.3628 0.5516 -0.0397 -0.0722 -0.0624 160 GLY D C   
14009 O O   . GLY D 160 ? 0.6433 0.3851 0.5765 -0.0380 -0.0689 -0.0678 160 GLY D O   
14010 N N   . HIS D 161 ? 0.5599 0.3351 0.5313 -0.0416 -0.0750 -0.0581 161 HIS D N   
14011 C CA  . HIS D 161 ? 0.5332 0.3056 0.5128 -0.0435 -0.0760 -0.0592 161 HIS D CA  
14012 C C   . HIS D 161 ? 0.5123 0.2969 0.5073 -0.0512 -0.0855 -0.0549 161 HIS D C   
14013 O O   . HIS D 161 ? 0.4849 0.2857 0.5009 -0.0497 -0.0842 -0.0507 161 HIS D O   
14014 C CB  . HIS D 161 ? 0.5140 0.2925 0.5065 -0.0354 -0.0659 -0.0589 161 HIS D CB  
14015 C CG  . HIS D 161 ? 0.5012 0.2732 0.4980 -0.0358 -0.0652 -0.0606 161 HIS D CG  
14016 N ND1 . HIS D 161 ? 0.4697 0.2463 0.4775 -0.0289 -0.0570 -0.0602 161 HIS D ND1 
14017 C CD2 . HIS D 161 ? 0.4955 0.2576 0.4883 -0.0424 -0.0718 -0.0622 161 HIS D CD2 
14018 C CE1 . HIS D 161 ? 0.4772 0.2468 0.4872 -0.0311 -0.0586 -0.0613 161 HIS D CE1 
14019 N NE2 . HIS D 161 ? 0.4885 0.2487 0.4892 -0.0393 -0.0674 -0.0627 161 HIS D NE2 
14020 N N   . PRO D 162 ? 0.5532 0.3304 0.5383 -0.0597 -0.0956 -0.0556 162 PRO D N   
14021 C CA  . PRO D 162 ? 0.5463 0.3383 0.5472 -0.0668 -0.1047 -0.0503 162 PRO D CA  
14022 C C   . PRO D 162 ? 0.5382 0.3381 0.5578 -0.0685 -0.1048 -0.0481 162 PRO D C   
14023 O O   . PRO D 162 ? 0.5605 0.3481 0.5752 -0.0688 -0.1027 -0.0515 162 PRO D O   
14024 C CB  . PRO D 162 ? 0.5632 0.3431 0.5465 -0.0759 -0.1154 -0.0521 162 PRO D CB  
14025 C CG  . PRO D 162 ? 0.5867 0.3452 0.5433 -0.0726 -0.1110 -0.0585 162 PRO D CG  
14026 C CD  . PRO D 162 ? 0.5760 0.3306 0.5348 -0.0632 -0.0987 -0.0612 162 PRO D CD  
14027 N N   . GLY D 163 ? 0.5140 0.3345 0.5547 -0.0695 -0.1073 -0.0422 163 GLY D N   
14028 C CA  . GLY D 163 ? 0.4920 0.3221 0.5507 -0.0725 -0.1089 -0.0391 163 GLY D CA  
14029 C C   . GLY D 163 ? 0.4862 0.3239 0.5584 -0.0648 -0.0993 -0.0384 163 GLY D C   
14030 O O   . GLY D 163 ? 0.5104 0.3557 0.5970 -0.0663 -0.0994 -0.0360 163 GLY D O   
14031 N N   . ILE D 164 ? 0.4788 0.3154 0.5468 -0.0569 -0.0914 -0.0401 164 ILE D N   
14032 C CA  . ILE D 164 ? 0.4626 0.3066 0.5428 -0.0497 -0.0827 -0.0394 164 ILE D CA  
14033 C C   . ILE D 164 ? 0.4388 0.3012 0.5341 -0.0465 -0.0812 -0.0347 164 ILE D C   
14034 O O   . ILE D 164 ? 0.4420 0.3059 0.5318 -0.0448 -0.0812 -0.0341 164 ILE D O   
14035 C CB  . ILE D 164 ? 0.4683 0.2995 0.5355 -0.0430 -0.0745 -0.0439 164 ILE D CB  
14036 C CG1 . ILE D 164 ? 0.5123 0.3225 0.5614 -0.0453 -0.0756 -0.0491 164 ILE D CG1 
14037 C CG2 . ILE D 164 ? 0.4604 0.3000 0.5412 -0.0366 -0.0667 -0.0427 164 ILE D CG2 
14038 C CD1 . ILE D 164 ? 0.5094 0.3156 0.5636 -0.0503 -0.0793 -0.0489 164 ILE D CD1 
14039 N N   . PRO D 165 ? 0.4171 0.2933 0.5311 -0.0459 -0.0802 -0.0311 165 PRO D N   
14040 C CA  . PRO D 165 ? 0.3951 0.2868 0.5228 -0.0421 -0.0779 -0.0272 165 PRO D CA  
14041 C C   . PRO D 165 ? 0.3947 0.2859 0.5192 -0.0353 -0.0705 -0.0283 165 PRO D C   
14042 O O   . PRO D 165 ? 0.4183 0.3017 0.5371 -0.0317 -0.0647 -0.0314 165 PRO D O   
14043 C CB  . PRO D 165 ? 0.3780 0.2795 0.5223 -0.0420 -0.0763 -0.0249 165 PRO D CB  
14044 C CG  . PRO D 165 ? 0.4056 0.3017 0.5478 -0.0489 -0.0822 -0.0252 165 PRO D CG  
14045 C CD  . PRO D 165 ? 0.4233 0.3003 0.5454 -0.0496 -0.0821 -0.0304 165 PRO D CD  
14046 N N   . VAL D 166 ? 0.3967 0.2971 0.5261 -0.0336 -0.0708 -0.0253 166 VAL D N   
14047 C CA  . VAL D 166 ? 0.3834 0.2846 0.5108 -0.0281 -0.0646 -0.0254 166 VAL D CA  
14048 C C   . VAL D 166 ? 0.3800 0.2951 0.5235 -0.0255 -0.0629 -0.0216 166 VAL D C   
14049 O O   . VAL D 166 ? 0.3670 0.2903 0.5176 -0.0273 -0.0676 -0.0181 166 VAL D O   
14050 C CB  . VAL D 166 ? 0.4022 0.2972 0.5153 -0.0287 -0.0667 -0.0258 166 VAL D CB  
14051 C CG1 . VAL D 166 ? 0.4077 0.3033 0.5180 -0.0235 -0.0599 -0.0255 166 VAL D CG1 
14052 C CG2 . VAL D 166 ? 0.4169 0.2968 0.5124 -0.0317 -0.0690 -0.0300 166 VAL D CG2 
14053 N N   . THR D 167 ? 0.3643 0.2818 0.5132 -0.0212 -0.0562 -0.0221 167 THR D N   
14054 C CA  . THR D 167 ? 0.3391 0.2669 0.4997 -0.0184 -0.0538 -0.0191 167 THR D CA  
14055 C C   . THR D 167 ? 0.3421 0.2685 0.5007 -0.0142 -0.0469 -0.0201 167 THR D C   
14056 O O   . THR D 167 ? 0.3630 0.2816 0.5102 -0.0132 -0.0444 -0.0222 167 THR D O   
14057 C CB  . THR D 167 ? 0.3219 0.2578 0.4960 -0.0192 -0.0547 -0.0177 167 THR D CB  
14058 O OG1 . THR D 167 ? 0.2826 0.2278 0.4667 -0.0170 -0.0540 -0.0146 167 THR D OG1 
14059 C CG2 . THR D 167 ? 0.3107 0.2437 0.4864 -0.0180 -0.0506 -0.0200 167 THR D CG2 
14060 N N   . LEU D 168 ? 0.3299 0.2639 0.4992 -0.0118 -0.0438 -0.0184 168 LEU D N   
14061 C CA  . LEU D 168 ? 0.3179 0.2521 0.4865 -0.0087 -0.0381 -0.0185 168 LEU D CA  
14062 C C   . LEU D 168 ? 0.3238 0.2636 0.5029 -0.0070 -0.0346 -0.0185 168 LEU D C   
14063 O O   . LEU D 168 ? 0.3218 0.2660 0.5089 -0.0078 -0.0365 -0.0178 168 LEU D O   
14064 C CB  . LEU D 168 ? 0.3074 0.2437 0.4750 -0.0082 -0.0385 -0.0159 168 LEU D CB  
14065 C CG  . LEU D 168 ? 0.2886 0.2323 0.4671 -0.0072 -0.0385 -0.0133 168 LEU D CG  
14066 C CD1 . LEU D 168 ? 0.3160 0.2589 0.4911 -0.0065 -0.0381 -0.0109 168 LEU D CD1 
14067 C CD2 . LEU D 168 ? 0.2968 0.2452 0.4823 -0.0085 -0.0432 -0.0119 168 LEU D CD2 
14068 N N   . SER D 169 ? 0.3236 0.2636 0.5023 -0.0047 -0.0296 -0.0187 169 SER D N   
14069 C CA  . SER D 169 ? 0.3087 0.2543 0.4965 -0.0032 -0.0265 -0.0183 169 SER D CA  
14070 C C   . SER D 169 ? 0.3163 0.2664 0.5087 -0.0031 -0.0260 -0.0159 169 SER D C   
14071 O O   . SER D 169 ? 0.3147 0.2639 0.5036 -0.0025 -0.0235 -0.0151 169 SER D O   
14072 C CB  . SER D 169 ? 0.3086 0.2523 0.4938 -0.0010 -0.0217 -0.0196 169 SER D CB  
14073 O OG  . SER D 169 ? 0.3025 0.2523 0.4960 0.0002  -0.0188 -0.0186 169 SER D OG  
14074 N N   . ALA D 170 ? 0.3255 0.2799 0.5252 -0.0035 -0.0282 -0.0148 170 ALA D N   
14075 C CA  . ALA D 170 ? 0.3040 0.2607 0.5071 -0.0031 -0.0279 -0.0129 170 ALA D CA  
14076 C C   . ALA D 170 ? 0.3008 0.2620 0.5122 -0.0026 -0.0273 -0.0128 170 ALA D C   
14077 O O   . ALA D 170 ? 0.3002 0.2637 0.5156 -0.0027 -0.0293 -0.0129 170 ALA D O   
14078 C CB  . ALA D 170 ? 0.3172 0.2732 0.5185 -0.0034 -0.0316 -0.0111 170 ALA D CB  
14079 N N   . ASN D 171 ? 0.3043 0.2665 0.5179 -0.0024 -0.0247 -0.0124 171 ASN D N   
14080 C CA  . ASN D 171 ? 0.2964 0.2617 0.5160 -0.0022 -0.0241 -0.0127 171 ASN D CA  
14081 C C   . ASN D 171 ? 0.3146 0.2801 0.5366 -0.0013 -0.0258 -0.0118 171 ASN D C   
14082 O O   . ASN D 171 ? 0.3063 0.2691 0.5262 -0.0010 -0.0263 -0.0104 171 ASN D O   
14083 C CB  . ASN D 171 ? 0.2949 0.2607 0.5151 -0.0029 -0.0215 -0.0124 171 ASN D CB  
14084 C CG  . ASN D 171 ? 0.3053 0.2737 0.5302 -0.0031 -0.0211 -0.0130 171 ASN D CG  
14085 O OD1 . ASN D 171 ? 0.3080 0.2755 0.5342 -0.0029 -0.0220 -0.0129 171 ASN D OD1 
14086 N ND2 . ASN D 171 ? 0.2915 0.2629 0.5185 -0.0035 -0.0197 -0.0134 171 ASN D ND2 
14087 N N   . ALA D 172 ? 0.3152 0.2837 0.5418 -0.0007 -0.0264 -0.0122 172 ALA D N   
14088 C CA  . ALA D 172 ? 0.3029 0.2725 0.5324 0.0009  -0.0275 -0.0112 172 ALA D CA  
14089 C C   . ALA D 172 ? 0.2948 0.2612 0.5235 0.0017  -0.0261 -0.0110 172 ALA D C   
14090 O O   . ALA D 172 ? 0.2777 0.2431 0.5073 0.0038  -0.0267 -0.0099 172 ALA D O   
14091 C CB  . ALA D 172 ? 0.2781 0.2520 0.5124 0.0013  -0.0275 -0.0116 172 ALA D CB  
14092 N N   . MET D 173 ? 0.2815 0.2463 0.5087 0.0002  -0.0244 -0.0119 173 MET D N   
14093 C CA  . MET D 173 ? 0.2932 0.2541 0.5191 0.0002  -0.0235 -0.0121 173 MET D CA  
14094 C C   . MET D 173 ? 0.3010 0.2569 0.5231 -0.0002 -0.0238 -0.0105 173 MET D C   
14095 O O   . MET D 173 ? 0.3064 0.2573 0.5269 0.0005  -0.0236 -0.0102 173 MET D O   
14096 C CB  . MET D 173 ? 0.3170 0.2788 0.5433 -0.0021 -0.0222 -0.0133 173 MET D CB  
14097 C CG  . MET D 173 ? 0.3226 0.2876 0.5516 -0.0015 -0.0219 -0.0146 173 MET D CG  
14098 S SD  . MET D 173 ? 0.3246 0.2863 0.5528 0.0008  -0.0214 -0.0155 173 MET D SD  
14099 C CE  . MET D 173 ? 0.3196 0.2747 0.5432 -0.0018 -0.0212 -0.0164 173 MET D CE  
14100 N N   . ILE D 174 ? 0.2842 0.2406 0.5041 -0.0009 -0.0243 -0.0094 174 ILE D N   
14101 C CA  . ILE D 174 ? 0.2783 0.2301 0.4937 -0.0015 -0.0244 -0.0075 174 ILE D CA  
14102 C C   . ILE D 174 ? 0.2765 0.2278 0.4898 0.0000  -0.0266 -0.0058 174 ILE D C   
14103 O O   . ILE D 174 ? 0.3104 0.2573 0.5199 0.0002  -0.0272 -0.0038 174 ILE D O   
14104 C CB  . ILE D 174 ? 0.2606 0.2127 0.4737 -0.0043 -0.0225 -0.0070 174 ILE D CB  
14105 C CG1 . ILE D 174 ? 0.2813 0.2373 0.4939 -0.0043 -0.0219 -0.0078 174 ILE D CG1 
14106 C CG2 . ILE D 174 ? 0.2415 0.1941 0.4570 -0.0064 -0.0211 -0.0078 174 ILE D CG2 
14107 C CD1 . ILE D 174 ? 0.2782 0.2344 0.4876 -0.0058 -0.0195 -0.0068 174 ILE D CD1 
14108 N N   . SER D 175 ? 0.2736 0.2292 0.4891 0.0009  -0.0282 -0.0064 175 SER D N   
14109 C CA  . SER D 175 ? 0.2691 0.2249 0.4823 0.0014  -0.0310 -0.0049 175 SER D CA  
14110 C C   . SER D 175 ? 0.2961 0.2561 0.5148 0.0034  -0.0334 -0.0042 175 SER D C   
14111 O O   . SER D 175 ? 0.3010 0.2633 0.5194 0.0032  -0.0364 -0.0031 175 SER D O   
14112 C CB  . SER D 175 ? 0.2888 0.2451 0.4980 -0.0004 -0.0311 -0.0059 175 SER D CB  
14113 O OG  . SER D 175 ? 0.3087 0.2619 0.5130 -0.0017 -0.0285 -0.0058 175 SER D OG  
14114 N N   . ASP D 176 ? 0.3094 0.2706 0.5329 0.0052  -0.0319 -0.0047 176 ASP D N   
14115 C CA  . ASP D 176 ? 0.3052 0.2705 0.5345 0.0081  -0.0330 -0.0035 176 ASP D CA  
14116 C C   . ASP D 176 ? 0.3311 0.2962 0.5600 0.0100  -0.0360 -0.0003 176 ASP D C   
14117 O O   . ASP D 176 ? 0.3809 0.3519 0.6149 0.0114  -0.0383 0.0016  176 ASP D O   
14118 C CB  . ASP D 176 ? 0.3223 0.2857 0.5537 0.0103  -0.0302 -0.0045 176 ASP D CB  
14119 C CG  . ASP D 176 ? 0.3226 0.2778 0.5489 0.0103  -0.0286 -0.0048 176 ASP D CG  
14120 O OD1 . ASP D 176 ? 0.3268 0.2784 0.5484 0.0081  -0.0291 -0.0041 176 ASP D OD1 
14121 O OD2 . ASP D 176 ? 0.3301 0.2818 0.5564 0.0121  -0.0267 -0.0057 176 ASP D OD2 
14122 N N   . TYR D 177 ? 0.3152 0.2738 0.5383 0.0100  -0.0360 0.0009  177 TYR D N   
14123 C CA  . TYR D 177 ? 0.3266 0.2838 0.5488 0.0123  -0.0386 0.0044  177 TYR D CA  
14124 C C   . TYR D 177 ? 0.3300 0.2900 0.5496 0.0104  -0.0426 0.0060  177 TYR D C   
14125 O O   . TYR D 177 ? 0.3284 0.2900 0.5489 0.0122  -0.0459 0.0093  177 TYR D O   
14126 C CB  . TYR D 177 ? 0.3251 0.2733 0.5411 0.0125  -0.0373 0.0055  177 TYR D CB  
14127 C CG  . TYR D 177 ? 0.3372 0.2822 0.5459 0.0086  -0.0368 0.0050  177 TYR D CG  
14128 C CD1 . TYR D 177 ? 0.3340 0.2780 0.5414 0.0058  -0.0337 0.0023  177 TYR D CD1 
14129 C CD2 . TYR D 177 ? 0.3428 0.2863 0.5459 0.0078  -0.0395 0.0075  177 TYR D CD2 
14130 C CE1 . TYR D 177 ? 0.3239 0.2661 0.5256 0.0028  -0.0326 0.0021  177 TYR D CE1 
14131 C CE2 . TYR D 177 ? 0.3474 0.2879 0.5433 0.0046  -0.0383 0.0070  177 TYR D CE2 
14132 C CZ  . TYR D 177 ? 0.3429 0.2831 0.5386 0.0024  -0.0346 0.0044  177 TYR D CZ  
14133 O OH  . TYR D 177 ? 0.3606 0.2989 0.5500 -0.0002 -0.0328 0.0043  177 TYR D OH  
14134 N N   . MET D 178 ? 0.3192 0.2795 0.5352 0.0068  -0.0424 0.0036  178 MET D N   
14135 C CA  . MET D 178 ? 0.3068 0.2665 0.5168 0.0045  -0.0457 0.0045  178 MET D CA  
14136 C C   . MET D 178 ? 0.3043 0.2708 0.5190 0.0041  -0.0502 0.0057  178 MET D C   
14137 O O   . MET D 178 ? 0.2992 0.2710 0.5209 0.0040  -0.0496 0.0045  178 MET D O   
14138 C CB  . MET D 178 ? 0.3101 0.2671 0.5143 0.0014  -0.0435 0.0013  178 MET D CB  
14139 C CG  . MET D 178 ? 0.3321 0.2865 0.5277 -0.0008 -0.0463 0.0016  178 MET D CG  
14140 S SD  . MET D 178 ? 0.3569 0.3081 0.5470 -0.0029 -0.0423 -0.0024 178 MET D SD  
14141 C CE  . MET D 178 ? 0.3752 0.3226 0.5622 -0.0025 -0.0368 -0.0023 178 MET D CE  
14142 N N   . ASP D 179 ? 0.3260 0.2922 0.5366 0.0034  -0.0547 0.0084  179 ASP D N   
14143 C CA  . ASP D 179 ? 0.3524 0.3243 0.5652 0.0015  -0.0601 0.0098  179 ASP D CA  
14144 C C   . ASP D 179 ? 0.3249 0.2941 0.5314 -0.0029 -0.0607 0.0064  179 ASP D C   
14145 O O   . ASP D 179 ? 0.3292 0.2915 0.5249 -0.0046 -0.0602 0.0049  179 ASP D O   
14146 C CB  . ASP D 179 ? 0.3958 0.3671 0.6044 0.0018  -0.0651 0.0138  179 ASP D CB  
14147 C CG  . ASP D 179 ? 0.4409 0.4193 0.6528 -0.0004 -0.0719 0.0162  179 ASP D CG  
14148 O OD1 . ASP D 179 ? 0.4310 0.4152 0.6495 -0.0023 -0.0726 0.0150  179 ASP D OD1 
14149 O OD2 . ASP D 179 ? 0.5260 0.5043 0.7339 -0.0006 -0.0767 0.0196  179 ASP D OD2 
14150 N N   . GLU D 180 ? 0.3298 0.3040 0.5424 -0.0046 -0.0615 0.0052  180 GLU D N   
14151 C CA  . GLU D 180 ? 0.3120 0.2824 0.5186 -0.0085 -0.0620 0.0018  180 GLU D CA  
14152 C C   . GLU D 180 ? 0.3191 0.2921 0.5248 -0.0123 -0.0688 0.0032  180 GLU D C   
14153 O O   . GLU D 180 ? 0.3297 0.2987 0.5300 -0.0160 -0.0701 0.0006  180 GLU D O   
14154 C CB  . GLU D 180 ? 0.3122 0.2844 0.5246 -0.0085 -0.0580 -0.0008 180 GLU D CB  
14155 C CG  . GLU D 180 ? 0.3072 0.2751 0.5176 -0.0063 -0.0519 -0.0031 180 GLU D CG  
14156 C CD  . GLU D 180 ? 0.3174 0.2854 0.5304 -0.0071 -0.0489 -0.0059 180 GLU D CD  
14157 O OE1 . GLU D 180 ? 0.3075 0.2776 0.5229 -0.0096 -0.0512 -0.0064 180 GLU D OE1 
14158 O OE2 . GLU D 180 ? 0.2936 0.2594 0.5060 -0.0055 -0.0443 -0.0074 180 GLU D OE2 
14159 N N   . SER D 181 ? 0.3018 0.2807 0.5117 -0.0116 -0.0734 0.0075  181 SER D N   
14160 C CA  . SER D 181 ? 0.3099 0.2941 0.5221 -0.0154 -0.0805 0.0098  181 SER D CA  
14161 C C   . SER D 181 ? 0.3441 0.3198 0.5417 -0.0198 -0.0849 0.0082  181 SER D C   
14162 O O   . SER D 181 ? 0.3304 0.3082 0.5273 -0.0245 -0.0912 0.0090  181 SER D O   
14163 C CB  . SER D 181 ? 0.2967 0.2906 0.5186 -0.0125 -0.0839 0.0154  181 SER D CB  
14164 O OG  . SER D 181 ? 0.2911 0.2804 0.5047 -0.0113 -0.0863 0.0174  181 SER D OG  
14165 N N   . ILE D 182 ? 0.3664 0.3324 0.5518 -0.0185 -0.0817 0.0061  182 ILE D N   
14166 C CA  . ILE D 182 ? 0.3872 0.3434 0.5565 -0.0220 -0.0843 0.0038  182 ILE D CA  
14167 C C   . ILE D 182 ? 0.3780 0.3275 0.5417 -0.0249 -0.0823 -0.0012 182 ILE D C   
14168 O O   . ILE D 182 ? 0.3829 0.3240 0.5336 -0.0283 -0.0851 -0.0036 182 ILE D O   
14169 C CB  . ILE D 182 ? 0.4122 0.3611 0.5708 -0.0193 -0.0807 0.0037  182 ILE D CB  
14170 C CG1 . ILE D 182 ? 0.3932 0.3404 0.5549 -0.0158 -0.0723 0.0015  182 ILE D CG1 
14171 C CG2 . ILE D 182 ? 0.4118 0.3648 0.5722 -0.0174 -0.0844 0.0089  182 ILE D CG2 
14172 C CD1 . ILE D 182 ? 0.4091 0.3488 0.5596 -0.0142 -0.0682 0.0011  182 ILE D CD1 
14173 N N   . PHE D 183 ? 0.3676 0.3197 0.5400 -0.0231 -0.0771 -0.0029 183 PHE D N   
14174 C CA  . PHE D 183 ? 0.3684 0.3144 0.5368 -0.0250 -0.0748 -0.0072 183 PHE D CA  
14175 C C   . PHE D 183 ? 0.3584 0.3089 0.5334 -0.0294 -0.0801 -0.0063 183 PHE D C   
14176 O O   . PHE D 183 ? 0.3599 0.3208 0.5458 -0.0299 -0.0838 -0.0023 183 PHE D O   
14177 C CB  . PHE D 183 ? 0.3413 0.2881 0.5156 -0.0212 -0.0672 -0.0089 183 PHE D CB  
14178 C CG  . PHE D 183 ? 0.3601 0.3029 0.5284 -0.0177 -0.0623 -0.0094 183 PHE D CG  
14179 C CD1 . PHE D 183 ? 0.3850 0.3181 0.5397 -0.0178 -0.0599 -0.0123 183 PHE D CD1 
14180 C CD2 . PHE D 183 ? 0.3594 0.3077 0.5352 -0.0143 -0.0597 -0.0068 183 PHE D CD2 
14181 C CE1 . PHE D 183 ? 0.3731 0.3038 0.5232 -0.0149 -0.0550 -0.0121 183 PHE D CE1 
14182 C CE2 . PHE D 183 ? 0.3374 0.2820 0.5080 -0.0119 -0.0554 -0.0069 183 PHE D CE2 
14183 C CZ  . PHE D 183 ? 0.3384 0.2749 0.4967 -0.0123 -0.0530 -0.0093 183 PHE D CZ  
14184 N N   . ASP D 184 ? 0.3731 0.3156 0.5413 -0.0326 -0.0803 -0.0099 184 ASP D N   
14185 C CA  . ASP D 184 ? 0.3604 0.3054 0.5334 -0.0378 -0.0852 -0.0093 184 ASP D CA  
14186 C C   . ASP D 184 ? 0.3318 0.2845 0.5189 -0.0364 -0.0814 -0.0084 184 ASP D C   
14187 O O   . ASP D 184 ? 0.3323 0.2924 0.5287 -0.0398 -0.0851 -0.0059 184 ASP D O   
14188 C CB  . ASP D 184 ? 0.3635 0.2948 0.5226 -0.0419 -0.0869 -0.0136 184 ASP D CB  
14189 C CG  . ASP D 184 ? 0.3882 0.3091 0.5300 -0.0436 -0.0902 -0.0154 184 ASP D CG  
14190 O OD1 . ASP D 184 ? 0.3921 0.3177 0.5337 -0.0461 -0.0965 -0.0123 184 ASP D OD1 
14191 O OD2 . ASP D 184 ? 0.4066 0.3148 0.5351 -0.0423 -0.0863 -0.0199 184 ASP D OD2 
14192 N N   . VAL D 185 ? 0.3194 0.2704 0.5077 -0.0316 -0.0742 -0.0104 185 VAL D N   
14193 C CA  . VAL D 185 ? 0.3139 0.2715 0.5140 -0.0298 -0.0702 -0.0096 185 VAL D CA  
14194 C C   . VAL D 185 ? 0.2892 0.2519 0.4948 -0.0241 -0.0649 -0.0087 185 VAL D C   
14195 O O   . VAL D 185 ? 0.2899 0.2477 0.4882 -0.0216 -0.0627 -0.0099 185 VAL D O   
14196 C CB  . VAL D 185 ? 0.3272 0.2754 0.5212 -0.0306 -0.0673 -0.0134 185 VAL D CB  
14197 C CG1 . VAL D 185 ? 0.3175 0.2700 0.5203 -0.0275 -0.0618 -0.0134 185 VAL D CG1 
14198 C CG2 . VAL D 185 ? 0.3317 0.2756 0.5227 -0.0368 -0.0727 -0.0137 185 VAL D CG2 
14199 N N   . TYR D 186 ? 0.2887 0.2605 0.5064 -0.0222 -0.0627 -0.0067 186 TYR D N   
14200 C CA  . TYR D 186 ? 0.2780 0.2528 0.4999 -0.0172 -0.0577 -0.0063 186 TYR D CA  
14201 C C   . TYR D 186 ? 0.3007 0.2714 0.5213 -0.0158 -0.0525 -0.0092 186 TYR D C   
14202 O O   . TYR D 186 ? 0.3272 0.2964 0.5486 -0.0179 -0.0524 -0.0102 186 TYR D O   
14203 C CB  . TYR D 186 ? 0.2722 0.2578 0.5063 -0.0151 -0.0575 -0.0029 186 TYR D CB  
14204 C CG  . TYR D 186 ? 0.2787 0.2704 0.5164 -0.0155 -0.0625 0.0008  186 TYR D CG  
14205 C CD1 . TYR D 186 ? 0.3097 0.2977 0.5408 -0.0145 -0.0644 0.0014  186 TYR D CD1 
14206 C CD2 . TYR D 186 ? 0.2977 0.2994 0.5456 -0.0171 -0.0655 0.0042  186 TYR D CD2 
14207 C CE1 . TYR D 186 ? 0.3501 0.3439 0.5845 -0.0146 -0.0693 0.0052  186 TYR D CE1 
14208 C CE2 . TYR D 186 ? 0.3086 0.3171 0.5608 -0.0174 -0.0704 0.0081  186 TYR D CE2 
14209 C CZ  . TYR D 186 ? 0.3475 0.3519 0.5928 -0.0160 -0.0726 0.0087  186 TYR D CZ  
14210 O OH  . TYR D 186 ? 0.3344 0.3456 0.5838 -0.0159 -0.0778 0.0130  186 TYR D OH  
14211 N N   . ALA D 187 ? 0.2883 0.2569 0.5066 -0.0124 -0.0484 -0.0102 187 ALA D N   
14212 C CA  . ALA D 187 ? 0.2715 0.2365 0.4881 -0.0111 -0.0439 -0.0125 187 ALA D CA  
14213 C C   . ALA D 187 ? 0.2623 0.2289 0.4809 -0.0078 -0.0400 -0.0124 187 ALA D C   
14214 O O   . ALA D 187 ? 0.2942 0.2599 0.5101 -0.0068 -0.0403 -0.0114 187 ALA D O   
14215 C CB  . ALA D 187 ? 0.2688 0.2250 0.4751 -0.0121 -0.0437 -0.0151 187 ALA D CB  
14216 N N   . TYR D 188 ? 0.2645 0.2327 0.4870 -0.0066 -0.0367 -0.0131 188 TYR D N   
14217 C CA  . TYR D 188 ? 0.2706 0.2391 0.4937 -0.0045 -0.0332 -0.0134 188 TYR D CA  
14218 C C   . TYR D 188 ? 0.2895 0.2570 0.5127 -0.0041 -0.0302 -0.0149 188 TYR D C   
14219 O O   . TYR D 188 ? 0.2721 0.2399 0.4970 -0.0048 -0.0305 -0.0154 188 TYR D O   
14220 C CB  . TYR D 188 ? 0.2677 0.2409 0.4972 -0.0030 -0.0325 -0.0121 188 TYR D CB  
14221 C CG  . TYR D 188 ? 0.2741 0.2492 0.5051 -0.0023 -0.0350 -0.0100 188 TYR D CG  
14222 C CD1 . TYR D 188 ? 0.2778 0.2496 0.5044 -0.0016 -0.0353 -0.0093 188 TYR D CD1 
14223 C CD2 . TYR D 188 ? 0.2948 0.2753 0.5317 -0.0023 -0.0370 -0.0083 188 TYR D CD2 
14224 C CE1 . TYR D 188 ? 0.2924 0.2658 0.5203 -0.0006 -0.0379 -0.0070 188 TYR D CE1 
14225 C CE2 . TYR D 188 ? 0.2992 0.2825 0.5386 -0.0011 -0.0393 -0.0059 188 TYR D CE2 
14226 C CZ  . TYR D 188 ? 0.2768 0.2562 0.5113 -0.0001 -0.0399 -0.0053 188 TYR D CZ  
14227 O OH  . TYR D 188 ? 0.2652 0.2468 0.5016 0.0013  -0.0425 -0.0025 188 TYR D OH  
14228 N N   . ASN D 189 ? 0.2923 0.2591 0.5141 -0.0029 -0.0275 -0.0152 189 ASN D N   
14229 C CA  . ASN D 189 ? 0.2948 0.2633 0.5193 -0.0023 -0.0249 -0.0157 189 ASN D CA  
14230 C C   . ASN D 189 ? 0.2863 0.2585 0.5159 -0.0021 -0.0248 -0.0151 189 ASN D C   
14231 O O   . ASN D 189 ? 0.3263 0.2983 0.5557 -0.0018 -0.0248 -0.0144 189 ASN D O   
14232 C CB  . ASN D 189 ? 0.2981 0.2657 0.5201 -0.0016 -0.0222 -0.0158 189 ASN D CB  
14233 C CG  . ASN D 189 ? 0.2921 0.2553 0.5078 -0.0011 -0.0215 -0.0167 189 ASN D CG  
14234 O OD1 . ASN D 189 ? 0.3172 0.2790 0.5290 -0.0010 -0.0203 -0.0162 189 ASN D OD1 
14235 N ND2 . ASN D 189 ? 0.2809 0.2414 0.4948 -0.0011 -0.0223 -0.0178 189 ASN D ND2 
14236 N N   . CYS D 190 ? 0.2745 0.2491 0.5075 -0.0021 -0.0245 -0.0152 190 CYS D N   
14237 C CA  . CYS D 190 ? 0.2874 0.2650 0.5239 -0.0017 -0.0243 -0.0148 190 CYS D CA  
14238 C C   . CYS D 190 ? 0.2950 0.2740 0.5327 -0.0018 -0.0228 -0.0151 190 CYS D C   
14239 O O   . CYS D 190 ? 0.3024 0.2822 0.5409 -0.0019 -0.0227 -0.0150 190 CYS D O   
14240 C CB  . CYS D 190 ? 0.2782 0.2582 0.5177 -0.0020 -0.0256 -0.0140 190 CYS D CB  
14241 S SG  . CYS D 190 ? 0.2830 0.2625 0.5219 -0.0027 -0.0284 -0.0131 190 CYS D SG  
14242 N N   . TYR D 191 ? 0.2680 0.2469 0.5053 -0.0018 -0.0221 -0.0153 191 TYR D N   
14243 C CA  . TYR D 191 ? 0.2868 0.2672 0.5248 -0.0025 -0.0215 -0.0154 191 TYR D CA  
14244 C C   . TYR D 191 ? 0.2703 0.2503 0.5078 -0.0023 -0.0213 -0.0159 191 TYR D C   
14245 O O   . TYR D 191 ? 0.2481 0.2256 0.4842 -0.0017 -0.0212 -0.0162 191 TYR D O   
14246 C CB  . TYR D 191 ? 0.2962 0.2766 0.5336 -0.0035 -0.0209 -0.0152 191 TYR D CB  
14247 C CG  . TYR D 191 ? 0.2590 0.2405 0.4969 -0.0030 -0.0202 -0.0147 191 TYR D CG  
14248 C CD1 . TYR D 191 ? 0.2768 0.2611 0.5168 -0.0025 -0.0198 -0.0141 191 TYR D CD1 
14249 C CD2 . TYR D 191 ? 0.2690 0.2481 0.5045 -0.0025 -0.0197 -0.0147 191 TYR D CD2 
14250 C CE1 . TYR D 191 ? 0.2424 0.2267 0.4825 -0.0010 -0.0186 -0.0138 191 TYR D CE1 
14251 C CE2 . TYR D 191 ? 0.2763 0.2552 0.5108 -0.0014 -0.0185 -0.0147 191 TYR D CE2 
14252 C CZ  . TYR D 191 ? 0.2656 0.2469 0.5026 -0.0004 -0.0178 -0.0143 191 TYR D CZ  
14253 O OH  . TYR D 191 ? 0.3197 0.2999 0.5553 0.0015  -0.0161 -0.0143 191 TYR D OH  
14254 N N   . ASP D 192 ? 0.2662 0.2480 0.5039 -0.0027 -0.0212 -0.0160 192 ASP D N   
14255 C CA  . ASP D 192 ? 0.2822 0.2631 0.5180 -0.0025 -0.0207 -0.0167 192 ASP D CA  
14256 C C   . ASP D 192 ? 0.3022 0.2821 0.5355 -0.0044 -0.0214 -0.0173 192 ASP D C   
14257 O O   . ASP D 192 ? 0.2873 0.2697 0.5207 -0.0052 -0.0220 -0.0168 192 ASP D O   
14258 C CB  . ASP D 192 ? 0.2752 0.2587 0.5120 -0.0018 -0.0202 -0.0161 192 ASP D CB  
14259 C CG  . ASP D 192 ? 0.2789 0.2613 0.5127 -0.0009 -0.0189 -0.0169 192 ASP D CG  
14260 O OD1 . ASP D 192 ? 0.3108 0.2891 0.5412 -0.0007 -0.0186 -0.0183 192 ASP D OD1 
14261 O OD2 . ASP D 192 ? 0.2677 0.2527 0.5021 -0.0006 -0.0182 -0.0160 192 ASP D OD2 
14262 N N   . HIS D 193 ? 0.3114 0.2874 0.5421 -0.0053 -0.0216 -0.0181 193 HIS D N   
14263 C CA  . HIS D 193 ? 0.3086 0.2830 0.5365 -0.0080 -0.0229 -0.0186 193 HIS D CA  
14264 C C   . HIS D 193 ? 0.3254 0.2936 0.5472 -0.0079 -0.0225 -0.0206 193 HIS D C   
14265 O O   . HIS D 193 ? 0.3346 0.2994 0.5527 -0.0108 -0.0240 -0.0214 193 HIS D O   
14266 C CB  . HIS D 193 ? 0.3076 0.2811 0.5363 -0.0101 -0.0235 -0.0180 193 HIS D CB  
14267 C CG  . HIS D 193 ? 0.2936 0.2725 0.5272 -0.0099 -0.0232 -0.0162 193 HIS D CG  
14268 N ND1 . HIS D 193 ? 0.2679 0.2460 0.5022 -0.0094 -0.0223 -0.0156 193 HIS D ND1 
14269 C CD2 . HIS D 193 ? 0.2939 0.2782 0.5309 -0.0097 -0.0234 -0.0151 193 HIS D CD2 
14270 C CE1 . HIS D 193 ? 0.2954 0.2781 0.5332 -0.0089 -0.0217 -0.0143 193 HIS D CE1 
14271 N NE2 . HIS D 193 ? 0.2811 0.2676 0.5208 -0.0088 -0.0223 -0.0140 193 HIS D NE2 
14272 N N   . ASN D 194 ? 0.3092 0.2760 0.5302 -0.0047 -0.0207 -0.0212 194 ASN D N   
14273 C CA  . ASN D 194 ? 0.2990 0.2596 0.5138 -0.0035 -0.0195 -0.0231 194 ASN D CA  
14274 C C   . ASN D 194 ? 0.3230 0.2754 0.5332 -0.0049 -0.0202 -0.0243 194 ASN D C   
14275 O O   . ASN D 194 ? 0.3205 0.2669 0.5242 -0.0070 -0.0211 -0.0261 194 ASN D O   
14276 C CB  . ASN D 194 ? 0.2727 0.2335 0.4832 -0.0050 -0.0200 -0.0240 194 ASN D CB  
14277 C CG  . ASN D 194 ? 0.2704 0.2244 0.4733 -0.0029 -0.0180 -0.0262 194 ASN D CG  
14278 O OD1 . ASN D 194 ? 0.2846 0.2368 0.4879 0.0009  -0.0154 -0.0265 194 ASN D OD1 
14279 N ND2 . ASN D 194 ? 0.2654 0.2156 0.4610 -0.0051 -0.0190 -0.0278 194 ASN D ND2 
14280 N N   . GLU D 195 ? 0.3129 0.2645 0.5260 -0.0042 -0.0202 -0.0233 195 GLU D N   
14281 C CA  . GLU D 195 ? 0.3441 0.2876 0.5531 -0.0055 -0.0208 -0.0238 195 GLU D CA  
14282 C C   . GLU D 195 ? 0.3246 0.2669 0.5359 -0.0021 -0.0197 -0.0226 195 GLU D C   
14283 O O   . GLU D 195 ? 0.3064 0.2554 0.5232 -0.0003 -0.0193 -0.0211 195 GLU D O   
14284 C CB  . GLU D 195 ? 0.3319 0.2764 0.5418 -0.0105 -0.0230 -0.0228 195 GLU D CB  
14285 C CG  . GLU D 195 ? 0.3396 0.2920 0.5564 -0.0105 -0.0230 -0.0205 195 GLU D CG  
14286 C CD  . GLU D 195 ? 0.3325 0.2886 0.5518 -0.0147 -0.0243 -0.0190 195 GLU D CD  
14287 O OE1 . GLU D 195 ? 0.3560 0.3091 0.5725 -0.0185 -0.0259 -0.0193 195 GLU D OE1 
14288 O OE2 . GLU D 195 ? 0.3435 0.3057 0.5676 -0.0140 -0.0237 -0.0173 195 GLU D OE2 
14289 N N   . GLY D 196 ? 0.3154 0.2484 0.5219 -0.0015 -0.0195 -0.0231 196 GLY D N   
14290 C CA  . GLY D 196 ? 0.3071 0.2382 0.5151 0.0022  -0.0187 -0.0217 196 GLY D CA  
14291 C C   . GLY D 196 ? 0.2849 0.2219 0.4973 0.0071  -0.0170 -0.0211 196 GLY D C   
14292 O O   . GLY D 196 ? 0.2751 0.2116 0.4857 0.0094  -0.0152 -0.0226 196 GLY D O   
14293 N N   . GLN D 197 ? 0.2795 0.2226 0.4975 0.0082  -0.0177 -0.0188 197 GLN D N   
14294 C CA  . GLN D 197 ? 0.3003 0.2506 0.5239 0.0118  -0.0168 -0.0175 197 GLN D CA  
14295 C C   . GLN D 197 ? 0.2702 0.2267 0.4959 0.0114  -0.0158 -0.0184 197 GLN D C   
14296 O O   . GLN D 197 ? 0.2584 0.2187 0.4869 0.0147  -0.0141 -0.0178 197 GLN D O   
14297 C CB  . GLN D 197 ? 0.3094 0.2650 0.5376 0.0112  -0.0188 -0.0151 197 GLN D CB  
14298 C CG  . GLN D 197 ? 0.3008 0.2510 0.5269 0.0122  -0.0199 -0.0136 197 GLN D CG  
14299 C CD  . GLN D 197 ? 0.2967 0.2431 0.5192 0.0080  -0.0210 -0.0136 197 GLN D CD  
14300 O OE1 . GLN D 197 ? 0.3017 0.2443 0.5209 0.0053  -0.0205 -0.0152 197 GLN D OE1 
14301 N NE2 . GLN D 197 ? 0.2812 0.2292 0.5044 0.0073  -0.0225 -0.0117 197 GLN D NE2 
14302 N N   . THR D 198 ? 0.2514 0.2093 0.4761 0.0076  -0.0167 -0.0193 198 THR D N   
14303 C CA  . THR D 198 ? 0.2495 0.2135 0.4765 0.0072  -0.0160 -0.0193 198 THR D CA  
14304 C C   . THR D 198 ? 0.2679 0.2280 0.4894 0.0080  -0.0143 -0.0214 198 THR D C   
14305 O O   . THR D 198 ? 0.2826 0.2470 0.5050 0.0084  -0.0131 -0.0213 198 THR D O   
14306 C CB  . THR D 198 ? 0.2318 0.1999 0.4607 0.0037  -0.0177 -0.0189 198 THR D CB  
14307 O OG1 . THR D 198 ? 0.2165 0.1809 0.4417 0.0007  -0.0188 -0.0200 198 THR D OG1 
14308 C CG2 . THR D 198 ? 0.2298 0.2012 0.4628 0.0034  -0.0191 -0.0173 198 THR D CG2 
14309 N N   . ALA D 199 ? 0.2761 0.2273 0.4912 0.0077  -0.0142 -0.0231 199 ALA D N   
14310 C CA  . ALA D 199 ? 0.2921 0.2369 0.4998 0.0085  -0.0126 -0.0255 199 ALA D CA  
14311 C C   . ALA D 199 ? 0.2871 0.2295 0.4940 0.0144  -0.0092 -0.0257 199 ALA D C   
14312 O O   . ALA D 199 ? 0.3152 0.2572 0.5186 0.0164  -0.0067 -0.0270 199 ALA D O   
14313 C CB  . ALA D 199 ? 0.3093 0.2446 0.5098 0.0051  -0.0145 -0.0274 199 ALA D CB  
14314 N N   . THR D 200 ? 0.2820 0.2235 0.4922 0.0173  -0.0090 -0.0243 200 THR D N   
14315 C CA  . THR D 200 ? 0.3048 0.2448 0.5153 0.0236  -0.0057 -0.0239 200 THR D CA  
14316 C C   . THR D 200 ? 0.3223 0.2745 0.5415 0.0262  -0.0040 -0.0214 200 THR D C   
14317 O O   . THR D 200 ? 0.3397 0.2939 0.5581 0.0293  -0.0005 -0.0218 200 THR D O   
14318 C CB  . THR D 200 ? 0.3215 0.2561 0.5326 0.0257  -0.0066 -0.0227 200 THR D CB  
14319 O OG1 . THR D 200 ? 0.3350 0.2769 0.5530 0.0233  -0.0096 -0.0200 200 THR D OG1 
14320 C CG2 . THR D 200 ? 0.3342 0.2558 0.5363 0.0229  -0.0080 -0.0249 200 THR D CG2 
14321 N N   . MET D 201 ? 0.3142 0.2747 0.5413 0.0242  -0.0066 -0.0188 201 MET D N   
14322 C CA  . MET D 201 ? 0.3187 0.2904 0.5547 0.0258  -0.0059 -0.0159 201 MET D CA  
14323 C C   . MET D 201 ? 0.3260 0.3038 0.5635 0.0222  -0.0062 -0.0158 201 MET D C   
14324 O O   . MET D 201 ? 0.2932 0.2796 0.5367 0.0231  -0.0048 -0.0137 201 MET D O   
14325 C CB  . MET D 201 ? 0.3397 0.3155 0.5819 0.0252  -0.0091 -0.0132 201 MET D CB  
14326 C CG  . MET D 201 ? 0.3329 0.3042 0.5749 0.0295  -0.0090 -0.0122 201 MET D CG  
14327 S SD  . MET D 201 ? 0.3099 0.2839 0.5562 0.0277  -0.0136 -0.0093 201 MET D SD  
14328 C CE  . MET D 201 ? 0.3190 0.2806 0.5556 0.0242  -0.0146 -0.0121 201 MET D CE  
14329 N N   . GLY D 202 ? 0.3082 0.2821 0.5409 0.0179  -0.0081 -0.0177 202 GLY D N   
14330 C CA  . GLY D 202 ? 0.2883 0.2675 0.5226 0.0146  -0.0088 -0.0171 202 GLY D CA  
14331 C C   . GLY D 202 ? 0.2980 0.2819 0.5382 0.0121  -0.0119 -0.0152 202 GLY D C   
14332 O O   . GLY D 202 ? 0.3004 0.2852 0.5440 0.0133  -0.0130 -0.0140 202 GLY D O   
14333 N N   . PHE D 203 ? 0.2867 0.2727 0.5273 0.0087  -0.0133 -0.0151 203 PHE D N   
14334 C CA  . PHE D 203 ? 0.2773 0.2653 0.5211 0.0063  -0.0161 -0.0141 203 PHE D CA  
14335 C C   . PHE D 203 ? 0.2542 0.2482 0.5043 0.0067  -0.0166 -0.0117 203 PHE D C   
14336 O O   . PHE D 203 ? 0.2461 0.2404 0.4982 0.0065  -0.0186 -0.0109 203 PHE D O   
14337 C CB  . PHE D 203 ? 0.2973 0.2856 0.5399 0.0035  -0.0170 -0.0143 203 PHE D CB  
14338 C CG  . PHE D 203 ? 0.2829 0.2709 0.5266 0.0014  -0.0192 -0.0139 203 PHE D CG  
14339 C CD1 . PHE D 203 ? 0.3047 0.2898 0.5472 0.0013  -0.0204 -0.0145 203 PHE D CD1 
14340 C CD2 . PHE D 203 ? 0.2860 0.2758 0.5311 -0.0002 -0.0199 -0.0131 203 PHE D CD2 
14341 C CE1 . PHE D 203 ? 0.2989 0.2832 0.5413 -0.0001 -0.0217 -0.0144 203 PHE D CE1 
14342 C CE2 . PHE D 203 ? 0.2951 0.2833 0.5400 -0.0014 -0.0214 -0.0131 203 PHE D CE2 
14343 C CZ  . PHE D 203 ? 0.3046 0.2903 0.5481 -0.0012 -0.0222 -0.0139 203 PHE D CZ  
14344 N N   . LYS D 204 ? 0.2621 0.2613 0.5153 0.0069  -0.0151 -0.0102 204 LYS D N   
14345 C CA  . LYS D 204 ? 0.2661 0.2720 0.5261 0.0066  -0.0159 -0.0075 204 LYS D CA  
14346 C C   . LYS D 204 ? 0.2662 0.2737 0.5293 0.0096  -0.0161 -0.0065 204 LYS D C   
14347 O O   . LYS D 204 ? 0.2951 0.3046 0.5614 0.0084  -0.0191 -0.0051 204 LYS D O   
14348 C CB  . LYS D 204 ? 0.2628 0.2750 0.5264 0.0065  -0.0136 -0.0054 204 LYS D CB  
14349 C CG  . LYS D 204 ? 0.2714 0.2924 0.5437 0.0064  -0.0141 -0.0019 204 LYS D CG  
14350 C CD  . LYS D 204 ? 0.2537 0.2820 0.5301 0.0073  -0.0105 0.0005  204 LYS D CD  
14351 C CE  . LYS D 204 ? 0.2589 0.2976 0.5452 0.0074  -0.0106 0.0045  204 LYS D CE  
14352 N NZ  . LYS D 204 ? 0.2517 0.2975 0.5413 0.0088  -0.0060 0.0069  204 LYS D NZ  
14353 N N   . ASP D 205 ? 0.2803 0.2869 0.5423 0.0136  -0.0130 -0.0070 205 ASP D N   
14354 C CA  . ASP D 205 ? 0.2990 0.3088 0.5656 0.0173  -0.0127 -0.0051 205 ASP D CA  
14355 C C   . ASP D 205 ? 0.2921 0.2962 0.5560 0.0174  -0.0156 -0.0057 205 ASP D C   
14356 O O   . ASP D 205 ? 0.2942 0.3020 0.5628 0.0186  -0.0175 -0.0034 205 ASP D O   
14357 C CB  . ASP D 205 ? 0.3160 0.3258 0.5818 0.0225  -0.0080 -0.0053 205 ASP D CB  
14358 C CG  . ASP D 205 ? 0.3196 0.3377 0.5899 0.0231  -0.0048 -0.0034 205 ASP D CG  
14359 O OD1 . ASP D 205 ? 0.2974 0.3214 0.5722 0.0189  -0.0067 -0.0015 205 ASP D OD1 
14360 O OD2 . ASP D 205 ? 0.3077 0.3254 0.5763 0.0277  -0.0002 -0.0038 205 ASP D OD2 
14361 N N   . TYR D 206 ? 0.3151 0.3109 0.5718 0.0157  -0.0161 -0.0085 206 TYR D N   
14362 C CA  . TYR D 206 ? 0.2973 0.2877 0.5509 0.0150  -0.0186 -0.0089 206 TYR D CA  
14363 C C   . TYR D 206 ? 0.2530 0.2470 0.5094 0.0121  -0.0222 -0.0073 206 TYR D C   
14364 O O   . TYR D 206 ? 0.2508 0.2455 0.5087 0.0129  -0.0244 -0.0056 206 TYR D O   
14365 C CB  . TYR D 206 ? 0.3036 0.2864 0.5501 0.0126  -0.0186 -0.0116 206 TYR D CB  
14366 C CG  . TYR D 206 ? 0.2877 0.2655 0.5311 0.0117  -0.0206 -0.0115 206 TYR D CG  
14367 C CD1 . TYR D 206 ? 0.2898 0.2654 0.5334 0.0145  -0.0211 -0.0101 206 TYR D CD1 
14368 C CD2 . TYR D 206 ? 0.2784 0.2540 0.5190 0.0082  -0.0218 -0.0125 206 TYR D CD2 
14369 C CE1 . TYR D 206 ? 0.2872 0.2580 0.5274 0.0135  -0.0228 -0.0096 206 TYR D CE1 
14370 C CE2 . TYR D 206 ? 0.2977 0.2691 0.5351 0.0073  -0.0231 -0.0121 206 TYR D CE2 
14371 C CZ  . TYR D 206 ? 0.3072 0.2758 0.5440 0.0098  -0.0236 -0.0107 206 TYR D CZ  
14372 O OH  . TYR D 206 ? 0.3025 0.2667 0.5357 0.0089  -0.0248 -0.0099 206 TYR D OH  
14373 N N   . ILE D 207 ? 0.2411 0.2365 0.4974 0.0086  -0.0230 -0.0079 207 ILE D N   
14374 C CA  . ILE D 207 ? 0.2358 0.2326 0.4930 0.0056  -0.0264 -0.0070 207 ILE D CA  
14375 C C   . ILE D 207 ? 0.2249 0.2294 0.4890 0.0059  -0.0282 -0.0039 207 ILE D C   
14376 O O   . ILE D 207 ? 0.2375 0.2428 0.5023 0.0049  -0.0315 -0.0025 207 ILE D O   
14377 C CB  . ILE D 207 ? 0.2387 0.2341 0.4937 0.0024  -0.0266 -0.0083 207 ILE D CB  
14378 C CG1 . ILE D 207 ? 0.2599 0.2495 0.5094 0.0022  -0.0252 -0.0107 207 ILE D CG1 
14379 C CG2 . ILE D 207 ? 0.2530 0.2483 0.5077 -0.0006 -0.0300 -0.0077 207 ILE D CG2 
14380 C CD1 . ILE D 207 ? 0.2635 0.2483 0.5090 0.0025  -0.0260 -0.0112 207 ILE D CD1 
14381 N N   . LYS D 208 ? 0.2425 0.2532 0.5120 0.0070  -0.0260 -0.0026 208 LYS D N   
14382 C CA  . LYS D 208 ? 0.2528 0.2728 0.5307 0.0075  -0.0271 0.0010  208 LYS D CA  
14383 C C   . LYS D 208 ? 0.2468 0.2685 0.5272 0.0112  -0.0281 0.0029  208 LYS D C   
14384 O O   . LYS D 208 ? 0.2495 0.2775 0.5355 0.0104  -0.0315 0.0060  208 LYS D O   
14385 C CB  . LYS D 208 ? 0.2865 0.3125 0.5690 0.0095  -0.0231 0.0021  208 LYS D CB  
14386 C CG  . LYS D 208 ? 0.3360 0.3735 0.6286 0.0093  -0.0237 0.0063  208 LYS D CG  
14387 C CD  . LYS D 208 ? 0.4107 0.4542 0.7072 0.0112  -0.0188 0.0075  208 LYS D CD  
14388 C CE  . LYS D 208 ? 0.5120 0.5684 0.8199 0.0119  -0.0190 0.0124  208 LYS D CE  
14389 N NZ  . LYS D 208 ? 0.6140 0.6768 0.9255 0.0128  -0.0142 0.0139  208 LYS D NZ  
14390 N N   . GLY D 209 ? 0.2351 0.2508 0.5113 0.0152  -0.0255 0.0013  209 GLY D N   
14391 C CA  . GLY D 209 ? 0.2437 0.2595 0.5216 0.0194  -0.0261 0.0032  209 GLY D CA  
14392 C C   . GLY D 209 ? 0.2564 0.2695 0.5316 0.0170  -0.0309 0.0040  209 GLY D C   
14393 O O   . GLY D 209 ? 0.2522 0.2699 0.5319 0.0188  -0.0334 0.0072  209 GLY D O   
14394 N N   . LEU D 210 ? 0.2842 0.2901 0.5520 0.0132  -0.0320 0.0013  210 LEU D N   
14395 C CA  . LEU D 210 ? 0.2835 0.2859 0.5468 0.0108  -0.0360 0.0016  210 LEU D CA  
14396 C C   . LEU D 210 ? 0.2948 0.3037 0.5621 0.0073  -0.0404 0.0038  210 LEU D C   
14397 O O   . LEU D 210 ? 0.2891 0.2994 0.5565 0.0070  -0.0443 0.0060  210 LEU D O   
14398 C CB  . LEU D 210 ? 0.2736 0.2678 0.5287 0.0081  -0.0350 -0.0018 210 LEU D CB  
14399 C CG  . LEU D 210 ? 0.2657 0.2531 0.5163 0.0103  -0.0316 -0.0037 210 LEU D CG  
14400 C CD1 . LEU D 210 ? 0.2639 0.2454 0.5081 0.0074  -0.0309 -0.0062 210 LEU D CD1 
14401 C CD2 . LEU D 210 ? 0.2538 0.2379 0.5032 0.0135  -0.0320 -0.0019 210 LEU D CD2 
14402 N N   . ASN D 211 ? 0.3041 0.3169 0.5745 0.0045  -0.0400 0.0033  211 ASN D N   
14403 C CA  . ASN D 211 ? 0.2833 0.3019 0.5576 0.0004  -0.0443 0.0054  211 ASN D CA  
14404 C C   . ASN D 211 ? 0.2777 0.3062 0.5611 0.0025  -0.0465 0.0099  211 ASN D C   
14405 O O   . ASN D 211 ? 0.2885 0.3197 0.5728 -0.0002 -0.0517 0.0120  211 ASN D O   
14406 C CB  . ASN D 211 ? 0.2911 0.3120 0.5680 -0.0027 -0.0430 0.0047  211 ASN D CB  
14407 C CG  . ASN D 211 ? 0.3118 0.3341 0.5890 -0.0084 -0.0478 0.0057  211 ASN D CG  
14408 O OD1 . ASN D 211 ? 0.2740 0.2908 0.5447 -0.0109 -0.0516 0.0048  211 ASN D OD1 
14409 N ND2 . ASN D 211 ? 0.3300 0.3592 0.6141 -0.0108 -0.0478 0.0077  211 ASN D ND2 
14410 N N   . GLU D 212 ? 0.2756 0.3094 0.5655 0.0074  -0.0425 0.0113  212 GLU D N   
14411 C CA  . GLU D 212 ? 0.2747 0.3193 0.5747 0.0106  -0.0436 0.0161  212 GLU D CA  
14412 C C   . GLU D 212 ? 0.2696 0.3110 0.5668 0.0133  -0.0466 0.0175  212 GLU D C   
14413 O O   . GLU D 212 ? 0.2562 0.3047 0.5587 0.0126  -0.0513 0.0215  212 GLU D O   
14414 C CB  . GLU D 212 ? 0.2873 0.3370 0.5935 0.0163  -0.0377 0.0170  212 GLU D CB  
14415 C CG  . GLU D 212 ? 0.3111 0.3668 0.6220 0.0140  -0.0349 0.0170  212 GLU D CG  
14416 C CD  . GLU D 212 ? 0.3282 0.3843 0.6401 0.0195  -0.0279 0.0161  212 GLU D CD  
14417 O OE1 . GLU D 212 ? 0.3181 0.3680 0.6259 0.0249  -0.0252 0.0147  212 GLU D OE1 
14418 O OE2 . GLU D 212 ? 0.2955 0.3575 0.6115 0.0180  -0.0251 0.0168  212 GLU D OE2 
14419 N N   . LEU D 213 ? 0.2614 0.2919 0.5499 0.0157  -0.0443 0.0147  213 LEU D N   
14420 C CA  . LEU D 213 ? 0.2754 0.3017 0.5602 0.0179  -0.0469 0.0163  213 LEU D CA  
14421 C C   . LEU D 213 ? 0.2724 0.2973 0.5523 0.0125  -0.0531 0.0168  213 LEU D C   
14422 O O   . LEU D 213 ? 0.2656 0.2917 0.5454 0.0134  -0.0572 0.0199  213 LEU D O   
14423 C CB  . LEU D 213 ? 0.2858 0.3001 0.5617 0.0205  -0.0431 0.0131  213 LEU D CB  
14424 C CG  . LEU D 213 ? 0.2983 0.3114 0.5769 0.0268  -0.0379 0.0130  213 LEU D CG  
14425 C CD1 . LEU D 213 ? 0.2906 0.2910 0.5593 0.0267  -0.0347 0.0089  213 LEU D CD1 
14426 C CD2 . LEU D 213 ? 0.2760 0.2925 0.5599 0.0329  -0.0387 0.0173  213 LEU D CD2 
14427 N N   . ASN D 214 ? 0.2863 0.3079 0.5613 0.0071  -0.0538 0.0137  214 ASN D N   
14428 C CA  . ASN D 214 ? 0.2775 0.2958 0.5459 0.0019  -0.0591 0.0134  214 ASN D CA  
14429 C C   . ASN D 214 ? 0.2815 0.3101 0.5575 -0.0011 -0.0648 0.0173  214 ASN D C   
14430 O O   . ASN D 214 ? 0.2833 0.3099 0.5539 -0.0048 -0.0704 0.0180  214 ASN D O   
14431 C CB  . ASN D 214 ? 0.2724 0.2826 0.5325 -0.0020 -0.0576 0.0088  214 ASN D CB  
14432 C CG  . ASN D 214 ? 0.2710 0.2714 0.5226 0.0000  -0.0536 0.0058  214 ASN D CG  
14433 O OD1 . ASN D 214 ? 0.2628 0.2598 0.5112 0.0026  -0.0536 0.0068  214 ASN D OD1 
14434 N ND2 . ASN D 214 ? 0.2796 0.2752 0.5273 -0.0017 -0.0506 0.0022  214 ASN D ND2 
14435 N N   . GLY D 215 ? 0.2651 0.3048 0.5532 0.0003  -0.0634 0.0199  215 GLY D N   
14436 C CA  . GLY D 215 ? 0.2796 0.3317 0.5777 -0.0018 -0.0686 0.0249  215 GLY D CA  
14437 C C   . GLY D 215 ? 0.2894 0.3476 0.5930 -0.0076 -0.0699 0.0253  215 GLY D C   
14438 O O   . GLY D 215 ? 0.3007 0.3702 0.6135 -0.0103 -0.0743 0.0297  215 GLY D O   
14439 N N   . LEU D 216 ? 0.3099 0.3610 0.6081 -0.0097 -0.0662 0.0211  216 LEU D N   
14440 C CA  . LEU D 216 ? 0.3009 0.3558 0.6031 -0.0152 -0.0670 0.0213  216 LEU D CA  
14441 C C   . LEU D 216 ? 0.2935 0.3503 0.5951 -0.0223 -0.0751 0.0232  216 LEU D C   
14442 O O   . LEU D 216 ? 0.2918 0.3572 0.6016 -0.0268 -0.0775 0.0262  216 LEU D O   
14443 C CB  . LEU D 216 ? 0.3078 0.3758 0.6237 -0.0124 -0.0630 0.0249  216 LEU D CB  
14444 C CG  . LEU D 216 ? 0.2703 0.3365 0.5864 -0.0054 -0.0551 0.0230  216 LEU D CG  
14445 C CD1 . LEU D 216 ? 0.2480 0.3277 0.5771 -0.0022 -0.0511 0.0269  216 LEU D CD1 
14446 C CD2 . LEU D 216 ? 0.2671 0.3220 0.5736 -0.0073 -0.0520 0.0180  216 LEU D CD2 
14447 N N   . ASP D 217 ? 0.3132 0.3608 0.6037 -0.0240 -0.0793 0.0214  217 ASP D N   
14448 C CA  . ASP D 217 ? 0.3298 0.3771 0.6170 -0.0311 -0.0874 0.0226  217 ASP D CA  
14449 C C   . ASP D 217 ? 0.3449 0.3763 0.6165 -0.0356 -0.0884 0.0171  217 ASP D C   
14450 O O   . ASP D 217 ? 0.3477 0.3748 0.6125 -0.0415 -0.0950 0.0169  217 ASP D O   
14451 C CB  . ASP D 217 ? 0.3166 0.3685 0.6046 -0.0295 -0.0926 0.0261  217 ASP D CB  
14452 C CG  . ASP D 217 ? 0.3411 0.3830 0.6187 -0.0244 -0.0900 0.0236  217 ASP D CG  
14453 O OD1 . ASP D 217 ? 0.3452 0.3775 0.6157 -0.0222 -0.0842 0.0191  217 ASP D OD1 
14454 O OD2 . ASP D 217 ? 0.3962 0.4409 0.6737 -0.0225 -0.0938 0.0267  217 ASP D OD2 
14455 N N   . LYS D 218 ? 0.3616 0.3836 0.6268 -0.0328 -0.0821 0.0127  218 LYS D N   
14456 C CA  . LYS D 218 ? 0.3613 0.3687 0.6125 -0.0360 -0.0823 0.0078  218 LYS D CA  
14457 C C   . LYS D 218 ? 0.3297 0.3338 0.5818 -0.0348 -0.0762 0.0052  218 LYS D C   
14458 O O   . LYS D 218 ? 0.3545 0.3662 0.6157 -0.0307 -0.0717 0.0067  218 LYS D O   
14459 C CB  . LYS D 218 ? 0.4120 0.4088 0.6503 -0.0332 -0.0812 0.0046  218 LYS D CB  
14460 C CG  . LYS D 218 ? 0.4676 0.4656 0.7022 -0.0346 -0.0874 0.0069  218 LYS D CG  
14461 C CD  . LYS D 218 ? 0.5087 0.4980 0.7316 -0.0313 -0.0860 0.0050  218 LYS D CD  
14462 C CE  . LYS D 218 ? 0.5163 0.5074 0.7356 -0.0337 -0.0934 0.0079  218 LYS D CE  
14463 N NZ  . LYS D 218 ? 0.5418 0.5262 0.7516 -0.0299 -0.0913 0.0070  218 LYS D NZ  
14464 N N   . PRO D 219 ? 0.3061 0.2991 0.5490 -0.0382 -0.0763 0.0017  219 PRO D N   
14465 C CA  . PRO D 219 ? 0.2857 0.2744 0.5283 -0.0365 -0.0707 -0.0006 219 PRO D CA  
14466 C C   . PRO D 219 ? 0.2817 0.2679 0.5217 -0.0301 -0.0649 -0.0028 219 PRO D C   
14467 O O   . PRO D 219 ? 0.3044 0.2858 0.5371 -0.0281 -0.0652 -0.0042 219 PRO D O   
14468 C CB  . PRO D 219 ? 0.3068 0.2819 0.5376 -0.0407 -0.0727 -0.0041 219 PRO D CB  
14469 C CG  . PRO D 219 ? 0.3200 0.2954 0.5486 -0.0469 -0.0805 -0.0025 219 PRO D CG  
14470 C CD  . PRO D 219 ? 0.3298 0.3133 0.5620 -0.0441 -0.0822 0.0000  219 PRO D CD  
14471 N N   . PHE D 220 ? 0.2754 0.2642 0.5205 -0.0273 -0.0598 -0.0030 220 PHE D N   
14472 C CA  . PHE D 220 ? 0.2697 0.2558 0.5123 -0.0221 -0.0545 -0.0050 220 PHE D CA  
14473 C C   . PHE D 220 ? 0.2662 0.2449 0.5042 -0.0221 -0.0514 -0.0078 220 PHE D C   
14474 O O   . PHE D 220 ? 0.2353 0.2160 0.4775 -0.0241 -0.0510 -0.0068 220 PHE D O   
14475 C CB  . PHE D 220 ? 0.2490 0.2449 0.5015 -0.0184 -0.0515 -0.0027 220 PHE D CB  
14476 C CG  . PHE D 220 ? 0.2842 0.2777 0.5352 -0.0142 -0.0461 -0.0047 220 PHE D CG  
14477 C CD1 . PHE D 220 ? 0.3250 0.3115 0.5684 -0.0123 -0.0448 -0.0070 220 PHE D CD1 
14478 C CD2 . PHE D 220 ? 0.2931 0.2911 0.5497 -0.0124 -0.0425 -0.0041 220 PHE D CD2 
14479 C CE1 . PHE D 220 ? 0.3133 0.2984 0.5560 -0.0091 -0.0404 -0.0084 220 PHE D CE1 
14480 C CE2 . PHE D 220 ? 0.2910 0.2862 0.5454 -0.0093 -0.0383 -0.0059 220 PHE D CE2 
14481 C CZ  . PHE D 220 ? 0.2966 0.2858 0.5447 -0.0078 -0.0376 -0.0080 220 PHE D CZ  
14482 N N   . ILE D 221 ? 0.2712 0.2422 0.5012 -0.0198 -0.0489 -0.0107 221 ILE D N   
14483 C CA  . ILE D 221 ? 0.2716 0.2366 0.4980 -0.0186 -0.0455 -0.0129 221 ILE D CA  
14484 C C   . ILE D 221 ? 0.2754 0.2415 0.5020 -0.0142 -0.0411 -0.0137 221 ILE D C   
14485 O O   . ILE D 221 ? 0.2567 0.2243 0.4825 -0.0127 -0.0411 -0.0135 221 ILE D O   
14486 C CB  . ILE D 221 ? 0.2714 0.2252 0.4871 -0.0204 -0.0470 -0.0155 221 ILE D CB  
14487 C CG1 . ILE D 221 ? 0.2767 0.2261 0.4847 -0.0182 -0.0461 -0.0172 221 ILE D CG1 
14488 C CG2 . ILE D 221 ? 0.2752 0.2275 0.4901 -0.0258 -0.0525 -0.0145 221 ILE D CG2 
14489 C CD1 . ILE D 221 ? 0.3045 0.2422 0.5006 -0.0186 -0.0461 -0.0202 221 ILE D CD1 
14490 N N   . THR D 222 ? 0.2589 0.2243 0.4867 -0.0125 -0.0378 -0.0144 222 THR D N   
14491 C CA  . THR D 222 ? 0.2667 0.2324 0.4939 -0.0092 -0.0341 -0.0153 222 THR D CA  
14492 C C   . THR D 222 ? 0.3002 0.2586 0.5203 -0.0080 -0.0324 -0.0174 222 THR D C   
14493 O O   . THR D 222 ? 0.2998 0.2530 0.5170 -0.0087 -0.0327 -0.0183 222 THR D O   
14494 C CB  . THR D 222 ? 0.2589 0.2296 0.4920 -0.0079 -0.0317 -0.0145 222 THR D CB  
14495 O OG1 . THR D 222 ? 0.2658 0.2335 0.4982 -0.0085 -0.0312 -0.0147 222 THR D OG1 
14496 C CG2 . THR D 222 ? 0.2604 0.2380 0.5000 -0.0084 -0.0325 -0.0125 222 THR D CG2 
14497 N N   . THR D 223 ? 0.3140 0.2719 0.5313 -0.0061 -0.0305 -0.0180 223 THR D N   
14498 C CA  . THR D 223 ? 0.3073 0.2592 0.5179 -0.0045 -0.0283 -0.0197 223 THR D CA  
14499 C C   . THR D 223 ? 0.3039 0.2588 0.5178 -0.0018 -0.0244 -0.0195 223 THR D C   
14500 O O   . THR D 223 ? 0.2842 0.2360 0.4944 0.0004  -0.0217 -0.0203 223 THR D O   
14501 C CB  . THR D 223 ? 0.3093 0.2581 0.5132 -0.0046 -0.0289 -0.0202 223 THR D CB  
14502 O OG1 . THR D 223 ? 0.2882 0.2424 0.4959 -0.0043 -0.0287 -0.0187 223 THR D OG1 
14503 C CG2 . THR D 223 ? 0.3014 0.2457 0.5002 -0.0075 -0.0332 -0.0207 223 THR D CG2 
14504 N N   . ALA D 224 ? 0.2941 0.2553 0.5150 -0.0018 -0.0242 -0.0181 224 ALA D N   
14505 C CA  . ALA D 224 ? 0.2754 0.2401 0.5000 -0.0001 -0.0217 -0.0176 224 ALA D CA  
14506 C C   . ALA D 224 ? 0.2682 0.2384 0.4986 -0.0009 -0.0223 -0.0164 224 ALA D C   
14507 O O   . ALA D 224 ? 0.2343 0.2063 0.4662 -0.0020 -0.0238 -0.0160 224 ALA D O   
14508 C CB  . ALA D 224 ? 0.3029 0.2688 0.5263 0.0012  -0.0192 -0.0175 224 ALA D CB  
14509 N N   . PHE D 225 ? 0.2686 0.2413 0.5021 -0.0001 -0.0212 -0.0158 225 PHE D N   
14510 C CA  . PHE D 225 ? 0.2673 0.2446 0.5046 -0.0006 -0.0214 -0.0149 225 PHE D CA  
14511 C C   . PHE D 225 ? 0.2898 0.2691 0.5291 0.0005  -0.0205 -0.0140 225 PHE D C   
14512 O O   . PHE D 225 ? 0.3526 0.3292 0.5911 0.0016  -0.0202 -0.0138 225 PHE D O   
14513 C CB  . PHE D 225 ? 0.2558 0.2339 0.4945 -0.0018 -0.0228 -0.0145 225 PHE D CB  
14514 C CG  . PHE D 225 ? 0.2573 0.2331 0.4958 -0.0024 -0.0236 -0.0140 225 PHE D CG  
14515 C CD1 . PHE D 225 ? 0.2498 0.2215 0.4858 -0.0035 -0.0251 -0.0145 225 PHE D CD1 
14516 C CD2 . PHE D 225 ? 0.2710 0.2483 0.5114 -0.0024 -0.0234 -0.0129 225 PHE D CD2 
14517 C CE1 . PHE D 225 ? 0.2436 0.2121 0.4789 -0.0048 -0.0262 -0.0140 225 PHE D CE1 
14518 C CE2 . PHE D 225 ? 0.2564 0.2308 0.4963 -0.0033 -0.0242 -0.0120 225 PHE D CE2 
14519 C CZ  . PHE D 225 ? 0.2459 0.2157 0.4834 -0.0047 -0.0256 -0.0126 225 PHE D CZ  
14520 N N   . GLY D 226 ? 0.2609 0.2444 0.5026 0.0001  -0.0204 -0.0134 226 GLY D N   
14521 C CA  . GLY D 226 ? 0.2519 0.2382 0.4958 0.0010  -0.0202 -0.0120 226 GLY D CA  
14522 C C   . GLY D 226 ? 0.2481 0.2390 0.4940 -0.0001 -0.0204 -0.0113 226 GLY D C   
14523 O O   . GLY D 226 ? 0.2280 0.2186 0.4728 -0.0017 -0.0207 -0.0122 226 GLY D O   
14524 N N   . TYR D 227 ? 0.2267 0.2215 0.4755 0.0007  -0.0205 -0.0096 227 TYR D N   
14525 C CA  . TYR D 227 ? 0.2113 0.2112 0.4624 -0.0010 -0.0218 -0.0084 227 TYR D CA  
14526 C C   . TYR D 227 ? 0.2267 0.2319 0.4824 0.0008  -0.0210 -0.0062 227 TYR D C   
14527 O O   . TYR D 227 ? 0.2097 0.2143 0.4666 0.0039  -0.0199 -0.0052 227 TYR D O   
14528 C CB  . TYR D 227 ? 0.2262 0.2265 0.4757 -0.0022 -0.0237 -0.0081 227 TYR D CB  
14529 C CG  . TYR D 227 ? 0.2283 0.2245 0.4738 -0.0035 -0.0238 -0.0101 227 TYR D CG  
14530 C CD1 . TYR D 227 ? 0.2209 0.2159 0.4642 -0.0055 -0.0242 -0.0115 227 TYR D CD1 
14531 C CD2 . TYR D 227 ? 0.2122 0.2056 0.4562 -0.0026 -0.0232 -0.0104 227 TYR D CD2 
14532 C CE1 . TYR D 227 ? 0.2124 0.2036 0.4524 -0.0057 -0.0237 -0.0131 227 TYR D CE1 
14533 C CE2 . TYR D 227 ? 0.2199 0.2110 0.4616 -0.0032 -0.0228 -0.0117 227 TYR D CE2 
14534 C CZ  . TYR D 227 ? 0.2359 0.2260 0.4757 -0.0043 -0.0228 -0.0131 227 TYR D CZ  
14535 O OH  . TYR D 227 ? 0.2704 0.2583 0.5081 -0.0040 -0.0220 -0.0143 227 TYR D OH  
14536 N N   . SER D 228 ? 0.2283 0.2385 0.4868 -0.0013 -0.0216 -0.0052 228 SER D N   
14537 C CA  . SER D 228 ? 0.2148 0.2326 0.4794 -0.0002 -0.0209 -0.0024 228 SER D CA  
14538 C C   . SER D 228 ? 0.2365 0.2601 0.5042 -0.0017 -0.0240 -0.0001 228 SER D C   
14539 O O   . SER D 228 ? 0.2293 0.2519 0.4941 -0.0054 -0.0267 -0.0010 228 SER D O   
14540 C CB  . SER D 228 ? 0.2128 0.2333 0.4790 -0.0026 -0.0199 -0.0021 228 SER D CB  
14541 O OG  . SER D 228 ? 0.2091 0.2388 0.4825 -0.0019 -0.0191 0.0012  228 SER D OG  
14542 N N   . VAL D 229 ? 0.2292 0.2588 0.5024 0.0014  -0.0237 0.0029  229 VAL D N   
14543 C CA  . VAL D 229 ? 0.2366 0.2729 0.5134 0.0003  -0.0271 0.0058  229 VAL D CA  
14544 C C   . VAL D 229 ? 0.2357 0.2831 0.5209 -0.0007 -0.0276 0.0093  229 VAL D C   
14545 O O   . VAL D 229 ? 0.2044 0.2597 0.4953 0.0004  -0.0296 0.0130  229 VAL D O   
14546 C CB  . VAL D 229 ? 0.2527 0.2876 0.5297 0.0045  -0.0271 0.0074  229 VAL D CB  
14547 C CG1 . VAL D 229 ? 0.2478 0.2730 0.5171 0.0044  -0.0270 0.0047  229 VAL D CG1 
14548 C CG2 . VAL D 229 ? 0.2614 0.2980 0.5429 0.0103  -0.0236 0.0092  229 VAL D CG2 
14549 N N   . SER D 230 ? 0.2458 0.2944 0.5320 -0.0031 -0.0261 0.0086  230 SER D N   
14550 C CA  . SER D 230 ? 0.2428 0.3024 0.5372 -0.0052 -0.0266 0.0122  230 SER D CA  
14551 C C   . SER D 230 ? 0.2420 0.3076 0.5386 -0.0099 -0.0322 0.0143  230 SER D C   
14552 O O   . SER D 230 ? 0.2439 0.3030 0.5332 -0.0131 -0.0353 0.0119  230 SER D O   
14553 C CB  . SER D 230 ? 0.2512 0.3094 0.5446 -0.0085 -0.0247 0.0110  230 SER D CB  
14554 O OG  . SER D 230 ? 0.2781 0.3282 0.5639 -0.0132 -0.0273 0.0078  230 SER D OG  
14555 N N   . PRO D 231 ? 0.2270 0.3054 0.5334 -0.0098 -0.0335 0.0191  231 PRO D N   
14556 C CA  . PRO D 231 ? 0.2249 0.3102 0.5339 -0.0149 -0.0395 0.0217  231 PRO D CA  
14557 C C   . PRO D 231 ? 0.2428 0.3233 0.5459 -0.0228 -0.0427 0.0193  231 PRO D C   
14558 O O   . PRO D 231 ? 0.2463 0.3247 0.5444 -0.0270 -0.0477 0.0186  231 PRO D O   
14559 C CB  . PRO D 231 ? 0.2337 0.3347 0.5559 -0.0137 -0.0393 0.0275  231 PRO D CB  
14560 C CG  . PRO D 231 ? 0.2479 0.3488 0.5734 -0.0051 -0.0331 0.0280  231 PRO D CG  
14561 C CD  . PRO D 231 ? 0.2336 0.3202 0.5489 -0.0040 -0.0293 0.0225  231 PRO D CD  
14562 N N   . GLU D 232 ? 0.2715 0.3502 0.5749 -0.0245 -0.0396 0.0182  232 GLU D N   
14563 C CA  . GLU D 232 ? 0.3134 0.3857 0.6107 -0.0316 -0.0420 0.0158  232 GLU D CA  
14564 C C   . GLU D 232 ? 0.2814 0.3468 0.5757 -0.0308 -0.0373 0.0134  232 GLU D C   
14565 O O   . GLU D 232 ? 0.2622 0.3273 0.5580 -0.0249 -0.0324 0.0132  232 GLU D O   
14566 C CB  . GLU D 232 ? 0.3485 0.4312 0.6524 -0.0385 -0.0469 0.0197  232 GLU D CB  
14567 C CG  . GLU D 232 ? 0.3987 0.4956 0.7158 -0.0378 -0.0442 0.0249  232 GLU D CG  
14568 C CD  . GLU D 232 ? 0.4264 0.5369 0.7530 -0.0444 -0.0490 0.0300  232 GLU D CD  
14569 O OE1 . GLU D 232 ? 0.4845 0.5928 0.8071 -0.0522 -0.0552 0.0296  232 GLU D OE1 
14570 O OE2 . GLU D 232 ? 0.4358 0.5599 0.7745 -0.0413 -0.0460 0.0348  232 GLU D OE2 
14571 N N   . GLY D 233 ? 0.2688 0.3267 0.5570 -0.0365 -0.0390 0.0113  233 GLY D N   
14572 C CA  . GLY D 233 ? 0.2541 0.3054 0.5391 -0.0366 -0.0353 0.0096  233 GLY D CA  
14573 C C   . GLY D 233 ? 0.2543 0.2918 0.5288 -0.0336 -0.0338 0.0047  233 GLY D C   
14574 O O   . GLY D 233 ? 0.2749 0.3089 0.5455 -0.0311 -0.0350 0.0028  233 GLY D O   
14575 N N   . GLY D 234 ? 0.2482 0.2790 0.5191 -0.0338 -0.0311 0.0033  234 GLY D N   
14576 C CA  . GLY D 234 ? 0.2706 0.2893 0.5327 -0.0315 -0.0299 -0.0007 234 GLY D CA  
14577 C C   . GLY D 234 ? 0.2921 0.3015 0.5463 -0.0357 -0.0333 -0.0033 234 GLY D C   
14578 O O   . GLY D 234 ? 0.2751 0.2845 0.5291 -0.0414 -0.0360 -0.0022 234 GLY D O   
14579 N N   . ASN D 235 ? 0.3188 0.3194 0.5659 -0.0328 -0.0328 -0.0067 235 ASN D N   
14580 C CA  A ASN D 235 ? 0.3260 0.3166 0.5645 -0.0355 -0.0352 -0.0096 235 ASN D CA  
14581 C CA  B ASN D 235 ? 0.3304 0.3207 0.5688 -0.0354 -0.0350 -0.0096 235 ASN D CA  
14582 C C   . ASN D 235 ? 0.3223 0.3086 0.5561 -0.0310 -0.0343 -0.0123 235 ASN D C   
14583 O O   . ASN D 235 ? 0.2731 0.2590 0.5080 -0.0263 -0.0314 -0.0128 235 ASN D O   
14584 C CB  A ASN D 235 ? 0.3276 0.3089 0.5612 -0.0377 -0.0346 -0.0106 235 ASN D CB  
14585 C CB  B ASN D 235 ? 0.3349 0.3165 0.5690 -0.0374 -0.0342 -0.0104 235 ASN D CB  
14586 C CG  A ASN D 235 ? 0.3353 0.3048 0.5590 -0.0393 -0.0365 -0.0140 235 ASN D CG  
14587 C CG  B ASN D 235 ? 0.3365 0.3128 0.5684 -0.0324 -0.0308 -0.0118 235 ASN D CG  
14588 O OD1 A ASN D 235 ? 0.3200 0.2877 0.5404 -0.0440 -0.0400 -0.0145 235 ASN D OD1 
14589 O OD1 B ASN D 235 ? 0.3713 0.3528 0.6078 -0.0293 -0.0283 -0.0103 235 ASN D OD1 
14590 N ND2 A ASN D 235 ? 0.3405 0.3017 0.5591 -0.0351 -0.0342 -0.0164 235 ASN D ND2 
14591 N ND2 B ASN D 235 ? 0.3262 0.2920 0.5508 -0.0313 -0.0308 -0.0145 235 ASN D ND2 
14592 N N   . GLY D 236 ? 0.3253 0.3085 0.5537 -0.0328 -0.0369 -0.0138 236 GLY D N   
14593 C CA  . GLY D 236 ? 0.3318 0.3121 0.5558 -0.0292 -0.0360 -0.0158 236 GLY D CA  
14594 C C   . GLY D 236 ? 0.3349 0.3235 0.5656 -0.0252 -0.0345 -0.0139 236 GLY D C   
14595 O O   . GLY D 236 ? 0.3082 0.3052 0.5445 -0.0259 -0.0360 -0.0112 236 GLY D O   
14596 N N   . GLN D 237 ? 0.2816 0.2676 0.5116 -0.0209 -0.0316 -0.0150 237 GLN D N   
14597 C CA  . GLN D 237 ? 0.2835 0.2748 0.5180 -0.0174 -0.0303 -0.0136 237 GLN D CA  
14598 C C   . GLN D 237 ? 0.2852 0.2810 0.5261 -0.0160 -0.0286 -0.0119 237 GLN D C   
14599 O O   . GLN D 237 ? 0.2790 0.2777 0.5230 -0.0129 -0.0274 -0.0109 237 GLN D O   
14600 C CB  . GLN D 237 ? 0.2911 0.2779 0.5224 -0.0141 -0.0281 -0.0154 237 GLN D CB  
14601 C CG  . GLN D 237 ? 0.2904 0.2745 0.5160 -0.0142 -0.0287 -0.0166 237 GLN D CG  
14602 C CD  . GLN D 237 ? 0.2956 0.2779 0.5203 -0.0108 -0.0261 -0.0173 237 GLN D CD  
14603 O OE1 . GLN D 237 ? 0.2725 0.2584 0.5008 -0.0090 -0.0253 -0.0159 237 GLN D OE1 
14604 N NE2 . GLN D 237 ? 0.2917 0.2683 0.5115 -0.0100 -0.0248 -0.0194 237 GLN D NE2 
14605 N N   . TYR D 238 ? 0.2808 0.2757 0.5224 -0.0179 -0.0283 -0.0116 238 TYR D N   
14606 C CA  . TYR D 238 ? 0.2812 0.2802 0.5278 -0.0167 -0.0263 -0.0099 238 TYR D CA  
14607 C C   . TYR D 238 ? 0.2784 0.2860 0.5310 -0.0187 -0.0275 -0.0070 238 TYR D C   
14608 O O   . TYR D 238 ? 0.2884 0.2973 0.5414 -0.0231 -0.0297 -0.0061 238 TYR D O   
14609 C CB  . TYR D 238 ? 0.2972 0.2919 0.5420 -0.0178 -0.0250 -0.0102 238 TYR D CB  
14610 C CG  . TYR D 238 ? 0.2948 0.2940 0.5438 -0.0166 -0.0226 -0.0083 238 TYR D CG  
14611 C CD1 . TYR D 238 ? 0.2755 0.2743 0.5245 -0.0125 -0.0204 -0.0087 238 TYR D CD1 
14612 C CD2 . TYR D 238 ? 0.2989 0.3027 0.5515 -0.0197 -0.0224 -0.0059 238 TYR D CD2 
14613 C CE1 . TYR D 238 ? 0.2731 0.2749 0.5243 -0.0111 -0.0178 -0.0072 238 TYR D CE1 
14614 C CE2 . TYR D 238 ? 0.2750 0.2834 0.5311 -0.0182 -0.0195 -0.0039 238 TYR D CE2 
14615 C CZ  . TYR D 238 ? 0.2776 0.2845 0.5323 -0.0135 -0.0169 -0.0048 238 TYR D CZ  
14616 O OH  . TYR D 238 ? 0.2849 0.2948 0.5412 -0.0115 -0.0136 -0.0034 238 TYR D OH  
14617 N N   . GLY D 239 ? 0.2743 0.2877 0.5318 -0.0153 -0.0262 -0.0053 239 GLY D N   
14618 C CA  . GLY D 239 ? 0.2809 0.3036 0.5449 -0.0159 -0.0275 -0.0021 239 GLY D CA  
14619 C C   . GLY D 239 ? 0.2561 0.2797 0.5185 -0.0174 -0.0311 -0.0019 239 GLY D C   
14620 O O   . GLY D 239 ? 0.2556 0.2723 0.5114 -0.0182 -0.0322 -0.0045 239 GLY D O   
14621 N N   . SER D 240 ? 0.2670 0.2996 0.5357 -0.0172 -0.0327 0.0014  240 SER D N   
14622 C CA  . SER D 240 ? 0.2721 0.3081 0.5405 -0.0200 -0.0371 0.0028  240 SER D CA  
14623 C C   . SER D 240 ? 0.2734 0.3042 0.5358 -0.0181 -0.0379 0.0012  240 SER D C   
14624 O O   . SER D 240 ? 0.2958 0.3259 0.5540 -0.0211 -0.0415 0.0011  240 SER D O   
14625 C CB  . SER D 240 ? 0.2805 0.3148 0.5457 -0.0266 -0.0404 0.0020  240 SER D CB  
14626 O OG  . SER D 240 ? 0.2672 0.3092 0.5398 -0.0291 -0.0403 0.0048  240 SER D OG  
14627 N N   . ASN D 241 ? 0.2778 0.3049 0.5393 -0.0134 -0.0348 0.0003  241 ASN D N   
14628 C CA  . ASN D 241 ? 0.2723 0.2956 0.5290 -0.0118 -0.0355 -0.0002 241 ASN D CA  
14629 C C   . ASN D 241 ? 0.2471 0.2769 0.5083 -0.0098 -0.0372 0.0036  241 ASN D C   
14630 O O   . ASN D 241 ? 0.2195 0.2559 0.4881 -0.0077 -0.0365 0.0062  241 ASN D O   
14631 C CB  . ASN D 241 ? 0.2999 0.3168 0.5542 -0.0085 -0.0321 -0.0022 241 ASN D CB  
14632 C CG  . ASN D 241 ? 0.2934 0.3040 0.5429 -0.0101 -0.0308 -0.0055 241 ASN D CG  
14633 O OD1 . ASN D 241 ? 0.2956 0.3015 0.5394 -0.0110 -0.0312 -0.0074 241 ASN D OD1 
14634 N ND2 . ASN D 241 ? 0.3198 0.3304 0.5716 -0.0102 -0.0293 -0.0060 241 ASN D ND2 
14635 N N   . THR D 242 ? 0.2636 0.2917 0.5202 -0.0102 -0.0393 0.0040  242 THR D N   
14636 C CA  . THR D 242 ? 0.2860 0.3178 0.5455 -0.0072 -0.0404 0.0076  242 THR D CA  
14637 C C   . THR D 242 ? 0.2580 0.2850 0.5181 -0.0025 -0.0367 0.0073  242 THR D C   
14638 O O   . THR D 242 ? 0.2311 0.2519 0.4879 -0.0023 -0.0340 0.0042  242 THR D O   
14639 C CB  . THR D 242 ? 0.3095 0.3398 0.5622 -0.0093 -0.0437 0.0082  242 THR D CB  
14640 O OG1 . THR D 242 ? 0.2742 0.2960 0.5196 -0.0092 -0.0413 0.0051  242 THR D OG1 
14641 C CG2 . THR D 242 ? 0.3347 0.3683 0.5854 -0.0146 -0.0479 0.0082  242 THR D CG2 
14642 N N   . LEU D 243 ? 0.2517 0.2814 0.5157 0.0013  -0.0367 0.0107  243 LEU D N   
14643 C CA  . LEU D 243 ? 0.2509 0.2746 0.5144 0.0054  -0.0338 0.0106  243 LEU D CA  
14644 C C   . LEU D 243 ? 0.2480 0.2642 0.5041 0.0037  -0.0335 0.0087  243 LEU D C   
14645 O O   . LEU D 243 ? 0.2439 0.2539 0.4981 0.0048  -0.0309 0.0068  243 LEU D O   
14646 C CB  . LEU D 243 ? 0.2819 0.3085 0.5496 0.0096  -0.0345 0.0149  243 LEU D CB  
14647 C CG  . LEU D 243 ? 0.3081 0.3434 0.5848 0.0125  -0.0341 0.0177  243 LEU D CG  
14648 C CD1 . LEU D 243 ? 0.2993 0.3366 0.5799 0.0177  -0.0345 0.0222  243 LEU D CD1 
14649 C CD2 . LEU D 243 ? 0.3187 0.3518 0.5971 0.0145  -0.0298 0.0152  243 LEU D CD2 
14650 N N   . LYS D 244 ? 0.2653 0.2827 0.5173 0.0010  -0.0362 0.0095  244 LYS D N   
14651 C CA  . LYS D 244 ? 0.2876 0.2993 0.5326 -0.0005 -0.0355 0.0081  244 LYS D CA  
14652 C C   . LYS D 244 ? 0.2889 0.2971 0.5312 -0.0025 -0.0334 0.0039  244 LYS D C   
14653 O O   . LYS D 244 ? 0.3617 0.3653 0.6016 -0.0022 -0.0312 0.0026  244 LYS D O   
14654 C CB  . LYS D 244 ? 0.3260 0.3396 0.5660 -0.0028 -0.0385 0.0097  244 LYS D CB  
14655 C CG  . LYS D 244 ? 0.3624 0.3708 0.5956 -0.0035 -0.0371 0.0095  244 LYS D CG  
14656 C CD  . LYS D 244 ? 0.4104 0.4188 0.6355 -0.0064 -0.0390 0.0093  244 LYS D CD  
14657 C CE  . LYS D 244 ? 0.4699 0.4734 0.6887 -0.0069 -0.0360 0.0081  244 LYS D CE  
14658 N NZ  . LYS D 244 ? 0.5158 0.5169 0.7377 -0.0049 -0.0338 0.0102  244 LYS D NZ  
14659 N N   . GLN D 245 ? 0.2457 0.2561 0.4884 -0.0046 -0.0342 0.0021  245 GLN D N   
14660 C CA  . GLN D 245 ? 0.2411 0.2477 0.4813 -0.0058 -0.0323 -0.0015 245 GLN D CA  
14661 C C   . GLN D 245 ? 0.2440 0.2483 0.4877 -0.0036 -0.0296 -0.0025 245 GLN D C   
14662 O O   . GLN D 245 ? 0.2353 0.2357 0.4769 -0.0036 -0.0278 -0.0045 245 GLN D O   
14663 C CB  . GLN D 245 ? 0.2321 0.2401 0.4714 -0.0087 -0.0338 -0.0032 245 GLN D CB  
14664 C CG  . GLN D 245 ? 0.2258 0.2333 0.4587 -0.0117 -0.0365 -0.0034 245 GLN D CG  
14665 C CD  . GLN D 245 ? 0.2557 0.2652 0.4888 -0.0152 -0.0392 -0.0040 245 GLN D CD  
14666 O OE1 . GLN D 245 ? 0.2340 0.2494 0.4739 -0.0156 -0.0404 -0.0020 245 GLN D OE1 
14667 N NE2 . GLN D 245 ? 0.2712 0.2754 0.4967 -0.0178 -0.0397 -0.0068 245 GLN D NE2 
14668 N N   . GLN D 246 ? 0.2463 0.2533 0.4952 -0.0014 -0.0293 -0.0009 246 GLN D N   
14669 C CA  . GLN D 246 ? 0.2401 0.2441 0.4909 0.0007  -0.0269 -0.0019 246 GLN D CA  
14670 C C   . GLN D 246 ? 0.2426 0.2412 0.4909 0.0016  -0.0259 -0.0020 246 GLN D C   
14671 O O   . GLN D 246 ? 0.2211 0.2159 0.4679 0.0012  -0.0246 -0.0039 246 GLN D O   
14672 C CB  . GLN D 246 ? 0.2392 0.2468 0.4952 0.0035  -0.0263 0.0000  246 GLN D CB  
14673 C CG  . GLN D 246 ? 0.2622 0.2652 0.5182 0.0060  -0.0235 -0.0014 246 GLN D CG  
14674 C CD  . GLN D 246 ? 0.2556 0.2604 0.5154 0.0101  -0.0220 0.0005  246 GLN D CD  
14675 O OE1 . GLN D 246 ? 0.2519 0.2583 0.5138 0.0124  -0.0228 0.0033  246 GLN D OE1 
14676 N NE2 . GLN D 246 ? 0.2552 0.2598 0.5159 0.0114  -0.0196 -0.0007 246 GLN D NE2 
14677 N N   . SER D 247 ? 0.2668 0.2653 0.5146 0.0024  -0.0269 0.0005  247 SER D N   
14678 C CA  . SER D 247 ? 0.2600 0.2534 0.5057 0.0029  -0.0262 0.0013  247 SER D CA  
14679 C C   . SER D 247 ? 0.2693 0.2614 0.5119 0.0003  -0.0257 -0.0001 247 SER D C   
14680 O O   . SER D 247 ? 0.2529 0.2415 0.4951 -0.0003 -0.0246 -0.0010 247 SER D O   
14681 C CB  . SER D 247 ? 0.2644 0.2581 0.5100 0.0042  -0.0275 0.0048  247 SER D CB  
14682 O OG  . SER D 247 ? 0.2941 0.2821 0.5376 0.0041  -0.0269 0.0059  247 SER D OG  
14683 N N   . ASP D 248 ? 0.2685 0.2635 0.5085 -0.0013 -0.0265 -0.0001 248 ASP D N   
14684 C CA  . ASP D 248 ? 0.2668 0.2610 0.5035 -0.0030 -0.0253 -0.0011 248 ASP D CA  
14685 C C   . ASP D 248 ? 0.2768 0.2700 0.5146 -0.0032 -0.0239 -0.0040 248 ASP D C   
14686 O O   . ASP D 248 ? 0.2749 0.2672 0.5126 -0.0037 -0.0225 -0.0043 248 ASP D O   
14687 C CB  . ASP D 248 ? 0.2884 0.2846 0.5207 -0.0042 -0.0262 -0.0010 248 ASP D CB  
14688 C CG  . ASP D 248 ? 0.2969 0.2939 0.5269 -0.0042 -0.0277 0.0022  248 ASP D CG  
14689 O OD1 . ASP D 248 ? 0.3294 0.3249 0.5616 -0.0031 -0.0275 0.0046  248 ASP D OD1 
14690 O OD2 . ASP D 248 ? 0.2557 0.2542 0.4812 -0.0054 -0.0292 0.0024  248 ASP D OD2 
14691 N N   . GLY D 249 ? 0.2578 0.2518 0.4970 -0.0030 -0.0244 -0.0055 249 GLY D N   
14692 C CA  . GLY D 249 ? 0.2536 0.2465 0.4935 -0.0031 -0.0235 -0.0078 249 GLY D CA  
14693 C C   . GLY D 249 ? 0.2618 0.2523 0.5038 -0.0024 -0.0228 -0.0081 249 GLY D C   
14694 O O   . GLY D 249 ? 0.2766 0.2663 0.5187 -0.0028 -0.0221 -0.0092 249 GLY D O   
14695 N N   . LEU D 250 ? 0.2592 0.2482 0.5026 -0.0013 -0.0231 -0.0070 250 LEU D N   
14696 C CA  . LEU D 250 ? 0.2638 0.2488 0.5072 -0.0010 -0.0228 -0.0074 250 LEU D CA  
14697 C C   . LEU D 250 ? 0.2500 0.2341 0.4932 -0.0027 -0.0228 -0.0066 250 LEU D C   
14698 O O   . LEU D 250 ? 0.2614 0.2443 0.5050 -0.0037 -0.0229 -0.0075 250 LEU D O   
14699 C CB  . LEU D 250 ? 0.2583 0.2401 0.5019 0.0009  -0.0227 -0.0066 250 LEU D CB  
14700 C CG  . LEU D 250 ? 0.2658 0.2469 0.5097 0.0027  -0.0218 -0.0079 250 LEU D CG  
14701 C CD1 . LEU D 250 ? 0.2623 0.2402 0.5042 0.0018  -0.0216 -0.0100 250 LEU D CD1 
14702 C CD2 . LEU D 250 ? 0.2938 0.2807 0.5398 0.0028  -0.0218 -0.0077 250 LEU D CD2 
14703 N N   . ILE D 251 ? 0.2454 0.2308 0.4881 -0.0033 -0.0227 -0.0047 251 ILE D N   
14704 C CA  . ILE D 251 ? 0.2690 0.2544 0.5120 -0.0051 -0.0224 -0.0031 251 ILE D CA  
14705 C C   . ILE D 251 ? 0.2630 0.2523 0.5068 -0.0057 -0.0212 -0.0041 251 ILE D C   
14706 O O   . ILE D 251 ? 0.2705 0.2610 0.5166 -0.0070 -0.0209 -0.0034 251 ILE D O   
14707 C CB  . ILE D 251 ? 0.2797 0.2653 0.5212 -0.0054 -0.0223 -0.0003 251 ILE D CB  
14708 C CG1 . ILE D 251 ? 0.3113 0.2927 0.5522 -0.0040 -0.0234 0.0010  251 ILE D CG1 
14709 C CG2 . ILE D 251 ? 0.2844 0.2709 0.5265 -0.0077 -0.0215 0.0018  251 ILE D CG2 
14710 C CD1 . ILE D 251 ? 0.3304 0.3056 0.5713 -0.0044 -0.0239 0.0007  251 ILE D CD1 
14711 N N   . SER D 252 ? 0.2463 0.2377 0.4886 -0.0047 -0.0206 -0.0054 252 SER D N   
14712 C CA  . SER D 252 ? 0.2464 0.2401 0.4887 -0.0043 -0.0192 -0.0065 252 SER D CA  
14713 C C   . SER D 252 ? 0.2470 0.2403 0.4919 -0.0041 -0.0196 -0.0078 252 SER D C   
14714 O O   . SER D 252 ? 0.2069 0.2027 0.4543 -0.0042 -0.0188 -0.0073 252 SER D O   
14715 C CB  . SER D 252 ? 0.2517 0.2453 0.4901 -0.0036 -0.0188 -0.0081 252 SER D CB  
14716 O OG  . SER D 252 ? 0.2628 0.2564 0.5007 -0.0026 -0.0176 -0.0098 252 SER D OG  
14717 N N   . ASN D 253 ? 0.2271 0.2177 0.4716 -0.0038 -0.0209 -0.0090 253 ASN D N   
14718 C CA  . ASN D 253 ? 0.2311 0.2206 0.4767 -0.0037 -0.0215 -0.0101 253 ASN D CA  
14719 C C   . ASN D 253 ? 0.2507 0.2398 0.4984 -0.0053 -0.0226 -0.0089 253 ASN D C   
14720 O O   . ASN D 253 ? 0.2677 0.2580 0.5172 -0.0057 -0.0233 -0.0089 253 ASN D O   
14721 C CB  . ASN D 253 ? 0.2353 0.2220 0.4796 -0.0032 -0.0222 -0.0113 253 ASN D CB  
14722 C CG  . ASN D 253 ? 0.2404 0.2277 0.4833 -0.0025 -0.0217 -0.0123 253 ASN D CG  
14723 O OD1 . ASN D 253 ? 0.2699 0.2585 0.5118 -0.0026 -0.0211 -0.0125 253 ASN D OD1 
14724 N ND2 . ASN D 253 ? 0.2243 0.2105 0.4669 -0.0022 -0.0219 -0.0127 253 ASN D ND2 
14725 N N   . TYR D 254 ? 0.2416 0.2284 0.4887 -0.0063 -0.0231 -0.0077 254 TYR D N   
14726 C CA  . TYR D 254 ? 0.2559 0.2406 0.5039 -0.0086 -0.0247 -0.0067 254 TYR D CA  
14727 C C   . TYR D 254 ? 0.2317 0.2220 0.4839 -0.0101 -0.0244 -0.0048 254 TYR D C   
14728 O O   . TYR D 254 ? 0.2620 0.2534 0.5164 -0.0118 -0.0259 -0.0044 254 TYR D O   
14729 C CB  . TYR D 254 ? 0.2690 0.2487 0.5151 -0.0094 -0.0252 -0.0056 254 TYR D CB  
14730 C CG  . TYR D 254 ? 0.2684 0.2415 0.5122 -0.0110 -0.0272 -0.0063 254 TYR D CG  
14731 C CD1 . TYR D 254 ? 0.2767 0.2498 0.5221 -0.0146 -0.0291 -0.0050 254 TYR D CD1 
14732 C CD2 . TYR D 254 ? 0.2643 0.2311 0.5041 -0.0091 -0.0272 -0.0080 254 TYR D CD2 
14733 C CE1 . TYR D 254 ? 0.2925 0.2580 0.5344 -0.0167 -0.0314 -0.0059 254 TYR D CE1 
14734 C CE2 . TYR D 254 ? 0.2942 0.2533 0.5302 -0.0104 -0.0288 -0.0090 254 TYR D CE2 
14735 C CZ  . TYR D 254 ? 0.2856 0.2432 0.5218 -0.0144 -0.0312 -0.0082 254 TYR D CZ  
14736 O OH  . TYR D 254 ? 0.2508 0.1993 0.4817 -0.0163 -0.0333 -0.0096 254 TYR D OH  
14737 N N   . ARG D 255 ? 0.2213 0.2156 0.4743 -0.0095 -0.0223 -0.0035 255 ARG D N   
14738 C CA  . ARG D 255 ? 0.2297 0.2304 0.4869 -0.0102 -0.0210 -0.0014 255 ARG D CA  
14739 C C   . ARG D 255 ? 0.2284 0.2326 0.4882 -0.0085 -0.0207 -0.0024 255 ARG D C   
14740 O O   . ARG D 255 ? 0.2031 0.2113 0.4675 -0.0097 -0.0217 -0.0009 255 ARG D O   
14741 C CB  . ARG D 255 ? 0.2404 0.2432 0.4958 -0.0092 -0.0182 -0.0004 255 ARG D CB  
14742 C CG  . ARG D 255 ? 0.2597 0.2694 0.5181 -0.0086 -0.0153 0.0014  255 ARG D CG  
14743 C CD  . ARG D 255 ? 0.2936 0.3072 0.5569 -0.0119 -0.0155 0.0051  255 ARG D CD  
14744 N NE  . ARG D 255 ? 0.2787 0.2952 0.5476 -0.0137 -0.0177 0.0059  255 ARG D NE  
14745 C CZ  . ARG D 255 ? 0.3152 0.3306 0.5867 -0.0178 -0.0207 0.0075  255 ARG D CZ  
14746 N NH1 . ARG D 255 ? 0.2965 0.3060 0.5650 -0.0206 -0.0220 0.0085  255 ARG D NH1 
14747 N NH2 . ARG D 255 ? 0.3217 0.3414 0.5983 -0.0190 -0.0227 0.0083  255 ARG D NH2 
14748 N N   . ASP D 256 ? 0.2413 0.2439 0.4980 -0.0057 -0.0196 -0.0047 256 ASP D N   
14749 C CA  . ASP D 256 ? 0.2434 0.2481 0.5016 -0.0035 -0.0189 -0.0055 256 ASP D CA  
14750 C C   . ASP D 256 ? 0.2498 0.2541 0.5103 -0.0047 -0.0218 -0.0053 256 ASP D C   
14751 O O   . ASP D 256 ? 0.2380 0.2469 0.5028 -0.0040 -0.0221 -0.0040 256 ASP D O   
14752 C CB  . ASP D 256 ? 0.2512 0.2520 0.5045 -0.0013 -0.0179 -0.0080 256 ASP D CB  
14753 C CG  . ASP D 256 ? 0.2564 0.2574 0.5065 -0.0002 -0.0154 -0.0084 256 ASP D CG  
14754 O OD1 . ASP D 256 ? 0.2865 0.2913 0.5383 -0.0005 -0.0137 -0.0064 256 ASP D OD1 
14755 O OD2 . ASP D 256 ? 0.2799 0.2772 0.5254 0.0006  -0.0151 -0.0104 256 ASP D OD2 
14756 N N   . LEU D 257 ? 0.2533 0.2522 0.5106 -0.0062 -0.0240 -0.0065 257 LEU D N   
14757 C CA  . LEU D 257 ? 0.2534 0.2507 0.5106 -0.0072 -0.0268 -0.0069 257 LEU D CA  
14758 C C   . LEU D 257 ? 0.2664 0.2669 0.5277 -0.0104 -0.0290 -0.0045 257 LEU D C   
14759 O O   . LEU D 257 ? 0.2685 0.2719 0.5325 -0.0109 -0.0311 -0.0036 257 LEU D O   
14760 C CB  . LEU D 257 ? 0.2597 0.2500 0.5114 -0.0075 -0.0277 -0.0090 257 LEU D CB  
14761 C CG  . LEU D 257 ? 0.2610 0.2493 0.5097 -0.0050 -0.0259 -0.0108 257 LEU D CG  
14762 C CD1 . LEU D 257 ? 0.2557 0.2388 0.5003 -0.0050 -0.0259 -0.0122 257 LEU D CD1 
14763 C CD2 . LEU D 257 ? 0.2419 0.2310 0.4908 -0.0036 -0.0262 -0.0111 257 LEU D CD2 
14764 N N   . ILE D 258 ? 0.2755 0.2759 0.5376 -0.0127 -0.0289 -0.0032 258 ILE D N   
14765 C CA  . ILE D 258 ? 0.2735 0.2781 0.5404 -0.0164 -0.0310 -0.0004 258 ILE D CA  
14766 C C   . ILE D 258 ? 0.2572 0.2718 0.5314 -0.0148 -0.0295 0.0019  258 ILE D C   
14767 O O   . ILE D 258 ? 0.2647 0.2844 0.5438 -0.0165 -0.0320 0.0040  258 ILE D O   
14768 C CB  . ILE D 258 ? 0.2702 0.2732 0.5371 -0.0192 -0.0305 0.0013  258 ILE D CB  
14769 C CG1 . ILE D 258 ? 0.2945 0.2867 0.5544 -0.0205 -0.0322 -0.0008 258 ILE D CG1 
14770 C CG2 . ILE D 258 ? 0.2594 0.2685 0.5326 -0.0235 -0.0322 0.0049  258 ILE D CG2 
14771 C CD1 . ILE D 258 ? 0.2746 0.2634 0.5334 -0.0227 -0.0318 0.0010  258 ILE D CD1 
14772 N N   . ASP D 259 ? 0.2607 0.2780 0.5351 -0.0112 -0.0255 0.0017  259 ASP D N   
14773 C CA  . ASP D 259 ? 0.2859 0.3120 0.5664 -0.0087 -0.0230 0.0039  259 ASP D CA  
14774 C C   . ASP D 259 ? 0.2584 0.2866 0.5413 -0.0063 -0.0243 0.0037  259 ASP D C   
14775 O O   . ASP D 259 ? 0.2394 0.2759 0.5290 -0.0043 -0.0230 0.0062  259 ASP D O   
14776 C CB  . ASP D 259 ? 0.3017 0.3278 0.5795 -0.0054 -0.0183 0.0030  259 ASP D CB  
14777 C CG  . ASP D 259 ? 0.3217 0.3484 0.5987 -0.0076 -0.0166 0.0046  259 ASP D CG  
14778 O OD1 . ASP D 259 ? 0.3041 0.3356 0.5863 -0.0112 -0.0176 0.0078  259 ASP D OD1 
14779 O OD2 . ASP D 259 ? 0.3047 0.3274 0.5760 -0.0059 -0.0144 0.0029  259 ASP D OD2 
14780 N N   . ALA D 260 ? 0.2658 0.2870 0.5434 -0.0062 -0.0267 0.0012  260 ALA D N   
14781 C CA  . ALA D 260 ? 0.2900 0.3116 0.5682 -0.0041 -0.0282 0.0010  260 ALA D CA  
14782 C C   . ALA D 260 ? 0.2731 0.2961 0.5534 -0.0077 -0.0332 0.0026  260 ALA D C   
14783 O O   . ALA D 260 ? 0.2637 0.2873 0.5444 -0.0065 -0.0353 0.0031  260 ALA D O   
14784 C CB  . ALA D 260 ? 0.3143 0.3274 0.5849 -0.0021 -0.0276 -0.0024 260 ALA D CB  
14785 N N   . GLY D 261 ? 0.2581 0.2811 0.5391 -0.0124 -0.0353 0.0036  261 GLY D N   
14786 C CA  . GLY D 261 ? 0.2409 0.2651 0.5235 -0.0169 -0.0405 0.0052  261 GLY D CA  
14787 C C   . GLY D 261 ? 0.2478 0.2607 0.5210 -0.0200 -0.0434 0.0022  261 GLY D C   
14788 O O   . GLY D 261 ? 0.2976 0.3092 0.5696 -0.0237 -0.0481 0.0028  261 GLY D O   
14789 N N   . ALA D 262 ? 0.2301 0.2350 0.4966 -0.0184 -0.0408 -0.0009 262 ALA D N   
14790 C CA  . ALA D 262 ? 0.2457 0.2401 0.5035 -0.0203 -0.0426 -0.0036 262 ALA D CA  
14791 C C   . ALA D 262 ? 0.2442 0.2353 0.5012 -0.0255 -0.0454 -0.0027 262 ALA D C   
14792 O O   . ALA D 262 ? 0.2269 0.2212 0.4882 -0.0270 -0.0442 -0.0008 262 ALA D O   
14793 C CB  . ALA D 262 ? 0.2559 0.2448 0.5089 -0.0172 -0.0389 -0.0062 262 ALA D CB  
14794 N N   . VAL D 263 ? 0.2619 0.2455 0.5123 -0.0284 -0.0492 -0.0042 263 VAL D N   
14795 C CA  . VAL D 263 ? 0.2874 0.2649 0.5348 -0.0337 -0.0524 -0.0040 263 VAL D CA  
14796 C C   . VAL D 263 ? 0.2865 0.2502 0.5224 -0.0329 -0.0519 -0.0079 263 VAL D C   
14797 O O   . VAL D 263 ? 0.3014 0.2564 0.5316 -0.0369 -0.0548 -0.0087 263 VAL D O   
14798 C CB  . VAL D 263 ? 0.2989 0.2794 0.5482 -0.0390 -0.0583 -0.0020 263 VAL D CB  
14799 C CG1 . VAL D 263 ? 0.2781 0.2735 0.5403 -0.0399 -0.0584 0.0026  263 VAL D CG1 
14800 C CG2 . VAL D 263 ? 0.3273 0.3046 0.5705 -0.0381 -0.0609 -0.0038 263 VAL D CG2 
14801 N N   . GLY D 264 ? 0.3073 0.2690 0.5401 -0.0277 -0.0481 -0.0101 264 GLY D N   
14802 C CA  . GLY D 264 ? 0.3128 0.2633 0.5360 -0.0255 -0.0464 -0.0134 264 GLY D CA  
14803 C C   . GLY D 264 ? 0.3112 0.2650 0.5364 -0.0202 -0.0415 -0.0140 264 GLY D C   
14804 O O   . GLY D 264 ? 0.3164 0.2780 0.5465 -0.0184 -0.0406 -0.0131 264 GLY D O   
14805 N N   . MET D 265 ? 0.3280 0.2764 0.5502 -0.0179 -0.0388 -0.0152 265 MET D N   
14806 C CA  . MET D 265 ? 0.3144 0.2670 0.5395 -0.0136 -0.0348 -0.0152 265 MET D CA  
14807 C C   . MET D 265 ? 0.3522 0.2976 0.5711 -0.0103 -0.0323 -0.0173 265 MET D C   
14808 O O   . MET D 265 ? 0.3482 0.2853 0.5623 -0.0103 -0.0323 -0.0182 265 MET D O   
14809 C CB  . MET D 265 ? 0.3106 0.2678 0.5415 -0.0138 -0.0336 -0.0130 265 MET D CB  
14810 C CG  . MET D 265 ? 0.3380 0.3036 0.5758 -0.0161 -0.0348 -0.0106 265 MET D CG  
14811 S SD  . MET D 265 ? 0.2968 0.2716 0.5394 -0.0133 -0.0330 -0.0103 265 MET D SD  
14812 C CE  . MET D 265 ? 0.3145 0.2907 0.5583 -0.0109 -0.0296 -0.0099 265 MET D CE  
14813 N N   . CYS D 266 ? 0.3441 0.2928 0.5634 -0.0073 -0.0299 -0.0179 266 CYS D N   
14814 C CA  . CYS D 266 ? 0.3597 0.3042 0.5746 -0.0038 -0.0269 -0.0194 266 CYS D CA  
14815 C C   . CYS D 266 ? 0.3327 0.2841 0.5534 -0.0011 -0.0241 -0.0181 266 CYS D C   
14816 O O   . CYS D 266 ? 0.2926 0.2474 0.5139 0.0005  -0.0223 -0.0183 266 CYS D O   
14817 C CB  . CYS D 266 ? 0.3801 0.3220 0.5893 -0.0033 -0.0267 -0.0210 266 CYS D CB  
14818 S SG  . CYS D 266 ? 0.3621 0.2944 0.5620 -0.0066 -0.0305 -0.0228 266 CYS D SG  
14819 N N   . PRO D 267 ? 0.3259 0.2792 0.5504 -0.0007 -0.0238 -0.0167 267 PRO D N   
14820 C CA  . PRO D 267 ? 0.3010 0.2606 0.5302 0.0014  -0.0219 -0.0154 267 PRO D CA  
14821 C C   . PRO D 267 ? 0.3098 0.2690 0.5375 0.0047  -0.0192 -0.0160 267 PRO D C   
14822 O O   . PRO D 267 ? 0.3276 0.2801 0.5505 0.0066  -0.0180 -0.0171 267 PRO D O   
14823 C CB  . PRO D 267 ? 0.3066 0.2652 0.5376 0.0015  -0.0222 -0.0138 267 PRO D CB  
14824 C CG  . PRO D 267 ? 0.3040 0.2541 0.5305 -0.0001 -0.0238 -0.0144 267 PRO D CG  
14825 C CD  . PRO D 267 ? 0.3296 0.2785 0.5535 -0.0026 -0.0255 -0.0159 267 PRO D CD  
14826 N N   . PHE D 268 ? 0.3021 0.2683 0.5339 0.0054  -0.0180 -0.0152 268 PHE D N   
14827 C CA  . PHE D 268 ? 0.2876 0.2557 0.5195 0.0080  -0.0153 -0.0150 268 PHE D CA  
14828 C C   . PHE D 268 ? 0.2812 0.2546 0.5184 0.0101  -0.0143 -0.0129 268 PHE D C   
14829 O O   . PHE D 268 ? 0.3002 0.2795 0.5417 0.0085  -0.0156 -0.0116 268 PHE D O   
14830 C CB  . PHE D 268 ? 0.2714 0.2432 0.5038 0.0063  -0.0152 -0.0152 268 PHE D CB  
14831 C CG  . PHE D 268 ? 0.2698 0.2440 0.5023 0.0083  -0.0121 -0.0148 268 PHE D CG  
14832 C CD1 . PHE D 268 ? 0.3063 0.2880 0.5447 0.0089  -0.0110 -0.0127 268 PHE D CD1 
14833 C CD2 . PHE D 268 ? 0.2752 0.2443 0.5016 0.0094  -0.0104 -0.0161 268 PHE D CD2 
14834 C CE1 . PHE D 268 ? 0.3079 0.2932 0.5476 0.0106  -0.0079 -0.0117 268 PHE D CE1 
14835 C CE2 . PHE D 268 ? 0.3133 0.2853 0.5399 0.0116  -0.0068 -0.0153 268 PHE D CE2 
14836 C CZ  . PHE D 268 ? 0.2932 0.2737 0.5271 0.0122  -0.0054 -0.0129 268 PHE D CZ  
14837 N N   . TYR D 269 ? 0.2803 0.2513 0.5170 0.0138  -0.0122 -0.0124 269 TYR D N   
14838 C CA  . TYR D 269 ? 0.2888 0.2511 0.5191 0.0164  -0.0103 -0.0141 269 TYR D CA  
14839 C C   . TYR D 269 ? 0.2705 0.2322 0.5028 0.0210  -0.0083 -0.0125 269 TYR D C   
14840 O O   . TYR D 269 ? 0.2738 0.2426 0.5127 0.0215  -0.0090 -0.0099 269 TYR D O   
14841 C CB  . TYR D 269 ? 0.3027 0.2644 0.5294 0.0173  -0.0077 -0.0154 269 TYR D CB  
14842 C CG  . TYR D 269 ? 0.2853 0.2548 0.5166 0.0203  -0.0041 -0.0136 269 TYR D CG  
14843 C CD1 . TYR D 269 ? 0.2823 0.2618 0.5224 0.0204  -0.0044 -0.0107 269 TYR D CD1 
14844 C CD2 . TYR D 269 ? 0.2835 0.2511 0.5104 0.0223  -0.0006 -0.0146 269 TYR D CD2 
14845 C CE1 . TYR D 269 ? 0.2651 0.2529 0.5105 0.0224  -0.0014 -0.0086 269 TYR D CE1 
14846 C CE2 . TYR D 269 ? 0.2700 0.2457 0.5018 0.0247  0.0031  -0.0124 269 TYR D CE2 
14847 C CZ  . TYR D 269 ? 0.2523 0.2388 0.4941 0.0246  0.0026  -0.0092 269 TYR D CZ  
14848 O OH  . TYR D 269 ? 0.2673 0.2631 0.5150 0.0265  0.0060  -0.0066 269 TYR D OH  
14849 N N   . TYR D 270 ? 0.3011 0.2541 0.5275 0.0246  -0.0059 -0.0139 270 TYR D N   
14850 C CA  . TYR D 270 ? 0.2911 0.2402 0.5178 0.0295  -0.0042 -0.0127 270 TYR D CA  
14851 C C   . TYR D 270 ? 0.2900 0.2505 0.5257 0.0332  -0.0021 -0.0092 270 TYR D C   
14852 O O   . TYR D 270 ? 0.2716 0.2353 0.5123 0.0342  -0.0035 -0.0065 270 TYR D O   
14853 C CB  . TYR D 270 ? 0.3112 0.2483 0.5285 0.0330  -0.0012 -0.0154 270 TYR D CB  
14854 C CG  . TYR D 270 ? 0.3078 0.2396 0.5245 0.0396  0.0018  -0.0143 270 TYR D CG  
14855 C CD1 . TYR D 270 ? 0.3126 0.2393 0.5297 0.0397  -0.0005 -0.0129 270 TYR D CD1 
14856 C CD2 . TYR D 270 ? 0.3225 0.2539 0.5379 0.0459  0.0071  -0.0144 270 TYR D CD2 
14857 C CE1 . TYR D 270 ? 0.3409 0.2614 0.5569 0.0461  0.0021  -0.0117 270 TYR D CE1 
14858 C CE2 . TYR D 270 ? 0.3499 0.2761 0.5647 0.0528  0.0101  -0.0133 270 TYR D CE2 
14859 C CZ  . TYR D 270 ? 0.3584 0.2784 0.5732 0.0529  0.0074  -0.0121 270 TYR D CZ  
14860 O OH  . TYR D 270 ? 0.4001 0.3143 0.6146 0.0599  0.0101  -0.0105 270 TYR D OH  
14861 N N   . ALA D 271 ? 0.2839 0.2509 0.5221 0.0352  0.0013  -0.0088 271 ALA D N   
14862 C CA  . ALA D 271 ? 0.2841 0.2622 0.5315 0.0391  0.0034  -0.0051 271 ALA D CA  
14863 C C   . ALA D 271 ? 0.2702 0.2597 0.5230 0.0373  0.0049  -0.0038 271 ALA D C   
14864 O O   . ALA D 271 ? 0.2711 0.2579 0.5189 0.0359  0.0066  -0.0060 271 ALA D O   
14865 C CB  . ALA D 271 ? 0.2843 0.2573 0.5299 0.0467  0.0079  -0.0046 271 ALA D CB  
14866 N N   . ASP D 272 ? 0.2676 0.2696 0.5305 0.0373  0.0041  0.0000  272 ASP D N   
14867 C CA  . ASP D 272 ? 0.2793 0.2929 0.5486 0.0351  0.0051  0.0020  272 ASP D CA  
14868 C C   . ASP D 272 ? 0.2880 0.3017 0.5553 0.0388  0.0110  0.0016  272 ASP D C   
14869 O O   . ASP D 272 ? 0.2859 0.2962 0.5517 0.0454  0.0152  0.0018  272 ASP D O   
14870 C CB  . ASP D 272 ? 0.2675 0.2946 0.5484 0.0359  0.0039  0.0068  272 ASP D CB  
14871 C CG  . ASP D 272 ? 0.2803 0.3107 0.5639 0.0308  -0.0020 0.0077  272 ASP D CG  
14872 O OD1 . ASP D 272 ? 0.3063 0.3296 0.5835 0.0264  -0.0048 0.0047  272 ASP D OD1 
14873 O OD2 . ASP D 272 ? 0.3235 0.3638 0.6153 0.0316  -0.0037 0.0117  272 ASP D OD2 
14874 N N   . GLY D 273 ? 0.2615 0.2788 0.5285 0.0347  0.0114  0.0013  273 GLY D N   
14875 C CA  . GLY D 273 ? 0.2754 0.2958 0.5419 0.0373  0.0170  0.0020  273 GLY D CA  
14876 C C   . GLY D 273 ? 0.2724 0.3083 0.5499 0.0345  0.0174  0.0063  273 GLY D C   
14877 O O   . GLY D 273 ? 0.2740 0.3120 0.5517 0.0282  0.0147  0.0063  273 GLY D O   
14878 N N   . TRP D 274 ? 0.2582 0.3045 0.5445 0.0394  0.0211  0.0102  274 TRP D N   
14879 C CA  . TRP D 274 ? 0.2470 0.3095 0.5453 0.0365  0.0211  0.0151  274 TRP D CA  
14880 C C   . TRP D 274 ? 0.2700 0.3342 0.5658 0.0334  0.0244  0.0152  274 TRP D C   
14881 O O   . TRP D 274 ? 0.2973 0.3708 0.5996 0.0276  0.0225  0.0180  274 TRP D O   
14882 C CB  . TRP D 274 ? 0.2371 0.3116 0.5465 0.0430  0.0246  0.0198  274 TRP D CB  
14883 C CG  . TRP D 274 ? 0.2255 0.3010 0.5394 0.0454  0.0206  0.0211  274 TRP D CG  
14884 C CD1 . TRP D 274 ? 0.2120 0.2766 0.5192 0.0438  0.0158  0.0180  274 TRP D CD1 
14885 C CD2 . TRP D 274 ? 0.2288 0.3175 0.5552 0.0506  0.0217  0.0265  274 TRP D CD2 
14886 N NE1 . TRP D 274 ? 0.2104 0.2800 0.5244 0.0470  0.0135  0.0211  274 TRP D NE1 
14887 C CE2 . TRP D 274 ? 0.2168 0.3006 0.5424 0.0515  0.0169  0.0263  274 TRP D CE2 
14888 C CE3 . TRP D 274 ? 0.2217 0.3265 0.5604 0.0543  0.0261  0.0319  274 TRP D CE3 
14889 C CZ2 . TRP D 274 ? 0.2242 0.3182 0.5603 0.0562  0.0161  0.0312  274 TRP D CZ2 
14890 C CZ3 . TRP D 274 ? 0.2286 0.3445 0.5788 0.0591  0.0253  0.0370  274 TRP D CZ3 
14891 C CH2 . TRP D 274 ? 0.2300 0.3401 0.5785 0.0602  0.0203  0.0366  274 TRP D CH2 
14892 N N   . TRP D 275 ? 0.2856 0.3398 0.5708 0.0367  0.0290  0.0121  275 TRP D N   
14893 C CA  . TRP D 275 ? 0.2996 0.3543 0.5810 0.0342  0.0324  0.0123  275 TRP D CA  
14894 C C   . TRP D 275 ? 0.3325 0.3838 0.6107 0.0257  0.0270  0.0111  275 TRP D C   
14895 O O   . TRP D 275 ? 0.3145 0.3686 0.5920 0.0224  0.0289  0.0126  275 TRP D O   
14896 C CB  . TRP D 275 ? 0.3053 0.3475 0.5734 0.0391  0.0374  0.0086  275 TRP D CB  
14897 C CG  . TRP D 275 ? 0.2937 0.3195 0.5489 0.0372  0.0332  0.0032  275 TRP D CG  
14898 C CD1 . TRP D 275 ? 0.2886 0.3041 0.5384 0.0401  0.0311  0.0000  275 TRP D CD1 
14899 C CD2 . TRP D 275 ? 0.2925 0.3106 0.5388 0.0319  0.0308  0.0008  275 TRP D CD2 
14900 N NE1 . TRP D 275 ? 0.2947 0.2978 0.5337 0.0367  0.0275  -0.0041 275 TRP D NE1 
14901 C CE2 . TRP D 275 ? 0.2908 0.2954 0.5275 0.0320  0.0272  -0.0036 275 TRP D CE2 
14902 C CE3 . TRP D 275 ? 0.2912 0.3127 0.5370 0.0272  0.0312  0.0025  275 TRP D CE3 
14903 C CZ2 . TRP D 275 ? 0.2869 0.2826 0.5145 0.0277  0.0239  -0.0063 275 TRP D CZ2 
14904 C CZ3 . TRP D 275 ? 0.2977 0.3090 0.5334 0.0234  0.0281  -0.0004 275 TRP D CZ3 
14905 C CH2 . TRP D 275 ? 0.3053 0.3044 0.5324 0.0239  0.0245  -0.0046 275 TRP D CH2 
14906 N N   . LYS D 276 ? 0.3303 0.3755 0.6065 0.0225  0.0207  0.0087  276 LYS D N   
14907 C CA  . LYS D 276 ? 0.3135 0.3509 0.5829 0.0167  0.0167  0.0062  276 LYS D CA  
14908 C C   . LYS D 276 ? 0.3113 0.3569 0.5874 0.0101  0.0142  0.0092  276 LYS D C   
14909 O O   . LYS D 276 ? 0.3381 0.3783 0.6087 0.0058  0.0128  0.0082  276 LYS D O   
14910 C CB  . LYS D 276 ? 0.3016 0.3294 0.5659 0.0162  0.0118  0.0026  276 LYS D CB  
14911 C CG  . LYS D 276 ? 0.3160 0.3318 0.5701 0.0204  0.0133  -0.0012 276 LYS D CG  
14912 C CD  . LYS D 276 ? 0.3168 0.3253 0.5682 0.0204  0.0091  -0.0037 276 LYS D CD  
14913 C CE  . LYS D 276 ? 0.3301 0.3342 0.5781 0.0151  0.0045  -0.0055 276 LYS D CE  
14914 N NZ  . LYS D 276 ? 0.3391 0.3352 0.5779 0.0141  0.0051  -0.0076 276 LYS D NZ  
14915 N N   . GLY D 277 ? 0.3354 0.3935 0.6228 0.0089  0.0134  0.0131  277 GLY D N   
14916 C CA  . GLY D 277 ? 0.3588 0.4244 0.6521 0.0020  0.0113  0.0163  277 GLY D CA  
14917 C C   . GLY D 277 ? 0.3918 0.4688 0.6919 0.0022  0.0166  0.0209  277 GLY D C   
14918 O O   . GLY D 277 ? 0.3935 0.4801 0.7016 -0.0033 0.0150  0.0247  277 GLY D O   
14919 N N   . GLY D 278 ? 0.3951 0.4709 0.6915 0.0082  0.0231  0.0207  278 GLY D N   
14920 C CA  . GLY D 278 ? 0.4165 0.5051 0.7209 0.0101  0.0292  0.0255  278 GLY D CA  
14921 C C   . GLY D 278 ? 0.4722 0.5739 0.7892 0.0144  0.0299  0.0290  278 GLY D C   
14922 O O   . GLY D 278 ? 0.5579 0.6601 0.8785 0.0136  0.0244  0.0284  278 GLY D O   
14923 N N   . GLU D 279 ? 0.4180 0.5301 0.7412 0.0195  0.0371  0.0327  279 GLU D N   
14924 C CA  . GLU D 279 ? 0.4109 0.5365 0.7468 0.0251  0.0392  0.0367  279 GLU D CA  
14925 C C   . GLU D 279 ? 0.3806 0.4961 0.7107 0.0328  0.0390  0.0328  279 GLU D C   
14926 O O   . GLU D 279 ? 0.3742 0.4898 0.7077 0.0317  0.0330  0.0325  279 GLU D O   
14927 C CB  . GLU D 279 ? 0.4346 0.5749 0.7848 0.0189  0.0332  0.0415  279 GLU D CB  
14928 C CG  . GLU D 279 ? 0.5008 0.6533 0.8593 0.0106  0.0327  0.0465  279 GLU D CG  
14929 C CD  . GLU D 279 ? 0.5240 0.6830 0.8839 0.0122  0.0411  0.0497  279 GLU D CD  
14930 O OE1 . GLU D 279 ? 0.6027 0.7723 0.9697 0.0196  0.0482  0.0531  279 GLU D OE1 
14931 O OE2 . GLU D 279 ? 0.6337 0.7860 0.9865 0.0059  0.0405  0.0487  279 GLU D OE2 
14932 N N   . LYS D 280 ? 0.3543 0.4607 0.6750 0.0403  0.0454  0.0300  280 LYS D N   
14933 C CA  . LYS D 280 ? 0.3543 0.4473 0.6666 0.0467  0.0451  0.0255  280 LYS D CA  
14934 C C   . LYS D 280 ? 0.3237 0.4260 0.6472 0.0533  0.0457  0.0290  280 LYS D C   
14935 O O   . LYS D 280 ? 0.3153 0.4082 0.6343 0.0566  0.0432  0.0263  280 LYS D O   
14936 C CB  . LYS D 280 ? 0.3672 0.4475 0.6657 0.0528  0.0520  0.0217  280 LYS D CB  
14937 C CG  . LYS D 280 ? 0.4078 0.4989 0.7125 0.0602  0.0611  0.0256  280 LYS D CG  
14938 C CD  . LYS D 280 ? 0.4434 0.5262 0.7354 0.0638  0.0687  0.0232  280 LYS D CD  
14939 C CE  . LYS D 280 ? 0.4465 0.5428 0.7465 0.0706  0.0782  0.0280  280 LYS D CE  
14940 N NZ  . LYS D 280 ? 0.4803 0.5633 0.7637 0.0756  0.0853  0.0240  280 LYS D NZ  
14941 N N   . SER D 281 ? 0.3021 0.4232 0.6403 0.0550  0.0489  0.0353  281 SER D N   
14942 C CA  . SER D 281 ? 0.3131 0.4456 0.6639 0.0610  0.0491  0.0397  281 SER D CA  
14943 C C   . SER D 281 ? 0.2958 0.4385 0.6574 0.0541  0.0403  0.0430  281 SER D C   
14944 O O   . SER D 281 ? 0.3029 0.4568 0.6761 0.0582  0.0392  0.0475  281 SER D O   
14945 C CB  . SER D 281 ? 0.3335 0.4824 0.6956 0.0671  0.0575  0.0454  281 SER D CB  
14946 O OG  . SER D 281 ? 0.3452 0.4826 0.6957 0.0755  0.0660  0.0420  281 SER D OG  
14947 N N   . ASP D 282 ? 0.2993 0.4380 0.6568 0.0441  0.0341  0.0410  282 ASP D N   
14948 C CA  . ASP D 282 ? 0.3126 0.4589 0.6777 0.0370  0.0256  0.0434  282 ASP D CA  
14949 C C   . ASP D 282 ? 0.2980 0.4276 0.6508 0.0326  0.0192  0.0376  282 ASP D C   
14950 O O   . ASP D 282 ? 0.2739 0.3905 0.6148 0.0298  0.0196  0.0328  282 ASP D O   
14951 C CB  . ASP D 282 ? 0.3773 0.5377 0.7518 0.0286  0.0240  0.0478  282 ASP D CB  
14952 C CG  . ASP D 282 ? 0.4051 0.5748 0.7881 0.0211  0.0152  0.0509  282 ASP D CG  
14953 O OD1 . ASP D 282 ? 0.4286 0.6114 0.8235 0.0247  0.0139  0.0557  282 ASP D OD1 
14954 O OD2 . ASP D 282 ? 0.4367 0.5994 0.8134 0.0122  0.0098  0.0482  282 ASP D OD2 
14955 N N   . HIS D 283 ? 0.2982 0.4290 0.6541 0.0324  0.0134  0.0384  283 HIS D N   
14956 C CA  . HIS D 283 ? 0.2839 0.4014 0.6297 0.0279  0.0074  0.0338  283 HIS D CA  
14957 C C   . HIS D 283 ? 0.2843 0.4079 0.6336 0.0180  0.0007  0.0352  283 HIS D C   
14958 O O   . HIS D 283 ? 0.2972 0.4299 0.6541 0.0161  -0.0043 0.0386  283 HIS D O   
14959 C CB  . HIS D 283 ? 0.2847 0.3976 0.6294 0.0331  0.0051  0.0335  283 HIS D CB  
14960 C CG  . HIS D 283 ? 0.2694 0.3655 0.6012 0.0309  0.0019  0.0279  283 HIS D CG  
14961 N ND1 . HIS D 283 ? 0.2303 0.3207 0.5594 0.0328  -0.0016 0.0273  283 HIS D ND1 
14962 C CD2 . HIS D 283 ? 0.2648 0.3490 0.5859 0.0270  0.0019  0.0229  283 HIS D CD2 
14963 C CE1 . HIS D 283 ? 0.2357 0.3120 0.5533 0.0299  -0.0033 0.0223  283 HIS D CE1 
14964 N NE2 . HIS D 283 ? 0.2424 0.3148 0.5552 0.0268  -0.0013 0.0195  283 HIS D NE2 
14965 N N   . SER D 284 ? 0.2788 0.3971 0.6223 0.0121  0.0007  0.0327  284 SER D N   
14966 C CA  . SER D 284 ? 0.2825 0.4052 0.6283 0.0026  -0.0046 0.0340  284 SER D CA  
14967 C C   . SER D 284 ? 0.2638 0.3794 0.6041 -0.0015 -0.0119 0.0314  284 SER D C   
14968 O O   . SER D 284 ? 0.2569 0.3589 0.5868 0.0001  -0.0123 0.0266  284 SER D O   
14969 C CB  . SER D 284 ? 0.2888 0.4049 0.6281 -0.0015 -0.0022 0.0318  284 SER D CB  
14970 O OG  . SER D 284 ? 0.3064 0.4225 0.6452 -0.0107 -0.0078 0.0319  284 SER D OG  
14971 N N   . LEU D 285 ? 0.2559 0.3812 0.6031 -0.0070 -0.0176 0.0348  285 LEU D N   
14972 C CA  . LEU D 285 ? 0.2542 0.3734 0.5955 -0.0110 -0.0244 0.0327  285 LEU D CA  
14973 C C   . LEU D 285 ? 0.2784 0.3832 0.6076 -0.0164 -0.0260 0.0274  285 LEU D C   
14974 O O   . LEU D 285 ? 0.3192 0.4140 0.6399 -0.0165 -0.0287 0.0238  285 LEU D O   
14975 C CB  . LEU D 285 ? 0.2685 0.4010 0.6189 -0.0163 -0.0305 0.0375  285 LEU D CB  
14976 C CG  . LEU D 285 ? 0.2807 0.4297 0.6450 -0.0110 -0.0297 0.0438  285 LEU D CG  
14977 C CD1 . LEU D 285 ? 0.2794 0.4408 0.6514 -0.0172 -0.0374 0.0485  285 LEU D CD1 
14978 C CD2 . LEU D 285 ? 0.2604 0.4047 0.6226 -0.0015 -0.0269 0.0430  285 LEU D CD2 
14979 N N   . ASN D 286 ? 0.2673 0.3705 0.5953 -0.0200 -0.0237 0.0269  286 ASN D N   
14980 C CA  . ASN D 286 ? 0.3006 0.3913 0.6184 -0.0256 -0.0259 0.0228  286 ASN D CA  
14981 C C   . ASN D 286 ? 0.3002 0.3800 0.6101 -0.0226 -0.0210 0.0192  286 ASN D C   
14982 O O   . ASN D 286 ? 0.2762 0.3471 0.5791 -0.0270 -0.0221 0.0168  286 ASN D O   
14983 C CB  . ASN D 286 ? 0.2827 0.3780 0.6035 -0.0344 -0.0295 0.0252  286 ASN D CB  
14984 C CG  . ASN D 286 ? 0.3087 0.4122 0.6366 -0.0356 -0.0252 0.0288  286 ASN D CG  
14985 O OD1 . ASN D 286 ? 0.3392 0.4477 0.6714 -0.0295 -0.0193 0.0304  286 ASN D OD1 
14986 N ND2 . ASN D 286 ? 0.3777 0.4830 0.7070 -0.0439 -0.0282 0.0306  286 ASN D ND2 
14987 N N   . GLN D 287 ? 0.2791 0.3583 0.5891 -0.0152 -0.0161 0.0188  287 GLN D N   
14988 C CA  . GLN D 287 ? 0.2890 0.3573 0.5905 -0.0122 -0.0122 0.0152  287 GLN D CA  
14989 C C   . GLN D 287 ? 0.2808 0.3389 0.5748 -0.0083 -0.0130 0.0112  287 GLN D C   
14990 O O   . GLN D 287 ? 0.2644 0.3232 0.5597 -0.0026 -0.0109 0.0114  287 GLN D O   
14991 C CB  . GLN D 287 ? 0.3110 0.3838 0.6156 -0.0070 -0.0058 0.0170  287 GLN D CB  
14992 C CG  . GLN D 287 ? 0.3468 0.4296 0.6583 -0.0106 -0.0037 0.0211  287 GLN D CG  
14993 C CD  . GLN D 287 ? 0.3402 0.4149 0.6447 -0.0159 -0.0040 0.0196  287 GLN D CD  
14994 O OE1 . GLN D 287 ? 0.3470 0.4094 0.6415 -0.0145 -0.0032 0.0157  287 GLN D OE1 
14995 N NE2 . GLN D 287 ? 0.3394 0.4209 0.6493 -0.0224 -0.0055 0.0229  287 GLN D NE2 
14996 N N   . PRO D 288 ? 0.2814 0.3293 0.5674 -0.0114 -0.0158 0.0077  288 PRO D N   
14997 C CA  . PRO D 288 ? 0.2933 0.3322 0.5727 -0.0083 -0.0164 0.0043  288 PRO D CA  
14998 C C   . PRO D 288 ? 0.3026 0.3366 0.5788 -0.0026 -0.0124 0.0028  288 PRO D C   
14999 O O   . PRO D 288 ? 0.3126 0.3435 0.5872 0.0009  -0.0125 0.0017  288 PRO D O   
15000 C CB  . PRO D 288 ? 0.2650 0.2950 0.5372 -0.0124 -0.0188 0.0013  288 PRO D CB  
15001 C CG  . PRO D 288 ? 0.2732 0.3080 0.5486 -0.0183 -0.0216 0.0034  288 PRO D CG  
15002 C CD  . PRO D 288 ? 0.2620 0.3073 0.5456 -0.0180 -0.0188 0.0073  288 PRO D CD  
15003 N N   . GLU D 289 ? 0.2918 0.3251 0.5667 -0.0020 -0.0089 0.0029  289 GLU D N   
15004 C CA  . GLU D 289 ? 0.2806 0.3077 0.5502 0.0025  -0.0053 0.0010  289 GLU D CA  
15005 C C   . GLU D 289 ? 0.2673 0.2981 0.5406 0.0083  -0.0025 0.0024  289 GLU D C   
15006 O O   . GLU D 289 ? 0.2939 0.3178 0.5617 0.0123  -0.0001 0.0004  289 GLU D O   
15007 C CB  . GLU D 289 ? 0.2693 0.2956 0.5363 0.0015  -0.0023 0.0014  289 GLU D CB  
15008 C CG  . GLU D 289 ? 0.2548 0.2738 0.5157 -0.0027 -0.0045 -0.0004 289 GLU D CG  
15009 C CD  . GLU D 289 ? 0.2883 0.2976 0.5419 -0.0010 -0.0059 -0.0039 289 GLU D CD  
15010 O OE1 . GLU D 289 ? 0.2949 0.3005 0.5449 0.0028  -0.0037 -0.0051 289 GLU D OE1 
15011 O OE2 . GLU D 289 ? 0.2984 0.3037 0.5500 -0.0036 -0.0092 -0.0053 289 GLU D OE2 
15012 N N   . GLU D 290 ? 0.2421 0.2835 0.5243 0.0088  -0.0028 0.0059  290 GLU D N   
15013 C CA  . GLU D 290 ? 0.2391 0.2851 0.5260 0.0149  0.0001  0.0080  290 GLU D CA  
15014 C C   . GLU D 290 ? 0.2352 0.2785 0.5221 0.0169  -0.0029 0.0076  290 GLU D C   
15015 O O   . GLU D 290 ? 0.2043 0.2510 0.4954 0.0222  -0.0011 0.0097  290 GLU D O   
15016 C CB  . GLU D 290 ? 0.2301 0.2909 0.5282 0.0143  0.0012  0.0129  290 GLU D CB  
15017 C CG  . GLU D 290 ? 0.2337 0.2985 0.5330 0.0155  0.0068  0.0143  290 GLU D CG  
15018 C CD  . GLU D 290 ? 0.2243 0.3053 0.5359 0.0143  0.0081  0.0198  290 GLU D CD  
15019 O OE1 . GLU D 290 ? 0.1875 0.2787 0.5084 0.0174  0.0081  0.0234  290 GLU D OE1 
15020 O OE2 . GLU D 290 ? 0.2710 0.3543 0.5826 0.0100  0.0093  0.0207  290 GLU D OE2 
15021 N N   . TRP D 291 ? 0.2397 0.2775 0.5223 0.0130  -0.0072 0.0055  291 TRP D N   
15022 C CA  . TRP D 291 ? 0.2416 0.2784 0.5246 0.0137  -0.0104 0.0059  291 TRP D CA  
15023 C C   . TRP D 291 ? 0.2257 0.2512 0.5002 0.0125  -0.0121 0.0023  291 TRP D C   
15024 O O   . TRP D 291 ? 0.2339 0.2589 0.5076 0.0101  -0.0156 0.0022  291 TRP D O   
15025 C CB  . TRP D 291 ? 0.2594 0.3049 0.5480 0.0094  -0.0148 0.0086  291 TRP D CB  
15026 C CG  . TRP D 291 ? 0.2436 0.3025 0.5425 0.0099  -0.0142 0.0131  291 TRP D CG  
15027 C CD1 . TRP D 291 ? 0.2287 0.2940 0.5316 0.0074  -0.0125 0.0145  291 TRP D CD1 
15028 C CD2 . TRP D 291 ? 0.2189 0.2872 0.5259 0.0127  -0.0154 0.0174  291 TRP D CD2 
15029 N NE1 . TRP D 291 ? 0.2233 0.3021 0.5369 0.0083  -0.0125 0.0194  291 TRP D NE1 
15030 C CE2 . TRP D 291 ? 0.2104 0.2916 0.5269 0.0116  -0.0145 0.0213  291 TRP D CE2 
15031 C CE3 . TRP D 291 ? 0.2192 0.2867 0.5267 0.0162  -0.0173 0.0187  291 TRP D CE3 
15032 C CZ2 . TRP D 291 ? 0.2071 0.3012 0.5343 0.0141  -0.0154 0.0265  291 TRP D CZ2 
15033 C CZ3 . TRP D 291 ? 0.1985 0.2777 0.5157 0.0189  -0.0182 0.0238  291 TRP D CZ3 
15034 C CH2 . TRP D 291 ? 0.1948 0.2876 0.5221 0.0180  -0.0174 0.0277  291 TRP D CH2 
15035 N N   . PHE D 292 ? 0.2608 0.2779 0.5291 0.0140  -0.0097 -0.0005 292 PHE D N   
15036 C CA  . PHE D 292 ? 0.2356 0.2433 0.4969 0.0125  -0.0114 -0.0036 292 PHE D CA  
15037 C C   . PHE D 292 ? 0.2534 0.2546 0.5119 0.0162  -0.0108 -0.0040 292 PHE D C   
15038 O O   . PHE D 292 ? 0.2654 0.2601 0.5196 0.0148  -0.0125 -0.0056 292 PHE D O   
15039 C CB  . PHE D 292 ? 0.2525 0.2546 0.5083 0.0111  -0.0101 -0.0061 292 PHE D CB  
15040 C CG  . PHE D 292 ? 0.2540 0.2572 0.5091 0.0064  -0.0122 -0.0068 292 PHE D CG  
15041 C CD1 . PHE D 292 ? 0.2518 0.2510 0.5040 0.0042  -0.0148 -0.0084 292 PHE D CD1 
15042 C CD2 . PHE D 292 ? 0.2637 0.2720 0.5215 0.0044  -0.0114 -0.0055 292 PHE D CD2 
15043 C CE1 . PHE D 292 ? 0.2406 0.2396 0.4917 0.0008  -0.0163 -0.0090 292 PHE D CE1 
15044 C CE2 . PHE D 292 ? 0.2577 0.2652 0.5142 0.0003  -0.0133 -0.0062 292 PHE D CE2 
15045 C CZ  . PHE D 292 ? 0.2545 0.2570 0.5074 -0.0012 -0.0157 -0.0081 292 PHE D CZ  
15046 N N   . GLY D 293 ? 0.2445 0.2477 0.5060 0.0209  -0.0082 -0.0022 293 GLY D N   
15047 C CA  . GLY D 293 ? 0.2484 0.2434 0.5061 0.0248  -0.0072 -0.0028 293 GLY D CA  
15048 C C   . GLY D 293 ? 0.2325 0.2252 0.4901 0.0238  -0.0105 -0.0018 293 GLY D C   
15049 O O   . GLY D 293 ? 0.2114 0.2111 0.4736 0.0220  -0.0130 0.0005  293 GLY D O   
15050 N N   . PHE D 294 ? 0.2309 0.2131 0.4825 0.0247  -0.0105 -0.0034 294 PHE D N   
15051 C CA  . PHE D 294 ? 0.2349 0.2139 0.4862 0.0249  -0.0127 -0.0017 294 PHE D CA  
15052 C C   . PHE D 294 ? 0.2413 0.2217 0.4962 0.0307  -0.0110 0.0012  294 PHE D C   
15053 O O   . PHE D 294 ? 0.2370 0.2181 0.4937 0.0313  -0.0129 0.0039  294 PHE D O   
15054 C CB  . PHE D 294 ? 0.2361 0.2033 0.4801 0.0232  -0.0135 -0.0040 294 PHE D CB  
15055 C CG  . PHE D 294 ? 0.2243 0.1912 0.4661 0.0177  -0.0156 -0.0061 294 PHE D CG  
15056 C CD1 . PHE D 294 ? 0.2318 0.2065 0.4764 0.0151  -0.0161 -0.0065 294 PHE D CD1 
15057 C CD2 . PHE D 294 ? 0.2363 0.1946 0.4729 0.0153  -0.0169 -0.0075 294 PHE D CD2 
15058 C CE1 . PHE D 294 ? 0.2300 0.2041 0.4727 0.0111  -0.0176 -0.0081 294 PHE D CE1 
15059 C CE2 . PHE D 294 ? 0.2428 0.2020 0.4785 0.0108  -0.0186 -0.0089 294 PHE D CE2 
15060 C CZ  . PHE D 294 ? 0.2465 0.2136 0.4853 0.0092  -0.0188 -0.0092 294 PHE D CZ  
15061 N N   . TRP D 295 ? 0.2554 0.2368 0.5115 0.0352  -0.0072 0.0011  295 TRP D N   
15062 C CA  . TRP D 295 ? 0.2611 0.2455 0.5218 0.0418  -0.0048 0.0042  295 TRP D CA  
15063 C C   . TRP D 295 ? 0.2724 0.2709 0.5418 0.0429  -0.0032 0.0066  295 TRP D C   
15064 O O   . TRP D 295 ? 0.3002 0.3016 0.5691 0.0403  -0.0019 0.0047  295 TRP D O   
15065 C CB  . TRP D 295 ? 0.2732 0.2451 0.5268 0.0471  -0.0008 0.0019  295 TRP D CB  
15066 C CG  . TRP D 295 ? 0.2822 0.2394 0.5278 0.0468  -0.0023 0.0005  295 TRP D CG  
15067 C CD1 . TRP D 295 ? 0.2814 0.2313 0.5211 0.0408  -0.0055 -0.0019 295 TRP D CD1 
15068 C CD2 . TRP D 295 ? 0.2786 0.2264 0.5215 0.0528  -0.0007 0.0017  295 TRP D CD2 
15069 N NE1 . TRP D 295 ? 0.2887 0.2259 0.5225 0.0420  -0.0062 -0.0021 295 TRP D NE1 
15070 C CE2 . TRP D 295 ? 0.2936 0.2285 0.5288 0.0493  -0.0034 0.0000  295 TRP D CE2 
15071 C CE3 . TRP D 295 ? 0.2826 0.2321 0.5294 0.0609  0.0028  0.0044  295 TRP D CE3 
15072 C CZ2 . TRP D 295 ? 0.2925 0.2146 0.5228 0.0532  -0.0028 0.0008  295 TRP D CZ2 
15073 C CZ3 . TRP D 295 ? 0.2946 0.2317 0.5368 0.0656  0.0035  0.0052  295 TRP D CZ3 
15074 C CH2 . TRP D 295 ? 0.3006 0.2233 0.5340 0.0616  0.0006  0.0032  295 TRP D CH2 
15075 N N   . GLY D 296 ? 0.2613 0.2689 0.5390 0.0464  -0.0035 0.0111  296 GLY D N   
15076 C CA  . GLY D 296 ? 0.2557 0.2785 0.5434 0.0470  -0.0026 0.0144  296 GLY D CA  
15077 C C   . GLY D 296 ? 0.2623 0.2895 0.5561 0.0554  0.0013  0.0179  296 GLY D C   
15078 O O   . GLY D 296 ? 0.2524 0.2741 0.5454 0.0601  0.0011  0.0196  296 GLY D O   
15079 N N   . TYR D 297 ? 0.2619 0.2996 0.5624 0.0573  0.0050  0.0195  297 TYR D N   
15080 C CA  . TYR D 297 ? 0.2580 0.3015 0.5651 0.0660  0.0100  0.0229  297 TYR D CA  
15081 C C   . TYR D 297 ? 0.2557 0.3175 0.5769 0.0659  0.0072  0.0292  297 TYR D C   
15082 O O   . TYR D 297 ? 0.2768 0.3480 0.6022 0.0588  0.0035  0.0301  297 TYR D O   
15083 C CB  . TYR D 297 ? 0.2629 0.3068 0.5683 0.0685  0.0166  0.0211  297 TYR D CB  
15084 C CG  . TYR D 297 ? 0.2826 0.3077 0.5731 0.0689  0.0190  0.0149  297 TYR D CG  
15085 C CD1 . TYR D 297 ? 0.2924 0.3031 0.5749 0.0756  0.0219  0.0130  297 TYR D CD1 
15086 C CD2 . TYR D 297 ? 0.2656 0.2866 0.5493 0.0619  0.0176  0.0110  297 TYR D CD2 
15087 C CE1 . TYR D 297 ? 0.3050 0.2982 0.5732 0.0743  0.0228  0.0073  297 TYR D CE1 
15088 C CE2 . TYR D 297 ? 0.2641 0.2691 0.5346 0.0613  0.0187  0.0058  297 TYR D CE2 
15089 C CZ  . TYR D 297 ? 0.2880 0.2792 0.5507 0.0671  0.0211  0.0038  297 TYR D CZ  
15090 O OH  . TYR D 297 ? 0.2985 0.2746 0.5480 0.0650  0.0213  -0.0013 297 TYR D OH  
15091 N N   . SER D 298 ? 0.2699 0.3358 0.5976 0.0736  0.0085  0.0336  298 SER D N   
15092 C CA  . SER D 298 ? 0.2849 0.3678 0.6256 0.0732  0.0045  0.0401  298 SER D CA  
15093 C C   . SER D 298 ? 0.2627 0.3642 0.6160 0.0733  0.0072  0.0439  298 SER D C   
15094 O O   . SER D 298 ? 0.2307 0.3473 0.5940 0.0688  0.0024  0.0483  298 SER D O   
15095 C CB  . SER D 298 ? 0.2784 0.3600 0.6226 0.0815  0.0044  0.0442  298 SER D CB  
15096 O OG  . SER D 298 ? 0.2931 0.3750 0.6403 0.0911  0.0118  0.0453  298 SER D OG  
15097 N N   . ASP D 299 ? 0.2849 0.3852 0.6375 0.0787  0.0148  0.0427  299 ASP D N   
15098 C CA  . ASP D 299 ? 0.2923 0.4099 0.6567 0.0799  0.0189  0.0466  299 ASP D CA  
15099 C C   . ASP D 299 ? 0.2941 0.4029 0.6507 0.0847  0.0275  0.0427  299 ASP D C   
15100 O O   . ASP D 299 ? 0.3168 0.4065 0.6592 0.0863  0.0292  0.0370  299 ASP D O   
15101 C CB  . ASP D 299 ? 0.3005 0.4357 0.6810 0.0864  0.0193  0.0544  299 ASP D CB  
15102 C CG  . ASP D 299 ? 0.3401 0.4684 0.7198 0.0990  0.0248  0.0556  299 ASP D CG  
15103 O OD1 . ASP D 299 ? 0.3512 0.4648 0.7200 0.1041  0.0313  0.0508  299 ASP D OD1 
15104 O OD2 . ASP D 299 ? 0.4025 0.5399 0.7920 0.1036  0.0224  0.0613  299 ASP D OD2 
15105 N N   . LEU D 300 ? 0.2916 0.4145 0.6571 0.0861  0.0326  0.0458  300 LEU D N   
15106 C CA  . LEU D 300 ? 0.3188 0.4353 0.6769 0.0896  0.0407  0.0426  300 LEU D CA  
15107 C C   . LEU D 300 ? 0.3477 0.4495 0.6969 0.1008  0.0473  0.0400  300 LEU D C   
15108 O O   . LEU D 300 ? 0.3620 0.4510 0.6989 0.1027  0.0526  0.0351  300 LEU D O   
15109 C CB  . LEU D 300 ? 0.2953 0.4333 0.6679 0.0900  0.0451  0.0484  300 LEU D CB  
15110 C CG  . LEU D 300 ? 0.2997 0.4346 0.6661 0.0929  0.0540  0.0461  300 LEU D CG  
15111 C CD1 . LEU D 300 ? 0.3011 0.4223 0.6531 0.0843  0.0518  0.0399  300 LEU D CD1 
15112 C CD2 . LEU D 300 ? 0.2926 0.4510 0.6755 0.0933  0.0582  0.0531  300 LEU D CD2 
15113 N N   . ASN D 301 ? 0.3820 0.4851 0.7369 0.1084  0.0471  0.0433  301 ASN D N   
15114 C CA  . ASN D 301 ? 0.4069 0.4959 0.7538 0.1198  0.0537  0.0413  301 ASN D CA  
15115 C C   . ASN D 301 ? 0.3859 0.4512 0.7171 0.1188  0.0498  0.0356  301 ASN D C   
15116 O O   . ASN D 301 ? 0.4203 0.4708 0.7430 0.1273  0.0542  0.0335  301 ASN D O   
15117 C CB  . ASN D 301 ? 0.4126 0.5137 0.7733 0.1300  0.0561  0.0482  301 ASN D CB  
15118 C CG  . ASN D 301 ? 0.4269 0.5546 0.8063 0.1306  0.0588  0.0553  301 ASN D CG  
15119 O OD1 . ASN D 301 ? 0.4001 0.5448 0.7946 0.1295  0.0537  0.0618  301 ASN D OD1 
15120 N ND2 . ASN D 301 ? 0.4074 0.5389 0.7857 0.1319  0.0664  0.0542  301 ASN D ND2 
15121 N N   . ASP D 302 ? 0.3586 0.4204 0.6862 0.1086  0.0417  0.0336  302 ASP D N   
15122 C CA  . ASP D 302 ? 0.3557 0.3978 0.6706 0.1069  0.0376  0.0293  302 ASP D CA  
15123 C C   . ASP D 302 ? 0.3814 0.4061 0.6799 0.1038  0.0399  0.0219  302 ASP D C   
15124 O O   . ASP D 302 ? 0.3813 0.4095 0.6781 0.0960  0.0382  0.0199  302 ASP D O   
15125 C CB  . ASP D 302 ? 0.3414 0.3888 0.6608 0.0987  0.0286  0.0312  302 ASP D CB  
15126 C CG  . ASP D 302 ? 0.3484 0.3774 0.6561 0.0964  0.0242  0.0277  302 ASP D CG  
15127 O OD1 . ASP D 302 ? 0.3868 0.3984 0.6836 0.1017  0.0279  0.0243  302 ASP D OD1 
15128 O OD2 . ASP D 302 ? 0.3150 0.3470 0.6242 0.0892  0.0174  0.0285  302 ASP D OD2 
15129 N N   . LYS D 303 ? 0.4028 0.4086 0.6890 0.1101  0.0436  0.0183  303 LYS D N   
15130 C CA  . LYS D 303 ? 0.4343 0.4217 0.7036 0.1078  0.0453  0.0113  303 LYS D CA  
15131 C C   . LYS D 303 ? 0.3978 0.3698 0.6573 0.1013  0.0385  0.0078  303 LYS D C   
15132 O O   . LYS D 303 ? 0.3860 0.3443 0.6325 0.0970  0.0379  0.0023  303 LYS D O   
15133 C CB  . LYS D 303 ? 0.5221 0.4965 0.7821 0.1183  0.0535  0.0090  303 LYS D CB  
15134 C CG  . LYS D 303 ? 0.5627 0.5504 0.8300 0.1255  0.0620  0.0118  303 LYS D CG  
15135 C CD  . LYS D 303 ? 0.6346 0.6249 0.8966 0.1200  0.0642  0.0089  303 LYS D CD  
15136 C CE  . LYS D 303 ? 0.6776 0.6784 0.9440 0.1273  0.0737  0.0112  303 LYS D CE  
15137 N NZ  . LYS D 303 ? 0.6563 0.6833 0.9435 0.1271  0.0736  0.0186  303 LYS D NZ  
15138 N N   . TYR D 304 ? 0.3791 0.3547 0.6453 0.1000  0.0332  0.0112  304 TYR D N   
15139 C CA  . TYR D 304 ? 0.3727 0.3330 0.6300 0.0956  0.0279  0.0087  304 TYR D CA  
15140 C C   . TYR D 304 ? 0.3504 0.3194 0.6125 0.0858  0.0207  0.0098  304 TYR D C   
15141 O O   . TYR D 304 ? 0.3345 0.2944 0.5881 0.0787  0.0174  0.0058  304 TYR D O   
15142 C CB  . TYR D 304 ? 0.3586 0.3105 0.6158 0.1032  0.0284  0.0114  304 TYR D CB  
15143 C CG  . TYR D 304 ? 0.3828 0.3238 0.6331 0.1133  0.0362  0.0095  304 TYR D CG  
15144 C CD1 . TYR D 304 ? 0.3913 0.3129 0.6251 0.1125  0.0384  0.0030  304 TYR D CD1 
15145 C CD2 . TYR D 304 ? 0.4145 0.3655 0.6745 0.1235  0.0414  0.0142  304 TYR D CD2 
15146 C CE1 . TYR D 304 ? 0.4193 0.3294 0.6446 0.1216  0.0457  0.0006  304 TYR D CE1 
15147 C CE2 . TYR D 304 ? 0.4557 0.3965 0.7088 0.1334  0.0494  0.0122  304 TYR D CE2 
15148 C CZ  . TYR D 304 ? 0.4732 0.3926 0.7081 0.1324  0.0516  0.0051  304 TYR D CZ  
15149 O OH  . TYR D 304 ? 0.4790 0.3867 0.7050 0.1421  0.0596  0.0027  304 TYR D OH  
15150 N N   . GLY D 305 ? 0.3353 0.3216 0.6108 0.0855  0.0182  0.0152  305 GLY D N   
15151 C CA  . GLY D 305 ? 0.3185 0.3132 0.5984 0.0769  0.0117  0.0165  305 GLY D CA  
15152 C C   . GLY D 305 ? 0.3263 0.3100 0.6006 0.0746  0.0070  0.0164  305 GLY D C   
15153 O O   . GLY D 305 ? 0.3445 0.3139 0.6118 0.0792  0.0086  0.0154  305 GLY D O   
15154 N N   . THR D 306 ? 0.3174 0.3077 0.5945 0.0674  0.0014  0.0176  306 THR D N   
15155 C CA  . THR D 306 ? 0.3167 0.2986 0.5892 0.0646  -0.0028 0.0181  306 THR D CA  
15156 C C   . THR D 306 ? 0.3139 0.2957 0.5825 0.0554  -0.0064 0.0151  306 THR D C   
15157 O O   . THR D 306 ? 0.3078 0.2993 0.5801 0.0516  -0.0068 0.0143  306 THR D O   
15158 C CB  . THR D 306 ? 0.3090 0.2994 0.5893 0.0671  -0.0058 0.0241  306 THR D CB  
15159 O OG1 . THR D 306 ? 0.3001 0.3066 0.5880 0.0622  -0.0085 0.0256  306 THR D OG1 
15160 C CG2 . THR D 306 ? 0.3007 0.2912 0.5855 0.0771  -0.0023 0.0278  306 THR D CG2 
15161 N N   . PRO D 307 ? 0.3144 0.2852 0.5758 0.0519  -0.0090 0.0137  307 PRO D N   
15162 C CA  . PRO D 307 ? 0.2963 0.2672 0.5544 0.0439  -0.0121 0.0113  307 PRO D CA  
15163 C C   . PRO D 307 ? 0.2807 0.2632 0.5441 0.0398  -0.0160 0.0141  307 PRO D C   
15164 O O   . PRO D 307 ? 0.2979 0.2833 0.5640 0.0414  -0.0181 0.0181  307 PRO D O   
15165 C CB  . PRO D 307 ? 0.3030 0.2588 0.5526 0.0424  -0.0129 0.0098  307 PRO D CB  
15166 C CG  . PRO D 307 ? 0.3088 0.2597 0.5590 0.0485  -0.0123 0.0134  307 PRO D CG  
15167 C CD  . PRO D 307 ? 0.3116 0.2688 0.5675 0.0555  -0.0087 0.0146  307 PRO D CD  
15168 N N   . ARG D 308 ? 0.2605 0.2486 0.5242 0.0345  -0.0170 0.0119  308 ARG D N   
15169 C CA  . ARG D 308 ? 0.2459 0.2422 0.5119 0.0298  -0.0207 0.0134  308 ARG D CA  
15170 C C   . ARG D 308 ? 0.2420 0.2310 0.5017 0.0258  -0.0225 0.0123  308 ARG D C   
15171 O O   . ARG D 308 ? 0.2445 0.2233 0.4990 0.0256  -0.0213 0.0102  308 ARG D O   
15172 C CB  . ARG D 308 ? 0.2491 0.2529 0.5175 0.0264  -0.0205 0.0112  308 ARG D CB  
15173 C CG  . ARG D 308 ? 0.2325 0.2452 0.5080 0.0298  -0.0185 0.0129  308 ARG D CG  
15174 C CD  . ARG D 308 ? 0.2359 0.2523 0.5116 0.0258  -0.0178 0.0103  308 ARG D CD  
15175 N NE  . ARG D 308 ? 0.2144 0.2416 0.4979 0.0274  -0.0165 0.0125  308 ARG D NE  
15176 C CZ  . ARG D 308 ? 0.2228 0.2525 0.5074 0.0269  -0.0137 0.0111  308 ARG D CZ  
15177 N NH1 . ARG D 308 ? 0.2253 0.2475 0.5035 0.0247  -0.0123 0.0071  308 ARG D NH1 
15178 N NH2 . ARG D 308 ? 0.2349 0.2760 0.5279 0.0282  -0.0127 0.0143  308 ARG D NH2 
15179 N N   . PRO D 309 ? 0.2478 0.2418 0.5075 0.0224  -0.0256 0.0141  309 PRO D N   
15180 C CA  . PRO D 309 ? 0.2488 0.2369 0.5030 0.0191  -0.0268 0.0140  309 PRO D CA  
15181 C C   . PRO D 309 ? 0.2693 0.2514 0.5194 0.0158  -0.0255 0.0101  309 PRO D C   
15182 O O   . PRO D 309 ? 0.3188 0.2940 0.5651 0.0142  -0.0256 0.0103  309 PRO D O   
15183 C CB  . PRO D 309 ? 0.2480 0.2442 0.5026 0.0159  -0.0297 0.0155  309 PRO D CB  
15184 C CG  . PRO D 309 ? 0.2585 0.2630 0.5193 0.0191  -0.0310 0.0188  309 PRO D CG  
15185 C CD  . PRO D 309 ? 0.2571 0.2622 0.5218 0.0220  -0.0280 0.0169  309 PRO D CD  
15186 N N   . VAL D 310 ? 0.2476 0.2329 0.4988 0.0144  -0.0246 0.0071  310 VAL D N   
15187 C CA  . VAL D 310 ? 0.2571 0.2378 0.5050 0.0115  -0.0237 0.0037  310 VAL D CA  
15188 C C   . VAL D 310 ? 0.2686 0.2393 0.5133 0.0129  -0.0225 0.0029  310 VAL D C   
15189 O O   . VAL D 310 ? 0.2701 0.2361 0.5118 0.0099  -0.0228 0.0014  310 VAL D O   
15190 C CB  . VAL D 310 ? 0.2303 0.2151 0.4798 0.0107  -0.0228 0.0011  310 VAL D CB  
15191 C CG1 . VAL D 310 ? 0.2271 0.2130 0.4793 0.0146  -0.0209 0.0011  310 VAL D CG1 
15192 C CG2 . VAL D 310 ? 0.2238 0.2044 0.4702 0.0081  -0.0223 -0.0019 310 VAL D CG2 
15193 N N   . TRP D 311 ? 0.2734 0.2406 0.5186 0.0175  -0.0212 0.0038  311 TRP D N   
15194 C CA  . TRP D 311 ? 0.2758 0.2316 0.5164 0.0190  -0.0201 0.0026  311 TRP D CA  
15195 C C   . TRP D 311 ? 0.2742 0.2231 0.5114 0.0164  -0.0217 0.0042  311 TRP D C   
15196 O O   . TRP D 311 ? 0.3015 0.2427 0.5346 0.0136  -0.0220 0.0023  311 TRP D O   
15197 C CB  . TRP D 311 ? 0.2720 0.2252 0.5135 0.0253  -0.0180 0.0038  311 TRP D CB  
15198 C CG  . TRP D 311 ? 0.2770 0.2163 0.5122 0.0276  -0.0166 0.0022  311 TRP D CG  
15199 C CD1 . TRP D 311 ? 0.2688 0.1989 0.5012 0.0302  -0.0167 0.0043  311 TRP D CD1 
15200 C CD2 . TRP D 311 ? 0.2650 0.1972 0.4950 0.0278  -0.0148 -0.0018 311 TRP D CD2 
15201 N NE1 . TRP D 311 ? 0.2673 0.1841 0.4926 0.0317  -0.0152 0.0016  311 TRP D NE1 
15202 C CE2 . TRP D 311 ? 0.2730 0.1910 0.4965 0.0303  -0.0140 -0.0023 311 TRP D CE2 
15203 C CE3 . TRP D 311 ? 0.2548 0.1905 0.4842 0.0262  -0.0139 -0.0048 311 TRP D CE3 
15204 C CZ2 . TRP D 311 ? 0.2718 0.1788 0.4875 0.0310  -0.0125 -0.0061 311 TRP D CZ2 
15205 C CZ3 . TRP D 311 ? 0.2627 0.1884 0.4849 0.0269  -0.0124 -0.0082 311 TRP D CZ3 
15206 C CH2 . TRP D 311 ? 0.2789 0.1905 0.4942 0.0294  -0.0116 -0.0090 311 TRP D CH2 
15207 N N   . PHE D 312 ? 0.2836 0.2361 0.5228 0.0168  -0.0230 0.0079  312 PHE D N   
15208 C CA  . PHE D 312 ? 0.2905 0.2368 0.5266 0.0146  -0.0243 0.0104  312 PHE D CA  
15209 C C   . PHE D 312 ? 0.2910 0.2412 0.5267 0.0088  -0.0252 0.0100  312 PHE D C   
15210 O O   . PHE D 312 ? 0.2714 0.2157 0.5044 0.0056  -0.0257 0.0106  312 PHE D O   
15211 C CB  . PHE D 312 ? 0.2979 0.2468 0.5358 0.0179  -0.0252 0.0149  312 PHE D CB  
15212 C CG  . PHE D 312 ? 0.3182 0.2630 0.5572 0.0244  -0.0239 0.0159  312 PHE D CG  
15213 C CD1 . PHE D 312 ? 0.3298 0.2613 0.5643 0.0268  -0.0230 0.0162  312 PHE D CD1 
15214 C CD2 . PHE D 312 ? 0.3248 0.2791 0.5694 0.0283  -0.0233 0.0166  312 PHE D CD2 
15215 C CE1 . PHE D 312 ? 0.3451 0.2723 0.5802 0.0337  -0.0212 0.0171  312 PHE D CE1 
15216 C CE2 . PHE D 312 ? 0.3422 0.2943 0.5889 0.0351  -0.0215 0.0180  312 PHE D CE2 
15217 C CZ  . PHE D 312 ? 0.3341 0.2723 0.5758 0.0382  -0.0201 0.0181  312 PHE D CZ  
15218 N N   . ALA D 313 ? 0.2770 0.2371 0.5154 0.0076  -0.0254 0.0090  313 ALA D N   
15219 C CA  . ALA D 313 ? 0.2683 0.2318 0.5061 0.0031  -0.0255 0.0084  313 ALA D CA  
15220 C C   . ALA D 313 ? 0.2795 0.2390 0.5166 0.0008  -0.0251 0.0055  313 ALA D C   
15221 O O   . ALA D 313 ? 0.3193 0.2781 0.5559 -0.0028 -0.0254 0.0062  313 ALA D O   
15222 C CB  . ALA D 313 ? 0.2617 0.2344 0.5012 0.0026  -0.0257 0.0076  313 ALA D CB  
15223 N N   . MET D 314 ? 0.2786 0.2359 0.5156 0.0027  -0.0245 0.0027  314 MET D N   
15224 C CA  . MET D 314 ? 0.2930 0.2461 0.5283 0.0005  -0.0247 0.0000  314 MET D CA  
15225 C C   . MET D 314 ? 0.2974 0.2399 0.5290 -0.0009 -0.0255 0.0006  314 MET D C   
15226 O O   . MET D 314 ? 0.2901 0.2308 0.5210 -0.0050 -0.0267 0.0002  314 MET D O   
15227 C CB  . MET D 314 ? 0.3013 0.2543 0.5363 0.0031  -0.0236 -0.0029 314 MET D CB  
15228 C CG  . MET D 314 ? 0.2973 0.2593 0.5354 0.0030  -0.0232 -0.0040 314 MET D CG  
15229 S SD  . MET D 314 ? 0.3349 0.2990 0.5731 -0.0011 -0.0240 -0.0057 314 MET D SD  
15230 C CE  . MET D 314 ? 0.3483 0.3052 0.5827 -0.0008 -0.0241 -0.0086 314 MET D CE  
15231 N N   . ARG D 315 ? 0.3227 0.2579 0.5518 0.0023  -0.0251 0.0018  315 ARG D N   
15232 C CA  . ARG D 315 ? 0.3428 0.2660 0.5672 0.0008  -0.0261 0.0023  315 ARG D CA  
15233 C C   . ARG D 315 ? 0.3509 0.2752 0.5763 -0.0044 -0.0275 0.0053  315 ARG D C   
15234 O O   . ARG D 315 ? 0.3434 0.2617 0.5665 -0.0088 -0.0290 0.0050  315 ARG D O   
15235 C CB  . ARG D 315 ? 0.3585 0.2739 0.5805 0.0057  -0.0252 0.0040  315 ARG D CB  
15236 C CG  . ARG D 315 ? 0.3661 0.2666 0.5820 0.0040  -0.0263 0.0044  315 ARG D CG  
15237 C CD  . ARG D 315 ? 0.4172 0.3103 0.6310 0.0095  -0.0253 0.0068  315 ARG D CD  
15238 N NE  . ARG D 315 ? 0.4657 0.3661 0.6836 0.0098  -0.0258 0.0114  315 ARG D NE  
15239 C CZ  . ARG D 315 ? 0.4616 0.3613 0.6804 0.0151  -0.0252 0.0145  315 ARG D CZ  
15240 N NH1 . ARG D 315 ? 0.4559 0.3466 0.6720 0.0209  -0.0238 0.0139  315 ARG D NH1 
15241 N NH2 . ARG D 315 ? 0.4778 0.3858 0.7000 0.0147  -0.0262 0.0185  315 ARG D NH2 
15242 N N   . ASP D 316 ? 0.3672 0.2989 0.5955 -0.0039 -0.0271 0.0083  316 ASP D N   
15243 C CA  . ASP D 316 ? 0.3730 0.3061 0.6019 -0.0082 -0.0277 0.0117  316 ASP D CA  
15244 C C   . ASP D 316 ? 0.3321 0.2726 0.5641 -0.0126 -0.0278 0.0106  316 ASP D C   
15245 O O   . ASP D 316 ? 0.3209 0.2600 0.5532 -0.0173 -0.0286 0.0124  316 ASP D O   
15246 C CB  . ASP D 316 ? 0.3768 0.3156 0.6066 -0.0065 -0.0272 0.0152  316 ASP D CB  
15247 C CG  . ASP D 316 ? 0.3776 0.3100 0.6051 -0.0023 -0.0275 0.0177  316 ASP D CG  
15248 O OD1 . ASP D 316 ? 0.3926 0.3147 0.6175 -0.0002 -0.0277 0.0167  316 ASP D OD1 
15249 O OD2 . ASP D 316 ? 0.3917 0.3296 0.6200 -0.0007 -0.0276 0.0205  316 ASP D OD2 
15250 N N   . TYR D 317 ? 0.3008 0.2488 0.5352 -0.0111 -0.0270 0.0078  317 TYR D N   
15251 C CA  . TYR D 317 ? 0.3045 0.2597 0.5422 -0.0142 -0.0269 0.0069  317 TYR D CA  
15252 C C   . TYR D 317 ? 0.3053 0.2551 0.5423 -0.0177 -0.0288 0.0057  317 TYR D C   
15253 O O   . TYR D 317 ? 0.2833 0.2373 0.5234 -0.0218 -0.0294 0.0071  317 TYR D O   
15254 C CB  . TYR D 317 ? 0.2858 0.2479 0.5253 -0.0115 -0.0260 0.0041  317 TYR D CB  
15255 C CG  . TYR D 317 ? 0.2694 0.2391 0.5124 -0.0137 -0.0255 0.0037  317 TYR D CG  
15256 C CD1 . TYR D 317 ? 0.2656 0.2422 0.5104 -0.0144 -0.0239 0.0057  317 TYR D CD1 
15257 C CD2 . TYR D 317 ? 0.2804 0.2503 0.5245 -0.0147 -0.0265 0.0014  317 TYR D CD2 
15258 C CE1 . TYR D 317 ? 0.2630 0.2467 0.5114 -0.0156 -0.0229 0.0056  317 TYR D CE1 
15259 C CE2 . TYR D 317 ? 0.2856 0.2629 0.5337 -0.0162 -0.0261 0.0016  317 TYR D CE2 
15260 C CZ  . TYR D 317 ? 0.2507 0.2350 0.5012 -0.0163 -0.0241 0.0037  317 TYR D CZ  
15261 O OH  . TYR D 317 ? 0.2566 0.2483 0.5112 -0.0168 -0.0231 0.0040  317 TYR D OH  
15262 N N   . MET D 318 ? 0.3325 0.2732 0.5654 -0.0162 -0.0297 0.0033  318 MET D N   
15263 C CA  . MET D 318 ? 0.3338 0.2690 0.5645 -0.0196 -0.0319 0.0013  318 MET D CA  
15264 C C   . MET D 318 ? 0.3278 0.2553 0.5566 -0.0247 -0.0341 0.0036  318 MET D C   
15265 O O   . MET D 318 ? 0.3431 0.2666 0.5703 -0.0286 -0.0366 0.0024  318 MET D O   
15266 C CB  . MET D 318 ? 0.3284 0.2554 0.5536 -0.0162 -0.0319 -0.0024 318 MET D CB  
15267 C CG  . MET D 318 ? 0.3084 0.2429 0.5357 -0.0130 -0.0304 -0.0047 318 MET D CG  
15268 S SD  . MET D 318 ? 0.3212 0.2466 0.5417 -0.0093 -0.0298 -0.0087 318 MET D SD  
15269 C CE  . MET D 318 ? 0.3087 0.2277 0.5271 -0.0042 -0.0276 -0.0073 318 MET D CE  
15270 N N   . LYS D 319 ? 0.3482 0.2737 0.5769 -0.0251 -0.0334 0.0071  319 LYS D N   
15271 C CA  . LYS D 319 ? 0.4127 0.3297 0.6391 -0.0303 -0.0354 0.0097  319 LYS D CA  
15272 C C   . LYS D 319 ? 0.4043 0.3287 0.6360 -0.0370 -0.0370 0.0117  319 LYS D C   
15273 O O   . LYS D 319 ? 0.4029 0.3201 0.6326 -0.0425 -0.0401 0.0121  319 LYS D O   
15274 C CB  . LYS D 319 ? 0.4668 0.3804 0.6920 -0.0290 -0.0341 0.0135  319 LYS D CB  
15275 C CG  . LYS D 319 ? 0.4986 0.4026 0.7185 -0.0228 -0.0332 0.0126  319 LYS D CG  
15276 C CD  . LYS D 319 ? 0.5359 0.4374 0.7550 -0.0216 -0.0324 0.0172  319 LYS D CD  
15277 C CE  . LYS D 319 ? 0.5974 0.4914 0.8129 -0.0147 -0.0314 0.0172  319 LYS D CE  
15278 N NZ  . LYS D 319 ? 0.5690 0.4648 0.7849 -0.0131 -0.0308 0.0220  319 LYS D NZ  
15279 N N   . GLY D 320 ? 0.3731 0.3120 0.6116 -0.0366 -0.0351 0.0132  320 GLY D N   
15280 C CA  . GLY D 320 ? 0.3676 0.3160 0.6127 -0.0417 -0.0361 0.0152  320 GLY D CA  
15281 C C   . GLY D 320 ? 0.3628 0.3239 0.6131 -0.0386 -0.0343 0.0136  320 GLY D C   
15282 O O   . GLY D 320 ? 0.3305 0.2985 0.5826 -0.0350 -0.0311 0.0142  320 GLY D O   
15283 N N   . LEU D 321 ? 0.3729 0.3360 0.6250 -0.0403 -0.0367 0.0117  321 LEU D N   
15284 C CA  . LEU D 321 ? 0.3546 0.3279 0.6110 -0.0371 -0.0354 0.0101  321 LEU D CA  
15285 C C   . LEU D 321 ? 0.3183 0.3038 0.5834 -0.0405 -0.0353 0.0136  321 LEU D C   
15286 O O   . LEU D 321 ? 0.3500 0.3353 0.6176 -0.0463 -0.0384 0.0158  321 LEU D O   
15287 C CB  . LEU D 321 ? 0.3485 0.3167 0.6010 -0.0357 -0.0377 0.0059  321 LEU D CB  
15288 C CG  . LEU D 321 ? 0.3593 0.3178 0.6043 -0.0311 -0.0366 0.0025  321 LEU D CG  
15289 C CD1 . LEU D 321 ? 0.3760 0.3292 0.6163 -0.0302 -0.0386 -0.0012 321 LEU D CD1 
15290 C CD2 . LEU D 321 ? 0.3504 0.3143 0.5965 -0.0257 -0.0330 0.0020  321 LEU D CD2 
15291 N N   . ILE D 322 ? 0.2883 0.2842 0.5578 -0.0368 -0.0317 0.0142  322 ILE D N   
15292 C CA  . ILE D 322 ? 0.2749 0.2839 0.5532 -0.0381 -0.0305 0.0174  322 ILE D CA  
15293 C C   . ILE D 322 ? 0.2695 0.2828 0.5500 -0.0352 -0.0314 0.0149  322 ILE D C   
15294 O O   . ILE D 322 ? 0.2690 0.2816 0.5465 -0.0299 -0.0292 0.0121  322 ILE D O   
15295 C CB  . ILE D 322 ? 0.2578 0.2743 0.5382 -0.0353 -0.0253 0.0196  322 ILE D CB  
15296 C CG1 . ILE D 322 ? 0.2661 0.2774 0.5426 -0.0371 -0.0241 0.0219  322 ILE D CG1 
15297 C CG2 . ILE D 322 ? 0.2408 0.2713 0.5308 -0.0362 -0.0233 0.0234  322 ILE D CG2 
15298 C CD1 . ILE D 322 ? 0.2585 0.2733 0.5326 -0.0328 -0.0194 0.0223  322 ILE D CD1 
15299 N N   . ILE D 323 ? 0.2666 0.2841 0.5521 -0.0389 -0.0350 0.0163  323 ILE D N   
15300 C CA  . ILE D 323 ? 0.2720 0.2942 0.5601 -0.0365 -0.0364 0.0149  323 ILE D CA  
15301 C C   . ILE D 323 ? 0.2661 0.3032 0.5646 -0.0350 -0.0339 0.0185  323 ILE D C   
15302 O O   . ILE D 323 ? 0.2544 0.2958 0.5546 -0.0302 -0.0325 0.0173  323 ILE D O   
15303 C CB  . ILE D 323 ? 0.2898 0.3065 0.5757 -0.0412 -0.0424 0.0141  323 ILE D CB  
15304 C CG1 . ILE D 323 ? 0.3054 0.3072 0.5801 -0.0404 -0.0437 0.0096  323 ILE D CG1 
15305 C CG2 . ILE D 323 ? 0.3000 0.3243 0.5907 -0.0399 -0.0446 0.0143  323 ILE D CG2 
15306 C CD1 . ILE D 323 ? 0.3370 0.3288 0.6065 -0.0441 -0.0447 0.0099  323 ILE D CD1 
15307 N N   . SER D 324 ? 0.2569 0.3019 0.5625 -0.0390 -0.0334 0.0232  324 SER D N   
15308 C CA  . SER D 324 ? 0.2698 0.3296 0.5854 -0.0368 -0.0297 0.0271  324 SER D CA  
15309 C C   . SER D 324 ? 0.2804 0.3437 0.5981 -0.0393 -0.0261 0.0308  324 SER D C   
15310 O O   . SER D 324 ? 0.3184 0.3748 0.6330 -0.0449 -0.0287 0.0317  324 SER D O   
15311 C CB  . SER D 324 ? 0.2768 0.3472 0.6024 -0.0398 -0.0335 0.0305  324 SER D CB  
15312 O OG  . SER D 324 ? 0.2612 0.3264 0.5831 -0.0388 -0.0378 0.0273  324 SER D OG  
15313 N N   . PRO D 325 ? 0.2585 0.3310 0.5801 -0.0351 -0.0200 0.0328  325 PRO D N   
15314 C CA  . PRO D 325 ? 0.2363 0.3136 0.5590 -0.0277 -0.0163 0.0310  325 PRO D CA  
15315 C C   . PRO D 325 ? 0.2418 0.3071 0.5534 -0.0231 -0.0158 0.0251  325 PRO D C   
15316 O O   . PRO D 325 ? 0.2176 0.2728 0.5213 -0.0247 -0.0167 0.0231  325 PRO D O   
15317 C CB  . PRO D 325 ? 0.2347 0.3218 0.5616 -0.0253 -0.0096 0.0345  325 PRO D CB  
15318 C CG  . PRO D 325 ? 0.2364 0.3180 0.5586 -0.0299 -0.0093 0.0359  325 PRO D CG  
15319 C CD  . PRO D 325 ? 0.2467 0.3245 0.5710 -0.0374 -0.0161 0.0372  325 PRO D CD  
15320 N N   . LYS D 326 ? 0.2479 0.3149 0.5596 -0.0172 -0.0141 0.0229  326 LYS D N   
15321 C CA  . LYS D 326 ? 0.2470 0.3036 0.5493 -0.0133 -0.0140 0.0177  326 LYS D CA  
15322 C C   . LYS D 326 ? 0.2305 0.2862 0.5277 -0.0084 -0.0082 0.0162  326 LYS D C   
15323 O O   . LYS D 326 ? 0.2062 0.2701 0.5077 -0.0052 -0.0037 0.0183  326 LYS D O   
15324 C CB  . LYS D 326 ? 0.2741 0.3309 0.5783 -0.0111 -0.0167 0.0162  326 LYS D CB  
15325 C CG  . LYS D 326 ? 0.3013 0.3548 0.6059 -0.0161 -0.0230 0.0162  326 LYS D CG  
15326 C CD  . LYS D 326 ? 0.3095 0.3644 0.6162 -0.0140 -0.0259 0.0155  326 LYS D CD  
15327 C CE  . LYS D 326 ? 0.3287 0.3801 0.6346 -0.0192 -0.0322 0.0155  326 LYS D CE  
15328 N NZ  . LYS D 326 ? 0.3174 0.3731 0.6283 -0.0256 -0.0346 0.0190  326 LYS D NZ  
15329 N N   . ASN D 327 ? 0.2349 0.2806 0.5227 -0.0078 -0.0085 0.0127  327 ASN D N   
15330 C CA  . ASN D 327 ? 0.2369 0.2796 0.5178 -0.0039 -0.0043 0.0106  327 ASN D CA  
15331 C C   . ASN D 327 ? 0.2354 0.2794 0.5165 0.0016  -0.0019 0.0087  327 ASN D C   
15332 O O   . ASN D 327 ? 0.2165 0.2581 0.4985 0.0025  -0.0047 0.0071  327 ASN D O   
15333 C CB  . ASN D 327 ? 0.2239 0.2562 0.4958 -0.0046 -0.0063 0.0073  327 ASN D CB  
15334 C CG  . ASN D 327 ? 0.2410 0.2706 0.5054 -0.0023 -0.0028 0.0061  327 ASN D CG  
15335 O OD1 . ASN D 327 ? 0.2410 0.2749 0.5055 -0.0025 0.0006  0.0086  327 ASN D OD1 
15336 N ND2 . ASN D 327 ? 0.2600 0.2825 0.5174 -0.0005 -0.0036 0.0024  327 ASN D ND2 
15337 N N   . LYS D 328 ? 0.2452 0.2924 0.5248 0.0054  0.0034  0.0091  328 LYS D N   
15338 C CA  . LYS D 328 ? 0.2831 0.3309 0.5623 0.0113  0.0067  0.0077  328 LYS D CA  
15339 C C   . LYS D 328 ? 0.2819 0.3389 0.5722 0.0127  0.0060  0.0106  328 LYS D C   
15340 O O   . LYS D 328 ? 0.3340 0.3894 0.6246 0.0170  0.0064  0.0092  328 LYS D O   
15341 C CB  . LYS D 328 ? 0.2855 0.3220 0.5556 0.0132  0.0052  0.0027  328 LYS D CB  
15342 C CG  . LYS D 328 ? 0.3040 0.3326 0.5639 0.0115  0.0051  0.0002  328 LYS D CG  
15343 C CD  . LYS D 328 ? 0.3327 0.3630 0.5880 0.0132  0.0102  0.0010  328 LYS D CD  
15344 C CE  . LYS D 328 ? 0.3520 0.3750 0.5974 0.0109  0.0090  -0.0011 328 LYS D CE  
15345 N NZ  . LYS D 328 ? 0.3644 0.3780 0.6021 0.0120  0.0071  -0.0055 328 LYS D NZ  
15346 N N   . SER D 329 ? 0.2559 0.3225 0.5554 0.0090  0.0051  0.0152  329 SER D N   
15347 C CA  . SER D 329 ? 0.2386 0.3163 0.5500 0.0098  0.0043  0.0190  329 SER D CA  
15348 C C   . SER D 329 ? 0.2355 0.3237 0.5525 0.0144  0.0110  0.0222  329 SER D C   
15349 O O   . SER D 329 ? 0.2431 0.3319 0.5564 0.0143  0.0155  0.0228  329 SER D O   
15350 C CB  . SER D 329 ? 0.2317 0.3146 0.5504 0.0027  -0.0009 0.0224  329 SER D CB  
15351 O OG  . SER D 329 ? 0.2135 0.3010 0.5340 -0.0009 0.0013  0.0255  329 SER D OG  
15352 N N   . ILE D 330 ? 0.2545 0.3513 0.5807 0.0184  0.0117  0.0247  330 ILE D N   
15353 C CA  . ILE D 330 ? 0.2608 0.3690 0.5941 0.0240  0.0185  0.0282  330 ILE D CA  
15354 C C   . ILE D 330 ? 0.2512 0.3759 0.6005 0.0206  0.0163  0.0348  330 ILE D C   
15355 O O   . ILE D 330 ? 0.2747 0.4009 0.6293 0.0180  0.0101  0.0357  330 ILE D O   
15356 C CB  . ILE D 330 ? 0.2834 0.3873 0.6136 0.0327  0.0217  0.0256  330 ILE D CB  
15357 C CG1 . ILE D 330 ? 0.2954 0.3830 0.6090 0.0352  0.0241  0.0192  330 ILE D CG1 
15358 C CG2 . ILE D 330 ? 0.2840 0.4015 0.6241 0.0393  0.0284  0.0300  330 ILE D CG2 
15359 C CD1 . ILE D 330 ? 0.3243 0.4036 0.6326 0.0425  0.0259  0.0159  330 ILE D CD1 
15360 N N   . HIS D 331 ? 0.2455 0.3821 0.6018 0.0203  0.0214  0.0394  331 HIS D N   
15361 C CA  . HIS D 331 ? 0.2380 0.3908 0.6095 0.0153  0.0194  0.0463  331 HIS D CA  
15362 C C   . HIS D 331 ? 0.2428 0.4118 0.6254 0.0216  0.0268  0.0514  331 HIS D C   
15363 O O   . HIS D 331 ? 0.2398 0.4072 0.6163 0.0268  0.0346  0.0502  331 HIS D O   
15364 C CB  . HIS D 331 ? 0.2391 0.3906 0.6083 0.0067  0.0179  0.0479  331 HIS D CB  
15365 C CG  . HIS D 331 ? 0.2478 0.3874 0.6108 -0.0001 0.0096  0.0447  331 HIS D CG  
15366 N ND1 . HIS D 331 ? 0.2576 0.3803 0.6061 0.0004  0.0082  0.0384  331 HIS D ND1 
15367 C CD2 . HIS D 331 ? 0.2459 0.3884 0.6155 -0.0067 0.0021  0.0469  331 HIS D CD2 
15368 C CE1 . HIS D 331 ? 0.2626 0.3786 0.6092 -0.0056 0.0008  0.0370  331 HIS D CE1 
15369 N NE2 . HIS D 331 ? 0.2560 0.3829 0.6144 -0.0101 -0.0030 0.0419  331 HIS D NE2 
15370 N N   . THR D 332 ? 0.2760 0.4605 0.6746 0.0214  0.0244  0.0570  332 THR D N   
15371 C CA  . THR D 332 ? 0.3032 0.5052 0.7147 0.0284  0.0315  0.0625  332 THR D CA  
15372 C C   . THR D 332 ? 0.3158 0.5372 0.7440 0.0213  0.0299  0.0708  332 THR D C   
15373 O O   . THR D 332 ? 0.3898 0.6295 0.8329 0.0254  0.0340  0.0769  332 THR D O   
15374 C CB  . THR D 332 ? 0.3025 0.5065 0.7188 0.0366  0.0309  0.0623  332 THR D CB  
15375 O OG1 . THR D 332 ? 0.2938 0.4972 0.7141 0.0301  0.0206  0.0629  332 THR D OG1 
15376 C CG2 . THR D 332 ? 0.2963 0.4817 0.6963 0.0443  0.0340  0.0548  332 THR D CG2 
15377 N N   . ASN D 333 ? 0.3549 0.5719 0.7803 0.0108  0.0245  0.0710  333 ASN D N   
15378 C CA  . ASN D 333 ? 0.3254 0.5570 0.7642 0.0016  0.0214  0.0781  333 ASN D CA  
15379 C C   . ASN D 333 ? 0.2951 0.5173 0.7238 -0.0052 0.0223  0.0769  333 ASN D C   
15380 O O   . ASN D 333 ? 0.3156 0.5192 0.7295 -0.0072 0.0188  0.0706  333 ASN D O   
15381 C CB  . ASN D 333 ? 0.3460 0.5784 0.7907 -0.0056 0.0103  0.0792  333 ASN D CB  
15382 C CG  . ASN D 333 ? 0.4328 0.6839 0.8945 -0.0141 0.0071  0.0878  333 ASN D CG  
15383 O OD1 . ASN D 333 ? 0.4228 0.6712 0.8828 -0.0236 0.0046  0.0893  333 ASN D OD1 
15384 N ND2 . ASN D 333 ? 0.4536 0.7243 0.9325 -0.0108 0.0075  0.0939  333 ASN D ND2 
15385 N N   . THR D 334 ? 0.2760 0.5111 0.7130 -0.0090 0.0266  0.0832  334 THR D N   
15386 C CA  . THR D 334 ? 0.2812 0.5078 0.7091 -0.0156 0.0275  0.0829  334 THR D CA  
15387 C C   . THR D 334 ? 0.2905 0.5112 0.7187 -0.0278 0.0176  0.0839  334 THR D C   
15388 O O   . THR D 334 ? 0.2858 0.4982 0.7065 -0.0337 0.0173  0.0838  334 THR D O   
15389 C CB  . THR D 334 ? 0.2696 0.5118 0.7054 -0.0147 0.0366  0.0896  334 THR D CB  
15390 O OG1 . THR D 334 ? 0.2607 0.5224 0.7159 -0.0205 0.0335  0.0976  334 THR D OG1 
15391 C CG2 . THR D 334 ? 0.2770 0.5250 0.7121 -0.0024 0.0471  0.0888  334 THR D CG2 
15392 N N   . LYS D 335 ? 0.3053 0.5284 0.7405 -0.0315 0.0092  0.0844  335 LYS D N   
15393 C CA  . LYS D 335 ? 0.3340 0.5463 0.7648 -0.0419 -0.0004 0.0831  335 LYS D CA  
15394 C C   . LYS D 335 ? 0.3432 0.5361 0.7597 -0.0390 -0.0050 0.0747  335 LYS D C   
15395 O O   . LYS D 335 ? 0.3776 0.5724 0.7969 -0.0348 -0.0078 0.0731  335 LYS D O   
15396 C CB  . LYS D 335 ? 0.3761 0.6013 0.8217 -0.0495 -0.0081 0.0887  335 LYS D CB  
15397 C CG  . LYS D 335 ? 0.4283 0.6716 0.8891 -0.0571 -0.0070 0.0980  335 LYS D CG  
15398 C CD  . LYS D 335 ? 0.4923 0.7258 0.9474 -0.0687 -0.0110 0.0991  335 LYS D CD  
15399 C CE  . LYS D 335 ? 0.4703 0.7215 0.9415 -0.0784 -0.0123 0.1087  335 LYS D CE  
15400 N NZ  . LYS D 335 ? 0.4851 0.7474 0.9610 -0.0761 -0.0022 0.1138  335 LYS D NZ  
15401 N N   . ILE D 336 ? 0.3287 0.5039 0.7305 -0.0417 -0.0060 0.0701  336 ILE D N   
15402 C CA  . ILE D 336 ? 0.3698 0.5264 0.7569 -0.0383 -0.0086 0.0622  336 ILE D CA  
15403 C C   . ILE D 336 ? 0.3507 0.4959 0.7330 -0.0467 -0.0176 0.0604  336 ILE D C   
15404 O O   . ILE D 336 ? 0.3946 0.5336 0.7731 -0.0532 -0.0187 0.0616  336 ILE D O   
15405 C CB  . ILE D 336 ? 0.3966 0.5420 0.7707 -0.0343 -0.0027 0.0584  336 ILE D CB  
15406 C CG1 . ILE D 336 ? 0.4251 0.5794 0.8012 -0.0257 0.0063  0.0592  336 ILE D CG1 
15407 C CG2 . ILE D 336 ? 0.4349 0.5615 0.7943 -0.0321 -0.0058 0.0508  336 ILE D CG2 
15408 C CD1 . ILE D 336 ? 0.4213 0.5857 0.8062 -0.0191 0.0072  0.0597  336 ILE D CD1 
15409 N N   . PRO D 337 ? 0.2963 0.4370 0.6772 -0.0465 -0.0237 0.0573  337 PRO D N   
15410 C CA  . PRO D 337 ? 0.3060 0.4330 0.6791 -0.0537 -0.0316 0.0546  337 PRO D CA  
15411 C C   . PRO D 337 ? 0.3589 0.4677 0.7168 -0.0526 -0.0300 0.0493  337 PRO D C   
15412 O O   . PRO D 337 ? 0.3287 0.4318 0.6793 -0.0453 -0.0255 0.0451  337 PRO D O   
15413 C CB  . PRO D 337 ? 0.2814 0.4078 0.6548 -0.0516 -0.0369 0.0521  337 PRO D CB  
15414 C CG  . PRO D 337 ? 0.2718 0.4156 0.6576 -0.0450 -0.0328 0.0558  337 PRO D CG  
15415 C CD  . PRO D 337 ? 0.2831 0.4307 0.6689 -0.0396 -0.0235 0.0565  337 PRO D CD  
15416 N N   . LEU D 338 ? 0.3548 0.4547 0.7083 -0.0604 -0.0336 0.0500  338 LEU D N   
15417 C CA  . LEU D 338 ? 0.3422 0.4243 0.6820 -0.0603 -0.0336 0.0454  338 LEU D CA  
15418 C C   . LEU D 338 ? 0.3039 0.3724 0.6361 -0.0644 -0.0410 0.0417  338 LEU D C   
15419 O O   . LEU D 338 ? 0.2904 0.3613 0.6270 -0.0714 -0.0467 0.0441  338 LEU D O   
15420 C CB  . LEU D 338 ? 0.3950 0.4778 0.7358 -0.0651 -0.0311 0.0498  338 LEU D CB  
15421 C CG  . LEU D 338 ? 0.4238 0.4885 0.7519 -0.0670 -0.0322 0.0470  338 LEU D CG  
15422 C CD1 . LEU D 338 ? 0.4208 0.4791 0.7402 -0.0589 -0.0276 0.0426  338 LEU D CD1 
15423 C CD2 . LEU D 338 ? 0.4575 0.5237 0.7881 -0.0733 -0.0310 0.0525  338 LEU D CD2 
15424 N N   . GLU D 339 ? 0.2852 0.3402 0.6059 -0.0599 -0.0409 0.0358  339 GLU D N   
15425 C CA  . GLU D 339 ? 0.2864 0.3273 0.5981 -0.0628 -0.0467 0.0318  339 GLU D CA  
15426 C C   . GLU D 339 ? 0.2826 0.3083 0.5824 -0.0595 -0.0446 0.0275  339 GLU D C   
15427 O O   . GLU D 339 ? 0.2814 0.3075 0.5786 -0.0526 -0.0403 0.0250  339 GLU D O   
15428 C CB  . GLU D 339 ? 0.3158 0.3576 0.6267 -0.0592 -0.0491 0.0286  339 GLU D CB  
15429 C CG  . GLU D 339 ? 0.3258 0.3828 0.6486 -0.0614 -0.0519 0.0327  339 GLU D CG  
15430 C CD  . GLU D 339 ? 0.3500 0.4066 0.6707 -0.0574 -0.0544 0.0297  339 GLU D CD  
15431 O OE1 . GLU D 339 ? 0.3696 0.4304 0.6914 -0.0499 -0.0502 0.0283  339 GLU D OE1 
15432 O OE2 . GLU D 339 ? 0.3602 0.4103 0.6765 -0.0621 -0.0608 0.0284  339 GLU D OE2 
15433 N N   . LEU D 340 ? 0.2795 0.2921 0.5722 -0.0646 -0.0478 0.0269  340 LEU D N   
15434 C CA  . LEU D 340 ? 0.2774 0.2756 0.5595 -0.0618 -0.0462 0.0236  340 LEU D CA  
15435 C C   . LEU D 340 ? 0.2829 0.2653 0.5550 -0.0638 -0.0509 0.0195  340 LEU D C   
15436 O O   . LEU D 340 ? 0.2726 0.2533 0.5451 -0.0699 -0.0561 0.0202  340 LEU D O   
15437 C CB  . LEU D 340 ? 0.2923 0.2886 0.5748 -0.0652 -0.0444 0.0276  340 LEU D CB  
15438 C CG  . LEU D 340 ? 0.2789 0.2897 0.5698 -0.0636 -0.0391 0.0320  340 LEU D CG  
15439 C CD1 . LEU D 340 ? 0.2795 0.2857 0.5688 -0.0680 -0.0382 0.0360  340 LEU D CD1 
15440 C CD2 . LEU D 340 ? 0.2676 0.2819 0.5567 -0.0552 -0.0342 0.0294  340 LEU D CD2 
15441 N N   . TYR D 341 ? 0.3107 0.2820 0.5737 -0.0585 -0.0491 0.0153  341 TYR D N   
15442 C CA  . TYR D 341 ? 0.3314 0.2860 0.5834 -0.0592 -0.0521 0.0114  341 TYR D CA  
15443 C C   . TYR D 341 ? 0.3560 0.2996 0.6017 -0.0568 -0.0495 0.0110  341 TYR D C   
15444 O O   . TYR D 341 ? 0.3458 0.2908 0.5905 -0.0503 -0.0455 0.0098  341 TYR D O   
15445 C CB  . TYR D 341 ? 0.3310 0.2831 0.5781 -0.0544 -0.0523 0.0066  341 TYR D CB  
15446 C CG  . TYR D 341 ? 0.3677 0.3035 0.6034 -0.0560 -0.0558 0.0027  341 TYR D CG  
15447 C CD1 . TYR D 341 ? 0.3762 0.3094 0.6097 -0.0617 -0.0612 0.0021  341 TYR D CD1 
15448 C CD2 . TYR D 341 ? 0.3935 0.3159 0.6201 -0.0519 -0.0536 -0.0002 341 TYR D CD2 
15449 C CE1 . TYR D 341 ? 0.3884 0.3050 0.6095 -0.0634 -0.0643 -0.0018 341 TYR D CE1 
15450 C CE2 . TYR D 341 ? 0.4055 0.3117 0.6206 -0.0529 -0.0561 -0.0039 341 TYR D CE2 
15451 C CZ  . TYR D 341 ? 0.4051 0.3078 0.6167 -0.0586 -0.0613 -0.0050 341 TYR D CZ  
15452 O OH  . TYR D 341 ? 0.4116 0.2968 0.6099 -0.0593 -0.0634 -0.0090 341 TYR D OH  
15453 N N   . ASN D 342 ? 0.3926 0.3250 0.6339 -0.0622 -0.0521 0.0124  342 ASN D N   
15454 C CA  . ASN D 342 ? 0.3920 0.3149 0.6287 -0.0609 -0.0500 0.0137  342 ASN D CA  
15455 C C   . ASN D 342 ? 0.4347 0.3379 0.6593 -0.0597 -0.0517 0.0098  342 ASN D C   
15456 O O   . ASN D 342 ? 0.4978 0.3918 0.7171 -0.0647 -0.0560 0.0081  342 ASN D O   
15457 C CB  . ASN D 342 ? 0.3999 0.3244 0.6409 -0.0683 -0.0513 0.0192  342 ASN D CB  
15458 C CG  . ASN D 342 ? 0.3743 0.3179 0.6269 -0.0690 -0.0485 0.0237  342 ASN D CG  
15459 O OD1 . ASN D 342 ? 0.4059 0.3579 0.6658 -0.0756 -0.0505 0.0276  342 ASN D OD1 
15460 N ND2 . ASN D 342 ? 0.3380 0.2883 0.5921 -0.0623 -0.0438 0.0235  342 ASN D ND2 
15461 N N   . ASP D 343 ? 0.4468 0.3428 0.6664 -0.0531 -0.0485 0.0085  343 ASP D N   
15462 C CA  . ASP D 343 ? 0.4728 0.3494 0.6811 -0.0516 -0.0494 0.0056  343 ASP D CA  
15463 C C   . ASP D 343 ? 0.4637 0.3294 0.6691 -0.0573 -0.0514 0.0091  343 ASP D C   
15464 O O   . ASP D 343 ? 0.4065 0.2813 0.6191 -0.0621 -0.0515 0.0139  343 ASP D O   
15465 C CB  . ASP D 343 ? 0.4747 0.3481 0.6795 -0.0423 -0.0455 0.0031  343 ASP D CB  
15466 C CG  . ASP D 343 ? 0.4780 0.3508 0.6839 -0.0384 -0.0425 0.0064  343 ASP D CG  
15467 O OD1 . ASP D 343 ? 0.4799 0.3540 0.6887 -0.0427 -0.0431 0.0108  343 ASP D OD1 
15468 O OD2 . ASP D 343 ? 0.5116 0.3834 0.7158 -0.0309 -0.0397 0.0049  343 ASP D OD2 
15469 N N   . LYS D 344 ? 0.5269 0.3729 0.7213 -0.0563 -0.0523 0.0067  344 LYS D N   
15470 C CA  . LYS D 344 ? 0.5668 0.3977 0.7555 -0.0627 -0.0553 0.0090  344 LYS D CA  
15471 C C   . LYS D 344 ? 0.5146 0.3470 0.7068 -0.0619 -0.0528 0.0145  344 LYS D C   
15472 O O   . LYS D 344 ? 0.4959 0.3188 0.6856 -0.0683 -0.0551 0.0178  344 LYS D O   
15473 C CB  . LYS D 344 ? 0.7106 0.5180 0.8850 -0.0605 -0.0563 0.0046  344 LYS D CB  
15474 C CG  . LYS D 344 ? 0.8219 0.6230 0.9923 -0.0497 -0.0515 0.0033  344 LYS D CG  
15475 C CD  . LYS D 344 ? 0.9152 0.6967 1.0723 -0.0445 -0.0509 -0.0022 344 LYS D CD  
15476 C CE  . LYS D 344 ? 0.9686 0.7570 1.1270 -0.0341 -0.0463 -0.0051 344 LYS D CE  
15477 N NZ  . LYS D 344 ? 0.9561 0.7593 1.1243 -0.0285 -0.0426 -0.0015 344 LYS D NZ  
15478 N N   . ASP D 345 ? 0.4431 0.2873 0.6409 -0.0548 -0.0486 0.0156  345 ASP D N   
15479 C CA  . ASP D 345 ? 0.4205 0.2661 0.6206 -0.0538 -0.0465 0.0208  345 ASP D CA  
15480 C C   . ASP D 345 ? 0.3992 0.2609 0.6089 -0.0596 -0.0461 0.0260  345 ASP D C   
15481 O O   . ASP D 345 ? 0.4080 0.2676 0.6180 -0.0621 -0.0456 0.0311  345 ASP D O   
15482 C CB  . ASP D 345 ? 0.4281 0.2779 0.6287 -0.0441 -0.0427 0.0202  345 ASP D CB  
15483 C CG  . ASP D 345 ? 0.4279 0.2610 0.6194 -0.0376 -0.0420 0.0170  345 ASP D CG  
15484 O OD1 . ASP D 345 ? 0.4557 0.2713 0.6390 -0.0405 -0.0443 0.0157  345 ASP D OD1 
15485 O OD2 . ASP D 345 ? 0.4146 0.2529 0.6077 -0.0297 -0.0392 0.0160  345 ASP D OD2 
15486 N N   . VAL D 346 ? 0.3698 0.2473 0.5872 -0.0615 -0.0463 0.0251  346 VAL D N   
15487 C CA  . VAL D 346 ? 0.3577 0.2515 0.5847 -0.0660 -0.0451 0.0299  346 VAL D CA  
15488 C C   . VAL D 346 ? 0.3764 0.2661 0.6045 -0.0761 -0.0485 0.0339  346 VAL D C   
15489 O O   . VAL D 346 ? 0.3707 0.2566 0.5980 -0.0813 -0.0525 0.0319  346 VAL D O   
15490 C CB  . VAL D 346 ? 0.3501 0.2609 0.5848 -0.0647 -0.0443 0.0279  346 VAL D CB  
15491 C CG1 . VAL D 346 ? 0.3376 0.2651 0.5824 -0.0690 -0.0427 0.0330  346 VAL D CG1 
15492 C CG2 . VAL D 346 ? 0.3582 0.2737 0.5922 -0.0555 -0.0410 0.0244  346 VAL D CG2 
15493 N N   . LYS D 347 ? 0.4043 0.2960 0.6348 -0.0794 -0.0469 0.0399  347 LYS D N   
15494 C CA  . LYS D 347 ? 0.4506 0.3400 0.6834 -0.0898 -0.0499 0.0447  347 LYS D CA  
15495 C C   . LYS D 347 ? 0.4399 0.3499 0.6845 -0.0939 -0.0475 0.0503  347 LYS D C   
15496 O O   . LYS D 347 ? 0.4883 0.4006 0.7374 -0.1030 -0.0500 0.0545  347 LYS D O   
15497 C CB  . LYS D 347 ? 0.4651 0.3378 0.6904 -0.0922 -0.0504 0.0484  347 LYS D CB  
15498 C CG  . LYS D 347 ? 0.5171 0.3678 0.7303 -0.0879 -0.0523 0.0434  347 LYS D CG  
15499 C CD  . LYS D 347 ? 0.5608 0.4019 0.7692 -0.0911 -0.0569 0.0380  347 LYS D CD  
15500 C CE  . LYS D 347 ? 0.6173 0.4355 0.8124 -0.0860 -0.0577 0.0332  347 LYS D CE  
15501 N NZ  . LYS D 347 ? 0.6171 0.4277 0.8068 -0.0880 -0.0615 0.0273  347 LYS D NZ  
15502 N N   . LYS D 348 ? 0.4192 0.3437 0.6684 -0.0873 -0.0427 0.0504  348 LYS D N   
15503 C CA  . LYS D 348 ? 0.4007 0.3449 0.6606 -0.0898 -0.0395 0.0552  348 LYS D CA  
15504 C C   . LYS D 348 ? 0.3737 0.3314 0.6370 -0.0815 -0.0355 0.0520  348 LYS D C   
15505 O O   . LYS D 348 ? 0.3633 0.3154 0.6204 -0.0741 -0.0342 0.0481  348 LYS D O   
15506 C CB  . LYS D 348 ? 0.4035 0.3473 0.6626 -0.0925 -0.0366 0.0619  348 LYS D CB  
15507 C CG  . LYS D 348 ? 0.4049 0.3690 0.6744 -0.0950 -0.0324 0.0674  348 LYS D CG  
15508 C CD  . LYS D 348 ? 0.4047 0.3688 0.6733 -0.0987 -0.0294 0.0747  348 LYS D CD  
15509 C CE  . LYS D 348 ? 0.4027 0.3572 0.6614 -0.0921 -0.0272 0.0742  348 LYS D CE  
15510 N NZ  . LYS D 348 ? 0.4128 0.3679 0.6702 -0.0957 -0.0243 0.0816  348 LYS D NZ  
15511 N N   . VAL D 349 ? 0.3534 0.3288 0.6269 -0.0830 -0.0335 0.0541  349 VAL D N   
15512 C CA  . VAL D 349 ? 0.3388 0.3274 0.6159 -0.0758 -0.0294 0.0518  349 VAL D CA  
15513 C C   . VAL D 349 ? 0.3260 0.3312 0.6114 -0.0772 -0.0246 0.0575  349 VAL D C   
15514 O O   . VAL D 349 ? 0.3334 0.3473 0.6273 -0.0837 -0.0254 0.0618  349 VAL D O   
15515 C CB  . VAL D 349 ? 0.3541 0.3473 0.6351 -0.0743 -0.0320 0.0473  349 VAL D CB  
15516 C CG1 . VAL D 349 ? 0.3458 0.3527 0.6311 -0.0674 -0.0275 0.0456  349 VAL D CG1 
15517 C CG2 . VAL D 349 ? 0.3669 0.3441 0.6388 -0.0719 -0.0358 0.0414  349 VAL D CG2 
15518 N N   . VAL D 350 ? 0.3149 0.3245 0.5974 -0.0711 -0.0195 0.0574  350 VAL D N   
15519 C CA  . VAL D 350 ? 0.3021 0.3271 0.5908 -0.0710 -0.0139 0.0620  350 VAL D CA  
15520 C C   . VAL D 350 ? 0.3092 0.3433 0.5991 -0.0631 -0.0103 0.0579  350 VAL D C   
15521 O O   . VAL D 350 ? 0.3177 0.3446 0.6008 -0.0575 -0.0112 0.0525  350 VAL D O   
15522 C CB  . VAL D 350 ? 0.3196 0.3399 0.6015 -0.0714 -0.0109 0.0661  350 VAL D CB  
15523 C CG1 . VAL D 350 ? 0.3291 0.3646 0.6160 -0.0712 -0.0044 0.0711  350 VAL D CG1 
15524 C CG2 . VAL D 350 ? 0.3424 0.3506 0.6216 -0.0788 -0.0147 0.0700  350 VAL D CG2 
15525 N N   . VAL D 351 ? 0.2907 0.3407 0.5898 -0.0628 -0.0066 0.0605  351 VAL D N   
15526 C CA  . VAL D 351 ? 0.2775 0.3358 0.5766 -0.0552 -0.0017 0.0577  351 VAL D CA  
15527 C C   . VAL D 351 ? 0.2771 0.3440 0.5760 -0.0543 0.0051  0.0624  351 VAL D C   
15528 O O   . VAL D 351 ? 0.2935 0.3703 0.6006 -0.0592 0.0071  0.0685  351 VAL D O   
15529 C CB  . VAL D 351 ? 0.2814 0.3505 0.5902 -0.0535 -0.0022 0.0562  351 VAL D CB  
15530 C CG1 . VAL D 351 ? 0.2663 0.3433 0.5747 -0.0455 0.0037  0.0540  351 VAL D CG1 
15531 C CG2 . VAL D 351 ? 0.2930 0.3532 0.6002 -0.0536 -0.0086 0.0511  351 VAL D CG2 
15532 N N   . LYS D 352 ? 0.2852 0.3492 0.5750 -0.0481 0.0087  0.0596  352 LYS D N   
15533 C CA  . LYS D 352 ? 0.3001 0.3722 0.5879 -0.0457 0.0159  0.0629  352 LYS D CA  
15534 C C   . LYS D 352 ? 0.3053 0.3842 0.5928 -0.0380 0.0204  0.0589  352 LYS D C   
15535 O O   . LYS D 352 ? 0.2986 0.3721 0.5830 -0.0338 0.0179  0.0529  352 LYS D O   
15536 C CB  . LYS D 352 ? 0.3257 0.3877 0.6009 -0.0452 0.0165  0.0635  352 LYS D CB  
15537 C CG  . LYS D 352 ? 0.3508 0.4070 0.6252 -0.0523 0.0141  0.0690  352 LYS D CG  
15538 C CD  . LYS D 352 ? 0.3857 0.4283 0.6474 -0.0511 0.0121  0.0683  352 LYS D CD  
15539 C CE  . LYS D 352 ? 0.4288 0.4645 0.6913 -0.0584 0.0090  0.0737  352 LYS D CE  
15540 N NZ  . LYS D 352 ? 0.4414 0.4624 0.6936 -0.0578 0.0056  0.0734  352 LYS D NZ  
15541 N N   . PHE D 353 ? 0.2794 0.3698 0.5696 -0.0362 0.0275  0.0626  353 PHE D N   
15542 C CA  . PHE D 353 ? 0.2705 0.3647 0.5561 -0.0285 0.0335  0.0595  353 PHE D CA  
15543 C C   . PHE D 353 ? 0.2678 0.3634 0.5449 -0.0276 0.0399  0.0627  353 PHE D C   
15544 O O   . PHE D 353 ? 0.2823 0.3869 0.5652 -0.0313 0.0436  0.0693  353 PHE D O   
15545 C CB  . PHE D 353 ? 0.2577 0.3663 0.5565 -0.0262 0.0366  0.0609  353 PHE D CB  
15546 C CG  . PHE D 353 ? 0.2491 0.3604 0.5433 -0.0175 0.0428  0.0572  353 PHE D CG  
15547 C CD1 . PHE D 353 ? 0.2369 0.3368 0.5208 -0.0127 0.0407  0.0500  353 PHE D CD1 
15548 C CD2 . PHE D 353 ? 0.2593 0.3840 0.5588 -0.0142 0.0510  0.0610  353 PHE D CD2 
15549 C CE1 . PHE D 353 ? 0.2341 0.3343 0.5121 -0.0051 0.0462  0.0464  353 PHE D CE1 
15550 C CE2 . PHE D 353 ? 0.2540 0.3788 0.5474 -0.0057 0.0570  0.0572  353 PHE D CE2 
15551 C CZ  . PHE D 353 ? 0.2405 0.3522 0.5227 -0.0014 0.0543  0.0497  353 PHE D CZ  
15552 N N   . ARG D 354 ? 0.2676 0.3541 0.5306 -0.0230 0.0410  0.0583  354 ARG D N   
15553 C CA  . ARG D 354 ? 0.2883 0.3740 0.5402 -0.0218 0.0465  0.0606  354 ARG D CA  
15554 C C   . ARG D 354 ? 0.2977 0.3814 0.5491 -0.0288 0.0448  0.0669  354 ARG D C   
15555 O O   . ARG D 354 ? 0.3038 0.3937 0.5538 -0.0301 0.0506  0.0724  354 ARG D O   
15556 C CB  . ARG D 354 ? 0.3044 0.4028 0.5596 -0.0174 0.0557  0.0626  354 ARG D CB  
15557 C CG  . ARG D 354 ? 0.3059 0.4029 0.5578 -0.0096 0.0578  0.0559  354 ARG D CG  
15558 C CD  . ARG D 354 ? 0.3007 0.4083 0.5541 -0.0039 0.0674  0.0573  354 ARG D CD  
15559 N NE  . ARG D 354 ? 0.3024 0.4077 0.5538 0.0035  0.0689  0.0510  354 ARG D NE  
15560 C CZ  . ARG D 354 ? 0.2870 0.4021 0.5434 0.0097  0.0765  0.0517  354 ARG D CZ  
15561 N NH1 . ARG D 354 ? 0.2955 0.4225 0.5560 0.0100  0.0843  0.0577  354 ARG D NH1 
15562 N NH2 . ARG D 354 ? 0.2702 0.3831 0.5277 0.0157  0.0765  0.0466  354 ARG D NH2 
15563 N N   . ASP D 355 ? 0.2975 0.3719 0.5497 -0.0329 0.0371  0.0663  355 ASP D N   
15564 C CA  . ASP D 355 ? 0.3155 0.3840 0.5645 -0.0388 0.0347  0.0715  355 ASP D CA  
15565 C C   . ASP D 355 ? 0.3255 0.4040 0.5863 -0.0451 0.0368  0.0788  355 ASP D C   
15566 O O   . ASP D 355 ? 0.3113 0.3878 0.5696 -0.0500 0.0373  0.0846  355 ASP D O   
15567 C CB  . ASP D 355 ? 0.3143 0.3782 0.5488 -0.0369 0.0380  0.0728  355 ASP D CB  
15568 C CG  . ASP D 355 ? 0.3236 0.3808 0.5467 -0.0306 0.0374  0.0659  355 ASP D CG  
15569 O OD1 . ASP D 355 ? 0.3069 0.3542 0.5266 -0.0304 0.0309  0.0623  355 ASP D OD1 
15570 O OD2 . ASP D 355 ? 0.3329 0.3948 0.5505 -0.0260 0.0434  0.0642  355 ASP D OD2 
15571 N N   . LYS D 356 ? 0.3320 0.4218 0.6058 -0.0450 0.0380  0.0788  356 LYS D N   
15572 C CA  . LYS D 356 ? 0.3230 0.4226 0.6100 -0.0520 0.0381  0.0855  356 LYS D CA  
15573 C C   . LYS D 356 ? 0.2980 0.3954 0.5944 -0.0553 0.0307  0.0832  356 LYS D C   
15574 O O   . LYS D 356 ? 0.2696 0.3681 0.5685 -0.0506 0.0292  0.0776  356 LYS D O   
15575 C CB  . LYS D 356 ? 0.3292 0.4472 0.6258 -0.0498 0.0461  0.0893  356 LYS D CB  
15576 C CG  . LYS D 356 ? 0.3383 0.4677 0.6500 -0.0580 0.0456  0.0970  356 LYS D CG  
15577 C CD  . LYS D 356 ? 0.3735 0.5190 0.6905 -0.0581 0.0548  0.1041  356 LYS D CD  
15578 C CE  . LYS D 356 ? 0.3918 0.5501 0.7142 -0.0499 0.0613  0.1019  356 LYS D CE  
15579 N NZ  . LYS D 356 ? 0.4305 0.6066 0.7625 -0.0517 0.0693  0.1102  356 LYS D NZ  
15580 N N   . VAL D 357 ? 0.3033 0.3973 0.6041 -0.0638 0.0263  0.0877  357 VAL D N   
15581 C CA  . VAL D 357 ? 0.3063 0.3974 0.6150 -0.0687 0.0190  0.0865  357 VAL D CA  
15582 C C   . VAL D 357 ? 0.2773 0.3862 0.6014 -0.0694 0.0208  0.0887  357 VAL D C   
15583 O O   . VAL D 357 ? 0.2638 0.3856 0.5964 -0.0733 0.0249  0.0958  357 VAL D O   
15584 C CB  . VAL D 357 ? 0.3044 0.3864 0.6131 -0.0781 0.0139  0.0911  357 VAL D CB  
15585 C CG1 . VAL D 357 ? 0.2870 0.3655 0.6026 -0.0830 0.0064  0.0891  357 VAL D CG1 
15586 C CG2 . VAL D 357 ? 0.3072 0.3715 0.6015 -0.0774 0.0118  0.0897  357 VAL D CG2 
15587 N N   . ILE D 358 ? 0.2752 0.3844 0.6027 -0.0656 0.0175  0.0832  358 ILE D N   
15588 C CA  . ILE D 358 ? 0.2817 0.4063 0.6240 -0.0663 0.0173  0.0850  358 ILE D CA  
15589 C C   . ILE D 358 ? 0.2920 0.4112 0.6390 -0.0723 0.0084  0.0836  358 ILE D C   
15590 O O   . ILE D 358 ? 0.3186 0.4502 0.6783 -0.0746 0.0067  0.0860  358 ILE D O   
15591 C CB  . ILE D 358 ? 0.2772 0.4091 0.6205 -0.0565 0.0218  0.0807  358 ILE D CB  
15592 C CG1 . ILE D 358 ? 0.2911 0.4093 0.6253 -0.0516 0.0173  0.0723  358 ILE D CG1 
15593 C CG2 . ILE D 358 ? 0.2784 0.4166 0.6171 -0.0509 0.0312  0.0825  358 ILE D CG2 
15594 C CD1 . ILE D 358 ? 0.3005 0.4253 0.6373 -0.0432 0.0202  0.0683  358 ILE D CD1 
15595 N N   . TYR D 359 ? 0.3099 0.4109 0.6467 -0.0746 0.0026  0.0798  359 TYR D N   
15596 C CA  . TYR D 359 ? 0.3046 0.3984 0.6437 -0.0808 -0.0056 0.0785  359 TYR D CA  
15597 C C   . TYR D 359 ? 0.3296 0.4033 0.6567 -0.0844 -0.0098 0.0769  359 TYR D C   
15598 O O   . TYR D 359 ? 0.3196 0.3831 0.6356 -0.0791 -0.0080 0.0736  359 TYR D O   
15599 C CB  . TYR D 359 ? 0.2998 0.3936 0.6398 -0.0755 -0.0085 0.0723  359 TYR D CB  
15600 C CG  . TYR D 359 ? 0.3169 0.4014 0.6567 -0.0813 -0.0171 0.0700  359 TYR D CG  
15601 C CD1 . TYR D 359 ? 0.3462 0.4411 0.6978 -0.0879 -0.0211 0.0739  359 TYR D CD1 
15602 C CD2 . TYR D 359 ? 0.3208 0.3866 0.6485 -0.0802 -0.0213 0.0643  359 TYR D CD2 
15603 C CE1 . TYR D 359 ? 0.3937 0.4789 0.7433 -0.0937 -0.0293 0.0717  359 TYR D CE1 
15604 C CE2 . TYR D 359 ? 0.3356 0.3918 0.6614 -0.0851 -0.0286 0.0619  359 TYR D CE2 
15605 C CZ  . TYR D 359 ? 0.3789 0.4441 0.7149 -0.0922 -0.0328 0.0654  359 TYR D CZ  
15606 O OH  . TYR D 359 ? 0.4173 0.4721 0.7500 -0.0977 -0.0404 0.0631  359 TYR D OH  
15607 N N   . SER D 360 ? 0.3581 0.4265 0.6878 -0.0935 -0.0157 0.0796  360 SER D N   
15608 C CA  . SER D 360 ? 0.3798 0.4286 0.6992 -0.0979 -0.0200 0.0789  360 SER D CA  
15609 C C   . SER D 360 ? 0.4006 0.4424 0.7220 -0.1055 -0.0280 0.0779  360 SER D C   
15610 O O   . SER D 360 ? 0.3898 0.4433 0.7224 -0.1124 -0.0300 0.0825  360 SER D O   
15611 C CB  . SER D 360 ? 0.3815 0.4303 0.7002 -0.1030 -0.0170 0.0858  360 SER D CB  
15612 O OG  . SER D 360 ? 0.3945 0.4236 0.7002 -0.1023 -0.0190 0.0838  360 SER D OG  
15613 N N   . LYS D 361 ? 0.4001 0.4227 0.7103 -0.1045 -0.0326 0.0724  361 LYS D N   
15614 C CA  . LYS D 361 ? 0.4082 0.4203 0.7169 -0.1120 -0.0401 0.0711  361 LYS D CA  
15615 C C   . LYS D 361 ? 0.4039 0.3919 0.6981 -0.1114 -0.0430 0.0674  361 LYS D C   
15616 O O   . LYS D 361 ? 0.3409 0.3213 0.6270 -0.1030 -0.0411 0.0623  361 LYS D O   
15617 C CB  . LYS D 361 ? 0.4476 0.4650 0.7601 -0.1098 -0.0436 0.0665  361 LYS D CB  
15618 C CG  . LYS D 361 ? 0.5343 0.5435 0.8462 -0.1190 -0.0519 0.0661  361 LYS D CG  
15619 C CD  . LYS D 361 ? 0.6268 0.6483 0.9472 -0.1198 -0.0555 0.0649  361 LYS D CD  
15620 C CE  . LYS D 361 ? 0.6699 0.6824 0.9879 -0.1288 -0.0644 0.0638  361 LYS D CE  
15621 N NZ  . LYS D 361 ? 0.7177 0.7476 1.0472 -0.1296 -0.0670 0.0649  361 LYS D NZ  
15622 N N   . ASN D 362 ? 0.4197 0.3959 0.7110 -0.1208 -0.0477 0.0702  362 ASN D N   
15623 C CA  . ASN D 362 ? 0.4240 0.3758 0.7018 -0.1213 -0.0519 0.0661  362 ASN D CA  
15624 C C   . ASN D 362 ? 0.4160 0.3619 0.6904 -0.1205 -0.0569 0.0594  362 ASN D C   
15625 O O   . ASN D 362 ? 0.4019 0.3566 0.6836 -0.1263 -0.0608 0.0604  362 ASN D O   
15626 C CB  . ASN D 362 ? 0.4649 0.4047 0.7398 -0.1318 -0.0554 0.0711  362 ASN D CB  
15627 C CG  . ASN D 362 ? 0.4897 0.4357 0.7677 -0.1329 -0.0502 0.0783  362 ASN D CG  
15628 O OD1 . ASN D 362 ? 0.5524 0.5063 0.8382 -0.1420 -0.0507 0.0851  362 ASN D OD1 
15629 N ND2 . ASN D 362 ? 0.5254 0.4694 0.7979 -0.1240 -0.0452 0.0771  362 ASN D ND2 
15630 N N   . ILE D 363 ? 0.4221 0.3542 0.6857 -0.1128 -0.0567 0.0530  363 ILE D N   
15631 C CA  . ILE D 363 ? 0.4272 0.3514 0.6853 -0.1116 -0.0610 0.0465  363 ILE D CA  
15632 C C   . ILE D 363 ? 0.4465 0.3481 0.6937 -0.1185 -0.0668 0.0451  363 ILE D C   
15633 O O   . ILE D 363 ? 0.4595 0.3440 0.6971 -0.1168 -0.0660 0.0447  363 ILE D O   
15634 C CB  . ILE D 363 ? 0.4067 0.3284 0.6592 -0.1000 -0.0574 0.0407  363 ILE D CB  
15635 C CG1 . ILE D 363 ? 0.4016 0.3431 0.6631 -0.0935 -0.0517 0.0420  363 ILE D CG1 
15636 C CG2 . ILE D 363 ? 0.4142 0.3280 0.6605 -0.0984 -0.0612 0.0342  363 ILE D CG2 
15637 C CD1 . ILE D 363 ? 0.4215 0.3830 0.6957 -0.0967 -0.0521 0.0446  363 ILE D CD1 
15638 N N   . THR D 364 ? 0.4993 0.4008 0.7480 -0.1264 -0.0729 0.0446  364 THR D N   
15639 C CA  . THR D 364 ? 0.5304 0.4111 0.7689 -0.1350 -0.0794 0.0434  364 THR D CA  
15640 C C   . THR D 364 ? 0.5299 0.3954 0.7559 -0.1307 -0.0822 0.0352  364 THR D C   
15641 O O   . THR D 364 ? 0.5852 0.4288 0.7985 -0.1349 -0.0865 0.0324  364 THR D O   
15642 C CB  . THR D 364 ? 0.5114 0.4025 0.7594 -0.1475 -0.0850 0.0484  364 THR D CB  
15643 O OG1 . THR D 364 ? 0.5368 0.4439 0.7921 -0.1451 -0.0862 0.0463  364 THR D OG1 
15644 C CG2 . THR D 364 ? 0.5118 0.4199 0.7732 -0.1522 -0.0819 0.0571  364 THR D CG2 
15645 N N   . SER D 365 ? 0.5004 0.3773 0.7295 -0.1224 -0.0795 0.0316  365 SER D N   
15646 C CA  . SER D 365 ? 0.5024 0.3695 0.7217 -0.1188 -0.0820 0.0245  365 SER D CA  
15647 C C   . SER D 365 ? 0.4666 0.3421 0.6874 -0.1066 -0.0760 0.0211  365 SER D C   
15648 O O   . SER D 365 ? 0.4200 0.3151 0.6525 -0.1032 -0.0723 0.0239  365 SER D O   
15649 C CB  . SER D 365 ? 0.5220 0.3976 0.7463 -0.1270 -0.0884 0.0252  365 SER D CB  
15650 O OG  . SER D 365 ? 0.5637 0.4311 0.7784 -0.1240 -0.0910 0.0187  365 SER D OG  
15651 N N   . GLU D 366 ? 0.4664 0.3270 0.6752 -0.0996 -0.0747 0.0152  366 GLU D N   
15652 C CA  . GLU D 366 ? 0.4498 0.3186 0.6603 -0.0890 -0.0695 0.0122  366 GLU D CA  
15653 C C   . GLU D 366 ? 0.3965 0.2771 0.6110 -0.0884 -0.0714 0.0099  366 GLU D C   
15654 O O   . GLU D 366 ? 0.3827 0.2621 0.5960 -0.0954 -0.0770 0.0096  366 GLU D O   
15655 C CB  . GLU D 366 ? 0.4893 0.3392 0.6866 -0.0819 -0.0674 0.0072  366 GLU D CB  
15656 C CG  . GLU D 366 ? 0.5418 0.3772 0.7269 -0.0829 -0.0711 0.0014  366 GLU D CG  
15657 C CD  . GLU D 366 ? 0.6135 0.4330 0.7868 -0.0740 -0.0673 -0.0033 366 GLU D CD  
15658 O OE1 . GLU D 366 ? 0.6253 0.4533 0.8021 -0.0653 -0.0625 -0.0045 366 GLU D OE1 
15659 O OE2 . GLU D 366 ? 0.7180 0.5163 0.8788 -0.0759 -0.0693 -0.0056 366 GLU D OE2 
15660 N N   . GLY D 367 ? 0.3720 0.2631 0.5904 -0.0801 -0.0670 0.0083  367 GLY D N   
15661 C CA  . GLY D 367 ? 0.3719 0.2735 0.5936 -0.0787 -0.0683 0.0063  367 GLY D CA  
15662 C C   . GLY D 367 ? 0.3599 0.2835 0.5968 -0.0807 -0.0679 0.0112  367 GLY D C   
15663 O O   . GLY D 367 ? 0.3604 0.2935 0.6049 -0.0789 -0.0638 0.0147  367 GLY D O   
15664 N N   . TYR D 368 ? 0.3649 0.2966 0.6057 -0.0841 -0.0720 0.0113  368 TYR D N   
15665 C CA  . TYR D 368 ? 0.3608 0.3138 0.6157 -0.0836 -0.0708 0.0153  368 TYR D CA  
15666 C C   . TYR D 368 ? 0.3883 0.3502 0.6531 -0.0913 -0.0724 0.0215  368 TYR D C   
15667 O O   . TYR D 368 ? 0.3997 0.3528 0.6608 -0.0996 -0.0777 0.0225  368 TYR D O   
15668 C CB  . TYR D 368 ? 0.3505 0.3090 0.6065 -0.0849 -0.0754 0.0140  368 TYR D CB  
15669 C CG  . TYR D 368 ? 0.3377 0.3180 0.6086 -0.0839 -0.0745 0.0184  368 TYR D CG  
15670 C CD1 . TYR D 368 ? 0.3352 0.3248 0.6102 -0.0754 -0.0695 0.0174  368 TYR D CD1 
15671 C CD2 . TYR D 368 ? 0.3481 0.3396 0.6291 -0.0915 -0.0787 0.0236  368 TYR D CD2 
15672 C CE1 . TYR D 368 ? 0.3199 0.3280 0.6078 -0.0739 -0.0684 0.0212  368 TYR D CE1 
15673 C CE2 . TYR D 368 ? 0.3269 0.3389 0.6222 -0.0899 -0.0776 0.0279  368 TYR D CE2 
15674 C CZ  . TYR D 368 ? 0.3088 0.3286 0.6073 -0.0808 -0.0722 0.0266  368 TYR D CZ  
15675 O OH  . TYR D 368 ? 0.2781 0.3170 0.5903 -0.0790 -0.0710 0.0310  368 TYR D OH  
15676 N N   . MET D 369 ? 0.3872 0.3659 0.6639 -0.0886 -0.0677 0.0257  369 MET D N   
15677 C CA  . MET D 369 ? 0.4416 0.4339 0.7304 -0.0955 -0.0689 0.0323  369 MET D CA  
15678 C C   . MET D 369 ? 0.4162 0.4301 0.7185 -0.0908 -0.0648 0.0355  369 MET D C   
15679 O O   . MET D 369 ? 0.3884 0.4052 0.6902 -0.0825 -0.0589 0.0337  369 MET D O   
15680 C CB  . MET D 369 ? 0.5368 0.5237 0.8248 -0.0992 -0.0667 0.0357  369 MET D CB  
15681 C CG  . MET D 369 ? 0.6120 0.6025 0.9006 -0.0914 -0.0591 0.0361  369 MET D CG  
15682 S SD  . MET D 369 ? 0.7413 0.7454 1.0410 -0.0956 -0.0551 0.0442  369 MET D SD  
15683 C CE  . MET D 369 ? 0.5588 0.5850 0.8749 -0.1006 -0.0576 0.0493  369 MET D CE  
15684 N N   . ALA D 370 ? 0.4096 0.4384 0.7239 -0.0965 -0.0679 0.0406  370 ALA D N   
15685 C CA  . ALA D 370 ? 0.3952 0.4452 0.7234 -0.0923 -0.0643 0.0444  370 ALA D CA  
15686 C C   . ALA D 370 ? 0.3881 0.4522 0.7286 -0.0974 -0.0621 0.0518  370 ALA D C   
15687 O O   . ALA D 370 ? 0.4405 0.5017 0.7822 -0.1069 -0.0667 0.0550  370 ALA D O   
15688 C CB  . ALA D 370 ? 0.3828 0.4400 0.7155 -0.0934 -0.0698 0.0444  370 ALA D CB  
15689 N N   . ASP D 371 ? 0.3563 0.4351 0.7056 -0.0912 -0.0550 0.0547  371 ASP D N   
15690 C CA  . ASP D 371 ? 0.3416 0.4351 0.7028 -0.0951 -0.0517 0.0620  371 ASP D CA  
15691 C C   . ASP D 371 ? 0.3110 0.4217 0.6815 -0.0864 -0.0443 0.0639  371 ASP D C   
15692 O O   . ASP D 371 ? 0.2869 0.4000 0.6573 -0.0796 -0.0440 0.0606  371 ASP D O   
15693 C CB  . ASP D 371 ? 0.3418 0.4230 0.6951 -0.0990 -0.0500 0.0627  371 ASP D CB  
15694 C CG  . ASP D 371 ? 0.3328 0.4231 0.6953 -0.1073 -0.0493 0.0705  371 ASP D CG  
15695 O OD1 . ASP D 371 ? 0.3264 0.4359 0.7037 -0.1102 -0.0494 0.0763  371 ASP D OD1 
15696 O OD2 . ASP D 371 ? 0.3810 0.4591 0.7358 -0.1106 -0.0485 0.0709  371 ASP D OD2 
15697 N N   . GLU D 372 ? 0.3462 0.4692 0.7250 -0.0868 -0.0384 0.0696  372 GLU D N   
15698 C CA  . GLU D 372 ? 0.3715 0.5098 0.7580 -0.0783 -0.0305 0.0714  372 GLU D CA  
15699 C C   . GLU D 372 ? 0.3492 0.4886 0.7335 -0.0766 -0.0227 0.0738  372 GLU D C   
15700 O O   . GLU D 372 ? 0.3490 0.4889 0.7354 -0.0841 -0.0232 0.0785  372 GLU D O   
15701 C CB  . GLU D 372 ? 0.3895 0.5508 0.7943 -0.0798 -0.0300 0.0784  372 GLU D CB  
15702 C CG  . GLU D 372 ? 0.4398 0.6052 0.8502 -0.0817 -0.0377 0.0780  372 GLU D CG  
15703 C CD  . GLU D 372 ? 0.5287 0.7190 0.9587 -0.0829 -0.0366 0.0861  372 GLU D CD  
15704 O OE1 . GLU D 372 ? 0.5240 0.7247 0.9635 -0.0902 -0.0360 0.0929  372 GLU D OE1 
15705 O OE2 . GLU D 372 ? 0.6552 0.8548 1.0913 -0.0760 -0.0360 0.0858  372 GLU D OE2 
15706 N N   . LEU D 373 ? 0.3810 0.5205 0.7606 -0.0668 -0.0158 0.0707  373 LEU D N   
15707 C CA  . LEU D 373 ? 0.3846 0.5286 0.7629 -0.0632 -0.0074 0.0731  373 LEU D CA  
15708 C C   . LEU D 373 ? 0.3174 0.4831 0.7103 -0.0597 -0.0019 0.0784  373 LEU D C   
15709 O O   . LEU D 373 ? 0.3337 0.5058 0.7320 -0.0546 -0.0026 0.0769  373 LEU D O   
15710 C CB  . LEU D 373 ? 0.4027 0.5365 0.7682 -0.0540 -0.0027 0.0668  373 LEU D CB  
15711 C CG  . LEU D 373 ? 0.4430 0.5564 0.7941 -0.0540 -0.0071 0.0603  373 LEU D CG  
15712 C CD1 . LEU D 373 ? 0.4716 0.5795 0.8135 -0.0447 -0.0026 0.0548  373 LEU D CD1 
15713 C CD2 . LEU D 373 ? 0.4564 0.5607 0.8016 -0.0604 -0.0081 0.0625  373 LEU D CD2 
15714 N N   . THR D 374 ? 0.2887 0.4638 0.6859 -0.0609 0.0045  0.0840  374 THR D N   
15715 C CA  . THR D 374 ? 0.2889 0.4823 0.6960 -0.0547 0.0128  0.0881  374 THR D CA  
15716 C C   . THR D 374 ? 0.2884 0.4749 0.6829 -0.0470 0.0211  0.0849  374 THR D C   
15717 O O   . THR D 374 ? 0.3296 0.5059 0.7141 -0.0502 0.0220  0.0847  374 THR D O   
15718 C CB  . THR D 374 ? 0.2930 0.5031 0.7144 -0.0626 0.0140  0.0976  374 THR D CB  
15719 O OG1 . THR D 374 ? 0.2904 0.5054 0.7220 -0.0696 0.0052  0.0996  374 THR D OG1 
15720 C CG2 . THR D 374 ? 0.2814 0.5119 0.7139 -0.0561 0.0238  0.1027  374 THR D CG2 
15721 N N   . ILE D 375 ? 0.2664 0.4581 0.6610 -0.0369 0.0268  0.0824  375 ILE D N   
15722 C CA  . ILE D 375 ? 0.2606 0.4471 0.6436 -0.0292 0.0349  0.0793  375 ILE D CA  
15723 C C   . ILE D 375 ? 0.2702 0.4750 0.6630 -0.0230 0.0444  0.0841  375 ILE D C   
15724 O O   . ILE D 375 ? 0.2474 0.4690 0.6566 -0.0230 0.0444  0.0890  375 ILE D O   
15725 C CB  . ILE D 375 ? 0.2652 0.4371 0.6363 -0.0222 0.0331  0.0706  375 ILE D CB  
15726 C CG1 . ILE D 375 ? 0.2569 0.4370 0.6376 -0.0168 0.0320  0.0698  375 ILE D CG1 
15727 C CG2 . ILE D 375 ? 0.2748 0.4286 0.6353 -0.0275 0.0249  0.0660  375 ILE D CG2 
15728 C CD1 . ILE D 375 ? 0.2531 0.4209 0.6228 -0.0087 0.0321  0.0620  375 ILE D CD1 
15729 N N   . ASP D 376 ? 0.2954 0.4969 0.6775 -0.0174 0.0526  0.0828  376 ASP D N   
15730 C CA  . ASP D 376 ? 0.3095 0.5267 0.6983 -0.0111 0.0630  0.0872  376 ASP D CA  
15731 C C   . ASP D 376 ? 0.2978 0.5059 0.6728 0.0000  0.0694  0.0806  376 ASP D C   
15732 O O   . ASP D 376 ? 0.3170 0.5233 0.6824 0.0031  0.0769  0.0808  376 ASP D O   
15733 C CB  . ASP D 376 ? 0.3328 0.5578 0.7235 -0.0168 0.0679  0.0942  376 ASP D CB  
15734 C CG  . ASP D 376 ? 0.3818 0.6289 0.7860 -0.0130 0.0775  0.1015  376 ASP D CG  
15735 O OD1 . ASP D 376 ? 0.4522 0.7114 0.8683 -0.0068 0.0794  0.1023  376 ASP D OD1 
15736 O OD2 . ASP D 376 ? 0.4271 0.6799 0.8303 -0.0159 0.0835  0.1068  376 ASP D OD2 
15737 N N   . PRO D 377 ? 0.2923 0.4940 0.6652 0.0060  0.0666  0.0748  377 PRO D N   
15738 C CA  . PRO D 377 ? 0.2900 0.4823 0.6499 0.0163  0.0724  0.0685  377 PRO D CA  
15739 C C   . PRO D 377 ? 0.2948 0.5003 0.6591 0.0245  0.0839  0.0720  377 PRO D C   
15740 O O   . PRO D 377 ? 0.2890 0.5126 0.6708 0.0261  0.0861  0.0778  377 PRO D O   
15741 C CB  . PRO D 377 ? 0.2920 0.4791 0.6545 0.0195  0.0663  0.0640  377 PRO D CB  
15742 C CG  . PRO D 377 ? 0.2859 0.4887 0.6681 0.0142  0.0614  0.0703  377 PRO D CG  
15743 C CD  . PRO D 377 ? 0.2930 0.4955 0.6754 0.0033  0.0578  0.0740  377 PRO D CD  
15744 N N   . VAL D 378 ? 0.3117 0.5082 0.6598 0.0295  0.0910  0.0686  378 VAL D N   
15745 C CA  . VAL D 378 ? 0.3184 0.5227 0.6659 0.0395  0.1025  0.0697  378 VAL D CA  
15746 C C   . VAL D 378 ? 0.3256 0.5201 0.6675 0.0487  0.1024  0.0628  378 VAL D C   
15747 O O   . VAL D 378 ? 0.3383 0.5137 0.6640 0.0492  0.0986  0.0554  378 VAL D O   
15748 C CB  . VAL D 378 ? 0.3337 0.5313 0.6642 0.0410  0.1102  0.0687  378 VAL D CB  
15749 C CG1 . VAL D 378 ? 0.3302 0.5355 0.6594 0.0520  0.1230  0.0697  378 VAL D CG1 
15750 C CG2 . VAL D 378 ? 0.3236 0.5275 0.6573 0.0311  0.1092  0.0752  378 VAL D CG2 
15751 N N   . GLY D 379 ? 0.3265 0.5348 0.6825 0.0558  0.1067  0.0660  379 GLY D N   
15752 C CA  . GLY D 379 ? 0.3259 0.5268 0.6793 0.0648  0.1068  0.0609  379 GLY D CA  
15753 C C   . GLY D 379 ? 0.3106 0.4977 0.6603 0.0598  0.0952  0.0557  379 GLY D C   
15754 O O   . GLY D 379 ? 0.3161 0.5104 0.6783 0.0524  0.0872  0.0591  379 GLY D O   
15755 N N   . ILE D 380 ? 0.2888 0.4563 0.6210 0.0643  0.0947  0.0476  380 ILE D N   
15756 C CA  . ILE D 380 ? 0.2814 0.4338 0.6067 0.0597  0.0848  0.0421  380 ILE D CA  
15757 C C   . ILE D 380 ? 0.2801 0.4195 0.5894 0.0534  0.0827  0.0387  380 ILE D C   
15758 O O   . ILE D 380 ? 0.2851 0.4162 0.5796 0.0573  0.0889  0.0356  380 ILE D O   
15759 C CB  . ILE D 380 ? 0.2734 0.4125 0.5899 0.0680  0.0853  0.0358  380 ILE D CB  
15760 C CG1 . ILE D 380 ? 0.2754 0.4269 0.6066 0.0760  0.0886  0.0394  380 ILE D CG1 
15761 C CG2 . ILE D 380 ? 0.2654 0.3892 0.5744 0.0625  0.0753  0.0305  380 ILE D CG2 
15762 C CD1 . ILE D 380 ? 0.2767 0.4139 0.5981 0.0853  0.0905  0.0335  380 ILE D CD1 
15763 N N   . GLU D 381 ? 0.2802 0.4173 0.5919 0.0440  0.0739  0.0393  381 GLU D N   
15764 C CA  . GLU D 381 ? 0.2779 0.4060 0.5778 0.0376  0.0717  0.0380  381 GLU D CA  
15765 C C   . GLU D 381 ? 0.2611 0.3771 0.5568 0.0316  0.0616  0.0340  381 GLU D C   
15766 O O   . GLU D 381 ? 0.2341 0.3544 0.5405 0.0269  0.0552  0.0360  381 GLU D O   
15767 C CB  . GLU D 381 ? 0.2926 0.4347 0.6019 0.0321  0.0740  0.0454  381 GLU D CB  
15768 C CG  . GLU D 381 ? 0.3269 0.4604 0.6227 0.0273  0.0743  0.0449  381 GLU D CG  
15769 C CD  . GLU D 381 ? 0.3175 0.4634 0.6219 0.0209  0.0761  0.0527  381 GLU D CD  
15770 O OE1 . GLU D 381 ? 0.3147 0.4750 0.6277 0.0237  0.0835  0.0579  381 GLU D OE1 
15771 O OE2 . GLU D 381 ? 0.3523 0.4931 0.6548 0.0130  0.0701  0.0537  381 GLU D OE2 
15772 N N   . ASP D 382 ? 0.2727 0.3730 0.5516 0.0320  0.0605  0.0283  382 ASP D N   
15773 C CA  . ASP D 382 ? 0.2683 0.3574 0.5415 0.0261  0.0521  0.0251  382 ASP D CA  
15774 C C   . ASP D 382 ? 0.2556 0.3470 0.5293 0.0186  0.0500  0.0290  382 ASP D C   
15775 O O   . ASP D 382 ? 0.2487 0.3413 0.5159 0.0188  0.0551  0.0309  382 ASP D O   
15776 C CB  . ASP D 382 ? 0.2787 0.3520 0.5348 0.0290  0.0519  0.0183  382 ASP D CB  
15777 C CG  . ASP D 382 ? 0.2941 0.3634 0.5367 0.0309  0.0579  0.0176  382 ASP D CG  
15778 O OD1 . ASP D 382 ? 0.2693 0.3456 0.5129 0.0362  0.0660  0.0196  382 ASP D OD1 
15779 O OD2 . ASP D 382 ? 0.3031 0.3625 0.5342 0.0271  0.0543  0.0153  382 ASP D OD2 
15780 N N   . MET D 383 ? 0.2362 0.3278 0.5172 0.0124  0.0426  0.0303  383 MET D N   
15781 C CA  . MET D 383 ? 0.2517 0.3441 0.5341 0.0050  0.0397  0.0342  383 MET D CA  
15782 C C   . MET D 383 ? 0.2269 0.3073 0.5040 0.0009  0.0318  0.0307  383 MET D C   
15783 O O   . MET D 383 ? 0.1929 0.2710 0.4742 0.0008  0.0270  0.0283  383 MET D O   
15784 C CB  . MET D 383 ? 0.2413 0.3473 0.5398 0.0007  0.0388  0.0405  383 MET D CB  
15785 C CG  . MET D 383 ? 0.2574 0.3775 0.5648 0.0054  0.0460  0.0441  383 MET D CG  
15786 S SD  . MET D 383 ? 0.2554 0.3940 0.5831 -0.0001 0.0451  0.0524  383 MET D SD  
15787 C CE  . MET D 383 ? 0.2611 0.3995 0.5858 -0.0082 0.0454  0.0575  383 MET D CE  
15788 N N   . GLU D 384 ? 0.2409 0.3139 0.5083 -0.0019 0.0308  0.0307  384 GLU D N   
15789 C CA  . GLU D 384 ? 0.2567 0.3198 0.5201 -0.0060 0.0239  0.0288  384 GLU D CA  
15790 C C   . GLU D 384 ? 0.2590 0.3255 0.5294 -0.0125 0.0214  0.0341  384 GLU D C   
15791 O O   . GLU D 384 ? 0.2682 0.3365 0.5360 -0.0149 0.0241  0.0381  384 GLU D O   
15792 C CB  . GLU D 384 ? 0.2836 0.3366 0.5329 -0.0051 0.0236  0.0261  384 GLU D CB  
15793 C CG  . GLU D 384 ? 0.2922 0.3360 0.5387 -0.0082 0.0168  0.0243  384 GLU D CG  
15794 C CD  . GLU D 384 ? 0.2887 0.3236 0.5227 -0.0077 0.0153  0.0220  384 GLU D CD  
15795 O OE1 . GLU D 384 ? 0.2585 0.2939 0.4848 -0.0060 0.0195  0.0227  384 GLU D OE1 
15796 O OE2 . GLU D 384 ? 0.2909 0.3189 0.5233 -0.0087 0.0100  0.0197  384 GLU D OE2 
15797 N N   . LEU D 385 ? 0.2645 0.3326 0.5440 -0.0155 0.0167  0.0345  385 LEU D N   
15798 C CA  . LEU D 385 ? 0.2696 0.3392 0.5556 -0.0224 0.0133  0.0389  385 LEU D CA  
15799 C C   . LEU D 385 ? 0.2686 0.3252 0.5468 -0.0252 0.0083  0.0372  385 LEU D C   
15800 O O   . LEU D 385 ? 0.2683 0.3172 0.5434 -0.0238 0.0042  0.0327  385 LEU D O   
15801 C CB  . LEU D 385 ? 0.2582 0.3337 0.5554 -0.0241 0.0099  0.0394  385 LEU D CB  
15802 C CG  . LEU D 385 ? 0.2711 0.3602 0.5776 -0.0205 0.0143  0.0412  385 LEU D CG  
15803 C CD1 . LEU D 385 ? 0.2703 0.3645 0.5874 -0.0228 0.0095  0.0419  385 LEU D CD1 
15804 C CD2 . LEU D 385 ? 0.2687 0.3692 0.5805 -0.0219 0.0201  0.0474  385 LEU D CD2 
15805 N N   . ALA D 386 ? 0.2602 0.3144 0.5347 -0.0285 0.0090  0.0409  386 ALA D N   
15806 C CA  . ALA D 386 ? 0.2689 0.3109 0.5355 -0.0301 0.0050  0.0399  386 ALA D CA  
15807 C C   . ALA D 386 ? 0.2567 0.2941 0.5279 -0.0361 0.0000  0.0420  386 ALA D C   
15808 O O   . ALA D 386 ? 0.2393 0.2796 0.5138 -0.0410 0.0008  0.0473  386 ALA D O   
15809 C CB  . ALA D 386 ? 0.2779 0.3189 0.5370 -0.0302 0.0084  0.0431  386 ALA D CB  
15810 N N   . PHE D 387 ? 0.2460 0.2761 0.5167 -0.0357 -0.0048 0.0380  387 PHE D N   
15811 C CA  . PHE D 387 ? 0.2424 0.2656 0.5151 -0.0409 -0.0096 0.0390  387 PHE D CA  
15812 C C   . PHE D 387 ? 0.2643 0.2754 0.5287 -0.0415 -0.0115 0.0395  387 PHE D C   
15813 O O   . PHE D 387 ? 0.2706 0.2770 0.5282 -0.0370 -0.0112 0.0369  387 PHE D O   
15814 C CB  . PHE D 387 ? 0.2376 0.2580 0.5127 -0.0404 -0.0137 0.0347  387 PHE D CB  
15815 C CG  . PHE D 387 ? 0.2526 0.2844 0.5371 -0.0411 -0.0133 0.0353  387 PHE D CG  
15816 C CD1 . PHE D 387 ? 0.2181 0.2597 0.5053 -0.0363 -0.0090 0.0346  387 PHE D CD1 
15817 C CD2 . PHE D 387 ? 0.2599 0.2926 0.5504 -0.0466 -0.0174 0.0368  387 PHE D CD2 
15818 C CE1 . PHE D 387 ? 0.2322 0.2848 0.5289 -0.0364 -0.0084 0.0359  387 PHE D CE1 
15819 C CE2 . PHE D 387 ? 0.2471 0.2915 0.5470 -0.0473 -0.0174 0.0382  387 PHE D CE2 
15820 C CZ  . PHE D 387 ? 0.2361 0.2910 0.5398 -0.0419 -0.0128 0.0380  387 PHE D CZ  
15821 N N   . GLU D 388 ? 0.2827 0.2889 0.5481 -0.0472 -0.0136 0.0433  388 GLU D N   
15822 C CA  . GLU D 388 ? 0.3025 0.2958 0.5606 -0.0481 -0.0158 0.0444  388 GLU D CA  
15823 C C   . GLU D 388 ? 0.3129 0.2964 0.5717 -0.0528 -0.0206 0.0441  388 GLU D C   
15824 O O   . GLU D 388 ? 0.3248 0.3123 0.5896 -0.0588 -0.0217 0.0469  388 GLU D O   
15825 C CB  . GLU D 388 ? 0.3152 0.3095 0.5715 -0.0511 -0.0133 0.0506  388 GLU D CB  
15826 C CG  . GLU D 388 ? 0.3198 0.3206 0.5722 -0.0467 -0.0087 0.0513  388 GLU D CG  
15827 C CD  . GLU D 388 ? 0.3371 0.3419 0.5890 -0.0504 -0.0053 0.0579  388 GLU D CD  
15828 O OE1 . GLU D 388 ? 0.3259 0.3305 0.5823 -0.0568 -0.0062 0.0624  388 GLU D OE1 
15829 O OE2 . GLU D 388 ? 0.3633 0.3719 0.6100 -0.0472 -0.0017 0.0588  388 GLU D OE2 
15830 N N   . PHE D 389 ? 0.2956 0.2666 0.5478 -0.0500 -0.0233 0.0408  389 PHE D N   
15831 C CA  . PHE D 389 ? 0.3119 0.2703 0.5616 -0.0531 -0.0275 0.0396  389 PHE D CA  
15832 C C   . PHE D 389 ? 0.3545 0.2998 0.5973 -0.0535 -0.0283 0.0424  389 PHE D C   
15833 O O   . PHE D 389 ? 0.3418 0.2844 0.5800 -0.0480 -0.0271 0.0419  389 PHE D O   
15834 C CB  . PHE D 389 ? 0.2896 0.2443 0.5373 -0.0485 -0.0292 0.0333  389 PHE D CB  
15835 C CG  . PHE D 389 ? 0.2688 0.2347 0.5226 -0.0478 -0.0288 0.0306  389 PHE D CG  
15836 C CD1 . PHE D 389 ? 0.2687 0.2348 0.5260 -0.0525 -0.0320 0.0299  389 PHE D CD1 
15837 C CD2 . PHE D 389 ? 0.2571 0.2322 0.5123 -0.0425 -0.0258 0.0286  389 PHE D CD2 
15838 C CE1 . PHE D 389 ? 0.2604 0.2368 0.5233 -0.0515 -0.0319 0.0279  389 PHE D CE1 
15839 C CE2 . PHE D 389 ? 0.2471 0.2315 0.5076 -0.0416 -0.0254 0.0266  389 PHE D CE2 
15840 C CZ  . PHE D 389 ? 0.2560 0.2413 0.5207 -0.0458 -0.0284 0.0263  389 PHE D CZ  
15841 N N   . TYR D 390 ? 0.3539 0.2906 0.5959 -0.0601 -0.0308 0.0453  390 TYR D N   
15842 C CA  . TYR D 390 ? 0.3905 0.3140 0.6263 -0.0617 -0.0317 0.0490  390 TYR D CA  
15843 C C   . TYR D 390 ? 0.4070 0.3126 0.6369 -0.0634 -0.0358 0.0463  390 TYR D C   
15844 O O   . TYR D 390 ? 0.3966 0.3008 0.6283 -0.0676 -0.0386 0.0438  390 TYR D O   
15845 C CB  . TYR D 390 ? 0.3992 0.3260 0.6380 -0.0694 -0.0310 0.0558  390 TYR D CB  
15846 C CG  . TYR D 390 ? 0.4286 0.3712 0.6717 -0.0684 -0.0263 0.0596  390 TYR D CG  
15847 C CD1 . TYR D 390 ? 0.4201 0.3792 0.6708 -0.0677 -0.0238 0.0583  390 TYR D CD1 
15848 C CD2 . TYR D 390 ? 0.4526 0.3930 0.6912 -0.0680 -0.0241 0.0646  390 TYR D CD2 
15849 C CE1 . TYR D 390 ? 0.3908 0.3631 0.6441 -0.0663 -0.0189 0.0614  390 TYR D CE1 
15850 C CE2 . TYR D 390 ? 0.4514 0.4053 0.6923 -0.0670 -0.0195 0.0679  390 TYR D CE2 
15851 C CZ  . TYR D 390 ? 0.4118 0.3814 0.6597 -0.0660 -0.0167 0.0661  390 TYR D CZ  
15852 O OH  . TYR D 390 ? 0.3997 0.3812 0.6484 -0.0646 -0.0116 0.0690  390 TYR D OH  
15853 N N   . ASP D 391 ? 0.4041 0.2954 0.6264 -0.0605 -0.0363 0.0474  391 ASP D N   
15854 C CA  . ASP D 391 ? 0.4042 0.2761 0.6191 -0.0606 -0.0394 0.0449  391 ASP D CA  
15855 C C   . ASP D 391 ? 0.4240 0.2844 0.6360 -0.0687 -0.0415 0.0499  391 ASP D C   
15856 O O   . ASP D 391 ? 0.3911 0.2609 0.6083 -0.0747 -0.0406 0.0550  391 ASP D O   
15857 C CB  . ASP D 391 ? 0.4056 0.2692 0.6146 -0.0514 -0.0383 0.0429  391 ASP D CB  
15858 C CG  . ASP D 391 ? 0.4275 0.2873 0.6335 -0.0488 -0.0369 0.0483  391 ASP D CG  
15859 O OD1 . ASP D 391 ? 0.4225 0.2829 0.6292 -0.0548 -0.0368 0.0539  391 ASP D OD1 
15860 O OD2 . ASP D 391 ? 0.4660 0.3228 0.6691 -0.0408 -0.0360 0.0471  391 ASP D OD2 
15861 N N   . SER D 392 ? 0.4633 0.3031 0.6666 -0.0689 -0.0442 0.0484  392 SER D N   
15862 C CA  . SER D 392 ? 0.5260 0.3527 0.7257 -0.0777 -0.0469 0.0525  392 SER D CA  
15863 C C   . SER D 392 ? 0.5391 0.3625 0.7369 -0.0776 -0.0451 0.0594  392 SER D C   
15864 O O   . SER D 392 ? 0.5390 0.3558 0.7358 -0.0858 -0.0467 0.0643  392 SER D O   
15865 C CB  . SER D 392 ? 0.5426 0.3469 0.7325 -0.0786 -0.0505 0.0482  392 SER D CB  
15866 O OG  . SER D 392 ? 0.5531 0.3472 0.7362 -0.0683 -0.0489 0.0446  392 SER D OG  
15867 N N   . ASP D 393 ? 0.5654 0.3953 0.7634 -0.0692 -0.0419 0.0604  393 ASP D N   
15868 C CA  . ASP D 393 ? 0.5634 0.3935 0.7600 -0.0691 -0.0401 0.0674  393 ASP D CA  
15869 C C   . ASP D 393 ? 0.5211 0.3728 0.7255 -0.0714 -0.0369 0.0711  393 ASP D C   
15870 O O   . ASP D 393 ? 0.4811 0.3361 0.6841 -0.0698 -0.0348 0.0763  393 ASP D O   
15871 C CB  . ASP D 393 ? 0.6220 0.4471 0.8138 -0.0588 -0.0389 0.0670  393 ASP D CB  
15872 C CG  . ASP D 393 ? 0.7121 0.5136 0.8948 -0.0561 -0.0409 0.0673  393 ASP D CG  
15873 O OD1 . ASP D 393 ? 0.7360 0.5239 0.9144 -0.0633 -0.0427 0.0713  393 ASP D OD1 
15874 O OD2 . ASP D 393 ? 0.7135 0.5106 0.8935 -0.0469 -0.0404 0.0637  393 ASP D OD2 
15875 N N   . ASN D 394 ? 0.5046 0.3709 0.7167 -0.0744 -0.0364 0.0684  394 ASN D N   
15876 C CA  . ASN D 394 ? 0.5006 0.3872 0.7199 -0.0755 -0.0328 0.0712  394 ASN D CA  
15877 C C   . ASN D 394 ? 0.4928 0.3879 0.7108 -0.0667 -0.0298 0.0701  394 ASN D C   
15878 O O   . ASN D 394 ? 0.4387 0.3449 0.6582 -0.0670 -0.0265 0.0742  394 ASN D O   
15879 C CB  . ASN D 394 ? 0.5218 0.4097 0.7425 -0.0838 -0.0319 0.0791  394 ASN D CB  
15880 C CG  . ASN D 394 ? 0.5582 0.4674 0.7882 -0.0871 -0.0284 0.0815  394 ASN D CG  
15881 O OD1 . ASN D 394 ? 0.5281 0.4474 0.7651 -0.0879 -0.0287 0.0777  394 ASN D OD1 
15882 N ND2 . ASN D 394 ? 0.5802 0.4961 0.8102 -0.0888 -0.0248 0.0879  394 ASN D ND2 
15883 N N   . LYS D 395 ? 0.5046 0.3952 0.7198 -0.0592 -0.0308 0.0645  395 LYS D N   
15884 C CA  . LYS D 395 ? 0.5268 0.4264 0.7416 -0.0515 -0.0287 0.0628  395 LYS D CA  
15885 C C   . LYS D 395 ? 0.4739 0.3853 0.6941 -0.0489 -0.0279 0.0567  395 LYS D C   
15886 O O   . LYS D 395 ? 0.4565 0.3641 0.6782 -0.0499 -0.0298 0.0525  395 LYS D O   
15887 C CB  . LYS D 395 ? 0.5767 0.4651 0.7855 -0.0443 -0.0301 0.0619  395 LYS D CB  
15888 C CG  . LYS D 395 ? 0.6793 0.5566 0.8822 -0.0451 -0.0307 0.0683  395 LYS D CG  
15889 C CD  . LYS D 395 ? 0.7812 0.6483 0.9793 -0.0371 -0.0320 0.0676  395 LYS D CD  
15890 C CE  . LYS D 395 ? 0.8531 0.7104 1.0456 -0.0377 -0.0326 0.0747  395 LYS D CE  
15891 N NZ  . LYS D 395 ? 0.9071 0.7533 1.0955 -0.0298 -0.0341 0.0746  395 LYS D NZ  
15892 N N   . ILE D 396 ? 0.4527 0.3775 0.6747 -0.0456 -0.0251 0.0564  396 ILE D N   
15893 C CA  . ILE D 396 ? 0.4230 0.3587 0.6498 -0.0433 -0.0242 0.0511  396 ILE D CA  
15894 C C   . ILE D 396 ? 0.3637 0.2938 0.5882 -0.0369 -0.0259 0.0461  396 ILE D C   
15895 O O   . ILE D 396 ? 0.3668 0.2944 0.5875 -0.0323 -0.0260 0.0470  396 ILE D O   
15896 C CB  . ILE D 396 ? 0.4510 0.4011 0.6794 -0.0422 -0.0205 0.0523  396 ILE D CB  
15897 C CG1 . ILE D 396 ? 0.5077 0.4651 0.7408 -0.0488 -0.0182 0.0568  396 ILE D CG1 
15898 C CG2 . ILE D 396 ? 0.4407 0.3995 0.6722 -0.0381 -0.0196 0.0466  396 ILE D CG2 
15899 C CD1 . ILE D 396 ? 0.5287 0.4983 0.7617 -0.0482 -0.0136 0.0596  396 ILE D CD1 
15900 N N   . ILE D 397 ? 0.3460 0.2744 0.5729 -0.0371 -0.0273 0.0413  397 ILE D N   
15901 C CA  . ILE D 397 ? 0.3579 0.2826 0.5833 -0.0313 -0.0283 0.0364  397 ILE D CA  
15902 C C   . ILE D 397 ? 0.3411 0.2777 0.5706 -0.0289 -0.0271 0.0321  397 ILE D C   
15903 O O   . ILE D 397 ? 0.3204 0.2564 0.5492 -0.0240 -0.0274 0.0285  397 ILE D O   
15904 C CB  . ILE D 397 ? 0.3810 0.2923 0.6037 -0.0326 -0.0308 0.0340  397 ILE D CB  
15905 C CG1 . ILE D 397 ? 0.4070 0.3219 0.6336 -0.0378 -0.0319 0.0317  397 ILE D CG1 
15906 C CG2 . ILE D 397 ? 0.3929 0.2904 0.6106 -0.0348 -0.0321 0.0382  397 ILE D CG2 
15907 C CD1 . ILE D 397 ? 0.4301 0.3306 0.6527 -0.0415 -0.0349 0.0303  397 ILE D CD1 
15908 N N   . LYS D 398 ? 0.3221 0.2696 0.5560 -0.0320 -0.0254 0.0328  398 LYS D N   
15909 C CA  . LYS D 398 ? 0.3262 0.2840 0.5635 -0.0295 -0.0240 0.0291  398 LYS D CA  
15910 C C   . LYS D 398 ? 0.3201 0.2893 0.5610 -0.0319 -0.0212 0.0315  398 LYS D C   
15911 O O   . LYS D 398 ? 0.2874 0.2585 0.5315 -0.0369 -0.0209 0.0347  398 LYS D O   
15912 C CB  . LYS D 398 ? 0.3318 0.2884 0.5715 -0.0298 -0.0257 0.0248  398 LYS D CB  
15913 C CG  . LYS D 398 ? 0.3276 0.2936 0.5702 -0.0267 -0.0244 0.0211  398 LYS D CG  
15914 C CD  . LYS D 398 ? 0.3215 0.2874 0.5666 -0.0274 -0.0260 0.0175  398 LYS D CD  
15915 C CE  . LYS D 398 ? 0.2973 0.2720 0.5450 -0.0245 -0.0245 0.0146  398 LYS D CE  
15916 N NZ  . LYS D 398 ? 0.2802 0.2541 0.5294 -0.0247 -0.0262 0.0114  398 LYS D NZ  
15917 N N   . ASN D 399 ? 0.2979 0.2741 0.5376 -0.0282 -0.0190 0.0303  399 ASN D N   
15918 C CA  . ASN D 399 ? 0.2857 0.2727 0.5279 -0.0285 -0.0156 0.0310  399 ASN D CA  
15919 C C   . ASN D 399 ? 0.2677 0.2596 0.5124 -0.0255 -0.0153 0.0261  399 ASN D C   
15920 O O   . ASN D 399 ? 0.2653 0.2537 0.5073 -0.0221 -0.0168 0.0229  399 ASN D O   
15921 C CB  . ASN D 399 ? 0.2931 0.2828 0.5298 -0.0261 -0.0134 0.0325  399 ASN D CB  
15922 C CG  . ASN D 399 ? 0.3174 0.3041 0.5512 -0.0290 -0.0128 0.0380  399 ASN D CG  
15923 O OD1 . ASN D 399 ? 0.3806 0.3722 0.6170 -0.0325 -0.0104 0.0416  399 ASN D OD1 
15924 N ND2 . ASN D 399 ? 0.3395 0.3188 0.5680 -0.0274 -0.0149 0.0393  399 ASN D ND2 
15925 N N   . GLU D 400 ? 0.2707 0.2707 0.5208 -0.0266 -0.0134 0.0261  400 GLU D N   
15926 C CA  . GLU D 400 ? 0.2413 0.2461 0.4934 -0.0234 -0.0126 0.0221  400 GLU D CA  
15927 C C   . GLU D 400 ? 0.2526 0.2678 0.5094 -0.0236 -0.0087 0.0238  400 GLU D C   
15928 O O   . GLU D 400 ? 0.2455 0.2655 0.5076 -0.0272 -0.0079 0.0276  400 GLU D O   
15929 C CB  . GLU D 400 ? 0.2493 0.2503 0.5043 -0.0241 -0.0160 0.0193  400 GLU D CB  
15930 C CG  . GLU D 400 ? 0.2569 0.2611 0.5131 -0.0206 -0.0157 0.0152  400 GLU D CG  
15931 C CD  . GLU D 400 ? 0.2635 0.2643 0.5215 -0.0210 -0.0187 0.0124  400 GLU D CD  
15932 O OE1 . GLU D 400 ? 0.2613 0.2576 0.5202 -0.0245 -0.0213 0.0136  400 GLU D OE1 
15933 O OE2 . GLU D 400 ? 0.2627 0.2647 0.5205 -0.0179 -0.0186 0.0092  400 GLU D OE2 
15934 N N   . SER D 401 ? 0.2476 0.2662 0.5026 -0.0195 -0.0064 0.0209  401 SER D N   
15935 C CA  . SER D 401 ? 0.2312 0.2589 0.4895 -0.0179 -0.0020 0.0219  401 SER D CA  
15936 C C   . SER D 401 ? 0.2292 0.2610 0.4939 -0.0164 -0.0026 0.0197  401 SER D C   
15937 O O   . SER D 401 ? 0.2099 0.2370 0.4733 -0.0149 -0.0054 0.0160  401 SER D O   
15938 C CB  . SER D 401 ? 0.2459 0.2729 0.4962 -0.0144 0.0012  0.0205  401 SER D CB  
15939 O OG  . SER D 401 ? 0.2583 0.2855 0.5046 -0.0161 0.0031  0.0242  401 SER D OG  
15940 N N   . ILE D 402 ? 0.2178 0.2592 0.4901 -0.0169 0.0000  0.0226  402 ILE D N   
15941 C CA  . ILE D 402 ? 0.2257 0.2723 0.5040 -0.0144 0.0001  0.0211  402 ILE D CA  
15942 C C   . ILE D 402 ? 0.2223 0.2763 0.5011 -0.0100 0.0061  0.0218  402 ILE D C   
15943 O O   . ILE D 402 ? 0.2382 0.2995 0.5204 -0.0112 0.0097  0.0260  402 ILE D O   
15944 C CB  . ILE D 402 ? 0.2323 0.2842 0.5204 -0.0189 -0.0032 0.0241  402 ILE D CB  
15945 C CG1 . ILE D 402 ? 0.2425 0.2848 0.5278 -0.0230 -0.0088 0.0229  402 ILE D CG1 
15946 C CG2 . ILE D 402 ? 0.2237 0.2822 0.5187 -0.0162 -0.0034 0.0234  402 ILE D CG2 
15947 C CD1 . ILE D 402 ? 0.2412 0.2761 0.5223 -0.0205 -0.0119 0.0179  402 ILE D CD1 
15948 N N   . ASN D 403 ? 0.2193 0.2706 0.4940 -0.0049 0.0075  0.0178  403 ASN D N   
15949 C CA  . ASN D 403 ? 0.2260 0.2817 0.4989 0.0001  0.0136  0.0177  403 ASN D CA  
15950 C C   . ASN D 403 ? 0.2204 0.2848 0.5035 0.0029  0.0148  0.0189  403 ASN D C   
15951 O O   . ASN D 403 ? 0.2160 0.2777 0.5010 0.0039  0.0114  0.0166  403 ASN D O   
15952 C CB  . ASN D 403 ? 0.2341 0.2805 0.4956 0.0039  0.0146  0.0127  403 ASN D CB  
15953 C CG  . ASN D 403 ? 0.2548 0.2945 0.5063 0.0019  0.0140  0.0120  403 ASN D CG  
15954 O OD1 . ASN D 403 ? 0.2703 0.3117 0.5170 0.0027  0.0182  0.0136  403 ASN D OD1 
15955 N ND2 . ASN D 403 ? 0.2649 0.2972 0.5132 -0.0004 0.0089  0.0100  403 ASN D ND2 
15956 N N   . ILE D 404 ? 0.2121 0.2876 0.5022 0.0040  0.0196  0.0232  404 ILE D N   
15957 C CA  . ILE D 404 ? 0.2125 0.2977 0.5133 0.0070  0.0207  0.0251  404 ILE D CA  
15958 C C   . ILE D 404 ? 0.2073 0.2968 0.5064 0.0141  0.0285  0.0251  404 ILE D C   
15959 O O   . ILE D 404 ? 0.2011 0.2883 0.4923 0.0152  0.0330  0.0249  404 ILE D O   
15960 C CB  . ILE D 404 ? 0.2193 0.3165 0.5336 0.0017  0.0185  0.0310  404 ILE D CB  
15961 C CG1 . ILE D 404 ? 0.2255 0.3316 0.5430 -0.0002 0.0236  0.0361  404 ILE D CG1 
15962 C CG2 . ILE D 404 ? 0.2248 0.3155 0.5390 -0.0051 0.0108  0.0304  404 ILE D CG2 
15963 C CD1 . ILE D 404 ? 0.2297 0.3502 0.5623 -0.0046 0.0225  0.0427  404 ILE D CD1 
15964 N N   . LEU D 405 ? 0.2154 0.3102 0.5212 0.0192  0.0299  0.0253  405 LEU D N   
15965 C CA  . LEU D 405 ? 0.2199 0.3211 0.5269 0.0264  0.0379  0.0265  405 LEU D CA  
15966 C C   . LEU D 405 ? 0.2234 0.3423 0.5475 0.0264  0.0392  0.0331  405 LEU D C   
15967 O O   . LEU D 405 ? 0.2381 0.3610 0.5709 0.0267  0.0350  0.0340  405 LEU D O   
15968 C CB  . LEU D 405 ? 0.2240 0.3153 0.5235 0.0332  0.0388  0.0212  405 LEU D CB  
15969 C CG  . LEU D 405 ? 0.2303 0.3257 0.5298 0.0421  0.0472  0.0216  405 LEU D CG  
15970 C CD1 . LEU D 405 ? 0.2422 0.3353 0.5313 0.0431  0.0537  0.0211  405 LEU D CD1 
15971 C CD2 . LEU D 405 ? 0.2248 0.3096 0.5177 0.0487  0.0476  0.0168  405 LEU D CD2 
15972 N N   . ALA D 406 ? 0.2357 0.3660 0.5652 0.0263  0.0450  0.0380  406 ALA D N   
15973 C CA  . ALA D 406 ? 0.2318 0.3802 0.5791 0.0239  0.0448  0.0451  406 ALA D CA  
15974 C C   . ALA D 406 ? 0.2350 0.3975 0.5901 0.0310  0.0541  0.0493  406 ALA D C   
15975 O O   . ALA D 406 ? 0.2372 0.3970 0.5832 0.0350  0.0615  0.0482  406 ALA D O   
15976 C CB  . ALA D 406 ? 0.2366 0.3878 0.5868 0.0141  0.0411  0.0488  406 ALA D CB  
15977 N N   . SER D 407 ? 0.2439 0.4225 0.6161 0.0320  0.0534  0.0547  407 SER D N   
15978 C CA  . SER D 407 ? 0.2704 0.4663 0.6541 0.0379  0.0619  0.0604  407 SER D CA  
15979 C C   . SER D 407 ? 0.2726 0.4886 0.6772 0.0326  0.0583  0.0685  407 SER D C   
15980 O O   . SER D 407 ? 0.2947 0.5102 0.7048 0.0273  0.0493  0.0687  407 SER D O   
15981 C CB  . SER D 407 ? 0.2698 0.4641 0.6520 0.0497  0.0672  0.0578  407 SER D CB  
15982 O OG  . SER D 407 ? 0.2806 0.4918 0.6732 0.0561  0.0765  0.0634  407 SER D OG  
15983 N N   . LYS D 408 ? 0.2787 0.5129 0.6951 0.0343  0.0654  0.0754  408 LYS D N   
15984 C CA  . LYS D 408 ? 0.3073 0.5625 0.7451 0.0295  0.0620  0.0837  408 LYS D CA  
15985 C C   . LYS D 408 ? 0.3122 0.5741 0.7605 0.0357  0.0592  0.0845  408 LYS D C   
15986 O O   . LYS D 408 ? 0.2924 0.5698 0.7576 0.0310  0.0538  0.0907  408 LYS D O   
15987 C CB  . LYS D 408 ? 0.3149 0.5909 0.7654 0.0308  0.0710  0.0918  408 LYS D CB  
15988 C CG  . LYS D 408 ? 0.3355 0.6189 0.7884 0.0445  0.0818  0.0923  408 LYS D CG  
15989 C CD  . LYS D 408 ? 0.3266 0.6303 0.7908 0.0468  0.0922  0.1001  408 LYS D CD  
15990 C CE  . LYS D 408 ? 0.3449 0.6545 0.8115 0.0612  0.1020  0.1000  408 LYS D CE  
15991 N NZ  . LYS D 408 ? 0.3667 0.6990 0.8471 0.0643  0.1123  0.1084  408 LYS D NZ  
15992 N N   . THR D 409 ? 0.3271 0.5773 0.7655 0.0457  0.0622  0.0786  409 THR D N   
15993 C CA  . THR D 409 ? 0.3456 0.6026 0.7943 0.0525  0.0602  0.0802  409 THR D CA  
15994 C C   . THR D 409 ? 0.3606 0.5964 0.7933 0.0592  0.0592  0.0718  409 THR D C   
15995 O O   . THR D 409 ? 0.4053 0.6221 0.8198 0.0578  0.0592  0.0648  409 THR D O   
15996 C CB  . THR D 409 ? 0.3435 0.6217 0.8074 0.0610  0.0698  0.0871  409 THR D CB  
15997 O OG1 . THR D 409 ? 0.3521 0.6425 0.8319 0.0627  0.0642  0.0915  409 THR D OG1 
15998 C CG2 . THR D 409 ? 0.3490 0.6186 0.8008 0.0733  0.0813  0.0829  409 THR D CG2 
15999 N N   . ALA D 410 ? 0.3633 0.6025 0.8031 0.0659  0.0574  0.0727  410 ALA D N   
16000 C CA  . ALA D 410 ? 0.3553 0.5747 0.7808 0.0717  0.0559  0.0654  410 ALA D CA  
16001 C C   . ALA D 410 ? 0.3573 0.5654 0.7689 0.0814  0.0663  0.0606  410 ALA D C   
16002 O O   . ALA D 410 ? 0.3435 0.5633 0.7611 0.0878  0.0756  0.0642  410 ALA D O   
16003 C CB  . ALA D 410 ? 0.3421 0.5686 0.7790 0.0769  0.0520  0.0686  410 ALA D CB  
16004 N N   . PHE D 411 ? 0.3647 0.5499 0.7570 0.0818  0.0648  0.0524  411 PHE D N   
16005 C CA  . PHE D 411 ? 0.3743 0.5461 0.7511 0.0903  0.0735  0.0470  411 PHE D CA  
16006 C C   . PHE D 411 ? 0.3769 0.5289 0.7412 0.0945  0.0704  0.0405  411 PHE D C   
16007 O O   . PHE D 411 ? 0.3692 0.5159 0.7339 0.0893  0.0615  0.0394  411 PHE D O   
16008 C CB  . PHE D 411 ? 0.3686 0.5336 0.7329 0.0847  0.0762  0.0442  411 PHE D CB  
16009 C CG  . PHE D 411 ? 0.3670 0.5195 0.7218 0.0740  0.0673  0.0401  411 PHE D CG  
16010 C CD1 . PHE D 411 ? 0.3393 0.5015 0.7034 0.0638  0.0614  0.0442  411 PHE D CD1 
16011 C CD2 . PHE D 411 ? 0.3473 0.4782 0.6838 0.0741  0.0652  0.0323  411 PHE D CD2 
16012 C CE1 . PHE D 411 ? 0.3046 0.4548 0.6596 0.0550  0.0540  0.0405  411 PHE D CE1 
16013 C CE2 . PHE D 411 ? 0.3192 0.4402 0.6480 0.0649  0.0577  0.0291  411 PHE D CE2 
16014 C CZ  . PHE D 411 ? 0.3081 0.4385 0.6461 0.0560  0.0524  0.0331  411 PHE D CZ  
16015 N N   . GLU D 412 ? 0.3868 0.5273 0.7394 0.1042  0.0780  0.0364  412 GLU D N   
16016 C CA  . GLU D 412 ? 0.4111 0.5315 0.7508 0.1080  0.0756  0.0303  412 GLU D CA  
16017 C C   . GLU D 412 ? 0.3701 0.4718 0.6915 0.1003  0.0714  0.0233  412 GLU D C   
16018 O O   . GLU D 412 ? 0.3665 0.4654 0.6790 0.0978  0.0752  0.0213  412 GLU D O   
16019 C CB  . GLU D 412 ? 0.4906 0.6039 0.8238 0.1211  0.0849  0.0284  412 GLU D CB  
16020 C CG  . GLU D 412 ? 0.5684 0.6970 0.9192 0.1303  0.0877  0.0348  412 GLU D CG  
16021 C CD  . GLU D 412 ? 0.6608 0.7764 1.0019 0.1437  0.0957  0.0315  412 GLU D CD  
16022 O OE1 . GLU D 412 ? 0.6964 0.7901 1.0226 0.1450  0.0928  0.0254  412 GLU D OE1 
16023 O OE2 . GLU D 412 ? 0.6273 0.7541 0.9750 0.1528  0.1053  0.0350  412 GLU D OE2 
16024 N N   . LEU D 413 ? 0.3618 0.4516 0.6783 0.0969  0.0637  0.0201  413 LEU D N   
16025 C CA  . LEU D 413 ? 0.3491 0.4199 0.6485 0.0912  0.0596  0.0133  413 LEU D CA  
16026 C C   . LEU D 413 ? 0.3606 0.4131 0.6479 0.0976  0.0607  0.0083  413 LEU D C   
16027 O O   . LEU D 413 ? 0.3388 0.3932 0.6329 0.1039  0.0609  0.0105  413 LEU D O   
16028 C CB  . LEU D 413 ? 0.3464 0.4192 0.6511 0.0815  0.0497  0.0142  413 LEU D CB  
16029 C CG  . LEU D 413 ? 0.3569 0.4438 0.6710 0.0734  0.0472  0.0183  413 LEU D CG  
16030 C CD1 . LEU D 413 ? 0.3591 0.4512 0.6823 0.0662  0.0380  0.0208  413 LEU D CD1 
16031 C CD2 . LEU D 413 ? 0.3640 0.4417 0.6647 0.0682  0.0480  0.0143  413 LEU D CD2 
16032 N N   . PRO D 414 ? 0.3954 0.4292 0.6645 0.0949  0.0600  0.0016  414 PRO D N   
16033 C CA  . PRO D 414 ? 0.3842 0.3990 0.6414 0.0981  0.0585  -0.0032 414 PRO D CA  
16034 C C   . PRO D 414 ? 0.3793 0.3942 0.6431 0.0932  0.0498  -0.0019 414 PRO D C   
16035 O O   . PRO D 414 ? 0.3652 0.3887 0.6360 0.0852  0.0443  0.0002  414 PRO D O   
16036 C CB  . PRO D 414 ? 0.3997 0.3979 0.6380 0.0940  0.0586  -0.0097 414 PRO D CB  
16037 C CG  . PRO D 414 ? 0.3949 0.4037 0.6366 0.0861  0.0569  -0.0080 414 PRO D CG  
16038 C CD  . PRO D 414 ? 0.3727 0.4031 0.6323 0.0880  0.0597  -0.0010 414 PRO D CD  
16039 N N   . GLU D 415 ? 0.4031 0.4076 0.6639 0.0983  0.0490  -0.0029 415 GLU D N   
16040 C CA  . GLU D 415 ? 0.4229 0.4275 0.6897 0.0952  0.0417  -0.0010 415 GLU D CA  
16041 C C   . GLU D 415 ? 0.4065 0.3896 0.6585 0.0949  0.0394  -0.0062 415 GLU D C   
16042 O O   . GLU D 415 ? 0.4002 0.3708 0.6431 0.1019  0.0442  -0.0089 415 GLU D O   
16043 C CB  . GLU D 415 ? 0.4805 0.4958 0.7612 0.1026  0.0424  0.0046  415 GLU D CB  
16044 C CG  . GLU D 415 ? 0.5439 0.5828 0.8426 0.1019  0.0428  0.0112  415 GLU D CG  
16045 C CD  . GLU D 415 ? 0.5763 0.6272 0.8895 0.1098  0.0437  0.0173  415 GLU D CD  
16046 O OE1 . GLU D 415 ? 0.6461 0.6917 0.9569 0.1201  0.0498  0.0171  415 GLU D OE1 
16047 O OE2 . GLU D 415 ? 0.6123 0.6781 0.9392 0.1057  0.0383  0.0224  415 GLU D OE2 
16048 N N   . LEU D 416 ? 0.3717 0.3505 0.6215 0.0866  0.0323  -0.0074 416 LEU D N   
16049 C CA  . LEU D 416 ? 0.3665 0.3275 0.6052 0.0853  0.0292  -0.0109 416 LEU D CA  
16050 C C   . LEU D 416 ? 0.3401 0.3049 0.5875 0.0853  0.0241  -0.0069 416 LEU D C   
16051 O O   . LEU D 416 ? 0.3735 0.3501 0.6300 0.0798  0.0194  -0.0040 416 LEU D O   
16052 C CB  . LEU D 416 ? 0.3595 0.3136 0.5889 0.0760  0.0256  -0.0150 416 LEU D CB  
16053 C CG  . LEU D 416 ? 0.3778 0.3131 0.5944 0.0732  0.0226  -0.0190 416 LEU D CG  
16054 C CD1 . LEU D 416 ? 0.3885 0.3167 0.5943 0.0661  0.0213  -0.0234 416 LEU D CD1 
16055 C CD2 . LEU D 416 ? 0.3710 0.3078 0.5933 0.0696  0.0166  -0.0164 416 LEU D CD2 
16056 N N   . THR D 417 ? 0.3305 0.2844 0.5740 0.0915  0.0250  -0.0069 417 THR D N   
16057 C CA  . THR D 417 ? 0.3265 0.2797 0.5745 0.0911  0.0198  -0.0037 417 THR D CA  
16058 C C   . THR D 417 ? 0.3347 0.2665 0.5686 0.0902  0.0185  -0.0075 417 THR D C   
16059 O O   . THR D 417 ? 0.3528 0.2704 0.5749 0.0929  0.0225  -0.0118 417 THR D O   
16060 C CB  . THR D 417 ? 0.3230 0.2862 0.5830 0.1001  0.0216  0.0019  417 THR D CB  
16061 O OG1 . THR D 417 ? 0.3087 0.2604 0.5616 0.1095  0.0281  0.0001  417 THR D OG1 
16062 C CG2 . THR D 417 ? 0.3055 0.2914 0.5810 0.0995  0.0219  0.0065  417 THR D CG2 
16063 N N   . ILE D 418 ? 0.3303 0.2596 0.5649 0.0859  0.0127  -0.0057 418 ILE D N   
16064 C CA  . ILE D 418 ? 0.3355 0.2458 0.5585 0.0850  0.0111  -0.0079 418 ILE D CA  
16065 C C   . ILE D 418 ? 0.3378 0.2475 0.5658 0.0895  0.0086  -0.0031 418 ILE D C   
16066 O O   . ILE D 418 ? 0.3199 0.2449 0.5601 0.0904  0.0061  0.0019  418 ILE D O   
16067 C CB  . ILE D 418 ? 0.3254 0.2313 0.5424 0.0744  0.0066  -0.0107 418 ILE D CB  
16068 C CG1 . ILE D 418 ? 0.3203 0.2381 0.5463 0.0695  0.0011  -0.0067 418 ILE D CG1 
16069 C CG2 . ILE D 418 ? 0.3113 0.2193 0.5244 0.0702  0.0085  -0.0147 418 ILE D CG2 
16070 C CD1 . ILE D 418 ? 0.3137 0.2289 0.5349 0.0597  -0.0029 -0.0088 418 ILE D CD1 
16071 N N   . GLU D 419 ? 0.3623 0.2534 0.5800 0.0924  0.0093  -0.0045 419 GLU D N   
16072 C CA  . GLU D 419 ? 0.3775 0.2631 0.5961 0.0953  0.0064  -0.0004 419 GLU D CA  
16073 C C   . GLU D 419 ? 0.3909 0.2602 0.5976 0.0877  0.0031  -0.0030 419 GLU D C   
16074 O O   . GLU D 419 ? 0.4006 0.2543 0.5953 0.0862  0.0052  -0.0079 419 GLU D O   
16075 C CB  . GLU D 419 ? 0.3980 0.2735 0.6143 0.1067  0.0108  0.0008  419 GLU D CB  
16076 C CG  . GLU D 419 ? 0.4109 0.3017 0.6395 0.1162  0.0151  0.0042  419 GLU D CG  
16077 C CD  . GLU D 419 ? 0.4664 0.3434 0.6893 0.1279  0.0211  0.0036  419 GLU D CD  
16078 O OE1 . GLU D 419 ? 0.4882 0.3448 0.6960 0.1283  0.0242  -0.0018 419 GLU D OE1 
16079 O OE2 . GLU D 419 ? 0.4916 0.3782 0.7251 0.1371  0.0230  0.0087  419 GLU D OE2 
16080 N N   . VAL D 420 ? 0.3767 0.2499 0.5864 0.0827  -0.0022 0.0003  420 VAL D N   
16081 C CA  . VAL D 420 ? 0.3704 0.2319 0.5708 0.0744  -0.0054 -0.0014 420 VAL D CA  
16082 C C   . VAL D 420 ? 0.3769 0.2271 0.5736 0.0768  -0.0076 0.0024  420 VAL D C   
16083 O O   . VAL D 420 ? 0.3779 0.2359 0.5823 0.0816  -0.0092 0.0075  420 VAL D O   
16084 C CB  . VAL D 420 ? 0.3450 0.2200 0.5505 0.0657  -0.0092 -0.0011 420 VAL D CB  
16085 C CG1 . VAL D 420 ? 0.3516 0.2164 0.5485 0.0570  -0.0117 -0.0028 420 VAL D CG1 
16086 C CG2 . VAL D 420 ? 0.3325 0.2198 0.5430 0.0640  -0.0073 -0.0038 420 VAL D CG2 
16087 N N   . THR D 421 ? 0.4030 0.2345 0.5877 0.0732  -0.0078 0.0000  421 THR D N   
16088 C CA  . THR D 421 ? 0.4028 0.2206 0.5817 0.0739  -0.0099 0.0033  421 THR D CA  
16089 C C   . THR D 421 ? 0.4077 0.2217 0.5812 0.0629  -0.0134 0.0028  421 THR D C   
16090 O O   . THR D 421 ? 0.3980 0.2088 0.5666 0.0564  -0.0129 -0.0017 421 THR D O   
16091 C CB  . THR D 421 ? 0.4108 0.2075 0.5791 0.0796  -0.0063 0.0007  421 THR D CB  
16092 O OG1 . THR D 421 ? 0.3986 0.2024 0.5730 0.0893  -0.0021 0.0005  421 THR D OG1 
16093 C CG2 . THR D 421 ? 0.4241 0.2050 0.5864 0.0826  -0.0077 0.0045  421 THR D CG2 
16094 N N   . PRO D 422 ? 0.4342 0.2494 0.6086 0.0602  -0.0170 0.0075  422 PRO D N   
16095 C CA  . PRO D 422 ? 0.4392 0.2630 0.6211 0.0662  -0.0189 0.0133  422 PRO D CA  
16096 C C   . PRO D 422 ? 0.4285 0.2743 0.6224 0.0670  -0.0196 0.0140  422 PRO D C   
16097 O O   . PRO D 422 ? 0.4290 0.2839 0.6248 0.0602  -0.0202 0.0113  422 PRO D O   
16098 C CB  . PRO D 422 ? 0.4426 0.2616 0.6200 0.0605  -0.0227 0.0172  422 PRO D CB  
16099 C CG  . PRO D 422 ? 0.4444 0.2459 0.6107 0.0544  -0.0217 0.0140  422 PRO D CG  
16100 C CD  . PRO D 422 ? 0.4555 0.2619 0.6226 0.0513  -0.0194 0.0079  422 PRO D CD  
16101 N N   . GLU D 423 ? 0.4188 0.2723 0.6207 0.0755  -0.0195 0.0178  423 GLU D N   
16102 C CA  . GLU D 423 ? 0.4116 0.2852 0.6257 0.0777  -0.0198 0.0189  423 GLU D CA  
16103 C C   . GLU D 423 ? 0.3971 0.2836 0.6159 0.0720  -0.0250 0.0221  423 GLU D C   
16104 O O   . GLU D 423 ? 0.3921 0.2932 0.6178 0.0689  -0.0258 0.0211  423 GLU D O   
16105 C CB  . GLU D 423 ? 0.4248 0.3016 0.6459 0.0889  -0.0179 0.0225  423 GLU D CB  
16106 C CG  . GLU D 423 ? 0.4474 0.3459 0.6823 0.0912  -0.0182 0.0243  423 GLU D CG  
16107 C CD  . GLU D 423 ? 0.4741 0.3805 0.7190 0.1019  -0.0172 0.0296  423 GLU D CD  
16108 O OE1 . GLU D 423 ? 0.4523 0.3479 0.6942 0.1090  -0.0165 0.0324  423 GLU D OE1 
16109 O OE2 . GLU D 423 ? 0.5236 0.4483 0.7803 0.1030  -0.0173 0.0311  423 GLU D OE2 
16110 N N   . LYS D 424 ? 0.4183 0.2984 0.6324 0.0705  -0.0284 0.0260  424 LYS D N   
16111 C CA  . LYS D 424 ? 0.4535 0.3446 0.6709 0.0667  -0.0334 0.0297  424 LYS D CA  
16112 C C   . LYS D 424 ? 0.4331 0.3157 0.6409 0.0591  -0.0355 0.0299  424 LYS D C   
16113 O O   . LYS D 424 ? 0.4348 0.3259 0.6430 0.0534  -0.0383 0.0303  424 LYS D O   
16114 C CB  . LYS D 424 ? 0.5138 0.4095 0.7369 0.0739  -0.0364 0.0363  424 LYS D CB  
16115 C CG  . LYS D 424 ? 0.5750 0.4858 0.8108 0.0801  -0.0356 0.0376  424 LYS D CG  
16116 C CD  . LYS D 424 ? 0.6385 0.5547 0.8814 0.0881  -0.0384 0.0446  424 LYS D CD  
16117 C CE  . LYS D 424 ? 0.6610 0.5890 0.9158 0.0953  -0.0353 0.0450  424 LYS D CE  
16118 N NZ  . LYS D 424 ? 0.6915 0.6343 0.9574 0.0996  -0.0398 0.0520  424 LYS D NZ  
16119 N N   . ASP D 425 ? 0.4235 0.2891 0.6221 0.0589  -0.0341 0.0300  425 ASP D N   
16120 C CA  . ASP D 425 ? 0.4268 0.2854 0.6171 0.0519  -0.0359 0.0312  425 ASP D CA  
16121 C C   . ASP D 425 ? 0.4191 0.2627 0.6008 0.0474  -0.0329 0.0276  425 ASP D C   
16122 O O   . ASP D 425 ? 0.4535 0.2822 0.6299 0.0508  -0.0314 0.0281  425 ASP D O   
16123 C CB  . ASP D 425 ? 0.4249 0.2802 0.6130 0.0551  -0.0394 0.0378  425 ASP D CB  
16124 C CG  . ASP D 425 ? 0.4383 0.2863 0.6170 0.0482  -0.0409 0.0400  425 ASP D CG  
16125 O OD1 . ASP D 425 ? 0.4135 0.2587 0.5880 0.0410  -0.0390 0.0364  425 ASP D OD1 
16126 O OD2 . ASP D 425 ? 0.4912 0.3369 0.6672 0.0501  -0.0440 0.0455  425 ASP D OD2 
16127 N N   . LEU D 426 ? 0.4027 0.2493 0.5824 0.0393  -0.0323 0.0244  426 LEU D N   
16128 C CA  . LEU D 426 ? 0.4045 0.2394 0.5776 0.0342  -0.0300 0.0210  426 LEU D CA  
16129 C C   . LEU D 426 ? 0.4286 0.2473 0.5925 0.0320  -0.0306 0.0243  426 LEU D C   
16130 O O   . LEU D 426 ? 0.4363 0.2427 0.5943 0.0285  -0.0291 0.0219  426 LEU D O   
16131 C CB  . LEU D 426 ? 0.3784 0.2226 0.5529 0.0264  -0.0296 0.0179  426 LEU D CB  
16132 C CG  . LEU D 426 ? 0.3481 0.2061 0.5306 0.0278  -0.0288 0.0142  426 LEU D CG  
16133 C CD1 . LEU D 426 ? 0.3452 0.2097 0.5279 0.0201  -0.0283 0.0116  426 LEU D CD1 
16134 C CD2 . LEU D 426 ? 0.3381 0.1920 0.5217 0.0325  -0.0263 0.0108  426 LEU D CD2 
16135 N N   . ASN D 427 ? 0.4474 0.2657 0.6099 0.0338  -0.0331 0.0299  427 ASN D N   
16136 C CA  . ASN D 427 ? 0.4592 0.2618 0.6129 0.0320  -0.0337 0.0339  427 ASN D CA  
16137 C C   . ASN D 427 ? 0.5028 0.2892 0.6527 0.0387  -0.0326 0.0342  427 ASN D C   
16138 O O   . ASN D 427 ? 0.5403 0.3105 0.6818 0.0366  -0.0327 0.0364  427 ASN D O   
16139 C CB  . ASN D 427 ? 0.4421 0.2476 0.5940 0.0325  -0.0368 0.0402  427 ASN D CB  
16140 C CG  . ASN D 427 ? 0.4501 0.2660 0.6014 0.0250  -0.0374 0.0405  427 ASN D CG  
16141 O OD1 . ASN D 427 ? 0.4853 0.3116 0.6386 0.0262  -0.0399 0.0431  427 ASN D OD1 
16142 N ND2 . ASN D 427 ? 0.4275 0.2412 0.5760 0.0174  -0.0352 0.0379  427 ASN D ND2 
16143 N N   . GLU D 428 ? 0.5317 0.3219 0.6874 0.0469  -0.0315 0.0324  428 GLU D N   
16144 C CA  . GLU D 428 ? 0.5276 0.3027 0.6798 0.0547  -0.0298 0.0326  428 GLU D CA  
16145 C C   . GLU D 428 ? 0.5241 0.2846 0.6692 0.0518  -0.0268 0.0269  428 GLU D C   
16146 O O   . GLU D 428 ? 0.5556 0.3026 0.6966 0.0583  -0.0248 0.0258  428 GLU D O   
16147 C CB  . GLU D 428 ? 0.5779 0.3639 0.7396 0.0646  -0.0288 0.0325  428 GLU D CB  
16148 C CG  . GLU D 428 ? 0.6420 0.4440 0.8118 0.0676  -0.0324 0.0380  428 GLU D CG  
16149 C CD  . GLU D 428 ? 0.6951 0.5032 0.8732 0.0790  -0.0321 0.0409  428 GLU D CD  
16150 O OE1 . GLU D 428 ? 0.6986 0.5017 0.8777 0.0850  -0.0282 0.0376  428 GLU D OE1 
16151 O OE2 . GLU D 428 ? 0.7128 0.5304 0.8961 0.0819  -0.0359 0.0466  428 GLU D OE2 
16152 N N   . GLY D 429 ? 0.5236 0.2867 0.6669 0.0423  -0.0266 0.0232  429 GLY D N   
16153 C CA  . GLY D 429 ? 0.5062 0.2538 0.6412 0.0381  -0.0248 0.0186  429 GLY D CA  
16154 C C   . GLY D 429 ? 0.4907 0.2451 0.6259 0.0271  -0.0254 0.0158  429 GLY D C   
16155 O O   . GLY D 429 ? 0.4788 0.2512 0.6214 0.0243  -0.0262 0.0163  429 GLY D O   
16156 N N   . LYS D 430 ? 0.5128 0.2520 0.6394 0.0210  -0.0251 0.0131  430 LYS D N   
16157 C CA  . LYS D 430 ? 0.5186 0.2627 0.6452 0.0107  -0.0256 0.0103  430 LYS D CA  
16158 C C   . LYS D 430 ? 0.4718 0.2212 0.6004 0.0117  -0.0241 0.0039  430 LYS D C   
16159 O O   . LYS D 430 ? 0.4176 0.1766 0.5492 0.0048  -0.0246 0.0016  430 LYS D O   
16160 C CB  . LYS D 430 ? 0.5884 0.3139 0.7051 0.0030  -0.0268 0.0112  430 LYS D CB  
16161 C CG  . LYS D 430 ? 0.6622 0.3867 0.7777 -0.0016 -0.0283 0.0176  430 LYS D CG  
16162 C CD  . LYS D 430 ? 0.8185 0.5266 0.9253 -0.0112 -0.0294 0.0186  430 LYS D CD  
16163 C CE  . LYS D 430 ? 0.9127 0.6133 1.0155 -0.0137 -0.0304 0.0255  430 LYS D CE  
16164 N NZ  . LYS D 430 ? 0.9956 0.7157 1.1060 -0.0143 -0.0303 0.0294  430 LYS D NZ  
16165 N N   . ILE D 431 ? 0.4624 0.2058 0.5895 0.0207  -0.0220 0.0014  431 ILE D N   
16166 C CA  . ILE D 431 ? 0.4459 0.1905 0.5723 0.0221  -0.0201 -0.0045 431 ILE D CA  
16167 C C   . ILE D 431 ? 0.4216 0.1796 0.5565 0.0318  -0.0179 -0.0047 431 ILE D C   
16168 O O   . ILE D 431 ? 0.4181 0.1734 0.5545 0.0401  -0.0171 -0.0016 431 ILE D O   
16169 C CB  . ILE D 431 ? 0.4752 0.1960 0.5887 0.0232  -0.0190 -0.0081 431 ILE D CB  
16170 C CG1 . ILE D 431 ? 0.4829 0.1894 0.5878 0.0130  -0.0216 -0.0076 431 ILE D CG1 
16171 C CG2 . ILE D 431 ? 0.4842 0.2067 0.5959 0.0251  -0.0168 -0.0143 431 ILE D CG2 
16172 C CD1 . ILE D 431 ? 0.5085 0.1899 0.5992 0.0128  -0.0211 -0.0115 431 ILE D CD1 
16173 N N   . ALA D 432 ? 0.4086 0.1802 0.5488 0.0307  -0.0170 -0.0081 432 ALA D N   
16174 C CA  . ALA D 432 ? 0.4004 0.1860 0.5493 0.0387  -0.0148 -0.0082 432 ALA D CA  
16175 C C   . ALA D 432 ? 0.4034 0.1840 0.5480 0.0425  -0.0115 -0.0135 432 ALA D C   
16176 O O   . ALA D 432 ? 0.4218 0.1928 0.5581 0.0369  -0.0117 -0.0176 432 ALA D O   
16177 C CB  . ALA D 432 ? 0.3898 0.1967 0.5489 0.0346  -0.0164 -0.0072 432 ALA D CB  
16178 N N   . SER D 433 ? 0.4098 0.1978 0.5602 0.0518  -0.0085 -0.0132 433 SER D N   
16179 C CA  . SER D 433 ? 0.4166 0.2049 0.5647 0.0550  -0.0049 -0.0179 433 SER D CA  
16180 C C   . SER D 433 ? 0.4268 0.2369 0.5877 0.0590  -0.0035 -0.0165 433 SER D C   
16181 O O   . SER D 433 ? 0.4218 0.2435 0.5925 0.0624  -0.0045 -0.0119 433 SER D O   
16182 C CB  . SER D 433 ? 0.4231 0.1939 0.5621 0.0631  -0.0011 -0.0200 433 SER D CB  
16183 O OG  . SER D 433 ? 0.4217 0.1982 0.5682 0.0737  0.0013  -0.0162 433 SER D OG  
16184 N N   . ILE D 434 ? 0.4388 0.2535 0.5987 0.0581  -0.0012 -0.0206 434 ILE D N   
16185 C CA  . ILE D 434 ? 0.4167 0.2491 0.5868 0.0625  0.0011  -0.0198 434 ILE D CA  
16186 C C   . ILE D 434 ? 0.4449 0.2698 0.6089 0.0699  0.0067  -0.0232 434 ILE D C   
16187 O O   . ILE D 434 ? 0.4743 0.2887 0.6275 0.0667  0.0078  -0.0281 434 ILE D O   
16188 C CB  . ILE D 434 ? 0.4031 0.2488 0.5775 0.0543  -0.0011 -0.0210 434 ILE D CB  
16189 C CG1 . ILE D 434 ? 0.3913 0.2440 0.5710 0.0478  -0.0058 -0.0178 434 ILE D CG1 
16190 C CG2 . ILE D 434 ? 0.4071 0.2697 0.5908 0.0580  0.0015  -0.0205 434 ILE D CG2 
16191 C CD1 . ILE D 434 ? 0.4134 0.2751 0.5949 0.0394  -0.0079 -0.0194 434 ILE D CD1 
16192 N N   . LYS D 435 ? 0.4603 0.2906 0.6311 0.0799  0.0101  -0.0203 435 LYS D N   
16193 C CA  . LYS D 435 ? 0.4776 0.3037 0.6445 0.0884  0.0164  -0.0229 435 LYS D CA  
16194 C C   . LYS D 435 ? 0.4519 0.2987 0.6293 0.0888  0.0184  -0.0221 435 LYS D C   
16195 O O   . LYS D 435 ? 0.4493 0.3138 0.6406 0.0895  0.0167  -0.0173 435 LYS D O   
16196 C CB  . LYS D 435 ? 0.5039 0.3248 0.6731 0.0996  0.0194  -0.0196 435 LYS D CB  
16197 C CG  . LYS D 435 ? 0.5694 0.3658 0.7253 0.1000  0.0185  -0.0211 435 LYS D CG  
16198 C CD  . LYS D 435 ? 0.6308 0.4170 0.7856 0.1123  0.0224  -0.0188 435 LYS D CD  
16199 C CE  . LYS D 435 ? 0.6719 0.4696 0.8397 0.1154  0.0191  -0.0115 435 LYS D CE  
16200 N NZ  . LYS D 435 ? 0.7314 0.5129 0.8943 0.1245  0.0209  -0.0093 435 LYS D NZ  
16201 N N   . THR D 436 ? 0.4571 0.3015 0.6273 0.0877  0.0216  -0.0266 436 THR D N   
16202 C CA  . THR D 436 ? 0.4497 0.3128 0.6290 0.0875  0.0236  -0.0257 436 THR D CA  
16203 C C   . THR D 436 ? 0.4323 0.2960 0.6110 0.0979  0.0312  -0.0262 436 THR D C   
16204 O O   . THR D 436 ? 0.4162 0.2624 0.5808 0.1014  0.0350  -0.0307 436 THR D O   
16205 C CB  . THR D 436 ? 0.4348 0.2981 0.6079 0.0781  0.0214  -0.0295 436 THR D CB  
16206 O OG1 . THR D 436 ? 0.4214 0.2860 0.5970 0.0698  0.0151  -0.0282 436 THR D OG1 
16207 C CG2 . THR D 436 ? 0.4241 0.3061 0.6062 0.0773  0.0231  -0.0282 436 THR D CG2 
16208 N N   . LYS D 437 ? 0.4145 0.2983 0.6084 0.1022  0.0332  -0.0215 437 LYS D N   
16209 C CA  . LYS D 437 ? 0.4265 0.3164 0.6232 0.1115  0.0408  -0.0209 437 LYS D CA  
16210 C C   . LYS D 437 ? 0.4012 0.3091 0.6055 0.1075  0.0418  -0.0200 437 LYS D C   
16211 O O   . LYS D 437 ? 0.3837 0.3078 0.6004 0.1021  0.0374  -0.0163 437 LYS D O   
16212 C CB  . LYS D 437 ? 0.4486 0.3469 0.6581 0.1205  0.0420  -0.0151 437 LYS D CB  
16213 C CG  . LYS D 437 ? 0.4991 0.4055 0.7139 0.1314  0.0503  -0.0133 437 LYS D CG  
16214 C CD  . LYS D 437 ? 0.5392 0.4553 0.7680 0.1405  0.0510  -0.0068 437 LYS D CD  
16215 C CE  . LYS D 437 ? 0.5936 0.5268 0.8343 0.1495  0.0581  -0.0030 437 LYS D CE  
16216 N NZ  . LYS D 437 ? 0.6534 0.5923 0.9052 0.1602  0.0598  0.0028  437 LYS D NZ  
16217 N N   . ILE D 438 ? 0.3989 0.3022 0.5936 0.1094  0.0473  -0.0239 438 ILE D N   
16218 C CA  . ILE D 438 ? 0.3950 0.3144 0.5959 0.1070  0.0496  -0.0226 438 ILE D CA  
16219 C C   . ILE D 438 ? 0.4160 0.3420 0.6205 0.1177  0.0585  -0.0209 438 ILE D C   
16220 O O   . ILE D 438 ? 0.4552 0.3664 0.6460 0.1238  0.0644  -0.0251 438 ILE D O   
16221 C CB  . ILE D 438 ? 0.3937 0.3042 0.5806 0.0992  0.0484  -0.0280 438 ILE D CB  
16222 C CG1 . ILE D 438 ? 0.3904 0.2947 0.5740 0.0890  0.0401  -0.0296 438 ILE D CG1 
16223 C CG2 . ILE D 438 ? 0.3744 0.3013 0.5675 0.0973  0.0511  -0.0262 438 ILE D CG2 
16224 C CD1 . ILE D 438 ? 0.3949 0.2888 0.5640 0.0819  0.0385  -0.0348 438 ILE D CD1 
16225 N N   . GLU D 439 ? 0.4313 0.3795 0.6538 0.1198  0.0597  -0.0148 439 GLU D N   
16226 C CA  . GLU D 439 ? 0.4572 0.4163 0.6853 0.1285  0.0684  -0.0123 439 GLU D CA  
16227 C C   . GLU D 439 ? 0.4602 0.4263 0.6851 0.1232  0.0708  -0.0136 439 GLU D C   
16228 O O   . GLU D 439 ? 0.4489 0.4282 0.6829 0.1148  0.0659  -0.0110 439 GLU D O   
16229 C CB  . GLU D 439 ? 0.4813 0.4624 0.7313 0.1328  0.0684  -0.0044 439 GLU D CB  
16230 C CG  . GLU D 439 ? 0.5432 0.5191 0.7975 0.1369  0.0646  -0.0022 439 GLU D CG  
16231 C CD  . GLU D 439 ? 0.6162 0.6065 0.8864 0.1474  0.0685  0.0044  439 GLU D CD  
16232 O OE1 . GLU D 439 ? 0.6940 0.7001 0.9732 0.1517  0.0747  0.0075  439 GLU D OE1 
16233 O OE2 . GLU D 439 ? 0.6602 0.6454 0.9332 0.1517  0.0656  0.0065  439 GLU D OE2 
16234 N N   . THR D 440 ? 0.4747 0.4304 0.6854 0.1279  0.0780  -0.0179 440 THR D N   
16235 C CA  . THR D 440 ? 0.4672 0.4277 0.6726 0.1231  0.0804  -0.0192 440 THR D CA  
16236 C C   . THR D 440 ? 0.4676 0.4509 0.6885 0.1274  0.0865  -0.0130 440 THR D C   
16237 O O   . THR D 440 ? 0.4492 0.4424 0.6824 0.1360  0.0907  -0.0086 440 THR D O   
16238 C CB  . THR D 440 ? 0.4872 0.4270 0.6695 0.1257  0.0854  -0.0263 440 THR D CB  
16239 O OG1 . THR D 440 ? 0.4700 0.4047 0.6500 0.1383  0.0938  -0.0264 440 THR D OG1 
16240 C CG2 . THR D 440 ? 0.4988 0.4175 0.6655 0.1188  0.0785  -0.0323 440 THR D CG2 
16241 N N   . SER D 441 ? 0.4660 0.4572 0.6860 0.1214  0.0873  -0.0125 441 SER D N   
16242 C CA  . SER D 441 ? 0.4808 0.4932 0.7142 0.1241  0.0933  -0.0066 441 SER D CA  
16243 C C   . SER D 441 ? 0.4978 0.5063 0.7175 0.1214  0.0977  -0.0095 441 SER D C   
16244 O O   . SER D 441 ? 0.5128 0.5125 0.7222 0.1125  0.0920  -0.0130 441 SER D O   
16245 C CB  . SER D 441 ? 0.5095 0.5417 0.7632 0.1167  0.0864  -0.0002 441 SER D CB  
16246 O OG  . SER D 441 ? 0.5354 0.5885 0.8080 0.1223  0.0908  0.0070  441 SER D OG  
16247 N N   . GLU D 442 ? 0.5476 0.5626 0.7670 0.1293  0.1079  -0.0078 442 GLU D N   
16248 C CA  . GLU D 442 ? 0.6322 0.6453 0.8389 0.1274  0.1131  -0.0097 442 GLU D CA  
16249 C C   . GLU D 442 ? 0.6634 0.6910 0.8794 0.1165  0.1078  -0.0055 442 GLU D C   
16250 O O   . GLU D 442 ? 0.6275 0.6736 0.8637 0.1134  0.1047  0.0009  442 GLU D O   
16251 C CB  . GLU D 442 ? 0.7103 0.7298 0.9167 0.1387  0.1259  -0.0077 442 GLU D CB  
16252 C CG  . GLU D 442 ? 0.7247 0.7720 0.9557 0.1412  0.1297  0.0015  442 GLU D CG  
16253 C CD  . GLU D 442 ? 0.8534 0.9082 1.0871 0.1543  0.1427  0.0040  442 GLU D CD  
16254 O OE1 . GLU D 442 ? 0.9133 0.9504 1.1271 0.1615  0.1497  -0.0019 442 GLU D OE1 
16255 O OE2 . GLU D 442 ? 0.8458 0.9240 1.1015 0.1575  0.1459  0.0120  442 GLU D OE2 
16256 N N   . ASN D 443 ? 0.6499 0.6676 0.8500 0.1104  0.1065  -0.0093 443 ASN D N   
16257 C CA  . ASN D 443 ? 0.5815 0.6093 0.7865 0.1005  0.1021  -0.0060 443 ASN D CA  
16258 C C   . ASN D 443 ? 0.5312 0.5514 0.7356 0.0913  0.0906  -0.0084 443 ASN D C   
16259 O O   . ASN D 443 ? 0.4755 0.4959 0.6763 0.0832  0.0863  -0.0082 443 ASN D O   
16260 C CB  . ASN D 443 ? 0.6064 0.6587 0.8329 0.1000  0.1047  0.0025  443 ASN D CB  
16261 C CG  . ASN D 443 ? 0.6736 0.7349 0.9017 0.1094  0.1167  0.0053  443 ASN D CG  
16262 O OD1 . ASN D 443 ? 0.7018 0.7788 0.9474 0.1149  0.1204  0.0108  443 ASN D OD1 
16263 N ND2 . ASN D 443 ? 0.6929 0.7442 0.9024 0.1116  0.1230  0.0017  443 ASN D ND2 
16264 N N   . PHE D 444 ? 0.5094 0.5229 0.7168 0.0928  0.0860  -0.0103 444 PHE D N   
16265 C CA  . PHE D 444 ? 0.4356 0.4411 0.6413 0.0847  0.0759  -0.0128 444 PHE D CA  
16266 C C   . PHE D 444 ? 0.4565 0.4395 0.6419 0.0853  0.0747  -0.0202 444 PHE D C   
16267 O O   . PHE D 444 ? 0.4691 0.4420 0.6482 0.0928  0.0786  -0.0230 444 PHE D O   
16268 C CB  . PHE D 444 ? 0.4093 0.4223 0.6312 0.0842  0.0706  -0.0096 444 PHE D CB  
16269 C CG  . PHE D 444 ? 0.3847 0.4192 0.6267 0.0818  0.0698  -0.0023 444 PHE D CG  
16270 C CD1 . PHE D 444 ? 0.4031 0.4520 0.6566 0.0885  0.0768  0.0026  444 PHE D CD1 
16271 C CD2 . PHE D 444 ? 0.3678 0.4079 0.6169 0.0726  0.0621  -0.0003 444 PHE D CD2 
16272 C CE1 . PHE D 444 ? 0.3930 0.4618 0.6650 0.0854  0.0755  0.0095  444 PHE D CE1 
16273 C CE2 . PHE D 444 ? 0.3615 0.4196 0.6276 0.0697  0.0609  0.0061  444 PHE D CE2 
16274 C CZ  . PHE D 444 ? 0.3736 0.4462 0.6513 0.0756  0.0672  0.0110  444 PHE D CZ  
16275 N N   . THR D 445 ? 0.4455 0.4211 0.6215 0.0770  0.0687  -0.0229 445 THR D N   
16276 C CA  . THR D 445 ? 0.4568 0.4123 0.6136 0.0752  0.0662  -0.0295 445 THR D CA  
16277 C C   . THR D 445 ? 0.4695 0.4195 0.6297 0.0696  0.0573  -0.0308 445 THR D C   
16278 O O   . THR D 445 ? 0.4361 0.3945 0.6054 0.0626  0.0512  -0.0282 445 THR D O   
16279 C CB  . THR D 445 ? 0.4548 0.4080 0.5995 0.0701  0.0660  -0.0308 445 THR D CB  
16280 O OG1 . THR D 445 ? 0.4534 0.4096 0.5938 0.0772  0.0757  -0.0300 445 THR D OG1 
16281 C CG2 . THR D 445 ? 0.4733 0.4073 0.5984 0.0661  0.0619  -0.0371 445 THR D CG2 
16282 N N   . LEU D 446 ? 0.4763 0.4112 0.6280 0.0727  0.0568  -0.0349 446 LEU D N   
16283 C CA  . LEU D 446 ? 0.4785 0.4059 0.6306 0.0672  0.0489  -0.0365 446 LEU D CA  
16284 C C   . LEU D 446 ? 0.5228 0.4398 0.6607 0.0597  0.0442  -0.0404 446 LEU D C   
16285 O O   . LEU D 446 ? 0.5805 0.4871 0.7027 0.0612  0.0474  -0.0442 446 LEU D O   
16286 C CB  . LEU D 446 ? 0.4754 0.3905 0.6240 0.0729  0.0499  -0.0388 446 LEU D CB  
16287 C CG  . LEU D 446 ? 0.4695 0.3939 0.6306 0.0820  0.0554  -0.0350 446 LEU D CG  
16288 C CD1 . LEU D 446 ? 0.4769 0.3862 0.6312 0.0887  0.0574  -0.0377 446 LEU D CD1 
16289 C CD2 . LEU D 446 ? 0.4445 0.3866 0.6257 0.0792  0.0513  -0.0292 446 LEU D CD2 
16290 N N   . LEU D 447 ? 0.5315 0.4521 0.6751 0.0519  0.0367  -0.0393 447 LEU D N   
16291 C CA  . LEU D 447 ? 0.6391 0.5515 0.7716 0.0446  0.0314  -0.0423 447 LEU D CA  
16292 C C   . LEU D 447 ? 0.7804 0.6790 0.9065 0.0414  0.0262  -0.0457 447 LEU D C   
16293 O O   . LEU D 447 ? 0.8792 0.7758 1.0115 0.0437  0.0256  -0.0451 447 LEU D O   
16294 C CB  . LEU D 447 ? 0.5949 0.5209 0.7380 0.0384  0.0269  -0.0384 447 LEU D CB  
16295 C CG  . LEU D 447 ? 0.6219 0.5607 0.7704 0.0400  0.0312  -0.0348 447 LEU D CG  
16296 C CD1 . LEU D 447 ? 0.6159 0.5647 0.7731 0.0334  0.0259  -0.0315 447 LEU D CD1 
16297 C CD2 . LEU D 447 ? 0.6820 0.6137 0.8147 0.0420  0.0359  -0.0374 447 LEU D CD2 
16298 N N   . ASP D 448 ? 0.8586 0.7476 0.9718 0.0356  0.0223  -0.0489 448 ASP D N   
16299 C CA  . ASP D 448 ? 0.8529 0.7327 0.9621 0.0293  0.0156  -0.0510 448 ASP D CA  
16300 C C   . ASP D 448 ? 0.6929 0.5648 0.8042 0.0330  0.0164  -0.0518 448 ASP D C   
16301 O O   . ASP D 448 ? 0.6868 0.5511 0.7926 0.0401  0.0219  -0.0535 448 ASP D O   
16302 C CB  . ASP D 448 ? 0.8033 0.6947 0.9232 0.0221  0.0094  -0.0477 448 ASP D CB  
16303 C CG  . ASP D 448 ? 0.7554 0.6545 0.8737 0.0185  0.0080  -0.0464 448 ASP D CG  
16304 O OD1 . ASP D 448 ? 0.7295 0.6204 0.8334 0.0173  0.0084  -0.0493 448 ASP D OD1 
16305 O OD2 . ASP D 448 ? 0.7281 0.6407 0.8591 0.0166  0.0063  -0.0423 448 ASP D OD2 
16306 N N   . ASP D 449 ? 0.7056 0.5803 0.8256 0.0285  0.0111  -0.0499 449 ASP D N   
16307 C CA  . ASP D 449 ? 0.7437 0.6084 0.8632 0.0293  0.0098  -0.0508 449 ASP D CA  
16308 C C   . ASP D 449 ? 0.6103 0.4870 0.7462 0.0331  0.0108  -0.0463 449 ASP D C   
16309 O O   . ASP D 449 ? 0.4687 0.3602 0.6164 0.0308  0.0091  -0.0429 449 ASP D O   
16310 C CB  . ASP D 449 ? 0.7381 0.5963 0.8543 0.0208  0.0030  -0.0518 449 ASP D CB  
16311 C CG  . ASP D 449 ? 0.8653 0.7069 0.9638 0.0164  0.0006  -0.0565 449 ASP D CG  
16312 O OD1 . ASP D 449 ? 0.8693 0.7039 0.9557 0.0194  0.0042  -0.0597 449 ASP D OD1 
16313 O OD2 . ASP D 449 ? 0.9269 0.7626 1.0234 0.0096  -0.0048 -0.0570 449 ASP D OD2 
16314 N N   . LEU D 450 ? 0.5800 0.4487 0.7149 0.0391  0.0137  -0.0467 450 LEU D N   
16315 C CA  . LEU D 450 ? 0.5118 0.3865 0.6589 0.0413  0.0128  -0.0431 450 LEU D CA  
16316 C C   . LEU D 450 ? 0.4490 0.3230 0.5986 0.0335  0.0063  -0.0423 450 LEU D C   
16317 O O   . LEU D 450 ? 0.4548 0.3158 0.5939 0.0290  0.0036  -0.0452 450 LEU D O   
16318 C CB  . LEU D 450 ? 0.4903 0.3519 0.6313 0.0489  0.0167  -0.0445 450 LEU D CB  
16319 C CG  . LEU D 450 ? 0.4812 0.3459 0.6326 0.0522  0.0158  -0.0407 450 LEU D CG  
16320 C CD1 . LEU D 450 ? 0.4675 0.3524 0.6353 0.0550  0.0169  -0.0359 450 LEU D CD1 
16321 C CD2 . LEU D 450 ? 0.5075 0.3576 0.6515 0.0600  0.0197  -0.0422 450 LEU D CD2 
16322 N N   . LYS D 451 ? 0.4049 0.2920 0.5677 0.0319  0.0040  -0.0383 451 LYS D N   
16323 C CA  . LYS D 451 ? 0.4237 0.3104 0.5893 0.0256  -0.0011 -0.0372 451 LYS D CA  
16324 C C   . LYS D 451 ? 0.4096 0.2964 0.5817 0.0287  -0.0014 -0.0343 451 LYS D C   
16325 O O   . LYS D 451 ? 0.3840 0.2789 0.5641 0.0343  0.0010  -0.0318 451 LYS D O   
16326 C CB  . LYS D 451 ? 0.4376 0.3375 0.6106 0.0202  -0.0040 -0.0354 451 LYS D CB  
16327 C CG  . LYS D 451 ? 0.5226 0.4198 0.6872 0.0164  -0.0047 -0.0381 451 LYS D CG  
16328 C CD  . LYS D 451 ? 0.5902 0.4980 0.7606 0.0106  -0.0081 -0.0365 451 LYS D CD  
16329 C CE  . LYS D 451 ? 0.6424 0.5514 0.8069 0.0092  -0.0077 -0.0380 451 LYS D CE  
16330 N NZ  . LYS D 451 ? 0.6265 0.5483 0.7994 0.0064  -0.0097 -0.0353 451 LYS D NZ  
16331 N N   . ILE D 452 ? 0.4052 0.2830 0.5736 0.0246  -0.0046 -0.0345 452 ILE D N   
16332 C CA  . ILE D 452 ? 0.4222 0.2975 0.5943 0.0266  -0.0054 -0.0318 452 ILE D CA  
16333 C C   . ILE D 452 ? 0.4068 0.2861 0.5829 0.0196  -0.0098 -0.0298 452 ILE D C   
16334 O O   . ILE D 452 ? 0.4479 0.3232 0.6193 0.0132  -0.0122 -0.0314 452 ILE D O   
16335 C CB  . ILE D 452 ? 0.4511 0.3081 0.6128 0.0294  -0.0042 -0.0338 452 ILE D CB  
16336 C CG1 . ILE D 452 ? 0.4760 0.3253 0.6296 0.0354  0.0003  -0.0371 452 ILE D CG1 
16337 C CG2 . ILE D 452 ? 0.4511 0.3065 0.6174 0.0332  -0.0045 -0.0302 452 ILE D CG2 
16338 C CD1 . ILE D 452 ? 0.4861 0.3433 0.6469 0.0446  0.0048  -0.0350 452 ILE D CD1 
16339 N N   . SER D 453 ? 0.3795 0.2661 0.5639 0.0210  -0.0107 -0.0262 453 SER D N   
16340 C CA  . SER D 453 ? 0.3388 0.2298 0.5269 0.0153  -0.0139 -0.0241 453 SER D CA  
16341 C C   . SER D 453 ? 0.3207 0.2075 0.5097 0.0176  -0.0146 -0.0212 453 SER D C   
16342 O O   . SER D 453 ? 0.3025 0.1940 0.4965 0.0232  -0.0135 -0.0192 453 SER D O   
16343 C CB  . SER D 453 ? 0.3250 0.2315 0.5221 0.0141  -0.0146 -0.0226 453 SER D CB  
16344 O OG  . SER D 453 ? 0.3082 0.2189 0.5086 0.0100  -0.0171 -0.0204 453 SER D OG  
16345 N N   . TYR D 454 ? 0.3268 0.2061 0.5117 0.0129  -0.0167 -0.0204 454 TYR D N   
16346 C CA  . TYR D 454 ? 0.3298 0.2067 0.5159 0.0136  -0.0178 -0.0169 454 TYR D CA  
16347 C C   . TYR D 454 ? 0.3385 0.2230 0.5281 0.0075  -0.0199 -0.0150 454 TYR D C   
16348 O O   . TYR D 454 ? 0.3343 0.2125 0.5198 0.0022  -0.0211 -0.0146 454 TYR D O   
16349 C CB  . TYR D 454 ? 0.3314 0.1910 0.5085 0.0141  -0.0176 -0.0173 454 TYR D CB  
16350 C CG  . TYR D 454 ? 0.3328 0.1883 0.5104 0.0175  -0.0182 -0.0135 454 TYR D CG  
16351 C CD1 . TYR D 454 ? 0.3410 0.1978 0.5217 0.0256  -0.0168 -0.0119 454 TYR D CD1 
16352 C CD2 . TYR D 454 ? 0.3340 0.1842 0.5088 0.0126  -0.0201 -0.0110 454 TYR D CD2 
16353 C CE1 . TYR D 454 ? 0.3315 0.1849 0.5128 0.0289  -0.0178 -0.0078 454 TYR D CE1 
16354 C CE2 . TYR D 454 ? 0.3345 0.1807 0.5090 0.0156  -0.0208 -0.0071 454 TYR D CE2 
16355 C CZ  . TYR D 454 ? 0.3385 0.1860 0.5160 0.0239  -0.0199 -0.0055 454 TYR D CZ  
16356 O OH  . TYR D 454 ? 0.3331 0.1761 0.5099 0.0270  -0.0210 -0.0012 454 TYR D OH  
16357 N N   . ASN D 455 ? 0.3104 0.2078 0.5073 0.0084  -0.0202 -0.0136 455 ASN D N   
16358 C CA  . ASN D 455 ? 0.3053 0.2105 0.5053 0.0035  -0.0215 -0.0124 455 ASN D CA  
16359 C C   . ASN D 455 ? 0.2933 0.1971 0.4928 0.0031  -0.0225 -0.0089 455 ASN D C   
16360 O O   . ASN D 455 ? 0.2625 0.1713 0.4651 0.0065  -0.0231 -0.0071 455 ASN D O   
16361 C CB  . ASN D 455 ? 0.3098 0.2275 0.5161 0.0041  -0.0213 -0.0130 455 ASN D CB  
16362 C CG  . ASN D 455 ? 0.3115 0.2359 0.5202 -0.0004 -0.0221 -0.0121 455 ASN D CG  
16363 O OD1 . ASN D 455 ? 0.3068 0.2283 0.5133 -0.0034 -0.0225 -0.0104 455 ASN D OD1 
16364 N ND2 . ASN D 455 ? 0.2848 0.2181 0.4978 -0.0006 -0.0219 -0.0131 455 ASN D ND2 
16365 N N   . THR D 456 ? 0.2957 0.1935 0.4912 -0.0017 -0.0230 -0.0079 456 THR D N   
16366 C CA  . THR D 456 ? 0.2959 0.1887 0.4884 -0.0024 -0.0236 -0.0045 456 THR D CA  
16367 C C   . THR D 456 ? 0.2988 0.2009 0.4941 -0.0048 -0.0238 -0.0024 456 THR D C   
16368 O O   . THR D 456 ? 0.3051 0.2043 0.4975 -0.0053 -0.0242 0.0007  456 THR D O   
16369 C CB  . THR D 456 ? 0.3191 0.2005 0.5057 -0.0069 -0.0238 -0.0043 456 THR D CB  
16370 O OG1 . THR D 456 ? 0.3274 0.2127 0.5153 -0.0119 -0.0238 -0.0065 456 THR D OG1 
16371 C CG2 . THR D 456 ? 0.3258 0.1939 0.5070 -0.0033 -0.0236 -0.0055 456 THR D CG2 
16372 N N   . HIS D 457 ? 0.2750 0.1870 0.4748 -0.0062 -0.0233 -0.0042 457 HIS D N   
16373 C CA  . HIS D 457 ? 0.2758 0.1965 0.4780 -0.0068 -0.0231 -0.0030 457 HIS D CA  
16374 C C   . HIS D 457 ? 0.2793 0.2000 0.4795 -0.0115 -0.0221 -0.0009 457 HIS D C   
16375 O O   . HIS D 457 ? 0.2724 0.1961 0.4714 -0.0115 -0.0217 0.0010  457 HIS D O   
16376 C CB  . HIS D 457 ? 0.2763 0.1979 0.4781 -0.0028 -0.0244 -0.0013 457 HIS D CB  
16377 C CG  . HIS D 457 ? 0.2768 0.2039 0.4831 0.0010  -0.0251 -0.0030 457 HIS D CG  
16378 N ND1 . HIS D 457 ? 0.2935 0.2284 0.5026 0.0017  -0.0258 -0.0032 457 HIS D ND1 
16379 C CD2 . HIS D 457 ? 0.2825 0.2080 0.4907 0.0042  -0.0249 -0.0043 457 HIS D CD2 
16380 C CE1 . HIS D 457 ? 0.2835 0.2221 0.4968 0.0046  -0.0263 -0.0043 457 HIS D CE1 
16381 N NE2 . HIS D 457 ? 0.2908 0.2243 0.5038 0.0065  -0.0255 -0.0050 457 HIS D NE2 
16382 N N   . LEU D 458 ? 0.3035 0.2206 0.5029 -0.0158 -0.0218 -0.0009 458 LEU D N   
16383 C CA  . LEU D 458 ? 0.3302 0.2488 0.5292 -0.0208 -0.0206 0.0016  458 LEU D CA  
16384 C C   . LEU D 458 ? 0.3091 0.2393 0.5135 -0.0222 -0.0191 0.0009  458 LEU D C   
16385 O O   . LEU D 458 ? 0.3337 0.2676 0.5417 -0.0244 -0.0193 -0.0005 458 LEU D O   
16386 C CB  . LEU D 458 ? 0.3454 0.2558 0.5419 -0.0254 -0.0213 0.0021  458 LEU D CB  
16387 C CG  . LEU D 458 ? 0.3989 0.2958 0.5893 -0.0235 -0.0225 0.0026  458 LEU D CG  
16388 C CD1 . LEU D 458 ? 0.3767 0.2636 0.5632 -0.0290 -0.0234 0.0031  458 LEU D CD1 
16389 C CD2 . LEU D 458 ? 0.3993 0.2929 0.5861 -0.0207 -0.0224 0.0059  458 LEU D CD2 
16390 N N   . GLY D 459 ? 0.3199 0.2556 0.5244 -0.0205 -0.0177 0.0020  459 GLY D N   
16391 C CA  . GLY D 459 ? 0.3332 0.2786 0.5424 -0.0201 -0.0162 0.0008  459 GLY D CA  
16392 C C   . GLY D 459 ? 0.3179 0.2655 0.5305 -0.0177 -0.0176 -0.0025 459 GLY D C   
16393 O O   . GLY D 459 ? 0.2711 0.2152 0.4822 -0.0144 -0.0191 -0.0038 459 GLY D O   
16394 N N   . TRP D 460 ? 0.3206 0.2745 0.5381 -0.0195 -0.0172 -0.0033 460 TRP D N   
16395 C CA  . TRP D 460 ? 0.3022 0.2587 0.5226 -0.0180 -0.0184 -0.0060 460 TRP D CA  
16396 C C   . TRP D 460 ? 0.3096 0.2607 0.5288 -0.0198 -0.0202 -0.0073 460 TRP D C   
16397 O O   . TRP D 460 ? 0.3097 0.2623 0.5303 -0.0187 -0.0210 -0.0094 460 TRP D O   
16398 C CB  . TRP D 460 ? 0.2945 0.2601 0.5203 -0.0187 -0.0172 -0.0059 460 TRP D CB  
16399 C CG  . TRP D 460 ? 0.2828 0.2530 0.5091 -0.0162 -0.0150 -0.0053 460 TRP D CG  
16400 C CD1 . TRP D 460 ? 0.2774 0.2521 0.5048 -0.0171 -0.0123 -0.0031 460 TRP D CD1 
16401 C CD2 . TRP D 460 ? 0.2611 0.2308 0.4859 -0.0124 -0.0152 -0.0070 460 TRP D CD2 
16402 N NE1 . TRP D 460 ? 0.2940 0.2698 0.5195 -0.0137 -0.0107 -0.0037 460 TRP D NE1 
16403 C CE2 . TRP D 460 ? 0.2692 0.2418 0.4930 -0.0111 -0.0127 -0.0062 460 TRP D CE2 
16404 C CE3 . TRP D 460 ? 0.2927 0.2602 0.5170 -0.0101 -0.0171 -0.0089 460 TRP D CE3 
16405 C CZ2 . TRP D 460 ? 0.2865 0.2584 0.5079 -0.0082 -0.0126 -0.0076 460 TRP D CZ2 
16406 C CZ3 . TRP D 460 ? 0.2910 0.2589 0.5140 -0.0075 -0.0171 -0.0098 460 TRP D CZ3 
16407 C CH2 . TRP D 460 ? 0.2895 0.2590 0.5107 -0.0068 -0.0152 -0.0094 460 TRP D CH2 
16408 N N   . ALA D 461 ? 0.3090 0.2530 0.5247 -0.0228 -0.0208 -0.0061 461 ALA D N   
16409 C CA  . ALA D 461 ? 0.3476 0.2843 0.5603 -0.0247 -0.0225 -0.0078 461 ALA D CA  
16410 C C   . ALA D 461 ? 0.3772 0.3082 0.5869 -0.0197 -0.0228 -0.0101 461 ALA D C   
16411 O O   . ALA D 461 ? 0.3756 0.3046 0.5841 -0.0162 -0.0223 -0.0092 461 ALA D O   
16412 C CB  . ALA D 461 ? 0.3274 0.2565 0.5364 -0.0293 -0.0231 -0.0058 461 ALA D CB  
16413 N N   . ILE D 462 ? 0.3739 0.3028 0.5824 -0.0193 -0.0236 -0.0127 462 ILE D N   
16414 C CA  . ILE D 462 ? 0.4083 0.3342 0.6152 -0.0140 -0.0231 -0.0146 462 ILE D CA  
16415 C C   . ILE D 462 ? 0.3850 0.2983 0.5855 -0.0128 -0.0232 -0.0153 462 ILE D C   
16416 O O   . ILE D 462 ? 0.3807 0.2914 0.5803 -0.0077 -0.0224 -0.0163 462 ILE D O   
16417 C CB  . ILE D 462 ? 0.4561 0.3866 0.6647 -0.0131 -0.0232 -0.0169 462 ILE D CB  
16418 C CG1 . ILE D 462 ? 0.5068 0.4325 0.7113 -0.0174 -0.0245 -0.0185 462 ILE D CG1 
16419 C CG2 . ILE D 462 ? 0.4322 0.3742 0.6470 -0.0131 -0.0229 -0.0161 462 ILE D CG2 
16420 C CD1 . ILE D 462 ? 0.5728 0.4990 0.7755 -0.0157 -0.0245 -0.0212 462 ILE D CD1 
16421 N N   . GLY D 463 ? 0.3957 0.3011 0.5919 -0.0173 -0.0242 -0.0148 463 GLY D N   
16422 C CA  . GLY D 463 ? 0.3886 0.2799 0.5775 -0.0161 -0.0243 -0.0154 463 GLY D CA  
16423 C C   . GLY D 463 ? 0.3934 0.2772 0.5767 -0.0162 -0.0246 -0.0191 463 GLY D C   
16424 O O   . GLY D 463 ? 0.4457 0.3356 0.6306 -0.0182 -0.0252 -0.0207 463 GLY D O   
16425 N N   . SER D 464 ? 0.4039 0.2739 0.5799 -0.0137 -0.0241 -0.0203 464 SER D N   
16426 C CA  . SER D 464 ? 0.4262 0.2861 0.5943 -0.0131 -0.0239 -0.0241 464 SER D CA  
16427 C C   . SER D 464 ? 0.4232 0.2901 0.5938 -0.0074 -0.0218 -0.0261 464 SER D C   
16428 O O   . SER D 464 ? 0.3814 0.2555 0.5579 -0.0019 -0.0202 -0.0246 464 SER D O   
16429 C CB  . SER D 464 ? 0.4419 0.2851 0.6017 -0.0102 -0.0232 -0.0247 464 SER D CB  
16430 O OG  . SER D 464 ? 0.4756 0.3106 0.6321 -0.0160 -0.0252 -0.0227 464 SER D OG  
16431 N N   . GLN D 465 ? 0.4363 0.3003 0.6016 -0.0092 -0.0222 -0.0294 465 GLN D N   
16432 C CA  . GLN D 465 ? 0.4256 0.2923 0.5900 -0.0039 -0.0197 -0.0318 465 GLN D CA  
16433 C C   . GLN D 465 ? 0.4450 0.2962 0.5968 -0.0033 -0.0190 -0.0358 465 GLN D C   
16434 O O   . GLN D 465 ? 0.4664 0.3068 0.6108 -0.0090 -0.0215 -0.0370 465 GLN D O   
16435 C CB  . GLN D 465 ? 0.4038 0.2838 0.5736 -0.0062 -0.0205 -0.0318 465 GLN D CB  
16436 C CG  . GLN D 465 ? 0.4054 0.2995 0.5863 -0.0065 -0.0210 -0.0284 465 GLN D CG  
16437 C CD  . GLN D 465 ? 0.4114 0.3172 0.5970 -0.0083 -0.0216 -0.0284 465 GLN D CD  
16438 O OE1 . GLN D 465 ? 0.4614 0.3719 0.6491 -0.0136 -0.0240 -0.0276 465 GLN D OE1 
16439 N NE2 . GLN D 465 ? 0.4090 0.3195 0.5963 -0.0037 -0.0194 -0.0291 465 GLN D NE2 
16440 N N   . ALA D 466 ? 0.4233 0.2733 0.5726 0.0035  -0.0154 -0.0377 466 ALA D N   
16441 C CA  . ALA D 466 ? 0.4349 0.2710 0.5712 0.0042  -0.0143 -0.0421 466 ALA D CA  
16442 C C   . ALA D 466 ? 0.4149 0.2582 0.5513 0.0084  -0.0112 -0.0436 466 ALA D C   
16443 O O   . ALA D 466 ? 0.4121 0.2677 0.5580 0.0133  -0.0088 -0.0414 466 ALA D O   
16444 C CB  . ALA D 466 ? 0.4581 0.2776 0.5867 0.0093  -0.0120 -0.0432 466 ALA D CB  
16445 N N   . SER D 467 ? 0.4523 0.2878 0.5776 0.0057  -0.0118 -0.0474 467 SER D N   
16446 C CA  . SER D 467 ? 0.4901 0.3279 0.6111 0.0096  -0.0085 -0.0496 467 SER D CA  
16447 C C   . SER D 467 ? 0.5019 0.3214 0.6086 0.0146  -0.0049 -0.0536 467 SER D C   
16448 O O   . SER D 467 ? 0.5339 0.3375 0.6291 0.0104  -0.0075 -0.0564 467 SER D O   
16449 C CB  . SER D 467 ? 0.5154 0.3574 0.6329 0.0027  -0.0119 -0.0507 467 SER D CB  
16450 O OG  . SER D 467 ? 0.5421 0.4025 0.6729 0.0009  -0.0134 -0.0471 467 SER D OG  
16451 N N   . VAL D 468 ? 0.4918 0.3135 0.5993 0.0235  0.0009  -0.0538 468 VAL D N   
16452 C CA  . VAL D 468 ? 0.5101 0.3149 0.6047 0.0300  0.0055  -0.0574 468 VAL D CA  
16453 C C   . VAL D 468 ? 0.5179 0.3256 0.6068 0.0342  0.0102  -0.0596 468 VAL D C   
16454 O O   . VAL D 468 ? 0.5026 0.3267 0.6026 0.0380  0.0131  -0.0566 468 VAL D O   
16455 C CB  . VAL D 468 ? 0.5055 0.3092 0.6070 0.0381  0.0088  -0.0548 468 VAL D CB  
16456 C CG1 . VAL D 468 ? 0.5034 0.2892 0.5921 0.0463  0.0142  -0.0583 468 VAL D CG1 
16457 C CG2 . VAL D 468 ? 0.4881 0.2898 0.5950 0.0333  0.0040  -0.0522 468 VAL D CG2 
16458 N N   . SER D 469 ? 0.5650 0.3562 0.6358 0.0324  0.0103  -0.0647 469 SER D N   
16459 C CA  . SER D 469 ? 0.5931 0.3817 0.6537 0.0372  0.0155  -0.0677 469 SER D CA  
16460 C C   . SER D 469 ? 0.6126 0.3974 0.6734 0.0491  0.0235  -0.0677 469 SER D C   
16461 O O   . SER D 469 ? 0.6097 0.3802 0.6657 0.0527  0.0244  -0.0689 469 SER D O   
16462 C CB  . SER D 469 ? 0.6145 0.3839 0.6537 0.0320  0.0132  -0.0734 469 SER D CB  
16463 O OG  . SER D 469 ? 0.6366 0.4070 0.6666 0.0345  0.0170  -0.0757 469 SER D OG  
16464 N N   . ILE D 470 ? 0.6295 0.4273 0.6960 0.0551  0.0291  -0.0660 470 ILE D N   
16465 C CA  . ILE D 470 ? 0.6865 0.4820 0.7527 0.0668  0.0374  -0.0659 470 ILE D CA  
16466 C C   . ILE D 470 ? 0.7311 0.5218 0.7835 0.0706  0.0433  -0.0695 470 ILE D C   
16467 O O   . ILE D 470 ? 0.7409 0.5353 0.7953 0.0805  0.0513  -0.0686 470 ILE D O   
16468 C CB  . ILE D 470 ? 0.6614 0.4789 0.7498 0.0715  0.0395  -0.0595 470 ILE D CB  
16469 C CG1 . ILE D 470 ? 0.6428 0.4799 0.7402 0.0683  0.0395  -0.0566 470 ILE D CG1 
16470 C CG2 . ILE D 470 ? 0.6287 0.4493 0.7287 0.0681  0.0337  -0.0562 470 ILE D CG2 
16471 C CD1 . ILE D 470 ? 0.6885 0.5461 0.8056 0.0736  0.0425  -0.0507 470 ILE D CD1 
16472 N N   . SER D 471 ? 0.7969 0.5793 0.8349 0.0628  0.0394  -0.0733 471 SER D N   
16473 C CA  . SER D 471 ? 0.8303 0.6051 0.8513 0.0648  0.0440  -0.0774 471 SER D CA  
16474 C C   . SER D 471 ? 0.7850 0.5420 0.7916 0.0754  0.0522  -0.0815 471 SER D C   
16475 O O   . SER D 471 ? 0.7743 0.5331 0.7748 0.0821  0.0598  -0.0824 471 SER D O   
16476 C CB  . SER D 471 ? 0.8855 0.6504 0.8916 0.0540  0.0368  -0.0811 471 SER D CB  
16477 O OG  . SER D 471 ? 0.8513 0.6351 0.8675 0.0479  0.0332  -0.0775 471 SER D OG  
16478 N N   . ASP D 472 ? 0.7867 0.5268 0.7882 0.0776  0.0513  -0.0836 472 ASP D N   
16479 C CA  . ASP D 472 ? 0.8168 0.5368 0.8028 0.0876  0.0587  -0.0880 472 ASP D CA  
16480 C C   . ASP D 472 ? 0.8352 0.5668 0.8363 0.1006  0.0671  -0.0836 472 ASP D C   
16481 O O   . ASP D 472 ? 0.7826 0.4987 0.7746 0.1105  0.0734  -0.0861 472 ASP D O   
16482 C CB  . ASP D 472 ? 0.8557 0.5502 0.8275 0.0833  0.0536  -0.0923 472 ASP D CB  
16483 C CG  . ASP D 472 ? 0.8697 0.5674 0.8565 0.0812  0.0485  -0.0883 472 ASP D CG  
16484 O OD1 . ASP D 472 ? 0.8843 0.6037 0.8908 0.0762  0.0441  -0.0828 472 ASP D OD1 
16485 O OD2 . ASP D 472 ? 0.8666 0.5438 0.8443 0.0843  0.0489  -0.0906 472 ASP D OD2 
16486 N N   . GLN D 473 ? 0.7545 0.5133 0.7786 0.1008  0.0671  -0.0769 473 GLN D N   
16487 C CA  . GLN D 473 ? 0.7270 0.4995 0.7693 0.1108  0.0724  -0.0715 473 GLN D CA  
16488 C C   . GLN D 473 ? 0.7385 0.5373 0.7967 0.1140  0.0772  -0.0663 473 GLN D C   
16489 O O   . GLN D 473 ? 0.7015 0.5150 0.7769 0.1213  0.0809  -0.0609 473 GLN D O   
16490 C CB  . GLN D 473 ? 0.6990 0.4774 0.7569 0.1069  0.0653  -0.0673 473 GLN D CB  
16491 C CG  . GLN D 473 ? 0.7034 0.4592 0.7519 0.1081  0.0629  -0.0699 473 GLN D CG  
16492 C CD  . GLN D 473 ? 0.6553 0.4210 0.7219 0.1068  0.0579  -0.0643 473 GLN D CD  
16493 O OE1 . GLN D 473 ? 0.6570 0.4332 0.7374 0.1154  0.0616  -0.0596 473 GLN D OE1 
16494 N NE2 . GLN D 473 ? 0.6138 0.3775 0.6812 0.0958  0.0493  -0.0643 473 GLN D NE2 
16495 N N   . LEU D 474 ? 0.7975 0.6023 0.8501 0.1087  0.0772  -0.0673 474 LEU D N   
16496 C CA  . LEU D 474 ? 0.7952 0.6258 0.8647 0.1084  0.0793  -0.0615 474 LEU D CA  
16497 C C   . LEU D 474 ? 0.8322 0.6723 0.9078 0.1208  0.0903  -0.0588 474 LEU D C   
16498 O O   . LEU D 474 ? 0.8118 0.6740 0.9080 0.1234  0.0921  -0.0523 474 LEU D O   
16499 C CB  . LEU D 474 ? 0.8319 0.6643 0.8919 0.0998  0.0766  -0.0633 474 LEU D CB  
16500 C CG  . LEU D 474 ? 0.8468 0.6856 0.9135 0.0873  0.0661  -0.0619 474 LEU D CG  
16501 C CD1 . LEU D 474 ? 0.8321 0.6880 0.9221 0.0859  0.0621  -0.0559 474 LEU D CD1 
16502 C CD2 . LEU D 474 ? 0.8770 0.6947 0.9273 0.0806  0.0594  -0.0674 474 LEU D CD2 
16503 N N   . ASP D 475 ? 0.8679 0.6905 0.9247 0.1284  0.0976  -0.0638 475 ASP D N   
16504 C CA  . ASP D 475 ? 0.9280 0.7571 0.9875 0.1411  0.1092  -0.0619 475 ASP D CA  
16505 C C   . ASP D 475 ? 0.8922 0.7290 0.9694 0.1502  0.1116  -0.0572 475 ASP D C   
16506 O O   . ASP D 475 ? 0.8832 0.7311 0.9686 0.1607  0.1207  -0.0538 475 ASP D O   
16507 C CB  . ASP D 475 ? 1.0263 0.8307 1.0588 0.1472  0.1160  -0.0694 475 ASP D CB  
16508 C CG  . ASP D 475 ? 1.0451 0.8210 1.0607 0.1469  0.1121  -0.0756 475 ASP D CG  
16509 O OD1 . ASP D 475 ? 1.0957 0.8687 1.1156 0.1376  0.1020  -0.0754 475 ASP D OD1 
16510 O OD2 . ASP D 475 ? 0.9700 0.7264 0.9684 0.1561  0.1194  -0.0804 475 ASP D OD2 
16511 N N   . LYS D 476 ? 0.8372 0.6678 0.9197 0.1468  0.1039  -0.0568 476 LYS D N   
16512 C CA  . LYS D 476 ? 0.7505 0.5844 0.8462 0.1560  0.1060  -0.0528 476 LYS D CA  
16513 C C   . LYS D 476 ? 0.6725 0.5361 0.7959 0.1547  0.1038  -0.0442 476 LYS D C   
16514 O O   . LYS D 476 ? 0.5838 0.4606 0.7156 0.1444  0.0974  -0.0420 476 LYS D O   
16515 C CB  . LYS D 476 ? 0.7488 0.5630 0.8380 0.1537  0.0994  -0.0555 476 LYS D CB  
16516 C CG  . LYS D 476 ? 0.8414 0.6237 0.9032 0.1543  0.1004  -0.0639 476 LYS D CG  
16517 C CD  . LYS D 476 ? 0.8997 0.6621 0.9563 0.1560  0.0967  -0.0654 476 LYS D CD  
16518 C CE  . LYS D 476 ? 0.8959 0.6577 0.9570 0.1432  0.0851  -0.0646 476 LYS D CE  
16519 N NZ  . LYS D 476 ? 0.8997 0.6511 0.9640 0.1461  0.0821  -0.0629 476 LYS D NZ  
16520 N N   . LYS D 477 ? 0.6746 0.5482 0.8121 0.1655  0.1089  -0.0393 477 LYS D N   
16521 C CA  . LYS D 477 ? 0.6747 0.5762 0.8384 0.1652  0.1070  -0.0309 477 LYS D CA  
16522 C C   . LYS D 477 ? 0.5944 0.4968 0.7666 0.1565  0.0959  -0.0290 477 LYS D C   
16523 O O   . LYS D 477 ? 0.5884 0.5098 0.7762 0.1494  0.0905  -0.0243 477 LYS D O   
16524 C CB  . LYS D 477 ? 0.7483 0.6588 0.9232 0.1798  0.1159  -0.0263 477 LYS D CB  
16525 C CG  . LYS D 477 ? 0.8937 0.8360 1.0938 0.1817  0.1181  -0.0175 477 LYS D CG  
16526 C CD  . LYS D 477 ? 1.0195 0.9751 1.2200 0.1819  0.1255  -0.0166 477 LYS D CD  
16527 C CE  . LYS D 477 ? 1.0756 1.0629 1.3013 0.1798  0.1254  -0.0077 477 LYS D CE  
16528 N NZ  . LYS D 477 ? 1.1174 1.1128 1.3507 0.1657  0.1144  -0.0062 477 LYS D NZ  
16529 N N   . ILE D 478 ? 0.5859 0.4664 0.7464 0.1569  0.0925  -0.0329 478 ILE D N   
16530 C CA  . ILE D 478 ? 0.5479 0.4264 0.7145 0.1504  0.0831  -0.0312 478 ILE D CA  
16531 C C   . ILE D 478 ? 0.5496 0.4043 0.6964 0.1420  0.0776  -0.0380 478 ILE D C   
16532 O O   . ILE D 478 ? 0.5630 0.3948 0.6926 0.1464  0.0804  -0.0431 478 ILE D O   
16533 C CB  . ILE D 478 ? 0.5480 0.4251 0.7228 0.1608  0.0847  -0.0273 478 ILE D CB  
16534 C CG1 . ILE D 478 ? 0.5554 0.4586 0.7517 0.1686  0.0895  -0.0197 478 ILE D CG1 
16535 C CG2 . ILE D 478 ? 0.5404 0.4122 0.7185 0.1544  0.0753  -0.0258 478 ILE D CG2 
16536 C CD1 . ILE D 478 ? 0.5548 0.4622 0.7638 0.1775  0.0893  -0.0141 478 ILE D CD1 
16537 N N   . ILE D 479 ? 0.5380 0.3981 0.6875 0.1297  0.0695  -0.0380 479 ILE D N   
16538 C CA  . ILE D 479 ? 0.5473 0.3883 0.6808 0.1207  0.0637  -0.0435 479 ILE D CA  
16539 C C   . ILE D 479 ? 0.5407 0.3785 0.6800 0.1164  0.0563  -0.0412 479 ILE D C   
16540 O O   . ILE D 479 ? 0.5417 0.3974 0.6976 0.1132  0.0522  -0.0360 479 ILE D O   
16541 C CB  . ILE D 479 ? 0.5481 0.3975 0.6801 0.1104  0.0603  -0.0448 479 ILE D CB  
16542 C CG1 . ILE D 479 ? 0.5958 0.4474 0.7206 0.1150  0.0681  -0.0468 479 ILE D CG1 
16543 C CG2 . ILE D 479 ? 0.5387 0.3721 0.6572 0.1000  0.0532  -0.0494 479 ILE D CG2 
16544 C CD1 . ILE D 479 ? 0.5872 0.4519 0.7144 0.1065  0.0658  -0.0462 479 ILE D CD1 
16545 N N   . THR D 480 ? 0.5385 0.3531 0.6638 0.1161  0.0544  -0.0449 480 THR D N   
16546 C CA  . THR D 480 ? 0.5244 0.3359 0.6548 0.1118  0.0477  -0.0423 480 THR D CA  
16547 C C   . THR D 480 ? 0.5328 0.3294 0.6502 0.1004  0.0413  -0.0466 480 THR D C   
16548 O O   . THR D 480 ? 0.5628 0.3459 0.6644 0.0976  0.0424  -0.0522 480 THR D O   
16549 C CB  . THR D 480 ? 0.5149 0.3144 0.6439 0.1220  0.0506  -0.0409 480 THR D CB  
16550 O OG1 . THR D 480 ? 0.5449 0.3201 0.6527 0.1229  0.0536  -0.0477 480 THR D OG1 
16551 C CG2 . THR D 480 ? 0.4980 0.3136 0.6414 0.1337  0.0569  -0.0359 480 THR D CG2 
16552 N N   . SER D 481 ? 0.5056 0.3052 0.6302 0.0940  0.0346  -0.0437 481 SER D N   
16553 C CA  . SER D 481 ? 0.5022 0.2886 0.6170 0.0837  0.0285  -0.0464 481 SER D CA  
16554 C C   . SER D 481 ? 0.4710 0.2546 0.5916 0.0826  0.0243  -0.0425 481 SER D C   
16555 O O   . SER D 481 ? 0.4365 0.2343 0.5714 0.0870  0.0243  -0.0372 481 SER D O   
16556 C CB  . SER D 481 ? 0.5168 0.3160 0.6354 0.0735  0.0242  -0.0467 481 SER D CB  
16557 O OG  . SER D 481 ? 0.5387 0.3284 0.6512 0.0636  0.0179  -0.0481 481 SER D OG  
16558 N N   . GLU D 482 ? 0.4802 0.2455 0.5893 0.0766  0.0204  -0.0448 482 GLU D N   
16559 C CA  . GLU D 482 ? 0.4799 0.2429 0.5938 0.0739  0.0160  -0.0409 482 GLU D CA  
16560 C C   . GLU D 482 ? 0.4940 0.2512 0.6022 0.0611  0.0099  -0.0424 482 GLU D C   
16561 O O   . GLU D 482 ? 0.5360 0.2761 0.6297 0.0566  0.0090  -0.0471 482 GLU D O   
16562 C CB  . GLU D 482 ? 0.4789 0.2242 0.5863 0.0832  0.0193  -0.0405 482 GLU D CB  
16563 C CG  . GLU D 482 ? 0.4678 0.2058 0.5765 0.0805  0.0148  -0.0367 482 GLU D CG  
16564 C CD  . GLU D 482 ? 0.4846 0.2033 0.5857 0.0900  0.0180  -0.0362 482 GLU D CD  
16565 O OE1 . GLU D 482 ? 0.4983 0.1977 0.5846 0.0932  0.0215  -0.0413 482 GLU D OE1 
16566 O OE2 . GLU D 482 ? 0.4705 0.1928 0.5799 0.0940  0.0168  -0.0307 482 GLU D OE2 
16567 N N   . ASN D 483 ? 0.4907 0.2624 0.6104 0.0553  0.0056  -0.0383 483 ASN D N   
16568 C CA  . ASN D 483 ? 0.5064 0.2772 0.6239 0.0436  0.0002  -0.0388 483 ASN D CA  
16569 C C   . ASN D 483 ? 0.4792 0.2499 0.6018 0.0407  -0.0033 -0.0342 483 ASN D C   
16570 O O   . ASN D 483 ? 0.5063 0.2901 0.6404 0.0446  -0.0032 -0.0297 483 ASN D O   
16571 C CB  . ASN D 483 ? 0.5072 0.2975 0.6330 0.0388  -0.0010 -0.0389 483 ASN D CB  
16572 C CG  . ASN D 483 ? 0.5441 0.3319 0.6624 0.0406  0.0021  -0.0435 483 ASN D CG  
16573 O OD1 . ASN D 483 ? 0.5586 0.3337 0.6644 0.0351  0.0005  -0.0476 483 ASN D OD1 
16574 N ND2 . ASN D 483 ? 0.5315 0.3309 0.6565 0.0481  0.0065  -0.0427 483 ASN D ND2 
16575 N N   . PHE D 484 ? 0.4599 0.2170 0.5741 0.0328  -0.0068 -0.0349 484 PHE D N   
16576 C CA  . PHE D 484 ? 0.4516 0.2055 0.5682 0.0296  -0.0097 -0.0306 484 PHE D CA  
16577 C C   . PHE D 484 ? 0.4572 0.2224 0.5793 0.0189  -0.0139 -0.0289 484 PHE D C   
16578 O O   . PHE D 484 ? 0.4552 0.2221 0.5744 0.0120  -0.0156 -0.0318 484 PHE D O   
16579 C CB  . PHE D 484 ? 0.4601 0.1882 0.5623 0.0290  -0.0100 -0.0323 484 PHE D CB  
16580 C CG  . PHE D 484 ? 0.4687 0.1836 0.5644 0.0404  -0.0053 -0.0341 484 PHE D CG  
16581 C CD1 . PHE D 484 ? 0.4779 0.1840 0.5639 0.0435  -0.0022 -0.0397 484 PHE D CD1 
16582 C CD2 . PHE D 484 ? 0.4685 0.1801 0.5677 0.0485  -0.0039 -0.0298 484 PHE D CD2 
16583 C CE1 . PHE D 484 ? 0.5067 0.2007 0.5865 0.0549  0.0029  -0.0413 484 PHE D CE1 
16584 C CE2 . PHE D 484 ? 0.4901 0.1906 0.5843 0.0599  0.0007  -0.0310 484 PHE D CE2 
16585 C CZ  . PHE D 484 ? 0.5032 0.1945 0.5876 0.0633  0.0045  -0.0368 484 PHE D CZ  
16586 N N   . PHE D 485 ? 0.4589 0.2317 0.5887 0.0178  -0.0156 -0.0239 485 PHE D N   
16587 C CA  . PHE D 485 ? 0.4449 0.2290 0.5804 0.0089  -0.0187 -0.0217 485 PHE D CA  
16588 C C   . PHE D 485 ? 0.4495 0.2284 0.5849 0.0065  -0.0205 -0.0170 485 PHE D C   
16589 O O   . PHE D 485 ? 0.4649 0.2419 0.6020 0.0134  -0.0194 -0.0141 485 PHE D O   
16590 C CB  . PHE D 485 ? 0.4528 0.2589 0.6007 0.0108  -0.0183 -0.0200 485 PHE D CB  
16591 C CG  . PHE D 485 ? 0.4405 0.2533 0.5897 0.0140  -0.0162 -0.0238 485 PHE D CG  
16592 C CD1 . PHE D 485 ? 0.4339 0.2508 0.5818 0.0076  -0.0175 -0.0266 485 PHE D CD1 
16593 C CD2 . PHE D 485 ? 0.4429 0.2573 0.5941 0.0233  -0.0129 -0.0241 485 PHE D CD2 
16594 C CE1 . PHE D 485 ? 0.4471 0.2696 0.5953 0.0104  -0.0155 -0.0297 485 PHE D CE1 
16595 C CE2 . PHE D 485 ? 0.4522 0.2730 0.6044 0.0260  -0.0106 -0.0272 485 PHE D CE2 
16596 C CZ  . PHE D 485 ? 0.4381 0.2623 0.5881 0.0195  -0.0119 -0.0300 485 PHE D CZ  
16597 N N   . ASN D 486 ? 0.4371 0.2142 0.5705 -0.0033 -0.0231 -0.0161 486 ASN D N   
16598 C CA  . ASN D 486 ? 0.4225 0.1972 0.5565 -0.0070 -0.0246 -0.0111 486 ASN D CA  
16599 C C   . ASN D 486 ? 0.4182 0.2118 0.5629 -0.0053 -0.0245 -0.0074 486 ASN D C   
16600 O O   . ASN D 486 ? 0.3952 0.2048 0.5472 -0.0064 -0.0243 -0.0086 486 ASN D O   
16601 C CB  . ASN D 486 ? 0.4264 0.1953 0.5561 -0.0180 -0.0271 -0.0111 486 ASN D CB  
16602 C CG  . ASN D 486 ? 0.4511 0.1968 0.5680 -0.0193 -0.0278 -0.0138 486 ASN D CG  
16603 O OD1 . ASN D 486 ? 0.4465 0.1875 0.5584 -0.0249 -0.0292 -0.0175 486 ASN D OD1 
16604 N ND2 . ASN D 486 ? 0.4651 0.1957 0.5760 -0.0140 -0.0268 -0.0121 486 ASN D ND2 
16605 N N   . ILE D 487 ? 0.4180 0.2090 0.5630 -0.0020 -0.0246 -0.0030 487 ILE D N   
16606 C CA  . ILE D 487 ? 0.4117 0.2188 0.5649 -0.0008 -0.0248 0.0004  487 ILE D CA  
16607 C C   . ILE D 487 ? 0.4068 0.2152 0.5594 -0.0089 -0.0260 0.0039  487 ILE D C   
16608 O O   . ILE D 487 ? 0.4057 0.2021 0.5526 -0.0104 -0.0266 0.0071  487 ILE D O   
16609 C CB  . ILE D 487 ? 0.4176 0.2244 0.5725 0.0079  -0.0245 0.0035  487 ILE D CB  
16610 C CG1 . ILE D 487 ? 0.4199 0.2231 0.5748 0.0164  -0.0228 0.0007  487 ILE D CG1 
16611 C CG2 . ILE D 487 ? 0.3923 0.2164 0.5550 0.0084  -0.0253 0.0062  487 ILE D CG2 
16612 C CD1 . ILE D 487 ? 0.4125 0.2135 0.5688 0.0251  -0.0227 0.0044  487 ILE D CD1 
16613 N N   . PRO D 488 ? 0.4157 0.2388 0.5743 -0.0139 -0.0260 0.0038  488 PRO D N   
16614 C CA  . PRO D 488 ? 0.4157 0.2422 0.5747 -0.0208 -0.0263 0.0075  488 PRO D CA  
16615 C C   . PRO D 488 ? 0.4205 0.2470 0.5785 -0.0175 -0.0263 0.0123  488 PRO D C   
16616 O O   . PRO D 488 ? 0.3922 0.2247 0.5532 -0.0109 -0.0263 0.0124  488 PRO D O   
16617 C CB  . PRO D 488 ? 0.3993 0.2432 0.5661 -0.0238 -0.0256 0.0060  488 PRO D CB  
16618 C CG  . PRO D 488 ? 0.3903 0.2365 0.5591 -0.0203 -0.0256 0.0010  488 PRO D CG  
16619 C CD  . PRO D 488 ? 0.3885 0.2259 0.5540 -0.0124 -0.0253 0.0005  488 PRO D CD  
16620 N N   . ASP D 489 ? 0.4367 0.2572 0.5906 -0.0227 -0.0264 0.0164  489 ASP D N   
16621 C CA  . ASP D 489 ? 0.4483 0.2676 0.5997 -0.0205 -0.0266 0.0215  489 ASP D CA  
16622 C C   . ASP D 489 ? 0.4302 0.2659 0.5866 -0.0199 -0.0258 0.0225  489 ASP D C   
16623 O O   . ASP D 489 ? 0.4301 0.2669 0.5848 -0.0161 -0.0264 0.0256  489 ASP D O   
16624 C CB  . ASP D 489 ? 0.4801 0.2891 0.6255 -0.0269 -0.0266 0.0259  489 ASP D CB  
16625 C CG  . ASP D 489 ? 0.5310 0.3207 0.6695 -0.0283 -0.0276 0.0254  489 ASP D CG  
16626 O OD1 . ASP D 489 ? 0.4991 0.2802 0.6351 -0.0212 -0.0282 0.0237  489 ASP D OD1 
16627 O OD2 . ASP D 489 ? 0.5954 0.3789 0.7310 -0.0365 -0.0278 0.0268  489 ASP D OD2 
16628 N N   . ASN D 490 ? 0.4264 0.2741 0.5883 -0.0234 -0.0246 0.0201  490 ASN D N   
16629 C CA  . ASN D 490 ? 0.4419 0.3040 0.6081 -0.0220 -0.0236 0.0201  490 ASN D CA  
16630 C C   . ASN D 490 ? 0.4105 0.2807 0.5822 -0.0169 -0.0242 0.0158  490 ASN D C   
16631 O O   . ASN D 490 ? 0.3618 0.2437 0.5377 -0.0169 -0.0233 0.0145  490 ASN D O   
16632 C CB  . ASN D 490 ? 0.4567 0.3261 0.6247 -0.0287 -0.0215 0.0216  490 ASN D CB  
16633 C CG  . ASN D 490 ? 0.4910 0.3651 0.6644 -0.0322 -0.0212 0.0180  490 ASN D CG  
16634 O OD1 . ASN D 490 ? 0.4817 0.3480 0.6541 -0.0320 -0.0227 0.0154  490 ASN D OD1 
16635 N ND2 . ASN D 490 ? 0.5074 0.3940 0.6858 -0.0349 -0.0193 0.0180  490 ASN D ND2 
16636 N N   . CYS D 491 ? 0.3996 0.2635 0.5712 -0.0124 -0.0253 0.0136  491 CYS D N   
16637 C CA  . CYS D 491 ? 0.3797 0.2516 0.5564 -0.0070 -0.0257 0.0107  491 CYS D CA  
16638 C C   . CYS D 491 ? 0.3687 0.2420 0.5449 -0.0017 -0.0272 0.0134  491 CYS D C   
16639 O O   . CYS D 491 ? 0.3632 0.2269 0.5356 0.0012  -0.0282 0.0161  491 CYS D O   
16640 C CB  . CYS D 491 ? 0.3847 0.2509 0.5619 -0.0039 -0.0256 0.0073  491 CYS D CB  
16641 S SG  . CYS D 491 ? 0.3652 0.2413 0.5489 0.0032  -0.0259 0.0051  491 CYS D SG  
16642 N N   . TRP D 492 ? 0.3291 0.2141 0.5091 -0.0008 -0.0276 0.0130  492 TRP D N   
16643 C CA  . TRP D 492 ? 0.3361 0.2237 0.5153 0.0029  -0.0297 0.0158  492 TRP D CA  
16644 C C   . TRP D 492 ? 0.3284 0.2216 0.5135 0.0083  -0.0310 0.0141  492 TRP D C   
16645 O O   . TRP D 492 ? 0.3541 0.2479 0.5398 0.0126  -0.0333 0.0168  492 TRP D O   
16646 C CB  . TRP D 492 ? 0.3435 0.2387 0.5211 0.0000  -0.0296 0.0167  492 TRP D CB  
16647 C CG  . TRP D 492 ? 0.3448 0.2376 0.5181 -0.0056 -0.0273 0.0181  492 TRP D CG  
16648 C CD1 . TRP D 492 ? 0.3489 0.2489 0.5238 -0.0091 -0.0250 0.0164  492 TRP D CD1 
16649 C CD2 . TRP D 492 ? 0.3561 0.2394 0.5234 -0.0082 -0.0268 0.0219  492 TRP D CD2 
16650 N NE1 . TRP D 492 ? 0.3776 0.2748 0.5489 -0.0136 -0.0229 0.0189  492 TRP D NE1 
16651 C CE2 . TRP D 492 ? 0.3720 0.2588 0.5384 -0.0136 -0.0240 0.0224  492 TRP D CE2 
16652 C CE3 . TRP D 492 ? 0.3749 0.2472 0.5377 -0.0064 -0.0283 0.0253  492 TRP D CE3 
16653 C CZ2 . TRP D 492 ? 0.3770 0.2572 0.5384 -0.0180 -0.0226 0.0262  492 TRP D CZ2 
16654 C CZ3 . TRP D 492 ? 0.3970 0.2611 0.5541 -0.0106 -0.0271 0.0288  492 TRP D CZ3 
16655 C CH2 . TRP D 492 ? 0.3985 0.2670 0.5550 -0.0167 -0.0244 0.0294  492 TRP D CH2 
16656 N N   . VAL D 493 ? 0.3206 0.2188 0.5104 0.0079  -0.0296 0.0101  493 VAL D N   
16657 C CA  . VAL D 493 ? 0.3159 0.2204 0.5120 0.0124  -0.0302 0.0085  493 VAL D CA  
16658 C C   . VAL D 493 ? 0.3029 0.2065 0.5009 0.0117  -0.0279 0.0045  493 VAL D C   
16659 O O   . VAL D 493 ? 0.2996 0.2034 0.4964 0.0069  -0.0266 0.0026  493 VAL D O   
16660 C CB  . VAL D 493 ? 0.3261 0.2419 0.5258 0.0119  -0.0317 0.0083  493 VAL D CB  
16661 C CG1 . VAL D 493 ? 0.3338 0.2537 0.5327 0.0069  -0.0302 0.0060  493 VAL D CG1 
16662 C CG2 . VAL D 493 ? 0.3044 0.2278 0.5114 0.0158  -0.0324 0.0071  493 VAL D CG2 
16663 N N   . VAL D 494 ? 0.2917 0.1951 0.4929 0.0167  -0.0274 0.0035  494 VAL D N   
16664 C CA  . VAL D 494 ? 0.2902 0.1931 0.4925 0.0167  -0.0252 -0.0003 494 VAL D CA  
16665 C C   . VAL D 494 ? 0.2948 0.2078 0.5042 0.0207  -0.0250 -0.0011 494 VAL D C   
16666 O O   . VAL D 494 ? 0.2933 0.2106 0.5066 0.0250  -0.0262 0.0015  494 VAL D O   
16667 C CB  . VAL D 494 ? 0.2991 0.1884 0.4958 0.0185  -0.0238 -0.0012 494 VAL D CB  
16668 C CG1 . VAL D 494 ? 0.3176 0.2024 0.5146 0.0255  -0.0239 0.0013  494 VAL D CG1 
16669 C CG2 . VAL D 494 ? 0.3012 0.1890 0.4973 0.0180  -0.0218 -0.0055 494 VAL D CG2 
16670 N N   . ASN D 495 ? 0.2951 0.2123 0.5063 0.0187  -0.0235 -0.0044 495 ASN D N   
16671 C CA  . ASN D 495 ? 0.2893 0.2140 0.5061 0.0221  -0.0224 -0.0055 495 ASN D CA  
16672 C C   . ASN D 495 ? 0.2879 0.2051 0.5011 0.0241  -0.0197 -0.0083 495 ASN D C   
16673 O O   . ASN D 495 ? 0.3010 0.2148 0.5104 0.0201  -0.0190 -0.0110 495 ASN D O   
16674 C CB  . ASN D 495 ? 0.2940 0.2281 0.5143 0.0183  -0.0227 -0.0071 495 ASN D CB  
16675 C CG  . ASN D 495 ? 0.2987 0.2410 0.5250 0.0212  -0.0217 -0.0075 495 ASN D CG  
16676 O OD1 . ASN D 495 ? 0.3102 0.2499 0.5362 0.0248  -0.0193 -0.0086 495 ASN D OD1 
16677 N ND2 . ASN D 495 ? 0.2799 0.2316 0.5112 0.0198  -0.0233 -0.0065 495 ASN D ND2 
16678 N N   . ALA D 496 ? 0.2980 0.2122 0.5119 0.0304  -0.0181 -0.0074 496 ALA D N   
16679 C CA  . ALA D 496 ? 0.3057 0.2103 0.5142 0.0332  -0.0152 -0.0103 496 ALA D CA  
16680 C C   . ALA D 496 ? 0.3060 0.2197 0.5200 0.0369  -0.0127 -0.0112 496 ALA D C   
16681 O O   . ALA D 496 ? 0.3050 0.2285 0.5269 0.0406  -0.0129 -0.0083 496 ALA D O   
16682 C CB  . ALA D 496 ? 0.3215 0.2148 0.5260 0.0383  -0.0145 -0.0087 496 ALA D CB  
16683 N N   . SER D 497 ? 0.3035 0.2149 0.5135 0.0352  -0.0107 -0.0148 497 SER D N   
16684 C CA  . SER D 497 ? 0.3150 0.2361 0.5298 0.0374  -0.0083 -0.0155 497 SER D CA  
16685 C C   . SER D 497 ? 0.3239 0.2367 0.5308 0.0387  -0.0050 -0.0194 497 SER D C   
16686 O O   . SER D 497 ? 0.3266 0.2272 0.5243 0.0356  -0.0056 -0.0221 497 SER D O   
16687 C CB  . SER D 497 ? 0.3065 0.2395 0.5271 0.0322  -0.0105 -0.0150 497 SER D CB  
16688 O OG  . SER D 497 ? 0.3059 0.2354 0.5215 0.0261  -0.0118 -0.0174 497 SER D OG  
16689 N N   . ALA D 498 ? 0.3111 0.2307 0.5213 0.0428  -0.0017 -0.0195 498 ALA D N   
16690 C CA  . ALA D 498 ? 0.3304 0.2437 0.5327 0.0438  0.0016  -0.0233 498 ALA D CA  
16691 C C   . ALA D 498 ? 0.3198 0.2461 0.5283 0.0450  0.0041  -0.0225 498 ALA D C   
16692 O O   . ALA D 498 ? 0.3121 0.2504 0.5310 0.0476  0.0044  -0.0190 498 ALA D O   
16693 C CB  . ALA D 498 ? 0.3568 0.2579 0.5525 0.0507  0.0052  -0.0244 498 ALA D CB  
16694 N N   . GLY D 499 ? 0.3276 0.2512 0.5293 0.0430  0.0057  -0.0256 499 GLY D N   
16695 C CA  . GLY D 499 ? 0.3225 0.2577 0.5291 0.0434  0.0080  -0.0246 499 GLY D CA  
16696 C C   . GLY D 499 ? 0.3354 0.2644 0.5315 0.0427  0.0106  -0.0283 499 GLY D C   
16697 O O   . GLY D 499 ? 0.3896 0.3065 0.5750 0.0394  0.0090  -0.0317 499 GLY D O   
16698 N N   . ILE D 500 ? 0.3144 0.2518 0.5133 0.0455  0.0145  -0.0273 500 ILE D N   
16699 C CA  . ILE D 500 ? 0.3380 0.2700 0.5262 0.0455  0.0175  -0.0305 500 ILE D CA  
16700 C C   . ILE D 500 ? 0.3505 0.2964 0.5455 0.0444  0.0191  -0.0278 500 ILE D C   
16701 O O   . ILE D 500 ? 0.3605 0.3189 0.5678 0.0466  0.0201  -0.0238 500 ILE D O   
16702 C CB  . ILE D 500 ? 0.3555 0.2767 0.5346 0.0529  0.0231  -0.0330 500 ILE D CB  
16703 C CG1 . ILE D 500 ? 0.3762 0.2872 0.5401 0.0514  0.0248  -0.0374 500 ILE D CG1 
16704 C CG2 . ILE D 500 ? 0.3504 0.2823 0.5390 0.0607  0.0287  -0.0296 500 ILE D CG2 
16705 C CD1 . ILE D 500 ? 0.4215 0.3185 0.5734 0.0585  0.0303  -0.0408 500 ILE D CD1 
16706 N N   . SER D 501 ? 0.3452 0.2889 0.5322 0.0406  0.0188  -0.0298 501 SER D N   
16707 C CA  . SER D 501 ? 0.3525 0.3077 0.5443 0.0391  0.0202  -0.0273 501 SER D CA  
16708 C C   . SER D 501 ? 0.3800 0.3379 0.5701 0.0456  0.0274  -0.0268 501 SER D C   
16709 O O   . SER D 501 ? 0.4212 0.3683 0.6011 0.0502  0.0310  -0.0300 501 SER D O   
16710 C CB  . SER D 501 ? 0.3406 0.2927 0.5247 0.0330  0.0171  -0.0290 501 SER D CB  
16711 O OG  . SER D 501 ? 0.3493 0.3015 0.5373 0.0276  0.0110  -0.0286 501 SER D OG  
16712 N N   . VAL D 502 ? 0.3766 0.3486 0.5766 0.0459  0.0296  -0.0226 502 VAL D N   
16713 C CA  . VAL D 502 ? 0.3974 0.3753 0.5983 0.0518  0.0369  -0.0210 502 VAL D CA  
16714 C C   . VAL D 502 ? 0.4088 0.3959 0.6114 0.0480  0.0377  -0.0184 502 VAL D C   
16715 O O   . VAL D 502 ? 0.3817 0.3757 0.5919 0.0422  0.0330  -0.0159 502 VAL D O   
16716 C CB  . VAL D 502 ? 0.4213 0.4097 0.6365 0.0570  0.0391  -0.0170 502 VAL D CB  
16717 C CG1 . VAL D 502 ? 0.4291 0.4248 0.6466 0.0641  0.0475  -0.0148 502 VAL D CG1 
16718 C CG2 . VAL D 502 ? 0.4279 0.4074 0.6423 0.0603  0.0373  -0.0188 502 VAL D CG2 
16719 N N   . ARG D 503 ? 0.4330 0.4202 0.6286 0.0517  0.0442  -0.0186 503 ARG D N   
16720 C CA  . ARG D 503 ? 0.4255 0.4202 0.6208 0.0485  0.0458  -0.0160 503 ARG D CA  
16721 C C   . ARG D 503 ? 0.3716 0.3781 0.5739 0.0539  0.0537  -0.0121 503 ARG D C   
16722 O O   . ARG D 503 ? 0.3390 0.3420 0.5363 0.0612  0.0601  -0.0136 503 ARG D O   
16723 C CB  . ARG D 503 ? 0.4790 0.4615 0.6562 0.0461  0.0455  -0.0202 503 ARG D CB  
16724 C CG  . ARG D 503 ? 0.5499 0.5386 0.7243 0.0433  0.0476  -0.0175 503 ARG D CG  
16725 C CD  . ARG D 503 ? 0.6287 0.6054 0.7843 0.0411  0.0469  -0.0214 503 ARG D CD  
16726 N NE  . ARG D 503 ? 0.7344 0.7037 0.8865 0.0350  0.0385  -0.0238 503 ARG D NE  
16727 C CZ  . ARG D 503 ? 0.7981 0.7726 0.9563 0.0289  0.0327  -0.0212 503 ARG D CZ  
16728 N NH1 . ARG D 503 ? 0.8217 0.8072 0.9877 0.0271  0.0338  -0.0163 503 ARG D NH1 
16729 N NH2 . ARG D 503 ? 0.7723 0.7406 0.9285 0.0245  0.0259  -0.0234 503 ARG D NH2 
16730 N N   . TYR D 504 ? 0.3210 0.3413 0.5346 0.0503  0.0534  -0.0067 504 TYR D N   
16731 C CA  . TYR D 504 ? 0.3047 0.3369 0.5234 0.0534  0.0607  -0.0024 504 TYR D CA  
16732 C C   . TYR D 504 ? 0.2875 0.3237 0.5042 0.0468  0.0594  0.0003  504 TYR D C   
16733 O O   . TYR D 504 ? 0.2624 0.3045 0.4886 0.0408  0.0539  0.0032  504 TYR D O   
16734 C CB  . TYR D 504 ? 0.2937 0.3412 0.5315 0.0558  0.0618  0.0029  504 TYR D CB  
16735 C CG  . TYR D 504 ? 0.3057 0.3669 0.5506 0.0603  0.0703  0.0078  504 TYR D CG  
16736 C CD1 . TYR D 504 ? 0.3148 0.3872 0.5653 0.0554  0.0715  0.0128  504 TYR D CD1 
16737 C CD2 . TYR D 504 ? 0.3268 0.3898 0.5726 0.0696  0.0776  0.0076  504 TYR D CD2 
16738 C CE1 . TYR D 504 ? 0.3189 0.4048 0.5764 0.0592  0.0797  0.0178  504 TYR D CE1 
16739 C CE2 . TYR D 504 ? 0.3224 0.3993 0.5756 0.0742  0.0861  0.0125  504 TYR D CE2 
16740 C CZ  . TYR D 504 ? 0.3176 0.4065 0.5770 0.0687  0.0871  0.0177  504 TYR D CZ  
16741 O OH  . TYR D 504 ? 0.3256 0.4289 0.5927 0.0730  0.0956  0.0229  504 TYR D OH  
16742 N N   . GLY D 505 ? 0.2994 0.3314 0.5031 0.0482  0.0644  -0.0008 505 GLY D N   
16743 C CA  . GLY D 505 ? 0.3086 0.3406 0.5062 0.0424  0.0629  0.0009  505 GLY D CA  
16744 C C   . GLY D 505 ? 0.3228 0.3465 0.5170 0.0359  0.0536  -0.0015 505 GLY D C   
16745 O O   . GLY D 505 ? 0.3422 0.3533 0.5250 0.0364  0.0510  -0.0068 505 GLY D O   
16746 N N   . LYS D 506 ? 0.3248 0.3555 0.5292 0.0300  0.0488  0.0024  506 LYS D N   
16747 C CA  . LYS D 506 ? 0.3106 0.3348 0.5131 0.0244  0.0406  0.0008  506 LYS D CA  
16748 C C   . LYS D 506 ? 0.2928 0.3185 0.5066 0.0235  0.0356  0.0003  506 LYS D C   
16749 O O   . LYS D 506 ? 0.3063 0.3271 0.5198 0.0196  0.0293  -0.0011 506 LYS D O   
16750 C CB  . LYS D 506 ? 0.3071 0.3364 0.5125 0.0188  0.0386  0.0054  506 LYS D CB  
16751 C CG  . LYS D 506 ? 0.3234 0.3529 0.5188 0.0187  0.0432  0.0074  506 LYS D CG  
16752 C CD  . LYS D 506 ? 0.3239 0.3579 0.5240 0.0127  0.0401  0.0125  506 LYS D CD  
16753 C CE  . LYS D 506 ? 0.3393 0.3749 0.5313 0.0119  0.0444  0.0158  506 LYS D CE  
16754 N NZ  . LYS D 506 ? 0.3466 0.3843 0.5427 0.0060  0.0404  0.0205  506 LYS D NZ  
16755 N N   . PHE D 507 ? 0.2943 0.3271 0.5182 0.0274  0.0386  0.0018  507 PHE D N   
16756 C CA  . PHE D 507 ? 0.2792 0.3136 0.5132 0.0268  0.0341  0.0016  507 PHE D CA  
16757 C C   . PHE D 507 ? 0.2784 0.3020 0.5053 0.0303  0.0330  -0.0036 507 PHE D C   
16758 O O   . PHE D 507 ? 0.2732 0.2945 0.4964 0.0363  0.0380  -0.0053 507 PHE D O   
16759 C CB  . PHE D 507 ? 0.2715 0.3193 0.5195 0.0293  0.0376  0.0063  507 PHE D CB  
16760 C CG  . PHE D 507 ? 0.2774 0.3295 0.5373 0.0280  0.0327  0.0075  507 PHE D CG  
16761 C CD1 . PHE D 507 ? 0.2857 0.3336 0.5459 0.0325  0.0322  0.0048  507 PHE D CD1 
16762 C CD2 . PHE D 507 ? 0.2705 0.3298 0.5404 0.0222  0.0284  0.0113  507 PHE D CD2 
16763 C CE1 . PHE D 507 ? 0.2760 0.3276 0.5461 0.0313  0.0275  0.0061  507 PHE D CE1 
16764 C CE2 . PHE D 507 ? 0.2594 0.3221 0.5387 0.0210  0.0238  0.0122  507 PHE D CE2 
16765 C CZ  . PHE D 507 ? 0.2665 0.3260 0.5462 0.0256  0.0234  0.0098  507 PHE D CZ  
16766 N N   . THR D 508 ? 0.3027 0.3199 0.5284 0.0268  0.0266  -0.0059 508 THR D N   
16767 C CA  . THR D 508 ? 0.3377 0.3447 0.5575 0.0288  0.0248  -0.0104 508 THR D CA  
16768 C C   . THR D 508 ? 0.3132 0.3234 0.5436 0.0277  0.0205  -0.0092 508 THR D C   
16769 O O   . THR D 508 ? 0.3411 0.3555 0.5777 0.0231  0.0164  -0.0072 508 THR D O   
16770 C CB  . THR D 508 ? 0.3848 0.3811 0.5926 0.0252  0.0211  -0.0140 508 THR D CB  
16771 O OG1 . THR D 508 ? 0.4690 0.4683 0.6815 0.0196  0.0158  -0.0122 508 THR D OG1 
16772 C CG2 . THR D 508 ? 0.3797 0.3719 0.5752 0.0257  0.0244  -0.0152 508 THR D CG2 
16773 N N   . PHE D 509 ? 0.2962 0.3031 0.5274 0.0320  0.0214  -0.0107 509 PHE D N   
16774 C CA  . PHE D 509 ? 0.3002 0.3087 0.5395 0.0311  0.0171  -0.0098 509 PHE D CA  
16775 C C   . PHE D 509 ? 0.3422 0.3401 0.5752 0.0344  0.0169  -0.0133 509 PHE D C   
16776 O O   . PHE D 509 ? 0.3913 0.3805 0.6140 0.0372  0.0200  -0.0165 509 PHE D O   
16777 C CB  . PHE D 509 ? 0.3036 0.3253 0.5563 0.0330  0.0188  -0.0051 509 PHE D CB  
16778 C CG  . PHE D 509 ? 0.2940 0.3195 0.5487 0.0402  0.0251  -0.0040 509 PHE D CG  
16779 C CD1 . PHE D 509 ? 0.3186 0.3450 0.5680 0.0430  0.0312  -0.0041 509 PHE D CD1 
16780 C CD2 . PHE D 509 ? 0.2974 0.3258 0.5593 0.0446  0.0252  -0.0026 509 PHE D CD2 
16781 C CE1 . PHE D 509 ? 0.3558 0.3861 0.6074 0.0504  0.0378  -0.0029 509 PHE D CE1 
16782 C CE2 . PHE D 509 ? 0.3043 0.3368 0.5691 0.0522  0.0313  -0.0011 509 PHE D CE2 
16783 C CZ  . PHE D 509 ? 0.3300 0.3636 0.5898 0.0553  0.0379  -0.0014 509 PHE D CZ  
16784 N N   . LYS D 510 ? 0.3624 0.3604 0.6011 0.0340  0.0133  -0.0127 510 LYS D N   
16785 C CA  . LYS D 510 ? 0.3792 0.3673 0.6128 0.0374  0.0132  -0.0152 510 LYS D CA  
16786 C C   . LYS D 510 ? 0.3582 0.3522 0.6009 0.0427  0.0148  -0.0123 510 LYS D C   
16787 O O   . LYS D 510 ? 0.3456 0.3508 0.5993 0.0414  0.0129  -0.0085 510 LYS D O   
16788 C CB  . LYS D 510 ? 0.4128 0.3941 0.6433 0.0324  0.0077  -0.0170 510 LYS D CB  
16789 C CG  . LYS D 510 ? 0.4351 0.4101 0.6565 0.0279  0.0061  -0.0199 510 LYS D CG  
16790 C CD  . LYS D 510 ? 0.4947 0.4631 0.7129 0.0236  0.0014  -0.0216 510 LYS D CD  
16791 C CE  . LYS D 510 ? 0.5324 0.4907 0.7392 0.0213  0.0008  -0.0251 510 LYS D CE  
16792 N NZ  . LYS D 510 ? 0.5516 0.4998 0.7516 0.0253  0.0031  -0.0274 510 LYS D NZ  
16793 N N   . ILE D 511 ? 0.3356 0.3218 0.5731 0.0487  0.0180  -0.0140 511 ILE D N   
16794 C CA  . ILE D 511 ? 0.3176 0.3069 0.5627 0.0539  0.0184  -0.0114 511 ILE D CA  
16795 C C   . ILE D 511 ? 0.3432 0.3195 0.5816 0.0532  0.0150  -0.0138 511 ILE D C   
16796 O O   . ILE D 511 ? 0.3785 0.3424 0.6052 0.0513  0.0148  -0.0179 511 ILE D O   
16797 C CB  . ILE D 511 ? 0.3176 0.3089 0.5636 0.0625  0.0254  -0.0104 511 ILE D CB  
16798 C CG1 . ILE D 511 ? 0.3079 0.2829 0.5384 0.0660  0.0293  -0.0156 511 ILE D CG1 
16799 C CG2 . ILE D 511 ? 0.3057 0.3123 0.5604 0.0625  0.0287  -0.0069 511 ILE D CG2 
16800 C CD1 . ILE D 511 ? 0.3062 0.2817 0.5356 0.0751  0.0370  -0.0153 511 ILE D CD1 
16801 N N   . HIS D 512 ? 0.3328 0.3124 0.5785 0.0544  0.0121  -0.0110 512 HIS D N   
16802 C CA  . HIS D 512 ? 0.3467 0.3161 0.5873 0.0519  0.0080  -0.0124 512 HIS D CA  
16803 C C   . HIS D 512 ? 0.3480 0.3218 0.5968 0.0555  0.0062  -0.0085 512 HIS D C   
16804 O O   . HIS D 512 ? 0.3104 0.2973 0.5700 0.0580  0.0069  -0.0046 512 HIS D O   
16805 C CB  . HIS D 512 ? 0.3412 0.3124 0.5816 0.0437  0.0032  -0.0131 512 HIS D CB  
16806 C CG  . HIS D 512 ? 0.3658 0.3512 0.6162 0.0411  0.0019  -0.0099 512 HIS D CG  
16807 N ND1 . HIS D 512 ? 0.3413 0.3359 0.6015 0.0414  -0.0007 -0.0060 512 HIS D ND1 
16808 C CD2 . HIS D 512 ? 0.3545 0.3458 0.6060 0.0380  0.0028  -0.0100 512 HIS D CD2 
16809 C CE1 . HIS D 512 ? 0.3648 0.3698 0.6315 0.0380  -0.0016 -0.0041 512 HIS D CE1 
16810 N NE2 . HIS D 512 ? 0.3496 0.3526 0.6112 0.0360  0.0007  -0.0064 512 HIS D NE2 
16811 N N   . ASP D 513 ? 0.3534 0.3168 0.5972 0.0554  0.0036  -0.0092 513 ASP D N   
16812 C CA  . ASP D 513 ? 0.3344 0.3009 0.5844 0.0573  0.0005  -0.0053 513 ASP D CA  
16813 C C   . ASP D 513 ? 0.3211 0.2790 0.5652 0.0517  -0.0041 -0.0065 513 ASP D C   
16814 O O   . ASP D 513 ? 0.3169 0.2658 0.5524 0.0475  -0.0043 -0.0101 513 ASP D O   
16815 C CB  . ASP D 513 ? 0.3339 0.2972 0.5851 0.0663  0.0041  -0.0037 513 ASP D CB  
16816 C CG  . ASP D 513 ? 0.3340 0.3050 0.5948 0.0702  0.0015  0.0016  513 ASP D CG  
16817 O OD1 . ASP D 513 ? 0.3410 0.3223 0.6090 0.0657  -0.0030 0.0044  513 ASP D OD1 
16818 O OD2 . ASP D 513 ? 0.3669 0.3328 0.6274 0.0777  0.0040  0.0030  513 ASP D OD2 
16819 N N   . GLN D 514 ? 0.3220 0.2833 0.5708 0.0514  -0.0079 -0.0030 514 GLN D N   
16820 C CA  . GLN D 514 ? 0.3229 0.2796 0.5676 0.0456  -0.0122 -0.0033 514 GLN D CA  
16821 C C   . GLN D 514 ? 0.3361 0.2919 0.5831 0.0487  -0.0148 0.0006  514 GLN D C   
16822 O O   . GLN D 514 ? 0.3022 0.2680 0.5578 0.0521  -0.0157 0.0043  514 GLN D O   
16823 C CB  . GLN D 514 ? 0.3007 0.2671 0.5496 0.0395  -0.0151 -0.0030 514 GLN D CB  
16824 C CG  . GLN D 514 ? 0.3036 0.2663 0.5483 0.0340  -0.0189 -0.0032 514 GLN D CG  
16825 C CD  . GLN D 514 ? 0.2953 0.2670 0.5441 0.0291  -0.0217 -0.0026 514 GLN D CD  
16826 O OE1 . GLN D 514 ? 0.2807 0.2513 0.5264 0.0245  -0.0219 -0.0049 514 GLN D OE1 
16827 N NE2 . GLN D 514 ? 0.2865 0.2669 0.5421 0.0300  -0.0243 0.0008  514 GLN D NE2 
16828 N N   . LYS D 515 ? 0.3481 0.2921 0.5873 0.0473  -0.0162 0.0001  515 LYS D N   
16829 C CA  . LYS D 515 ? 0.3445 0.2874 0.5847 0.0489  -0.0194 0.0040  515 LYS D CA  
16830 C C   . LYS D 515 ? 0.3457 0.2837 0.5800 0.0422  -0.0225 0.0035  515 LYS D C   
16831 O O   . LYS D 515 ? 0.3716 0.3004 0.5985 0.0388  -0.0212 0.0003  515 LYS D O   
16832 C CB  . LYS D 515 ? 0.3501 0.2811 0.5858 0.0551  -0.0175 0.0049  515 LYS D CB  
16833 C CG  . LYS D 515 ? 0.3457 0.2782 0.5853 0.0631  -0.0132 0.0051  515 LYS D CG  
16834 C CD  . LYS D 515 ? 0.3212 0.2690 0.5732 0.0678  -0.0142 0.0099  515 LYS D CD  
16835 C CE  . LYS D 515 ? 0.3129 0.2625 0.5682 0.0754  -0.0087 0.0095  515 LYS D CE  
16836 N NZ  . LYS D 515 ? 0.3190 0.2862 0.5879 0.0788  -0.0095 0.0142  515 LYS D NZ  
16837 N N   . ILE D 516 ? 0.3253 0.2690 0.5622 0.0406  -0.0264 0.0068  516 ILE D N   
16838 C CA  . ILE D 516 ? 0.3246 0.2637 0.5552 0.0350  -0.0289 0.0067  516 ILE D CA  
16839 C C   . ILE D 516 ? 0.3179 0.2500 0.5450 0.0375  -0.0308 0.0104  516 ILE D C   
16840 O O   . ILE D 516 ? 0.3097 0.2473 0.5414 0.0410  -0.0332 0.0143  516 ILE D O   
16841 C CB  . ILE D 516 ? 0.3211 0.2705 0.5550 0.0305  -0.0316 0.0069  516 ILE D CB  
16842 C CG1 . ILE D 516 ? 0.3161 0.2701 0.5523 0.0280  -0.0295 0.0033  516 ILE D CG1 
16843 C CG2 . ILE D 516 ? 0.3333 0.2786 0.5606 0.0258  -0.0338 0.0074  516 ILE D CG2 
16844 C CD1 . ILE D 516 ? 0.3437 0.3071 0.5834 0.0242  -0.0319 0.0034  516 ILE D CD1 
16845 N N   . ILE D 517 ? 0.3418 0.2619 0.5607 0.0353  -0.0300 0.0097  517 ILE D N   
16846 C CA  . ILE D 517 ? 0.3660 0.2768 0.5806 0.0382  -0.0311 0.0132  517 ILE D CA  
16847 C C   . ILE D 517 ? 0.3660 0.2709 0.5731 0.0323  -0.0325 0.0139  517 ILE D C   
16848 O O   . ILE D 517 ? 0.3483 0.2498 0.5516 0.0272  -0.0309 0.0109  517 ILE D O   
16849 C CB  . ILE D 517 ? 0.3957 0.2948 0.6070 0.0428  -0.0279 0.0119  517 ILE D CB  
16850 C CG1 . ILE D 517 ? 0.4278 0.3338 0.6465 0.0490  -0.0256 0.0110  517 ILE D CG1 
16851 C CG2 . ILE D 517 ? 0.4146 0.3027 0.6211 0.0461  -0.0291 0.0159  517 ILE D CG2 
16852 C CD1 . ILE D 517 ? 0.4595 0.3538 0.6737 0.0534  -0.0214 0.0083  517 ILE D CD1 
16853 N N   . TYR D 518 ? 0.3587 0.2630 0.5640 0.0332  -0.0356 0.0184  518 TYR D N   
16854 C CA  . TYR D 518 ? 0.3624 0.2624 0.5605 0.0281  -0.0368 0.0199  518 TYR D CA  
16855 C C   . TYR D 518 ? 0.3868 0.2726 0.5778 0.0289  -0.0364 0.0225  518 TYR D C   
16856 O O   . TYR D 518 ? 0.3827 0.2623 0.5742 0.0348  -0.0364 0.0245  518 TYR D O   
16857 C CB  . TYR D 518 ? 0.3566 0.2650 0.5560 0.0282  -0.0409 0.0232  518 TYR D CB  
16858 C CG  . TYR D 518 ? 0.3582 0.2792 0.5635 0.0265  -0.0419 0.0210  518 TYR D CG  
16859 C CD1 . TYR D 518 ? 0.3560 0.2798 0.5592 0.0210  -0.0406 0.0176  518 TYR D CD1 
16860 C CD2 . TYR D 518 ? 0.3593 0.2897 0.5724 0.0304  -0.0445 0.0228  518 TYR D CD2 
16861 C CE1 . TYR D 518 ? 0.3321 0.2659 0.5398 0.0195  -0.0418 0.0158  518 TYR D CE1 
16862 C CE2 . TYR D 518 ? 0.3639 0.3051 0.5820 0.0281  -0.0458 0.0211  518 TYR D CE2 
16863 C CZ  . TYR D 518 ? 0.3364 0.2785 0.5513 0.0227  -0.0445 0.0174  518 TYR D CZ  
16864 O OH  . TYR D 518 ? 0.3000 0.2512 0.5193 0.0207  -0.0459 0.0159  518 TYR D OH  
16865 N N   . ARG D 519 ? 0.3702 0.2509 0.5544 0.0231  -0.0361 0.0231  519 ARG D N   
16866 C CA  . ARG D 519 ? 0.3821 0.2503 0.5588 0.0227  -0.0364 0.0268  519 ARG D CA  
16867 C C   . ARG D 519 ? 0.3995 0.2706 0.5736 0.0236  -0.0399 0.0319  519 ARG D C   
16868 O O   . ARG D 519 ? 0.4031 0.2807 0.5752 0.0195  -0.0407 0.0320  519 ARG D O   
16869 C CB  . ARG D 519 ? 0.3642 0.2261 0.5351 0.0155  -0.0342 0.0256  519 ARG D CB  
16870 C CG  . ARG D 519 ? 0.3662 0.2142 0.5293 0.0143  -0.0344 0.0297  519 ARG D CG  
16871 C CD  . ARG D 519 ? 0.3625 0.2069 0.5211 0.0063  -0.0323 0.0293  519 ARG D CD  
16872 N NE  . ARG D 519 ? 0.3636 0.2046 0.5238 0.0038  -0.0303 0.0248  519 ARG D NE  
16873 C CZ  . ARG D 519 ? 0.3730 0.2011 0.5303 0.0052  -0.0298 0.0239  519 ARG D CZ  
16874 N NH1 . ARG D 519 ? 0.3752 0.1909 0.5274 0.0087  -0.0308 0.0274  519 ARG D NH1 
16875 N NH2 . ARG D 519 ? 0.3834 0.2101 0.5418 0.0028  -0.0284 0.0194  519 ARG D NH2 
16876 N N   . GLY D 520 ? 0.3968 0.2619 0.5699 0.0290  -0.0419 0.0362  520 GLY D N   
16877 C CA  . GLY D 520 ? 0.3948 0.2618 0.5648 0.0301  -0.0458 0.0415  520 GLY D CA  
16878 C C   . GLY D 520 ? 0.3774 0.2593 0.5525 0.0300  -0.0487 0.0411  520 GLY D C   
16879 O O   . GLY D 520 ? 0.3540 0.2448 0.5373 0.0319  -0.0483 0.0379  520 GLY D O   
16880 N N   . ASP D 521 ? 0.3922 0.2761 0.5614 0.0275  -0.0517 0.0442  521 ASP D N   
16881 C CA  . ASP D 521 ? 0.4153 0.3110 0.5875 0.0275  -0.0558 0.0448  521 ASP D CA  
16882 C C   . ASP D 521 ? 0.4030 0.3032 0.5708 0.0211  -0.0547 0.0412  521 ASP D C   
16883 O O   . ASP D 521 ? 0.4277 0.3348 0.5941 0.0198  -0.0583 0.0418  521 ASP D O   
16884 C CB  . ASP D 521 ? 0.4595 0.3538 0.6276 0.0301  -0.0609 0.0513  521 ASP D CB  
16885 C CG  . ASP D 521 ? 0.5000 0.3858 0.6553 0.0257  -0.0606 0.0539  521 ASP D CG  
16886 O OD1 . ASP D 521 ? 0.5158 0.3977 0.6670 0.0209  -0.0562 0.0506  521 ASP D OD1 
16887 O OD2 . ASP D 521 ? 0.5458 0.4300 0.6955 0.0267  -0.0648 0.0592  521 ASP D OD2 
16888 N N   . TRP D 522 ? 0.3660 0.2625 0.5317 0.0172  -0.0499 0.0376  522 TRP D N   
16889 C CA  . TRP D 522 ? 0.3688 0.2682 0.5291 0.0118  -0.0483 0.0352  522 TRP D CA  
16890 C C   . TRP D 522 ? 0.3615 0.2714 0.5265 0.0113  -0.0500 0.0318  522 TRP D C   
16891 O O   . TRP D 522 ? 0.3804 0.2925 0.5395 0.0080  -0.0502 0.0306  522 TRP D O   
16892 C CB  . TRP D 522 ? 0.3605 0.2560 0.5199 0.0079  -0.0430 0.0323  522 TRP D CB  
16893 C CG  . TRP D 522 ? 0.3618 0.2622 0.5297 0.0081  -0.0407 0.0273  522 TRP D CG  
16894 C CD1 . TRP D 522 ? 0.3642 0.2622 0.5381 0.0113  -0.0400 0.0261  522 TRP D CD1 
16895 C CD2 . TRP D 522 ? 0.3780 0.2861 0.5488 0.0056  -0.0390 0.0229  522 TRP D CD2 
16896 N NE1 . TRP D 522 ? 0.3650 0.2691 0.5451 0.0105  -0.0381 0.0215  522 TRP D NE1 
16897 C CE2 . TRP D 522 ? 0.3564 0.2668 0.5351 0.0071  -0.0376 0.0196  522 TRP D CE2 
16898 C CE3 . TRP D 522 ? 0.3801 0.2925 0.5468 0.0026  -0.0383 0.0215  522 TRP D CE3 
16899 C CZ2 . TRP D 522 ? 0.3545 0.2716 0.5375 0.0054  -0.0359 0.0155  522 TRP D CZ2 
16900 C CZ3 . TRP D 522 ? 0.3784 0.2968 0.5496 0.0013  -0.0365 0.0172  522 TRP D CZ3 
16901 C CH2 . TRP D 522 ? 0.3672 0.2882 0.5466 0.0025  -0.0354 0.0144  522 TRP D CH2 
16902 N N   . ALA D 523 ? 0.3621 0.2776 0.5370 0.0143  -0.0506 0.0300  523 ALA D N   
16903 C CA  . ALA D 523 ? 0.3685 0.2936 0.5487 0.0133  -0.0518 0.0267  523 ALA D CA  
16904 C C   . ALA D 523 ? 0.3795 0.3113 0.5628 0.0154  -0.0576 0.0296  523 ALA D C   
16905 O O   . ALA D 523 ? 0.3551 0.2950 0.5447 0.0150  -0.0590 0.0275  523 ALA D O   
16906 C CB  . ALA D 523 ? 0.3562 0.2842 0.5450 0.0146  -0.0486 0.0230  523 ALA D CB  
16907 N N   . LYS D 524 ? 0.4199 0.3486 0.5989 0.0173  -0.0612 0.0347  524 LYS D N   
16908 C CA  . LYS D 524 ? 0.4743 0.4102 0.6567 0.0190  -0.0675 0.0382  524 LYS D CA  
16909 C C   . LYS D 524 ? 0.4381 0.3805 0.6185 0.0145  -0.0705 0.0356  524 LYS D C   
16910 O O   . LYS D 524 ? 0.4577 0.4089 0.6455 0.0152  -0.0748 0.0367  524 LYS D O   
16911 C CB  . LYS D 524 ? 0.5158 0.4473 0.6928 0.0214  -0.0715 0.0444  524 LYS D CB  
16912 C CG  . LYS D 524 ? 0.6054 0.5318 0.7685 0.0177  -0.0741 0.0466  524 LYS D CG  
16913 C CD  . LYS D 524 ? 0.7077 0.6292 0.8668 0.0210  -0.0777 0.0534  524 LYS D CD  
16914 C CE  . LYS D 524 ? 0.7535 0.6683 0.8974 0.0178  -0.0798 0.0564  524 LYS D CE  
16915 N NZ  . LYS D 524 ? 0.7548 0.6622 0.8890 0.0135  -0.0740 0.0532  524 LYS D NZ  
16916 N N   . GLU D 525 ? 0.4111 0.3492 0.5821 0.0100  -0.0682 0.0322  525 GLU D N   
16917 C CA  . GLU D 525 ? 0.4028 0.3446 0.5702 0.0060  -0.0708 0.0293  525 GLU D CA  
16918 C C   . GLU D 525 ? 0.3998 0.3446 0.5730 0.0046  -0.0666 0.0239  525 GLU D C   
16919 O O   . GLU D 525 ? 0.3999 0.3511 0.5783 0.0033  -0.0692 0.0224  525 GLU D O   
16920 C CB  . GLU D 525 ? 0.4004 0.3355 0.5524 0.0023  -0.0712 0.0290  525 GLU D CB  
16921 C CG  . GLU D 525 ? 0.4070 0.3377 0.5510 0.0033  -0.0747 0.0345  525 GLU D CG  
16922 C CD  . GLU D 525 ? 0.4188 0.3411 0.5575 0.0046  -0.0701 0.0367  525 GLU D CD  
16923 O OE1 . GLU D 525 ? 0.4061 0.3259 0.5472 0.0043  -0.0638 0.0339  525 GLU D OE1 
16924 O OE2 . GLU D 525 ? 0.4186 0.3369 0.5504 0.0054  -0.0731 0.0416  525 GLU D OE2 
16925 N N   . VAL D 526 ? 0.3814 0.3217 0.5538 0.0045  -0.0603 0.0213  526 VAL D N   
16926 C CA  . VAL D 526 ? 0.3541 0.2966 0.5301 0.0029  -0.0565 0.0164  526 VAL D CA  
16927 C C   . VAL D 526 ? 0.3480 0.2965 0.5368 0.0054  -0.0557 0.0156  526 VAL D C   
16928 O O   . VAL D 526 ? 0.3274 0.2798 0.5204 0.0040  -0.0545 0.0122  526 VAL D O   
16929 C CB  . VAL D 526 ? 0.3552 0.2921 0.5257 0.0013  -0.0506 0.0141  526 VAL D CB  
16930 C CG1 . VAL D 526 ? 0.3536 0.2866 0.5267 0.0031  -0.0473 0.0157  526 VAL D CG1 
16931 C CG2 . VAL D 526 ? 0.3457 0.2853 0.5191 -0.0003 -0.0474 0.0094  526 VAL D CG2 
16932 N N   . GLY D 527 ? 0.3484 0.2975 0.5431 0.0093  -0.0561 0.0186  527 GLY D N   
16933 C CA  . GLY D 527 ? 0.3422 0.2960 0.5476 0.0122  -0.0542 0.0176  527 GLY D CA  
16934 C C   . GLY D 527 ? 0.3595 0.3232 0.5735 0.0132  -0.0583 0.0191  527 GLY D C   
16935 O O   . GLY D 527 ? 0.3721 0.3387 0.5847 0.0126  -0.0635 0.0222  527 GLY D O   
16936 N N   . ARG D 528 ? 0.4080 0.3774 0.6308 0.0143  -0.0561 0.0173  528 ARG D N   
16937 C CA  . ARG D 528 ? 0.4559 0.4358 0.6879 0.0146  -0.0595 0.0189  528 ARG D CA  
16938 C C   . ARG D 528 ? 0.4835 0.4678 0.7216 0.0195  -0.0622 0.0241  528 ARG D C   
16939 O O   . ARG D 528 ? 0.4592 0.4388 0.6978 0.0240  -0.0594 0.0252  528 ARG D O   
16940 C CB  . ARG D 528 ? 0.4477 0.4326 0.6876 0.0150  -0.0558 0.0162  528 ARG D CB  
16941 C CG  . ARG D 528 ? 0.4069 0.4034 0.6563 0.0141  -0.0590 0.0180  528 ARG D CG  
16942 C CD  . ARG D 528 ? 0.3741 0.3753 0.6314 0.0156  -0.0546 0.0162  528 ARG D CD  
16943 N NE  . ARG D 528 ? 0.3595 0.3562 0.6122 0.0121  -0.0516 0.0115  528 ARG D NE  
16944 C CZ  . ARG D 528 ? 0.3863 0.3759 0.6345 0.0128  -0.0470 0.0083  528 ARG D CZ  
16945 N NH1 . ARG D 528 ? 0.3888 0.3734 0.6358 0.0167  -0.0444 0.0088  528 ARG D NH1 
16946 N NH2 . ARG D 528 ? 0.3608 0.3478 0.6055 0.0094  -0.0452 0.0048  528 ARG D NH2 
16947 N N   . LYS D 529 ? 0.5247 0.5178 0.7674 0.0184  -0.0680 0.0275  529 LYS D N   
16948 C CA  . LYS D 529 ? 0.6900 0.6888 0.9395 0.0231  -0.0712 0.0332  529 LYS D CA  
16949 C C   . LYS D 529 ? 0.6653 0.6759 0.9295 0.0270  -0.0697 0.0349  529 LYS D C   
16950 O O   . LYS D 529 ? 0.6155 0.6325 0.8845 0.0235  -0.0694 0.0328  529 LYS D O   
16951 C CB  . LYS D 529 ? 0.7956 0.7983 1.0420 0.0198  -0.0790 0.0367  529 LYS D CB  
16952 C CG  . LYS D 529 ? 0.8013 0.7934 1.0339 0.0182  -0.0810 0.0373  529 LYS D CG  
16953 C CD  . LYS D 529 ? 0.8327 0.8177 1.0536 0.0120  -0.0802 0.0324  529 LYS D CD  
16954 C CE  . LYS D 529 ? 0.8224 0.7974 1.0295 0.0108  -0.0812 0.0333  529 LYS D CE  
16955 N NZ  . LYS D 529 ? 0.8452 0.8145 1.0416 0.0054  -0.0801 0.0286  529 LYS D NZ  
# 
