data_9G5G
# 
_entry.id   9G5G 
# 
_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   9G5G         pdb_00009g5g 10.2210/pdb9g5g/pdb 
WWPDB D_1292140358 ?            ?                   
# 
_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                        9G5G 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-16 
_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              pedrobuleg@gmail.com 
_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' 61514.047 4   ? ? ? ? 
2 branched    man 'beta-D-glucopyranose-(1-3)-beta-D-glucopyranose'                  342.297   2   ? ? ? ? 
3 non-polymer syn 'MALONIC ACID'                                                     104.061   4   ? ? ? ? 
4 non-polymer syn GLYCEROL                                                           92.094    4   ? ? ? ? 
5 non-polymer syn beta-D-glucopyranose                                               180.156   2   ? ? ? ? 
6 non-polymer syn 'TETRAETHYLENE GLYCOL'                                             194.226   1   ? ? ? ? 
7 water       nat water                                                              18.015    189 ? ? ? ? 
# 
_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
HPGIPVTLSANAMISDYMDESIFDVYAYNCYDHNEGQTATMGFKDYIKGLNELNGLDKPFITTEFGYSVSPEGGNGQYGS
NTLKQQSDGLISNYRDLIDAGAVGMCPFYYADGWWKGGEKSDHSLNQPEEWFGFWGYSDLNDKYGTPRPVWFAMRDYMKG
LIISPKNKSIHTNTKIPLELYNDKDVKKVVVKFRDKVIYSKNITSEGYMADELTIDPVGIEDMELAFEFYDSDNKIIKNE
SINILASKTAFELPELTIEVTPEKDLNEGKIASIKTKIETSENFTLLDDLKISYNTHLGWAIGSQASVSISDQLDKKIIT
SENFFNIPDNCWVVNASAGISVRYGKFTFKIHDQKIIYRGDWAKEVGRKLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MQSKTKIELKDNWYHLDGEKYFIKAIGYEIGARPGQAPYEDERKDELELMKFDLENIKEGGYNTIRTWSQYSENQLKLVQ
ESGLKLIMGIDIKPEEDYGDPEFVKDSEIELKRVLNYAKKYDCIITYLVINEPQTDHIHSVTGKAFVDLMNTLINIIHKG
HPGIPVTLSANAMISDYMDESIFDVYAYNCYDHNEGQTATMGFKDYIKGLNELNGLDKPFITTEFGYSVSPEGGNGQYGS
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 'MALONIC ACID'         MLA 
4 GLYCEROL               GOL 
5 beta-D-glucopyranose   BGC 
6 'TETRAETHYLENE GLYCOL' PG4 
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 GLU 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-ROH                        'Glycam Condensed Sequence' GMML       1.0   
2 2 'WURCS=2.0/1,2,1/[a2122h-1b_1-5]/1-1/a3-b1' WURCS                       PDB2Glycan 1.1.0 
3 2 '[][b-D-Glcp]{[(3+1)][b-D-Glcp]{}}'         LINUCS                      PDB-CARE   ?     
# 
_pdbx_entity_branch_link.link_id                    1 
_pdbx_entity_branch_link.entity_id                  2 
_pdbx_entity_branch_link.entity_branch_list_num_1   2 
_pdbx_entity_branch_link.comp_id_1                  BGC 
_pdbx_entity_branch_link.atom_id_1                  C1 
_pdbx_entity_branch_link.leaving_atom_id_1          O1 
_pdbx_entity_branch_link.entity_branch_list_num_2   1 
_pdbx_entity_branch_link.comp_id_2                  BGC 
_pdbx_entity_branch_link.atom_id_2                  O3 
_pdbx_entity_branch_link.leaving_atom_id_2          HO3 
_pdbx_entity_branch_link.value_order                sing 
_pdbx_entity_branch_link.details                    ? 
# 
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 
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 
MLA non-polymer                  . 'MALONIC ACID'         'DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID; METHANEDICARBOXYLIC ACID' 
'C3 H4 O4'       104.061 
PG4 non-polymer                  . 'TETRAETHYLENE GLYCOL' ?                                                                    
'C8 H18 O5'      194.226 
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 GLU 224 224 224 GLU GLU 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   3   SER SER 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 GLU 224 224 224 GLU GLU 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 530 530 530 LEU LEU 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 GLU 224 224 224 GLU GLU 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 530 530 530 LEU LEU 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 GLU 224 224 224 GLU GLU 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 530 530 530 LEU LEU 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 
F 2 BGC 1 F BGC 1 F BGC 1 n 
F 2 BGC 2 F BGC 2 F BGC 2 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 
G 3 MLA 1  601 601 MLA MLA A . 
H 3 MLA 1  602 602 MLA MLA A . 
I 4 GOL 1  603 601 GOL GOL A . 
J 4 GOL 1  604 602 GOL GOL A . 
K 4 GOL 1  601 601 GOL GOL B . 
L 5 BGC 1  602 6   BGC BGC B . 
M 4 GOL 1  601 602 GOL GOL C . 
N 3 MLA 1  602 602 MLA MLA C . 
O 6 PG4 1  603 603 PG4 PG4 C . 
P 5 BGC 1  601 3   BGC BGC D . 
Q 3 MLA 1  602 1   MLA MLA D . 
R 7 HOH 1  701 331 HOH HOH A . 
R 7 HOH 2  702 119 HOH HOH A . 
R 7 HOH 3  703 282 HOH HOH A . 
R 7 HOH 4  704 135 HOH HOH A . 
R 7 HOH 5  705 246 HOH HOH A . 
R 7 HOH 6  706 66  HOH HOH A . 
R 7 HOH 7  707 259 HOH HOH A . 
R 7 HOH 8  708 142 HOH HOH A . 
R 7 HOH 9  709 70  HOH HOH A . 
R 7 HOH 10 710 167 HOH HOH A . 
R 7 HOH 11 711 49  HOH HOH A . 
R 7 HOH 12 712 144 HOH HOH A . 
R 7 HOH 13 713 38  HOH HOH A . 
R 7 HOH 14 714 56  HOH HOH A . 
R 7 HOH 15 715 52  HOH HOH A . 
R 7 HOH 16 716 116 HOH HOH A . 
R 7 HOH 17 717 33  HOH HOH A . 
R 7 HOH 18 718 324 HOH HOH A . 
R 7 HOH 19 719 84  HOH HOH A . 
R 7 HOH 20 720 172 HOH HOH A . 
R 7 HOH 21 721 347 HOH HOH A . 
R 7 HOH 22 722 204 HOH HOH A . 
R 7 HOH 23 723 261 HOH HOH A . 
R 7 HOH 24 724 230 HOH HOH A . 
R 7 HOH 25 725 4   HOH HOH A . 
R 7 HOH 26 726 224 HOH HOH A . 
R 7 HOH 27 727 185 HOH HOH A . 
R 7 HOH 28 728 132 HOH HOH A . 
R 7 HOH 29 729 102 HOH HOH A . 
R 7 HOH 30 730 256 HOH HOH A . 
R 7 HOH 31 731 305 HOH HOH A . 
R 7 HOH 32 732 111 HOH HOH A . 
R 7 HOH 33 733 342 HOH HOH A . 
R 7 HOH 34 734 178 HOH HOH A . 
R 7 HOH 35 735 289 HOH HOH A . 
R 7 HOH 36 736 134 HOH HOH A . 
R 7 HOH 37 737 320 HOH HOH A . 
R 7 HOH 38 738 15  HOH HOH A . 
R 7 HOH 39 739 328 HOH HOH A . 
R 7 HOH 40 740 1   HOH HOH A . 
R 7 HOH 41 741 133 HOH HOH A . 
R 7 HOH 42 742 50  HOH HOH A . 
R 7 HOH 43 743 184 HOH HOH A . 
R 7 HOH 44 744 157 HOH HOH A . 
R 7 HOH 45 745 61  HOH HOH A . 
R 7 HOH 46 746 283 HOH HOH A . 
R 7 HOH 47 747 117 HOH HOH A . 
R 7 HOH 48 748 95  HOH HOH A . 
R 7 HOH 49 749 182 HOH HOH A . 
R 7 HOH 50 750 239 HOH HOH A . 
R 7 HOH 51 751 146 HOH HOH A . 
R 7 HOH 52 752 96  HOH HOH A . 
R 7 HOH 53 753 110 HOH HOH A . 
R 7 HOH 54 754 164 HOH HOH A . 
R 7 HOH 55 755 195 HOH HOH A . 
R 7 HOH 56 756 277 HOH HOH A . 
R 7 HOH 57 757 114 HOH HOH A . 
R 7 HOH 58 758 276 HOH HOH A . 
R 7 HOH 59 759 161 HOH HOH A . 
R 7 HOH 60 760 109 HOH HOH A . 
R 7 HOH 61 761 214 HOH HOH A . 
R 7 HOH 62 762 221 HOH HOH A . 
R 7 HOH 63 763 238 HOH HOH A . 
R 7 HOH 64 764 341 HOH HOH A . 
R 7 HOH 65 765 171 HOH HOH A . 
R 7 HOH 66 766 115 HOH HOH A . 
R 7 HOH 67 767 343 HOH HOH A . 
R 7 HOH 68 768 225 HOH HOH A . 
R 7 HOH 69 769 340 HOH HOH A . 
R 7 HOH 70 770 112 HOH HOH A . 
S 7 HOH 1  701 104 HOH HOH B . 
S 7 HOH 2  702 94  HOH HOH B . 
S 7 HOH 3  703 241 HOH HOH B . 
S 7 HOH 4  704 193 HOH HOH B . 
S 7 HOH 5  705 210 HOH HOH B . 
S 7 HOH 6  706 16  HOH HOH B . 
S 7 HOH 7  707 209 HOH HOH B . 
S 7 HOH 8  708 271 HOH HOH B . 
S 7 HOH 9  709 217 HOH HOH B . 
S 7 HOH 10 710 188 HOH HOH B . 
S 7 HOH 11 711 183 HOH HOH B . 
S 7 HOH 12 712 98  HOH HOH B . 
S 7 HOH 13 713 228 HOH HOH B . 
S 7 HOH 14 714 92  HOH HOH B . 
S 7 HOH 15 715 223 HOH HOH B . 
S 7 HOH 16 716 317 HOH HOH B . 
S 7 HOH 17 717 6   HOH HOH B . 
S 7 HOH 18 718 226 HOH HOH B . 
S 7 HOH 19 719 191 HOH HOH B . 
S 7 HOH 20 720 252 HOH HOH B . 
S 7 HOH 21 721 72  HOH HOH B . 
S 7 HOH 22 722 45  HOH HOH B . 
S 7 HOH 23 723 28  HOH HOH B . 
S 7 HOH 24 724 268 HOH HOH B . 
S 7 HOH 25 725 251 HOH HOH B . 
S 7 HOH 26 726 37  HOH HOH B . 
S 7 HOH 27 727 105 HOH HOH B . 
S 7 HOH 28 728 265 HOH HOH B . 
S 7 HOH 29 729 333 HOH HOH B . 
S 7 HOH 30 730 280 HOH HOH B . 
S 7 HOH 31 731 89  HOH HOH B . 
S 7 HOH 32 732 155 HOH HOH B . 
S 7 HOH 33 733 138 HOH HOH B . 
S 7 HOH 34 734 215 HOH HOH B . 
S 7 HOH 35 735 83  HOH HOH B . 
T 7 HOH 1  701 69  HOH HOH C . 
T 7 HOH 2  702 25  HOH HOH C . 
T 7 HOH 3  703 170 HOH HOH C . 
T 7 HOH 4  704 143 HOH HOH C . 
T 7 HOH 5  705 136 HOH HOH C . 
T 7 HOH 6  706 235 HOH HOH C . 
T 7 HOH 7  707 88  HOH HOH C . 
T 7 HOH 8  708 275 HOH HOH C . 
T 7 HOH 9  709 51  HOH HOH C . 
T 7 HOH 10 710 279 HOH HOH C . 
T 7 HOH 11 711 80  HOH HOH C . 
T 7 HOH 12 712 163 HOH HOH C . 
T 7 HOH 13 713 198 HOH HOH C . 
T 7 HOH 14 714 127 HOH HOH C . 
T 7 HOH 15 715 266 HOH HOH C . 
T 7 HOH 16 716 334 HOH HOH C . 
T 7 HOH 17 717 220 HOH HOH C . 
T 7 HOH 18 718 247 HOH HOH C . 
T 7 HOH 19 719 321 HOH HOH C . 
T 7 HOH 20 720 281 HOH HOH C . 
T 7 HOH 21 721 57  HOH HOH C . 
T 7 HOH 22 722 315 HOH HOH C . 
T 7 HOH 23 723 186 HOH HOH C . 
T 7 HOH 24 724 227 HOH HOH C . 
T 7 HOH 25 725 260 HOH HOH C . 
T 7 HOH 26 726 41  HOH HOH C . 
T 7 HOH 27 727 290 HOH HOH C . 
T 7 HOH 28 728 187 HOH HOH C . 
T 7 HOH 29 729 314 HOH HOH C . 
U 7 HOH 1  701 34  HOH HOH D . 
U 7 HOH 2  702 237 HOH HOH D . 
U 7 HOH 3  703 346 HOH HOH D . 
U 7 HOH 4  704 30  HOH HOH D . 
U 7 HOH 5  705 174 HOH HOH D . 
U 7 HOH 6  706 338 HOH HOH D . 
U 7 HOH 7  707 68  HOH HOH D . 
U 7 HOH 8  708 43  HOH HOH D . 
U 7 HOH 9  709 302 HOH HOH D . 
U 7 HOH 10 710 152 HOH HOH D . 
U 7 HOH 11 711 18  HOH HOH D . 
U 7 HOH 12 712 24  HOH HOH D . 
U 7 HOH 13 713 313 HOH HOH D . 
U 7 HOH 14 714 222 HOH HOH D . 
U 7 HOH 15 715 31  HOH HOH D . 
U 7 HOH 16 716 100 HOH HOH D . 
U 7 HOH 17 717 103 HOH HOH D . 
U 7 HOH 18 718 329 HOH HOH D . 
U 7 HOH 19 719 139 HOH HOH D . 
U 7 HOH 20 720 17  HOH HOH D . 
U 7 HOH 21 721 126 HOH HOH D . 
U 7 HOH 22 722 7   HOH HOH D . 
U 7 HOH 23 723 168 HOH HOH D . 
U 7 HOH 24 724 162 HOH HOH D . 
U 7 HOH 25 725 153 HOH HOH D . 
U 7 HOH 26 726 310 HOH HOH D . 
U 7 HOH 27 727 27  HOH HOH D . 
U 7 HOH 28 728 71  HOH HOH D . 
U 7 HOH 29 729 65  HOH HOH D . 
U 7 HOH 30 730 206 HOH HOH D . 
U 7 HOH 31 731 179 HOH HOH D . 
U 7 HOH 32 732 307 HOH HOH D . 
U 7 HOH 33 733 93  HOH HOH D . 
U 7 HOH 34 734 85  HOH HOH D . 
U 7 HOH 35 735 150 HOH HOH D . 
U 7 HOH 36 736 99  HOH HOH D . 
U 7 HOH 37 737 298 HOH HOH D . 
U 7 HOH 38 738 60  HOH HOH D . 
U 7 HOH 39 739 190 HOH HOH D . 
U 7 HOH 40 740 234 HOH HOH D . 
U 7 HOH 41 741 10  HOH HOH D . 
U 7 HOH 42 742 287 HOH HOH D . 
U 7 HOH 43 743 107 HOH HOH D . 
U 7 HOH 44 744 249 HOH HOH D . 
U 7 HOH 45 745 97  HOH HOH D . 
U 7 HOH 46 746 244 HOH HOH D . 
U 7 HOH 47 747 197 HOH HOH D . 
U 7 HOH 48 748 203 HOH HOH D . 
U 7 HOH 49 749 245 HOH HOH D . 
U 7 HOH 50 750 292 HOH HOH D . 
U 7 HOH 51 751 106 HOH HOH D . 
U 7 HOH 52 752 46  HOH HOH D . 
U 7 HOH 53 753 344 HOH HOH D . 
U 7 HOH 54 754 335 HOH HOH D . 
U 7 HOH 55 755 345 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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        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                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G5G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     208.628 
_cell.length_a_esd                 ? 
_cell.length_b                     208.628 
_cell.length_b_esd                 ? 
_cell.length_c                     165.285 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        36 
_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                         9G5G 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'H 3' 
_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                   9G5G 
_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             2.81 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.28 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1M Sodium malonate, 10% PEG3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2021-10-12 
_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                                       9G5G 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.71 
_reflns.d_resolution_low                               121.95 
_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                                     71618 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.6 
_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                                0.182 
_reflns.pdbx_Rpim_I_all                                0.074 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       429854 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.166 
_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                                    2.71 
_reflns_shell.d_res_low                                     2.77 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           21966 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3895 
_reflns_shell.percent_possible_obs                          83.1 
_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                               5.6 
_reflns_shell.pdbx_chi_squared                              0.71 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               2.086 
_reflns_shell.pdbx_Rpim_I_all                               0.860 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.375 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.894 
_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]                            4.19 
_refine.aniso_B[1][2]                            2.10 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            4.19 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -13.60 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               84.207 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.938 
_refine.correlation_coeff_Fo_to_Fc_free          0.900 
_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                                 9G5G 
_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                            2.71 
_refine.ls_d_res_low                             121.95 
_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                     68000 
_refine.ls_number_reflns_R_free                  3618 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.55 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.21388 
_refine.ls_R_factor_R_free                       0.27230 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.21083 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.381 
_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                             52.537 
_refine.overall_SU_ML                            0.460 
_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                       2.71 
_refine_hist.d_res_low                        121.95 
_refine_hist.number_atoms_solvent             189 
_refine_hist.number_atoms_total               17324 
_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        17000 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         135 
_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' ? 0.007  0.012  17522 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  16232 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.623  1.820  23681 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.552  1.778  37666 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 8.031  5.000  2108  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.511  5.000  44    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 14.613 10.000 3116  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.073  0.200  2536  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  20200 ? 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' ? 1.054  1.499  8444  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.054  1.499  8444  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.769  2.691  10548 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.769  2.692  10549 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.439  1.649  9078  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.438  1.648  9077  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.204  2.979  13134 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.492  14.48  19649 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 7.491  14.46  19639 ? 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                       2.712 
_refine_ls_shell.d_res_low                        2.783 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             237 
_refine_ls_shell.number_reflns_R_work             4357 
_refine_ls_shell.percent_reflns_obs               85.20 
_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                  0.355 
_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                  0.394 
# 
_struct.entry_id                     9G5G 
_struct.title                        
'Glycoside Hydrolase Family 157 from Labilibaculum antarcticum (LaGH157) in complex with Laminaribiose' 
_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        9G5G 
_struct_keywords.text            'Glycoside hydrolase, endo-beta-1, 3-glucanase, cazyme, ligand complex, 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 3 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 5 ? 
M N N 4 ? 
N N N 3 ? 
O N N 6 ? 
P N N 5 ? 
Q N N 3 ? 
R N N 7 ? 
S N N 7 ? 
T N N 7 ? 
U 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 9G5G A 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
2 1 9G5G B 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
3 1 9G5G C 2 ? 529 ? A0A1Y1CQ89 22 ? 549 ? 2 529 
4 1 9G5G 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 9G5G MET A 1   ? UNP A0A1Y1CQ89 ? ? 'initiating methionine' 1   1  
1 9G5G LEU A 530 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        530 2  
1 9G5G GLU A 531 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        531 3  
1 9G5G HIS A 532 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        532 4  
1 9G5G HIS A 533 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        533 5  
1 9G5G HIS A 534 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        534 6  
1 9G5G HIS A 535 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        535 7  
1 9G5G HIS A 536 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        536 8  
1 9G5G HIS A 537 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        537 9  
2 9G5G MET B 1   ? UNP A0A1Y1CQ89 ? ? 'initiating methionine' 1   10 
2 9G5G LEU B 530 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        530 11 
2 9G5G GLU B 531 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        531 12 
2 9G5G HIS B 532 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        532 13 
2 9G5G HIS B 533 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        533 14 
2 9G5G HIS B 534 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        534 15 
2 9G5G HIS B 535 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        535 16 
2 9G5G HIS B 536 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        536 17 
2 9G5G HIS B 537 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        537 18 
3 9G5G MET C 1   ? UNP A0A1Y1CQ89 ? ? 'initiating methionine' 1   19 
3 9G5G LEU C 530 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        530 20 
3 9G5G GLU C 531 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        531 21 
3 9G5G HIS C 532 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        532 22 
3 9G5G HIS C 533 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        533 23 
3 9G5G HIS C 534 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        534 24 
3 9G5G HIS C 535 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        535 25 
3 9G5G HIS C 536 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        536 26 
3 9G5G HIS C 537 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        537 27 
4 9G5G MET D 1   ? UNP A0A1Y1CQ89 ? ? 'initiating methionine' 1   28 
4 9G5G LEU D 530 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        530 29 
4 9G5G GLU D 531 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        531 30 
4 9G5G HIS D 532 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        532 31 
4 9G5G HIS D 533 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        533 32 
4 9G5G HIS D 534 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        534 33 
4 9G5G HIS D 535 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        535 34 
4 9G5G HIS D 536 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        536 35 
4 9G5G HIS D 537 ? UNP A0A1Y1CQ89 ? ? 'expression tag'        537 36 
# 
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,G,H,I,J,R 
2 1 B,K,L,S       
3 1 C,M,N,O,T     
4 1 D,F,P,Q,U     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_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 ? PHE A 292 ? GLN A 287 PHE A 292 5 ? 6  
HELX_P HELX_P11 AB2 ARG A 308 ? LYS A 319 ? ARG A 308 LYS A 319 1 ? 12 
HELX_P HELX_P12 AB3 ASP A 425 ? GLY A 429 ? ASP A 425 GLY A 429 5 ? 5  
HELX_P HELX_P13 AB4 SER A 471 ? LEU A 474 ? SER A 471 LEU A 474 5 ? 4  
HELX_P HELX_P14 AB5 GLU B 46  ? GLY B 61  ? GLU B 46  GLY B 61  1 ? 16 
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 GLY B 196 ? MET B 201 ? GLY B 196 MET B 201 1 ? 6  
HELX_P HELX_P20 AC2 GLY B 202 ? GLY B 215 ? GLY B 202 GLY B 215 1 ? 14 
HELX_P HELX_P21 AC3 THR B 242 ? ASP B 259 ? THR B 242 ASP B 259 1 ? 18 
HELX_P HELX_P22 AC4 GLY B 273 ? GLY B 278 ? GLY B 273 GLY B 278 5 ? 6  
HELX_P HELX_P23 AC5 GLN B 287 ? PHE B 292 ? GLN B 287 PHE B 292 5 ? 6  
HELX_P HELX_P24 AC6 ARG B 308 ? LYS B 319 ? ARG B 308 LYS B 319 1 ? 12 
HELX_P HELX_P25 AC7 ASP B 425 ? GLY B 429 ? ASP B 425 GLY B 429 5 ? 5  
HELX_P HELX_P26 AC8 SER B 471 ? LEU B 474 ? SER B 471 LEU B 474 5 ? 4  
HELX_P HELX_P27 AC9 GLU C 46  ? GLY C 60  ? GLU C 46  GLY C 60  1 ? 15 
HELX_P HELX_P28 AD1 SER C 72  ? GLY C 83  ? SER C 72  GLY C 83  1 ? 12 
HELX_P HELX_P29 AD2 ASP C 100 ? LYS C 119 ? ASP C 100 LYS C 119 1 ? 20 
HELX_P HELX_P30 AD3 GLN C 134 ? THR C 142 ? GLN C 134 THR C 142 1 ? 9  
HELX_P HELX_P31 AD4 THR C 142 ? HIS C 161 ? THR C 142 HIS C 161 1 ? 20 
HELX_P HELX_P32 AD5 GLY C 196 ? MET C 201 ? GLY C 196 MET C 201 1 ? 6  
HELX_P HELX_P33 AD6 GLY C 202 ? GLY C 215 ? GLY C 202 GLY C 215 1 ? 14 
HELX_P HELX_P34 AD7 THR C 242 ? ALA C 260 ? THR C 242 ALA C 260 1 ? 19 
HELX_P HELX_P35 AD8 GLN C 287 ? TRP C 291 ? GLN C 287 TRP C 291 5 ? 5  
HELX_P HELX_P36 AD9 ARG C 308 ? MET C 318 ? ARG C 308 MET C 318 1 ? 11 
HELX_P HELX_P37 AE1 ASP C 425 ? GLY C 429 ? ASP C 425 GLY C 429 5 ? 5  
HELX_P HELX_P38 AE2 ILE C 470 ? LEU C 474 ? ILE C 470 LEU C 474 5 ? 5  
HELX_P HELX_P39 AE3 GLU D 46  ? GLY D 60  ? GLU D 46  GLY D 60  1 ? 15 
HELX_P HELX_P40 AE4 SER D 72  ? GLY D 83  ? SER D 72  GLY D 83  1 ? 12 
HELX_P HELX_P41 AE5 ASP D 100 ? LYS D 119 ? ASP D 100 LYS D 119 1 ? 20 
HELX_P HELX_P42 AE6 GLN D 134 ? THR D 142 ? GLN D 134 THR D 142 1 ? 9  
HELX_P HELX_P43 AE7 THR D 142 ? HIS D 161 ? THR D 142 HIS D 161 1 ? 20 
HELX_P HELX_P44 AE8 GLY D 196 ? MET D 201 ? GLY D 196 MET D 201 1 ? 6  
HELX_P HELX_P45 AE9 GLY D 202 ? GLY D 215 ? GLY D 202 GLY D 215 1 ? 14 
HELX_P HELX_P46 AF1 THR D 242 ? ALA D 260 ? THR D 242 ALA D 260 1 ? 19 
HELX_P HELX_P47 AF2 GLN D 287 ? PHE D 292 ? GLN D 287 PHE D 292 5 ? 6  
HELX_P HELX_P48 AF3 ARG D 308 ? MET D 318 ? ARG D 308 MET D 318 1 ? 11 
HELX_P HELX_P49 AF4 ASP D 425 ? GLY D 429 ? ASP D 425 GLY D 429 5 ? 5  
HELX_P HELX_P50 AF5 SER D 471 ? LEU D 474 ? SER D 471 LEU D 474 5 ? 4  
# 
_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 ? ? ? ? ? ? ? 1.392 ? ? 
covale2 covale both ? F BGC . O3 ? ? ? 1_555 F BGC . C1 ? ? F BGC 1 F BGC 2 1_555 ? ? ? ? ? ? ? 1.391 ? ? 
# 
_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 SER 324 A . ? SER 324 A PRO 325 A ? PRO 325 A 1 -5.91  
2 THR 421 A . ? THR 421 A PRO 422 A ? PRO 422 A 1 -12.83 
3 SER 324 B . ? SER 324 B PRO 325 B ? PRO 325 B 1 7.45   
4 THR 421 B . ? THR 421 B PRO 422 B ? PRO 422 B 1 -14.57 
5 SER 324 C . ? SER 324 C PRO 325 C ? PRO 325 C 1 -0.47  
6 THR 421 C . ? THR 421 C PRO 422 C ? PRO 422 C 1 -22.84 
7 SER 324 D . ? SER 324 D PRO 325 D ? PRO 325 D 1 -4.35  
8 THR 421 D . ? THR 421 D PRO 422 D ? PRO 422 D 1 -20.07 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 9 ? 
AA3 ? 2 ? 
AA4 ? 3 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
AA9 ? 4 ? 
AB1 ? 4 ? 
AB2 ? 2 ? 
AB3 ? 3 ? 
AB4 ? 5 ? 
AB5 ? 3 ? 
AB6 ? 4 ? 
AB7 ? 3 ? 
AB8 ? 3 ? 
AB9 ? 4 ? 
AC1 ? 4 ? 
AC2 ? 2 ? 
AC3 ? 3 ? 
AC4 ? 5 ? 
AC5 ? 4 ? 
AC6 ? 3 ? 
AC7 ? 4 ? 
AC8 ? 2 ? 
AC9 ? 6 ? 
AD1 ? 2 ? 
AD2 ? 2 ? 
AD3 ? 3 ? 
AD4 ? 5 ? 
AD5 ? 3 ? 
AD6 ? 4 ? 
AD7 ? 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      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? parallel      
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB5 2 3 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? parallel      
AB9 3 4 ? parallel      
AC1 1 2 ? parallel      
AC1 2 3 ? parallel      
AC1 3 4 ? 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 ? parallel      
AC5 2 3 ? anti-parallel 
AC5 3 4 ? anti-parallel 
AC6 1 2 ? anti-parallel 
AC6 2 3 ? anti-parallel 
AC7 1 2 ? anti-parallel 
AC7 2 3 ? anti-parallel 
AC7 3 4 ? anti-parallel 
AC8 1 2 ? anti-parallel 
AC9 1 2 ? parallel      
AC9 2 3 ? parallel      
AC9 3 4 ? parallel      
AC9 4 5 ? parallel      
AC9 5 6 ? parallel      
AD1 1 2 ? parallel      
AD2 1 2 ? anti-parallel 
AD3 1 2 ? anti-parallel 
AD3 2 3 ? anti-parallel 
AD4 1 2 ? parallel      
AD4 2 3 ? anti-parallel 
AD4 3 4 ? anti-parallel 
AD4 4 5 ? anti-parallel 
AD5 1 2 ? anti-parallel 
AD5 2 3 ? anti-parallel 
AD6 1 2 ? anti-parallel 
AD6 2 3 ? anti-parallel 
AD6 3 4 ? anti-parallel 
AD7 1 2 ? anti-parallel 
AD7 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 LEU A 9   ? LYS A 10  ? LEU A 9   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 ILE A 23  ? GLY A 27  ? ILE A 23  GLY A 27  
AA2 2 THR A 64  ? ARG A 66  ? THR A 64  ARG A 66  
AA2 3 LYS A 85  ? GLY A 89  ? LYS A 85  GLY A 89  
AA2 4 ILE A 124 ? ASN A 131 ? ILE A 124 ASN A 131 
AA2 5 VAL A 166 ? ASN A 171 ? VAL A 166 ASN A 171 
AA2 6 TYR A 186 ? ASN A 189 ? TYR A 186 ASN A 189 
AA2 7 PHE A 220 ? GLU A 224 ? PHE A 220 GLU A 224 
AA2 8 GLY A 264 ? MET A 265 ? GLY A 264 MET A 265 
AA2 9 ILE A 23  ? GLY A 27  ? ILE A 23  GLY A 27  
AA3 1 TRP A 295 ? GLY A 296 ? TRP A 295 GLY A 296 
AA3 2 THR A 306 ? PRO A 307 ? THR A 306 PRO A 307 
AA4 1 GLY A 320 ? SER A 324 ? GLY A 320 SER A 324 
AA4 2 LYS A 335 ? ASN A 342 ? LYS A 335 ASN A 342 
AA4 3 GLY A 367 ? THR A 374 ? GLY A 367 THR A 374 
AA5 1 SER A 329 ? HIS A 331 ? SER A 329 HIS A 331 
AA5 2 ILE A 396 ? ALA A 406 ? ILE A 396 ALA A 406 
AA5 3 GLU A 381 ? TYR A 390 ? GLU A 381 TYR A 390 
AA5 4 LYS A 348 ? PHE A 353 ? LYS A 348 PHE A 353 
AA5 5 LYS A 356 ? ASN A 362 ? LYS A 356 ASN A 362 
AA6 1 GLU A 415 ? THR A 421 ? GLU A 415 THR A 421 
AA6 2 ILE A 431 ? GLU A 439 ? ILE A 431 GLU A 439 
AA6 3 ILE A 478 ? ASN A 486 ? ILE A 478 ASN A 486 
AA7 1 SER A 464 ? SER A 469 ? SER A 464 SER A 469 
AA7 2 THR A 445 ? ASN A 455 ? THR A 445 ASN A 455 
AA7 3 VAL A 493 ? TYR A 504 ? VAL A 493 TYR A 504 
AA7 4 PHE A 507 ? TYR A 518 ? PHE A 507 TYR A 518 
AA8 1 ILE B 7   ? LYS B 10  ? ILE B 7   LYS B 10  
AA8 2 TRP B 13  ? LEU B 16  ? TRP B 13  LEU B 16  
AA8 3 GLU B 19  ? LYS B 20  ? GLU B 19  LYS B 20  
AA9 1 ILE B 23  ? LYS B 24  ? ILE B 23  LYS B 24  
AA9 2 GLY B 264 ? MET B 265 ? GLY B 264 MET B 265 
AA9 3 PHE B 220 ? GLU B 224 ? PHE B 220 GLU B 224 
AA9 4 TYR B 186 ? ASN B 189 ? TYR B 186 ASN B 189 
AB1 1 THR B 64  ? ARG B 66  ? THR B 64  ARG B 66  
AB1 2 LYS B 85  ? GLY B 89  ? LYS B 85  GLY B 89  
AB1 3 ILE B 124 ? ASN B 131 ? ILE B 124 ASN B 131 
AB1 4 VAL B 166 ? SER B 169 ? VAL B 166 SER B 169 
AB2 1 TRP B 295 ? GLY B 296 ? TRP B 295 GLY B 296 
AB2 2 THR B 306 ? PRO B 307 ? THR B 306 PRO B 307 
AB3 1 GLY B 320 ? SER B 324 ? GLY B 320 SER B 324 
AB3 2 LYS B 335 ? ASN B 342 ? LYS B 335 ASN B 342 
AB3 3 GLY B 367 ? THR B 374 ? GLY B 367 THR B 374 
AB4 1 SER B 329 ? THR B 332 ? SER B 329 THR B 332 
AB4 2 ILE B 396 ? SER B 407 ? ILE B 396 SER B 407 
AB4 3 GLU B 381 ? TYR B 390 ? GLU B 381 TYR B 390 
AB4 4 LYS B 348 ? LYS B 352 ? LYS B 348 LYS B 352 
AB4 5 VAL B 357 ? ASN B 362 ? VAL B 357 ASN B 362 
AB5 1 GLU B 415 ? THR B 421 ? GLU B 415 THR B 421 
AB5 2 ILE B 431 ? GLU B 439 ? ILE B 431 GLU B 439 
AB5 3 ILE B 478 ? ASN B 486 ? ILE B 478 ASN B 486 
AB6 1 THR B 445 ? LEU B 446 ? THR B 445 LEU B 446 
AB6 2 VAL B 493 ? TYR B 504 ? VAL B 493 TYR B 504 
AB6 3 ASP B 449 ? ASN B 455 ? ASP B 449 ASN B 455 
AB6 4 SER B 464 ? SER B 469 ? SER B 464 SER B 469 
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 PHE B 507 ? TYR B 518 ? PHE B 507 TYR B 518 
AB8 1 ILE C 7   ? LYS C 10  ? ILE C 7   LYS C 10  
AB8 2 TRP C 13  ? LEU C 16  ? TRP C 13  LEU C 16  
AB8 3 GLU C 19  ? LYS C 20  ? GLU C 19  LYS C 20  
AB9 1 ILE C 23  ? LYS C 24  ? ILE C 23  LYS C 24  
AB9 2 GLY C 264 ? MET C 265 ? GLY C 264 MET C 265 
AB9 3 PHE C 220 ? GLU C 224 ? PHE C 220 GLU C 224 
AB9 4 TYR C 186 ? ASN C 189 ? TYR C 186 ASN C 189 
AC1 1 THR C 64  ? ARG C 66  ? THR C 64  ARG C 66  
AC1 2 LYS C 85  ? GLY C 89  ? LYS C 85  GLY C 89  
AC1 3 ILE C 124 ? ASN C 131 ? ILE C 124 ASN C 131 
AC1 4 VAL C 166 ? SER C 169 ? VAL C 166 SER C 169 
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 SER C 401 ? ALA C 406 ? SER C 401 ALA C 406 
AC4 3 GLU C 381 ? TYR C 390 ? GLU C 381 TYR C 390 
AC4 4 LYS C 348 ? LYS C 352 ? LYS C 348 LYS C 352 
AC4 5 VAL C 357 ? ASN C 362 ? VAL C 357 ASN C 362 
AC5 1 SER C 329 ? HIS C 331 ? SER C 329 HIS C 331 
AC5 2 SER C 401 ? ALA C 406 ? SER C 401 ALA C 406 
AC5 3 GLU C 381 ? TYR C 390 ? GLU C 381 TYR C 390 
AC5 4 ILE C 396 ? LYS C 398 ? ILE C 396 LYS C 398 
AC6 1 GLU C 415 ? THR C 421 ? GLU C 415 THR C 421 
AC6 2 ILE C 431 ? GLU C 439 ? ILE C 431 GLU C 439 
AC6 3 ILE C 478 ? ASN C 486 ? ILE C 478 ASN C 486 
AC7 1 SER C 464 ? VAL C 468 ? SER C 464 VAL C 468 
AC7 2 THR C 445 ? ASN C 455 ? THR C 445 ASN C 455 
AC7 3 VAL C 493 ? TYR C 504 ? VAL C 493 TYR C 504 
AC7 4 PHE C 507 ? TYR C 518 ? PHE C 507 TYR C 518 
AC8 1 HIS D 15  ? LEU D 16  ? HIS D 15  LEU D 16  
AC8 2 GLU D 19  ? LYS D 20  ? GLU D 19  LYS D 20  
AC9 1 VAL D 166 ? SER D 169 ? VAL D 166 SER D 169 
AC9 2 ILE D 124 ? ASN D 131 ? ILE D 124 ASN D 131 
AC9 3 LYS D 85  ? GLY D 89  ? LYS D 85  GLY D 89  
AC9 4 THR D 64  ? ARG D 66  ? THR D 64  ARG D 66  
AC9 5 ILE D 23  ? GLY D 27  ? ILE D 23  GLY D 27  
AC9 6 GLY D 264 ? MET D 265 ? GLY D 264 MET D 265 
AD1 1 TYR D 186 ? ASN D 189 ? TYR D 186 ASN D 189 
AD1 2 PHE D 220 ? GLU D 224 ? PHE D 220 GLU D 224 
AD2 1 TRP D 295 ? GLY D 296 ? TRP D 295 GLY D 296 
AD2 2 THR D 306 ? PRO D 307 ? THR D 306 PRO D 307 
AD3 1 GLY D 320 ? SER D 324 ? GLY D 320 SER D 324 
AD3 2 LYS D 335 ? ASN D 342 ? LYS D 335 ASN D 342 
AD3 3 GLY D 367 ? THR D 374 ? GLY D 367 THR D 374 
AD4 1 SER D 329 ? HIS D 331 ? SER D 329 HIS D 331 
AD4 2 ILE D 396 ? SER D 407 ? ILE D 396 SER D 407 
AD4 3 ILE D 380 ? TYR D 390 ? ILE D 380 TYR D 390 
AD4 4 LYS D 348 ? PHE D 353 ? LYS D 348 PHE D 353 
AD4 5 LYS D 356 ? ASN D 362 ? LYS D 356 ASN D 362 
AD5 1 GLU D 415 ? THR D 421 ? GLU D 415 THR D 421 
AD5 2 ILE D 431 ? GLU D 439 ? ILE D 431 GLU D 439 
AD5 3 ILE D 478 ? ASN D 486 ? ILE D 478 ASN D 486 
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 ASP D 449 ? ASN D 455 ? ASP D 449 ASN D 455 
AD6 4 SER D 464 ? SER D 469 ? SER D 464 SER D 469 
AD7 1 THR D 445 ? LEU D 446 ? THR D 445 LEU D 446 
AD7 2 VAL D 493 ? TYR D 504 ? VAL D 493 TYR D 504 
AD7 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 N ILE A 26  ? N ILE A 26  O ARG A 66  ? O ARG A 66  
AA2 2 3 N ILE A 65  ? N ILE A 65  O ILE A 87  ? O ILE A 87  
AA2 3 4 N MET A 88  ? N MET A 88  O THR A 126 ? O THR A 126 
AA2 4 5 N ILE A 130 ? N ILE A 130 O SER A 169 ? O SER A 169 
AA2 5 6 N ALA A 170 ? N ALA A 170 O ASN A 189 ? O ASN A 189 
AA2 6 7 N TYR A 186 ? N TYR A 186 O ILE A 221 ? O ILE A 221 
AA2 7 8 N THR A 222 ? N THR A 222 O GLY A 264 ? O GLY A 264 
AA2 8 9 O MET A 265 ? O MET A 265 N ILE A 23  ? N ILE A 23  
AA3 1 2 N GLY A 296 ? N GLY A 296 O THR A 306 ? O THR A 306 
AA4 1 2 N ILE A 323 ? N ILE A 323 O GLU A 339 ? O GLU A 339 
AA4 2 3 N ILE A 336 ? N ILE A 336 O LEU A 373 ? O LEU A 373 
AA5 1 2 N HIS A 331 ? N HIS A 331 O LEU A 405 ? O LEU A 405 
AA5 2 3 O ILE A 402 ? O ILE A 402 N LEU A 385 ? N LEU A 385 
AA5 3 4 O ALA A 386 ? O ALA A 386 N LYS A 352 ? N LYS A 352 
AA5 4 5 N VAL A 351 ? N VAL A 351 O ILE A 358 ? O ILE A 358 
AA6 1 2 N GLU A 415 ? N GLU A 415 O GLU A 439 ? O GLU A 439 
AA6 2 3 N ALA A 432 ? N ALA A 432 O PHE A 485 ? O PHE A 485 
AA7 1 2 O ALA A 466 ? O ALA A 466 N ILE A 452 ? N ILE A 452 
AA7 2 3 N LYS A 451 ? N LYS A 451 O GLY A 499 ? O GLY A 499 
AA7 3 4 N ALA A 496 ? N ALA A 496 O LYS A 515 ? O LYS A 515 
AA8 1 2 N GLU B 8   ? N GLU B 8   O HIS B 15  ? O HIS B 15  
AA8 2 3 N LEU B 16  ? N LEU B 16  O GLU B 19  ? O GLU B 19  
AA9 1 2 N ILE B 23  ? N ILE B 23  O MET B 265 ? O MET B 265 
AA9 2 3 O GLY B 264 ? O GLY B 264 N THR B 222 ? N THR B 222 
AA9 3 4 O ILE B 221 ? O ILE B 221 N TYR B 186 ? N TYR B 186 
AB1 1 2 N ILE B 65  ? N ILE B 65  O ILE B 87  ? O ILE B 87  
AB1 2 3 N LEU B 86  ? N LEU B 86  O ILE B 125 ? O ILE B 125 
AB1 3 4 N TYR B 127 ? N TYR B 127 O THR B 167 ? O THR B 167 
AB2 1 2 N GLY B 296 ? N GLY B 296 O THR B 306 ? O THR B 306 
AB3 1 2 N ILE B 323 ? N ILE B 323 O GLU B 339 ? O GLU B 339 
AB3 2 3 N LEU B 338 ? N LEU B 338 O ASP B 371 ? O ASP B 371 
AB4 1 2 N HIS B 331 ? N HIS B 331 O SER B 407 ? O SER B 407 
AB4 2 3 O ILE B 402 ? O ILE B 402 N LEU B 385 ? N LEU B 385 
AB4 3 4 O TYR B 390 ? O TYR B 390 N LYS B 348 ? N LYS B 348 
AB4 4 5 N VAL B 351 ? N VAL B 351 O ILE B 358 ? O ILE B 358 
AB5 1 2 N GLU B 415 ? N GLU B 415 O GLU B 439 ? O GLU B 439 
AB5 2 3 N THR B 436 ? N THR B 436 O SER B 481 ? O SER B 481 
AB6 1 2 N THR B 445 ? N THR B 445 O ARG B 503 ? O ARG B 503 
AB6 2 3 O SER B 497 ? O SER B 497 N SER B 453 ? N SER B 453 
AB6 3 4 N ILE B 452 ? N ILE B 452 O ALA B 466 ? O ALA B 466 
AB7 1 2 N THR B 445 ? N THR B 445 O ARG B 503 ? O ARG B 503 
AB7 2 3 N VAL B 502 ? N VAL B 502 O PHE B 509 ? O PHE B 509 
AB8 1 2 N LYS C 10  ? N LYS C 10  O TRP C 13  ? O TRP C 13  
AB8 2 3 N LEU C 16  ? N LEU C 16  O GLU C 19  ? O GLU C 19  
AB9 1 2 N ILE C 23  ? N ILE C 23  O MET C 265 ? O MET C 265 
AB9 2 3 O GLY C 264 ? O GLY C 264 N THR C 222 ? N THR C 222 
AB9 3 4 O ILE C 221 ? O ILE C 221 N TYR C 186 ? N TYR C 186 
AC1 1 2 N ILE C 65  ? N ILE C 65  O ILE C 87  ? O ILE C 87  
AC1 2 3 N LEU C 86  ? N LEU C 86  O ILE C 125 ? O ILE C 125 
AC1 3 4 N ILE C 130 ? N ILE C 130 O SER C 169 ? O SER C 169 
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 ALA C 406 ? O ALA C 406 N GLU C 381 ? N GLU C 381 
AC4 3 4 O ALA C 386 ? O ALA C 386 N LYS C 352 ? N LYS C 352 
AC4 4 5 N VAL C 351 ? N VAL C 351 O ILE C 358 ? O ILE C 358 
AC5 1 2 N HIS C 331 ? N HIS C 331 O LEU C 405 ? O LEU C 405 
AC5 2 3 O ALA C 406 ? O ALA C 406 N GLU C 381 ? N GLU C 381 
AC5 3 4 N PHE C 389 ? N PHE C 389 O ILE C 397 ? O ILE C 397 
AC6 1 2 N GLU C 415 ? N GLU C 415 O GLU C 439 ? O GLU C 439 
AC6 2 3 N ALA C 432 ? N ALA C 432 O PHE C 485 ? O PHE C 485 
AC7 1 2 O VAL C 468 ? O VAL C 468 N LEU C 450 ? N LEU C 450 
AC7 2 3 N LYS C 451 ? N LYS C 451 O GLY C 499 ? O GLY C 499 
AC7 3 4 N TYR C 504 ? N TYR C 504 O PHE C 507 ? O PHE C 507 
AC8 1 2 N LEU D 16  ? N LEU D 16  O GLU D 19  ? O GLU D 19  
AC9 1 2 O THR D 167 ? O THR D 167 N VAL D 129 ? N VAL D 129 
AC9 2 3 O ILE D 125 ? O ILE D 125 N LEU D 86  ? N LEU D 86  
AC9 3 4 O LYS D 85  ? O LYS D 85  N ILE D 65  ? N ILE D 65  
AC9 4 5 O ARG D 66  ? O ARG D 66  N ILE D 26  ? N ILE D 26  
AC9 5 6 N ILE D 23  ? N ILE D 23  O MET D 265 ? O MET D 265 
AD1 1 2 N TYR D 188 ? N TYR D 188 O THR D 223 ? O THR D 223 
AD2 1 2 N GLY D 296 ? N GLY D 296 O THR D 306 ? O THR D 306 
AD3 1 2 N LEU D 321 ? N LEU D 321 O TYR D 341 ? O TYR D 341 
AD3 2 3 N LEU D 338 ? N LEU D 338 O ASP D 371 ? O ASP D 371 
AD4 1 2 N HIS D 331 ? N HIS D 331 O LEU D 405 ? O LEU D 405 
AD4 2 3 O ILE D 397 ? O ILE D 397 N PHE D 389 ? N PHE D 389 
AD4 3 4 O ALA D 386 ? O ALA D 386 N LYS D 352 ? N LYS D 352 
AD4 4 5 N PHE D 353 ? N PHE D 353 O LYS D 356 ? O LYS D 356 
AD5 1 2 N THR D 421 ? N THR D 421 O SER D 433 ? O SER D 433 
AD5 2 3 N ILE D 438 ? N ILE D 438 O ILE D 479 ? O ILE D 479 
AD6 1 2 N THR D 445 ? N THR D 445 O ARG D 503 ? O ARG D 503 
AD6 2 3 O GLY D 499 ? O GLY D 499 N LYS D 451 ? N LYS D 451 
AD6 3 4 N LEU D 450 ? N LEU D 450 O VAL D 468 ? O VAL D 468 
AD7 1 2 N THR D 445 ? N THR D 445 O ARG D 503 ? O ARG D 503 
AD7 2 3 N VAL D 502 ? N VAL D 502 O PHE D 509 ? O PHE D 509 
# 
_pdbx_entry_details.entry_id                   9G5G 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_1              280 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_2              280 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             C 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             LYS 
_pdbx_validate_rmsd_angle.auth_seq_id_3              280 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                95.63 
_pdbx_validate_rmsd_angle.angle_target_value         110.40 
_pdbx_validate_rmsd_angle.angle_deviation            -14.77 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.00 
_pdbx_validate_rmsd_angle.linker_flag                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 46  ? ? 70.52   37.54   
2  1 GLU A 59  ? ? -49.98  -18.30  
3  1 GLU A 132 ? ? 36.20   61.85   
4  1 THR A 142 ? ? 86.63   140.14  
5  1 SER A 169 ? ? -101.21 68.53   
6  1 ASN A 194 ? ? 30.23   60.05   
7  1 PHE A 225 ? ? -177.91 137.81  
8  1 ASN A 235 ? ? -178.79 136.00  
9  1 TYR A 254 ? ? -44.36  -74.62  
10 1 TYR A 269 ? ? 77.70   111.96  
11 1 LYS A 344 ? ? -69.32  5.34    
12 1 SER A 360 ? ? -154.84 89.21   
13 1 MET A 369 ? ? -170.41 129.73  
14 1 ASP A 371 ? ? -165.03 -163.98 
15 1 ASP A 391 ? ? -109.87 -166.66 
16 1 ASN A 394 ? ? 81.42   42.57   
17 1 ASN A 443 ? ? 72.26   -22.84  
18 1 ASP A 448 ? ? 49.70   -112.31 
19 1 LYS B 20  ? ? -39.38  134.33  
20 1 ASP B 91  ? ? -69.25  76.93   
21 1 PRO B 101 ? ? -37.47  -37.14  
22 1 THR B 126 ? ? -172.50 145.48  
23 1 THR B 142 ? ? 97.69   142.65  
24 1 SER B 169 ? ? -106.03 70.87   
25 1 PHE B 225 ? ? -175.93 135.94  
26 1 ALA B 260 ? ? 80.35   -4.75   
27 1 TYR B 269 ? ? 68.46   141.54  
28 1 GLU B 279 ? ? 59.13   95.08   
29 1 PRO B 288 ? ? -33.12  -36.14  
30 1 TYR B 304 ? ? -128.20 -61.88  
31 1 LYS B 328 ? ? 70.72   34.24   
32 1 ASN B 333 ? ? -177.92 148.51  
33 1 ASP B 371 ? ? -174.07 -170.90 
34 1 ASP B 393 ? ? 117.24  -28.28  
35 1 ASN B 394 ? ? 75.69   41.39   
36 1 SER B 441 ? ? -160.98 105.96  
37 1 ASN B 443 ? ? 78.72   -14.42  
38 1 ASP B 448 ? ? 37.86   -122.25 
39 1 ALA C 32  ? ? -143.44 53.81   
40 1 GLU C 42  ? ? -54.47  106.62  
41 1 LYS C 120 ? ? -98.31  32.27   
42 1 THR C 142 ? ? 88.71   145.90  
43 1 SER C 169 ? ? -104.37 57.44   
44 1 LEU C 216 ? ? 48.78   29.91   
45 1 GLU C 232 ? ? -170.27 -170.67 
46 1 PRO C 267 ? ? -47.48  153.93  
47 1 TYR C 269 ? ? 74.08   125.71  
48 1 TRP C 291 ? ? -145.01 33.29   
49 1 ASP C 302 ? ? -70.16  -81.10  
50 1 LYS C 303 ? ? 81.61   -0.44   
51 1 TYR C 304 ? ? -132.37 -62.46  
52 1 SER C 360 ? ? -168.05 119.31  
53 1 ASP C 371 ? ? -170.05 -171.92 
54 1 ASP C 376 ? ? -146.80 59.26   
55 1 ASP C 391 ? ? -102.53 -167.74 
56 1 ASN C 394 ? ? 81.25   44.81   
57 1 ASN C 443 ? ? 72.46   -12.77  
58 1 ASP C 448 ? ? 81.35   -133.09 
59 1 LEU C 458 ? ? -63.40  90.61   
60 1 HIS C 512 ? ? -179.99 -179.68 
61 1 GLU C 525 ? ? -98.99  -60.13  
62 1 GLU D 59  ? ? -48.59  -17.46  
63 1 GLU D 132 ? ? 30.00   70.62   
64 1 THR D 142 ? ? 91.03   139.16  
65 1 ASN D 194 ? ? 36.31   59.01   
66 1 PHE D 225 ? ? -179.05 149.09  
67 1 VAL D 229 ? ? -101.71 59.57   
68 1 TYR D 269 ? ? 79.35   127.89  
69 1 TYR D 304 ? ? -123.12 -58.51  
70 1 ARG D 354 ? ? 38.46   43.68   
71 1 GLU D 400 ? ? -171.03 131.77  
72 1 ASN D 443 ? ? 91.82   -12.91  
73 1 ASP D 448 ? ? 42.65   -118.34 
74 1 HIS D 457 ? ? 84.35   19.13   
# 
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 43  ? ? 0.156 'SIDE CHAIN' 
2 1 ARG A 66  ? ? 0.083 'SIDE CHAIN' 
3 1 ARG A 255 ? ? 0.094 'SIDE CHAIN' 
4 1 ARG B 66  ? ? 0.104 'SIDE CHAIN' 
5 1 ARG B 528 ? ? 0.157 'SIDE CHAIN' 
6 1 ARG C 43  ? ? 0.241 'SIDE CHAIN' 
7 1 ARG C 308 ? ? 0.199 'SIDE CHAIN' 
# 
_pdbx_molecule_features.prd_id    PRD_900024 
_pdbx_molecule_features.name      beta-laminaribiose 
_pdbx_molecule_features.type      Oligosaccharide 
_pdbx_molecule_features.class     Antimicrobial 
_pdbx_molecule_features.details   oligosaccharide 
# 
loop_
_pdbx_molecule.instance_id 
_pdbx_molecule.prd_id 
_pdbx_molecule.asym_id 
1 PRD_900024 E 
2 PRD_900024 F 
# 
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 44.1320 -19.0770 -2.1040  0.0579 ? 0.0171 ? 0.0513  ? 0.0667 ? -0.0254 ? 1.6227 ? 1.0970 ? 0.0899  
? 0.0496 ? 2.2142 ? 0.4484  ? 0.8100 ? -0.0452 ? 0.1362  ? -0.0520 ? 0.0840 ? 0.0903  ? -0.2666 ? 0.2059  ? 0.1065  ? -0.0451 ? 
2 'X-RAY DIFFRACTION' ? refined 33.0640 18.1650  12.6820  0.0618 ? 0.0184 ? -0.0398 ? 0.0076 ? 0.0017  ? 1.6667 ? 0.7354 ? 0.1172  
? 0.1253 ? 1.9093 ? 0.3929  ? 1.0560 ? -0.0696 ? 0.0037  ? 0.0735  ? 0.2682 ? 0.0709  ? -0.1329 ? -0.0728 ? -0.0543 ? -0.0012 ? 
3 'X-RAY DIFFRACTION' ? refined 41.8650 41.0020  -48.2590 0.2366 ? 0.2293 ? 0.1334  ? 0.3082 ? -0.0294 ? 1.8141 ? 2.7830 ? -0.2942 
? 0.5005 ? 0.7587 ? -0.0708 ? 2.2949 ? -0.0665 ? -0.1437 ? 0.3582  ? 0.1418 ? 0.0224  ? 0.0841  ? -0.4650 ? -0.5353 ? 0.0442  ? 
4 'X-RAY DIFFRACTION' ? refined 78.8810 30.1520  -32.8890 0.2541 ? 0.0873 ? 0.0357  ? 0.4949 ? -0.0480 ? 1.7801 ? 3.4173 ? -0.2179 
? 0.2541 ? 1.3021 ? -0.3103 ? 1.3452 ? -0.0591 ? -0.8834 ? 0.4735  ? 0.2716 ? -0.0615 ? -0.1667 ? -0.1962 ? 0.2533  ? 0.1206  ? 
# 
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 ? ? D 3 ? ? ? D 530 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? A 3 ? ? ? A 530 ? ? ? 
3 'X-RAY DIFFRACTION' 3 ? ? B 3 ? ? ? B 530 ? ? ? 
4 'X-RAY DIFFRACTION' 4 ? ? C 3 ? ? ? C 530 ? ? ? 
# 
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 GLU 531 ? B GLU 531 
13 1 Y 1 B HIS 532 ? B HIS 532 
14 1 Y 1 B HIS 533 ? B HIS 533 
15 1 Y 1 B HIS 534 ? B HIS 534 
16 1 Y 1 B HIS 535 ? B HIS 535 
17 1 Y 1 B HIS 536 ? B HIS 536 
18 1 Y 1 B HIS 537 ? B HIS 537 
19 1 Y 1 C MET 1   ? C MET 1   
20 1 Y 1 C GLN 2   ? C GLN 2   
21 1 Y 1 C GLU 531 ? C GLU 531 
22 1 Y 1 C HIS 532 ? C HIS 532 
23 1 Y 1 C HIS 533 ? C HIS 533 
24 1 Y 1 C HIS 534 ? C HIS 534 
25 1 Y 1 C HIS 535 ? C HIS 535 
26 1 Y 1 C HIS 536 ? C HIS 536 
27 1 Y 1 C HIS 537 ? C HIS 537 
28 1 Y 1 D MET 1   ? D MET 1   
29 1 Y 1 D GLN 2   ? D GLN 2   
30 1 Y 1 D GLU 531 ? D GLU 531 
31 1 Y 1 D HIS 532 ? D HIS 532 
32 1 Y 1 D HIS 533 ? D HIS 533 
33 1 Y 1 D HIS 534 ? D HIS 534 
34 1 Y 1 D HIS 535 ? D HIS 535 
35 1 Y 1 D HIS 536 ? D HIS 536 
36 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 
GLN N    N N N 112 
GLN CA   C N S 113 
GLN C    C N N 114 
GLN O    O N N 115 
GLN CB   C N N 116 
GLN CG   C N N 117 
GLN CD   C N N 118 
GLN OE1  O N N 119 
GLN NE2  N N N 120 
GLN OXT  O N N 121 
GLN H    H N N 122 
GLN H2   H N N 123 
GLN HA   H N N 124 
GLN HB2  H N N 125 
GLN HB3  H N N 126 
GLN HG2  H N N 127 
GLN HG3  H N N 128 
GLN HE21 H N N 129 
GLN HE22 H N N 130 
GLN HXT  H N N 131 
GLU N    N N N 132 
GLU CA   C N S 133 
GLU C    C N N 134 
GLU O    O N N 135 
GLU CB   C N N 136 
GLU CG   C N N 137 
GLU CD   C N N 138 
GLU OE1  O N N 139 
GLU OE2  O N N 140 
GLU OXT  O N N 141 
GLU H    H N N 142 
GLU H2   H N N 143 
GLU HA   H N N 144 
GLU HB2  H N N 145 
GLU HB3  H N N 146 
GLU HG2  H N N 147 
GLU HG3  H N N 148 
GLU HE2  H N N 149 
GLU HXT  H N N 150 
GLY N    N N N 151 
GLY CA   C N N 152 
GLY C    C N N 153 
GLY O    O N N 154 
GLY OXT  O N N 155 
GLY H    H N N 156 
GLY H2   H N N 157 
GLY HA2  H N N 158 
GLY HA3  H N N 159 
GLY HXT  H N N 160 
GOL C1   C N N 161 
GOL O1   O N N 162 
GOL C2   C N N 163 
GOL O2   O N N 164 
GOL C3   C N N 165 
GOL O3   O N N 166 
GOL H11  H N N 167 
GOL H12  H N N 168 
GOL HO1  H N N 169 
GOL H2   H N N 170 
GOL HO2  H N N 171 
GOL H31  H N N 172 
GOL H32  H N N 173 
GOL HO3  H N N 174 
HIS N    N N N 175 
HIS CA   C N S 176 
HIS C    C N N 177 
HIS O    O N N 178 
HIS CB   C N N 179 
HIS CG   C Y N 180 
HIS ND1  N Y N 181 
HIS CD2  C Y N 182 
HIS CE1  C Y N 183 
HIS NE2  N Y N 184 
HIS OXT  O N N 185 
HIS H    H N N 186 
HIS H2   H N N 187 
HIS HA   H N N 188 
HIS HB2  H N N 189 
HIS HB3  H N N 190 
HIS HD1  H N N 191 
HIS HD2  H N N 192 
HIS HE1  H N N 193 
HIS HE2  H N N 194 
HIS HXT  H N N 195 
HOH O    O N N 196 
HOH H1   H N N 197 
HOH H2   H N N 198 
ILE N    N N N 199 
ILE CA   C N S 200 
ILE C    C N N 201 
ILE O    O N N 202 
ILE CB   C N S 203 
ILE CG1  C N N 204 
ILE CG2  C N N 205 
ILE CD1  C N N 206 
ILE OXT  O N N 207 
ILE H    H N N 208 
ILE H2   H N N 209 
ILE HA   H N N 210 
ILE HB   H N N 211 
ILE HG12 H N N 212 
ILE HG13 H N N 213 
ILE HG21 H N N 214 
ILE HG22 H N N 215 
ILE HG23 H N N 216 
ILE HD11 H N N 217 
ILE HD12 H N N 218 
ILE HD13 H N N 219 
ILE HXT  H N N 220 
LEU N    N N N 221 
LEU CA   C N S 222 
LEU C    C N N 223 
LEU O    O N N 224 
LEU CB   C N N 225 
LEU CG   C N N 226 
LEU CD1  C N N 227 
LEU CD2  C N N 228 
LEU OXT  O N N 229 
LEU H    H N N 230 
LEU H2   H N N 231 
LEU HA   H N N 232 
LEU HB2  H N N 233 
LEU HB3  H N N 234 
LEU HG   H N N 235 
LEU HD11 H N N 236 
LEU HD12 H N N 237 
LEU HD13 H N N 238 
LEU HD21 H N N 239 
LEU HD22 H N N 240 
LEU HD23 H N N 241 
LEU HXT  H N N 242 
LYS N    N N N 243 
LYS CA   C N S 244 
LYS C    C N N 245 
LYS O    O N N 246 
LYS CB   C N N 247 
LYS CG   C N N 248 
LYS CD   C N N 249 
LYS CE   C N N 250 
LYS NZ   N N N 251 
LYS OXT  O N N 252 
LYS H    H N N 253 
LYS H2   H N N 254 
LYS HA   H N N 255 
LYS HB2  H N N 256 
LYS HB3  H N N 257 
LYS HG2  H N N 258 
LYS HG3  H N N 259 
LYS HD2  H N N 260 
LYS HD3  H N N 261 
LYS HE2  H N N 262 
LYS HE3  H N N 263 
LYS HZ1  H N N 264 
LYS HZ2  H N N 265 
LYS HZ3  H N N 266 
LYS HXT  H N N 267 
MET N    N N N 268 
MET CA   C N S 269 
MET C    C N N 270 
MET O    O N N 271 
MET CB   C N N 272 
MET CG   C N N 273 
MET SD   S N N 274 
MET CE   C N N 275 
MET OXT  O N N 276 
MET H    H N N 277 
MET H2   H N N 278 
MET HA   H N N 279 
MET HB2  H N N 280 
MET HB3  H N N 281 
MET HG2  H N N 282 
MET HG3  H N N 283 
MET HE1  H N N 284 
MET HE2  H N N 285 
MET HE3  H N N 286 
MET HXT  H N N 287 
MLA C1   C N N 288 
MLA O1A  O N N 289 
MLA O1B  O N N 290 
MLA C2   C N N 291 
MLA C3   C N N 292 
MLA O3A  O N N 293 
MLA O3B  O N N 294 
MLA H1A  H N N 295 
MLA HC21 H N N 296 
MLA HC22 H N N 297 
MLA H3B  H N N 298 
PG4 O1   O N N 299 
PG4 C1   C N N 300 
PG4 C2   C N N 301 
PG4 O2   O N N 302 
PG4 C3   C N N 303 
PG4 C4   C N N 304 
PG4 O3   O N N 305 
PG4 C5   C N N 306 
PG4 C6   C N N 307 
PG4 O4   O N N 308 
PG4 C7   C N N 309 
PG4 C8   C N N 310 
PG4 O5   O N N 311 
PG4 HO1  H N N 312 
PG4 H11  H N N 313 
PG4 H12  H N N 314 
PG4 H21  H N N 315 
PG4 H22  H N N 316 
PG4 H31  H N N 317 
PG4 H32  H N N 318 
PG4 H41  H N N 319 
PG4 H42  H N N 320 
PG4 H51  H N N 321 
PG4 H52  H N N 322 
PG4 H61  H N N 323 
PG4 H62  H N N 324 
PG4 H71  H N N 325 
PG4 H72  H N N 326 
PG4 H81  H N N 327 
PG4 H82  H N N 328 
PG4 HO5  H N N 329 
PHE N    N N N 330 
PHE CA   C N S 331 
PHE C    C N N 332 
PHE O    O N N 333 
PHE CB   C N N 334 
PHE CG   C Y N 335 
PHE CD1  C Y N 336 
PHE CD2  C Y N 337 
PHE CE1  C Y N 338 
PHE CE2  C Y N 339 
PHE CZ   C Y N 340 
PHE OXT  O N N 341 
PHE H    H N N 342 
PHE H2   H N N 343 
PHE HA   H N N 344 
PHE HB2  H N N 345 
PHE HB3  H N N 346 
PHE HD1  H N N 347 
PHE HD2  H N N 348 
PHE HE1  H N N 349 
PHE HE2  H N N 350 
PHE HZ   H N N 351 
PHE HXT  H N N 352 
PRO N    N N N 353 
PRO CA   C N S 354 
PRO C    C N N 355 
PRO O    O N N 356 
PRO CB   C N N 357 
PRO CG   C N N 358 
PRO CD   C N N 359 
PRO OXT  O N N 360 
PRO H    H N N 361 
PRO HA   H N N 362 
PRO HB2  H N N 363 
PRO HB3  H N N 364 
PRO HG2  H N N 365 
PRO HG3  H N N 366 
PRO HD2  H N N 367 
PRO HD3  H N N 368 
PRO HXT  H N N 369 
SER N    N N N 370 
SER CA   C N S 371 
SER C    C N N 372 
SER O    O N N 373 
SER CB   C N N 374 
SER OG   O N N 375 
SER OXT  O N N 376 
SER H    H N N 377 
SER H2   H N N 378 
SER HA   H N N 379 
SER HB2  H N N 380 
SER HB3  H N N 381 
SER HG   H N N 382 
SER HXT  H N N 383 
THR N    N N N 384 
THR CA   C N S 385 
THR C    C N N 386 
THR O    O N N 387 
THR CB   C N R 388 
THR OG1  O N N 389 
THR CG2  C N N 390 
THR OXT  O N N 391 
THR H    H N N 392 
THR H2   H N N 393 
THR HA   H N N 394 
THR HB   H N N 395 
THR HG1  H N N 396 
THR HG21 H N N 397 
THR HG22 H N N 398 
THR HG23 H N N 399 
THR HXT  H N N 400 
TRP N    N N N 401 
TRP CA   C N S 402 
TRP C    C N N 403 
TRP O    O N N 404 
TRP CB   C N N 405 
TRP CG   C Y N 406 
TRP CD1  C Y N 407 
TRP CD2  C Y N 408 
TRP NE1  N Y N 409 
TRP CE2  C Y N 410 
TRP CE3  C Y N 411 
TRP CZ2  C Y N 412 
TRP CZ3  C Y N 413 
TRP CH2  C Y N 414 
TRP OXT  O N N 415 
TRP H    H N N 416 
TRP H2   H N N 417 
TRP HA   H N N 418 
TRP HB2  H N N 419 
TRP HB3  H N N 420 
TRP HD1  H N N 421 
TRP HE1  H N N 422 
TRP HE3  H N N 423 
TRP HZ2  H N N 424 
TRP HZ3  H N N 425 
TRP HH2  H N N 426 
TRP HXT  H N N 427 
TYR N    N N N 428 
TYR CA   C N S 429 
TYR C    C N N 430 
TYR O    O N N 431 
TYR CB   C N N 432 
TYR CG   C Y N 433 
TYR CD1  C Y N 434 
TYR CD2  C Y N 435 
TYR CE1  C Y N 436 
TYR CE2  C Y N 437 
TYR CZ   C Y N 438 
TYR OH   O N N 439 
TYR OXT  O N N 440 
TYR H    H N N 441 
TYR H2   H N N 442 
TYR HA   H N N 443 
TYR HB2  H N N 444 
TYR HB3  H N N 445 
TYR HD1  H N N 446 
TYR HD2  H N N 447 
TYR HE1  H N N 448 
TYR HE2  H N N 449 
TYR HH   H N N 450 
TYR HXT  H N N 451 
VAL N    N N N 452 
VAL CA   C N S 453 
VAL C    C N N 454 
VAL O    O N N 455 
VAL CB   C N N 456 
VAL CG1  C N N 457 
VAL CG2  C N N 458 
VAL OXT  O N N 459 
VAL H    H N N 460 
VAL H2   H N N 461 
VAL HA   H N N 462 
VAL HB   H N N 463 
VAL HG11 H N N 464 
VAL HG12 H N N 465 
VAL HG13 H N N 466 
VAL HG21 H N N 467 
VAL HG22 H N N 468 
VAL HG23 H N N 469 
VAL HXT  H N N 470 
# 
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 
GLN N   CA   sing N N 107 
GLN N   H    sing N N 108 
GLN N   H2   sing N N 109 
GLN CA  C    sing N N 110 
GLN CA  CB   sing N N 111 
GLN CA  HA   sing N N 112 
GLN C   O    doub N N 113 
GLN C   OXT  sing N N 114 
GLN CB  CG   sing N N 115 
GLN CB  HB2  sing N N 116 
GLN CB  HB3  sing N N 117 
GLN CG  CD   sing N N 118 
GLN CG  HG2  sing N N 119 
GLN CG  HG3  sing N N 120 
GLN CD  OE1  doub N N 121 
GLN CD  NE2  sing N N 122 
GLN NE2 HE21 sing N N 123 
GLN NE2 HE22 sing N N 124 
GLN OXT HXT  sing N N 125 
GLU N   CA   sing N N 126 
GLU N   H    sing N N 127 
GLU N   H2   sing N N 128 
GLU CA  C    sing N N 129 
GLU CA  CB   sing N N 130 
GLU CA  HA   sing N N 131 
GLU C   O    doub N N 132 
GLU C   OXT  sing N N 133 
GLU CB  CG   sing N N 134 
GLU CB  HB2  sing N N 135 
GLU CB  HB3  sing N N 136 
GLU CG  CD   sing N N 137 
GLU CG  HG2  sing N N 138 
GLU CG  HG3  sing N N 139 
GLU CD  OE1  doub N N 140 
GLU CD  OE2  sing N N 141 
GLU OE2 HE2  sing N N 142 
GLU OXT HXT  sing N N 143 
GLY N   CA   sing N N 144 
GLY N   H    sing N N 145 
GLY N   H2   sing N N 146 
GLY CA  C    sing N N 147 
GLY CA  HA2  sing N N 148 
GLY CA  HA3  sing N N 149 
GLY C   O    doub N N 150 
GLY C   OXT  sing N N 151 
GLY OXT HXT  sing N N 152 
GOL C1  O1   sing N N 153 
GOL C1  C2   sing N N 154 
GOL C1  H11  sing N N 155 
GOL C1  H12  sing N N 156 
GOL O1  HO1  sing N N 157 
GOL C2  O2   sing N N 158 
GOL C2  C3   sing N N 159 
GOL C2  H2   sing N N 160 
GOL O2  HO2  sing N N 161 
GOL C3  O3   sing N N 162 
GOL C3  H31  sing N N 163 
GOL C3  H32  sing N N 164 
GOL O3  HO3  sing N N 165 
HIS N   CA   sing N N 166 
HIS N   H    sing N N 167 
HIS N   H2   sing N N 168 
HIS CA  C    sing N N 169 
HIS CA  CB   sing N N 170 
HIS CA  HA   sing N N 171 
HIS C   O    doub N N 172 
HIS C   OXT  sing N N 173 
HIS CB  CG   sing N N 174 
HIS CB  HB2  sing N N 175 
HIS CB  HB3  sing N N 176 
HIS CG  ND1  sing Y N 177 
HIS CG  CD2  doub Y N 178 
HIS ND1 CE1  doub Y N 179 
HIS ND1 HD1  sing N N 180 
HIS CD2 NE2  sing Y N 181 
HIS CD2 HD2  sing N N 182 
HIS CE1 NE2  sing Y N 183 
HIS CE1 HE1  sing N N 184 
HIS NE2 HE2  sing N N 185 
HIS OXT HXT  sing N N 186 
HOH O   H1   sing N N 187 
HOH O   H2   sing N N 188 
ILE N   CA   sing N N 189 
ILE N   H    sing N N 190 
ILE N   H2   sing N N 191 
ILE CA  C    sing N N 192 
ILE CA  CB   sing N N 193 
ILE CA  HA   sing N N 194 
ILE C   O    doub N N 195 
ILE C   OXT  sing N N 196 
ILE CB  CG1  sing N N 197 
ILE CB  CG2  sing N N 198 
ILE CB  HB   sing N N 199 
ILE CG1 CD1  sing N N 200 
ILE CG1 HG12 sing N N 201 
ILE CG1 HG13 sing N N 202 
ILE CG2 HG21 sing N N 203 
ILE CG2 HG22 sing N N 204 
ILE CG2 HG23 sing N N 205 
ILE CD1 HD11 sing N N 206 
ILE CD1 HD12 sing N N 207 
ILE CD1 HD13 sing N N 208 
ILE OXT HXT  sing N N 209 
LEU N   CA   sing N N 210 
LEU N   H    sing N N 211 
LEU N   H2   sing N N 212 
LEU CA  C    sing N N 213 
LEU CA  CB   sing N N 214 
LEU CA  HA   sing N N 215 
LEU C   O    doub N N 216 
LEU C   OXT  sing N N 217 
LEU CB  CG   sing N N 218 
LEU CB  HB2  sing N N 219 
LEU CB  HB3  sing N N 220 
LEU CG  CD1  sing N N 221 
LEU CG  CD2  sing N N 222 
LEU CG  HG   sing N N 223 
LEU CD1 HD11 sing N N 224 
LEU CD1 HD12 sing N N 225 
LEU CD1 HD13 sing N N 226 
LEU CD2 HD21 sing N N 227 
LEU CD2 HD22 sing N N 228 
LEU CD2 HD23 sing N N 229 
LEU OXT HXT  sing N N 230 
LYS N   CA   sing N N 231 
LYS N   H    sing N N 232 
LYS N   H2   sing N N 233 
LYS CA  C    sing N N 234 
LYS CA  CB   sing N N 235 
LYS CA  HA   sing N N 236 
LYS C   O    doub N N 237 
LYS C   OXT  sing N N 238 
LYS CB  CG   sing N N 239 
LYS CB  HB2  sing N N 240 
LYS CB  HB3  sing N N 241 
LYS CG  CD   sing N N 242 
LYS CG  HG2  sing N N 243 
LYS CG  HG3  sing N N 244 
LYS CD  CE   sing N N 245 
LYS CD  HD2  sing N N 246 
LYS CD  HD3  sing N N 247 
LYS CE  NZ   sing N N 248 
LYS CE  HE2  sing N N 249 
LYS CE  HE3  sing N N 250 
LYS NZ  HZ1  sing N N 251 
LYS NZ  HZ2  sing N N 252 
LYS NZ  HZ3  sing N N 253 
LYS OXT HXT  sing N N 254 
MET N   CA   sing N N 255 
MET N   H    sing N N 256 
MET N   H2   sing N N 257 
MET CA  C    sing N N 258 
MET CA  CB   sing N N 259 
MET CA  HA   sing N N 260 
MET C   O    doub N N 261 
MET C   OXT  sing N N 262 
MET CB  CG   sing N N 263 
MET CB  HB2  sing N N 264 
MET CB  HB3  sing N N 265 
MET CG  SD   sing N N 266 
MET CG  HG2  sing N N 267 
MET CG  HG3  sing N N 268 
MET SD  CE   sing N N 269 
MET CE  HE1  sing N N 270 
MET CE  HE2  sing N N 271 
MET CE  HE3  sing N N 272 
MET OXT HXT  sing N N 273 
MLA C1  O1A  sing N N 274 
MLA C1  O1B  doub N N 275 
MLA C1  C2   sing N N 276 
MLA O1A H1A  sing N N 277 
MLA C2  C3   sing N N 278 
MLA C2  HC21 sing N N 279 
MLA C2  HC22 sing N N 280 
MLA C3  O3A  doub N N 281 
MLA C3  O3B  sing N N 282 
MLA O3B H3B  sing N N 283 
PG4 O1  C1   sing N N 284 
PG4 O1  HO1  sing N N 285 
PG4 C1  C2   sing N N 286 
PG4 C1  H11  sing N N 287 
PG4 C1  H12  sing N N 288 
PG4 C2  O2   sing N N 289 
PG4 C2  H21  sing N N 290 
PG4 C2  H22  sing N N 291 
PG4 O2  C3   sing N N 292 
PG4 C3  C4   sing N N 293 
PG4 C3  H31  sing N N 294 
PG4 C3  H32  sing N N 295 
PG4 C4  O3   sing N N 296 
PG4 C4  H41  sing N N 297 
PG4 C4  H42  sing N N 298 
PG4 O3  C5   sing N N 299 
PG4 C5  C6   sing N N 300 
PG4 C5  H51  sing N N 301 
PG4 C5  H52  sing N N 302 
PG4 C6  O4   sing N N 303 
PG4 C6  H61  sing N N 304 
PG4 C6  H62  sing N N 305 
PG4 O4  C7   sing N N 306 
PG4 C7  C8   sing N N 307 
PG4 C7  H71  sing N N 308 
PG4 C7  H72  sing N N 309 
PG4 C8  O5   sing N N 310 
PG4 C8  H81  sing N N 311 
PG4 C8  H82  sing N N 312 
PG4 O5  HO5  sing N N 313 
PHE N   CA   sing N N 314 
PHE N   H    sing N N 315 
PHE N   H2   sing N N 316 
PHE CA  C    sing N N 317 
PHE CA  CB   sing N N 318 
PHE CA  HA   sing N N 319 
PHE C   O    doub N N 320 
PHE C   OXT  sing N N 321 
PHE CB  CG   sing N N 322 
PHE CB  HB2  sing N N 323 
PHE CB  HB3  sing N N 324 
PHE CG  CD1  doub Y N 325 
PHE CG  CD2  sing Y N 326 
PHE CD1 CE1  sing Y N 327 
PHE CD1 HD1  sing N N 328 
PHE CD2 CE2  doub Y N 329 
PHE CD2 HD2  sing N N 330 
PHE CE1 CZ   doub Y N 331 
PHE CE1 HE1  sing N N 332 
PHE CE2 CZ   sing Y N 333 
PHE CE2 HE2  sing N N 334 
PHE CZ  HZ   sing N N 335 
PHE OXT HXT  sing N N 336 
PRO N   CA   sing N N 337 
PRO N   CD   sing N N 338 
PRO N   H    sing N N 339 
PRO CA  C    sing N N 340 
PRO CA  CB   sing N N 341 
PRO CA  HA   sing N N 342 
PRO C   O    doub N N 343 
PRO C   OXT  sing N N 344 
PRO CB  CG   sing N N 345 
PRO CB  HB2  sing N N 346 
PRO CB  HB3  sing N N 347 
PRO CG  CD   sing N N 348 
PRO CG  HG2  sing N N 349 
PRO CG  HG3  sing N N 350 
PRO CD  HD2  sing N N 351 
PRO CD  HD3  sing N N 352 
PRO OXT HXT  sing N N 353 
SER N   CA   sing N N 354 
SER N   H    sing N N 355 
SER N   H2   sing N N 356 
SER CA  C    sing N N 357 
SER CA  CB   sing N N 358 
SER CA  HA   sing N N 359 
SER C   O    doub N N 360 
SER C   OXT  sing N N 361 
SER CB  OG   sing N N 362 
SER CB  HB2  sing N N 363 
SER CB  HB3  sing N N 364 
SER OG  HG   sing N N 365 
SER OXT HXT  sing N N 366 
THR N   CA   sing N N 367 
THR N   H    sing N N 368 
THR N   H2   sing N N 369 
THR CA  C    sing N N 370 
THR CA  CB   sing N N 371 
THR CA  HA   sing N N 372 
THR C   O    doub N N 373 
THR C   OXT  sing N N 374 
THR CB  OG1  sing N N 375 
THR CB  CG2  sing N N 376 
THR CB  HB   sing N N 377 
THR OG1 HG1  sing N N 378 
THR CG2 HG21 sing N N 379 
THR CG2 HG22 sing N N 380 
THR CG2 HG23 sing N N 381 
THR OXT HXT  sing N N 382 
TRP N   CA   sing N N 383 
TRP N   H    sing N N 384 
TRP N   H2   sing N N 385 
TRP CA  C    sing N N 386 
TRP CA  CB   sing N N 387 
TRP CA  HA   sing N N 388 
TRP C   O    doub N N 389 
TRP C   OXT  sing N N 390 
TRP CB  CG   sing N N 391 
TRP CB  HB2  sing N N 392 
TRP CB  HB3  sing N N 393 
TRP CG  CD1  doub Y N 394 
TRP CG  CD2  sing Y N 395 
TRP CD1 NE1  sing Y N 396 
TRP CD1 HD1  sing N N 397 
TRP CD2 CE2  doub Y N 398 
TRP CD2 CE3  sing Y N 399 
TRP NE1 CE2  sing Y N 400 
TRP NE1 HE1  sing N N 401 
TRP CE2 CZ2  sing Y N 402 
TRP CE3 CZ3  doub Y N 403 
TRP CE3 HE3  sing N N 404 
TRP CZ2 CH2  doub Y N 405 
TRP CZ2 HZ2  sing N N 406 
TRP CZ3 CH2  sing Y N 407 
TRP CZ3 HZ3  sing N N 408 
TRP CH2 HH2  sing N N 409 
TRP OXT HXT  sing N N 410 
TYR N   CA   sing N N 411 
TYR N   H    sing N N 412 
TYR N   H2   sing N N 413 
TYR CA  C    sing N N 414 
TYR CA  CB   sing N N 415 
TYR CA  HA   sing N N 416 
TYR C   O    doub N N 417 
TYR C   OXT  sing N N 418 
TYR CB  CG   sing N N 419 
TYR CB  HB2  sing N N 420 
TYR CB  HB3  sing N N 421 
TYR CG  CD1  doub Y N 422 
TYR CG  CD2  sing Y N 423 
TYR CD1 CE1  sing Y N 424 
TYR CD1 HD1  sing N N 425 
TYR CD2 CE2  doub Y N 426 
TYR CD2 HD2  sing N N 427 
TYR CE1 CZ   doub Y N 428 
TYR CE1 HE1  sing N N 429 
TYR CE2 CZ   sing Y N 430 
TYR CE2 HE2  sing N N 431 
TYR CZ  OH   sing N N 432 
TYR OH  HH   sing N N 433 
TYR OXT HXT  sing N N 434 
VAL N   CA   sing N N 435 
VAL N   H    sing N N 436 
VAL N   H2   sing N N 437 
VAL CA  C    sing N N 438 
VAL CA  CB   sing N N 439 
VAL CA  HA   sing N N 440 
VAL C   O    doub N N 441 
VAL C   OXT  sing N N 442 
VAL CB  CG1  sing N N 443 
VAL CB  CG2  sing N N 444 
VAL CB  HB   sing N N 445 
VAL CG1 HG11 sing N N 446 
VAL CG1 HG12 sing N N 447 
VAL CG1 HG13 sing N N 448 
VAL CG2 HG21 sing N N 449 
VAL CG2 HG22 sing N N 450 
VAL CG2 HG23 sing N N 451 
VAL OXT HXT  sing N N 452 
# 
_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, UIDB/00276/2020, LA/P/0059/2020' 
_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 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'SeMet derivative' 
# 
_atom_sites.entry_id                    9G5G 
_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]   0.004793 
_atom_sites.fract_transf_matrix[1][2]   0.002767 
_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]   0.005535 
_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]   0.006050 
_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   ? 24.358  42.765  -7.824  1.00 88.72  ? 3   SER A N   1 
ATOM   2     C CA  . SER A 1 3   ? 23.545  41.674  -7.226  1.00 87.08  ? 3   SER A CA  1 
ATOM   3     C C   . SER A 1 3   ? 24.464  40.591  -6.671  1.00 86.31  ? 3   SER A C   1 
ATOM   4     O O   . SER A 1 3   ? 25.231  39.985  -7.422  1.00 87.31  ? 3   SER A O   1 
ATOM   5     C CB  . SER A 1 3   ? 22.622  41.103  -8.233  1.00 87.12  ? 3   SER A CB  1 
ATOM   6     O OG  . SER A 1 3   ? 21.913  40.031  -7.642  1.00 86.58  ? 3   SER A OG  1 
ATOM   7     N N   . LYS A 1 4   ? 24.348  40.329  -5.365  1.00 84.90  ? 4   LYS A N   1 
ATOM   8     C CA  . LYS A 1 4   ? 25.341  39.536  -4.664  1.00 83.58  ? 4   LYS A CA  1 
ATOM   9     C C   . LYS A 1 4   ? 24.689  38.464  -3.795  1.00 79.08  ? 4   LYS A C   1 
ATOM   10    O O   . LYS A 1 4   ? 23.569  38.597  -3.355  1.00 78.14  ? 4   LYS A O   1 
ATOM   11    C CB  . LYS A 1 4   ? 26.191  40.488  -3.822  1.00 86.02  ? 4   LYS A CB  1 
ATOM   12    C CG  . LYS A 1 4   ? 25.456  41.136  -2.668  1.00 89.17  ? 4   LYS A CG  1 
ATOM   13    C CD  . LYS A 1 4   ? 26.384  41.960  -1.782  1.00 95.28  ? 4   LYS A CD  1 
ATOM   14    C CE  . LYS A 1 4   ? 25.701  42.651  -0.633  1.00 99.84  ? 4   LYS A CE  1 
ATOM   15    N NZ  . LYS A 1 4   ? 25.156  41.670  0.313   1.00 100.06 ? 4   LYS A NZ  1 
ATOM   16    N N   . THR A 1 5   ? 25.452  37.434  -3.458  1.00 76.23  ? 5   THR A N   1 
ATOM   17    C CA  . THR A 1 5   ? 24.875  36.259  -2.841  1.00 75.15  ? 5   THR A CA  1 
ATOM   18    C C   . THR A 1 5   ? 24.088  36.645  -1.596  1.00 74.28  ? 5   THR A C   1 
ATOM   19    O O   . THR A 1 5   ? 24.584  37.376  -0.749  1.00 72.48  ? 5   THR A O   1 
ATOM   20    C CB  . THR A 1 5   ? 25.981  35.254  -2.535  1.00 73.52  ? 5   THR A CB  1 
ATOM   21    O OG1 . THR A 1 5   ? 26.408  34.932  -3.850  1.00 74.67  ? 5   THR A OG1 1 
ATOM   22    C CG2 . THR A 1 5   ? 25.496  33.995  -1.844  1.00 71.65  ? 5   THR A CG2 1 
ATOM   23    N N   . LYS A 1 6   ? 22.868  36.097  -1.525  1.00 75.33  ? 6   LYS A N   1 
ATOM   24    C CA  . LYS A 1 6   ? 22.017  36.159  -0.356  1.00 76.48  ? 6   LYS A CA  1 
ATOM   25    C C   . LYS A 1 6   ? 22.042  34.810  0.353   1.00 74.46  ? 6   LYS A C   1 
ATOM   26    O O   . LYS A 1 6   ? 21.883  33.751  -0.262  1.00 72.07  ? 6   LYS A O   1 
ATOM   27    C CB  . LYS A 1 6   ? 20.643  36.581  -0.875  1.00 81.21  ? 6   LYS A CB  1 
ATOM   28    C CG  . LYS A 1 6   ? 19.572  36.765  0.184   1.00 87.36  ? 6   LYS A CG  1 
ATOM   29    C CD  . LYS A 1 6   ? 19.749  37.889  1.208   1.00 92.57  ? 6   LYS A CD  1 
ATOM   30    C CE  . LYS A 1 6   ? 18.527  38.035  2.109   1.00 96.13  ? 6   LYS A CE  1 
ATOM   31    N NZ  . LYS A 1 6   ? 18.195  36.802  2.851   1.00 94.96  ? 6   LYS A NZ  1 
ATOM   32    N N   . ILE A 1 7   ? 22.251  34.873  1.668   1.00 74.42  ? 7   ILE A N   1 
ATOM   33    C CA  . ILE A 1 7   ? 22.461  33.694  2.486   1.00 72.86  ? 7   ILE A CA  1 
ATOM   34    C C   . ILE A 1 7   ? 21.476  33.723  3.636   1.00 75.20  ? 7   ILE A C   1 
ATOM   35    O O   . ILE A 1 7   ? 21.558  34.613  4.479   1.00 74.71  ? 7   ILE A O   1 
ATOM   36    C CB  . ILE A 1 7   ? 23.871  33.692  3.085   1.00 72.31  ? 7   ILE A CB  1 
ATOM   37    C CG1 . ILE A 1 7   ? 24.971  33.457  2.041   1.00 72.14  ? 7   ILE A CG1 1 
ATOM   38    C CG2 . ILE A 1 7   ? 23.941  32.691  4.233   1.00 71.25  ? 7   ILE A CG2 1 
ATOM   39    C CD1 . ILE A 1 7   ? 26.378  33.632  2.579   1.00 71.17  ? 7   ILE A CD1 1 
ATOM   40    N N   . GLU A 1 8   ? 20.620  32.700  3.713   1.00 80.03  ? 8   GLU A N   1 
ATOM   41    C CA  . GLU A 1 8   ? 19.768  32.514  4.878   1.00 83.02  ? 8   GLU A CA  1 
ATOM   42    C C   . GLU A 1 8   ? 19.812  31.049  5.352   1.00 80.30  ? 8   GLU A C   1 
ATOM   43    O O   . GLU A 1 8   ? 19.993  30.102  4.580   1.00 75.69  ? 8   GLU A O   1 
ATOM   44    C CB  . GLU A 1 8   ? 18.405  33.150  4.583   1.00 88.73  ? 8   GLU A CB  1 
ATOM   45    C CG  . GLU A 1 8   ? 17.457  32.259  3.780   1.00 97.15  ? 8   GLU A CG  1 
ATOM   46    C CD  . GLU A 1 8   ? 17.802  31.984  2.322   1.00 102.16 ? 8   GLU A CD  1 
ATOM   47    O OE1 . GLU A 1 8   ? 18.715  32.663  1.732   1.00 98.77  ? 8   GLU A OE1 1 
ATOM   48    O OE2 . GLU A 1 8   ? 17.124  31.029  1.818   1.00 97.00  ? 8   GLU A OE2 1 
ATOM   49    N N   . LEU A 1 9   ? 19.639  30.906  6.672   1.00 80.16  ? 9   LEU A N   1 
ATOM   50    C CA  . LEU A 1 9   ? 19.736  29.662  7.411   1.00 78.00  ? 9   LEU A CA  1 
ATOM   51    C C   . LEU A 1 9   ? 18.352  29.334  7.943   1.00 80.04  ? 9   LEU A C   1 
ATOM   52    O O   . LEU A 1 9   ? 17.815  30.061  8.768   1.00 82.55  ? 9   LEU A O   1 
ATOM   53    C CB  . LEU A 1 9   ? 20.688  29.875  8.589   1.00 76.31  ? 9   LEU A CB  1 
ATOM   54    C CG  . LEU A 1 9   ? 21.888  30.808  8.389   1.00 75.18  ? 9   LEU A CG  1 
ATOM   55    C CD1 . LEU A 1 9   ? 22.663  30.898  9.695   1.00 74.97  ? 9   LEU A CD1 1 
ATOM   56    C CD2 . LEU A 1 9   ? 22.836  30.386  7.280   1.00 76.10  ? 9   LEU A CD2 1 
ATOM   57    N N   . LYS A 1 10  ? 17.754  28.261  7.464   1.00 82.84  ? 10  LYS A N   1 
ATOM   58    C CA  . LYS A 1 10  ? 16.443  27.874  7.961   1.00 86.58  ? 10  LYS A CA  1 
ATOM   59    C C   . LYS A 1 10  ? 16.296  26.412  7.631   1.00 82.03  ? 10  LYS A C   1 
ATOM   60    O O   . LYS A 1 10  ? 16.973  25.947  6.718   1.00 81.23  ? 10  LYS A O   1 
ATOM   61    C CB  . LYS A 1 10  ? 15.214  28.549  7.347   1.00 90.24  ? 10  LYS A CB  1 
ATOM   62    C CG  . LYS A 1 10  ? 15.023  28.227  5.877   1.00 95.77  ? 10  LYS A CG  1 
ATOM   63    C CD  . LYS A 1 10  ? 13.959  29.059  5.170   1.00 103.67 ? 10  LYS A CD  1 
ATOM   64    C CE  . LYS A 1 10  ? 14.117  28.984  3.676   1.00 109.44 ? 10  LYS A CE  1 
ATOM   65    N NZ  . LYS A 1 10  ? 15.327  29.671  3.196   1.00 113.24 ? 10  LYS A NZ  1 
ATOM   66    N N   . ASP A 1 11  ? 15.449  25.732  8.407   1.00 78.64  ? 11  ASP A N   1 
ATOM   67    C CA  . ASP A 1 11  ? 15.549  24.286  8.542   1.00 76.77  ? 11  ASP A CA  1 
ATOM   68    C C   . ASP A 1 11  ? 17.026  23.882  8.652   1.00 71.89  ? 11  ASP A C   1 
ATOM   69    O O   . ASP A 1 11  ? 17.449  22.919  8.042   1.00 69.45  ? 11  ASP A O   1 
ATOM   70    C CB  . ASP A 1 11  ? 14.761  23.592  7.440   1.00 76.67  ? 11  ASP A CB  1 
ATOM   71    C CG  . ASP A 1 11  ? 13.410  24.249  7.210   1.00 80.31  ? 11  ASP A CG  1 
ATOM   72    O OD1 . ASP A 1 11  ? 12.637  24.352  8.182   1.00 83.39  ? 11  ASP A OD1 1 
ATOM   73    O OD2 . ASP A 1 11  ? 13.166  24.733  6.089   1.00 81.47  ? 11  ASP A OD2 1 
ATOM   74    N N   . ASN A 1 12  ? 17.825  24.649  9.402   1.00 70.59  ? 12  ASN A N   1 
ATOM   75    C CA  . ASN A 1 12  ? 19.190  24.261  9.755   1.00 69.53  ? 12  ASN A CA  1 
ATOM   76    C C   . ASN A 1 12  ? 20.075  23.961  8.536   1.00 68.23  ? 12  ASN A C   1 
ATOM   77    O O   . ASN A 1 12  ? 20.944  23.106  8.613   1.00 70.98  ? 12  ASN A O   1 
ATOM   78    C CB  . ASN A 1 12  ? 19.165  23.148  10.800  1.00 67.73  ? 12  ASN A CB  1 
ATOM   79    C CG  . ASN A 1 12  ? 18.383  23.546  12.040  1.00 68.66  ? 12  ASN A CG  1 
ATOM   80    O OD1 . ASN A 1 12  ? 18.086  24.741  12.274  1.00 68.48  ? 12  ASN A OD1 1 
ATOM   81    N ND2 . ASN A 1 12  ? 18.051  22.549  12.853  1.00 66.92  ? 12  ASN A ND2 1 
ATOM   82    N N   . TRP A 1 13  ? 19.940  24.731  7.449   1.00 67.72  ? 13  TRP A N   1 
ATOM   83    C CA  . TRP A 1 13  ? 20.774  24.561  6.268   1.00 66.72  ? 13  TRP A CA  1 
ATOM   84    C C   . TRP A 1 13  ? 21.238  25.917  5.766   1.00 65.97  ? 13  TRP A C   1 
ATOM   85    O O   . TRP A 1 13  ? 20.494  26.878  5.824   1.00 69.50  ? 13  TRP A O   1 
ATOM   86    C CB  . TRP A 1 13  ? 19.984  23.878  5.141   1.00 68.33  ? 13  TRP A CB  1 
ATOM   87    C CG  . TRP A 1 13  ? 20.081  22.372  5.033   1.00 66.82  ? 13  TRP A CG  1 
ATOM   88    C CD1 . TRP A 1 13  ? 19.367  21.469  5.750   1.00 65.85  ? 13  TRP A CD1 1 
ATOM   89    C CD2 . TRP A 1 13  ? 20.833  21.607  4.063   1.00 66.22  ? 13  TRP A CD2 1 
ATOM   90    N NE1 . TRP A 1 13  ? 19.688  20.206  5.350   1.00 66.48  ? 13  TRP A NE1 1 
ATOM   91    C CE2 . TRP A 1 13  ? 20.560  20.251  4.309   1.00 64.75  ? 13  TRP A CE2 1 
ATOM   92    C CE3 . TRP A 1 13  ? 21.731  21.932  3.035   1.00 67.06  ? 13  TRP A CE3 1 
ATOM   93    C CZ2 . TRP A 1 13  ? 21.120  19.219  3.572   1.00 64.18  ? 13  TRP A CZ2 1 
ATOM   94    C CZ3 . TRP A 1 13  ? 22.279  20.909  2.288   1.00 66.77  ? 13  TRP A CZ3 1 
ATOM   95    C CH2 . TRP A 1 13  ? 21.961  19.569  2.547   1.00 65.35  ? 13  TRP A CH2 1 
ATOM   96    N N   . TYR A 1 14  ? 22.433  25.983  5.190   1.00 63.50  ? 14  TYR A N   1 
ATOM   97    C CA  . TYR A 1 14  ? 22.809  27.181  4.461   1.00 62.22  ? 14  TYR A CA  1 
ATOM   98    C C   . TYR A 1 14  ? 21.973  27.195  3.192   1.00 62.03  ? 14  TYR A C   1 
ATOM   99    O O   . TYR A 1 14  ? 21.750  26.150  2.595   1.00 61.60  ? 14  TYR A O   1 
ATOM   100   C CB  . TYR A 1 14  ? 24.302  27.244  4.095   1.00 61.19  ? 14  TYR A CB  1 
ATOM   101   C CG  . TYR A 1 14  ? 25.260  27.566  5.239   1.00 59.48  ? 14  TYR A CG  1 
ATOM   102   C CD1 . TYR A 1 14  ? 25.371  26.712  6.330   1.00 58.46  ? 14  TYR A CD1 1 
ATOM   103   C CD2 . TYR A 1 14  ? 26.048  28.712  5.233   1.00 58.90  ? 14  TYR A CD2 1 
ATOM   104   C CE1 . TYR A 1 14  ? 26.226  26.994  7.381   1.00 57.81  ? 14  TYR A CE1 1 
ATOM   105   C CE2 . TYR A 1 14  ? 26.920  28.992  6.272   1.00 58.11  ? 14  TYR A CE2 1 
ATOM   106   C CZ  . TYR A 1 14  ? 27.005  28.132  7.348   1.00 57.29  ? 14  TYR A CZ  1 
ATOM   107   O OH  . TYR A 1 14  ? 27.796  28.349  8.419   1.00 56.53  ? 14  TYR A OH  1 
ATOM   108   N N   . HIS A 1 15  ? 21.507  28.381  2.807   1.00 62.74  ? 15  HIS A N   1 
ATOM   109   C CA  . HIS A 1 15  ? 20.956  28.604  1.485   1.00 63.54  ? 15  HIS A CA  1 
ATOM   110   C C   . HIS A 1 15  ? 21.817  29.615  0.757   1.00 64.39  ? 15  HIS A C   1 
ATOM   111   O O   . HIS A 1 15  ? 22.415  30.478  1.383   1.00 66.15  ? 15  HIS A O   1 
ATOM   112   C CB  . HIS A 1 15  ? 19.537  29.147  1.576   1.00 64.75  ? 15  HIS A CB  1 
ATOM   113   C CG  . HIS A 1 15  ? 18.603  28.113  2.096   1.00 64.46  ? 15  HIS A CG  1 
ATOM   114   N ND1 . HIS A 1 15  ? 18.627  27.727  3.419   1.00 64.07  ? 15  HIS A ND1 1 
ATOM   115   C CD2 . HIS A 1 15  ? 17.704  27.346  1.492   1.00 64.15  ? 15  HIS A CD2 1 
ATOM   116   C CE1 . HIS A 1 15  ? 17.739  26.772  3.610   1.00 63.69  ? 15  HIS A CE1 1 
ATOM   117   N NE2 . HIS A 1 15  ? 17.158  26.541  2.455   1.00 64.39  ? 15  HIS A NE2 1 
ATOM   118   N N   . LEU A 1 16  ? 21.879  29.520  -0.566  1.00 64.48  ? 16  LEU A N   1 
ATOM   119   C CA  . LEU A 1 16  ? 22.651  30.481  -1.332  1.00 64.36  ? 16  LEU A CA  1 
ATOM   120   C C   . LEU A 1 16  ? 21.809  30.891  -2.526  1.00 65.34  ? 16  LEU A C   1 
ATOM   121   O O   . LEU A 1 16  ? 21.583  30.107  -3.441  1.00 64.64  ? 16  LEU A O   1 
ATOM   122   C CB  . LEU A 1 16  ? 24.004  29.916  -1.743  1.00 63.78  ? 16  LEU A CB  1 
ATOM   123   C CG  . LEU A 1 16  ? 25.203  30.384  -0.919  1.00 63.54  ? 16  LEU A CG  1 
ATOM   124   C CD1 . LEU A 1 16  ? 25.225  29.869  0.506   1.00 62.39  ? 16  LEU A CD1 1 
ATOM   125   C CD2 . LEU A 1 16  ? 26.415  29.941  -1.697  1.00 64.03  ? 16  LEU A CD2 1 
ATOM   126   N N   . ASP A 1 17  ? 21.288  32.116  -2.445  1.00 66.56  ? 17  ASP A N   1 
ATOM   127   C CA  . ASP A 1 17  ? 20.248  32.541  -3.356  1.00 67.81  ? 17  ASP A CA  1 
ATOM   128   C C   . ASP A 1 17  ? 19.096  31.536  -3.407  1.00 66.86  ? 17  ASP A C   1 
ATOM   129   O O   . ASP A 1 17  ? 18.644  31.179  -4.490  1.00 66.47  ? 17  ASP A O   1 
ATOM   130   C CB  . ASP A 1 17  ? 20.813  32.737  -4.749  1.00 68.93  ? 17  ASP A CB  1 
ATOM   131   C CG  . ASP A 1 17  ? 22.035  33.624  -4.826  1.00 69.52  ? 17  ASP A CG  1 
ATOM   132   O OD1 . ASP A 1 17  ? 21.939  34.837  -4.469  1.00 70.61  ? 17  ASP A OD1 1 
ATOM   133   O OD2 . ASP A 1 17  ? 23.059  33.084  -5.273  1.00 70.21  ? 17  ASP A OD2 1 
ATOM   134   N N   . GLY A 1 18  ? 18.625  31.087  -2.242  1.00 66.40  ? 18  GLY A N   1 
ATOM   135   C CA  . GLY A 1 18  ? 17.361  30.363  -2.168  1.00 67.53  ? 18  GLY A CA  1 
ATOM   136   C C   . GLY A 1 18  ? 17.523  28.837  -2.131  1.00 67.27  ? 18  GLY A C   1 
ATOM   137   O O   . GLY A 1 18  ? 16.646  28.141  -1.628  1.00 66.59  ? 18  GLY A O   1 
ATOM   138   N N   . GLU A 1 19  ? 18.651  28.319  -2.637  1.00 67.22  ? 19  GLU A N   1 
ATOM   139   C CA  . GLU A 1 19  ? 18.832  26.886  -2.796  1.00 67.08  ? 19  GLU A CA  1 
ATOM   140   C C   . GLU A 1 19  ? 19.780  26.379  -1.721  1.00 66.32  ? 19  GLU A C   1 
ATOM   141   O O   . GLU A 1 19  ? 20.723  27.061  -1.350  1.00 68.45  ? 19  GLU A O   1 
ATOM   142   C CB  . GLU A 1 19  ? 19.295  26.632  -4.230  1.00 67.53  ? 19  GLU A CB  1 
ATOM   143   C CG  . GLU A 1 19  ? 18.262  27.103  -5.256  1.00 69.48  ? 19  GLU A CG  1 
ATOM   144   C CD  . GLU A 1 19  ? 16.917  26.389  -5.096  1.00 71.24  ? 19  GLU A CD  1 
ATOM   145   O OE1 . GLU A 1 19  ? 16.892  25.122  -4.947  1.00 70.98  ? 19  GLU A OE1 1 
ATOM   146   O OE2 . GLU A 1 19  ? 15.889  27.102  -5.106  1.00 72.88  ? 19  GLU A OE2 1 
ATOM   147   N N   . LYS A 1 20  ? 19.499  25.189  -1.200  1.00 66.18  ? 20  LYS A N   1 
ATOM   148   C CA  . LYS A 1 20  ? 20.313  24.582  -0.161  1.00 64.53  ? 20  LYS A CA  1 
ATOM   149   C C   . LYS A 1 20  ? 21.719  24.386  -0.712  1.00 62.48  ? 20  LYS A C   1 
ATOM   150   O O   . LYS A 1 20  ? 21.865  23.903  -1.832  1.00 61.80  ? 20  LYS A O   1 
ATOM   151   C CB  . LYS A 1 20  ? 19.665  23.256  0.268   1.00 65.89  ? 20  LYS A CB  1 
ATOM   152   C CG  . LYS A 1 20  ? 18.310  23.346  0.990   1.00 68.30  ? 20  LYS A CG  1 
ATOM   153   C CD  . LYS A 1 20  ? 17.994  22.079  1.780   1.00 69.58  ? 20  LYS A CD  1 
ATOM   154   C CE  . LYS A 1 20  ? 16.813  22.139  2.727   1.00 71.31  ? 20  LYS A CE  1 
ATOM   155   N NZ  . LYS A 1 20  ? 15.614  21.413  2.287   1.00 71.94  ? 20  LYS A NZ  1 
ATOM   156   N N   . TYR A 1 21  ? 22.726  24.786  0.079   1.00 61.31  ? 21  TYR A N   1 
ATOM   157   C CA  . TYR A 1 21  ? 24.134  24.603  -0.250  1.00 60.44  ? 21  TYR A CA  1 
ATOM   158   C C   . TYR A 1 21  ? 24.847  23.834  0.859   1.00 59.07  ? 21  TYR A C   1 
ATOM   159   O O   . TYR A 1 21  ? 24.785  24.207  2.041   1.00 58.29  ? 21  TYR A O   1 
ATOM   160   C CB  . TYR A 1 21  ? 24.859  25.936  -0.337  1.00 61.47  ? 21  TYR A CB  1 
ATOM   161   C CG  . TYR A 1 21  ? 26.225  26.008  -1.019  1.00 61.72  ? 21  TYR A CG  1 
ATOM   162   C CD1 . TYR A 1 21  ? 26.320  26.134  -2.401  1.00 62.42  ? 21  TYR A CD1 1 
ATOM   163   C CD2 . TYR A 1 21  ? 27.401  26.112  -0.289  1.00 61.41  ? 21  TYR A CD2 1 
ATOM   164   C CE1 . TYR A 1 21  ? 27.530  26.259  -3.048  1.00 62.25  ? 21  TYR A CE1 1 
ATOM   165   C CE2 . TYR A 1 21  ? 28.630  26.236  -0.923  1.00 61.64  ? 21  TYR A CE2 1 
ATOM   166   C CZ  . TYR A 1 21  ? 28.693  26.314  -2.306  1.00 62.11  ? 21  TYR A CZ  1 
ATOM   167   O OH  . TYR A 1 21  ? 29.868  26.462  -2.979  1.00 61.77  ? 21  TYR A OH  1 
ATOM   168   N N   . PHE A 1 22  ? 25.512  22.751  0.442   1.00 57.91  ? 22  PHE A N   1 
ATOM   169   C CA  . PHE A 1 22  ? 26.200  21.868  1.355   1.00 57.43  ? 22  PHE A CA  1 
ATOM   170   C C   . PHE A 1 22  ? 27.668  22.223  1.236   1.00 57.64  ? 22  PHE A C   1 
ATOM   171   O O   . PHE A 1 22  ? 28.239  22.133  0.151   1.00 57.93  ? 22  PHE A O   1 
ATOM   172   C CB  . PHE A 1 22  ? 25.998  20.388  0.994   1.00 57.95  ? 22  PHE A CB  1 
ATOM   173   C CG  . PHE A 1 22  ? 26.495  19.454  2.085   1.00 57.77  ? 22  PHE A CG  1 
ATOM   174   C CD1 . PHE A 1 22  ? 27.849  19.216  2.258   1.00 58.01  ? 22  PHE A CD1 1 
ATOM   175   C CD2 . PHE A 1 22  ? 25.614  18.853  2.968   1.00 58.16  ? 22  PHE A CD2 1 
ATOM   176   C CE1 . PHE A 1 22  ? 28.296  18.396  3.281   1.00 58.17  ? 22  PHE A CE1 1 
ATOM   177   C CE2 . PHE A 1 22  ? 26.069  18.045  3.993   1.00 57.82  ? 22  PHE A CE2 1 
ATOM   178   C CZ  . PHE A 1 22  ? 27.403  17.806  4.140   1.00 57.77  ? 22  PHE A CZ  1 
ATOM   179   N N   . ILE A 1 23  ? 28.283  22.624  2.344   1.00 57.87  ? 23  ILE A N   1 
ATOM   180   C CA  . ILE A 1 23  ? 29.599  23.222  2.248   1.00 58.64  ? 23  ILE A CA  1 
ATOM   181   C C   . ILE A 1 23  ? 30.621  22.094  2.166   1.00 59.17  ? 23  ILE A C   1 
ATOM   182   O O   . ILE A 1 23  ? 30.883  21.433  3.174   1.00 59.24  ? 23  ILE A O   1 
ATOM   183   C CB  . ILE A 1 23  ? 29.856  24.180  3.423   1.00 58.86  ? 23  ILE A CB  1 
ATOM   184   C CG1 . ILE A 1 23  ? 28.751  25.228  3.548   1.00 59.86  ? 23  ILE A CG1 1 
ATOM   185   C CG2 . ILE A 1 23  ? 31.219  24.854  3.273   1.00 58.93  ? 23  ILE A CG2 1 
ATOM   186   C CD1 . ILE A 1 23  ? 28.808  26.031  4.837   1.00 60.41  ? 23  ILE A CD1 1 
ATOM   187   N N   . LYS A 1 24  ? 31.159  21.866  0.954   1.00 59.88  ? 24  LYS A N   1 
ATOM   188   C CA  . LYS A 1 24  ? 32.194  20.858  0.718   1.00 59.62  ? 24  LYS A CA  1 
ATOM   189   C C   . LYS A 1 24  ? 33.540  21.573  0.772   1.00 59.20  ? 24  LYS A C   1 
ATOM   190   O O   . LYS A 1 24  ? 34.053  22.047  -0.248  1.00 58.67  ? 24  LYS A O   1 
ATOM   191   C CB  . LYS A 1 24  ? 31.958  20.086  -0.592  1.00 60.56  ? 24  LYS A CB  1 
ATOM   192   C CG  . LYS A 1 24  ? 30.568  19.451  -0.704  1.00 61.73  ? 24  LYS A CG  1 
ATOM   193   C CD  . LYS A 1 24  ? 30.359  18.421  -1.811  1.00 63.39  ? 24  LYS A CD  1 
ATOM   194   C CE  . LYS A 1 24  ? 30.343  18.894  -3.238  1.00 65.06  ? 24  LYS A CE  1 
ATOM   195   N NZ  . LYS A 1 24  ? 30.733  17.778  -4.117  1.00 65.95  ? 24  LYS A NZ  1 
ATOM   196   N N   . ALA A 1 25  ? 34.058  21.700  1.997   1.00 58.84  ? 25  ALA A N   1 
ATOM   197   C CA  . ALA A 1 25  ? 35.197  22.562  2.247   1.00 59.93  ? 25  ALA A CA  1 
ATOM   198   C C   . ALA A 1 25  ? 36.471  21.736  2.510   1.00 60.89  ? 25  ALA A C   1 
ATOM   199   O O   . ALA A 1 25  ? 36.440  20.514  2.605   1.00 60.63  ? 25  ALA A O   1 
ATOM   200   C CB  . ALA A 1 25  ? 34.849  23.512  3.383   1.00 59.36  ? 25  ALA A CB  1 
ATOM   201   N N   . ILE A 1 26  ? 37.623  22.420  2.563   1.00 62.06  ? 26  ILE A N   1 
ATOM   202   C CA  . ILE A 1 26  ? 38.864  21.850  3.082   1.00 61.67  ? 26  ILE A CA  1 
ATOM   203   C C   . ILE A 1 26  ? 39.593  22.953  3.847   1.00 62.07  ? 26  ILE A C   1 
ATOM   204   O O   . ILE A 1 26  ? 39.547  24.121  3.437   1.00 62.59  ? 26  ILE A O   1 
ATOM   205   C CB  . ILE A 1 26  ? 39.754  21.288  1.961   1.00 61.05  ? 26  ILE A CB  1 
ATOM   206   C CG1 . ILE A 1 26  ? 40.833  20.402  2.522   1.00 60.85  ? 26  ILE A CG1 1 
ATOM   207   C CG2 . ILE A 1 26  ? 40.353  22.407  1.105   1.00 61.70  ? 26  ILE A CG2 1 
ATOM   208   C CD1 . ILE A 1 26  ? 41.541  19.568  1.469   1.00 61.16  ? 26  ILE A CD1 1 
ATOM   209   N N   . GLY A 1 27  ? 40.223  22.586  4.971   1.00 61.20  ? 27  GLY A N   1 
ATOM   210   C CA  . GLY A 1 27  ? 41.144  23.504  5.615   1.00 62.05  ? 27  GLY A CA  1 
ATOM   211   C C   . GLY A 1 27  ? 42.247  23.912  4.637   1.00 62.30  ? 27  GLY A C   1 
ATOM   212   O O   . GLY A 1 27  ? 42.721  23.056  3.891   1.00 62.93  ? 27  GLY A O   1 
ATOM   213   N N   . TYR A 1 28  ? 42.655  25.194  4.641   1.00 62.11  ? 28  TYR A N   1 
ATOM   214   C CA  . TYR A 1 28  ? 43.717  25.671  3.758   1.00 62.97  ? 28  TYR A CA  1 
ATOM   215   C C   . TYR A 1 28  ? 44.473  26.796  4.441   1.00 63.85  ? 28  TYR A C   1 
ATOM   216   O O   . TYR A 1 28  ? 43.826  27.641  5.032   1.00 64.54  ? 28  TYR A O   1 
ATOM   217   C CB  . TYR A 1 28  ? 43.128  26.169  2.438   1.00 63.04  ? 28  TYR A CB  1 
ATOM   218   C CG  . TYR A 1 28  ? 44.111  26.799  1.472   1.00 64.52  ? 28  TYR A CG  1 
ATOM   219   C CD1 . TYR A 1 28  ? 45.289  26.151  1.120   1.00 66.11  ? 28  TYR A CD1 1 
ATOM   220   C CD2 . TYR A 1 28  ? 43.867  28.056  0.924   1.00 65.90  ? 28  TYR A CD2 1 
ATOM   221   C CE1 . TYR A 1 28  ? 46.220  26.753  0.276   1.00 68.08  ? 28  TYR A CE1 1 
ATOM   222   C CE2 . TYR A 1 28  ? 44.781  28.668  0.074   1.00 68.00  ? 28  TYR A CE2 1 
ATOM   223   C CZ  . TYR A 1 28  ? 45.967  28.013  -0.253  1.00 68.99  ? 28  TYR A CZ  1 
ATOM   224   O OH  . TYR A 1 28  ? 46.871  28.558  -1.117  1.00 68.99  ? 28  TYR A OH  1 
ATOM   225   N N   . GLU A 1 29  ? 45.818  26.801  4.329   1.00 65.11  ? 29  GLU A N   1 
ATOM   226   C CA  . GLU A 1 29  ? 46.706  27.776  4.964   1.00 65.11  ? 29  GLU A CA  1 
ATOM   227   C C   . GLU A 1 29  ? 47.895  28.080  4.060   1.00 66.47  ? 29  GLU A C   1 
ATOM   228   O O   . GLU A 1 29  ? 48.818  27.299  3.970   1.00 67.55  ? 29  GLU A O   1 
ATOM   229   C CB  . GLU A 1 29  ? 47.273  27.216  6.268   1.00 64.81  ? 29  GLU A CB  1 
ATOM   230   C CG  . GLU A 1 29  ? 48.112  28.181  7.091   1.00 65.79  ? 29  GLU A CG  1 
ATOM   231   C CD  . GLU A 1 29  ? 48.351  27.616  8.482   1.00 66.26  ? 29  GLU A CD  1 
ATOM   232   O OE1 . GLU A 1 29  ? 49.060  26.536  8.628   1.00 66.13  ? 29  GLU A OE1 1 
ATOM   233   O OE2 . GLU A 1 29  ? 47.782  28.295  9.402   1.00 65.67  ? 29  GLU A OE2 1 
ATOM   234   N N   . ILE A 1 30  ? 47.895  29.260  3.437   1.00 68.32  ? 30  ILE A N   1 
ATOM   235   C CA  . ILE A 1 30  ? 49.022  29.780  2.669   1.00 69.56  ? 30  ILE A CA  1 
ATOM   236   C C   . ILE A 1 30  ? 50.152  30.215  3.608   1.00 71.28  ? 30  ILE A C   1 
ATOM   237   O O   . ILE A 1 30  ? 49.908  30.436  4.796   1.00 72.44  ? 30  ILE A O   1 
ATOM   238   C CB  . ILE A 1 30  ? 48.540  30.944  1.778   1.00 69.85  ? 30  ILE A CB  1 
ATOM   239   C CG1 . ILE A 1 30  ? 49.498  31.237  0.606   1.00 71.00  ? 30  ILE A CG1 1 
ATOM   240   C CG2 . ILE A 1 30  ? 48.212  32.197  2.609   1.00 69.47  ? 30  ILE A CG2 1 
ATOM   241   C CD1 . ILE A 1 30  ? 49.617  30.094  -0.392  1.00 70.92  ? 30  ILE A CD1 1 
ATOM   242   N N   . GLY A 1 31  ? 51.374  30.344  3.047   1.00 72.14  ? 31  GLY A N   1 
ATOM   243   C CA  . GLY A 1 31  ? 52.563  30.750  3.772   1.00 72.95  ? 31  GLY A CA  1 
ATOM   244   C C   . GLY A 1 31  ? 52.991  29.684  4.770   1.00 72.86  ? 31  GLY A C   1 
ATOM   245   O O   . GLY A 1 31  ? 53.526  29.980  5.833   1.00 73.56  ? 31  GLY A O   1 
ATOM   246   N N   . ALA A 1 32  ? 52.768  28.419  4.425   1.00 73.01  ? 32  ALA A N   1 
ATOM   247   C CA  . ALA A 1 32  ? 53.086  27.322  5.371   1.00 72.15  ? 32  ALA A CA  1 
ATOM   248   C C   . ALA A 1 32  ? 53.816  26.200  4.640   1.00 71.50  ? 32  ALA A C   1 
ATOM   249   O O   . ALA A 1 32  ? 53.837  25.078  5.161   1.00 71.92  ? 32  ALA A O   1 
ATOM   250   C CB  . ALA A 1 32  ? 51.835  26.826  6.045   1.00 70.34  ? 32  ALA A CB  1 
ATOM   251   N N   . ARG A 1 33  ? 54.397  26.501  3.481   1.00 71.14  ? 33  ARG A N   1 
ATOM   252   C CA  . ARG A 1 33  ? 55.232  25.509  2.769   1.00 71.29  ? 33  ARG A CA  1 
ATOM   253   C C   . ARG A 1 33  ? 56.468  25.226  3.627   1.00 72.09  ? 33  ARG A C   1 
ATOM   254   O O   . ARG A 1 33  ? 56.674  25.919  4.639   1.00 71.38  ? 33  ARG A O   1 
ATOM   255   C CB  . ARG A 1 33  ? 55.618  26.060  1.397   1.00 72.20  ? 33  ARG A CB  1 
ATOM   256   C CG  . ARG A 1 33  ? 54.987  25.381  0.195   1.00 71.39  ? 33  ARG A CG  1 
ATOM   257   C CD  . ARG A 1 33  ? 53.560  25.848  0.057   1.00 69.72  ? 33  ARG A CD  1 
ATOM   258   N NE  . ARG A 1 33  ? 53.059  25.558  -1.287  1.00 69.48  ? 33  ARG A NE  1 
ATOM   259   C CZ  . ARG A 1 33  ? 51.877  25.953  -1.716  1.00 68.61  ? 33  ARG A CZ  1 
ATOM   260   N NH1 . ARG A 1 33  ? 51.011  26.453  -0.858  1.00 67.53  ? 33  ARG A NH1 1 
ATOM   261   N NH2 . ARG A 1 33  ? 51.574  25.853  -2.996  1.00 68.74  ? 33  ARG A NH2 1 
ATOM   262   N N   . PRO A 1 34  ? 57.282  24.196  3.316   1.00 73.49  ? 34  PRO A N   1 
ATOM   263   C CA  . PRO A 1 34  ? 58.523  23.984  4.049   1.00 74.85  ? 34  PRO A CA  1 
ATOM   264   C C   . PRO A 1 34  ? 59.410  25.237  4.022   1.00 76.44  ? 34  PRO A C   1 
ATOM   265   O O   . PRO A 1 34  ? 59.638  25.794  2.930   1.00 77.30  ? 34  PRO A O   1 
ATOM   266   C CB  . PRO A 1 34  ? 59.112  22.786  3.305   1.00 75.36  ? 34  PRO A CB  1 
ATOM   267   C CG  . PRO A 1 34  ? 58.449  22.802  1.957   1.00 74.54  ? 34  PRO A CG  1 
ATOM   268   C CD  . PRO A 1 34  ? 57.037  23.201  2.295   1.00 72.98  ? 34  PRO A CD  1 
ATOM   269   N N   . GLY A 1 35  ? 59.926  25.663  5.177   1.00 77.04  ? 35  GLY A N   1 
ATOM   270   C CA  . GLY A 1 35  ? 60.676  26.900  5.274   1.00 78.60  ? 35  GLY A CA  1 
ATOM   271   C C   . GLY A 1 35  ? 59.873  28.001  5.961   1.00 78.28  ? 35  GLY A C   1 
ATOM   272   O O   . GLY A 1 35  ? 60.420  28.785  6.726   1.00 79.31  ? 35  GLY A O   1 
ATOM   273   N N   . GLN A 1 36  ? 58.561  28.017  5.728   1.00 77.31  ? 36  GLN A N   1 
ATOM   274   C CA  . GLN A 1 36  ? 57.713  29.124  6.140   1.00 77.36  ? 36  GLN A CA  1 
ATOM   275   C C   . GLN A 1 36  ? 57.055  28.867  7.498   1.00 79.04  ? 36  GLN A C   1 
ATOM   276   O O   . GLN A 1 36  ? 56.742  27.748  7.866   1.00 78.87  ? 36  GLN A O   1 
ATOM   277   C CB  . GLN A 1 36  ? 56.600  29.342  5.113   1.00 75.38  ? 36  GLN A CB  1 
ATOM   278   C CG  . GLN A 1 36  ? 57.007  29.175  3.652   1.00 75.49  ? 36  GLN A CG  1 
ATOM   279   C CD  . GLN A 1 36  ? 55.974  29.725  2.689   1.00 74.90  ? 36  GLN A CD  1 
ATOM   280   O OE1 . GLN A 1 36  ? 54.795  29.305  2.662   1.00 73.77  ? 36  GLN A OE1 1 
ATOM   281   N NE2 . GLN A 1 36  ? 56.403  30.716  1.914   1.00 75.81  ? 36  GLN A NE2 1 
ATOM   282   N N   . ALA A 1 37  ? 56.830  29.942  8.247   1.00 84.18  ? 37  ALA A N   1 
ATOM   283   C CA  . ALA A 1 37  ? 55.919  29.955  9.386   1.00 85.92  ? 37  ALA A CA  1 
ATOM   284   C C   . ALA A 1 37  ? 54.930  31.119  9.222   1.00 83.82  ? 37  ALA A C   1 
ATOM   285   O O   . ALA A 1 37  ? 55.297  32.304  9.125   1.00 81.47  ? 37  ALA A O   1 
ATOM   286   C CB  . ALA A 1 37  ? 56.717  30.078  10.671  1.00 90.18  ? 37  ALA A CB  1 
ATOM   287   N N   . PRO A 1 38  ? 53.626  30.803  9.145   1.00 80.73  ? 38  PRO A N   1 
ATOM   288   C CA  . PRO A 1 38  ? 52.619  31.802  8.786   1.00 80.17  ? 38  PRO A CA  1 
ATOM   289   C C   . PRO A 1 38  ? 52.426  32.913  9.817   1.00 79.97  ? 38  PRO A C   1 
ATOM   290   O O   . PRO A 1 38  ? 52.252  34.041  9.408   1.00 81.12  ? 38  PRO A O   1 
ATOM   291   C CB  . PRO A 1 38  ? 51.332  31.031  8.533   1.00 77.10  ? 38  PRO A CB  1 
ATOM   292   C CG  . PRO A 1 38  ? 51.570  29.674  9.121   1.00 77.97  ? 38  PRO A CG  1 
ATOM   293   C CD  . PRO A 1 38  ? 53.065  29.475  9.387   1.00 79.90  ? 38  PRO A CD  1 
ATOM   294   N N   . TYR A 1 39  ? 52.504  32.600  11.121  1.00 79.63  ? 39  TYR A N   1 
ATOM   295   C CA  . TYR A 1 39  ? 52.297  33.556  12.201  1.00 78.70  ? 39  TYR A CA  1 
ATOM   296   C C   . TYR A 1 39  ? 53.604  34.195  12.672  1.00 82.71  ? 39  TYR A C   1 
ATOM   297   O O   . TYR A 1 39  ? 53.574  34.970  13.621  1.00 83.47  ? 39  TYR A O   1 
ATOM   298   C CB  . TYR A 1 39  ? 51.626  32.879  13.402  1.00 76.68  ? 39  TYR A CB  1 
ATOM   299   C CG  . TYR A 1 39  ? 50.259  32.287  13.075  1.00 74.19  ? 39  TYR A CG  1 
ATOM   300   C CD1 . TYR A 1 39  ? 49.108  33.069  13.157  1.00 73.33  ? 39  TYR A CD1 1 
ATOM   301   C CD2 . TYR A 1 39  ? 50.122  30.979  12.645  1.00 71.42  ? 39  TYR A CD2 1 
ATOM   302   C CE1 . TYR A 1 39  ? 47.864  32.570  12.818  1.00 71.20  ? 39  TYR A CE1 1 
ATOM   303   C CE2 . TYR A 1 39  ? 48.880  30.476  12.301  1.00 70.72  ? 39  TYR A CE2 1 
ATOM   304   C CZ  . TYR A 1 39  ? 47.746  31.267  12.380  1.00 69.82  ? 39  TYR A CZ  1 
ATOM   305   O OH  . TYR A 1 39  ? 46.513  30.785  12.052  1.00 67.39  ? 39  TYR A OH  1 
ATOM   306   N N   . GLU A 1 40  ? 54.741  33.864  12.045  1.00 86.02  ? 40  GLU A N   1 
ATOM   307   C CA  . GLU A 1 40  ? 56.021  34.415  12.459  1.00 90.18  ? 40  GLU A CA  1 
ATOM   308   C C   . GLU A 1 40  ? 56.599  35.282  11.341  1.00 92.21  ? 40  GLU A C   1 
ATOM   309   O O   . GLU A 1 40  ? 57.200  36.321  11.607  1.00 92.40  ? 40  GLU A O   1 
ATOM   310   C CB  . GLU A 1 40  ? 57.046  33.331  12.802  1.00 94.30  ? 40  GLU A CB  1 
ATOM   311   C CG  . GLU A 1 40  ? 56.572  32.202  13.719  1.00 95.11  ? 40  GLU A CG  1 
ATOM   312   C CD  . GLU A 1 40  ? 57.735  31.285  14.127  1.00 100.87 ? 40  GLU A CD  1 
ATOM   313   O OE1 . GLU A 1 40  ? 58.568  30.934  13.260  1.00 103.87 ? 40  GLU A OE1 1 
ATOM   314   O OE2 . GLU A 1 40  ? 57.847  30.891  15.309  1.00 104.98 ? 40  GLU A OE2 1 
ATOM   315   N N   . ASP A 1 41  ? 56.419  34.843  10.088  1.00 93.94  ? 41  ASP A N   1 
ATOM   316   C CA  . ASP A 1 41  ? 57.000  35.515  8.936   1.00 97.19  ? 41  ASP A CA  1 
ATOM   317   C C   . ASP A 1 41  ? 56.258  36.809  8.616   1.00 100.83 ? 41  ASP A C   1 
ATOM   318   O O   . ASP A 1 41  ? 55.028  36.900  8.764   1.00 101.48 ? 41  ASP A O   1 
ATOM   319   C CB  . ASP A 1 41  ? 56.961  34.648  7.686   1.00 95.78  ? 41  ASP A CB  1 
ATOM   320   C CG  . ASP A 1 41  ? 58.061  33.605  7.550   1.00 97.88  ? 41  ASP A CG  1 
ATOM   321   O OD1 . ASP A 1 41  ? 59.100  33.707  8.248   1.00 99.81  ? 41  ASP A OD1 1 
ATOM   322   O OD2 . ASP A 1 41  ? 57.875  32.697  6.730   1.00 97.21  ? 41  ASP A OD2 1 
ATOM   323   N N   . GLU A 1 42  ? 57.033  37.784  8.118   1.00 101.09 ? 42  GLU A N   1 
ATOM   324   C CA  . GLU A 1 42  ? 56.469  38.918  7.412   1.00 102.99 ? 42  GLU A CA  1 
ATOM   325   C C   . GLU A 1 42  ? 55.395  38.456  6.422   1.00 101.15 ? 42  GLU A C   1 
ATOM   326   O O   . GLU A 1 42  ? 55.645  37.609  5.571   1.00 99.90  ? 42  GLU A O   1 
ATOM   327   C CB  . GLU A 1 42  ? 57.580  39.672  6.684   1.00 107.77 ? 42  GLU A CB  1 
ATOM   328   C CG  . GLU A 1 42  ? 57.071  40.818  5.810   1.00 111.67 ? 42  GLU A CG  1 
ATOM   329   C CD  . GLU A 1 42  ? 58.171  41.681  5.215   1.00 117.48 ? 42  GLU A CD  1 
ATOM   330   O OE1 . GLU A 1 42  ? 59.020  42.182  5.991   1.00 115.62 ? 42  GLU A OE1 1 
ATOM   331   O OE2 . GLU A 1 42  ? 58.171  41.851  3.975   1.00 124.28 ? 42  GLU A OE2 1 
ATOM   332   N N   . ARG A 1 43  ? 54.222  39.088  6.496   1.00 100.01 ? 43  ARG A N   1 
ATOM   333   C CA  . ARG A 1 43  ? 53.071  38.685  5.717   1.00 102.23 ? 43  ARG A CA  1 
ATOM   334   C C   . ARG A 1 43  ? 53.250  39.003  4.233   1.00 97.82  ? 43  ARG A C   1 
ATOM   335   O O   . ARG A 1 43  ? 53.580  40.130  3.885   1.00 98.94  ? 43  ARG A O   1 
ATOM   336   C CB  . ARG A 1 43  ? 51.848  39.470  6.197   1.00 111.19 ? 43  ARG A CB  1 
ATOM   337   C CG  . ARG A 1 43  ? 51.507  39.442  7.684   1.00 118.45 ? 43  ARG A CG  1 
ATOM   338   C CD  . ARG A 1 43  ? 50.215  40.230  7.923   1.00 125.94 ? 43  ARG A CD  1 
ATOM   339   N NE  . ARG A 1 43  ? 49.432  40.334  6.681   1.00 127.33 ? 43  ARG A NE  1 
ATOM   340   C CZ  . ARG A 1 43  ? 49.146  41.477  6.044   1.00 125.31 ? 43  ARG A CZ  1 
ATOM   341   N NH1 . ARG A 1 43  ? 49.070  41.479  4.721   1.00 125.09 ? 43  ARG A NH1 1 
ATOM   342   N NH2 . ARG A 1 43  ? 49.081  42.627  6.701   1.00 121.07 ? 43  ARG A NH2 1 
ATOM   343   N N   . LYS A 1 44  ? 52.954  38.019  3.372   1.00 94.28  ? 44  LYS A N   1 
ATOM   344   C CA  . LYS A 1 44  ? 52.953  38.184  1.928   1.00 93.65  ? 44  LYS A CA  1 
ATOM   345   C C   . LYS A 1 44  ? 51.740  37.475  1.329   1.00 92.18  ? 44  LYS A C   1 
ATOM   346   O O   . LYS A 1 44  ? 51.280  36.443  1.836   1.00 92.60  ? 44  LYS A O   1 
ATOM   347   C CB  . LYS A 1 44  ? 54.200  37.561  1.291   1.00 95.93  ? 44  LYS A CB  1 
ATOM   348   C CG  . LYS A 1 44  ? 55.491  37.654  2.114   1.00 98.74  ? 44  LYS A CG  1 
ATOM   349   C CD  . LYS A 1 44  ? 56.732  37.086  1.431   1.00 100.83 ? 44  LYS A CD  1 
ATOM   350   C CE  . LYS A 1 44  ? 57.022  37.836  0.168   1.00 103.51 ? 44  LYS A CE  1 
ATOM   351   N NZ  . LYS A 1 44  ? 58.447  37.813  -0.187  1.00 106.53 ? 44  LYS A NZ  1 
ATOM   352   N N   . ASP A 1 45  ? 51.278  37.991  0.188   1.00 88.84  ? 45  ASP A N   1 
ATOM   353   C CA  . ASP A 1 45  ? 50.035  37.534  -0.409  1.00 84.66  ? 45  ASP A CA  1 
ATOM   354   C C   . ASP A 1 45  ? 50.199  36.102  -0.933  1.00 82.74  ? 45  ASP A C   1 
ATOM   355   O O   . ASP A 1 45  ? 49.338  35.247  -0.721  1.00 81.95  ? 45  ASP A O   1 
ATOM   356   C CB  . ASP A 1 45  ? 49.535  38.595  -1.383  1.00 84.24  ? 45  ASP A CB  1 
ATOM   357   C CG  . ASP A 1 45  ? 49.167  39.906  -0.704  1.00 84.44  ? 45  ASP A CG  1 
ATOM   358   O OD1 . ASP A 1 45  ? 48.863  39.847  0.505   1.00 82.90  ? 45  ASP A OD1 1 
ATOM   359   O OD2 . ASP A 1 45  ? 49.265  40.982  -1.352  1.00 86.35  ? 45  ASP A OD2 1 
ATOM   360   N N   . GLU A 1 46  ? 51.304  35.853  -1.637  1.00 82.64  ? 46  GLU A N   1 
ATOM   361   C CA  . GLU A 1 46  ? 51.630  34.538  -2.166  1.00 80.69  ? 46  GLU A CA  1 
ATOM   362   C C   . GLU A 1 46  ? 50.697  34.158  -3.314  1.00 77.64  ? 46  GLU A C   1 
ATOM   363   O O   . GLU A 1 46  ? 50.401  33.001  -3.484  1.00 76.82  ? 46  GLU A O   1 
ATOM   364   C CB  . GLU A 1 46  ? 51.623  33.486  -1.054  1.00 80.13  ? 46  GLU A CB  1 
ATOM   365   C CG  . GLU A 1 46  ? 52.704  33.692  0.006   1.00 81.28  ? 46  GLU A CG  1 
ATOM   366   C CD  . GLU A 1 46  ? 53.998  32.919  -0.184  1.00 82.66  ? 46  GLU A CD  1 
ATOM   367   O OE1 . GLU A 1 46  ? 54.188  32.240  -1.226  1.00 83.66  ? 46  GLU A OE1 1 
ATOM   368   O OE2 . GLU A 1 46  ? 54.828  33.001  0.753   1.00 83.12  ? 46  GLU A OE2 1 
ATOM   369   N N   . LEU A 1 47  ? 50.316  35.104  -4.164  1.00 77.61  ? 47  LEU A N   1 
ATOM   370   C CA  . LEU A 1 47  ? 49.416  34.838  -5.273  1.00 77.50  ? 47  LEU A CA  1 
ATOM   371   C C   . LEU A 1 47  ? 49.848  33.608  -6.073  1.00 79.08  ? 47  LEU A C   1 
ATOM   372   O O   . LEU A 1 47  ? 49.028  32.745  -6.361  1.00 79.95  ? 47  LEU A O   1 
ATOM   373   C CB  . LEU A 1 47  ? 49.257  36.049  -6.190  1.00 78.23  ? 47  LEU A CB  1 
ATOM   374   C CG  . LEU A 1 47  ? 48.777  37.343  -5.520  1.00 78.66  ? 47  LEU A CG  1 
ATOM   375   C CD1 . LEU A 1 47  ? 48.402  38.403  -6.550  1.00 79.64  ? 47  LEU A CD1 1 
ATOM   376   C CD2 . LEU A 1 47  ? 47.612  37.104  -4.557  1.00 77.46  ? 47  LEU A CD2 1 
ATOM   377   N N   . GLU A 1 48  ? 51.120  33.502  -6.441  1.00 82.61  ? 48  GLU A N   1 
ATOM   378   C CA  . GLU A 1 48  ? 51.535  32.531  -7.445  1.00 84.32  ? 48  GLU A CA  1 
ATOM   379   C C   . GLU A 1 48  ? 51.214  31.118  -6.967  1.00 82.90  ? 48  GLU A C   1 
ATOM   380   O O   . GLU A 1 48  ? 50.737  30.294  -7.750  1.00 83.10  ? 48  GLU A O   1 
ATOM   381   C CB  . GLU A 1 48  ? 53.024  32.720  -7.715  1.00 88.05  ? 48  GLU A CB  1 
ATOM   382   C CG  . GLU A 1 48  ? 53.506  32.194  -9.064  1.00 90.75  ? 48  GLU A CG  1 
ATOM   383   C CD  . GLU A 1 48  ? 54.997  32.506  -9.227  1.00 95.03  ? 48  GLU A CD  1 
ATOM   384   O OE1 . GLU A 1 48  ? 55.743  31.518  -9.066  1.00 96.40  ? 48  GLU A OE1 1 
ATOM   385   O OE2 . GLU A 1 48  ? 55.439  33.677  -9.457  1.00 95.19  ? 48  GLU A OE2 1 
ATOM   386   N N   . LEU A 1 49  ? 51.463  30.858  -5.674  1.00 82.02  ? 49  LEU A N   1 
ATOM   387   C CA  . LEU A 1 49  ? 51.138  29.578  -5.059  1.00 80.72  ? 49  LEU A CA  1 
ATOM   388   C C   . LEU A 1 49  ? 49.630  29.457  -4.809  1.00 79.16  ? 49  LEU A C   1 
ATOM   389   O O   . LEU A 1 49  ? 49.087  28.355  -4.847  1.00 78.56  ? 49  LEU A O   1 
ATOM   390   C CB  . LEU A 1 49  ? 51.914  29.370  -3.757  1.00 80.36  ? 49  LEU A CB  1 
ATOM   391   C CG  . LEU A 1 49  ? 53.443  29.272  -3.835  1.00 81.37  ? 49  LEU A CG  1 
ATOM   392   C CD1 . LEU A 1 49  ? 53.926  28.793  -2.469  1.00 80.49  ? 49  LEU A CD1 1 
ATOM   393   C CD2 . LEU A 1 49  ? 53.964  28.385  -4.957  1.00 81.73  ? 49  LEU A CD2 1 
ATOM   394   N N   . MET A 1 50  ? 48.934  30.564  -4.527  1.00 79.45  ? 50  MET A N   1 
ATOM   395   C CA  . MET A 1 50  ? 47.497  30.467  -4.299  1.00 80.03  ? 50  MET A CA  1 
ATOM   396   C C   . MET A 1 50  ? 46.768  30.038  -5.580  1.00 79.50  ? 50  MET A C   1 
ATOM   397   O O   . MET A 1 50  ? 45.818  29.266  -5.481  1.00 78.58  ? 50  MET A O   1 
ATOM   398   C CB  . MET A 1 50  ? 46.880  31.743  -3.709  1.00 80.43  ? 50  MET A CB  1 
ATOM   399   C CG  . MET A 1 50  ? 46.943  31.833  -2.182  1.00 80.64  ? 50  MET A CG  1 
ATOM   400   S SD  . MET A 1 50  ? 46.261  33.367  -1.499  1.00 82.39  ? 50  MET A SD  1 
ATOM   401   C CE  . MET A 1 50  ? 44.545  32.837  -1.468  1.00 80.23  ? 50  MET A CE  1 
ATOM   402   N N   . LYS A 1 51  ? 47.228  30.482  -6.767  1.00 79.25  ? 51  LYS A N   1 
ATOM   403   C CA  . LYS A 1 51  ? 46.632  30.067  -8.035  1.00 77.98  ? 51  LYS A CA  1 
ATOM   404   C C   . LYS A 1 51  ? 46.782  28.558  -8.221  1.00 75.56  ? 51  LYS A C   1 
ATOM   405   O O   . LYS A 1 51  ? 45.895  27.907  -8.773  1.00 74.84  ? 51  LYS A O   1 
ATOM   406   C CB  . LYS A 1 51  ? 47.265  30.716  -9.271  1.00 80.39  ? 51  LYS A CB  1 
ATOM   407   C CG  . LYS A 1 51  ? 47.175  32.229  -9.318  1.00 83.60  ? 51  LYS A CG  1 
ATOM   408   C CD  . LYS A 1 51  ? 48.148  32.948  -10.260 1.00 86.83  ? 51  LYS A CD  1 
ATOM   409   C CE  . LYS A 1 51  ? 48.183  34.433  -10.014 1.00 88.72  ? 51  LYS A CE  1 
ATOM   410   N NZ  . LYS A 1 51  ? 49.248  35.158  -10.724 1.00 91.33  ? 51  LYS A NZ  1 
ATOM   411   N N   . PHE A 1 52  ? 47.921  28.014  -7.779  1.00 74.05  ? 52  PHE A N   1 
ATOM   412   C CA  . PHE A 1 52  ? 48.184  26.590  -7.904  1.00 72.77  ? 52  PHE A CA  1 
ATOM   413   C C   . PHE A 1 52  ? 47.271  25.822  -6.946  1.00 70.35  ? 52  PHE A C   1 
ATOM   414   O O   . PHE A 1 52  ? 46.629  24.846  -7.351  1.00 69.10  ? 52  PHE A O   1 
ATOM   415   C CB  . PHE A 1 52  ? 49.678  26.307  -7.699  1.00 73.19  ? 52  PHE A CB  1 
ATOM   416   C CG  . PHE A 1 52  ? 50.066  24.841  -7.518  1.00 72.63  ? 52  PHE A CG  1 
ATOM   417   C CD1 . PHE A 1 52  ? 50.131  23.965  -8.607  1.00 72.84  ? 52  PHE A CD1 1 
ATOM   418   C CD2 . PHE A 1 52  ? 50.396  24.344  -6.257  1.00 71.79  ? 52  PHE A CD2 1 
ATOM   419   C CE1 . PHE A 1 52  ? 50.523  22.639  -8.444  1.00 72.10  ? 52  PHE A CE1 1 
ATOM   420   C CE2 . PHE A 1 52  ? 50.784  23.016  -6.095  1.00 71.59  ? 52  PHE A CE2 1 
ATOM   421   C CZ  . PHE A 1 52  ? 50.845  22.164  -7.187  1.00 71.57  ? 52  PHE A CZ  1 
ATOM   422   N N   . ASP A 1 53  ? 47.211  26.289  -5.691  1.00 68.89  ? 53  ASP A N   1 
ATOM   423   C CA  . ASP A 1 53  ? 46.502  25.579  -4.638  1.00 67.66  ? 53  ASP A CA  1 
ATOM   424   C C   . ASP A 1 53  ? 44.989  25.565  -4.852  1.00 66.62  ? 53  ASP A C   1 
ATOM   425   O O   . ASP A 1 53  ? 44.362  24.512  -4.744  1.00 65.04  ? 53  ASP A O   1 
ATOM   426   C CB  . ASP A 1 53  ? 46.749  26.232  -3.294  1.00 67.44  ? 53  ASP A CB  1 
ATOM   427   C CG  . ASP A 1 53  ? 48.177  26.140  -2.795  1.00 67.80  ? 53  ASP A CG  1 
ATOM   428   O OD1 . ASP A 1 53  ? 48.790  25.059  -2.960  1.00 66.63  ? 53  ASP A OD1 1 
ATOM   429   O OD2 . ASP A 1 53  ? 48.629  27.148  -2.217  1.00 68.73  ? 53  ASP A OD2 1 
ATOM   430   N N   . LEU A 1 54  ? 44.439  26.764  -5.116  1.00 66.87  ? 54  LEU A N   1 
ATOM   431   C CA  . LEU A 1 54  ? 43.022  26.980  -5.358  1.00 66.26  ? 54  LEU A CA  1 
ATOM   432   C C   . LEU A 1 54  ? 42.558  26.097  -6.505  1.00 67.13  ? 54  LEU A C   1 
ATOM   433   O O   . LEU A 1 54  ? 41.522  25.472  -6.409  1.00 66.64  ? 54  LEU A O   1 
ATOM   434   C CB  . LEU A 1 54  ? 42.724  28.453  -5.665  1.00 66.31  ? 54  LEU A CB  1 
ATOM   435   C CG  . LEU A 1 54  ? 42.866  29.430  -4.495  1.00 65.53  ? 54  LEU A CG  1 
ATOM   436   C CD1 . LEU A 1 54  ? 42.417  30.777  -4.967  1.00 66.47  ? 54  LEU A CD1 1 
ATOM   437   C CD2 . LEU A 1 54  ? 42.103  29.038  -3.251  1.00 64.02  ? 54  LEU A CD2 1 
ATOM   438   N N   . GLU A 1 55  ? 43.313  26.083  -7.595  1.00 70.09  ? 55  GLU A N   1 
ATOM   439   C CA  . GLU A 1 55  ? 42.994  25.244  -8.731  1.00 72.44  ? 55  GLU A CA  1 
ATOM   440   C C   . GLU A 1 55  ? 43.048  23.768  -8.322  1.00 71.01  ? 55  GLU A C   1 
ATOM   441   O O   . GLU A 1 55  ? 42.156  22.984  -8.691  1.00 71.76  ? 55  GLU A O   1 
ATOM   442   C CB  . GLU A 1 55  ? 43.963  25.661  -9.835  1.00 78.19  ? 55  GLU A CB  1 
ATOM   443   C CG  . GLU A 1 55  ? 43.767  24.933  -11.161 1.00 82.24  ? 55  GLU A CG  1 
ATOM   444   C CD  . GLU A 1 55  ? 42.431  25.190  -11.825 1.00 86.34  ? 55  GLU A CD  1 
ATOM   445   O OE1 . GLU A 1 55  ? 41.894  26.357  -11.863 1.00 88.08  ? 55  GLU A OE1 1 
ATOM   446   O OE2 . GLU A 1 55  ? 41.960  24.132  -12.325 1.00 90.46  ? 55  GLU A OE2 1 
ATOM   447   N N   . ASN A 1 56  ? 44.054  23.372  -7.525  1.00 69.09  ? 56  ASN A N   1 
ATOM   448   C CA  . ASN A 1 56  ? 44.072  21.995  -7.049  1.00 67.92  ? 56  ASN A CA  1 
ATOM   449   C C   . ASN A 1 56  ? 42.783  21.712  -6.261  1.00 65.59  ? 56  ASN A C   1 
ATOM   450   O O   . ASN A 1 56  ? 42.110  20.708  -6.487  1.00 63.79  ? 56  ASN A O   1 
ATOM   451   C CB  . ASN A 1 56  ? 45.315  21.638  -6.234  1.00 68.19  ? 56  ASN A CB  1 
ATOM   452   C CG  . ASN A 1 56  ? 46.589  21.667  -7.047  1.00 70.08  ? 56  ASN A CG  1 
ATOM   453   O OD1 . ASN A 1 56  ? 46.575  21.354  -8.242  1.00 71.76  ? 56  ASN A OD1 1 
ATOM   454   N ND2 . ASN A 1 56  ? 47.687  22.090  -6.438  1.00 69.96  ? 56  ASN A ND2 1 
ATOM   455   N N   . ILE A 1 57  ? 42.458  22.609  -5.330  1.00 64.54  ? 57  ILE A N   1 
ATOM   456   C CA  . ILE A 1 57  ? 41.348  22.409  -4.428  1.00 63.24  ? 57  ILE A CA  1 
ATOM   457   C C   . ILE A 1 57  ? 40.056  22.352  -5.230  1.00 64.38  ? 57  ILE A C   1 
ATOM   458   O O   . ILE A 1 57  ? 39.136  21.641  -4.839  1.00 63.09  ? 57  ILE A O   1 
ATOM   459   C CB  . ILE A 1 57  ? 41.336  23.504  -3.353  1.00 62.23  ? 57  ILE A CB  1 
ATOM   460   C CG1 . ILE A 1 57  ? 42.446  23.275  -2.362  1.00 61.53  ? 57  ILE A CG1 1 
ATOM   461   C CG2 . ILE A 1 57  ? 39.982  23.583  -2.654  1.00 61.29  ? 57  ILE A CG2 1 
ATOM   462   C CD1 . ILE A 1 57  ? 42.587  24.385  -1.349  1.00 61.62  ? 57  ILE A CD1 1 
ATOM   463   N N   . LYS A 1 58  ? 40.005  23.050  -6.368  1.00 67.07  ? 58  LYS A N   1 
ATOM   464   C CA  . LYS A 1 58  ? 38.867  22.926  -7.268  1.00 69.72  ? 58  LYS A CA  1 
ATOM   465   C C   . LYS A 1 58  ? 38.825  21.500  -7.813  1.00 71.08  ? 58  LYS A C   1 
ATOM   466   O O   . LYS A 1 58  ? 37.976  20.745  -7.405  1.00 70.35  ? 58  LYS A O   1 
ATOM   467   C CB  . LYS A 1 58  ? 38.845  24.018  -8.345  1.00 72.27  ? 58  LYS A CB  1 
ATOM   468   C CG  . LYS A 1 58  ? 38.330  25.364  -7.833  1.00 73.60  ? 58  LYS A CG  1 
ATOM   469   C CD  . LYS A 1 58  ? 38.758  26.592  -8.632  1.00 76.07  ? 58  LYS A CD  1 
ATOM   470   C CE  . LYS A 1 58  ? 38.168  26.617  -10.011 1.00 77.87  ? 58  LYS A CE  1 
ATOM   471   N NZ  . LYS A 1 58  ? 38.808  27.662  -10.813 1.00 79.27  ? 58  LYS A NZ  1 
ATOM   472   N N   . GLU A 1 59  ? 39.797  21.091  -8.639  1.00 76.50  ? 59  GLU A N   1 
ATOM   473   C CA  . GLU A 1 59  ? 39.882  19.726  -9.165  1.00 76.17  ? 59  GLU A CA  1 
ATOM   474   C C   . GLU A 1 59  ? 39.763  18.669  -8.062  1.00 73.69  ? 59  GLU A C   1 
ATOM   475   O O   . GLU A 1 59  ? 39.502  17.501  -8.355  1.00 73.59  ? 59  GLU A O   1 
ATOM   476   C CB  . GLU A 1 59  ? 41.210  19.493  -9.893  1.00 79.07  ? 59  GLU A CB  1 
ATOM   477   C CG  . GLU A 1 59  ? 41.224  19.941  -11.352 1.00 83.10  ? 59  GLU A CG  1 
ATOM   478   C CD  . GLU A 1 59  ? 42.630  20.227  -11.868 1.00 90.53  ? 59  GLU A CD  1 
ATOM   479   O OE1 . GLU A 1 59  ? 43.450  19.309  -12.166 1.00 90.74  ? 59  GLU A OE1 1 
ATOM   480   O OE2 . GLU A 1 59  ? 42.923  21.447  -11.928 1.00 97.73  ? 59  GLU A OE2 1 
ATOM   481   N N   . GLY A 1 60  ? 39.978  19.061  -6.799  1.00 72.36  ? 60  GLY A N   1 
ATOM   482   C CA  . GLY A 1 60  ? 39.992  18.116  -5.691  1.00 71.70  ? 60  GLY A CA  1 
ATOM   483   C C   . GLY A 1 60  ? 38.588  17.739  -5.233  1.00 69.90  ? 60  GLY A C   1 
ATOM   484   O O   . GLY A 1 60  ? 38.434  16.753  -4.513  1.00 72.05  ? 60  GLY A O   1 
ATOM   485   N N   . GLY A 1 61  ? 37.606  18.551  -5.654  1.00 67.35  ? 61  GLY A N   1 
ATOM   486   C CA  . GLY A 1 61  ? 36.195  18.254  -5.520  1.00 65.24  ? 61  GLY A CA  1 
ATOM   487   C C   . GLY A 1 61  ? 35.492  19.182  -4.538  1.00 64.00  ? 61  GLY A C   1 
ATOM   488   O O   . GLY A 1 61  ? 34.307  18.997  -4.288  1.00 66.19  ? 61  GLY A O   1 
ATOM   489   N N   . TYR A 1 62  ? 36.209  20.186  -4.020  1.00 63.17  ? 62  TYR A N   1 
ATOM   490   C CA  . TYR A 1 62  ? 35.713  21.066  -2.970  1.00 61.77  ? 62  TYR A CA  1 
ATOM   491   C C   . TYR A 1 62  ? 35.035  22.274  -3.624  1.00 60.74  ? 62  TYR A C   1 
ATOM   492   O O   . TYR A 1 62  ? 35.138  22.454  -4.840  1.00 59.99  ? 62  TYR A O   1 
ATOM   493   C CB  . TYR A 1 62  ? 36.858  21.369  -1.986  1.00 61.98  ? 62  TYR A CB  1 
ATOM   494   C CG  . TYR A 1 62  ? 37.621  20.139  -1.502  1.00 62.70  ? 62  TYR A CG  1 
ATOM   495   C CD1 . TYR A 1 62  ? 37.189  19.384  -0.421  1.00 63.00  ? 62  TYR A CD1 1 
ATOM   496   C CD2 . TYR A 1 62  ? 38.767  19.701  -2.150  1.00 64.30  ? 62  TYR A CD2 1 
ATOM   497   C CE1 . TYR A 1 62  ? 37.841  18.216  -0.024  1.00 63.06  ? 62  TYR A CE1 1 
ATOM   498   C CE2 . TYR A 1 62  ? 39.451  18.562  -1.742  1.00 64.47  ? 62  TYR A CE2 1 
ATOM   499   C CZ  . TYR A 1 62  ? 38.997  17.812  -0.672  1.00 63.68  ? 62  TYR A CZ  1 
ATOM   500   O OH  . TYR A 1 62  ? 39.726  16.713  -0.282  1.00 62.60  ? 62  TYR A OH  1 
ATOM   501   N N   . ASN A 1 63  ? 34.270  23.021  -2.805  1.00 59.85  ? 63  ASN A N   1 
ATOM   502   C CA  . ASN A 1 63  ? 33.561  24.222  -3.234  1.00 60.61  ? 63  ASN A CA  1 
ATOM   503   C C   . ASN A 1 63  ? 33.820  25.396  -2.280  1.00 62.49  ? 63  ASN A C   1 
ATOM   504   O O   . ASN A 1 63  ? 33.361  26.526  -2.531  1.00 62.49  ? 63  ASN A O   1 
ATOM   505   C CB  . ASN A 1 63  ? 32.061  23.961  -3.416  1.00 59.68  ? 63  ASN A CB  1 
ATOM   506   C CG  . ASN A 1 63  ? 31.283  23.749  -2.131  1.00 58.22  ? 63  ASN A CG  1 
ATOM   507   O OD1 . ASN A 1 63  ? 31.724  24.065  -1.016  1.00 57.62  ? 63  ASN A OD1 1 
ATOM   508   N ND2 . ASN A 1 63  ? 30.094  23.198  -2.273  1.00 57.74  ? 63  ASN A ND2 1 
ATOM   509   N N   . THR A 1 64  ? 34.581  25.132  -1.200  1.00 64.38  ? 64  THR A N   1 
ATOM   510   C CA  . THR A 1 64  ? 34.877  26.129  -0.174  1.00 66.00  ? 64  THR A CA  1 
ATOM   511   C C   . THR A 1 64  ? 36.275  25.916  0.429   1.00 66.06  ? 64  THR A C   1 
ATOM   512   O O   . THR A 1 64  ? 36.809  24.801  0.438   1.00 64.91  ? 64  THR A O   1 
ATOM   513   C CB  . THR A 1 64  ? 33.763  26.030  0.871   1.00 66.05  ? 64  THR A CB  1 
ATOM   514   O OG1 . THR A 1 64  ? 32.600  26.291  0.103   1.00 68.05  ? 64  THR A OG1 1 
ATOM   515   C CG2 . THR A 1 64  ? 33.824  27.067  1.978   1.00 65.69  ? 64  THR A CG2 1 
ATOM   516   N N   . ILE A 1 65  ? 36.821  26.979  1.040   1.00 66.66  ? 65  ILE A N   1 
ATOM   517   C CA  . ILE A 1 65  ? 38.109  26.854  1.782   1.00 67.07  ? 65  ILE A CA  1 
ATOM   518   C C   . ILE A 1 65  ? 37.882  27.402  3.196   1.00 66.14  ? 65  ILE A C   1 
ATOM   519   O O   . ILE A 1 65  ? 37.146  28.384  3.326   1.00 66.54  ? 65  ILE A O   1 
ATOM   520   C CB  . ILE A 1 65  ? 39.252  27.574  1.051   1.00 68.47  ? 65  ILE A CB  1 
ATOM   521   C CG1 . ILE A 1 65  ? 38.888  29.012  0.697   1.00 69.58  ? 65  ILE A CG1 1 
ATOM   522   C CG2 . ILE A 1 65  ? 39.691  26.788  -0.183  1.00 70.17  ? 65  ILE A CG2 1 
ATOM   523   C CD1 . ILE A 1 65  ? 40.088  29.914  0.483   1.00 70.37  ? 65  ILE A CD1 1 
ATOM   524   N N   . ARG A 1 66  ? 38.445  26.753  4.210   1.00 64.82  ? 66  ARG A N   1 
ATOM   525   C CA  . ARG A 1 66  ? 38.324  27.221  5.612   1.00 64.31  ? 66  ARG A CA  1 
ATOM   526   C C   . ARG A 1 66  ? 39.689  27.782  6.031   1.00 63.66  ? 66  ARG A C   1 
ATOM   527   O O   . ARG A 1 66  ? 40.700  27.201  5.611   1.00 64.27  ? 66  ARG A O   1 
ATOM   528   C CB  . ARG A 1 66  ? 37.894  26.099  6.557   1.00 64.08  ? 66  ARG A CB  1 
ATOM   529   C CG  . ARG A 1 66  ? 37.783  26.447  8.033   1.00 65.32  ? 66  ARG A CG  1 
ATOM   530   C CD  . ARG A 1 66  ? 39.030  26.049  8.798   1.00 66.73  ? 66  ARG A CD  1 
ATOM   531   N NE  . ARG A 1 66  ? 38.721  25.567  10.145  1.00 67.51  ? 66  ARG A NE  1 
ATOM   532   C CZ  . ARG A 1 66  ? 38.985  26.223  11.259  1.00 70.99  ? 66  ARG A CZ  1 
ATOM   533   N NH1 . ARG A 1 66  ? 39.258  27.513  11.220  1.00 70.68  ? 66  ARG A NH1 1 
ATOM   534   N NH2 . ARG A 1 66  ? 38.982  25.584  12.410  1.00 72.09  ? 66  ARG A NH2 1 
ATOM   535   N N   . THR A 1 67  ? 39.715  28.868  6.814   1.00 62.11  ? 67  THR A N   1 
ATOM   536   C CA  . THR A 1 67  ? 40.993  29.517  7.168   1.00 61.84  ? 67  THR A CA  1 
ATOM   537   C C   . THR A 1 67  ? 41.053  29.804  8.647   1.00 61.00  ? 67  THR A C   1 
ATOM   538   O O   . THR A 1 67  ? 40.053  29.557  9.336   1.00 60.07  ? 67  THR A O   1 
ATOM   539   C CB  . THR A 1 67  ? 41.191  30.776  6.331   1.00 62.34  ? 67  THR A CB  1 
ATOM   540   O OG1 . THR A 1 67  ? 40.274  31.716  6.875   1.00 63.56  ? 67  THR A OG1 1 
ATOM   541   C CG2 . THR A 1 67  ? 40.919  30.567  4.853   1.00 62.50  ? 67  THR A CG2 1 
ATOM   542   N N   . TRP A 1 68  ? 42.212  30.248  9.131   1.00 60.79  ? 68  TRP A N   1 
ATOM   543   C CA  . TRP A 1 68  ? 42.420  30.510  10.546  1.00 61.20  ? 68  TRP A CA  1 
ATOM   544   C C   . TRP A 1 68  ? 42.847  31.957  10.760  1.00 62.64  ? 68  TRP A C   1 
ATOM   545   O O   . TRP A 1 68  ? 42.840  32.460  11.885  1.00 63.81  ? 68  TRP A O   1 
ATOM   546   C CB  . TRP A 1 68  ? 43.478  29.545  11.098  1.00 61.50  ? 68  TRP A CB  1 
ATOM   547   C CG  . TRP A 1 68  ? 43.015  28.111  11.174  1.00 61.15  ? 68  TRP A CG  1 
ATOM   548   C CD1 . TRP A 1 68  ? 42.511  27.467  12.265  1.00 60.81  ? 68  TRP A CD1 1 
ATOM   549   C CD2 . TRP A 1 68  ? 42.991  27.145  10.104  1.00 61.32  ? 68  TRP A CD2 1 
ATOM   550   N NE1 . TRP A 1 68  ? 42.149  26.190  11.948  1.00 60.37  ? 68  TRP A NE1 1 
ATOM   551   C CE2 . TRP A 1 68  ? 42.454  25.958  10.634  1.00 60.63  ? 68  TRP A CE2 1 
ATOM   552   C CE3 . TRP A 1 68  ? 43.387  27.159  8.762   1.00 62.34  ? 68  TRP A CE3 1 
ATOM   553   C CZ2 . TRP A 1 68  ? 42.308  24.808  9.866   1.00 60.57  ? 68  TRP A CZ2 1 
ATOM   554   C CZ3 . TRP A 1 68  ? 43.243  26.013  8.006   1.00 61.93  ? 68  TRP A CZ3 1 
ATOM   555   C CH2 . TRP A 1 68  ? 42.701  24.860  8.550   1.00 60.64  ? 68  TRP A CH2 1 
ATOM   556   N N   . SER A 1 69  ? 43.199  32.600  9.640   1.00 62.61  ? 69  SER A N   1 
ATOM   557   C CA  . SER A 1 69  ? 43.879  33.869  9.584   1.00 62.88  ? 69  SER A CA  1 
ATOM   558   C C   . SER A 1 69  ? 43.267  34.630  8.423   1.00 62.88  ? 69  SER A C   1 
ATOM   559   O O   . SER A 1 69  ? 42.933  34.013  7.408   1.00 61.95  ? 69  SER A O   1 
ATOM   560   C CB  . SER A 1 69  ? 45.349  33.627  9.386   1.00 63.70  ? 69  SER A CB  1 
ATOM   561   O OG  . SER A 1 69  ? 46.088  34.821  9.144   1.00 64.77  ? 69  SER A OG  1 
ATOM   562   N N   . GLN A 1 70  ? 43.134  35.954  8.587   1.00 63.61  ? 70  GLN A N   1 
ATOM   563   C CA  . GLN A 1 70  ? 42.357  36.766  7.667   1.00 64.04  ? 70  GLN A CA  1 
ATOM   564   C C   . GLN A 1 70  ? 43.170  37.015  6.401   1.00 64.83  ? 70  GLN A C   1 
ATOM   565   O O   . GLN A 1 70  ? 44.343  37.266  6.499   1.00 65.30  ? 70  GLN A O   1 
ATOM   566   C CB  . GLN A 1 70  ? 41.965  38.081  8.339   1.00 64.96  ? 70  GLN A CB  1 
ATOM   567   C CG  . GLN A 1 70  ? 43.114  38.856  8.981   1.00 66.07  ? 70  GLN A CG  1 
ATOM   568   C CD  . GLN A 1 70  ? 43.230  38.647  10.477  1.00 66.24  ? 70  GLN A CD  1 
ATOM   569   O OE1 . GLN A 1 70  ? 43.190  37.519  10.980  1.00 65.77  ? 70  GLN A OE1 1 
ATOM   570   N NE2 . GLN A 1 70  ? 43.392  39.737  11.213  1.00 67.34  ? 70  GLN A NE2 1 
ATOM   571   N N   . TYR A 1 71  ? 42.548  36.945  5.222   1.00 65.56  ? 71  TYR A N   1 
ATOM   572   C CA  . TYR A 1 71  ? 43.231  37.211  3.965   1.00 67.67  ? 71  TYR A CA  1 
ATOM   573   C C   . TYR A 1 71  ? 43.272  38.723  3.710   1.00 70.27  ? 71  TYR A C   1 
ATOM   574   O O   . TYR A 1 71  ? 42.421  39.477  4.202   1.00 71.30  ? 71  TYR A O   1 
ATOM   575   C CB  . TYR A 1 71  ? 42.511  36.437  2.847   1.00 68.11  ? 71  TYR A CB  1 
ATOM   576   C CG  . TYR A 1 71  ? 42.877  34.952  2.688   1.00 68.40  ? 71  TYR A CG  1 
ATOM   577   C CD1 . TYR A 1 71  ? 44.174  34.522  2.940   1.00 69.32  ? 71  TYR A CD1 1 
ATOM   578   C CD2 . TYR A 1 71  ? 41.961  33.989  2.263   1.00 66.84  ? 71  TYR A CD2 1 
ATOM   579   C CE1 . TYR A 1 71  ? 44.538  33.193  2.832   1.00 69.54  ? 71  TYR A CE1 1 
ATOM   580   C CE2 . TYR A 1 71  ? 42.327  32.662  2.096   1.00 67.14  ? 71  TYR A CE2 1 
ATOM   581   C CZ  . TYR A 1 71  ? 43.624  32.255  2.394   1.00 69.03  ? 71  TYR A CZ  1 
ATOM   582   O OH  . TYR A 1 71  ? 44.180  30.988  2.320   1.00 69.49  ? 71  TYR A OH  1 
ATOM   583   N N   . SER A 1 72  ? 44.280  39.188  2.949   1.00 71.46  ? 72  SER A N   1 
ATOM   584   C CA  . SER A 1 72  ? 44.332  40.573  2.487   1.00 71.75  ? 72  SER A CA  1 
ATOM   585   C C   . SER A 1 72  ? 43.283  40.795  1.400   1.00 71.47  ? 72  SER A C   1 
ATOM   586   O O   . SER A 1 72  ? 42.701  39.835  0.910   1.00 70.72  ? 72  SER A O   1 
ATOM   587   C CB  . SER A 1 72  ? 45.673  40.880  1.921   1.00 72.72  ? 72  SER A CB  1 
ATOM   588   O OG  . SER A 1 72  ? 45.767  40.294  0.626   1.00 72.55  ? 72  SER A OG  1 
ATOM   589   N N   . GLU A 1 73  ? 43.115  42.043  0.949   1.00 72.61  ? 73  GLU A N   1 
ATOM   590   C CA  . GLU A 1 73  ? 42.267  42.319  -0.198  1.00 73.15  ? 73  GLU A CA  1 
ATOM   591   C C   . GLU A 1 73  ? 42.768  41.596  -1.453  1.00 73.78  ? 73  GLU A C   1 
ATOM   592   O O   . GLU A 1 73  ? 41.951  41.097  -2.233  1.00 73.95  ? 73  GLU A O   1 
ATOM   593   C CB  . GLU A 1 73  ? 42.079  43.797  -0.528  1.00 74.67  ? 73  GLU A CB  1 
ATOM   594   C CG  . GLU A 1 73  ? 41.145  43.947  -1.723  1.00 75.31  ? 73  GLU A CG  1 
ATOM   595   C CD  . GLU A 1 73  ? 40.358  45.222  -1.851  1.00 76.59  ? 73  GLU A CD  1 
ATOM   596   O OE1 . GLU A 1 73  ? 40.678  46.235  -1.202  1.00 78.30  ? 73  GLU A OE1 1 
ATOM   597   O OE2 . GLU A 1 73  ? 39.390  45.159  -2.632  1.00 76.25  ? 73  GLU A OE2 1 
ATOM   598   N N   . ASN A 1 74  ? 44.093  41.533  -1.661  1.00 74.60  ? 74  ASN A N   1 
ATOM   599   C CA  . ASN A 1 74  ? 44.642  40.999  -2.901  1.00 74.96  ? 74  ASN A CA  1 
ATOM   600   C C   . ASN A 1 74  ? 44.400  39.503  -2.979  1.00 73.93  ? 74  ASN A C   1 
ATOM   601   O O   . ASN A 1 74  ? 44.183  38.971  -4.066  1.00 74.14  ? 74  ASN A O   1 
ATOM   602   C CB  . ASN A 1 74  ? 46.149  41.147  -3.047  1.00 75.99  ? 74  ASN A CB  1 
ATOM   603   C CG  . ASN A 1 74  ? 46.603  42.581  -3.134  1.00 77.45  ? 74  ASN A CG  1 
ATOM   604   O OD1 . ASN A 1 74  ? 46.087  43.343  -3.960  1.00 78.24  ? 74  ASN A OD1 1 
ATOM   605   N ND2 . ASN A 1 74  ? 47.579  42.941  -2.309  1.00 77.80  ? 74  ASN A ND2 1 
ATOM   606   N N   . GLN A 1 75  ? 44.500  38.854  -1.816  1.00 73.18  ? 75  GLN A N   1 
ATOM   607   C CA  . GLN A 1 75  ? 44.259  37.426  -1.684  1.00 72.20  ? 75  GLN A CA  1 
ATOM   608   C C   . GLN A 1 75  ? 42.777  37.074  -1.913  1.00 71.72  ? 75  GLN A C   1 
ATOM   609   O O   . GLN A 1 75  ? 42.480  36.040  -2.528  1.00 70.42  ? 75  GLN A O   1 
ATOM   610   C CB  . GLN A 1 75  ? 44.764  36.992  -0.308  1.00 71.17  ? 75  GLN A CB  1 
ATOM   611   C CG  . GLN A 1 75  ? 46.279  36.899  -0.192  1.00 71.88  ? 75  GLN A CG  1 
ATOM   612   C CD  . GLN A 1 75  ? 46.677  36.433  1.188   1.00 71.69  ? 75  GLN A CD  1 
ATOM   613   O OE1 . GLN A 1 75  ? 46.153  36.970  2.165   1.00 72.81  ? 75  GLN A OE1 1 
ATOM   614   N NE2 . GLN A 1 75  ? 47.543  35.428  1.297   1.00 70.90  ? 75  GLN A NE2 1 
ATOM   615   N N   . LEU A 1 76  ? 41.861  37.924  -1.401  1.00 72.02  ? 76  LEU A N   1 
ATOM   616   C CA  . LEU A 1 76  ? 40.426  37.709  -1.537  1.00 71.67  ? 76  LEU A CA  1 
ATOM   617   C C   . LEU A 1 76  ? 40.088  37.670  -3.017  1.00 72.90  ? 76  LEU A C   1 
ATOM   618   O O   . LEU A 1 76  ? 39.334  36.808  -3.463  1.00 72.48  ? 76  LEU A O   1 
ATOM   619   C CB  . LEU A 1 76  ? 39.596  38.791  -0.845  1.00 71.68  ? 76  LEU A CB  1 
ATOM   620   C CG  . LEU A 1 76  ? 39.423  38.628  0.666   1.00 70.77  ? 76  LEU A CG  1 
ATOM   621   C CD1 . LEU A 1 76  ? 38.588  39.729  1.289   1.00 71.02  ? 76  LEU A CD1 1 
ATOM   622   C CD2 . LEU A 1 76  ? 38.819  37.272  0.941   1.00 69.27  ? 76  LEU A CD2 1 
ATOM   623   N N   . LYS A 1 77  ? 40.693  38.607  -3.755  1.00 74.97  ? 77  LYS A N   1 
ATOM   624   C CA  . LYS A 1 77  ? 40.371  38.815  -5.155  1.00 76.43  ? 77  LYS A CA  1 
ATOM   625   C C   . LYS A 1 77  ? 40.594  37.508  -5.897  1.00 75.30  ? 77  LYS A C   1 
ATOM   626   O O   . LYS A 1 77  ? 39.799  37.168  -6.762  1.00 75.19  ? 77  LYS A O   1 
ATOM   627   C CB  . LYS A 1 77  ? 41.173  39.956  -5.806  1.00 78.46  ? 77  LYS A CB  1 
ATOM   628   C CG  . LYS A 1 77  ? 40.684  41.383  -5.536  1.00 79.27  ? 77  LYS A CG  1 
ATOM   629   C CD  . LYS A 1 77  ? 41.653  42.431  -6.092  1.00 81.98  ? 77  LYS A CD  1 
ATOM   630   C CE  . LYS A 1 77  ? 41.340  43.873  -5.776  1.00 83.00  ? 77  LYS A CE  1 
ATOM   631   N NZ  . LYS A 1 77  ? 42.478  44.746  -6.095  1.00 84.65  ? 77  LYS A NZ  1 
ATOM   632   N N   . LEU A 1 78  ? 41.659  36.789  -5.519  1.00 74.75  ? 78  LEU A N   1 
ATOM   633   C CA  . LEU A 1 78  ? 42.065  35.573  -6.204  1.00 74.74  ? 78  LEU A CA  1 
ATOM   634   C C   . LEU A 1 78  ? 41.107  34.430  -5.876  1.00 73.24  ? 78  LEU A C   1 
ATOM   635   O O   . LEU A 1 78  ? 40.914  33.515  -6.681  1.00 71.36  ? 78  LEU A O   1 
ATOM   636   C CB  . LEU A 1 78  ? 43.482  35.233  -5.759  1.00 75.47  ? 78  LEU A CB  1 
ATOM   637   C CG  . LEU A 1 78  ? 44.101  34.007  -6.431  1.00 77.02  ? 78  LEU A CG  1 
ATOM   638   C CD1 . LEU A 1 78  ? 44.189  34.184  -7.935  1.00 79.11  ? 78  LEU A CD1 1 
ATOM   639   C CD2 . LEU A 1 78  ? 45.470  33.725  -5.850  1.00 78.20  ? 78  LEU A CD2 1 
ATOM   640   N N   . VAL A 1 79  ? 40.585  34.471  -4.648  1.00 72.54  ? 79  VAL A N   1 
ATOM   641   C CA  . VAL A 1 79  ? 39.549  33.550  -4.234  1.00 72.65  ? 79  VAL A CA  1 
ATOM   642   C C   . VAL A 1 79  ? 38.291  33.864  -5.035  1.00 71.67  ? 79  VAL A C   1 
ATOM   643   O O   . VAL A 1 79  ? 37.878  33.053  -5.856  1.00 69.68  ? 79  VAL A O   1 
ATOM   644   C CB  . VAL A 1 79  ? 39.309  33.607  -2.712  1.00 72.77  ? 79  VAL A CB  1 
ATOM   645   C CG1 . VAL A 1 79  ? 38.079  32.783  -2.295  1.00 70.28  ? 79  VAL A CG1 1 
ATOM   646   C CG2 . VAL A 1 79  ? 40.590  33.190  -1.966  1.00 72.23  ? 79  VAL A CG2 1 
ATOM   647   N N   . GLN A 1 80  ? 37.747  35.069  -4.823  1.00 72.42  ? 80  GLN A N   1 
ATOM   648   C CA  . GLN A 1 80  ? 36.562  35.544  -5.519  1.00 72.27  ? 80  GLN A CA  1 
ATOM   649   C C   . GLN A 1 80  ? 36.583  35.068  -6.965  1.00 72.98  ? 80  GLN A C   1 
ATOM   650   O O   . GLN A 1 80  ? 35.582  34.566  -7.452  1.00 74.03  ? 80  GLN A O   1 
ATOM   651   C CB  . GLN A 1 80  ? 36.572  37.066  -5.525  1.00 74.27  ? 80  GLN A CB  1 
ATOM   652   C CG  . GLN A 1 80  ? 35.261  37.728  -5.937  1.00 75.12  ? 80  GLN A CG  1 
ATOM   653   C CD  . GLN A 1 80  ? 34.169  37.465  -4.928  1.00 74.68  ? 80  GLN A CD  1 
ATOM   654   O OE1 . GLN A 1 80  ? 34.423  37.372  -3.719  1.00 74.19  ? 80  GLN A OE1 1 
ATOM   655   N NE2 . GLN A 1 80  ? 32.957  37.263  -5.428  1.00 74.63  ? 80  GLN A NE2 1 
ATOM   656   N N   . GLU A 1 81  ? 37.737  35.175  -7.630  1.00 74.01  ? 81  GLU A N   1 
ATOM   657   C CA  . GLU A 1 81  ? 37.839  34.863  -9.048  1.00 75.39  ? 81  GLU A CA  1 
ATOM   658   C C   . GLU A 1 81  ? 37.785  33.360  -9.281  1.00 72.26  ? 81  GLU A C   1 
ATOM   659   O O   . GLU A 1 81  ? 37.402  32.923  -10.359 1.00 71.72  ? 81  GLU A O   1 
ATOM   660   C CB  . GLU A 1 81  ? 39.139  35.366  -9.674  1.00 79.09  ? 81  GLU A CB  1 
ATOM   661   C CG  . GLU A 1 81  ? 39.226  36.887  -9.809  1.00 83.30  ? 81  GLU A CG  1 
ATOM   662   C CD  . GLU A 1 81  ? 40.660  37.429  -9.756  1.00 89.39  ? 81  GLU A CD  1 
ATOM   663   O OE1 . GLU A 1 81  ? 41.601  36.569  -9.706  1.00 87.35  ? 81  GLU A OE1 1 
ATOM   664   O OE2 . GLU A 1 81  ? 40.859  38.698  -9.757  1.00 95.85  ? 81  GLU A OE2 1 
ATOM   665   N N   . SER A 1 82  ? 38.187  32.582  -8.275  1.00 70.13  ? 82  SER A N   1 
ATOM   666   C CA  . SER A 1 82  ? 38.438  31.160  -8.463  1.00 69.53  ? 82  SER A CA  1 
ATOM   667   C C   . SER A 1 82  ? 37.149  30.395  -8.732  1.00 69.40  ? 82  SER A C   1 
ATOM   668   O O   . SER A 1 82  ? 37.156  29.376  -9.423  1.00 70.13  ? 82  SER A O   1 
ATOM   669   C CB  . SER A 1 82  ? 39.171  30.538  -7.279  1.00 68.37  ? 82  SER A CB  1 
ATOM   670   O OG  . SER A 1 82  ? 38.477  30.686  -6.045  1.00 66.85  ? 82  SER A OG  1 
ATOM   671   N N   . GLY A 1 83  ? 36.060  30.873  -8.135  1.00 68.86  ? 83  GLY A N   1 
ATOM   672   C CA  . GLY A 1 83  ? 34.853  30.096  -8.042  1.00 67.97  ? 83  GLY A CA  1 
ATOM   673   C C   . GLY A 1 83  ? 34.628  29.643  -6.608  1.00 67.15  ? 83  GLY A C   1 
ATOM   674   O O   . GLY A 1 83  ? 33.521  29.211  -6.289  1.00 68.37  ? 83  GLY A O   1 
ATOM   675   N N   . LEU A 1 84  ? 35.641  29.746  -5.740  1.00 66.19  ? 84  LEU A N   1 
ATOM   676   C CA  . LEU A 1 84  ? 35.539  29.058  -4.459  1.00 66.34  ? 84  LEU A CA  1 
ATOM   677   C C   . LEU A 1 84  ? 34.933  29.970  -3.402  1.00 67.54  ? 84  LEU A C   1 
ATOM   678   O O   . LEU A 1 84  ? 35.135  31.178  -3.434  1.00 69.30  ? 84  LEU A O   1 
ATOM   679   C CB  . LEU A 1 84  ? 36.839  28.461  -3.931  1.00 65.98  ? 84  LEU A CB  1 
ATOM   680   C CG  . LEU A 1 84  ? 37.363  27.233  -4.668  1.00 65.72  ? 84  LEU A CG  1 
ATOM   681   C CD1 . LEU A 1 84  ? 38.799  26.984  -4.276  1.00 65.98  ? 84  LEU A CD1 1 
ATOM   682   C CD2 . LEU A 1 84  ? 36.481  26.058  -4.338  1.00 65.05  ? 84  LEU A CD2 1 
ATOM   683   N N   . LYS A 1 85  ? 34.187  29.341  -2.477  1.00 68.63  ? 85  LYS A N   1 
ATOM   684   C CA  . LYS A 1 85  ? 33.625  30.005  -1.309  1.00 68.76  ? 85  LYS A CA  1 
ATOM   685   C C   . LYS A 1 85  ? 34.680  30.030  -0.197  1.00 66.94  ? 85  LYS A C   1 
ATOM   686   O O   . LYS A 1 85  ? 35.575  29.185  -0.154  1.00 66.43  ? 85  LYS A O   1 
ATOM   687   C CB  . LYS A 1 85  ? 32.318  29.304  -0.895  1.00 68.21  ? 85  LYS A CB  1 
ATOM   688   C CG  . LYS A 1 85  ? 31.200  29.350  -1.936  1.00 69.41  ? 85  LYS A CG  1 
ATOM   689   C CD  . LYS A 1 85  ? 30.938  30.753  -2.470  1.00 71.07  ? 85  LYS A CD  1 
ATOM   690   C CE  . LYS A 1 85  ? 29.675  30.940  -3.262  1.00 72.39  ? 85  LYS A CE  1 
ATOM   691   N NZ  . LYS A 1 85  ? 29.804  30.649  -4.694  1.00 72.84  ? 85  LYS A NZ  1 
ATOM   692   N N   . LEU A 1 86  ? 34.523  30.964  0.744   1.00 65.08  ? 86  LEU A N   1 
ATOM   693   C CA  . LEU A 1 86  ? 35.490  31.115  1.809   1.00 64.51  ? 86  LEU A CA  1 
ATOM   694   C C   . LEU A 1 86  ? 34.782  31.084  3.156   1.00 63.77  ? 86  LEU A C   1 
ATOM   695   O O   . LEU A 1 86  ? 33.775  31.766  3.339   1.00 65.09  ? 86  LEU A O   1 
ATOM   696   C CB  . LEU A 1 86  ? 36.163  32.459  1.544   1.00 65.63  ? 86  LEU A CB  1 
ATOM   697   C CG  . LEU A 1 86  ? 37.582  32.659  2.078   1.00 65.75  ? 86  LEU A CG  1 
ATOM   698   C CD1 . LEU A 1 86  ? 38.010  34.049  1.697   1.00 66.49  ? 86  LEU A CD1 1 
ATOM   699   C CD2 . LEU A 1 86  ? 37.698  32.456  3.572   1.00 65.48  ? 86  LEU A CD2 1 
ATOM   700   N N   . ILE A 1 87  ? 35.319  30.280  4.074   1.00 62.87  ? 87  ILE A N   1 
ATOM   701   C CA  . ILE A 1 87  ? 35.062  30.442  5.493   1.00 63.76  ? 87  ILE A CA  1 
ATOM   702   C C   . ILE A 1 87  ? 36.295  31.103  6.108   1.00 66.99  ? 87  ILE A C   1 
ATOM   703   O O   . ILE A 1 87  ? 37.370  30.517  6.154   1.00 72.86  ? 87  ILE A O   1 
ATOM   704   C CB  . ILE A 1 87  ? 34.723  29.087  6.145   1.00 62.25  ? 87  ILE A CB  1 
ATOM   705   C CG1 . ILE A 1 87  ? 33.371  28.523  5.631   1.00 61.61  ? 87  ILE A CG1 1 
ATOM   706   C CG2 . ILE A 1 87  ? 34.717  29.191  7.670   1.00 61.95  ? 87  ILE A CG2 1 
ATOM   707   C CD1 . ILE A 1 87  ? 33.121  27.053  5.952   1.00 60.29  ? 87  ILE A CD1 1 
ATOM   708   N N   . MET A 1 88  ? 36.182  32.353  6.546   1.00 68.39  ? 88  MET A N   1 
ATOM   709   C CA  . MET A 1 88  ? 37.369  33.122  6.868   1.00 68.88  ? 88  MET A CA  1 
ATOM   710   C C   . MET A 1 88  ? 37.541  33.202  8.381   1.00 68.90  ? 88  MET A C   1 
ATOM   711   O O   . MET A 1 88  ? 36.720  33.804  9.062   1.00 69.40  ? 88  MET A O   1 
ATOM   712   C CB  . MET A 1 88  ? 37.303  34.540  6.293   1.00 70.63  ? 88  MET A CB  1 
ATOM   713   C CG  . MET A 1 88  ? 38.565  35.338  6.577   1.00 74.66  ? 88  MET A CG  1 
ATOM   714   S SD  . MET A 1 88  ? 38.659  36.945  5.765   1.00 80.01  ? 88  MET A SD  1 
ATOM   715   C CE  . MET A 1 88  ? 39.002  36.270  4.136   1.00 77.71  ? 88  MET A CE  1 
ATOM   716   N N   . GLY A 1 89  ? 38.662  32.666  8.885   1.00 68.46  ? 89  GLY A N   1 
ATOM   717   C CA  . GLY A 1 89  ? 39.044  32.810  10.282  1.00 68.08  ? 89  GLY A CA  1 
ATOM   718   C C   . GLY A 1 89  ? 39.718  34.151  10.546  1.00 69.26  ? 89  GLY A C   1 
ATOM   719   O O   . GLY A 1 89  ? 40.387  34.689  9.659   1.00 71.06  ? 89  GLY A O   1 
ATOM   720   N N   . ILE A 1 90  ? 39.489  34.687  11.759  1.00 69.06  ? 90  ILE A N   1 
ATOM   721   C CA  . ILE A 1 90  ? 40.090  35.936  12.210  1.00 69.78  ? 90  ILE A CA  1 
ATOM   722   C C   . ILE A 1 90  ? 41.089  35.599  13.322  1.00 70.13  ? 90  ILE A C   1 
ATOM   723   O O   . ILE A 1 90  ? 40.745  35.026  14.348  1.00 69.14  ? 90  ILE A O   1 
ATOM   724   C CB  . ILE A 1 90  ? 39.025  36.967  12.663  1.00 69.47  ? 90  ILE A CB  1 
ATOM   725   C CG1 . ILE A 1 90  ? 37.884  37.140  11.641  1.00 68.74  ? 90  ILE A CG1 1 
ATOM   726   C CG2 . ILE A 1 90  ? 39.659  38.321  13.012  1.00 69.83  ? 90  ILE A CG2 1 
ATOM   727   C CD1 . ILE A 1 90  ? 38.252  37.922  10.393  1.00 69.73  ? 90  ILE A CD1 1 
ATOM   728   N N   . ASP A 1 91  ? 42.346  35.994  13.136  1.00 71.28  ? 91  ASP A N   1 
ATOM   729   C CA  . ASP A 1 91  ? 43.396  35.589  14.047  1.00 71.26  ? 91  ASP A CA  1 
ATOM   730   C C   . ASP A 1 91  ? 43.263  36.335  15.374  1.00 71.78  ? 91  ASP A C   1 
ATOM   731   O O   . ASP A 1 91  ? 43.893  37.372  15.585  1.00 72.30  ? 91  ASP A O   1 
ATOM   732   C CB  . ASP A 1 91  ? 44.732  35.753  13.355  1.00 72.40  ? 91  ASP A CB  1 
ATOM   733   C CG  . ASP A 1 91  ? 45.933  35.215  14.119  1.00 73.80  ? 91  ASP A CG  1 
ATOM   734   O OD1 . ASP A 1 91  ? 45.710  34.295  14.959  1.00 73.49  ? 91  ASP A OD1 1 
ATOM   735   O OD2 . ASP A 1 91  ? 47.062  35.768  13.898  1.00 74.38  ? 91  ASP A OD2 1 
ATOM   736   N N   . ILE A 1 92  ? 42.399  35.808  16.244  1.00 71.65  ? 92  ILE A N   1 
ATOM   737   C CA  . ILE A 1 92  ? 42.339  36.222  17.633  1.00 74.48  ? 92  ILE A CA  1 
ATOM   738   C C   . ILE A 1 92  ? 43.142  35.200  18.432  1.00 77.87  ? 92  ILE A C   1 
ATOM   739   O O   . ILE A 1 92  ? 42.734  34.050  18.614  1.00 82.30  ? 92  ILE A O   1 
ATOM   740   C CB  . ILE A 1 92  ? 40.876  36.361  18.115  1.00 74.59  ? 92  ILE A CB  1 
ATOM   741   C CG1 . ILE A 1 92  ? 40.260  37.716  17.741  1.00 73.63  ? 92  ILE A CG1 1 
ATOM   742   C CG2 . ILE A 1 92  ? 40.745  36.134  19.623  1.00 75.85  ? 92  ILE A CG2 1 
ATOM   743   C CD1 . ILE A 1 92  ? 40.039  37.897  16.254  1.00 72.75  ? 92  ILE A CD1 1 
ATOM   744   N N   . LYS A 1 93  ? 44.323  35.606  18.885  1.00 82.21  ? 93  LYS A N   1 
ATOM   745   C CA  . LYS A 1 93  ? 45.209  34.694  19.599  1.00 83.50  ? 93  LYS A CA  1 
ATOM   746   C C   . LYS A 1 93  ? 44.416  34.062  20.736  1.00 82.14  ? 93  LYS A C   1 
ATOM   747   O O   . LYS A 1 93  ? 43.841  34.754  21.574  1.00 85.90  ? 93  LYS A O   1 
ATOM   748   C CB  . LYS A 1 93  ? 46.472  35.373  20.159  1.00 85.21  ? 93  LYS A CB  1 
ATOM   749   C CG  . LYS A 1 93  ? 47.776  35.176  19.390  1.00 85.85  ? 93  LYS A CG  1 
ATOM   750   C CD  . LYS A 1 93  ? 47.802  35.667  17.950  1.00 86.83  ? 93  LYS A CD  1 
ATOM   751   C CE  . LYS A 1 93  ? 48.898  34.991  17.186  1.00 91.82  ? 93  LYS A CE  1 
ATOM   752   N NZ  . LYS A 1 93  ? 49.176  35.648  15.905  1.00 95.60  ? 93  LYS A NZ  1 
ATOM   753   N N   . PRO A 1 94  ? 44.339  32.730  20.805  1.00 77.92  ? 94  PRO A N   1 
ATOM   754   C CA  . PRO A 1 94  ? 43.549  32.103  21.854  1.00 77.19  ? 94  PRO A CA  1 
ATOM   755   C C   . PRO A 1 94  ? 44.104  32.334  23.252  1.00 77.93  ? 94  PRO A C   1 
ATOM   756   O O   . PRO A 1 94  ? 43.397  32.090  24.220  1.00 77.46  ? 94  PRO A O   1 
ATOM   757   C CB  . PRO A 1 94  ? 43.550  30.630  21.490  1.00 76.46  ? 94  PRO A CB  1 
ATOM   758   C CG  . PRO A 1 94  ? 44.024  30.594  20.052  1.00 76.71  ? 94  PRO A CG  1 
ATOM   759   C CD  . PRO A 1 94  ? 44.946  31.787  19.870  1.00 77.26  ? 94  PRO A CD  1 
ATOM   760   N N   . GLU A 1 95  ? 45.353  32.796  23.369  1.00 78.86  ? 95  GLU A N   1 
ATOM   761   C CA  . GLU A 1 95  ? 46.005  32.770  24.666  1.00 82.63  ? 95  GLU A CA  1 
ATOM   762   C C   . GLU A 1 95  ? 46.017  34.143  25.324  1.00 84.79  ? 95  GLU A C   1 
ATOM   763   O O   . GLU A 1 95  ? 46.517  34.254  26.440  1.00 86.91  ? 95  GLU A O   1 
ATOM   764   C CB  . GLU A 1 95  ? 47.442  32.277  24.580  1.00 87.33  ? 95  GLU A CB  1 
ATOM   765   C CG  . GLU A 1 95  ? 47.602  31.004  23.750  1.00 91.62  ? 95  GLU A CG  1 
ATOM   766   C CD  . GLU A 1 95  ? 47.853  31.248  22.261  1.00 96.31  ? 95  GLU A CD  1 
ATOM   767   O OE1 . GLU A 1 95  ? 47.878  32.454  21.811  1.00 91.94  ? 95  GLU A OE1 1 
ATOM   768   O OE2 . GLU A 1 95  ? 48.031  30.188  21.568  1.00 95.93  ? 95  GLU A OE2 1 
ATOM   769   N N   . GLU A 1 96  ? 45.464  35.161  24.636  1.00 83.87  ? 96  GLU A N   1 
ATOM   770   C CA  . GLU A 1 96  ? 45.412  36.534  25.123  1.00 82.66  ? 96  GLU A CA  1 
ATOM   771   C C   . GLU A 1 96  ? 44.311  36.691  26.171  1.00 81.92  ? 96  GLU A C   1 
ATOM   772   O O   . GLU A 1 96  ? 43.392  35.864  26.246  1.00 82.02  ? 96  GLU A O   1 
ATOM   773   C CB  . GLU A 1 96  ? 45.157  37.489  23.956  1.00 82.67  ? 96  GLU A CB  1 
ATOM   774   C CG  . GLU A 1 96  ? 46.397  37.774  23.107  1.00 83.70  ? 96  GLU A CG  1 
ATOM   775   C CD  . GLU A 1 96  ? 47.619  38.295  23.854  1.00 84.96  ? 96  GLU A CD  1 
ATOM   776   O OE1 . GLU A 1 96  ? 47.500  39.332  24.540  1.00 83.00  ? 96  GLU A OE1 1 
ATOM   777   O OE2 . GLU A 1 96  ? 48.692  37.626  23.785  1.00 88.51  ? 96  GLU A OE2 1 
ATOM   778   N N   . ASP A 1 97  ? 44.421  37.735  27.008  1.00 80.08  ? 97  ASP A N   1 
ATOM   779   C CA  . ASP A 1 97  ? 43.400  37.962  28.015  1.00 79.18  ? 97  ASP A CA  1 
ATOM   780   C C   . ASP A 1 97  ? 42.239  38.640  27.319  1.00 78.60  ? 97  ASP A C   1 
ATOM   781   O O   . ASP A 1 97  ? 42.306  39.823  27.019  1.00 82.31  ? 97  ASP A O   1 
ATOM   782   C CB  . ASP A 1 97  ? 43.871  38.753  29.226  1.00 80.03  ? 97  ASP A CB  1 
ATOM   783   C CG  . ASP A 1 97  ? 42.746  39.254  30.129  1.00 80.92  ? 97  ASP A CG  1 
ATOM   784   O OD1 . ASP A 1 97  ? 41.623  38.700  30.036  1.00 79.51  ? 97  ASP A OD1 1 
ATOM   785   O OD2 . ASP A 1 97  ? 42.972  40.240  30.881  1.00 82.84  ? 97  ASP A OD2 1 
ATOM   786   N N   . TYR A 1 98  ? 41.165  37.892  27.106  1.00 77.04  ? 98  TYR A N   1 
ATOM   787   C CA  . TYR A 1 98  ? 40.008  38.386  26.384  1.00 76.45  ? 98  TYR A CA  1 
ATOM   788   C C   . TYR A 1 98  ? 39.418  39.589  27.115  1.00 77.97  ? 98  TYR A C   1 
ATOM   789   O O   . TYR A 1 98  ? 38.674  40.352  26.516  1.00 77.77  ? 98  TYR A O   1 
ATOM   790   C CB  . TYR A 1 98  ? 38.973  37.262  26.264  1.00 75.78  ? 98  TYR A CB  1 
ATOM   791   C CG  . TYR A 1 98  ? 39.463  35.922  25.725  1.00 75.30  ? 98  TYR A CG  1 
ATOM   792   C CD1 . TYR A 1 98  ? 40.320  35.848  24.630  1.00 75.74  ? 98  TYR A CD1 1 
ATOM   793   C CD2 . TYR A 1 98  ? 39.091  34.726  26.325  1.00 75.40  ? 98  TYR A CD2 1 
ATOM   794   C CE1 . TYR A 1 98  ? 40.808  34.638  24.156  1.00 74.52  ? 98  TYR A CE1 1 
ATOM   795   C CE2 . TYR A 1 98  ? 39.555  33.508  25.851  1.00 75.05  ? 98  TYR A CE2 1 
ATOM   796   C CZ  . TYR A 1 98  ? 40.414  33.470  24.769  1.00 74.27  ? 98  TYR A CZ  1 
ATOM   797   O OH  . TYR A 1 98  ? 40.866  32.301  24.277  1.00 73.77  ? 98  TYR A OH  1 
ATOM   798   N N   . GLY A 1 99  ? 39.731  39.721  28.413  1.00 80.14  ? 99  GLY A N   1 
ATOM   799   C CA  . GLY A 1 99  ? 39.202  40.774  29.263  1.00 81.58  ? 99  GLY A CA  1 
ATOM   800   C C   . GLY A 1 99  ? 40.102  42.006  29.289  1.00 84.76  ? 99  GLY A C   1 
ATOM   801   O O   . GLY A 1 99  ? 39.748  43.028  29.882  1.00 88.12  ? 99  GLY A O   1 
ATOM   802   N N   . ASP A 1 100 ? 41.270  41.935  28.638  1.00 86.21  ? 100 ASP A N   1 
ATOM   803   C CA  . ASP A 1 100 ? 42.198  43.062  28.636  1.00 86.70  ? 100 ASP A CA  1 
ATOM   804   C C   . ASP A 1 100 ? 41.764  44.133  27.628  1.00 84.40  ? 100 ASP A C   1 
ATOM   805   O O   . ASP A 1 100 ? 41.877  43.950  26.416  1.00 82.38  ? 100 ASP A O   1 
ATOM   806   C CB  . ASP A 1 100 ? 43.628  42.608  28.416  1.00 87.89  ? 100 ASP A CB  1 
ATOM   807   C CG  . ASP A 1 100 ? 44.598  43.754  28.182  1.00 91.45  ? 100 ASP A CG  1 
ATOM   808   O OD1 . ASP A 1 100 ? 44.537  44.745  28.940  1.00 93.69  ? 100 ASP A OD1 1 
ATOM   809   O OD2 . ASP A 1 100 ? 45.399  43.655  27.238  1.00 94.32  ? 100 ASP A OD2 1 
ATOM   810   N N   . PRO A 1 101 ? 41.319  45.316  28.103  1.00 84.16  ? 101 PRO A N   1 
ATOM   811   C CA  . PRO A 1 101 ? 40.827  46.385  27.219  1.00 84.00  ? 101 PRO A CA  1 
ATOM   812   C C   . PRO A 1 101 ? 41.633  46.700  25.958  1.00 83.97  ? 101 PRO A C   1 
ATOM   813   O O   . PRO A 1 101 ? 41.067  47.055  24.925  1.00 81.80  ? 101 PRO A O   1 
ATOM   814   C CB  . PRO A 1 101 ? 40.844  47.592  28.157  1.00 85.20  ? 101 PRO A CB  1 
ATOM   815   C CG  . PRO A 1 101 ? 40.595  47.016  29.526  1.00 85.91  ? 101 PRO A CG  1 
ATOM   816   C CD  . PRO A 1 101 ? 41.319  45.689  29.525  1.00 85.20  ? 101 PRO A CD  1 
ATOM   817   N N   . GLU A 1 102 ? 42.965  46.588  26.075  1.00 86.22  ? 102 GLU A N   1 
ATOM   818   C CA  . GLU A 1 102 ? 43.890  46.919  25.000  1.00 88.11  ? 102 GLU A CA  1 
ATOM   819   C C   . GLU A 1 102 ? 43.716  45.917  23.862  1.00 84.98  ? 102 GLU A C   1 
ATOM   820   O O   . GLU A 1 102 ? 43.645  46.301  22.689  1.00 82.56  ? 102 GLU A O   1 
ATOM   821   C CB  . GLU A 1 102 ? 45.313  46.957  25.559  1.00 93.54  ? 102 GLU A CB  1 
ATOM   822   C CG  . GLU A 1 102 ? 46.210  48.006  24.900  1.00 100.74 ? 102 GLU A CG  1 
ATOM   823   C CD  . GLU A 1 102 ? 47.657  48.121  25.397  1.00 108.39 ? 102 GLU A CD  1 
ATOM   824   O OE1 . GLU A 1 102 ? 48.134  47.426  26.335  1.00 111.66 ? 102 GLU A OE1 1 
ATOM   825   O OE2 . GLU A 1 102 ? 48.357  48.949  24.783  1.00 113.41 ? 102 GLU A OE2 1 
ATOM   826   N N   . PHE A 1 103 ? 43.605  44.633  24.257  1.00 83.74  ? 103 PHE A N   1 
ATOM   827   C CA  . PHE A 1 103 ? 43.458  43.520  23.342  1.00 80.92  ? 103 PHE A CA  1 
ATOM   828   C C   . PHE A 1 103 ? 42.121  43.593  22.630  1.00 79.70  ? 103 PHE A C   1 
ATOM   829   O O   . PHE A 1 103 ? 42.050  43.235  21.457  1.00 79.52  ? 103 PHE A O   1 
ATOM   830   C CB  . PHE A 1 103 ? 43.452  42.140  24.001  1.00 81.22  ? 103 PHE A CB  1 
ATOM   831   C CG  . PHE A 1 103 ? 43.316  40.998  22.997  1.00 79.57  ? 103 PHE A CG  1 
ATOM   832   C CD1 . PHE A 1 103 ? 44.087  40.964  21.839  1.00 79.60  ? 103 PHE A CD1 1 
ATOM   833   C CD2 . PHE A 1 103 ? 42.391  39.994  23.192  1.00 79.08  ? 103 PHE A CD2 1 
ATOM   834   C CE1 . PHE A 1 103 ? 43.951  39.952  20.915  1.00 78.43  ? 103 PHE A CE1 1 
ATOM   835   C CE2 . PHE A 1 103 ? 42.271  38.970  22.270  1.00 79.18  ? 103 PHE A CE2 1 
ATOM   836   C CZ  . PHE A 1 103 ? 43.066  38.945  21.142  1.00 78.88  ? 103 PHE A CZ  1 
ATOM   837   N N   . VAL A 1 104 ? 41.072  43.996  23.366  1.00 79.25  ? 104 VAL A N   1 
ATOM   838   C CA  . VAL A 1 104 ? 39.749  44.180  22.788  1.00 77.53  ? 104 VAL A CA  1 
ATOM   839   C C   . VAL A 1 104 ? 39.836  45.256  21.711  1.00 77.47  ? 104 VAL A C   1 
ATOM   840   O O   . VAL A 1 104 ? 39.325  45.082  20.611  1.00 75.39  ? 104 VAL A O   1 
ATOM   841   C CB  . VAL A 1 104 ? 38.690  44.544  23.846  1.00 77.79  ? 104 VAL A CB  1 
ATOM   842   C CG1 . VAL A 1 104 ? 37.323  44.838  23.227  1.00 76.97  ? 104 VAL A CG1 1 
ATOM   843   C CG2 . VAL A 1 104 ? 38.571  43.459  24.906  1.00 77.43  ? 104 VAL A CG2 1 
ATOM   844   N N   . LYS A 1 105 ? 40.513  46.360  22.034  1.00 79.93  ? 105 LYS A N   1 
ATOM   845   C CA  . LYS A 1 105 ? 40.535  47.523  21.160  1.00 82.11  ? 105 LYS A CA  1 
ATOM   846   C C   . LYS A 1 105 ? 41.282  47.156  19.872  1.00 81.99  ? 105 LYS A C   1 
ATOM   847   O O   . LYS A 1 105 ? 40.754  47.316  18.768  1.00 81.21  ? 105 LYS A O   1 
ATOM   848   C CB  . LYS A 1 105 ? 41.073  48.680  22.017  1.00 84.39  ? 105 LYS A CB  1 
ATOM   849   C CG  . LYS A 1 105 ? 41.191  50.086  21.401  1.00 85.86  ? 105 LYS A CG  1 
ATOM   850   C CD  . LYS A 1 105 ? 39.931  50.655  20.755  1.00 86.15  ? 105 LYS A CD  1 
ATOM   851   C CE  . LYS A 1 105 ? 38.792  51.096  21.646  1.00 86.07  ? 105 LYS A CE  1 
ATOM   852   N NZ  . LYS A 1 105 ? 37.546  51.197  20.868  1.00 84.62  ? 105 LYS A NZ  1 
ATOM   853   N N   . ASP A 1 106 ? 42.492  46.609  20.021  1.00 82.40  ? 106 ASP A N   1 
ATOM   854   C CA  . ASP A 1 106 ? 43.229  46.066  18.887  1.00 82.73  ? 106 ASP A CA  1 
ATOM   855   C C   . ASP A 1 106 ? 42.392  45.080  18.060  1.00 81.77  ? 106 ASP A C   1 
ATOM   856   O O   . ASP A 1 106 ? 42.536  44.997  16.840  1.00 85.31  ? 106 ASP A O   1 
ATOM   857   C CB  . ASP A 1 106 ? 44.513  45.414  19.354  1.00 82.46  ? 106 ASP A CB  1 
ATOM   858   C CG  . ASP A 1 106 ? 45.438  46.412  20.021  1.00 85.29  ? 106 ASP A CG  1 
ATOM   859   O OD1 . ASP A 1 106 ? 45.379  47.576  19.614  1.00 86.26  ? 106 ASP A OD1 1 
ATOM   860   O OD2 . ASP A 1 106 ? 46.210  46.025  20.917  1.00 86.34  ? 106 ASP A OD2 1 
ATOM   861   N N   . SER A 1 107 ? 41.526  44.295  18.695  1.00 77.41  ? 107 SER A N   1 
ATOM   862   C CA  . SER A 1 107 ? 40.790  43.317  17.928  1.00 74.82  ? 107 SER A CA  1 
ATOM   863   C C   . SER A 1 107 ? 39.690  44.030  17.139  1.00 73.67  ? 107 SER A C   1 
ATOM   864   O O   . SER A 1 107 ? 39.587  43.875  15.919  1.00 72.65  ? 107 SER A O   1 
ATOM   865   C CB  . SER A 1 107 ? 40.307  42.219  18.841  1.00 74.32  ? 107 SER A CB  1 
ATOM   866   O OG  . SER A 1 107 ? 41.430  41.668  19.529  1.00 74.72  ? 107 SER A OG  1 
ATOM   867   N N   . GLU A 1 108 ? 38.914  44.872  17.840  1.00 73.01  ? 108 GLU A N   1 
ATOM   868   C CA  . GLU A 1 108 ? 37.918  45.726  17.211  1.00 72.00  ? 108 GLU A CA  1 
ATOM   869   C C   . GLU A 1 108 ? 38.546  46.422  15.995  1.00 71.77  ? 108 GLU A C   1 
ATOM   870   O O   . GLU A 1 108 ? 37.963  46.369  14.913  1.00 70.59  ? 108 GLU A O   1 
ATOM   871   C CB  . GLU A 1 108 ? 37.331  46.745  18.193  1.00 73.23  ? 108 GLU A CB  1 
ATOM   872   C CG  . GLU A 1 108 ? 36.584  46.199  19.411  1.00 73.18  ? 108 GLU A CG  1 
ATOM   873   C CD  . GLU A 1 108 ? 36.159  47.240  20.463  1.00 75.61  ? 108 GLU A CD  1 
ATOM   874   O OE1 . GLU A 1 108 ? 36.618  48.413  20.505  1.00 77.15  ? 108 GLU A OE1 1 
ATOM   875   O OE2 . GLU A 1 108 ? 35.323  46.869  21.310  1.00 76.50  ? 108 GLU A OE2 1 
ATOM   876   N N   . ILE A 1 109 ? 39.742  47.043  16.157  1.00 72.30  ? 109 ILE A N   1 
ATOM   877   C CA  . ILE A 1 109 ? 40.364  47.803  15.074  1.00 72.75  ? 109 ILE A CA  1 
ATOM   878   C C   . ILE A 1 109 ? 40.832  46.868  13.954  1.00 72.07  ? 109 ILE A C   1 
ATOM   879   O O   . ILE A 1 109 ? 40.643  47.152  12.773  1.00 72.43  ? 109 ILE A O   1 
ATOM   880   C CB  . ILE A 1 109 ? 41.511  48.716  15.550  1.00 73.97  ? 109 ILE A CB  1 
ATOM   881   C CG1 . ILE A 1 109 ? 41.054  49.732  16.610  1.00 74.81  ? 109 ILE A CG1 1 
ATOM   882   C CG2 . ILE A 1 109 ? 42.144  49.453  14.361  1.00 74.56  ? 109 ILE A CG2 1 
ATOM   883   C CD1 . ILE A 1 109 ? 42.185  50.416  17.367  1.00 75.76  ? 109 ILE A CD1 1 
ATOM   884   N N   . GLU A 1 110 ? 41.438  45.731  14.293  1.00 71.50  ? 110 GLU A N   1 
ATOM   885   C CA  . GLU A 1 110 ? 41.899  44.822  13.254  1.00 70.43  ? 110 GLU A CA  1 
ATOM   886   C C   . GLU A 1 110 ? 40.709  44.333  12.419  1.00 69.29  ? 110 GLU A C   1 
ATOM   887   O O   . GLU A 1 110 ? 40.681  44.526  11.195  1.00 70.11  ? 110 GLU A O   1 
ATOM   888   C CB  . GLU A 1 110 ? 42.713  43.680  13.862  1.00 69.72  ? 110 GLU A CB  1 
ATOM   889   C CG  . GLU A 1 110 ? 43.324  42.770  12.801  1.00 69.19  ? 110 GLU A CG  1 
ATOM   890   C CD  . GLU A 1 110 ? 44.033  43.524  11.677  1.00 69.92  ? 110 GLU A CD  1 
ATOM   891   O OE1 . GLU A 1 110 ? 44.354  44.736  11.789  1.00 70.96  ? 110 GLU A OE1 1 
ATOM   892   O OE2 . GLU A 1 110 ? 44.249  42.864  10.639  1.00 68.98  ? 110 GLU A OE2 1 
ATOM   893   N N   . LEU A 1 111 ? 39.713  43.741  13.094  1.00 67.23  ? 111 LEU A N   1 
ATOM   894   C CA  . LEU A 1 111 ? 38.560  43.181  12.417  1.00 65.53  ? 111 LEU A CA  1 
ATOM   895   C C   . LEU A 1 111 ? 37.915  44.223  11.512  1.00 65.41  ? 111 LEU A C   1 
ATOM   896   O O   . LEU A 1 111 ? 37.590  43.908  10.366  1.00 65.13  ? 111 LEU A O   1 
ATOM   897   C CB  . LEU A 1 111 ? 37.581  42.679  13.476  1.00 65.13  ? 111 LEU A CB  1 
ATOM   898   C CG  . LEU A 1 111 ? 36.296  41.990  12.994  1.00 64.13  ? 111 LEU A CG  1 
ATOM   899   C CD1 . LEU A 1 111 ? 36.438  41.029  11.820  1.00 63.20  ? 111 LEU A CD1 1 
ATOM   900   C CD2 . LEU A 1 111 ? 35.766  41.253  14.204  1.00 63.63  ? 111 LEU A CD2 1 
ATOM   901   N N   . LYS A 1 112 ? 37.750  45.454  12.037  1.00 65.64  ? 112 LYS A N   1 
ATOM   902   C CA  . LYS A 1 112 ? 37.062  46.539  11.334  1.00 65.59  ? 112 LYS A CA  1 
ATOM   903   C C   . LYS A 1 112 ? 37.774  46.878  10.029  1.00 64.82  ? 112 LYS A C   1 
ATOM   904   O O   . LYS A 1 112 ? 37.110  47.221  9.046   1.00 62.78  ? 112 LYS A O   1 
ATOM   905   C CB  . LYS A 1 112 ? 36.885  47.810  12.170  1.00 67.06  ? 112 LYS A CB  1 
ATOM   906   C CG  . LYS A 1 112 ? 35.579  47.875  12.948  1.00 67.42  ? 112 LYS A CG  1 
ATOM   907   C CD  . LYS A 1 112 ? 35.572  48.924  14.050  1.00 69.03  ? 112 LYS A CD  1 
ATOM   908   C CE  . LYS A 1 112 ? 34.527  48.648  15.087  1.00 69.25  ? 112 LYS A CE  1 
ATOM   909   N NZ  . LYS A 1 112 ? 34.384  49.824  15.953  1.00 70.98  ? 112 LYS A NZ  1 
ATOM   910   N N   . ARG A 1 113 ? 39.109  46.711  10.033  1.00 64.20  ? 113 ARG A N   1 
ATOM   911   C CA  . ARG A 1 113 ? 39.924  47.023  8.873   1.00 64.34  ? 113 ARG A CA  1 
ATOM   912   C C   . ARG A 1 113 ? 39.700  45.947  7.824   1.00 63.93  ? 113 ARG A C   1 
ATOM   913   O O   . ARG A 1 113 ? 39.571  46.234  6.643   1.00 64.41  ? 113 ARG A O   1 
ATOM   914   C CB  . ARG A 1 113 ? 41.404  47.149  9.231   1.00 64.06  ? 113 ARG A CB  1 
ATOM   915   C CG  . ARG A 1 113 ? 42.293  47.507  8.047   1.00 64.96  ? 113 ARG A CG  1 
ATOM   916   C CD  . ARG A 1 113 ? 43.775  47.312  8.416   1.00 65.45  ? 113 ARG A CD  1 
ATOM   917   N NE  . ARG A 1 113 ? 44.111  45.943  8.823   1.00 64.27  ? 113 ARG A NE  1 
ATOM   918   C CZ  . ARG A 1 113 ? 44.354  44.964  7.969   1.00 63.62  ? 113 ARG A CZ  1 
ATOM   919   N NH1 . ARG A 1 113 ? 44.575  45.258  6.698   1.00 64.24  ? 113 ARG A NH1 1 
ATOM   920   N NH2 . ARG A 1 113 ? 44.455  43.700  8.376   1.00 62.49  ? 113 ARG A NH2 1 
ATOM   921   N N   . VAL A 1 114 ? 39.596  44.700  8.262   1.00 63.34  ? 114 VAL A N   1 
ATOM   922   C CA  . VAL A 1 114 ? 39.376  43.620  7.312   1.00 62.89  ? 114 VAL A CA  1 
ATOM   923   C C   . VAL A 1 114 ? 37.996  43.754  6.669   1.00 63.12  ? 114 VAL A C   1 
ATOM   924   O O   . VAL A 1 114 ? 37.832  43.632  5.452   1.00 63.37  ? 114 VAL A O   1 
ATOM   925   C CB  . VAL A 1 114 ? 39.521  42.300  8.051   1.00 61.74  ? 114 VAL A CB  1 
ATOM   926   C CG1 . VAL A 1 114 ? 39.399  41.159  7.068   1.00 61.11  ? 114 VAL A CG1 1 
ATOM   927   C CG2 . VAL A 1 114 ? 40.838  42.231  8.794   1.00 62.07  ? 114 VAL A CG2 1 
ATOM   928   N N   . LEU A 1 115 ? 37.001  44.040  7.504   1.00 63.37  ? 115 LEU A N   1 
ATOM   929   C CA  . LEU A 1 115 ? 35.629  44.021  7.047   1.00 63.55  ? 115 LEU A CA  1 
ATOM   930   C C   . LEU A 1 115 ? 35.446  45.109  6.004   1.00 65.21  ? 115 LEU A C   1 
ATOM   931   O O   . LEU A 1 115 ? 34.647  44.980  5.072   1.00 65.08  ? 115 LEU A O   1 
ATOM   932   C CB  . LEU A 1 115 ? 34.707  44.220  8.248   1.00 63.46  ? 115 LEU A CB  1 
ATOM   933   C CG  . LEU A 1 115 ? 34.645  43.054  9.239   1.00 62.36  ? 115 LEU A CG  1 
ATOM   934   C CD1 . LEU A 1 115 ? 33.885  43.463  10.493  1.00 62.57  ? 115 LEU A CD1 1 
ATOM   935   C CD2 . LEU A 1 115 ? 34.038  41.825  8.568   1.00 61.28  ? 115 LEU A CD2 1 
ATOM   936   N N   . ASN A 1 116 ? 36.208  46.193  6.194   1.00 66.97  ? 116 ASN A N   1 
ATOM   937   C CA  . ASN A 1 116 ? 36.047  47.388  5.388   1.00 68.41  ? 116 ASN A CA  1 
ATOM   938   C C   . ASN A 1 116 ? 36.274  47.097  3.903   1.00 68.77  ? 116 ASN A C   1 
ATOM   939   O O   . ASN A 1 116 ? 35.639  47.764  3.068   1.00 69.50  ? 116 ASN A O   1 
ATOM   940   C CB  . ASN A 1 116 ? 37.000  48.475  5.842   1.00 69.71  ? 116 ASN A CB  1 
ATOM   941   C CG  . ASN A 1 116 ? 36.641  49.768  5.172   1.00 71.27  ? 116 ASN A CG  1 
ATOM   942   O OD1 . ASN A 1 116 ? 37.504  50.541  4.775   1.00 72.04  ? 116 ASN A OD1 1 
ATOM   943   N ND2 . ASN A 1 116 ? 35.347  50.001  5.037   1.00 71.79  ? 116 ASN A ND2 1 
ATOM   944   N N   . TYR A 1 117 ? 37.177  46.114  3.608   1.00 68.02  ? 117 TYR A N   1 
ATOM   945   C CA  . TYR A 1 117 ? 37.380  45.590  2.256   1.00 67.87  ? 117 TYR A CA  1 
ATOM   946   C C   . TYR A 1 117 ? 36.698  44.220  2.033   1.00 66.78  ? 117 TYR A C   1 
ATOM   947   O O   . TYR A 1 117 ? 36.286  43.905  0.912   1.00 66.68  ? 117 TYR A O   1 
ATOM   948   C CB  . TYR A 1 117 ? 38.872  45.590  1.882   1.00 68.00  ? 117 TYR A CB  1 
ATOM   949   C CG  . TYR A 1 117 ? 39.810  44.612  2.587   1.00 66.92  ? 117 TYR A CG  1 
ATOM   950   C CD1 . TYR A 1 117 ? 39.737  43.239  2.360   1.00 65.59  ? 117 TYR A CD1 1 
ATOM   951   C CD2 . TYR A 1 117 ? 40.797  45.064  3.451   1.00 67.18  ? 117 TYR A CD2 1 
ATOM   952   C CE1 . TYR A 1 117 ? 40.590  42.361  2.993   1.00 64.83  ? 117 TYR A CE1 1 
ATOM   953   C CE2 . TYR A 1 117 ? 41.663  44.197  4.085   1.00 66.47  ? 117 TYR A CE2 1 
ATOM   954   C CZ  . TYR A 1 117 ? 41.570  42.840  3.845   1.00 65.40  ? 117 TYR A CZ  1 
ATOM   955   O OH  . TYR A 1 117 ? 42.444  41.969  4.450   1.00 64.84  ? 117 TYR A OH  1 
ATOM   956   N N   . ALA A 1 118 ? 36.571  43.376  3.058   1.00 65.98  ? 118 ALA A N   1 
ATOM   957   C CA  . ALA A 1 118 ? 36.060  42.030  2.821   1.00 65.57  ? 118 ALA A CA  1 
ATOM   958   C C   . ALA A 1 118 ? 34.564  42.022  2.474   1.00 66.23  ? 118 ALA A C   1 
ATOM   959   O O   . ALA A 1 118 ? 34.055  41.076  1.871   1.00 65.60  ? 118 ALA A O   1 
ATOM   960   C CB  . ALA A 1 118 ? 36.339  41.159  4.029   1.00 64.64  ? 118 ALA A CB  1 
ATOM   961   N N   . LYS A 1 119 ? 33.848  43.087  2.845   1.00 67.89  ? 119 LYS A N   1 
ATOM   962   C CA  . LYS A 1 119 ? 32.412  43.168  2.621   1.00 68.66  ? 119 LYS A CA  1 
ATOM   963   C C   . LYS A 1 119 ? 32.059  43.358  1.141   1.00 69.68  ? 119 LYS A C   1 
ATOM   964   O O   . LYS A 1 119 ? 30.873  43.379  0.800   1.00 70.08  ? 119 LYS A O   1 
ATOM   965   C CB  . LYS A 1 119 ? 31.787  44.319  3.419   1.00 69.75  ? 119 LYS A CB  1 
ATOM   966   C CG  . LYS A 1 119 ? 32.188  45.700  2.933   1.00 71.36  ? 119 LYS A CG  1 
ATOM   967   C CD  . LYS A 1 119 ? 31.729  46.828  3.839   1.00 72.43  ? 119 LYS A CD  1 
ATOM   968   C CE  . LYS A 1 119 ? 31.845  48.088  3.075   1.00 74.58  ? 119 LYS A CE  1 
ATOM   969   N NZ  . LYS A 1 119 ? 32.011  49.186  4.018   1.00 76.20  ? 119 LYS A NZ  1 
ATOM   970   N N   . LYS A 1 120 ? 33.072  43.488  0.271   1.00 70.23  ? 120 LYS A N   1 
ATOM   971   C CA  . LYS A 1 120 ? 32.845  43.567  -1.164  1.00 70.90  ? 120 LYS A CA  1 
ATOM   972   C C   . LYS A 1 120 ? 33.152  42.231  -1.853  1.00 70.02  ? 120 LYS A C   1 
ATOM   973   O O   . LYS A 1 120 ? 33.184  42.178  -3.083  1.00 70.46  ? 120 LYS A O   1 
ATOM   974   C CB  . LYS A 1 120 ? 33.716  44.667  -1.777  1.00 72.29  ? 120 LYS A CB  1 
ATOM   975   C CG  . LYS A 1 120 ? 33.831  45.943  -0.961  1.00 73.08  ? 120 LYS A CG  1 
ATOM   976   C CD  . LYS A 1 120 ? 34.643  47.042  -1.631  1.00 74.57  ? 120 LYS A CD  1 
ATOM   977   C CE  . LYS A 1 120 ? 36.072  46.634  -1.796  1.00 74.64  ? 120 LYS A CE  1 
ATOM   978   N NZ  . LYS A 1 120 ? 36.857  47.654  -2.490  1.00 76.25  ? 120 LYS A NZ  1 
ATOM   979   N N   . TYR A 1 121 ? 33.367  41.153  -1.082  1.00 68.75  ? 121 TYR A N   1 
ATOM   980   C CA  . TYR A 1 121 ? 33.666  39.857  -1.680  1.00 68.49  ? 121 TYR A CA  1 
ATOM   981   C C   . TYR A 1 121 ? 32.621  38.835  -1.217  1.00 67.08  ? 121 TYR A C   1 
ATOM   982   O O   . TYR A 1 121 ? 32.676  38.344  -0.092  1.00 66.41  ? 121 TYR A O   1 
ATOM   983   C CB  . TYR A 1 121 ? 35.151  39.550  -1.405  1.00 68.73  ? 121 TYR A CB  1 
ATOM   984   C CG  . TYR A 1 121 ? 36.080  40.542  -2.096  1.00 70.33  ? 121 TYR A CG  1 
ATOM   985   C CD1 . TYR A 1 121 ? 36.326  40.469  -3.463  1.00 71.20  ? 121 TYR A CD1 1 
ATOM   986   C CD2 . TYR A 1 121 ? 36.640  41.603  -1.397  1.00 71.42  ? 121 TYR A CD2 1 
ATOM   987   C CE1 . TYR A 1 121 ? 37.113  41.405  -4.112  1.00 72.73  ? 121 TYR A CE1 1 
ATOM   988   C CE2 . TYR A 1 121 ? 37.427  42.547  -2.034  1.00 72.96  ? 121 TYR A CE2 1 
ATOM   989   C CZ  . TYR A 1 121 ? 37.668  42.448  -3.394  1.00 73.93  ? 121 TYR A CZ  1 
ATOM   990   O OH  . TYR A 1 121 ? 38.474  43.369  -4.022  1.00 76.58  ? 121 TYR A OH  1 
ATOM   991   N N   . ASP A 1 122 ? 31.661  38.498  -2.090  1.00 66.86  ? 122 ASP A N   1 
ATOM   992   C CA  . ASP A 1 122 ? 30.503  37.740  -1.645  1.00 65.96  ? 122 ASP A CA  1 
ATOM   993   C C   . ASP A 1 122 ? 30.855  36.269  -1.538  1.00 64.87  ? 122 ASP A C   1 
ATOM   994   O O   . ASP A 1 122 ? 29.957  35.457  -1.229  1.00 65.18  ? 122 ASP A O   1 
ATOM   995   C CB  . ASP A 1 122 ? 29.261  37.965  -2.496  1.00 67.11  ? 122 ASP A CB  1 
ATOM   996   C CG  . ASP A 1 122 ? 29.243  37.485  -3.942  1.00 68.04  ? 122 ASP A CG  1 
ATOM   997   O OD1 . ASP A 1 122 ? 30.215  36.867  -4.385  1.00 67.74  ? 122 ASP A OD1 1 
ATOM   998   O OD2 . ASP A 1 122 ? 28.231  37.764  -4.630  1.00 69.85  ? 122 ASP A OD2 1 
ATOM   999   N N   . CYS A 1 123 ? 32.139  35.963  -1.830  1.00 63.63  ? 123 CYS A N   1 
ATOM   1000  C CA  . CYS A 1 123 ? 32.656  34.613  -1.704  1.00 62.15  ? 123 CYS A CA  1 
ATOM   1001  C C   . CYS A 1 123 ? 32.681  34.242  -0.225  1.00 61.01  ? 123 CYS A C   1 
ATOM   1002  O O   . CYS A 1 123 ? 32.600  33.065  0.127   1.00 60.28  ? 123 CYS A O   1 
ATOM   1003  C CB  . CYS A 1 123 ? 33.995  34.407  -2.428  1.00 62.54  ? 123 CYS A CB  1 
ATOM   1004  S SG  . CYS A 1 123 ? 35.425  35.308  -1.768  1.00 62.45  ? 123 CYS A SG  1 
ATOM   1005  N N   . ILE A 1 124 ? 32.766  35.245  0.649   1.00 60.99  ? 124 ILE A N   1 
ATOM   1006  C CA  . ILE A 1 124 ? 32.765  34.964  2.074   1.00 60.31  ? 124 ILE A CA  1 
ATOM   1007  C C   . ILE A 1 124 ? 31.374  34.497  2.519   1.00 60.40  ? 124 ILE A C   1 
ATOM   1008  O O   . ILE A 1 124 ? 30.398  35.268  2.456   1.00 61.15  ? 124 ILE A O   1 
ATOM   1009  C CB  . ILE A 1 124 ? 33.244  36.201  2.847   1.00 60.67  ? 124 ILE A CB  1 
ATOM   1010  C CG1 . ILE A 1 124 ? 34.715  36.556  2.459   1.00 60.99  ? 124 ILE A CG1 1 
ATOM   1011  C CG2 . ILE A 1 124 ? 33.053  35.988  4.351   1.00 60.07  ? 124 ILE A CG2 1 
ATOM   1012  C CD1 . ILE A 1 124 ? 35.305  37.755  3.185   1.00 61.66  ? 124 ILE A CD1 1 
ATOM   1013  N N   . ILE A 1 125 ? 31.291  33.235  2.992   1.00 59.30  ? 125 ILE A N   1 
ATOM   1014  C CA  . ILE A 1 125 ? 30.011  32.681  3.426   1.00 58.75  ? 125 ILE A CA  1 
ATOM   1015  C C   . ILE A 1 125 ? 29.999  32.395  4.935   1.00 58.93  ? 125 ILE A C   1 
ATOM   1016  O O   . ILE A 1 125 ? 28.951  32.067  5.483   1.00 58.85  ? 125 ILE A O   1 
ATOM   1017  C CB  . ILE A 1 125 ? 29.633  31.449  2.587   1.00 57.65  ? 125 ILE A CB  1 
ATOM   1018  C CG1 . ILE A 1 125 ? 30.581  30.281  2.838   1.00 57.17  ? 125 ILE A CG1 1 
ATOM   1019  C CG2 . ILE A 1 125 ? 29.556  31.799  1.103   1.00 57.95  ? 125 ILE A CG2 1 
ATOM   1020  C CD1 . ILE A 1 125 ? 30.117  28.957  2.249   1.00 56.70  ? 125 ILE A CD1 1 
ATOM   1021  N N   . THR A 1 126 ? 31.140  32.537  5.629   1.00 59.70  ? 126 THR A N   1 
ATOM   1022  C CA  . THR A 1 126 ? 31.162  32.446  7.087   1.00 60.07  ? 126 THR A CA  1 
ATOM   1023  C C   . THR A 1 126 ? 32.458  33.040  7.657   1.00 60.55  ? 126 THR A C   1 
ATOM   1024  O O   . THR A 1 126 ? 33.525  32.837  7.088   1.00 59.56  ? 126 THR A O   1 
ATOM   1025  C CB  . THR A 1 126 ? 30.992  30.988  7.517   1.00 59.64  ? 126 THR A CB  1 
ATOM   1026  O OG1 . THR A 1 126 ? 29.612  30.676  7.363   1.00 59.96  ? 126 THR A OG1 1 
ATOM   1027  C CG2 . THR A 1 126 ? 31.341  30.760  8.976   1.00 59.62  ? 126 THR A CG2 1 
ATOM   1028  N N   . TYR A 1 127 ? 32.320  33.780  8.774   1.00 61.21  ? 127 TYR A N   1 
ATOM   1029  C CA  . TYR A 1 127 ? 33.432  34.239  9.585   1.00 62.14  ? 127 TYR A CA  1 
ATOM   1030  C C   . TYR A 1 127 ? 33.575  33.329  10.806  1.00 63.12  ? 127 TYR A C   1 
ATOM   1031  O O   . TYR A 1 127 ? 32.640  33.178  11.580  1.00 63.77  ? 127 TYR A O   1 
ATOM   1032  C CB  . TYR A 1 127 ? 33.289  35.684  10.091  1.00 62.67  ? 127 TYR A CB  1 
ATOM   1033  C CG  . TYR A 1 127 ? 33.432  36.755  9.015   1.00 62.67  ? 127 TYR A CG  1 
ATOM   1034  C CD1 . TYR A 1 127 ? 32.362  37.067  8.195   1.00 62.67  ? 127 TYR A CD1 1 
ATOM   1035  C CD2 . TYR A 1 127 ? 34.619  37.440  8.803   1.00 62.35  ? 127 TYR A CD2 1 
ATOM   1036  C CE1 . TYR A 1 127 ? 32.466  38.014  7.194   1.00 62.92  ? 127 TYR A CE1 1 
ATOM   1037  C CE2 . TYR A 1 127 ? 34.735  38.382  7.797   1.00 62.69  ? 127 TYR A CE2 1 
ATOM   1038  C CZ  . TYR A 1 127 ? 33.657  38.664  6.992   1.00 62.86  ? 127 TYR A CZ  1 
ATOM   1039  O OH  . TYR A 1 127 ? 33.662  39.551  5.973   1.00 63.93  ? 127 TYR A OH  1 
ATOM   1040  N N   . LEU A 1 128 ? 34.774  32.766  11.003  1.00 64.38  ? 128 LEU A N   1 
ATOM   1041  C CA  . LEU A 1 128 ? 35.145  32.151  12.270  1.00 64.73  ? 128 LEU A CA  1 
ATOM   1042  C C   . LEU A 1 128 ? 35.894  33.161  13.134  1.00 66.39  ? 128 LEU A C   1 
ATOM   1043  O O   . LEU A 1 128 ? 36.954  33.653  12.761  1.00 66.78  ? 128 LEU A O   1 
ATOM   1044  C CB  . LEU A 1 128 ? 35.977  30.901  12.026  1.00 63.40  ? 128 LEU A CB  1 
ATOM   1045  C CG  . LEU A 1 128 ? 35.305  29.864  11.130  1.00 63.37  ? 128 LEU A CG  1 
ATOM   1046  C CD1 . LEU A 1 128 ? 36.220  28.683  10.816  1.00 63.35  ? 128 LEU A CD1 1 
ATOM   1047  C CD2 . LEU A 1 128 ? 33.999  29.395  11.769  1.00 63.47  ? 128 LEU A CD2 1 
ATOM   1048  N N   . VAL A 1 129 ? 35.344  33.399  14.323  1.00 67.43  ? 129 VAL A N   1 
ATOM   1049  C CA  . VAL A 1 129 ? 35.763  34.465  15.208  1.00 68.43  ? 129 VAL A CA  1 
ATOM   1050  C C   . VAL A 1 129 ? 36.985  34.080  16.041  1.00 68.47  ? 129 VAL A C   1 
ATOM   1051  O O   . VAL A 1 129 ? 37.714  34.955  16.459  1.00 69.00  ? 129 VAL A O   1 
ATOM   1052  C CB  . VAL A 1 129 ? 34.508  34.761  16.050  1.00 69.47  ? 129 VAL A CB  1 
ATOM   1053  C CG1 . VAL A 1 129 ? 34.757  34.668  17.549  1.00 70.02  ? 129 VAL A CG1 1 
ATOM   1054  C CG2 . VAL A 1 129 ? 33.885  36.094  15.653  1.00 70.64  ? 129 VAL A CG2 1 
ATOM   1055  N N   . ILE A 1 130 ? 37.226  32.791  16.295  1.00 68.95  ? 130 ILE A N   1 
ATOM   1056  C CA  . ILE A 1 130 ? 38.362  32.355  17.101  1.00 70.18  ? 130 ILE A CA  1 
ATOM   1057  C C   . ILE A 1 130 ? 38.508  30.852  16.935  1.00 71.79  ? 130 ILE A C   1 
ATOM   1058  O O   . ILE A 1 130 ? 37.522  30.182  16.654  1.00 74.37  ? 130 ILE A O   1 
ATOM   1059  C CB  . ILE A 1 130 ? 38.152  32.698  18.588  1.00 70.76  ? 130 ILE A CB  1 
ATOM   1060  C CG1 . ILE A 1 130 ? 39.380  32.341  19.425  1.00 70.65  ? 130 ILE A CG1 1 
ATOM   1061  C CG2 . ILE A 1 130 ? 36.887  32.026  19.140  1.00 70.88  ? 130 ILE A CG2 1 
ATOM   1062  C CD1 . ILE A 1 130 ? 39.393  32.962  20.813  1.00 71.59  ? 130 ILE A CD1 1 
ATOM   1063  N N   . ASN A 1 131 ? 39.691  30.301  17.207  1.00 73.39  ? 131 ASN A N   1 
ATOM   1064  C CA  . ASN A 1 131 ? 39.886  28.855  17.096  1.00 72.31  ? 131 ASN A CA  1 
ATOM   1065  C C   . ASN A 1 131 ? 40.347  28.247  18.425  1.00 73.57  ? 131 ASN A C   1 
ATOM   1066  O O   . ASN A 1 131 ? 41.123  28.836  19.163  1.00 76.52  ? 131 ASN A O   1 
ATOM   1067  C CB  . ASN A 1 131 ? 40.890  28.568  15.988  1.00 70.80  ? 131 ASN A CB  1 
ATOM   1068  C CG  . ASN A 1 131 ? 41.198  27.110  15.796  1.00 68.52  ? 131 ASN A CG  1 
ATOM   1069  O OD1 . ASN A 1 131 ? 40.338  26.261  15.991  1.00 68.14  ? 131 ASN A OD1 1 
ATOM   1070  N ND2 . ASN A 1 131 ? 42.397  26.799  15.347  1.00 68.20  ? 131 ASN A ND2 1 
ATOM   1071  N N   . GLU A 1 132 ? 39.874  27.038  18.706  1.00 73.76  ? 132 GLU A N   1 
ATOM   1072  C CA  . GLU A 1 132 ? 40.270  26.246  19.860  1.00 74.70  ? 132 GLU A CA  1 
ATOM   1073  C C   . GLU A 1 132 ? 40.533  27.049  21.125  1.00 75.29  ? 132 GLU A C   1 
ATOM   1074  O O   . GLU A 1 132 ? 41.618  26.955  21.673  1.00 77.85  ? 132 GLU A O   1 
ATOM   1075  C CB  . GLU A 1 132 ? 41.574  25.503  19.600  1.00 75.80  ? 132 GLU A CB  1 
ATOM   1076  C CG  . GLU A 1 132 ? 41.500  24.638  18.352  1.00 78.08  ? 132 GLU A CG  1 
ATOM   1077  C CD  . GLU A 1 132 ? 42.078  23.266  18.605  1.00 80.15  ? 132 GLU A CD  1 
ATOM   1078  O OE1 . GLU A 1 132 ? 43.274  23.281  18.954  1.00 82.91  ? 132 GLU A OE1 1 
ATOM   1079  O OE2 . GLU A 1 132 ? 41.363  22.241  18.480  1.00 76.73  ? 132 GLU A OE2 1 
ATOM   1080  N N   . PRO A 1 133 ? 39.556  27.772  21.698  1.00 74.32  ? 133 PRO A N   1 
ATOM   1081  C CA  . PRO A 1 133 ? 39.721  28.323  23.046  1.00 74.57  ? 133 PRO A CA  1 
ATOM   1082  C C   . PRO A 1 133 ? 39.747  27.216  24.105  1.00 74.87  ? 133 PRO A C   1 
ATOM   1083  O O   . PRO A 1 133 ? 38.899  26.307  24.117  1.00 75.89  ? 133 PRO A O   1 
ATOM   1084  C CB  . PRO A 1 133 ? 38.546  29.280  23.191  1.00 75.83  ? 133 PRO A CB  1 
ATOM   1085  C CG  . PRO A 1 133 ? 37.493  28.720  22.249  1.00 75.91  ? 133 PRO A CG  1 
ATOM   1086  C CD  . PRO A 1 133 ? 38.248  28.041  21.103  1.00 74.85  ? 133 PRO A CD  1 
ATOM   1087  N N   . GLN A 1 134 ? 40.772  27.296  24.962  1.00 75.25  ? 134 GLN A N   1 
ATOM   1088  C CA  . GLN A 1 134 ? 41.123  26.257  25.918  1.00 75.84  ? 134 GLN A CA  1 
ATOM   1089  C C   . GLN A 1 134 ? 40.382  26.564  27.216  1.00 75.15  ? 134 GLN A C   1 
ATOM   1090  O O   . GLN A 1 134 ? 40.108  27.724  27.534  1.00 74.95  ? 134 GLN A O   1 
ATOM   1091  C CB  . GLN A 1 134 ? 42.650  26.172  26.087  1.00 78.51  ? 134 GLN A CB  1 
ATOM   1092  C CG  . GLN A 1 134 ? 43.155  25.048  26.987  1.00 81.50  ? 134 GLN A CG  1 
ATOM   1093  C CD  . GLN A 1 134 ? 42.916  23.683  26.377  1.00 84.04  ? 134 GLN A CD  1 
ATOM   1094  O OE1 . GLN A 1 134 ? 43.327  23.462  25.235  1.00 88.33  ? 134 GLN A OE1 1 
ATOM   1095  N NE2 . GLN A 1 134 ? 42.220  22.782  27.073  1.00 83.62  ? 134 GLN A NE2 1 
ATOM   1096  N N   . THR A 1 135 ? 40.081  25.501  27.963  1.00 74.25  ? 135 THR A N   1 
ATOM   1097  C CA  . THR A 1 135 ? 39.134  25.559  29.059  1.00 74.68  ? 135 THR A CA  1 
ATOM   1098  C C   . THR A 1 135 ? 39.772  26.105  30.345  1.00 74.76  ? 135 THR A C   1 
ATOM   1099  O O   . THR A 1 135 ? 39.149  26.901  31.043  1.00 75.38  ? 135 THR A O   1 
ATOM   1100  C CB  . THR A 1 135 ? 38.524  24.166  29.178  1.00 75.20  ? 135 THR A CB  1 
ATOM   1101  O OG1 . THR A 1 135 ? 37.754  24.138  27.973  1.00 74.61  ? 135 THR A OG1 1 
ATOM   1102  C CG2 . THR A 1 135 ? 37.683  24.005  30.431  1.00 76.53  ? 135 THR A CG2 1 
ATOM   1103  N N   . ASP A 1 136 ? 41.016  25.722  30.665  1.00 74.45  ? 136 ASP A N   1 
ATOM   1104  C CA  . ASP A 1 136 ? 41.723  26.320  31.792  1.00 74.69  ? 136 ASP A CA  1 
ATOM   1105  C C   . ASP A 1 136 ? 41.858  27.826  31.581  1.00 74.67  ? 136 ASP A C   1 
ATOM   1106  O O   . ASP A 1 136 ? 41.764  28.631  32.517  1.00 75.02  ? 136 ASP A O   1 
ATOM   1107  C CB  . ASP A 1 136 ? 43.151  25.830  31.917  1.00 75.14  ? 136 ASP A CB  1 
ATOM   1108  C CG  . ASP A 1 136 ? 43.911  26.444  33.085  1.00 77.29  ? 136 ASP A CG  1 
ATOM   1109  O OD1 . ASP A 1 136 ? 43.591  26.033  34.224  1.00 77.45  ? 136 ASP A OD1 1 
ATOM   1110  O OD2 . ASP A 1 136 ? 44.783  27.367  32.853  1.00 78.03  ? 136 ASP A OD2 1 
ATOM   1111  N N   . HIS A 1 137 ? 42.113  28.181  30.319  1.00 73.32  ? 137 HIS A N   1 
ATOM   1112  C CA  . HIS A 1 137 ? 42.323  29.563  29.948  1.00 73.15  ? 137 HIS A CA  1 
ATOM   1113  C C   . HIS A 1 137 ? 41.109  30.378  30.335  1.00 73.31  ? 137 HIS A C   1 
ATOM   1114  O O   . HIS A 1 137 ? 41.242  31.414  30.985  1.00 74.23  ? 137 HIS A O   1 
ATOM   1115  C CB  . HIS A 1 137 ? 42.521  29.745  28.444  1.00 71.73  ? 137 HIS A CB  1 
ATOM   1116  C CG  . HIS A 1 137 ? 43.105  31.077  28.160  1.00 72.32  ? 137 HIS A CG  1 
ATOM   1117  N ND1 . HIS A 1 137 ? 42.708  31.845  27.090  1.00 71.93  ? 137 HIS A ND1 1 
ATOM   1118  C CD2 . HIS A 1 137 ? 44.047  31.782  28.813  1.00 73.46  ? 137 HIS A CD2 1 
ATOM   1119  C CE1 . HIS A 1 137 ? 43.404  32.972  27.090  1.00 72.90  ? 137 HIS A CE1 1 
ATOM   1120  N NE2 . HIS A 1 137 ? 44.231  32.947  28.119  1.00 73.97  ? 137 HIS A NE2 1 
ATOM   1121  N N   . ILE A 1 138 ? 39.945  29.878  29.906  1.00 72.72  ? 138 ILE A N   1 
ATOM   1122  C CA  . ILE A 1 138 ? 38.704  30.607  30.075  1.00 72.57  ? 138 ILE A CA  1 
ATOM   1123  C C   . ILE A 1 138 ? 38.393  30.680  31.569  1.00 73.31  ? 138 ILE A C   1 
ATOM   1124  O O   . ILE A 1 138 ? 37.822  31.650  32.026  1.00 73.64  ? 138 ILE A O   1 
ATOM   1125  C CB  . ILE A 1 138 ? 37.575  29.982  29.236  1.00 71.86  ? 138 ILE A CB  1 
ATOM   1126  C CG1 . ILE A 1 138 ? 37.870  30.057  27.725  1.00 70.85  ? 138 ILE A CG1 1 
ATOM   1127  C CG2 . ILE A 1 138 ? 36.233  30.632  29.570  1.00 72.65  ? 138 ILE A CG2 1 
ATOM   1128  C CD1 . ILE A 1 138 ? 36.713  29.632  26.822  1.00 69.77  ? 138 ILE A CD1 1 
ATOM   1129  N N   . HIS A 1 139 ? 38.828  29.692  32.352  1.00 73.95  ? 139 HIS A N   1 
ATOM   1130  C CA  . HIS A 1 139 ? 38.661  29.773  33.794  1.00 75.06  ? 139 HIS A CA  1 
ATOM   1131  C C   . HIS A 1 139 ? 39.464  30.958  34.305  1.00 75.86  ? 139 HIS A C   1 
ATOM   1132  O O   . HIS A 1 139 ? 38.964  31.737  35.114  1.00 76.60  ? 139 HIS A O   1 
ATOM   1133  C CB  . HIS A 1 139 ? 39.084  28.467  34.484  1.00 75.43  ? 139 HIS A CB  1 
ATOM   1134  C CG  . HIS A 1 139 ? 38.827  28.424  35.958  1.00 76.79  ? 139 HIS A CG  1 
ATOM   1135  N ND1 . HIS A 1 139 ? 37.642  27.993  36.525  1.00 77.16  ? 139 HIS A ND1 1 
ATOM   1136  C CD2 . HIS A 1 139 ? 39.624  28.744  36.976  1.00 78.07  ? 139 HIS A CD2 1 
ATOM   1137  C CE1 . HIS A 1 139 ? 37.728  28.062  37.845  1.00 78.50  ? 139 HIS A CE1 1 
ATOM   1138  N NE2 . HIS A 1 139 ? 38.924  28.521  38.138  1.00 79.31  ? 139 HIS A NE2 1 
ATOM   1139  N N   . SER A 1 140 ? 40.700  31.086  33.797  1.00 75.88  ? 140 SER A N   1 
ATOM   1140  C CA  . SER A 1 140 ? 41.671  32.018  34.361  1.00 76.88  ? 140 SER A CA  1 
ATOM   1141  C C   . SER A 1 140 ? 41.257  33.451  34.086  1.00 76.44  ? 140 SER A C   1 
ATOM   1142  O O   . SER A 1 140 ? 41.261  34.246  35.017  1.00 77.04  ? 140 SER A O   1 
ATOM   1143  C CB  . SER A 1 140 ? 43.076  31.795  33.876  1.00 76.86  ? 140 SER A CB  1 
ATOM   1144  O OG  . SER A 1 140 ? 43.965  32.599  34.638  1.00 78.53  ? 140 SER A OG  1 
ATOM   1145  N N   . VAL A 1 141 ? 40.919  33.727  32.814  1.00 75.43  ? 141 VAL A N   1 
ATOM   1146  C CA  . VAL A 1 141 ? 40.528  35.050  32.331  1.00 75.75  ? 141 VAL A CA  1 
ATOM   1147  C C   . VAL A 1 141 ? 39.018  35.271  32.494  1.00 75.55  ? 141 VAL A C   1 
ATOM   1148  O O   . VAL A 1 141 ? 38.552  36.393  32.255  1.00 76.94  ? 141 VAL A O   1 
ATOM   1149  C CB  . VAL A 1 141 ? 40.920  35.314  30.858  1.00 74.73  ? 141 VAL A CB  1 
ATOM   1150  C CG1 . VAL A 1 141 ? 42.402  35.096  30.588  1.00 74.90  ? 141 VAL A CG1 1 
ATOM   1151  C CG2 . VAL A 1 141 ? 40.100  34.482  29.879  1.00 73.21  ? 141 VAL A CG2 1 
ATOM   1152  N N   . THR A 1 142 ? 38.277  34.222  32.886  1.00 73.87  ? 142 THR A N   1 
ATOM   1153  C CA  . THR A 1 142 ? 36.863  34.284  33.216  1.00 73.80  ? 142 THR A CA  1 
ATOM   1154  C C   . THR A 1 142 ? 36.056  34.110  31.939  1.00 72.60  ? 142 THR A C   1 
ATOM   1155  O O   . THR A 1 142 ? 36.412  34.655  30.886  1.00 71.15  ? 142 THR A O   1 
ATOM   1156  C CB  . THR A 1 142 ? 36.391  35.552  33.944  1.00 75.02  ? 142 THR A CB  1 
ATOM   1157  O OG1 . THR A 1 142 ? 36.369  36.637  33.014  1.00 74.13  ? 142 THR A OG1 1 
ATOM   1158  C CG2 . THR A 1 142 ? 37.140  35.787  35.244  1.00 76.30  ? 142 THR A CG2 1 
ATOM   1159  N N   . GLY A 1 143 ? 34.959  33.345  32.094  1.00 72.73  ? 143 GLY A N   1 
ATOM   1160  C CA  . GLY A 1 143 ? 33.979  33.167  31.040  1.00 72.25  ? 143 GLY A CA  1 
ATOM   1161  C C   . GLY A 1 143 ? 33.367  34.507  30.638  1.00 72.97  ? 143 GLY A C   1 
ATOM   1162  O O   . GLY A 1 143 ? 33.073  34.733  29.463  1.00 71.42  ? 143 GLY A O   1 
ATOM   1163  N N   . LYS A 1 144 ? 33.192  35.399  31.614  1.00 75.06  ? 144 LYS A N   1 
ATOM   1164  C CA  . LYS A 1 144 ? 32.553  36.668  31.313  1.00 77.30  ? 144 LYS A CA  1 
ATOM   1165  C C   . LYS A 1 144 ? 33.313  37.323  30.169  1.00 76.49  ? 144 LYS A C   1 
ATOM   1166  O O   . LYS A 1 144 ? 32.720  37.801  29.206  1.00 75.05  ? 144 LYS A O   1 
ATOM   1167  C CB  . LYS A 1 144 ? 32.500  37.659  32.484  1.00 80.10  ? 144 LYS A CB  1 
ATOM   1168  C CG  . LYS A 1 144 ? 31.877  39.002  32.131  1.00 81.17  ? 144 LYS A CG  1 
ATOM   1169  C CD  . LYS A 1 144 ? 31.396  39.834  33.316  1.00 83.59  ? 144 LYS A CD  1 
ATOM   1170  C CE  . LYS A 1 144 ? 30.978  41.227  32.943  1.00 83.67  ? 144 LYS A CE  1 
ATOM   1171  N NZ  . LYS A 1 144 ? 29.944  41.178  31.902  1.00 83.28  ? 144 LYS A NZ  1 
ATOM   1172  N N   . ALA A 1 145 ? 34.641  37.323  30.307  1.00 77.46  ? 145 ALA A N   1 
ATOM   1173  C CA  . ALA A 1 145 ? 35.511  37.991  29.354  1.00 76.94  ? 145 ALA A CA  1 
ATOM   1174  C C   . ALA A 1 145 ? 35.330  37.342  27.984  1.00 75.22  ? 145 ALA A C   1 
ATOM   1175  O O   . ALA A 1 145 ? 35.216  38.020  26.962  1.00 73.49  ? 145 ALA A O   1 
ATOM   1176  C CB  . ALA A 1 145 ? 36.946  37.922  29.839  1.00 77.18  ? 145 ALA A CB  1 
ATOM   1177  N N   . PHE A 1 146 ? 35.274  36.010  27.987  1.00 74.58  ? 146 PHE A N   1 
ATOM   1178  C CA  . PHE A 1 146 ? 35.159  35.275  26.740  1.00 74.25  ? 146 PHE A CA  1 
ATOM   1179  C C   . PHE A 1 146 ? 33.897  35.694  25.981  1.00 73.61  ? 146 PHE A C   1 
ATOM   1180  O O   . PHE A 1 146 ? 33.996  36.082  24.819  1.00 75.04  ? 146 PHE A O   1 
ATOM   1181  C CB  . PHE A 1 146 ? 35.215  33.760  26.962  1.00 74.15  ? 146 PHE A CB  1 
ATOM   1182  C CG  . PHE A 1 146 ? 34.985  32.951  25.693  1.00 72.64  ? 146 PHE A CG  1 
ATOM   1183  C CD1 . PHE A 1 146 ? 35.944  32.908  24.692  1.00 72.47  ? 146 PHE A CD1 1 
ATOM   1184  C CD2 . PHE A 1 146 ? 33.814  32.229  25.507  1.00 71.81  ? 146 PHE A CD2 1 
ATOM   1185  C CE1 . PHE A 1 146 ? 35.731  32.155  23.543  1.00 71.35  ? 146 PHE A CE1 1 
ATOM   1186  C CE2 . PHE A 1 146 ? 33.618  31.484  24.358  1.00 70.38  ? 146 PHE A CE2 1 
ATOM   1187  C CZ  . PHE A 1 146 ? 34.571  31.459  23.375  1.00 69.87  ? 146 PHE A CZ  1 
ATOM   1188  N N   . VAL A 1 147 ? 32.720  35.636  26.617  1.00 72.36  ? 147 VAL A N   1 
ATOM   1189  C CA  . VAL A 1 147 ? 31.476  35.944  25.915  1.00 71.42  ? 147 VAL A CA  1 
ATOM   1190  C C   . VAL A 1 147 ? 31.492  37.391  25.391  1.00 71.74  ? 147 VAL A C   1 
ATOM   1191  O O   . VAL A 1 147 ? 31.148  37.676  24.238  1.00 70.66  ? 147 VAL A O   1 
ATOM   1192  C CB  . VAL A 1 147 ? 30.257  35.722  26.831  1.00 71.32  ? 147 VAL A CB  1 
ATOM   1193  C CG1 . VAL A 1 147 ? 28.957  35.868  26.062  1.00 70.67  ? 147 VAL A CG1 1 
ATOM   1194  C CG2 . VAL A 1 147 ? 30.315  34.377  27.539  1.00 71.24  ? 147 VAL A CG2 1 
ATOM   1195  N N   . ASP A 1 148 ? 31.872  38.324  26.266  1.00 72.53  ? 148 ASP A N   1 
ATOM   1196  C CA  . ASP A 1 148 ? 31.823  39.737  25.944  1.00 73.54  ? 148 ASP A CA  1 
ATOM   1197  C C   . ASP A 1 148 ? 32.626  40.010  24.670  1.00 73.01  ? 148 ASP A C   1 
ATOM   1198  O O   . ASP A 1 148 ? 32.213  40.830  23.838  1.00 73.11  ? 148 ASP A O   1 
ATOM   1199  C CB  . ASP A 1 148 ? 32.178  40.537  27.185  1.00 74.80  ? 148 ASP A CB  1 
ATOM   1200  C CG  . ASP A 1 148 ? 31.168  40.397  28.326  1.00 75.91  ? 148 ASP A CG  1 
ATOM   1201  O OD1 . ASP A 1 148 ? 30.022  39.899  28.080  1.00 74.47  ? 148 ASP A OD1 1 
ATOM   1202  O OD2 . ASP A 1 148 ? 31.523  40.803  29.460  1.00 77.44  ? 148 ASP A OD2 1 
ATOM   1203  N N   . LEU A 1 149 ? 33.743  39.283  24.511  1.00 72.27  ? 149 LEU A N   1 
ATOM   1204  C CA  . LEU A 1 149 ? 34.573  39.398  23.323  1.00 72.06  ? 149 LEU A CA  1 
ATOM   1205  C C   . LEU A 1 149 ? 33.782  38.932  22.111  1.00 71.45  ? 149 LEU A C   1 
ATOM   1206  O O   . LEU A 1 149 ? 33.504  39.734  21.216  1.00 71.72  ? 149 LEU A O   1 
ATOM   1207  C CB  . LEU A 1 149 ? 35.876  38.614  23.427  1.00 71.93  ? 149 LEU A CB  1 
ATOM   1208  C CG  . LEU A 1 149 ? 36.820  38.770  22.230  1.00 71.76  ? 149 LEU A CG  1 
ATOM   1209  C CD1 . LEU A 1 149 ? 37.217  40.215  21.986  1.00 72.51  ? 149 LEU A CD1 1 
ATOM   1210  C CD2 . LEU A 1 149 ? 38.061  37.935  22.450  1.00 71.98  ? 149 LEU A CD2 1 
ATOM   1211  N N   . MET A 1 150 ? 33.418  37.639  22.122  1.00 70.33  ? 150 MET A N   1 
ATOM   1212  C CA  . MET A 1 150 ? 32.571  37.059  21.095  1.00 69.33  ? 150 MET A CA  1 
ATOM   1213  C C   . MET A 1 150 ? 31.415  38.018  20.769  1.00 70.36  ? 150 MET A C   1 
ATOM   1214  O O   . MET A 1 150 ? 31.113  38.268  19.599  1.00 70.42  ? 150 MET A O   1 
ATOM   1215  C CB  . MET A 1 150 ? 31.989  35.714  21.551  1.00 69.29  ? 150 MET A CB  1 
ATOM   1216  C CG  . MET A 1 150 ? 32.995  34.603  21.894  1.00 69.09  ? 150 MET A CG  1 
ATOM   1217  S SD  . MET A 1 150 ? 34.072  34.055  20.557  1.00 67.08  ? 150 MET A SD  1 
ATOM   1218  C CE  . MET A 1 150 ? 35.605  34.901  20.966  1.00 68.22  ? 150 MET A CE  1 
ATOM   1219  N N   . ASN A 1 151 ? 30.737  38.577  21.780  1.00 70.72  ? 151 ASN A N   1 
ATOM   1220  C CA  . ASN A 1 151 ? 29.629  39.467  21.452  1.00 71.93  ? 151 ASN A CA  1 
ATOM   1221  C C   . ASN A 1 151 ? 30.136  40.704  20.715  1.00 71.90  ? 151 ASN A C   1 
ATOM   1222  O O   . ASN A 1 151 ? 29.525  41.078  19.713  1.00 70.95  ? 151 ASN A O   1 
ATOM   1223  C CB  . ASN A 1 151 ? 28.760  39.869  22.642  1.00 73.11  ? 151 ASN A CB  1 
ATOM   1224  C CG  . ASN A 1 151 ? 27.858  38.736  23.062  1.00 72.13  ? 151 ASN A CG  1 
ATOM   1225  O OD1 . ASN A 1 151 ? 27.730  38.458  24.257  1.00 72.84  ? 151 ASN A OD1 1 
ATOM   1226  N ND2 . ASN A 1 151 ? 27.240  38.072  22.099  1.00 71.01  ? 151 ASN A ND2 1 
ATOM   1227  N N   . THR A 1 152 ? 31.238  41.306  21.205  1.00 71.89  ? 152 THR A N   1 
ATOM   1228  C CA  . THR A 1 152 ? 31.845  42.430  20.508  1.00 72.40  ? 152 THR A CA  1 
ATOM   1229  C C   . THR A 1 152 ? 32.094  42.030  19.058  1.00 70.77  ? 152 THR A C   1 
ATOM   1230  O O   . THR A 1 152 ? 31.679  42.729  18.134  1.00 70.95  ? 152 THR A O   1 
ATOM   1231  C CB  . THR A 1 152 ? 33.156  42.906  21.139  1.00 73.39  ? 152 THR A CB  1 
ATOM   1232  O OG1 . THR A 1 152 ? 32.887  43.469  22.414  1.00 75.58  ? 152 THR A OG1 1 
ATOM   1233  C CG2 . THR A 1 152 ? 33.802  44.031  20.354  1.00 73.47  ? 152 THR A CG2 1 
ATOM   1234  N N   . LEU A 1 153 ? 32.798  40.910  18.872  1.00 69.09  ? 153 LEU A N   1 
ATOM   1235  C CA  . LEU A 1 153 ? 33.295  40.562  17.555  1.00 68.28  ? 153 LEU A CA  1 
ATOM   1236  C C   . LEU A 1 153 ? 32.124  40.230  16.627  1.00 68.60  ? 153 LEU A C   1 
ATOM   1237  O O   . LEU A 1 153 ? 32.028  40.796  15.536  1.00 69.85  ? 153 LEU A O   1 
ATOM   1238  C CB  . LEU A 1 153 ? 34.312  39.433  17.673  1.00 67.30  ? 153 LEU A CB  1 
ATOM   1239  C CG  . LEU A 1 153 ? 35.627  39.758  18.401  1.00 67.50  ? 153 LEU A CG  1 
ATOM   1240  C CD1 . LEU A 1 153 ? 36.460  38.505  18.635  1.00 66.76  ? 153 LEU A CD1 1 
ATOM   1241  C CD2 . LEU A 1 153 ? 36.434  40.762  17.615  1.00 68.01  ? 153 LEU A CD2 1 
ATOM   1242  N N   . ILE A 1 154 ? 31.200  39.369  17.085  1.00 67.52  ? 154 ILE A N   1 
ATOM   1243  C CA  . ILE A 1 154 ? 30.015  39.042  16.320  1.00 66.27  ? 154 ILE A CA  1 
ATOM   1244  C C   . ILE A 1 154 ? 29.353  40.336  15.847  1.00 66.73  ? 154 ILE A C   1 
ATOM   1245  O O   . ILE A 1 154 ? 29.187  40.568  14.646  1.00 66.78  ? 154 ILE A O   1 
ATOM   1246  C CB  . ILE A 1 154 ? 29.064  38.193  17.178  1.00 66.70  ? 154 ILE A CB  1 
ATOM   1247  C CG1 . ILE A 1 154 ? 29.602  36.778  17.408  1.00 66.38  ? 154 ILE A CG1 1 
ATOM   1248  C CG2 . ILE A 1 154 ? 27.658  38.149  16.569  1.00 66.59  ? 154 ILE A CG2 1 
ATOM   1249  C CD1 . ILE A 1 154 ? 28.856  36.008  18.489  1.00 66.59  ? 154 ILE A CD1 1 
ATOM   1250  N N   . ASN A 1 155 ? 28.955  41.175  16.806  1.00 66.74  ? 155 ASN A N   1 
ATOM   1251  C CA  . ASN A 1 155 ? 28.187  42.364  16.494  1.00 67.49  ? 155 ASN A CA  1 
ATOM   1252  C C   . ASN A 1 155 ? 28.900  43.134  15.381  1.00 68.52  ? 155 ASN A C   1 
ATOM   1253  O O   . ASN A 1 155 ? 28.307  43.367  14.332  1.00 69.55  ? 155 ASN A O   1 
ATOM   1254  C CB  . ASN A 1 155 ? 27.901  43.171  17.756  1.00 68.03  ? 155 ASN A CB  1 
ATOM   1255  C CG  . ASN A 1 155 ? 26.952  42.470  18.704  1.00 67.67  ? 155 ASN A CG  1 
ATOM   1256  O OD1 . ASN A 1 155 ? 26.205  41.560  18.316  1.00 67.08  ? 155 ASN A OD1 1 
ATOM   1257  N ND2 . ASN A 1 155 ? 26.948  42.876  19.964  1.00 68.17  ? 155 ASN A ND2 1 
ATOM   1258  N N   . ILE A 1 156 ? 30.184  43.478  15.590  1.00 68.79  ? 156 ILE A N   1 
ATOM   1259  C CA  . ILE A 1 156 ? 30.999  44.176  14.603  1.00 68.90  ? 156 ILE A CA  1 
ATOM   1260  C C   . ILE A 1 156 ? 30.887  43.525  13.225  1.00 68.24  ? 156 ILE A C   1 
ATOM   1261  O O   . ILE A 1 156 ? 30.741  44.198  12.220  1.00 68.56  ? 156 ILE A O   1 
ATOM   1262  C CB  . ILE A 1 156 ? 32.462  44.265  15.069  1.00 69.21  ? 156 ILE A CB  1 
ATOM   1263  C CG1 . ILE A 1 156 ? 32.608  45.245  16.232  1.00 70.14  ? 156 ILE A CG1 1 
ATOM   1264  C CG2 . ILE A 1 156 ? 33.420  44.620  13.922  1.00 69.48  ? 156 ILE A CG2 1 
ATOM   1265  C CD1 . ILE A 1 156 ? 33.947  45.154  16.938  1.00 70.24  ? 156 ILE A CD1 1 
ATOM   1266  N N   . ILE A 1 157 ? 30.943  42.203  13.142  1.00 68.02  ? 157 ILE A N   1 
ATOM   1267  C CA  . ILE A 1 157 ? 30.864  41.577  11.833  1.00 67.62  ? 157 ILE A CA  1 
ATOM   1268  C C   . ILE A 1 157 ? 29.451  41.746  11.268  1.00 67.63  ? 157 ILE A C   1 
ATOM   1269  O O   . ILE A 1 157 ? 29.302  41.983  10.068  1.00 67.71  ? 157 ILE A O   1 
ATOM   1270  C CB  . ILE A 1 157 ? 31.311  40.111  11.897  1.00 66.97  ? 157 ILE A CB  1 
ATOM   1271  C CG1 . ILE A 1 157 ? 32.734  39.951  12.451  1.00 67.00  ? 157 ILE A CG1 1 
ATOM   1272  C CG2 . ILE A 1 157 ? 31.194  39.472  10.514  1.00 67.18  ? 157 ILE A CG2 1 
ATOM   1273  C CD1 . ILE A 1 157 ? 33.121  38.508  12.784  1.00 66.04  ? 157 ILE A CD1 1 
ATOM   1274  N N   . HIS A 1 158 ? 28.421  41.647  12.122  1.00 67.33  ? 158 HIS A N   1 
ATOM   1275  C CA  . HIS A 1 158 ? 27.064  41.783  11.623  1.00 68.18  ? 158 HIS A CA  1 
ATOM   1276  C C   . HIS A 1 158 ? 26.889  43.130  10.931  1.00 69.45  ? 158 HIS A C   1 
ATOM   1277  O O   . HIS A 1 158 ? 26.354  43.176  9.823   1.00 69.14  ? 158 HIS A O   1 
ATOM   1278  C CB  . HIS A 1 158 ? 25.982  41.563  12.692  1.00 68.46  ? 158 HIS A CB  1 
ATOM   1279  C CG  . HIS A 1 158 ? 25.789  40.132  13.042  1.00 67.16  ? 158 HIS A CG  1 
ATOM   1280  N ND1 . HIS A 1 158 ? 25.211  39.740  14.228  1.00 67.08  ? 158 HIS A ND1 1 
ATOM   1281  C CD2 . HIS A 1 158 ? 26.141  39.013  12.397  1.00 65.92  ? 158 HIS A CD2 1 
ATOM   1282  C CE1 . HIS A 1 158 ? 25.200  38.418  14.282  1.00 66.21  ? 158 HIS A CE1 1 
ATOM   1283  N NE2 . HIS A 1 158 ? 25.778  37.956  13.194  1.00 65.56  ? 158 HIS A NE2 1 
ATOM   1284  N N   . LYS A 1 159 ? 27.325  44.212  11.592  1.00 71.09  ? 159 LYS A N   1 
ATOM   1285  C CA  . LYS A 1 159 ? 27.153  45.545  11.036  1.00 73.02  ? 159 LYS A CA  1 
ATOM   1286  C C   . LYS A 1 159 ? 28.064  45.707  9.822   1.00 70.72  ? 159 LYS A C   1 
ATOM   1287  O O   . LYS A 1 159 ? 27.655  46.318  8.833   1.00 70.53  ? 159 LYS A O   1 
ATOM   1288  C CB  . LYS A 1 159 ? 27.385  46.660  12.063  1.00 77.45  ? 159 LYS A CB  1 
ATOM   1289  C CG  . LYS A 1 159 ? 26.517  46.607  13.331  1.00 82.54  ? 159 LYS A CG  1 
ATOM   1290  C CD  . LYS A 1 159 ? 26.716  47.731  14.356  1.00 88.63  ? 159 LYS A CD  1 
ATOM   1291  C CE  . LYS A 1 159 ? 28.123  47.749  14.996  1.00 94.14  ? 159 LYS A CE  1 
ATOM   1292  N NZ  . LYS A 1 159 ? 28.642  46.490  15.589  1.00 91.27  ? 159 LYS A NZ  1 
ATOM   1293  N N   . GLY A 1 160 ? 29.275  45.126  9.911   1.00 68.23  ? 160 GLY A N   1 
ATOM   1294  C CA  . GLY A 1 160 ? 30.353  45.414  8.983   1.00 67.66  ? 160 GLY A CA  1 
ATOM   1295  C C   . GLY A 1 160 ? 30.251  44.607  7.694   1.00 66.73  ? 160 GLY A C   1 
ATOM   1296  O O   . GLY A 1 160 ? 30.613  45.101  6.636   1.00 67.03  ? 160 GLY A O   1 
ATOM   1297  N N   . HIS A 1 161 ? 29.827  43.343  7.793   1.00 65.73  ? 161 HIS A N   1 
ATOM   1298  C CA  . HIS A 1 161 ? 29.568  42.533  6.615   1.00 65.37  ? 161 HIS A CA  1 
ATOM   1299  C C   . HIS A 1 161 ? 28.178  41.899  6.752   1.00 65.26  ? 161 HIS A C   1 
ATOM   1300  O O   . HIS A 1 161 ? 28.029  40.707  7.038   1.00 63.42  ? 161 HIS A O   1 
ATOM   1301  C CB  . HIS A 1 161 ? 30.716  41.545  6.405   1.00 64.57  ? 161 HIS A CB  1 
ATOM   1302  C CG  . HIS A 1 161 ? 30.766  40.980  5.024   1.00 64.57  ? 161 HIS A CG  1 
ATOM   1303  N ND1 . HIS A 1 161 ? 31.706  40.049  4.625   1.00 64.03  ? 161 HIS A ND1 1 
ATOM   1304  C CD2 . HIS A 1 161 ? 29.955  41.182  3.964   1.00 65.07  ? 161 HIS A CD2 1 
ATOM   1305  C CE1 . HIS A 1 161 ? 31.481  39.724  3.355   1.00 64.15  ? 161 HIS A CE1 1 
ATOM   1306  N NE2 . HIS A 1 161 ? 30.411  40.389  2.935   1.00 64.65  ? 161 HIS A NE2 1 
ATOM   1307  N N   . PRO A 1 162 ? 27.095  42.701  6.581   1.00 67.03  ? 162 PRO A N   1 
ATOM   1308  C CA  . PRO A 1 162 ? 25.731  42.206  6.796   1.00 66.98  ? 162 PRO A CA  1 
ATOM   1309  C C   . PRO A 1 162 ? 25.485  41.082  5.809   1.00 66.63  ? 162 PRO A C   1 
ATOM   1310  O O   . PRO A 1 162 ? 25.942  41.181  4.672   1.00 67.52  ? 162 PRO A O   1 
ATOM   1311  C CB  . PRO A 1 162 ? 24.864  43.389  6.527   1.00 68.57  ? 162 PRO A CB  1 
ATOM   1312  C CG  . PRO A 1 162 ? 25.719  44.305  5.667   1.00 69.33  ? 162 PRO A CG  1 
ATOM   1313  C CD  . PRO A 1 162 ? 27.134  44.107  6.141   1.00 68.34  ? 162 PRO A CD  1 
ATOM   1314  N N   . GLY A 1 163 ? 24.841  40.007  6.279   1.00 65.56  ? 163 GLY A N   1 
ATOM   1315  C CA  . GLY A 1 163 ? 24.488  38.900  5.418   1.00 64.73  ? 163 GLY A CA  1 
ATOM   1316  C C   . GLY A 1 163 ? 25.091  37.599  5.925   1.00 64.09  ? 163 GLY A C   1 
ATOM   1317  O O   . GLY A 1 163 ? 24.489  36.548  5.728   1.00 65.47  ? 163 GLY A O   1 
ATOM   1318  N N   . ILE A 1 164 ? 26.245  37.674  6.606   1.00 63.13  ? 164 ILE A N   1 
ATOM   1319  C CA  . ILE A 1 164 ? 27.187  36.563  6.668   1.00 61.49  ? 164 ILE A CA  1 
ATOM   1320  C C   . ILE A 1 164 ? 27.179  35.912  8.053   1.00 61.34  ? 164 ILE A C   1 
ATOM   1321  O O   . ILE A 1 164 ? 27.510  36.514  9.064   1.00 62.17  ? 164 ILE A O   1 
ATOM   1322  C CB  . ILE A 1 164 ? 28.620  37.021  6.316   1.00 60.94  ? 164 ILE A CB  1 
ATOM   1323  C CG1 . ILE A 1 164 ? 28.720  37.757  4.975   1.00 61.30  ? 164 ILE A CG1 1 
ATOM   1324  C CG2 . ILE A 1 164 ? 29.572  35.830  6.346   1.00 60.11  ? 164 ILE A CG2 1 
ATOM   1325  C CD1 . ILE A 1 164 ? 28.239  36.962  3.773   1.00 61.07  ? 164 ILE A CD1 1 
ATOM   1326  N N   . PRO A 1 165 ? 26.915  34.604  8.158   1.00 60.94  ? 165 PRO A N   1 
ATOM   1327  C CA  . PRO A 1 165 ? 27.077  33.910  9.436   1.00 60.82  ? 165 PRO A CA  1 
ATOM   1328  C C   . PRO A 1 165 ? 28.432  34.030  10.153  1.00 61.20  ? 165 PRO A C   1 
ATOM   1329  O O   . PRO A 1 165 ? 29.507  33.901  9.553   1.00 60.89  ? 165 PRO A O   1 
ATOM   1330  C CB  . PRO A 1 165 ? 26.813  32.460  9.003   1.00 60.17  ? 165 PRO A CB  1 
ATOM   1331  C CG  . PRO A 1 165 ? 25.892  32.573  7.813   1.00 60.50  ? 165 PRO A CG  1 
ATOM   1332  C CD  . PRO A 1 165 ? 26.443  33.749  7.061   1.00 60.90  ? 165 PRO A CD  1 
ATOM   1333  N N   . VAL A 1 166 ? 28.359  34.219  11.476  1.00 61.64  ? 166 VAL A N   1 
ATOM   1334  C CA  . VAL A 1 166 ? 29.507  34.246  12.364  1.00 61.41  ? 166 VAL A CA  1 
ATOM   1335  C C   . VAL A 1 166 ? 29.369  33.090  13.342  1.00 61.84  ? 166 VAL A C   1 
ATOM   1336  O O   . VAL A 1 166 ? 28.340  32.967  13.992  1.00 62.25  ? 166 VAL A O   1 
ATOM   1337  C CB  . VAL A 1 166 ? 29.504  35.587  13.117  1.00 61.87  ? 166 VAL A CB  1 
ATOM   1338  C CG1 . VAL A 1 166 ? 30.564  35.656  14.200  1.00 61.80  ? 166 VAL A CG1 1 
ATOM   1339  C CG2 . VAL A 1 166 ? 29.610  36.759  12.155  1.00 62.41  ? 166 VAL A CG2 1 
ATOM   1340  N N   . THR A 1 167 ? 30.407  32.256  13.441  1.00 62.58  ? 167 THR A N   1 
ATOM   1341  C CA  . THR A 1 167 ? 30.491  31.218  14.458  1.00 62.66  ? 167 THR A CA  1 
ATOM   1342  C C   . THR A 1 167 ? 31.961  31.111  14.839  1.00 62.16  ? 167 THR A C   1 
ATOM   1343  O O   . THR A 1 167 ? 32.737  31.941  14.394  1.00 63.27  ? 167 THR A O   1 
ATOM   1344  C CB  . THR A 1 167 ? 29.883  29.917  13.935  1.00 62.10  ? 167 THR A CB  1 
ATOM   1345  O OG1 . THR A 1 167 ? 29.997  28.948  14.967  1.00 62.01  ? 167 THR A OG1 1 
ATOM   1346  C CG2 . THR A 1 167 ? 30.631  29.351  12.745  1.00 61.72  ? 167 THR A CG2 1 
ATOM   1347  N N   . LEU A 1 168 ? 32.304  30.131  15.673  1.00 61.75  ? 168 LEU A N   1 
ATOM   1348  C CA  . LEU A 1 168 ? 33.666  29.900  16.130  1.00 62.53  ? 168 LEU A CA  1 
ATOM   1349  C C   . LEU A 1 168 ? 34.087  28.449  15.866  1.00 62.94  ? 168 LEU A C   1 
ATOM   1350  O O   . LEU A 1 168 ? 33.289  27.536  15.722  1.00 62.81  ? 168 LEU A O   1 
ATOM   1351  C CB  . LEU A 1 168 ? 33.744  30.234  17.620  1.00 63.24  ? 168 LEU A CB  1 
ATOM   1352  C CG  . LEU A 1 168 ? 33.346  29.132  18.607  1.00 63.49  ? 168 LEU A CG  1 
ATOM   1353  C CD1 . LEU A 1 168 ? 33.680  29.476  20.031  1.00 64.09  ? 168 LEU A CD1 1 
ATOM   1354  C CD2 . LEU A 1 168 ? 31.865  28.826  18.533  1.00 64.18  ? 168 LEU A CD2 1 
ATOM   1355  N N   . SER A 1 169 ? 35.387  28.221  15.852  1.00 64.45  ? 169 SER A N   1 
ATOM   1356  C CA  . SER A 1 169 ? 35.966  26.914  15.580  1.00 64.12  ? 169 SER A CA  1 
ATOM   1357  C C   . SER A 1 169 ? 36.384  26.269  16.909  1.00 63.36  ? 169 SER A C   1 
ATOM   1358  O O   . SER A 1 169 ? 37.562  26.212  17.247  1.00 62.61  ? 169 SER A O   1 
ATOM   1359  C CB  . SER A 1 169 ? 37.101  27.105  14.590  1.00 64.97  ? 169 SER A CB  1 
ATOM   1360  O OG  . SER A 1 169 ? 38.148  26.193  14.816  1.00 68.76  ? 169 SER A OG  1 
ATOM   1361  N N   . ALA A 1 170 ? 35.388  25.908  17.729  1.00 62.86  ? 170 ALA A N   1 
ATOM   1362  C CA  . ALA A 1 170 ? 35.634  25.333  19.045  1.00 63.34  ? 170 ALA A CA  1 
ATOM   1363  C C   . ALA A 1 170 ? 35.792  23.823  18.917  1.00 64.08  ? 170 ALA A C   1 
ATOM   1364  O O   . ALA A 1 170 ? 35.178  23.219  18.041  1.00 64.63  ? 170 ALA A O   1 
ATOM   1365  C CB  . ALA A 1 170 ? 34.507  25.629  19.993  1.00 63.40  ? 170 ALA A CB  1 
ATOM   1366  N N   . ASN A 1 171 ? 36.587  23.239  19.828  1.00 63.74  ? 171 ASN A N   1 
ATOM   1367  C CA  . ASN A 1 171 ? 36.903  21.830  19.825  1.00 62.28  ? 171 ASN A CA  1 
ATOM   1368  C C   . ASN A 1 171 ? 35.866  21.008  20.612  1.00 62.89  ? 171 ASN A C   1 
ATOM   1369  O O   . ASN A 1 171 ? 35.731  21.180  21.833  1.00 63.57  ? 171 ASN A O   1 
ATOM   1370  C CB  . ASN A 1 171 ? 38.283  21.644  20.416  1.00 62.73  ? 171 ASN A CB  1 
ATOM   1371  C CG  . ASN A 1 171 ? 38.693  20.196  20.325  1.00 61.99  ? 171 ASN A CG  1 
ATOM   1372  O OD1 . ASN A 1 171 ? 38.112  19.340  21.003  1.00 62.36  ? 171 ASN A OD1 1 
ATOM   1373  N ND2 . ASN A 1 171 ? 39.643  19.906  19.449  1.00 61.09  ? 171 ASN A ND2 1 
ATOM   1374  N N   . ALA A 1 172 ? 35.192  20.073  19.902  1.00 61.28  ? 172 ALA A N   1 
ATOM   1375  C CA  . ALA A 1 172 ? 34.149  19.206  20.439  1.00 61.63  ? 172 ALA A CA  1 
ATOM   1376  C C   . ALA A 1 172 ? 34.570  18.476  21.718  1.00 63.03  ? 172 ALA A C   1 
ATOM   1377  O O   . ALA A 1 172 ? 33.727  18.248  22.603  1.00 62.39  ? 172 ALA A O   1 
ATOM   1378  C CB  . ALA A 1 172 ? 33.752  18.184  19.386  1.00 61.00  ? 172 ALA A CB  1 
ATOM   1379  N N   . MET A 1 173 ? 35.867  18.099  21.777  1.00 63.25  ? 173 MET A N   1 
ATOM   1380  C CA  . MET A 1 173 ? 36.391  17.249  22.828  1.00 63.85  ? 173 MET A CA  1 
ATOM   1381  C C   . MET A 1 173 ? 36.819  18.005  24.089  1.00 64.90  ? 173 MET A C   1 
ATOM   1382  O O   . MET A 1 173 ? 36.953  17.369  25.129  1.00 65.11  ? 173 MET A O   1 
ATOM   1383  C CB  . MET A 1 173 ? 37.566  16.454  22.273  1.00 64.68  ? 173 MET A CB  1 
ATOM   1384  C CG  . MET A 1 173 ? 37.131  15.304  21.385  1.00 65.34  ? 173 MET A CG  1 
ATOM   1385  S SD  . MET A 1 173 ? 36.398  13.883  22.231  1.00 66.22  ? 173 MET A SD  1 
ATOM   1386  C CE  . MET A 1 173 ? 37.683  13.517  23.432  1.00 67.48  ? 173 MET A CE  1 
ATOM   1387  N N   . ILE A 1 174 ? 37.048  19.333  24.014  1.00 66.21  ? 174 ILE A N   1 
ATOM   1388  C CA  . ILE A 1 174 ? 37.301  20.160  25.197  1.00 67.33  ? 174 ILE A CA  1 
ATOM   1389  C C   . ILE A 1 174 ? 36.287  21.292  25.356  1.00 68.55  ? 174 ILE A C   1 
ATOM   1390  O O   . ILE A 1 174 ? 36.313  21.951  26.397  1.00 70.58  ? 174 ILE A O   1 
ATOM   1391  C CB  . ILE A 1 174 ? 38.702  20.798  25.205  1.00 67.62  ? 174 ILE A CB  1 
ATOM   1392  C CG1 . ILE A 1 174 ? 38.929  21.658  23.976  1.00 66.38  ? 174 ILE A CG1 1 
ATOM   1393  C CG2 . ILE A 1 174 ? 39.803  19.754  25.390  1.00 68.53  ? 174 ILE A CG2 1 
ATOM   1394  C CD1 . ILE A 1 174 ? 40.187  22.504  24.061  1.00 66.72  ? 174 ILE A CD1 1 
ATOM   1395  N N   . SER A 1 175 ? 35.475  21.605  24.337  1.00 67.67  ? 175 SER A N   1 
ATOM   1396  C CA  . SER A 1 175 ? 34.550  22.719  24.485  1.00 69.10  ? 175 SER A CA  1 
ATOM   1397  C C   . SER A 1 175 ? 33.098  22.226  24.341  1.00 68.51  ? 175 SER A C   1 
ATOM   1398  O O   . SER A 1 175 ? 32.184  22.950  23.930  1.00 69.09  ? 175 SER A O   1 
ATOM   1399  C CB  . SER A 1 175 ? 34.951  23.897  23.579  1.00 69.98  ? 175 SER A CB  1 
ATOM   1400  O OG  . SER A 1 175 ? 36.252  24.396  23.925  1.00 72.49  ? 175 SER A OG  1 
ATOM   1401  N N   . ASP A 1 176 ? 32.870  20.985  24.797  1.00 67.15  ? 176 ASP A N   1 
ATOM   1402  C CA  . ASP A 1 176 ? 31.551  20.367  24.802  1.00 65.20  ? 176 ASP A CA  1 
ATOM   1403  C C   . ASP A 1 176 ? 30.571  21.141  25.678  1.00 64.40  ? 176 ASP A C   1 
ATOM   1404  O O   . ASP A 1 176 ? 29.376  21.085  25.439  1.00 65.10  ? 176 ASP A O   1 
ATOM   1405  C CB  . ASP A 1 176 ? 31.640  18.923  25.282  1.00 65.14  ? 176 ASP A CB  1 
ATOM   1406  C CG  . ASP A 1 176 ? 32.374  18.673  26.593  1.00 65.43  ? 176 ASP A CG  1 
ATOM   1407  O OD1 . ASP A 1 176 ? 32.836  19.621  27.244  1.00 66.94  ? 176 ASP A OD1 1 
ATOM   1408  O OD2 . ASP A 1 176 ? 32.533  17.524  26.939  1.00 65.56  ? 176 ASP A OD2 1 
ATOM   1409  N N   . TYR A 1 177 ? 31.086  21.811  26.707  1.00 63.89  ? 177 TYR A N   1 
ATOM   1410  C CA  . TYR A 1 177 ? 30.294  22.484  27.721  1.00 64.92  ? 177 TYR A CA  1 
ATOM   1411  C C   . TYR A 1 177 ? 29.838  23.882  27.292  1.00 64.37  ? 177 TYR A C   1 
ATOM   1412  O O   . TYR A 1 177 ? 29.198  24.579  28.073  1.00 64.18  ? 177 TYR A O   1 
ATOM   1413  C CB  . TYR A 1 177 ? 31.168  22.700  28.964  1.00 66.51  ? 177 TYR A CB  1 
ATOM   1414  C CG  . TYR A 1 177 ? 32.352  23.655  28.773  1.00 66.68  ? 177 TYR A CG  1 
ATOM   1415  C CD1 . TYR A 1 177 ? 33.506  23.218  28.154  1.00 66.89  ? 177 TYR A CD1 1 
ATOM   1416  C CD2 . TYR A 1 177 ? 32.333  24.967  29.199  1.00 67.38  ? 177 TYR A CD2 1 
ATOM   1417  C CE1 . TYR A 1 177 ? 34.601  24.036  27.958  1.00 67.51  ? 177 TYR A CE1 1 
ATOM   1418  C CE2 . TYR A 1 177 ? 33.419  25.810  29.007  1.00 68.29  ? 177 TYR A CE2 1 
ATOM   1419  C CZ  . TYR A 1 177 ? 34.570  25.346  28.383  1.00 68.68  ? 177 TYR A CZ  1 
ATOM   1420  O OH  . TYR A 1 177 ? 35.729  26.074  28.157  1.00 68.79  ? 177 TYR A OH  1 
ATOM   1421  N N   . MET A 1 178 ? 30.239  24.323  26.099  1.00 63.60  ? 178 MET A N   1 
ATOM   1422  C CA  . MET A 1 178 ? 30.253  25.748  25.814  1.00 64.69  ? 178 MET A CA  1 
ATOM   1423  C C   . MET A 1 178 ? 28.947  26.120  25.135  1.00 65.01  ? 178 MET A C   1 
ATOM   1424  O O   . MET A 1 178 ? 28.525  25.398  24.238  1.00 65.10  ? 178 MET A O   1 
ATOM   1425  C CB  . MET A 1 178 ? 31.412  26.142  24.889  1.00 64.09  ? 178 MET A CB  1 
ATOM   1426  C CG  . MET A 1 178 ? 31.379  27.571  24.398  1.00 63.91  ? 178 MET A CG  1 
ATOM   1427  S SD  . MET A 1 178 ? 32.868  28.031  23.480  1.00 64.08  ? 178 MET A SD  1 
ATOM   1428  C CE  . MET A 1 178 ? 34.089  27.712  24.757  1.00 65.34  ? 178 MET A CE  1 
ATOM   1429  N N   . ASP A 1 179 ? 28.329  27.228  25.576  1.00 65.42  ? 179 ASP A N   1 
ATOM   1430  C CA  . ASP A 1 179 ? 27.179  27.770  24.879  1.00 64.82  ? 179 ASP A CA  1 
ATOM   1431  C C   . ASP A 1 179 ? 27.646  28.365  23.556  1.00 64.20  ? 179 ASP A C   1 
ATOM   1432  O O   . ASP A 1 179 ? 28.585  29.138  23.552  1.00 64.23  ? 179 ASP A O   1 
ATOM   1433  C CB  . ASP A 1 179 ? 26.483  28.839  25.691  1.00 65.32  ? 179 ASP A CB  1 
ATOM   1434  C CG  . ASP A 1 179 ? 25.196  29.353  25.066  1.00 65.23  ? 179 ASP A CG  1 
ATOM   1435  O OD1 . ASP A 1 179 ? 24.277  28.529  24.745  1.00 65.03  ? 179 ASP A OD1 1 
ATOM   1436  O OD2 . ASP A 1 179 ? 25.116  30.574  24.923  1.00 65.36  ? 179 ASP A OD2 1 
ATOM   1437  N N   . GLU A 1 180 ? 27.020  27.959  22.445  1.00 64.09  ? 180 GLU A N   1 
ATOM   1438  C CA  . GLU A 1 180 ? 27.249  28.574  21.147  1.00 63.57  ? 180 GLU A CA  1 
ATOM   1439  C C   . GLU A 1 180 ? 25.975  29.260  20.643  1.00 65.17  ? 180 GLU A C   1 
ATOM   1440  O O   . GLU A 1 180 ? 25.857  29.597  19.460  1.00 65.12  ? 180 GLU A O   1 
ATOM   1441  C CB  . GLU A 1 180 ? 27.656  27.543  20.103  1.00 61.64  ? 180 GLU A CB  1 
ATOM   1442  C CG  . GLU A 1 180 ? 29.022  26.944  20.360  1.00 61.05  ? 180 GLU A CG  1 
ATOM   1443  C CD  . GLU A 1 180 ? 29.474  26.091  19.193  1.00 60.30  ? 180 GLU A CD  1 
ATOM   1444  O OE1 . GLU A 1 180 ? 28.684  26.005  18.210  1.00 58.86  ? 180 GLU A OE1 1 
ATOM   1445  O OE2 . GLU A 1 180 ? 30.612  25.515  19.291  1.00 60.19  ? 180 GLU A OE2 1 
ATOM   1446  N N   . SER A 1 181 ? 25.011  29.496  21.535  1.00 66.44  ? 181 SER A N   1 
ATOM   1447  C CA  . SER A 1 181 ? 23.756  30.048  21.074  1.00 67.69  ? 181 SER A CA  1 
ATOM   1448  C C   . SER A 1 181 ? 23.944  31.503  20.636  1.00 67.87  ? 181 SER A C   1 
ATOM   1449  O O   . SER A 1 181 ? 23.126  32.040  19.902  1.00 68.10  ? 181 SER A O   1 
ATOM   1450  C CB  . SER A 1 181 ? 22.703  29.900  22.120  1.00 69.83  ? 181 SER A CB  1 
ATOM   1451  O OG  . SER A 1 181 ? 23.184  30.434  23.339  1.00 71.69  ? 181 SER A OG  1 
ATOM   1452  N N   . ILE A 1 182 ? 25.033  32.155  21.045  1.00 68.06  ? 182 ILE A N   1 
ATOM   1453  C CA  . ILE A 1 182 ? 25.245  33.531  20.620  1.00 68.65  ? 182 ILE A CA  1 
ATOM   1454  C C   . ILE A 1 182 ? 25.639  33.593  19.143  1.00 68.05  ? 182 ILE A C   1 
ATOM   1455  O O   . ILE A 1 182 ? 25.568  34.678  18.564  1.00 69.14  ? 182 ILE A O   1 
ATOM   1456  C CB  . ILE A 1 182 ? 26.264  34.278  21.497  1.00 69.41  ? 182 ILE A CB  1 
ATOM   1457  C CG1 . ILE A 1 182 ? 27.630  33.638  21.421  1.00 70.41  ? 182 ILE A CG1 1 
ATOM   1458  C CG2 . ILE A 1 182 ? 25.788  34.403  22.943  1.00 70.03  ? 182 ILE A CG2 1 
ATOM   1459  C CD1 . ILE A 1 182 ? 28.707  34.455  22.121  1.00 72.48  ? 182 ILE A CD1 1 
ATOM   1460  N N   . PHE A 1 183 ? 26.036  32.460  18.537  1.00 66.79  ? 183 PHE A N   1 
ATOM   1461  C CA  . PHE A 1 183 ? 26.561  32.446  17.173  1.00 66.14  ? 183 PHE A CA  1 
ATOM   1462  C C   . PHE A 1 183 ? 25.418  32.137  16.212  1.00 64.30  ? 183 PHE A C   1 
ATOM   1463  O O   . PHE A 1 183 ? 24.430  31.567  16.639  1.00 65.34  ? 183 PHE A O   1 
ATOM   1464  C CB  . PHE A 1 183 ? 27.718  31.447  16.972  1.00 66.90  ? 183 PHE A CB  1 
ATOM   1465  C CG  . PHE A 1 183 ? 28.896  31.726  17.898  1.00 68.48  ? 183 PHE A CG  1 
ATOM   1466  C CD1 . PHE A 1 183 ? 29.857  32.690  17.575  1.00 70.74  ? 183 PHE A CD1 1 
ATOM   1467  C CD2 . PHE A 1 183 ? 28.985  31.101  19.133  1.00 68.38  ? 183 PHE A CD2 1 
ATOM   1468  C CE1 . PHE A 1 183 ? 30.904  32.982  18.446  1.00 71.04  ? 183 PHE A CE1 1 
ATOM   1469  C CE2 . PHE A 1 183 ? 30.012  31.411  20.007  1.00 69.67  ? 183 PHE A CE2 1 
ATOM   1470  C CZ  . PHE A 1 183 ? 30.971  32.346  19.666  1.00 70.69  ? 183 PHE A CZ  1 
ATOM   1471  N N   . ASP A 1 184 ? 25.600  32.472  14.927  1.00 62.48  ? 184 ASP A N   1 
ATOM   1472  C CA  . ASP A 1 184 ? 24.656  32.195  13.856  1.00 61.52  ? 184 ASP A CA  1 
ATOM   1473  C C   . ASP A 1 184 ? 24.677  30.713  13.429  1.00 60.95  ? 184 ASP A C   1 
ATOM   1474  O O   . ASP A 1 184 ? 23.727  30.205  12.844  1.00 60.60  ? 184 ASP A O   1 
ATOM   1475  C CB  . ASP A 1 184 ? 24.921  33.129  12.688  1.00 61.31  ? 184 ASP A CB  1 
ATOM   1476  C CG  . ASP A 1 184 ? 24.932  34.614  13.025  1.00 62.33  ? 184 ASP A CG  1 
ATOM   1477  O OD1 . ASP A 1 184 ? 23.906  35.074  13.596  1.00 63.47  ? 184 ASP A OD1 1 
ATOM   1478  O OD2 . ASP A 1 184 ? 25.954  35.302  12.710  1.00 61.48  ? 184 ASP A OD2 1 
ATOM   1479  N N   . VAL A 1 185 ? 25.764  29.983  13.705  1.00 60.82  ? 185 VAL A N   1 
ATOM   1480  C CA  . VAL A 1 185 ? 25.874  28.577  13.334  1.00 59.37  ? 185 VAL A CA  1 
ATOM   1481  C C   . VAL A 1 185 ? 26.535  27.821  14.481  1.00 59.34  ? 185 VAL A C   1 
ATOM   1482  O O   . VAL A 1 185 ? 27.304  28.389  15.235  1.00 59.81  ? 185 VAL A O   1 
ATOM   1483  C CB  . VAL A 1 185 ? 26.700  28.511  12.038  1.00 58.52  ? 185 VAL A CB  1 
ATOM   1484  C CG1 . VAL A 1 185 ? 27.158  27.122  11.706  1.00 58.09  ? 185 VAL A CG1 1 
ATOM   1485  C CG2 . VAL A 1 185 ? 25.958  29.066  10.844  1.00 59.00  ? 185 VAL A CG2 1 
ATOM   1486  N N   . TYR A 1 186 ? 26.211  26.539  14.634  1.00 60.10  ? 186 TYR A N   1 
ATOM   1487  C CA  . TYR A 1 186 ? 26.915  25.664  15.563  1.00 60.13  ? 186 TYR A CA  1 
ATOM   1488  C C   . TYR A 1 186 ? 28.126  25.111  14.828  1.00 58.64  ? 186 TYR A C   1 
ATOM   1489  O O   . TYR A 1 186 ? 27.986  24.639  13.705  1.00 58.12  ? 186 TYR A O   1 
ATOM   1490  C CB  . TYR A 1 186 ? 25.956  24.576  16.077  1.00 60.78  ? 186 TYR A CB  1 
ATOM   1491  C CG  . TYR A 1 186 ? 24.877  25.115  17.008  1.00 61.93  ? 186 TYR A CG  1 
ATOM   1492  C CD1 . TYR A 1 186 ? 25.208  25.893  18.103  1.00 63.12  ? 186 TYR A CD1 1 
ATOM   1493  C CD2 . TYR A 1 186 ? 23.538  24.868  16.788  1.00 63.31  ? 186 TYR A CD2 1 
ATOM   1494  C CE1 . TYR A 1 186 ? 24.253  26.417  18.955  1.00 65.25  ? 186 TYR A CE1 1 
ATOM   1495  C CE2 . TYR A 1 186 ? 22.561  25.390  17.628  1.00 66.01  ? 186 TYR A CE2 1 
ATOM   1496  C CZ  . TYR A 1 186 ? 22.906  26.193  18.712  1.00 66.66  ? 186 TYR A CZ  1 
ATOM   1497  O OH  . TYR A 1 186 ? 21.965  26.753  19.562  1.00 65.93  ? 186 TYR A OH  1 
ATOM   1498  N N   . ALA A 1 187 ? 29.309  25.188  15.434  1.00 58.59  ? 187 ALA A N   1 
ATOM   1499  C CA  . ALA A 1 187 ? 30.501  24.680  14.760  1.00 58.17  ? 187 ALA A CA  1 
ATOM   1500  C C   . ALA A 1 187 ? 31.498  24.122  15.764  1.00 58.55  ? 187 ALA A C   1 
ATOM   1501  O O   . ALA A 1 187 ? 31.566  24.571  16.897  1.00 58.11  ? 187 ALA A O   1 
ATOM   1502  C CB  . ALA A 1 187 ? 31.115  25.752  13.904  1.00 58.07  ? 187 ALA A CB  1 
ATOM   1503  N N   . TYR A 1 188 ? 32.235  23.096  15.325  1.00 60.63  ? 188 TYR A N   1 
ATOM   1504  C CA  . TYR A 1 188 ? 33.108  22.286  16.179  1.00 61.46  ? 188 TYR A CA  1 
ATOM   1505  C C   . TYR A 1 188 ? 34.189  21.664  15.316  1.00 60.51  ? 188 TYR A C   1 
ATOM   1506  O O   . TYR A 1 188 ? 33.950  21.332  14.162  1.00 59.75  ? 188 TYR A O   1 
ATOM   1507  C CB  . TYR A 1 188 ? 32.496  21.095  16.933  1.00 62.38  ? 188 TYR A CB  1 
ATOM   1508  C CG  . TYR A 1 188 ? 31.497  21.497  18.011  1.00 64.48  ? 188 TYR A CG  1 
ATOM   1509  C CD1 . TYR A 1 188 ? 31.941  22.019  19.219  1.00 66.35  ? 188 TYR A CD1 1 
ATOM   1510  C CD2 . TYR A 1 188 ? 30.125  21.397  17.817  1.00 64.88  ? 188 TYR A CD2 1 
ATOM   1511  C CE1 . TYR A 1 188 ? 31.054  22.452  20.196  1.00 68.24  ? 188 TYR A CE1 1 
ATOM   1512  C CE2 . TYR A 1 188 ? 29.229  21.790  18.803  1.00 67.09  ? 188 TYR A CE2 1 
ATOM   1513  C CZ  . TYR A 1 188 ? 29.690  22.329  19.998  1.00 68.81  ? 188 TYR A CZ  1 
ATOM   1514  O OH  . TYR A 1 188 ? 28.859  22.738  21.010  1.00 69.08  ? 188 TYR A OH  1 
ATOM   1515  N N   . ASN A 1 189 ? 35.369  21.538  15.913  1.00 62.14  ? 189 ASN A N   1 
ATOM   1516  C CA  . ASN A 1 189 ? 36.478  20.776  15.373  1.00 62.34  ? 189 ASN A CA  1 
ATOM   1517  C C   . ASN A 1 189 ? 36.351  19.362  15.936  1.00 65.30  ? 189 ASN A C   1 
ATOM   1518  O O   . ASN A 1 189 ? 36.476  19.160  17.148  1.00 70.21  ? 189 ASN A O   1 
ATOM   1519  C CB  . ASN A 1 189 ? 37.817  21.398  15.761  1.00 62.25  ? 189 ASN A CB  1 
ATOM   1520  C CG  . ASN A 1 189 ? 38.118  22.737  15.104  1.00 62.34  ? 189 ASN A CG  1 
ATOM   1521  O OD1 . ASN A 1 189 ? 37.752  22.981  13.945  1.00 61.90  ? 189 ASN A OD1 1 
ATOM   1522  N ND2 . ASN A 1 189 ? 38.837  23.605  15.808  1.00 62.26  ? 189 ASN A ND2 1 
ATOM   1523  N N   . CYS A 1 190 ? 36.100  18.382  15.060  1.00 64.97  ? 190 CYS A N   1 
ATOM   1524  C CA  . CYS A 1 190 ? 35.756  17.036  15.490  1.00 65.21  ? 190 CYS A CA  1 
ATOM   1525  C C   . CYS A 1 190 ? 36.894  16.052  15.173  1.00 64.30  ? 190 CYS A C   1 
ATOM   1526  O O   . CYS A 1 190 ? 37.329  15.938  14.028  1.00 62.45  ? 190 CYS A O   1 
ATOM   1527  C CB  . CYS A 1 190 ? 34.419  16.678  14.859  1.00 64.17  ? 190 CYS A CB  1 
ATOM   1528  S SG  . CYS A 1 190 ? 33.168  17.947  15.180  1.00 65.83  ? 190 CYS A SG  1 
ATOM   1529  N N   . TYR A 1 191 ? 37.340  15.301  16.187  1.00 63.58  ? 191 TYR A N   1 
ATOM   1530  C CA  . TYR A 1 191 ? 38.413  14.336  15.993  1.00 62.43  ? 191 TYR A CA  1 
ATOM   1531  C C   . TYR A 1 191 ? 38.069  13.060  16.730  1.00 60.24  ? 191 TYR A C   1 
ATOM   1532  O O   . TYR A 1 191 ? 37.801  13.055  17.926  1.00 59.47  ? 191 TYR A O   1 
ATOM   1533  C CB  . TYR A 1 191 ? 39.816  14.802  16.427  1.00 63.84  ? 191 TYR A CB  1 
ATOM   1534  C CG  . TYR A 1 191 ? 40.395  15.885  15.528  1.00 63.74  ? 191 TYR A CG  1 
ATOM   1535  C CD1 . TYR A 1 191 ? 41.036  15.568  14.334  1.00 63.20  ? 191 TYR A CD1 1 
ATOM   1536  C CD2 . TYR A 1 191 ? 40.207  17.217  15.831  1.00 64.56  ? 191 TYR A CD2 1 
ATOM   1537  C CE1 . TYR A 1 191 ? 41.521  16.545  13.488  1.00 63.63  ? 191 TYR A CE1 1 
ATOM   1538  C CE2 . TYR A 1 191 ? 40.676  18.208  14.987  1.00 65.41  ? 191 TYR A CE2 1 
ATOM   1539  C CZ  . TYR A 1 191 ? 41.344  17.876  13.818  1.00 65.37  ? 191 TYR A CZ  1 
ATOM   1540  O OH  . TYR A 1 191 ? 41.798  18.882  12.998  1.00 66.67  ? 191 TYR A OH  1 
ATOM   1541  N N   . ASP A 1 192 ? 38.174  11.978  15.980  1.00 59.59  ? 192 ASP A N   1 
ATOM   1542  C CA  . ASP A 1 192 ? 37.750  10.663  16.428  1.00 59.58  ? 192 ASP A CA  1 
ATOM   1543  C C   . ASP A 1 192 ? 38.961  9.781   16.686  1.00 59.88  ? 192 ASP A C   1 
ATOM   1544  O O   . ASP A 1 192 ? 39.438  9.112   15.772  1.00 58.89  ? 192 ASP A O   1 
ATOM   1545  C CB  . ASP A 1 192 ? 36.930  9.969   15.360  1.00 58.86  ? 192 ASP A CB  1 
ATOM   1546  C CG  . ASP A 1 192 ? 36.474  8.581   15.742  1.00 59.25  ? 192 ASP A CG  1 
ATOM   1547  O OD1 . ASP A 1 192 ? 36.835  8.129   16.852  1.00 59.70  ? 192 ASP A OD1 1 
ATOM   1548  O OD2 . ASP A 1 192 ? 35.730  8.000   14.938  1.00 60.04  ? 192 ASP A OD2 1 
ATOM   1549  N N   . HIS A 1 193 ? 39.423  9.805   17.941  1.00 60.93  ? 193 HIS A N   1 
ATOM   1550  C CA  . HIS A 1 193 ? 40.523  8.984   18.419  1.00 61.62  ? 193 HIS A CA  1 
ATOM   1551  C C   . HIS A 1 193 ? 39.979  7.890   19.341  1.00 60.88  ? 193 HIS A C   1 
ATOM   1552  O O   . HIS A 1 193 ? 40.607  7.515   20.307  1.00 61.28  ? 193 HIS A O   1 
ATOM   1553  C CB  . HIS A 1 193 ? 41.579  9.869   19.112  1.00 63.01  ? 193 HIS A CB  1 
ATOM   1554  C CG  . HIS A 1 193 ? 42.130  10.985  18.285  1.00 64.51  ? 193 HIS A CG  1 
ATOM   1555  N ND1 . HIS A 1 193 ? 41.945  12.316  18.610  1.00 65.45  ? 193 HIS A ND1 1 
ATOM   1556  C CD2 . HIS A 1 193 ? 42.884  10.993  17.177  1.00 66.00  ? 193 HIS A CD2 1 
ATOM   1557  C CE1 . HIS A 1 193 ? 42.573  13.086  17.725  1.00 65.37  ? 193 HIS A CE1 1 
ATOM   1558  N NE2 . HIS A 1 193 ? 43.159  12.319  16.845  1.00 66.01  ? 193 HIS A NE2 1 
ATOM   1559  N N   . ASN A 1 194 ? 38.765  7.412   19.085  1.00 60.54  ? 194 ASN A N   1 
ATOM   1560  C CA  . ASN A 1 194 ? 38.147  6.347   19.863  1.00 60.34  ? 194 ASN A CA  1 
ATOM   1561  C C   . ASN A 1 194 ? 38.624  6.364   21.316  1.00 60.91  ? 194 ASN A C   1 
ATOM   1562  O O   . ASN A 1 194 ? 39.183  5.386   21.773  1.00 61.38  ? 194 ASN A O   1 
ATOM   1563  C CB  . ASN A 1 194 ? 38.410  5.019   19.175  1.00 60.38  ? 194 ASN A CB  1 
ATOM   1564  C CG  . ASN A 1 194 ? 37.756  3.875   19.902  1.00 61.94  ? 194 ASN A CG  1 
ATOM   1565  O OD1 . ASN A 1 194 ? 36.522  3.775   19.954  1.00 64.47  ? 194 ASN A OD1 1 
ATOM   1566  N ND2 . ASN A 1 194 ? 38.542  3.005   20.504  1.00 62.51  ? 194 ASN A ND2 1 
ATOM   1567  N N   . GLU A 1 195 ? 38.391  7.464   22.042  1.00 61.07  ? 195 GLU A N   1 
ATOM   1568  C CA  . GLU A 1 195 ? 38.885  7.624   23.401  1.00 62.46  ? 195 GLU A CA  1 
ATOM   1569  C C   . GLU A 1 195 ? 38.033  8.654   24.137  1.00 63.56  ? 195 GLU A C   1 
ATOM   1570  O O   . GLU A 1 195 ? 37.303  9.402   23.496  1.00 63.16  ? 195 GLU A O   1 
ATOM   1571  C CB  . GLU A 1 195 ? 40.331  8.129   23.370  1.00 62.46  ? 195 GLU A CB  1 
ATOM   1572  C CG  . GLU A 1 195 ? 40.512  9.554   22.845  1.00 61.18  ? 195 GLU A CG  1 
ATOM   1573  C CD  . GLU A 1 195 ? 41.920  10.120  22.940  1.00 61.33  ? 195 GLU A CD  1 
ATOM   1574  O OE1 . GLU A 1 195 ? 42.839  9.374   23.298  1.00 62.32  ? 195 GLU A OE1 1 
ATOM   1575  O OE2 . GLU A 1 195 ? 42.129  11.307  22.666  1.00 60.74  ? 195 GLU A OE2 1 
ATOM   1576  N N   . GLY A 1 196 ? 38.167  8.739   25.470  1.00 65.48  ? 196 GLY A N   1 
ATOM   1577  C CA  . GLY A 1 196 ? 37.330  9.638   26.260  1.00 65.91  ? 196 GLY A CA  1 
ATOM   1578  C C   . GLY A 1 196 ? 35.864  9.561   25.814  1.00 65.44  ? 196 GLY A C   1 
ATOM   1579  O O   . GLY A 1 196 ? 35.259  8.495   25.748  1.00 64.88  ? 196 GLY A O   1 
ATOM   1580  N N   . GLN A 1 197 ? 35.312  10.700  25.422  1.00 65.43  ? 197 GLN A N   1 
ATOM   1581  C CA  . GLN A 1 197 ? 33.932  10.764  24.968  1.00 65.43  ? 197 GLN A CA  1 
ATOM   1582  C C   . GLN A 1 197 ? 33.697  9.867   23.748  1.00 64.90  ? 197 GLN A C   1 
ATOM   1583  O O   . GLN A 1 197 ? 32.565  9.404   23.591  1.00 67.34  ? 197 GLN A O   1 
ATOM   1584  C CB  . GLN A 1 197 ? 33.498  12.194  24.604  1.00 64.96  ? 197 GLN A CB  1 
ATOM   1585  C CG  . GLN A 1 197 ? 33.439  13.173  25.773  1.00 65.26  ? 197 GLN A CG  1 
ATOM   1586  C CD  . GLN A 1 197 ? 34.746  13.899  26.030  1.00 65.38  ? 197 GLN A CD  1 
ATOM   1587  O OE1 . GLN A 1 197 ? 35.821  13.299  26.087  1.00 63.74  ? 197 GLN A OE1 1 
ATOM   1588  N NE2 . GLN A 1 197 ? 34.669  15.214  26.209  1.00 66.24  ? 197 GLN A NE2 1 
ATOM   1589  N N   . THR A 1 198 ? 34.699  9.646   22.871  1.00 63.53  ? 198 THR A N   1 
ATOM   1590  C CA  . THR A 1 198 ? 34.414  9.076   21.551  1.00 62.86  ? 198 THR A CA  1 
ATOM   1591  C C   . THR A 1 198 ? 34.574  7.561   21.559  1.00 63.30  ? 198 THR A C   1 
ATOM   1592  O O   . THR A 1 198 ? 34.368  6.899   20.533  1.00 62.11  ? 198 THR A O   1 
ATOM   1593  C CB  . THR A 1 198 ? 35.262  9.692   20.441  1.00 62.19  ? 198 THR A CB  1 
ATOM   1594  O OG1 . THR A 1 198 ? 36.610  9.501   20.851  1.00 62.65  ? 198 THR A OG1 1 
ATOM   1595  C CG2 . THR A 1 198 ? 34.886  11.143  20.189  1.00 61.76  ? 198 THR A CG2 1 
ATOM   1596  N N   . ALA A 1 199 ? 34.956  7.053   22.734  1.00 64.80  ? 199 ALA A N   1 
ATOM   1597  C CA  . ALA A 1 199 ? 34.984  5.634   23.030  1.00 65.14  ? 199 ALA A CA  1 
ATOM   1598  C C   . ALA A 1 199 ? 33.688  5.212   23.716  1.00 66.30  ? 199 ALA A C   1 
ATOM   1599  O O   . ALA A 1 199 ? 33.289  4.049   23.604  1.00 66.14  ? 199 ALA A O   1 
ATOM   1600  C CB  . ALA A 1 199 ? 36.154  5.362   23.921  1.00 65.98  ? 199 ALA A CB  1 
ATOM   1601  N N   . THR A 1 200 ? 33.065  6.150   24.455  1.00 66.69  ? 200 THR A N   1 
ATOM   1602  C CA  . THR A 1 200 ? 31.804  5.871   25.125  1.00 67.79  ? 200 THR A CA  1 
ATOM   1603  C C   . THR A 1 200 ? 30.674  5.985   24.109  1.00 67.11  ? 200 THR A C   1 
ATOM   1604  O O   . THR A 1 200 ? 29.975  5.013   23.854  1.00 66.14  ? 200 THR A O   1 
ATOM   1605  C CB  . THR A 1 200 ? 31.571  6.789   26.327  1.00 68.70  ? 200 THR A CB  1 
ATOM   1606  O OG1 . THR A 1 200 ? 31.470  8.130   25.845  1.00 67.69  ? 200 THR A OG1 1 
ATOM   1607  C CG2 . THR A 1 200 ? 32.644  6.611   27.387  1.00 69.52  ? 200 THR A CG2 1 
ATOM   1608  N N   . MET A 1 201 ? 30.501  7.174   23.523  1.00 66.93  ? 201 MET A N   1 
ATOM   1609  C CA  . MET A 1 201 ? 29.300  7.420   22.735  1.00 67.32  ? 201 MET A CA  1 
ATOM   1610  C C   . MET A 1 201 ? 29.528  6.982   21.291  1.00 67.81  ? 201 MET A C   1 
ATOM   1611  O O   . MET A 1 201 ? 28.610  6.558   20.590  1.00 70.42  ? 201 MET A O   1 
ATOM   1612  C CB  . MET A 1 201 ? 28.884  8.887   22.833  1.00 65.80  ? 201 MET A CB  1 
ATOM   1613  C CG  . MET A 1 201 ? 28.453  9.256   24.234  1.00 66.40  ? 201 MET A CG  1 
ATOM   1614  S SD  . MET A 1 201 ? 28.478  11.024  24.580  1.00 66.35  ? 201 MET A SD  1 
ATOM   1615  C CE  . MET A 1 201 ? 30.121  11.371  25.213  1.00 67.49  ? 201 MET A CE  1 
ATOM   1616  N N   . GLY A 1 202 ? 30.782  7.034   20.868  1.00 67.21  ? 202 GLY A N   1 
ATOM   1617  C CA  . GLY A 1 202 ? 31.080  6.876   19.463  1.00 66.09  ? 202 GLY A CA  1 
ATOM   1618  C C   . GLY A 1 202 ? 31.039  8.244   18.811  1.00 64.57  ? 202 GLY A C   1 
ATOM   1619  O O   . GLY A 1 202 ? 30.556  9.191   19.409  1.00 67.12  ? 202 GLY A O   1 
ATOM   1620  N N   . PHE A 1 203 ? 31.576  8.343   17.603  1.00 62.56  ? 203 PHE A N   1 
ATOM   1621  C CA  . PHE A 1 203 ? 31.795  9.636   16.991  1.00 60.64  ? 203 PHE A CA  1 
ATOM   1622  C C   . PHE A 1 203 ? 30.435  10.230  16.617  1.00 60.51  ? 203 PHE A C   1 
ATOM   1623  O O   . PHE A 1 203 ? 30.065  11.283  17.117  1.00 61.24  ? 203 PHE A O   1 
ATOM   1624  C CB  . PHE A 1 203 ? 32.784  9.425   15.843  1.00 58.99  ? 203 PHE A CB  1 
ATOM   1625  C CG  . PHE A 1 203 ? 33.430  10.715  15.376  1.00 58.01  ? 203 PHE A CG  1 
ATOM   1626  C CD1 . PHE A 1 203 ? 33.921  11.633  16.290  1.00 58.03  ? 203 PHE A CD1 1 
ATOM   1627  C CD2 . PHE A 1 203 ? 33.521  11.001  14.023  1.00 57.10  ? 203 PHE A CD2 1 
ATOM   1628  C CE1 . PHE A 1 203 ? 34.518  12.791  15.853  1.00 58.24  ? 203 PHE A CE1 1 
ATOM   1629  C CE2 . PHE A 1 203 ? 34.123  12.150  13.589  1.00 57.00  ? 203 PHE A CE2 1 
ATOM   1630  C CZ  . PHE A 1 203 ? 34.610  13.051  14.504  1.00 58.10  ? 203 PHE A CZ  1 
ATOM   1631  N N   . LYS A 1 204 ? 29.663  9.542   15.776  1.00 59.85  ? 204 LYS A N   1 
ATOM   1632  C CA  . LYS A 1 204 ? 28.359  10.046  15.365  1.00 59.95  ? 204 LYS A CA  1 
ATOM   1633  C C   . LYS A 1 204 ? 27.560  10.565  16.560  1.00 60.45  ? 204 LYS A C   1 
ATOM   1634  O O   . LYS A 1 204 ? 27.159  11.720  16.567  1.00 61.97  ? 204 LYS A O   1 
ATOM   1635  C CB  . LYS A 1 204 ? 27.519  8.942   14.720  1.00 60.14  ? 204 LYS A CB  1 
ATOM   1636  C CG  . LYS A 1 204 ? 26.163  9.304   14.213  1.00 60.05  ? 204 LYS A CG  1 
ATOM   1637  C CD  . LYS A 1 204 ? 25.051  8.381   14.682  1.00 61.09  ? 204 LYS A CD  1 
ATOM   1638  C CE  . LYS A 1 204 ? 24.151  7.897   13.573  1.00 61.48  ? 204 LYS A CE  1 
ATOM   1639  N NZ  . LYS A 1 204 ? 22.936  7.218   14.054  1.00 61.92  ? 204 LYS A NZ  1 
ATOM   1640  N N   . ASP A 1 205 ? 27.308  9.725   17.561  1.00 60.88  ? 205 ASP A N   1 
ATOM   1641  C CA  . ASP A 1 205 ? 26.391  10.083  18.629  1.00 61.93  ? 205 ASP A CA  1 
ATOM   1642  C C   . ASP A 1 205 ? 26.955  11.174  19.526  1.00 62.75  ? 205 ASP A C   1 
ATOM   1643  O O   . ASP A 1 205 ? 26.196  12.023  20.001  1.00 63.93  ? 205 ASP A O   1 
ATOM   1644  C CB  . ASP A 1 205 ? 26.052  8.910   19.524  1.00 62.80  ? 205 ASP A CB  1 
ATOM   1645  C CG  . ASP A 1 205 ? 25.153  7.891   18.861  1.00 62.64  ? 205 ASP A CG  1 
ATOM   1646  O OD1 . ASP A 1 205 ? 24.982  8.039   17.633  1.00 61.40  ? 205 ASP A OD1 1 
ATOM   1647  O OD2 . ASP A 1 205 ? 24.640  7.000   19.587  1.00 63.49  ? 205 ASP A OD2 1 
ATOM   1648  N N   . TYR A 1 206 ? 28.267  11.126  19.786  1.00 62.75  ? 206 TYR A N   1 
ATOM   1649  C CA  . TYR A 1 206 ? 28.881  12.136  20.640  1.00 63.47  ? 206 TYR A CA  1 
ATOM   1650  C C   . TYR A 1 206 ? 28.512  13.532  20.145  1.00 62.46  ? 206 TYR A C   1 
ATOM   1651  O O   . TYR A 1 206 ? 27.848  14.279  20.863  1.00 61.91  ? 206 TYR A O   1 
ATOM   1652  C CB  . TYR A 1 206 ? 30.404  12.079  20.697  1.00 62.84  ? 206 TYR A CB  1 
ATOM   1653  C CG  . TYR A 1 206 ? 31.011  13.179  21.551  1.00 63.92  ? 206 TYR A CG  1 
ATOM   1654  C CD1 . TYR A 1 206 ? 30.535  13.453  22.827  1.00 65.01  ? 206 TYR A CD1 1 
ATOM   1655  C CD2 . TYR A 1 206 ? 32.087  13.921  21.086  1.00 64.04  ? 206 TYR A CD2 1 
ATOM   1656  C CE1 . TYR A 1 206 ? 31.112  14.436  23.616  1.00 66.25  ? 206 TYR A CE1 1 
ATOM   1657  C CE2 . TYR A 1 206 ? 32.677  14.895  21.868  1.00 65.46  ? 206 TYR A CE2 1 
ATOM   1658  C CZ  . TYR A 1 206 ? 32.183  15.159  23.130  1.00 66.67  ? 206 TYR A CZ  1 
ATOM   1659  O OH  . TYR A 1 206 ? 32.773  16.144  23.869  1.00 70.13  ? 206 TYR A OH  1 
ATOM   1660  N N   . ILE A 1 207 ? 28.927  13.805  18.903  1.00 61.99  ? 207 ILE A N   1 
ATOM   1661  C CA  . ILE A 1 207 ? 28.680  15.042  18.193  1.00 63.31  ? 207 ILE A CA  1 
ATOM   1662  C C   . ILE A 1 207 ? 27.176  15.301  18.084  1.00 66.43  ? 207 ILE A C   1 
ATOM   1663  O O   . ILE A 1 207 ? 26.682  16.397  18.392  1.00 68.95  ? 207 ILE A O   1 
ATOM   1664  C CB  . ILE A 1 207 ? 29.335  14.952  16.808  1.00 63.41  ? 207 ILE A CB  1 
ATOM   1665  C CG1 . ILE A 1 207 ? 30.892  14.738  16.871  1.00 63.40  ? 207 ILE A CG1 1 
ATOM   1666  C CG2 . ILE A 1 207 ? 28.978  16.174  15.971  1.00 63.71  ? 207 ILE A CG2 1 
ATOM   1667  C CD1 . ILE A 1 207 ? 31.638  15.638  17.838  1.00 63.64  ? 207 ILE A CD1 1 
ATOM   1668  N N   . LYS A 1 208 ? 26.427  14.278  17.662  1.00 67.26  ? 208 LYS A N   1 
ATOM   1669  C CA  . LYS A 1 208 ? 24.989  14.429  17.502  1.00 67.94  ? 208 LYS A CA  1 
ATOM   1670  C C   . LYS A 1 208 ? 24.330  14.919  18.795  1.00 68.47  ? 208 LYS A C   1 
ATOM   1671  O O   . LYS A 1 208 ? 23.355  15.671  18.758  1.00 67.51  ? 208 LYS A O   1 
ATOM   1672  C CB  . LYS A 1 208 ? 24.403  13.090  17.072  1.00 68.28  ? 208 LYS A CB  1 
ATOM   1673  C CG  . LYS A 1 208 ? 22.933  13.165  16.790  1.00 70.47  ? 208 LYS A CG  1 
ATOM   1674  C CD  . LYS A 1 208 ? 22.415  11.891  16.167  1.00 71.01  ? 208 LYS A CD  1 
ATOM   1675  C CE  . LYS A 1 208 ? 22.224  10.859  17.230  1.00 74.88  ? 208 LYS A CE  1 
ATOM   1676  N NZ  . LYS A 1 208 ? 20.932  11.030  17.920  1.00 78.66  ? 208 LYS A NZ  1 
ATOM   1677  N N   . GLY A 1 209 ? 24.862  14.459  19.933  1.00 68.86  ? 209 GLY A N   1 
ATOM   1678  C CA  . GLY A 1 209 ? 24.308  14.783  21.236  1.00 69.43  ? 209 GLY A CA  1 
ATOM   1679  C C   . GLY A 1 209 ? 24.631  16.215  21.633  1.00 69.18  ? 209 GLY A C   1 
ATOM   1680  O O   . GLY A 1 209 ? 23.939  16.791  22.467  1.00 68.14  ? 209 GLY A O   1 
ATOM   1681  N N   . LEU A 1 210 ? 25.712  16.762  21.062  1.00 70.51  ? 210 LEU A N   1 
ATOM   1682  C CA  . LEU A 1 210 ? 26.039  18.171  21.261  1.00 72.31  ? 210 LEU A CA  1 
ATOM   1683  C C   . LEU A 1 210 ? 25.052  19.019  20.458  1.00 72.17  ? 210 LEU A C   1 
ATOM   1684  O O   . LEU A 1 210 ? 24.496  19.997  20.951  1.00 71.92  ? 210 LEU A O   1 
ATOM   1685  C CB  . LEU A 1 210 ? 27.497  18.457  20.907  1.00 71.97  ? 210 LEU A CB  1 
ATOM   1686  C CG  . LEU A 1 210 ? 28.533  17.687  21.741  1.00 74.73  ? 210 LEU A CG  1 
ATOM   1687  C CD1 . LEU A 1 210 ? 29.966  18.028  21.336  1.00 76.87  ? 210 LEU A CD1 1 
ATOM   1688  C CD2 . LEU A 1 210 ? 28.391  17.902  23.238  1.00 75.64  ? 210 LEU A CD2 1 
ATOM   1689  N N   . ASN A 1 211 ? 24.786  18.579  19.231  1.00 71.61  ? 211 ASN A N   1 
ATOM   1690  C CA  . ASN A 1 211 ? 23.817  19.227  18.369  1.00 70.51  ? 211 ASN A CA  1 
ATOM   1691  C C   . ASN A 1 211 ? 22.433  19.246  19.021  1.00 72.63  ? 211 ASN A C   1 
ATOM   1692  O O   . ASN A 1 211 ? 21.717  20.251  18.951  1.00 73.05  ? 211 ASN A O   1 
ATOM   1693  C CB  . ASN A 1 211 ? 23.794  18.524  17.023  1.00 69.14  ? 211 ASN A CB  1 
ATOM   1694  C CG  . ASN A 1 211 ? 23.574  19.516  15.923  1.00 69.52  ? 211 ASN A CG  1 
ATOM   1695  O OD1 . ASN A 1 211 ? 24.153  20.611  15.964  1.00 73.84  ? 211 ASN A OD1 1 
ATOM   1696  N ND2 . ASN A 1 211 ? 22.744  19.168  14.960  1.00 69.36  ? 211 ASN A ND2 1 
ATOM   1697  N N   . GLU A 1 212 ? 22.057  18.115  19.641  1.00 71.29  ? 212 GLU A N   1 
ATOM   1698  C CA  . GLU A 1 212 ? 20.812  18.002  20.381  1.00 69.58  ? 212 GLU A CA  1 
ATOM   1699  C C   . GLU A 1 212 ? 20.856  18.837  21.656  1.00 68.63  ? 212 GLU A C   1 
ATOM   1700  O O   . GLU A 1 212 ? 19.902  19.501  21.980  1.00 67.91  ? 212 GLU A O   1 
ATOM   1701  C CB  . GLU A 1 212 ? 20.583  16.539  20.728  1.00 71.14  ? 212 GLU A CB  1 
ATOM   1702  C CG  . GLU A 1 212 ? 20.265  15.701  19.492  1.00 71.92  ? 212 GLU A CG  1 
ATOM   1703  C CD  . GLU A 1 212 ? 20.190  14.198  19.680  1.00 71.16  ? 212 GLU A CD  1 
ATOM   1704  O OE1 . GLU A 1 212 ? 20.489  13.691  20.783  1.00 71.49  ? 212 GLU A OE1 1 
ATOM   1705  O OE2 . GLU A 1 212 ? 19.839  13.548  18.678  1.00 70.03  ? 212 GLU A OE2 1 
ATOM   1706  N N   . LEU A 1 213 ? 21.956  18.823  22.406  1.00 68.28  ? 213 LEU A N   1 
ATOM   1707  C CA  . LEU A 1 213 ? 22.027  19.695  23.570  1.00 68.96  ? 213 LEU A CA  1 
ATOM   1708  C C   . LEU A 1 213 ? 21.979  21.162  23.123  1.00 69.23  ? 213 LEU A C   1 
ATOM   1709  O O   . LEU A 1 213 ? 21.422  21.992  23.838  1.00 69.28  ? 213 LEU A O   1 
ATOM   1710  C CB  . LEU A 1 213 ? 23.255  19.425  24.441  1.00 67.96  ? 213 LEU A CB  1 
ATOM   1711  C CG  . LEU A 1 213 ? 23.195  18.227  25.399  1.00 67.24  ? 213 LEU A CG  1 
ATOM   1712  C CD1 . LEU A 1 213 ? 24.577  18.110  26.028  1.00 67.46  ? 213 LEU A CD1 1 
ATOM   1713  C CD2 . LEU A 1 213 ? 22.169  18.274  26.507  1.00 67.56  ? 213 LEU A CD2 1 
ATOM   1714  N N   . ASN A 1 214 ? 22.548  21.465  21.945  1.00 69.06  ? 214 ASN A N   1 
ATOM   1715  C CA  . ASN A 1 214 ? 22.629  22.830  21.437  1.00 70.41  ? 214 ASN A CA  1 
ATOM   1716  C C   . ASN A 1 214 ? 21.237  23.396  21.134  1.00 70.71  ? 214 ASN A C   1 
ATOM   1717  O O   . ASN A 1 214 ? 21.030  24.597  21.292  1.00 71.88  ? 214 ASN A O   1 
ATOM   1718  C CB  . ASN A 1 214 ? 23.566  22.953  20.232  1.00 70.58  ? 214 ASN A CB  1 
ATOM   1719  C CG  . ASN A 1 214 ? 25.022  22.948  20.637  1.00 72.46  ? 214 ASN A CG  1 
ATOM   1720  O OD1 . ASN A 1 214 ? 25.324  23.090  21.829  1.00 73.27  ? 214 ASN A OD1 1 
ATOM   1721  N ND2 . ASN A 1 214 ? 25.933  22.775  19.683  1.00 72.26  ? 214 ASN A ND2 1 
ATOM   1722  N N   . GLY A 1 215 ? 20.302  22.558  20.659  1.00 69.66  ? 215 GLY A N   1 
ATOM   1723  C CA  . GLY A 1 215 ? 18.910  22.979  20.510  1.00 70.03  ? 215 GLY A CA  1 
ATOM   1724  C C   . GLY A 1 215 ? 18.319  22.746  19.118  1.00 68.05  ? 215 GLY A C   1 
ATOM   1725  O O   . GLY A 1 215 ? 17.155  23.080  18.885  1.00 68.22  ? 215 GLY A O   1 
ATOM   1726  N N   . LEU A 1 216 ? 19.137  22.212  18.203  1.00 65.31  ? 216 LEU A N   1 
ATOM   1727  C CA  . LEU A 1 216 ? 18.694  21.833  16.877  1.00 64.35  ? 216 LEU A CA  1 
ATOM   1728  C C   . LEU A 1 216 ? 17.919  22.978  16.251  1.00 65.34  ? 216 LEU A C   1 
ATOM   1729  O O   . LEU A 1 216 ? 16.853  22.750  15.717  1.00 67.42  ? 216 LEU A O   1 
ATOM   1730  C CB  . LEU A 1 216 ? 17.825  20.578  16.946  1.00 64.35  ? 216 LEU A CB  1 
ATOM   1731  C CG  . LEU A 1 216 ? 18.432  19.361  17.650  1.00 63.42  ? 216 LEU A CG  1 
ATOM   1732  C CD1 . LEU A 1 216 ? 17.281  18.437  17.875  1.00 63.63  ? 216 LEU A CD1 1 
ATOM   1733  C CD2 . LEU A 1 216 ? 19.590  18.667  16.920  1.00 61.69  ? 216 LEU A CD2 1 
ATOM   1734  N N   . ASP A 1 217 ? 18.460  24.194  16.316  1.00 65.97  ? 217 ASP A N   1 
ATOM   1735  C CA  . ASP A 1 217 ? 17.759  25.385  15.873  1.00 66.70  ? 217 ASP A CA  1 
ATOM   1736  C C   . ASP A 1 217 ? 18.640  26.190  14.926  1.00 66.08  ? 217 ASP A C   1 
ATOM   1737  O O   . ASP A 1 217 ? 18.331  27.341  14.622  1.00 66.97  ? 217 ASP A O   1 
ATOM   1738  C CB  . ASP A 1 217 ? 17.348  26.218  17.078  1.00 68.54  ? 217 ASP A CB  1 
ATOM   1739  C CG  . ASP A 1 217 ? 18.396  26.320  18.177  1.00 69.49  ? 217 ASP A CG  1 
ATOM   1740  O OD1 . ASP A 1 217 ? 19.528  25.833  17.967  1.00 70.37  ? 217 ASP A OD1 1 
ATOM   1741  O OD2 . ASP A 1 217 ? 18.073  26.849  19.250  1.00 71.03  ? 217 ASP A OD2 1 
ATOM   1742  N N   . LYS A 1 218 ? 19.766  25.612  14.501  1.00 64.63  ? 218 LYS A N   1 
ATOM   1743  C CA  . LYS A 1 218 ? 20.716  26.347  13.676  1.00 64.34  ? 218 LYS A CA  1 
ATOM   1744  C C   . LYS A 1 218 ? 21.484  25.344  12.835  1.00 62.95  ? 218 LYS A C   1 
ATOM   1745  O O   . LYS A 1 218 ? 21.676  24.200  13.251  1.00 64.43  ? 218 LYS A O   1 
ATOM   1746  C CB  . LYS A 1 218 ? 21.784  27.135  14.437  1.00 64.31  ? 218 LYS A CB  1 
ATOM   1747  C CG  . LYS A 1 218 ? 21.323  27.864  15.671  1.00 66.01  ? 218 LYS A CG  1 
ATOM   1748  C CD  . LYS A 1 218 ? 22.372  28.775  16.303  1.00 67.45  ? 218 LYS A CD  1 
ATOM   1749  C CE  . LYS A 1 218 ? 21.657  30.003  16.778  1.00 70.63  ? 218 LYS A CE  1 
ATOM   1750  N NZ  . LYS A 1 218 ? 22.404  30.728  17.795  1.00 72.05  ? 218 LYS A NZ  1 
ATOM   1751  N N   . PRO A 1 219 ? 21.969  25.729  11.643  1.00 61.59  ? 219 PRO A N   1 
ATOM   1752  C CA  . PRO A 1 219 ? 22.807  24.815  10.873  1.00 61.52  ? 219 PRO A CA  1 
ATOM   1753  C C   . PRO A 1 219 ? 24.021  24.372  11.696  1.00 61.97  ? 219 PRO A C   1 
ATOM   1754  O O   . PRO A 1 219 ? 24.557  25.138  12.496  1.00 60.82  ? 219 PRO A O   1 
ATOM   1755  C CB  . PRO A 1 219 ? 23.173  25.665  9.652   1.00 61.59  ? 219 PRO A CB  1 
ATOM   1756  C CG  . PRO A 1 219 ? 22.077  26.711  9.574   1.00 61.67  ? 219 PRO A CG  1 
ATOM   1757  C CD  . PRO A 1 219 ? 21.790  27.045  11.017  1.00 61.69  ? 219 PRO A CD  1 
ATOM   1758  N N   . PHE A 1 220 ? 24.436  23.105  11.535  1.00 63.87  ? 220 PHE A N   1 
ATOM   1759  C CA  . PHE A 1 220 ? 25.646  22.610  12.198  1.00 64.84  ? 220 PHE A CA  1 
ATOM   1760  C C   . PHE A 1 220 ? 26.713  22.269  11.154  1.00 62.11  ? 220 PHE A C   1 
ATOM   1761  O O   . PHE A 1 220 ? 26.418  21.586  10.173  1.00 60.74  ? 220 PHE A O   1 
ATOM   1762  C CB  . PHE A 1 220 ? 25.237  21.484  13.151  1.00 66.82  ? 220 PHE A CB  1 
ATOM   1763  C CG  . PHE A 1 220 ? 26.376  20.613  13.639  1.00 72.53  ? 220 PHE A CG  1 
ATOM   1764  C CD1 . PHE A 1 220 ? 27.105  20.936  14.781  1.00 78.17  ? 220 PHE A CD1 1 
ATOM   1765  C CD2 . PHE A 1 220 ? 26.717  19.454  12.949  1.00 74.69  ? 220 PHE A CD2 1 
ATOM   1766  C CE1 . PHE A 1 220 ? 28.147  20.111  15.208  1.00 76.03  ? 220 PHE A CE1 1 
ATOM   1767  C CE2 . PHE A 1 220 ? 27.758  18.646  13.379  1.00 73.73  ? 220 PHE A CE2 1 
ATOM   1768  C CZ  . PHE A 1 220 ? 28.462  18.976  14.510  1.00 73.97  ? 220 PHE A CZ  1 
ATOM   1769  N N   . ILE A 1 221 ? 27.939  22.786  11.351  1.00 60.72  ? 221 ILE A N   1 
ATOM   1770  C CA  . ILE A 1 221 ? 29.048  22.470  10.457  1.00 59.95  ? 221 ILE A CA  1 
ATOM   1771  C C   . ILE A 1 221 ? 30.231  21.948  11.262  1.00 60.05  ? 221 ILE A C   1 
ATOM   1772  O O   . ILE A 1 221 ? 30.345  22.243  12.449  1.00 60.72  ? 221 ILE A O   1 
ATOM   1773  C CB  . ILE A 1 221 ? 29.441  23.676  9.583   1.00 59.35  ? 221 ILE A CB  1 
ATOM   1774  C CG1 . ILE A 1 221 ? 30.099  24.824  10.385  1.00 58.90  ? 221 ILE A CG1 1 
ATOM   1775  C CG2 . ILE A 1 221 ? 28.216  24.146  8.797   1.00 59.87  ? 221 ILE A CG2 1 
ATOM   1776  C CD1 . ILE A 1 221 ? 30.467  26.042  9.556   1.00 58.59  ? 221 ILE A CD1 1 
ATOM   1777  N N   . THR A 1 222 ? 31.066  21.133  10.600  1.00 59.91  ? 222 THR A N   1 
ATOM   1778  C CA  . THR A 1 222 ? 32.386  20.796  11.106  1.00 60.28  ? 222 THR A CA  1 
ATOM   1779  C C   . THR A 1 222 ? 33.393  21.755  10.490  1.00 60.96  ? 222 THR A C   1 
ATOM   1780  O O   . THR A 1 222 ? 33.377  22.032  9.291   1.00 61.00  ? 222 THR A O   1 
ATOM   1781  C CB  . THR A 1 222 ? 32.778  19.362  10.770  1.00 59.82  ? 222 THR A CB  1 
ATOM   1782  O OG1 . THR A 1 222 ? 32.706  19.335  9.347   1.00 59.78  ? 222 THR A OG1 1 
ATOM   1783  C CG2 . THR A 1 222 ? 31.903  18.331  11.457  1.00 59.61  ? 222 THR A CG2 1 
ATOM   1784  N N   . THR A 1 223 ? 34.302  22.223  11.333  1.00 62.10  ? 223 THR A N   1 
ATOM   1785  C CA  . THR A 1 223 ? 35.345  23.140  10.920  1.00 61.80  ? 223 THR A CA  1 
ATOM   1786  C C   . THR A 1 223 ? 36.693  22.430  10.818  1.00 63.86  ? 223 THR A C   1 
ATOM   1787  O O   . THR A 1 223 ? 37.603  22.954  10.186  1.00 66.80  ? 223 THR A O   1 
ATOM   1788  C CB  . THR A 1 223 ? 35.336  24.258  11.949  1.00 61.01  ? 223 THR A CB  1 
ATOM   1789  O OG1 . THR A 1 223 ? 34.937  23.676  13.190  1.00 59.40  ? 223 THR A OG1 1 
ATOM   1790  C CG2 . THR A 1 223 ? 34.345  25.336  11.559  1.00 60.99  ? 223 THR A CG2 1 
ATOM   1791  N N   . GLU A 1 224 ? 36.844  21.240  11.423  1.00 64.84  ? 224 GLU A N   1 
ATOM   1792  C CA  . GLU A 1 224 ? 38.040  20.429  11.184  1.00 66.30  ? 224 GLU A CA  1 
ATOM   1793  C C   . GLU A 1 224 ? 37.743  18.955  11.457  1.00 63.16  ? 224 GLU A C   1 
ATOM   1794  O O   . GLU A 1 224 ? 36.861  18.640  12.242  1.00 62.15  ? 224 GLU A O   1 
ATOM   1795  C CB  . GLU A 1 224 ? 39.264  20.783  12.046  1.00 68.68  ? 224 GLU A CB  1 
ATOM   1796  C CG  . GLU A 1 224 ? 39.943  22.122  11.747  1.00 70.05  ? 224 GLU A CG  1 
ATOM   1797  C CD  . GLU A 1 224 ? 41.203  22.381  12.588  1.00 73.13  ? 224 GLU A CD  1 
ATOM   1798  O OE1 . GLU A 1 224 ? 41.346  23.478  13.167  1.00 76.32  ? 224 GLU A OE1 1 
ATOM   1799  O OE2 . GLU A 1 224 ? 42.070  21.487  12.696  1.00 75.37  ? 224 GLU A OE2 1 
ATOM   1800  N N   . PHE A 1 225 ? 38.512  18.064  10.823  1.00 62.49  ? 225 PHE A N   1 
ATOM   1801  C CA  . PHE A 1 225 ? 38.569  16.655  11.212  1.00 61.01  ? 225 PHE A CA  1 
ATOM   1802  C C   . PHE A 1 225 ? 39.577  15.915  10.326  1.00 60.11  ? 225 PHE A C   1 
ATOM   1803  O O   . PHE A 1 225 ? 39.588  16.117  9.115   1.00 59.55  ? 225 PHE A O   1 
ATOM   1804  C CB  . PHE A 1 225 ? 37.186  15.988  11.153  1.00 59.24  ? 225 PHE A CB  1 
ATOM   1805  C CG  . PHE A 1 225 ? 36.538  15.985  9.780   1.00 57.93  ? 225 PHE A CG  1 
ATOM   1806  C CD1 . PHE A 1 225 ? 35.724  17.020  9.376   1.00 57.23  ? 225 PHE A CD1 1 
ATOM   1807  C CD2 . PHE A 1 225 ? 36.717  14.921  8.911   1.00 57.83  ? 225 PHE A CD2 1 
ATOM   1808  C CE1 . PHE A 1 225 ? 35.125  16.999  8.128   1.00 57.27  ? 225 PHE A CE1 1 
ATOM   1809  C CE2 . PHE A 1 225 ? 36.114  14.906  7.663   1.00 57.27  ? 225 PHE A CE2 1 
ATOM   1810  C CZ  . PHE A 1 225 ? 35.336  15.951  7.268   1.00 57.03  ? 225 PHE A CZ  1 
ATOM   1811  N N   . GLY A 1 226 ? 40.398  15.032  10.917  1.00 60.33  ? 226 GLY A N   1 
ATOM   1812  C CA  . GLY A 1 226 ? 41.353  14.252  10.127  1.00 60.60  ? 226 GLY A CA  1 
ATOM   1813  C C   . GLY A 1 226 ? 42.401  13.505  10.954  1.00 60.05  ? 226 GLY A C   1 
ATOM   1814  O O   . GLY A 1 226 ? 42.202  13.159  12.112  1.00 59.49  ? 226 GLY A O   1 
ATOM   1815  N N   . TYR A 1 227 ? 43.535  13.218  10.338  1.00 60.67  ? 227 TYR A N   1 
ATOM   1816  C CA  . TYR A 1 227 ? 44.417  12.211  10.928  1.00 62.51  ? 227 TYR A CA  1 
ATOM   1817  C C   . TYR A 1 227 ? 45.829  12.481  10.459  1.00 62.89  ? 227 TYR A C   1 
ATOM   1818  O O   . TYR A 1 227 ? 46.035  12.903  9.321   1.00 63.97  ? 227 TYR A O   1 
ATOM   1819  C CB  . TYR A 1 227 ? 44.056  10.743  10.607  1.00 62.38  ? 227 TYR A CB  1 
ATOM   1820  C CG  . TYR A 1 227 ? 42.745  10.270  11.243  1.00 61.97  ? 227 TYR A CG  1 
ATOM   1821  C CD1 . TYR A 1 227 ? 42.656  10.039  12.613  1.00 62.39  ? 227 TYR A CD1 1 
ATOM   1822  C CD2 . TYR A 1 227 ? 41.584  10.069  10.499  1.00 61.91  ? 227 TYR A CD2 1 
ATOM   1823  C CE1 . TYR A 1 227 ? 41.478  9.633   13.225  1.00 62.25  ? 227 TYR A CE1 1 
ATOM   1824  C CE2 . TYR A 1 227 ? 40.397  9.643   11.095  1.00 61.68  ? 227 TYR A CE2 1 
ATOM   1825  C CZ  . TYR A 1 227 ? 40.337  9.415   12.466  1.00 61.63  ? 227 TYR A CZ  1 
ATOM   1826  O OH  . TYR A 1 227 ? 39.178  9.009   13.089  1.00 59.56  ? 227 TYR A OH  1 
ATOM   1827  N N   . SER A 1 228 ? 46.785  12.240  11.354  1.00 63.31  ? 228 SER A N   1 
ATOM   1828  C CA  . SER A 1 228 ? 48.187  12.507  11.045  1.00 63.68  ? 228 SER A CA  1 
ATOM   1829  C C   . SER A 1 228 ? 48.908  11.226  10.601  1.00 64.53  ? 228 SER A C   1 
ATOM   1830  O O   . SER A 1 228 ? 48.633  10.114  11.083  1.00 63.34  ? 228 SER A O   1 
ATOM   1831  C CB  . SER A 1 228 ? 48.872  13.156  12.208  1.00 63.64  ? 228 SER A CB  1 
ATOM   1832  O OG  . SER A 1 228 ? 50.271  13.206  11.986  1.00 64.73  ? 228 SER A OG  1 
ATOM   1833  N N   . VAL A 1 229 ? 49.860  11.401  9.673   1.00 65.75  ? 229 VAL A N   1 
ATOM   1834  C CA  . VAL A 1 229 ? 50.572  10.263  9.116   1.00 66.68  ? 229 VAL A CA  1 
ATOM   1835  C C   . VAL A 1 229 ? 52.035  10.362  9.509   1.00 67.04  ? 229 VAL A C   1 
ATOM   1836  O O   . VAL A 1 229 ? 52.885  9.827   8.789   1.00 69.42  ? 229 VAL A O   1 
ATOM   1837  C CB  . VAL A 1 229 ? 50.430  10.120  7.588   1.00 66.83  ? 229 VAL A CB  1 
ATOM   1838  C CG1 . VAL A 1 229 ? 48.960  10.032  7.176   1.00 65.34  ? 229 VAL A CG1 1 
ATOM   1839  C CG2 . VAL A 1 229 ? 51.136  11.259  6.856   1.00 67.48  ? 229 VAL A CG2 1 
ATOM   1840  N N   . SER A 1 230 ? 52.316  10.957  10.676  1.00 66.32  ? 230 SER A N   1 
ATOM   1841  C CA  . SER A 1 230 ? 53.708  11.067  11.095  1.00 67.98  ? 230 SER A CA  1 
ATOM   1842  C C   . SER A 1 230 ? 54.370  9.685   11.139  1.00 69.74  ? 230 SER A C   1 
ATOM   1843  O O   . SER A 1 230 ? 53.748  8.642   11.380  1.00 69.60  ? 230 SER A O   1 
ATOM   1844  C CB  . SER A 1 230 ? 53.880  11.802  12.397  1.00 67.73  ? 230 SER A CB  1 
ATOM   1845  O OG  . SER A 1 230 ? 53.015  11.296  13.398  1.00 66.69  ? 230 SER A OG  1 
ATOM   1846  N N   . PRO A 1 231 ? 55.668  9.631   10.822  1.00 71.24  ? 231 PRO A N   1 
ATOM   1847  C CA  . PRO A 1 231 ? 56.442  8.400   10.936  1.00 72.96  ? 231 PRO A CA  1 
ATOM   1848  C C   . PRO A 1 231 ? 56.254  7.762   12.306  1.00 73.70  ? 231 PRO A C   1 
ATOM   1849  O O   . PRO A 1 231 ? 56.141  6.516   12.426  1.00 73.95  ? 231 PRO A O   1 
ATOM   1850  C CB  . PRO A 1 231 ? 57.893  8.827   10.724  1.00 74.80  ? 231 PRO A CB  1 
ATOM   1851  C CG  . PRO A 1 231 ? 57.800  10.143  9.988   1.00 74.60  ? 231 PRO A CG  1 
ATOM   1852  C CD  . PRO A 1 231 ? 56.426  10.752  10.273  1.00 72.79  ? 231 PRO A CD  1 
ATOM   1853  N N   . GLU A 1 232 ? 56.250  8.643   13.319  1.00 73.14  ? 232 GLU A N   1 
ATOM   1854  C CA  . GLU A 1 232 ? 56.057  8.201   14.688  1.00 73.99  ? 232 GLU A CA  1 
ATOM   1855  C C   . GLU A 1 232 ? 55.479  9.360   15.476  1.00 73.10  ? 232 GLU A C   1 
ATOM   1856  O O   . GLU A 1 232 ? 55.122  10.373  14.888  1.00 71.75  ? 232 GLU A O   1 
ATOM   1857  C CB  . GLU A 1 232 ? 57.333  7.612   15.305  1.00 76.10  ? 232 GLU A CB  1 
ATOM   1858  C CG  . GLU A 1 232 ? 58.476  8.605   15.440  1.00 78.07  ? 232 GLU A CG  1 
ATOM   1859  C CD  . GLU A 1 232 ? 59.842  8.030   15.775  1.00 81.26  ? 232 GLU A CD  1 
ATOM   1860  O OE1 . GLU A 1 232 ? 60.411  8.492   16.794  1.00 83.26  ? 232 GLU A OE1 1 
ATOM   1861  O OE2 . GLU A 1 232 ? 60.367  7.175   15.015  1.00 82.39  ? 232 GLU A OE2 1 
ATOM   1862  N N   . GLY A 1 233 ? 55.358  9.155   16.791  1.00 74.07  ? 233 GLY A N   1 
ATOM   1863  C CA  . GLY A 1 233 ? 54.995  10.214  17.713  1.00 73.98  ? 233 GLY A CA  1 
ATOM   1864  C C   . GLY A 1 233 ? 53.483  10.302  17.861  1.00 72.83  ? 233 GLY A C   1 
ATOM   1865  O O   . GLY A 1 233 ? 52.754  9.768   17.038  1.00 72.74  ? 233 GLY A O   1 
ATOM   1866  N N   . GLY A 1 234 ? 53.039  11.013  18.899  1.00 73.12  ? 234 GLY A N   1 
ATOM   1867  C CA  . GLY A 1 234 ? 51.631  11.214  19.165  1.00 71.51  ? 234 GLY A CA  1 
ATOM   1868  C C   . GLY A 1 234 ? 51.141  10.186  20.176  1.00 72.29  ? 234 GLY A C   1 
ATOM   1869  O O   . GLY A 1 234 ? 51.786  9.947   21.189  1.00 72.72  ? 234 GLY A O   1 
ATOM   1870  N N   . ASN A 1 235 ? 49.999  9.567   19.877  1.00 73.01  ? 235 ASN A N   1 
ATOM   1871  C CA  . ASN A 1 235 ? 49.361  8.660   20.804  1.00 74.24  ? 235 ASN A CA  1 
ATOM   1872  C C   . ASN A 1 235 ? 48.107  8.107   20.151  1.00 72.17  ? 235 ASN A C   1 
ATOM   1873  O O   . ASN A 1 235 ? 47.322  8.858   19.566  1.00 71.84  ? 235 ASN A O   1 
ATOM   1874  C CB  . ASN A 1 235 ? 49.036  9.368   22.111  1.00 77.06  ? 235 ASN A CB  1 
ATOM   1875  C CG  . ASN A 1 235 ? 48.294  8.470   23.062  1.00 79.50  ? 235 ASN A CG  1 
ATOM   1876  O OD1 . ASN A 1 235 ? 48.589  7.272   23.151  1.00 80.95  ? 235 ASN A OD1 1 
ATOM   1877  N ND2 . ASN A 1 235 ? 47.327  9.044   23.762  1.00 81.33  ? 235 ASN A ND2 1 
ATOM   1878  N N   . GLY A 1 236 ? 47.926  6.800   20.306  1.00 70.68  ? 236 GLY A N   1 
ATOM   1879  C CA  . GLY A 1 236 ? 46.826  6.106   19.684  1.00 70.28  ? 236 GLY A CA  1 
ATOM   1880  C C   . GLY A 1 236 ? 46.664  6.539   18.234  1.00 69.70  ? 236 GLY A C   1 
ATOM   1881  O O   . GLY A 1 236 ? 47.607  6.504   17.457  1.00 68.67  ? 236 GLY A O   1 
ATOM   1882  N N   . GLN A 1 237 ? 45.443  6.942   17.880  1.00 71.01  ? 237 GLN A N   1 
ATOM   1883  C CA  . GLN A 1 237 ? 45.175  7.415   16.534  1.00 71.49  ? 237 GLN A CA  1 
ATOM   1884  C C   . GLN A 1 237 ? 45.719  8.831   16.309  1.00 71.91  ? 237 GLN A C   1 
ATOM   1885  O O   . GLN A 1 237 ? 45.774  9.299   15.172  1.00 69.83  ? 237 GLN A O   1 
ATOM   1886  C CB  . GLN A 1 237 ? 43.678  7.339   16.282  1.00 69.59  ? 237 GLN A CB  1 
ATOM   1887  C CG  . GLN A 1 237 ? 43.200  5.913   16.106  1.00 70.07  ? 237 GLN A CG  1 
ATOM   1888  C CD  . GLN A 1 237 ? 41.762  5.830   15.655  1.00 69.65  ? 237 GLN A CD  1 
ATOM   1889  O OE1 . GLN A 1 237 ? 41.432  6.100   14.495  1.00 68.01  ? 237 GLN A OE1 1 
ATOM   1890  N NE2 . GLN A 1 237 ? 40.902  5.435   16.578  1.00 70.56  ? 237 GLN A NE2 1 
ATOM   1891  N N   . TYR A 1 238 ? 46.108  9.520   17.383  1.00 73.82  ? 238 TYR A N   1 
ATOM   1892  C CA  . TYR A 1 238 ? 46.620  10.872  17.227  1.00 78.38  ? 238 TYR A CA  1 
ATOM   1893  C C   . TYR A 1 238 ? 48.102  10.757  16.886  1.00 77.47  ? 238 TYR A C   1 
ATOM   1894  O O   . TYR A 1 238 ? 48.914  10.537  17.769  1.00 77.55  ? 238 TYR A O   1 
ATOM   1895  C CB  . TYR A 1 238 ? 46.404  11.808  18.425  1.00 79.44  ? 238 TYR A CB  1 
ATOM   1896  C CG  . TYR A 1 238 ? 47.150  13.126  18.305  1.00 79.00  ? 238 TYR A CG  1 
ATOM   1897  C CD1 . TYR A 1 238 ? 46.710  14.119  17.442  1.00 79.92  ? 238 TYR A CD1 1 
ATOM   1898  C CD2 . TYR A 1 238 ? 48.286  13.376  19.048  1.00 82.22  ? 238 TYR A CD2 1 
ATOM   1899  C CE1 . TYR A 1 238 ? 47.352  15.342  17.342  1.00 80.08  ? 238 TYR A CE1 1 
ATOM   1900  C CE2 . TYR A 1 238 ? 48.959  14.582  18.943  1.00 85.05  ? 238 TYR A CE2 1 
ATOM   1901  C CZ  . TYR A 1 238 ? 48.486  15.570  18.095  1.00 83.55  ? 238 TYR A CZ  1 
ATOM   1902  O OH  . TYR A 1 238 ? 49.161  16.743  17.974  1.00 84.44  ? 238 TYR A OH  1 
ATOM   1903  N N   . GLY A 1 239 ? 48.409  10.906  15.594  1.00 76.59  ? 239 GLY A N   1 
ATOM   1904  C CA  . GLY A 1 239 ? 49.726  10.651  15.048  1.00 76.74  ? 239 GLY A CA  1 
ATOM   1905  C C   . GLY A 1 239 ? 49.858  9.216   14.551  1.00 75.01  ? 239 GLY A C   1 
ATOM   1906  O O   . GLY A 1 239 ? 49.028  8.365   14.848  1.00 74.89  ? 239 GLY A O   1 
ATOM   1907  N N   . SER A 1 240 ? 50.896  9.010   13.736  1.00 74.17  ? 240 SER A N   1 
ATOM   1908  C CA  . SER A 1 240 ? 51.450  7.703   13.428  1.00 72.08  ? 240 SER A CA  1 
ATOM   1909  C C   . SER A 1 240 ? 50.457  6.819   12.670  1.00 70.89  ? 240 SER A C   1 
ATOM   1910  O O   . SER A 1 240 ? 50.543  5.610   12.760  1.00 71.54  ? 240 SER A O   1 
ATOM   1911  C CB  . SER A 1 240 ? 51.959  7.081   14.691  1.00 71.53  ? 240 SER A CB  1 
ATOM   1912  O OG  . SER A 1 240 ? 53.016  7.875   15.206  1.00 70.79  ? 240 SER A OG  1 
ATOM   1913  N N   . ASN A 1 241 ? 49.553  7.402   11.874  1.00 70.52  ? 241 ASN A N   1 
ATOM   1914  C CA  . ASN A 1 241 ? 48.692  6.610   11.001  1.00 70.99  ? 241 ASN A CA  1 
ATOM   1915  C C   . ASN A 1 241 ? 49.394  6.325   9.672   1.00 69.75  ? 241 ASN A C   1 
ATOM   1916  O O   . ASN A 1 241 ? 50.175  7.166   9.219   1.00 71.01  ? 241 ASN A O   1 
ATOM   1917  C CB  . ASN A 1 241 ? 47.405  7.333   10.624  1.00 72.04  ? 241 ASN A CB  1 
ATOM   1918  C CG  . ASN A 1 241 ? 46.466  7.526   11.787  1.00 73.60  ? 241 ASN A CG  1 
ATOM   1919  O OD1 . ASN A 1 241 ? 45.566  6.708   11.970  1.00 76.25  ? 241 ASN A OD1 1 
ATOM   1920  N ND2 . ASN A 1 241 ? 46.636  8.587   12.564  1.00 74.73  ? 241 ASN A ND2 1 
ATOM   1921  N N   . THR A 1 242 ? 49.062  5.189   9.031   1.00 66.51  ? 242 THR A N   1 
ATOM   1922  C CA  . THR A 1 242 ? 49.517  4.905   7.681   1.00 66.30  ? 242 THR A CA  1 
ATOM   1923  C C   . THR A 1 242 ? 48.674  5.708   6.718   1.00 64.28  ? 242 THR A C   1 
ATOM   1924  O O   . THR A 1 242 ? 47.611  6.167   7.113   1.00 65.84  ? 242 THR A O   1 
ATOM   1925  C CB  . THR A 1 242 ? 49.386  3.429   7.333   1.00 67.62  ? 242 THR A CB  1 
ATOM   1926  O OG1 . THR A 1 242 ? 48.146  3.028   7.918   1.00 69.87  ? 242 THR A OG1 1 
ATOM   1927  C CG2 . THR A 1 242 ? 50.553  2.601   7.826   1.00 68.19  ? 242 THR A CG2 1 
ATOM   1928  N N   . LEU A 1 243 ? 49.118  5.820   5.458   1.00 63.05  ? 243 LEU A N   1 
ATOM   1929  C CA  . LEU A 1 243 ? 48.355  6.517   4.430   1.00 61.38  ? 243 LEU A CA  1 
ATOM   1930  C C   . LEU A 1 243 ? 47.003  5.809   4.249   1.00 60.80  ? 243 LEU A C   1 
ATOM   1931  O O   . LEU A 1 243 ? 45.998  6.423   3.920   1.00 59.12  ? 243 LEU A O   1 
ATOM   1932  C CB  . LEU A 1 243 ? 49.132  6.613   3.117   1.00 61.31  ? 243 LEU A CB  1 
ATOM   1933  C CG  . LEU A 1 243 ? 50.505  7.300   3.206   1.00 62.38  ? 243 LEU A CG  1 
ATOM   1934  C CD1 . LEU A 1 243 ? 51.396  6.941   2.008   1.00 63.31  ? 243 LEU A CD1 1 
ATOM   1935  C CD2 . LEU A 1 243 ? 50.442  8.822   3.375   1.00 61.76  ? 243 LEU A CD2 1 
ATOM   1936  N N   . LYS A 1 244 ? 46.956  4.496   4.467   1.00 61.29  ? 244 LYS A N   1 
ATOM   1937  C CA  . LYS A 1 244 ? 45.699  3.805   4.278   1.00 61.48  ? 244 LYS A CA  1 
ATOM   1938  C C   . LYS A 1 244 ? 44.712  4.258   5.356   1.00 60.91  ? 244 LYS A C   1 
ATOM   1939  O O   . LYS A 1 244 ? 43.540  4.527   5.059   1.00 58.76  ? 244 LYS A O   1 
ATOM   1940  C CB  . LYS A 1 244 ? 45.840  2.278   4.293   1.00 62.00  ? 244 LYS A CB  1 
ATOM   1941  C CG  . LYS A 1 244 ? 44.501  1.544   4.264   1.00 61.08  ? 244 LYS A CG  1 
ATOM   1942  C CD  . LYS A 1 244 ? 44.639  0.063   3.976   1.00 61.97  ? 244 LYS A CD  1 
ATOM   1943  C CE  . LYS A 1 244 ? 43.392  -0.744  4.143   1.00 62.30  ? 244 LYS A CE  1 
ATOM   1944  N NZ  . LYS A 1 244 ? 42.187  -0.298  3.426   1.00 61.55  ? 244 LYS A NZ  1 
ATOM   1945  N N   . GLN A 1 245 ? 45.208  4.297   6.602   1.00 61.20  ? 245 GLN A N   1 
ATOM   1946  C CA  . GLN A 1 245 ? 44.345  4.561   7.728   1.00 60.85  ? 245 GLN A CA  1 
ATOM   1947  C C   . GLN A 1 245 ? 43.788  5.968   7.596   1.00 60.45  ? 245 GLN A C   1 
ATOM   1948  O O   . GLN A 1 245 ? 42.606  6.176   7.870   1.00 59.76  ? 245 GLN A O   1 
ATOM   1949  C CB  . GLN A 1 245 ? 45.064  4.471   9.060   1.00 61.62  ? 245 GLN A CB  1 
ATOM   1950  C CG  . GLN A 1 245 ? 45.342  3.063   9.543   1.00 62.31  ? 245 GLN A CG  1 
ATOM   1951  C CD  . GLN A 1 245 ? 46.406  3.102   10.607  1.00 64.88  ? 245 GLN A CD  1 
ATOM   1952  O OE1 . GLN A 1 245 ? 47.238  4.007   10.598  1.00 68.96  ? 245 GLN A OE1 1 
ATOM   1953  N NE2 . GLN A 1 245 ? 46.403  2.189   11.559  1.00 66.16  ? 245 GLN A NE2 1 
ATOM   1954  N N   . GLN A 1 246 ? 44.649  6.904   7.177   1.00 60.88  ? 246 GLN A N   1 
ATOM   1955  C CA  . GLN A 1 246 ? 44.241  8.294   6.990   1.00 60.92  ? 246 GLN A CA  1 
ATOM   1956  C C   . GLN A 1 246 ? 43.102  8.401   5.982   1.00 59.30  ? 246 GLN A C   1 
ATOM   1957  O O   . GLN A 1 246 ? 42.073  8.963   6.301   1.00 59.71  ? 246 GLN A O   1 
ATOM   1958  C CB  . GLN A 1 246 ? 45.433  9.098   6.483   1.00 62.58  ? 246 GLN A CB  1 
ATOM   1959  C CG  . GLN A 1 246 ? 45.237  10.609  6.424   1.00 62.69  ? 246 GLN A CG  1 
ATOM   1960  C CD  . GLN A 1 246 ? 46.165  11.202  5.390   1.00 64.04  ? 246 GLN A CD  1 
ATOM   1961  O OE1 . GLN A 1 246 ? 46.386  10.589  4.332   1.00 66.23  ? 246 GLN A OE1 1 
ATOM   1962  N NE2 . GLN A 1 246 ? 46.765  12.336  5.714   1.00 63.95  ? 246 GLN A NE2 1 
ATOM   1963  N N   . SER A 1 247 ? 43.328  7.887   4.777   1.00 58.79  ? 247 SER A N   1 
ATOM   1964  C CA  . SER A 1 247 ? 42.323  7.946   3.691   1.00 58.06  ? 247 SER A CA  1 
ATOM   1965  C C   . SER A 1 247 ? 41.033  7.254   4.109   1.00 59.10  ? 247 SER A C   1 
ATOM   1966  O O   . SER A 1 247 ? 39.997  7.546   3.509   1.00 58.10  ? 247 SER A O   1 
ATOM   1967  C CB  . SER A 1 247 ? 42.841  7.279   2.469   1.00 57.79  ? 247 SER A CB  1 
ATOM   1968  O OG  . SER A 1 247 ? 41.795  6.942   1.575   1.00 56.77  ? 247 SER A OG  1 
ATOM   1969  N N   . ASP A 1 248 ? 41.110  6.359   5.082   1.00 60.16  ? 248 ASP A N   1 
ATOM   1970  C CA  . ASP A 1 248 ? 39.917  5.555   5.431   1.00 59.98  ? 248 ASP A CA  1 
ATOM   1971  C C   . ASP A 1 248 ? 39.223  6.222   6.616   1.00 63.02  ? 248 ASP A C   1 
ATOM   1972  O O   . ASP A 1 248 ? 37.990  6.137   6.699   1.00 69.93  ? 248 ASP A O   1 
ATOM   1973  C CB  . ASP A 1 248 ? 40.300  4.091   5.606   1.00 58.96  ? 248 ASP A CB  1 
ATOM   1974  C CG  . ASP A 1 248 ? 40.578  3.343   4.313   1.00 58.58  ? 248 ASP A CG  1 
ATOM   1975  O OD1 . ASP A 1 248 ? 40.434  3.961   3.240   1.00 59.58  ? 248 ASP A OD1 1 
ATOM   1976  O OD2 . ASP A 1 248 ? 40.933  2.153   4.392   1.00 56.09  ? 248 ASP A OD2 1 
ATOM   1977  N N   . GLY A 1 249 ? 39.982  6.864   7.487   1.00 63.00  ? 249 GLY A N   1 
ATOM   1978  C CA  . GLY A 1 249 ? 39.348  7.592   8.595   1.00 64.02  ? 249 GLY A CA  1 
ATOM   1979  C C   . GLY A 1 249 ? 38.699  8.870   8.101   1.00 65.14  ? 249 GLY A C   1 
ATOM   1980  O O   . GLY A 1 249 ? 37.612  9.201   8.587   1.00 63.92  ? 249 GLY A O   1 
ATOM   1981  N N   . LEU A 1 250 ? 39.343  9.570   7.167   1.00 64.37  ? 250 LEU A N   1 
ATOM   1982  C CA  . LEU A 1 250 ? 38.724  10.767  6.620   1.00 62.41  ? 250 LEU A CA  1 
ATOM   1983  C C   . LEU A 1 250 ? 37.319  10.442  6.131   1.00 60.38  ? 250 LEU A C   1 
ATOM   1984  O O   . LEU A 1 250 ? 36.428  11.257  6.342   1.00 58.92  ? 250 LEU A O   1 
ATOM   1985  C CB  . LEU A 1 250 ? 39.570  11.399  5.513   1.00 62.60  ? 250 LEU A CB  1 
ATOM   1986  C CG  . LEU A 1 250 ? 40.369  12.645  5.911   1.00 61.86  ? 250 LEU A CG  1 
ATOM   1987  C CD1 . LEU A 1 250 ? 39.399  13.751  6.340   1.00 60.87  ? 250 LEU A CD1 1 
ATOM   1988  C CD2 . LEU A 1 250 ? 41.387  12.309  6.991   1.00 61.56  ? 250 LEU A CD2 1 
ATOM   1989  N N   . ILE A 1 251 ? 37.150  9.241   5.538   1.00 59.52  ? 251 ILE A N   1 
ATOM   1990  C CA  . ILE A 1 251 ? 35.872  8.827   4.990   1.00 58.65  ? 251 ILE A CA  1 
ATOM   1991  C C   . ILE A 1 251 ? 34.929  8.415   6.125   1.00 59.72  ? 251 ILE A C   1 
ATOM   1992  O O   . ILE A 1 251 ? 33.774  8.834   6.160   1.00 58.29  ? 251 ILE A O   1 
ATOM   1993  C CB  . ILE A 1 251 ? 35.991  7.727   3.924   1.00 57.17  ? 251 ILE A CB  1 
ATOM   1994  C CG1 . ILE A 1 251 ? 36.977  8.071   2.813   1.00 56.10  ? 251 ILE A CG1 1 
ATOM   1995  C CG2 . ILE A 1 251 ? 34.583  7.428   3.376   1.00 57.46  ? 251 ILE A CG2 1 
ATOM   1996  C CD1 . ILE A 1 251 ? 36.719  9.369   2.079   1.00 56.08  ? 251 ILE A CD1 1 
ATOM   1997  N N   . SER A 1 252 ? 35.437  7.638   7.085   1.00 60.61  ? 252 SER A N   1 
ATOM   1998  C CA  . SER A 1 252 ? 34.642  7.271   8.250   1.00 60.41  ? 252 SER A CA  1 
ATOM   1999  C C   . SER A 1 252 ? 34.253  8.486   9.091   1.00 60.45  ? 252 SER A C   1 
ATOM   2000  O O   . SER A 1 252 ? 33.342  8.420   9.893   1.00 59.67  ? 252 SER A O   1 
ATOM   2001  C CB  . SER A 1 252 ? 35.397  6.294   9.088   1.00 60.81  ? 252 SER A CB  1 
ATOM   2002  O OG  . SER A 1 252 ? 34.779  6.142   10.355  1.00 61.13  ? 252 SER A OG  1 
ATOM   2003  N N   . ASN A 1 253 ? 35.026  9.564   8.989   1.00 62.66  ? 253 ASN A N   1 
ATOM   2004  C CA  . ASN A 1 253 ? 34.706  10.808  9.660   1.00 63.36  ? 253 ASN A CA  1 
ATOM   2005  C C   . ASN A 1 253 ? 33.526  11.436  8.930   1.00 63.51  ? 253 ASN A C   1 
ATOM   2006  O O   . ASN A 1 253 ? 32.525  11.817  9.539   1.00 62.00  ? 253 ASN A O   1 
ATOM   2007  C CB  . ASN A 1 253 ? 35.899  11.760  9.658   1.00 65.15  ? 253 ASN A CB  1 
ATOM   2008  C CG  . ASN A 1 253 ? 36.996  11.423  10.647  1.00 67.35  ? 253 ASN A CG  1 
ATOM   2009  O OD1 . ASN A 1 253 ? 37.972  12.178  10.768  1.00 70.10  ? 253 ASN A OD1 1 
ATOM   2010  N ND2 . ASN A 1 253 ? 36.862  10.336  11.390  1.00 68.49  ? 253 ASN A ND2 1 
ATOM   2011  N N   . TYR A 1 254 ? 33.713  11.666  7.635   1.00 63.75  ? 254 TYR A N   1 
ATOM   2012  C CA  . TYR A 1 254 ? 32.676  12.357  6.834   1.00 62.61  ? 254 TYR A CA  1 
ATOM   2013  C C   . TYR A 1 254 ? 31.314  11.807  7.157   1.00 61.73  ? 254 TYR A C   1 
ATOM   2014  O O   . TYR A 1 254 ? 30.523  12.526  7.796   1.00 65.69  ? 254 TYR A O   1 
ATOM   2015  C CB  . TYR A 1 254 ? 33.042  12.185  5.363   1.00 62.79  ? 254 TYR A CB  1 
ATOM   2016  C CG  . TYR A 1 254 ? 32.769  13.444  4.557   1.00 63.44  ? 254 TYR A CG  1 
ATOM   2017  C CD1 . TYR A 1 254 ? 31.472  13.806  4.226   1.00 62.37  ? 254 TYR A CD1 1 
ATOM   2018  C CD2 . TYR A 1 254 ? 33.800  14.282  4.153   1.00 64.98  ? 254 TYR A CD2 1 
ATOM   2019  C CE1 . TYR A 1 254 ? 31.208  14.954  3.501   1.00 63.81  ? 254 TYR A CE1 1 
ATOM   2020  C CE2 . TYR A 1 254 ? 33.548  15.434  3.428   1.00 64.95  ? 254 TYR A CE2 1 
ATOM   2021  C CZ  . TYR A 1 254 ? 32.248  15.769  3.100   1.00 65.59  ? 254 TYR A CZ  1 
ATOM   2022  O OH  . TYR A 1 254 ? 31.967  16.900  2.393   1.00 69.65  ? 254 TYR A OH  1 
ATOM   2023  N N   . ARG A 1 255 ? 31.014  10.606  6.666   1.00 59.34  ? 255 ARG A N   1 
ATOM   2024  C CA  . ARG A 1 255 ? 29.729  9.941   6.958   1.00 58.98  ? 255 ARG A CA  1 
ATOM   2025  C C   . ARG A 1 255 ? 29.335  10.183  8.411   1.00 59.30  ? 255 ARG A C   1 
ATOM   2026  O O   . ARG A 1 255 ? 28.300  10.798  8.654   1.00 59.83  ? 255 ARG A O   1 
ATOM   2027  C CB  . ARG A 1 255 ? 29.944  8.451   6.707   1.00 58.94  ? 255 ARG A CB  1 
ATOM   2028  C CG  . ARG A 1 255 ? 28.821  7.520   7.141   1.00 59.35  ? 255 ARG A CG  1 
ATOM   2029  C CD  . ARG A 1 255 ? 27.680  7.488   6.143   1.00 58.84  ? 255 ARG A CD  1 
ATOM   2030  N NE  . ARG A 1 255 ? 26.748  8.600   6.347   1.00 57.94  ? 255 ARG A NE  1 
ATOM   2031  C CZ  . ARG A 1 255 ? 26.239  9.336   5.376   1.00 57.26  ? 255 ARG A CZ  1 
ATOM   2032  N NH1 . ARG A 1 255 ? 26.815  9.359   4.189   1.00 56.26  ? 255 ARG A NH1 1 
ATOM   2033  N NH2 . ARG A 1 255 ? 25.147  10.038  5.602   1.00 57.62  ? 255 ARG A NH2 1 
ATOM   2034  N N   . ASP A 1 256 ? 30.129  9.697   9.341   1.00 60.11  ? 256 ASP A N   1 
ATOM   2035  C CA  . ASP A 1 256 ? 29.738  9.827   10.763  1.00 61.94  ? 256 ASP A CA  1 
ATOM   2036  C C   . ASP A 1 256 ? 29.296  11.261  11.073  1.00 61.15  ? 256 ASP A C   1 
ATOM   2037  O O   . ASP A 1 256 ? 28.320  11.396  11.820  1.00 62.59  ? 256 ASP A O   1 
ATOM   2038  C CB  . ASP A 1 256 ? 30.836  9.319   11.682  1.00 64.97  ? 256 ASP A CB  1 
ATOM   2039  C CG  . ASP A 1 256 ? 30.944  7.812   11.830  1.00 70.98  ? 256 ASP A CG  1 
ATOM   2040  O OD1 . ASP A 1 256 ? 30.831  7.115   10.804  1.00 74.75  ? 256 ASP A OD1 1 
ATOM   2041  O OD2 . ASP A 1 256 ? 31.154  7.355   12.969  1.00 80.83  ? 256 ASP A OD2 1 
ATOM   2042  N N   . LEU A 1 257 ? 29.994  12.293  10.568  1.00 59.97  ? 257 LEU A N   1 
ATOM   2043  C CA  . LEU A 1 257 ? 29.632  13.660  10.939  1.00 59.74  ? 257 LEU A CA  1 
ATOM   2044  C C   . LEU A 1 257 ? 28.322  14.127  10.267  1.00 59.28  ? 257 LEU A C   1 
ATOM   2045  O O   . LEU A 1 257 ? 27.508  14.803  10.896  1.00 58.01  ? 257 LEU A O   1 
ATOM   2046  C CB  . LEU A 1 257 ? 30.832  14.568  10.658  1.00 59.25  ? 257 LEU A CB  1 
ATOM   2047  C CG  . LEU A 1 257 ? 32.046  14.345  11.584  1.00 59.74  ? 257 LEU A CG  1 
ATOM   2048  C CD1 . LEU A 1 257 ? 33.408  14.720  10.997  1.00 59.10  ? 257 LEU A CD1 1 
ATOM   2049  C CD2 . LEU A 1 257 ? 31.900  15.058  12.934  1.00 60.03  ? 257 LEU A CD2 1 
ATOM   2050  N N   . ILE A 1 258 ? 28.101  13.769  8.996   1.00 58.80  ? 258 ILE A N   1 
ATOM   2051  C CA  . ILE A 1 258 ? 26.815  13.976  8.341   1.00 58.95  ? 258 ILE A CA  1 
ATOM   2052  C C   . ILE A 1 258 ? 25.718  13.286  9.156   1.00 59.59  ? 258 ILE A C   1 
ATOM   2053  O O   . ILE A 1 258 ? 24.637  13.859  9.390   1.00 60.12  ? 258 ILE A O   1 
ATOM   2054  C CB  . ILE A 1 258 ? 26.856  13.446  6.895   1.00 58.74  ? 258 ILE A CB  1 
ATOM   2055  C CG1 . ILE A 1 258 ? 27.745  14.284  6.023   1.00 59.49  ? 258 ILE A CG1 1 
ATOM   2056  C CG2 . ILE A 1 258 ? 25.473  13.348  6.277   1.00 58.82  ? 258 ILE A CG2 1 
ATOM   2057  C CD1 . ILE A 1 258 ? 27.982  13.699  4.641   1.00 59.86  ? 258 ILE A CD1 1 
ATOM   2058  N N   . ASP A 1 259 ? 26.007  12.059  9.599   1.00 58.77  ? 259 ASP A N   1 
ATOM   2059  C CA  . ASP A 1 259 ? 25.047  11.303  10.383  1.00 60.40  ? 259 ASP A CA  1 
ATOM   2060  C C   . ASP A 1 259 ? 24.743  12.084  11.660  1.00 61.45  ? 259 ASP A C   1 
ATOM   2061  O O   . ASP A 1 259 ? 23.604  12.108  12.127  1.00 65.97  ? 259 ASP A O   1 
ATOM   2062  C CB  . ASP A 1 259 ? 25.465  9.850   10.568  1.00 60.45  ? 259 ASP A CB  1 
ATOM   2063  C CG  . ASP A 1 259 ? 25.637  9.057   9.276   1.00 60.95  ? 259 ASP A CG  1 
ATOM   2064  O OD1 . ASP A 1 259 ? 25.017  9.445   8.260   1.00 60.56  ? 259 ASP A OD1 1 
ATOM   2065  O OD2 . ASP A 1 259 ? 26.424  8.068   9.272   1.00 61.95  ? 259 ASP A OD2 1 
ATOM   2066  N N   . ALA A 1 260 ? 25.737  12.786  12.199  1.00 59.76  ? 260 ALA A N   1 
ATOM   2067  C CA  . ALA A 1 260 ? 25.474  13.604  13.371  1.00 59.49  ? 260 ALA A CA  1 
ATOM   2068  C C   . ALA A 1 260 ? 24.643  14.837  13.007  1.00 57.81  ? 260 ALA A C   1 
ATOM   2069  O O   . ALA A 1 260 ? 24.187  15.510  13.919  1.00 57.70  ? 260 ALA A O   1 
ATOM   2070  C CB  . ALA A 1 260 ? 26.795  13.979  14.034  1.00 60.13  ? 260 ALA A CB  1 
ATOM   2071  N N   . GLY A 1 261 ? 24.509  15.148  11.702  1.00 56.91  ? 261 GLY A N   1 
ATOM   2072  C CA  . GLY A 1 261 ? 23.595  16.165  11.185  1.00 57.50  ? 261 GLY A CA  1 
ATOM   2073  C C   . GLY A 1 261 ? 24.284  17.424  10.655  1.00 57.75  ? 261 GLY A C   1 
ATOM   2074  O O   . GLY A 1 261 ? 23.691  18.493  10.585  1.00 56.98  ? 261 GLY A O   1 
ATOM   2075  N N   . ALA A 1 262 ? 25.558  17.303  10.287  1.00 58.46  ? 262 ALA A N   1 
ATOM   2076  C CA  . ALA A 1 262 ? 26.310  18.414  9.738   1.00 59.01  ? 262 ALA A CA  1 
ATOM   2077  C C   . ALA A 1 262 ? 25.793  18.798  8.360   1.00 59.58  ? 262 ALA A C   1 
ATOM   2078  O O   . ALA A 1 262 ? 25.525  17.932  7.548   1.00 61.52  ? 262 ALA A O   1 
ATOM   2079  C CB  . ALA A 1 262 ? 27.755  18.014  9.644   1.00 59.17  ? 262 ALA A CB  1 
ATOM   2080  N N   . VAL A 1 263 ? 25.715  20.095  8.065   1.00 59.77  ? 263 VAL A N   1 
ATOM   2081  C CA  . VAL A 1 263 ? 25.304  20.494  6.733   1.00 59.47  ? 263 VAL A CA  1 
ATOM   2082  C C   . VAL A 1 263 ? 26.462  21.235  6.067   1.00 58.70  ? 263 VAL A C   1 
ATOM   2083  O O   . VAL A 1 263 ? 26.323  21.736  4.948   1.00 58.56  ? 263 VAL A O   1 
ATOM   2084  C CB  . VAL A 1 263 ? 23.962  21.261  6.771   1.00 60.76  ? 263 VAL A CB  1 
ATOM   2085  C CG1 . VAL A 1 263 ? 22.956  20.636  7.751   1.00 60.76  ? 263 VAL A CG1 1 
ATOM   2086  C CG2 . VAL A 1 263 ? 24.123  22.747  7.063   1.00 61.13  ? 263 VAL A CG2 1 
ATOM   2087  N N   . GLY A 1 264 ? 27.627  21.220  6.738   1.00 58.39  ? 264 GLY A N   1 
ATOM   2088  C CA  . GLY A 1 264 ? 28.869  21.734  6.170   1.00 58.72  ? 264 GLY A CA  1 
ATOM   2089  C C   . GLY A 1 264 ? 30.112  21.033  6.727   1.00 58.92  ? 264 GLY A C   1 
ATOM   2090  O O   . GLY A 1 264 ? 30.255  20.846  7.939   1.00 59.15  ? 264 GLY A O   1 
ATOM   2091  N N   . MET A 1 265 ? 31.054  20.701  5.834   1.00 59.26  ? 265 MET A N   1 
ATOM   2092  C CA  . MET A 1 265 ? 32.204  19.893  6.201   1.00 59.23  ? 265 MET A CA  1 
ATOM   2093  C C   . MET A 1 265 ? 33.489  20.592  5.791   1.00 59.04  ? 265 MET A C   1 
ATOM   2094  O O   . MET A 1 265 ? 33.655  20.974  4.632   1.00 58.87  ? 265 MET A O   1 
ATOM   2095  C CB  . MET A 1 265 ? 32.152  18.519  5.516   1.00 60.09  ? 265 MET A CB  1 
ATOM   2096  C CG  . MET A 1 265 ? 30.912  17.737  5.862   1.00 60.44  ? 265 MET A CG  1 
ATOM   2097  S SD  . MET A 1 265 ? 30.916  17.327  7.617   1.00 62.15  ? 265 MET A SD  1 
ATOM   2098  C CE  . MET A 1 265 ? 31.903  15.837  7.447   1.00 62.21  ? 265 MET A CE  1 
ATOM   2099  N N   . CYS A 1 266 ? 34.399  20.685  6.765   1.00 59.50  ? 266 CYS A N   1 
ATOM   2100  C CA  . CYS A 1 266 ? 35.744  21.208  6.573   1.00 59.97  ? 266 CYS A CA  1 
ATOM   2101  C C   . CYS A 1 266 ? 36.770  20.141  6.971   1.00 59.22  ? 266 CYS A C   1 
ATOM   2102  O O   . CYS A 1 266 ? 37.394  20.239  8.029   1.00 59.62  ? 266 CYS A O   1 
ATOM   2103  C CB  . CYS A 1 266 ? 35.913  22.500  7.370   1.00 60.35  ? 266 CYS A CB  1 
ATOM   2104  S SG  . CYS A 1 266 ? 34.799  23.813  6.803   1.00 62.75  ? 266 CYS A SG  1 
ATOM   2105  N N   . PRO A 1 267 ? 36.990  19.073  6.168   1.00 57.93  ? 267 PRO A N   1 
ATOM   2106  C CA  . PRO A 1 267 ? 38.095  18.147  6.428   1.00 58.03  ? 267 PRO A CA  1 
ATOM   2107  C C   . PRO A 1 267 ? 39.401  18.921  6.652   1.00 58.97  ? 267 PRO A C   1 
ATOM   2108  O O   . PRO A 1 267 ? 39.587  19.975  6.038   1.00 58.89  ? 267 PRO A O   1 
ATOM   2109  C CB  . PRO A 1 267 ? 38.132  17.247  5.180   1.00 57.16  ? 267 PRO A CB  1 
ATOM   2110  C CG  . PRO A 1 267 ? 37.297  17.973  4.164   1.00 57.20  ? 267 PRO A CG  1 
ATOM   2111  C CD  . PRO A 1 267 ? 36.219  18.700  4.976   1.00 57.40  ? 267 PRO A CD  1 
ATOM   2112  N N   . PHE A 1 268 ? 40.292  18.377  7.509   1.00 59.87  ? 268 PHE A N   1 
ATOM   2113  C CA  . PHE A 1 268 ? 41.450  19.109  8.004   1.00 61.42  ? 268 PHE A CA  1 
ATOM   2114  C C   . PHE A 1 268 ? 42.650  18.966  7.053   1.00 62.29  ? 268 PHE A C   1 
ATOM   2115  O O   . PHE A 1 268 ? 43.180  17.877  6.839   1.00 59.23  ? 268 PHE A O   1 
ATOM   2116  C CB  . PHE A 1 268 ? 41.942  18.820  9.432   1.00 62.16  ? 268 PHE A CB  1 
ATOM   2117  C CG  . PHE A 1 268 ? 43.156  19.664  9.833   1.00 62.85  ? 268 PHE A CG  1 
ATOM   2118  C CD1 . PHE A 1 268 ? 43.172  21.053  9.641   1.00 62.77  ? 268 PHE A CD1 1 
ATOM   2119  C CD2 . PHE A 1 268 ? 44.327  19.060  10.321  1.00 63.80  ? 268 PHE A CD2 1 
ATOM   2120  C CE1 . PHE A 1 268 ? 44.308  21.813  9.962   1.00 64.29  ? 268 PHE A CE1 1 
ATOM   2121  C CE2 . PHE A 1 268 ? 45.457  19.824  10.657  1.00 65.03  ? 268 PHE A CE2 1 
ATOM   2122  C CZ  . PHE A 1 268 ? 45.452  21.203  10.477  1.00 64.82  ? 268 PHE A CZ  1 
ATOM   2123  N N   . TYR A 1 269 ? 42.995  20.150  6.488   1.00 64.26  ? 269 TYR A N   1 
ATOM   2124  C CA  . TYR A 1 269 ? 44.287  20.555  5.959   1.00 64.38  ? 269 TYR A CA  1 
ATOM   2125  C C   . TYR A 1 269 ? 44.483  19.918  4.582   1.00 62.76  ? 269 TYR A C   1 
ATOM   2126  O O   . TYR A 1 269 ? 44.555  18.696  4.469   1.00 61.97  ? 269 TYR A O   1 
ATOM   2127  C CB  . TYR A 1 269 ? 45.351  20.240  7.023   1.00 66.84  ? 269 TYR A CB  1 
ATOM   2128  C CG  . TYR A 1 269 ? 46.524  21.213  7.143   1.00 68.52  ? 269 TYR A CG  1 
ATOM   2129  C CD1 . TYR A 1 269 ? 46.386  22.568  6.858   1.00 69.41  ? 269 TYR A CD1 1 
ATOM   2130  C CD2 . TYR A 1 269 ? 47.781  20.760  7.544   1.00 69.33  ? 269 TYR A CD2 1 
ATOM   2131  C CE1 . TYR A 1 269 ? 47.474  23.427  6.946   1.00 72.79  ? 269 TYR A CE1 1 
ATOM   2132  C CE2 . TYR A 1 269 ? 48.876  21.606  7.650   1.00 70.93  ? 269 TYR A CE2 1 
ATOM   2133  C CZ  . TYR A 1 269 ? 48.735  22.950  7.333   1.00 73.99  ? 269 TYR A CZ  1 
ATOM   2134  O OH  . TYR A 1 269 ? 49.826  23.810  7.399   1.00 73.83  ? 269 TYR A OH  1 
ATOM   2135  N N   . TYR A 1 270 ? 44.482  20.788  3.556   1.00 61.15  ? 270 TYR A N   1 
ATOM   2136  C CA  . TYR A 1 270 ? 45.116  20.578  2.252   1.00 60.56  ? 270 TYR A CA  1 
ATOM   2137  C C   . TYR A 1 270 ? 46.555  20.029  2.356   1.00 60.65  ? 270 TYR A C   1 
ATOM   2138  O O   . TYR A 1 270 ? 46.797  18.913  1.931   1.00 59.99  ? 270 TYR A O   1 
ATOM   2139  C CB  . TYR A 1 270 ? 45.050  21.944  1.545   1.00 60.35  ? 270 TYR A CB  1 
ATOM   2140  C CG  . TYR A 1 270 ? 45.887  22.171  0.285   1.00 60.58  ? 270 TYR A CG  1 
ATOM   2141  C CD1 . TYR A 1 270 ? 45.595  21.517  -0.906  1.00 60.10  ? 270 TYR A CD1 1 
ATOM   2142  C CD2 . TYR A 1 270 ? 46.915  23.106  0.259   1.00 61.11  ? 270 TYR A CD2 1 
ATOM   2143  C CE1 . TYR A 1 270 ? 46.322  21.743  -2.064  1.00 60.70  ? 270 TYR A CE1 1 
ATOM   2144  C CE2 . TYR A 1 270 ? 47.647  23.345  -0.896  1.00 61.77  ? 270 TYR A CE2 1 
ATOM   2145  C CZ  . TYR A 1 270 ? 47.345  22.665  -2.062  1.00 61.61  ? 270 TYR A CZ  1 
ATOM   2146  O OH  . TYR A 1 270 ? 48.009  22.873  -3.235  1.00 62.41  ? 270 TYR A OH  1 
ATOM   2147  N N   . ALA A 1 271 ? 47.523  20.822  2.851   1.00 61.34  ? 271 ALA A N   1 
ATOM   2148  C CA  . ALA A 1 271 ? 48.939  20.457  2.793   1.00 62.65  ? 271 ALA A CA  1 
ATOM   2149  C C   . ALA A 1 271 ? 49.589  20.473  4.180   1.00 63.18  ? 271 ALA A C   1 
ATOM   2150  O O   . ALA A 1 271 ? 49.057  21.067  5.109   1.00 62.56  ? 271 ALA A O   1 
ATOM   2151  C CB  . ALA A 1 271 ? 49.674  21.353  1.827   1.00 63.55  ? 271 ALA A CB  1 
ATOM   2152  N N   . ASP A 1 272 ? 50.708  19.755  4.332   1.00 64.67  ? 272 ASP A N   1 
ATOM   2153  C CA  . ASP A 1 272 ? 51.423  19.715  5.594   1.00 66.47  ? 272 ASP A CA  1 
ATOM   2154  C C   . ASP A 1 272 ? 52.019  21.097  5.900   1.00 68.54  ? 272 ASP A C   1 
ATOM   2155  O O   . ASP A 1 272 ? 52.098  21.997  5.048   1.00 69.72  ? 272 ASP A O   1 
ATOM   2156  C CB  . ASP A 1 272 ? 52.600  18.762  5.538   1.00 68.64  ? 272 ASP A CB  1 
ATOM   2157  C CG  . ASP A 1 272 ? 52.375  17.246  5.507   1.00 69.67  ? 272 ASP A CG  1 
ATOM   2158  O OD1 . ASP A 1 272 ? 51.217  16.755  5.630   1.00 69.67  ? 272 ASP A OD1 1 
ATOM   2159  O OD2 . ASP A 1 272 ? 53.401  16.533  5.362   1.00 71.77  ? 272 ASP A OD2 1 
ATOM   2160  N N   . GLY A 1 273 ? 52.443  21.263  7.155   1.00 68.50  ? 273 GLY A N   1 
ATOM   2161  C CA  . GLY A 1 273 ? 53.072  22.484  7.613   1.00 68.15  ? 273 GLY A CA  1 
ATOM   2162  C C   . GLY A 1 273 ? 54.180  22.139  8.596   1.00 68.93  ? 273 GLY A C   1 
ATOM   2163  O O   . GLY A 1 273 ? 53.888  21.840  9.758   1.00 67.39  ? 273 GLY A O   1 
ATOM   2164  N N   . TRP A 1 274 ? 55.433  22.203  8.110   1.00 70.44  ? 274 TRP A N   1 
ATOM   2165  C CA  . TRP A 1 274 ? 56.583  21.749  8.871   1.00 72.42  ? 274 TRP A CA  1 
ATOM   2166  C C   . TRP A 1 274 ? 56.810  22.619  10.107  1.00 74.10  ? 274 TRP A C   1 
ATOM   2167  O O   . TRP A 1 274 ? 57.640  22.257  10.953  1.00 77.71  ? 274 TRP A O   1 
ATOM   2168  C CB  . TRP A 1 274 ? 57.852  21.716  7.995   1.00 74.08  ? 274 TRP A CB  1 
ATOM   2169  C CG  . TRP A 1 274 ? 57.805  20.738  6.842   1.00 73.21  ? 274 TRP A CG  1 
ATOM   2170  C CD1 . TRP A 1 274 ? 56.704  20.092  6.367   1.00 70.97  ? 274 TRP A CD1 1 
ATOM   2171  C CD2 . TRP A 1 274 ? 58.900  20.308  6.001   1.00 73.80  ? 274 TRP A CD2 1 
ATOM   2172  N NE1 . TRP A 1 274 ? 57.028  19.321  5.289   1.00 70.85  ? 274 TRP A NE1 1 
ATOM   2173  C CE2 . TRP A 1 274 ? 58.366  19.429  5.039   1.00 72.61  ? 274 TRP A CE2 1 
ATOM   2174  C CE3 . TRP A 1 274 ? 60.271  20.575  5.963   1.00 75.96  ? 274 TRP A CE3 1 
ATOM   2175  C CZ2 . TRP A 1 274 ? 59.145  18.815  4.064   1.00 73.33  ? 274 TRP A CZ2 1 
ATOM   2176  C CZ3 . TRP A 1 274 ? 61.045  19.978  4.991   1.00 76.60  ? 274 TRP A CZ3 1 
ATOM   2177  C CH2 . TRP A 1 274 ? 60.480  19.117  4.049   1.00 75.54  ? 274 TRP A CH2 1 
ATOM   2178  N N   . TRP A 1 275 ? 56.117  23.770  10.177  1.00 73.37  ? 275 TRP A N   1 
ATOM   2179  C CA  . TRP A 1 275 ? 56.310  24.754  11.226  1.00 73.95  ? 275 TRP A CA  1 
ATOM   2180  C C   . TRP A 1 275 ? 55.531  24.428  12.489  1.00 73.28  ? 275 TRP A C   1 
ATOM   2181  O O   . TRP A 1 275 ? 55.801  24.977  13.556  1.00 71.99  ? 275 TRP A O   1 
ATOM   2182  C CB  . TRP A 1 275 ? 55.857  26.110  10.706  1.00 74.65  ? 275 TRP A CB  1 
ATOM   2183  C CG  . TRP A 1 275 ? 54.376  26.207  10.446  1.00 73.26  ? 275 TRP A CG  1 
ATOM   2184  C CD1 . TRP A 1 275 ? 53.752  25.969  9.257   1.00 72.49  ? 275 TRP A CD1 1 
ATOM   2185  C CD2 . TRP A 1 275 ? 53.340  26.605  11.375  1.00 71.93  ? 275 TRP A CD2 1 
ATOM   2186  N NE1 . TRP A 1 275 ? 52.409  26.221  9.369   1.00 71.60  ? 275 TRP A NE1 1 
ATOM   2187  C CE2 . TRP A 1 275 ? 52.121  26.581  10.658  1.00 71.13  ? 275 TRP A CE2 1 
ATOM   2188  C CE3 . TRP A 1 275 ? 53.319  26.962  12.729  1.00 71.60  ? 275 TRP A CE3 1 
ATOM   2189  C CZ2 . TRP A 1 275 ? 50.896  26.872  11.254  1.00 69.80  ? 275 TRP A CZ2 1 
ATOM   2190  C CZ3 . TRP A 1 275 ? 52.113  27.275  13.313  1.00 70.65  ? 275 TRP A CZ3 1 
ATOM   2191  C CH2 . TRP A 1 275 ? 50.915  27.204  12.592  1.00 69.95  ? 275 TRP A CH2 1 
ATOM   2192  N N   . LYS A 1 276 ? 54.544  23.541  12.341  1.00 74.56  ? 276 LYS A N   1 
ATOM   2193  C CA  . LYS A 1 276 ? 53.599  23.261  13.408  1.00 75.29  ? 276 LYS A CA  1 
ATOM   2194  C C   . LYS A 1 276 ? 54.289  22.452  14.505  1.00 77.25  ? 276 LYS A C   1 
ATOM   2195  O O   . LYS A 1 276 ? 53.723  22.288  15.576  1.00 77.92  ? 276 LYS A O   1 
ATOM   2196  C CB  . LYS A 1 276 ? 52.336  22.560  12.887  1.00 74.14  ? 276 LYS A CB  1 
ATOM   2197  C CG  . LYS A 1 276 ? 51.581  23.314  11.796  1.00 73.97  ? 276 LYS A CG  1 
ATOM   2198  C CD  . LYS A 1 276 ? 50.415  22.563  11.150  1.00 73.15  ? 276 LYS A CD  1 
ATOM   2199  C CE  . LYS A 1 276 ? 49.246  22.337  12.055  1.00 73.08  ? 276 LYS A CE  1 
ATOM   2200  N NZ  . LYS A 1 276 ? 48.673  23.595  12.564  1.00 74.26  ? 276 LYS A NZ  1 
ATOM   2201  N N   . GLY A 1 277 ? 55.496  21.936  14.248  1.00 79.76  ? 277 GLY A N   1 
ATOM   2202  C CA  . GLY A 1 277 ? 56.140  21.030  15.184  1.00 82.39  ? 277 GLY A CA  1 
ATOM   2203  C C   . GLY A 1 277 ? 57.382  21.631  15.837  1.00 86.58  ? 277 GLY A C   1 
ATOM   2204  O O   . GLY A 1 277 ? 57.945  21.023  16.738  1.00 90.98  ? 277 GLY A O   1 
ATOM   2205  N N   . GLY A 1 278 ? 57.813  22.815  15.399  1.00 87.29  ? 278 GLY A N   1 
ATOM   2206  C CA  . GLY A 1 278 ? 58.822  23.539  16.142  1.00 88.98  ? 278 GLY A CA  1 
ATOM   2207  C C   . GLY A 1 278 ? 59.896  24.166  15.259  1.00 91.51  ? 278 GLY A C   1 
ATOM   2208  O O   . GLY A 1 278 ? 60.581  25.067  15.721  1.00 92.08  ? 278 GLY A O   1 
ATOM   2209  N N   . GLU A 1 279 ? 60.074  23.673  14.027  1.00 93.46  ? 279 GLU A N   1 
ATOM   2210  C CA  . GLU A 1 279 ? 61.163  24.142  13.181  1.00 95.54  ? 279 GLU A CA  1 
ATOM   2211  C C   . GLU A 1 279 ? 60.735  24.059  11.720  1.00 96.59  ? 279 GLU A C   1 
ATOM   2212  O O   . GLU A 1 279 ? 60.585  22.974  11.177  1.00 104.35 ? 279 GLU A O   1 
ATOM   2213  C CB  . GLU A 1 279 ? 62.433  23.323  13.390  1.00 96.73  ? 279 GLU A CB  1 
ATOM   2214  C CG  . GLU A 1 279 ? 63.711  24.152  13.570  1.00 104.65 ? 279 GLU A CG  1 
ATOM   2215  C CD  . GLU A 1 279 ? 64.077  25.315  12.633  1.00 108.75 ? 279 GLU A CD  1 
ATOM   2216  O OE1 . GLU A 1 279 ? 64.617  26.342  13.129  1.00 109.23 ? 279 GLU A OE1 1 
ATOM   2217  O OE2 . GLU A 1 279 ? 63.841  25.229  11.407  1.00 113.27 ? 279 GLU A OE2 1 
ATOM   2218  N N   . LYS A 1 280 ? 60.570  25.224  11.092  1.00 95.70  ? 280 LYS A N   1 
ATOM   2219  C CA  . LYS A 1 280 ? 59.960  25.358  9.777   1.00 92.29  ? 280 LYS A CA  1 
ATOM   2220  C C   . LYS A 1 280 ? 60.757  24.610  8.714   1.00 88.66  ? 280 LYS A C   1 
ATOM   2221  O O   . LYS A 1 280 ? 60.315  24.452  7.583   1.00 85.63  ? 280 LYS A O   1 
ATOM   2222  C CB  . LYS A 1 280 ? 59.985  26.813  9.292   1.00 94.48  ? 280 LYS A CB  1 
ATOM   2223  C CG  . LYS A 1 280 ? 60.205  27.884  10.346  1.00 95.95  ? 280 LYS A CG  1 
ATOM   2224  C CD  . LYS A 1 280 ? 61.199  28.925  9.859   1.00 99.52  ? 280 LYS A CD  1 
ATOM   2225  C CE  . LYS A 1 280 ? 60.632  30.258  9.488   1.00 99.65  ? 280 LYS A CE  1 
ATOM   2226  N NZ  . LYS A 1 280 ? 61.081  31.288  10.434  1.00 99.46  ? 280 LYS A NZ  1 
ATOM   2227  N N   . SER A 1 281 ? 61.975  24.211  9.053   1.00 89.06  ? 281 SER A N   1 
ATOM   2228  C CA  . SER A 1 281 ? 62.869  23.665  8.044   1.00 90.20  ? 281 SER A CA  1 
ATOM   2229  C C   . SER A 1 281 ? 63.062  22.164  8.261   1.00 91.58  ? 281 SER A C   1 
ATOM   2230  O O   . SER A 1 281 ? 63.660  21.490  7.426   1.00 96.82  ? 281 SER A O   1 
ATOM   2231  C CB  . SER A 1 281 ? 64.196  24.405  8.014   1.00 90.07  ? 281 SER A CB  1 
ATOM   2232  O OG  . SER A 1 281 ? 64.056  25.800  8.267   1.00 88.64  ? 281 SER A OG  1 
ATOM   2233  N N   . ASP A 1 282 ? 62.570  21.654  9.393   1.00 90.27  ? 282 ASP A N   1 
ATOM   2234  C CA  . ASP A 1 282 ? 62.637  20.243  9.700   1.00 90.13  ? 282 ASP A CA  1 
ATOM   2235  C C   . ASP A 1 282 ? 61.225  19.658  9.606   1.00 87.76  ? 282 ASP A C   1 
ATOM   2236  O O   . ASP A 1 282 ? 60.223  20.252  10.078  1.00 82.42  ? 282 ASP A O   1 
ATOM   2237  C CB  . ASP A 1 282 ? 63.330  20.070  11.036  1.00 94.65  ? 282 ASP A CB  1 
ATOM   2238  C CG  . ASP A 1 282 ? 63.624  18.636  11.425  1.00 100.76 ? 282 ASP A CG  1 
ATOM   2239  O OD1 . ASP A 1 282 ? 64.427  17.993  10.715  1.00 106.97 ? 282 ASP A OD1 1 
ATOM   2240  O OD2 . ASP A 1 282 ? 63.031  18.180  12.426  1.00 107.24 ? 282 ASP A OD2 1 
ATOM   2241  N N   . HIS A 1 283 ? 61.168  18.503  8.919   1.00 86.94  ? 283 HIS A N   1 
ATOM   2242  C CA  . HIS A 1 283 ? 59.993  17.647  8.911   1.00 84.24  ? 283 HIS A CA  1 
ATOM   2243  C C   . HIS A 1 283 ? 60.213  16.599  9.999   1.00 82.23  ? 283 HIS A C   1 
ATOM   2244  O O   . HIS A 1 283 ? 60.531  15.456  9.706   1.00 82.46  ? 283 HIS A O   1 
ATOM   2245  C CB  . HIS A 1 283 ? 59.719  17.071  7.511   1.00 84.74  ? 283 HIS A CB  1 
ATOM   2246  C CG  . HIS A 1 283 ? 58.278  16.827  7.201   1.00 84.68  ? 283 HIS A CG  1 
ATOM   2247  N ND1 . HIS A 1 283 ? 57.238  17.265  7.999   1.00 83.49  ? 283 HIS A ND1 1 
ATOM   2248  C CD2 . HIS A 1 283 ? 57.694  16.191  6.164   1.00 86.04  ? 283 HIS A CD2 1 
ATOM   2249  C CE1 . HIS A 1 283 ? 56.077  16.894  7.462   1.00 81.30  ? 283 HIS A CE1 1 
ATOM   2250  N NE2 . HIS A 1 283 ? 56.318  16.264  6.334   1.00 82.31  ? 283 HIS A NE2 1 
ATOM   2251  N N   . SER A 1 284 ? 60.067  17.033  11.257  1.00 80.62  ? 284 SER A N   1 
ATOM   2252  C CA  . SER A 1 284 ? 60.162  16.172  12.422  1.00 80.08  ? 284 SER A CA  1 
ATOM   2253  C C   . SER A 1 284 ? 59.366  14.882  12.213  1.00 77.49  ? 284 SER A C   1 
ATOM   2254  O O   . SER A 1 284 ? 58.225  14.894  11.751  1.00 75.59  ? 284 SER A O   1 
ATOM   2255  C CB  . SER A 1 284 ? 59.729  16.912  13.673  1.00 80.02  ? 284 SER A CB  1 
ATOM   2256  O OG  . SER A 1 284 ? 59.578  16.029  14.777  1.00 80.49  ? 284 SER A OG  1 
ATOM   2257  N N   . LEU A 1 285 ? 60.014  13.763  12.550  1.00 77.68  ? 285 LEU A N   1 
ATOM   2258  C CA  . LEU A 1 285 ? 59.495  12.440  12.254  1.00 76.80  ? 285 LEU A CA  1 
ATOM   2259  C C   . LEU A 1 285 ? 58.509  12.060  13.349  1.00 76.16  ? 285 LEU A C   1 
ATOM   2260  O O   . LEU A 1 285 ? 57.689  11.168  13.153  1.00 75.56  ? 285 LEU A O   1 
ATOM   2261  C CB  . LEU A 1 285 ? 60.603  11.385  12.123  1.00 78.03  ? 285 LEU A CB  1 
ATOM   2262  C CG  . LEU A 1 285 ? 61.636  11.580  11.003  1.00 78.90  ? 285 LEU A CG  1 
ATOM   2263  C CD1 . LEU A 1 285 ? 62.613  10.451  11.014  1.00 79.78  ? 285 LEU A CD1 1 
ATOM   2264  C CD2 . LEU A 1 285 ? 61.038  11.725  9.599   1.00 78.05  ? 285 LEU A CD2 1 
ATOM   2265  N N   . ASN A 1 286 ? 58.588  12.741  14.494  1.00 76.76  ? 286 ASN A N   1 
ATOM   2266  C CA  . ASN A 1 286 ? 57.774  12.352  15.626  1.00 76.68  ? 286 ASN A CA  1 
ATOM   2267  C C   . ASN A 1 286 ? 56.914  13.529  16.059  1.00 75.63  ? 286 ASN A C   1 
ATOM   2268  O O   . ASN A 1 286 ? 56.540  13.612  17.227  1.00 75.79  ? 286 ASN A O   1 
ATOM   2269  C CB  . ASN A 1 286 ? 58.639  11.830  16.760  1.00 79.05  ? 286 ASN A CB  1 
ATOM   2270  C CG  . ASN A 1 286 ? 59.429  12.958  17.362  1.00 80.91  ? 286 ASN A CG  1 
ATOM   2271  O OD1 . ASN A 1 286 ? 59.884  13.833  16.621  1.00 82.92  ? 286 ASN A OD1 1 
ATOM   2272  N ND2 . ASN A 1 286 ? 59.567  12.980  18.679  1.00 81.86  ? 286 ASN A ND2 1 
ATOM   2273  N N   . GLN A 1 287 ? 56.588  14.400  15.090  1.00 74.83  ? 287 GLN A N   1 
ATOM   2274  C CA  . GLN A 1 287 ? 55.701  15.533  15.306  1.00 72.97  ? 287 GLN A CA  1 
ATOM   2275  C C   . GLN A 1 287 ? 54.429  15.343  14.478  1.00 70.32  ? 287 GLN A C   1 
ATOM   2276  O O   . GLN A 1 287 ? 54.345  15.730  13.311  1.00 69.38  ? 287 GLN A O   1 
ATOM   2277  C CB  . GLN A 1 287 ? 56.372  16.874  14.997  1.00 73.71  ? 287 GLN A CB  1 
ATOM   2278  C CG  . GLN A 1 287 ? 57.392  17.330  16.034  1.00 75.77  ? 287 GLN A CG  1 
ATOM   2279  C CD  . GLN A 1 287 ? 56.831  17.589  17.416  1.00 76.02  ? 287 GLN A CD  1 
ATOM   2280  O OE1 . GLN A 1 287 ? 55.628  17.558  17.665  1.00 75.09  ? 287 GLN A OE1 1 
ATOM   2281  N NE2 . GLN A 1 287 ? 57.715  17.877  18.351  1.00 78.14  ? 287 GLN A NE2 1 
ATOM   2282  N N   . PRO A 1 288 ? 53.381  14.754  15.085  1.00 68.76  ? 288 PRO A N   1 
ATOM   2283  C CA  . PRO A 1 288 ? 52.063  14.657  14.438  1.00 67.08  ? 288 PRO A CA  1 
ATOM   2284  C C   . PRO A 1 288 ? 51.591  15.913  13.699  1.00 66.33  ? 288 PRO A C   1 
ATOM   2285  O O   . PRO A 1 288 ? 51.003  15.818  12.625  1.00 64.91  ? 288 PRO A O   1 
ATOM   2286  C CB  . PRO A 1 288 ? 51.140  14.324  15.622  1.00 66.29  ? 288 PRO A CB  1 
ATOM   2287  C CG  . PRO A 1 288 ? 52.027  13.548  16.577  1.00 67.79  ? 288 PRO A CG  1 
ATOM   2288  C CD  . PRO A 1 288 ? 53.429  14.146  16.427  1.00 68.99  ? 288 PRO A CD  1 
ATOM   2289  N N   . GLU A 1 289 ? 51.858  17.101  14.252  1.00 66.86  ? 289 GLU A N   1 
ATOM   2290  C CA  . GLU A 1 289 ? 51.192  18.283  13.722  1.00 66.70  ? 289 GLU A CA  1 
ATOM   2291  C C   . GLU A 1 289 ? 51.693  18.576  12.309  1.00 66.14  ? 289 GLU A C   1 
ATOM   2292  O O   . GLU A 1 289 ? 51.006  19.182  11.465  1.00 64.44  ? 289 GLU A O   1 
ATOM   2293  C CB  . GLU A 1 289 ? 51.326  19.449  14.702  1.00 67.98  ? 289 GLU A CB  1 
ATOM   2294  C CG  . GLU A 1 289 ? 50.447  19.296  15.946  1.00 68.15  ? 289 GLU A CG  1 
ATOM   2295  C CD  . GLU A 1 289 ? 48.929  19.266  15.753  1.00 67.09  ? 289 GLU A CD  1 
ATOM   2296  O OE1 . GLU A 1 289 ? 48.371  20.250  15.229  1.00 68.19  ? 289 GLU A OE1 1 
ATOM   2297  O OE2 . GLU A 1 289 ? 48.278  18.288  16.169  1.00 67.16  ? 289 GLU A OE2 1 
ATOM   2298  N N   . GLU A 1 290 ? 52.893  18.072  12.040  1.00 67.11  ? 290 GLU A N   1 
ATOM   2299  C CA  . GLU A 1 290 ? 53.510  18.333  10.763  1.00 67.68  ? 290 GLU A CA  1 
ATOM   2300  C C   . GLU A 1 290 ? 52.982  17.390  9.681   1.00 67.20  ? 290 GLU A C   1 
ATOM   2301  O O   . GLU A 1 290 ? 53.361  17.536  8.534   1.00 68.11  ? 290 GLU A O   1 
ATOM   2302  C CB  . GLU A 1 290 ? 55.020  18.261  10.942  1.00 69.39  ? 290 GLU A CB  1 
ATOM   2303  C CG  . GLU A 1 290 ? 55.562  19.245  11.978  1.00 70.37  ? 290 GLU A CG  1 
ATOM   2304  C CD  . GLU A 1 290 ? 57.075  19.223  12.043  1.00 72.44  ? 290 GLU A CD  1 
ATOM   2305  O OE1 . GLU A 1 290 ? 57.635  18.527  11.174  1.00 72.56  ? 290 GLU A OE1 1 
ATOM   2306  O OE2 . GLU A 1 290 ? 57.697  19.855  12.927  1.00 74.64  ? 290 GLU A OE2 1 
ATOM   2307  N N   . TRP A 1 291 ? 52.076  16.455  9.972   1.00 66.23  ? 291 TRP A N   1 
ATOM   2308  C CA  . TRP A 1 291 ? 51.753  15.482  8.937   1.00 66.05  ? 291 TRP A CA  1 
ATOM   2309  C C   . TRP A 1 291 ? 50.251  15.329  8.718   1.00 64.06  ? 291 TRP A C   1 
ATOM   2310  O O   . TRP A 1 291 ? 49.785  14.224  8.472   1.00 64.92  ? 291 TRP A O   1 
ATOM   2311  C CB  . TRP A 1 291 ? 52.397  14.121  9.276   1.00 67.19  ? 291 TRP A CB  1 
ATOM   2312  C CG  . TRP A 1 291 ? 53.904  14.114  9.353   1.00 68.73  ? 291 TRP A CG  1 
ATOM   2313  C CD1 . TRP A 1 291 ? 54.674  14.545  10.393  1.00 70.42  ? 291 TRP A CD1 1 
ATOM   2314  C CD2 . TRP A 1 291 ? 54.826  13.620  8.356   1.00 69.70  ? 291 TRP A CD2 1 
ATOM   2315  N NE1 . TRP A 1 291 ? 56.009  14.351  10.121  1.00 72.22  ? 291 TRP A NE1 1 
ATOM   2316  C CE2 . TRP A 1 291 ? 56.130  13.789  8.876   1.00 71.44  ? 291 TRP A CE2 1 
ATOM   2317  C CE3 . TRP A 1 291 ? 54.688  13.067  7.080   1.00 69.22  ? 291 TRP A CE3 1 
ATOM   2318  C CZ2 . TRP A 1 291 ? 57.262  13.427  8.160   1.00 71.80  ? 291 TRP A CZ2 1 
ATOM   2319  C CZ3 . TRP A 1 291 ? 55.820  12.719  6.373   1.00 70.20  ? 291 TRP A CZ3 1 
ATOM   2320  C CH2 . TRP A 1 291 ? 57.080  12.892  6.909   1.00 71.19  ? 291 TRP A CH2 1 
ATOM   2321  N N   . PHE A 1 292 ? 49.493  16.420  8.751   1.00 63.07  ? 292 PHE A N   1 
ATOM   2322  C CA  . PHE A 1 292 ? 48.051  16.341  8.594   1.00 61.69  ? 292 PHE A CA  1 
ATOM   2323  C C   . PHE A 1 292 ? 47.602  16.559  7.156   1.00 61.19  ? 292 PHE A C   1 
ATOM   2324  O O   . PHE A 1 292 ? 46.433  16.331  6.872   1.00 60.77  ? 292 PHE A O   1 
ATOM   2325  C CB  . PHE A 1 292 ? 47.300  17.311  9.499   1.00 61.37  ? 292 PHE A CB  1 
ATOM   2326  C CG  . PHE A 1 292 ? 46.992  16.695  10.854  1.00 61.65  ? 292 PHE A CG  1 
ATOM   2327  C CD1 . PHE A 1 292 ? 45.885  15.879  11.021  1.00 60.77  ? 292 PHE A CD1 1 
ATOM   2328  C CD2 . PHE A 1 292 ? 47.843  16.888  11.941  1.00 63.12  ? 292 PHE A CD2 1 
ATOM   2329  C CE1 . PHE A 1 292 ? 45.597  15.330  12.260  1.00 61.13  ? 292 PHE A CE1 1 
ATOM   2330  C CE2 . PHE A 1 292 ? 47.561  16.311  13.175  1.00 63.18  ? 292 PHE A CE2 1 
ATOM   2331  C CZ  . PHE A 1 292 ? 46.438  15.544  13.332  1.00 62.00  ? 292 PHE A CZ  1 
ATOM   2332  N N   . GLY A 1 293 ? 48.518  16.854  6.235   1.00 61.96  ? 293 GLY A N   1 
ATOM   2333  C CA  . GLY A 1 293 ? 48.135  17.270  4.896   1.00 62.51  ? 293 GLY A CA  1 
ATOM   2334  C C   . GLY A 1 293 ? 47.520  16.136  4.079   1.00 62.74  ? 293 GLY A C   1 
ATOM   2335  O O   . GLY A 1 293 ? 47.779  14.969  4.331   1.00 65.72  ? 293 GLY A O   1 
ATOM   2336  N N   . PHE A 1 294 ? 46.665  16.475  3.114   1.00 61.91  ? 294 PHE A N   1 
ATOM   2337  C CA  . PHE A 1 294 ? 46.315  15.544  2.050   1.00 60.93  ? 294 PHE A CA  1 
ATOM   2338  C C   . PHE A 1 294 ? 47.406  15.641  0.986   1.00 61.33  ? 294 PHE A C   1 
ATOM   2339  O O   . PHE A 1 294 ? 47.504  14.751  0.145   1.00 61.61  ? 294 PHE A O   1 
ATOM   2340  C CB  . PHE A 1 294 ? 44.931  15.782  1.412   1.00 60.18  ? 294 PHE A CB  1 
ATOM   2341  C CG  . PHE A 1 294 ? 43.715  15.713  2.320   1.00 59.00  ? 294 PHE A CG  1 
ATOM   2342  C CD1 . PHE A 1 294 ? 43.792  15.196  3.605   1.00 59.06  ? 294 PHE A CD1 1 
ATOM   2343  C CD2 . PHE A 1 294 ? 42.472  16.139  1.860   1.00 59.79  ? 294 PHE A CD2 1 
ATOM   2344  C CE1 . PHE A 1 294 ? 42.661  15.125  4.412   1.00 59.00  ? 294 PHE A CE1 1 
ATOM   2345  C CE2 . PHE A 1 294 ? 41.319  16.083  2.667   1.00 58.77  ? 294 PHE A CE2 1 
ATOM   2346  C CZ  . PHE A 1 294 ? 41.422  15.587  3.949   1.00 58.65  ? 294 PHE A CZ  1 
ATOM   2347  N N   . TRP A 1 295 ? 48.184  16.740  1.022   1.00 61.67  ? 295 TRP A N   1 
ATOM   2348  C CA  . TRP A 1 295 ? 49.392  16.893  0.228   1.00 63.03  ? 295 TRP A CA  1 
ATOM   2349  C C   . TRP A 1 295 ? 50.607  16.897  1.152   1.00 65.35  ? 295 TRP A C   1 
ATOM   2350  O O   . TRP A 1 295 ? 50.514  17.439  2.257   1.00 65.85  ? 295 TRP A O   1 
ATOM   2351  C CB  . TRP A 1 295 ? 49.367  18.191  -0.585  1.00 62.50  ? 295 TRP A CB  1 
ATOM   2352  C CG  . TRP A 1 295 ? 48.360  18.216  -1.699  1.00 61.38  ? 295 TRP A CG  1 
ATOM   2353  C CD1 . TRP A 1 295 ? 47.019  17.999  -1.592  1.00 60.10  ? 295 TRP A CD1 1 
ATOM   2354  C CD2 . TRP A 1 295 ? 48.627  18.409  -3.104  1.00 61.54  ? 295 TRP A CD2 1 
ATOM   2355  N NE1 . TRP A 1 295 ? 46.432  18.062  -2.830  1.00 60.17  ? 295 TRP A NE1 1 
ATOM   2356  C CE2 . TRP A 1 295 ? 47.398  18.316  -3.776  1.00 61.11  ? 295 TRP A CE2 1 
ATOM   2357  C CE3 . TRP A 1 295 ? 49.770  18.626  -3.866  1.00 62.82  ? 295 TRP A CE3 1 
ATOM   2358  C CZ2 . TRP A 1 295 ? 47.292  18.459  -5.161  1.00 61.63  ? 295 TRP A CZ2 1 
ATOM   2359  C CZ3 . TRP A 1 295 ? 49.658  18.766  -5.233  1.00 63.32  ? 295 TRP A CZ3 1 
ATOM   2360  C CH2 . TRP A 1 295 ? 48.438  18.694  -5.873  1.00 62.41  ? 295 TRP A CH2 1 
ATOM   2361  N N   . GLY A 1 296 ? 51.726  16.313  0.680   1.00 66.92  ? 296 GLY A N   1 
ATOM   2362  C CA  . GLY A 1 296 ? 52.972  16.263  1.434   1.00 68.53  ? 296 GLY A CA  1 
ATOM   2363  C C   . GLY A 1 296 ? 54.163  16.776  0.616   1.00 70.58  ? 296 GLY A C   1 
ATOM   2364  O O   . GLY A 1 296 ? 54.267  16.494  -0.578  1.00 71.53  ? 296 GLY A O   1 
ATOM   2365  N N   . TYR A 1 297 ? 55.084  17.505  1.263   1.00 70.99  ? 297 TYR A N   1 
ATOM   2366  C CA  . TYR A 1 297 ? 56.201  18.059  0.526   1.00 72.90  ? 297 TYR A CA  1 
ATOM   2367  C C   . TYR A 1 297 ? 57.327  17.024  0.523   1.00 74.10  ? 297 TYR A C   1 
ATOM   2368  O O   . TYR A 1 297 ? 57.454  16.197  1.424   1.00 73.45  ? 297 TYR A O   1 
ATOM   2369  C CB  . TYR A 1 297 ? 56.481  19.476  1.047   1.00 73.60  ? 297 TYR A CB  1 
ATOM   2370  C CG  . TYR A 1 297 ? 55.294  20.422  0.849   1.00 73.09  ? 297 TYR A CG  1 
ATOM   2371  C CD1 . TYR A 1 297 ? 54.941  20.889  -0.413  1.00 73.15  ? 297 TYR A CD1 1 
ATOM   2372  C CD2 . TYR A 1 297 ? 54.504  20.833  1.923   1.00 71.78  ? 297 TYR A CD2 1 
ATOM   2373  C CE1 . TYR A 1 297 ? 53.854  21.727  -0.588  1.00 72.44  ? 297 TYR A CE1 1 
ATOM   2374  C CE2 . TYR A 1 297 ? 53.412  21.662  1.758   1.00 70.84  ? 297 TYR A CE2 1 
ATOM   2375  C CZ  . TYR A 1 297 ? 53.077  22.106  0.495   1.00 71.65  ? 297 TYR A CZ  1 
ATOM   2376  O OH  . TYR A 1 297 ? 51.993  22.931  0.338   1.00 71.10  ? 297 TYR A OH  1 
ATOM   2377  N N   . SER A 1 298 ? 58.115  17.067  -0.547  1.00 75.84  ? 298 SER A N   1 
ATOM   2378  C CA  . SER A 1 298 ? 59.164  16.104  -0.809  1.00 78.04  ? 298 SER A CA  1 
ATOM   2379  C C   . SER A 1 298 ? 60.385  16.378  0.067   1.00 81.27  ? 298 SER A C   1 
ATOM   2380  O O   . SER A 1 298 ? 60.704  15.522  0.892   1.00 82.68  ? 298 SER A O   1 
ATOM   2381  C CB  . SER A 1 298 ? 59.483  16.126  -2.258  1.00 79.12  ? 298 SER A CB  1 
ATOM   2382  O OG  . SER A 1 298 ? 60.620  15.333  -2.494  1.00 83.42  ? 298 SER A OG  1 
ATOM   2383  N N   . ASP A 1 299 ? 61.046  17.546  -0.138  1.00 83.30  ? 299 ASP A N   1 
ATOM   2384  C CA  . ASP A 1 299 ? 62.124  18.093  0.691   1.00 83.83  ? 299 ASP A CA  1 
ATOM   2385  C C   . ASP A 1 299 ? 61.833  19.568  0.979   1.00 83.58  ? 299 ASP A C   1 
ATOM   2386  O O   . ASP A 1 299 ? 60.758  20.082  0.628   1.00 81.04  ? 299 ASP A O   1 
ATOM   2387  C CB  . ASP A 1 299 ? 63.466  18.044  -0.011  1.00 86.52  ? 299 ASP A CB  1 
ATOM   2388  C CG  . ASP A 1 299 ? 63.389  18.315  -1.502  1.00 88.64  ? 299 ASP A CG  1 
ATOM   2389  O OD1 . ASP A 1 299 ? 62.991  19.446  -1.881  1.00 87.43  ? 299 ASP A OD1 1 
ATOM   2390  O OD2 . ASP A 1 299 ? 63.623  17.340  -2.261  1.00 93.48  ? 299 ASP A OD2 1 
ATOM   2391  N N   . LEU A 1 300 ? 62.819  20.237  1.605   1.00 84.18  ? 300 LEU A N   1 
ATOM   2392  C CA  . LEU A 1 300 ? 62.753  21.658  1.911   1.00 83.65  ? 300 LEU A CA  1 
ATOM   2393  C C   . LEU A 1 300 ? 62.501  22.450  0.634   1.00 84.49  ? 300 LEU A C   1 
ATOM   2394  O O   . LEU A 1 300 ? 61.720  23.400  0.649   1.00 86.64  ? 300 LEU A O   1 
ATOM   2395  C CB  . LEU A 1 300 ? 64.004  22.186  2.624   1.00 84.59  ? 300 LEU A CB  1 
ATOM   2396  C CG  . LEU A 1 300 ? 63.822  23.432  3.500   1.00 83.95  ? 300 LEU A CG  1 
ATOM   2397  C CD1 . LEU A 1 300 ? 62.635  23.377  4.442   1.00 83.02  ? 300 LEU A CD1 1 
ATOM   2398  C CD2 . LEU A 1 300 ? 65.005  23.612  4.358   1.00 85.34  ? 300 LEU A CD2 1 
ATOM   2399  N N   . ASN A 1 301 ? 63.113  22.051  -0.479  1.00 84.30  ? 301 ASN A N   1 
ATOM   2400  C CA  . ASN A 1 301 ? 62.947  22.811  -1.703  1.00 84.70  ? 301 ASN A CA  1 
ATOM   2401  C C   . ASN A 1 301 ? 61.555  22.671  -2.345  1.00 82.87  ? 301 ASN A C   1 
ATOM   2402  O O   . ASN A 1 301 ? 61.234  23.487  -3.205  1.00 83.35  ? 301 ASN A O   1 
ATOM   2403  C CB  . ASN A 1 301 ? 64.074  22.510  -2.673  1.00 87.65  ? 301 ASN A CB  1 
ATOM   2404  C CG  . ASN A 1 301 ? 65.369  23.190  -2.276  1.00 91.02  ? 301 ASN A CG  1 
ATOM   2405  O OD1 . ASN A 1 301 ? 65.562  23.610  -1.128  1.00 92.71  ? 301 ASN A OD1 1 
ATOM   2406  N ND2 . ASN A 1 301 ? 66.272  23.349  -3.226  1.00 93.49  ? 301 ASN A ND2 1 
ATOM   2407  N N   . ASP A 1 302 ? 60.692  21.713  -1.945  1.00 79.55  ? 302 ASP A N   1 
ATOM   2408  C CA  . ASP A 1 302 ? 59.434  21.539  -2.654  1.00 77.09  ? 302 ASP A CA  1 
ATOM   2409  C C   . ASP A 1 302 ? 58.439  22.664  -2.321  1.00 76.53  ? 302 ASP A C   1 
ATOM   2410  O O   . ASP A 1 302 ? 58.021  22.813  -1.169  1.00 76.03  ? 302 ASP A O   1 
ATOM   2411  C CB  . ASP A 1 302 ? 58.795  20.196  -2.342  1.00 74.98  ? 302 ASP A CB  1 
ATOM   2412  C CG  . ASP A 1 302 ? 57.647  19.755  -3.250  1.00 72.84  ? 302 ASP A CG  1 
ATOM   2413  O OD1 . ASP A 1 302 ? 57.410  20.458  -4.253  1.00 72.33  ? 302 ASP A OD1 1 
ATOM   2414  O OD2 . ASP A 1 302 ? 57.039  18.667  -2.982  1.00 70.99  ? 302 ASP A OD2 1 
ATOM   2415  N N   . LYS A 1 303 ? 57.968  23.387  -3.354  1.00 76.23  ? 303 LYS A N   1 
ATOM   2416  C CA  . LYS A 1 303 ? 56.924  24.394  -3.194  1.00 74.85  ? 303 LYS A CA  1 
ATOM   2417  C C   . LYS A 1 303 ? 55.526  23.874  -3.579  1.00 72.27  ? 303 LYS A C   1 
ATOM   2418  O O   . LYS A 1 303 ? 54.550  24.616  -3.441  1.00 70.90  ? 303 LYS A O   1 
ATOM   2419  C CB  . LYS A 1 303 ? 57.310  25.654  -3.987  1.00 76.52  ? 303 LYS A CB  1 
ATOM   2420  C CG  . LYS A 1 303 ? 58.594  26.427  -3.566  1.00 78.42  ? 303 LYS A CG  1 
ATOM   2421  C CD  . LYS A 1 303 ? 58.528  27.148  -2.220  1.00 78.19  ? 303 LYS A CD  1 
ATOM   2422  C CE  . LYS A 1 303 ? 59.640  28.092  -1.894  1.00 79.98  ? 303 LYS A CE  1 
ATOM   2423  N NZ  . LYS A 1 303 ? 60.912  27.375  -1.718  1.00 81.35  ? 303 LYS A NZ  1 
ATOM   2424  N N   . TYR A 1 304 ? 55.399  22.612  -4.026  1.00 71.04  ? 304 TYR A N   1 
ATOM   2425  C CA  . TYR A 1 304 ? 54.167  22.163  -4.670  1.00 69.42  ? 304 TYR A CA  1 
ATOM   2426  C C   . TYR A 1 304 ? 53.510  21.004  -3.907  1.00 68.26  ? 304 TYR A C   1 
ATOM   2427  O O   . TYR A 1 304 ? 52.280  21.051  -3.591  1.00 67.07  ? 304 TYR A O   1 
ATOM   2428  C CB  . TYR A 1 304 ? 54.435  21.802  -6.141  1.00 69.93  ? 304 TYR A CB  1 
ATOM   2429  C CG  . TYR A 1 304 ? 54.851  23.028  -6.934  1.00 71.05  ? 304 TYR A CG  1 
ATOM   2430  C CD1 . TYR A 1 304 ? 53.911  23.991  -7.300  1.00 70.50  ? 304 TYR A CD1 1 
ATOM   2431  C CD2 . TYR A 1 304 ? 56.192  23.276  -7.223  1.00 72.55  ? 304 TYR A CD2 1 
ATOM   2432  C CE1 . TYR A 1 304 ? 54.294  25.157  -7.947  1.00 71.83  ? 304 TYR A CE1 1 
ATOM   2433  C CE2 . TYR A 1 304 ? 56.584  24.424  -7.892  1.00 73.80  ? 304 TYR A CE2 1 
ATOM   2434  C CZ  . TYR A 1 304 ? 55.637  25.375  -8.236  1.00 73.43  ? 304 TYR A CZ  1 
ATOM   2435  O OH  . TYR A 1 304 ? 56.004  26.497  -8.910  1.00 74.47  ? 304 TYR A OH  1 
ATOM   2436  N N   . GLY A 1 305 ? 54.335  19.961  -3.679  1.00 68.35  ? 305 GLY A N   1 
ATOM   2437  C CA  . GLY A 1 305 ? 53.910  18.694  -3.091  1.00 67.12  ? 305 GLY A CA  1 
ATOM   2438  C C   . GLY A 1 305 ? 53.238  17.771  -4.109  1.00 66.43  ? 305 GLY A C   1 
ATOM   2439  O O   . GLY A 1 305 ? 53.191  18.056  -5.303  1.00 67.13  ? 305 GLY A O   1 
ATOM   2440  N N   . THR A 1 306 ? 52.747  16.635  -3.614  1.00 65.43  ? 306 THR A N   1 
ATOM   2441  C CA  . THR A 1 306 ? 51.896  15.731  -4.384  1.00 64.59  ? 306 THR A CA  1 
ATOM   2442  C C   . THR A 1 306 ? 50.809  15.179  -3.465  1.00 62.92  ? 306 THR A C   1 
ATOM   2443  O O   . THR A 1 306 ? 50.951  15.067  -2.250  1.00 62.03  ? 306 THR A O   1 
ATOM   2444  C CB  . THR A 1 306 ? 52.709  14.594  -5.005  1.00 65.29  ? 306 THR A CB  1 
ATOM   2445  O OG1 . THR A 1 306 ? 53.391  13.988  -3.917  1.00 65.33  ? 306 THR A OG1 1 
ATOM   2446  C CG2 . THR A 1 306 ? 53.748  15.045  -6.011  1.00 66.73  ? 306 THR A CG2 1 
ATOM   2447  N N   . PRO A 1 307 ? 49.658  14.804  -4.023  1.00 62.87  ? 307 PRO A N   1 
ATOM   2448  C CA  . PRO A 1 307 ? 48.577  14.239  -3.204  1.00 62.29  ? 307 PRO A CA  1 
ATOM   2449  C C   . PRO A 1 307 ? 48.792  12.819  -2.646  1.00 62.69  ? 307 PRO A C   1 
ATOM   2450  O O   . PRO A 1 307 ? 49.237  11.896  -3.340  1.00 62.68  ? 307 PRO A O   1 
ATOM   2451  C CB  . PRO A 1 307 ? 47.394  14.318  -4.193  1.00 61.76  ? 307 PRO A CB  1 
ATOM   2452  C CG  . PRO A 1 307 ? 48.046  14.085  -5.551  1.00 62.83  ? 307 PRO A CG  1 
ATOM   2453  C CD  . PRO A 1 307 ? 49.342  14.904  -5.453  1.00 63.74  ? 307 PRO A CD  1 
ATOM   2454  N N   . ARG A 1 308 ? 48.491  12.670  -1.350  1.00 62.58  ? 308 ARG A N   1 
ATOM   2455  C CA  . ARG A 1 308 ? 48.467  11.379  -0.691  1.00 63.04  ? 308 ARG A CA  1 
ATOM   2456  C C   . ARG A 1 308 ? 47.187  10.635  -1.097  1.00 62.94  ? 308 ARG A C   1 
ATOM   2457  O O   . ARG A 1 308 ? 46.273  11.225  -1.687  1.00 63.98  ? 308 ARG A O   1 
ATOM   2458  C CB  . ARG A 1 308 ? 48.523  11.653  0.817   1.00 62.73  ? 308 ARG A CB  1 
ATOM   2459  C CG  . ARG A 1 308 ? 49.909  12.020  1.309   1.00 64.07  ? 308 ARG A CG  1 
ATOM   2460  C CD  . ARG A 1 308 ? 50.009  12.270  2.812   1.00 63.95  ? 308 ARG A CD  1 
ATOM   2461  N NE  . ARG A 1 308 ? 51.370  12.669  3.213   1.00 64.44  ? 308 ARG A NE  1 
ATOM   2462  C CZ  . ARG A 1 308 ? 51.643  13.647  4.071   1.00 64.72  ? 308 ARG A CZ  1 
ATOM   2463  N NH1 . ARG A 1 308 ? 50.667  14.256  4.743   1.00 63.74  ? 308 ARG A NH1 1 
ATOM   2464  N NH2 . ARG A 1 308 ? 52.900  14.014  4.268   1.00 65.75  ? 308 ARG A NH2 1 
ATOM   2465  N N   . PRO A 1 309 ? 47.050  9.338   -0.770  1.00 61.72  ? 309 PRO A N   1 
ATOM   2466  C CA  . PRO A 1 309 ? 45.854  8.583   -1.130  1.00 61.04  ? 309 PRO A CA  1 
ATOM   2467  C C   . PRO A 1 309 ? 44.529  9.212   -0.716  1.00 60.28  ? 309 PRO A C   1 
ATOM   2468  O O   . PRO A 1 309 ? 43.533  9.173   -1.455  1.00 59.71  ? 309 PRO A O   1 
ATOM   2469  C CB  . PRO A 1 309 ? 46.122  7.255   -0.425  1.00 61.42  ? 309 PRO A CB  1 
ATOM   2470  C CG  . PRO A 1 309 ? 47.630  7.113   -0.531  1.00 63.15  ? 309 PRO A CG  1 
ATOM   2471  C CD  . PRO A 1 309 ? 48.091  8.512   -0.158  1.00 62.99  ? 309 PRO A CD  1 
ATOM   2472  N N   . VAL A 1 310 ? 44.534  9.833   0.466   1.00 59.90  ? 310 VAL A N   1 
ATOM   2473  C CA  . VAL A 1 310 ? 43.297  10.363  1.021   1.00 57.85  ? 310 VAL A CA  1 
ATOM   2474  C C   . VAL A 1 310 ? 42.663  11.332  0.044   1.00 56.99  ? 310 VAL A C   1 
ATOM   2475  O O   . VAL A 1 310 ? 41.468  11.548  0.089   1.00 56.27  ? 310 VAL A O   1 
ATOM   2476  C CB  . VAL A 1 310 ? 43.497  11.065  2.370   1.00 57.58  ? 310 VAL A CB  1 
ATOM   2477  C CG1 . VAL A 1 310 ? 44.532  12.173  2.283   1.00 58.16  ? 310 VAL A CG1 1 
ATOM   2478  C CG2 . VAL A 1 310 ? 42.181  11.578  2.936   1.00 56.55  ? 310 VAL A CG2 1 
ATOM   2479  N N   . TRP A 1 311 ? 43.461  11.958  -0.801  1.00 57.36  ? 311 TRP A N   1 
ATOM   2480  C CA  . TRP A 1 311 ? 42.924  13.038  -1.606  1.00 57.41  ? 311 TRP A CA  1 
ATOM   2481  C C   . TRP A 1 311 ? 42.029  12.469  -2.689  1.00 57.77  ? 311 TRP A C   1 
ATOM   2482  O O   . TRP A 1 311 ? 40.937  12.956  -2.899  1.00 57.26  ? 311 TRP A O   1 
ATOM   2483  C CB  . TRP A 1 311 ? 44.088  13.842  -2.184  1.00 57.98  ? 311 TRP A CB  1 
ATOM   2484  C CG  . TRP A 1 311 ? 43.791  14.807  -3.286  1.00 57.50  ? 311 TRP A CG  1 
ATOM   2485  C CD1 . TRP A 1 311 ? 43.849  14.613  -4.635  1.00 57.87  ? 311 TRP A CD1 1 
ATOM   2486  C CD2 . TRP A 1 311 ? 43.558  16.201  -3.083  1.00 57.49  ? 311 TRP A CD2 1 
ATOM   2487  N NE1 . TRP A 1 311 ? 43.608  15.787  -5.294  1.00 58.31  ? 311 TRP A NE1 1 
ATOM   2488  C CE2 . TRP A 1 311 ? 43.438  16.784  -4.365  1.00 58.22  ? 311 TRP A CE2 1 
ATOM   2489  C CE3 . TRP A 1 311 ? 43.444  17.000  -1.944  1.00 57.15  ? 311 TRP A CE3 1 
ATOM   2490  C CZ2 . TRP A 1 311 ? 43.201  18.150  -4.530  1.00 58.72  ? 311 TRP A CZ2 1 
ATOM   2491  C CZ3 . TRP A 1 311 ? 43.246  18.356  -2.113  1.00 57.67  ? 311 TRP A CZ3 1 
ATOM   2492  C CH2 . TRP A 1 311 ? 43.127  18.924  -3.389  1.00 58.40  ? 311 TRP A CH2 1 
ATOM   2493  N N   . PHE A 1 312 ? 42.480  11.407  -3.343  1.00 59.36  ? 312 PHE A N   1 
ATOM   2494  C CA  . PHE A 1 312 ? 41.657  10.790  -4.373  1.00 60.45  ? 312 PHE A CA  1 
ATOM   2495  C C   . PHE A 1 312 ? 40.375  10.178  -3.776  1.00 59.89  ? 312 PHE A C   1 
ATOM   2496  O O   . PHE A 1 312 ? 39.293  10.253  -4.371  1.00 59.62  ? 312 PHE A O   1 
ATOM   2497  C CB  . PHE A 1 312 ? 42.614  9.850   -5.111  1.00 61.68  ? 312 PHE A CB  1 
ATOM   2498  C CG  . PHE A 1 312 ? 43.757  10.571  -5.815  1.00 62.81  ? 312 PHE A CG  1 
ATOM   2499  C CD1 . PHE A 1 312 ? 43.536  11.294  -6.981  1.00 63.78  ? 312 PHE A CD1 1 
ATOM   2500  C CD2 . PHE A 1 312 ? 45.051  10.510  -5.318  1.00 64.15  ? 312 PHE A CD2 1 
ATOM   2501  C CE1 . PHE A 1 312 ? 44.579  11.939  -7.637  1.00 65.31  ? 312 PHE A CE1 1 
ATOM   2502  C CE2 . PHE A 1 312 ? 46.111  11.131  -5.987  1.00 65.91  ? 312 PHE A CE2 1 
ATOM   2503  C CZ  . PHE A 1 312 ? 45.874  11.843  -7.150  1.00 66.43  ? 312 PHE A CZ  1 
ATOM   2504  N N   . ALA A 1 313 ? 40.486  9.572   -2.584  1.00 59.78  ? 313 ALA A N   1 
ATOM   2505  C CA  . ALA A 1 313 ? 39.340  8.984   -1.901  1.00 58.46  ? 313 ALA A CA  1 
ATOM   2506  C C   . ALA A 1 313 ? 38.305  10.063  -1.586  1.00 58.64  ? 313 ALA A C   1 
ATOM   2507  O O   . ALA A 1 313 ? 37.115  9.834   -1.801  1.00 58.84  ? 313 ALA A O   1 
ATOM   2508  C CB  . ALA A 1 313 ? 39.766  8.250   -0.645  1.00 57.49  ? 313 ALA A CB  1 
ATOM   2509  N N   . MET A 1 314 ? 38.753  11.201  -1.043  1.00 58.74  ? 314 MET A N   1 
ATOM   2510  C CA  . MET A 1 314 ? 37.835  12.264  -0.678  1.00 59.46  ? 314 MET A CA  1 
ATOM   2511  C C   . MET A 1 314 ? 37.175  12.812  -1.932  1.00 59.60  ? 314 MET A C   1 
ATOM   2512  O O   . MET A 1 314 ? 35.974  13.052  -1.926  1.00 59.99  ? 314 MET A O   1 
ATOM   2513  C CB  . MET A 1 314 ? 38.544  13.429  0.008   1.00 60.94  ? 314 MET A CB  1 
ATOM   2514  C CG  . MET A 1 314 ? 38.928  13.131  1.431   1.00 61.98  ? 314 MET A CG  1 
ATOM   2515  S SD  . MET A 1 314 ? 37.468  13.159  2.474   1.00 63.82  ? 314 MET A SD  1 
ATOM   2516  C CE  . MET A 1 314 ? 37.237  14.937  2.376   1.00 62.65  ? 314 MET A CE  1 
ATOM   2517  N N   . ARG A 1 315 ? 37.961  13.007  -2.993  1.00 60.05  ? 315 ARG A N   1 
ATOM   2518  C CA  . ARG A 1 315 ? 37.421  13.525  -4.234  1.00 60.68  ? 315 ARG A CA  1 
ATOM   2519  C C   . ARG A 1 315 ? 36.224  12.668  -4.624  1.00 61.26  ? 315 ARG A C   1 
ATOM   2520  O O   . ARG A 1 315 ? 35.093  13.147  -4.689  1.00 62.86  ? 315 ARG A O   1 
ATOM   2521  C CB  . ARG A 1 315 ? 38.409  13.515  -5.402  1.00 61.41  ? 315 ARG A CB  1 
ATOM   2522  C CG  . ARG A 1 315 ? 37.773  13.891  -6.733  1.00 62.43  ? 315 ARG A CG  1 
ATOM   2523  C CD  . ARG A 1 315 ? 38.731  13.899  -7.910  1.00 63.77  ? 315 ARG A CD  1 
ATOM   2524  N NE  . ARG A 1 315 ? 39.141  12.519  -8.182  1.00 65.06  ? 315 ARG A NE  1 
ATOM   2525  C CZ  . ARG A 1 315 ? 40.224  12.115  -8.840  1.00 66.59  ? 315 ARG A CZ  1 
ATOM   2526  N NH1 . ARG A 1 315 ? 41.021  12.965  -9.445  1.00 69.69  ? 315 ARG A NH1 1 
ATOM   2527  N NH2 . ARG A 1 315 ? 40.531  10.845  -8.887  1.00 66.89  ? 315 ARG A NH2 1 
ATOM   2528  N N   . ASP A 1 316 ? 36.483  11.383  -4.838  1.00 61.33  ? 316 ASP A N   1 
ATOM   2529  C CA  . ASP A 1 316 ? 35.481  10.455  -5.341  1.00 60.91  ? 316 ASP A CA  1 
ATOM   2530  C C   . ASP A 1 316 ? 34.241  10.375  -4.444  1.00 59.75  ? 316 ASP A C   1 
ATOM   2531  O O   . ASP A 1 316 ? 33.141  10.135  -4.932  1.00 59.37  ? 316 ASP A O   1 
ATOM   2532  C CB  . ASP A 1 316 ? 36.131  9.098   -5.539  1.00 60.91  ? 316 ASP A CB  1 
ATOM   2533  C CG  . ASP A 1 316 ? 37.157  9.057   -6.661  1.00 62.00  ? 316 ASP A CG  1 
ATOM   2534  O OD1 . ASP A 1 316 ? 37.337  10.101  -7.346  1.00 61.64  ? 316 ASP A OD1 1 
ATOM   2535  O OD2 . ASP A 1 316 ? 37.731  7.968   -6.862  1.00 62.98  ? 316 ASP A OD2 1 
ATOM   2536  N N   . TYR A 1 317 ? 34.432  10.512  -3.132  1.00 59.69  ? 317 TYR A N   1 
ATOM   2537  C CA  . TYR A 1 317 ? 33.393  10.214  -2.168  1.00 60.18  ? 317 TYR A CA  1 
ATOM   2538  C C   . TYR A 1 317 ? 32.458  11.393  -2.106  1.00 61.75  ? 317 TYR A C   1 
ATOM   2539  O O   . TYR A 1 317 ? 31.276  11.220  -1.826  1.00 63.84  ? 317 TYR A O   1 
ATOM   2540  C CB  . TYR A 1 317 ? 33.907  10.025  -0.741  1.00 60.66  ? 317 TYR A CB  1 
ATOM   2541  C CG  . TYR A 1 317 ? 32.853  9.872   0.345   1.00 60.58  ? 317 TYR A CG  1 
ATOM   2542  C CD1 . TYR A 1 317 ? 32.334  8.622   0.654   1.00 60.99  ? 317 TYR A CD1 1 
ATOM   2543  C CD2 . TYR A 1 317 ? 32.388  10.968  1.070   1.00 59.99  ? 317 TYR A CD2 1 
ATOM   2544  C CE1 . TYR A 1 317 ? 31.333  8.466   1.606   1.00 60.95  ? 317 TYR A CE1 1 
ATOM   2545  C CE2 . TYR A 1 317 ? 31.424  10.820  2.056   1.00 60.45  ? 317 TYR A CE2 1 
ATOM   2546  C CZ  . TYR A 1 317 ? 30.906  9.564   2.328   1.00 61.32  ? 317 TYR A CZ  1 
ATOM   2547  O OH  . TYR A 1 317 ? 30.000  9.367   3.313   1.00 63.37  ? 317 TYR A OH  1 
ATOM   2548  N N   . MET A 1 318 ? 33.021  12.579  -2.355  1.00 63.12  ? 318 MET A N   1 
ATOM   2549  C CA  . MET A 1 318 ? 32.261  13.818  -2.324  1.00 63.35  ? 318 MET A CA  1 
ATOM   2550  C C   . MET A 1 318 ? 31.280  13.924  -3.485  1.00 62.08  ? 318 MET A C   1 
ATOM   2551  O O   . MET A 1 318 ? 30.366  14.706  -3.382  1.00 61.91  ? 318 MET A O   1 
ATOM   2552  C CB  . MET A 1 318 ? 33.192  15.036  -2.340  1.00 65.10  ? 318 MET A CB  1 
ATOM   2553  C CG  . MET A 1 318 ? 33.558  15.522  -0.960  1.00 65.46  ? 318 MET A CG  1 
ATOM   2554  S SD  . MET A 1 318 ? 34.771  16.838  -1.103  1.00 69.75  ? 318 MET A SD  1 
ATOM   2555  C CE  . MET A 1 318 ? 34.421  17.529  0.526   1.00 68.05  ? 318 MET A CE  1 
ATOM   2556  N N   . LYS A 1 319 ? 31.465  13.170  -4.567  1.00 62.87  ? 319 LYS A N   1 
ATOM   2557  C CA  . LYS A 1 319 ? 30.687  13.361  -5.780  1.00 65.98  ? 319 LYS A CA  1 
ATOM   2558  C C   . LYS A 1 319 ? 29.186  13.134  -5.573  1.00 67.58  ? 319 LYS A C   1 
ATOM   2559  O O   . LYS A 1 319 ? 28.371  13.725  -6.288  1.00 72.16  ? 319 LYS A O   1 
ATOM   2560  C CB  . LYS A 1 319 ? 31.153  12.415  -6.887  1.00 67.86  ? 319 LYS A CB  1 
ATOM   2561  C CG  . LYS A 1 319 ? 32.506  12.791  -7.470  1.00 69.71  ? 319 LYS A CG  1 
ATOM   2562  C CD  . LYS A 1 319 ? 32.558  12.798  -8.995  1.00 71.85  ? 319 LYS A CD  1 
ATOM   2563  C CE  . LYS A 1 319 ? 33.260  14.034  -9.470  1.00 74.71  ? 319 LYS A CE  1 
ATOM   2564  N NZ  . LYS A 1 319 ? 32.696  14.430  -10.757 1.00 77.00  ? 319 LYS A NZ  1 
ATOM   2565  N N   . GLY A 1 320 ? 28.823  12.270  -4.620  1.00 65.51  ? 320 GLY A N   1 
ATOM   2566  C CA  . GLY A 1 320 ? 27.438  12.085  -4.227  1.00 64.37  ? 320 GLY A CA  1 
ATOM   2567  C C   . GLY A 1 320 ? 27.334  11.861  -2.720  1.00 63.13  ? 320 GLY A C   1 
ATOM   2568  O O   . GLY A 1 320 ? 27.740  10.815  -2.190  1.00 62.37  ? 320 GLY A O   1 
ATOM   2569  N N   . LEU A 1 321 ? 26.767  12.858  -2.037  1.00 61.12  ? 321 LEU A N   1 
ATOM   2570  C CA  . LEU A 1 321 ? 26.619  12.796  -0.593  1.00 59.93  ? 321 LEU A CA  1 
ATOM   2571  C C   . LEU A 1 321 ? 25.199  12.351  -0.234  1.00 59.54  ? 321 LEU A C   1 
ATOM   2572  O O   . LEU A 1 321 ? 24.237  12.826  -0.811  1.00 60.13  ? 321 LEU A O   1 
ATOM   2573  C CB  . LEU A 1 321 ? 26.980  14.157  0.004   1.00 59.39  ? 321 LEU A CB  1 
ATOM   2574  C CG  . LEU A 1 321 ? 28.428  14.636  -0.205  1.00 58.19  ? 321 LEU A CG  1 
ATOM   2575  C CD1 . LEU A 1 321 ? 28.508  16.092  0.151   1.00 57.74  ? 321 LEU A CD1 1 
ATOM   2576  C CD2 . LEU A 1 321 ? 29.474  13.895  0.582   1.00 57.00  ? 321 LEU A CD2 1 
ATOM   2577  N N   . ILE A 1 322 ? 25.099  11.378  0.676   1.00 58.76  ? 322 ILE A N   1 
ATOM   2578  C CA  . ILE A 1 322 ? 23.864  10.995  1.316   1.00 58.54  ? 322 ILE A CA  1 
ATOM   2579  C C   . ILE A 1 322 ? 23.782  11.741  2.645   1.00 57.29  ? 322 ILE A C   1 
ATOM   2580  O O   . ILE A 1 322 ? 24.558  11.459  3.537   1.00 55.09  ? 322 ILE A O   1 
ATOM   2581  C CB  . ILE A 1 322 ? 23.811  9.459   1.499   1.00 60.85  ? 322 ILE A CB  1 
ATOM   2582  C CG1 . ILE A 1 322 ? 23.726  8.708   0.157   1.00 62.03  ? 322 ILE A CG1 1 
ATOM   2583  C CG2 . ILE A 1 322 ? 22.643  9.013   2.403   1.00 62.41  ? 322 ILE A CG2 1 
ATOM   2584  C CD1 . ILE A 1 322 ? 25.008  8.069   -0.317  1.00 62.31  ? 322 ILE A CD1 1 
ATOM   2585  N N   . ILE A 1 323 ? 22.794  12.642  2.804   1.00 58.51  ? 323 ILE A N   1 
ATOM   2586  C CA  . ILE A 1 323 ? 22.508  13.266  4.097   1.00 59.31  ? 323 ILE A CA  1 
ATOM   2587  C C   . ILE A 1 323 ? 21.389  12.520  4.829   1.00 59.65  ? 323 ILE A C   1 
ATOM   2588  O O   . ILE A 1 323 ? 21.325  12.521  6.062   1.00 59.75  ? 323 ILE A O   1 
ATOM   2589  C CB  . ILE A 1 323 ? 22.169  14.764  3.960   1.00 61.11  ? 323 ILE A CB  1 
ATOM   2590  C CG1 . ILE A 1 323 ? 23.328  15.558  3.372   1.00 61.91  ? 323 ILE A CG1 1 
ATOM   2591  C CG2 . ILE A 1 323 ? 21.749  15.368  5.305   1.00 61.63  ? 323 ILE A CG2 1 
ATOM   2592  C CD1 . ILE A 1 323 ? 23.734  15.126  1.973   1.00 62.86  ? 323 ILE A CD1 1 
ATOM   2593  N N   . SER A 1 324 ? 20.502  11.869  4.084   1.00 59.55  ? 324 SER A N   1 
ATOM   2594  C CA  . SER A 1 324 ? 19.476  11.072  4.723   1.00 60.60  ? 324 SER A CA  1 
ATOM   2595  C C   . SER A 1 324 ? 19.072  9.971   3.750   1.00 60.79  ? 324 SER A C   1 
ATOM   2596  O O   . SER A 1 324 ? 19.054  10.227  2.548   1.00 62.31  ? 324 SER A O   1 
ATOM   2597  C CB  . SER A 1 324 ? 18.270  11.944  5.110   1.00 62.48  ? 324 SER A CB  1 
ATOM   2598  O OG  . SER A 1 324 ? 18.611  12.966  6.046   1.00 62.02  ? 324 SER A OG  1 
ATOM   2599  N N   . PRO A 1 325 ? 18.755  8.733   4.200   1.00 59.58  ? 325 PRO A N   1 
ATOM   2600  C CA  . PRO A 1 325 ? 18.896  8.333   5.600   1.00 59.45  ? 325 PRO A CA  1 
ATOM   2601  C C   . PRO A 1 325 ? 20.334  8.410   6.104   1.00 60.68  ? 325 PRO A C   1 
ATOM   2602  O O   . PRO A 1 325 ? 21.328  8.257   5.358   1.00 58.93  ? 325 PRO A O   1 
ATOM   2603  C CB  . PRO A 1 325 ? 18.449  6.908   5.584   1.00 59.27  ? 325 PRO A CB  1 
ATOM   2604  C CG  . PRO A 1 325 ? 18.793  6.467   4.186   1.00 58.98  ? 325 PRO A CG  1 
ATOM   2605  C CD  . PRO A 1 325 ? 18.316  7.629   3.341   1.00 59.15  ? 325 PRO A CD  1 
ATOM   2606  N N   . LYS A 1 326 ? 20.414  8.649   7.413   1.00 61.91  ? 326 LYS A N   1 
ATOM   2607  C CA  . LYS A 1 326 ? 21.691  8.637   8.086   1.00 61.18  ? 326 LYS A CA  1 
ATOM   2608  C C   . LYS A 1 326 ? 21.948  7.193   8.452   1.00 61.65  ? 326 LYS A C   1 
ATOM   2609  O O   . LYS A 1 326 ? 21.011  6.466   8.831   1.00 61.27  ? 326 LYS A O   1 
ATOM   2610  C CB  . LYS A 1 326 ? 21.673  9.551   9.308   1.00 61.64  ? 326 LYS A CB  1 
ATOM   2611  C CG  . LYS A 1 326 ? 21.407  10.999  8.919   1.00 62.02  ? 326 LYS A CG  1 
ATOM   2612  C CD  . LYS A 1 326 ? 21.230  11.914  10.121  1.00 62.40  ? 326 LYS A CD  1 
ATOM   2613  C CE  . LYS A 1 326 ? 21.373  13.316  9.749   1.00 62.74  ? 326 LYS A CE  1 
ATOM   2614  N NZ  . LYS A 1 326 ? 20.685  13.586  8.482   1.00 63.57  ? 326 LYS A NZ  1 
ATOM   2615  N N   . ASN A 1 327 ? 23.222  6.831   8.299   1.00 60.08  ? 327 ASN A N   1 
ATOM   2616  C CA  . ASN A 1 327 ? 23.714  5.539   8.713   1.00 60.64  ? 327 ASN A CA  1 
ATOM   2617  C C   . ASN A 1 327 ? 23.634  5.416   10.232  1.00 60.51  ? 327 ASN A C   1 
ATOM   2618  O O   . ASN A 1 327 ? 23.914  6.386   10.938  1.00 59.60  ? 327 ASN A O   1 
ATOM   2619  C CB  . ASN A 1 327 ? 25.136  5.341   8.203   1.00 61.03  ? 327 ASN A CB  1 
ATOM   2620  C CG  . ASN A 1 327 ? 25.590  3.921   8.404   1.00 61.03  ? 327 ASN A CG  1 
ATOM   2621  O OD1 . ASN A 1 327 ? 24.976  2.978   7.884   1.00 60.31  ? 327 ASN A OD1 1 
ATOM   2622  N ND2 . ASN A 1 327 ? 26.673  3.775   9.146   1.00 62.00  ? 327 ASN A ND2 1 
ATOM   2623  N N   . LYS A 1 328 ? 23.262  4.204   10.682  1.00 60.46  ? 328 LYS A N   1 
ATOM   2624  C CA  . LYS A 1 328 ? 22.971  3.860   12.071  1.00 61.00  ? 328 LYS A CA  1 
ATOM   2625  C C   . LYS A 1 328 ? 21.772  4.650   12.614  1.00 61.25  ? 328 LYS A C   1 
ATOM   2626  O O   . LYS A 1 328 ? 21.685  4.981   13.803  1.00 60.99  ? 328 LYS A O   1 
ATOM   2627  C CB  . LYS A 1 328 ? 24.259  3.923   12.900  1.00 60.72  ? 328 LYS A CB  1 
ATOM   2628  C CG  . LYS A 1 328 ? 25.398  3.079   12.368  1.00 60.91  ? 328 LYS A CG  1 
ATOM   2629  C CD  . LYS A 1 328 ? 25.079  1.620   12.060  1.00 61.87  ? 328 LYS A CD  1 
ATOM   2630  C CE  . LYS A 1 328 ? 26.207  0.658   12.271  1.00 63.36  ? 328 LYS A CE  1 
ATOM   2631  N NZ  . LYS A 1 328 ? 27.512  1.002   11.686  1.00 64.33  ? 328 LYS A NZ  1 
ATOM   2632  N N   . SER A 1 329 ? 20.824  4.934   11.723  1.00 61.53  ? 329 SER A N   1 
ATOM   2633  C CA  . SER A 1 329 ? 19.580  5.559   12.128  1.00 62.17  ? 329 SER A CA  1 
ATOM   2634  C C   . SER A 1 329 ? 18.562  4.445   12.321  1.00 63.04  ? 329 SER A C   1 
ATOM   2635  O O   . SER A 1 329 ? 18.683  3.396   11.696  1.00 62.90  ? 329 SER A O   1 
ATOM   2636  C CB  . SER A 1 329 ? 19.107  6.574   11.127  1.00 61.39  ? 329 SER A CB  1 
ATOM   2637  O OG  . SER A 1 329 ? 18.829  5.961   9.875   1.00 61.41  ? 329 SER A OG  1 
ATOM   2638  N N   . ILE A 1 330 ? 17.594  4.706   13.199  1.00 63.36  ? 330 ILE A N   1 
ATOM   2639  C CA  . ILE A 1 330 ? 16.499  3.817   13.494  1.00 64.25  ? 330 ILE A CA  1 
ATOM   2640  C C   . ILE A 1 330 ? 15.217  4.451   12.968  1.00 64.88  ? 330 ILE A C   1 
ATOM   2641  O O   . ILE A 1 330 ? 14.966  5.623   13.165  1.00 64.20  ? 330 ILE A O   1 
ATOM   2642  C CB  . ILE A 1 330 ? 16.413  3.591   15.006  1.00 66.04  ? 330 ILE A CB  1 
ATOM   2643  C CG1 . ILE A 1 330 ? 17.710  3.108   15.576  1.00 66.72  ? 330 ILE A CG1 1 
ATOM   2644  C CG2 . ILE A 1 330 ? 15.299  2.607   15.333  1.00 68.37  ? 330 ILE A CG2 1 
ATOM   2645  C CD1 . ILE A 1 330 ? 17.638  2.769   17.054  1.00 67.80  ? 330 ILE A CD1 1 
ATOM   2646  N N   . HIS A 1 331 ? 14.450  3.646   12.238  1.00 66.27  ? 331 HIS A N   1 
ATOM   2647  C CA  . HIS A 1 331 ? 13.224  4.154   11.583  1.00 66.32  ? 331 HIS A CA  1 
ATOM   2648  C C   . HIS A 1 331 ? 11.990  3.325   11.956  1.00 67.55  ? 331 HIS A C   1 
ATOM   2649  O O   . HIS A 1 331 ? 11.829  2.229   11.403  1.00 67.49  ? 331 HIS A O   1 
ATOM   2650  C CB  . HIS A 1 331 ? 13.448  4.101   10.075  1.00 65.64  ? 331 HIS A CB  1 
ATOM   2651  C CG  . HIS A 1 331 ? 14.478  5.051   9.581   1.00 64.70  ? 331 HIS A CG  1 
ATOM   2652  N ND1 . HIS A 1 331 ? 14.157  6.293   9.083   1.00 65.52  ? 331 HIS A ND1 1 
ATOM   2653  C CD2 . HIS A 1 331 ? 15.802  4.946   9.488   1.00 64.94  ? 331 HIS A CD2 1 
ATOM   2654  C CE1 . HIS A 1 331 ? 15.262  6.908   8.703   1.00 65.56  ? 331 HIS A CE1 1 
ATOM   2655  N NE2 . HIS A 1 331 ? 16.274  6.109   8.943   1.00 65.36  ? 331 HIS A NE2 1 
ATOM   2656  N N   . THR A 1 332 ? 11.118  3.853   12.820  1.00 68.74  ? 332 THR A N   1 
ATOM   2657  C CA  . THR A 1 332 ? 9.855   3.163   13.164  1.00 70.25  ? 332 THR A CA  1 
ATOM   2658  C C   . THR A 1 332 ? 8.792   3.565   12.173  1.00 71.67  ? 332 THR A C   1 
ATOM   2659  O O   . THR A 1 332 ? 7.704   3.935   12.616  1.00 74.79  ? 332 THR A O   1 
ATOM   2660  C CB  . THR A 1 332 ? 9.447   3.507   14.590  1.00 70.69  ? 332 THR A CB  1 
ATOM   2661  O OG1 . THR A 1 332 ? 9.253   4.916   14.580  1.00 71.59  ? 332 THR A OG1 1 
ATOM   2662  C CG2 . THR A 1 332 ? 10.507  3.130   15.607  1.00 70.28  ? 332 THR A CG2 1 
ATOM   2663  N N   . ASN A 1 333 ? 9.080   3.455   10.878  1.00 72.40  ? 333 ASN A N   1 
ATOM   2664  C CA  . ASN A 1 333 ? 8.121   3.857   9.823   1.00 75.05  ? 333 ASN A CA  1 
ATOM   2665  C C   . ASN A 1 333 ? 8.445   3.170   8.499   1.00 76.83  ? 333 ASN A C   1 
ATOM   2666  O O   . ASN A 1 333 ? 9.538   2.600   8.388   1.00 82.23  ? 333 ASN A O   1 
ATOM   2667  C CB  . ASN A 1 333 ? 8.123   5.365   9.621   1.00 75.49  ? 333 ASN A CB  1 
ATOM   2668  C CG  . ASN A 1 333 ? 6.888   5.866   8.915   1.00 78.76  ? 333 ASN A CG  1 
ATOM   2669  O OD1 . ASN A 1 333 ? 6.952   6.236   7.738   1.00 80.76  ? 333 ASN A OD1 1 
ATOM   2670  N ND2 . ASN A 1 333 ? 5.760   5.879   9.607   1.00 82.61  ? 333 ASN A ND2 1 
ATOM   2671  N N   . THR A 1 334 ? 7.533   3.234   7.535   1.00 76.47  ? 334 THR A N   1 
ATOM   2672  C CA  . THR A 1 334 ? 7.689   2.627   6.215   1.00 75.01  ? 334 THR A CA  1 
ATOM   2673  C C   . THR A 1 334 ? 8.117   3.666   5.168   1.00 74.20  ? 334 THR A C   1 
ATOM   2674  O O   . THR A 1 334 ? 8.323   3.336   4.003   1.00 72.30  ? 334 THR A O   1 
ATOM   2675  C CB  . THR A 1 334 ? 6.380   1.926   5.826   1.00 75.59  ? 334 THR A CB  1 
ATOM   2676  O OG1 . THR A 1 334 ? 6.071   2.218   4.466   1.00 74.67  ? 334 THR A OG1 1 
ATOM   2677  C CG2 . THR A 1 334 ? 5.154   2.419   6.576   1.00 77.12  ? 334 THR A CG2 1 
ATOM   2678  N N   . LYS A 1 335 ? 8.230   4.934   5.572   1.00 76.17  ? 335 LYS A N   1 
ATOM   2679  C CA  . LYS A 1 335 ? 8.651   6.000   4.675   1.00 78.68  ? 335 LYS A CA  1 
ATOM   2680  C C   . LYS A 1 335 ? 9.966   6.587   5.186   1.00 77.14  ? 335 LYS A C   1 
ATOM   2681  O O   . LYS A 1 335 ? 10.022  7.142   6.283   1.00 77.69  ? 335 LYS A O   1 
ATOM   2682  C CB  . LYS A 1 335 ? 7.685   7.188   4.577   1.00 83.53  ? 335 LYS A CB  1 
ATOM   2683  C CG  . LYS A 1 335 ? 6.253   6.944   4.101   1.00 89.06  ? 335 LYS A CG  1 
ATOM   2684  C CD  . LYS A 1 335 ? 6.109   6.729   2.600   1.00 93.20  ? 335 LYS A CD  1 
ATOM   2685  C CE  . LYS A 1 335 ? 6.218   5.281   2.244   1.00 97.46  ? 335 LYS A CE  1 
ATOM   2686  N NZ  . LYS A 1 335 ? 5.250   4.916   1.197   1.00 101.30 ? 335 LYS A NZ  1 
ATOM   2687  N N   . ILE A 1 336 ? 11.011  6.471   4.360   1.00 74.91  ? 336 ILE A N   1 
ATOM   2688  C CA  . ILE A 1 336 ? 12.350  6.877   4.730   1.00 73.33  ? 336 ILE A CA  1 
ATOM   2689  C C   . ILE A 1 336 ? 12.690  8.161   3.982   1.00 72.02  ? 336 ILE A C   1 
ATOM   2690  O O   . ILE A 1 336 ? 12.882  8.113   2.769   1.00 74.50  ? 336 ILE A O   1 
ATOM   2691  C CB  . ILE A 1 336 ? 13.331  5.750   4.362   1.00 74.15  ? 336 ILE A CB  1 
ATOM   2692  C CG1 . ILE A 1 336 ? 12.931  4.470   5.017   1.00 75.42  ? 336 ILE A CG1 1 
ATOM   2693  C CG2 . ILE A 1 336 ? 14.778  6.107   4.714   1.00 73.81  ? 336 ILE A CG2 1 
ATOM   2694  C CD1 . ILE A 1 336 ? 13.109  4.492   6.524   1.00 76.29  ? 336 ILE A CD1 1 
ATOM   2695  N N   . PRO A 1 337 ? 12.801  9.331   4.662   1.00 68.99  ? 337 PRO A N   1 
ATOM   2696  C CA  . PRO A 1 337 ? 13.299  10.552  4.029   1.00 66.62  ? 337 PRO A CA  1 
ATOM   2697  C C   . PRO A 1 337 ? 14.650  10.290  3.375   1.00 66.60  ? 337 PRO A C   1 
ATOM   2698  O O   . PRO A 1 337 ? 15.549  9.714   4.019   1.00 65.31  ? 337 PRO A O   1 
ATOM   2699  C CB  . PRO A 1 337 ? 13.433  11.575  5.154   1.00 66.12  ? 337 PRO A CB  1 
ATOM   2700  C CG  . PRO A 1 337 ? 12.686  11.001  6.329   1.00 66.95  ? 337 PRO A CG  1 
ATOM   2701  C CD  . PRO A 1 337 ? 12.470  9.524   6.081   1.00 68.38  ? 337 PRO A CD  1 
ATOM   2702  N N   . LEU A 1 338 ? 14.757  10.753  2.112   1.00 66.86  ? 338 LEU A N   1 
ATOM   2703  C CA  . LEU A 1 338 ? 15.974  10.692  1.310   1.00 66.33  ? 338 LEU A CA  1 
ATOM   2704  C C   . LEU A 1 338 ? 16.522  12.090  0.998   1.00 65.26  ? 338 LEU A C   1 
ATOM   2705  O O   . LEU A 1 338 ? 15.836  12.920  0.426   1.00 65.54  ? 338 LEU A O   1 
ATOM   2706  C CB  . LEU A 1 338 ? 15.597  9.954   0.024   1.00 67.03  ? 338 LEU A CB  1 
ATOM   2707  C CG  . LEU A 1 338 ? 16.721  9.756   -1.002  1.00 66.87  ? 338 LEU A CG  1 
ATOM   2708  C CD1 . LEU A 1 338 ? 17.825  8.879   -0.451  1.00 65.88  ? 338 LEU A CD1 1 
ATOM   2709  C CD2 . LEU A 1 338 ? 16.180  9.151   -2.299  1.00 67.47  ? 338 LEU A CD2 1 
ATOM   2710  N N   . GLU A 1 339 ? 17.800  12.332  1.259   1.00 63.90  ? 339 GLU A N   1 
ATOM   2711  C CA  . GLU A 1 339 ? 18.390  13.607  0.881   1.00 63.61  ? 339 GLU A CA  1 
ATOM   2712  C C   . GLU A 1 339 ? 19.792  13.411  0.305   1.00 61.92  ? 339 GLU A C   1 
ATOM   2713  O O   . GLU A 1 339 ? 20.674  12.894  0.991   1.00 60.59  ? 339 GLU A O   1 
ATOM   2714  C CB  . GLU A 1 339 ? 18.487  14.522  2.098   1.00 63.69  ? 339 GLU A CB  1 
ATOM   2715  C CG  . GLU A 1 339 ? 17.153  15.118  2.525   1.00 64.78  ? 339 GLU A CG  1 
ATOM   2716  C CD  . GLU A 1 339 ? 17.340  15.872  3.825   1.00 65.04  ? 339 GLU A CD  1 
ATOM   2717  O OE1 . GLU A 1 339 ? 17.508  15.140  4.811   1.00 64.84  ? 339 GLU A OE1 1 
ATOM   2718  O OE2 . GLU A 1 339 ? 17.401  17.123  3.865   1.00 65.20  ? 339 GLU A OE2 1 
ATOM   2719  N N   . LEU A 1 340 ? 19.990  13.882  -0.934  1.00 61.73  ? 340 LEU A N   1 
ATOM   2720  C CA  . LEU A 1 340 ? 21.302  13.875  -1.567  1.00 62.03  ? 340 LEU A CA  1 
ATOM   2721  C C   . LEU A 1 340 ? 21.793  15.293  -1.944  1.00 62.63  ? 340 LEU A C   1 
ATOM   2722  O O   . LEU A 1 340 ? 21.018  16.189  -2.242  1.00 62.76  ? 340 LEU A O   1 
ATOM   2723  C CB  . LEU A 1 340 ? 21.219  12.990  -2.809  1.00 62.28  ? 340 LEU A CB  1 
ATOM   2724  C CG  . LEU A 1 340 ? 20.680  11.571  -2.632  1.00 62.74  ? 340 LEU A CG  1 
ATOM   2725  C CD1 . LEU A 1 340 ? 20.711  10.892  -3.981  1.00 63.38  ? 340 LEU A CD1 1 
ATOM   2726  C CD2 . LEU A 1 340 ? 21.485  10.773  -1.630  1.00 61.97  ? 340 LEU A CD2 1 
ATOM   2727  N N   . TYR A 1 341 ? 23.119  15.469  -1.975  1.00 62.28  ? 341 TYR A N   1 
ATOM   2728  C CA  . TYR A 1 341 ? 23.788  16.571  -2.641  1.00 62.66  ? 341 TYR A CA  1 
ATOM   2729  C C   . TYR A 1 341 ? 24.724  15.994  -3.698  1.00 63.33  ? 341 TYR A C   1 
ATOM   2730  O O   . TYR A 1 341 ? 25.624  15.238  -3.346  1.00 63.94  ? 341 TYR A O   1 
ATOM   2731  C CB  . TYR A 1 341 ? 24.634  17.358  -1.634  1.00 62.10  ? 341 TYR A CB  1 
ATOM   2732  C CG  . TYR A 1 341 ? 24.871  18.803  -2.037  1.00 61.36  ? 341 TYR A CG  1 
ATOM   2733  C CD1 . TYR A 1 341 ? 23.861  19.748  -1.893  1.00 62.45  ? 341 TYR A CD1 1 
ATOM   2734  C CD2 . TYR A 1 341 ? 26.036  19.194  -2.653  1.00 59.83  ? 341 TYR A CD2 1 
ATOM   2735  C CE1 . TYR A 1 341 ? 24.044  21.058  -2.288  1.00 62.35  ? 341 TYR A CE1 1 
ATOM   2736  C CE2 . TYR A 1 341 ? 26.222  20.491  -3.076  1.00 61.41  ? 341 TYR A CE2 1 
ATOM   2737  C CZ  . TYR A 1 341 ? 25.231  21.437  -2.879  1.00 62.68  ? 341 TYR A CZ  1 
ATOM   2738  O OH  . TYR A 1 341 ? 25.402  22.759  -3.233  1.00 65.23  ? 341 TYR A OH  1 
ATOM   2739  N N   . ASN A 1 342 ? 24.531  16.363  -4.971  1.00 64.53  ? 342 ASN A N   1 
ATOM   2740  C CA  . ASN A 1 342 ? 25.210  15.694  -6.071  1.00 66.24  ? 342 ASN A CA  1 
ATOM   2741  C C   . ASN A 1 342 ? 25.977  16.670  -6.945  1.00 67.43  ? 342 ASN A C   1 
ATOM   2742  O O   . ASN A 1 342 ? 25.397  17.648  -7.415  1.00 66.98  ? 342 ASN A O   1 
ATOM   2743  C CB  . ASN A 1 342 ? 24.246  15.031  -7.037  1.00 67.54  ? 342 ASN A CB  1 
ATOM   2744  C CG  . ASN A 1 342 ? 23.455  13.984  -6.320  1.00 68.48  ? 342 ASN A CG  1 
ATOM   2745  O OD1 . ASN A 1 342 ? 23.973  13.379  -5.380  1.00 71.47  ? 342 ASN A OD1 1 
ATOM   2746  N ND2 . ASN A 1 342 ? 22.235  13.744  -6.758  1.00 70.06  ? 342 ASN A ND2 1 
ATOM   2747  N N   . ASP A 1 343 ? 27.244  16.332  -7.244  1.00 66.82  ? 343 ASP A N   1 
ATOM   2748  C CA  . ASP A 1 343 ? 28.002  17.139  -8.183  1.00 67.67  ? 343 ASP A CA  1 
ATOM   2749  C C   . ASP A 1 343 ? 27.452  16.874  -9.586  1.00 67.31  ? 343 ASP A C   1 
ATOM   2750  O O   . ASP A 1 343 ? 26.675  15.943  -9.788  1.00 68.86  ? 343 ASP A O   1 
ATOM   2751  C CB  . ASP A 1 343 ? 29.498  16.990  -7.940  1.00 68.90  ? 343 ASP A CB  1 
ATOM   2752  C CG  . ASP A 1 343 ? 30.274  16.144  -8.934  1.00 69.76  ? 343 ASP A CG  1 
ATOM   2753  O OD1 . ASP A 1 343 ? 29.747  15.064  -9.311  1.00 68.44  ? 343 ASP A OD1 1 
ATOM   2754  O OD2 . ASP A 1 343 ? 31.393  16.597  -9.313  1.00 70.10  ? 343 ASP A OD2 1 
ATOM   2755  N N   . LYS A 1 344 ? 27.880  17.687  -10.552 1.00 66.34  ? 344 LYS A N   1 
ATOM   2756  C CA  . LYS A 1 344 ? 27.250  17.773  -11.860 1.00 66.95  ? 344 LYS A CA  1 
ATOM   2757  C C   . LYS A 1 344 ? 27.451  16.523  -12.708 1.00 66.66  ? 344 LYS A C   1 
ATOM   2758  O O   . LYS A 1 344 ? 27.095  16.516  -13.883 1.00 67.23  ? 344 LYS A O   1 
ATOM   2759  C CB  . LYS A 1 344 ? 27.878  18.933  -12.637 1.00 69.00  ? 344 LYS A CB  1 
ATOM   2760  C CG  . LYS A 1 344 ? 29.388  18.835  -12.774 1.00 69.79  ? 344 LYS A CG  1 
ATOM   2761  C CD  . LYS A 1 344 ? 30.042  19.847  -13.699 1.00 72.47  ? 344 LYS A CD  1 
ATOM   2762  C CE  . LYS A 1 344 ? 31.515  19.937  -13.448 1.00 74.65  ? 344 LYS A CE  1 
ATOM   2763  N NZ  . LYS A 1 344 ? 32.170  18.615  -13.376 1.00 76.29  ? 344 LYS A NZ  1 
ATOM   2764  N N   . ASP A 1 345 ? 28.065  15.481  -12.132 1.00 65.98  ? 345 ASP A N   1 
ATOM   2765  C CA  . ASP A 1 345 ? 28.472  14.318  -12.903 1.00 65.45  ? 345 ASP A CA  1 
ATOM   2766  C C   . ASP A 1 345 ? 27.528  13.146  -12.661 1.00 64.68  ? 345 ASP A C   1 
ATOM   2767  O O   . ASP A 1 345 ? 27.540  12.222  -13.477 1.00 64.70  ? 345 ASP A O   1 
ATOM   2768  C CB  . ASP A 1 345 ? 29.922  13.958  -12.645 1.00 65.12  ? 345 ASP A CB  1 
ATOM   2769  C CG  . ASP A 1 345 ? 30.945  14.869  -13.310 1.00 65.77  ? 345 ASP A CG  1 
ATOM   2770  O OD1 . ASP A 1 345 ? 30.593  15.990  -13.707 1.00 66.04  ? 345 ASP A OD1 1 
ATOM   2771  O OD2 . ASP A 1 345 ? 32.082  14.426  -13.481 1.00 65.87  ? 345 ASP A OD2 1 
ATOM   2772  N N   . VAL A 1 346 ? 26.727  13.248  -11.575 1.00 63.05  ? 346 VAL A N   1 
ATOM   2773  C CA  . VAL A 1 346 ? 25.759  12.257  -11.123 1.00 61.82  ? 346 VAL A CA  1 
ATOM   2774  C C   . VAL A 1 346 ? 24.481  12.420  -11.917 1.00 62.83  ? 346 VAL A C   1 
ATOM   2775  O O   . VAL A 1 346 ? 23.655  13.236  -11.573 1.00 62.58  ? 346 VAL A O   1 
ATOM   2776  C CB  . VAL A 1 346 ? 25.434  12.422  -9.625  1.00 60.48  ? 346 VAL A CB  1 
ATOM   2777  C CG1 . VAL A 1 346 ? 24.347  11.481  -9.150  1.00 60.19  ? 346 VAL A CG1 1 
ATOM   2778  C CG2 . VAL A 1 346 ? 26.663  12.233  -8.748  1.00 59.80  ? 346 VAL A CG2 1 
ATOM   2779  N N   . LYS A 1 347 ? 24.306  11.595  -12.934 1.00 65.21  ? 347 LYS A N   1 
ATOM   2780  C CA  . LYS A 1 347 ? 23.116  11.628  -13.762 1.00 67.65  ? 347 LYS A CA  1 
ATOM   2781  C C   . LYS A 1 347 ? 22.061  10.636  -13.274 1.00 68.47  ? 347 LYS A C   1 
ATOM   2782  O O   . LYS A 1 347 ? 20.877  10.869  -13.549 1.00 69.80  ? 347 LYS A O   1 
ATOM   2783  C CB  . LYS A 1 347 ? 23.522  11.387  -15.218 1.00 69.38  ? 347 LYS A CB  1 
ATOM   2784  C CG  . LYS A 1 347 ? 24.529  12.416  -15.731 1.00 69.93  ? 347 LYS A CG  1 
ATOM   2785  C CD  . LYS A 1 347 ? 24.009  13.836  -15.663 1.00 70.98  ? 347 LYS A CD  1 
ATOM   2786  C CE  . LYS A 1 347 ? 25.007  14.831  -16.122 1.00 72.54  ? 347 LYS A CE  1 
ATOM   2787  N NZ  . LYS A 1 347 ? 24.302  16.117  -16.189 1.00 74.69  ? 347 LYS A NZ  1 
ATOM   2788  N N   . LYS A 1 348 ? 22.453  9.582   -12.531 1.00 67.86  ? 348 LYS A N   1 
ATOM   2789  C CA  . LYS A 1 348 ? 21.450  8.685   -11.970 1.00 68.80  ? 348 LYS A CA  1 
ATOM   2790  C C   . LYS A 1 348 ? 21.808  8.217   -10.561 1.00 67.28  ? 348 LYS A C   1 
ATOM   2791  O O   . LYS A 1 348 ? 22.966  8.059   -10.237 1.00 66.30  ? 348 LYS A O   1 
ATOM   2792  C CB  . LYS A 1 348 ? 21.257  7.505   -12.919 1.00 70.23  ? 348 LYS A CB  1 
ATOM   2793  C CG  . LYS A 1 348 ? 20.137  6.603   -12.491 1.00 71.81  ? 348 LYS A CG  1 
ATOM   2794  C CD  . LYS A 1 348 ? 19.727  5.648   -13.600 1.00 75.11  ? 348 LYS A CD  1 
ATOM   2795  C CE  . LYS A 1 348 ? 20.876  4.760   -14.006 1.00 76.67  ? 348 LYS A CE  1 
ATOM   2796  N NZ  . LYS A 1 348 ? 20.396  3.713   -14.921 1.00 79.30  ? 348 LYS A NZ  1 
ATOM   2797  N N   . VAL A 1 349 ? 20.794  7.982   -9.725  1.00 66.84  ? 349 VAL A N   1 
ATOM   2798  C CA  . VAL A 1 349 ? 21.005  7.406   -8.410  1.00 66.23  ? 349 VAL A CA  1 
ATOM   2799  C C   . VAL A 1 349 ? 20.008  6.274   -8.239  1.00 69.29  ? 349 VAL A C   1 
ATOM   2800  O O   . VAL A 1 349 ? 18.808  6.506   -8.407  1.00 72.98  ? 349 VAL A O   1 
ATOM   2801  C CB  . VAL A 1 349 ? 20.804  8.397   -7.262  1.00 64.69  ? 349 VAL A CB  1 
ATOM   2802  C CG1 . VAL A 1 349 ? 20.991  7.742   -5.905  1.00 63.14  ? 349 VAL A CG1 1 
ATOM   2803  C CG2 . VAL A 1 349 ? 21.723  9.589   -7.419  1.00 65.39  ? 349 VAL A CG2 1 
ATOM   2804  N N   . VAL A 1 350 ? 20.507  5.079   -7.865  1.00 68.90  ? 350 VAL A N   1 
ATOM   2805  C CA  . VAL A 1 350 ? 19.647  3.954   -7.546  1.00 68.59  ? 350 VAL A CA  1 
ATOM   2806  C C   . VAL A 1 350 ? 19.925  3.519   -6.114  1.00 67.02  ? 350 VAL A C   1 
ATOM   2807  O O   . VAL A 1 350 ? 21.031  3.734   -5.639  1.00 66.10  ? 350 VAL A O   1 
ATOM   2808  C CB  . VAL A 1 350 ? 19.909  2.826   -8.554  1.00 69.39  ? 350 VAL A CB  1 
ATOM   2809  C CG1 . VAL A 1 350 ? 19.288  1.512   -8.108  1.00 69.43  ? 350 VAL A CG1 1 
ATOM   2810  C CG2 . VAL A 1 350 ? 19.409  3.208   -9.942  1.00 70.68  ? 350 VAL A CG2 1 
ATOM   2811  N N   . VAL A 1 351 ? 18.914  2.934   -5.451  1.00 66.56  ? 351 VAL A N   1 
ATOM   2812  C CA  . VAL A 1 351 ? 19.095  2.278   -4.162  1.00 65.50  ? 351 VAL A CA  1 
ATOM   2813  C C   . VAL A 1 351 ? 18.624  0.827   -4.269  1.00 66.10  ? 351 VAL A C   1 
ATOM   2814  O O   . VAL A 1 351 ? 17.510  0.546   -4.737  1.00 67.15  ? 351 VAL A O   1 
ATOM   2815  C CB  . VAL A 1 351 ? 18.369  2.957   -2.986  1.00 65.61  ? 351 VAL A CB  1 
ATOM   2816  C CG1 . VAL A 1 351 ? 18.612  2.213   -1.676  1.00 65.14  ? 351 VAL A CG1 1 
ATOM   2817  C CG2 . VAL A 1 351 ? 18.748  4.421   -2.838  1.00 65.63  ? 351 VAL A CG2 1 
ATOM   2818  N N   . LYS A 1 352 ? 19.469  -0.089  -3.765  1.00 65.27  ? 352 LYS A N   1 
ATOM   2819  C CA  . LYS A 1 352 ? 19.158  -1.513  -3.766  1.00 64.93  ? 352 LYS A CA  1 
ATOM   2820  C C   . LYS A 1 352 ? 19.064  -2.019  -2.325  1.00 62.79  ? 352 LYS A C   1 
ATOM   2821  O O   . LYS A 1 352 ? 19.741  -1.496  -1.424  1.00 62.98  ? 352 LYS A O   1 
ATOM   2822  C CB  . LYS A 1 352 ? 20.180  -2.309  -4.598  1.00 65.43  ? 352 LYS A CB  1 
ATOM   2823  C CG  . LYS A 1 352 ? 19.918  -2.356  -6.107  1.00 66.51  ? 352 LYS A CG  1 
ATOM   2824  C CD  . LYS A 1 352 ? 21.039  -2.909  -6.979  1.00 67.06  ? 352 LYS A CD  1 
ATOM   2825  C CE  . LYS A 1 352 ? 20.962  -2.362  -8.373  1.00 68.17  ? 352 LYS A CE  1 
ATOM   2826  N NZ  . LYS A 1 352 ? 22.253  -2.400  -9.068  1.00 68.02  ? 352 LYS A NZ  1 
ATOM   2827  N N   . PHE A 1 353 ? 18.218  -3.039  -2.151  1.00 61.00  ? 353 PHE A N   1 
ATOM   2828  C CA  . PHE A 1 353 ? 18.203  -3.870  -0.965  1.00 60.03  ? 353 PHE A CA  1 
ATOM   2829  C C   . PHE A 1 353 ? 17.971  -5.324  -1.356  1.00 60.87  ? 353 PHE A C   1 
ATOM   2830  O O   . PHE A 1 353 ? 16.974  -5.594  -2.028  1.00 61.80  ? 353 PHE A O   1 
ATOM   2831  C CB  . PHE A 1 353 ? 17.064  -3.536  -0.024  1.00 59.81  ? 353 PHE A CB  1 
ATOM   2832  C CG  . PHE A 1 353 ? 16.994  -4.425  1.193   1.00 59.28  ? 353 PHE A CG  1 
ATOM   2833  C CD1 . PHE A 1 353 ? 17.954  -4.327  2.181   1.00 58.54  ? 353 PHE A CD1 1 
ATOM   2834  C CD2 . PHE A 1 353 ? 15.912  -5.241  1.404   1.00 60.01  ? 353 PHE A CD2 1 
ATOM   2835  C CE1 . PHE A 1 353 ? 17.881  -5.104  3.322   1.00 58.85  ? 353 PHE A CE1 1 
ATOM   2836  C CE2 . PHE A 1 353 ? 15.826  -5.991  2.563   1.00 60.58  ? 353 PHE A CE2 1 
ATOM   2837  C CZ  . PHE A 1 353 ? 16.823  -5.938  3.511   1.00 59.84  ? 353 PHE A CZ  1 
ATOM   2838  N N   . ARG A 1 354 ? 18.883  -6.201  -0.879  1.00 60.29  ? 354 ARG A N   1 
ATOM   2839  C CA  . ARG A 1 354 ? 19.069  -7.587  -1.275  1.00 60.80  ? 354 ARG A CA  1 
ATOM   2840  C C   . ARG A 1 354 ? 19.034  -7.701  -2.794  1.00 61.35  ? 354 ARG A C   1 
ATOM   2841  O O   . ARG A 1 354 ? 18.279  -8.485  -3.345  1.00 62.90  ? 354 ARG A O   1 
ATOM   2842  C CB  . ARG A 1 354 ? 18.085  -8.505  -0.536  1.00 61.75  ? 354 ARG A CB  1 
ATOM   2843  C CG  . ARG A 1 354 ? 18.406  -8.587  0.951   1.00 61.60  ? 354 ARG A CG  1 
ATOM   2844  C CD  . ARG A 1 354 ? 17.318  -9.287  1.718   1.00 62.77  ? 354 ARG A CD  1 
ATOM   2845  N NE  . ARG A 1 354 ? 17.435  -9.065  3.161   1.00 62.89  ? 354 ARG A NE  1 
ATOM   2846  C CZ  . ARG A 1 354 ? 16.464  -9.398  4.004   1.00 64.09  ? 354 ARG A CZ  1 
ATOM   2847  N NH1 . ARG A 1 354 ? 15.331  -9.911  3.562   1.00 64.97  ? 354 ARG A NH1 1 
ATOM   2848  N NH2 . ARG A 1 354 ? 16.630  -9.223  5.299   1.00 64.75  ? 354 ARG A NH2 1 
ATOM   2849  N N   . ASP A 1 355 ? 19.821  -6.872  -3.459  1.00 60.96  ? 355 ASP A N   1 
ATOM   2850  C CA  . ASP A 1 355 ? 20.061  -6.942  -4.890  1.00 61.74  ? 355 ASP A CA  1 
ATOM   2851  C C   . ASP A 1 355 ? 18.854  -6.632  -5.752  1.00 63.71  ? 355 ASP A C   1 
ATOM   2852  O O   . ASP A 1 355 ? 19.005  -6.850  -6.954  1.00 64.11  ? 355 ASP A O   1 
ATOM   2853  C CB  . ASP A 1 355 ? 20.693  -8.254  -5.266  1.00 62.07  ? 355 ASP A CB  1 
ATOM   2854  C CG  . ASP A 1 355 ? 21.860  -8.480  -4.336  1.00 61.83  ? 355 ASP A CG  1 
ATOM   2855  O OD1 . ASP A 1 355 ? 22.913  -7.849  -4.582  1.00 61.77  ? 355 ASP A OD1 1 
ATOM   2856  O OD2 . ASP A 1 355 ? 21.627  -9.087  -3.279  1.00 61.87  ? 355 ASP A OD2 1 
ATOM   2857  N N   . LYS A 1 356 ? 17.761  -6.087  -5.149  1.00 65.25  ? 356 LYS A N   1 
ATOM   2858  C CA  . LYS A 1 356 ? 16.557  -5.634  -5.835  1.00 67.08  ? 356 LYS A CA  1 
ATOM   2859  C C   . LYS A 1 356 ? 16.426  -4.121  -5.724  1.00 65.45  ? 356 LYS A C   1 
ATOM   2860  O O   . LYS A 1 356 ? 16.683  -3.555  -4.667  1.00 64.24  ? 356 LYS A O   1 
ATOM   2861  C CB  . LYS A 1 356 ? 15.299  -6.188  -5.163  1.00 71.41  ? 356 LYS A CB  1 
ATOM   2862  C CG  . LYS A 1 356 ? 14.030  -6.095  -6.022  1.00 76.29  ? 356 LYS A CG  1 
ATOM   2863  C CD  . LYS A 1 356 ? 12.814  -6.891  -5.563  1.00 79.66  ? 356 LYS A CD  1 
ATOM   2864  C CE  . LYS A 1 356 ? 12.436  -6.518  -4.160  1.00 82.85  ? 356 LYS A CE  1 
ATOM   2865  N NZ  . LYS A 1 356 ? 11.312  -7.352  -3.700  1.00 86.53  ? 356 LYS A NZ  1 
ATOM   2866  N N   . VAL A 1 357 ? 15.993  -3.477  -6.811  1.00 65.44  ? 357 VAL A N   1 
ATOM   2867  C CA  . VAL A 1 357 ? 15.824  -2.026  -6.850  1.00 65.04  ? 357 VAL A CA  1 
ATOM   2868  C C   . VAL A 1 357 ? 14.558  -1.602  -6.087  1.00 66.27  ? 357 VAL A C   1 
ATOM   2869  O O   . VAL A 1 357 ? 13.464  -2.136  -6.302  1.00 66.03  ? 357 VAL A O   1 
ATOM   2870  C CB  . VAL A 1 357 ? 15.735  -1.523  -8.302  1.00 65.12  ? 357 VAL A CB  1 
ATOM   2871  C CG1 . VAL A 1 357 ? 15.352  -0.058  -8.369  1.00 65.50  ? 357 VAL A CG1 1 
ATOM   2872  C CG2 . VAL A 1 357 ? 17.022  -1.738  -9.061  1.00 64.60  ? 357 VAL A CG2 1 
ATOM   2873  N N   . ILE A 1 358 ? 14.723  -0.585  -5.225  1.00 66.57  ? 358 ILE A N   1 
ATOM   2874  C CA  . ILE A 1 358 ? 13.623  0.002   -4.477  1.00 66.89  ? 358 ILE A CA  1 
ATOM   2875  C C   . ILE A 1 358 ? 13.497  1.494   -4.798  1.00 67.80  ? 358 ILE A C   1 
ATOM   2876  O O   . ILE A 1 358 ? 12.443  2.062   -4.539  1.00 69.93  ? 358 ILE A O   1 
ATOM   2877  C CB  . ILE A 1 358 ? 13.802  -0.251  -2.970  1.00 65.69  ? 358 ILE A CB  1 
ATOM   2878  C CG1 . ILE A 1 358 ? 14.935  0.576   -2.399  1.00 65.17  ? 358 ILE A CG1 1 
ATOM   2879  C CG2 . ILE A 1 358 ? 13.995  -1.740  -2.689  1.00 65.07  ? 358 ILE A CG2 1 
ATOM   2880  C CD1 . ILE A 1 358 ? 15.139  0.372   -0.911  1.00 65.50  ? 358 ILE A CD1 1 
ATOM   2881  N N   . TYR A 1 359 ? 14.550  2.135   -5.336  1.00 67.34  ? 359 TYR A N   1 
ATOM   2882  C CA  . TYR A 1 359 ? 14.459  3.519   -5.783  1.00 67.54  ? 359 TYR A CA  1 
ATOM   2883  C C   . TYR A 1 359 ? 15.357  3.750   -6.994  1.00 67.43  ? 359 TYR A C   1 
ATOM   2884  O O   . TYR A 1 359 ? 16.492  3.276   -7.031  1.00 67.65  ? 359 TYR A O   1 
ATOM   2885  C CB  . TYR A 1 359 ? 14.873  4.472   -4.660  1.00 67.62  ? 359 TYR A CB  1 
ATOM   2886  C CG  . TYR A 1 359 ? 14.777  5.965   -4.973  1.00 68.30  ? 359 TYR A CG  1 
ATOM   2887  C CD1 . TYR A 1 359 ? 15.843  6.665   -5.522  1.00 69.15  ? 359 TYR A CD1 1 
ATOM   2888  C CD2 . TYR A 1 359 ? 13.636  6.686   -4.674  1.00 68.83  ? 359 TYR A CD2 1 
ATOM   2889  C CE1 . TYR A 1 359 ? 15.761  8.022   -5.781  1.00 69.68  ? 359 TYR A CE1 1 
ATOM   2890  C CE2 . TYR A 1 359 ? 13.523  8.036   -4.951  1.00 69.25  ? 359 TYR A CE2 1 
ATOM   2891  C CZ  . TYR A 1 359 ? 14.591  8.713   -5.501  1.00 70.31  ? 359 TYR A CZ  1 
ATOM   2892  O OH  . TYR A 1 359 ? 14.489  10.060  -5.742  1.00 69.69  ? 359 TYR A OH  1 
ATOM   2893  N N   . SER A 1 360 ? 14.877  4.567   -7.939  1.00 68.11  ? 360 SER A N   1 
ATOM   2894  C CA  . SER A 1 360 ? 15.641  4.870   -9.141  1.00 68.55  ? 360 SER A CA  1 
ATOM   2895  C C   . SER A 1 360 ? 15.233  6.227   -9.747  1.00 69.43  ? 360 SER A C   1 
ATOM   2896  O O   . SER A 1 360 ? 14.382  6.312   -10.626 1.00 70.33  ? 360 SER A O   1 
ATOM   2897  C CB  . SER A 1 360 ? 15.515  3.710   -10.106 1.00 68.61  ? 360 SER A CB  1 
ATOM   2898  O OG  . SER A 1 360 ? 15.976  4.054   -11.401 1.00 69.27  ? 360 SER A OG  1 
ATOM   2899  N N   . LYS A 1 361 ? 15.890  7.307   -9.309  1.00 69.68  ? 361 LYS A N   1 
ATOM   2900  C CA  . LYS A 1 361 ? 15.674  8.638   -9.871  1.00 70.55  ? 361 LYS A CA  1 
ATOM   2901  C C   . LYS A 1 361 ? 16.807  9.011   -10.820 1.00 68.14  ? 361 LYS A C   1 
ATOM   2902  O O   . LYS A 1 361 ? 17.955  8.856   -10.448 1.00 66.35  ? 361 LYS A O   1 
ATOM   2903  C CB  . LYS A 1 361 ? 15.658  9.681   -8.748  1.00 71.86  ? 361 LYS A CB  1 
ATOM   2904  C CG  . LYS A 1 361 ? 15.264  11.109  -9.109  1.00 74.43  ? 361 LYS A CG  1 
ATOM   2905  C CD  . LYS A 1 361 ? 13.776  11.391  -8.981  1.00 78.87  ? 361 LYS A CD  1 
ATOM   2906  C CE  . LYS A 1 361 ? 13.445  12.846  -9.003  1.00 81.36  ? 361 LYS A CE  1 
ATOM   2907  N NZ  . LYS A 1 361 ? 13.975  13.430  -10.236 1.00 84.14  ? 361 LYS A NZ  1 
ATOM   2908  N N   . ASN A 1 362 ? 16.465  9.491   -12.024 1.00 68.85  ? 362 ASN A N   1 
ATOM   2909  C CA  . ASN A 1 362 ? 17.397  10.173  -12.906 1.00 70.36  ? 362 ASN A CA  1 
ATOM   2910  C C   . ASN A 1 362 ? 17.584  11.622  -12.425 1.00 71.35  ? 362 ASN A C   1 
ATOM   2911  O O   . ASN A 1 362 ? 16.601  12.351  -12.251 1.00 72.41  ? 362 ASN A O   1 
ATOM   2912  C CB  . ASN A 1 362 ? 16.892  10.205  -14.343 1.00 72.45  ? 362 ASN A CB  1 
ATOM   2913  C CG  . ASN A 1 362 ? 16.821  8.853   -15.008 1.00 75.19  ? 362 ASN A CG  1 
ATOM   2914  O OD1 . ASN A 1 362 ? 17.540  7.911   -14.634 1.00 77.71  ? 362 ASN A OD1 1 
ATOM   2915  N ND2 . ASN A 1 362 ? 15.972  8.749   -16.024 1.00 76.79  ? 362 ASN A ND2 1 
ATOM   2916  N N   . ILE A 1 363 ? 18.836  12.068  -12.242 1.00 69.99  ? 363 ILE A N   1 
ATOM   2917  C CA  . ILE A 1 363 ? 19.079  13.394  -11.699 1.00 71.00  ? 363 ILE A CA  1 
ATOM   2918  C C   . ILE A 1 363 ? 19.122  14.401  -12.847 1.00 73.46  ? 363 ILE A C   1 
ATOM   2919  O O   . ILE A 1 363 ? 19.955  14.240  -13.739 1.00 74.65  ? 363 ILE A O   1 
ATOM   2920  C CB  . ILE A 1 363 ? 20.387  13.426  -10.888 1.00 69.12  ? 363 ILE A CB  1 
ATOM   2921  C CG1 . ILE A 1 363 ? 20.463  12.319  -9.831  1.00 67.47  ? 363 ILE A CG1 1 
ATOM   2922  C CG2 . ILE A 1 363 ? 20.583  14.810  -10.272 1.00 69.17  ? 363 ILE A CG2 1 
ATOM   2923  C CD1 . ILE A 1 363 ? 19.348  12.362  -8.809  1.00 67.53  ? 363 ILE A CD1 1 
ATOM   2924  N N   . THR A 1 364 ? 18.255  15.432  -12.831 1.00 74.37  ? 364 THR A N   1 
ATOM   2925  C CA  . THR A 1 364 ? 18.237  16.365  -13.954 1.00 77.37  ? 364 THR A CA  1 
ATOM   2926  C C   . THR A 1 364 ? 19.092  17.584  -13.632 1.00 76.49  ? 364 THR A C   1 
ATOM   2927  O O   . THR A 1 364 ? 19.845  18.044  -14.491 1.00 76.91  ? 364 THR A O   1 
ATOM   2928  C CB  . THR A 1 364 ? 16.837  16.796  -14.378 1.00 80.14  ? 364 THR A CB  1 
ATOM   2929  O OG1 . THR A 1 364 ? 16.260  17.254  -13.163 1.00 82.05  ? 364 THR A OG1 1 
ATOM   2930  C CG2 . THR A 1 364 ? 16.069  15.661  -15.031 1.00 81.49  ? 364 THR A CG2 1 
ATOM   2931  N N   . SER A 1 365 ? 18.982  18.083  -12.397 1.00 74.54  ? 365 SER A N   1 
ATOM   2932  C CA  . SER A 1 365 ? 19.817  19.193  -11.980 1.00 73.43  ? 365 SER A CA  1 
ATOM   2933  C C   . SER A 1 365 ? 20.697  18.786  -10.799 1.00 71.19  ? 365 SER A C   1 
ATOM   2934  O O   . SER A 1 365 ? 20.420  17.847  -10.066 1.00 70.06  ? 365 SER A O   1 
ATOM   2935  C CB  . SER A 1 365 ? 18.987  20.425  -11.701 1.00 74.41  ? 365 SER A CB  1 
ATOM   2936  O OG  . SER A 1 365 ? 18.302  20.326  -10.462 1.00 74.58  ? 365 SER A OG  1 
ATOM   2937  N N   . GLU A 1 366 ? 21.812  19.492  -10.645 1.00 71.89  ? 366 GLU A N   1 
ATOM   2938  C CA  . GLU A 1 366 ? 22.762  19.142  -9.610  1.00 70.47  ? 366 GLU A CA  1 
ATOM   2939  C C   . GLU A 1 366 ? 22.279  19.742  -8.299  1.00 68.22  ? 366 GLU A C   1 
ATOM   2940  O O   . GLU A 1 366 ? 21.273  20.428  -8.263  1.00 70.30  ? 366 GLU A O   1 
ATOM   2941  C CB  . GLU A 1 366 ? 24.163  19.599  -10.004 1.00 71.18  ? 366 GLU A CB  1 
ATOM   2942  C CG  . GLU A 1 366 ? 24.395  21.098  -9.894  1.00 72.59  ? 366 GLU A CG  1 
ATOM   2943  C CD  . GLU A 1 366 ? 25.873  21.433  -9.905  1.00 75.06  ? 366 GLU A CD  1 
ATOM   2944  O OE1 . GLU A 1 366 ? 26.541  20.997  -8.938  1.00 75.77  ? 366 GLU A OE1 1 
ATOM   2945  O OE2 . GLU A 1 366 ? 26.375  22.079  -10.859 1.00 78.01  ? 366 GLU A OE2 1 
ATOM   2946  N N   . GLY A 1 367 ? 22.972  19.412  -7.221  1.00 66.11  ? 367 GLY A N   1 
ATOM   2947  C CA  . GLY A 1 367 ? 22.782  20.061  -5.943  1.00 65.22  ? 367 GLY A CA  1 
ATOM   2948  C C   . GLY A 1 367 ? 21.957  19.194  -5.009  1.00 64.95  ? 367 GLY A C   1 
ATOM   2949  O O   . GLY A 1 367 ? 21.942  17.972  -5.125  1.00 66.40  ? 367 GLY A O   1 
ATOM   2950  N N   . TYR A 1 368 ? 21.244  19.874  -4.114  1.00 65.18  ? 368 TYR A N   1 
ATOM   2951  C CA  . TYR A 1 368 ? 20.340  19.252  -3.172  1.00 64.15  ? 368 TYR A CA  1 
ATOM   2952  C C   . TYR A 1 368 ? 19.170  18.686  -3.942  1.00 64.83  ? 368 TYR A C   1 
ATOM   2953  O O   . TYR A 1 368 ? 18.886  19.147  -5.033  1.00 66.03  ? 368 TYR A O   1 
ATOM   2954  C CB  . TYR A 1 368 ? 19.827  20.266  -2.157  1.00 64.21  ? 368 TYR A CB  1 
ATOM   2955  C CG  . TYR A 1 368 ? 18.885  19.716  -1.101  1.00 63.74  ? 368 TYR A CG  1 
ATOM   2956  C CD1 . TYR A 1 368 ? 17.518  19.715  -1.300  1.00 63.68  ? 368 TYR A CD1 1 
ATOM   2957  C CD2 . TYR A 1 368 ? 19.369  19.273  0.122   1.00 63.19  ? 368 TYR A CD2 1 
ATOM   2958  C CE1 . TYR A 1 368 ? 16.650  19.271  -0.320  1.00 64.16  ? 368 TYR A CE1 1 
ATOM   2959  C CE2 . TYR A 1 368 ? 18.512  18.801  1.102   1.00 63.57  ? 368 TYR A CE2 1 
ATOM   2960  C CZ  . TYR A 1 368 ? 17.147  18.808  0.882   1.00 63.97  ? 368 TYR A CZ  1 
ATOM   2961  O OH  . TYR A 1 368 ? 16.311  18.350  1.855   1.00 64.47  ? 368 TYR A OH  1 
ATOM   2962  N N   . MET A 1 369 ? 18.541  17.679  -3.347  1.00 65.17  ? 369 MET A N   1 
ATOM   2963  C CA  . MET A 1 369 ? 17.506  16.891  -3.986  1.00 65.94  ? 369 MET A CA  1 
ATOM   2964  C C   . MET A 1 369 ? 16.931  16.047  -2.868  1.00 64.29  ? 369 MET A C   1 
ATOM   2965  O O   . MET A 1 369 ? 17.690  15.431  -2.135  1.00 63.42  ? 369 MET A O   1 
ATOM   2966  C CB  . MET A 1 369 ? 18.088  16.017  -5.099  1.00 68.00  ? 369 MET A CB  1 
ATOM   2967  C CG  . MET A 1 369 ? 17.075  15.324  -5.986  1.00 71.66  ? 369 MET A CG  1 
ATOM   2968  S SD  . MET A 1 369 ? 16.605  13.641  -5.517  1.00 77.27  ? 369 MET A SD  1 
ATOM   2969  C CE  . MET A 1 369 ? 18.309  13.051  -5.525  1.00 73.70  ? 369 MET A CE  1 
ATOM   2970  N N   . ALA A 1 370 ? 15.604  16.061  -2.747  1.00 64.61  ? 370 ALA A N   1 
ATOM   2971  C CA  . ALA A 1 370 ? 14.940  15.246  -1.706  1.00 64.30  ? 370 ALA A CA  1 
ATOM   2972  C C   . ALA A 1 370 ? 13.830  14.377  -2.306  1.00 64.30  ? 370 ALA A C   1 
ATOM   2973  O O   . ALA A 1 370 ? 13.322  14.723  -3.391  1.00 63.92  ? 370 ALA A O   1 
ATOM   2974  C CB  . ALA A 1 370 ? 14.446  16.136  -0.599  1.00 64.53  ? 370 ALA A CB  1 
ATOM   2975  N N   . ASP A 1 371 ? 13.515  13.260  -1.646  1.00 64.78  ? 371 ASP A N   1 
ATOM   2976  C CA  . ASP A 1 371 ? 12.444  12.330  -2.092  1.00 65.95  ? 371 ASP A CA  1 
ATOM   2977  C C   . ASP A 1 371 ? 12.146  11.421  -0.913  1.00 66.19  ? 371 ASP A C   1 
ATOM   2978  O O   . ASP A 1 371 ? 12.537  11.762  0.217   1.00 66.71  ? 371 ASP A O   1 
ATOM   2979  C CB  . ASP A 1 371 ? 12.814  11.501  -3.305  1.00 65.90  ? 371 ASP A CB  1 
ATOM   2980  C CG  . ASP A 1 371 ? 11.677  11.154  -4.250  1.00 68.05  ? 371 ASP A CG  1 
ATOM   2981  O OD1 . ASP A 1 371 ? 10.639  10.681  -3.756  1.00 70.81  ? 371 ASP A OD1 1 
ATOM   2982  O OD2 . ASP A 1 371 ? 11.851  11.344  -5.469  1.00 68.72  ? 371 ASP A OD2 1 
ATOM   2983  N N   . GLU A 1 372 ? 11.467  10.316  -1.182  1.00 67.07  ? 372 GLU A N   1 
ATOM   2984  C CA  . GLU A 1 372 ? 11.119  9.371   -0.099  1.00 67.20  ? 372 GLU A CA  1 
ATOM   2985  C C   . GLU A 1 372 ? 11.448  7.957   -0.557  1.00 66.74  ? 372 GLU A C   1 
ATOM   2986  O O   . GLU A 1 372 ? 11.384  7.700   -1.770  1.00 66.79  ? 372 GLU A O   1 
ATOM   2987  C CB  . GLU A 1 372 ? 9.630   9.461   0.217   1.00 69.35  ? 372 GLU A CB  1 
ATOM   2988  C CG  . GLU A 1 372 ? 9.319   9.717   1.687   1.00 70.53  ? 372 GLU A CG  1 
ATOM   2989  C CD  . GLU A 1 372 ? 7.841   10.015  1.841   1.00 74.03  ? 372 GLU A CD  1 
ATOM   2990  O OE1 . GLU A 1 372 ? 7.159   10.075  0.798   1.00 75.24  ? 372 GLU A OE1 1 
ATOM   2991  O OE2 . GLU A 1 372 ? 7.372   10.185  2.983   1.00 77.79  ? 372 GLU A OE2 1 
ATOM   2992  N N   . LEU A 1 373 ? 11.814  7.094   0.383   1.00 65.98  ? 373 LEU A N   1 
ATOM   2993  C CA  . LEU A 1 373 ? 12.029  5.671   0.024   1.00 66.42  ? 373 LEU A CA  1 
ATOM   2994  C C   . LEU A 1 373 ? 10.958  4.842   0.718   1.00 67.68  ? 373 LEU A C   1 
ATOM   2995  O O   . LEU A 1 373 ? 10.709  5.099   1.910   1.00 67.30  ? 373 LEU A O   1 
ATOM   2996  C CB  . LEU A 1 373 ? 13.407  5.170   0.457   1.00 64.81  ? 373 LEU A CB  1 
ATOM   2997  C CG  . LEU A 1 373 ? 14.620  5.982   0.003   1.00 64.52  ? 373 LEU A CG  1 
ATOM   2998  C CD1 . LEU A 1 373 ? 15.745  5.692   0.971   1.00 64.32  ? 373 LEU A CD1 1 
ATOM   2999  C CD2 . LEU A 1 373 ? 15.009  5.549   -1.389  1.00 64.57  ? 373 LEU A CD2 1 
ATOM   3000  N N   . THR A 1 374 ? 10.333  3.904   -0.001  1.00 68.63  ? 374 THR A N   1 
ATOM   3001  C CA  . THR A 1 374 ? 9.443   3.009   0.702   1.00 71.30  ? 374 THR A CA  1 
ATOM   3002  C C   . THR A 1 374 ? 10.147  1.664   0.902   1.00 71.06  ? 374 THR A C   1 
ATOM   3003  O O   . THR A 1 374 ? 10.636  1.041   -0.039  1.00 70.07  ? 374 THR A O   1 
ATOM   3004  C CB  . THR A 1 374 ? 8.112   2.915   -0.048  1.00 74.49  ? 374 THR A CB  1 
ATOM   3005  O OG1 . THR A 1 374 ? 8.336   2.102   -1.191  1.00 74.51  ? 374 THR A OG1 1 
ATOM   3006  C CG2 . THR A 1 374 ? 7.608   4.258   -0.557  1.00 76.39  ? 374 THR A CG2 1 
ATOM   3007  N N   . ILE A 1 375 ? 10.168  1.219   2.159   1.00 72.05  ? 375 ILE A N   1 
ATOM   3008  C CA  . ILE A 1 375 ? 10.666  -0.098  2.530   1.00 73.67  ? 375 ILE A CA  1 
ATOM   3009  C C   . ILE A 1 375 ? 9.496   -0.956  3.032   1.00 76.13  ? 375 ILE A C   1 
ATOM   3010  O O   . ILE A 1 375 ? 8.475   -0.418  3.437   1.00 76.43  ? 375 ILE A O   1 
ATOM   3011  C CB  . ILE A 1 375 ? 11.758  0.081   3.601   1.00 72.38  ? 375 ILE A CB  1 
ATOM   3012  C CG1 . ILE A 1 375 ? 11.236  0.821   4.834   1.00 73.06  ? 375 ILE A CG1 1 
ATOM   3013  C CG2 . ILE A 1 375 ? 12.949  0.824   3.009   1.00 71.57  ? 375 ILE A CG2 1 
ATOM   3014  C CD1 . ILE A 1 375 ? 12.106  0.673   6.066   1.00 72.52  ? 375 ILE A CD1 1 
ATOM   3015  N N   . ASP A 1 376 ? 9.648   -2.285  3.065   1.00 77.63  ? 376 ASP A N   1 
ATOM   3016  C CA  . ASP A 1 376 ? 8.681   -3.130  3.757   1.00 79.27  ? 376 ASP A CA  1 
ATOM   3017  C C   . ASP A 1 376 ? 9.423   -3.938  4.829   1.00 79.49  ? 376 ASP A C   1 
ATOM   3018  O O   . ASP A 1 376 ? 9.858   -5.064  4.582   1.00 85.72  ? 376 ASP A O   1 
ATOM   3019  C CB  . ASP A 1 376 ? 7.878   -3.988  2.781   1.00 81.06  ? 376 ASP A CB  1 
ATOM   3020  C CG  . ASP A 1 376 ? 6.532   -4.481  3.311   1.00 84.29  ? 376 ASP A CG  1 
ATOM   3021  O OD1 . ASP A 1 376 ? 6.233   -4.155  4.473   1.00 85.40  ? 376 ASP A OD1 1 
ATOM   3022  O OD2 . ASP A 1 376 ? 5.768   -5.167  2.571   1.00 84.93  ? 376 ASP A OD2 1 
ATOM   3023  N N   . PRO A 1 377 ? 9.645   -3.407  6.053   1.00 74.77  ? 377 PRO A N   1 
ATOM   3024  C CA  . PRO A 1 377 ? 10.296  -4.181  7.110   1.00 72.35  ? 377 PRO A CA  1 
ATOM   3025  C C   . PRO A 1 377 ? 9.422   -5.171  7.877   1.00 71.39  ? 377 PRO A C   1 
ATOM   3026  O O   . PRO A 1 377 ? 8.348   -4.839  8.377   1.00 72.16  ? 377 PRO A O   1 
ATOM   3027  C CB  . PRO A 1 377 ? 10.839  -3.061  8.025   1.00 72.20  ? 377 PRO A CB  1 
ATOM   3028  C CG  . PRO A 1 377 ? 9.817   -1.972  7.918   1.00 73.22  ? 377 PRO A CG  1 
ATOM   3029  C CD  . PRO A 1 377 ? 9.381   -2.023  6.459   1.00 74.21  ? 377 PRO A CD  1 
ATOM   3030  N N   . VAL A 1 378 ? 9.952   -6.382  8.000   1.00 69.97  ? 378 VAL A N   1 
ATOM   3031  C CA  . VAL A 1 378 ? 9.356   -7.470  8.768   1.00 70.11  ? 378 VAL A CA  1 
ATOM   3032  C C   . VAL A 1 378 ? 9.876   -7.394  10.208  1.00 70.53  ? 378 VAL A C   1 
ATOM   3033  O O   . VAL A 1 378 ? 11.089  -7.274  10.433  1.00 71.10  ? 378 VAL A O   1 
ATOM   3034  C CB  . VAL A 1 378 ? 9.719   -8.833  8.144   1.00 68.55  ? 378 VAL A CB  1 
ATOM   3035  C CG1 . VAL A 1 378 ? 9.038   -9.946  8.899   1.00 70.06  ? 378 VAL A CG1 1 
ATOM   3036  C CG2 . VAL A 1 378 ? 9.432   -8.928  6.650   1.00 67.80  ? 378 VAL A CG2 1 
ATOM   3037  N N   . GLY A 1 379 ? 8.957   -7.448  11.173  1.00 71.50  ? 379 GLY A N   1 
ATOM   3038  C CA  . GLY A 1 379 ? 9.279   -7.382  12.590  1.00 71.80  ? 379 GLY A CA  1 
ATOM   3039  C C   . GLY A 1 379 ? 10.191  -6.201  12.913  1.00 70.90  ? 379 GLY A C   1 
ATOM   3040  O O   . GLY A 1 379 ? 9.782   -5.042  12.849  1.00 71.19  ? 379 GLY A O   1 
ATOM   3041  N N   . ILE A 1 380 ? 11.432  -6.522  13.293  1.00 69.92  ? 380 ILE A N   1 
ATOM   3042  C CA  . ILE A 1 380 ? 12.486  -5.537  13.420  1.00 68.02  ? 380 ILE A CA  1 
ATOM   3043  C C   . ILE A 1 380 ? 13.606  -5.969  12.486  1.00 67.36  ? 380 ILE A C   1 
ATOM   3044  O O   . ILE A 1 380 ? 14.237  -6.991  12.732  1.00 68.27  ? 380 ILE A O   1 
ATOM   3045  C CB  . ILE A 1 380 ? 13.033  -5.421  14.854  1.00 67.73  ? 380 ILE A CB  1 
ATOM   3046  C CG1 . ILE A 1 380 ? 11.984  -5.037  15.900  1.00 68.62  ? 380 ILE A CG1 1 
ATOM   3047  C CG2 . ILE A 1 380 ? 14.180  -4.417  14.831  1.00 66.64  ? 380 ILE A CG2 1 
ATOM   3048  C CD1 . ILE A 1 380 ? 12.493  -5.080  17.336  1.00 68.76  ? 380 ILE A CD1 1 
ATOM   3049  N N   . GLU A 1 381 ? 13.921  -5.161  11.472  1.00 66.45  ? 381 GLU A N   1 
ATOM   3050  C CA  . GLU A 1 381 ? 14.740  -5.661  10.384  1.00 65.62  ? 381 GLU A CA  1 
ATOM   3051  C C   . GLU A 1 381 ? 15.914  -4.731  10.170  1.00 64.49  ? 381 GLU A C   1 
ATOM   3052  O O   . GLU A 1 381 ? 15.686  -3.591  9.792   1.00 64.41  ? 381 GLU A O   1 
ATOM   3053  C CB  . GLU A 1 381 ? 13.938  -5.729  9.088   1.00 65.74  ? 381 GLU A CB  1 
ATOM   3054  C CG  . GLU A 1 381 ? 14.672  -6.423  7.949   1.00 64.98  ? 381 GLU A CG  1 
ATOM   3055  C CD  . GLU A 1 381 ? 13.834  -6.671  6.714   1.00 65.43  ? 381 GLU A CD  1 
ATOM   3056  O OE1 . GLU A 1 381 ? 12.658  -7.119  6.841   1.00 66.46  ? 381 GLU A OE1 1 
ATOM   3057  O OE2 . GLU A 1 381 ? 14.396  -6.422  5.622   1.00 64.48  ? 381 GLU A OE2 1 
ATOM   3058  N N   . ASP A 1 382 ? 17.146  -5.227  10.394  1.00 63.87  ? 382 ASP A N   1 
ATOM   3059  C CA  . ASP A 1 382 ? 18.312  -4.460  9.984   1.00 62.78  ? 382 ASP A CA  1 
ATOM   3060  C C   . ASP A 1 382 ? 18.368  -4.482  8.465   1.00 62.39  ? 382 ASP A C   1 
ATOM   3061  O O   . ASP A 1 382 ? 17.991  -5.469  7.858   1.00 62.57  ? 382 ASP A O   1 
ATOM   3062  C CB  . ASP A 1 382 ? 19.598  -4.985  10.592  1.00 62.69  ? 382 ASP A CB  1 
ATOM   3063  C CG  . ASP A 1 382 ? 19.893  -6.449  10.329  1.00 62.52  ? 382 ASP A CG  1 
ATOM   3064  O OD1 . ASP A 1 382 ? 19.028  -7.266  10.677  1.00 63.44  ? 382 ASP A OD1 1 
ATOM   3065  O OD2 . ASP A 1 382 ? 20.972  -6.726  9.775   1.00 61.15  ? 382 ASP A OD2 1 
ATOM   3066  N N   . MET A 1 383 ? 18.792  -3.383  7.849   1.00 62.29  ? 383 MET A N   1 
ATOM   3067  C CA  . MET A 1 383 ? 18.913  -3.364  6.406   1.00 63.29  ? 383 MET A CA  1 
ATOM   3068  C C   . MET A 1 383 ? 20.137  -2.552  6.032   1.00 64.10  ? 383 MET A C   1 
ATOM   3069  O O   . MET A 1 383 ? 20.333  -1.473  6.574   1.00 66.60  ? 383 MET A O   1 
ATOM   3070  C CB  . MET A 1 383 ? 17.705  -2.707  5.753   1.00 64.28  ? 383 MET A CB  1 
ATOM   3071  C CG  . MET A 1 383 ? 16.372  -3.299  6.214   1.00 66.34  ? 383 MET A CG  1 
ATOM   3072  S SD  . MET A 1 383 ? 14.913  -2.370  5.703   1.00 66.45  ? 383 MET A SD  1 
ATOM   3073  C CE  . MET A 1 383 ? 14.926  -2.569  3.917   1.00 66.24  ? 383 MET A CE  1 
ATOM   3074  N N   . GLU A 1 384 ? 20.967  -3.108  5.146   1.00 63.68  ? 384 GLU A N   1 
ATOM   3075  C CA  . GLU A 1 384 ? 21.933  -2.323  4.406   1.00 62.42  ? 384 GLU A CA  1 
ATOM   3076  C C   . GLU A 1 384 ? 21.269  -1.879  3.102   1.00 61.53  ? 384 GLU A C   1 
ATOM   3077  O O   . GLU A 1 384 ? 20.986  -2.703  2.229   1.00 62.10  ? 384 GLU A O   1 
ATOM   3078  C CB  . GLU A 1 384 ? 23.203  -3.163  4.242   1.00 62.73  ? 384 GLU A CB  1 
ATOM   3079  C CG  . GLU A 1 384 ? 24.241  -2.534  3.327   1.00 61.88  ? 384 GLU A CG  1 
ATOM   3080  C CD  . GLU A 1 384 ? 25.561  -3.256  3.270   1.00 62.22  ? 384 GLU A CD  1 
ATOM   3081  O OE1 . GLU A 1 384 ? 25.495  -4.508  3.185   1.00 61.02  ? 384 GLU A OE1 1 
ATOM   3082  O OE2 . GLU A 1 384 ? 26.636  -2.541  3.244   1.00 63.64  ? 384 GLU A OE2 1 
ATOM   3083  N N   . LEU A 1 385 ? 20.997  -0.573  3.013   1.00 60.12  ? 385 LEU A N   1 
ATOM   3084  C CA  . LEU A 1 385 ? 20.547  0.049   1.784   1.00 59.47  ? 385 LEU A CA  1 
ATOM   3085  C C   . LEU A 1 385 ? 21.787  0.349   0.969   1.00 59.46  ? 385 LEU A C   1 
ATOM   3086  O O   . LEU A 1 385 ? 22.760  0.849   1.522   1.00 58.73  ? 385 LEU A O   1 
ATOM   3087  C CB  . LEU A 1 385 ? 19.798  1.334   2.115   1.00 58.65  ? 385 LEU A CB  1 
ATOM   3088  C CG  . LEU A 1 385 ? 18.621  1.185   3.077   1.00 58.84  ? 385 LEU A CG  1 
ATOM   3089  C CD1 . LEU A 1 385 ? 18.015  2.537   3.357   1.00 58.74  ? 385 LEU A CD1 1 
ATOM   3090  C CD2 . LEU A 1 385 ? 17.584  0.234   2.504   1.00 59.73  ? 385 LEU A CD2 1 
ATOM   3091  N N   . ALA A 1 386 ? 21.756  0.040   -0.327  1.00 60.09  ? 386 ALA A N   1 
ATOM   3092  C CA  . ALA A 1 386 ? 22.978  0.152   -1.103  1.00 60.14  ? 386 ALA A CA  1 
ATOM   3093  C C   . ALA A 1 386 ? 22.807  1.181   -2.215  1.00 60.89  ? 386 ALA A C   1 
ATOM   3094  O O   . ALA A 1 386 ? 22.201  0.904   -3.244  1.00 62.83  ? 386 ALA A O   1 
ATOM   3095  C CB  . ALA A 1 386 ? 23.369  -1.205  -1.643  1.00 60.80  ? 386 ALA A CB  1 
ATOM   3096  N N   . PHE A 1 387 ? 23.394  2.357   -2.017  1.00 60.35  ? 387 PHE A N   1 
ATOM   3097  C CA  . PHE A 1 387 ? 23.262  3.440   -2.969  1.00 61.16  ? 387 PHE A CA  1 
ATOM   3098  C C   . PHE A 1 387 ? 24.280  3.307   -4.092  1.00 60.74  ? 387 PHE A C   1 
ATOM   3099  O O   . PHE A 1 387 ? 25.419  2.961   -3.837  1.00 60.17  ? 387 PHE A O   1 
ATOM   3100  C CB  . PHE A 1 387 ? 23.470  4.757   -2.218  1.00 61.72  ? 387 PHE A CB  1 
ATOM   3101  C CG  . PHE A 1 387 ? 22.302  5.146   -1.321  1.00 62.27  ? 387 PHE A CG  1 
ATOM   3102  C CD1 . PHE A 1 387 ? 21.964  4.377   -0.208  1.00 62.58  ? 387 PHE A CD1 1 
ATOM   3103  C CD2 . PHE A 1 387 ? 21.556  6.282   -1.592  1.00 62.14  ? 387 PHE A CD2 1 
ATOM   3104  C CE1 . PHE A 1 387 ? 20.913  4.748   0.612   1.00 62.73  ? 387 PHE A CE1 1 
ATOM   3105  C CE2 . PHE A 1 387 ? 20.504  6.636   -0.773  1.00 62.86  ? 387 PHE A CE2 1 
ATOM   3106  C CZ  . PHE A 1 387 ? 20.187  5.876   0.328   1.00 62.95  ? 387 PHE A CZ  1 
ATOM   3107  N N   . GLU A 1 388 ? 23.870  3.647   -5.320  1.00 61.33  ? 388 GLU A N   1 
ATOM   3108  C CA  . GLU A 1 388 ? 24.761  3.640   -6.470  1.00 61.32  ? 388 GLU A CA  1 
ATOM   3109  C C   . GLU A 1 388 ? 24.590  4.938   -7.260  1.00 61.34  ? 388 GLU A C   1 
ATOM   3110  O O   . GLU A 1 388 ? 23.491  5.241   -7.715  1.00 61.92  ? 388 GLU A O   1 
ATOM   3111  C CB  . GLU A 1 388 ? 24.456  2.466   -7.398  1.00 62.04  ? 388 GLU A CB  1 
ATOM   3112  C CG  . GLU A 1 388 ? 24.591  1.093   -6.746  1.00 61.89  ? 388 GLU A CG  1 
ATOM   3113  C CD  . GLU A 1 388 ? 23.954  -0.060  -7.508  1.00 62.62  ? 388 GLU A CD  1 
ATOM   3114  O OE1 . GLU A 1 388 ? 23.153  0.196   -8.451  1.00 62.83  ? 388 GLU A OE1 1 
ATOM   3115  O OE2 . GLU A 1 388 ? 24.270  -1.234  -7.138  1.00 62.86  ? 388 GLU A OE2 1 
ATOM   3116  N N   . PHE A 1 389 ? 25.694  5.672   -7.449  1.00 60.23  ? 389 PHE A N   1 
ATOM   3117  C CA  . PHE A 1 389 ? 25.684  6.862   -8.266  1.00 60.73  ? 389 PHE A CA  1 
ATOM   3118  C C   . PHE A 1 389 ? 26.229  6.549   -9.650  1.00 61.88  ? 389 PHE A C   1 
ATOM   3119  O O   . PHE A 1 389 ? 27.307  5.970   -9.758  1.00 62.04  ? 389 PHE A O   1 
ATOM   3120  C CB  . PHE A 1 389 ? 26.529  7.894   -7.531  1.00 60.70  ? 389 PHE A CB  1 
ATOM   3121  C CG  . PHE A 1 389 ? 25.988  8.206   -6.149  1.00 60.73  ? 389 PHE A CG  1 
ATOM   3122  C CD1 . PHE A 1 389 ? 26.217  7.362   -5.081  1.00 60.95  ? 389 PHE A CD1 1 
ATOM   3123  C CD2 . PHE A 1 389 ? 25.221  9.326   -5.927  1.00 61.13  ? 389 PHE A CD2 1 
ATOM   3124  C CE1 . PHE A 1 389 ? 25.709  7.645   -3.825  1.00 59.87  ? 389 PHE A CE1 1 
ATOM   3125  C CE2 . PHE A 1 389 ? 24.740  9.590   -4.667  1.00 61.14  ? 389 PHE A CE2 1 
ATOM   3126  C CZ  . PHE A 1 389 ? 24.983  8.741   -3.622  1.00 59.46  ? 389 PHE A CZ  1 
ATOM   3127  N N   . TYR A 1 390 ? 25.514  6.995   -10.691 1.00 63.68  ? 390 TYR A N   1 
ATOM   3128  C CA  . TYR A 1 390 ? 25.869  6.726   -12.077 1.00 66.20  ? 390 TYR A CA  1 
ATOM   3129  C C   . TYR A 1 390 ? 26.152  8.039   -12.795 1.00 67.51  ? 390 TYR A C   1 
ATOM   3130  O O   . TYR A 1 390 ? 25.651  9.074   -12.392 1.00 67.86  ? 390 TYR A O   1 
ATOM   3131  C CB  . TYR A 1 390 ? 24.771  6.007   -12.869 1.00 68.12  ? 390 TYR A CB  1 
ATOM   3132  C CG  . TYR A 1 390 ? 24.449  4.612   -12.355 1.00 68.50  ? 390 TYR A CG  1 
ATOM   3133  C CD1 . TYR A 1 390 ? 23.809  4.452   -11.141 1.00 68.42  ? 390 TYR A CD1 1 
ATOM   3134  C CD2 . TYR A 1 390 ? 24.815  3.466   -13.061 1.00 69.65  ? 390 TYR A CD2 1 
ATOM   3135  C CE1 . TYR A 1 390 ? 23.531  3.189   -10.652 1.00 70.20  ? 390 TYR A CE1 1 
ATOM   3136  C CE2 . TYR A 1 390 ? 24.552  2.189   -12.578 1.00 69.33  ? 390 TYR A CE2 1 
ATOM   3137  C CZ  . TYR A 1 390 ? 23.897  2.055   -11.367 1.00 69.78  ? 390 TYR A CZ  1 
ATOM   3138  O OH  . TYR A 1 390 ? 23.566  0.854   -10.820 1.00 68.22  ? 390 TYR A OH  1 
ATOM   3139  N N   . ASP A 1 391 ? 26.933  7.957   -13.880 1.00 68.87  ? 391 ASP A N   1 
ATOM   3140  C CA  . ASP A 1 391 ? 27.335  9.108   -14.658 1.00 69.60  ? 391 ASP A CA  1 
ATOM   3141  C C   . ASP A 1 391 ? 26.624  9.065   -16.008 1.00 70.71  ? 391 ASP A C   1 
ATOM   3142  O O   . ASP A 1 391 ? 25.674  8.318   -16.177 1.00 70.71  ? 391 ASP A O   1 
ATOM   3143  C CB  . ASP A 1 391 ? 28.852  9.199   -14.682 1.00 70.67  ? 391 ASP A CB  1 
ATOM   3144  C CG  . ASP A 1 391 ? 29.578  8.291   -15.658 1.00 73.35  ? 391 ASP A CG  1 
ATOM   3145  O OD1 . ASP A 1 391 ? 28.937  7.313   -16.156 1.00 75.37  ? 391 ASP A OD1 1 
ATOM   3146  O OD2 . ASP A 1 391 ? 30.776  8.594   -15.923 1.00 74.56  ? 391 ASP A OD2 1 
ATOM   3147  N N   . SER A 1 392 ? 27.069  9.886   -16.963 1.00 72.78  ? 392 SER A N   1 
ATOM   3148  C CA  . SER A 1 392 ? 26.327  10.077  -18.201 1.00 75.58  ? 392 SER A CA  1 
ATOM   3149  C C   . SER A 1 392 ? 26.343  8.805   -19.042 1.00 78.32  ? 392 SER A C   1 
ATOM   3150  O O   . SER A 1 392 ? 25.368  8.520   -19.727 1.00 78.93  ? 392 SER A O   1 
ATOM   3151  C CB  . SER A 1 392 ? 26.846  11.253  -18.990 1.00 75.85  ? 392 SER A CB  1 
ATOM   3152  O OG  . SER A 1 392 ? 28.019  10.926  -19.719 1.00 75.82  ? 392 SER A OG  1 
ATOM   3153  N N   . ASP A 1 393 ? 27.464  8.071   -18.980 1.00 81.31  ? 393 ASP A N   1 
ATOM   3154  C CA  . ASP A 1 393 ? 27.667  6.839   -19.726 1.00 83.90  ? 393 ASP A CA  1 
ATOM   3155  C C   . ASP A 1 393 ? 27.023  5.682   -18.979 1.00 84.64  ? 393 ASP A C   1 
ATOM   3156  O O   . ASP A 1 393 ? 26.979  4.575   -19.497 1.00 87.25  ? 393 ASP A O   1 
ATOM   3157  C CB  . ASP A 1 393 ? 29.141  6.563   -19.983 1.00 85.06  ? 393 ASP A CB  1 
ATOM   3158  C CG  . ASP A 1 393 ? 29.809  7.602   -20.871 1.00 87.96  ? 393 ASP A CG  1 
ATOM   3159  O OD1 . ASP A 1 393 ? 29.254  7.871   -21.961 1.00 90.76  ? 393 ASP A OD1 1 
ATOM   3160  O OD2 . ASP A 1 393 ? 30.849  8.163   -20.459 1.00 87.96  ? 393 ASP A OD2 1 
ATOM   3161  N N   . ASN A 1 394 ? 26.534  5.956   -17.766 1.00 84.33  ? 394 ASN A N   1 
ATOM   3162  C CA  . ASN A 1 394 ? 25.756  4.999   -16.996 1.00 83.25  ? 394 ASN A CA  1 
ATOM   3163  C C   . ASN A 1 394 ? 26.718  4.039   -16.302 1.00 81.80  ? 394 ASN A C   1 
ATOM   3164  O O   . ASN A 1 394 ? 26.464  2.844   -16.253 1.00 82.16  ? 394 ASN A O   1 
ATOM   3165  C CB  . ASN A 1 394 ? 24.697  4.307   -17.848 1.00 83.61  ? 394 ASN A CB  1 
ATOM   3166  C CG  . ASN A 1 394 ? 23.670  3.610   -16.989 1.00 85.44  ? 394 ASN A CG  1 
ATOM   3167  O OD1 . ASN A 1 394 ? 23.121  4.228   -16.064 1.00 85.44  ? 394 ASN A OD1 1 
ATOM   3168  N ND2 . ASN A 1 394 ? 23.409  2.334   -17.258 1.00 86.21  ? 394 ASN A ND2 1 
ATOM   3169  N N   . LYS A 1 395 ? 27.803  4.597   -15.751 1.00 81.26  ? 395 LYS A N   1 
ATOM   3170  C CA  . LYS A 1 395 ? 28.880  3.830   -15.155 1.00 80.92  ? 395 LYS A CA  1 
ATOM   3171  C C   . LYS A 1 395 ? 29.008  4.213   -13.690 1.00 75.94  ? 395 LYS A C   1 
ATOM   3172  O O   . LYS A 1 395 ? 29.215  5.372   -13.392 1.00 74.61  ? 395 LYS A O   1 
ATOM   3173  C CB  . LYS A 1 395 ? 30.199  4.173   -15.842 1.00 85.89  ? 395 LYS A CB  1 
ATOM   3174  C CG  . LYS A 1 395 ? 30.267  3.753   -17.299 1.00 95.52  ? 395 LYS A CG  1 
ATOM   3175  C CD  . LYS A 1 395 ? 31.540  4.234   -17.987 1.00 104.01 ? 395 LYS A CD  1 
ATOM   3176  C CE  . LYS A 1 395 ? 31.585  3.961   -19.464 1.00 111.66 ? 395 LYS A CE  1 
ATOM   3177  N NZ  . LYS A 1 395 ? 32.617  4.801   -20.089 1.00 114.06 ? 395 LYS A NZ  1 
ATOM   3178  N N   . ILE A 1 396 ? 28.891  3.239   -12.784 1.00 73.56  ? 396 ILE A N   1 
ATOM   3179  C CA  . ILE A 1 396 ? 28.842  3.537   -11.364 1.00 69.69  ? 396 ILE A CA  1 
ATOM   3180  C C   . ILE A 1 396 ? 30.137  4.226   -11.005 1.00 67.34  ? 396 ILE A C   1 
ATOM   3181  O O   . ILE A 1 396 ? 31.179  3.831   -11.491 1.00 68.76  ? 396 ILE A O   1 
ATOM   3182  C CB  . ILE A 1 396 ? 28.615  2.296   -10.484 1.00 69.68  ? 396 ILE A CB  1 
ATOM   3183  C CG1 . ILE A 1 396 ? 27.213  1.679   -10.731 1.00 71.51  ? 396 ILE A CG1 1 
ATOM   3184  C CG2 . ILE A 1 396 ? 28.835  2.661   -9.016  1.00 68.42  ? 396 ILE A CG2 1 
ATOM   3185  C CD1 . ILE A 1 396 ? 26.873  0.442   -9.914  1.00 71.49  ? 396 ILE A CD1 1 
ATOM   3186  N N   . ILE A 1 397 ? 30.032  5.272   -10.194 1.00 65.20  ? 397 ILE A N   1 
ATOM   3187  C CA  . ILE A 1 397 ? 31.175  6.088   -9.829  1.00 62.78  ? 397 ILE A CA  1 
ATOM   3188  C C   . ILE A 1 397 ? 31.253  6.160   -8.309  1.00 60.57  ? 397 ILE A C   1 
ATOM   3189  O O   . ILE A 1 397 ? 32.293  6.484   -7.755  1.00 60.78  ? 397 ILE A O   1 
ATOM   3190  C CB  . ILE A 1 397 ? 31.080  7.496   -10.450 1.00 62.62  ? 397 ILE A CB  1 
ATOM   3191  C CG1 . ILE A 1 397 ? 29.863  8.242   -9.946  1.00 62.76  ? 397 ILE A CG1 1 
ATOM   3192  C CG2 . ILE A 1 397 ? 31.114  7.448   -11.978 1.00 63.26  ? 397 ILE A CG2 1 
ATOM   3193  C CD1 . ILE A 1 397 ? 29.888  9.724   -10.292 1.00 64.31  ? 397 ILE A CD1 1 
ATOM   3194  N N   . LYS A 1 398 ? 30.151  5.903   -7.617  1.00 58.78  ? 398 LYS A N   1 
ATOM   3195  C CA  . LYS A 1 398 ? 30.254  5.708   -6.190  1.00 57.76  ? 398 LYS A CA  1 
ATOM   3196  C C   . LYS A 1 398 ? 29.326  4.575   -5.770  1.00 58.95  ? 398 LYS A C   1 
ATOM   3197  O O   . LYS A 1 398 ? 28.245  4.431   -6.320  1.00 60.58  ? 398 LYS A O   1 
ATOM   3198  C CB  . LYS A 1 398 ? 29.991  7.021   -5.459  1.00 56.50  ? 398 LYS A CB  1 
ATOM   3199  C CG  . LYS A 1 398 ? 30.089  6.920   -3.953  1.00 55.59  ? 398 LYS A CG  1 
ATOM   3200  C CD  . LYS A 1 398 ? 29.876  8.251   -3.257  1.00 55.23  ? 398 LYS A CD  1 
ATOM   3201  C CE  . LYS A 1 398 ? 29.964  8.232   -1.764  1.00 54.94  ? 398 LYS A CE  1 
ATOM   3202  N NZ  . LYS A 1 398 ? 29.311  9.407   -1.160  1.00 55.34  ? 398 LYS A NZ  1 
ATOM   3203  N N   . ASN A 1 399 ? 29.798  3.743   -4.840  1.00 59.28  ? 399 ASN A N   1 
ATOM   3204  C CA  . ASN A 1 399 ? 28.951  2.911   -4.016  1.00 59.87  ? 399 ASN A CA  1 
ATOM   3205  C C   . ASN A 1 399 ? 29.017  3.492   -2.607  1.00 59.98  ? 399 ASN A C   1 
ATOM   3206  O O   . ASN A 1 399 ? 30.006  4.097   -2.221  1.00 62.62  ? 399 ASN A O   1 
ATOM   3207  C CB  . ASN A 1 399 ? 29.361  1.453   -4.149  1.00 61.48  ? 399 ASN A CB  1 
ATOM   3208  C CG  . ASN A 1 399 ? 29.090  0.914   -5.536  1.00 63.52  ? 399 ASN A CG  1 
ATOM   3209  O OD1 . ASN A 1 399 ? 27.926  0.784   -5.926  1.00 66.28  ? 399 ASN A OD1 1 
ATOM   3210  N ND2 . ASN A 1 399 ? 30.124  0.565   -6.290  1.00 63.91  ? 399 ASN A ND2 1 
ATOM   3211  N N   . GLU A 1 400 ? 27.906  3.466   -1.892  1.00 60.13  ? 400 GLU A N   1 
ATOM   3212  C CA  . GLU A 1 400 ? 27.891  3.767   -0.475  1.00 60.29  ? 400 GLU A CA  1 
ATOM   3213  C C   . GLU A 1 400 ? 26.649  3.106   0.112   1.00 61.54  ? 400 GLU A C   1 
ATOM   3214  O O   . GLU A 1 400 ? 25.548  3.162   -0.460  1.00 61.77  ? 400 GLU A O   1 
ATOM   3215  C CB  . GLU A 1 400 ? 27.777  5.242   -0.084  1.00 60.56  ? 400 GLU A CB  1 
ATOM   3216  C CG  . GLU A 1 400 ? 28.176  5.508   1.369   1.00 61.85  ? 400 GLU A CG  1 
ATOM   3217  C CD  . GLU A 1 400 ? 28.284  6.966   1.846   1.00 63.95  ? 400 GLU A CD  1 
ATOM   3218  O OE1 . GLU A 1 400 ? 28.155  7.910   1.018   1.00 66.82  ? 400 GLU A OE1 1 
ATOM   3219  O OE2 . GLU A 1 400 ? 28.551  7.176   3.061   1.00 63.74  ? 400 GLU A OE2 1 
ATOM   3220  N N   . SER A 1 401 ? 26.820  2.556   1.308   1.00 60.73  ? 401 SER A N   1 
ATOM   3221  C CA  . SER A 1 401 ? 25.764  1.801   1.927   1.00 60.25  ? 401 SER A CA  1 
ATOM   3222  C C   . SER A 1 401 ? 25.309  2.506   3.204   1.00 61.27  ? 401 SER A C   1 
ATOM   3223  O O   . SER A 1 401 ? 26.121  3.048   3.928   1.00 63.10  ? 401 SER A O   1 
ATOM   3224  C CB  . SER A 1 401 ? 26.275  0.400   2.105   1.00 59.92  ? 401 SER A CB  1 
ATOM   3225  O OG  . SER A 1 401 ? 26.699  -0.132  0.843   1.00 59.01  ? 401 SER A OG  1 
ATOM   3226  N N   . ILE A 1 402 ? 23.999  2.579   3.436   1.00 62.15  ? 402 ILE A N   1 
ATOM   3227  C CA  . ILE A 1 402 ? 23.467  3.122   4.667   1.00 62.95  ? 402 ILE A CA  1 
ATOM   3228  C C   . ILE A 1 402 ? 22.778  1.996   5.421   1.00 64.39  ? 402 ILE A C   1 
ATOM   3229  O O   . ILE A 1 402 ? 21.824  1.411   4.890   1.00 66.68  ? 402 ILE A O   1 
ATOM   3230  C CB  . ILE A 1 402 ? 22.457  4.233   4.339   1.00 65.09  ? 402 ILE A CB  1 
ATOM   3231  C CG1 . ILE A 1 402 ? 23.079  5.326   3.461   1.00 67.03  ? 402 ILE A CG1 1 
ATOM   3232  C CG2 . ILE A 1 402 ? 21.831  4.815   5.610   1.00 64.85  ? 402 ILE A CG2 1 
ATOM   3233  C CD1 . ILE A 1 402 ? 24.065  6.252   4.169   1.00 67.49  ? 402 ILE A CD1 1 
ATOM   3234  N N   . ASN A 1 403 ? 23.225  1.724   6.658   1.00 63.28  ? 403 ASN A N   1 
ATOM   3235  C CA  . ASN A 1 403 ? 22.585  0.712   7.493   1.00 62.42  ? 403 ASN A CA  1 
ATOM   3236  C C   . ASN A 1 403 ? 21.529  1.338   8.402   1.00 60.43  ? 403 ASN A C   1 
ATOM   3237  O O   . ASN A 1 403 ? 21.793  2.229   9.187   1.00 59.28  ? 403 ASN A O   1 
ATOM   3238  C CB  . ASN A 1 403 ? 23.560  -0.027  8.400   1.00 63.34  ? 403 ASN A CB  1 
ATOM   3239  C CG  . ASN A 1 403 ? 24.670  -0.732  7.661   1.00 64.56  ? 403 ASN A CG  1 
ATOM   3240  O OD1 . ASN A 1 403 ? 24.517  -1.858  7.163   1.00 63.97  ? 403 ASN A OD1 1 
ATOM   3241  N ND2 . ASN A 1 403 ? 25.830  -0.092  7.647   1.00 65.64  ? 403 ASN A ND2 1 
ATOM   3242  N N   . ILE A 1 404 ? 20.319  0.818   8.354   1.00 60.50  ? 404 ILE A N   1 
ATOM   3243  C CA  . ILE A 1 404 ? 19.285  1.299   9.251   1.00 61.18  ? 404 ILE A CA  1 
ATOM   3244  C C   . ILE A 1 404 ? 18.774  0.114   10.042  1.00 61.79  ? 404 ILE A C   1 
ATOM   3245  O O   . ILE A 1 404 ? 19.038  -1.005  9.642   1.00 63.05  ? 404 ILE A O   1 
ATOM   3246  C CB  . ILE A 1 404 ? 18.157  1.993   8.470   1.00 60.70  ? 404 ILE A CB  1 
ATOM   3247  C CG1 . ILE A 1 404 ? 17.499  1.036   7.475   1.00 60.70  ? 404 ILE A CG1 1 
ATOM   3248  C CG2 . ILE A 1 404 ? 18.698  3.266   7.803   1.00 59.73  ? 404 ILE A CG2 1 
ATOM   3249  C CD1 . ILE A 1 404 ? 16.253  1.572   6.793   1.00 61.18  ? 404 ILE A CD1 1 
ATOM   3250  N N   . LEU A 1 405 ? 18.064  0.382   11.137  1.00 62.45  ? 405 LEU A N   1 
ATOM   3251  C CA  . LEU A 1 405 ? 17.241  -0.615  11.801  1.00 64.22  ? 405 LEU A CA  1 
ATOM   3252  C C   . LEU A 1 405 ? 15.779  -0.172  11.734  1.00 66.37  ? 405 LEU A C   1 
ATOM   3253  O O   . LEU A 1 405 ? 15.404  0.771   12.421  1.00 68.56  ? 405 LEU A O   1 
ATOM   3254  C CB  . LEU A 1 405 ? 17.754  -0.695  13.235  1.00 63.92  ? 405 LEU A CB  1 
ATOM   3255  C CG  . LEU A 1 405 ? 17.029  -1.703  14.123  1.00 64.94  ? 405 LEU A CG  1 
ATOM   3256  C CD1 . LEU A 1 405 ? 17.273  -3.105  13.628  1.00 65.41  ? 405 LEU A CD1 1 
ATOM   3257  C CD2 . LEU A 1 405 ? 17.494  -1.590  15.541  1.00 65.40  ? 405 LEU A CD2 1 
ATOM   3258  N N   . ALA A 1 406 ? 14.953  -0.826  10.900  1.00 67.25  ? 406 ALA A N   1 
ATOM   3259  C CA  . ALA A 1 406 ? 13.630  -0.326  10.525  1.00 66.93  ? 406 ALA A CA  1 
ATOM   3260  C C   . ALA A 1 406 ? 12.534  -1.285  10.940  1.00 69.21  ? 406 ALA A C   1 
ATOM   3261  O O   . ALA A 1 406 ? 12.783  -2.478  11.074  1.00 70.03  ? 406 ALA A O   1 
ATOM   3262  C CB  . ALA A 1 406 ? 13.523  -0.149  9.032   1.00 66.30  ? 406 ALA A CB  1 
ATOM   3263  N N   . SER A 1 407 ? 11.303  -0.748  10.982  1.00 70.92  ? 407 SER A N   1 
ATOM   3264  C CA  . SER A 1 407 ? 10.123  -1.425  11.489  1.00 70.97  ? 407 SER A CA  1 
ATOM   3265  C C   . SER A 1 407 ? 8.919   -0.549  11.171  1.00 72.08  ? 407 SER A C   1 
ATOM   3266  O O   . SER A 1 407 ? 9.066   0.648   10.950  1.00 71.27  ? 407 SER A O   1 
ATOM   3267  C CB  . SER A 1 407 ? 10.242  -1.639  12.960  1.00 71.35  ? 407 SER A CB  1 
ATOM   3268  O OG  . SER A 1 407 ? 9.260   -2.539  13.437  1.00 73.74  ? 407 SER A OG  1 
ATOM   3269  N N   . LYS A 1 408 ? 7.730   -1.151  11.153  1.00 74.14  ? 408 LYS A N   1 
ATOM   3270  C CA  . LYS A 1 408 ? 6.505   -0.432  10.842  1.00 75.78  ? 408 LYS A CA  1 
ATOM   3271  C C   . LYS A 1 408 ? 5.848   0.090   12.118  1.00 77.43  ? 408 LYS A C   1 
ATOM   3272  O O   . LYS A 1 408 ? 5.040   1.012   12.049  1.00 78.52  ? 408 LYS A O   1 
ATOM   3273  C CB  . LYS A 1 408 ? 5.485   -1.293  10.087  1.00 76.96  ? 408 LYS A CB  1 
ATOM   3274  C CG  . LYS A 1 408 ? 5.875   -1.765  8.695   1.00 76.66  ? 408 LYS A CG  1 
ATOM   3275  C CD  . LYS A 1 408 ? 4.830   -2.753  8.188   1.00 78.87  ? 408 LYS A CD  1 
ATOM   3276  C CE  . LYS A 1 408 ? 5.187   -3.426  6.896   1.00 78.98  ? 408 LYS A CE  1 
ATOM   3277  N NZ  . LYS A 1 408 ? 4.015   -4.051  6.257   1.00 80.61  ? 408 LYS A NZ  1 
ATOM   3278  N N   . THR A 1 409 ? 6.168   -0.529  13.259  1.00 78.21  ? 409 THR A N   1 
ATOM   3279  C CA  . THR A 1 409 ? 5.583   -0.174  14.542  1.00 80.21  ? 409 THR A CA  1 
ATOM   3280  C C   . THR A 1 409 ? 6.738   0.280   15.423  1.00 80.21  ? 409 THR A C   1 
ATOM   3281  O O   . THR A 1 409 ? 7.893   0.193   15.010  1.00 81.64  ? 409 THR A O   1 
ATOM   3282  C CB  . THR A 1 409 ? 4.760   -1.331  15.144  1.00 82.53  ? 409 THR A CB  1 
ATOM   3283  O OG1 . THR A 1 409 ? 5.215   -1.610  16.468  1.00 82.80  ? 409 THR A OG1 1 
ATOM   3284  C CG2 . THR A 1 409 ? 4.877   -2.691  14.463  1.00 82.70  ? 409 THR A CG2 1 
ATOM   3285  N N   . ALA A 1 410 ? 6.430   0.771   16.624  1.00 81.35  ? 410 ALA A N   1 
ATOM   3286  C CA  . ALA A 1 410 ? 7.465   1.079   17.603  1.00 81.78  ? 410 ALA A CA  1 
ATOM   3287  C C   . ALA A 1 410 ? 8.115   -0.204  18.124  1.00 83.30  ? 410 ALA A C   1 
ATOM   3288  O O   . ALA A 1 410 ? 7.541   -1.288  17.992  1.00 87.46  ? 410 ALA A O   1 
ATOM   3289  C CB  . ALA A 1 410 ? 6.851   1.858   18.738  1.00 82.85  ? 410 ALA A CB  1 
ATOM   3290  N N   . PHE A 1 411 ? 9.299   -0.082  18.745  1.00 81.40  ? 411 PHE A N   1 
ATOM   3291  C CA  . PHE A 1 411 ? 9.886   -1.201  19.472  1.00 80.66  ? 411 PHE A CA  1 
ATOM   3292  C C   . PHE A 1 411 ? 10.851  -0.707  20.545  1.00 80.56  ? 411 PHE A C   1 
ATOM   3293  O O   . PHE A 1 411 ? 11.370  0.402   20.469  1.00 81.26  ? 411 PHE A O   1 
ATOM   3294  C CB  . PHE A 1 411 ? 10.589  -2.155  18.510  1.00 79.15  ? 411 PHE A CB  1 
ATOM   3295  C CG  . PHE A 1 411 ? 11.629  -1.487  17.625  1.00 76.46  ? 411 PHE A CG  1 
ATOM   3296  C CD1 . PHE A 1 411 ? 11.257  -0.878  16.435  1.00 75.97  ? 411 PHE A CD1 1 
ATOM   3297  C CD2 . PHE A 1 411 ? 12.971  -1.490  17.972  1.00 75.54  ? 411 PHE A CD2 1 
ATOM   3298  C CE1 . PHE A 1 411 ? 12.205  -0.278  15.622  1.00 75.31  ? 411 PHE A CE1 1 
ATOM   3299  C CE2 . PHE A 1 411 ? 13.918  -0.887  17.154  1.00 74.84  ? 411 PHE A CE2 1 
ATOM   3300  C CZ  . PHE A 1 411 ? 13.532  -0.272  15.985  1.00 74.33  ? 411 PHE A CZ  1 
ATOM   3301  N N   . GLU A 1 412 ? 11.063  -1.550  21.558  1.00 82.11  ? 412 GLU A N   1 
ATOM   3302  C CA  . GLU A 1 412 ? 11.978  -1.253  22.644  1.00 83.36  ? 412 GLU A CA  1 
ATOM   3303  C C   . GLU A 1 412 ? 13.413  -1.392  22.155  1.00 82.03  ? 412 GLU A C   1 
ATOM   3304  O O   . GLU A 1 412 ? 13.713  -2.226  21.308  1.00 82.74  ? 412 GLU A O   1 
ATOM   3305  C CB  . GLU A 1 412 ? 11.897  -2.219  23.824  1.00 87.32  ? 412 GLU A CB  1 
ATOM   3306  C CG  . GLU A 1 412 ? 10.635  -2.072  24.662  1.00 92.56  ? 412 GLU A CG  1 
ATOM   3307  C CD  . GLU A 1 412 ? 10.770  -2.771  26.000  1.00 98.17  ? 412 GLU A CD  1 
ATOM   3308  O OE1 . GLU A 1 412 ? 11.204  -3.951  26.041  1.00 101.90 ? 412 GLU A OE1 1 
ATOM   3309  O OE2 . GLU A 1 412 ? 10.422  -2.112  27.003  1.00 102.55 ? 412 GLU A OE2 1 
ATOM   3310  N N   . LEU A 1 413 ? 14.293  -0.556  22.711  1.00 80.62  ? 413 LEU A N   1 
ATOM   3311  C CA  . LEU A 1 413 ? 15.722  -0.773  22.628  1.00 78.38  ? 413 LEU A CA  1 
ATOM   3312  C C   . LEU A 1 413 ? 16.225  -0.926  24.052  1.00 78.70  ? 413 LEU A C   1 
ATOM   3313  O O   . LEU A 1 413 ? 15.545  -0.531  24.997  1.00 79.42  ? 413 LEU A O   1 
ATOM   3314  C CB  . LEU A 1 413 ? 16.392  0.402   21.926  1.00 76.87  ? 413 LEU A CB  1 
ATOM   3315  C CG  . LEU A 1 413 ? 15.953  0.624   20.477  1.00 76.19  ? 413 LEU A CG  1 
ATOM   3316  C CD1 . LEU A 1 413 ? 16.453  1.932   19.913  1.00 74.42  ? 413 LEU A CD1 1 
ATOM   3317  C CD2 . LEU A 1 413 ? 16.405  -0.532  19.611  1.00 75.96  ? 413 LEU A CD2 1 
ATOM   3318  N N   . PRO A 1 414 ? 17.416  -1.518  24.254  1.00 77.49  ? 414 PRO A N   1 
ATOM   3319  C CA  . PRO A 1 414 ? 18.059  -1.435  25.556  1.00 78.50  ? 414 PRO A CA  1 
ATOM   3320  C C   . PRO A 1 414 ? 18.504  0.020   25.717  1.00 78.41  ? 414 PRO A C   1 
ATOM   3321  O O   . PRO A 1 414 ? 18.698  0.741   24.740  1.00 75.10  ? 414 PRO A O   1 
ATOM   3322  C CB  . PRO A 1 414 ? 19.196  -2.466  25.468  1.00 77.82  ? 414 PRO A CB  1 
ATOM   3323  C CG  . PRO A 1 414 ? 19.505  -2.559  23.987  1.00 76.31  ? 414 PRO A CG  1 
ATOM   3324  C CD  . PRO A 1 414 ? 18.193  -2.277  23.265  1.00 76.25  ? 414 PRO A CD  1 
ATOM   3325  N N   . GLU A 1 415 ? 18.606  0.463   26.965  1.00 81.32  ? 415 GLU A N   1 
ATOM   3326  C CA  . GLU A 1 415 ? 19.032  1.818   27.230  1.00 83.66  ? 415 GLU A CA  1 
ATOM   3327  C C   . GLU A 1 415 ? 20.018  1.796   28.385  1.00 82.83  ? 415 GLU A C   1 
ATOM   3328  O O   . GLU A 1 415 ? 19.945  0.918   29.242  1.00 84.65  ? 415 GLU A O   1 
ATOM   3329  C CB  . GLU A 1 415 ? 17.848  2.720   27.563  1.00 89.83  ? 415 GLU A CB  1 
ATOM   3330  C CG  . GLU A 1 415 ? 17.146  2.332   28.860  1.00 96.39  ? 415 GLU A CG  1 
ATOM   3331  C CD  . GLU A 1 415 ? 15.931  3.202   29.098  1.00 102.29 ? 415 GLU A CD  1 
ATOM   3332  O OE1 . GLU A 1 415 ? 14.779  2.729   28.897  1.00 101.97 ? 415 GLU A OE1 1 
ATOM   3333  O OE2 . GLU A 1 415 ? 16.184  4.392   29.447  1.00 110.02 ? 415 GLU A OE2 1 
ATOM   3334  N N   . LEU A 1 416 ? 20.926  2.779   28.359  1.00 79.93  ? 416 LEU A N   1 
ATOM   3335  C CA  . LEU A 1 416 ? 21.982  2.925   29.341  1.00 77.54  ? 416 LEU A CA  1 
ATOM   3336  C C   . LEU A 1 416 ? 21.822  4.313   29.922  1.00 75.61  ? 416 LEU A C   1 
ATOM   3337  O O   . LEU A 1 416 ? 21.670  5.262   29.160  1.00 75.46  ? 416 LEU A O   1 
ATOM   3338  C CB  . LEU A 1 416 ? 23.345  2.757   28.675  1.00 76.17  ? 416 LEU A CB  1 
ATOM   3339  C CG  . LEU A 1 416 ? 24.544  2.645   29.624  1.00 77.40  ? 416 LEU A CG  1 
ATOM   3340  C CD1 . LEU A 1 416 ? 25.779  2.112   28.912  1.00 76.50  ? 416 LEU A CD1 1 
ATOM   3341  C CD2 . LEU A 1 416 ? 24.899  3.979   30.258  1.00 78.33  ? 416 LEU A CD2 1 
ATOM   3342  N N   . THR A 1 417 ? 21.800  4.410   31.255  1.00 75.06  ? 417 THR A N   1 
ATOM   3343  C CA  . THR A 1 417 ? 21.777  5.707   31.924  1.00 74.01  ? 417 THR A CA  1 
ATOM   3344  C C   . THR A 1 417 ? 22.781  5.656   33.077  1.00 74.17  ? 417 THR A C   1 
ATOM   3345  O O   . THR A 1 417 ? 23.059  4.575   33.602  1.00 74.61  ? 417 THR A O   1 
ATOM   3346  C CB  . THR A 1 417 ? 20.370  6.102   32.407  1.00 74.29  ? 417 THR A CB  1 
ATOM   3347  O OG1 . THR A 1 417 ? 20.112  5.318   33.568  1.00 75.75  ? 417 THR A OG1 1 
ATOM   3348  C CG2 . THR A 1 417 ? 19.281  5.963   31.352  1.00 73.20  ? 417 THR A CG2 1 
ATOM   3349  N N   . ILE A 1 418 ? 23.303  6.833   33.474  1.00 73.21  ? 418 ILE A N   1 
ATOM   3350  C CA  . ILE A 1 418 ? 24.332  6.908   34.501  1.00 73.28  ? 418 ILE A CA  1 
ATOM   3351  C C   . ILE A 1 418 ? 23.907  7.893   35.588  1.00 73.93  ? 418 ILE A C   1 
ATOM   3352  O O   . ILE A 1 418 ? 23.250  8.882   35.298  1.00 73.97  ? 418 ILE A O   1 
ATOM   3353  C CB  . ILE A 1 418 ? 25.693  7.264   33.875  1.00 72.01  ? 418 ILE A CB  1 
ATOM   3354  C CG1 . ILE A 1 418 ? 25.648  8.591   33.116  1.00 70.82  ? 418 ILE A CG1 1 
ATOM   3355  C CG2 . ILE A 1 418 ? 26.212  6.124   32.991  1.00 71.12  ? 418 ILE A CG2 1 
ATOM   3356  C CD1 . ILE A 1 418 ? 27.011  9.131   32.701  1.00 69.74  ? 418 ILE A CD1 1 
ATOM   3357  N N   . GLU A 1 419 ? 24.254  7.586   36.840  1.00 75.00  ? 419 GLU A N   1 
ATOM   3358  C CA  . GLU A 1 419 ? 24.099  8.513   37.946  1.00 76.30  ? 419 GLU A CA  1 
ATOM   3359  C C   . GLU A 1 419 ? 25.477  8.830   38.514  1.00 76.84  ? 419 GLU A C   1 
ATOM   3360  O O   . GLU A 1 419 ? 26.179  7.938   38.991  1.00 77.88  ? 419 GLU A O   1 
ATOM   3361  C CB  . GLU A 1 419 ? 23.263  7.979   39.100  1.00 78.26  ? 419 GLU A CB  1 
ATOM   3362  C CG  . GLU A 1 419 ? 21.869  7.543   38.678  1.00 78.51  ? 419 GLU A CG  1 
ATOM   3363  C CD  . GLU A 1 419 ? 21.216  6.722   39.769  1.00 80.79  ? 419 GLU A CD  1 
ATOM   3364  O OE1 . GLU A 1 419 ? 20.859  7.288   40.823  1.00 82.34  ? 419 GLU A OE1 1 
ATOM   3365  O OE2 . GLU A 1 419 ? 21.129  5.491   39.566  1.00 81.26  ? 419 GLU A OE2 1 
ATOM   3366  N N   . VAL A 1 420 ? 25.820  10.119  38.493  1.00 76.52  ? 420 VAL A N   1 
ATOM   3367  C CA  . VAL A 1 420 ? 27.163  10.579  38.769  1.00 76.78  ? 420 VAL A CA  1 
ATOM   3368  C C   . VAL A 1 420 ? 27.211  11.356  40.083  1.00 79.17  ? 420 VAL A C   1 
ATOM   3369  O O   . VAL A 1 420 ? 26.304  12.123  40.410  1.00 80.15  ? 420 VAL A O   1 
ATOM   3370  C CB  . VAL A 1 420 ? 27.565  11.435  37.561  1.00 74.75  ? 420 VAL A CB  1 
ATOM   3371  C CG1 . VAL A 1 420 ? 29.001  11.938  37.671  1.00 74.54  ? 420 VAL A CG1 1 
ATOM   3372  C CG2 . VAL A 1 420 ? 27.322  10.674  36.261  1.00 73.19  ? 420 VAL A CG2 1 
ATOM   3373  N N   . THR A 1 421 ? 28.285  11.127  40.839  1.00 80.69  ? 421 THR A N   1 
ATOM   3374  C CA  . THR A 1 421 ? 28.555  11.858  42.061  1.00 83.03  ? 421 THR A CA  1 
ATOM   3375  C C   . THR A 1 421 ? 29.841  12.633  41.853  1.00 83.55  ? 421 THR A C   1 
ATOM   3376  O O   . THR A 1 421 ? 30.767  12.084  41.276  1.00 84.01  ? 421 THR A O   1 
ATOM   3377  C CB  . THR A 1 421 ? 28.721  10.890  43.223  1.00 84.74  ? 421 THR A CB  1 
ATOM   3378  O OG1 . THR A 1 421 ? 27.412  10.369  43.371  1.00 85.12  ? 421 THR A OG1 1 
ATOM   3379  C CG2 . THR A 1 421 ? 29.193  11.575  44.493  1.00 86.49  ? 421 THR A CG2 1 
ATOM   3380  N N   . PRO A 1 422 ? 29.933  13.908  42.283  1.00 84.98  ? 422 PRO A N   1 
ATOM   3381  C CA  . PRO A 1 422 ? 28.766  14.676  42.699  1.00 86.20  ? 422 PRO A CA  1 
ATOM   3382  C C   . PRO A 1 422 ? 27.906  14.842  41.456  1.00 85.20  ? 422 PRO A C   1 
ATOM   3383  O O   . PRO A 1 422 ? 28.391  14.698  40.333  1.00 83.19  ? 422 PRO A O   1 
ATOM   3384  C CB  . PRO A 1 422 ? 29.319  16.010  43.219  1.00 86.54  ? 422 PRO A CB  1 
ATOM   3385  C CG  . PRO A 1 422 ? 30.782  15.728  43.458  1.00 86.74  ? 422 PRO A CG  1 
ATOM   3386  C CD  . PRO A 1 422 ? 31.175  14.676  42.420  1.00 85.15  ? 422 PRO A CD  1 
ATOM   3387  N N   . GLU A 1 423 ? 26.627  15.117  41.694  1.00 87.05  ? 423 GLU A N   1 
ATOM   3388  C CA  . GLU A 1 423 ? 25.669  15.288  40.625  1.00 87.39  ? 423 GLU A CA  1 
ATOM   3389  C C   . GLU A 1 423 ? 25.815  16.667  39.994  1.00 87.21  ? 423 GLU A C   1 
ATOM   3390  O O   . GLU A 1 423 ? 25.857  16.755  38.770  1.00 86.96  ? 423 GLU A O   1 
ATOM   3391  C CB  . GLU A 1 423 ? 24.248  15.149  41.159  1.00 90.10  ? 423 GLU A CB  1 
ATOM   3392  C CG  . GLU A 1 423 ? 23.198  15.257  40.059  1.00 90.05  ? 423 GLU A CG  1 
ATOM   3393  C CD  . GLU A 1 423 ? 21.807  14.887  40.527  1.00 92.38  ? 423 GLU A CD  1 
ATOM   3394  O OE1 . GLU A 1 423 ? 21.570  14.934  41.756  1.00 95.19  ? 423 GLU A OE1 1 
ATOM   3395  O OE2 . GLU A 1 423 ? 20.985  14.506  39.665  1.00 92.07  ? 423 GLU A OE2 1 
ATOM   3396  N N   . LYS A 1 424 ? 25.874  17.720  40.836  1.00 88.14  ? 424 LYS A N   1 
ATOM   3397  C CA  . LYS A 1 424 ? 25.655  19.096  40.405  1.00 86.57  ? 424 LYS A CA  1 
ATOM   3398  C C   . LYS A 1 424 ? 26.931  19.931  40.505  1.00 84.84  ? 424 LYS A C   1 
ATOM   3399  O O   . LYS A 1 424 ? 27.225  20.690  39.579  1.00 83.01  ? 424 LYS A O   1 
ATOM   3400  C CB  . LYS A 1 424 ? 24.546  19.773  41.223  1.00 89.15  ? 424 LYS A CB  1 
ATOM   3401  C CG  . LYS A 1 424 ? 23.141  19.146  41.139  1.00 91.62  ? 424 LYS A CG  1 
ATOM   3402  C CD  . LYS A 1 424 ? 21.986  20.052  41.601  1.00 94.79  ? 424 LYS A CD  1 
ATOM   3403  C CE  . LYS A 1 424 ? 20.760  19.411  42.268  1.00 97.26  ? 424 LYS A CE  1 
ATOM   3404  N NZ  . LYS A 1 424 ? 19.843  18.633  41.420  1.00 96.88  ? 424 LYS A NZ  1 
ATOM   3405  N N   . ASP A 1 425 ? 27.661  19.822  41.630  1.00 85.04  ? 425 ASP A N   1 
ATOM   3406  C CA  . ASP A 1 425 ? 28.740  20.757  41.954  1.00 84.31  ? 425 ASP A CA  1 
ATOM   3407  C C   . ASP A 1 425 ? 29.990  20.007  42.454  1.00 84.50  ? 425 ASP A C   1 
ATOM   3408  O O   . ASP A 1 425 ? 30.009  19.514  43.583  1.00 86.12  ? 425 ASP A O   1 
ATOM   3409  C CB  . ASP A 1 425 ? 28.242  21.823  42.927  1.00 85.09  ? 425 ASP A CB  1 
ATOM   3410  C CG  . ASP A 1 425 ? 29.281  22.836  43.392  1.00 85.51  ? 425 ASP A CG  1 
ATOM   3411  O OD1 . ASP A 1 425 ? 30.360  22.880  42.759  1.00 84.66  ? 425 ASP A OD1 1 
ATOM   3412  O OD2 . ASP A 1 425 ? 29.029  23.544  44.402  1.00 86.13  ? 425 ASP A OD2 1 
ATOM   3413  N N   . LEU A 1 426 ? 31.063  19.997  41.635  1.00 82.70  ? 426 LEU A N   1 
ATOM   3414  C CA  . LEU A 1 426 ? 32.323  19.296  41.896  1.00 82.59  ? 426 LEU A CA  1 
ATOM   3415  C C   . LEU A 1 426 ? 33.015  19.732  43.193  1.00 84.32  ? 426 LEU A C   1 
ATOM   3416  O O   . LEU A 1 426 ? 33.979  19.086  43.615  1.00 84.51  ? 426 LEU A O   1 
ATOM   3417  C CB  . LEU A 1 426 ? 33.274  19.505  40.712  1.00 80.89  ? 426 LEU A CB  1 
ATOM   3418  C CG  . LEU A 1 426 ? 33.328  18.386  39.666  1.00 79.73  ? 426 LEU A CG  1 
ATOM   3419  C CD1 . LEU A 1 426 ? 31.918  17.997  39.257  1.00 79.57  ? 426 LEU A CD1 1 
ATOM   3420  C CD2 . LEU A 1 426 ? 34.152  18.744  38.431  1.00 77.69  ? 426 LEU A CD2 1 
ATOM   3421  N N   . ASN A 1 427 ? 32.573  20.845  43.805  1.00 85.16  ? 427 ASN A N   1 
ATOM   3422  C CA  . ASN A 1 427 ? 33.139  21.274  45.077  1.00 86.79  ? 427 ASN A CA  1 
ATOM   3423  C C   . ASN A 1 427 ? 32.644  20.382  46.220  1.00 89.00  ? 427 ASN A C   1 
ATOM   3424  O O   . ASN A 1 427 ? 33.161  20.475  47.329  1.00 90.75  ? 427 ASN A O   1 
ATOM   3425  C CB  . ASN A 1 427 ? 32.871  22.750  45.366  1.00 86.72  ? 427 ASN A CB  1 
ATOM   3426  C CG  . ASN A 1 427 ? 33.897  23.696  44.775  1.00 85.21  ? 427 ASN A CG  1 
ATOM   3427  O OD1 . ASN A 1 427 ? 35.019  23.289  44.446  1.00 84.15  ? 427 ASN A OD1 1 
ATOM   3428  N ND2 . ASN A 1 427 ? 33.539  24.969  44.663  1.00 84.61  ? 427 ASN A ND2 1 
ATOM   3429  N N   . GLU A 1 428 ? 31.663  19.507  45.955  1.00 89.10  ? 428 GLU A N   1 
ATOM   3430  C CA  . GLU A 1 428 ? 31.014  18.747  47.014  1.00 91.29  ? 428 GLU A CA  1 
ATOM   3431  C C   . GLU A 1 428 ? 31.856  17.550  47.457  1.00 92.03  ? 428 GLU A C   1 
ATOM   3432  O O   . GLU A 1 428 ? 31.557  16.941  48.482  1.00 94.14  ? 428 GLU A O   1 
ATOM   3433  C CB  . GLU A 1 428 ? 29.604  18.310  46.611  1.00 91.18  ? 428 GLU A CB  1 
ATOM   3434  C CG  . GLU A 1 428 ? 28.574  19.435  46.734  1.00 91.35  ? 428 GLU A CG  1 
ATOM   3435  C CD  . GLU A 1 428 ? 27.156  18.928  46.926  1.00 91.87  ? 428 GLU A CD  1 
ATOM   3436  O OE1 . GLU A 1 428 ? 26.973  17.663  46.881  1.00 91.00  ? 428 GLU A OE1 1 
ATOM   3437  O OE2 . GLU A 1 428 ? 26.268  19.815  47.118  1.00 91.36  ? 428 GLU A OE2 1 
ATOM   3438  N N   . GLY A 1 429 ? 32.901  17.199  46.704  1.00 90.72  ? 429 GLY A N   1 
ATOM   3439  C CA  . GLY A 1 429 ? 33.740  16.095  47.131  1.00 92.00  ? 429 GLY A CA  1 
ATOM   3440  C C   . GLY A 1 429 ? 35.017  15.978  46.309  1.00 91.00  ? 429 GLY A C   1 
ATOM   3441  O O   . GLY A 1 429 ? 35.117  16.538  45.217  1.00 88.49  ? 429 GLY A O   1 
ATOM   3442  N N   . LYS A 1 430 ? 35.959  15.192  46.846  1.00 92.72  ? 430 LYS A N   1 
ATOM   3443  C CA  . LYS A 1 430 ? 37.241  14.981  46.202  1.00 92.44  ? 430 LYS A CA  1 
ATOM   3444  C C   . LYS A 1 430 ? 37.131  13.791  45.255  1.00 90.73  ? 430 LYS A C   1 
ATOM   3445  O O   . LYS A 1 430 ? 37.884  13.693  44.284  1.00 89.55  ? 430 LYS A O   1 
ATOM   3446  C CB  . LYS A 1 430 ? 38.344  14.763  47.245  1.00 95.40  ? 430 LYS A CB  1 
ATOM   3447  C CG  . LYS A 1 430 ? 38.157  15.508  48.565  1.00 98.48  ? 430 LYS A CG  1 
ATOM   3448  C CD  . LYS A 1 430 ? 39.453  15.824  49.306  1.00 101.18 ? 430 LYS A CD  1 
ATOM   3449  C CE  . LYS A 1 430 ? 39.393  15.580  50.801  1.00 104.80 ? 430 LYS A CE  1 
ATOM   3450  N NZ  . LYS A 1 430 ? 38.489  16.453  51.560  1.00 105.87 ? 430 LYS A NZ  1 
ATOM   3451  N N   . ILE A 1 431 ? 36.175  12.897  45.537  1.00 90.65  ? 431 ILE A N   1 
ATOM   3452  C CA  . ILE A 1 431 ? 36.082  11.636  44.822  1.00 89.45  ? 431 ILE A CA  1 
ATOM   3453  C C   . ILE A 1 431 ? 34.723  11.520  44.146  1.00 87.74  ? 431 ILE A C   1 
ATOM   3454  O O   . ILE A 1 431 ? 33.704  11.751  44.784  1.00 88.35  ? 431 ILE A O   1 
ATOM   3455  C CB  . ILE A 1 431 ? 36.333  10.460  45.778  1.00 91.46  ? 431 ILE A CB  1 
ATOM   3456  C CG1 . ILE A 1 431 ? 37.740  10.538  46.386  1.00 93.07  ? 431 ILE A CG1 1 
ATOM   3457  C CG2 . ILE A 1 431 ? 36.084  9.129   45.067  1.00 90.53  ? 431 ILE A CG2 1 
ATOM   3458  C CD1 . ILE A 1 431 ? 37.981  9.572   47.535  1.00 95.88  ? 431 ILE A CD1 1 
ATOM   3459  N N   . ALA A 1 432 ? 34.751  11.086  42.879  1.00 85.83  ? 432 ALA A N   1 
ATOM   3460  C CA  . ALA A 1 432 ? 33.580  10.956  42.027  1.00 84.88  ? 432 ALA A CA  1 
ATOM   3461  C C   . ALA A 1 432 ? 33.193  9.490   41.833  1.00 85.97  ? 432 ALA A C   1 
ATOM   3462  O O   . ALA A 1 432 ? 34.048  8.599   41.926  1.00 87.17  ? 432 ALA A O   1 
ATOM   3463  C CB  . ALA A 1 432 ? 33.896  11.580  40.689  1.00 82.76  ? 432 ALA A CB  1 
ATOM   3464  N N   . SER A 1 433 ? 31.918  9.243   41.486  1.00 85.33  ? 433 SER A N   1 
ATOM   3465  C CA  . SER A 1 433 ? 31.514  7.912   41.042  1.00 85.08  ? 433 SER A CA  1 
ATOM   3466  C C   . SER A 1 433 ? 30.596  7.975   39.823  1.00 82.77  ? 433 SER A C   1 
ATOM   3467  O O   . SER A 1 433 ? 29.859  8.934   39.645  1.00 83.05  ? 433 SER A O   1 
ATOM   3468  C CB  . SER A 1 433 ? 30.849  7.135   42.139  1.00 87.62  ? 433 SER A CB  1 
ATOM   3469  O OG  . SER A 1 433 ? 29.474  7.476   42.240  1.00 88.38  ? 433 SER A OG  1 
ATOM   3470  N N   . ILE A 1 434 ? 30.650  6.934   38.990  1.00 81.11  ? 434 ILE A N   1 
ATOM   3471  C CA  . ILE A 1 434 ? 29.712  6.759   37.898  1.00 79.19  ? 434 ILE A CA  1 
ATOM   3472  C C   . ILE A 1 434 ? 29.018  5.422   38.130  1.00 80.68  ? 434 ILE A C   1 
ATOM   3473  O O   . ILE A 1 434 ? 29.644  4.371   38.035  1.00 80.89  ? 434 ILE A O   1 
ATOM   3474  C CB  . ILE A 1 434 ? 30.421  6.812   36.530  1.00 76.62  ? 434 ILE A CB  1 
ATOM   3475  C CG1 . ILE A 1 434 ? 31.067  8.177   36.283  1.00 75.83  ? 434 ILE A CG1 1 
ATOM   3476  C CG2 . ILE A 1 434 ? 29.468  6.438   35.397  1.00 75.15  ? 434 ILE A CG2 1 
ATOM   3477  C CD1 . ILE A 1 434 ? 31.859  8.290   34.987  1.00 74.08  ? 434 ILE A CD1 1 
ATOM   3478  N N   . LYS A 1 435 ? 27.725  5.475   38.467  1.00 81.74  ? 435 LYS A N   1 
ATOM   3479  C CA  . LYS A 1 435 ? 26.899  4.284   38.544  1.00 81.84  ? 435 LYS A CA  1 
ATOM   3480  C C   . LYS A 1 435 ? 26.223  4.089   37.198  1.00 80.79  ? 435 LYS A C   1 
ATOM   3481  O O   . LYS A 1 435 ? 25.274  4.790   36.904  1.00 81.08  ? 435 LYS A O   1 
ATOM   3482  C CB  . LYS A 1 435 ? 25.879  4.445   39.673  1.00 83.14  ? 435 LYS A CB  1 
ATOM   3483  C CG  . LYS A 1 435 ? 26.541  4.397   41.031  1.00 85.03  ? 435 LYS A CG  1 
ATOM   3484  C CD  . LYS A 1 435 ? 25.605  4.065   42.180  1.00 87.17  ? 435 LYS A CD  1 
ATOM   3485  C CE  . LYS A 1 435 ? 24.806  5.228   42.630  1.00 87.56  ? 435 LYS A CE  1 
ATOM   3486  N NZ  . LYS A 1 435 ? 24.115  4.835   43.858  1.00 90.04  ? 435 LYS A NZ  1 
ATOM   3487  N N   . THR A 1 436 ? 26.726  3.159   36.384  1.00 80.94  ? 436 THR A N   1 
ATOM   3488  C CA  . THR A 1 436 ? 26.090  2.805   35.123  1.00 80.50  ? 436 THR A CA  1 
ATOM   3489  C C   . THR A 1 436 ? 24.951  1.818   35.391  1.00 82.26  ? 436 THR A C   1 
ATOM   3490  O O   . THR A 1 436 ? 25.017  1.042   36.345  1.00 84.02  ? 436 THR A O   1 
ATOM   3491  C CB  . THR A 1 436 ? 27.139  2.241   34.163  1.00 79.59  ? 436 THR A CB  1 
ATOM   3492  O OG1 . THR A 1 436 ? 28.089  3.291   33.992  1.00 78.66  ? 436 THR A OG1 1 
ATOM   3493  C CG2 . THR A 1 436 ? 26.567  1.854   32.811  1.00 77.94  ? 436 THR A CG2 1 
ATOM   3494  N N   . LYS A 1 437 ? 23.898  1.897   34.555  1.00 82.35  ? 437 LYS A N   1 
ATOM   3495  C CA  . LYS A 1 437 ? 22.726  1.028   34.615  1.00 84.04  ? 437 LYS A CA  1 
ATOM   3496  C C   . LYS A 1 437 ? 22.236  0.740   33.197  1.00 82.55  ? 437 LYS A C   1 
ATOM   3497  O O   . LYS A 1 437 ? 21.972  1.671   32.443  1.00 81.42  ? 437 LYS A O   1 
ATOM   3498  C CB  . LYS A 1 437 ? 21.554  1.667   35.361  1.00 85.77  ? 437 LYS A CB  1 
ATOM   3499  C CG  . LYS A 1 437 ? 20.240  0.924   35.223  1.00 87.71  ? 437 LYS A CG  1 
ATOM   3500  C CD  . LYS A 1 437 ? 19.018  1.813   35.407  1.00 89.42  ? 437 LYS A CD  1 
ATOM   3501  C CE  . LYS A 1 437 ? 17.731  1.128   35.049  1.00 90.41  ? 437 LYS A CE  1 
ATOM   3502  N NZ  . LYS A 1 437 ? 16.580  2.030   35.182  1.00 91.17  ? 437 LYS A NZ  1 
ATOM   3503  N N   . ILE A 1 438 ? 22.116  -0.548  32.852  1.00 83.03  ? 438 ILE A N   1 
ATOM   3504  C CA  . ILE A 1 438 ? 21.792  -0.955  31.494  1.00 82.72  ? 438 ILE A CA  1 
ATOM   3505  C C   . ILE A 1 438 ? 20.518  -1.791  31.556  1.00 85.26  ? 438 ILE A C   1 
ATOM   3506  O O   . ILE A 1 438 ? 20.532  -2.908  32.081  1.00 88.29  ? 438 ILE A O   1 
ATOM   3507  C CB  . ILE A 1 438 ? 22.937  -1.754  30.818  1.00 81.91  ? 438 ILE A CB  1 
ATOM   3508  C CG1 . ILE A 1 438 ? 24.334  -1.144  31.034  1.00 80.69  ? 438 ILE A CG1 1 
ATOM   3509  C CG2 . ILE A 1 438 ? 22.651  -1.944  29.327  1.00 80.86  ? 438 ILE A CG2 1 
ATOM   3510  C CD1 . ILE A 1 438 ? 25.414  -1.613  30.063  1.00 78.62  ? 438 ILE A CD1 1 
ATOM   3511  N N   . GLU A 1 439 ? 19.426  -1.262  30.999  1.00 85.40  ? 439 GLU A N   1 
ATOM   3512  C CA  . GLU A 1 439 ? 18.247  -2.079  30.759  1.00 88.01  ? 439 GLU A CA  1 
ATOM   3513  C C   . GLU A 1 439 ? 18.492  -2.891  29.486  1.00 85.25  ? 439 GLU A C   1 
ATOM   3514  O O   . GLU A 1 439 ? 18.673  -2.312  28.419  1.00 83.40  ? 439 GLU A O   1 
ATOM   3515  C CB  . GLU A 1 439 ? 16.980  -1.222  30.654  1.00 91.25  ? 439 GLU A CB  1 
ATOM   3516  C CG  . GLU A 1 439 ? 16.251  -0.985  31.981  1.00 96.02  ? 439 GLU A CG  1 
ATOM   3517  C CD  . GLU A 1 439 ? 15.029  -0.054  31.979  1.00 98.23  ? 439 GLU A CD  1 
ATOM   3518  O OE1 . GLU A 1 439 ? 14.946  0.831   31.094  1.00 97.22  ? 439 GLU A OE1 1 
ATOM   3519  O OE2 . GLU A 1 439 ? 14.148  -0.201  32.867  1.00 99.83  ? 439 GLU A OE2 1 
ATOM   3520  N N   . THR A 1 440 ? 18.503  -4.222  29.601  1.00 84.42  ? 440 THR A N   1 
ATOM   3521  C CA  . THR A 1 440 ? 18.700  -5.091  28.451  1.00 83.86  ? 440 THR A CA  1 
ATOM   3522  C C   . THR A 1 440 ? 17.388  -5.201  27.684  1.00 85.39  ? 440 THR A C   1 
ATOM   3523  O O   . THR A 1 440 ? 16.357  -4.820  28.214  1.00 86.73  ? 440 THR A O   1 
ATOM   3524  C CB  . THR A 1 440 ? 19.198  -6.462  28.915  1.00 84.33  ? 440 THR A CB  1 
ATOM   3525  O OG1 . THR A 1 440 ? 18.324  -6.963  29.925  1.00 84.57  ? 440 THR A OG1 1 
ATOM   3526  C CG2 . THR A 1 440 ? 20.611  -6.387  29.466  1.00 84.17  ? 440 THR A CG2 1 
ATOM   3527  N N   . SER A 1 441 ? 17.428  -5.710  26.445  1.00 86.55  ? 441 SER A N   1 
ATOM   3528  C CA  . SER A 1 441 ? 16.213  -6.029  25.702  1.00 89.17  ? 441 SER A CA  1 
ATOM   3529  C C   . SER A 1 441 ? 16.458  -7.287  24.875  1.00 90.33  ? 441 SER A C   1 
ATOM   3530  O O   . SER A 1 441 ? 17.533  -7.444  24.281  1.00 88.82  ? 441 SER A O   1 
ATOM   3531  C CB  . SER A 1 441 ? 15.750  -4.869  24.835  1.00 88.72  ? 441 SER A CB  1 
ATOM   3532  O OG  . SER A 1 441 ? 14.396  -5.016  24.425  1.00 90.66  ? 441 SER A OG  1 
ATOM   3533  N N   . GLU A 1 442 ? 15.468  -8.192  24.852  1.00 91.82  ? 442 GLU A N   1 
ATOM   3534  C CA  . GLU A 1 442 ? 15.654  -9.422  24.104  1.00 91.96  ? 442 GLU A CA  1 
ATOM   3535  C C   . GLU A 1 442 ? 15.711  -9.100  22.610  1.00 92.94  ? 442 GLU A C   1 
ATOM   3536  O O   . GLU A 1 442 ? 15.242  -8.057  22.150  1.00 93.53  ? 442 GLU A O   1 
ATOM   3537  C CB  . GLU A 1 442 ? 14.737  -10.582 24.494  1.00 93.14  ? 442 GLU A CB  1 
ATOM   3538  C CG  . GLU A 1 442 ? 13.232  -10.427 24.279  1.00 93.67  ? 442 GLU A CG  1 
ATOM   3539  C CD  . GLU A 1 442 ? 12.506  -11.760 24.530  1.00 94.84  ? 442 GLU A CD  1 
ATOM   3540  O OE1 . GLU A 1 442 ? 13.229  -12.799 24.510  1.00 92.59  ? 442 GLU A OE1 1 
ATOM   3541  O OE2 . GLU A 1 442 ? 11.261  -11.794 24.760  1.00 94.44  ? 442 GLU A OE2 1 
ATOM   3542  N N   . ASN A 1 443 ? 16.383  -10.004 21.891  1.00 94.01  ? 443 ASN A N   1 
ATOM   3543  C CA  . ASN A 1 443 ? 16.824  -9.837  20.513  1.00 92.49  ? 443 ASN A CA  1 
ATOM   3544  C C   . ASN A 1 443 ? 17.989  -8.854  20.420  1.00 87.55  ? 443 ASN A C   1 
ATOM   3545  O O   . ASN A 1 443 ? 18.774  -8.982  19.484  1.00 88.42  ? 443 ASN A O   1 
ATOM   3546  C CB  . ASN A 1 443 ? 15.696  -9.533  19.531  1.00 94.42  ? 443 ASN A CB  1 
ATOM   3547  C CG  . ASN A 1 443 ? 14.718  -10.684 19.408  1.00 95.90  ? 443 ASN A CG  1 
ATOM   3548  O OD1 . ASN A 1 443 ? 15.026  -11.737 18.834  1.00 92.70  ? 443 ASN A OD1 1 
ATOM   3549  N ND2 . ASN A 1 443 ? 13.518  -10.490 19.928  1.00 98.04  ? 443 ASN A ND2 1 
ATOM   3550  N N   . PHE A 1 444 ? 18.171  -7.949  21.394  1.00 84.21  ? 444 PHE A N   1 
ATOM   3551  C CA  . PHE A 1 444 ? 19.277  -6.996  21.314  1.00 81.49  ? 444 PHE A CA  1 
ATOM   3552  C C   . PHE A 1 444 ? 20.469  -7.532  22.106  1.00 82.21  ? 444 PHE A C   1 
ATOM   3553  O O   . PHE A 1 444 ? 20.349  -7.704  23.314  1.00 85.08  ? 444 PHE A O   1 
ATOM   3554  C CB  . PHE A 1 444 ? 18.838  -5.591  21.748  1.00 78.54  ? 444 PHE A CB  1 
ATOM   3555  C CG  . PHE A 1 444 ? 17.979  -4.941  20.675  1.00 76.03  ? 444 PHE A CG  1 
ATOM   3556  C CD1 . PHE A 1 444 ? 18.562  -4.319  19.580  1.00 73.36  ? 444 PHE A CD1 1 
ATOM   3557  C CD2 . PHE A 1 444 ? 16.594  -5.008  20.734  1.00 76.82  ? 444 PHE A CD2 1 
ATOM   3558  C CE1 . PHE A 1 444 ? 17.794  -3.764  18.577  1.00 72.07  ? 444 PHE A CE1 1 
ATOM   3559  C CE2 . PHE A 1 444 ? 15.829  -4.433  19.737  1.00 76.02  ? 444 PHE A CE2 1 
ATOM   3560  C CZ  . PHE A 1 444 ? 16.436  -3.813  18.662  1.00 73.70  ? 444 PHE A CZ  1 
ATOM   3561  N N   . THR A 1 445 ? 21.610  -7.763  21.425  1.00 80.05  ? 445 THR A N   1 
ATOM   3562  C CA  . THR A 1 445 ? 22.778  -8.383  22.042  1.00 80.02  ? 445 THR A CA  1 
ATOM   3563  C C   . THR A 1 445 ? 23.834  -7.333  22.375  1.00 77.86  ? 445 THR A C   1 
ATOM   3564  O O   . THR A 1 445 ? 24.415  -6.704  21.490  1.00 74.66  ? 445 THR A O   1 
ATOM   3565  C CB  . THR A 1 445 ? 23.374  -9.463  21.141  1.00 80.92  ? 445 THR A CB  1 
ATOM   3566  O OG1 . THR A 1 445 ? 22.734  -9.243  19.894  1.00 83.73  ? 445 THR A OG1 1 
ATOM   3567  C CG2 . THR A 1 445 ? 23.024  -10.871 21.572  1.00 82.99  ? 445 THR A CG2 1 
ATOM   3568  N N   . LEU A 1 446 ? 24.096  -7.209  23.679  1.00 78.39  ? 446 LEU A N   1 
ATOM   3569  C CA  . LEU A 1 446 ? 25.201  -6.433  24.201  1.00 77.94  ? 446 LEU A CA  1 
ATOM   3570  C C   . LEU A 1 446 ? 26.490  -7.192  23.965  1.00 80.19  ? 446 LEU A C   1 
ATOM   3571  O O   . LEU A 1 446 ? 26.532  -8.415  24.084  1.00 82.42  ? 446 LEU A O   1 
ATOM   3572  C CB  . LEU A 1 446 ? 25.035  -6.229  25.703  1.00 78.32  ? 446 LEU A CB  1 
ATOM   3573  C CG  . LEU A 1 446 ? 23.775  -5.509  26.169  1.00 78.00  ? 446 LEU A CG  1 
ATOM   3574  C CD1 . LEU A 1 446 ? 23.824  -5.313  27.675  1.00 78.48  ? 446 LEU A CD1 1 
ATOM   3575  C CD2 . LEU A 1 446 ? 23.662  -4.194  25.420  1.00 77.27  ? 446 LEU A CD2 1 
ATOM   3576  N N   . LEU A 1 447 ? 27.583  -6.470  23.763  1.00 81.91  ? 447 LEU A N   1 
ATOM   3577  C CA  . LEU A 1 447 ? 28.792  -7.198  23.456  1.00 86.06  ? 447 LEU A CA  1 
ATOM   3578  C C   . LEU A 1 447 ? 30.044  -6.589  24.090  1.00 88.46  ? 447 LEU A C   1 
ATOM   3579  O O   . LEU A 1 447 ? 30.051  -5.433  24.466  1.00 89.23  ? 447 LEU A O   1 
ATOM   3580  C CB  . LEU A 1 447 ? 28.783  -7.301  21.931  1.00 84.60  ? 447 LEU A CB  1 
ATOM   3581  C CG  . LEU A 1 447 ? 28.813  -6.003  21.127  1.00 81.01  ? 447 LEU A CG  1 
ATOM   3582  C CD1 . LEU A 1 447 ? 30.245  -5.545  21.080  1.00 81.27  ? 447 LEU A CD1 1 
ATOM   3583  C CD2 . LEU A 1 447 ? 28.264  -6.197  19.727  1.00 79.24  ? 447 LEU A CD2 1 
ATOM   3584  N N   . ASP A 1 448 ? 31.074  -7.425  24.284  1.00 96.14  ? 448 ASP A N   1 
ATOM   3585  C CA  . ASP A 1 448 ? 32.353  -6.999  24.837  1.00 104.76 ? 448 ASP A CA  1 
ATOM   3586  C C   . ASP A 1 448 ? 32.148  -6.188  26.120  1.00 100.35 ? 448 ASP A C   1 
ATOM   3587  O O   . ASP A 1 448 ? 31.699  -6.714  27.145  1.00 101.43 ? 448 ASP A O   1 
ATOM   3588  C CB  . ASP A 1 448 ? 33.189  -6.202  23.831  1.00 110.62 ? 448 ASP A CB  1 
ATOM   3589  C CG  . ASP A 1 448 ? 33.903  -6.979  22.731  1.00 114.29 ? 448 ASP A CG  1 
ATOM   3590  O OD1 . ASP A 1 448 ? 34.956  -7.598  23.033  1.00 114.45 ? 448 ASP A OD1 1 
ATOM   3591  O OD2 . ASP A 1 448 ? 33.405  -6.942  21.578  1.00 116.05 ? 448 ASP A OD2 1 
ATOM   3592  N N   . ASP A 1 449 ? 32.480  -4.896  26.012  1.00 92.30  ? 449 ASP A N   1 
ATOM   3593  C CA  . ASP A 1 449 ? 32.903  -4.100  27.142  1.00 91.04  ? 449 ASP A CA  1 
ATOM   3594  C C   . ASP A 1 449 ? 32.188  -2.758  27.062  1.00 83.17  ? 449 ASP A C   1 
ATOM   3595  O O   . ASP A 1 449 ? 32.249  -2.049  26.062  1.00 78.46  ? 449 ASP A O   1 
ATOM   3596  C CB  . ASP A 1 449 ? 34.418  -3.927  27.210  1.00 96.13  ? 449 ASP A CB  1 
ATOM   3597  C CG  . ASP A 1 449 ? 35.257  -5.099  27.720  1.00 103.28 ? 449 ASP A CG  1 
ATOM   3598  O OD1 . ASP A 1 449 ? 34.717  -6.229  27.875  1.00 105.85 ? 449 ASP A OD1 1 
ATOM   3599  O OD2 . ASP A 1 449 ? 36.467  -4.871  27.973  1.00 106.75 ? 449 ASP A OD2 1 
ATOM   3600  N N   . LEU A 1 450 ? 31.414  -2.530  28.118  1.00 79.70  ? 450 LEU A N   1 
ATOM   3601  C CA  . LEU A 1 450 ? 31.035  -1.237  28.634  1.00 76.73  ? 450 LEU A CA  1 
ATOM   3602  C C   . LEU A 1 450 ? 32.284  -0.389  28.825  1.00 76.89  ? 450 LEU A C   1 
ATOM   3603  O O   . LEU A 1 450 ? 33.284  -0.902  29.315  1.00 78.13  ? 450 LEU A O   1 
ATOM   3604  C CB  . LEU A 1 450 ? 30.397  -1.644  29.959  1.00 76.82  ? 450 LEU A CB  1 
ATOM   3605  C CG  . LEU A 1 450 ? 30.179  -0.539  30.985  1.00 76.90  ? 450 LEU A CG  1 
ATOM   3606  C CD1 . LEU A 1 450 ? 29.201  0.463   30.421  1.00 76.11  ? 450 LEU A CD1 1 
ATOM   3607  C CD2 . LEU A 1 450 ? 29.699  -1.123  32.295  1.00 78.43  ? 450 LEU A CD2 1 
ATOM   3608  N N   . LYS A 1 451 ? 32.224  0.900   28.477  1.00 76.04  ? 451 LYS A N   1 
ATOM   3609  C CA  . LYS A 1 451 ? 33.380  1.769   28.653  1.00 77.14  ? 451 LYS A CA  1 
ATOM   3610  C C   . LYS A 1 451 ? 32.985  2.983   29.486  1.00 77.21  ? 451 LYS A C   1 
ATOM   3611  O O   . LYS A 1 451 ? 31.913  3.534   29.288  1.00 78.70  ? 451 LYS A O   1 
ATOM   3612  C CB  . LYS A 1 451 ? 34.001  2.131   27.297  1.00 77.11  ? 451 LYS A CB  1 
ATOM   3613  C CG  . LYS A 1 451 ? 34.752  0.969   26.627  1.00 78.72  ? 451 LYS A CG  1 
ATOM   3614  C CD  . LYS A 1 451 ? 35.521  1.290   25.351  1.00 77.94  ? 451 LYS A CD  1 
ATOM   3615  C CE  . LYS A 1 451 ? 36.030  0.044   24.716  1.00 79.82  ? 451 LYS A CE  1 
ATOM   3616  N NZ  . LYS A 1 451 ? 36.578  0.365   23.397  1.00 80.62  ? 451 LYS A NZ  1 
ATOM   3617  N N   . ILE A 1 452 ? 33.836  3.385   30.436  1.00 76.36  ? 452 ILE A N   1 
ATOM   3618  C CA  . ILE A 1 452 ? 33.505  4.509   31.298  1.00 75.97  ? 452 ILE A CA  1 
ATOM   3619  C C   . ILE A 1 452 ? 34.549  5.624   31.084  1.00 75.13  ? 452 ILE A C   1 
ATOM   3620  O O   . ILE A 1 452 ? 35.713  5.311   30.799  1.00 75.52  ? 452 ILE A O   1 
ATOM   3621  C CB  . ILE A 1 452 ? 33.392  4.018   32.759  1.00 77.37  ? 452 ILE A CB  1 
ATOM   3622  C CG1 . ILE A 1 452 ? 32.104  3.255   33.052  1.00 77.56  ? 452 ILE A CG1 1 
ATOM   3623  C CG2 . ILE A 1 452 ? 33.481  5.194   33.720  1.00 78.74  ? 452 ILE A CG2 1 
ATOM   3624  C CD1 . ILE A 1 452 ? 31.934  1.955   32.306  1.00 76.98  ? 452 ILE A CD1 1 
ATOM   3625  N N   . SER A 1 453 ? 34.147  6.913   31.212  1.00 73.32  ? 453 SER A N   1 
ATOM   3626  C CA  . SER A 1 453 ? 35.052  8.050   31.028  1.00 72.44  ? 453 SER A CA  1 
ATOM   3627  C C   . SER A 1 453 ? 34.664  9.268   31.871  1.00 72.74  ? 453 SER A C   1 
ATOM   3628  O O   . SER A 1 453 ? 33.613  9.884   31.653  1.00 72.29  ? 453 SER A O   1 
ATOM   3629  C CB  . SER A 1 453 ? 35.148  8.492   29.581  1.00 71.00  ? 453 SER A CB  1 
ATOM   3630  O OG  . SER A 1 453 ? 35.711  9.801   29.478  1.00 70.56  ? 453 SER A OG  1 
ATOM   3631  N N   . TYR A 1 454 ? 35.588  9.668   32.753  1.00 72.71  ? 454 TYR A N   1 
ATOM   3632  C CA  . TYR A 1 454 ? 35.461  10.887  33.535  1.00 72.54  ? 454 TYR A CA  1 
ATOM   3633  C C   . TYR A 1 454 ? 36.492  11.863  32.959  1.00 71.60  ? 454 TYR A C   1 
ATOM   3634  O O   . TYR A 1 454 ? 37.627  11.925  33.424  1.00 71.87  ? 454 TYR A O   1 
ATOM   3635  C CB  . TYR A 1 454 ? 35.590  10.484  35.015  1.00 74.54  ? 454 TYR A CB  1 
ATOM   3636  C CG  . TYR A 1 454 ? 35.107  11.503  36.041  1.00 75.87  ? 454 TYR A CG  1 
ATOM   3637  C CD1 . TYR A 1 454 ? 33.776  11.569  36.422  1.00 76.48  ? 454 TYR A CD1 1 
ATOM   3638  C CD2 . TYR A 1 454 ? 35.973  12.413  36.637  1.00 77.20  ? 454 TYR A CD2 1 
ATOM   3639  C CE1 . TYR A 1 454 ? 33.318  12.525  37.324  1.00 77.93  ? 454 TYR A CE1 1 
ATOM   3640  C CE2 . TYR A 1 454 ? 35.527  13.375  37.540  1.00 78.40  ? 454 TYR A CE2 1 
ATOM   3641  C CZ  . TYR A 1 454 ? 34.191  13.436  37.898  1.00 78.73  ? 454 TYR A CZ  1 
ATOM   3642  O OH  . TYR A 1 454 ? 33.736  14.364  38.808  1.00 79.15  ? 454 TYR A OH  1 
ATOM   3643  N N   . ASN A 1 455 ? 36.105  12.568  31.884  1.00 69.99  ? 455 ASN A N   1 
ATOM   3644  C CA  . ASN A 1 455 ? 37.003  13.462  31.176  1.00 69.16  ? 455 ASN A CA  1 
ATOM   3645  C C   . ASN A 1 455 ? 37.073  14.776  31.940  1.00 69.85  ? 455 ASN A C   1 
ATOM   3646  O O   . ASN A 1 455 ? 36.099  15.512  31.941  1.00 70.29  ? 455 ASN A O   1 
ATOM   3647  C CB  . ASN A 1 455 ? 36.576  13.703  29.730  1.00 67.48  ? 455 ASN A CB  1 
ATOM   3648  C CG  . ASN A 1 455 ? 37.592  14.535  28.968  1.00 67.60  ? 455 ASN A CG  1 
ATOM   3649  O OD1 . ASN A 1 455 ? 38.285  15.391  29.543  1.00 67.82  ? 455 ASN A OD1 1 
ATOM   3650  N ND2 . ASN A 1 455 ? 37.663  14.348  27.657  1.00 66.62  ? 455 ASN A ND2 1 
ATOM   3651  N N   . THR A 1 456 ? 38.242  15.083  32.514  1.00 70.30  ? 456 THR A N   1 
ATOM   3652  C CA  . THR A 1 456 ? 38.384  16.181  33.458  1.00 71.30  ? 456 THR A CA  1 
ATOM   3653  C C   . THR A 1 456 ? 38.859  17.469  32.776  1.00 70.33  ? 456 THR A C   1 
ATOM   3654  O O   . THR A 1 456 ? 39.171  18.413  33.487  1.00 70.72  ? 456 THR A O   1 
ATOM   3655  C CB  . THR A 1 456 ? 39.345  15.764  34.576  1.00 72.90  ? 456 THR A CB  1 
ATOM   3656  O OG1 . THR A 1 456 ? 40.395  15.063  33.922  1.00 72.58  ? 456 THR A OG1 1 
ATOM   3657  C CG2 . THR A 1 456 ? 38.716  14.860  35.618  1.00 73.79  ? 456 THR A CG2 1 
ATOM   3658  N N   . HIS A 1 457 ? 38.973  17.486  31.432  1.00 69.21  ? 457 HIS A N   1 
ATOM   3659  C CA  . HIS A 1 457 ? 39.118  18.695  30.612  1.00 68.81  ? 457 HIS A CA  1 
ATOM   3660  C C   . HIS A 1 457 ? 40.442  19.454  30.788  1.00 69.87  ? 457 HIS A C   1 
ATOM   3661  O O   . HIS A 1 457 ? 40.552  20.594  30.287  1.00 70.50  ? 457 HIS A O   1 
ATOM   3662  C CB  . HIS A 1 457 ? 37.922  19.646  30.794  1.00 68.70  ? 457 HIS A CB  1 
ATOM   3663  C CG  . HIS A 1 457 ? 36.780  19.252  29.922  1.00 68.00  ? 457 HIS A CG  1 
ATOM   3664  N ND1 . HIS A 1 457 ? 35.908  18.221  30.215  1.00 68.50  ? 457 HIS A ND1 1 
ATOM   3665  C CD2 . HIS A 1 457 ? 36.425  19.715  28.712  1.00 67.05  ? 457 HIS A CD2 1 
ATOM   3666  C CE1 . HIS A 1 457 ? 35.034  18.101  29.221  1.00 67.66  ? 457 HIS A CE1 1 
ATOM   3667  N NE2 . HIS A 1 457 ? 35.325  19.012  28.301  1.00 66.77  ? 457 HIS A NE2 1 
ATOM   3668  N N   . LEU A 1 458 ? 41.421  18.817  31.466  1.00 70.23  ? 458 LEU A N   1 
ATOM   3669  C CA  . LEU A 1 458 ? 42.735  19.378  31.742  1.00 70.44  ? 458 LEU A CA  1 
ATOM   3670  C C   . LEU A 1 458 ? 43.547  19.356  30.456  1.00 69.93  ? 458 LEU A C   1 
ATOM   3671  O O   . LEU A 1 458 ? 44.306  18.418  30.220  1.00 70.37  ? 458 LEU A O   1 
ATOM   3672  C CB  . LEU A 1 458 ? 43.509  18.587  32.796  1.00 71.72  ? 458 LEU A CB  1 
ATOM   3673  C CG  . LEU A 1 458 ? 42.861  18.395  34.165  1.00 72.67  ? 458 LEU A CG  1 
ATOM   3674  C CD1 . LEU A 1 458 ? 43.818  17.681  35.106  1.00 74.10  ? 458 LEU A CD1 1 
ATOM   3675  C CD2 . LEU A 1 458 ? 42.433  19.720  34.740  1.00 72.92  ? 458 LEU A CD2 1 
ATOM   3676  N N   . GLY A 1 459 ? 43.394  20.390  29.636  1.00 69.30  ? 459 GLY A N   1 
ATOM   3677  C CA  . GLY A 1 459 ? 44.169  20.500  28.418  1.00 69.38  ? 459 GLY A CA  1 
ATOM   3678  C C   . GLY A 1 459 ? 43.610  19.586  27.343  1.00 68.99  ? 459 GLY A C   1 
ATOM   3679  O O   . GLY A 1 459 ? 42.461  19.759  26.960  1.00 72.07  ? 459 GLY A O   1 
ATOM   3680  N N   . TRP A 1 460 ? 44.425  18.649  26.852  1.00 68.84  ? 460 TRP A N   1 
ATOM   3681  C CA  . TRP A 1 460 ? 43.956  17.594  25.969  1.00 68.59  ? 460 TRP A CA  1 
ATOM   3682  C C   . TRP A 1 460 ? 43.836  16.253  26.704  1.00 69.38  ? 460 TRP A C   1 
ATOM   3683  O O   . TRP A 1 460 ? 43.228  15.315  26.183  1.00 69.48  ? 460 TRP A O   1 
ATOM   3684  C CB  . TRP A 1 460 ? 44.894  17.444  24.769  1.00 68.63  ? 460 TRP A CB  1 
ATOM   3685  C CG  . TRP A 1 460 ? 45.052  18.694  23.964  1.00 68.87  ? 460 TRP A CG  1 
ATOM   3686  C CD1 . TRP A 1 460 ? 46.134  19.516  23.900  1.00 71.14  ? 460 TRP A CD1 1 
ATOM   3687  C CD2 . TRP A 1 460 ? 44.061  19.266  23.099  1.00 68.73  ? 460 TRP A CD2 1 
ATOM   3688  N NE1 . TRP A 1 460 ? 45.871  20.582  23.073  1.00 71.39  ? 460 TRP A NE1 1 
ATOM   3689  C CE2 . TRP A 1 460 ? 44.612  20.446  22.559  1.00 69.41  ? 460 TRP A CE2 1 
ATOM   3690  C CE3 . TRP A 1 460 ? 42.766  18.900  22.746  1.00 67.89  ? 460 TRP A CE3 1 
ATOM   3691  C CZ2 . TRP A 1 460 ? 43.918  21.249  21.668  1.00 68.47  ? 460 TRP A CZ2 1 
ATOM   3692  C CZ3 . TRP A 1 460 ? 42.080  19.690  21.860  1.00 67.66  ? 460 TRP A CZ3 1 
ATOM   3693  C CH2 . TRP A 1 460 ? 42.643  20.856  21.341  1.00 67.88  ? 460 TRP A CH2 1 
ATOM   3694  N N   . ALA A 1 461 ? 44.443  16.154  27.895  1.00 69.79  ? 461 ALA A N   1 
ATOM   3695  C CA  . ALA A 1 461 ? 44.279  15.002  28.766  1.00 70.37  ? 461 ALA A CA  1 
ATOM   3696  C C   . ALA A 1 461 ? 42.798  14.621  28.912  1.00 69.98  ? 461 ALA A C   1 
ATOM   3697  O O   . ALA A 1 461 ? 42.008  15.416  29.424  1.00 69.49  ? 461 ALA A O   1 
ATOM   3698  C CB  . ALA A 1 461 ? 44.923  15.302  30.107  1.00 71.60  ? 461 ALA A CB  1 
ATOM   3699  N N   . ILE A 1 462 ? 42.459  13.388  28.490  1.00 69.88  ? 462 ILE A N   1 
ATOM   3700  C CA  . ILE A 1 462 ? 41.095  12.874  28.484  1.00 70.60  ? 462 ILE A CA  1 
ATOM   3701  C C   . ILE A 1 462 ? 40.741  12.190  29.812  1.00 72.18  ? 462 ILE A C   1 
ATOM   3702  O O   . ILE A 1 462 ? 39.625  11.663  29.963  1.00 73.04  ? 462 ILE A O   1 
ATOM   3703  C CB  . ILE A 1 462 ? 40.866  11.918  27.294  1.00 70.37  ? 462 ILE A CB  1 
ATOM   3704  C CG1 . ILE A 1 462 ? 41.719  10.661  27.378  1.00 71.32  ? 462 ILE A CG1 1 
ATOM   3705  C CG2 . ILE A 1 462 ? 41.063  12.621  25.955  1.00 69.36  ? 462 ILE A CG2 1 
ATOM   3706  C CD1 . ILE A 1 462 ? 41.066  9.496   28.099  1.00 72.79  ? 462 ILE A CD1 1 
ATOM   3707  N N   . GLY A 1 463 ? 41.671  12.197  30.776  1.00 72.66  ? 463 GLY A N   1 
ATOM   3708  C CA  . GLY A 1 463 ? 41.354  11.791  32.135  1.00 74.25  ? 463 GLY A CA  1 
ATOM   3709  C C   . GLY A 1 463 ? 41.158  10.274  32.256  1.00 75.45  ? 463 GLY A C   1 
ATOM   3710  O O   . GLY A 1 463 ? 41.693  9.485   31.469  1.00 74.26  ? 463 GLY A O   1 
ATOM   3711  N N   . SER A 1 464 ? 40.399  9.863   33.277  1.00 76.92  ? 464 SER A N   1 
ATOM   3712  C CA  . SER A 1 464 ? 40.226  8.453   33.561  1.00 78.24  ? 464 SER A CA  1 
ATOM   3713  C C   . SER A 1 464 ? 39.420  7.772   32.460  1.00 77.12  ? 464 SER A C   1 
ATOM   3714  O O   . SER A 1 464 ? 38.725  8.428   31.677  1.00 76.31  ? 464 SER A O   1 
ATOM   3715  C CB  . SER A 1 464 ? 39.585  8.237   34.887  1.00 80.12  ? 464 SER A CB  1 
ATOM   3716  O OG  . SER A 1 464 ? 40.496  8.524   35.935  1.00 82.24  ? 464 SER A OG  1 
ATOM   3717  N N   . GLN A 1 465 ? 39.573  6.450   32.417  1.00 77.22  ? 465 GLN A N   1 
ATOM   3718  C CA  . GLN A 1 465 ? 38.737  5.588   31.610  1.00 77.88  ? 465 GLN A CA  1 
ATOM   3719  C C   . GLN A 1 465 ? 38.719  4.208   32.255  1.00 80.36  ? 465 GLN A C   1 
ATOM   3720  O O   . GLN A 1 465 ? 39.514  3.906   33.144  1.00 83.78  ? 465 GLN A O   1 
ATOM   3721  C CB  . GLN A 1 465 ? 39.267  5.439   30.189  1.00 77.34  ? 465 GLN A CB  1 
ATOM   3722  C CG  . GLN A 1 465 ? 38.879  6.562   29.244  1.00 77.34  ? 465 GLN A CG  1 
ATOM   3723  C CD  . GLN A 1 465 ? 39.372  6.295   27.844  1.00 78.06  ? 465 GLN A CD  1 
ATOM   3724  O OE1 . GLN A 1 465 ? 40.584  6.306   27.596  1.00 80.75  ? 465 GLN A OE1 1 
ATOM   3725  N NE2 . GLN A 1 465 ? 38.454  6.019   26.929  1.00 77.56  ? 465 GLN A NE2 1 
ATOM   3726  N N   . ALA A 1 466 ? 37.829  3.343   31.785  1.00 79.27  ? 466 ALA A N   1 
ATOM   3727  C CA  . ALA A 1 466 ? 37.769  2.007   32.344  1.00 79.90  ? 466 ALA A CA  1 
ATOM   3728  C C   . ALA A 1 466 ? 37.129  1.052   31.341  1.00 78.48  ? 466 ALA A C   1 
ATOM   3729  O O   . ALA A 1 466 ? 36.313  1.448   30.527  1.00 77.27  ? 466 ALA A O   1 
ATOM   3730  C CB  . ALA A 1 466 ? 37.031  2.070   33.665  1.00 81.12  ? 466 ALA A CB  1 
ATOM   3731  N N   . SER A 1 467 ? 37.552  -0.201  31.361  1.00 80.07  ? 467 SER A N   1 
ATOM   3732  C CA  . SER A 1 467 ? 36.809  -1.250  30.688  1.00 81.26  ? 467 SER A CA  1 
ATOM   3733  C C   . SER A 1 467 ? 36.267  -2.224  31.730  1.00 80.94  ? 467 SER A C   1 
ATOM   3734  O O   . SER A 1 467 ? 37.036  -2.891  32.412  1.00 80.37  ? 467 SER A O   1 
ATOM   3735  C CB  . SER A 1 467 ? 37.650  -1.955  29.654  1.00 82.86  ? 467 SER A CB  1 
ATOM   3736  O OG  . SER A 1 467 ? 37.911  -1.071  28.570  1.00 83.88  ? 467 SER A OG  1 
ATOM   3737  N N   . VAL A 1 468 ? 34.935  -2.258  31.849  1.00 79.82  ? 468 VAL A N   1 
ATOM   3738  C CA  . VAL A 1 468 ? 34.253  -3.186  32.737  1.00 80.22  ? 468 VAL A CA  1 
ATOM   3739  C C   . VAL A 1 468 ? 33.670  -4.342  31.918  1.00 78.61  ? 468 VAL A C   1 
ATOM   3740  O O   . VAL A 1 468 ? 32.940  -4.146  30.947  1.00 76.13  ? 468 VAL A O   1 
ATOM   3741  C CB  . VAL A 1 468 ? 33.203  -2.381  33.530  1.00 80.00  ? 468 VAL A CB  1 
ATOM   3742  C CG1 . VAL A 1 468 ? 32.338  -3.229  34.443  1.00 81.15  ? 468 VAL A CG1 1 
ATOM   3743  C CG2 . VAL A 1 468 ? 33.884  -1.319  34.366  1.00 80.63  ? 468 VAL A CG2 1 
ATOM   3744  N N   . SER A 1 469 ? 34.057  -5.557  32.301  1.00 80.01  ? 469 SER A N   1 
ATOM   3745  C CA  . SER A 1 469 ? 33.484  -6.766  31.734  1.00 80.53  ? 469 SER A CA  1 
ATOM   3746  C C   . SER A 1 469 ? 32.090  -6.981  32.321  1.00 81.58  ? 469 SER A C   1 
ATOM   3747  O O   . SER A 1 469 ? 31.868  -6.802  33.517  1.00 82.61  ? 469 SER A O   1 
ATOM   3748  C CB  . SER A 1 469 ? 34.389  -7.950  31.993  1.00 81.63  ? 469 SER A CB  1 
ATOM   3749  O OG  . SER A 1 469 ? 33.808  -9.173  31.558  1.00 81.83  ? 469 SER A OG  1 
ATOM   3750  N N   . ILE A 1 470 ? 31.146  -7.395  31.481  1.00 81.42  ? 470 ILE A N   1 
ATOM   3751  C CA  . ILE A 1 470 ? 29.829  -7.746  31.987  1.00 83.32  ? 470 ILE A CA  1 
ATOM   3752  C C   . ILE A 1 470 ? 29.519  -9.200  31.652  1.00 84.30  ? 470 ILE A C   1 
ATOM   3753  O O   . ILE A 1 470 ? 28.347  -9.544  31.566  1.00 85.02  ? 470 ILE A O   1 
ATOM   3754  C CB  . ILE A 1 470 ? 28.751  -6.816  31.403  1.00 82.61  ? 470 ILE A CB  1 
ATOM   3755  C CG1 . ILE A 1 470 ? 28.631  -7.026  29.880  1.00 82.03  ? 470 ILE A CG1 1 
ATOM   3756  C CG2 . ILE A 1 470 ? 29.023  -5.362  31.782  1.00 81.65  ? 470 ILE A CG2 1 
ATOM   3757  C CD1 . ILE A 1 470 ? 27.807  -5.986  29.149  1.00 80.68  ? 470 ILE A CD1 1 
ATOM   3758  N N   . SER A 1 471 ? 30.558  -10.034 31.470  1.00 85.29  ? 471 SER A N   1 
ATOM   3759  C CA  . SER A 1 471 ? 30.400  -11.463 31.210  1.00 86.30  ? 471 SER A CA  1 
ATOM   3760  C C   . SER A 1 471 ? 29.421  -12.068 32.205  1.00 87.65  ? 471 SER A C   1 
ATOM   3761  O O   . SER A 1 471 ? 28.469  -12.744 31.833  1.00 87.20  ? 471 SER A O   1 
ATOM   3762  C CB  . SER A 1 471 ? 31.715  -12.189 31.314  1.00 87.33  ? 471 SER A CB  1 
ATOM   3763  O OG  . SER A 1 471 ? 32.785  -11.312 31.001  1.00 86.98  ? 471 SER A OG  1 
ATOM   3764  N N   . ASP A 1 472 ? 29.682  -11.769 33.477  1.00 89.62  ? 472 ASP A N   1 
ATOM   3765  C CA  . ASP A 1 472 ? 29.054  -12.437 34.597  1.00 93.09  ? 472 ASP A CA  1 
ATOM   3766  C C   . ASP A 1 472 ? 27.666  -11.864 34.885  1.00 94.42  ? 472 ASP A C   1 
ATOM   3767  O O   . ASP A 1 472 ? 27.051  -12.282 35.860  1.00 97.95  ? 472 ASP A O   1 
ATOM   3768  C CB  . ASP A 1 472 ? 29.946  -12.317 35.822  1.00 94.72  ? 472 ASP A CB  1 
ATOM   3769  C CG  . ASP A 1 472 ? 30.347  -10.889 36.154  1.00 93.81  ? 472 ASP A CG  1 
ATOM   3770  O OD1 . ASP A 1 472 ? 29.622  -9.968  35.724  1.00 93.69  ? 472 ASP A OD1 1 
ATOM   3771  O OD2 . ASP A 1 472 ? 31.397  -10.706 36.793  1.00 94.26  ? 472 ASP A OD2 1 
ATOM   3772  N N   . GLN A 1 473 ? 27.179  -10.910 34.070  1.00 93.03  ? 473 GLN A N   1 
ATOM   3773  C CA  . GLN A 1 473 ? 25.872  -10.298 34.278  1.00 92.10  ? 473 GLN A CA  1 
ATOM   3774  C C   . GLN A 1 473 ? 24.956  -10.449 33.054  1.00 92.81  ? 473 GLN A C   1 
ATOM   3775  O O   . GLN A 1 473 ? 23.819  -9.979  33.108  1.00 93.61  ? 473 GLN A O   1 
ATOM   3776  C CB  . GLN A 1 473 ? 26.041  -8.814  34.604  1.00 90.99  ? 473 GLN A CB  1 
ATOM   3777  C CG  . GLN A 1 473 ? 26.510  -8.482  36.021  1.00 91.72  ? 473 GLN A CG  1 
ATOM   3778  C CD  . GLN A 1 473 ? 26.541  -6.986  36.313  1.00 89.33  ? 473 GLN A CD  1 
ATOM   3779  O OE1 . GLN A 1 473 ? 25.531  -6.276  36.306  1.00 87.52  ? 473 GLN A OE1 1 
ATOM   3780  N NE2 . GLN A 1 473 ? 27.719  -6.469  36.604  1.00 89.11  ? 473 GLN A NE2 1 
ATOM   3781  N N   . LEU A 1 474 ? 25.408  -11.125 31.977  1.00 94.54  ? 474 LEU A N   1 
ATOM   3782  C CA  . LEU A 1 474 ? 24.659  -11.218 30.722  1.00 95.86  ? 474 LEU A CA  1 
ATOM   3783  C C   . LEU A 1 474 ? 23.234  -11.707 30.970  1.00 100.02 ? 474 LEU A C   1 
ATOM   3784  O O   . LEU A 1 474 ? 22.318  -11.166 30.364  1.00 105.08 ? 474 LEU A O   1 
ATOM   3785  C CB  . LEU A 1 474 ? 25.288  -12.106 29.646  1.00 96.45  ? 474 LEU A CB  1 
ATOM   3786  C CG  . LEU A 1 474 ? 26.188  -11.452 28.589  1.00 95.65  ? 474 LEU A CG  1 
ATOM   3787  C CD1 . LEU A 1 474 ? 25.697  -10.136 27.991  1.00 93.77  ? 474 LEU A CD1 1 
ATOM   3788  C CD2 . LEU A 1 474 ? 27.584  -11.290 29.162  1.00 97.32  ? 474 LEU A CD2 1 
ATOM   3789  N N   . ASP A 1 475 ? 23.065  -12.738 31.814  1.00 102.38 ? 475 ASP A N   1 
ATOM   3790  C CA  . ASP A 1 475 ? 21.762  -13.313 32.119  1.00 103.47 ? 475 ASP A CA  1 
ATOM   3791  C C   . ASP A 1 475 ? 20.741  -12.263 32.538  1.00 102.61 ? 475 ASP A C   1 
ATOM   3792  O O   . ASP A 1 475 ? 19.586  -12.359 32.135  1.00 102.12 ? 475 ASP A O   1 
ATOM   3793  C CB  . ASP A 1 475 ? 21.841  -14.333 33.244  1.00 108.20 ? 475 ASP A CB  1 
ATOM   3794  C CG  . ASP A 1 475 ? 22.235  -15.735 32.803  1.00 111.07 ? 475 ASP A CG  1 
ATOM   3795  O OD1 . ASP A 1 475 ? 22.518  -15.892 31.596  1.00 112.93 ? 475 ASP A OD1 1 
ATOM   3796  O OD2 . ASP A 1 475 ? 22.252  -16.656 33.659  1.00 112.01 ? 475 ASP A OD2 1 
ATOM   3797  N N   . LYS A 1 476 ? 21.182  -11.272 33.334  1.00 103.90 ? 476 LYS A N   1 
ATOM   3798  C CA  . LYS A 1 476 ? 20.311  -10.341 34.050  1.00 101.06 ? 476 LYS A CA  1 
ATOM   3799  C C   . LYS A 1 476 ? 19.619  -9.359  33.114  1.00 96.20  ? 476 LYS A C   1 
ATOM   3800  O O   . LYS A 1 476 ? 20.114  -9.046  32.027  1.00 91.43  ? 476 LYS A O   1 
ATOM   3801  C CB  . LYS A 1 476 ? 21.079  -9.484  35.063  1.00 100.90 ? 476 LYS A CB  1 
ATOM   3802  C CG  . LYS A 1 476 ? 21.906  -10.255 36.080  1.00 102.49 ? 476 LYS A CG  1 
ATOM   3803  C CD  . LYS A 1 476 ? 22.995  -9.429  36.747  1.00 102.53 ? 476 LYS A CD  1 
ATOM   3804  C CE  . LYS A 1 476 ? 22.439  -8.448  37.727  1.00 104.74 ? 476 LYS A CE  1 
ATOM   3805  N NZ  . LYS A 1 476 ? 23.363  -7.329  37.950  1.00 104.76 ? 476 LYS A NZ  1 
ATOM   3806  N N   . LYS A 1 477 ? 18.485  -8.855  33.606  1.00 97.00  ? 477 LYS A N   1 
ATOM   3807  C CA  . LYS A 1 477 ? 17.723  -7.856  32.892  1.00 96.41  ? 477 LYS A CA  1 
ATOM   3808  C C   . LYS A 1 477 ? 18.425  -6.515  33.089  1.00 94.01  ? 477 LYS A C   1 
ATOM   3809  O O   . LYS A 1 477 ? 18.691  -5.843  32.098  1.00 93.95  ? 477 LYS A O   1 
ATOM   3810  C CB  . LYS A 1 477 ? 16.248  -7.987  33.290  1.00 99.36  ? 477 LYS A CB  1 
ATOM   3811  C CG  . LYS A 1 477 ? 15.303  -7.244  32.367  1.00 101.28 ? 477 LYS A CG  1 
ATOM   3812  C CD  . LYS A 1 477 ? 14.775  -5.931  32.944  1.00 105.45 ? 477 LYS A CD  1 
ATOM   3813  C CE  . LYS A 1 477 ? 15.096  -4.667  32.169  1.00 107.20 ? 477 LYS A CE  1 
ATOM   3814  N NZ  . LYS A 1 477 ? 15.283  -4.790  30.716  1.00 107.16 ? 477 LYS A NZ  1 
ATOM   3815  N N   . ILE A 1 478 ? 18.785  -6.175  34.343  1.00 94.17  ? 478 ILE A N   1 
ATOM   3816  C CA  . ILE A 1 478 ? 19.388  -4.883  34.684  1.00 92.20  ? 478 ILE A CA  1 
ATOM   3817  C C   . ILE A 1 478 ? 20.855  -5.095  35.052  1.00 90.64  ? 478 ILE A C   1 
ATOM   3818  O O   . ILE A 1 478 ? 21.144  -5.690  36.094  1.00 90.90  ? 478 ILE A O   1 
ATOM   3819  C CB  . ILE A 1 478 ? 18.650  -4.192  35.851  1.00 93.64  ? 478 ILE A CB  1 
ATOM   3820  C CG1 . ILE A 1 478 ? 17.145  -4.064  35.607  1.00 94.76  ? 478 ILE A CG1 1 
ATOM   3821  C CG2 . ILE A 1 478 ? 19.278  -2.841  36.183  1.00 93.27  ? 478 ILE A CG2 1 
ATOM   3822  C CD1 . ILE A 1 478 ? 16.674  -2.701  35.135  1.00 93.96  ? 478 ILE A CD1 1 
ATOM   3823  N N   . ILE A 1 479 ? 21.757  -4.565  34.208  1.00 87.67  ? 479 ILE A N   1 
ATOM   3824  C CA  . ILE A 1 479 ? 23.194  -4.628  34.446  1.00 86.48  ? 479 ILE A CA  1 
ATOM   3825  C C   . ILE A 1 479 ? 23.649  -3.337  35.117  1.00 84.90  ? 479 ILE A C   1 
ATOM   3826  O O   . ILE A 1 479 ? 23.329  -2.242  34.649  1.00 82.74  ? 479 ILE A O   1 
ATOM   3827  C CB  . ILE A 1 479 ? 23.960  -4.890  33.138  1.00 85.29  ? 479 ILE A CB  1 
ATOM   3828  C CG1 . ILE A 1 479 ? 23.434  -6.148  32.434  1.00 86.54  ? 479 ILE A CG1 1 
ATOM   3829  C CG2 . ILE A 1 479 ? 25.459  -4.990  33.401  1.00 85.05  ? 479 ILE A CG2 1 
ATOM   3830  C CD1 . ILE A 1 479 ? 24.153  -6.491  31.139  1.00 85.20  ? 479 ILE A CD1 1 
ATOM   3831  N N   . THR A 1 480 ? 24.411  -3.483  36.209  1.00 85.20  ? 480 THR A N   1 
ATOM   3832  C CA  . THR A 1 480 ? 24.815  -2.336  37.013  1.00 85.41  ? 480 THR A CA  1 
ATOM   3833  C C   . THR A 1 480 ? 26.329  -2.342  37.212  1.00 84.80  ? 480 THR A C   1 
ATOM   3834  O O   . THR A 1 480 ? 26.936  -3.390  37.234  1.00 85.93  ? 480 THR A O   1 
ATOM   3835  C CB  . THR A 1 480 ? 24.081  -2.390  38.347  1.00 87.31  ? 480 THR A CB  1 
ATOM   3836  O OG1 . THR A 1 480 ? 24.443  -3.671  38.854  1.00 88.82  ? 480 THR A OG1 1 
ATOM   3837  C CG2 . THR A 1 480 ? 22.576  -2.326  38.184  1.00 87.43  ? 480 THR A CG2 1 
ATOM   3838  N N   . SER A 1 481 ? 26.937  -1.163  37.353  1.00 84.42  ? 481 SER A N   1 
ATOM   3839  C CA  . SER A 1 481 ? 28.378  -1.044  37.513  1.00 84.17  ? 481 SER A CA  1 
ATOM   3840  C C   . SER A 1 481 ? 28.723  0.305   38.133  1.00 82.92  ? 481 SER A C   1 
ATOM   3841  O O   . SER A 1 481 ? 28.389  1.339   37.580  1.00 81.28  ? 481 SER A O   1 
ATOM   3842  C CB  . SER A 1 481 ? 29.106  -1.204  36.203  1.00 83.18  ? 481 SER A CB  1 
ATOM   3843  O OG  . SER A 1 481 ? 30.519  -1.184  36.396  1.00 84.72  ? 481 SER A OG  1 
ATOM   3844  N N   . GLU A 1 482 ? 29.450  0.257   39.249  1.00 83.81  ? 482 GLU A N   1 
ATOM   3845  C CA  . GLU A 1 482 ? 29.869  1.431   39.989  1.00 83.74  ? 482 GLU A CA  1 
ATOM   3846  C C   . GLU A 1 482 ? 31.384  1.577   39.909  1.00 83.59  ? 482 GLU A C   1 
ATOM   3847  O O   . GLU A 1 482 ? 32.126  0.693   40.291  1.00 84.81  ? 482 GLU A O   1 
ATOM   3848  C CB  . GLU A 1 482 ? 29.412  1.252   41.431  1.00 85.58  ? 482 GLU A CB  1 
ATOM   3849  C CG  . GLU A 1 482 ? 29.879  2.370   42.348  1.00 86.30  ? 482 GLU A CG  1 
ATOM   3850  C CD  . GLU A 1 482 ? 29.121  2.424   43.658  1.00 88.56  ? 482 GLU A CD  1 
ATOM   3851  O OE1 . GLU A 1 482 ? 29.303  1.440   44.397  1.00 90.35  ? 482 GLU A OE1 1 
ATOM   3852  O OE2 . GLU A 1 482 ? 28.376  3.406   43.942  1.00 88.62  ? 482 GLU A OE2 1 
ATOM   3853  N N   . ASN A 1 483 ? 31.831  2.723   39.424  1.00 83.30  ? 483 ASN A N   1 
ATOM   3854  C CA  . ASN A 1 483 ? 33.233  2.994   39.170  1.00 84.16  ? 483 ASN A CA  1 
ATOM   3855  C C   . ASN A 1 483 ? 33.582  4.298   39.887  1.00 85.25  ? 483 ASN A C   1 
ATOM   3856  O O   . ASN A 1 483 ? 32.748  5.199   39.911  1.00 85.99  ? 483 ASN A O   1 
ATOM   3857  C CB  . ASN A 1 483 ? 33.475  3.083   37.665  1.00 82.63  ? 483 ASN A CB  1 
ATOM   3858  C CG  . ASN A 1 483 ? 32.913  1.901   36.906  1.00 82.79  ? 483 ASN A CG  1 
ATOM   3859  O OD1 . ASN A 1 483 ? 33.680  1.127   36.329  1.00 82.36  ? 483 ASN A OD1 1 
ATOM   3860  N ND2 . ASN A 1 483 ? 31.596  1.747   36.869  1.00 83.44  ? 483 ASN A ND2 1 
ATOM   3861  N N   . PHE A 1 484 ? 34.791  4.407   40.462  1.00 86.46  ? 484 PHE A N   1 
ATOM   3862  C CA  . PHE A 1 484 ? 35.206  5.608   41.187  1.00 87.36  ? 484 PHE A CA  1 
ATOM   3863  C C   . PHE A 1 484 ? 36.258  6.397   40.401  1.00 86.52  ? 484 PHE A C   1 
ATOM   3864  O O   . PHE A 1 484 ? 36.913  5.852   39.521  1.00 86.52  ? 484 PHE A O   1 
ATOM   3865  C CB  . PHE A 1 484 ? 35.694  5.168   42.570  1.00 89.30  ? 484 PHE A CB  1 
ATOM   3866  C CG  . PHE A 1 484 ? 34.544  4.606   43.389  1.00 90.61  ? 484 PHE A CG  1 
ATOM   3867  C CD1 . PHE A 1 484 ? 33.657  5.459   44.041  1.00 90.97  ? 484 PHE A CD1 1 
ATOM   3868  C CD2 . PHE A 1 484 ? 34.315  3.233   43.452  1.00 91.11  ? 484 PHE A CD2 1 
ATOM   3869  C CE1 . PHE A 1 484 ? 32.591  4.946   44.769  1.00 92.37  ? 484 PHE A CE1 1 
ATOM   3870  C CE2 . PHE A 1 484 ? 33.244  2.724   44.177  1.00 92.27  ? 484 PHE A CE2 1 
ATOM   3871  C CZ  . PHE A 1 484 ? 32.392  3.579   44.844  1.00 93.12  ? 484 PHE A CZ  1 
ATOM   3872  N N   . PHE A 1 485 ? 36.422  7.688   40.710  1.00 86.24  ? 485 PHE A N   1 
ATOM   3873  C CA  . PHE A 1 485 ? 37.540  8.443   40.168  1.00 85.64  ? 485 PHE A CA  1 
ATOM   3874  C C   . PHE A 1 485 ? 37.951  9.535   41.140  1.00 87.71  ? 485 PHE A C   1 
ATOM   3875  O O   . PHE A 1 485 ? 37.088  10.184  41.724  1.00 91.36  ? 485 PHE A O   1 
ATOM   3876  C CB  . PHE A 1 485 ? 37.188  9.140   38.856  1.00 83.25  ? 485 PHE A CB  1 
ATOM   3877  C CG  . PHE A 1 485 ? 36.547  8.189   37.871  1.00 81.78  ? 485 PHE A CG  1 
ATOM   3878  C CD1 . PHE A 1 485 ? 35.194  7.889   37.942  1.00 81.94  ? 485 PHE A CD1 1 
ATOM   3879  C CD2 . PHE A 1 485 ? 37.323  7.551   36.920  1.00 81.08  ? 485 PHE A CD2 1 
ATOM   3880  C CE1 . PHE A 1 485 ? 34.630  6.989   37.050  1.00 81.16  ? 485 PHE A CE1 1 
ATOM   3881  C CE2 . PHE A 1 485 ? 36.758  6.654   36.031  1.00 80.15  ? 485 PHE A CE2 1 
ATOM   3882  C CZ  . PHE A 1 485 ? 35.414  6.378   36.098  1.00 80.11  ? 485 PHE A CZ  1 
ATOM   3883  N N   . ASN A 1 486 ? 39.264  9.769   41.255  1.00 87.53  ? 486 ASN A N   1 
ATOM   3884  C CA  . ASN A 1 486 ? 39.780  10.949  41.935  1.00 87.64  ? 486 ASN A CA  1 
ATOM   3885  C C   . ASN A 1 486 ? 39.409  12.173  41.098  1.00 85.70  ? 486 ASN A C   1 
ATOM   3886  O O   . ASN A 1 486 ? 39.619  12.145  39.884  1.00 84.58  ? 486 ASN A O   1 
ATOM   3887  C CB  . ASN A 1 486 ? 41.281  10.831  42.190  1.00 87.67  ? 486 ASN A CB  1 
ATOM   3888  C CG  . ASN A 1 486 ? 41.604  9.697   43.132  1.00 89.09  ? 486 ASN A CG  1 
ATOM   3889  O OD1 . ASN A 1 486 ? 42.159  8.675   42.715  1.00 89.24  ? 486 ASN A OD1 1 
ATOM   3890  N ND2 . ASN A 1 486 ? 41.239  9.828   44.397  1.00 90.45  ? 486 ASN A ND2 1 
ATOM   3891  N N   . ILE A 1 487 ? 38.820  13.201  41.739  1.00 85.54  ? 487 ILE A N   1 
ATOM   3892  C CA  . ILE A 1 487 ? 38.553  14.474  41.076  1.00 83.73  ? 487 ILE A CA  1 
ATOM   3893  C C   . ILE A 1 487 ? 39.778  15.358  41.238  1.00 83.49  ? 487 ILE A C   1 
ATOM   3894  O O   . ILE A 1 487 ? 40.221  15.603  42.353  1.00 86.12  ? 487 ILE A O   1 
ATOM   3895  C CB  . ILE A 1 487 ? 37.297  15.194  41.602  1.00 84.32  ? 487 ILE A CB  1 
ATOM   3896  C CG1 . ILE A 1 487 ? 36.057  14.307  41.536  1.00 84.91  ? 487 ILE A CG1 1 
ATOM   3897  C CG2 . ILE A 1 487 ? 37.065  16.485  40.824  1.00 83.12  ? 487 ILE A CG2 1 
ATOM   3898  C CD1 . ILE A 1 487 ? 34.775  14.977  41.996  1.00 85.39  ? 487 ILE A CD1 1 
ATOM   3899  N N   . PRO A 1 488 ? 40.375  15.843  40.133  1.00 81.07  ? 488 PRO A N   1 
ATOM   3900  C CA  . PRO A 1 488 ? 41.439  16.848  40.227  1.00 81.00  ? 488 PRO A CA  1 
ATOM   3901  C C   . PRO A 1 488 ? 40.955  18.160  40.839  1.00 81.08  ? 488 PRO A C   1 
ATOM   3902  O O   . PRO A 1 488 ? 39.866  18.615  40.539  1.00 80.41  ? 488 PRO A O   1 
ATOM   3903  C CB  . PRO A 1 488 ? 41.890  17.053  38.776  1.00 79.27  ? 488 PRO A CB  1 
ATOM   3904  C CG  . PRO A 1 488 ? 41.329  15.860  38.019  1.00 78.42  ? 488 PRO A CG  1 
ATOM   3905  C CD  . PRO A 1 488 ? 40.086  15.404  38.758  1.00 78.86  ? 488 PRO A CD  1 
ATOM   3906  N N   . ASP A 1 489 ? 41.792  18.804  41.651  1.00 82.35  ? 489 ASP A N   1 
ATOM   3907  C CA  . ASP A 1 489 ? 41.466  20.093  42.237  1.00 82.82  ? 489 ASP A CA  1 
ATOM   3908  C C   . ASP A 1 489 ? 41.285  21.173  41.176  1.00 81.26  ? 489 ASP A C   1 
ATOM   3909  O O   . ASP A 1 489 ? 40.514  22.110  41.388  1.00 81.44  ? 489 ASP A O   1 
ATOM   3910  C CB  . ASP A 1 489 ? 42.557  20.573  43.173  1.00 84.56  ? 489 ASP A CB  1 
ATOM   3911  C CG  . ASP A 1 489 ? 42.626  19.842  44.500  1.00 86.62  ? 489 ASP A CG  1 
ATOM   3912  O OD1 . ASP A 1 489 ? 41.684  19.086  44.797  1.00 86.74  ? 489 ASP A OD1 1 
ATOM   3913  O OD2 . ASP A 1 489 ? 43.626  20.036  45.210  1.00 88.40  ? 489 ASP A OD2 1 
ATOM   3914  N N   . ASN A 1 490 ? 42.015  21.043  40.064  1.00 80.03  ? 490 ASN A N   1 
ATOM   3915  C CA  . ASN A 1 490 ? 42.085  22.085  39.056  1.00 78.93  ? 490 ASN A CA  1 
ATOM   3916  C C   . ASN A 1 490 ? 41.241  21.715  37.837  1.00 76.88  ? 490 ASN A C   1 
ATOM   3917  O O   . ASN A 1 490 ? 41.434  22.302  36.765  1.00 75.22  ? 490 ASN A O   1 
ATOM   3918  C CB  . ASN A 1 490 ? 43.536  22.364  38.696  1.00 79.55  ? 490 ASN A CB  1 
ATOM   3919  C CG  . ASN A 1 490 ? 44.104  21.316  37.772  1.00 79.35  ? 490 ASN A CG  1 
ATOM   3920  O OD1 . ASN A 1 490 ? 44.310  20.152  38.156  1.00 79.91  ? 490 ASN A OD1 1 
ATOM   3921  N ND2 . ASN A 1 490 ? 44.351  21.726  36.535  1.00 78.53  ? 490 ASN A ND2 1 
ATOM   3922  N N   . CYS A 1 491 ? 40.335  20.736  38.036  1.00 77.08  ? 491 CYS A N   1 
ATOM   3923  C CA  . CYS A 1 491 ? 39.302  20.352  37.083  1.00 75.79  ? 491 CYS A CA  1 
ATOM   3924  C C   . CYS A 1 491 ? 38.117  21.294  37.235  1.00 75.86  ? 491 CYS A C   1 
ATOM   3925  O O   . CYS A 1 491 ? 37.510  21.355  38.302  1.00 76.90  ? 491 CYS A O   1 
ATOM   3926  C CB  . CYS A 1 491 ? 38.805  18.926  37.323  1.00 76.26  ? 491 CYS A CB  1 
ATOM   3927  S SG  . CYS A 1 491 ? 37.275  18.488  36.441  1.00 75.22  ? 491 CYS A SG  1 
ATOM   3928  N N   . TRP A 1 492 ? 37.819  22.036  36.167  1.00 74.92  ? 492 TRP A N   1 
ATOM   3929  C CA  . TRP A 1 492 ? 36.787  23.058  36.215  1.00 75.26  ? 492 TRP A CA  1 
ATOM   3930  C C   . TRP A 1 492 ? 35.456  22.477  35.733  1.00 74.63  ? 492 TRP A C   1 
ATOM   3931  O O   . TRP A 1 492 ? 34.412  22.822  36.280  1.00 74.55  ? 492 TRP A O   1 
ATOM   3932  C CB  . TRP A 1 492 ? 37.206  24.283  35.386  1.00 74.52  ? 492 TRP A CB  1 
ATOM   3933  C CG  . TRP A 1 492 ? 38.583  24.797  35.704  1.00 75.21  ? 492 TRP A CG  1 
ATOM   3934  C CD1 . TRP A 1 492 ? 39.591  25.049  34.820  1.00 74.68  ? 492 TRP A CD1 1 
ATOM   3935  C CD2 . TRP A 1 492 ? 39.105  25.133  37.005  1.00 76.90  ? 492 TRP A CD2 1 
ATOM   3936  N NE1 . TRP A 1 492 ? 40.708  25.499  35.476  1.00 75.62  ? 492 TRP A NE1 1 
ATOM   3937  C CE2 . TRP A 1 492 ? 40.440  25.563  36.815  1.00 76.84  ? 492 TRP A CE2 1 
ATOM   3938  C CE3 . TRP A 1 492 ? 38.579  25.115  38.301  1.00 78.33  ? 492 TRP A CE3 1 
ATOM   3939  C CZ2 . TRP A 1 492 ? 41.251  25.962  37.870  1.00 78.10  ? 492 TRP A CZ2 1 
ATOM   3940  C CZ3 . TRP A 1 492 ? 39.387  25.516  39.344  1.00 79.95  ? 492 TRP A CZ3 1 
ATOM   3941  C CH2 . TRP A 1 492 ? 40.705  25.925  39.130  1.00 79.71  ? 492 TRP A CH2 1 
ATOM   3942  N N   . VAL A 1 493 ? 35.507  21.587  34.724  1.00 73.91  ? 493 VAL A N   1 
ATOM   3943  C CA  . VAL A 1 493 ? 34.318  20.928  34.193  1.00 73.43  ? 493 VAL A CA  1 
ATOM   3944  C C   . VAL A 1 493 ? 34.672  19.486  33.847  1.00 72.46  ? 493 VAL A C   1 
ATOM   3945  O O   . VAL A 1 493 ? 35.832  19.221  33.554  1.00 73.10  ? 493 VAL A O   1 
ATOM   3946  C CB  . VAL A 1 493 ? 33.761  21.653  32.955  1.00 72.47  ? 493 VAL A CB  1 
ATOM   3947  C CG1 . VAL A 1 493 ? 34.823  21.870  31.885  1.00 71.47  ? 493 VAL A CG1 1 
ATOM   3948  C CG2 . VAL A 1 493 ? 32.579  20.891  32.365  1.00 72.18  ? 493 VAL A CG2 1 
ATOM   3949  N N   . VAL A 1 494 ? 33.683  18.577  33.866  1.00 71.43  ? 494 VAL A N   1 
ATOM   3950  C CA  . VAL A 1 494 ? 33.923  17.173  33.560  1.00 70.51  ? 494 VAL A CA  1 
ATOM   3951  C C   . VAL A 1 494 ? 32.788  16.587  32.722  1.00 69.45  ? 494 VAL A C   1 
ATOM   3952  O O   . VAL A 1 494 ? 31.611  16.805  33.011  1.00 69.39  ? 494 VAL A O   1 
ATOM   3953  C CB  . VAL A 1 494 ? 34.118  16.342  34.844  1.00 72.11  ? 494 VAL A CB  1 
ATOM   3954  C CG1 . VAL A 1 494 ? 32.876  16.344  35.725  1.00 73.23  ? 494 VAL A CG1 1 
ATOM   3955  C CG2 . VAL A 1 494 ? 34.558  14.903  34.562  1.00 71.84  ? 494 VAL A CG2 1 
ATOM   3956  N N   . ASN A 1 495 ? 33.164  15.737  31.748  1.00 69.02  ? 495 ASN A N   1 
ATOM   3957  C CA  . ASN A 1 495 ? 32.214  15.007  30.909  1.00 68.07  ? 495 ASN A CA  1 
ATOM   3958  C C   . ASN A 1 495 ? 32.198  13.512  31.299  1.00 68.72  ? 495 ASN A C   1 
ATOM   3959  O O   . ASN A 1 495 ? 32.828  12.653  30.669  1.00 68.76  ? 495 ASN A O   1 
ATOM   3960  C CB  . ASN A 1 495 ? 32.431  15.356  29.434  1.00 66.05  ? 495 ASN A CB  1 
ATOM   3961  C CG  . ASN A 1 495 ? 31.498  14.615  28.507  1.00 64.97  ? 495 ASN A CG  1 
ATOM   3962  O OD1 . ASN A 1 495 ? 31.002  13.545  28.875  1.00 66.72  ? 495 ASN A OD1 1 
ATOM   3963  N ND2 . ASN A 1 495 ? 31.284  15.114  27.297  1.00 63.34  ? 495 ASN A ND2 1 
ATOM   3964  N N   . ALA A 1 496 ? 31.383  13.203  32.320  1.00 70.00  ? 496 ALA A N   1 
ATOM   3965  C CA  . ALA A 1 496 ? 31.080  11.844  32.743  1.00 70.87  ? 496 ALA A CA  1 
ATOM   3966  C C   . ALA A 1 496 ? 30.267  11.153  31.659  1.00 70.35  ? 496 ALA A C   1 
ATOM   3967  O O   . ALA A 1 496 ? 29.184  11.613  31.353  1.00 71.92  ? 496 ALA A O   1 
ATOM   3968  C CB  . ALA A 1 496 ? 30.307  11.881  34.045  1.00 72.02  ? 496 ALA A CB  1 
ATOM   3969  N N   . SER A 1 497 ? 30.798  10.098  31.046  1.00 69.91  ? 497 SER A N   1 
ATOM   3970  C CA  . SER A 1 497 ? 30.028  9.333   30.078  1.00 69.35  ? 497 SER A CA  1 
ATOM   3971  C C   . SER A 1 497 ? 30.334  7.841   30.221  1.00 70.43  ? 497 SER A C   1 
ATOM   3972  O O   . SER A 1 497 ? 31.358  7.458   30.790  1.00 71.14  ? 497 SER A O   1 
ATOM   3973  C CB  . SER A 1 497 ? 30.292  9.793   28.672  1.00 67.88  ? 497 SER A CB  1 
ATOM   3974  O OG  . SER A 1 497 ? 31.576  9.375   28.222  1.00 67.83  ? 497 SER A OG  1 
ATOM   3975  N N   . ALA A 1 498 ? 29.417  7.020   29.699  1.00 70.11  ? 498 ALA A N   1 
ATOM   3976  C CA  . ALA A 1 498 ? 29.586  5.585   29.617  1.00 70.93  ? 498 ALA A CA  1 
ATOM   3977  C C   . ALA A 1 498 ? 28.810  5.081   28.416  1.00 70.85  ? 498 ALA A C   1 
ATOM   3978  O O   . ALA A 1 498 ? 27.835  5.675   28.009  1.00 73.13  ? 498 ALA A O   1 
ATOM   3979  C CB  . ALA A 1 498 ? 29.104  4.910   30.876  1.00 72.59  ? 498 ALA A CB  1 
ATOM   3980  N N   . GLY A 1 499 ? 29.222  3.956   27.869  1.00 71.90  ? 499 GLY A N   1 
ATOM   3981  C CA  . GLY A 1 499 ? 28.566  3.425   26.692  1.00 71.19  ? 499 GLY A CA  1 
ATOM   3982  C C   . GLY A 1 499 ? 28.998  1.987   26.425  1.00 71.22  ? 499 GLY A C   1 
ATOM   3983  O O   . GLY A 1 499 ? 30.038  1.553   26.931  1.00 69.98  ? 499 GLY A O   1 
ATOM   3984  N N   . ILE A 1 500 ? 28.159  1.285   25.638  1.00 71.88  ? 500 ILE A N   1 
ATOM   3985  C CA  . ILE A 1 500 ? 28.384  -0.108  25.272  1.00 72.14  ? 500 ILE A CA  1 
ATOM   3986  C C   . ILE A 1 500 ? 27.837  -0.364  23.870  1.00 71.46  ? 500 ILE A C   1 
ATOM   3987  O O   . ILE A 1 500 ? 26.914  0.308   23.442  1.00 71.84  ? 500 ILE A O   1 
ATOM   3988  C CB  . ILE A 1 500 ? 27.776  -1.059  26.311  1.00 72.47  ? 500 ILE A CB  1 
ATOM   3989  C CG1 . ILE A 1 500 ? 28.333  -2.445  26.116  1.00 73.04  ? 500 ILE A CG1 1 
ATOM   3990  C CG2 . ILE A 1 500 ? 26.251  -1.028  26.271  1.00 72.26  ? 500 ILE A CG2 1 
ATOM   3991  C CD1 . ILE A 1 500 ? 27.934  -3.416  27.207  1.00 75.00  ? 500 ILE A CD1 1 
ATOM   3992  N N   . SER A 1 501 ? 28.465  -1.300  23.151  1.00 71.52  ? 501 SER A N   1 
ATOM   3993  C CA  . SER A 1 501 ? 28.105  -1.593  21.776  1.00 71.09  ? 501 SER A CA  1 
ATOM   3994  C C   . SER A 1 501 ? 26.904  -2.525  21.799  1.00 70.56  ? 501 SER A C   1 
ATOM   3995  O O   . SER A 1 501 ? 26.729  -3.242  22.775  1.00 71.36  ? 501 SER A O   1 
ATOM   3996  C CB  . SER A 1 501 ? 29.250  -2.233  21.039  1.00 72.39  ? 501 SER A CB  1 
ATOM   3997  O OG  . SER A 1 501 ? 30.454  -1.488  21.158  1.00 73.50  ? 501 SER A OG  1 
ATOM   3998  N N   . VAL A 1 502 ? 26.096  -2.506  20.735  1.00 69.41  ? 502 VAL A N   1 
ATOM   3999  C CA  . VAL A 1 502 ? 24.904  -3.331  20.672  1.00 70.11  ? 502 VAL A CA  1 
ATOM   4000  C C   . VAL A 1 502 ? 24.696  -3.803  19.237  1.00 69.48  ? 502 VAL A C   1 
ATOM   4001  O O   . VAL A 1 502 ? 24.875  -3.018  18.309  1.00 68.17  ? 502 VAL A O   1 
ATOM   4002  C CB  . VAL A 1 502 ? 23.666  -2.585  21.192  1.00 71.31  ? 502 VAL A CB  1 
ATOM   4003  C CG1 . VAL A 1 502 ? 22.437  -3.488  21.195  1.00 73.15  ? 502 VAL A CG1 1 
ATOM   4004  C CG2 . VAL A 1 502 ? 23.891  -2.024  22.584  1.00 72.27  ? 502 VAL A CG2 1 
ATOM   4005  N N   . ARG A 1 503 ? 24.289  -5.081  19.095  1.00 70.19  ? 503 ARG A N   1 
ATOM   4006  C CA  . ARG A 1 503 ? 24.105  -5.741  17.811  1.00 70.00  ? 503 ARG A CA  1 
ATOM   4007  C C   . ARG A 1 503 ? 22.659  -6.218  17.655  1.00 68.23  ? 503 ARG A C   1 
ATOM   4008  O O   . ARG A 1 503 ? 22.058  -6.746  18.589  1.00 68.32  ? 503 ARG A O   1 
ATOM   4009  C CB  . ARG A 1 503 ? 25.029  -6.958  17.640  1.00 73.14  ? 503 ARG A CB  1 
ATOM   4010  C CG  . ARG A 1 503 ? 25.008  -7.575  16.243  1.00 76.11  ? 503 ARG A CG  1 
ATOM   4011  C CD  . ARG A 1 503 ? 25.845  -8.846  16.001  1.00 80.76  ? 503 ARG A CD  1 
ATOM   4012  N NE  . ARG A 1 503 ? 27.300  -8.649  15.916  1.00 88.78  ? 503 ARG A NE  1 
ATOM   4013  C CZ  . ARG A 1 503 ? 27.966  -7.810  15.093  1.00 95.26  ? 503 ARG A CZ  1 
ATOM   4014  N NH1 . ARG A 1 503 ? 27.354  -7.220  14.072  1.00 93.35  ? 503 ARG A NH1 1 
ATOM   4015  N NH2 . ARG A 1 503 ? 29.263  -7.586  15.275  1.00 96.94  ? 503 ARG A NH2 1 
ATOM   4016  N N   . TYR A 1 504 ? 22.121  -5.972  16.457  1.00 65.49  ? 504 TYR A N   1 
ATOM   4017  C CA  . TYR A 1 504 ? 20.916  -6.597  15.960  1.00 64.74  ? 504 TYR A CA  1 
ATOM   4018  C C   . TYR A 1 504 ? 21.203  -6.963  14.507  1.00 63.71  ? 504 TYR A C   1 
ATOM   4019  O O   . TYR A 1 504 ? 21.277  -6.099  13.640  1.00 61.87  ? 504 TYR A O   1 
ATOM   4020  C CB  . TYR A 1 504 ? 19.657  -5.728  16.084  1.00 64.55  ? 504 TYR A CB  1 
ATOM   4021  C CG  . TYR A 1 504 ? 18.362  -6.452  15.715  1.00 65.16  ? 504 TYR A CG  1 
ATOM   4022  C CD1 . TYR A 1 504 ? 18.020  -6.674  14.385  1.00 64.39  ? 504 TYR A CD1 1 
ATOM   4023  C CD2 . TYR A 1 504 ? 17.488  -6.911  16.698  1.00 66.13  ? 504 TYR A CD2 1 
ATOM   4024  C CE1 . TYR A 1 504 ? 16.852  -7.326  14.046  1.00 65.32  ? 504 TYR A CE1 1 
ATOM   4025  C CE2 . TYR A 1 504 ? 16.316  -7.560  16.369  1.00 67.03  ? 504 TYR A CE2 1 
ATOM   4026  C CZ  . TYR A 1 504 ? 16.000  -7.771  15.038  1.00 66.81  ? 504 TYR A CZ  1 
ATOM   4027  O OH  . TYR A 1 504 ? 14.874  -8.462  14.670  1.00 68.58  ? 504 TYR A OH  1 
ATOM   4028  N N   . GLY A 1 505 ? 21.374  -8.262  14.262  1.00 64.66  ? 505 GLY A N   1 
ATOM   4029  C CA  . GLY A 1 505 ? 21.731  -8.761  12.947  1.00 64.66  ? 505 GLY A CA  1 
ATOM   4030  C C   . GLY A 1 505 ? 23.048  -8.148  12.480  1.00 64.30  ? 505 GLY A C   1 
ATOM   4031  O O   . GLY A 1 505 ? 24.064  -8.225  13.176  1.00 65.06  ? 505 GLY A O   1 
ATOM   4032  N N   . LYS A 1 506 ? 23.013  -7.486  11.318  1.00 63.74  ? 506 LYS A N   1 
ATOM   4033  C CA  . LYS A 1 506 ? 24.187  -6.807  10.803  1.00 62.59  ? 506 LYS A CA  1 
ATOM   4034  C C   . LYS A 1 506 ? 24.329  -5.413  11.383  1.00 61.36  ? 506 LYS A C   1 
ATOM   4035  O O   . LYS A 1 506 ? 25.248  -4.728  11.005  1.00 61.88  ? 506 LYS A O   1 
ATOM   4036  C CB  . LYS A 1 506 ? 24.158  -6.652  9.282   1.00 62.75  ? 506 LYS A CB  1 
ATOM   4037  C CG  . LYS A 1 506 ? 24.332  -7.990  8.561   1.00 64.38  ? 506 LYS A CG  1 
ATOM   4038  C CD  . LYS A 1 506 ? 24.449  -7.848  7.047   1.00 65.05  ? 506 LYS A CD  1 
ATOM   4039  C CE  . LYS A 1 506 ? 24.403  -9.161  6.350   1.00 66.89  ? 506 LYS A CE  1 
ATOM   4040  N NZ  . LYS A 1 506 ? 23.642  -9.072  5.095   1.00 68.10  ? 506 LYS A NZ  1 
ATOM   4041  N N   . PHE A 1 507 ? 23.449  -4.972  12.273  1.00 61.69  ? 507 PHE A N   1 
ATOM   4042  C CA  . PHE A 1 507 ? 23.401  -3.561  12.606  1.00 61.42  ? 507 PHE A CA  1 
ATOM   4043  C C   . PHE A 1 507 ? 23.960  -3.404  14.013  1.00 62.03  ? 507 PHE A C   1 
ATOM   4044  O O   . PHE A 1 507 ? 23.462  -4.027  14.954  1.00 62.25  ? 507 PHE A O   1 
ATOM   4045  C CB  . PHE A 1 507 ? 21.962  -3.059  12.442  1.00 61.77  ? 507 PHE A CB  1 
ATOM   4046  C CG  . PHE A 1 507 ? 21.695  -1.619  12.865  1.00 61.38  ? 507 PHE A CG  1 
ATOM   4047  C CD1 . PHE A 1 507 ? 21.555  -1.271  14.206  1.00 61.77  ? 507 PHE A CD1 1 
ATOM   4048  C CD2 . PHE A 1 507 ? 21.521  -0.628  11.906  1.00 60.96  ? 507 PHE A CD2 1 
ATOM   4049  C CE1 . PHE A 1 507 ? 21.310  0.041   14.576  1.00 61.70  ? 507 PHE A CE1 1 
ATOM   4050  C CE2 . PHE A 1 507 ? 21.253  0.672   12.276  1.00 61.03  ? 507 PHE A CE2 1 
ATOM   4051  C CZ  . PHE A 1 507 ? 21.152  1.005   13.613  1.00 61.53  ? 507 PHE A CZ  1 
ATOM   4052  N N   . THR A 1 508 ? 25.003  -2.572  14.135  1.00 61.91  ? 508 THR A N   1 
ATOM   4053  C CA  . THR A 1 508 ? 25.636  -2.367  15.424  1.00 63.43  ? 508 THR A CA  1 
ATOM   4054  C C   . THR A 1 508 ? 25.616  -0.879  15.693  1.00 63.11  ? 508 THR A C   1 
ATOM   4055  O O   . THR A 1 508 ? 25.735  -0.086  14.775  1.00 63.25  ? 508 THR A O   1 
ATOM   4056  C CB  . THR A 1 508 ? 27.069  -2.922  15.506  1.00 64.35  ? 508 THR A CB  1 
ATOM   4057  O OG1 . THR A 1 508 ? 27.779  -2.381  14.400  1.00 65.20  ? 508 THR A OG1 1 
ATOM   4058  C CG2 . THR A 1 508 ? 27.166  -4.436  15.432  1.00 65.17  ? 508 THR A CG2 1 
ATOM   4059  N N   . PHE A 1 509 ? 25.497  -0.527  16.966  1.00 63.94  ? 509 PHE A N   1 
ATOM   4060  C CA  . PHE A 1 509 ? 25.386  0.854   17.379  1.00 63.39  ? 509 PHE A CA  1 
ATOM   4061  C C   . PHE A 1 509 ? 25.663  0.883   18.868  1.00 63.85  ? 509 PHE A C   1 
ATOM   4062  O O   . PHE A 1 509 ? 25.395  -0.090  19.564  1.00 66.24  ? 509 PHE A O   1 
ATOM   4063  C CB  . PHE A 1 509 ? 23.969  1.341   17.052  1.00 64.14  ? 509 PHE A CB  1 
ATOM   4064  C CG  . PHE A 1 509 ? 22.842  0.703   17.859  1.00 65.61  ? 509 PHE A CG  1 
ATOM   4065  C CD1 . PHE A 1 509 ? 22.392  -0.579  17.576  1.00 66.87  ? 509 PHE A CD1 1 
ATOM   4066  C CD2 . PHE A 1 509 ? 22.208  1.400   18.886  1.00 66.72  ? 509 PHE A CD2 1 
ATOM   4067  C CE1 . PHE A 1 509 ? 21.354  -1.157  18.307  1.00 68.39  ? 509 PHE A CE1 1 
ATOM   4068  C CE2 . PHE A 1 509 ? 21.168  0.827   19.607  1.00 67.63  ? 509 PHE A CE2 1 
ATOM   4069  C CZ  . PHE A 1 509 ? 20.754  -0.454  19.327  1.00 68.55  ? 509 PHE A CZ  1 
ATOM   4070  N N   . LYS A 1 510 ? 26.122  2.014   19.363  1.00 63.15  ? 510 LYS A N   1 
ATOM   4071  C CA  . LYS A 1 510 ? 26.404  2.134   20.776  1.00 64.20  ? 510 LYS A CA  1 
ATOM   4072  C C   . LYS A 1 510 ? 25.214  2.787   21.472  1.00 63.92  ? 510 LYS A C   1 
ATOM   4073  O O   . LYS A 1 510 ? 24.458  3.530   20.852  1.00 63.60  ? 510 LYS A O   1 
ATOM   4074  C CB  . LYS A 1 510 ? 27.724  2.907   20.864  1.00 65.29  ? 510 LYS A CB  1 
ATOM   4075  C CG  . LYS A 1 510 ? 28.886  2.278   20.084  1.00 65.10  ? 510 LYS A CG  1 
ATOM   4076  C CD  . LYS A 1 510 ? 30.254  2.936   20.247  1.00 65.15  ? 510 LYS A CD  1 
ATOM   4077  C CE  . LYS A 1 510 ? 30.775  2.945   21.659  1.00 66.09  ? 510 LYS A CE  1 
ATOM   4078  N NZ  . LYS A 1 510 ? 30.815  1.633   22.306  1.00 66.81  ? 510 LYS A NZ  1 
ATOM   4079  N N   . ILE A 1 511 ? 25.040  2.439   22.749  1.00 64.54  ? 511 ILE A N   1 
ATOM   4080  C CA  . ILE A 1 511 ? 24.089  3.083   23.639  1.00 65.31  ? 511 ILE A CA  1 
ATOM   4081  C C   . ILE A 1 511 ? 24.893  3.659   24.791  1.00 65.49  ? 511 ILE A C   1 
ATOM   4082  O O   . ILE A 1 511 ? 25.861  3.044   25.228  1.00 66.56  ? 511 ILE A O   1 
ATOM   4083  C CB  . ILE A 1 511 ? 22.966  2.140   24.133  1.00 66.15  ? 511 ILE A CB  1 
ATOM   4084  C CG1 . ILE A 1 511 ? 23.496  0.908   24.928  1.00 67.34  ? 511 ILE A CG1 1 
ATOM   4085  C CG2 . ILE A 1 511 ? 22.081  1.739   22.951  1.00 65.48  ? 511 ILE A CG2 1 
ATOM   4086  C CD1 . ILE A 1 511 ? 22.440  0.022   25.611  1.00 68.54  ? 511 ILE A CD1 1 
ATOM   4087  N N   . HIS A 1 512 ? 24.474  4.835   25.269  1.00 64.94  ? 512 HIS A N   1 
ATOM   4088  C CA  . HIS A 1 512 ? 25.336  5.654   26.098  1.00 63.90  ? 512 HIS A CA  1 
ATOM   4089  C C   . HIS A 1 512 ? 24.536  6.708   26.841  1.00 64.10  ? 512 HIS A C   1 
ATOM   4090  O O   . HIS A 1 512 ? 23.366  6.948   26.535  1.00 63.56  ? 512 HIS A O   1 
ATOM   4091  C CB  . HIS A 1 512 ? 26.355  6.324   25.189  1.00 62.12  ? 512 HIS A CB  1 
ATOM   4092  C CG  . HIS A 1 512 ? 25.718  6.788   23.939  1.00 60.66  ? 512 HIS A CG  1 
ATOM   4093  N ND1 . HIS A 1 512 ? 24.933  7.915   23.902  1.00 60.29  ? 512 HIS A ND1 1 
ATOM   4094  C CD2 . HIS A 1 512 ? 25.722  6.279   22.708  1.00 59.58  ? 512 HIS A CD2 1 
ATOM   4095  C CE1 . HIS A 1 512 ? 24.510  8.089   22.663  1.00 59.43  ? 512 HIS A CE1 1 
ATOM   4096  N NE2 . HIS A 1 512 ? 24.968  7.103   21.926  1.00 58.74  ? 512 HIS A NE2 1 
ATOM   4097  N N   . ASP A 1 513 ? 25.212  7.304   27.829  1.00 64.98  ? 513 ASP A N   1 
ATOM   4098  C CA  . ASP A 1 513 ? 24.722  8.496   28.507  1.00 65.99  ? 513 ASP A CA  1 
ATOM   4099  C C   . ASP A 1 513 ? 25.915  9.405   28.805  1.00 65.71  ? 513 ASP A C   1 
ATOM   4100  O O   . ASP A 1 513 ? 27.046  8.936   28.750  1.00 65.04  ? 513 ASP A O   1 
ATOM   4101  C CB  . ASP A 1 513 ? 23.861  8.127   29.711  1.00 67.57  ? 513 ASP A CB  1 
ATOM   4102  C CG  . ASP A 1 513 ? 22.976  9.225   30.281  1.00 68.10  ? 513 ASP A CG  1 
ATOM   4103  O OD1 . ASP A 1 513 ? 22.818  10.272  29.603  1.00 67.06  ? 513 ASP A OD1 1 
ATOM   4104  O OD2 . ASP A 1 513 ? 22.485  9.040   31.414  1.00 69.44  ? 513 ASP A OD2 1 
ATOM   4105  N N   . GLN A 1 514 ? 25.612  10.678  29.138  1.00 66.33  ? 514 GLN A N   1 
ATOM   4106  C CA  . GLN A 1 514 ? 26.562  11.768  29.295  1.00 66.53  ? 514 GLN A CA  1 
ATOM   4107  C C   . GLN A 1 514 ? 26.064  12.788  30.319  1.00 68.14  ? 514 GLN A C   1 
ATOM   4108  O O   . GLN A 1 514 ? 24.983  13.327  30.156  1.00 69.47  ? 514 GLN A O   1 
ATOM   4109  C CB  . GLN A 1 514 ? 26.625  12.475  27.941  1.00 65.46  ? 514 GLN A CB  1 
ATOM   4110  C CG  . GLN A 1 514 ? 27.693  13.557  27.811  1.00 65.46  ? 514 GLN A CG  1 
ATOM   4111  C CD  . GLN A 1 514 ? 27.574  14.290  26.493  1.00 64.82  ? 514 GLN A CD  1 
ATOM   4112  O OE1 . GLN A 1 514 ? 28.345  14.101  25.551  1.00 64.27  ? 514 GLN A OE1 1 
ATOM   4113  N NE2 . GLN A 1 514 ? 26.547  15.111  26.396  1.00 65.66  ? 514 GLN A NE2 1 
ATOM   4114  N N   . LYS A 1 515 ? 26.854  13.118  31.344  1.00 69.11  ? 515 LYS A N   1 
ATOM   4115  C CA  . LYS A 1 515 ? 26.546  14.265  32.184  1.00 70.01  ? 515 LYS A CA  1 
ATOM   4116  C C   . LYS A 1 515 ? 27.756  15.190  32.187  1.00 70.43  ? 515 LYS A C   1 
ATOM   4117  O O   . LYS A 1 515 ? 28.873  14.738  32.448  1.00 71.28  ? 515 LYS A O   1 
ATOM   4118  C CB  . LYS A 1 515 ? 26.229  13.951  33.648  1.00 71.77  ? 515 LYS A CB  1 
ATOM   4119  C CG  . LYS A 1 515 ? 25.194  12.871  33.853  1.00 72.90  ? 515 LYS A CG  1 
ATOM   4120  C CD  . LYS A 1 515 ? 23.844  13.156  33.214  1.00 72.63  ? 515 LYS A CD  1 
ATOM   4121  C CE  . LYS A 1 515 ? 22.837  12.071  33.405  1.00 73.32  ? 515 LYS A CE  1 
ATOM   4122  N NZ  . LYS A 1 515 ? 21.617  12.527  32.739  1.00 73.15  ? 515 LYS A NZ  1 
ATOM   4123  N N   . ILE A 1 516 ? 27.515  16.476  31.881  1.00 69.85  ? 516 ILE A N   1 
ATOM   4124  C CA  . ILE A 1 516 ? 28.535  17.505  31.931  1.00 68.98  ? 516 ILE A CA  1 
ATOM   4125  C C   . ILE A 1 516 ? 28.368  18.248  33.248  1.00 70.60  ? 516 ILE A C   1 
ATOM   4126  O O   . ILE A 1 516 ? 27.340  18.879  33.447  1.00 71.32  ? 516 ILE A O   1 
ATOM   4127  C CB  . ILE A 1 516 ? 28.382  18.448  30.729  1.00 67.22  ? 516 ILE A CB  1 
ATOM   4128  C CG1 . ILE A 1 516 ? 28.771  17.745  29.443  1.00 65.44  ? 516 ILE A CG1 1 
ATOM   4129  C CG2 . ILE A 1 516 ? 29.185  19.730  30.944  1.00 67.65  ? 516 ILE A CG2 1 
ATOM   4130  C CD1 . ILE A 1 516 ? 28.712  18.625  28.209  1.00 64.14  ? 516 ILE A CD1 1 
ATOM   4131  N N   . ILE A 1 517 ? 29.370  18.191  34.128  1.00 71.58  ? 517 ILE A N   1 
ATOM   4132  C CA  . ILE A 1 517 ? 29.219  18.758  35.454  1.00 73.68  ? 517 ILE A CA  1 
ATOM   4133  C C   . ILE A 1 517 ? 30.335  19.763  35.719  1.00 75.11  ? 517 ILE A C   1 
ATOM   4134  O O   . ILE A 1 517 ? 31.462  19.559  35.276  1.00 75.22  ? 517 ILE A O   1 
ATOM   4135  C CB  . ILE A 1 517 ? 29.157  17.635  36.490  1.00 74.75  ? 517 ILE A CB  1 
ATOM   4136  C CG1 . ILE A 1 517 ? 28.038  16.666  36.144  1.00 75.24  ? 517 ILE A CG1 1 
ATOM   4137  C CG2 . ILE A 1 517 ? 28.981  18.202  37.890  1.00 76.49  ? 517 ILE A CG2 1 
ATOM   4138  C CD1 . ILE A 1 517 ? 28.041  15.361  36.936  1.00 76.78  ? 517 ILE A CD1 1 
ATOM   4139  N N   . TYR A 1 518 ? 29.994  20.852  36.439  1.00 77.64  ? 518 TYR A N   1 
ATOM   4140  C CA  . TYR A 1 518 ? 30.878  22.001  36.658  1.00 78.66  ? 518 TYR A CA  1 
ATOM   4141  C C   . TYR A 1 518 ? 31.334  22.096  38.118  1.00 81.60  ? 518 TYR A C   1 
ATOM   4142  O O   . TYR A 1 518 ? 30.773  21.473  39.013  1.00 85.22  ? 518 TYR A O   1 
ATOM   4143  C CB  . TYR A 1 518 ? 30.172  23.308  36.290  1.00 77.76  ? 518 TYR A CB  1 
ATOM   4144  C CG  . TYR A 1 518 ? 29.792  23.437  34.823  1.00 75.95  ? 518 TYR A CG  1 
ATOM   4145  C CD1 . TYR A 1 518 ? 30.676  23.964  33.901  1.00 75.37  ? 518 TYR A CD1 1 
ATOM   4146  C CD2 . TYR A 1 518 ? 28.552  23.038  34.357  1.00 75.45  ? 518 TYR A CD2 1 
ATOM   4147  C CE1 . TYR A 1 518 ? 30.341  24.090  32.563  1.00 74.03  ? 518 TYR A CE1 1 
ATOM   4148  C CE2 . TYR A 1 518 ? 28.201  23.164  33.024  1.00 74.08  ? 518 TYR A CE2 1 
ATOM   4149  C CZ  . TYR A 1 518 ? 29.099  23.691  32.120  1.00 73.08  ? 518 TYR A CZ  1 
ATOM   4150  O OH  . TYR A 1 518 ? 28.795  23.853  30.800  1.00 72.07  ? 518 TYR A OH  1 
ATOM   4151  N N   . ARG A 1 519 ? 32.381  22.883  38.353  1.00 81.95  ? 519 ARG A N   1 
ATOM   4152  C CA  . ARG A 1 519 ? 32.833  23.182  39.698  1.00 83.89  ? 519 ARG A CA  1 
ATOM   4153  C C   . ARG A 1 519 ? 32.422  24.616  40.018  1.00 85.03  ? 519 ARG A C   1 
ATOM   4154  O O   . ARG A 1 519 ? 32.765  25.536  39.276  1.00 84.77  ? 519 ARG A O   1 
ATOM   4155  C CB  . ARG A 1 519 ? 34.353  23.006  39.769  1.00 83.88  ? 519 ARG A CB  1 
ATOM   4156  C CG  . ARG A 1 519 ? 34.887  23.181  41.183  1.00 86.30  ? 519 ARG A CG  1 
ATOM   4157  C CD  . ARG A 1 519 ? 36.396  23.310  41.207  1.00 86.65  ? 519 ARG A CD  1 
ATOM   4158  N NE  . ARG A 1 519 ? 37.077  22.027  41.056  1.00 86.58  ? 519 ARG A NE  1 
ATOM   4159  C CZ  . ARG A 1 519 ? 37.046  21.102  41.997  1.00 89.15  ? 519 ARG A CZ  1 
ATOM   4160  N NH1 . ARG A 1 519 ? 36.370  21.336  43.111  1.00 91.20  ? 519 ARG A NH1 1 
ATOM   4161  N NH2 . ARG A 1 519 ? 37.674  19.946  41.826  1.00 89.12  ? 519 ARG A NH2 1 
ATOM   4162  N N   . GLY A 1 520 ? 31.668  24.807  41.109  1.00 86.75  ? 520 GLY A N   1 
ATOM   4163  C CA  . GLY A 1 520 ? 31.123  26.117  41.436  1.00 86.96  ? 520 GLY A CA  1 
ATOM   4164  C C   . GLY A 1 520 ? 30.472  26.764  40.213  1.00 85.16  ? 520 GLY A C   1 
ATOM   4165  O O   . GLY A 1 520 ? 29.992  26.072  39.314  1.00 83.22  ? 520 GLY A O   1 
ATOM   4166  N N   . ASP A 1 521 ? 30.482  28.100  40.167  1.00 85.51  ? 521 ASP A N   1 
ATOM   4167  C CA  . ASP A 1 521 ? 29.623  28.807  39.224  1.00 84.54  ? 521 ASP A CA  1 
ATOM   4168  C C   . ASP A 1 521 ? 30.440  29.487  38.125  1.00 82.20  ? 521 ASP A C   1 
ATOM   4169  O O   . ASP A 1 521 ? 29.890  30.301  37.390  1.00 80.27  ? 521 ASP A O   1 
ATOM   4170  C CB  . ASP A 1 521 ? 28.700  29.776  39.940  1.00 86.14  ? 521 ASP A CB  1 
ATOM   4171  C CG  . ASP A 1 521 ? 29.413  30.913  40.649  1.00 88.50  ? 521 ASP A CG  1 
ATOM   4172  O OD1 . ASP A 1 521 ? 30.671  30.987  40.548  1.00 88.47  ? 521 ASP A OD1 1 
ATOM   4173  O OD2 . ASP A 1 521 ? 28.701  31.715  41.291  1.00 91.08  ? 521 ASP A OD2 1 
ATOM   4174  N N   . TRP A 1 522 ? 31.710  29.073  37.958  1.00 81.56  ? 522 TRP A N   1 
ATOM   4175  C CA  . TRP A 1 522 ? 32.646  29.707  37.033  1.00 79.33  ? 522 TRP A CA  1 
ATOM   4176  C C   . TRP A 1 522 ? 32.108  29.735  35.596  1.00 78.14  ? 522 TRP A C   1 
ATOM   4177  O O   . TRP A 1 522 ? 32.474  30.636  34.839  1.00 77.97  ? 522 TRP A O   1 
ATOM   4178  C CB  . TRP A 1 522 ? 34.008  28.998  37.090  1.00 77.83  ? 522 TRP A CB  1 
ATOM   4179  C CG  . TRP A 1 522 ? 34.062  27.779  36.217  1.00 75.85  ? 522 TRP A CG  1 
ATOM   4180  C CD1 . TRP A 1 522 ? 33.721  26.511  36.589  1.00 75.38  ? 522 TRP A CD1 1 
ATOM   4181  C CD2 . TRP A 1 522 ? 34.391  27.712  34.809  1.00 73.52  ? 522 TRP A CD2 1 
ATOM   4182  N NE1 . TRP A 1 522 ? 33.844  25.659  35.528  1.00 73.35  ? 522 TRP A NE1 1 
ATOM   4183  C CE2 . TRP A 1 522 ? 34.243  26.357  34.422  1.00 72.13  ? 522 TRP A CE2 1 
ATOM   4184  C CE3 . TRP A 1 522 ? 34.799  28.643  33.846  1.00 72.07  ? 522 TRP A CE3 1 
ATOM   4185  C CZ2 . TRP A 1 522 ? 34.482  25.919  33.124  1.00 70.11  ? 522 TRP A CZ2 1 
ATOM   4186  C CZ3 . TRP A 1 522 ? 35.024  28.208  32.557  1.00 70.50  ? 522 TRP A CZ3 1 
ATOM   4187  C CH2 . TRP A 1 522 ? 34.839  26.866  32.196  1.00 69.60  ? 522 TRP A CH2 1 
ATOM   4188  N N   . ALA A 1 523 ? 31.223  28.775  35.245  1.00 77.48  ? 523 ALA A N   1 
ATOM   4189  C CA  . ALA A 1 523 ? 30.687  28.609  33.898  1.00 75.31  ? 523 ALA A CA  1 
ATOM   4190  C C   . ALA A 1 523 ? 29.384  29.380  33.688  1.00 75.31  ? 523 ALA A C   1 
ATOM   4191  O O   . ALA A 1 523 ? 28.788  29.270  32.617  1.00 73.62  ? 523 ALA A O   1 
ATOM   4192  C CB  . ALA A 1 523 ? 30.476  27.144  33.625  1.00 74.45  ? 523 ALA A CB  1 
ATOM   4193  N N   . LYS A 1 524 ? 28.986  30.195  34.678  1.00 77.09  ? 524 LYS A N   1 
ATOM   4194  C CA  . LYS A 1 524 ? 27.695  30.878  34.693  1.00 78.40  ? 524 LYS A CA  1 
ATOM   4195  C C   . LYS A 1 524 ? 27.371  31.515  33.349  1.00 76.17  ? 524 LYS A C   1 
ATOM   4196  O O   . LYS A 1 524 ? 26.232  31.468  32.926  1.00 75.64  ? 524 LYS A O   1 
ATOM   4197  C CB  . LYS A 1 524 ? 27.638  31.997  35.736  1.00 81.35  ? 524 LYS A CB  1 
ATOM   4198  C CG  . LYS A 1 524 ? 26.280  32.642  35.924  1.00 84.43  ? 524 LYS A CG  1 
ATOM   4199  C CD  . LYS A 1 524 ? 26.301  33.936  36.746  1.00 87.55  ? 524 LYS A CD  1 
ATOM   4200  C CE  . LYS A 1 524 ? 26.670  33.708  38.185  1.00 89.52  ? 524 LYS A CE  1 
ATOM   4201  N NZ  . LYS A 1 524 ? 26.859  34.981  38.878  1.00 90.95  ? 524 LYS A NZ  1 
ATOM   4202  N N   . GLU A 1 525 ? 28.367  32.114  32.703  1.00 75.78  ? 525 GLU A N   1 
ATOM   4203  C CA  . GLU A 1 525 ? 28.153  32.870  31.482  1.00 75.78  ? 525 GLU A CA  1 
ATOM   4204  C C   . GLU A 1 525 ? 28.424  31.997  30.261  1.00 74.22  ? 525 GLU A C   1 
ATOM   4205  O O   . GLU A 1 525 ? 27.615  31.914  29.347  1.00 73.59  ? 525 GLU A O   1 
ATOM   4206  C CB  . GLU A 1 525 ? 29.063  34.101  31.426  1.00 76.69  ? 525 GLU A CB  1 
ATOM   4207  C CG  . GLU A 1 525 ? 28.825  35.112  32.545  1.00 79.15  ? 525 GLU A CG  1 
ATOM   4208  C CD  . GLU A 1 525 ? 29.651  35.044  33.824  1.00 81.20  ? 525 GLU A CD  1 
ATOM   4209  O OE1 . GLU A 1 525 ? 30.715  34.392  33.887  1.00 80.76  ? 525 GLU A OE1 1 
ATOM   4210  O OE2 . GLU A 1 525 ? 29.203  35.708  34.789  1.00 84.44  ? 525 GLU A OE2 1 
ATOM   4211  N N   . VAL A 1 526 ? 29.604  31.391  30.229  1.00 74.24  ? 526 VAL A N   1 
ATOM   4212  C CA  . VAL A 1 526 ? 30.080  30.698  29.042  1.00 73.38  ? 526 VAL A CA  1 
ATOM   4213  C C   . VAL A 1 526 ? 29.335  29.375  28.847  1.00 73.78  ? 526 VAL A C   1 
ATOM   4214  O O   . VAL A 1 526 ? 29.182  28.908  27.718  1.00 74.28  ? 526 VAL A O   1 
ATOM   4215  C CB  . VAL A 1 526 ? 31.603  30.480  29.156  1.00 72.21  ? 526 VAL A CB  1 
ATOM   4216  C CG1 . VAL A 1 526 ? 31.976  29.596  30.337  1.00 72.74  ? 526 VAL A CG1 1 
ATOM   4217  C CG2 . VAL A 1 526 ? 32.184  29.922  27.869  1.00 70.59  ? 526 VAL A CG2 1 
ATOM   4218  N N   . GLY A 1 527 ? 28.887  28.752  29.941  1.00 74.41  ? 527 GLY A N   1 
ATOM   4219  C CA  . GLY A 1 527 ? 28.272  27.438  29.843  1.00 74.53  ? 527 GLY A CA  1 
ATOM   4220  C C   . GLY A 1 527 ? 26.906  27.487  29.159  1.00 73.61  ? 527 GLY A C   1 
ATOM   4221  O O   . GLY A 1 527 ? 26.161  28.432  29.361  1.00 74.44  ? 527 GLY A O   1 
ATOM   4222  N N   . ARG A 1 528 ? 26.603  26.453  28.362  1.00 73.31  ? 528 ARG A N   1 
ATOM   4223  C CA  . ARG A 1 528 ? 25.299  26.231  27.749  1.00 73.93  ? 528 ARG A CA  1 
ATOM   4224  C C   . ARG A 1 528 ? 24.195  26.229  28.806  1.00 78.17  ? 528 ARG A C   1 
ATOM   4225  O O   . ARG A 1 528 ? 24.383  25.610  29.848  1.00 79.03  ? 528 ARG A O   1 
ATOM   4226  C CB  . ARG A 1 528 ? 25.310  24.861  27.070  1.00 71.63  ? 528 ARG A CB  1 
ATOM   4227  C CG  . ARG A 1 528 ? 24.047  24.516  26.296  1.00 70.66  ? 528 ARG A CG  1 
ATOM   4228  C CD  . ARG A 1 528 ? 23.976  23.040  25.869  1.00 69.15  ? 528 ARG A CD  1 
ATOM   4229  N NE  . ARG A 1 528 ? 24.919  22.718  24.794  1.00 66.41  ? 528 ARG A NE  1 
ATOM   4230  C CZ  . ARG A 1 528 ? 26.067  22.117  24.995  1.00 65.29  ? 528 ARG A CZ  1 
ATOM   4231  N NH1 . ARG A 1 528 ? 26.303  21.558  26.164  1.00 65.98  ? 528 ARG A NH1 1 
ATOM   4232  N NH2 . ARG A 1 528 ? 26.966  22.064  24.026  1.00 63.86  ? 528 ARG A NH2 1 
ATOM   4233  N N   . LYS A 1 529 ? 23.053  26.891  28.519  1.00 81.98  ? 529 LYS A N   1 
ATOM   4234  C CA  . LYS A 1 529 ? 21.916  26.935  29.439  1.00 86.59  ? 529 LYS A CA  1 
ATOM   4235  C C   . LYS A 1 529 ? 20.885  25.835  29.137  1.00 89.27  ? 529 LYS A C   1 
ATOM   4236  O O   . LYS A 1 529 ? 21.066  25.041  28.215  1.00 88.29  ? 529 LYS A O   1 
ATOM   4237  C CB  . LYS A 1 529 ? 21.284  28.328  29.382  1.00 88.58  ? 529 LYS A CB  1 
ATOM   4238  C CG  . LYS A 1 529 ? 22.150  29.440  29.947  1.00 91.24  ? 529 LYS A CG  1 
ATOM   4239  C CD  . LYS A 1 529 ? 22.946  30.218  28.905  1.00 92.77  ? 529 LYS A CD  1 
ATOM   4240  C CE  . LYS A 1 529 ? 23.819  31.320  29.464  1.00 93.37  ? 529 LYS A CE  1 
ATOM   4241  N NZ  . LYS A 1 529 ? 25.027  30.789  30.106  1.00 92.57  ? 529 LYS A NZ  1 
ATOM   4242  N N   . LEU A 1 530 ? 19.810  25.779  29.946  1.00 94.41  ? 530 LEU A N   1 
ATOM   4243  C CA  . LEU A 1 530 ? 18.659  24.902  29.732  1.00 98.57  ? 530 LEU A CA  1 
ATOM   4244  C C   . LEU A 1 530 ? 19.063  23.442  30.007  1.00 103.58 ? 530 LEU A C   1 
ATOM   4245  O O   . LEU A 1 530 ? 18.182  22.557  29.816  1.00 103.79 ? 530 LEU A O   1 
ATOM   4246  C CB  . LEU A 1 530 ? 18.041  25.009  28.335  1.00 99.16  ? 530 LEU A CB  1 
ATOM   4247  C CG  . LEU A 1 530 ? 17.120  26.203  28.052  1.00 102.52 ? 530 LEU A CG  1 
ATOM   4248  C CD1 . LEU A 1 530 ? 17.372  26.628  26.601  1.00 102.43 ? 530 LEU A CD1 1 
ATOM   4249  C CD2 . LEU A 1 530 ? 15.608  25.942  28.301  1.00 101.12 ? 530 LEU A CD2 1 
ATOM   4250  N N   . SER B 1 3   ? 17.603  51.486  -29.321 1.00 147.93 ? 3   SER B N   1 
ATOM   4251  C CA  . SER B 1 3   ? 19.065  51.747  -29.390 1.00 147.64 ? 3   SER B CA  1 
ATOM   4252  C C   . SER B 1 3   ? 19.764  50.666  -30.220 1.00 145.26 ? 3   SER B C   1 
ATOM   4253  O O   . SER B 1 3   ? 20.602  49.934  -29.698 1.00 144.73 ? 3   SER B O   1 
ATOM   4254  C CB  . SER B 1 3   ? 19.653  51.872  -27.993 1.00 149.41 ? 3   SER B CB  1 
ATOM   4255  O OG  . SER B 1 3   ? 21.076  51.907  -27.995 1.00 146.81 ? 3   SER B OG  1 
ATOM   4256  N N   . LYS B 1 4   ? 19.421  50.574  -31.515 1.00 144.54 ? 4   LYS B N   1 
ATOM   4257  C CA  . LYS B 1 4   ? 20.177  49.749  -32.448 1.00 140.16 ? 4   LYS B CA  1 
ATOM   4258  C C   . LYS B 1 4   ? 21.530  50.424  -32.671 1.00 135.91 ? 4   LYS B C   1 
ATOM   4259  O O   . LYS B 1 4   ? 21.603  51.657  -32.676 1.00 133.50 ? 4   LYS B O   1 
ATOM   4260  C CB  . LYS B 1 4   ? 19.452  49.502  -33.782 1.00 142.47 ? 4   LYS B CB  1 
ATOM   4261  C CG  . LYS B 1 4   ? 19.167  50.715  -34.680 1.00 146.83 ? 4   LYS B CG  1 
ATOM   4262  C CD  . LYS B 1 4   ? 19.557  50.534  -36.147 1.00 146.93 ? 4   LYS B CD  1 
ATOM   4263  C CE  . LYS B 1 4   ? 18.855  49.419  -36.872 1.00 147.38 ? 4   LYS B CE  1 
ATOM   4264  N NZ  . LYS B 1 4   ? 19.572  48.988  -38.082 1.00 144.62 ? 4   LYS B NZ  1 
ATOM   4265  N N   . THR B 1 5   ? 22.597  49.614  -32.816 1.00 130.97 ? 5   THR B N   1 
ATOM   4266  C CA  . THR B 1 5   ? 23.911  50.153  -33.134 1.00 127.23 ? 5   THR B CA  1 
ATOM   4267  C C   . THR B 1 5   ? 23.836  50.766  -34.534 1.00 123.60 ? 5   THR B C   1 
ATOM   4268  O O   . THR B 1 5   ? 23.365  50.123  -35.472 1.00 120.05 ? 5   THR B O   1 
ATOM   4269  C CB  . THR B 1 5   ? 24.997  49.085  -33.006 1.00 127.49 ? 5   THR B CB  1 
ATOM   4270  O OG1 . THR B 1 5   ? 24.632  47.966  -33.807 1.00 128.43 ? 5   THR B OG1 1 
ATOM   4271  C CG2 . THR B 1 5   ? 25.191  48.614  -31.575 1.00 129.24 ? 5   THR B CG2 1 
ATOM   4272  N N   . LYS B 1 6   ? 24.247  52.040  -34.643 1.00 123.64 ? 6   LYS B N   1 
ATOM   4273  C CA  . LYS B 1 6   ? 24.109  52.823  -35.867 1.00 123.00 ? 6   LYS B CA  1 
ATOM   4274  C C   . LYS B 1 6   ? 25.415  52.760  -36.666 1.00 119.32 ? 6   LYS B C   1 
ATOM   4275  O O   . LYS B 1 6   ? 26.484  53.132  -36.164 1.00 118.50 ? 6   LYS B O   1 
ATOM   4276  C CB  . LYS B 1 6   ? 23.791  54.296  -35.579 1.00 126.16 ? 6   LYS B CB  1 
ATOM   4277  C CG  . LYS B 1 6   ? 22.706  54.580  -34.549 1.00 130.20 ? 6   LYS B CG  1 
ATOM   4278  C CD  . LYS B 1 6   ? 21.300  54.275  -35.052 1.00 132.01 ? 6   LYS B CD  1 
ATOM   4279  C CE  . LYS B 1 6   ? 20.174  54.703  -34.139 1.00 135.77 ? 6   LYS B CE  1 
ATOM   4280  N NZ  . LYS B 1 6   ? 20.374  55.982  -33.450 1.00 138.36 ? 6   LYS B NZ  1 
ATOM   4281  N N   . ILE B 1 7   ? 25.317  52.317  -37.929 1.00 115.81 ? 7   ILE B N   1 
ATOM   4282  C CA  . ILE B 1 7   ? 26.492  52.094  -38.759 1.00 111.75 ? 7   ILE B CA  1 
ATOM   4283  C C   . ILE B 1 7   ? 26.610  53.214  -39.792 1.00 112.46 ? 7   ILE B C   1 
ATOM   4284  O O   . ILE B 1 7   ? 25.832  53.265  -40.744 1.00 111.62 ? 7   ILE B O   1 
ATOM   4285  C CB  . ILE B 1 7   ? 26.447  50.706  -39.427 1.00 107.76 ? 7   ILE B CB  1 
ATOM   4286  C CG1 . ILE B 1 7   ? 26.339  49.597  -38.390 1.00 106.69 ? 7   ILE B CG1 1 
ATOM   4287  C CG2 . ILE B 1 7   ? 27.647  50.503  -40.350 1.00 104.50 ? 7   ILE B CG2 1 
ATOM   4288  C CD1 . ILE B 1 7   ? 26.183  48.217  -38.992 1.00 104.47 ? 7   ILE B CD1 1 
ATOM   4289  N N   . GLU B 1 8   ? 27.647  54.053  -39.618 1.00 113.53 ? 8   GLU B N   1 
ATOM   4290  C CA  . GLU B 1 8   ? 27.949  55.166  -40.513 1.00 114.16 ? 8   GLU B CA  1 
ATOM   4291  C C   . GLU B 1 8   ? 29.229  54.865  -41.317 1.00 111.35 ? 8   GLU B C   1 
ATOM   4292  O O   . GLU B 1 8   ? 30.271  54.553  -40.740 1.00 108.44 ? 8   GLU B O   1 
ATOM   4293  C CB  . GLU B 1 8   ? 28.040  56.468  -39.706 1.00 116.56 ? 8   GLU B CB  1 
ATOM   4294  C CG  . GLU B 1 8   ? 27.064  56.552  -38.532 1.00 118.15 ? 8   GLU B CG  1 
ATOM   4295  C CD  . GLU B 1 8   ? 26.330  57.871  -38.422 1.00 121.37 ? 8   GLU B CD  1 
ATOM   4296  O OE1 . GLU B 1 8   ? 25.946  58.326  -39.513 1.00 121.51 ? 8   GLU B OE1 1 
ATOM   4297  O OE2 . GLU B 1 8   ? 26.102  58.421  -37.317 1.00 123.23 ? 8   GLU B OE2 1 
ATOM   4298  N N   . LEU B 1 9   ? 29.104  54.950  -42.657 1.00 111.51 ? 9   LEU B N   1 
ATOM   4299  C CA  . LEU B 1 9   ? 30.172  54.743  -43.628 1.00 109.38 ? 9   LEU B CA  1 
ATOM   4300  C C   . LEU B 1 9   ? 30.595  56.107  -44.191 1.00 112.72 ? 9   LEU B C   1 
ATOM   4301  O O   . LEU B 1 9   ? 30.034  56.599  -45.172 1.00 112.36 ? 9   LEU B O   1 
ATOM   4302  C CB  . LEU B 1 9   ? 29.711  53.802  -44.749 1.00 106.80 ? 9   LEU B CB  1 
ATOM   4303  C CG  . LEU B 1 9   ? 29.258  52.390  -44.356 1.00 105.56 ? 9   LEU B CG  1 
ATOM   4304  C CD1 . LEU B 1 9   ? 29.053  51.509  -45.593 1.00 103.39 ? 9   LEU B CD1 1 
ATOM   4305  C CD2 . LEU B 1 9   ? 30.235  51.718  -43.397 1.00 105.08 ? 9   LEU B CD2 1 
ATOM   4306  N N   . LYS B 1 10  ? 31.590  56.729  -43.544 1.00 115.47 ? 10  LYS B N   1 
ATOM   4307  C CA  . LYS B 1 10  ? 32.215  57.953  -44.031 1.00 117.99 ? 10  LYS B CA  1 
ATOM   4308  C C   . LYS B 1 10  ? 33.737  57.818  -43.946 1.00 116.72 ? 10  LYS B C   1 
ATOM   4309  O O   . LYS B 1 10  ? 34.256  57.180  -43.037 1.00 115.36 ? 10  LYS B O   1 
ATOM   4310  C CB  . LYS B 1 10  ? 31.771  59.181  -43.231 1.00 122.41 ? 10  LYS B CB  1 
ATOM   4311  C CG  . LYS B 1 10  ? 31.091  58.891  -41.890 1.00 125.29 ? 10  LYS B CG  1 
ATOM   4312  C CD  . LYS B 1 10  ? 31.216  59.991  -40.832 1.00 128.75 ? 10  LYS B CD  1 
ATOM   4313  C CE  . LYS B 1 10  ? 30.214  59.898  -39.711 1.00 129.11 ? 10  LYS B CE  1 
ATOM   4314  N NZ  . LYS B 1 10  ? 28.853  60.104  -40.196 1.00 129.84 ? 10  LYS B NZ  1 
ATOM   4315  N N   . ASP B 1 11  ? 34.449  58.428  -44.901 1.00 115.97 ? 11  ASP B N   1 
ATOM   4316  C CA  . ASP B 1 11  ? 35.901  58.456  -44.889 1.00 113.51 ? 11  ASP B CA  1 
ATOM   4317  C C   . ASP B 1 11  ? 36.462  57.037  -44.972 1.00 109.11 ? 11  ASP B C   1 
ATOM   4318  O O   . ASP B 1 11  ? 37.498  56.720  -44.379 1.00 106.86 ? 11  ASP B O   1 
ATOM   4319  C CB  . ASP B 1 11  ? 36.422  59.180  -43.661 1.00 116.11 ? 11  ASP B CB  1 
ATOM   4320  C CG  . ASP B 1 11  ? 35.821  60.551  -43.469 1.00 121.46 ? 11  ASP B CG  1 
ATOM   4321  O OD1 . ASP B 1 11  ? 35.920  61.338  -44.422 1.00 124.48 ? 11  ASP B OD1 1 
ATOM   4322  O OD2 . ASP B 1 11  ? 35.228  60.784  -42.399 1.00 126.52 ? 11  ASP B OD2 1 
ATOM   4323  N N   . ASN B 1 12  ? 35.776  56.182  -45.735 1.00 106.04 ? 12  ASN B N   1 
ATOM   4324  C CA  . ASN B 1 12  ? 36.252  54.831  -45.988 1.00 100.33 ? 12  ASN B CA  1 
ATOM   4325  C C   . ASN B 1 12  ? 36.518  54.105  -44.667 1.00 98.79  ? 12  ASN B C   1 
ATOM   4326  O O   . ASN B 1 12  ? 37.481  53.358  -44.542 1.00 98.53  ? 12  ASN B O   1 
ATOM   4327  C CB  . ASN B 1 12  ? 37.444  54.909  -46.931 1.00 98.30  ? 12  ASN B CB  1 
ATOM   4328  C CG  . ASN B 1 12  ? 37.100  55.554  -48.252 1.00 98.64  ? 12  ASN B CG  1 
ATOM   4329  O OD1 . ASN B 1 12  ? 35.944  55.521  -48.689 1.00 100.43 ? 12  ASN B OD1 1 
ATOM   4330  N ND2 . ASN B 1 12  ? 38.091  56.113  -48.924 1.00 98.02  ? 12  ASN B ND2 1 
ATOM   4331  N N   . TRP B 1 13  ? 35.648  54.330  -43.679 1.00 100.17 ? 13  TRP B N   1 
ATOM   4332  C CA  . TRP B 1 13  ? 35.702  53.695  -42.372 1.00 99.57  ? 13  TRP B CA  1 
ATOM   4333  C C   . TRP B 1 13  ? 34.287  53.323  -41.922 1.00 99.99  ? 13  TRP B C   1 
ATOM   4334  O O   . TRP B 1 13  ? 33.342  54.112  -42.060 1.00 101.45 ? 13  TRP B O   1 
ATOM   4335  C CB  . TRP B 1 13  ? 36.371  54.631  -41.352 1.00 102.10 ? 13  TRP B CB  1 
ATOM   4336  C CG  . TRP B 1 13  ? 37.870  54.493  -41.272 1.00 101.89 ? 13  TRP B CG  1 
ATOM   4337  C CD1 . TRP B 1 13  ? 38.804  55.045  -42.099 1.00 101.90 ? 13  TRP B CD1 1 
ATOM   4338  C CD2 . TRP B 1 13  ? 38.613  53.750  -40.283 1.00 101.20 ? 13  TRP B CD2 1 
ATOM   4339  N NE1 . TRP B 1 13  ? 40.065  54.688  -41.709 1.00 100.40 ? 13  TRP B NE1 1 
ATOM   4340  C CE2 . TRP B 1 13  ? 39.979  53.902  -40.594 1.00 100.00 ? 13  TRP B CE2 1 
ATOM   4341  C CE3 . TRP B 1 13  ? 38.258  52.973  -39.175 1.00 101.66 ? 13  TRP B CE3 1 
ATOM   4342  C CZ2 . TRP B 1 13  ? 40.981  53.308  -39.834 1.00 99.29  ? 13  TRP B CZ2 1 
ATOM   4343  C CZ3 . TRP B 1 13  ? 39.252  52.384  -38.424 1.00 100.33 ? 13  TRP B CZ3 1 
ATOM   4344  C CH2 . TRP B 1 13  ? 40.595  52.559  -38.746 1.00 99.31  ? 13  TRP B CH2 1 
ATOM   4345  N N   . TYR B 1 14  ? 34.140  52.097  -41.405 1.00 97.91  ? 14  TYR B N   1 
ATOM   4346  C CA  . TYR B 1 14  ? 32.962  51.750  -40.626 1.00 98.43  ? 14  TYR B CA  1 
ATOM   4347  C C   . TYR B 1 14  ? 33.037  52.591  -39.356 1.00 101.01 ? 14  TYR B C   1 
ATOM   4348  O O   . TYR B 1 14  ? 34.121  52.759  -38.792 1.00 100.46 ? 14  TYR B O   1 
ATOM   4349  C CB  . TYR B 1 14  ? 32.846  50.273  -40.219 1.00 96.01  ? 14  TYR B CB  1 
ATOM   4350  C CG  . TYR B 1 14  ? 32.468  49.258  -41.294 1.00 93.60  ? 14  TYR B CG  1 
ATOM   4351  C CD1 . TYR B 1 14  ? 33.316  48.973  -42.361 1.00 91.44  ? 14  TYR B CD1 1 
ATOM   4352  C CD2 . TYR B 1 14  ? 31.306  48.506  -41.189 1.00 93.40  ? 14  TYR B CD2 1 
ATOM   4353  C CE1 . TYR B 1 14  ? 32.981  48.036  -43.326 1.00 89.45  ? 14  TYR B CE1 1 
ATOM   4354  C CE2 . TYR B 1 14  ? 30.962  47.565  -42.144 1.00 91.53  ? 14  TYR B CE2 1 
ATOM   4355  C CZ  . TYR B 1 14  ? 31.794  47.339  -43.222 1.00 89.60  ? 14  TYR B CZ  1 
ATOM   4356  O OH  . TYR B 1 14  ? 31.467  46.416  -44.168 1.00 88.08  ? 14  TYR B OH  1 
ATOM   4357  N N   . HIS B 1 15  ? 31.887  53.123  -38.934 1.00 103.68 ? 15  HIS B N   1 
ATOM   4358  C CA  . HIS B 1 15  ? 31.774  53.818  -37.668 1.00 106.73 ? 15  HIS B CA  1 
ATOM   4359  C C   . HIS B 1 15  ? 30.606  53.224  -36.894 1.00 107.05 ? 15  HIS B C   1 
ATOM   4360  O O   . HIS B 1 15  ? 29.464  53.391  -37.316 1.00 109.19 ? 15  HIS B O   1 
ATOM   4361  C CB  . HIS B 1 15  ? 31.427  55.296  -37.876 1.00 110.90 ? 15  HIS B CB  1 
ATOM   4362  C CG  . HIS B 1 15  ? 32.469  56.156  -38.516 1.00 112.12 ? 15  HIS B CG  1 
ATOM   4363  N ND1 . HIS B 1 15  ? 32.689  56.233  -39.875 1.00 111.52 ? 15  HIS B ND1 1 
ATOM   4364  C CD2 . HIS B 1 15  ? 33.303  57.037  -37.957 1.00 114.05 ? 15  HIS B CD2 1 
ATOM   4365  C CE1 . HIS B 1 15  ? 33.639  57.124  -40.112 1.00 112.24 ? 15  HIS B CE1 1 
ATOM   4366  N NE2 . HIS B 1 15  ? 34.023  57.622  -38.963 1.00 114.09 ? 15  HIS B NE2 1 
ATOM   4367  N N   . LEU B 1 16  ? 30.892  52.561  -35.766 1.00 105.45 ? 16  LEU B N   1 
ATOM   4368  C CA  . LEU B 1 16  ? 29.849  52.132  -34.844 1.00 106.13 ? 16  LEU B CA  1 
ATOM   4369  C C   . LEU B 1 16  ? 29.609  53.219  -33.798 1.00 108.61 ? 16  LEU B C   1 
ATOM   4370  O O   . LEU B 1 16  ? 30.477  53.465  -32.959 1.00 108.56 ? 16  LEU B O   1 
ATOM   4371  C CB  . LEU B 1 16  ? 30.191  50.798  -34.185 1.00 104.26 ? 16  LEU B CB  1 
ATOM   4372  C CG  . LEU B 1 16  ? 29.764  49.543  -34.954 1.00 102.15 ? 16  LEU B CG  1 
ATOM   4373  C CD1 . LEU B 1 16  ? 30.204  49.555  -36.408 1.00 100.11 ? 16  LEU B CD1 1 
ATOM   4374  C CD2 . LEU B 1 16  ? 30.314  48.319  -34.247 1.00 100.51 ? 16  LEU B CD2 1 
ATOM   4375  N N   . ASP B 1 17  ? 28.422  53.847  -33.870 1.00 110.21 ? 17  ASP B N   1 
ATOM   4376  C CA  . ASP B 1 17  ? 27.957  54.794  -32.868 1.00 113.34 ? 17  ASP B CA  1 
ATOM   4377  C C   . ASP B 1 17  ? 28.898  56.001  -32.820 1.00 114.39 ? 17  ASP B C   1 
ATOM   4378  O O   . ASP B 1 17  ? 29.436  56.324  -31.761 1.00 115.43 ? 17  ASP B O   1 
ATOM   4379  C CB  . ASP B 1 17  ? 27.762  54.111  -31.518 1.00 113.93 ? 17  ASP B CB  1 
ATOM   4380  C CG  . ASP B 1 17  ? 26.823  52.911  -31.519 1.00 113.10 ? 17  ASP B CG  1 
ATOM   4381  O OD1 . ASP B 1 17  ? 25.732  53.024  -32.121 1.00 114.28 ? 17  ASP B OD1 1 
ATOM   4382  O OD2 . ASP B 1 17  ? 27.169  51.880  -30.899 1.00 111.59 ? 17  ASP B OD2 1 
ATOM   4383  N N   . GLY B 1 18  ? 29.100  56.644  -33.984 1.00 114.08 ? 18  GLY B N   1 
ATOM   4384  C CA  . GLY B 1 18  ? 30.045  57.742  -34.142 1.00 115.13 ? 18  GLY B CA  1 
ATOM   4385  C C   . GLY B 1 18  ? 31.514  57.285  -34.243 1.00 113.06 ? 18  GLY B C   1 
ATOM   4386  O O   . GLY B 1 18  ? 32.363  58.032  -34.739 1.00 113.52 ? 18  GLY B O   1 
ATOM   4387  N N   . GLU B 1 19  ? 31.841  56.062  -33.791 1.00 110.64 ? 19  GLU B N   1 
ATOM   4388  C CA  . GLU B 1 19  ? 33.206  55.762  -33.392 1.00 109.20 ? 19  GLU B CA  1 
ATOM   4389  C C   . GLU B 1 19  ? 33.862  54.832  -34.405 1.00 106.16 ? 19  GLU B C   1 
ATOM   4390  O O   . GLU B 1 19  ? 33.559  53.644  -34.458 1.00 104.42 ? 19  GLU B O   1 
ATOM   4391  C CB  . GLU B 1 19  ? 33.206  55.186  -31.975 1.00 109.58 ? 19  GLU B CB  1 
ATOM   4392  C CG  . GLU B 1 19  ? 33.004  56.241  -30.889 1.00 112.92 ? 19  GLU B CG  1 
ATOM   4393  C CD  . GLU B 1 19  ? 34.202  57.159  -30.696 1.00 113.67 ? 19  GLU B CD  1 
ATOM   4394  O OE1 . GLU B 1 19  ? 35.246  56.939  -31.362 1.00 111.56 ? 19  GLU B OE1 1 
ATOM   4395  O OE2 . GLU B 1 19  ? 34.121  58.080  -29.865 1.00 116.37 ? 19  GLU B OE2 1 
ATOM   4396  N N   . LYS B 1 20  ? 34.799  55.366  -35.187 1.00 105.93 ? 20  LYS B N   1 
ATOM   4397  C CA  . LYS B 1 20  ? 35.506  54.528  -36.141 1.00 103.68 ? 20  LYS B CA  1 
ATOM   4398  C C   . LYS B 1 20  ? 35.798  53.163  -35.512 1.00 101.24 ? 20  LYS B C   1 
ATOM   4399  O O   . LYS B 1 20  ? 36.245  53.091  -34.365 1.00 101.56 ? 20  LYS B O   1 
ATOM   4400  C CB  . LYS B 1 20  ? 36.777  55.219  -36.650 1.00 104.15 ? 20  LYS B CB  1 
ATOM   4401  C CG  . LYS B 1 20  ? 36.514  56.327  -37.673 1.00 106.04 ? 20  LYS B CG  1 
ATOM   4402  C CD  . LYS B 1 20  ? 37.782  56.947  -38.256 1.00 106.21 ? 20  LYS B CD  1 
ATOM   4403  C CE  . LYS B 1 20  ? 38.303  58.089  -37.439 1.00 109.11 ? 20  LYS B CE  1 
ATOM   4404  N NZ  . LYS B 1 20  ? 37.395  59.238  -37.443 1.00 112.20 ? 20  LYS B NZ  1 
ATOM   4405  N N   . TYR B 1 21  ? 35.529  52.100  -36.293 1.00 98.89  ? 21  TYR B N   1 
ATOM   4406  C CA  . TYR B 1 21  ? 35.603  50.713  -35.844 1.00 97.19  ? 21  TYR B CA  1 
ATOM   4407  C C   . TYR B 1 21  ? 36.410  49.896  -36.850 1.00 94.67  ? 21  TYR B C   1 
ATOM   4408  O O   . TYR B 1 21  ? 36.088  49.810  -38.036 1.00 93.31  ? 21  TYR B O   1 
ATOM   4409  C CB  . TYR B 1 21  ? 34.187  50.139  -35.683 1.00 97.44  ? 21  TYR B CB  1 
ATOM   4410  C CG  . TYR B 1 21  ? 34.036  48.825  -34.918 1.00 96.03  ? 21  TYR B CG  1 
ATOM   4411  C CD1 . TYR B 1 21  ? 33.852  48.821  -33.536 1.00 97.44  ? 21  TYR B CD1 1 
ATOM   4412  C CD2 . TYR B 1 21  ? 34.023  47.591  -35.571 1.00 93.29  ? 21  TYR B CD2 1 
ATOM   4413  C CE1 . TYR B 1 21  ? 33.697  47.636  -32.830 1.00 96.49  ? 21  TYR B CE1 1 
ATOM   4414  C CE2 . TYR B 1 21  ? 33.862  46.401  -34.875 1.00 92.32  ? 21  TYR B CE2 1 
ATOM   4415  C CZ  . TYR B 1 21  ? 33.697  46.426  -33.500 1.00 93.89  ? 21  TYR B CZ  1 
ATOM   4416  O OH  . TYR B 1 21  ? 33.527  45.286  -32.774 1.00 93.35  ? 21  TYR B OH  1 
ATOM   4417  N N   . PHE B 1 22  ? 37.483  49.291  -36.357 1.00 94.69  ? 22  PHE B N   1 
ATOM   4418  C CA  . PHE B 1 22  ? 38.299  48.420  -37.186 1.00 93.44  ? 22  PHE B CA  1 
ATOM   4419  C C   . PHE B 1 22  ? 37.824  46.983  -36.965 1.00 93.38  ? 22  PHE B C   1 
ATOM   4420  O O   . PHE B 1 22  ? 37.976  46.429  -35.870 1.00 94.05  ? 22  PHE B O   1 
ATOM   4421  C CB  . PHE B 1 22  ? 39.800  48.602  -36.915 1.00 92.57  ? 22  PHE B CB  1 
ATOM   4422  C CG  . PHE B 1 22  ? 40.679  48.076  -38.043 1.00 90.15  ? 22  PHE B CG  1 
ATOM   4423  C CD1 . PHE B 1 22  ? 41.025  46.728  -38.104 1.00 88.35  ? 22  PHE B CD1 1 
ATOM   4424  C CD2 . PHE B 1 22  ? 41.124  48.920  -39.057 1.00 90.05  ? 22  PHE B CD2 1 
ATOM   4425  C CE1 . PHE B 1 22  ? 41.809  46.247  -39.137 1.00 86.54  ? 22  PHE B CE1 1 
ATOM   4426  C CE2 . PHE B 1 22  ? 41.902  48.431  -40.092 1.00 88.29  ? 22  PHE B CE2 1 
ATOM   4427  C CZ  . PHE B 1 22  ? 42.250  47.100  -40.125 1.00 86.64  ? 22  PHE B CZ  1 
ATOM   4428  N N   . ILE B 1 23  ? 37.247  46.395  -38.025 1.00 93.08  ? 23  ILE B N   1 
ATOM   4429  C CA  . ILE B 1 23  ? 36.703  45.048  -37.972 1.00 92.18  ? 23  ILE B CA  1 
ATOM   4430  C C   . ILE B 1 23  ? 37.871  44.065  -37.910 1.00 91.41  ? 23  ILE B C   1 
ATOM   4431  O O   . ILE B 1 23  ? 38.495  43.750  -38.921 1.00 88.69  ? 23  ILE B O   1 
ATOM   4432  C CB  . ILE B 1 23  ? 35.769  44.776  -39.164 1.00 90.72  ? 23  ILE B CB  1 
ATOM   4433  C CG1 . ILE B 1 23  ? 34.643  45.792  -39.251 1.00 91.79  ? 23  ILE B CG1 1 
ATOM   4434  C CG2 . ILE B 1 23  ? 35.227  43.351  -39.094 1.00 90.12  ? 23  ILE B CG2 1 
ATOM   4435  C CD1 . ILE B 1 23  ? 33.968  45.815  -40.606 1.00 91.16  ? 23  ILE B CD1 1 
ATOM   4436  N N   . LYS B 1 24  ? 38.171  43.634  -36.683 1.00 93.98  ? 24  LYS B N   1 
ATOM   4437  C CA  . LYS B 1 24  ? 39.136  42.586  -36.423 1.00 94.51  ? 24  LYS B CA  1 
ATOM   4438  C C   . LYS B 1 24  ? 38.393  41.258  -36.400 1.00 94.08  ? 24  LYS B C   1 
ATOM   4439  O O   . LYS B 1 24  ? 38.036  40.770  -35.332 1.00 95.99  ? 24  LYS B O   1 
ATOM   4440  C CB  . LYS B 1 24  ? 39.818  42.840  -35.075 1.00 97.49  ? 24  LYS B CB  1 
ATOM   4441  C CG  . LYS B 1 24  ? 40.538  44.177  -34.957 1.00 99.83  ? 24  LYS B CG  1 
ATOM   4442  C CD  . LYS B 1 24  ? 41.334  44.316  -33.667 1.00 102.64 ? 24  LYS B CD  1 
ATOM   4443  C CE  . LYS B 1 24  ? 40.455  44.252  -32.460 1.00 106.74 ? 24  LYS B CE  1 
ATOM   4444  N NZ  . LYS B 1 24  ? 41.280  44.355  -31.257 1.00 110.50 ? 24  LYS B NZ  1 
ATOM   4445  N N   . ALA B 1 25  ? 38.154  40.697  -37.588 1.00 92.23  ? 25  ALA B N   1 
ATOM   4446  C CA  . ALA B 1 25  ? 37.350  39.494  -37.717 1.00 92.00  ? 25  ALA B CA  1 
ATOM   4447  C C   . ALA B 1 25  ? 38.233  38.254  -37.782 1.00 92.42  ? 25  ALA B C   1 
ATOM   4448  O O   . ALA B 1 25  ? 39.473  38.360  -37.833 1.00 94.14  ? 25  ALA B O   1 
ATOM   4449  C CB  . ALA B 1 25  ? 36.481  39.577  -38.946 1.00 91.30  ? 25  ALA B CB  1 
ATOM   4450  N N   . ILE B 1 26  ? 37.539  37.098  -37.755 1.00 90.73  ? 26  ILE B N   1 
ATOM   4451  C CA  . ILE B 1 26  ? 38.060  35.810  -38.186 1.00 87.62  ? 26  ILE B CA  1 
ATOM   4452  C C   . ILE B 1 26  ? 36.945  35.076  -38.935 1.00 86.44  ? 26  ILE B C   1 
ATOM   4453  O O   . ILE B 1 26  ? 35.783  35.153  -38.559 1.00 86.65  ? 26  ILE B O   1 
ATOM   4454  C CB  . ILE B 1 26  ? 38.607  35.005  -36.990 1.00 87.66  ? 26  ILE B CB  1 
ATOM   4455  C CG1 . ILE B 1 26  ? 39.342  33.722  -37.435 1.00 86.24  ? 26  ILE B CG1 1 
ATOM   4456  C CG2 . ILE B 1 26  ? 37.502  34.711  -35.976 1.00 88.76  ? 26  ILE B CG2 1 
ATOM   4457  C CD1 . ILE B 1 26  ? 40.074  32.997  -36.317 1.00 86.18  ? 26  ILE B CD1 1 
ATOM   4458  N N   . GLY B 1 27  ? 37.298  34.416  -40.042 1.00 84.85  ? 27  GLY B N   1 
ATOM   4459  C CA  . GLY B 1 27  ? 36.396  33.485  -40.698 1.00 84.16  ? 27  GLY B CA  1 
ATOM   4460  C C   . GLY B 1 27  ? 36.078  32.318  -39.768 1.00 83.91  ? 27  GLY B C   1 
ATOM   4461  O O   . GLY B 1 27  ? 36.975  31.752  -39.152 1.00 81.86  ? 27  GLY B O   1 
ATOM   4462  N N   . TYR B 1 28  ? 34.779  32.011  -39.660 1.00 85.88  ? 28  TYR B N   1 
ATOM   4463  C CA  . TYR B 1 28  ? 34.252  31.018  -38.733 1.00 86.85  ? 28  TYR B CA  1 
ATOM   4464  C C   . TYR B 1 28  ? 33.215  30.180  -39.460 1.00 87.01  ? 28  TYR B C   1 
ATOM   4465  O O   . TYR B 1 28  ? 32.364  30.758  -40.136 1.00 89.11  ? 28  TYR B O   1 
ATOM   4466  C CB  . TYR B 1 28  ? 33.542  31.661  -37.536 1.00 88.24  ? 28  TYR B CB  1 
ATOM   4467  C CG  . TYR B 1 28  ? 32.995  30.664  -36.524 1.00 89.48  ? 28  TYR B CG  1 
ATOM   4468  C CD1 . TYR B 1 28  ? 33.843  29.879  -35.760 1.00 89.33  ? 28  TYR B CD1 1 
ATOM   4469  C CD2 . TYR B 1 28  ? 31.638  30.532  -36.311 1.00 91.61  ? 28  TYR B CD2 1 
ATOM   4470  C CE1 . TYR B 1 28  ? 33.362  28.983  -34.825 1.00 90.75  ? 28  TYR B CE1 1 
ATOM   4471  C CE2 . TYR B 1 28  ? 31.139  29.631  -35.386 1.00 93.42  ? 28  TYR B CE2 1 
ATOM   4472  C CZ  . TYR B 1 28  ? 32.006  28.866  -34.635 1.00 92.71  ? 28  TYR B CZ  1 
ATOM   4473  O OH  . TYR B 1 28  ? 31.529  27.989  -33.720 1.00 95.39  ? 28  TYR B OH  1 
ATOM   4474  N N   . GLU B 1 29  ? 33.264  28.855  -39.268 1.00 85.93  ? 29  GLU B N   1 
ATOM   4475  C CA  . GLU B 1 29  ? 32.277  27.961  -39.850 1.00 86.55  ? 29  GLU B CA  1 
ATOM   4476  C C   . GLU B 1 29  ? 31.908  26.882  -38.833 1.00 88.72  ? 29  GLU B C   1 
ATOM   4477  O O   . GLU B 1 29  ? 32.737  26.033  -38.516 1.00 89.90  ? 29  GLU B O   1 
ATOM   4478  C CB  . GLU B 1 29  ? 32.830  27.407  -41.161 1.00 84.69  ? 29  GLU B CB  1 
ATOM   4479  C CG  . GLU B 1 29  ? 31.837  26.572  -41.967 1.00 85.67  ? 29  GLU B CG  1 
ATOM   4480  C CD  . GLU B 1 29  ? 32.383  26.045  -43.290 1.00 84.95  ? 29  GLU B CD  1 
ATOM   4481  O OE1 . GLU B 1 29  ? 33.395  25.288  -43.256 1.00 84.48  ? 29  GLU B OE1 1 
ATOM   4482  O OE2 . GLU B 1 29  ? 31.814  26.402  -44.355 1.00 84.56  ? 29  GLU B OE2 1 
ATOM   4483  N N   . ILE B 1 30  ? 30.665  26.925  -38.328 1.00 90.42  ? 30  ILE B N   1 
ATOM   4484  C CA  . ILE B 1 30  ? 30.132  25.894  -37.446 1.00 92.14  ? 30  ILE B CA  1 
ATOM   4485  C C   . ILE B 1 30  ? 29.615  24.724  -38.287 1.00 92.32  ? 30  ILE B C   1 
ATOM   4486  O O   . ILE B 1 30  ? 29.281  24.890  -39.458 1.00 90.98  ? 30  ILE B O   1 
ATOM   4487  C CB  . ILE B 1 30  ? 29.041  26.484  -36.530 1.00 94.50  ? 30  ILE B CB  1 
ATOM   4488  C CG1 . ILE B 1 30  ? 28.620  25.523  -35.401 1.00 96.97  ? 30  ILE B CG1 1 
ATOM   4489  C CG2 . ILE B 1 30  ? 27.830  26.945  -37.343 1.00 94.99  ? 30  ILE B CG2 1 
ATOM   4490  C CD1 . ILE B 1 30  ? 29.721  25.171  -34.417 1.00 97.14  ? 30  ILE B CD1 1 
ATOM   4491  N N   . GLY B 1 31  ? 29.568  23.534  -37.674 1.00 93.97  ? 31  GLY B N   1 
ATOM   4492  C CA  . GLY B 1 31  ? 29.147  22.317  -38.351 1.00 95.17  ? 31  GLY B CA  1 
ATOM   4493  C C   . GLY B 1 31  ? 30.178  21.821  -39.369 1.00 94.28  ? 31  GLY B C   1 
ATOM   4494  O O   . GLY B 1 31  ? 29.792  21.331  -40.430 1.00 94.00  ? 31  GLY B O   1 
ATOM   4495  N N   . ALA B 1 32  ? 31.482  21.955  -39.040 1.00 94.00  ? 32  ALA B N   1 
ATOM   4496  C CA  . ALA B 1 32  ? 32.578  21.442  -39.864 1.00 92.58  ? 32  ALA B CA  1 
ATOM   4497  C C   . ALA B 1 32  ? 33.617  20.694  -39.026 1.00 92.14  ? 32  ALA B C   1 
ATOM   4498  O O   . ALA B 1 32  ? 34.809  20.760  -39.304 1.00 90.55  ? 32  ALA B O   1 
ATOM   4499  C CB  . ALA B 1 32  ? 33.228  22.576  -40.622 1.00 90.79  ? 32  ALA B CB  1 
ATOM   4500  N N   . ARG B 1 33  ? 33.154  19.985  -37.995 1.00 94.68  ? 33  ARG B N   1 
ATOM   4501  C CA  . ARG B 1 33  ? 34.013  19.119  -37.208 1.00 96.30  ? 33  ARG B CA  1 
ATOM   4502  C C   . ARG B 1 33  ? 34.324  17.861  -38.010 1.00 98.56  ? 33  ARG B C   1 
ATOM   4503  O O   . ARG B 1 33  ? 33.585  17.510  -38.929 1.00 99.28  ? 33  ARG B O   1 
ATOM   4504  C CB  . ARG B 1 33  ? 33.395  18.674  -35.877 1.00 97.82  ? 33  ARG B CB  1 
ATOM   4505  C CG  . ARG B 1 33  ? 33.862  19.436  -34.646 1.00 96.75  ? 33  ARG B CG  1 
ATOM   4506  C CD  . ARG B 1 33  ? 33.550  20.896  -34.799 1.00 94.79  ? 33  ARG B CD  1 
ATOM   4507  N NE  . ARG B 1 33  ? 33.820  21.628  -33.562 1.00 94.81  ? 33  ARG B NE  1 
ATOM   4508  C CZ  . ARG B 1 33  ? 33.684  22.940  -33.432 1.00 94.26  ? 33  ARG B CZ  1 
ATOM   4509  N NH1 . ARG B 1 33  ? 33.149  23.666  -34.403 1.00 93.16  ? 33  ARG B NH1 1 
ATOM   4510  N NH2 . ARG B 1 33  ? 34.048  23.521  -32.304 1.00 95.30  ? 33  ARG B NH2 1 
ATOM   4511  N N   . PRO B 1 34  ? 35.441  17.167  -37.695 1.00 99.85  ? 34  PRO B N   1 
ATOM   4512  C CA  . PRO B 1 34  ? 35.757  15.887  -38.318 1.00 100.55 ? 34  PRO B CA  1 
ATOM   4513  C C   . PRO B 1 34  ? 34.490  15.056  -38.266 1.00 102.49 ? 34  PRO B C   1 
ATOM   4514  O O   . PRO B 1 34  ? 33.991  14.795  -37.180 1.00 104.75 ? 34  PRO B O   1 
ATOM   4515  C CB  . PRO B 1 34  ? 36.903  15.287  -37.477 1.00 101.69 ? 34  PRO B CB  1 
ATOM   4516  C CG  . PRO B 1 34  ? 37.550  16.496  -36.812 1.00 101.09 ? 34  PRO B CG  1 
ATOM   4517  C CD  . PRO B 1 34  ? 36.494  17.616  -36.770 1.00 100.58 ? 34  PRO B CD  1 
ATOM   4518  N N   . GLY B 1 35  ? 33.971  14.705  -39.450 1.00 102.43 ? 35  GLY B N   1 
ATOM   4519  C CA  . GLY B 1 35  ? 32.775  13.889  -39.576 1.00 104.21 ? 35  GLY B CA  1 
ATOM   4520  C C   . GLY B 1 35  ? 31.550  14.687  -40.023 1.00 103.71 ? 35  GLY B C   1 
ATOM   4521  O O   . GLY B 1 35  ? 30.561  14.100  -40.441 1.00 105.97 ? 35  GLY B O   1 
ATOM   4522  N N   . GLN B 1 36  ? 31.595  16.018  -39.928 1.00 101.83 ? 36  GLN B N   1 
ATOM   4523  C CA  . GLN B 1 36  ? 30.473  16.837  -40.351 1.00 102.07 ? 36  GLN B CA  1 
ATOM   4524  C C   . GLN B 1 36  ? 30.820  17.543  -41.651 1.00 101.11 ? 36  GLN B C   1 
ATOM   4525  O O   . GLN B 1 36  ? 31.916  18.081  -41.792 1.00 101.41 ? 36  GLN B O   1 
ATOM   4526  C CB  . GLN B 1 36  ? 30.148  17.939  -39.350 1.00 101.72 ? 36  GLN B CB  1 
ATOM   4527  C CG  . GLN B 1 36  ? 30.179  17.480  -37.901 1.00 103.98 ? 36  GLN B CG  1 
ATOM   4528  C CD  . GLN B 1 36  ? 29.763  18.576  -36.948 1.00 105.17 ? 36  GLN B CD  1 
ATOM   4529  O OE1 . GLN B 1 36  ? 30.213  19.723  -37.055 1.00 102.87 ? 36  GLN B OE1 1 
ATOM   4530  N NE2 . GLN B 1 36  ? 28.864  18.243  -36.030 1.00 108.93 ? 36  GLN B NE2 1 
ATOM   4531  N N   . ALA B 1 37  ? 29.864  17.556  -42.578 1.00 102.52 ? 37  ALA B N   1 
ATOM   4532  C CA  . ALA B 1 37  ? 29.890  18.478  -43.702 1.00 102.05 ? 37  ALA B CA  1 
ATOM   4533  C C   . ALA B 1 37  ? 28.678  19.411  -43.594 1.00 101.87 ? 37  ALA B C   1 
ATOM   4534  O O   . ALA B 1 37  ? 27.554  18.931  -43.424 1.00 102.90 ? 37  ALA B O   1 
ATOM   4535  C CB  . ALA B 1 37  ? 29.925  17.695  -45.001 1.00 103.10 ? 37  ALA B CB  1 
ATOM   4536  N N   . PRO B 1 38  ? 28.866  20.757  -43.661 1.00 99.16  ? 38  PRO B N   1 
ATOM   4537  C CA  . PRO B 1 38  ? 27.816  21.710  -43.278 1.00 100.18 ? 38  PRO B CA  1 
ATOM   4538  C C   . PRO B 1 38  ? 26.686  21.908  -44.292 1.00 101.45 ? 38  PRO B C   1 
ATOM   4539  O O   . PRO B 1 38  ? 25.518  21.958  -43.910 1.00 103.98 ? 38  PRO B O   1 
ATOM   4540  C CB  . PRO B 1 38  ? 28.557  23.023  -42.984 1.00 97.85  ? 38  PRO B CB  1 
ATOM   4541  C CG  . PRO B 1 38  ? 29.934  22.856  -43.589 1.00 95.93  ? 38  PRO B CG  1 
ATOM   4542  C CD  . PRO B 1 38  ? 30.103  21.423  -44.082 1.00 96.60  ? 38  PRO B CD  1 
ATOM   4543  N N   . TYR B 1 39  ? 27.026  21.946  -45.586 1.00 100.13 ? 39  TYR B N   1 
ATOM   4544  C CA  . TYR B 1 39  ? 26.040  22.135  -46.643 1.00 100.54 ? 39  TYR B CA  1 
ATOM   4545  C C   . TYR B 1 39  ? 25.279  20.846  -47.007 1.00 102.42 ? 39  TYR B C   1 
ATOM   4546  O O   . TYR B 1 39  ? 24.352  20.930  -47.801 1.00 101.90 ? 39  TYR B O   1 
ATOM   4547  C CB  . TYR B 1 39  ? 26.769  22.721  -47.860 1.00 97.91  ? 39  TYR B CB  1 
ATOM   4548  C CG  . TYR B 1 39  ? 27.368  24.105  -47.651 1.00 96.29  ? 39  TYR B CG  1 
ATOM   4549  C CD1 . TYR B 1 39  ? 28.607  24.271  -47.033 1.00 95.98  ? 39  TYR B CD1 1 
ATOM   4550  C CD2 . TYR B 1 39  ? 26.726  25.239  -48.118 1.00 95.14  ? 39  TYR B CD2 1 
ATOM   4551  C CE1 . TYR B 1 39  ? 29.161  25.525  -46.840 1.00 93.46  ? 39  TYR B CE1 1 
ATOM   4552  C CE2 . TYR B 1 39  ? 27.275  26.496  -47.940 1.00 94.01  ? 39  TYR B CE2 1 
ATOM   4553  C CZ  . TYR B 1 39  ? 28.486  26.642  -47.291 1.00 92.96  ? 39  TYR B CZ  1 
ATOM   4554  O OH  . TYR B 1 39  ? 29.010  27.883  -47.111 1.00 92.07  ? 39  TYR B OH  1 
ATOM   4555  N N   . GLU B 1 40  ? 25.669  19.672  -46.470 1.00 104.96 ? 40  GLU B N   1 
ATOM   4556  C CA  . GLU B 1 40  ? 25.116  18.373  -46.854 1.00 109.44 ? 40  GLU B CA  1 
ATOM   4557  C C   . GLU B 1 40  ? 24.189  17.821  -45.764 1.00 112.26 ? 40  GLU B C   1 
ATOM   4558  O O   . GLU B 1 40  ? 23.123  17.263  -46.044 1.00 113.31 ? 40  GLU B O   1 
ATOM   4559  C CB  . GLU B 1 40  ? 26.149  17.246  -46.993 1.00 112.07 ? 40  GLU B CB  1 
ATOM   4560  C CG  . GLU B 1 40  ? 27.313  17.466  -47.960 1.00 112.08 ? 40  GLU B CG  1 
ATOM   4561  C CD  . GLU B 1 40  ? 28.149  16.201  -48.193 1.00 116.43 ? 40  GLU B CD  1 
ATOM   4562  O OE1 . GLU B 1 40  ? 28.275  15.361  -47.265 1.00 117.69 ? 40  GLU B OE1 1 
ATOM   4563  O OE2 . GLU B 1 40  ? 28.715  16.045  -49.300 1.00 121.07 ? 40  GLU B OE2 1 
ATOM   4564  N N   . ASP B 1 41  ? 24.660  17.912  -44.515 1.00 112.80 ? 41  ASP B N   1 
ATOM   4565  C CA  . ASP B 1 41  ? 23.998  17.313  -43.371 1.00 115.54 ? 41  ASP B CA  1 
ATOM   4566  C C   . ASP B 1 41  ? 22.736  18.098  -43.063 1.00 116.91 ? 41  ASP B C   1 
ATOM   4567  O O   . ASP B 1 41  ? 22.670  19.287  -43.358 1.00 116.62 ? 41  ASP B O   1 
ATOM   4568  C CB  . ASP B 1 41  ? 24.883  17.380  -42.137 1.00 115.47 ? 41  ASP B CB  1 
ATOM   4569  C CG  . ASP B 1 41  ? 26.214  16.645  -42.227 1.00 113.40 ? 41  ASP B CG  1 
ATOM   4570  O OD1 . ASP B 1 41  ? 26.433  15.922  -43.227 1.00 112.43 ? 41  ASP B OD1 1 
ATOM   4571  O OD2 . ASP B 1 41  ? 27.020  16.815  -41.293 1.00 112.70 ? 41  ASP B OD2 1 
ATOM   4572  N N   . GLU B 1 42  ? 21.751  17.427  -42.461 1.00 120.01 ? 42  GLU B N   1 
ATOM   4573  C CA  . GLU B 1 42  ? 20.618  18.126  -41.878 1.00 120.85 ? 42  GLU B CA  1 
ATOM   4574  C C   . GLU B 1 42  ? 21.159  19.146  -40.875 1.00 120.86 ? 42  GLU B C   1 
ATOM   4575  O O   . GLU B 1 42  ? 21.927  18.777  -39.986 1.00 120.10 ? 42  GLU B O   1 
ATOM   4576  C CB  . GLU B 1 42  ? 19.689  17.138  -41.177 1.00 123.04 ? 42  GLU B CB  1 
ATOM   4577  C CG  . GLU B 1 42  ? 18.440  17.801  -40.602 1.00 124.12 ? 42  GLU B CG  1 
ATOM   4578  C CD  . GLU B 1 42  ? 17.802  17.046  -39.456 1.00 126.44 ? 42  GLU B CD  1 
ATOM   4579  O OE1 . GLU B 1 42  ? 18.463  16.113  -38.957 1.00 126.53 ? 42  GLU B OE1 1 
ATOM   4580  O OE2 . GLU B 1 42  ? 16.661  17.391  -39.072 1.00 128.01 ? 42  GLU B OE2 1 
ATOM   4581  N N   . ARG B 1 43  ? 20.758  20.421  -41.025 1.00 120.83 ? 43  ARG B N   1 
ATOM   4582  C CA  . ARG B 1 43  ? 21.419  21.517  -40.328 1.00 118.55 ? 43  ARG B CA  1 
ATOM   4583  C C   . ARG B 1 43  ? 20.978  21.551  -38.866 1.00 118.56 ? 43  ARG B C   1 
ATOM   4584  O O   . ARG B 1 43  ? 19.814  21.303  -38.557 1.00 120.30 ? 43  ARG B O   1 
ATOM   4585  C CB  . ARG B 1 43  ? 21.198  22.888  -40.984 1.00 117.16 ? 43  ARG B CB  1 
ATOM   4586  C CG  . ARG B 1 43  ? 19.788  23.463  -40.944 1.00 118.57 ? 43  ARG B CG  1 
ATOM   4587  C CD  . ARG B 1 43  ? 19.788  24.833  -41.608 1.00 116.94 ? 43  ARG B CD  1 
ATOM   4588  N NE  . ARG B 1 43  ? 18.446  25.364  -41.873 1.00 119.05 ? 43  ARG B NE  1 
ATOM   4589  C CZ  . ARG B 1 43  ? 17.551  25.703  -40.951 1.00 121.68 ? 43  ARG B CZ  1 
ATOM   4590  N NH1 . ARG B 1 43  ? 17.825  25.478  -39.679 1.00 122.76 ? 43  ARG B NH1 1 
ATOM   4591  N NH2 . ARG B 1 43  ? 16.386  26.249  -41.296 1.00 122.80 ? 43  ARG B NH2 1 
ATOM   4592  N N   . LYS B 1 44  ? 21.934  21.881  -37.990 1.00 116.09 ? 44  LYS B N   1 
ATOM   4593  C CA  . LYS B 1 44  ? 21.691  21.978  -36.563 1.00 116.51 ? 44  LYS B CA  1 
ATOM   4594  C C   . LYS B 1 44  ? 22.443  23.191  -36.005 1.00 112.69 ? 44  LYS B C   1 
ATOM   4595  O O   . LYS B 1 44  ? 23.468  23.620  -36.548 1.00 109.85 ? 44  LYS B O   1 
ATOM   4596  C CB  . LYS B 1 44  ? 22.012  20.620  -35.924 1.00 118.43 ? 44  LYS B CB  1 
ATOM   4597  C CG  . LYS B 1 44  ? 21.608  20.472  -34.458 1.00 122.36 ? 44  LYS B CG  1 
ATOM   4598  C CD  . LYS B 1 44  ? 22.683  20.861  -33.442 1.00 122.06 ? 44  LYS B CD  1 
ATOM   4599  C CE  . LYS B 1 44  ? 22.120  21.201  -32.080 1.00 124.44 ? 44  LYS B CE  1 
ATOM   4600  N NZ  . LYS B 1 44  ? 23.136  21.399  -31.041 1.00 123.36 ? 44  LYS B NZ  1 
ATOM   4601  N N   . ASP B 1 45  ? 21.899  23.718  -34.900 1.00 112.36 ? 45  ASP B N   1 
ATOM   4602  C CA  . ASP B 1 45  ? 22.288  24.997  -34.331 1.00 110.69 ? 45  ASP B CA  1 
ATOM   4603  C C   . ASP B 1 45  ? 23.706  24.921  -33.771 1.00 108.71 ? 45  ASP B C   1 
ATOM   4604  O O   . ASP B 1 45  ? 24.478  25.860  -33.932 1.00 105.89 ? 45  ASP B O   1 
ATOM   4605  C CB  . ASP B 1 45  ? 21.276  25.451  -33.287 1.00 112.95 ? 45  ASP B CB  1 
ATOM   4606  C CG  . ASP B 1 45  ? 19.917  25.889  -33.824 1.00 113.82 ? 45  ASP B CG  1 
ATOM   4607  O OD1 . ASP B 1 45  ? 19.907  26.621  -34.838 1.00 111.15 ? 45  ASP B OD1 1 
ATOM   4608  O OD2 . ASP B 1 45  ? 18.878  25.513  -33.213 1.00 117.17 ? 45  ASP B OD2 1 
ATOM   4609  N N   . GLU B 1 46  ? 23.988  23.813  -33.074 1.00 110.29 ? 46  GLU B N   1 
ATOM   4610  C CA  . GLU B 1 46  ? 25.315  23.395  -32.645 1.00 108.48 ? 46  GLU B CA  1 
ATOM   4611  C C   . GLU B 1 46  ? 25.841  24.369  -31.595 1.00 108.19 ? 46  GLU B C   1 
ATOM   4612  O O   . GLU B 1 46  ? 26.994  24.779  -31.657 1.00 108.77 ? 46  GLU B O   1 
ATOM   4613  C CB  . GLU B 1 46  ? 26.270  23.243  -33.834 1.00 105.78 ? 46  GLU B CB  1 
ATOM   4614  C CG  . GLU B 1 46  ? 26.026  22.006  -34.699 1.00 106.12 ? 46  GLU B CG  1 
ATOM   4615  C CD  . GLU B 1 46  ? 26.762  20.727  -34.293 1.00 106.31 ? 46  GLU B CD  1 
ATOM   4616  O OE1 . GLU B 1 46  ? 27.461  20.697  -33.251 1.00 105.69 ? 46  GLU B OE1 1 
ATOM   4617  O OE2 . GLU B 1 46  ? 26.641  19.736  -35.048 1.00 106.10 ? 46  GLU B OE2 1 
ATOM   4618  N N   . LEU B 1 47  ? 25.011  24.689  -30.606 1.00 110.05 ? 47  LEU B N   1 
ATOM   4619  C CA  . LEU B 1 47  ? 25.247  25.830  -29.738 1.00 110.00 ? 47  LEU B CA  1 
ATOM   4620  C C   . LEU B 1 47  ? 26.327  25.506  -28.715 1.00 109.52 ? 47  LEU B C   1 
ATOM   4621  O O   . LEU B 1 47  ? 27.210  26.321  -28.464 1.00 108.50 ? 47  LEU B O   1 
ATOM   4622  C CB  . LEU B 1 47  ? 23.945  26.228  -29.051 1.00 112.88 ? 47  LEU B CB  1 
ATOM   4623  C CG  . LEU B 1 47  ? 22.754  26.420  -29.990 1.00 113.76 ? 47  LEU B CG  1 
ATOM   4624  C CD1 . LEU B 1 47  ? 21.471  25.894  -29.366 1.00 117.36 ? 47  LEU B CD1 1 
ATOM   4625  C CD2 . LEU B 1 47  ? 22.641  27.883  -30.397 1.00 113.01 ? 47  LEU B CD2 1 
ATOM   4626  N N   . GLU B 1 48  ? 26.265  24.320  -28.116 1.00 110.70 ? 48  GLU B N   1 
ATOM   4627  C CA  . GLU B 1 48  ? 27.227  24.009  -27.077 1.00 111.34 ? 48  GLU B CA  1 
ATOM   4628  C C   . GLU B 1 48  ? 28.647  24.135  -27.639 1.00 108.44 ? 48  GLU B C   1 
ATOM   4629  O O   . GLU B 1 48  ? 29.563  24.567  -26.935 1.00 107.64 ? 48  GLU B O   1 
ATOM   4630  C CB  . GLU B 1 48  ? 26.941  22.627  -26.508 1.00 113.98 ? 48  GLU B CB  1 
ATOM   4631  C CG  . GLU B 1 48  ? 27.458  22.486  -25.083 1.00 115.89 ? 48  GLU B CG  1 
ATOM   4632  C CD  . GLU B 1 48  ? 27.275  21.089  -24.540 1.00 118.55 ? 48  GLU B CD  1 
ATOM   4633  O OE1 . GLU B 1 48  ? 26.934  20.194  -25.337 1.00 118.85 ? 48  GLU B OE1 1 
ATOM   4634  O OE2 . GLU B 1 48  ? 27.447  20.910  -23.320 1.00 120.69 ? 48  GLU B OE2 1 
ATOM   4635  N N   . LEU B 1 49  ? 28.812  23.772  -28.921 1.00 106.51 ? 49  LEU B N   1 
ATOM   4636  C CA  . LEU B 1 49  ? 30.081  23.909  -29.612 1.00 103.65 ? 49  LEU B CA  1 
ATOM   4637  C C   . LEU B 1 49  ? 30.383  25.377  -29.870 1.00 102.22 ? 49  LEU B C   1 
ATOM   4638  O O   . LEU B 1 49  ? 31.535  25.788  -29.725 1.00 100.90 ? 49  LEU B O   1 
ATOM   4639  C CB  . LEU B 1 49  ? 30.117  23.120  -30.920 1.00 102.63 ? 49  LEU B CB  1 
ATOM   4640  C CG  . LEU B 1 49  ? 30.564  21.656  -30.814 1.00 103.57 ? 49  LEU B CG  1 
ATOM   4641  C CD1 . LEU B 1 49  ? 30.784  21.090  -32.210 1.00 102.17 ? 49  LEU B CD1 1 
ATOM   4642  C CD2 . LEU B 1 49  ? 31.814  21.443  -29.956 1.00 102.61 ? 49  LEU B CD2 1 
ATOM   4643  N N   . MET B 1 50  ? 29.362  26.129  -30.298 1.00 102.44 ? 50  MET B N   1 
ATOM   4644  C CA  . MET B 1 50  ? 29.528  27.546  -30.573 1.00 101.75 ? 50  MET B CA  1 
ATOM   4645  C C   . MET B 1 50  ? 30.084  28.253  -29.334 1.00 103.09 ? 50  MET B C   1 
ATOM   4646  O O   . MET B 1 50  ? 31.172  28.827  -29.415 1.00 102.36 ? 50  MET B O   1 
ATOM   4647  C CB  . MET B 1 50  ? 28.232  28.180  -31.100 1.00 102.84 ? 50  MET B CB  1 
ATOM   4648  C CG  . MET B 1 50  ? 27.987  27.906  -32.590 1.00 101.52 ? 50  MET B CG  1 
ATOM   4649  S SD  . MET B 1 50  ? 26.482  28.601  -33.320 1.00 101.61 ? 50  MET B SD  1 
ATOM   4650  C CE  . MET B 1 50  ? 27.029  30.290  -33.599 1.00 100.51 ? 50  MET B CE  1 
ATOM   4651  N N   . LYS B 1 51  ? 29.398  28.166  -28.183 1.00 105.60 ? 51  LYS B N   1 
ATOM   4652  C CA  . LYS B 1 51  ? 29.853  28.836  -26.965 1.00 107.24 ? 51  LYS B CA  1 
ATOM   4653  C C   . LYS B 1 51  ? 31.370  28.683  -26.776 1.00 105.70 ? 51  LYS B C   1 
ATOM   4654  O O   . LYS B 1 51  ? 32.066  29.648  -26.448 1.00 104.73 ? 51  LYS B O   1 
ATOM   4655  C CB  . LYS B 1 51  ? 29.140  28.351  -25.696 1.00 110.50 ? 51  LYS B CB  1 
ATOM   4656  C CG  . LYS B 1 51  ? 27.685  28.745  -25.574 1.00 113.09 ? 51  LYS B CG  1 
ATOM   4657  C CD  . LYS B 1 51  ? 26.976  28.159  -24.360 1.00 116.75 ? 51  LYS B CD  1 
ATOM   4658  C CE  . LYS B 1 51  ? 25.499  28.287  -24.527 1.00 119.25 ? 51  LYS B CE  1 
ATOM   4659  N NZ  . LYS B 1 51  ? 24.738  27.996  -23.311 1.00 123.18 ? 51  LYS B NZ  1 
ATOM   4660  N N   . PHE B 1 52  ? 31.889  27.465  -26.968 1.00 105.25 ? 52  PHE B N   1 
ATOM   4661  C CA  . PHE B 1 52  ? 33.329  27.243  -26.914 1.00 104.28 ? 52  PHE B CA  1 
ATOM   4662  C C   . PHE B 1 52  ? 34.020  28.158  -27.926 1.00 101.62 ? 52  PHE B C   1 
ATOM   4663  O O   . PHE B 1 52  ? 34.787  29.038  -27.545 1.00 101.05 ? 52  PHE B O   1 
ATOM   4664  C CB  . PHE B 1 52  ? 33.576  25.742  -27.114 1.00 104.07 ? 52  PHE B CB  1 
ATOM   4665  C CG  . PHE B 1 52  ? 35.019  25.259  -27.184 1.00 101.66 ? 52  PHE B CG  1 
ATOM   4666  C CD1 . PHE B 1 52  ? 35.756  25.017  -26.029 1.00 101.94 ? 52  PHE B CD1 1 
ATOM   4667  C CD2 . PHE B 1 52  ? 35.594  24.971  -28.417 1.00 99.25  ? 52  PHE B CD2 1 
ATOM   4668  C CE1 . PHE B 1 52  ? 37.046  24.546  -26.117 1.00 100.92 ? 52  PHE B CE1 1 
ATOM   4669  C CE2 . PHE B 1 52  ? 36.881  24.492  -28.499 1.00 97.85  ? 52  PHE B CE2 1 
ATOM   4670  C CZ  . PHE B 1 52  ? 37.606  24.287  -27.350 1.00 99.14  ? 52  PHE B CZ  1 
ATOM   4671  N N   . ASP B 1 53  ? 33.681  27.977  -29.208 1.00 100.26 ? 53  ASP B N   1 
ATOM   4672  C CA  . ASP B 1 53  ? 34.306  28.692  -30.308 1.00 97.63  ? 53  ASP B CA  1 
ATOM   4673  C C   . ASP B 1 53  ? 34.171  30.199  -30.119 1.00 98.36  ? 53  ASP B C   1 
ATOM   4674  O O   . ASP B 1 53  ? 35.118  30.944  -30.343 1.00 97.40  ? 53  ASP B O   1 
ATOM   4675  C CB  . ASP B 1 53  ? 33.715  28.272  -31.643 1.00 96.27  ? 53  ASP B CB  1 
ATOM   4676  C CG  . ASP B 1 53  ? 33.809  26.783  -31.945 1.00 96.22  ? 53  ASP B CG  1 
ATOM   4677  O OD1 . ASP B 1 53  ? 34.900  26.214  -31.724 1.00 95.25  ? 53  ASP B OD1 1 
ATOM   4678  O OD2 . ASP B 1 53  ? 32.790  26.188  -32.376 1.00 96.77  ? 53  ASP B OD2 1 
ATOM   4679  N N   . LEU B 1 54  ? 32.986  30.652  -29.717 1.00 100.90 ? 54  LEU B N   1 
ATOM   4680  C CA  . LEU B 1 54  ? 32.764  32.078  -29.558 1.00 102.26 ? 54  LEU B CA  1 
ATOM   4681  C C   . LEU B 1 54  ? 33.661  32.609  -28.438 1.00 102.88 ? 54  LEU B C   1 
ATOM   4682  O O   . LEU B 1 54  ? 34.159  33.731  -28.526 1.00 102.26 ? 54  LEU B O   1 
ATOM   4683  C CB  . LEU B 1 54  ? 31.285  32.396  -29.311 1.00 105.05 ? 54  LEU B CB  1 
ATOM   4684  C CG  . LEU B 1 54  ? 30.361  32.461  -30.537 1.00 105.11 ? 54  LEU B CG  1 
ATOM   4685  C CD1 . LEU B 1 54  ? 30.800  33.442  -31.616 1.00 103.26 ? 54  LEU B CD1 1 
ATOM   4686  C CD2 . LEU B 1 54  ? 30.178  31.103  -31.169 1.00 105.13 ? 54  LEU B CD2 1 
ATOM   4687  N N   . GLU B 1 55  ? 33.873  31.799  -27.393 1.00 104.39 ? 55  GLU B N   1 
ATOM   4688  C CA  . GLU B 1 55  ? 34.638  32.243  -26.238 1.00 106.17 ? 55  GLU B CA  1 
ATOM   4689  C C   . GLU B 1 55  ? 36.133  32.242  -26.572 1.00 104.46 ? 55  GLU B C   1 
ATOM   4690  O O   . GLU B 1 55  ? 36.855  33.159  -26.185 1.00 104.32 ? 55  GLU B O   1 
ATOM   4691  C CB  . GLU B 1 55  ? 34.292  31.396  -25.012 1.00 109.12 ? 55  GLU B CB  1 
ATOM   4692  C CG  . GLU B 1 55  ? 34.723  32.037  -23.694 1.00 111.63 ? 55  GLU B CG  1 
ATOM   4693  C CD  . GLU B 1 55  ? 34.104  33.406  -23.415 1.00 114.33 ? 55  GLU B CD  1 
ATOM   4694  O OE1 . GLU B 1 55  ? 32.861  33.514  -23.187 1.00 114.61 ? 55  GLU B OE1 1 
ATOM   4695  O OE2 . GLU B 1 55  ? 34.895  34.383  -23.435 1.00 114.72 ? 55  GLU B OE2 1 
ATOM   4696  N N   . ASN B 1 56  ? 36.587  31.201  -27.287 1.00 102.55 ? 56  ASN B N   1 
ATOM   4697  C CA  . ASN B 1 56  ? 37.954  31.114  -27.769 1.00 100.08 ? 56  ASN B CA  1 
ATOM   4698  C C   . ASN B 1 56  ? 38.258  32.342  -28.615 1.00 98.91  ? 56  ASN B C   1 
ATOM   4699  O O   . ASN B 1 56  ? 39.239  33.038  -28.365 1.00 99.13  ? 56  ASN B O   1 
ATOM   4700  C CB  . ASN B 1 56  ? 38.201  29.839  -28.570 1.00 98.97  ? 56  ASN B CB  1 
ATOM   4701  C CG  . ASN B 1 56  ? 38.400  28.617  -27.696 1.00 101.16 ? 56  ASN B CG  1 
ATOM   4702  O OD1 . ASN B 1 56  ? 38.790  28.728  -26.526 1.00 103.32 ? 56  ASN B OD1 1 
ATOM   4703  N ND2 . ASN B 1 56  ? 38.181  27.431  -28.250 1.00 100.69 ? 56  ASN B ND2 1 
ATOM   4704  N N   . ILE B 1 57  ? 37.381  32.611  -29.589 1.00 98.06  ? 57  ILE B N   1 
ATOM   4705  C CA  . ILE B 1 57  ? 37.596  33.668  -30.567 1.00 96.30  ? 57  ILE B CA  1 
ATOM   4706  C C   . ILE B 1 57  ? 37.719  35.030  -29.872 1.00 97.69  ? 57  ILE B C   1 
ATOM   4707  O O   . ILE B 1 57  ? 38.472  35.886  -30.334 1.00 95.82  ? 57  ILE B O   1 
ATOM   4708  C CB  . ILE B 1 57  ? 36.495  33.641  -31.647 1.00 95.03  ? 57  ILE B CB  1 
ATOM   4709  C CG1 . ILE B 1 57  ? 36.591  32.375  -32.507 1.00 92.82  ? 57  ILE B CG1 1 
ATOM   4710  C CG2 . ILE B 1 57  ? 36.542  34.901  -32.514 1.00 94.08  ? 57  ILE B CG2 1 
ATOM   4711  C CD1 . ILE B 1 57  ? 35.339  32.065  -33.305 1.00 92.61  ? 57  ILE B CD1 1 
ATOM   4712  N N   . LYS B 1 58  ? 36.993  35.238  -28.765 1.00 100.12 ? 58  LYS B N   1 
ATOM   4713  C CA  . LYS B 1 58  ? 37.183  36.432  -27.952 1.00 100.59 ? 58  LYS B CA  1 
ATOM   4714  C C   . LYS B 1 58  ? 38.593  36.461  -27.357 1.00 99.37  ? 58  LYS B C   1 
ATOM   4715  O O   . LYS B 1 58  ? 39.225  37.509  -27.380 1.00 99.56  ? 58  LYS B O   1 
ATOM   4716  C CB  . LYS B 1 58  ? 36.140  36.544  -26.840 1.00 103.29 ? 58  LYS B CB  1 
ATOM   4717  C CG  . LYS B 1 58  ? 34.762  36.920  -27.349 1.00 105.29 ? 58  LYS B CG  1 
ATOM   4718  C CD  . LYS B 1 58  ? 33.615  36.671  -26.369 1.00 108.53 ? 58  LYS B CD  1 
ATOM   4719  C CE  . LYS B 1 58  ? 33.725  37.435  -25.079 1.00 110.56 ? 58  LYS B CE  1 
ATOM   4720  N NZ  . LYS B 1 58  ? 32.935  36.791  -24.027 1.00 112.88 ? 58  LYS B NZ  1 
ATOM   4721  N N   . GLU B 1 59  ? 39.088  35.324  -26.837 1.00 98.33  ? 59  GLU B N   1 
ATOM   4722  C CA  . GLU B 1 59  ? 40.383  35.273  -26.164 1.00 98.01  ? 59  GLU B CA  1 
ATOM   4723  C C   . GLU B 1 59  ? 41.527  35.395  -27.168 1.00 95.72  ? 59  GLU B C   1 
ATOM   4724  O O   . GLU B 1 59  ? 42.661  35.701  -26.800 1.00 93.45  ? 59  GLU B O   1 
ATOM   4725  C CB  . GLU B 1 59  ? 40.617  33.980  -25.387 1.00 98.65  ? 59  GLU B CB  1 
ATOM   4726  C CG  . GLU B 1 59  ? 39.705  33.820  -24.177 1.00 101.66 ? 59  GLU B CG  1 
ATOM   4727  C CD  . GLU B 1 59  ? 40.036  32.625  -23.308 1.00 102.84 ? 59  GLU B CD  1 
ATOM   4728  O OE1 . GLU B 1 59  ? 41.192  32.126  -23.375 1.00 102.20 ? 59  GLU B OE1 1 
ATOM   4729  O OE2 . GLU B 1 59  ? 39.112  32.183  -22.583 1.00 104.37 ? 59  GLU B OE2 1 
ATOM   4730  N N   . GLY B 1 60  ? 41.205  35.130  -28.437 1.00 95.40  ? 60  GLY B N   1 
ATOM   4731  C CA  . GLY B 1 60  ? 42.145  35.282  -29.532 1.00 93.59  ? 60  GLY B CA  1 
ATOM   4732  C C   . GLY B 1 60  ? 42.378  36.748  -29.881 1.00 94.84  ? 60  GLY B C   1 
ATOM   4733  O O   . GLY B 1 60  ? 43.409  37.069  -30.469 1.00 97.33  ? 60  GLY B O   1 
ATOM   4734  N N   . GLY B 1 61  ? 41.415  37.621  -29.542 1.00 95.44  ? 61  GLY B N   1 
ATOM   4735  C CA  . GLY B 1 61  ? 41.579  39.060  -29.688 1.00 95.19  ? 61  GLY B CA  1 
ATOM   4736  C C   . GLY B 1 61  ? 40.695  39.654  -30.785 1.00 94.39  ? 61  GLY B C   1 
ATOM   4737  O O   . GLY B 1 61  ? 40.736  40.860  -31.043 1.00 95.48  ? 61  GLY B O   1 
ATOM   4738  N N   . TYR B 1 62  ? 39.883  38.803  -31.415 1.00 92.94  ? 62  TYR B N   1 
ATOM   4739  C CA  . TYR B 1 62  ? 38.991  39.216  -32.489 1.00 91.64  ? 62  TYR B CA  1 
ATOM   4740  C C   . TYR B 1 62  ? 37.823  39.976  -31.862 1.00 91.86  ? 62  TYR B C   1 
ATOM   4741  O O   . TYR B 1 62  ? 37.643  39.907  -30.650 1.00 91.96  ? 62  TYR B O   1 
ATOM   4742  C CB  . TYR B 1 62  ? 38.638  37.954  -33.296 1.00 90.91  ? 62  TYR B CB  1 
ATOM   4743  C CG  . TYR B 1 62  ? 39.856  37.148  -33.743 1.00 89.12  ? 62  TYR B CG  1 
ATOM   4744  C CD1 . TYR B 1 62  ? 40.403  36.168  -32.929 1.00 89.29  ? 62  TYR B CD1 1 
ATOM   4745  C CD2 . TYR B 1 62  ? 40.481  37.397  -34.958 1.00 88.18  ? 62  TYR B CD2 1 
ATOM   4746  C CE1 . TYR B 1 62  ? 41.526  35.457  -33.308 1.00 88.75  ? 62  TYR B CE1 1 
ATOM   4747  C CE2 . TYR B 1 62  ? 41.606  36.691  -35.352 1.00 87.48  ? 62  TYR B CE2 1 
ATOM   4748  C CZ  . TYR B 1 62  ? 42.138  35.722  -34.519 1.00 88.16  ? 62  TYR B CZ  1 
ATOM   4749  O OH  . TYR B 1 62  ? 43.257  35.009  -34.860 1.00 89.01  ? 62  TYR B OH  1 
ATOM   4750  N N   . ASN B 1 63  ? 37.096  40.746  -32.690 1.00 91.37  ? 63  ASN B N   1 
ATOM   4751  C CA  . ASN B 1 63  ? 35.903  41.474  -32.280 1.00 93.13  ? 63  ASN B CA  1 
ATOM   4752  C C   . ASN B 1 63  ? 34.742  41.234  -33.249 1.00 94.29  ? 63  ASN B C   1 
ATOM   4753  O O   . ASN B 1 63  ? 33.646  41.782  -33.055 1.00 96.40  ? 63  ASN B O   1 
ATOM   4754  C CB  . ASN B 1 63  ? 36.171  42.971  -32.174 1.00 93.46  ? 63  ASN B CB  1 
ATOM   4755  C CG  . ASN B 1 63  ? 36.370  43.635  -33.518 1.00 91.79  ? 63  ASN B CG  1 
ATOM   4756  O OD1 . ASN B 1 63  ? 36.292  42.980  -34.568 1.00 89.65  ? 63  ASN B OD1 1 
ATOM   4757  N ND2 . ASN B 1 63  ? 36.646  44.933  -33.497 1.00 92.35  ? 63  ASN B ND2 1 
ATOM   4758  N N   . THR B 1 64  ? 34.989  40.439  -34.302 1.00 93.02  ? 64  THR B N   1 
ATOM   4759  C CA  . THR B 1 64  ? 33.980  40.135  -35.305 1.00 93.61  ? 64  THR B CA  1 
ATOM   4760  C C   . THR B 1 64  ? 34.168  38.701  -35.798 1.00 91.56  ? 64  THR B C   1 
ATOM   4761  O O   . THR B 1 64  ? 35.225  38.106  -35.616 1.00 90.11  ? 64  THR B O   1 
ATOM   4762  C CB  . THR B 1 64  ? 34.069  41.154  -36.443 1.00 94.31  ? 64  THR B CB  1 
ATOM   4763  O OG1 . THR B 1 64  ? 33.869  42.430  -35.837 1.00 98.32  ? 64  THR B OG1 1 
ATOM   4764  C CG2 . THR B 1 64  ? 32.985  40.978  -37.495 1.00 94.52  ? 64  THR B CG2 1 
ATOM   4765  N N   . ILE B 1 65  ? 33.106  38.134  -36.385 1.00 91.59  ? 65  ILE B N   1 
ATOM   4766  C CA  . ILE B 1 65  ? 33.202  36.869  -37.100 1.00 89.21  ? 65  ILE B CA  1 
ATOM   4767  C C   . ILE B 1 65  ? 32.573  37.032  -38.486 1.00 87.81  ? 65  ILE B C   1 
ATOM   4768  O O   . ILE B 1 65  ? 31.851  37.988  -38.754 1.00 88.91  ? 65  ILE B O   1 
ATOM   4769  C CB  . ILE B 1 65  ? 32.567  35.709  -36.304 1.00 90.08  ? 65  ILE B CB  1 
ATOM   4770  C CG1 . ILE B 1 65  ? 31.085  36.003  -35.912 1.00 91.38  ? 65  ILE B CG1 1 
ATOM   4771  C CG2 . ILE B 1 65  ? 33.443  35.348  -35.094 1.00 89.79  ? 65  ILE B CG2 1 
ATOM   4772  C CD1 . ILE B 1 65  ? 30.300  34.778  -35.475 1.00 92.02  ? 65  ILE B CD1 1 
ATOM   4773  N N   . ARG B 1 66  ? 32.937  36.119  -39.384 1.00 85.30  ? 66  ARG B N   1 
ATOM   4774  C CA  . ARG B 1 66  ? 32.444  36.171  -40.779 1.00 83.57  ? 66  ARG B CA  1 
ATOM   4775  C C   . ARG B 1 66  ? 31.944  34.772  -41.134 1.00 82.82  ? 66  ARG B C   1 
ATOM   4776  O O   . ARG B 1 66  ? 32.543  33.800  -40.641 1.00 81.73  ? 66  ARG B O   1 
ATOM   4777  C CB  . ARG B 1 66  ? 33.559  36.591  -41.737 1.00 81.62  ? 66  ARG B CB  1 
ATOM   4778  C CG  . ARG B 1 66  ? 33.219  36.560  -43.219 1.00 80.48  ? 66  ARG B CG  1 
ATOM   4779  C CD  . ARG B 1 66  ? 33.892  35.399  -43.921 1.00 79.28  ? 66  ARG B CD  1 
ATOM   4780  N NE  . ARG B 1 66  ? 34.224  35.722  -45.311 1.00 77.97  ? 66  ARG B NE  1 
ATOM   4781  C CZ  . ARG B 1 66  ? 33.573  35.251  -46.359 1.00 78.29  ? 66  ARG B CZ  1 
ATOM   4782  N NH1 . ARG B 1 66  ? 32.343  34.797  -46.218 1.00 80.01  ? 66  ARG B NH1 1 
ATOM   4783  N NH2 . ARG B 1 66  ? 34.150  35.232  -47.543 1.00 77.16  ? 66  ARG B NH2 1 
ATOM   4784  N N   . THR B 1 67  ? 30.885  34.680  -41.940 1.00 82.87  ? 67  THR B N   1 
ATOM   4785  C CA  . THR B 1 67  ? 30.290  33.371  -42.247 1.00 82.51  ? 67  THR B CA  1 
ATOM   4786  C C   . THR B 1 67  ? 30.003  33.283  -43.720 1.00 81.72  ? 67  THR B C   1 
ATOM   4787  O O   . THR B 1 67  ? 30.127  34.309  -44.404 1.00 81.57  ? 67  THR B O   1 
ATOM   4788  C CB  . THR B 1 67  ? 29.037  33.194  -41.401 1.00 83.98  ? 67  THR B CB  1 
ATOM   4789  O OG1 . THR B 1 67  ? 29.178  33.987  -40.228 1.00 84.19  ? 67  THR B OG1 1 
ATOM   4790  C CG2 . THR B 1 67  ? 28.853  31.752  -40.967 1.00 84.81  ? 67  THR B CG2 1 
ATOM   4791  N N   . TRP B 1 68  ? 29.682  32.085  -44.202 1.00 81.11  ? 68  TRP B N   1 
ATOM   4792  C CA  . TRP B 1 68  ? 29.355  31.874  -45.632 1.00 80.43  ? 68  TRP B CA  1 
ATOM   4793  C C   . TRP B 1 68  ? 27.930  31.341  -45.707 1.00 82.31  ? 68  TRP B C   1 
ATOM   4794  O O   . TRP B 1 68  ? 27.478  31.000  -46.819 1.00 82.53  ? 68  TRP B O   1 
ATOM   4795  C CB  . TRP B 1 68  ? 30.335  30.860  -46.239 1.00 78.52  ? 68  TRP B CB  1 
ATOM   4796  C CG  . TRP B 1 68  ? 31.773  31.297  -46.322 1.00 77.02  ? 68  TRP B CG  1 
ATOM   4797  C CD1 . TRP B 1 68  ? 32.438  31.684  -47.447 1.00 75.74  ? 68  TRP B CD1 1 
ATOM   4798  C CD2 . TRP B 1 68  ? 32.735  31.357  -45.247 1.00 76.72  ? 68  TRP B CD2 1 
ATOM   4799  N NE1 . TRP B 1 68  ? 33.735  31.997  -47.148 1.00 74.54  ? 68  TRP B NE1 1 
ATOM   4800  C CE2 . TRP B 1 68  ? 33.947  31.805  -45.809 1.00 74.92  ? 68  TRP B CE2 1 
ATOM   4801  C CE3 . TRP B 1 68  ? 32.692  31.083  -43.876 1.00 77.75  ? 68  TRP B CE3 1 
ATOM   4802  C CZ2 . TRP B 1 68  ? 35.096  31.985  -45.046 1.00 74.10  ? 68  TRP B CZ2 1 
ATOM   4803  C CZ3 . TRP B 1 68  ? 33.828  31.264  -43.123 1.00 76.86  ? 68  TRP B CZ3 1 
ATOM   4804  C CH2 . TRP B 1 68  ? 35.013  31.707  -43.702 1.00 74.91  ? 68  TRP B CH2 1 
ATOM   4805  N N   . SER B 1 69  ? 27.235  31.308  -44.569 1.00 83.49  ? 69  SER B N   1 
ATOM   4806  C CA  . SER B 1 69  ? 25.926  30.698  -44.501 1.00 85.09  ? 69  SER B CA  1 
ATOM   4807  C C   . SER B 1 69  ? 25.102  31.381  -43.413 1.00 87.13  ? 69  SER B C   1 
ATOM   4808  O O   . SER B 1 69  ? 25.629  31.829  -42.392 1.00 86.76  ? 69  SER B O   1 
ATOM   4809  C CB  . SER B 1 69  ? 26.076  29.229  -44.272 1.00 85.08  ? 69  SER B CB  1 
ATOM   4810  O OG  . SER B 1 69  ? 24.821  28.604  -44.090 1.00 87.24  ? 69  SER B OG  1 
ATOM   4811  N N   . GLN B 1 70  ? 23.789  31.473  -43.655 1.00 89.25  ? 70  GLN B N   1 
ATOM   4812  C CA  . GLN B 1 70  ? 22.911  32.220  -42.773 1.00 91.40  ? 70  GLN B CA  1 
ATOM   4813  C C   . GLN B 1 70  ? 22.757  31.446  -41.465 1.00 93.45  ? 70  GLN B C   1 
ATOM   4814  O O   . GLN B 1 70  ? 22.587  30.238  -41.473 1.00 93.84  ? 70  GLN B O   1 
ATOM   4815  C CB  . GLN B 1 70  ? 21.587  32.581  -43.454 1.00 92.71  ? 70  GLN B CB  1 
ATOM   4816  C CG  . GLN B 1 70  ? 20.809  31.417  -44.063 1.00 93.43  ? 70  GLN B CG  1 
ATOM   4817  C CD  . GLN B 1 70  ? 21.056  31.182  -45.541 1.00 91.88  ? 70  GLN B CD  1 
ATOM   4818  O OE1 . GLN B 1 70  ? 22.011  31.698  -46.131 1.00 89.68  ? 70  GLN B OE1 1 
ATOM   4819  N NE2 . GLN B 1 70  ? 20.198  30.372  -46.152 1.00 92.96  ? 70  GLN B NE2 1 
ATOM   4820  N N   . TYR B 1 71  ? 22.885  32.145  -40.336 1.00 95.34  ? 71  TYR B N   1 
ATOM   4821  C CA  . TYR B 1 71  ? 22.622  31.553  -39.038 1.00 97.91  ? 71  TYR B CA  1 
ATOM   4822  C C   . TYR B 1 71  ? 21.117  31.589  -38.791 1.00 101.74 ? 71  TYR B C   1 
ATOM   4823  O O   . TYR B 1 71  ? 20.433  32.498  -39.266 1.00 102.55 ? 71  TYR B O   1 
ATOM   4824  C CB  . TYR B 1 71  ? 23.319  32.322  -37.913 1.00 98.23  ? 71  TYR B CB  1 
ATOM   4825  C CG  . TYR B 1 71  ? 24.822  32.138  -37.765 1.00 96.62  ? 71  TYR B CG  1 
ATOM   4826  C CD1 . TYR B 1 71  ? 25.451  30.960  -38.145 1.00 95.85  ? 71  TYR B CD1 1 
ATOM   4827  C CD2 . TYR B 1 71  ? 25.606  33.128  -37.185 1.00 96.01  ? 71  TYR B CD2 1 
ATOM   4828  C CE1 . TYR B 1 71  ? 26.818  30.790  -37.995 1.00 94.16  ? 71  TYR B CE1 1 
ATOM   4829  C CE2 . TYR B 1 71  ? 26.972  32.967  -37.019 1.00 94.45  ? 71  TYR B CE2 1 
ATOM   4830  C CZ  . TYR B 1 71  ? 27.584  31.793  -37.428 1.00 93.30  ? 71  TYR B CZ  1 
ATOM   4831  O OH  . TYR B 1 71  ? 28.926  31.571  -37.284 1.00 91.32  ? 71  TYR B OH  1 
ATOM   4832  N N   . SER B 1 72  ? 20.622  30.585  -38.046 1.00 104.05 ? 72  SER B N   1 
ATOM   4833  C CA  . SER B 1 72  ? 19.251  30.531  -37.557 1.00 106.03 ? 72  SER B CA  1 
ATOM   4834  C C   . SER B 1 72  ? 19.067  31.532  -36.419 1.00 108.21 ? 72  SER B C   1 
ATOM   4835  O O   . SER B 1 72  ? 20.035  31.959  -35.798 1.00 107.36 ? 72  SER B O   1 
ATOM   4836  C CB  . SER B 1 72  ? 18.923  29.146  -37.075 1.00 106.86 ? 72  SER B CB  1 
ATOM   4837  O OG  . SER B 1 72  ? 19.526  28.905  -35.809 1.00 106.70 ? 72  SER B OG  1 
ATOM   4838  N N   . GLU B 1 73  ? 17.810  31.849  -36.091 1.00 111.97 ? 73  GLU B N   1 
ATOM   4839  C CA  . GLU B 1 73  ? 17.523  32.811  -35.040 1.00 113.92 ? 73  GLU B CA  1 
ATOM   4840  C C   . GLU B 1 73  ? 18.195  32.396  -33.730 1.00 113.95 ? 73  GLU B C   1 
ATOM   4841  O O   . GLU B 1 73  ? 18.725  33.246  -33.012 1.00 113.80 ? 73  GLU B O   1 
ATOM   4842  C CB  . GLU B 1 73  ? 16.018  32.947  -34.828 1.00 117.61 ? 73  GLU B CB  1 
ATOM   4843  C CG  . GLU B 1 73  ? 15.661  34.130  -33.935 1.00 119.95 ? 73  GLU B CG  1 
ATOM   4844  C CD  . GLU B 1 73  ? 14.169  34.274  -33.788 1.00 123.80 ? 73  GLU B CD  1 
ATOM   4845  O OE1 . GLU B 1 73  ? 13.480  33.352  -34.276 1.00 124.66 ? 73  GLU B OE1 1 
ATOM   4846  O OE2 . GLU B 1 73  ? 13.705  35.281  -33.210 1.00 126.91 ? 73  GLU B OE2 1 
ATOM   4847  N N   . ASN B 1 74  ? 18.147  31.087  -33.434 1.00 113.99 ? 74  ASN B N   1 
ATOM   4848  C CA  . ASN B 1 74  ? 18.717  30.524  -32.219 1.00 113.51 ? 74  ASN B CA  1 
ATOM   4849  C C   . ASN B 1 74  ? 20.205  30.832  -32.158 1.00 109.75 ? 74  ASN B C   1 
ATOM   4850  O O   . ASN B 1 74  ? 20.696  31.216  -31.106 1.00 109.99 ? 74  ASN B O   1 
ATOM   4851  C CB  . ASN B 1 74  ? 18.512  29.014  -32.112 1.00 114.32 ? 74  ASN B CB  1 
ATOM   4852  C CG  . ASN B 1 74  ? 17.061  28.600  -32.215 1.00 116.35 ? 74  ASN B CG  1 
ATOM   4853  O OD1 . ASN B 1 74  ? 16.191  29.277  -31.660 1.00 118.94 ? 74  ASN B OD1 1 
ATOM   4854  N ND2 . ASN B 1 74  ? 16.778  27.516  -32.928 1.00 115.81 ? 74  ASN B ND2 1 
ATOM   4855  N N   . GLN B 1 75  ? 20.891  30.667  -33.296 1.00 106.72 ? 75  GLN B N   1 
ATOM   4856  C CA  . GLN B 1 75  ? 22.335  30.868  -33.381 1.00 104.09 ? 75  GLN B CA  1 
ATOM   4857  C C   . GLN B 1 75  ? 22.651  32.352  -33.168 1.00 104.15 ? 75  GLN B C   1 
ATOM   4858  O O   . GLN B 1 75  ? 23.530  32.683  -32.376 1.00 104.08 ? 75  GLN B O   1 
ATOM   4859  C CB  . GLN B 1 75  ? 22.914  30.266  -34.673 1.00 100.89 ? 75  GLN B CB  1 
ATOM   4860  C CG  . GLN B 1 75  ? 22.978  28.734  -34.697 1.00 100.59 ? 75  GLN B CG  1 
ATOM   4861  C CD  . GLN B 1 75  ? 23.207  28.124  -36.070 1.00 98.50  ? 75  GLN B CD  1 
ATOM   4862  O OE1 . GLN B 1 75  ? 22.577  28.516  -37.059 1.00 97.98  ? 75  GLN B OE1 1 
ATOM   4863  N NE2 . GLN B 1 75  ? 24.096  27.141  -36.155 1.00 97.12  ? 75  GLN B NE2 1 
ATOM   4864  N N   . LEU B 1 76  ? 21.905  33.238  -33.839 1.00 105.08 ? 76  LEU B N   1 
ATOM   4865  C CA  . LEU B 1 76  ? 22.111  34.679  -33.738 1.00 105.75 ? 76  LEU B CA  1 
ATOM   4866  C C   . LEU B 1 76  ? 22.044  35.154  -32.291 1.00 107.89 ? 76  LEU B C   1 
ATOM   4867  O O   . LEU B 1 76  ? 22.735  36.100  -31.933 1.00 108.24 ? 76  LEU B O   1 
ATOM   4868  C CB  . LEU B 1 76  ? 21.096  35.481  -34.548 1.00 107.19 ? 76  LEU B CB  1 
ATOM   4869  C CG  . LEU B 1 76  ? 21.442  35.752  -36.014 1.00 105.71 ? 76  LEU B CG  1 
ATOM   4870  C CD1 . LEU B 1 76  ? 21.315  34.483  -36.819 1.00 105.12 ? 76  LEU B CD1 1 
ATOM   4871  C CD2 . LEU B 1 76  ? 20.522  36.838  -36.558 1.00 107.10 ? 76  LEU B CD2 1 
ATOM   4872  N N   . LYS B 1 77  ? 21.156  34.565  -31.488 1.00 110.52 ? 77  LYS B N   1 
ATOM   4873  C CA  . LYS B 1 77  ? 20.989  34.999  -30.109 1.00 112.93 ? 77  LYS B CA  1 
ATOM   4874  C C   . LYS B 1 77  ? 22.298  34.776  -29.356 1.00 111.52 ? 77  LYS B C   1 
ATOM   4875  O O   . LYS B 1 77  ? 22.705  35.601  -28.541 1.00 112.16 ? 77  LYS B O   1 
ATOM   4876  C CB  . LYS B 1 77  ? 19.827  34.288  -29.403 1.00 115.94 ? 77  LYS B CB  1 
ATOM   4877  C CG  . LYS B 1 77  ? 18.437  34.715  -29.840 1.00 118.39 ? 77  LYS B CG  1 
ATOM   4878  C CD  . LYS B 1 77  ? 17.323  33.874  -29.225 1.00 121.76 ? 77  LYS B CD  1 
ATOM   4879  C CE  . LYS B 1 77  ? 16.027  34.030  -29.941 1.00 123.65 ? 77  LYS B CE  1 
ATOM   4880  N NZ  . LYS B 1 77  ? 15.042  33.047  -29.485 1.00 127.04 ? 77  LYS B NZ  1 
ATOM   4881  N N   . LEU B 1 78  ? 22.949  33.645  -29.635 1.00 109.80 ? 78  LEU B N   1 
ATOM   4882  C CA  . LEU B 1 78  ? 24.164  33.280  -28.932 1.00 109.12 ? 78  LEU B CA  1 
ATOM   4883  C C   . LEU B 1 78  ? 25.261  34.264  -29.317 1.00 107.48 ? 78  LEU B C   1 
ATOM   4884  O O   . LEU B 1 78  ? 25.988  34.762  -28.460 1.00 106.87 ? 78  LEU B O   1 
ATOM   4885  C CB  . LEU B 1 78  ? 24.525  31.841  -29.294 1.00 107.56 ? 78  LEU B CB  1 
ATOM   4886  C CG  . LEU B 1 78  ? 25.713  31.226  -28.551 1.00 106.24 ? 78  LEU B CG  1 
ATOM   4887  C CD1 . LEU B 1 78  ? 25.653  31.406  -27.044 1.00 108.52 ? 78  LEU B CD1 1 
ATOM   4888  C CD2 . LEU B 1 78  ? 25.760  29.758  -28.916 1.00 105.63 ? 78  LEU B CD2 1 
ATOM   4889  N N   . VAL B 1 79  ? 25.326  34.550  -30.619 1.00 106.79 ? 79  VAL B N   1 
ATOM   4890  C CA  . VAL B 1 79  ? 26.263  35.519  -31.144 1.00 106.68 ? 79  VAL B CA  1 
ATOM   4891  C C   . VAL B 1 79  ? 25.996  36.865  -30.480 1.00 109.40 ? 79  VAL B C   1 
ATOM   4892  O O   . VAL B 1 79  ? 26.902  37.476  -29.919 1.00 109.85 ? 79  VAL B O   1 
ATOM   4893  C CB  . VAL B 1 79  ? 26.173  35.608  -32.678 1.00 106.02 ? 79  VAL B CB  1 
ATOM   4894  C CG1 . VAL B 1 79  ? 27.092  36.696  -33.224 1.00 105.10 ? 79  VAL B CG1 1 
ATOM   4895  C CG2 . VAL B 1 79  ? 26.508  34.274  -33.344 1.00 104.71 ? 79  VAL B CG2 1 
ATOM   4896  N N   . GLN B 1 80  ? 24.739  37.310  -30.543 1.00 112.58 ? 80  GLN B N   1 
ATOM   4897  C CA  . GLN B 1 80  ? 24.314  38.544  -29.902 1.00 115.19 ? 80  GLN B CA  1 
ATOM   4898  C C   . GLN B 1 80  ? 24.856  38.609  -28.474 1.00 117.47 ? 80  GLN B C   1 
ATOM   4899  O O   . GLN B 1 80  ? 25.432  39.615  -28.069 1.00 117.76 ? 80  GLN B O   1 
ATOM   4900  C CB  . GLN B 1 80  ? 22.786  38.628  -29.893 1.00 117.32 ? 80  GLN B CB  1 
ATOM   4901  C CG  . GLN B 1 80  ? 22.244  40.027  -29.630 1.00 119.55 ? 80  GLN B CG  1 
ATOM   4902  C CD  . GLN B 1 80  ? 22.637  41.022  -30.702 1.00 118.61 ? 80  GLN B CD  1 
ATOM   4903  O OE1 . GLN B 1 80  ? 22.491  40.767  -31.905 1.00 116.97 ? 80  GLN B OE1 1 
ATOM   4904  N NE2 . GLN B 1 80  ? 23.168  42.163  -30.283 1.00 119.51 ? 80  GLN B NE2 1 
ATOM   4905  N N   . GLU B 1 81  ? 24.675  37.516  -27.726 1.00 119.91 ? 81  GLU B N   1 
ATOM   4906  C CA  . GLU B 1 81  ? 24.975  37.487  -26.303 1.00 123.02 ? 81  GLU B CA  1 
ATOM   4907  C C   . GLU B 1 81  ? 26.484  37.483  -26.054 1.00 120.65 ? 81  GLU B C   1 
ATOM   4908  O O   . GLU B 1 81  ? 26.932  37.970  -25.020 1.00 121.83 ? 81  GLU B O   1 
ATOM   4909  C CB  . GLU B 1 81  ? 24.314  36.263  -25.667 1.00 126.11 ? 81  GLU B CB  1 
ATOM   4910  C CG  . GLU B 1 81  ? 24.313  36.288  -24.139 1.00 129.91 ? 81  GLU B CG  1 
ATOM   4911  C CD  . GLU B 1 81  ? 23.777  35.023  -23.486 1.00 132.68 ? 81  GLU B CD  1 
ATOM   4912  O OE1 . GLU B 1 81  ? 24.538  34.030  -23.470 1.00 131.91 ? 81  GLU B OE1 1 
ATOM   4913  O OE2 . GLU B 1 81  ? 22.615  35.013  -23.010 1.00 135.51 ? 81  GLU B OE2 1 
ATOM   4914  N N   . SER B 1 82  ? 27.265  36.934  -26.993 1.00 117.30 ? 82  SER B N   1 
ATOM   4915  C CA  . SER B 1 82  ? 28.704  36.779  -26.814 1.00 114.76 ? 82  SER B CA  1 
ATOM   4916  C C   . SER B 1 82  ? 29.399  38.137  -26.709 1.00 113.70 ? 82  SER B C   1 
ATOM   4917  O O   . SER B 1 82  ? 30.379  38.282  -25.975 1.00 112.77 ? 82  SER B O   1 
ATOM   4918  C CB  . SER B 1 82  ? 29.288  35.974  -27.942 1.00 112.00 ? 82  SER B CB  1 
ATOM   4919  O OG  . SER B 1 82  ? 29.174  36.683  -29.170 1.00 110.83 ? 82  SER B OG  1 
ATOM   4920  N N   . GLY B 1 83  ? 28.885  39.114  -27.469 1.00 112.82 ? 83  GLY B N   1 
ATOM   4921  C CA  . GLY B 1 83  ? 29.506  40.420  -27.597 1.00 112.18 ? 83  GLY B CA  1 
ATOM   4922  C C   . GLY B 1 83  ? 30.060  40.633  -29.003 1.00 109.02 ? 83  GLY B C   1 
ATOM   4923  O O   . GLY B 1 83  ? 30.227  41.767  -29.439 1.00 109.20 ? 83  GLY B O   1 
ATOM   4924  N N   . LEU B 1 84  ? 30.312  39.538  -29.724 1.00 106.32 ? 84  LEU B N   1 
ATOM   4925  C CA  . LEU B 1 84  ? 30.965  39.609  -31.021 1.00 103.95 ? 84  LEU B CA  1 
ATOM   4926  C C   . LEU B 1 84  ? 30.014  40.160  -32.075 1.00 104.26 ? 84  LEU B C   1 
ATOM   4927  O O   . LEU B 1 84  ? 28.836  39.828  -32.055 1.00 107.17 ? 84  LEU B O   1 
ATOM   4928  C CB  . LEU B 1 84  ? 31.431  38.211  -31.405 1.00 102.13 ? 84  LEU B CB  1 
ATOM   4929  C CG  . LEU B 1 84  ? 32.655  37.704  -30.644 1.00 102.10 ? 84  LEU B CG  1 
ATOM   4930  C CD1 . LEU B 1 84  ? 32.821  36.202  -30.784 1.00 101.19 ? 84  LEU B CD1 1 
ATOM   4931  C CD2 . LEU B 1 84  ? 33.909  38.427  -31.136 1.00 100.95 ? 84  LEU B CD2 1 
ATOM   4932  N N   . LYS B 1 85  ? 30.555  40.974  -32.996 1.00 102.66 ? 85  LYS B N   1 
ATOM   4933  C CA  . LYS B 1 85  ? 29.848  41.406  -34.193 1.00 101.69 ? 85  LYS B CA  1 
ATOM   4934  C C   . LYS B 1 85  ? 29.958  40.322  -35.263 1.00 98.58  ? 85  LYS B C   1 
ATOM   4935  O O   . LYS B 1 85  ? 30.765  39.401  -35.143 1.00 98.24  ? 85  LYS B O   1 
ATOM   4936  C CB  . LYS B 1 85  ? 30.413  42.705  -34.778 1.00 102.00 ? 85  LYS B CB  1 
ATOM   4937  C CG  . LYS B 1 85  ? 30.620  43.854  -33.798 1.00 104.35 ? 85  LYS B CG  1 
ATOM   4938  C CD  . LYS B 1 85  ? 29.416  44.226  -32.937 1.00 107.41 ? 85  LYS B CD  1 
ATOM   4939  C CE  . LYS B 1 85  ? 29.701  45.393  -32.030 1.00 109.39 ? 85  LYS B CE  1 
ATOM   4940  N NZ  . LYS B 1 85  ? 28.571  45.714  -31.152 1.00 112.63 ? 85  LYS B NZ  1 
ATOM   4941  N N   . LEU B 1 86  ? 29.164  40.465  -36.327 1.00 97.10  ? 86  LEU B N   1 
ATOM   4942  C CA  . LEU B 1 86  ? 28.939  39.385  -37.270 1.00 95.36  ? 86  LEU B CA  1 
ATOM   4943  C C   . LEU B 1 86  ? 28.924  39.954  -38.681 1.00 93.25  ? 86  LEU B C   1 
ATOM   4944  O O   . LEU B 1 86  ? 28.329  40.995  -38.917 1.00 95.15  ? 86  LEU B O   1 
ATOM   4945  C CB  . LEU B 1 86  ? 27.601  38.727  -36.917 1.00 97.80  ? 86  LEU B CB  1 
ATOM   4946  C CG  . LEU B 1 86  ? 27.403  37.266  -37.342 1.00 98.01  ? 86  LEU B CG  1 
ATOM   4947  C CD1 . LEU B 1 86  ? 25.985  36.820  -37.053 1.00 100.80 ? 86  LEU B CD1 1 
ATOM   4948  C CD2 . LEU B 1 86  ? 27.706  37.004  -38.799 1.00 96.63  ? 86  LEU B CD2 1 
ATOM   4949  N N   . ILE B 1 87  ? 29.546  39.242  -39.623 1.00 90.35  ? 87  ILE B N   1 
ATOM   4950  C CA  . ILE B 1 87  ? 29.417  39.567  -41.071 1.00 89.33  ? 87  ILE B CA  1 
ATOM   4951  C C   . ILE B 1 87  ? 28.730  38.304  -41.602 1.00 89.55  ? 87  ILE B C   1 
ATOM   4952  O O   . ILE B 1 87  ? 29.458  37.347  -41.899 1.00 88.33  ? 87  ILE B O   1 
ATOM   4953  C CB  . ILE B 1 87  ? 30.772  39.856  -41.730 1.00 86.68  ? 87  ILE B CB  1 
ATOM   4954  C CG1 . ILE B 1 87  ? 31.540  40.928  -40.967 1.00 87.22  ? 87  ILE B CG1 1 
ATOM   4955  C CG2 . ILE B 1 87  ? 30.599  40.223  -43.201 1.00 85.46  ? 87  ILE B CG2 1 
ATOM   4956  C CD1 . ILE B 1 87  ? 32.396  41.818  -41.847 1.00 85.83  ? 87  ILE B CD1 1 
ATOM   4957  N N   . MET B 1 88  ? 27.407  38.296  -41.706 1.00 91.95  ? 88  MET B N   1 
ATOM   4958  C CA  . MET B 1 88  ? 26.727  37.043  -42.107 1.00 93.90  ? 88  MET B CA  1 
ATOM   4959  C C   . MET B 1 88  ? 26.755  36.933  -43.628 1.00 94.48  ? 88  MET B C   1 
ATOM   4960  O O   . MET B 1 88  ? 26.670  37.965  -44.309 1.00 95.22  ? 88  MET B O   1 
ATOM   4961  C CB  . MET B 1 88  ? 25.288  37.015  -41.592 1.00 97.19  ? 88  MET B CB  1 
ATOM   4962  C CG  . MET B 1 88  ? 24.452  35.867  -42.125 1.00 99.01  ? 88  MET B CG  1 
ATOM   4963  S SD  . MET B 1 88  ? 22.854  35.754  -41.298 1.00 105.16 ? 88  MET B SD  1 
ATOM   4964  C CE  . MET B 1 88  ? 23.422  35.686  -39.595 1.00 105.91 ? 88  MET B CE  1 
ATOM   4965  N N   . GLY B 1 89  ? 26.900  35.713  -44.122 1.00 94.88  ? 89  GLY B N   1 
ATOM   4966  C CA  . GLY B 1 89  ? 26.881  35.511  -45.573 1.00 93.82  ? 89  GLY B CA  1 
ATOM   4967  C C   . GLY B 1 89  ? 25.650  34.740  -45.955 1.00 94.50  ? 89  GLY B C   1 
ATOM   4968  O O   . GLY B 1 89  ? 25.107  34.024  -45.099 1.00 95.71  ? 89  GLY B O   1 
ATOM   4969  N N   . ILE B 1 90  ? 25.214  34.902  -47.195 1.00 92.91  ? 90  ILE B N   1 
ATOM   4970  C CA  . ILE B 1 90  ? 23.959  34.228  -47.610 1.00 93.26  ? 90  ILE B CA  1 
ATOM   4971  C C   . ILE B 1 90  ? 24.332  33.162  -48.638 1.00 91.46  ? 90  ILE B C   1 
ATOM   4972  O O   . ILE B 1 90  ? 24.896  33.513  -49.685 1.00 89.56  ? 90  ILE B O   1 
ATOM   4973  C CB  . ILE B 1 90  ? 22.895  35.221  -48.121 1.00 94.15  ? 90  ILE B CB  1 
ATOM   4974  C CG1 . ILE B 1 90  ? 22.584  36.296  -47.084 1.00 95.32  ? 90  ILE B CG1 1 
ATOM   4975  C CG2 . ILE B 1 90  ? 21.630  34.485  -48.559 1.00 95.38  ? 90  ILE B CG2 1 
ATOM   4976  C CD1 . ILE B 1 90  ? 22.082  35.749  -45.762 1.00 96.81  ? 90  ILE B CD1 1 
ATOM   4977  N N   . ASP B 1 91  ? 24.008  31.916  -48.327 1.00 92.31  ? 91  ASP B N   1 
ATOM   4978  C CA  . ASP B 1 91  ? 24.357  30.811  -49.203 1.00 91.45  ? 91  ASP B CA  1 
ATOM   4979  C C   . ASP B 1 91  ? 23.542  30.859  -50.502 1.00 92.09  ? 91  ASP B C   1 
ATOM   4980  O O   . ASP B 1 91  ? 22.591  30.102  -50.687 1.00 92.46  ? 91  ASP B O   1 
ATOM   4981  C CB  . ASP B 1 91  ? 24.296  29.500  -48.437 1.00 91.94  ? 91  ASP B CB  1 
ATOM   4982  C CG  . ASP B 1 91  ? 24.631  28.272  -49.265 1.00 91.69  ? 91  ASP B CG  1 
ATOM   4983  O OD1 . ASP B 1 91  ? 25.621  28.336  -50.044 1.00 89.92  ? 91  ASP B OD1 1 
ATOM   4984  O OD2 . ASP B 1 91  ? 23.894  27.269  -49.124 1.00 93.45  ? 91  ASP B OD2 1 
ATOM   4985  N N   . ILE B 1 92  ? 23.950  31.767  -51.402 1.00 92.00  ? 92  ILE B N   1 
ATOM   4986  C CA  . ILE B 1 92  ? 23.533  31.782  -52.800 1.00 93.26  ? 92  ILE B CA  1 
ATOM   4987  C C   . ILE B 1 92  ? 24.546  30.936  -53.580 1.00 93.14  ? 92  ILE B C   1 
ATOM   4988  O O   . ILE B 1 92  ? 25.659  31.384  -53.848 1.00 90.76  ? 92  ILE B O   1 
ATOM   4989  C CB  . ILE B 1 92  ? 23.428  33.236  -53.334 1.00 92.49  ? 92  ILE B CB  1 
ATOM   4990  C CG1 . ILE B 1 92  ? 22.406  34.113  -52.550 1.00 93.79  ? 92  ILE B CG1 1 
ATOM   4991  C CG2 . ILE B 1 92  ? 23.159  33.278  -54.843 1.00 92.52  ? 92  ILE B CG2 1 
ATOM   4992  C CD1 . ILE B 1 92  ? 21.099  33.431  -52.170 1.00 95.28  ? 92  ILE B CD1 1 
ATOM   4993  N N   . LYS B 1 93  ? 24.170  29.697  -53.917 1.00 96.39  ? 93  LYS B N   1 
ATOM   4994  C CA  . LYS B 1 93  ? 25.111  28.753  -54.498 1.00 97.81  ? 93  LYS B CA  1 
ATOM   4995  C C   . LYS B 1 93  ? 25.710  29.378  -55.753 1.00 96.67  ? 93  LYS B C   1 
ATOM   4996  O O   . LYS B 1 93  ? 24.949  29.745  -56.649 1.00 98.44  ? 93  LYS B O   1 
ATOM   4997  C CB  . LYS B 1 93  ? 24.460  27.418  -54.881 1.00 102.19 ? 93  LYS B CB  1 
ATOM   4998  C CG  . LYS B 1 93  ? 24.035  26.487  -53.739 1.00 105.53 ? 93  LYS B CG  1 
ATOM   4999  C CD  . LYS B 1 93  ? 25.164  25.986  -52.840 1.00 106.41 ? 93  LYS B CD  1 
ATOM   5000  C CE  . LYS B 1 93  ? 24.774  24.746  -52.068 1.00 108.25 ? 93  LYS B CE  1 
ATOM   5001  N NZ  . LYS B 1 93  ? 23.564  24.885  -51.251 1.00 108.54 ? 93  LYS B NZ  1 
ATOM   5002  N N   . PRO B 1 94  ? 27.063  29.503  -55.852 1.00 93.58  ? 94  PRO B N   1 
ATOM   5003  C CA  . PRO B 1 94  ? 27.714  30.233  -56.948 1.00 92.43  ? 94  PRO B CA  1 
ATOM   5004  C C   . PRO B 1 94  ? 27.467  29.687  -58.352 1.00 94.27  ? 94  PRO B C   1 
ATOM   5005  O O   . PRO B 1 94  ? 27.570  30.431  -59.330 1.00 91.98  ? 94  PRO B O   1 
ATOM   5006  C CB  . PRO B 1 94  ? 29.223  30.167  -56.606 1.00 89.59  ? 94  PRO B CB  1 
ATOM   5007  C CG  . PRO B 1 94  ? 29.294  29.757  -55.150 1.00 89.25  ? 94  PRO B CG  1 
ATOM   5008  C CD  . PRO B 1 94  ? 28.041  28.949  -54.898 1.00 91.84  ? 94  PRO B CD  1 
ATOM   5009  N N   . GLU B 1 95  ? 27.145  28.386  -58.424 1.00 98.49  ? 95  GLU B N   1 
ATOM   5010  C CA  . GLU B 1 95  ? 27.142  27.638  -59.670 1.00 101.06 ? 95  GLU B CA  1 
ATOM   5011  C C   . GLU B 1 95  ? 25.797  27.793  -60.385 1.00 101.21 ? 95  GLU B C   1 
ATOM   5012  O O   . GLU B 1 95  ? 25.707  27.462  -61.560 1.00 103.27 ? 95  GLU B O   1 
ATOM   5013  C CB  . GLU B 1 95  ? 27.589  26.188  -59.433 1.00 103.70 ? 95  GLU B CB  1 
ATOM   5014  C CG  . GLU B 1 95  ? 26.676  25.329  -58.552 1.00 108.64 ? 95  GLU B CG  1 
ATOM   5015  C CD  . GLU B 1 95  ? 26.924  25.247  -57.042 1.00 111.64 ? 95  GLU B CD  1 
ATOM   5016  O OE1 . GLU B 1 95  ? 27.623  26.116  -56.486 1.00 111.43 ? 95  GLU B OE1 1 
ATOM   5017  O OE2 . GLU B 1 95  ? 26.423  24.287  -56.399 1.00 116.63 ? 95  GLU B OE2 1 
ATOM   5018  N N   . GLU B 1 96  ? 24.771  28.339  -59.714 1.00 100.57 ? 96  GLU B N   1 
ATOM   5019  C CA  . GLU B 1 96  ? 23.406  28.326  -60.238 1.00 102.76 ? 96  GLU B CA  1 
ATOM   5020  C C   . GLU B 1 96  ? 23.194  29.406  -61.303 1.00 101.66 ? 96  GLU B C   1 
ATOM   5021  O O   . GLU B 1 96  ? 23.941  30.386  -61.362 1.00 101.93 ? 96  GLU B O   1 
ATOM   5022  C CB  . GLU B 1 96  ? 22.372  28.459  -59.113 1.00 104.54 ? 96  GLU B CB  1 
ATOM   5023  C CG  . GLU B 1 96  ? 22.256  27.201  -58.250 1.00 105.68 ? 96  GLU B CG  1 
ATOM   5024  C CD  . GLU B 1 96  ? 21.981  25.937  -59.057 1.00 106.17 ? 96  GLU B CD  1 
ATOM   5025  O OE1 . GLU B 1 96  ? 20.861  25.973  -59.626 1.00 106.53 ? 96  GLU B OE1 1 
ATOM   5026  O OE2 . GLU B 1 96  ? 22.831  24.989  -59.159 1.00 102.74 ? 96  GLU B OE2 1 
ATOM   5027  N N   . ASP B 1 97  ? 22.173  29.208  -62.152 1.00 100.60 ? 97  ASP B N   1 
ATOM   5028  C CA  . ASP B 1 97  ? 21.872  30.140  -63.229 1.00 100.82 ? 97  ASP B CA  1 
ATOM   5029  C C   . ASP B 1 97  ? 21.150  31.342  -62.625 1.00 101.23 ? 97  ASP B C   1 
ATOM   5030  O O   . ASP B 1 97  ? 19.944  31.296  -62.368 1.00 103.87 ? 97  ASP B O   1 
ATOM   5031  C CB  . ASP B 1 97  ? 21.121  29.486  -64.386 1.00 102.95 ? 97  ASP B CB  1 
ATOM   5032  C CG  . ASP B 1 97  ? 20.554  30.400  -65.475 1.00 104.90 ? 97  ASP B CG  1 
ATOM   5033  O OD1 . ASP B 1 97  ? 20.939  31.596  -65.546 1.00 104.04 ? 97  ASP B OD1 1 
ATOM   5034  O OD2 . ASP B 1 97  ? 19.691  29.921  -66.243 1.00 107.03 ? 97  ASP B OD2 1 
ATOM   5035  N N   . TYR B 1 98  ? 21.900  32.436  -62.450 1.00 98.63  ? 98  TYR B N   1 
ATOM   5036  C CA  . TYR B 1 98  ? 21.397  33.624  -61.789 1.00 98.62  ? 98  TYR B CA  1 
ATOM   5037  C C   . TYR B 1 98  ? 20.195  34.173  -62.572 1.00 101.84 ? 98  TYR B C   1 
ATOM   5038  O O   . TYR B 1 98  ? 19.365  34.896  -62.018 1.00 103.24 ? 98  TYR B O   1 
ATOM   5039  C CB  . TYR B 1 98  ? 22.547  34.629  -61.636 1.00 96.20  ? 98  TYR B CB  1 
ATOM   5040  C CG  . TYR B 1 98  ? 23.879  34.129  -61.069 1.00 93.93  ? 98  TYR B CG  1 
ATOM   5041  C CD1 . TYR B 1 98  ? 23.958  33.326  -59.934 1.00 92.95  ? 98  TYR B CD1 1 
ATOM   5042  C CD2 . TYR B 1 98  ? 25.080  34.463  -61.690 1.00 91.75  ? 98  TYR B CD2 1 
ATOM   5043  C CE1 . TYR B 1 98  ? 25.178  32.884  -59.438 1.00 90.27  ? 98  TYR B CE1 1 
ATOM   5044  C CE2 . TYR B 1 98  ? 26.300  34.023  -61.208 1.00 89.64  ? 98  TYR B CE2 1 
ATOM   5045  C CZ  . TYR B 1 98  ? 26.357  33.236  -60.075 1.00 88.91  ? 98  TYR B CZ  1 
ATOM   5046  O OH  . TYR B 1 98  ? 27.594  32.828  -59.647 1.00 85.86  ? 98  TYR B OH  1 
ATOM   5047  N N   . GLY B 1 99  ? 20.085  33.818  -63.863 1.00 102.74 ? 99  GLY B N   1 
ATOM   5048  C CA  . GLY B 1 99  ? 19.031  34.350  -64.717 1.00 104.11 ? 99  GLY B CA  1 
ATOM   5049  C C   . GLY B 1 99  ? 17.861  33.389  -64.896 1.00 105.62 ? 99  GLY B C   1 
ATOM   5050  O O   . GLY B 1 99  ? 17.001  33.650  -65.725 1.00 106.08 ? 99  GLY B O   1 
ATOM   5051  N N   . ASP B 1 100 ? 17.854  32.277  -64.141 1.00 106.50 ? 100 ASP B N   1 
ATOM   5052  C CA  . ASP B 1 100 ? 16.735  31.338  -64.121 1.00 108.85 ? 100 ASP B CA  1 
ATOM   5053  C C   . ASP B 1 100 ? 15.684  31.797  -63.105 1.00 109.36 ? 100 ASP B C   1 
ATOM   5054  O O   . ASP B 1 100 ? 15.874  31.656  -61.901 1.00 108.25 ? 100 ASP B O   1 
ATOM   5055  C CB  . ASP B 1 100 ? 17.176  29.906  -63.827 1.00 108.37 ? 100 ASP B CB  1 
ATOM   5056  C CG  . ASP B 1 100 ? 16.052  28.877  -63.743 1.00 110.85 ? 100 ASP B CG  1 
ATOM   5057  O OD1 . ASP B 1 100 ? 15.434  28.592  -64.790 1.00 112.56 ? 100 ASP B OD1 1 
ATOM   5058  O OD2 . ASP B 1 100 ? 15.778  28.384  -62.628 1.00 111.52 ? 100 ASP B OD2 1 
ATOM   5059  N N   . PRO B 1 101 ? 14.513  32.301  -63.556 1.00 111.48 ? 101 PRO B N   1 
ATOM   5060  C CA  . PRO B 1 101 ? 13.459  32.783  -62.655 1.00 112.75 ? 101 PRO B CA  1 
ATOM   5061  C C   . PRO B 1 101 ? 13.214  32.026  -61.350 1.00 113.36 ? 101 PRO B C   1 
ATOM   5062  O O   . PRO B 1 101 ? 12.893  32.634  -60.333 1.00 113.65 ? 101 PRO B O   1 
ATOM   5063  C CB  . PRO B 1 101 ? 12.214  32.682  -63.556 1.00 115.32 ? 101 PRO B CB  1 
ATOM   5064  C CG  . PRO B 1 101 ? 12.721  32.955  -64.946 1.00 115.09 ? 101 PRO B CG  1 
ATOM   5065  C CD  . PRO B 1 101 ? 14.132  32.397  -64.973 1.00 112.82 ? 101 PRO B CD  1 
ATOM   5066  N N   . GLU B 1 102 ? 13.330  30.694  -61.382 1.00 114.07 ? 102 GLU B N   1 
ATOM   5067  C CA  . GLU B 1 102 ? 12.970  29.891  -60.225 1.00 115.23 ? 102 GLU B CA  1 
ATOM   5068  C C   . GLU B 1 102 ? 13.994  30.045  -59.105 1.00 112.76 ? 102 GLU B C   1 
ATOM   5069  O O   . GLU B 1 102 ? 13.610  30.012  -57.936 1.00 112.12 ? 102 GLU B O   1 
ATOM   5070  C CB  . GLU B 1 102 ? 12.695  28.434  -60.600 1.00 117.47 ? 102 GLU B CB  1 
ATOM   5071  C CG  . GLU B 1 102 ? 11.218  28.236  -60.947 1.00 121.36 ? 102 GLU B CG  1 
ATOM   5072  C CD  . GLU B 1 102 ? 10.725  26.816  -61.109 1.00 122.92 ? 102 GLU B CD  1 
ATOM   5073  O OE1 . GLU B 1 102 ? 11.519  25.847  -61.099 1.00 121.54 ? 102 GLU B OE1 1 
ATOM   5074  O OE2 . GLU B 1 102 ? 9.489   26.724  -61.231 1.00 126.01 ? 102 GLU B OE2 1 
ATOM   5075  N N   . PHE B 1 103 ? 15.277  30.232  -59.466 1.00 110.76 ? 103 PHE B N   1 
ATOM   5076  C CA  . PHE B 1 103 ? 16.346  30.387  -58.487 1.00 108.43 ? 103 PHE B CA  1 
ATOM   5077  C C   . PHE B 1 103 ? 16.316  31.777  -57.835 1.00 107.65 ? 103 PHE B C   1 
ATOM   5078  O O   . PHE B 1 103 ? 16.463  31.895  -56.618 1.00 108.09 ? 103 PHE B O   1 
ATOM   5079  C CB  . PHE B 1 103 ? 17.705  30.139  -59.139 1.00 106.86 ? 103 PHE B CB  1 
ATOM   5080  C CG  . PHE B 1 103 ? 18.840  30.297  -58.142 1.00 105.90 ? 103 PHE B CG  1 
ATOM   5081  C CD1 . PHE B 1 103 ? 18.852  29.559  -56.964 1.00 106.64 ? 103 PHE B CD1 1 
ATOM   5082  C CD2 . PHE B 1 103 ? 19.833  31.246  -58.346 1.00 104.67 ? 103 PHE B CD2 1 
ATOM   5083  C CE1 . PHE B 1 103 ? 19.879  29.710  -56.052 1.00 105.56 ? 103 PHE B CE1 1 
ATOM   5084  C CE2 . PHE B 1 103 ? 20.840  31.413  -57.415 1.00 103.78 ? 103 PHE B CE2 1 
ATOM   5085  C CZ  . PHE B 1 103 ? 20.864  30.637  -56.276 1.00 104.17 ? 103 PHE B CZ  1 
ATOM   5086  N N   . VAL B 1 104 ? 16.138  32.832  -58.646 1.00 106.50 ? 104 VAL B N   1 
ATOM   5087  C CA  . VAL B 1 104 ? 15.911  34.187  -58.151 1.00 105.63 ? 104 VAL B CA  1 
ATOM   5088  C C   . VAL B 1 104 ? 14.805  34.170  -57.087 1.00 107.15 ? 104 VAL B C   1 
ATOM   5089  O O   . VAL B 1 104 ? 14.962  34.774  -56.027 1.00 106.75 ? 104 VAL B O   1 
ATOM   5090  C CB  . VAL B 1 104 ? 15.563  35.164  -59.296 1.00 106.03 ? 104 VAL B CB  1 
ATOM   5091  C CG1 . VAL B 1 104 ? 15.494  36.603  -58.803 1.00 106.45 ? 104 VAL B CG1 1 
ATOM   5092  C CG2 . VAL B 1 104 ? 16.530  35.074  -60.470 1.00 104.20 ? 104 VAL B CG2 1 
ATOM   5093  N N   . LYS B 1 105 ? 13.697  33.461  -57.380 1.00 108.50 ? 105 LYS B N   1 
ATOM   5094  C CA  . LYS B 1 105 ? 12.515  33.375  -56.528 1.00 109.63 ? 105 LYS B CA  1 
ATOM   5095  C C   . LYS B 1 105 ? 12.820  32.682  -55.198 1.00 108.08 ? 105 LYS B C   1 
ATOM   5096  O O   . LYS B 1 105 ? 12.500  33.207  -54.133 1.00 107.95 ? 105 LYS B O   1 
ATOM   5097  C CB  . LYS B 1 105 ? 11.424  32.586  -57.262 1.00 112.04 ? 105 LYS B CB  1 
ATOM   5098  C CG  . LYS B 1 105 ? 10.082  32.524  -56.551 1.00 115.10 ? 105 LYS B CG  1 
ATOM   5099  C CD  . LYS B 1 105 ? 8.990   31.801  -57.326 1.00 117.89 ? 105 LYS B CD  1 
ATOM   5100  C CE  . LYS B 1 105 ? 8.837   32.304  -58.730 1.00 118.47 ? 105 LYS B CE  1 
ATOM   5101  N NZ  . LYS B 1 105 ? 7.464   32.138  -59.216 1.00 121.61 ? 105 LYS B NZ  1 
ATOM   5102  N N   . ASP B 1 106 ? 13.425  31.487  -55.267 1.00 106.38 ? 106 ASP B N   1 
ATOM   5103  C CA  . ASP B 1 106 ? 13.799  30.752  -54.067 1.00 105.00 ? 106 ASP B CA  1 
ATOM   5104  C C   . ASP B 1 106 ? 14.777  31.598  -53.266 1.00 101.96 ? 106 ASP B C   1 
ATOM   5105  O O   . ASP B 1 106 ? 14.680  31.642  -52.041 1.00 102.31 ? 106 ASP B O   1 
ATOM   5106  C CB  . ASP B 1 106 ? 14.305  29.351  -54.376 1.00 104.28 ? 106 ASP B CB  1 
ATOM   5107  C CG  . ASP B 1 106 ? 13.224  28.402  -54.881 1.00 107.21 ? 106 ASP B CG  1 
ATOM   5108  O OD1 . ASP B 1 106 ? 12.118  28.356  -54.259 1.00 108.90 ? 106 ASP B OD1 1 
ATOM   5109  O OD2 . ASP B 1 106 ? 13.490  27.723  -55.902 1.00 107.31 ? 106 ASP B OD2 1 
ATOM   5110  N N   . SER B 1 107 ? 15.660  32.308  -53.984 1.00 99.01  ? 107 SER B N   1 
ATOM   5111  C CA  . SER B 1 107 ? 16.679  33.132  -53.359 1.00 96.58  ? 107 SER B CA  1 
ATOM   5112  C C   . SER B 1 107 ? 16.028  34.281  -52.597 1.00 97.14  ? 107 SER B C   1 
ATOM   5113  O O   . SER B 1 107 ? 16.423  34.562  -51.470 1.00 96.75  ? 107 SER B O   1 
ATOM   5114  C CB  . SER B 1 107 ? 17.715  33.607  -54.361 1.00 94.99  ? 107 SER B CB  1 
ATOM   5115  O OG  . SER B 1 107 ? 18.672  32.579  -54.650 1.00 93.68  ? 107 SER B OG  1 
ATOM   5116  N N   . GLU B 1 108 ? 15.005  34.898  -53.204 1.00 98.12  ? 108 GLU B N   1 
ATOM   5117  C CA  . GLU B 1 108 ? 14.263  35.988  -52.592 1.00 99.11  ? 108 GLU B CA  1 
ATOM   5118  C C   . GLU B 1 108 ? 13.515  35.523  -51.338 1.00 100.02 ? 108 GLU B C   1 
ATOM   5119  O O   . GLU B 1 108 ? 13.581  36.195  -50.307 1.00 100.59 ? 108 GLU B O   1 
ATOM   5120  C CB  . GLU B 1 108 ? 13.301  36.586  -53.620 1.00 100.99 ? 108 GLU B CB  1 
ATOM   5121  C CG  . GLU B 1 108 ? 14.023  37.328  -54.739 1.00 99.76  ? 108 GLU B CG  1 
ATOM   5122  C CD  . GLU B 1 108 ? 13.097  38.078  -55.673 1.00 101.78 ? 108 GLU B CD  1 
ATOM   5123  O OE1 . GLU B 1 108 ? 12.125  37.480  -56.167 1.00 103.57 ? 108 GLU B OE1 1 
ATOM   5124  O OE2 . GLU B 1 108 ? 13.359  39.270  -55.908 1.00 101.89 ? 108 GLU B OE2 1 
ATOM   5125  N N   . ILE B 1 109 ? 12.796  34.390  -51.429 1.00 100.22 ? 109 ILE B N   1 
ATOM   5126  C CA  . ILE B 1 109 ? 12.006  33.879  -50.313 1.00 101.42 ? 109 ILE B CA  1 
ATOM   5127  C C   . ILE B 1 109 ? 12.927  33.575  -49.136 1.00 99.44  ? 109 ILE B C   1 
ATOM   5128  O O   . ILE B 1 109 ? 12.660  34.016  -48.019 1.00 100.30 ? 109 ILE B O   1 
ATOM   5129  C CB  . ILE B 1 109 ? 11.195  32.628  -50.707 1.00 102.91 ? 109 ILE B CB  1 
ATOM   5130  C CG1 . ILE B 1 109 ? 10.150  32.952  -51.782 1.00 104.75 ? 109 ILE B CG1 1 
ATOM   5131  C CG2 . ILE B 1 109 ? 10.544  31.978  -49.479 1.00 104.76 ? 109 ILE B CG2 1 
ATOM   5132  C CD1 . ILE B 1 109 ? 9.733   31.762  -52.628 1.00 105.51 ? 109 ILE B CD1 1 
ATOM   5133  N N   . GLU B 1 110 ? 13.993  32.803  -49.410 1.00 96.70  ? 110 GLU B N   1 
ATOM   5134  C CA  . GLU B 1 110 ? 14.924  32.353  -48.382 1.00 94.99  ? 110 GLU B CA  1 
ATOM   5135  C C   . GLU B 1 110 ? 15.514  33.559  -47.650 1.00 93.78  ? 110 GLU B C   1 
ATOM   5136  O O   . GLU B 1 110 ? 15.479  33.612  -46.416 1.00 94.49  ? 110 GLU B O   1 
ATOM   5137  C CB  . GLU B 1 110 ? 16.050  31.478  -48.949 1.00 92.73  ? 110 GLU B CB  1 
ATOM   5138  C CG  . GLU B 1 110 ? 17.191  31.198  -47.969 1.00 91.09  ? 110 GLU B CG  1 
ATOM   5139  C CD  . GLU B 1 110 ? 16.785  30.631  -46.617 1.00 92.64  ? 110 GLU B CD  1 
ATOM   5140  O OE1 . GLU B 1 110 ? 15.686  30.049  -46.442 1.00 94.96  ? 110 GLU B OE1 1 
ATOM   5141  O OE2 . GLU B 1 110 ? 17.597  30.826  -45.698 1.00 91.69  ? 110 GLU B OE2 1 
ATOM   5142  N N   . LEU B 1 111 ? 16.056  34.520  -48.416 1.00 91.99  ? 111 LEU B N   1 
ATOM   5143  C CA  . LEU B 1 111 ? 16.625  35.723  -47.834 1.00 91.04  ? 111 LEU B CA  1 
ATOM   5144  C C   . LEU B 1 111 ? 15.584  36.372  -46.927 1.00 93.06  ? 111 LEU B C   1 
ATOM   5145  O O   . LEU B 1 111 ? 15.797  36.439  -45.717 1.00 93.38  ? 111 LEU B O   1 
ATOM   5146  C CB  . LEU B 1 111 ? 17.103  36.679  -48.921 1.00 90.20  ? 111 LEU B CB  1 
ATOM   5147  C CG  . LEU B 1 111 ? 17.817  37.942  -48.429 1.00 89.87  ? 111 LEU B CG  1 
ATOM   5148  C CD1 . LEU B 1 111 ? 18.666  37.693  -47.190 1.00 88.92  ? 111 LEU B CD1 1 
ATOM   5149  C CD2 . LEU B 1 111 ? 18.716  38.495  -49.543 1.00 88.28  ? 111 LEU B CD2 1 
ATOM   5150  N N   . LYS B 1 112 ? 14.448  36.779  -47.517 1.00 95.03  ? 112 LYS B N   1 
ATOM   5151  C CA  . LYS B 1 112 ? 13.352  37.399  -46.781 1.00 97.78  ? 112 LYS B CA  1 
ATOM   5152  C C   . LYS B 1 112 ? 13.074  36.657  -45.468 1.00 98.91  ? 112 LYS B C   1 
ATOM   5153  O O   . LYS B 1 112 ? 12.745  37.295  -44.472 1.00 100.45 ? 112 LYS B O   1 
ATOM   5154  C CB  . LYS B 1 112 ? 12.070  37.531  -47.622 1.00 99.95  ? 112 LYS B CB  1 
ATOM   5155  C CG  . LYS B 1 112 ? 12.065  38.695  -48.623 1.00 99.90  ? 112 LYS B CG  1 
ATOM   5156  C CD  . LYS B 1 112 ? 10.833  38.832  -49.514 1.00 102.09 ? 112 LYS B CD  1 
ATOM   5157  C CE  . LYS B 1 112 ? 11.063  39.641  -50.757 1.00 101.49 ? 112 LYS B CE  1 
ATOM   5158  N NZ  . LYS B 1 112 ? 9.975   39.428  -51.717 1.00 103.33 ? 112 LYS B NZ  1 
ATOM   5159  N N   . ARG B 1 113 ? 13.188  35.319  -45.457 1.00 98.40  ? 113 ARG B N   1 
ATOM   5160  C CA  . ARG B 1 113 ? 12.951  34.546  -44.244 1.00 99.61  ? 113 ARG B CA  1 
ATOM   5161  C C   . ARG B 1 113 ? 13.990  34.887  -43.181 1.00 98.33  ? 113 ARG B C   1 
ATOM   5162  O O   . ARG B 1 113 ? 13.672  35.007  -41.999 1.00 99.94  ? 113 ARG B O   1 
ATOM   5163  C CB  . ARG B 1 113 ? 13.028  33.030  -44.454 1.00 99.25  ? 113 ARG B CB  1 
ATOM   5164  C CG  . ARG B 1 113 ? 12.578  32.225  -43.239 1.00 101.12 ? 113 ARG B CG  1 
ATOM   5165  C CD  . ARG B 1 113 ? 12.518  30.744  -43.562 1.00 101.22 ? 113 ARG B CD  1 
ATOM   5166  N NE  . ARG B 1 113 ? 13.840  30.200  -43.886 1.00 98.39  ? 113 ARG B NE  1 
ATOM   5167  C CZ  . ARG B 1 113 ? 14.783  29.902  -43.007 1.00 97.22  ? 113 ARG B CZ  1 
ATOM   5168  N NH1 . ARG B 1 113 ? 14.543  29.905  -41.707 1.00 98.75  ? 113 ARG B NH1 1 
ATOM   5169  N NH2 . ARG B 1 113 ? 15.992  29.578  -43.445 1.00 94.62  ? 113 ARG B NH2 1 
ATOM   5170  N N   . VAL B 1 114 ? 15.249  34.985  -43.613 1.00 96.03  ? 114 VAL B N   1 
ATOM   5171  C CA  . VAL B 1 114 ? 16.336  35.233  -42.686 1.00 95.59  ? 114 VAL B CA  1 
ATOM   5172  C C   . VAL B 1 114 ? 16.166  36.647  -42.125 1.00 97.61  ? 114 VAL B C   1 
ATOM   5173  O O   . VAL B 1 114 ? 16.101  36.847  -40.909 1.00 99.03  ? 114 VAL B O   1 
ATOM   5174  C CB  . VAL B 1 114 ? 17.682  35.008  -43.394 1.00 92.69  ? 114 VAL B CB  1 
ATOM   5175  C CG1 . VAL B 1 114 ? 18.883  35.245  -42.476 1.00 91.32  ? 114 VAL B CG1 1 
ATOM   5176  C CG2 . VAL B 1 114 ? 17.756  33.609  -44.002 1.00 92.02  ? 114 VAL B CG2 1 
ATOM   5177  N N   . LEU B 1 115 ? 15.978  37.616  -43.027 1.00 98.77  ? 115 LEU B N   1 
ATOM   5178  C CA  . LEU B 1 115 ? 15.922  39.023  -42.654 1.00 100.73 ? 115 LEU B CA  1 
ATOM   5179  C C   . LEU B 1 115 ? 14.848  39.249  -41.606 1.00 104.16 ? 115 LEU B C   1 
ATOM   5180  O O   . LEU B 1 115 ? 15.026  40.062  -40.705 1.00 105.12 ? 115 LEU B O   1 
ATOM   5181  C CB  . LEU B 1 115 ? 15.696  39.887  -43.891 1.00 101.17 ? 115 LEU B CB  1 
ATOM   5182  C CG  . LEU B 1 115 ? 16.892  39.931  -44.852 1.00 98.95  ? 115 LEU B CG  1 
ATOM   5183  C CD1 . LEU B 1 115 ? 16.525  40.746  -46.078 1.00 99.69  ? 115 LEU B CD1 1 
ATOM   5184  C CD2 . LEU B 1 115 ? 18.152  40.472  -44.189 1.00 97.49  ? 115 LEU B CD2 1 
ATOM   5185  N N   . ASN B 1 116 ? 13.772  38.475  -41.732 1.00 106.46 ? 116 ASN B N   1 
ATOM   5186  C CA  . ASN B 1 116 ? 12.549  38.658  -40.973 1.00 110.13 ? 116 ASN B CA  1 
ATOM   5187  C C   . ASN B 1 116 ? 12.766  38.354  -39.490 1.00 111.37 ? 116 ASN B C   1 
ATOM   5188  O O   . ASN B 1 116 ? 11.901  38.646  -38.683 1.00 114.10 ? 116 ASN B O   1 
ATOM   5189  C CB  . ASN B 1 116 ? 11.470  37.778  -41.583 1.00 111.60 ? 116 ASN B CB  1 
ATOM   5190  C CG  . ASN B 1 116 ? 10.128  38.029  -40.964 1.00 115.55 ? 116 ASN B CG  1 
ATOM   5191  O OD1 . ASN B 1 116 ? 9.500   39.061  -41.226 1.00 117.40 ? 116 ASN B OD1 1 
ATOM   5192  N ND2 . ASN B 1 116 ? 9.679   37.098  -40.141 1.00 117.32 ? 116 ASN B ND2 1 
ATOM   5193  N N   . TYR B 1 117 ? 13.893  37.717  -39.131 1.00 109.85 ? 117 TYR B N   1 
ATOM   5194  C CA  . TYR B 1 117 ? 14.285  37.577  -37.733 1.00 110.83 ? 117 TYR B CA  1 
ATOM   5195  C C   . TYR B 1 117 ? 15.685  38.155  -37.513 1.00 108.94 ? 117 TYR B C   1 
ATOM   5196  O O   . TYR B 1 117 ? 16.041  38.482  -36.383 1.00 109.83 ? 117 TYR B O   1 
ATOM   5197  C CB  . TYR B 1 117 ? 14.202  36.118  -37.260 1.00 111.03 ? 117 TYR B CB  1 
ATOM   5198  C CG  . TYR B 1 117 ? 15.100  35.131  -37.996 1.00 108.21 ? 117 TYR B CG  1 
ATOM   5199  C CD1 . TYR B 1 117 ? 16.447  34.992  -37.660 1.00 105.98 ? 117 TYR B CD1 1 
ATOM   5200  C CD2 . TYR B 1 117 ? 14.606  34.322  -39.015 1.00 107.91 ? 117 TYR B CD2 1 
ATOM   5201  C CE1 . TYR B 1 117 ? 17.276  34.101  -38.326 1.00 103.45 ? 117 TYR B CE1 1 
ATOM   5202  C CE2 . TYR B 1 117 ? 15.420  33.407  -39.669 1.00 105.65 ? 117 TYR B CE2 1 
ATOM   5203  C CZ  . TYR B 1 117 ? 16.759  33.307  -39.332 1.00 103.33 ? 117 TYR B CZ  1 
ATOM   5204  O OH  . TYR B 1 117 ? 17.572  32.440  -39.993 1.00 101.13 ? 117 TYR B OH  1 
ATOM   5205  N N   . ALA B 1 118 ? 16.476  38.271  -38.588 1.00 106.68 ? 118 ALA B N   1 
ATOM   5206  C CA  . ALA B 1 118 ? 17.833  38.788  -38.502 1.00 104.96 ? 118 ALA B CA  1 
ATOM   5207  C C   . ALA B 1 118 ? 17.817  40.210  -37.958 1.00 106.84 ? 118 ALA B C   1 
ATOM   5208  O O   . ALA B 1 118 ? 18.642  40.571  -37.121 1.00 106.46 ? 118 ALA B O   1 
ATOM   5209  C CB  . ALA B 1 118 ? 18.490  38.757  -39.865 1.00 102.38 ? 118 ALA B CB  1 
ATOM   5210  N N   . LYS B 1 119 ? 16.843  40.980  -38.454 1.00 109.30 ? 119 LYS B N   1 
ATOM   5211  C CA  . LYS B 1 119 ? 16.776  42.422  -38.287 1.00 111.15 ? 119 LYS B CA  1 
ATOM   5212  C C   . LYS B 1 119 ? 16.703  42.827  -36.814 1.00 114.10 ? 119 LYS B C   1 
ATOM   5213  O O   . LYS B 1 119 ? 16.897  43.998  -36.496 1.00 114.83 ? 119 LYS B O   1 
ATOM   5214  C CB  . LYS B 1 119 ? 15.579  42.941  -39.091 1.00 112.73 ? 119 LYS B CB  1 
ATOM   5215  C CG  . LYS B 1 119 ? 14.188  42.464  -38.657 1.00 115.36 ? 119 LYS B CG  1 
ATOM   5216  C CD  . LYS B 1 119 ? 13.098  43.063  -39.538 1.00 116.95 ? 119 LYS B CD  1 
ATOM   5217  C CE  . LYS B 1 119 ? 11.728  42.753  -39.103 1.00 119.89 ? 119 LYS B CE  1 
ATOM   5218  N NZ  . LYS B 1 119 ? 10.828  43.229  -40.148 1.00 121.28 ? 119 LYS B NZ  1 
ATOM   5219  N N   . LYS B 1 120 ? 16.441  41.857  -35.925 1.00 116.09 ? 120 LYS B N   1 
ATOM   5220  C CA  . LYS B 1 120 ? 16.308  42.101  -34.495 1.00 118.97 ? 120 LYS B CA  1 
ATOM   5221  C C   . LYS B 1 120 ? 17.661  41.999  -33.789 1.00 118.36 ? 120 LYS B C   1 
ATOM   5222  O O   . LYS B 1 120 ? 17.744  42.214  -32.582 1.00 119.83 ? 120 LYS B O   1 
ATOM   5223  C CB  . LYS B 1 120 ? 15.325  41.085  -33.896 1.00 120.69 ? 120 LYS B CB  1 
ATOM   5224  C CG  . LYS B 1 120 ? 14.000  40.943  -34.645 1.00 122.14 ? 120 LYS B CG  1 
ATOM   5225  C CD  . LYS B 1 120 ? 12.864  40.275  -33.870 1.00 125.10 ? 120 LYS B CD  1 
ATOM   5226  C CE  . LYS B 1 120 ? 12.943  38.779  -33.866 1.00 123.94 ? 120 LYS B CE  1 
ATOM   5227  N NZ  . LYS B 1 120 ? 11.879  38.164  -33.076 1.00 126.64 ? 120 LYS B NZ  1 
ATOM   5228  N N   . TYR B 1 121 ? 18.719  41.660  -34.535 1.00 116.94 ? 121 TYR B N   1 
ATOM   5229  C CA  . TYR B 1 121 ? 20.031  41.441  -33.945 1.00 116.76 ? 121 TYR B CA  1 
ATOM   5230  C C   . TYR B 1 121 ? 21.015  42.459  -34.525 1.00 114.92 ? 121 TYR B C   1 
ATOM   5231  O O   . TYR B 1 121 ? 21.390  42.359  -35.694 1.00 113.07 ? 121 TYR B O   1 
ATOM   5232  C CB  . TYR B 1 121 ? 20.346  39.952  -34.144 1.00 115.85 ? 121 TYR B CB  1 
ATOM   5233  C CG  . TYR B 1 121 ? 19.288  39.068  -33.492 1.00 119.78 ? 121 TYR B CG  1 
ATOM   5234  C CD1 . TYR B 1 121 ? 19.245  38.878  -32.113 1.00 122.42 ? 121 TYR B CD1 1 
ATOM   5235  C CD2 . TYR B 1 121 ? 18.292  38.467  -34.252 1.00 121.73 ? 121 TYR B CD2 1 
ATOM   5236  C CE1 . TYR B 1 121 ? 18.270  38.091  -31.517 1.00 125.76 ? 121 TYR B CE1 1 
ATOM   5237  C CE2 . TYR B 1 121 ? 17.309  37.680  -33.668 1.00 125.23 ? 121 TYR B CE2 1 
ATOM   5238  C CZ  . TYR B 1 121 ? 17.296  37.488  -32.297 1.00 127.62 ? 121 TYR B CZ  1 
ATOM   5239  O OH  . TYR B 1 121 ? 16.302  36.716  -31.750 1.00 130.71 ? 121 TYR B OH  1 
ATOM   5240  N N   . ASP B 1 122 ? 21.422  43.424  -33.675 1.00 115.64 ? 122 ASP B N   1 
ATOM   5241  C CA  . ASP B 1 122 ? 22.278  44.543  -34.058 1.00 113.99 ? 122 ASP B CA  1 
ATOM   5242  C C   . ASP B 1 122 ? 23.759  44.150  -34.019 1.00 110.70 ? 122 ASP B C   1 
ATOM   5243  O O   . ASP B 1 122 ? 24.600  45.015  -34.255 1.00 109.86 ? 122 ASP B O   1 
ATOM   5244  C CB  . ASP B 1 122 ? 21.922  45.825  -33.297 1.00 116.68 ? 122 ASP B CB  1 
ATOM   5245  C CG  . ASP B 1 122 ? 22.502  46.083  -31.903 1.00 117.60 ? 122 ASP B CG  1 
ATOM   5246  O OD1 . ASP B 1 122 ? 23.485  45.409  -31.514 1.00 115.12 ? 122 ASP B OD1 1 
ATOM   5247  O OD2 . ASP B 1 122 ? 21.971  46.989  -31.201 1.00 119.80 ? 122 ASP B OD2 1 
ATOM   5248  N N   . CYS B 1 123 ? 24.076  42.865  -33.747 1.00 108.90 ? 123 CYS B N   1 
ATOM   5249  C CA  . CYS B 1 123 ? 25.444  42.348  -33.856 1.00 105.57 ? 123 CYS B CA  1 
ATOM   5250  C C   . CYS B 1 123 ? 25.874  42.269  -35.323 1.00 102.61 ? 123 CYS B C   1 
ATOM   5251  O O   . CYS B 1 123 ? 27.040  42.507  -35.618 1.00 100.78 ? 123 CYS B O   1 
ATOM   5252  C CB  . CYS B 1 123 ? 25.660  41.007  -33.142 1.00 104.79 ? 123 CYS B CB  1 
ATOM   5253  S SG  . CYS B 1 123 ? 24.665  39.605  -33.742 1.00 104.46 ? 123 CYS B SG  1 
ATOM   5254  N N   . ILE B 1 124 ? 24.929  41.953  -36.228 1.00 102.53 ? 124 ILE B N   1 
ATOM   5255  C CA  . ILE B 1 124 ? 25.197  41.842  -37.659 1.00 100.34 ? 124 ILE B CA  1 
ATOM   5256  C C   . ILE B 1 124 ? 25.581  43.216  -38.203 1.00 100.07 ? 124 ILE B C   1 
ATOM   5257  O O   . ILE B 1 124 ? 24.752  44.133  -38.169 1.00 102.46 ? 124 ILE B O   1 
ATOM   5258  C CB  . ILE B 1 124 ? 23.988  41.270  -38.433 1.00 101.18 ? 124 ILE B CB  1 
ATOM   5259  C CG1 . ILE B 1 124 ? 23.591  39.857  -37.954 1.00 101.13 ? 124 ILE B CG1 1 
ATOM   5260  C CG2 . ILE B 1 124 ? 24.252  41.305  -39.944 1.00 99.61  ? 124 ILE B CG2 1 
ATOM   5261  C CD1 . ILE B 1 124 ? 22.450  39.223  -38.732 1.00 101.69 ? 124 ILE B CD1 1 
ATOM   5262  N N   . ILE B 1 125 ? 26.820  43.330  -38.719 1.00 97.26  ? 125 ILE B N   1 
ATOM   5263  C CA  . ILE B 1 125 ? 27.346  44.604  -39.188 1.00 97.06  ? 125 ILE B CA  1 
ATOM   5264  C C   . ILE B 1 125 ? 27.650  44.567  -40.687 1.00 95.48  ? 125 ILE B C   1 
ATOM   5265  O O   . ILE B 1 125 ? 28.139  45.564  -41.215 1.00 95.52  ? 125 ILE B O   1 
ATOM   5266  C CB  . ILE B 1 125 ? 28.580  45.036  -38.376 1.00 96.32  ? 125 ILE B CB  1 
ATOM   5267  C CG1 . ILE B 1 125 ? 29.732  44.074  -38.548 1.00 93.74  ? 125 ILE B CG1 1 
ATOM   5268  C CG2 . ILE B 1 125 ? 28.222  45.236  -36.904 1.00 98.24  ? 125 ILE B CG2 1 
ATOM   5269  C CD1 . ILE B 1 125 ? 31.011  44.518  -37.870 1.00 93.46  ? 125 ILE B CD1 1 
ATOM   5270  N N   . THR B 1 126 ? 27.352  43.451  -41.374 1.00 94.23  ? 126 THR B N   1 
ATOM   5271  C CA  . THR B 1 126 ? 27.434  43.419  -42.830 1.00 93.17  ? 126 THR B CA  1 
ATOM   5272  C C   . THR B 1 126 ? 26.871  42.106  -43.370 1.00 92.47  ? 126 THR B C   1 
ATOM   5273  O O   . THR B 1 126 ? 27.062  41.070  -42.747 1.00 92.23  ? 126 THR B O   1 
ATOM   5274  C CB  . THR B 1 126 ? 28.878  43.592  -43.293 1.00 91.24  ? 126 THR B CB  1 
ATOM   5275  O OG1 . THR B 1 126 ? 29.332  44.902  -42.962 1.00 92.04  ? 126 THR B OG1 1 
ATOM   5276  C CG2 . THR B 1 126 ? 29.005  43.403  -44.793 1.00 90.26  ? 126 THR B CG2 1 
ATOM   5277  N N   . TYR B 1 127 ? 26.225  42.160  -44.549 1.00 92.55  ? 127 TYR B N   1 
ATOM   5278  C CA  . TYR B 1 127 ? 25.723  40.980  -45.244 1.00 91.76  ? 127 TYR B CA  1 
ATOM   5279  C C   . TYR B 1 127 ? 26.604  40.705  -46.462 1.00 90.16  ? 127 TYR B C   1 
ATOM   5280  O O   . TYR B 1 127 ? 26.871  41.602  -47.260 1.00 89.98  ? 127 TYR B O   1 
ATOM   5281  C CB  . TYR B 1 127 ? 24.255  41.111  -45.682 1.00 93.11  ? 127 TYR B CB  1 
ATOM   5282  C CG  . TYR B 1 127 ? 23.220  41.013  -44.565 1.00 94.71  ? 127 TYR B CG  1 
ATOM   5283  C CD1 . TYR B 1 127 ? 22.874  42.124  -43.810 1.00 96.20  ? 127 TYR B CD1 1 
ATOM   5284  C CD2 . TYR B 1 127 ? 22.574  39.815  -44.275 1.00 94.97  ? 127 TYR B CD2 1 
ATOM   5285  C CE1 . TYR B 1 127 ? 21.933  42.047  -42.797 1.00 98.00  ? 127 TYR B CE1 1 
ATOM   5286  C CE2 . TYR B 1 127 ? 21.639  39.720  -43.257 1.00 96.74  ? 127 TYR B CE2 1 
ATOM   5287  C CZ  . TYR B 1 127 ? 21.314  40.844  -42.518 1.00 98.28  ? 127 TYR B CZ  1 
ATOM   5288  O OH  . TYR B 1 127 ? 20.396  40.790  -41.507 1.00 100.60 ? 127 TYR B OH  1 
ATOM   5289  N N   . LEU B 1 128 ? 27.066  39.455  -46.593 1.00 89.08  ? 128 LEU B N   1 
ATOM   5290  C CA  . LEU B 1 128 ? 27.731  39.025  -47.809 1.00 87.62  ? 128 LEU B CA  1 
ATOM   5291  C C   . LEU B 1 128 ? 26.728  38.262  -48.660 1.00 88.80  ? 128 LEU B C   1 
ATOM   5292  O O   . LEU B 1 128 ? 26.096  37.340  -48.182 1.00 90.95  ? 128 LEU B O   1 
ATOM   5293  C CB  . LEU B 1 128 ? 28.944  38.169  -47.473 1.00 85.88  ? 128 LEU B CB  1 
ATOM   5294  C CG  . LEU B 1 128 ? 29.975  38.798  -46.540 1.00 85.40  ? 128 LEU B CG  1 
ATOM   5295  C CD1 . LEU B 1 128 ? 31.088  37.792  -46.286 1.00 83.47  ? 128 LEU B CD1 1 
ATOM   5296  C CD2 . LEU B 1 128 ? 30.513  40.092  -47.126 1.00 85.63  ? 128 LEU B CD2 1 
ATOM   5297  N N   . VAL B 1 129 ? 26.579  38.642  -49.922 1.00 89.30  ? 129 VAL B N   1 
ATOM   5298  C CA  . VAL B 1 129 ? 25.445  38.182  -50.698 1.00 91.23  ? 129 VAL B CA  1 
ATOM   5299  C C   . VAL B 1 129 ? 25.797  36.923  -51.500 1.00 90.28  ? 129 VAL B C   1 
ATOM   5300  O O   . VAL B 1 129 ? 24.954  36.063  -51.724 1.00 90.33  ? 129 VAL B O   1 
ATOM   5301  C CB  . VAL B 1 129 ? 24.978  39.385  -51.541 1.00 93.24  ? 129 VAL B CB  1 
ATOM   5302  C CG1 . VAL B 1 129 ? 24.743  39.027  -53.002 1.00 94.10  ? 129 VAL B CG1 1 
ATOM   5303  C CG2 . VAL B 1 129 ? 23.747  40.057  -50.929 1.00 95.45  ? 129 VAL B CG2 1 
ATOM   5304  N N   . ILE B 1 130 ? 27.052  36.789  -51.923 1.00 89.69  ? 130 ILE B N   1 
ATOM   5305  C CA  . ILE B 1 130 ? 27.478  35.625  -52.682 1.00 89.81  ? 130 ILE B CA  1 
ATOM   5306  C C   . ILE B 1 130 ? 28.962  35.433  -52.419 1.00 88.84  ? 130 ILE B C   1 
ATOM   5307  O O   . ILE B 1 130 ? 29.601  36.381  -51.986 1.00 89.11  ? 130 ILE B O   1 
ATOM   5308  C CB  . ILE B 1 130 ? 27.178  35.812  -54.182 1.00 91.04  ? 130 ILE B CB  1 
ATOM   5309  C CG1 . ILE B 1 130 ? 27.394  34.523  -54.982 1.00 91.21  ? 130 ILE B CG1 1 
ATOM   5310  C CG2 . ILE B 1 130 ? 27.998  36.961  -54.769 1.00 90.34  ? 130 ILE B CG2 1 
ATOM   5311  C CD1 . ILE B 1 130 ? 26.775  34.544  -56.370 1.00 92.22  ? 130 ILE B CD1 1 
ATOM   5312  N N   . ASN B 1 131 ? 29.501  34.229  -52.678 1.00 89.37  ? 131 ASN B N   1 
ATOM   5313  C CA  . ASN B 1 131 ? 30.920  33.969  -52.446 1.00 88.44  ? 131 ASN B CA  1 
ATOM   5314  C C   . ASN B 1 131 ? 31.605  33.349  -53.673 1.00 86.61  ? 131 ASN B C   1 
ATOM   5315  O O   . ASN B 1 131 ? 31.216  32.293  -54.171 1.00 84.88  ? 131 ASN B O   1 
ATOM   5316  C CB  . ASN B 1 131 ? 31.117  33.134  -51.186 1.00 90.45  ? 131 ASN B CB  1 
ATOM   5317  C CG  . ASN B 1 131 ? 32.577  32.889  -50.861 1.00 90.92  ? 131 ASN B CG  1 
ATOM   5318  O OD1 . ASN B 1 131 ? 33.365  33.838  -50.784 1.00 92.81  ? 131 ASN B OD1 1 
ATOM   5319  N ND2 . ASN B 1 131 ? 32.964  31.638  -50.655 1.00 89.64  ? 131 ASN B ND2 1 
ATOM   5320  N N   . GLU B 1 132 ? 32.665  34.030  -54.124 1.00 86.66  ? 132 GLU B N   1 
ATOM   5321  C CA  . GLU B 1 132 ? 33.586  33.559  -55.150 1.00 88.82  ? 132 GLU B CA  1 
ATOM   5322  C C   . GLU B 1 132 ? 32.817  33.126  -56.400 1.00 88.70  ? 132 GLU B C   1 
ATOM   5323  O O   . GLU B 1 132 ? 32.978  32.006  -56.875 1.00 91.22  ? 132 GLU B O   1 
ATOM   5324  C CB  . GLU B 1 132 ? 34.541  32.461  -54.645 1.00 90.17  ? 132 GLU B CB  1 
ATOM   5325  C CG  . GLU B 1 132 ? 35.338  32.844  -53.395 1.00 92.07  ? 132 GLU B CG  1 
ATOM   5326  C CD  . GLU B 1 132 ? 36.576  32.025  -53.016 1.00 93.79  ? 132 GLU B CD  1 
ATOM   5327  O OE1 . GLU B 1 132 ? 37.629  32.236  -53.666 1.00 89.55  ? 132 GLU B OE1 1 
ATOM   5328  O OE2 . GLU B 1 132 ? 36.503  31.201  -52.055 1.00 97.07  ? 132 GLU B OE2 1 
ATOM   5329  N N   . PRO B 1 133 ? 32.010  34.001  -57.031 1.00 87.62  ? 133 PRO B N   1 
ATOM   5330  C CA  . PRO B 1 133 ? 31.503  33.724  -58.373 1.00 87.91  ? 133 PRO B CA  1 
ATOM   5331  C C   . PRO B 1 133 ? 32.642  33.612  -59.382 1.00 87.47  ? 133 PRO B C   1 
ATOM   5332  O O   . PRO B 1 133 ? 33.520  34.493  -59.448 1.00 86.26  ? 133 PRO B O   1 
ATOM   5333  C CB  . PRO B 1 133 ? 30.608  34.913  -58.674 1.00 88.71  ? 133 PRO B CB  1 
ATOM   5334  C CG  . PRO B 1 133 ? 31.167  36.009  -57.808 1.00 88.21  ? 133 PRO B CG  1 
ATOM   5335  C CD  . PRO B 1 133 ? 31.580  35.310  -56.525 1.00 87.90  ? 133 PRO B CD  1 
ATOM   5336  N N   . GLN B 1 134 ? 32.597  32.523  -60.166 1.00 86.77  ? 134 GLN B N   1 
ATOM   5337  C CA  . GLN B 1 134 ? 33.661  32.239  -61.113 1.00 86.24  ? 134 GLN B CA  1 
ATOM   5338  C C   . GLN B 1 134 ? 33.292  32.828  -62.473 1.00 85.26  ? 134 GLN B C   1 
ATOM   5339  O O   . GLN B 1 134 ? 32.155  32.734  -62.929 1.00 86.23  ? 134 GLN B O   1 
ATOM   5340  C CB  . GLN B 1 134 ? 34.038  30.756  -61.160 1.00 87.77  ? 134 GLN B CB  1 
ATOM   5341  C CG  . GLN B 1 134 ? 35.206  30.435  -62.087 1.00 89.73  ? 134 GLN B CG  1 
ATOM   5342  C CD  . GLN B 1 134 ? 36.540  30.958  -61.596 1.00 90.73  ? 134 GLN B CD  1 
ATOM   5343  O OE1 . GLN B 1 134 ? 36.997  30.577  -60.511 1.00 92.66  ? 134 GLN B OE1 1 
ATOM   5344  N NE2 . GLN B 1 134 ? 37.190  31.813  -62.385 1.00 90.75  ? 134 GLN B NE2 1 
ATOM   5345  N N   . THR B 1 135 ? 34.325  33.395  -63.091 1.00 83.43  ? 135 THR B N   1 
ATOM   5346  C CA  . THR B 1 135 ? 34.295  34.256  -64.258 1.00 84.13  ? 135 THR B CA  1 
ATOM   5347  C C   . THR B 1 135 ? 33.668  33.554  -65.459 1.00 83.92  ? 135 THR B C   1 
ATOM   5348  O O   . THR B 1 135 ? 32.742  34.077  -66.066 1.00 85.84  ? 135 THR B O   1 
ATOM   5349  C CB  . THR B 1 135 ? 35.756  34.680  -64.451 1.00 85.00  ? 135 THR B CB  1 
ATOM   5350  O OG1 . THR B 1 135 ? 35.840  35.680  -63.436 1.00 86.04  ? 135 THR B OG1 1 
ATOM   5351  C CG2 . THR B 1 135 ? 36.114  35.223  -65.824 1.00 86.13  ? 135 THR B CG2 1 
ATOM   5352  N N   . ASP B 1 136 ? 34.149  32.364  -65.813 1.00 83.35  ? 136 ASP B N   1 
ATOM   5353  C CA  . ASP B 1 136 ? 33.612  31.658  -66.971 1.00 83.96  ? 136 ASP B CA  1 
ATOM   5354  C C   . ASP B 1 136 ? 32.129  31.345  -66.759 1.00 84.85  ? 136 ASP B C   1 
ATOM   5355  O O   . ASP B 1 136 ? 31.356  31.255  -67.723 1.00 85.64  ? 136 ASP B O   1 
ATOM   5356  C CB  . ASP B 1 136 ? 34.429  30.419  -67.305 1.00 83.13  ? 136 ASP B CB  1 
ATOM   5357  C CG  . ASP B 1 136 ? 33.725  29.432  -68.219 1.00 83.72  ? 136 ASP B CG  1 
ATOM   5358  O OD1 . ASP B 1 136 ? 32.768  28.823  -67.745 1.00 84.63  ? 136 ASP B OD1 1 
ATOM   5359  O OD2 . ASP B 1 136 ? 34.110  29.305  -69.393 1.00 83.71  ? 136 ASP B OD2 1 
ATOM   5360  N N   . HIS B 1 137 ? 31.752  31.186  -65.483 1.00 84.12  ? 137 HIS B N   1 
ATOM   5361  C CA  . HIS B 1 137 ? 30.374  30.932  -65.106 1.00 85.08  ? 137 HIS B CA  1 
ATOM   5362  C C   . HIS B 1 137 ? 29.504  32.159  -65.352 1.00 86.05  ? 137 HIS B C   1 
ATOM   5363  O O   . HIS B 1 137 ? 28.346  32.012  -65.751 1.00 87.73  ? 137 HIS B O   1 
ATOM   5364  C CB  . HIS B 1 137 ? 30.243  30.552  -63.630 1.00 84.30  ? 137 HIS B CB  1 
ATOM   5365  C CG  . HIS B 1 137 ? 28.836  30.219  -63.319 1.00 85.81  ? 137 HIS B CG  1 
ATOM   5366  N ND1 . HIS B 1 137 ? 28.072  30.927  -62.416 1.00 85.67  ? 137 HIS B ND1 1 
ATOM   5367  C CD2 . HIS B 1 137 ? 28.031  29.330  -63.890 1.00 87.40  ? 137 HIS B CD2 1 
ATOM   5368  C CE1 . HIS B 1 137 ? 26.857  30.416  -62.397 1.00 87.58  ? 137 HIS B CE1 1 
ATOM   5369  N NE2 . HIS B 1 137 ? 26.798  29.460  -63.299 1.00 88.28  ? 137 HIS B NE2 1 
ATOM   5370  N N   . ILE B 1 138 ? 30.049  33.353  -65.066 1.00 84.68  ? 138 ILE B N   1 
ATOM   5371  C CA  . ILE B 1 138 ? 29.302  34.587  -65.241 1.00 85.09  ? 138 ILE B CA  1 
ATOM   5372  C C   . ILE B 1 138 ? 29.040  34.767  -66.735 1.00 86.37  ? 138 ILE B C   1 
ATOM   5373  O O   . ILE B 1 138 ? 27.897  34.971  -67.149 1.00 87.23  ? 138 ILE B O   1 
ATOM   5374  C CB  . ILE B 1 138 ? 30.043  35.768  -64.587 1.00 83.80  ? 138 ILE B CB  1 
ATOM   5375  C CG1 . ILE B 1 138 ? 30.126  35.570  -63.075 1.00 82.93  ? 138 ILE B CG1 1 
ATOM   5376  C CG2 . ILE B 1 138 ? 29.401  37.114  -64.938 1.00 84.80  ? 138 ILE B CG2 1 
ATOM   5377  C CD1 . ILE B 1 138 ? 30.794  36.702  -62.316 1.00 82.27  ? 138 ILE B CD1 1 
ATOM   5378  N N   . HIS B 1 139 ? 30.108  34.611  -67.527 1.00 86.03  ? 139 HIS B N   1 
ATOM   5379  C CA  . HIS B 1 139 ? 30.032  34.637  -68.980 1.00 87.96  ? 139 HIS B CA  1 
ATOM   5380  C C   . HIS B 1 139 ? 28.941  33.693  -69.500 1.00 89.72  ? 139 HIS B C   1 
ATOM   5381  O O   . HIS B 1 139 ? 28.216  34.044  -70.430 1.00 91.88  ? 139 HIS B O   1 
ATOM   5382  C CB  . HIS B 1 139 ? 31.407  34.306  -69.581 1.00 87.22  ? 139 HIS B CB  1 
ATOM   5383  C CG  . HIS B 1 139 ? 31.465  34.402  -71.071 1.00 88.91  ? 139 HIS B CG  1 
ATOM   5384  N ND1 . HIS B 1 139 ? 31.800  35.570  -71.730 1.00 89.45  ? 139 HIS B ND1 1 
ATOM   5385  C CD2 . HIS B 1 139 ? 31.229  33.482  -72.025 1.00 89.97  ? 139 HIS B CD2 1 
ATOM   5386  C CE1 . HIS B 1 139 ? 31.766  35.359  -73.041 1.00 90.83  ? 139 HIS B CE1 1 
ATOM   5387  N NE2 . HIS B 1 139 ? 31.426  34.094  -73.243 1.00 91.41  ? 139 HIS B NE2 1 
ATOM   5388  N N   . SER B 1 140 ? 28.819  32.501  -68.895 1.00 89.05  ? 140 SER B N   1 
ATOM   5389  C CA  . SER B 1 140 ? 27.925  31.459  -69.389 1.00 89.91  ? 140 SER B CA  1 
ATOM   5390  C C   . SER B 1 140 ? 26.476  31.705  -68.968 1.00 91.84  ? 140 SER B C   1 
ATOM   5391  O O   . SER B 1 140 ? 25.550  31.130  -69.545 1.00 94.16  ? 140 SER B O   1 
ATOM   5392  C CB  . SER B 1 140 ? 28.376  30.093  -68.928 1.00 88.62  ? 140 SER B CB  1 
ATOM   5393  O OG  . SER B 1 140 ? 27.900  29.090  -69.810 1.00 89.31  ? 140 SER B OG  1 
ATOM   5394  N N   . VAL B 1 141 ? 26.261  32.501  -67.918 1.00 91.14  ? 141 VAL B N   1 
ATOM   5395  C CA  . VAL B 1 141 ? 24.896  32.791  -67.502 1.00 92.57  ? 141 VAL B CA  1 
ATOM   5396  C C   . VAL B 1 141 ? 24.582  34.274  -67.739 1.00 93.10  ? 141 VAL B C   1 
ATOM   5397  O O   . VAL B 1 141 ? 23.420  34.680  -67.609 1.00 93.14  ? 141 VAL B O   1 
ATOM   5398  C CB  . VAL B 1 141 ? 24.636  32.340  -66.050 1.00 91.85  ? 141 VAL B CB  1 
ATOM   5399  C CG1 . VAL B 1 141 ? 24.865  30.842  -65.883 1.00 91.22  ? 141 VAL B CG1 1 
ATOM   5400  C CG2 . VAL B 1 141 ? 25.444  33.148  -65.037 1.00 90.39  ? 141 VAL B CG2 1 
ATOM   5401  N N   . THR B 1 142 ? 25.641  35.035  -68.099 1.00 92.16  ? 142 THR B N   1 
ATOM   5402  C CA  . THR B 1 142 ? 25.601  36.406  -68.606 1.00 92.70  ? 142 THR B CA  1 
ATOM   5403  C C   . THR B 1 142 ? 25.876  37.383  -67.464 1.00 91.86  ? 142 THR B C   1 
ATOM   5404  O O   . THR B 1 142 ? 25.436  37.176  -66.332 1.00 90.97  ? 142 THR B O   1 
ATOM   5405  C CB  . THR B 1 142 ? 24.303  36.771  -69.331 1.00 94.45  ? 142 THR B CB  1 
ATOM   5406  O OG1 . THR B 1 142 ? 23.303  36.710  -68.323 1.00 95.42  ? 142 THR B OG1 1 
ATOM   5407  C CG2 . THR B 1 142 ? 23.987  35.869  -70.512 1.00 95.22  ? 142 THR B CG2 1 
ATOM   5408  N N   . GLY B 1 143 ? 26.610  38.455  -67.797 1.00 92.13  ? 143 GLY B N   1 
ATOM   5409  C CA  . GLY B 1 143 ? 26.865  39.550  -66.877 1.00 91.92  ? 143 GLY B CA  1 
ATOM   5410  C C   . GLY B 1 143 ? 25.571  40.236  -66.437 1.00 94.00  ? 143 GLY B C   1 
ATOM   5411  O O   . GLY B 1 143 ? 25.534  40.856  -65.374 1.00 94.26  ? 143 GLY B O   1 
ATOM   5412  N N   . LYS B 1 144 ? 24.512  40.119  -67.252 1.00 95.60  ? 144 LYS B N   1 
ATOM   5413  C CA  . LYS B 1 144 ? 23.240  40.747  -66.929 1.00 97.82  ? 144 LYS B CA  1 
ATOM   5414  C C   . LYS B 1 144 ? 22.523  39.979  -65.818 1.00 97.90  ? 144 LYS B C   1 
ATOM   5415  O O   . LYS B 1 144 ? 21.921  40.583  -64.933 1.00 99.25  ? 144 LYS B O   1 
ATOM   5416  C CB  . LYS B 1 144 ? 22.323  40.889  -68.153 1.00 100.05 ? 144 LYS B CB  1 
ATOM   5417  C CG  . LYS B 1 144 ? 21.015  41.650  -67.911 1.00 101.64 ? 144 LYS B CG  1 
ATOM   5418  C CD  . LYS B 1 144 ? 20.443  42.303  -69.165 1.00 103.67 ? 144 LYS B CD  1 
ATOM   5419  C CE  . LYS B 1 144 ? 19.059  42.817  -68.971 1.00 105.56 ? 144 LYS B CE  1 
ATOM   5420  N NZ  . LYS B 1 144 ? 19.031  43.786  -67.876 1.00 105.67 ? 144 LYS B NZ  1 
ATOM   5421  N N   . ALA B 1 145 ? 22.544  38.647  -65.893 1.00 97.24  ? 145 ALA B N   1 
ATOM   5422  C CA  . ALA B 1 145 ? 21.909  37.823  -64.877 1.00 97.06  ? 145 ALA B CA  1 
ATOM   5423  C C   . ALA B 1 145 ? 22.576  38.046  -63.518 1.00 95.78  ? 145 ALA B C   1 
ATOM   5424  O O   . ALA B 1 145 ? 21.893  38.056  -62.496 1.00 96.40  ? 145 ALA B O   1 
ATOM   5425  C CB  . ALA B 1 145 ? 21.953  36.367  -65.292 1.00 96.63  ? 145 ALA B CB  1 
ATOM   5426  N N   . PHE B 1 146 ? 23.905  38.250  -63.520 1.00 94.31  ? 146 PHE B N   1 
ATOM   5427  C CA  . PHE B 1 146 ? 24.677  38.374  -62.291 1.00 92.76  ? 146 PHE B CA  1 
ATOM   5428  C C   . PHE B 1 146 ? 24.348  39.708  -61.615 1.00 94.85  ? 146 PHE B C   1 
ATOM   5429  O O   . PHE B 1 146 ? 23.866  39.719  -60.483 1.00 96.69  ? 146 PHE B O   1 
ATOM   5430  C CB  . PHE B 1 146 ? 26.181  38.174  -62.531 1.00 89.45  ? 146 PHE B CB  1 
ATOM   5431  C CG  . PHE B 1 146 ? 27.036  38.409  -61.291 1.00 86.84  ? 146 PHE B CG  1 
ATOM   5432  C CD1 . PHE B 1 146 ? 27.197  37.415  -60.334 1.00 85.45  ? 146 PHE B CD1 1 
ATOM   5433  C CD2 . PHE B 1 146 ? 27.671  39.631  -61.083 1.00 86.05  ? 146 PHE B CD2 1 
ATOM   5434  C CE1 . PHE B 1 146 ? 27.953  37.644  -59.197 1.00 84.14  ? 146 PHE B CE1 1 
ATOM   5435  C CE2 . PHE B 1 146 ? 28.426  39.865  -59.944 1.00 84.50  ? 146 PHE B CE2 1 
ATOM   5436  C CZ  . PHE B 1 146 ? 28.557  38.876  -59.001 1.00 84.00  ? 146 PHE B CZ  1 
ATOM   5437  N N   . VAL B 1 147 ? 24.586  40.835  -62.292 1.00 95.94  ? 147 VAL B N   1 
ATOM   5438  C CA  . VAL B 1 147 ? 24.308  42.123  -61.668 1.00 98.64  ? 147 VAL B CA  1 
ATOM   5439  C C   . VAL B 1 147 ? 22.862  42.123  -61.148 1.00 99.07  ? 147 VAL B C   1 
ATOM   5440  O O   . VAL B 1 147 ? 22.621  42.424  -59.977 1.00 98.00  ? 147 VAL B O   1 
ATOM   5441  C CB  . VAL B 1 147 ? 24.576  43.357  -62.562 1.00 101.44 ? 147 VAL B CB  1 
ATOM   5442  C CG1 . VAL B 1 147 ? 23.819  43.306  -63.885 1.00 104.49 ? 147 VAL B CG1 1 
ATOM   5443  C CG2 . VAL B 1 147 ? 24.234  44.664  -61.850 1.00 102.60 ? 147 VAL B CG2 1 
ATOM   5444  N N   . ASP B 1 148 ? 21.911  41.752  -62.018 1.00 99.99  ? 148 ASP B N   1 
ATOM   5445  C CA  . ASP B 1 148 ? 20.488  41.833  -61.713 1.00 101.43 ? 148 ASP B CA  1 
ATOM   5446  C C   . ASP B 1 148 ? 20.188  41.063  -60.427 1.00 100.89 ? 148 ASP B C   1 
ATOM   5447  O O   . ASP B 1 148 ? 19.464  41.557  -59.563 1.00 103.52 ? 148 ASP B O   1 
ATOM   5448  C CB  . ASP B 1 148 ? 19.645  41.410  -62.908 1.00 102.18 ? 148 ASP B CB  1 
ATOM   5449  C CG  . ASP B 1 148 ? 19.507  42.450  -64.011 1.00 103.21 ? 148 ASP B CG  1 
ATOM   5450  O OD1 . ASP B 1 148 ? 19.644  43.655  -63.703 1.00 103.26 ? 148 ASP B OD1 1 
ATOM   5451  O OD2 . ASP B 1 148 ? 19.281  42.047  -65.172 1.00 103.75 ? 148 ASP B OD2 1 
ATOM   5452  N N   . LEU B 1 149 ? 20.754  39.861  -60.288 1.00 98.20  ? 149 LEU B N   1 
ATOM   5453  C CA  . LEU B 1 149 ? 20.600  39.115  -59.053 1.00 97.18  ? 149 LEU B CA  1 
ATOM   5454  C C   . LEU B 1 149 ? 21.162  39.922  -57.883 1.00 96.01  ? 149 LEU B C   1 
ATOM   5455  O O   . LEU B 1 149 ? 20.504  40.024  -56.849 1.00 97.20  ? 149 LEU B O   1 
ATOM   5456  C CB  . LEU B 1 149 ? 21.277  37.755  -59.152 1.00 95.75  ? 149 LEU B CB  1 
ATOM   5457  C CG  . LEU B 1 149 ? 20.903  36.757  -58.054 1.00 95.80  ? 149 LEU B CG  1 
ATOM   5458  C CD1 . LEU B 1 149 ? 19.505  36.281  -58.289 1.00 97.99  ? 149 LEU B CD1 1 
ATOM   5459  C CD2 . LEU B 1 149 ? 21.840  35.571  -57.983 1.00 94.67  ? 149 LEU B CD2 1 
ATOM   5460  N N   . MET B 1 150 ? 22.356  40.507  -58.063 1.00 93.33  ? 150 MET B N   1 
ATOM   5461  C CA  . MET B 1 150 ? 22.998  41.290  -57.017 1.00 92.62  ? 150 MET B CA  1 
ATOM   5462  C C   . MET B 1 150 ? 22.134  42.483  -56.594 1.00 94.09  ? 150 MET B C   1 
ATOM   5463  O O   . MET B 1 150 ? 21.892  42.696  -55.407 1.00 93.97  ? 150 MET B O   1 
ATOM   5464  C CB  . MET B 1 150 ? 24.367  41.821  -57.466 1.00 91.68  ? 150 MET B CB  1 
ATOM   5465  C CG  . MET B 1 150 ? 25.444  40.772  -57.693 1.00 89.59  ? 150 MET B CG  1 
ATOM   5466  S SD  . MET B 1 150 ? 25.898  39.833  -56.219 1.00 88.48  ? 150 MET B SD  1 
ATOM   5467  C CE  . MET B 1 150 ? 24.863  38.398  -56.540 1.00 90.08  ? 150 MET B CE  1 
ATOM   5468  N N   . ASN B 1 151 ? 21.677  43.280  -57.561 1.00 95.38  ? 151 ASN B N   1 
ATOM   5469  C CA  . ASN B 1 151 ? 20.775  44.385  -57.266 1.00 97.67  ? 151 ASN B CA  1 
ATOM   5470  C C   . ASN B 1 151 ? 19.557  43.901  -56.476 1.00 98.59  ? 151 ASN B C   1 
ATOM   5471  O O   . ASN B 1 151 ? 19.142  44.560  -55.525 1.00 99.69  ? 151 ASN B O   1 
ATOM   5472  C CB  . ASN B 1 151 ? 20.385  45.150  -58.529 1.00 99.60  ? 151 ASN B CB  1 
ATOM   5473  C CG  . ASN B 1 151 ? 21.464  46.115  -58.974 1.00 99.76  ? 151 ASN B CG  1 
ATOM   5474  O OD1 . ASN B 1 151 ? 21.921  46.073  -60.123 1.00 99.93  ? 151 ASN B OD1 1 
ATOM   5475  N ND2 . ASN B 1 151 ? 21.882  47.012  -58.091 1.00 100.28 ? 151 ASN B ND2 1 
ATOM   5476  N N   . THR B 1 152 ? 19.000  42.743  -56.857 1.00 98.42  ? 152 THR B N   1 
ATOM   5477  C CA  . THR B 1 152 ? 17.769  42.222  -56.271 1.00 99.77  ? 152 THR B CA  1 
ATOM   5478  C C   . THR B 1 152 ? 17.970  41.816  -54.810 1.00 99.62  ? 152 THR B C   1 
ATOM   5479  O O   . THR B 1 152 ? 17.134  42.137  -53.971 1.00 100.85 ? 152 THR B O   1 
ATOM   5480  C CB  . THR B 1 152 ? 17.269  41.052  -57.115 1.00 99.44  ? 152 THR B CB  1 
ATOM   5481  O OG1 . THR B 1 152 ? 16.952  41.698  -58.346 1.00 100.01 ? 152 THR B OG1 1 
ATOM   5482  C CG2 . THR B 1 152 ? 16.071  40.357  -56.495 1.00 101.03 ? 152 THR B CG2 1 
ATOM   5483  N N   . LEU B 1 153 ? 19.057  41.088  -54.500 1.00 98.23  ? 153 LEU B N   1 
ATOM   5484  C CA  . LEU B 1 153 ? 19.351  40.752  -53.110 1.00 97.99  ? 153 LEU B CA  1 
ATOM   5485  C C   . LEU B 1 153 ? 19.628  42.039  -52.324 1.00 99.44  ? 153 LEU B C   1 
ATOM   5486  O O   . LEU B 1 153 ? 18.992  42.291  -51.294 1.00 100.34 ? 153 LEU B O   1 
ATOM   5487  C CB  . LEU B 1 153 ? 20.497  39.755  -52.976 1.00 95.28  ? 153 LEU B CB  1 
ATOM   5488  C CG  . LEU B 1 153 ? 20.199  38.305  -53.380 1.00 94.88  ? 153 LEU B CG  1 
ATOM   5489  C CD1 . LEU B 1 153 ? 18.825  37.808  -52.978 1.00 96.30  ? 153 LEU B CD1 1 
ATOM   5490  C CD2 . LEU B 1 153 ? 20.403  38.080  -54.862 1.00 94.55  ? 153 LEU B CD2 1 
ATOM   5491  N N   . ILE B 1 154 ? 20.566  42.857  -52.837 1.00 99.24  ? 154 ILE B N   1 
ATOM   5492  C CA  . ILE B 1 154 ? 20.976  44.090  -52.178 1.00 99.58  ? 154 ILE B CA  1 
ATOM   5493  C C   . ILE B 1 154 ? 19.734  44.826  -51.693 1.00 102.55 ? 154 ILE B C   1 
ATOM   5494  O O   . ILE B 1 154 ? 19.611  45.103  -50.503 1.00 103.76 ? 154 ILE B O   1 
ATOM   5495  C CB  . ILE B 1 154 ? 21.838  44.969  -53.104 1.00 98.42  ? 154 ILE B CB  1 
ATOM   5496  C CG1 . ILE B 1 154 ? 23.243  44.418  -53.219 1.00 95.34  ? 154 ILE B CG1 1 
ATOM   5497  C CG2 . ILE B 1 154 ? 21.845  46.433  -52.644 1.00 99.98  ? 154 ILE B CG2 1 
ATOM   5498  C CD1 . ILE B 1 154 ? 24.017  44.953  -54.411 1.00 94.79  ? 154 ILE B CD1 1 
ATOM   5499  N N   . ASN B 1 155 ? 18.823  45.132  -52.623 1.00 104.45 ? 155 ASN B N   1 
ATOM   5500  C CA  . ASN B 1 155 ? 17.706  46.009  -52.315 1.00 107.73 ? 155 ASN B CA  1 
ATOM   5501  C C   . ASN B 1 155 ? 16.862  45.372  -51.206 1.00 109.25 ? 155 ASN B C   1 
ATOM   5502  O O   . ASN B 1 155 ? 16.475  46.047  -50.254 1.00 112.61 ? 155 ASN B O   1 
ATOM   5503  C CB  . ASN B 1 155 ? 16.921  46.387  -53.573 1.00 109.36 ? 155 ASN B CB  1 
ATOM   5504  C CG  . ASN B 1 155 ? 17.686  47.288  -54.528 1.00 108.56 ? 155 ASN B CG  1 
ATOM   5505  O OD1 . ASN B 1 155 ? 18.282  48.292  -54.114 1.00 108.36 ? 155 ASN B OD1 1 
ATOM   5506  N ND2 . ASN B 1 155 ? 17.661  46.973  -55.817 1.00 108.00 ? 155 ASN B ND2 1 
ATOM   5507  N N   . ILE B 1 156 ? 16.608  44.064  -51.325 1.00 108.26 ? 156 ILE B N   1 
ATOM   5508  C CA  . ILE B 1 156 ? 15.786  43.321  -50.381 1.00 109.31 ? 156 ILE B CA  1 
ATOM   5509  C C   . ILE B 1 156 ? 16.347  43.467  -48.964 1.00 108.56 ? 156 ILE B C   1 
ATOM   5510  O O   . ILE B 1 156 ? 15.575  43.486  -48.009 1.00 110.02 ? 156 ILE B O   1 
ATOM   5511  C CB  . ILE B 1 156 ? 15.670  41.850  -50.838 1.00 108.77 ? 156 ILE B CB  1 
ATOM   5512  C CG1 . ILE B 1 156 ? 14.675  41.710  -51.992 1.00 110.05 ? 156 ILE B CG1 1 
ATOM   5513  C CG2 . ILE B 1 156 ? 15.312  40.907  -49.686 1.00 109.59 ? 156 ILE B CG2 1 
ATOM   5514  C CD1 . ILE B 1 156 ? 14.704  40.348  -52.662 1.00 108.80 ? 156 ILE B CD1 1 
ATOM   5515  N N   . ILE B 1 157 ? 17.679  43.555  -48.836 1.00 106.61 ? 157 ILE B N   1 
ATOM   5516  C CA  . ILE B 1 157 ? 18.352  43.600  -47.543 1.00 106.16 ? 157 ILE B CA  1 
ATOM   5517  C C   . ILE B 1 157 ? 18.294  45.018  -46.975 1.00 108.21 ? 157 ILE B C   1 
ATOM   5518  O O   . ILE B 1 157 ? 18.165  45.177  -45.761 1.00 108.99 ? 157 ILE B O   1 
ATOM   5519  C CB  . ILE B 1 157 ? 19.809  43.101  -47.650 1.00 103.03 ? 157 ILE B CB  1 
ATOM   5520  C CG1 . ILE B 1 157 ? 19.893  41.645  -48.129 1.00 101.51 ? 157 ILE B CG1 1 
ATOM   5521  C CG2 . ILE B 1 157 ? 20.540  43.292  -46.318 1.00 102.94 ? 157 ILE B CG2 1 
ATOM   5522  C CD1 . ILE B 1 157 ? 21.312  41.107  -48.330 1.00 98.75  ? 157 ILE B CD1 1 
ATOM   5523  N N   . HIS B 1 158 ? 18.438  46.030  -47.852 1.00 108.99 ? 158 HIS B N   1 
ATOM   5524  C CA  . HIS B 1 158 ? 18.345  47.427  -47.456 1.00 111.15 ? 158 HIS B CA  1 
ATOM   5525  C C   . HIS B 1 158 ? 16.961  47.721  -46.889 1.00 114.27 ? 158 HIS B C   1 
ATOM   5526  O O   . HIS B 1 158 ? 16.852  48.576  -46.015 1.00 116.87 ? 158 HIS B O   1 
ATOM   5527  C CB  . HIS B 1 158 ? 18.637  48.389  -48.616 1.00 111.53 ? 158 HIS B CB  1 
ATOM   5528  C CG  . HIS B 1 158 ? 20.085  48.592  -48.950 1.00 109.62 ? 158 HIS B CG  1 
ATOM   5529  N ND1 . HIS B 1 158 ? 20.478  49.259  -50.095 1.00 109.84 ? 158 HIS B ND1 1 
ATOM   5530  C CD2 . HIS B 1 158 ? 21.217  48.278  -48.304 1.00 107.25 ? 158 HIS B CD2 1 
ATOM   5531  C CE1 . HIS B 1 158 ? 21.802  49.303  -50.145 1.00 107.22 ? 158 HIS B CE1 1 
ATOM   5532  N NE2 . HIS B 1 158 ? 22.268  48.720  -49.065 1.00 105.47 ? 158 HIS B NE2 1 
ATOM   5533  N N   . LYS B 1 159 ? 15.928  47.021  -47.396 1.00 115.11 ? 159 LYS B N   1 
ATOM   5534  C CA  . LYS B 1 159 ? 14.540  47.220  -46.994 1.00 118.17 ? 159 LYS B CA  1 
ATOM   5535  C C   . LYS B 1 159 ? 14.113  46.296  -45.850 1.00 117.06 ? 159 LYS B C   1 
ATOM   5536  O O   . LYS B 1 159 ? 13.295  46.667  -45.019 1.00 118.63 ? 159 LYS B O   1 
ATOM   5537  C CB  . LYS B 1 159 ? 13.636  47.022  -48.214 1.00 120.81 ? 159 LYS B CB  1 
ATOM   5538  C CG  . LYS B 1 159 ? 13.690  48.171  -49.224 1.00 123.17 ? 159 LYS B CG  1 
ATOM   5539  C CD  . LYS B 1 159 ? 12.355  48.502  -49.890 1.00 126.29 ? 159 LYS B CD  1 
ATOM   5540  C CE  . LYS B 1 159 ? 11.961  47.527  -50.959 1.00 126.28 ? 159 LYS B CE  1 
ATOM   5541  N NZ  . LYS B 1 159 ? 10.634  47.863  -51.488 1.00 129.90 ? 159 LYS B NZ  1 
ATOM   5542  N N   . GLY B 1 160 ? 14.658  45.082  -45.823 1.00 114.67 ? 160 GLY B N   1 
ATOM   5543  C CA  . GLY B 1 160 ? 14.366  44.110  -44.780 1.00 114.98 ? 160 GLY B CA  1 
ATOM   5544  C C   . GLY B 1 160 ? 15.218  44.286  -43.517 1.00 114.46 ? 160 GLY B C   1 
ATOM   5545  O O   . GLY B 1 160 ? 14.696  44.089  -42.423 1.00 116.03 ? 160 GLY B O   1 
ATOM   5546  N N   . HIS B 1 161 ? 16.531  44.581  -43.660 1.00 112.28 ? 161 HIS B N   1 
ATOM   5547  C CA  . HIS B 1 161 ? 17.382  44.943  -42.528 1.00 111.09 ? 161 HIS B CA  1 
ATOM   5548  C C   . HIS B 1 161 ? 18.132  46.240  -42.833 1.00 110.52 ? 161 HIS B C   1 
ATOM   5549  O O   . HIS B 1 161 ? 19.249  46.207  -43.336 1.00 108.69 ? 161 HIS B O   1 
ATOM   5550  C CB  . HIS B 1 161 ? 18.330  43.800  -42.150 1.00 108.40 ? 161 HIS B CB  1 
ATOM   5551  C CG  . HIS B 1 161 ? 18.927  43.980  -40.789 1.00 108.82 ? 161 HIS B CG  1 
ATOM   5552  N ND1 . HIS B 1 161 ? 19.766  43.051  -40.207 1.00 107.22 ? 161 HIS B ND1 1 
ATOM   5553  C CD2 . HIS B 1 161 ? 18.834  44.999  -39.911 1.00 110.77 ? 161 HIS B CD2 1 
ATOM   5554  C CE1 . HIS B 1 161 ? 20.154  43.494  -39.017 1.00 108.06 ? 161 HIS B CE1 1 
ATOM   5555  N NE2 . HIS B 1 161 ? 19.597  44.674  -38.815 1.00 110.29 ? 161 HIS B NE2 1 
ATOM   5556  N N   . PRO B 1 162 ? 17.552  47.427  -42.527 1.00 113.29 ? 162 PRO B N   1 
ATOM   5557  C CA  . PRO B 1 162 ? 18.107  48.701  -42.981 1.00 113.34 ? 162 PRO B CA  1 
ATOM   5558  C C   . PRO B 1 162 ? 19.335  49.116  -42.187 1.00 112.79 ? 162 PRO B C   1 
ATOM   5559  O O   . PRO B 1 162 ? 19.593  48.609  -41.092 1.00 112.94 ? 162 PRO B O   1 
ATOM   5560  C CB  . PRO B 1 162 ? 16.949  49.675  -42.780 1.00 116.37 ? 162 PRO B CB  1 
ATOM   5561  C CG  . PRO B 1 162 ? 16.232  49.122  -41.577 1.00 117.93 ? 162 PRO B CG  1 
ATOM   5562  C CD  . PRO B 1 162 ? 16.326  47.618  -41.734 1.00 116.05 ? 162 PRO B CD  1 
ATOM   5563  N N   . GLY B 1 163 ? 20.090  50.031  -42.796 1.00 112.35 ? 163 GLY B N   1 
ATOM   5564  C CA  . GLY B 1 163 ? 21.252  50.622  -42.168 1.00 111.75 ? 163 GLY B CA  1 
ATOM   5565  C C   . GLY B 1 163 ? 22.390  49.625  -41.996 1.00 108.78 ? 163 GLY B C   1 
ATOM   5566  O O   . GLY B 1 163 ? 23.287  49.926  -41.218 1.00 108.87 ? 163 GLY B O   1 
ATOM   5567  N N   . ILE B 1 164 ? 22.355  48.479  -42.712 1.00 106.92 ? 164 ILE B N   1 
ATOM   5568  C CA  . ILE B 1 164 ? 23.401  47.455  -42.610 1.00 104.34 ? 164 ILE B CA  1 
ATOM   5569  C C   . ILE B 1 164 ? 24.145  47.272  -43.940 1.00 101.70 ? 164 ILE B C   1 
ATOM   5570  O O   . ILE B 1 164 ? 23.616  46.705  -44.891 1.00 100.97 ? 164 ILE B O   1 
ATOM   5571  C CB  . ILE B 1 164 ? 22.836  46.094  -42.157 1.00 104.02 ? 164 ILE B CB  1 
ATOM   5572  C CG1 . ILE B 1 164 ? 22.101  46.152  -40.805 1.00 106.34 ? 164 ILE B CG1 1 
ATOM   5573  C CG2 . ILE B 1 164 ? 23.957  45.050  -42.149 1.00 101.31 ? 164 ILE B CG2 1 
ATOM   5574  C CD1 . ILE B 1 164 ? 22.983  46.499  -39.618 1.00 106.46 ? 164 ILE B CD1 1 
ATOM   5575  N N   . PRO B 1 165 ? 25.443  47.626  -44.041 1.00 100.49 ? 165 PRO B N   1 
ATOM   5576  C CA  . PRO B 1 165 ? 26.181  47.440  -45.294 1.00 99.05  ? 165 PRO B CA  1 
ATOM   5577  C C   . PRO B 1 165 ? 26.047  46.042  -45.909 1.00 98.22  ? 165 PRO B C   1 
ATOM   5578  O O   . PRO B 1 165 ? 25.966  45.036  -45.205 1.00 97.68  ? 165 PRO B O   1 
ATOM   5579  C CB  . PRO B 1 165 ? 27.641  47.762  -44.910 1.00 97.19  ? 165 PRO B CB  1 
ATOM   5580  C CG  . PRO B 1 165 ? 27.536  48.647  -43.690 1.00 99.02  ? 165 PRO B CG  1 
ATOM   5581  C CD  . PRO B 1 165 ? 26.274  48.198  -42.969 1.00 100.87 ? 165 PRO B CD  1 
ATOM   5582  N N   . VAL B 1 166 ? 26.014  46.010  -47.247 1.00 97.88  ? 166 VAL B N   1 
ATOM   5583  C CA  . VAL B 1 166 ? 25.853  44.800  -48.032 1.00 96.36  ? 166 VAL B CA  1 
ATOM   5584  C C   . VAL B 1 166 ? 27.017  44.772  -49.011 1.00 95.53  ? 166 VAL B C   1 
ATOM   5585  O O   . VAL B 1 166 ? 27.273  45.782  -49.660 1.00 96.77  ? 166 VAL B O   1 
ATOM   5586  C CB  . VAL B 1 166 ? 24.512  44.788  -48.797 1.00 97.95  ? 166 VAL B CB  1 
ATOM   5587  C CG1 . VAL B 1 166 ? 24.377  43.564  -49.694 1.00 97.19  ? 166 VAL B CG1 1 
ATOM   5588  C CG2 . VAL B 1 166 ? 23.305  44.912  -47.873 1.00 99.61  ? 166 VAL B CG2 1 
ATOM   5589  N N   . THR B 1 167 ? 27.722  43.635  -49.096 1.00 94.11  ? 167 THR B N   1 
ATOM   5590  C CA  . THR B 1 167 ? 28.750  43.438  -50.105 1.00 91.73  ? 167 THR B CA  1 
ATOM   5591  C C   . THR B 1 167 ? 28.802  41.947  -50.415 1.00 89.52  ? 167 THR B C   1 
ATOM   5592  O O   . THR B 1 167 ? 27.852  41.249  -50.068 1.00 89.45  ? 167 THR B O   1 
ATOM   5593  C CB  . THR B 1 167 ? 30.088  44.014  -49.635 1.00 91.24  ? 167 THR B CB  1 
ATOM   5594  O OG1 . THR B 1 167 ? 30.995  43.806  -50.710 1.00 90.09  ? 167 THR B OG1 1 
ATOM   5595  C CG2 . THR B 1 167 ? 30.660  43.336  -48.402 1.00 90.55  ? 167 THR B CG2 1 
ATOM   5596  N N   . LEU B 1 168 ? 29.899  41.506  -51.068 1.00 87.30  ? 168 LEU B N   1 
ATOM   5597  C CA  . LEU B 1 168 ? 30.098  40.122  -51.475 1.00 86.13  ? 168 LEU B CA  1 
ATOM   5598  C C   . LEU B 1 168 ? 31.547  39.687  -51.216 1.00 86.17  ? 168 LEU B C   1 
ATOM   5599  O O   . LEU B 1 168 ? 32.400  40.505  -50.860 1.00 86.36  ? 168 LEU B O   1 
ATOM   5600  C CB  . LEU B 1 168 ? 29.710  39.970  -52.948 1.00 85.38  ? 168 LEU B CB  1 
ATOM   5601  C CG  . LEU B 1 168 ? 30.755  40.361  -53.998 1.00 83.82  ? 168 LEU B CG  1 
ATOM   5602  C CD1 . LEU B 1 168 ? 30.327  39.903  -55.379 1.00 83.96  ? 168 LEU B CD1 1 
ATOM   5603  C CD2 . LEU B 1 168 ? 31.009  41.844  -54.009 1.00 84.29  ? 168 LEU B CD2 1 
ATOM   5604  N N   . SER B 1 169 ? 31.818  38.381  -51.411 1.00 86.30  ? 169 SER B N   1 
ATOM   5605  C CA  . SER B 1 169 ? 33.140  37.793  -51.213 1.00 84.95  ? 169 SER B CA  1 
ATOM   5606  C C   . SER B 1 169 ? 33.786  37.489  -52.562 1.00 85.05  ? 169 SER B C   1 
ATOM   5607  O O   . SER B 1 169 ? 33.921  36.330  -52.937 1.00 85.32  ? 169 SER B O   1 
ATOM   5608  C CB  . SER B 1 169 ? 33.073  36.520  -50.404 1.00 84.32  ? 169 SER B CB  1 
ATOM   5609  O OG  . SER B 1 169 ? 32.379  36.675  -49.177 1.00 86.33  ? 169 SER B OG  1 
ATOM   5610  N N   . ALA B 1 170 ? 34.188  38.526  -53.298 1.00 85.81  ? 170 ALA B N   1 
ATOM   5611  C CA  . ALA B 1 170 ? 34.722  38.333  -54.637 1.00 84.99  ? 170 ALA B CA  1 
ATOM   5612  C C   . ALA B 1 170 ? 36.213  38.099  -54.543 1.00 83.77  ? 170 ALA B C   1 
ATOM   5613  O O   . ALA B 1 170 ? 36.918  38.881  -53.916 1.00 84.33  ? 170 ALA B O   1 
ATOM   5614  C CB  . ALA B 1 170 ? 34.461  39.543  -55.489 1.00 86.80  ? 170 ALA B CB  1 
ATOM   5615  N N   . ASN B 1 171 ? 36.696  37.050  -55.205 1.00 82.52  ? 171 ASN B N   1 
ATOM   5616  C CA  . ASN B 1 171 ? 38.109  36.726  -55.110 1.00 78.70  ? 171 ASN B CA  1 
ATOM   5617  C C   . ASN B 1 171 ? 38.898  37.665  -56.008 1.00 77.19  ? 171 ASN B C   1 
ATOM   5618  O O   . ASN B 1 171 ? 38.712  37.661  -57.222 1.00 76.54  ? 171 ASN B O   1 
ATOM   5619  C CB  . ASN B 1 171 ? 38.359  35.268  -55.456 1.00 78.28  ? 171 ASN B CB  1 
ATOM   5620  C CG  . ASN B 1 171 ? 39.786  34.849  -55.206 1.00 76.64  ? 171 ASN B CG  1 
ATOM   5621  O OD1 . ASN B 1 171 ? 40.704  35.289  -55.915 1.00 76.52  ? 171 ASN B OD1 1 
ATOM   5622  N ND2 . ASN B 1 171 ? 39.978  33.987  -54.218 1.00 75.51  ? 171 ASN B ND2 1 
ATOM   5623  N N   . ALA B 1 172 ? 39.817  38.399  -55.368 1.00 76.65  ? 172 ALA B N   1 
ATOM   5624  C CA  . ALA B 1 172 ? 40.636  39.443  -55.974 1.00 76.03  ? 172 ALA B CA  1 
ATOM   5625  C C   . ALA B 1 172 ? 41.488  38.945  -57.140 1.00 75.23  ? 172 ALA B C   1 
ATOM   5626  O O   . ALA B 1 172 ? 41.782  39.743  -58.024 1.00 76.52  ? 172 ALA B O   1 
ATOM   5627  C CB  . ALA B 1 172 ? 41.527  40.071  -54.923 1.00 75.44  ? 172 ALA B CB  1 
ATOM   5628  N N   . MET B 1 173 ? 41.902  37.666  -57.135 1.00 73.32  ? 173 MET B N   1 
ATOM   5629  C CA  . MET B 1 173 ? 42.754  37.157  -58.199 1.00 72.29  ? 173 MET B CA  1 
ATOM   5630  C C   . MET B 1 173 ? 41.970  36.875  -59.485 1.00 72.93  ? 173 MET B C   1 
ATOM   5631  O O   . MET B 1 173 ? 42.553  36.940  -60.568 1.00 72.27  ? 173 MET B O   1 
ATOM   5632  C CB  . MET B 1 173 ? 43.482  35.888  -57.749 1.00 71.43  ? 173 MET B CB  1 
ATOM   5633  C CG  . MET B 1 173 ? 44.515  36.120  -56.658 1.00 70.67  ? 173 MET B CG  1 
ATOM   5634  S SD  . MET B 1 173 ? 45.955  37.050  -57.228 1.00 70.35  ? 173 MET B SD  1 
ATOM   5635  C CE  . MET B 1 173 ? 46.503  36.016  -58.598 1.00 69.78  ? 173 MET B CE  1 
ATOM   5636  N N   . ILE B 1 174 ? 40.671  36.547  -59.369 1.00 73.97  ? 174 ILE B N   1 
ATOM   5637  C CA  . ILE B 1 174 ? 39.851  36.182  -60.522 1.00 75.51  ? 174 ILE B CA  1 
ATOM   5638  C C   . ILE B 1 174 ? 38.742  37.204  -60.763 1.00 77.11  ? 174 ILE B C   1 
ATOM   5639  O O   . ILE B 1 174 ? 38.236  37.302  -61.877 1.00 77.71  ? 174 ILE B O   1 
ATOM   5640  C CB  . ILE B 1 174 ? 39.225  34.782  -60.367 1.00 76.09  ? 174 ILE B CB  1 
ATOM   5641  C CG1 . ILE B 1 174 ? 38.626  34.592  -58.977 1.00 76.56  ? 174 ILE B CG1 1 
ATOM   5642  C CG2 . ILE B 1 174 ? 40.222  33.676  -60.703 1.00 75.17  ? 174 ILE B CG2 1 
ATOM   5643  C CD1 . ILE B 1 174 ? 37.336  33.791  -58.958 1.00 77.08  ? 174 ILE B CD1 1 
ATOM   5644  N N   . SER B 1 175 ? 38.315  37.911  -59.713 1.00 77.90  ? 175 SER B N   1 
ATOM   5645  C CA  . SER B 1 175 ? 37.238  38.873  -59.853 1.00 79.90  ? 175 SER B CA  1 
ATOM   5646  C C   . SER B 1 175 ? 37.777  40.321  -59.799 1.00 81.51  ? 175 SER B C   1 
ATOM   5647  O O   . SER B 1 175 ? 37.064  41.257  -59.399 1.00 84.03  ? 175 SER B O   1 
ATOM   5648  C CB  . SER B 1 175 ? 36.140  38.554  -58.834 1.00 80.56  ? 175 SER B CB  1 
ATOM   5649  O OG  . SER B 1 175 ? 35.561  37.261  -59.048 1.00 80.55  ? 175 SER B OG  1 
ATOM   5650  N N   . ASP B 1 176 ? 39.016  40.536  -60.299 1.00 80.31  ? 176 ASP B N   1 
ATOM   5651  C CA  . ASP B 1 176 ? 39.628  41.861  -60.350 1.00 80.50  ? 176 ASP B CA  1 
ATOM   5652  C C   . ASP B 1 176 ? 38.878  42.796  -61.300 1.00 81.64  ? 176 ASP B C   1 
ATOM   5653  O O   . ASP B 1 176 ? 38.680  43.966  -60.978 1.00 84.10  ? 176 ASP B O   1 
ATOM   5654  C CB  . ASP B 1 176 ? 41.097  41.806  -60.727 1.00 80.66  ? 176 ASP B CB  1 
ATOM   5655  C CG  . ASP B 1 176 ? 41.451  40.974  -61.953 1.00 80.76  ? 176 ASP B CG  1 
ATOM   5656  O OD1 . ASP B 1 176 ? 40.519  40.493  -62.628 1.00 81.13  ? 176 ASP B OD1 1 
ATOM   5657  O OD2 . ASP B 1 176 ? 42.663  40.783  -62.199 1.00 79.95  ? 176 ASP B OD2 1 
ATOM   5658  N N   . TYR B 1 177 ? 38.444  42.268  -62.450 1.00 80.34  ? 177 TYR B N   1 
ATOM   5659  C CA  . TYR B 1 177 ? 37.704  43.037  -63.433 1.00 81.14  ? 177 TYR B CA  1 
ATOM   5660  C C   . TYR B 1 177 ? 36.403  43.586  -62.842 1.00 82.16  ? 177 TYR B C   1 
ATOM   5661  O O   . TYR B 1 177 ? 35.902  44.603  -63.319 1.00 83.47  ? 177 TYR B O   1 
ATOM   5662  C CB  . TYR B 1 177 ? 37.409  42.169  -64.658 1.00 80.71  ? 177 TYR B CB  1 
ATOM   5663  C CG  . TYR B 1 177 ? 36.395  41.074  -64.370 1.00 80.64  ? 177 TYR B CG  1 
ATOM   5664  C CD1 . TYR B 1 177 ? 35.017  41.295  -64.476 1.00 81.54  ? 177 TYR B CD1 1 
ATOM   5665  C CD2 . TYR B 1 177 ? 36.821  39.803  -63.986 1.00 79.11  ? 177 TYR B CD2 1 
ATOM   5666  C CE1 . TYR B 1 177 ? 34.104  40.282  -64.207 1.00 81.08  ? 177 TYR B CE1 1 
ATOM   5667  C CE2 . TYR B 1 177 ? 35.921  38.789  -63.711 1.00 79.00  ? 177 TYR B CE2 1 
ATOM   5668  C CZ  . TYR B 1 177 ? 34.558  39.032  -63.808 1.00 80.24  ? 177 TYR B CZ  1 
ATOM   5669  O OH  . TYR B 1 177 ? 33.725  37.986  -63.529 1.00 80.15  ? 177 TYR B OH  1 
ATOM   5670  N N   . MET B 1 178 ? 35.857  42.918  -61.815 1.00 81.36  ? 178 MET B N   1 
ATOM   5671  C CA  . MET B 1 178 ? 34.442  43.051  -61.473 1.00 82.45  ? 178 MET B CA  1 
ATOM   5672  C C   . MET B 1 178 ? 34.136  44.425  -60.884 1.00 83.45  ? 178 MET B C   1 
ATOM   5673  O O   . MET B 1 178 ? 34.966  44.986  -60.180 1.00 83.15  ? 178 MET B O   1 
ATOM   5674  C CB  . MET B 1 178 ? 34.026  41.983  -60.452 1.00 81.51  ? 178 MET B CB  1 
ATOM   5675  C CG  . MET B 1 178 ? 32.622  42.131  -59.906 1.00 82.42  ? 178 MET B CG  1 
ATOM   5676  S SD  . MET B 1 178 ? 32.114  40.740  -58.871 1.00 81.84  ? 178 MET B SD  1 
ATOM   5677  C CE  . MET B 1 178 ? 31.820  39.443  -60.080 1.00 81.77  ? 178 MET B CE  1 
ATOM   5678  N N   . ASP B 1 179 ? 32.924  44.924  -61.167 1.00 85.13  ? 179 ASP B N   1 
ATOM   5679  C CA  . ASP B 1 179 ? 32.426  46.191  -60.653 1.00 86.19  ? 179 ASP B CA  1 
ATOM   5680  C C   . ASP B 1 179 ? 31.755  45.948  -59.307 1.00 85.42  ? 179 ASP B C   1 
ATOM   5681  O O   . ASP B 1 179 ? 30.942  45.037  -59.204 1.00 84.70  ? 179 ASP B O   1 
ATOM   5682  C CB  . ASP B 1 179 ? 31.395  46.792  -61.590 1.00 88.47  ? 179 ASP B CB  1 
ATOM   5683  C CG  . ASP B 1 179 ? 30.904  48.184  -61.212 1.00 91.20  ? 179 ASP B CG  1 
ATOM   5684  O OD1 . ASP B 1 179 ? 31.760  49.116  -61.195 1.00 91.99  ? 179 ASP B OD1 1 
ATOM   5685  O OD2 . ASP B 1 179 ? 29.669  48.327  -60.951 1.00 92.28  ? 179 ASP B OD2 1 
ATOM   5686  N N   . GLU B 1 180 ? 32.087  46.777  -58.303 1.00 85.54  ? 180 GLU B N   1 
ATOM   5687  C CA  . GLU B 1 180 ? 31.549  46.639  -56.954 1.00 85.44  ? 180 GLU B CA  1 
ATOM   5688  C C   . GLU B 1 180 ? 30.907  47.951  -56.504 1.00 88.33  ? 180 GLU B C   1 
ATOM   5689  O O   . GLU B 1 180 ? 30.698  48.173  -55.309 1.00 88.76  ? 180 GLU B O   1 
ATOM   5690  C CB  . GLU B 1 180 ? 32.600  46.266  -55.905 1.00 83.35  ? 180 GLU B CB  1 
ATOM   5691  C CG  . GLU B 1 180 ? 33.155  44.851  -56.033 1.00 80.75  ? 180 GLU B CG  1 
ATOM   5692  C CD  . GLU B 1 180 ? 33.944  44.370  -54.822 1.00 79.27  ? 180 GLU B CD  1 
ATOM   5693  O OE1 . GLU B 1 180 ? 33.883  45.022  -53.750 1.00 79.29  ? 180 GLU B OE1 1 
ATOM   5694  O OE2 . GLU B 1 180 ? 34.633  43.315  -54.963 1.00 77.79  ? 180 GLU B OE2 1 
ATOM   5695  N N   . SER B 1 181 ? 30.565  48.817  -57.466 1.00 90.71  ? 181 SER B N   1 
ATOM   5696  C CA  . SER B 1 181 ? 30.005  50.116  -57.137 1.00 93.55  ? 181 SER B CA  1 
ATOM   5697  C C   . SER B 1 181 ? 28.532  49.967  -56.751 1.00 95.02  ? 181 SER B C   1 
ATOM   5698  O O   . SER B 1 181 ? 27.954  50.880  -56.170 1.00 97.05  ? 181 SER B O   1 
ATOM   5699  C CB  . SER B 1 181 ? 30.198  51.104  -58.270 1.00 95.36  ? 181 SER B CB  1 
ATOM   5700  O OG  . SER B 1 181 ? 29.391  50.766  -59.391 1.00 96.20  ? 181 SER B OG  1 
ATOM   5701  N N   . ILE B 1 182 ? 27.929  48.810  -57.060 1.00 94.25  ? 182 ILE B N   1 
ATOM   5702  C CA  . ILE B 1 182 ? 26.547  48.539  -56.679 1.00 95.81  ? 182 ILE B CA  1 
ATOM   5703  C C   . ILE B 1 182 ? 26.453  48.064  -55.226 1.00 94.67  ? 182 ILE B C   1 
ATOM   5704  O O   . ILE B 1 182 ? 25.341  47.929  -54.727 1.00 97.03  ? 182 ILE B O   1 
ATOM   5705  C CB  . ILE B 1 182 ? 25.896  47.502  -57.614 1.00 96.01  ? 182 ILE B CB  1 
ATOM   5706  C CG1 . ILE B 1 182 ? 26.630  46.139  -57.496 1.00 93.91  ? 182 ILE B CG1 1 
ATOM   5707  C CG2 . ILE B 1 182 ? 25.820  48.029  -59.051 1.00 97.04  ? 182 ILE B CG2 1 
ATOM   5708  C CD1 . ILE B 1 182 ? 25.980  44.974  -58.225 1.00 93.68  ? 182 ILE B CD1 1 
ATOM   5709  N N   . PHE B 1 183 ? 27.584  47.772  -54.567 1.00 91.49  ? 183 PHE B N   1 
ATOM   5710  C CA  . PHE B 1 183 ? 27.589  47.373  -53.166 1.00 90.41  ? 183 PHE B CA  1 
ATOM   5711  C C   . PHE B 1 183 ? 27.984  48.570  -52.306 1.00 90.77  ? 183 PHE B C   1 
ATOM   5712  O O   . PHE B 1 183 ? 28.533  49.541  -52.808 1.00 91.63  ? 183 PHE B O   1 
ATOM   5713  C CB  . PHE B 1 183 ? 28.559  46.209  -52.914 1.00 88.57  ? 183 PHE B CB  1 
ATOM   5714  C CG  . PHE B 1 183 ? 28.307  44.967  -53.764 1.00 87.53  ? 183 PHE B CG  1 
ATOM   5715  C CD1 . PHE B 1 183 ? 27.322  44.043  -53.411 1.00 87.98  ? 183 PHE B CD1 1 
ATOM   5716  C CD2 . PHE B 1 183 ? 29.022  44.760  -54.936 1.00 86.15  ? 183 PHE B CD2 1 
ATOM   5717  C CE1 . PHE B 1 183 ? 27.066  42.945  -54.210 1.00 87.23  ? 183 PHE B CE1 1 
ATOM   5718  C CE2 . PHE B 1 183 ? 28.759  43.664  -55.733 1.00 85.63  ? 183 PHE B CE2 1 
ATOM   5719  C CZ  . PHE B 1 183 ? 27.794  42.754  -55.364 1.00 86.19  ? 183 PHE B CZ  1 
ATOM   5720  N N   . ASP B 1 184 ? 27.740  48.468  -50.998 1.00 90.55  ? 184 ASP B N   1 
ATOM   5721  C CA  . ASP B 1 184 ? 27.951  49.570  -50.073 1.00 91.82  ? 184 ASP B CA  1 
ATOM   5722  C C   . ASP B 1 184 ? 29.381  49.604  -49.545 1.00 90.16  ? 184 ASP B C   1 
ATOM   5723  O O   . ASP B 1 184 ? 29.773  50.596  -48.941 1.00 91.48  ? 184 ASP B O   1 
ATOM   5724  C CB  . ASP B 1 184 ? 27.012  49.466  -48.888 1.00 93.33  ? 184 ASP B CB  1 
ATOM   5725  C CG  . ASP B 1 184 ? 25.536  49.347  -49.250 1.00 95.31  ? 184 ASP B CG  1 
ATOM   5726  O OD1 . ASP B 1 184 ? 25.021  50.226  -50.015 1.00 96.77  ? 184 ASP B OD1 1 
ATOM   5727  O OD2 . ASP B 1 184 ? 24.909  48.380  -48.751 1.00 95.33  ? 184 ASP B OD2 1 
ATOM   5728  N N   . VAL B 1 185 ? 30.109  48.492  -49.717 1.00 87.56  ? 185 VAL B N   1 
ATOM   5729  C CA  . VAL B 1 185 ? 31.439  48.282  -49.164 1.00 85.78  ? 185 VAL B CA  1 
ATOM   5730  C C   . VAL B 1 185 ? 32.207  47.461  -50.193 1.00 83.77  ? 185 VAL B C   1 
ATOM   5731  O O   . VAL B 1 185 ? 31.681  46.484  -50.708 1.00 83.07  ? 185 VAL B O   1 
ATOM   5732  C CB  . VAL B 1 185 ? 31.441  47.562  -47.798 1.00 85.05  ? 185 VAL B CB  1 
ATOM   5733  C CG1 . VAL B 1 185 ? 32.830  47.110  -47.394 1.00 83.48  ? 185 VAL B CG1 1 
ATOM   5734  C CG2 . VAL B 1 185 ? 30.881  48.407  -46.669 1.00 87.17  ? 185 VAL B CG2 1 
ATOM   5735  N N   . TYR B 1 186 ? 33.444  47.859  -50.498 1.00 83.27  ? 186 TYR B N   1 
ATOM   5736  C CA  . TYR B 1 186 ? 34.304  47.047  -51.340 1.00 81.59  ? 186 TYR B CA  1 
ATOM   5737  C C   . TYR B 1 186 ? 34.855  45.899  -50.509 1.00 79.91  ? 186 TYR B C   1 
ATOM   5738  O O   . TYR B 1 186 ? 35.190  46.078  -49.339 1.00 79.59  ? 186 TYR B O   1 
ATOM   5739  C CB  . TYR B 1 186 ? 35.428  47.886  -51.951 1.00 81.95  ? 186 TYR B CB  1 
ATOM   5740  C CG  . TYR B 1 186 ? 34.897  49.013  -52.829 1.00 83.70  ? 186 TYR B CG  1 
ATOM   5741  C CD1 . TYR B 1 186 ? 34.205  48.738  -54.003 1.00 83.64  ? 186 TYR B CD1 1 
ATOM   5742  C CD2 . TYR B 1 186 ? 35.116  50.341  -52.497 1.00 85.62  ? 186 TYR B CD2 1 
ATOM   5743  C CE1 . TYR B 1 186 ? 33.738  49.756  -54.818 1.00 85.89  ? 186 TYR B CE1 1 
ATOM   5744  C CE2 . TYR B 1 186 ? 34.616  51.372  -53.285 1.00 88.05  ? 186 TYR B CE2 1 
ATOM   5745  C CZ  . TYR B 1 186 ? 33.918  51.087  -54.449 1.00 87.80  ? 186 TYR B CZ  1 
ATOM   5746  O OH  . TYR B 1 186 ? 33.465  52.120  -55.222 1.00 88.58  ? 186 TYR B OH  1 
ATOM   5747  N N   . ALA B 1 187 ? 34.919  44.717  -51.124 1.00 78.91  ? 187 ALA B N   1 
ATOM   5748  C CA  . ALA B 1 187 ? 35.409  43.552  -50.415 1.00 78.10  ? 187 ALA B CA  1 
ATOM   5749  C C   . ALA B 1 187 ? 35.969  42.511  -51.385 1.00 77.17  ? 187 ALA B C   1 
ATOM   5750  O O   . ALA B 1 187 ? 35.564  42.439  -52.545 1.00 77.56  ? 187 ALA B O   1 
ATOM   5751  C CB  . ALA B 1 187 ? 34.298  42.996  -49.560 1.00 78.94  ? 187 ALA B CB  1 
ATOM   5752  N N   . TYR B 1 188 ? 36.897  41.694  -50.871 1.00 76.50  ? 188 TYR B N   1 
ATOM   5753  C CA  . TYR B 1 188 ? 37.734  40.814  -51.678 1.00 75.45  ? 188 TYR B CA  1 
ATOM   5754  C C   . TYR B 1 188 ? 38.427  39.773  -50.790 1.00 75.14  ? 188 TYR B C   1 
ATOM   5755  O O   . TYR B 1 188 ? 38.979  40.104  -49.737 1.00 74.89  ? 188 TYR B O   1 
ATOM   5756  C CB  . TYR B 1 188 ? 38.857  41.530  -52.442 1.00 74.57  ? 188 TYR B CB  1 
ATOM   5757  C CG  . TYR B 1 188 ? 38.460  42.361  -53.655 1.00 74.92  ? 188 TYR B CG  1 
ATOM   5758  C CD1 . TYR B 1 188 ? 38.097  41.757  -54.850 1.00 74.51  ? 188 TYR B CD1 1 
ATOM   5759  C CD2 . TYR B 1 188 ? 38.499  43.748  -53.627 1.00 75.96  ? 188 TYR B CD2 1 
ATOM   5760  C CE1 . TYR B 1 188 ? 37.739  42.505  -55.963 1.00 75.50  ? 188 TYR B CE1 1 
ATOM   5761  C CE2 . TYR B 1 188 ? 38.135  44.507  -54.731 1.00 77.04  ? 188 TYR B CE2 1 
ATOM   5762  C CZ  . TYR B 1 188 ? 37.756  43.887  -55.911 1.00 76.56  ? 188 TYR B CZ  1 
ATOM   5763  O OH  . TYR B 1 188 ? 37.410  44.589  -57.036 1.00 77.25  ? 188 TYR B OH  1 
ATOM   5764  N N   . ASN B 1 189 ? 38.399  38.512  -51.249 1.00 75.05  ? 189 ASN B N   1 
ATOM   5765  C CA  . ASN B 1 189 ? 39.226  37.455  -50.703 1.00 74.26  ? 189 ASN B CA  1 
ATOM   5766  C C   . ASN B 1 189 ? 40.606  37.579  -51.332 1.00 73.96  ? 189 ASN B C   1 
ATOM   5767  O O   . ASN B 1 189 ? 40.715  37.488  -52.553 1.00 75.17  ? 189 ASN B O   1 
ATOM   5768  C CB  . ASN B 1 189 ? 38.623  36.095  -51.018 1.00 75.19  ? 189 ASN B CB  1 
ATOM   5769  C CG  . ASN B 1 189 ? 37.268  35.877  -50.375 1.00 77.51  ? 189 ASN B CG  1 
ATOM   5770  O OD1 . ASN B 1 189 ? 36.898  36.587  -49.430 1.00 79.58  ? 189 ASN B OD1 1 
ATOM   5771  N ND2 . ASN B 1 189 ? 36.518  34.888  -50.854 1.00 77.64  ? 189 ASN B ND2 1 
ATOM   5772  N N   . CYS B 1 190 ? 41.644  37.768  -50.497 1.00 73.41  ? 190 CYS B N   1 
ATOM   5773  C CA  . CYS B 1 190 ? 42.998  38.078  -50.953 1.00 72.52  ? 190 CYS B CA  1 
ATOM   5774  C C   . CYS B 1 190 ? 43.987  36.983  -50.521 1.00 72.13  ? 190 CYS B C   1 
ATOM   5775  O O   . CYS B 1 190 ? 44.319  36.859  -49.342 1.00 71.73  ? 190 CYS B O   1 
ATOM   5776  C CB  . CYS B 1 190 ? 43.411  39.451  -50.432 1.00 72.36  ? 190 CYS B CB  1 
ATOM   5777  S SG  . CYS B 1 190 ? 42.127  40.720  -50.649 1.00 72.66  ? 190 CYS B SG  1 
ATOM   5778  N N   . TYR B 1 191 ? 44.475  36.185  -51.475 1.00 71.34  ? 191 TYR B N   1 
ATOM   5779  C CA  . TYR B 1 191 ? 45.543  35.256  -51.165 1.00 71.84  ? 191 TYR B CA  1 
ATOM   5780  C C   . TYR B 1 191 ? 46.816  35.742  -51.848 1.00 72.61  ? 191 TYR B C   1 
ATOM   5781  O O   . TYR B 1 191 ? 46.755  36.204  -52.984 1.00 73.72  ? 191 TYR B O   1 
ATOM   5782  C CB  . TYR B 1 191 ? 45.155  33.821  -51.549 1.00 72.46  ? 191 TYR B CB  1 
ATOM   5783  C CG  . TYR B 1 191 ? 43.978  33.322  -50.729 1.00 74.06  ? 191 TYR B CG  1 
ATOM   5784  C CD1 . TYR B 1 191 ? 44.161  32.680  -49.507 1.00 73.88  ? 191 TYR B CD1 1 
ATOM   5785  C CD2 . TYR B 1 191 ? 42.678  33.612  -51.124 1.00 75.27  ? 191 TYR B CD2 1 
ATOM   5786  C CE1 . TYR B 1 191 ? 43.081  32.280  -48.732 1.00 75.16  ? 191 TYR B CE1 1 
ATOM   5787  C CE2 . TYR B 1 191 ? 41.594  33.235  -50.348 1.00 76.83  ? 191 TYR B CE2 1 
ATOM   5788  C CZ  . TYR B 1 191 ? 41.785  32.562  -49.149 1.00 77.17  ? 191 TYR B CZ  1 
ATOM   5789  O OH  . TYR B 1 191 ? 40.650  32.192  -48.447 1.00 79.25  ? 191 TYR B OH  1 
ATOM   5790  N N   . ASP B 1 192 ? 47.957  35.590  -51.153 1.00 72.34  ? 192 ASP B N   1 
ATOM   5791  C CA  . ASP B 1 192 ? 49.246  36.074  -51.616 1.00 72.25  ? 192 ASP B CA  1 
ATOM   5792  C C   . ASP B 1 192 ? 50.152  34.875  -51.850 1.00 71.43  ? 192 ASP B C   1 
ATOM   5793  O O   . ASP B 1 192 ? 50.826  34.407  -50.936 1.00 70.31  ? 192 ASP B O   1 
ATOM   5794  C CB  . ASP B 1 192 ? 49.854  37.026  -50.597 1.00 73.39  ? 192 ASP B CB  1 
ATOM   5795  C CG  . ASP B 1 192 ? 51.299  37.456  -50.831 1.00 73.83  ? 192 ASP B CG  1 
ATOM   5796  O OD1 . ASP B 1 192 ? 51.891  37.025  -51.847 1.00 74.21  ? 192 ASP B OD1 1 
ATOM   5797  O OD2 . ASP B 1 192 ? 51.827  38.211  -49.982 1.00 74.20  ? 192 ASP B OD2 1 
ATOM   5798  N N   . HIS B 1 193 ? 50.147  34.381  -53.087 1.00 71.72  ? 193 HIS B N   1 
ATOM   5799  C CA  . HIS B 1 193 ? 50.909  33.198  -53.456 1.00 70.58  ? 193 HIS B CA  1 
ATOM   5800  C C   . HIS B 1 193 ? 51.989  33.601  -54.444 1.00 70.97  ? 193 HIS B C   1 
ATOM   5801  O O   . HIS B 1 193 ? 52.414  32.796  -55.271 1.00 71.32  ? 193 HIS B O   1 
ATOM   5802  C CB  . HIS B 1 193 ? 50.013  32.176  -54.154 1.00 70.35  ? 193 HIS B CB  1 
ATOM   5803  C CG  . HIS B 1 193 ? 48.890  31.674  -53.333 1.00 70.35  ? 193 HIS B CG  1 
ATOM   5804  N ND1 . HIS B 1 193 ? 47.602  31.706  -53.822 1.00 70.59  ? 193 HIS B ND1 1 
ATOM   5805  C CD2 . HIS B 1 193 ? 48.826  31.136  -52.105 1.00 70.54  ? 193 HIS B CD2 1 
ATOM   5806  C CE1 . HIS B 1 193 ? 46.787  31.147  -52.928 1.00 71.33  ? 193 HIS B CE1 1 
ATOM   5807  N NE2 . HIS B 1 193 ? 47.502  30.809  -51.866 1.00 71.42  ? 193 HIS B NE2 1 
ATOM   5808  N N   . ASN B 1 194 ? 52.388  34.873  -54.360 1.00 71.48  ? 194 ASN B N   1 
ATOM   5809  C CA  . ASN B 1 194 ? 53.521  35.379  -55.109 1.00 71.09  ? 194 ASN B CA  1 
ATOM   5810  C C   . ASN B 1 194 ? 53.512  34.797  -56.516 1.00 70.99  ? 194 ASN B C   1 
ATOM   5811  O O   . ASN B 1 194 ? 54.503  34.201  -56.915 1.00 70.83  ? 194 ASN B O   1 
ATOM   5812  C CB  . ASN B 1 194 ? 54.836  35.064  -54.416 1.00 70.20  ? 194 ASN B CB  1 
ATOM   5813  C CG  . ASN B 1 194 ? 55.985  35.666  -55.185 1.00 71.07  ? 194 ASN B CG  1 
ATOM   5814  O OD1 . ASN B 1 194 ? 55.903  36.819  -55.606 1.00 73.25  ? 194 ASN B OD1 1 
ATOM   5815  N ND2 . ASN B 1 194 ? 57.046  34.916  -55.418 1.00 71.03  ? 194 ASN B ND2 1 
ATOM   5816  N N   . GLU B 1 195 ? 52.380  34.960  -57.227 1.00 71.12  ? 195 GLU B N   1 
ATOM   5817  C CA  . GLU B 1 195 ? 52.183  34.405  -58.564 1.00 70.93  ? 195 GLU B CA  1 
ATOM   5818  C C   . GLU B 1 195 ? 51.219  35.301  -59.342 1.00 70.99  ? 195 GLU B C   1 
ATOM   5819  O O   . GLU B 1 195 ? 50.482  36.082  -58.740 1.00 70.04  ? 195 GLU B O   1 
ATOM   5820  C CB  . GLU B 1 195 ? 51.661  32.973  -58.479 1.00 70.15  ? 195 GLU B CB  1 
ATOM   5821  C CG  . GLU B 1 195 ? 50.327  32.907  -57.754 1.00 70.20  ? 195 GLU B CG  1 
ATOM   5822  C CD  . GLU B 1 195 ? 49.632  31.561  -57.672 1.00 70.87  ? 195 GLU B CD  1 
ATOM   5823  O OE1 . GLU B 1 195 ? 50.184  30.521  -58.106 1.00 71.92  ? 195 GLU B OE1 1 
ATOM   5824  O OE2 . GLU B 1 195 ? 48.499  31.585  -57.149 1.00 71.13  ? 195 GLU B OE2 1 
ATOM   5825  N N   . GLY B 1 196 ? 51.255  35.200  -60.681 1.00 71.04  ? 196 GLY B N   1 
ATOM   5826  C CA  . GLY B 1 196 ? 50.506  36.100  -61.548 1.00 70.89  ? 196 GLY B CA  1 
ATOM   5827  C C   . GLY B 1 196 ? 50.566  37.537  -61.028 1.00 70.96  ? 196 GLY B C   1 
ATOM   5828  O O   . GLY B 1 196 ? 51.639  38.093  -60.806 1.00 69.83  ? 196 GLY B O   1 
ATOM   5829  N N   . GLN B 1 197 ? 49.392  38.112  -60.764 1.00 71.82  ? 197 GLN B N   1 
ATOM   5830  C CA  . GLN B 1 197 ? 49.286  39.511  -60.406 1.00 72.69  ? 197 GLN B CA  1 
ATOM   5831  C C   . GLN B 1 197 ? 50.029  39.856  -59.118 1.00 73.73  ? 197 GLN B C   1 
ATOM   5832  O O   . GLN B 1 197 ? 50.526  40.978  -59.008 1.00 75.42  ? 197 GLN B O   1 
ATOM   5833  C CB  . GLN B 1 197 ? 47.818  39.848  -60.284 1.00 72.90  ? 197 GLN B CB  1 
ATOM   5834  C CG  . GLN B 1 197 ? 47.083  39.638  -61.596 1.00 73.68  ? 197 GLN B CG  1 
ATOM   5835  C CD  . GLN B 1 197 ? 46.069  38.524  -61.506 1.00 73.00  ? 197 GLN B CD  1 
ATOM   5836  O OE1 . GLN B 1 197 ? 46.404  37.337  -61.598 1.00 72.01  ? 197 GLN B OE1 1 
ATOM   5837  N NE2 . GLN B 1 197 ? 44.814  38.909  -61.323 1.00 73.27  ? 197 GLN B NE2 1 
ATOM   5838  N N   . THR B 1 198 ? 50.128  38.913  -58.166 1.00 73.26  ? 198 THR B N   1 
ATOM   5839  C CA  . THR B 1 198 ? 50.797  39.175  -56.893 1.00 73.12  ? 198 THR B CA  1 
ATOM   5840  C C   . THR B 1 198 ? 52.288  38.898  -56.995 1.00 72.15  ? 198 THR B C   1 
ATOM   5841  O O   . THR B 1 198 ? 52.987  39.021  -55.992 1.00 71.45  ? 198 THR B O   1 
ATOM   5842  C CB  . THR B 1 198 ? 50.203  38.368  -55.734 1.00 73.09  ? 198 THR B CB  1 
ATOM   5843  O OG1 . THR B 1 198 ? 50.480  36.975  -55.946 1.00 73.02  ? 198 THR B OG1 1 
ATOM   5844  C CG2 . THR B 1 198 ? 48.737  38.718  -55.515 1.00 72.87  ? 198 THR B CG2 1 
ATOM   5845  N N   . ALA B 1 199 ? 52.738  38.471  -58.180 1.00 72.82  ? 199 ALA B N   1 
ATOM   5846  C CA  . ALA B 1 199 ? 54.161  38.283  -58.446 1.00 73.94  ? 199 ALA B CA  1 
ATOM   5847  C C   . ALA B 1 199 ? 54.713  39.485  -59.205 1.00 75.71  ? 199 ALA B C   1 
ATOM   5848  O O   . ALA B 1 199 ? 55.911  39.739  -59.156 1.00 75.81  ? 199 ALA B O   1 
ATOM   5849  C CB  . ALA B 1 199 ? 54.403  36.998  -59.228 1.00 73.61  ? 199 ALA B CB  1 
ATOM   5850  N N   . THR B 1 200 ? 53.817  40.189  -59.914 1.00 77.30  ? 200 THR B N   1 
ATOM   5851  C CA  . THR B 1 200 ? 54.151  41.373  -60.680 1.00 78.68  ? 200 THR B CA  1 
ATOM   5852  C C   . THR B 1 200 ? 54.168  42.589  -59.754 1.00 79.86  ? 200 THR B C   1 
ATOM   5853  O O   . THR B 1 200 ? 55.162  43.307  -59.720 1.00 82.82  ? 200 THR B O   1 
ATOM   5854  C CB  . THR B 1 200 ? 53.165  41.537  -61.845 1.00 80.08  ? 200 THR B CB  1 
ATOM   5855  O OG1 . THR B 1 200 ? 51.806  41.597  -61.393 1.00 78.45  ? 200 THR B OG1 1 
ATOM   5856  C CG2 . THR B 1 200 ? 53.341  40.430  -62.874 1.00 79.96  ? 200 THR B CG2 1 
ATOM   5857  N N   . MET B 1 201 ? 53.075  42.804  -59.009 1.00 79.09  ? 201 MET B N   1 
ATOM   5858  C CA  . MET B 1 201 ? 52.804  44.068  -58.331 1.00 79.14  ? 201 MET B CA  1 
ATOM   5859  C C   . MET B 1 201 ? 53.136  43.991  -56.835 1.00 78.11  ? 201 MET B C   1 
ATOM   5860  O O   . MET B 1 201 ? 53.292  45.005  -56.136 1.00 76.87  ? 201 MET B O   1 
ATOM   5861  C CB  . MET B 1 201 ? 51.325  44.412  -58.540 1.00 79.29  ? 201 MET B CB  1 
ATOM   5862  C CG  . MET B 1 201 ? 50.992  44.748  -59.983 1.00 80.14  ? 201 MET B CG  1 
ATOM   5863  S SD  . MET B 1 201 ? 49.224  44.793  -60.344 1.00 80.44  ? 201 MET B SD  1 
ATOM   5864  C CE  . MET B 1 201 ? 48.963  43.075  -60.796 1.00 79.77  ? 201 MET B CE  1 
ATOM   5865  N N   . GLY B 1 202 ? 53.275  42.755  -56.346 1.00 77.55  ? 202 GLY B N   1 
ATOM   5866  C CA  . GLY B 1 202 ? 53.288  42.508  -54.917 1.00 77.30  ? 202 GLY B CA  1 
ATOM   5867  C C   . GLY B 1 202 ? 51.887  42.683  -54.344 1.00 77.36  ? 202 GLY B C   1 
ATOM   5868  O O   . GLY B 1 202 ? 51.013  43.240  -55.011 1.00 78.72  ? 202 GLY B O   1 
ATOM   5869  N N   . PHE B 1 203 ? 51.697  42.207  -53.108 1.00 76.17  ? 203 PHE B N   1 
ATOM   5870  C CA  . PHE B 1 203 ? 50.368  41.950  -52.580 1.00 76.49  ? 203 PHE B CA  1 
ATOM   5871  C C   . PHE B 1 203 ? 49.694  43.295  -52.312 1.00 77.49  ? 203 PHE B C   1 
ATOM   5872  O O   . PHE B 1 203 ? 48.654  43.592  -52.907 1.00 78.05  ? 203 PHE B O   1 
ATOM   5873  C CB  . PHE B 1 203 ? 50.495  41.031  -51.357 1.00 76.16  ? 203 PHE B CB  1 
ATOM   5874  C CG  . PHE B 1 203 ? 49.201  40.421  -50.828 1.00 76.88  ? 203 PHE B CG  1 
ATOM   5875  C CD1 . PHE B 1 203 ? 48.241  39.891  -51.692 1.00 77.14  ? 203 PHE B CD1 1 
ATOM   5876  C CD2 . PHE B 1 203 ? 48.958  40.363  -49.458 1.00 77.31  ? 203 PHE B CD2 1 
ATOM   5877  C CE1 . PHE B 1 203 ? 47.074  39.321  -51.197 1.00 77.39  ? 203 PHE B CE1 1 
ATOM   5878  C CE2 . PHE B 1 203 ? 47.796  39.787  -48.968 1.00 77.86  ? 203 PHE B CE2 1 
ATOM   5879  C CZ  . PHE B 1 203 ? 46.851  39.272  -49.837 1.00 77.87  ? 203 PHE B CZ  1 
ATOM   5880  N N   . LYS B 1 204 ? 50.338  44.111  -51.457 1.00 77.36  ? 204 LYS B N   1 
ATOM   5881  C CA  . LYS B 1 204 ? 49.905  45.472  -51.153 1.00 77.96  ? 204 LYS B CA  1 
ATOM   5882  C C   . LYS B 1 204 ? 49.408  46.158  -52.423 1.00 77.91  ? 204 LYS B C   1 
ATOM   5883  O O   . LYS B 1 204 ? 48.209  46.436  -52.542 1.00 78.83  ? 204 LYS B O   1 
ATOM   5884  C CB  . LYS B 1 204 ? 51.029  46.295  -50.515 1.00 78.43  ? 204 LYS B CB  1 
ATOM   5885  C CG  . LYS B 1 204 ? 50.759  47.762  -50.332 1.00 80.85  ? 204 LYS B CG  1 
ATOM   5886  C CD  . LYS B 1 204 ? 52.007  48.614  -50.139 1.00 82.81  ? 204 LYS B CD  1 
ATOM   5887  C CE  . LYS B 1 204 ? 51.773  50.101  -50.230 1.00 85.78  ? 204 LYS B CE  1 
ATOM   5888  N NZ  . LYS B 1 204 ? 53.062  50.781  -50.428 1.00 87.34  ? 204 LYS B NZ  1 
ATOM   5889  N N   . ASP B 1 205 ? 50.330  46.364  -53.370 1.00 76.81  ? 205 ASP B N   1 
ATOM   5890  C CA  . ASP B 1 205 ? 50.092  47.214  -54.526 1.00 78.00  ? 205 ASP B CA  1 
ATOM   5891  C C   . ASP B 1 205 ? 48.986  46.659  -55.426 1.00 78.16  ? 205 ASP B C   1 
ATOM   5892  O O   . ASP B 1 205 ? 48.187  47.445  -55.946 1.00 79.57  ? 205 ASP B O   1 
ATOM   5893  C CB  . ASP B 1 205 ? 51.375  47.499  -55.294 1.00 77.85  ? 205 ASP B CB  1 
ATOM   5894  C CG  . ASP B 1 205 ? 52.358  48.452  -54.629 1.00 78.26  ? 205 ASP B CG  1 
ATOM   5895  O OD1 . ASP B 1 205 ? 52.095  48.877  -53.477 1.00 77.81  ? 205 ASP B OD1 1 
ATOM   5896  O OD2 . ASP B 1 205 ? 53.378  48.758  -55.277 1.00 78.61  ? 205 ASP B OD2 1 
ATOM   5897  N N   . TYR B 1 206 ? 48.931  45.328  -55.603 1.00 77.02  ? 206 TYR B N   1 
ATOM   5898  C CA  . TYR B 1 206 ? 47.877  44.706  -56.394 1.00 77.36  ? 206 TYR B CA  1 
ATOM   5899  C C   . TYR B 1 206 ? 46.516  45.093  -55.848 1.00 77.81  ? 206 TYR B C   1 
ATOM   5900  O O   . TYR B 1 206 ? 45.656  45.560  -56.593 1.00 78.00  ? 206 TYR B O   1 
ATOM   5901  C CB  . TYR B 1 206 ? 47.861  43.181  -56.342 1.00 77.20  ? 206 TYR B CB  1 
ATOM   5902  C CG  . TYR B 1 206 ? 46.760  42.482  -57.133 1.00 78.34  ? 206 TYR B CG  1 
ATOM   5903  C CD1 . TYR B 1 206 ? 46.384  42.909  -58.403 1.00 80.00  ? 206 TYR B CD1 1 
ATOM   5904  C CD2 . TYR B 1 206 ? 46.108  41.372  -56.602 1.00 78.17  ? 206 TYR B CD2 1 
ATOM   5905  C CE1 . TYR B 1 206 ? 45.407  42.238  -59.122 1.00 80.94  ? 206 TYR B CE1 1 
ATOM   5906  C CE2 . TYR B 1 206 ? 45.130  40.693  -57.307 1.00 78.82  ? 206 TYR B CE2 1 
ATOM   5907  C CZ  . TYR B 1 206 ? 44.781  41.128  -58.571 1.00 80.73  ? 206 TYR B CZ  1 
ATOM   5908  O OH  . TYR B 1 206 ? 43.808  40.450  -59.248 1.00 81.96  ? 206 TYR B OH  1 
ATOM   5909  N N   . ILE B 1 207 ? 46.360  44.868  -54.541 1.00 78.22  ? 207 ILE B N   1 
ATOM   5910  C CA  . ILE B 1 207 ? 45.094  45.053  -53.848 1.00 80.08  ? 207 ILE B CA  1 
ATOM   5911  C C   . ILE B 1 207 ? 44.820  46.555  -53.736 1.00 84.37  ? 207 ILE B C   1 
ATOM   5912  O O   . ILE B 1 207 ? 43.685  47.023  -53.898 1.00 87.93  ? 207 ILE B O   1 
ATOM   5913  C CB  . ILE B 1 207 ? 45.143  44.328  -52.481 1.00 78.37  ? 207 ILE B CB  1 
ATOM   5914  C CG1 . ILE B 1 207 ? 45.288  42.784  -52.614 1.00 75.77  ? 207 ILE B CG1 1 
ATOM   5915  C CG2 . ILE B 1 207 ? 43.962  44.692  -51.589 1.00 79.17  ? 207 ILE B CG2 1 
ATOM   5916  C CD1 . ILE B 1 207 ? 44.473  42.140  -53.719 1.00 75.25  ? 207 ILE B CD1 1 
ATOM   5917  N N   . LYS B 1 208 ? 45.883  47.324  -53.483 1.00 85.96  ? 208 LYS B N   1 
ATOM   5918  C CA  . LYS B 1 208 ? 45.787  48.773  -53.505 1.00 88.57  ? 208 LYS B CA  1 
ATOM   5919  C C   . LYS B 1 208 ? 45.245  49.223  -54.856 1.00 89.88  ? 208 LYS B C   1 
ATOM   5920  O O   . LYS B 1 208 ? 44.435  50.151  -54.928 1.00 92.63  ? 208 LYS B O   1 
ATOM   5921  C CB  . LYS B 1 208 ? 47.168  49.394  -53.279 1.00 89.98  ? 208 LYS B CB  1 
ATOM   5922  C CG  . LYS B 1 208 ? 47.140  50.885  -53.034 1.00 92.78  ? 208 LYS B CG  1 
ATOM   5923  C CD  . LYS B 1 208 ? 48.419  51.444  -52.441 1.00 93.60  ? 208 LYS B CD  1 
ATOM   5924  C CE  . LYS B 1 208 ? 48.125  52.670  -51.646 1.00 97.07  ? 208 LYS B CE  1 
ATOM   5925  N NZ  . LYS B 1 208 ? 49.341  53.469  -51.475 1.00 100.21 ? 208 LYS B NZ  1 
ATOM   5926  N N   . GLY B 1 209 ? 45.724  48.554  -55.914 1.00 88.85  ? 209 GLY B N   1 
ATOM   5927  C CA  . GLY B 1 209 ? 45.399  48.906  -57.286 1.00 89.82  ? 209 GLY B CA  1 
ATOM   5928  C C   . GLY B 1 209 ? 43.926  48.677  -57.621 1.00 89.76  ? 209 GLY B C   1 
ATOM   5929  O O   . GLY B 1 209 ? 43.402  49.338  -58.515 1.00 90.63  ? 209 GLY B O   1 
ATOM   5930  N N   . LEU B 1 210 ? 43.282  47.719  -56.933 1.00 88.40  ? 210 LEU B N   1 
ATOM   5931  C CA  . LEU B 1 210 ? 41.864  47.439  -57.124 1.00 88.57  ? 210 LEU B CA  1 
ATOM   5932  C C   . LEU B 1 210 ? 41.016  48.481  -56.397 1.00 90.90  ? 210 LEU B C   1 
ATOM   5933  O O   . LEU B 1 210 ? 39.903  48.781  -56.822 1.00 91.52  ? 210 LEU B O   1 
ATOM   5934  C CB  . LEU B 1 210 ? 41.531  46.030  -56.649 1.00 86.17  ? 210 LEU B CB  1 
ATOM   5935  C CG  . LEU B 1 210 ? 42.244  44.901  -57.398 1.00 84.74  ? 210 LEU B CG  1 
ATOM   5936  C CD1 . LEU B 1 210 ? 41.883  43.542  -56.801 1.00 83.95  ? 210 LEU B CD1 1 
ATOM   5937  C CD2 . LEU B 1 210 ? 41.937  44.926  -58.889 1.00 84.95  ? 210 LEU B CD2 1 
ATOM   5938  N N   . ASN B 1 211 ? 41.571  49.044  -55.316 1.00 90.94  ? 211 ASN B N   1 
ATOM   5939  C CA  . ASN B 1 211 ? 40.877  50.002  -54.469 1.00 90.64  ? 211 ASN B CA  1 
ATOM   5940  C C   . ASN B 1 211 ? 40.863  51.376  -55.128 1.00 94.13  ? 211 ASN B C   1 
ATOM   5941  O O   . ASN B 1 211 ? 39.945  52.169  -54.903 1.00 95.85  ? 211 ASN B O   1 
ATOM   5942  C CB  . ASN B 1 211 ? 41.569  50.105  -53.116 1.00 88.80  ? 211 ASN B CB  1 
ATOM   5943  C CG  . ASN B 1 211 ? 40.622  50.379  -51.980 1.00 87.78  ? 211 ASN B CG  1 
ATOM   5944  O OD1 . ASN B 1 211 ? 40.990  51.107  -51.054 1.00 87.54  ? 211 ASN B OD1 1 
ATOM   5945  N ND2 . ASN B 1 211 ? 39.467  49.730  -51.983 1.00 86.74  ? 211 ASN B ND2 1 
ATOM   5946  N N   . GLU B 1 212 ? 41.922  51.658  -55.904 1.00 94.86  ? 212 GLU B N   1 
ATOM   5947  C CA  . GLU B 1 212 ? 42.022  52.899  -56.666 1.00 96.66  ? 212 GLU B CA  1 
ATOM   5948  C C   . GLU B 1 212 ? 41.139  52.810  -57.912 1.00 95.97  ? 212 GLU B C   1 
ATOM   5949  O O   . GLU B 1 212 ? 40.454  53.778  -58.259 1.00 96.92  ? 212 GLU B O   1 
ATOM   5950  C CB  . GLU B 1 212 ? 43.483  53.211  -57.003 1.00 96.94  ? 212 GLU B CB  1 
ATOM   5951  C CG  . GLU B 1 212 ? 44.259  53.749  -55.803 1.00 97.84  ? 212 GLU B CG  1 
ATOM   5952  C CD  . GLU B 1 212 ? 45.746  53.459  -55.815 1.00 96.30  ? 212 GLU B CD  1 
ATOM   5953  O OE1 . GLU B 1 212 ? 46.204  52.829  -56.783 1.00 94.45  ? 212 GLU B OE1 1 
ATOM   5954  O OE2 . GLU B 1 212 ? 46.441  53.858  -54.855 1.00 96.71  ? 212 GLU B OE2 1 
ATOM   5955  N N   . LEU B 1 213 ? 41.168  51.639  -58.575 1.00 92.88  ? 213 LEU B N   1 
ATOM   5956  C CA  . LEU B 1 213 ? 40.297  51.387  -59.711 1.00 91.92  ? 213 LEU B CA  1 
ATOM   5957  C C   . LEU B 1 213 ? 38.852  51.554  -59.248 1.00 92.33  ? 213 LEU B C   1 
ATOM   5958  O O   . LEU B 1 213 ? 38.099  52.260  -59.913 1.00 95.81  ? 213 LEU B O   1 
ATOM   5959  C CB  . LEU B 1 213 ? 40.522  50.035  -60.392 1.00 89.24  ? 213 LEU B CB  1 
ATOM   5960  C CG  . LEU B 1 213 ? 41.766  49.877  -61.278 1.00 88.20  ? 213 LEU B CG  1 
ATOM   5961  C CD1 . LEU B 1 213 ? 41.523  48.742  -62.248 1.00 87.06  ? 213 LEU B CD1 1 
ATOM   5962  C CD2 . LEU B 1 213 ? 42.212  51.107  -62.056 1.00 89.90  ? 213 LEU B CD2 1 
ATOM   5963  N N   . ASN B 1 214 ? 38.513  50.980  -58.080 1.00 90.34  ? 214 ASN B N   1 
ATOM   5964  C CA  . ASN B 1 214 ? 37.158  50.997  -57.535 1.00 90.91  ? 214 ASN B CA  1 
ATOM   5965  C C   . ASN B 1 214 ? 36.653  52.423  -57.300 1.00 93.90  ? 214 ASN B C   1 
ATOM   5966  O O   . ASN B 1 214 ? 35.473  52.696  -57.517 1.00 93.06  ? 214 ASN B O   1 
ATOM   5967  C CB  . ASN B 1 214 ? 37.055  50.134  -56.279 1.00 89.00  ? 214 ASN B CB  1 
ATOM   5968  C CG  . ASN B 1 214 ? 37.065  48.664  -56.631 1.00 86.93  ? 214 ASN B CG  1 
ATOM   5969  O OD1 . ASN B 1 214 ? 36.813  48.328  -57.794 1.00 86.56  ? 214 ASN B OD1 1 
ATOM   5970  N ND2 . ASN B 1 214 ? 37.366  47.788  -55.675 1.00 85.02  ? 214 ASN B ND2 1 
ATOM   5971  N N   . GLY B 1 215 ? 37.562  53.300  -56.842 1.00 96.54  ? 215 GLY B N   1 
ATOM   5972  C CA  . GLY B 1 215 ? 37.325  54.730  -56.738 1.00 99.52  ? 215 GLY B CA  1 
ATOM   5973  C C   . GLY B 1 215 ? 37.659  55.317  -55.360 1.00 101.51 ? 215 GLY B C   1 
ATOM   5974  O O   . GLY B 1 215 ? 37.450  56.510  -55.163 1.00 106.80 ? 215 GLY B O   1 
ATOM   5975  N N   . LEU B 1 216 ? 38.143  54.509  -54.399 1.00 99.98  ? 216 LEU B N   1 
ATOM   5976  C CA  . LEU B 1 216 ? 38.545  54.991  -53.076 1.00 100.55 ? 216 LEU B CA  1 
ATOM   5977  C C   . LEU B 1 216 ? 37.406  55.731  -52.355 1.00 100.80 ? 216 LEU B C   1 
ATOM   5978  O O   . LEU B 1 216 ? 37.666  56.620  -51.543 1.00 100.89 ? 216 LEU B O   1 
ATOM   5979  C CB  . LEU B 1 216 ? 39.754  55.927  -53.139 1.00 103.46 ? 216 LEU B CB  1 
ATOM   5980  C CG  . LEU B 1 216 ? 40.922  55.576  -54.068 1.00 104.83 ? 216 LEU B CG  1 
ATOM   5981  C CD1 . LEU B 1 216 ? 40.675  55.986  -55.522 1.00 106.48 ? 216 LEU B CD1 1 
ATOM   5982  C CD2 . LEU B 1 216 ? 42.198  56.253  -53.562 1.00 106.54 ? 216 LEU B CD2 1 
ATOM   5983  N N   . ASP B 1 217 ? 36.148  55.351  -52.610 1.00 99.33  ? 217 ASP B N   1 
ATOM   5984  C CA  . ASP B 1 217 ? 35.010  56.130  -52.170 1.00 100.34 ? 217 ASP B CA  1 
ATOM   5985  C C   . ASP B 1 217 ? 34.159  55.326  -51.188 1.00 99.92  ? 217 ASP B C   1 
ATOM   5986  O O   . ASP B 1 217 ? 33.059  55.721  -50.859 1.00 102.99 ? 217 ASP B O   1 
ATOM   5987  C CB  . ASP B 1 217 ? 34.283  56.658  -53.395 1.00 101.30 ? 217 ASP B CB  1 
ATOM   5988  C CG  . ASP B 1 217 ? 33.911  55.605  -54.423 1.00 99.29  ? 217 ASP B CG  1 
ATOM   5989  O OD1 . ASP B 1 217 ? 33.801  54.429  -54.024 1.00 98.44  ? 217 ASP B OD1 1 
ATOM   5990  O OD2 . ASP B 1 217 ? 33.781  55.952  -55.611 1.00 99.21  ? 217 ASP B OD2 1 
ATOM   5991  N N   . LYS B 1 218 ? 34.652  54.198  -50.689 1.00 98.31  ? 218 LYS B N   1 
ATOM   5992  C CA  . LYS B 1 218 ? 33.905  53.401  -49.727 1.00 98.39  ? 218 LYS B CA  1 
ATOM   5993  C C   . LYS B 1 218 ? 34.876  52.738  -48.757 1.00 95.41  ? 218 LYS B C   1 
ATOM   5994  O O   . LYS B 1 218 ? 36.074  52.672  -49.017 1.00 94.43  ? 218 LYS B O   1 
ATOM   5995  C CB  . LYS B 1 218 ? 33.100  52.284  -50.403 1.00 98.84  ? 218 LYS B CB  1 
ATOM   5996  C CG  . LYS B 1 218 ? 32.271  52.730  -51.591 1.00 102.39 ? 218 LYS B CG  1 
ATOM   5997  C CD  . LYS B 1 218 ? 31.380  51.672  -52.235 1.00 103.91 ? 218 LYS B CD  1 
ATOM   5998  C CE  . LYS B 1 218 ? 30.262  52.368  -52.982 1.00 108.80 ? 218 LYS B CE  1 
ATOM   5999  N NZ  . LYS B 1 218 ? 29.769  51.518  -54.066 1.00 109.16 ? 218 LYS B NZ  1 
ATOM   6000  N N   . PRO B 1 219 ? 34.399  52.214  -47.614 1.00 94.36  ? 219 PRO B N   1 
ATOM   6001  C CA  . PRO B 1 219 ? 35.186  51.259  -46.837 1.00 93.08  ? 219 PRO B CA  1 
ATOM   6002  C C   . PRO B 1 219 ? 35.584  50.060  -47.698 1.00 90.73  ? 219 PRO B C   1 
ATOM   6003  O O   . PRO B 1 219 ? 34.794  49.671  -48.561 1.00 91.39  ? 219 PRO B O   1 
ATOM   6004  C CB  . PRO B 1 219 ? 34.221  50.877  -45.715 1.00 93.50  ? 219 PRO B CB  1 
ATOM   6005  C CG  . PRO B 1 219 ? 33.355  52.099  -45.574 1.00 96.31  ? 219 PRO B CG  1 
ATOM   6006  C CD  . PRO B 1 219 ? 33.104  52.524  -47.003 1.00 96.49  ? 219 PRO B CD  1 
ATOM   6007  N N   . PHE B 1 220 ? 36.798  49.516  -47.477 1.00 88.09  ? 220 PHE B N   1 
ATOM   6008  C CA  . PHE B 1 220 ? 37.268  48.307  -48.155 1.00 86.04  ? 220 PHE B CA  1 
ATOM   6009  C C   . PHE B 1 220 ? 37.724  47.277  -47.118 1.00 84.59  ? 220 PHE B C   1 
ATOM   6010  O O   . PHE B 1 220 ? 38.559  47.548  -46.265 1.00 84.24  ? 220 PHE B O   1 
ATOM   6011  C CB  . PHE B 1 220 ? 38.381  48.577  -49.181 1.00 85.39  ? 220 PHE B CB  1 
ATOM   6012  C CG  . PHE B 1 220 ? 39.323  47.413  -49.464 1.00 83.18  ? 220 PHE B CG  1 
ATOM   6013  C CD1 . PHE B 1 220 ? 38.849  46.228  -50.019 1.00 82.40  ? 220 PHE B CD1 1 
ATOM   6014  C CD2 . PHE B 1 220 ? 40.688  47.509  -49.201 1.00 82.77  ? 220 PHE B CD2 1 
ATOM   6015  C CE1 . PHE B 1 220 ? 39.712  45.153  -50.275 1.00 80.93  ? 220 PHE B CE1 1 
ATOM   6016  C CE2 . PHE B 1 220 ? 41.540  46.436  -49.459 1.00 81.12  ? 220 PHE B CE2 1 
ATOM   6017  C CZ  . PHE B 1 220 ? 41.052  45.252  -49.987 1.00 79.64  ? 220 PHE B CZ  1 
ATOM   6018  N N   . ILE B 1 221 ? 37.184  46.064  -47.200 1.00 84.09  ? 221 ILE B N   1 
ATOM   6019  C CA  . ILE B 1 221 ? 37.500  45.037  -46.220 1.00 83.53  ? 221 ILE B CA  1 
ATOM   6020  C C   . ILE B 1 221 ? 38.031  43.800  -46.943 1.00 81.75  ? 221 ILE B C   1 
ATOM   6021  O O   . ILE B 1 221 ? 37.695  43.593  -48.106 1.00 81.35  ? 221 ILE B O   1 
ATOM   6022  C CB  . ILE B 1 221 ? 36.263  44.732  -45.359 1.00 84.57  ? 221 ILE B CB  1 
ATOM   6023  C CG1 . ILE B 1 221 ? 35.115  44.145  -46.181 1.00 84.43  ? 221 ILE B CG1 1 
ATOM   6024  C CG2 . ILE B 1 221 ? 35.832  45.987  -44.604 1.00 86.73  ? 221 ILE B CG2 1 
ATOM   6025  C CD1 . ILE B 1 221 ? 33.925  43.716  -45.340 1.00 85.72  ? 221 ILE B CD1 1 
ATOM   6026  N N   . THR B 1 222 ? 38.889  43.023  -46.258 1.00 81.20  ? 222 THR B N   1 
ATOM   6027  C CA  . THR B 1 222 ? 39.290  41.695  -46.710 1.00 79.92  ? 222 THR B CA  1 
ATOM   6028  C C   . THR B 1 222 ? 38.368  40.678  -46.041 1.00 81.30  ? 222 THR B C   1 
ATOM   6029  O O   . THR B 1 222 ? 38.099  40.768  -44.842 1.00 82.51  ? 222 THR B O   1 
ATOM   6030  C CB  . THR B 1 222 ? 40.764  41.412  -46.416 1.00 78.27  ? 222 THR B CB  1 
ATOM   6031  O OG1 . THR B 1 222 ? 40.963  41.491  -45.010 1.00 78.62  ? 222 THR B OG1 1 
ATOM   6032  C CG2 . THR B 1 222 ? 41.696  42.412  -47.070 1.00 78.45  ? 222 THR B CG2 1 
ATOM   6033  N N   . THR B 1 223 ? 37.859  39.743  -46.849 1.00 81.85  ? 223 THR B N   1 
ATOM   6034  C CA  . THR B 1 223 ? 36.876  38.764  -46.408 1.00 83.21  ? 223 THR B CA  1 
ATOM   6035  C C   . THR B 1 223 ? 37.519  37.390  -46.163 1.00 83.99  ? 223 THR B C   1 
ATOM   6036  O O   . THR B 1 223 ? 37.003  36.611  -45.363 1.00 83.96  ? 223 THR B O   1 
ATOM   6037  C CB  . THR B 1 223 ? 35.792  38.767  -47.474 1.00 83.00  ? 223 THR B CB  1 
ATOM   6038  O OG1 . THR B 1 223 ? 36.423  39.304  -48.632 1.00 80.68  ? 223 THR B OG1 1 
ATOM   6039  C CG2 . THR B 1 223 ? 34.706  39.771  -47.150 1.00 85.83  ? 223 THR B CG2 1 
ATOM   6040  N N   . GLU B 1 224 ? 38.668  37.124  -46.817 1.00 84.38  ? 224 GLU B N   1 
ATOM   6041  C CA  . GLU B 1 224 ? 39.505  35.952  -46.583 1.00 84.65  ? 224 GLU B CA  1 
ATOM   6042  C C   . GLU B 1 224 ? 40.979  36.343  -46.827 1.00 81.13  ? 224 GLU B C   1 
ATOM   6043  O O   . GLU B 1 224 ? 41.251  37.252  -47.608 1.00 78.47  ? 224 GLU B O   1 
ATOM   6044  C CB  . GLU B 1 224 ? 39.169  34.777  -47.525 1.00 89.07  ? 224 GLU B CB  1 
ATOM   6045  C CG  . GLU B 1 224 ? 37.791  34.101  -47.436 1.00 94.66  ? 224 GLU B CG  1 
ATOM   6046  C CD  . GLU B 1 224 ? 37.561  32.907  -48.395 1.00 99.79  ? 224 GLU B CD  1 
ATOM   6047  O OE1 . GLU B 1 224 ? 38.141  32.875  -49.520 1.00 102.93 ? 224 GLU B OE1 1 
ATOM   6048  O OE2 . GLU B 1 224 ? 36.783  31.974  -48.052 1.00 102.31 ? 224 GLU B OE2 1 
ATOM   6049  N N   . PHE B 1 225 ? 41.930  35.637  -46.173 1.00 79.10  ? 225 PHE B N   1 
ATOM   6050  C CA  . PHE B 1 225 ? 43.358  35.639  -46.495 1.00 75.84  ? 225 PHE B CA  1 
ATOM   6051  C C   . PHE B 1 225 ? 44.079  34.632  -45.585 1.00 74.36  ? 225 PHE B C   1 
ATOM   6052  O O   . PHE B 1 225 ? 43.801  34.590  -44.387 1.00 73.21  ? 225 PHE B O   1 
ATOM   6053  C CB  . PHE B 1 225 ? 43.981  37.045  -46.394 1.00 75.93  ? 225 PHE B CB  1 
ATOM   6054  C CG  . PHE B 1 225 ? 43.958  37.724  -45.026 1.00 75.45  ? 225 PHE B CG  1 
ATOM   6055  C CD1 . PHE B 1 225 ? 42.877  38.494  -44.629 1.00 75.90  ? 225 PHE B CD1 1 
ATOM   6056  C CD2 . PHE B 1 225 ? 45.031  37.609  -44.148 1.00 74.53  ? 225 PHE B CD2 1 
ATOM   6057  C CE1 . PHE B 1 225 ? 42.862  39.097  -43.378 1.00 76.86  ? 225 PHE B CE1 1 
ATOM   6058  C CE2 . PHE B 1 225 ? 45.013  38.216  -42.904 1.00 74.85  ? 225 PHE B CE2 1 
ATOM   6059  C CZ  . PHE B 1 225 ? 43.922  38.936  -42.512 1.00 76.48  ? 225 PHE B CZ  1 
ATOM   6060  N N   . GLY B 1 226 ? 44.999  33.812  -46.147 1.00 73.63  ? 226 GLY B N   1 
ATOM   6061  C CA  . GLY B 1 226 ? 45.783  32.872  -45.338 1.00 73.24  ? 226 GLY B CA  1 
ATOM   6062  C C   . GLY B 1 226 ? 46.416  31.684  -46.084 1.00 71.87  ? 226 GLY B C   1 
ATOM   6063  O O   . GLY B 1 226 ? 46.606  31.678  -47.296 1.00 72.54  ? 226 GLY B O   1 
ATOM   6064  N N   . TYR B 1 227 ? 46.776  30.640  -45.339 1.00 70.19  ? 227 TYR B N   1 
ATOM   6065  C CA  . TYR B 1 227 ? 47.710  29.669  -45.870 1.00 69.07  ? 227 TYR B CA  1 
ATOM   6066  C C   . TYR B 1 227 ? 47.383  28.300  -45.306 1.00 69.41  ? 227 TYR B C   1 
ATOM   6067  O O   . TYR B 1 227 ? 46.989  28.206  -44.146 1.00 69.74  ? 227 TYR B O   1 
ATOM   6068  C CB  . TYR B 1 227 ? 49.153  30.078  -45.517 1.00 68.55  ? 227 TYR B CB  1 
ATOM   6069  C CG  . TYR B 1 227 ? 49.646  31.309  -46.272 1.00 67.32  ? 227 TYR B CG  1 
ATOM   6070  C CD1 . TYR B 1 227 ? 49.981  31.228  -47.617 1.00 66.25  ? 227 TYR B CD1 1 
ATOM   6071  C CD2 . TYR B 1 227 ? 49.708  32.563  -45.659 1.00 68.07  ? 227 TYR B CD2 1 
ATOM   6072  C CE1 . TYR B 1 227 ? 50.369  32.348  -48.328 1.00 66.29  ? 227 TYR B CE1 1 
ATOM   6073  C CE2 . TYR B 1 227 ? 50.131  33.694  -46.345 1.00 67.32  ? 227 TYR B CE2 1 
ATOM   6074  C CZ  . TYR B 1 227 ? 50.473  33.575  -47.684 1.00 66.74  ? 227 TYR B CZ  1 
ATOM   6075  O OH  . TYR B 1 227 ? 50.888  34.649  -48.399 1.00 66.10  ? 227 TYR B OH  1 
ATOM   6076  N N   . SER B 1 228 ? 47.599  27.260  -46.130 1.00 69.47  ? 228 SER B N   1 
ATOM   6077  C CA  . SER B 1 228 ? 47.274  25.882  -45.769 1.00 69.84  ? 228 SER B CA  1 
ATOM   6078  C C   . SER B 1 228 ? 48.521  25.161  -45.278 1.00 69.31  ? 228 SER B C   1 
ATOM   6079  O O   . SER B 1 228 ? 49.575  25.290  -45.880 1.00 68.60  ? 228 SER B O   1 
ATOM   6080  C CB  . SER B 1 228 ? 46.675  25.106  -46.911 1.00 70.24  ? 228 SER B CB  1 
ATOM   6081  O OG  . SER B 1 228 ? 46.940  23.710  -46.775 1.00 70.99  ? 228 SER B OG  1 
ATOM   6082  N N   . VAL B 1 229 ? 48.365  24.350  -44.232 1.00 69.96  ? 229 VAL B N   1 
ATOM   6083  C CA  . VAL B 1 229 ? 49.494  23.668  -43.628 1.00 70.31  ? 229 VAL B CA  1 
ATOM   6084  C C   . VAL B 1 229 ? 49.405  22.169  -43.920 1.00 71.42  ? 229 VAL B C   1 
ATOM   6085  O O   . VAL B 1 229 ? 49.858  21.366  -43.112 1.00 72.33  ? 229 VAL B O   1 
ATOM   6086  C CB  . VAL B 1 229 ? 49.586  23.953  -42.113 1.00 70.70  ? 229 VAL B CB  1 
ATOM   6087  C CG1 . VAL B 1 229 ? 50.010  25.392  -41.817 1.00 69.56  ? 229 VAL B CG1 1 
ATOM   6088  C CG2 . VAL B 1 229 ? 48.296  23.608  -41.374 1.00 71.99  ? 229 VAL B CG2 1 
ATOM   6089  N N   . SER B 1 230 ? 48.864  21.805  -45.091 1.00 71.74  ? 230 SER B N   1 
ATOM   6090  C CA  . SER B 1 230 ? 48.677  20.410  -45.455 1.00 73.43  ? 230 SER B CA  1 
ATOM   6091  C C   . SER B 1 230 ? 50.027  19.691  -45.566 1.00 74.61  ? 230 SER B C   1 
ATOM   6092  O O   . SER B 1 230 ? 50.987  20.239  -46.078 1.00 75.02  ? 230 SER B O   1 
ATOM   6093  C CB  . SER B 1 230 ? 47.858  20.291  -46.722 1.00 73.22  ? 230 SER B CB  1 
ATOM   6094  O OG  . SER B 1 230 ? 48.264  21.213  -47.719 1.00 71.80  ? 230 SER B OG  1 
ATOM   6095  N N   . PRO B 1 231 ? 50.177  18.440  -45.085 1.00 76.20  ? 231 PRO B N   1 
ATOM   6096  C CA  . PRO B 1 231 ? 51.444  17.734  -45.197 1.00 77.07  ? 231 PRO B CA  1 
ATOM   6097  C C   . PRO B 1 231 ? 51.979  17.844  -46.615 1.00 77.27  ? 231 PRO B C   1 
ATOM   6098  O O   . PRO B 1 231 ? 53.191  17.937  -46.803 1.00 77.87  ? 231 PRO B O   1 
ATOM   6099  C CB  . PRO B 1 231 ? 51.096  16.300  -44.853 1.00 78.72  ? 231 PRO B CB  1 
ATOM   6100  C CG  . PRO B 1 231 ? 49.901  16.422  -43.959 1.00 79.20  ? 231 PRO B CG  1 
ATOM   6101  C CD  . PRO B 1 231 ? 49.138  17.627  -44.452 1.00 77.89  ? 231 PRO B CD  1 
ATOM   6102  N N   . GLU B 1 232 ? 51.062  17.801  -47.592 1.00 77.61  ? 232 GLU B N   1 
ATOM   6103  C CA  . GLU B 1 232 ? 51.425  17.960  -48.991 1.00 77.42  ? 232 GLU B CA  1 
ATOM   6104  C C   . GLU B 1 232 ? 50.200  18.378  -49.802 1.00 77.63  ? 232 GLU B C   1 
ATOM   6105  O O   . GLU B 1 232 ? 49.144  18.667  -49.234 1.00 77.13  ? 232 GLU B O   1 
ATOM   6106  C CB  . GLU B 1 232 ? 52.036  16.664  -49.520 1.00 78.82  ? 232 GLU B CB  1 
ATOM   6107  C CG  . GLU B 1 232 ? 51.027  15.535  -49.684 1.00 80.72  ? 232 GLU B CG  1 
ATOM   6108  C CD  . GLU B 1 232 ? 51.668  14.161  -49.685 1.00 82.69  ? 232 GLU B CD  1 
ATOM   6109  O OE1 . GLU B 1 232 ? 52.288  13.816  -48.652 1.00 83.42  ? 232 GLU B OE1 1 
ATOM   6110  O OE2 . GLU B 1 232 ? 51.533  13.442  -50.702 1.00 83.84  ? 232 GLU B OE2 1 
ATOM   6111  N N   . GLY B 1 233 ? 50.376  18.409  -51.132 1.00 77.71  ? 233 GLY B N   1 
ATOM   6112  C CA  . GLY B 1 233 ? 49.331  18.790  -52.068 1.00 77.33  ? 233 GLY B CA  1 
ATOM   6113  C C   . GLY B 1 233 ? 49.407  20.281  -52.395 1.00 76.08  ? 233 GLY B C   1 
ATOM   6114  O O   . GLY B 1 233 ? 49.867  21.088  -51.591 1.00 74.19  ? 233 GLY B O   1 
ATOM   6115  N N   . GLY B 1 234 ? 48.935  20.636  -53.588 1.00 76.65  ? 234 GLY B N   1 
ATOM   6116  C CA  . GLY B 1 234 ? 48.715  22.028  -53.923 1.00 77.24  ? 234 GLY B CA  1 
ATOM   6117  C C   . GLY B 1 234 ? 49.668  22.459  -55.022 1.00 79.47  ? 234 GLY B C   1 
ATOM   6118  O O   . GLY B 1 234 ? 49.946  21.672  -55.919 1.00 82.76  ? 234 GLY B O   1 
ATOM   6119  N N   . ASN B 1 235 ? 50.146  23.705  -54.923 1.00 80.89  ? 235 ASN B N   1 
ATOM   6120  C CA  . ASN B 1 235 ? 51.230  24.203  -55.751 1.00 82.31  ? 235 ASN B CA  1 
ATOM   6121  C C   . ASN B 1 235 ? 51.797  25.474  -55.112 1.00 78.92  ? 235 ASN B C   1 
ATOM   6122  O O   . ASN B 1 235 ? 51.069  26.260  -54.510 1.00 76.93  ? 235 ASN B O   1 
ATOM   6123  C CB  . ASN B 1 235 ? 50.781  24.403  -57.194 1.00 87.29  ? 235 ASN B CB  1 
ATOM   6124  C CG  . ASN B 1 235 ? 51.889  24.980  -58.044 1.00 93.47  ? 235 ASN B CG  1 
ATOM   6125  O OD1 . ASN B 1 235 ? 52.904  24.312  -58.287 1.00 101.80 ? 235 ASN B OD1 1 
ATOM   6126  N ND2 . ASN B 1 235 ? 51.732  26.221  -58.485 1.00 94.29  ? 235 ASN B ND2 1 
ATOM   6127  N N   . GLY B 1 236 ? 53.117  25.646  -55.237 1.00 77.21  ? 236 GLY B N   1 
ATOM   6128  C CA  . GLY B 1 236 ? 53.839  26.678  -54.521 1.00 75.40  ? 236 GLY B CA  1 
ATOM   6129  C C   . GLY B 1 236 ? 53.306  26.833  -53.102 1.00 75.04  ? 236 GLY B C   1 
ATOM   6130  O O   . GLY B 1 236 ? 53.360  25.925  -52.284 1.00 76.39  ? 236 GLY B O   1 
ATOM   6131  N N   . GLN B 1 237 ? 52.740  27.996  -52.837 1.00 74.19  ? 237 GLN B N   1 
ATOM   6132  C CA  . GLN B 1 237 ? 52.412  28.372  -51.482 1.00 74.57  ? 237 GLN B CA  1 
ATOM   6133  C C   . GLN B 1 237 ? 50.991  27.959  -51.124 1.00 75.34  ? 237 GLN B C   1 
ATOM   6134  O O   . GLN B 1 237 ? 50.657  27.871  -49.942 1.00 75.19  ? 237 GLN B O   1 
ATOM   6135  C CB  . GLN B 1 237 ? 52.518  29.892  -51.398 1.00 74.16  ? 237 GLN B CB  1 
ATOM   6136  C CG  . GLN B 1 237 ? 53.931  30.433  -51.521 1.00 72.68  ? 237 GLN B CG  1 
ATOM   6137  C CD  . GLN B 1 237 ? 54.015  31.738  -50.784 1.00 73.20  ? 237 GLN B CD  1 
ATOM   6138  O OE1 . GLN B 1 237 ? 53.761  31.784  -49.575 1.00 72.99  ? 237 GLN B OE1 1 
ATOM   6139  N NE2 . GLN B 1 237 ? 54.286  32.811  -51.514 1.00 74.10  ? 237 GLN B NE2 1 
ATOM   6140  N N   . TYR B 1 238 ? 50.135  27.843  -52.150 1.00 76.13  ? 238 TYR B N   1 
ATOM   6141  C CA  . TYR B 1 238 ? 48.828  27.230  -51.991 1.00 75.47  ? 238 TYR B CA  1 
ATOM   6142  C C   . TYR B 1 238 ? 49.064  25.786  -51.551 1.00 76.66  ? 238 TYR B C   1 
ATOM   6143  O O   . TYR B 1 238 ? 49.469  24.957  -52.364 1.00 77.00  ? 238 TYR B O   1 
ATOM   6144  C CB  . TYR B 1 238 ? 48.013  27.310  -53.286 1.00 74.68  ? 238 TYR B CB  1 
ATOM   6145  C CG  . TYR B 1 238 ? 46.683  26.577  -53.178 1.00 74.24  ? 238 TYR B CG  1 
ATOM   6146  C CD1 . TYR B 1 238 ? 45.693  27.045  -52.328 1.00 73.69  ? 238 TYR B CD1 1 
ATOM   6147  C CD2 . TYR B 1 238 ? 46.432  25.402  -53.881 1.00 74.75  ? 238 TYR B CD2 1 
ATOM   6148  C CE1 . TYR B 1 238 ? 44.479  26.391  -52.196 1.00 74.44  ? 238 TYR B CE1 1 
ATOM   6149  C CE2 . TYR B 1 238 ? 45.222  24.736  -53.759 1.00 75.79  ? 238 TYR B CE2 1 
ATOM   6150  C CZ  . TYR B 1 238 ? 44.231  25.247  -52.928 1.00 75.11  ? 238 TYR B CZ  1 
ATOM   6151  O OH  . TYR B 1 238 ? 43.019  24.652  -52.771 1.00 73.97  ? 238 TYR B OH  1 
ATOM   6152  N N   . GLY B 1 239 ? 48.894  25.529  -50.244 1.00 76.52  ? 239 GLY B N   1 
ATOM   6153  C CA  . GLY B 1 239 ? 49.172  24.229  -49.652 1.00 76.11  ? 239 GLY B CA  1 
ATOM   6154  C C   . GLY B 1 239 ? 50.605  24.062  -49.135 1.00 74.78  ? 239 GLY B C   1 
ATOM   6155  O O   . GLY B 1 239 ? 51.470  24.932  -49.271 1.00 73.66  ? 239 GLY B O   1 
ATOM   6156  N N   . SER B 1 240 ? 50.803  22.911  -48.483 1.00 75.44  ? 240 SER B N   1 
ATOM   6157  C CA  . SER B 1 240 ? 52.111  22.366  -48.155 1.00 76.14  ? 240 SER B CA  1 
ATOM   6158  C C   . SER B 1 240 ? 52.981  23.384  -47.424 1.00 74.94  ? 240 SER B C   1 
ATOM   6159  O O   . SER B 1 240 ? 54.194  23.380  -47.606 1.00 75.48  ? 240 SER B O   1 
ATOM   6160  C CB  . SER B 1 240 ? 52.799  21.838  -49.384 1.00 76.45  ? 240 SER B CB  1 
ATOM   6161  O OG  . SER B 1 240 ? 52.007  20.825  -49.988 1.00 77.42  ? 240 SER B OG  1 
ATOM   6162  N N   . ASN B 1 241 ? 52.351  24.205  -46.574 1.00 72.75  ? 241 ASN B N   1 
ATOM   6163  C CA  . ASN B 1 241 ? 53.064  25.113  -45.703 1.00 71.13  ? 241 ASN B CA  1 
ATOM   6164  C C   . ASN B 1 241 ? 53.405  24.459  -44.371 1.00 70.61  ? 241 ASN B C   1 
ATOM   6165  O O   . ASN B 1 241 ? 52.676  23.596  -43.892 1.00 70.00  ? 241 ASN B O   1 
ATOM   6166  C CB  . ASN B 1 241 ? 52.239  26.358  -45.438 1.00 71.66  ? 241 ASN B CB  1 
ATOM   6167  C CG  . ASN B 1 241 ? 52.385  27.332  -46.572 1.00 71.66  ? 241 ASN B CG  1 
ATOM   6168  O OD1 . ASN B 1 241 ? 53.393  28.043  -46.612 1.00 71.89  ? 241 ASN B OD1 1 
ATOM   6169  N ND2 . ASN B 1 241 ? 51.420  27.374  -47.481 1.00 72.18  ? 241 ASN B ND2 1 
ATOM   6170  N N   . THR B 1 242 ? 54.518  24.912  -43.772 1.00 70.32  ? 242 THR B N   1 
ATOM   6171  C CA  . THR B 1 242 ? 54.779  24.628  -42.370 1.00 71.24  ? 242 THR B CA  1 
ATOM   6172  C C   . THR B 1 242 ? 53.905  25.522  -41.488 1.00 72.21  ? 242 THR B C   1 
ATOM   6173  O O   . THR B 1 242 ? 53.232  26.450  -41.949 1.00 72.47  ? 242 THR B O   1 
ATOM   6174  C CB  . THR B 1 242 ? 56.257  24.790  -42.035 1.00 70.75  ? 242 THR B CB  1 
ATOM   6175  O OG1 . THR B 1 242 ? 56.560  26.172  -42.126 1.00 69.18  ? 242 THR B OG1 1 
ATOM   6176  C CG2 . THR B 1 242 ? 57.136  23.959  -42.951 1.00 71.40  ? 242 THR B CG2 1 
ATOM   6177  N N   . LEU B 1 243 ? 53.912  25.218  -40.190 1.00 73.00  ? 243 LEU B N   1 
ATOM   6178  C CA  . LEU B 1 243 ? 53.203  26.027  -39.219 1.00 72.92  ? 243 LEU B CA  1 
ATOM   6179  C C   . LEU B 1 243 ? 53.826  27.420  -39.189 1.00 71.99  ? 243 LEU B C   1 
ATOM   6180  O O   . LEU B 1 243 ? 53.098  28.420  -39.201 1.00 70.89  ? 243 LEU B O   1 
ATOM   6181  C CB  . LEU B 1 243 ? 53.278  25.304  -37.874 1.00 74.20  ? 243 LEU B CB  1 
ATOM   6182  C CG  . LEU B 1 243 ? 52.500  23.988  -37.787 1.00 74.94  ? 243 LEU B CG  1 
ATOM   6183  C CD1 . LEU B 1 243 ? 52.767  23.228  -36.495 1.00 76.27  ? 243 LEU B CD1 1 
ATOM   6184  C CD2 . LEU B 1 243 ? 51.023  24.307  -37.939 1.00 74.98  ? 243 LEU B CD2 1 
ATOM   6185  N N   . LYS B 1 244 ? 55.174  27.449  -39.184 1.00 71.63  ? 244 LYS B N   1 
ATOM   6186  C CA  . LYS B 1 244 ? 55.920  28.691  -39.108 1.00 71.40  ? 244 LYS B CA  1 
ATOM   6187  C C   . LYS B 1 244 ? 55.657  29.550  -40.344 1.00 70.30  ? 244 LYS B C   1 
ATOM   6188  O O   . LYS B 1 244 ? 55.513  30.771  -40.232 1.00 69.27  ? 244 LYS B O   1 
ATOM   6189  C CB  . LYS B 1 244 ? 57.424  28.449  -39.004 1.00 72.03  ? 244 LYS B CB  1 
ATOM   6190  C CG  . LYS B 1 244 ? 58.275  29.725  -39.047 1.00 72.00  ? 244 LYS B CG  1 
ATOM   6191  C CD  . LYS B 1 244 ? 59.751  29.509  -38.754 1.00 72.30  ? 244 LYS B CD  1 
ATOM   6192  C CE  . LYS B 1 244 ? 60.332  30.634  -37.953 1.00 73.39  ? 244 LYS B CE  1 
ATOM   6193  N NZ  . LYS B 1 244 ? 59.935  31.960  -38.443 1.00 73.58  ? 244 LYS B NZ  1 
ATOM   6194  N N   . GLN B 1 245 ? 55.615  28.898  -41.513 1.00 69.54  ? 245 GLN B N   1 
ATOM   6195  C CA  . GLN B 1 245 ? 55.271  29.589  -42.737 1.00 69.92  ? 245 GLN B CA  1 
ATOM   6196  C C   . GLN B 1 245 ? 53.908  30.249  -42.569 1.00 70.48  ? 245 GLN B C   1 
ATOM   6197  O O   . GLN B 1 245 ? 53.738  31.408  -42.950 1.00 70.34  ? 245 GLN B O   1 
ATOM   6198  C CB  . GLN B 1 245 ? 55.314  28.647  -43.931 1.00 70.72  ? 245 GLN B CB  1 
ATOM   6199  C CG  . GLN B 1 245 ? 56.751  28.358  -44.337 1.00 73.45  ? 245 GLN B CG  1 
ATOM   6200  C CD  . GLN B 1 245 ? 56.923  27.306  -45.407 1.00 76.59  ? 245 GLN B CD  1 
ATOM   6201  O OE1 . GLN B 1 245 ? 56.455  26.153  -45.298 1.00 78.40  ? 245 GLN B OE1 1 
ATOM   6202  N NE2 . GLN B 1 245 ? 57.653  27.718  -46.437 1.00 76.79  ? 245 GLN B NE2 1 
ATOM   6203  N N   . GLN B 1 246 ? 52.960  29.506  -41.979 1.00 69.85  ? 246 GLN B N   1 
ATOM   6204  C CA  . GLN B 1 246 ? 51.608  30.000  -41.822 1.00 69.51  ? 246 GLN B CA  1 
ATOM   6205  C C   . GLN B 1 246 ? 51.618  31.187  -40.870 1.00 69.06  ? 246 GLN B C   1 
ATOM   6206  O O   . GLN B 1 246 ? 51.270  32.285  -41.281 1.00 69.60  ? 246 GLN B O   1 
ATOM   6207  C CB  . GLN B 1 246 ? 50.704  28.871  -41.339 1.00 70.40  ? 246 GLN B CB  1 
ATOM   6208  C CG  . GLN B 1 246 ? 49.232  29.234  -41.199 1.00 70.79  ? 246 GLN B CG  1 
ATOM   6209  C CD  . GLN B 1 246 ? 48.510  28.216  -40.342 1.00 72.16  ? 246 GLN B CD  1 
ATOM   6210  O OE1 . GLN B 1 246 ? 48.840  28.028  -39.162 1.00 73.54  ? 246 GLN B OE1 1 
ATOM   6211  N NE2 . GLN B 1 246 ? 47.545  27.519  -40.929 1.00 72.06  ? 246 GLN B NE2 1 
ATOM   6212  N N   . SER B 1 247 ? 52.027  30.961  -39.617 1.00 68.61  ? 247 SER B N   1 
ATOM   6213  C CA  . SER B 1 247 ? 52.063  32.015  -38.611 1.00 68.78  ? 247 SER B CA  1 
ATOM   6214  C C   . SER B 1 247 ? 52.760  33.268  -39.174 1.00 68.48  ? 247 SER B C   1 
ATOM   6215  O O   . SER B 1 247 ? 52.134  34.300  -39.381 1.00 67.98  ? 247 SER B O   1 
ATOM   6216  C CB  . SER B 1 247 ? 52.679  31.468  -37.333 1.00 69.43  ? 247 SER B CB  1 
ATOM   6217  O OG  . SER B 1 247 ? 52.865  32.444  -36.318 1.00 70.09  ? 247 SER B OG  1 
ATOM   6218  N N   . ASP B 1 248 ? 54.034  33.157  -39.560 1.00 68.48  ? 248 ASP B N   1 
ATOM   6219  C CA  . ASP B 1 248 ? 54.734  34.243  -40.230 1.00 68.35  ? 248 ASP B CA  1 
ATOM   6220  C C   . ASP B 1 248 ? 53.929  34.876  -41.386 1.00 68.75  ? 248 ASP B C   1 
ATOM   6221  O O   . ASP B 1 248 ? 54.069  36.079  -41.618 1.00 70.74  ? 248 ASP B O   1 
ATOM   6222  C CB  . ASP B 1 248 ? 56.107  33.801  -40.727 1.00 67.39  ? 248 ASP B CB  1 
ATOM   6223  C CG  . ASP B 1 248 ? 57.184  33.423  -39.713 1.00 67.60  ? 248 ASP B CG  1 
ATOM   6224  O OD1 . ASP B 1 248 ? 57.117  33.832  -38.541 1.00 67.65  ? 248 ASP B OD1 1 
ATOM   6225  O OD2 . ASP B 1 248 ? 58.074  32.647  -40.102 1.00 67.70  ? 248 ASP B OD2 1 
ATOM   6226  N N   . GLY B 1 249 ? 53.135  34.101  -42.138 1.00 68.34  ? 249 GLY B N   1 
ATOM   6227  C CA  . GLY B 1 249 ? 52.548  34.545  -43.396 1.00 68.53  ? 249 GLY B CA  1 
ATOM   6228  C C   . GLY B 1 249 ? 51.203  35.256  -43.210 1.00 70.29  ? 249 GLY B C   1 
ATOM   6229  O O   . GLY B 1 249 ? 50.861  36.169  -43.963 1.00 71.60  ? 249 GLY B O   1 
ATOM   6230  N N   . LEU B 1 250 ? 50.412  34.855  -42.209 1.00 71.06  ? 250 LEU B N   1 
ATOM   6231  C CA  . LEU B 1 250 ? 49.224  35.621  -41.848 1.00 71.64  ? 250 LEU B CA  1 
ATOM   6232  C C   . LEU B 1 250 ? 49.599  37.065  -41.530 1.00 72.70  ? 250 LEU B C   1 
ATOM   6233  O O   . LEU B 1 250 ? 49.016  37.991  -42.081 1.00 72.52  ? 250 LEU B O   1 
ATOM   6234  C CB  . LEU B 1 250 ? 48.484  34.992  -40.670 1.00 72.32  ? 250 LEU B CB  1 
ATOM   6235  C CG  . LEU B 1 250 ? 47.300  34.090  -41.033 1.00 72.10  ? 250 LEU B CG  1 
ATOM   6236  C CD1 . LEU B 1 250 ? 46.147  34.903  -41.613 1.00 71.74  ? 250 LEU B CD1 1 
ATOM   6237  C CD2 . LEU B 1 250 ? 47.767  32.998  -41.998 1.00 71.32  ? 250 LEU B CD2 1 
ATOM   6238  N N   . ILE B 1 251 ? 50.588  37.233  -40.643 1.00 74.12  ? 251 ILE B N   1 
ATOM   6239  C CA  . ILE B 1 251 ? 51.101  38.535  -40.230 1.00 74.93  ? 251 ILE B CA  1 
ATOM   6240  C C   . ILE B 1 251 ? 51.534  39.335  -41.464 1.00 75.03  ? 251 ILE B C   1 
ATOM   6241  O O   . ILE B 1 251 ? 51.234  40.528  -41.590 1.00 75.11  ? 251 ILE B O   1 
ATOM   6242  C CB  . ILE B 1 251 ? 52.248  38.367  -39.206 1.00 74.54  ? 251 ILE B CB  1 
ATOM   6243  C CG1 . ILE B 1 251 ? 51.813  37.578  -37.950 1.00 74.66  ? 251 ILE B CG1 1 
ATOM   6244  C CG2 . ILE B 1 251 ? 52.839  39.727  -38.821 1.00 75.55  ? 251 ILE B CG2 1 
ATOM   6245  C CD1 . ILE B 1 251 ? 50.482  38.033  -37.348 1.00 75.53  ? 251 ILE B CD1 1 
ATOM   6246  N N   . SER B 1 252 ? 52.210  38.666  -42.406 1.00 74.41  ? 252 SER B N   1 
ATOM   6247  C CA  . SER B 1 252 ? 52.664  39.350  -43.608 1.00 75.25  ? 252 SER B CA  1 
ATOM   6248  C C   . SER B 1 252 ? 51.461  39.931  -44.341 1.00 74.62  ? 252 SER B C   1 
ATOM   6249  O O   . SER B 1 252 ? 51.436  41.099  -44.690 1.00 75.50  ? 252 SER B O   1 
ATOM   6250  C CB  . SER B 1 252 ? 53.463  38.444  -44.491 1.00 75.14  ? 252 SER B CB  1 
ATOM   6251  O OG  . SER B 1 252 ? 54.174  39.204  -45.454 1.00 77.13  ? 252 SER B OG  1 
ATOM   6252  N N   . ASN B 1 253 ? 50.435  39.102  -44.482 1.00 74.27  ? 253 ASN B N   1 
ATOM   6253  C CA  . ASN B 1 253 ? 49.152  39.501  -45.029 1.00 73.96  ? 253 ASN B CA  1 
ATOM   6254  C C   . ASN B 1 253 ? 48.538  40.678  -44.251 1.00 75.30  ? 253 ASN B C   1 
ATOM   6255  O O   . ASN B 1 253 ? 48.091  41.651  -44.857 1.00 75.63  ? 253 ASN B O   1 
ATOM   6256  C CB  . ASN B 1 253 ? 48.234  38.282  -45.077 1.00 73.08  ? 253 ASN B CB  1 
ATOM   6257  C CG  . ASN B 1 253 ? 48.690  37.233  -46.059 1.00 71.31  ? 253 ASN B CG  1 
ATOM   6258  O OD1 . ASN B 1 253 ? 49.712  37.402  -46.727 1.00 70.90  ? 253 ASN B OD1 1 
ATOM   6259  N ND2 . ASN B 1 253 ? 47.916  36.169  -46.199 1.00 71.13  ? 253 ASN B ND2 1 
ATOM   6260  N N   . TYR B 1 254 ? 48.497  40.601  -42.911 1.00 75.54  ? 254 TYR B N   1 
ATOM   6261  C CA  . TYR B 1 254 ? 47.743  41.561  -42.116 1.00 76.74  ? 254 TYR B CA  1 
ATOM   6262  C C   . TYR B 1 254 ? 48.274  42.978  -42.338 1.00 78.60  ? 254 TYR B C   1 
ATOM   6263  O O   . TYR B 1 254 ? 47.500  43.932  -42.383 1.00 79.66  ? 254 TYR B O   1 
ATOM   6264  C CB  . TYR B 1 254 ? 47.810  41.262  -40.615 1.00 77.32  ? 254 TYR B CB  1 
ATOM   6265  C CG  . TYR B 1 254 ? 46.504  41.493  -39.867 1.00 79.05  ? 254 TYR B CG  1 
ATOM   6266  C CD1 . TYR B 1 254 ? 45.966  42.775  -39.704 1.00 80.10  ? 254 TYR B CD1 1 
ATOM   6267  C CD2 . TYR B 1 254 ? 45.790  40.417  -39.330 1.00 79.38  ? 254 TYR B CD2 1 
ATOM   6268  C CE1 . TYR B 1 254 ? 44.765  42.980  -39.035 1.00 80.82  ? 254 TYR B CE1 1 
ATOM   6269  C CE2 . TYR B 1 254 ? 44.580  40.616  -38.670 1.00 80.79  ? 254 TYR B CE2 1 
ATOM   6270  C CZ  . TYR B 1 254 ? 44.072  41.898  -38.512 1.00 81.16  ? 254 TYR B CZ  1 
ATOM   6271  O OH  . TYR B 1 254 ? 42.887  41.996  -37.836 1.00 82.38  ? 254 TYR B OH  1 
ATOM   6272  N N   . ARG B 1 255 ? 49.609  43.106  -42.418 1.00 79.61  ? 255 ARG B N   1 
ATOM   6273  C CA  . ARG B 1 255 ? 50.282  44.383  -42.616 1.00 80.49  ? 255 ARG B CA  1 
ATOM   6274  C C   . ARG B 1 255 ? 50.031  44.864  -44.036 1.00 79.88  ? 255 ARG B C   1 
ATOM   6275  O O   . ARG B 1 255 ? 49.588  45.980  -44.238 1.00 79.92  ? 255 ARG B O   1 
ATOM   6276  C CB  . ARG B 1 255 ? 51.799  44.225  -42.441 1.00 80.80  ? 255 ARG B CB  1 
ATOM   6277  C CG  . ARG B 1 255 ? 52.681  45.338  -42.997 1.00 81.90  ? 255 ARG B CG  1 
ATOM   6278  C CD  . ARG B 1 255 ? 52.642  46.587  -42.127 1.00 84.83  ? 255 ARG B CD  1 
ATOM   6279  N NE  . ARG B 1 255 ? 51.438  47.425  -42.210 1.00 86.53  ? 255 ARG B NE  1 
ATOM   6280  C CZ  . ARG B 1 255 ? 50.665  47.848  -41.196 1.00 89.22  ? 255 ARG B CZ  1 
ATOM   6281  N NH1 . ARG B 1 255 ? 50.791  47.369  -39.965 1.00 90.02  ? 255 ARG B NH1 1 
ATOM   6282  N NH2 . ARG B 1 255 ? 49.722  48.752  -41.425 1.00 89.97  ? 255 ARG B NH2 1 
ATOM   6283  N N   . ASP B 1 256 ? 50.386  44.014  -45.007 1.00 79.34  ? 256 ASP B N   1 
ATOM   6284  C CA  . ASP B 1 256 ? 50.261  44.338  -46.419 1.00 79.37  ? 256 ASP B CA  1 
ATOM   6285  C C   . ASP B 1 256 ? 48.869  44.901  -46.709 1.00 78.88  ? 256 ASP B C   1 
ATOM   6286  O O   . ASP B 1 256 ? 48.754  45.875  -47.433 1.00 79.97  ? 256 ASP B O   1 
ATOM   6287  C CB  . ASP B 1 256 ? 50.536  43.130  -47.309 1.00 78.55  ? 256 ASP B CB  1 
ATOM   6288  C CG  . ASP B 1 256 ? 51.977  42.844  -47.710 1.00 79.11  ? 256 ASP B CG  1 
ATOM   6289  O OD1 . ASP B 1 256 ? 52.759  42.386  -46.841 1.00 80.73  ? 256 ASP B OD1 1 
ATOM   6290  O OD2 . ASP B 1 256 ? 52.292  43.025  -48.914 1.00 79.21  ? 256 ASP B OD2 1 
ATOM   6291  N N   . LEU B 1 257 ? 47.820  44.265  -46.170 1.00 78.10  ? 257 LEU B N   1 
ATOM   6292  C CA  . LEU B 1 257 ? 46.440  44.523  -46.582 1.00 78.42  ? 257 LEU B CA  1 
ATOM   6293  C C   . LEU B 1 257 ? 45.929  45.833  -45.971 1.00 79.78  ? 257 LEU B C   1 
ATOM   6294  O O   . LEU B 1 257 ? 45.114  46.526  -46.578 1.00 79.79  ? 257 LEU B O   1 
ATOM   6295  C CB  . LEU B 1 257 ? 45.552  43.322  -46.228 1.00 76.86  ? 257 LEU B CB  1 
ATOM   6296  C CG  . LEU B 1 257 ? 45.776  42.051  -47.060 1.00 75.08  ? 257 LEU B CG  1 
ATOM   6297  C CD1 . LEU B 1 257 ? 45.144  40.785  -46.461 1.00 74.74  ? 257 LEU B CD1 1 
ATOM   6298  C CD2 . LEU B 1 257 ? 45.271  42.245  -48.482 1.00 74.93  ? 257 LEU B CD2 1 
ATOM   6299  N N   . ILE B 1 258 ? 46.439  46.170  -44.780 1.00 80.66  ? 258 ILE B N   1 
ATOM   6300  C CA  . ILE B 1 258 ? 46.168  47.444  -44.134 1.00 83.19  ? 258 ILE B CA  1 
ATOM   6301  C C   . ILE B 1 258 ? 46.798  48.579  -44.936 1.00 84.32  ? 258 ILE B C   1 
ATOM   6302  O O   . ILE B 1 258 ? 46.131  49.581  -45.226 1.00 86.41  ? 258 ILE B O   1 
ATOM   6303  C CB  . ILE B 1 258 ? 46.653  47.429  -42.674 1.00 83.97  ? 258 ILE B CB  1 
ATOM   6304  C CG1 . ILE B 1 258 ? 45.736  46.550  -41.821 1.00 84.25  ? 258 ILE B CG1 1 
ATOM   6305  C CG2 . ILE B 1 258 ? 46.754  48.847  -42.117 1.00 86.34  ? 258 ILE B CG2 1 
ATOM   6306  C CD1 . ILE B 1 258 ? 46.259  46.252  -40.429 1.00 84.97  ? 258 ILE B CD1 1 
ATOM   6307  N N   . ASP B 1 259 ? 48.086  48.435  -45.252 1.00 83.08  ? 259 ASP B N   1 
ATOM   6308  C CA  . ASP B 1 259 ? 48.643  49.154  -46.384 1.00 84.37  ? 259 ASP B CA  1 
ATOM   6309  C C   . ASP B 1 259 ? 47.758  48.751  -47.557 1.00 84.36  ? 259 ASP B C   1 
ATOM   6310  O O   . ASP B 1 259 ? 47.297  47.622  -47.582 1.00 82.45  ? 259 ASP B O   1 
ATOM   6311  C CB  . ASP B 1 259 ? 50.125  48.858  -46.565 1.00 83.79  ? 259 ASP B CB  1 
ATOM   6312  C CG  . ASP B 1 259 ? 50.911  48.697  -45.269 1.00 83.80  ? 259 ASP B CG  1 
ATOM   6313  O OD1 . ASP B 1 259 ? 50.658  49.508  -44.341 1.00 85.33  ? 259 ASP B OD1 1 
ATOM   6314  O OD2 . ASP B 1 259 ? 51.750  47.763  -45.190 1.00 81.04  ? 259 ASP B OD2 1 
ATOM   6315  N N   . ALA B 1 260 ? 47.443  49.680  -48.464 1.00 87.21  ? 260 ALA B N   1 
ATOM   6316  C CA  . ALA B 1 260 ? 46.398  49.458  -49.462 1.00 87.78  ? 260 ALA B CA  1 
ATOM   6317  C C   . ALA B 1 260 ? 44.998  49.689  -48.882 1.00 89.13  ? 260 ALA B C   1 
ATOM   6318  O O   . ALA B 1 260 ? 44.014  49.594  -49.610 1.00 91.83  ? 260 ALA B O   1 
ATOM   6319  C CB  . ALA B 1 260 ? 46.510  48.080  -50.080 1.00 85.85  ? 260 ALA B CB  1 
ATOM   6320  N N   . GLY B 1 261 ? 44.897  49.953  -47.574 1.00 88.85  ? 261 GLY B N   1 
ATOM   6321  C CA  . GLY B 1 261 ? 43.827  50.778  -47.040 1.00 90.02  ? 261 GLY B CA  1 
ATOM   6322  C C   . GLY B 1 261 ? 42.688  49.982  -46.410 1.00 89.15  ? 261 GLY B C   1 
ATOM   6323  O O   . GLY B 1 261 ? 41.637  50.535  -46.128 1.00 90.20  ? 261 GLY B O   1 
ATOM   6324  N N   . ALA B 1 262 ? 42.864  48.687  -46.166 1.00 88.06  ? 262 ALA B N   1 
ATOM   6325  C CA  . ALA B 1 262 ? 41.774  47.932  -45.565 1.00 87.73  ? 262 ALA B CA  1 
ATOM   6326  C C   . ALA B 1 262 ? 41.508  48.488  -44.170 1.00 89.51  ? 262 ALA B C   1 
ATOM   6327  O O   . ALA B 1 262 ? 42.439  48.820  -43.438 1.00 90.72  ? 262 ALA B O   1 
ATOM   6328  C CB  . ALA B 1 262 ? 42.065  46.447  -45.525 1.00 85.21  ? 262 ALA B CB  1 
ATOM   6329  N N   . VAL B 1 263 ? 40.222  48.632  -43.856 1.00 90.35  ? 263 VAL B N   1 
ATOM   6330  C CA  . VAL B 1 263 ? 39.756  49.094  -42.562 1.00 92.22  ? 263 VAL B CA  1 
ATOM   6331  C C   . VAL B 1 263 ? 38.965  47.942  -41.929 1.00 91.76  ? 263 VAL B C   1 
ATOM   6332  O O   . VAL B 1 263 ? 38.332  48.100  -40.887 1.00 93.18  ? 263 VAL B O   1 
ATOM   6333  C CB  . VAL B 1 263 ? 38.941  50.414  -42.685 1.00 94.92  ? 263 VAL B CB  1 
ATOM   6334  C CG1 . VAL B 1 263 ? 39.513  51.353  -43.740 1.00 94.78  ? 263 VAL B CG1 1 
ATOM   6335  C CG2 . VAL B 1 263 ? 37.451  50.213  -42.981 1.00 95.64  ? 263 VAL B CG2 1 
ATOM   6336  N N   . GLY B 1 264 ? 38.992  46.768  -42.573 1.00 90.58  ? 264 GLY B N   1 
ATOM   6337  C CA  . GLY B 1 264 ? 38.370  45.570  -42.021 1.00 90.18  ? 264 GLY B CA  1 
ATOM   6338  C C   . GLY B 1 264 ? 39.116  44.314  -42.464 1.00 87.48  ? 264 GLY B C   1 
ATOM   6339  O O   . GLY B 1 264 ? 39.615  44.256  -43.584 1.00 87.07  ? 264 GLY B O   1 
ATOM   6340  N N   . MET B 1 265 ? 39.198  43.310  -41.584 1.00 86.37  ? 265 MET B N   1 
ATOM   6341  C CA  . MET B 1 265 ? 40.040  42.157  -41.855 1.00 84.01  ? 265 MET B CA  1 
ATOM   6342  C C   . MET B 1 265 ? 39.329  40.889  -41.394 1.00 84.81  ? 265 MET B C   1 
ATOM   6343  O O   . MET B 1 265 ? 38.860  40.826  -40.261 1.00 87.21  ? 265 MET B O   1 
ATOM   6344  C CB  . MET B 1 265 ? 41.396  42.311  -41.154 1.00 82.72  ? 265 MET B CB  1 
ATOM   6345  C CG  . MET B 1 265 ? 42.217  43.513  -41.622 1.00 82.04  ? 265 MET B CG  1 
ATOM   6346  S SD  . MET B 1 265 ? 42.802  43.388  -43.324 1.00 79.05  ? 265 MET B SD  1 
ATOM   6347  C CE  . MET B 1 265 ? 44.264  42.399  -43.006 1.00 76.77  ? 265 MET B CE  1 
ATOM   6348  N N   . CYS B 1 266 ? 39.251  39.894  -42.290 1.00 83.65  ? 266 CYS B N   1 
ATOM   6349  C CA  . CYS B 1 266 ? 38.598  38.624  -42.004 1.00 83.97  ? 266 CYS B CA  1 
ATOM   6350  C C   . CYS B 1 266 ? 39.545  37.467  -42.340 1.00 84.58  ? 266 CYS B C   1 
ATOM   6351  O O   . CYS B 1 266 ? 39.327  36.729  -43.310 1.00 85.77  ? 266 CYS B O   1 
ATOM   6352  C CB  . CYS B 1 266 ? 37.286  38.482  -42.773 1.00 83.81  ? 266 CYS B CB  1 
ATOM   6353  S SG  . CYS B 1 266 ? 35.983  39.664  -42.317 1.00 82.94  ? 266 CYS B SG  1 
ATOM   6354  N N   . PRO B 1 267 ? 40.616  37.214  -41.532 1.00 84.86  ? 267 PRO B N   1 
ATOM   6355  C CA  . PRO B 1 267 ? 41.512  36.088  -41.755 1.00 82.11  ? 267 PRO B CA  1 
ATOM   6356  C C   . PRO B 1 267 ? 40.768  34.804  -42.042 1.00 81.15  ? 267 PRO B C   1 
ATOM   6357  O O   . PRO B 1 267 ? 39.732  34.553  -41.407 1.00 80.61  ? 267 PRO B O   1 
ATOM   6358  C CB  . PRO B 1 267 ? 42.339  35.998  -40.466 1.00 82.62  ? 267 PRO B CB  1 
ATOM   6359  C CG  . PRO B 1 267 ? 41.633  36.887  -39.492 1.00 85.52  ? 267 PRO B CG  1 
ATOM   6360  C CD  . PRO B 1 267 ? 41.115  37.987  -40.383 1.00 86.65  ? 267 PRO B CD  1 
ATOM   6361  N N   . PHE B 1 268 ? 41.294  33.970  -42.944 1.00 79.98  ? 268 PHE B N   1 
ATOM   6362  C CA  . PHE B 1 268 ? 40.531  32.769  -43.388 1.00 79.46  ? 268 PHE B CA  1 
ATOM   6363  C C   . PHE B 1 268 ? 40.546  31.632  -42.384 1.00 79.62  ? 268 PHE B C   1 
ATOM   6364  O O   . PHE B 1 268 ? 41.651  31.188  -42.030 1.00 76.87  ? 268 PHE B O   1 
ATOM   6365  C CB  . PHE B 1 268 ? 40.996  32.207  -44.733 1.00 78.33  ? 268 PHE B CB  1 
ATOM   6366  C CG  . PHE B 1 268 ? 40.150  31.048  -45.241 1.00 79.27  ? 268 PHE B CG  1 
ATOM   6367  C CD1 . PHE B 1 268 ? 38.763  31.087  -45.164 1.00 78.90  ? 268 PHE B CD1 1 
ATOM   6368  C CD2 . PHE B 1 268 ? 40.742  29.917  -45.788 1.00 80.30  ? 268 PHE B CD2 1 
ATOM   6369  C CE1 . PHE B 1 268 ? 37.996  30.028  -45.619 1.00 80.11  ? 268 PHE B CE1 1 
ATOM   6370  C CE2 . PHE B 1 268 ? 39.969  28.863  -46.247 1.00 81.52  ? 268 PHE B CE2 1 
ATOM   6371  C CZ  . PHE B 1 268 ? 38.599  28.921  -46.162 1.00 82.01  ? 268 PHE B CZ  1 
ATOM   6372  N N   . TYR B 1 269 ? 39.362  31.207  -41.935 1.00 81.38  ? 269 TYR B N   1 
ATOM   6373  C CA  . TYR B 1 269 ? 39.183  30.001  -41.077 1.00 83.38  ? 269 TYR B CA  1 
ATOM   6374  C C   . TYR B 1 269 ? 39.738  30.109  -39.662 1.00 82.91  ? 269 TYR B C   1 
ATOM   6375  O O   . TYR B 1 269 ? 40.805  30.688  -39.430 1.00 82.90  ? 269 TYR B O   1 
ATOM   6376  C CB  . TYR B 1 269 ? 39.695  28.787  -41.857 1.00 84.82  ? 269 TYR B CB  1 
ATOM   6377  C CG  . TYR B 1 269 ? 38.660  27.700  -42.095 1.00 85.07  ? 269 TYR B CG  1 
ATOM   6378  C CD1 . TYR B 1 269 ? 37.364  27.824  -41.612 1.00 87.54  ? 269 TYR B CD1 1 
ATOM   6379  C CD2 . TYR B 1 269 ? 38.987  26.549  -42.796 1.00 85.16  ? 269 TYR B CD2 1 
ATOM   6380  C CE1 . TYR B 1 269 ? 36.423  26.829  -41.818 1.00 91.36  ? 269 TYR B CE1 1 
ATOM   6381  C CE2 . TYR B 1 269 ? 38.057  25.547  -43.006 1.00 87.64  ? 269 TYR B CE2 1 
ATOM   6382  C CZ  . TYR B 1 269 ? 36.770  25.688  -42.519 1.00 91.77  ? 269 TYR B CZ  1 
ATOM   6383  O OH  . TYR B 1 269 ? 35.853  24.700  -42.728 1.00 90.94  ? 269 TYR B OH  1 
ATOM   6384  N N   . TYR B 1 270 ? 38.990  29.535  -38.721 1.00 83.01  ? 270 TYR B N   1 
ATOM   6385  C CA  . TYR B 1 270 ? 39.418  29.482  -37.304 1.00 82.75  ? 270 TYR B CA  1 
ATOM   6386  C C   . TYR B 1 270 ? 39.861  28.070  -37.067 1.00 82.93  ? 270 TYR B C   1 
ATOM   6387  O O   . TYR B 1 270 ? 40.790  27.847  -36.278 1.00 82.65  ? 270 TYR B O   1 
ATOM   6388  C CB  . TYR B 1 270 ? 38.186  29.817  -36.462 1.00 83.33  ? 270 TYR B CB  1 
ATOM   6389  C CG  . TYR B 1 270 ? 37.995  29.087  -35.139 1.00 83.88  ? 270 TYR B CG  1 
ATOM   6390  C CD1 . TYR B 1 270 ? 38.586  29.549  -33.971 1.00 84.31  ? 270 TYR B CD1 1 
ATOM   6391  C CD2 . TYR B 1 270 ? 37.191  27.960  -35.052 1.00 84.58  ? 270 TYR B CD2 1 
ATOM   6392  C CE1 . TYR B 1 270 ? 38.404  28.898  -32.763 1.00 85.99  ? 270 TYR B CE1 1 
ATOM   6393  C CE2 . TYR B 1 270 ? 37.008  27.295  -33.853 1.00 86.41  ? 270 TYR B CE2 1 
ATOM   6394  C CZ  . TYR B 1 270 ? 37.614  27.766  -32.703 1.00 87.14  ? 270 TYR B CZ  1 
ATOM   6395  O OH  . TYR B 1 270 ? 37.431  27.116  -31.518 1.00 89.29  ? 270 TYR B OH  1 
ATOM   6396  N N   . ALA B 1 271 ? 39.177  27.122  -37.716 1.00 84.14  ? 271 ALA B N   1 
ATOM   6397  C CA  . ALA B 1 271 ? 39.577  25.712  -37.614 1.00 84.01  ? 271 ALA B CA  1 
ATOM   6398  C C   . ALA B 1 271 ? 39.431  24.973  -38.946 1.00 83.47  ? 271 ALA B C   1 
ATOM   6399  O O   . ALA B 1 271 ? 38.806  25.454  -39.880 1.00 82.54  ? 271 ALA B O   1 
ATOM   6400  C CB  . ALA B 1 271 ? 38.762  25.008  -36.551 1.00 85.92  ? 271 ALA B CB  1 
ATOM   6401  N N   . ASP B 1 272 ? 40.000  23.765  -39.010 1.00 85.12  ? 272 ASP B N   1 
ATOM   6402  C CA  . ASP B 1 272 ? 40.050  22.966  -40.227 1.00 85.11  ? 272 ASP B CA  1 
ATOM   6403  C C   . ASP B 1 272 ? 38.721  22.276  -40.517 1.00 85.08  ? 272 ASP B C   1 
ATOM   6404  O O   . ASP B 1 272 ? 38.048  21.792  -39.615 1.00 86.65  ? 272 ASP B O   1 
ATOM   6405  C CB  . ASP B 1 272 ? 41.025  21.811  -40.100 1.00 87.09  ? 272 ASP B CB  1 
ATOM   6406  C CG  . ASP B 1 272 ? 42.497  22.156  -40.229 1.00 86.99  ? 272 ASP B CG  1 
ATOM   6407  O OD1 . ASP B 1 272 ? 42.826  23.354  -40.340 1.00 87.65  ? 272 ASP B OD1 1 
ATOM   6408  O OD2 . ASP B 1 272 ? 43.297  21.209  -40.250 1.00 88.19  ? 272 ASP B OD2 1 
ATOM   6409  N N   . GLY B 1 273 ? 38.406  22.177  -41.809 1.00 82.98  ? 273 GLY B N   1 
ATOM   6410  C CA  . GLY B 1 273 ? 37.236  21.470  -42.290 1.00 82.42  ? 273 GLY B CA  1 
ATOM   6411  C C   . GLY B 1 273 ? 37.674  20.305  -43.161 1.00 80.67  ? 273 GLY B C   1 
ATOM   6412  O O   . GLY B 1 273 ? 38.030  20.477  -44.325 1.00 78.04  ? 273 GLY B O   1 
ATOM   6413  N N   . TRP B 1 274 ? 37.652  19.117  -42.564 1.00 81.73  ? 274 TRP B N   1 
ATOM   6414  C CA  . TRP B 1 274 ? 38.087  17.919  -43.264 1.00 81.77  ? 274 TRP B CA  1 
ATOM   6415  C C   . TRP B 1 274 ? 37.177  17.647  -44.464 1.00 82.57  ? 274 TRP B C   1 
ATOM   6416  O O   . TRP B 1 274 ? 37.609  16.936  -45.375 1.00 82.95  ? 274 TRP B O   1 
ATOM   6417  C CB  . TRP B 1 274 ? 38.116  16.696  -42.334 1.00 83.20  ? 274 TRP B CB  1 
ATOM   6418  C CG  . TRP B 1 274 ? 39.051  16.770  -41.156 1.00 82.35  ? 274 TRP B CG  1 
ATOM   6419  C CD1 . TRP B 1 274 ? 39.657  17.869  -40.636 1.00 80.71  ? 274 TRP B CD1 1 
ATOM   6420  C CD2 . TRP B 1 274 ? 39.444  15.667  -40.311 1.00 83.98  ? 274 TRP B CD2 1 
ATOM   6421  N NE1 . TRP B 1 274 ? 40.408  17.537  -39.542 1.00 81.18  ? 274 TRP B NE1 1 
ATOM   6422  C CE2 . TRP B 1 274 ? 40.299  16.194  -39.316 1.00 83.10  ? 274 TRP B CE2 1 
ATOM   6423  C CE3 . TRP B 1 274 ? 39.162  14.294  -40.301 1.00 86.06  ? 274 TRP B CE3 1 
ATOM   6424  C CZ2 . TRP B 1 274 ? 40.874  15.402  -38.327 1.00 84.16  ? 274 TRP B CZ2 1 
ATOM   6425  C CZ3 . TRP B 1 274 ? 39.734  13.512  -39.322 1.00 87.27  ? 274 TRP B CZ3 1 
ATOM   6426  C CH2 . TRP B 1 274 ? 40.570  14.062  -38.345 1.00 86.26  ? 274 TRP B CH2 1 
ATOM   6427  N N   . TRP B 1 275 ? 35.938  18.195  -44.446 1.00 82.91  ? 275 TRP B N   1 
ATOM   6428  C CA  . TRP B 1 275 ? 34.948  17.953  -45.485 1.00 83.42  ? 275 TRP B CA  1 
ATOM   6429  C C   . TRP B 1 275 ? 35.339  18.590  -46.819 1.00 81.56  ? 275 TRP B C   1 
ATOM   6430  O O   . TRP B 1 275 ? 34.841  18.187  -47.867 1.00 81.31  ? 275 TRP B O   1 
ATOM   6431  C CB  . TRP B 1 275 ? 33.577  18.463  -45.025 1.00 84.92  ? 275 TRP B CB  1 
ATOM   6432  C CG  . TRP B 1 275 ? 33.455  19.962  -44.953 1.00 83.72  ? 275 TRP B CG  1 
ATOM   6433  C CD1 . TRP B 1 275 ? 33.666  20.739  -43.854 1.00 83.63  ? 275 TRP B CD1 1 
ATOM   6434  C CD2 . TRP B 1 275 ? 33.100  20.866  -46.021 1.00 82.64  ? 275 TRP B CD2 1 
ATOM   6435  N NE1 . TRP B 1 275 ? 33.479  22.060  -44.161 1.00 82.38  ? 275 TRP B NE1 1 
ATOM   6436  C CE2 . TRP B 1 275 ? 33.138  22.171  -45.483 1.00 81.98  ? 275 TRP B CE2 1 
ATOM   6437  C CE3 . TRP B 1 275 ? 32.770  20.705  -47.370 1.00 82.68  ? 275 TRP B CE3 1 
ATOM   6438  C CZ2 . TRP B 1 275 ? 32.856  23.305  -46.248 1.00 81.14  ? 275 TRP B CZ2 1 
ATOM   6439  C CZ3 . TRP B 1 275 ? 32.487  21.822  -48.125 1.00 82.00  ? 275 TRP B CZ3 1 
ATOM   6440  C CH2 . TRP B 1 275 ? 32.542  23.106  -47.574 1.00 81.24  ? 275 TRP B CH2 1 
ATOM   6441  N N   . LYS B 1 276 ? 36.248  19.572  -46.776 1.00 80.42  ? 276 LYS B N   1 
ATOM   6442  C CA  . LYS B 1 276 ? 36.426  20.530  -47.862 1.00 79.53  ? 276 LYS B CA  1 
ATOM   6443  C C   . LYS B 1 276 ? 37.141  19.896  -49.055 1.00 79.44  ? 276 LYS B C   1 
ATOM   6444  O O   . LYS B 1 276 ? 37.056  20.388  -50.169 1.00 78.61  ? 276 LYS B O   1 
ATOM   6445  C CB  . LYS B 1 276 ? 37.179  21.778  -47.378 1.00 77.83  ? 276 LYS B CB  1 
ATOM   6446  C CG  . LYS B 1 276 ? 36.489  22.609  -46.286 1.00 77.85  ? 276 LYS B CG  1 
ATOM   6447  C CD  . LYS B 1 276 ? 37.291  23.794  -45.738 1.00 76.33  ? 276 LYS B CD  1 
ATOM   6448  C CE  . LYS B 1 276 ? 37.641  24.809  -46.769 1.00 74.98  ? 276 LYS B CE  1 
ATOM   6449  N NZ  . LYS B 1 276 ? 36.418  25.259  -47.450 1.00 75.61  ? 276 LYS B NZ  1 
ATOM   6450  N N   . GLY B 1 277 ? 37.850  18.799  -48.825 1.00 81.21  ? 277 GLY B N   1 
ATOM   6451  C CA  . GLY B 1 277 ? 38.495  18.070  -49.909 1.00 81.97  ? 277 GLY B CA  1 
ATOM   6452  C C   . GLY B 1 277 ? 37.819  16.727  -50.185 1.00 83.82  ? 277 GLY B C   1 
ATOM   6453  O O   . GLY B 1 277 ? 38.486  15.771  -50.553 1.00 83.83  ? 277 GLY B O   1 
ATOM   6454  N N   . GLY B 1 278 ? 36.533  16.625  -49.861 1.00 85.65  ? 278 GLY B N   1 
ATOM   6455  C CA  . GLY B 1 278 ? 35.858  15.320  -49.960 1.00 89.23  ? 278 GLY B CA  1 
ATOM   6456  C C   . GLY B 1 278 ? 36.021  14.583  -48.649 1.00 90.37  ? 278 GLY B C   1 
ATOM   6457  O O   . GLY B 1 278 ? 37.016  14.859  -47.958 1.00 90.93  ? 278 GLY B O   1 
ATOM   6458  N N   . GLU B 1 279 ? 35.060  13.744  -48.284 1.00 91.12  ? 279 GLU B N   1 
ATOM   6459  C CA  . GLU B 1 279 ? 35.170  12.901  -47.068 1.00 93.09  ? 279 GLU B CA  1 
ATOM   6460  C C   . GLU B 1 279 ? 35.349  13.729  -45.792 1.00 92.13  ? 279 GLU B C   1 
ATOM   6461  O O   . GLU B 1 279 ? 36.492  14.024  -45.422 1.00 91.30  ? 279 GLU B O   1 
ATOM   6462  C CB  . GLU B 1 279 ? 36.290  11.870  -47.211 1.00 93.74  ? 279 GLU B CB  1 
ATOM   6463  C CG  . GLU B 1 279 ? 36.130  10.690  -46.257 1.00 96.84  ? 279 GLU B CG  1 
ATOM   6464  C CD  . GLU B 1 279 ? 34.691  10.265  -46.033 1.00 99.77  ? 279 GLU B CD  1 
ATOM   6465  O OE1 . GLU B 1 279 ? 34.143  10.556  -44.951 1.00 100.38 ? 279 GLU B OE1 1 
ATOM   6466  O OE2 . GLU B 1 279 ? 34.117  9.642   -46.949 1.00 101.65 ? 279 GLU B OE2 1 
ATOM   6467  N N   . LYS B 1 280 ? 34.251  14.007  -45.102 1.00 93.26  ? 280 LYS B N   1 
ATOM   6468  C CA  . LYS B 1 280 ? 34.364  14.704  -43.806 1.00 93.09  ? 280 LYS B CA  1 
ATOM   6469  C C   . LYS B 1 280 ? 35.033  13.790  -42.798 1.00 94.47  ? 280 LYS B C   1 
ATOM   6470  O O   . LYS B 1 280 ? 35.432  14.296  -41.736 1.00 94.27  ? 280 LYS B O   1 
ATOM   6471  C CB  . LYS B 1 280 ? 33.057  14.847  -43.034 1.00 94.80  ? 280 LYS B CB  1 
ATOM   6472  C CG  . LYS B 1 280 ? 31.786  15.097  -43.805 1.00 97.60  ? 280 LYS B CG  1 
ATOM   6473  C CD  . LYS B 1 280 ? 30.663  14.100  -43.543 1.00 99.04  ? 280 LYS B CD  1 
ATOM   6474  C CE  . LYS B 1 280 ? 31.157  12.705  -43.341 1.00 101.21 ? 280 LYS B CE  1 
ATOM   6475  N NZ  . LYS B 1 280 ? 31.424  12.025  -44.610 1.00 100.97 ? 280 LYS B NZ  1 
ATOM   6476  N N   . SER B 1 281 ? 35.065  12.485  -43.067 1.00 96.28  ? 281 SER B N   1 
ATOM   6477  C CA  . SER B 1 281 ? 35.624  11.629  -42.026 1.00 98.07  ? 281 SER B CA  1 
ATOM   6478  C C   . SER B 1 281 ? 37.082  11.237  -42.308 1.00 98.41  ? 281 SER B C   1 
ATOM   6479  O O   . SER B 1 281 ? 37.654  10.391  -41.611 1.00 100.16 ? 281 SER B O   1 
ATOM   6480  C CB  . SER B 1 281 ? 34.785  10.415  -41.839 1.00 100.91 ? 281 SER B CB  1 
ATOM   6481  O OG  . SER B 1 281 ? 33.414  10.769  -41.755 1.00 102.10 ? 281 SER B OG  1 
ATOM   6482  N N   . ASP B 1 282 ? 37.699  11.850  -43.328 1.00 96.53  ? 282 ASP B N   1 
ATOM   6483  C CA  . ASP B 1 282 ? 39.123  11.679  -43.559 1.00 94.87  ? 282 ASP B CA  1 
ATOM   6484  C C   . ASP B 1 282 ? 39.746  13.066  -43.622 1.00 89.90  ? 282 ASP B C   1 
ATOM   6485  O O   . ASP B 1 282 ? 39.169  13.981  -44.204 1.00 88.19  ? 282 ASP B O   1 
ATOM   6486  C CB  . ASP B 1 282 ? 39.425  10.792  -44.764 1.00 96.67  ? 282 ASP B CB  1 
ATOM   6487  C CG  . ASP B 1 282 ? 40.907  10.537  -45.018 1.00 96.67  ? 282 ASP B CG  1 
ATOM   6488  O OD1 . ASP B 1 282 ? 41.569  9.972   -44.123 1.00 98.08  ? 282 ASP B OD1 1 
ATOM   6489  O OD2 . ASP B 1 282 ? 41.401  10.926  -46.098 1.00 95.96  ? 282 ASP B OD2 1 
ATOM   6490  N N   . HIS B 1 283 ? 40.900  13.188  -42.958 1.00 87.79  ? 283 HIS B N   1 
ATOM   6491  C CA  . HIS B 1 283 ? 41.807  14.321  -43.084 1.00 84.16  ? 283 HIS B CA  1 
ATOM   6492  C C   . HIS B 1 283 ? 42.819  13.952  -44.159 1.00 82.36  ? 283 HIS B C   1 
ATOM   6493  O O   . HIS B 1 283 ? 43.756  13.218  -43.887 1.00 83.14  ? 283 HIS B O   1 
ATOM   6494  C CB  . HIS B 1 283 ? 42.500  14.569  -41.738 1.00 83.72  ? 283 HIS B CB  1 
ATOM   6495  C CG  . HIS B 1 283 ? 42.929  15.957  -41.424 1.00 81.58  ? 283 HIS B CG  1 
ATOM   6496  N ND1 . HIS B 1 283 ? 42.577  17.092  -42.122 1.00 80.17  ? 283 HIS B ND1 1 
ATOM   6497  C CD2 . HIS B 1 283 ? 43.713  16.365  -40.407 1.00 81.07  ? 283 HIS B CD2 1 
ATOM   6498  C CE1 . HIS B 1 283 ? 43.118  18.146  -41.522 1.00 78.78  ? 283 HIS B CE1 1 
ATOM   6499  N NE2 . HIS B 1 283 ? 43.823  17.723  -40.487 1.00 79.30  ? 283 HIS B NE2 1 
ATOM   6500  N N   . SER B 1 284 ? 42.582  14.418  -45.381 1.00 80.71  ? 284 SER B N   1 
ATOM   6501  C CA  . SER B 1 284 ? 43.431  14.128  -46.522 1.00 80.09  ? 284 SER B CA  1 
ATOM   6502  C C   . SER B 1 284 ? 44.814  14.795  -46.375 1.00 79.30  ? 284 SER B C   1 
ATOM   6503  O O   . SER B 1 284 ? 44.972  15.972  -46.064 1.00 77.69  ? 284 SER B O   1 
ATOM   6504  C CB  . SER B 1 284 ? 42.688  14.546  -47.760 1.00 79.13  ? 284 SER B CB  1 
ATOM   6505  O OG  . SER B 1 284 ? 43.316  14.155  -48.966 1.00 78.77  ? 284 SER B OG  1 
ATOM   6506  N N   . LEU B 1 285 ? 45.872  14.021  -46.585 1.00 80.87  ? 285 LEU B N   1 
ATOM   6507  C CA  . LEU B 1 285 ? 47.217  14.532  -46.422 1.00 80.21  ? 285 LEU B CA  1 
ATOM   6508  C C   . LEU B 1 285 ? 47.530  15.515  -47.541 1.00 78.96  ? 285 LEU B C   1 
ATOM   6509  O O   . LEU B 1 285 ? 48.470  16.307  -47.408 1.00 77.57  ? 285 LEU B O   1 
ATOM   6510  C CB  . LEU B 1 285 ? 48.224  13.382  -46.448 1.00 82.27  ? 285 LEU B CB  1 
ATOM   6511  C CG  . LEU B 1 285 ? 48.090  12.299  -45.370 1.00 85.16  ? 285 LEU B CG  1 
ATOM   6512  C CD1 . LEU B 1 285 ? 49.233  11.312  -45.520 1.00 86.35  ? 285 LEU B CD1 1 
ATOM   6513  C CD2 . LEU B 1 285 ? 48.068  12.865  -43.960 1.00 85.14  ? 285 LEU B CD2 1 
ATOM   6514  N N   . ASN B 1 286 ? 46.783  15.433  -48.653 1.00 79.75  ? 286 ASN B N   1 
ATOM   6515  C CA  . ASN B 1 286 ? 47.167  16.175  -49.844 1.00 79.75  ? 286 ASN B CA  1 
ATOM   6516  C C   . ASN B 1 286 ? 46.017  17.020  -50.389 1.00 80.38  ? 286 ASN B C   1 
ATOM   6517  O O   . ASN B 1 286 ? 45.947  17.259  -51.594 1.00 80.48  ? 286 ASN B O   1 
ATOM   6518  C CB  . ASN B 1 286 ? 47.684  15.234  -50.918 1.00 80.53  ? 286 ASN B CB  1 
ATOM   6519  C CG  . ASN B 1 286 ? 46.542  14.470  -51.518 1.00 81.53  ? 286 ASN B CG  1 
ATOM   6520  O OD1 . ASN B 1 286 ? 45.796  13.828  -50.779 1.00 82.67  ? 286 ASN B OD1 1 
ATOM   6521  N ND2 . ASN B 1 286 ? 46.360  14.583  -52.823 1.00 81.71  ? 286 ASN B ND2 1 
ATOM   6522  N N   . GLN B 1 287 ? 45.151  17.499  -49.492 1.00 81.08  ? 287 GLN B N   1 
ATOM   6523  C CA  . GLN B 1 287 ? 44.060  18.369  -49.873 1.00 82.12  ? 287 GLN B CA  1 
ATOM   6524  C C   . GLN B 1 287 ? 44.213  19.685  -49.115 1.00 82.28  ? 287 GLN B C   1 
ATOM   6525  O O   . GLN B 1 287 ? 43.644  19.843  -48.031 1.00 85.25  ? 287 GLN B O   1 
ATOM   6526  C CB  . GLN B 1 287 ? 42.705  17.718  -49.580 1.00 85.29  ? 287 GLN B CB  1 
ATOM   6527  C CG  . GLN B 1 287 ? 42.279  16.639  -50.575 1.00 86.65  ? 287 GLN B CG  1 
ATOM   6528  C CD  . GLN B 1 287 ? 41.857  17.204  -51.914 1.00 86.65  ? 287 GLN B CD  1 
ATOM   6529  O OE1 . GLN B 1 287 ? 41.856  18.424  -52.139 1.00 85.78  ? 287 GLN B OE1 1 
ATOM   6530  N NE2 . GLN B 1 287 ? 41.505  16.313  -52.829 1.00 87.48  ? 287 GLN B NE2 1 
ATOM   6531  N N   . PRO B 1 288 ? 44.948  20.676  -49.684 1.00 79.56  ? 288 PRO B N   1 
ATOM   6532  C CA  . PRO B 1 288 ? 45.097  22.002  -49.071 1.00 76.93  ? 288 PRO B CA  1 
ATOM   6533  C C   . PRO B 1 288 ? 43.917  22.556  -48.271 1.00 76.26  ? 288 PRO B C   1 
ATOM   6534  O O   . PRO B 1 288 ? 44.122  23.221  -47.257 1.00 74.77  ? 288 PRO B O   1 
ATOM   6535  C CB  . PRO B 1 288 ? 45.344  22.856  -50.321 1.00 76.28  ? 288 PRO B CB  1 
ATOM   6536  C CG  . PRO B 1 288 ? 46.124  21.967  -51.262 1.00 76.63  ? 288 PRO B CG  1 
ATOM   6537  C CD  . PRO B 1 288 ? 45.633  20.568  -50.987 1.00 78.36  ? 288 PRO B CD  1 
ATOM   6538  N N   . GLU B 1 289 ? 42.684  22.272  -48.730 1.00 76.85  ? 289 GLU B N   1 
ATOM   6539  C CA  . GLU B 1 289 ? 41.482  22.928  -48.212 1.00 76.81  ? 289 GLU B CA  1 
ATOM   6540  C C   . GLU B 1 289 ? 41.209  22.470  -46.775 1.00 76.36  ? 289 GLU B C   1 
ATOM   6541  O O   . GLU B 1 289 ? 40.527  23.165  -45.997 1.00 74.67  ? 289 GLU B O   1 
ATOM   6542  C CB  . GLU B 1 289 ? 40.265  22.686  -49.118 1.00 77.81  ? 289 GLU B CB  1 
ATOM   6543  C CG  . GLU B 1 289 ? 40.364  23.324  -50.504 1.00 77.18  ? 289 GLU B CG  1 
ATOM   6544  C CD  . GLU B 1 289 ? 40.410  24.842  -50.507 1.00 76.61  ? 289 GLU B CD  1 
ATOM   6545  O OE1 . GLU B 1 289 ? 39.490  25.412  -49.898 1.00 79.75  ? 289 GLU B OE1 1 
ATOM   6546  O OE2 . GLU B 1 289 ? 41.312  25.470  -51.090 1.00 75.80  ? 289 GLU B OE2 1 
ATOM   6547  N N   . GLU B 1 290 ? 41.776  21.298  -46.443 1.00 76.17  ? 290 GLU B N   1 
ATOM   6548  C CA  . GLU B 1 290 ? 41.489  20.643  -45.179 1.00 77.13  ? 290 GLU B CA  1 
ATOM   6549  C C   . GLU B 1 290 ? 42.469  21.086  -44.093 1.00 76.34  ? 290 GLU B C   1 
ATOM   6550  O O   . GLU B 1 290 ? 42.386  20.558  -42.983 1.00 76.87  ? 290 GLU B O   1 
ATOM   6551  C CB  . GLU B 1 290 ? 41.514  19.126  -45.353 1.00 78.29  ? 290 GLU B CB  1 
ATOM   6552  C CG  . GLU B 1 290 ? 40.442  18.606  -46.309 1.00 79.45  ? 290 GLU B CG  1 
ATOM   6553  C CD  . GLU B 1 290 ? 40.330  17.084  -46.378 1.00 81.19  ? 290 GLU B CD  1 
ATOM   6554  O OE1 . GLU B 1 290 ? 41.116  16.425  -45.643 1.00 81.57  ? 290 GLU B OE1 1 
ATOM   6555  O OE2 . GLU B 1 290 ? 39.465  16.553  -47.131 1.00 81.65  ? 290 GLU B OE2 1 
ATOM   6556  N N   . TRP B 1 291 ? 43.358  22.055  -44.403 1.00 74.58  ? 291 TRP B N   1 
ATOM   6557  C CA  . TRP B 1 291 ? 44.432  22.451  -43.498 1.00 74.25  ? 291 TRP B CA  1 
ATOM   6558  C C   . TRP B 1 291 ? 44.616  23.969  -43.454 1.00 73.72  ? 291 TRP B C   1 
ATOM   6559  O O   . TRP B 1 291 ? 45.749  24.458  -43.493 1.00 73.78  ? 291 TRP B O   1 
ATOM   6560  C CB  . TRP B 1 291 ? 45.758  21.800  -43.925 1.00 73.48  ? 291 TRP B CB  1 
ATOM   6561  C CG  . TRP B 1 291 ? 45.705  20.302  -43.952 1.00 74.44  ? 291 TRP B CG  1 
ATOM   6562  C CD1 . TRP B 1 291 ? 45.239  19.507  -44.955 1.00 74.80  ? 291 TRP B CD1 1 
ATOM   6563  C CD2 . TRP B 1 291 ? 46.119  19.425  -42.889 1.00 75.54  ? 291 TRP B CD2 1 
ATOM   6564  N NE1 . TRP B 1 291 ? 45.335  18.191  -44.593 1.00 76.31  ? 291 TRP B NE1 1 
ATOM   6565  C CE2 . TRP B 1 291 ? 45.863  18.108  -43.332 1.00 76.76  ? 291 TRP B CE2 1 
ATOM   6566  C CE3 . TRP B 1 291 ? 46.667  19.629  -41.616 1.00 75.76  ? 291 TRP B CE3 1 
ATOM   6567  C CZ2 . TRP B 1 291 ? 46.144  16.996  -42.544 1.00 78.41  ? 291 TRP B CZ2 1 
ATOM   6568  C CZ3 . TRP B 1 291 ? 46.941  18.529  -40.836 1.00 77.45  ? 291 TRP B CZ3 1 
ATOM   6569  C CH2 . TRP B 1 291 ? 46.675  17.232  -41.296 1.00 78.84  ? 291 TRP B CH2 1 
ATOM   6570  N N   . PHE B 1 292 ? 43.523  24.722  -43.350 1.00 73.78  ? 292 PHE B N   1 
ATOM   6571  C CA  . PHE B 1 292 ? 43.616  26.172  -43.330 1.00 73.15  ? 292 PHE B CA  1 
ATOM   6572  C C   . PHE B 1 292 ? 43.214  26.682  -41.951 1.00 74.32  ? 292 PHE B C   1 
ATOM   6573  O O   . PHE B 1 292 ? 42.809  27.837  -41.790 1.00 74.80  ? 292 PHE B O   1 
ATOM   6574  C CB  . PHE B 1 292 ? 42.680  26.776  -44.372 1.00 73.08  ? 292 PHE B CB  1 
ATOM   6575  C CG  . PHE B 1 292 ? 43.216  27.118  -45.750 1.00 72.60  ? 292 PHE B CG  1 
ATOM   6576  C CD1 . PHE B 1 292 ? 44.041  28.219  -45.935 1.00 72.47  ? 292 PHE B CD1 1 
ATOM   6577  C CD2 . PHE B 1 292 ? 42.754  26.449  -46.876 1.00 73.18  ? 292 PHE B CD2 1 
ATOM   6578  C CE1 . PHE B 1 292 ? 44.457  28.591  -47.207 1.00 72.25  ? 292 PHE B CE1 1 
ATOM   6579  C CE2 . PHE B 1 292 ? 43.165  26.825  -48.143 1.00 73.36  ? 292 PHE B CE2 1 
ATOM   6580  C CZ  . PHE B 1 292 ? 44.020  27.893  -48.308 1.00 72.58  ? 292 PHE B CZ  1 
ATOM   6581  N N   . GLY B 1 293 ? 43.255  25.792  -40.959 1.00 75.29  ? 293 GLY B N   1 
ATOM   6582  C CA  . GLY B 1 293 ? 42.766  26.150  -39.639 1.00 76.34  ? 293 GLY B CA  1 
ATOM   6583  C C   . GLY B 1 293 ? 43.813  26.956  -38.887 1.00 75.50  ? 293 GLY B C   1 
ATOM   6584  O O   . GLY B 1 293 ? 44.995  26.840  -39.157 1.00 74.50  ? 293 GLY B O   1 
ATOM   6585  N N   . PHE B 1 294 ? 43.362  27.819  -37.989 1.00 76.41  ? 294 PHE B N   1 
ATOM   6586  C CA  . PHE B 1 294 ? 44.212  28.248  -36.899 1.00 76.99  ? 294 PHE B CA  1 
ATOM   6587  C C   . PHE B 1 294 ? 44.219  27.132  -35.861 1.00 78.11  ? 294 PHE B C   1 
ATOM   6588  O O   . PHE B 1 294 ? 45.186  26.976  -35.126 1.00 78.39  ? 294 PHE B O   1 
ATOM   6589  C CB  . PHE B 1 294 ? 43.736  29.615  -36.390 1.00 78.00  ? 294 PHE B CB  1 
ATOM   6590  C CG  . PHE B 1 294 ? 44.099  30.823  -37.252 1.00 76.93  ? 294 PHE B CG  1 
ATOM   6591  C CD1 . PHE B 1 294 ? 44.546  30.673  -38.561 1.00 75.20  ? 294 PHE B CD1 1 
ATOM   6592  C CD2 . PHE B 1 294 ? 43.937  32.122  -36.753 1.00 78.07  ? 294 PHE B CD2 1 
ATOM   6593  C CE1 . PHE B 1 294 ? 44.850  31.782  -39.330 1.00 74.95  ? 294 PHE B CE1 1 
ATOM   6594  C CE2 . PHE B 1 294 ? 44.225  33.231  -37.527 1.00 76.97  ? 294 PHE B CE2 1 
ATOM   6595  C CZ  . PHE B 1 294 ? 44.684  33.059  -38.812 1.00 76.06  ? 294 PHE B CZ  1 
ATOM   6596  N N   . TRP B 1 295 ? 43.125  26.362  -35.832 1.00 80.01  ? 295 TRP B N   1 
ATOM   6597  C CA  . TRP B 1 295 ? 42.906  25.272  -34.894 1.00 81.99  ? 295 TRP B CA  1 
ATOM   6598  C C   . TRP B 1 295 ? 42.903  23.958  -35.679 1.00 82.31  ? 295 TRP B C   1 
ATOM   6599  O O   . TRP B 1 295 ? 42.318  23.871  -36.759 1.00 82.84  ? 295 TRP B O   1 
ATOM   6600  C CB  . TRP B 1 295 ? 41.584  25.491  -34.130 1.00 83.99  ? 295 TRP B CB  1 
ATOM   6601  C CG  . TRP B 1 295 ? 41.650  26.524  -33.027 1.00 85.44  ? 295 TRP B CG  1 
ATOM   6602  C CD1 . TRP B 1 295 ? 41.852  27.872  -33.166 1.00 85.24  ? 295 TRP B CD1 1 
ATOM   6603  C CD2 . TRP B 1 295 ? 41.496  26.294  -31.605 1.00 87.60  ? 295 TRP B CD2 1 
ATOM   6604  N NE1 . TRP B 1 295 ? 41.852  28.493  -31.943 1.00 86.39  ? 295 TRP B NE1 1 
ATOM   6605  C CE2 . TRP B 1 295 ? 41.641  27.551  -30.968 1.00 88.00  ? 295 TRP B CE2 1 
ATOM   6606  C CE3 . TRP B 1 295 ? 41.246  25.160  -30.818 1.00 89.47  ? 295 TRP B CE3 1 
ATOM   6607  C CZ2 . TRP B 1 295 ? 41.558  27.694  -29.583 1.00 89.75  ? 295 TRP B CZ2 1 
ATOM   6608  C CZ3 . TRP B 1 295 ? 41.162  25.305  -29.449 1.00 91.26  ? 295 TRP B CZ3 1 
ATOM   6609  C CH2 . TRP B 1 295 ? 41.330  26.553  -28.843 1.00 91.51  ? 295 TRP B CH2 1 
ATOM   6610  N N   . GLY B 1 296 ? 43.517  22.927  -35.109 1.00 82.03  ? 296 GLY B N   1 
ATOM   6611  C CA  . GLY B 1 296 ? 43.498  21.630  -35.798 1.00 81.72  ? 296 GLY B CA  1 
ATOM   6612  C C   . GLY B 1 296 ? 42.978  20.531  -34.911 1.00 83.40  ? 296 GLY B C   1 
ATOM   6613  O O   . GLY B 1 296 ? 43.002  20.702  -33.679 1.00 84.45  ? 296 GLY B O   1 
ATOM   6614  N N   . TYR B 1 297 ? 42.560  19.425  -35.524 1.00 83.33  ? 297 TYR B N   1 
ATOM   6615  C CA  . TYR B 1 297 ? 41.984  18.301  -34.745 1.00 85.28  ? 297 TYR B CA  1 
ATOM   6616  C C   . TYR B 1 297 ? 42.967  17.145  -34.710 1.00 85.79  ? 297 TYR B C   1 
ATOM   6617  O O   . TYR B 1 297 ? 43.678  16.919  -35.708 1.00 83.88  ? 297 TYR B O   1 
ATOM   6618  C CB  . TYR B 1 297 ? 40.625  17.971  -35.367 1.00 85.90  ? 297 TYR B CB  1 
ATOM   6619  C CG  . TYR B 1 297 ? 39.625  19.110  -35.222 1.00 85.49  ? 297 TYR B CG  1 
ATOM   6620  C CD1 . TYR B 1 297 ? 39.091  19.440  -33.983 1.00 86.57  ? 297 TYR B CD1 1 
ATOM   6621  C CD2 . TYR B 1 297 ? 39.238  19.872  -36.317 1.00 83.86  ? 297 TYR B CD2 1 
ATOM   6622  C CE1 . TYR B 1 297 ? 38.189  20.479  -33.841 1.00 86.05  ? 297 TYR B CE1 1 
ATOM   6623  C CE2 . TYR B 1 297 ? 38.337  20.914  -36.187 1.00 83.61  ? 297 TYR B CE2 1 
ATOM   6624  C CZ  . TYR B 1 297 ? 37.812  21.219  -34.945 1.00 84.66  ? 297 TYR B CZ  1 
ATOM   6625  O OH  . TYR B 1 297 ? 36.930  22.249  -34.811 1.00 84.14  ? 297 TYR B OH  1 
ATOM   6626  N N   . SER B 1 298 ? 43.005  16.434  -33.584 1.00 88.36  ? 298 SER B N   1 
ATOM   6627  C CA  . SER B 1 298 ? 43.918  15.277  -33.417 1.00 89.48  ? 298 SER B CA  1 
ATOM   6628  C C   . SER B 1 298 ? 43.386  14.046  -34.149 1.00 90.89  ? 298 SER B C   1 
ATOM   6629  O O   . SER B 1 298 ? 44.209  13.315  -34.725 1.00 90.92  ? 298 SER B O   1 
ATOM   6630  C CB  . SER B 1 298 ? 44.080  14.971  -31.964 1.00 91.56  ? 298 SER B CB  1 
ATOM   6631  O OG  . SER B 1 298 ? 44.281  13.581  -31.764 1.00 93.98  ? 298 SER B OG  1 
ATOM   6632  N N   . ASP B 1 299 ? 42.066  13.848  -34.156 1.00 92.24  ? 299 ASP B N   1 
ATOM   6633  C CA  . ASP B 1 299 ? 41.510  12.624  -34.710 1.00 93.50  ? 299 ASP B CA  1 
ATOM   6634  C C   . ASP B 1 299 ? 40.046  12.874  -35.070 1.00 94.37  ? 299 ASP B C   1 
ATOM   6635  O O   . ASP B 1 299 ? 39.546  13.997  -34.953 1.00 93.38  ? 299 ASP B O   1 
ATOM   6636  C CB  . ASP B 1 299 ? 41.680  11.474  -33.733 1.00 95.86  ? 299 ASP B CB  1 
ATOM   6637  C CG  . ASP B 1 299 ? 41.253  11.743  -32.295 1.00 97.33  ? 299 ASP B CG  1 
ATOM   6638  O OD1 . ASP B 1 299 ? 40.036  11.825  -32.028 1.00 98.33  ? 299 ASP B OD1 1 
ATOM   6639  O OD2 . ASP B 1 299 ? 42.148  11.862  -31.438 1.00 97.62  ? 299 ASP B OD2 1 
ATOM   6640  N N   . LEU B 1 300 ? 39.352  11.814  -35.500 1.00 96.30  ? 300 LEU B N   1 
ATOM   6641  C CA  . LEU B 1 300 ? 37.949  11.918  -35.885 1.00 97.02  ? 300 LEU B CA  1 
ATOM   6642  C C   . LEU B 1 300 ? 37.063  12.282  -34.689 1.00 98.66  ? 300 LEU B C   1 
ATOM   6643  O O   . LEU B 1 300 ? 36.042  12.939  -34.867 1.00 98.00  ? 300 LEU B O   1 
ATOM   6644  C CB  . LEU B 1 300 ? 37.515  10.609  -36.546 1.00 98.66  ? 300 LEU B CB  1 
ATOM   6645  C CG  . LEU B 1 300 ? 36.126  10.577  -37.195 1.00 99.29  ? 300 LEU B CG  1 
ATOM   6646  C CD1 . LEU B 1 300 ? 35.625  11.894  -37.779 1.00 96.91  ? 300 LEU B CD1 1 
ATOM   6647  C CD2 . LEU B 1 300 ? 36.170  9.519   -38.286 1.00 100.11 ? 300 LEU B CD2 1 
ATOM   6648  N N   . ASN B 1 301 ? 37.467  11.877  -33.478 1.00 100.62 ? 301 ASN B N   1 
ATOM   6649  C CA  . ASN B 1 301 ? 36.691  12.123  -32.271 1.00 102.73 ? 301 ASN B CA  1 
ATOM   6650  C C   . ASN B 1 301 ? 36.901  13.553  -31.754 1.00 100.69 ? 301 ASN B C   1 
ATOM   6651  O O   . ASN B 1 301 ? 36.006  14.100  -31.117 1.00 102.44 ? 301 ASN B O   1 
ATOM   6652  C CB  . ASN B 1 301 ? 36.986  11.067  -31.206 1.00 106.06 ? 301 ASN B CB  1 
ATOM   6653  C CG  . ASN B 1 301 ? 36.696  9.658   -31.678 1.00 109.06 ? 301 ASN B CG  1 
ATOM   6654  O OD1 . ASN B 1 301 ? 36.256  9.449   -32.814 1.00 109.68 ? 301 ASN B OD1 1 
ATOM   6655  N ND2 . ASN B 1 301 ? 36.920  8.670   -30.824 1.00 111.68 ? 301 ASN B ND2 1 
ATOM   6656  N N   . ASP B 1 302 ? 38.060  14.178  -32.018 1.00 97.45  ? 302 ASP B N   1 
ATOM   6657  C CA  . ASP B 1 302 ? 38.360  15.495  -31.466 1.00 95.51  ? 302 ASP B CA  1 
ATOM   6658  C C   . ASP B 1 302 ? 37.288  16.492  -31.899 1.00 94.26  ? 302 ASP B C   1 
ATOM   6659  O O   . ASP B 1 302 ? 37.197  16.831  -33.074 1.00 92.27  ? 302 ASP B O   1 
ATOM   6660  C CB  . ASP B 1 302 ? 39.740  15.992  -31.884 1.00 93.09  ? 302 ASP B CB  1 
ATOM   6661  C CG  . ASP B 1 302 ? 40.256  17.289  -31.259 1.00 91.60  ? 302 ASP B CG  1 
ATOM   6662  O OD1 . ASP B 1 302 ? 39.505  17.958  -30.531 1.00 92.18  ? 302 ASP B OD1 1 
ATOM   6663  O OD2 . ASP B 1 302 ? 41.440  17.620  -31.480 1.00 89.97  ? 302 ASP B OD2 1 
ATOM   6664  N N   . LYS B 1 303 ? 36.512  16.987  -30.933 1.00 95.32  ? 303 LYS B N   1 
ATOM   6665  C CA  . LYS B 1 303 ? 35.411  17.882  -31.236 1.00 95.42  ? 303 LYS B CA  1 
ATOM   6666  C C   . LYS B 1 303 ? 35.790  19.339  -30.986 1.00 93.67  ? 303 LYS B C   1 
ATOM   6667  O O   . LYS B 1 303 ? 34.962  20.203  -31.227 1.00 93.02  ? 303 LYS B O   1 
ATOM   6668  C CB  . LYS B 1 303 ? 34.199  17.526  -30.365 1.00 98.56  ? 303 LYS B CB  1 
ATOM   6669  C CG  . LYS B 1 303 ? 33.545  16.163  -30.612 1.00 100.70 ? 303 LYS B CG  1 
ATOM   6670  C CD  . LYS B 1 303 ? 32.883  16.060  -31.981 1.00 99.89  ? 303 LYS B CD  1 
ATOM   6671  C CE  . LYS B 1 303 ? 31.626  15.252  -32.018 1.00 102.25 ? 303 LYS B CE  1 
ATOM   6672  N NZ  . LYS B 1 303 ? 30.868  15.673  -33.198 1.00 101.21 ? 303 LYS B NZ  1 
ATOM   6673  N N   . TYR B 1 304 ? 37.034  19.599  -30.544 1.00 93.27  ? 304 TYR B N   1 
ATOM   6674  C CA  . TYR B 1 304 ? 37.441  20.886  -29.978 1.00 92.71  ? 304 TYR B CA  1 
ATOM   6675  C C   . TYR B 1 304 ? 38.704  21.428  -30.663 1.00 89.93  ? 304 TYR B C   1 
ATOM   6676  O O   . TYR B 1 304 ? 38.690  22.514  -31.240 1.00 88.95  ? 304 TYR B O   1 
ATOM   6677  C CB  . TYR B 1 304 ? 37.650  20.729  -28.462 1.00 94.91  ? 304 TYR B CB  1 
ATOM   6678  C CG  . TYR B 1 304 ? 36.396  20.387  -27.655 1.00 97.87  ? 304 TYR B CG  1 
ATOM   6679  C CD1 . TYR B 1 304 ? 35.504  21.382  -27.276 1.00 98.24  ? 304 TYR B CD1 1 
ATOM   6680  C CD2 . TYR B 1 304 ? 36.123  19.084  -27.234 1.00 99.83  ? 304 TYR B CD2 1 
ATOM   6681  C CE1 . TYR B 1 304 ? 34.372  21.089  -26.536 1.00 101.01 ? 304 TYR B CE1 1 
ATOM   6682  C CE2 . TYR B 1 304 ? 35.001  18.785  -26.477 1.00 102.34 ? 304 TYR B CE2 1 
ATOM   6683  C CZ  . TYR B 1 304 ? 34.108  19.789  -26.140 1.00 103.01 ? 304 TYR B CZ  1 
ATOM   6684  O OH  . TYR B 1 304 ? 32.959  19.556  -25.420 1.00 105.35 ? 304 TYR B OH  1 
ATOM   6685  N N   . GLY B 1 305 ? 39.819  20.695  -30.564 1.00 89.40  ? 305 GLY B N   1 
ATOM   6686  C CA  . GLY B 1 305 ? 41.056  21.073  -31.238 1.00 86.75  ? 305 GLY B CA  1 
ATOM   6687  C C   . GLY B 1 305 ? 42.057  21.737  -30.297 1.00 86.09  ? 305 GLY B C   1 
ATOM   6688  O O   . GLY B 1 305 ? 41.810  21.868  -29.099 1.00 87.33  ? 305 GLY B O   1 
ATOM   6689  N N   . THR B 1 306 ? 43.215  22.111  -30.855 1.00 83.99  ? 306 THR B N   1 
ATOM   6690  C CA  . THR B 1 306 ? 44.119  23.038  -30.195 1.00 83.51  ? 306 THR B CA  1 
ATOM   6691  C C   . THR B 1 306 ? 44.568  24.092  -31.206 1.00 81.16  ? 306 THR B C   1 
ATOM   6692  O O   . THR B 1 306 ? 44.536  23.848  -32.412 1.00 79.24  ? 306 THR B O   1 
ATOM   6693  C CB  . THR B 1 306 ? 45.315  22.314  -29.574 1.00 84.50  ? 306 THR B CB  1 
ATOM   6694  O OG1 . THR B 1 306 ? 46.037  21.664  -30.615 1.00 83.72  ? 306 THR B OG1 1 
ATOM   6695  C CG2 . THR B 1 306 ? 44.916  21.262  -28.557 1.00 87.03  ? 306 THR B CG2 1 
ATOM   6696  N N   . PRO B 1 307 ? 44.953  25.310  -30.739 1.00 81.36  ? 307 PRO B N   1 
ATOM   6697  C CA  . PRO B 1 307 ? 45.570  26.330  -31.596 1.00 79.53  ? 307 PRO B CA  1 
ATOM   6698  C C   . PRO B 1 307 ? 46.962  25.991  -32.124 1.00 78.69  ? 307 PRO B C   1 
ATOM   6699  O O   . PRO B 1 307 ? 47.838  25.570  -31.362 1.00 79.47  ? 307 PRO B O   1 
ATOM   6700  C CB  . PRO B 1 307 ? 45.611  27.571  -30.669 1.00 80.01  ? 307 PRO B CB  1 
ATOM   6701  C CG  . PRO B 1 307 ? 45.668  27.014  -29.267 1.00 81.80  ? 307 PRO B CG  1 
ATOM   6702  C CD  . PRO B 1 307 ? 44.770  25.793  -29.355 1.00 82.97  ? 307 PRO B CD  1 
ATOM   6703  N N   . ARG B 1 308 ? 47.151  26.197  -33.438 1.00 77.44  ? 308 ARG B N   1 
ATOM   6704  C CA  . ARG B 1 308 ? 48.463  26.146  -34.069 1.00 76.17  ? 308 ARG B CA  1 
ATOM   6705  C C   . ARG B 1 308 ? 49.202  27.451  -33.789 1.00 76.50  ? 308 ARG B C   1 
ATOM   6706  O O   . ARG B 1 308 ? 48.604  28.454  -33.406 1.00 77.73  ? 308 ARG B O   1 
ATOM   6707  C CB  . ARG B 1 308 ? 48.310  25.979  -35.585 1.00 74.57  ? 308 ARG B CB  1 
ATOM   6708  C CG  . ARG B 1 308 ? 47.849  24.590  -36.000 1.00 75.08  ? 308 ARG B CG  1 
ATOM   6709  C CD  . ARG B 1 308 ? 47.511  24.548  -37.480 1.00 73.86  ? 308 ARG B CD  1 
ATOM   6710  N NE  . ARG B 1 308 ? 46.968  23.245  -37.879 1.00 74.28  ? 308 ARG B NE  1 
ATOM   6711  C CZ  . ARG B 1 308 ? 45.986  22.995  -38.754 1.00 73.94  ? 308 ARG B CZ  1 
ATOM   6712  N NH1 . ARG B 1 308 ? 45.378  23.955  -39.423 1.00 72.73  ? 308 ARG B NH1 1 
ATOM   6713  N NH2 . ARG B 1 308 ? 45.644  21.741  -38.992 1.00 74.81  ? 308 ARG B NH2 1 
ATOM   6714  N N   . PRO B 1 309 ? 50.527  27.538  -34.006 1.00 76.16  ? 309 PRO B N   1 
ATOM   6715  C CA  . PRO B 1 309 ? 51.241  28.762  -33.662 1.00 75.99  ? 309 PRO B CA  1 
ATOM   6716  C C   . PRO B 1 309 ? 50.632  30.044  -34.219 1.00 75.56  ? 309 PRO B C   1 
ATOM   6717  O O   . PRO B 1 309 ? 50.720  31.069  -33.550 1.00 76.98  ? 309 PRO B O   1 
ATOM   6718  C CB  . PRO B 1 309 ? 52.632  28.456  -34.208 1.00 74.92  ? 309 PRO B CB  1 
ATOM   6719  C CG  . PRO B 1 309 ? 52.723  26.974  -34.003 1.00 75.41  ? 309 PRO B CG  1 
ATOM   6720  C CD  . PRO B 1 309 ? 51.410  26.490  -34.540 1.00 75.39  ? 309 PRO B CD  1 
ATOM   6721  N N   . VAL B 1 310 ? 49.983  29.983  -35.394 1.00 74.60  ? 310 VAL B N   1 
ATOM   6722  C CA  . VAL B 1 310 ? 49.463  31.190  -36.041 1.00 74.17  ? 310 VAL B CA  1 
ATOM   6723  C C   . VAL B 1 310 ? 48.528  31.968  -35.103 1.00 76.01  ? 310 VAL B C   1 
ATOM   6724  O O   . VAL B 1 310 ? 48.468  33.206  -35.163 1.00 75.36  ? 310 VAL B O   1 
ATOM   6725  C CB  . VAL B 1 310 ? 48.774  30.896  -37.391 1.00 72.61  ? 310 VAL B CB  1 
ATOM   6726  C CG1 . VAL B 1 310 ? 47.525  30.060  -37.209 1.00 73.27  ? 310 VAL B CG1 1 
ATOM   6727  C CG2 . VAL B 1 310 ? 48.433  32.173  -38.154 1.00 72.05  ? 310 VAL B CG2 1 
ATOM   6728  N N   . TRP B 1 311 ? 47.787  31.233  -34.257 1.00 78.18  ? 311 TRP B N   1 
ATOM   6729  C CA  . TRP B 1 311 ? 46.825  31.816  -33.332 1.00 80.74  ? 311 TRP B CA  1 
ATOM   6730  C C   . TRP B 1 311 ? 47.477  32.863  -32.428 1.00 82.27  ? 311 TRP B C   1 
ATOM   6731  O O   . TRP B 1 311 ? 46.972  33.977  -32.306 1.00 83.13  ? 311 TRP B O   1 
ATOM   6732  C CB  . TRP B 1 311 ? 46.182  30.696  -32.508 1.00 81.78  ? 311 TRP B CB  1 
ATOM   6733  C CG  . TRP B 1 311 ? 45.118  31.100  -31.518 1.00 83.45  ? 311 TRP B CG  1 
ATOM   6734  C CD1 . TRP B 1 311 ? 45.205  31.062  -30.158 1.00 85.16  ? 311 TRP B CD1 1 
ATOM   6735  C CD2 . TRP B 1 311 ? 43.764  31.489  -31.812 1.00 84.26  ? 311 TRP B CD2 1 
ATOM   6736  N NE1 . TRP B 1 311 ? 44.021  31.440  -29.584 1.00 86.33  ? 311 TRP B NE1 1 
ATOM   6737  C CE2 . TRP B 1 311 ? 43.116  31.690  -30.575 1.00 86.12  ? 311 TRP B CE2 1 
ATOM   6738  C CE3 . TRP B 1 311 ? 43.042  31.679  -32.993 1.00 84.10  ? 311 TRP B CE3 1 
ATOM   6739  C CZ2 . TRP B 1 311 ? 41.781  32.066  -30.492 1.00 88.06  ? 311 TRP B CZ2 1 
ATOM   6740  C CZ3 . TRP B 1 311 ? 41.714  32.033  -32.910 1.00 85.66  ? 311 TRP B CZ3 1 
ATOM   6741  C CH2 . TRP B 1 311 ? 41.091  32.213  -31.675 1.00 87.63  ? 311 TRP B CH2 1 
ATOM   6742  N N   . PHE B 1 312 ? 48.584  32.480  -31.786 1.00 83.14  ? 312 PHE B N   1 
ATOM   6743  C CA  . PHE B 1 312 ? 49.205  33.291  -30.746 1.00 85.11  ? 312 PHE B CA  1 
ATOM   6744  C C   . PHE B 1 312 ? 49.793  34.553  -31.378 1.00 83.03  ? 312 PHE B C   1 
ATOM   6745  O O   . PHE B 1 312 ? 49.676  35.650  -30.836 1.00 82.51  ? 312 PHE B O   1 
ATOM   6746  C CB  . PHE B 1 312 ? 50.170  32.384  -29.962 1.00 87.04  ? 312 PHE B CB  1 
ATOM   6747  C CG  . PHE B 1 312 ? 49.417  31.329  -29.153 1.00 90.75  ? 312 PHE B CG  1 
ATOM   6748  C CD1 . PHE B 1 312 ? 48.919  31.611  -27.876 1.00 93.98  ? 312 PHE B CD1 1 
ATOM   6749  C CD2 . PHE B 1 312 ? 49.132  30.082  -29.697 1.00 91.01  ? 312 PHE B CD2 1 
ATOM   6750  C CE1 . PHE B 1 312 ? 48.189  30.667  -27.157 1.00 95.31  ? 312 PHE B CE1 1 
ATOM   6751  C CE2 . PHE B 1 312 ? 48.418  29.139  -28.968 1.00 93.56  ? 312 PHE B CE2 1 
ATOM   6752  C CZ  . PHE B 1 312 ? 47.934  29.435  -27.705 1.00 95.26  ? 312 PHE B CZ  1 
ATOM   6753  N N   . ALA B 1 313 ? 50.413  34.375  -32.546 1.00 81.26  ? 313 ALA B N   1 
ATOM   6754  C CA  . ALA B 1 313 ? 50.957  35.482  -33.307 1.00 80.09  ? 313 ALA B CA  1 
ATOM   6755  C C   . ALA B 1 313 ? 49.845  36.486  -33.605 1.00 80.48  ? 313 ALA B C   1 
ATOM   6756  O O   . ALA B 1 313 ? 49.955  37.660  -33.274 1.00 81.91  ? 313 ALA B O   1 
ATOM   6757  C CB  . ALA B 1 313 ? 51.603  34.957  -34.568 1.00 77.70  ? 313 ALA B CB  1 
ATOM   6758  N N   . MET B 1 314 ? 48.764  36.023  -34.224 1.00 79.98  ? 314 MET B N   1 
ATOM   6759  C CA  . MET B 1 314 ? 47.682  36.928  -34.581 1.00 81.53  ? 314 MET B CA  1 
ATOM   6760  C C   . MET B 1 314 ? 47.183  37.698  -33.356 1.00 82.95  ? 314 MET B C   1 
ATOM   6761  O O   . MET B 1 314 ? 46.848  38.871  -33.463 1.00 82.81  ? 314 MET B O   1 
ATOM   6762  C CB  . MET B 1 314 ? 46.513  36.150  -35.193 1.00 81.61  ? 314 MET B CB  1 
ATOM   6763  C CG  . MET B 1 314 ? 46.809  35.653  -36.588 1.00 80.03  ? 314 MET B CG  1 
ATOM   6764  S SD  . MET B 1 314 ? 46.708  36.998  -37.778 1.00 77.81  ? 314 MET B SD  1 
ATOM   6765  C CE  . MET B 1 314 ? 44.937  37.302  -37.687 1.00 80.38  ? 314 MET B CE  1 
ATOM   6766  N N   . ARG B 1 315 ? 47.122  37.011  -32.209 1.00 84.61  ? 315 ARG B N   1 
ATOM   6767  C CA  . ARG B 1 315 ? 46.567  37.568  -30.993 1.00 87.10  ? 315 ARG B CA  1 
ATOM   6768  C C   . ARG B 1 315 ? 47.460  38.717  -30.562 1.00 88.81  ? 315 ARG B C   1 
ATOM   6769  O O   . ARG B 1 315 ? 46.986  39.844  -30.418 1.00 93.61  ? 315 ARG B O   1 
ATOM   6770  C CB  . ARG B 1 315 ? 46.432  36.561  -29.846 1.00 88.27  ? 315 ARG B CB  1 
ATOM   6771  C CG  . ARG B 1 315 ? 45.832  37.175  -28.587 1.00 90.91  ? 315 ARG B CG  1 
ATOM   6772  C CD  . ARG B 1 315 ? 45.970  36.314  -27.354 1.00 92.37  ? 315 ARG B CD  1 
ATOM   6773  N NE  . ARG B 1 315 ? 47.393  36.137  -27.046 1.00 92.68  ? 315 ARG B NE  1 
ATOM   6774  C CZ  . ARG B 1 315 ? 47.872  35.227  -26.218 1.00 93.22  ? 315 ARG B CZ  1 
ATOM   6775  N NH1 . ARG B 1 315 ? 47.051  34.495  -25.483 1.00 94.74  ? 315 ARG B NH1 1 
ATOM   6776  N NH2 . ARG B 1 315 ? 49.176  35.058  -26.125 1.00 92.69  ? 315 ARG B NH2 1 
ATOM   6777  N N   . ASP B 1 316 ? 48.747  38.426  -30.390 1.00 88.12  ? 316 ASP B N   1 
ATOM   6778  C CA  . ASP B 1 316 ? 49.706  39.460  -30.040 1.00 89.01  ? 316 ASP B CA  1 
ATOM   6779  C C   . ASP B 1 316 ? 49.664  40.577  -31.074 1.00 87.93  ? 316 ASP B C   1 
ATOM   6780  O O   . ASP B 1 316 ? 49.593  41.736  -30.687 1.00 90.61  ? 316 ASP B O   1 
ATOM   6781  C CB  . ASP B 1 316 ? 51.096  38.891  -29.833 1.00 89.42  ? 316 ASP B CB  1 
ATOM   6782  C CG  . ASP B 1 316 ? 51.165  37.859  -28.719 1.00 91.40  ? 316 ASP B CG  1 
ATOM   6783  O OD1 . ASP B 1 316 ? 50.114  37.655  -28.052 1.00 94.00  ? 316 ASP B OD1 1 
ATOM   6784  O OD2 . ASP B 1 316 ? 52.247  37.256  -28.548 1.00 90.78  ? 316 ASP B OD2 1 
ATOM   6785  N N   . TYR B 1 317 ? 49.638  40.238  -32.367 1.00 85.40  ? 317 TYR B N   1 
ATOM   6786  C CA  . TYR B 1 317 ? 49.716  41.249  -33.410 1.00 85.72  ? 317 TYR B CA  1 
ATOM   6787  C C   . TYR B 1 317 ? 48.544  42.223  -33.317 1.00 88.31  ? 317 TYR B C   1 
ATOM   6788  O O   . TYR B 1 317 ? 48.730  43.437  -33.480 1.00 90.09  ? 317 TYR B O   1 
ATOM   6789  C CB  . TYR B 1 317 ? 49.729  40.679  -34.828 1.00 84.21  ? 317 TYR B CB  1 
ATOM   6790  C CG  . TYR B 1 317 ? 49.923  41.727  -35.916 1.00 84.43  ? 317 TYR B CG  1 
ATOM   6791  C CD1 . TYR B 1 317 ? 51.197  42.117  -36.322 1.00 85.10  ? 317 TYR B CD1 1 
ATOM   6792  C CD2 . TYR B 1 317 ? 48.839  42.314  -36.550 1.00 84.40  ? 317 TYR B CD2 1 
ATOM   6793  C CE1 . TYR B 1 317 ? 51.385  43.073  -37.310 1.00 85.49  ? 317 TYR B CE1 1 
ATOM   6794  C CE2 . TYR B 1 317 ? 49.013  43.266  -37.540 1.00 85.59  ? 317 TYR B CE2 1 
ATOM   6795  C CZ  . TYR B 1 317 ? 50.287  43.649  -37.922 1.00 85.88  ? 317 TYR B CZ  1 
ATOM   6796  O OH  . TYR B 1 317 ? 50.451  44.590  -38.900 1.00 87.39  ? 317 TYR B OH  1 
ATOM   6797  N N   . MET B 1 318 ? 47.342  41.685  -33.045 1.00 89.27  ? 318 MET B N   1 
ATOM   6798  C CA  . MET B 1 318 ? 46.096  42.430  -33.202 1.00 89.58  ? 318 MET B CA  1 
ATOM   6799  C C   . MET B 1 318 ? 45.910  43.473  -32.105 1.00 91.55  ? 318 MET B C   1 
ATOM   6800  O O   . MET B 1 318 ? 45.032  44.311  -32.236 1.00 94.38  ? 318 MET B O   1 
ATOM   6801  C CB  . MET B 1 318 ? 44.884  41.488  -33.216 1.00 88.91  ? 318 MET B CB  1 
ATOM   6802  C CG  . MET B 1 318 ? 44.583  40.882  -34.578 1.00 86.90  ? 318 MET B CG  1 
ATOM   6803  S SD  . MET B 1 318 ? 43.019  39.984  -34.647 1.00 86.86  ? 318 MET B SD  1 
ATOM   6804  C CE  . MET B 1 318 ? 43.244  39.022  -33.145 1.00 87.07  ? 318 MET B CE  1 
ATOM   6805  N N   . LYS B 1 319 ? 46.698  43.382  -31.036 1.00 92.60  ? 319 LYS B N   1 
ATOM   6806  C CA  . LYS B 1 319 ? 46.498  44.268  -29.863 1.00 95.53  ? 319 LYS B CA  1 
ATOM   6807  C C   . LYS B 1 319 ? 47.106  45.660  -30.082 1.00 96.14  ? 319 LYS B C   1 
ATOM   6808  O O   . LYS B 1 319 ? 47.489  46.287  -29.089 1.00 97.90  ? 319 LYS B O   1 
ATOM   6809  C CB  . LYS B 1 319 ? 47.136  43.550  -28.671 1.00 96.85  ? 319 LYS B CB  1 
ATOM   6810  C CG  . LYS B 1 319 ? 46.470  42.234  -28.322 1.00 97.02  ? 319 LYS B CG  1 
ATOM   6811  C CD  . LYS B 1 319 ? 46.826  41.724  -26.933 1.00 98.37  ? 319 LYS B CD  1 
ATOM   6812  C CE  . LYS B 1 319 ? 47.489  42.765  -26.098 1.00 101.02 ? 319 LYS B CE  1 
ATOM   6813  N NZ  . LYS B 1 319 ? 47.428  42.403  -24.681 1.00 102.49 ? 319 LYS B NZ  1 
ATOM   6814  N N   . GLY B 1 320 ? 47.174  46.127  -31.323 1.00 94.43  ? 320 GLY B N   1 
ATOM   6815  C CA  . GLY B 1 320 ? 47.795  47.428  -31.615 1.00 95.55  ? 320 GLY B CA  1 
ATOM   6816  C C   . GLY B 1 320 ? 48.018  47.535  -33.099 1.00 94.62  ? 320 GLY B C   1 
ATOM   6817  O O   . GLY B 1 320 ? 49.025  46.994  -33.573 1.00 94.98  ? 320 GLY B O   1 
ATOM   6818  N N   . LEU B 1 321 ? 47.139  48.227  -33.816 1.00 94.33  ? 321 LEU B N   1 
ATOM   6819  C CA  . LEU B 1 321 ? 47.252  48.206  -35.292 1.00 93.25  ? 321 LEU B CA  1 
ATOM   6820  C C   . LEU B 1 321 ? 47.684  49.547  -35.882 1.00 95.62  ? 321 LEU B C   1 
ATOM   6821  O O   . LEU B 1 321 ? 47.084  50.564  -35.520 1.00 99.09  ? 321 LEU B O   1 
ATOM   6822  C CB  . LEU B 1 321 ? 45.887  47.796  -35.841 1.00 92.79  ? 321 LEU B CB  1 
ATOM   6823  C CG  . LEU B 1 321 ? 45.628  46.299  -36.031 1.00 91.15  ? 321 LEU B CG  1 
ATOM   6824  C CD1 . LEU B 1 321 ? 46.877  45.470  -35.825 1.00 89.32  ? 321 LEU B CD1 1 
ATOM   6825  C CD2 . LEU B 1 321 ? 44.522  45.845  -35.102 1.00 92.13  ? 321 LEU B CD2 1 
ATOM   6826  N N   . ILE B 1 322 ? 48.716  49.550  -36.719 1.00 94.96  ? 322 ILE B N   1 
ATOM   6827  C CA  . ILE B 1 322 ? 49.068  50.742  -37.471 1.00 96.21  ? 322 ILE B CA  1 
ATOM   6828  C C   . ILE B 1 322 ? 48.271  50.706  -38.777 1.00 95.30  ? 322 ILE B C   1 
ATOM   6829  O O   . ILE B 1 322 ? 48.360  49.705  -39.497 1.00 94.18  ? 322 ILE B O   1 
ATOM   6830  C CB  . ILE B 1 322 ? 50.589  50.807  -37.726 1.00 96.40  ? 322 ILE B CB  1 
ATOM   6831  C CG1 . ILE B 1 322 ? 51.380  50.863  -36.413 1.00 97.96  ? 322 ILE B CG1 1 
ATOM   6832  C CG2 . ILE B 1 322 ? 50.963  51.974  -38.650 1.00 97.58  ? 322 ILE B CG2 1 
ATOM   6833  C CD1 . ILE B 1 322 ? 51.817  49.520  -35.870 1.00 96.09  ? 322 ILE B CD1 1 
ATOM   6834  N N   . ILE B 1 323 ? 47.501  51.782  -39.052 1.00 95.41  ? 323 ILE B N   1 
ATOM   6835  C CA  . ILE B 1 323 ? 46.825  52.015  -40.328 1.00 94.21  ? 323 ILE B CA  1 
ATOM   6836  C C   . ILE B 1 323 ? 47.647  52.996  -41.173 1.00 93.65  ? 323 ILE B C   1 
ATOM   6837  O O   . ILE B 1 323 ? 47.676  52.894  -42.401 1.00 91.23  ? 323 ILE B O   1 
ATOM   6838  C CB  . ILE B 1 323 ? 45.378  52.529  -40.121 1.00 96.84  ? 323 ILE B CB  1 
ATOM   6839  C CG1 . ILE B 1 323 ? 44.491  51.497  -39.427 1.00 97.11  ? 323 ILE B CG1 1 
ATOM   6840  C CG2 . ILE B 1 323 ? 44.730  52.979  -41.435 1.00 96.60  ? 323 ILE B CG2 1 
ATOM   6841  C CD1 . ILE B 1 323 ? 44.785  51.310  -37.950 1.00 98.86  ? 323 ILE B CD1 1 
ATOM   6842  N N   . SER B 1 324 ? 48.275  53.972  -40.499 1.00 95.44  ? 324 SER B N   1 
ATOM   6843  C CA  . SER B 1 324 ? 49.077  55.012  -41.134 1.00 96.75  ? 324 SER B CA  1 
ATOM   6844  C C   . SER B 1 324 ? 50.171  55.452  -40.163 1.00 97.72  ? 324 SER B C   1 
ATOM   6845  O O   . SER B 1 324 ? 49.869  55.770  -39.011 1.00 99.45  ? 324 SER B O   1 
ATOM   6846  C CB  . SER B 1 324 ? 48.250  56.224  -41.535 1.00 99.26  ? 324 SER B CB  1 
ATOM   6847  O OG  . SER B 1 324 ? 47.209  55.893  -42.442 1.00 98.27  ? 324 SER B OG  1 
ATOM   6848  N N   . PRO B 1 325 ? 51.452  55.567  -40.595 1.00 96.38  ? 325 PRO B N   1 
ATOM   6849  C CA  . PRO B 1 325 ? 51.828  55.441  -42.002 1.00 94.22  ? 325 PRO B CA  1 
ATOM   6850  C C   . PRO B 1 325 ? 51.804  53.984  -42.419 1.00 90.45  ? 325 PRO B C   1 
ATOM   6851  O O   . PRO B 1 325 ? 51.818  53.095  -41.571 1.00 88.63  ? 325 PRO B O   1 
ATOM   6852  C CB  . PRO B 1 325 ? 53.225  56.022  -42.073 1.00 95.23  ? 325 PRO B CB  1 
ATOM   6853  C CG  . PRO B 1 325 ? 53.776  55.776  -40.691 1.00 95.86  ? 325 PRO B CG  1 
ATOM   6854  C CD  . PRO B 1 325 ? 52.607  55.845  -39.730 1.00 96.90  ? 325 PRO B CD  1 
ATOM   6855  N N   . LYS B 1 326 ? 51.728  53.798  -43.738 1.00 89.21  ? 326 LYS B N   1 
ATOM   6856  C CA  . LYS B 1 326 ? 51.684  52.487  -44.351 1.00 86.50  ? 326 LYS B CA  1 
ATOM   6857  C C   . LYS B 1 326 ? 53.125  52.093  -44.679 1.00 86.41  ? 326 LYS B C   1 
ATOM   6858  O O   . LYS B 1 326 ? 53.926  52.943  -45.094 1.00 87.27  ? 326 LYS B O   1 
ATOM   6859  C CB  . LYS B 1 326 ? 50.731  52.516  -45.556 1.00 85.65  ? 326 LYS B CB  1 
ATOM   6860  C CG  . LYS B 1 326 ? 49.234  52.654  -45.225 1.00 86.02  ? 326 LYS B CG  1 
ATOM   6861  C CD  . LYS B 1 326 ? 48.308  52.918  -46.413 1.00 85.99  ? 326 LYS B CD  1 
ATOM   6862  C CE  . LYS B 1 326 ? 46.833  52.972  -46.092 1.00 86.57  ? 326 LYS B CE  1 
ATOM   6863  N NZ  . LYS B 1 326 ? 46.460  53.806  -44.946 1.00 88.36  ? 326 LYS B NZ  1 
ATOM   6864  N N   . ASN B 1 327 ? 53.445  50.811  -44.430 1.00 84.58  ? 327 ASN B N   1 
ATOM   6865  C CA  . ASN B 1 327 ? 54.724  50.244  -44.794 1.00 84.24  ? 327 ASN B CA  1 
ATOM   6866  C C   . ASN B 1 327 ? 54.837  50.296  -46.316 1.00 84.94  ? 327 ASN B C   1 
ATOM   6867  O O   . ASN B 1 327 ? 53.899  49.893  -47.008 1.00 83.22  ? 327 ASN B O   1 
ATOM   6868  C CB  . ASN B 1 327 ? 54.895  48.859  -44.178 1.00 82.77  ? 327 ASN B CB  1 
ATOM   6869  C CG  . ASN B 1 327 ? 56.147  48.120  -44.626 1.00 81.96  ? 327 ASN B CG  1 
ATOM   6870  O OD1 . ASN B 1 327 ? 57.268  48.650  -44.594 1.00 83.51  ? 327 ASN B OD1 1 
ATOM   6871  N ND2 . ASN B 1 327 ? 55.992  46.868  -45.027 1.00 79.45  ? 327 ASN B ND2 1 
ATOM   6872  N N   . LYS B 1 328 ? 55.991  50.826  -46.783 1.00 87.11  ? 328 LYS B N   1 
ATOM   6873  C CA  . LYS B 1 328 ? 56.340  51.020  -48.188 1.00 88.10  ? 328 LYS B CA  1 
ATOM   6874  C C   . LYS B 1 328 ? 55.506  52.141  -48.819 1.00 89.38  ? 328 LYS B C   1 
ATOM   6875  O O   . LYS B 1 328 ? 55.144  52.072  -49.999 1.00 89.13  ? 328 LYS B O   1 
ATOM   6876  C CB  . LYS B 1 328 ? 56.238  49.686  -48.931 1.00 87.75  ? 328 LYS B CB  1 
ATOM   6877  C CG  . LYS B 1 328 ? 57.064  48.541  -48.320 1.00 88.39  ? 328 LYS B CG  1 
ATOM   6878  C CD  . LYS B 1 328 ? 58.547  48.881  -48.188 1.00 91.64  ? 328 LYS B CD  1 
ATOM   6879  C CE  . LYS B 1 328 ? 59.439  47.700  -48.085 1.00 91.39  ? 328 LYS B CE  1 
ATOM   6880  N NZ  . LYS B 1 328 ? 59.134  46.983  -46.851 1.00 92.65  ? 328 LYS B NZ  1 
ATOM   6881  N N   . SER B 1 329 ? 55.195  53.162  -48.007 1.00 90.23  ? 329 SER B N   1 
ATOM   6882  C CA  . SER B 1 329 ? 54.685  54.436  -48.488 1.00 91.94  ? 329 SER B CA  1 
ATOM   6883  C C   . SER B 1 329 ? 55.851  55.386  -48.777 1.00 94.46  ? 329 SER B C   1 
ATOM   6884  O O   . SER B 1 329 ? 57.009  55.133  -48.412 1.00 93.66  ? 329 SER B O   1 
ATOM   6885  C CB  . SER B 1 329 ? 53.712  55.042  -47.510 1.00 92.28  ? 329 SER B CB  1 
ATOM   6886  O OG  . SER B 1 329 ? 54.246  55.044  -46.193 1.00 92.10  ? 329 SER B OG  1 
ATOM   6887  N N   . ILE B 1 330 ? 55.509  56.471  -49.477 1.00 95.91  ? 330 ILE B N   1 
ATOM   6888  C CA  . ILE B 1 330 ? 56.459  57.457  -49.940 1.00 97.71  ? 330 ILE B CA  1 
ATOM   6889  C C   . ILE B 1 330 ? 55.956  58.813  -49.468 1.00 101.13 ? 330 ILE B C   1 
ATOM   6890  O O   . ILE B 1 330 ? 54.837  59.228  -49.777 1.00 101.40 ? 330 ILE B O   1 
ATOM   6891  C CB  . ILE B 1 330 ? 56.606  57.364  -51.468 1.00 97.68  ? 330 ILE B CB  1 
ATOM   6892  C CG1 . ILE B 1 330 ? 57.376  56.112  -51.855 1.00 95.97  ? 330 ILE B CG1 1 
ATOM   6893  C CG2 . ILE B 1 330 ? 57.271  58.610  -52.039 1.00 101.10 ? 330 ILE B CG2 1 
ATOM   6894  C CD1 . ILE B 1 330 ? 57.508  55.901  -53.351 1.00 96.13  ? 330 ILE B CD1 1 
ATOM   6895  N N   . HIS B 1 331 ? 56.789  59.498  -48.690 1.00 103.82 ? 331 HIS B N   1 
ATOM   6896  C CA  . HIS B 1 331 ? 56.360  60.719  -48.029 1.00 107.45 ? 331 HIS B CA  1 
ATOM   6897  C C   . HIS B 1 331 ? 57.148  61.936  -48.520 1.00 111.11 ? 331 HIS B C   1 
ATOM   6898  O O   . HIS B 1 331 ? 58.242  62.221  -48.032 1.00 112.24 ? 331 HIS B O   1 
ATOM   6899  C CB  . HIS B 1 331 ? 56.412  60.500  -46.515 1.00 107.28 ? 331 HIS B CB  1 
ATOM   6900  C CG  . HIS B 1 331 ? 55.390  59.522  -46.097 1.00 104.97 ? 331 HIS B CG  1 
ATOM   6901  N ND1 . HIS B 1 331 ? 54.336  59.865  -45.285 1.00 106.31 ? 331 HIS B ND1 1 
ATOM   6902  C CD2 . HIS B 1 331 ? 55.187  58.265  -46.462 1.00 103.30 ? 331 HIS B CD2 1 
ATOM   6903  C CE1 . HIS B 1 331 ? 53.543  58.825  -45.135 1.00 104.43 ? 331 HIS B CE1 1 
ATOM   6904  N NE2 . HIS B 1 331 ? 54.044  57.834  -45.834 1.00 102.96 ? 331 HIS B NE2 1 
ATOM   6905  N N   . THR B 1 332 ? 56.554  62.679  -49.463 1.00 113.66 ? 332 THR B N   1 
ATOM   6906  C CA  . THR B 1 332 ? 57.095  63.961  -49.885 1.00 117.98 ? 332 THR B CA  1 
ATOM   6907  C C   . THR B 1 332 ? 56.539  65.044  -48.961 1.00 121.74 ? 332 THR B C   1 
ATOM   6908  O O   . THR B 1 332 ? 55.842  65.944  -49.418 1.00 125.13 ? 332 THR B O   1 
ATOM   6909  C CB  . THR B 1 332 ? 56.755  64.213  -51.357 1.00 118.29 ? 332 THR B CB  1 
ATOM   6910  O OG1 . THR B 1 332 ? 55.336  64.183  -51.407 1.00 117.93 ? 332 THR B OG1 1 
ATOM   6911  C CG2 . THR B 1 332 ? 57.272  63.135  -52.293 1.00 116.22 ? 332 THR B CG2 1 
ATOM   6912  N N   . ASN B 1 333 ? 56.840  64.938  -47.656 1.00 122.65 ? 333 ASN B N   1 
ATOM   6913  C CA  . ASN B 1 333 ? 56.371  65.887  -46.655 1.00 125.96 ? 333 ASN B CA  1 
ATOM   6914  C C   . ASN B 1 333 ? 56.934  65.506  -45.285 1.00 125.06 ? 333 ASN B C   1 
ATOM   6915  O O   . ASN B 1 333 ? 57.115  64.321  -45.008 1.00 122.80 ? 333 ASN B O   1 
ATOM   6916  C CB  . ASN B 1 333 ? 54.847  65.953  -46.603 1.00 127.58 ? 333 ASN B CB  1 
ATOM   6917  C CG  . ASN B 1 333 ? 54.356  67.268  -46.045 1.00 134.57 ? 333 ASN B CG  1 
ATOM   6918  O OD1 . ASN B 1 333 ? 54.493  67.520  -44.842 1.00 139.82 ? 333 ASN B OD1 1 
ATOM   6919  N ND2 . ASN B 1 333 ? 53.790  68.124  -46.886 1.00 137.60 ? 333 ASN B ND2 1 
ATOM   6920  N N   . THR B 1 334 ? 57.173  66.517  -44.434 1.00 127.96 ? 334 THR B N   1 
ATOM   6921  C CA  . THR B 1 334 ? 57.746  66.345  -43.103 1.00 128.76 ? 334 THR B CA  1 
ATOM   6922  C C   . THR B 1 334 ? 56.648  66.164  -42.056 1.00 128.84 ? 334 THR B C   1 
ATOM   6923  O O   . THR B 1 334 ? 56.928  66.155  -40.860 1.00 128.62 ? 334 THR B O   1 
ATOM   6924  C CB  . THR B 1 334 ? 58.641  67.537  -42.746 1.00 133.69 ? 334 THR B CB  1 
ATOM   6925  O OG1 . THR B 1 334 ? 57.946  68.781  -42.874 1.00 136.72 ? 334 THR B OG1 1 
ATOM   6926  C CG2 . THR B 1 334 ? 59.866  67.609  -43.639 1.00 134.69 ? 334 THR B CG2 1 
ATOM   6927  N N   . LYS B 1 335 ? 55.399  66.040  -42.512 1.00 129.84 ? 335 LYS B N   1 
ATOM   6928  C CA  . LYS B 1 335 ? 54.261  65.766  -41.651 1.00 131.47 ? 335 LYS B CA  1 
ATOM   6929  C C   . LYS B 1 335 ? 53.648  64.443  -42.093 1.00 126.13 ? 335 LYS B C   1 
ATOM   6930  O O   . LYS B 1 335 ? 53.106  64.370  -43.192 1.00 126.61 ? 335 LYS B O   1 
ATOM   6931  C CB  . LYS B 1 335 ? 53.235  66.902  -41.772 1.00 138.11 ? 335 LYS B CB  1 
ATOM   6932  C CG  . LYS B 1 335 ? 53.185  67.924  -40.647 1.00 145.02 ? 335 LYS B CG  1 
ATOM   6933  C CD  . LYS B 1 335 ? 54.514  68.577  -40.279 1.00 151.31 ? 335 LYS B CD  1 
ATOM   6934  C CE  . LYS B 1 335 ? 54.571  69.007  -38.844 1.00 156.61 ? 335 LYS B CE  1 
ATOM   6935  N NZ  . LYS B 1 335 ? 54.283  67.872  -37.955 1.00 156.10 ? 335 LYS B NZ  1 
ATOM   6936  N N   . ILE B 1 336 ? 53.737  63.412  -41.240 1.00 121.96 ? 336 ILE B N   1 
ATOM   6937  C CA  . ILE B 1 336 ? 53.295  62.067  -41.592 1.00 117.09 ? 336 ILE B CA  1 
ATOM   6938  C C   . ILE B 1 336 ? 52.000  61.746  -40.844 1.00 115.13 ? 336 ILE B C   1 
ATOM   6939  O O   . ILE B 1 336 ? 52.049  61.612  -39.622 1.00 115.86 ? 336 ILE B O   1 
ATOM   6940  C CB  . ILE B 1 336 ? 54.368  61.018  -41.233 1.00 116.38 ? 336 ILE B CB  1 
ATOM   6941  C CG1 . ILE B 1 336 ? 55.806  61.435  -41.600 1.00 118.30 ? 336 ILE B CG1 1 
ATOM   6942  C CG2 . ILE B 1 336 ? 54.011  59.662  -41.842 1.00 112.61 ? 336 ILE B CG2 1 
ATOM   6943  C CD1 . ILE B 1 336 ? 56.099  61.452  -43.089 1.00 118.20 ? 336 ILE B CD1 1 
ATOM   6944  N N   . PRO B 1 337 ? 50.824  61.585  -41.514 1.00 111.92 ? 337 PRO B N   1 
ATOM   6945  C CA  . PRO B 1 337 ? 49.599  61.161  -40.826 1.00 110.53 ? 337 PRO B CA  1 
ATOM   6946  C C   . PRO B 1 337 ? 49.792  59.849  -40.065 1.00 108.18 ? 337 PRO B C   1 
ATOM   6947  O O   . PRO B 1 337 ? 50.376  58.892  -40.593 1.00 104.47 ? 337 PRO B O   1 
ATOM   6948  C CB  . PRO B 1 337 ? 48.539  61.043  -41.938 1.00 109.19 ? 337 PRO B CB  1 
ATOM   6949  C CG  . PRO B 1 337 ? 49.080  61.875  -43.081 1.00 110.29 ? 337 PRO B CG  1 
ATOM   6950  C CD  . PRO B 1 337 ? 50.593  61.841  -42.946 1.00 110.77 ? 337 PRO B CD  1 
ATOM   6951  N N   . LEU B 1 338 ? 49.307  59.848  -38.814 1.00 109.60 ? 338 LEU B N   1 
ATOM   6952  C CA  . LEU B 1 338 ? 49.365  58.693  -37.937 1.00 108.63 ? 338 LEU B CA  1 
ATOM   6953  C C   . LEU B 1 338 ? 47.940  58.227  -37.630 1.00 109.80 ? 338 LEU B C   1 
ATOM   6954  O O   . LEU B 1 338 ? 47.080  59.051  -37.315 1.00 111.09 ? 338 LEU B O   1 
ATOM   6955  C CB  . LEU B 1 338 ? 50.151  59.036  -36.670 1.00 110.35 ? 338 LEU B CB  1 
ATOM   6956  C CG  . LEU B 1 338 ? 50.276  57.919  -35.623 1.00 109.47 ? 338 LEU B CG  1 
ATOM   6957  C CD1 . LEU B 1 338 ? 51.678  57.773  -35.041 1.00 109.57 ? 338 LEU B CD1 1 
ATOM   6958  C CD2 . LEU B 1 338 ? 49.295  58.164  -34.484 1.00 111.44 ? 338 LEU B CD2 1 
ATOM   6959  N N   . GLU B 1 339 ? 47.716  56.897  -37.722 1.00 109.59 ? 339 GLU B N   1 
ATOM   6960  C CA  . GLU B 1 339 ? 46.410  56.270  -37.512 1.00 109.73 ? 339 GLU B CA  1 
ATOM   6961  C C   . GLU B 1 339 ? 46.567  54.898  -36.851 1.00 106.49 ? 339 GLU B C   1 
ATOM   6962  O O   . GLU B 1 339 ? 47.055  53.970  -37.486 1.00 103.40 ? 339 GLU B O   1 
ATOM   6963  C CB  . GLU B 1 339 ? 45.640  56.116  -38.832 1.00 109.90 ? 339 GLU B CB  1 
ATOM   6964  C CG  . GLU B 1 339 ? 44.969  57.407  -39.309 1.00 113.49 ? 339 GLU B CG  1 
ATOM   6965  C CD  . GLU B 1 339 ? 44.305  57.366  -40.681 1.00 112.89 ? 339 GLU B CD  1 
ATOM   6966  O OE1 . GLU B 1 339 ? 43.516  56.425  -40.983 1.00 108.98 ? 339 GLU B OE1 1 
ATOM   6967  O OE2 . GLU B 1 339 ? 44.598  58.324  -41.446 1.00 114.18 ? 339 GLU B OE2 1 
ATOM   6968  N N   . LEU B 1 340 ? 46.112  54.775  -35.594 1.00 107.99 ? 340 LEU B N   1 
ATOM   6969  C CA  . LEU B 1 340 ? 46.253  53.552  -34.809 1.00 107.47 ? 340 LEU B CA  1 
ATOM   6970  C C   . LEU B 1 340 ? 44.888  53.013  -34.382 1.00 109.02 ? 340 LEU B C   1 
ATOM   6971  O O   . LEU B 1 340 ? 43.906  53.755  -34.340 1.00 112.10 ? 340 LEU B O   1 
ATOM   6972  C CB  . LEU B 1 340 ? 47.093  53.858  -33.572 1.00 108.71 ? 340 LEU B CB  1 
ATOM   6973  C CG  . LEU B 1 340 ? 48.609  53.907  -33.770 1.00 107.75 ? 340 LEU B CG  1 
ATOM   6974  C CD1 . LEU B 1 340 ? 49.020  54.844  -34.887 1.00 108.43 ? 340 LEU B CD1 1 
ATOM   6975  C CD2 . LEU B 1 340 ? 49.260  54.308  -32.465 1.00 109.35 ? 340 LEU B CD2 1 
ATOM   6976  N N   . TYR B 1 341 ? 44.855  51.724  -34.009 1.00 107.93 ? 341 TYR B N   1 
ATOM   6977  C CA  . TYR B 1 341 ? 43.666  51.101  -33.436 1.00 108.45 ? 341 TYR B CA  1 
ATOM   6978  C C   . TYR B 1 341 ? 44.073  50.132  -32.328 1.00 107.20 ? 341 TYR B C   1 
ATOM   6979  O O   . TYR B 1 341 ? 44.493  49.007  -32.594 1.00 104.86 ? 341 TYR B O   1 
ATOM   6980  C CB  . TYR B 1 341 ? 42.805  50.305  -34.421 1.00 107.62 ? 341 TYR B CB  1 
ATOM   6981  C CG  . TYR B 1 341 ? 41.413  49.967  -33.893 1.00 109.37 ? 341 TYR B CG  1 
ATOM   6982  C CD1 . TYR B 1 341 ? 40.401  50.927  -33.904 1.00 110.61 ? 341 TYR B CD1 1 
ATOM   6983  C CD2 . TYR B 1 341 ? 41.107  48.699  -33.396 1.00 106.50 ? 341 TYR B CD2 1 
ATOM   6984  C CE1 . TYR B 1 341 ? 39.134  50.632  -33.435 1.00 112.21 ? 341 TYR B CE1 1 
ATOM   6985  C CE2 . TYR B 1 341 ? 39.844  48.396  -32.916 1.00 107.56 ? 341 TYR B CE2 1 
ATOM   6986  C CZ  . TYR B 1 341 ? 38.855  49.365  -32.943 1.00 111.87 ? 341 TYR B CZ  1 
ATOM   6987  O OH  . TYR B 1 341 ? 37.587  49.096  -32.504 1.00 115.14 ? 341 TYR B OH  1 
ATOM   6988  N N   . ASN B 1 342 ? 43.886  50.576  -31.083 1.00 109.26 ? 342 ASN B N   1 
ATOM   6989  C CA  . ASN B 1 342 ? 44.479  49.933  -29.923 1.00 109.12 ? 342 ASN B CA  1 
ATOM   6990  C C   . ASN B 1 342 ? 43.397  49.193  -29.140 1.00 109.36 ? 342 ASN B C   1 
ATOM   6991  O O   . ASN B 1 342 ? 42.238  49.614  -29.115 1.00 109.64 ? 342 ASN B O   1 
ATOM   6992  C CB  . ASN B 1 342 ? 45.200  50.965  -29.059 1.00 111.22 ? 342 ASN B CB  1 
ATOM   6993  C CG  . ASN B 1 342 ? 46.312  51.676  -29.797 1.00 110.51 ? 342 ASN B CG  1 
ATOM   6994  O OD1 . ASN B 1 342 ? 46.935  51.112  -30.705 1.00 107.90 ? 342 ASN B OD1 1 
ATOM   6995  N ND2 . ASN B 1 342 ? 46.609  52.902  -29.397 1.00 112.56 ? 342 ASN B ND2 1 
ATOM   6996  N N   . ASP B 1 343 ? 43.793  48.087  -28.497 1.00 108.62 ? 343 ASP B N   1 
ATOM   6997  C CA  . ASP B 1 343 ? 42.898  47.373  -27.605 1.00 109.83 ? 343 ASP B CA  1 
ATOM   6998  C C   . ASP B 1 343 ? 43.105  47.951  -26.208 1.00 112.79 ? 343 ASP B C   1 
ATOM   6999  O O   . ASP B 1 343 ? 43.854  48.908  -26.053 1.00 114.70 ? 343 ASP B O   1 
ATOM   7000  C CB  . ASP B 1 343 ? 43.056  45.869  -27.741 1.00 107.61 ? 343 ASP B CB  1 
ATOM   7001  C CG  . ASP B 1 343 ? 43.987  45.218  -26.738 1.00 108.83 ? 343 ASP B CG  1 
ATOM   7002  O OD1 . ASP B 1 343 ? 45.203  45.353  -26.917 1.00 110.22 ? 343 ASP B OD1 1 
ATOM   7003  O OD2 . ASP B 1 343 ? 43.476  44.574  -25.803 1.00 110.70 ? 343 ASP B OD2 1 
ATOM   7004  N N   . LYS B 1 344 ? 42.440  47.373  -25.202 1.00 114.17 ? 344 LYS B N   1 
ATOM   7005  C CA  . LYS B 1 344 ? 42.345  47.996  -23.890 1.00 116.48 ? 344 LYS B CA  1 
ATOM   7006  C C   . LYS B 1 344 ? 43.681  47.983  -23.143 1.00 115.06 ? 344 LYS B C   1 
ATOM   7007  O O   . LYS B 1 344 ? 43.801  48.680  -22.137 1.00 117.88 ? 344 LYS B O   1 
ATOM   7008  C CB  . LYS B 1 344 ? 41.283  47.322  -23.011 1.00 118.49 ? 344 LYS B CB  1 
ATOM   7009  C CG  . LYS B 1 344 ? 41.668  46.002  -22.331 1.00 118.98 ? 344 LYS B CG  1 
ATOM   7010  C CD  . LYS B 1 344 ? 41.050  44.735  -22.929 1.00 118.23 ? 344 LYS B CD  1 
ATOM   7011  C CE  . LYS B 1 344 ? 41.064  43.512  -22.033 1.00 118.97 ? 344 LYS B CE  1 
ATOM   7012  N NZ  . LYS B 1 344 ? 40.866  43.821  -20.611 1.00 122.64 ? 344 LYS B NZ  1 
ATOM   7013  N N   . ASP B 1 345 ? 44.667  47.207  -23.623 1.00 109.69 ? 345 ASP B N   1 
ATOM   7014  C CA  . ASP B 1 345 ? 45.897  46.965  -22.877 1.00 109.24 ? 345 ASP B CA  1 
ATOM   7015  C C   . ASP B 1 345 ? 46.984  47.999  -23.200 1.00 107.15 ? 345 ASP B C   1 
ATOM   7016  O O   . ASP B 1 345 ? 47.891  48.198  -22.393 1.00 107.28 ? 345 ASP B O   1 
ATOM   7017  C CB  . ASP B 1 345 ? 46.401  45.539  -23.093 1.00 107.83 ? 345 ASP B CB  1 
ATOM   7018  C CG  . ASP B 1 345 ? 45.483  44.409  -22.630 1.00 107.73 ? 345 ASP B CG  1 
ATOM   7019  O OD1 . ASP B 1 345 ? 45.151  44.367  -21.432 1.00 110.90 ? 345 ASP B OD1 1 
ATOM   7020  O OD2 . ASP B 1 345 ? 45.108  43.562  -23.465 1.00 104.38 ? 345 ASP B OD2 1 
ATOM   7021  N N   . VAL B 1 346 ? 46.897  48.629  -24.383 1.00 104.56 ? 346 VAL B N   1 
ATOM   7022  C CA  . VAL B 1 346 ? 47.859  49.624  -24.841 1.00 103.88 ? 346 VAL B CA  1 
ATOM   7023  C C   . VAL B 1 346 ? 47.696  50.924  -24.054 1.00 106.79 ? 346 VAL B C   1 
ATOM   7024  O O   . VAL B 1 346 ? 46.685  51.621  -24.190 1.00 108.60 ? 346 VAL B O   1 
ATOM   7025  C CB  . VAL B 1 346 ? 47.678  49.865  -26.352 1.00 101.64 ? 346 VAL B CB  1 
ATOM   7026  C CG1 . VAL B 1 346 ? 48.523  51.030  -26.864 1.00 102.08 ? 346 VAL B CG1 1 
ATOM   7027  C CG2 . VAL B 1 346 ? 47.953  48.598  -27.155 1.00 98.55  ? 346 VAL B CG2 1 
ATOM   7028  N N   . LYS B 1 347 ? 48.704  51.250  -23.238 1.00 107.67 ? 347 LYS B N   1 
ATOM   7029  C CA  . LYS B 1 347 ? 48.688  52.471  -22.448 1.00 111.04 ? 347 LYS B CA  1 
ATOM   7030  C C   . LYS B 1 347 ? 49.629  53.514  -23.051 1.00 111.41 ? 347 LYS B C   1 
ATOM   7031  O O   . LYS B 1 347 ? 49.400  54.713  -22.872 1.00 114.61 ? 347 LYS B O   1 
ATOM   7032  C CB  . LYS B 1 347 ? 48.987  52.194  -20.970 1.00 113.03 ? 347 LYS B CB  1 
ATOM   7033  C CG  . LYS B 1 347 ? 47.905  51.434  -20.222 1.00 114.00 ? 347 LYS B CG  1 
ATOM   7034  C CD  . LYS B 1 347 ? 46.517  52.072  -20.240 1.00 116.28 ? 347 LYS B CD  1 
ATOM   7035  C CE  . LYS B 1 347 ? 45.675  51.802  -21.472 1.00 114.60 ? 347 LYS B CE  1 
ATOM   7036  N NZ  . LYS B 1 347 ? 44.256  52.164  -21.304 1.00 117.07 ? 347 LYS B NZ  1 
ATOM   7037  N N   . LYS B 1 348 ? 50.665  53.078  -23.780 1.00 108.43 ? 348 LYS B N   1 
ATOM   7038  C CA  . LYS B 1 348 ? 51.594  54.027  -24.370 1.00 108.55 ? 348 LYS B CA  1 
ATOM   7039  C C   . LYS B 1 348 ? 52.110  53.517  -25.706 1.00 105.22 ? 348 LYS B C   1 
ATOM   7040  O O   . LYS B 1 348 ? 52.366  52.328  -25.843 1.00 103.48 ? 348 LYS B O   1 
ATOM   7041  C CB  . LYS B 1 348 ? 52.789  54.286  -23.452 1.00 109.87 ? 348 LYS B CB  1 
ATOM   7042  C CG  . LYS B 1 348 ? 53.693  55.405  -23.955 1.00 111.03 ? 348 LYS B CG  1 
ATOM   7043  C CD  . LYS B 1 348 ? 54.799  55.802  -22.986 1.00 113.12 ? 348 LYS B CD  1 
ATOM   7044  C CE  . LYS B 1 348 ? 55.870  54.769  -22.893 1.00 111.12 ? 348 LYS B CE  1 
ATOM   7045  N NZ  . LYS B 1 348 ? 56.647  54.919  -21.665 1.00 113.47 ? 348 LYS B NZ  1 
ATOM   7046  N N   . VAL B 1 349 ? 52.278  54.441  -26.662 1.00 105.27 ? 349 VAL B N   1 
ATOM   7047  C CA  . VAL B 1 349 ? 52.850  54.147  -27.967 1.00 102.73 ? 349 VAL B CA  1 
ATOM   7048  C C   . VAL B 1 349 ? 53.999  55.114  -28.227 1.00 103.99 ? 349 VAL B C   1 
ATOM   7049  O O   . VAL B 1 349 ? 53.856  56.313  -27.977 1.00 107.59 ? 349 VAL B O   1 
ATOM   7050  C CB  . VAL B 1 349 ? 51.820  54.251  -29.105 1.00 101.85 ? 349 VAL B CB  1 
ATOM   7051  C CG1 . VAL B 1 349 ? 52.473  53.986  -30.459 1.00 99.72  ? 349 VAL B CG1 1 
ATOM   7052  C CG2 . VAL B 1 349 ? 50.629  53.325  -28.879 1.00 100.63 ? 349 VAL B CG2 1 
ATOM   7053  N N   . VAL B 1 350 ? 55.115  54.585  -28.751 1.00 101.40 ? 350 VAL B N   1 
ATOM   7054  C CA  . VAL B 1 350 ? 56.335  55.353  -28.946 1.00 101.99 ? 350 VAL B CA  1 
ATOM   7055  C C   . VAL B 1 350 ? 56.911  55.000  -30.307 1.00 99.34  ? 350 VAL B C   1 
ATOM   7056  O O   . VAL B 1 350 ? 56.915  53.832  -30.674 1.00 97.04  ? 350 VAL B O   1 
ATOM   7057  C CB  . VAL B 1 350 ? 57.358  55.036  -27.841 1.00 102.67 ? 350 VAL B CB  1 
ATOM   7058  C CG1 . VAL B 1 350 ? 58.705  55.717  -28.087 1.00 103.79 ? 350 VAL B CG1 1 
ATOM   7059  C CG2 . VAL B 1 350 ? 56.818  55.370  -26.457 1.00 105.14 ? 350 VAL B CG2 1 
ATOM   7060  N N   . VAL B 1 351 ? 57.433  55.991  -31.031 1.00 100.08 ? 351 VAL B N   1 
ATOM   7061  C CA  . VAL B 1 351 ? 58.074  55.722  -32.308 1.00 97.96  ? 351 VAL B CA  1 
ATOM   7062  C C   . VAL B 1 351 ? 59.513  56.225  -32.264 1.00 99.24  ? 351 VAL B C   1 
ATOM   7063  O O   . VAL B 1 351 ? 59.777  57.343  -31.814 1.00 102.13 ? 351 VAL B O   1 
ATOM   7064  C CB  . VAL B 1 351 ? 57.333  56.344  -33.503 1.00 97.91  ? 351 VAL B CB  1 
ATOM   7065  C CG1 . VAL B 1 351 ? 58.016  56.002  -34.822 1.00 96.03  ? 351 VAL B CG1 1 
ATOM   7066  C CG2 . VAL B 1 351 ? 55.867  55.938  -33.527 1.00 96.95  ? 351 VAL B CG2 1 
ATOM   7067  N N   . LYS B 1 352 ? 60.422  55.383  -32.783 1.00 97.09  ? 352 LYS B N   1 
ATOM   7068  C CA  . LYS B 1 352 ? 61.857  55.640  -32.774 1.00 97.72  ? 352 LYS B CA  1 
ATOM   7069  C C   . LYS B 1 352 ? 62.412  55.516  -34.189 1.00 95.76  ? 352 LYS B C   1 
ATOM   7070  O O   . LYS B 1 352 ? 61.914  54.719  -34.990 1.00 93.12  ? 352 LYS B O   1 
ATOM   7071  C CB  . LYS B 1 352 ? 62.635  54.659  -31.886 1.00 97.03  ? 352 LYS B CB  1 
ATOM   7072  C CG  . LYS B 1 352 ? 62.482  54.866  -30.382 1.00 99.22  ? 352 LYS B CG  1 
ATOM   7073  C CD  . LYS B 1 352 ? 63.022  53.726  -29.519 1.00 98.17  ? 352 LYS B CD  1 
ATOM   7074  C CE  . LYS B 1 352 ? 62.555  53.841  -28.098 1.00 100.01 ? 352 LYS B CE  1 
ATOM   7075  N NZ  . LYS B 1 352 ? 62.869  52.658  -27.301 1.00 98.93  ? 352 LYS B NZ  1 
ATOM   7076  N N   . PHE B 1 353 ? 63.448  56.322  -34.459 1.00 97.14  ? 353 PHE B N   1 
ATOM   7077  C CA  . PHE B 1 353 ? 64.216  56.229  -35.688 1.00 95.96  ? 353 PHE B CA  1 
ATOM   7078  C C   . PHE B 1 353 ? 65.703  56.379  -35.365 1.00 97.21  ? 353 PHE B C   1 
ATOM   7079  O O   . PHE B 1 353 ? 66.139  57.450  -34.931 1.00 99.97  ? 353 PHE B O   1 
ATOM   7080  C CB  . PHE B 1 353 ? 63.767  57.261  -36.723 1.00 97.04  ? 353 PHE B CB  1 
ATOM   7081  C CG  . PHE B 1 353 ? 64.638  57.223  -37.968 1.00 96.47  ? 353 PHE B CG  1 
ATOM   7082  C CD1 . PHE B 1 353 ? 64.675  56.088  -38.768 1.00 93.51  ? 353 PHE B CD1 1 
ATOM   7083  C CD2 . PHE B 1 353 ? 65.430  58.307  -38.327 1.00 99.13  ? 353 PHE B CD2 1 
ATOM   7084  C CE1 . PHE B 1 353 ? 65.479  56.035  -39.897 1.00 93.15  ? 353 PHE B CE1 1 
ATOM   7085  C CE2 . PHE B 1 353 ? 66.217  58.258  -39.467 1.00 98.83  ? 353 PHE B CE2 1 
ATOM   7086  C CZ  . PHE B 1 353 ? 66.243  57.116  -40.246 1.00 95.83  ? 353 PHE B CZ  1 
ATOM   7087  N N   . ARG B 1 354 ? 66.452  55.287  -35.609 1.00 95.03  ? 354 ARG B N   1 
ATOM   7088  C CA  . ARG B 1 354 ? 67.843  55.119  -35.205 1.00 95.85  ? 354 ARG B CA  1 
ATOM   7089  C C   . ARG B 1 354 ? 67.968  55.242  -33.688 1.00 97.50  ? 354 ARG B C   1 
ATOM   7090  O O   . ARG B 1 354 ? 68.916  55.845  -33.185 1.00 99.75  ? 354 ARG B O   1 
ATOM   7091  C CB  . ARG B 1 354 ? 68.792  56.058  -35.959 1.00 97.87  ? 354 ARG B CB  1 
ATOM   7092  C CG  . ARG B 1 354 ? 68.758  55.840  -37.464 1.00 96.43  ? 354 ARG B CG  1 
ATOM   7093  C CD  . ARG B 1 354 ? 69.516  56.950  -38.176 1.00 99.07  ? 354 ARG B CD  1 
ATOM   7094  N NE  . ARG B 1 354 ? 69.278  56.972  -39.624 1.00 98.32  ? 354 ARG B NE  1 
ATOM   7095  C CZ  . ARG B 1 354 ? 69.771  57.872  -40.485 1.00 100.43 ? 354 ARG B CZ  1 
ATOM   7096  N NH1 . ARG B 1 354 ? 70.691  58.748  -40.113 1.00 103.40 ? 354 ARG B NH1 1 
ATOM   7097  N NH2 . ARG B 1 354 ? 69.362  57.869  -41.745 1.00 99.66  ? 354 ARG B NH2 1 
ATOM   7098  N N   . ASP B 1 355 ? 66.989  54.656  -32.986 1.00 96.46  ? 355 ASP B N   1 
ATOM   7099  C CA  . ASP B 1 355 ? 67.046  54.415  -31.554 1.00 97.71  ? 355 ASP B CA  1 
ATOM   7100  C C   . ASP B 1 355 ? 66.940  55.734  -30.783 1.00 101.46 ? 355 ASP B C   1 
ATOM   7101  O O   . ASP B 1 355 ? 67.399  55.802  -29.646 1.00 103.25 ? 355 ASP B O   1 
ATOM   7102  C CB  . ASP B 1 355 ? 68.245  53.540  -31.186 1.00 97.24  ? 355 ASP B CB  1 
ATOM   7103  C CG  . ASP B 1 355 ? 68.432  52.239  -31.975 1.00 94.28  ? 355 ASP B CG  1 
ATOM   7104  O OD1 . ASP B 1 355 ? 67.559  51.338  -31.900 1.00 92.21  ? 355 ASP B OD1 1 
ATOM   7105  O OD2 . ASP B 1 355 ? 69.466  52.108  -32.665 1.00 94.17  ? 355 ASP B OD2 1 
ATOM   7106  N N   . LYS B 1 356 ? 66.325  56.764  -31.398 1.00 103.00 ? 356 LYS B N   1 
ATOM   7107  C CA  . LYS B 1 356 ? 65.964  58.012  -30.733 1.00 106.46 ? 356 LYS B CA  1 
ATOM   7108  C C   . LYS B 1 356 ? 64.449  58.216  -30.852 1.00 106.52 ? 356 LYS B C   1 
ATOM   7109  O O   . LYS B 1 356 ? 63.856  57.821  -31.853 1.00 104.32 ? 356 LYS B O   1 
ATOM   7110  C CB  . LYS B 1 356 ? 66.717  59.204  -31.335 1.00 108.86 ? 356 LYS B CB  1 
ATOM   7111  C CG  . LYS B 1 356 ? 66.318  60.555  -30.744 1.00 112.45 ? 356 LYS B CG  1 
ATOM   7112  C CD  . LYS B 1 356 ? 67.190  61.749  -31.117 1.00 115.51 ? 356 LYS B CD  1 
ATOM   7113  C CE  . LYS B 1 356 ? 66.916  62.298  -32.479 1.00 115.22 ? 356 LYS B CE  1 
ATOM   7114  N NZ  . LYS B 1 356 ? 67.600  63.586  -32.630 1.00 118.76 ? 356 LYS B NZ  1 
ATOM   7115  N N   . VAL B 1 357 ? 63.833  58.849  -29.838 1.00 109.37 ? 357 VAL B N   1 
ATOM   7116  C CA  . VAL B 1 357 ? 62.380  58.994  -29.757 1.00 109.70 ? 357 VAL B CA  1 
ATOM   7117  C C   . VAL B 1 357 ? 61.930  60.176  -30.621 1.00 112.02 ? 357 VAL B C   1 
ATOM   7118  O O   . VAL B 1 357 ? 62.497  61.267  -30.506 1.00 115.66 ? 357 VAL B O   1 
ATOM   7119  C CB  . VAL B 1 357 ? 61.918  59.173  -28.291 1.00 111.48 ? 357 VAL B CB  1 
ATOM   7120  C CG1 . VAL B 1 357 ? 60.424  59.484  -28.179 1.00 111.68 ? 357 VAL B CG1 1 
ATOM   7121  C CG2 . VAL B 1 357 ? 62.291  57.968  -27.429 1.00 109.83 ? 357 VAL B CG2 1 
ATOM   7122  N N   . ILE B 1 358 ? 60.905  59.958  -31.467 1.00 110.53 ? 358 ILE B N   1 
ATOM   7123  C CA  . ILE B 1 358 ? 60.320  61.027  -32.271 1.00 112.57 ? 358 ILE B CA  1 
ATOM   7124  C C   . ILE B 1 358 ? 58.828  61.188  -31.959 1.00 113.70 ? 358 ILE B C   1 
ATOM   7125  O O   . ILE B 1 358 ? 58.251  62.245  -32.232 1.00 115.87 ? 358 ILE B O   1 
ATOM   7126  C CB  . ILE B 1 358 ? 60.562  60.820  -33.782 1.00 110.37 ? 358 ILE B CB  1 
ATOM   7127  C CG1 . ILE B 1 358 ? 59.827  59.579  -34.333 1.00 106.60 ? 358 ILE B CG1 1 
ATOM   7128  C CG2 . ILE B 1 358 ? 62.058  60.795  -34.093 1.00 110.36 ? 358 ILE B CG2 1 
ATOM   7129  C CD1 . ILE B 1 358 ? 59.871  59.441  -35.848 1.00 104.89 ? 358 ILE B CD1 1 
ATOM   7130  N N   . TYR B 1 359 ? 58.197  60.140  -31.409 1.00 112.37 ? 359 TYR B N   1 
ATOM   7131  C CA  . TYR B 1 359 ? 56.806  60.219  -30.993 1.00 113.37 ? 359 TYR B CA  1 
ATOM   7132  C C   . TYR B 1 359 ? 56.612  59.383  -29.729 1.00 112.89 ? 359 TYR B C   1 
ATOM   7133  O O   . TYR B 1 359 ? 57.134  58.281  -29.622 1.00 111.04 ? 359 TYR B O   1 
ATOM   7134  C CB  . TYR B 1 359 ? 55.887  59.763  -32.135 1.00 111.38 ? 359 TYR B CB  1 
ATOM   7135  C CG  . TYR B 1 359 ? 54.391  59.857  -31.839 1.00 112.21 ? 359 TYR B CG  1 
ATOM   7136  C CD1 . TYR B 1 359 ? 53.719  58.808  -31.220 1.00 110.46 ? 359 TYR B CD1 1 
ATOM   7137  C CD2 . TYR B 1 359 ? 53.652  60.993  -32.158 1.00 114.41 ? 359 TYR B CD2 1 
ATOM   7138  C CE1 . TYR B 1 359 ? 52.367  58.880  -30.925 1.00 110.86 ? 359 TYR B CE1 1 
ATOM   7139  C CE2 . TYR B 1 359 ? 52.295  61.068  -31.881 1.00 114.92 ? 359 TYR B CE2 1 
ATOM   7140  C CZ  . TYR B 1 359 ? 51.650  60.011  -31.258 1.00 113.05 ? 359 TYR B CZ  1 
ATOM   7141  O OH  . TYR B 1 359 ? 50.316  60.045  -30.960 1.00 113.50 ? 359 TYR B OH  1 
ATOM   7142  N N   . SER B 1 360 ? 55.832  59.920  -28.788 1.00 115.28 ? 360 SER B N   1 
ATOM   7143  C CA  . SER B 1 360 ? 55.419  59.203  -27.594 1.00 115.04 ? 360 SER B CA  1 
ATOM   7144  C C   . SER B 1 360 ? 54.069  59.754  -27.122 1.00 117.74 ? 360 SER B C   1 
ATOM   7145  O O   . SER B 1 360 ? 53.977  60.920  -26.746 1.00 120.74 ? 360 SER B O   1 
ATOM   7146  C CB  . SER B 1 360 ? 56.474  59.310  -26.537 1.00 116.19 ? 360 SER B CB  1 
ATOM   7147  O OG  . SER B 1 360 ? 55.914  59.071  -25.256 1.00 117.23 ? 360 SER B OG  1 
ATOM   7148  N N   . LYS B 1 361 ? 53.017  58.921  -27.183 1.00 116.71 ? 361 LYS B N   1 
ATOM   7149  C CA  . LYS B 1 361 ? 51.676  59.325  -26.777 1.00 119.15 ? 361 LYS B CA  1 
ATOM   7150  C C   . LYS B 1 361 ? 51.119  58.325  -25.763 1.00 118.71 ? 361 LYS B C   1 
ATOM   7151  O O   . LYS B 1 361 ? 51.017  57.129  -26.046 1.00 114.90 ? 361 LYS B O   1 
ATOM   7152  C CB  . LYS B 1 361 ? 50.744  59.453  -27.989 1.00 118.36 ? 361 LYS B CB  1 
ATOM   7153  C CG  . LYS B 1 361 ? 49.317  59.934  -27.715 1.00 120.88 ? 361 LYS B CG  1 
ATOM   7154  C CD  . LYS B 1 361 ? 49.244  61.387  -27.256 1.00 126.21 ? 361 LYS B CD  1 
ATOM   7155  C CE  . LYS B 1 361 ? 47.903  62.046  -27.387 1.00 128.81 ? 361 LYS B CE  1 
ATOM   7156  N NZ  . LYS B 1 361 ? 47.453  62.057  -28.781 1.00 127.76 ? 361 LYS B NZ  1 
ATOM   7157  N N   . ASN B 1 362 ? 50.766  58.841  -24.577 1.00 122.13 ? 362 ASN B N   1 
ATOM   7158  C CA  . ASN B 1 362 ? 50.073  58.055  -23.571 1.00 122.81 ? 362 ASN B CA  1 
ATOM   7159  C C   . ASN B 1 362 ? 48.624  57.918  -24.020 1.00 123.07 ? 362 ASN B C   1 
ATOM   7160  O O   . ASN B 1 362 ? 48.026  58.896  -24.468 1.00 124.73 ? 362 ASN B O   1 
ATOM   7161  C CB  . ASN B 1 362 ? 50.153  58.683  -22.185 1.00 126.54 ? 362 ASN B CB  1 
ATOM   7162  C CG  . ASN B 1 362 ? 51.572  58.996  -21.773 1.00 128.09 ? 362 ASN B CG  1 
ATOM   7163  O OD1 . ASN B 1 362 ? 52.469  58.168  -21.974 1.00 126.59 ? 362 ASN B OD1 1 
ATOM   7164  N ND2 . ASN B 1 362 ? 51.803  60.178  -21.215 1.00 131.60 ? 362 ASN B ND2 1 
ATOM   7165  N N   . ILE B 1 363 ? 48.073  56.705  -23.899 1.00 121.15 ? 363 ILE B N   1 
ATOM   7166  C CA  . ILE B 1 363 ? 46.787  56.381  -24.496 1.00 120.46 ? 363 ILE B CA  1 
ATOM   7167  C C   . ILE B 1 363 ? 45.696  56.440  -23.422 1.00 124.20 ? 363 ILE B C   1 
ATOM   7168  O O   . ILE B 1 363 ? 45.622  55.539  -22.591 1.00 125.87 ? 363 ILE B O   1 
ATOM   7169  C CB  . ILE B 1 363 ? 46.920  55.013  -25.194 1.00 115.23 ? 363 ILE B CB  1 
ATOM   7170  C CG1 . ILE B 1 363 ? 47.965  55.086  -26.284 1.00 112.88 ? 363 ILE B CG1 1 
ATOM   7171  C CG2 . ILE B 1 363 ? 45.599  54.488  -25.752 1.00 114.24 ? 363 ILE B CG2 1 
ATOM   7172  C CD1 . ILE B 1 363 ? 47.669  56.093  -27.376 1.00 112.94 ? 363 ILE B CD1 1 
ATOM   7173  N N   . THR B 1 364 ? 44.860  57.495  -23.431 1.00 126.71 ? 364 THR B N   1 
ATOM   7174  C CA  . THR B 1 364 ? 43.863  57.685  -22.380 1.00 130.36 ? 364 THR B CA  1 
ATOM   7175  C C   . THR B 1 364 ? 42.568  56.949  -22.725 1.00 129.24 ? 364 THR B C   1 
ATOM   7176  O O   . THR B 1 364 ? 41.696  56.805  -21.870 1.00 131.21 ? 364 THR B O   1 
ATOM   7177  C CB  . THR B 1 364 ? 43.554  59.162  -22.099 1.00 135.21 ? 364 THR B CB  1 
ATOM   7178  O OG1 . THR B 1 364 ? 43.165  59.783  -23.321 1.00 135.67 ? 364 THR B OG1 1 
ATOM   7179  C CG2 . THR B 1 364 ? 44.704  59.921  -21.458 1.00 137.21 ? 364 THR B CG2 1 
ATOM   7180  N N   . SER B 1 365 ? 42.405  56.539  -23.987 1.00 126.19 ? 365 SER B N   1 
ATOM   7181  C CA  . SER B 1 365 ? 41.233  55.776  -24.380 1.00 124.25 ? 365 SER B CA  1 
ATOM   7182  C C   . SER B 1 365 ? 41.607  54.868  -25.544 1.00 119.88 ? 365 SER B C   1 
ATOM   7183  O O   . SER B 1 365 ? 42.553  55.159  -26.268 1.00 118.75 ? 365 SER B O   1 
ATOM   7184  C CB  . SER B 1 365 ? 40.070  56.676  -24.709 1.00 126.49 ? 365 SER B CB  1 
ATOM   7185  O OG  . SER B 1 365 ? 40.379  57.529  -25.798 1.00 126.49 ? 365 SER B OG  1 
ATOM   7186  N N   . GLU B 1 366 ? 40.872  53.759  -25.679 1.00 117.60 ? 366 GLU B N   1 
ATOM   7187  C CA  . GLU B 1 366 ? 41.174  52.728  -26.660 1.00 113.63 ? 366 GLU B CA  1 
ATOM   7188  C C   . GLU B 1 366 ? 40.463  53.036  -27.975 1.00 112.02 ? 366 GLU B C   1 
ATOM   7189  O O   . GLU B 1 366 ? 39.658  53.961  -28.058 1.00 113.19 ? 366 GLU B O   1 
ATOM   7190  C CB  . GLU B 1 366 ? 40.796  51.345  -26.121 1.00 112.86 ? 366 GLU B CB  1 
ATOM   7191  C CG  . GLU B 1 366 ? 39.309  51.140  -25.830 1.00 114.10 ? 366 GLU B CG  1 
ATOM   7192  C CD  . GLU B 1 366 ? 39.006  49.854  -25.071 1.00 113.64 ? 366 GLU B CD  1 
ATOM   7193  O OE1 . GLU B 1 366 ? 39.411  48.771  -25.553 1.00 111.04 ? 366 GLU B OE1 1 
ATOM   7194  O OE2 . GLU B 1 366 ? 38.380  49.931  -23.991 1.00 115.62 ? 366 GLU B OE2 1 
ATOM   7195  N N   . GLY B 1 367 ? 40.798  52.257  -29.007 1.00 108.70 ? 367 GLY B N   1 
ATOM   7196  C CA  . GLY B 1 367 ? 40.157  52.377  -30.304 1.00 107.64 ? 367 GLY B CA  1 
ATOM   7197  C C   . GLY B 1 367 ? 40.961  53.267  -31.247 1.00 107.39 ? 367 GLY B C   1 
ATOM   7198  O O   . GLY B 1 367 ? 42.186  53.308  -31.179 1.00 106.25 ? 367 GLY B O   1 
ATOM   7199  N N   . TYR B 1 368 ? 40.247  53.983  -32.121 1.00 108.68 ? 368 TYR B N   1 
ATOM   7200  C CA  . TYR B 1 368 ? 40.883  54.782  -33.154 1.00 108.74 ? 368 TYR B CA  1 
ATOM   7201  C C   . TYR B 1 368 ? 41.493  56.022  -32.512 1.00 111.74 ? 368 TYR B C   1 
ATOM   7202  O O   . TYR B 1 368 ? 40.905  56.625  -31.618 1.00 113.69 ? 368 TYR B O   1 
ATOM   7203  C CB  . TYR B 1 368 ? 39.897  55.190  -34.254 1.00 109.04 ? 368 TYR B CB  1 
ATOM   7204  C CG  . TYR B 1 368 ? 40.495  56.029  -35.381 1.00 109.33 ? 368 TYR B CG  1 
ATOM   7205  C CD1 . TYR B 1 368 ? 40.708  57.397  -35.231 1.00 111.86 ? 368 TYR B CD1 1 
ATOM   7206  C CD2 . TYR B 1 368 ? 40.821  55.461  -36.608 1.00 106.84 ? 368 TYR B CD2 1 
ATOM   7207  C CE1 . TYR B 1 368 ? 41.246  58.163  -36.252 1.00 111.95 ? 368 TYR B CE1 1 
ATOM   7208  C CE2 . TYR B 1 368 ? 41.352  56.220  -37.641 1.00 106.97 ? 368 TYR B CE2 1 
ATOM   7209  C CZ  . TYR B 1 368 ? 41.568  57.575  -37.462 1.00 109.46 ? 368 TYR B CZ  1 
ATOM   7210  O OH  . TYR B 1 368 ? 42.090  58.320  -38.476 1.00 109.45 ? 368 TYR B OH  1 
ATOM   7211  N N   . MET B 1 369 ? 42.673  56.397  -33.001 1.00 111.67 ? 369 MET B N   1 
ATOM   7212  C CA  . MET B 1 369 ? 43.378  57.554  -32.494 1.00 114.91 ? 369 MET B CA  1 
ATOM   7213  C C   . MET B 1 369 ? 44.256  58.079  -33.620 1.00 113.51 ? 369 MET B C   1 
ATOM   7214  O O   . MET B 1 369 ? 45.097  57.340  -34.122 1.00 112.27 ? 369 MET B O   1 
ATOM   7215  C CB  . MET B 1 369 ? 44.207  57.162  -31.266 1.00 117.05 ? 369 MET B CB  1 
ATOM   7216  C CG  . MET B 1 369 ? 45.087  58.273  -30.705 1.00 122.04 ? 369 MET B CG  1 
ATOM   7217  S SD  . MET B 1 369 ? 46.835  58.150  -31.159 1.00 124.01 ? 369 MET B SD  1 
ATOM   7218  C CE  . MET B 1 369 ? 47.270  56.526  -30.526 1.00 119.23 ? 369 MET B CE  1 
ATOM   7219  N N   . ALA B 1 370 ? 44.038  59.339  -34.012 1.00 114.63 ? 370 ALA B N   1 
ATOM   7220  C CA  . ALA B 1 370 ? 44.775  59.963  -35.101 1.00 113.72 ? 370 ALA B CA  1 
ATOM   7221  C C   . ALA B 1 370 ? 45.774  60.982  -34.550 1.00 115.06 ? 370 ALA B C   1 
ATOM   7222  O O   . ALA B 1 370 ? 45.571  61.517  -33.461 1.00 117.67 ? 370 ALA B O   1 
ATOM   7223  C CB  . ALA B 1 370 ? 43.809  60.618  -36.066 1.00 114.77 ? 370 ALA B CB  1 
ATOM   7224  N N   . ASP B 1 371 ? 46.832  61.259  -35.330 1.00 112.86 ? 371 ASP B N   1 
ATOM   7225  C CA  . ASP B 1 371 ? 47.907  62.139  -34.902 1.00 114.04 ? 371 ASP B CA  1 
ATOM   7226  C C   . ASP B 1 371 ? 48.871  62.357  -36.072 1.00 113.14 ? 371 ASP B C   1 
ATOM   7227  O O   . ASP B 1 371 ? 48.568  61.958  -37.197 1.00 110.43 ? 371 ASP B O   1 
ATOM   7228  C CB  . ASP B 1 371 ? 48.579  61.562  -33.666 1.00 113.26 ? 371 ASP B CB  1 
ATOM   7229  C CG  . ASP B 1 371 ? 48.957  62.543  -32.569 1.00 116.38 ? 371 ASP B CG  1 
ATOM   7230  O OD1 . ASP B 1 371 ? 49.682  63.503  -32.873 1.00 118.23 ? 371 ASP B OD1 1 
ATOM   7231  O OD2 . ASP B 1 371 ? 48.557  62.305  -31.414 1.00 116.95 ? 371 ASP B OD2 1 
ATOM   7232  N N   . GLU B 1 372 ? 50.023  62.996  -35.785 1.00 115.58 ? 372 GLU B N   1 
ATOM   7233  C CA  . GLU B 1 372 ? 51.085  63.263  -36.754 1.00 116.44 ? 372 GLU B CA  1 
ATOM   7234  C C   . GLU B 1 372 ? 52.459  62.834  -36.214 1.00 116.29 ? 372 GLU B C   1 
ATOM   7235  O O   . GLU B 1 372 ? 52.707  62.893  -35.010 1.00 118.50 ? 372 GLU B O   1 
ATOM   7236  C CB  . GLU B 1 372 ? 51.213  64.760  -37.060 1.00 120.70 ? 372 GLU B CB  1 
ATOM   7237  C CG  . GLU B 1 372 ? 50.140  65.315  -37.991 1.00 122.24 ? 372 GLU B CG  1 
ATOM   7238  C CD  . GLU B 1 372 ? 50.312  66.799  -38.253 1.00 127.25 ? 372 GLU B CD  1 
ATOM   7239  O OE1 . GLU B 1 372 ? 51.269  67.410  -37.724 1.00 129.80 ? 372 GLU B OE1 1 
ATOM   7240  O OE2 . GLU B 1 372 ? 49.470  67.357  -38.985 1.00 129.79 ? 372 GLU B OE2 1 
ATOM   7241  N N   . LEU B 1 373 ? 53.373  62.436  -37.113 1.00 113.96 ? 373 LEU B N   1 
ATOM   7242  C CA  . LEU B 1 373 ? 54.790  62.433  -36.794 1.00 114.51 ? 373 LEU B CA  1 
ATOM   7243  C C   . LEU B 1 373 ? 55.432  63.646  -37.456 1.00 117.88 ? 373 LEU B C   1 
ATOM   7244  O O   . LEU B 1 373 ? 54.879  64.209  -38.400 1.00 119.03 ? 373 LEU B O   1 
ATOM   7245  C CB  . LEU B 1 373 ? 55.489  61.164  -37.270 1.00 111.39 ? 373 LEU B CB  1 
ATOM   7246  C CG  . LEU B 1 373 ? 54.919  59.828  -36.779 1.00 108.66 ? 373 LEU B CG  1 
ATOM   7247  C CD1 . LEU B 1 373 ? 55.604  58.702  -37.529 1.00 105.20 ? 373 LEU B CD1 1 
ATOM   7248  C CD2 . LEU B 1 373 ? 55.056  59.624  -35.277 1.00 109.48 ? 373 LEU B CD2 1 
ATOM   7249  N N   . THR B 1 374 ? 56.612  64.029  -36.958 1.00 119.71 ? 374 THR B N   1 
ATOM   7250  C CA  . THR B 1 374 ? 57.454  64.998  -37.641 1.00 122.40 ? 374 THR B CA  1 
ATOM   7251  C C   . THR B 1 374 ? 58.859  64.402  -37.772 1.00 121.56 ? 374 THR B C   1 
ATOM   7252  O O   . THR B 1 374 ? 59.509  64.054  -36.783 1.00 120.40 ? 374 THR B O   1 
ATOM   7253  C CB  . THR B 1 374 ? 57.445  66.351  -36.917 1.00 126.63 ? 374 THR B CB  1 
ATOM   7254  O OG1 . THR B 1 374 ? 56.080  66.727  -36.757 1.00 127.53 ? 374 THR B OG1 1 
ATOM   7255  C CG2 . THR B 1 374 ? 58.171  67.446  -37.681 1.00 128.91 ? 374 THR B CG2 1 
ATOM   7256  N N   . ILE B 1 375 ? 59.306  64.291  -39.027 1.00 121.81 ? 375 ILE B N   1 
ATOM   7257  C CA  . ILE B 1 375 ? 60.619  63.771  -39.364 1.00 122.03 ? 375 ILE B CA  1 
ATOM   7258  C C   . ILE B 1 375 ? 61.430  64.893  -40.000 1.00 125.66 ? 375 ILE B C   1 
ATOM   7259  O O   . ILE B 1 375 ? 60.876  65.893  -40.447 1.00 128.25 ? 375 ILE B O   1 
ATOM   7260  C CB  . ILE B 1 375 ? 60.511  62.538  -40.288 1.00 119.76 ? 375 ILE B CB  1 
ATOM   7261  C CG1 . ILE B 1 375 ? 59.644  62.800  -41.547 1.00 120.16 ? 375 ILE B CG1 1 
ATOM   7262  C CG2 . ILE B 1 375 ? 60.010  61.314  -39.515 1.00 116.43 ? 375 ILE B CG2 1 
ATOM   7263  C CD1 . ILE B 1 375 ? 59.632  61.651  -42.550 1.00 116.62 ? 375 ILE B CD1 1 
ATOM   7264  N N   . ASP B 1 376 ? 62.750  64.714  -40.031 1.00 126.79 ? 376 ASP B N   1 
ATOM   7265  C CA  . ASP B 1 376 ? 63.628  65.664  -40.689 1.00 130.40 ? 376 ASP B CA  1 
ATOM   7266  C C   . ASP B 1 376 ? 64.457  64.891  -41.710 1.00 129.06 ? 376 ASP B C   1 
ATOM   7267  O O   . ASP B 1 376 ? 65.654  64.699  -41.516 1.00 130.80 ? 376 ASP B O   1 
ATOM   7268  C CB  . ASP B 1 376 ? 64.429  66.462  -39.668 1.00 134.00 ? 376 ASP B CB  1 
ATOM   7269  C CG  . ASP B 1 376 ? 65.285  67.588  -40.243 1.00 138.90 ? 376 ASP B CG  1 
ATOM   7270  O OD1 . ASP B 1 376 ? 65.729  67.444  -41.402 1.00 139.31 ? 376 ASP B OD1 1 
ATOM   7271  O OD2 . ASP B 1 376 ? 65.468  68.631  -39.558 1.00 142.41 ? 376 ASP B OD2 1 
ATOM   7272  N N   . PRO B 1 377 ? 63.856  64.419  -42.829 1.00 126.55 ? 377 PRO B N   1 
ATOM   7273  C CA  . PRO B 1 377 ? 64.570  63.572  -43.784 1.00 124.06 ? 377 PRO B CA  1 
ATOM   7274  C C   . PRO B 1 377 ? 65.488  64.380  -44.698 1.00 126.50 ? 377 PRO B C   1 
ATOM   7275  O O   . PRO B 1 377 ? 65.057  65.374  -45.295 1.00 127.80 ? 377 PRO B O   1 
ATOM   7276  C CB  . PRO B 1 377 ? 63.413  62.923  -44.547 1.00 121.07 ? 377 PRO B CB  1 
ATOM   7277  C CG  . PRO B 1 377 ? 62.376  64.012  -44.611 1.00 123.05 ? 377 PRO B CG  1 
ATOM   7278  C CD  . PRO B 1 377 ? 62.484  64.714  -43.264 1.00 125.84 ? 377 PRO B CD  1 
ATOM   7279  N N   . VAL B 1 378 ? 66.751  63.930  -44.784 1.00 125.81 ? 378 VAL B N   1 
ATOM   7280  C CA  . VAL B 1 378 ? 67.755  64.544  -45.645 1.00 127.63 ? 378 VAL B CA  1 
ATOM   7281  C C   . VAL B 1 378 ? 67.571  63.989  -47.063 1.00 125.57 ? 378 VAL B C   1 
ATOM   7282  O O   . VAL B 1 378 ? 67.282  62.796  -47.231 1.00 121.81 ? 378 VAL B O   1 
ATOM   7283  C CB  . VAL B 1 378 ? 69.188  64.324  -45.105 1.00 127.50 ? 378 VAL B CB  1 
ATOM   7284  C CG1 . VAL B 1 378 ? 70.248  65.040  -45.939 1.00 129.80 ? 378 VAL B CG1 1 
ATOM   7285  C CG2 . VAL B 1 378 ? 69.322  64.730  -43.639 1.00 128.91 ? 378 VAL B CG2 1 
ATOM   7286  N N   . GLY B 1 379 ? 67.695  64.887  -48.063 1.00 126.75 ? 379 GLY B N   1 
ATOM   7287  C CA  . GLY B 1 379 ? 67.609  64.563  -49.483 1.00 124.88 ? 379 GLY B CA  1 
ATOM   7288  C C   . GLY B 1 379 ? 66.510  63.545  -49.801 1.00 120.47 ? 379 GLY B C   1 
ATOM   7289  O O   . GLY B 1 379 ? 65.327  63.879  -49.757 1.00 119.78 ? 379 GLY B O   1 
ATOM   7290  N N   . ILE B 1 380 ? 66.932  62.326  -50.178 1.00 116.72 ? 380 ILE B N   1 
ATOM   7291  C CA  . ILE B 1 380 ? 66.069  61.157  -50.176 1.00 112.85 ? 380 ILE B CA  1 
ATOM   7292  C C   . ILE B 1 380 ? 66.614  60.168  -49.137 1.00 110.50 ? 380 ILE B C   1 
ATOM   7293  O O   . ILE B 1 380 ? 67.742  59.683  -49.237 1.00 110.01 ? 380 ILE B O   1 
ATOM   7294  C CB  . ILE B 1 380 ? 65.923  60.525  -51.579 1.00 111.20 ? 380 ILE B CB  1 
ATOM   7295  C CG1 . ILE B 1 380 ? 65.635  61.560  -52.686 1.00 113.44 ? 380 ILE B CG1 1 
ATOM   7296  C CG2 . ILE B 1 380 ? 64.850  59.432  -51.554 1.00 107.82 ? 380 ILE B CG2 1 
ATOM   7297  C CD1 . ILE B 1 380 ? 65.544  60.981  -54.092 1.00 111.79 ? 380 ILE B CD1 1 
ATOM   7298  N N   . GLU B 1 381 ? 65.773  59.864  -48.138 1.00 108.97 ? 381 GLU B N   1 
ATOM   7299  C CA  . GLU B 1 381 ? 66.159  59.078  -46.978 1.00 106.76 ? 381 GLU B CA  1 
ATOM   7300  C C   . GLU B 1 381 ? 65.114  57.988  -46.719 1.00 103.91 ? 381 GLU B C   1 
ATOM   7301  O O   . GLU B 1 381 ? 63.946  58.254  -46.423 1.00 103.97 ? 381 GLU B O   1 
ATOM   7302  C CB  . GLU B 1 381 ? 66.303  60.013  -45.779 1.00 108.71 ? 381 GLU B CB  1 
ATOM   7303  C CG  . GLU B 1 381 ? 66.979  59.369  -44.576 1.00 107.55 ? 381 GLU B CG  1 
ATOM   7304  C CD  . GLU B 1 381 ? 67.125  60.287  -43.377 1.00 109.88 ? 381 GLU B CD  1 
ATOM   7305  O OE1 . GLU B 1 381 ? 67.749  61.360  -43.520 1.00 112.50 ? 381 GLU B OE1 1 
ATOM   7306  O OE2 . GLU B 1 381 ? 66.612  59.918  -42.298 1.00 108.69 ? 381 GLU B OE2 1 
ATOM   7307  N N   . ASP B 1 382 ? 65.556  56.740  -46.845 1.00 101.11 ? 382 ASP B N   1 
ATOM   7308  C CA  . ASP B 1 382 ? 64.765  55.618  -46.384 1.00 98.24  ? 382 ASP B CA  1 
ATOM   7309  C C   . ASP B 1 382 ? 64.798  55.611  -44.859 1.00 98.24  ? 382 ASP B C   1 
ATOM   7310  O O   . ASP B 1 382 ? 65.807  55.944  -44.243 1.00 99.37  ? 382 ASP B O   1 
ATOM   7311  C CB  . ASP B 1 382 ? 65.254  54.313  -46.991 1.00 95.94  ? 382 ASP B CB  1 
ATOM   7312  C CG  . ASP B 1 382 ? 66.692  53.951  -46.659 1.00 96.24  ? 382 ASP B CG  1 
ATOM   7313  O OD1 . ASP B 1 382 ? 67.598  54.725  -47.050 1.00 98.48  ? 382 ASP B OD1 1 
ATOM   7314  O OD2 . ASP B 1 382 ? 66.878  52.914  -45.994 1.00 94.53  ? 382 ASP B OD2 1 
ATOM   7315  N N   . MET B 1 383 ? 63.666  55.228  -44.269 1.00 97.13  ? 383 MET B N   1 
ATOM   7316  C CA  . MET B 1 383 ? 63.500  55.229  -42.829 1.00 97.28  ? 383 MET B CA  1 
ATOM   7317  C C   . MET B 1 383 ? 62.615  54.042  -42.454 1.00 93.65  ? 383 MET B C   1 
ATOM   7318  O O   . MET B 1 383 ? 61.619  53.778  -43.116 1.00 92.01  ? 383 MET B O   1 
ATOM   7319  C CB  . MET B 1 383 ? 62.923  56.577  -42.382 1.00 100.66 ? 383 MET B CB  1 
ATOM   7320  C CG  . MET B 1 383 ? 63.712  57.751  -42.936 1.00 103.95 ? 383 MET B CG  1 
ATOM   7321  S SD  . MET B 1 383 ? 63.086  59.387  -42.523 1.00 108.88 ? 383 MET B SD  1 
ATOM   7322  C CE  . MET B 1 383 ? 63.082  59.360  -40.725 1.00 109.62 ? 383 MET B CE  1 
ATOM   7323  N N   . GLU B 1 384 ? 63.067  53.282  -41.455 1.00 92.23  ? 384 GLU B N   1 
ATOM   7324  C CA  . GLU B 1 384 ? 62.267  52.274  -40.796 1.00 90.08  ? 384 GLU B CA  1 
ATOM   7325  C C   . GLU B 1 384 ? 61.846  52.827  -39.447 1.00 91.02  ? 384 GLU B C   1 
ATOM   7326  O O   . GLU B 1 384 ? 62.662  52.963  -38.539 1.00 91.73  ? 384 GLU B O   1 
ATOM   7327  C CB  . GLU B 1 384 ? 63.102  51.023  -40.544 1.00 89.46  ? 384 GLU B CB  1 
ATOM   7328  C CG  . GLU B 1 384 ? 62.360  49.884  -39.845 1.00 87.84  ? 384 GLU B CG  1 
ATOM   7329  C CD  . GLU B 1 384 ? 63.308  48.755  -39.512 1.00 87.18  ? 384 GLU B CD  1 
ATOM   7330  O OE1 . GLU B 1 384 ? 64.504  49.036  -39.639 1.00 87.44  ? 384 GLU B OE1 1 
ATOM   7331  O OE2 . GLU B 1 384 ? 62.899  47.623  -39.170 1.00 87.99  ? 384 GLU B OE2 1 
ATOM   7332  N N   . LEU B 1 385 ? 60.565  53.157  -39.349 1.00 91.07  ? 385 LEU B N   1 
ATOM   7333  C CA  . LEU B 1 385 ? 60.017  53.715  -38.127 1.00 92.57  ? 385 LEU B CA  1 
ATOM   7334  C C   . LEU B 1 385 ? 59.689  52.538  -37.209 1.00 90.08  ? 385 LEU B C   1 
ATOM   7335  O O   . LEU B 1 385 ? 58.879  51.689  -37.567 1.00 87.17  ? 385 LEU B O   1 
ATOM   7336  C CB  . LEU B 1 385 ? 58.775  54.583  -38.392 1.00 93.76  ? 385 LEU B CB  1 
ATOM   7337  C CG  . LEU B 1 385 ? 58.867  55.698  -39.449 1.00 95.28  ? 385 LEU B CG  1 
ATOM   7338  C CD1 . LEU B 1 385 ? 57.445  56.133  -39.814 1.00 95.50  ? 385 LEU B CD1 1 
ATOM   7339  C CD2 . LEU B 1 385 ? 59.689  56.943  -39.058 1.00 98.23  ? 385 LEU B CD2 1 
ATOM   7340  N N   . ALA B 1 386 ? 60.289  52.542  -36.015 1.00 90.91  ? 386 ALA B N   1 
ATOM   7341  C CA  . ALA B 1 386 ? 60.123  51.472  -35.048 1.00 90.00  ? 386 ALA B CA  1 
ATOM   7342  C C   . ALA B 1 386 ? 59.021  51.788  -34.043 1.00 91.16  ? 386 ALA B C   1 
ATOM   7343  O O   . ALA B 1 386 ? 59.237  52.594  -33.144 1.00 93.70  ? 386 ALA B O   1 
ATOM   7344  C CB  . ALA B 1 386 ? 61.434  51.266  -34.325 1.00 91.00  ? 386 ALA B CB  1 
ATOM   7345  N N   . PHE B 1 387 ? 57.881  51.096  -34.152 1.00 89.76  ? 387 PHE B N   1 
ATOM   7346  C CA  . PHE B 1 387 ? 56.743  51.335  -33.271 1.00 91.49  ? 387 PHE B CA  1 
ATOM   7347  C C   . PHE B 1 387 ? 56.824  50.458  -32.022 1.00 91.59  ? 387 PHE B C   1 
ATOM   7348  O O   . PHE B 1 387 ? 57.122  49.275  -32.122 1.00 89.81  ? 387 PHE B O   1 
ATOM   7349  C CB  . PHE B 1 387 ? 55.411  51.093  -33.994 1.00 90.30  ? 387 PHE B CB  1 
ATOM   7350  C CG  . PHE B 1 387 ? 54.936  52.239  -34.884 1.00 91.25  ? 387 PHE B CG  1 
ATOM   7351  C CD1 . PHE B 1 387 ? 55.559  52.501  -36.101 1.00 90.78  ? 387 PHE B CD1 1 
ATOM   7352  C CD2 . PHE B 1 387 ? 53.856  53.034  -34.521 1.00 92.45  ? 387 PHE B CD2 1 
ATOM   7353  C CE1 . PHE B 1 387 ? 55.123  53.538  -36.916 1.00 91.63  ? 387 PHE B CE1 1 
ATOM   7354  C CE2 . PHE B 1 387 ? 53.408  54.037  -35.361 1.00 93.50  ? 387 PHE B CE2 1 
ATOM   7355  C CZ  . PHE B 1 387 ? 54.049  54.297  -36.547 1.00 92.90  ? 387 PHE B CZ  1 
ATOM   7356  N N   . GLU B 1 388 ? 56.486  51.038  -30.863 1.00 94.38  ? 388 GLU B N   1 
ATOM   7357  C CA  . GLU B 1 388 ? 56.649  50.375  -29.580 1.00 95.78  ? 388 GLU B CA  1 
ATOM   7358  C C   . GLU B 1 388 ? 55.395  50.557  -28.726 1.00 97.86  ? 388 GLU B C   1 
ATOM   7359  O O   . GLU B 1 388 ? 55.124  51.657  -28.236 1.00 99.86  ? 388 GLU B O   1 
ATOM   7360  C CB  . GLU B 1 388 ? 57.867  50.929  -28.839 1.00 98.09  ? 388 GLU B CB  1 
ATOM   7361  C CG  . GLU B 1 388 ? 59.193  50.620  -29.531 1.00 97.32  ? 388 GLU B CG  1 
ATOM   7362  C CD  . GLU B 1 388 ? 60.433  51.100  -28.796 1.00 99.11  ? 388 GLU B CD  1 
ATOM   7363  O OE1 . GLU B 1 388 ? 60.292  51.699  -27.709 1.00 101.23 ? 388 GLU B OE1 1 
ATOM   7364  O OE2 . GLU B 1 388 ? 61.544  50.856  -29.310 1.00 98.40  ? 388 GLU B OE2 1 
ATOM   7365  N N   . PHE B 1 389 ? 54.676  49.443  -28.504 1.00 97.59  ? 389 PHE B N   1 
ATOM   7366  C CA  . PHE B 1 389 ? 53.417  49.456  -27.772 1.00 99.78  ? 389 PHE B CA  1 
ATOM   7367  C C   . PHE B 1 389 ? 53.657  48.957  -26.348 1.00 101.33 ? 389 PHE B C   1 
ATOM   7368  O O   . PHE B 1 389 ? 54.212  47.878  -26.148 1.00 99.46  ? 389 PHE B O   1 
ATOM   7369  C CB  . PHE B 1 389 ? 52.342  48.622  -28.484 1.00 97.90  ? 389 PHE B CB  1 
ATOM   7370  C CG  . PHE B 1 389 ? 51.974  49.092  -29.889 1.00 96.91  ? 389 PHE B CG  1 
ATOM   7371  C CD1 . PHE B 1 389 ? 52.789  48.807  -30.981 1.00 95.17  ? 389 PHE B CD1 1 
ATOM   7372  C CD2 . PHE B 1 389 ? 50.813  49.818  -30.126 1.00 98.46  ? 389 PHE B CD2 1 
ATOM   7373  C CE1 . PHE B 1 389 ? 52.459  49.242  -32.261 1.00 94.24  ? 389 PHE B CE1 1 
ATOM   7374  C CE2 . PHE B 1 389 ? 50.483  50.239  -31.412 1.00 97.62  ? 389 PHE B CE2 1 
ATOM   7375  C CZ  . PHE B 1 389 ? 51.303  49.948  -32.478 1.00 95.21  ? 389 PHE B CZ  1 
ATOM   7376  N N   . TYR B 1 390 ? 53.187  49.754  -25.377 1.00 104.60 ? 390 TYR B N   1 
ATOM   7377  C CA  . TYR B 1 390 ? 53.386  49.486  -23.961 1.00 106.46 ? 390 TYR B CA  1 
ATOM   7378  C C   . TYR B 1 390 ? 52.035  49.237  -23.280 1.00 107.36 ? 390 TYR B C   1 
ATOM   7379  O O   . TYR B 1 390 ? 50.990  49.621  -23.795 1.00 106.94 ? 390 TYR B O   1 
ATOM   7380  C CB  . TYR B 1 390 ? 54.141  50.666  -23.332 1.00 108.83 ? 390 TYR B CB  1 
ATOM   7381  C CG  . TYR B 1 390 ? 55.556  50.896  -23.848 1.00 107.60 ? 390 TYR B CG  1 
ATOM   7382  C CD1 . TYR B 1 390 ? 55.788  51.611  -25.020 1.00 106.74 ? 390 TYR B CD1 1 
ATOM   7383  C CD2 . TYR B 1 390 ? 56.659  50.412  -23.148 1.00 107.75 ? 390 TYR B CD2 1 
ATOM   7384  C CE1 . TYR B 1 390 ? 57.076  51.824  -25.486 1.00 106.58 ? 390 TYR B CE1 1 
ATOM   7385  C CE2 . TYR B 1 390 ? 57.952  50.615  -23.604 1.00 107.07 ? 390 TYR B CE2 1 
ATOM   7386  C CZ  . TYR B 1 390 ? 58.157  51.315  -24.782 1.00 106.60 ? 390 TYR B CZ  1 
ATOM   7387  O OH  . TYR B 1 390 ? 59.425  51.511  -25.239 1.00 105.90 ? 390 TYR B OH  1 
ATOM   7388  N N   . ASP B 1 391 ? 52.098  48.583  -22.111 1.00 108.39 ? 391 ASP B N   1 
ATOM   7389  C CA  . ASP B 1 391 ? 50.955  48.284  -21.266 1.00 109.36 ? 391 ASP B CA  1 
ATOM   7390  C C   . ASP B 1 391 ? 51.063  49.120  -19.992 1.00 113.23 ? 391 ASP B C   1 
ATOM   7391  O O   . ASP B 1 391 ? 51.933  49.977  -19.885 1.00 113.60 ? 391 ASP B O   1 
ATOM   7392  C CB  . ASP B 1 391 ? 50.849  46.782  -21.024 1.00 107.71 ? 391 ASP B CB  1 
ATOM   7393  C CG  . ASP B 1 391 ? 52.037  46.056  -20.391 1.00 107.26 ? 391 ASP B CG  1 
ATOM   7394  O OD1 . ASP B 1 391 ? 52.905  46.716  -19.781 1.00 109.36 ? 391 ASP B OD1 1 
ATOM   7395  O OD2 . ASP B 1 391 ? 52.090  44.815  -20.513 1.00 104.86 ? 391 ASP B OD2 1 
ATOM   7396  N N   . SER B 1 392 ? 50.135  48.908  -19.051 1.00 116.73 ? 392 SER B N   1 
ATOM   7397  C CA  . SER B 1 392 ? 50.309  49.370  -17.681 1.00 120.84 ? 392 SER B CA  1 
ATOM   7398  C C   . SER B 1 392 ? 51.281  48.413  -16.999 1.00 121.97 ? 392 SER B C   1 
ATOM   7399  O O   . SER B 1 392 ? 51.023  47.213  -16.982 1.00 121.96 ? 392 SER B O   1 
ATOM   7400  C CB  . SER B 1 392 ? 48.996  49.422  -16.948 1.00 122.21 ? 392 SER B CB  1 
ATOM   7401  O OG  . SER B 1 392 ? 48.425  48.124  -16.861 1.00 120.47 ? 392 SER B OG  1 
ATOM   7402  N N   . ASP B 1 393 ? 52.374  48.952  -16.440 1.00 124.54 ? 393 ASP B N   1 
ATOM   7403  C CA  . ASP B 1 393 ? 53.586  48.215  -16.067 1.00 124.76 ? 393 ASP B CA  1 
ATOM   7404  C C   . ASP B 1 393 ? 54.771  48.739  -16.889 1.00 123.65 ? 393 ASP B C   1 
ATOM   7405  O O   . ASP B 1 393 ? 55.911  48.679  -16.436 1.00 124.33 ? 393 ASP B O   1 
ATOM   7406  C CB  . ASP B 1 393 ? 53.502  46.689  -16.169 1.00 122.79 ? 393 ASP B CB  1 
ATOM   7407  C CG  . ASP B 1 393 ? 52.721  45.955  -15.081 1.00 124.47 ? 393 ASP B CG  1 
ATOM   7408  O OD1 . ASP B 1 393 ? 52.974  46.213  -13.887 1.00 127.22 ? 393 ASP B OD1 1 
ATOM   7409  O OD2 . ASP B 1 393 ? 51.882  45.098  -15.429 1.00 122.85 ? 393 ASP B OD2 1 
ATOM   7410  N N   . ASN B 1 394 ? 54.491  49.249  -18.098 1.00 122.14 ? 394 ASN B N   1 
ATOM   7411  C CA  . ASN B 1 394 ? 55.474  49.893  -18.959 1.00 120.49 ? 394 ASN B CA  1 
ATOM   7412  C C   . ASN B 1 394 ? 56.351  48.815  -19.592 1.00 118.30 ? 394 ASN B C   1 
ATOM   7413  O O   . ASN B 1 394 ? 57.572  48.975  -19.705 1.00 118.51 ? 394 ASN B O   1 
ATOM   7414  C CB  . ASN B 1 394 ? 56.232  50.993  -18.219 1.00 123.21 ? 394 ASN B CB  1 
ATOM   7415  C CG  . ASN B 1 394 ? 56.995  51.903  -19.151 1.00 122.64 ? 394 ASN B CG  1 
ATOM   7416  O OD1 . ASN B 1 394 ? 56.506  52.248  -20.233 1.00 121.12 ? 394 ASN B OD1 1 
ATOM   7417  N ND2 . ASN B 1 394 ? 58.199  52.292  -18.762 1.00 123.92 ? 394 ASN B ND2 1 
ATOM   7418  N N   . LYS B 1 395 ? 55.689  47.722  -20.004 1.00 115.59 ? 395 LYS B N   1 
ATOM   7419  C CA  . LYS B 1 395 ? 56.328  46.626  -20.710 1.00 113.09 ? 395 LYS B CA  1 
ATOM   7420  C C   . LYS B 1 395 ? 56.005  46.742  -22.197 1.00 108.86 ? 395 LYS B C   1 
ATOM   7421  O O   . LYS B 1 395 ? 54.890  47.111  -22.550 1.00 106.94 ? 395 LYS B O   1 
ATOM   7422  C CB  . LYS B 1 395 ? 55.869  45.291  -20.111 1.00 114.38 ? 395 LYS B CB  1 
ATOM   7423  C CG  . LYS B 1 395 ? 56.352  45.092  -18.683 1.00 118.81 ? 395 LYS B CG  1 
ATOM   7424  C CD  . LYS B 1 395 ? 56.374  43.650  -18.184 1.00 119.85 ? 395 LYS B CD  1 
ATOM   7425  C CE  . LYS B 1 395 ? 57.402  43.454  -17.099 1.00 122.79 ? 395 LYS B CE  1 
ATOM   7426  N NZ  . LYS B 1 395 ? 57.279  44.468  -16.042 1.00 126.77 ? 395 LYS B NZ  1 
ATOM   7427  N N   . ILE B 1 396 ? 57.001  46.462  -23.053 1.00 106.46 ? 396 ILE B N   1 
ATOM   7428  C CA  . ILE B 1 396 ? 56.778  46.398  -24.488 1.00 103.42 ? 396 ILE B CA  1 
ATOM   7429  C C   . ILE B 1 396 ? 56.062  45.089  -24.775 1.00 100.33 ? 396 ILE B C   1 
ATOM   7430  O O   . ILE B 1 396 ? 56.566  44.037  -24.409 1.00 99.90  ? 396 ILE B O   1 
ATOM   7431  C CB  . ILE B 1 396 ? 58.079  46.517  -25.305 1.00 102.90 ? 396 ILE B CB  1 
ATOM   7432  C CG1 . ILE B 1 396 ? 58.739  47.888  -25.097 1.00 106.32 ? 396 ILE B CG1 1 
ATOM   7433  C CG2 . ILE B 1 396 ? 57.795  46.243  -26.783 1.00 100.52 ? 396 ILE B CG2 1 
ATOM   7434  C CD1 . ILE B 1 396 ? 59.923  48.207  -25.997 1.00 105.63 ? 396 ILE B CD1 1 
ATOM   7435  N N   . ILE B 1 397 ? 54.894  45.184  -25.418 1.00 98.65  ? 397 ILE B N   1 
ATOM   7436  C CA  . ILE B 1 397 ? 54.054  44.031  -25.693 1.00 96.26  ? 397 ILE B CA  1 
ATOM   7437  C C   . ILE B 1 397 ? 54.008  43.757  -27.199 1.00 92.67  ? 397 ILE B C   1 
ATOM   7438  O O   . ILE B 1 397 ? 53.639  42.657  -27.607 1.00 90.04  ? 397 ILE B O   1 
ATOM   7439  C CB  . ILE B 1 397 ? 52.654  44.233  -25.078 1.00 98.77  ? 397 ILE B CB  1 
ATOM   7440  C CG1 . ILE B 1 397 ? 51.873  45.407  -25.699 1.00 99.24  ? 397 ILE B CG1 1 
ATOM   7441  C CG2 . ILE B 1 397 ? 52.757  44.372  -23.557 1.00 101.55 ? 397 ILE B CG2 1 
ATOM   7442  C CD1 . ILE B 1 397 ? 50.425  45.485  -25.249 1.00 100.23 ? 397 ILE B CD1 1 
ATOM   7443  N N   . LYS B 1 398 ? 54.395  44.747  -28.018 1.00 92.03  ? 398 LYS B N   1 
ATOM   7444  C CA  . LYS B 1 398 ? 54.429  44.589  -29.464 1.00 89.14  ? 398 LYS B CA  1 
ATOM   7445  C C   . LYS B 1 398 ? 55.475  45.514  -30.081 1.00 88.99  ? 398 LYS B C   1 
ATOM   7446  O O   . LYS B 1 398 ? 55.583  46.688  -29.716 1.00 90.54  ? 398 LYS B O   1 
ATOM   7447  C CB  . LYS B 1 398 ? 53.060  44.902  -30.078 1.00 88.52  ? 398 LYS B CB  1 
ATOM   7448  C CG  . LYS B 1 398 ? 52.984  44.825  -31.602 1.00 86.66  ? 398 LYS B CG  1 
ATOM   7449  C CD  . LYS B 1 398 ? 51.564  44.966  -32.140 1.00 86.71  ? 398 LYS B CD  1 
ATOM   7450  C CE  . LYS B 1 398 ? 51.412  44.595  -33.583 1.00 85.09  ? 398 LYS B CE  1 
ATOM   7451  N NZ  . LYS B 1 398 ? 51.954  45.581  -34.514 1.00 85.45  ? 398 LYS B NZ  1 
ATOM   7452  N N   . ASN B 1 399 ? 56.239  44.956  -31.026 1.00 86.82  ? 399 ASN B N   1 
ATOM   7453  C CA  . ASN B 1 399 ? 57.027  45.742  -31.958 1.00 86.75  ? 399 ASN B CA  1 
ATOM   7454  C C   . ASN B 1 399 ? 56.444  45.581  -33.355 1.00 85.14  ? 399 ASN B C   1 
ATOM   7455  O O   . ASN B 1 399 ? 56.081  44.476  -33.752 1.00 83.98  ? 399 ASN B O   1 
ATOM   7456  C CB  . ASN B 1 399 ? 58.494  45.327  -32.010 1.00 85.88  ? 399 ASN B CB  1 
ATOM   7457  C CG  . ASN B 1 399 ? 59.230  45.706  -30.751 1.00 87.93  ? 399 ASN B CG  1 
ATOM   7458  O OD1 . ASN B 1 399 ? 59.449  46.901  -30.501 1.00 89.92  ? 399 ASN B OD1 1 
ATOM   7459  N ND2 . ASN B 1 399 ? 59.635  44.710  -29.972 1.00 87.67  ? 399 ASN B ND2 1 
ATOM   7460  N N   . GLU B 1 400 ? 56.357  46.698  -34.080 1.00 85.60  ? 400 GLU B N   1 
ATOM   7461  C CA  . GLU B 1 400 ? 56.227  46.663  -35.526 1.00 84.01  ? 400 GLU B CA  1 
ATOM   7462  C C   . GLU B 1 400 ? 57.043  47.813  -36.087 1.00 84.44  ? 400 GLU B C   1 
ATOM   7463  O O   . GLU B 1 400 ? 57.200  48.837  -35.436 1.00 86.74  ? 400 GLU B O   1 
ATOM   7464  C CB  . GLU B 1 400 ? 54.773  46.750  -35.988 1.00 84.14  ? 400 GLU B CB  1 
ATOM   7465  C CG  . GLU B 1 400 ? 54.551  46.470  -37.474 1.00 82.99  ? 400 GLU B CG  1 
ATOM   7466  C CD  . GLU B 1 400 ? 53.094  46.163  -37.847 1.00 82.91  ? 400 GLU B CD  1 
ATOM   7467  O OE1 . GLU B 1 400 ? 52.158  46.588  -37.126 1.00 84.25  ? 400 GLU B OE1 1 
ATOM   7468  O OE2 . GLU B 1 400 ? 52.875  45.460  -38.864 1.00 81.74  ? 400 GLU B OE2 1 
ATOM   7469  N N   . SER B 1 401 ? 57.595  47.596  -37.275 1.00 82.72  ? 401 SER B N   1 
ATOM   7470  C CA  . SER B 1 401 ? 58.295  48.633  -38.001 1.00 83.25  ? 401 SER B CA  1 
ATOM   7471  C C   . SER B 1 401 ? 57.403  49.061  -39.158 1.00 83.12  ? 401 SER B C   1 
ATOM   7472  O O   . SER B 1 401 ? 56.525  48.302  -39.566 1.00 81.85  ? 401 SER B O   1 
ATOM   7473  C CB  . SER B 1 401 ? 59.656  48.157  -38.466 1.00 82.29  ? 401 SER B CB  1 
ATOM   7474  O OG  . SER B 1 401 ? 60.454  47.707  -37.376 1.00 82.28  ? 401 SER B OG  1 
ATOM   7475  N N   . ILE B 1 402 ? 57.591  50.302  -39.610 1.00 85.18  ? 402 ILE B N   1 
ATOM   7476  C CA  . ILE B 1 402 ? 56.955  50.810  -40.812 1.00 85.79  ? 402 ILE B CA  1 
ATOM   7477  C C   . ILE B 1 402 ? 58.061  51.459  -41.634 1.00 87.28  ? 402 ILE B C   1 
ATOM   7478  O O   . ILE B 1 402 ? 58.749  52.355  -41.145 1.00 89.03  ? 402 ILE B O   1 
ATOM   7479  C CB  . ILE B 1 402 ? 55.806  51.798  -40.493 1.00 87.43  ? 402 ILE B CB  1 
ATOM   7480  C CG1 . ILE B 1 402 ? 54.657  51.148  -39.671 1.00 86.41  ? 402 ILE B CG1 1 
ATOM   7481  C CG2 . ILE B 1 402 ? 55.269  52.451  -41.770 1.00 87.72  ? 402 ILE B CG2 1 
ATOM   7482  C CD1 . ILE B 1 402 ? 53.842  50.104  -40.418 1.00 83.93  ? 402 ILE B CD1 1 
ATOM   7483  N N   . ASN B 1 403 ? 58.241  50.969  -42.864 1.00 86.87  ? 403 ASN B N   1 
ATOM   7484  C CA  . ASN B 1 403 ? 59.299  51.456  -43.730 1.00 88.65  ? 403 ASN B CA  1 
ATOM   7485  C C   . ASN B 1 403 ? 58.721  52.469  -44.707 1.00 89.94  ? 403 ASN B C   1 
ATOM   7486  O O   . ASN B 1 403 ? 57.798  52.151  -45.450 1.00 88.48  ? 403 ASN B O   1 
ATOM   7487  C CB  . ASN B 1 403 ? 59.995  50.320  -44.472 1.00 87.69  ? 403 ASN B CB  1 
ATOM   7488  C CG  . ASN B 1 403 ? 60.902  49.531  -43.562 1.00 87.56  ? 403 ASN B CG  1 
ATOM   7489  O OD1 . ASN B 1 403 ? 61.982  50.010  -43.198 1.00 89.48  ? 403 ASN B OD1 1 
ATOM   7490  N ND2 . ASN B 1 403 ? 60.487  48.333  -43.188 1.00 85.71  ? 403 ASN B ND2 1 
ATOM   7491  N N   . ILE B 1 404 ? 59.299  53.675  -44.689 1.00 93.15  ? 404 ILE B N   1 
ATOM   7492  C CA  . ILE B 1 404 ? 58.937  54.749  -45.596 1.00 94.44  ? 404 ILE B CA  1 
ATOM   7493  C C   . ILE B 1 404 ? 60.201  55.235  -46.303 1.00 95.24  ? 404 ILE B C   1 
ATOM   7494  O O   . ILE B 1 404 ? 61.291  55.173  -45.747 1.00 94.00  ? 404 ILE B O   1 
ATOM   7495  C CB  . ILE B 1 404 ? 58.244  55.883  -44.820 1.00 96.80  ? 404 ILE B CB  1 
ATOM   7496  C CG1 . ILE B 1 404 ? 59.264  56.683  -43.964 1.00 99.13  ? 404 ILE B CG1 1 
ATOM   7497  C CG2 . ILE B 1 404 ? 57.079  55.329  -43.995 1.00 95.37  ? 404 ILE B CG2 1 
ATOM   7498  C CD1 . ILE B 1 404 ? 58.683  57.873  -43.218 1.00 101.52 ? 404 ILE B CD1 1 
ATOM   7499  N N   . LEU B 1 405 ? 60.015  55.670  -47.549 1.00 96.87  ? 405 LEU B N   1 
ATOM   7500  C CA  . LEU B 1 405 ? 60.971  56.484  -48.265 1.00 100.81 ? 405 LEU B CA  1 
ATOM   7501  C C   . LEU B 1 405 ? 60.493  57.934  -48.259 1.00 105.46 ? 405 LEU B C   1 
ATOM   7502  O O   . LEU B 1 405 ? 59.479  58.251  -48.880 1.00 106.60 ? 405 LEU B O   1 
ATOM   7503  C CB  . LEU B 1 405 ? 61.040  55.934  -49.684 1.00 100.57 ? 405 LEU B CB  1 
ATOM   7504  C CG  . LEU B 1 405 ? 62.003  56.673  -50.616 1.00 104.16 ? 405 LEU B CG  1 
ATOM   7505  C CD1 . LEU B 1 405 ? 63.445  56.477  -50.155 1.00 105.04 ? 405 LEU B CD1 1 
ATOM   7506  C CD2 . LEU B 1 405 ? 61.812  56.221  -52.052 1.00 103.84 ? 405 LEU B CD2 1 
ATOM   7507  N N   . ALA B 1 406 ? 61.244  58.822  -47.596 1.00 109.15 ? 406 ALA B N   1 
ATOM   7508  C CA  . ALA B 1 406 ? 60.761  60.169  -47.330 1.00 112.82 ? 406 ALA B CA  1 
ATOM   7509  C C   . ALA B 1 406 ? 61.726  61.234  -47.865 1.00 117.29 ? 406 ALA B C   1 
ATOM   7510  O O   . ALA B 1 406 ? 62.921  60.981  -48.045 1.00 116.94 ? 406 ALA B O   1 
ATOM   7511  C CB  . ALA B 1 406 ? 60.529  60.320  -45.840 1.00 113.33 ? 406 ALA B CB  1 
ATOM   7512  N N   . SER B 1 407 ? 61.168  62.429  -48.114 1.00 119.76 ? 407 SER B N   1 
ATOM   7513  C CA  . SER B 1 407 ? 61.913  63.601  -48.538 1.00 123.69 ? 407 SER B CA  1 
ATOM   7514  C C   . SER B 1 407 ? 61.083  64.838  -48.202 1.00 128.63 ? 407 SER B C   1 
ATOM   7515  O O   . SER B 1 407 ? 59.862  64.740  -48.070 1.00 129.03 ? 407 SER B O   1 
ATOM   7516  C CB  . SER B 1 407 ? 62.244  63.557  -50.013 1.00 123.35 ? 407 SER B CB  1 
ATOM   7517  O OG  . SER B 1 407 ? 62.881  64.756  -50.447 1.00 127.41 ? 407 SER B OG  1 
ATOM   7518  N N   . LYS B 1 408 ? 61.754  65.990  -48.061 1.00 131.65 ? 408 LYS B N   1 
ATOM   7519  C CA  . LYS B 1 408 ? 61.074  67.244  -47.789 1.00 134.75 ? 408 LYS B CA  1 
ATOM   7520  C C   . LYS B 1 408 ? 60.409  67.738  -49.067 1.00 135.75 ? 408 LYS B C   1 
ATOM   7521  O O   . LYS B 1 408 ? 59.422  68.464  -49.010 1.00 136.43 ? 408 LYS B O   1 
ATOM   7522  C CB  . LYS B 1 408 ? 62.047  68.293  -47.241 1.00 138.92 ? 408 LYS B CB  1 
ATOM   7523  C CG  . LYS B 1 408 ? 62.659  67.889  -45.915 1.00 138.67 ? 408 LYS B CG  1 
ATOM   7524  C CD  . LYS B 1 408 ? 63.539  68.943  -45.266 1.00 142.54 ? 408 LYS B CD  1 
ATOM   7525  C CE  . LYS B 1 408 ? 64.129  68.410  -44.000 1.00 142.57 ? 408 LYS B CE  1 
ATOM   7526  N NZ  . LYS B 1 408 ? 65.229  69.239  -43.500 1.00 147.04 ? 408 LYS B NZ  1 
ATOM   7527  N N   . THR B 1 409 ? 60.963  67.335  -50.214 1.00 135.81 ? 409 THR B N   1 
ATOM   7528  C CA  . THR B 1 409 ? 60.419  67.723  -51.503 1.00 137.19 ? 409 THR B CA  1 
ATOM   7529  C C   . THR B 1 409 ? 60.271  66.485  -52.386 1.00 134.53 ? 409 THR B C   1 
ATOM   7530  O O   . THR B 1 409 ? 60.812  65.420  -52.082 1.00 130.42 ? 409 THR B O   1 
ATOM   7531  C CB  . THR B 1 409 ? 61.313  68.791  -52.133 1.00 140.59 ? 409 THR B CB  1 
ATOM   7532  O OG1 . THR B 1 409 ? 60.597  69.087  -53.325 1.00 142.51 ? 409 THR B OG1 1 
ATOM   7533  C CG2 . THR B 1 409 ? 62.728  68.329  -52.439 1.00 139.18 ? 409 THR B CG2 1 
ATOM   7534  N N   . ALA B 1 410 ? 59.516  66.656  -53.481 1.00 135.87 ? 410 ALA B N   1 
ATOM   7535  C CA  . ALA B 1 410 ? 59.244  65.583  -54.424 1.00 133.44 ? 410 ALA B CA  1 
ATOM   7536  C C   . ALA B 1 410 ? 60.542  65.161  -55.101 1.00 133.63 ? 410 ALA B C   1 
ATOM   7537  O O   . ALA B 1 410 ? 61.469  65.962  -55.220 1.00 136.58 ? 410 ALA B O   1 
ATOM   7538  C CB  . ALA B 1 410 ? 58.224  66.035  -55.444 1.00 135.08 ? 410 ALA B CB  1 
ATOM   7539  N N   . PHE B 1 411 ? 60.592  63.894  -55.533 1.00 130.27 ? 411 PHE B N   1 
ATOM   7540  C CA  . PHE B 1 411 ? 61.748  63.366  -56.241 1.00 128.85 ? 411 PHE B CA  1 
ATOM   7541  C C   . PHE B 1 411 ? 61.260  62.400  -57.315 1.00 124.59 ? 411 PHE B C   1 
ATOM   7542  O O   . PHE B 1 411 ? 60.164  61.853  -57.207 1.00 123.60 ? 411 PHE B O   1 
ATOM   7543  C CB  . PHE B 1 411 ? 62.731  62.715  -55.261 1.00 128.18 ? 411 PHE B CB  1 
ATOM   7544  C CG  . PHE B 1 411 ? 62.095  61.727  -54.292 1.00 125.25 ? 411 PHE B CG  1 
ATOM   7545  C CD1 . PHE B 1 411 ? 61.534  62.165  -53.096 1.00 125.89 ? 411 PHE B CD1 1 
ATOM   7546  C CD2 . PHE B 1 411 ? 62.039  60.367  -54.589 1.00 122.07 ? 411 PHE B CD2 1 
ATOM   7547  C CE1 . PHE B 1 411 ? 60.937  61.267  -52.222 1.00 123.51 ? 411 PHE B CE1 1 
ATOM   7548  C CE2 . PHE B 1 411 ? 61.431  59.477  -53.715 1.00 118.52 ? 411 PHE B CE2 1 
ATOM   7549  C CZ  . PHE B 1 411 ? 60.889  59.927  -52.532 1.00 119.48 ? 411 PHE B CZ  1 
ATOM   7550  N N   . GLU B 1 412 ? 62.083  62.214  -58.350 1.00 123.44 ? 412 GLU B N   1 
ATOM   7551  C CA  . GLU B 1 412 ? 61.782  61.252  -59.393 1.00 121.15 ? 412 GLU B CA  1 
ATOM   7552  C C   . GLU B 1 412 ? 62.016  59.844  -58.856 1.00 115.95 ? 412 GLU B C   1 
ATOM   7553  O O   . GLU B 1 412 ? 62.980  59.613  -58.126 1.00 115.09 ? 412 GLU B O   1 
ATOM   7554  C CB  . GLU B 1 412 ? 62.621  61.524  -60.635 1.00 125.09 ? 412 GLU B CB  1 
ATOM   7555  C CG  . GLU B 1 412 ? 62.224  62.829  -61.315 1.00 131.17 ? 412 GLU B CG  1 
ATOM   7556  C CD  . GLU B 1 412 ? 63.125  63.296  -62.446 1.00 137.73 ? 412 GLU B CD  1 
ATOM   7557  O OE1 . GLU B 1 412 ? 64.374  63.297  -62.282 1.00 139.76 ? 412 GLU B OE1 1 
ATOM   7558  O OE2 . GLU B 1 412 ? 62.555  63.707  -63.487 1.00 143.21 ? 412 GLU B OE2 1 
ATOM   7559  N N   . LEU B 1 413 ? 61.077  58.946  -59.192 1.00 111.69 ? 413 LEU B N   1 
ATOM   7560  C CA  . LEU B 1 413 ? 61.216  57.504  -59.028 1.00 106.73 ? 413 LEU B CA  1 
ATOM   7561  C C   . LEU B 1 413 ? 61.343  56.876  -60.410 1.00 104.26 ? 413 LEU B C   1 
ATOM   7562  O O   . LEU B 1 413 ? 60.904  57.459  -61.393 1.00 105.49 ? 413 LEU B O   1 
ATOM   7563  C CB  . LEU B 1 413 ? 59.991  56.900  -58.342 1.00 104.86 ? 413 LEU B CB  1 
ATOM   7564  C CG  . LEU B 1 413 ? 59.624  57.424  -56.952 1.00 105.50 ? 413 LEU B CG  1 
ATOM   7565  C CD1 . LEU B 1 413 ? 58.280  56.867  -56.523 1.00 103.19 ? 413 LEU B CD1 1 
ATOM   7566  C CD2 . LEU B 1 413 ? 60.688  57.069  -55.938 1.00 105.37 ? 413 LEU B CD2 1 
ATOM   7567  N N   . PRO B 1 414 ? 61.874  55.644  -60.538 1.00 101.23 ? 414 PRO B N   1 
ATOM   7568  C CA  . PRO B 1 414 ? 61.759  54.912  -61.800 1.00 100.03 ? 414 PRO B CA  1 
ATOM   7569  C C   . PRO B 1 414 ? 60.306  54.466  -61.970 1.00 98.09  ? 414 PRO B C   1 
ATOM   7570  O O   . PRO B 1 414 ? 59.619  54.225  -60.976 1.00 96.45  ? 414 PRO B O   1 
ATOM   7571  C CB  . PRO B 1 414 ? 62.751  53.746  -61.609 1.00 98.08  ? 414 PRO B CB  1 
ATOM   7572  C CG  . PRO B 1 414 ? 62.766  53.508  -60.103 1.00 96.84  ? 414 PRO B CG  1 
ATOM   7573  C CD  . PRO B 1 414 ? 62.597  54.892  -59.494 1.00 99.64  ? 414 PRO B CD  1 
ATOM   7574  N N   . GLU B 1 415 ? 59.829  54.367  -63.220 1.00 98.01  ? 415 GLU B N   1 
ATOM   7575  C CA  . GLU B 1 415 ? 58.473  53.890  -63.463 1.00 96.27  ? 415 GLU B CA  1 
ATOM   7576  C C   . GLU B 1 415 ? 58.448  52.804  -64.537 1.00 95.43  ? 415 GLU B C   1 
ATOM   7577  O O   . GLU B 1 415 ? 59.379  52.633  -65.322 1.00 96.23  ? 415 GLU B O   1 
ATOM   7578  C CB  . GLU B 1 415 ? 57.515  55.014  -63.843 1.00 97.77  ? 415 GLU B CB  1 
ATOM   7579  C CG  . GLU B 1 415 ? 57.826  55.670  -65.183 1.00 99.55  ? 415 GLU B CG  1 
ATOM   7580  C CD  . GLU B 1 415 ? 56.820  56.749  -65.521 1.00 101.02 ? 415 GLU B CD  1 
ATOM   7581  O OE1 . GLU B 1 415 ? 55.755  56.811  -64.862 1.00 99.33  ? 415 GLU B OE1 1 
ATOM   7582  O OE2 . GLU B 1 415 ? 57.134  57.526  -66.446 1.00 103.37 ? 415 GLU B OE2 1 
ATOM   7583  N N   . LEU B 1 416 ? 57.349  52.053  -64.532 1.00 94.02  ? 416 LEU B N   1 
ATOM   7584  C CA  . LEU B 1 416 ? 57.178  50.926  -65.427 1.00 92.86  ? 416 LEU B CA  1 
ATOM   7585  C C   . LEU B 1 416 ? 55.793  51.077  -66.023 1.00 92.40  ? 416 LEU B C   1 
ATOM   7586  O O   . LEU B 1 416 ? 54.837  51.363  -65.293 1.00 91.72  ? 416 LEU B O   1 
ATOM   7587  C CB  . LEU B 1 416 ? 57.350  49.605  -64.668 1.00 91.09  ? 416 LEU B CB  1 
ATOM   7588  C CG  . LEU B 1 416 ? 57.491  48.321  -65.498 1.00 90.41  ? 416 LEU B CG  1 
ATOM   7589  C CD1 . LEU B 1 416 ? 57.893  47.195  -64.584 1.00 88.42  ? 416 LEU B CD1 1 
ATOM   7590  C CD2 . LEU B 1 416 ? 56.214  47.913  -66.221 1.00 90.58  ? 416 LEU B CD2 1 
ATOM   7591  N N   . THR B 1 417 ? 55.732  50.961  -67.353 1.00 92.94  ? 417 THR B N   1 
ATOM   7592  C CA  . THR B 1 417 ? 54.459  51.000  -68.059 1.00 92.95  ? 417 THR B CA  1 
ATOM   7593  C C   . THR B 1 417 ? 54.472  49.922  -69.144 1.00 92.60  ? 417 THR B C   1 
ATOM   7594  O O   . THR B 1 417 ? 55.542  49.507  -69.614 1.00 91.41  ? 417 THR B O   1 
ATOM   7595  C CB  . THR B 1 417 ? 54.191  52.400  -68.608 1.00 94.53  ? 417 THR B CB  1 
ATOM   7596  O OG1 . THR B 1 417 ? 55.168  52.606  -69.624 1.00 95.92  ? 417 THR B OG1 1 
ATOM   7597  C CG2 . THR B 1 417 ? 54.280  53.464  -67.529 1.00 95.20  ? 417 THR B CG2 1 
ATOM   7598  N N   . ILE B 1 418 ? 53.262  49.447  -69.486 1.00 92.11  ? 418 ILE B N   1 
ATOM   7599  C CA  . ILE B 1 418 ? 53.115  48.365  -70.445 1.00 92.01  ? 418 ILE B CA  1 
ATOM   7600  C C   . ILE B 1 418 ? 52.135  48.786  -71.529 1.00 93.88  ? 418 ILE B C   1 
ATOM   7601  O O   . ILE B 1 418 ? 51.172  49.501  -71.266 1.00 96.81  ? 418 ILE B O   1 
ATOM   7602  C CB  . ILE B 1 418 ? 52.707  47.035  -69.777 1.00 89.77  ? 418 ILE B CB  1 
ATOM   7603  C CG1 . ILE B 1 418 ? 51.324  47.058  -69.167 1.00 88.86  ? 418 ILE B CG1 1 
ATOM   7604  C CG2 . ILE B 1 418 ? 53.753  46.610  -68.745 1.00 89.35  ? 418 ILE B CG2 1 
ATOM   7605  C CD1 . ILE B 1 418 ? 50.955  45.773  -68.455 1.00 86.25  ? 418 ILE B CD1 1 
ATOM   7606  N N   . GLU B 1 419 ? 52.432  48.350  -72.752 1.00 94.25  ? 419 GLU B N   1 
ATOM   7607  C CA  . GLU B 1 419 ? 51.525  48.473  -73.871 1.00 95.62  ? 419 GLU B CA  1 
ATOM   7608  C C   . GLU B 1 419 ? 51.180  47.074  -74.343 1.00 94.41  ? 419 GLU B C   1 
ATOM   7609  O O   . GLU B 1 419 ? 52.032  46.331  -74.815 1.00 96.17  ? 419 GLU B O   1 
ATOM   7610  C CB  . GLU B 1 419 ? 52.175  49.209  -75.032 1.00 98.50  ? 419 GLU B CB  1 
ATOM   7611  C CG  . GLU B 1 419 ? 52.573  50.637  -74.693 1.00 100.50 ? 419 GLU B CG  1 
ATOM   7612  C CD  . GLU B 1 419 ? 53.144  51.269  -75.937 1.00 103.64 ? 419 GLU B CD  1 
ATOM   7613  O OE1 . GLU B 1 419 ? 53.800  50.493  -76.671 1.00 103.78 ? 419 GLU B OE1 1 
ATOM   7614  O OE2 . GLU B 1 419 ? 52.955  52.486  -76.162 1.00 106.02 ? 419 GLU B OE2 1 
ATOM   7615  N N   . VAL B 1 420 ? 49.921  46.716  -74.208 1.00 93.02  ? 420 VAL B N   1 
ATOM   7616  C CA  . VAL B 1 420 ? 49.519  45.362  -74.505 1.00 92.09  ? 420 VAL B CA  1 
ATOM   7617  C C   . VAL B 1 420 ? 48.943  45.306  -75.916 1.00 94.67  ? 420 VAL B C   1 
ATOM   7618  O O   . VAL B 1 420 ? 48.561  46.331  -76.475 1.00 97.62  ? 420 VAL B O   1 
ATOM   7619  C CB  . VAL B 1 420 ? 48.521  44.978  -73.401 1.00 90.06  ? 420 VAL B CB  1 
ATOM   7620  C CG1 . VAL B 1 420 ? 47.953  43.573  -73.583 1.00 88.46  ? 420 VAL B CG1 1 
ATOM   7621  C CG2 . VAL B 1 420 ? 49.160  45.165  -72.023 1.00 88.58  ? 420 VAL B CG2 1 
ATOM   7622  N N   . THR B 1 421 ? 48.946  44.101  -76.497 1.00 94.70  ? 421 THR B N   1 
ATOM   7623  C CA  . THR B 1 421 ? 48.248  43.810  -77.739 1.00 96.11  ? 421 THR B CA  1 
ATOM   7624  C C   . THR B 1 421 ? 47.396  42.561  -77.501 1.00 95.38  ? 421 THR B C   1 
ATOM   7625  O O   . THR B 1 421 ? 47.820  41.647  -76.802 1.00 95.92  ? 421 THR B O   1 
ATOM   7626  C CB  . THR B 1 421 ? 49.249  43.623  -78.884 1.00 97.07  ? 421 THR B CB  1 
ATOM   7627  O OG1 . THR B 1 421 ? 50.028  44.813  -79.005 1.00 98.38  ? 421 THR B OG1 1 
ATOM   7628  C CG2 . THR B 1 421 ? 48.571  43.349  -80.216 1.00 98.44  ? 421 THR B CG2 1 
ATOM   7629  N N   . PRO B 1 422 ? 46.140  42.490  -77.985 1.00 95.38  ? 422 PRO B N   1 
ATOM   7630  C CA  . PRO B 1 422 ? 45.423  43.667  -78.469 1.00 96.93  ? 422 PRO B CA  1 
ATOM   7631  C C   . PRO B 1 422 ? 45.116  44.550  -77.264 1.00 95.91  ? 422 PRO B C   1 
ATOM   7632  O O   . PRO B 1 422 ? 44.882  44.055  -76.160 1.00 93.47  ? 422 PRO B O   1 
ATOM   7633  C CB  . PRO B 1 422 ? 44.180  43.081  -79.137 1.00 97.78  ? 422 PRO B CB  1 
ATOM   7634  C CG  . PRO B 1 422 ? 44.514  41.616  -79.321 1.00 96.90  ? 422 PRO B CG  1 
ATOM   7635  C CD  . PRO B 1 422 ? 45.370  41.252  -78.122 1.00 94.59  ? 422 PRO B CD  1 
ATOM   7636  N N   . GLU B 1 423 ? 45.132  45.862  -77.492 1.00 97.71  ? 423 GLU B N   1 
ATOM   7637  C CA  . GLU B 1 423 ? 44.932  46.826  -76.425 1.00 98.00  ? 423 GLU B CA  1 
ATOM   7638  C C   . GLU B 1 423 ? 43.491  46.837  -75.884 1.00 98.02  ? 423 GLU B C   1 
ATOM   7639  O O   . GLU B 1 423 ? 43.298  47.080  -74.691 1.00 96.81  ? 423 GLU B O   1 
ATOM   7640  C CB  . GLU B 1 423 ? 45.335  48.198  -76.961 1.00 100.29 ? 423 GLU B CB  1 
ATOM   7641  C CG  . GLU B 1 423 ? 45.268  49.292  -75.902 1.00 99.97  ? 423 GLU B CG  1 
ATOM   7642  C CD  . GLU B 1 423 ? 45.329  50.690  -76.464 1.00 102.10 ? 423 GLU B CD  1 
ATOM   7643  O OE1 . GLU B 1 423 ? 45.248  50.882  -77.693 1.00 103.82 ? 423 GLU B OE1 1 
ATOM   7644  O OE2 . GLU B 1 423 ? 45.474  51.588  -75.625 1.00 102.07 ? 423 GLU B OE2 1 
ATOM   7645  N N   . LYS B 1 424 ? 42.470  46.603  -76.728 1.00 99.23  ? 424 LYS B N   1 
ATOM   7646  C CA  . LYS B 1 424 ? 41.098  46.893  -76.323 1.00 100.14 ? 424 LYS B CA  1 
ATOM   7647  C C   . LYS B 1 424 ? 40.210  45.653  -76.320 1.00 98.41  ? 424 LYS B C   1 
ATOM   7648  O O   . LYS B 1 424 ? 39.445  45.480  -75.370 1.00 97.94  ? 424 LYS B O   1 
ATOM   7649  C CB  . LYS B 1 424 ? 40.459  47.977  -77.199 1.00 104.38 ? 424 LYS B CB  1 
ATOM   7650  C CG  . LYS B 1 424 ? 41.209  49.322  -77.250 1.00 107.69 ? 424 LYS B CG  1 
ATOM   7651  C CD  . LYS B 1 424 ? 40.428  50.469  -77.891 1.00 111.78 ? 424 LYS B CD  1 
ATOM   7652  C CE  . LYS B 1 424 ? 41.258  51.663  -78.308 1.00 115.41 ? 424 LYS B CE  1 
ATOM   7653  N NZ  . LYS B 1 424 ? 41.757  52.515  -77.222 1.00 115.68 ? 424 LYS B NZ  1 
ATOM   7654  N N   . ASP B 1 425 ? 40.283  44.829  -77.383 1.00 97.90  ? 425 ASP B N   1 
ATOM   7655  C CA  . ASP B 1 425 ? 39.358  43.716  -77.590 1.00 96.63  ? 425 ASP B CA  1 
ATOM   7656  C C   . ASP B 1 425 ? 40.112  42.462  -78.031 1.00 94.68  ? 425 ASP B C   1 
ATOM   7657  O O   . ASP B 1 425 ? 40.741  42.469  -79.087 1.00 96.04  ? 425 ASP B O   1 
ATOM   7658  C CB  . ASP B 1 425 ? 38.299  44.060  -78.631 1.00 99.20  ? 425 ASP B CB  1 
ATOM   7659  C CG  . ASP B 1 425 ? 37.145  43.071  -78.794 1.00 99.50  ? 425 ASP B CG  1 
ATOM   7660  O OD1 . ASP B 1 425 ? 37.226  41.971  -78.212 1.00 98.08  ? 425 ASP B OD1 1 
ATOM   7661  O OD2 . ASP B 1 425 ? 36.145  43.412  -79.480 1.00 101.05 ? 425 ASP B OD2 1 
ATOM   7662  N N   . LEU B 1 426 ? 39.980  41.370  -77.261 1.00 91.66  ? 426 LEU B N   1 
ATOM   7663  C CA  . LEU B 1 426 ? 40.732  40.142  -77.499 1.00 90.36  ? 426 LEU B CA  1 
ATOM   7664  C C   . LEU B 1 426 ? 40.266  39.403  -78.754 1.00 92.12  ? 426 LEU B C   1 
ATOM   7665  O O   . LEU B 1 426 ? 40.818  38.360  -79.091 1.00 91.60  ? 426 LEU B O   1 
ATOM   7666  C CB  . LEU B 1 426 ? 40.630  39.199  -76.303 1.00 87.78  ? 426 LEU B CB  1 
ATOM   7667  C CG  . LEU B 1 426 ? 41.113  39.738  -74.955 1.00 86.04  ? 426 LEU B CG  1 
ATOM   7668  C CD1 . LEU B 1 426 ? 40.992  38.618  -73.935 1.00 84.21  ? 426 LEU B CD1 1 
ATOM   7669  C CD2 . LEU B 1 426 ? 42.523  40.273  -74.984 1.00 85.71  ? 426 LEU B CD2 1 
ATOM   7670  N N   . ASN B 1 427 ? 39.227  39.895  -79.429 1.00 94.78  ? 427 ASN B N   1 
ATOM   7671  C CA  . ASN B 1 427 ? 38.770  39.262  -80.655 1.00 97.16  ? 427 ASN B CA  1 
ATOM   7672  C C   . ASN B 1 427 ? 39.671  39.701  -81.807 1.00 99.50  ? 427 ASN B C   1 
ATOM   7673  O O   . ASN B 1 427 ? 39.603  39.117  -82.882 1.00 101.27 ? 427 ASN B O   1 
ATOM   7674  C CB  . ASN B 1 427 ? 37.305  39.565  -80.975 1.00 98.67  ? 427 ASN B CB  1 
ATOM   7675  C CG  . ASN B 1 427 ? 36.303  38.806  -80.127 1.00 97.42  ? 427 ASN B CG  1 
ATOM   7676  O OD1 . ASN B 1 427 ? 36.480  37.607  -79.884 1.00 96.08  ? 427 ASN B OD1 1 
ATOM   7677  N ND2 . ASN B 1 427 ? 35.235  39.469  -79.691 1.00 97.50  ? 427 ASN B ND2 1 
ATOM   7678  N N   . GLU B 1 428 ? 40.502  40.730  -81.576 1.00 100.41 ? 428 GLU B N   1 
ATOM   7679  C CA  . GLU B 1 428 ? 41.309  41.346  -82.624 1.00 103.34 ? 428 GLU B CA  1 
ATOM   7680  C C   . GLU B 1 428 ? 42.502  40.473  -83.029 1.00 103.89 ? 428 GLU B C   1 
ATOM   7681  O O   . GLU B 1 428 ? 43.109  40.740  -84.063 1.00 106.85 ? 428 GLU B O   1 
ATOM   7682  C CB  . GLU B 1 428 ? 41.855  42.724  -82.230 1.00 103.95 ? 428 GLU B CB  1 
ATOM   7683  C CG  . GLU B 1 428 ? 40.827  43.850  -82.341 1.00 106.19 ? 428 GLU B CG  1 
ATOM   7684  C CD  . GLU B 1 428 ? 41.347  45.285  -82.382 1.00 107.60 ? 428 GLU B CD  1 
ATOM   7685  O OE1 . GLU B 1 428 ? 42.572  45.518  -82.251 1.00 107.11 ? 428 GLU B OE1 1 
ATOM   7686  O OE2 . GLU B 1 428 ? 40.488  46.182  -82.559 1.00 108.77 ? 428 GLU B OE2 1 
ATOM   7687  N N   . GLY B 1 429 ? 42.861  39.465  -82.218 1.00 101.39 ? 429 GLY B N   1 
ATOM   7688  C CA  . GLY B 1 429 ? 44.013  38.630  -82.512 1.00 101.07 ? 429 GLY B CA  1 
ATOM   7689  C C   . GLY B 1 429 ? 44.057  37.390  -81.625 1.00 99.33  ? 429 GLY B C   1 
ATOM   7690  O O   . GLY B 1 429 ? 43.507  37.408  -80.528 1.00 98.15  ? 429 GLY B O   1 
ATOM   7691  N N   . LYS B 1 430 ? 44.734  36.339  -82.118 1.00 99.75  ? 430 LYS B N   1 
ATOM   7692  C CA  . LYS B 1 430 ? 44.889  35.077  -81.410 1.00 97.80  ? 430 LYS B CA  1 
ATOM   7693  C C   . LYS B 1 430 ? 46.176  35.078  -80.596 1.00 94.61  ? 430 LYS B C   1 
ATOM   7694  O O   . LYS B 1 430 ? 46.326  34.268  -79.685 1.00 92.87  ? 430 LYS B O   1 
ATOM   7695  C CB  . LYS B 1 430 ? 44.870  33.909  -82.402 1.00 100.62 ? 430 LYS B CB  1 
ATOM   7696  C CG  . LYS B 1 430 ? 43.485  33.650  -82.991 1.00 103.17 ? 430 LYS B CG  1 
ATOM   7697  C CD  . LYS B 1 430 ? 43.418  32.529  -84.019 1.00 106.00 ? 430 LYS B CD  1 
ATOM   7698  C CE  . LYS B 1 430 ? 42.067  32.472  -84.671 1.00 108.72 ? 430 LYS B CE  1 
ATOM   7699  N NZ  . LYS B 1 430 ? 42.112  31.667  -85.895 1.00 111.78 ? 430 LYS B NZ  1 
ATOM   7700  N N   . ILE B 1 431 ? 47.097  35.987  -80.928 1.00 93.66  ? 431 ILE B N   1 
ATOM   7701  C CA  . ILE B 1 431 ? 48.320  36.122  -80.164 1.00 91.50  ? 431 ILE B CA  1 
ATOM   7702  C C   . ILE B 1 431 ? 48.311  37.462  -79.452 1.00 90.07  ? 431 ILE B C   1 
ATOM   7703  O O   . ILE B 1 431 ? 47.790  38.421  -80.008 1.00 91.03  ? 431 ILE B O   1 
ATOM   7704  C CB  . ILE B 1 431 ? 49.523  36.019  -81.103 1.00 93.45  ? 431 ILE B CB  1 
ATOM   7705  C CG1 . ILE B 1 431 ? 49.515  34.717  -81.900 1.00 94.81  ? 431 ILE B CG1 1 
ATOM   7706  C CG2 . ILE B 1 431 ? 50.821  36.205  -80.324 1.00 92.68  ? 431 ILE B CG2 1 
ATOM   7707  C CD1 . ILE B 1 431 ? 49.529  33.461  -81.046 1.00 93.45  ? 431 ILE B CD1 1 
ATOM   7708  N N   . ALA B 1 432 ? 48.925  37.514  -78.260 1.00 87.98  ? 432 ALA B N   1 
ATOM   7709  C CA  . ALA B 1 432 ? 49.080  38.747  -77.490 1.00 87.63  ? 432 ALA B CA  1 
ATOM   7710  C C   . ALA B 1 432 ? 50.556  39.100  -77.270 1.00 87.64  ? 432 ALA B C   1 
ATOM   7711  O O   . ALA B 1 432 ? 51.430  38.255  -77.430 1.00 86.56  ? 432 ALA B O   1 
ATOM   7712  C CB  . ALA B 1 432 ? 48.382  38.607  -76.157 1.00 85.75  ? 432 ALA B CB  1 
ATOM   7713  N N   . SER B 1 433 ? 50.823  40.356  -76.872 1.00 88.40  ? 433 SER B N   1 
ATOM   7714  C CA  . SER B 1 433 ? 52.180  40.783  -76.546 1.00 88.83  ? 433 SER B CA  1 
ATOM   7715  C C   . SER B 1 433 ? 52.189  41.894  -75.494 1.00 89.01  ? 433 SER B C   1 
ATOM   7716  O O   . SER B 1 433 ? 51.447  42.871  -75.606 1.00 90.17  ? 433 SER B O   1 
ATOM   7717  C CB  . SER B 1 433 ? 52.979  41.199  -77.785 1.00 90.90  ? 433 SER B CB  1 
ATOM   7718  O OG  . SER B 1 433 ? 52.585  42.451  -78.334 1.00 92.25  ? 433 SER B OG  1 
ATOM   7719  N N   . ILE B 1 434 ? 53.088  41.747  -74.505 1.00 88.18  ? 434 ILE B N   1 
ATOM   7720  C CA  . ILE B 1 434 ? 53.331  42.762  -73.488 1.00 88.23  ? 434 ILE B CA  1 
ATOM   7721  C C   . ILE B 1 434 ? 54.696  43.413  -73.711 1.00 89.66  ? 434 ILE B C   1 
ATOM   7722  O O   . ILE B 1 434 ? 55.741  42.824  -73.414 1.00 88.67  ? 434 ILE B O   1 
ATOM   7723  C CB  . ILE B 1 434 ? 53.253  42.168  -72.074 1.00 86.05  ? 434 ILE B CB  1 
ATOM   7724  C CG1 . ILE B 1 434 ? 51.921  41.462  -71.837 1.00 85.10  ? 434 ILE B CG1 1 
ATOM   7725  C CG2 . ILE B 1 434 ? 53.531  43.260  -71.038 1.00 86.04  ? 434 ILE B CG2 1 
ATOM   7726  C CD1 . ILE B 1 434 ? 51.823  40.721  -70.514 1.00 83.25  ? 434 ILE B CD1 1 
ATOM   7727  N N   . LYS B 1 435 ? 54.657  44.655  -74.202 1.00 91.64  ? 435 LYS B N   1 
ATOM   7728  C CA  . LYS B 1 435 ? 55.845  45.471  -74.342 1.00 93.23  ? 435 LYS B CA  1 
ATOM   7729  C C   . LYS B 1 435 ? 56.061  46.197  -73.018 1.00 92.71  ? 435 LYS B C   1 
ATOM   7730  O O   . LYS B 1 435 ? 55.301  47.095  -72.670 1.00 92.96  ? 435 LYS B O   1 
ATOM   7731  C CB  . LYS B 1 435 ? 55.683  46.438  -75.521 1.00 96.23  ? 435 LYS B CB  1 
ATOM   7732  C CG  . LYS B 1 435 ? 55.569  45.809  -76.920 1.00 97.45  ? 435 LYS B CG  1 
ATOM   7733  C CD  . LYS B 1 435 ? 55.090  46.769  -78.015 1.00 100.10 ? 435 LYS B CD  1 
ATOM   7734  C CE  . LYS B 1 435 ? 55.214  46.268  -79.435 1.00 101.36 ? 435 LYS B CE  1 
ATOM   7735  N NZ  . LYS B 1 435 ? 54.736  44.889  -79.608 1.00 99.59  ? 435 LYS B NZ  1 
ATOM   7736  N N   . THR B 1 436 ? 57.109  45.798  -72.291 1.00 92.47  ? 436 THR B N   1 
ATOM   7737  C CA  . THR B 1 436 ? 57.453  46.406  -71.016 1.00 91.97  ? 436 THR B CA  1 
ATOM   7738  C C   . THR B 1 436 ? 58.463  47.534  -71.257 1.00 93.41  ? 436 THR B C   1 
ATOM   7739  O O   . THR B 1 436 ? 59.199  47.516  -72.239 1.00 93.65  ? 436 THR B O   1 
ATOM   7740  C CB  . THR B 1 436 ? 57.970  45.332  -70.056 1.00 90.50  ? 436 THR B CB  1 
ATOM   7741  O OG1 . THR B 1 436 ? 57.217  44.124  -70.202 1.00 89.66  ? 436 THR B OG1 1 
ATOM   7742  C CG2 . THR B 1 436 ? 57.868  45.787  -68.613 1.00 89.69  ? 436 THR B CG2 1 
ATOM   7743  N N   . LYS B 1 437 ? 58.437  48.542  -70.374 1.00 94.09  ? 437 LYS B N   1 
ATOM   7744  C CA  . LYS B 1 437 ? 59.093  49.822  -70.594 1.00 96.68  ? 437 LYS B CA  1 
ATOM   7745  C C   . LYS B 1 437 ? 59.402  50.446  -69.235 1.00 96.75  ? 437 LYS B C   1 
ATOM   7746  O O   . LYS B 1 437 ? 58.493  50.960  -68.568 1.00 96.23  ? 437 LYS B O   1 
ATOM   7747  C CB  . LYS B 1 437 ? 58.241  50.808  -71.408 1.00 98.46  ? 437 LYS B CB  1 
ATOM   7748  C CG  . LYS B 1 437 ? 58.924  52.149  -71.630 1.00 101.57 ? 437 LYS B CG  1 
ATOM   7749  C CD  . LYS B 1 437 ? 58.159  53.211  -72.407 1.00 104.20 ? 437 LYS B CD  1 
ATOM   7750  C CE  . LYS B 1 437 ? 59.011  54.435  -72.541 1.00 107.21 ? 437 LYS B CE  1 
ATOM   7751  N NZ  . LYS B 1 437 ? 58.343  55.494  -73.299 1.00 110.05 ? 437 LYS B NZ  1 
ATOM   7752  N N   . ILE B 1 438 ? 60.696  50.403  -68.871 1.00 97.15  ? 438 ILE B N   1 
ATOM   7753  C CA  . ILE B 1 438 ? 61.173  50.852  -67.575 1.00 96.88  ? 438 ILE B CA  1 
ATOM   7754  C C   . ILE B 1 438 ? 62.005  52.100  -67.798 1.00 100.45 ? 438 ILE B C   1 
ATOM   7755  O O   . ILE B 1 438 ? 62.981  52.065  -68.538 1.00 102.97 ? 438 ILE B O   1 
ATOM   7756  C CB  . ILE B 1 438 ? 61.997  49.771  -66.850 1.00 94.63  ? 438 ILE B CB  1 
ATOM   7757  C CG1 . ILE B 1 438 ? 61.268  48.428  -66.822 1.00 92.66  ? 438 ILE B CG1 1 
ATOM   7758  C CG2 . ILE B 1 438 ? 62.350  50.234  -65.437 1.00 94.13  ? 438 ILE B CG2 1 
ATOM   7759  C CD1 . ILE B 1 438 ? 62.075  47.263  -66.273 1.00 90.64  ? 438 ILE B CD1 1 
ATOM   7760  N N   . GLU B 1 439 ? 61.582  53.201  -67.178 1.00 102.50 ? 439 GLU B N   1 
ATOM   7761  C CA  . GLU B 1 439 ? 62.402  54.398  -67.091 1.00 105.81 ? 439 GLU B CA  1 
ATOM   7762  C C   . GLU B 1 439 ? 63.157  54.290  -65.768 1.00 103.82 ? 439 GLU B C   1 
ATOM   7763  O O   . GLU B 1 439 ? 62.564  54.007  -64.725 1.00 100.48 ? 439 GLU B O   1 
ATOM   7764  C CB  . GLU B 1 439 ? 61.554  55.666  -67.290 1.00 108.98 ? 439 GLU B CB  1 
ATOM   7765  C CG  . GLU B 1 439 ? 61.357  56.057  -68.758 1.00 111.78 ? 439 GLU B CG  1 
ATOM   7766  C CD  . GLU B 1 439 ? 60.398  57.194  -69.118 1.00 114.94 ? 439 GLU B CD  1 
ATOM   7767  O OE1 . GLU B 1 439 ? 59.402  57.457  -68.398 1.00 115.11 ? 439 GLU B OE1 1 
ATOM   7768  O OE2 . GLU B 1 439 ? 60.651  57.840  -70.165 1.00 117.46 ? 439 GLU B OE2 1 
ATOM   7769  N N   . THR B 1 440 ? 64.480  54.442  -65.837 1.00 105.07 ? 440 THR B N   1 
ATOM   7770  C CA  . THR B 1 440 ? 65.314  54.288  -64.658 1.00 104.84 ? 440 THR B CA  1 
ATOM   7771  C C   . THR B 1 440 ? 65.464  55.650  -63.988 1.00 107.63 ? 440 THR B C   1 
ATOM   7772  O O   . THR B 1 440 ? 64.932  56.644  -64.465 1.00 108.51 ? 440 THR B O   1 
ATOM   7773  C CB  . THR B 1 440 ? 66.655  53.662  -65.044 1.00 105.02 ? 440 THR B CB  1 
ATOM   7774  O OG1 . THR B 1 440 ? 67.375  54.575  -65.871 1.00 108.30 ? 440 THR B OG1 1 
ATOM   7775  C CG2 . THR B 1 440 ? 66.463  52.337  -65.757 1.00 102.92 ? 440 THR B CG2 1 
ATOM   7776  N N   . SER B 1 441 ? 66.173  55.664  -62.861 1.00 108.53 ? 441 SER B N   1 
ATOM   7777  C CA  . SER B 1 441 ? 66.374  56.863  -62.075 1.00 111.74 ? 441 SER B CA  1 
ATOM   7778  C C   . SER B 1 441 ? 67.574  56.626  -61.172 1.00 113.41 ? 441 SER B C   1 
ATOM   7779  O O   . SER B 1 441 ? 67.457  55.879  -60.209 1.00 110.71 ? 441 SER B O   1 
ATOM   7780  C CB  . SER B 1 441 ? 65.136  57.180  -61.277 1.00 110.71 ? 441 SER B CB  1 
ATOM   7781  O OG  . SER B 1 441 ? 65.329  58.308  -60.436 1.00 113.68 ? 441 SER B OG  1 
ATOM   7782  N N   . GLU B 1 442 ? 68.719  57.244  -61.489 1.00 119.45 ? 442 GLU B N   1 
ATOM   7783  C CA  . GLU B 1 442 ? 69.962  56.906  -60.807 1.00 122.12 ? 442 GLU B CA  1 
ATOM   7784  C C   . GLU B 1 442 ? 69.752  57.007  -59.296 1.00 125.21 ? 442 GLU B C   1 
ATOM   7785  O O   . GLU B 1 442 ? 68.918  57.792  -58.847 1.00 131.04 ? 442 GLU B O   1 
ATOM   7786  C CB  . GLU B 1 442 ? 71.147  57.773  -61.235 1.00 124.17 ? 442 GLU B CB  1 
ATOM   7787  C CG  . GLU B 1 442 ? 70.996  59.253  -60.896 1.00 126.07 ? 442 GLU B CG  1 
ATOM   7788  C CD  . GLU B 1 442 ? 72.288  60.025  -61.064 1.00 128.05 ? 442 GLU B CD  1 
ATOM   7789  O OE1 . GLU B 1 442 ? 73.294  59.383  -61.407 1.00 127.27 ? 442 GLU B OE1 1 
ATOM   7790  O OE2 . GLU B 1 442 ? 72.298  61.247  -60.840 1.00 129.64 ? 442 GLU B OE2 1 
ATOM   7791  N N   . ASN B 1 443 ? 70.511  56.192  -58.546 1.00 124.81 ? 443 ASN B N   1 
ATOM   7792  C CA  . ASN B 1 443 ? 70.399  56.028  -57.099 1.00 124.47 ? 443 ASN B CA  1 
ATOM   7793  C C   . ASN B 1 443 ? 69.216  55.112  -56.752 1.00 119.82 ? 443 ASN B C   1 
ATOM   7794  O O   . ASN B 1 443 ? 69.146  54.633  -55.625 1.00 122.07 ? 443 ASN B O   1 
ATOM   7795  C CB  . ASN B 1 443 ? 70.501  57.349  -56.324 1.00 128.97 ? 443 ASN B CB  1 
ATOM   7796  C CG  . ASN B 1 443 ? 69.269  58.233  -56.377 1.00 132.55 ? 443 ASN B CG  1 
ATOM   7797  O OD1 . ASN B 1 443 ? 68.189  57.836  -55.922 1.00 131.99 ? 443 ASN B OD1 1 
ATOM   7798  N ND2 . ASN B 1 443 ? 69.407  59.453  -56.886 1.00 134.75 ? 443 ASN B ND2 1 
ATOM   7799  N N   . PHE B 1 444 ? 68.305  54.842  -57.704 1.00 115.02 ? 444 PHE B N   1 
ATOM   7800  C CA  . PHE B 1 444 ? 67.350  53.747  -57.584 1.00 108.38 ? 444 PHE B CA  1 
ATOM   7801  C C   . PHE B 1 444 ? 67.849  52.600  -58.457 1.00 106.43 ? 444 PHE B C   1 
ATOM   7802  O O   . PHE B 1 444 ? 67.795  52.705  -59.683 1.00 105.06 ? 444 PHE B O   1 
ATOM   7803  C CB  . PHE B 1 444 ? 65.918  54.108  -58.002 1.00 107.29 ? 444 PHE B CB  1 
ATOM   7804  C CG  . PHE B 1 444 ? 65.178  55.023  -57.033 1.00 107.16 ? 444 PHE B CG  1 
ATOM   7805  C CD1 . PHE B 1 444 ? 65.347  56.403  -57.094 1.00 109.83 ? 444 PHE B CD1 1 
ATOM   7806  C CD2 . PHE B 1 444 ? 64.321  54.504  -56.065 1.00 103.97 ? 444 PHE B CD2 1 
ATOM   7807  C CE1 . PHE B 1 444 ? 64.690  57.232  -56.199 1.00 110.50 ? 444 PHE B CE1 1 
ATOM   7808  C CE2 . PHE B 1 444 ? 63.671  55.337  -55.172 1.00 104.46 ? 444 PHE B CE2 1 
ATOM   7809  C CZ  . PHE B 1 444 ? 63.860  56.698  -55.240 1.00 108.08 ? 444 PHE B CZ  1 
ATOM   7810  N N   . THR B 1 445 ? 68.342  51.533  -57.801 1.00 105.15 ? 445 THR B N   1 
ATOM   7811  C CA  . THR B 1 445 ? 68.880  50.350  -58.460 1.00 103.16 ? 445 THR B CA  1 
ATOM   7812  C C   . THR B 1 445 ? 67.766  49.321  -58.601 1.00 98.06  ? 445 THR B C   1 
ATOM   7813  O O   . THR B 1 445 ? 67.182  48.931  -57.595 1.00 95.75  ? 445 THR B O   1 
ATOM   7814  C CB  . THR B 1 445 ? 70.059  49.789  -57.655 1.00 105.11 ? 445 THR B CB  1 
ATOM   7815  O OG1 . THR B 1 445 ? 70.003  50.333  -56.338 1.00 107.48 ? 445 THR B OG1 1 
ATOM   7816  C CG2 . THR B 1 445 ? 71.415  50.200  -58.209 1.00 107.49 ? 445 THR B CG2 1 
ATOM   7817  N N   . LEU B 1 446 ? 67.472  48.921  -59.851 1.00 97.00  ? 446 LEU B N   1 
ATOM   7818  C CA  . LEU B 1 446 ? 66.533  47.841  -60.150 1.00 94.92  ? 446 LEU B CA  1 
ATOM   7819  C C   . LEU B 1 446 ? 67.168  46.537  -59.690 1.00 95.09  ? 446 LEU B C   1 
ATOM   7820  O O   . LEU B 1 446 ? 68.354  46.514  -59.391 1.00 96.70  ? 446 LEU B O   1 
ATOM   7821  C CB  . LEU B 1 446 ? 66.238  47.744  -61.645 1.00 93.84  ? 446 LEU B CB  1 
ATOM   7822  C CG  . LEU B 1 446 ? 65.696  49.004  -62.309 1.00 94.64  ? 446 LEU B CG  1 
ATOM   7823  C CD1 . LEU B 1 446 ? 65.641  48.805  -63.812 1.00 94.95  ? 446 LEU B CD1 1 
ATOM   7824  C CD2 . LEU B 1 446 ? 64.347  49.350  -61.709 1.00 93.46  ? 446 LEU B CD2 1 
ATOM   7825  N N   . LEU B 1 447 ? 66.437  45.427  -59.674 1.00 93.96  ? 447 LEU B N   1 
ATOM   7826  C CA  . LEU B 1 447 ? 67.162  44.225  -59.323 1.00 95.17  ? 447 LEU B CA  1 
ATOM   7827  C C   . LEU B 1 447 ? 66.539  42.969  -59.918 1.00 97.16  ? 447 LEU B C   1 
ATOM   7828  O O   . LEU B 1 447 ? 65.466  43.016  -60.500 1.00 97.84  ? 447 LEU B O   1 
ATOM   7829  C CB  . LEU B 1 447 ? 67.387  44.168  -57.812 1.00 93.05  ? 447 LEU B CB  1 
ATOM   7830  C CG  . LEU B 1 447 ? 66.186  44.317  -56.885 1.00 90.86  ? 447 LEU B CG  1 
ATOM   7831  C CD1 . LEU B 1 447 ? 65.484  42.990  -56.720 1.00 90.10  ? 447 LEU B CD1 1 
ATOM   7832  C CD2 . LEU B 1 447 ? 66.679  44.833  -55.553 1.00 90.42  ? 447 LEU B CD2 1 
ATOM   7833  N N   . ASP B 1 448 ? 67.247  41.856  -59.708 1.00 102.73 ? 448 ASP B N   1 
ATOM   7834  C CA  . ASP B 1 448 ? 66.799  40.514  -60.168 1.00 107.14 ? 448 ASP B CA  1 
ATOM   7835  C C   . ASP B 1 448 ? 66.117  40.563  -61.528 1.00 106.33 ? 448 ASP B C   1 
ATOM   7836  O O   . ASP B 1 448 ? 66.760  40.998  -62.504 1.00 111.51 ? 448 ASP B O   1 
ATOM   7837  C CB  . ASP B 1 448 ? 65.964  39.821  -59.106 1.00 111.04 ? 448 ASP B CB  1 
ATOM   7838  C CG  . ASP B 1 448 ? 66.719  39.451  -57.838 1.00 115.58 ? 448 ASP B CG  1 
ATOM   7839  O OD1 . ASP B 1 448 ? 67.509  40.291  -57.363 1.00 126.78 ? 448 ASP B OD1 1 
ATOM   7840  O OD2 . ASP B 1 448 ? 66.514  38.325  -57.341 1.00 113.63 ? 448 ASP B OD2 1 
ATOM   7841  N N   . ASP B 1 449 ? 64.874  40.096  -61.584 1.00 100.90 ? 449 ASP B N   1 
ATOM   7842  C CA  . ASP B 1 449 ? 64.233  39.979  -62.915 1.00 100.58 ? 449 ASP B CA  1 
ATOM   7843  C C   . ASP B 1 449 ? 62.906  40.719  -62.985 1.00 95.72  ? 449 ASP B C   1 
ATOM   7844  O O   . ASP B 1 449 ? 62.185  40.790  -61.968 1.00 89.94  ? 449 ASP B O   1 
ATOM   7845  C CB  . ASP B 1 449 ? 63.981  38.529  -63.295 1.00 102.93 ? 449 ASP B CB  1 
ATOM   7846  C CG  . ASP B 1 449 ? 65.201  37.736  -63.741 1.00 106.93 ? 449 ASP B CG  1 
ATOM   7847  O OD1 . ASP B 1 449 ? 66.214  38.371  -64.099 1.00 110.67 ? 449 ASP B OD1 1 
ATOM   7848  O OD2 . ASP B 1 449 ? 65.128  36.491  -63.727 1.00 102.57 ? 449 ASP B OD2 1 
ATOM   7849  N N   . LEU B 1 450 ? 62.629  41.255  -64.164 1.00 94.98  ? 450 LEU B N   1 
ATOM   7850  C CA  . LEU B 1 450 ? 61.327  41.889  -64.399 1.00 92.55  ? 450 LEU B CA  1 
ATOM   7851  C C   . LEU B 1 450 ? 60.375  40.742  -64.692 1.00 88.95  ? 450 LEU B C   1 
ATOM   7852  O O   . LEU B 1 450 ? 60.666  39.961  -65.617 1.00 88.98  ? 450 LEU B O   1 
ATOM   7853  C CB  . LEU B 1 450 ? 61.533  42.779  -65.614 1.00 96.02  ? 450 LEU B CB  1 
ATOM   7854  C CG  . LEU B 1 450 ? 60.289  43.087  -66.446 1.00 98.19  ? 450 LEU B CG  1 
ATOM   7855  C CD1 . LEU B 1 450 ? 59.407  44.085  -65.724 1.00 98.68  ? 450 LEU B CD1 1 
ATOM   7856  C CD2 . LEU B 1 450 ? 60.710  43.594  -67.810 1.00 100.93 ? 450 LEU B CD2 1 
ATOM   7857  N N   . LYS B 1 451 ? 59.303  40.634  -63.915 1.00 87.48  ? 451 LYS B N   1 
ATOM   7858  C CA  . LYS B 1 451 ? 58.362  39.531  -64.090 1.00 85.73  ? 451 LYS B CA  1 
ATOM   7859  C C   . LYS B 1 451 ? 57.122  39.990  -64.866 1.00 84.76  ? 451 LYS B C   1 
ATOM   7860  O O   . LYS B 1 451 ? 56.570  41.047  -64.579 1.00 85.32  ? 451 LYS B O   1 
ATOM   7861  C CB  . LYS B 1 451 ? 57.976  38.957  -62.722 1.00 84.66  ? 451 LYS B CB  1 
ATOM   7862  C CG  . LYS B 1 451 ? 59.065  38.168  -61.995 1.00 83.94  ? 451 LYS B CG  1 
ATOM   7863  C CD  . LYS B 1 451 ? 58.671  37.698  -60.599 1.00 83.51  ? 451 LYS B CD  1 
ATOM   7864  C CE  . LYS B 1 451 ? 59.801  37.084  -59.840 1.00 84.66  ? 451 LYS B CE  1 
ATOM   7865  N NZ  . LYS B 1 451 ? 59.492  36.997  -58.410 1.00 85.44  ? 451 LYS B NZ  1 
ATOM   7866  N N   . ILE B 1 452 ? 56.697  39.177  -65.845 1.00 83.51  ? 452 ILE B N   1 
ATOM   7867  C CA  . ILE B 1 452 ? 55.537  39.454  -66.677 1.00 83.63  ? 452 ILE B CA  1 
ATOM   7868  C C   . ILE B 1 452 ? 54.450  38.414  -66.385 1.00 81.84  ? 452 ILE B C   1 
ATOM   7869  O O   . ILE B 1 452 ? 54.784  37.262  -66.092 1.00 80.50  ? 452 ILE B O   1 
ATOM   7870  C CB  . ILE B 1 452 ? 55.954  39.456  -68.160 1.00 85.52  ? 452 ILE B CB  1 
ATOM   7871  C CG1 . ILE B 1 452 ? 56.629  40.769  -68.564 1.00 88.19  ? 452 ILE B CG1 1 
ATOM   7872  C CG2 . ILE B 1 452 ? 54.757  39.182  -69.069 1.00 86.00  ? 452 ILE B CG2 1 
ATOM   7873  C CD1 . ILE B 1 452 ? 57.917  41.082  -67.835 1.00 88.46  ? 452 ILE B CD1 1 
ATOM   7874  N N   . SER B 1 453 ? 53.164  38.814  -66.499 1.00 80.47  ? 453 SER B N   1 
ATOM   7875  C CA  . SER B 1 453 ? 52.040  37.918  -66.243 1.00 78.97  ? 453 SER B CA  1 
ATOM   7876  C C   . SER B 1 453 ? 50.878  38.197  -67.189 1.00 79.29  ? 453 SER B C   1 
ATOM   7877  O O   . SER B 1 453 ? 50.366  39.303  -67.191 1.00 81.03  ? 453 SER B O   1 
ATOM   7878  C CB  . SER B 1 453 ? 51.562  38.045  -64.824 1.00 78.04  ? 453 SER B CB  1 
ATOM   7879  O OG  . SER B 1 453 ? 50.388  37.267  -64.621 1.00 78.31  ? 453 SER B OG  1 
ATOM   7880  N N   . TYR B 1 454 ? 50.424  37.190  -67.943 1.00 78.68  ? 454 TYR B N   1 
ATOM   7881  C CA  . TYR B 1 454 ? 49.245  37.336  -68.785 1.00 79.16  ? 454 TYR B CA  1 
ATOM   7882  C C   . TYR B 1 454 ? 48.173  36.410  -68.233 1.00 78.64  ? 454 TYR B C   1 
ATOM   7883  O O   . TYR B 1 454 ? 48.139  35.242  -68.613 1.00 79.90  ? 454 TYR B O   1 
ATOM   7884  C CB  . TYR B 1 454 ? 49.539  37.017  -70.258 1.00 80.22  ? 454 TYR B CB  1 
ATOM   7885  C CG  . TYR B 1 454 ? 48.480  37.453  -71.272 1.00 81.45  ? 454 TYR B CG  1 
ATOM   7886  C CD1 . TYR B 1 454 ? 48.263  38.803  -71.562 1.00 82.29  ? 454 TYR B CD1 1 
ATOM   7887  C CD2 . TYR B 1 454 ? 47.728  36.528  -71.993 1.00 81.42  ? 454 TYR B CD2 1 
ATOM   7888  C CE1 . TYR B 1 454 ? 47.312  39.212  -72.489 1.00 83.03  ? 454 TYR B CE1 1 
ATOM   7889  C CE2 . TYR B 1 454 ? 46.785  36.930  -72.935 1.00 82.44  ? 454 TYR B CE2 1 
ATOM   7890  C CZ  . TYR B 1 454 ? 46.574  38.275  -73.185 1.00 82.88  ? 454 TYR B CZ  1 
ATOM   7891  O OH  . TYR B 1 454 ? 45.663  38.676  -74.115 1.00 83.83  ? 454 TYR B OH  1 
ATOM   7892  N N   . ASN B 1 455 ? 47.326  36.921  -67.323 1.00 77.49  ? 455 ASN B N   1 
ATOM   7893  C CA  . ASN B 1 455 ? 46.456  36.050  -66.535 1.00 76.31  ? 455 ASN B CA  1 
ATOM   7894  C C   . ASN B 1 455 ? 45.071  35.909  -67.166 1.00 76.50  ? 455 ASN B C   1 
ATOM   7895  O O   . ASN B 1 455 ? 44.238  36.809  -67.061 1.00 76.33  ? 455 ASN B O   1 
ATOM   7896  C CB  . ASN B 1 455 ? 46.297  36.541  -65.103 1.00 75.35  ? 455 ASN B CB  1 
ATOM   7897  C CG  . ASN B 1 455 ? 45.519  35.555  -64.263 1.00 74.73  ? 455 ASN B CG  1 
ATOM   7898  O OD1 . ASN B 1 455 ? 44.536  34.955  -64.735 1.00 74.55  ? 455 ASN B OD1 1 
ATOM   7899  N ND2 . ASN B 1 455 ? 45.964  35.363  -63.027 1.00 73.78  ? 455 ASN B ND2 1 
ATOM   7900  N N   . THR B 1 456 ? 44.798  34.733  -67.731 1.00 76.11  ? 456 THR B N   1 
ATOM   7901  C CA  . THR B 1 456 ? 43.714  34.610  -68.687 1.00 77.51  ? 456 THR B CA  1 
ATOM   7902  C C   . THR B 1 456 ? 42.409  34.195  -68.007 1.00 77.36  ? 456 THR B C   1 
ATOM   7903  O O   . THR B 1 456 ? 41.398  34.042  -68.693 1.00 78.60  ? 456 THR B O   1 
ATOM   7904  C CB  . THR B 1 456 ? 44.131  33.641  -69.789 1.00 78.46  ? 456 THR B CB  1 
ATOM   7905  O OG1 . THR B 1 456 ? 44.727  32.555  -69.092 1.00 78.02  ? 456 THR B OG1 1 
ATOM   7906  C CG2 . THR B 1 456 ? 45.104  34.263  -70.775 1.00 78.98  ? 456 THR B CG2 1 
ATOM   7907  N N   . HIS B 1 457 ? 42.422  34.020  -66.673 1.00 76.08  ? 457 HIS B N   1 
ATOM   7908  C CA  . HIS B 1 457 ? 41.197  33.958  -65.879 1.00 75.46  ? 457 HIS B CA  1 
ATOM   7909  C C   . HIS B 1 457 ? 40.354  32.721  -66.181 1.00 75.75  ? 457 HIS B C   1 
ATOM   7910  O O   . HIS B 1 457 ? 39.132  32.757  -66.004 1.00 76.93  ? 457 HIS B O   1 
ATOM   7911  C CB  . HIS B 1 457 ? 40.338  35.205  -66.123 1.00 76.60  ? 457 HIS B CB  1 
ATOM   7912  C CG  . HIS B 1 457 ? 40.675  36.368  -65.264 1.00 76.08  ? 457 HIS B CG  1 
ATOM   7913  N ND1 . HIS B 1 457 ? 41.751  37.194  -65.484 1.00 76.11  ? 457 HIS B ND1 1 
ATOM   7914  C CD2 . HIS B 1 457 ? 40.066  36.814  -64.161 1.00 75.81  ? 457 HIS B CD2 1 
ATOM   7915  C CE1 . HIS B 1 457 ? 41.776  38.107  -64.528 1.00 76.19  ? 457 HIS B CE1 1 
ATOM   7916  N NE2 . HIS B 1 457 ? 40.750  37.906  -63.724 1.00 75.74  ? 457 HIS B NE2 1 
ATOM   7917  N N   . LEU B 1 458 ? 41.020  31.648  -66.621 1.00 75.61  ? 458 LEU B N   1 
ATOM   7918  C CA  . LEU B 1 458 ? 40.409  30.347  -66.848 1.00 76.51  ? 458 LEU B CA  1 
ATOM   7919  C C   . LEU B 1 458 ? 40.446  29.574  -65.528 1.00 77.16  ? 458 LEU B C   1 
ATOM   7920  O O   . LEU B 1 458 ? 41.462  28.951  -65.206 1.00 77.28  ? 458 LEU B O   1 
ATOM   7921  C CB  . LEU B 1 458 ? 41.150  29.561  -67.938 1.00 76.34  ? 458 LEU B CB  1 
ATOM   7922  C CG  . LEU B 1 458 ? 41.492  30.295  -69.238 1.00 76.68  ? 458 LEU B CG  1 
ATOM   7923  C CD1 . LEU B 1 458 ? 42.377  29.450  -70.113 1.00 77.05  ? 458 LEU B CD1 1 
ATOM   7924  C CD2 . LEU B 1 458 ? 40.262  30.701  -70.006 1.00 77.89  ? 458 LEU B CD2 1 
ATOM   7925  N N   . GLY B 1 459 ? 39.341  29.600  -64.770 1.00 78.30  ? 459 GLY B N   1 
ATOM   7926  C CA  . GLY B 1 459 ? 39.309  29.009  -63.439 1.00 79.08  ? 459 GLY B CA  1 
ATOM   7927  C C   . GLY B 1 459 ? 40.358  29.638  -62.522 1.00 79.06  ? 459 GLY B C   1 
ATOM   7928  O O   . GLY B 1 459 ? 40.508  30.860  -62.521 1.00 82.46  ? 459 GLY B O   1 
ATOM   7929  N N   . TRP B 1 460 ? 41.092  28.812  -61.757 1.00 77.38  ? 460 TRP B N   1 
ATOM   7930  C CA  . TRP B 1 460 ? 42.136  29.338  -60.888 1.00 76.25  ? 460 TRP B CA  1 
ATOM   7931  C C   . TRP B 1 460 ? 43.480  29.441  -61.615 1.00 74.84  ? 460 TRP B C   1 
ATOM   7932  O O   . TRP B 1 460 ? 44.486  29.764  -60.997 1.00 73.35  ? 460 TRP B O   1 
ATOM   7933  C CB  . TRP B 1 460 ? 42.293  28.464  -59.639 1.00 77.08  ? 460 TRP B CB  1 
ATOM   7934  C CG  . TRP B 1 460 ? 41.073  28.408  -58.775 1.00 79.42  ? 460 TRP B CG  1 
ATOM   7935  C CD1 . TRP B 1 460 ? 40.231  27.356  -58.604 1.00 81.97  ? 460 TRP B CD1 1 
ATOM   7936  C CD2 . TRP B 1 460 ? 40.536  29.482  -57.987 1.00 81.57  ? 460 TRP B CD2 1 
ATOM   7937  N NE1 . TRP B 1 460 ? 39.223  27.691  -57.742 1.00 82.54  ? 460 TRP B NE1 1 
ATOM   7938  C CE2 . TRP B 1 460 ? 39.374  28.993  -57.360 1.00 83.05  ? 460 TRP B CE2 1 
ATOM   7939  C CE3 . TRP B 1 460 ? 40.916  30.805  -57.760 1.00 83.54  ? 460 TRP B CE3 1 
ATOM   7940  C CZ2 . TRP B 1 460 ? 38.588  29.786  -56.526 1.00 85.76  ? 460 TRP B CZ2 1 
ATOM   7941  C CZ3 . TRP B 1 460 ? 40.132  31.597  -56.946 1.00 84.95  ? 460 TRP B CZ3 1 
ATOM   7942  C CH2 . TRP B 1 460 ? 38.980  31.094  -56.340 1.00 85.69  ? 460 TRP B CH2 1 
ATOM   7943  N N   . ALA B 1 461 ? 43.507  29.128  -62.915 1.00 74.83  ? 461 ALA B N   1 
ATOM   7944  C CA  . ALA B 1 461 ? 44.739  29.087  -63.681 1.00 74.19  ? 461 ALA B CA  1 
ATOM   7945  C C   . ALA B 1 461 ? 45.207  30.514  -63.976 1.00 74.18  ? 461 ALA B C   1 
ATOM   7946  O O   . ALA B 1 461 ? 44.538  31.268  -64.682 1.00 74.65  ? 461 ALA B O   1 
ATOM   7947  C CB  . ALA B 1 461 ? 44.528  28.282  -64.948 1.00 74.84  ? 461 ALA B CB  1 
ATOM   7948  N N   . ILE B 1 462 ? 46.392  30.867  -63.456 1.00 74.11  ? 462 ILE B N   1 
ATOM   7949  C CA  . ILE B 1 462 ? 46.901  32.222  -63.571 1.00 73.54  ? 462 ILE B CA  1 
ATOM   7950  C C   . ILE B 1 462 ? 47.577  32.402  -64.922 1.00 74.60  ? 462 ILE B C   1 
ATOM   7951  O O   . ILE B 1 462 ? 48.186  33.446  -65.151 1.00 76.33  ? 462 ILE B O   1 
ATOM   7952  C CB  . ILE B 1 462 ? 47.877  32.569  -62.439 1.00 71.97  ? 462 ILE B CB  1 
ATOM   7953  C CG1 . ILE B 1 462 ? 49.130  31.763  -62.548 1.00 72.52  ? 462 ILE B CG1 1 
ATOM   7954  C CG2 . ILE B 1 462 ? 47.238  32.409  -61.063 1.00 71.05  ? 462 ILE B CG2 1 
ATOM   7955  C CD1 . ILE B 1 462 ? 50.338  32.430  -61.908 1.00 72.78  ? 462 ILE B CD1 1 
ATOM   7956  N N   . GLY B 1 463 ? 47.489  31.385  -65.788 1.00 75.13  ? 463 GLY B N   1 
ATOM   7957  C CA  . GLY B 1 463 ? 47.972  31.512  -67.150 1.00 76.85  ? 463 GLY B CA  1 
ATOM   7958  C C   . GLY B 1 463 ? 49.475  31.782  -67.156 1.00 77.91  ? 463 GLY B C   1 
ATOM   7959  O O   . GLY B 1 463 ? 50.179  31.487  -66.188 1.00 76.71  ? 463 GLY B O   1 
ATOM   7960  N N   . SER B 1 464 ? 49.961  32.398  -68.233 1.00 80.05  ? 464 SER B N   1 
ATOM   7961  C CA  . SER B 1 464 ? 51.394  32.455  -68.459 1.00 80.83  ? 464 SER B CA  1 
ATOM   7962  C C   . SER B 1 464 ? 52.047  33.499  -67.563 1.00 79.09  ? 464 SER B C   1 
ATOM   7963  O O   . SER B 1 464 ? 51.364  34.401  -67.051 1.00 80.48  ? 464 SER B O   1 
ATOM   7964  C CB  . SER B 1 464 ? 51.679  32.695  -69.900 1.00 83.72  ? 464 SER B CB  1 
ATOM   7965  O OG  . SER B 1 464 ? 51.162  31.607  -70.658 1.00 86.94  ? 464 SER B OG  1 
ATOM   7966  N N   . GLN B 1 465 ? 53.352  33.275  -67.354 1.00 76.73  ? 465 GLN B N   1 
ATOM   7967  C CA  . GLN B 1 465 ? 54.270  34.178  -66.695 1.00 75.82  ? 465 GLN B CA  1 
ATOM   7968  C C   . GLN B 1 465 ? 55.599  34.166  -67.448 1.00 76.32  ? 465 GLN B C   1 
ATOM   7969  O O   . GLN B 1 465 ? 55.807  33.363  -68.352 1.00 76.71  ? 465 GLN B O   1 
ATOM   7970  C CB  . GLN B 1 465 ? 54.563  33.720  -65.273 1.00 75.08  ? 465 GLN B CB  1 
ATOM   7971  C CG  . GLN B 1 465 ? 53.474  34.086  -64.289 1.00 76.19  ? 465 GLN B CG  1 
ATOM   7972  C CD  . GLN B 1 465 ? 53.913  33.988  -62.848 1.00 77.92  ? 465 GLN B CD  1 
ATOM   7973  O OE1 . GLN B 1 465 ? 54.504  34.918  -62.291 1.00 81.84  ? 465 GLN B OE1 1 
ATOM   7974  N NE2 . GLN B 1 465 ? 53.572  32.878  -62.211 1.00 78.73  ? 465 GLN B NE2 1 
ATOM   7975  N N   . ALA B 1 466 ? 56.507  35.065  -67.063 1.00 75.64  ? 466 ALA B N   1 
ATOM   7976  C CA  . ALA B 1 466 ? 57.831  35.106  -67.651 1.00 75.96  ? 466 ALA B CA  1 
ATOM   7977  C C   . ALA B 1 466 ? 58.739  35.867  -66.703 1.00 75.78  ? 466 ALA B C   1 
ATOM   7978  O O   . ALA B 1 466 ? 58.293  36.845  -66.107 1.00 75.45  ? 466 ALA B O   1 
ATOM   7979  C CB  . ALA B 1 466 ? 57.804  35.749  -69.023 1.00 77.11  ? 466 ALA B CB  1 
ATOM   7980  N N   . SER B 1 467 ? 59.965  35.349  -66.531 1.00 75.98  ? 467 SER B N   1 
ATOM   7981  C CA  . SER B 1 467 ? 61.082  36.100  -65.984 1.00 76.43  ? 467 SER B CA  1 
ATOM   7982  C C   . SER B 1 467 ? 61.960  36.590  -67.134 1.00 78.19  ? 467 SER B C   1 
ATOM   7983  O O   . SER B 1 467 ? 62.152  35.902  -68.131 1.00 79.19  ? 467 SER B O   1 
ATOM   7984  C CB  . SER B 1 467 ? 61.889  35.272  -65.012 1.00 76.04  ? 467 SER B CB  1 
ATOM   7985  O OG  . SER B 1 467 ? 61.244  35.138  -63.755 1.00 75.12  ? 467 SER B OG  1 
ATOM   7986  N N   . VAL B 1 468 ? 62.510  37.790  -66.995 1.00 79.06  ? 468 VAL B N   1 
ATOM   7987  C CA  . VAL B 1 468 ? 63.336  38.355  -68.047 1.00 80.85  ? 468 VAL B CA  1 
ATOM   7988  C C   . VAL B 1 468 ? 64.557  38.924  -67.354 1.00 81.49  ? 468 VAL B C   1 
ATOM   7989  O O   . VAL B 1 468 ? 64.414  39.709  -66.418 1.00 80.45  ? 468 VAL B O   1 
ATOM   7990  C CB  . VAL B 1 468 ? 62.605  39.418  -68.897 1.00 81.53  ? 468 VAL B CB  1 
ATOM   7991  C CG1 . VAL B 1 468 ? 63.472  39.983  -70.011 1.00 83.17  ? 468 VAL B CG1 1 
ATOM   7992  C CG2 . VAL B 1 468 ? 61.318  38.857  -69.493 1.00 81.10  ? 468 VAL B CG2 1 
ATOM   7993  N N   . SER B 1 469 ? 65.731  38.431  -67.774 1.00 83.43  ? 469 SER B N   1 
ATOM   7994  C CA  . SER B 1 469 ? 67.006  38.983  -67.358 1.00 84.42  ? 469 SER B CA  1 
ATOM   7995  C C   . SER B 1 469 ? 67.088  40.376  -67.956 1.00 86.95  ? 469 SER B C   1 
ATOM   7996  O O   . SER B 1 469 ? 66.741  40.556  -69.122 1.00 87.19  ? 469 SER B O   1 
ATOM   7997  C CB  . SER B 1 469 ? 68.154  38.103  -67.808 1.00 85.27  ? 469 SER B CB  1 
ATOM   7998  O OG  . SER B 1 469 ? 69.447  38.670  -67.584 1.00 86.53  ? 469 SER B OG  1 
ATOM   7999  N N   . ILE B 1 470 ? 67.494  41.352  -67.142 1.00 89.24  ? 470 ILE B N   1 
ATOM   8000  C CA  . ILE B 1 470 ? 67.783  42.675  -67.668 1.00 93.94  ? 470 ILE B CA  1 
ATOM   8001  C C   . ILE B 1 470 ? 69.268  42.994  -67.519 1.00 96.73  ? 470 ILE B C   1 
ATOM   8002  O O   . ILE B 1 470 ? 69.645  44.136  -67.718 1.00 98.56  ? 470 ILE B O   1 
ATOM   8003  C CB  . ILE B 1 470 ? 66.905  43.745  -66.999 1.00 94.59  ? 470 ILE B CB  1 
ATOM   8004  C CG1 . ILE B 1 470 ? 67.118  43.798  -65.480 1.00 94.97  ? 470 ILE B CG1 1 
ATOM   8005  C CG2 . ILE B 1 470 ? 65.440  43.532  -67.369 1.00 93.03  ? 470 ILE B CG2 1 
ATOM   8006  C CD1 . ILE B 1 470 ? 66.326  44.894  -64.779 1.00 95.67  ? 470 ILE B CD1 1 
ATOM   8007  N N   . SER B 1 471 ? 70.098  41.980  -67.224 1.00 98.95  ? 471 SER B N   1 
ATOM   8008  C CA  . SER B 1 471 ? 71.526  42.146  -66.977 1.00 101.95 ? 471 SER B CA  1 
ATOM   8009  C C   . SER B 1 471 ? 72.178  43.020  -68.050 1.00 106.64 ? 471 SER B C   1 
ATOM   8010  O O   . SER B 1 471 ? 72.844  44.004  -67.730 1.00 108.02 ? 471 SER B O   1 
ATOM   8011  C CB  . SER B 1 471 ? 72.221  40.809  -66.867 1.00 100.96 ? 471 SER B CB  1 
ATOM   8012  O OG  . SER B 1 471 ? 71.656  39.882  -67.782 1.00 101.04 ? 471 SER B OG  1 
ATOM   8013  N N   . ASP B 1 472 ? 71.940  42.682  -69.322 1.00 109.35 ? 472 ASP B N   1 
ATOM   8014  C CA  . ASP B 1 472 ? 72.622  43.333  -70.426 1.00 114.41 ? 472 ASP B CA  1 
ATOM   8015  C C   . ASP B 1 472 ? 72.159  44.780  -70.631 1.00 117.46 ? 472 ASP B C   1 
ATOM   8016  O O   . ASP B 1 472 ? 72.779  45.493  -71.415 1.00 121.92 ? 472 ASP B O   1 
ATOM   8017  C CB  . ASP B 1 472 ? 72.490  42.514  -71.698 1.00 116.09 ? 472 ASP B CB  1 
ATOM   8018  C CG  . ASP B 1 472 ? 71.093  42.390  -72.285 1.00 118.73 ? 472 ASP B CG  1 
ATOM   8019  O OD1 . ASP B 1 472 ? 70.089  42.655  -71.565 1.00 117.28 ? 472 ASP B OD1 1 
ATOM   8020  O OD2 . ASP B 1 472 ? 71.030  42.053  -73.480 1.00 124.67 ? 472 ASP B OD2 1 
ATOM   8021  N N   . GLN B 1 473 ? 71.104  45.224  -69.924 1.00 117.41 ? 473 GLN B N   1 
ATOM   8022  C CA  . GLN B 1 473 ? 70.457  46.502  -70.201 1.00 119.85 ? 473 GLN B CA  1 
ATOM   8023  C C   . GLN B 1 473 ? 70.485  47.464  -69.003 1.00 123.31 ? 473 GLN B C   1 
ATOM   8024  O O   . GLN B 1 473 ? 69.836  48.510  -69.053 1.00 125.24 ? 473 GLN B O   1 
ATOM   8025  C CB  . GLN B 1 473 ? 68.986  46.297  -70.577 1.00 116.98 ? 473 GLN B CB  1 
ATOM   8026  C CG  . GLN B 1 473 ? 68.719  45.822  -72.004 1.00 116.26 ? 473 GLN B CG  1 
ATOM   8027  C CD  . GLN B 1 473 ? 67.280  46.064  -72.426 1.00 114.44 ? 473 GLN B CD  1 
ATOM   8028  O OE1 . GLN B 1 473 ? 66.782  47.191  -72.374 1.00 113.06 ? 473 GLN B OE1 1 
ATOM   8029  N NE2 . GLN B 1 473 ? 66.575  45.020  -72.836 1.00 112.96 ? 473 GLN B NE2 1 
ATOM   8030  N N   . LEU B 1 474 ? 71.233  47.141  -67.934 1.00 125.76 ? 474 LEU B N   1 
ATOM   8031  C CA  . LEU B 1 474 ? 71.221  47.948  -66.713 1.00 126.91 ? 474 LEU B CA  1 
ATOM   8032  C C   . LEU B 1 474 ? 71.697  49.379  -67.000 1.00 126.43 ? 474 LEU B C   1 
ATOM   8033  O O   . LEU B 1 474 ? 71.139  50.333  -66.457 1.00 124.08 ? 474 LEU B O   1 
ATOM   8034  C CB  . LEU B 1 474 ? 72.053  47.318  -65.586 1.00 129.49 ? 474 LEU B CB  1 
ATOM   8035  C CG  . LEU B 1 474 ? 71.365  46.357  -64.596 1.00 126.47 ? 474 LEU B CG  1 
ATOM   8036  C CD1 . LEU B 1 474 ? 70.022  46.822  -64.039 1.00 124.20 ? 474 LEU B CD1 1 
ATOM   8037  C CD2 . LEU B 1 474 ? 71.210  44.972  -65.185 1.00 125.34 ? 474 LEU B CD2 1 
ATOM   8038  N N   . ASP B 1 475 ? 72.720  49.535  -67.855 1.00 125.72 ? 475 ASP B N   1 
ATOM   8039  C CA  . ASP B 1 475 ? 73.302  50.845  -68.120 1.00 127.59 ? 475 ASP B CA  1 
ATOM   8040  C C   . ASP B 1 475 ? 72.274  51.808  -68.728 1.00 129.28 ? 475 ASP B C   1 
ATOM   8041  O O   . ASP B 1 475 ? 72.372  53.022  -68.530 1.00 132.78 ? 475 ASP B O   1 
ATOM   8042  C CB  . ASP B 1 475 ? 74.559  50.752  -68.976 1.00 127.72 ? 475 ASP B CB  1 
ATOM   8043  C CG  . ASP B 1 475 ? 74.383  50.353  -70.436 1.00 127.86 ? 475 ASP B CG  1 
ATOM   8044  O OD1 . ASP B 1 475 ? 73.263  49.998  -70.832 1.00 126.35 ? 475 ASP B OD1 1 
ATOM   8045  O OD2 . ASP B 1 475 ? 75.384  50.393  -71.176 1.00 131.78 ? 475 ASP B OD2 1 
ATOM   8046  N N   . LYS B 1 476 ? 71.295  51.270  -69.473 1.00 124.78 ? 476 LYS B N   1 
ATOM   8047  C CA  . LYS B 1 476 ? 70.456  52.089  -70.332 1.00 123.10 ? 476 LYS B CA  1 
ATOM   8048  C C   . LYS B 1 476 ? 69.476  52.892  -69.486 1.00 119.53 ? 476 LYS B C   1 
ATOM   8049  O O   . LYS B 1 476 ? 69.182  52.505  -68.359 1.00 115.51 ? 476 LYS B O   1 
ATOM   8050  C CB  . LYS B 1 476 ? 69.694  51.230  -71.343 1.00 123.10 ? 476 LYS B CB  1 
ATOM   8051  C CG  . LYS B 1 476 ? 70.564  50.464  -72.329 1.00 125.25 ? 476 LYS B CG  1 
ATOM   8052  C CD  . LYS B 1 476 ? 69.787  49.476  -73.194 1.00 125.45 ? 476 LYS B CD  1 
ATOM   8053  C CE  . LYS B 1 476 ? 68.851  50.134  -74.164 1.00 127.43 ? 476 LYS B CE  1 
ATOM   8054  N NZ  . LYS B 1 476 ? 68.146  49.146  -74.983 1.00 125.99 ? 476 LYS B NZ  1 
ATOM   8055  N N   . LYS B 1 477 ? 68.997  54.006  -70.064 1.00 120.43 ? 477 LYS B N   1 
ATOM   8056  C CA  . LYS B 1 477 ? 68.044  54.907  -69.427 1.00 117.52 ? 477 LYS B CA  1 
ATOM   8057  C C   . LYS B 1 477 ? 66.624  54.381  -69.620 1.00 113.54 ? 477 LYS B C   1 
ATOM   8058  O O   . LYS B 1 477 ? 65.802  54.494  -68.713 1.00 112.61 ? 477 LYS B O   1 
ATOM   8059  C CB  . LYS B 1 477 ? 68.204  56.330  -69.966 1.00 120.04 ? 477 LYS B CB  1 
ATOM   8060  C CG  . LYS B 1 477 ? 69.549  56.955  -69.625 1.00 122.63 ? 477 LYS B CG  1 
ATOM   8061  C CD  . LYS B 1 477 ? 69.733  58.399  -70.081 1.00 126.26 ? 477 LYS B CD  1 
ATOM   8062  C CE  . LYS B 1 477 ? 69.974  58.511  -71.550 1.00 127.87 ? 477 LYS B CE  1 
ATOM   8063  N NZ  . LYS B 1 477 ? 69.635  59.844  -72.040 1.00 130.91 ? 477 LYS B NZ  1 
ATOM   8064  N N   . ILE B 1 478 ? 66.346  53.800  -70.795 1.00 111.73 ? 478 ILE B N   1 
ATOM   8065  C CA  . ILE B 1 478 ? 65.088  53.095  -71.025 1.00 108.36 ? 478 ILE B CA  1 
ATOM   8066  C C   . ILE B 1 478 ? 65.389  51.615  -71.301 1.00 105.46 ? 478 ILE B C   1 
ATOM   8067  O O   . ILE B 1 478 ? 66.047  51.273  -72.287 1.00 106.42 ? 478 ILE B O   1 
ATOM   8068  C CB  . ILE B 1 478 ? 64.262  53.770  -72.147 1.00 109.43 ? 478 ILE B CB  1 
ATOM   8069  C CG1 . ILE B 1 478 ? 63.946  55.246  -71.830 1.00 111.04 ? 478 ILE B CG1 1 
ATOM   8070  C CG2 . ILE B 1 478 ? 62.981  52.992  -72.440 1.00 106.96 ? 478 ILE B CG2 1 
ATOM   8071  C CD1 . ILE B 1 478 ? 63.371  56.027  -72.997 1.00 113.16 ? 478 ILE B CD1 1 
ATOM   8072  N N   . ILE B 1 479 ? 64.906  50.750  -70.396 1.00 101.64 ? 479 ILE B N   1 
ATOM   8073  C CA  . ILE B 1 479 ? 64.963  49.303  -70.538 1.00 98.84  ? 479 ILE B CA  1 
ATOM   8074  C C   . ILE B 1 479 ? 63.627  48.816  -71.093 1.00 96.77  ? 479 ILE B C   1 
ATOM   8075  O O   . ILE B 1 479 ? 62.585  49.117  -70.510 1.00 95.65  ? 479 ILE B O   1 
ATOM   8076  C CB  . ILE B 1 479 ? 65.240  48.633  -69.180 1.00 97.24  ? 479 ILE B CB  1 
ATOM   8077  C CG1 . ILE B 1 479 ? 66.350  49.335  -68.400 1.00 98.46  ? 479 ILE B CG1 1 
ATOM   8078  C CG2 . ILE B 1 479 ? 65.522  47.135  -69.357 1.00 95.94  ? 479 ILE B CG2 1 
ATOM   8079  C CD1 . ILE B 1 479 ? 66.575  48.765  -67.009 1.00 96.65  ? 479 ILE B CD1 1 
ATOM   8080  N N   . THR B 1 480 ? 63.664  48.052  -72.194 1.00 96.00  ? 480 THR B N   1 
ATOM   8081  C CA  . THR B 1 480 ? 62.449  47.565  -72.825 1.00 94.85  ? 480 THR B CA  1 
ATOM   8082  C C   . THR B 1 480 ? 62.494  46.047  -72.918 1.00 93.22  ? 480 THR B C   1 
ATOM   8083  O O   . THR B 1 480 ? 63.556  45.446  -72.835 1.00 93.03  ? 480 THR B O   1 
ATOM   8084  C CB  . THR B 1 480 ? 62.241  48.158  -74.217 1.00 96.78  ? 480 THR B CB  1 
ATOM   8085  O OG1 . THR B 1 480 ? 62.883  47.232  -75.085 1.00 97.00  ? 480 THR B OG1 1 
ATOM   8086  C CG2 . THR B 1 480 ? 62.763  49.574  -74.345 1.00 99.15  ? 480 THR B CG2 1 
ATOM   8087  N N   . SER B 1 481 ? 61.314  45.464  -73.159 1.00 92.93  ? 481 SER B N   1 
ATOM   8088  C CA  . SER B 1 481 ? 61.111  44.025  -73.147 1.00 91.68  ? 481 SER B CA  1 
ATOM   8089  C C   . SER B 1 481 ? 59.780  43.692  -73.809 1.00 91.72  ? 481 SER B C   1 
ATOM   8090  O O   . SER B 1 481 ? 58.763  44.267  -73.442 1.00 91.93  ? 481 SER B O   1 
ATOM   8091  C CB  . SER B 1 481 ? 61.142  43.494  -71.741 1.00 89.45  ? 481 SER B CB  1 
ATOM   8092  O OG  . SER B 1 481 ? 60.730  42.137  -71.700 1.00 88.12  ? 481 SER B OG  1 
ATOM   8093  N N   . GLU B 1 482 ? 59.803  42.753  -74.762 1.00 92.41  ? 482 GLU B N   1 
ATOM   8094  C CA  . GLU B 1 482 ? 58.612  42.321  -75.476 1.00 93.08  ? 482 GLU B CA  1 
ATOM   8095  C C   . GLU B 1 482 ? 58.379  40.846  -75.176 1.00 91.38  ? 482 GLU B C   1 
ATOM   8096  O O   . GLU B 1 482 ? 59.325  40.076  -75.146 1.00 92.12  ? 482 GLU B O   1 
ATOM   8097  C CB  . GLU B 1 482 ? 58.800  42.591  -76.972 1.00 95.76  ? 482 GLU B CB  1 
ATOM   8098  C CG  . GLU B 1 482 ? 57.603  42.225  -77.853 1.00 95.98  ? 482 GLU B CG  1 
ATOM   8099  C CD  . GLU B 1 482 ? 57.774  42.695  -79.289 1.00 98.61  ? 482 GLU B CD  1 
ATOM   8100  O OE1 . GLU B 1 482 ? 58.825  42.407  -79.906 1.00 100.97 ? 482 GLU B OE1 1 
ATOM   8101  O OE2 . GLU B 1 482 ? 56.872  43.370  -79.798 1.00 99.07  ? 482 GLU B OE2 1 
ATOM   8102  N N   . ASN B 1 483 ? 57.127  40.461  -74.936 1.00 90.61  ? 483 ASN B N   1 
ATOM   8103  C CA  . ASN B 1 483 ? 56.814  39.105  -74.520 1.00 89.61  ? 483 ASN B CA  1 
ATOM   8104  C C   . ASN B 1 483 ? 55.513  38.691  -75.191 1.00 89.36  ? 483 ASN B C   1 
ATOM   8105  O O   . ASN B 1 483 ? 54.646  39.525  -75.352 1.00 91.09  ? 483 ASN B O   1 
ATOM   8106  C CB  . ASN B 1 483 ? 56.760  38.990  -73.000 1.00 88.42  ? 483 ASN B CB  1 
ATOM   8107  C CG  . ASN B 1 483 ? 58.108  39.276  -72.377 1.00 89.45  ? 483 ASN B CG  1 
ATOM   8108  O OD1 . ASN B 1 483 ? 58.895  38.344  -72.143 1.00 88.06  ? 483 ASN B OD1 1 
ATOM   8109  N ND2 . ASN B 1 483 ? 58.404  40.554  -72.156 1.00 90.74  ? 483 ASN B ND2 1 
ATOM   8110  N N   . PHE B 1 484 ? 55.398  37.411  -75.566 1.00 88.88  ? 484 PHE B N   1 
ATOM   8111  C CA  . PHE B 1 484 ? 54.315  36.907  -76.397 1.00 88.81  ? 484 PHE B CA  1 
ATOM   8112  C C   . PHE B 1 484 ? 53.524  35.804  -75.675 1.00 88.16  ? 484 PHE B C   1 
ATOM   8113  O O   . PHE B 1 484 ? 54.083  34.979  -74.948 1.00 88.79  ? 484 PHE B O   1 
ATOM   8114  C CB  . PHE B 1 484 ? 54.982  36.444  -77.697 1.00 89.49  ? 484 PHE B CB  1 
ATOM   8115  C CG  . PHE B 1 484 ? 55.508  37.572  -78.571 1.00 90.42  ? 484 PHE B CG  1 
ATOM   8116  C CD1 . PHE B 1 484 ? 54.654  38.296  -79.393 1.00 91.41  ? 484 PHE B CD1 1 
ATOM   8117  C CD2 . PHE B 1 484 ? 56.854  37.902  -78.578 1.00 90.56  ? 484 PHE B CD2 1 
ATOM   8118  C CE1 . PHE B 1 484 ? 55.138  39.315  -80.195 1.00 93.28  ? 484 PHE B CE1 1 
ATOM   8119  C CE2 . PHE B 1 484 ? 57.329  38.925  -79.378 1.00 92.23  ? 484 PHE B CE2 1 
ATOM   8120  C CZ  . PHE B 1 484 ? 56.473  39.632  -80.181 1.00 93.59  ? 484 PHE B CZ  1 
ATOM   8121  N N   . PHE B 1 485 ? 52.207  35.757  -75.912 1.00 87.62  ? 485 PHE B N   1 
ATOM   8122  C CA  . PHE B 1 485 ? 51.377  34.725  -75.321 1.00 86.43  ? 485 PHE B CA  1 
ATOM   8123  C C   . PHE B 1 485 ? 50.221  34.366  -76.241 1.00 88.01  ? 485 PHE B C   1 
ATOM   8124  O O   . PHE B 1 485 ? 49.534  35.250  -76.748 1.00 89.35  ? 485 PHE B O   1 
ATOM   8125  C CB  . PHE B 1 485 ? 50.781  35.215  -74.008 1.00 85.00  ? 485 PHE B CB  1 
ATOM   8126  C CG  . PHE B 1 485 ? 51.824  35.835  -73.104 1.00 83.99  ? 485 PHE B CG  1 
ATOM   8127  C CD1 . PHE B 1 485 ? 52.191  37.157  -73.252 1.00 84.92  ? 485 PHE B CD1 1 
ATOM   8128  C CD2 . PHE B 1 485 ? 52.434  35.087  -72.122 1.00 82.88  ? 485 PHE B CD2 1 
ATOM   8129  C CE1 . PHE B 1 485 ? 53.142  37.716  -72.430 1.00 84.67  ? 485 PHE B CE1 1 
ATOM   8130  C CE2 . PHE B 1 485 ? 53.372  35.660  -71.292 1.00 82.71  ? 485 PHE B CE2 1 
ATOM   8131  C CZ  . PHE B 1 485 ? 53.727  36.969  -71.452 1.00 83.33  ? 485 PHE B CZ  1 
ATOM   8132  N N   . ASN B 1 486 ? 50.014  33.059  -76.416 1.00 88.38  ? 486 ASN B N   1 
ATOM   8133  C CA  . ASN B 1 486 ? 48.838  32.529  -77.082 1.00 90.89  ? 486 ASN B CA  1 
ATOM   8134  C C   . ASN B 1 486 ? 47.600  32.896  -76.262 1.00 88.97  ? 486 ASN B C   1 
ATOM   8135  O O   . ASN B 1 486 ? 47.658  32.838  -75.035 1.00 87.58  ? 486 ASN B O   1 
ATOM   8136  C CB  . ASN B 1 486 ? 48.932  31.013  -77.231 1.00 92.91  ? 486 ASN B CB  1 
ATOM   8137  C CG  . ASN B 1 486 ? 50.115  30.560  -78.054 1.00 96.30  ? 486 ASN B CG  1 
ATOM   8138  O OD1 . ASN B 1 486 ? 51.107  30.043  -77.518 1.00 98.56  ? 486 ASN B OD1 1 
ATOM   8139  N ND2 . ASN B 1 486 ? 50.028  30.731  -79.364 1.00 99.24  ? 486 ASN B ND2 1 
ATOM   8140  N N   . ILE B 1 487 ? 46.494  33.260  -76.935 1.00 88.97  ? 487 ILE B N   1 
ATOM   8141  C CA  . ILE B 1 487 ? 45.290  33.715  -76.248 1.00 87.98  ? 487 ILE B CA  1 
ATOM   8142  C C   . ILE B 1 487 ? 44.203  32.644  -76.356 1.00 87.67  ? 487 ILE B C   1 
ATOM   8143  O O   . ILE B 1 487 ? 43.571  32.505  -77.401 1.00 89.72  ? 487 ILE B O   1 
ATOM   8144  C CB  . ILE B 1 487 ? 44.746  35.047  -76.806 1.00 89.26  ? 487 ILE B CB  1 
ATOM   8145  C CG1 . ILE B 1 487 ? 45.760  36.207  -76.781 1.00 89.58  ? 487 ILE B CG1 1 
ATOM   8146  C CG2 . ILE B 1 487 ? 43.462  35.428  -76.065 1.00 88.81  ? 487 ILE B CG2 1 
ATOM   8147  C CD1 . ILE B 1 487 ? 45.210  37.517  -77.343 1.00 91.01  ? 487 ILE B CD1 1 
ATOM   8148  N N   . PRO B 1 488 ? 43.849  31.927  -75.266 1.00 84.97  ? 488 PRO B N   1 
ATOM   8149  C CA  . PRO B 1 488 ? 42.777  30.938  -75.339 1.00 84.80  ? 488 PRO B CA  1 
ATOM   8150  C C   . PRO B 1 488 ? 41.533  31.568  -75.963 1.00 85.71  ? 488 PRO B C   1 
ATOM   8151  O O   . PRO B 1 488 ? 41.330  32.777  -75.855 1.00 85.84  ? 488 PRO B O   1 
ATOM   8152  C CB  . PRO B 1 488 ? 42.547  30.522  -73.876 1.00 83.21  ? 488 PRO B CB  1 
ATOM   8153  C CG  . PRO B 1 488 ? 43.825  30.901  -73.163 1.00 81.87  ? 488 PRO B CG  1 
ATOM   8154  C CD  . PRO B 1 488 ? 44.403  32.082  -73.912 1.00 82.77  ? 488 PRO B CD  1 
ATOM   8155  N N   . ASP B 1 489 ? 40.688  30.727  -76.580 1.00 86.45  ? 489 ASP B N   1 
ATOM   8156  C CA  . ASP B 1 489 ? 39.440  31.157  -77.210 1.00 86.96  ? 489 ASP B CA  1 
ATOM   8157  C C   . ASP B 1 489 ? 38.278  31.197  -76.216 1.00 85.96  ? 489 ASP B C   1 
ATOM   8158  O O   . ASP B 1 489 ? 37.186  31.632  -76.581 1.00 87.26  ? 489 ASP B O   1 
ATOM   8159  C CB  . ASP B 1 489 ? 39.100  30.287  -78.414 1.00 88.26  ? 489 ASP B CB  1 
ATOM   8160  C CG  . ASP B 1 489 ? 40.065  30.386  -79.589 1.00 89.01  ? 489 ASP B CG  1 
ATOM   8161  O OD1 . ASP B 1 489 ? 41.014  31.210  -79.521 1.00 87.95  ? 489 ASP B OD1 1 
ATOM   8162  O OD2 . ASP B 1 489 ? 39.850  29.655  -80.570 1.00 90.31  ? 489 ASP B OD2 1 
ATOM   8163  N N   . ASN B 1 490 ? 38.507  30.712  -74.985 1.00 84.34  ? 490 ASN B N   1 
ATOM   8164  C CA  . ASN B 1 490 ? 37.527  30.767  -73.906 1.00 83.83  ? 490 ASN B CA  1 
ATOM   8165  C C   . ASN B 1 490 ? 38.024  31.692  -72.795 1.00 82.07  ? 490 ASN B C   1 
ATOM   8166  O O   . ASN B 1 490 ? 37.507  31.667  -71.669 1.00 80.88  ? 490 ASN B O   1 
ATOM   8167  C CB  . ASN B 1 490 ? 37.226  29.380  -73.352 1.00 83.85  ? 490 ASN B CB  1 
ATOM   8168  C CG  . ASN B 1 490 ? 38.449  28.769  -72.723 1.00 83.09  ? 490 ASN B CG  1 
ATOM   8169  O OD1 . ASN B 1 490 ? 39.558  29.040  -73.188 1.00 84.48  ? 490 ASN B OD1 1 
ATOM   8170  N ND2 . ASN B 1 490 ? 38.298  28.000  -71.655 1.00 82.51  ? 490 ASN B ND2 1 
ATOM   8171  N N   . CYS B 1 491 ? 39.059  32.478  -73.134 1.00 81.78  ? 491 CYS B N   1 
ATOM   8172  C CA  . CYS B 1 491 ? 39.532  33.562  -72.294 1.00 80.68  ? 491 CYS B CA  1 
ATOM   8173  C C   . CYS B 1 491 ? 38.623  34.776  -72.453 1.00 82.15  ? 491 CYS B C   1 
ATOM   8174  O O   . CYS B 1 491 ? 38.581  35.411  -73.508 1.00 83.81  ? 491 CYS B O   1 
ATOM   8175  C CB  . CYS B 1 491 ? 40.941  34.009  -72.661 1.00 79.91  ? 491 CYS B CB  1 
ATOM   8176  S SG  . CYS B 1 491 ? 41.452  35.444  -71.685 1.00 78.22  ? 491 CYS B SG  1 
ATOM   8177  N N   . TRP B 1 492 ? 37.896  35.114  -71.392 1.00 82.02  ? 492 TRP B N   1 
ATOM   8178  C CA  . TRP B 1 492 ? 36.885  36.150  -71.521 1.00 83.40  ? 492 TRP B CA  1 
ATOM   8179  C C   . TRP B 1 492 ? 37.475  37.497  -71.119 1.00 82.71  ? 492 TRP B C   1 
ATOM   8180  O O   . TRP B 1 492 ? 37.184  38.513  -71.737 1.00 83.73  ? 492 TRP B O   1 
ATOM   8181  C CB  . TRP B 1 492 ? 35.640  35.774  -70.703 1.00 83.74  ? 492 TRP B CB  1 
ATOM   8182  C CG  . TRP B 1 492 ? 35.133  34.378  -70.983 1.00 84.33  ? 492 TRP B CG  1 
ATOM   8183  C CD1 . TRP B 1 492 ? 34.859  33.416  -70.054 1.00 83.83  ? 492 TRP B CD1 1 
ATOM   8184  C CD2 . TRP B 1 492 ? 34.850  33.775  -72.267 1.00 85.47  ? 492 TRP B CD2 1 
ATOM   8185  N NE1 . TRP B 1 492 ? 34.417  32.272  -70.660 1.00 84.17  ? 492 TRP B NE1 1 
ATOM   8186  C CE2 . TRP B 1 492 ? 34.407  32.461  -72.014 1.00 85.25  ? 492 TRP B CE2 1 
ATOM   8187  C CE3 . TRP B 1 492 ? 34.928  34.209  -73.596 1.00 86.88  ? 492 TRP B CE3 1 
ATOM   8188  C CZ2 . TRP B 1 492 ? 34.050  31.590  -73.036 1.00 86.59  ? 492 TRP B CZ2 1 
ATOM   8189  C CZ3 . TRP B 1 492 ? 34.594  33.338  -74.608 1.00 88.09  ? 492 TRP B CZ3 1 
ATOM   8190  C CH2 . TRP B 1 492 ? 34.156  32.047  -74.329 1.00 87.99  ? 492 TRP B CH2 1 
ATOM   8191  N N   . VAL B 1 493 ? 38.313  37.476  -70.082 1.00 81.25  ? 493 VAL B N   1 
ATOM   8192  C CA  . VAL B 1 493 ? 39.075  38.644  -69.686 1.00 81.02  ? 493 VAL B CA  1 
ATOM   8193  C C   . VAL B 1 493 ? 40.495  38.200  -69.331 1.00 79.90  ? 493 VAL B C   1 
ATOM   8194  O O   . VAL B 1 493 ? 40.726  37.034  -68.982 1.00 77.78  ? 493 VAL B O   1 
ATOM   8195  C CB  . VAL B 1 493 ? 38.374  39.353  -68.517 1.00 80.65  ? 493 VAL B CB  1 
ATOM   8196  C CG1 . VAL B 1 493 ? 38.411  38.497  -67.258 1.00 79.37  ? 493 VAL B CG1 1 
ATOM   8197  C CG2 . VAL B 1 493 ? 38.925  40.749  -68.251 1.00 80.80  ? 493 VAL B CG2 1 
ATOM   8198  N N   . VAL B 1 494 ? 41.428  39.158  -69.469 1.00 80.50  ? 494 VAL B N   1 
ATOM   8199  C CA  . VAL B 1 494 ? 42.816  38.970  -69.084 1.00 79.85  ? 494 VAL B CA  1 
ATOM   8200  C C   . VAL B 1 494 ? 43.221  40.107  -68.148 1.00 79.38  ? 494 VAL B C   1 
ATOM   8201  O O   . VAL B 1 494 ? 42.485  41.084  -68.044 1.00 81.12  ? 494 VAL B O   1 
ATOM   8202  C CB  . VAL B 1 494 ? 43.710  38.878  -70.336 1.00 81.20  ? 494 VAL B CB  1 
ATOM   8203  C CG1 . VAL B 1 494 ? 43.743  40.175  -71.133 1.00 82.96  ? 494 VAL B CG1 1 
ATOM   8204  C CG2 . VAL B 1 494 ? 45.122  38.397  -70.001 1.00 80.50  ? 494 VAL B CG2 1 
ATOM   8205  N N   . ASN B 1 495 ? 44.313  39.888  -67.397 1.00 78.00  ? 495 ASN B N   1 
ATOM   8206  C CA  . ASN B 1 495 ? 45.005  40.881  -66.587 1.00 77.44  ? 495 ASN B CA  1 
ATOM   8207  C C   . ASN B 1 495 ? 46.503  40.797  -66.896 1.00 77.89  ? 495 ASN B C   1 
ATOM   8208  O O   . ASN B 1 495 ? 47.277  40.084  -66.238 1.00 76.61  ? 495 ASN B O   1 
ATOM   8209  C CB  . ASN B 1 495 ? 44.755  40.681  -65.095 1.00 75.80  ? 495 ASN B CB  1 
ATOM   8210  C CG  . ASN B 1 495 ? 45.558  41.648  -64.260 1.00 75.66  ? 495 ASN B CG  1 
ATOM   8211  O OD1 . ASN B 1 495 ? 46.680  41.993  -64.640 1.00 76.88  ? 495 ASN B OD1 1 
ATOM   8212  N ND2 . ASN B 1 495 ? 45.028  42.108  -63.137 1.00 75.30  ? 495 ASN B ND2 1 
ATOM   8213  N N   . ALA B 1 496 ? 46.894  41.531  -67.940 1.00 80.06  ? 496 ALA B N   1 
ATOM   8214  C CA  . ALA B 1 496 ? 48.288  41.699  -68.318 1.00 80.73  ? 496 ALA B CA  1 
ATOM   8215  C C   . ALA B 1 496 ? 48.990  42.626  -67.327 1.00 81.35  ? 496 ALA B C   1 
ATOM   8216  O O   . ALA B 1 496 ? 48.639  43.795  -67.195 1.00 82.29  ? 496 ALA B O   1 
ATOM   8217  C CB  . ALA B 1 496 ? 48.379  42.247  -69.726 1.00 82.27  ? 496 ALA B CB  1 
ATOM   8218  N N   . SER B 1 497 ? 49.985  42.080  -66.633 1.00 81.33  ? 497 SER B N   1 
ATOM   8219  C CA  . SER B 1 497 ? 50.693  42.811  -65.602 1.00 82.51  ? 497 SER B CA  1 
ATOM   8220  C C   . SER B 1 497 ? 52.185  42.519  -65.702 1.00 82.49  ? 497 SER B C   1 
ATOM   8221  O O   . SER B 1 497 ? 52.591  41.413  -66.061 1.00 83.04  ? 497 SER B O   1 
ATOM   8222  C CB  . SER B 1 497 ? 50.162  42.455  -64.238 1.00 82.61  ? 497 SER B CB  1 
ATOM   8223  O OG  . SER B 1 497 ? 50.114  41.045  -64.042 1.00 82.57  ? 497 SER B OG  1 
ATOM   8224  N N   . ALA B 1 498 ? 52.993  43.528  -65.383 1.00 82.64  ? 498 ALA B N   1 
ATOM   8225  C CA  . ALA B 1 498 ? 54.423  43.348  -65.263 1.00 82.36  ? 498 ALA B CA  1 
ATOM   8226  C C   . ALA B 1 498 ? 54.903  44.132  -64.049 1.00 82.63  ? 498 ALA B C   1 
ATOM   8227  O O   . ALA B 1 498 ? 54.197  45.023  -63.576 1.00 81.60  ? 498 ALA B O   1 
ATOM   8228  C CB  . ALA B 1 498 ? 55.103  43.772  -66.540 1.00 84.22  ? 498 ALA B CB  1 
ATOM   8229  N N   . GLY B 1 499 ? 56.087  43.764  -63.528 1.00 82.97  ? 499 GLY B N   1 
ATOM   8230  C CA  . GLY B 1 499 ? 56.615  44.433  -62.349 1.00 83.30  ? 499 GLY B CA  1 
ATOM   8231  C C   . GLY B 1 499 ? 58.015  43.969  -61.980 1.00 82.45  ? 499 GLY B C   1 
ATOM   8232  O O   . GLY B 1 499 ? 58.381  42.852  -62.324 1.00 82.01  ? 499 GLY B O   1 
ATOM   8233  N N   . ILE B 1 500 ? 58.753  44.836  -61.261 1.00 83.21  ? 500 ILE B N   1 
ATOM   8234  C CA  . ILE B 1 500 ? 60.150  44.612  -60.901 1.00 83.19  ? 500 ILE B CA  1 
ATOM   8235  C C   . ILE B 1 500 ? 60.465  45.282  -59.560 1.00 84.01  ? 500 ILE B C   1 
ATOM   8236  O O   . ILE B 1 500 ? 59.924  46.332  -59.226 1.00 85.05  ? 500 ILE B O   1 
ATOM   8237  C CB  . ILE B 1 500 ? 61.094  45.092  -62.019 1.00 84.13  ? 500 ILE B CB  1 
ATOM   8238  C CG1 . ILE B 1 500 ? 62.511  44.566  -61.817 1.00 83.72  ? 500 ILE B CG1 1 
ATOM   8239  C CG2 . ILE B 1 500 ? 61.076  46.613  -62.149 1.00 86.43  ? 500 ILE B CG2 1 
ATOM   8240  C CD1 . ILE B 1 500 ? 63.471  44.898  -62.944 1.00 85.03  ? 500 ILE B CD1 1 
ATOM   8241  N N   . SER B 1 501 ? 61.364  44.661  -58.789 1.00 84.99  ? 501 SER B N   1 
ATOM   8242  C CA  . SER B 1 501 ? 61.676  45.108  -57.440 1.00 86.53  ? 501 SER B CA  1 
ATOM   8243  C C   . SER B 1 501 ? 62.752  46.192  -57.477 1.00 89.65  ? 501 SER B C   1 
ATOM   8244  O O   . SER B 1 501 ? 63.757  46.044  -58.175 1.00 91.10  ? 501 SER B O   1 
ATOM   8245  C CB  . SER B 1 501 ? 62.110  43.944  -56.594 1.00 85.26  ? 501 SER B CB  1 
ATOM   8246  O OG  . SER B 1 501 ? 61.039  43.031  -56.395 1.00 83.46  ? 501 SER B OG  1 
ATOM   8247  N N   . VAL B 1 502 ? 62.531  47.276  -56.715 1.00 90.83  ? 502 VAL B N   1 
ATOM   8248  C CA  . VAL B 1 502 ? 63.429  48.424  -56.711 1.00 92.41  ? 502 VAL B CA  1 
ATOM   8249  C C   . VAL B 1 502 ? 63.849  48.722  -55.278 1.00 92.20  ? 502 VAL B C   1 
ATOM   8250  O O   . VAL B 1 502 ? 63.082  48.532  -54.341 1.00 91.26  ? 502 VAL B O   1 
ATOM   8251  C CB  . VAL B 1 502 ? 62.799  49.679  -57.331 1.00 95.01  ? 502 VAL B CB  1 
ATOM   8252  C CG1 . VAL B 1 502 ? 63.800  50.817  -57.415 1.00 98.17  ? 502 VAL B CG1 1 
ATOM   8253  C CG2 . VAL B 1 502 ? 62.208  49.404  -58.703 1.00 95.67  ? 502 VAL B CG2 1 
ATOM   8254  N N   . ARG B 1 503 ? 65.075  49.223  -55.133 1.00 94.24  ? 503 ARG B N   1 
ATOM   8255  C CA  . ARG B 1 503 ? 65.683  49.410  -53.830 1.00 94.96  ? 503 ARG B CA  1 
ATOM   8256  C C   . ARG B 1 503 ? 66.273  50.819  -53.728 1.00 95.82  ? 503 ARG B C   1 
ATOM   8257  O O   . ARG B 1 503 ? 67.022  51.257  -54.611 1.00 96.89  ? 503 ARG B O   1 
ATOM   8258  C CB  . ARG B 1 503 ? 66.783  48.359  -53.621 1.00 95.30  ? 503 ARG B CB  1 
ATOM   8259  C CG  . ARG B 1 503 ? 67.424  48.404  -52.240 1.00 97.90  ? 503 ARG B CG  1 
ATOM   8260  C CD  . ARG B 1 503 ? 68.723  47.594  -52.087 1.00 99.88  ? 503 ARG B CD  1 
ATOM   8261  N NE  . ARG B 1 503 ? 68.525  46.138  -52.061 1.00 99.19  ? 503 ARG B NE  1 
ATOM   8262  C CZ  . ARG B 1 503 ? 67.875  45.426  -51.138 1.00 98.78  ? 503 ARG B CZ  1 
ATOM   8263  N NH1 . ARG B 1 503 ? 67.301  45.993  -50.085 1.00 98.29  ? 503 ARG B NH1 1 
ATOM   8264  N NH2 . ARG B 1 503 ? 67.808  44.113  -51.279 1.00 99.34  ? 503 ARG B NH2 1 
ATOM   8265  N N   . TYR B 1 504 ? 65.923  51.515  -52.633 1.00 93.59  ? 504 TYR B N   1 
ATOM   8266  C CA  . TYR B 1 504 ? 66.715  52.630  -52.126 1.00 93.82  ? 504 TYR B CA  1 
ATOM   8267  C C   . TYR B 1 504 ? 67.228  52.230  -50.737 1.00 92.59  ? 504 TYR B C   1 
ATOM   8268  O O   . TYR B 1 504 ? 66.430  51.916  -49.856 1.00 91.26  ? 504 TYR B O   1 
ATOM   8269  C CB  . TYR B 1 504 ? 65.905  53.940  -52.127 1.00 94.68  ? 504 TYR B CB  1 
ATOM   8270  C CG  . TYR B 1 504 ? 66.712  55.190  -51.790 1.00 96.49  ? 504 TYR B CG  1 
ATOM   8271  C CD1 . TYR B 1 504 ? 66.955  55.548  -50.468 1.00 96.75  ? 504 TYR B CD1 1 
ATOM   8272  C CD2 . TYR B 1 504 ? 67.262  55.995  -52.784 1.00 98.28  ? 504 TYR B CD2 1 
ATOM   8273  C CE1 . TYR B 1 504 ? 67.721  56.657  -50.143 1.00 99.47  ? 504 TYR B CE1 1 
ATOM   8274  C CE2 . TYR B 1 504 ? 68.025  57.116  -52.471 1.00 101.03 ? 504 TYR B CE2 1 
ATOM   8275  C CZ  . TYR B 1 504 ? 68.254  57.448  -51.144 1.00 101.54 ? 504 TYR B CZ  1 
ATOM   8276  O OH  . TYR B 1 504 ? 68.983  58.533  -50.750 1.00 103.86 ? 504 TYR B OH  1 
ATOM   8277  N N   . GLY B 1 505 ? 68.559  52.209  -50.547 1.00 92.79  ? 505 GLY B N   1 
ATOM   8278  C CA  . GLY B 1 505 ? 69.147  51.886  -49.253 1.00 91.98  ? 505 GLY B CA  1 
ATOM   8279  C C   . GLY B 1 505 ? 68.586  50.572  -48.707 1.00 88.57  ? 505 GLY B C   1 
ATOM   8280  O O   . GLY B 1 505 ? 68.847  49.520  -49.278 1.00 86.38  ? 505 GLY B O   1 
ATOM   8281  N N   . LYS B 1 506 ? 67.811  50.644  -47.615 1.00 87.88  ? 506 LYS B N   1 
ATOM   8282  C CA  . LYS B 1 506 ? 67.197  49.470  -47.001 1.00 85.82  ? 506 LYS B CA  1 
ATOM   8283  C C   . LYS B 1 506 ? 65.763  49.239  -47.498 1.00 84.32  ? 506 LYS B C   1 
ATOM   8284  O O   . LYS B 1 506 ? 65.199  48.162  -47.277 1.00 82.05  ? 506 LYS B O   1 
ATOM   8285  C CB  . LYS B 1 506 ? 67.122  49.559  -45.472 1.00 86.38  ? 506 LYS B CB  1 
ATOM   8286  C CG  . LYS B 1 506 ? 68.429  49.406  -44.734 1.00 87.63  ? 506 LYS B CG  1 
ATOM   8287  C CD  . LYS B 1 506 ? 68.275  49.407  -43.217 1.00 88.51  ? 506 LYS B CD  1 
ATOM   8288  C CE  . LYS B 1 506 ? 69.622  49.609  -42.578 1.00 91.00  ? 506 LYS B CE  1 
ATOM   8289  N NZ  . LYS B 1 506 ? 69.555  50.042  -41.178 1.00 92.75  ? 506 LYS B NZ  1 
ATOM   8290  N N   . PHE B 1 507 ? 65.177  50.246  -48.163 1.00 85.11  ? 507 PHE B N   1 
ATOM   8291  C CA  . PHE B 1 507 ? 63.788  50.204  -48.593 1.00 83.84  ? 507 PHE B CA  1 
ATOM   8292  C C   . PHE B 1 507 ? 63.679  49.497  -49.945 1.00 82.76  ? 507 PHE B C   1 
ATOM   8293  O O   . PHE B 1 507 ? 64.299  49.936  -50.926 1.00 83.32  ? 507 PHE B O   1 
ATOM   8294  C CB  . PHE B 1 507 ? 63.347  51.668  -48.595 1.00 85.79  ? 507 PHE B CB  1 
ATOM   8295  C CG  . PHE B 1 507 ? 61.924  51.995  -49.019 1.00 85.72  ? 507 PHE B CG  1 
ATOM   8296  C CD1 . PHE B 1 507 ? 61.582  52.120  -50.362 1.00 85.66  ? 507 PHE B CD1 1 
ATOM   8297  C CD2 . PHE B 1 507 ? 60.952  52.254  -48.059 1.00 86.17  ? 507 PHE B CD2 1 
ATOM   8298  C CE1 . PHE B 1 507 ? 60.293  52.460  -50.730 1.00 86.08  ? 507 PHE B CE1 1 
ATOM   8299  C CE2 . PHE B 1 507 ? 59.662  52.589  -48.431 1.00 86.49  ? 507 PHE B CE2 1 
ATOM   8300  C CZ  . PHE B 1 507 ? 59.333  52.690  -49.765 1.00 86.58  ? 507 PHE B CZ  1 
ATOM   8301  N N   . THR B 1 508 ? 62.866  48.421  -49.980 1.00 80.38  ? 508 THR B N   1 
ATOM   8302  C CA  . THR B 1 508 ? 62.556  47.747  -51.227 1.00 79.78  ? 508 THR B CA  1 
ATOM   8303  C C   . THR B 1 508 ? 61.083  47.939  -51.567 1.00 79.64  ? 508 THR B C   1 
ATOM   8304  O O   . THR B 1 508 ? 60.228  47.954  -50.688 1.00 79.46  ? 508 THR B O   1 
ATOM   8305  C CB  . THR B 1 508 ? 62.924  46.271  -51.107 1.00 78.91  ? 508 THR B CB  1 
ATOM   8306  O OG1 . THR B 1 508 ? 62.451  45.910  -49.812 1.00 78.65  ? 508 THR B OG1 1 
ATOM   8307  C CG2 . THR B 1 508 ? 64.422  46.037  -51.238 1.00 79.71  ? 508 THR B CG2 1 
ATOM   8308  N N   . PHE B 1 509 ? 60.788  48.079  -52.862 1.00 80.09  ? 509 PHE B N   1 
ATOM   8309  C CA  . PHE B 1 509 ? 59.414  48.172  -53.316 1.00 79.81  ? 509 PHE B CA  1 
ATOM   8310  C C   . PHE B 1 509 ? 59.338  47.731  -54.771 1.00 80.19  ? 509 PHE B C   1 
ATOM   8311  O O   . PHE B 1 509 ? 60.366  47.437  -55.389 1.00 80.25  ? 509 PHE B O   1 
ATOM   8312  C CB  . PHE B 1 509 ? 58.905  49.604  -53.146 1.00 81.81  ? 509 PHE B CB  1 
ATOM   8313  C CG  . PHE B 1 509 ? 59.552  50.653  -54.040 1.00 83.67  ? 509 PHE B CG  1 
ATOM   8314  C CD1 . PHE B 1 509 ? 60.769  51.230  -53.690 1.00 84.84  ? 509 PHE B CD1 1 
ATOM   8315  C CD2 . PHE B 1 509 ? 58.920  51.095  -55.200 1.00 84.19  ? 509 PHE B CD2 1 
ATOM   8316  C CE1 . PHE B 1 509 ? 61.340  52.214  -54.486 1.00 87.06  ? 509 PHE B CE1 1 
ATOM   8317  C CE2 . PHE B 1 509 ? 59.498  52.083  -55.991 1.00 86.31  ? 509 PHE B CE2 1 
ATOM   8318  C CZ  . PHE B 1 509 ? 60.711  52.629  -55.641 1.00 87.79  ? 509 PHE B CZ  1 
ATOM   8319  N N   . LYS B 1 510 ? 58.109  47.701  -55.300 1.00 80.79  ? 510 LYS B N   1 
ATOM   8320  C CA  . LYS B 1 510 ? 57.872  47.190  -56.637 1.00 81.76  ? 510 LYS B CA  1 
ATOM   8321  C C   . LYS B 1 510 ? 57.240  48.266  -57.512 1.00 83.69  ? 510 LYS B C   1 
ATOM   8322  O O   . LYS B 1 510 ? 56.281  48.898  -57.099 1.00 85.24  ? 510 LYS B O   1 
ATOM   8323  C CB  . LYS B 1 510 ? 57.005  45.928  -56.564 1.00 80.16  ? 510 LYS B CB  1 
ATOM   8324  C CG  . LYS B 1 510 ? 57.704  44.731  -55.943 1.00 78.99  ? 510 LYS B CG  1 
ATOM   8325  C CD  . LYS B 1 510 ? 56.956  43.411  -56.115 1.00 78.69  ? 510 LYS B CD  1 
ATOM   8326  C CE  . LYS B 1 510 ? 57.063  42.767  -57.484 1.00 78.99  ? 510 LYS B CE  1 
ATOM   8327  N NZ  . LYS B 1 510 ? 58.335  42.072  -57.714 1.00 78.97  ? 510 LYS B NZ  1 
ATOM   8328  N N   . ILE B 1 511 ? 57.786  48.443  -58.723 1.00 85.09  ? 511 ILE B N   1 
ATOM   8329  C CA  . ILE B 1 511 ? 57.154  49.240  -59.767 1.00 87.10  ? 511 ILE B CA  1 
ATOM   8330  C C   . ILE B 1 511 ? 56.522  48.295  -60.791 1.00 85.62  ? 511 ILE B C   1 
ATOM   8331  O O   . ILE B 1 511 ? 57.046  47.213  -61.045 1.00 83.99  ? 511 ILE B O   1 
ATOM   8332  C CB  . ILE B 1 511 ? 58.153  50.216  -60.415 1.00 89.90  ? 511 ILE B CB  1 
ATOM   8333  C CG1 . ILE B 1 511 ? 59.326  49.482  -61.107 1.00 90.46  ? 511 ILE B CG1 1 
ATOM   8334  C CG2 . ILE B 1 511 ? 58.644  51.235  -59.385 1.00 91.01  ? 511 ILE B CG2 1 
ATOM   8335  C CD1 . ILE B 1 511 ? 60.326  50.407  -61.791 1.00 93.17  ? 511 ILE B CD1 1 
ATOM   8336  N N   . HIS B 1 512 ? 55.404  48.726  -61.399 1.00 85.37  ? 512 HIS B N   1 
ATOM   8337  C CA  . HIS B 1 512 ? 54.553  47.817  -62.145 1.00 82.71  ? 512 HIS B CA  1 
ATOM   8338  C C   . HIS B 1 512 ? 53.499  48.577  -62.953 1.00 82.74  ? 512 HIS B C   1 
ATOM   8339  O O   . HIS B 1 512 ? 53.362  49.783  -62.805 1.00 84.97  ? 512 HIS B O   1 
ATOM   8340  C CB  . HIS B 1 512 ? 53.928  46.881  -61.120 1.00 80.90  ? 512 HIS B CB  1 
ATOM   8341  C CG  . HIS B 1 512 ? 53.320  47.643  -59.986 1.00 81.31  ? 512 HIS B CG  1 
ATOM   8342  N ND1 . HIS B 1 512 ? 52.122  48.317  -60.098 1.00 81.50  ? 512 HIS B ND1 1 
ATOM   8343  C CD2 . HIS B 1 512 ? 53.741  47.823  -58.722 1.00 80.93  ? 512 HIS B CD2 1 
ATOM   8344  C CE1 . HIS B 1 512 ? 51.834  48.876  -58.929 1.00 81.91  ? 512 HIS B CE1 1 
ATOM   8345  N NE2 . HIS B 1 512 ? 52.793  48.578  -58.076 1.00 81.21  ? 512 HIS B NE2 1 
ATOM   8346  N N   . ASP B 1 513 ? 52.794  47.868  -63.840 1.00 81.19  ? 513 ASP B N   1 
ATOM   8347  C CA  . ASP B 1 513 ? 51.637  48.409  -64.531 1.00 82.03  ? 513 ASP B CA  1 
ATOM   8348  C C   . ASP B 1 513 ? 50.666  47.269  -64.846 1.00 80.58  ? 513 ASP B C   1 
ATOM   8349  O O   . ASP B 1 513 ? 51.115  46.140  -65.027 1.00 78.67  ? 513 ASP B O   1 
ATOM   8350  C CB  . ASP B 1 513 ? 52.020  49.216  -65.768 1.00 83.83  ? 513 ASP B CB  1 
ATOM   8351  C CG  . ASP B 1 513 ? 50.942  50.187  -66.250 1.00 85.42  ? 513 ASP B CG  1 
ATOM   8352  O OD1 . ASP B 1 513 ? 49.970  50.403  -65.486 1.00 84.79  ? 513 ASP B OD1 1 
ATOM   8353  O OD2 . ASP B 1 513 ? 51.062  50.710  -67.387 1.00 87.04  ? 513 ASP B OD2 1 
ATOM   8354  N N   . GLN B 1 514 ? 49.355  47.592  -64.945 1.00 80.99  ? 514 GLN B N   1 
ATOM   8355  C CA  . GLN B 1 514 ? 48.285  46.598  -65.044 1.00 79.98  ? 514 GLN B CA  1 
ATOM   8356  C C   . GLN B 1 514 ? 47.285  47.015  -66.126 1.00 82.12  ? 514 GLN B C   1 
ATOM   8357  O O   . GLN B 1 514 ? 46.864  48.178  -66.152 1.00 84.21  ? 514 GLN B O   1 
ATOM   8358  C CB  . GLN B 1 514 ? 47.626  46.454  -63.663 1.00 78.40  ? 514 GLN B CB  1 
ATOM   8359  C CG  . GLN B 1 514 ? 46.354  45.603  -63.584 1.00 76.92  ? 514 GLN B CG  1 
ATOM   8360  C CD  . GLN B 1 514 ? 45.752  45.537  -62.189 1.00 75.46  ? 514 GLN B CD  1 
ATOM   8361  O OE1 . GLN B 1 514 ? 45.663  44.477  -61.554 1.00 73.47  ? 514 GLN B OE1 1 
ATOM   8362  N NE2 . GLN B 1 514 ? 45.326  46.685  -61.690 1.00 76.31  ? 514 GLN B NE2 1 
ATOM   8363  N N   . LYS B 1 515 ? 46.897  46.062  -66.999 1.00 81.87  ? 515 LYS B N   1 
ATOM   8364  C CA  . LYS B 1 515 ? 45.850  46.312  -67.986 1.00 83.64  ? 515 LYS B CA  1 
ATOM   8365  C C   . LYS B 1 515 ? 44.829  45.178  -67.972 1.00 82.50  ? 515 LYS B C   1 
ATOM   8366  O O   . LYS B 1 515 ? 45.173  44.024  -68.248 1.00 80.82  ? 515 LYS B O   1 
ATOM   8367  C CB  . LYS B 1 515 ? 46.283  46.463  -69.452 1.00 85.33  ? 515 LYS B CB  1 
ATOM   8368  C CG  . LYS B 1 515 ? 47.185  47.651  -69.812 1.00 87.45  ? 515 LYS B CG  1 
ATOM   8369  C CD  . LYS B 1 515 ? 46.888  49.059  -69.296 1.00 88.69  ? 515 LYS B CD  1 
ATOM   8370  C CE  . LYS B 1 515 ? 48.109  49.941  -69.465 1.00 90.33  ? 515 LYS B CE  1 
ATOM   8371  N NZ  . LYS B 1 515 ? 48.242  50.978  -68.433 1.00 91.20  ? 515 LYS B NZ  1 
ATOM   8372  N N   . ILE B 1 516 ? 43.568  45.546  -67.678 1.00 83.04  ? 516 ILE B N   1 
ATOM   8373  C CA  . ILE B 1 516 ? 42.459  44.602  -67.693 1.00 82.75  ? 516 ILE B CA  1 
ATOM   8374  C C   . ILE B 1 516 ? 41.696  44.758  -69.007 1.00 84.37  ? 516 ILE B C   1 
ATOM   8375  O O   . ILE B 1 516 ? 41.110  45.812  -69.262 1.00 86.56  ? 516 ILE B O   1 
ATOM   8376  C CB  . ILE B 1 516 ? 41.533  44.766  -66.476 1.00 82.50  ? 516 ILE B CB  1 
ATOM   8377  C CG1 . ILE B 1 516 ? 42.279  44.576  -65.147 1.00 81.42  ? 516 ILE B CG1 1 
ATOM   8378  C CG2 . ILE B 1 516 ? 40.354  43.804  -66.598 1.00 82.28  ? 516 ILE B CG2 1 
ATOM   8379  C CD1 . ILE B 1 516 ? 41.422  44.773  -63.902 1.00 81.41  ? 516 ILE B CD1 1 
ATOM   8380  N N   . ILE B 1 517 ? 41.691  43.680  -69.806 1.00 83.77  ? 517 ILE B N   1 
ATOM   8381  C CA  . ILE B 1 517 ? 41.223  43.719  -71.181 1.00 85.56  ? 517 ILE B CA  1 
ATOM   8382  C C   . ILE B 1 517 ? 40.262  42.555  -71.401 1.00 86.12  ? 517 ILE B C   1 
ATOM   8383  O O   . ILE B 1 517 ? 40.623  41.410  -71.118 1.00 85.07  ? 517 ILE B O   1 
ATOM   8384  C CB  . ILE B 1 517 ? 42.384  43.672  -72.190 1.00 85.68  ? 517 ILE B CB  1 
ATOM   8385  C CG1 . ILE B 1 517 ? 43.471  44.733  -71.892 1.00 85.91  ? 517 ILE B CG1 1 
ATOM   8386  C CG2 . ILE B 1 517 ? 41.840  43.779  -73.616 1.00 87.49  ? 517 ILE B CG2 1 
ATOM   8387  C CD1 . ILE B 1 517 ? 44.797  44.505  -72.605 1.00 85.73  ? 517 ILE B CD1 1 
ATOM   8388  N N   . TYR B 1 518 ? 39.059  42.887  -71.913 1.00 87.53  ? 518 TYR B N   1 
ATOM   8389  C CA  . TYR B 1 518 ? 38.006  41.926  -72.177 1.00 87.33  ? 518 TYR B CA  1 
ATOM   8390  C C   . TYR B 1 518 ? 38.050  41.436  -73.626 1.00 88.51  ? 518 TYR B C   1 
ATOM   8391  O O   . TYR B 1 518 ? 38.805  41.938  -74.449 1.00 90.00  ? 518 TYR B O   1 
ATOM   8392  C CB  . TYR B 1 518 ? 36.696  42.643  -71.840 1.00 88.57  ? 518 TYR B CB  1 
ATOM   8393  C CG  . TYR B 1 518 ? 36.580  43.152  -70.405 1.00 87.84  ? 518 TYR B CG  1 
ATOM   8394  C CD1 . TYR B 1 518 ? 36.124  42.332  -69.378 1.00 86.55  ? 518 TYR B CD1 1 
ATOM   8395  C CD2 . TYR B 1 518 ? 36.922  44.456  -70.073 1.00 88.76  ? 518 TYR B CD2 1 
ATOM   8396  C CE1 . TYR B 1 518 ? 36.025  42.787  -68.071 1.00 85.94  ? 518 TYR B CE1 1 
ATOM   8397  C CE2 . TYR B 1 518 ? 36.808  44.931  -68.775 1.00 87.97  ? 518 TYR B CE2 1 
ATOM   8398  C CZ  . TYR B 1 518 ? 36.363  44.095  -67.769 1.00 86.52  ? 518 TYR B CZ  1 
ATOM   8399  O OH  . TYR B 1 518 ? 36.257  44.560  -66.489 1.00 85.96  ? 518 TYR B OH  1 
ATOM   8400  N N   . ARG B 1 519 ? 37.253  40.399  -73.904 1.00 88.59  ? 519 ARG B N   1 
ATOM   8401  C CA  . ARG B 1 519 ? 36.885  39.985  -75.250 1.00 89.87  ? 519 ARG B CA  1 
ATOM   8402  C C   . ARG B 1 519 ? 35.470  40.483  -75.523 1.00 91.72  ? 519 ARG B C   1 
ATOM   8403  O O   . ARG B 1 519 ? 34.569  40.204  -74.746 1.00 91.15  ? 519 ARG B O   1 
ATOM   8404  C CB  . ARG B 1 519 ? 36.884  38.454  -75.364 1.00 88.69  ? 519 ARG B CB  1 
ATOM   8405  C CG  . ARG B 1 519 ? 36.516  37.882  -76.728 1.00 90.03  ? 519 ARG B CG  1 
ATOM   8406  C CD  . ARG B 1 519 ? 36.250  36.382  -76.653 1.00 89.20  ? 519 ARG B CD  1 
ATOM   8407  N NE  . ARG B 1 519 ? 37.465  35.599  -76.431 1.00 87.61  ? 519 ARG B NE  1 
ATOM   8408  C CZ  . ARG B 1 519 ? 38.360  35.302  -77.369 1.00 88.57  ? 519 ARG B CZ  1 
ATOM   8409  N NH1 . ARG B 1 519 ? 38.150  35.614  -78.640 1.00 90.35  ? 519 ARG B NH1 1 
ATOM   8410  N NH2 . ARG B 1 519 ? 39.466  34.654  -77.031 1.00 87.73  ? 519 ARG B NH2 1 
ATOM   8411  N N   . GLY B 1 520 ? 35.282  41.228  -76.614 1.00 94.19  ? 520 GLY B N   1 
ATOM   8412  C CA  . GLY B 1 520 ? 33.983  41.798  -76.940 1.00 96.62  ? 520 GLY B CA  1 
ATOM   8413  C C   . GLY B 1 520 ? 33.334  42.537  -75.768 1.00 96.53  ? 520 GLY B C   1 
ATOM   8414  O O   . GLY B 1 520 ? 33.990  43.119  -74.912 1.00 94.89  ? 520 GLY B O   1 
ATOM   8415  N N   . ASP B 1 521 ? 32.007  42.513  -75.732 1.00 98.75  ? 521 ASP B N   1 
ATOM   8416  C CA  . ASP B 1 521 ? 31.290  43.413  -74.848 1.00 100.00 ? 521 ASP B CA  1 
ATOM   8417  C C   . ASP B 1 521 ? 30.510  42.632  -73.787 1.00 99.23  ? 521 ASP B C   1 
ATOM   8418  O O   . ASP B 1 521 ? 29.586  43.182  -73.185 1.00 99.24  ? 521 ASP B O   1 
ATOM   8419  C CB  . ASP B 1 521 ? 30.422  44.344  -75.674 1.00 103.04 ? 521 ASP B CB  1 
ATOM   8420  C CG  . ASP B 1 521 ? 29.243  43.686  -76.380 1.00 105.55 ? 521 ASP B CG  1 
ATOM   8421  O OD1 . ASP B 1 521 ? 29.100  42.442  -76.270 1.00 104.29 ? 521 ASP B OD1 1 
ATOM   8422  O OD2 . ASP B 1 521 ? 28.456  44.429  -77.025 1.00 108.77 ? 521 ASP B OD2 1 
ATOM   8423  N N   . TRP B 1 522 ? 30.906  41.370  -73.526 1.00 98.04  ? 522 TRP B N   1 
ATOM   8424  C CA  . TRP B 1 522 ? 30.176  40.516  -72.598 1.00 96.95  ? 522 TRP B CA  1 
ATOM   8425  C C   . TRP B 1 522 ? 30.112  41.160  -71.220 1.00 96.01  ? 522 TRP B C   1 
ATOM   8426  O O   . TRP B 1 522 ? 29.238  40.825  -70.429 1.00 95.41  ? 522 TRP B O   1 
ATOM   8427  C CB  . TRP B 1 522 ? 30.829  39.139  -72.467 1.00 95.98  ? 522 TRP B CB  1 
ATOM   8428  C CG  . TRP B 1 522 ? 32.046  39.123  -71.581 1.00 95.22  ? 522 TRP B CG  1 
ATOM   8429  C CD1 . TRP B 1 522 ? 33.328  39.318  -71.992 1.00 95.99  ? 522 TRP B CD1 1 
ATOM   8430  C CD2 . TRP B 1 522 ? 32.124  38.902  -70.152 1.00 94.51  ? 522 TRP B CD2 1 
ATOM   8431  N NE1 . TRP B 1 522 ? 34.195  39.226  -70.936 1.00 94.46  ? 522 TRP B NE1 1 
ATOM   8432  C CE2 . TRP B 1 522 ? 33.487  38.975  -69.793 1.00 93.28  ? 522 TRP B CE2 1 
ATOM   8433  C CE3 . TRP B 1 522 ? 31.195  38.649  -69.140 1.00 95.16  ? 522 TRP B CE3 1 
ATOM   8434  C CZ2 . TRP B 1 522 ? 33.931  38.807  -68.484 1.00 91.53  ? 522 TRP B CZ2 1 
ATOM   8435  C CZ3 . TRP B 1 522 ? 31.639  38.482  -67.843 1.00 93.69  ? 522 TRP B CZ3 1 
ATOM   8436  C CH2 . TRP B 1 522 ? 32.989  38.563  -67.518 1.00 91.32  ? 522 TRP B CH2 1 
ATOM   8437  N N   . ALA B 1 523 ? 31.082  42.041  -70.938 1.00 96.23  ? 523 ALA B N   1 
ATOM   8438  C CA  . ALA B 1 523 ? 31.269  42.613  -69.616 1.00 94.84  ? 523 ALA B CA  1 
ATOM   8439  C C   . ALA B 1 523 ? 30.570  43.965  -69.500 1.00 95.70  ? 523 ALA B C   1 
ATOM   8440  O O   . ALA B 1 523 ? 30.888  44.739  -68.600 1.00 96.08  ? 523 ALA B O   1 
ATOM   8441  C CB  . ALA B 1 523 ? 32.754  42.728  -69.329 1.00 93.05  ? 523 ALA B CB  1 
ATOM   8442  N N   . LYS B 1 524 ? 29.606  44.237  -70.389 1.00 96.87  ? 524 LYS B N   1 
ATOM   8443  C CA  . LYS B 1 524 ? 28.960  45.543  -70.441 1.00 98.26  ? 524 LYS B CA  1 
ATOM   8444  C C   . LYS B 1 524 ? 28.415  45.927  -69.065 1.00 96.86  ? 524 LYS B C   1 
ATOM   8445  O O   . LYS B 1 524 ? 28.584  47.058  -68.628 1.00 96.32  ? 524 LYS B O   1 
ATOM   8446  C CB  . LYS B 1 524 ? 27.851  45.564  -71.497 1.00 100.62 ? 524 LYS B CB  1 
ATOM   8447  C CG  . LYS B 1 524 ? 27.355  46.970  -71.754 1.00 103.55 ? 524 LYS B CG  1 
ATOM   8448  C CD  . LYS B 1 524 ? 26.412  47.126  -72.940 1.00 106.33 ? 524 LYS B CD  1 
ATOM   8449  C CE  . LYS B 1 524 ? 25.931  48.544  -73.122 1.00 108.73 ? 524 LYS B CE  1 
ATOM   8450  N NZ  . LYS B 1 524 ? 25.027  49.001  -72.059 1.00 108.97 ? 524 LYS B NZ  1 
ATOM   8451  N N   . GLU B 1 525 ? 27.822  44.953  -68.369 1.00 95.95  ? 525 GLU B N   1 
ATOM   8452  C CA  . GLU B 1 525 ? 27.190  45.181  -67.083 1.00 95.98  ? 525 GLU B CA  1 
ATOM   8453  C C   . GLU B 1 525 ? 28.130  44.841  -65.921 1.00 93.60  ? 525 GLU B C   1 
ATOM   8454  O O   . GLU B 1 525 ? 28.341  45.683  -65.049 1.00 93.11  ? 525 GLU B O   1 
ATOM   8455  C CB  . GLU B 1 525 ? 25.887  44.380  -67.026 1.00 97.08  ? 525 GLU B CB  1 
ATOM   8456  C CG  . GLU B 1 525 ? 24.894  44.738  -68.132 1.00 99.53  ? 525 GLU B CG  1 
ATOM   8457  C CD  . GLU B 1 525 ? 25.050  43.971  -69.439 1.00 99.92  ? 525 GLU B CD  1 
ATOM   8458  O OE1 . GLU B 1 525 ? 25.737  42.924  -69.467 1.00 98.64  ? 525 GLU B OE1 1 
ATOM   8459  O OE2 . GLU B 1 525 ? 24.482  44.432  -70.450 1.00 101.85 ? 525 GLU B OE2 1 
ATOM   8460  N N   . VAL B 1 526 ? 28.678  43.617  -65.896 1.00 91.72  ? 526 VAL B N   1 
ATOM   8461  C CA  . VAL B 1 526 ? 29.376  43.105  -64.719 1.00 90.75  ? 526 VAL B CA  1 
ATOM   8462  C C   . VAL B 1 526 ? 30.694  43.845  -64.475 1.00 91.31  ? 526 VAL B C   1 
ATOM   8463  O O   . VAL B 1 526 ? 31.086  44.036  -63.325 1.00 90.89  ? 526 VAL B O   1 
ATOM   8464  C CB  . VAL B 1 526 ? 29.645  41.586  -64.811 1.00 89.35  ? 526 VAL B CB  1 
ATOM   8465  C CG1 . VAL B 1 526 ? 30.584  41.212  -65.950 1.00 88.50  ? 526 VAL B CG1 1 
ATOM   8466  C CG2 . VAL B 1 526 ? 30.182  41.004  -63.506 1.00 87.61  ? 526 VAL B CG2 1 
ATOM   8467  N N   . GLY B 1 527 ? 31.390  44.224  -65.556 1.00 92.81  ? 527 GLY B N   1 
ATOM   8468  C CA  . GLY B 1 527 ? 32.739  44.771  -65.479 1.00 92.89  ? 527 GLY B CA  1 
ATOM   8469  C C   . GLY B 1 527 ? 32.762  46.191  -64.914 1.00 94.33  ? 527 GLY B C   1 
ATOM   8470  O O   . GLY B 1 527 ? 31.735  46.865  -64.893 1.00 94.77  ? 527 GLY B O   1 
ATOM   8471  N N   . ARG B 1 528 ? 33.934  46.677  -64.512 1.00 94.05  ? 528 ARG B N   1 
ATOM   8472  C CA  . ARG B 1 528 ? 34.038  48.034  -63.925 1.00 96.20  ? 528 ARG B CA  1 
ATOM   8473  C C   . ARG B 1 528 ? 34.084  49.081  -65.040 1.00 101.17 ? 528 ARG B C   1 
ATOM   8474  O O   . ARG B 1 528 ? 34.234  48.681  -66.209 1.00 101.01 ? 528 ARG B O   1 
ATOM   8475  C CB  . ARG B 1 528 ? 35.328  48.177  -63.119 1.00 94.29  ? 528 ARG B CB  1 
ATOM   8476  C CG  . ARG B 1 528 ? 35.234  48.731  -61.706 1.00 94.86  ? 528 ARG B CG  1 
ATOM   8477  C CD  . ARG B 1 528 ? 36.571  49.335  -61.307 1.00 92.42  ? 528 ARG B CD  1 
ATOM   8478  N NE  . ARG B 1 528 ? 37.307  48.512  -60.342 1.00 89.79  ? 528 ARG B NE  1 
ATOM   8479  C CZ  . ARG B 1 528 ? 37.843  47.328  -60.602 1.00 88.25  ? 528 ARG B CZ  1 
ATOM   8480  N NH1 . ARG B 1 528 ? 38.331  47.068  -61.801 1.00 88.22  ? 528 ARG B NH1 1 
ATOM   8481  N NH2 . ARG B 1 528 ? 37.886  46.406  -59.659 1.00 86.62  ? 528 ARG B NH2 1 
ATOM   8482  N N   . LYS B 1 529 ? 33.958  50.365  -64.687 1.00 106.68 ? 529 LYS B N   1 
ATOM   8483  C CA  . LYS B 1 529 ? 34.097  51.454  -65.693 1.00 113.44 ? 529 LYS B CA  1 
ATOM   8484  C C   . LYS B 1 529 ? 34.702  52.704  -65.033 1.00 118.52 ? 529 LYS B C   1 
ATOM   8485  O O   . LYS B 1 529 ? 34.876  52.688  -63.797 1.00 119.10 ? 529 LYS B O   1 
ATOM   8486  C CB  . LYS B 1 529 ? 32.764  51.805  -66.356 1.00 116.00 ? 529 LYS B CB  1 
ATOM   8487  C CG  . LYS B 1 529 ? 32.867  51.990  -67.862 1.00 116.68 ? 529 LYS B CG  1 
ATOM   8488  C CD  . LYS B 1 529 ? 34.193  51.479  -68.413 1.00 116.96 ? 529 LYS B CD  1 
ATOM   8489  C CE  . LYS B 1 529 ? 34.587  52.159  -69.682 1.00 117.11 ? 529 LYS B CE  1 
ATOM   8490  N NZ  . LYS B 1 529 ? 33.567  51.989  -70.719 1.00 113.93 ? 529 LYS B NZ  1 
ATOM   8491  N N   . LEU B 1 530 ? 34.988  53.743  -65.822 1.00 123.29 ? 530 LEU B N   1 
ATOM   8492  C CA  . LEU B 1 530 ? 35.632  54.986  -65.312 1.00 128.12 ? 530 LEU B CA  1 
ATOM   8493  C C   . LEU B 1 530 ? 35.013  55.440  -63.983 1.00 130.00 ? 530 LEU B C   1 
ATOM   8494  O O   . LEU B 1 530 ? 33.796  55.401  -63.852 1.00 131.74 ? 530 LEU B O   1 
ATOM   8495  C CB  . LEU B 1 530 ? 35.479  56.064  -66.380 1.00 128.13 ? 530 LEU B CB  1 
ATOM   8496  C CG  . LEU B 1 530 ? 34.576  55.704  -67.563 1.00 129.88 ? 530 LEU B CG  1 
ATOM   8497  C CD1 . LEU B 1 530 ? 33.255  56.450  -67.482 1.00 129.68 ? 530 LEU B CD1 1 
ATOM   8498  C CD2 . LEU B 1 530 ? 35.270  55.979  -68.885 1.00 132.06 ? 530 LEU B CD2 1 
ATOM   8499  N N   . SER C 1 3   ? 83.064  26.512  -0.031  1.00 155.84 ? 3   SER C N   1 
ATOM   8500  C CA  . SER C 1 3   ? 82.428  25.668  -1.076  1.00 151.65 ? 3   SER C CA  1 
ATOM   8501  C C   . SER C 1 3   ? 82.319  26.440  -2.394  1.00 147.97 ? 3   SER C C   1 
ATOM   8502  O O   . SER C 1 3   ? 81.515  27.364  -2.496  1.00 147.99 ? 3   SER C O   1 
ATOM   8503  C CB  . SER C 1 3   ? 81.088  25.197  -0.597  1.00 152.48 ? 3   SER C CB  1 
ATOM   8504  O OG  . SER C 1 3   ? 80.500  24.324  -1.549  1.00 148.72 ? 3   SER C OG  1 
ATOM   8505  N N   . LYS C 1 4   ? 83.116  26.037  -3.403  1.00 145.16 ? 4   LYS C N   1 
ATOM   8506  C CA  . LYS C 1 4   ? 83.162  26.717  -4.693  1.00 141.37 ? 4   LYS C CA  1 
ATOM   8507  C C   . LYS C 1 4   ? 82.601  25.823  -5.803  1.00 137.75 ? 4   LYS C C   1 
ATOM   8508  O O   . LYS C 1 4   ? 82.365  24.627  -5.613  1.00 137.82 ? 4   LYS C O   1 
ATOM   8509  C CB  . LYS C 1 4   ? 84.582  27.190  -5.033  1.00 140.77 ? 4   LYS C CB  1 
ATOM   8510  C CG  . LYS C 1 4   ? 85.659  26.113  -5.060  1.00 140.53 ? 4   LYS C CG  1 
ATOM   8511  C CD  . LYS C 1 4   ? 87.055  26.613  -5.422  1.00 140.33 ? 4   LYS C CD  1 
ATOM   8512  C CE  . LYS C 1 4   ? 87.163  27.203  -6.798  1.00 136.45 ? 4   LYS C CE  1 
ATOM   8513  N NZ  . LYS C 1 4   ? 86.789  26.270  -7.862  1.00 132.53 ? 4   LYS C NZ  1 
ATOM   8514  N N   . THR C 1 5   ? 82.386  26.434  -6.974  1.00 134.61 ? 5   THR C N   1 
ATOM   8515  C CA  . THR C 1 5   ? 81.801  25.756  -8.120  1.00 130.48 ? 5   THR C CA  1 
ATOM   8516  C C   . THR C 1 5   ? 82.748  24.658  -8.600  1.00 129.06 ? 5   THR C C   1 
ATOM   8517  O O   . THR C 1 5   ? 83.922  24.918  -8.848  1.00 128.20 ? 5   THR C O   1 
ATOM   8518  C CB  . THR C 1 5   ? 81.541  26.773  -9.232  1.00 127.39 ? 5   THR C CB  1 
ATOM   8519  O OG1 . THR C 1 5   ? 80.910  27.894  -8.621  1.00 128.97 ? 5   THR C OG1 1 
ATOM   8520  C CG2 . THR C 1 5   ? 80.691  26.196  -10.350 1.00 123.68 ? 5   THR C CG2 1 
ATOM   8521  N N   . LYS C 1 6   ? 82.209  23.441  -8.729  1.00 128.46 ? 6   LYS C N   1 
ATOM   8522  C CA  . LYS C 1 6   ? 82.886  22.346  -9.401  1.00 127.21 ? 6   LYS C CA  1 
ATOM   8523  C C   . LYS C 1 6   ? 82.412  22.275  -10.855 1.00 123.82 ? 6   LYS C C   1 
ATOM   8524  O O   . LYS C 1 6   ? 81.208  22.152  -11.090 1.00 123.90 ? 6   LYS C O   1 
ATOM   8525  C CB  . LYS C 1 6   ? 82.540  21.069  -8.630  1.00 128.89 ? 6   LYS C CB  1 
ATOM   8526  C CG  . LYS C 1 6   ? 83.239  19.821  -9.121  1.00 127.99 ? 6   LYS C CG  1 
ATOM   8527  C CD  . LYS C 1 6   ? 84.730  19.784  -8.792  1.00 129.81 ? 6   LYS C CD  1 
ATOM   8528  C CE  . LYS C 1 6   ? 85.343  18.465  -9.132  1.00 129.45 ? 6   LYS C CE  1 
ATOM   8529  N NZ  . LYS C 1 6   ? 84.516  17.362  -8.625  1.00 130.90 ? 6   LYS C NZ  1 
ATOM   8530  N N   . ILE C 1 7   ? 83.352  22.352  -11.818 1.00 121.58 ? 7   ILE C N   1 
ATOM   8531  C CA  . ILE C 1 7   ? 83.040  22.252  -13.244 1.00 117.70 ? 7   ILE C CA  1 
ATOM   8532  C C   . ILE C 1 7   ? 83.517  20.889  -13.751 1.00 116.53 ? 7   ILE C C   1 
ATOM   8533  O O   . ILE C 1 7   ? 84.443  20.318  -13.176 1.00 118.70 ? 7   ILE C O   1 
ATOM   8534  C CB  . ILE C 1 7   ? 83.646  23.429  -14.043 1.00 115.98 ? 7   ILE C CB  1 
ATOM   8535  C CG1 . ILE C 1 7   ? 83.145  24.776  -13.517 1.00 117.39 ? 7   ILE C CG1 1 
ATOM   8536  C CG2 . ILE C 1 7   ? 83.389  23.300  -15.549 1.00 111.92 ? 7   ILE C CG2 1 
ATOM   8537  C CD1 . ILE C 1 7   ? 83.866  25.976  -14.103 1.00 116.86 ? 7   ILE C CD1 1 
ATOM   8538  N N   . GLU C 1 8   ? 82.865  20.368  -14.808 1.00 113.55 ? 8   GLU C N   1 
ATOM   8539  C CA  . GLU C 1 8   ? 83.168  19.045  -15.343 1.00 112.63 ? 8   GLU C CA  1 
ATOM   8540  C C   . GLU C 1 8   ? 82.619  18.891  -16.768 1.00 109.74 ? 8   GLU C C   1 
ATOM   8541  O O   . GLU C 1 8   ? 81.426  19.087  -17.002 1.00 109.94 ? 8   GLU C O   1 
ATOM   8542  C CB  . GLU C 1 8   ? 82.599  17.981  -14.401 1.00 114.52 ? 8   GLU C CB  1 
ATOM   8543  C CG  . GLU C 1 8   ? 83.096  16.574  -14.712 1.00 114.36 ? 8   GLU C CG  1 
ATOM   8544  C CD  . GLU C 1 8   ? 82.489  15.490  -13.845 1.00 116.76 ? 8   GLU C CD  1 
ATOM   8545  O OE1 . GLU C 1 8   ? 81.434  15.736  -13.221 1.00 117.65 ? 8   GLU C OE1 1 
ATOM   8546  O OE2 . GLU C 1 8   ? 83.101  14.398  -13.785 1.00 117.94 ? 8   GLU C OE2 1 
ATOM   8547  N N   . LEU C 1 9   ? 83.498  18.502  -17.710 1.00 107.94 ? 9   LEU C N   1 
ATOM   8548  C CA  . LEU C 1 9   ? 83.192  18.438  -19.136 1.00 104.63 ? 9   LEU C CA  1 
ATOM   8549  C C   . LEU C 1 9   ? 83.144  16.985  -19.608 1.00 104.43 ? 9   LEU C C   1 
ATOM   8550  O O   . LEU C 1 9   ? 84.181  16.401  -19.930 1.00 104.35 ? 9   LEU C O   1 
ATOM   8551  C CB  . LEU C 1 9   ? 84.248  19.202  -19.933 1.00 103.16 ? 9   LEU C CB  1 
ATOM   8552  C CG  . LEU C 1 9   ? 84.229  20.730  -19.848 1.00 103.44 ? 9   LEU C CG  1 
ATOM   8553  C CD1 . LEU C 1 9   ? 84.167  21.261  -18.426 1.00 106.57 ? 9   LEU C CD1 1 
ATOM   8554  C CD2 . LEU C 1 9   ? 85.460  21.277  -20.562 1.00 102.71 ? 9   LEU C CD2 1 
ATOM   8555  N N   . LYS C 1 10  ? 81.935  16.414  -19.669 1.00 104.39 ? 10  LYS C N   1 
ATOM   8556  C CA  . LYS C 1 10  ? 81.760  15.053  -20.155 1.00 104.27 ? 10  LYS C CA  1 
ATOM   8557  C C   . LYS C 1 10  ? 80.606  15.045  -21.156 1.00 101.06 ? 10  LYS C C   1 
ATOM   8558  O O   . LYS C 1 10  ? 79.710  15.870  -21.055 1.00 100.36 ? 10  LYS C O   1 
ATOM   8559  C CB  . LYS C 1 10  ? 81.565  14.102  -18.967 1.00 108.02 ? 10  LYS C CB  1 
ATOM   8560  C CG  . LYS C 1 10  ? 81.851  12.628  -19.275 1.00 110.05 ? 10  LYS C CG  1 
ATOM   8561  C CD  . LYS C 1 10  ? 81.163  11.588  -18.383 1.00 113.32 ? 10  LYS C CD  1 
ATOM   8562  C CE  . LYS C 1 10  ? 82.000  11.030  -17.258 1.00 116.37 ? 10  LYS C CE  1 
ATOM   8563  N NZ  . LYS C 1 10  ? 81.153  10.266  -16.334 1.00 118.27 ? 10  LYS C NZ  1 
ATOM   8564  N N   . ASP C 1 11  ? 80.678  14.156  -22.156 1.00 99.27  ? 11  ASP C N   1 
ATOM   8565  C CA  . ASP C 1 11  ? 79.644  14.002  -23.171 1.00 96.63  ? 11  ASP C CA  1 
ATOM   8566  C C   . ASP C 1 11  ? 79.404  15.313  -23.922 1.00 94.05  ? 11  ASP C C   1 
ATOM   8567  O O   . ASP C 1 11  ? 78.317  15.536  -24.448 1.00 93.01  ? 11  ASP C O   1 
ATOM   8568  C CB  . ASP C 1 11  ? 78.376  13.437  -22.553 1.00 97.99  ? 11  ASP C CB  1 
ATOM   8569  C CG  . ASP C 1 11  ? 78.542  12.083  -21.877 1.00 100.16 ? 11  ASP C CG  1 
ATOM   8570  O OD1 . ASP C 1 11  ? 79.587  11.856  -21.238 1.00 100.51 ? 11  ASP C OD1 1 
ATOM   8571  O OD2 . ASP C 1 11  ? 77.602  11.279  -21.964 1.00 101.57 ? 11  ASP C OD2 1 
ATOM   8572  N N   . ASN C 1 12  ? 80.431  16.169  -23.978 1.00 93.85  ? 12  ASN C N   1 
ATOM   8573  C CA  . ASN C 1 12  ? 80.389  17.425  -24.717 1.00 92.37  ? 12  ASN C CA  1 
ATOM   8574  C C   . ASN C 1 12  ? 79.407  18.402  -24.080 1.00 91.62  ? 12  ASN C C   1 
ATOM   8575  O O   . ASN C 1 12  ? 78.676  19.091  -24.783 1.00 89.05  ? 12  ASN C O   1 
ATOM   8576  C CB  . ASN C 1 12  ? 80.080  17.188  -26.189 1.00 90.56  ? 12  ASN C CB  1 
ATOM   8577  C CG  . ASN C 1 12  ? 81.105  16.270  -26.807 1.00 90.66  ? 12  ASN C CG  1 
ATOM   8578  O OD1 . ASN C 1 12  ? 82.263  16.218  -26.363 1.00 90.77  ? 12  ASN C OD1 1 
ATOM   8579  N ND2 . ASN C 1 12  ? 80.690  15.560  -27.843 1.00 89.98  ? 12  ASN C ND2 1 
ATOM   8580  N N   . TRP C 1 13  ? 79.448  18.458  -22.747 1.00 93.52  ? 13  TRP C N   1 
ATOM   8581  C CA  . TRP C 1 13  ? 78.569  19.288  -21.946 1.00 94.89  ? 13  TRP C CA  1 
ATOM   8582  C C   . TRP C 1 13  ? 79.336  19.807  -20.736 1.00 96.92  ? 13  TRP C C   1 
ATOM   8583  O O   . TRP C 1 13  ? 79.949  19.024  -20.010 1.00 98.59  ? 13  TRP C O   1 
ATOM   8584  C CB  . TRP C 1 13  ? 77.335  18.492  -21.487 1.00 95.87  ? 13  TRP C CB  1 
ATOM   8585  C CG  . TRP C 1 13  ? 76.179  18.552  -22.444 1.00 94.95  ? 13  TRP C CG  1 
ATOM   8586  C CD1 . TRP C 1 13  ? 75.951  17.757  -23.529 1.00 93.86  ? 13  TRP C CD1 1 
ATOM   8587  C CD2 . TRP C 1 13  ? 75.071  19.482  -22.381 1.00 95.76  ? 13  TRP C CD2 1 
ATOM   8588  N NE1 . TRP C 1 13  ? 74.783  18.127  -24.150 1.00 92.94  ? 13  TRP C NE1 1 
ATOM   8589  C CE2 . TRP C 1 13  ? 74.221  19.179  -23.468 1.00 93.73  ? 13  TRP C CE2 1 
ATOM   8590  C CE3 . TRP C 1 13  ? 74.712  20.528  -21.513 1.00 96.79  ? 13  TRP C CE3 1 
ATOM   8591  C CZ2 . TRP C 1 13  ? 73.044  19.892  -23.700 1.00 92.63  ? 13  TRP C CZ2 1 
ATOM   8592  C CZ3 . TRP C 1 13  ? 73.540  21.216  -21.736 1.00 95.37  ? 13  TRP C CZ3 1 
ATOM   8593  C CH2 . TRP C 1 13  ? 72.729  20.912  -22.827 1.00 93.43  ? 13  TRP C CH2 1 
ATOM   8594  N N   . TYR C 1 14  ? 79.272  21.125  -20.512 1.00 96.76  ? 14  TYR C N   1 
ATOM   8595  C CA  . TYR C 1 14  ? 79.672  21.682  -19.235 1.00 98.81  ? 14  TYR C CA  1 
ATOM   8596  C C   . TYR C 1 14  ? 78.732  21.136  -18.166 1.00 101.19 ? 14  TYR C C   1 
ATOM   8597  O O   . TYR C 1 14  ? 77.537  21.013  -18.406 1.00 100.56 ? 14  TYR C O   1 
ATOM   8598  C CB  . TYR C 1 14  ? 79.575  23.205  -19.201 1.00 97.98  ? 14  TYR C CB  1 
ATOM   8599  C CG  . TYR C 1 14  ? 80.613  24.021  -19.957 1.00 95.95  ? 14  TYR C CG  1 
ATOM   8600  C CD1 . TYR C 1 14  ? 80.633  24.064  -21.344 1.00 92.63  ? 14  TYR C CD1 1 
ATOM   8601  C CD2 . TYR C 1 14  ? 81.488  24.857  -19.274 1.00 97.70  ? 14  TYR C CD2 1 
ATOM   8602  C CE1 . TYR C 1 14  ? 81.517  24.884  -22.026 1.00 91.73  ? 14  TYR C CE1 1 
ATOM   8603  C CE2 . TYR C 1 14  ? 82.383  25.678  -19.943 1.00 96.70  ? 14  TYR C CE2 1 
ATOM   8604  C CZ  . TYR C 1 14  ? 82.395  25.697  -21.327 1.00 93.77  ? 14  TYR C CZ  1 
ATOM   8605  O OH  . TYR C 1 14  ? 83.279  26.498  -22.000 1.00 92.91  ? 14  TYR C OH  1 
ATOM   8606  N N   . HIS C 1 15  ? 79.295  20.786  -17.007 1.00 104.53 ? 15  HIS C N   1 
ATOM   8607  C CA  . HIS C 1 15  ? 78.522  20.477  -15.818 1.00 107.75 ? 15  HIS C CA  1 
ATOM   8608  C C   . HIS C 1 15  ? 78.974  21.396  -14.685 1.00 111.31 ? 15  HIS C C   1 
ATOM   8609  O O   . HIS C 1 15  ? 80.157  21.416  -14.345 1.00 112.15 ? 15  HIS C O   1 
ATOM   8610  C CB  . HIS C 1 15  ? 78.764  19.042  -15.340 1.00 109.28 ? 15  HIS C CB  1 
ATOM   8611  C CG  . HIS C 1 15  ? 78.458  17.969  -16.323 1.00 107.36 ? 15  HIS C CG  1 
ATOM   8612  N ND1 . HIS C 1 15  ? 79.135  17.823  -17.513 1.00 104.95 ? 15  HIS C ND1 1 
ATOM   8613  C CD2 . HIS C 1 15  ? 77.552  16.984  -16.282 1.00 107.72 ? 15  HIS C CD2 1 
ATOM   8614  C CE1 . HIS C 1 15  ? 78.646  16.775  -18.160 1.00 103.86 ? 15  HIS C CE1 1 
ATOM   8615  N NE2 . HIS C 1 15  ? 77.690  16.244  -17.428 1.00 105.42 ? 15  HIS C NE2 1 
ATOM   8616  N N   . LEU C 1 16  ? 78.025  22.143  -14.101 1.00 113.10 ? 16  LEU C N   1 
ATOM   8617  C CA  . LEU C 1 16  ? 78.278  22.926  -12.899 1.00 116.54 ? 16  LEU C CA  1 
ATOM   8618  C C   . LEU C 1 16  ? 77.677  22.189  -11.700 1.00 119.35 ? 16  LEU C C   1 
ATOM   8619  O O   . LEU C 1 16  ? 76.460  22.024  -11.623 1.00 118.87 ? 16  LEU C O   1 
ATOM   8620  C CB  . LEU C 1 16  ? 77.692  24.330  -13.074 1.00 116.79 ? 16  LEU C CB  1 
ATOM   8621  C CG  . LEU C 1 16  ? 78.568  25.358  -13.806 1.00 115.92 ? 16  LEU C CG  1 
ATOM   8622  C CD1 . LEU C 1 16  ? 79.060  24.867  -15.161 1.00 113.00 ? 16  LEU C CD1 1 
ATOM   8623  C CD2 . LEU C 1 16  ? 77.841  26.691  -13.977 1.00 115.71 ? 16  LEU C CD2 1 
ATOM   8624  N N   . ASP C 1 17  ? 78.547  21.716  -10.791 1.00 121.73 ? 17  ASP C N   1 
ATOM   8625  C CA  . ASP C 1 17  ? 78.133  20.986  -9.598  1.00 124.59 ? 17  ASP C CA  1 
ATOM   8626  C C   . ASP C 1 17  ? 77.277  19.767  -9.958  1.00 123.39 ? 17  ASP C C   1 
ATOM   8627  O O   . ASP C 1 17  ? 76.291  19.478  -9.285  1.00 125.13 ? 17  ASP C O   1 
ATOM   8628  C CB  . ASP C 1 17  ? 77.401  21.888  -8.611  1.00 126.95 ? 17  ASP C CB  1 
ATOM   8629  C CG  . ASP C 1 17  ? 78.282  22.830  -7.808  1.00 128.96 ? 17  ASP C CG  1 
ATOM   8630  O OD1 . ASP C 1 17  ? 79.341  22.360  -7.338  1.00 130.20 ? 17  ASP C OD1 1 
ATOM   8631  O OD2 . ASP C 1 17  ? 77.878  24.001  -7.633  1.00 128.89 ? 17  ASP C OD2 1 
ATOM   8632  N N   . GLY C 1 18  ? 77.660  19.049  -11.021 1.00 120.59 ? 18  GLY C N   1 
ATOM   8633  C CA  . GLY C 1 18  ? 77.018  17.791  -11.371 1.00 119.54 ? 18  GLY C CA  1 
ATOM   8634  C C   . GLY C 1 18  ? 75.981  17.943  -12.483 1.00 116.38 ? 18  GLY C C   1 
ATOM   8635  O O   . GLY C 1 18  ? 75.765  17.007  -13.249 1.00 114.64 ? 18  GLY C O   1 
ATOM   8636  N N   . GLU C 1 19  ? 75.341  19.116  -12.568 1.00 115.85 ? 19  GLU C N   1 
ATOM   8637  C CA  . GLU C 1 19  ? 74.196  19.292  -13.448 1.00 113.73 ? 19  GLU C CA  1 
ATOM   8638  C C   . GLU C 1 19  ? 74.655  19.918  -14.758 1.00 110.15 ? 19  GLU C C   1 
ATOM   8639  O O   . GLU C 1 19  ? 75.490  20.811  -14.749 1.00 110.44 ? 19  GLU C O   1 
ATOM   8640  C CB  . GLU C 1 19  ? 73.108  20.131  -12.773 1.00 115.49 ? 19  GLU C CB  1 
ATOM   8641  C CG  . GLU C 1 19  ? 72.559  19.511  -11.490 1.00 119.16 ? 19  GLU C CG  1 
ATOM   8642  C CD  . GLU C 1 19  ? 72.017  18.094  -11.623 1.00 119.49 ? 19  GLU C CD  1 
ATOM   8643  O OE1 . GLU C 1 19  ? 71.970  17.540  -12.747 1.00 116.66 ? 19  GLU C OE1 1 
ATOM   8644  O OE2 . GLU C 1 19  ? 71.648  17.528  -10.573 1.00 122.90 ? 19  GLU C OE2 1 
ATOM   8645  N N   . LYS C 1 20  ? 74.093  19.434  -15.871 1.00 107.49 ? 20  LYS C N   1 
ATOM   8646  C CA  . LYS C 1 20  ? 74.431  19.913  -17.202 1.00 104.62 ? 20  LYS C CA  1 
ATOM   8647  C C   . LYS C 1 20  ? 74.011  21.376  -17.346 1.00 104.01 ? 20  LYS C C   1 
ATOM   8648  O O   . LYS C 1 20  ? 72.836  21.677  -17.183 1.00 105.19 ? 20  LYS C O   1 
ATOM   8649  C CB  . LYS C 1 20  ? 73.713  19.070  -18.268 1.00 102.29 ? 20  LYS C CB  1 
ATOM   8650  C CG  . LYS C 1 20  ? 74.160  17.611  -18.434 1.00 102.06 ? 20  LYS C CG  1 
ATOM   8651  C CD  . LYS C 1 20  ? 73.829  17.032  -19.806 1.00 99.04  ? 20  LYS C CD  1 
ATOM   8652  C CE  . LYS C 1 20  ? 73.723  15.543  -19.817 1.00 100.06 ? 20  LYS C CE  1 
ATOM   8653  N NZ  . LYS C 1 20  ? 75.018  14.882  -19.644 1.00 101.40 ? 20  LYS C NZ  1 
ATOM   8654  N N   . TYR C 1 21  ? 74.959  22.268  -17.678 1.00 103.29 ? 21  TYR C N   1 
ATOM   8655  C CA  . TYR C 1 21  ? 74.714  23.708  -17.711 1.00 103.33 ? 21  TYR C CA  1 
ATOM   8656  C C   . TYR C 1 21  ? 74.910  24.245  -19.129 1.00 99.90  ? 21  TYR C C   1 
ATOM   8657  O O   . TYR C 1 21  ? 76.031  24.274  -19.646 1.00 99.04  ? 21  TYR C O   1 
ATOM   8658  C CB  . TYR C 1 21  ? 75.631  24.466  -16.742 1.00 106.00 ? 21  TYR C CB  1 
ATOM   8659  C CG  . TYR C 1 21  ? 75.221  25.891  -16.363 1.00 107.31 ? 21  TYR C CG  1 
ATOM   8660  C CD1 . TYR C 1 21  ? 75.697  26.999  -17.062 1.00 106.51 ? 21  TYR C CD1 1 
ATOM   8661  C CD2 . TYR C 1 21  ? 74.404  26.140  -15.262 1.00 109.47 ? 21  TYR C CD2 1 
ATOM   8662  C CE1 . TYR C 1 21  ? 75.352  28.295  -16.695 1.00 107.58 ? 21  TYR C CE1 1 
ATOM   8663  C CE2 . TYR C 1 21  ? 74.058  27.431  -14.883 1.00 110.72 ? 21  TYR C CE2 1 
ATOM   8664  C CZ  . TYR C 1 21  ? 74.528  28.516  -15.601 1.00 109.39 ? 21  TYR C CZ  1 
ATOM   8665  O OH  . TYR C 1 21  ? 74.164  29.777  -15.207 1.00 109.84 ? 21  TYR C OH  1 
ATOM   8666  N N   . PHE C 1 22  ? 73.793  24.664  -19.740 1.00 97.88  ? 22  PHE C N   1 
ATOM   8667  C CA  . PHE C 1 22  ? 73.805  25.348  -21.019 1.00 94.97  ? 22  PHE C CA  1 
ATOM   8668  C C   . PHE C 1 22  ? 74.133  26.813  -20.749 1.00 96.52  ? 22  PHE C C   1 
ATOM   8669  O O   . PHE C 1 22  ? 73.507  27.442  -19.902 1.00 98.81  ? 22  PHE C O   1 
ATOM   8670  C CB  . PHE C 1 22  ? 72.451  25.176  -21.715 1.00 92.69  ? 22  PHE C CB  1 
ATOM   8671  C CG  . PHE C 1 22  ? 72.488  25.457  -23.209 1.00 89.20  ? 22  PHE C CG  1 
ATOM   8672  C CD1 . PHE C 1 22  ? 72.468  26.763  -23.692 1.00 88.51  ? 22  PHE C CD1 1 
ATOM   8673  C CD2 . PHE C 1 22  ? 72.534  24.410  -24.121 1.00 86.96  ? 22  PHE C CD2 1 
ATOM   8674  C CE1 . PHE C 1 22  ? 72.506  27.015  -25.054 1.00 86.16  ? 22  PHE C CE1 1 
ATOM   8675  C CE2 . PHE C 1 22  ? 72.575  24.665  -25.481 1.00 84.68  ? 22  PHE C CE2 1 
ATOM   8676  C CZ  . PHE C 1 22  ? 72.565  25.965  -25.943 1.00 84.40  ? 22  PHE C CZ  1 
ATOM   8677  N N   . ILE C 1 23  ? 75.127  27.347  -21.458 1.00 95.54  ? 23  ILE C N   1 
ATOM   8678  C CA  . ILE C 1 23  ? 75.585  28.702  -21.212 1.00 97.08  ? 23  ILE C CA  1 
ATOM   8679  C C   . ILE C 1 23  ? 74.796  29.653  -22.109 1.00 96.24  ? 23  ILE C C   1 
ATOM   8680  O O   . ILE C 1 23  ? 75.139  29.835  -23.280 1.00 94.73  ? 23  ILE C O   1 
ATOM   8681  C CB  . ILE C 1 23  ? 77.107  28.811  -21.430 1.00 96.66  ? 23  ILE C CB  1 
ATOM   8682  C CG1 . ILE C 1 23  ? 77.868  27.904  -20.475 1.00 98.00  ? 23  ILE C CG1 1 
ATOM   8683  C CG2 . ILE C 1 23  ? 77.579  30.258  -21.312 1.00 97.90  ? 23  ILE C CG2 1 
ATOM   8684  C CD1 . ILE C 1 23  ? 79.295  27.643  -20.901 1.00 97.50  ? 23  ILE C CD1 1 
ATOM   8685  N N   . LYS C 1 24  ? 73.743  30.249  -21.537 1.00 97.32  ? 24  LYS C N   1 
ATOM   8686  C CA  . LYS C 1 24  ? 72.957  31.255  -22.229 1.00 97.09  ? 24  LYS C CA  1 
ATOM   8687  C C   . LYS C 1 24  ? 73.602  32.612  -21.980 1.00 98.70  ? 24  LYS C C   1 
ATOM   8688  O O   . LYS C 1 24  ? 73.269  33.290  -21.015 1.00 101.54 ? 24  LYS C O   1 
ATOM   8689  C CB  . LYS C 1 24  ? 71.500  31.299  -21.744 1.00 97.95  ? 24  LYS C CB  1 
ATOM   8690  C CG  . LYS C 1 24  ? 70.672  30.024  -21.887 1.00 96.30  ? 24  LYS C CG  1 
ATOM   8691  C CD  . LYS C 1 24  ? 69.242  30.141  -21.356 1.00 96.98  ? 24  LYS C CD  1 
ATOM   8692  C CE  . LYS C 1 24  ? 69.171  30.435  -19.886 1.00 99.60  ? 24  LYS C CE  1 
ATOM   8693  N NZ  . LYS C 1 24  ? 67.833  30.248  -19.334 1.00 100.27 ? 24  LYS C NZ  1 
ATOM   8694  N N   . ALA C 1 25  ? 74.529  33.000  -22.854 1.00 98.04  ? 25  ALA C N   1 
ATOM   8695  C CA  . ALA C 1 25  ? 75.362  34.161  -22.594 1.00 100.26 ? 25  ALA C CA  1 
ATOM   8696  C C   . ALA C 1 25  ? 74.937  35.321  -23.486 1.00 100.23 ? 25  ALA C C   1 
ATOM   8697  O O   . ALA C 1 25  ? 74.015  35.196  -24.292 1.00 98.43  ? 25  ALA C O   1 
ATOM   8698  C CB  . ALA C 1 25  ? 76.830  33.818  -22.784 1.00 99.50  ? 25  ALA C CB  1 
ATOM   8699  N N   . ILE C 1 26  ? 75.615  36.454  -23.270 1.00 102.60 ? 26  ILE C N   1 
ATOM   8700  C CA  . ILE C 1 26  ? 75.605  37.594  -24.169 1.00 102.10 ? 26  ILE C CA  1 
ATOM   8701  C C   . ILE C 1 26  ? 76.958  38.294  -24.047 1.00 103.44 ? 26  ILE C C   1 
ATOM   8702  O O   . ILE C 1 26  ? 77.551  38.351  -22.967 1.00 104.92 ? 26  ILE C O   1 
ATOM   8703  C CB  . ILE C 1 26  ? 74.410  38.527  -23.868 1.00 103.31 ? 26  ILE C CB  1 
ATOM   8704  C CG1 . ILE C 1 26  ? 74.318  39.697  -24.861 1.00 102.97 ? 26  ILE C CG1 1 
ATOM   8705  C CG2 . ILE C 1 26  ? 74.429  39.019  -22.419 1.00 106.56 ? 26  ILE C CG2 1 
ATOM   8706  C CD1 . ILE C 1 26  ? 73.038  40.507  -24.751 1.00 104.23 ? 26  ILE C CD1 1 
ATOM   8707  N N   . GLY C 1 27  ? 77.413  38.878  -25.152 1.00 102.74 ? 27  GLY C N   1 
ATOM   8708  C CA  . GLY C 1 27  ? 78.658  39.659  -25.093 1.00 104.22 ? 27  GLY C CA  1 
ATOM   8709  C C   . GLY C 1 27  ? 78.388  41.064  -24.600 1.00 106.67 ? 27  GLY C C   1 
ATOM   8710  O O   . GLY C 1 27  ? 77.573  41.763  -25.230 1.00 106.62 ? 27  GLY C O   1 
ATOM   8711  N N   . TYR C 1 28  ? 79.050  41.469  -23.517 1.00 109.25 ? 28  TYR C N   1 
ATOM   8712  C CA  . TYR C 1 28  ? 78.892  42.848  -22.991 1.00 112.37 ? 28  TYR C CA  1 
ATOM   8713  C C   . TYR C 1 28  ? 80.245  43.547  -22.967 1.00 113.46 ? 28  TYR C C   1 
ATOM   8714  O O   . TYR C 1 28  ? 81.238  42.928  -22.540 1.00 113.20 ? 28  TYR C O   1 
ATOM   8715  C CB  . TYR C 1 28  ? 78.286  42.726  -21.596 1.00 115.04 ? 28  TYR C CB  1 
ATOM   8716  C CG  . TYR C 1 28  ? 78.290  43.999  -20.764 1.00 119.55 ? 28  TYR C CG  1 
ATOM   8717  C CD1 . TYR C 1 28  ? 77.559  45.112  -21.152 1.00 121.55 ? 28  TYR C CD1 1 
ATOM   8718  C CD2 . TYR C 1 28  ? 79.018  44.079  -19.585 1.00 122.86 ? 28  TYR C CD2 1 
ATOM   8719  C CE1 . TYR C 1 28  ? 77.560  46.267  -20.392 1.00 125.64 ? 28  TYR C CE1 1 
ATOM   8720  C CE2 . TYR C 1 28  ? 79.019  45.223  -18.810 1.00 127.20 ? 28  TYR C CE2 1 
ATOM   8721  C CZ  . TYR C 1 28  ? 78.288  46.321  -19.218 1.00 128.60 ? 28  TYR C CZ  1 
ATOM   8722  O OH  . TYR C 1 28  ? 78.291  47.444  -18.448 1.00 132.36 ? 28  TYR C OH  1 
ATOM   8723  N N   . GLU C 1 29  ? 80.279  44.813  -23.390 1.00 114.16 ? 29  GLU C N   1 
ATOM   8724  C CA  . GLU C 1 29  ? 81.546  45.586  -23.414 1.00 115.17 ? 29  GLU C CA  1 
ATOM   8725  C C   . GLU C 1 29  ? 81.401  46.888  -22.621 1.00 118.49 ? 29  GLU C C   1 
ATOM   8726  O O   . GLU C 1 29  ? 80.921  47.878  -23.208 1.00 118.25 ? 29  GLU C O   1 
ATOM   8727  C CB  . GLU C 1 29  ? 81.956  45.946  -24.842 1.00 113.23 ? 29  GLU C CB  1 
ATOM   8728  C CG  . GLU C 1 29  ? 83.430  46.314  -24.978 1.00 114.64 ? 29  GLU C CG  1 
ATOM   8729  C CD  . GLU C 1 29  ? 83.914  46.301  -26.415 1.00 112.56 ? 29  GLU C CD  1 
ATOM   8730  O OE1 . GLU C 1 29  ? 83.244  46.911  -27.271 1.00 112.25 ? 29  GLU C OE1 1 
ATOM   8731  O OE2 . GLU C 1 29  ? 84.959  45.675  -26.679 1.00 111.78 ? 29  GLU C OE2 1 
ATOM   8732  N N   . ILE C 1 30  ? 81.782  46.888  -21.343 1.00 121.19 ? 30  ILE C N   1 
ATOM   8733  C CA  . ILE C 1 30  ? 81.811  48.122  -20.570 1.00 124.89 ? 30  ILE C CA  1 
ATOM   8734  C C   . ILE C 1 30  ? 82.907  49.030  -21.135 1.00 126.26 ? 30  ILE C C   1 
ATOM   8735  O O   . ILE C 1 30  ? 83.845  48.556  -21.770 1.00 124.47 ? 30  ILE C O   1 
ATOM   8736  C CB  . ILE C 1 30  ? 82.000  47.823  -19.068 1.00 127.34 ? 30  ILE C CB  1 
ATOM   8737  C CG1 . ILE C 1 30  ? 81.781  49.057  -18.206 1.00 132.02 ? 30  ILE C CG1 1 
ATOM   8738  C CG2 . ILE C 1 30  ? 83.359  47.192  -18.775 1.00 127.39 ? 30  ILE C CG2 1 
ATOM   8739  C CD1 . ILE C 1 30  ? 80.392  49.665  -18.314 1.00 132.54 ? 30  ILE C CD1 1 
ATOM   8740  N N   . GLY C 1 31  ? 82.761  50.344  -20.930 1.00 129.80 ? 31  GLY C N   1 
ATOM   8741  C CA  . GLY C 1 31  ? 83.716  51.322  -21.429 1.00 131.80 ? 31  GLY C CA  1 
ATOM   8742  C C   . GLY C 1 31  ? 83.541  51.572  -22.926 1.00 129.76 ? 31  GLY C C   1 
ATOM   8743  O O   . GLY C 1 31  ? 84.496  51.940  -23.611 1.00 130.10 ? 31  GLY C O   1 
ATOM   8744  N N   . ALA C 1 32  ? 82.303  51.394  -23.412 1.00 128.09 ? 32  ALA C N   1 
ATOM   8745  C CA  . ALA C 1 32  ? 81.972  51.589  -24.815 1.00 125.82 ? 32  ALA C CA  1 
ATOM   8746  C C   . ALA C 1 32  ? 80.577  52.199  -24.946 1.00 125.98 ? 32  ALA C C   1 
ATOM   8747  O O   . ALA C 1 32  ? 79.702  51.680  -25.639 1.00 122.51 ? 32  ALA C O   1 
ATOM   8748  C CB  . ALA C 1 32  ? 82.093  50.275  -25.546 1.00 122.02 ? 32  ALA C CB  1 
ATOM   8749  N N   . ARG C 1 33  ? 80.391  53.320  -24.249 1.00 130.10 ? 33  ARG C N   1 
ATOM   8750  C CA  . ARG C 1 33  ? 79.277  54.215  -24.487 1.00 131.55 ? 33  ARG C CA  1 
ATOM   8751  C C   . ARG C 1 33  ? 79.627  55.111  -25.668 1.00 132.77 ? 33  ARG C C   1 
ATOM   8752  O O   . ARG C 1 33  ? 80.714  54.996  -26.228 1.00 132.52 ? 33  ARG C O   1 
ATOM   8753  C CB  . ARG C 1 33  ? 79.028  55.062  -23.234 1.00 135.70 ? 33  ARG C CB  1 
ATOM   8754  C CG  . ARG C 1 33  ? 78.478  54.313  -22.030 1.00 135.69 ? 33  ARG C CG  1 
ATOM   8755  C CD  . ARG C 1 33  ? 77.269  53.478  -22.403 1.00 132.40 ? 33  ARG C CD  1 
ATOM   8756  N NE  . ARG C 1 33  ? 76.589  52.956  -21.215 1.00 133.18 ? 33  ARG C NE  1 
ATOM   8757  C CZ  . ARG C 1 33  ? 76.583  51.694  -20.810 1.00 130.66 ? 33  ARG C CZ  1 
ATOM   8758  N NH1 . ARG C 1 33  ? 77.314  50.785  -21.425 1.00 127.28 ? 33  ARG C NH1 1 
ATOM   8759  N NH2 . ARG C 1 33  ? 75.855  51.352  -19.765 1.00 132.12 ? 33  ARG C NH2 1 
ATOM   8760  N N   . PRO C 1 34  ? 78.711  56.014  -26.090 1.00 135.20 ? 34  PRO C N   1 
ATOM   8761  C CA  . PRO C 1 34  ? 79.096  57.184  -26.878 1.00 137.47 ? 34  PRO C CA  1 
ATOM   8762  C C   . PRO C 1 34  ? 80.091  58.042  -26.098 1.00 142.41 ? 34  PRO C C   1 
ATOM   8763  O O   . PRO C 1 34  ? 79.800  58.453  -24.974 1.00 145.80 ? 34  PRO C O   1 
ATOM   8764  C CB  . PRO C 1 34  ? 77.763  57.913  -27.125 1.00 138.15 ? 34  PRO C CB  1 
ATOM   8765  C CG  . PRO C 1 34  ? 76.701  56.857  -26.942 1.00 134.92 ? 34  PRO C CG  1 
ATOM   8766  C CD  . PRO C 1 34  ? 77.256  55.935  -25.875 1.00 134.81 ? 34  PRO C CD  1 
ATOM   8767  N N   . GLY C 1 35  ? 81.266  58.283  -26.702 1.00 143.18 ? 35  GLY C N   1 
ATOM   8768  C CA  . GLY C 1 35  ? 82.298  59.135  -26.132 1.00 146.95 ? 35  GLY C CA  1 
ATOM   8769  C C   . GLY C 1 35  ? 83.380  58.341  -25.398 1.00 147.18 ? 35  GLY C C   1 
ATOM   8770  O O   . GLY C 1 35  ? 84.181  58.933  -24.686 1.00 151.16 ? 35  GLY C O   1 
ATOM   8771  N N   . GLN C 1 36  ? 83.405  57.010  -25.566 1.00 143.78 ? 36  GLN C N   1 
ATOM   8772  C CA  . GLN C 1 36  ? 84.377  56.159  -24.893 1.00 143.40 ? 36  GLN C CA  1 
ATOM   8773  C C   . GLN C 1 36  ? 85.026  55.232  -25.908 1.00 139.80 ? 36  GLN C C   1 
ATOM   8774  O O   . GLN C 1 36  ? 84.348  54.727  -26.801 1.00 136.64 ? 36  GLN C O   1 
ATOM   8775  C CB  . GLN C 1 36  ? 83.796  55.179  -23.874 1.00 142.78 ? 36  GLN C CB  1 
ATOM   8776  C CG  . GLN C 1 36  ? 82.947  55.823  -22.786 1.00 146.70 ? 36  GLN C CG  1 
ATOM   8777  C CD  . GLN C 1 36  ? 82.431  54.818  -21.778 1.00 146.03 ? 36  GLN C CD  1 
ATOM   8778  O OE1 . GLN C 1 36  ? 81.804  53.815  -22.133 1.00 142.35 ? 36  GLN C OE1 1 
ATOM   8779  N NE2 . GLN C 1 36  ? 82.687  55.074  -20.504 1.00 149.87 ? 36  GLN C NE2 1 
ATOM   8780  N N   . ALA C 1 37  ? 86.336  55.015  -25.724 1.00 140.73 ? 37  ALA C N   1 
ATOM   8781  C CA  . ALA C 1 37  ? 87.097  53.987  -26.419 1.00 137.56 ? 37  ALA C CA  1 
ATOM   8782  C C   . ALA C 1 37  ? 87.756  53.061  -25.396 1.00 136.78 ? 37  ALA C C   1 
ATOM   8783  O O   . ALA C 1 37  ? 88.678  53.470  -24.684 1.00 140.15 ? 37  ALA C O   1 
ATOM   8784  C CB  . ALA C 1 37  ? 88.130  54.623  -27.320 1.00 138.92 ? 37  ALA C CB  1 
ATOM   8785  N N   . PRO C 1 38  ? 87.306  51.790  -25.287 1.00 131.71 ? 38  PRO C N   1 
ATOM   8786  C CA  . PRO C 1 38  ? 87.747  50.928  -24.191 1.00 131.17 ? 38  PRO C CA  1 
ATOM   8787  C C   . PRO C 1 38  ? 89.211  50.484  -24.236 1.00 130.42 ? 38  PRO C C   1 
ATOM   8788  O O   . PRO C 1 38  ? 89.781  50.142  -23.201 1.00 131.14 ? 38  PRO C O   1 
ATOM   8789  C CB  . PRO C 1 38  ? 86.757  49.750  -24.260 1.00 127.98 ? 38  PRO C CB  1 
ATOM   8790  C CG  . PRO C 1 38  ? 86.272  49.718  -25.696 1.00 125.29 ? 38  PRO C CG  1 
ATOM   8791  C CD  . PRO C 1 38  ? 86.330  51.150  -26.182 1.00 127.64 ? 38  PRO C CD  1 
ATOM   8792  N N   . TYR C 1 39  ? 89.836  50.516  -25.418 1.00 128.55 ? 39  TYR C N   1 
ATOM   8793  C CA  . TYR C 1 39  ? 91.213  50.064  -25.527 1.00 129.17 ? 39  TYR C CA  1 
ATOM   8794  C C   . TYR C 1 39  ? 92.190  51.250  -25.530 1.00 133.36 ? 39  TYR C C   1 
ATOM   8795  O O   . TYR C 1 39  ? 93.405  51.047  -25.550 1.00 133.36 ? 39  TYR C O   1 
ATOM   8796  C CB  . TYR C 1 39  ? 91.287  49.142  -26.750 1.00 125.23 ? 39  TYR C CB  1 
ATOM   8797  C CG  . TYR C 1 39  ? 90.499  47.841  -26.641 1.00 122.08 ? 39  TYR C CG  1 
ATOM   8798  C CD1 . TYR C 1 39  ? 90.353  47.158  -25.434 1.00 122.71 ? 39  TYR C CD1 1 
ATOM   8799  C CD2 . TYR C 1 39  ? 89.887  47.291  -27.761 1.00 119.15 ? 39  TYR C CD2 1 
ATOM   8800  C CE1 . TYR C 1 39  ? 89.616  45.982  -25.349 1.00 120.22 ? 39  TYR C CE1 1 
ATOM   8801  C CE2 . TYR C 1 39  ? 89.153  46.112  -27.690 1.00 116.44 ? 39  TYR C CE2 1 
ATOM   8802  C CZ  . TYR C 1 39  ? 89.016  45.451  -26.482 1.00 116.64 ? 39  TYR C CZ  1 
ATOM   8803  O OH  . TYR C 1 39  ? 88.285  44.295  -26.445 1.00 113.32 ? 39  TYR C OH  1 
ATOM   8804  N N   . GLU C 1 40  ? 91.668  52.485  -25.471 1.00 136.39 ? 40  GLU C N   1 
ATOM   8805  C CA  . GLU C 1 40  ? 92.491  53.677  -25.606 1.00 140.24 ? 40  GLU C CA  1 
ATOM   8806  C C   . GLU C 1 40  ? 92.427  54.532  -24.346 1.00 145.03 ? 40  GLU C C   1 
ATOM   8807  O O   . GLU C 1 40  ? 93.408  55.206  -24.007 1.00 148.15 ? 40  GLU C O   1 
ATOM   8808  C CB  . GLU C 1 40  ? 92.042  54.475  -26.826 1.00 140.05 ? 40  GLU C CB  1 
ATOM   8809  C CG  . GLU C 1 40  ? 92.323  53.714  -28.115 1.00 136.92 ? 40  GLU C CG  1 
ATOM   8810  C CD  . GLU C 1 40  ? 92.156  54.521  -29.379 1.00 137.35 ? 40  GLU C CD  1 
ATOM   8811  O OE1 . GLU C 1 40  ? 91.003  54.905  -29.698 1.00 136.46 ? 40  GLU C OE1 1 
ATOM   8812  O OE2 . GLU C 1 40  ? 93.208  54.748  -30.026 1.00 138.07 ? 40  GLU C OE2 1 
ATOM   8813  N N   . ASP C 1 41  ? 91.286  54.468  -23.658 1.00 145.00 ? 41  ASP C N   1 
ATOM   8814  C CA  . ASP C 1 41  ? 91.069  55.384  -22.507 1.00 149.47 ? 41  ASP C CA  1 
ATOM   8815  C C   . ASP C 1 41  ? 91.525  54.784  -21.176 1.00 150.22 ? 41  ASP C C   1 
ATOM   8816  O O   . ASP C 1 41  ? 91.551  53.546  -21.051 1.00 148.12 ? 41  ASP C O   1 
ATOM   8817  C CB  . ASP C 1 41  ? 89.615  55.831  -22.462 1.00 149.39 ? 41  ASP C CB  1 
ATOM   8818  C CG  . ASP C 1 41  ? 89.082  56.420  -23.760 1.00 148.88 ? 41  ASP C CG  1 
ATOM   8819  O OD1 . ASP C 1 41  ? 89.906  56.736  -24.643 1.00 150.03 ? 41  ASP C OD1 1 
ATOM   8820  O OD2 . ASP C 1 41  ? 87.847  56.550  -23.882 1.00 147.27 ? 41  ASP C OD2 1 
ATOM   8821  N N   . GLU C 1 42  ? 91.845  55.656  -20.219 1.00 153.63 ? 42  GLU C N   1 
ATOM   8822  C CA  . GLU C 1 42  ? 92.274  55.209  -18.872 1.00 155.07 ? 42  GLU C CA  1 
ATOM   8823  C C   . GLU C 1 42  ? 91.209  54.278  -18.310 1.00 152.78 ? 42  GLU C C   1 
ATOM   8824  O O   . GLU C 1 42  ? 90.142  54.767  -17.895 1.00 154.07 ? 42  GLU C O   1 
ATOM   8825  C CB  . GLU C 1 42  ? 92.439  56.399  -17.930 1.00 160.40 ? 42  GLU C CB  1 
ATOM   8826  C CG  . GLU C 1 42  ? 91.982  57.721  -18.539 1.00 162.17 ? 42  GLU C CG  1 
ATOM   8827  C CD  . GLU C 1 42  ? 91.671  58.782  -17.500 1.00 167.35 ? 42  GLU C CD  1 
ATOM   8828  O OE1 . GLU C 1 42  ? 92.466  58.923  -16.547 1.00 169.52 ? 42  GLU C OE1 1 
ATOM   8829  O OE2 . GLU C 1 42  ? 90.633  59.463  -17.640 1.00 168.69 ? 42  GLU C OE2 1 
ATOM   8830  N N   . ARG C 1 43  ? 91.516  52.990  -18.276 1.00 149.46 ? 43  ARG C N   1 
ATOM   8831  C CA  . ARG C 1 43  ? 90.509  51.997  -17.833 1.00 146.87 ? 43  ARG C CA  1 
ATOM   8832  C C   . ARG C 1 43  ? 89.881  52.397  -16.493 1.00 149.63 ? 43  ARG C C   1 
ATOM   8833  O O   . ARG C 1 43  ? 90.634  52.586  -15.514 1.00 153.41 ? 43  ARG C O   1 
ATOM   8834  C CB  . ARG C 1 43  ? 91.168  50.615  -17.748 1.00 143.86 ? 43  ARG C CB  1 
ATOM   8835  C CG  . ARG C 1 43  ? 92.592  50.575  -17.214 1.00 146.36 ? 43  ARG C CG  1 
ATOM   8836  C CD  . ARG C 1 43  ? 92.773  49.404  -16.260 1.00 143.28 ? 43  ARG C CD  1 
ATOM   8837  N NE  . ARG C 1 43  ? 93.900  48.540  -16.630 1.00 146.02 ? 43  ARG C NE  1 
ATOM   8838  C CZ  . ARG C 1 43  ? 93.784  47.328  -17.159 1.00 144.34 ? 43  ARG C CZ  1 
ATOM   8839  N NH1 . ARG C 1 43  ? 93.095  47.153  -18.272 1.00 140.01 ? 43  ARG C NH1 1 
ATOM   8840  N NH2 . ARG C 1 43  ? 94.360  46.294  -16.572 1.00 147.11 ? 43  ARG C NH2 1 
ATOM   8841  N N   . LYS C 1 44  ? 88.558  52.561  -16.462 1.00 146.97 ? 44  LYS C N   1 
ATOM   8842  C CA  . LYS C 1 44  ? 87.862  52.778  -15.208 1.00 149.20 ? 44  LYS C CA  1 
ATOM   8843  C C   . LYS C 1 44  ? 86.971  51.567  -14.954 1.00 145.79 ? 44  LYS C C   1 
ATOM   8844  O O   . LYS C 1 44  ? 86.630  50.849  -15.889 1.00 141.29 ? 44  LYS C O   1 
ATOM   8845  C CB  . LYS C 1 44  ? 87.110  54.116  -15.252 1.00 151.38 ? 44  LYS C CB  1 
ATOM   8846  C CG  . LYS C 1 44  ? 86.565  54.587  -13.916 1.00 155.29 ? 44  LYS C CG  1 
ATOM   8847  C CD  . LYS C 1 44  ? 87.619  54.694  -12.824 1.00 159.07 ? 44  LYS C CD  1 
ATOM   8848  C CE  . LYS C 1 44  ? 87.014  55.106  -11.532 1.00 163.17 ? 44  LYS C CE  1 
ATOM   8849  N NZ  . LYS C 1 44  ? 88.045  55.151  -10.498 1.00 166.94 ? 44  LYS C NZ  1 
ATOM   8850  N N   . ASP C 1 45  ? 86.625  51.345  -13.683 1.00 148.07 ? 45  ASP C N   1 
ATOM   8851  C CA  . ASP C 1 45  ? 85.777  50.235  -13.281 1.00 145.94 ? 45  ASP C CA  1 
ATOM   8852  C C   . ASP C 1 45  ? 84.336  50.468  -13.743 1.00 144.48 ? 45  ASP C C   1 
ATOM   8853  O O   . ASP C 1 45  ? 83.668  49.535  -14.183 1.00 140.70 ? 45  ASP C O   1 
ATOM   8854  C CB  . ASP C 1 45  ? 85.825  50.027  -11.775 1.00 149.33 ? 45  ASP C CB  1 
ATOM   8855  C CG  . ASP C 1 45  ? 87.212  49.946  -11.161 1.00 151.48 ? 45  ASP C CG  1 
ATOM   8856  O OD1 . ASP C 1 45  ? 88.188  49.882  -11.936 1.00 149.70 ? 45  ASP C OD1 1 
ATOM   8857  O OD2 . ASP C 1 45  ? 87.295  49.960  -9.917  1.00 154.91 ? 45  ASP C OD2 1 
ATOM   8858  N N   . GLU C 1 46  ? 83.859  51.714  -13.610 1.00 147.57 ? 46  GLU C N   1 
ATOM   8859  C CA  . GLU C 1 46  ? 82.512  52.090  -14.010 1.00 146.77 ? 46  GLU C CA  1 
ATOM   8860  C C   . GLU C 1 46  ? 81.510  51.134  -13.382 1.00 145.76 ? 46  GLU C C   1 
ATOM   8861  O O   . GLU C 1 46  ? 80.710  50.507  -14.077 1.00 141.71 ? 46  GLU C O   1 
ATOM   8862  C CB  . GLU C 1 46  ? 82.322  52.065  -15.522 1.00 142.92 ? 46  GLU C CB  1 
ATOM   8863  C CG  . GLU C 1 46  ? 83.271  53.006  -16.250 1.00 144.04 ? 46  GLU C CG  1 
ATOM   8864  C CD  . GLU C 1 46  ? 82.747  53.425  -17.608 1.00 141.75 ? 46  GLU C CD  1 
ATOM   8865  O OE1 . GLU C 1 46  ? 81.615  53.041  -17.993 1.00 139.28 ? 46  GLU C OE1 1 
ATOM   8866  O OE2 . GLU C 1 46  ? 83.503  54.150  -18.282 1.00 142.58 ? 46  GLU C OE2 1 
ATOM   8867  N N   . LEU C 1 47  ? 81.580  51.037  -12.054 1.00 149.40 ? 47  LEU C N   1 
ATOM   8868  C CA  . LEU C 1 47  ? 80.687  50.173  -11.306 1.00 149.35 ? 47  LEU C CA  1 
ATOM   8869  C C   . LEU C 1 47  ? 79.253  50.586  -11.618 1.00 149.39 ? 47  LEU C C   1 
ATOM   8870  O O   . LEU C 1 47  ? 78.402  49.731  -11.851 1.00 146.97 ? 47  LEU C O   1 
ATOM   8871  C CB  . LEU C 1 47  ? 80.952  50.250  -9.803  1.00 153.65 ? 47  LEU C CB  1 
ATOM   8872  C CG  . LEU C 1 47  ? 82.377  49.951  -9.332  1.00 154.88 ? 47  LEU C CG  1 
ATOM   8873  C CD1 . LEU C 1 47  ? 83.011  48.877  -10.204 1.00 150.29 ? 47  LEU C CD1 1 
ATOM   8874  C CD2 . LEU C 1 47  ? 83.254  51.196  -9.256  1.00 158.41 ? 47  LEU C CD2 1 
ATOM   8875  N N   . GLU C 1 48  ? 79.013  51.906  -11.623 1.00 152.67 ? 48  GLU C N   1 
ATOM   8876  C CA  . GLU C 1 48  ? 77.674  52.458  -11.755 1.00 153.20 ? 48  GLU C CA  1 
ATOM   8877  C C   . GLU C 1 48  ? 76.982  51.826  -12.966 1.00 148.40 ? 48  GLU C C   1 
ATOM   8878  O O   . GLU C 1 48  ? 76.032  51.064  -12.801 1.00 146.67 ? 48  GLU C O   1 
ATOM   8879  C CB  . GLU C 1 48  ? 77.723  53.989  -11.789 1.00 156.80 ? 48  GLU C CB  1 
ATOM   8880  C CG  . GLU C 1 48  ? 78.257  54.632  -10.509 1.00 162.33 ? 48  GLU C CG  1 
ATOM   8881  C CD  . GLU C 1 48  ? 77.449  54.434  -9.233  1.00 165.41 ? 48  GLU C CD  1 
ATOM   8882  O OE1 . GLU C 1 48  ? 76.212  54.646  -9.219  1.00 165.61 ? 48  GLU C OE1 1 
ATOM   8883  O OE2 . GLU C 1 48  ? 78.097  54.092  -8.220  1.00 167.91 ? 48  GLU C OE2 1 
ATOM   8884  N N   . LEU C 1 49  ? 77.497  52.089  -14.173 1.00 146.42 ? 49  LEU C N   1 
ATOM   8885  C CA  . LEU C 1 49  ? 76.838  51.659  -15.401 1.00 142.52 ? 49  LEU C CA  1 
ATOM   8886  C C   . LEU C 1 49  ? 76.736  50.130  -15.489 1.00 139.47 ? 49  LEU C C   1 
ATOM   8887  O O   . LEU C 1 49  ? 75.830  49.617  -16.149 1.00 137.10 ? 49  LEU C O   1 
ATOM   8888  C CB  . LEU C 1 49  ? 77.544  52.234  -16.631 1.00 140.95 ? 49  LEU C CB  1 
ATOM   8889  C CG  . LEU C 1 49  ? 77.353  53.731  -16.904 1.00 143.65 ? 49  LEU C CG  1 
ATOM   8890  C CD1 . LEU C 1 49  ? 78.087  54.080  -18.190 1.00 141.67 ? 49  LEU C CD1 1 
ATOM   8891  C CD2 . LEU C 1 49  ? 75.891  54.173  -16.994 1.00 143.92 ? 49  LEU C CD2 1 
ATOM   8892  N N   . MET C 1 50  ? 77.654  49.398  -14.839 1.00 140.11 ? 50  MET C N   1 
ATOM   8893  C CA  . MET C 1 50  ? 77.601  47.943  -14.853 1.00 137.13 ? 50  MET C CA  1 
ATOM   8894  C C   . MET C 1 50  ? 76.349  47.459  -14.127 1.00 137.59 ? 50  MET C C   1 
ATOM   8895  O O   . MET C 1 50  ? 75.679  46.570  -14.641 1.00 134.76 ? 50  MET C O   1 
ATOM   8896  C CB  . MET C 1 50  ? 78.848  47.287  -14.245 1.00 138.19 ? 50  MET C CB  1 
ATOM   8897  C CG  . MET C 1 50  ? 80.002  47.146  -15.226 1.00 136.38 ? 50  MET C CG  1 
ATOM   8898  S SD  . MET C 1 50  ? 81.491  46.380  -14.549 1.00 137.58 ? 50  MET C SD  1 
ATOM   8899  C CE  . MET C 1 50  ? 81.064  44.635  -14.647 1.00 133.79 ? 50  MET C CE  1 
ATOM   8900  N N   . LYS C 1 51  ? 76.010  48.042  -12.966 1.00 141.29 ? 51  LYS C N   1 
ATOM   8901  C CA  . LYS C 1 51  ? 74.845  47.563  -12.231 1.00 141.88 ? 51  LYS C CA  1 
ATOM   8902  C C   . LYS C 1 51  ? 73.585  47.746  -13.082 1.00 140.01 ? 51  LYS C C   1 
ATOM   8903  O O   . LYS C 1 51  ? 72.736  46.857  -13.079 1.00 137.90 ? 51  LYS C O   1 
ATOM   8904  C CB  . LYS C 1 51  ? 74.685  48.036  -10.778 1.00 146.60 ? 51  LYS C CB  1 
ATOM   8905  C CG  . LYS C 1 51  ? 75.372  49.316  -10.338 1.00 150.61 ? 51  LYS C CG  1 
ATOM   8906  C CD  . LYS C 1 51  ? 75.231  49.559  -8.839  1.00 155.51 ? 51  LYS C CD  1 
ATOM   8907  C CE  . LYS C 1 51  ? 75.999  50.746  -8.350  1.00 159.93 ? 51  LYS C CE  1 
ATOM   8908  N NZ  . LYS C 1 51  ? 77.448  50.556  -8.449  1.00 159.67 ? 51  LYS C NZ  1 
ATOM   8909  N N   . PHE C 1 52  ? 73.491  48.851  -13.845 1.00 140.86 ? 52  PHE C N   1 
ATOM   8910  C CA  . PHE C 1 52  ? 72.345  49.118  -14.715 1.00 139.68 ? 52  PHE C CA  1 
ATOM   8911  C C   . PHE C 1 52  ? 72.305  48.089  -15.847 1.00 135.04 ? 52  PHE C C   1 
ATOM   8912  O O   . PHE C 1 52  ? 71.239  47.590  -16.195 1.00 132.88 ? 52  PHE C O   1 
ATOM   8913  C CB  . PHE C 1 52  ? 72.341  50.554  -15.270 1.00 141.24 ? 52  PHE C CB  1 
ATOM   8914  C CG  . PHE C 1 52  ? 71.375  50.906  -16.408 1.00 138.71 ? 52  PHE C CG  1 
ATOM   8915  C CD1 . PHE C 1 52  ? 70.046  51.244  -16.160 1.00 139.17 ? 52  PHE C CD1 1 
ATOM   8916  C CD2 . PHE C 1 52  ? 71.818  50.951  -17.732 1.00 135.62 ? 52  PHE C CD2 1 
ATOM   8917  C CE1 . PHE C 1 52  ? 69.192  51.576  -17.203 1.00 137.14 ? 52  PHE C CE1 1 
ATOM   8918  C CE2 . PHE C 1 52  ? 70.956  51.289  -18.769 1.00 133.29 ? 52  PHE C CE2 1 
ATOM   8919  C CZ  . PHE C 1 52  ? 69.649  51.603  -18.501 1.00 134.08 ? 52  PHE C CZ  1 
ATOM   8920  N N   . ASP C 1 53  ? 73.468  47.788  -16.429 1.00 133.67 ? 53  ASP C N   1 
ATOM   8921  C CA  . ASP C 1 53  ? 73.543  46.819  -17.508 1.00 129.64 ? 53  ASP C CA  1 
ATOM   8922  C C   . ASP C 1 53  ? 73.339  45.416  -16.941 1.00 128.70 ? 53  ASP C C   1 
ATOM   8923  O O   . ASP C 1 53  ? 72.384  44.741  -17.315 1.00 126.12 ? 53  ASP C O   1 
ATOM   8924  C CB  . ASP C 1 53  ? 74.847  46.978  -18.268 1.00 128.56 ? 53  ASP C CB  1 
ATOM   8925  C CG  . ASP C 1 53  ? 75.074  48.365  -18.848 1.00 130.14 ? 53  ASP C CG  1 
ATOM   8926  O OD1 . ASP C 1 53  ? 74.076  49.093  -19.043 1.00 131.25 ? 53  ASP C OD1 1 
ATOM   8927  O OD2 . ASP C 1 53  ? 76.252  48.724  -19.054 1.00 131.01 ? 53  ASP C OD2 1 
ATOM   8928  N N   . LEU C 1 54  ? 74.231  45.011  -16.021 1.00 131.15 ? 54  LEU C N   1 
ATOM   8929  C CA  . LEU C 1 54  ? 74.236  43.682  -15.418 1.00 130.54 ? 54  LEU C CA  1 
ATOM   8930  C C   . LEU C 1 54  ? 72.846  43.297  -14.917 1.00 130.79 ? 54  LEU C C   1 
ATOM   8931  O O   . LEU C 1 54  ? 72.564  42.104  -14.831 1.00 130.59 ? 54  LEU C O   1 
ATOM   8932  C CB  . LEU C 1 54  ? 75.238  43.561  -14.267 1.00 133.62 ? 54  LEU C CB  1 
ATOM   8933  C CG  . LEU C 1 54  ? 76.640  43.044  -14.607 1.00 132.30 ? 54  LEU C CG  1 
ATOM   8934  C CD1 . LEU C 1 54  ? 77.383  43.904  -15.617 1.00 131.55 ? 54  LEU C CD1 1 
ATOM   8935  C CD2 . LEU C 1 54  ? 77.424  42.934  -13.305 1.00 135.76 ? 54  LEU C CD2 1 
ATOM   8936  N N   . GLU C 1 55  ? 72.021  44.287  -14.534 1.00 132.34 ? 55  GLU C N   1 
ATOM   8937  C CA  . GLU C 1 55  ? 70.652  44.035  -14.102 1.00 132.05 ? 55  GLU C CA  1 
ATOM   8938  C C   . GLU C 1 55  ? 69.749  43.818  -15.318 1.00 127.65 ? 55  GLU C C   1 
ATOM   8939  O O   . GLU C 1 55  ? 68.887  42.946  -15.294 1.00 125.88 ? 55  GLU C O   1 
ATOM   8940  C CB  . GLU C 1 55  ? 70.166  45.173  -13.202 1.00 136.34 ? 55  GLU C CB  1 
ATOM   8941  C CG  . GLU C 1 55  ? 68.854  44.874  -12.483 1.00 137.89 ? 55  GLU C CG  1 
ATOM   8942  C CD  . GLU C 1 55  ? 68.855  43.599  -11.658 1.00 137.94 ? 55  GLU C CD  1 
ATOM   8943  O OE1 . GLU C 1 55  ? 69.812  43.404  -10.881 1.00 139.52 ? 55  GLU C OE1 1 
ATOM   8944  O OE2 . GLU C 1 55  ? 67.893  42.809  -11.778 1.00 136.58 ? 55  GLU C OE2 1 
ATOM   8945  N N   . ASN C 1 56  ? 69.956  44.612  -16.375 1.00 126.09 ? 56  ASN C N   1 
ATOM   8946  C CA  . ASN C 1 56  ? 69.237  44.450  -17.627 1.00 123.07 ? 56  ASN C CA  1 
ATOM   8947  C C   . ASN C 1 56  ? 69.544  43.078  -18.222 1.00 119.42 ? 56  ASN C C   1 
ATOM   8948  O O   . ASN C 1 56  ? 68.639  42.374  -18.666 1.00 117.81 ? 56  ASN C O   1 
ATOM   8949  C CB  . ASN C 1 56  ? 69.549  45.575  -18.611 1.00 123.48 ? 56  ASN C CB  1 
ATOM   8950  C CG  . ASN C 1 56  ? 68.963  46.916  -18.202 1.00 128.14 ? 56  ASN C CG  1 
ATOM   8951  O OD1 . ASN C 1 56  ? 68.134  47.007  -17.287 1.00 130.80 ? 56  ASN C OD1 1 
ATOM   8952  N ND2 . ASN C 1 56  ? 69.371  47.985  -18.872 1.00 129.28 ? 56  ASN C ND2 1 
ATOM   8953  N N   . ILE C 1 57  ? 70.824  42.685  -18.206 1.00 118.80 ? 57  ILE C N   1 
ATOM   8954  C CA  . ILE C 1 57  ? 71.236  41.405  -18.766 1.00 115.03 ? 57  ILE C CA  1 
ATOM   8955  C C   . ILE C 1 57  ? 70.545  40.277  -18.005 1.00 114.63 ? 57  ILE C C   1 
ATOM   8956  O O   . ILE C 1 57  ? 70.252  39.242  -18.591 1.00 112.07 ? 57  ILE C O   1 
ATOM   8957  C CB  . ILE C 1 57  ? 72.769  41.239  -18.773 1.00 114.95 ? 57  ILE C CB  1 
ATOM   8958  C CG1 . ILE C 1 57  ? 73.417  42.046  -19.895 1.00 114.16 ? 57  ILE C CG1 1 
ATOM   8959  C CG2 . ILE C 1 57  ? 73.170  39.767  -18.881 1.00 112.47 ? 57  ILE C CG2 1 
ATOM   8960  C CD1 . ILE C 1 57  ? 73.449  43.543  -19.667 1.00 117.18 ? 57  ILE C CD1 1 
ATOM   8961  N N   . LYS C 1 58  ? 70.295  40.475  -16.706 1.00 117.58 ? 58  LYS C N   1 
ATOM   8962  C CA  . LYS C 1 58  ? 69.549  39.504  -15.921 1.00 118.25 ? 58  LYS C CA  1 
ATOM   8963  C C   . LYS C 1 58  ? 68.090  39.466  -16.390 1.00 117.10 ? 58  LYS C C   1 
ATOM   8964  O O   . LYS C 1 58  ? 67.539  38.390  -16.620 1.00 115.26 ? 58  LYS C O   1 
ATOM   8965  C CB  . LYS C 1 58  ? 69.710  39.761  -14.417 1.00 122.30 ? 58  LYS C CB  1 
ATOM   8966  C CG  . LYS C 1 58  ? 71.058  39.333  -13.836 1.00 123.11 ? 58  LYS C CG  1 
ATOM   8967  C CD  . LYS C 1 58  ? 71.134  39.265  -12.313 1.00 127.05 ? 58  LYS C CD  1 
ATOM   8968  C CE  . LYS C 1 58  ? 70.840  40.561  -11.622 1.00 130.71 ? 58  LYS C CE  1 
ATOM   8969  N NZ  . LYS C 1 58  ? 70.988  40.439  -10.169 1.00 134.58 ? 58  LYS C NZ  1 
ATOM   8970  N N   . GLU C 1 59  ? 67.472  40.635  -16.568 1.00 118.21 ? 59  GLU C N   1 
ATOM   8971  C CA  . GLU C 1 59  ? 66.104  40.695  -17.060 1.00 117.64 ? 59  GLU C CA  1 
ATOM   8972  C C   . GLU C 1 59  ? 66.050  40.156  -18.495 1.00 113.52 ? 59  GLU C C   1 
ATOM   8973  O O   . GLU C 1 59  ? 65.023  39.620  -18.912 1.00 112.73 ? 59  GLU C O   1 
ATOM   8974  C CB  . GLU C 1 59  ? 65.524  42.106  -16.907 1.00 120.24 ? 59  GLU C CB  1 
ATOM   8975  C CG  . GLU C 1 59  ? 65.208  42.491  -15.461 1.00 124.62 ? 59  GLU C CG  1 
ATOM   8976  C CD  . GLU C 1 59  ? 64.958  43.972  -15.163 1.00 128.03 ? 59  GLU C CD  1 
ATOM   8977  O OE1 . GLU C 1 59  ? 65.107  44.828  -16.061 1.00 127.50 ? 59  GLU C OE1 1 
ATOM   8978  O OE2 . GLU C 1 59  ? 64.619  44.290  -14.002 1.00 131.37 ? 59  GLU C OE2 1 
ATOM   8979  N N   . GLY C 1 60  ? 67.159  40.269  -19.240 1.00 111.18 ? 60  GLY C N   1 
ATOM   8980  C CA  . GLY C 1 60  ? 67.196  39.849  -20.635 1.00 107.81 ? 60  GLY C CA  1 
ATOM   8981  C C   . GLY C 1 60  ? 67.111  38.330  -20.817 1.00 105.83 ? 60  GLY C C   1 
ATOM   8982  O O   . GLY C 1 60  ? 67.010  37.856  -21.953 1.00 103.10 ? 60  GLY C O   1 
ATOM   8983  N N   . GLY C 1 61  ? 67.204  37.579  -19.704 1.00 107.21 ? 61  GLY C N   1 
ATOM   8984  C CA  . GLY C 1 61  ? 67.060  36.130  -19.703 1.00 105.76 ? 61  GLY C CA  1 
ATOM   8985  C C   . GLY C 1 61  ? 68.398  35.393  -19.587 1.00 105.38 ? 61  GLY C C   1 
ATOM   8986  O O   . GLY C 1 61  ? 68.427  34.157  -19.520 1.00 103.46 ? 61  GLY C O   1 
ATOM   8987  N N   . TYR C 1 62  ? 69.500  36.157  -19.538 1.00 106.75 ? 62  TYR C N   1 
ATOM   8988  C CA  . TYR C 1 62  ? 70.838  35.606  -19.721 1.00 106.30 ? 62  TYR C CA  1 
ATOM   8989  C C   . TYR C 1 62  ? 71.457  35.232  -18.374 1.00 108.22 ? 62  TYR C C   1 
ATOM   8990  O O   . TYR C 1 62  ? 71.312  35.967  -17.401 1.00 110.80 ? 62  TYR C O   1 
ATOM   8991  C CB  . TYR C 1 62  ? 71.731  36.615  -20.451 1.00 106.54 ? 62  TYR C CB  1 
ATOM   8992  C CG  . TYR C 1 62  ? 71.222  37.130  -21.793 1.00 105.14 ? 62  TYR C CG  1 
ATOM   8993  C CD1 . TYR C 1 62  ? 70.373  38.231  -21.874 1.00 106.59 ? 62  TYR C CD1 1 
ATOM   8994  C CD2 . TYR C 1 62  ? 71.623  36.536  -22.983 1.00 102.63 ? 62  TYR C CD2 1 
ATOM   8995  C CE1 . TYR C 1 62  ? 69.924  38.710  -23.095 1.00 105.41 ? 62  TYR C CE1 1 
ATOM   8996  C CE2 . TYR C 1 62  ? 71.181  37.004  -24.210 1.00 101.29 ? 62  TYR C CE2 1 
ATOM   8997  C CZ  . TYR C 1 62  ? 70.330  38.094  -24.268 1.00 102.65 ? 62  TYR C CZ  1 
ATOM   8998  O OH  . TYR C 1 62  ? 69.905  38.542  -25.486 1.00 101.64 ? 62  TYR C OH  1 
ATOM   8999  N N   . ASN C 1 63  ? 72.165  34.092  -18.344 1.00 106.94 ? 63  ASN C N   1 
ATOM   9000  C CA  . ASN C 1 63  ? 72.799  33.584  -17.134 1.00 109.45 ? 63  ASN C CA  1 
ATOM   9001  C C   . ASN C 1 63  ? 74.310  33.863  -17.112 1.00 110.91 ? 63  ASN C C   1 
ATOM   9002  O O   . ASN C 1 63  ? 74.957  33.715  -16.073 1.00 113.41 ? 63  ASN C O   1 
ATOM   9003  C CB  . ASN C 1 63  ? 72.567  32.086  -16.990 1.00 107.93 ? 63  ASN C CB  1 
ATOM   9004  C CG  . ASN C 1 63  ? 73.257  31.282  -18.068 1.00 104.75 ? 63  ASN C CG  1 
ATOM   9005  O OD1 . ASN C 1 63  ? 73.846  31.830  -19.006 1.00 102.94 ? 63  ASN C OD1 1 
ATOM   9006  N ND2 . ASN C 1 63  ? 73.191  29.969  -17.962 1.00 104.18 ? 63  ASN C ND2 1 
ATOM   9007  N N   . THR C 1 64  ? 74.877  34.240  -18.266 1.00 109.01 ? 64  THR C N   1 
ATOM   9008  C CA  . THR C 1 64  ? 76.313  34.390  -18.404 1.00 109.56 ? 64  THR C CA  1 
ATOM   9009  C C   . THR C 1 64  ? 76.617  35.618  -19.250 1.00 109.76 ? 64  THR C C   1 
ATOM   9010  O O   . THR C 1 64  ? 75.782  36.045  -20.044 1.00 108.17 ? 64  THR C O   1 
ATOM   9011  C CB  . THR C 1 64  ? 76.872  33.119  -19.034 1.00 107.41 ? 64  THR C CB  1 
ATOM   9012  O OG1 . THR C 1 64  ? 76.538  32.133  -18.064 1.00 108.81 ? 64  THR C OG1 1 
ATOM   9013  C CG2 . THR C 1 64  ? 78.373  33.163  -19.261 1.00 107.61 ? 64  THR C CG2 1 
ATOM   9014  N N   . ILE C 1 65  ? 77.834  36.149  -19.068 1.00 111.50 ? 65  ILE C N   1 
ATOM   9015  C CA  . ILE C 1 65  ? 78.327  37.310  -19.788 1.00 111.91 ? 65  ILE C CA  1 
ATOM   9016  C C   . ILE C 1 65  ? 79.691  36.926  -20.361 1.00 111.41 ? 65  ILE C C   1 
ATOM   9017  O O   . ILE C 1 65  ? 80.395  36.133  -19.746 1.00 112.31 ? 65  ILE C O   1 
ATOM   9018  C CB  . ILE C 1 65  ? 78.360  38.517  -18.827 1.00 115.74 ? 65  ILE C CB  1 
ATOM   9019  C CG1 . ILE C 1 65  ? 78.641  39.844  -19.524 1.00 116.09 ? 65  ILE C CG1 1 
ATOM   9020  C CG2 . ILE C 1 65  ? 79.333  38.277  -17.670 1.00 118.37 ? 65  ILE C CG2 1 
ATOM   9021  C CD1 . ILE C 1 65  ? 78.722  41.017  -18.560 1.00 119.85 ? 65  ILE C CD1 1 
ATOM   9022  N N   . ARG C 1 66  ? 80.032  37.442  -21.553 1.00 110.98 ? 66  ARG C N   1 
ATOM   9023  C CA  . ARG C 1 66  ? 81.286  37.130  -22.232 1.00 110.85 ? 66  ARG C CA  1 
ATOM   9024  C C   . ARG C 1 66  ? 82.051  38.417  -22.539 1.00 113.45 ? 66  ARG C C   1 
ATOM   9025  O O   . ARG C 1 66  ? 81.470  39.343  -23.100 1.00 114.73 ? 66  ARG C O   1 
ATOM   9026  C CB  . ARG C 1 66  ? 80.959  36.357  -23.515 1.00 108.07 ? 66  ARG C CB  1 
ATOM   9027  C CG  . ARG C 1 66  ? 82.076  36.165  -24.533 1.00 107.72 ? 66  ARG C CG  1 
ATOM   9028  C CD  . ARG C 1 66  ? 82.069  37.223  -25.634 1.00 107.82 ? 66  ARG C CD  1 
ATOM   9029  N NE  . ARG C 1 66  ? 82.763  36.796  -26.857 1.00 106.07 ? 66  ARG C NE  1 
ATOM   9030  C CZ  . ARG C 1 66  ? 84.018  37.080  -27.191 1.00 106.27 ? 66  ARG C CZ  1 
ATOM   9031  N NH1 . ARG C 1 66  ? 84.872  37.520  -26.284 1.00 108.67 ? 66  ARG C NH1 1 
ATOM   9032  N NH2 . ARG C 1 66  ? 84.431  36.848  -28.424 1.00 104.78 ? 66  ARG C NH2 1 
ATOM   9033  N N   . THR C 1 67  ? 83.351  38.467  -22.191 1.00 115.61 ? 67  THR C N   1 
ATOM   9034  C CA  . THR C 1 67  ? 84.160  39.674  -22.361 1.00 117.93 ? 67  THR C CA  1 
ATOM   9035  C C   . THR C 1 67  ? 85.227  39.446  -23.434 1.00 115.24 ? 67  THR C C   1 
ATOM   9036  O O   . THR C 1 67  ? 85.398  38.334  -23.918 1.00 112.74 ? 67  THR C O   1 
ATOM   9037  C CB  . THR C 1 67  ? 84.789  40.114  -21.032 1.00 122.40 ? 67  THR C CB  1 
ATOM   9038  O OG1 . THR C 1 67  ? 85.860  39.235  -20.712 1.00 122.90 ? 67  THR C OG1 1 
ATOM   9039  C CG2 . THR C 1 67  ? 83.801  40.106  -19.877 1.00 124.86 ? 67  THR C CG2 1 
ATOM   9040  N N   . TRP C 1 68  ? 85.913  40.529  -23.818 1.00 116.27 ? 68  TRP C N   1 
ATOM   9041  C CA  . TRP C 1 68  ? 87.067  40.476  -24.707 1.00 115.31 ? 68  TRP C CA  1 
ATOM   9042  C C   . TRP C 1 68  ? 88.323  40.912  -23.957 1.00 116.20 ? 68  TRP C C   1 
ATOM   9043  O O   . TRP C 1 68  ? 89.436  40.765  -24.457 1.00 114.72 ? 68  TRP C O   1 
ATOM   9044  C CB  . TRP C 1 68  ? 86.835  41.363  -25.941 1.00 116.43 ? 68  TRP C CB  1 
ATOM   9045  C CG  . TRP C 1 68  ? 85.732  40.872  -26.841 1.00 115.61 ? 68  TRP C CG  1 
ATOM   9046  C CD1 . TRP C 1 68  ? 85.866  40.193  -28.017 1.00 113.63 ? 68  TRP C CD1 1 
ATOM   9047  C CD2 . TRP C 1 68  ? 84.315  40.996  -26.610 1.00 116.50 ? 68  TRP C CD2 1 
ATOM   9048  N NE1 . TRP C 1 68  ? 84.639  39.890  -28.537 1.00 112.20 ? 68  TRP C NE1 1 
ATOM   9049  C CE2 . TRP C 1 68  ? 83.667  40.363  -27.694 1.00 115.40 ? 68  TRP C CE2 1 
ATOM   9050  C CE3 . TRP C 1 68  ? 83.534  41.572  -25.603 1.00 120.31 ? 68  TRP C CE3 1 
ATOM   9051  C CZ2 . TRP C 1 68  ? 82.274  40.292  -27.791 1.00 116.69 ? 68  TRP C CZ2 1 
ATOM   9052  C CZ3 . TRP C 1 68  ? 82.157  41.506  -25.703 1.00 121.66 ? 68  TRP C CZ3 1 
ATOM   9053  C CH2 . TRP C 1 68  ? 81.534  40.869  -26.781 1.00 118.38 ? 68  TRP C CH2 1 
ATOM   9054  N N   . SER C 1 69  ? 88.119  41.444  -22.748 1.00 118.51 ? 69  SER C N   1 
ATOM   9055  C CA  . SER C 1 69  ? 89.182  42.053  -21.978 1.00 121.65 ? 69  SER C CA  1 
ATOM   9056  C C   . SER C 1 69  ? 88.986  41.773  -20.491 1.00 123.34 ? 69  SER C C   1 
ATOM   9057  O O   . SER C 1 69  ? 87.879  41.485  -20.035 1.00 122.95 ? 69  SER C O   1 
ATOM   9058  C CB  . SER C 1 69  ? 89.248  43.520  -22.249 1.00 124.09 ? 69  SER C CB  1 
ATOM   9059  O OG  . SER C 1 69  ? 90.553  44.000  -21.970 1.00 128.59 ? 69  SER C OG  1 
ATOM   9060  N N   . GLN C 1 70  ? 90.092  41.874  -19.749 1.00 125.53 ? 70  GLN C N   1 
ATOM   9061  C CA  . GLN C 1 70  ? 90.153  41.437  -18.364 1.00 127.66 ? 70  GLN C CA  1 
ATOM   9062  C C   . GLN C 1 70  ? 89.526  42.494  -17.459 1.00 130.86 ? 70  GLN C C   1 
ATOM   9063  O O   . GLN C 1 70  ? 89.848  43.674  -17.564 1.00 132.51 ? 70  GLN C O   1 
ATOM   9064  C CB  . GLN C 1 70  ? 91.586  41.134  -17.919 1.00 129.23 ? 70  GLN C CB  1 
ATOM   9065  C CG  . GLN C 1 70  ? 92.624  42.171  -18.339 1.00 131.25 ? 70  GLN C CG  1 
ATOM   9066  C CD  . GLN C 1 70  ? 93.248  41.903  -19.694 1.00 128.63 ? 70  GLN C CD  1 
ATOM   9067  O OE1 . GLN C 1 70  ? 92.541  41.672  -20.686 1.00 125.65 ? 70  GLN C OE1 1 
ATOM   9068  N NE2 . GLN C 1 70  ? 94.578  41.943  -19.742 1.00 129.05 ? 70  GLN C NE2 1 
ATOM   9069  N N   . TYR C 1 71  ? 88.630  42.049  -16.568 1.00 131.91 ? 71  TYR C N   1 
ATOM   9070  C CA  . TYR C 1 71  ? 88.026  42.909  -15.560 1.00 135.22 ? 71  TYR C CA  1 
ATOM   9071  C C   . TYR C 1 71  ? 89.020  43.152  -14.424 1.00 138.39 ? 71  TYR C C   1 
ATOM   9072  O O   . TYR C 1 71  ? 90.041  42.474  -14.324 1.00 137.97 ? 71  TYR C O   1 
ATOM   9073  C CB  . TYR C 1 71  ? 86.717  42.289  -15.047 1.00 134.69 ? 71  TYR C CB  1 
ATOM   9074  C CG  . TYR C 1 71  ? 85.496  42.409  -15.955 1.00 132.73 ? 71  TYR C CG  1 
ATOM   9075  C CD1 . TYR C 1 71  ? 85.423  43.374  -16.958 1.00 132.18 ? 71  TYR C CD1 1 
ATOM   9076  C CD2 . TYR C 1 71  ? 84.384  41.581  -15.784 1.00 131.66 ? 71  TYR C CD2 1 
ATOM   9077  C CE1 . TYR C 1 71  ? 84.306  43.494  -17.772 1.00 129.80 ? 71  TYR C CE1 1 
ATOM   9078  C CE2 . TYR C 1 71  ? 83.257  41.693  -16.591 1.00 128.49 ? 71  TYR C CE2 1 
ATOM   9079  C CZ  . TYR C 1 71  ? 83.219  42.654  -17.590 1.00 127.54 ? 71  TYR C CZ  1 
ATOM   9080  O OH  . TYR C 1 71  ? 82.146  42.796  -18.419 1.00 124.09 ? 71  TYR C OH  1 
ATOM   9081  N N   . SER C 1 72  ? 88.714  44.155  -13.592 1.00 141.49 ? 72  SER C N   1 
ATOM   9082  C CA  . SER C 1 72  ? 89.422  44.386  -12.344 1.00 145.62 ? 72  SER C CA  1 
ATOM   9083  C C   . SER C 1 72  ? 88.788  43.549  -11.235 1.00 145.97 ? 72  SER C C   1 
ATOM   9084  O O   . SER C 1 72  ? 87.748  42.928  -11.442 1.00 143.34 ? 72  SER C O   1 
ATOM   9085  C CB  . SER C 1 72  ? 89.426  45.853  -11.983 1.00 149.67 ? 72  SER C CB  1 
ATOM   9086  O OG  . SER C 1 72  ? 88.100  46.333  -11.808 1.00 150.27 ? 72  SER C OG  1 
ATOM   9087  N N   . GLU C 1 73  ? 89.435  43.547  -10.064 1.00 149.25 ? 73  GLU C N   1 
ATOM   9088  C CA  . GLU C 1 73  ? 88.939  42.834  -8.899  1.00 150.65 ? 73  GLU C CA  1 
ATOM   9089  C C   . GLU C 1 73  ? 87.637  43.491  -8.439  1.00 152.28 ? 73  GLU C C   1 
ATOM   9090  O O   . GLU C 1 73  ? 86.708  42.794  -8.031  1.00 152.29 ? 73  GLU C O   1 
ATOM   9091  C CB  . GLU C 1 73  ? 90.068  42.762  -7.866  1.00 154.34 ? 73  GLU C CB  1 
ATOM   9092  C CG  . GLU C 1 73  ? 89.814  41.805  -6.705  1.00 155.95 ? 73  GLU C CG  1 
ATOM   9093  C CD  . GLU C 1 73  ? 89.382  42.484  -5.419  1.00 160.83 ? 73  GLU C CD  1 
ATOM   9094  O OE1 . GLU C 1 73  ? 90.238  43.062  -4.717  1.00 164.56 ? 73  GLU C OE1 1 
ATOM   9095  O OE2 . GLU C 1 73  ? 88.174  42.446  -5.129  1.00 161.27 ? 73  GLU C OE2 1 
ATOM   9096  N N   . ASN C 1 74  ? 87.562  44.829  -8.549  1.00 153.97 ? 74  ASN C N   1 
ATOM   9097  C CA  . ASN C 1 74  ? 86.349  45.579  -8.243  1.00 154.93 ? 74  ASN C CA  1 
ATOM   9098  C C   . ASN C 1 74  ? 85.225  45.178  -9.193  1.00 150.33 ? 74  ASN C C   1 
ATOM   9099  O O   . ASN C 1 74  ? 84.107  44.929  -8.760  1.00 150.43 ? 74  ASN C O   1 
ATOM   9100  C CB  . ASN C 1 74  ? 86.554  47.088  -8.330  1.00 157.53 ? 74  ASN C CB  1 
ATOM   9101  C CG  . ASN C 1 74  ? 87.408  47.612  -7.202  1.00 162.23 ? 74  ASN C CG  1 
ATOM   9102  O OD1 . ASN C 1 74  ? 86.988  47.568  -6.040  1.00 165.17 ? 74  ASN C OD1 1 
ATOM   9103  N ND2 . ASN C 1 74  ? 88.594  48.108  -7.520  1.00 163.02 ? 74  ASN C ND2 1 
ATOM   9104  N N   . GLN C 1 75  ? 85.534  45.129  -10.490 1.00 146.57 ? 75  GLN C N   1 
ATOM   9105  C CA  . GLN C 1 75  ? 84.566  44.707  -11.489 1.00 142.42 ? 75  GLN C CA  1 
ATOM   9106  C C   . GLN C 1 75  ? 84.142  43.260  -11.229 1.00 140.82 ? 75  GLN C C   1 
ATOM   9107  O O   . GLN C 1 75  ? 82.959  42.954  -11.323 1.00 140.40 ? 75  GLN C O   1 
ATOM   9108  C CB  . GLN C 1 75  ? 85.121  44.924  -12.900 1.00 138.94 ? 75  GLN C CB  1 
ATOM   9109  C CG  . GLN C 1 75  ? 85.343  46.392  -13.260 1.00 140.45 ? 75  GLN C CG  1 
ATOM   9110  C CD  . GLN C 1 75  ? 86.082  46.587  -14.568 1.00 137.48 ? 75  GLN C CD  1 
ATOM   9111  O OE1 . GLN C 1 75  ? 87.191  46.080  -14.763 1.00 136.54 ? 75  GLN C OE1 1 
ATOM   9112  N NE2 . GLN C 1 75  ? 85.487  47.334  -15.484 1.00 136.05 ? 75  GLN C NE2 1 
ATOM   9113  N N   . LEU C 1 76  ? 85.092  42.380  -10.882 1.00 141.07 ? 76  LEU C N   1 
ATOM   9114  C CA  . LEU C 1 76  ? 84.796  40.970  -10.662 1.00 139.24 ? 76  LEU C CA  1 
ATOM   9115  C C   . LEU C 1 76  ? 83.796  40.798  -9.518  1.00 141.27 ? 76  LEU C C   1 
ATOM   9116  O O   . LEU C 1 76  ? 82.896  39.969  -9.630  1.00 138.69 ? 76  LEU C O   1 
ATOM   9117  C CB  . LEU C 1 76  ? 86.059  40.144  -10.397 1.00 139.73 ? 76  LEU C CB  1 
ATOM   9118  C CG  . LEU C 1 76  ? 86.911  39.737  -11.606 1.00 136.47 ? 76  LEU C CG  1 
ATOM   9119  C CD1 . LEU C 1 76  ? 87.570  38.402  -11.299 1.00 136.01 ? 76  LEU C CD1 1 
ATOM   9120  C CD2 . LEU C 1 76  ? 86.154  39.646  -12.923 1.00 132.48 ? 76  LEU C CD2 1 
ATOM   9121  N N   . LYS C 1 77  ? 83.962  41.561  -8.424  1.00 145.75 ? 77  LYS C N   1 
ATOM   9122  C CA  . LYS C 1 77  ? 83.154  41.370  -7.225  1.00 148.75 ? 77  LYS C CA  1 
ATOM   9123  C C   . LYS C 1 77  ? 81.691  41.690  -7.523  1.00 148.22 ? 77  LYS C C   1 
ATOM   9124  O O   . LYS C 1 77  ? 80.799  41.133  -6.886  1.00 149.12 ? 77  LYS C O   1 
ATOM   9125  C CB  . LYS C 1 77  ? 83.636  42.153  -5.991  1.00 153.80 ? 77  LYS C CB  1 
ATOM   9126  C CG  . LYS C 1 77  ? 83.690  43.678  -6.088  1.00 155.87 ? 77  LYS C CG  1 
ATOM   9127  C CD  . LYS C 1 77  ? 83.453  44.430  -4.779  1.00 160.98 ? 77  LYS C CD  1 
ATOM   9128  C CE  . LYS C 1 77  ? 84.572  44.388  -3.783  1.00 164.60 ? 77  LYS C CE  1 
ATOM   9129  N NZ  . LYS C 1 77  ? 85.612  45.381  -4.063  1.00 166.09 ? 77  LYS C NZ  1 
ATOM   9130  N N   . LEU C 1 78  ? 81.468  42.579  -8.500  1.00 147.29 ? 78  LEU C N   1 
ATOM   9131  C CA  . LEU C 1 78  ? 80.134  43.003  -8.903  1.00 146.75 ? 78  LEU C CA  1 
ATOM   9132  C C   . LEU C 1 78  ? 79.428  41.887  -9.678  1.00 141.95 ? 78  LEU C C   1 
ATOM   9133  O O   . LEU C 1 78  ? 78.277  41.560  -9.394  1.00 141.34 ? 78  LEU C O   1 
ATOM   9134  C CB  . LEU C 1 78  ? 80.277  44.275  -9.738  1.00 147.23 ? 78  LEU C CB  1 
ATOM   9135  C CG  . LEU C 1 78  ? 79.013  45.125  -9.892  1.00 148.37 ? 78  LEU C CG  1 
ATOM   9136  C CD1 . LEU C 1 78  ? 78.708  45.851  -8.589  1.00 153.71 ? 78  LEU C CD1 1 
ATOM   9137  C CD2 . LEU C 1 78  ? 79.145  46.107  -11.048 1.00 147.26 ? 78  LEU C CD2 1 
ATOM   9138  N N   . VAL C 1 79  ? 80.133  41.313  -10.661 1.00 138.26 ? 79  VAL C N   1 
ATOM   9139  C CA  . VAL C 1 79  ? 79.630  40.193  -11.442 1.00 134.09 ? 79  VAL C CA  1 
ATOM   9140  C C   . VAL C 1 79  ? 79.353  39.008  -10.519 1.00 134.32 ? 79  VAL C C   1 
ATOM   9141  O O   . VAL C 1 79  ? 78.393  38.267  -10.729 1.00 132.59 ? 79  VAL C O   1 
ATOM   9142  C CB  . VAL C 1 79  ? 80.615  39.779  -12.553 1.00 131.20 ? 79  VAL C CB  1 
ATOM   9143  C CG1 . VAL C 1 79  ? 80.156  38.515  -13.271 1.00 127.38 ? 79  VAL C CG1 1 
ATOM   9144  C CG2 . VAL C 1 79  ? 80.860  40.899  -13.558 1.00 130.58 ? 79  VAL C CG2 1 
ATOM   9145  N N   . GLN C 1 80  ? 80.231  38.816  -9.527  1.00 136.58 ? 80  GLN C N   1 
ATOM   9146  C CA  . GLN C 1 80  ? 80.092  37.738  -8.561  1.00 137.59 ? 80  GLN C CA  1 
ATOM   9147  C C   . GLN C 1 80  ? 78.746  37.866  -7.854  1.00 139.26 ? 80  GLN C C   1 
ATOM   9148  O O   . GLN C 1 80  ? 77.952  36.923  -7.851  1.00 138.08 ? 80  GLN C O   1 
ATOM   9149  C CB  . GLN C 1 80  ? 81.242  37.785  -7.552  1.00 141.02 ? 80  GLN C CB  1 
ATOM   9150  C CG  . GLN C 1 80  ? 81.335  36.585  -6.609  1.00 142.14 ? 80  GLN C CG  1 
ATOM   9151  C CD  . GLN C 1 80  ? 81.734  35.295  -7.295  1.00 138.45 ? 80  GLN C CD  1 
ATOM   9152  O OE1 . GLN C 1 80  ? 82.545  35.282  -8.227  1.00 135.86 ? 80  GLN C OE1 1 
ATOM   9153  N NE2 . GLN C 1 80  ? 81.154  34.188  -6.851  1.00 138.29 ? 80  GLN C NE2 1 
ATOM   9154  N N   . GLU C 1 81  ? 78.502  39.060  -7.298  1.00 142.05 ? 81  GLU C N   1 
ATOM   9155  C CA  . GLU C 1 81  ? 77.344  39.332  -6.457  1.00 144.26 ? 81  GLU C CA  1 
ATOM   9156  C C   . GLU C 1 81  ? 76.044  39.272  -7.267  1.00 141.47 ? 81  GLU C C   1 
ATOM   9157  O O   . GLU C 1 81  ? 75.010  38.875  -6.736  1.00 142.14 ? 81  GLU C O   1 
ATOM   9158  C CB  . GLU C 1 81  ? 77.641  40.664  -5.764  1.00 147.97 ? 81  GLU C CB  1 
ATOM   9159  C CG  . GLU C 1 81  ? 76.430  41.347  -5.142  1.00 150.52 ? 81  GLU C CG  1 
ATOM   9160  C CD  . GLU C 1 81  ? 76.780  42.664  -4.480  1.00 154.72 ? 81  GLU C CD  1 
ATOM   9161  O OE1 . GLU C 1 81  ? 77.980  42.919  -4.274  1.00 156.15 ? 81  GLU C OE1 1 
ATOM   9162  O OE2 . GLU C 1 81  ? 75.858  43.445  -4.183  1.00 156.82 ? 81  GLU C OE2 1 
ATOM   9163  N N   . SER C 1 82  ? 76.112  39.632  -8.556  1.00 138.43 ? 82  SER C N   1 
ATOM   9164  C CA  . SER C 1 82  ? 74.938  39.785  -9.406  1.00 136.24 ? 82  SER C CA  1 
ATOM   9165  C C   . SER C 1 82  ? 74.178  38.472  -9.577  1.00 133.81 ? 82  SER C C   1 
ATOM   9166  O O   . SER C 1 82  ? 72.957  38.488  -9.727  1.00 133.09 ? 82  SER C O   1 
ATOM   9167  C CB  . SER C 1 82  ? 75.326  40.343  -10.758 1.00 133.56 ? 82  SER C CB  1 
ATOM   9168  O OG  . SER C 1 82  ? 76.301  39.533  -11.402 1.00 130.90 ? 82  SER C OG  1 
ATOM   9169  N N   . GLY C 1 83  ? 74.917  37.354  -9.596  1.00 132.41 ? 83  GLY C N   1 
ATOM   9170  C CA  . GLY C 1 83  ? 74.357  36.046  -9.892  1.00 129.95 ? 83  GLY C CA  1 
ATOM   9171  C C   . GLY C 1 83  ? 74.844  35.517  -11.241 1.00 125.90 ? 83  GLY C C   1 
ATOM   9172  O O   . GLY C 1 83  ? 74.764  34.315  -11.496 1.00 123.78 ? 83  GLY C O   1 
ATOM   9173  N N   . LEU C 1 84  ? 75.364  36.422  -12.084 1.00 125.07 ? 84  LEU C N   1 
ATOM   9174  C CA  . LEU C 1 84  ? 75.755  36.097  -13.450 1.00 121.69 ? 84  LEU C CA  1 
ATOM   9175  C C   . LEU C 1 84  ? 77.074  35.321  -13.469 1.00 121.75 ? 84  LEU C C   1 
ATOM   9176  O O   . LEU C 1 84  ? 77.881  35.469  -12.552 1.00 123.63 ? 84  LEU C O   1 
ATOM   9177  C CB  . LEU C 1 84  ? 75.863  37.389  -14.262 1.00 120.88 ? 84  LEU C CB  1 
ATOM   9178  C CG  . LEU C 1 84  ? 74.541  38.064  -14.639 1.00 120.30 ? 84  LEU C CG  1 
ATOM   9179  C CD1 . LEU C 1 84  ? 74.727  39.465  -15.202 1.00 120.68 ? 84  LEU C CD1 1 
ATOM   9180  C CD2 . LEU C 1 84  ? 73.823  37.188  -15.643 1.00 116.67 ? 84  LEU C CD2 1 
ATOM   9181  N N   . LYS C 1 85  ? 77.253  34.503  -14.529 1.00 119.50 ? 85  LYS C N   1 
ATOM   9182  C CA  . LYS C 1 85  ? 78.484  33.772  -14.817 1.00 119.54 ? 85  LYS C CA  1 
ATOM   9183  C C   . LYS C 1 85  ? 79.289  34.514  -15.889 1.00 118.88 ? 85  LYS C C   1 
ATOM   9184  O O   . LYS C 1 85  ? 78.732  35.326  -16.629 1.00 117.47 ? 85  LYS C O   1 
ATOM   9185  C CB  . LYS C 1 85  ? 78.211  32.347  -15.316 1.00 116.93 ? 85  LYS C CB  1 
ATOM   9186  C CG  . LYS C 1 85  ? 77.278  31.503  -14.464 1.00 118.10 ? 85  LYS C CG  1 
ATOM   9187  C CD  . LYS C 1 85  ? 77.748  31.248  -13.037 1.00 121.80 ? 85  LYS C CD  1 
ATOM   9188  C CE  . LYS C 1 85  ? 76.845  30.286  -12.325 1.00 123.03 ? 85  LYS C CE  1 
ATOM   9189  N NZ  . LYS C 1 85  ? 77.050  30.288  -10.875 1.00 127.07 ? 85  LYS C NZ  1 
ATOM   9190  N N   . LEU C 1 86  ? 80.594  34.203  -15.988 1.00 119.79 ? 86  LEU C N   1 
ATOM   9191  C CA  . LEU C 1 86  ? 81.541  35.044  -16.713 1.00 120.11 ? 86  LEU C CA  1 
ATOM   9192  C C   . LEU C 1 86  ? 82.493  34.185  -17.537 1.00 117.74 ? 86  LEU C C   1 
ATOM   9193  O O   . LEU C 1 86  ? 83.186  33.331  -16.992 1.00 117.60 ? 86  LEU C O   1 
ATOM   9194  C CB  . LEU C 1 86  ? 82.309  35.940  -15.736 1.00 124.38 ? 86  LEU C CB  1 
ATOM   9195  C CG  . LEU C 1 86  ? 83.435  36.820  -16.303 1.00 125.27 ? 86  LEU C CG  1 
ATOM   9196  C CD1 . LEU C 1 86  ? 83.073  37.580  -17.569 1.00 123.18 ? 86  LEU C CD1 1 
ATOM   9197  C CD2 . LEU C 1 86  ? 83.899  37.823  -15.246 1.00 129.50 ? 86  LEU C CD2 1 
ATOM   9198  N N   . ILE C 1 87  ? 82.496  34.436  -18.853 1.00 115.82 ? 87  ILE C N   1 
ATOM   9199  C CA  . ILE C 1 87  ? 83.510  33.935  -19.764 1.00 114.85 ? 87  ILE C CA  1 
ATOM   9200  C C   . ILE C 1 87  ? 84.509  35.074  -19.948 1.00 117.07 ? 87  ILE C C   1 
ATOM   9201  O O   . ILE C 1 87  ? 84.335  35.910  -20.831 1.00 116.55 ? 87  ILE C O   1 
ATOM   9202  C CB  . ILE C 1 87  ? 82.904  33.489  -21.112 1.00 112.07 ? 87  ILE C CB  1 
ATOM   9203  C CG1 . ILE C 1 87  ? 81.567  32.736  -20.964 1.00 112.12 ? 87  ILE C CG1 1 
ATOM   9204  C CG2 . ILE C 1 87  ? 83.918  32.678  -21.921 1.00 109.83 ? 87  ILE C CG2 1 
ATOM   9205  C CD1 . ILE C 1 87  ? 81.686  31.354  -20.348 1.00 113.11 ? 87  ILE C CD1 1 
ATOM   9206  N N   . MET C 1 88  ? 85.519  35.126  -19.068 1.00 120.28 ? 88  MET C N   1 
ATOM   9207  C CA  . MET C 1 88  ? 86.452  36.241  -18.992 1.00 122.14 ? 88  MET C CA  1 
ATOM   9208  C C   . MET C 1 88  ? 87.476  36.164  -20.124 1.00 119.62 ? 88  MET C C   1 
ATOM   9209  O O   . MET C 1 88  ? 88.225  35.196  -20.230 1.00 119.09 ? 88  MET C O   1 
ATOM   9210  C CB  . MET C 1 88  ? 87.208  36.216  -17.660 1.00 126.66 ? 88  MET C CB  1 
ATOM   9211  C CG  . MET C 1 88  ? 87.925  37.503  -17.319 1.00 131.30 ? 88  MET C CG  1 
ATOM   9212  S SD  . MET C 1 88  ? 88.939  37.286  -15.843 1.00 137.95 ? 88  MET C SD  1 
ATOM   9213  C CE  . MET C 1 88  ? 88.986  38.987  -15.265 1.00 141.78 ? 88  MET C CE  1 
ATOM   9214  N N   . GLY C 1 89  ? 87.532  37.218  -20.942 1.00 118.97 ? 89  GLY C N   1 
ATOM   9215  C CA  . GLY C 1 89  ? 88.488  37.302  -22.034 1.00 117.63 ? 89  GLY C CA  1 
ATOM   9216  C C   . GLY C 1 89  ? 89.743  38.053  -21.604 1.00 120.61 ? 89  GLY C C   1 
ATOM   9217  O O   . GLY C 1 89  ? 89.652  39.080  -20.931 1.00 121.79 ? 89  GLY C O   1 
ATOM   9218  N N   . ILE C 1 90  ? 90.915  37.535  -21.990 1.00 121.39 ? 90  ILE C N   1 
ATOM   9219  C CA  . ILE C 1 90  ? 92.197  38.245  -21.698 1.00 124.27 ? 90  ILE C CA  1 
ATOM   9220  C C   . ILE C 1 90  ? 92.645  38.882  -23.021 1.00 125.58 ? 90  ILE C C   1 
ATOM   9221  O O   . ILE C 1 90  ? 92.649  38.153  -24.029 1.00 123.17 ? 90  ILE C O   1 
ATOM   9222  C CB  . ILE C 1 90  ? 93.228  37.285  -21.083 1.00 123.38 ? 90  ILE C CB  1 
ATOM   9223  C CG1 . ILE C 1 90  ? 93.065  37.200  -19.569 1.00 125.84 ? 90  ILE C CG1 1 
ATOM   9224  C CG2 . ILE C 1 90  ? 94.651  37.685  -21.459 1.00 123.92 ? 90  ILE C CG2 1 
ATOM   9225  C CD1 . ILE C 1 90  ? 91.878  36.375  -19.110 1.00 125.31 ? 90  ILE C CD1 1 
ATOM   9226  N N   . ASP C 1 91  ? 92.986  40.175  -22.986 1.00 130.27 ? 91  ASP C N   1 
ATOM   9227  C CA  . ASP C 1 91  ? 93.304  40.927  -24.230 1.00 129.52 ? 91  ASP C CA  1 
ATOM   9228  C C   . ASP C 1 91  ? 94.741  40.708  -24.694 1.00 128.97 ? 91  ASP C C   1 
ATOM   9229  O O   . ASP C 1 91  ? 95.605  41.538  -24.354 1.00 129.56 ? 91  ASP C O   1 
ATOM   9230  C CB  . ASP C 1 91  ? 93.052  42.417  -24.054 1.00 129.94 ? 91  ASP C CB  1 
ATOM   9231  C CG  . ASP C 1 91  ? 93.033  43.237  -25.336 1.00 127.54 ? 91  ASP C CG  1 
ATOM   9232  O OD1 . ASP C 1 91  ? 92.931  42.631  -26.422 1.00 123.07 ? 91  ASP C OD1 1 
ATOM   9233  O OD2 . ASP C 1 91  ? 93.119  44.476  -25.235 1.00 128.89 ? 91  ASP C OD2 1 
ATOM   9234  N N   . ILE C 1 92  ? 94.992  39.634  -25.435 1.00 129.80 ? 92  ILE C N   1 
ATOM   9235  C CA  . ILE C 1 92  ? 96.343  39.506  -26.046 1.00 129.05 ? 92  ILE C CA  1 
ATOM   9236  C C   . ILE C 1 92  ? 96.167  40.076  -27.461 1.00 126.42 ? 92  ILE C C   1 
ATOM   9237  O O   . ILE C 1 92  ? 95.484  39.441  -28.290 1.00 120.45 ? 92  ILE C O   1 
ATOM   9238  C CB  . ILE C 1 92  ? 96.880  38.065  -25.963 1.00 127.76 ? 92  ILE C CB  1 
ATOM   9239  C CG1 . ILE C 1 92  ? 97.827  37.922  -24.783 1.00 129.32 ? 92  ILE C CG1 1 
ATOM   9240  C CG2 . ILE C 1 92  ? 97.564  37.617  -27.255 1.00 127.26 ? 92  ILE C CG2 1 
ATOM   9241  C CD1 . ILE C 1 92  ? 97.259  37.132  -23.623 1.00 131.43 ? 92  ILE C CD1 1 
ATOM   9242  N N   . LYS C 1 93  ? 96.643  41.300  -27.679 1.00 129.36 ? 93  LYS C N   1 
ATOM   9243  C CA  . LYS C 1 93  ? 96.420  41.956  -28.991 1.00 127.44 ? 93  LYS C CA  1 
ATOM   9244  C C   . LYS C 1 93  ? 96.751  40.964  -30.108 1.00 123.52 ? 93  LYS C C   1 
ATOM   9245  O O   . LYS C 1 93  ? 97.866  40.414  -30.123 1.00 124.88 ? 93  LYS C O   1 
ATOM   9246  C CB  . LYS C 1 93  ? 97.251  43.233  -29.144 1.00 131.12 ? 93  LYS C CB  1 
ATOM   9247  C CG  . LYS C 1 93  ? 97.255  44.137  -27.923 1.00 134.31 ? 93  LYS C CG  1 
ATOM   9248  C CD  . LYS C 1 93  ? 95.970  44.939  -27.766 1.00 132.91 ? 93  LYS C CD  1 
ATOM   9249  C CE  . LYS C 1 93  ? 95.991  45.785  -26.535 1.00 135.80 ? 93  LYS C CE  1 
ATOM   9250  N NZ  . LYS C 1 93  ? 94.695  46.419  -26.287 1.00 136.92 ? 93  LYS C NZ  1 
ATOM   9251  N N   . PRO C 1 94  ? 95.830  40.735  -31.057 1.00 117.62 ? 94  PRO C N   1 
ATOM   9252  C CA  . PRO C 1 94  ? 96.063  39.749  -32.116 1.00 113.74 ? 94  PRO C CA  1 
ATOM   9253  C C   . PRO C 1 94  ? 97.181  40.053  -33.112 1.00 113.12 ? 94  PRO C C   1 
ATOM   9254  O O   . PRO C 1 94  ? 97.708  39.129  -33.735 1.00 110.19 ? 94  PRO C O   1 
ATOM   9255  C CB  . PRO C 1 94  ? 94.692  39.694  -32.832 1.00 111.58 ? 94  PRO C CB  1 
ATOM   9256  C CG  . PRO C 1 94  ? 94.041  41.018  -32.557 1.00 112.98 ? 94  PRO C CG  1 
ATOM   9257  C CD  . PRO C 1 94  ? 94.522  41.397  -31.173 1.00 116.61 ? 94  PRO C CD  1 
ATOM   9258  N N   . GLU C 1 95  ? 97.507  41.347  -33.265 1.00 114.16 ? 95  GLU C N   1 
ATOM   9259  C CA  . GLU C 1 95  ? 98.395  41.806  -34.317 1.00 114.33 ? 95  GLU C CA  1 
ATOM   9260  C C   . GLU C 1 95  ? 99.827  41.883  -33.803 1.00 115.29 ? 95  GLU C C   1 
ATOM   9261  O O   . GLU C 1 95  ? 100.689 42.311  -34.558 1.00 115.63 ? 95  GLU C O   1 
ATOM   9262  C CB  . GLU C 1 95  ? 98.064  43.195  -34.868 1.00 117.18 ? 95  GLU C CB  1 
ATOM   9263  C CG  . GLU C 1 95  ? 96.600  43.425  -35.231 1.00 117.56 ? 95  GLU C CG  1 
ATOM   9264  C CD  . GLU C 1 95  ? 95.698  43.885  -34.090 1.00 121.22 ? 95  GLU C CD  1 
ATOM   9265  O OE1 . GLU C 1 95  ? 96.246  44.020  -32.970 1.00 123.82 ? 95  GLU C OE1 1 
ATOM   9266  O OE2 . GLU C 1 95  ? 94.466  44.115  -34.300 1.00 121.52 ? 95  GLU C OE2 1 
ATOM   9267  N N   . GLU C 1 96  ? 100.078 41.496  -32.539 1.00 115.50 ? 96  GLU C N   1 
ATOM   9268  C CA  . GLU C 1 96  ? 101.433 41.490  -31.989 1.00 117.59 ? 96  GLU C CA  1 
ATOM   9269  C C   . GLU C 1 96  ? 102.161 40.205  -32.389 1.00 115.35 ? 96  GLU C C   1 
ATOM   9270  O O   . GLU C 1 96  ? 101.538 39.212  -32.772 1.00 112.22 ? 96  GLU C O   1 
ATOM   9271  C CB  . GLU C 1 96  ? 101.525 41.609  -30.463 1.00 120.17 ? 96  GLU C CB  1 
ATOM   9272  C CG  . GLU C 1 96  ? 101.092 42.954  -29.886 1.00 123.16 ? 96  GLU C CG  1 
ATOM   9273  C CD  . GLU C 1 96  ? 101.623 44.196  -30.578 1.00 125.82 ? 96  GLU C CD  1 
ATOM   9274  O OE1 . GLU C 1 96  ? 102.855 44.302  -30.808 1.00 126.92 ? 96  GLU C OE1 1 
ATOM   9275  O OE2 . GLU C 1 96  ? 100.764 45.068  -30.880 1.00 126.58 ? 96  GLU C OE2 1 
ATOM   9276  N N   . ASP C 1 97  ? 103.496 40.244  -32.321 1.00 115.98 ? 97  ASP C N   1 
ATOM   9277  C CA  . ASP C 1 97  ? 104.312 39.048  -32.671 1.00 114.85 ? 97  ASP C CA  1 
ATOM   9278  C C   . ASP C 1 97  ? 104.306 38.098  -31.476 1.00 115.17 ? 97  ASP C C   1 
ATOM   9279  O O   . ASP C 1 97  ? 104.727 38.519  -30.385 1.00 118.20 ? 97  ASP C O   1 
ATOM   9280  C CB  . ASP C 1 97  ? 105.716 39.432  -33.105 1.00 116.71 ? 97  ASP C CB  1 
ATOM   9281  C CG  . ASP C 1 97  ? 106.676 38.282  -33.375 1.00 116.31 ? 97  ASP C CG  1 
ATOM   9282  O OD1 . ASP C 1 97  ? 106.208 37.132  -33.498 1.00 113.54 ? 97  ASP C OD1 1 
ATOM   9283  O OD2 . ASP C 1 97  ? 107.889 38.553  -33.468 1.00 118.21 ? 97  ASP C OD2 1 
ATOM   9284  N N   . TYR C 1 98  ? 103.866 36.860  -31.691 1.00 112.09 ? 98  TYR C N   1 
ATOM   9285  C CA  . TYR C 1 98  ? 103.739 35.903  -30.564 1.00 111.49 ? 98  TYR C CA  1 
ATOM   9286  C C   . TYR C 1 98  ? 105.090 35.269  -30.308 1.00 113.05 ? 98  TYR C C   1 
ATOM   9287  O O   . TYR C 1 98  ? 105.344 34.817  -29.177 1.00 113.24 ? 98  TYR C O   1 
ATOM   9288  C CB  . TYR C 1 98  ? 102.686 34.853  -30.929 1.00 108.56 ? 98  TYR C CB  1 
ATOM   9289  C CG  . TYR C 1 98  ? 101.406 35.338  -31.597 1.00 106.67 ? 98  TYR C CG  1 
ATOM   9290  C CD1 . TYR C 1 98  ? 100.588 36.284  -30.994 1.00 108.01 ? 98  TYR C CD1 1 
ATOM   9291  C CD2 . TYR C 1 98  ? 101.000 34.822  -32.821 1.00 104.03 ? 98  TYR C CD2 1 
ATOM   9292  C CE1 . TYR C 1 98  ? 99.416  36.714  -31.592 1.00 106.03 ? 98  TYR C CE1 1 
ATOM   9293  C CE2 . TYR C 1 98  ? 99.833  35.245  -33.433 1.00 102.05 ? 98  TYR C CE2 1 
ATOM   9294  C CZ  . TYR C 1 98  ? 99.038  36.193  -32.815 1.00 103.14 ? 98  TYR C CZ  1 
ATOM   9295  O OH  . TYR C 1 98  ? 97.886  36.615  -33.409 1.00 102.35 ? 98  TYR C OH  1 
ATOM   9296  N N   . GLY C 1 99  ? 105.930 35.222  -31.342 1.00 113.80 ? 99  GLY C N   1 
ATOM   9297  C CA  . GLY C 1 99  ? 107.277 34.638  -31.205 1.00 115.90 ? 99  GLY C CA  1 
ATOM   9298  C C   . GLY C 1 99  ? 108.266 35.681  -30.740 1.00 120.17 ? 99  GLY C C   1 
ATOM   9299  O O   . GLY C 1 99  ? 109.472 35.523  -31.013 1.00 121.16 ? 99  GLY C O   1 
ATOM   9300  N N   . ASP C 1 100 ? 107.770 36.721  -30.074 1.00 122.59 ? 100 ASP C N   1 
ATOM   9301  C CA  . ASP C 1 100 ? 108.635 37.767  -29.574 1.00 126.49 ? 100 ASP C CA  1 
ATOM   9302  C C   . ASP C 1 100 ? 108.606 37.685  -28.050 1.00 130.05 ? 100 ASP C C   1 
ATOM   9303  O O   . ASP C 1 100 ? 107.593 38.028  -27.438 1.00 129.24 ? 100 ASP C O   1 
ATOM   9304  C CB  . ASP C 1 100 ? 108.174 39.092  -30.143 1.00 125.75 ? 100 ASP C CB  1 
ATOM   9305  C CG  . ASP C 1 100 ? 109.027 40.276  -29.762 1.00 128.47 ? 100 ASP C CG  1 
ATOM   9306  O OD1 . ASP C 1 100 ? 109.937 40.090  -28.939 1.00 130.81 ? 100 ASP C OD1 1 
ATOM   9307  O OD2 . ASP C 1 100 ? 108.751 41.353  -30.300 1.00 128.90 ? 100 ASP C OD2 1 
ATOM   9308  N N   . PRO C 1 101 ? 109.693 37.199  -27.400 1.00 134.45 ? 101 PRO C N   1 
ATOM   9309  C CA  . PRO C 1 101 ? 109.682 36.907  -25.963 1.00 137.86 ? 101 PRO C CA  1 
ATOM   9310  C C   . PRO C 1 101 ? 109.116 37.995  -25.058 1.00 142.57 ? 101 PRO C C   1 
ATOM   9311  O O   . PRO C 1 101 ? 108.585 37.673  -23.995 1.00 145.01 ? 101 PRO C O   1 
ATOM   9312  C CB  . PRO C 1 101 ? 111.152 36.646  -25.629 1.00 139.60 ? 101 PRO C CB  1 
ATOM   9313  C CG  . PRO C 1 101 ? 111.730 36.143  -26.916 1.00 137.90 ? 101 PRO C CG  1 
ATOM   9314  C CD  . PRO C 1 101 ? 110.994 36.893  -28.016 1.00 135.71 ? 101 PRO C CD  1 
ATOM   9315  N N   . GLU C 1 102 ? 109.263 39.268  -25.466 1.00 145.69 ? 102 GLU C N   1 
ATOM   9316  C CA  . GLU C 1 102 ? 108.765 40.384  -24.671 1.00 148.36 ? 102 GLU C CA  1 
ATOM   9317  C C   . GLU C 1 102 ? 107.237 40.323  -24.603 1.00 143.85 ? 102 GLU C C   1 
ATOM   9318  O O   . GLU C 1 102 ? 106.660 40.586  -23.549 1.00 145.20 ? 102 GLU C O   1 
ATOM   9319  C CB  . GLU C 1 102 ? 109.299 41.771  -25.063 1.00 152.19 ? 102 GLU C CB  1 
ATOM   9320  C CG  . GLU C 1 102 ? 109.135 42.188  -26.526 1.00 151.61 ? 102 GLU C CG  1 
ATOM   9321  C CD  . GLU C 1 102 ? 109.576 43.624  -26.815 1.00 155.16 ? 102 GLU C CD  1 
ATOM   9322  O OE1 . GLU C 1 102 ? 109.266 44.140  -27.915 1.00 155.00 ? 102 GLU C OE1 1 
ATOM   9323  O OE2 . GLU C 1 102 ? 110.248 44.244  -25.954 1.00 159.13 ? 102 GLU C OE2 1 
ATOM   9324  N N   . PHE C 1 103 ? 106.589 39.957  -25.717 1.00 138.71 ? 103 PHE C N   1 
ATOM   9325  C CA  . PHE C 1 103 ? 105.139 39.864  -25.745 1.00 134.79 ? 103 PHE C CA  1 
ATOM   9326  C C   . PHE C 1 103 ? 104.713 38.756  -24.794 1.00 132.46 ? 103 PHE C C   1 
ATOM   9327  O O   . PHE C 1 103 ? 103.779 38.929  -24.017 1.00 131.97 ? 103 PHE C O   1 
ATOM   9328  C CB  . PHE C 1 103 ? 104.619 39.575  -27.152 1.00 131.29 ? 103 PHE C CB  1 
ATOM   9329  C CG  . PHE C 1 103 ? 103.107 39.640  -27.274 1.00 129.87 ? 103 PHE C CG  1 
ATOM   9330  C CD1 . PHE C 1 103 ? 102.362 40.567  -26.551 1.00 131.38 ? 103 PHE C CD1 1 
ATOM   9331  C CD2 . PHE C 1 103 ? 102.439 38.759  -28.114 1.00 127.40 ? 103 PHE C CD2 1 
ATOM   9332  C CE1 . PHE C 1 103 ? 100.987 40.611  -26.670 1.00 130.02 ? 103 PHE C CE1 1 
ATOM   9333  C CE2 . PHE C 1 103 ? 101.062 38.805  -28.226 1.00 125.86 ? 103 PHE C CE2 1 
ATOM   9334  C CZ  . PHE C 1 103 ? 100.340 39.732  -27.509 1.00 127.71 ? 103 PHE C CZ  1 
ATOM   9335  N N   . VAL C 1 104 ? 105.442 37.638  -24.865 1.00 130.68 ? 104 VAL C N   1 
ATOM   9336  C CA  . VAL C 1 104 ? 105.124 36.463  -24.074 1.00 129.24 ? 104 VAL C CA  1 
ATOM   9337  C C   . VAL C 1 104 ? 105.335 36.795  -22.600 1.00 130.66 ? 104 VAL C C   1 
ATOM   9338  O O   . VAL C 1 104 ? 104.514 36.425  -21.763 1.00 129.78 ? 104 VAL C O   1 
ATOM   9339  C CB  . VAL C 1 104 ? 105.942 35.232  -24.505 1.00 128.99 ? 104 VAL C CB  1 
ATOM   9340  C CG1 . VAL C 1 104 ? 105.418 33.956  -23.848 1.00 128.26 ? 104 VAL C CG1 1 
ATOM   9341  C CG2 . VAL C 1 104 ? 105.961 35.063  -26.021 1.00 126.74 ? 104 VAL C CG2 1 
ATOM   9342  N N   . LYS C 1 105 ? 106.420 37.517  -22.297 1.00 132.42 ? 105 LYS C N   1 
ATOM   9343  C CA  . LYS C 1 105 ? 106.751 37.832  -20.914 1.00 135.06 ? 105 LYS C CA  1 
ATOM   9344  C C   . LYS C 1 105 ? 105.727 38.836  -20.361 1.00 134.92 ? 105 LYS C C   1 
ATOM   9345  O O   . LYS C 1 105 ? 105.250 38.662  -19.238 1.00 136.01 ? 105 LYS C O   1 
ATOM   9346  C CB  . LYS C 1 105 ? 108.243 38.185  -20.769 1.00 137.87 ? 105 LYS C CB  1 
ATOM   9347  C CG  . LYS C 1 105 ? 108.649 39.616  -21.110 1.00 139.96 ? 105 LYS C CG  1 
ATOM   9348  C CD  . LYS C 1 105 ? 110.142 39.835  -21.344 1.00 142.39 ? 105 LYS C CD  1 
ATOM   9349  C CE  . LYS C 1 105 ? 110.497 41.245  -21.723 1.00 144.35 ? 105 LYS C CE  1 
ATOM   9350  N NZ  . LYS C 1 105 ? 110.556 42.146  -20.572 1.00 148.07 ? 105 LYS C NZ  1 
ATOM   9351  N N   . ASP C 1 106 ? 105.359 39.863  -21.149 1.00 133.18 ? 106 ASP C N   1 
ATOM   9352  C CA  . ASP C 1 106 ? 104.334 40.817  -20.739 1.00 132.72 ? 106 ASP C CA  1 
ATOM   9353  C C   . ASP C 1 106 ? 103.004 40.093  -20.546 1.00 129.24 ? 106 ASP C C   1 
ATOM   9354  O O   . ASP C 1 106 ? 102.294 40.362  -19.582 1.00 130.26 ? 106 ASP C O   1 
ATOM   9355  C CB  . ASP C 1 106 ? 104.166 41.982  -21.706 1.00 132.27 ? 106 ASP C CB  1 
ATOM   9356  C CG  . ASP C 1 106 ? 105.204 43.092  -21.608 1.00 135.95 ? 106 ASP C CG  1 
ATOM   9357  O OD1 . ASP C 1 106 ? 105.660 43.389  -20.485 1.00 139.10 ? 106 ASP C OD1 1 
ATOM   9358  O OD2 . ASP C 1 106 ? 105.518 43.684  -22.654 1.00 135.76 ? 106 ASP C OD2 1 
ATOM   9359  N N   . SER C 1 107 ? 102.684 39.175  -21.469 1.00 125.04 ? 107 SER C N   1 
ATOM   9360  C CA  . SER C 1 107 ? 101.439 38.423  -21.429 1.00 121.77 ? 107 SER C CA  1 
ATOM   9361  C C   . SER C 1 107 ? 101.400 37.541  -20.184 1.00 122.97 ? 107 SER C C   1 
ATOM   9362  O O   . SER C 1 107 ? 100.335 37.348  -19.596 1.00 122.40 ? 107 SER C O   1 
ATOM   9363  C CB  . SER C 1 107 ? 101.244 37.582  -22.680 1.00 117.76 ? 107 SER C CB  1 
ATOM   9364  O OG  . SER C 1 107 ? 101.150 38.360  -23.867 1.00 116.23 ? 107 SER C OG  1 
ATOM   9365  N N   . GLU C 1 108 ? 102.563 36.985  -19.810 1.00 124.67 ? 108 GLU C N   1 
ATOM   9366  C CA  . GLU C 1 108 ? 102.642 36.057  -18.691 1.00 126.03 ? 108 GLU C CA  1 
ATOM   9367  C C   . GLU C 1 108 ? 102.356 36.813  -17.396 1.00 129.24 ? 108 GLU C C   1 
ATOM   9368  O O   . GLU C 1 108 ? 101.530 36.377  -16.592 1.00 129.61 ? 108 GLU C O   1 
ATOM   9369  C CB  . GLU C 1 108 ? 103.982 35.320  -18.599 1.00 127.36 ? 108 GLU C CB  1 
ATOM   9370  C CG  . GLU C 1 108 ? 104.144 34.168  -19.589 1.00 124.61 ? 108 GLU C CG  1 
ATOM   9371  C CD  . GLU C 1 108 ? 105.148 33.091  -19.195 1.00 126.16 ? 108 GLU C CD  1 
ATOM   9372  O OE1 . GLU C 1 108 ? 105.502 32.980  -18.002 1.00 129.21 ? 108 GLU C OE1 1 
ATOM   9373  O OE2 . GLU C 1 108 ? 105.595 32.352  -20.098 1.00 124.91 ? 108 GLU C OE2 1 
ATOM   9374  N N   . ILE C 1 109 ? 103.038 37.954  -17.228 1.00 131.84 ? 109 ILE C N   1 
ATOM   9375  C CA  . ILE C 1 109 ? 102.979 38.737  -16.003 1.00 135.54 ? 109 ILE C CA  1 
ATOM   9376  C C   . ILE C 1 109 ? 101.598 39.395  -15.904 1.00 135.23 ? 109 ILE C C   1 
ATOM   9377  O O   . ILE C 1 109 ? 101.002 39.430  -14.827 1.00 137.41 ? 109 ILE C O   1 
ATOM   9378  C CB  . ILE C 1 109 ? 104.169 39.726  -15.942 1.00 138.55 ? 109 ILE C CB  1 
ATOM   9379  C CG1 . ILE C 1 109 ? 104.395 40.285  -14.535 1.00 142.93 ? 109 ILE C CG1 1 
ATOM   9380  C CG2 . ILE C 1 109 ? 104.053 40.846  -16.979 1.00 137.75 ? 109 ILE C CG2 1 
ATOM   9381  C CD1 . ILE C 1 109 ? 105.041 39.309  -13.566 1.00 144.65 ? 109 ILE C CD1 1 
ATOM   9382  N N   . GLU C 1 110 ? 101.062 39.859  -17.045 1.00 132.64 ? 110 GLU C N   1 
ATOM   9383  C CA  . GLU C 1 110 ? 99.729  40.445  -17.103 1.00 131.51 ? 110 GLU C CA  1 
ATOM   9384  C C   . GLU C 1 110 ? 98.694  39.417  -16.660 1.00 129.82 ? 110 GLU C C   1 
ATOM   9385  O O   . GLU C 1 110 ? 97.818  39.715  -15.851 1.00 131.24 ? 110 GLU C O   1 
ATOM   9386  C CB  . GLU C 1 110 ? 99.412  40.920  -18.524 1.00 128.50 ? 110 GLU C CB  1 
ATOM   9387  C CG  . GLU C 1 110 ? 98.001  41.466  -18.703 1.00 127.05 ? 110 GLU C CG  1 
ATOM   9388  C CD  . GLU C 1 110 ? 97.640  42.617  -17.787 1.00 130.43 ? 110 GLU C CD  1 
ATOM   9389  O OE1 . GLU C 1 110 ? 98.550  43.296  -17.290 1.00 133.68 ? 110 GLU C OE1 1 
ATOM   9390  O OE2 . GLU C 1 110 ? 96.432  42.817  -17.552 1.00 130.14 ? 110 GLU C OE2 1 
ATOM   9391  N N   . LEU C 1 111 ? 98.803  38.209  -17.214 1.00 127.04 ? 111 LEU C N   1 
ATOM   9392  C CA  . LEU C 1 111 ? 97.850  37.160  -16.917 1.00 125.37 ? 111 LEU C CA  1 
ATOM   9393  C C   . LEU C 1 111 ? 97.982  36.764  -15.451 1.00 128.28 ? 111 LEU C C   1 
ATOM   9394  O O   . LEU C 1 111 ? 97.014  36.824  -14.697 1.00 128.82 ? 111 LEU C O   1 
ATOM   9395  C CB  . LEU C 1 111 ? 98.093  35.985  -17.859 1.00 122.41 ? 111 LEU C CB  1 
ATOM   9396  C CG  . LEU C 1 111 ? 97.094  34.829  -17.755 1.00 120.18 ? 111 LEU C CG  1 
ATOM   9397  C CD1 . LEU C 1 111 ? 97.216  33.962  -18.994 1.00 116.86 ? 111 LEU C CD1 1 
ATOM   9398  C CD2 . LEU C 1 111 ? 97.315  34.008  -16.493 1.00 122.28 ? 111 LEU C CD2 1 
ATOM   9399  N N   . LYS C 1 112 ? 99.190  36.366  -15.047 1.00 130.15 ? 112 LYS C N   1 
ATOM   9400  C CA  . LYS C 1 112 ? 99.377  35.865  -13.698 1.00 133.20 ? 112 LYS C CA  1 
ATOM   9401  C C   . LYS C 1 112 ? 98.785  36.866  -12.711 1.00 136.67 ? 112 LYS C C   1 
ATOM   9402  O O   . LYS C 1 112 ? 98.199  36.466  -11.709 1.00 138.22 ? 112 LYS C O   1 
ATOM   9403  C CB  . LYS C 1 112 ? 100.838 35.586  -13.341 1.00 135.35 ? 112 LYS C CB  1 
ATOM   9404  C CG  . LYS C 1 112 ? 101.013 34.605  -12.189 1.00 137.23 ? 112 LYS C CG  1 
ATOM   9405  C CD  . LYS C 1 112 ? 101.875 33.397  -12.541 1.00 136.28 ? 112 LYS C CD  1 
ATOM   9406  C CE  . LYS C 1 112 ? 103.338 33.770  -12.630 1.00 138.50 ? 112 LYS C CE  1 
ATOM   9407  N NZ  . LYS C 1 112 ? 104.245 32.646  -12.881 1.00 137.93 ? 112 LYS C NZ  1 
ATOM   9408  N N   . ARG C 1 113 ? 98.931  38.164  -13.017 1.00 138.25 ? 113 ARG C N   1 
ATOM   9409  C CA  . ARG C 1 113 ? 98.375  39.210  -12.177 1.00 141.72 ? 113 ARG C CA  1 
ATOM   9410  C C   . ARG C 1 113 ? 96.868  39.010  -12.052 1.00 140.70 ? 113 ARG C C   1 
ATOM   9411  O O   . ARG C 1 113 ? 96.373  38.790  -10.950 1.00 143.06 ? 113 ARG C O   1 
ATOM   9412  C CB  . ARG C 1 113 ? 98.600  40.630  -12.708 1.00 142.73 ? 113 ARG C CB  1 
ATOM   9413  C CG  . ARG C 1 113 ? 98.073  41.709  -11.768 1.00 146.30 ? 113 ARG C CG  1 
ATOM   9414  C CD  . ARG C 1 113 ? 97.143  42.675  -12.481 1.00 145.12 ? 113 ARG C CD  1 
ATOM   9415  N NE  . ARG C 1 113 ? 97.795  43.435  -13.555 1.00 144.46 ? 113 ARG C NE  1 
ATOM   9416  C CZ  . ARG C 1 113 ? 97.165  44.069  -14.546 1.00 142.40 ? 113 ARG C CZ  1 
ATOM   9417  N NH1 . ARG C 1 113 ? 97.829  44.910  -15.323 1.00 142.71 ? 113 ARG C NH1 1 
ATOM   9418  N NH2 . ARG C 1 113 ? 95.865  43.903  -14.737 1.00 140.23 ? 113 ARG C NH2 1 
ATOM   9419  N N   . VAL C 1 114 ? 96.149  39.082  -13.181 1.00 137.58 ? 114 VAL C N   1 
ATOM   9420  C CA  . VAL C 1 114 ? 94.695  39.047  -13.131 1.00 136.59 ? 114 VAL C CA  1 
ATOM   9421  C C   . VAL C 1 114 ? 94.301  37.776  -12.390 1.00 136.51 ? 114 VAL C C   1 
ATOM   9422  O O   . VAL C 1 114 ? 93.414  37.809  -11.543 1.00 138.52 ? 114 VAL C O   1 
ATOM   9423  C CB  . VAL C 1 114 ? 93.930  39.142  -14.468 1.00 132.63 ? 114 VAL C CB  1 
ATOM   9424  C CG1 . VAL C 1 114 ? 94.115  40.496  -15.142 1.00 133.40 ? 114 VAL C CG1 1 
ATOM   9425  C CG2 . VAL C 1 114 ? 94.289  38.012  -15.422 1.00 129.10 ? 114 VAL C CG2 1 
ATOM   9426  N N   . LEU C 1 115 ? 94.985  36.669  -12.687 1.00 134.97 ? 115 LEU C N   1 
ATOM   9427  C CA  . LEU C 1 115 ? 94.646  35.406  -12.060 1.00 134.88 ? 115 LEU C CA  1 
ATOM   9428  C C   . LEU C 1 115 ? 94.859  35.486  -10.554 1.00 138.98 ? 115 LEU C C   1 
ATOM   9429  O O   . LEU C 1 115 ? 94.125  34.837  -9.814  1.00 140.06 ? 115 LEU C O   1 
ATOM   9430  C CB  . LEU C 1 115 ? 95.398  34.228  -12.668 1.00 133.06 ? 115 LEU C CB  1 
ATOM   9431  C CG  . LEU C 1 115 ? 94.548  33.352  -13.592 1.00 129.38 ? 115 LEU C CG  1 
ATOM   9432  C CD1 . LEU C 1 115 ? 94.054  34.116  -14.812 1.00 126.90 ? 115 LEU C CD1 1 
ATOM   9433  C CD2 . LEU C 1 115 ? 95.313  32.115  -14.005 1.00 128.03 ? 115 LEU C CD2 1 
ATOM   9434  N N   . ASN C 1 116 ? 95.830  36.295  -10.113 1.00 141.55 ? 116 ASN C N   1 
ATOM   9435  C CA  . ASN C 1 116 ? 96.200  36.349  -8.707  1.00 145.63 ? 116 ASN C CA  1 
ATOM   9436  C C   . ASN C 1 116 ? 95.025  36.783  -7.825  1.00 147.73 ? 116 ASN C C   1 
ATOM   9437  O O   . ASN C 1 116 ? 95.058  36.564  -6.615  1.00 150.91 ? 116 ASN C O   1 
ATOM   9438  C CB  . ASN C 1 116 ? 97.419  37.232  -8.472  1.00 148.36 ? 116 ASN C CB  1 
ATOM   9439  C CG  . ASN C 1 116 ? 97.945  37.075  -7.067  1.00 152.45 ? 116 ASN C CG  1 
ATOM   9440  O OD1 . ASN C 1 116 ? 97.733  37.953  -6.228  1.00 155.70 ? 116 ASN C OD1 1 
ATOM   9441  N ND2 . ASN C 1 116 ? 98.577  35.947  -6.778  1.00 152.44 ? 116 ASN C ND2 1 
ATOM   9442  N N   . TYR C 1 117 ? 93.997  37.407  -8.418  1.00 146.26 ? 117 TYR C N   1 
ATOM   9443  C CA  . TYR C 1 117 ? 92.760  37.692  -7.701  1.00 147.88 ? 117 TYR C CA  1 
ATOM   9444  C C   . TYR C 1 117 ? 91.581  36.927  -8.324  1.00 144.15 ? 117 TYR C C   1 
ATOM   9445  O O   . TYR C 1 117 ? 90.706  36.462  -7.599  1.00 145.08 ? 117 TYR C O   1 
ATOM   9446  C CB  . TYR C 1 117 ? 92.551  39.210  -7.602  1.00 150.20 ? 117 TYR C CB  1 
ATOM   9447  C CG  . TYR C 1 117 ? 92.490  39.945  -8.933  1.00 147.55 ? 117 TYR C CG  1 
ATOM   9448  C CD1 . TYR C 1 117 ? 91.303  40.020  -9.654  1.00 144.93 ? 117 TYR C CD1 1 
ATOM   9449  C CD2 . TYR C 1 117 ? 93.615  40.560  -9.472  1.00 148.10 ? 117 TYR C CD2 1 
ATOM   9450  C CE1 . TYR C 1 117 ? 91.235  40.678  -10.872 1.00 142.63 ? 117 TYR C CE1 1 
ATOM   9451  C CE2 . TYR C 1 117 ? 93.561  41.227  -10.686 1.00 145.86 ? 117 TYR C CE2 1 
ATOM   9452  C CZ  . TYR C 1 117 ? 92.369  41.281  -11.390 1.00 143.16 ? 117 TYR C CZ  1 
ATOM   9453  O OH  . TYR C 1 117 ? 92.300  41.923  -12.593 1.00 141.01 ? 117 TYR C OH  1 
ATOM   9454  N N   . ALA C 1 118 ? 91.557  36.765  -9.655  1.00 140.26 ? 118 ALA C N   1 
ATOM   9455  C CA  . ALA C 1 118 ? 90.408  36.192  -10.350 1.00 136.87 ? 118 ALA C CA  1 
ATOM   9456  C C   . ALA C 1 118 ? 90.041  34.812  -9.802  1.00 136.66 ? 118 ALA C C   1 
ATOM   9457  O O   . ALA C 1 118 ? 88.872  34.429  -9.816  1.00 135.21 ? 118 ALA C O   1 
ATOM   9458  C CB  . ALA C 1 118 ? 90.688  36.106  -11.834 1.00 133.08 ? 118 ALA C CB  1 
ATOM   9459  N N   . LYS C 1 119 ? 91.060  34.067  -9.357  1.00 138.16 ? 119 LYS C N   1 
ATOM   9460  C CA  . LYS C 1 119 ? 90.910  32.725  -8.806  1.00 138.20 ? 119 LYS C CA  1 
ATOM   9461  C C   . LYS C 1 119 ? 89.821  32.645  -7.733  1.00 140.03 ? 119 LYS C C   1 
ATOM   9462  O O   . LYS C 1 119 ? 89.258  31.571  -7.540  1.00 138.95 ? 119 LYS C O   1 
ATOM   9463  C CB  . LYS C 1 119 ? 92.255  32.238  -8.242  1.00 140.46 ? 119 LYS C CB  1 
ATOM   9464  C CG  . LYS C 1 119 ? 92.884  33.155  -7.190  1.00 144.89 ? 119 LYS C CG  1 
ATOM   9465  C CD  . LYS C 1 119 ? 94.268  32.775  -6.681  1.00 147.26 ? 119 LYS C CD  1 
ATOM   9466  C CE  . LYS C 1 119 ? 95.268  32.617  -7.782  1.00 144.85 ? 119 LYS C CE  1 
ATOM   9467  N NZ  . LYS C 1 119 ? 96.614  33.005  -7.357  1.00 147.68 ? 119 LYS C NZ  1 
ATOM   9468  N N   . LYS C 1 120 ? 89.533  33.761  -7.040  1.00 143.04 ? 120 LYS C N   1 
ATOM   9469  C CA  . LYS C 1 120 ? 88.634  33.761  -5.891  1.00 146.04 ? 120 LYS C CA  1 
ATOM   9470  C C   . LYS C 1 120 ? 87.237  34.218  -6.324  1.00 144.54 ? 120 LYS C C   1 
ATOM   9471  O O   . LYS C 1 120 ? 86.510  34.846  -5.548  1.00 147.17 ? 120 LYS C O   1 
ATOM   9472  C CB  . LYS C 1 120 ? 89.111  34.682  -4.756  1.00 150.99 ? 120 LYS C CB  1 
ATOM   9473  C CG  . LYS C 1 120 ? 90.591  35.079  -4.723  1.00 152.85 ? 120 LYS C CG  1 
ATOM   9474  C CD  . LYS C 1 120 ? 90.901  36.468  -4.158  1.00 156.80 ? 120 LYS C CD  1 
ATOM   9475  C CE  . LYS C 1 120 ? 89.805  37.499  -4.316  1.00 156.86 ? 120 LYS C CE  1 
ATOM   9476  N NZ  . LYS C 1 120 ? 90.286  38.885  -4.360  1.00 159.02 ? 120 LYS C NZ  1 
ATOM   9477  N N   . TYR C 1 121 ? 86.867  33.896  -7.571  1.00 140.31 ? 121 TYR C N   1 
ATOM   9478  C CA  . TYR C 1 121 ? 85.575  34.261  -8.133  1.00 138.08 ? 121 TYR C CA  1 
ATOM   9479  C C   . TYR C 1 121 ? 85.085  33.069  -8.955  1.00 134.26 ? 121 TYR C C   1 
ATOM   9480  O O   . TYR C 1 121 ? 85.454  32.913  -10.120 1.00 130.84 ? 121 TYR C O   1 
ATOM   9481  C CB  . TYR C 1 121 ? 85.690  35.565  -8.938  1.00 137.25 ? 121 TYR C CB  1 
ATOM   9482  C CG  . TYR C 1 121 ? 86.017  36.804  -8.110  1.00 141.12 ? 121 TYR C CG  1 
ATOM   9483  C CD1 . TYR C 1 121 ? 85.031  37.456  -7.379  1.00 143.20 ? 121 TYR C CD1 1 
ATOM   9484  C CD2 . TYR C 1 121 ? 87.310  37.321  -8.054  1.00 142.72 ? 121 TYR C CD2 1 
ATOM   9485  C CE1 . TYR C 1 121 ? 85.320  38.572  -6.612  1.00 147.10 ? 121 TYR C CE1 1 
ATOM   9486  C CE2 . TYR C 1 121 ? 87.610  38.440  -7.293  1.00 146.39 ? 121 TYR C CE2 1 
ATOM   9487  C CZ  . TYR C 1 121 ? 86.611  39.065  -6.570  1.00 148.69 ? 121 TYR C CZ  1 
ATOM   9488  O OH  . TYR C 1 121 ? 86.900  40.163  -5.820  1.00 152.81 ? 121 TYR C OH  1 
ATOM   9489  N N   . ASP C 1 122 ? 84.257  32.221  -8.329  1.00 134.94 ? 122 ASP C N   1 
ATOM   9490  C CA  . ASP C 1 122 ? 83.762  31.009  -8.968  1.00 131.90 ? 122 ASP C CA  1 
ATOM   9491  C C   . ASP C 1 122 ? 82.570  31.341  -9.871  1.00 129.64 ? 122 ASP C C   1 
ATOM   9492  O O   . ASP C 1 122 ? 81.740  30.473  -10.150 1.00 128.06 ? 122 ASP C O   1 
ATOM   9493  C CB  . ASP C 1 122 ? 83.490  29.910  -7.945  1.00 133.52 ? 122 ASP C CB  1 
ATOM   9494  C CG  . ASP C 1 122 ? 82.264  30.068  -7.052  1.00 135.48 ? 122 ASP C CG  1 
ATOM   9495  O OD1 . ASP C 1 122 ? 81.504  31.036  -7.243  1.00 135.22 ? 122 ASP C OD1 1 
ATOM   9496  O OD2 . ASP C 1 122 ? 82.063  29.205  -6.173  1.00 137.02 ? 122 ASP C OD2 1 
ATOM   9497  N N   . CYS C 1 123 ? 82.482  32.605  -10.311 1.00 129.82 ? 123 CYS C N   1 
ATOM   9498  C CA  . CYS C 1 123 ? 81.559  33.013  -11.358 1.00 127.27 ? 123 CYS C CA  1 
ATOM   9499  C C   . CYS C 1 123 ? 82.207  32.874  -12.734 1.00 124.71 ? 123 CYS C C   1 
ATOM   9500  O O   . CYS C 1 123 ? 81.505  32.818  -13.744 1.00 121.91 ? 123 CYS C O   1 
ATOM   9501  C CB  . CYS C 1 123 ? 81.076  34.442  -11.143 1.00 129.18 ? 123 CYS C CB  1 
ATOM   9502  S SG  . CYS C 1 123 ? 82.385  35.693  -11.072 1.00 131.24 ? 123 CYS C SG  1 
ATOM   9503  N N   . ILE C 1 124 ? 83.546  32.826  -12.760 1.00 126.27 ? 124 ILE C N   1 
ATOM   9504  C CA  . ILE C 1 124 ? 84.286  32.635  -13.996 1.00 124.19 ? 124 ILE C CA  1 
ATOM   9505  C C   . ILE C 1 124 ? 84.250  31.147  -14.345 1.00 121.90 ? 124 ILE C C   1 
ATOM   9506  O O   . ILE C 1 124 ? 84.621  30.308  -13.524 1.00 122.57 ? 124 ILE C O   1 
ATOM   9507  C CB  . ILE C 1 124 ? 85.722  33.188  -13.882 1.00 126.87 ? 124 ILE C CB  1 
ATOM   9508  C CG1 . ILE C 1 124 ? 85.727  34.616  -13.283 1.00 130.15 ? 124 ILE C CG1 1 
ATOM   9509  C CG2 . ILE C 1 124 ? 86.447  33.112  -15.231 1.00 124.23 ? 124 ILE C CG2 1 
ATOM   9510  C CD1 . ILE C 1 124 ? 86.835  35.534  -13.778 1.00 130.75 ? 124 ILE C CD1 1 
ATOM   9511  N N   . ILE C 1 125 ? 83.795  30.861  -15.575 1.00 118.90 ? 125 ILE C N   1 
ATOM   9512  C CA  . ILE C 1 125 ? 83.428  29.526  -16.028 1.00 116.81 ? 125 ILE C CA  1 
ATOM   9513  C C   . ILE C 1 125 ? 84.222  29.135  -17.277 1.00 113.21 ? 125 ILE C C   1 
ATOM   9514  O O   . ILE C 1 125 ? 84.275  27.956  -17.617 1.00 112.01 ? 125 ILE C O   1 
ATOM   9515  C CB  . ILE C 1 125 ? 81.897  29.447  -16.239 1.00 116.80 ? 125 ILE C CB  1 
ATOM   9516  C CG1 . ILE C 1 125 ? 81.235  28.596  -15.162 1.00 119.30 ? 125 ILE C CG1 1 
ATOM   9517  C CG2 . ILE C 1 125 ? 81.505  28.936  -17.626 1.00 113.43 ? 125 ILE C CG2 1 
ATOM   9518  C CD1 . ILE C 1 125 ? 81.168  29.261  -13.800 1.00 123.59 ? 125 ILE C CD1 1 
ATOM   9519  N N   . THR C 1 126 ? 84.809  30.112  -17.977 1.00 111.79 ? 126 THR C N   1 
ATOM   9520  C CA  . THR C 1 126 ? 85.788  29.832  -19.020 1.00 109.65 ? 126 THR C CA  1 
ATOM   9521  C C   . THR C 1 126 ? 86.689  31.059  -19.188 1.00 110.30 ? 126 THR C C   1 
ATOM   9522  O O   . THR C 1 126 ? 86.246  32.181  -18.942 1.00 111.66 ? 126 THR C O   1 
ATOM   9523  C CB  . THR C 1 126 ? 85.062  29.439  -20.311 1.00 106.03 ? 126 THR C CB  1 
ATOM   9524  O OG1 . THR C 1 126 ? 84.682  28.077  -20.144 1.00 105.41 ? 126 THR C OG1 1 
ATOM   9525  C CG2 . THR C 1 126 ? 85.931  29.501  -21.555 1.00 104.02 ? 126 THR C CG2 1 
ATOM   9526  N N   . TYR C 1 127 ? 87.957  30.831  -19.573 1.00 108.88 ? 127 TYR C N   1 
ATOM   9527  C CA  . TYR C 1 127 ? 88.860  31.900  -19.974 1.00 108.59 ? 127 TYR C CA  1 
ATOM   9528  C C   . TYR C 1 127 ? 89.010  31.856  -21.492 1.00 106.14 ? 127 TYR C C   1 
ATOM   9529  O O   . TYR C 1 127 ? 89.102  30.775  -22.067 1.00 105.32 ? 127 TYR C O   1 
ATOM   9530  C CB  . TYR C 1 127 ? 90.229  31.785  -19.296 1.00 110.01 ? 127 TYR C CB  1 
ATOM   9531  C CG  . TYR C 1 127 ? 90.280  32.201  -17.830 1.00 112.74 ? 127 TYR C CG  1 
ATOM   9532  C CD1 . TYR C 1 127 ? 90.045  31.284  -16.809 1.00 113.67 ? 127 TYR C CD1 1 
ATOM   9533  C CD2 . TYR C 1 127 ? 90.594  33.502  -17.457 1.00 114.54 ? 127 TYR C CD2 1 
ATOM   9534  C CE1 . TYR C 1 127 ? 90.099  31.651  -15.472 1.00 116.80 ? 127 TYR C CE1 1 
ATOM   9535  C CE2 . TYR C 1 127 ? 90.656  33.881  -16.123 1.00 117.77 ? 127 TYR C CE2 1 
ATOM   9536  C CZ  . TYR C 1 127 ? 90.410  32.954  -15.125 1.00 118.85 ? 127 TYR C CZ  1 
ATOM   9537  O OH  . TYR C 1 127 ? 90.468  33.314  -13.809 1.00 122.17 ? 127 TYR C OH  1 
ATOM   9538  N N   . LEU C 1 128 ? 89.010  33.037  -22.126 1.00 106.02 ? 128 LEU C N   1 
ATOM   9539  C CA  . LEU C 1 128 ? 89.314  33.170  -23.545 1.00 103.79 ? 128 LEU C CA  1 
ATOM   9540  C C   . LEU C 1 128 ? 90.701  33.809  -23.696 1.00 104.37 ? 128 LEU C C   1 
ATOM   9541  O O   . LEU C 1 128 ? 90.968  34.924  -23.239 1.00 106.38 ? 128 LEU C O   1 
ATOM   9542  C CB  . LEU C 1 128 ? 88.223  33.952  -24.284 1.00 103.00 ? 128 LEU C CB  1 
ATOM   9543  C CG  . LEU C 1 128 ? 86.805  33.365  -24.227 1.00 102.68 ? 128 LEU C CG  1 
ATOM   9544  C CD1 . LEU C 1 128 ? 85.806  34.277  -24.941 1.00 102.06 ? 128 LEU C CD1 1 
ATOM   9545  C CD2 . LEU C 1 128 ? 86.688  31.942  -24.785 1.00 100.57 ? 128 LEU C CD2 1 
ATOM   9546  N N   . VAL C 1 129 ? 91.587  33.075  -24.367 1.00 102.07 ? 129 VAL C N   1 
ATOM   9547  C CA  . VAL C 1 129 ? 93.010  33.363  -24.355 1.00 102.89 ? 129 VAL C CA  1 
ATOM   9548  C C   . VAL C 1 129 ? 93.362  34.338  -25.475 1.00 102.32 ? 129 VAL C C   1 
ATOM   9549  O O   . VAL C 1 129 ? 94.373  35.029  -25.394 1.00 104.65 ? 129 VAL C O   1 
ATOM   9550  C CB  . VAL C 1 129 ? 93.781  32.029  -24.451 1.00 101.44 ? 129 VAL C CB  1 
ATOM   9551  C CG1 . VAL C 1 129 ? 94.877  32.052  -25.503 1.00 100.78 ? 129 VAL C CG1 1 
ATOM   9552  C CG2 . VAL C 1 129 ? 94.313  31.592  -23.092 1.00 103.60 ? 129 VAL C CG2 1 
ATOM   9553  N N   . ILE C 1 130 ? 92.550  34.375  -26.531 1.00 99.68  ? 130 ILE C N   1 
ATOM   9554  C CA  . ILE C 1 130 ? 92.810  35.258  -27.650 1.00 99.29  ? 130 ILE C CA  1 
ATOM   9555  C C   . ILE C 1 130 ? 91.555  35.303  -28.489 1.00 97.96  ? 130 ILE C C   1 
ATOM   9556  O O   . ILE C 1 130 ? 90.743  34.388  -28.409 1.00 96.77  ? 130 ILE C O   1 
ATOM   9557  C CB  . ILE C 1 130 ? 94.000  34.787  -28.496 1.00 98.46  ? 130 ILE C CB  1 
ATOM   9558  C CG1 . ILE C 1 130 ? 94.429  35.855  -29.478 1.00 98.94  ? 130 ILE C CG1 1 
ATOM   9559  C CG2 . ILE C 1 130 ? 93.686  33.479  -29.215 1.00 95.72  ? 130 ILE C CG2 1 
ATOM   9560  C CD1 . ILE C 1 130 ? 95.834  35.662  -30.014 1.00 99.76  ? 130 ILE C CD1 1 
ATOM   9561  N N   . ASN C 1 131 ? 91.432  36.355  -29.299 1.00 99.30  ? 131 ASN C N   1 
ATOM   9562  C CA  . ASN C 1 131 ? 90.227  36.589  -30.073 1.00 98.58  ? 131 ASN C CA  1 
ATOM   9563  C C   . ASN C 1 131 ? 90.585  36.944  -31.516 1.00 98.86  ? 131 ASN C C   1 
ATOM   9564  O O   . ASN C 1 131 ? 91.375  37.858  -31.752 1.00 101.16 ? 131 ASN C O   1 
ATOM   9565  C CB  . ASN C 1 131 ? 89.383  37.678  -29.426 1.00 100.11 ? 131 ASN C CB  1 
ATOM   9566  C CG  . ASN C 1 131 ? 88.239  38.094  -30.317 1.00 99.55  ? 131 ASN C CG  1 
ATOM   9567  O OD1 . ASN C 1 131 ? 88.365  39.062  -31.076 1.00 100.65 ? 131 ASN C OD1 1 
ATOM   9568  N ND2 . ASN C 1 131 ? 87.136  37.360  -30.276 1.00 98.11  ? 131 ASN C ND2 1 
ATOM   9569  N N   . GLU C 1 132 ? 89.988  36.216  -32.473 1.00 97.22  ? 132 GLU C N   1 
ATOM   9570  C CA  . GLU C 1 132 ? 90.103  36.538  -33.889 1.00 97.40  ? 132 GLU C CA  1 
ATOM   9571  C C   . GLU C 1 132 ? 91.577  36.684  -34.292 1.00 97.25  ? 132 GLU C C   1 
ATOM   9572  O O   . GLU C 1 132 ? 92.009  37.750  -34.710 1.00 97.53  ? 132 GLU C O   1 
ATOM   9573  C CB  . GLU C 1 132 ? 89.326  37.816  -34.238 1.00 99.85  ? 132 GLU C CB  1 
ATOM   9574  C CG  . GLU C 1 132 ? 87.805  37.716  -34.095 1.00 101.85 ? 132 GLU C CG  1 
ATOM   9575  C CD  . GLU C 1 132 ? 87.005  38.881  -34.680 1.00 105.68 ? 132 GLU C CD  1 
ATOM   9576  O OE1 . GLU C 1 132 ? 87.502  39.327  -35.743 1.00 105.50 ? 132 GLU C OE1 1 
ATOM   9577  O OE2 . GLU C 1 132 ? 85.923  39.328  -34.161 1.00 109.72 ? 132 GLU C OE2 1 
ATOM   9578  N N   . PRO C 1 133 ? 92.422  35.641  -34.168 1.00 96.44  ? 133 PRO C N   1 
ATOM   9579  C CA  . PRO C 1 133 ? 93.739  35.682  -34.790 1.00 97.10  ? 133 PRO C CA  1 
ATOM   9580  C C   . PRO C 1 133 ? 93.628  35.433  -36.291 1.00 96.05  ? 133 PRO C C   1 
ATOM   9581  O O   . PRO C 1 133 ? 93.074  34.417  -36.721 1.00 93.28  ? 133 PRO C O   1 
ATOM   9582  C CB  . PRO C 1 133 ? 94.502  34.601  -34.045 1.00 97.48  ? 133 PRO C CB  1 
ATOM   9583  C CG  . PRO C 1 133 ? 93.430  33.601  -33.672 1.00 95.83  ? 133 PRO C CG  1 
ATOM   9584  C CD  . PRO C 1 133 ? 92.189  34.420  -33.385 1.00 95.98  ? 133 PRO C CD  1 
ATOM   9585  N N   . GLN C 1 134 ? 94.190  36.353  -37.079 1.00 98.61  ? 134 GLN C N   1 
ATOM   9586  C CA  . GLN C 1 134 ? 94.081  36.263  -38.556 1.00 99.63  ? 134 GLN C CA  1 
ATOM   9587  C C   . GLN C 1 134 ? 95.088  35.259  -39.124 1.00 100.38 ? 134 GLN C C   1 
ATOM   9588  O O   . GLN C 1 134 ? 96.168  35.103  -38.532 1.00 101.03 ? 134 GLN C O   1 
ATOM   9589  C CB  . GLN C 1 134 ? 94.302  37.638  -39.177 1.00 103.49 ? 134 GLN C CB  1 
ATOM   9590  C CG  . GLN C 1 134 ? 94.092  37.697  -40.687 1.00 104.86 ? 134 GLN C CG  1 
ATOM   9591  C CD  . GLN C 1 134 ? 92.706  37.276  -41.124 1.00 106.11 ? 134 GLN C CD  1 
ATOM   9592  O OE1 . GLN C 1 134 ? 91.698  37.903  -40.778 1.00 102.82 ? 134 GLN C OE1 1 
ATOM   9593  N NE2 . GLN C 1 134 ? 92.645  36.210  -41.908 1.00 108.03 ? 134 GLN C NE2 1 
ATOM   9594  N N   . THR C 1 135 ? 94.742  34.628  -40.244 1.00 98.95  ? 135 THR C N   1 
ATOM   9595  C CA  . THR C 1 135 ? 95.602  33.606  -40.860 1.00 96.93  ? 135 THR C CA  1 
ATOM   9596  C C   . THR C 1 135 ? 96.928  34.211  -41.261 1.00 97.73  ? 135 THR C C   1 
ATOM   9597  O O   . THR C 1 135 ? 97.949  33.778  -40.703 1.00 98.54  ? 135 THR C O   1 
ATOM   9598  C CB  . THR C 1 135 ? 94.834  33.023  -42.043 1.00 94.52  ? 135 THR C CB  1 
ATOM   9599  O OG1 . THR C 1 135 ? 93.609  32.582  -41.468 1.00 91.23  ? 135 THR C OG1 1 
ATOM   9600  C CG2 . THR C 1 135 ? 95.560  31.863  -42.697 1.00 94.22  ? 135 THR C CG2 1 
ATOM   9601  N N   . ASP C 1 136 ? 96.937  35.153  -42.207 1.00 98.80  ? 136 ASP C N   1 
ATOM   9602  C CA  . ASP C 1 136 ? 98.230  35.712  -42.696 1.00 100.23 ? 136 ASP C CA  1 
ATOM   9603  C C   . ASP C 1 136 ? 99.108  36.069  -41.500 1.00 102.60 ? 136 ASP C C   1 
ATOM   9604  O O   . ASP C 1 136 ? 100.295 35.699  -41.498 1.00 106.14 ? 136 ASP C O   1 
ATOM   9605  C CB  . ASP C 1 136 ? 98.068  36.939  -43.575 1.00 100.30 ? 136 ASP C CB  1 
ATOM   9606  C CG  . ASP C 1 136 ? 99.351  37.451  -44.207 1.00 102.48 ? 136 ASP C CG  1 
ATOM   9607  O OD1 . ASP C 1 136 ? 100.022 38.286  -43.570 1.00 104.81 ? 136 ASP C OD1 1 
ATOM   9608  O OD2 . ASP C 1 136 ? 99.666  37.007  -45.328 1.00 102.54 ? 136 ASP C OD2 1 
ATOM   9609  N N   . HIS C 1 137 ? 98.546  36.768  -40.522 1.00 101.80 ? 137 HIS C N   1 
ATOM   9610  C CA  . HIS C 1 137 ? 99.405  37.169  -39.413 1.00 102.31 ? 137 HIS C CA  1 
ATOM   9611  C C   . HIS C 1 137 ? 100.089 35.940  -38.804 1.00 101.41 ? 137 HIS C C   1 
ATOM   9612  O O   . HIS C 1 137 ? 101.280 35.981  -38.523 1.00 103.64 ? 137 HIS C O   1 
ATOM   9613  C CB  . HIS C 1 137 ? 98.640  38.051  -38.414 1.00 102.10 ? 137 HIS C CB  1 
ATOM   9614  C CG  . HIS C 1 137 ? 99.432  38.407  -37.204 1.00 103.15 ? 137 HIS C CG  1 
ATOM   9615  N ND1 . HIS C 1 137 ? 100.335 39.445  -37.175 1.00 104.73 ? 137 HIS C ND1 1 
ATOM   9616  C CD2 . HIS C 1 137 ? 99.466  37.845  -35.991 1.00 103.03 ? 137 HIS C CD2 1 
ATOM   9617  C CE1 . HIS C 1 137 ? 100.892 39.499  -35.974 1.00 106.42 ? 137 HIS C CE1 1 
ATOM   9618  N NE2 . HIS C 1 137 ? 100.376 38.545  -35.239 1.00 105.33 ? 137 HIS C NE2 1 
ATOM   9619  N N   . ILE C 1 138 ? 99.368  34.826  -38.645 1.00 98.39  ? 138 ILE C N   1 
ATOM   9620  C CA  . ILE C 1 138 ? 99.974  33.623  -38.096 1.00 97.90  ? 138 ILE C CA  1 
ATOM   9621  C C   . ILE C 1 138 ? 101.096 33.140  -39.021 1.00 98.76  ? 138 ILE C C   1 
ATOM   9622  O O   . ILE C 1 138 ? 102.163 32.748  -38.541 1.00 100.54 ? 138 ILE C O   1 
ATOM   9623  C CB  . ILE C 1 138 ? 98.927  32.528  -37.825 1.00 95.70  ? 138 ILE C CB  1 
ATOM   9624  C CG1 . ILE C 1 138 ? 97.924  32.967  -36.748 1.00 95.51  ? 138 ILE C CG1 1 
ATOM   9625  C CG2 . ILE C 1 138 ? 99.603  31.207  -37.444 1.00 95.65  ? 138 ILE C CG2 1 
ATOM   9626  C CD1 . ILE C 1 138 ? 96.710  32.070  -36.589 1.00 92.73  ? 138 ILE C CD1 1 
ATOM   9627  N N   . HIS C 1 139 ? 100.878 33.173  -40.345 1.00 97.28  ? 139 HIS C N   1 
ATOM   9628  C CA  . HIS C 1 139 ? 101.906 32.741  -41.285 1.00 97.21  ? 139 HIS C CA  1 
ATOM   9629  C C   . HIS C 1 139 ? 103.157 33.586  -41.090 1.00 99.64  ? 139 HIS C C   1 
ATOM   9630  O O   . HIS C 1 139 ? 104.246 33.031  -40.988 1.00 100.67 ? 139 HIS C O   1 
ATOM   9631  C CB  . HIS C 1 139 ? 101.433 32.836  -42.739 1.00 96.20  ? 139 HIS C CB  1 
ATOM   9632  C CG  . HIS C 1 139 ? 102.400 32.357  -43.776 1.00 97.19  ? 139 HIS C CG  1 
ATOM   9633  N ND1 . HIS C 1 139 ? 103.506 33.086  -44.156 1.00 100.06 ? 139 HIS C ND1 1 
ATOM   9634  C CD2 . HIS C 1 139 ? 102.428 31.252  -44.536 1.00 96.61  ? 139 HIS C CD2 1 
ATOM   9635  C CE1 . HIS C 1 139 ? 104.184 32.431  -45.092 1.00 100.07 ? 139 HIS C CE1 1 
ATOM   9636  N NE2 . HIS C 1 139 ? 103.542 31.321  -45.349 1.00 98.28  ? 139 HIS C NE2 1 
ATOM   9637  N N   . SER C 1 140 ? 102.993 34.918  -41.036 1.00 100.42 ? 140 SER C N   1 
ATOM   9638  C CA  . SER C 1 140 ? 104.130 35.826  -40.916 1.00 102.76 ? 140 SER C CA  1 
ATOM   9639  C C   . SER C 1 140 ? 105.001 35.497  -39.708 1.00 104.14 ? 140 SER C C   1 
ATOM   9640  O O   . SER C 1 140 ? 106.222 35.400  -39.840 1.00 106.16 ? 140 SER C O   1 
ATOM   9641  C CB  . SER C 1 140 ? 103.720 37.261  -40.866 1.00 103.69 ? 140 SER C CB  1 
ATOM   9642  O OG  . SER C 1 140 ? 103.878 37.859  -42.143 1.00 104.50 ? 140 SER C OG  1 
ATOM   9643  N N   . VAL C 1 141 ? 104.373 35.332  -38.540 1.00 103.36 ? 141 VAL C N   1 
ATOM   9644  C CA  . VAL C 1 141 ? 105.105 35.103  -37.300 1.00 104.93 ? 141 VAL C CA  1 
ATOM   9645  C C   . VAL C 1 141 ? 105.297 33.604  -37.012 1.00 103.72 ? 141 VAL C C   1 
ATOM   9646  O O   . VAL C 1 141 ? 105.969 33.256  -36.040 1.00 104.50 ? 141 VAL C O   1 
ATOM   9647  C CB  . VAL C 1 141 ? 104.372 35.825  -36.150 1.00 105.45 ? 141 VAL C CB  1 
ATOM   9648  C CG1 . VAL C 1 141 ? 104.168 37.311  -36.451 1.00 106.43 ? 141 VAL C CG1 1 
ATOM   9649  C CG2 . VAL C 1 141 ? 103.046 35.147  -35.795 1.00 102.96 ? 141 VAL C CG2 1 
ATOM   9650  N N   . THR C 1 142 ? 104.680 32.736  -37.844 1.00 101.29 ? 142 THR C N   1 
ATOM   9651  C CA  . THR C 1 142 ? 104.772 31.273  -37.823 1.00 99.33  ? 142 THR C CA  1 
ATOM   9652  C C   . THR C 1 142 ? 103.705 30.699  -36.900 1.00 97.76  ? 142 THR C C   1 
ATOM   9653  O O   . THR C 1 142 ? 103.402 31.277  -35.858 1.00 98.45  ? 142 THR C O   1 
ATOM   9654  C CB  . THR C 1 142 ? 106.117 30.709  -37.384 1.00 100.78 ? 142 THR C CB  1 
ATOM   9655  O OG1 . THR C 1 142 ? 105.995 30.776  -35.965 1.00 101.20 ? 142 THR C OG1 1 
ATOM   9656  C CG2 . THR C 1 142 ? 107.304 31.394  -38.039 1.00 102.73 ? 142 THR C CG2 1 
ATOM   9657  N N   . GLY C 1 143 ? 103.198 29.519  -37.289 1.00 95.80  ? 143 GLY C N   1 
ATOM   9658  C CA  . GLY C 1 143 ? 102.285 28.724  -36.480 1.00 93.74  ? 143 GLY C CA  1 
ATOM   9659  C C   . GLY C 1 143 ? 102.972 28.184  -35.227 1.00 94.71  ? 143 GLY C C   1 
ATOM   9660  O O   . GLY C 1 143 ? 102.322 27.991  -34.205 1.00 94.08  ? 143 GLY C O   1 
ATOM   9661  N N   . LYS C 1 144 ? 104.296 27.975  -35.302 1.00 95.86  ? 144 LYS C N   1 
ATOM   9662  C CA  . LYS C 1 144 ? 105.041 27.534  -34.138 1.00 97.15  ? 144 LYS C CA  1 
ATOM   9663  C C   . LYS C 1 144 ? 104.842 28.515  -32.986 1.00 98.14  ? 144 LYS C C   1 
ATOM   9664  O O   . LYS C 1 144 ? 104.499 28.105  -31.872 1.00 98.29  ? 144 LYS C O   1 
ATOM   9665  C CB  . LYS C 1 144 ? 106.542 27.436  -34.402 1.00 99.03  ? 144 LYS C CB  1 
ATOM   9666  C CG  . LYS C 1 144 ? 107.272 27.093  -33.130 1.00 101.00 ? 144 LYS C CG  1 
ATOM   9667  C CD  . LYS C 1 144 ? 108.679 26.544  -33.297 1.00 102.86 ? 144 LYS C CD  1 
ATOM   9668  C CE  . LYS C 1 144 ? 109.253 26.295  -31.938 1.00 104.99 ? 144 LYS C CE  1 
ATOM   9669  N NZ  . LYS C 1 144 ? 108.285 25.611  -31.063 1.00 104.08 ? 144 LYS C NZ  1 
ATOM   9670  N N   . ALA C 1 145 ? 105.087 29.800  -33.287 1.00 98.74  ? 145 ALA C N   1 
ATOM   9671  C CA  . ALA C 1 145 ? 105.011 30.886  -32.323 1.00 100.11 ? 145 ALA C CA  1 
ATOM   9672  C C   . ALA C 1 145 ? 103.624 30.954  -31.676 1.00 98.87  ? 145 ALA C C   1 
ATOM   9673  O O   . ALA C 1 145 ? 103.511 31.185  -30.474 1.00 99.94  ? 145 ALA C O   1 
ATOM   9674  C CB  . ALA C 1 145 ? 105.370 32.182  -33.015 1.00 100.82 ? 145 ALA C CB  1 
ATOM   9675  N N   . PHE C 1 146 ? 102.571 30.744  -32.478 1.00 96.59  ? 146 PHE C N   1 
ATOM   9676  C CA  . PHE C 1 146 ? 101.198 30.873  -32.003 1.00 95.72  ? 146 PHE C CA  1 
ATOM   9677  C C   . PHE C 1 146 ? 100.890 29.782  -30.975 1.00 95.64  ? 146 PHE C C   1 
ATOM   9678  O O   . PHE C 1 146 ? 100.277 30.056  -29.940 1.00 96.52  ? 146 PHE C O   1 
ATOM   9679  C CB  . PHE C 1 146 ? 100.202 30.838  -33.173 1.00 93.34  ? 146 PHE C CB  1 
ATOM   9680  C CG  . PHE C 1 146 ? 98.720  30.881  -32.820 1.00 91.85  ? 146 PHE C CG  1 
ATOM   9681  C CD1 . PHE C 1 146 ? 98.094  29.808  -32.197 1.00 90.98  ? 146 PHE C CD1 1 
ATOM   9682  C CD2 . PHE C 1 146 ? 97.934  31.967  -33.189 1.00 91.77  ? 146 PHE C CD2 1 
ATOM   9683  C CE1 . PHE C 1 146 ? 96.735  29.851  -31.903 1.00 89.94  ? 146 PHE C CE1 1 
ATOM   9684  C CE2 . PHE C 1 146 ? 96.571  32.002  -32.907 1.00 90.33  ? 146 PHE C CE2 1 
ATOM   9685  C CZ  . PHE C 1 146 ? 95.975  30.946  -32.256 1.00 89.51  ? 146 PHE C CZ  1 
ATOM   9686  N N   . VAL C 1 147 ? 101.296 28.543  -31.279 1.00 94.77  ? 147 VAL C N   1 
ATOM   9687  C CA  . VAL C 1 147 ? 100.845 27.390  -30.519 1.00 94.16  ? 147 VAL C CA  1 
ATOM   9688  C C   . VAL C 1 147 ? 101.593 27.324  -29.185 1.00 96.86  ? 147 VAL C C   1 
ATOM   9689  O O   . VAL C 1 147 ? 101.091 26.763  -28.216 1.00 96.96  ? 147 VAL C O   1 
ATOM   9690  C CB  . VAL C 1 147 ? 100.991 26.090  -31.335 1.00 92.48  ? 147 VAL C CB  1 
ATOM   9691  C CG1 . VAL C 1 147 ? 100.539 24.877  -30.537 1.00 92.33  ? 147 VAL C CG1 1 
ATOM   9692  C CG2 . VAL C 1 147 ? 100.230 26.146  -32.654 1.00 90.07  ? 147 VAL C CG2 1 
ATOM   9693  N N   . ASP C 1 148 ? 102.799 27.898  -29.126 1.00 99.43  ? 148 ASP C N   1 
ATOM   9694  C CA  . ASP C 1 148 ? 103.566 27.897  -27.887 1.00 102.49 ? 148 ASP C CA  1 
ATOM   9695  C C   . ASP C 1 148 ? 103.044 28.975  -26.937 1.00 104.58 ? 148 ASP C C   1 
ATOM   9696  O O   . ASP C 1 148 ? 103.042 28.773  -25.718 1.00 106.64 ? 148 ASP C O   1 
ATOM   9697  C CB  . ASP C 1 148 ? 105.051 27.919  -28.185 1.00 103.80 ? 148 ASP C CB  1 
ATOM   9698  C CG  . ASP C 1 148 ? 105.485 26.699  -28.971 1.00 102.66 ? 148 ASP C CG  1 
ATOM   9699  O OD1 . ASP C 1 148 ? 104.895 25.631  -28.721 1.00 101.08 ? 148 ASP C OD1 1 
ATOM   9700  O OD2 . ASP C 1 148 ? 106.383 26.836  -29.830 1.00 103.34 ? 148 ASP C OD2 1 
ATOM   9701  N N   . LEU C 1 149 ? 102.590 30.107  -27.504 1.00 104.31 ? 149 LEU C N   1 
ATOM   9702  C CA  . LEU C 1 149 ? 101.924 31.155  -26.741 1.00 105.03 ? 149 LEU C CA  1 
ATOM   9703  C C   . LEU C 1 149 ? 100.655 30.589  -26.110 1.00 103.90 ? 149 LEU C C   1 
ATOM   9704  O O   . LEU C 1 149 ? 100.394 30.790  -24.926 1.00 105.28 ? 149 LEU C O   1 
ATOM   9705  C CB  . LEU C 1 149 ? 101.611 32.360  -27.630 1.00 103.99 ? 149 LEU C CB  1 
ATOM   9706  C CG  . LEU C 1 149 ? 100.861 33.520  -26.969 1.00 104.65 ? 149 LEU C CG  1 
ATOM   9707  C CD1 . LEU C 1 149 ? 101.479 34.007  -25.670 1.00 107.80 ? 149 LEU C CD1 1 
ATOM   9708  C CD2 . LEU C 1 149 ? 100.801 34.641  -27.971 1.00 104.27 ? 149 LEU C CD2 1 
ATOM   9709  N N   . MET C 1 150 ? 99.886  29.859  -26.916 1.00 101.52 ? 150 MET C N   1 
ATOM   9710  C CA  . MET C 1 150 ? 98.642  29.282  -26.446 1.00 100.94 ? 150 MET C CA  1 
ATOM   9711  C C   . MET C 1 150 ? 98.941  28.280  -25.331 1.00 103.17 ? 150 MET C C   1 
ATOM   9712  O O   . MET C 1 150 ? 98.293  28.303  -24.288 1.00 104.01 ? 150 MET C O   1 
ATOM   9713  C CB  . MET C 1 150 ? 97.889  28.635  -27.612 1.00 97.86  ? 150 MET C CB  1 
ATOM   9714  C CG  . MET C 1 150 ? 97.547  29.598  -28.737 1.00 96.50  ? 150 MET C CG  1 
ATOM   9715  S SD  . MET C 1 150 ? 96.353  30.861  -28.262 1.00 96.70  ? 150 MET C SD  1 
ATOM   9716  C CE  . MET C 1 150 ? 96.971  32.256  -29.207 1.00 97.74  ? 150 MET C CE  1 
ATOM   9717  N N   . ASN C 1 151 ? 99.952  27.429  -25.546 1.00 104.91 ? 151 ASN C N   1 
ATOM   9718  C CA  . ASN C 1 151 ? 100.340 26.420  -24.567 1.00 107.41 ? 151 ASN C CA  1 
ATOM   9719  C C   . ASN C 1 151 ? 100.840 27.085  -23.282 1.00 110.10 ? 151 ASN C C   1 
ATOM   9720  O O   . ASN C 1 151 ? 100.448 26.679  -22.185 1.00 111.32 ? 151 ASN C O   1 
ATOM   9721  C CB  . ASN C 1 151 ? 101.380 25.438  -25.113 1.00 108.16 ? 151 ASN C CB  1 
ATOM   9722  C CG  . ASN C 1 151 ? 100.784 24.412  -26.056 1.00 106.22 ? 151 ASN C CG  1 
ATOM   9723  O OD1 . ASN C 1 151 ? 99.727  23.826  -25.774 1.00 105.91 ? 151 ASN C OD1 1 
ATOM   9724  N ND2 . ASN C 1 151 ? 101.429 24.195  -27.193 1.00 105.17 ? 151 ASN C ND2 1 
ATOM   9725  N N   . THR C 1 152 ? 101.708 28.097  -23.422 1.00 110.75 ? 152 THR C N   1 
ATOM   9726  C CA  . THR C 1 152 ? 102.181 28.847  -22.270 1.00 113.49 ? 152 THR C CA  1 
ATOM   9727  C C   . THR C 1 152 ? 100.969 29.427  -21.525 1.00 113.32 ? 152 THR C C   1 
ATOM   9728  O O   . THR C 1 152 ? 100.811 29.184  -20.330 1.00 114.96 ? 152 THR C O   1 
ATOM   9729  C CB  . THR C 1 152 ? 103.196 29.901  -22.724 1.00 115.03 ? 152 THR C CB  1 
ATOM   9730  O OG1 . THR C 1 152 ? 104.300 29.267  -23.370 1.00 114.92 ? 152 THR C OG1 1 
ATOM   9731  C CG2 . THR C 1 152 ? 103.803 30.675  -21.569 1.00 118.54 ? 152 THR C CG2 1 
ATOM   9732  N N   . LEU C 1 153 ? 100.076 30.128  -22.244 1.00 111.07 ? 153 LEU C N   1 
ATOM   9733  C CA  . LEU C 1 153 ? 98.925  30.794  -21.637 1.00 111.34 ? 153 LEU C CA  1 
ATOM   9734  C C   . LEU C 1 153 ? 97.962  29.782  -21.004 1.00 110.73 ? 153 LEU C C   1 
ATOM   9735  O O   . LEU C 1 153 ? 97.548  29.955  -19.856 1.00 113.07 ? 153 LEU C O   1 
ATOM   9736  C CB  . LEU C 1 153 ? 98.165  31.675  -22.636 1.00 109.11 ? 153 LEU C CB  1 
ATOM   9737  C CG  . LEU C 1 153 ? 98.816  32.995  -23.063 1.00 109.97 ? 153 LEU C CG  1 
ATOM   9738  C CD1 . LEU C 1 153 ? 98.012  33.627  -24.184 1.00 107.47 ? 153 LEU C CD1 1 
ATOM   9739  C CD2 . LEU C 1 153 ? 98.960  33.973  -21.913 1.00 113.18 ? 153 LEU C CD2 1 
ATOM   9740  N N   . ILE C 1 154 ? 97.555  28.755  -21.759 1.00 107.60 ? 154 ILE C N   1 
ATOM   9741  C CA  . ILE C 1 154 ? 96.651  27.755  -21.217 1.00 106.54 ? 154 ILE C CA  1 
ATOM   9742  C C   . ILE C 1 154 ? 97.216  27.238  -19.896 1.00 109.21 ? 154 ILE C C   1 
ATOM   9743  O O   . ILE C 1 154 ? 96.566  27.356  -18.860 1.00 110.63 ? 154 ILE C O   1 
ATOM   9744  C CB  . ILE C 1 154 ? 96.410  26.609  -22.211 1.00 103.73 ? 154 ILE C CB  1 
ATOM   9745  C CG1 . ILE C 1 154 ? 95.681  27.094  -23.452 1.00 100.98 ? 154 ILE C CG1 1 
ATOM   9746  C CG2 . ILE C 1 154 ? 95.655  25.457  -21.543 1.00 103.64 ? 154 ILE C CG2 1 
ATOM   9747  C CD1 . ILE C 1 154 ? 95.882  26.194  -24.654 1.00 98.90  ? 154 ILE C CD1 1 
ATOM   9748  N N   . ASN C 1 155 ? 98.440  26.697  -19.936 1.00 110.06 ? 155 ASN C N   1 
ATOM   9749  C CA  . ASN C 1 155 ? 98.993  25.991  -18.789 1.00 112.63 ? 155 ASN C CA  1 
ATOM   9750  C C   . ASN C 1 155 ? 99.052  26.916  -17.572 1.00 115.33 ? 155 ASN C C   1 
ATOM   9751  O O   . ASN C 1 155 ? 98.792  26.482  -16.450 1.00 116.88 ? 155 ASN C O   1 
ATOM   9752  C CB  . ASN C 1 155 ? 100.332 25.326  -19.107 1.00 113.46 ? 155 ASN C CB  1 
ATOM   9753  C CG  . ASN C 1 155 ? 100.198 24.084  -19.969 1.00 111.28 ? 155 ASN C CG  1 
ATOM   9754  O OD1 . ASN C 1 155 ? 99.329  23.225  -19.741 1.00 110.13 ? 155 ASN C OD1 1 
ATOM   9755  N ND2 . ASN C 1 155 ? 101.062 23.964  -20.968 1.00 110.61 ? 155 ASN C ND2 1 
ATOM   9756  N N   . ILE C 1 156 ? 99.364  28.197  -17.792 1.00 115.95 ? 156 ILE C N   1 
ATOM   9757  C CA  . ILE C 1 156 ? 99.434  29.148  -16.693 1.00 119.20 ? 156 ILE C CA  1 
ATOM   9758  C C   . ILE C 1 156 ? 98.076  29.258  -16.004 1.00 119.06 ? 156 ILE C C   1 
ATOM   9759  O O   . ILE C 1 156 ? 98.031  29.489  -14.797 1.00 122.05 ? 156 ILE C O   1 
ATOM   9760  C CB  . ILE C 1 156 ? 99.963  30.513  -17.171 1.00 120.01 ? 156 ILE C CB  1 
ATOM   9761  C CG1 . ILE C 1 156 ? 101.457 30.412  -17.507 1.00 121.17 ? 156 ILE C CG1 1 
ATOM   9762  C CG2 . ILE C 1 156 ? 99.697  31.613  -16.138 1.00 122.81 ? 156 ILE C CG2 1 
ATOM   9763  C CD1 . ILE C 1 156 ? 101.975 31.536  -18.386 1.00 121.00 ? 156 ILE C CD1 1 
ATOM   9764  N N   . ILE C 1 157 ? 96.989  29.092  -16.772 1.00 115.81 ? 157 ILE C N   1 
ATOM   9765  C CA  . ILE C 1 157 ? 95.643  29.246  -16.245 1.00 115.48 ? 157 ILE C CA  1 
ATOM   9766  C C   . ILE C 1 157 ? 95.244  27.996  -15.462 1.00 116.18 ? 157 ILE C C   1 
ATOM   9767  O O   . ILE C 1 157 ? 94.610  28.127  -14.419 1.00 118.13 ? 157 ILE C O   1 
ATOM   9768  C CB  . ILE C 1 157 ? 94.647  29.602  -17.366 1.00 112.05 ? 157 ILE C CB  1 
ATOM   9769  C CG1 . ILE C 1 157 ? 94.911  31.024  -17.910 1.00 111.96 ? 157 ILE C CG1 1 
ATOM   9770  C CG2 . ILE C 1 157 ? 93.203  29.433  -16.887 1.00 111.53 ? 157 ILE C CG2 1 
ATOM   9771  C CD1 . ILE C 1 157 ? 94.298  31.309  -19.272 1.00 108.65 ? 157 ILE C CD1 1 
ATOM   9772  N N   . HIS C 1 158 ? 95.631  26.804  -15.951 1.00 115.04 ? 158 HIS C N   1 
ATOM   9773  C CA  . HIS C 1 158 ? 95.312  25.542  -15.287 1.00 115.81 ? 158 HIS C CA  1 
ATOM   9774  C C   . HIS C 1 158 ? 95.941  25.488  -13.892 1.00 119.89 ? 158 HIS C C   1 
ATOM   9775  O O   . HIS C 1 158 ? 95.331  24.978  -12.958 1.00 121.20 ? 158 HIS C O   1 
ATOM   9776  C CB  . HIS C 1 158 ? 95.742  24.318  -16.110 1.00 113.87 ? 158 HIS C CB  1 
ATOM   9777  C CG  . HIS C 1 158 ? 94.942  24.015  -17.339 1.00 110.43 ? 158 HIS C CG  1 
ATOM   9778  N ND1 . HIS C 1 158 ? 95.462  23.249  -18.361 1.00 108.63 ? 158 HIS C ND1 1 
ATOM   9779  C CD2 . HIS C 1 158 ? 93.701  24.324  -17.717 1.00 108.81 ? 158 HIS C CD2 1 
ATOM   9780  C CE1 . HIS C 1 158 ? 94.568  23.120  -19.325 1.00 105.84 ? 158 HIS C CE1 1 
ATOM   9781  N NE2 . HIS C 1 158 ? 93.491  23.765  -18.954 1.00 106.00 ? 158 HIS C NE2 1 
ATOM   9782  N N   . LYS C 1 159 ? 97.171  25.999  -13.754 1.00 122.37 ? 159 LYS C N   1 
ATOM   9783  C CA  . LYS C 1 159 ? 97.850  26.033  -12.466 1.00 126.64 ? 159 LYS C CA  1 
ATOM   9784  C C   . LYS C 1 159 ? 97.352  27.200  -11.615 1.00 129.50 ? 159 LYS C C   1 
ATOM   9785  O O   . LYS C 1 159 ? 97.404  27.126  -10.388 1.00 132.83 ? 159 LYS C O   1 
ATOM   9786  C CB  . LYS C 1 159 ? 99.369  26.178  -12.605 1.00 128.02 ? 159 LYS C CB  1 
ATOM   9787  C CG  . LYS C 1 159 ? 99.913  27.515  -13.136 1.00 128.16 ? 159 LYS C CG  1 
ATOM   9788  C CD  . LYS C 1 159 ? 99.928  28.707  -12.175 1.00 131.24 ? 159 LYS C CD  1 
ATOM   9789  C CE  . LYS C 1 159 ? 100.669 29.913  -12.673 1.00 131.71 ? 159 LYS C CE  1 
ATOM   9790  N NZ  . LYS C 1 159 ? 102.111 29.791  -12.443 1.00 134.02 ? 159 LYS C NZ  1 
ATOM   9791  N N   . GLY C 1 160 ? 96.918  28.287  -12.278 1.00 128.36 ? 160 GLY C N   1 
ATOM   9792  C CA  . GLY C 1 160 ? 96.633  29.551  -11.618 1.00 130.53 ? 160 GLY C CA  1 
ATOM   9793  C C   . GLY C 1 160 ? 95.201  29.600  -11.100 1.00 130.57 ? 160 GLY C C   1 
ATOM   9794  O O   . GLY C 1 160 ? 94.978  29.890  -9.927  1.00 134.18 ? 160 GLY C O   1 
ATOM   9795  N N   . HIS C 1 161 ? 94.243  29.336  -11.996 1.00 126.83 ? 161 HIS C N   1 
ATOM   9796  C CA  . HIS C 1 161 ? 92.853  29.159  -11.612 1.00 126.13 ? 161 HIS C CA  1 
ATOM   9797  C C   . HIS C 1 161 ? 92.487  27.706  -11.920 1.00 124.30 ? 161 HIS C C   1 
ATOM   9798  O O   . HIS C 1 161 ? 92.121  27.371  -13.051 1.00 121.01 ? 161 HIS C O   1 
ATOM   9799  C CB  . HIS C 1 161 ? 91.967  30.214  -12.288 1.00 124.09 ? 161 HIS C CB  1 
ATOM   9800  C CG  . HIS C 1 161 ? 90.655  30.439  -11.605 1.00 124.69 ? 161 HIS C CG  1 
ATOM   9801  N ND1 . HIS C 1 161 ? 89.737  31.363  -12.057 1.00 123.16 ? 161 HIS C ND1 1 
ATOM   9802  C CD2 . HIS C 1 161 ? 90.095  29.849  -10.537 1.00 126.38 ? 161 HIS C CD2 1 
ATOM   9803  C CE1 . HIS C 1 161 ? 88.678  31.340  -11.267 1.00 124.27 ? 161 HIS C CE1 1 
ATOM   9804  N NE2 . HIS C 1 161 ? 88.875  30.431  -10.337 1.00 126.20 ? 161 HIS C NE2 1 
ATOM   9805  N N   . PRO C 1 162 ? 92.624  26.785  -10.933 1.00 126.44 ? 162 PRO C N   1 
ATOM   9806  C CA  . PRO C 1 162 ? 92.434  25.354  -11.179 1.00 124.76 ? 162 PRO C CA  1 
ATOM   9807  C C   . PRO C 1 162 ? 90.974  24.980  -11.407 1.00 122.76 ? 162 PRO C C   1 
ATOM   9808  O O   . PRO C 1 162 ? 90.103  25.400  -10.648 1.00 124.24 ? 162 PRO C O   1 
ATOM   9809  C CB  . PRO C 1 162 ? 93.018  24.710  -9.904  1.00 128.40 ? 162 PRO C CB  1 
ATOM   9810  C CG  . PRO C 1 162 ? 92.780  25.744  -8.829  1.00 131.61 ? 162 PRO C CG  1 
ATOM   9811  C CD  . PRO C 1 162 ? 92.982  27.075  -9.533  1.00 130.59 ? 162 PRO C CD  1 
ATOM   9812  N N   . GLY C 1 163 ? 90.734  24.212  -12.476 1.00 119.61 ? 163 GLY C N   1 
ATOM   9813  C CA  . GLY C 1 163 ? 89.442  23.598  -12.731 1.00 117.93 ? 163 GLY C CA  1 
ATOM   9814  C C   . GLY C 1 163 ? 88.606  24.396  -13.729 1.00 115.37 ? 163 GLY C C   1 
ATOM   9815  O O   . GLY C 1 163 ? 87.433  24.073  -13.952 1.00 114.12 ? 163 GLY C O   1 
ATOM   9816  N N   . ILE C 1 164 ? 89.206  25.444  -14.308 1.00 114.73 ? 164 ILE C N   1 
ATOM   9817  C CA  . ILE C 1 164 ? 88.489  26.305  -15.235 1.00 112.56 ? 164 ILE C CA  1 
ATOM   9818  C C   . ILE C 1 164 ? 88.904  25.916  -16.653 1.00 109.49 ? 164 ILE C C   1 
ATOM   9819  O O   . ILE C 1 164 ? 90.088  25.743  -16.942 1.00 109.76 ? 164 ILE C O   1 
ATOM   9820  C CB  . ILE C 1 164 ? 88.700  27.809  -14.941 1.00 114.03 ? 164 ILE C CB  1 
ATOM   9821  C CG1 . ILE C 1 164 ? 88.136  28.236  -13.572 1.00 117.19 ? 164 ILE C CG1 1 
ATOM   9822  C CG2 . ILE C 1 164 ? 88.084  28.664  -16.049 1.00 111.39 ? 164 ILE C CG2 1 
ATOM   9823  C CD1 . ILE C 1 164 ? 88.776  27.577  -12.363 1.00 120.25 ? 164 ILE C CD1 1 
ATOM   9824  N N   . PRO C 1 165 ? 87.924  25.710  -17.562 1.00 106.72 ? 165 PRO C N   1 
ATOM   9825  C CA  . PRO C 1 165 ? 88.205  25.605  -18.993 1.00 103.88 ? 165 PRO C CA  1 
ATOM   9826  C C   . PRO C 1 165 ? 88.922  26.817  -19.584 1.00 103.85 ? 165 PRO C C   1 
ATOM   9827  O O   . PRO C 1 165 ? 88.679  27.956  -19.187 1.00 105.13 ? 165 PRO C O   1 
ATOM   9828  C CB  . PRO C 1 165 ? 86.819  25.427  -19.617 1.00 101.43 ? 165 PRO C CB  1 
ATOM   9829  C CG  . PRO C 1 165 ? 85.994  24.825  -18.511 1.00 103.22 ? 165 PRO C CG  1 
ATOM   9830  C CD  . PRO C 1 165 ? 86.508  25.482  -17.247 1.00 106.42 ? 165 PRO C CD  1 
ATOM   9831  N N   . VAL C 1 166 ? 89.801  26.539  -20.550 1.00 102.31 ? 166 VAL C N   1 
ATOM   9832  C CA  . VAL C 1 166 ? 90.389  27.558  -21.393 1.00 101.46 ? 166 VAL C CA  1 
ATOM   9833  C C   . VAL C 1 166 ? 90.052  27.225  -22.843 1.00 98.20  ? 166 VAL C C   1 
ATOM   9834  O O   . VAL C 1 166 ? 90.050  26.059  -23.233 1.00 97.11  ? 166 VAL C O   1 
ATOM   9835  C CB  . VAL C 1 166 ? 91.912  27.610  -21.179 1.00 103.36 ? 166 VAL C CB  1 
ATOM   9836  C CG1 . VAL C 1 166 ? 92.544  28.778  -21.929 1.00 103.13 ? 166 VAL C CG1 1 
ATOM   9837  C CG2 . VAL C 1 166 ? 92.279  27.649  -19.698 1.00 106.66 ? 166 VAL C CG2 1 
ATOM   9838  N N   . THR C 1 167 ? 89.782  28.263  -23.634 1.00 96.81  ? 167 THR C N   1 
ATOM   9839  C CA  . THR C 1 167 ? 89.704  28.130  -25.078 1.00 93.97  ? 167 THR C CA  1 
ATOM   9840  C C   . THR C 1 167 ? 90.032  29.493  -25.685 1.00 93.56  ? 167 THR C C   1 
ATOM   9841  O O   . THR C 1 167 ? 90.659  30.311  -25.020 1.00 95.46  ? 167 THR C O   1 
ATOM   9842  C CB  . THR C 1 167 ? 88.328  27.590  -25.461 1.00 92.09  ? 167 THR C CB  1 
ATOM   9843  O OG1 . THR C 1 167 ? 88.331  27.528  -26.882 1.00 90.04  ? 167 THR C OG1 1 
ATOM   9844  C CG2 . THR C 1 167 ? 87.199  28.480  -24.987 1.00 92.77  ? 167 THR C CG2 1 
ATOM   9845  N N   . LEU C 1 168 ? 89.636  29.718  -26.943 1.00 91.10  ? 168 LEU C N   1 
ATOM   9846  C CA  . LEU C 1 168 ? 89.908  30.972  -27.624 1.00 91.05  ? 168 LEU C CA  1 
ATOM   9847  C C   . LEU C 1 168 ? 88.700  31.336  -28.468 1.00 89.02  ? 168 LEU C C   1 
ATOM   9848  O O   . LEU C 1 168 ? 87.805  30.524  -28.655 1.00 87.21  ? 168 LEU C O   1 
ATOM   9849  C CB  . LEU C 1 168 ? 91.160  30.917  -28.498 1.00 90.93  ? 168 LEU C CB  1 
ATOM   9850  C CG  . LEU C 1 168 ? 90.978  30.379  -29.920 1.00 88.66  ? 168 LEU C CG  1 
ATOM   9851  C CD1 . LEU C 1 168 ? 92.246  30.489  -30.716 1.00 89.08  ? 168 LEU C CD1 1 
ATOM   9852  C CD2 . LEU C 1 168 ? 90.539  28.936  -29.892 1.00 87.67  ? 168 LEU C CD2 1 
ATOM   9853  N N   . SER C 1 169 ? 88.730  32.552  -29.015 1.00 89.51  ? 169 SER C N   1 
ATOM   9854  C CA  . SER C 1 169 ? 87.606  33.098  -29.753 1.00 88.29  ? 169 SER C CA  1 
ATOM   9855  C C   . SER C 1 169 ? 87.898  33.051  -31.252 1.00 86.63  ? 169 SER C C   1 
ATOM   9856  O O   . SER C 1 169 ? 87.891  34.084  -31.921 1.00 87.22  ? 169 SER C O   1 
ATOM   9857  C CB  . SER C 1 169 ? 87.316  34.524  -29.316 1.00 90.10  ? 169 SER C CB  1 
ATOM   9858  O OG  . SER C 1 169 ? 87.376  34.708  -27.907 1.00 92.21  ? 169 SER C OG  1 
ATOM   9859  N N   . ALA C 1 170 ? 88.176  31.861  -31.788 1.00 84.98  ? 170 ALA C N   1 
ATOM   9860  C CA  . ALA C 1 170 ? 88.633  31.788  -33.165 1.00 83.75  ? 170 ALA C CA  1 
ATOM   9861  C C   . ALA C 1 170 ? 87.440  32.040  -34.070 1.00 81.98  ? 170 ALA C C   1 
ATOM   9862  O O   . ALA C 1 170 ? 86.318  31.798  -33.660 1.00 81.71  ? 170 ALA C O   1 
ATOM   9863  C CB  . ALA C 1 170 ? 89.300  30.468  -33.444 1.00 82.99  ? 170 ALA C CB  1 
ATOM   9864  N N   . ASN C 1 171 ? 87.687  32.576  -35.263 1.00 81.88  ? 171 ASN C N   1 
ATOM   9865  C CA  . ASN C 1 171 ? 86.619  32.947  -36.173 1.00 81.19  ? 171 ASN C CA  1 
ATOM   9866  C C   . ASN C 1 171 ? 86.416  31.822  -37.179 1.00 79.36  ? 171 ASN C C   1 
ATOM   9867  O O   . ASN C 1 171 ? 87.354  31.395  -37.837 1.00 78.65  ? 171 ASN C O   1 
ATOM   9868  C CB  . ASN C 1 171 ? 86.896  34.287  -36.845 1.00 82.51  ? 171 ASN C CB  1 
ATOM   9869  C CG  . ASN C 1 171 ? 85.897  34.594  -37.940 1.00 81.67  ? 171 ASN C CG  1 
ATOM   9870  O OD1 . ASN C 1 171 ? 85.853  33.907  -38.967 1.00 80.61  ? 171 ASN C OD1 1 
ATOM   9871  N ND2 . ASN C 1 171 ? 85.096  35.630  -37.756 1.00 82.38  ? 171 ASN C ND2 1 
ATOM   9872  N N   . ALA C 1 172 ? 85.170  31.365  -37.327 1.00 78.51  ? 172 ALA C N   1 
ATOM   9873  C CA  . ALA C 1 172 ? 84.935  30.137  -38.073 1.00 77.39  ? 172 ALA C CA  1 
ATOM   9874  C C   . ALA C 1 172 ? 85.186  30.355  -39.560 1.00 77.39  ? 172 ALA C C   1 
ATOM   9875  O O   . ALA C 1 172 ? 85.531  29.420  -40.269 1.00 79.28  ? 172 ALA C O   1 
ATOM   9876  C CB  . ALA C 1 172 ? 83.552  29.588  -37.840 1.00 75.69  ? 172 ALA C CB  1 
ATOM   9877  N N   . MET C 1 173 ? 85.030  31.581  -40.041 1.00 77.13  ? 173 MET C N   1 
ATOM   9878  C CA  . MET C 1 173 ? 85.135  31.799  -41.469 1.00 76.27  ? 173 MET C CA  1 
ATOM   9879  C C   . MET C 1 173 ? 86.595  31.816  -41.913 1.00 77.44  ? 173 MET C C   1 
ATOM   9880  O O   . MET C 1 173 ? 86.832  31.753  -43.117 1.00 77.37  ? 173 MET C O   1 
ATOM   9881  C CB  . MET C 1 173 ? 84.449  33.110  -41.850 1.00 76.38  ? 173 MET C CB  1 
ATOM   9882  C CG  . MET C 1 173 ? 82.943  33.037  -41.799 1.00 74.71  ? 173 MET C CG  1 
ATOM   9883  S SD  . MET C 1 173 ? 82.368  31.988  -43.147 1.00 73.12  ? 173 MET C SD  1 
ATOM   9884  C CE  . MET C 1 173 ? 82.863  32.819  -44.666 1.00 73.23  ? 173 MET C CE  1 
ATOM   9885  N N   . ILE C 1 174 ? 87.545  31.914  -40.958 1.00 78.76  ? 174 ILE C N   1 
ATOM   9886  C CA  . ILE C 1 174 ? 88.961  32.147  -41.264 1.00 80.17  ? 174 ILE C CA  1 
ATOM   9887  C C   . ILE C 1 174 ? 89.894  31.200  -40.506 1.00 80.89  ? 174 ILE C C   1 
ATOM   9888  O O   . ILE C 1 174 ? 91.013  30.975  -40.956 1.00 80.96  ? 174 ILE C O   1 
ATOM   9889  C CB  . ILE C 1 174 ? 89.392  33.595  -40.967 1.00 81.55  ? 174 ILE C CB  1 
ATOM   9890  C CG1 . ILE C 1 174 ? 89.280  33.915  -39.466 1.00 82.26  ? 174 ILE C CG1 1 
ATOM   9891  C CG2 . ILE C 1 174 ? 88.622  34.579  -41.851 1.00 81.62  ? 174 ILE C CG2 1 
ATOM   9892  C CD1 . ILE C 1 174 ? 90.127  35.085  -39.009 1.00 84.31  ? 174 ILE C CD1 1 
ATOM   9893  N N   . SER C 1 175 ? 89.463  30.716  -39.332 1.00 81.70  ? 175 SER C N   1 
ATOM   9894  C CA  . SER C 1 175 ? 90.221  29.766  -38.527 1.00 82.20  ? 175 SER C CA  1 
ATOM   9895  C C   . SER C 1 175 ? 89.533  28.389  -38.557 1.00 80.54  ? 175 SER C C   1 
ATOM   9896  O O   . SER C 1 175 ? 89.488  27.665  -37.561 1.00 81.34  ? 175 SER C O   1 
ATOM   9897  C CB  . SER C 1 175 ? 90.409  30.302  -37.102 1.00 83.63  ? 175 SER C CB  1 
ATOM   9898  O OG  . SER C 1 175 ? 90.589  31.719  -37.065 1.00 85.10  ? 175 SER C OG  1 
ATOM   9899  N N   . ASP C 1 176 ? 89.006  28.006  -39.723 1.00 78.50  ? 176 ASP C N   1 
ATOM   9900  C CA  . ASP C 1 176 ? 88.434  26.681  -39.911 1.00 77.30  ? 176 ASP C CA  1 
ATOM   9901  C C   . ASP C 1 176 ? 89.535  25.621  -39.810 1.00 78.34  ? 176 ASP C C   1 
ATOM   9902  O O   . ASP C 1 176 ? 89.388  24.625  -39.097 1.00 77.79  ? 176 ASP C O   1 
ATOM   9903  C CB  . ASP C 1 176 ? 87.707  26.612  -41.244 1.00 75.63  ? 176 ASP C CB  1 
ATOM   9904  C CG  . ASP C 1 176 ? 88.443  27.279  -42.398 1.00 75.66  ? 176 ASP C CG  1 
ATOM   9905  O OD1 . ASP C 1 176 ? 89.494  27.907  -42.122 1.00 76.35  ? 176 ASP C OD1 1 
ATOM   9906  O OD2 . ASP C 1 176 ? 87.963  27.175  -43.553 1.00 74.41  ? 176 ASP C OD2 1 
ATOM   9907  N N   . TYR C 1 177 ? 90.638  25.888  -40.531 1.00 79.40  ? 177 TYR C N   1 
ATOM   9908  C CA  . TYR C 1 177 ? 91.789  25.010  -40.678 1.00 80.05  ? 177 TYR C CA  1 
ATOM   9909  C C   . TYR C 1 177 ? 92.474  24.789  -39.331 1.00 82.32  ? 177 TYR C C   1 
ATOM   9910  O O   . TYR C 1 177 ? 93.306  23.885  -39.186 1.00 83.36  ? 177 TYR C O   1 
ATOM   9911  C CB  . TYR C 1 177 ? 92.788  25.684  -41.628 1.00 80.54  ? 177 TYR C CB  1 
ATOM   9912  C CG  . TYR C 1 177 ? 93.463  26.892  -40.986 1.00 81.97  ? 177 TYR C CG  1 
ATOM   9913  C CD1 . TYR C 1 177 ? 92.837  28.138  -40.970 1.00 82.18  ? 177 TYR C CD1 1 
ATOM   9914  C CD2 . TYR C 1 177 ? 94.695  26.790  -40.345 1.00 83.05  ? 177 TYR C CD2 1 
ATOM   9915  C CE1 . TYR C 1 177 ? 93.420  29.243  -40.367 1.00 83.36  ? 177 TYR C CE1 1 
ATOM   9916  C CE2 . TYR C 1 177 ? 95.284  27.888  -39.732 1.00 84.43  ? 177 TYR C CE2 1 
ATOM   9917  C CZ  . TYR C 1 177 ? 94.644  29.115  -39.745 1.00 84.58  ? 177 TYR C CZ  1 
ATOM   9918  O OH  . TYR C 1 177 ? 95.133  30.228  -39.143 1.00 86.24  ? 177 TYR C OH  1 
ATOM   9919  N N   . MET C 1 178 ? 92.161  25.658  -38.360 1.00 83.54  ? 178 MET C N   1 
ATOM   9920  C CA  . MET C 1 178 ? 92.911  25.712  -37.113 1.00 85.60  ? 178 MET C CA  1 
ATOM   9921  C C   . MET C 1 178 ? 92.547  24.537  -36.197 1.00 85.81  ? 178 MET C C   1 
ATOM   9922  O O   . MET C 1 178 ? 91.373  24.213  -36.021 1.00 84.22  ? 178 MET C O   1 
ATOM   9923  C CB  . MET C 1 178 ? 92.655  27.047  -36.396 1.00 86.16  ? 178 MET C CB  1 
ATOM   9924  C CG  . MET C 1 178 ? 93.213  27.100  -34.979 1.00 87.98  ? 178 MET C CG  1 
ATOM   9925  S SD  . MET C 1 178 ? 93.067  28.694  -34.147 1.00 89.94  ? 178 MET C SD  1 
ATOM   9926  C CE  . MET C 1 178 ? 94.161  29.706  -35.163 1.00 91.16  ? 178 MET C CE  1 
ATOM   9927  N N   . ASP C 1 179 ? 93.577  23.941  -35.582 1.00 87.62  ? 179 ASP C N   1 
ATOM   9928  C CA  . ASP C 1 179 ? 93.421  22.907  -34.568 1.00 88.63  ? 179 ASP C CA  1 
ATOM   9929  C C   . ASP C 1 179 ? 93.048  23.533  -33.226 1.00 89.01  ? 179 ASP C C   1 
ATOM   9930  O O   . ASP C 1 179 ? 93.719  24.462  -32.805 1.00 90.96  ? 179 ASP C O   1 
ATOM   9931  C CB  . ASP C 1 179 ? 94.738  22.183  -34.370 1.00 90.65  ? 179 ASP C CB  1 
ATOM   9932  C CG  . ASP C 1 179 ? 94.838  21.314  -33.128 1.00 93.29  ? 179 ASP C CG  1 
ATOM   9933  O OD1 . ASP C 1 179 ? 94.509  21.828  -32.031 1.00 93.90  ? 179 ASP C OD1 1 
ATOM   9934  O OD2 . ASP C 1 179 ? 95.291  20.148  -33.265 1.00 95.60  ? 179 ASP C OD2 1 
ATOM   9935  N N   . GLU C 1 180 ? 92.044  22.995  -32.518 1.00 87.96  ? 180 GLU C N   1 
ATOM   9936  C CA  . GLU C 1 180 ? 91.721  23.495  -31.187 1.00 88.41  ? 180 GLU C CA  1 
ATOM   9937  C C   . GLU C 1 180 ? 91.831  22.395  -30.128 1.00 89.56  ? 180 GLU C C   1 
ATOM   9938  O O   . GLU C 1 180 ? 91.426  22.597  -28.985 1.00 90.71  ? 180 GLU C O   1 
ATOM   9939  C CB  . GLU C 1 180 ? 90.322  24.108  -31.110 1.00 87.12  ? 180 GLU C CB  1 
ATOM   9940  C CG  . GLU C 1 180 ? 90.073  25.277  -32.065 1.00 85.66  ? 180 GLU C CG  1 
ATOM   9941  C CD  . GLU C 1 180 ? 88.815  26.104  -31.806 1.00 84.39  ? 180 GLU C CD  1 
ATOM   9942  O OE1 . GLU C 1 180 ? 88.371  26.156  -30.645 1.00 85.20  ? 180 GLU C OE1 1 
ATOM   9943  O OE2 . GLU C 1 180 ? 88.271  26.690  -32.765 1.00 82.62  ? 180 GLU C OE2 1 
ATOM   9944  N N   . SER C 1 181 ? 92.426  21.255  -30.487 1.00 89.45  ? 181 SER C N   1 
ATOM   9945  C CA  . SER C 1 181 ? 92.540  20.109  -29.596 1.00 90.64  ? 181 SER C CA  1 
ATOM   9946  C C   . SER C 1 181 ? 93.375  20.391  -28.342 1.00 92.91  ? 181 SER C C   1 
ATOM   9947  O O   . SER C 1 181 ? 93.202  19.722  -27.330 1.00 94.52  ? 181 SER C O   1 
ATOM   9948  C CB  . SER C 1 181 ? 93.118  18.919  -30.328 1.00 90.34  ? 181 SER C CB  1 
ATOM   9949  O OG  . SER C 1 181 ? 94.399  19.233  -30.850 1.00 89.81  ? 181 SER C OG  1 
ATOM   9950  N N   . ILE C 1 182 ? 94.320  21.331  -28.392 1.00 93.76  ? 182 ILE C N   1 
ATOM   9951  C CA  . ILE C 1 182 ? 95.104  21.623  -27.200 1.00 96.10  ? 182 ILE C CA  1 
ATOM   9952  C C   . ILE C 1 182 ? 94.208  22.291  -26.147 1.00 96.19  ? 182 ILE C C   1 
ATOM   9953  O O   . ILE C 1 182 ? 94.481  22.221  -24.952 1.00 97.80  ? 182 ILE C O   1 
ATOM   9954  C CB  . ILE C 1 182 ? 96.361  22.450  -27.543 1.00 97.30  ? 182 ILE C CB  1 
ATOM   9955  C CG1 . ILE C 1 182 ? 96.009  23.864  -28.055 1.00 97.04  ? 182 ILE C CG1 1 
ATOM   9956  C CG2 . ILE C 1 182 ? 97.256  21.694  -28.526 1.00 96.69  ? 182 ILE C CG2 1 
ATOM   9957  C CD1 . ILE C 1 182 ? 97.218  24.760  -28.285 1.00 98.36  ? 182 ILE C CD1 1 
ATOM   9958  N N   . PHE C 1 183 ? 93.111  22.920  -26.579 1.00 94.40  ? 183 PHE C N   1 
ATOM   9959  C CA  . PHE C 1 183 ? 92.237  23.631  -25.658 1.00 94.85  ? 183 PHE C CA  1 
ATOM   9960  C C   . PHE C 1 183 ? 91.204  22.683  -25.051 1.00 93.99  ? 183 PHE C C   1 
ATOM   9961  O O   . PHE C 1 183 ? 90.909  21.640  -25.618 1.00 92.30  ? 183 PHE C O   1 
ATOM   9962  C CB  . PHE C 1 183 ? 91.512  24.786  -26.356 1.00 93.28  ? 183 PHE C CB  1 
ATOM   9963  C CG  . PHE C 1 183 ? 92.401  25.836  -27.013 1.00 92.79  ? 183 PHE C CG  1 
ATOM   9964  C CD1 . PHE C 1 183 ? 92.950  26.877  -26.273 1.00 94.54  ? 183 PHE C CD1 1 
ATOM   9965  C CD2 . PHE C 1 183 ? 92.633  25.810  -28.382 1.00 90.64  ? 183 PHE C CD2 1 
ATOM   9966  C CE1 . PHE C 1 183 ? 93.720  27.855  -26.884 1.00 94.51  ? 183 PHE C CE1 1 
ATOM   9967  C CE2 . PHE C 1 183 ? 93.392  26.793  -28.987 1.00 90.78  ? 183 PHE C CE2 1 
ATOM   9968  C CZ  . PHE C 1 183 ? 93.940  27.808  -28.236 1.00 92.76  ? 183 PHE C CZ  1 
ATOM   9969  N N   . ASP C 1 184 ? 90.635  23.102  -23.914 1.00 95.31  ? 184 ASP C N   1 
ATOM   9970  C CA  . ASP C 1 184 ? 89.692  22.302  -23.150 1.00 95.84  ? 184 ASP C CA  1 
ATOM   9971  C C   . ASP C 1 184 ? 88.339  22.237  -23.855 1.00 94.33  ? 184 ASP C C   1 
ATOM   9972  O O   . ASP C 1 184 ? 87.609  21.273  -23.655 1.00 94.08  ? 184 ASP C O   1 
ATOM   9973  C CB  . ASP C 1 184 ? 89.512  22.837  -21.737 1.00 97.67  ? 184 ASP C CB  1 
ATOM   9974  C CG  . ASP C 1 184 ? 90.791  22.987  -20.927 1.00 99.66  ? 184 ASP C CG  1 
ATOM   9975  O OD1 . ASP C 1 184 ? 91.672  22.124  -21.087 1.00 99.70  ? 184 ASP C OD1 1 
ATOM   9976  O OD2 . ASP C 1 184 ? 90.884  23.949  -20.130 1.00 100.87 ? 184 ASP C OD2 1 
ATOM   9977  N N   . VAL C 1 185 ? 88.024  23.259  -24.668 1.00 93.79  ? 185 VAL C N   1 
ATOM   9978  C CA  . VAL C 1 185 ? 86.730  23.396  -25.331 1.00 92.79  ? 185 VAL C CA  1 
ATOM   9979  C C   . VAL C 1 185 ? 86.939  23.825  -26.789 1.00 91.48  ? 185 VAL C C   1 
ATOM   9980  O O   . VAL C 1 185 ? 87.978  24.372  -27.128 1.00 93.20  ? 185 VAL C O   1 
ATOM   9981  C CB  . VAL C 1 185 ? 85.866  24.412  -24.545 1.00 93.65  ? 185 VAL C CB  1 
ATOM   9982  C CG1 . VAL C 1 185 ? 84.670  24.933  -25.335 1.00 91.77  ? 185 VAL C CG1 1 
ATOM   9983  C CG2 . VAL C 1 185 ? 85.405  23.854  -23.201 1.00 95.13  ? 185 VAL C CG2 1 
ATOM   9984  N N   . TYR C 1 186 ? 85.952  23.549  -27.651 1.00 90.07  ? 186 TYR C N   1 
ATOM   9985  C CA  . TYR C 1 186 ? 85.888  24.065  -29.013 1.00 88.57  ? 186 TYR C CA  1 
ATOM   9986  C C   . TYR C 1 186 ? 85.084  25.363  -28.997 1.00 87.65  ? 186 TYR C C   1 
ATOM   9987  O O   . TYR C 1 186 ? 84.057  25.434  -28.323 1.00 87.97  ? 186 TYR C O   1 
ATOM   9988  C CB  . TYR C 1 186 ? 85.274  22.986  -29.926 1.00 87.89  ? 186 TYR C CB  1 
ATOM   9989  C CG  . TYR C 1 186 ? 86.157  21.746  -29.950 1.00 89.22  ? 186 TYR C CG  1 
ATOM   9990  C CD1 . TYR C 1 186 ? 87.411  21.806  -30.536 1.00 90.46  ? 186 TYR C CD1 1 
ATOM   9991  C CD2 . TYR C 1 186 ? 85.792  20.560  -29.330 1.00 89.43  ? 186 TYR C CD2 1 
ATOM   9992  C CE1 . TYR C 1 186 ? 88.266  20.721  -30.527 1.00 91.40  ? 186 TYR C CE1 1 
ATOM   9993  C CE2 . TYR C 1 186 ? 86.638  19.464  -29.316 1.00 90.46  ? 186 TYR C CE2 1 
ATOM   9994  C CZ  . TYR C 1 186 ? 87.880  19.547  -29.916 1.00 91.43  ? 186 TYR C CZ  1 
ATOM   9995  O OH  . TYR C 1 186 ? 88.763  18.505  -29.929 1.00 92.99  ? 186 TYR C OH  1 
ATOM   9996  N N   . ALA C 1 187 ? 85.535  26.378  -29.750 1.00 86.42  ? 187 ALA C N   1 
ATOM   9997  C CA  . ALA C 1 187 ? 84.833  27.656  -29.792 1.00 86.26  ? 187 ALA C CA  1 
ATOM   9998  C C   . ALA C 1 187 ? 85.064  28.382  -31.117 1.00 84.43  ? 187 ALA C C   1 
ATOM   9999  O O   . ALA C 1 187 ? 86.139  28.277  -31.708 1.00 84.90  ? 187 ALA C O   1 
ATOM   10000 C CB  . ALA C 1 187 ? 85.263  28.509  -28.617 1.00 88.36  ? 187 ALA C CB  1 
ATOM   10001 N N   . TYR C 1 188 ? 84.048  29.132  -31.562 1.00 82.40  ? 188 TYR C N   1 
ATOM   10002 C CA  . TYR C 1 188 ? 84.143  29.918  -32.782 1.00 81.36  ? 188 TYR C CA  1 
ATOM   10003 C C   . TYR C 1 188 ? 83.220  31.140  -32.752 1.00 81.77  ? 188 TYR C C   1 
ATOM   10004 O O   . TYR C 1 188 ? 82.099  31.100  -32.227 1.00 81.93  ? 188 TYR C O   1 
ATOM   10005 C CB  . TYR C 1 188 ? 83.735  29.140  -34.031 1.00 79.42  ? 188 TYR C CB  1 
ATOM   10006 C CG  . TYR C 1 188 ? 84.688  28.023  -34.389 1.00 79.51  ? 188 TYR C CG  1 
ATOM   10007 C CD1 . TYR C 1 188 ? 85.985  28.314  -34.793 1.00 80.12  ? 188 TYR C CD1 1 
ATOM   10008 C CD2 . TYR C 1 188 ? 84.295  26.692  -34.317 1.00 79.05  ? 188 TYR C CD2 1 
ATOM   10009 C CE1 . TYR C 1 188 ? 86.874  27.305  -35.109 1.00 80.16  ? 188 TYR C CE1 1 
ATOM   10010 C CE2 . TYR C 1 188 ? 85.182  25.675  -34.633 1.00 79.21  ? 188 TYR C CE2 1 
ATOM   10011 C CZ  . TYR C 1 188 ? 86.466  25.988  -35.028 1.00 79.73  ? 188 TYR C CZ  1 
ATOM   10012 O OH  . TYR C 1 188 ? 87.324  24.986  -35.331 1.00 81.25  ? 188 TYR C OH  1 
ATOM   10013 N N   . ASN C 1 189 ? 83.707  32.228  -33.362 1.00 81.41  ? 189 ASN C N   1 
ATOM   10014 C CA  . ASN C 1 189 ? 82.856  33.329  -33.772 1.00 80.85  ? 189 ASN C CA  1 
ATOM   10015 C C   . ASN C 1 189 ? 82.181  32.916  -35.077 1.00 78.13  ? 189 ASN C C   1 
ATOM   10016 O O   . ASN C 1 189 ? 82.818  32.781  -36.117 1.00 77.89  ? 189 ASN C O   1 
ATOM   10017 C CB  . ASN C 1 189 ? 83.650  34.627  -33.922 1.00 82.64  ? 189 ASN C CB  1 
ATOM   10018 C CG  . ASN C 1 189 ? 84.185  35.166  -32.610 1.00 84.99  ? 189 ASN C CG  1 
ATOM   10019 O OD1 . ASN C 1 189 ? 83.576  34.913  -31.562 1.00 85.97  ? 189 ASN C OD1 1 
ATOM   10020 N ND2 . ASN C 1 189 ? 85.286  35.920  -32.647 1.00 85.72  ? 189 ASN C ND2 1 
ATOM   10021 N N   . CYS C 1 190 ? 80.881  32.692  -35.019 1.00 76.52  ? 190 CYS C N   1 
ATOM   10022 C CA  . CYS C 1 190 ? 80.173  32.205  -36.184 1.00 74.76  ? 190 CYS C CA  1 
ATOM   10023 C C   . CYS C 1 190 ? 79.213  33.304  -36.677 1.00 74.97  ? 190 CYS C C   1 
ATOM   10024 O O   . CYS C 1 190 ? 78.483  33.897  -35.895 1.00 74.80  ? 190 CYS C O   1 
ATOM   10025 C CB  . CYS C 1 190 ? 79.488  30.876  -35.850 1.00 73.46  ? 190 CYS C CB  1 
ATOM   10026 S SG  . CYS C 1 190 ? 80.397  29.774  -34.722 1.00 73.50  ? 190 CYS C SG  1 
ATOM   10027 N N   . TYR C 1 191 ? 79.243  33.574  -37.989 1.00 74.76  ? 191 TYR C N   1 
ATOM   10028 C CA  . TYR C 1 191 ? 78.392  34.550  -38.629 1.00 75.40  ? 191 TYR C CA  1 
ATOM   10029 C C   . TYR C 1 191 ? 77.923  34.076  -40.001 1.00 74.04  ? 191 TYR C C   1 
ATOM   10030 O O   . TYR C 1 191 ? 78.724  33.783  -40.893 1.00 72.24  ? 191 TYR C O   1 
ATOM   10031 C CB  . TYR C 1 191 ? 79.119  35.877  -38.827 1.00 77.96  ? 191 TYR C CB  1 
ATOM   10032 C CG  . TYR C 1 191 ? 79.359  36.668  -37.556 1.00 80.87  ? 191 TYR C CG  1 
ATOM   10033 C CD1 . TYR C 1 191 ? 80.398  36.351  -36.686 1.00 83.01  ? 191 TYR C CD1 1 
ATOM   10034 C CD2 . TYR C 1 191 ? 78.577  37.761  -37.256 1.00 82.41  ? 191 TYR C CD2 1 
ATOM   10035 C CE1 . TYR C 1 191 ? 80.628  37.088  -35.534 1.00 85.70  ? 191 TYR C CE1 1 
ATOM   10036 C CE2 . TYR C 1 191 ? 78.806  38.516  -36.119 1.00 85.54  ? 191 TYR C CE2 1 
ATOM   10037 C CZ  . TYR C 1 191 ? 79.824  38.181  -35.245 1.00 86.99  ? 191 TYR C CZ  1 
ATOM   10038 O OH  . TYR C 1 191 ? 80.011  38.968  -34.131 1.00 90.10  ? 191 TYR C OH  1 
ATOM   10039 N N   . ASP C 1 192 ? 76.596  34.164  -40.177 1.00 74.61  ? 192 ASP C N   1 
ATOM   10040 C CA  . ASP C 1 192 ? 75.916  33.680  -41.361 1.00 74.57  ? 192 ASP C CA  1 
ATOM   10041 C C   . ASP C 1 192 ? 75.617  34.864  -42.275 1.00 75.51  ? 192 ASP C C   1 
ATOM   10042 O O   . ASP C 1 192 ? 74.669  35.613  -42.025 1.00 76.12  ? 192 ASP C O   1 
ATOM   10043 C CB  . ASP C 1 192 ? 74.661  32.900  -40.982 1.00 74.04  ? 192 ASP C CB  1 
ATOM   10044 C CG  . ASP C 1 192 ? 73.856  32.368  -42.158 1.00 73.55  ? 192 ASP C CG  1 
ATOM   10045 O OD1 . ASP C 1 192 ? 74.404  32.322  -43.278 1.00 73.48  ? 192 ASP C OD1 1 
ATOM   10046 O OD2 . ASP C 1 192 ? 72.675  32.032  -41.956 1.00 74.93  ? 192 ASP C OD2 1 
ATOM   10047 N N   . HIS C 1 193 ? 76.409  34.990  -43.349 1.00 76.32  ? 193 HIS C N   1 
ATOM   10048 C CA  . HIS C 1 193 ? 76.196  36.011  -44.370 1.00 77.59  ? 193 HIS C CA  1 
ATOM   10049 C C   . HIS C 1 193 ? 75.802  35.385  -45.712 1.00 77.04  ? 193 HIS C C   1 
ATOM   10050 O O   . HIS C 1 193 ? 75.764  36.071  -46.728 1.00 78.06  ? 193 HIS C O   1 
ATOM   10051 C CB  . HIS C 1 193 ? 77.444  36.887  -44.517 1.00 78.49  ? 193 HIS C CB  1 
ATOM   10052 C CG  . HIS C 1 193 ? 77.804  37.595  -43.264 1.00 80.61  ? 193 HIS C CG  1 
ATOM   10053 N ND1 . HIS C 1 193 ? 79.057  37.542  -42.696 1.00 82.40  ? 193 HIS C ND1 1 
ATOM   10054 C CD2 . HIS C 1 193 ? 77.075  38.362  -42.461 1.00 83.03  ? 193 HIS C CD2 1 
ATOM   10055 C CE1 . HIS C 1 193 ? 79.071  38.243  -41.575 1.00 84.14  ? 193 HIS C CE1 1 
ATOM   10056 N NE2 . HIS C 1 193 ? 77.879  38.770  -41.423 1.00 85.04  ? 193 HIS C NE2 1 
ATOM   10057 N N   . ASN C 1 194 ? 75.507  34.080  -45.719 1.00 75.67  ? 194 ASN C N   1 
ATOM   10058 C CA  . ASN C 1 194 ? 75.212  33.362  -46.951 1.00 74.56  ? 194 ASN C CA  1 
ATOM   10059 C C   . ASN C 1 194 ? 76.236  33.718  -48.034 1.00 75.02  ? 194 ASN C C   1 
ATOM   10060 O O   . ASN C 1 194 ? 75.860  34.154  -49.125 1.00 74.54  ? 194 ASN C O   1 
ATOM   10061 C CB  . ASN C 1 194 ? 73.759  33.561  -47.383 1.00 73.76  ? 194 ASN C CB  1 
ATOM   10062 C CG  . ASN C 1 194 ? 73.362  32.641  -48.518 1.00 73.20  ? 194 ASN C CG  1 
ATOM   10063 O OD1 . ASN C 1 194 ? 73.650  31.429  -48.493 1.00 74.44  ? 194 ASN C OD1 1 
ATOM   10064 N ND2 . ASN C 1 194 ? 72.726  33.185  -49.543 1.00 72.77  ? 194 ASN C ND2 1 
ATOM   10065 N N   . GLU C 1 195 ? 77.526  33.486  -47.717 1.00 75.23  ? 195 GLU C N   1 
ATOM   10066 C CA  . GLU C 1 195 ? 78.640  33.721  -48.637 1.00 75.83  ? 195 GLU C CA  1 
ATOM   10067 C C   . GLU C 1 195 ? 79.793  32.743  -48.368 1.00 76.12  ? 195 GLU C C   1 
ATOM   10068 O O   . GLU C 1 195 ? 80.120  32.445  -47.219 1.00 77.14  ? 195 GLU C O   1 
ATOM   10069 C CB  . GLU C 1 195 ? 79.182  35.149  -48.514 1.00 76.42  ? 195 GLU C CB  1 
ATOM   10070 C CG  . GLU C 1 195 ? 79.886  35.406  -47.184 1.00 75.91  ? 195 GLU C CG  1 
ATOM   10071 C CD  . GLU C 1 195 ? 80.275  36.837  -46.902 1.00 76.44  ? 195 GLU C CD  1 
ATOM   10072 O OE1 . GLU C 1 195 ? 80.054  37.722  -47.767 1.00 76.78  ? 195 GLU C OE1 1 
ATOM   10073 O OE2 . GLU C 1 195 ? 80.787  37.018  -45.776 1.00 76.01  ? 195 GLU C OE2 1 
ATOM   10074 N N   . GLY C 1 196 ? 80.441  32.248  -49.427 1.00 76.07  ? 196 GLY C N   1 
ATOM   10075 C CA  . GLY C 1 196 ? 81.529  31.298  -49.255 1.00 76.34  ? 196 GLY C CA  1 
ATOM   10076 C C   . GLY C 1 196 ? 81.055  30.056  -48.500 1.00 75.61  ? 196 GLY C C   1 
ATOM   10077 O O   . GLY C 1 196 ? 80.061  29.443  -48.895 1.00 74.71  ? 196 GLY C O   1 
ATOM   10078 N N   . GLN C 1 197 ? 81.730  29.722  -47.388 1.00 75.78  ? 197 GLN C N   1 
ATOM   10079 C CA  . GLN C 1 197 ? 81.459  28.486  -46.666 1.00 74.87  ? 197 GLN C CA  1 
ATOM   10080 C C   . GLN C 1 197 ? 79.994  28.398  -46.229 1.00 73.92  ? 197 GLN C C   1 
ATOM   10081 O O   . GLN C 1 197 ? 79.475  27.290  -46.120 1.00 74.12  ? 197 GLN C O   1 
ATOM   10082 C CB  . GLN C 1 197 ? 82.315  28.278  -45.417 1.00 75.97  ? 197 GLN C CB  1 
ATOM   10083 C CG  . GLN C 1 197 ? 83.795  28.044  -45.703 1.00 78.20  ? 197 GLN C CG  1 
ATOM   10084 C CD  . GLN C 1 197 ? 84.576  29.334  -45.813 1.00 80.24  ? 197 GLN C CD  1 
ATOM   10085 O OE1 . GLN C 1 197 ? 84.269  30.189  -46.649 1.00 82.70  ? 197 GLN C OE1 1 
ATOM   10086 N NE2 . GLN C 1 197 ? 85.579  29.503  -44.965 1.00 81.03  ? 197 GLN C NE2 1 
ATOM   10087 N N   . THR C 1 198 ? 79.328  29.537  -45.959 1.00 72.83  ? 198 THR C N   1 
ATOM   10088 C CA  . THR C 1 198 ? 77.962  29.497  -45.457 1.00 71.23  ? 198 THR C CA  1 
ATOM   10089 C C   . THR C 1 198 ? 76.973  29.557  -46.613 1.00 70.18  ? 198 THR C C   1 
ATOM   10090 O O   . THR C 1 198 ? 75.787  29.431  -46.388 1.00 70.82  ? 198 THR C O   1 
ATOM   10091 C CB  . THR C 1 198 ? 77.677  30.613  -44.454 1.00 72.02  ? 198 THR C CB  1 
ATOM   10092 O OG1 . THR C 1 198 ? 77.782  31.859  -45.140 1.00 73.61  ? 198 THR C OG1 1 
ATOM   10093 C CG2 . THR C 1 198 ? 78.584  30.554  -43.239 1.00 72.57  ? 198 THR C CG2 1 
ATOM   10094 N N   . ALA C 1 199 ? 77.431  29.757  -47.844 1.00 69.98  ? 199 ALA C N   1 
ATOM   10095 C CA  . ALA C 1 199 ? 76.548  29.645  -48.993 1.00 69.58  ? 199 ALA C CA  1 
ATOM   10096 C C   . ALA C 1 199 ? 76.607  28.232  -49.586 1.00 69.07  ? 199 ALA C C   1 
ATOM   10097 O O   . ALA C 1 199 ? 75.641  27.697  -50.122 1.00 67.76  ? 199 ALA C O   1 
ATOM   10098 C CB  . ALA C 1 199 ? 76.917  30.705  -49.998 1.00 70.21  ? 199 ALA C CB  1 
ATOM   10099 N N   . THR C 1 200 ? 77.772  27.609  -49.497 1.00 70.37  ? 200 THR C N   1 
ATOM   10100 C CA  . THR C 1 200 ? 77.930  26.284  -50.060 1.00 70.75  ? 200 THR C CA  1 
ATOM   10101 C C   . THR C 1 200 ? 77.263  25.266  -49.152 1.00 68.96  ? 200 THR C C   1 
ATOM   10102 O O   . THR C 1 200 ? 76.502  24.446  -49.637 1.00 68.43  ? 200 THR C O   1 
ATOM   10103 C CB  . THR C 1 200 ? 79.410  25.981  -50.305 1.00 72.99  ? 200 THR C CB  1 
ATOM   10104 O OG1 . THR C 1 200 ? 80.189  26.257  -49.138 1.00 73.77  ? 200 THR C OG1 1 
ATOM   10105 C CG2 . THR C 1 200 ? 79.929  26.798  -51.476 1.00 74.40  ? 200 THR C CG2 1 
ATOM   10106 N N   . MET C 1 201 ? 77.567  25.325  -47.854 1.00 68.66  ? 201 MET C N   1 
ATOM   10107 C CA  . MET C 1 201 ? 77.104  24.326  -46.903 1.00 68.55  ? 201 MET C CA  1 
ATOM   10108 C C   . MET C 1 201 ? 75.923  24.880  -46.116 1.00 67.71  ? 201 MET C C   1 
ATOM   10109 O O   . MET C 1 201 ? 75.093  24.136  -45.596 1.00 67.97  ? 201 MET C O   1 
ATOM   10110 C CB  . MET C 1 201 ? 78.229  23.921  -45.940 1.00 69.67  ? 201 MET C CB  1 
ATOM   10111 C CG  . MET C 1 201 ? 79.394  23.225  -46.629 1.00 70.31  ? 201 MET C CG  1 
ATOM   10112 S SD  . MET C 1 201 ? 80.909  23.181  -45.653 1.00 72.61  ? 201 MET C SD  1 
ATOM   10113 C CE  . MET C 1 201 ? 81.712  24.738  -46.063 1.00 73.35  ? 201 MET C CE  1 
ATOM   10114 N N   . GLY C 1 202 ? 75.842  26.204  -46.026 1.00 66.91  ? 202 GLY C N   1 
ATOM   10115 C CA  . GLY C 1 202 ? 74.935  26.782  -45.065 1.00 66.20  ? 202 GLY C CA  1 
ATOM   10116 C C   . GLY C 1 202 ? 75.528  26.736  -43.662 1.00 66.46  ? 202 GLY C C   1 
ATOM   10117 O O   . GLY C 1 202 ? 76.542  26.090  -43.409 1.00 67.02  ? 202 GLY C O   1 
ATOM   10118 N N   . PHE C 1 203 ? 74.834  27.414  -42.753 1.00 66.98  ? 203 PHE C N   1 
ATOM   10119 C CA  . PHE C 1 203 ? 75.380  27.828  -41.476 1.00 68.02  ? 203 PHE C CA  1 
ATOM   10120 C C   . PHE C 1 203 ? 75.514  26.600  -40.587 1.00 68.40  ? 203 PHE C C   1 
ATOM   10121 O O   . PHE C 1 203 ? 76.636  26.194  -40.319 1.00 69.34  ? 203 PHE C O   1 
ATOM   10122 C CB  . PHE C 1 203 ? 74.506  28.974  -40.951 1.00 68.45  ? 203 PHE C CB  1 
ATOM   10123 C CG  . PHE C 1 203 ? 75.093  29.707  -39.758 1.00 69.42  ? 203 PHE C CG  1 
ATOM   10124 C CD1 . PHE C 1 203 ? 76.387  30.177  -39.790 1.00 70.18  ? 203 PHE C CD1 1 
ATOM   10125 C CD2 . PHE C 1 203 ? 74.348  29.919  -38.607 1.00 70.29  ? 203 PHE C CD2 1 
ATOM   10126 C CE1 . PHE C 1 203 ? 76.909  30.851  -38.702 1.00 71.71  ? 203 PHE C CE1 1 
ATOM   10127 C CE2 . PHE C 1 203 ? 74.880  30.574  -37.514 1.00 71.50  ? 203 PHE C CE2 1 
ATOM   10128 C CZ  . PHE C 1 203 ? 76.156  31.041  -37.565 1.00 72.26  ? 203 PHE C CZ  1 
ATOM   10129 N N   . LYS C 1 204 ? 74.393  25.980  -40.193 1.00 68.70  ? 204 LYS C N   1 
ATOM   10130 C CA  . LYS C 1 204 ? 74.433  24.770  -39.377 1.00 69.66  ? 204 LYS C CA  1 
ATOM   10131 C C   . LYS C 1 204 ? 75.489  23.779  -39.894 1.00 69.12  ? 204 LYS C C   1 
ATOM   10132 O O   . LYS C 1 204 ? 76.403  23.325  -39.180 1.00 68.67  ? 204 LYS C O   1 
ATOM   10133 C CB  . LYS C 1 204 ? 73.051  24.114  -39.357 1.00 70.11  ? 204 LYS C CB  1 
ATOM   10134 C CG  . LYS C 1 204 ? 72.984  22.739  -38.695 1.00 71.50  ? 204 LYS C CG  1 
ATOM   10135 C CD  . LYS C 1 204 ? 71.842  21.865  -39.214 1.00 71.92  ? 204 LYS C CD  1 
ATOM   10136 C CE  . LYS C 1 204 ? 71.782  20.474  -38.667 1.00 72.60  ? 204 LYS C CE  1 
ATOM   10137 N NZ  . LYS C 1 204 ? 71.229  19.570  -39.682 1.00 72.89  ? 204 LYS C NZ  1 
ATOM   10138 N N   . ASP C 1 205 ? 75.379  23.441  -41.174 1.00 67.93  ? 205 ASP C N   1 
ATOM   10139 C CA  . ASP C 1 205 ? 76.254  22.403  -41.681 1.00 67.55  ? 205 ASP C CA  1 
ATOM   10140 C C   . ASP C 1 205 ? 77.715  22.853  -41.574 1.00 68.39  ? 205 ASP C C   1 
ATOM   10141 O O   . ASP C 1 205 ? 78.538  22.137  -41.010 1.00 68.85  ? 205 ASP C O   1 
ATOM   10142 C CB  . ASP C 1 205 ? 75.759  21.887  -43.028 1.00 66.70  ? 205 ASP C CB  1 
ATOM   10143 C CG  . ASP C 1 205 ? 74.551  20.934  -43.065 1.00 65.70  ? 205 ASP C CG  1 
ATOM   10144 O OD1 . ASP C 1 205 ? 73.810  20.762  -42.043 1.00 65.03  ? 205 ASP C OD1 1 
ATOM   10145 O OD2 . ASP C 1 205 ? 74.320  20.391  -44.163 1.00 64.63  ? 205 ASP C OD2 1 
ATOM   10146 N N   . TYR C 1 206 ? 78.051  24.043  -42.091 1.00 69.04  ? 206 TYR C N   1 
ATOM   10147 C CA  . TYR C 1 206 ? 79.423  24.526  -42.050 1.00 69.58  ? 206 TYR C CA  1 
ATOM   10148 C C   . TYR C 1 206 ? 79.983  24.482  -40.637 1.00 70.09  ? 206 TYR C C   1 
ATOM   10149 O O   . TYR C 1 206 ? 81.060  23.954  -40.428 1.00 72.41  ? 206 TYR C O   1 
ATOM   10150 C CB  . TYR C 1 206 ? 79.598  25.970  -42.495 1.00 70.62  ? 206 TYR C CB  1 
ATOM   10151 C CG  . TYR C 1 206 ? 81.020  26.503  -42.374 1.00 72.43  ? 206 TYR C CG  1 
ATOM   10152 C CD1 . TYR C 1 206 ? 82.123  25.722  -42.730 1.00 73.33  ? 206 TYR C CD1 1 
ATOM   10153 C CD2 . TYR C 1 206 ? 81.263  27.791  -41.907 1.00 73.33  ? 206 TYR C CD2 1 
ATOM   10154 C CE1 . TYR C 1 206 ? 83.417  26.204  -42.623 1.00 74.12  ? 206 TYR C CE1 1 
ATOM   10155 C CE2 . TYR C 1 206 ? 82.555  28.285  -41.791 1.00 74.58  ? 206 TYR C CE2 1 
ATOM   10156 C CZ  . TYR C 1 206 ? 83.629  27.489  -42.158 1.00 75.28  ? 206 TYR C CZ  1 
ATOM   10157 O OH  . TYR C 1 206 ? 84.920  27.911  -42.092 1.00 76.77  ? 206 TYR C OH  1 
ATOM   10158 N N   . ILE C 1 207 ? 79.276  25.020  -39.657 1.00 69.97  ? 207 ILE C N   1 
ATOM   10159 C CA  . ILE C 1 207 ? 79.807  25.003  -38.306 1.00 71.59  ? 207 ILE C CA  1 
ATOM   10160 C C   . ILE C 1 207 ? 79.897  23.568  -37.781 1.00 73.72  ? 207 ILE C C   1 
ATOM   10161 O O   . ILE C 1 207 ? 80.867  23.222  -37.088 1.00 74.92  ? 207 ILE C O   1 
ATOM   10162 C CB  . ILE C 1 207 ? 78.977  25.934  -37.411 1.00 71.62  ? 207 ILE C CB  1 
ATOM   10163 C CG1 . ILE C 1 207 ? 79.138  27.386  -37.872 1.00 71.71  ? 207 ILE C CG1 1 
ATOM   10164 C CG2 . ILE C 1 207 ? 79.307  25.779  -35.928 1.00 72.78  ? 207 ILE C CG2 1 
ATOM   10165 C CD1 . ILE C 1 207 ? 80.570  27.848  -38.070 1.00 71.99  ? 207 ILE C CD1 1 
ATOM   10166 N N   . LYS C 1 208 ? 78.897  22.740  -38.131 1.00 74.69  ? 208 LYS C N   1 
ATOM   10167 C CA  . LYS C 1 208 ? 78.883  21.331  -37.768 1.00 75.80  ? 208 LYS C CA  1 
ATOM   10168 C C   . LYS C 1 208 ? 80.059  20.594  -38.419 1.00 74.81  ? 208 LYS C C   1 
ATOM   10169 O O   . LYS C 1 208 ? 80.759  19.830  -37.748 1.00 74.53  ? 208 LYS C O   1 
ATOM   10170 C CB  . LYS C 1 208 ? 77.556  20.665  -38.158 1.00 76.70  ? 208 LYS C CB  1 
ATOM   10171 C CG  . LYS C 1 208 ? 77.489  19.177  -37.767 1.00 79.43  ? 208 LYS C CG  1 
ATOM   10172 C CD  . LYS C 1 208 ? 76.222  18.389  -38.123 1.00 80.75  ? 208 LYS C CD  1 
ATOM   10173 C CE  . LYS C 1 208 ? 76.164  17.950  -39.559 1.00 80.42  ? 208 LYS C CE  1 
ATOM   10174 N NZ  . LYS C 1 208 ? 75.180  16.883  -39.733 1.00 80.06  ? 208 LYS C NZ  1 
ATOM   10175 N N   . GLY C 1 209 ? 80.237  20.814  -39.731 1.00 73.66  ? 209 GLY C N   1 
ATOM   10176 C CA  . GLY C 1 209 ? 81.341  20.251  -40.494 1.00 74.12  ? 209 GLY C CA  1 
ATOM   10177 C C   . GLY C 1 209 ? 82.673  20.461  -39.778 1.00 75.58  ? 209 GLY C C   1 
ATOM   10178 O O   . GLY C 1 209 ? 83.484  19.536  -39.662 1.00 75.11  ? 209 GLY C O   1 
ATOM   10179 N N   . LEU C 1 210 ? 82.874  21.683  -39.268 1.00 76.33  ? 210 LEU C N   1 
ATOM   10180 C CA  . LEU C 1 210 ? 84.012  21.938  -38.402 1.00 78.64  ? 210 LEU C CA  1 
ATOM   10181 C C   . LEU C 1 210 ? 83.970  21.012  -37.182 1.00 79.65  ? 210 LEU C C   1 
ATOM   10182 O O   . LEU C 1 210 ? 84.959  20.364  -36.853 1.00 80.44  ? 210 LEU C O   1 
ATOM   10183 C CB  . LEU C 1 210 ? 84.096  23.416  -38.020 1.00 79.40  ? 210 LEU C CB  1 
ATOM   10184 C CG  . LEU C 1 210 ? 84.193  24.404  -39.192 1.00 79.13  ? 210 LEU C CG  1 
ATOM   10185 C CD1 . LEU C 1 210 ? 84.526  25.822  -38.731 1.00 79.23  ? 210 LEU C CD1 1 
ATOM   10186 C CD2 . LEU C 1 210 ? 85.207  23.920  -40.219 1.00 79.56  ? 210 LEU C CD2 1 
ATOM   10187 N N   . ASN C 1 211 ? 82.827  20.915  -36.508 1.00 79.58  ? 211 ASN C N   1 
ATOM   10188 C CA  . ASN C 1 211 ? 82.816  20.176  -35.260 1.00 80.09  ? 211 ASN C CA  1 
ATOM   10189 C C   . ASN C 1 211 ? 83.136  18.707  -35.516 1.00 80.14  ? 211 ASN C C   1 
ATOM   10190 O O   . ASN C 1 211 ? 83.795  18.083  -34.690 1.00 80.45  ? 211 ASN C O   1 
ATOM   10191 C CB  . ASN C 1 211 ? 81.536  20.381  -34.467 1.00 79.47  ? 211 ASN C CB  1 
ATOM   10192 C CG  . ASN C 1 211 ? 81.900  20.699  -33.039 1.00 81.63  ? 211 ASN C CG  1 
ATOM   10193 O OD1 . ASN C 1 211 ? 82.739  21.593  -32.799 1.00 83.41  ? 211 ASN C OD1 1 
ATOM   10194 N ND2 . ASN C 1 211 ? 81.321  19.964  -32.100 1.00 82.03  ? 211 ASN C ND2 1 
ATOM   10195 N N   . GLU C 1 212 ? 82.673  18.179  -36.658 1.00 78.92  ? 212 GLU C N   1 
ATOM   10196 C CA  . GLU C 1 212 ? 82.934  16.802  -37.054 1.00 78.84  ? 212 GLU C CA  1 
ATOM   10197 C C   . GLU C 1 212 ? 84.429  16.632  -37.368 1.00 80.45  ? 212 GLU C C   1 
ATOM   10198 O O   . GLU C 1 212 ? 85.038  15.610  -37.053 1.00 80.77  ? 212 GLU C O   1 
ATOM   10199 C CB  . GLU C 1 212 ? 81.963  16.420  -38.180 1.00 77.36  ? 212 GLU C CB  1 
ATOM   10200 C CG  . GLU C 1 212 ? 80.579  16.049  -37.647 1.00 77.66  ? 212 GLU C CG  1 
ATOM   10201 C CD  . GLU C 1 212 ? 79.311  16.150  -38.505 1.00 76.62  ? 212 GLU C CD  1 
ATOM   10202 O OE1 . GLU C 1 212 ? 79.338  16.573  -39.679 1.00 76.17  ? 212 GLU C OE1 1 
ATOM   10203 O OE2 . GLU C 1 212 ? 78.236  15.798  -37.953 1.00 76.35  ? 212 GLU C OE2 1 
ATOM   10204 N N   . LEU C 1 213 ? 85.061  17.650  -37.958 1.00 80.77  ? 213 LEU C N   1 
ATOM   10205 C CA  . LEU C 1 213 ? 86.499  17.582  -38.169 1.00 82.15  ? 213 LEU C CA  1 
ATOM   10206 C C   . LEU C 1 213 ? 87.231  17.628  -36.827 1.00 83.79  ? 213 LEU C C   1 
ATOM   10207 O O   . LEU C 1 213 ? 88.214  16.920  -36.664 1.00 86.15  ? 213 LEU C O   1 
ATOM   10208 C CB  . LEU C 1 213 ? 86.988  18.673  -39.119 1.00 82.13  ? 213 LEU C CB  1 
ATOM   10209 C CG  . LEU C 1 213 ? 86.445  18.597  -40.551 1.00 81.58  ? 213 LEU C CG  1 
ATOM   10210 C CD1 . LEU C 1 213 ? 86.854  19.822  -41.354 1.00 81.55  ? 213 LEU C CD1 1 
ATOM   10211 C CD2 . LEU C 1 213 ? 86.921  17.350  -41.252 1.00 81.83  ? 213 LEU C CD2 1 
ATOM   10212 N N   . ASN C 1 214 ? 86.737  18.426  -35.869 1.00 84.56  ? 214 ASN C N   1 
ATOM   10213 C CA  . ASN C 1 214 ? 87.393  18.634  -34.580 1.00 85.50  ? 214 ASN C CA  1 
ATOM   10214 C C   . ASN C 1 214 ? 87.341  17.364  -33.725 1.00 86.61  ? 214 ASN C C   1 
ATOM   10215 O O   . ASN C 1 214 ? 88.140  17.233  -32.797 1.00 89.55  ? 214 ASN C O   1 
ATOM   10216 C CB  . ASN C 1 214 ? 86.812  19.833  -33.824 1.00 85.01  ? 214 ASN C CB  1 
ATOM   10217 C CG  . ASN C 1 214 ? 87.228  21.148  -34.441 1.00 84.75  ? 214 ASN C CG  1 
ATOM   10218 O OD1 . ASN C 1 214 ? 88.316  21.240  -35.024 1.00 84.76  ? 214 ASN C OD1 1 
ATOM   10219 N ND2 . ASN C 1 214 ? 86.388  22.169  -34.321 1.00 84.60  ? 214 ASN C ND2 1 
ATOM   10220 N N   . GLY C 1 215 ? 86.393  16.454  -34.004 1.00 84.76  ? 215 GLY C N   1 
ATOM   10221 C CA  . GLY C 1 215 ? 86.409  15.136  -33.392 1.00 86.27  ? 215 GLY C CA  1 
ATOM   10222 C C   . GLY C 1 215 ? 85.484  14.985  -32.178 1.00 87.58  ? 215 GLY C C   1 
ATOM   10223 O O   . GLY C 1 215 ? 85.730  14.120  -31.336 1.00 90.69  ? 215 GLY C O   1 
ATOM   10224 N N   . LEU C 1 216 ? 84.441  15.824  -32.076 1.00 85.70  ? 216 LEU C N   1 
ATOM   10225 C CA  . LEU C 1 216 ? 83.254  15.577  -31.255 1.00 85.14  ? 216 LEU C CA  1 
ATOM   10226 C C   . LEU C 1 216 ? 83.576  15.144  -29.823 1.00 86.95  ? 216 LEU C C   1 
ATOM   10227 O O   . LEU C 1 216 ? 82.764  14.448  -29.216 1.00 87.57  ? 216 LEU C O   1 
ATOM   10228 C CB  . LEU C 1 216 ? 82.368  14.540  -31.950 1.00 83.85  ? 216 LEU C CB  1 
ATOM   10229 C CG  . LEU C 1 216 ? 81.790  14.942  -33.315 1.00 82.03  ? 216 LEU C CG  1 
ATOM   10230 C CD1 . LEU C 1 216 ? 80.693  13.970  -33.732 1.00 82.04  ? 216 LEU C CD1 1 
ATOM   10231 C CD2 . LEU C 1 216 ? 81.253  16.365  -33.370 1.00 80.30  ? 216 LEU C CD2 1 
ATOM   10232 N N   . ASP C 1 217 ? 84.715  15.593  -29.267 1.00 87.68  ? 217 ASP C N   1 
ATOM   10233 C CA  . ASP C 1 217 ? 85.263  14.999  -28.051 1.00 89.53  ? 217 ASP C CA  1 
ATOM   10234 C C   . ASP C 1 217 ? 85.385  16.018  -26.917 1.00 90.39  ? 217 ASP C C   1 
ATOM   10235 O O   . ASP C 1 217 ? 86.022  15.743  -25.898 1.00 91.90  ? 217 ASP C O   1 
ATOM   10236 C CB  . ASP C 1 217 ? 86.595  14.319  -28.320 1.00 90.34  ? 217 ASP C CB  1 
ATOM   10237 C CG  . ASP C 1 217 ? 87.577  15.113  -29.162 1.00 90.03  ? 217 ASP C CG  1 
ATOM   10238 O OD1 . ASP C 1 217 ? 87.129  16.068  -29.833 1.00 88.81  ? 217 ASP C OD1 1 
ATOM   10239 O OD2 . ASP C 1 217 ? 88.779  14.768  -29.134 1.00 92.89  ? 217 ASP C OD2 1 
ATOM   10240 N N   . LYS C 1 218 ? 84.773  17.192  -27.096 1.00 89.12  ? 218 LYS C N   1 
ATOM   10241 C CA  . LYS C 1 218 ? 84.774  18.227  -26.077 1.00 89.92  ? 218 LYS C CA  1 
ATOM   10242 C C   . LYS C 1 218 ? 83.579  19.132  -26.327 1.00 88.30  ? 218 LYS C C   1 
ATOM   10243 O O   . LYS C 1 218 ? 83.104  19.207  -27.459 1.00 86.02  ? 218 LYS C O   1 
ATOM   10244 C CB  . LYS C 1 218 ? 86.008  19.141  -26.110 1.00 90.35  ? 218 LYS C CB  1 
ATOM   10245 C CG  . LYS C 1 218 ? 87.348  18.456  -26.178 1.00 90.81  ? 218 LYS C CG  1 
ATOM   10246 C CD  . LYS C 1 218 ? 88.533  19.390  -26.351 1.00 91.17  ? 218 LYS C CD  1 
ATOM   10247 C CE  . LYS C 1 218 ? 89.764  18.552  -26.159 1.00 92.55  ? 218 LYS C CE  1 
ATOM   10248 N NZ  . LYS C 1 218 ? 90.927  19.173  -26.779 1.00 92.33  ? 218 LYS C NZ  1 
ATOM   10249 N N   . PRO C 1 219 ? 83.089  19.855  -25.294 1.00 89.51  ? 219 PRO C N   1 
ATOM   10250 C CA  . PRO C 1 219 ? 82.014  20.833  -25.475 1.00 88.60  ? 219 PRO C CA  1 
ATOM   10251 C C   . PRO C 1 219 ? 82.303  21.779  -26.635 1.00 87.52  ? 219 PRO C C   1 
ATOM   10252 O O   . PRO C 1 219 ? 83.458  22.062  -26.926 1.00 88.49  ? 219 PRO C O   1 
ATOM   10253 C CB  . PRO C 1 219 ? 81.978  21.573  -24.132 1.00 90.38  ? 219 PRO C CB  1 
ATOM   10254 C CG  . PRO C 1 219 ? 82.495  20.560  -23.141 1.00 92.43  ? 219 PRO C CG  1 
ATOM   10255 C CD  . PRO C 1 219 ? 83.546  19.764  -23.897 1.00 91.74  ? 219 PRO C CD  1 
ATOM   10256 N N   . PHE C 1 220 ? 81.247  22.227  -27.316 1.00 87.01  ? 220 PHE C N   1 
ATOM   10257 C CA  . PHE C 1 220 ? 81.350  23.260  -28.335 1.00 87.05  ? 220 PHE C CA  1 
ATOM   10258 C C   . PHE C 1 220 ? 80.433  24.424  -27.955 1.00 87.42  ? 220 PHE C C   1 
ATOM   10259 O O   . PHE C 1 220 ? 79.285  24.204  -27.577 1.00 87.12  ? 220 PHE C O   1 
ATOM   10260 C CB  . PHE C 1 220 ? 81.013  22.724  -29.731 1.00 85.76  ? 220 PHE C CB  1 
ATOM   10261 C CG  . PHE C 1 220 ? 80.735  23.802  -30.777 1.00 84.52  ? 220 PHE C CG  1 
ATOM   10262 C CD1 . PHE C 1 220 ? 81.702  24.738  -31.123 1.00 85.00  ? 220 PHE C CD1 1 
ATOM   10263 C CD2 . PHE C 1 220 ? 79.527  23.845  -31.447 1.00 83.02  ? 220 PHE C CD2 1 
ATOM   10264 C CE1 . PHE C 1 220 ? 81.459  25.697  -32.086 1.00 83.42  ? 220 PHE C CE1 1 
ATOM   10265 C CE2 . PHE C 1 220 ? 79.295  24.807  -32.413 1.00 82.44  ? 220 PHE C CE2 1 
ATOM   10266 C CZ  . PHE C 1 220 ? 80.258  25.730  -32.725 1.00 82.42  ? 220 PHE C CZ  1 
ATOM   10267 N N   . ILE C 1 221 ? 80.983  25.647  -28.041 1.00 88.11  ? 221 ILE C N   1 
ATOM   10268 C CA  . ILE C 1 221 ? 80.290  26.871  -27.673 1.00 89.28  ? 221 ILE C CA  1 
ATOM   10269 C C   . ILE C 1 221 ? 80.584  27.920  -28.738 1.00 89.70  ? 221 ILE C C   1 
ATOM   10270 O O   . ILE C 1 221 ? 81.689  27.927  -29.287 1.00 91.04  ? 221 ILE C O   1 
ATOM   10271 C CB  . ILE C 1 221 ? 80.717  27.380  -26.281 1.00 90.99  ? 221 ILE C CB  1 
ATOM   10272 C CG1 . ILE C 1 221 ? 82.143  27.947  -26.277 1.00 91.74  ? 221 ILE C CG1 1 
ATOM   10273 C CG2 . ILE C 1 221 ? 80.534  26.289  -25.230 1.00 92.08  ? 221 ILE C CG2 1 
ATOM   10274 C CD1 . ILE C 1 221 ? 82.571  28.561  -24.955 1.00 94.27  ? 221 ILE C CD1 1 
ATOM   10275 N N   . THR C 1 222 ? 79.591  28.788  -28.994 1.00 89.14  ? 222 THR C N   1 
ATOM   10276 C CA  . THR C 1 222 ? 79.732  29.942  -29.867 1.00 88.76  ? 222 THR C CA  1 
ATOM   10277 C C   . THR C 1 222 ? 80.094  31.147  -29.008 1.00 91.11  ? 222 THR C C   1 
ATOM   10278 O O   . THR C 1 222 ? 79.419  31.415  -28.012 1.00 93.00  ? 222 THR C O   1 
ATOM   10279 C CB  . THR C 1 222 ? 78.424  30.183  -30.617 1.00 88.09  ? 222 THR C CB  1 
ATOM   10280 O OG1 . THR C 1 222 ? 77.407  30.355  -29.633 1.00 88.02  ? 222 THR C OG1 1 
ATOM   10281 C CG2 . THR C 1 222 ? 78.033  29.007  -31.491 1.00 87.59  ? 222 THR C CG2 1 
ATOM   10282 N N   . THR C 1 223 ? 81.145  31.871  -29.418 1.00 90.86  ? 223 THR C N   1 
ATOM   10283 C CA  . THR C 1 223 ? 81.638  33.032  -28.689 1.00 92.46  ? 223 THR C CA  1 
ATOM   10284 C C   . THR C 1 223 ? 81.100  34.347  -29.260 1.00 91.35  ? 223 THR C C   1 
ATOM   10285 O O   . THR C 1 223 ? 81.154  35.355  -28.564 1.00 92.57  ? 223 THR C O   1 
ATOM   10286 C CB  . THR C 1 223 ? 83.163  33.026  -28.732 1.00 94.00  ? 223 THR C CB  1 
ATOM   10287 O OG1 . THR C 1 223 ? 83.489  32.746  -30.092 1.00 91.72  ? 223 THR C OG1 1 
ATOM   10288 C CG2 . THR C 1 223 ? 83.764  32.018  -27.770 1.00 95.47  ? 223 THR C CG2 1 
ATOM   10289 N N   . GLU C 1 224 ? 80.654  34.340  -30.530 1.00 88.78  ? 224 GLU C N   1 
ATOM   10290 C CA  . GLU C 1 224 ? 79.974  35.464  -31.175 1.00 87.75  ? 224 GLU C CA  1 
ATOM   10291 C C   . GLU C 1 224 ? 78.984  34.921  -32.220 1.00 83.81  ? 224 GLU C C   1 
ATOM   10292 O O   . GLU C 1 224 ? 79.209  33.866  -32.808 1.00 82.15  ? 224 GLU C O   1 
ATOM   10293 C CB  . GLU C 1 224 ? 80.918  36.443  -31.904 1.00 88.51  ? 224 GLU C CB  1 
ATOM   10294 C CG  . GLU C 1 224 ? 81.835  37.314  -31.039 1.00 91.28  ? 224 GLU C CG  1 
ATOM   10295 C CD  . GLU C 1 224 ? 82.922  38.167  -31.731 1.00 92.19  ? 224 GLU C CD  1 
ATOM   10296 O OE1 . GLU C 1 224 ? 82.852  38.465  -32.959 1.00 91.16  ? 224 GLU C OE1 1 
ATOM   10297 O OE2 . GLU C 1 224 ? 83.897  38.545  -31.021 1.00 93.02  ? 224 GLU C OE2 1 
ATOM   10298 N N   . PHE C 1 225 ? 77.883  35.650  -32.448 1.00 82.72  ? 225 PHE C N   1 
ATOM   10299 C CA  . PHE C 1 225 ? 77.062  35.558  -33.656 1.00 80.08  ? 225 PHE C CA  1 
ATOM   10300 C C   . PHE C 1 225 ? 76.070  36.718  -33.630 1.00 80.65  ? 225 PHE C C   1 
ATOM   10301 O O   . PHE C 1 225 ? 75.641  37.109  -32.547 1.00 82.27  ? 225 PHE C O   1 
ATOM   10302 C CB  . PHE C 1 225 ? 76.295  34.237  -33.823 1.00 77.59  ? 225 PHE C CB  1 
ATOM   10303 C CG  . PHE C 1 225 ? 75.370  33.876  -32.673 1.00 77.49  ? 225 PHE C CG  1 
ATOM   10304 C CD1 . PHE C 1 225 ? 75.872  33.300  -31.513 1.00 78.08  ? 225 PHE C CD1 1 
ATOM   10305 C CD2 . PHE C 1 225 ? 74.008  34.126  -32.752 1.00 77.15  ? 225 PHE C CD2 1 
ATOM   10306 C CE1 . PHE C 1 225 ? 75.035  32.998  -30.452 1.00 79.00  ? 225 PHE C CE1 1 
ATOM   10307 C CE2 . PHE C 1 225 ? 73.171  33.802  -31.693 1.00 77.89  ? 225 PHE C CE2 1 
ATOM   10308 C CZ  . PHE C 1 225 ? 73.683  33.248  -30.542 1.00 78.78  ? 225 PHE C CZ  1 
ATOM   10309 N N   . GLY C 1 226 ? 75.717  37.283  -34.795 1.00 79.96  ? 226 GLY C N   1 
ATOM   10310 C CA  . GLY C 1 226 ? 74.759  38.383  -34.798 1.00 81.10  ? 226 GLY C CA  1 
ATOM   10311 C C   . GLY C 1 226 ? 74.801  39.237  -36.062 1.00 81.17  ? 226 GLY C C   1 
ATOM   10312 O O   . GLY C 1 226 ? 75.517  38.941  -37.017 1.00 79.29  ? 226 GLY C O   1 
ATOM   10313 N N   . TYR C 1 227 ? 73.994  40.310  -36.043 1.00 83.21  ? 227 TYR C N   1 
ATOM   10314 C CA  . TYR C 1 227 ? 73.781  41.131  -37.221 1.00 83.27  ? 227 TYR C CA  1 
ATOM   10315 C C   . TYR C 1 227 ? 73.802  42.590  -36.816 1.00 85.11  ? 227 TYR C C   1 
ATOM   10316 O O   . TYR C 1 227 ? 73.609  42.902  -35.642 1.00 86.01  ? 227 TYR C O   1 
ATOM   10317 C CB  . TYR C 1 227 ? 72.464  40.752  -37.897 1.00 82.81  ? 227 TYR C CB  1 
ATOM   10318 C CG  . TYR C 1 227 ? 72.474  39.360  -38.507 1.00 81.63  ? 227 TYR C CG  1 
ATOM   10319 C CD1 . TYR C 1 227 ? 73.077  39.128  -39.736 1.00 82.07  ? 227 TYR C CD1 1 
ATOM   10320 C CD2 . TYR C 1 227 ? 71.919  38.278  -37.846 1.00 81.26  ? 227 TYR C CD2 1 
ATOM   10321 C CE1 . TYR C 1 227 ? 73.113  37.865  -40.306 1.00 80.64  ? 227 TYR C CE1 1 
ATOM   10322 C CE2 . TYR C 1 227 ? 71.936  37.009  -38.406 1.00 80.32  ? 227 TYR C CE2 1 
ATOM   10323 C CZ  . TYR C 1 227 ? 72.537  36.801  -39.639 1.00 79.93  ? 227 TYR C CZ  1 
ATOM   10324 O OH  . TYR C 1 227 ? 72.574  35.564  -40.216 1.00 78.46  ? 227 TYR C OH  1 
ATOM   10325 N N   . SER C 1 228 ? 73.995  43.433  -37.839 1.00 85.83  ? 228 SER C N   1 
ATOM   10326 C CA  . SER C 1 228 ? 74.232  44.869  -37.711 1.00 88.45  ? 228 SER C CA  1 
ATOM   10327 C C   . SER C 1 228 ? 73.157  45.676  -38.441 1.00 88.73  ? 228 SER C C   1 
ATOM   10328 O O   . SER C 1 228 ? 72.793  45.336  -39.566 1.00 87.26  ? 228 SER C O   1 
ATOM   10329 C CB  . SER C 1 228 ? 75.613  45.216  -38.240 1.00 88.96  ? 228 SER C CB  1 
ATOM   10330 O OG  . SER C 1 228 ? 75.771  46.599  -38.520 1.00 91.29  ? 228 SER C OG  1 
ATOM   10331 N N   . VAL C 1 229 ? 72.715  46.784  -37.820 1.00 90.80  ? 229 VAL C N   1 
ATOM   10332 C CA  . VAL C 1 229 ? 71.605  47.581  -38.329 1.00 91.52  ? 229 VAL C CA  1 
ATOM   10333 C C   . VAL C 1 229 ? 72.072  49.004  -38.642 1.00 94.45  ? 229 VAL C C   1 
ATOM   10334 O O   . VAL C 1 229 ? 71.364  49.976  -38.371 1.00 96.20  ? 229 VAL C O   1 
ATOM   10335 C CB  . VAL C 1 229 ? 70.412  47.563  -37.353 1.00 91.62  ? 229 VAL C CB  1 
ATOM   10336 C CG1 . VAL C 1 229 ? 69.876  46.141  -37.222 1.00 89.15  ? 229 VAL C CG1 1 
ATOM   10337 C CG2 . VAL C 1 229 ? 70.725  48.156  -35.979 1.00 93.66  ? 229 VAL C CG2 1 
ATOM   10338 N N   . SER C 1 230 ? 73.258  49.112  -39.255 1.00 94.65  ? 230 SER C N   1 
ATOM   10339 C CA  . SER C 1 230 ? 73.762  50.395  -39.715 1.00 97.14  ? 230 SER C CA  1 
ATOM   10340 C C   . SER C 1 230 ? 72.838  50.961  -40.791 1.00 97.37  ? 230 SER C C   1 
ATOM   10341 O O   . SER C 1 230 ? 72.352  50.219  -41.641 1.00 95.60  ? 230 SER C O   1 
ATOM   10342 C CB  . SER C 1 230 ? 75.171  50.253  -40.233 1.00 97.06  ? 230 SER C CB  1 
ATOM   10343 O OG  . SER C 1 230 ? 75.217  49.474  -41.420 1.00 94.78  ? 230 SER C OG  1 
ATOM   10344 N N   . PRO C 1 231 ? 72.550  52.282  -40.813 1.00 100.06 ? 231 PRO C N   1 
ATOM   10345 C CA  . PRO C 1 231 ? 71.828  52.866  -41.945 1.00 100.65 ? 231 PRO C CA  1 
ATOM   10346 C C   . PRO C 1 231 ? 72.326  52.359  -43.304 1.00 99.13  ? 231 PRO C C   1 
ATOM   10347 O O   . PRO C 1 231 ? 71.549  52.210  -44.242 1.00 98.40  ? 231 PRO C O   1 
ATOM   10348 C CB  . PRO C 1 231 ? 72.041  54.384  -41.733 1.00 104.10 ? 231 PRO C CB  1 
ATOM   10349 C CG  . PRO C 1 231 ? 72.152  54.533  -40.224 1.00 105.27 ? 231 PRO C CG  1 
ATOM   10350 C CD  . PRO C 1 231 ? 72.853  53.266  -39.756 1.00 102.94 ? 231 PRO C CD  1 
ATOM   10351 N N   . GLU C 1 232 ? 73.623  52.063  -43.411 1.00 98.96  ? 232 GLU C N   1 
ATOM   10352 C CA  . GLU C 1 232 ? 74.197  51.665  -44.684 1.00 98.07  ? 232 GLU C CA  1 
ATOM   10353 C C   . GLU C 1 232 ? 75.615  51.162  -44.460 1.00 97.89  ? 232 GLU C C   1 
ATOM   10354 O O   . GLU C 1 232 ? 76.039  50.966  -43.322 1.00 97.93  ? 232 GLU C O   1 
ATOM   10355 C CB  . GLU C 1 232 ? 74.176  52.840  -45.669 1.00 100.55 ? 232 GLU C CB  1 
ATOM   10356 C CG  . GLU C 1 232 ? 75.024  54.045  -45.248 1.00 103.49 ? 232 GLU C CG  1 
ATOM   10357 C CD  . GLU C 1 232 ? 75.195  55.108  -46.321 1.00 105.32 ? 232 GLU C CD  1 
ATOM   10358 O OE1 . GLU C 1 232 ? 76.077  54.977  -47.194 1.00 105.05 ? 232 GLU C OE1 1 
ATOM   10359 O OE2 . GLU C 1 232 ? 74.406  56.061  -46.298 1.00 107.16 ? 232 GLU C OE2 1 
ATOM   10360 N N   . GLY C 1 233 ? 76.333  50.944  -45.564 1.00 98.21  ? 233 GLY C N   1 
ATOM   10361 C CA  . GLY C 1 233 ? 77.711  50.487  -45.495 1.00 98.77  ? 233 GLY C CA  1 
ATOM   10362 C C   . GLY C 1 233 ? 77.792  49.013  -45.114 1.00 96.62  ? 233 GLY C C   1 
ATOM   10363 O O   . GLY C 1 233 ? 76.889  48.503  -44.449 1.00 95.37  ? 233 GLY C O   1 
ATOM   10364 N N   . GLY C 1 234 ? 78.891  48.361  -45.538 1.00 97.15  ? 234 GLY C N   1 
ATOM   10365 C CA  . GLY C 1 234 ? 79.059  46.914  -45.418 1.00 95.39  ? 234 GLY C CA  1 
ATOM   10366 C C   . GLY C 1 234 ? 78.811  46.220  -46.758 1.00 94.75  ? 234 GLY C C   1 
ATOM   10367 O O   . GLY C 1 234 ? 78.976  46.840  -47.807 1.00 96.70  ? 234 GLY C O   1 
ATOM   10368 N N   . ASN C 1 235 ? 78.410  44.941  -46.716 1.00 93.28  ? 235 ASN C N   1 
ATOM   10369 C CA  . ASN C 1 235 ? 78.064  44.184  -47.915 1.00 92.25  ? 235 ASN C CA  1 
ATOM   10370 C C   . ASN C 1 235 ? 77.049  43.096  -47.563 1.00 87.57  ? 235 ASN C C   1 
ATOM   10371 O O   . ASN C 1 235 ? 77.106  42.531  -46.480 1.00 85.41  ? 235 ASN C O   1 
ATOM   10372 C CB  . ASN C 1 235 ? 79.303  43.601  -48.590 1.00 94.30  ? 235 ASN C CB  1 
ATOM   10373 C CG  . ASN C 1 235 ? 78.942  42.828  -49.835 1.00 95.67  ? 235 ASN C CG  1 
ATOM   10374 O OD1 . ASN C 1 235 ? 78.174  43.327  -50.665 1.00 97.74  ? 235 ASN C OD1 1 
ATOM   10375 N ND2 . ASN C 1 235 ? 79.452  41.611  -49.970 1.00 96.06  ? 235 ASN C ND2 1 
ATOM   10376 N N   . GLY C 1 236 ? 76.115  42.828  -48.483 1.00 85.71  ? 236 GLY C N   1 
ATOM   10377 C CA  . GLY C 1 236 ? 74.975  41.962  -48.224 1.00 83.19  ? 236 GLY C CA  1 
ATOM   10378 C C   . GLY C 1 236 ? 74.497  42.084  -46.779 1.00 82.93  ? 236 GLY C C   1 
ATOM   10379 O O   . GLY C 1 236 ? 74.078  43.145  -46.344 1.00 85.24  ? 236 GLY C O   1 
ATOM   10380 N N   . GLN C 1 237 ? 74.635  41.000  -46.016 1.00 81.84  ? 237 GLN C N   1 
ATOM   10381 C CA  . GLN C 1 237 ? 74.052  40.886  -44.689 1.00 81.75  ? 237 GLN C CA  1 
ATOM   10382 C C   . GLN C 1 237 ? 74.957  41.454  -43.599 1.00 83.81  ? 237 GLN C C   1 
ATOM   10383 O O   . GLN C 1 237 ? 74.548  41.559  -42.438 1.00 83.77  ? 237 GLN C O   1 
ATOM   10384 C CB  . GLN C 1 237 ? 73.774  39.405  -44.479 1.00 79.70  ? 237 GLN C CB  1 
ATOM   10385 C CG  . GLN C 1 237 ? 72.662  38.900  -45.394 1.00 78.50  ? 237 GLN C CG  1 
ATOM   10386 C CD  . GLN C 1 237 ? 72.157  37.542  -44.987 1.00 76.24  ? 237 GLN C CD  1 
ATOM   10387 O OE1 . GLN C 1 237 ? 71.682  37.370  -43.861 1.00 76.07  ? 237 GLN C OE1 1 
ATOM   10388 N NE2 . GLN C 1 237 ? 72.291  36.579  -45.888 1.00 75.01  ? 237 GLN C NE2 1 
ATOM   10389 N N   . TYR C 1 238 ? 76.195  41.791  -43.980 1.00 85.29  ? 238 TYR C N   1 
ATOM   10390 C CA  . TYR C 1 238 ? 77.120  42.450  -43.079 1.00 86.75  ? 238 TYR C CA  1 
ATOM   10391 C C   . TYR C 1 238 ? 76.767  43.936  -43.096 1.00 87.80  ? 238 TYR C C   1 
ATOM   10392 O O   . TYR C 1 238 ? 77.072  44.649  -44.049 1.00 88.46  ? 238 TYR C O   1 
ATOM   10393 C CB  . TYR C 1 238 ? 78.567  42.094  -43.461 1.00 87.73  ? 238 TYR C CB  1 
ATOM   10394 C CG  . TYR C 1 238 ? 79.570  42.894  -42.640 1.00 90.03  ? 238 TYR C CG  1 
ATOM   10395 C CD1 . TYR C 1 238 ? 79.857  42.539  -41.327 1.00 90.57  ? 238 TYR C CD1 1 
ATOM   10396 C CD2 . TYR C 1 238 ? 80.156  44.045  -43.148 1.00 92.00  ? 238 TYR C CD2 1 
ATOM   10397 C CE1 . TYR C 1 238 ? 80.722  43.291  -40.551 1.00 92.72  ? 238 TYR C CE1 1 
ATOM   10398 C CE2 . TYR C 1 238 ? 81.027  44.800  -42.384 1.00 94.29  ? 238 TYR C CE2 1 
ATOM   10399 C CZ  . TYR C 1 238 ? 81.312  44.421  -41.084 1.00 94.58  ? 238 TYR C CZ  1 
ATOM   10400 O OH  . TYR C 1 238 ? 82.157  45.164  -40.316 1.00 97.42  ? 238 TYR C OH  1 
ATOM   10401 N N   . GLY C 1 239 ? 76.075  44.386  -42.048 1.00 88.28  ? 239 GLY C N   1 
ATOM   10402 C CA  . GLY C 1 239 ? 75.590  45.758  -41.981 1.00 90.06  ? 239 GLY C CA  1 
ATOM   10403 C C   . GLY C 1 239 ? 74.299  45.949  -42.780 1.00 89.14  ? 239 GLY C C   1 
ATOM   10404 O O   . GLY C 1 239 ? 73.798  45.003  -43.389 1.00 87.22  ? 239 GLY C O   1 
ATOM   10405 N N   . SER C 1 240 ? 73.753  47.175  -42.723 1.00 90.57  ? 240 SER C N   1 
ATOM   10406 C CA  . SER C 1 240 ? 72.579  47.592  -43.487 1.00 90.77  ? 240 SER C CA  1 
ATOM   10407 C C   . SER C 1 240 ? 71.360  46.665  -43.312 1.00 89.19  ? 240 SER C C   1 
ATOM   10408 O O   . SER C 1 240 ? 70.597  46.482  -44.262 1.00 87.69  ? 240 SER C O   1 
ATOM   10409 C CB  . SER C 1 240 ? 72.915  47.727  -44.959 1.00 90.17  ? 240 SER C CB  1 
ATOM   10410 O OG  . SER C 1 240 ? 74.123  48.431  -45.162 1.00 91.29  ? 240 SER C OG  1 
ATOM   10411 N N   . ASN C 1 241 ? 71.143  46.107  -42.109 1.00 89.20  ? 241 ASN C N   1 
ATOM   10412 C CA  . ASN C 1 241 ? 69.966  45.292  -41.834 1.00 88.14  ? 241 ASN C CA  1 
ATOM   10413 C C   . ASN C 1 241 ? 68.863  46.142  -41.210 1.00 90.04  ? 241 ASN C C   1 
ATOM   10414 O O   . ASN C 1 241 ? 69.135  47.223  -40.682 1.00 92.92  ? 241 ASN C O   1 
ATOM   10415 C CB  . ASN C 1 241 ? 70.289  44.135  -40.904 1.00 87.49  ? 241 ASN C CB  1 
ATOM   10416 C CG  . ASN C 1 241 ? 71.116  43.081  -41.599 1.00 86.23  ? 241 ASN C CG  1 
ATOM   10417 O OD1 . ASN C 1 241 ? 70.571  42.213  -42.292 1.00 84.65  ? 241 ASN C OD1 1 
ATOM   10418 N ND2 . ASN C 1 241 ? 72.425  43.129  -41.416 1.00 87.33  ? 241 ASN C ND2 1 
ATOM   10419 N N   . THR C 1 242 ? 67.612  45.660  -41.278 1.00 88.07  ? 242 THR C N   1 
ATOM   10420 C CA  . THR C 1 242 ? 66.531  46.317  -40.552 1.00 88.62  ? 242 THR C CA  1 
ATOM   10421 C C   . THR C 1 242 ? 66.458  45.715  -39.150 1.00 87.42  ? 242 THR C C   1 
ATOM   10422 O O   . THR C 1 242 ? 67.117  44.697  -38.884 1.00 85.48  ? 242 THR C O   1 
ATOM   10423 C CB  . THR C 1 242 ? 65.216  46.186  -41.310 1.00 88.30  ? 242 THR C CB  1 
ATOM   10424 O OG1 . THR C 1 242 ? 65.148  44.813  -41.682 1.00 87.10  ? 242 THR C OG1 1 
ATOM   10425 C CG2 . THR C 1 242 ? 65.180  47.033  -42.567 1.00 89.12  ? 242 THR C CG2 1 
ATOM   10426 N N   . LEU C 1 243 ? 65.676  46.367  -38.270 1.00 88.08  ? 243 LEU C N   1 
ATOM   10427 C CA  . LEU C 1 243 ? 65.532  45.942  -36.884 1.00 88.18  ? 243 LEU C CA  1 
ATOM   10428 C C   . LEU C 1 243 ? 64.884  44.559  -36.854 1.00 85.89  ? 243 LEU C C   1 
ATOM   10429 O O   . LEU C 1 243 ? 65.156  43.763  -35.946 1.00 85.56  ? 243 LEU C O   1 
ATOM   10430 C CB  . LEU C 1 243 ? 64.686  46.902  -36.053 1.00 90.75  ? 243 LEU C CB  1 
ATOM   10431 C CG  . LEU C 1 243 ? 65.285  48.255  -35.643 1.00 93.73  ? 243 LEU C CG  1 
ATOM   10432 C CD1 . LEU C 1 243 ? 66.665  48.123  -35.007 1.00 93.83  ? 243 LEU C CD1 1 
ATOM   10433 C CD2 . LEU C 1 243 ? 65.308  49.257  -36.791 1.00 94.61  ? 243 LEU C CD2 1 
ATOM   10434 N N   . LYS C 1 244 ? 64.005  44.328  -37.849 1.00 84.23  ? 244 LYS C N   1 
ATOM   10435 C CA  . LYS C 1 244 ? 63.337  43.059  -38.071 1.00 81.68  ? 244 LYS C CA  1 
ATOM   10436 C C   . LYS C 1 244 ? 64.347  41.965  -38.416 1.00 79.69  ? 244 LYS C C   1 
ATOM   10437 O O   . LYS C 1 244 ? 64.298  40.883  -37.846 1.00 78.58  ? 244 LYS C O   1 
ATOM   10438 C CB  . LYS C 1 244 ? 62.312  43.159  -39.208 1.00 80.75  ? 244 LYS C CB  1 
ATOM   10439 C CG  . LYS C 1 244 ? 61.520  41.864  -39.421 1.00 78.57  ? 244 LYS C CG  1 
ATOM   10440 C CD  . LYS C 1 244 ? 60.490  41.852  -40.546 1.00 77.89  ? 244 LYS C CD  1 
ATOM   10441 C CE  . LYS C 1 244 ? 59.964  40.492  -40.974 1.00 75.79  ? 244 LYS C CE  1 
ATOM   10442 N NZ  . LYS C 1 244 ? 59.647  39.563  -39.880 1.00 75.29  ? 244 LYS C NZ  1 
ATOM   10443 N N   . GLN C 1 245 ? 65.229  42.239  -39.379 1.00 79.33  ? 245 GLN C N   1 
ATOM   10444 C CA  . GLN C 1 245 ? 66.138  41.233  -39.900 1.00 77.60  ? 245 GLN C CA  1 
ATOM   10445 C C   . GLN C 1 245 ? 67.192  40.831  -38.873 1.00 78.03  ? 245 GLN C C   1 
ATOM   10446 O O   . GLN C 1 245 ? 67.686  39.690  -38.896 1.00 76.49  ? 245 GLN C O   1 
ATOM   10447 C CB  . GLN C 1 245 ? 66.830  41.748  -41.155 1.00 77.35  ? 245 GLN C CB  1 
ATOM   10448 C CG  . GLN C 1 245 ? 65.875  41.895  -42.326 1.00 77.04  ? 245 GLN C CG  1 
ATOM   10449 C CD  . GLN C 1 245 ? 66.554  42.505  -43.520 1.00 77.57  ? 245 GLN C CD  1 
ATOM   10450 O OE1 . GLN C 1 245 ? 67.313  43.470  -43.377 1.00 80.18  ? 245 GLN C OE1 1 
ATOM   10451 N NE2 . GLN C 1 245 ? 66.298  41.953  -44.695 1.00 76.21  ? 245 GLN C NE2 1 
ATOM   10452 N N   . GLN C 1 246 ? 67.545  41.788  -38.008 1.00 80.37  ? 246 GLN C N   1 
ATOM   10453 C CA  . GLN C 1 246 ? 68.485  41.529  -36.932 1.00 81.31  ? 246 GLN C CA  1 
ATOM   10454 C C   . GLN C 1 246 ? 67.795  40.561  -35.980 1.00 81.33  ? 246 GLN C C   1 
ATOM   10455 O O   . GLN C 1 246 ? 68.276  39.452  -35.787 1.00 80.50  ? 246 GLN C O   1 
ATOM   10456 C CB  . GLN C 1 246 ? 68.912  42.857  -36.309 1.00 83.91  ? 246 GLN C CB  1 
ATOM   10457 C CG  . GLN C 1 246 ? 69.967  42.772  -35.210 1.00 84.69  ? 246 GLN C CG  1 
ATOM   10458 C CD  . GLN C 1 246 ? 69.893  43.943  -34.244 1.00 87.37  ? 246 GLN C CD  1 
ATOM   10459 O OE1 . GLN C 1 246 ? 68.999  44.793  -34.332 1.00 88.35  ? 246 GLN C OE1 1 
ATOM   10460 N NE2 . GLN C 1 246 ? 70.788  43.973  -33.266 1.00 88.55  ? 246 GLN C NE2 1 
ATOM   10461 N N   . SER C 1 247 ? 66.618  40.950  -35.479 1.00 82.86  ? 247 SER C N   1 
ATOM   10462 C CA  . SER C 1 247 ? 65.804  40.067  -34.653 1.00 82.91  ? 247 SER C CA  1 
ATOM   10463 C C   . SER C 1 247 ? 65.744  38.677  -35.290 1.00 80.54  ? 247 SER C C   1 
ATOM   10464 O O   . SER C 1 247 ? 66.284  37.695  -34.766 1.00 79.77  ? 247 SER C O   1 
ATOM   10465 C CB  . SER C 1 247 ? 64.413  40.654  -34.450 1.00 84.24  ? 247 SER C CB  1 
ATOM   10466 O OG  . SER C 1 247 ? 63.750  40.041  -33.353 1.00 85.06  ? 247 SER C OG  1 
ATOM   10467 N N   . ASP C 1 248 ? 65.149  38.633  -36.482 1.00 79.31  ? 248 ASP C N   1 
ATOM   10468 C CA  . ASP C 1 248 ? 64.837  37.386  -37.138 1.00 77.43  ? 248 ASP C CA  1 
ATOM   10469 C C   . ASP C 1 248 ? 66.088  36.559  -37.345 1.00 76.69  ? 248 ASP C C   1 
ATOM   10470 O O   . ASP C 1 248 ? 65.996  35.328  -37.274 1.00 75.94  ? 248 ASP C O   1 
ATOM   10471 C CB  . ASP C 1 248 ? 64.084  37.633  -38.424 1.00 76.59  ? 248 ASP C CB  1 
ATOM   10472 C CG  . ASP C 1 248 ? 62.622  37.955  -38.175 1.00 77.39  ? 248 ASP C CG  1 
ATOM   10473 O OD1 . ASP C 1 248 ? 62.202  37.908  -36.984 1.00 77.91  ? 248 ASP C OD1 1 
ATOM   10474 O OD2 . ASP C 1 248 ? 61.935  38.269  -39.164 1.00 77.30  ? 248 ASP C OD2 1 
ATOM   10475 N N   . GLY C 1 249 ? 67.207  37.254  -37.619 1.00 77.29  ? 249 GLY C N   1 
ATOM   10476 C CA  . GLY C 1 249 ? 68.474  36.609  -37.919 1.00 76.24  ? 249 GLY C CA  1 
ATOM   10477 C C   . GLY C 1 249 ? 69.090  35.987  -36.671 1.00 76.42  ? 249 GLY C C   1 
ATOM   10478 O O   . GLY C 1 249 ? 69.516  34.839  -36.708 1.00 74.95  ? 249 GLY C O   1 
ATOM   10479 N N   . LEU C 1 250 ? 69.112  36.750  -35.569 1.00 78.37  ? 250 LEU C N   1 
ATOM   10480 C CA  . LEU C 1 250 ? 69.661  36.277  -34.306 1.00 79.48  ? 250 LEU C CA  1 
ATOM   10481 C C   . LEU C 1 250 ? 69.037  34.933  -33.959 1.00 78.50  ? 250 LEU C C   1 
ATOM   10482 O O   . LEU C 1 250 ? 69.744  34.011  -33.583 1.00 78.27  ? 250 LEU C O   1 
ATOM   10483 C CB  . LEU C 1 250 ? 69.469  37.259  -33.148 1.00 81.94  ? 250 LEU C CB  1 
ATOM   10484 C CG  . LEU C 1 250 ? 70.646  38.183  -32.810 1.00 83.70  ? 250 LEU C CG  1 
ATOM   10485 C CD1 . LEU C 1 250 ? 71.870  37.398  -32.353 1.00 83.43  ? 250 LEU C CD1 1 
ATOM   10486 C CD2 . LEU C 1 250 ? 71.021  39.083  -33.973 1.00 83.84  ? 250 LEU C CD2 1 
ATOM   10487 N N   . ILE C 1 251 ? 67.712  34.855  -34.079 1.00 78.64  ? 251 ILE C N   1 
ATOM   10488 C CA  . ILE C 1 251 ? 66.957  33.664  -33.728 1.00 77.97  ? 251 ILE C CA  1 
ATOM   10489 C C   . ILE C 1 251 ? 67.314  32.556  -34.706 1.00 76.87  ? 251 ILE C C   1 
ATOM   10490 O O   . ILE C 1 251 ? 67.521  31.414  -34.300 1.00 77.15  ? 251 ILE C O   1 
ATOM   10491 C CB  . ILE C 1 251 ? 65.445  33.976  -33.708 1.00 77.72  ? 251 ILE C CB  1 
ATOM   10492 C CG1 . ILE C 1 251 ? 65.125  35.055  -32.657 1.00 79.44  ? 251 ILE C CG1 1 
ATOM   10493 C CG2 . ILE C 1 251 ? 64.594  32.716  -33.520 1.00 76.85  ? 251 ILE C CG2 1 
ATOM   10494 C CD1 . ILE C 1 251 ? 65.551  34.740  -31.230 1.00 80.57  ? 251 ILE C CD1 1 
ATOM   10495 N N   . SER C 1 252 ? 67.411  32.919  -35.988 1.00 76.83  ? 252 SER C N   1 
ATOM   10496 C CA  . SER C 1 252 ? 67.747  31.956  -37.025 1.00 76.89  ? 252 SER C CA  1 
ATOM   10497 C C   . SER C 1 252 ? 69.121  31.319  -36.770 1.00 76.16  ? 252 SER C C   1 
ATOM   10498 O O   . SER C 1 252 ? 69.305  30.124  -36.989 1.00 74.45  ? 252 SER C O   1 
ATOM   10499 C CB  . SER C 1 252 ? 67.658  32.599  -38.392 1.00 77.30  ? 252 SER C CB  1 
ATOM   10500 O OG  . SER C 1 252 ? 67.548  31.621  -39.423 1.00 77.28  ? 252 SER C OG  1 
ATOM   10501 N N   . ASN C 1 253 ? 70.070  32.125  -36.285 1.00 77.45  ? 253 ASN C N   1 
ATOM   10502 C CA  . ASN C 1 253 ? 71.409  31.667  -35.938 1.00 78.29  ? 253 ASN C CA  1 
ATOM   10503 C C   . ASN C 1 253 ? 71.387  30.779  -34.690 1.00 78.89  ? 253 ASN C C   1 
ATOM   10504 O O   . ASN C 1 253 ? 72.116  29.790  -34.635 1.00 77.86  ? 253 ASN C O   1 
ATOM   10505 C CB  . ASN C 1 253 ? 72.355  32.840  -35.678 1.00 79.64  ? 253 ASN C CB  1 
ATOM   10506 C CG  . ASN C 1 253 ? 72.719  33.648  -36.903 1.00 79.01  ? 253 ASN C CG  1 
ATOM   10507 O OD1 . ASN C 1 253 ? 73.358  34.696  -36.751 1.00 79.36  ? 253 ASN C OD1 1 
ATOM   10508 N ND2 . ASN C 1 253 ? 72.359  33.188  -38.097 1.00 78.04  ? 253 ASN C ND2 1 
ATOM   10509 N N   . TYR C 1 254 ? 70.578  31.165  -33.686 1.00 79.98  ? 254 TYR C N   1 
ATOM   10510 C CA  . TYR C 1 254 ? 70.566  30.511  -32.381 1.00 80.81  ? 254 TYR C CA  1 
ATOM   10511 C C   . TYR C 1 254 ? 70.190  29.051  -32.583 1.00 79.82  ? 254 TYR C C   1 
ATOM   10512 O O   . TYR C 1 254 ? 70.794  28.171  -31.978 1.00 81.09  ? 254 TYR C O   1 
ATOM   10513 C CB  . TYR C 1 254 ? 69.584  31.090  -31.351 1.00 81.72  ? 254 TYR C CB  1 
ATOM   10514 C CG  . TYR C 1 254 ? 70.004  31.015  -29.884 1.00 82.96  ? 254 TYR C CG  1 
ATOM   10515 C CD1 . TYR C 1 254 ? 69.957  29.826  -29.167 1.00 83.05  ? 254 TYR C CD1 1 
ATOM   10516 C CD2 . TYR C 1 254 ? 70.411  32.153  -29.198 1.00 84.45  ? 254 TYR C CD2 1 
ATOM   10517 C CE1 . TYR C 1 254 ? 70.332  29.766  -27.831 1.00 84.89  ? 254 TYR C CE1 1 
ATOM   10518 C CE2 . TYR C 1 254 ? 70.793  32.108  -27.866 1.00 86.31  ? 254 TYR C CE2 1 
ATOM   10519 C CZ  . TYR C 1 254 ? 70.741  30.914  -27.174 1.00 86.50  ? 254 TYR C CZ  1 
ATOM   10520 O OH  . TYR C 1 254 ? 71.120  30.903  -25.858 1.00 88.59  ? 254 TYR C OH  1 
ATOM   10521 N N   . ARG C 1 255 ? 69.196  28.827  -33.447 1.00 78.36  ? 255 ARG C N   1 
ATOM   10522 C CA  . ARG C 1 255 ? 68.701  27.494  -33.741 1.00 76.99  ? 255 ARG C CA  1 
ATOM   10523 C C   . ARG C 1 255 ? 69.766  26.713  -34.504 1.00 76.82  ? 255 ARG C C   1 
ATOM   10524 O O   . ARG C 1 255 ? 70.029  25.557  -34.161 1.00 77.61  ? 255 ARG C O   1 
ATOM   10525 C CB  . ARG C 1 255 ? 67.397  27.554  -34.546 1.00 75.30  ? 255 ARG C CB  1 
ATOM   10526 C CG  . ARG C 1 255 ? 67.043  26.287  -35.320 1.00 73.69  ? 255 ARG C CG  1 
ATOM   10527 C CD  . ARG C 1 255 ? 66.336  25.203  -34.504 1.00 73.96  ? 255 ARG C CD  1 
ATOM   10528 N NE  . ARG C 1 255 ? 67.185  24.331  -33.677 1.00 73.99  ? 255 ARG C NE  1 
ATOM   10529 C CZ  . ARG C 1 255 ? 66.964  24.037  -32.391 1.00 75.19  ? 255 ARG C CZ  1 
ATOM   10530 N NH1 . ARG C 1 255 ? 65.904  24.506  -31.730 1.00 76.67  ? 255 ARG C NH1 1 
ATOM   10531 N NH2 . ARG C 1 255 ? 67.803  23.249  -31.762 1.00 75.20  ? 255 ARG C NH2 1 
ATOM   10532 N N   . ASP C 1 256 ? 70.353  27.347  -35.537 1.00 76.33  ? 256 ASP C N   1 
ATOM   10533 C CA  . ASP C 1 256 ? 71.347  26.695  -36.384 1.00 75.25  ? 256 ASP C CA  1 
ATOM   10534 C C   . ASP C 1 256 ? 72.512  26.171  -35.542 1.00 74.90  ? 256 ASP C C   1 
ATOM   10535 O O   . ASP C 1 256 ? 72.845  24.996  -35.634 1.00 75.12  ? 256 ASP C O   1 
ATOM   10536 C CB  . ASP C 1 256 ? 71.773  27.567  -37.557 1.00 74.56  ? 256 ASP C CB  1 
ATOM   10537 C CG  . ASP C 1 256 ? 70.737  27.745  -38.660 1.00 74.06  ? 256 ASP C CG  1 
ATOM   10538 O OD1 . ASP C 1 256 ? 69.529  27.665  -38.359 1.00 73.80  ? 256 ASP C OD1 1 
ATOM   10539 O OD2 . ASP C 1 256 ? 71.152  27.915  -39.823 1.00 74.00  ? 256 ASP C OD2 1 
ATOM   10540 N N   . LEU C 1 257 ? 73.075  27.018  -34.675 1.00 75.32  ? 257 LEU C N   1 
ATOM   10541 C CA  . LEU C 1 257 ? 74.333  26.719  -34.002 1.00 76.04  ? 257 LEU C CA  1 
ATOM   10542 C C   . LEU C 1 257 ? 74.150  25.612  -32.964 1.00 76.29  ? 257 LEU C C   1 
ATOM   10543 O O   . LEU C 1 257 ? 75.068  24.825  -32.720 1.00 74.90  ? 257 LEU C O   1 
ATOM   10544 C CB  . LEU C 1 257 ? 74.886  28.009  -33.388 1.00 76.96  ? 257 LEU C CB  1 
ATOM   10545 C CG  . LEU C 1 257 ? 75.264  29.093  -34.403 1.00 76.07  ? 257 LEU C CG  1 
ATOM   10546 C CD1 . LEU C 1 257 ? 75.554  30.420  -33.767 1.00 77.35  ? 257 LEU C CD1 1 
ATOM   10547 C CD2 . LEU C 1 257 ? 76.440  28.617  -35.211 1.00 75.54  ? 257 LEU C CD2 1 
ATOM   10548 N N   . ILE C 1 258 ? 72.958  25.571  -32.360 1.00 77.17  ? 258 ILE C N   1 
ATOM   10549 C CA  . ILE C 1 258 ? 72.588  24.453  -31.510 1.00 78.84  ? 258 ILE C CA  1 
ATOM   10550 C C   . ILE C 1 258 ? 72.556  23.183  -32.365 1.00 78.05  ? 258 ILE C C   1 
ATOM   10551 O O   . ILE C 1 258 ? 73.180  22.169  -31.997 1.00 77.86  ? 258 ILE C O   1 
ATOM   10552 C CB  . ILE C 1 258 ? 71.244  24.700  -30.800 1.00 80.05  ? 258 ILE C CB  1 
ATOM   10553 C CG1 . ILE C 1 258 ? 71.319  25.865  -29.816 1.00 82.42  ? 258 ILE C CG1 1 
ATOM   10554 C CG2 . ILE C 1 258 ? 70.775  23.431  -30.093 1.00 80.97  ? 258 ILE C CG2 1 
ATOM   10555 C CD1 . ILE C 1 258 ? 69.989  26.209  -29.159 1.00 83.35  ? 258 ILE C CD1 1 
ATOM   10556 N N   . ASP C 1 259 ? 71.850  23.281  -33.513 1.00 76.48  ? 259 ASP C N   1 
ATOM   10557 C CA  . ASP C 1 259 ? 71.704  22.186  -34.465 1.00 75.31  ? 259 ASP C CA  1 
ATOM   10558 C C   . ASP C 1 259 ? 73.068  21.636  -34.885 1.00 74.98  ? 259 ASP C C   1 
ATOM   10559 O O   . ASP C 1 259 ? 73.134  20.490  -35.339 1.00 75.15  ? 259 ASP C O   1 
ATOM   10560 C CB  . ASP C 1 259 ? 70.911  22.589  -35.700 1.00 73.86  ? 259 ASP C CB  1 
ATOM   10561 C CG  . ASP C 1 259 ? 69.445  22.894  -35.453 1.00 74.30  ? 259 ASP C CG  1 
ATOM   10562 O OD1 . ASP C 1 259 ? 68.922  22.436  -34.418 1.00 75.15  ? 259 ASP C OD1 1 
ATOM   10563 O OD2 . ASP C 1 259 ? 68.855  23.624  -36.277 1.00 73.83  ? 259 ASP C OD2 1 
ATOM   10564 N N   . ALA C 1 260 ? 74.129  22.456  -34.745 1.00 74.14  ? 260 ALA C N   1 
ATOM   10565 C CA  . ALA C 1 260 ? 75.484  22.082  -35.129 1.00 73.14  ? 260 ALA C CA  1 
ATOM   10566 C C   . ALA C 1 260 ? 76.322  21.627  -33.936 1.00 73.03  ? 260 ALA C C   1 
ATOM   10567 O O   . ALA C 1 260 ? 77.497  21.338  -34.117 1.00 72.47  ? 260 ALA C O   1 
ATOM   10568 C CB  . ALA C 1 260 ? 76.148  23.249  -35.827 1.00 73.06  ? 260 ALA C CB  1 
ATOM   10569 N N   . GLY C 1 261 ? 75.741  21.624  -32.729 1.00 73.47  ? 261 GLY C N   1 
ATOM   10570 C CA  . GLY C 1 261 ? 76.363  20.988  -31.579 1.00 74.73  ? 261 GLY C CA  1 
ATOM   10571 C C   . GLY C 1 261 ? 76.567  21.910  -30.373 1.00 76.33  ? 261 GLY C C   1 
ATOM   10572 O O   . GLY C 1 261 ? 76.903  21.424  -29.294 1.00 77.67  ? 261 GLY C O   1 
ATOM   10573 N N   . ALA C 1 262 ? 76.362  23.228  -30.525 1.00 76.35  ? 262 ALA C N   1 
ATOM   10574 C CA  . ALA C 1 262 ? 76.644  24.161  -29.441 1.00 77.66  ? 262 ALA C CA  1 
ATOM   10575 C C   . ALA C 1 262 ? 75.903  23.744  -28.173 1.00 79.09  ? 262 ALA C C   1 
ATOM   10576 O O   . ALA C 1 262 ? 74.732  23.366  -28.228 1.00 78.76  ? 262 ALA C O   1 
ATOM   10577 C CB  . ALA C 1 262 ? 76.277  25.570  -29.846 1.00 77.29  ? 262 ALA C CB  1 
ATOM   10578 N N   . VAL C 1 263 ? 76.616  23.777  -27.046 1.00 80.90  ? 263 VAL C N   1 
ATOM   10579 C CA  . VAL C 1 263 ? 76.002  23.642  -25.739 1.00 83.14  ? 263 VAL C CA  1 
ATOM   10580 C C   . VAL C 1 263 ? 76.324  24.894  -24.937 1.00 85.17  ? 263 VAL C C   1 
ATOM   10581 O O   . VAL C 1 263 ? 76.160  24.911  -23.717 1.00 87.38  ? 263 VAL C O   1 
ATOM   10582 C CB  . VAL C 1 263 ? 76.487  22.395  -24.985 1.00 84.79  ? 263 VAL C CB  1 
ATOM   10583 C CG1 . VAL C 1 263 ? 76.340  21.142  -25.838 1.00 83.62  ? 263 VAL C CG1 1 
ATOM   10584 C CG2 . VAL C 1 263 ? 77.931  22.559  -24.502 1.00 86.06  ? 263 VAL C CG2 1 
ATOM   10585 N N   . GLY C 1 264 ? 76.835  25.911  -25.637 1.00 84.86  ? 264 GLY C N   1 
ATOM   10586 C CA  . GLY C 1 264 ? 77.031  27.230  -25.064 1.00 86.99  ? 264 GLY C CA  1 
ATOM   10587 C C   . GLY C 1 264 ? 76.829  28.282  -26.148 1.00 86.12  ? 264 GLY C C   1 
ATOM   10588 O O   . GLY C 1 264 ? 77.182  28.047  -27.302 1.00 85.20  ? 264 GLY C O   1 
ATOM   10589 N N   . MET C 1 265 ? 76.229  29.419  -25.791 1.00 86.92  ? 265 MET C N   1 
ATOM   10590 C CA  . MET C 1 265 ? 75.902  30.400  -26.802 1.00 86.10  ? 265 MET C CA  1 
ATOM   10591 C C   . MET C 1 265 ? 76.216  31.802  -26.290 1.00 89.44  ? 265 MET C C   1 
ATOM   10592 O O   . MET C 1 265 ? 75.825  32.166  -25.184 1.00 91.89  ? 265 MET C O   1 
ATOM   10593 C CB  . MET C 1 265 ? 74.433  30.261  -27.189 1.00 84.39  ? 265 MET C CB  1 
ATOM   10594 C CG  . MET C 1 265 ? 74.100  28.934  -27.808 1.00 82.30  ? 265 MET C CG  1 
ATOM   10595 S SD  . MET C 1 265 ? 74.875  28.780  -29.426 1.00 80.13  ? 265 MET C SD  1 
ATOM   10596 C CE  . MET C 1 265 ? 73.759  29.741  -30.452 1.00 79.36  ? 265 MET C CE  1 
ATOM   10597 N N   . CYS C 1 266 ? 76.947  32.569  -27.109 1.00 90.11  ? 266 CYS C N   1 
ATOM   10598 C CA  . CYS C 1 266 ? 77.364  33.913  -26.751 1.00 92.89  ? 266 CYS C CA  1 
ATOM   10599 C C   . CYS C 1 266 ? 76.919  34.894  -27.834 1.00 92.66  ? 266 CYS C C   1 
ATOM   10600 O O   . CYS C 1 266 ? 77.768  35.402  -28.579 1.00 92.53  ? 266 CYS C O   1 
ATOM   10601 C CB  . CYS C 1 266 ? 78.872  33.985  -26.562 1.00 94.03  ? 266 CYS C CB  1 
ATOM   10602 S SG  . CYS C 1 266 ? 79.480  32.926  -25.227 1.00 96.53  ? 266 CYS C SG  1 
ATOM   10603 N N   . PRO C 1 267 ? 75.596  35.231  -27.955 1.00 91.35  ? 267 PRO C N   1 
ATOM   10604 C CA  . PRO C 1 267 ? 75.114  36.211  -28.924 1.00 90.34  ? 267 PRO C CA  1 
ATOM   10605 C C   . PRO C 1 267 ? 75.934  37.477  -28.916 1.00 92.18  ? 267 PRO C C   1 
ATOM   10606 O O   . PRO C 1 267 ? 76.464  37.876  -27.861 1.00 93.34  ? 267 PRO C O   1 
ATOM   10607 C CB  . PRO C 1 267 ? 73.647  36.463  -28.557 1.00 90.88  ? 267 PRO C CB  1 
ATOM   10608 C CG  . PRO C 1 267 ? 73.488  35.851  -27.202 1.00 92.45  ? 267 PRO C CG  1 
ATOM   10609 C CD  . PRO C 1 267 ? 74.430  34.673  -27.250 1.00 91.70  ? 267 PRO C CD  1 
ATOM   10610 N N   . PHE C 1 268 ? 75.959  38.185  -30.040 1.00 92.31  ? 268 PHE C N   1 
ATOM   10611 C CA  . PHE C 1 268 ? 76.912  39.324  -30.112 1.00 95.35  ? 268 PHE C CA  1 
ATOM   10612 C C   . PHE C 1 268 ? 76.390  40.677  -29.652 1.00 96.79  ? 268 PHE C C   1 
ATOM   10613 O O   . PHE C 1 268 ? 75.404  41.149  -30.247 1.00 94.93  ? 268 PHE C O   1 
ATOM   10614 C CB  . PHE C 1 268 ? 77.479  39.545  -31.519 1.00 95.24  ? 268 PHE C CB  1 
ATOM   10615 C CG  . PHE C 1 268 ? 78.656  40.509  -31.554 1.00 97.54  ? 268 PHE C CG  1 
ATOM   10616 C CD1 . PHE C 1 268 ? 79.652  40.454  -30.588 1.00 99.73  ? 268 PHE C CD1 1 
ATOM   10617 C CD2 . PHE C 1 268 ? 78.757  41.474  -32.547 1.00 98.68  ? 268 PHE C CD2 1 
ATOM   10618 C CE1 . PHE C 1 268 ? 80.715  41.338  -30.618 1.00 101.73 ? 268 PHE C CE1 1 
ATOM   10619 C CE2 . PHE C 1 268 ? 79.828  42.351  -32.575 1.00 101.43 ? 268 PHE C CE2 1 
ATOM   10620 C CZ  . PHE C 1 268 ? 80.803  42.281  -31.611 1.00 102.63 ? 268 PHE C CZ  1 
ATOM   10621 N N   . TYR C 1 269 ? 77.033  41.261  -28.633 1.00 99.64  ? 269 TYR C N   1 
ATOM   10622 C CA  . TYR C 1 269 ? 76.805  42.672  -28.210 1.00 101.62 ? 269 TYR C CA  1 
ATOM   10623 C C   . TYR C 1 269 ? 75.518  42.970  -27.470 1.00 101.50 ? 269 TYR C C   1 
ATOM   10624 O O   . TYR C 1 269 ? 74.422  42.702  -27.980 1.00 99.79  ? 269 TYR C O   1 
ATOM   10625 C CB  . TYR C 1 269 ? 76.964  43.591  -29.426 1.00 102.71 ? 269 TYR C CB  1 
ATOM   10626 C CG  . TYR C 1 269 ? 78.061  44.628  -29.247 1.00 105.82 ? 269 TYR C CG  1 
ATOM   10627 C CD1 . TYR C 1 269 ? 78.817  44.667  -28.083 1.00 108.00 ? 269 TYR C CD1 1 
ATOM   10628 C CD2 . TYR C 1 269 ? 78.336  45.563  -30.234 1.00 107.40 ? 269 TYR C CD2 1 
ATOM   10629 C CE1 . TYR C 1 269 ? 79.815  45.609  -27.907 1.00 111.88 ? 269 TYR C CE1 1 
ATOM   10630 C CE2 . TYR C 1 269 ? 79.331  46.511  -30.069 1.00 111.02 ? 269 TYR C CE2 1 
ATOM   10631 C CZ  . TYR C 1 269 ? 80.074  46.533  -28.903 1.00 112.98 ? 269 TYR C CZ  1 
ATOM   10632 O OH  . TYR C 1 269 ? 81.056  47.463  -28.727 1.00 115.17 ? 269 TYR C OH  1 
ATOM   10633 N N   . TYR C 1 270 ? 75.668  43.577  -26.291 1.00 103.13 ? 270 TYR C N   1 
ATOM   10634 C CA  . TYR C 1 270 ? 74.485  44.076  -25.551 1.00 104.62 ? 270 TYR C CA  1 
ATOM   10635 C C   . TYR C 1 270 ? 74.214  45.484  -26.071 1.00 105.83 ? 270 TYR C C   1 
ATOM   10636 O O   . TYR C 1 270 ? 73.038  45.854  -26.207 1.00 105.30 ? 270 TYR C O   1 
ATOM   10637 C CB  . TYR C 1 270 ? 74.768  44.074  -24.049 1.00 106.82 ? 270 TYR C CB  1 
ATOM   10638 C CG  . TYR C 1 270 ? 74.188  45.235  -23.251 1.00 109.51 ? 270 TYR C CG  1 
ATOM   10639 C CD1 . TYR C 1 270 ? 74.927  46.386  -23.013 1.00 111.75 ? 270 TYR C CD1 1 
ATOM   10640 C CD2 . TYR C 1 270 ? 72.911  45.168  -22.714 1.00 110.13 ? 270 TYR C CD2 1 
ATOM   10641 C CE1 . TYR C 1 270 ? 74.408  47.442  -22.284 1.00 115.00 ? 270 TYR C CE1 1 
ATOM   10642 C CE2 . TYR C 1 270 ? 72.383  46.213  -21.974 1.00 113.31 ? 270 TYR C CE2 1 
ATOM   10643 C CZ  . TYR C 1 270 ? 73.131  47.356  -21.764 1.00 115.74 ? 270 TYR C CZ  1 
ATOM   10644 O OH  . TYR C 1 270 ? 72.612  48.389  -21.041 1.00 118.94 ? 270 TYR C OH  1 
ATOM   10645 N N   . ALA C 1 271 ? 75.277  46.233  -26.396 1.00 107.45 ? 271 ALA C N   1 
ATOM   10646 C CA  . ALA C 1 271 ? 75.089  47.598  -26.866 1.00 109.78 ? 271 ALA C CA  1 
ATOM   10647 C C   . ALA C 1 271 ? 76.168  48.028  -27.860 1.00 109.53 ? 271 ALA C C   1 
ATOM   10648 O O   . ALA C 1 271 ? 77.318  47.599  -27.791 1.00 108.24 ? 271 ALA C O   1 
ATOM   10649 C CB  . ALA C 1 271 ? 75.034  48.552  -25.691 1.00 113.70 ? 271 ALA C CB  1 
ATOM   10650 N N   . ASP C 1 272 ? 75.757  48.943  -28.747 1.00 110.90 ? 272 ASP C N   1 
ATOM   10651 C CA  . ASP C 1 272 ? 76.604  49.541  -29.763 1.00 111.86 ? 272 ASP C CA  1 
ATOM   10652 C C   . ASP C 1 272 ? 77.858  50.158  -29.136 1.00 115.25 ? 272 ASP C C   1 
ATOM   10653 O O   . ASP C 1 272 ? 77.818  50.753  -28.052 1.00 118.27 ? 272 ASP C O   1 
ATOM   10654 C CB  . ASP C 1 272 ? 75.873  50.656  -30.501 1.00 113.02 ? 272 ASP C CB  1 
ATOM   10655 C CG  . ASP C 1 272 ? 74.659  50.266  -31.337 1.00 111.11 ? 272 ASP C CG  1 
ATOM   10656 O OD1 . ASP C 1 272 ? 74.531  49.069  -31.679 1.00 107.88 ? 272 ASP C OD1 1 
ATOM   10657 O OD2 . ASP C 1 272 ? 73.833  51.169  -31.624 1.00 112.81 ? 272 ASP C OD2 1 
ATOM   10658 N N   . GLY C 1 273 ? 78.971  50.042  -29.867 1.00 114.18 ? 273 GLY C N   1 
ATOM   10659 C CA  . GLY C 1 273 ? 80.146  50.849  -29.605 1.00 116.76 ? 273 GLY C CA  1 
ATOM   10660 C C   . GLY C 1 273 ? 80.327  51.858  -30.734 1.00 117.72 ? 273 GLY C C   1 
ATOM   10661 O O   . GLY C 1 273 ? 80.470  51.468  -31.891 1.00 114.77 ? 273 GLY C O   1 
ATOM   10662 N N   . TRP C 1 274 ? 80.303  53.153  -30.397 1.00 121.41 ? 274 TRP C N   1 
ATOM   10663 C CA  . TRP C 1 274 ? 80.492  54.192  -31.396 1.00 122.92 ? 274 TRP C CA  1 
ATOM   10664 C C   . TRP C 1 274 ? 81.959  54.322  -31.794 1.00 122.68 ? 274 TRP C C   1 
ATOM   10665 O O   . TRP C 1 274 ? 82.280  55.120  -32.672 1.00 122.60 ? 274 TRP C O   1 
ATOM   10666 C CB  . TRP C 1 274 ? 79.977  55.530  -30.860 1.00 127.61 ? 274 TRP C CB  1 
ATOM   10667 C CG  . TRP C 1 274 ? 78.485  55.582  -30.713 1.00 127.73 ? 274 TRP C CG  1 
ATOM   10668 C CD1 . TRP C 1 274 ? 77.615  54.556  -30.485 1.00 124.82 ? 274 TRP C CD1 1 
ATOM   10669 C CD2 . TRP C 1 274 ? 77.694  56.782  -30.789 1.00 130.57 ? 274 TRP C CD2 1 
ATOM   10670 N NE1 . TRP C 1 274 ? 76.334  55.038  -30.417 1.00 125.79 ? 274 TRP C NE1 1 
ATOM   10671 C CE2 . TRP C 1 274 ? 76.353  56.397  -30.598 1.00 129.19 ? 274 TRP C CE2 1 
ATOM   10672 C CE3 . TRP C 1 274 ? 77.994  58.131  -31.000 1.00 134.64 ? 274 TRP C CE3 1 
ATOM   10673 C CZ2 . TRP C 1 274 ? 75.315  57.324  -30.615 1.00 131.89 ? 274 TRP C CZ2 1 
ATOM   10674 C CZ3 . TRP C 1 274 ? 76.965  59.047  -31.014 1.00 137.10 ? 274 TRP C CZ3 1 
ATOM   10675 C CH2 . TRP C 1 274 ? 75.645  58.645  -30.819 1.00 135.55 ? 274 TRP C CH2 1 
ATOM   10676 N N   . TRP C 1 275 ? 82.822  53.542  -31.131 1.00 122.48 ? 275 TRP C N   1 
ATOM   10677 C CA  . TRP C 1 275 ? 84.266  53.611  -31.306 1.00 124.14 ? 275 TRP C CA  1 
ATOM   10678 C C   . TRP C 1 275 ? 84.756  52.647  -32.382 1.00 120.98 ? 275 TRP C C   1 
ATOM   10679 O O   . TRP C 1 275 ? 85.774  52.908  -33.026 1.00 120.85 ? 275 TRP C O   1 
ATOM   10680 C CB  . TRP C 1 275 ? 84.988  53.331  -29.977 1.00 125.90 ? 275 TRP C CB  1 
ATOM   10681 C CG  . TRP C 1 275 ? 84.804  51.944  -29.421 1.00 123.12 ? 275 TRP C CG  1 
ATOM   10682 C CD1 . TRP C 1 275 ? 83.836  51.532  -28.556 1.00 123.13 ? 275 TRP C CD1 1 
ATOM   10683 C CD2 . TRP C 1 275 ? 85.636  50.789  -29.668 1.00 121.00 ? 275 TRP C CD2 1 
ATOM   10684 N NE1 . TRP C 1 275 ? 83.991  50.203  -28.265 1.00 121.15 ? 275 TRP C NE1 1 
ATOM   10685 C CE2 . TRP C 1 275 ? 85.087  49.719  -28.926 1.00 119.50 ? 275 TRP C CE2 1 
ATOM   10686 C CE3 . TRP C 1 275 ? 86.779  50.549  -30.439 1.00 119.98 ? 275 TRP C CE3 1 
ATOM   10687 C CZ2 . TRP C 1 275 ? 85.644  48.442  -28.932 1.00 116.82 ? 275 TRP C CZ2 1 
ATOM   10688 C CZ3 . TRP C 1 275 ? 87.322  49.283  -30.450 1.00 117.20 ? 275 TRP C CZ3 1 
ATOM   10689 C CH2 . TRP C 1 275 ? 86.769  48.248  -29.697 1.00 115.60 ? 275 TRP C CH2 1 
ATOM   10690 N N   . LYS C 1 276 ? 84.025  51.543  -32.571 1.00 118.36 ? 276 LYS C N   1 
ATOM   10691 C CA  . LYS C 1 276 ? 84.514  50.438  -33.379 1.00 116.50 ? 276 LYS C CA  1 
ATOM   10692 C C   . LYS C 1 276 ? 84.701  50.891  -34.832 1.00 116.92 ? 276 LYS C C   1 
ATOM   10693 O O   . LYS C 1 276 ? 85.355  50.192  -35.601 1.00 116.36 ? 276 LYS C O   1 
ATOM   10694 C CB  . LYS C 1 276 ? 83.618  49.191  -33.265 1.00 113.60 ? 276 LYS C CB  1 
ATOM   10695 C CG  . LYS C 1 276 ? 83.413  48.572  -31.859 1.00 113.77 ? 276 LYS C CG  1 
ATOM   10696 C CD  . LYS C 1 276 ? 82.288  47.536  -31.708 1.00 110.86 ? 276 LYS C CD  1 
ATOM   10697 C CE  . LYS C 1 276 ? 82.689  46.088  -31.881 1.00 107.99 ? 276 LYS C CE  1 
ATOM   10698 N NZ  . LYS C 1 276 ? 83.483  45.528  -30.774 1.00 108.46 ? 276 LYS C NZ  1 
ATOM   10699 N N   . GLY C 1 277 ? 84.148  52.053  -35.215 1.00 118.77 ? 277 GLY C N   1 
ATOM   10700 C CA  . GLY C 1 277 ? 84.238  52.516  -36.590 1.00 119.08 ? 277 GLY C CA  1 
ATOM   10701 C C   . GLY C 1 277 ? 85.190  53.700  -36.775 1.00 123.50 ? 277 GLY C C   1 
ATOM   10702 O O   . GLY C 1 277 ? 85.068  54.422  -37.762 1.00 125.79 ? 277 GLY C O   1 
ATOM   10703 N N   . GLY C 1 278 ? 86.116  53.925  -35.831 1.00 124.83 ? 278 GLY C N   1 
ATOM   10704 C CA  . GLY C 1 278 ? 87.203  54.872  -36.048 1.00 127.45 ? 278 GLY C CA  1 
ATOM   10705 C C   . GLY C 1 278 ? 87.062  56.180  -35.262 1.00 131.34 ? 278 GLY C C   1 
ATOM   10706 O O   . GLY C 1 278 ? 88.080  56.809  -34.949 1.00 134.36 ? 278 GLY C O   1 
ATOM   10707 N N   . GLU C 1 279 ? 85.816  56.612  -34.991 1.00 130.67 ? 279 GLU C N   1 
ATOM   10708 C CA  . GLU C 1 279 ? 85.568  57.813  -34.203 1.00 133.62 ? 279 GLU C CA  1 
ATOM   10709 C C   . GLU C 1 279 ? 84.465  57.545  -33.176 1.00 133.33 ? 279 GLU C C   1 
ATOM   10710 O O   . GLU C 1 279 ? 83.336  57.182  -33.529 1.00 131.22 ? 279 GLU C O   1 
ATOM   10711 C CB  . GLU C 1 279 ? 85.264  58.999  -35.114 1.00 134.93 ? 279 GLU C CB  1 
ATOM   10712 C CG  . GLU C 1 279 ? 86.393  59.256  -36.103 1.00 135.24 ? 279 GLU C CG  1 
ATOM   10713 C CD  . GLU C 1 279 ? 86.288  60.609  -36.761 1.00 138.37 ? 279 GLU C CD  1 
ATOM   10714 O OE1 . GLU C 1 279 ? 85.172  60.941  -37.211 1.00 137.77 ? 279 GLU C OE1 1 
ATOM   10715 O OE2 . GLU C 1 279 ? 87.310  61.318  -36.817 1.00 141.12 ? 279 GLU C OE2 1 
ATOM   10716 N N   . LYS C 1 280 ? 84.824  57.760  -31.900 1.00 135.55 ? 280 LYS C N   1 
ATOM   10717 C CA  . LYS C 1 280 ? 84.063  57.288  -30.753 1.00 135.08 ? 280 LYS C CA  1 
ATOM   10718 C C   . LYS C 1 280 ? 83.015  58.298  -30.294 1.00 138.00 ? 280 LYS C C   1 
ATOM   10719 O O   . LYS C 1 280 ? 82.468  58.129  -29.207 1.00 138.93 ? 280 LYS C O   1 
ATOM   10720 C CB  . LYS C 1 280 ? 84.978  57.028  -29.548 1.00 136.54 ? 280 LYS C CB  1 
ATOM   10721 C CG  . LYS C 1 280 ? 85.634  58.279  -28.953 1.00 141.63 ? 280 LYS C CG  1 
ATOM   10722 C CD  . LYS C 1 280 ? 86.422  58.042  -27.670 1.00 143.27 ? 280 LYS C CD  1 
ATOM   10723 C CE  . LYS C 1 280 ? 86.854  59.304  -26.982 1.00 147.58 ? 280 LYS C CE  1 
ATOM   10724 N NZ  . LYS C 1 280 ? 87.146  59.031  -25.573 1.00 149.10 ? 280 LYS C NZ  1 
ATOM   10725 N N   . SER C 1 281 ? 82.769  59.355  -31.084 1.00 140.29 ? 281 SER C N   1 
ATOM   10726 C CA  . SER C 1 281 ? 81.711  60.320  -30.790 1.00 143.03 ? 281 SER C CA  1 
ATOM   10727 C C   . SER C 1 281 ? 80.783  60.514  -31.990 1.00 141.25 ? 281 SER C C   1 
ATOM   10728 O O   . SER C 1 281 ? 79.729  61.134  -31.851 1.00 142.72 ? 281 SER C O   1 
ATOM   10729 C CB  . SER C 1 281 ? 82.278  61.654  -30.340 1.00 148.84 ? 281 SER C CB  1 
ATOM   10730 O OG  . SER C 1 281 ? 82.849  61.600  -29.038 1.00 151.62 ? 281 SER C OG  1 
ATOM   10731 N N   . ASP C 1 282 ? 81.195  60.000  -33.158 1.00 138.76 ? 282 ASP C N   1 
ATOM   10732 C CA  . ASP C 1 282 ? 80.371  59.965  -34.353 1.00 137.09 ? 282 ASP C CA  1 
ATOM   10733 C C   . ASP C 1 282 ? 79.868  58.540  -34.545 1.00 133.26 ? 282 ASP C C   1 
ATOM   10734 O O   . ASP C 1 282 ? 80.634  57.648  -34.935 1.00 131.70 ? 282 ASP C O   1 
ATOM   10735 C CB  . ASP C 1 282 ? 81.145  60.432  -35.576 1.00 137.49 ? 282 ASP C CB  1 
ATOM   10736 C CG  . ASP C 1 282 ? 80.379  60.406  -36.891 1.00 135.54 ? 282 ASP C CG  1 
ATOM   10737 O OD1 . ASP C 1 282 ? 79.599  61.346  -37.128 1.00 137.45 ? 282 ASP C OD1 1 
ATOM   10738 O OD2 . ASP C 1 282 ? 80.556  59.434  -37.657 1.00 132.86 ? 282 ASP C OD2 1 
ATOM   10739 N N   . HIS C 1 283 ? 78.585  58.337  -34.225 1.00 133.13 ? 283 HIS C N   1 
ATOM   10740 C CA  . HIS C 1 283 ? 77.870  57.148  -34.659 1.00 129.32 ? 283 HIS C CA  1 
ATOM   10741 C C   . HIS C 1 283 ? 77.773  57.227  -36.178 1.00 127.15 ? 283 HIS C C   1 
ATOM   10742 O O   . HIS C 1 283 ? 77.058  58.070  -36.705 1.00 129.23 ? 283 HIS C O   1 
ATOM   10743 C CB  . HIS C 1 283 ? 76.477  57.077  -34.027 1.00 130.08 ? 283 HIS C CB  1 
ATOM   10744 C CG  . HIS C 1 283 ? 75.985  55.693  -33.804 1.00 128.48 ? 283 HIS C CG  1 
ATOM   10745 N ND1 . HIS C 1 283 ? 74.780  55.406  -33.191 1.00 129.61 ? 283 HIS C ND1 1 
ATOM   10746 C CD2 . HIS C 1 283 ? 76.515  54.521  -34.150 1.00 126.93 ? 283 HIS C CD2 1 
ATOM   10747 C CE1 . HIS C 1 283 ? 74.603  54.095  -33.157 1.00 126.12 ? 283 HIS C CE1 1 
ATOM   10748 N NE2 . HIS C 1 283 ? 75.646  53.538  -33.734 1.00 126.05 ? 283 HIS C NE2 1 
ATOM   10749 N N   . SER C 1 284 ? 78.549  56.408  -36.887 1.00 124.07 ? 284 SER C N   1 
ATOM   10750 C CA  . SER C 1 284 ? 78.636  56.550  -38.330 1.00 122.52 ? 284 SER C CA  1 
ATOM   10751 C C   . SER C 1 284 ? 77.414  55.887  -38.973 1.00 117.73 ? 284 SER C C   1 
ATOM   10752 O O   . SER C 1 284 ? 76.711  55.110  -38.333 1.00 114.68 ? 284 SER C O   1 
ATOM   10753 C CB  . SER C 1 284 ? 79.962  56.019  -38.839 1.00 121.96 ? 284 SER C CB  1 
ATOM   10754 O OG  . SER C 1 284 ? 80.299  56.527  -40.130 1.00 123.14 ? 284 SER C OG  1 
ATOM   10755 N N   . LEU C 1 285 ? 77.114  56.298  -40.208 1.00 116.73 ? 285 LEU C N   1 
ATOM   10756 C CA  . LEU C 1 285 ? 76.013  55.761  -40.985 1.00 113.60 ? 285 LEU C CA  1 
ATOM   10757 C C   . LEU C 1 285 ? 76.517  54.562  -41.782 1.00 111.16 ? 285 LEU C C   1 
ATOM   10758 O O   . LEU C 1 285 ? 75.759  53.623  -42.016 1.00 109.52 ? 285 LEU C O   1 
ATOM   10759 C CB  . LEU C 1 285 ? 75.423  56.825  -41.914 1.00 114.87 ? 285 LEU C CB  1 
ATOM   10760 C CG  . LEU C 1 285 ? 74.904  58.121  -41.273 1.00 117.72 ? 285 LEU C CG  1 
ATOM   10761 C CD1 . LEU C 1 285 ? 74.460  59.046  -42.396 1.00 119.63 ? 285 LEU C CD1 1 
ATOM   10762 C CD2 . LEU C 1 285 ? 73.776  57.953  -40.265 1.00 116.86 ? 285 LEU C CD2 1 
ATOM   10763 N N   . ASN C 1 286 ? 77.800  54.582  -42.173 1.00 111.64 ? 286 ASN C N   1 
ATOM   10764 C CA  . ASN C 1 286 ? 78.355  53.553  -43.046 1.00 109.24 ? 286 ASN C CA  1 
ATOM   10765 C C   . ASN C 1 286 ? 79.409  52.710  -42.319 1.00 107.64 ? 286 ASN C C   1 
ATOM   10766 O O   . ASN C 1 286 ? 80.322  52.172  -42.952 1.00 105.08 ? 286 ASN C O   1 
ATOM   10767 C CB  . ASN C 1 286 ? 78.932  54.167  -44.318 1.00 111.04 ? 286 ASN C CB  1 
ATOM   10768 C CG  . ASN C 1 286 ? 80.100  55.084  -44.035 1.00 114.11 ? 286 ASN C CG  1 
ATOM   10769 O OD1 . ASN C 1 286 ? 80.313  55.477  -42.882 1.00 115.68 ? 286 ASN C OD1 1 
ATOM   10770 N ND2 . ASN C 1 286 ? 80.865  55.444  -45.059 1.00 115.38 ? 286 ASN C ND2 1 
ATOM   10771 N N   . GLN C 1 287 ? 79.258  52.590  -40.990 1.00 108.53 ? 287 GLN C N   1 
ATOM   10772 C CA  . GLN C 1 287 ? 80.126  51.756  -40.171 1.00 108.06 ? 287 GLN C CA  1 
ATOM   10773 C C   . GLN C 1 287 ? 79.306  50.639  -39.513 1.00 105.05 ? 287 GLN C C   1 
ATOM   10774 O O   . GLN C 1 287 ? 78.695  50.815  -38.458 1.00 104.43 ? 287 GLN C O   1 
ATOM   10775 C CB  . GLN C 1 287 ? 80.885  52.606  -39.147 1.00 111.32 ? 287 GLN C CB  1 
ATOM   10776 C CG  . GLN C 1 287 ? 81.973  53.507  -39.731 1.00 113.38 ? 287 GLN C CG  1 
ATOM   10777 C CD  . GLN C 1 287 ? 83.080  52.761  -40.442 1.00 111.57 ? 287 GLN C CD  1 
ATOM   10778 O OE1 . GLN C 1 287 ? 83.261  52.888  -41.658 1.00 111.01 ? 287 GLN C OE1 1 
ATOM   10779 N NE2 . GLN C 1 287 ? 83.833  51.973  -39.691 1.00 110.73 ? 287 GLN C NE2 1 
ATOM   10780 N N   . PRO C 1 288 ? 79.276  49.435  -40.125 1.00 102.54 ? 288 PRO C N   1 
ATOM   10781 C CA  . PRO C 1 288 ? 78.576  48.290  -39.547 1.00 100.53 ? 288 PRO C CA  1 
ATOM   10782 C C   . PRO C 1 288 ? 78.899  48.041  -38.078 1.00 101.52 ? 288 PRO C C   1 
ATOM   10783 O O   . PRO C 1 288 ? 77.990  47.859  -37.274 1.00 102.62 ? 288 PRO C O   1 
ATOM   10784 C CB  . PRO C 1 288 ? 79.033  47.137  -40.445 1.00 97.67  ? 288 PRO C CB  1 
ATOM   10785 C CG  . PRO C 1 288 ? 79.231  47.797  -41.784 1.00 98.46  ? 288 PRO C CG  1 
ATOM   10786 C CD  . PRO C 1 288 ? 79.881  49.122  -41.430 1.00 101.78 ? 288 PRO C CD  1 
ATOM   10787 N N   . GLU C 1 289 ? 80.188  48.077  -37.723 1.00 102.18 ? 289 GLU C N   1 
ATOM   10788 C CA  . GLU C 1 289 ? 80.638  47.628  -36.412 1.00 102.03 ? 289 GLU C CA  1 
ATOM   10789 C C   . GLU C 1 289 ? 80.076  48.513  -35.302 1.00 104.70 ? 289 GLU C C   1 
ATOM   10790 O O   . GLU C 1 289 ? 80.166  48.167  -34.120 1.00 104.41 ? 289 GLU C O   1 
ATOM   10791 C CB  . GLU C 1 289 ? 82.164  47.611  -36.359 1.00 102.48 ? 289 GLU C CB  1 
ATOM   10792 C CG  . GLU C 1 289 ? 82.774  46.524  -37.236 1.00 99.38  ? 289 GLU C CG  1 
ATOM   10793 C CD  . GLU C 1 289 ? 82.446  45.116  -36.772 1.00 96.68  ? 289 GLU C CD  1 
ATOM   10794 O OE1 . GLU C 1 289 ? 82.596  44.842  -35.559 1.00 97.10  ? 289 GLU C OE1 1 
ATOM   10795 O OE2 . GLU C 1 289 ? 82.065  44.280  -37.622 1.00 94.28  ? 289 GLU C OE2 1 
ATOM   10796 N N   . GLU C 1 290 ? 79.495  49.649  -35.699 1.00 106.60 ? 290 GLU C N   1 
ATOM   10797 C CA  . GLU C 1 290 ? 78.974  50.596  -34.738 1.00 110.61 ? 290 GLU C CA  1 
ATOM   10798 C C   . GLU C 1 290 ? 77.472  50.383  -34.518 1.00 110.39 ? 290 GLU C C   1 
ATOM   10799 O O   . GLU C 1 290 ? 76.818  51.247  -33.933 1.00 112.16 ? 290 GLU C O   1 
ATOM   10800 C CB  . GLU C 1 290 ? 79.269  52.030  -35.201 1.00 114.48 ? 290 GLU C CB  1 
ATOM   10801 C CG  . GLU C 1 290 ? 80.709  52.517  -35.019 1.00 116.57 ? 290 GLU C CG  1 
ATOM   10802 C CD  . GLU C 1 290 ? 80.863  54.033  -35.089 1.00 120.96 ? 290 GLU C CD  1 
ATOM   10803 O OE1 . GLU C 1 290 ? 79.842  54.677  -35.407 1.00 121.74 ? 290 GLU C OE1 1 
ATOM   10804 O OE2 . GLU C 1 290 ? 81.959  54.596  -34.828 1.00 123.77 ? 290 GLU C OE2 1 
ATOM   10805 N N   . TRP C 1 291 ? 76.897  49.254  -34.972 1.00 108.04 ? 291 TRP C N   1 
ATOM   10806 C CA  . TRP C 1 291 ? 75.456  49.035  -34.811 1.00 106.75 ? 291 TRP C CA  1 
ATOM   10807 C C   . TRP C 1 291 ? 75.114  47.561  -34.559 1.00 103.23 ? 291 TRP C C   1 
ATOM   10808 O O   . TRP C 1 291 ? 74.028  47.131  -34.959 1.00 102.71 ? 291 TRP C O   1 
ATOM   10809 C CB  . TRP C 1 291 ? 74.667  49.555  -36.029 1.00 106.32 ? 291 TRP C CB  1 
ATOM   10810 C CG  . TRP C 1 291 ? 74.773  51.037  -36.302 1.00 109.64 ? 291 TRP C CG  1 
ATOM   10811 C CD1 . TRP C 1 291 ? 75.800  51.670  -36.940 1.00 110.74 ? 291 TRP C CD1 1 
ATOM   10812 C CD2 . TRP C 1 291 ? 73.799  52.066  -36.001 1.00 112.22 ? 291 TRP C CD2 1 
ATOM   10813 N NE1 . TRP C 1 291 ? 75.549  53.011  -37.043 1.00 114.03 ? 291 TRP C NE1 1 
ATOM   10814 C CE2 . TRP C 1 291 ? 74.330  53.286  -36.479 1.00 114.69 ? 291 TRP C CE2 1 
ATOM   10815 C CE3 . TRP C 1 291 ? 72.544  52.088  -35.375 1.00 112.59 ? 291 TRP C CE3 1 
ATOM   10816 C CZ2 . TRP C 1 291 ? 73.649  54.495  -36.346 1.00 117.11 ? 291 TRP C CZ2 1 
ATOM   10817 C CZ3 . TRP C 1 291 ? 71.874  53.289  -35.243 1.00 114.81 ? 291 TRP C CZ3 1 
ATOM   10818 C CH2 . TRP C 1 291 ? 72.418  54.474  -35.730 1.00 116.84 ? 291 TRP C CH2 1 
ATOM   10819 N N   . PHE C 1 292 ? 75.995  46.810  -33.861 1.00 100.77 ? 292 PHE C N   1 
ATOM   10820 C CA  . PHE C 1 292 ? 75.773  45.396  -33.564 1.00 96.75  ? 292 PHE C CA  1 
ATOM   10821 C C   . PHE C 1 292 ? 75.013  45.183  -32.246 1.00 97.10  ? 292 PHE C C   1 
ATOM   10822 O O   . PHE C 1 292 ? 74.677  44.050  -31.896 1.00 95.37  ? 292 PHE C O   1 
ATOM   10823 C CB  . PHE C 1 292 ? 77.099  44.623  -33.536 1.00 95.44  ? 292 PHE C CB  1 
ATOM   10824 C CG  . PHE C 1 292 ? 77.416  43.949  -34.861 1.00 92.19  ? 292 PHE C CG  1 
ATOM   10825 C CD1 . PHE C 1 292 ? 76.713  42.813  -35.269 1.00 89.26  ? 292 PHE C CD1 1 
ATOM   10826 C CD2 . PHE C 1 292 ? 78.393  44.463  -35.700 1.00 91.87  ? 292 PHE C CD2 1 
ATOM   10827 C CE1 . PHE C 1 292 ? 76.978  42.217  -36.491 1.00 86.92  ? 292 PHE C CE1 1 
ATOM   10828 C CE2 . PHE C 1 292 ? 78.652  43.866  -36.921 1.00 89.71  ? 292 PHE C CE2 1 
ATOM   10829 C CZ  . PHE C 1 292 ? 77.942  42.749  -37.315 1.00 87.43  ? 292 PHE C CZ  1 
ATOM   10830 N N   . GLY C 1 293 ? 74.713  46.270  -31.524 1.00 99.66  ? 293 GLY C N   1 
ATOM   10831 C CA  . GLY C 1 293 ? 74.102  46.189  -30.204 1.00 100.42 ? 293 GLY C CA  1 
ATOM   10832 C C   . GLY C 1 293 ? 72.654  45.708  -30.248 1.00 98.35  ? 293 GLY C C   1 
ATOM   10833 O O   . GLY C 1 293 ? 71.974  45.857  -31.261 1.00 96.51  ? 293 GLY C O   1 
ATOM   10834 N N   . PHE C 1 294 ? 72.232  45.090  -29.139 1.00 98.27  ? 294 PHE C N   1 
ATOM   10835 C CA  . PHE C 1 294 ? 70.832  44.814  -28.862 1.00 97.93  ? 294 PHE C CA  1 
ATOM   10836 C C   . PHE C 1 294 ? 70.200  46.079  -28.280 1.00 101.33 ? 294 PHE C C   1 
ATOM   10837 O O   . PHE C 1 294 ? 68.993  46.285  -28.389 1.00 101.27 ? 294 PHE C O   1 
ATOM   10838 C CB  . PHE C 1 294 ? 70.683  43.631  -27.899 1.00 96.99  ? 294 PHE C CB  1 
ATOM   10839 C CG  . PHE C 1 294 ? 71.035  42.258  -28.459 1.00 93.49  ? 294 PHE C CG  1 
ATOM   10840 C CD1 . PHE C 1 294 ? 71.664  42.112  -29.695 1.00 91.31  ? 294 PHE C CD1 1 
ATOM   10841 C CD2 . PHE C 1 294 ? 70.770  41.111  -27.719 1.00 92.32  ? 294 PHE C CD2 1 
ATOM   10842 C CE1 . PHE C 1 294 ? 71.962  40.859  -30.194 1.00 88.30  ? 294 PHE C CE1 1 
ATOM   10843 C CE2 . PHE C 1 294 ? 71.077  39.864  -28.224 1.00 89.61  ? 294 PHE C CE2 1 
ATOM   10844 C CZ  . PHE C 1 294 ? 71.666  39.743  -29.458 1.00 87.72  ? 294 PHE C CZ  1 
ATOM   10845 N N   . TRP C 1 295 ? 71.033  46.937  -27.675 1.00 104.28 ? 295 TRP C N   1 
ATOM   10846 C CA  . TRP C 1 295 ? 70.597  48.267  -27.268 1.00 107.47 ? 295 TRP C CA  1 
ATOM   10847 C C   . TRP C 1 295 ? 71.189  49.316  -28.206 1.00 108.36 ? 295 TRP C C   1 
ATOM   10848 O O   . TRP C 1 295 ? 72.262  49.103  -28.767 1.00 107.49 ? 295 TRP C O   1 
ATOM   10849 C CB  . TRP C 1 295 ? 70.996  48.539  -25.811 1.00 110.21 ? 295 TRP C CB  1 
ATOM   10850 C CG  . TRP C 1 295 ? 70.310  47.663  -24.791 1.00 110.18 ? 295 TRP C CG  1 
ATOM   10851 C CD1 . TRP C 1 295 ? 70.266  46.297  -24.732 1.00 107.37 ? 295 TRP C CD1 1 
ATOM   10852 C CD2 . TRP C 1 295 ? 69.537  48.134  -23.664 1.00 113.14 ? 295 TRP C CD2 1 
ATOM   10853 N NE1 . TRP C 1 295 ? 69.547  45.891  -23.640 1.00 108.59 ? 295 TRP C NE1 1 
ATOM   10854 C CE2 . TRP C 1 295 ? 69.080  46.994  -22.970 1.00 112.15 ? 295 TRP C CE2 1 
ATOM   10855 C CE3 . TRP C 1 295 ? 69.194  49.402  -23.177 1.00 116.75 ? 295 TRP C CE3 1 
ATOM   10856 C CZ2 . TRP C 1 295 ? 68.297  47.096  -21.820 1.00 114.63 ? 295 TRP C CZ2 1 
ATOM   10857 C CZ3 . TRP C 1 295 ? 68.413  49.500  -22.046 1.00 119.13 ? 295 TRP C CZ3 1 
ATOM   10858 C CH2 . TRP C 1 295 ? 67.975  48.360  -21.376 1.00 118.05 ? 295 TRP C CH2 1 
ATOM   10859 N N   . GLY C 1 296 ? 70.478  50.439  -28.378 1.00 110.65 ? 296 GLY C N   1 
ATOM   10860 C CA  . GLY C 1 296 ? 70.997  51.587  -29.116 1.00 112.57 ? 296 GLY C CA  1 
ATOM   10861 C C   . GLY C 1 296 ? 71.096  52.841  -28.240 1.00 117.02 ? 296 GLY C C   1 
ATOM   10862 O O   . GLY C 1 296 ? 70.560  52.888  -27.136 1.00 118.28 ? 296 GLY C O   1 
ATOM   10863 N N   . TYR C 1 297 ? 71.796  53.863  -28.745 1.00 119.60 ? 297 TYR C N   1 
ATOM   10864 C CA  . TYR C 1 297 ? 72.050  55.078  -27.983 1.00 124.36 ? 297 TYR C CA  1 
ATOM   10865 C C   . TYR C 1 297 ? 71.474  56.269  -28.755 1.00 125.70 ? 297 TYR C C   1 
ATOM   10866 O O   . TYR C 1 297 ? 71.842  56.483  -29.908 1.00 124.63 ? 297 TYR C O   1 
ATOM   10867 C CB  . TYR C 1 297 ? 73.555  55.154  -27.671 1.00 126.22 ? 297 TYR C CB  1 
ATOM   10868 C CG  . TYR C 1 297 ? 74.094  54.087  -26.712 1.00 126.05 ? 297 TYR C CG  1 
ATOM   10869 C CD1 . TYR C 1 297 ? 73.687  54.053  -25.378 1.00 128.87 ? 297 TYR C CD1 1 
ATOM   10870 C CD2 . TYR C 1 297 ? 75.028  53.134  -27.112 1.00 123.03 ? 297 TYR C CD2 1 
ATOM   10871 C CE1 . TYR C 1 297 ? 74.156  53.094  -24.491 1.00 127.96 ? 297 TYR C CE1 1 
ATOM   10872 C CE2 . TYR C 1 297 ? 75.505  52.170  -26.231 1.00 122.40 ? 297 TYR C CE2 1 
ATOM   10873 C CZ  . TYR C 1 297 ? 75.068  52.148  -24.917 1.00 124.43 ? 297 TYR C CZ  1 
ATOM   10874 O OH  . TYR C 1 297 ? 75.503  51.233  -24.004 1.00 123.37 ? 297 TYR C OH  1 
ATOM   10875 N N   . SER C 1 298 ? 70.584  57.034  -28.088 1.00 128.19 ? 298 SER C N   1 
ATOM   10876 C CA  . SER C 1 298 ? 69.773  58.091  -28.688 1.00 129.44 ? 298 SER C CA  1 
ATOM   10877 C C   . SER C 1 298 ? 70.647  59.121  -29.387 1.00 130.76 ? 298 SER C C   1 
ATOM   10878 O O   . SER C 1 298 ? 70.339  59.551  -30.495 1.00 130.04 ? 298 SER C O   1 
ATOM   10879 C CB  . SER C 1 298 ? 68.927  58.822  -27.662 1.00 133.08 ? 298 SER C CB  1 
ATOM   10880 O OG  . SER C 1 298 ? 68.389  57.948  -26.682 1.00 132.47 ? 298 SER C OG  1 
ATOM   10881 N N   . ASP C 1 299 ? 71.686  59.542  -28.663 1.00 132.92 ? 299 ASP C N   1 
ATOM   10882 C CA  . ASP C 1 299 ? 72.615  60.569  -29.094 1.00 135.12 ? 299 ASP C CA  1 
ATOM   10883 C C   . ASP C 1 299 ? 73.944  60.327  -28.371 1.00 135.85 ? 299 ASP C C   1 
ATOM   10884 O O   . ASP C 1 299 ? 74.155  59.263  -27.786 1.00 133.55 ? 299 ASP C O   1 
ATOM   10885 C CB  . ASP C 1 299 ? 71.990  61.937  -28.874 1.00 139.28 ? 299 ASP C CB  1 
ATOM   10886 C CG  . ASP C 1 299 ? 71.456  62.180  -27.469 1.00 142.39 ? 299 ASP C CG  1 
ATOM   10887 O OD1 . ASP C 1 299 ? 72.233  62.008  -26.508 1.00 143.66 ? 299 ASP C OD1 1 
ATOM   10888 O OD2 . ASP C 1 299 ? 70.268  62.550  -27.344 1.00 143.92 ? 299 ASP C OD2 1 
ATOM   10889 N N   . LEU C 1 300 ? 74.841  61.319  -28.410 1.00 138.89 ? 300 LEU C N   1 
ATOM   10890 C CA  . LEU C 1 300 ? 76.141  61.217  -27.770 1.00 139.74 ? 300 LEU C CA  1 
ATOM   10891 C C   . LEU C 1 300 ? 75.992  61.303  -26.250 1.00 142.00 ? 300 LEU C C   1 
ATOM   10892 O O   . LEU C 1 300 ? 76.728  60.640  -25.523 1.00 141.16 ? 300 LEU C O   1 
ATOM   10893 C CB  . LEU C 1 300 ? 77.007  62.328  -28.364 1.00 142.95 ? 300 LEU C CB  1 
ATOM   10894 C CG  . LEU C 1 300 ? 78.438  62.467  -27.833 1.00 145.19 ? 300 LEU C CG  1 
ATOM   10895 C CD1 . LEU C 1 300 ? 79.104  61.130  -27.546 1.00 142.06 ? 300 LEU C CD1 1 
ATOM   10896 C CD2 . LEU C 1 300 ? 79.268  63.245  -28.844 1.00 146.53 ? 300 LEU C CD2 1 
ATOM   10897 N N   . ASN C 1 301 ? 74.891  61.900  -25.807 1.00 144.55 ? 301 ASN C N   1 
ATOM   10898 C CA  . ASN C 1 301 ? 74.699  62.081  -24.345 1.00 147.65 ? 301 ASN C CA  1 
ATOM   10899 C C   . ASN C 1 301 ? 73.782  60.998  -23.764 1.00 145.29 ? 301 ASN C C   1 
ATOM   10900 O O   . ASN C 1 301 ? 73.235  61.233  -22.670 1.00 147.46 ? 301 ASN C O   1 
ATOM   10901 C CB  . ASN C 1 301 ? 74.212  63.494  -24.051 1.00 152.53 ? 301 ASN C CB  1 
ATOM   10902 C CG  . ASN C 1 301 ? 75.197  64.528  -24.543 1.00 154.89 ? 301 ASN C CG  1 
ATOM   10903 O OD1 . ASN C 1 301 ? 75.067  65.033  -25.663 1.00 154.93 ? 301 ASN C OD1 1 
ATOM   10904 N ND2 . ASN C 1 301 ? 76.197  64.841  -23.733 1.00 156.80 ? 301 ASN C ND2 1 
ATOM   10905 N N   . ASP C 1 302 ? 73.637  59.857  -24.447 1.00 140.94 ? 302 ASP C N   1 
ATOM   10906 C CA  . ASP C 1 302 ? 72.693  58.818  -23.948 1.00 138.85 ? 302 ASP C CA  1 
ATOM   10907 C C   . ASP C 1 302 ? 73.261  58.192  -22.673 1.00 139.78 ? 302 ASP C C   1 
ATOM   10908 O O   . ASP C 1 302 ? 72.758  58.569  -21.595 1.00 144.19 ? 302 ASP C O   1 
ATOM   10909 C CB  . ASP C 1 302 ? 72.337  57.780  -24.999 1.00 133.90 ? 302 ASP C CB  1 
ATOM   10910 C CG  . ASP C 1 302 ? 71.121  56.929  -24.658 1.00 132.05 ? 302 ASP C CG  1 
ATOM   10911 O OD1 . ASP C 1 302 ? 70.931  56.616  -23.465 1.00 133.66 ? 302 ASP C OD1 1 
ATOM   10912 O OD2 . ASP C 1 302 ? 70.364  56.588  -25.584 1.00 128.93 ? 302 ASP C OD2 1 
ATOM   10913 N N   . LYS C 1 303 ? 74.189  57.238  -22.799 1.00 136.05 ? 303 LYS C N   1 
ATOM   10914 C CA  . LYS C 1 303 ? 74.859  56.605  -21.627 1.00 136.70 ? 303 LYS C CA  1 
ATOM   10915 C C   . LYS C 1 303 ? 73.981  55.499  -21.020 1.00 134.73 ? 303 LYS C C   1 
ATOM   10916 O O   . LYS C 1 303 ? 74.427  54.877  -20.037 1.00 134.34 ? 303 LYS C O   1 
ATOM   10917 C CB  . LYS C 1 303 ? 75.272  57.647  -20.577 1.00 141.60 ? 303 LYS C CB  1 
ATOM   10918 C CG  . LYS C 1 303 ? 76.757  57.720  -20.243 1.00 144.15 ? 303 LYS C CG  1 
ATOM   10919 C CD  . LYS C 1 303 ? 77.669  58.117  -21.397 1.00 142.85 ? 303 LYS C CD  1 
ATOM   10920 C CE  . LYS C 1 303 ? 77.180  59.281  -22.198 1.00 143.59 ? 303 LYS C CE  1 
ATOM   10921 N NZ  . LYS C 1 303 ? 77.104  58.931  -23.617 1.00 148.65 ? 303 LYS C NZ  1 
ATOM   10922 N N   . TYR C 1 304 ? 72.793  55.261  -21.577 1.00 133.76 ? 304 TYR C N   1 
ATOM   10923 C CA  . TYR C 1 304 ? 71.920  54.194  -21.097 1.00 132.12 ? 304 TYR C CA  1 
ATOM   10924 C C   . TYR C 1 304 ? 71.398  53.360  -22.271 1.00 128.11 ? 304 TYR C C   1 
ATOM   10925 O O   . TYR C 1 304 ? 71.665  52.160  -22.356 1.00 125.10 ? 304 TYR C O   1 
ATOM   10926 C CB  . TYR C 1 304 ? 70.783  54.804  -20.270 1.00 134.90 ? 304 TYR C CB  1 
ATOM   10927 C CG  . TYR C 1 304 ? 71.240  55.678  -19.112 1.00 139.41 ? 304 TYR C CG  1 
ATOM   10928 C CD1 . TYR C 1 304 ? 71.663  55.125  -17.909 1.00 140.72 ? 304 TYR C CD1 1 
ATOM   10929 C CD2 . TYR C 1 304 ? 71.236  57.064  -19.219 1.00 142.90 ? 304 TYR C CD2 1 
ATOM   10930 C CE1 . TYR C 1 304 ? 72.080  55.926  -16.855 1.00 145.35 ? 304 TYR C CE1 1 
ATOM   10931 C CE2 . TYR C 1 304 ? 71.642  57.877  -18.171 1.00 147.45 ? 304 TYR C CE2 1 
ATOM   10932 C CZ  . TYR C 1 304 ? 72.071  57.306  -16.987 1.00 148.65 ? 304 TYR C CZ  1 
ATOM   10933 O OH  . TYR C 1 304 ? 72.465  58.125  -15.971 1.00 153.32 ? 304 TYR C OH  1 
ATOM   10934 N N   . GLY C 1 305 ? 70.640  54.009  -23.164 1.00 128.29 ? 305 GLY C N   1 
ATOM   10935 C CA  . GLY C 1 305 ? 70.113  53.366  -24.356 1.00 124.72 ? 305 GLY C CA  1 
ATOM   10936 C C   . GLY C 1 305 ? 68.733  52.765  -24.102 1.00 123.90 ? 305 GLY C C   1 
ATOM   10937 O O   . GLY C 1 305 ? 68.182  52.918  -23.013 1.00 126.07 ? 305 GLY C O   1 
ATOM   10938 N N   . THR C 1 306 ? 68.192  52.101  -25.136 1.00 120.94 ? 306 THR C N   1 
ATOM   10939 C CA  . THR C 1 306 ? 67.001  51.264  -25.026 1.00 119.62 ? 306 THR C CA  1 
ATOM   10940 C C   . THR C 1 306 ? 67.260  49.936  -25.743 1.00 115.58 ? 306 THR C C   1 
ATOM   10941 O O   . THR C 1 306 ? 68.229  49.828  -26.492 1.00 114.42 ? 306 THR C O   1 
ATOM   10942 C CB  . THR C 1 306 ? 65.795  51.983  -25.629 1.00 120.12 ? 306 THR C CB  1 
ATOM   10943 O OG1 . THR C 1 306 ? 66.062  51.990  -27.030 1.00 117.76 ? 306 THR C OG1 1 
ATOM   10944 C CG2 . THR C 1 306 ? 65.601  53.381  -25.070 1.00 124.25 ? 306 THR C CG2 1 
ATOM   10945 N N   . PRO C 1 307 ? 66.493  48.851  -25.450 1.00 113.97 ? 307 PRO C N   1 
ATOM   10946 C CA  . PRO C 1 307 ? 66.653  47.602  -26.175 1.00 109.75 ? 307 PRO C CA  1 
ATOM   10947 C C   . PRO C 1 307 ? 65.904  47.591  -27.484 1.00 107.45 ? 307 PRO C C   1 
ATOM   10948 O O   . PRO C 1 307 ? 64.749  48.038  -27.547 1.00 108.89 ? 307 PRO C O   1 
ATOM   10949 C CB  . PRO C 1 307 ? 66.097  46.575  -25.197 1.00 109.79 ? 307 PRO C CB  1 
ATOM   10950 C CG  . PRO C 1 307 ? 64.984  47.283  -24.488 1.00 113.39 ? 307 PRO C CG  1 
ATOM   10951 C CD  . PRO C 1 307 ? 65.494  48.697  -24.364 1.00 115.96 ? 307 PRO C CD  1 
ATOM   10952 N N   . ARG C 1 308 ? 66.550  47.082  -28.526 1.00 105.20 ? 308 ARG C N   1 
ATOM   10953 C CA  . ARG C 1 308 ? 65.903  46.983  -29.855 1.00 103.38 ? 308 ARG C CA  1 
ATOM   10954 C C   . ARG C 1 308 ? 64.978  45.755  -29.852 1.00 101.91 ? 308 ARG C C   1 
ATOM   10955 O O   . ARG C 1 308 ? 64.945  45.036  -28.838 1.00 101.80 ? 308 ARG C O   1 
ATOM   10956 C CB  . ARG C 1 308 ? 67.032  46.929  -30.889 1.00 101.75 ? 308 ARG C CB  1 
ATOM   10957 C CG  . ARG C 1 308 ? 67.974  48.122  -30.862 1.00 103.86 ? 308 ARG C CG  1 
ATOM   10958 C CD  . ARG C 1 308 ? 69.311  47.760  -31.472 1.00 101.96 ? 308 ARG C CD  1 
ATOM   10959 N NE  . ARG C 1 308 ? 69.833  48.807  -32.355 1.00 103.96 ? 308 ARG C NE  1 
ATOM   10960 C CZ  . ARG C 1 308 ? 71.121  49.066  -32.515 1.00 104.52 ? 308 ARG C CZ  1 
ATOM   10961 N NH1 . ARG C 1 308 ? 71.983  48.076  -32.645 1.00 102.77 ? 308 ARG C NH1 1 
ATOM   10962 N NH2 . ARG C 1 308 ? 71.542  50.316  -32.548 1.00 106.72 ? 308 ARG C NH2 1 
ATOM   10963 N N   . PRO C 1 309 ? 64.205  45.488  -30.922 1.00 100.89 ? 309 PRO C N   1 
ATOM   10964 C CA  . PRO C 1 309 ? 63.377  44.297  -30.956 1.00 99.32  ? 309 PRO C CA  1 
ATOM   10965 C C   . PRO C 1 309 ? 64.136  43.023  -30.617 1.00 97.89  ? 309 PRO C C   1 
ATOM   10966 O O   . PRO C 1 309 ? 63.625  42.222  -29.812 1.00 98.97  ? 309 PRO C O   1 
ATOM   10967 C CB  . PRO C 1 309 ? 62.931  44.323  -32.415 1.00 97.98  ? 309 PRO C CB  1 
ATOM   10968 C CG  . PRO C 1 309 ? 62.809  45.784  -32.737 1.00 99.86  ? 309 PRO C CG  1 
ATOM   10969 C CD  . PRO C 1 309 ? 64.056  46.339  -32.093 1.00 100.83 ? 309 PRO C CD  1 
ATOM   10970 N N   . VAL C 1 310 ? 65.321  42.831  -31.203 1.00 96.64  ? 310 VAL C N   1 
ATOM   10971 C CA  . VAL C 1 310 ? 66.081  41.610  -31.006 1.00 94.67  ? 310 VAL C CA  1 
ATOM   10972 C C   . VAL C 1 310 ? 65.980  41.153  -29.555 1.00 94.92  ? 310 VAL C C   1 
ATOM   10973 O O   . VAL C 1 310 ? 65.683  40.007  -29.275 1.00 94.44  ? 310 VAL C O   1 
ATOM   10974 C CB  . VAL C 1 310 ? 67.550  41.838  -31.369 1.00 95.39  ? 310 VAL C CB  1 
ATOM   10975 C CG1 . VAL C 1 310 ? 68.392  40.618  -31.016 1.00 95.19  ? 310 VAL C CG1 1 
ATOM   10976 C CG2 . VAL C 1 310 ? 67.709  42.204  -32.831 1.00 94.38  ? 310 VAL C CG2 1 
ATOM   10977 N N   . TRP C 1 311 ? 66.287  42.064  -28.642 1.00 96.85  ? 311 TRP C N   1 
ATOM   10978 C CA  . TRP C 1 311 ? 66.318  41.809  -27.214 1.00 98.16  ? 311 TRP C CA  1 
ATOM   10979 C C   . TRP C 1 311 ? 65.165  40.924  -26.758 1.00 97.33  ? 311 TRP C C   1 
ATOM   10980 O O   . TRP C 1 311 ? 65.393  39.994  -25.993 1.00 97.88  ? 311 TRP C O   1 
ATOM   10981 C CB  . TRP C 1 311 ? 66.255  43.163  -26.501 1.00 101.54 ? 311 TRP C CB  1 
ATOM   10982 C CG  . TRP C 1 311 ? 66.386  43.124  -25.003 1.00 104.13 ? 311 TRP C CG  1 
ATOM   10983 C CD1 . TRP C 1 311 ? 65.393  43.307  -24.084 1.00 106.07 ? 311 TRP C CD1 1 
ATOM   10984 C CD2 . TRP C 1 311 ? 67.606  42.946  -24.251 1.00 104.88 ? 311 TRP C CD2 1 
ATOM   10985 N NE1 . TRP C 1 311 ? 65.904  43.237  -22.815 1.00 108.38 ? 311 TRP C NE1 1 
ATOM   10986 C CE2 . TRP C 1 311 ? 67.257  43.017  -22.885 1.00 107.65 ? 311 TRP C CE2 1 
ATOM   10987 C CE3 . TRP C 1 311 ? 68.941  42.733  -24.600 1.00 103.65 ? 311 TRP C CE3 1 
ATOM   10988 C CZ2 . TRP C 1 311 ? 68.195  42.877  -21.870 1.00 109.07 ? 311 TRP C CZ2 1 
ATOM   10989 C CZ3 . TRP C 1 311 ? 69.866  42.593  -23.593 1.00 105.48 ? 311 TRP C CZ3 1 
ATOM   10990 C CH2 . TRP C 1 311 ? 69.497  42.673  -22.249 1.00 108.06 ? 311 TRP C CH2 1 
ATOM   10991 N N   . PHE C 1 312 ? 63.944  41.265  -27.205 1.00 96.87  ? 312 PHE C N   1 
ATOM   10992 C CA  . PHE C 1 312 ? 62.696  40.715  -26.682 1.00 96.81  ? 312 PHE C CA  1 
ATOM   10993 C C   . PHE C 1 312 ? 62.408  39.368  -27.353 1.00 94.20  ? 312 PHE C C   1 
ATOM   10994 O O   . PHE C 1 312 ? 61.830  38.475  -26.729 1.00 94.42  ? 312 PHE C O   1 
ATOM   10995 C CB  . PHE C 1 312 ? 61.497  41.673  -26.846 1.00 97.52  ? 312 PHE C CB  1 
ATOM   10996 C CG  . PHE C 1 312 ? 61.531  42.979  -26.052 1.00 100.27 ? 312 PHE C CG  1 
ATOM   10997 C CD1 . PHE C 1 312 ? 61.074  43.042  -24.738 1.00 102.42 ? 312 PHE C CD1 1 
ATOM   10998 C CD2 . PHE C 1 312 ? 62.027  44.152  -26.621 1.00 101.02 ? 312 PHE C CD2 1 
ATOM   10999 C CE1 . PHE C 1 312 ? 61.133  44.229  -24.020 1.00 105.54 ? 312 PHE C CE1 1 
ATOM   11000 C CE2 . PHE C 1 312 ? 62.085  45.339  -25.897 1.00 103.90 ? 312 PHE C CE2 1 
ATOM   11001 C CZ  . PHE C 1 312 ? 61.637  45.373  -24.599 1.00 106.32 ? 312 PHE C CZ  1 
ATOM   11002 N N   . ALA C 1 313 ? 62.783  39.233  -28.634 1.00 91.81  ? 313 ALA C N   1 
ATOM   11003 C CA  . ALA C 1 313 ? 62.647  37.961  -29.321 1.00 89.23  ? 313 ALA C CA  1 
ATOM   11004 C C   . ALA C 1 313 ? 63.501  36.932  -28.590 1.00 90.07  ? 313 ALA C C   1 
ATOM   11005 O O   . ALA C 1 313 ? 63.006  35.852  -28.261 1.00 89.65  ? 313 ALA C O   1 
ATOM   11006 C CB  . ALA C 1 313 ? 63.030  38.082  -30.780 1.00 86.70  ? 313 ALA C CB  1 
ATOM   11007 N N   . MET C 1 314 ? 64.763  37.321  -28.322 1.00 91.83  ? 314 MET C N   1 
ATOM   11008 C CA  . MET C 1 314 ? 65.776  36.470  -27.717 1.00 92.60  ? 314 MET C CA  1 
ATOM   11009 C C   . MET C 1 314 ? 65.317  36.026  -26.331 1.00 93.97  ? 314 MET C C   1 
ATOM   11010 O O   . MET C 1 314 ? 65.324  34.839  -26.019 1.00 93.21  ? 314 MET C O   1 
ATOM   11011 C CB  . MET C 1 314 ? 67.109  37.215  -27.560 1.00 95.22  ? 314 MET C CB  1 
ATOM   11012 C CG  . MET C 1 314 ? 67.910  37.399  -28.846 1.00 94.89  ? 314 MET C CG  1 
ATOM   11013 S SD  . MET C 1 314 ? 68.792  35.932  -29.423 1.00 94.71  ? 314 MET C SD  1 
ATOM   11014 C CE  . MET C 1 314 ? 69.662  35.405  -27.940 1.00 95.94  ? 314 MET C CE  1 
ATOM   11015 N N   . ARG C 1 315 ? 64.928  36.994  -25.502 1.00 96.19  ? 315 ARG C N   1 
ATOM   11016 C CA  . ARG C 1 315 ? 64.483  36.702  -24.152 1.00 98.72  ? 315 ARG C CA  1 
ATOM   11017 C C   . ARG C 1 315 ? 63.464  35.565  -24.184 1.00 97.56  ? 315 ARG C C   1 
ATOM   11018 O O   . ARG C 1 315 ? 63.565  34.624  -23.399 1.00 97.88  ? 315 ARG C O   1 
ATOM   11019 C CB  . ARG C 1 315 ? 63.897  37.975  -23.529 1.00 101.91 ? 315 ARG C CB  1 
ATOM   11020 C CG  . ARG C 1 315 ? 63.418  37.831  -22.091 1.00 105.26 ? 315 ARG C CG  1 
ATOM   11021 C CD  . ARG C 1 315 ? 62.650  39.068  -21.596 1.00 108.40 ? 315 ARG C CD  1 
ATOM   11022 N NE  . ARG C 1 315 ? 61.383  39.322  -22.299 1.00 107.64 ? 315 ARG C NE  1 
ATOM   11023 C CZ  . ARG C 1 315 ? 60.621  40.418  -22.198 1.00 109.61 ? 315 ARG C CZ  1 
ATOM   11024 N NH1 . ARG C 1 315 ? 60.938  41.401  -21.370 1.00 112.37 ? 315 ARG C NH1 1 
ATOM   11025 N NH2 . ARG C 1 315 ? 59.521  40.529  -22.927 1.00 109.25 ? 315 ARG C NH2 1 
ATOM   11026 N N   . ASP C 1 316 ? 62.503  35.671  -25.114 1.00 96.27  ? 316 ASP C N   1 
ATOM   11027 C CA  . ASP C 1 316 ? 61.368  34.770  -25.206 1.00 95.67  ? 316 ASP C CA  1 
ATOM   11028 C C   . ASP C 1 316 ? 61.781  33.441  -25.807 1.00 94.15  ? 316 ASP C C   1 
ATOM   11029 O O   . ASP C 1 316 ? 61.201  32.415  -25.483 1.00 94.28  ? 316 ASP C O   1 
ATOM   11030 C CB  . ASP C 1 316 ? 60.276  35.312  -26.112 1.00 94.69  ? 316 ASP C CB  1 
ATOM   11031 C CG  . ASP C 1 316 ? 59.618  36.597  -25.640 1.00 96.26  ? 316 ASP C CG  1 
ATOM   11032 O OD1 . ASP C 1 316 ? 60.060  37.131  -24.604 1.00 97.68  ? 316 ASP C OD1 1 
ATOM   11033 O OD2 . ASP C 1 316 ? 58.667  37.036  -26.312 1.00 95.67  ? 316 ASP C OD2 1 
ATOM   11034 N N   . TYR C 1 317 ? 62.742  33.489  -26.727 1.00 93.97  ? 317 TYR C N   1 
ATOM   11035 C CA  . TYR C 1 317 ? 63.303  32.279  -27.302 1.00 93.27  ? 317 TYR C CA  1 
ATOM   11036 C C   . TYR C 1 317 ? 64.136  31.512  -26.270 1.00 95.60  ? 317 TYR C C   1 
ATOM   11037 O O   . TYR C 1 317 ? 64.243  30.291  -26.364 1.00 96.53  ? 317 TYR C O   1 
ATOM   11038 C CB  . TYR C 1 317 ? 64.176  32.593  -28.521 1.00 91.91  ? 317 TYR C CB  1 
ATOM   11039 C CG  . TYR C 1 317 ? 64.679  31.343  -29.234 1.00 90.43  ? 317 TYR C CG  1 
ATOM   11040 C CD1 . TYR C 1 317 ? 65.818  30.682  -28.795 1.00 90.58  ? 317 TYR C CD1 1 
ATOM   11041 C CD2 . TYR C 1 317 ? 64.002  30.811  -30.325 1.00 88.59  ? 317 TYR C CD2 1 
ATOM   11042 C CE1 . TYR C 1 317 ? 66.271  29.538  -29.425 1.00 89.52  ? 317 TYR C CE1 1 
ATOM   11043 C CE2 . TYR C 1 317 ? 64.446  29.670  -30.970 1.00 86.79  ? 317 TYR C CE2 1 
ATOM   11044 C CZ  . TYR C 1 317 ? 65.587  29.034  -30.516 1.00 88.29  ? 317 TYR C CZ  1 
ATOM   11045 O OH  . TYR C 1 317 ? 66.071  27.903  -31.117 1.00 88.69  ? 317 TYR C OH  1 
ATOM   11046 N N   . MET C 1 318 ? 64.749  32.213  -25.304 1.00 98.14  ? 318 MET C N   1 
ATOM   11047 C CA  . MET C 1 318 ? 65.705  31.590  -24.392 1.00 99.41  ? 318 MET C CA  1 
ATOM   11048 C C   . MET C 1 318 ? 65.024  30.861  -23.224 1.00 100.06 ? 318 MET C C   1 
ATOM   11049 O O   . MET C 1 318 ? 65.713  30.188  -22.456 1.00 101.61 ? 318 MET C O   1 
ATOM   11050 C CB  . MET C 1 318 ? 66.693  32.625  -23.831 1.00 101.80 ? 318 MET C CB  1 
ATOM   11051 C CG  . MET C 1 318 ? 67.935  32.840  -24.691 1.00 100.79 ? 318 MET C CG  1 
ATOM   11052 S SD  . MET C 1 318 ? 68.882  34.311  -24.238 1.00 104.41 ? 318 MET C SD  1 
ATOM   11053 C CE  . MET C 1 318 ? 69.048  34.041  -22.470 1.00 106.49 ? 318 MET C CE  1 
ATOM   11054 N N   . LYS C 1 319 ? 63.692  30.981  -23.086 1.00 98.84  ? 319 LYS C N   1 
ATOM   11055 C CA  . LYS C 1 319 ? 62.970  30.442  -21.936 1.00 99.49  ? 319 LYS C CA  1 
ATOM   11056 C C   . LYS C 1 319 ? 62.959  28.912  -21.981 1.00 96.89  ? 319 LYS C C   1 
ATOM   11057 O O   . LYS C 1 319 ? 63.014  28.240  -20.951 1.00 97.70  ? 319 LYS C O   1 
ATOM   11058 C CB  . LYS C 1 319 ? 61.519  30.954  -21.877 1.00 100.53 ? 319 LYS C CB  1 
ATOM   11059 C CG  . LYS C 1 319 ? 61.293  32.476  -21.933 1.00 101.62 ? 319 LYS C CG  1 
ATOM   11060 C CD  . LYS C 1 319 ? 62.118  33.324  -20.965 1.00 103.82 ? 319 LYS C CD  1 
ATOM   11061 C CE  . LYS C 1 319 ? 61.815  33.104  -19.510 1.00 106.42 ? 319 LYS C CE  1 
ATOM   11062 N NZ  . LYS C 1 319 ? 60.518  33.633  -19.099 1.00 107.93 ? 319 LYS C NZ  1 
ATOM   11063 N N   . GLY C 1 320 ? 62.833  28.375  -23.194 1.00 93.26  ? 320 GLY C N   1 
ATOM   11064 C CA  . GLY C 1 320 ? 62.793  26.945  -23.415 1.00 92.15  ? 320 GLY C CA  1 
ATOM   11065 C C   . GLY C 1 320 ? 63.544  26.640  -24.703 1.00 89.67  ? 320 GLY C C   1 
ATOM   11066 O O   . GLY C 1 320 ? 63.149  27.147  -25.753 1.00 87.56  ? 320 GLY C O   1 
ATOM   11067 N N   . LEU C 1 321 ? 64.638  25.860  -24.577 1.00 89.23  ? 321 LEU C N   1 
ATOM   11068 C CA  . LEU C 1 321 ? 65.549  25.562  -25.674 1.00 86.78  ? 321 LEU C CA  1 
ATOM   11069 C C   . LEU C 1 321 ? 65.426  24.096  -26.060 1.00 85.58  ? 321 LEU C C   1 
ATOM   11070 O O   . LEU C 1 321 ? 65.385  23.233  -25.188 1.00 86.44  ? 321 LEU C O   1 
ATOM   11071 C CB  . LEU C 1 321 ? 66.988  25.839  -25.251 1.00 87.11  ? 321 LEU C CB  1 
ATOM   11072 C CG  . LEU C 1 321 ? 67.387  27.301  -25.085 1.00 87.57  ? 321 LEU C CG  1 
ATOM   11073 C CD1 . LEU C 1 321 ? 68.741  27.366  -24.401 1.00 88.71  ? 321 LEU C CD1 1 
ATOM   11074 C CD2 . LEU C 1 321 ? 67.426  27.976  -26.435 1.00 85.62  ? 321 LEU C CD2 1 
ATOM   11075 N N   . ILE C 1 322 ? 65.443  23.832  -27.369 1.00 83.33  ? 322 ILE C N   1 
ATOM   11076 C CA  . ILE C 1 322 ? 65.473  22.466  -27.864 1.00 82.56  ? 322 ILE C CA  1 
ATOM   11077 C C   . ILE C 1 322 ? 66.881  22.171  -28.394 1.00 82.41  ? 322 ILE C C   1 
ATOM   11078 O O   . ILE C 1 322 ? 67.371  22.873  -29.285 1.00 80.23  ? 322 ILE C O   1 
ATOM   11079 C CB  . ILE C 1 322 ? 64.367  22.265  -28.915 1.00 80.62  ? 322 ILE C CB  1 
ATOM   11080 C CG1 . ILE C 1 322 ? 62.996  22.574  -28.309 1.00 82.01  ? 322 ILE C CG1 1 
ATOM   11081 C CG2 . ILE C 1 322 ? 64.419  20.856  -29.502 1.00 79.55  ? 322 ILE C CG2 1 
ATOM   11082 C CD1 . ILE C 1 322 ? 61.982  23.178  -29.267 1.00 80.87  ? 322 ILE C CD1 1 
ATOM   11083 N N   . ILE C 1 323 ? 67.527  21.144  -27.804 1.00 83.97  ? 323 ILE C N   1 
ATOM   11084 C CA  . ILE C 1 323 ? 68.870  20.713  -28.183 1.00 83.91  ? 323 ILE C CA  1 
ATOM   11085 C C   . ILE C 1 323 ? 68.780  19.424  -29.009 1.00 82.61  ? 323 ILE C C   1 
ATOM   11086 O O   . ILE C 1 323 ? 69.618  19.181  -29.885 1.00 81.36  ? 323 ILE C O   1 
ATOM   11087 C CB  . ILE C 1 323 ? 69.796  20.536  -26.958 1.00 86.55  ? 323 ILE C CB  1 
ATOM   11088 C CG1 . ILE C 1 323 ? 70.022  21.839  -26.170 1.00 88.15  ? 323 ILE C CG1 1 
ATOM   11089 C CG2 . ILE C 1 323 ? 71.137  19.942  -27.383 1.00 86.31  ? 323 ILE C CG2 1 
ATOM   11090 C CD1 . ILE C 1 323 ? 68.881  22.220  -25.241 1.00 90.20  ? 323 ILE C CD1 1 
ATOM   11091 N N   . SER C 1 324 ? 67.777  18.587  -28.712 1.00 81.73  ? 324 SER C N   1 
ATOM   11092 C CA  . SER C 1 324 ? 67.506  17.418  -29.522 1.00 80.10  ? 324 SER C CA  1 
ATOM   11093 C C   . SER C 1 324 ? 66.018  17.121  -29.428 1.00 80.21  ? 324 SER C C   1 
ATOM   11094 O O   . SER C 1 324 ? 65.435  17.226  -28.351 1.00 81.04  ? 324 SER C O   1 
ATOM   11095 C CB  . SER C 1 324 ? 68.324  16.235  -29.088 1.00 80.73  ? 324 SER C CB  1 
ATOM   11096 O OG  . SER C 1 324 ? 69.674  16.629  -28.908 1.00 80.50  ? 324 SER C OG  1 
ATOM   11097 N N   . PRO C 1 325 ? 65.362  16.730  -30.540 1.00 78.91  ? 325 PRO C N   1 
ATOM   11098 C CA  . PRO C 1 325 ? 66.021  16.588  -31.842 1.00 77.67  ? 325 PRO C CA  1 
ATOM   11099 C C   . PRO C 1 325 ? 66.539  17.909  -32.404 1.00 76.44  ? 325 PRO C C   1 
ATOM   11100 O O   . PRO C 1 325 ? 66.120  18.969  -31.954 1.00 77.13  ? 325 PRO C O   1 
ATOM   11101 C CB  . PRO C 1 325 ? 64.967  15.981  -32.780 1.00 76.75  ? 325 PRO C CB  1 
ATOM   11102 C CG  . PRO C 1 325 ? 63.685  15.987  -32.004 1.00 77.85  ? 325 PRO C CG  1 
ATOM   11103 C CD  . PRO C 1 325 ? 63.945  16.388  -30.572 1.00 79.17  ? 325 PRO C CD  1 
ATOM   11104 N N   . LYS C 1 326 ? 67.447  17.818  -33.388 1.00 75.25  ? 326 LYS C N   1 
ATOM   11105 C CA  . LYS C 1 326 ? 67.954  18.984  -34.093 1.00 73.61  ? 326 LYS C CA  1 
ATOM   11106 C C   . LYS C 1 326 ? 67.172  19.204  -35.384 1.00 73.11  ? 326 LYS C C   1 
ATOM   11107 O O   . LYS C 1 326 ? 66.798  18.245  -36.065 1.00 73.28  ? 326 LYS C O   1 
ATOM   11108 C CB  . LYS C 1 326 ? 69.449  18.835  -34.328 1.00 72.35  ? 326 LYS C CB  1 
ATOM   11109 C CG  . LYS C 1 326 ? 70.205  18.871  -33.012 1.00 73.59  ? 326 LYS C CG  1 
ATOM   11110 C CD  . LYS C 1 326 ? 71.629  18.324  -33.088 1.00 73.58  ? 326 LYS C CD  1 
ATOM   11111 C CE  . LYS C 1 326 ? 72.512  18.689  -31.923 1.00 74.79  ? 326 LYS C CE  1 
ATOM   11112 N NZ  . LYS C 1 326 ? 72.165  17.989  -30.683 1.00 76.42  ? 326 LYS C NZ  1 
ATOM   11113 N N   . ASN C 1 327 ? 66.907  20.488  -35.667 1.00 72.03  ? 327 ASN C N   1 
ATOM   11114 C CA  . ASN C 1 327 ? 66.221  20.905  -36.870 1.00 70.86  ? 327 ASN C CA  1 
ATOM   11115 C C   . ASN C 1 327 ? 67.065  20.589  -38.094 1.00 69.47  ? 327 ASN C C   1 
ATOM   11116 O O   . ASN C 1 327 ? 68.291  20.676  -38.059 1.00 69.51  ? 327 ASN C O   1 
ATOM   11117 C CB  . ASN C 1 327 ? 65.910  22.392  -36.845 1.00 71.99  ? 327 ASN C CB  1 
ATOM   11118 C CG  . ASN C 1 327 ? 65.027  22.795  -38.000 1.00 71.83  ? 327 ASN C CG  1 
ATOM   11119 O OD1 . ASN C 1 327 ? 63.941  22.229  -38.166 1.00 73.75  ? 327 ASN C OD1 1 
ATOM   11120 N ND2 . ASN C 1 327 ? 65.466  23.740  -38.814 1.00 71.20  ? 327 ASN C ND2 1 
ATOM   11121 N N   . LYS C 1 328 ? 66.364  20.224  -39.169 1.00 68.43  ? 328 LYS C N   1 
ATOM   11122 C CA  . LYS C 1 328 ? 66.934  19.541  -40.320 1.00 67.72  ? 328 LYS C CA  1 
ATOM   11123 C C   . LYS C 1 328 ? 67.879  18.424  -39.885 1.00 68.37  ? 328 LYS C C   1 
ATOM   11124 O O   . LYS C 1 328 ? 68.997  18.350  -40.375 1.00 67.32  ? 328 LYS C O   1 
ATOM   11125 C CB  . LYS C 1 328 ? 67.662  20.482  -41.276 1.00 66.58  ? 328 LYS C CB  1 
ATOM   11126 C CG  . LYS C 1 328 ? 66.832  21.649  -41.717 1.00 66.32  ? 328 LYS C CG  1 
ATOM   11127 C CD  . LYS C 1 328 ? 65.489  21.331  -42.355 1.00 66.61  ? 328 LYS C CD  1 
ATOM   11128 C CE  . LYS C 1 328 ? 64.668  22.563  -42.646 1.00 66.33  ? 328 LYS C CE  1 
ATOM   11129 N NZ  . LYS C 1 328 ? 65.397  23.513  -43.497 1.00 65.82  ? 328 LYS C NZ  1 
ATOM   11130 N N   . SER C 1 329 ? 67.395  17.548  -38.993 1.00 69.97  ? 329 SER C N   1 
ATOM   11131 C CA  . SER C 1 329 ? 68.044  16.271  -38.741 1.00 70.95  ? 329 SER C CA  1 
ATOM   11132 C C   . SER C 1 329 ? 67.329  15.133  -39.488 1.00 71.13  ? 329 SER C C   1 
ATOM   11133 O O   . SER C 1 329 ? 66.147  15.211  -39.820 1.00 70.02  ? 329 SER C O   1 
ATOM   11134 C CB  . SER C 1 329 ? 68.196  15.992  -37.247 1.00 72.25  ? 329 SER C CB  1 
ATOM   11135 O OG  . SER C 1 329 ? 66.994  15.565  -36.632 1.00 73.42  ? 329 SER C OG  1 
ATOM   11136 N N   . ILE C 1 330 ? 68.120  14.090  -39.782 1.00 72.41  ? 330 ILE C N   1 
ATOM   11137 C CA  . ILE C 1 330 ? 67.716  12.893  -40.501 1.00 72.77  ? 330 ILE C CA  1 
ATOM   11138 C C   . ILE C 1 330 ? 67.703  11.740  -39.509 1.00 74.11  ? 330 ILE C C   1 
ATOM   11139 O O   . ILE C 1 330 ? 68.717  11.462  -38.886 1.00 74.15  ? 330 ILE C O   1 
ATOM   11140 C CB  . ILE C 1 330 ? 68.686  12.645  -41.669 1.00 72.50  ? 330 ILE C CB  1 
ATOM   11141 C CG1 . ILE C 1 330 ? 68.526  13.728  -42.735 1.00 71.95  ? 330 ILE C CG1 1 
ATOM   11142 C CG2 . ILE C 1 330 ? 68.519  11.246  -42.249 1.00 73.57  ? 330 ILE C CG2 1 
ATOM   11143 C CD1 . ILE C 1 330 ? 69.411  13.545  -43.952 1.00 72.07  ? 330 ILE C CD1 1 
ATOM   11144 N N   . HIS C 1 331 ? 66.547  11.095  -39.349 1.00 75.82  ? 331 HIS C N   1 
ATOM   11145 C CA  . HIS C 1 331 ? 66.432  9.962   -38.447 1.00 78.61  ? 331 HIS C CA  1 
ATOM   11146 C C   . HIS C 1 331 ? 65.998  8.732   -39.246 1.00 80.11  ? 331 HIS C C   1 
ATOM   11147 O O   . HIS C 1 331 ? 65.127  8.814   -40.111 1.00 80.05  ? 331 HIS C O   1 
ATOM   11148 C CB  . HIS C 1 331 ? 65.537  10.335  -37.262 1.00 79.57  ? 331 HIS C CB  1 
ATOM   11149 C CG  . HIS C 1 331 ? 66.071  11.451  -36.429 1.00 79.61  ? 331 HIS C CG  1 
ATOM   11150 N ND1 . HIS C 1 331 ? 66.626  11.264  -35.181 1.00 81.36  ? 331 HIS C ND1 1 
ATOM   11151 C CD2 . HIS C 1 331 ? 66.111  12.772  -36.655 1.00 78.77  ? 331 HIS C CD2 1 
ATOM   11152 C CE1 . HIS C 1 331 ? 66.993  12.443  -34.682 1.00 80.98  ? 331 HIS C CE1 1 
ATOM   11153 N NE2 . HIS C 1 331 ? 66.696  13.376  -35.564 1.00 79.15  ? 331 HIS C NE2 1 
ATOM   11154 N N   . THR C 1 332 ? 66.654  7.599   -38.974 1.00 82.05  ? 332 THR C N   1 
ATOM   11155 C CA  . THR C 1 332 ? 66.329  6.340   -39.625 1.00 84.79  ? 332 THR C CA  1 
ATOM   11156 C C   . THR C 1 332 ? 65.853  5.385   -38.542 1.00 87.55  ? 332 THR C C   1 
ATOM   11157 O O   . THR C 1 332 ? 66.129  4.201   -38.617 1.00 89.70  ? 332 THR C O   1 
ATOM   11158 C CB  . THR C 1 332 ? 67.532  5.745   -40.365 1.00 85.18  ? 332 THR C CB  1 
ATOM   11159 O OG1 . THR C 1 332 ? 68.600  5.809   -39.429 1.00 86.72  ? 332 THR C OG1 1 
ATOM   11160 C CG2 . THR C 1 332 ? 67.972  6.519   -41.595 1.00 83.54  ? 332 THR C CG2 1 
ATOM   11161 N N   . ASN C 1 333 ? 65.140  5.923   -37.551 1.00 88.91  ? 333 ASN C N   1 
ATOM   11162 C CA  . ASN C 1 333 ? 64.854  5.215   -36.321 1.00 91.93  ? 333 ASN C CA  1 
ATOM   11163 C C   . ASN C 1 333 ? 63.586  5.801   -35.709 1.00 91.73  ? 333 ASN C C   1 
ATOM   11164 O O   . ASN C 1 333 ? 63.308  6.997   -35.841 1.00 89.51  ? 333 ASN C O   1 
ATOM   11165 C CB  . ASN C 1 333 ? 66.056  5.301   -35.393 1.00 94.71  ? 333 ASN C CB  1 
ATOM   11166 C CG  . ASN C 1 333 ? 65.985  4.304   -34.267 1.00 100.93 ? 333 ASN C CG  1 
ATOM   11167 O OD1 . ASN C 1 333 ? 66.031  3.089   -34.498 1.00 107.78 ? 333 ASN C OD1 1 
ATOM   11168 N ND2 . ASN C 1 333 ? 65.902  4.793   -33.041 1.00 103.15 ? 333 ASN C ND2 1 
ATOM   11169 N N   . THR C 1 334 ? 62.809  4.945   -35.044 1.00 93.97  ? 334 THR C N   1 
ATOM   11170 C CA  . THR C 1 334 ? 61.528  5.370   -34.507 1.00 94.35  ? 334 THR C CA  1 
ATOM   11171 C C   . THR C 1 334 ? 61.720  5.998   -33.125 1.00 95.91  ? 334 THR C C   1 
ATOM   11172 O O   . THR C 1 334 ? 60.780  6.613   -32.614 1.00 97.67  ? 334 THR C O   1 
ATOM   11173 C CB  . THR C 1 334 ? 60.526  4.216   -34.463 1.00 96.33  ? 334 THR C CB  1 
ATOM   11174 O OG1 . THR C 1 334 ? 60.974  3.383   -33.399 1.00 97.89  ? 334 THR C OG1 1 
ATOM   11175 C CG2 . THR C 1 334 ? 60.390  3.502   -35.798 1.00 96.17  ? 334 THR C CG2 1 
ATOM   11176 N N   . LYS C 1 335 ? 62.920  5.856   -32.529 1.00 96.36  ? 335 LYS C N   1 
ATOM   11177 C CA  . LYS C 1 335 ? 63.234  6.491   -31.252 1.00 96.72  ? 335 LYS C CA  1 
ATOM   11178 C C   . LYS C 1 335 ? 64.073  7.751   -31.486 1.00 93.59  ? 335 LYS C C   1 
ATOM   11179 O O   . LYS C 1 335 ? 65.108  7.696   -32.130 1.00 92.43  ? 335 LYS C O   1 
ATOM   11180 C CB  . LYS C 1 335 ? 63.898  5.491   -30.296 1.00 99.78  ? 335 LYS C CB  1 
ATOM   11181 C CG  . LYS C 1 335 ? 63.055  4.270   -29.936 1.00 103.80 ? 335 LYS C CG  1 
ATOM   11182 C CD  . LYS C 1 335 ? 61.837  4.599   -29.073 1.00 106.45 ? 335 LYS C CD  1 
ATOM   11183 C CE  . LYS C 1 335 ? 60.979  3.426   -28.733 1.00 109.67 ? 335 LYS C CE  1 
ATOM   11184 N NZ  . LYS C 1 335 ? 60.116  3.088   -29.866 1.00 110.14 ? 335 LYS C NZ  1 
ATOM   11185 N N   . ILE C 1 336 ? 63.608  8.890   -30.953 1.00 93.20  ? 336 ILE C N   1 
ATOM   11186 C CA  . ILE C 1 336 ? 64.225  10.190  -31.185 1.00 91.11  ? 336 ILE C CA  1 
ATOM   11187 C C   . ILE C 1 336 ? 64.685  10.783  -29.854 1.00 91.15  ? 336 ILE C C   1 
ATOM   11188 O O   . ILE C 1 336 ? 63.861  11.199  -29.044 1.00 90.99  ? 336 ILE C O   1 
ATOM   11189 C CB  . ILE C 1 336 ? 63.244  11.146  -31.885 1.00 89.98  ? 336 ILE C CB  1 
ATOM   11190 C CG1 . ILE C 1 336 ? 62.687  10.566  -33.185 1.00 90.17  ? 336 ILE C CG1 1 
ATOM   11191 C CG2 . ILE C 1 336 ? 63.889  12.509  -32.109 1.00 88.48  ? 336 ILE C CG2 1 
ATOM   11192 C CD1 . ILE C 1 336 ? 63.720  10.357  -34.276 1.00 89.32  ? 336 ILE C CD1 1 
ATOM   11193 N N   . PRO C 1 337 ? 66.010  10.835  -29.576 1.00 90.63  ? 337 PRO C N   1 
ATOM   11194 C CA  . PRO C 1 337 ? 66.504  11.451  -28.347 1.00 90.47  ? 337 PRO C CA  1 
ATOM   11195 C C   . PRO C 1 337 ? 65.927  12.856  -28.233 1.00 88.63  ? 337 PRO C C   1 
ATOM   11196 O O   . PRO C 1 337 ? 65.862  13.571  -29.232 1.00 87.15  ? 337 PRO C O   1 
ATOM   11197 C CB  . PRO C 1 337 ? 68.033  11.440  -28.475 1.00 89.96  ? 337 PRO C CB  1 
ATOM   11198 C CG  . PRO C 1 337 ? 68.324  10.370  -29.505 1.00 90.02  ? 337 PRO C CG  1 
ATOM   11199 C CD  . PRO C 1 337 ? 67.088  10.248  -30.388 1.00 89.69  ? 337 PRO C CD  1 
ATOM   11200 N N   . LEU C 1 338 ? 65.498  13.207  -27.013 1.00 89.38  ? 338 LEU C N   1 
ATOM   11201 C CA  . LEU C 1 338 ? 64.931  14.512  -26.699 1.00 88.84  ? 338 LEU C CA  1 
ATOM   11202 C C   . LEU C 1 338 ? 65.800  15.189  -25.640 1.00 89.17  ? 338 LEU C C   1 
ATOM   11203 O O   . LEU C 1 338 ? 66.023  14.639  -24.569 1.00 91.16  ? 338 LEU C O   1 
ATOM   11204 C CB  . LEU C 1 338 ? 63.484  14.369  -26.209 1.00 89.87  ? 338 LEU C CB  1 
ATOM   11205 C CG  . LEU C 1 338 ? 62.742  15.661  -25.825 1.00 89.41  ? 338 LEU C CG  1 
ATOM   11206 C CD1 . LEU C 1 338 ? 62.363  16.460  -27.046 1.00 86.96  ? 338 LEU C CD1 1 
ATOM   11207 C CD2 . LEU C 1 338 ? 61.497  15.401  -24.986 1.00 91.23  ? 338 LEU C CD2 1 
ATOM   11208 N N   . GLU C 1 339 ? 66.242  16.412  -25.918 1.00 87.71  ? 339 GLU C N   1 
ATOM   11209 C CA  . GLU C 1 339 ? 67.051  17.147  -24.964 1.00 88.78  ? 339 GLU C CA  1 
ATOM   11210 C C   . GLU C 1 339 ? 66.541  18.581  -24.861 1.00 88.03  ? 339 GLU C C   1 
ATOM   11211 O O   . GLU C 1 339 ? 66.348  19.247  -25.876 1.00 85.23  ? 339 GLU C O   1 
ATOM   11212 C CB  . GLU C 1 339 ? 68.512  17.085  -25.409 1.00 88.25  ? 339 GLU C CB  1 
ATOM   11213 C CG  . GLU C 1 339 ? 69.104  15.682  -25.335 1.00 88.88  ? 339 GLU C CG  1 
ATOM   11214 C CD  . GLU C 1 339 ? 70.586  15.651  -25.642 1.00 88.32  ? 339 GLU C CD  1 
ATOM   11215 O OE1 . GLU C 1 339 ? 71.331  16.349  -24.920 1.00 89.09  ? 339 GLU C OE1 1 
ATOM   11216 O OE2 . GLU C 1 339 ? 70.986  14.942  -26.596 1.00 87.31  ? 339 GLU C OE2 1 
ATOM   11217 N N   . LEU C 1 340 ? 66.363  19.048  -23.621 1.00 90.26  ? 340 LEU C N   1 
ATOM   11218 C CA  . LEU C 1 340 ? 65.791  20.360  -23.379 1.00 91.47  ? 340 LEU C CA  1 
ATOM   11219 C C   . LEU C 1 340 ? 66.540  21.077  -22.251 1.00 92.87  ? 340 LEU C C   1 
ATOM   11220 O O   . LEU C 1 340 ? 66.920  20.448  -21.260 1.00 94.21  ? 340 LEU C O   1 
ATOM   11221 C CB  . LEU C 1 340 ? 64.305  20.202  -23.042 1.00 93.58  ? 340 LEU C CB  1 
ATOM   11222 C CG  . LEU C 1 340 ? 63.339  19.751  -24.154 1.00 92.84  ? 340 LEU C CG  1 
ATOM   11223 C CD1 . LEU C 1 340 ? 61.908  19.934  -23.676 1.00 94.01  ? 340 LEU C CD1 1 
ATOM   11224 C CD2 . LEU C 1 340 ? 63.465  20.466  -25.492 1.00 90.90  ? 340 LEU C CD2 1 
ATOM   11225 N N   . TYR C 1 341 ? 66.720  22.404  -22.421 1.00 92.22  ? 341 TYR C N   1 
ATOM   11226 C CA  . TYR C 1 341 ? 67.089  23.313  -21.339 1.00 94.02  ? 341 TYR C CA  1 
ATOM   11227 C C   . TYR C 1 341 ? 65.931  24.288  -21.077 1.00 95.04  ? 341 TYR C C   1 
ATOM   11228 O O   . TYR C 1 341 ? 65.544  25.081  -21.939 1.00 92.65  ? 341 TYR C O   1 
ATOM   11229 C CB  . TYR C 1 341 ? 68.416  24.038  -21.606 1.00 92.95  ? 341 TYR C CB  1 
ATOM   11230 C CG  . TYR C 1 341 ? 69.069  24.524  -20.318 1.00 95.27  ? 341 TYR C CG  1 
ATOM   11231 C CD1 . TYR C 1 341 ? 69.799  23.657  -19.512 1.00 96.55  ? 341 TYR C CD1 1 
ATOM   11232 C CD2 . TYR C 1 341 ? 68.907  25.830  -19.873 1.00 96.72  ? 341 TYR C CD2 1 
ATOM   11233 C CE1 . TYR C 1 341 ? 70.366  24.076  -18.318 1.00 99.21  ? 341 TYR C CE1 1 
ATOM   11234 C CE2 . TYR C 1 341 ? 69.474  26.265  -18.683 1.00 99.37  ? 341 TYR C CE2 1 
ATOM   11235 C CZ  . TYR C 1 341 ? 70.213  25.388  -17.905 1.00 100.58 ? 341 TYR C CZ  1 
ATOM   11236 O OH  . TYR C 1 341 ? 70.784  25.793  -16.727 1.00 102.82 ? 341 TYR C OH  1 
ATOM   11237 N N   . ASN C 1 342 ? 65.380  24.205  -19.861 1.00 98.29  ? 342 ASN C N   1 
ATOM   11238 C CA  . ASN C 1 342 ? 64.191  24.940  -19.474 1.00 100.64 ? 342 ASN C CA  1 
ATOM   11239 C C   . ASN C 1 342 ? 64.515  25.809  -18.267 1.00 104.82 ? 342 ASN C C   1 
ATOM   11240 O O   . ASN C 1 342 ? 65.040  25.302  -17.275 1.00 107.06 ? 342 ASN C O   1 
ATOM   11241 C CB  . ASN C 1 342 ? 63.049  24.036  -19.017 1.00 101.56 ? 342 ASN C CB  1 
ATOM   11242 C CG  . ASN C 1 342 ? 62.554  23.081  -20.077 1.00 99.05  ? 342 ASN C CG  1 
ATOM   11243 O OD1 . ASN C 1 342 ? 62.644  21.864  -19.897 1.00 98.54  ? 342 ASN C OD1 1 
ATOM   11244 N ND2 . ASN C 1 342 ? 61.979  23.599  -21.153 1.00 97.48  ? 342 ASN C ND2 1 
ATOM   11245 N N   . ASP C 1 343 ? 64.162  27.097  -18.346 1.00 106.42 ? 343 ASP C N   1 
ATOM   11246 C CA  . ASP C 1 343 ? 64.236  27.969  -17.189 1.00 110.65 ? 343 ASP C CA  1 
ATOM   11247 C C   . ASP C 1 343 ? 62.985  27.739  -16.343 1.00 112.85 ? 343 ASP C C   1 
ATOM   11248 O O   . ASP C 1 343 ? 62.101  26.961  -16.712 1.00 112.27 ? 343 ASP C O   1 
ATOM   11249 C CB  . ASP C 1 343 ? 64.377  29.422  -17.602 1.00 112.38 ? 343 ASP C CB  1 
ATOM   11250 C CG  . ASP C 1 343 ? 63.051  30.063  -17.967 1.00 115.43 ? 343 ASP C CG  1 
ATOM   11251 O OD1 . ASP C 1 343 ? 62.399  29.544  -18.899 1.00 115.70 ? 343 ASP C OD1 1 
ATOM   11252 O OD2 . ASP C 1 343 ? 62.649  31.020  -17.268 1.00 120.90 ? 343 ASP C OD2 1 
ATOM   11253 N N   . LYS C 1 344 ? 62.890  28.479  -15.234 1.00 115.12 ? 344 LYS C N   1 
ATOM   11254 C CA  . LYS C 1 344 ? 61.984  28.139  -14.150 1.00 117.46 ? 344 LYS C CA  1 
ATOM   11255 C C   . LYS C 1 344 ? 60.530  28.475  -14.498 1.00 116.61 ? 344 LYS C C   1 
ATOM   11256 O O   . LYS C 1 344 ? 59.611  28.134  -13.747 1.00 117.72 ? 344 LYS C O   1 
ATOM   11257 C CB  . LYS C 1 344 ? 62.474  28.878  -12.901 1.00 121.03 ? 344 LYS C CB  1 
ATOM   11258 C CG  . LYS C 1 344 ? 61.983  28.309  -11.579 1.00 124.57 ? 344 LYS C CG  1 
ATOM   11259 C CD  . LYS C 1 344 ? 62.395  29.119  -10.354 1.00 128.03 ? 344 LYS C CD  1 
ATOM   11260 C CE  . LYS C 1 344 ? 61.799  30.491  -10.335 1.00 129.15 ? 344 LYS C CE  1 
ATOM   11261 N NZ  . LYS C 1 344 ? 62.039  31.165  -9.058  1.00 133.23 ? 344 LYS C NZ  1 
ATOM   11262 N N   . ASP C 1 345 ? 60.323  29.154  -15.634 1.00 113.64 ? 345 ASP C N   1 
ATOM   11263 C CA  . ASP C 1 345 ? 58.989  29.552  -16.051 1.00 113.08 ? 345 ASP C CA  1 
ATOM   11264 C C   . ASP C 1 345 ? 58.264  28.379  -16.695 1.00 109.99 ? 345 ASP C C   1 
ATOM   11265 O O   . ASP C 1 345 ? 57.052  28.287  -16.577 1.00 110.18 ? 345 ASP C O   1 
ATOM   11266 C CB  . ASP C 1 345 ? 59.019  30.745  -16.993 1.00 112.31 ? 345 ASP C CB  1 
ATOM   11267 C CG  . ASP C 1 345 ? 59.241  32.089  -16.316 1.00 115.44 ? 345 ASP C CG  1 
ATOM   11268 O OD1 . ASP C 1 345 ? 59.559  32.086  -15.113 1.00 118.55 ? 345 ASP C OD1 1 
ATOM   11269 O OD2 . ASP C 1 345 ? 59.058  33.130  -16.982 1.00 115.57 ? 345 ASP C OD2 1 
ATOM   11270 N N   . VAL C 1 346 ? 59.009  27.502  -17.380 1.00 106.85 ? 346 VAL C N   1 
ATOM   11271 C CA  . VAL C 1 346 ? 58.408  26.388  -18.095 1.00 104.43 ? 346 VAL C CA  1 
ATOM   11272 C C   . VAL C 1 346 ? 58.007  25.302  -17.100 1.00 106.05 ? 346 VAL C C   1 
ATOM   11273 O O   . VAL C 1 346 ? 58.853  24.717  -16.424 1.00 106.47 ? 346 VAL C O   1 
ATOM   11274 C CB  . VAL C 1 346 ? 59.335  25.835  -19.188 1.00 101.45 ? 346 VAL C CB  1 
ATOM   11275 C CG1 . VAL C 1 346 ? 58.752  24.602  -19.865 1.00 99.78  ? 346 VAL C CG1 1 
ATOM   11276 C CG2 . VAL C 1 346 ? 59.665  26.905  -20.220 1.00 99.72  ? 346 VAL C CG2 1 
ATOM   11277 N N   . LYS C 1 347 ? 56.694  25.050  -17.036 1.00 106.61 ? 347 LYS C N   1 
ATOM   11278 C CA  . LYS C 1 347 ? 56.136  24.045  -16.155 1.00 108.72 ? 347 LYS C CA  1 
ATOM   11279 C C   . LYS C 1 347 ? 55.499  22.908  -16.952 1.00 107.02 ? 347 LYS C C   1 
ATOM   11280 O O   . LYS C 1 347 ? 55.074  21.937  -16.336 1.00 108.33 ? 347 LYS C O   1 
ATOM   11281 C CB  . LYS C 1 347 ? 55.124  24.704  -15.218 1.00 112.09 ? 347 LYS C CB  1 
ATOM   11282 C CG  . LYS C 1 347 ? 55.671  25.795  -14.306 1.00 114.60 ? 347 LYS C CG  1 
ATOM   11283 C CD  . LYS C 1 347 ? 56.655  25.285  -13.259 1.00 117.03 ? 347 LYS C CD  1 
ATOM   11284 C CE  . LYS C 1 347 ? 57.065  26.337  -12.268 1.00 119.97 ? 347 LYS C CE  1 
ATOM   11285 N NZ  . LYS C 1 347 ? 58.214  25.918  -11.454 1.00 121.34 ? 347 LYS C NZ  1 
ATOM   11286 N N   . LYS C 1 348 ? 55.449  23.010  -18.294 1.00 104.29 ? 348 LYS C N   1 
ATOM   11287 C CA  . LYS C 1 348 ? 54.976  21.915  -19.139 1.00 103.32 ? 348 LYS C CA  1 
ATOM   11288 C C   . LYS C 1 348 ? 55.514  22.051  -20.565 1.00 99.82  ? 348 LYS C C   1 
ATOM   11289 O O   . LYS C 1 348 ? 55.728  23.158  -21.037 1.00 98.73  ? 348 LYS C O   1 
ATOM   11290 C CB  . LYS C 1 348 ? 53.440  21.868  -19.164 1.00 105.16 ? 348 LYS C CB  1 
ATOM   11291 C CG  . LYS C 1 348 ? 52.798  20.769  -20.023 1.00 104.30 ? 348 LYS C CG  1 
ATOM   11292 C CD  . LYS C 1 348 ? 51.315  20.504  -19.771 1.00 106.43 ? 348 LYS C CD  1 
ATOM   11293 C CE  . LYS C 1 348 ? 50.409  21.598  -20.221 1.00 106.49 ? 348 LYS C CE  1 
ATOM   11294 N NZ  . LYS C 1 348 ? 49.008  21.171  -20.151 1.00 108.17 ? 348 LYS C NZ  1 
ATOM   11295 N N   . VAL C 1 349 ? 55.690  20.916  -21.261 1.00 98.60  ? 349 VAL C N   1 
ATOM   11296 C CA  . VAL C 1 349 ? 56.270  20.885  -22.602 1.00 96.03  ? 349 VAL C CA  1 
ATOM   11297 C C   . VAL C 1 349 ? 55.562  19.826  -23.445 1.00 94.50  ? 349 VAL C C   1 
ATOM   11298 O O   . VAL C 1 349 ? 55.632  18.642  -23.124 1.00 95.25  ? 349 VAL C O   1 
ATOM   11299 C CB  . VAL C 1 349 ? 57.786  20.580  -22.606 1.00 95.86  ? 349 VAL C CB  1 
ATOM   11300 C CG1 . VAL C 1 349 ? 58.344  20.505  -24.026 1.00 92.88  ? 349 VAL C CG1 1 
ATOM   11301 C CG2 . VAL C 1 349 ? 58.592  21.575  -21.775 1.00 97.41  ? 349 VAL C CG2 1 
ATOM   11302 N N   . VAL C 1 350 ? 54.984  20.242  -24.577 1.00 92.33  ? 350 VAL C N   1 
ATOM   11303 C CA  . VAL C 1 350 ? 54.152  19.357  -25.378 1.00 91.80  ? 350 VAL C CA  1 
ATOM   11304 C C   . VAL C 1 350 ? 54.674  19.362  -26.813 1.00 89.22  ? 350 VAL C C   1 
ATOM   11305 O O   . VAL C 1 350 ? 54.966  20.424  -27.359 1.00 87.84  ? 350 VAL C O   1 
ATOM   11306 C CB  . VAL C 1 350 ? 52.661  19.767  -25.298 1.00 92.50  ? 350 VAL C CB  1 
ATOM   11307 C CG1 . VAL C 1 350 ? 51.759  18.902  -26.176 1.00 91.70  ? 350 VAL C CG1 1 
ATOM   11308 C CG2 . VAL C 1 350 ? 52.150  19.775  -23.861 1.00 95.17  ? 350 VAL C CG2 1 
ATOM   11309 N N   . VAL C 1 351 ? 54.788  18.162  -27.404 1.00 88.94  ? 351 VAL C N   1 
ATOM   11310 C CA  . VAL C 1 351 ? 55.203  18.014  -28.791 1.00 87.10  ? 351 VAL C CA  1 
ATOM   11311 C C   . VAL C 1 351 ? 54.029  17.472  -29.595 1.00 87.13  ? 351 VAL C C   1 
ATOM   11312 O O   . VAL C 1 351 ? 53.404  16.498  -29.178 1.00 89.07  ? 351 VAL C O   1 
ATOM   11313 C CB  . VAL C 1 351 ? 56.419  17.087  -28.954 1.00 86.86  ? 351 VAL C CB  1 
ATOM   11314 C CG1 . VAL C 1 351 ? 56.845  16.988  -30.412 1.00 85.14  ? 351 VAL C CG1 1 
ATOM   11315 C CG2 . VAL C 1 351 ? 57.599  17.525  -28.093 1.00 87.27  ? 351 VAL C CG2 1 
ATOM   11316 N N   . LYS C 1 352 ? 53.761  18.096  -30.750 1.00 85.17  ? 352 LYS C N   1 
ATOM   11317 C CA  . LYS C 1 352 ? 52.638  17.705  -31.587 1.00 84.32  ? 352 LYS C CA  1 
ATOM   11318 C C   . LYS C 1 352 ? 53.120  17.425  -33.009 1.00 82.23  ? 352 LYS C C   1 
ATOM   11319 O O   . LYS C 1 352 ? 54.134  17.974  -33.469 1.00 79.41  ? 352 LYS C O   1 
ATOM   11320 C CB  . LYS C 1 352 ? 51.548  18.780  -31.606 1.00 84.53  ? 352 LYS C CB  1 
ATOM   11321 C CG  . LYS C 1 352 ? 50.823  18.984  -30.283 1.00 86.58  ? 352 LYS C CG  1 
ATOM   11322 C CD  . LYS C 1 352 ? 49.815  20.128  -30.279 1.00 86.63  ? 352 LYS C CD  1 
ATOM   11323 C CE  . LYS C 1 352 ? 49.460  20.530  -28.881 1.00 88.78  ? 352 LYS C CE  1 
ATOM   11324 N NZ  . LYS C 1 352 ? 48.370  21.515  -28.817 1.00 89.81  ? 352 LYS C NZ  1 
ATOM   11325 N N   . PHE C 1 353 ? 52.349  16.558  -33.681 1.00 82.02  ? 353 PHE C N   1 
ATOM   11326 C CA  . PHE C 1 353 ? 52.516  16.285  -35.098 1.00 80.73  ? 353 PHE C CA  1 
ATOM   11327 C C   . PHE C 1 353 ? 51.131  16.100  -35.709 1.00 81.85  ? 353 PHE C C   1 
ATOM   11328 O O   . PHE C 1 353 ? 50.360  15.253  -35.260 1.00 83.76  ? 353 PHE C O   1 
ATOM   11329 C CB  . PHE C 1 353 ? 53.361  15.040  -35.377 1.00 80.25  ? 353 PHE C CB  1 
ATOM   11330 C CG  . PHE C 1 353 ? 53.497  14.668  -36.851 1.00 79.14  ? 353 PHE C CG  1 
ATOM   11331 C CD1 . PHE C 1 353 ? 54.138  15.518  -37.751 1.00 77.88  ? 353 PHE C CD1 1 
ATOM   11332 C CD2 . PHE C 1 353 ? 53.036  13.448  -37.332 1.00 79.77  ? 353 PHE C CD2 1 
ATOM   11333 C CE1 . PHE C 1 353 ? 54.283  15.166  -39.092 1.00 76.95  ? 353 PHE C CE1 1 
ATOM   11334 C CE2 . PHE C 1 353 ? 53.173  13.108  -38.676 1.00 79.05  ? 353 PHE C CE2 1 
ATOM   11335 C CZ  . PHE C 1 353 ? 53.792  13.966  -39.552 1.00 77.50  ? 353 PHE C CZ  1 
ATOM   11336 N N   . ARG C 1 354 ? 50.847  16.882  -36.758 1.00 81.27  ? 354 ARG C N   1 
ATOM   11337 C CA  . ARG C 1 354 ? 49.523  16.954  -37.359 1.00 81.85  ? 354 ARG C CA  1 
ATOM   11338 C C   . ARG C 1 354 ? 48.496  17.136  -36.246 1.00 83.26  ? 354 ARG C C   1 
ATOM   11339 O O   . ARG C 1 354 ? 47.612  16.299  -36.062 1.00 85.15  ? 354 ARG C O   1 
ATOM   11340 C CB  . ARG C 1 354 ? 49.310  15.696  -38.211 1.00 82.25  ? 354 ARG C CB  1 
ATOM   11341 C CG  . ARG C 1 354 ? 50.401  15.474  -39.249 1.00 80.81  ? 354 ARG C CG  1 
ATOM   11342 C CD  . ARG C 1 354 ? 50.055  14.395  -40.243 1.00 81.24  ? 354 ARG C CD  1 
ATOM   11343 N NE  . ARG C 1 354 ? 51.119  14.228  -41.238 1.00 80.25  ? 354 ARG C NE  1 
ATOM   11344 C CZ  . ARG C 1 354 ? 51.179  13.196  -42.060 1.00 81.33  ? 354 ARG C CZ  1 
ATOM   11345 N NH1 . ARG C 1 354 ? 50.157  12.361  -42.128 1.00 83.67  ? 354 ARG C NH1 1 
ATOM   11346 N NH2 . ARG C 1 354 ? 52.242  12.985  -42.806 1.00 80.44  ? 354 ARG C NH2 1 
ATOM   11347 N N   . ASP C 1 355 ? 48.702  18.174  -35.432 1.00 82.89  ? 355 ASP C N   1 
ATOM   11348 C CA  . ASP C 1 355 ? 47.783  18.499  -34.357 1.00 84.52  ? 355 ASP C CA  1 
ATOM   11349 C C   . ASP C 1 355 ? 47.475  17.281  -33.477 1.00 87.08  ? 355 ASP C C   1 
ATOM   11350 O O   . ASP C 1 355 ? 46.344  17.123  -33.022 1.00 89.87  ? 355 ASP C O   1 
ATOM   11351 C CB  . ASP C 1 355 ? 46.509  19.087  -34.950 1.00 84.37  ? 355 ASP C CB  1 
ATOM   11352 C CG  . ASP C 1 355 ? 46.725  20.192  -35.972 1.00 82.35  ? 355 ASP C CG  1 
ATOM   11353 O OD1 . ASP C 1 355 ? 46.967  21.344  -35.551 1.00 81.55  ? 355 ASP C OD1 1 
ATOM   11354 O OD2 . ASP C 1 355 ? 46.703  19.877  -37.180 1.00 81.24  ? 355 ASP C OD2 1 
ATOM   11355 N N   . LYS C 1 356 ? 48.454  16.404  -33.230 1.00 87.33  ? 356 LYS C N   1 
ATOM   11356 C CA  . LYS C 1 356 ? 48.251  15.271  -32.339 1.00 89.31  ? 356 LYS C CA  1 
ATOM   11357 C C   . LYS C 1 356 ? 49.432  15.173  -31.377 1.00 88.94  ? 356 LYS C C   1 
ATOM   11358 O O   . LYS C 1 356 ? 50.589  15.191  -31.798 1.00 88.02  ? 356 LYS C O   1 
ATOM   11359 C CB  . LYS C 1 356 ? 48.059  13.958  -33.106 1.00 90.83  ? 356 LYS C CB  1 
ATOM   11360 C CG  . LYS C 1 356 ? 47.868  12.736  -32.200 1.00 94.38  ? 356 LYS C CG  1 
ATOM   11361 C CD  . LYS C 1 356 ? 47.334  11.462  -32.850 1.00 96.60  ? 356 LYS C CD  1 
ATOM   11362 C CE  . LYS C 1 356 ? 47.430  10.267  -31.931 1.00 99.77  ? 356 LYS C CE  1 
ATOM   11363 N NZ  . LYS C 1 356 ? 47.153  8.971   -32.569 1.00 101.18 ? 356 LYS C NZ  1 
ATOM   11364 N N   . VAL C 1 357 ? 49.124  15.065  -30.081 1.00 90.07  ? 357 VAL C N   1 
ATOM   11365 C CA  . VAL C 1 357 ? 50.139  15.030  -29.040 1.00 90.22  ? 357 VAL C CA  1 
ATOM   11366 C C   . VAL C 1 357 ? 50.949  13.745  -29.166 1.00 89.93  ? 357 VAL C C   1 
ATOM   11367 O O   . VAL C 1 357 ? 50.379  12.675  -29.305 1.00 91.05  ? 357 VAL C O   1 
ATOM   11368 C CB  . VAL C 1 357 ? 49.508  15.152  -27.638 1.00 92.46  ? 357 VAL C CB  1 
ATOM   11369 C CG1 . VAL C 1 357 ? 50.540  14.911  -26.540 1.00 93.55  ? 357 VAL C CG1 1 
ATOM   11370 C CG2 . VAL C 1 357 ? 48.809  16.492  -27.435 1.00 92.23  ? 357 VAL C CG2 1 
ATOM   11371 N N   . ILE C 1 358 ? 52.278  13.861  -29.105 1.00 89.28  ? 358 ILE C N   1 
ATOM   11372 C CA  . ILE C 1 358 ? 53.150  12.687  -29.151 1.00 89.93  ? 358 ILE C CA  1 
ATOM   11373 C C   . ILE C 1 358 ? 54.189  12.704  -28.027 1.00 90.49  ? 358 ILE C C   1 
ATOM   11374 O O   . ILE C 1 358 ? 54.952  11.758  -27.898 1.00 91.22  ? 358 ILE C O   1 
ATOM   11375 C CB  . ILE C 1 358 ? 53.819  12.529  -30.534 1.00 87.73  ? 358 ILE C CB  1 
ATOM   11376 C CG1 . ILE C 1 358 ? 54.966  13.520  -30.756 1.00 85.60  ? 358 ILE C CG1 1 
ATOM   11377 C CG2 . ILE C 1 358 ? 52.762  12.610  -31.641 1.00 87.48  ? 358 ILE C CG2 1 
ATOM   11378 C CD1 . ILE C 1 358 ? 55.801  13.242  -31.994 1.00 83.58  ? 358 ILE C CD1 1 
ATOM   11379 N N   . TYR C 1 359 ? 54.225  13.774  -27.231 1.00 90.96  ? 359 TYR C N   1 
ATOM   11380 C CA  . TYR C 1 359 ? 55.005  13.824  -26.008 1.00 92.26  ? 359 TYR C CA  1 
ATOM   11381 C C   . TYR C 1 359 ? 54.349  14.857  -25.094 1.00 94.19  ? 359 TYR C C   1 
ATOM   11382 O O   . TYR C 1 359 ? 53.700  15.791  -25.581 1.00 93.66  ? 359 TYR C O   1 
ATOM   11383 C CB  . TYR C 1 359 ? 56.460  14.158  -26.360 1.00 90.57  ? 359 TYR C CB  1 
ATOM   11384 C CG  . TYR C 1 359 ? 57.379  14.180  -25.149 1.00 91.82  ? 359 TYR C CG  1 
ATOM   11385 C CD1 . TYR C 1 359 ? 57.914  13.001  -24.661 1.00 93.12  ? 359 TYR C CD1 1 
ATOM   11386 C CD2 . TYR C 1 359 ? 57.674  15.356  -24.470 1.00 92.03  ? 359 TYR C CD2 1 
ATOM   11387 C CE1 . TYR C 1 359 ? 58.716  12.986  -23.538 1.00 94.58  ? 359 TYR C CE1 1 
ATOM   11388 C CE2 . TYR C 1 359 ? 58.480  15.354  -23.343 1.00 93.57  ? 359 TYR C CE2 1 
ATOM   11389 C CZ  . TYR C 1 359 ? 59.003  14.161  -22.876 1.00 94.94  ? 359 TYR C CZ  1 
ATOM   11390 O OH  . TYR C 1 359 ? 59.811  14.052  -21.779 1.00 97.30  ? 359 TYR C OH  1 
ATOM   11391 N N   . SER C 1 360 ? 54.489  14.670  -23.775 1.00 96.59  ? 360 SER C N   1 
ATOM   11392 C CA  . SER C 1 360 ? 53.929  15.603  -22.805 1.00 98.43  ? 360 SER C CA  1 
ATOM   11393 C C   . SER C 1 360 ? 54.493  15.298  -21.424 1.00 101.55 ? 360 SER C C   1 
ATOM   11394 O O   . SER C 1 360 ? 54.303  14.201  -20.910 1.00 103.89 ? 360 SER C O   1 
ATOM   11395 C CB  . SER C 1 360 ? 52.423  15.567  -22.775 1.00 99.12  ? 360 SER C CB  1 
ATOM   11396 O OG  . SER C 1 360 ? 51.949  16.198  -21.595 1.00 101.02 ? 360 SER C OG  1 
ATOM   11397 N N   . LYS C 1 361 ? 55.187  16.273  -20.835 1.00 102.53 ? 361 LYS C N   1 
ATOM   11398 C CA  . LYS C 1 361 ? 55.816  16.081  -19.541 1.00 105.91 ? 361 LYS C CA  1 
ATOM   11399 C C   . LYS C 1 361 ? 55.689  17.378  -18.759 1.00 107.07 ? 361 LYS C C   1 
ATOM   11400 O O   . LYS C 1 361 ? 56.250  18.398  -19.157 1.00 106.24 ? 361 LYS C O   1 
ATOM   11401 C CB  . LYS C 1 361 ? 57.304  15.700  -19.649 1.00 106.08 ? 361 LYS C CB  1 
ATOM   11402 C CG  . LYS C 1 361 ? 57.865  14.856  -18.491 1.00 109.62 ? 361 LYS C CG  1 
ATOM   11403 C CD  . LYS C 1 361 ? 57.130  13.519  -18.320 1.00 112.03 ? 361 LYS C CD  1 
ATOM   11404 C CE  . LYS C 1 361 ? 57.532  12.623  -17.182 1.00 114.69 ? 361 LYS C CE  1 
ATOM   11405 N NZ  . LYS C 1 361 ? 58.847  12.017  -17.407 1.00 113.68 ? 361 LYS C NZ  1 
ATOM   11406 N N   . ASN C 1 362 ? 54.956  17.323  -17.645 1.00 109.49 ? 362 ASN C N   1 
ATOM   11407 C CA  . ASN C 1 362 ? 54.960  18.420  -16.692 1.00 111.01 ? 362 ASN C CA  1 
ATOM   11408 C C   . ASN C 1 362 ? 56.381  18.561  -16.149 1.00 110.80 ? 362 ASN C C   1 
ATOM   11409 O O   . ASN C 1 362 ? 57.051  17.558  -15.952 1.00 111.39 ? 362 ASN C O   1 
ATOM   11410 C CB  . ASN C 1 362 ? 53.942  18.198  -15.580 1.00 114.45 ? 362 ASN C CB  1 
ATOM   11411 C CG  . ASN C 1 362 ? 52.544  17.954  -16.103 1.00 114.36 ? 362 ASN C CG  1 
ATOM   11412 O OD1 . ASN C 1 362 ? 52.064  18.679  -16.980 1.00 112.35 ? 362 ASN C OD1 1 
ATOM   11413 N ND2 . ASN C 1 362 ? 51.876  16.933  -15.588 1.00 116.66 ? 362 ASN C ND2 1 
ATOM   11414 N N   . ILE C 1 363 ? 56.845  19.799  -15.941 1.00 110.25 ? 363 ILE C N   1 
ATOM   11415 C CA  . ILE C 1 363 ? 58.209  20.057  -15.500 1.00 110.19 ? 363 ILE C CA  1 
ATOM   11416 C C   . ILE C 1 363 ? 58.184  20.410  -14.012 1.00 113.59 ? 363 ILE C C   1 
ATOM   11417 O O   . ILE C 1 363 ? 57.521  21.358  -13.600 1.00 115.31 ? 363 ILE C O   1 
ATOM   11418 C CB  . ILE C 1 363 ? 58.868  21.156  -16.365 1.00 107.71 ? 363 ILE C CB  1 
ATOM   11419 C CG1 . ILE C 1 363 ? 58.934  20.755  -17.851 1.00 104.48 ? 363 ILE C CG1 1 
ATOM   11420 C CG2 . ILE C 1 363 ? 60.249  21.557  -15.841 1.00 108.12 ? 363 ILE C CG2 1 
ATOM   11421 C CD1 . ILE C 1 363 ? 59.646  19.439  -18.132 1.00 103.77 ? 363 ILE C CD1 1 
ATOM   11422 N N   . THR C 1 364 ? 58.900  19.612  -13.209 1.00 115.09 ? 364 THR C N   1 
ATOM   11423 C CA  . THR C 1 364 ? 59.095  19.872  -11.789 1.00 118.46 ? 364 THR C CA  1 
ATOM   11424 C C   . THR C 1 364 ? 60.359  20.702  -11.597 1.00 117.95 ? 364 THR C C   1 
ATOM   11425 O O   . THR C 1 364 ? 60.360  21.700  -10.881 1.00 119.92 ? 364 THR C O   1 
ATOM   11426 C CB  . THR C 1 364 ? 59.239  18.552  -11.033 1.00 120.62 ? 364 THR C CB  1 
ATOM   11427 O OG1 . THR C 1 364 ? 58.366  17.629  -11.671 1.00 119.43 ? 364 THR C OG1 1 
ATOM   11428 C CG2 . THR C 1 364 ? 58.900  18.686  -9.559  1.00 124.84 ? 364 THR C CG2 1 
ATOM   11429 N N   . SER C 1 365 ? 61.430  20.246  -12.252 1.00 115.34 ? 365 SER C N   1 
ATOM   11430 C CA  . SER C 1 365 ? 62.782  20.683  -11.977 1.00 115.10 ? 365 SER C CA  1 
ATOM   11431 C C   . SER C 1 365 ? 63.396  21.272  -13.245 1.00 111.28 ? 365 SER C C   1 
ATOM   11432 O O   . SER C 1 365 ? 63.300  20.672  -14.315 1.00 108.24 ? 365 SER C O   1 
ATOM   11433 C CB  . SER C 1 365 ? 63.556  19.508  -11.458 1.00 116.40 ? 365 SER C CB  1 
ATOM   11434 O OG  . SER C 1 365 ? 64.887  19.862  -11.133 1.00 117.09 ? 365 SER C OG  1 
ATOM   11435 N N   . GLU C 1 366 ? 64.034  22.446  -13.107 1.00 111.52 ? 366 GLU C N   1 
ATOM   11436 C CA  . GLU C 1 366 ? 64.444  23.263  -14.242 1.00 108.60 ? 366 GLU C CA  1 
ATOM   11437 C C   . GLU C 1 366 ? 65.788  22.805  -14.788 1.00 107.36 ? 366 GLU C C   1 
ATOM   11438 O O   . GLU C 1 366 ? 66.495  22.014  -14.168 1.00 108.33 ? 366 GLU C O   1 
ATOM   11439 C CB  . GLU C 1 366 ? 64.556  24.747  -13.890 1.00 109.66 ? 366 GLU C CB  1 
ATOM   11440 C CG  . GLU C 1 366 ? 65.626  25.096  -12.858 1.00 112.10 ? 366 GLU C CG  1 
ATOM   11441 C CD  . GLU C 1 366 ? 65.691  26.586  -12.553 1.00 113.51 ? 366 GLU C CD  1 
ATOM   11442 O OE1 . GLU C 1 366 ? 65.997  27.369  -13.483 1.00 111.50 ? 366 GLU C OE1 1 
ATOM   11443 O OE2 . GLU C 1 366 ? 65.420  26.972  -11.393 1.00 116.72 ? 366 GLU C OE2 1 
ATOM   11444 N N   . GLY C 1 367 ? 66.133  23.350  -15.956 1.00 105.28 ? 367 GLY C N   1 
ATOM   11445 C CA  . GLY C 1 367 ? 67.427  23.107  -16.564 1.00 103.97 ? 367 GLY C CA  1 
ATOM   11446 C C   . GLY C 1 367 ? 67.377  21.910  -17.509 1.00 102.37 ? 367 GLY C C   1 
ATOM   11447 O O   . GLY C 1 367 ? 66.420  21.745  -18.264 1.00 100.84 ? 367 GLY C O   1 
ATOM   11448 N N   . TYR C 1 368 ? 68.435  21.089  -17.462 1.00 103.19 ? 368 TYR C N   1 
ATOM   11449 C CA  . TYR C 1 368 ? 68.620  19.995  -18.404 1.00 101.28 ? 368 TYR C CA  1 
ATOM   11450 C C   . TYR C 1 368 ? 67.574  18.924  -18.135 1.00 102.35 ? 368 TYR C C   1 
ATOM   11451 O O   . TYR C 1 368 ? 67.220  18.656  -16.992 1.00 104.77 ? 368 TYR C O   1 
ATOM   11452 C CB  . TYR C 1 368 ? 70.012  19.347  -18.344 1.00 101.01 ? 368 TYR C CB  1 
ATOM   11453 C CG  . TYR C 1 368 ? 70.235  18.220  -19.351 1.00 98.49  ? 368 TYR C CG  1 
ATOM   11454 C CD1 . TYR C 1 368 ? 70.332  18.482  -20.717 1.00 95.31  ? 368 TYR C CD1 1 
ATOM   11455 C CD2 . TYR C 1 368 ? 70.354  16.897  -18.942 1.00 99.44  ? 368 TYR C CD2 1 
ATOM   11456 C CE1 . TYR C 1 368 ? 70.530  17.470  -21.644 1.00 93.64  ? 368 TYR C CE1 1 
ATOM   11457 C CE2 . TYR C 1 368 ? 70.563  15.875  -19.859 1.00 98.06  ? 368 TYR C CE2 1 
ATOM   11458 C CZ  . TYR C 1 368 ? 70.651  16.160  -21.213 1.00 95.11  ? 368 TYR C CZ  1 
ATOM   11459 O OH  . TYR C 1 368 ? 70.862  15.164  -22.124 1.00 93.94  ? 368 TYR C OH  1 
ATOM   11460 N N   . MET C 1 369 ? 67.129  18.284  -19.211 1.00 101.01 ? 369 MET C N   1 
ATOM   11461 C CA  . MET C 1 369 ? 66.124  17.248  -19.098 1.00 102.98 ? 369 MET C CA  1 
ATOM   11462 C C   . MET C 1 369 ? 66.200  16.426  -20.386 1.00 100.75 ? 369 MET C C   1 
ATOM   11463 O O   . MET C 1 369 ? 66.349  16.997  -21.468 1.00 99.03  ? 369 MET C O   1 
ATOM   11464 C CB  . MET C 1 369 ? 64.789  17.944  -18.784 1.00 104.63 ? 369 MET C CB  1 
ATOM   11465 C CG  . MET C 1 369 ? 63.603  17.046  -18.586 1.00 106.04 ? 369 MET C CG  1 
ATOM   11466 S SD  . MET C 1 369 ? 62.736  16.972  -20.158 1.00 104.63 ? 369 MET C SD  1 
ATOM   11467 C CE  . MET C 1 369 ? 62.164  18.667  -20.301 1.00 103.59 ? 369 MET C CE  1 
ATOM   11468 N N   . ALA C 1 370 ? 66.203  15.089  -20.247 1.00 101.40 ? 370 ALA C N   1 
ATOM   11469 C CA  . ALA C 1 370 ? 66.411  14.180  -21.368 1.00 98.97  ? 370 ALA C CA  1 
ATOM   11470 C C   . ALA C 1 370 ? 65.280  13.156  -21.438 1.00 99.33  ? 370 ALA C C   1 
ATOM   11471 O O   . ALA C 1 370 ? 64.717  12.785  -20.415 1.00 101.36 ? 370 ALA C O   1 
ATOM   11472 C CB  . ALA C 1 370 ? 67.753  13.498  -21.238 1.00 98.30  ? 370 ALA C CB  1 
ATOM   11473 N N   . ASP C 1 371 ? 64.961  12.688  -22.649 1.00 97.49  ? 371 ASP C N   1 
ATOM   11474 C CA  . ASP C 1 371 ? 63.910  11.697  -22.819 1.00 98.81  ? 371 ASP C CA  1 
ATOM   11475 C C   . ASP C 1 371 ? 63.916  11.157  -24.251 1.00 97.68  ? 371 ASP C C   1 
ATOM   11476 O O   . ASP C 1 371 ? 64.814  11.464  -25.028 1.00 96.73  ? 371 ASP C O   1 
ATOM   11477 C CB  . ASP C 1 371 ? 62.560  12.295  -22.457 1.00 98.99  ? 371 ASP C CB  1 
ATOM   11478 C CG  . ASP C 1 371 ? 61.587  11.308  -21.844 1.00 100.76 ? 371 ASP C CG  1 
ATOM   11479 O OD1 . ASP C 1 371 ? 61.969  10.664  -20.851 1.00 102.83 ? 371 ASP C OD1 1 
ATOM   11480 O OD2 . ASP C 1 371 ? 60.481  11.175  -22.381 1.00 100.33 ? 371 ASP C OD2 1 
ATOM   11481 N N   . GLU C 1 372 ? 62.899  10.360  -24.601 1.00 98.70  ? 372 GLU C N   1 
ATOM   11482 C CA  . GLU C 1 372 ? 62.721  9.897   -25.968 1.00 97.43  ? 372 GLU C CA  1 
ATOM   11483 C C   . GLU C 1 372 ? 61.316  10.208  -26.482 1.00 96.14  ? 372 GLU C C   1 
ATOM   11484 O O   . GLU C 1 372 ? 60.345  10.029  -25.755 1.00 97.38  ? 372 GLU C O   1 
ATOM   11485 C CB  . GLU C 1 372 ? 62.864  8.380   -26.031 1.00 99.54  ? 372 GLU C CB  1 
ATOM   11486 C CG  . GLU C 1 372 ? 64.292  7.896   -25.830 1.00 100.91 ? 372 GLU C CG  1 
ATOM   11487 C CD  . GLU C 1 372 ? 64.354  6.391   -25.941 1.00 103.43 ? 372 GLU C CD  1 
ATOM   11488 O OE1 . GLU C 1 372 ? 63.285  5.763   -26.056 1.00 105.68 ? 372 GLU C OE1 1 
ATOM   11489 O OE2 . GLU C 1 372 ? 65.469  5.846   -25.928 1.00 105.30 ? 372 GLU C OE2 1 
ATOM   11490 N N   . LEU C 1 373 ? 61.234  10.639  -27.750 1.00 93.17  ? 373 LEU C N   1 
ATOM   11491 C CA  . LEU C 1 373 ? 59.992  10.655  -28.507 1.00 92.55  ? 373 LEU C CA  1 
ATOM   11492 C C   . LEU C 1 373 ? 59.836  9.318   -29.221 1.00 92.41  ? 373 LEU C C   1 
ATOM   11493 O O   . LEU C 1 373 ? 60.829  8.705   -29.581 1.00 91.31  ? 373 LEU C O   1 
ATOM   11494 C CB  . LEU C 1 373 ? 60.001  11.780  -29.543 1.00 90.36  ? 373 LEU C CB  1 
ATOM   11495 C CG  . LEU C 1 373 ? 60.255  13.203  -29.034 1.00 89.70  ? 373 LEU C CG  1 
ATOM   11496 C CD1 . LEU C 1 373 ? 60.549  14.126  -30.211 1.00 87.04  ? 373 LEU C CD1 1 
ATOM   11497 C CD2 . LEU C 1 373 ? 59.069  13.709  -28.217 1.00 91.09  ? 373 LEU C CD2 1 
ATOM   11498 N N   . THR C 1 374 ? 58.590  8.898   -29.466 1.00 93.36  ? 374 THR C N   1 
ATOM   11499 C CA  . THR C 1 374 ? 58.338  7.808   -30.393 1.00 93.47  ? 374 THR C CA  1 
ATOM   11500 C C   . THR C 1 374 ? 57.610  8.375   -31.606 1.00 91.47  ? 374 THR C C   1 
ATOM   11501 O O   . THR C 1 374 ? 56.697  9.188   -31.459 1.00 91.68  ? 374 THR C O   1 
ATOM   11502 C CB  . THR C 1 374 ? 57.539  6.698   -29.714 1.00 96.87  ? 374 THR C CB  1 
ATOM   11503 O OG1 . THR C 1 374 ? 58.334  6.234   -28.627 1.00 98.73  ? 374 THR C OG1 1 
ATOM   11504 C CG2 . THR C 1 374 ? 57.292  5.520   -30.638 1.00 97.82  ? 374 THR C CG2 1 
ATOM   11505 N N   . ILE C 1 375 ? 58.031  7.950   -32.801 1.00 89.68  ? 375 ILE C N   1 
ATOM   11506 C CA  . ILE C 1 375 ? 57.343  8.332   -34.025 1.00 88.26  ? 375 ILE C CA  1 
ATOM   11507 C C   . ILE C 1 375 ? 57.060  7.069   -34.825 1.00 87.88  ? 375 ILE C C   1 
ATOM   11508 O O   . ILE C 1 375 ? 57.510  5.998   -34.449 1.00 89.18  ? 375 ILE C O   1 
ATOM   11509 C CB  . ILE C 1 375 ? 58.170  9.340   -34.834 1.00 87.04  ? 375 ILE C CB  1 
ATOM   11510 C CG1 . ILE C 1 375 ? 59.537  8.756   -35.206 1.00 87.60  ? 375 ILE C CG1 1 
ATOM   11511 C CG2 . ILE C 1 375 ? 58.298  10.661  -34.076 1.00 86.44  ? 375 ILE C CG2 1 
ATOM   11512 C CD1 . ILE C 1 375 ? 60.352  9.636   -36.139 1.00 86.30  ? 375 ILE C CD1 1 
ATOM   11513 N N   . ASP C 1 376 ? 56.298  7.214   -35.910 1.00 86.51  ? 376 ASP C N   1 
ATOM   11514 C CA  . ASP C 1 376 ? 55.817  6.086   -36.684 1.00 87.26  ? 376 ASP C CA  1 
ATOM   11515 C C   . ASP C 1 376 ? 55.739  6.492   -38.149 1.00 85.52  ? 376 ASP C C   1 
ATOM   11516 O O   . ASP C 1 376 ? 54.700  6.393   -38.785 1.00 85.92  ? 376 ASP C O   1 
ATOM   11517 C CB  . ASP C 1 376 ? 54.470  5.578   -36.188 1.00 89.12  ? 376 ASP C CB  1 
ATOM   11518 C CG  . ASP C 1 376 ? 54.081  4.203   -36.717 1.00 90.95  ? 376 ASP C CG  1 
ATOM   11519 O OD1 . ASP C 1 376 ? 54.973  3.521   -37.264 1.00 90.36  ? 376 ASP C OD1 1 
ATOM   11520 O OD2 . ASP C 1 376 ? 52.886  3.834   -36.601 1.00 93.47  ? 376 ASP C OD2 1 
ATOM   11521 N N   . PRO C 1 377 ? 56.860  6.899   -38.756 1.00 84.18  ? 377 PRO C N   1 
ATOM   11522 C CA  . PRO C 1 377 ? 56.824  7.464   -40.101 1.00 83.24  ? 377 PRO C CA  1 
ATOM   11523 C C   . PRO C 1 377 ? 56.430  6.433   -41.153 1.00 85.01  ? 377 PRO C C   1 
ATOM   11524 O O   . PRO C 1 377 ? 56.797  5.266   -41.043 1.00 87.11  ? 377 PRO C O   1 
ATOM   11525 C CB  . PRO C 1 377 ? 58.274  7.966   -40.286 1.00 81.94  ? 377 PRO C CB  1 
ATOM   11526 C CG  . PRO C 1 377 ? 59.116  7.096   -39.374 1.00 82.85  ? 377 PRO C CG  1 
ATOM   11527 C CD  . PRO C 1 377 ? 58.213  6.763   -38.200 1.00 84.33  ? 377 PRO C CD  1 
ATOM   11528 N N   . VAL C 1 378 ? 55.703  6.878   -42.182 1.00 84.78  ? 378 VAL C N   1 
ATOM   11529 C CA  . VAL C 1 378 ? 55.385  6.007   -43.299 1.00 85.97  ? 378 VAL C CA  1 
ATOM   11530 C C   . VAL C 1 378 ? 56.287  6.339   -44.480 1.00 85.50  ? 378 VAL C C   1 
ATOM   11531 O O   . VAL C 1 378 ? 56.173  7.414   -45.081 1.00 83.79  ? 378 VAL C O   1 
ATOM   11532 C CB  . VAL C 1 378 ? 53.918  6.114   -43.728 1.00 87.00  ? 378 VAL C CB  1 
ATOM   11533 C CG1 . VAL C 1 378 ? 53.676  5.390   -45.047 1.00 87.95  ? 378 VAL C CG1 1 
ATOM   11534 C CG2 . VAL C 1 378 ? 52.979  5.613   -42.636 1.00 88.68  ? 378 VAL C CG2 1 
ATOM   11535 N N   . GLY C 1 379 ? 57.146  5.362   -44.819 1.00 87.38  ? 379 GLY C N   1 
ATOM   11536 C CA  . GLY C 1 379 ? 58.102  5.481   -45.911 1.00 86.18  ? 379 GLY C CA  1 
ATOM   11537 C C   . GLY C 1 379 ? 59.185  6.474   -45.535 1.00 83.46  ? 379 GLY C C   1 
ATOM   11538 O O   . GLY C 1 379 ? 59.732  6.369   -44.446 1.00 84.68  ? 379 GLY C O   1 
ATOM   11539 N N   . ILE C 1 380 ? 59.469  7.425   -46.423 1.00 80.71  ? 380 ILE C N   1 
ATOM   11540 C CA  . ILE C 1 380 ? 60.309  8.551   -46.049 1.00 78.73  ? 380 ILE C CA  1 
ATOM   11541 C C   . ILE C 1 380 ? 59.384  9.716   -45.693 1.00 77.90  ? 380 ILE C C   1 
ATOM   11542 O O   . ILE C 1 380 ? 58.491  10.068  -46.468 1.00 77.64  ? 380 ILE C O   1 
ATOM   11543 C CB  . ILE C 1 380 ? 61.305  8.903   -47.166 1.00 77.61  ? 380 ILE C CB  1 
ATOM   11544 C CG1 . ILE C 1 380 ? 62.210  7.726   -47.480 1.00 79.26  ? 380 ILE C CG1 1 
ATOM   11545 C CG2 . ILE C 1 380 ? 62.117  10.130  -46.772 1.00 76.33  ? 380 ILE C CG2 1 
ATOM   11546 C CD1 . ILE C 1 380 ? 63.199  7.947   -48.614 1.00 78.68  ? 380 ILE C CD1 1 
ATOM   11547 N N   . GLU C 1 381 ? 59.565  10.277  -44.494 1.00 76.84  ? 381 GLU C N   1 
ATOM   11548 C CA  . GLU C 1 381 ? 58.591  11.219  -43.981 1.00 76.73  ? 381 GLU C CA  1 
ATOM   11549 C C   . GLU C 1 381 ? 59.318  12.419  -43.376 1.00 74.03  ? 381 GLU C C   1 
ATOM   11550 O O   . GLU C 1 381 ? 59.919  12.312  -42.310 1.00 73.26  ? 381 GLU C O   1 
ATOM   11551 C CB  . GLU C 1 381 ? 57.610  10.508  -43.040 1.00 79.66  ? 381 GLU C CB  1 
ATOM   11552 C CG  . GLU C 1 381 ? 56.201  11.097  -43.015 1.00 81.30  ? 381 GLU C CG  1 
ATOM   11553 C CD  . GLU C 1 381 ? 55.313  10.616  -41.871 1.00 84.99  ? 381 GLU C CD  1 
ATOM   11554 O OE1 . GLU C 1 381 ? 55.774  10.771  -40.715 1.00 85.10  ? 381 GLU C OE1 1 
ATOM   11555 O OE2 . GLU C 1 381 ? 54.163  10.136  -42.102 1.00 89.42  ? 381 GLU C OE2 1 
ATOM   11556 N N   . ASP C 1 382 ? 59.247  13.551  -44.100 1.00 71.98  ? 382 ASP C N   1 
ATOM   11557 C CA  . ASP C 1 382 ? 59.390  14.880  -43.534 1.00 70.19  ? 382 ASP C CA  1 
ATOM   11558 C C   . ASP C 1 382 ? 58.275  15.165  -42.532 1.00 69.88  ? 382 ASP C C   1 
ATOM   11559 O O   . ASP C 1 382 ? 57.113  14.958  -42.827 1.00 69.75  ? 382 ASP C O   1 
ATOM   11560 C CB  . ASP C 1 382 ? 59.323  15.944  -44.612 1.00 69.68  ? 382 ASP C CB  1 
ATOM   11561 C CG  . ASP C 1 382 ? 58.078  15.944  -45.490 1.00 70.33  ? 382 ASP C CG  1 
ATOM   11562 O OD1 . ASP C 1 382 ? 57.833  14.899  -46.147 1.00 71.10  ? 382 ASP C OD1 1 
ATOM   11563 O OD2 . ASP C 1 382 ? 57.404  17.005  -45.550 1.00 69.99  ? 382 ASP C OD2 1 
ATOM   11564 N N   . MET C 1 383 ? 58.659  15.634  -41.345 1.00 69.79  ? 383 MET C N   1 
ATOM   11565 C CA  . MET C 1 383 ? 57.747  15.890  -40.244 1.00 70.83  ? 383 MET C CA  1 
ATOM   11566 C C   . MET C 1 383 ? 58.182  17.165  -39.521 1.00 70.58  ? 383 MET C C   1 
ATOM   11567 O O   . MET C 1 383 ? 59.301  17.272  -39.026 1.00 70.46  ? 383 MET C O   1 
ATOM   11568 C CB  . MET C 1 383 ? 57.769  14.770  -39.198 1.00 72.57  ? 383 MET C CB  1 
ATOM   11569 C CG  . MET C 1 383 ? 57.571  13.351  -39.733 1.00 73.81  ? 383 MET C CG  1 
ATOM   11570 S SD  . MET C 1 383 ? 58.011  12.051  -38.557 1.00 75.47  ? 383 MET C SD  1 
ATOM   11571 C CE  . MET C 1 383 ? 56.906  12.430  -37.191 1.00 76.56  ? 383 MET C CE  1 
ATOM   11572 N N   . GLU C 1 384 ? 57.292  18.154  -39.477 1.00 70.99  ? 384 GLU C N   1 
ATOM   11573 C CA  . GLU C 1 384 ? 57.474  19.278  -38.585 1.00 71.23  ? 384 GLU C CA  1 
ATOM   11574 C C   . GLU C 1 384 ? 56.914  18.940  -37.206 1.00 72.82  ? 384 GLU C C   1 
ATOM   11575 O O   . GLU C 1 384 ? 55.710  18.962  -37.021 1.00 74.47  ? 384 GLU C O   1 
ATOM   11576 C CB  . GLU C 1 384 ? 56.727  20.460  -39.179 1.00 70.98  ? 384 GLU C CB  1 
ATOM   11577 C CG  . GLU C 1 384 ? 56.713  21.678  -38.262 1.00 71.32  ? 384 GLU C CG  1 
ATOM   11578 C CD  . GLU C 1 384 ? 56.098  22.896  -38.905 1.00 70.78  ? 384 GLU C CD  1 
ATOM   11579 O OE1 . GLU C 1 384 ? 55.260  22.747  -39.819 1.00 70.36  ? 384 GLU C OE1 1 
ATOM   11580 O OE2 . GLU C 1 384 ? 56.540  23.989  -38.515 1.00 70.92  ? 384 GLU C OE2 1 
ATOM   11581 N N   . LEU C 1 385 ? 57.786  18.626  -36.247 1.00 73.59  ? 385 LEU C N   1 
ATOM   11582 C CA  . LEU C 1 385 ? 57.394  18.473  -34.856 1.00 75.34  ? 385 LEU C CA  1 
ATOM   11583 C C   . LEU C 1 385 ? 57.092  19.848  -34.276 1.00 75.45  ? 385 LEU C C   1 
ATOM   11584 O O   . LEU C 1 385 ? 57.935  20.733  -34.362 1.00 75.10  ? 385 LEU C O   1 
ATOM   11585 C CB  . LEU C 1 385 ? 58.516  17.802  -34.067 1.00 76.35  ? 385 LEU C CB  1 
ATOM   11586 C CG  . LEU C 1 385 ? 58.665  16.290  -34.244 1.00 77.38  ? 385 LEU C CG  1 
ATOM   11587 C CD1 . LEU C 1 385 ? 58.466  15.881  -35.694 1.00 76.72  ? 385 LEU C CD1 1 
ATOM   11588 C CD2 . LEU C 1 385 ? 60.035  15.845  -33.747 1.00 77.50  ? 385 LEU C CD2 1 
ATOM   11589 N N   . ALA C 1 386 ? 55.922  20.005  -33.649 1.00 76.70  ? 386 ALA C N   1 
ATOM   11590 C CA  . ALA C 1 386 ? 55.541  21.287  -33.083 1.00 77.34  ? 386 ALA C CA  1 
ATOM   11591 C C   . ALA C 1 386 ? 55.666  21.247  -31.565 1.00 79.42  ? 386 ALA C C   1 
ATOM   11592 O O   . ALA C 1 386 ? 54.931  20.524  -30.900 1.00 81.30  ? 386 ALA C O   1 
ATOM   11593 C CB  . ALA C 1 386 ? 54.146  21.639  -33.508 1.00 77.71  ? 386 ALA C CB  1 
ATOM   11594 N N   . PHE C 1 387 ? 56.603  22.037  -31.032 1.00 79.67  ? 387 PHE C N   1 
ATOM   11595 C CA  . PHE C 1 387 ? 56.814  22.100  -29.602 1.00 81.81  ? 387 PHE C CA  1 
ATOM   11596 C C   . PHE C 1 387 ? 56.033  23.259  -29.004 1.00 83.12  ? 387 PHE C C   1 
ATOM   11597 O O   . PHE C 1 387 ? 55.631  24.201  -29.691 1.00 82.78  ? 387 PHE C O   1 
ATOM   11598 C CB  . PHE C 1 387 ? 58.292  22.275  -29.281 1.00 82.40  ? 387 PHE C CB  1 
ATOM   11599 C CG  . PHE C 1 387 ? 59.110  21.004  -29.435 1.00 82.72  ? 387 PHE C CG  1 
ATOM   11600 C CD1 . PHE C 1 387 ? 59.273  20.410  -30.682 1.00 81.63  ? 387 PHE C CD1 1 
ATOM   11601 C CD2 . PHE C 1 387 ? 59.755  20.440  -28.343 1.00 84.35  ? 387 PHE C CD2 1 
ATOM   11602 C CE1 . PHE C 1 387 ? 60.033  19.261  -30.825 1.00 81.73  ? 387 PHE C CE1 1 
ATOM   11603 C CE2 . PHE C 1 387 ? 60.520  19.297  -28.493 1.00 84.64  ? 387 PHE C CE2 1 
ATOM   11604 C CZ  . PHE C 1 387 ? 60.653  18.706  -29.732 1.00 83.31  ? 387 PHE C CZ  1 
ATOM   11605 N N   . GLU C 1 388 ? 55.820  23.147  -27.695 1.00 85.03  ? 388 GLU C N   1 
ATOM   11606 C CA  . GLU C 1 388 ? 55.005  24.084  -26.954 1.00 86.77  ? 388 GLU C CA  1 
ATOM   11607 C C   . GLU C 1 388 ? 55.502  24.103  -25.515 1.00 89.15  ? 388 GLU C C   1 
ATOM   11608 O O   . GLU C 1 388 ? 55.728  23.057  -24.914 1.00 89.48  ? 388 GLU C O   1 
ATOM   11609 C CB  . GLU C 1 388 ? 53.526  23.711  -27.012 1.00 87.66  ? 388 GLU C CB  1 
ATOM   11610 C CG  . GLU C 1 388 ? 52.960  23.726  -28.427 1.00 85.99  ? 388 GLU C CG  1 
ATOM   11611 C CD  . GLU C 1 388 ? 51.486  23.380  -28.474 1.00 87.37  ? 388 GLU C CD  1 
ATOM   11612 O OE1 . GLU C 1 388 ? 50.870  23.184  -27.399 1.00 89.45  ? 388 GLU C OE1 1 
ATOM   11613 O OE2 . GLU C 1 388 ? 50.972  23.285  -29.610 1.00 86.27  ? 388 GLU C OE2 1 
ATOM   11614 N N   . PHE C 1 389 ? 55.683  25.324  -25.001 1.00 91.19  ? 389 PHE C N   1 
ATOM   11615 C CA  . PHE C 1 389 ? 56.150  25.580  -23.648 1.00 93.58  ? 389 PHE C CA  1 
ATOM   11616 C C   . PHE C 1 389 ? 55.050  26.351  -22.924 1.00 95.49  ? 389 PHE C C   1 
ATOM   11617 O O   . PHE C 1 389 ? 54.598  27.372  -23.426 1.00 94.92  ? 389 PHE C O   1 
ATOM   11618 C CB  . PHE C 1 389 ? 57.481  26.347  -23.677 1.00 92.76  ? 389 PHE C CB  1 
ATOM   11619 C CG  . PHE C 1 389 ? 58.593  25.619  -24.418 1.00 90.98  ? 389 PHE C CG  1 
ATOM   11620 C CD1 . PHE C 1 389 ? 58.678  25.668  -25.805 1.00 88.61  ? 389 PHE C CD1 1 
ATOM   11621 C CD2 . PHE C 1 389 ? 59.554  24.883  -23.724 1.00 91.92  ? 389 PHE C CD2 1 
ATOM   11622 C CE1 . PHE C 1 389 ? 59.695  24.999  -26.475 1.00 86.95  ? 389 PHE C CE1 1 
ATOM   11623 C CE2 . PHE C 1 389 ? 60.560  24.213  -24.399 1.00 89.81  ? 389 PHE C CE2 1 
ATOM   11624 C CZ  . PHE C 1 389 ? 60.627  24.273  -25.772 1.00 87.59  ? 389 PHE C CZ  1 
ATOM   11625 N N   . TYR C 1 390 ? 54.644  25.844  -21.755 1.00 98.08  ? 390 TYR C N   1 
ATOM   11626 C CA  . TYR C 1 390 ? 53.564  26.410  -20.967 1.00 101.55 ? 390 TYR C CA  1 
ATOM   11627 C C   . TYR C 1 390 ? 54.120  26.968  -19.656 1.00 103.35 ? 390 TYR C C   1 
ATOM   11628 O O   . TYR C 1 390 ? 55.119  26.453  -19.164 1.00 103.56 ? 390 TYR C O   1 
ATOM   11629 C CB  . TYR C 1 390 ? 52.546  25.282  -20.755 1.00 103.74 ? 390 TYR C CB  1 
ATOM   11630 C CG  . TYR C 1 390 ? 51.752  24.844  -21.981 1.00 102.79 ? 390 TYR C CG  1 
ATOM   11631 C CD1 . TYR C 1 390 ? 52.213  23.830  -22.821 1.00 101.02 ? 390 TYR C CD1 1 
ATOM   11632 C CD2 . TYR C 1 390 ? 50.532  25.440  -22.290 1.00 103.78 ? 390 TYR C CD2 1 
ATOM   11633 C CE1 . TYR C 1 390 ? 51.487  23.431  -23.935 1.00 100.12 ? 390 TYR C CE1 1 
ATOM   11634 C CE2 . TYR C 1 390 ? 49.793  25.038  -23.391 1.00 102.77 ? 390 TYR C CE2 1 
ATOM   11635 C CZ  . TYR C 1 390 ? 50.272  24.035  -24.219 1.00 101.01 ? 390 TYR C CZ  1 
ATOM   11636 O OH  . TYR C 1 390 ? 49.532  23.664  -25.308 1.00 100.11 ? 390 TYR C OH  1 
ATOM   11637 N N   . ASP C 1 391 ? 53.452  27.991  -19.082 1.00 104.58 ? 391 ASP C N   1 
ATOM   11638 C CA  . ASP C 1 391 ? 53.875  28.599  -17.822 1.00 106.54 ? 391 ASP C CA  1 
ATOM   11639 C C   . ASP C 1 391 ? 52.981  28.086  -16.695 1.00 109.02 ? 391 ASP C C   1 
ATOM   11640 O O   . ASP C 1 391 ? 52.241  27.125  -16.903 1.00 108.81 ? 391 ASP C O   1 
ATOM   11641 C CB  . ASP C 1 391 ? 54.016  30.111  -17.943 1.00 106.92 ? 391 ASP C CB  1 
ATOM   11642 C CG  . ASP C 1 391 ? 52.741  30.928  -18.083 1.00 108.11 ? 391 ASP C CG  1 
ATOM   11643 O OD1 . ASP C 1 391 ? 51.698  30.493  -17.563 1.00 110.30 ? 391 ASP C OD1 1 
ATOM   11644 O OD2 . ASP C 1 391 ? 52.799  31.997  -18.723 1.00 107.32 ? 391 ASP C OD2 1 
ATOM   11645 N N   . SER C 1 392 ? 53.053  28.721  -15.511 1.00 111.58 ? 392 SER C N   1 
ATOM   11646 C CA  . SER C 1 392 ? 52.364  28.224  -14.325 1.00 114.68 ? 392 SER C CA  1 
ATOM   11647 C C   . SER C 1 392 ? 50.854  28.489  -14.371 1.00 116.06 ? 392 SER C C   1 
ATOM   11648 O O   . SER C 1 392 ? 50.126  27.947  -13.544 1.00 118.22 ? 392 SER C O   1 
ATOM   11649 C CB  . SER C 1 392 ? 52.976  28.761  -13.044 1.00 117.45 ? 392 SER C CB  1 
ATOM   11650 O OG  . SER C 1 392 ? 53.028  30.180  -13.036 1.00 118.01 ? 392 SER C OG  1 
ATOM   11651 N N   . ASP C 1 393 ? 50.392  29.309  -15.330 1.00 114.75 ? 393 ASP C N   1 
ATOM   11652 C CA  . ASP C 1 393 ? 48.970  29.552  -15.535 1.00 116.18 ? 393 ASP C CA  1 
ATOM   11653 C C   . ASP C 1 393 ? 48.409  28.563  -16.563 1.00 113.98 ? 393 ASP C C   1 
ATOM   11654 O O   . ASP C 1 393 ? 47.192  28.419  -16.687 1.00 114.91 ? 393 ASP C O   1 
ATOM   11655 C CB  . ASP C 1 393 ? 48.712  31.010  -15.901 1.00 116.41 ? 393 ASP C CB  1 
ATOM   11656 C CG  . ASP C 1 393 ? 49.075  32.063  -14.855 1.00 119.23 ? 393 ASP C CG  1 
ATOM   11657 O OD1 . ASP C 1 393 ? 49.663  31.694  -13.819 1.00 120.99 ? 393 ASP C OD1 1 
ATOM   11658 O OD2 . ASP C 1 393 ? 48.759  33.254  -15.077 1.00 119.61 ? 393 ASP C OD2 1 
ATOM   11659 N N   . ASN C 1 394 ? 49.310  27.872  -17.271 1.00 111.34 ? 394 ASN C N   1 
ATOM   11660 C CA  . ASN C 1 394 ? 48.972  26.940  -18.334 1.00 109.52 ? 394 ASN C CA  1 
ATOM   11661 C C   . ASN C 1 394 ? 48.706  27.712  -19.627 1.00 107.69 ? 394 ASN C C   1 
ATOM   11662 O O   . ASN C 1 394 ? 47.752  27.403  -20.331 1.00 107.32 ? 394 ASN C O   1 
ATOM   11663 C CB  . ASN C 1 394 ? 47.818  26.011  -17.959 1.00 111.30 ? 394 ASN C CB  1 
ATOM   11664 C CG  . ASN C 1 394 ? 47.700  24.844  -18.914 1.00 109.27 ? 394 ASN C CG  1 
ATOM   11665 O OD1 . ASN C 1 394 ? 48.493  23.899  -18.862 1.00 108.62 ? 394 ASN C OD1 1 
ATOM   11666 N ND2 . ASN C 1 394 ? 46.723  24.887  -19.805 1.00 108.70 ? 394 ASN C ND2 1 
ATOM   11667 N N   . LYS C 1 395 ? 49.574  28.690  -19.945 1.00 107.27 ? 395 LYS C N   1 
ATOM   11668 C CA  . LYS C 1 395 ? 49.508  29.464  -21.185 1.00 105.14 ? 395 LYS C CA  1 
ATOM   11669 C C   . LYS C 1 395 ? 50.837  29.350  -21.939 1.00 101.79 ? 395 LYS C C   1 
ATOM   11670 O O   . LYS C 1 395 ? 51.909  29.421  -21.337 1.00 101.61 ? 395 LYS C O   1 
ATOM   11671 C CB  . LYS C 1 395 ? 49.100  30.933  -20.967 1.00 107.29 ? 395 LYS C CB  1 
ATOM   11672 C CG  . LYS C 1 395 ? 49.807  31.760  -19.876 1.00 110.05 ? 395 LYS C CG  1 
ATOM   11673 C CD  . LYS C 1 395 ? 49.080  33.059  -19.502 1.00 112.86 ? 395 LYS C CD  1 
ATOM   11674 C CE  . LYS C 1 395 ? 49.599  33.789  -18.283 1.00 115.65 ? 395 LYS C CE  1 
ATOM   11675 N NZ  . LYS C 1 395 ? 50.973  34.276  -18.434 1.00 114.34 ? 395 LYS C NZ  1 
ATOM   11676 N N   . ILE C 1 396 ? 50.749  29.183  -23.266 1.00 98.73  ? 396 ILE C N   1 
ATOM   11677 C CA  . ILE C 1 396 ? 51.921  28.974  -24.101 1.00 95.90  ? 396 ILE C CA  1 
ATOM   11678 C C   . ILE C 1 396 ? 52.770  30.251  -24.132 1.00 95.80  ? 396 ILE C C   1 
ATOM   11679 O O   . ILE C 1 396 ? 52.254  31.323  -24.422 1.00 96.73  ? 396 ILE C O   1 
ATOM   11680 C CB  . ILE C 1 396 ? 51.504  28.511  -25.513 1.00 93.42  ? 396 ILE C CB  1 
ATOM   11681 C CG1 . ILE C 1 396 ? 50.833  27.138  -25.481 1.00 93.24  ? 396 ILE C CG1 1 
ATOM   11682 C CG2 . ILE C 1 396 ? 52.701  28.521  -26.471 1.00 90.99  ? 396 ILE C CG2 1 
ATOM   11683 C CD1 . ILE C 1 396 ? 50.619  26.511  -26.851 1.00 90.99  ? 396 ILE C CD1 1 
ATOM   11684 N N   . ILE C 1 397 ? 54.083  30.125  -23.867 1.00 95.13  ? 397 ILE C N   1 
ATOM   11685 C CA  . ILE C 1 397 ? 55.013  31.251  -23.878 1.00 94.79  ? 397 ILE C CA  1 
ATOM   11686 C C   . ILE C 1 397 ? 56.040  31.109  -24.999 1.00 91.77  ? 397 ILE C C   1 
ATOM   11687 O O   . ILE C 1 397 ? 56.860  31.999  -25.180 1.00 91.21  ? 397 ILE C O   1 
ATOM   11688 C CB  . ILE C 1 397 ? 55.719  31.407  -22.518 1.00 96.90  ? 397 ILE C CB  1 
ATOM   11689 C CG1 . ILE C 1 397 ? 56.532  30.162  -22.153 1.00 96.22  ? 397 ILE C CG1 1 
ATOM   11690 C CG2 . ILE C 1 397 ? 54.712  31.769  -21.429 1.00 99.96  ? 397 ILE C CG2 1 
ATOM   11691 C CD1 . ILE C 1 397 ? 57.279  30.271  -20.836 1.00 98.55  ? 397 ILE C CD1 1 
ATOM   11692 N N   . LYS C 1 398 ? 56.016  29.997  -25.738 1.00 90.11  ? 398 LYS C N   1 
ATOM   11693 C CA  . LYS C 1 398 ? 56.905  29.842  -26.878 1.00 88.33  ? 398 LYS C CA  1 
ATOM   11694 C C   . LYS C 1 398 ? 56.453  28.680  -27.755 1.00 86.46  ? 398 LYS C C   1 
ATOM   11695 O O   . LYS C 1 398 ? 56.106  27.626  -27.239 1.00 86.37  ? 398 LYS C O   1 
ATOM   11696 C CB  . LYS C 1 398 ? 58.349  29.517  -26.465 1.00 89.07  ? 398 LYS C CB  1 
ATOM   11697 C CG  . LYS C 1 398 ? 59.335  29.327  -27.626 1.00 86.98  ? 398 LYS C CG  1 
ATOM   11698 C CD  . LYS C 1 398 ? 60.780  29.153  -27.199 1.00 87.63  ? 398 LYS C CD  1 
ATOM   11699 C CE  . LYS C 1 398 ? 61.696  29.019  -28.375 1.00 86.19  ? 398 LYS C CE  1 
ATOM   11700 N NZ  . LYS C 1 398 ? 63.004  28.472  -27.986 1.00 86.02  ? 398 LYS C NZ  1 
ATOM   11701 N N   . ASN C 1 399 ? 56.522  28.890  -29.077 1.00 84.79  ? 399 ASN C N   1 
ATOM   11702 C CA  . ASN C 1 399 ? 56.244  27.869  -30.075 1.00 83.64  ? 399 ASN C CA  1 
ATOM   11703 C C   . ASN C 1 399 ? 57.445  27.740  -31.011 1.00 82.05  ? 399 ASN C C   1 
ATOM   11704 O O   . ASN C 1 399 ? 57.729  28.672  -31.751 1.00 82.73  ? 399 ASN C O   1 
ATOM   11705 C CB  . ASN C 1 399 ? 55.045  28.229  -30.954 1.00 83.35  ? 399 ASN C CB  1 
ATOM   11706 C CG  . ASN C 1 399 ? 53.720  28.144  -30.238 1.00 84.98  ? 399 ASN C CG  1 
ATOM   11707 O OD1 . ASN C 1 399 ? 53.172  27.051  -30.095 1.00 86.17  ? 399 ASN C OD1 1 
ATOM   11708 N ND2 . ASN C 1 399 ? 53.171  29.272  -29.815 1.00 86.47  ? 399 ASN C ND2 1 
ATOM   11709 N N   . GLU C 1 400 ? 58.102  26.576  -31.021 1.00 80.95  ? 400 GLU C N   1 
ATOM   11710 C CA  . GLU C 1 400 ? 59.175  26.288  -31.959 1.00 78.79  ? 400 GLU C CA  1 
ATOM   11711 C C   . GLU C 1 400 ? 58.937  24.913  -32.601 1.00 77.89  ? 400 GLU C C   1 
ATOM   11712 O O   . GLU C 1 400 ? 58.497  23.951  -31.958 1.00 77.79  ? 400 GLU C O   1 
ATOM   11713 C CB  . GLU C 1 400 ? 60.502  26.392  -31.205 1.00 79.16  ? 400 GLU C CB  1 
ATOM   11714 C CG  . GLU C 1 400 ? 61.720  26.348  -32.124 1.00 77.61  ? 400 GLU C CG  1 
ATOM   11715 C CD  . GLU C 1 400 ? 63.106  26.549  -31.518 1.00 77.64  ? 400 GLU C CD  1 
ATOM   11716 O OE1 . GLU C 1 400 ? 63.326  26.598  -30.287 1.00 78.79  ? 400 GLU C OE1 1 
ATOM   11717 O OE2 . GLU C 1 400 ? 64.015  26.609  -32.363 1.00 76.44  ? 400 GLU C OE2 1 
ATOM   11718 N N   . SER C 1 401 ? 59.204  24.838  -33.907 1.00 76.29  ? 401 SER C N   1 
ATOM   11719 C CA  . SER C 1 401 ? 59.155  23.579  -34.632 1.00 75.24  ? 401 SER C CA  1 
ATOM   11720 C C   . SER C 1 401 ? 60.562  22.984  -34.710 1.00 74.97  ? 401 SER C C   1 
ATOM   11721 O O   . SER C 1 401 ? 61.534  23.717  -34.578 1.00 74.60  ? 401 SER C O   1 
ATOM   11722 C CB  . SER C 1 401 ? 58.595  23.802  -36.009 1.00 73.71  ? 401 SER C CB  1 
ATOM   11723 O OG  . SER C 1 401 ? 57.239  24.188  -35.944 1.00 73.98  ? 401 SER C OG  1 
ATOM   11724 N N   . ILE C 1 402 ? 60.669  21.664  -34.914 1.00 75.47  ? 402 ILE C N   1 
ATOM   11725 C CA  . ILE C 1 402 ? 61.913  21.034  -35.358 1.00 74.91  ? 402 ILE C CA  1 
ATOM   11726 C C   . ILE C 1 402 ? 61.567  20.164  -36.567 1.00 74.64  ? 402 ILE C C   1 
ATOM   11727 O O   . ILE C 1 402 ? 60.643  19.347  -36.503 1.00 75.47  ? 402 ILE C O   1 
ATOM   11728 C CB  . ILE C 1 402 ? 62.602  20.213  -34.246 1.00 75.52  ? 402 ILE C CB  1 
ATOM   11729 C CG1 . ILE C 1 402 ? 63.391  21.079  -33.277 1.00 76.30  ? 402 ILE C CG1 1 
ATOM   11730 C CG2 . ILE C 1 402 ? 63.508  19.145  -34.845 1.00 75.06  ? 402 ILE C CG2 1 
ATOM   11731 C CD1 . ILE C 1 402 ? 62.545  21.777  -32.237 1.00 78.04  ? 402 ILE C CD1 1 
ATOM   11732 N N   . ASN C 1 403 ? 62.300  20.368  -37.667 1.00 73.05  ? 403 ASN C N   1 
ATOM   11733 C CA  . ASN C 1 403 ? 62.010  19.695  -38.919 1.00 72.99  ? 403 ASN C CA  1 
ATOM   11734 C C   . ASN C 1 403 ? 62.877  18.452  -39.045 1.00 73.36  ? 403 ASN C C   1 
ATOM   11735 O O   . ASN C 1 403 ? 64.104  18.568  -39.021 1.00 74.46  ? 403 ASN C O   1 
ATOM   11736 C CB  . ASN C 1 403 ? 62.299  20.585  -40.118 1.00 72.20  ? 403 ASN C CB  1 
ATOM   11737 C CG  . ASN C 1 403 ? 61.164  21.531  -40.399 1.00 73.21  ? 403 ASN C CG  1 
ATOM   11738 O OD1 . ASN C 1 403 ? 60.987  21.954  -41.547 1.00 72.92  ? 403 ASN C OD1 1 
ATOM   11739 N ND2 . ASN C 1 403 ? 60.378  21.853  -39.381 1.00 74.74  ? 403 ASN C ND2 1 
ATOM   11740 N N   . ILE C 1 404 ? 62.253  17.279  -39.222 1.00 72.68  ? 404 ILE C N   1 
ATOM   11741 C CA  . ILE C 1 404 ? 63.046  16.089  -39.437 1.00 72.12  ? 404 ILE C CA  1 
ATOM   11742 C C   . ILE C 1 404 ? 62.619  15.404  -40.728 1.00 71.98  ? 404 ILE C C   1 
ATOM   11743 O O   . ILE C 1 404 ? 61.554  15.692  -41.265 1.00 71.54  ? 404 ILE C O   1 
ATOM   11744 C CB  . ILE C 1 404 ? 62.982  15.157  -38.219 1.00 73.20  ? 404 ILE C CB  1 
ATOM   11745 C CG1 . ILE C 1 404 ? 61.598  14.543  -38.029 1.00 74.18  ? 404 ILE C CG1 1 
ATOM   11746 C CG2 . ILE C 1 404 ? 63.473  15.887  -36.969 1.00 73.43  ? 404 ILE C CG2 1 
ATOM   11747 C CD1 . ILE C 1 404 ? 61.551  13.447  -36.980 1.00 75.55  ? 404 ILE C CD1 1 
ATOM   11748 N N   . LEU C 1 405 ? 63.514  14.526  -41.210 1.00 72.18  ? 405 LEU C N   1 
ATOM   11749 C CA  . LEU C 1 405 ? 63.246  13.585  -42.283 1.00 72.32  ? 405 LEU C CA  1 
ATOM   11750 C C   . LEU C 1 405 ? 63.470  12.180  -41.730 1.00 74.31  ? 405 LEU C C   1 
ATOM   11751 O O   . LEU C 1 405 ? 64.597  11.810  -41.398 1.00 75.53  ? 405 LEU C O   1 
ATOM   11752 C CB  . LEU C 1 405 ? 64.155  13.865  -43.477 1.00 71.33  ? 405 LEU C CB  1 
ATOM   11753 C CG  . LEU C 1 405 ? 63.824  13.096  -44.759 1.00 71.57  ? 405 LEU C CG  1 
ATOM   11754 C CD1 . LEU C 1 405 ? 62.524  13.569  -45.361 1.00 71.76  ? 405 LEU C CD1 1 
ATOM   11755 C CD2 . LEU C 1 405 ? 64.941  13.219  -45.771 1.00 71.28  ? 405 LEU C CD2 1 
ATOM   11756 N N   . ALA C 1 406 ? 62.387  11.389  -41.657 1.00 75.56  ? 406 ALA C N   1 
ATOM   11757 C CA  . ALA C 1 406 ? 62.312  10.233  -40.780 1.00 76.11  ? 406 ALA C CA  1 
ATOM   11758 C C   . ALA C 1 406 ? 61.927  8.996   -41.564 1.00 76.72  ? 406 ALA C C   1 
ATOM   11759 O O   . ALA C 1 406 ? 61.101  9.082   -42.482 1.00 75.96  ? 406 ALA C O   1 
ATOM   11760 C CB  . ALA C 1 406 ? 61.290  10.484  -39.700 1.00 77.11  ? 406 ALA C CB  1 
ATOM   11761 N N   . SER C 1 407 ? 62.514  7.866   -41.123 1.00 77.72  ? 407 SER C N   1 
ATOM   11762 C CA  . SER C 1 407 ? 62.109  6.536   -41.555 1.00 78.71  ? 407 SER C CA  1 
ATOM   11763 C C   . SER C 1 407 ? 62.457  5.510   -40.483 1.00 80.93  ? 407 SER C C   1 
ATOM   11764 O O   . SER C 1 407 ? 63.165  5.813   -39.527 1.00 81.19  ? 407 SER C O   1 
ATOM   11765 C CB  . SER C 1 407 ? 62.727  6.177   -42.869 1.00 77.93  ? 407 SER C CB  1 
ATOM   11766 O OG  . SER C 1 407 ? 62.034  5.092   -43.464 1.00 78.90  ? 407 SER C OG  1 
ATOM   11767 N N   . LYS C 1 408 ? 61.940  4.293   -40.651 1.00 83.13  ? 408 LYS C N   1 
ATOM   11768 C CA  . LYS C 1 408 ? 62.169  3.234   -39.688 1.00 85.31  ? 408 LYS C CA  1 
ATOM   11769 C C   . LYS C 1 408 ? 63.445  2.478   -40.027 1.00 85.32  ? 408 LYS C C   1 
ATOM   11770 O O   . LYS C 1 408 ? 64.017  1.847   -39.142 1.00 86.49  ? 408 LYS C O   1 
ATOM   11771 C CB  . LYS C 1 408 ? 60.997  2.256   -39.710 1.00 88.30  ? 408 LYS C CB  1 
ATOM   11772 C CG  . LYS C 1 408 ? 59.678  2.944   -39.483 1.00 88.98  ? 408 LYS C CG  1 
ATOM   11773 C CD  . LYS C 1 408 ? 58.558  1.944   -39.241 1.00 92.24  ? 408 LYS C CD  1 
ATOM   11774 C CE  . LYS C 1 408 ? 57.236  2.621   -39.125 1.00 92.41  ? 408 LYS C CE  1 
ATOM   11775 N NZ  . LYS C 1 408 ? 56.277  1.636   -38.628 1.00 95.33  ? 408 LYS C NZ  1 
ATOM   11776 N N   . THR C 1 409 ? 63.814  2.487   -41.322 1.00 84.13  ? 409 THR C N   1 
ATOM   11777 C CA  . THR C 1 409 ? 65.042  1.878   -41.824 1.00 83.96  ? 409 THR C CA  1 
ATOM   11778 C C   . THR C 1 409 ? 65.790  2.945   -42.624 1.00 81.22  ? 409 THR C C   1 
ATOM   11779 O O   . THR C 1 409 ? 65.280  4.033   -42.834 1.00 79.62  ? 409 THR C O   1 
ATOM   11780 C CB  . THR C 1 409 ? 64.761  0.620   -42.662 1.00 85.73  ? 409 THR C CB  1 
ATOM   11781 O OG1 . THR C 1 409 ? 65.944  0.139   -43.292 1.00 85.89  ? 409 THR C OG1 1 
ATOM   11782 C CG2 . THR C 1 409 ? 63.863  0.868   -43.859 1.00 85.61  ? 409 THR C CG2 1 
ATOM   11783 N N   . ALA C 1 410 ? 66.989  2.601   -43.091 1.00 80.94  ? 410 ALA C N   1 
ATOM   11784 C CA  . ALA C 1 410 ? 67.860  3.535   -43.773 1.00 78.89  ? 410 ALA C CA  1 
ATOM   11785 C C   . ALA C 1 410 ? 67.340  3.862   -45.176 1.00 78.01  ? 410 ALA C C   1 
ATOM   11786 O O   . ALA C 1 410 ? 66.789  3.007   -45.849 1.00 78.78  ? 410 ALA C O   1 
ATOM   11787 C CB  . ALA C 1 410 ? 69.245  2.935   -43.790 1.00 79.54  ? 410 ALA C CB  1 
ATOM   11788 N N   . PHE C 1 411 ? 67.538  5.108   -45.631 1.00 76.37  ? 411 PHE C N   1 
ATOM   11789 C CA  . PHE C 1 411 ? 67.237  5.455   -47.013 1.00 76.11  ? 411 PHE C CA  1 
ATOM   11790 C C   . PHE C 1 411 ? 68.403  6.191   -47.666 1.00 74.82  ? 411 PHE C C   1 
ATOM   11791 O O   . PHE C 1 411 ? 69.276  6.724   -46.992 1.00 73.66  ? 411 PHE C O   1 
ATOM   11792 C CB  . PHE C 1 411 ? 65.985  6.313   -47.124 1.00 75.42  ? 411 PHE C CB  1 
ATOM   11793 C CG  . PHE C 1 411 ? 65.964  7.481   -46.157 1.00 74.30  ? 411 PHE C CG  1 
ATOM   11794 C CD1 . PHE C 1 411 ? 65.619  7.301   -44.822 1.00 74.75  ? 411 PHE C CD1 1 
ATOM   11795 C CD2 . PHE C 1 411 ? 66.252  8.768   -46.594 1.00 73.16  ? 411 PHE C CD2 1 
ATOM   11796 C CE1 . PHE C 1 411 ? 65.572  8.383   -43.948 1.00 73.62  ? 411 PHE C CE1 1 
ATOM   11797 C CE2 . PHE C 1 411 ? 66.167  9.856   -45.726 1.00 71.89  ? 411 PHE C CE2 1 
ATOM   11798 C CZ  . PHE C 1 411 ? 65.853  9.656   -44.400 1.00 72.07  ? 411 PHE C CZ  1 
ATOM   11799 N N   . GLU C 1 412 ? 68.390  6.138   -49.001 1.00 75.23  ? 412 GLU C N   1 
ATOM   11800 C CA  . GLU C 1 412 ? 69.303  6.844   -49.874 1.00 74.57  ? 412 GLU C CA  1 
ATOM   11801 C C   . GLU C 1 412 ? 69.071  8.347   -49.757 1.00 73.06  ? 412 GLU C C   1 
ATOM   11802 O O   . GLU C 1 412 ? 67.955  8.810   -49.502 1.00 72.69  ? 412 GLU C O   1 
ATOM   11803 C CB  . GLU C 1 412 ? 69.059  6.380   -51.309 1.00 76.01  ? 412 GLU C CB  1 
ATOM   11804 C CG  . GLU C 1 412 ? 69.764  7.220   -52.371 1.00 75.58  ? 412 GLU C CG  1 
ATOM   11805 C CD  . GLU C 1 412 ? 69.733  6.639   -53.783 1.00 77.65  ? 412 GLU C CD  1 
ATOM   11806 O OE1 . GLU C 1 412 ? 70.129  5.447   -54.082 1.00 79.74  ? 412 GLU C OE1 1 
ATOM   11807 O OE2 . GLU C 1 412 ? 69.312  7.484   -54.611 1.00 76.82  ? 412 GLU C OE2 1 
ATOM   11808 N N   . LEU C 1 413 ? 70.175  9.079   -49.930 1.00 72.07  ? 413 LEU C N   1 
ATOM   11809 C CA  . LEU C 1 413 ? 70.204  10.521  -49.987 1.00 70.46  ? 413 LEU C CA  1 
ATOM   11810 C C   . LEU C 1 413 ? 70.990  10.912  -51.229 1.00 70.77  ? 413 LEU C C   1 
ATOM   11811 O O   . LEU C 1 413 ? 71.819  10.155  -51.719 1.00 71.24  ? 413 LEU C O   1 
ATOM   11812 C CB  . LEU C 1 413 ? 70.881  11.024  -48.721 1.00 69.45  ? 413 LEU C CB  1 
ATOM   11813 C CG  . LEU C 1 413 ? 70.132  10.767  -47.412 1.00 69.42  ? 413 LEU C CG  1 
ATOM   11814 C CD1 . LEU C 1 413 ? 71.021  10.996  -46.221 1.00 69.25  ? 413 LEU C CD1 1 
ATOM   11815 C CD2 . LEU C 1 413 ? 68.964  11.702  -47.299 1.00 68.72  ? 413 LEU C CD2 1 
ATOM   11816 N N   . PRO C 1 414 ? 70.745  12.097  -51.806 1.00 70.77  ? 414 PRO C N   1 
ATOM   11817 C CA  . PRO C 1 414 ? 71.611  12.595  -52.863 1.00 71.87  ? 414 PRO C CA  1 
ATOM   11818 C C   . PRO C 1 414 ? 72.922  13.014  -52.199 1.00 72.58  ? 414 PRO C C   1 
ATOM   11819 O O   . PRO C 1 414 ? 72.962  13.327  -51.004 1.00 71.81  ? 414 PRO C O   1 
ATOM   11820 C CB  . PRO C 1 414 ? 70.828  13.730  -53.502 1.00 71.03  ? 414 PRO C CB  1 
ATOM   11821 C CG  . PRO C 1 414 ? 69.866  14.176  -52.423 1.00 69.99  ? 414 PRO C CG  1 
ATOM   11822 C CD  . PRO C 1 414 ? 69.636  12.996  -51.494 1.00 70.15  ? 414 PRO C CD  1 
ATOM   11823 N N   . GLU C 1 415 ? 74.009  12.917  -52.965 1.00 74.30  ? 415 GLU C N   1 
ATOM   11824 C CA  . GLU C 1 415 ? 75.330  13.042  -52.392 1.00 75.37  ? 415 GLU C CA  1 
ATOM   11825 C C   . GLU C 1 415 ? 76.168  13.914  -53.318 1.00 74.44  ? 415 GLU C C   1 
ATOM   11826 O O   . GLU C 1 415 ? 76.170  13.702  -54.537 1.00 74.77  ? 415 GLU C O   1 
ATOM   11827 C CB  . GLU C 1 415 ? 75.898  11.645  -52.153 1.00 79.15  ? 415 GLU C CB  1 
ATOM   11828 C CG  . GLU C 1 415 ? 75.265  10.907  -50.969 1.00 81.84  ? 415 GLU C CG  1 
ATOM   11829 C CD  . GLU C 1 415 ? 75.713  11.329  -49.571 1.00 83.79  ? 415 GLU C CD  1 
ATOM   11830 O OE1 . GLU C 1 415 ? 76.955  11.464  -49.393 1.00 89.78  ? 415 GLU C OE1 1 
ATOM   11831 O OE2 . GLU C 1 415 ? 74.872  11.474  -48.651 1.00 83.63  ? 415 GLU C OE2 1 
ATOM   11832 N N   . LEU C 1 416 ? 76.822  14.915  -52.713 1.00 72.30  ? 416 LEU C N   1 
ATOM   11833 C CA  . LEU C 1 416 ? 77.683  15.831  -53.433 1.00 71.97  ? 416 LEU C CA  1 
ATOM   11834 C C   . LEU C 1 416 ? 79.091  15.661  -52.875 1.00 71.11  ? 416 LEU C C   1 
ATOM   11835 O O   . LEU C 1 416 ? 79.293  15.567  -51.663 1.00 70.27  ? 416 LEU C O   1 
ATOM   11836 C CB  . LEU C 1 416 ? 77.160  17.270  -53.323 1.00 71.65  ? 416 LEU C CB  1 
ATOM   11837 C CG  . LEU C 1 416 ? 77.880  18.334  -54.169 1.00 72.24  ? 416 LEU C CG  1 
ATOM   11838 C CD1 . LEU C 1 416 ? 77.101  19.630  -54.234 1.00 71.98  ? 416 LEU C CD1 1 
ATOM   11839 C CD2 . LEU C 1 416 ? 79.260  18.661  -53.662 1.00 72.18  ? 416 LEU C CD2 1 
ATOM   11840 N N   . THR C 1 417 ? 80.046  15.560  -53.800 1.00 71.53  ? 417 THR C N   1 
ATOM   11841 C CA  . THR C 1 417 ? 81.454  15.372  -53.487 1.00 71.69  ? 417 THR C CA  1 
ATOM   11842 C C   . THR C 1 417 ? 82.244  16.192  -54.499 1.00 72.89  ? 417 THR C C   1 
ATOM   11843 O O   . THR C 1 417 ? 81.744  16.478  -55.591 1.00 73.13  ? 417 THR C O   1 
ATOM   11844 C CB  . THR C 1 417 ? 81.811  13.887  -53.538 1.00 72.07  ? 417 THR C CB  1 
ATOM   11845 O OG1 . THR C 1 417 ? 81.697  13.457  -54.889 1.00 72.67  ? 417 THR C OG1 1 
ATOM   11846 C CG2 . THR C 1 417 ? 80.871  13.056  -52.689 1.00 71.50  ? 417 THR C CG2 1 
ATOM   11847 N N   . ILE C 1 418 ? 83.463  16.590  -54.119 1.00 73.85  ? 418 ILE C N   1 
ATOM   11848 C CA  . ILE C 1 418 ? 84.263  17.469  -54.952 1.00 74.77  ? 418 ILE C CA  1 
ATOM   11849 C C   . ILE C 1 418 ? 85.701  17.008  -54.944 1.00 76.03  ? 418 ILE C C   1 
ATOM   11850 O O   . ILE C 1 418 ? 86.178  16.626  -53.885 1.00 76.54  ? 418 ILE C O   1 
ATOM   11851 C CB  . ILE C 1 418 ? 84.204  18.912  -54.441 1.00 74.40  ? 418 ILE C CB  1 
ATOM   11852 C CG1 . ILE C 1 418 ? 84.828  19.060  -53.035 1.00 74.10  ? 418 ILE C CG1 1 
ATOM   11853 C CG2 . ILE C 1 418 ? 82.768  19.407  -54.503 1.00 73.71  ? 418 ILE C CG2 1 
ATOM   11854 C CD1 . ILE C 1 418 ? 85.066  20.498  -52.601 1.00 73.73  ? 418 ILE C CD1 1 
ATOM   11855 N N   . GLU C 1 419 ? 86.371  17.155  -56.097 1.00 77.45  ? 419 GLU C N   1 
ATOM   11856 C CA  . GLU C 1 419 ? 87.784  16.848  -56.258 1.00 78.68  ? 419 GLU C CA  1 
ATOM   11857 C C   . GLU C 1 419 ? 88.495  18.129  -56.672 1.00 79.50  ? 419 GLU C C   1 
ATOM   11858 O O   . GLU C 1 419 ? 88.083  18.754  -57.645 1.00 80.19  ? 419 GLU C O   1 
ATOM   11859 C CB  . GLU C 1 419 ? 87.987  15.795  -57.349 1.00 80.23  ? 419 GLU C CB  1 
ATOM   11860 C CG  . GLU C 1 419 ? 87.576  14.371  -56.968 1.00 80.55  ? 419 GLU C CG  1 
ATOM   11861 C CD  . GLU C 1 419 ? 87.727  13.403  -58.134 1.00 82.84  ? 419 GLU C CD  1 
ATOM   11862 O OE1 . GLU C 1 419 ? 87.254  13.752  -59.250 1.00 82.79  ? 419 GLU C OE1 1 
ATOM   11863 O OE2 . GLU C 1 419 ? 88.355  12.325  -57.951 1.00 84.86  ? 419 GLU C OE2 1 
ATOM   11864 N N   . VAL C 1 420 ? 89.579  18.478  -55.960 1.00 79.91  ? 420 VAL C N   1 
ATOM   11865 C CA  . VAL C 1 420 ? 90.180  19.807  -56.003 1.00 79.95  ? 420 VAL C CA  1 
ATOM   11866 C C   . VAL C 1 420 ? 91.615  19.682  -56.496 1.00 82.35  ? 420 VAL C C   1 
ATOM   11867 O O   . VAL C 1 420 ? 92.368  18.828  -56.013 1.00 83.75  ? 420 VAL C O   1 
ATOM   11868 C CB  . VAL C 1 420 ? 90.154  20.460  -54.604 1.00 78.77  ? 420 VAL C CB  1 
ATOM   11869 C CG1 . VAL C 1 420 ? 90.658  21.890  -54.626 1.00 79.17  ? 420 VAL C CG1 1 
ATOM   11870 C CG2 . VAL C 1 420 ? 88.773  20.429  -53.950 1.00 77.34  ? 420 VAL C CG2 1 
ATOM   11871 N N   . THR C 1 421 ? 92.021  20.549  -57.431 1.00 83.19  ? 421 THR C N   1 
ATOM   11872 C CA  . THR C 1 421 ? 93.425  20.589  -57.812 1.00 84.61  ? 421 THR C CA  1 
ATOM   11873 C C   . THR C 1 421 ? 94.036  21.904  -57.332 1.00 85.07  ? 421 THR C C   1 
ATOM   11874 O O   . THR C 1 421 ? 93.365  22.934  -57.269 1.00 83.83  ? 421 THR C O   1 
ATOM   11875 C CB  . THR C 1 421 ? 93.580  20.388  -59.316 1.00 85.95  ? 421 THR C CB  1 
ATOM   11876 O OG1 . THR C 1 421 ? 93.084  19.073  -59.502 1.00 85.58  ? 421 THR C OG1 1 
ATOM   11877 C CG2 . THR C 1 421 ? 95.023  20.370  -59.789 1.00 88.01  ? 421 THR C CG2 1 
ATOM   11878 N N   . PRO C 1 422 ? 95.313  21.899  -56.878 1.00 86.59  ? 422 PRO C N   1 
ATOM   11879 C CA  . PRO C 1 422 ? 95.980  20.694  -56.365 1.00 86.86  ? 422 PRO C CA  1 
ATOM   11880 C C   . PRO C 1 422 ? 95.246  20.122  -55.153 1.00 85.20  ? 422 PRO C C   1 
ATOM   11881 O O   . PRO C 1 422 ? 94.552  20.834  -54.451 1.00 85.02  ? 422 PRO C O   1 
ATOM   11882 C CB  . PRO C 1 422 ? 97.384  21.202  -55.991 1.00 88.03  ? 422 PRO C CB  1 
ATOM   11883 C CG  . PRO C 1 422 ? 97.579  22.472  -56.793 1.00 88.72  ? 422 PRO C CG  1 
ATOM   11884 C CD  . PRO C 1 422 ? 96.193  23.077  -56.885 1.00 87.41  ? 422 PRO C CD  1 
ATOM   11885 N N   . GLU C 1 423 ? 95.409  18.834  -54.885 1.00 85.88  ? 423 GLU C N   1 
ATOM   11886 C CA  . GLU C 1 423 ? 94.634  18.151  -53.857 1.00 84.64  ? 423 GLU C CA  1 
ATOM   11887 C C   . GLU C 1 423 ? 95.266  18.353  -52.478 1.00 84.44  ? 423 GLU C C   1 
ATOM   11888 O O   . GLU C 1 423 ? 94.584  18.297  -51.466 1.00 83.02  ? 423 GLU C O   1 
ATOM   11889 C CB  . GLU C 1 423 ? 94.545  16.671  -54.250 1.00 85.59  ? 423 GLU C CB  1 
ATOM   11890 C CG  . GLU C 1 423 ? 93.773  15.774  -53.282 1.00 84.90  ? 423 GLU C CG  1 
ATOM   11891 C CD  . GLU C 1 423 ? 94.042  14.286  -53.448 1.00 86.22  ? 423 GLU C CD  1 
ATOM   11892 O OE1 . GLU C 1 423 ? 95.238  13.970  -53.503 1.00 87.60  ? 423 GLU C OE1 1 
ATOM   11893 O OE2 . GLU C 1 423 ? 93.115  13.444  -53.495 1.00 86.20  ? 423 GLU C OE2 1 
ATOM   11894 N N   . LYS C 1 424 ? 96.578  18.563  -52.417 1.00 86.54  ? 424 LYS C N   1 
ATOM   11895 C CA  . LYS C 1 424 ? 97.285  18.390  -51.159 1.00 87.50  ? 424 LYS C CA  1 
ATOM   11896 C C   . LYS C 1 424 ? 98.138  19.608  -50.835 1.00 87.84  ? 424 LYS C C   1 
ATOM   11897 O O   . LYS C 1 424 ? 98.111  20.069  -49.699 1.00 87.77  ? 424 LYS C O   1 
ATOM   11898 C CB  . LYS C 1 424 ? 98.236  17.186  -51.181 1.00 90.02  ? 424 LYS C CB  1 
ATOM   11899 C CG  . LYS C 1 424 ? 97.650  15.794  -51.445 1.00 90.88  ? 424 LYS C CG  1 
ATOM   11900 C CD  . LYS C 1 424 ? 98.620  14.700  -50.998 1.00 93.37  ? 424 LYS C CD  1 
ATOM   11901 C CE  . LYS C 1 424 ? 98.559  13.382  -51.712 1.00 94.60  ? 424 LYS C CE  1 
ATOM   11902 N NZ  . LYS C 1 424 ? 99.687  12.549  -51.277 1.00 96.39  ? 424 LYS C NZ  1 
ATOM   11903 N N   . ASP C 1 425 ? 98.922  20.077  -51.813 1.00 88.19  ? 425 ASP C N   1 
ATOM   11904 C CA  . ASP C 1 425 ? 99.810  21.202  -51.597 1.00 88.96  ? 425 ASP C CA  1 
ATOM   11905 C C   . ASP C 1 425 ? 99.607  22.260  -52.687 1.00 90.20  ? 425 ASP C C   1 
ATOM   11906 O O   . ASP C 1 425 ? 99.797  21.964  -53.868 1.00 92.73  ? 425 ASP C O   1 
ATOM   11907 C CB  . ASP C 1 425 ? 101.226 20.674  -51.547 1.00 90.13  ? 425 ASP C CB  1 
ATOM   11908 C CG  . ASP C 1 425 ? 102.363 21.682  -51.524 1.00 90.91  ? 425 ASP C CG  1 
ATOM   11909 O OD1 . ASP C 1 425 ? 102.068 22.886  -51.584 1.00 90.00  ? 425 ASP C OD1 1 
ATOM   11910 O OD2 . ASP C 1 425 ? 103.542 21.230  -51.442 1.00 92.18  ? 425 ASP C OD2 1 
ATOM   11911 N N   . LEU C 1 426 ? 99.321  23.508  -52.267 1.00 88.88  ? 426 LEU C N   1 
ATOM   11912 C CA  . LEU C 1 426 ? 99.042  24.621  -53.166 1.00 88.87  ? 426 LEU C CA  1 
ATOM   11913 C C   . LEU C 1 426 ? 100.263 25.090  -53.961 1.00 90.90  ? 426 LEU C C   1 
ATOM   11914 O O   . LEU C 1 426 ? 100.096 25.867  -54.901 1.00 91.02  ? 426 LEU C O   1 
ATOM   11915 C CB  . LEU C 1 426 ? 98.465  25.787  -52.357 1.00 88.33  ? 426 LEU C CB  1 
ATOM   11916 C CG  . LEU C 1 426 ? 97.075  25.587  -51.721 1.00 85.96  ? 426 LEU C CG  1 
ATOM   11917 C CD1 . LEU C 1 426 ? 96.545  26.878  -51.086 1.00 85.17  ? 426 LEU C CD1 1 
ATOM   11918 C CD2 . LEU C 1 426 ? 96.054  25.047  -52.703 1.00 84.84  ? 426 LEU C CD2 1 
ATOM   11919 N N   . ASN C 1 427 ? 101.478 24.643  -53.588 1.00 92.24  ? 427 ASN C N   1 
ATOM   11920 C CA  . ASN C 1 427 ? 102.684 24.951  -54.344 1.00 94.18  ? 427 ASN C CA  1 
ATOM   11921 C C   . ASN C 1 427 ? 102.713 24.216  -55.685 1.00 94.49  ? 427 ASN C C   1 
ATOM   11922 O O   . ASN C 1 427 ? 103.467 24.584  -56.569 1.00 96.48  ? 427 ASN C O   1 
ATOM   11923 C CB  . ASN C 1 427 ? 103.959 24.658  -53.554 1.00 96.03  ? 427 ASN C CB  1 
ATOM   11924 C CG  . ASN C 1 427 ? 104.407 25.816  -52.688 1.00 96.93  ? 427 ASN C CG  1 
ATOM   11925 O OD1 . ASN C 1 427 ? 104.561 25.674  -51.470 1.00 97.25  ? 427 ASN C OD1 1 
ATOM   11926 N ND2 . ASN C 1 427 ? 104.665 26.966  -53.291 1.00 98.06  ? 427 ASN C ND2 1 
ATOM   11927 N N   . GLU C 1 428 ? 101.882 23.198  -55.876 1.00 93.38  ? 428 GLU C N   1 
ATOM   11928 C CA  . GLU C 1 428 ? 102.009 22.358  -57.055 1.00 94.96  ? 428 GLU C CA  1 
ATOM   11929 C C   . GLU C 1 428 ? 101.512 23.044  -58.327 1.00 95.11  ? 428 GLU C C   1 
ATOM   11930 O O   . GLU C 1 428 ? 101.886 22.634  -59.417 1.00 97.24  ? 428 GLU C O   1 
ATOM   11931 C CB  . GLU C 1 428 ? 101.393 20.986  -56.774 1.00 94.52  ? 428 GLU C CB  1 
ATOM   11932 C CG  . GLU C 1 428 ? 102.324 20.155  -55.889 1.00 96.10  ? 428 GLU C CG  1 
ATOM   11933 C CD  . GLU C 1 428 ? 102.413 18.660  -56.123 1.00 97.27  ? 428 GLU C CD  1 
ATOM   11934 O OE1 . GLU C 1 428 ? 101.512 18.040  -56.729 1.00 98.06  ? 428 GLU C OE1 1 
ATOM   11935 O OE2 . GLU C 1 428 ? 103.437 18.114  -55.688 1.00 98.78  ? 428 GLU C OE2 1 
ATOM   11936 N N   . GLY C 1 429 ? 100.695 24.090  -58.214 1.00 93.61  ? 429 GLY C N   1 
ATOM   11937 C CA  . GLY C 1 429 ? 100.252 24.805  -59.397 1.00 93.96  ? 429 GLY C CA  1 
ATOM   11938 C C   . GLY C 1 429 ? 99.935  26.261  -59.075 1.00 93.35  ? 429 GLY C C   1 
ATOM   11939 O O   . GLY C 1 429 ? 99.860  26.652  -57.909 1.00 92.47  ? 429 GLY C O   1 
ATOM   11940 N N   . LYS C 1 430 ? 99.765  27.055  -60.134 1.00 93.83  ? 430 LYS C N   1 
ATOM   11941 C CA  . LYS C 1 430 ? 99.311  28.422  -59.999 1.00 92.90  ? 430 LYS C CA  1 
ATOM   11942 C C   . LYS C 1 430 ? 97.799  28.489  -60.192 1.00 90.62  ? 430 LYS C C   1 
ATOM   11943 O O   . LYS C 1 430 ? 97.187  29.469  -59.776 1.00 90.06  ? 430 LYS C O   1 
ATOM   11944 C CB  . LYS C 1 430 ? 100.070 29.278  -61.011 1.00 95.59  ? 430 LYS C CB  1 
ATOM   11945 C CG  . LYS C 1 430 ? 101.561 29.338  -60.747 1.00 97.79  ? 430 LYS C CG  1 
ATOM   11946 C CD  . LYS C 1 430 ? 102.285 30.576  -61.262 1.00 100.39 ? 430 LYS C CD  1 
ATOM   11947 C CE  . LYS C 1 430 ? 101.761 31.824  -60.622 1.00 99.92  ? 430 LYS C CE  1 
ATOM   11948 N NZ  . LYS C 1 430 ? 102.470 32.981  -61.162 1.00 102.84 ? 430 LYS C NZ  1 
ATOM   11949 N N   . ILE C 1 431 ? 97.215  27.454  -60.820 1.00 89.55  ? 431 ILE C N   1 
ATOM   11950 C CA  . ILE C 1 431 ? 95.793  27.414  -61.160 1.00 87.58  ? 431 ILE C CA  1 
ATOM   11951 C C   . ILE C 1 431 ? 95.133  26.234  -60.452 1.00 85.83  ? 431 ILE C C   1 
ATOM   11952 O O   . ILE C 1 431 ? 95.678  25.139  -60.456 1.00 86.15  ? 431 ILE C O   1 
ATOM   11953 C CB  . ILE C 1 431 ? 95.599  27.296  -62.682 1.00 88.53  ? 431 ILE C CB  1 
ATOM   11954 C CG1 . ILE C 1 431 ? 96.099  28.531  -63.416 1.00 90.20  ? 431 ILE C CG1 1 
ATOM   11955 C CG2 . ILE C 1 431 ? 94.146  26.999  -63.027 1.00 87.09  ? 431 ILE C CG2 1 
ATOM   11956 C CD1 . ILE C 1 431 ? 96.178  28.359  -64.923 1.00 92.19  ? 431 ILE C CD1 1 
ATOM   11957 N N   . ALA C 1 432 ? 93.939  26.455  -59.881 1.00 84.50  ? 432 ALA C N   1 
ATOM   11958 C CA  . ALA C 1 432 ? 93.189  25.411  -59.186 1.00 83.06  ? 432 ALA C CA  1 
ATOM   11959 C C   . ALA C 1 432 ? 91.982  24.983  -60.024 1.00 82.75  ? 432 ALA C C   1 
ATOM   11960 O O   . ALA C 1 432 ? 91.658  25.651  -61.007 1.00 83.26  ? 432 ALA C O   1 
ATOM   11961 C CB  . ALA C 1 432 ? 92.770  25.905  -57.814 1.00 81.40  ? 432 ALA C CB  1 
ATOM   11962 N N   . SER C 1 433 ? 91.358  23.852  -59.640 1.00 82.13  ? 433 SER C N   1 
ATOM   11963 C CA  . SER C 1 433 ? 90.031  23.458  -60.121 1.00 81.67  ? 433 SER C CA  1 
ATOM   11964 C C   . SER C 1 433 ? 89.237  22.801  -58.996 1.00 80.05  ? 433 SER C C   1 
ATOM   11965 O O   . SER C 1 433 ? 89.815  22.109  -58.163 1.00 80.01  ? 433 SER C O   1 
ATOM   11966 C CB  . SER C 1 433 ? 90.098  22.520  -61.324 1.00 83.23  ? 433 SER C CB  1 
ATOM   11967 O OG  . SER C 1 433 ? 90.147  21.145  -60.951 1.00 82.87  ? 433 SER C OG  1 
ATOM   11968 N N   . ILE C 1 434 ? 87.907  23.003  -59.005 1.00 79.84  ? 434 ILE C N   1 
ATOM   11969 C CA  . ILE C 1 434 ? 86.964  22.233  -58.195 1.00 78.43  ? 434 ILE C CA  1 
ATOM   11970 C C   . ILE C 1 434 ? 86.031  21.481  -59.143 1.00 79.79  ? 434 ILE C C   1 
ATOM   11971 O O   . ILE C 1 434 ? 85.244  22.124  -59.838 1.00 80.75  ? 434 ILE C O   1 
ATOM   11972 C CB  . ILE C 1 434 ? 86.168  23.117  -57.215 1.00 76.10  ? 434 ILE C CB  1 
ATOM   11973 C CG1 . ILE C 1 434 ? 87.053  23.792  -56.192 1.00 75.45  ? 434 ILE C CG1 1 
ATOM   11974 C CG2 . ILE C 1 434 ? 85.090  22.284  -56.525 1.00 75.29  ? 434 ILE C CG2 1 
ATOM   11975 C CD1 . ILE C 1 434 ? 86.413  24.917  -55.404 1.00 74.13  ? 434 ILE C CD1 1 
ATOM   11976 N N   . LYS C 1 435 ? 86.131  20.138  -59.161 1.00 81.14  ? 435 LYS C N   1 
ATOM   11977 C CA  . LYS C 1 435 ? 85.289  19.284  -59.988 1.00 82.71  ? 435 LYS C CA  1 
ATOM   11978 C C   . LYS C 1 435 ? 84.204  18.666  -59.115 1.00 81.44  ? 435 LYS C C   1 
ATOM   11979 O O   . LYS C 1 435 ? 84.517  17.763  -58.336 1.00 82.57  ? 435 LYS C O   1 
ATOM   11980 C CB  . LYS C 1 435 ? 86.030  18.118  -60.658 1.00 85.59  ? 435 LYS C CB  1 
ATOM   11981 C CG  . LYS C 1 435 ? 86.915  18.507  -61.835 1.00 88.80  ? 435 LYS C CG  1 
ATOM   11982 C CD  . LYS C 1 435 ? 87.547  17.356  -62.619 1.00 92.07  ? 435 LYS C CD  1 
ATOM   11983 C CE  . LYS C 1 435 ? 88.532  16.537  -61.840 1.00 93.22  ? 435 LYS C CE  1 
ATOM   11984 N NZ  . LYS C 1 435 ? 89.523  15.879  -62.698 1.00 95.59  ? 435 LYS C NZ  1 
ATOM   11985 N N   . THR C 1 436 ? 82.950  19.125  -59.311 1.00 80.02  ? 436 THR C N   1 
ATOM   11986 C CA  . THR C 1 436 ? 81.790  18.739  -58.512 1.00 77.85  ? 436 THR C CA  1 
ATOM   11987 C C   . THR C 1 436 ? 81.110  17.505  -59.109 1.00 77.42  ? 436 THR C C   1 
ATOM   11988 O O   . THR C 1 436 ? 81.035  17.333  -60.320 1.00 77.89  ? 436 THR C O   1 
ATOM   11989 C CB  . THR C 1 436 ? 80.816  19.923  -58.445 1.00 77.51  ? 436 THR C CB  1 
ATOM   11990 O OG1 . THR C 1 436 ? 81.510  21.168  -58.331 1.00 78.15  ? 436 THR C OG1 1 
ATOM   11991 C CG2 . THR C 1 436 ? 79.854  19.806  -57.275 1.00 76.02  ? 436 THR C CG2 1 
ATOM   11992 N N   . LYS C 1 437 ? 80.594  16.638  -58.244 1.00 76.79  ? 437 LYS C N   1 
ATOM   11993 C CA  . LYS C 1 437 ? 79.783  15.518  -58.689 1.00 78.47  ? 437 LYS C CA  1 
ATOM   11994 C C   . LYS C 1 437 ? 78.605  15.342  -57.741 1.00 79.26  ? 437 LYS C C   1 
ATOM   11995 O O   . LYS C 1 437 ? 78.810  15.084  -56.556 1.00 80.21  ? 437 LYS C O   1 
ATOM   11996 C CB  . LYS C 1 437 ? 80.576  14.217  -58.634 1.00 79.41  ? 437 LYS C CB  1 
ATOM   11997 C CG  . LYS C 1 437 ? 79.791  12.932  -58.760 1.00 79.69  ? 437 LYS C CG  1 
ATOM   11998 C CD  . LYS C 1 437 ? 80.654  11.710  -58.473 1.00 80.29  ? 437 LYS C CD  1 
ATOM   11999 C CE  . LYS C 1 437 ? 80.012  10.386  -58.771 1.00 81.26  ? 437 LYS C CE  1 
ATOM   12000 N NZ  . LYS C 1 437 ? 80.811  9.265   -58.244 1.00 82.18  ? 437 LYS C NZ  1 
ATOM   12001 N N   . ILE C 1 438 ? 77.385  15.456  -58.287 1.00 80.31  ? 438 ILE C N   1 
ATOM   12002 C CA  . ILE C 1 438 ? 76.151  15.260  -57.543 1.00 79.29  ? 438 ILE C CA  1 
ATOM   12003 C C   . ILE C 1 438 ? 75.543  13.933  -57.969 1.00 80.36  ? 438 ILE C C   1 
ATOM   12004 O O   . ILE C 1 438 ? 75.237  13.766  -59.149 1.00 81.85  ? 438 ILE C O   1 
ATOM   12005 C CB  . ILE C 1 438 ? 75.175  16.412  -57.828 1.00 79.05  ? 438 ILE C CB  1 
ATOM   12006 C CG1 . ILE C 1 438 ? 75.854  17.746  -57.702 1.00 78.39  ? 438 ILE C CG1 1 
ATOM   12007 C CG2 . ILE C 1 438 ? 73.934  16.344  -56.939 1.00 78.14  ? 438 ILE C CG2 1 
ATOM   12008 C CD1 . ILE C 1 438 ? 75.113  18.844  -58.428 1.00 78.74  ? 438 ILE C CD1 1 
ATOM   12009 N N   . GLU C 1 439 ? 75.377  13.016  -57.007 1.00 80.19  ? 439 GLU C N   1 
ATOM   12010 C CA  . GLU C 1 439 ? 74.550  11.833  -57.207 1.00 81.26  ? 439 GLU C CA  1 
ATOM   12011 C C   . GLU C 1 439 ? 73.091  12.156  -56.877 1.00 79.06  ? 439 GLU C C   1 
ATOM   12012 O O   . GLU C 1 439 ? 72.745  12.424  -55.729 1.00 76.51  ? 439 GLU C O   1 
ATOM   12013 C CB  . GLU C 1 439 ? 75.027  10.663  -56.349 1.00 82.93  ? 439 GLU C CB  1 
ATOM   12014 C CG  . GLU C 1 439 ? 76.367  10.087  -56.801 1.00 85.59  ? 439 GLU C CG  1 
ATOM   12015 C CD  . GLU C 1 439 ? 76.607  8.636   -56.416 1.00 88.18  ? 439 GLU C CD  1 
ATOM   12016 O OE1 . GLU C 1 439 ? 75.802  8.038   -55.669 1.00 89.17  ? 439 GLU C OE1 1 
ATOM   12017 O OE2 . GLU C 1 439 ? 77.608  8.084   -56.898 1.00 91.46  ? 439 GLU C OE2 1 
ATOM   12018 N N   . THR C 1 440 ? 72.233  12.128  -57.897 1.00 79.51  ? 440 THR C N   1 
ATOM   12019 C CA  . THR C 1 440 ? 70.820  12.408  -57.707 1.00 79.30  ? 440 THR C CA  1 
ATOM   12020 C C   . THR C 1 440 ? 70.156  11.208  -57.050 1.00 81.25  ? 440 THR C C   1 
ATOM   12021 O O   . THR C 1 440 ? 70.779  10.169  -56.889 1.00 84.90  ? 440 THR C O   1 
ATOM   12022 C CB  . THR C 1 440 ? 70.154  12.712  -59.043 1.00 79.90  ? 440 THR C CB  1 
ATOM   12023 O OG1 . THR C 1 440 ? 70.380  11.542  -59.821 1.00 81.18  ? 440 THR C OG1 1 
ATOM   12024 C CG2 . THR C 1 440 ? 70.686  13.970  -59.705 1.00 79.65  ? 440 THR C CG2 1 
ATOM   12025 N N   . SER C 1 441 ? 68.875  11.357  -56.720 1.00 81.95  ? 441 SER C N   1 
ATOM   12026 C CA  . SER C 1 441 ? 68.101  10.354  -56.014 1.00 83.26  ? 441 SER C CA  1 
ATOM   12027 C C   . SER C 1 441 ? 66.630  10.724  -56.131 1.00 84.04  ? 441 SER C C   1 
ATOM   12028 O O   . SER C 1 441 ? 66.290  11.858  -55.821 1.00 82.97  ? 441 SER C O   1 
ATOM   12029 C CB  . SER C 1 441 ? 68.509  10.317  -54.575 1.00 82.69  ? 441 SER C CB  1 
ATOM   12030 O OG  . SER C 1 441 ? 67.725  9.364   -53.878 1.00 85.64  ? 441 SER C OG  1 
ATOM   12031 N N   . GLU C 1 442 ? 65.755  9.798   -56.546 1.00 87.62  ? 442 GLU C N   1 
ATOM   12032 C CA  . GLU C 1 442 ? 64.413  10.223  -56.940 1.00 89.29  ? 442 GLU C CA  1 
ATOM   12033 C C   . GLU C 1 442 ? 63.640  10.712  -55.709 1.00 85.88  ? 442 GLU C C   1 
ATOM   12034 O O   . GLU C 1 442 ? 63.966  10.400  -54.566 1.00 84.89  ? 442 GLU C O   1 
ATOM   12035 C CB  . GLU C 1 442 ? 63.692  9.230   -57.858 1.00 93.17  ? 442 GLU C CB  1 
ATOM   12036 C CG  . GLU C 1 442 ? 63.274  7.918   -57.203 1.00 97.41  ? 442 GLU C CG  1 
ATOM   12037 C CD  . GLU C 1 442 ? 62.874  6.845   -58.212 1.00 103.14 ? 442 GLU C CD  1 
ATOM   12038 O OE1 . GLU C 1 442 ? 62.814  7.212   -59.405 1.00 107.19 ? 442 GLU C OE1 1 
ATOM   12039 O OE2 . GLU C 1 442 ? 62.661  5.658   -57.852 1.00 104.09 ? 442 GLU C OE2 1 
ATOM   12040 N N   . ASN C 1 443 ? 62.676  11.590  -55.954 1.00 83.98  ? 443 ASN C N   1 
ATOM   12041 C CA  . ASN C 1 443 ? 61.859  12.173  -54.901 1.00 84.55  ? 443 ASN C CA  1 
ATOM   12042 C C   . ASN C 1 443 ? 62.640  13.186  -54.067 1.00 82.87  ? 443 ASN C C   1 
ATOM   12043 O O   . ASN C 1 443 ? 62.033  13.943  -53.317 1.00 82.81  ? 443 ASN C O   1 
ATOM   12044 C CB  . ASN C 1 443 ? 61.187  11.137  -54.005 1.00 86.09  ? 443 ASN C CB  1 
ATOM   12045 C CG  . ASN C 1 443 ? 60.155  10.304  -54.737 1.00 87.20  ? 443 ASN C CG  1 
ATOM   12046 O OD1 . ASN C 1 443 ? 59.304  10.843  -55.446 1.00 85.54  ? 443 ASN C OD1 1 
ATOM   12047 N ND2 . ASN C 1 443 ? 60.236  8.986   -54.615 1.00 90.19  ? 443 ASN C ND2 1 
ATOM   12048 N N   . PHE C 1 444 ? 63.970  13.231  -54.199 1.00 82.03  ? 444 PHE C N   1 
ATOM   12049 C CA  . PHE C 1 444 ? 64.733  14.404  -53.778 1.00 78.66  ? 444 PHE C CA  1 
ATOM   12050 C C   . PHE C 1 444 ? 64.819  15.337  -54.987 1.00 78.40  ? 444 PHE C C   1 
ATOM   12051 O O   . PHE C 1 444 ? 65.155  14.893  -56.083 1.00 79.67  ? 444 PHE C O   1 
ATOM   12052 C CB  . PHE C 1 444 ? 66.088  13.999  -53.175 1.00 77.20  ? 444 PHE C CB  1 
ATOM   12053 C CG  . PHE C 1 444 ? 66.002  13.231  -51.855 1.00 75.75  ? 444 PHE C CG  1 
ATOM   12054 C CD1 . PHE C 1 444 ? 65.823  11.852  -51.829 1.00 75.77  ? 444 PHE C CD1 1 
ATOM   12055 C CD2 . PHE C 1 444 ? 66.100  13.895  -50.636 1.00 74.17  ? 444 PHE C CD2 1 
ATOM   12056 C CE1 . PHE C 1 444 ? 65.729  11.174  -50.623 1.00 75.75  ? 444 PHE C CE1 1 
ATOM   12057 C CE2 . PHE C 1 444 ? 66.006  13.207  -49.435 1.00 73.92  ? 444 PHE C CE2 1 
ATOM   12058 C CZ  . PHE C 1 444 ? 65.813  11.850  -49.428 1.00 74.68  ? 444 PHE C CZ  1 
ATOM   12059 N N   . THR C 1 445 ? 64.446  16.612  -54.782 1.00 77.28  ? 445 THR C N   1 
ATOM   12060 C CA  . THR C 1 445 ? 64.450  17.630  -55.827 1.00 76.37  ? 445 THR C CA  1 
ATOM   12061 C C   . THR C 1 445 ? 65.646  18.549  -55.613 1.00 75.23  ? 445 THR C C   1 
ATOM   12062 O O   . THR C 1 445 ? 65.823  19.065  -54.510 1.00 72.73  ? 445 THR C O   1 
ATOM   12063 C CB  . THR C 1 445 ? 63.147  18.430  -55.787 1.00 75.26  ? 445 THR C CB  1 
ATOM   12064 O OG1 . THR C 1 445 ? 62.125  17.443  -55.885 1.00 76.67  ? 445 THR C OG1 1 
ATOM   12065 C CG2 . THR C 1 445 ? 63.025  19.424  -56.928 1.00 75.09  ? 445 THR C CG2 1 
ATOM   12066 N N   . LEU C 1 446 ? 66.434  18.756  -56.676 1.00 76.72  ? 446 LEU C N   1 
ATOM   12067 C CA  . LEU C 1 446 ? 67.552  19.692  -56.627 1.00 79.21  ? 446 LEU C CA  1 
ATOM   12068 C C   . LEU C 1 446 ? 67.036  21.089  -56.978 1.00 80.61  ? 446 LEU C C   1 
ATOM   12069 O O   . LEU C 1 446 ? 66.410  21.298  -58.017 1.00 80.92  ? 446 LEU C O   1 
ATOM   12070 C CB  . LEU C 1 446 ? 68.724  19.242  -57.503 1.00 79.28  ? 446 LEU C CB  1 
ATOM   12071 C CG  . LEU C 1 446 ? 69.276  17.856  -57.146 1.00 80.31  ? 446 LEU C CG  1 
ATOM   12072 C CD1 . LEU C 1 446 ? 70.319  17.362  -58.127 1.00 81.69  ? 446 LEU C CD1 1 
ATOM   12073 C CD2 . LEU C 1 446 ? 69.829  17.840  -55.730 1.00 79.52  ? 446 LEU C CD2 1 
ATOM   12074 N N   . LEU C 1 447 ? 67.215  22.002  -56.031 1.00 81.04  ? 447 LEU C N   1 
ATOM   12075 C CA  . LEU C 1 447 ? 66.592  23.326  -56.246 1.00 83.48  ? 447 LEU C CA  1 
ATOM   12076 C C   . LEU C 1 447 ? 67.634  24.435  -56.348 1.00 82.26  ? 447 LEU C C   1 
ATOM   12077 O O   . LEU C 1 447 ? 68.631  24.383  -55.600 1.00 80.28  ? 447 LEU C O   1 
ATOM   12078 C CB  . LEU C 1 447 ? 65.558  23.611  -55.151 1.00 83.95  ? 447 LEU C CB  1 
ATOM   12079 C CG  . LEU C 1 447 ? 66.073  23.793  -53.722 1.00 85.12  ? 447 LEU C CG  1 
ATOM   12080 C CD1 . LEU C 1 447 ? 66.011  25.256  -53.345 1.00 89.57  ? 447 LEU C CD1 1 
ATOM   12081 C CD2 . LEU C 1 447 ? 65.224  22.991  -52.763 1.00 83.79  ? 447 LEU C CD2 1 
ATOM   12082 N N   . ASP C 1 448 ? 67.432  25.330  -57.306 1.00 84.70  ? 448 ASP C N   1 
ATOM   12083 C CA  . ASP C 1 448 ? 68.265  26.557  -57.413 1.00 87.06  ? 448 ASP C CA  1 
ATOM   12084 C C   . ASP C 1 448 ? 69.594  26.313  -58.103 1.00 82.79  ? 448 ASP C C   1 
ATOM   12085 O O   . ASP C 1 448 ? 69.618  25.685  -59.180 1.00 83.43  ? 448 ASP C O   1 
ATOM   12086 C CB  . ASP C 1 448 ? 68.457  27.266  -56.078 1.00 89.85  ? 448 ASP C CB  1 
ATOM   12087 C CG  . ASP C 1 448 ? 67.223  27.985  -55.553 1.00 87.79  ? 448 ASP C CG  1 
ATOM   12088 O OD1 . ASP C 1 448 ? 66.329  28.280  -56.370 1.00 87.20  ? 448 ASP C OD1 1 
ATOM   12089 O OD2 . ASP C 1 448 ? 67.165  28.239  -54.332 1.00 83.84  ? 448 ASP C OD2 1 
ATOM   12090 N N   . ASP C 1 449 ? 70.645  26.832  -57.488 1.00 81.25  ? 449 ASP C N   1 
ATOM   12091 C CA  . ASP C 1 449 ? 71.927  26.775  -58.217 1.00 82.65  ? 449 ASP C CA  1 
ATOM   12092 C C   . ASP C 1 449 ? 73.071  26.221  -57.391 1.00 77.68  ? 449 ASP C C   1 
ATOM   12093 O O   . ASP C 1 449 ? 73.224  26.631  -56.230 1.00 74.64  ? 449 ASP C O   1 
ATOM   12094 C CB  . ASP C 1 449 ? 72.318  28.148  -58.745 1.00 85.54  ? 449 ASP C CB  1 
ATOM   12095 C CG  . ASP C 1 449 ? 72.103  28.373  -60.233 1.00 88.17  ? 449 ASP C CG  1 
ATOM   12096 O OD1 . ASP C 1 449 ? 71.371  27.572  -60.846 1.00 91.22  ? 449 ASP C OD1 1 
ATOM   12097 O OD2 . ASP C 1 449 ? 72.666  29.351  -60.763 1.00 87.95  ? 449 ASP C OD2 1 
ATOM   12098 N N   . LEU C 1 450 ? 73.725  25.208  -57.926 1.00 76.97  ? 450 LEU C N   1 
ATOM   12099 C CA  . LEU C 1 450 ? 74.999  24.766  -57.408 1.00 76.49  ? 450 LEU C CA  1 
ATOM   12100 C C   . LEU C 1 450 ? 75.902  25.973  -57.158 1.00 76.38  ? 450 LEU C C   1 
ATOM   12101 O O   . LEU C 1 450 ? 76.084  26.813  -58.038 1.00 76.06  ? 450 LEU C O   1 
ATOM   12102 C CB  . LEU C 1 450 ? 75.540  23.856  -58.499 1.00 77.06  ? 450 LEU C CB  1 
ATOM   12103 C CG  . LEU C 1 450 ? 76.921  23.286  -58.221 1.00 77.76  ? 450 LEU C CG  1 
ATOM   12104 C CD1 . LEU C 1 450 ? 76.883  22.504  -56.922 1.00 77.07  ? 450 LEU C CD1 1 
ATOM   12105 C CD2 . LEU C 1 450 ? 77.376  22.440  -59.396 1.00 79.28  ? 450 LEU C CD2 1 
ATOM   12106 N N   . LYS C 1 451 ? 76.452  26.045  -55.942 1.00 75.84  ? 451 LYS C N   1 
ATOM   12107 C CA  . LYS C 1 451 ? 77.346  27.121  -55.541 1.00 76.12  ? 451 LYS C CA  1 
ATOM   12108 C C   . LYS C 1 451 ? 78.732  26.546  -55.251 1.00 76.19  ? 451 LYS C C   1 
ATOM   12109 O O   . LYS C 1 451 ? 78.842  25.475  -54.649 1.00 75.95  ? 451 LYS C O   1 
ATOM   12110 C CB  . LYS C 1 451 ? 76.766  27.841  -54.323 1.00 75.51  ? 451 LYS C CB  1 
ATOM   12111 C CG  . LYS C 1 451 ? 75.459  28.492  -54.640 1.00 76.80  ? 451 LYS C CG  1 
ATOM   12112 C CD  . LYS C 1 451 ? 74.999  29.490  -53.589 1.00 77.80  ? 451 LYS C CD  1 
ATOM   12113 C CE  . LYS C 1 451 ? 73.729  30.151  -53.998 1.00 78.39  ? 451 LYS C CE  1 
ATOM   12114 N NZ  . LYS C 1 451 ? 73.527  31.298  -53.117 1.00 80.55  ? 451 LYS C NZ  1 
ATOM   12115 N N   . ILE C 1 452 ? 79.769  27.253  -55.740 1.00 76.66  ? 452 ILE C N   1 
ATOM   12116 C CA  . ILE C 1 452 ? 81.163  26.832  -55.660 1.00 76.18  ? 452 ILE C CA  1 
ATOM   12117 C C   . ILE C 1 452 ? 81.951  27.977  -55.024 1.00 76.33  ? 452 ILE C C   1 
ATOM   12118 O O   . ILE C 1 452 ? 81.694  29.130  -55.379 1.00 77.81  ? 452 ILE C O   1 
ATOM   12119 C CB  . ILE C 1 452 ? 81.722  26.463  -57.052 1.00 76.88  ? 452 ILE C CB  1 
ATOM   12120 C CG1 . ILE C 1 452 ? 81.330  25.054  -57.538 1.00 76.79  ? 452 ILE C CG1 1 
ATOM   12121 C CG2 . ILE C 1 452 ? 83.237  26.559  -57.028 1.00 78.06  ? 452 ILE C CG2 1 
ATOM   12122 C CD1 . ILE C 1 452 ? 79.862  24.826  -57.834 1.00 75.64  ? 452 ILE C CD1 1 
ATOM   12123 N N   . SER C 1 453 ? 82.894  27.647  -54.107 1.00 75.47  ? 453 SER C N   1 
ATOM   12124 C CA  . SER C 1 453 ? 83.705  28.613  -53.357 1.00 74.75  ? 453 SER C CA  1 
ATOM   12125 C C   . SER C 1 453 ? 85.142  28.121  -53.143 1.00 74.80  ? 453 SER C C   1 
ATOM   12126 O O   . SER C 1 453 ? 85.379  27.038  -52.613 1.00 73.67  ? 453 SER C O   1 
ATOM   12127 C CB  . SER C 1 453 ? 83.087  28.944  -52.013 1.00 73.61  ? 453 SER C CB  1 
ATOM   12128 O OG  . SER C 1 453 ? 84.059  29.309  -51.039 1.00 73.79  ? 453 SER C OG  1 
ATOM   12129 N N   . TYR C 1 454 ? 86.090  29.007  -53.470 1.00 75.66  ? 454 TYR C N   1 
ATOM   12130 C CA  . TYR C 1 454 ? 87.498  28.851  -53.167 1.00 75.80  ? 454 TYR C CA  1 
ATOM   12131 C C   . TYR C 1 454 ? 87.963  29.983  -52.244 1.00 76.53  ? 454 TYR C C   1 
ATOM   12132 O O   . TYR C 1 454 ? 88.447  31.014  -52.720 1.00 78.38  ? 454 TYR C O   1 
ATOM   12133 C CB  . TYR C 1 454 ? 88.150  28.845  -54.552 1.00 76.94  ? 454 TYR C CB  1 
ATOM   12134 C CG  . TYR C 1 454 ? 89.543  28.229  -54.582 1.00 77.79  ? 454 TYR C CG  1 
ATOM   12135 C CD1 . TYR C 1 454 ? 89.709  26.847  -54.494 1.00 77.26  ? 454 TYR C CD1 1 
ATOM   12136 C CD2 . TYR C 1 454 ? 90.675  29.011  -54.691 1.00 78.91  ? 454 TYR C CD2 1 
ATOM   12137 C CE1 . TYR C 1 454 ? 90.954  26.256  -54.513 1.00 78.03  ? 454 TYR C CE1 1 
ATOM   12138 C CE2 . TYR C 1 454 ? 91.930  28.427  -54.732 1.00 80.53  ? 454 TYR C CE2 1 
ATOM   12139 C CZ  . TYR C 1 454 ? 92.076  27.048  -54.641 1.00 79.75  ? 454 TYR C CZ  1 
ATOM   12140 O OH  . TYR C 1 454 ? 93.308  26.455  -54.666 1.00 80.27  ? 454 TYR C OH  1 
ATOM   12141 N N   . ASN C 1 455 ? 87.825  29.798  -50.923 1.00 75.77  ? 455 ASN C N   1 
ATOM   12142 C CA  . ASN C 1 455 ? 88.084  30.864  -49.962 1.00 76.69  ? 455 ASN C CA  1 
ATOM   12143 C C   . ASN C 1 455 ? 89.567  30.896  -49.621 1.00 77.51  ? 455 ASN C C   1 
ATOM   12144 O O   . ASN C 1 455 ? 90.040  30.062  -48.850 1.00 77.07  ? 455 ASN C O   1 
ATOM   12145 C CB  . ASN C 1 455 ? 87.249  30.700  -48.697 1.00 76.58  ? 455 ASN C CB  1 
ATOM   12146 C CG  . ASN C 1 455 ? 87.271  31.907  -47.789 1.00 78.46  ? 455 ASN C CG  1 
ATOM   12147 O OD1 . ASN C 1 455 ? 86.466  31.988  -46.846 1.00 78.47  ? 455 ASN C OD1 1 
ATOM   12148 N ND2 . ASN C 1 455 ? 88.136  32.873  -48.069 1.00 80.42  ? 455 ASN C ND2 1 
ATOM   12149 N N   . THR C 1 456 ? 90.269  31.884  -50.197 1.00 78.58  ? 456 THR C N   1 
ATOM   12150 C CA  . THR C 1 456 ? 91.721  31.958  -50.163 1.00 79.71  ? 456 THR C CA  1 
ATOM   12151 C C   . THR C 1 456 ? 92.226  32.540  -48.844 1.00 79.89  ? 456 THR C C   1 
ATOM   12152 O O   . THR C 1 456 ? 93.417  32.633  -48.636 1.00 81.46  ? 456 THR C O   1 
ATOM   12153 C CB  . THR C 1 456 ? 92.187  32.751  -51.382 1.00 81.48  ? 456 THR C CB  1 
ATOM   12154 O OG1 . THR C 1 456 ? 91.231  33.779  -51.651 1.00 81.12  ? 456 THR C OG1 1 
ATOM   12155 C CG2 . THR C 1 456 ? 92.339  31.834  -52.583 1.00 81.82  ? 456 THR C CG2 1 
ATOM   12156 N N   . HIS C 1 457 ? 91.323  32.950  -47.958 1.00 79.27  ? 457 HIS C N   1 
ATOM   12157 C CA  . HIS C 1 457 ? 91.620  33.175  -46.550 1.00 79.45  ? 457 HIS C CA  1 
ATOM   12158 C C   . HIS C 1 457 ? 92.435  34.439  -46.327 1.00 81.16  ? 457 HIS C C   1 
ATOM   12159 O O   . HIS C 1 457 ? 92.810  34.686  -45.179 1.00 81.70  ? 457 HIS C O   1 
ATOM   12160 C CB  . HIS C 1 457 ? 92.300  31.965  -45.904 1.00 79.25  ? 457 HIS C CB  1 
ATOM   12161 C CG  . HIS C 1 457 ? 91.335  30.914  -45.467 1.00 77.78  ? 457 HIS C CG  1 
ATOM   12162 N ND1 . HIS C 1 457 ? 90.719  30.019  -46.321 1.00 76.52  ? 457 HIS C ND1 1 
ATOM   12163 C CD2 . HIS C 1 457 ? 90.867  30.648  -44.241 1.00 77.18  ? 457 HIS C CD2 1 
ATOM   12164 C CE1 . HIS C 1 457 ? 89.940  29.223  -45.614 1.00 75.36  ? 457 HIS C CE1 1 
ATOM   12165 N NE2 . HIS C 1 457 ? 90.006  29.589  -44.351 1.00 75.76  ? 457 HIS C NE2 1 
ATOM   12166 N N   . LEU C 1 458 ? 92.651  35.209  -47.418 1.00 82.04  ? 458 LEU C N   1 
ATOM   12167 C CA  . LEU C 1 458 ? 93.286  36.523  -47.404 1.00 83.49  ? 458 LEU C CA  1 
ATOM   12168 C C   . LEU C 1 458 ? 92.410  37.463  -46.595 1.00 83.07  ? 458 LEU C C   1 
ATOM   12169 O O   . LEU C 1 458 ? 91.501  38.074  -47.148 1.00 82.67  ? 458 LEU C O   1 
ATOM   12170 C CB  . LEU C 1 458 ? 93.454  37.123  -48.799 1.00 84.57  ? 458 LEU C CB  1 
ATOM   12171 C CG  . LEU C 1 458 ? 94.138  36.252  -49.852 1.00 84.93  ? 458 LEU C CG  1 
ATOM   12172 C CD1 . LEU C 1 458 ? 94.184  37.031  -51.160 1.00 86.24  ? 458 LEU C CD1 1 
ATOM   12173 C CD2 . LEU C 1 458 ? 95.526  35.771  -49.414 1.00 86.02  ? 458 LEU C CD2 1 
ATOM   12174 N N   . GLY C 1 459 ? 92.678  37.535  -45.293 1.00 83.30  ? 459 GLY C N   1 
ATOM   12175 C CA  . GLY C 1 459 ? 91.962  38.433  -44.405 1.00 83.87  ? 459 GLY C CA  1 
ATOM   12176 C C   . GLY C 1 459 ? 90.494  38.048  -44.251 1.00 81.94  ? 459 GLY C C   1 
ATOM   12177 O O   . GLY C 1 459 ? 90.203  36.976  -43.734 1.00 80.41  ? 459 GLY C O   1 
ATOM   12178 N N   . TRP C 1 460 ? 89.587  38.946  -44.688 1.00 82.43  ? 460 TRP C N   1 
ATOM   12179 C CA  . TRP C 1 460 ? 88.148  38.719  -44.615 1.00 80.89  ? 460 TRP C CA  1 
ATOM   12180 C C   . TRP C 1 460 ? 87.543  38.422  -45.990 1.00 80.44  ? 460 TRP C C   1 
ATOM   12181 O O   . TRP C 1 460 ? 86.418  37.920  -46.081 1.00 78.51  ? 460 TRP C O   1 
ATOM   12182 C CB  . TRP C 1 460 ? 87.461  39.914  -43.961 1.00 81.64  ? 460 TRP C CB  1 
ATOM   12183 C CG  . TRP C 1 460 ? 87.786  40.102  -42.508 1.00 82.43  ? 460 TRP C CG  1 
ATOM   12184 C CD1 . TRP C 1 460 ? 88.548  41.092  -41.979 1.00 84.75  ? 460 TRP C CD1 1 
ATOM   12185 C CD2 . TRP C 1 460 ? 87.376  39.282  -41.395 1.00 81.57  ? 460 TRP C CD2 1 
ATOM   12186 N NE1 . TRP C 1 460 ? 88.613  40.976  -40.619 1.00 85.22  ? 460 TRP C NE1 1 
ATOM   12187 C CE2 . TRP C 1 460 ? 87.914  39.872  -40.229 1.00 83.35  ? 460 TRP C CE2 1 
ATOM   12188 C CE3 . TRP C 1 460 ? 86.616  38.115  -41.264 1.00 79.71  ? 460 TRP C CE3 1 
ATOM   12189 C CZ2 . TRP C 1 460 ? 87.728  39.333  -38.958 1.00 83.43  ? 460 TRP C CZ2 1 
ATOM   12190 C CZ3 . TRP C 1 460 ? 86.430  37.579  -40.005 1.00 79.69  ? 460 TRP C CZ3 1 
ATOM   12191 C CH2 . TRP C 1 460 ? 86.989  38.172  -38.869 1.00 81.57  ? 460 TRP C CH2 1 
ATOM   12192 N N   . ALA C 1 461 ? 88.307  38.703  -47.056 1.00 82.28  ? 461 ALA C N   1 
ATOM   12193 C CA  . ALA C 1 461 ? 87.930  38.307  -48.405 1.00 82.80  ? 461 ALA C CA  1 
ATOM   12194 C C   . ALA C 1 461 ? 87.521  36.832  -48.444 1.00 82.17  ? 461 ALA C C   1 
ATOM   12195 O O   . ALA C 1 461 ? 88.282  35.954  -48.011 1.00 84.49  ? 461 ALA C O   1 
ATOM   12196 C CB  . ALA C 1 461 ? 89.087  38.565  -49.346 1.00 84.08  ? 461 ALA C CB  1 
ATOM   12197 N N   . ILE C 1 462 ? 86.367  36.547  -49.041 1.00 80.79  ? 462 ILE C N   1 
ATOM   12198 C CA  . ILE C 1 462 ? 85.920  35.170  -49.112 1.00 80.43  ? 462 ILE C CA  1 
ATOM   12199 C C   . ILE C 1 462 ? 86.419  34.465  -50.383 1.00 80.61  ? 462 ILE C C   1 
ATOM   12200 O O   . ILE C 1 462 ? 86.144  33.274  -50.567 1.00 80.07  ? 462 ILE C O   1 
ATOM   12201 C CB  . ILE C 1 462 ? 84.390  35.107  -48.978 1.00 80.10  ? 462 ILE C CB  1 
ATOM   12202 C CG1 . ILE C 1 462 ? 83.697  35.844  -50.124 1.00 81.44  ? 462 ILE C CG1 1 
ATOM   12203 C CG2 . ILE C 1 462 ? 83.938  35.607  -47.603 1.00 79.99  ? 462 ILE C CG2 1 
ATOM   12204 C CD1 . ILE C 1 462 ? 83.256  34.942  -51.264 1.00 81.07  ? 462 ILE C CD1 1 
ATOM   12205 N N   . GLY C 1 463 ? 87.135  35.181  -51.260 1.00 81.79  ? 463 GLY C N   1 
ATOM   12206 C CA  . GLY C 1 463 ? 87.692  34.597  -52.473 1.00 81.87  ? 463 GLY C CA  1 
ATOM   12207 C C   . GLY C 1 463 ? 86.633  34.492  -53.563 1.00 81.41  ? 463 GLY C C   1 
ATOM   12208 O O   . GLY C 1 463 ? 85.531  34.981  -53.385 1.00 80.87  ? 463 GLY C O   1 
ATOM   12209 N N   . SER C 1 464 ? 86.959  33.858  -54.690 1.00 82.69  ? 464 SER C N   1 
ATOM   12210 C CA  . SER C 1 464 ? 85.971  33.627  -55.732 1.00 83.32  ? 464 SER C CA  1 
ATOM   12211 C C   . SER C 1 464 ? 84.861  32.700  -55.244 1.00 83.55  ? 464 SER C C   1 
ATOM   12212 O O   . SER C 1 464 ? 85.023  31.937  -54.282 1.00 81.59  ? 464 SER C O   1 
ATOM   12213 C CB  . SER C 1 464 ? 86.581  33.082  -56.981 1.00 84.15  ? 464 SER C CB  1 
ATOM   12214 O OG  . SER C 1 464 ? 87.452  34.042  -57.552 1.00 86.04  ? 464 SER C OG  1 
ATOM   12215 N N   . GLN C 1 465 ? 83.712  32.868  -55.922 1.00 87.15  ? 465 GLN C N   1 
ATOM   12216 C CA  . GLN C 1 465 ? 82.508  32.050  -55.833 1.00 87.20  ? 465 GLN C CA  1 
ATOM   12217 C C   . GLN C 1 465 ? 81.989  31.805  -57.252 1.00 87.93  ? 465 GLN C C   1 
ATOM   12218 O O   . GLN C 1 465 ? 82.490  32.395  -58.204 1.00 91.01  ? 465 GLN C O   1 
ATOM   12219 C CB  . GLN C 1 465 ? 81.443  32.778  -55.014 1.00 88.09  ? 465 GLN C CB  1 
ATOM   12220 C CG  . GLN C 1 465 ? 81.478  32.449  -53.526 1.00 89.83  ? 465 GLN C CG  1 
ATOM   12221 C CD  . GLN C 1 465 ? 80.339  33.079  -52.749 1.00 91.79  ? 465 GLN C CD  1 
ATOM   12222 O OE1 . GLN C 1 465 ? 80.420  34.248  -52.339 1.00 98.25  ? 465 GLN C OE1 1 
ATOM   12223 N NE2 . GLN C 1 465 ? 79.280  32.310  -52.520 1.00 88.56  ? 465 GLN C NE2 1 
ATOM   12224 N N   . ALA C 1 466 ? 80.985  30.946  -57.424 1.00 86.72  ? 466 ALA C N   1 
ATOM   12225 C CA  . ALA C 1 466 ? 80.379  30.820  -58.740 1.00 87.16  ? 466 ALA C CA  1 
ATOM   12226 C C   . ALA C 1 466 ? 79.060  30.070  -58.641 1.00 86.13  ? 466 ALA C C   1 
ATOM   12227 O O   . ALA C 1 466 ? 78.967  29.079  -57.924 1.00 85.52  ? 466 ALA C O   1 
ATOM   12228 C CB  . ALA C 1 466 ? 81.336  30.133  -59.687 1.00 87.92  ? 466 ALA C CB  1 
ATOM   12229 N N   . SER C 1 467 ? 78.056  30.555  -59.371 1.00 86.96  ? 467 SER C N   1 
ATOM   12230 C CA  . SER C 1 467 ? 76.760  29.900  -59.442 1.00 86.10  ? 467 SER C CA  1 
ATOM   12231 C C   . SER C 1 467 ? 76.649  29.128  -60.749 1.00 85.40  ? 467 SER C C   1 
ATOM   12232 O O   . SER C 1 467 ? 76.747  29.715  -61.814 1.00 85.90  ? 467 SER C O   1 
ATOM   12233 C CB  . SER C 1 467 ? 75.644  30.894  -59.335 1.00 88.55  ? 467 SER C CB  1 
ATOM   12234 O OG  . SER C 1 467 ? 75.338  31.193  -57.981 1.00 91.19  ? 467 SER C OG  1 
ATOM   12235 N N   . VAL C 1 468 ? 76.411  27.821  -60.671 1.00 84.44  ? 468 VAL C N   1 
ATOM   12236 C CA  . VAL C 1 468 ? 76.320  27.011  -61.871 1.00 85.60  ? 468 VAL C CA  1 
ATOM   12237 C C   . VAL C 1 468 ? 74.886  26.515  -62.038 1.00 84.24  ? 468 VAL C C   1 
ATOM   12238 O O   . VAL C 1 468 ? 74.272  26.021  -61.093 1.00 81.78  ? 468 VAL C O   1 
ATOM   12239 C CB  . VAL C 1 468 ? 77.343  25.863  -61.768 1.00 87.83  ? 468 VAL C CB  1 
ATOM   12240 C CG1 . VAL C 1 468 ? 77.226  24.859  -62.915 1.00 89.24  ? 468 VAL C CG1 1 
ATOM   12241 C CG2 . VAL C 1 468 ? 78.769  26.401  -61.663 1.00 88.72  ? 468 VAL C CG2 1 
ATOM   12242 N N   . SER C 1 469 ? 74.365  26.679  -63.256 1.00 85.90  ? 469 SER C N   1 
ATOM   12243 C CA  . SER C 1 469 ? 73.024  26.235  -63.590 1.00 86.90  ? 469 SER C CA  1 
ATOM   12244 C C   . SER C 1 469 ? 73.085  24.757  -63.924 1.00 88.38  ? 469 SER C C   1 
ATOM   12245 O O   . SER C 1 469 ? 74.002  24.337  -64.619 1.00 90.59  ? 469 SER C O   1 
ATOM   12246 C CB  . SER C 1 469 ? 72.454  26.999  -64.748 1.00 88.65  ? 469 SER C CB  1 
ATOM   12247 O OG  . SER C 1 469 ? 71.108  26.607  -64.972 1.00 89.69  ? 469 SER C OG  1 
ATOM   12248 N N   . ILE C 1 470 ? 72.129  23.976  -63.413 1.00 88.37  ? 470 ILE C N   1 
ATOM   12249 C CA  . ILE C 1 470 ? 72.090  22.563  -63.743 1.00 89.72  ? 470 ILE C CA  1 
ATOM   12250 C C   . ILE C 1 470 ? 70.840  22.265  -64.557 1.00 92.80  ? 470 ILE C C   1 
ATOM   12251 O O   . ILE C 1 470 ? 70.628  21.105  -64.903 1.00 95.45  ? 470 ILE C O   1 
ATOM   12252 C CB  . ILE C 1 470 ? 72.177  21.675  -62.490 1.00 88.88  ? 470 ILE C CB  1 
ATOM   12253 C CG1 . ILE C 1 470 ? 71.083  22.000  -61.479 1.00 88.90  ? 470 ILE C CG1 1 
ATOM   12254 C CG2 . ILE C 1 470 ? 73.567  21.756  -61.856 1.00 87.78  ? 470 ILE C CG2 1 
ATOM   12255 C CD1 . ILE C 1 470 ? 71.073  21.054  -60.290 1.00 89.40  ? 470 ILE C CD1 1 
ATOM   12256 N N   . SER C 1 471 ? 70.062  23.315  -64.891 1.00 92.47  ? 471 SER C N   1 
ATOM   12257 C CA  . SER C 1 471 ? 68.842  23.182  -65.673 1.00 92.02  ? 471 SER C CA  1 
ATOM   12258 C C   . SER C 1 471 ? 69.047  22.221  -66.846 1.00 93.32  ? 471 SER C C   1 
ATOM   12259 O O   . SER C 1 471 ? 68.229  21.335  -67.056 1.00 94.79  ? 471 SER C O   1 
ATOM   12260 C CB  . SER C 1 471 ? 68.295  24.525  -66.120 1.00 93.41  ? 471 SER C CB  1 
ATOM   12261 O OG  . SER C 1 471 ? 69.304  25.476  -66.435 1.00 93.76  ? 471 SER C OG  1 
ATOM   12262 N N   . ASP C 1 472 ? 70.168  22.338  -67.564 1.00 94.55  ? 472 ASP C N   1 
ATOM   12263 C CA  . ASP C 1 472 ? 70.455  21.453  -68.685 1.00 95.69  ? 472 ASP C CA  1 
ATOM   12264 C C   . ASP C 1 472 ? 71.001  20.094  -68.246 1.00 94.67  ? 472 ASP C C   1 
ATOM   12265 O O   . ASP C 1 472 ? 71.494  19.378  -69.103 1.00 95.80  ? 472 ASP C O   1 
ATOM   12266 C CB  . ASP C 1 472 ? 71.456  22.067  -69.652 1.00 97.43  ? 472 ASP C CB  1 
ATOM   12267 C CG  . ASP C 1 472 ? 72.807  22.408  -69.039 1.00 97.72  ? 472 ASP C CG  1 
ATOM   12268 O OD1 . ASP C 1 472 ? 72.875  22.451  -67.792 1.00 96.49  ? 472 ASP C OD1 1 
ATOM   12269 O OD2 . ASP C 1 472 ? 73.782  22.604  -69.804 1.00 99.55  ? 472 ASP C OD2 1 
ATOM   12270 N N   . GLN C 1 473 ? 70.904  19.708  -66.961 1.00 93.50  ? 473 GLN C N   1 
ATOM   12271 C CA  . GLN C 1 473 ? 71.341  18.377  -66.533 1.00 94.55  ? 473 GLN C CA  1 
ATOM   12272 C C   . GLN C 1 473 ? 70.358  17.673  -65.583 1.00 94.34  ? 473 GLN C C   1 
ATOM   12273 O O   . GLN C 1 473 ? 70.720  16.653  -64.991 1.00 93.49  ? 473 GLN C O   1 
ATOM   12274 C CB  . GLN C 1 473 ? 72.711  18.417  -65.842 1.00 92.95  ? 473 GLN C CB  1 
ATOM   12275 C CG  . GLN C 1 473 ? 73.905  18.589  -66.774 1.00 94.15  ? 473 GLN C CG  1 
ATOM   12276 C CD  . GLN C 1 473 ? 75.222  18.661  -66.028 1.00 93.64  ? 473 GLN C CD  1 
ATOM   12277 O OE1 . GLN C 1 473 ? 75.786  17.647  -65.599 1.00 95.65  ? 473 GLN C OE1 1 
ATOM   12278 N NE2 . GLN C 1 473 ? 75.742  19.868  -65.873 1.00 92.73  ? 473 GLN C NE2 1 
ATOM   12279 N N   . LEU C 1 474 ? 69.116  18.164  -65.446 1.00 94.48  ? 474 LEU C N   1 
ATOM   12280 C CA  . LEU C 1 474 ? 68.201  17.616  -64.449 1.00 95.35  ? 474 LEU C CA  1 
ATOM   12281 C C   . LEU C 1 474 ? 67.901  16.144  -64.736 1.00 96.67  ? 474 LEU C C   1 
ATOM   12282 O O   . LEU C 1 474 ? 67.660  15.376  -63.808 1.00 96.24  ? 474 LEU C O   1 
ATOM   12283 C CB  . LEU C 1 474 ? 66.900  18.412  -64.342 1.00 97.72  ? 474 LEU C CB  1 
ATOM   12284 C CG  . LEU C 1 474 ? 66.860  19.565  -63.330 1.00 97.46  ? 474 LEU C CG  1 
ATOM   12285 C CD1 . LEU C 1 474 ? 67.355  19.151  -61.948 1.00 97.08  ? 474 LEU C CD1 1 
ATOM   12286 C CD2 . LEU C 1 474 ? 67.649  20.741  -63.846 1.00 97.87  ? 474 LEU C CD2 1 
ATOM   12287 N N   . ASP C 1 475 ? 67.917  15.751  -66.015 1.00 98.31  ? 475 ASP C N   1 
ATOM   12288 C CA  . ASP C 1 475 ? 67.644  14.375  -66.402 1.00 101.20 ? 475 ASP C CA  1 
ATOM   12289 C C   . ASP C 1 475 ? 68.650  13.394  -65.798 1.00 102.67 ? 475 ASP C C   1 
ATOM   12290 O O   . ASP C 1 475 ? 68.303  12.247  -65.519 1.00 103.36 ? 475 ASP C O   1 
ATOM   12291 C CB  . ASP C 1 475 ? 67.842  14.150  -67.890 1.00 105.05 ? 475 ASP C CB  1 
ATOM   12292 C CG  . ASP C 1 475 ? 67.009  14.982  -68.845 1.00 107.35 ? 475 ASP C CG  1 
ATOM   12293 O OD1 . ASP C 1 475 ? 65.956  15.512  -68.406 1.00 109.74 ? 475 ASP C OD1 1 
ATOM   12294 O OD2 . ASP C 1 475 ? 67.434  15.081  -70.022 1.00 108.06 ? 475 ASP C OD2 1 
ATOM   12295 N N   . LYS C 1 476 ? 69.913  13.831  -65.666 1.00 100.72 ? 476 LYS C N   1 
ATOM   12296 C CA  . LYS C 1 476 ? 71.035  12.924  -65.502 1.00 99.07  ? 476 LYS C CA  1 
ATOM   12297 C C   . LYS C 1 476 ? 71.089  12.385  -64.075 1.00 95.45  ? 476 LYS C C   1 
ATOM   12298 O O   . LYS C 1 476 ? 70.658  13.053  -63.140 1.00 91.25  ? 476 LYS C O   1 
ATOM   12299 C CB  . LYS C 1 476 ? 72.343  13.635  -65.878 1.00 100.17 ? 476 LYS C CB  1 
ATOM   12300 C CG  . LYS C 1 476 ? 72.480  14.015  -67.350 1.00 102.55 ? 476 LYS C CG  1 
ATOM   12301 C CD  . LYS C 1 476 ? 73.697  14.876  -67.666 1.00 103.34 ? 476 LYS C CD  1 
ATOM   12302 C CE  . LYS C 1 476 ? 75.005  14.148  -67.620 1.00 105.65 ? 476 LYS C CE  1 
ATOM   12303 N NZ  . LYS C 1 476 ? 76.138  15.029  -67.933 1.00 105.88 ? 476 LYS C NZ  1 
ATOM   12304 N N   . LYS C 1 477 ? 71.657  11.174  -63.938 1.00 96.24  ? 477 LYS C N   1 
ATOM   12305 C CA  . LYS C 1 477 ? 71.844  10.519  -62.653 1.00 94.49  ? 477 LYS C CA  1 
ATOM   12306 C C   . LYS C 1 477 ? 73.052  11.129  -61.942 1.00 92.57  ? 477 LYS C C   1 
ATOM   12307 O O   . LYS C 1 477 ? 73.041  11.330  -60.726 1.00 91.15  ? 477 LYS C O   1 
ATOM   12308 C CB  . LYS C 1 477 ? 71.998  9.014   -62.890 1.00 97.21  ? 477 LYS C CB  1 
ATOM   12309 C CG  . LYS C 1 477 ? 72.126  8.147   -61.632 1.00 98.74  ? 477 LYS C CG  1 
ATOM   12310 C CD  . LYS C 1 477 ? 70.839  7.900   -60.846 1.00 99.93  ? 477 LYS C CD  1 
ATOM   12311 C CE  . LYS C 1 477 ? 71.038  7.161   -59.547 1.00 99.77  ? 477 LYS C CE  1 
ATOM   12312 N NZ  . LYS C 1 477 ? 71.460  8.074   -58.478 1.00 96.94  ? 477 LYS C NZ  1 
ATOM   12313 N N   . ILE C 1 478 ? 74.099  11.417  -62.721 1.00 91.84  ? 478 ILE C N   1 
ATOM   12314 C CA  . ILE C 1 478 ? 75.269  12.102  -62.209 1.00 90.26  ? 478 ILE C CA  1 
ATOM   12315 C C   . ILE C 1 478 ? 75.366  13.483  -62.859 1.00 89.56  ? 478 ILE C C   1 
ATOM   12316 O O   . ILE C 1 478 ? 75.528  13.574  -64.075 1.00 93.32  ? 478 ILE C O   1 
ATOM   12317 C CB  . ILE C 1 478 ? 76.525  11.276  -62.510 1.00 92.01  ? 478 ILE C CB  1 
ATOM   12318 C CG1 . ILE C 1 478 ? 76.398  9.793   -62.082 1.00 92.94  ? 478 ILE C CG1 1 
ATOM   12319 C CG2 . ILE C 1 478 ? 77.734  11.965  -61.889 1.00 91.26  ? 478 ILE C CG2 1 
ATOM   12320 C CD1 . ILE C 1 478 ? 76.379  9.552   -60.581 1.00 91.37  ? 478 ILE C CD1 1 
ATOM   12321 N N   . ILE C 1 479 ? 75.295  14.552  -62.053 1.00 84.82  ? 479 ILE C N   1 
ATOM   12322 C CA  . ILE C 1 479 ? 75.472  15.906  -62.562 1.00 83.03  ? 479 ILE C CA  1 
ATOM   12323 C C   . ILE C 1 479 ? 76.880  16.376  -62.196 1.00 81.04  ? 479 ILE C C   1 
ATOM   12324 O O   . ILE C 1 479 ? 77.223  16.336  -61.017 1.00 79.36  ? 479 ILE C O   1 
ATOM   12325 C CB  . ILE C 1 479 ? 74.383  16.856  -62.008 1.00 81.06  ? 479 ILE C CB  1 
ATOM   12326 C CG1 . ILE C 1 479 ? 72.994  16.364  -62.371 1.00 81.56  ? 479 ILE C CG1 1 
ATOM   12327 C CG2 . ILE C 1 479 ? 74.607  18.288  -62.488 1.00 80.69  ? 479 ILE C CG2 1 
ATOM   12328 C CD1 . ILE C 1 479 ? 71.848  17.132  -61.743 1.00 80.42  ? 479 ILE C CD1 1 
ATOM   12329 N N   . THR C 1 480 ? 77.662  16.852  -63.185 1.00 81.21  ? 480 THR C N   1 
ATOM   12330 C CA  . THR C 1 480 ? 79.081  17.159  -62.978 1.00 81.05  ? 480 THR C CA  1 
ATOM   12331 C C   . THR C 1 480 ? 79.387  18.600  -63.408 1.00 81.34  ? 480 THR C C   1 
ATOM   12332 O O   . THR C 1 480 ? 78.811  19.091  -64.383 1.00 82.51  ? 480 THR C O   1 
ATOM   12333 C CB  . THR C 1 480 ? 79.991  16.171  -63.719 1.00 82.16  ? 480 THR C CB  1 
ATOM   12334 O OG1 . THR C 1 480 ? 80.223  16.695  -65.023 1.00 83.50  ? 480 THR C OG1 1 
ATOM   12335 C CG2 . THR C 1 480 ? 79.410  14.773  -63.841 1.00 82.62  ? 480 THR C CG2 1 
ATOM   12336 N N   . SER C 1 481 ? 80.293  19.265  -62.661 1.00 80.46  ? 481 SER C N   1 
ATOM   12337 C CA  . SER C 1 481 ? 80.821  20.577  -63.021 1.00 81.13  ? 481 SER C CA  1 
ATOM   12338 C C   . SER C 1 481 ? 82.344  20.590  -62.863 1.00 82.12  ? 481 SER C C   1 
ATOM   12339 O O   . SER C 1 481 ? 82.893  19.735  -62.180 1.00 82.01  ? 481 SER C O   1 
ATOM   12340 C CB  . SER C 1 481 ? 80.172  21.687  -62.208 1.00 79.23  ? 481 SER C CB  1 
ATOM   12341 O OG  . SER C 1 481 ? 80.581  22.976  -62.659 1.00 79.15  ? 481 SER C OG  1 
ATOM   12342 N N   . GLU C 1 482 ? 83.015  21.553  -63.515 1.00 83.53  ? 482 GLU C N   1 
ATOM   12343 C CA  . GLU C 1 482 ? 84.446  21.796  -63.344 1.00 84.63  ? 482 GLU C CA  1 
ATOM   12344 C C   . GLU C 1 482 ? 84.680  23.314  -63.387 1.00 84.35  ? 482 GLU C C   1 
ATOM   12345 O O   . GLU C 1 482 ? 84.304  23.962  -64.357 1.00 85.15  ? 482 GLU C O   1 
ATOM   12346 C CB  . GLU C 1 482 ? 85.224  20.966  -64.380 1.00 87.40  ? 482 GLU C CB  1 
ATOM   12347 C CG  . GLU C 1 482 ? 86.747  21.154  -64.368 1.00 89.00  ? 482 GLU C CG  1 
ATOM   12348 C CD  . GLU C 1 482 ? 87.541  20.424  -65.450 1.00 91.82  ? 482 GLU C CD  1 
ATOM   12349 O OE1 . GLU C 1 482 ? 87.071  20.421  -66.607 1.00 93.00  ? 482 GLU C OE1 1 
ATOM   12350 O OE2 . GLU C 1 482 ? 88.640  19.869  -65.171 1.00 93.81  ? 482 GLU C OE2 1 
ATOM   12351 N N   . ASN C 1 483 ? 85.284  23.884  -62.330 1.00 83.27  ? 483 ASN C N   1 
ATOM   12352 C CA  . ASN C 1 483 ? 85.329  25.328  -62.133 1.00 83.24  ? 483 ASN C CA  1 
ATOM   12353 C C   . ASN C 1 483 ? 86.725  25.800  -61.726 1.00 83.32  ? 483 ASN C C   1 
ATOM   12354 O O   . ASN C 1 483 ? 87.202  25.450  -60.656 1.00 82.68  ? 483 ASN C O   1 
ATOM   12355 C CB  . ASN C 1 483 ? 84.371  25.746  -61.032 1.00 82.06  ? 483 ASN C CB  1 
ATOM   12356 C CG  . ASN C 1 483 ? 82.978  25.239  -61.291 1.00 82.46  ? 483 ASN C CG  1 
ATOM   12357 O OD1 . ASN C 1 483 ? 82.623  24.134  -60.848 1.00 83.99  ? 483 ASN C OD1 1 
ATOM   12358 N ND2 . ASN C 1 483 ? 82.205  26.005  -62.042 1.00 82.93  ? 483 ASN C ND2 1 
ATOM   12359 N N   . PHE C 1 484 ? 87.339  26.665  -62.542 1.00 84.13  ? 484 PHE C N   1 
ATOM   12360 C CA  . PHE C 1 484 ? 88.742  27.032  -62.389 1.00 84.57  ? 484 PHE C CA  1 
ATOM   12361 C C   . PHE C 1 484 ? 88.916  28.315  -61.570 1.00 83.43  ? 484 PHE C C   1 
ATOM   12362 O O   . PHE C 1 484 ? 88.147  29.261  -61.679 1.00 82.94  ? 484 PHE C O   1 
ATOM   12363 C CB  . PHE C 1 484 ? 89.340  27.185  -63.790 1.00 86.92  ? 484 PHE C CB  1 
ATOM   12364 C CG  . PHE C 1 484 ? 89.350  25.878  -64.567 1.00 87.84  ? 484 PHE C CG  1 
ATOM   12365 C CD1 . PHE C 1 484 ? 90.448  25.014  -64.488 1.00 88.69  ? 484 PHE C CD1 1 
ATOM   12366 C CD2 . PHE C 1 484 ? 88.251  25.499  -65.337 1.00 87.63  ? 484 PHE C CD2 1 
ATOM   12367 C CE1 . PHE C 1 484 ? 90.450  23.804  -65.170 1.00 89.43  ? 484 PHE C CE1 1 
ATOM   12368 C CE2 . PHE C 1 484 ? 88.261  24.298  -66.031 1.00 88.81  ? 484 PHE C CE2 1 
ATOM   12369 C CZ  . PHE C 1 484 ? 89.359  23.447  -65.942 1.00 89.69  ? 484 PHE C CZ  1 
ATOM   12370 N N   . PHE C 1 485 ? 89.968  28.355  -60.753 1.00 83.14  ? 485 PHE C N   1 
ATOM   12371 C CA  . PHE C 1 485 ? 90.281  29.534  -59.964 1.00 82.82  ? 485 PHE C CA  1 
ATOM   12372 C C   . PHE C 1 485 ? 91.797  29.741  -59.961 1.00 83.90  ? 485 PHE C C   1 
ATOM   12373 O O   . PHE C 1 485 ? 92.556  28.780  -59.862 1.00 84.14  ? 485 PHE C O   1 
ATOM   12374 C CB  . PHE C 1 485 ? 89.694  29.353  -58.560 1.00 80.93  ? 485 PHE C CB  1 
ATOM   12375 C CG  . PHE C 1 485 ? 88.254  28.870  -58.536 1.00 79.58  ? 485 PHE C CG  1 
ATOM   12376 C CD1 . PHE C 1 485 ? 87.204  29.764  -58.692 1.00 79.51  ? 485 PHE C CD1 1 
ATOM   12377 C CD2 . PHE C 1 485 ? 87.942  27.517  -58.375 1.00 79.07  ? 485 PHE C CD2 1 
ATOM   12378 C CE1 . PHE C 1 485 ? 85.880  29.321  -58.679 1.00 78.05  ? 485 PHE C CE1 1 
ATOM   12379 C CE2 . PHE C 1 485 ? 86.618  27.081  -58.353 1.00 77.57  ? 485 PHE C CE2 1 
ATOM   12380 C CZ  . PHE C 1 485 ? 85.596  27.988  -58.511 1.00 77.02  ? 485 PHE C CZ  1 
ATOM   12381 N N   . ASN C 1 486 ? 92.220  31.002  -60.085 1.00 84.74  ? 486 ASN C N   1 
ATOM   12382 C CA  . ASN C 1 486 ? 93.618  31.391  -59.963 1.00 86.12  ? 486 ASN C CA  1 
ATOM   12383 C C   . ASN C 1 486 ? 94.010  31.369  -58.487 1.00 85.40  ? 486 ASN C C   1 
ATOM   12384 O O   . ASN C 1 486 ? 93.254  31.830  -57.642 1.00 83.86  ? 486 ASN C O   1 
ATOM   12385 C CB  . ASN C 1 486 ? 93.866  32.762  -60.585 1.00 87.61  ? 486 ASN C CB  1 
ATOM   12386 C CG  . ASN C 1 486 ? 93.810  32.743  -62.098 1.00 89.06  ? 486 ASN C CG  1 
ATOM   12387 O OD1 . ASN C 1 486 ? 94.037  31.705  -62.726 1.00 89.35  ? 486 ASN C OD1 1 
ATOM   12388 N ND2 . ASN C 1 486 ? 93.560  33.887  -62.715 1.00 90.29  ? 486 ASN C ND2 1 
ATOM   12389 N N   . ILE C 1 487 ? 95.184  30.800  -58.174 1.00 86.85  ? 487 ILE C N   1 
ATOM   12390 C CA  . ILE C 1 487 ? 95.632  30.703  -56.792 1.00 86.56  ? 487 ILE C CA  1 
ATOM   12391 C C   . ILE C 1 487 ? 96.524  31.890  -56.464 1.00 89.03  ? 487 ILE C C   1 
ATOM   12392 O O   . ILE C 1 487 ? 97.581  32.070  -57.070 1.00 90.62  ? 487 ILE C O   1 
ATOM   12393 C CB  . ILE C 1 487 ? 96.374  29.401  -56.496 1.00 86.44  ? 487 ILE C CB  1 
ATOM   12394 C CG1 . ILE C 1 487 ? 95.604  28.181  -56.981 1.00 85.58  ? 487 ILE C CG1 1 
ATOM   12395 C CG2 . ILE C 1 487 ? 96.661  29.341  -54.999 1.00 85.69  ? 487 ILE C CG2 1 
ATOM   12396 C CD1 . ILE C 1 487 ? 96.399  26.886  -56.924 1.00 86.10  ? 487 ILE C CD1 1 
ATOM   12397 N N   . PRO C 1 488 ? 96.107  32.753  -55.511 1.00 89.79  ? 488 PRO C N   1 
ATOM   12398 C CA  . PRO C 1 488 ? 96.942  33.869  -55.085 1.00 91.59  ? 488 PRO C CA  1 
ATOM   12399 C C   . PRO C 1 488 ? 98.171  33.281  -54.408 1.00 92.88  ? 488 PRO C C   1 
ATOM   12400 O O   . PRO C 1 488 ? 98.037  32.418  -53.544 1.00 91.17  ? 488 PRO C O   1 
ATOM   12401 C CB  . PRO C 1 488 ? 96.050  34.698  -54.128 1.00 90.63  ? 488 PRO C CB  1 
ATOM   12402 C CG  . PRO C 1 488 ? 94.634  34.190  -54.361 1.00 88.36  ? 488 PRO C CG  1 
ATOM   12403 C CD  . PRO C 1 488 ? 94.792  32.748  -54.839 1.00 87.88  ? 488 PRO C CD  1 
ATOM   12404 N N   . ASP C 1 489 ? 99.343  33.782  -54.829 1.00 96.65  ? 489 ASP C N   1 
ATOM   12405 C CA  . ASP C 1 489 ? 100.650 33.379  -54.337 1.00 98.64  ? 489 ASP C CA  1 
ATOM   12406 C C   . ASP C 1 489 ? 100.754 33.564  -52.824 1.00 99.32  ? 489 ASP C C   1 
ATOM   12407 O O   . ASP C 1 489 ? 101.490 32.823  -52.172 1.00 100.43 ? 489 ASP C O   1 
ATOM   12408 C CB  . ASP C 1 489 ? 101.743 34.175  -55.027 1.00 101.36 ? 489 ASP C CB  1 
ATOM   12409 C CG  . ASP C 1 489 ? 101.839 34.002  -56.536 1.00 102.67 ? 489 ASP C CG  1 
ATOM   12410 O OD1 . ASP C 1 489 ? 101.156 33.113  -57.075 1.00 101.20 ? 489 ASP C OD1 1 
ATOM   12411 O OD2 . ASP C 1 489 ? 102.593 34.770  -57.159 1.00 105.94 ? 489 ASP C OD2 1 
ATOM   12412 N N   . ASN C 1 490 ? 100.031 34.556  -52.282 1.00 99.84  ? 490 ASN C N   1 
ATOM   12413 C CA  . ASN C 1 490 ? 99.952  34.790  -50.845 1.00 100.49 ? 490 ASN C CA  1 
ATOM   12414 C C   . ASN C 1 490 ? 98.809  33.993  -50.205 1.00 99.46  ? 490 ASN C C   1 
ATOM   12415 O O   . ASN C 1 490 ? 98.530  34.191  -49.020 1.00 99.77  ? 490 ASN C O   1 
ATOM   12416 C CB  . ASN C 1 490 ? 99.826  36.276  -50.493 1.00 101.93 ? 490 ASN C CB  1 
ATOM   12417 C CG  . ASN C 1 490 ? 98.573  36.951  -51.011 1.00 101.09 ? 490 ASN C CG  1 
ATOM   12418 O OD1 . ASN C 1 490 ? 98.023  36.581  -52.054 1.00 101.74 ? 490 ASN C OD1 1 
ATOM   12419 N ND2 . ASN C 1 490 ? 98.117  37.983  -50.322 1.00 101.24 ? 490 ASN C ND2 1 
ATOM   12420 N N   . CYS C 1 491 ? 98.138  33.111  -50.973 1.00 99.07  ? 491 CYS C N   1 
ATOM   12421 C CA  . CYS C 1 491 ? 97.175  32.178  -50.403 1.00 97.21  ? 491 CYS C CA  1 
ATOM   12422 C C   . CYS C 1 491 ? 97.925  31.093  -49.640 1.00 97.43  ? 491 CYS C C   1 
ATOM   12423 O O   . CYS C 1 491 ? 98.664  30.320  -50.239 1.00 99.79  ? 491 CYS C O   1 
ATOM   12424 C CB  . CYS C 1 491 ? 96.318  31.493  -51.458 1.00 96.85  ? 491 CYS C CB  1 
ATOM   12425 S SG  . CYS C 1 491 ? 95.152  30.300  -50.742 1.00 99.68  ? 491 CYS C SG  1 
ATOM   12426 N N   . TRP C 1 492 ? 97.755  31.057  -48.315 1.00 96.33  ? 492 TRP C N   1 
ATOM   12427 C CA  . TRP C 1 492 ? 98.449  30.093  -47.476 1.00 95.17  ? 492 TRP C CA  1 
ATOM   12428 C C   . TRP C 1 492 ? 97.590  28.848  -47.259 1.00 92.63  ? 492 TRP C C   1 
ATOM   12429 O O   . TRP C 1 492 ? 98.118  27.742  -47.117 1.00 93.41  ? 492 TRP C O   1 
ATOM   12430 C CB  . TRP C 1 492 ? 98.809  30.735  -46.132 1.00 96.16  ? 492 TRP C CB  1 
ATOM   12431 C CG  . TRP C 1 492 ? 99.729  31.929  -46.194 1.00 99.03  ? 492 TRP C CG  1 
ATOM   12432 C CD1 . TRP C 1 492 ? 99.745  32.946  -45.287 1.00 100.52 ? 492 TRP C CD1 1 
ATOM   12433 C CD2 . TRP C 1 492 ? 100.766 32.245  -47.158 1.00 101.08 ? 492 TRP C CD2 1 
ATOM   12434 N NE1 . TRP C 1 492 ? 100.728 33.852  -45.596 1.00 102.82 ? 492 TRP C NE1 1 
ATOM   12435 C CE2 . TRP C 1 492 ? 101.355 33.459  -46.744 1.00 102.20 ? 492 TRP C CE2 1 
ATOM   12436 C CE3 . TRP C 1 492 ? 101.251 31.641  -48.325 1.00 101.76 ? 492 TRP C CE3 1 
ATOM   12437 C CZ2 . TRP C 1 492 ? 102.375 34.072  -47.455 1.00 104.10 ? 492 TRP C CZ2 1 
ATOM   12438 C CZ3 . TRP C 1 492 ? 102.274 32.244  -49.023 1.00 102.99 ? 492 TRP C CZ3 1 
ATOM   12439 C CH2 . TRP C 1 492 ? 102.818 33.447  -48.595 1.00 104.67 ? 492 TRP C CH2 1 
ATOM   12440 N N   . VAL C 1 493 ? 96.268  29.056  -47.203 1.00 89.87  ? 493 VAL C N   1 
ATOM   12441 C CA  . VAL C 1 493 ? 95.303  27.995  -46.957 1.00 87.27  ? 493 VAL C CA  1 
ATOM   12442 C C   . VAL C 1 493 ? 93.977  28.398  -47.604 1.00 85.70  ? 493 VAL C C   1 
ATOM   12443 O O   . VAL C 1 493 ? 93.610  29.577  -47.563 1.00 84.11  ? 493 VAL C O   1 
ATOM   12444 C CB  . VAL C 1 493 ? 95.150  27.712  -45.447 1.00 86.48  ? 493 VAL C CB  1 
ATOM   12445 C CG1 . VAL C 1 493 ? 94.515  28.878  -44.697 1.00 85.88  ? 493 VAL C CG1 1 
ATOM   12446 C CG2 . VAL C 1 493 ? 94.379  26.421  -45.189 1.00 85.57  ? 493 VAL C CG2 1 
ATOM   12447 N N   . VAL C 1 494 ? 93.286  27.407  -48.208 1.00 85.08  ? 494 VAL C N   1 
ATOM   12448 C CA  . VAL C 1 494 ? 92.026  27.613  -48.931 1.00 83.98  ? 494 VAL C CA  1 
ATOM   12449 C C   . VAL C 1 494 ? 90.956  26.649  -48.423 1.00 81.23  ? 494 VAL C C   1 
ATOM   12450 O O   . VAL C 1 494 ? 91.232  25.530  -48.017 1.00 80.23  ? 494 VAL C O   1 
ATOM   12451 C CB  . VAL C 1 494 ? 92.142  27.475  -50.468 1.00 85.02  ? 494 VAL C CB  1 
ATOM   12452 C CG1 . VAL C 1 494 ? 92.594  26.088  -50.908 1.00 85.66  ? 494 VAL C CG1 1 
ATOM   12453 C CG2 . VAL C 1 494 ? 90.853  27.848  -51.197 1.00 83.62  ? 494 VAL C CG2 1 
ATOM   12454 N N   . ASN C 1 495 ? 89.707  27.100  -48.475 1.00 80.50  ? 495 ASN C N   1 
ATOM   12455 C CA  . ASN C 1 495 ? 88.575  26.236  -48.207 1.00 78.42  ? 495 ASN C CA  1 
ATOM   12456 C C   . ASN C 1 495 ? 87.820  26.074  -49.518 1.00 78.04  ? 495 ASN C C   1 
ATOM   12457 O O   . ASN C 1 495 ? 87.058  26.955  -49.908 1.00 79.50  ? 495 ASN C O   1 
ATOM   12458 C CB  . ASN C 1 495 ? 87.736  26.768  -47.049 1.00 77.42  ? 495 ASN C CB  1 
ATOM   12459 C CG  . ASN C 1 495 ? 86.790  25.714  -46.534 1.00 76.63  ? 495 ASN C CG  1 
ATOM   12460 O OD1 . ASN C 1 495 ? 86.233  24.970  -47.345 1.00 77.33  ? 495 ASN C OD1 1 
ATOM   12461 N ND2 . ASN C 1 495 ? 86.635  25.594  -45.221 1.00 75.95  ? 495 ASN C ND2 1 
ATOM   12462 N N   . ALA C 1 496 ? 88.075  24.960  -50.208 1.00 78.02  ? 496 ALA C N   1 
ATOM   12463 C CA  . ALA C 1 496 ? 87.388  24.644  -51.448 1.00 77.82  ? 496 ALA C CA  1 
ATOM   12464 C C   . ALA C 1 496 ? 86.140  23.840  -51.120 1.00 75.94  ? 496 ALA C C   1 
ATOM   12465 O O   . ALA C 1 496 ? 86.241  22.731  -50.619 1.00 75.33  ? 496 ALA C O   1 
ATOM   12466 C CB  . ALA C 1 496 ? 88.295  23.871  -52.361 1.00 79.73  ? 496 ALA C CB  1 
ATOM   12467 N N   . SER C 1 497 ? 84.981  24.444  -51.385 1.00 75.33  ? 497 SER C N   1 
ATOM   12468 C CA  . SER C 1 497 ? 83.693  23.872  -51.049 1.00 74.32  ? 497 SER C CA  1 
ATOM   12469 C C   . SER C 1 497 ? 82.709  24.065  -52.204 1.00 73.83  ? 497 SER C C   1 
ATOM   12470 O O   . SER C 1 497 ? 82.902  24.918  -53.068 1.00 73.24  ? 497 SER C O   1 
ATOM   12471 C CB  . SER C 1 497 ? 83.167  24.483  -49.779 1.00 74.16  ? 497 SER C CB  1 
ATOM   12472 O OG  . SER C 1 497 ? 83.026  25.886  -49.931 1.00 75.20  ? 497 SER C OG  1 
ATOM   12473 N N   . ALA C 1 498 ? 81.659  23.227  -52.204 1.00 73.71  ? 498 ALA C N   1 
ATOM   12474 C CA  . ALA C 1 498 ? 80.536  23.329  -53.127 1.00 73.05  ? 498 ALA C CA  1 
ATOM   12475 C C   . ALA C 1 498 ? 79.281  22.861  -52.419 1.00 71.62  ? 498 ALA C C   1 
ATOM   12476 O O   . ALA C 1 498 ? 79.362  22.186  -51.399 1.00 70.81  ? 498 ALA C O   1 
ATOM   12477 C CB  . ALA C 1 498 ? 80.765  22.507  -54.374 1.00 73.99  ? 498 ALA C CB  1 
ATOM   12478 N N   . GLY C 1 499 ? 78.125  23.228  -52.968 1.00 71.88  ? 499 GLY C N   1 
ATOM   12479 C CA  . GLY C 1 499 ? 76.875  22.961  -52.277 1.00 70.99  ? 499 GLY C CA  1 
ATOM   12480 C C   . GLY C 1 499 ? 75.653  23.350  -53.101 1.00 70.79  ? 499 GLY C C   1 
ATOM   12481 O O   . GLY C 1 499 ? 75.737  24.192  -54.003 1.00 71.04  ? 499 GLY C O   1 
ATOM   12482 N N   . ILE C 1 500 ? 74.536  22.679  -52.767 1.00 70.11  ? 500 ILE C N   1 
ATOM   12483 C CA  . ILE C 1 500 ? 73.236  22.888  -53.386 1.00 69.18  ? 500 ILE C CA  1 
ATOM   12484 C C   . ILE C 1 500 ? 72.151  22.493  -52.392 1.00 68.41  ? 500 ILE C C   1 
ATOM   12485 O O   . ILE C 1 500 ? 72.337  21.585  -51.574 1.00 67.63  ? 500 ILE C O   1 
ATOM   12486 C CB  . ILE C 1 500 ? 73.112  22.075  -54.684 1.00 69.45  ? 500 ILE C CB  1 
ATOM   12487 C CG1 . ILE C 1 500 ? 71.966  22.571  -55.537 1.00 69.31  ? 500 ILE C CG1 1 
ATOM   12488 C CG2 . ILE C 1 500 ? 73.012  20.573  -54.397 1.00 69.35  ? 500 ILE C CG2 1 
ATOM   12489 C CD1 . ILE C 1 500 ? 72.023  22.046  -56.959 1.00 70.58  ? 500 ILE C CD1 1 
ATOM   12490 N N   . SER C 1 501 ? 71.011  23.177  -52.530 1.00 68.63  ? 501 SER C N   1 
ATOM   12491 C CA  . SER C 1 501 ? 69.823  22.955  -51.722 1.00 68.65  ? 501 SER C CA  1 
ATOM   12492 C C   . SER C 1 501 ? 68.994  21.821  -52.317 1.00 68.31  ? 501 SER C C   1 
ATOM   12493 O O   . SER C 1 501 ? 68.899  21.701  -53.540 1.00 67.85  ? 501 SER C O   1 
ATOM   12494 C CB  . SER C 1 501 ? 69.014  24.225  -51.648 1.00 69.57  ? 501 SER C CB  1 
ATOM   12495 O OG  . SER C 1 501 ? 69.864  25.358  -51.527 1.00 70.69  ? 501 SER C OG  1 
ATOM   12496 N N   . VAL C 1 502 ? 68.373  21.030  -51.429 1.00 69.07  ? 502 VAL C N   1 
ATOM   12497 C CA  . VAL C 1 502 ? 67.657  19.800  -51.787 1.00 71.05  ? 502 VAL C CA  1 
ATOM   12498 C C   . VAL C 1 502 ? 66.296  19.838  -51.110 1.00 71.25  ? 502 VAL C C   1 
ATOM   12499 O O   . VAL C 1 502 ? 66.231  20.343  -49.996 1.00 72.07  ? 502 VAL C O   1 
ATOM   12500 C CB  . VAL C 1 502 ? 68.437  18.531  -51.363 1.00 71.33  ? 502 VAL C CB  1 
ATOM   12501 C CG1 . VAL C 1 502 ? 67.791  17.256  -51.870 1.00 72.87  ? 502 VAL C CG1 1 
ATOM   12502 C CG2 . VAL C 1 502 ? 69.870  18.555  -51.853 1.00 71.08  ? 502 VAL C CG2 1 
ATOM   12503 N N   . ARG C 1 503 ? 65.232  19.326  -51.762 1.00 72.92  ? 503 ARG C N   1 
ATOM   12504 C CA  . ARG C 1 503 ? 63.885  19.347  -51.173 1.00 73.03  ? 503 ARG C CA  1 
ATOM   12505 C C   . ARG C 1 503 ? 63.239  17.962  -51.233 1.00 72.66  ? 503 ARG C C   1 
ATOM   12506 O O   . ARG C 1 503 ? 63.079  17.383  -52.307 1.00 72.89  ? 503 ARG C O   1 
ATOM   12507 C CB  . ARG C 1 503 ? 62.886  20.317  -51.821 1.00 74.10  ? 503 ARG C CB  1 
ATOM   12508 C CG  . ARG C 1 503 ? 61.543  20.414  -51.106 1.00 76.69  ? 503 ARG C CG  1 
ATOM   12509 C CD  . ARG C 1 503 ? 60.319  20.567  -52.038 1.00 79.25  ? 503 ARG C CD  1 
ATOM   12510 N NE  . ARG C 1 503 ? 60.358  21.851  -52.735 1.00 82.99  ? 503 ARG C NE  1 
ATOM   12511 C CZ  . ARG C 1 503 ? 60.336  23.051  -52.131 1.00 88.40  ? 503 ARG C CZ  1 
ATOM   12512 N NH1 . ARG C 1 503 ? 60.103  23.140  -50.825 1.00 88.59  ? 503 ARG C NH1 1 
ATOM   12513 N NH2 . ARG C 1 503 ? 60.508  24.170  -52.837 1.00 90.08  ? 503 ARG C NH2 1 
ATOM   12514 N N   . TYR C 1 504 ? 62.842  17.464  -50.056 1.00 72.17  ? 504 TYR C N   1 
ATOM   12515 C CA  . TYR C 1 504 ? 61.949  16.325  -49.923 1.00 72.23  ? 504 TYR C CA  1 
ATOM   12516 C C   . TYR C 1 504 ? 60.719  16.772  -49.146 1.00 72.18  ? 504 TYR C C   1 
ATOM   12517 O O   . TYR C 1 504 ? 60.788  16.879  -47.923 1.00 72.41  ? 504 TYR C O   1 
ATOM   12518 C CB  . TYR C 1 504 ? 62.596  15.186  -49.133 1.00 72.94  ? 504 TYR C CB  1 
ATOM   12519 C CG  . TYR C 1 504 ? 61.751  13.924  -49.177 1.00 74.82  ? 504 TYR C CG  1 
ATOM   12520 C CD1 . TYR C 1 504 ? 60.705  13.741  -48.283 1.00 74.56  ? 504 TYR C CD1 1 
ATOM   12521 C CD2 . TYR C 1 504 ? 61.992  12.925  -50.125 1.00 75.98  ? 504 TYR C CD2 1 
ATOM   12522 C CE1 . TYR C 1 504 ? 59.924  12.604  -48.327 1.00 75.62  ? 504 TYR C CE1 1 
ATOM   12523 C CE2 . TYR C 1 504 ? 61.203  11.794  -50.186 1.00 76.77  ? 504 TYR C CE2 1 
ATOM   12524 C CZ  . TYR C 1 504 ? 60.161  11.642  -49.287 1.00 76.74  ? 504 TYR C CZ  1 
ATOM   12525 O OH  . TYR C 1 504 ? 59.347  10.552  -49.287 1.00 78.31  ? 504 TYR C OH  1 
ATOM   12526 N N   . GLY C 1 505 ? 59.614  17.056  -49.850 1.00 71.93  ? 505 GLY C N   1 
ATOM   12527 C CA  . GLY C 1 505 ? 58.394  17.485  -49.195 1.00 71.62  ? 505 GLY C CA  1 
ATOM   12528 C C   . GLY C 1 505 ? 58.545  18.910  -48.706 1.00 70.86  ? 505 GLY C C   1 
ATOM   12529 O O   . GLY C 1 505 ? 58.886  19.769  -49.515 1.00 71.19  ? 505 GLY C O   1 
ATOM   12530 N N   . LYS C 1 506 ? 58.314  19.128  -47.396 1.00 70.94  ? 506 LYS C N   1 
ATOM   12531 C CA  . LYS C 1 506 ? 58.472  20.433  -46.749 1.00 70.16  ? 506 LYS C CA  1 
ATOM   12532 C C   . LYS C 1 506 ? 59.893  20.613  -46.209 1.00 68.80  ? 506 LYS C C   1 
ATOM   12533 O O   . LYS C 1 506 ? 60.214  21.643  -45.641 1.00 67.44  ? 506 LYS C O   1 
ATOM   12534 C CB  . LYS C 1 506 ? 57.512  20.558  -45.562 1.00 71.30  ? 506 LYS C CB  1 
ATOM   12535 C CG  . LYS C 1 506 ? 56.000  20.610  -45.876 1.00 72.82  ? 506 LYS C CG  1 
ATOM   12536 C CD  . LYS C 1 506 ? 55.160  21.067  -44.679 1.00 73.75  ? 506 LYS C CD  1 
ATOM   12537 C CE  . LYS C 1 506 ? 53.703  20.760  -44.751 1.00 75.71  ? 506 LYS C CE  1 
ATOM   12538 N NZ  . LYS C 1 506 ? 53.026  20.714  -43.439 1.00 77.12  ? 506 LYS C NZ  1 
ATOM   12539 N N   . PHE C 1 507 ? 60.720  19.565  -46.364 1.00 69.21  ? 507 PHE C N   1 
ATOM   12540 C CA  . PHE C 1 507 ? 62.058  19.470  -45.798 1.00 68.16  ? 507 PHE C CA  1 
ATOM   12541 C C   . PHE C 1 507 ? 63.062  19.800  -46.891 1.00 67.30  ? 507 PHE C C   1 
ATOM   12542 O O   . PHE C 1 507 ? 63.007  19.263  -47.997 1.00 66.29  ? 507 PHE C O   1 
ATOM   12543 C CB  . PHE C 1 507 ? 62.275  18.077  -45.201 1.00 68.73  ? 507 PHE C CB  1 
ATOM   12544 C CG  . PHE C 1 507 ? 63.546  17.851  -44.384 1.00 68.41  ? 507 PHE C CG  1 
ATOM   12545 C CD1 . PHE C 1 507 ? 64.728  17.463  -44.999 1.00 67.71  ? 507 PHE C CD1 1 
ATOM   12546 C CD2 . PHE C 1 507 ? 63.526  17.930  -42.994 1.00 68.40  ? 507 PHE C CD2 1 
ATOM   12547 C CE1 . PHE C 1 507 ? 65.860  17.229  -44.249 1.00 67.41  ? 507 PHE C CE1 1 
ATOM   12548 C CE2 . PHE C 1 507 ? 64.660  17.692  -42.252 1.00 67.86  ? 507 PHE C CE2 1 
ATOM   12549 C CZ  . PHE C 1 507 ? 65.822  17.346  -42.881 1.00 67.69  ? 507 PHE C CZ  1 
ATOM   12550 N N   . THR C 1 508 ? 63.910  20.774  -46.556 1.00 67.53  ? 508 THR C N   1 
ATOM   12551 C CA  . THR C 1 508 ? 64.944  21.296  -47.430 1.00 67.01  ? 508 THR C CA  1 
ATOM   12552 C C   . THR C 1 508 ? 66.214  21.364  -46.608 1.00 65.80  ? 508 THR C C   1 
ATOM   12553 O O   . THR C 1 508 ? 66.174  21.678  -45.424 1.00 65.16  ? 508 THR C O   1 
ATOM   12554 C CB  . THR C 1 508 ? 64.587  22.691  -47.936 1.00 67.94  ? 508 THR C CB  1 
ATOM   12555 O OG1 . THR C 1 508 ? 64.546  23.461  -46.736 1.00 68.89  ? 508 THR C OG1 1 
ATOM   12556 C CG2 . THR C 1 508 ? 63.258  22.753  -48.671 1.00 68.14  ? 508 THR C CG2 1 
ATOM   12557 N N   . PHE C 1 509 ? 67.331  21.060  -47.260 1.00 65.77  ? 509 PHE C N   1 
ATOM   12558 C CA  . PHE C 1 509 ? 68.620  20.961  -46.598 1.00 65.34  ? 509 PHE C CA  1 
ATOM   12559 C C   . PHE C 1 509 ? 69.665  21.155  -47.686 1.00 65.62  ? 509 PHE C C   1 
ATOM   12560 O O   . PHE C 1 509 ? 69.318  21.406  -48.845 1.00 65.19  ? 509 PHE C O   1 
ATOM   12561 C CB  . PHE C 1 509 ? 68.691  19.641  -45.822 1.00 65.39  ? 509 PHE C CB  1 
ATOM   12562 C CG  . PHE C 1 509 ? 68.606  18.414  -46.712 1.00 65.29  ? 509 PHE C CG  1 
ATOM   12563 C CD1 . PHE C 1 509 ? 67.433  18.088  -47.362 1.00 65.80  ? 509 PHE C CD1 1 
ATOM   12564 C CD2 . PHE C 1 509 ? 69.697  17.608  -46.901 1.00 65.35  ? 509 PHE C CD2 1 
ATOM   12565 C CE1 . PHE C 1 509 ? 67.359  16.985  -48.179 1.00 66.63  ? 509 PHE C CE1 1 
ATOM   12566 C CE2 . PHE C 1 509 ? 69.626  16.521  -47.735 1.00 66.25  ? 509 PHE C CE2 1 
ATOM   12567 C CZ  . PHE C 1 509 ? 68.459  16.203  -48.364 1.00 66.81  ? 509 PHE C CZ  1 
ATOM   12568 N N   . LYS C 1 510 ? 70.935  21.081  -47.306 1.00 66.26  ? 510 LYS C N   1 
ATOM   12569 C CA  . LYS C 1 510 ? 71.965  21.248  -48.298 1.00 67.81  ? 510 LYS C CA  1 
ATOM   12570 C C   . LYS C 1 510 ? 72.857  20.025  -48.280 1.00 68.82  ? 510 LYS C C   1 
ATOM   12571 O O   . LYS C 1 510 ? 73.179  19.496  -47.221 1.00 69.89  ? 510 LYS C O   1 
ATOM   12572 C CB  . LYS C 1 510 ? 72.738  22.530  -47.998 1.00 69.24  ? 510 LYS C CB  1 
ATOM   12573 C CG  . LYS C 1 510 ? 71.966  23.768  -48.337 1.00 70.53  ? 510 LYS C CG  1 
ATOM   12574 C CD  . LYS C 1 510 ? 72.767  25.038  -48.134 1.00 72.22  ? 510 LYS C CD  1 
ATOM   12575 C CE  . LYS C 1 510 ? 73.709  25.258  -49.274 1.00 73.83  ? 510 LYS C CE  1 
ATOM   12576 N NZ  . LYS C 1 510 ? 73.084  25.915  -50.428 1.00 74.63  ? 510 LYS C NZ  1 
ATOM   12577 N N   . ILE C 1 511 ? 73.246  19.590  -49.474 1.00 69.47  ? 511 ILE C N   1 
ATOM   12578 C CA  . ILE C 1 511 ? 74.280  18.577  -49.618 1.00 69.56  ? 511 ILE C CA  1 
ATOM   12579 C C   . ILE C 1 511 ? 75.510  19.310  -50.134 1.00 69.77  ? 511 ILE C C   1 
ATOM   12580 O O   . ILE C 1 511 ? 75.372  20.367  -50.748 1.00 70.71  ? 511 ILE C O   1 
ATOM   12581 C CB  . ILE C 1 511 ? 73.808  17.435  -50.535 1.00 69.35  ? 511 ILE C CB  1 
ATOM   12582 C CG1 . ILE C 1 511 ? 73.390  17.942  -51.925 1.00 69.39  ? 511 ILE C CG1 1 
ATOM   12583 C CG2 . ILE C 1 511 ? 72.694  16.652  -49.846 1.00 68.78  ? 511 ILE C CG2 1 
ATOM   12584 C CD1 . ILE C 1 511 ? 72.984  16.854  -52.896 1.00 70.20  ? 511 ILE C CD1 1 
ATOM   12585 N N   . HIS C 1 512 ? 76.703  18.804  -49.827 1.00 69.49  ? 512 HIS C N   1 
ATOM   12586 C CA  . HIS C 1 512 ? 77.882  19.648  -49.916 1.00 69.35  ? 512 HIS C CA  1 
ATOM   12587 C C   . HIS C 1 512 ? 79.136  18.868  -49.521 1.00 71.00  ? 512 HIS C C   1 
ATOM   12588 O O   . HIS C 1 512 ? 79.074  17.686  -49.213 1.00 74.23  ? 512 HIS C O   1 
ATOM   12589 C CB  . HIS C 1 512 ? 77.677  20.887  -49.040 1.00 67.80  ? 512 HIS C CB  1 
ATOM   12590 C CG  . HIS C 1 512 ? 77.307  20.545  -47.637 1.00 66.90  ? 512 HIS C CG  1 
ATOM   12591 N ND1 . HIS C 1 512 ? 78.148  19.837  -46.795 1.00 66.56  ? 512 HIS C ND1 1 
ATOM   12592 C CD2 . HIS C 1 512 ? 76.176  20.785  -46.942 1.00 66.10  ? 512 HIS C CD2 1 
ATOM   12593 C CE1 . HIS C 1 512 ? 77.565  19.693  -45.611 1.00 66.38  ? 512 HIS C CE1 1 
ATOM   12594 N NE2 . HIS C 1 512 ? 76.367  20.264  -45.680 1.00 66.34  ? 512 HIS C NE2 1 
ATOM   12595 N N   . ASP C 1 513 ? 80.288  19.542  -49.557 1.00 71.60  ? 513 ASP C N   1 
ATOM   12596 C CA  . ASP C 1 513 ? 81.591  18.936  -49.398 1.00 71.74  ? 513 ASP C CA  1 
ATOM   12597 C C   . ASP C 1 513 ? 82.584  20.064  -49.141 1.00 72.38  ? 513 ASP C C   1 
ATOM   12598 O O   . ASP C 1 513 ? 82.276  21.219  -49.429 1.00 72.04  ? 513 ASP C O   1 
ATOM   12599 C CB  . ASP C 1 513 ? 81.981  18.195  -50.664 1.00 72.69  ? 513 ASP C CB  1 
ATOM   12600 C CG  . ASP C 1 513 ? 82.913  17.022  -50.422 1.00 73.97  ? 513 ASP C CG  1 
ATOM   12601 O OD1 . ASP C 1 513 ? 82.911  16.559  -49.279 1.00 74.73  ? 513 ASP C OD1 1 
ATOM   12602 O OD2 . ASP C 1 513 ? 83.644  16.617  -51.354 1.00 74.86  ? 513 ASP C OD2 1 
ATOM   12603 N N   . GLN C 1 514 ? 83.779  19.715  -48.637 1.00 73.35  ? 514 GLN C N   1 
ATOM   12604 C CA  . GLN C 1 514 ? 84.769  20.674  -48.162 1.00 73.41  ? 514 GLN C CA  1 
ATOM   12605 C C   . GLN C 1 514 ? 86.155  20.034  -48.158 1.00 75.37  ? 514 GLN C C   1 
ATOM   12606 O O   . GLN C 1 514 ? 86.372  18.993  -47.530 1.00 75.79  ? 514 GLN C O   1 
ATOM   12607 C CB  . GLN C 1 514 ? 84.409  21.045  -46.724 1.00 72.59  ? 514 GLN C CB  1 
ATOM   12608 C CG  . GLN C 1 514 ? 85.151  22.244  -46.147 1.00 72.51  ? 514 GLN C CG  1 
ATOM   12609 C CD  . GLN C 1 514 ? 84.763  22.548  -44.713 1.00 72.06  ? 514 GLN C CD  1 
ATOM   12610 O OE1 . GLN C 1 514 ? 83.887  23.377  -44.426 1.00 71.60  ? 514 GLN C OE1 1 
ATOM   12611 N NE2 . GLN C 1 514 ? 85.388  21.836  -43.787 1.00 72.24  ? 514 GLN C NE2 1 
ATOM   12612 N N   . LYS C 1 515 ? 87.104  20.671  -48.851 1.00 76.63  ? 515 LYS C N   1 
ATOM   12613 C CA  . LYS C 1 515 ? 88.517  20.346  -48.686 1.00 77.71  ? 515 LYS C CA  1 
ATOM   12614 C C   . LYS C 1 515 ? 89.230  21.599  -48.183 1.00 77.44  ? 515 LYS C C   1 
ATOM   12615 O O   . LYS C 1 515 ? 88.933  22.692  -48.673 1.00 77.18  ? 515 LYS C O   1 
ATOM   12616 C CB  . LYS C 1 515 ? 89.126  19.826  -49.991 1.00 78.71  ? 515 LYS C CB  1 
ATOM   12617 C CG  . LYS C 1 515 ? 88.331  18.699  -50.618 1.00 78.99  ? 515 LYS C CG  1 
ATOM   12618 C CD  . LYS C 1 515 ? 88.066  17.516  -49.694 1.00 79.43  ? 515 LYS C CD  1 
ATOM   12619 C CE  . LYS C 1 515 ? 87.689  16.262  -50.451 1.00 80.78  ? 515 LYS C CE  1 
ATOM   12620 N NZ  . LYS C 1 515 ? 86.926  15.298  -49.643 1.00 80.85  ? 515 LYS C NZ  1 
ATOM   12621 N N   . ILE C 1 516 ? 90.107  21.421  -47.178 1.00 77.40  ? 516 ILE C N   1 
ATOM   12622 C CA  . ILE C 1 516 ? 90.913  22.493  -46.604 1.00 77.97  ? 516 ILE C CA  1 
ATOM   12623 C C   . ILE C 1 516 ? 92.370  22.242  -46.973 1.00 79.24  ? 516 ILE C C   1 
ATOM   12624 O O   . ILE C 1 516 ? 92.968  21.344  -46.395 1.00 80.80  ? 516 ILE C O   1 
ATOM   12625 C CB  . ILE C 1 516 ? 90.764  22.550  -45.069 1.00 77.72  ? 516 ILE C CB  1 
ATOM   12626 C CG1 . ILE C 1 516 ? 89.342  22.868  -44.625 1.00 76.33  ? 516 ILE C CG1 1 
ATOM   12627 C CG2 . ILE C 1 516 ? 91.752  23.546  -44.458 1.00 78.99  ? 516 ILE C CG2 1 
ATOM   12628 C CD1 . ILE C 1 516 ? 89.185  23.015  -43.118 1.00 76.38  ? 516 ILE C CD1 1 
ATOM   12629 N N   . ILE C 1 517 ? 92.959  23.034  -47.880 1.00 79.62  ? 517 ILE C N   1 
ATOM   12630 C CA  . ILE C 1 517 ? 94.264  22.674  -48.431 1.00 81.38  ? 517 ILE C CA  1 
ATOM   12631 C C   . ILE C 1 517 ? 95.270  23.810  -48.240 1.00 81.55  ? 517 ILE C C   1 
ATOM   12632 O O   . ILE C 1 517 ? 94.991  24.955  -48.593 1.00 81.24  ? 517 ILE C O   1 
ATOM   12633 C CB  . ILE C 1 517 ? 94.144  22.290  -49.920 1.00 82.47  ? 517 ILE C CB  1 
ATOM   12634 C CG1 . ILE C 1 517 ? 92.884  21.463  -50.206 1.00 82.07  ? 517 ILE C CG1 1 
ATOM   12635 C CG2 . ILE C 1 517 ? 95.410  21.579  -50.403 1.00 83.68  ? 517 ILE C CG2 1 
ATOM   12636 C CD1 . ILE C 1 517 ? 92.437  21.492  -51.660 1.00 82.67  ? 517 ILE C CD1 1 
ATOM   12637 N N   . TYR C 1 518 ? 96.468  23.454  -47.755 1.00 81.72  ? 518 TYR C N   1 
ATOM   12638 C CA  . TYR C 1 518 ? 97.484  24.421  -47.366 1.00 82.43  ? 518 TYR C CA  1 
ATOM   12639 C C   . TYR C 1 518 ? 98.610  24.517  -48.407 1.00 83.88  ? 518 TYR C C   1 
ATOM   12640 O O   . TYR C 1 518 ? 98.815  23.621  -49.233 1.00 84.12  ? 518 TYR C O   1 
ATOM   12641 C CB  . TYR C 1 518 ? 98.099  24.000  -46.030 1.00 82.72  ? 518 TYR C CB  1 
ATOM   12642 C CG  . TYR C 1 518 ? 97.196  23.762  -44.826 1.00 81.49  ? 518 TYR C CG  1 
ATOM   12643 C CD1 . TYR C 1 518 ? 96.569  22.541  -44.618 1.00 80.76  ? 518 TYR C CD1 1 
ATOM   12644 C CD2 . TYR C 1 518 ? 97.037  24.732  -43.843 1.00 81.68  ? 518 TYR C CD2 1 
ATOM   12645 C CE1 . TYR C 1 518 ? 95.778  22.307  -43.500 1.00 79.98  ? 518 TYR C CE1 1 
ATOM   12646 C CE2 . TYR C 1 518 ? 96.257  24.509  -42.716 1.00 80.83  ? 518 TYR C CE2 1 
ATOM   12647 C CZ  . TYR C 1 518 ? 95.628  23.289  -42.534 1.00 79.88  ? 518 TYR C CZ  1 
ATOM   12648 O OH  . TYR C 1 518 ? 94.864  23.048  -41.420 1.00 78.82  ? 518 TYR C OH  1 
ATOM   12649 N N   . ARG C 1 519 ? 99.371  25.617  -48.347 1.00 84.58  ? 519 ARG C N   1 
ATOM   12650 C CA  . ARG C 1 519 ? 100.541 25.770  -49.188 1.00 86.25  ? 519 ARG C CA  1 
ATOM   12651 C C   . ARG C 1 519 ? 101.768 25.295  -48.412 1.00 87.61  ? 519 ARG C C   1 
ATOM   12652 O O   . ARG C 1 519 ? 102.121 25.870  -47.389 1.00 88.33  ? 519 ARG C O   1 
ATOM   12653 C CB  . ARG C 1 519 ? 100.728 27.226  -49.622 1.00 87.17  ? 519 ARG C CB  1 
ATOM   12654 C CG  . ARG C 1 519 ? 102.037 27.434  -50.377 1.00 89.14  ? 519 ARG C CG  1 
ATOM   12655 C CD  . ARG C 1 519 ? 102.226 28.872  -50.799 1.00 90.16  ? 519 ARG C CD  1 
ATOM   12656 N NE  . ARG C 1 519 ? 101.205 29.378  -51.726 1.00 89.48  ? 519 ARG C NE  1 
ATOM   12657 C CZ  . ARG C 1 519 ? 101.087 29.078  -53.021 1.00 89.81  ? 519 ARG C CZ  1 
ATOM   12658 N NH1 . ARG C 1 519 ? 101.889 28.186  -53.582 1.00 90.71  ? 519 ARG C NH1 1 
ATOM   12659 N NH2 . ARG C 1 519 ? 100.157 29.674  -53.752 1.00 89.19  ? 519 ARG C NH2 1 
ATOM   12660 N N   . GLY C 1 520 ? 102.427 24.246  -48.911 1.00 88.13  ? 520 GLY C N   1 
ATOM   12661 C CA  . GLY C 1 520 ? 103.504 23.617  -48.173 1.00 89.03  ? 520 GLY C CA  1 
ATOM   12662 C C   . GLY C 1 520 ? 103.099 23.368  -46.726 1.00 88.13  ? 520 GLY C C   1 
ATOM   12663 O O   . GLY C 1 520 ? 101.934 23.074  -46.447 1.00 86.41  ? 520 GLY C O   1 
ATOM   12664 N N   . ASP C 1 521 ? 104.055 23.574  -45.817 1.00 89.63  ? 521 ASP C N   1 
ATOM   12665 C CA  . ASP C 1 521 ? 104.030 22.929  -44.515 1.00 89.95  ? 521 ASP C CA  1 
ATOM   12666 C C   . ASP C 1 521 ? 103.898 23.934  -43.377 1.00 90.30  ? 521 ASP C C   1 
ATOM   12667 O O   . ASP C 1 521 ? 104.013 23.546  -42.216 1.00 90.43  ? 521 ASP C O   1 
ATOM   12668 C CB  . ASP C 1 521 ? 105.271 22.078  -44.297 1.00 92.09  ? 521 ASP C CB  1 
ATOM   12669 C CG  . ASP C 1 521 ? 106.585 22.817  -44.058 1.00 94.28  ? 521 ASP C CG  1 
ATOM   12670 O OD1 . ASP C 1 521 ? 106.660 24.050  -44.343 1.00 94.52  ? 521 ASP C OD1 1 
ATOM   12671 O OD2 . ASP C 1 521 ? 107.521 22.152  -43.551 1.00 95.72  ? 521 ASP C OD2 1 
ATOM   12672 N N   . TRP C 1 522 ? 103.592 25.194  -43.698 1.00 90.57  ? 522 TRP C N   1 
ATOM   12673 C CA  . TRP C 1 522 ? 103.587 26.232  -42.687 1.00 91.72  ? 522 TRP C CA  1 
ATOM   12674 C C   . TRP C 1 522 ? 102.640 25.870  -41.542 1.00 91.07  ? 522 TRP C C   1 
ATOM   12675 O O   . TRP C 1 522 ? 102.738 26.427  -40.453 1.00 92.07  ? 522 TRP C O   1 
ATOM   12676 C CB  . TRP C 1 522 ? 103.203 27.573  -43.322 1.00 91.98  ? 522 TRP C CB  1 
ATOM   12677 C CG  . TRP C 1 522 ? 101.729 27.719  -43.598 1.00 90.63  ? 522 TRP C CG  1 
ATOM   12678 C CD1 . TRP C 1 522 ? 101.028 27.334  -44.708 1.00 89.80  ? 522 TRP C CD1 1 
ATOM   12679 C CD2 . TRP C 1 522 ? 100.762 28.320  -42.716 1.00 90.14  ? 522 TRP C CD2 1 
ATOM   12680 N NE1 . TRP C 1 522 ? 99.696  27.631  -44.577 1.00 87.84  ? 522 TRP C NE1 1 
ATOM   12681 C CE2 . TRP C 1 522 ? 99.507  28.241  -43.364 1.00 88.27  ? 522 TRP C CE2 1 
ATOM   12682 C CE3 . TRP C 1 522 ? 100.833 28.903  -41.446 1.00 91.14  ? 522 TRP C CE3 1 
ATOM   12683 C CZ2 . TRP C 1 522 ? 98.348  28.747  -42.782 1.00 87.33  ? 522 TRP C CZ2 1 
ATOM   12684 C CZ3 . TRP C 1 522 ? 99.676  29.396  -40.872 1.00 89.95  ? 522 TRP C CZ3 1 
ATOM   12685 C CH2 . TRP C 1 522 ? 98.457  29.329  -41.537 1.00 87.90  ? 522 TRP C CH2 1 
ATOM   12686 N N   . ALA C 1 523 ? 101.702 24.951  -41.779 1.00 89.97  ? 523 ALA C N   1 
ATOM   12687 C CA  . ALA C 1 523 ? 100.685 24.685  -40.776 1.00 89.82  ? 523 ALA C CA  1 
ATOM   12688 C C   . ALA C 1 523 ? 100.922 23.341  -40.107 1.00 90.76  ? 523 ALA C C   1 
ATOM   12689 O O   . ALA C 1 523 ? 99.973  22.736  -39.620 1.00 90.08  ? 523 ALA C O   1 
ATOM   12690 C CB  . ALA C 1 523 ? 99.308  24.746  -41.399 1.00 88.07  ? 523 ALA C CB  1 
ATOM   12691 N N   . LYS C 1 524 ? 102.186 22.907  -40.058 1.00 93.02  ? 524 LYS C N   1 
ATOM   12692 C CA  . LYS C 1 524 ? 102.532 21.635  -39.449 1.00 94.04  ? 524 LYS C CA  1 
ATOM   12693 C C   . LYS C 1 524 ? 102.249 21.671  -37.948 1.00 95.28  ? 524 LYS C C   1 
ATOM   12694 O O   . LYS C 1 524 ? 102.109 20.619  -37.331 1.00 95.95  ? 524 LYS C O   1 
ATOM   12695 C CB  . LYS C 1 524 ? 104.008 21.297  -39.670 1.00 95.89  ? 524 LYS C CB  1 
ATOM   12696 C CG  . LYS C 1 524 ? 104.982 22.157  -38.882 1.00 97.93  ? 524 LYS C CG  1 
ATOM   12697 C CD  . LYS C 1 524 ? 106.429 22.056  -39.355 1.00 99.95  ? 524 LYS C CD  1 
ATOM   12698 C CE  . LYS C 1 524 ? 107.346 23.038  -38.716 1.00 101.49 ? 524 LYS C CE  1 
ATOM   12699 N NZ  . LYS C 1 524 ? 108.713 22.643  -39.047 1.00 103.96 ? 524 LYS C NZ  1 
ATOM   12700 N N   . GLU C 1 525 ? 102.193 22.879  -37.363 1.00 96.23  ? 525 GLU C N   1 
ATOM   12701 C CA  . GLU C 1 525 ? 101.858 23.039  -35.956 1.00 96.75  ? 525 GLU C CA  1 
ATOM   12702 C C   . GLU C 1 525 ? 100.389 23.418  -35.814 1.00 95.22  ? 525 GLU C C   1 
ATOM   12703 O O   . GLU C 1 525 ? 99.612  22.700  -35.183 1.00 94.50  ? 525 GLU C O   1 
ATOM   12704 C CB  . GLU C 1 525 ? 102.697 24.116  -35.263 1.00 98.66  ? 525 GLU C CB  1 
ATOM   12705 C CG  . GLU C 1 525 ? 104.124 23.685  -34.919 1.00 100.86 ? 525 GLU C CG  1 
ATOM   12706 C CD  . GLU C 1 525 ? 105.266 24.286  -35.727 1.00 101.88 ? 525 GLU C CD  1 
ATOM   12707 O OE1 . GLU C 1 525 ? 105.059 25.288  -36.444 1.00 101.02 ? 525 GLU C OE1 1 
ATOM   12708 O OE2 . GLU C 1 525 ? 106.386 23.731  -35.622 1.00 104.09 ? 525 GLU C OE2 1 
ATOM   12709 N N   . VAL C 1 526 ? 100.026 24.557  -36.411 1.00 95.24  ? 526 VAL C N   1 
ATOM   12710 C CA  . VAL C 1 526 ? 98.803  25.264  -36.047 1.00 94.78  ? 526 VAL C CA  1 
ATOM   12711 C C   . VAL C 1 526 ? 97.575  24.609  -36.687 1.00 92.86  ? 526 VAL C C   1 
ATOM   12712 O O   . VAL C 1 526 ? 96.470  24.743  -36.167 1.00 91.95  ? 526 VAL C O   1 
ATOM   12713 C CB  . VAL C 1 526 ? 98.905  26.764  -36.403 1.00 95.09  ? 526 VAL C CB  1 
ATOM   12714 C CG1 . VAL C 1 526 ? 99.059  26.996  -37.902 1.00 94.65  ? 526 VAL C CG1 1 
ATOM   12715 C CG2 . VAL C 1 526 ? 97.732  27.573  -35.861 1.00 94.36  ? 526 VAL C CG2 1 
ATOM   12716 N N   . GLY C 1 527 ? 97.766  23.912  -37.813 1.00 92.92  ? 527 GLY C N   1 
ATOM   12717 C CA  . GLY C 1 527 ? 96.665  23.289  -38.529 1.00 91.71  ? 527 GLY C CA  1 
ATOM   12718 C C   . GLY C 1 527 ? 96.151  22.042  -37.812 1.00 92.52  ? 527 GLY C C   1 
ATOM   12719 O O   . GLY C 1 527 ? 96.891  21.400  -37.063 1.00 93.02  ? 527 GLY C O   1 
ATOM   12720 N N   . ARG C 1 528 ? 94.875  21.707  -38.075 1.00 92.93  ? 528 ARG C N   1 
ATOM   12721 C CA  . ARG C 1 528 ? 94.223  20.542  -37.491 1.00 93.23  ? 528 ARG C CA  1 
ATOM   12722 C C   . ARG C 1 528 ? 94.914  19.261  -37.947 1.00 96.62  ? 528 ARG C C   1 
ATOM   12723 O O   . ARG C 1 528 ? 95.164  19.108  -39.135 1.00 96.56  ? 528 ARG C O   1 
ATOM   12724 C CB  . ARG C 1 528 ? 92.754  20.474  -37.918 1.00 90.05  ? 528 ARG C CB  1 
ATOM   12725 C CG  . ARG C 1 528 ? 92.012  19.287  -37.314 1.00 88.92  ? 528 ARG C CG  1 
ATOM   12726 C CD  . ARG C 1 528 ? 90.553  19.239  -37.725 1.00 86.17  ? 528 ARG C CD  1 
ATOM   12727 N NE  . ARG C 1 528 ? 89.809  20.424  -37.296 1.00 84.29  ? 528 ARG C NE  1 
ATOM   12728 C CZ  . ARG C 1 528 ? 89.492  21.434  -38.095 1.00 83.22  ? 528 ARG C CZ  1 
ATOM   12729 N NH1 . ARG C 1 528 ? 89.856  21.429  -39.365 1.00 82.56  ? 528 ARG C NH1 1 
ATOM   12730 N NH2 . ARG C 1 528 ? 88.834  22.476  -37.616 1.00 82.87  ? 528 ARG C NH2 1 
ATOM   12731 N N   . LYS C 1 529 ? 95.164  18.337  -37.005 1.00 101.99 ? 529 LYS C N   1 
ATOM   12732 C CA  . LYS C 1 529 ? 95.777  17.044  -37.293 1.00 106.97 ? 529 LYS C CA  1 
ATOM   12733 C C   . LYS C 1 529 ? 94.710  15.979  -37.600 1.00 113.13 ? 529 LYS C C   1 
ATOM   12734 O O   . LYS C 1 529 ? 93.506  16.250  -37.552 1.00 113.66 ? 529 LYS C O   1 
ATOM   12735 C CB  . LYS C 1 529 ? 96.610  16.589  -36.086 1.00 108.28 ? 529 LYS C CB  1 
ATOM   12736 C CG  . LYS C 1 529 ? 97.621  17.567  -35.501 1.00 108.93 ? 529 LYS C CG  1 
ATOM   12737 C CD  . LYS C 1 529 ? 98.959  17.655  -36.233 1.00 109.33 ? 529 LYS C CD  1 
ATOM   12738 C CE  . LYS C 1 529 ? 99.941  18.552  -35.544 1.00 109.99 ? 529 LYS C CE  1 
ATOM   12739 N NZ  . LYS C 1 529 ? 99.430  19.929  -35.467 1.00 110.61 ? 529 LYS C NZ  1 
ATOM   12740 N N   . LEU C 1 530 ? 95.191  14.757  -37.904 1.00 121.44 ? 530 LEU C N   1 
ATOM   12741 C CA  . LEU C 1 530 ? 94.412  13.569  -38.262 1.00 125.80 ? 530 LEU C CA  1 
ATOM   12742 C C   . LEU C 1 530 ? 93.840  13.717  -39.694 1.00 124.49 ? 530 LEU C C   1 
ATOM   12743 O O   . LEU C 1 530 ? 93.021  12.835  -40.078 1.00 126.76 ? 530 LEU C O   1 
ATOM   12744 C CB  . LEU C 1 530 ? 93.329  13.168  -37.249 1.00 129.30 ? 530 LEU C CB  1 
ATOM   12745 C CG  . LEU C 1 530 ? 93.797  12.370  -36.023 1.00 129.04 ? 530 LEU C CG  1 
ATOM   12746 C CD1 . LEU C 1 530 ? 94.386  13.304  -34.965 1.00 129.85 ? 530 LEU C CD1 1 
ATOM   12747 C CD2 . LEU C 1 530 ? 92.671  11.504  -35.449 1.00 124.32 ? 530 LEU C CD2 1 
ATOM   12748 N N   . SER D 1 3   ? 50.309  -23.911 -34.471 1.00 110.99 ? 3   SER D N   1 
ATOM   12749 C CA  . SER D 1 3   ? 50.720  -23.065 -33.321 1.00 108.50 ? 3   SER D CA  1 
ATOM   12750 C C   . SER D 1 3   ? 49.642  -23.127 -32.236 1.00 105.17 ? 3   SER D C   1 
ATOM   12751 O O   . SER D 1 3   ? 48.522  -22.689 -32.473 1.00 106.82 ? 3   SER D O   1 
ATOM   12752 C CB  . SER D 1 3   ? 50.966  -21.654 -33.803 1.00 109.98 ? 3   SER D CB  1 
ATOM   12753 O OG  . SER D 1 3   ? 51.341  -20.788 -32.742 1.00 109.56 ? 3   SER D OG  1 
ATOM   12754 N N   . LYS D 1 4   ? 49.971  -23.699 -31.066 1.00 101.35 ? 4   LYS D N   1 
ATOM   12755 C CA  . LYS D 1 4   ? 49.082  -23.707 -29.910 1.00 97.04  ? 4   LYS D CA  1 
ATOM   12756 C C   . LYS D 1 4   ? 49.877  -23.468 -28.626 1.00 93.80  ? 4   LYS D C   1 
ATOM   12757 O O   . LYS D 1 4   ? 51.048  -23.822 -28.552 1.00 96.10  ? 4   LYS D O   1 
ATOM   12758 C CB  . LYS D 1 4   ? 48.316  -25.031 -29.839 1.00 97.81  ? 4   LYS D CB  1 
ATOM   12759 C CG  . LYS D 1 4   ? 49.131  -26.302 -29.655 1.00 98.79  ? 4   LYS D CG  1 
ATOM   12760 C CD  . LYS D 1 4   ? 48.228  -27.533 -29.542 1.00 100.38 ? 4   LYS D CD  1 
ATOM   12761 C CE  . LYS D 1 4   ? 48.949  -28.850 -29.556 1.00 101.63 ? 4   LYS D CE  1 
ATOM   12762 N NZ  . LYS D 1 4   ? 50.072  -28.841 -28.611 1.00 102.06 ? 4   LYS D NZ  1 
ATOM   12763 N N   . THR D 1 5   ? 49.223  -22.906 -27.601 1.00 89.62  ? 5   THR D N   1 
ATOM   12764 C CA  . THR D 1 5   ? 49.907  -22.313 -26.458 1.00 88.11  ? 5   THR D CA  1 
ATOM   12765 C C   . THR D 1 5   ? 50.904  -23.281 -25.840 1.00 86.46  ? 5   THR D C   1 
ATOM   12766 O O   . THR D 1 5   ? 50.521  -24.357 -25.414 1.00 84.30  ? 5   THR D O   1 
ATOM   12767 C CB  . THR D 1 5   ? 48.928  -21.910 -25.357 1.00 88.16  ? 5   THR D CB  1 
ATOM   12768 O OG1 . THR D 1 5   ? 47.893  -21.086 -25.885 1.00 92.59  ? 5   THR D OG1 1 
ATOM   12769 C CG2 . THR D 1 5   ? 49.637  -21.173 -24.234 1.00 87.04  ? 5   THR D CG2 1 
ATOM   12770 N N   . LYS D 1 6   ? 52.160  -22.842 -25.709 1.00 87.58  ? 6   LYS D N   1 
ATOM   12771 C CA  . LYS D 1 6   ? 53.133  -23.527 -24.876 1.00 87.30  ? 6   LYS D CA  1 
ATOM   12772 C C   . LYS D 1 6   ? 53.030  -22.996 -23.451 1.00 83.78  ? 6   LYS D C   1 
ATOM   12773 O O   . LYS D 1 6   ? 53.120  -21.791 -23.232 1.00 83.83  ? 6   LYS D O   1 
ATOM   12774 C CB  . LYS D 1 6   ? 54.541  -23.305 -25.425 1.00 91.28  ? 6   LYS D CB  1 
ATOM   12775 C CG  . LYS D 1 6   ? 55.598  -24.209 -24.801 1.00 96.12  ? 6   LYS D CG  1 
ATOM   12776 C CD  . LYS D 1 6   ? 57.004  -23.986 -25.365 1.00 102.87 ? 6   LYS D CD  1 
ATOM   12777 C CE  . LYS D 1 6   ? 58.073  -24.931 -24.863 1.00 106.65 ? 6   LYS D CE  1 
ATOM   12778 N NZ  . LYS D 1 6   ? 58.179  -24.915 -23.399 1.00 107.79 ? 6   LYS D NZ  1 
ATOM   12779 N N   . ILE D 1 7   ? 52.822  -23.895 -22.489 1.00 81.46  ? 7   ILE D N   1 
ATOM   12780 C CA  . ILE D 1 7   ? 52.717  -23.505 -21.096 1.00 79.69  ? 7   ILE D CA  1 
ATOM   12781 C C   . ILE D 1 7   ? 53.897  -24.088 -20.355 1.00 80.76  ? 7   ILE D C   1 
ATOM   12782 O O   . ILE D 1 7   ? 54.199  -25.249 -20.542 1.00 82.20  ? 7   ILE D O   1 
ATOM   12783 C CB  . ILE D 1 7   ? 51.417  -24.004 -20.455 1.00 77.93  ? 7   ILE D CB  1 
ATOM   12784 C CG1 . ILE D 1 7   ? 50.192  -23.344 -21.084 1.00 76.45  ? 7   ILE D CG1 1 
ATOM   12785 C CG2 . ILE D 1 7   ? 51.475  -23.788 -18.940 1.00 76.76  ? 7   ILE D CG2 1 
ATOM   12786 C CD1 . ILE D 1 7   ? 48.865  -23.843 -20.535 1.00 75.03  ? 7   ILE D CD1 1 
ATOM   12787 N N   . GLU D 1 8   ? 54.511  -23.305 -19.475 1.00 81.70  ? 8   GLU D N   1 
ATOM   12788 C CA  . GLU D 1 8   ? 55.793  -23.700 -18.926 1.00 84.07  ? 8   GLU D CA  1 
ATOM   12789 C C   . GLU D 1 8   ? 55.902  -23.167 -17.504 1.00 83.90  ? 8   GLU D C   1 
ATOM   12790 O O   . GLU D 1 8   ? 55.794  -21.960 -17.283 1.00 82.07  ? 8   GLU D O   1 
ATOM   12791 C CB  . GLU D 1 8   ? 56.872  -23.190 -19.883 1.00 86.62  ? 8   GLU D CB  1 
ATOM   12792 C CG  . GLU D 1 8   ? 58.259  -23.796 -19.684 1.00 88.97  ? 8   GLU D CG  1 
ATOM   12793 C CD  . GLU D 1 8   ? 59.283  -23.189 -20.636 1.00 93.03  ? 8   GLU D CD  1 
ATOM   12794 O OE1 . GLU D 1 8   ? 58.839  -22.347 -21.467 1.00 93.24  ? 8   GLU D OE1 1 
ATOM   12795 O OE2 . GLU D 1 8   ? 60.501  -23.527 -20.558 1.00 93.14  ? 8   GLU D OE2 1 
ATOM   12796 N N   . LEU D 1 9   ? 56.140  -24.094 -16.566 1.00 85.66  ? 9   LEU D N   1 
ATOM   12797 C CA  . LEU D 1 9   ? 56.268  -23.782 -15.151 1.00 86.86  ? 9   LEU D CA  1 
ATOM   12798 C C   . LEU D 1 9   ? 57.742  -23.730 -14.743 1.00 87.45  ? 9   LEU D C   1 
ATOM   12799 O O   . LEU D 1 9   ? 58.432  -24.748 -14.837 1.00 88.00  ? 9   LEU D O   1 
ATOM   12800 C CB  . LEU D 1 9   ? 55.506  -24.877 -14.403 1.00 87.46  ? 9   LEU D CB  1 
ATOM   12801 C CG  . LEU D 1 9   ? 53.977  -24.760 -14.404 1.00 88.27  ? 9   LEU D CG  1 
ATOM   12802 C CD1 . LEU D 1 9   ? 53.369  -24.462 -15.766 1.00 89.99  ? 9   LEU D CD1 1 
ATOM   12803 C CD2 . LEU D 1 9   ? 53.400  -26.046 -13.834 1.00 88.73  ? 9   LEU D CD2 1 
ATOM   12804 N N   . LYS D 1 10  ? 58.210  -22.547 -14.303 1.00 87.84  ? 10  LYS D N   1 
ATOM   12805 C CA  . LYS D 1 10  ? 59.590  -22.368 -13.857 1.00 90.08  ? 10  LYS D CA  1 
ATOM   12806 C C   . LYS D 1 10  ? 59.734  -21.084 -13.045 1.00 84.89  ? 10  LYS D C   1 
ATOM   12807 O O   . LYS D 1 10  ? 59.149  -20.067 -13.385 1.00 86.58  ? 10  LYS D O   1 
ATOM   12808 C CB  . LYS D 1 10  ? 60.626  -22.409 -14.991 1.00 96.94  ? 10  LYS D CB  1 
ATOM   12809 C CG  . LYS D 1 10  ? 60.598  -21.344 -16.090 1.00 102.86 ? 10  LYS D CG  1 
ATOM   12810 C CD  . LYS D 1 10  ? 61.701  -21.572 -17.132 1.00 110.66 ? 10  LYS D CD  1 
ATOM   12811 C CE  . LYS D 1 10  ? 61.959  -20.425 -18.073 1.00 114.17 ? 10  LYS D CE  1 
ATOM   12812 N NZ  . LYS D 1 10  ? 60.792  -20.127 -18.913 1.00 116.20 ? 10  LYS D NZ  1 
ATOM   12813 N N   . ASP D 1 11  ? 60.498  -21.157 -11.954 1.00 81.79  ? 11  ASP D N   1 
ATOM   12814 C CA  . ASP D 1 11  ? 60.592  -20.084 -10.978 1.00 80.21  ? 11  ASP D CA  1 
ATOM   12815 C C   . ASP D 1 11  ? 59.190  -19.835 -10.406 1.00 77.38  ? 11  ASP D C   1 
ATOM   12816 O O   . ASP D 1 11  ? 58.812  -18.702 -10.110 1.00 77.67  ? 11  ASP D O   1 
ATOM   12817 C CB  . ASP D 1 11  ? 61.348  -18.895 -11.567 1.00 82.00  ? 11  ASP D CB  1 
ATOM   12818 C CG  . ASP D 1 11  ? 62.673  -19.233 -12.248 1.00 85.41  ? 11  ASP D CG  1 
ATOM   12819 O OD1 . ASP D 1 11  ? 63.547  -19.833 -11.589 1.00 85.13  ? 11  ASP D OD1 1 
ATOM   12820 O OD2 . ASP D 1 11  ? 62.827  -18.931 -13.451 1.00 88.30  ? 11  ASP D OD2 1 
ATOM   12821 N N   . ASN D 1 12  ? 58.405  -20.917 -10.310 1.00 75.30  ? 12  ASN D N   1 
ATOM   12822 C CA  . ASN D 1 12  ? 57.106  -20.951 -9.646  1.00 72.10  ? 12  ASN D CA  1 
ATOM   12823 C C   . ASN D 1 12  ? 56.086  -19.988 -10.263 1.00 70.20  ? 12  ASN D C   1 
ATOM   12824 O O   . ASN D 1 12  ? 55.149  -19.513 -9.594  1.00 67.27  ? 12  ASN D O   1 
ATOM   12825 C CB  . ASN D 1 12  ? 57.289  -20.688 -8.167  1.00 71.25  ? 12  ASN D CB  1 
ATOM   12826 C CG  . ASN D 1 12  ? 58.240  -21.643 -7.503  1.00 72.15  ? 12  ASN D CG  1 
ATOM   12827 O OD1 . ASN D 1 12  ? 58.404  -22.827 -7.886  1.00 72.76  ? 12  ASN D OD1 1 
ATOM   12828 N ND2 . ASN D 1 12  ? 58.828  -21.107 -6.448  1.00 71.82  ? 12  ASN D ND2 1 
ATOM   12829 N N   . TRP D 1 13  ? 56.284  -19.748 -11.558 1.00 70.72  ? 13  TRP D N   1 
ATOM   12830 C CA  . TRP D 1 13  ? 55.434  -18.902 -12.369 1.00 70.59  ? 13  TRP D CA  1 
ATOM   12831 C C   . TRP D 1 13  ? 54.954  -19.724 -13.560 1.00 69.88  ? 13  TRP D C   1 
ATOM   12832 O O   . TRP D 1 13  ? 55.694  -20.537 -14.110 1.00 71.18  ? 13  TRP D O   1 
ATOM   12833 C CB  . TRP D 1 13  ? 56.212  -17.667 -12.849 1.00 73.03  ? 13  TRP D CB  1 
ATOM   12834 C CG  . TRP D 1 13  ? 56.215  -16.479 -11.923 1.00 72.88  ? 13  TRP D CG  1 
ATOM   12835 C CD1 . TRP D 1 13  ? 57.054  -16.196 -10.880 1.00 74.12  ? 13  TRP D CD1 1 
ATOM   12836 C CD2 . TRP D 1 13  ? 55.316  -15.363 -12.015 1.00 71.65  ? 13  TRP D CD2 1 
ATOM   12837 N NE1 . TRP D 1 13  ? 56.726  -14.993 -10.302 1.00 72.77  ? 13  TRP D NE1 1 
ATOM   12838 C CE2 . TRP D 1 13  ? 55.666  -14.463 -10.982 1.00 71.35  ? 13  TRP D CE2 1 
ATOM   12839 C CE3 . TRP D 1 13  ? 54.254  -15.052 -12.867 1.00 71.22  ? 13  TRP D CE3 1 
ATOM   12840 C CZ2 . TRP D 1 13  ? 54.972  -13.279 -10.774 1.00 70.72  ? 13  TRP D CZ2 1 
ATOM   12841 C CZ3 . TRP D 1 13  ? 53.552  -13.891 -12.642 1.00 70.32  ? 13  TRP D CZ3 1 
ATOM   12842 C CH2 . TRP D 1 13  ? 53.908  -13.021 -11.608 1.00 70.40  ? 13  TRP D CH2 1 
ATOM   12843 N N   . TYR D 1 14  ? 53.694  -19.521 -13.930 1.00 68.15  ? 14  TYR D N   1 
ATOM   12844 C CA  . TYR D 1 14  ? 53.191  -19.975 -15.211 1.00 67.44  ? 14  TYR D CA  1 
ATOM   12845 C C   . TYR D 1 14  ? 53.833  -19.082 -16.262 1.00 68.54  ? 14  TYR D C   1 
ATOM   12846 O O   . TYR D 1 14  ? 54.147  -17.935 -15.990 1.00 67.40  ? 14  TYR D O   1 
ATOM   12847 C CB  . TYR D 1 14  ? 51.665  -19.858 -15.323 1.00 65.03  ? 14  TYR D CB  1 
ATOM   12848 C CG  . TYR D 1 14  ? 50.806  -20.875 -14.595 1.00 62.81  ? 14  TYR D CG  1 
ATOM   12849 C CD1 . TYR D 1 14  ? 50.714  -20.898 -13.211 1.00 61.17  ? 14  TYR D CD1 1 
ATOM   12850 C CD2 . TYR D 1 14  ? 50.026  -21.770 -15.312 1.00 62.61  ? 14  TYR D CD2 1 
ATOM   12851 C CE1 . TYR D 1 14  ? 49.890  -21.807 -12.565 1.00 60.23  ? 14  TYR D CE1 1 
ATOM   12852 C CE2 . TYR D 1 14  ? 49.187  -22.673 -14.680 1.00 61.51  ? 14  TYR D CE2 1 
ATOM   12853 C CZ  . TYR D 1 14  ? 49.122  -22.697 -13.301 1.00 60.40  ? 14  TYR D CZ  1 
ATOM   12854 O OH  . TYR D 1 14  ? 48.286  -23.609 -12.707 1.00 59.69  ? 14  TYR D OH  1 
ATOM   12855 N N   . HIS D 1 15  ? 53.982  -19.629 -17.460 1.00 70.85  ? 15  HIS D N   1 
ATOM   12856 C CA  . HIS D 1 15  ? 54.433  -18.890 -18.620 1.00 73.54  ? 15  HIS D CA  1 
ATOM   12857 C C   . HIS D 1 15  ? 53.562  -19.339 -19.780 1.00 73.99  ? 15  HIS D C   1 
ATOM   12858 O O   . HIS D 1 15  ? 53.431  -20.537 -20.024 1.00 74.96  ? 15  HIS D O   1 
ATOM   12859 C CB  . HIS D 1 15  ? 55.870  -19.262 -19.014 1.00 76.43  ? 15  HIS D CB  1 
ATOM   12860 C CG  . HIS D 1 15  ? 56.921  -18.920 -18.006 1.00 77.94  ? 15  HIS D CG  1 
ATOM   12861 N ND1 . HIS D 1 15  ? 56.925  -19.429 -16.723 1.00 77.69  ? 15  HIS D ND1 1 
ATOM   12862 C CD2 . HIS D 1 15  ? 58.000  -18.115 -18.091 1.00 79.34  ? 15  HIS D CD2 1 
ATOM   12863 C CE1 . HIS D 1 15  ? 57.969  -18.934 -16.062 1.00 78.02  ? 15  HIS D CE1 1 
ATOM   12864 N NE2 . HIS D 1 15  ? 58.642  -18.148 -16.877 1.00 79.05  ? 15  HIS D NE2 1 
ATOM   12865 N N   . LEU D 1 16  ? 52.981  -18.379 -20.495 1.00 73.79  ? 16  LEU D N   1 
ATOM   12866 C CA  . LEU D 1 16  ? 52.292  -18.685 -21.736 1.00 74.04  ? 16  LEU D CA  1 
ATOM   12867 C C   . LEU D 1 16  ? 53.137  -18.142 -22.876 1.00 75.89  ? 16  LEU D C   1 
ATOM   12868 O O   . LEU D 1 16  ? 53.473  -16.971 -22.886 1.00 75.52  ? 16  LEU D O   1 
ATOM   12869 C CB  . LEU D 1 16  ? 50.884  -18.099 -21.743 1.00 72.18  ? 16  LEU D CB  1 
ATOM   12870 C CG  . LEU D 1 16  ? 49.828  -18.909 -20.995 1.00 70.11  ? 16  LEU D CG  1 
ATOM   12871 C CD1 . LEU D 1 16  ? 50.238  -19.300 -19.588 1.00 68.67  ? 16  LEU D CD1 1 
ATOM   12872 C CD2 . LEU D 1 16  ? 48.561  -18.070 -20.979 1.00 69.51  ? 16  LEU D CD2 1 
ATOM   12873 N N   . ASP D 1 17  ? 53.530  -19.021 -23.792 1.00 77.87  ? 17  ASP D N   1 
ATOM   12874 C CA  . ASP D 1 17  ? 54.395  -18.609 -24.878 1.00 80.82  ? 17  ASP D CA  1 
ATOM   12875 C C   . ASP D 1 17  ? 55.559  -17.769 -24.337 1.00 82.02  ? 17  ASP D C   1 
ATOM   12876 O O   . ASP D 1 17  ? 55.925  -16.744 -24.907 1.00 82.29  ? 17  ASP D O   1 
ATOM   12877 C CB  . ASP D 1 17  ? 53.564  -17.961 -25.970 1.00 81.06  ? 17  ASP D CB  1 
ATOM   12878 C CG  . ASP D 1 17  ? 52.563  -18.892 -26.631 1.00 81.12  ? 17  ASP D CG  1 
ATOM   12879 O OD1 . ASP D 1 17  ? 52.965  -19.960 -27.118 1.00 80.98  ? 17  ASP D OD1 1 
ATOM   12880 O OD2 . ASP D 1 17  ? 51.379  -18.536 -26.648 1.00 81.87  ? 17  ASP D OD2 1 
ATOM   12881 N N   . GLY D 1 18  ? 56.142  -18.236 -23.229 1.00 82.90  ? 18  GLY D N   1 
ATOM   12882 C CA  . GLY D 1 18  ? 57.455  -17.796 -22.798 1.00 84.86  ? 18  GLY D CA  1 
ATOM   12883 C C   . GLY D 1 18  ? 57.389  -16.486 -22.024 1.00 85.27  ? 18  GLY D C   1 
ATOM   12884 O O   . GLY D 1 18  ? 58.442  -15.883 -21.785 1.00 87.70  ? 18  GLY D O   1 
ATOM   12885 N N   . GLU D 1 19  ? 56.164  -16.065 -21.658 1.00 82.92  ? 19  GLU D N   1 
ATOM   12886 C CA  . GLU D 1 19  ? 55.932  -14.802 -20.967 1.00 81.79  ? 19  GLU D CA  1 
ATOM   12887 C C   . GLU D 1 19  ? 55.239  -15.111 -19.651 1.00 79.23  ? 19  GLU D C   1 
ATOM   12888 O O   . GLU D 1 19  ? 54.204  -15.773 -19.649 1.00 80.70  ? 19  GLU D O   1 
ATOM   12889 C CB  . GLU D 1 19  ? 55.006  -13.850 -21.724 1.00 82.42  ? 19  GLU D CB  1 
ATOM   12890 C CG  . GLU D 1 19  ? 55.469  -13.528 -23.139 1.00 86.01  ? 19  GLU D CG  1 
ATOM   12891 C CD  . GLU D 1 19  ? 56.765  -12.753 -23.179 1.00 90.42  ? 19  GLU D CD  1 
ATOM   12892 O OE1 . GLU D 1 19  ? 57.113  -12.101 -22.164 1.00 90.91  ? 19  GLU D OE1 1 
ATOM   12893 O OE2 . GLU D 1 19  ? 57.450  -12.842 -24.224 1.00 95.42  ? 19  GLU D OE2 1 
ATOM   12894 N N   . LYS D 1 20  ? 55.818  -14.648 -18.545 1.00 77.46  ? 20  LYS D N   1 
ATOM   12895 C CA  . LYS D 1 20  ? 55.232  -14.871 -17.236 1.00 76.19  ? 20  LYS D CA  1 
ATOM   12896 C C   . LYS D 1 20  ? 53.812  -14.303 -17.198 1.00 75.34  ? 20  LYS D C   1 
ATOM   12897 O O   . LYS D 1 20  ? 53.604  -13.157 -17.592 1.00 78.42  ? 20  LYS D O   1 
ATOM   12898 C CB  . LYS D 1 20  ? 56.058  -14.198 -16.139 1.00 76.04  ? 20  LYS D CB  1 
ATOM   12899 C CG  . LYS D 1 20  ? 57.308  -14.916 -15.679 1.00 76.64  ? 20  LYS D CG  1 
ATOM   12900 C CD  . LYS D 1 20  ? 57.846  -14.213 -14.437 1.00 76.01  ? 20  LYS D CD  1 
ATOM   12901 C CE  . LYS D 1 20  ? 59.028  -14.862 -13.806 1.00 76.28  ? 20  LYS D CE  1 
ATOM   12902 N NZ  . LYS D 1 20  ? 60.135  -14.848 -14.760 1.00 78.28  ? 20  LYS D NZ  1 
ATOM   12903 N N   . TYR D 1 21  ? 52.853  -15.103 -16.707 1.00 72.94  ? 21  TYR D N   1 
ATOM   12904 C CA  . TYR D 1 21  ? 51.435  -14.790 -16.812 1.00 71.00  ? 21  TYR D CA  1 
ATOM   12905 C C   . TYR D 1 21  ? 50.790  -15.018 -15.448 1.00 69.59  ? 21  TYR D C   1 
ATOM   12906 O O   . TYR D 1 21  ? 50.777  -16.142 -14.935 1.00 68.50  ? 21  TYR D O   1 
ATOM   12907 C CB  . TYR D 1 21  ? 50.823  -15.667 -17.912 1.00 70.68  ? 21  TYR D CB  1 
ATOM   12908 C CG  . TYR D 1 21  ? 49.376  -15.413 -18.335 1.00 69.42  ? 21  TYR D CG  1 
ATOM   12909 C CD1 . TYR D 1 21  ? 48.302  -15.979 -17.650 1.00 67.87  ? 21  TYR D CD1 1 
ATOM   12910 C CD2 . TYR D 1 21  ? 49.081  -14.703 -19.500 1.00 69.64  ? 21  TYR D CD2 1 
ATOM   12911 C CE1 . TYR D 1 21  ? 46.990  -15.788 -18.072 1.00 67.36  ? 21  TYR D CE1 1 
ATOM   12912 C CE2 . TYR D 1 21  ? 47.774  -14.525 -19.937 1.00 69.04  ? 21  TYR D CE2 1 
ATOM   12913 C CZ  . TYR D 1 21  ? 46.719  -15.058 -19.217 1.00 67.55  ? 21  TYR D CZ  1 
ATOM   12914 O OH  . TYR D 1 21  ? 45.430  -14.854 -19.628 1.00 66.40  ? 21  TYR D OH  1 
ATOM   12915 N N   . PHE D 1 22  ? 50.306  -13.920 -14.856 1.00 68.65  ? 22  PHE D N   1 
ATOM   12916 C CA  . PHE D 1 22  ? 49.604  -13.969 -13.590 1.00 66.99  ? 22  PHE D CA  1 
ATOM   12917 C C   . PHE D 1 22  ? 48.148  -14.302 -13.885 1.00 66.42  ? 22  PHE D C   1 
ATOM   12918 O O   . PHE D 1 22  ? 47.505  -13.564 -14.614 1.00 66.46  ? 22  PHE D O   1 
ATOM   12919 C CB  . PHE D 1 22  ? 49.721  -12.634 -12.857 1.00 66.37  ? 22  PHE D CB  1 
ATOM   12920 C CG  . PHE D 1 22  ? 49.324  -12.725 -11.393 1.00 65.06  ? 22  PHE D CG  1 
ATOM   12921 C CD1 . PHE D 1 22  ? 48.006  -12.905 -11.015 1.00 64.68  ? 22  PHE D CD1 1 
ATOM   12922 C CD2 . PHE D 1 22  ? 50.272  -12.636 -10.391 1.00 65.26  ? 22  PHE D CD2 1 
ATOM   12923 C CE1 . PHE D 1 22  ? 47.651  -12.996 -9.672  1.00 64.08  ? 22  PHE D CE1 1 
ATOM   12924 C CE2 . PHE D 1 22  ? 49.912  -12.717 -9.055  1.00 64.42  ? 22  PHE D CE2 1 
ATOM   12925 C CZ  . PHE D 1 22  ? 48.607  -12.880 -8.694  1.00 63.62  ? 22  PHE D CZ  1 
ATOM   12926 N N   . ILE D 1 23  ? 47.651  -15.419 -13.337 1.00 66.22  ? 23  ILE D N   1 
ATOM   12927 C CA  . ILE D 1 23  ? 46.311  -15.892 -13.637 1.00 65.88  ? 23  ILE D CA  1 
ATOM   12928 C C   . ILE D 1 23  ? 45.360  -15.057 -12.798 1.00 64.85  ? 23  ILE D C   1 
ATOM   12929 O O   . ILE D 1 23  ? 45.327  -15.209 -11.579 1.00 62.84  ? 23  ILE D O   1 
ATOM   12930 C CB  . ILE D 1 23  ? 46.157  -17.408 -13.372 1.00 66.04  ? 23  ILE D CB  1 
ATOM   12931 C CG1 . ILE D 1 23  ? 47.295  -18.242 -14.040 1.00 66.76  ? 23  ILE D CG1 1 
ATOM   12932 C CG2 . ILE D 1 23  ? 44.765  -17.907 -13.781 1.00 64.62  ? 23  ILE D CG2 1 
ATOM   12933 C CD1 . ILE D 1 23  ? 47.259  -19.732 -13.725 1.00 66.21  ? 23  ILE D CD1 1 
ATOM   12934 N N   . LYS D 1 24  ? 44.668  -14.134 -13.473 1.00 66.78  ? 24  LYS D N   1 
ATOM   12935 C CA  . LYS D 1 24  ? 43.686  -13.263 -12.844 1.00 68.73  ? 24  LYS D CA  1 
ATOM   12936 C C   . LYS D 1 24  ? 42.285  -13.809 -13.118 1.00 69.41  ? 24  LYS D C   1 
ATOM   12937 O O   . LYS D 1 24  ? 41.604  -13.347 -14.027 1.00 70.91  ? 24  LYS D O   1 
ATOM   12938 C CB  . LYS D 1 24  ? 43.830  -11.838 -13.382 1.00 69.91  ? 24  LYS D CB  1 
ATOM   12939 C CG  . LYS D 1 24  ? 45.082  -11.095 -12.957 1.00 70.88  ? 24  LYS D CG  1 
ATOM   12940 C CD  . LYS D 1 24  ? 45.043  -9.624  -13.356 1.00 73.50  ? 24  LYS D CD  1 
ATOM   12941 C CE  . LYS D 1 24  ? 44.717  -9.409  -14.809 1.00 76.73  ? 24  LYS D CE  1 
ATOM   12942 N NZ  . LYS D 1 24  ? 45.031  -8.049  -15.255 1.00 78.47  ? 24  LYS D NZ  1 
ATOM   12943 N N   . ALA D 1 25  ? 41.884  -14.817 -12.340 1.00 68.49  ? 25  ALA D N   1 
ATOM   12944 C CA  . ALA D 1 25  ? 40.730  -15.622 -12.674 1.00 68.59  ? 25  ALA D CA  1 
ATOM   12945 C C   . ALA D 1 25  ? 39.548  -15.215 -11.817 1.00 68.36  ? 25  ALA D C   1 
ATOM   12946 O O   . ALA D 1 25  ? 39.696  -14.388 -10.931 1.00 70.32  ? 25  ALA D O   1 
ATOM   12947 C CB  . ALA D 1 25  ? 41.053  -17.062 -12.440 1.00 69.19  ? 25  ALA D CB  1 
ATOM   12948 N N   . ILE D 1 26  ? 38.394  -15.824 -12.083 1.00 67.51  ? 26  ILE D N   1 
ATOM   12949 C CA  . ILE D 1 26  ? 37.244  -15.732 -11.200 1.00 67.53  ? 26  ILE D CA  1 
ATOM   12950 C C   . ILE D 1 26  ? 36.474  -17.032 -11.313 1.00 67.94  ? 26  ILE D C   1 
ATOM   12951 O O   . ILE D 1 26  ? 36.331  -17.564 -12.412 1.00 72.32  ? 26  ILE D O   1 
ATOM   12952 C CB  . ILE D 1 26  ? 36.314  -14.564 -11.559 1.00 68.45  ? 26  ILE D CB  1 
ATOM   12953 C CG1 . ILE D 1 26  ? 35.179  -14.466 -10.544 1.00 69.85  ? 26  ILE D CG1 1 
ATOM   12954 C CG2 . ILE D 1 26  ? 35.776  -14.696 -12.989 1.00 68.60  ? 26  ILE D CG2 1 
ATOM   12955 C CD1 . ILE D 1 26  ? 34.385  -13.165 -10.598 1.00 70.66  ? 26  ILE D CD1 1 
ATOM   12956 N N   . GLY D 1 27  ? 35.966  -17.523 -10.183 1.00 66.15  ? 27  GLY D N   1 
ATOM   12957 C CA  . GLY D 1 27  ? 35.122  -18.714 -10.185 1.00 63.97  ? 27  GLY D CA  1 
ATOM   12958 C C   . GLY D 1 27  ? 33.760  -18.433 -10.833 1.00 61.42  ? 27  GLY D C   1 
ATOM   12959 O O   . GLY D 1 27  ? 33.133  -17.418 -10.517 1.00 59.32  ? 27  GLY D O   1 
ATOM   12960 N N   . TYR D 1 28  ? 33.347  -19.375 -11.710 1.00 60.20  ? 28  TYR D N   1 
ATOM   12961 C CA  . TYR D 1 28  ? 32.194  -19.281 -12.597 1.00 59.70  ? 28  TYR D CA  1 
ATOM   12962 C C   . TYR D 1 28  ? 31.481  -20.629 -12.741 1.00 60.53  ? 28  TYR D C   1 
ATOM   12963 O O   . TYR D 1 28  ? 31.960  -21.549 -13.393 1.00 61.87  ? 28  TYR D O   1 
ATOM   12964 C CB  . TYR D 1 28  ? 32.666  -18.843 -13.983 1.00 59.27  ? 28  TYR D CB  1 
ATOM   12965 C CG  . TYR D 1 28  ? 31.570  -18.714 -15.024 1.00 59.22  ? 28  TYR D CG  1 
ATOM   12966 C CD1 . TYR D 1 28  ? 30.433  -17.973 -14.763 1.00 59.35  ? 28  TYR D CD1 1 
ATOM   12967 C CD2 . TYR D 1 28  ? 31.685  -19.294 -16.274 1.00 59.57  ? 28  TYR D CD2 1 
ATOM   12968 C CE1 . TYR D 1 28  ? 29.417  -17.851 -15.700 1.00 60.33  ? 28  TYR D CE1 1 
ATOM   12969 C CE2 . TYR D 1 28  ? 30.700  -19.151 -17.234 1.00 60.66  ? 28  TYR D CE2 1 
ATOM   12970 C CZ  . TYR D 1 28  ? 29.542  -18.441 -16.947 1.00 61.07  ? 28  TYR D CZ  1 
ATOM   12971 O OH  . TYR D 1 28  ? 28.514  -18.294 -17.857 1.00 61.89  ? 28  TYR D OH  1 
ATOM   12972 N N   . GLU D 1 29  ? 30.284  -20.718 -12.168 1.00 60.86  ? 29  GLU D N   1 
ATOM   12973 C CA  . GLU D 1 29  ? 29.357  -21.819 -12.395 1.00 61.53  ? 29  GLU D CA  1 
ATOM   12974 C C   . GLU D 1 29  ? 28.167  -21.345 -13.233 1.00 62.48  ? 29  GLU D C   1 
ATOM   12975 O O   . GLU D 1 29  ? 27.360  -20.557 -12.743 1.00 62.48  ? 29  GLU D O   1 
ATOM   12976 C CB  . GLU D 1 29  ? 28.879  -22.235 -11.004 1.00 61.04  ? 29  GLU D CB  1 
ATOM   12977 C CG  . GLU D 1 29  ? 27.782  -23.287 -10.957 1.00 61.69  ? 29  GLU D CG  1 
ATOM   12978 C CD  . GLU D 1 29  ? 27.975  -24.089 -9.677  1.00 62.34  ? 29  GLU D CD  1 
ATOM   12979 O OE1 . GLU D 1 29  ? 27.628  -23.440 -8.663  1.00 61.11  ? 29  GLU D OE1 1 
ATOM   12980 O OE2 . GLU D 1 29  ? 28.526  -25.270 -9.681  1.00 64.20  ? 29  GLU D OE2 1 
ATOM   12981 N N   . ILE D 1 30  ? 28.112  -21.770 -14.507 1.00 63.39  ? 30  ILE D N   1 
ATOM   12982 C CA  . ILE D 1 30  ? 26.914  -21.710 -15.334 1.00 64.16  ? 30  ILE D CA  1 
ATOM   12983 C C   . ILE D 1 30  ? 25.960  -22.732 -14.726 1.00 64.91  ? 30  ILE D C   1 
ATOM   12984 O O   . ILE D 1 30  ? 26.365  -23.414 -13.798 1.00 63.85  ? 30  ILE D O   1 
ATOM   12985 C CB  . ILE D 1 30  ? 27.257  -21.977 -16.815 1.00 64.70  ? 30  ILE D CB  1 
ATOM   12986 C CG1 . ILE D 1 30  ? 26.105  -21.750 -17.777 1.00 66.04  ? 30  ILE D CG1 1 
ATOM   12987 C CG2 . ILE D 1 30  ? 27.810  -23.381 -16.995 1.00 65.02  ? 30  ILE D CG2 1 
ATOM   12988 C CD1 . ILE D 1 30  ? 25.537  -20.348 -17.765 1.00 66.27  ? 30  ILE D CD1 1 
ATOM   12989 N N   . GLY D 1 31  ? 24.691  -22.739 -15.149 1.00 66.58  ? 31  GLY D N   1 
ATOM   12990 C CA  . GLY D 1 31  ? 23.717  -23.688 -14.661 1.00 67.41  ? 31  GLY D CA  1 
ATOM   12991 C C   . GLY D 1 31  ? 23.238  -23.419 -13.234 1.00 68.01  ? 31  GLY D C   1 
ATOM   12992 O O   . GLY D 1 31  ? 22.701  -24.322 -12.601 1.00 70.55  ? 31  GLY D O   1 
ATOM   12993 N N   . ALA D 1 32  ? 23.348  -22.190 -12.728 1.00 68.23  ? 32  ALA D N   1 
ATOM   12994 C CA  . ALA D 1 32  ? 23.024  -21.946 -11.329 1.00 68.40  ? 32  ALA D CA  1 
ATOM   12995 C C   . ALA D 1 32  ? 22.263  -20.642 -11.149 1.00 70.33  ? 32  ALA D C   1 
ATOM   12996 O O   . ALA D 1 32  ? 22.439  -19.940 -10.155 1.00 73.33  ? 32  ALA D O   1 
ATOM   12997 C CB  . ALA D 1 32  ? 24.284  -21.939 -10.497 1.00 66.87  ? 32  ALA D CB  1 
ATOM   12998 N N   . ARG D 1 33  ? 21.390  -20.306 -12.094 1.00 71.12  ? 33  ARG D N   1 
ATOM   12999 C CA  . ARG D 1 33  ? 20.564  -19.139 -11.886 1.00 70.31  ? 33  ARG D CA  1 
ATOM   13000 C C   . ARG D 1 33  ? 19.562  -19.496 -10.799 1.00 70.19  ? 33  ARG D C   1 
ATOM   13001 O O   . ARG D 1 33  ? 19.498  -20.659 -10.361 1.00 69.81  ? 33  ARG D O   1 
ATOM   13002 C CB  . ARG D 1 33  ? 19.878  -18.719 -13.190 1.00 72.82  ? 33  ARG D CB  1 
ATOM   13003 C CG  . ARG D 1 33  ? 20.740  -18.210 -14.342 1.00 73.47  ? 33  ARG D CG  1 
ATOM   13004 C CD  . ARG D 1 33  ? 21.842  -17.274 -13.906 1.00 73.34  ? 33  ARG D CD  1 
ATOM   13005 N NE  . ARG D 1 33  ? 22.430  -16.465 -14.981 1.00 74.64  ? 33  ARG D NE  1 
ATOM   13006 C CZ  . ARG D 1 33  ? 23.596  -16.663 -15.590 1.00 72.83  ? 33  ARG D CZ  1 
ATOM   13007 N NH1 . ARG D 1 33  ? 24.188  -17.826 -15.514 1.00 72.23  ? 33  ARG D NH1 1 
ATOM   13008 N NH2 . ARG D 1 33  ? 24.125  -15.720 -16.339 1.00 73.11  ? 33  ARG D NH2 1 
ATOM   13009 N N   . PRO D 1 34  ? 18.746  -18.510 -10.351 1.00 69.71  ? 34  PRO D N   1 
ATOM   13010 C CA  . PRO D 1 34  ? 17.549  -18.803 -9.565  1.00 68.79  ? 34  PRO D CA  1 
ATOM   13011 C C   . PRO D 1 34  ? 16.640  -19.761 -10.328 1.00 69.83  ? 34  PRO D C   1 
ATOM   13012 O O   . PRO D 1 34  ? 16.312  -19.533 -11.484 1.00 69.22  ? 34  PRO D O   1 
ATOM   13013 C CB  . PRO D 1 34  ? 16.961  -17.410 -9.364  1.00 69.49  ? 34  PRO D CB  1 
ATOM   13014 C CG  . PRO D 1 34  ? 18.158  -16.474 -9.373  1.00 68.25  ? 34  PRO D CG  1 
ATOM   13015 C CD  . PRO D 1 34  ? 18.973  -17.057 -10.509 1.00 69.04  ? 34  PRO D CD  1 
ATOM   13016 N N   . GLY D 1 35  ? 16.326  -20.887 -9.683  1.00 70.96  ? 35  GLY D N   1 
ATOM   13017 C CA  . GLY D 1 35  ? 15.515  -21.936 -10.274 1.00 72.66  ? 35  GLY D CA  1 
ATOM   13018 C C   . GLY D 1 35  ? 16.304  -23.199 -10.634 1.00 72.69  ? 35  GLY D C   1 
ATOM   13019 O O   . GLY D 1 35  ? 15.696  -24.249 -10.821 1.00 73.79  ? 35  GLY D O   1 
ATOM   13020 N N   . GLN D 1 36  ? 17.638  -23.100 -10.737 1.00 71.87  ? 36  GLN D N   1 
ATOM   13021 C CA  . GLN D 1 36  ? 18.468  -24.135 -11.349 1.00 72.11  ? 36  GLN D CA  1 
ATOM   13022 C C   . GLN D 1 36  ? 19.325  -24.876 -10.318 1.00 71.02  ? 36  GLN D C   1 
ATOM   13023 O O   . GLN D 1 36  ? 19.788  -24.305 -9.336  1.00 71.45  ? 36  GLN D O   1 
ATOM   13024 C CB  . GLN D 1 36  ? 19.472  -23.535 -12.338 1.00 71.87  ? 36  GLN D CB  1 
ATOM   13025 C CG  . GLN D 1 36  ? 18.845  -22.727 -13.466 1.00 72.65  ? 36  GLN D CG  1 
ATOM   13026 C CD  . GLN D 1 36  ? 19.824  -22.417 -14.576 1.00 73.21  ? 36  GLN D CD  1 
ATOM   13027 O OE1 . GLN D 1 36  ? 20.877  -21.796 -14.361 1.00 74.18  ? 36  GLN D OE1 1 
ATOM   13028 N NE2 . GLN D 1 36  ? 19.500  -22.874 -15.776 1.00 73.88  ? 36  GLN D NE2 1 
ATOM   13029 N N   . ALA D 1 37  ? 19.607  -26.149 -10.590 1.00 70.82  ? 37  ALA D N   1 
ATOM   13030 C CA  . ALA D 1 37  ? 20.537  -26.914 -9.777  1.00 69.47  ? 37  ALA D CA  1 
ATOM   13031 C C   . ALA D 1 37  ? 21.466  -27.662 -10.721 1.00 69.27  ? 37  ALA D C   1 
ATOM   13032 O O   . ALA D 1 37  ? 21.038  -28.541 -11.459 1.00 69.85  ? 37  ALA D O   1 
ATOM   13033 C CB  . ALA D 1 37  ? 19.805  -27.852 -8.848  1.00 70.31  ? 37  ALA D CB  1 
ATOM   13034 N N   . PRO D 1 38  ? 22.754  -27.284 -10.785 1.00 68.13  ? 38  PRO D N   1 
ATOM   13035 C CA  . PRO D 1 38  ? 23.599  -27.733 -11.880 1.00 68.61  ? 38  PRO D CA  1 
ATOM   13036 C C   . PRO D 1 38  ? 23.895  -29.217 -11.745 1.00 69.50  ? 38  PRO D C   1 
ATOM   13037 O O   . PRO D 1 38  ? 23.996  -29.891 -12.755 1.00 70.78  ? 38  PRO D O   1 
ATOM   13038 C CB  . PRO D 1 38  ? 24.840  -26.866 -11.805 1.00 67.12  ? 38  PRO D CB  1 
ATOM   13039 C CG  . PRO D 1 38  ? 24.884  -26.439 -10.356 1.00 66.63  ? 38  PRO D CG  1 
ATOM   13040 C CD  . PRO D 1 38  ? 23.447  -26.390 -9.853  1.00 67.07  ? 38  PRO D CD  1 
ATOM   13041 N N   . TYR D 1 39  ? 23.973  -29.741 -10.519 1.00 69.84  ? 39  TYR D N   1 
ATOM   13042 C CA  . TYR D 1 39  ? 24.291  -31.153 -10.360 1.00 71.03  ? 39  TYR D CA  1 
ATOM   13043 C C   . TYR D 1 39  ? 23.018  -31.993 -10.516 1.00 73.01  ? 39  TYR D C   1 
ATOM   13044 O O   . TYR D 1 39  ? 23.129  -33.153 -10.881 1.00 72.77  ? 39  TYR D O   1 
ATOM   13045 C CB  . TYR D 1 39  ? 25.069  -31.380 -9.058  1.00 70.57  ? 39  TYR D CB  1 
ATOM   13046 C CG  . TYR D 1 39  ? 26.436  -30.714 -9.065  1.00 71.73  ? 39  TYR D CG  1 
ATOM   13047 C CD1 . TYR D 1 39  ? 27.356  -30.938 -10.091 1.00 73.15  ? 39  TYR D CD1 1 
ATOM   13048 C CD2 . TYR D 1 39  ? 26.786  -29.812 -8.070  1.00 72.29  ? 39  TYR D CD2 1 
ATOM   13049 C CE1 . TYR D 1 39  ? 28.602  -30.332 -10.085 1.00 73.13  ? 39  TYR D CE1 1 
ATOM   13050 C CE2 . TYR D 1 39  ? 28.024  -29.196 -8.054  1.00 72.36  ? 39  TYR D CE2 1 
ATOM   13051 C CZ  . TYR D 1 39  ? 28.930  -29.444 -9.070  1.00 73.13  ? 39  TYR D CZ  1 
ATOM   13052 O OH  . TYR D 1 39  ? 30.111  -28.755 -9.043  1.00 73.08  ? 39  TYR D OH  1 
ATOM   13053 N N   . GLU D 1 40  ? 21.829  -31.400 -10.290 1.00 74.64  ? 40  GLU D N   1 
ATOM   13054 C CA  . GLU D 1 40  ? 20.569  -32.124 -10.275 1.00 76.32  ? 40  GLU D CA  1 
ATOM   13055 C C   . GLU D 1 40  ? 19.875  -32.040 -11.625 1.00 76.55  ? 40  GLU D C   1 
ATOM   13056 O O   . GLU D 1 40  ? 19.314  -33.035 -12.058 1.00 78.28  ? 40  GLU D O   1 
ATOM   13057 C CB  . GLU D 1 40  ? 19.588  -31.606 -9.228  1.00 78.97  ? 40  GLU D CB  1 
ATOM   13058 C CG  . GLU D 1 40  ? 20.208  -31.324 -7.863  1.00 81.46  ? 40  GLU D CG  1 
ATOM   13059 C CD  . GLU D 1 40  ? 20.956  -32.463 -7.182  1.00 85.50  ? 40  GLU D CD  1 
ATOM   13060 O OE1 . GLU D 1 40  ? 21.820  -33.062 -7.855  1.00 89.35  ? 40  GLU D OE1 1 
ATOM   13061 O OE2 . GLU D 1 40  ? 20.732  -32.735 -5.974  1.00 87.38  ? 40  GLU D OE2 1 
ATOM   13062 N N   . ASP D 1 41  ? 19.892  -30.871 -12.271 1.00 76.21  ? 41  ASP D N   1 
ATOM   13063 C CA  . ASP D 1 41  ? 19.115  -30.650 -13.486 1.00 78.63  ? 41  ASP D CA  1 
ATOM   13064 C C   . ASP D 1 41  ? 19.718  -31.435 -14.649 1.00 80.42  ? 41  ASP D C   1 
ATOM   13065 O O   . ASP D 1 41  ? 20.902  -31.740 -14.618 1.00 81.51  ? 41  ASP D O   1 
ATOM   13066 C CB  . ASP D 1 41  ? 19.091  -29.177 -13.895 1.00 77.67  ? 41  ASP D CB  1 
ATOM   13067 C CG  . ASP D 1 41  ? 18.356  -28.193 -12.989 1.00 76.51  ? 41  ASP D CG  1 
ATOM   13068 O OD1 . ASP D 1 41  ? 17.828  -28.625 -11.933 1.00 76.49  ? 41  ASP D OD1 1 
ATOM   13069 O OD2 . ASP D 1 41  ? 18.332  -26.992 -13.342 1.00 74.75  ? 41  ASP D OD2 1 
ATOM   13070 N N   . GLU D 1 42  ? 18.921  -31.712 -15.691 1.00 83.84  ? 42  GLU D N   1 
ATOM   13071 C CA  . GLU D 1 42  ? 19.458  -32.052 -17.002 1.00 88.38  ? 42  GLU D CA  1 
ATOM   13072 C C   . GLU D 1 42  ? 20.427  -30.958 -17.430 1.00 90.05  ? 42  GLU D C   1 
ATOM   13073 O O   . GLU D 1 42  ? 20.063  -29.784 -17.391 1.00 93.11  ? 42  GLU D O   1 
ATOM   13074 C CB  . GLU D 1 42  ? 18.376  -32.107 -18.084 1.00 94.97  ? 42  GLU D CB  1 
ATOM   13075 C CG  . GLU D 1 42  ? 18.911  -32.482 -19.470 1.00 99.86  ? 42  GLU D CG  1 
ATOM   13076 C CD  . GLU D 1 42  ? 17.932  -32.400 -20.635 1.00 104.47 ? 42  GLU D CD  1 
ATOM   13077 O OE1 . GLU D 1 42  ? 16.759  -32.042 -20.392 1.00 106.56 ? 42  GLU D OE1 1 
ATOM   13078 O OE2 . GLU D 1 42  ? 18.339  -32.704 -21.784 1.00 107.05 ? 42  GLU D OE2 1 
ATOM   13079 N N   . ARG D 1 43  ? 21.647  -31.329 -17.841 1.00 90.57  ? 43  ARG D N   1 
ATOM   13080 C CA  . ARG D 1 43  ? 22.642  -30.341 -18.231 1.00 89.03  ? 43  ARG D CA  1 
ATOM   13081 C C   . ARG D 1 43  ? 22.246  -29.710 -19.566 1.00 89.31  ? 43  ARG D C   1 
ATOM   13082 O O   . ARG D 1 43  ? 21.746  -30.396 -20.455 1.00 89.33  ? 43  ARG D O   1 
ATOM   13083 C CB  . ARG D 1 43  ? 24.031  -30.976 -18.341 1.00 91.29  ? 43  ARG D CB  1 
ATOM   13084 C CG  . ARG D 1 43  ? 24.319  -31.746 -19.624 1.00 94.33  ? 43  ARG D CG  1 
ATOM   13085 C CD  . ARG D 1 43  ? 25.721  -32.329 -19.610 1.00 96.59  ? 43  ARG D CD  1 
ATOM   13086 N NE  . ARG D 1 43  ? 25.880  -33.403 -20.601 1.00 100.68 ? 43  ARG D NE  1 
ATOM   13087 C CZ  . ARG D 1 43  ? 26.881  -34.290 -20.667 1.00 101.44 ? 43  ARG D CZ  1 
ATOM   13088 N NH1 . ARG D 1 43  ? 27.857  -34.299 -19.764 1.00 101.28 ? 43  ARG D NH1 1 
ATOM   13089 N NH2 . ARG D 1 43  ? 26.903  -35.167 -21.659 1.00 101.83 ? 43  ARG D NH2 1 
ATOM   13090 N N   . LYS D 1 44  ? 22.459  -28.393 -19.688 1.00 88.74  ? 44  LYS D N   1 
ATOM   13091 C CA  . LYS D 1 44  ? 22.301  -27.691 -20.953 1.00 89.28  ? 44  LYS D CA  1 
ATOM   13092 C C   . LYS D 1 44  ? 23.508  -26.780 -21.155 1.00 84.56  ? 44  LYS D C   1 
ATOM   13093 O O   . LYS D 1 44  ? 24.063  -26.263 -20.191 1.00 80.87  ? 44  LYS D O   1 
ATOM   13094 C CB  . LYS D 1 44  ? 21.047  -26.812 -21.035 1.00 93.09  ? 44  LYS D CB  1 
ATOM   13095 C CG  . LYS D 1 44  ? 19.750  -27.500 -21.403 1.00 99.62  ? 44  LYS D CG  1 
ATOM   13096 C CD  . LYS D 1 44  ? 18.993  -28.098 -20.222 1.00 106.84 ? 44  LYS D CD  1 
ATOM   13097 C CE  . LYS D 1 44  ? 18.552  -27.069 -19.207 1.00 111.28 ? 44  LYS D CE  1 
ATOM   13098 N NZ  . LYS D 1 44  ? 17.851  -27.680 -18.072 1.00 112.45 ? 44  LYS D NZ  1 
ATOM   13099 N N   . ASP D 1 45  ? 23.865  -26.570 -22.425 1.00 82.77  ? 45  ASP D N   1 
ATOM   13100 C CA  . ASP D 1 45  ? 24.995  -25.740 -22.800 1.00 80.70  ? 45  ASP D CA  1 
ATOM   13101 C C   . ASP D 1 45  ? 24.756  -24.291 -22.370 1.00 81.17  ? 45  ASP D C   1 
ATOM   13102 O O   . ASP D 1 45  ? 25.677  -23.604 -21.917 1.00 78.08  ? 45  ASP D O   1 
ATOM   13103 C CB  . ASP D 1 45  ? 25.229  -25.837 -24.297 1.00 80.33  ? 45  ASP D CB  1 
ATOM   13104 C CG  . ASP D 1 45  ? 25.829  -27.136 -24.797 1.00 79.19  ? 45  ASP D CG  1 
ATOM   13105 O OD1 . ASP D 1 45  ? 26.251  -27.951 -23.947 1.00 77.59  ? 45  ASP D OD1 1 
ATOM   13106 O OD2 . ASP D 1 45  ? 25.863  -27.308 -26.031 1.00 79.21  ? 45  ASP D OD2 1 
ATOM   13107 N N   . GLU D 1 46  ? 23.519  -23.822 -22.572 1.00 83.98  ? 46  GLU D N   1 
ATOM   13108 C CA  . GLU D 1 46  ? 23.109  -22.515 -22.090 1.00 85.60  ? 46  GLU D CA  1 
ATOM   13109 C C   . GLU D 1 46  ? 24.090  -21.447 -22.572 1.00 84.06  ? 46  GLU D C   1 
ATOM   13110 O O   . GLU D 1 46  ? 24.645  -20.708 -21.765 1.00 83.66  ? 46  GLU D O   1 
ATOM   13111 C CB  . GLU D 1 46  ? 23.044  -22.615 -20.566 1.00 85.43  ? 46  GLU D CB  1 
ATOM   13112 C CG  . GLU D 1 46  ? 22.037  -21.662 -19.926 1.00 85.51  ? 46  GLU D CG  1 
ATOM   13113 C CD  . GLU D 1 46  ? 21.559  -22.232 -18.610 1.00 84.14  ? 46  GLU D CD  1 
ATOM   13114 O OE1 . GLU D 1 46  ? 21.912  -23.385 -18.326 1.00 84.77  ? 46  GLU D OE1 1 
ATOM   13115 O OE2 . GLU D 1 46  ? 20.837  -21.554 -17.876 1.00 83.95  ? 46  GLU D OE2 1 
ATOM   13116 N N   . LEU D 1 47  ? 24.290  -21.382 -23.895 1.00 84.16  ? 47  LEU D N   1 
ATOM   13117 C CA  . LEU D 1 47  ? 25.280  -20.506 -24.501 1.00 82.42  ? 47  LEU D CA  1 
ATOM   13118 C C   . LEU D 1 47  ? 24.926  -19.042 -24.242 1.00 82.87  ? 47  LEU D C   1 
ATOM   13119 O O   . LEU D 1 47  ? 25.797  -18.249 -23.872 1.00 79.25  ? 47  LEU D O   1 
ATOM   13120 C CB  . LEU D 1 47  ? 25.369  -20.806 -25.998 1.00 83.00  ? 47  LEU D CB  1 
ATOM   13121 C CG  . LEU D 1 47  ? 25.800  -22.224 -26.388 1.00 82.78  ? 47  LEU D CG  1 
ATOM   13122 C CD1 . LEU D 1 47  ? 26.301  -22.240 -27.825 1.00 84.56  ? 47  LEU D CD1 1 
ATOM   13123 C CD2 . LEU D 1 47  ? 26.844  -22.806 -25.465 1.00 80.63  ? 47  LEU D CD2 1 
ATOM   13124 N N   . GLU D 1 48  ? 23.638  -18.703 -24.429 1.00 85.81  ? 48  GLU D N   1 
ATOM   13125 C CA  . GLU D 1 48  ? 23.197  -17.314 -24.426 1.00 86.75  ? 48  GLU D CA  1 
ATOM   13126 C C   . GLU D 1 48  ? 23.637  -16.612 -23.142 1.00 82.14  ? 48  GLU D C   1 
ATOM   13127 O O   . GLU D 1 48  ? 24.185  -15.511 -23.202 1.00 80.79  ? 48  GLU D O   1 
ATOM   13128 C CB  . GLU D 1 48  ? 21.688  -17.172 -24.646 1.00 91.70  ? 48  GLU D CB  1 
ATOM   13129 C CG  . GLU D 1 48  ? 21.267  -17.274 -26.111 1.00 97.72  ? 48  GLU D CG  1 
ATOM   13130 C CD  . GLU D 1 48  ? 21.921  -16.283 -27.070 1.00 102.81 ? 48  GLU D CD  1 
ATOM   13131 O OE1 . GLU D 1 48  ? 22.543  -15.280 -26.634 1.00 107.43 ? 48  GLU D OE1 1 
ATOM   13132 O OE2 . GLU D 1 48  ? 21.830  -16.543 -28.289 1.00 106.32 ? 48  GLU D OE2 1 
ATOM   13133 N N   . LEU D 1 49  ? 23.415  -17.260 -21.992 1.00 79.10  ? 49  LEU D N   1 
ATOM   13134 C CA  . LEU D 1 49  ? 23.750  -16.658 -20.714 1.00 76.88  ? 49  LEU D CA  1 
ATOM   13135 C C   . LEU D 1 49  ? 25.268  -16.588 -20.583 1.00 75.83  ? 49  LEU D C   1 
ATOM   13136 O O   . LEU D 1 49  ? 25.785  -15.587 -20.069 1.00 74.59  ? 49  LEU D O   1 
ATOM   13137 C CB  . LEU D 1 49  ? 23.105  -17.334 -19.506 1.00 76.16  ? 49  LEU D CB  1 
ATOM   13138 C CG  . LEU D 1 49  ? 21.598  -17.083 -19.342 1.00 78.13  ? 49  LEU D CG  1 
ATOM   13139 C CD1 . LEU D 1 49  ? 20.773  -17.870 -20.351 1.00 79.92  ? 49  LEU D CD1 1 
ATOM   13140 C CD2 . LEU D 1 49  ? 21.102  -17.404 -17.938 1.00 77.09  ? 49  LEU D CD2 1 
ATOM   13141 N N   . MET D 1 50  ? 25.990  -17.606 -21.081 1.00 74.82  ? 50  MET D N   1 
ATOM   13142 C CA  . MET D 1 50  ? 27.446  -17.521 -21.035 1.00 74.28  ? 50  MET D CA  1 
ATOM   13143 C C   . MET D 1 50  ? 27.926  -16.264 -21.767 1.00 74.14  ? 50  MET D C   1 
ATOM   13144 O O   . MET D 1 50  ? 28.777  -15.551 -21.237 1.00 73.33  ? 50  MET D O   1 
ATOM   13145 C CB  . MET D 1 50  ? 28.167  -18.744 -21.620 1.00 75.03  ? 50  MET D CB  1 
ATOM   13146 C CG  . MET D 1 50  ? 28.187  -19.968 -20.715 1.00 74.11  ? 50  MET D CG  1 
ATOM   13147 S SD  . MET D 1 50  ? 28.787  -21.461 -21.534 1.00 73.27  ? 50  MET D SD  1 
ATOM   13148 C CE  . MET D 1 50  ? 30.507  -21.472 -21.024 1.00 72.89  ? 50  MET D CE  1 
ATOM   13149 N N   . LYS D 1 51  ? 27.394  -15.975 -22.967 1.00 74.96  ? 51  LYS D N   1 
ATOM   13150 C CA  . LYS D 1 51  ? 27.880  -14.835 -23.737 1.00 76.34  ? 51  LYS D CA  1 
ATOM   13151 C C   . LYS D 1 51  ? 27.776  -13.555 -22.908 1.00 75.17  ? 51  LYS D C   1 
ATOM   13152 O O   . LYS D 1 51  ? 28.663  -12.705 -22.949 1.00 73.81  ? 51  LYS D O   1 
ATOM   13153 C CB  . LYS D 1 51  ? 27.184  -14.637 -25.088 1.00 78.77  ? 51  LYS D CB  1 
ATOM   13154 C CG  . LYS D 1 51  ? 27.564  -15.712 -26.101 1.00 80.78  ? 51  LYS D CG  1 
ATOM   13155 C CD  . LYS D 1 51  ? 26.691  -15.719 -27.350 1.00 83.46  ? 51  LYS D CD  1 
ATOM   13156 C CE  . LYS D 1 51  ? 26.517  -17.074 -27.962 1.00 83.76  ? 51  LYS D CE  1 
ATOM   13157 N NZ  . LYS D 1 51  ? 25.288  -17.073 -28.757 1.00 85.54  ? 51  LYS D NZ  1 
ATOM   13158 N N   . PHE D 1 52  ? 26.698  -13.452 -22.131 1.00 74.42  ? 52  PHE D N   1 
ATOM   13159 C CA  . PHE D 1 52  ? 26.498  -12.318 -21.251 1.00 73.44  ? 52  PHE D CA  1 
ATOM   13160 C C   . PHE D 1 52  ? 27.465  -12.368 -20.071 1.00 71.80  ? 52  PHE D C   1 
ATOM   13161 O O   . PHE D 1 52  ? 27.925  -11.328 -19.630 1.00 73.67  ? 52  PHE D O   1 
ATOM   13162 C CB  . PHE D 1 52  ? 25.034  -12.310 -20.808 1.00 73.83  ? 52  PHE D CB  1 
ATOM   13163 C CG  . PHE D 1 52  ? 24.768  -11.626 -19.480 1.00 72.44  ? 52  PHE D CG  1 
ATOM   13164 C CD1 . PHE D 1 52  ? 24.954  -12.317 -18.294 1.00 71.55  ? 52  PHE D CD1 1 
ATOM   13165 C CD2 . PHE D 1 52  ? 24.315  -10.315 -19.422 1.00 72.46  ? 52  PHE D CD2 1 
ATOM   13166 C CE1 . PHE D 1 52  ? 24.706  -11.712 -17.075 1.00 71.35  ? 52  PHE D CE1 1 
ATOM   13167 C CE2 . PHE D 1 52  ? 24.061  -9.715  -18.201 1.00 71.69  ? 52  PHE D CE2 1 
ATOM   13168 C CZ  . PHE D 1 52  ? 24.265  -10.408 -17.030 1.00 71.15  ? 52  PHE D CZ  1 
ATOM   13169 N N   . ASP D 1 53  ? 27.743  -13.549 -19.522 1.00 70.26  ? 53  ASP D N   1 
ATOM   13170 C CA  . ASP D 1 53  ? 28.609  -13.642 -18.357 1.00 68.16  ? 53  ASP D CA  1 
ATOM   13171 C C   . ASP D 1 53  ? 30.069  -13.447 -18.780 1.00 69.02  ? 53  ASP D C   1 
ATOM   13172 O O   . ASP D 1 53  ? 30.838  -12.685 -18.179 1.00 68.55  ? 53  ASP D O   1 
ATOM   13173 C CB  . ASP D 1 53  ? 28.444  -14.978 -17.646 1.00 66.85  ? 53  ASP D CB  1 
ATOM   13174 C CG  . ASP D 1 53  ? 27.052  -15.352 -17.145 1.00 65.96  ? 53  ASP D CG  1 
ATOM   13175 O OD1 . ASP D 1 53  ? 26.210  -14.465 -17.010 1.00 65.41  ? 53  ASP D OD1 1 
ATOM   13176 O OD2 . ASP D 1 53  ? 26.822  -16.552 -16.886 1.00 65.18  ? 53  ASP D OD2 1 
ATOM   13177 N N   . LEU D 1 54  ? 30.483  -14.165 -19.823 1.00 69.94  ? 54  LEU D N   1 
ATOM   13178 C CA  . LEU D 1 54  ? 31.883  -14.140 -20.210 1.00 69.34  ? 54  LEU D CA  1 
ATOM   13179 C C   . LEU D 1 54  ? 32.263  -12.707 -20.567 1.00 69.57  ? 54  LEU D C   1 
ATOM   13180 O O   . LEU D 1 54  ? 33.326  -12.229 -20.162 1.00 69.33  ? 54  LEU D O   1 
ATOM   13181 C CB  . LEU D 1 54  ? 32.154  -15.122 -21.351 1.00 69.85  ? 54  LEU D CB  1 
ATOM   13182 C CG  . LEU D 1 54  ? 31.985  -16.604 -21.006 1.00 69.11  ? 54  LEU D CG  1 
ATOM   13183 C CD1 . LEU D 1 54  ? 31.998  -17.404 -22.293 1.00 70.97  ? 54  LEU D CD1 1 
ATOM   13184 C CD2 . LEU D 1 54  ? 33.025  -17.136 -20.029 1.00 67.30  ? 54  LEU D CD2 1 
ATOM   13185 N N   . GLU D 1 55  ? 31.379  -12.032 -21.306 1.00 70.31  ? 55  GLU D N   1 
ATOM   13186 C CA  . GLU D 1 55  ? 31.606  -10.645 -21.666 1.00 72.17  ? 55  GLU D CA  1 
ATOM   13187 C C   . GLU D 1 55  ? 31.675  -9.770  -20.409 1.00 70.25  ? 55  GLU D C   1 
ATOM   13188 O O   . GLU D 1 55  ? 32.478  -8.846  -20.329 1.00 69.41  ? 55  GLU D O   1 
ATOM   13189 C CB  . GLU D 1 55  ? 30.530  -10.152 -22.635 1.00 75.30  ? 55  GLU D CB  1 
ATOM   13190 C CG  . GLU D 1 55  ? 30.780  -8.741  -23.173 1.00 77.69  ? 55  GLU D CG  1 
ATOM   13191 C CD  . GLU D 1 55  ? 32.091  -8.504  -23.925 1.00 78.79  ? 55  GLU D CD  1 
ATOM   13192 O OE1 . GLU D 1 55  ? 32.661  -9.480  -24.459 1.00 77.74  ? 55  GLU D OE1 1 
ATOM   13193 O OE2 . GLU D 1 55  ? 32.536  -7.328  -23.988 1.00 80.70  ? 55  GLU D OE2 1 
ATOM   13194 N N   . ASN D 1 56  ? 30.827  -10.040 -19.415 1.00 68.77  ? 56  ASN D N   1 
ATOM   13195 C CA  . ASN D 1 56  ? 30.891  -9.275  -18.179 1.00 67.14  ? 56  ASN D CA  1 
ATOM   13196 C C   . ASN D 1 56  ? 32.232  -9.510  -17.497 1.00 64.14  ? 56  ASN D C   1 
ATOM   13197 O O   . ASN D 1 56  ? 32.779  -8.596  -16.900 1.00 61.88  ? 56  ASN D O   1 
ATOM   13198 C CB  . ASN D 1 56  ? 29.791  -9.640  -17.185 1.00 66.97  ? 56  ASN D CB  1 
ATOM   13199 C CG  . ASN D 1 56  ? 28.424  -9.253  -17.667 1.00 68.91  ? 56  ASN D CG  1 
ATOM   13200 O OD1 . ASN D 1 56  ? 28.252  -8.842  -18.816 1.00 70.35  ? 56  ASN D OD1 1 
ATOM   13201 N ND2 . ASN D 1 56  ? 27.426  -9.431  -16.820 1.00 70.97  ? 56  ASN D ND2 1 
ATOM   13202 N N   . ILE D 1 57  ? 32.684  -10.767 -17.561 1.00 63.79  ? 57  ILE D N   1 
ATOM   13203 C CA  . ILE D 1 57  ? 33.865  -11.233 -16.850 1.00 63.11  ? 57  ILE D CA  1 
ATOM   13204 C C   . ILE D 1 57  ? 35.114  -10.565 -17.433 1.00 63.12  ? 57  ILE D C   1 
ATOM   13205 O O   . ILE D 1 57  ? 35.954  -10.089 -16.673 1.00 61.24  ? 57  ILE D O   1 
ATOM   13206 C CB  . ILE D 1 57  ? 33.891  -12.779 -16.825 1.00 63.06  ? 57  ILE D CB  1 
ATOM   13207 C CG1 . ILE D 1 57  ? 32.818  -13.292 -15.872 1.00 62.58  ? 57  ILE D CG1 1 
ATOM   13208 C CG2 . ILE D 1 57  ? 35.252  -13.348 -16.430 1.00 62.46  ? 57  ILE D CG2 1 
ATOM   13209 C CD1 . ILE D 1 57  ? 32.687  -14.798 -15.847 1.00 63.02  ? 57  ILE D CD1 1 
ATOM   13210 N N   . LYS D 1 58  ? 35.180  -10.436 -18.765 1.00 64.96  ? 58  LYS D N   1 
ATOM   13211 C CA  . LYS D 1 58  ? 36.205  -9.620  -19.406 1.00 66.33  ? 58  LYS D CA  1 
ATOM   13212 C C   . LYS D 1 58  ? 36.084  -8.177  -18.915 1.00 68.10  ? 58  LYS D C   1 
ATOM   13213 O O   . LYS D 1 58  ? 36.982  -7.711  -18.230 1.00 69.40  ? 58  LYS D O   1 
ATOM   13214 C CB  . LYS D 1 58  ? 36.185  -9.696  -20.936 1.00 67.65  ? 58  LYS D CB  1 
ATOM   13215 C CG  . LYS D 1 58  ? 36.262  -11.131 -21.434 1.00 68.15  ? 58  LYS D CG  1 
ATOM   13216 C CD  . LYS D 1 58  ? 36.545  -11.272 -22.918 1.00 69.92  ? 58  LYS D CD  1 
ATOM   13217 C CE  . LYS D 1 58  ? 35.357  -11.004 -23.755 1.00 71.12  ? 58  LYS D CE  1 
ATOM   13218 N NZ  . LYS D 1 58  ? 35.675  -11.137 -25.177 1.00 72.94  ? 58  LYS D NZ  1 
ATOM   13219 N N   . GLU D 1 59  ? 34.963  -7.481  -19.182 1.00 69.78  ? 59  GLU D N   1 
ATOM   13220 C CA  . GLU D 1 59  ? 34.779  -6.127  -18.679 1.00 69.90  ? 59  GLU D CA  1 
ATOM   13221 C C   . GLU D 1 59  ? 35.105  -6.053  -17.179 1.00 68.30  ? 59  GLU D C   1 
ATOM   13222 O O   . GLU D 1 59  ? 35.324  -4.973  -16.657 1.00 69.99  ? 59  GLU D O   1 
ATOM   13223 C CB  . GLU D 1 59  ? 33.379  -5.557  -18.906 1.00 71.69  ? 59  GLU D CB  1 
ATOM   13224 C CG  . GLU D 1 59  ? 32.930  -5.411  -20.362 1.00 75.79  ? 59  GLU D CG  1 
ATOM   13225 C CD  . GLU D 1 59  ? 31.390  -5.369  -20.588 1.00 80.90  ? 59  GLU D CD  1 
ATOM   13226 O OE1 . GLU D 1 59  ? 30.570  -5.245  -19.619 1.00 80.07  ? 59  GLU D OE1 1 
ATOM   13227 O OE2 . GLU D 1 59  ? 30.955  -5.512  -21.773 1.00 84.52  ? 59  GLU D OE2 1 
ATOM   13228 N N   . GLY D 1 60  ? 35.151  -7.176  -16.462 1.00 67.18  ? 60  GLY D N   1 
ATOM   13229 C CA  . GLY D 1 60  ? 35.311  -7.157  -15.017 1.00 66.08  ? 60  GLY D CA  1 
ATOM   13230 C C   . GLY D 1 60  ? 36.772  -7.144  -14.583 1.00 66.26  ? 60  GLY D C   1 
ATOM   13231 O O   . GLY D 1 60  ? 37.043  -7.069  -13.389 1.00 67.58  ? 60  GLY D O   1 
ATOM   13232 N N   . GLY D 1 61  ? 37.696  -7.267  -15.543 1.00 66.38  ? 61  GLY D N   1 
ATOM   13233 C CA  . GLY D 1 61  ? 39.133  -7.221  -15.280 1.00 65.54  ? 61  GLY D CA  1 
ATOM   13234 C C   . GLY D 1 61  ? 39.866  -8.572  -15.319 1.00 64.36  ? 61  GLY D C   1 
ATOM   13235 O O   . GLY D 1 61  ? 41.085  -8.597  -15.200 1.00 65.46  ? 61  GLY D O   1 
ATOM   13236 N N   . TYR D 1 62  ? 39.145  -9.682  -15.521 1.00 63.62  ? 62  TYR D N   1 
ATOM   13237 C CA  . TYR D 1 62  ? 39.660  -11.033 -15.361 1.00 62.58  ? 62  TYR D CA  1 
ATOM   13238 C C   . TYR D 1 62  ? 40.179  -11.526 -16.705 1.00 63.41  ? 62  TYR D C   1 
ATOM   13239 O O   . TYR D 1 62  ? 39.654  -11.145 -17.741 1.00 62.92  ? 62  TYR D O   1 
ATOM   13240 C CB  . TYR D 1 62  ? 38.549  -11.948 -14.823 1.00 62.94  ? 62  TYR D CB  1 
ATOM   13241 C CG  . TYR D 1 62  ? 37.930  -11.459 -13.520 1.00 63.23  ? 62  TYR D CG  1 
ATOM   13242 C CD1 . TYR D 1 62  ? 36.842  -10.594 -13.502 1.00 64.44  ? 62  TYR D CD1 1 
ATOM   13243 C CD2 . TYR D 1 62  ? 38.479  -11.819 -12.303 1.00 63.15  ? 62  TYR D CD2 1 
ATOM   13244 C CE1 . TYR D 1 62  ? 36.333  -10.103 -12.309 1.00 65.31  ? 62  TYR D CE1 1 
ATOM   13245 C CE2 . TYR D 1 62  ? 37.986  -11.332 -11.106 1.00 63.03  ? 62  TYR D CE2 1 
ATOM   13246 C CZ  . TYR D 1 62  ? 36.905  -10.481 -11.103 1.00 64.84  ? 62  TYR D CZ  1 
ATOM   13247 O OH  . TYR D 1 62  ? 36.439  -10.049 -9.889  1.00 66.52  ? 62  TYR D OH  1 
ATOM   13248 N N   . ASN D 1 63  ? 41.223  -12.374 -16.676 1.00 64.57  ? 63  ASN D N   1 
ATOM   13249 C CA  . ASN D 1 63  ? 41.718  -13.037 -17.873 1.00 66.59  ? 63  ASN D CA  1 
ATOM   13250 C C   . ASN D 1 63  ? 41.397  -14.534 -17.832 1.00 66.26  ? 63  ASN D C   1 
ATOM   13251 O O   . ASN D 1 63  ? 41.688  -15.227 -18.802 1.00 68.11  ? 63  ASN D O   1 
ATOM   13252 C CB  . ASN D 1 63  ? 43.211  -12.803 -18.051 1.00 68.90  ? 63  ASN D CB  1 
ATOM   13253 C CG  . ASN D 1 63  ? 44.000  -13.441 -16.930 1.00 70.91  ? 63  ASN D CG  1 
ATOM   13254 O OD1 . ASN D 1 63  ? 43.440  -14.194 -16.118 1.00 73.30  ? 63  ASN D OD1 1 
ATOM   13255 N ND2 . ASN D 1 63  ? 45.289  -13.156 -16.861 1.00 71.76  ? 63  ASN D ND2 1 
ATOM   13256 N N   . THR D 1 64  ? 40.790  -15.035 -16.741 1.00 64.67  ? 64  THR D N   1 
ATOM   13257 C CA  . THR D 1 64  ? 40.526  -16.461 -16.617 1.00 64.87  ? 64  THR D CA  1 
ATOM   13258 C C   . THR D 1 64  ? 39.256  -16.760 -15.815 1.00 63.31  ? 64  THR D C   1 
ATOM   13259 O O   . THR D 1 64  ? 38.967  -16.028 -14.868 1.00 62.06  ? 64  THR D O   1 
ATOM   13260 C CB  . THR D 1 64  ? 41.731  -17.086 -15.926 1.00 64.99  ? 64  THR D CB  1 
ATOM   13261 O OG1 . THR D 1 64  ? 42.827  -16.685 -16.740 1.00 66.86  ? 64  THR D OG1 1 
ATOM   13262 C CG2 . THR D 1 64  ? 41.595  -18.595 -15.796 1.00 65.10  ? 64  THR D CG2 1 
ATOM   13263 N N   . ILE D 1 65  ? 38.571  -17.875 -16.164 1.00 62.69  ? 65  ILE D N   1 
ATOM   13264 C CA  . ILE D 1 65  ? 37.513  -18.477 -15.348 1.00 62.58  ? 65  ILE D CA  1 
ATOM   13265 C C   . ILE D 1 65  ? 37.956  -19.827 -14.780 1.00 63.18  ? 65  ILE D C   1 
ATOM   13266 O O   . ILE D 1 65  ? 38.674  -20.607 -15.431 1.00 64.29  ? 65  ILE D O   1 
ATOM   13267 C CB  . ILE D 1 65  ? 36.181  -18.697 -16.101 1.00 62.57  ? 65  ILE D CB  1 
ATOM   13268 C CG1 . ILE D 1 65  ? 36.391  -19.533 -17.365 1.00 62.92  ? 65  ILE D CG1 1 
ATOM   13269 C CG2 . ILE D 1 65  ? 35.483  -17.363 -16.372 1.00 63.43  ? 65  ILE D CG2 1 
ATOM   13270 C CD1 . ILE D 1 65  ? 35.218  -19.588 -18.311 1.00 63.34  ? 65  ILE D CD1 1 
ATOM   13271 N N   . ARG D 1 66  ? 37.396  -20.133 -13.597 1.00 62.28  ? 66  ARG D N   1 
ATOM   13272 C CA  . ARG D 1 66  ? 37.694  -21.360 -12.873 1.00 62.30  ? 66  ARG D CA  1 
ATOM   13273 C C   . ARG D 1 66  ? 36.376  -22.089 -12.592 1.00 61.48  ? 66  ARG D C   1 
ATOM   13274 O O   . ARG D 1 66  ? 35.476  -21.498 -12.020 1.00 61.41  ? 66  ARG D O   1 
ATOM   13275 C CB  . ARG D 1 66  ? 38.488  -20.915 -11.637 1.00 61.72  ? 66  ARG D CB  1 
ATOM   13276 C CG  . ARG D 1 66  ? 38.796  -21.962 -10.579 1.00 61.71  ? 66  ARG D CG  1 
ATOM   13277 C CD  . ARG D 1 66  ? 37.540  -22.428 -9.830  1.00 61.70  ? 66  ARG D CD  1 
ATOM   13278 N NE  . ARG D 1 66  ? 37.847  -22.972 -8.500  1.00 60.84  ? 66  ARG D NE  1 
ATOM   13279 C CZ  . ARG D 1 66  ? 37.618  -24.203 -8.100  1.00 60.65  ? 66  ARG D CZ  1 
ATOM   13280 N NH1 . ARG D 1 66  ? 37.251  -25.128 -8.971  1.00 61.14  ? 66  ARG D NH1 1 
ATOM   13281 N NH2 . ARG D 1 66  ? 37.805  -24.502 -6.830  1.00 60.54  ? 66  ARG D NH2 1 
ATOM   13282 N N   . THR D 1 67  ? 36.261  -23.363 -12.990 1.00 60.96  ? 67  THR D N   1 
ATOM   13283 C CA  . THR D 1 67  ? 34.983  -24.054 -12.943 1.00 60.82  ? 67  THR D CA  1 
ATOM   13284 C C   . THR D 1 67  ? 35.150  -25.319 -12.105 1.00 60.33  ? 67  THR D C   1 
ATOM   13285 O O   . THR D 1 67  ? 36.283  -25.757 -11.931 1.00 59.79  ? 67  THR D O   1 
ATOM   13286 C CB  . THR D 1 67  ? 34.502  -24.342 -14.368 1.00 61.67  ? 67  THR D CB  1 
ATOM   13287 O OG1 . THR D 1 67  ? 35.141  -25.501 -14.890 1.00 62.07  ? 67  THR D OG1 1 
ATOM   13288 C CG2 . THR D 1 67  ? 34.734  -23.160 -15.295 1.00 61.75  ? 67  THR D CG2 1 
ATOM   13289 N N   . TRP D 1 68  ? 34.026  -25.889 -11.605 1.00 59.88  ? 68  TRP D N   1 
ATOM   13290 C CA  . TRP D 1 68  ? 34.075  -27.067 -10.742 1.00 59.19  ? 68  TRP D CA  1 
ATOM   13291 C C   . TRP D 1 68  ? 33.633  -28.338 -11.454 1.00 59.94  ? 68  TRP D C   1 
ATOM   13292 O O   . TRP D 1 68  ? 33.683  -29.416 -10.860 1.00 60.56  ? 68  TRP D O   1 
ATOM   13293 C CB  . TRP D 1 68  ? 33.232  -26.864 -9.489  1.00 58.13  ? 68  TRP D CB  1 
ATOM   13294 C CG  . TRP D 1 68  ? 33.788  -25.815 -8.578  1.00 57.11  ? 68  TRP D CG  1 
ATOM   13295 C CD1 . TRP D 1 68  ? 34.497  -26.003 -7.432  1.00 56.66  ? 68  TRP D CD1 1 
ATOM   13296 C CD2 . TRP D 1 68  ? 33.609  -24.393 -8.727  1.00 57.21  ? 68  TRP D CD2 1 
ATOM   13297 N NE1 . TRP D 1 68  ? 34.819  -24.798 -6.870  1.00 56.43  ? 68  TRP D NE1 1 
ATOM   13298 C CE2 . TRP D 1 68  ? 34.279  -23.785 -7.635  1.00 56.66  ? 68  TRP D CE2 1 
ATOM   13299 C CE3 . TRP D 1 68  ? 32.949  -23.582 -9.666  1.00 57.20  ? 68  TRP D CE3 1 
ATOM   13300 C CZ2 . TRP D 1 68  ? 34.283  -22.403 -7.455  1.00 55.19  ? 68  TRP D CZ2 1 
ATOM   13301 C CZ3 . TRP D 1 68  ? 32.979  -22.218 -9.495  1.00 56.14  ? 68  TRP D CZ3 1 
ATOM   13302 C CH2 . TRP D 1 68  ? 33.625  -21.651 -8.399  1.00 55.37  ? 68  TRP D CH2 1 
ATOM   13303 N N   . SER D 1 69  ? 33.309  -28.208 -12.740 1.00 60.40  ? 69  SER D N   1 
ATOM   13304 C CA  . SER D 1 69  ? 32.618  -29.236 -13.485 1.00 61.55  ? 69  SER D CA  1 
ATOM   13305 C C   . SER D 1 69  ? 32.818  -29.010 -14.980 1.00 62.91  ? 69  SER D C   1 
ATOM   13306 O O   . SER D 1 69  ? 32.761  -27.882 -15.448 1.00 63.11  ? 69  SER D O   1 
ATOM   13307 C CB  . SER D 1 69  ? 31.163  -29.258 -13.119 1.00 61.43  ? 69  SER D CB  1 
ATOM   13308 O OG  . SER D 1 69  ? 30.399  -29.739 -14.213 1.00 62.30  ? 69  SER D OG  1 
ATOM   13309 N N   . GLN D 1 70  ? 32.991  -30.114 -15.717 1.00 65.10  ? 70  GLN D N   1 
ATOM   13310 C CA  . GLN D 1 70  ? 33.491  -30.132 -17.087 1.00 66.74  ? 70  GLN D CA  1 
ATOM   13311 C C   . GLN D 1 70  ? 32.529  -29.424 -18.035 1.00 67.40  ? 70  GLN D C   1 
ATOM   13312 O O   . GLN D 1 70  ? 31.324  -29.603 -17.931 1.00 68.17  ? 70  GLN D O   1 
ATOM   13313 C CB  . GLN D 1 70  ? 33.753  -31.554 -17.607 1.00 68.03  ? 70  GLN D CB  1 
ATOM   13314 C CG  . GLN D 1 70  ? 32.662  -32.575 -17.298 1.00 68.53  ? 70  GLN D CG  1 
ATOM   13315 C CD  . GLN D 1 70  ? 32.885  -33.289 -15.987 1.00 68.31  ? 70  GLN D CD  1 
ATOM   13316 O OE1 . GLN D 1 70  ? 33.335  -32.668 -15.014 1.00 67.44  ? 70  GLN D OE1 1 
ATOM   13317 N NE2 . GLN D 1 70  ? 32.597  -34.589 -15.959 1.00 68.93  ? 70  GLN D NE2 1 
ATOM   13318 N N   . TYR D 1 71  ? 33.089  -28.653 -18.976 1.00 68.38  ? 71  TYR D N   1 
ATOM   13319 C CA  . TYR D 1 71  ? 32.298  -27.982 -19.995 1.00 69.92  ? 71  TYR D CA  1 
ATOM   13320 C C   . TYR D 1 71  ? 32.050  -28.949 -21.156 1.00 70.81  ? 71  TYR D C   1 
ATOM   13321 O O   . TYR D 1 71  ? 32.768  -29.935 -21.318 1.00 70.52  ? 71  TYR D O   1 
ATOM   13322 C CB  . TYR D 1 71  ? 32.980  -26.668 -20.409 1.00 70.62  ? 71  TYR D CB  1 
ATOM   13323 C CG  . TYR D 1 71  ? 32.726  -25.433 -19.535 1.00 70.32  ? 71  TYR D CG  1 
ATOM   13324 C CD1 . TYR D 1 71  ? 31.565  -25.283 -18.761 1.00 70.21  ? 71  TYR D CD1 1 
ATOM   13325 C CD2 . TYR D 1 71  ? 33.620  -24.370 -19.544 1.00 70.02  ? 71  TYR D CD2 1 
ATOM   13326 C CE1 . TYR D 1 71  ? 31.332  -24.155 -17.987 1.00 68.83  ? 71  TYR D CE1 1 
ATOM   13327 C CE2 . TYR D 1 71  ? 33.404  -23.232 -18.779 1.00 69.56  ? 71  TYR D CE2 1 
ATOM   13328 C CZ  . TYR D 1 71  ? 32.260  -23.129 -18.000 1.00 69.61  ? 71  TYR D CZ  1 
ATOM   13329 O OH  . TYR D 1 71  ? 32.077  -22.019 -17.234 1.00 69.59  ? 71  TYR D OH  1 
ATOM   13330 N N   . SER D 1 72  ? 30.997  -28.682 -21.942 1.00 70.94  ? 72  SER D N   1 
ATOM   13331 C CA  . SER D 1 72  ? 30.804  -29.394 -23.194 1.00 71.83  ? 72  SER D CA  1 
ATOM   13332 C C   . SER D 1 72  ? 31.705  -28.765 -24.250 1.00 71.84  ? 72  SER D C   1 
ATOM   13333 O O   . SER D 1 72  ? 32.221  -27.673 -24.053 1.00 70.72  ? 72  SER D O   1 
ATOM   13334 C CB  . SER D 1 72  ? 29.366  -29.378 -23.638 1.00 72.38  ? 72  SER D CB  1 
ATOM   13335 O OG  . SER D 1 72  ? 29.009  -28.089 -24.107 1.00 72.46  ? 72  SER D OG  1 
ATOM   13336 N N   . GLU D 1 73  ? 31.882  -29.465 -25.371 1.00 73.19  ? 73  GLU D N   1 
ATOM   13337 C CA  . GLU D 1 73  ? 32.697  -28.969 -26.468 1.00 74.26  ? 73  GLU D CA  1 
ATOM   13338 C C   . GLU D 1 73  ? 32.153  -27.635 -26.967 1.00 74.53  ? 73  GLU D C   1 
ATOM   13339 O O   . GLU D 1 73  ? 32.938  -26.714 -27.190 1.00 75.24  ? 73  GLU D O   1 
ATOM   13340 C CB  . GLU D 1 73  ? 32.816  -29.974 -27.615 1.00 75.95  ? 73  GLU D CB  1 
ATOM   13341 C CG  . GLU D 1 73  ? 33.728  -29.492 -28.740 1.00 77.18  ? 73  GLU D CG  1 
ATOM   13342 C CD  . GLU D 1 73  ? 34.138  -30.575 -29.717 1.00 79.11  ? 73  GLU D CD  1 
ATOM   13343 O OE1 . GLU D 1 73  ? 33.533  -31.677 -29.722 1.00 79.96  ? 73  GLU D OE1 1 
ATOM   13344 O OE2 . GLU D 1 73  ? 35.094  -30.308 -30.472 1.00 80.23  ? 73  GLU D OE2 1 
ATOM   13345 N N   . ASN D 1 74  ? 30.826  -27.576 -27.142 1.00 74.89  ? 74  ASN D N   1 
ATOM   13346 C CA  . ASN D 1 74  ? 30.102  -26.384 -27.540 1.00 75.25  ? 74  ASN D CA  1 
ATOM   13347 C C   . ASN D 1 74  ? 30.398  -25.254 -26.569 1.00 74.17  ? 74  ASN D C   1 
ATOM   13348 O O   . ASN D 1 74  ? 30.674  -24.152 -27.018 1.00 74.91  ? 74  ASN D O   1 
ATOM   13349 C CB  . ASN D 1 74  ? 28.591  -26.593 -27.540 1.00 75.98  ? 74  ASN D CB  1 
ATOM   13350 C CG  . ASN D 1 74  ? 28.013  -27.127 -28.835 1.00 77.93  ? 74  ASN D CG  1 
ATOM   13351 O OD1 . ASN D 1 74  ? 28.721  -27.407 -29.813 1.00 79.20  ? 74  ASN D OD1 1 
ATOM   13352 N ND2 . ASN D 1 74  ? 26.696  -27.260 -28.853 1.00 78.38  ? 74  ASN D ND2 1 
ATOM   13353 N N   . GLN D 1 75  ? 30.321  -25.514 -25.255 1.00 73.31  ? 75  GLN D N   1 
ATOM   13354 C CA  . GLN D 1 75  ? 30.668  -24.505 -24.257 1.00 72.80  ? 75  GLN D CA  1 
ATOM   13355 C C   . GLN D 1 75  ? 32.152  -24.148 -24.348 1.00 72.94  ? 75  GLN D C   1 
ATOM   13356 O O   . GLN D 1 75  ? 32.546  -23.004 -24.188 1.00 73.13  ? 75  GLN D O   1 
ATOM   13357 C CB  . GLN D 1 75  ? 30.353  -24.915 -22.816 1.00 71.87  ? 75  GLN D CB  1 
ATOM   13358 C CG  . GLN D 1 75  ? 28.865  -25.100 -22.523 1.00 72.51  ? 75  GLN D CG  1 
ATOM   13359 C CD  . GLN D 1 75  ? 28.591  -25.887 -21.255 1.00 72.02  ? 75  GLN D CD  1 
ATOM   13360 O OE1 . GLN D 1 75  ? 29.216  -26.936 -21.013 1.00 73.96  ? 75  GLN D OE1 1 
ATOM   13361 N NE2 . GLN D 1 75  ? 27.647  -25.410 -20.448 1.00 70.25  ? 75  GLN D NE2 1 
ATOM   13362 N N   . LEU D 1 76  ? 32.997  -25.126 -24.617 1.00 75.04  ? 76  LEU D N   1 
ATOM   13363 C CA  . LEU D 1 76  ? 34.401  -24.827 -24.778 1.00 77.10  ? 76  LEU D CA  1 
ATOM   13364 C C   . LEU D 1 76  ? 34.570  -23.856 -25.937 1.00 79.10  ? 76  LEU D C   1 
ATOM   13365 O O   . LEU D 1 76  ? 35.359  -22.915 -25.838 1.00 80.33  ? 76  LEU D O   1 
ATOM   13366 C CB  . LEU D 1 76  ? 35.215  -26.103 -24.963 1.00 78.31  ? 76  LEU D CB  1 
ATOM   13367 C CG  . LEU D 1 76  ? 35.715  -26.721 -23.657 1.00 77.42  ? 76  LEU D CG  1 
ATOM   13368 C CD1 . LEU D 1 76  ? 36.498  -27.997 -23.926 1.00 78.56  ? 76  LEU D CD1 1 
ATOM   13369 C CD2 . LEU D 1 76  ? 36.561  -25.691 -22.911 1.00 75.73  ? 76  LEU D CD2 1 
ATOM   13370 N N   . LYS D 1 77  ? 33.807  -24.073 -27.018 1.00 79.44  ? 77  LYS D N   1 
ATOM   13371 C CA  . LYS D 1 77  ? 34.017  -23.292 -28.229 1.00 80.46  ? 77  LYS D CA  1 
ATOM   13372 C C   . LYS D 1 77  ? 33.862  -21.802 -27.923 1.00 78.36  ? 77  LYS D C   1 
ATOM   13373 O O   . LYS D 1 77  ? 34.546  -20.955 -28.500 1.00 78.04  ? 77  LYS D O   1 
ATOM   13374 C CB  . LYS D 1 77  ? 33.108  -23.784 -29.358 1.00 82.15  ? 77  LYS D CB  1 
ATOM   13375 C CG  . LYS D 1 77  ? 33.649  -25.013 -30.069 1.00 83.80  ? 77  LYS D CG  1 
ATOM   13376 C CD  . LYS D 1 77  ? 32.772  -25.501 -31.215 1.00 86.24  ? 77  LYS D CD  1 
ATOM   13377 C CE  . LYS D 1 77  ? 33.391  -26.690 -31.874 1.00 87.68  ? 77  LYS D CE  1 
ATOM   13378 N NZ  . LYS D 1 77  ? 32.613  -27.129 -33.030 1.00 89.97  ? 77  LYS D NZ  1 
ATOM   13379 N N   . LEU D 1 78  ? 32.964  -21.525 -26.981 1.00 76.32  ? 78  LEU D N   1 
ATOM   13380 C CA  . LEU D 1 78  ? 32.584  -20.178 -26.638 1.00 75.55  ? 78  LEU D CA  1 
ATOM   13381 C C   . LEU D 1 78  ? 33.692  -19.558 -25.810 1.00 74.37  ? 78  LEU D C   1 
ATOM   13382 O O   . LEU D 1 78  ? 34.055  -18.405 -26.021 1.00 74.51  ? 78  LEU D O   1 
ATOM   13383 C CB  . LEU D 1 78  ? 31.285  -20.239 -25.851 1.00 74.95  ? 78  LEU D CB  1 
ATOM   13384 C CG  . LEU D 1 78  ? 30.524  -18.921 -25.711 1.00 74.96  ? 78  LEU D CG  1 
ATOM   13385 C CD1 . LEU D 1 78  ? 30.116  -18.403 -27.078 1.00 77.13  ? 78  LEU D CD1 1 
ATOM   13386 C CD2 . LEU D 1 78  ? 29.311  -19.148 -24.826 1.00 74.23  ? 78  LEU D CD2 1 
ATOM   13387 N N   . VAL D 1 79  ? 34.230  -20.335 -24.868 1.00 73.00  ? 79  VAL D N   1 
ATOM   13388 C CA  . VAL D 1 79  ? 35.342  -19.835 -24.078 1.00 71.10  ? 79  VAL D CA  1 
ATOM   13389 C C   . VAL D 1 79  ? 36.499  -19.558 -25.034 1.00 71.98  ? 79  VAL D C   1 
ATOM   13390 O O   . VAL D 1 79  ? 37.071  -18.469 -25.002 1.00 71.93  ? 79  VAL D O   1 
ATOM   13391 C CB  . VAL D 1 79  ? 35.778  -20.735 -22.911 1.00 69.24  ? 79  VAL D CB  1 
ATOM   13392 C CG1 . VAL D 1 79  ? 36.892  -20.081 -22.110 1.00 68.12  ? 79  VAL D CG1 1 
ATOM   13393 C CG2 . VAL D 1 79  ? 34.616  -21.076 -21.987 1.00 68.41  ? 79  VAL D CG2 1 
ATOM   13394 N N   . GLN D 1 80  ? 36.786  -20.507 -25.933 1.00 73.03  ? 80  GLN D N   1 
ATOM   13395 C CA  . GLN D 1 80  ? 37.857  -20.321 -26.897 1.00 74.71  ? 80  GLN D CA  1 
ATOM   13396 C C   . GLN D 1 80  ? 37.744  -18.937 -27.553 1.00 75.55  ? 80  GLN D C   1 
ATOM   13397 O O   . GLN D 1 80  ? 38.681  -18.113 -27.507 1.00 75.34  ? 80  GLN D O   1 
ATOM   13398 C CB  . GLN D 1 80  ? 37.870  -21.411 -27.967 1.00 76.47  ? 80  GLN D CB  1 
ATOM   13399 C CG  . GLN D 1 80  ? 39.213  -21.516 -28.688 1.00 78.19  ? 80  GLN D CG  1 
ATOM   13400 C CD  . GLN D 1 80  ? 40.345  -21.980 -27.791 1.00 78.08  ? 80  GLN D CD  1 
ATOM   13401 O OE1 . GLN D 1 80  ? 40.134  -22.520 -26.700 1.00 77.33  ? 80  GLN D OE1 1 
ATOM   13402 N NE2 . GLN D 1 80  ? 41.580  -21.793 -28.235 1.00 79.67  ? 80  GLN D NE2 1 
ATOM   13403 N N   . GLU D 1 81  ? 36.579  -18.687 -28.161 1.00 75.29  ? 81  GLU D N   1 
ATOM   13404 C CA  . GLU D 1 81  ? 36.383  -17.504 -28.977 1.00 76.16  ? 81  GLU D CA  1 
ATOM   13405 C C   . GLU D 1 81  ? 36.377  -16.241 -28.115 1.00 73.45  ? 81  GLU D C   1 
ATOM   13406 O O   . GLU D 1 81  ? 36.478  -15.145 -28.642 1.00 73.27  ? 81  GLU D O   1 
ATOM   13407 C CB  . GLU D 1 81  ? 35.075  -17.699 -29.744 1.00 78.48  ? 81  GLU D CB  1 
ATOM   13408 C CG  . GLU D 1 81  ? 34.532  -16.445 -30.436 1.00 80.80  ? 81  GLU D CG  1 
ATOM   13409 C CD  . GLU D 1 81  ? 33.029  -16.500 -30.718 1.00 82.64  ? 81  GLU D CD  1 
ATOM   13410 O OE1 . GLU D 1 81  ? 32.412  -17.579 -30.508 1.00 83.54  ? 81  GLU D OE1 1 
ATOM   13411 O OE2 . GLU D 1 81  ? 32.457  -15.464 -31.137 1.00 83.89  ? 81  GLU D OE2 1 
ATOM   13412 N N   . SER D 1 82  ? 36.217  -16.398 -26.800 1.00 70.97  ? 82  SER D N   1 
ATOM   13413 C CA  . SER D 1 82  ? 35.905  -15.275 -25.937 1.00 69.77  ? 82  SER D CA  1 
ATOM   13414 C C   . SER D 1 82  ? 37.188  -14.554 -25.553 1.00 69.36  ? 82  SER D C   1 
ATOM   13415 O O   . SER D 1 82  ? 37.134  -13.398 -25.142 1.00 68.40  ? 82  SER D O   1 
ATOM   13416 C CB  . SER D 1 82  ? 35.156  -15.714 -24.703 1.00 68.09  ? 82  SER D CB  1 
ATOM   13417 O OG  . SER D 1 82  ? 36.025  -16.387 -23.802 1.00 66.86  ? 82  SER D OG  1 
ATOM   13418 N N   . GLY D 1 83  ? 38.315  -15.278 -25.673 1.00 69.96  ? 83  GLY D N   1 
ATOM   13419 C CA  . GLY D 1 83  ? 39.652  -14.799 -25.342 1.00 69.67  ? 83  GLY D CA  1 
ATOM   13420 C C   . GLY D 1 83  ? 40.085  -15.230 -23.936 1.00 68.25  ? 83  GLY D C   1 
ATOM   13421 O O   . GLY D 1 83  ? 41.254  -15.090 -23.568 1.00 67.32  ? 83  GLY D O   1 
ATOM   13422 N N   . LEU D 1 84  ? 39.117  -15.729 -23.146 1.00 67.90  ? 84  LEU D N   1 
ATOM   13423 C CA  . LEU D 1 84  ? 39.331  -16.021 -21.736 1.00 66.89  ? 84  LEU D CA  1 
ATOM   13424 C C   . LEU D 1 84  ? 40.116  -17.323 -21.584 1.00 67.80  ? 84  LEU D C   1 
ATOM   13425 O O   . LEU D 1 84  ? 40.180  -18.116 -22.523 1.00 68.79  ? 84  LEU D O   1 
ATOM   13426 C CB  . LEU D 1 84  ? 37.987  -16.070 -21.014 1.00 65.48  ? 84  LEU D CB  1 
ATOM   13427 C CG  . LEU D 1 84  ? 37.315  -14.725 -20.724 1.00 65.03  ? 84  LEU D CG  1 
ATOM   13428 C CD1 . LEU D 1 84  ? 35.893  -14.986 -20.234 1.00 64.79  ? 84  LEU D CD1 1 
ATOM   13429 C CD2 . LEU D 1 84  ? 38.058  -13.905 -19.689 1.00 63.76  ? 84  LEU D CD2 1 
ATOM   13430 N N   . LYS D 1 85  ? 40.744  -17.495 -20.411 1.00 68.08  ? 85  LYS D N   1 
ATOM   13431 C CA  . LYS D 1 85  ? 41.474  -18.710 -20.087 1.00 70.12  ? 85  LYS D CA  1 
ATOM   13432 C C   . LYS D 1 85  ? 40.659  -19.488 -19.063 1.00 71.29  ? 85  LYS D C   1 
ATOM   13433 O O   . LYS D 1 85  ? 39.928  -18.883 -18.277 1.00 73.24  ? 85  LYS D O   1 
ATOM   13434 C CB  . LYS D 1 85  ? 42.884  -18.506 -19.519 1.00 70.18  ? 85  LYS D CB  1 
ATOM   13435 C CG  . LYS D 1 85  ? 43.837  -17.692 -20.373 1.00 71.60  ? 85  LYS D CG  1 
ATOM   13436 C CD  . LYS D 1 85  ? 44.057  -18.148 -21.812 1.00 73.54  ? 85  LYS D CD  1 
ATOM   13437 C CE  . LYS D 1 85  ? 45.017  -17.203 -22.490 1.00 75.29  ? 85  LYS D CE  1 
ATOM   13438 N NZ  . LYS D 1 85  ? 45.111  -17.431 -23.933 1.00 77.65  ? 85  LYS D NZ  1 
ATOM   13439 N N   . LEU D 1 86  ? 40.802  -20.824 -19.090 1.00 71.87  ? 86  LEU D N   1 
ATOM   13440 C CA  . LEU D 1 86  ? 39.922  -21.732 -18.369 1.00 70.52  ? 86  LEU D CA  1 
ATOM   13441 C C   . LEU D 1 86  ? 40.757  -22.714 -17.555 1.00 70.23  ? 86  LEU D C   1 
ATOM   13442 O O   . LEU D 1 86  ? 41.592  -23.445 -18.085 1.00 69.82  ? 86  LEU D O   1 
ATOM   13443 C CB  . LEU D 1 86  ? 39.029  -22.470 -19.365 1.00 71.54  ? 86  LEU D CB  1 
ATOM   13444 C CG  . LEU D 1 86  ? 38.298  -23.730 -18.871 1.00 70.72  ? 86  LEU D CG  1 
ATOM   13445 C CD1 . LEU D 1 86  ? 37.473  -23.479 -17.624 1.00 69.56  ? 86  LEU D CD1 1 
ATOM   13446 C CD2 . LEU D 1 86  ? 37.414  -24.286 -19.981 1.00 70.88  ? 86  LEU D CD2 1 
ATOM   13447 N N   . ILE D 1 87  ? 40.508  -22.697 -16.248 1.00 69.47  ? 87  ILE D N   1 
ATOM   13448 C CA  . ILE D 1 87  ? 40.889  -23.775 -15.361 1.00 68.90  ? 87  ILE D CA  1 
ATOM   13449 C C   . ILE D 1 87  ? 39.628  -24.623 -15.166 1.00 69.59  ? 87  ILE D C   1 
ATOM   13450 O O   . ILE D 1 87  ? 38.684  -24.171 -14.523 1.00 72.13  ? 87  ILE D O   1 
ATOM   13451 C CB  . ILE D 1 87  ? 41.419  -23.186 -14.039 1.00 67.38  ? 87  ILE D CB  1 
ATOM   13452 C CG1 . ILE D 1 87  ? 42.599  -22.244 -14.251 1.00 66.21  ? 87  ILE D CG1 1 
ATOM   13453 C CG2 . ILE D 1 87  ? 41.752  -24.282 -13.027 1.00 67.55  ? 87  ILE D CG2 1 
ATOM   13454 C CD1 . ILE D 1 87  ? 43.023  -21.523 -12.985 1.00 65.04  ? 87  ILE D CD1 1 
ATOM   13455 N N   . MET D 1 88  ? 39.585  -25.813 -15.778 1.00 68.93  ? 88  MET D N   1 
ATOM   13456 C CA  . MET D 1 88  ? 38.369  -26.603 -15.847 1.00 68.24  ? 88  MET D CA  1 
ATOM   13457 C C   . MET D 1 88  ? 38.378  -27.632 -14.735 1.00 67.94  ? 88  MET D C   1 
ATOM   13458 O O   . MET D 1 88  ? 39.331  -28.392 -14.613 1.00 67.00  ? 88  MET D O   1 
ATOM   13459 C CB  . MET D 1 88  ? 38.250  -27.365 -17.166 1.00 68.73  ? 88  MET D CB  1 
ATOM   13460 C CG  . MET D 1 88  ? 36.947  -28.104 -17.318 1.00 68.57  ? 88  MET D CG  1 
ATOM   13461 S SD  . MET D 1 88  ? 36.967  -28.917 -18.925 1.00 70.66  ? 88  MET D SD  1 
ATOM   13462 C CE  . MET D 1 88  ? 36.373  -27.579 -19.958 1.00 71.35  ? 88  MET D CE  1 
ATOM   13463 N N   . GLY D 1 89  ? 37.293  -27.653 -13.956 1.00 68.37  ? 89  GLY D N   1 
ATOM   13464 C CA  . GLY D 1 89  ? 37.138  -28.645 -12.904 1.00 69.26  ? 89  GLY D CA  1 
ATOM   13465 C C   . GLY D 1 89  ? 36.559  -29.948 -13.459 1.00 70.40  ? 89  GLY D C   1 
ATOM   13466 O O   . GLY D 1 89  ? 35.749  -29.931 -14.390 1.00 71.15  ? 89  GLY D O   1 
ATOM   13467 N N   . ILE D 1 90  ? 36.975  -31.077 -12.886 1.00 69.52  ? 90  ILE D N   1 
ATOM   13468 C CA  . ILE D 1 90  ? 36.325  -32.327 -13.229 1.00 71.34  ? 90  ILE D CA  1 
ATOM   13469 C C   . ILE D 1 90  ? 35.458  -32.748 -12.042 1.00 73.25  ? 90  ILE D C   1 
ATOM   13470 O O   . ILE D 1 90  ? 35.954  -32.904 -10.935 1.00 75.33  ? 90  ILE D O   1 
ATOM   13471 C CB  . ILE D 1 90  ? 37.332  -33.417 -13.638 1.00 69.70  ? 90  ILE D CB  1 
ATOM   13472 C CG1 . ILE D 1 90  ? 38.524  -32.871 -14.436 1.00 68.77  ? 90  ILE D CG1 1 
ATOM   13473 C CG2 . ILE D 1 90  ? 36.593  -34.505 -14.410 1.00 69.94  ? 90  ILE D CG2 1 
ATOM   13474 C CD1 . ILE D 1 90  ? 38.213  -32.478 -15.869 1.00 69.14  ? 90  ILE D CD1 1 
ATOM   13475 N N   . ASP D 1 91  ? 34.149  -32.906 -12.276 1.00 75.59  ? 91  ASP D N   1 
ATOM   13476 C CA  . ASP D 1 91  ? 33.210  -33.354 -11.250 1.00 75.28  ? 91  ASP D CA  1 
ATOM   13477 C C   . ASP D 1 91  ? 33.384  -34.856 -11.016 1.00 74.28  ? 91  ASP D C   1 
ATOM   13478 O O   . ASP D 1 91  ? 32.681  -35.666 -11.615 1.00 73.52  ? 91  ASP D O   1 
ATOM   13479 C CB  . ASP D 1 91  ? 31.772  -33.023 -11.616 1.00 75.61  ? 91  ASP D CB  1 
ATOM   13480 C CG  . ASP D 1 91  ? 30.702  -33.619 -10.713 1.00 75.73  ? 91  ASP D CG  1 
ATOM   13481 O OD1 . ASP D 1 91  ? 31.037  -33.941 -9.557  1.00 75.56  ? 91  ASP D OD1 1 
ATOM   13482 O OD2 . ASP D 1 91  ? 29.551  -33.757 -11.184 1.00 74.21  ? 91  ASP D OD2 1 
ATOM   13483 N N   . ILE D 1 92  ? 34.395  -35.176 -10.201 1.00 73.99  ? 92  ILE D N   1 
ATOM   13484 C CA  . ILE D 1 92  ? 34.530  -36.434 -9.492  1.00 75.45  ? 92  ILE D CA  1 
ATOM   13485 C C   . ILE D 1 92  ? 33.883  -36.206 -8.134  1.00 75.07  ? 92  ILE D C   1 
ATOM   13486 O O   . ILE D 1 92  ? 34.247  -35.279 -7.430  1.00 74.13  ? 92  ILE D O   1 
ATOM   13487 C CB  . ILE D 1 92  ? 36.022  -36.813 -9.363  1.00 77.18  ? 92  ILE D CB  1 
ATOM   13488 C CG1 . ILE D 1 92  ? 36.522  -37.613 -10.564 1.00 78.24  ? 92  ILE D CG1 1 
ATOM   13489 C CG2 . ILE D 1 92  ? 36.309  -37.558 -8.058  1.00 78.20  ? 92  ILE D CG2 1 
ATOM   13490 C CD1 . ILE D 1 92  ? 36.755  -36.781 -11.804 1.00 78.29  ? 92  ILE D CD1 1 
ATOM   13491 N N   . LYS D 1 93  ? 32.913  -37.027 -7.757  1.00 77.45  ? 93  LYS D N   1 
ATOM   13492 C CA  . LYS D 1 93  ? 32.141  -36.717 -6.565  1.00 76.83  ? 93  LYS D CA  1 
ATOM   13493 C C   . LYS D 1 93  ? 33.027  -36.947 -5.339  1.00 74.86  ? 93  LYS D C   1 
ATOM   13494 O O   . LYS D 1 93  ? 33.546  -38.049 -5.166  1.00 77.99  ? 93  LYS D O   1 
ATOM   13495 C CB  . LYS D 1 93  ? 30.878  -37.581 -6.600  1.00 79.36  ? 93  LYS D CB  1 
ATOM   13496 C CG  . LYS D 1 93  ? 29.985  -37.384 -7.818  1.00 80.58  ? 93  LYS D CG  1 
ATOM   13497 C CD  . LYS D 1 93  ? 29.402  -35.978 -7.871  1.00 80.54  ? 93  LYS D CD  1 
ATOM   13498 C CE  . LYS D 1 93  ? 28.248  -35.826 -8.826  1.00 81.48  ? 93  LYS D CE  1 
ATOM   13499 N NZ  . LYS D 1 93  ? 27.467  -34.609 -8.578  1.00 79.77  ? 93  LYS D NZ  1 
ATOM   13500 N N   . PRO D 1 94  ? 33.261  -35.930 -4.477  1.00 71.27  ? 94  PRO D N   1 
ATOM   13501 C CA  . PRO D 1 94  ? 34.076  -36.084 -3.274  1.00 70.98  ? 94  PRO D CA  1 
ATOM   13502 C C   . PRO D 1 94  ? 33.610  -37.051 -2.202  1.00 72.45  ? 94  PRO D C   1 
ATOM   13503 O O   . PRO D 1 94  ? 34.428  -37.445 -1.368  1.00 72.92  ? 94  PRO D O   1 
ATOM   13504 C CB  . PRO D 1 94  ? 34.097  -34.664 -2.684  1.00 70.93  ? 94  PRO D CB  1 
ATOM   13505 C CG  . PRO D 1 94  ? 32.863  -34.004 -3.212  1.00 70.30  ? 94  PRO D CG  1 
ATOM   13506 C CD  . PRO D 1 94  ? 32.795  -34.546 -4.629  1.00 71.11  ? 94  PRO D CD  1 
ATOM   13507 N N   . GLU D 1 95  ? 32.309  -37.396 -2.225  1.00 73.41  ? 95  GLU D N   1 
ATOM   13508 C CA  . GLU D 1 95  ? 31.708  -38.262 -1.217  1.00 74.16  ? 95  GLU D CA  1 
ATOM   13509 C C   . GLU D 1 95  ? 31.766  -39.745 -1.605  1.00 73.87  ? 95  GLU D C   1 
ATOM   13510 O O   . GLU D 1 95  ? 31.561  -40.585 -0.745  1.00 74.25  ? 95  GLU D O   1 
ATOM   13511 C CB  . GLU D 1 95  ? 30.268  -37.830 -0.934  1.00 75.85  ? 95  GLU D CB  1 
ATOM   13512 C CG  . GLU D 1 95  ? 30.138  -36.693 0.075   1.00 77.95  ? 95  GLU D CG  1 
ATOM   13513 C CD  . GLU D 1 95  ? 28.714  -36.204 0.394   1.00 81.63  ? 95  GLU D CD  1 
ATOM   13514 O OE1 . GLU D 1 95  ? 27.887  -37.060 0.834   1.00 82.61  ? 95  GLU D OE1 1 
ATOM   13515 O OE2 . GLU D 1 95  ? 28.423  -34.964 0.224   1.00 81.12  ? 95  GLU D OE2 1 
ATOM   13516 N N   . GLU D 1 96  ? 32.015  -40.076 -2.878  1.00 73.76  ? 96  GLU D N   1 
ATOM   13517 C CA  . GLU D 1 96  ? 32.115  -41.460 -3.330  1.00 76.01  ? 96  GLU D CA  1 
ATOM   13518 C C   . GLU D 1 96  ? 33.351  -42.187 -2.789  1.00 76.47  ? 96  GLU D C   1 
ATOM   13519 O O   . GLU D 1 96  ? 34.339  -41.583 -2.357  1.00 76.33  ? 96  GLU D O   1 
ATOM   13520 C CB  . GLU D 1 96  ? 32.269  -41.511 -4.850  1.00 77.43  ? 96  GLU D CB  1 
ATOM   13521 C CG  . GLU D 1 96  ? 31.052  -40.978 -5.595  1.00 78.90  ? 96  GLU D CG  1 
ATOM   13522 C CD  . GLU D 1 96  ? 29.846  -41.901 -5.503  1.00 82.69  ? 96  GLU D CD  1 
ATOM   13523 O OE1 . GLU D 1 96  ? 29.982  -43.170 -5.479  1.00 84.78  ? 96  GLU D OE1 1 
ATOM   13524 O OE2 . GLU D 1 96  ? 28.745  -41.309 -5.481  1.00 82.09  ? 96  GLU D OE2 1 
ATOM   13525 N N   . ASP D 1 97  ? 33.318  -43.516 -2.886  1.00 77.57  ? 97  ASP D N   1 
ATOM   13526 C CA  . ASP D 1 97  ? 34.459  -44.339 -2.521  1.00 78.62  ? 97  ASP D CA  1 
ATOM   13527 C C   . ASP D 1 97  ? 35.471  -44.361 -3.665  1.00 77.76  ? 97  ASP D C   1 
ATOM   13528 O O   . ASP D 1 97  ? 35.208  -44.901 -4.731  1.00 76.76  ? 97  ASP D O   1 
ATOM   13529 C CB  . ASP D 1 97  ? 34.001  -45.730 -2.131  1.00 81.38  ? 97  ASP D CB  1 
ATOM   13530 C CG  . ASP D 1 97  ? 35.108  -46.719 -1.810  1.00 83.97  ? 97  ASP D CG  1 
ATOM   13531 O OD1 . ASP D 1 97  ? 36.297  -46.356 -2.046  1.00 85.13  ? 97  ASP D OD1 1 
ATOM   13532 O OD2 . ASP D 1 97  ? 34.767  -47.826 -1.325  1.00 83.23  ? 97  ASP D OD2 1 
ATOM   13533 N N   . TYR D 1 98  ? 36.650  -43.781 -3.429  1.00 77.83  ? 98  TYR D N   1 
ATOM   13534 C CA  . TYR D 1 98  ? 37.677  -43.715 -4.453  1.00 77.73  ? 98  TYR D CA  1 
ATOM   13535 C C   . TYR D 1 98  ? 38.189  -45.122 -4.750  1.00 80.58  ? 98  TYR D C   1 
ATOM   13536 O O   . TYR D 1 98  ? 38.787  -45.335 -5.802  1.00 83.45  ? 98  TYR D O   1 
ATOM   13537 C CB  . TYR D 1 98  ? 38.808  -42.785 -4.005  1.00 76.68  ? 98  TYR D CB  1 
ATOM   13538 C CG  . TYR D 1 98  ? 38.336  -41.440 -3.457  1.00 75.02  ? 98  TYR D CG  1 
ATOM   13539 C CD1 . TYR D 1 98  ? 37.239  -40.786 -4.016  1.00 74.91  ? 98  TYR D CD1 1 
ATOM   13540 C CD2 . TYR D 1 98  ? 38.963  -40.835 -2.367  1.00 73.35  ? 98  TYR D CD2 1 
ATOM   13541 C CE1 . TYR D 1 98  ? 36.779  -39.572 -3.523  1.00 73.11  ? 98  TYR D CE1 1 
ATOM   13542 C CE2 . TYR D 1 98  ? 38.504  -39.635 -1.849  1.00 72.08  ? 98  TYR D CE2 1 
ATOM   13543 C CZ  . TYR D 1 98  ? 37.417  -39.002 -2.434  1.00 71.98  ? 98  TYR D CZ  1 
ATOM   13544 O OH  . TYR D 1 98  ? 36.934  -37.827 -1.967  1.00 70.41  ? 98  TYR D OH  1 
ATOM   13545 N N   . GLY D 1 99  ? 37.964  -46.067 -3.818  1.00 80.87  ? 99  GLY D N   1 
ATOM   13546 C CA  . GLY D 1 99  ? 38.583  -47.383 -3.861  1.00 81.50  ? 99  GLY D CA  1 
ATOM   13547 C C   . GLY D 1 99  ? 37.689  -48.399 -4.571  1.00 83.16  ? 99  GLY D C   1 
ATOM   13548 O O   . GLY D 1 99  ? 38.038  -49.579 -4.734  1.00 83.48  ? 99  GLY D O   1 
ATOM   13549 N N   . ASP D 1 100 ? 36.510  -47.914 -4.964  1.00 82.14  ? 100 ASP D N   1 
ATOM   13550 C CA  . ASP D 1 100 ? 35.550  -48.720 -5.683  1.00 82.27  ? 100 ASP D CA  1 
ATOM   13551 C C   . ASP D 1 100 ? 35.996  -48.819 -7.134  1.00 83.02  ? 100 ASP D C   1 
ATOM   13552 O O   . ASP D 1 100 ? 36.011  -47.825 -7.848  1.00 82.06  ? 100 ASP D O   1 
ATOM   13553 C CB  . ASP D 1 100 ? 34.162  -48.119 -5.591  1.00 80.69  ? 100 ASP D CB  1 
ATOM   13554 C CG  . ASP D 1 100 ? 33.053  -49.059 -6.024  1.00 81.55  ? 100 ASP D CG  1 
ATOM   13555 O OD1 . ASP D 1 100 ? 33.337  -50.035 -6.746  1.00 81.24  ? 100 ASP D OD1 1 
ATOM   13556 O OD2 . ASP D 1 100 ? 31.930  -48.811 -5.597  1.00 81.78  ? 100 ASP D OD2 1 
ATOM   13557 N N   . PRO D 1 101 ? 36.356  -50.021 -7.626  1.00 85.54  ? 101 PRO D N   1 
ATOM   13558 C CA  . PRO D 1 101 ? 36.783  -50.178 -9.017  1.00 86.99  ? 101 PRO D CA  1 
ATOM   13559 C C   . PRO D 1 101 ? 35.785  -49.565 -9.993  1.00 88.25  ? 101 PRO D C   1 
ATOM   13560 O O   . PRO D 1 101 ? 36.167  -48.999 -11.014 1.00 90.28  ? 101 PRO D O   1 
ATOM   13561 C CB  . PRO D 1 101 ? 36.895  -51.693 -9.191  1.00 87.34  ? 101 PRO D CB  1 
ATOM   13562 C CG  . PRO D 1 101 ? 37.157  -52.208 -7.794  1.00 87.47  ? 101 PRO D CG  1 
ATOM   13563 C CD  . PRO D 1 101 ? 36.366  -51.288 -6.882  1.00 86.57  ? 101 PRO D CD  1 
ATOM   13564 N N   . GLU D 1 102 ? 34.501  -49.676 -9.658  1.00 88.50  ? 102 GLU D N   1 
ATOM   13565 C CA  . GLU D 1 102 ? 33.456  -49.185 -10.536 1.00 89.34  ? 102 GLU D CA  1 
ATOM   13566 C C   . GLU D 1 102 ? 33.579  -47.663 -10.657 1.00 85.00  ? 102 GLU D C   1 
ATOM   13567 O O   . GLU D 1 102 ? 33.430  -47.111 -11.748 1.00 83.86  ? 102 GLU D O   1 
ATOM   13568 C CB  . GLU D 1 102 ? 32.104  -49.686 -10.012 1.00 93.15  ? 102 GLU D CB  1 
ATOM   13569 C CG  . GLU D 1 102 ? 31.089  -50.018 -11.107 1.00 95.74  ? 102 GLU D CG  1 
ATOM   13570 C CD  . GLU D 1 102 ? 29.622  -49.832 -10.736 1.00 96.57  ? 102 GLU D CD  1 
ATOM   13571 O OE1 . GLU D 1 102 ? 29.066  -50.550 -9.874  1.00 97.89  ? 102 GLU D OE1 1 
ATOM   13572 O OE2 . GLU D 1 102 ? 29.018  -48.929 -11.349 1.00 97.11  ? 102 GLU D OE2 1 
ATOM   13573 N N   . PHE D 1 103 ? 33.859  -46.989 -9.531  1.00 82.30  ? 103 PHE D N   1 
ATOM   13574 C CA  . PHE D 1 103 ? 33.985  -45.537 -9.518  1.00 79.83  ? 103 PHE D CA  1 
ATOM   13575 C C   . PHE D 1 103 ? 35.210  -45.137 -10.332 1.00 78.68  ? 103 PHE D C   1 
ATOM   13576 O O   . PHE D 1 103 ? 35.156  -44.226 -11.148 1.00 77.58  ? 103 PHE D O   1 
ATOM   13577 C CB  . PHE D 1 103 ? 34.120  -44.908 -8.126  1.00 78.71  ? 103 PHE D CB  1 
ATOM   13578 C CG  . PHE D 1 103 ? 34.062  -43.384 -8.155  1.00 78.66  ? 103 PHE D CG  1 
ATOM   13579 C CD1 . PHE D 1 103 ? 33.022  -42.707 -8.788  1.00 78.21  ? 103 PHE D CD1 1 
ATOM   13580 C CD2 . PHE D 1 103 ? 35.085  -42.619 -7.606  1.00 78.87  ? 103 PHE D CD2 1 
ATOM   13581 C CE1 . PHE D 1 103 ? 33.011  -41.329 -8.869  1.00 76.42  ? 103 PHE D CE1 1 
ATOM   13582 C CE2 . PHE D 1 103 ? 35.056  -41.239 -7.685  1.00 76.62  ? 103 PHE D CE2 1 
ATOM   13583 C CZ  . PHE D 1 103 ? 34.015  -40.602 -8.308  1.00 76.00  ? 103 PHE D CZ  1 
ATOM   13584 N N   . VAL D 1 104 ? 36.318  -45.848 -10.129 1.00 78.72  ? 104 VAL D N   1 
ATOM   13585 C CA  . VAL D 1 104 ? 37.531  -45.547 -10.863 1.00 78.08  ? 104 VAL D CA  1 
ATOM   13586 C C   . VAL D 1 104 ? 37.231  -45.692 -12.352 1.00 78.95  ? 104 VAL D C   1 
ATOM   13587 O O   . VAL D 1 104 ? 37.627  -44.859 -13.156 1.00 80.11  ? 104 VAL D O   1 
ATOM   13588 C CB  . VAL D 1 104 ? 38.733  -46.411 -10.428 1.00 77.95  ? 104 VAL D CB  1 
ATOM   13589 C CG1 . VAL D 1 104 ? 39.980  -46.115 -11.255 1.00 77.63  ? 104 VAL D CG1 1 
ATOM   13590 C CG2 . VAL D 1 104 ? 39.045  -46.253 -8.942  1.00 77.05  ? 104 VAL D CG2 1 
ATOM   13591 N N   . LYS D 1 105 ? 36.497  -46.732 -12.719 1.00 79.94  ? 105 LYS D N   1 
ATOM   13592 C CA  . LYS D 1 105 ? 36.301  -47.024 -14.126 1.00 81.71  ? 105 LYS D CA  1 
ATOM   13593 C C   . LYS D 1 105 ? 35.405  -45.962 -14.766 1.00 79.84  ? 105 LYS D C   1 
ATOM   13594 O O   . LYS D 1 105 ? 35.666  -45.579 -15.896 1.00 80.16  ? 105 LYS D O   1 
ATOM   13595 C CB  . LYS D 1 105 ? 35.789  -48.461 -14.293 1.00 84.76  ? 105 LYS D CB  1 
ATOM   13596 C CG  . LYS D 1 105 ? 35.753  -49.012 -15.716 1.00 88.04  ? 105 LYS D CG  1 
ATOM   13597 C CD  . LYS D 1 105 ? 35.002  -50.343 -15.802 1.00 91.94  ? 105 LYS D CD  1 
ATOM   13598 C CE  . LYS D 1 105 ? 34.888  -50.970 -17.169 1.00 94.18  ? 105 LYS D CE  1 
ATOM   13599 N NZ  . LYS D 1 105 ? 34.129  -52.229 -17.160 1.00 95.37  ? 105 LYS D NZ  1 
ATOM   13600 N N   . ASP D 1 106 ? 34.353  -45.488 -14.085 1.00 78.17  ? 106 ASP D N   1 
ATOM   13601 C CA  . ASP D 1 106 ? 33.507  -44.463 -14.689 1.00 78.24  ? 106 ASP D CA  1 
ATOM   13602 C C   . ASP D 1 106 ? 34.274  -43.136 -14.794 1.00 76.02  ? 106 ASP D C   1 
ATOM   13603 O O   . ASP D 1 106 ? 34.058  -42.361 -15.732 1.00 75.97  ? 106 ASP D O   1 
ATOM   13604 C CB  . ASP D 1 106 ? 32.194  -44.234 -13.954 1.00 78.84  ? 106 ASP D CB  1 
ATOM   13605 C CG  . ASP D 1 106 ? 31.291  -45.446 -13.794 1.00 82.54  ? 106 ASP D CG  1 
ATOM   13606 O OD1 . ASP D 1 106 ? 31.240  -46.305 -14.711 1.00 84.27  ? 106 ASP D OD1 1 
ATOM   13607 O OD2 . ASP D 1 106 ? 30.613  -45.502 -12.756 1.00 85.96  ? 106 ASP D OD2 1 
ATOM   13608 N N   . SER D 1 107 ? 35.153  -42.880 -13.809 1.00 73.11  ? 107 SER D N   1 
ATOM   13609 C CA  . SER D 1 107 ? 35.962  -41.679 -13.758 1.00 70.41  ? 107 SER D CA  1 
ATOM   13610 C C   . SER D 1 107 ? 36.873  -41.635 -14.980 1.00 70.93  ? 107 SER D C   1 
ATOM   13611 O O   . SER D 1 107 ? 36.762  -40.746 -15.809 1.00 70.34  ? 107 SER D O   1 
ATOM   13612 C CB  . SER D 1 107 ? 36.724  -41.623 -12.472 1.00 69.15  ? 107 SER D CB  1 
ATOM   13613 O OG  . SER D 1 107 ? 35.890  -41.273 -11.377 1.00 67.95  ? 107 SER D OG  1 
ATOM   13614 N N   . GLU D 1 108 ? 37.739  -42.641 -15.120 1.00 72.33  ? 108 GLU D N   1 
ATOM   13615 C CA  . GLU D 1 108 ? 38.600  -42.771 -16.287 1.00 73.24  ? 108 GLU D CA  1 
ATOM   13616 C C   . GLU D 1 108 ? 37.810  -42.442 -17.557 1.00 73.53  ? 108 GLU D C   1 
ATOM   13617 O O   . GLU D 1 108 ? 38.257  -41.619 -18.351 1.00 73.20  ? 108 GLU D O   1 
ATOM   13618 C CB  . GLU D 1 108 ? 39.199  -44.179 -16.418 1.00 74.90  ? 108 GLU D CB  1 
ATOM   13619 C CG  . GLU D 1 108 ? 40.208  -44.567 -15.337 1.00 75.10  ? 108 GLU D CG  1 
ATOM   13620 C CD  . GLU D 1 108 ? 40.854  -45.941 -15.494 1.00 77.57  ? 108 GLU D CD  1 
ATOM   13621 O OE1 . GLU D 1 108 ? 40.428  -46.770 -16.348 1.00 80.15  ? 108 GLU D OE1 1 
ATOM   13622 O OE2 . GLU D 1 108 ? 41.817  -46.197 -14.741 1.00 77.63  ? 108 GLU D OE2 1 
ATOM   13623 N N   . ILE D 1 109 ? 36.647  -43.096 -17.730 1.00 73.98  ? 109 ILE D N   1 
ATOM   13624 C CA  . ILE D 1 109 ? 35.931  -43.134 -19.000 1.00 74.90  ? 109 ILE D CA  1 
ATOM   13625 C C   . ILE D 1 109 ? 35.395  -41.747 -19.302 1.00 73.78  ? 109 ILE D C   1 
ATOM   13626 O O   . ILE D 1 109 ? 35.349  -41.350 -20.461 1.00 74.71  ? 109 ILE D O   1 
ATOM   13627 C CB  . ILE D 1 109 ? 34.789  -44.180 -18.995 1.00 76.11  ? 109 ILE D CB  1 
ATOM   13628 C CG1 . ILE D 1 109 ? 35.342  -45.622 -19.080 1.00 77.17  ? 109 ILE D CG1 1 
ATOM   13629 C CG2 . ILE D 1 109 ? 33.778  -43.915 -20.115 1.00 76.70  ? 109 ILE D CG2 1 
ATOM   13630 C CD1 . ILE D 1 109 ? 34.376  -46.690 -18.608 1.00 77.60  ? 109 ILE D CD1 1 
ATOM   13631 N N   . GLU D 1 110 ? 34.975  -41.060 -18.238 1.00 72.20  ? 110 GLU D N   1 
ATOM   13632 C CA  . GLU D 1 110 ? 34.347  -39.752 -18.335 1.00 71.31  ? 110 GLU D CA  1 
ATOM   13633 C C   . GLU D 1 110 ? 35.420  -38.715 -18.636 1.00 70.98  ? 110 GLU D C   1 
ATOM   13634 O O   . GLU D 1 110 ? 35.206  -37.795 -19.421 1.00 71.29  ? 110 GLU D O   1 
ATOM   13635 C CB  . GLU D 1 110 ? 33.569  -39.479 -17.040 1.00 69.86  ? 110 GLU D CB  1 
ATOM   13636 C CG  . GLU D 1 110 ? 33.003  -38.072 -16.907 1.00 68.46  ? 110 GLU D CG  1 
ATOM   13637 C CD  . GLU D 1 110 ? 32.190  -37.552 -18.082 1.00 69.02  ? 110 GLU D CD  1 
ATOM   13638 O OE1 . GLU D 1 110 ? 31.798  -38.255 -19.035 1.00 69.56  ? 110 GLU D OE1 1 
ATOM   13639 O OE2 . GLU D 1 110 ? 31.982  -36.324 -18.036 1.00 68.94  ? 110 GLU D OE2 1 
ATOM   13640 N N   . LEU D 1 111 ? 36.584  -38.890 -18.006 1.00 70.75  ? 111 LEU D N   1 
ATOM   13641 C CA  . LEU D 1 111 ? 37.689  -37.969 -18.181 1.00 70.06  ? 111 LEU D CA  1 
ATOM   13642 C C   . LEU D 1 111 ? 38.235  -38.125 -19.590 1.00 71.33  ? 111 LEU D C   1 
ATOM   13643 O O   . LEU D 1 111 ? 38.448  -37.143 -20.288 1.00 71.57  ? 111 LEU D O   1 
ATOM   13644 C CB  . LEU D 1 111 ? 38.758  -38.217 -17.125 1.00 69.39  ? 111 LEU D CB  1 
ATOM   13645 C CG  . LEU D 1 111 ? 39.891  -37.192 -17.062 1.00 69.11  ? 111 LEU D CG  1 
ATOM   13646 C CD1 . LEU D 1 111 ? 39.503  -35.730 -17.251 1.00 68.08  ? 111 LEU D CD1 1 
ATOM   13647 C CD2 . LEU D 1 111 ? 40.552  -37.354 -15.705 1.00 68.87  ? 111 LEU D CD2 1 
ATOM   13648 N N   . LYS D 1 112 ? 38.430  -39.370 -20.016 1.00 72.80  ? 112 LYS D N   1 
ATOM   13649 C CA  . LYS D 1 112 ? 38.943  -39.608 -21.353 1.00 74.55  ? 112 LYS D CA  1 
ATOM   13650 C C   . LYS D 1 112 ? 37.947  -39.043 -22.358 1.00 75.60  ? 112 LYS D C   1 
ATOM   13651 O O   . LYS D 1 112 ? 38.349  -38.565 -23.420 1.00 76.87  ? 112 LYS D O   1 
ATOM   13652 C CB  . LYS D 1 112 ? 39.250  -41.084 -21.602 1.00 75.66  ? 112 LYS D CB  1 
ATOM   13653 C CG  . LYS D 1 112 ? 40.483  -41.592 -20.866 1.00 75.76  ? 112 LYS D CG  1 
ATOM   13654 C CD  . LYS D 1 112 ? 40.821  -43.063 -21.121 1.00 77.27  ? 112 LYS D CD  1 
ATOM   13655 C CE  . LYS D 1 112 ? 41.728  -43.701 -20.118 1.00 77.27  ? 112 LYS D CE  1 
ATOM   13656 N NZ  . LYS D 1 112 ? 41.805  -45.159 -20.312 1.00 79.10  ? 112 LYS D NZ  1 
ATOM   13657 N N   . ARG D 1 113 ? 36.655  -39.070 -21.997 1.00 75.34  ? 113 ARG D N   1 
ATOM   13658 C CA  . ARG D 1 113 ? 35.614  -38.693 -22.936 1.00 75.79  ? 113 ARG D CA  1 
ATOM   13659 C C   . ARG D 1 113 ? 35.739  -37.212 -23.219 1.00 75.18  ? 113 ARG D C   1 
ATOM   13660 O O   . ARG D 1 113 ? 35.712  -36.829 -24.384 1.00 75.67  ? 113 ARG D O   1 
ATOM   13661 C CB  . ARG D 1 113 ? 34.176  -38.933 -22.480 1.00 75.27  ? 113 ARG D CB  1 
ATOM   13662 C CG  . ARG D 1 113 ? 33.199  -38.511 -23.573 1.00 76.18  ? 113 ARG D CG  1 
ATOM   13663 C CD  . ARG D 1 113 ? 31.750  -38.725 -23.196 1.00 75.65  ? 113 ARG D CD  1 
ATOM   13664 N NE  . ARG D 1 113 ? 31.476  -37.994 -21.960 1.00 73.72  ? 113 ARG D NE  1 
ATOM   13665 C CZ  . ARG D 1 113 ? 31.320  -36.695 -21.926 1.00 73.44  ? 113 ARG D CZ  1 
ATOM   13666 N NH1 . ARG D 1 113 ? 31.327  -36.007 -23.053 1.00 74.59  ? 113 ARG D NH1 1 
ATOM   13667 N NH2 . ARG D 1 113 ? 31.140  -36.075 -20.776 1.00 72.10  ? 113 ARG D NH2 1 
ATOM   13668 N N   . VAL D 1 114 ? 35.829  -36.438 -22.127 1.00 74.61  ? 114 VAL D N   1 
ATOM   13669 C CA  . VAL D 1 114 ? 36.011  -34.992 -22.161 1.00 74.74  ? 114 VAL D CA  1 
ATOM   13670 C C   . VAL D 1 114 ? 37.296  -34.687 -22.917 1.00 76.25  ? 114 VAL D C   1 
ATOM   13671 O O   . VAL D 1 114 ? 37.282  -33.946 -23.898 1.00 77.21  ? 114 VAL D O   1 
ATOM   13672 C CB  . VAL D 1 114 ? 36.084  -34.395 -20.744 1.00 73.03  ? 114 VAL D CB  1 
ATOM   13673 C CG1 . VAL D 1 114 ? 36.635  -32.982 -20.734 1.00 72.30  ? 114 VAL D CG1 1 
ATOM   13674 C CG2 . VAL D 1 114 ? 34.736  -34.415 -20.048 1.00 73.05  ? 114 VAL D CG2 1 
ATOM   13675 N N   . LEU D 1 115 ? 38.388  -35.315 -22.454 1.00 76.86  ? 115 LEU D N   1 
ATOM   13676 C CA  . LEU D 1 115 ? 39.727  -35.049 -22.949 1.00 76.91  ? 115 LEU D CA  1 
ATOM   13677 C C   . LEU D 1 115 ? 39.766  -35.249 -24.454 1.00 77.94  ? 115 LEU D C   1 
ATOM   13678 O O   . LEU D 1 115 ? 40.642  -34.739 -25.126 1.00 79.27  ? 115 LEU D O   1 
ATOM   13679 C CB  . LEU D 1 115 ? 40.736  -35.956 -22.251 1.00 76.94  ? 115 LEU D CB  1 
ATOM   13680 C CG  . LEU D 1 115 ? 41.109  -35.559 -20.820 1.00 76.26  ? 115 LEU D CG  1 
ATOM   13681 C CD1 . LEU D 1 115 ? 42.200  -36.475 -20.302 1.00 77.21  ? 115 LEU D CD1 1 
ATOM   13682 C CD2 . LEU D 1 115 ? 41.579  -34.119 -20.713 1.00 76.04  ? 115 LEU D CD2 1 
ATOM   13683 N N   . ASN D 1 116 ? 38.807  -35.989 -24.988 1.00 78.09  ? 116 ASN D N   1 
ATOM   13684 C CA  . ASN D 1 116 ? 38.894  -36.369 -26.380 1.00 79.40  ? 116 ASN D CA  1 
ATOM   13685 C C   . ASN D 1 116 ? 38.618  -35.158 -27.270 1.00 78.26  ? 116 ASN D C   1 
ATOM   13686 O O   . ASN D 1 116 ? 39.068  -35.124 -28.409 1.00 79.23  ? 116 ASN D O   1 
ATOM   13687 C CB  . ASN D 1 116 ? 38.019  -37.587 -26.646 1.00 80.57  ? 116 ASN D CB  1 
ATOM   13688 C CG  . ASN D 1 116 ? 38.342  -38.199 -27.982 1.00 83.31  ? 116 ASN D CG  1 
ATOM   13689 O OD1 . ASN D 1 116 ? 37.465  -38.303 -28.843 1.00 85.67  ? 116 ASN D OD1 1 
ATOM   13690 N ND2 . ASN D 1 116 ? 39.598  -38.565 -28.191 1.00 84.55  ? 116 ASN D ND2 1 
ATOM   13691 N N   . TYR D 1 117 ? 37.889  -34.168 -26.750 1.00 76.18  ? 117 TYR D N   1 
ATOM   13692 C CA  . TYR D 1 117 ? 37.672  -32.928 -27.483 1.00 76.22  ? 117 TYR D CA  1 
ATOM   13693 C C   . TYR D 1 117 ? 38.402  -31.766 -26.793 1.00 74.73  ? 117 TYR D C   1 
ATOM   13694 O O   . TYR D 1 117 ? 38.983  -30.914 -27.466 1.00 75.13  ? 117 TYR D O   1 
ATOM   13695 C CB  . TYR D 1 117 ? 36.172  -32.676 -27.687 1.00 76.12  ? 117 TYR D CB  1 
ATOM   13696 C CG  . TYR D 1 117 ? 35.364  -32.523 -26.408 1.00 74.25  ? 117 TYR D CG  1 
ATOM   13697 C CD1 . TYR D 1 117 ? 35.357  -31.333 -25.692 1.00 73.00  ? 117 TYR D CD1 1 
ATOM   13698 C CD2 . TYR D 1 117 ? 34.610  -33.572 -25.918 1.00 74.03  ? 117 TYR D CD2 1 
ATOM   13699 C CE1 . TYR D 1 117 ? 34.636  -31.211 -24.516 1.00 71.75  ? 117 TYR D CE1 1 
ATOM   13700 C CE2 . TYR D 1 117 ? 33.885  -33.465 -24.748 1.00 72.71  ? 117 TYR D CE2 1 
ATOM   13701 C CZ  . TYR D 1 117 ? 33.891  -32.280 -24.048 1.00 71.74  ? 117 TYR D CZ  1 
ATOM   13702 O OH  . TYR D 1 117 ? 33.163  -32.195 -22.899 1.00 70.95  ? 117 TYR D OH  1 
ATOM   13703 N N   . ALA D 1 118 ? 38.413  -31.745 -25.453 1.00 72.96  ? 118 ALA D N   1 
ATOM   13704 C CA  . ALA D 1 118 ? 39.026  -30.663 -24.696 1.00 71.75  ? 118 ALA D CA  1 
ATOM   13705 C C   . ALA D 1 118 ? 40.442  -30.387 -25.187 1.00 73.37  ? 118 ALA D C   1 
ATOM   13706 O O   . ALA D 1 118 ? 40.941  -29.262 -25.122 1.00 73.33  ? 118 ALA D O   1 
ATOM   13707 C CB  . ALA D 1 118 ? 39.044  -31.003 -23.227 1.00 70.00  ? 118 ALA D CB  1 
ATOM   13708 N N   . LYS D 1 119 ? 41.098  -31.443 -25.672 1.00 75.61  ? 119 LYS D N   1 
ATOM   13709 C CA  . LYS D 1 119 ? 42.507  -31.377 -26.007 1.00 76.91  ? 119 LYS D CA  1 
ATOM   13710 C C   . LYS D 1 119 ? 42.739  -30.515 -27.241 1.00 78.13  ? 119 LYS D C   1 
ATOM   13711 O O   . LYS D 1 119 ? 43.873  -30.455 -27.688 1.00 79.22  ? 119 LYS D O   1 
ATOM   13712 C CB  . LYS D 1 119 ? 43.081  -32.769 -26.289 1.00 78.61  ? 119 LYS D CB  1 
ATOM   13713 C CG  . LYS D 1 119 ? 42.675  -33.413 -27.614 1.00 80.89  ? 119 LYS D CG  1 
ATOM   13714 C CD  . LYS D 1 119 ? 43.381  -34.736 -27.870 1.00 82.72  ? 119 LYS D CD  1 
ATOM   13715 C CE  . LYS D 1 119 ? 43.042  -35.297 -29.213 1.00 85.72  ? 119 LYS D CE  1 
ATOM   13716 N NZ  . LYS D 1 119 ? 43.941  -36.409 -29.570 1.00 87.75  ? 119 LYS D NZ  1 
ATOM   13717 N N   . LYS D 1 120 ? 41.676  -29.919 -27.809 1.00 78.11  ? 120 LYS D N   1 
ATOM   13718 C CA  . LYS D 1 120 ? 41.800  -29.080 -28.993 1.00 79.06  ? 120 LYS D CA  1 
ATOM   13719 C C   . LYS D 1 120 ? 41.601  -27.612 -28.624 1.00 77.12  ? 120 LYS D C   1 
ATOM   13720 O O   . LYS D 1 120 ? 41.657  -26.748 -29.492 1.00 77.51  ? 120 LYS D O   1 
ATOM   13721 C CB  . LYS D 1 120 ? 40.789  -29.509 -30.063 1.00 80.94  ? 120 LYS D CB  1 
ATOM   13722 C CG  . LYS D 1 120 ? 40.813  -30.987 -30.423 1.00 82.45  ? 120 LYS D CG  1 
ATOM   13723 C CD  . LYS D 1 120 ? 39.834  -31.380 -31.524 1.00 84.67  ? 120 LYS D CD  1 
ATOM   13724 C CE  . LYS D 1 120 ? 38.381  -31.121 -31.184 1.00 84.16  ? 120 LYS D CE  1 
ATOM   13725 N NZ  . LYS D 1 120 ? 37.487  -31.514 -32.279 1.00 85.94  ? 120 LYS D NZ  1 
ATOM   13726 N N   . TYR D 1 121 ? 41.382  -27.337 -27.337 1.00 74.91  ? 121 TYR D N   1 
ATOM   13727 C CA  . TYR D 1 121 ? 41.079  -25.986 -26.906 1.00 74.32  ? 121 TYR D CA  1 
ATOM   13728 C C   . TYR D 1 121 ? 42.212  -25.487 -26.008 1.00 73.76  ? 121 TYR D C   1 
ATOM   13729 O O   . TYR D 1 121 ? 42.226  -25.749 -24.801 1.00 72.16  ? 121 TYR D O   1 
ATOM   13730 C CB  . TYR D 1 121 ? 39.653  -26.033 -26.343 1.00 72.91  ? 121 TYR D CB  1 
ATOM   13731 C CG  . TYR D 1 121 ? 38.668  -26.366 -27.453 1.00 74.16  ? 121 TYR D CG  1 
ATOM   13732 C CD1 . TYR D 1 121 ? 38.261  -25.405 -28.373 1.00 75.15  ? 121 TYR D CD1 1 
ATOM   13733 C CD2 . TYR D 1 121 ? 38.190  -27.661 -27.622 1.00 74.70  ? 121 TYR D CD2 1 
ATOM   13734 C CE1 . TYR D 1 121 ? 37.377  -25.713 -29.398 1.00 76.49  ? 121 TYR D CE1 1 
ATOM   13735 C CE2 . TYR D 1 121 ? 37.316  -27.989 -28.651 1.00 75.91  ? 121 TYR D CE2 1 
ATOM   13736 C CZ  . TYR D 1 121 ? 36.911  -27.011 -29.540 1.00 76.81  ? 121 TYR D CZ  1 
ATOM   13737 O OH  . TYR D 1 121 ? 36.067  -27.346 -30.552 1.00 78.01  ? 121 TYR D OH  1 
ATOM   13738 N N   . ASP D 1 122 ? 43.146  -24.731 -26.608 1.00 75.12  ? 122 ASP D N   1 
ATOM   13739 C CA  . ASP D 1 122 ? 44.332  -24.282 -25.886 1.00 75.02  ? 122 ASP D CA  1 
ATOM   13740 C C   . ASP D 1 122 ? 43.976  -23.225 -24.842 1.00 73.67  ? 122 ASP D C   1 
ATOM   13741 O O   . ASP D 1 122 ? 44.843  -22.855 -24.060 1.00 73.75  ? 122 ASP D O   1 
ATOM   13742 C CB  . ASP D 1 122 ? 45.474  -23.812 -26.782 1.00 76.17  ? 122 ASP D CB  1 
ATOM   13743 C CG  . ASP D 1 122 ? 45.271  -22.483 -27.494 1.00 76.70  ? 122 ASP D CG  1 
ATOM   13744 O OD1 . ASP D 1 122 ? 44.314  -21.763 -27.134 1.00 75.77  ? 122 ASP D OD1 1 
ATOM   13745 O OD2 . ASP D 1 122 ? 46.049  -22.201 -28.430 1.00 78.01  ? 122 ASP D OD2 1 
ATOM   13746 N N   . CYS D 1 123 ? 42.716  -22.779 -24.781 1.00 72.58  ? 123 CYS D N   1 
ATOM   13747 C CA  . CYS D 1 123 ? 42.334  -21.883 -23.710 1.00 71.42  ? 123 CYS D CA  1 
ATOM   13748 C C   . CYS D 1 123 ? 42.494  -22.560 -22.351 1.00 70.03  ? 123 CYS D C   1 
ATOM   13749 O O   . CYS D 1 123 ? 42.641  -21.879 -21.342 1.00 69.14  ? 123 CYS D O   1 
ATOM   13750 C CB  . CYS D 1 123 ? 40.934  -21.311 -23.909 1.00 71.80  ? 123 CYS D CB  1 
ATOM   13751 S SG  . CYS D 1 123 ? 39.600  -22.537 -23.853 1.00 72.80  ? 123 CYS D SG  1 
ATOM   13752 N N   . ILE D 1 124 ? 42.465  -23.893 -22.301 1.00 70.10  ? 124 ILE D N   1 
ATOM   13753 C CA  . ILE D 1 124 ? 42.630  -24.563 -21.022 1.00 69.47  ? 124 ILE D CA  1 
ATOM   13754 C C   . ILE D 1 124 ? 44.087  -24.467 -20.546 1.00 70.40  ? 124 ILE D C   1 
ATOM   13755 O O   . ILE D 1 124 ? 45.043  -24.743 -21.281 1.00 72.97  ? 124 ILE D O   1 
ATOM   13756 C CB  . ILE D 1 124 ? 42.137  -26.014 -21.100 1.00 69.91  ? 124 ILE D CB  1 
ATOM   13757 C CG1 . ILE D 1 124 ? 40.675  -26.090 -21.580 1.00 70.12  ? 124 ILE D CG1 1 
ATOM   13758 C CG2 . ILE D 1 124 ? 42.322  -26.699 -19.746 1.00 68.86  ? 124 ILE D CG2 1 
ATOM   13759 C CD1 . ILE D 1 124 ? 40.199  -27.490 -21.910 1.00 70.81  ? 124 ILE D CD1 1 
ATOM   13760 N N   . ILE D 1 125 ? 44.276  -24.072 -19.284 1.00 68.66  ? 125 ILE D N   1 
ATOM   13761 C CA  . ILE D 1 125 ? 45.620  -23.893 -18.771 1.00 68.28  ? 125 ILE D CA  1 
ATOM   13762 C C   . ILE D 1 125 ? 45.827  -24.687 -17.486 1.00 66.75  ? 125 ILE D C   1 
ATOM   13763 O O   . ILE D 1 125 ? 46.951  -24.697 -16.988 1.00 69.12  ? 125 ILE D O   1 
ATOM   13764 C CB  . ILE D 1 125 ? 45.980  -22.399 -18.564 1.00 67.99  ? 125 ILE D CB  1 
ATOM   13765 C CG1 . ILE D 1 125 ? 45.065  -21.718 -17.562 1.00 66.60  ? 125 ILE D CG1 1 
ATOM   13766 C CG2 . ILE D 1 125 ? 46.033  -21.634 -19.888 1.00 69.02  ? 125 ILE D CG2 1 
ATOM   13767 C CD1 . ILE D 1 125 ? 45.406  -20.261 -17.289 1.00 66.79  ? 125 ILE D CD1 1 
ATOM   13768 N N   . THR D 1 126 ? 44.791  -25.305 -16.927 1.00 64.67  ? 126 THR D N   1 
ATOM   13769 C CA  . THR D 1 126 ? 44.953  -26.092 -15.712 1.00 64.29  ? 126 THR D CA  1 
ATOM   13770 C C   . THR D 1 126 ? 43.708  -26.959 -15.459 1.00 65.06  ? 126 THR D C   1 
ATOM   13771 O O   . THR D 1 126 ? 42.613  -26.426 -15.370 1.00 64.85  ? 126 THR D O   1 
ATOM   13772 C CB  . THR D 1 126 ? 45.191  -25.158 -14.528 1.00 62.83  ? 126 THR D CB  1 
ATOM   13773 O OG1 . THR D 1 126 ? 46.433  -24.476 -14.632 1.00 63.38  ? 126 THR D OG1 1 
ATOM   13774 C CG2 . THR D 1 126 ? 45.286  -25.883 -13.200 1.00 62.35  ? 126 THR D CG2 1 
ATOM   13775 N N   . TYR D 1 127 ? 43.866  -28.288 -15.311 1.00 65.60  ? 127 TYR D N   1 
ATOM   13776 C CA  . TYR D 1 127 ? 42.756  -29.146 -14.930 1.00 65.62  ? 127 TYR D CA  1 
ATOM   13777 C C   . TYR D 1 127 ? 42.741  -29.354 -13.413 1.00 65.90  ? 127 TYR D C   1 
ATOM   13778 O O   . TYR D 1 127 ? 43.777  -29.730 -12.856 1.00 65.25  ? 127 TYR D O   1 
ATOM   13779 C CB  . TYR D 1 127 ? 42.850  -30.515 -15.607 1.00 66.14  ? 127 TYR D CB  1 
ATOM   13780 C CG  . TYR D 1 127 ? 42.539  -30.542 -17.097 1.00 66.42  ? 127 TYR D CG  1 
ATOM   13781 C CD1 . TYR D 1 127 ? 43.466  -30.140 -18.043 1.00 67.52  ? 127 TYR D CD1 1 
ATOM   13782 C CD2 . TYR D 1 127 ? 41.333  -31.013 -17.560 1.00 66.05  ? 127 TYR D CD2 1 
ATOM   13783 C CE1 . TYR D 1 127 ? 43.192  -30.190 -19.402 1.00 68.37  ? 127 TYR D CE1 1 
ATOM   13784 C CE2 . TYR D 1 127 ? 41.040  -31.057 -18.911 1.00 67.06  ? 127 TYR D CE2 1 
ATOM   13785 C CZ  . TYR D 1 127 ? 41.964  -30.646 -19.840 1.00 67.73  ? 127 TYR D CZ  1 
ATOM   13786 O OH  . TYR D 1 127 ? 41.636  -30.715 -21.159 1.00 68.45  ? 127 TYR D OH  1 
ATOM   13787 N N   . LEU D 1 128 ? 41.566  -29.128 -12.772 1.00 65.62  ? 128 LEU D N   1 
ATOM   13788 C CA  . LEU D 1 128 ? 41.358  -29.474 -11.370 1.00 65.61  ? 128 LEU D CA  1 
ATOM   13789 C C   . LEU D 1 128 ? 40.683  -30.842 -11.302 1.00 69.68  ? 128 LEU D C   1 
ATOM   13790 O O   . LEU D 1 128 ? 39.570  -31.047 -11.791 1.00 75.50  ? 128 LEU D O   1 
ATOM   13791 C CB  . LEU D 1 128 ? 40.587  -28.419 -10.586 1.00 63.46  ? 128 LEU D CB  1 
ATOM   13792 C CG  . LEU D 1 128 ? 41.159  -26.992 -10.623 1.00 63.17  ? 128 LEU D CG  1 
ATOM   13793 C CD1 . LEU D 1 128 ? 40.326  -25.939 -9.911  1.00 61.43  ? 128 LEU D CD1 1 
ATOM   13794 C CD2 . LEU D 1 128 ? 42.574  -26.937 -10.061 1.00 63.67  ? 128 LEU D CD2 1 
ATOM   13795 N N   . VAL D 1 129 ? 41.371  -31.806 -10.691 1.00 71.25  ? 129 VAL D N   1 
ATOM   13796 C CA  . VAL D 1 129 ? 40.944  -33.189 -10.750 1.00 71.25  ? 129 VAL D CA  1 
ATOM   13797 C C   . VAL D 1 129 ? 39.854  -33.485 -9.725  1.00 70.72  ? 129 VAL D C   1 
ATOM   13798 O O   . VAL D 1 129 ? 39.137  -34.471 -9.867  1.00 75.43  ? 129 VAL D O   1 
ATOM   13799 C CB  . VAL D 1 129 ? 42.211  -34.030 -10.544 1.00 72.56  ? 129 VAL D CB  1 
ATOM   13800 C CG1 . VAL D 1 129 ? 42.027  -35.141 -9.525  1.00 73.17  ? 129 VAL D CG1 1 
ATOM   13801 C CG2 . VAL D 1 129 ? 42.718  -34.561 -11.876 1.00 74.45  ? 129 VAL D CG2 1 
ATOM   13802 N N   . ILE D 1 130 ? 39.752  -32.680 -8.671  1.00 68.68  ? 130 ILE D N   1 
ATOM   13803 C CA  . ILE D 1 130 ? 38.776  -32.925 -7.625  1.00 68.89  ? 130 ILE D CA  1 
ATOM   13804 C C   . ILE D 1 130 ? 38.654  -31.691 -6.741  1.00 70.37  ? 130 ILE D C   1 
ATOM   13805 O O   . ILE D 1 130 ? 39.593  -30.903 -6.651  1.00 71.75  ? 130 ILE D O   1 
ATOM   13806 C CB  . ILE D 1 130 ? 39.155  -34.151 -6.784  1.00 69.01  ? 130 ILE D CB  1 
ATOM   13807 C CG1 . ILE D 1 130 ? 38.028  -34.546 -5.866  1.00 69.02  ? 130 ILE D CG1 1 
ATOM   13808 C CG2 . ILE D 1 130 ? 40.437  -33.901 -5.995  1.00 69.69  ? 130 ILE D CG2 1 
ATOM   13809 C CD1 . ILE D 1 130 ? 38.084  -35.993 -5.417  1.00 70.17  ? 130 ILE D CD1 1 
ATOM   13810 N N   . ASN D 1 131 ? 37.516  -31.558 -6.046  1.00 71.62  ? 131 ASN D N   1 
ATOM   13811 C CA  . ASN D 1 131 ? 37.287  -30.409 -5.186  1.00 71.52  ? 131 ASN D CA  1 
ATOM   13812 C C   . ASN D 1 131 ? 36.918  -30.842 -3.767  1.00 71.45  ? 131 ASN D C   1 
ATOM   13813 O O   . ASN D 1 131 ? 36.140  -31.766 -3.569  1.00 74.83  ? 131 ASN D O   1 
ATOM   13814 C CB  . ASN D 1 131 ? 36.227  -29.502 -5.790  1.00 72.54  ? 131 ASN D CB  1 
ATOM   13815 C CG  . ASN D 1 131 ? 36.231  -28.138 -5.144  1.00 73.72  ? 131 ASN D CG  1 
ATOM   13816 O OD1 . ASN D 1 131 ? 37.225  -27.394 -5.236  1.00 70.70  ? 131 ASN D OD1 1 
ATOM   13817 N ND2 . ASN D 1 131 ? 35.125  -27.801 -4.488  1.00 74.28  ? 131 ASN D ND2 1 
ATOM   13818 N N   . GLU D 1 132 ? 37.502  -30.144 -2.792  1.00 70.79  ? 132 GLU D N   1 
ATOM   13819 C CA  . GLU D 1 132 ? 37.290  -30.361 -1.371  1.00 72.32  ? 132 GLU D CA  1 
ATOM   13820 C C   . GLU D 1 132 ? 36.963  -31.806 -1.037  1.00 71.20  ? 132 GLU D C   1 
ATOM   13821 O O   . GLU D 1 132 ? 35.870  -32.116 -0.579  1.00 71.67  ? 132 GLU D O   1 
ATOM   13822 C CB  . GLU D 1 132 ? 36.205  -29.461 -0.803  1.00 76.28  ? 132 GLU D CB  1 
ATOM   13823 C CG  . GLU D 1 132 ? 36.572  -27.991 -0.952  1.00 82.47  ? 132 GLU D CG  1 
ATOM   13824 C CD  . GLU D 1 132 ? 35.895  -27.070 0.050   1.00 87.03  ? 132 GLU D CD  1 
ATOM   13825 O OE1 . GLU D 1 132 ? 34.697  -27.291 0.377   1.00 86.80  ? 132 GLU D OE1 1 
ATOM   13826 O OE2 . GLU D 1 132 ? 36.587  -26.109 0.473   1.00 87.13  ? 132 GLU D OE2 1 
ATOM   13827 N N   . PRO D 1 133 ? 37.952  -32.707 -1.154  1.00 70.80  ? 133 PRO D N   1 
ATOM   13828 C CA  . PRO D 1 133 ? 37.878  -33.996 -0.491  1.00 71.11  ? 133 PRO D CA  1 
ATOM   13829 C C   . PRO D 1 133 ? 38.018  -33.758 1.009   1.00 71.50  ? 133 PRO D C   1 
ATOM   13830 O O   . PRO D 1 133 ? 38.913  -33.049 1.469   1.00 73.68  ? 133 PRO D O   1 
ATOM   13831 C CB  . PRO D 1 133 ? 39.052  -34.800 -1.070  1.00 72.34  ? 133 PRO D CB  1 
ATOM   13832 C CG  . PRO D 1 133 ? 39.715  -33.890 -2.110  1.00 71.87  ? 133 PRO D CG  1 
ATOM   13833 C CD  . PRO D 1 133 ? 39.240  -32.486 -1.831  1.00 71.54  ? 133 PRO D CD  1 
ATOM   13834 N N   . GLN D 1 134 ? 37.133  -34.382 1.771   1.00 72.05  ? 134 GLN D N   1 
ATOM   13835 C CA  . GLN D 1 134 ? 37.155  -34.288 3.221   1.00 72.99  ? 134 GLN D CA  1 
ATOM   13836 C C   . GLN D 1 134 ? 38.190  -35.254 3.821   1.00 71.65  ? 134 GLN D C   1 
ATOM   13837 O O   . GLN D 1 134 ? 38.654  -36.185 3.168   1.00 70.96  ? 134 GLN D O   1 
ATOM   13838 C CB  . GLN D 1 134 ? 35.710  -34.484 3.692   1.00 74.57  ? 134 GLN D CB  1 
ATOM   13839 C CG  . GLN D 1 134 ? 34.962  -33.174 3.900   1.00 74.84  ? 134 GLN D CG  1 
ATOM   13840 C CD  . GLN D 1 134 ? 35.447  -32.459 5.138   1.00 78.11  ? 134 GLN D CD  1 
ATOM   13841 O OE1 . GLN D 1 134 ? 36.355  -32.922 5.844   1.00 79.01  ? 134 GLN D OE1 1 
ATOM   13842 N NE2 . GLN D 1 134 ? 34.856  -31.305 5.405   1.00 80.50  ? 134 GLN D NE2 1 
ATOM   13843 N N   . THR D 1 135 ? 38.528  -35.017 5.094   1.00 69.72  ? 135 THR D N   1 
ATOM   13844 C CA  . THR D 1 135 ? 39.599  -35.703 5.791   1.00 68.81  ? 135 THR D CA  1 
ATOM   13845 C C   . THR D 1 135 ? 39.093  -37.024 6.361   1.00 69.43  ? 135 THR D C   1 
ATOM   13846 O O   . THR D 1 135 ? 39.670  -38.075 6.098   1.00 70.13  ? 135 THR D O   1 
ATOM   13847 C CB  . THR D 1 135 ? 40.106  -34.742 6.861   1.00 68.90  ? 135 THR D CB  1 
ATOM   13848 O OG1 . THR D 1 135 ? 40.688  -33.663 6.112   1.00 68.93  ? 135 THR D OG1 1 
ATOM   13849 C CG2 . THR D 1 135 ? 41.058  -35.399 7.846   1.00 69.52  ? 135 THR D CG2 1 
ATOM   13850 N N   . ASP D 1 136 ? 37.998  -36.974 7.123   1.00 69.22  ? 136 ASP D N   1 
ATOM   13851 C CA  . ASP D 1 136 ? 37.395  -38.181 7.667   1.00 69.85  ? 136 ASP D CA  1 
ATOM   13852 C C   . ASP D 1 136 ? 37.078  -39.171 6.541   1.00 70.32  ? 136 ASP D C   1 
ATOM   13853 O O   . ASP D 1 136 ? 37.185  -40.395 6.719   1.00 70.74  ? 136 ASP D O   1 
ATOM   13854 C CB  . ASP D 1 136 ? 36.178  -37.859 8.517   1.00 69.58  ? 136 ASP D CB  1 
ATOM   13855 C CG  . ASP D 1 136 ? 35.428  -39.070 9.049   1.00 71.03  ? 136 ASP D CG  1 
ATOM   13856 O OD1 . ASP D 1 136 ? 34.544  -39.605 8.323   1.00 70.74  ? 136 ASP D OD1 1 
ATOM   13857 O OD2 . ASP D 1 136 ? 35.752  -39.494 10.178  1.00 72.29  ? 136 ASP D OD2 1 
ATOM   13858 N N   . HIS D 1 137 ? 36.689  -38.626 5.378   1.00 69.42  ? 137 HIS D N   1 
ATOM   13859 C CA  . HIS D 1 137 ? 36.267  -39.445 4.254   1.00 69.78  ? 137 HIS D CA  1 
ATOM   13860 C C   . HIS D 1 137 ? 37.452  -40.204 3.689   1.00 69.80  ? 137 HIS D C   1 
ATOM   13861 O O   . HIS D 1 137 ? 37.336  -41.404 3.429   1.00 70.88  ? 137 HIS D O   1 
ATOM   13862 C CB  . HIS D 1 137 ? 35.679  -38.600 3.123   1.00 69.44  ? 137 HIS D CB  1 
ATOM   13863 C CG  . HIS D 1 137 ? 35.315  -39.393 1.912   1.00 70.47  ? 137 HIS D CG  1 
ATOM   13864 N ND1 . HIS D 1 137 ? 34.348  -40.370 1.937   1.00 71.92  ? 137 HIS D ND1 1 
ATOM   13865 C CD2 . HIS D 1 137 ? 35.799  -39.382 0.664   1.00 70.93  ? 137 HIS D CD2 1 
ATOM   13866 C CE1 . HIS D 1 137 ? 34.268  -40.922 0.733   1.00 72.93  ? 137 HIS D CE1 1 
ATOM   13867 N NE2 . HIS D 1 137 ? 35.134  -40.335 -0.060  1.00 71.64  ? 137 HIS D NE2 1 
ATOM   13868 N N   . ILE D 1 138 ? 38.565  -39.481 3.479   1.00 68.77  ? 138 ILE D N   1 
ATOM   13869 C CA  . ILE D 1 138 ? 39.781  -40.105 2.979   1.00 69.26  ? 138 ILE D CA  1 
ATOM   13870 C C   . ILE D 1 138 ? 40.208  -41.233 3.929   1.00 70.48  ? 138 ILE D C   1 
ATOM   13871 O O   . ILE D 1 138 ? 40.419  -42.368 3.485   1.00 70.60  ? 138 ILE D O   1 
ATOM   13872 C CB  . ILE D 1 138 ? 40.910  -39.096 2.749   1.00 68.42  ? 138 ILE D CB  1 
ATOM   13873 C CG1 . ILE D 1 138 ? 40.612  -38.154 1.610   1.00 67.26  ? 138 ILE D CG1 1 
ATOM   13874 C CG2 . ILE D 1 138 ? 42.214  -39.841 2.481   1.00 69.93  ? 138 ILE D CG2 1 
ATOM   13875 C CD1 . ILE D 1 138 ? 41.760  -37.206 1.279   1.00 66.38  ? 138 ILE D CD1 1 
ATOM   13876 N N   . HIS D 1 139 ? 40.286  -40.914 5.230   1.00 70.34  ? 139 HIS D N   1 
ATOM   13877 C CA  . HIS D 1 139 ? 40.581  -41.901 6.249   1.00 71.94  ? 139 HIS D CA  1 
ATOM   13878 C C   . HIS D 1 139 ? 39.685  -43.132 6.122   1.00 73.62  ? 139 HIS D C   1 
ATOM   13879 O O   . HIS D 1 139 ? 40.166  -44.242 6.279   1.00 74.86  ? 139 HIS D O   1 
ATOM   13880 C CB  . HIS D 1 139 ? 40.428  -41.317 7.650   1.00 72.26  ? 139 HIS D CB  1 
ATOM   13881 C CG  . HIS D 1 139 ? 40.625  -42.327 8.730   1.00 74.26  ? 139 HIS D CG  1 
ATOM   13882 N ND1 . HIS D 1 139 ? 41.868  -42.819 9.066   1.00 75.93  ? 139 HIS D ND1 1 
ATOM   13883 C CD2 . HIS D 1 139 ? 39.754  -42.946 9.533   1.00 75.26  ? 139 HIS D CD2 1 
ATOM   13884 C CE1 . HIS D 1 139 ? 41.739  -43.711 10.041  1.00 77.48  ? 139 HIS D CE1 1 
ATOM   13885 N NE2 . HIS D 1 139 ? 40.463  -43.767 10.364  1.00 77.15  ? 139 HIS D NE2 1 
ATOM   13886 N N   . SER D 1 140 ? 38.389  -42.941 5.861   1.00 74.01  ? 140 SER D N   1 
ATOM   13887 C CA  . SER D 1 140 ? 37.453  -44.052 5.821   1.00 75.27  ? 140 SER D CA  1 
ATOM   13888 C C   . SER D 1 140 ? 37.712  -44.925 4.596   1.00 75.72  ? 140 SER D C   1 
ATOM   13889 O O   . SER D 1 140 ? 37.635  -46.152 4.695   1.00 78.52  ? 140 SER D O   1 
ATOM   13890 C CB  . SER D 1 140 ? 36.035  -43.567 5.850   1.00 75.63  ? 140 SER D CB  1 
ATOM   13891 O OG  . SER D 1 140 ? 35.130  -44.652 5.991   1.00 77.63  ? 140 SER D OG  1 
ATOM   13892 N N   . VAL D 1 141 ? 38.051  -44.307 3.454   1.00 73.98  ? 141 VAL D N   1 
ATOM   13893 C CA  . VAL D 1 141 ? 38.290  -45.073 2.234   1.00 73.78  ? 141 VAL D CA  1 
ATOM   13894 C C   . VAL D 1 141 ? 39.778  -45.399 2.053   1.00 74.11  ? 141 VAL D C   1 
ATOM   13895 O O   . VAL D 1 141 ? 40.112  -46.182 1.160   1.00 73.96  ? 141 VAL D O   1 
ATOM   13896 C CB  . VAL D 1 141 ? 37.738  -44.363 0.984   1.00 72.19  ? 141 VAL D CB  1 
ATOM   13897 C CG1 . VAL D 1 141 ? 36.239  -44.128 1.096   1.00 71.70  ? 141 VAL D CG1 1 
ATOM   13898 C CG2 . VAL D 1 141 ? 38.503  -43.080 0.671   1.00 70.65  ? 141 VAL D CG2 1 
ATOM   13899 N N   . THR D 1 142 ? 40.638  -44.774 2.887   1.00 73.93  ? 142 THR D N   1 
ATOM   13900 C CA  . THR D 1 142 ? 42.094  -44.911 2.902   1.00 73.98  ? 142 THR D CA  1 
ATOM   13901 C C   . THR D 1 142 ? 42.716  -43.853 1.995   1.00 72.93  ? 142 THR D C   1 
ATOM   13902 O O   . THR D 1 142 ? 42.238  -43.566 0.899   1.00 72.05  ? 142 THR D O   1 
ATOM   13903 C CB  . THR D 1 142 ? 42.591  -46.308 2.519   1.00 75.13  ? 142 THR D CB  1 
ATOM   13904 O OG1 . THR D 1 142 ? 42.374  -46.469 1.120   1.00 74.42  ? 142 THR D OG1 1 
ATOM   13905 C CG2 . THR D 1 142 ? 41.948  -47.402 3.352   1.00 76.05  ? 142 THR D CG2 1 
ATOM   13906 N N   . GLY D 1 143 ? 43.815  -43.277 2.465   1.00 73.33  ? 143 GLY D N   1 
ATOM   13907 C CA  . GLY D 1 143 ? 44.598  -42.378 1.639   1.00 73.21  ? 143 GLY D CA  1 
ATOM   13908 C C   . GLY D 1 143 ? 45.164  -43.099 0.419   1.00 74.47  ? 143 GLY D C   1 
ATOM   13909 O O   . GLY D 1 143 ? 45.341  -42.504 -0.644  1.00 74.24  ? 143 GLY D O   1 
ATOM   13910 N N   . LYS D 1 144 ? 45.429  -44.399 0.565   1.00 76.49  ? 144 LYS D N   1 
ATOM   13911 C CA  . LYS D 1 144 ? 45.897  -45.155 -0.578  1.00 76.91  ? 144 LYS D CA  1 
ATOM   13912 C C   . LYS D 1 144 ? 44.882  -45.032 -1.718  1.00 75.41  ? 144 LYS D C   1 
ATOM   13913 O O   . LYS D 1 144 ? 45.239  -44.708 -2.852  1.00 75.28  ? 144 LYS D O   1 
ATOM   13914 C CB  . LYS D 1 144 ? 46.215  -46.602 -0.216  1.00 78.54  ? 144 LYS D CB  1 
ATOM   13915 C CG  . LYS D 1 144 ? 46.744  -47.346 -1.430  1.00 80.04  ? 144 LYS D CG  1 
ATOM   13916 C CD  . LYS D 1 144 ? 47.243  -48.764 -1.167  1.00 82.65  ? 144 LYS D CD  1 
ATOM   13917 C CE  . LYS D 1 144 ? 48.036  -49.260 -2.329  1.00 83.96  ? 144 LYS D CE  1 
ATOM   13918 N NZ  . LYS D 1 144 ? 47.223  -49.310 -3.546  1.00 83.62  ? 144 LYS D NZ  1 
ATOM   13919 N N   . ALA D 1 145 ? 43.605  -45.267 -1.428  1.00 74.26  ? 145 ALA D N   1 
ATOM   13920 C CA  . ALA D 1 145 ? 42.619  -45.180 -2.489  1.00 73.65  ? 145 ALA D CA  1 
ATOM   13921 C C   . ALA D 1 145 ? 42.698  -43.793 -3.120  1.00 72.09  ? 145 ALA D C   1 
ATOM   13922 O O   . ALA D 1 145 ? 42.772  -43.653 -4.339  1.00 71.89  ? 145 ALA D O   1 
ATOM   13923 C CB  . ALA D 1 145 ? 41.241  -45.492 -1.953  1.00 73.86  ? 145 ALA D CB  1 
ATOM   13924 N N   . PHE D 1 146 ? 42.724  -42.773 -2.268  1.00 70.68  ? 146 PHE D N   1 
ATOM   13925 C CA  . PHE D 1 146 ? 42.802  -41.423 -2.766  1.00 70.24  ? 146 PHE D CA  1 
ATOM   13926 C C   . PHE D 1 146 ? 44.009  -41.244 -3.684  1.00 70.79  ? 146 PHE D C   1 
ATOM   13927 O O   . PHE D 1 146 ? 43.875  -40.743 -4.802  1.00 71.01  ? 146 PHE D O   1 
ATOM   13928 C CB  . PHE D 1 146 ? 42.921  -40.447 -1.598  1.00 70.03  ? 146 PHE D CB  1 
ATOM   13929 C CG  . PHE D 1 146 ? 43.022  -38.998 -2.047  1.00 68.35  ? 146 PHE D CG  1 
ATOM   13930 C CD1 . PHE D 1 146 ? 41.894  -38.299 -2.419  1.00 67.08  ? 146 PHE D CD1 1 
ATOM   13931 C CD2 . PHE D 1 146 ? 44.251  -38.351 -2.103  1.00 68.27  ? 146 PHE D CD2 1 
ATOM   13932 C CE1 . PHE D 1 146 ? 41.993  -36.975 -2.814  1.00 66.62  ? 146 PHE D CE1 1 
ATOM   13933 C CE2 . PHE D 1 146 ? 44.341  -37.035 -2.509  1.00 66.92  ? 146 PHE D CE2 1 
ATOM   13934 C CZ  . PHE D 1 146 ? 43.214  -36.349 -2.862  1.00 66.18  ? 146 PHE D CZ  1 
ATOM   13935 N N   . VAL D 1 147 ? 45.198  -41.598 -3.194  1.00 71.17  ? 147 VAL D N   1 
ATOM   13936 C CA  . VAL D 1 147 ? 46.403  -41.244 -3.926  1.00 71.70  ? 147 VAL D CA  1 
ATOM   13937 C C   . VAL D 1 147 ? 46.387  -41.956 -5.279  1.00 72.61  ? 147 VAL D C   1 
ATOM   13938 O O   . VAL D 1 147 ? 46.788  -41.389 -6.297  1.00 72.55  ? 147 VAL D O   1 
ATOM   13939 C CB  . VAL D 1 147 ? 47.746  -41.513 -3.216  1.00 72.24  ? 147 VAL D CB  1 
ATOM   13940 C CG1 . VAL D 1 147 ? 48.892  -41.122 -4.128  1.00 72.41  ? 147 VAL D CG1 1 
ATOM   13941 C CG2 . VAL D 1 147 ? 47.895  -40.763 -1.896  1.00 71.62  ? 147 VAL D CG2 1 
ATOM   13942 N N   . ASP D 1 148 ? 45.929  -43.209 -5.285  1.00 73.63  ? 148 ASP D N   1 
ATOM   13943 C CA  . ASP D 1 148 ? 45.924  -44.000 -6.508  1.00 74.54  ? 148 ASP D CA  1 
ATOM   13944 C C   . ASP D 1 148 ? 44.983  -43.341 -7.526  1.00 73.95  ? 148 ASP D C   1 
ATOM   13945 O O   . ASP D 1 148 ? 45.375  -43.156 -8.685  1.00 75.02  ? 148 ASP D O   1 
ATOM   13946 C CB  . ASP D 1 148 ? 45.745  -45.474 -6.185  1.00 75.19  ? 148 ASP D CB  1 
ATOM   13947 C CG  . ASP D 1 148 ? 46.889  -46.113 -5.397  1.00 76.65  ? 148 ASP D CG  1 
ATOM   13948 O OD1 . ASP D 1 148 ? 47.986  -45.505 -5.298  1.00 76.34  ? 148 ASP D OD1 1 
ATOM   13949 O OD2 . ASP D 1 148 ? 46.689  -47.226 -4.873  1.00 78.25  ? 148 ASP D OD2 1 
ATOM   13950 N N   . LEU D 1 149 ? 43.790  -42.903 -7.075  1.00 71.79  ? 149 LEU D N   1 
ATOM   13951 C CA  . LEU D 1 149 ? 42.818  -42.284 -7.964  1.00 69.91  ? 149 LEU D CA  1 
ATOM   13952 C C   . LEU D 1 149 ? 43.450  -41.080 -8.649  1.00 69.10  ? 149 LEU D C   1 
ATOM   13953 O O   . LEU D 1 149 ? 43.488  -41.003 -9.880  1.00 68.35  ? 149 LEU D O   1 
ATOM   13954 C CB  . LEU D 1 149 ? 41.540  -41.905 -7.215  1.00 68.36  ? 149 LEU D CB  1 
ATOM   13955 C CG  . LEU D 1 149 ? 40.467  -41.192 -8.042  1.00 66.96  ? 149 LEU D CG  1 
ATOM   13956 C CD1 . LEU D 1 149 ? 40.152  -41.905 -9.338  1.00 67.46  ? 149 LEU D CD1 1 
ATOM   13957 C CD2 . LEU D 1 149 ? 39.234  -41.016 -7.194  1.00 66.32  ? 149 LEU D CD2 1 
ATOM   13958 N N   . MET D 1 150 ? 43.960  -40.166 -7.814  1.00 69.50  ? 150 MET D N   1 
ATOM   13959 C CA  . MET D 1 150 ? 44.598  -38.948 -8.284  1.00 69.77  ? 150 MET D CA  1 
ATOM   13960 C C   . MET D 1 150 ? 45.650  -39.303 -9.331  1.00 70.91  ? 150 MET D C   1 
ATOM   13961 O O   . MET D 1 150 ? 45.640  -38.746 -10.421 1.00 70.74  ? 150 MET D O   1 
ATOM   13962 C CB  . MET D 1 150 ? 45.255  -38.183 -7.133  1.00 70.08  ? 150 MET D CB  1 
ATOM   13963 C CG  . MET D 1 150 ? 44.279  -37.713 -6.073  1.00 69.79  ? 150 MET D CG  1 
ATOM   13964 S SD  . MET D 1 150 ? 43.319  -36.295 -6.629  1.00 70.04  ? 150 MET D SD  1 
ATOM   13965 C CE  . MET D 1 150 ? 41.676  -36.929 -6.251  1.00 71.10  ? 150 MET D CE  1 
ATOM   13966 N N   . ASN D 1 151 ? 46.529  -40.262 -9.020  1.00 72.38  ? 151 ASN D N   1 
ATOM   13967 C CA  . ASN D 1 151 ? 47.594  -40.624 -9.942  1.00 74.23  ? 151 ASN D CA  1 
ATOM   13968 C C   . ASN D 1 151 ? 47.014  -41.108 -11.273 1.00 75.30  ? 151 ASN D C   1 
ATOM   13969 O O   . ASN D 1 151 ? 47.585  -40.809 -12.330 1.00 75.15  ? 151 ASN D O   1 
ATOM   13970 C CB  . ASN D 1 151 ? 48.573  -41.631 -9.337  1.00 76.04  ? 151 ASN D CB  1 
ATOM   13971 C CG  . ASN D 1 151 ? 49.636  -40.979 -8.476  1.00 76.43  ? 151 ASN D CG  1 
ATOM   13972 O OD1 . ASN D 1 151 ? 49.988  -41.507 -7.419  1.00 77.19  ? 151 ASN D OD1 1 
ATOM   13973 N ND2 . ASN D 1 151 ? 50.193  -39.855 -8.906  1.00 76.37  ? 151 ASN D ND2 1 
ATOM   13974 N N   . THR D 1 152 ? 45.886  -41.844 -11.211 1.00 75.88  ? 152 THR D N   1 
ATOM   13975 C CA  . THR D 1 152 ? 45.232  -42.366 -12.403 1.00 77.00  ? 152 THR D CA  1 
ATOM   13976 C C   . THR D 1 152 ? 44.735  -41.198 -13.248 1.00 75.75  ? 152 THR D C   1 
ATOM   13977 O O   . THR D 1 152 ? 45.047  -41.112 -14.433 1.00 76.03  ? 152 THR D O   1 
ATOM   13978 C CB  . THR D 1 152 ? 44.083  -43.303 -12.025 1.00 78.48  ? 152 THR D CB  1 
ATOM   13979 O OG1 . THR D 1 152 ? 44.606  -44.260 -11.112 1.00 80.93  ? 152 THR D OG1 1 
ATOM   13980 C CG2 . THR D 1 152 ? 43.498  -44.060 -13.206 1.00 79.23  ? 152 THR D CG2 1 
ATOM   13981 N N   . LEU D 1 153 ? 43.972  -40.297 -12.629 1.00 74.22  ? 153 LEU D N   1 
ATOM   13982 C CA  . LEU D 1 153 ? 43.443  -39.149 -13.351 1.00 74.77  ? 153 LEU D CA  1 
ATOM   13983 C C   . LEU D 1 153 ? 44.578  -38.257 -13.877 1.00 74.19  ? 153 LEU D C   1 
ATOM   13984 O O   . LEU D 1 153 ? 44.516  -37.792 -15.014 1.00 74.65  ? 153 LEU D O   1 
ATOM   13985 C CB  . LEU D 1 153 ? 42.484  -38.366 -12.454 1.00 74.25  ? 153 LEU D CB  1 
ATOM   13986 C CG  . LEU D 1 153 ? 41.308  -39.162 -11.877 1.00 75.75  ? 153 LEU D CG  1 
ATOM   13987 C CD1 . LEU D 1 153 ? 40.582  -38.337 -10.820 1.00 75.08  ? 153 LEU D CD1 1 
ATOM   13988 C CD2 . LEU D 1 153 ? 40.336  -39.617 -12.962 1.00 76.55  ? 153 LEU D CD2 1 
ATOM   13989 N N   . ILE D 1 154 ? 45.611  -37.995 -13.061 1.00 72.80  ? 154 ILE D N   1 
ATOM   13990 C CA  . ILE D 1 154 ? 46.698  -37.129 -13.492 1.00 72.27  ? 154 ILE D CA  1 
ATOM   13991 C C   . ILE D 1 154 ? 47.308  -37.685 -14.776 1.00 73.54  ? 154 ILE D C   1 
ATOM   13992 O O   . ILE D 1 154 ? 47.485  -36.941 -15.736 1.00 73.18  ? 154 ILE D O   1 
ATOM   13993 C CB  . ILE D 1 154 ? 47.788  -36.934 -12.419 1.00 72.04  ? 154 ILE D CB  1 
ATOM   13994 C CG1 . ILE D 1 154 ? 47.290  -36.205 -11.164 1.00 70.81  ? 154 ILE D CG1 1 
ATOM   13995 C CG2 . ILE D 1 154 ? 48.972  -36.180 -13.018 1.00 72.33  ? 154 ILE D CG2 1 
ATOM   13996 C CD1 . ILE D 1 154 ? 48.194  -36.379 -9.953  1.00 70.65  ? 154 ILE D CD1 1 
ATOM   13997 N N   . ASN D 1 155 ? 47.638  -38.986 -14.783 1.00 75.14  ? 155 ASN D N   1 
ATOM   13998 C CA  . ASN D 1 155 ? 48.377  -39.561 -15.891 1.00 76.95  ? 155 ASN D CA  1 
ATOM   13999 C C   . ASN D 1 155 ? 47.537  -39.581 -17.167 1.00 77.48  ? 155 ASN D C   1 
ATOM   14000 O O   . ASN D 1 155 ? 48.085  -39.410 -18.249 1.00 78.13  ? 155 ASN D O   1 
ATOM   14001 C CB  . ASN D 1 155 ? 48.979  -40.905 -15.526 1.00 79.37  ? 155 ASN D CB  1 
ATOM   14002 C CG  . ASN D 1 155 ? 50.014  -40.796 -14.424 1.00 81.33  ? 155 ASN D CG  1 
ATOM   14003 O OD1 . ASN D 1 155 ? 50.770  -39.808 -14.311 1.00 80.96  ? 155 ASN D OD1 1 
ATOM   14004 N ND2 . ASN D 1 155 ? 50.067  -41.830 -13.595 1.00 82.97  ? 155 ASN D ND2 1 
ATOM   14005 N N   . ILE D 1 156 ? 46.215  -39.764 -17.051 1.00 77.40  ? 156 ILE D N   1 
ATOM   14006 C CA  . ILE D 1 156 ? 45.325  -39.699 -18.206 1.00 78.39  ? 156 ILE D CA  1 
ATOM   14007 C C   . ILE D 1 156 ? 45.313  -38.281 -18.800 1.00 78.21  ? 156 ILE D C   1 
ATOM   14008 O O   . ILE D 1 156 ? 45.193  -38.125 -20.016 1.00 79.75  ? 156 ILE D O   1 
ATOM   14009 C CB  . ILE D 1 156 ? 43.903  -40.153 -17.819 1.00 78.54  ? 156 ILE D CB  1 
ATOM   14010 C CG1 . ILE D 1 156 ? 43.847  -41.650 -17.554 1.00 79.34  ? 156 ILE D CG1 1 
ATOM   14011 C CG2 . ILE D 1 156 ? 42.866  -39.730 -18.866 1.00 78.55  ? 156 ILE D CG2 1 
ATOM   14012 C CD1 . ILE D 1 156 ? 42.556  -42.117 -16.900 1.00 78.54  ? 156 ILE D CD1 1 
ATOM   14013 N N   . ILE D 1 157 ? 45.384  -37.236 -17.957 1.00 76.16  ? 157 ILE D N   1 
ATOM   14014 C CA  . ILE D 1 157 ? 45.358  -35.872 -18.467 1.00 75.02  ? 157 ILE D CA  1 
ATOM   14015 C C   . ILE D 1 157 ? 46.713  -35.568 -19.098 1.00 75.52  ? 157 ILE D C   1 
ATOM   14016 O O   . ILE D 1 157 ? 46.777  -34.924 -20.142 1.00 75.97  ? 157 ILE D O   1 
ATOM   14017 C CB  . ILE D 1 157 ? 44.953  -34.831 -17.400 1.00 73.60  ? 157 ILE D CB  1 
ATOM   14018 C CG1 . ILE D 1 157 ? 43.503  -35.036 -16.894 1.00 72.59  ? 157 ILE D CG1 1 
ATOM   14019 C CG2 . ILE D 1 157 ? 45.130  -33.397 -17.924 1.00 73.52  ? 157 ILE D CG2 1 
ATOM   14020 C CD1 . ILE D 1 157 ? 43.153  -34.223 -15.656 1.00 70.61  ? 157 ILE D CD1 1 
ATOM   14021 N N   . HIS D 1 158 ? 47.797  -36.053 -18.481 1.00 75.81  ? 158 HIS D N   1 
ATOM   14022 C CA  . HIS D 1 158 ? 49.131  -35.765 -18.989 1.00 76.17  ? 158 HIS D CA  1 
ATOM   14023 C C   . HIS D 1 158 ? 49.313  -36.346 -20.392 1.00 78.62  ? 158 HIS D C   1 
ATOM   14024 O O   . HIS D 1 158 ? 50.054  -35.758 -21.181 1.00 80.22  ? 158 HIS D O   1 
ATOM   14025 C CB  . HIS D 1 158 ? 50.234  -36.289 -18.066 1.00 75.35  ? 158 HIS D CB  1 
ATOM   14026 C CG  . HIS D 1 158 ? 50.489  -35.478 -16.851 1.00 73.31  ? 158 HIS D CG  1 
ATOM   14027 N ND1 . HIS D 1 158 ? 51.266  -35.963 -15.825 1.00 72.96  ? 158 HIS D ND1 1 
ATOM   14028 C CD2 . HIS D 1 158 ? 50.121  -34.256 -16.489 1.00 72.48  ? 158 HIS D CD2 1 
ATOM   14029 C CE1 . HIS D 1 158 ? 51.387  -35.049 -14.883 1.00 71.88  ? 158 HIS D CE1 1 
ATOM   14030 N NE2 . HIS D 1 158 ? 50.703  -34.001 -15.266 1.00 71.92  ? 158 HIS D NE2 1 
ATOM   14031 N N   . LYS D 1 159 ? 48.653  -37.485 -20.693 1.00 79.24  ? 159 LYS D N   1 
ATOM   14032 C CA  . LYS D 1 159 ? 48.739  -38.109 -22.008 1.00 80.87  ? 159 LYS D CA  1 
ATOM   14033 C C   . LYS D 1 159 ? 47.615  -37.608 -22.914 1.00 79.86  ? 159 LYS D C   1 
ATOM   14034 O O   . LYS D 1 159 ? 47.786  -37.487 -24.125 1.00 80.49  ? 159 LYS D O   1 
ATOM   14035 C CB  . LYS D 1 159 ? 48.649  -39.632 -21.925 1.00 83.30  ? 159 LYS D CB  1 
ATOM   14036 C CG  . LYS D 1 159 ? 49.820  -40.357 -21.300 1.00 85.63  ? 159 LYS D CG  1 
ATOM   14037 C CD  . LYS D 1 159 ? 49.797  -41.839 -21.634 1.00 89.87  ? 159 LYS D CD  1 
ATOM   14038 C CE  . LYS D 1 159 ? 49.000  -42.676 -20.681 1.00 92.92  ? 159 LYS D CE  1 
ATOM   14039 N NZ  . LYS D 1 159 ? 49.893  -43.255 -19.670 1.00 96.37  ? 159 LYS D NZ  1 
ATOM   14040 N N   . GLY D 1 160 ? 46.454  -37.312 -22.328 1.00 77.80  ? 160 GLY D N   1 
ATOM   14041 C CA  . GLY D 1 160 ? 45.265  -37.056 -23.120 1.00 77.96  ? 160 GLY D CA  1 
ATOM   14042 C C   . GLY D 1 160 ? 45.224  -35.626 -23.642 1.00 77.82  ? 160 GLY D C   1 
ATOM   14043 O O   . GLY D 1 160 ? 44.718  -35.369 -24.737 1.00 78.21  ? 160 GLY D O   1 
ATOM   14044 N N   . HIS D 1 161 ? 45.737  -34.716 -22.805 1.00 77.24  ? 161 HIS D N   1 
ATOM   14045 C CA  . HIS D 1 161 ? 45.929  -33.321 -23.153 1.00 76.88  ? 161 HIS D CA  1 
ATOM   14046 C C   . HIS D 1 161 ? 47.323  -32.887 -22.712 1.00 76.32  ? 161 HIS D C   1 
ATOM   14047 O O   . HIS D 1 161 ? 47.500  -32.223 -21.688 1.00 74.51  ? 161 HIS D O   1 
ATOM   14048 C CB  . HIS D 1 161 ? 44.860  -32.462 -22.478 1.00 76.00  ? 161 HIS D CB  1 
ATOM   14049 C CG  . HIS D 1 161 ? 44.713  -31.156 -23.149 1.00 76.17  ? 161 HIS D CG  1 
ATOM   14050 N ND1 . HIS D 1 161 ? 43.704  -30.285 -22.833 1.00 75.44  ? 161 HIS D ND1 1 
ATOM   14051 C CD2 . HIS D 1 161 ? 45.425  -30.583 -24.121 1.00 77.70  ? 161 HIS D CD2 1 
ATOM   14052 C CE1 . HIS D 1 161 ? 43.820  -29.213 -23.599 1.00 76.49  ? 161 HIS D CE1 1 
ATOM   14053 N NE2 . HIS D 1 161 ? 44.867  -29.365 -24.380 1.00 77.34  ? 161 HIS D NE2 1 
ATOM   14054 N N   . PRO D 1 162 ? 48.373  -33.253 -23.473 1.00 78.11  ? 162 PRO D N   1 
ATOM   14055 C CA  . PRO D 1 162 ? 49.745  -32.936 -23.064 1.00 77.86  ? 162 PRO D CA  1 
ATOM   14056 C C   . PRO D 1 162 ? 49.953  -31.433 -22.871 1.00 76.14  ? 162 PRO D C   1 
ATOM   14057 O O   . PRO D 1 162 ? 49.333  -30.611 -23.544 1.00 75.43  ? 162 PRO D O   1 
ATOM   14058 C CB  . PRO D 1 162 ? 50.618  -33.521 -24.175 1.00 80.11  ? 162 PRO D CB  1 
ATOM   14059 C CG  . PRO D 1 162 ? 49.678  -33.669 -25.356 1.00 81.22  ? 162 PRO D CG  1 
ATOM   14060 C CD  . PRO D 1 162 ? 48.304  -33.958 -24.764 1.00 79.87  ? 162 PRO D CD  1 
ATOM   14061 N N   . GLY D 1 163 ? 50.784  -31.109 -21.877 1.00 74.80  ? 163 GLY D N   1 
ATOM   14062 C CA  . GLY D 1 163 ? 51.229  -29.755 -21.641 1.00 73.95  ? 163 GLY D CA  1 
ATOM   14063 C C   . GLY D 1 163 ? 50.387  -29.037 -20.599 1.00 72.10  ? 163 GLY D C   1 
ATOM   14064 O O   . GLY D 1 163 ? 50.757  -27.942 -20.179 1.00 71.70  ? 163 GLY D O   1 
ATOM   14065 N N   . ILE D 1 164 ? 49.241  -29.606 -20.196 1.00 70.99  ? 164 ILE D N   1 
ATOM   14066 C CA  . ILE D 1 164 ? 48.372  -28.829 -19.328 1.00 68.92  ? 164 ILE D CA  1 
ATOM   14067 C C   . ILE D 1 164 ? 48.555  -29.271 -17.881 1.00 67.27  ? 164 ILE D C   1 
ATOM   14068 O O   . ILE D 1 164 ? 48.252  -30.411 -17.552 1.00 67.80  ? 164 ILE D O   1 
ATOM   14069 C CB  . ILE D 1 164 ? 46.900  -28.883 -19.761 1.00 68.76  ? 164 ILE D CB  1 
ATOM   14070 C CG1 . ILE D 1 164 ? 46.637  -28.091 -21.052 1.00 69.91  ? 164 ILE D CG1 1 
ATOM   14071 C CG2 . ILE D 1 164 ? 46.036  -28.344 -18.626 1.00 67.20  ? 164 ILE D CG2 1 
ATOM   14072 C CD1 . ILE D 1 164 ? 47.185  -28.719 -22.315 1.00 71.99  ? 164 ILE D CD1 1 
ATOM   14073 N N   . PRO D 1 165 ? 49.038  -28.376 -16.990 1.00 65.54  ? 165 PRO D N   1 
ATOM   14074 C CA  . PRO D 1 165 ? 49.162  -28.660 -15.564 1.00 64.64  ? 165 PRO D CA  1 
ATOM   14075 C C   . PRO D 1 165 ? 47.861  -29.200 -15.006 1.00 64.20  ? 165 PRO D C   1 
ATOM   14076 O O   . PRO D 1 165 ? 46.802  -28.716 -15.395 1.00 64.34  ? 165 PRO D O   1 
ATOM   14077 C CB  . PRO D 1 165 ? 49.478  -27.332 -14.869 1.00 63.60  ? 165 PRO D CB  1 
ATOM   14078 C CG  . PRO D 1 165 ? 49.859  -26.398 -15.980 1.00 64.33  ? 165 PRO D CG  1 
ATOM   14079 C CD  . PRO D 1 165 ? 49.485  -27.023 -17.319 1.00 65.39  ? 165 PRO D CD  1 
ATOM   14080 N N   . VAL D 1 166 ? 47.983  -30.103 -14.023 1.00 64.12  ? 166 VAL D N   1 
ATOM   14081 C CA  . VAL D 1 166 ? 46.866  -30.644 -13.274 1.00 63.38  ? 166 VAL D CA  1 
ATOM   14082 C C   . VAL D 1 166 ? 47.130  -30.495 -11.779 1.00 62.82  ? 166 VAL D C   1 
ATOM   14083 O O   . VAL D 1 166 ? 48.197  -30.820 -11.296 1.00 63.96  ? 166 VAL D O   1 
ATOM   14084 C CB  . VAL D 1 166 ? 46.720  -32.118 -13.674 1.00 64.79  ? 166 VAL D CB  1 
ATOM   14085 C CG1 . VAL D 1 166 ? 45.464  -32.773 -13.085 1.00 64.42  ? 166 VAL D CG1 1 
ATOM   14086 C CG2 . VAL D 1 166 ? 46.770  -32.272 -15.191 1.00 66.06  ? 166 VAL D CG2 1 
ATOM   14087 N N   . THR D 1 167 ? 46.153  -29.971 -11.047 1.00 62.38  ? 167 THR D N   1 
ATOM   14088 C CA  . THR D 1 167 ? 46.167  -29.972 -9.591  1.00 61.85  ? 167 THR D CA  1 
ATOM   14089 C C   . THR D 1 167 ? 44.738  -30.255 -9.080  1.00 62.23  ? 167 THR D C   1 
ATOM   14090 O O   . THR D 1 167 ? 43.885  -30.790 -9.800  1.00 61.94  ? 167 THR D O   1 
ATOM   14091 C CB  . THR D 1 167 ? 46.749  -28.629 -9.144  1.00 60.51  ? 167 THR D CB  1 
ATOM   14092 O OG1 . THR D 1 167 ? 46.832  -28.622 -7.721  1.00 59.50  ? 167 THR D OG1 1 
ATOM   14093 C CG2 . THR D 1 167 ? 45.917  -27.461 -9.643  1.00 59.53  ? 167 THR D CG2 1 
ATOM   14094 N N   . LEU D 1 168 ? 44.492  -29.953 -7.803  1.00 62.74  ? 168 LEU D N   1 
ATOM   14095 C CA  . LEU D 1 168 ? 43.195  -30.177 -7.197  1.00 63.75  ? 168 LEU D CA  1 
ATOM   14096 C C   . LEU D 1 168 ? 42.844  -28.950 -6.361  1.00 64.69  ? 168 LEU D C   1 
ATOM   14097 O O   . LEU D 1 168 ? 43.755  -28.271 -5.900  1.00 67.93  ? 168 LEU D O   1 
ATOM   14098 C CB  . LEU D 1 168 ? 43.231  -31.454 -6.362  1.00 64.09  ? 168 LEU D CB  1 
ATOM   14099 C CG  . LEU D 1 168 ? 43.667  -31.284 -4.907  1.00 63.95  ? 168 LEU D CG  1 
ATOM   14100 C CD1 . LEU D 1 168 ? 43.523  -32.542 -4.109  1.00 64.32  ? 168 LEU D CD1 1 
ATOM   14101 C CD2 . LEU D 1 168 ? 45.101  -30.856 -4.877  1.00 65.25  ? 168 LEU D CD2 1 
ATOM   14102 N N   . SER D 1 169 ? 41.545  -28.642 -6.229  1.00 65.17  ? 169 SER D N   1 
ATOM   14103 C CA  . SER D 1 169 ? 41.070  -27.624 -5.306  1.00 65.43  ? 169 SER D CA  1 
ATOM   14104 C C   . SER D 1 169 ? 41.009  -28.215 -3.902  1.00 64.40  ? 169 SER D C   1 
ATOM   14105 O O   . SER D 1 169 ? 39.969  -28.655 -3.437  1.00 64.97  ? 169 SER D O   1 
ATOM   14106 C CB  . SER D 1 169 ? 39.698  -27.086 -5.685  1.00 67.94  ? 169 SER D CB  1 
ATOM   14107 O OG  . SER D 1 169 ? 39.030  -27.825 -6.719  1.00 70.99  ? 169 SER D OG  1 
ATOM   14108 N N   . ALA D 1 170 ? 42.136  -28.322 -3.229  1.00 64.05  ? 170 ALA D N   1 
ATOM   14109 C CA  . ALA D 1 170 ? 42.084  -28.801 -1.864  1.00 64.50  ? 170 ALA D CA  1 
ATOM   14110 C C   . ALA D 1 170 ? 41.804  -27.594 -0.995  1.00 64.29  ? 170 ALA D C   1 
ATOM   14111 O O   . ALA D 1 170 ? 42.232  -26.495 -1.334  1.00 65.51  ? 170 ALA D O   1 
ATOM   14112 C CB  . ALA D 1 170 ? 43.379  -29.501 -1.492  1.00 65.29  ? 170 ALA D CB  1 
ATOM   14113 N N   . ASN D 1 171 ? 41.079  -27.801 0.101   1.00 64.48  ? 171 ASN D N   1 
ATOM   14114 C CA  . ASN D 1 171 ? 40.787  -26.712 1.016   1.00 63.97  ? 171 ASN D CA  1 
ATOM   14115 C C   . ASN D 1 171 ? 41.916  -26.560 2.032   1.00 64.72  ? 171 ASN D C   1 
ATOM   14116 O O   . ASN D 1 171 ? 42.254  -27.555 2.680   1.00 68.32  ? 171 ASN D O   1 
ATOM   14117 C CB  . ASN D 1 171 ? 39.501  -26.963 1.774   1.00 63.83  ? 171 ASN D CB  1 
ATOM   14118 C CG  . ASN D 1 171 ? 39.279  -25.888 2.808   1.00 64.02  ? 171 ASN D CG  1 
ATOM   14119 O OD1 . ASN D 1 171 ? 39.843  -25.956 3.906   1.00 62.92  ? 171 ASN D OD1 1 
ATOM   14120 N ND2 . ASN D 1 171 ? 38.451  -24.899 2.484   1.00 64.97  ? 171 ASN D ND2 1 
ATOM   14121 N N   . ALA D 1 172 ? 42.418  -25.327 2.231   1.00 61.02  ? 172 ALA D N   1 
ATOM   14122 C CA  . ALA D 1 172 ? 43.590  -25.130 3.057   1.00 60.49  ? 172 ALA D CA  1 
ATOM   14123 C C   . ALA D 1 172 ? 43.318  -25.298 4.544   1.00 60.39  ? 172 ALA D C   1 
ATOM   14124 O O   . ALA D 1 172 ? 44.208  -25.645 5.295   1.00 62.79  ? 172 ALA D O   1 
ATOM   14125 C CB  . ALA D 1 172 ? 44.205  -23.785 2.809   1.00 60.49  ? 172 ALA D CB  1 
ATOM   14126 N N   . MET D 1 173 ? 42.114  -25.075 5.010   1.00 60.12  ? 173 MET D N   1 
ATOM   14127 C CA  . MET D 1 173 ? 41.880  -25.239 6.435   1.00 61.79  ? 173 MET D CA  1 
ATOM   14128 C C   . MET D 1 173 ? 41.796  -26.712 6.862   1.00 64.36  ? 173 MET D C   1 
ATOM   14129 O O   . MET D 1 173 ? 42.036  -27.010 8.036   1.00 66.44  ? 173 MET D O   1 
ATOM   14130 C CB  . MET D 1 173 ? 40.587  -24.528 6.839   1.00 61.74  ? 173 MET D CB  1 
ATOM   14131 C CG  . MET D 1 173 ? 40.698  -23.012 6.819   1.00 60.75  ? 173 MET D CG  1 
ATOM   14132 S SD  . MET D 1 173 ? 41.785  -22.443 8.141   1.00 61.54  ? 173 MET D SD  1 
ATOM   14133 C CE  . MET D 1 173 ? 40.768  -22.799 9.586   1.00 61.77  ? 173 MET D CE  1 
ATOM   14134 N N   . ILE D 1 174 ? 41.473  -27.638 5.935   1.00 64.64  ? 174 ILE D N   1 
ATOM   14135 C CA  . ILE D 1 174 ? 41.227  -29.030 6.285   1.00 65.73  ? 174 ILE D CA  1 
ATOM   14136 C C   . ILE D 1 174 ? 42.175  -29.973 5.557   1.00 67.37  ? 174 ILE D C   1 
ATOM   14137 O O   . ILE D 1 174 ? 42.198  -31.180 5.854   1.00 68.56  ? 174 ILE D O   1 
ATOM   14138 C CB  . ILE D 1 174 ? 39.789  -29.451 5.939   1.00 65.94  ? 174 ILE D CB  1 
ATOM   14139 C CG1 . ILE D 1 174 ? 39.561  -29.342 4.435   1.00 65.56  ? 174 ILE D CG1 1 
ATOM   14140 C CG2 . ILE D 1 174 ? 38.741  -28.677 6.747   1.00 65.65  ? 174 ILE D CG2 1 
ATOM   14141 C CD1 . ILE D 1 174 ? 38.646  -30.417 3.894   1.00 66.46  ? 174 ILE D CD1 1 
ATOM   14142 N N   . SER D 1 175 ? 42.867  -29.461 4.539   1.00 68.17  ? 175 SER D N   1 
ATOM   14143 C CA  . SER D 1 175 ? 43.748  -30.322 3.768   1.00 70.60  ? 175 SER D CA  1 
ATOM   14144 C C   . SER D 1 175 ? 45.198  -29.823 3.833   1.00 70.47  ? 175 SER D C   1 
ATOM   14145 O O   . SER D 1 175 ? 46.054  -30.162 3.013   1.00 70.47  ? 175 SER D O   1 
ATOM   14146 C CB  . SER D 1 175 ? 43.188  -30.523 2.384   1.00 71.48  ? 175 SER D CB  1 
ATOM   14147 O OG  . SER D 1 175 ? 41.984  -31.292 2.474   1.00 74.47  ? 175 SER D OG  1 
ATOM   14148 N N   . ASP D 1 176 ? 45.504  -29.112 4.915   1.00 70.29  ? 176 ASP D N   1 
ATOM   14149 C CA  . ASP D 1 176 ? 46.864  -28.663 5.145   1.00 71.76  ? 176 ASP D CA  1 
ATOM   14150 C C   . ASP D 1 176 ? 47.834  -29.840 4.998   1.00 71.93  ? 176 ASP D C   1 
ATOM   14151 O O   . ASP D 1 176 ? 48.825  -29.746 4.271   1.00 71.65  ? 176 ASP D O   1 
ATOM   14152 C CB  . ASP D 1 176 ? 46.949  -27.865 6.442   1.00 72.52  ? 176 ASP D CB  1 
ATOM   14153 C CG  . ASP D 1 176 ? 46.209  -28.456 7.631   1.00 72.81  ? 176 ASP D CG  1 
ATOM   14154 O OD1 . ASP D 1 176 ? 45.423  -29.397 7.393   1.00 73.63  ? 176 ASP D OD1 1 
ATOM   14155 O OD2 . ASP D 1 176 ? 46.438  -27.984 8.771   1.00 71.81  ? 176 ASP D OD2 1 
ATOM   14156 N N   . TYR D 1 177 ? 47.528  -30.950 5.678   1.00 71.61  ? 177 TYR D N   1 
ATOM   14157 C CA  . TYR D 1 177 ? 48.458  -32.058 5.828   1.00 72.30  ? 177 TYR D CA  1 
ATOM   14158 C C   . TYR D 1 177 ? 48.812  -32.680 4.476   1.00 72.31  ? 177 TYR D C   1 
ATOM   14159 O O   . TYR D 1 177 ? 49.902  -33.237 4.304   1.00 75.33  ? 177 TYR D O   1 
ATOM   14160 C CB  . TYR D 1 177 ? 47.840  -33.152 6.706   1.00 74.10  ? 177 TYR D CB  1 
ATOM   14161 C CG  . TYR D 1 177 ? 46.591  -33.796 6.106   1.00 73.92  ? 177 TYR D CG  1 
ATOM   14162 C CD1 . TYR D 1 177 ? 45.318  -33.236 6.298   1.00 72.27  ? 177 TYR D CD1 1 
ATOM   14163 C CD2 . TYR D 1 177 ? 46.680  -34.943 5.325   1.00 73.34  ? 177 TYR D CD2 1 
ATOM   14164 C CE1 . TYR D 1 177 ? 44.182  -33.800 5.740   1.00 71.22  ? 177 TYR D CE1 1 
ATOM   14165 C CE2 . TYR D 1 177 ? 45.545  -35.516 4.766   1.00 73.01  ? 177 TYR D CE2 1 
ATOM   14166 C CZ  . TYR D 1 177 ? 44.300  -34.943 4.974   1.00 71.70  ? 177 TYR D CZ  1 
ATOM   14167 O OH  . TYR D 1 177 ? 43.188  -35.496 4.427   1.00 71.21  ? 177 TYR D OH  1 
ATOM   14168 N N   . MET D 1 178 ? 47.873  -32.626 3.529   1.00 69.69  ? 178 MET D N   1 
ATOM   14169 C CA  . MET D 1 178 ? 47.916  -33.441 2.325   1.00 69.01  ? 178 MET D CA  1 
ATOM   14170 C C   . MET D 1 178 ? 49.100  -33.079 1.438   1.00 68.98  ? 178 MET D C   1 
ATOM   14171 O O   . MET D 1 178 ? 49.298  -31.930 1.107   1.00 70.55  ? 178 MET D O   1 
ATOM   14172 C CB  . MET D 1 178 ? 46.632  -33.218 1.524   1.00 67.86  ? 178 MET D CB  1 
ATOM   14173 C CG  . MET D 1 178 ? 46.702  -33.620 0.066   1.00 67.52  ? 178 MET D CG  1 
ATOM   14174 S SD  . MET D 1 178 ? 45.093  -33.454 -0.729  1.00 66.04  ? 178 MET D SD  1 
ATOM   14175 C CE  . MET D 1 178 ? 44.061  -34.262 0.500   1.00 67.58  ? 178 MET D CE  1 
ATOM   14176 N N   . ASP D 1 179 ? 49.847  -34.077 1.002   1.00 70.05  ? 179 ASP D N   1 
ATOM   14177 C CA  . ASP D 1 179 ? 50.908  -33.895 0.036   1.00 70.95  ? 179 ASP D CA  1 
ATOM   14178 C C   . ASP D 1 179 ? 50.311  -33.462 -1.288  1.00 68.90  ? 179 ASP D C   1 
ATOM   14179 O O   . ASP D 1 179 ? 49.324  -34.045 -1.691  1.00 68.14  ? 179 ASP D O   1 
ATOM   14180 C CB  . ASP D 1 179 ? 51.599  -35.224 -0.203  1.00 74.43  ? 179 ASP D CB  1 
ATOM   14181 C CG  . ASP D 1 179 ? 52.748  -35.189 -1.189  1.00 76.78  ? 179 ASP D CG  1 
ATOM   14182 O OD1 . ASP D 1 179 ? 52.468  -35.149 -2.414  1.00 77.39  ? 179 ASP D OD1 1 
ATOM   14183 O OD2 . ASP D 1 179 ? 53.899  -35.173 -0.705  1.00 79.33  ? 179 ASP D OD2 1 
ATOM   14184 N N   . GLU D 1 180 ? 50.921  -32.483 -1.973  1.00 68.51  ? 180 GLU D N   1 
ATOM   14185 C CA  . GLU D 1 180 ? 50.469  -32.128 -3.315  1.00 67.48  ? 180 GLU D CA  1 
ATOM   14186 C C   . GLU D 1 180 ? 51.584  -32.335 -4.349  1.00 67.95  ? 180 GLU D C   1 
ATOM   14187 O O   . GLU D 1 180 ? 51.443  -31.922 -5.497  1.00 67.67  ? 180 GLU D O   1 
ATOM   14188 C CB  . GLU D 1 180 ? 49.898  -30.715 -3.417  1.00 66.39  ? 180 GLU D CB  1 
ATOM   14189 C CG  . GLU D 1 180 ? 48.699  -30.407 -2.515  1.00 66.06  ? 180 GLU D CG  1 
ATOM   14190 C CD  . GLU D 1 180 ? 47.992  -29.088 -2.848  1.00 65.81  ? 180 GLU D CD  1 
ATOM   14191 O OE1 . GLU D 1 180 ? 48.500  -28.404 -3.763  1.00 66.48  ? 180 GLU D OE1 1 
ATOM   14192 O OE2 . GLU D 1 180 ? 46.942  -28.723 -2.258  1.00 65.26  ? 180 GLU D OE2 1 
ATOM   14193 N N   . SER D 1 181 ? 52.649  -33.062 -3.993  1.00 68.34  ? 181 SER D N   1 
ATOM   14194 C CA  . SER D 1 181 ? 53.798  -33.166 -4.877  1.00 69.31  ? 181 SER D CA  1 
ATOM   14195 C C   . SER D 1 181 ? 53.529  -33.996 -6.131  1.00 69.51  ? 181 SER D C   1 
ATOM   14196 O O   . SER D 1 181 ? 54.283  -33.901 -7.092  1.00 70.28  ? 181 SER D O   1 
ATOM   14197 C CB  . SER D 1 181 ? 54.988  -33.700 -4.151  1.00 70.53  ? 181 SER D CB  1 
ATOM   14198 O OG  . SER D 1 181 ? 54.558  -34.565 -3.122  1.00 71.29  ? 181 SER D OG  1 
ATOM   14199 N N   . ILE D 1 182 ? 52.489  -34.830 -6.146  1.00 68.90  ? 182 ILE D N   1 
ATOM   14200 C CA  . ILE D 1 182 ? 52.156  -35.534 -7.378  1.00 69.10  ? 182 ILE D CA  1 
ATOM   14201 C C   . ILE D 1 182 ? 51.611  -34.564 -8.437  1.00 67.94  ? 182 ILE D C   1 
ATOM   14202 O O   . ILE D 1 182 ? 51.631  -34.861 -9.631  1.00 67.94  ? 182 ILE D O   1 
ATOM   14203 C CB  . ILE D 1 182 ? 51.192  -36.695 -7.101  1.00 69.30  ? 182 ILE D CB  1 
ATOM   14204 C CG1 . ILE D 1 182 ? 49.861  -36.230 -6.554  1.00 67.81  ? 182 ILE D CG1 1 
ATOM   14205 C CG2 . ILE D 1 182 ? 51.848  -37.707 -6.166  1.00 70.85  ? 182 ILE D CG2 1 
ATOM   14206 C CD1 . ILE D 1 182 ? 48.888  -37.370 -6.313  1.00 68.25  ? 182 ILE D CD1 1 
ATOM   14207 N N   . PHE D 1 183 ? 51.133  -33.391 -8.013  1.00 66.49  ? 183 PHE D N   1 
ATOM   14208 C CA  . PHE D 1 183 ? 50.527  -32.458 -8.945  1.00 65.91  ? 183 PHE D CA  1 
ATOM   14209 C C   . PHE D 1 183 ? 51.616  -31.568 -9.553  1.00 67.25  ? 183 PHE D C   1 
ATOM   14210 O O   . PHE D 1 183 ? 52.746  -31.463 -9.042  1.00 67.87  ? 183 PHE D O   1 
ATOM   14211 C CB  . PHE D 1 183 ? 49.427  -31.665 -8.234  1.00 64.49  ? 183 PHE D CB  1 
ATOM   14212 C CG  . PHE D 1 183 ? 48.340  -32.535 -7.608  1.00 64.26  ? 183 PHE D CG  1 
ATOM   14213 C CD1 . PHE D 1 183 ? 47.442  -33.249 -8.396  1.00 64.27  ? 183 PHE D CD1 1 
ATOM   14214 C CD2 . PHE D 1 183 ? 48.212  -32.628 -6.224  1.00 63.92  ? 183 PHE D CD2 1 
ATOM   14215 C CE1 . PHE D 1 183 ? 46.464  -34.048 -7.815  1.00 64.29  ? 183 PHE D CE1 1 
ATOM   14216 C CE2 . PHE D 1 183 ? 47.236  -33.425 -5.651  1.00 63.80  ? 183 PHE D CE2 1 
ATOM   14217 C CZ  . PHE D 1 183 ? 46.360  -34.132 -6.446  1.00 64.02  ? 183 PHE D CZ  1 
ATOM   14218 N N   . ASP D 1 184 ? 51.250  -30.948 -10.681 1.00 66.72  ? 184 ASP D N   1 
ATOM   14219 C CA  . ASP D 1 184 ? 52.128  -30.043 -11.380 1.00 66.72  ? 184 ASP D CA  1 
ATOM   14220 C C   . ASP D 1 184 ? 52.176  -28.723 -10.621 1.00 67.09  ? 184 ASP D C   1 
ATOM   14221 O O   . ASP D 1 184 ? 53.148  -27.975 -10.745 1.00 67.90  ? 184 ASP D O   1 
ATOM   14222 C CB  . ASP D 1 184 ? 51.621  -29.782 -12.786 1.00 66.42  ? 184 ASP D CB  1 
ATOM   14223 C CG  . ASP D 1 184 ? 51.616  -30.952 -13.752 1.00 67.54  ? 184 ASP D CG  1 
ATOM   14224 O OD1 . ASP D 1 184 ? 52.658  -31.659 -13.854 1.00 69.03  ? 184 ASP D OD1 1 
ATOM   14225 O OD2 . ASP D 1 184 ? 50.589  -31.116 -14.430 1.00 66.74  ? 184 ASP D OD2 1 
ATOM   14226 N N   . VAL D 1 185 ? 51.073  -28.402 -9.913  1.00 67.26  ? 185 VAL D N   1 
ATOM   14227 C CA  . VAL D 1 185 ? 50.856  -27.071 -9.355  1.00 66.21  ? 185 VAL D CA  1 
ATOM   14228 C C   . VAL D 1 185 ? 50.332  -27.219 -7.932  1.00 65.02  ? 185 VAL D C   1 
ATOM   14229 O O   . VAL D 1 185 ? 49.577  -28.154 -7.682  1.00 65.73  ? 185 VAL D O   1 
ATOM   14230 C CB  . VAL D 1 185 ? 49.846  -26.364 -10.273 1.00 66.03  ? 185 VAL D CB  1 
ATOM   14231 C CG1 . VAL D 1 185 ? 49.406  -25.008 -9.719  1.00 65.49  ? 185 VAL D CG1 1 
ATOM   14232 C CG2 . VAL D 1 185 ? 50.368  -26.209 -11.696 1.00 66.97  ? 185 VAL D CG2 1 
ATOM   14233 N N   . TYR D 1 186 ? 50.763  -26.345 -7.015  1.00 63.88  ? 186 TYR D N   1 
ATOM   14234 C CA  . TYR D 1 186 ? 50.151  -26.275 -5.697  1.00 63.82  ? 186 TYR D CA  1 
ATOM   14235 C C   . TYR D 1 186 ? 48.887  -25.404 -5.797  1.00 63.81  ? 186 TYR D C   1 
ATOM   14236 O O   . TYR D 1 186 ? 48.869  -24.405 -6.519  1.00 65.61  ? 186 TYR D O   1 
ATOM   14237 C CB  . TYR D 1 186 ? 51.206  -25.763 -4.708  1.00 64.38  ? 186 TYR D CB  1 
ATOM   14238 C CG  . TYR D 1 186 ? 52.400  -26.698 -4.536  1.00 66.98  ? 186 TYR D CG  1 
ATOM   14239 C CD1 . TYR D 1 186 ? 52.219  -28.084 -4.450  1.00 67.06  ? 186 TYR D CD1 1 
ATOM   14240 C CD2 . TYR D 1 186 ? 53.719  -26.216 -4.476  1.00 66.89  ? 186 TYR D CD2 1 
ATOM   14241 C CE1 . TYR D 1 186 ? 53.303  -28.935 -4.301  1.00 68.49  ? 186 TYR D CE1 1 
ATOM   14242 C CE2 . TYR D 1 186 ? 54.807  -27.064 -4.313  1.00 67.29  ? 186 TYR D CE2 1 
ATOM   14243 C CZ  . TYR D 1 186 ? 54.599  -28.427 -4.237  1.00 69.07  ? 186 TYR D CZ  1 
ATOM   14244 O OH  . TYR D 1 186 ? 55.636  -29.331 -4.107  1.00 71.46  ? 186 TYR D OH  1 
ATOM   14245 N N   . ALA D 1 187 ? 47.820  -25.751 -5.060  1.00 62.81  ? 187 ALA D N   1 
ATOM   14246 C CA  . ALA D 1 187 ? 46.584  -24.974 -5.054  1.00 61.19  ? 187 ALA D CA  1 
ATOM   14247 C C   . ALA D 1 187 ? 45.854  -25.159 -3.731  1.00 60.83  ? 187 ALA D C   1 
ATOM   14248 O O   . ALA D 1 187 ? 45.892  -26.244 -3.152  1.00 61.59  ? 187 ALA D O   1 
ATOM   14249 C CB  . ALA D 1 187 ? 45.708  -25.387 -6.211  1.00 61.17  ? 187 ALA D CB  1 
ATOM   14250 N N   . TYR D 1 188 ? 45.166  -24.114 -3.270  1.00 60.19  ? 188 TYR D N   1 
ATOM   14251 C CA  . TYR D 1 188 ? 44.295  -24.263 -2.112  1.00 61.66  ? 188 TYR D CA  1 
ATOM   14252 C C   . TYR D 1 188 ? 42.999  -23.423 -2.195  1.00 62.25  ? 188 TYR D C   1 
ATOM   14253 O O   . TYR D 1 188 ? 42.902  -22.400 -2.876  1.00 62.45  ? 188 TYR D O   1 
ATOM   14254 C CB  . TYR D 1 188 ? 45.146  -23.902 -0.892  1.00 61.63  ? 188 TYR D CB  1 
ATOM   14255 C CG  . TYR D 1 188 ? 46.198  -24.921 -0.477  1.00 63.56  ? 188 TYR D CG  1 
ATOM   14256 C CD1 . TYR D 1 188 ? 45.857  -26.073 0.226   1.00 64.10  ? 188 TYR D CD1 1 
ATOM   14257 C CD2 . TYR D 1 188 ? 47.543  -24.715 -0.756  1.00 64.13  ? 188 TYR D CD2 1 
ATOM   14258 C CE1 . TYR D 1 188 ? 46.819  -26.981 0.630   1.00 64.67  ? 188 TYR D CE1 1 
ATOM   14259 C CE2 . TYR D 1 188 ? 48.507  -25.629 -0.373  1.00 65.23  ? 188 TYR D CE2 1 
ATOM   14260 C CZ  . TYR D 1 188 ? 48.148  -26.766 0.322   1.00 66.04  ? 188 TYR D CZ  1 
ATOM   14261 O OH  . TYR D 1 188 ? 49.127  -27.668 0.667   1.00 69.83  ? 188 TYR D OH  1 
ATOM   14262 N N   . ASN D 1 189 ? 41.972  -23.853 -1.454  1.00 62.54  ? 189 ASN D N   1 
ATOM   14263 C CA  . ASN D 1 189 ? 40.815  -23.012 -1.212  1.00 62.84  ? 189 ASN D CA  1 
ATOM   14264 C C   . ASN D 1 189 ? 41.076  -22.277 0.101   1.00 61.98  ? 189 ASN D C   1 
ATOM   14265 O O   . ASN D 1 189 ? 40.976  -22.859 1.187   1.00 62.88  ? 189 ASN D O   1 
ATOM   14266 C CB  . ASN D 1 189 ? 39.517  -23.822 -1.249  1.00 63.80  ? 189 ASN D CB  1 
ATOM   14267 C CG  . ASN D 1 189 ? 39.138  -24.301 -2.639  1.00 64.84  ? 189 ASN D CG  1 
ATOM   14268 O OD1 . ASN D 1 189 ? 39.485  -23.668 -3.646  1.00 65.11  ? 189 ASN D OD1 1 
ATOM   14269 N ND2 . ASN D 1 189 ? 38.379  -25.387 -2.723  1.00 65.62  ? 189 ASN D ND2 1 
ATOM   14270 N N   . CYS D 1 190 ? 41.418  -20.993 -0.017  1.00 59.75  ? 190 CYS D N   1 
ATOM   14271 C CA  . CYS D 1 190 ? 41.921  -20.232 1.112   1.00 59.56  ? 190 CYS D CA  1 
ATOM   14272 C C   . CYS D 1 190 ? 40.841  -19.270 1.622   1.00 57.66  ? 190 CYS D C   1 
ATOM   14273 O O   . CYS D 1 190 ? 40.404  -18.394 0.895   1.00 56.38  ? 190 CYS D O   1 
ATOM   14274 C CB  . CYS D 1 190 ? 43.185  -19.476 0.708   1.00 60.68  ? 190 CYS D CB  1 
ATOM   14275 S SG  . CYS D 1 190 ? 44.477  -20.524 -0.027  1.00 63.15  ? 190 CYS D SG  1 
ATOM   14276 N N   . TYR D 1 191 ? 40.419  -19.430 2.878   1.00 56.90  ? 191 TYR D N   1 
ATOM   14277 C CA  . TYR D 1 191 ? 39.412  -18.570 3.461   1.00 57.04  ? 191 TYR D CA  1 
ATOM   14278 C C   . TYR D 1 191 ? 39.944  -18.075 4.806   1.00 58.80  ? 191 TYR D C   1 
ATOM   14279 O O   . TYR D 1 191 ? 40.301  -18.874 5.680   1.00 57.40  ? 191 TYR D O   1 
ATOM   14280 C CB  . TYR D 1 191 ? 38.006  -19.195 3.592   1.00 56.48  ? 191 TYR D CB  1 
ATOM   14281 C CG  . TYR D 1 191 ? 37.296  -19.493 2.278   1.00 55.61  ? 191 TYR D CG  1 
ATOM   14282 C CD1 . TYR D 1 191 ? 36.577  -18.508 1.628   1.00 55.86  ? 191 TYR D CD1 1 
ATOM   14283 C CD2 . TYR D 1 191 ? 37.345  -20.740 1.673   1.00 55.73  ? 191 TYR D CD2 1 
ATOM   14284 C CE1 . TYR D 1 191 ? 35.895  -18.751 0.442   1.00 55.72  ? 191 TYR D CE1 1 
ATOM   14285 C CE2 . TYR D 1 191 ? 36.692  -20.990 0.473   1.00 55.60  ? 191 TYR D CE2 1 
ATOM   14286 C CZ  . TYR D 1 191 ? 35.952  -19.999 -0.143  1.00 55.20  ? 191 TYR D CZ  1 
ATOM   14287 O OH  . TYR D 1 191 ? 35.324  -20.161 -1.343  1.00 54.79  ? 191 TYR D OH  1 
ATOM   14288 N N   . ASP D 1 192 ? 39.906  -16.730 4.944   1.00 61.93  ? 192 ASP D N   1 
ATOM   14289 C CA  . ASP D 1 192 ? 40.326  -15.998 6.124   1.00 63.94  ? 192 ASP D CA  1 
ATOM   14290 C C   . ASP D 1 192 ? 39.092  -15.642 6.932   1.00 63.97  ? 192 ASP D C   1 
ATOM   14291 O O   . ASP D 1 192 ? 38.494  -14.620 6.655   1.00 66.60  ? 192 ASP D O   1 
ATOM   14292 C CB  . ASP D 1 192 ? 41.015  -14.696 5.743   1.00 65.96  ? 192 ASP D CB  1 
ATOM   14293 C CG  . ASP D 1 192 ? 41.546  -13.875 6.913   1.00 69.83  ? 192 ASP D CG  1 
ATOM   14294 O OD1 . ASP D 1 192 ? 41.370  -14.367 8.060   1.00 70.10  ? 192 ASP D OD1 1 
ATOM   14295 O OD2 . ASP D 1 192 ? 42.114  -12.747 6.670   1.00 71.41  ? 192 ASP D OD2 1 
ATOM   14296 N N   . HIS D 1 193 ? 38.702  -16.491 7.890   1.00 63.89  ? 193 HIS D N   1 
ATOM   14297 C CA  . HIS D 1 193 ? 37.691  -16.137 8.873   1.00 64.16  ? 193 HIS D CA  1 
ATOM   14298 C C   . HIS D 1 193 ? 38.350  -15.932 10.234  1.00 65.40  ? 193 HIS D C   1 
ATOM   14299 O O   . HIS D 1 193 ? 37.720  -16.114 11.258  1.00 66.59  ? 193 HIS D O   1 
ATOM   14300 C CB  . HIS D 1 193 ? 36.623  -17.227 9.035   1.00 65.01  ? 193 HIS D CB  1 
ATOM   14301 C CG  . HIS D 1 193 ? 36.039  -17.769 7.776   1.00 65.44  ? 193 HIS D CG  1 
ATOM   14302 N ND1 . HIS D 1 193 ? 35.290  -17.011 6.892   1.00 66.15  ? 193 HIS D ND1 1 
ATOM   14303 C CD2 . HIS D 1 193 ? 36.116  -19.011 7.266   1.00 64.55  ? 193 HIS D CD2 1 
ATOM   14304 C CE1 . HIS D 1 193 ? 34.924  -17.783 5.875   1.00 65.84  ? 193 HIS D CE1 1 
ATOM   14305 N NE2 . HIS D 1 193 ? 35.426  -19.004 6.089   1.00 65.46  ? 193 HIS D NE2 1 
ATOM   14306 N N   . ASN D 1 194 ? 39.637  -15.582 10.257  1.00 67.07  ? 194 ASN D N   1 
ATOM   14307 C CA  . ASN D 1 194 ? 40.366  -15.385 11.506  1.00 67.07  ? 194 ASN D CA  1 
ATOM   14308 C C   . ASN D 1 194 ? 39.927  -16.381 12.594  1.00 67.17  ? 194 ASN D C   1 
ATOM   14309 O O   . ASN D 1 194 ? 39.510  -15.952 13.668  1.00 67.61  ? 194 ASN D O   1 
ATOM   14310 C CB  . ASN D 1 194 ? 40.240  -13.937 11.964  1.00 65.92  ? 194 ASN D CB  1 
ATOM   14311 C CG  . ASN D 1 194 ? 41.001  -13.674 13.240  1.00 68.09  ? 194 ASN D CG  1 
ATOM   14312 O OD1 . ASN D 1 194 ? 40.421  -13.207 14.217  1.00 69.32  ? 194 ASN D OD1 1 
ATOM   14313 N ND2 . ASN D 1 194 ? 42.304  -13.917 13.260  1.00 70.80  ? 194 ASN D ND2 1 
ATOM   14314 N N   . GLU D 1 195 ? 40.060  -17.698 12.338  1.00 65.28  ? 195 GLU D N   1 
ATOM   14315 C CA  . GLU D 1 195 ? 39.801  -18.725 13.349  1.00 65.16  ? 195 GLU D CA  1 
ATOM   14316 C C   . GLU D 1 195 ? 40.801  -19.882 13.198  1.00 65.34  ? 195 GLU D C   1 
ATOM   14317 O O   . GLU D 1 195 ? 41.282  -20.171 12.102  1.00 64.63  ? 195 GLU D O   1 
ATOM   14318 C CB  . GLU D 1 195 ? 38.370  -19.257 13.249  1.00 64.04  ? 195 GLU D CB  1 
ATOM   14319 C CG  . GLU D 1 195 ? 38.127  -19.929 11.902  1.00 62.88  ? 195 GLU D CG  1 
ATOM   14320 C CD  . GLU D 1 195 ? 36.715  -20.291 11.510  1.00 62.74  ? 195 GLU D CD  1 
ATOM   14321 O OE1 . GLU D 1 195 ? 35.786  -20.127 12.348  1.00 63.77  ? 195 GLU D OE1 1 
ATOM   14322 O OE2 . GLU D 1 195 ? 36.585  -20.699 10.323  1.00 61.25  ? 195 GLU D OE2 1 
ATOM   14323 N N   . GLY D 1 196 ? 41.096  -20.578 14.300  1.00 65.78  ? 196 GLY D N   1 
ATOM   14324 C CA  . GLY D 1 196 ? 42.085  -21.640 14.265  1.00 67.30  ? 196 GLY D CA  1 
ATOM   14325 C C   . GLY D 1 196 ? 43.393  -21.185 13.618  1.00 67.37  ? 196 GLY D C   1 
ATOM   14326 O O   . GLY D 1 196 ? 44.059  -20.301 14.155  1.00 68.87  ? 196 GLY D O   1 
ATOM   14327 N N   . GLN D 1 197 ? 43.723  -21.748 12.443  1.00 66.51  ? 197 GLN D N   1 
ATOM   14328 C CA  . GLN D 1 197 ? 45.011  -21.512 11.805  1.00 66.94  ? 197 GLN D CA  1 
ATOM   14329 C C   . GLN D 1 197 ? 45.192  -20.055 11.367  1.00 66.67  ? 197 GLN D C   1 
ATOM   14330 O O   . GLN D 1 197 ? 46.302  -19.524 11.455  1.00 68.60  ? 197 GLN D O   1 
ATOM   14331 C CB  . GLN D 1 197 ? 45.220  -22.444 10.617  1.00 67.13  ? 197 GLN D CB  1 
ATOM   14332 C CG  . GLN D 1 197 ? 45.367  -23.907 11.030  1.00 68.82  ? 197 GLN D CG  1 
ATOM   14333 C CD  . GLN D 1 197 ? 44.077  -24.684 10.947  1.00 68.63  ? 197 GLN D CD  1 
ATOM   14334 O OE1 . GLN D 1 197 ? 43.062  -24.386 11.598  1.00 66.41  ? 197 GLN D OE1 1 
ATOM   14335 N NE2 . GLN D 1 197 ? 44.140  -25.715 10.122  1.00 70.23  ? 197 GLN D NE2 1 
ATOM   14336 N N   . THR D 1 198 ? 44.113  -19.413 10.898  1.00 64.19  ? 198 THR D N   1 
ATOM   14337 C CA  . THR D 1 198 ? 44.194  -18.047 10.413  1.00 62.42  ? 198 THR D CA  1 
ATOM   14338 C C   . THR D 1 198 ? 44.113  -17.073 11.588  1.00 63.38  ? 198 THR D C   1 
ATOM   14339 O O   . THR D 1 198 ? 44.200  -15.865 11.386  1.00 62.81  ? 198 THR D O   1 
ATOM   14340 C CB  . THR D 1 198 ? 43.112  -17.768 9.367   1.00 60.68  ? 198 THR D CB  1 
ATOM   14341 O OG1 . THR D 1 198 ? 41.825  -18.061 9.917   1.00 61.28  ? 198 THR D OG1 1 
ATOM   14342 C CG2 . THR D 1 198 ? 43.336  -18.543 8.082   1.00 59.75  ? 198 THR D CG2 1 
ATOM   14343 N N   . ALA D 1 199 ? 43.930  -17.592 12.810  1.00 64.76  ? 199 ALA D N   1 
ATOM   14344 C CA  . ALA D 1 199 ? 43.882  -16.750 13.999  1.00 64.93  ? 199 ALA D CA  1 
ATOM   14345 C C   . ALA D 1 199 ? 45.265  -16.712 14.650  1.00 66.40  ? 199 ALA D C   1 
ATOM   14346 O O   . ALA D 1 199 ? 45.701  -15.664 15.133  1.00 65.43  ? 199 ALA D O   1 
ATOM   14347 C CB  . ALA D 1 199 ? 42.812  -17.233 14.963  1.00 64.55  ? 199 ALA D CB  1 
ATOM   14348 N N   . THR D 1 200 ? 45.947  -17.866 14.654  1.00 67.22  ? 200 THR D N   1 
ATOM   14349 C CA  . THR D 1 200 ? 47.283  -17.937 15.212  1.00 69.39  ? 200 THR D CA  1 
ATOM   14350 C C   . THR D 1 200 ? 48.295  -17.346 14.223  1.00 69.28  ? 200 THR D C   1 
ATOM   14351 O O   . THR D 1 200 ? 49.052  -16.442 14.559  1.00 69.84  ? 200 THR D O   1 
ATOM   14352 C CB  . THR D 1 200 ? 47.603  -19.381 15.594  1.00 71.54  ? 200 THR D CB  1 
ATOM   14353 O OG1 . THR D 1 200 ? 47.668  -20.171 14.404  1.00 71.36  ? 200 THR D OG1 1 
ATOM   14354 C CG2 . THR D 1 200 ? 46.589  -19.906 16.597  1.00 72.02  ? 200 THR D CG2 1 
ATOM   14355 N N   . MET D 1 201 ? 48.332  -17.853 12.992  1.00 68.89  ? 201 MET D N   1 
ATOM   14356 C CA  . MET D 1 201 ? 49.378  -17.448 12.062  1.00 68.76  ? 201 MET D CA  1 
ATOM   14357 C C   . MET D 1 201 ? 48.895  -16.249 11.257  1.00 66.39  ? 201 MET D C   1 
ATOM   14358 O O   . MET D 1 201 ? 49.679  -15.442 10.768  1.00 67.13  ? 201 MET D O   1 
ATOM   14359 C CB  . MET D 1 201 ? 49.765  -18.625 11.151  1.00 69.57  ? 201 MET D CB  1 
ATOM   14360 C CG  . MET D 1 201 ? 50.321  -19.824 11.906  1.00 70.41  ? 201 MET D CG  1 
ATOM   14361 S SD  . MET D 1 201 ? 50.380  -21.353 10.948  1.00 72.20  ? 201 MET D SD  1 
ATOM   14362 C CE  . MET D 1 201 ? 48.659  -21.800 11.225  1.00 73.40  ? 201 MET D CE  1 
ATOM   14363 N N   . GLY D 1 202 ? 47.581  -16.115 11.125  1.00 64.18  ? 202 GLY D N   1 
ATOM   14364 C CA  . GLY D 1 202 ? 47.057  -15.138 10.197  1.00 62.29  ? 202 GLY D CA  1 
ATOM   14365 C C   . GLY D 1 202 ? 47.112  -15.677 8.771   1.00 61.35  ? 202 GLY D C   1 
ATOM   14366 O O   . GLY D 1 202 ? 47.854  -16.621 8.469   1.00 60.96  ? 202 GLY D O   1 
ATOM   14367 N N   . PHE D 1 203 ? 46.313  -15.029 7.911   1.00 60.45  ? 203 PHE D N   1 
ATOM   14368 C CA  . PHE D 1 203 ? 46.010  -15.515 6.576   1.00 59.80  ? 203 PHE D CA  1 
ATOM   14369 C C   . PHE D 1 203 ? 47.294  -15.605 5.746   1.00 60.62  ? 203 PHE D C   1 
ATOM   14370 O O   . PHE D 1 203 ? 47.629  -16.682 5.252   1.00 60.11  ? 203 PHE D O   1 
ATOM   14371 C CB  . PHE D 1 203 ? 44.926  -14.607 5.981   1.00 58.50  ? 203 PHE D CB  1 
ATOM   14372 C CG  . PHE D 1 203 ? 44.214  -15.208 4.781   1.00 58.05  ? 203 PHE D CG  1 
ATOM   14373 C CD1 . PHE D 1 203 ? 43.672  -16.488 4.840   1.00 58.57  ? 203 PHE D CD1 1 
ATOM   14374 C CD2 . PHE D 1 203 ? 44.132  -14.522 3.580   1.00 57.49  ? 203 PHE D CD2 1 
ATOM   14375 C CE1 . PHE D 1 203 ? 43.031  -17.031 3.745   1.00 58.03  ? 203 PHE D CE1 1 
ATOM   14376 C CE2 . PHE D 1 203 ? 43.488  -15.073 2.485   1.00 57.12  ? 203 PHE D CE2 1 
ATOM   14377 C CZ  . PHE D 1 203 ? 42.940  -16.320 2.572   1.00 57.51  ? 203 PHE D CZ  1 
ATOM   14378 N N   . LYS D 1 204 ? 48.016  -14.480 5.596   1.00 61.38  ? 204 LYS D N   1 
ATOM   14379 C CA  . LYS D 1 204 ? 49.194  -14.476 4.749   1.00 62.77  ? 204 LYS D CA  1 
ATOM   14380 C C   . LYS D 1 204 ? 50.149  -15.584 5.191   1.00 65.01  ? 204 LYS D C   1 
ATOM   14381 O O   . LYS D 1 204 ? 50.564  -16.420 4.385   1.00 66.25  ? 204 LYS D O   1 
ATOM   14382 C CB  . LYS D 1 204 ? 49.930  -13.140 4.784   1.00 64.06  ? 204 LYS D CB  1 
ATOM   14383 C CG  . LYS D 1 204 ? 51.348  -13.123 4.200   1.00 64.98  ? 204 LYS D CG  1 
ATOM   14384 C CD  . LYS D 1 204 ? 52.256  -12.025 4.757   1.00 65.18  ? 204 LYS D CD  1 
ATOM   14385 C CE  . LYS D 1 204 ? 53.732  -12.115 4.339   1.00 64.30  ? 204 LYS D CE  1 
ATOM   14386 N NZ  . LYS D 1 204 ? 54.605  -11.458 5.320   1.00 64.10  ? 204 LYS D NZ  1 
ATOM   14387 N N   . ASP D 1 205 ? 50.476  -15.616 6.486   1.00 65.53  ? 205 ASP D N   1 
ATOM   14388 C CA  . ASP D 1 205 ? 51.483  -16.546 6.982   1.00 65.05  ? 205 ASP D CA  1 
ATOM   14389 C C   . ASP D 1 205 ? 51.031  -18.002 6.878   1.00 66.02  ? 205 ASP D C   1 
ATOM   14390 O O   . ASP D 1 205 ? 51.818  -18.872 6.469   1.00 66.38  ? 205 ASP D O   1 
ATOM   14391 C CB  . ASP D 1 205 ? 51.895  -16.218 8.407   1.00 64.81  ? 205 ASP D CB  1 
ATOM   14392 C CG  . ASP D 1 205 ? 52.836  -15.032 8.574   1.00 64.08  ? 205 ASP D CG  1 
ATOM   14393 O OD1 . ASP D 1 205 ? 53.243  -14.429 7.543   1.00 63.34  ? 205 ASP D OD1 1 
ATOM   14394 O OD2 . ASP D 1 205 ? 53.127  -14.713 9.745   1.00 63.66  ? 205 ASP D OD2 1 
ATOM   14395 N N   . TYR D 1 206 ? 49.786  -18.281 7.290   1.00 66.49  ? 206 TYR D N   1 
ATOM   14396 C CA  . TYR D 1 206 ? 49.302  -19.653 7.280   1.00 66.96  ? 206 TYR D CA  1 
ATOM   14397 C C   . TYR D 1 206 ? 49.454  -20.211 5.875   1.00 66.07  ? 206 TYR D C   1 
ATOM   14398 O O   . TYR D 1 206 ? 50.107  -21.235 5.686   1.00 66.76  ? 206 TYR D O   1 
ATOM   14399 C CB  . TYR D 1 206 ? 47.848  -19.747 7.717   1.00 67.66  ? 206 TYR D CB  1 
ATOM   14400 C CG  . TYR D 1 206 ? 47.242  -21.132 7.567   1.00 68.66  ? 206 TYR D CG  1 
ATOM   14401 C CD1 . TYR D 1 206 ? 47.897  -22.248 8.043   1.00 70.26  ? 206 TYR D CD1 1 
ATOM   14402 C CD2 . TYR D 1 206 ? 46.019  -21.318 6.942   1.00 67.70  ? 206 TYR D CD2 1 
ATOM   14403 C CE1 . TYR D 1 206 ? 47.344  -23.512 7.922   1.00 71.85  ? 206 TYR D CE1 1 
ATOM   14404 C CE2 . TYR D 1 206 ? 45.470  -22.579 6.791   1.00 68.17  ? 206 TYR D CE2 1 
ATOM   14405 C CZ  . TYR D 1 206 ? 46.128  -23.682 7.294   1.00 69.97  ? 206 TYR D CZ  1 
ATOM   14406 O OH  . TYR D 1 206 ? 45.648  -24.957 7.203   1.00 71.83  ? 206 TYR D OH  1 
ATOM   14407 N N   . ILE D 1 207 ? 48.917  -19.485 4.891   1.00 64.36  ? 207 ILE D N   1 
ATOM   14408 C CA  . ILE D 1 207 ? 48.981  -19.978 3.532   1.00 65.03  ? 207 ILE D CA  1 
ATOM   14409 C C   . ILE D 1 207 ? 50.428  -20.082 3.080   1.00 67.83  ? 207 ILE D C   1 
ATOM   14410 O O   . ILE D 1 207 ? 50.754  -21.038 2.385   1.00 70.37  ? 207 ILE D O   1 
ATOM   14411 C CB  . ILE D 1 207 ? 48.143  -19.133 2.567   1.00 63.68  ? 207 ILE D CB  1 
ATOM   14412 C CG1 . ILE D 1 207 ? 46.696  -19.179 2.957   1.00 62.62  ? 207 ILE D CG1 1 
ATOM   14413 C CG2 . ILE D 1 207 ? 48.323  -19.609 1.129   1.00 64.24  ? 207 ILE D CG2 1 
ATOM   14414 C CD1 . ILE D 1 207 ? 46.166  -20.574 3.182   1.00 62.37  ? 207 ILE D CD1 1 
ATOM   14415 N N   . LYS D 1 208 ? 51.250  -19.098 3.475   1.00 69.83  ? 208 LYS D N   1 
ATOM   14416 C CA  . LYS D 1 208 ? 52.661  -19.022 3.128   1.00 71.82  ? 208 LYS D CA  1 
ATOM   14417 C C   . LYS D 1 208 ? 53.387  -20.220 3.735   1.00 73.95  ? 208 LYS D C   1 
ATOM   14418 O O   . LYS D 1 208 ? 54.280  -20.782 3.103   1.00 75.29  ? 208 LYS D O   1 
ATOM   14419 C CB  . LYS D 1 208 ? 53.279  -17.690 3.598   1.00 72.63  ? 208 LYS D CB  1 
ATOM   14420 C CG  . LYS D 1 208 ? 54.801  -17.531 3.438   1.00 75.55  ? 208 LYS D CG  1 
ATOM   14421 C CD  . LYS D 1 208 ? 55.355  -16.101 3.454   1.00 77.68  ? 208 LYS D CD  1 
ATOM   14422 C CE  . LYS D 1 208 ? 55.693  -15.493 4.789   1.00 78.42  ? 208 LYS D CE  1 
ATOM   14423 N NZ  . LYS D 1 208 ? 56.947  -16.028 5.298   1.00 80.56  ? 208 LYS D NZ  1 
ATOM   14424 N N   . GLY D 1 209 ? 52.997  -20.604 4.960   1.00 74.34  ? 209 GLY D N   1 
ATOM   14425 C CA  . GLY D 1 209 ? 53.615  -21.735 5.645   1.00 74.51  ? 209 GLY D CA  1 
ATOM   14426 C C   . GLY D 1 209 ? 53.353  -23.057 4.926   1.00 73.19  ? 209 GLY D C   1 
ATOM   14427 O O   . GLY D 1 209 ? 54.205  -23.946 4.903   1.00 73.32  ? 209 GLY D O   1 
ATOM   14428 N N   . LEU D 1 210 ? 52.163  -23.190 4.333   1.00 71.81  ? 210 LEU D N   1 
ATOM   14429 C CA  . LEU D 1 210 ? 51.887  -24.375 3.539   1.00 72.79  ? 210 LEU D CA  1 
ATOM   14430 C C   . LEU D 1 210 ? 52.842  -24.393 2.350   1.00 73.54  ? 210 LEU D C   1 
ATOM   14431 O O   . LEU D 1 210 ? 53.471  -25.422 2.068   1.00 74.12  ? 210 LEU D O   1 
ATOM   14432 C CB  . LEU D 1 210 ? 50.424  -24.473 3.126   1.00 71.24  ? 210 LEU D CB  1 
ATOM   14433 C CG  . LEU D 1 210 ? 49.431  -24.514 4.297   1.00 71.42  ? 210 LEU D CG  1 
ATOM   14434 C CD1 . LEU D 1 210 ? 47.979  -24.538 3.797   1.00 71.37  ? 210 LEU D CD1 1 
ATOM   14435 C CD2 . LEU D 1 210 ? 49.686  -25.670 5.258   1.00 70.72  ? 210 LEU D CD2 1 
ATOM   14436 N N   . ASN D 1 211 ? 53.039  -23.215 1.748   1.00 71.74  ? 211 ASN D N   1 
ATOM   14437 C CA  . ASN D 1 211 ? 53.838  -23.140 0.543   1.00 71.56  ? 211 ASN D CA  1 
ATOM   14438 C C   . ASN D 1 211 ? 55.288  -23.516 0.844   1.00 73.74  ? 211 ASN D C   1 
ATOM   14439 O O   . ASN D 1 211 ? 55.952  -24.135 0.008   1.00 73.99  ? 211 ASN D O   1 
ATOM   14440 C CB  . ASN D 1 211 ? 53.722  -21.803 -0.167  1.00 69.45  ? 211 ASN D CB  1 
ATOM   14441 C CG  . ASN D 1 211 ? 53.868  -22.034 -1.648  1.00 70.49  ? 211 ASN D CG  1 
ATOM   14442 O OD1 . ASN D 1 211 ? 53.402  -23.069 -2.145  1.00 74.08  ? 211 ASN D OD1 1 
ATOM   14443 N ND2 . ASN D 1 211 ? 54.500  -21.121 -2.368  1.00 70.99  ? 211 ASN D ND2 1 
ATOM   14444 N N   . GLU D 1 212 ? 55.755  -23.173 2.053   1.00 73.66  ? 212 GLU D N   1 
ATOM   14445 C CA  . GLU D 1 212 ? 57.112  -23.488 2.481   1.00 74.32  ? 212 GLU D CA  1 
ATOM   14446 C C   . GLU D 1 212 ? 57.233  -24.977 2.820   1.00 75.29  ? 212 GLU D C   1 
ATOM   14447 O O   . GLU D 1 212 ? 58.263  -25.599 2.555   1.00 76.61  ? 212 GLU D O   1 
ATOM   14448 C CB  . GLU D 1 212 ? 57.541  -22.528 3.593   1.00 73.70  ? 212 GLU D CB  1 
ATOM   14449 C CG  . GLU D 1 212 ? 58.015  -21.199 3.011   1.00 74.11  ? 212 GLU D CG  1 
ATOM   14450 C CD  . GLU D 1 212 ? 57.981  -20.034 3.971   1.00 75.51  ? 212 GLU D CD  1 
ATOM   14451 O OE1 . GLU D 1 212 ? 57.585  -20.341 5.113   1.00 78.67  ? 212 GLU D OE1 1 
ATOM   14452 O OE2 . GLU D 1 212 ? 58.294  -18.865 3.609   1.00 74.73  ? 212 GLU D OE2 1 
ATOM   14453 N N   . LEU D 1 213 ? 56.188  -25.554 3.417   1.00 74.47  ? 213 LEU D N   1 
ATOM   14454 C CA  . LEU D 1 213 ? 56.171  -26.988 3.622   1.00 74.59  ? 213 LEU D CA  1 
ATOM   14455 C C   . LEU D 1 213 ? 56.035  -27.669 2.266   1.00 73.77  ? 213 LEU D C   1 
ATOM   14456 O O   . LEU D 1 213 ? 56.562  -28.740 2.085   1.00 73.10  ? 213 LEU D O   1 
ATOM   14457 C CB  . LEU D 1 213 ? 55.046  -27.412 4.561   1.00 75.12  ? 213 LEU D CB  1 
ATOM   14458 C CG  . LEU D 1 213 ? 55.226  -27.041 6.035   1.00 75.44  ? 213 LEU D CG  1 
ATOM   14459 C CD1 . LEU D 1 213 ? 53.898  -27.072 6.779   1.00 74.02  ? 213 LEU D CD1 1 
ATOM   14460 C CD2 . LEU D 1 213 ? 56.233  -27.961 6.685   1.00 75.61  ? 213 LEU D CD2 1 
ATOM   14461 N N   . ASN D 1 214 ? 55.312  -27.091 1.298   1.00 73.51  ? 214 ASN D N   1 
ATOM   14462 C CA  . ASN D 1 214 ? 55.203  -27.789 0.022   1.00 72.74  ? 214 ASN D CA  1 
ATOM   14463 C C   . ASN D 1 214 ? 56.529  -27.765 -0.729  1.00 72.83  ? 214 ASN D C   1 
ATOM   14464 O O   . ASN D 1 214 ? 56.657  -28.535 -1.666  1.00 74.47  ? 214 ASN D O   1 
ATOM   14465 C CB  . ASN D 1 214 ? 54.075  -27.312 -0.878  1.00 71.15  ? 214 ASN D CB  1 
ATOM   14466 C CG  . ASN D 1 214 ? 52.742  -27.705 -0.301  1.00 71.72  ? 214 ASN D CG  1 
ATOM   14467 O OD1 . ASN D 1 214 ? 52.635  -28.787 0.273   1.00 71.95  ? 214 ASN D OD1 1 
ATOM   14468 N ND2 . ASN D 1 214 ? 51.749  -26.824 -0.362  1.00 73.25  ? 214 ASN D ND2 1 
ATOM   14469 N N   . GLY D 1 215 ? 57.456  -26.860 -0.357  1.00 72.05  ? 215 GLY D N   1 
ATOM   14470 C CA  . GLY D 1 215 ? 58.842  -26.901 -0.797  1.00 72.33  ? 215 GLY D CA  1 
ATOM   14471 C C   . GLY D 1 215 ? 59.216  -25.879 -1.875  1.00 72.14  ? 215 GLY D C   1 
ATOM   14472 O O   . GLY D 1 215 ? 60.302  -25.943 -2.430  1.00 74.04  ? 215 GLY D O   1 
ATOM   14473 N N   . LEU D 1 216 ? 58.343  -24.936 -2.215  1.00 70.60  ? 216 LEU D N   1 
ATOM   14474 C CA  . LEU D 1 216 ? 58.709  -23.832 -3.093  1.00 69.84  ? 216 LEU D CA  1 
ATOM   14475 C C   . LEU D 1 216 ? 59.187  -24.281 -4.484  1.00 70.08  ? 216 LEU D C   1 
ATOM   14476 O O   . LEU D 1 216 ? 59.828  -23.538 -5.195  1.00 69.29  ? 216 LEU D O   1 
ATOM   14477 C CB  . LEU D 1 216 ? 59.757  -23.031 -2.323  1.00 71.12  ? 216 LEU D CB  1 
ATOM   14478 C CG  . LEU D 1 216 ? 59.346  -22.487 -0.942  1.00 71.39  ? 216 LEU D CG  1 
ATOM   14479 C CD1 . LEU D 1 216 ? 60.418  -21.514 -0.393  1.00 71.85  ? 216 LEU D CD1 1 
ATOM   14480 C CD2 . LEU D 1 216 ? 57.950  -21.792 -0.919  1.00 69.87  ? 216 LEU D CD2 1 
ATOM   14481 N N   . ASP D 1 217 ? 58.797  -25.466 -4.957  1.00 71.19  ? 217 ASP D N   1 
ATOM   14482 C CA  . ASP D 1 217 ? 59.320  -25.974 -6.223  1.00 72.16  ? 217 ASP D CA  1 
ATOM   14483 C C   . ASP D 1 217 ? 58.254  -25.984 -7.323  1.00 71.81  ? 217 ASP D C   1 
ATOM   14484 O O   . ASP D 1 217 ? 58.453  -26.631 -8.353  1.00 71.74  ? 217 ASP D O   1 
ATOM   14485 C CB  . ASP D 1 217 ? 59.883  -27.371 -6.054  1.00 72.87  ? 217 ASP D CB  1 
ATOM   14486 C CG  . ASP D 1 217 ? 58.913  -28.361 -5.446  1.00 72.67  ? 217 ASP D CG  1 
ATOM   14487 O OD1 . ASP D 1 217 ? 57.953  -27.891 -4.830  1.00 72.86  ? 217 ASP D OD1 1 
ATOM   14488 O OD2 . ASP D 1 217 ? 59.097  -29.577 -5.636  1.00 74.17  ? 217 ASP D OD2 1 
ATOM   14489 N N   . LYS D 1 218 ? 57.121  -25.296 -7.103  1.00 70.52  ? 218 LYS D N   1 
ATOM   14490 C CA  . LYS D 1 218 ? 56.056  -25.272 -8.094  1.00 70.39  ? 218 LYS D CA  1 
ATOM   14491 C C   . LYS D 1 218 ? 55.290  -23.957 -8.028  1.00 68.77  ? 218 LYS D C   1 
ATOM   14492 O O   . LYS D 1 218 ? 55.305  -23.257 -7.016  1.00 68.01  ? 218 LYS D O   1 
ATOM   14493 C CB  . LYS D 1 218 ? 55.071  -26.430 -7.905  1.00 71.86  ? 218 LYS D CB  1 
ATOM   14494 C CG  . LYS D 1 218 ? 55.781  -27.800 -7.866  1.00 74.72  ? 218 LYS D CG  1 
ATOM   14495 C CD  . LYS D 1 218 ? 55.001  -29.104 -7.959  1.00 74.58  ? 218 LYS D CD  1 
ATOM   14496 C CE  . LYS D 1 218 ? 56.001  -30.192 -8.192  1.00 76.97  ? 218 LYS D CE  1 
ATOM   14497 N NZ  . LYS D 1 218 ? 55.284  -31.463 -8.266  1.00 78.62  ? 218 LYS D NZ  1 
ATOM   14498 N N   . PRO D 1 219 ? 54.608  -23.573 -9.128  1.00 67.68  ? 219 PRO D N   1 
ATOM   14499 C CA  . PRO D 1 219 ? 53.619  -22.520 -9.057  1.00 66.24  ? 219 PRO D CA  1 
ATOM   14500 C C   . PRO D 1 219 ? 52.620  -22.906 -7.975  1.00 65.98  ? 219 PRO D C   1 
ATOM   14501 O O   . PRO D 1 219 ? 52.312  -24.083 -7.794  1.00 68.09  ? 219 PRO D O   1 
ATOM   14502 C CB  . PRO D 1 219 ? 53.017  -22.498 -10.450 1.00 66.23  ? 219 PRO D CB  1 
ATOM   14503 C CG  . PRO D 1 219 ? 54.112  -23.019 -11.312 1.00 67.76  ? 219 PRO D CG  1 
ATOM   14504 C CD  . PRO D 1 219 ? 54.725  -24.136 -10.482 1.00 68.49  ? 219 PRO D CD  1 
ATOM   14505 N N   . PHE D 1 220 ? 52.167  -21.882 -7.252  1.00 65.83  ? 220 PHE D N   1 
ATOM   14506 C CA  . PHE D 1 220 ? 51.127  -21.971 -6.251  1.00 65.69  ? 220 PHE D CA  1 
ATOM   14507 C C   . PHE D 1 220 ? 50.040  -20.949 -6.586  1.00 65.93  ? 220 PHE D C   1 
ATOM   14508 O O   . PHE D 1 220 ? 50.326  -19.745 -6.695  1.00 64.94  ? 220 PHE D O   1 
ATOM   14509 C CB  . PHE D 1 220 ? 51.688  -21.679 -4.856  1.00 65.48  ? 220 PHE D CB  1 
ATOM   14510 C CG  . PHE D 1 220 ? 50.602  -21.237 -3.882  1.00 64.73  ? 220 PHE D CG  1 
ATOM   14511 C CD1 . PHE D 1 220 ? 49.483  -22.042 -3.657  1.00 64.23  ? 220 PHE D CD1 1 
ATOM   14512 C CD2 . PHE D 1 220 ? 50.644  -19.977 -3.286  1.00 63.52  ? 220 PHE D CD2 1 
ATOM   14513 C CE1 . PHE D 1 220 ? 48.470  -21.612 -2.810  1.00 63.09  ? 220 PHE D CE1 1 
ATOM   14514 C CE2 . PHE D 1 220 ? 49.643  -19.575 -2.417  1.00 62.51  ? 220 PHE D CE2 1 
ATOM   14515 C CZ  . PHE D 1 220 ? 48.554  -20.392 -2.184  1.00 62.11  ? 220 PHE D CZ  1 
ATOM   14516 N N   . ILE D 1 221 ? 48.791  -21.431 -6.682  1.00 65.07  ? 221 ILE D N   1 
ATOM   14517 C CA  . ILE D 1 221 ? 47.682  -20.559 -7.025  1.00 65.74  ? 221 ILE D CA  1 
ATOM   14518 C C   . ILE D 1 221 ? 46.583  -20.751 -5.989  1.00 66.11  ? 221 ILE D C   1 
ATOM   14519 O O   . ILE D 1 221 ? 46.525  -21.816 -5.394  1.00 68.85  ? 221 ILE D O   1 
ATOM   14520 C CB  . ILE D 1 221 ? 47.185  -20.863 -8.448  1.00 66.77  ? 221 ILE D CB  1 
ATOM   14521 C CG1 . ILE D 1 221 ? 46.552  -22.258 -8.531  1.00 67.92  ? 221 ILE D CG1 1 
ATOM   14522 C CG2 . ILE D 1 221 ? 48.308  -20.671 -9.469  1.00 67.50  ? 221 ILE D CG2 1 
ATOM   14523 C CD1 . ILE D 1 221 ? 46.050  -22.639 -9.910  1.00 69.17  ? 221 ILE D CD1 1 
ATOM   14524 N N   . THR D 1 222 ? 45.719  -19.742 -5.781  1.00 64.94  ? 222 THR D N   1 
ATOM   14525 C CA  . THR D 1 222 ? 44.517  -19.932 -4.976  1.00 63.81  ? 222 THR D CA  1 
ATOM   14526 C C   . THR D 1 222 ? 43.374  -20.271 -5.910  1.00 62.53  ? 222 THR D C   1 
ATOM   14527 O O   . THR D 1 222 ? 43.205  -19.638 -6.951  1.00 62.58  ? 222 THR D O   1 
ATOM   14528 C CB  . THR D 1 222 ? 44.169  -18.694 -4.161  1.00 64.08  ? 222 THR D CB  1 
ATOM   14529 O OG1 . THR D 1 222 ? 43.849  -17.715 -5.150  1.00 63.99  ? 222 THR D OG1 1 
ATOM   14530 C CG2 . THR D 1 222 ? 45.336  -18.263 -3.292  1.00 64.93  ? 222 THR D CG2 1 
ATOM   14531 N N   . THR D 1 223 ? 42.583  -21.254 -5.488  1.00 62.39  ? 223 THR D N   1 
ATOM   14532 C CA  . THR D 1 223 ? 41.467  -21.739 -6.281  1.00 61.61  ? 223 THR D CA  1 
ATOM   14533 C C   . THR D 1 223 ? 40.147  -21.184 -5.757  1.00 61.43  ? 223 THR D C   1 
ATOM   14534 O O   . THR D 1 223 ? 39.184  -21.154 -6.514  1.00 63.02  ? 223 THR D O   1 
ATOM   14535 C CB  . THR D 1 223 ? 41.495  -23.259 -6.319  1.00 60.51  ? 223 THR D CB  1 
ATOM   14536 O OG1 . THR D 1 223 ? 41.988  -23.712 -5.061  1.00 59.34  ? 223 THR D OG1 1 
ATOM   14537 C CG2 . THR D 1 223 ? 42.391  -23.731 -7.442  1.00 60.94  ? 223 THR D CG2 1 
ATOM   14538 N N   . GLU D 1 224 ? 40.109  -20.741 -4.493  1.00 61.05  ? 224 GLU D N   1 
ATOM   14539 C CA  . GLU D 1 224 ? 38.983  -19.957 -4.012  1.00 61.45  ? 224 GLU D CA  1 
ATOM   14540 C C   . GLU D 1 224 ? 39.414  -18.978 -2.918  1.00 60.07  ? 224 GLU D C   1 
ATOM   14541 O O   . GLU D 1 224 ? 40.415  -19.210 -2.246  1.00 59.57  ? 224 GLU D O   1 
ATOM   14542 C CB  . GLU D 1 224 ? 37.902  -20.859 -3.416  1.00 62.79  ? 224 GLU D CB  1 
ATOM   14543 C CG  . GLU D 1 224 ? 37.184  -21.750 -4.425  1.00 63.65  ? 224 GLU D CG  1 
ATOM   14544 C CD  . GLU D 1 224 ? 36.180  -22.674 -3.779  1.00 63.75  ? 224 GLU D CD  1 
ATOM   14545 O OE1 . GLU D 1 224 ? 35.867  -22.425 -2.599  1.00 63.32  ? 224 GLU D OE1 1 
ATOM   14546 O OE2 . GLU D 1 224 ? 35.745  -23.643 -4.445  1.00 65.96  ? 224 GLU D OE2 1 
ATOM   14547 N N   . PHE D 1 225 ? 38.583  -17.940 -2.708  1.00 58.84  ? 225 PHE D N   1 
ATOM   14548 C CA  . PHE D 1 225 ? 38.625  -17.086 -1.526  1.00 57.97  ? 225 PHE D CA  1 
ATOM   14549 C C   . PHE D 1 225 ? 37.511  -16.046 -1.655  1.00 57.28  ? 225 PHE D C   1 
ATOM   14550 O O   . PHE D 1 225 ? 37.204  -15.626 -2.769  1.00 57.85  ? 225 PHE D O   1 
ATOM   14551 C CB  . PHE D 1 225 ? 39.972  -16.363 -1.346  1.00 57.54  ? 225 PHE D CB  1 
ATOM   14552 C CG  . PHE D 1 225 ? 40.389  -15.392 -2.445  1.00 57.24  ? 225 PHE D CG  1 
ATOM   14553 C CD1 . PHE D 1 225 ? 40.031  -14.057 -2.395  1.00 58.48  ? 225 PHE D CD1 1 
ATOM   14554 C CD2 . PHE D 1 225 ? 41.146  -15.813 -3.524  1.00 57.36  ? 225 PHE D CD2 1 
ATOM   14555 C CE1 . PHE D 1 225 ? 40.423  -13.185 -3.406  1.00 59.03  ? 225 PHE D CE1 1 
ATOM   14556 C CE2 . PHE D 1 225 ? 41.518  -14.952 -4.536  1.00 57.31  ? 225 PHE D CE2 1 
ATOM   14557 C CZ  . PHE D 1 225 ? 41.167  -13.642 -4.474  1.00 58.51  ? 225 PHE D CZ  1 
ATOM   14558 N N   . GLY D 1 226 ? 36.922  -15.575 -0.551  1.00 55.53  ? 226 GLY D N   1 
ATOM   14559 C CA  . GLY D 1 226 ? 35.747  -14.750 -0.751  1.00 54.99  ? 226 GLY D CA  1 
ATOM   14560 C C   . GLY D 1 226 ? 34.873  -14.706 0.483   1.00 55.12  ? 226 GLY D C   1 
ATOM   14561 O O   . GLY D 1 226 ? 35.204  -15.338 1.483   1.00 55.05  ? 226 GLY D O   1 
ATOM   14562 N N   . TYR D 1 227 ? 33.784  -13.932 0.387   1.00 55.60  ? 227 TYR D N   1 
ATOM   14563 C CA  . TYR D 1 227 ? 32.916  -13.707 1.534   1.00 56.80  ? 227 TYR D CA  1 
ATOM   14564 C C   . TYR D 1 227 ? 31.463  -13.690 1.080   1.00 56.21  ? 227 TYR D C   1 
ATOM   14565 O O   . TYR D 1 227 ? 31.183  -13.355 -0.075  1.00 54.13  ? 227 TYR D O   1 
ATOM   14566 C CB  . TYR D 1 227 ? 33.248  -12.423 2.306   1.00 58.13  ? 227 TYR D CB  1 
ATOM   14567 C CG  . TYR D 1 227 ? 34.589  -12.485 3.011   1.00 59.59  ? 227 TYR D CG  1 
ATOM   14568 C CD1 . TYR D 1 227 ? 34.700  -12.996 4.292   1.00 62.07  ? 227 TYR D CD1 1 
ATOM   14569 C CD2 . TYR D 1 227 ? 35.740  -12.050 2.387   1.00 60.20  ? 227 TYR D CD2 1 
ATOM   14570 C CE1 . TYR D 1 227 ? 35.922  -13.097 4.936   1.00 62.99  ? 227 TYR D CE1 1 
ATOM   14571 C CE2 . TYR D 1 227 ? 36.961  -12.107 3.030   1.00 62.66  ? 227 TYR D CE2 1 
ATOM   14572 C CZ  . TYR D 1 227 ? 37.059  -12.643 4.304   1.00 64.44  ? 227 TYR D CZ  1 
ATOM   14573 O OH  . TYR D 1 227 ? 38.271  -12.712 4.942   1.00 69.86  ? 227 TYR D OH  1 
ATOM   14574 N N   . SER D 1 228 ? 30.559  -13.938 2.037   1.00 57.64  ? 228 SER D N   1 
ATOM   14575 C CA  . SER D 1 228 ? 29.104  -14.035 1.739   1.00 58.95  ? 228 SER D CA  1 
ATOM   14576 C C   . SER D 1 228 ? 28.294  -12.906 2.380   1.00 59.14  ? 228 SER D C   1 
ATOM   14577 O O   . SER D 1 228 ? 28.427  -12.696 3.601   1.00 58.68  ? 228 SER D O   1 
ATOM   14578 C CB  . SER D 1 228 ? 28.560  -15.334 2.229   1.00 59.95  ? 228 SER D CB  1 
ATOM   14579 O OG  . SER D 1 228 ? 27.233  -15.541 1.773   1.00 62.20  ? 228 SER D OG  1 
ATOM   14580 N N   . VAL D 1 229 ? 27.415  -12.286 1.593   1.00 59.81  ? 229 VAL D N   1 
ATOM   14581 C CA  . VAL D 1 229 ? 26.549  -11.186 2.106   1.00 61.34  ? 229 VAL D CA  1 
ATOM   14582 C C   . VAL D 1 229 ? 25.138  -11.739 2.374   1.00 61.99  ? 229 VAL D C   1 
ATOM   14583 O O   . VAL D 1 229 ? 24.178  -11.228 1.787   1.00 63.10  ? 229 VAL D O   1 
ATOM   14584 C CB  . VAL D 1 229 ? 26.572  -10.062 1.060   1.00 61.56  ? 229 VAL D CB  1 
ATOM   14585 C CG1 . VAL D 1 229 ? 27.853  -9.254  1.158   1.00 61.34  ? 229 VAL D CG1 1 
ATOM   14586 C CG2 . VAL D 1 229 ? 26.403  -10.597 -0.355  1.00 62.81  ? 229 VAL D CG2 1 
ATOM   14587 N N   . SER D 1 230 ? 25.029  -12.730 3.252   1.00 61.17  ? 230 SER D N   1 
ATOM   14588 C CA  . SER D 1 230 ? 23.737  -13.387 3.534   1.00 61.59  ? 230 SER D CA  1 
ATOM   14589 C C   . SER D 1 230 ? 23.056  -12.624 4.668   1.00 61.74  ? 230 SER D C   1 
ATOM   14590 O O   . SER D 1 230 ? 23.764  -12.212 5.592   1.00 60.90  ? 230 SER D O   1 
ATOM   14591 C CB  . SER D 1 230 ? 23.954  -14.840 3.893   1.00 62.13  ? 230 SER D CB  1 
ATOM   14592 O OG  . SER D 1 230 ? 24.404  -14.982 5.233   1.00 61.32  ? 230 SER D OG  1 
ATOM   14593 N N   . PRO D 1 231 ? 21.731  -12.394 4.639   1.00 62.38  ? 231 PRO D N   1 
ATOM   14594 C CA  . PRO D 1 231 ? 21.111  -11.613 5.711   1.00 63.19  ? 231 PRO D CA  1 
ATOM   14595 C C   . PRO D 1 231 ? 21.515  -12.033 7.118   1.00 64.71  ? 231 PRO D C   1 
ATOM   14596 O O   . PRO D 1 231 ? 21.850  -11.199 7.955   1.00 64.05  ? 231 PRO D O   1 
ATOM   14597 C CB  . PRO D 1 231 ? 19.621  -11.802 5.444   1.00 63.48  ? 231 PRO D CB  1 
ATOM   14598 C CG  . PRO D 1 231 ? 19.567  -11.946 3.937   1.00 63.01  ? 231 PRO D CG  1 
ATOM   14599 C CD  . PRO D 1 231 ? 20.778  -12.780 3.582   1.00 62.25  ? 231 PRO D CD  1 
ATOM   14600 N N   . GLU D 1 232 ? 21.501  -13.344 7.367   1.00 67.14  ? 232 GLU D N   1 
ATOM   14601 C CA  . GLU D 1 232 ? 21.954  -13.852 8.651   1.00 68.42  ? 232 GLU D CA  1 
ATOM   14602 C C   . GLU D 1 232 ? 22.589  -15.212 8.422   1.00 66.26  ? 232 GLU D C   1 
ATOM   14603 O O   . GLU D 1 232 ? 22.824  -15.589 7.277   1.00 65.62  ? 232 GLU D O   1 
ATOM   14604 C CB  . GLU D 1 232 ? 20.789  -13.805 9.640   1.00 71.73  ? 232 GLU D CB  1 
ATOM   14605 C CG  . GLU D 1 232 ? 19.576  -14.577 9.147   1.00 74.93  ? 232 GLU D CG  1 
ATOM   14606 C CD  . GLU D 1 232 ? 18.304  -14.326 9.932   1.00 79.34  ? 232 GLU D CD  1 
ATOM   14607 O OE1 . GLU D 1 232 ? 18.348  -14.483 11.169  1.00 81.66  ? 232 GLU D OE1 1 
ATOM   14608 O OE2 . GLU D 1 232 ? 17.272  -13.990 9.303   1.00 83.93  ? 232 GLU D OE2 1 
ATOM   14609 N N   . GLY D 1 233 ? 22.928  -15.891 9.521   1.00 65.81  ? 233 GLY D N   1 
ATOM   14610 C CA  . GLY D 1 233 ? 23.384  -17.271 9.460   1.00 64.95  ? 233 GLY D CA  1 
ATOM   14611 C C   . GLY D 1 233 ? 24.885  -17.361 9.268   1.00 63.53  ? 233 GLY D C   1 
ATOM   14612 O O   . GLY D 1 233 ? 25.523  -16.384 8.926   1.00 63.50  ? 233 GLY D O   1 
ATOM   14613 N N   . GLY D 1 234 ? 25.431  -18.560 9.458   1.00 64.81  ? 234 GLY D N   1 
ATOM   14614 C CA  . GLY D 1 234 ? 26.869  -18.817 9.415   1.00 63.44  ? 234 GLY D CA  1 
ATOM   14615 C C   . GLY D 1 234 ? 27.468  -18.696 10.816  1.00 64.50  ? 234 GLY D C   1 
ATOM   14616 O O   . GLY D 1 234 ? 26.759  -18.815 11.805  1.00 64.80  ? 234 GLY D O   1 
ATOM   14617 N N   . ASN D 1 235 ? 28.777  -18.432 10.912  1.00 65.76  ? 235 ASN D N   1 
ATOM   14618 C CA  . ASN D 1 235 ? 29.363  -18.011 12.175  1.00 66.98  ? 235 ASN D CA  1 
ATOM   14619 C C   . ASN D 1 235 ? 30.460  -17.008 11.871  1.00 66.25  ? 235 ASN D C   1 
ATOM   14620 O O   . ASN D 1 235 ? 31.123  -17.143 10.846  1.00 65.30  ? 235 ASN D O   1 
ATOM   14621 C CB  . ASN D 1 235 ? 29.913  -19.166 13.003  1.00 69.30  ? 235 ASN D CB  1 
ATOM   14622 C CG  . ASN D 1 235 ? 30.447  -18.643 14.316  1.00 71.78  ? 235 ASN D CG  1 
ATOM   14623 O OD1 . ASN D 1 235 ? 29.698  -18.018 15.078  1.00 72.52  ? 235 ASN D OD1 1 
ATOM   14624 N ND2 . ASN D 1 235 ? 31.740  -18.804 14.565  1.00 73.23  ? 235 ASN D ND2 1 
ATOM   14625 N N   . GLY D 1 236 ? 30.642  -16.012 12.756  1.00 66.81  ? 236 GLY D N   1 
ATOM   14626 C CA  . GLY D 1 236 ? 31.678  -15.009 12.546  1.00 64.77  ? 236 GLY D CA  1 
ATOM   14627 C C   . GLY D 1 236 ? 31.586  -14.503 11.112  1.00 63.31  ? 236 GLY D C   1 
ATOM   14628 O O   . GLY D 1 236 ? 30.488  -14.281 10.624  1.00 66.49  ? 236 GLY D O   1 
ATOM   14629 N N   . GLN D 1 237 ? 32.706  -14.474 10.400  1.00 61.94  ? 237 GLN D N   1 
ATOM   14630 C CA  . GLN D 1 237 ? 32.761  -13.934 9.049   1.00 60.80  ? 237 GLN D CA  1 
ATOM   14631 C C   . GLN D 1 237 ? 32.342  -14.957 7.987   1.00 60.83  ? 237 GLN D C   1 
ATOM   14632 O O   . GLN D 1 237 ? 32.280  -14.673 6.783   1.00 60.20  ? 237 GLN D O   1 
ATOM   14633 C CB  . GLN D 1 237 ? 34.212  -13.526 8.813   1.00 60.84  ? 237 GLN D CB  1 
ATOM   14634 C CG  . GLN D 1 237 ? 34.686  -12.325 9.635   1.00 60.77  ? 237 GLN D CG  1 
ATOM   14635 C CD  . GLN D 1 237 ? 36.190  -12.169 9.558   1.00 60.19  ? 237 GLN D CD  1 
ATOM   14636 O OE1 . GLN D 1 237 ? 36.752  -11.933 8.479   1.00 58.47  ? 237 GLN D OE1 1 
ATOM   14637 N NE2 . GLN D 1 237 ? 36.855  -12.377 10.689  1.00 60.98  ? 237 GLN D NE2 1 
ATOM   14638 N N   . TYR D 1 238 ? 32.111  -16.198 8.406   1.00 61.00  ? 238 TYR D N   1 
ATOM   14639 C CA  . TYR D 1 238 ? 31.428  -17.112 7.524   1.00 60.88  ? 238 TYR D CA  1 
ATOM   14640 C C   . TYR D 1 238 ? 29.971  -16.659 7.544   1.00 62.74  ? 238 TYR D C   1 
ATOM   14641 O O   . TYR D 1 238 ? 29.315  -16.741 8.582   1.00 64.21  ? 238 TYR D O   1 
ATOM   14642 C CB  . TYR D 1 238 ? 31.669  -18.568 7.949   1.00 60.78  ? 238 TYR D CB  1 
ATOM   14643 C CG  . TYR D 1 238 ? 30.945  -19.549 7.044   1.00 59.17  ? 238 TYR D CG  1 
ATOM   14644 C CD1 . TYR D 1 238 ? 31.261  -19.646 5.700   1.00 57.99  ? 238 TYR D CD1 1 
ATOM   14645 C CD2 . TYR D 1 238 ? 29.890  -20.292 7.519   1.00 60.22  ? 238 TYR D CD2 1 
ATOM   14646 C CE1 . TYR D 1 238 ? 30.556  -20.482 4.858   1.00 58.69  ? 238 TYR D CE1 1 
ATOM   14647 C CE2 . TYR D 1 238 ? 29.171  -21.136 6.690   1.00 60.63  ? 238 TYR D CE2 1 
ATOM   14648 C CZ  . TYR D 1 238 ? 29.518  -21.247 5.356   1.00 60.03  ? 238 TYR D CZ  1 
ATOM   14649 O OH  . TYR D 1 238 ? 28.810  -22.102 4.555   1.00 61.35  ? 238 TYR D OH  1 
ATOM   14650 N N   . GLY D 1 239 ? 29.519  -16.078 6.423   1.00 63.52  ? 239 GLY D N   1 
ATOM   14651 C CA  . GLY D 1 239 ? 28.161  -15.557 6.279   1.00 63.98  ? 239 GLY D CA  1 
ATOM   14652 C C   . GLY D 1 239 ? 27.945  -14.217 6.992   1.00 62.38  ? 239 GLY D C   1 
ATOM   14653 O O   . GLY D 1 239 ? 28.775  -13.790 7.782   1.00 61.07  ? 239 GLY D O   1 
ATOM   14654 N N   . SER D 1 240 ? 26.794  -13.592 6.718   1.00 62.15  ? 240 SER D N   1 
ATOM   14655 C CA  . SER D 1 240 ? 26.349  -12.383 7.406   1.00 62.88  ? 240 SER D CA  1 
ATOM   14656 C C   . SER D 1 240 ? 27.349  -11.231 7.321   1.00 63.36  ? 240 SER D C   1 
ATOM   14657 O O   . SER D 1 240 ? 27.460  -10.498 8.286   1.00 64.37  ? 240 SER D O   1 
ATOM   14658 C CB  . SER D 1 240 ? 26.046  -12.657 8.850   1.00 62.86  ? 240 SER D CB  1 
ATOM   14659 O OG  . SER D 1 240 ? 25.198  -13.783 8.967   1.00 63.19  ? 240 SER D OG  1 
ATOM   14660 N N   . ASN D 1 241 ? 28.082  -11.089 6.210   1.00 64.46  ? 241 ASN D N   1 
ATOM   14661 C CA  . ASN D 1 241 ? 28.921  -9.926  5.986   1.00 65.87  ? 241 ASN D CA  1 
ATOM   14662 C C   . ASN D 1 241 ? 28.107  -8.867  5.247   1.00 65.89  ? 241 ASN D C   1 
ATOM   14663 O O   . ASN D 1 241 ? 27.234  -9.217  4.456   1.00 67.82  ? 241 ASN D O   1 
ATOM   14664 C CB  . ASN D 1 241 ? 30.173  -10.266 5.185   1.00 67.61  ? 241 ASN D CB  1 
ATOM   14665 C CG  . ASN D 1 241 ? 31.240  -10.969 5.994   1.00 68.41  ? 241 ASN D CG  1 
ATOM   14666 O OD1 . ASN D 1 241 ? 32.052  -10.340 6.682   1.00 70.28  ? 241 ASN D OD1 1 
ATOM   14667 N ND2 . ASN D 1 241 ? 31.318  -12.274 5.858   1.00 69.26  ? 241 ASN D ND2 1 
ATOM   14668 N N   . THR D 1 242 ? 28.380  -7.583  5.521   1.00 64.17  ? 242 THR D N   1 
ATOM   14669 C CA  . THR D 1 242 ? 27.791  -6.484  4.759   1.00 63.43  ? 242 THR D CA  1 
ATOM   14670 C C   . THR D 1 242 ? 28.488  -6.434  3.404   1.00 63.46  ? 242 THR D C   1 
ATOM   14671 O O   . THR D 1 242 ? 29.465  -7.162  3.201   1.00 67.00  ? 242 THR D O   1 
ATOM   14672 C CB  . THR D 1 242 ? 27.927  -5.147  5.487   1.00 61.79  ? 242 THR D CB  1 
ATOM   14673 O OG1 . THR D 1 242 ? 29.312  -4.888  5.612   1.00 60.05  ? 242 THR D OG1 1 
ATOM   14674 C CG2 . THR D 1 242 ? 27.382  -5.188  6.898   1.00 62.62  ? 242 THR D CG2 1 
ATOM   14675 N N   . LEU D 1 243 ? 27.991  -5.582  2.496   1.00 61.75  ? 243 LEU D N   1 
ATOM   14676 C CA  . LEU D 1 243 ? 28.471  -5.560  1.121   1.00 60.29  ? 243 LEU D CA  1 
ATOM   14677 C C   . LEU D 1 243 ? 29.896  -5.033  1.081   1.00 60.14  ? 243 LEU D C   1 
ATOM   14678 O O   . LEU D 1 243 ? 30.652  -5.418  0.182   1.00 60.02  ? 243 LEU D O   1 
ATOM   14679 C CB  . LEU D 1 243 ? 27.565  -4.704  0.243   1.00 59.99  ? 243 LEU D CB  1 
ATOM   14680 C CG  . LEU D 1 243 ? 26.197  -5.307  -0.090  1.00 59.36  ? 243 LEU D CG  1 
ATOM   14681 C CD1 . LEU D 1 243 ? 25.208  -4.271  -0.643  1.00 59.66  ? 243 LEU D CD1 1 
ATOM   14682 C CD2 . LEU D 1 243 ? 26.498  -6.390  -1.090  1.00 58.55  ? 243 LEU D CD2 1 
ATOM   14683 N N   . LYS D 1 244 ? 30.166  -4.158  2.072   1.00 60.42  ? 244 LYS D N   1 
ATOM   14684 C CA  . LYS D 1 244 ? 31.389  -3.398  2.307   1.00 59.56  ? 244 LYS D CA  1 
ATOM   14685 C C   . LYS D 1 244 ? 32.440  -4.304  2.947   1.00 59.76  ? 244 LYS D C   1 
ATOM   14686 O O   . LYS D 1 244 ? 33.640  -4.224  2.625   1.00 59.18  ? 244 LYS D O   1 
ATOM   14687 C CB  . LYS D 1 244 ? 31.157  -2.240  3.298   1.00 59.30  ? 244 LYS D CB  1 
ATOM   14688 C CG  . LYS D 1 244 ? 32.466  -1.618  3.763   1.00 60.10  ? 244 LYS D CG  1 
ATOM   14689 C CD  . LYS D 1 244 ? 32.469  -0.246  4.431   1.00 61.36  ? 244 LYS D CD  1 
ATOM   14690 C CE  . LYS D 1 244 ? 33.827  0.317   4.753   1.00 61.67  ? 244 LYS D CE  1 
ATOM   14691 N NZ  . LYS D 1 244 ? 34.711  0.326   3.583   1.00 61.78  ? 244 LYS D NZ  1 
ATOM   14692 N N   . GLN D 1 245 ? 31.986  -5.130  3.906   1.00 59.39  ? 245 GLN D N   1 
ATOM   14693 C CA  . GLN D 1 245 ? 32.856  -6.144  4.491   1.00 58.67  ? 245 GLN D CA  1 
ATOM   14694 C C   . GLN D 1 245 ? 33.318  -7.100  3.398   1.00 57.71  ? 245 GLN D C   1 
ATOM   14695 O O   . GLN D 1 245 ? 34.518  -7.377  3.273   1.00 56.08  ? 245 GLN D O   1 
ATOM   14696 C CB  . GLN D 1 245 ? 32.160  -6.929  5.598   1.00 58.23  ? 245 GLN D CB  1 
ATOM   14697 C CG  . GLN D 1 245 ? 31.996  -6.137  6.889   1.00 57.94  ? 245 GLN D CG  1 
ATOM   14698 C CD  . GLN D 1 245 ? 31.111  -6.862  7.877   1.00 59.07  ? 245 GLN D CD  1 
ATOM   14699 O OE1 . GLN D 1 245 ? 30.232  -7.669  7.514   1.00 59.18  ? 245 GLN D OE1 1 
ATOM   14700 N NE2 . GLN D 1 245 ? 31.355  -6.590  9.150   1.00 59.33  ? 245 GLN D NE2 1 
ATOM   14701 N N   . GLN D 1 246 ? 32.337  -7.560  2.609   1.00 58.36  ? 246 GLN D N   1 
ATOM   14702 C CA  . GLN D 1 246 ? 32.629  -8.408  1.467   1.00 59.40  ? 246 GLN D CA  1 
ATOM   14703 C C   . GLN D 1 246 ? 33.671  -7.723  0.570   1.00 59.28  ? 246 GLN D C   1 
ATOM   14704 O O   . GLN D 1 246 ? 34.616  -8.353  0.115   1.00 59.59  ? 246 GLN D O   1 
ATOM   14705 C CB  . GLN D 1 246 ? 31.349  -8.801  0.726   1.00 59.40  ? 246 GLN D CB  1 
ATOM   14706 C CG  . GLN D 1 246 ? 31.606  -9.776  -0.420  1.00 59.54  ? 246 GLN D CG  1 
ATOM   14707 C CD  . GLN D 1 246 ? 30.556  -9.721  -1.508  1.00 59.99  ? 246 GLN D CD  1 
ATOM   14708 O OE1 . GLN D 1 246 ? 30.215  -8.640  -1.980  1.00 65.12  ? 246 GLN D OE1 1 
ATOM   14709 N NE2 . GLN D 1 246 ? 30.040  -10.851 -1.951  1.00 59.62  ? 246 GLN D NE2 1 
ATOM   14710 N N   . SER D 1 247 ? 33.538  -6.425  0.313   1.00 58.99  ? 247 SER D N   1 
ATOM   14711 C CA  . SER D 1 247 ? 34.433  -5.809  -0.651  1.00 59.92  ? 247 SER D CA  1 
ATOM   14712 C C   . SER D 1 247 ? 35.871  -5.687  -0.109  1.00 60.35  ? 247 SER D C   1 
ATOM   14713 O O   . SER D 1 247 ? 36.841  -6.077  -0.770  1.00 59.43  ? 247 SER D O   1 
ATOM   14714 C CB  . SER D 1 247 ? 33.906  -4.509  -1.094  1.00 60.81  ? 247 SER D CB  1 
ATOM   14715 O OG  . SER D 1 247 ? 34.519  -4.183  -2.328  1.00 63.14  ? 247 SER D OG  1 
ATOM   14716 N N   . ASP D 1 248 ? 36.012  -5.178  1.119   1.00 59.28  ? 248 ASP D N   1 
ATOM   14717 C CA  . ASP D 1 248 ? 37.315  -5.050  1.743   1.00 58.25  ? 248 ASP D CA  1 
ATOM   14718 C C   . ASP D 1 248 ? 37.954  -6.438  1.905   1.00 58.46  ? 248 ASP D C   1 
ATOM   14719 O O   . ASP D 1 248 ? 39.130  -6.616  1.594   1.00 59.92  ? 248 ASP D O   1 
ATOM   14720 C CB  . ASP D 1 248 ? 37.204  -4.180  2.984   1.00 57.83  ? 248 ASP D CB  1 
ATOM   14721 C CG  . ASP D 1 248 ? 36.494  -2.843  2.765   1.00 57.66  ? 248 ASP D CG  1 
ATOM   14722 O OD1 . ASP D 1 248 ? 36.376  -2.431  1.583   1.00 56.38  ? 248 ASP D OD1 1 
ATOM   14723 O OD2 . ASP D 1 248 ? 36.008  -2.245  3.764   1.00 57.01  ? 248 ASP D OD2 1 
ATOM   14724 N N   . GLY D 1 249 ? 37.194  -7.441  2.357   1.00 58.55  ? 249 GLY D N   1 
ATOM   14725 C CA  . GLY D 1 249 ? 37.729  -8.781  2.560   1.00 58.25  ? 249 GLY D CA  1 
ATOM   14726 C C   . GLY D 1 249 ? 38.384  -9.343  1.292   1.00 57.49  ? 249 GLY D C   1 
ATOM   14727 O O   . GLY D 1 249 ? 39.449  -9.994  1.353   1.00 55.30  ? 249 GLY D O   1 
ATOM   14728 N N   . LEU D 1 250 ? 37.724  -9.080  0.146   1.00 56.51  ? 250 LEU D N   1 
ATOM   14729 C CA  . LEU D 1 250 ? 38.216  -9.565  -1.139  1.00 55.99  ? 250 LEU D CA  1 
ATOM   14730 C C   . LEU D 1 250 ? 39.547  -8.910  -1.486  1.00 54.62  ? 250 LEU D C   1 
ATOM   14731 O O   . LEU D 1 250 ? 40.488  -9.584  -1.845  1.00 53.57  ? 250 LEU D O   1 
ATOM   14732 C CB  . LEU D 1 250 ? 37.202  -9.388  -2.268  1.00 56.39  ? 250 LEU D CB  1 
ATOM   14733 C CG  . LEU D 1 250 ? 36.380  -10.635 -2.635  1.00 56.32  ? 250 LEU D CG  1 
ATOM   14734 C CD1 . LEU D 1 250 ? 37.262  -11.775 -3.127  1.00 55.95  ? 250 LEU D CD1 1 
ATOM   14735 C CD2 . LEU D 1 250 ? 35.505  -11.094 -1.489  1.00 56.33  ? 250 LEU D CD2 1 
ATOM   14736 N N   . ILE D 1 251 ? 39.612  -7.580  -1.363  1.00 55.14  ? 251 ILE D N   1 
ATOM   14737 C CA  . ILE D 1 251 ? 40.843  -6.826  -1.584  1.00 54.05  ? 251 ILE D CA  1 
ATOM   14738 C C   . ILE D 1 251 ? 41.920  -7.323  -0.627  1.00 54.03  ? 251 ILE D C   1 
ATOM   14739 O O   . ILE D 1 251 ? 43.046  -7.545  -1.034  1.00 53.86  ? 251 ILE D O   1 
ATOM   14740 C CB  . ILE D 1 251 ? 40.575  -5.325  -1.437  1.00 53.36  ? 251 ILE D CB  1 
ATOM   14741 C CG1 . ILE D 1 251 ? 39.530  -4.859  -2.437  1.00 53.15  ? 251 ILE D CG1 1 
ATOM   14742 C CG2 . ILE D 1 251 ? 41.870  -4.525  -1.553  1.00 54.22  ? 251 ILE D CG2 1 
ATOM   14743 C CD1 . ILE D 1 251 ? 39.632  -5.455  -3.829  1.00 53.03  ? 251 ILE D CD1 1 
ATOM   14744 N N   . SER D 1 252 ? 41.528  -7.515  0.631   1.00 54.22  ? 252 SER D N   1 
ATOM   14745 C CA  . SER D 1 252 ? 42.395  -7.965  1.701   1.00 54.79  ? 252 SER D CA  1 
ATOM   14746 C C   . SER D 1 252 ? 42.910  -9.390  1.458   1.00 56.03  ? 252 SER D C   1 
ATOM   14747 O O   . SER D 1 252 ? 44.100  -9.656  1.533   1.00 57.22  ? 252 SER D O   1 
ATOM   14748 C CB  . SER D 1 252 ? 41.619  -7.820  2.971   1.00 54.49  ? 252 SER D CB  1 
ATOM   14749 O OG  . SER D 1 252 ? 42.435  -7.920  4.119   1.00 54.86  ? 252 SER D OG  1 
ATOM   14750 N N   . ASN D 1 253 ? 42.035  -10.336 1.137   1.00 57.63  ? 253 ASN D N   1 
ATOM   14751 C CA  . ASN D 1 253 ? 42.489  -11.684 0.810   1.00 58.63  ? 253 ASN D CA  1 
ATOM   14752 C C   . ASN D 1 253 ? 43.459  -11.594 -0.366  1.00 59.18  ? 253 ASN D C   1 
ATOM   14753 O O   . ASN D 1 253 ? 44.512  -12.214 -0.312  1.00 61.92  ? 253 ASN D O   1 
ATOM   14754 C CB  . ASN D 1 253 ? 41.367  -12.654 0.415   1.00 59.19  ? 253 ASN D CB  1 
ATOM   14755 C CG  . ASN D 1 253 ? 40.340  -12.979 1.485   1.00 59.30  ? 253 ASN D CG  1 
ATOM   14756 O OD1 . ASN D 1 253 ? 39.296  -13.574 1.177   1.00 59.09  ? 253 ASN D OD1 1 
ATOM   14757 N ND2 . ASN D 1 253 ? 40.610  -12.663 2.744   1.00 60.04  ? 253 ASN D ND2 1 
ATOM   14758 N N   . TYR D 1 254 ? 43.138  -10.786 -1.390  1.00 58.70  ? 254 TYR D N   1 
ATOM   14759 C CA  . TYR D 1 254 ? 43.912  -10.733 -2.625  1.00 59.36  ? 254 TYR D CA  1 
ATOM   14760 C C   . TYR D 1 254 ? 45.359  -10.332 -2.322  1.00 60.08  ? 254 TYR D C   1 
ATOM   14761 O O   . TYR D 1 254 ? 46.304  -10.914 -2.869  1.00 61.56  ? 254 TYR D O   1 
ATOM   14762 C CB  . TYR D 1 254 ? 43.382  -9.752  -3.679  1.00 59.81  ? 254 TYR D CB  1 
ATOM   14763 C CG  . TYR D 1 254 ? 43.504  -10.216 -5.126  1.00 60.26  ? 254 TYR D CG  1 
ATOM   14764 C CD1 . TYR D 1 254 ? 44.739  -10.412 -5.722  1.00 61.98  ? 254 TYR D CD1 1 
ATOM   14765 C CD2 . TYR D 1 254 ? 42.387  -10.435 -5.913  1.00 60.11  ? 254 TYR D CD2 1 
ATOM   14766 C CE1 . TYR D 1 254 ? 44.853  -10.863 -7.031  1.00 61.97  ? 254 TYR D CE1 1 
ATOM   14767 C CE2 . TYR D 1 254 ? 42.486  -10.875 -7.226  1.00 60.72  ? 254 TYR D CE2 1 
ATOM   14768 C CZ  . TYR D 1 254 ? 43.725  -11.091 -7.789  1.00 60.87  ? 254 TYR D CZ  1 
ATOM   14769 O OH  . TYR D 1 254 ? 43.859  -11.486 -9.084  1.00 61.30  ? 254 TYR D OH  1 
ATOM   14770 N N   . ARG D 1 255 ? 45.542  -9.346  -1.438  1.00 59.27  ? 255 ARG D N   1 
ATOM   14771 C CA  . ARG D 1 255 ? 46.880  -8.898  -1.099  1.00 59.77  ? 255 ARG D CA  1 
ATOM   14772 C C   . ARG D 1 255 ? 47.567  -9.989  -0.284  1.00 61.90  ? 255 ARG D C   1 
ATOM   14773 O O   . ARG D 1 255 ? 48.698  -10.381 -0.608  1.00 62.85  ? 255 ARG D O   1 
ATOM   14774 C CB  . ARG D 1 255 ? 46.871  -7.553  -0.368  1.00 58.85  ? 255 ARG D CB  1 
ATOM   14775 C CG  . ARG D 1 255 ? 48.085  -7.159  0.459   1.00 59.00  ? 255 ARG D CG  1 
ATOM   14776 C CD  . ARG D 1 255 ? 49.232  -6.521  -0.293  1.00 59.65  ? 255 ARG D CD  1 
ATOM   14777 N NE  . ARG D 1 255 ? 50.084  -7.374  -1.131  1.00 60.31  ? 255 ARG D NE  1 
ATOM   14778 C CZ  . ARG D 1 255 ? 50.288  -7.182  -2.447  1.00 61.44  ? 255 ARG D CZ  1 
ATOM   14779 N NH1 . ARG D 1 255 ? 49.570  -6.272  -3.120  1.00 61.29  ? 255 ARG D NH1 1 
ATOM   14780 N NH2 . ARG D 1 255 ? 51.178  -7.932  -3.097  1.00 61.91  ? 255 ARG D NH2 1 
ATOM   14781 N N   . ASP D 1 256 ? 46.870  -10.467 0.760   1.00 62.06  ? 256 ASP D N   1 
ATOM   14782 C CA  . ASP D 1 256 ? 47.428  -11.455 1.680   1.00 62.78  ? 256 ASP D CA  1 
ATOM   14783 C C   . ASP D 1 256 ? 47.977  -12.698 0.977   1.00 61.69  ? 256 ASP D C   1 
ATOM   14784 O O   . ASP D 1 256 ? 49.000  -13.222 1.392   1.00 61.93  ? 256 ASP D O   1 
ATOM   14785 C CB  . ASP D 1 256 ? 46.406  -11.869 2.721   1.00 63.28  ? 256 ASP D CB  1 
ATOM   14786 C CG  . ASP D 1 256 ? 46.290  -10.909 3.887   1.00 64.21  ? 256 ASP D CG  1 
ATOM   14787 O OD1 . ASP D 1 256 ? 46.140  -9.711  3.618   1.00 64.38  ? 256 ASP D OD1 1 
ATOM   14788 O OD2 . ASP D 1 256 ? 46.412  -11.373 5.037   1.00 66.33  ? 256 ASP D OD2 1 
ATOM   14789 N N   . LEU D 1 257 ? 47.284  -13.176 -0.061  1.00 60.21  ? 257 LEU D N   1 
ATOM   14790 C CA  . LEU D 1 257 ? 47.639  -14.420 -0.719  1.00 59.50  ? 257 LEU D CA  1 
ATOM   14791 C C   . LEU D 1 257 ? 48.808  -14.198 -1.674  1.00 59.61  ? 257 LEU D C   1 
ATOM   14792 O O   . LEU D 1 257 ? 49.642  -15.091 -1.836  1.00 60.48  ? 257 LEU D O   1 
ATOM   14793 C CB  . LEU D 1 257 ? 46.394  -14.945 -1.427  1.00 59.25  ? 257 LEU D CB  1 
ATOM   14794 C CG  . LEU D 1 257 ? 45.223  -15.246 -0.483  1.00 58.95  ? 257 LEU D CG  1 
ATOM   14795 C CD1 . LEU D 1 257 ? 43.865  -15.432 -1.122  1.00 57.70  ? 257 LEU D CD1 1 
ATOM   14796 C CD2 . LEU D 1 257 ? 45.623  -16.478 0.285   1.00 60.30  ? 257 LEU D CD2 1 
ATOM   14797 N N   . ILE D 1 258 ? 48.889  -13.019 -2.302  1.00 58.68  ? 258 ILE D N   1 
ATOM   14798 C CA  . ILE D 1 258 ? 50.035  -12.744 -3.147  1.00 59.12  ? 258 ILE D CA  1 
ATOM   14799 C C   . ILE D 1 258 ? 51.277  -12.736 -2.262  1.00 60.65  ? 258 ILE D C   1 
ATOM   14800 O O   . ILE D 1 258 ? 52.312  -13.319 -2.638  1.00 61.16  ? 258 ILE D O   1 
ATOM   14801 C CB  . ILE D 1 258 ? 49.870  -11.441 -3.932  1.00 58.48  ? 258 ILE D CB  1 
ATOM   14802 C CG1 . ILE D 1 258 ? 48.785  -11.573 -4.994  1.00 58.31  ? 258 ILE D CG1 1 
ATOM   14803 C CG2 . ILE D 1 258 ? 51.201  -10.990 -4.540  1.00 58.85  ? 258 ILE D CG2 1 
ATOM   14804 C CD1 . ILE D 1 258 ? 48.292  -10.228 -5.526  1.00 58.58  ? 258 ILE D CD1 1 
ATOM   14805 N N   . ASP D 1 259 ? 51.108  -12.128 -1.073  1.00 60.98  ? 259 ASP D N   1 
ATOM   14806 C CA  . ASP D 1 259 ? 52.145  -12.003 -0.059  1.00 62.41  ? 259 ASP D CA  1 
ATOM   14807 C C   . ASP D 1 259 ? 52.550  -13.374 0.469   1.00 64.30  ? 259 ASP D C   1 
ATOM   14808 O O   . ASP D 1 259 ? 53.660  -13.540 0.997   1.00 66.15  ? 259 ASP D O   1 
ATOM   14809 C CB  . ASP D 1 259 ? 51.707  -11.141 1.116   1.00 62.11  ? 259 ASP D CB  1 
ATOM   14810 C CG  . ASP D 1 259 ? 51.469  -9.677  0.779   1.00 62.14  ? 259 ASP D CG  1 
ATOM   14811 O OD1 . ASP D 1 259 ? 52.251  -9.160  -0.056  1.00 62.36  ? 259 ASP D OD1 1 
ATOM   14812 O OD2 . ASP D 1 259 ? 50.513  -9.076  1.349   1.00 60.86  ? 259 ASP D OD2 1 
ATOM   14813 N N   . ALA D 1 260 ? 51.633  -14.346 0.322   1.00 64.15  ? 260 ALA D N   1 
ATOM   14814 C CA  . ALA D 1 260 ? 51.900  -15.734 0.666   1.00 64.10  ? 260 ALA D CA  1 
ATOM   14815 C C   . ALA D 1 260 ? 52.629  -16.481 -0.446  1.00 64.17  ? 260 ALA D C   1 
ATOM   14816 O O   . ALA D 1 260 ? 53.035  -17.613 -0.214  1.00 65.36  ? 260 ALA D O   1 
ATOM   14817 C CB  . ALA D 1 260 ? 50.604  -16.436 0.983   1.00 63.62  ? 260 ALA D CB  1 
ATOM   14818 N N   . GLY D 1 261 ? 52.705  -15.906 -1.657  1.00 63.62  ? 261 GLY D N   1 
ATOM   14819 C CA  . GLY D 1 261 ? 53.420  -16.537 -2.762  1.00 63.75  ? 261 GLY D CA  1 
ATOM   14820 C C   . GLY D 1 261 ? 52.566  -16.790 -4.012  1.00 62.79  ? 261 GLY D C   1 
ATOM   14821 O O   . GLY D 1 261 ? 53.078  -17.223 -5.032  1.00 63.03  ? 261 GLY D O   1 
ATOM   14822 N N   . ALA D 1 262 ? 51.281  -16.467 -3.996  1.00 61.49  ? 262 ALA D N   1 
ATOM   14823 C CA  . ALA D 1 262 ? 50.441  -16.819 -5.126  1.00 61.74  ? 262 ALA D CA  1 
ATOM   14824 C C   . ALA D 1 262 ? 50.918  -16.159 -6.419  1.00 61.55  ? 262 ALA D C   1 
ATOM   14825 O O   . ALA D 1 262 ? 51.190  -14.965 -6.442  1.00 61.08  ? 262 ALA D O   1 
ATOM   14826 C CB  . ALA D 1 262 ? 49.003  -16.404 -4.807  1.00 61.88  ? 262 ALA D CB  1 
ATOM   14827 N N   . VAL D 1 263 ? 50.901  -16.917 -7.516  1.00 62.39  ? 263 VAL D N   1 
ATOM   14828 C CA  . VAL D 1 263 ? 51.114  -16.354 -8.841  1.00 64.16  ? 263 VAL D CA  1 
ATOM   14829 C C   . VAL D 1 263 ? 49.888  -16.608 -9.701  1.00 63.99  ? 263 VAL D C   1 
ATOM   14830 O O   . VAL D 1 263 ? 49.992  -16.563 -10.919 1.00 65.13  ? 263 VAL D O   1 
ATOM   14831 C CB  . VAL D 1 263 ? 52.335  -16.936 -9.579  1.00 66.00  ? 263 VAL D CB  1 
ATOM   14832 C CG1 . VAL D 1 263 ? 53.564  -16.930 -8.681  1.00 67.20  ? 263 VAL D CG1 1 
ATOM   14833 C CG2 . VAL D 1 263 ? 52.077  -18.349 -10.120 1.00 66.04  ? 263 VAL D CG2 1 
ATOM   14834 N N   . GLY D 1 264 ? 48.761  -16.945 -9.080  1.00 64.26  ? 264 GLY D N   1 
ATOM   14835 C CA  . GLY D 1 264 ? 47.501  -17.104 -9.798  1.00 64.93  ? 264 GLY D CA  1 
ATOM   14836 C C   . GLY D 1 264 ? 46.318  -17.026 -8.835  1.00 64.34  ? 264 GLY D C   1 
ATOM   14837 O O   . GLY D 1 264 ? 46.346  -17.651 -7.774  1.00 63.85  ? 264 GLY D O   1 
ATOM   14838 N N   . MET D 1 265 ? 45.276  -16.270 -9.198  1.00 64.95  ? 265 MET D N   1 
ATOM   14839 C CA  . MET D 1 265 ? 44.207  -16.021 -8.240  1.00 64.54  ? 265 MET D CA  1 
ATOM   14840 C C   . MET D 1 265 ? 42.822  -16.393 -8.794  1.00 63.29  ? 265 MET D C   1 
ATOM   14841 O O   . MET D 1 265 ? 42.409  -16.058 -9.907  1.00 62.63  ? 265 MET D O   1 
ATOM   14842 C CB  . MET D 1 265 ? 44.318  -14.575 -7.755  1.00 65.46  ? 265 MET D CB  1 
ATOM   14843 C CG  . MET D 1 265 ? 45.664  -14.247 -7.117  1.00 66.82  ? 265 MET D CG  1 
ATOM   14844 S SD  . MET D 1 265 ? 45.754  -14.913 -5.441  1.00 69.65  ? 265 MET D SD  1 
ATOM   14845 C CE  . MET D 1 265 ? 44.818  -13.705 -4.508  1.00 66.87  ? 265 MET D CE  1 
ATOM   14846 N N   . CYS D 1 266 ? 42.077  -17.115 -7.970  1.00 62.36  ? 266 CYS D N   1 
ATOM   14847 C CA  . CYS D 1 266 ? 40.729  -17.504 -8.323  1.00 62.58  ? 266 CYS D CA  1 
ATOM   14848 C C   . CYS D 1 266 ? 39.758  -16.976 -7.259  1.00 62.46  ? 266 CYS D C   1 
ATOM   14849 O O   . CYS D 1 266 ? 39.184  -17.745 -6.483  1.00 65.91  ? 266 CYS D O   1 
ATOM   14850 C CB  . CYS D 1 266 ? 40.654  -19.023 -8.485  1.00 62.08  ? 266 CYS D CB  1 
ATOM   14851 S SG  . CYS D 1 266 ? 41.466  -19.644 -9.981  1.00 61.98  ? 266 CYS D SG  1 
ATOM   14852 N N   . PRO D 1 267 ? 39.489  -15.637 -7.195  1.00 60.40  ? 267 PRO D N   1 
ATOM   14853 C CA  . PRO D 1 267 ? 38.515  -15.084 -6.263  1.00 59.49  ? 267 PRO D CA  1 
ATOM   14854 C C   . PRO D 1 267 ? 37.217  -15.857 -6.299  1.00 59.78  ? 267 PRO D C   1 
ATOM   14855 O O   . PRO D 1 267 ? 36.781  -16.288 -7.383  1.00 58.42  ? 267 PRO D O   1 
ATOM   14856 C CB  . PRO D 1 267 ? 38.357  -13.637 -6.720  1.00 59.42  ? 267 PRO D CB  1 
ATOM   14857 C CG  . PRO D 1 267 ? 38.923  -13.613 -8.101  1.00 60.34  ? 267 PRO D CG  1 
ATOM   14858 C CD  . PRO D 1 267 ? 40.108  -14.525 -7.933  1.00 60.73  ? 267 PRO D CD  1 
ATOM   14859 N N   . PHE D 1 268 ? 36.539  -15.970 -5.161  1.00 60.58  ? 268 PHE D N   1 
ATOM   14860 C CA  . PHE D 1 268 ? 35.358  -16.881 -5.148  1.00 63.48  ? 268 PHE D CA  1 
ATOM   14861 C C   . PHE D 1 268 ? 34.025  -16.310 -5.629  1.00 62.18  ? 268 PHE D C   1 
ATOM   14862 O O   . PHE D 1 268 ? 33.473  -15.430 -4.943  1.00 58.16  ? 268 PHE D O   1 
ATOM   14863 C CB  . PHE D 1 268 ? 35.008  -17.547 -3.811  1.00 66.86  ? 268 PHE D CB  1 
ATOM   14864 C CG  . PHE D 1 268 ? 33.904  -18.584 -3.955  1.00 65.77  ? 268 PHE D CG  1 
ATOM   14865 C CD1 . PHE D 1 268 ? 33.950  -19.535 -4.966  1.00 66.30  ? 268 PHE D CD1 1 
ATOM   14866 C CD2 . PHE D 1 268 ? 32.808  -18.586 -3.104  1.00 66.60  ? 268 PHE D CD2 1 
ATOM   14867 C CE1 . PHE D 1 268 ? 32.933  -20.460 -5.112  1.00 71.10  ? 268 PHE D CE1 1 
ATOM   14868 C CE2 . PHE D 1 268 ? 31.797  -19.518 -3.256  1.00 67.45  ? 268 PHE D CE2 1 
ATOM   14869 C CZ  . PHE D 1 268 ? 31.861  -20.448 -4.261  1.00 69.42  ? 268 PHE D CZ  1 
ATOM   14870 N N   . TYR D 1 269 ? 33.541  -16.810 -6.769  1.00 64.57  ? 269 TYR D N   1 
ATOM   14871 C CA  . TYR D 1 269 ? 32.154  -16.567 -7.257  1.00 66.25  ? 269 TYR D CA  1 
ATOM   14872 C C   . TYR D 1 269 ? 31.872  -15.238 -7.934  1.00 64.27  ? 269 TYR D C   1 
ATOM   14873 O O   . TYR D 1 269 ? 32.115  -14.177 -7.364  1.00 62.63  ? 269 TYR D O   1 
ATOM   14874 C CB  . TYR D 1 269 ? 31.132  -16.901 -6.159  1.00 69.82  ? 269 TYR D CB  1 
ATOM   14875 C CG  . TYR D 1 269 ? 30.093  -17.940 -6.555  1.00 71.02  ? 269 TYR D CG  1 
ATOM   14876 C CD1 . TYR D 1 269 ? 30.131  -18.555 -7.800  1.00 70.95  ? 269 TYR D CD1 1 
ATOM   14877 C CD2 . TYR D 1 269 ? 29.071  -18.296 -5.686  1.00 73.94  ? 269 TYR D CD2 1 
ATOM   14878 C CE1 . TYR D 1 269 ? 29.182  -19.494 -8.167  1.00 74.20  ? 269 TYR D CE1 1 
ATOM   14879 C CE2 . TYR D 1 269 ? 28.120  -19.237 -6.040  1.00 73.31  ? 269 TYR D CE2 1 
ATOM   14880 C CZ  . TYR D 1 269 ? 28.172  -19.834 -7.284  1.00 73.78  ? 269 TYR D CZ  1 
ATOM   14881 O OH  . TYR D 1 269 ? 27.227  -20.756 -7.624  1.00 70.68  ? 269 TYR D OH  1 
ATOM   14882 N N   . TYR D 1 270 ? 31.292  -15.343 -9.126  1.00 64.14  ? 270 TYR D N   1 
ATOM   14883 C CA  . TYR D 1 270 ? 30.824  -14.163 -9.869  1.00 64.67  ? 270 TYR D CA  1 
ATOM   14884 C C   . TYR D 1 270 ? 29.380  -13.953 -9.514  1.00 64.45  ? 270 TYR D C   1 
ATOM   14885 O O   . TYR D 1 270 ? 29.017  -12.798 -9.259  1.00 63.99  ? 270 TYR D O   1 
ATOM   14886 C CB  . TYR D 1 270 ? 30.936  -14.623 -11.317 1.00 65.67  ? 270 TYR D CB  1 
ATOM   14887 C CG  . TYR D 1 270 ? 29.968  -14.056 -12.347 1.00 65.91  ? 270 TYR D CG  1 
ATOM   14888 C CD1 . TYR D 1 270 ? 30.081  -12.752 -12.807 1.00 66.24  ? 270 TYR D CD1 1 
ATOM   14889 C CD2 . TYR D 1 270 ? 28.977  -14.852 -12.905 1.00 66.43  ? 270 TYR D CD2 1 
ATOM   14890 C CE1 . TYR D 1 270 ? 29.219  -12.248 -13.766 1.00 67.42  ? 270 TYR D CE1 1 
ATOM   14891 C CE2 . TYR D 1 270 ? 28.103  -14.359 -13.858 1.00 66.75  ? 270 TYR D CE2 1 
ATOM   14892 C CZ  . TYR D 1 270 ? 28.225  -13.053 -14.291 1.00 67.72  ? 270 TYR D CZ  1 
ATOM   14893 O OH  . TYR D 1 270 ? 27.365  -12.569 -15.232 1.00 69.28  ? 270 TYR D OH  1 
ATOM   14894 N N   . ALA D 1 271 ? 28.588  -15.035 -9.431  1.00 63.57  ? 271 ALA D N   1 
ATOM   14895 C CA  . ALA D 1 271 ? 27.147  -14.878 -9.214  1.00 62.67  ? 271 ALA D CA  1 
ATOM   14896 C C   . ALA D 1 271 ? 26.618  -15.828 -8.136  1.00 63.32  ? 271 ALA D C   1 
ATOM   14897 O O   . ALA D 1 271 ? 27.027  -16.982 -8.048  1.00 64.67  ? 271 ALA D O   1 
ATOM   14898 C CB  . ALA D 1 271 ? 26.425  -15.115 -10.518 1.00 62.43  ? 271 ALA D CB  1 
ATOM   14899 N N   . ASP D 1 272 ? 25.647  -15.382 -7.338  1.00 64.04  ? 272 ASP D N   1 
ATOM   14900 C CA  . ASP D 1 272 ? 25.037  -16.279 -6.364  1.00 64.62  ? 272 ASP D CA  1 
ATOM   14901 C C   . ASP D 1 272 ? 24.437  -17.517 -7.031  1.00 65.11  ? 272 ASP D C   1 
ATOM   14902 O O   . ASP D 1 272 ? 24.070  -17.512 -8.215  1.00 63.75  ? 272 ASP D O   1 
ATOM   14903 C CB  . ASP D 1 272 ? 23.904  -15.651 -5.566  1.00 65.62  ? 272 ASP D CB  1 
ATOM   14904 C CG  . ASP D 1 272 ? 24.269  -14.580 -4.538  1.00 65.68  ? 272 ASP D CG  1 
ATOM   14905 O OD1 . ASP D 1 272 ? 25.505  -14.446 -4.233  1.00 62.76  ? 272 ASP D OD1 1 
ATOM   14906 O OD2 . ASP D 1 272 ? 23.287  -13.897 -4.041  1.00 65.53  ? 272 ASP D OD2 1 
ATOM   14907 N N   . GLY D 1 273 ? 24.371  -18.567 -6.197  1.00 65.79  ? 273 GLY D N   1 
ATOM   14908 C CA  . GLY D 1 273 ? 23.743  -19.839 -6.502  1.00 66.68  ? 273 GLY D CA  1 
ATOM   14909 C C   . GLY D 1 273 ? 22.734  -20.193 -5.409  1.00 68.58  ? 273 GLY D C   1 
ATOM   14910 O O   . GLY D 1 273 ? 23.137  -20.610 -4.322  1.00 68.09  ? 273 GLY D O   1 
ATOM   14911 N N   . TRP D 1 274 ? 21.428  -20.014 -5.714  1.00 68.67  ? 274 TRP D N   1 
ATOM   14912 C CA  . TRP D 1 274 ? 20.356  -20.229 -4.765  1.00 67.20  ? 274 TRP D CA  1 
ATOM   14913 C C   . TRP D 1 274 ? 20.143  -21.699 -4.446  1.00 67.25  ? 274 TRP D C   1 
ATOM   14914 O O   . TRP D 1 274 ? 19.321  -22.008 -3.561  1.00 67.74  ? 274 TRP D O   1 
ATOM   14915 C CB  . TRP D 1 274 ? 19.067  -19.683 -5.364  1.00 69.20  ? 274 TRP D CB  1 
ATOM   14916 C CG  . TRP D 1 274 ? 18.981  -18.184 -5.402  1.00 68.24  ? 274 TRP D CG  1 
ATOM   14917 C CD1 . TRP D 1 274 ? 19.984  -17.282 -5.281  1.00 65.99  ? 274 TRP D CD1 1 
ATOM   14918 C CD2 . TRP D 1 274 ? 17.770  -17.427 -5.595  1.00 68.70  ? 274 TRP D CD2 1 
ATOM   14919 N NE1 . TRP D 1 274 ? 19.479  -16.017 -5.377  1.00 65.96  ? 274 TRP D NE1 1 
ATOM   14920 C CE2 . TRP D 1 274 ? 18.137  -16.072 -5.576  1.00 68.06  ? 274 TRP D CE2 1 
ATOM   14921 C CE3 . TRP D 1 274 ? 16.425  -17.768 -5.760  1.00 69.78  ? 274 TRP D CE3 1 
ATOM   14922 C CZ2 . TRP D 1 274 ? 17.203  -15.048 -5.717  1.00 71.21  ? 274 TRP D CZ2 1 
ATOM   14923 C CZ3 . TRP D 1 274 ? 15.504  -16.757 -5.916  1.00 71.58  ? 274 TRP D CZ3 1 
ATOM   14924 C CH2 . TRP D 1 274 ? 15.881  -15.413 -5.891  1.00 71.59  ? 274 TRP D CH2 1 
ATOM   14925 N N   . TRP D 1 275 ? 20.811  -22.576 -5.220  1.00 66.37  ? 275 TRP D N   1 
ATOM   14926 C CA  . TRP D 1 275 ? 20.729  -24.021 -5.003  1.00 67.05  ? 275 TRP D CA  1 
ATOM   14927 C C   . TRP D 1 275 ? 21.577  -24.489 -3.815  1.00 66.62  ? 275 TRP D C   1 
ATOM   14928 O O   . TRP D 1 275 ? 21.304  -25.533 -3.241  1.00 65.94  ? 275 TRP D O   1 
ATOM   14929 C CB  . TRP D 1 275 ? 21.142  -24.803 -6.261  1.00 66.87  ? 275 TRP D CB  1 
ATOM   14930 C CG  . TRP D 1 275 ? 22.619  -24.749 -6.560  1.00 65.51  ? 275 TRP D CG  1 
ATOM   14931 C CD1 . TRP D 1 275 ? 23.262  -23.798 -7.294  1.00 64.86  ? 275 TRP D CD1 1 
ATOM   14932 C CD2 . TRP D 1 275 ? 23.639  -25.674 -6.140  1.00 64.81  ? 275 TRP D CD2 1 
ATOM   14933 N NE1 . TRP D 1 275 ? 24.601  -24.050 -7.350  1.00 63.53  ? 275 TRP D NE1 1 
ATOM   14934 C CE2 . TRP D 1 275 ? 24.865  -25.193 -6.654  1.00 63.70  ? 275 TRP D CE2 1 
ATOM   14935 C CE3 . TRP D 1 275 ? 23.639  -26.861 -5.398  1.00 65.40  ? 275 TRP D CE3 1 
ATOM   14936 C CZ2 . TRP D 1 275 ? 26.074  -25.853 -6.444  1.00 63.11  ? 275 TRP D CZ2 1 
ATOM   14937 C CZ3 . TRP D 1 275 ? 24.831  -27.528 -5.210  1.00 64.54  ? 275 TRP D CZ3 1 
ATOM   14938 C CH2 . TRP D 1 275 ? 26.032  -27.023 -5.717  1.00 63.83  ? 275 TRP D CH2 1 
ATOM   14939 N N   . LYS D 1 276 ? 22.594  -23.715 -3.427  1.00 67.24  ? 276 LYS D N   1 
ATOM   14940 C CA  . LYS D 1 276 ? 23.679  -24.239 -2.604  1.00 68.13  ? 276 LYS D CA  1 
ATOM   14941 C C   . LYS D 1 276 ? 23.207  -24.540 -1.180  1.00 68.99  ? 276 LYS D C   1 
ATOM   14942 O O   . LYS D 1 276 ? 23.814  -25.331 -0.466  1.00 66.38  ? 276 LYS D O   1 
ATOM   14943 C CB  . LYS D 1 276 ? 24.867  -23.260 -2.643  1.00 66.95  ? 276 LYS D CB  1 
ATOM   14944 C CG  . LYS D 1 276 ? 25.527  -23.141 -4.017  1.00 65.99  ? 276 LYS D CG  1 
ATOM   14945 C CD  . LYS D 1 276 ? 26.635  -22.113 -4.127  1.00 64.86  ? 276 LYS D CD  1 
ATOM   14946 C CE  . LYS D 1 276 ? 27.817  -22.525 -3.338  1.00 65.43  ? 276 LYS D CE  1 
ATOM   14947 N NZ  . LYS D 1 276 ? 28.746  -23.396 -4.072  1.00 65.54  ? 276 LYS D NZ  1 
ATOM   14948 N N   . GLY D 1 277 ? 22.106  -23.931 -0.777  1.00 71.87  ? 277 GLY D N   1 
ATOM   14949 C CA  . GLY D 1 277 ? 21.652  -24.136 0.607   1.00 74.78  ? 277 GLY D CA  1 
ATOM   14950 C C   . GLY D 1 277 ? 20.413  -25.000 0.636   1.00 79.34  ? 277 GLY D C   1 
ATOM   14951 O O   . GLY D 1 277 ? 19.879  -25.234 1.732   1.00 84.45  ? 277 GLY D O   1 
ATOM   14952 N N   . GLY D 1 278 ? 19.972  -25.450 -0.533  1.00 79.92  ? 278 GLY D N   1 
ATOM   14953 C CA  . GLY D 1 278 ? 18.730  -26.223 -0.588  1.00 84.77  ? 278 GLY D CA  1 
ATOM   14954 C C   . GLY D 1 278 ? 17.809  -25.731 -1.675  1.00 87.52  ? 278 GLY D C   1 
ATOM   14955 O O   . GLY D 1 278 ? 18.093  -26.000 -2.852  1.00 103.71 ? 278 GLY D O   1 
ATOM   14956 N N   . GLU D 1 279 ? 16.753  -25.015 -1.307  1.00 83.32  ? 279 GLU D N   1 
ATOM   14957 C CA  . GLU D 1 279 ? 15.729  -24.635 -2.312  1.00 80.24  ? 279 GLU D CA  1 
ATOM   14958 C C   . GLU D 1 279 ? 16.373  -23.826 -3.440  1.00 80.88  ? 279 GLU D C   1 
ATOM   14959 O O   . GLU D 1 279 ? 16.872  -22.743 -3.150  1.00 80.60  ? 279 GLU D O   1 
ATOM   14960 C CB  . GLU D 1 279 ? 14.545  -24.058 -1.540  1.00 77.76  ? 279 GLU D CB  1 
ATOM   14961 C CG  . GLU D 1 279 ? 13.914  -25.080 -0.602  1.00 78.20  ? 279 GLU D CG  1 
ATOM   14962 C CD  . GLU D 1 279 ? 13.838  -24.629 0.841   1.00 79.58  ? 279 GLU D CD  1 
ATOM   14963 O OE1 . GLU D 1 279 ? 13.054  -23.701 1.118   1.00 84.27  ? 279 GLU D OE1 1 
ATOM   14964 O OE2 . GLU D 1 279 ? 14.553  -25.201 1.685   1.00 77.30  ? 279 GLU D OE2 1 
ATOM   14965 N N   . LYS D 1 280 ? 16.274  -24.312 -4.666  1.00 77.94  ? 280 LYS D N   1 
ATOM   14966 C CA  . LYS D 1 280 ? 16.880  -23.750 -5.857  1.00 76.32  ? 280 LYS D CA  1 
ATOM   14967 C C   . LYS D 1 280 ? 16.054  -22.565 -6.334  1.00 75.48  ? 280 LYS D C   1 
ATOM   14968 O O   . LYS D 1 280 ? 16.509  -21.814 -7.193  1.00 74.31  ? 280 LYS D O   1 
ATOM   14969 C CB  . LYS D 1 280 ? 17.066  -24.755 -6.992  1.00 76.14  ? 280 LYS D CB  1 
ATOM   14970 C CG  . LYS D 1 280 ? 15.808  -25.337 -7.592  1.00 77.44  ? 280 LYS D CG  1 
ATOM   14971 C CD  . LYS D 1 280 ? 16.156  -26.487 -8.525  1.00 77.66  ? 280 LYS D CD  1 
ATOM   14972 C CE  . LYS D 1 280 ? 14.949  -27.131 -9.105  1.00 79.93  ? 280 LYS D CE  1 
ATOM   14973 N NZ  . LYS D 1 280 ? 15.331  -28.009 -10.212 1.00 81.06  ? 280 LYS D NZ  1 
ATOM   14974 N N   . SER D 1 281 ? 14.860  -22.405 -5.752  1.00 74.80  ? 281 SER D N   1 
ATOM   14975 C CA  . SER D 1 281 ? 14.026  -21.247 -6.028  1.00 74.11  ? 281 SER D CA  1 
ATOM   14976 C C   . SER D 1 281 ? 13.736  -20.441 -4.756  1.00 72.75  ? 281 SER D C   1 
ATOM   14977 O O   . SER D 1 281 ? 12.809  -19.654 -4.763  1.00 78.12  ? 281 SER D O   1 
ATOM   14978 C CB  . SER D 1 281 ? 12.733  -21.682 -6.707  1.00 75.55  ? 281 SER D CB  1 
ATOM   14979 O OG  . SER D 1 281 ? 12.995  -22.484 -7.852  1.00 75.86  ? 281 SER D OG  1 
ATOM   14980 N N   . ASP D 1 282 ? 14.455  -20.658 -3.649  1.00 69.70  ? 282 ASP D N   1 
ATOM   14981 C CA  . ASP D 1 282 ? 14.381  -19.795 -2.477  1.00 68.13  ? 282 ASP D CA  1 
ATOM   14982 C C   . ASP D 1 282 ? 15.794  -19.317 -2.142  1.00 66.84  ? 282 ASP D C   1 
ATOM   14983 O O   . ASP D 1 282 ? 16.709  -20.149 -1.961  1.00 67.33  ? 282 ASP D O   1 
ATOM   14984 C CB  . ASP D 1 282 ? 13.756  -20.495 -1.283  1.00 68.11  ? 282 ASP D CB  1 
ATOM   14985 C CG  . ASP D 1 282 ? 13.732  -19.748 0.050   1.00 68.02  ? 282 ASP D CG  1 
ATOM   14986 O OD1 . ASP D 1 282 ? 12.997  -18.766 0.183   1.00 69.28  ? 282 ASP D OD1 1 
ATOM   14987 O OD2 . ASP D 1 282 ? 14.416  -20.164 0.987   1.00 67.80  ? 282 ASP D OD2 1 
ATOM   14988 N N   . HIS D 1 283 ? 15.953  -17.983 -2.119  1.00 65.85  ? 283 HIS D N   1 
ATOM   14989 C CA  . HIS D 1 283 ? 17.129  -17.316 -1.581  1.00 64.43  ? 283 HIS D CA  1 
ATOM   14990 C C   . HIS D 1 283 ? 16.973  -17.244 -0.065  1.00 64.71  ? 283 HIS D C   1 
ATOM   14991 O O   . HIS D 1 283 ? 16.430  -16.298 0.470   1.00 65.05  ? 283 HIS D O   1 
ATOM   14992 C CB  . HIS D 1 283 ? 17.370  -15.948 -2.233  1.00 63.88  ? 283 HIS D CB  1 
ATOM   14993 C CG  . HIS D 1 283 ? 18.799  -15.523 -2.326  1.00 63.31  ? 283 HIS D CG  1 
ATOM   14994 N ND1 . HIS D 1 283 ? 19.189  -14.259 -2.718  1.00 63.89  ? 283 HIS D ND1 1 
ATOM   14995 C CD2 . HIS D 1 283 ? 19.944  -16.216 -2.158  1.00 62.80  ? 283 HIS D CD2 1 
ATOM   14996 C CE1 . HIS D 1 283 ? 20.529  -14.207 -2.770  1.00 63.12  ? 283 HIS D CE1 1 
ATOM   14997 N NE2 . HIS D 1 283 ? 21.008  -15.376 -2.404  1.00 61.97  ? 283 HIS D NE2 1 
ATOM   14998 N N   . SER D 1 284 ? 17.478  -18.264 0.624   1.00 65.30  ? 284 SER D N   1 
ATOM   14999 C CA  . SER D 1 284 ? 17.407  -18.355 2.072   1.00 65.83  ? 284 SER D CA  1 
ATOM   15000 C C   . SER D 1 284 ? 18.151  -17.190 2.715   1.00 64.79  ? 284 SER D C   1 
ATOM   15001 O O   . SER D 1 284 ? 19.224  -16.811 2.260   1.00 64.21  ? 284 SER D O   1 
ATOM   15002 C CB  . SER D 1 284 ? 17.968  -19.687 2.502   1.00 66.47  ? 284 SER D CB  1 
ATOM   15003 O OG  . SER D 1 284 ? 17.945  -19.870 3.912   1.00 67.30  ? 284 SER D OG  1 
ATOM   15004 N N   . LEU D 1 285 ? 17.543  -16.599 3.748   1.00 65.06  ? 285 LEU D N   1 
ATOM   15005 C CA  . LEU D 1 285 ? 18.074  -15.413 4.401   1.00 63.59  ? 285 LEU D CA  1 
ATOM   15006 C C   . LEU D 1 285 ? 19.238  -15.852 5.265   1.00 64.01  ? 285 LEU D C   1 
ATOM   15007 O O   . LEU D 1 285 ? 20.067  -15.006 5.625   1.00 63.69  ? 285 LEU D O   1 
ATOM   15008 C CB  . LEU D 1 285 ? 17.062  -14.700 5.300   1.00 63.69  ? 285 LEU D CB  1 
ATOM   15009 C CG  . LEU D 1 285 ? 15.769  -14.207 4.647   1.00 64.01  ? 285 LEU D CG  1 
ATOM   15010 C CD1 . LEU D 1 285 ? 14.906  -13.631 5.767   1.00 65.00  ? 285 LEU D CD1 1 
ATOM   15011 C CD2 . LEU D 1 285 ? 16.004  -13.203 3.511   1.00 63.12  ? 285 LEU D CD2 1 
ATOM   15012 N N   . ASN D 1 286 ? 19.272  -17.151 5.626   1.00 64.89  ? 286 ASN D N   1 
ATOM   15013 C CA  . ASN D 1 286 ? 20.294  -17.607 6.548   1.00 65.73  ? 286 ASN D CA  1 
ATOM   15014 C C   . ASN D 1 286 ? 21.064  -18.766 5.956   1.00 65.09  ? 286 ASN D C   1 
ATOM   15015 O O   . ASN D 1 286 ? 21.483  -19.643 6.702   1.00 66.61  ? 286 ASN D O   1 
ATOM   15016 C CB  . ASN D 1 286 ? 19.726  -18.010 7.897   1.00 68.73  ? 286 ASN D CB  1 
ATOM   15017 C CG  . ASN D 1 286 ? 18.821  -19.208 7.767   1.00 73.02  ? 286 ASN D CG  1 
ATOM   15018 O OD1 . ASN D 1 286 ? 18.459  -19.603 6.652   1.00 75.87  ? 286 ASN D OD1 1 
ATOM   15019 N ND2 . ASN D 1 286 ? 18.449  -19.812 8.884   1.00 75.64  ? 286 ASN D ND2 1 
ATOM   15020 N N   . GLN D 1 287 ? 21.264  -18.769 4.635   1.00 64.37  ? 287 GLN D N   1 
ATOM   15021 C CA  . GLN D 1 287 ? 22.134  -19.768 4.018   1.00 63.40  ? 287 GLN D CA  1 
ATOM   15022 C C   . GLN D 1 287 ? 23.361  -19.070 3.438   1.00 61.40  ? 287 GLN D C   1 
ATOM   15023 O O   . GLN D 1 287 ? 23.384  -18.680 2.270   1.00 60.07  ? 287 GLN D O   1 
ATOM   15024 C CB  . GLN D 1 287 ? 21.439  -20.624 2.959   1.00 63.77  ? 287 GLN D CB  1 
ATOM   15025 C CG  . GLN D 1 287 ? 20.359  -21.512 3.547   1.00 65.50  ? 287 GLN D CG  1 
ATOM   15026 C CD  . GLN D 1 287 ? 20.890  -22.733 4.257   1.00 66.43  ? 287 GLN D CD  1 
ATOM   15027 O OE1 . GLN D 1 287 ? 21.984  -23.207 3.978   1.00 66.75  ? 287 GLN D OE1 1 
ATOM   15028 N NE2 . GLN D 1 287 ? 20.101  -23.290 5.157   1.00 68.39  ? 287 GLN D NE2 1 
ATOM   15029 N N   . PRO D 1 288 ? 24.428  -18.924 4.246   1.00 60.75  ? 288 PRO D N   1 
ATOM   15030 C CA  . PRO D 1 288 ? 25.677  -18.339 3.765   1.00 60.55  ? 288 PRO D CA  1 
ATOM   15031 C C   . PRO D 1 288 ? 26.120  -18.800 2.384   1.00 60.94  ? 288 PRO D C   1 
ATOM   15032 O O   . PRO D 1 288 ? 26.791  -18.047 1.683   1.00 61.61  ? 288 PRO D O   1 
ATOM   15033 C CB  . PRO D 1 288 ? 26.680  -18.769 4.839   1.00 59.93  ? 288 PRO D CB  1 
ATOM   15034 C CG  . PRO D 1 288 ? 25.849  -18.776 6.097   1.00 60.82  ? 288 PRO D CG  1 
ATOM   15035 C CD  . PRO D 1 288 ? 24.483  -19.305 5.666   1.00 61.23  ? 288 PRO D CD  1 
ATOM   15036 N N   . GLU D 1 289 ? 25.766  -20.034 2.016   1.00 62.13  ? 289 GLU D N   1 
ATOM   15037 C CA  . GLU D 1 289 ? 26.242  -20.608 0.770   1.00 62.76  ? 289 GLU D CA  1 
ATOM   15038 C C   . GLU D 1 289 ? 25.637  -19.831 -0.400  1.00 61.52  ? 289 GLU D C   1 
ATOM   15039 O O   . GLU D 1 289 ? 26.225  -19.745 -1.472  1.00 61.00  ? 289 GLU D O   1 
ATOM   15040 C CB  . GLU D 1 289 ? 25.985  -22.122 0.764   1.00 65.21  ? 289 GLU D CB  1 
ATOM   15041 C CG  . GLU D 1 289 ? 27.030  -22.938 1.532   1.00 66.34  ? 289 GLU D CG  1 
ATOM   15042 C CD  . GLU D 1 289 ? 28.501  -22.630 1.219   1.00 68.95  ? 289 GLU D CD  1 
ATOM   15043 O OE1 . GLU D 1 289 ? 28.981  -22.816 0.062   1.00 70.66  ? 289 GLU D OE1 1 
ATOM   15044 O OE2 . GLU D 1 289 ? 29.220  -22.201 2.161   1.00 69.36  ? 289 GLU D OE2 1 
ATOM   15045 N N   . GLU D 1 290 ? 24.473  -19.224 -0.183  1.00 61.58  ? 290 GLU D N   1 
ATOM   15046 C CA  . GLU D 1 290 ? 23.673  -18.758 -1.298  1.00 62.22  ? 290 GLU D CA  1 
ATOM   15047 C C   . GLU D 1 290 ? 23.985  -17.288 -1.611  1.00 62.89  ? 290 GLU D C   1 
ATOM   15048 O O   . GLU D 1 290 ? 23.298  -16.685 -2.438  1.00 63.67  ? 290 GLU D O   1 
ATOM   15049 C CB  . GLU D 1 290 ? 22.189  -18.989 -0.981  1.00 62.87  ? 290 GLU D CB  1 
ATOM   15050 C CG  . GLU D 1 290 ? 21.693  -20.439 -0.989  1.00 63.39  ? 290 GLU D CG  1 
ATOM   15051 C CD  . GLU D 1 290 ? 20.178  -20.637 -1.024  1.00 64.70  ? 290 GLU D CD  1 
ATOM   15052 O OE1 . GLU D 1 290 ? 19.488  -19.597 -1.079  1.00 64.65  ? 290 GLU D OE1 1 
ATOM   15053 O OE2 . GLU D 1 290 ? 19.645  -21.780 -1.027  1.00 66.07  ? 290 GLU D OE2 1 
ATOM   15054 N N   . TRP D 1 291 ? 25.014  -16.692 -0.977  1.00 62.44  ? 291 TRP D N   1 
ATOM   15055 C CA  . TRP D 1 291 ? 25.221  -15.252 -1.094  1.00 61.69  ? 291 TRP D CA  1 
ATOM   15056 C C   . TRP D 1 291 ? 26.674  -14.859 -1.324  1.00 61.25  ? 291 TRP D C   1 
ATOM   15057 O O   . TRP D 1 291 ? 27.006  -13.726 -0.988  1.00 61.63  ? 291 TRP D O   1 
ATOM   15058 C CB  . TRP D 1 291 ? 24.696  -14.533 0.157   1.00 61.85  ? 291 TRP D CB  1 
ATOM   15059 C CG  . TRP D 1 291 ? 23.199  -14.630 0.333   1.00 61.90  ? 291 TRP D CG  1 
ATOM   15060 C CD1 . TRP D 1 291 ? 22.549  -15.717 0.812   1.00 62.12  ? 291 TRP D CD1 1 
ATOM   15061 C CD2 . TRP D 1 291 ? 22.192  -13.631 0.086   1.00 61.19  ? 291 TRP D CD2 1 
ATOM   15062 N NE1 . TRP D 1 291 ? 21.216  -15.477 0.867   1.00 63.55  ? 291 TRP D NE1 1 
ATOM   15063 C CE2 . TRP D 1 291 ? 20.962  -14.202 0.442   1.00 63.23  ? 291 TRP D CE2 1 
ATOM   15064 C CE3 . TRP D 1 291 ? 22.190  -12.326 -0.405  1.00 61.08  ? 291 TRP D CE3 1 
ATOM   15065 C CZ2 . TRP D 1 291 ? 19.750  -13.516 0.327   1.00 63.54  ? 291 TRP D CZ2 1 
ATOM   15066 C CZ3 . TRP D 1 291 ? 20.995  -11.645 -0.518  1.00 61.54  ? 291 TRP D CZ3 1 
ATOM   15067 C CH2 . TRP D 1 291 ? 19.796  -12.225 -0.146  1.00 62.46  ? 291 TRP D CH2 1 
ATOM   15068 N N   . PHE D 1 292 ? 27.501  -15.744 -1.920  1.00 60.92  ? 292 PHE D N   1 
ATOM   15069 C CA  . PHE D 1 292 ? 28.922  -15.466 -2.139  1.00 59.81  ? 292 PHE D CA  1 
ATOM   15070 C C   . PHE D 1 292 ? 29.179  -14.718 -3.448  1.00 59.97  ? 292 PHE D C   1 
ATOM   15071 O O   . PHE D 1 292 ? 30.320  -14.463 -3.787  1.00 59.47  ? 292 PHE D O   1 
ATOM   15072 C CB  . PHE D 1 292 ? 29.754  -16.752 -2.175  1.00 59.99  ? 292 PHE D CB  1 
ATOM   15073 C CG  . PHE D 1 292 ? 30.215  -17.296 -0.821  1.00 59.57  ? 292 PHE D CG  1 
ATOM   15074 C CD1 . PHE D 1 292 ? 31.415  -16.876 -0.263  1.00 57.94  ? 292 PHE D CD1 1 
ATOM   15075 C CD2 . PHE D 1 292 ? 29.444  -18.209 -0.100  1.00 59.58  ? 292 PHE D CD2 1 
ATOM   15076 C CE1 . PHE D 1 292 ? 31.823  -17.325 0.975   1.00 57.82  ? 292 PHE D CE1 1 
ATOM   15077 C CE2 . PHE D 1 292 ? 29.865  -18.661 1.141   1.00 58.95  ? 292 PHE D CE2 1 
ATOM   15078 C CZ  . PHE D 1 292 ? 31.061  -18.238 1.661   1.00 58.41  ? 292 PHE D CZ  1 
ATOM   15079 N N   . GLY D 1 293 ? 28.124  -14.289 -4.153  1.00 62.14  ? 293 GLY D N   1 
ATOM   15080 C CA  . GLY D 1 293 ? 28.265  -13.694 -5.476  1.00 61.77  ? 293 GLY D CA  1 
ATOM   15081 C C   . GLY D 1 293 ? 28.949  -12.333 -5.422  1.00 60.89  ? 293 GLY D C   1 
ATOM   15082 O O   . GLY D 1 293 ? 28.881  -11.657 -4.403  1.00 61.32  ? 293 GLY D O   1 
ATOM   15083 N N   . PHE D 1 294 ? 29.660  -11.985 -6.505  1.00 59.83  ? 294 PHE D N   1 
ATOM   15084 C CA  . PHE D 1 294 ? 29.926  -10.601 -6.848  1.00 59.05  ? 294 PHE D CA  1 
ATOM   15085 C C   . PHE D 1 294 ? 28.675  -10.003 -7.517  1.00 60.94  ? 294 PHE D C   1 
ATOM   15086 O O   . PHE D 1 294 ? 28.496  -8.772  -7.534  1.00 62.53  ? 294 PHE D O   1 
ATOM   15087 C CB  . PHE D 1 294 ? 31.159  -10.491 -7.748  1.00 58.27  ? 294 PHE D CB  1 
ATOM   15088 C CG  . PHE D 1 294 ? 32.506  -10.846 -7.129  1.00 57.36  ? 294 PHE D CG  1 
ATOM   15089 C CD1 . PHE D 1 294 ? 32.601  -11.333 -5.826  1.00 57.03  ? 294 PHE D CD1 1 
ATOM   15090 C CD2 . PHE D 1 294 ? 33.671  -10.785 -7.893  1.00 56.90  ? 294 PHE D CD2 1 
ATOM   15091 C CE1 . PHE D 1 294 ? 33.829  -11.672 -5.275  1.00 56.18  ? 294 PHE D CE1 1 
ATOM   15092 C CE2 . PHE D 1 294 ? 34.894  -11.135 -7.345  1.00 56.60  ? 294 PHE D CE2 1 
ATOM   15093 C CZ  . PHE D 1 294 ? 34.971  -11.575 -6.038  1.00 56.37  ? 294 PHE D CZ  1 
ATOM   15094 N N   . TRP D 1 295 ? 27.791  -10.876 -8.050  1.00 60.68  ? 295 TRP D N   1 
ATOM   15095 C CA  . TRP D 1 295 ? 26.540  -10.471 -8.685  1.00 60.33  ? 295 TRP D CA  1 
ATOM   15096 C C   . TRP D 1 295 ? 25.347  -11.101 -7.969  1.00 59.69  ? 295 TRP D C   1 
ATOM   15097 O O   . TRP D 1 295 ? 25.392  -12.251 -7.551  1.00 59.71  ? 295 TRP D O   1 
ATOM   15098 C CB  . TRP D 1 295 ? 26.499  -10.856 -10.173 1.00 60.89  ? 295 TRP D CB  1 
ATOM   15099 C CG  . TRP D 1 295 ? 27.400  -10.081 -11.106 1.00 61.58  ? 295 TRP D CG  1 
ATOM   15100 C CD1 . TRP D 1 295 ? 28.766  -9.962  -11.071 1.00 61.59  ? 295 TRP D CD1 1 
ATOM   15101 C CD2 . TRP D 1 295 ? 26.968  -9.328  -12.261 1.00 62.61  ? 295 TRP D CD2 1 
ATOM   15102 N NE1 . TRP D 1 295 ? 29.214  -9.206  -12.124 1.00 62.13  ? 295 TRP D NE1 1 
ATOM   15103 C CE2 . TRP D 1 295 ? 28.130  -8.805  -12.872 1.00 63.54  ? 295 TRP D CE2 1 
ATOM   15104 C CE3 . TRP D 1 295 ? 25.725  -9.055  -12.835 1.00 63.48  ? 295 TRP D CE3 1 
ATOM   15105 C CZ2 . TRP D 1 295 ? 28.066  -8.017  -14.024 1.00 64.38  ? 295 TRP D CZ2 1 
ATOM   15106 C CZ3 . TRP D 1 295 ? 25.670  -8.309  -13.986 1.00 64.73  ? 295 TRP D CZ3 1 
ATOM   15107 C CH2 . TRP D 1 295 ? 26.822  -7.771  -14.555 1.00 64.88  ? 295 TRP D CH2 1 
ATOM   15108 N N   . GLY D 1 296 ? 24.260  -10.338 -7.893  1.00 59.73  ? 296 GLY D N   1 
ATOM   15109 C CA  . GLY D 1 296 ? 23.105  -10.665 -7.080  1.00 59.84  ? 296 GLY D CA  1 
ATOM   15110 C C   . GLY D 1 296 ? 21.872  -10.734 -7.966  1.00 60.99  ? 296 GLY D C   1 
ATOM   15111 O O   . GLY D 1 296 ? 21.784  -9.997  -8.937  1.00 61.86  ? 296 GLY D O   1 
ATOM   15112 N N   . TYR D 1 297 ? 20.983  -11.694 -7.684  1.00 61.90  ? 297 TYR D N   1 
ATOM   15113 C CA  . TYR D 1 297 ? 19.772  -11.867 -8.468  1.00 62.88  ? 297 TYR D CA  1 
ATOM   15114 C C   . TYR D 1 297 ? 18.634  -11.235 -7.690  1.00 63.60  ? 297 TYR D C   1 
ATOM   15115 O O   . TYR D 1 297 ? 18.512  -11.467 -6.498  1.00 63.35  ? 297 TYR D O   1 
ATOM   15116 C CB  . TYR D 1 297 ? 19.641  -13.348 -8.802  1.00 62.50  ? 297 TYR D CB  1 
ATOM   15117 C CG  . TYR D 1 297 ? 20.769  -13.810 -9.715  1.00 61.17  ? 297 TYR D CG  1 
ATOM   15118 C CD1 . TYR D 1 297 ? 20.820  -13.398 -11.044 1.00 61.67  ? 297 TYR D CD1 1 
ATOM   15119 C CD2 . TYR D 1 297 ? 21.755  -14.668 -9.271  1.00 59.56  ? 297 TYR D CD2 1 
ATOM   15120 C CE1 . TYR D 1 297 ? 21.798  -13.855 -11.911 1.00 61.31  ? 297 TYR D CE1 1 
ATOM   15121 C CE2 . TYR D 1 297 ? 22.734  -15.142 -10.130 1.00 59.37  ? 297 TYR D CE2 1 
ATOM   15122 C CZ  . TYR D 1 297 ? 22.774  -14.722 -11.450 1.00 60.22  ? 297 TYR D CZ  1 
ATOM   15123 O OH  . TYR D 1 297 ? 23.775  -15.098 -12.315 1.00 60.05  ? 297 TYR D OH  1 
ATOM   15124 N N   . SER D 1 298 ? 17.893  -10.383 -8.393  1.00 65.14  ? 298 SER D N   1 
ATOM   15125 C CA  . SER D 1 298 ? 16.846  -9.540  -7.849  1.00 66.74  ? 298 SER D CA  1 
ATOM   15126 C C   . SER D 1 298 ? 15.738  -10.384 -7.217  1.00 68.80  ? 298 SER D C   1 
ATOM   15127 O O   . SER D 1 298 ? 15.471  -10.256 -6.020  1.00 69.00  ? 298 SER D O   1 
ATOM   15128 C CB  . SER D 1 298 ? 16.329  -8.659  -8.958  1.00 67.79  ? 298 SER D CB  1 
ATOM   15129 O OG  . SER D 1 298 ? 14.960  -8.349  -8.779  1.00 70.44  ? 298 SER D OG  1 
ATOM   15130 N N   . ASP D 1 299 ? 15.126  -11.243 -8.053  1.00 70.49  ? 299 ASP D N   1 
ATOM   15131 C CA  . ASP D 1 299 ? 14.063  -12.163 -7.682  1.00 71.71  ? 299 ASP D CA  1 
ATOM   15132 C C   . ASP D 1 299 ? 14.161  -13.414 -8.561  1.00 73.20  ? 299 ASP D C   1 
ATOM   15133 O O   . ASP D 1 299 ? 15.125  -13.580 -9.304  1.00 72.54  ? 299 ASP D O   1 
ATOM   15134 C CB  . ASP D 1 299 ? 12.731  -11.459 -7.795  1.00 73.03  ? 299 ASP D CB  1 
ATOM   15135 C CG  . ASP D 1 299 ? 12.363  -10.965 -9.186  1.00 74.47  ? 299 ASP D CG  1 
ATOM   15136 O OD1 . ASP D 1 299 ? 13.053  -11.353 -10.153 1.00 72.70  ? 299 ASP D OD1 1 
ATOM   15137 O OD2 . ASP D 1 299 ? 11.348  -10.209 -9.283  1.00 77.55  ? 299 ASP D OD2 1 
ATOM   15138 N N   . LEU D 1 300 ? 13.177  -14.321 -8.475  1.00 75.27  ? 300 LEU D N   1 
ATOM   15139 C CA  . LEU D 1 300 ? 13.338  -15.657 -9.042  1.00 75.19  ? 300 LEU D CA  1 
ATOM   15140 C C   . LEU D 1 300 ? 13.482  -15.591 -10.559 1.00 76.44  ? 300 LEU D C   1 
ATOM   15141 O O   . LEU D 1 300 ? 14.196  -16.410 -11.136 1.00 76.55  ? 300 LEU D O   1 
ATOM   15142 C CB  . LEU D 1 300 ? 12.183  -16.587 -8.687  1.00 76.19  ? 300 LEU D CB  1 
ATOM   15143 C CG  . LEU D 1 300 ? 12.263  -17.999 -9.281  1.00 76.50  ? 300 LEU D CG  1 
ATOM   15144 C CD1 . LEU D 1 300 ? 13.346  -18.809 -8.580  1.00 75.98  ? 300 LEU D CD1 1 
ATOM   15145 C CD2 . LEU D 1 300 ? 10.931  -18.711 -9.201  1.00 78.09  ? 300 LEU D CD2 1 
ATOM   15146 N N   . ASN D 1 301 ? 12.790  -14.639 -11.206 1.00 76.78  ? 301 ASN D N   1 
ATOM   15147 C CA  . ASN D 1 301 ? 12.735  -14.627 -12.657 1.00 77.02  ? 301 ASN D CA  1 
ATOM   15148 C C   . ASN D 1 301 ? 13.946  -13.925 -13.256 1.00 75.80  ? 301 ASN D C   1 
ATOM   15149 O O   . ASN D 1 301 ? 14.011  -13.826 -14.478 1.00 78.44  ? 301 ASN D O   1 
ATOM   15150 C CB  . ASN D 1 301 ? 11.500  -13.928 -13.192 1.00 79.17  ? 301 ASN D CB  1 
ATOM   15151 C CG  . ASN D 1 301 ? 10.236  -14.531 -12.634 1.00 80.82  ? 301 ASN D CG  1 
ATOM   15152 O OD1 . ASN D 1 301 ? 10.008  -15.746 -12.743 1.00 81.04  ? 301 ASN D OD1 1 
ATOM   15153 N ND2 . ASN D 1 301 ? 9.418   -13.687 -12.025 1.00 81.48  ? 301 ASN D ND2 1 
ATOM   15154 N N   . ASP D 1 302 ? 14.884  -13.452 -12.418 1.00 72.39  ? 302 ASP D N   1 
ATOM   15155 C CA  . ASP D 1 302 ? 16.021  -12.676 -12.885 1.00 70.35  ? 302 ASP D CA  1 
ATOM   15156 C C   . ASP D 1 302 ? 17.155  -13.613 -13.315 1.00 68.97  ? 302 ASP D C   1 
ATOM   15157 O O   . ASP D 1 302 ? 17.774  -14.295 -12.496 1.00 66.63  ? 302 ASP D O   1 
ATOM   15158 C CB  . ASP D 1 302 ? 16.477  -11.699 -11.811 1.00 69.35  ? 302 ASP D CB  1 
ATOM   15159 C CG  . ASP D 1 302 ? 17.672  -10.821 -12.153 1.00 68.71  ? 302 ASP D CG  1 
ATOM   15160 O OD1 . ASP D 1 302 ? 18.090  -10.830 -13.329 1.00 69.04  ? 302 ASP D OD1 1 
ATOM   15161 O OD2 . ASP D 1 302 ? 18.185  -10.132 -11.239 1.00 68.28  ? 302 ASP D OD2 1 
ATOM   15162 N N   . LYS D 1 303 ? 17.457  -13.559 -14.618 1.00 69.36  ? 303 LYS D N   1 
ATOM   15163 C CA  . LYS D 1 303 ? 18.529  -14.308 -15.246 1.00 68.54  ? 303 LYS D CA  1 
ATOM   15164 C C   . LYS D 1 303 ? 19.836  -13.516 -15.393 1.00 66.89  ? 303 LYS D C   1 
ATOM   15165 O O   . LYS D 1 303 ? 20.803  -14.061 -15.932 1.00 65.92  ? 303 LYS D O   1 
ATOM   15166 C CB  . LYS D 1 303 ? 18.040  -14.725 -16.641 1.00 70.75  ? 303 LYS D CB  1 
ATOM   15167 C CG  . LYS D 1 303 ? 16.808  -15.619 -16.693 1.00 72.63  ? 303 LYS D CG  1 
ATOM   15168 C CD  . LYS D 1 303 ? 16.871  -16.836 -15.783 1.00 72.95  ? 303 LYS D CD  1 
ATOM   15169 C CE  . LYS D 1 303 ? 15.500  -17.287 -15.434 1.00 75.81  ? 303 LYS D CE  1 
ATOM   15170 N NZ  . LYS D 1 303 ? 15.589  -18.367 -14.450 1.00 76.68  ? 303 LYS D NZ  1 
ATOM   15171 N N   . TYR D 1 304 ? 19.887  -12.253 -14.927 1.00 66.25  ? 304 TYR D N   1 
ATOM   15172 C CA  . TYR D 1 304 ? 20.997  -11.361 -15.265 1.00 65.64  ? 304 TYR D CA  1 
ATOM   15173 C C   . TYR D 1 304 ? 21.669  -10.853 -13.992 1.00 64.13  ? 304 TYR D C   1 
ATOM   15174 O O   . TYR D 1 304 ? 22.859  -11.080 -13.797 1.00 63.17  ? 304 TYR D O   1 
ATOM   15175 C CB  . TYR D 1 304 ? 20.499  -10.272 -16.225 1.00 66.83  ? 304 TYR D CB  1 
ATOM   15176 C CG  . TYR D 1 304 ? 20.003  -10.882 -17.529 1.00 67.91  ? 304 TYR D CG  1 
ATOM   15177 C CD1 . TYR D 1 304 ? 20.902  -11.309 -18.497 1.00 67.88  ? 304 TYR D CD1 1 
ATOM   15178 C CD2 . TYR D 1 304 ? 18.650  -11.089 -17.766 1.00 69.23  ? 304 TYR D CD2 1 
ATOM   15179 C CE1 . TYR D 1 304 ? 20.480  -11.904 -19.671 1.00 69.18  ? 304 TYR D CE1 1 
ATOM   15180 C CE2 . TYR D 1 304 ? 18.207  -11.682 -18.940 1.00 70.74  ? 304 TYR D CE2 1 
ATOM   15181 C CZ  . TYR D 1 304 ? 19.129  -12.110 -19.886 1.00 70.81  ? 304 TYR D CZ  1 
ATOM   15182 O OH  . TYR D 1 304 ? 18.713  -12.704 -21.046 1.00 72.22  ? 304 TYR D OH  1 
ATOM   15183 N N   . GLY D 1 305 ? 20.896  -10.186 -13.130 1.00 64.35  ? 305 GLY D N   1 
ATOM   15184 C CA  . GLY D 1 305 ? 21.388  -9.732  -11.840 1.00 63.44  ? 305 GLY D CA  1 
ATOM   15185 C C   . GLY D 1 305 ? 22.116  -8.394  -11.957 1.00 63.47  ? 305 GLY D C   1 
ATOM   15186 O O   . GLY D 1 305 ? 22.100  -7.751  -13.004 1.00 64.17  ? 305 GLY D O   1 
ATOM   15187 N N   . THR D 1 306 ? 22.737  -7.958  -10.863 1.00 62.79  ? 306 THR D N   1 
ATOM   15188 C CA  . THR D 1 306 ? 23.551  -6.756  -10.911 1.00 63.14  ? 306 THR D CA  1 
ATOM   15189 C C   . THR D 1 306 ? 24.797  -6.967  -10.062 1.00 61.83  ? 306 THR D C   1 
ATOM   15190 O O   . THR D 1 306 ? 24.739  -7.603  -9.022  1.00 60.80  ? 306 THR D O   1 
ATOM   15191 C CB  . THR D 1 306 ? 22.778  -5.528  -10.430 1.00 63.79  ? 306 THR D CB  1 
ATOM   15192 O OG1 . THR D 1 306 ? 22.531  -5.764  -9.046  1.00 63.89  ? 306 THR D OG1 1 
ATOM   15193 C CG2 . THR D 1 306 ? 21.507  -5.257  -11.213 1.00 64.77  ? 306 THR D CG2 1 
ATOM   15194 N N   . PRO D 1 307 ? 25.938  -6.371  -10.457 1.00 61.93  ? 307 PRO D N   1 
ATOM   15195 C CA  . PRO D 1 307 ? 27.163  -6.452  -9.667  1.00 61.19  ? 307 PRO D CA  1 
ATOM   15196 C C   . PRO D 1 307 ? 27.068  -5.709  -8.340  1.00 60.87  ? 307 PRO D C   1 
ATOM   15197 O O   . PRO D 1 307 ? 26.802  -4.505  -8.338  1.00 62.98  ? 307 PRO D O   1 
ATOM   15198 C CB  . PRO D 1 307 ? 28.237  -5.766  -10.579 1.00 61.40  ? 307 PRO D CB  1 
ATOM   15199 C CG  . PRO D 1 307 ? 27.457  -4.860  -11.501 1.00 62.36  ? 307 PRO D CG  1 
ATOM   15200 C CD  . PRO D 1 307 ? 26.080  -5.520  -11.650 1.00 62.96  ? 307 PRO D CD  1 
ATOM   15201 N N   . ARG D 1 308 ? 27.399  -6.389  -7.241  1.00 59.55  ? 308 ARG D N   1 
ATOM   15202 C CA  . ARG D 1 308 ? 27.632  -5.709  -5.979  1.00 59.72  ? 308 ARG D CA  1 
ATOM   15203 C C   . ARG D 1 308 ? 28.968  -4.939  -5.952  1.00 61.18  ? 308 ARG D C   1 
ATOM   15204 O O   . ARG D 1 308 ? 29.877  -5.073  -6.795  1.00 61.11  ? 308 ARG D O   1 
ATOM   15205 C CB  . ARG D 1 308 ? 27.633  -6.740  -4.855  1.00 59.12  ? 308 ARG D CB  1 
ATOM   15206 C CG  . ARG D 1 308 ? 26.350  -7.551  -4.762  1.00 59.49  ? 308 ARG D CG  1 
ATOM   15207 C CD  . ARG D 1 308 ? 26.496  -8.773  -3.861  1.00 58.35  ? 308 ARG D CD  1 
ATOM   15208 N NE  . ARG D 1 308 ? 25.195  -9.433  -3.711  1.00 58.56  ? 308 ARG D NE  1 
ATOM   15209 C CZ  . ARG D 1 308 ? 24.996  -10.740 -3.744  1.00 58.54  ? 308 ARG D CZ  1 
ATOM   15210 N NH1 . ARG D 1 308 ? 26.051  -11.553 -3.882  1.00 58.55  ? 308 ARG D NH1 1 
ATOM   15211 N NH2 . ARG D 1 308 ? 23.769  -11.215 -3.585  1.00 58.16  ? 308 ARG D NH2 1 
ATOM   15212 N N   . PRO D 1 309 ? 29.156  -4.068  -4.944  1.00 61.40  ? 309 PRO D N   1 
ATOM   15213 C CA  . PRO D 1 309 ? 30.379  -3.283  -4.873  1.00 61.34  ? 309 PRO D CA  1 
ATOM   15214 C C   . PRO D 1 309 ? 31.699  -4.025  -5.067  1.00 61.22  ? 309 PRO D C   1 
ATOM   15215 O O   . PRO D 1 309 ? 32.627  -3.507  -5.695  1.00 62.42  ? 309 PRO D O   1 
ATOM   15216 C CB  . PRO D 1 309 ? 30.196  -2.672  -3.471  1.00 61.31  ? 309 PRO D CB  1 
ATOM   15217 C CG  . PRO D 1 309 ? 28.719  -2.386  -3.422  1.00 61.75  ? 309 PRO D CG  1 
ATOM   15218 C CD  . PRO D 1 309 ? 28.181  -3.712  -3.896  1.00 61.50  ? 309 PRO D CD  1 
ATOM   15219 N N   . VAL D 1 310 ? 31.809  -5.245  -4.552  1.00 60.71  ? 310 VAL D N   1 
ATOM   15220 C CA  . VAL D 1 310 ? 33.110  -5.900  -4.583  1.00 58.68  ? 310 VAL D CA  1 
ATOM   15221 C C   . VAL D 1 310 ? 33.615  -6.025  -6.020  1.00 57.72  ? 310 VAL D C   1 
ATOM   15222 O O   . VAL D 1 310 ? 34.815  -6.035  -6.250  1.00 57.25  ? 310 VAL D O   1 
ATOM   15223 C CB  . VAL D 1 310 ? 33.014  -7.275  -3.912  1.00 59.04  ? 310 VAL D CB  1 
ATOM   15224 C CG1 . VAL D 1 310 ? 32.142  -8.228  -4.721  1.00 59.33  ? 310 VAL D CG1 1 
ATOM   15225 C CG2 . VAL D 1 310 ? 34.381  -7.893  -3.661  1.00 59.09  ? 310 VAL D CG2 1 
ATOM   15226 N N   . TRP D 1 311 ? 32.700  -6.160  -6.985  1.00 57.65  ? 311 TRP D N   1 
ATOM   15227 C CA  . TRP D 1 311 ? 33.052  -6.294  -8.392  1.00 57.46  ? 311 TRP D CA  1 
ATOM   15228 C C   . TRP D 1 311 ? 33.977  -5.167  -8.799  1.00 58.63  ? 311 TRP D C   1 
ATOM   15229 O O   . TRP D 1 311 ? 35.049  -5.402  -9.360  1.00 60.40  ? 311 TRP D O   1 
ATOM   15230 C CB  . TRP D 1 311 ? 31.773  -6.254  -9.228  1.00 57.29  ? 311 TRP D CB  1 
ATOM   15231 C CG  . TRP D 1 311 ? 31.897  -6.406  -10.721 1.00 57.01  ? 311 TRP D CG  1 
ATOM   15232 C CD1 . TRP D 1 311 ? 31.659  -5.424  -11.632 1.00 57.65  ? 311 TRP D CD1 1 
ATOM   15233 C CD2 . TRP D 1 311 ? 32.117  -7.609  -11.493 1.00 56.74  ? 311 TRP D CD2 1 
ATOM   15234 N NE1 . TRP D 1 311 ? 31.755  -5.910  -12.907 1.00 58.08  ? 311 TRP D NE1 1 
ATOM   15235 C CE2 . TRP D 1 311 ? 32.042  -7.243  -12.858 1.00 57.54  ? 311 TRP D CE2 1 
ATOM   15236 C CE3 . TRP D 1 311 ? 32.393  -8.945  -11.174 1.00 55.95  ? 311 TRP D CE3 1 
ATOM   15237 C CZ2 . TRP D 1 311 ? 32.239  -8.150  -13.896 1.00 57.78  ? 311 TRP D CZ2 1 
ATOM   15238 C CZ3 . TRP D 1 311 ? 32.592  -9.845  -12.202 1.00 56.21  ? 311 TRP D CZ3 1 
ATOM   15239 C CH2 . TRP D 1 311 ? 32.506  -9.454  -13.544 1.00 57.18  ? 311 TRP D CH2 1 
ATOM   15240 N N   . PHE D 1 312 ? 33.536  -3.951  -8.457  1.00 59.18  ? 312 PHE D N   1 
ATOM   15241 C CA  . PHE D 1 312 ? 34.182  -2.725  -8.900  1.00 60.00  ? 312 PHE D CA  1 
ATOM   15242 C C   . PHE D 1 312 ? 35.529  -2.562  -8.190  1.00 59.65  ? 312 PHE D C   1 
ATOM   15243 O O   . PHE D 1 312 ? 36.501  -2.152  -8.816  1.00 59.35  ? 312 PHE D O   1 
ATOM   15244 C CB  . PHE D 1 312 ? 33.205  -1.572  -8.678  1.00 60.09  ? 312 PHE D CB  1 
ATOM   15245 C CG  . PHE D 1 312 ? 31.971  -1.597  -9.568  1.00 61.27  ? 312 PHE D CG  1 
ATOM   15246 C CD1 . PHE D 1 312 ? 32.052  -1.314  -10.927 1.00 62.86  ? 312 PHE D CD1 1 
ATOM   15247 C CD2 . PHE D 1 312 ? 30.717  -1.847  -9.032  1.00 61.90  ? 312 PHE D CD2 1 
ATOM   15248 C CE1 . PHE D 1 312 ? 30.909  -1.315  -11.728 1.00 64.46  ? 312 PHE D CE1 1 
ATOM   15249 C CE2 . PHE D 1 312 ? 29.581  -1.852  -9.835  1.00 63.10  ? 312 PHE D CE2 1 
ATOM   15250 C CZ  . PHE D 1 312 ? 29.677  -1.581  -11.178 1.00 64.01  ? 312 PHE D CZ  1 
ATOM   15251 N N   . ALA D 1 313 ? 35.549  -2.913  -6.894  1.00 58.52  ? 313 ALA D N   1 
ATOM   15252 C CA  . ALA D 1 313 ? 36.747  -2.913  -6.085  1.00 57.68  ? 313 ALA D CA  1 
ATOM   15253 C C   . ALA D 1 313 ? 37.790  -3.815  -6.736  1.00 59.62  ? 313 ALA D C   1 
ATOM   15254 O O   . ALA D 1 313 ? 38.959  -3.413  -6.898  1.00 59.42  ? 313 ALA D O   1 
ATOM   15255 C CB  . ALA D 1 313 ? 36.415  -3.314  -4.658  1.00 55.99  ? 313 ALA D CB  1 
ATOM   15256 N N   . MET D 1 314 ? 37.345  -5.022  -7.132  1.00 62.58  ? 314 MET D N   1 
ATOM   15257 C CA  . MET D 1 314 ? 38.244  -6.064  -7.641  1.00 64.03  ? 314 MET D CA  1 
ATOM   15258 C C   . MET D 1 314 ? 38.812  -5.655  -9.001  1.00 65.80  ? 314 MET D C   1 
ATOM   15259 O O   . MET D 1 314 ? 40.004  -5.816  -9.245  1.00 66.85  ? 314 MET D O   1 
ATOM   15260 C CB  . MET D 1 314 ? 37.537  -7.415  -7.753  1.00 63.18  ? 314 MET D CB  1 
ATOM   15261 C CG  . MET D 1 314 ? 37.373  -8.081  -6.411  1.00 63.10  ? 314 MET D CG  1 
ATOM   15262 S SD  . MET D 1 314 ? 38.954  -8.635  -5.750  1.00 64.60  ? 314 MET D SD  1 
ATOM   15263 C CE  . MET D 1 314 ? 39.229  -9.946  -6.959  1.00 63.73  ? 314 MET D CE  1 
ATOM   15264 N N   . ARG D 1 315 ? 37.964  -5.076  -9.863  1.00 65.55  ? 315 ARG D N   1 
ATOM   15265 C CA  . ARG D 1 315 ? 38.405  -4.672  -11.182 1.00 65.51  ? 315 ARG D CA  1 
ATOM   15266 C C   . ARG D 1 315 ? 39.541  -3.654  -11.045 1.00 66.05  ? 315 ARG D C   1 
ATOM   15267 O O   . ARG D 1 315 ? 40.660  -3.889  -11.534 1.00 66.07  ? 315 ARG D O   1 
ATOM   15268 C CB  . ARG D 1 315 ? 37.191  -4.130  -11.933 1.00 66.48  ? 315 ARG D CB  1 
ATOM   15269 C CG  . ARG D 1 315 ? 37.533  -3.567  -13.305 1.00 68.01  ? 315 ARG D CG  1 
ATOM   15270 C CD  . ARG D 1 315 ? 36.357  -2.793  -13.870 1.00 68.58  ? 315 ARG D CD  1 
ATOM   15271 N NE  . ARG D 1 315 ? 36.049  -1.667  -12.992 1.00 68.62  ? 315 ARG D NE  1 
ATOM   15272 C CZ  . ARG D 1 315 ? 35.081  -0.808  -13.217 1.00 70.36  ? 315 ARG D CZ  1 
ATOM   15273 N NH1 . ARG D 1 315 ? 34.242  -1.005  -14.212 1.00 70.57  ? 315 ARG D NH1 1 
ATOM   15274 N NH2 . ARG D 1 315 ? 34.969  0.262   -12.451 1.00 71.93  ? 315 ARG D NH2 1 
ATOM   15275 N N   . ASP D 1 316 ? 39.204  -2.529  -10.386 1.00 64.89  ? 316 ASP D N   1 
ATOM   15276 C CA  . ASP D 1 316 ? 40.096  -1.423  -10.096 1.00 63.44  ? 316 ASP D CA  1 
ATOM   15277 C C   . ASP D 1 316 ? 41.415  -1.971  -9.533  1.00 64.64  ? 316 ASP D C   1 
ATOM   15278 O O   . ASP D 1 316 ? 42.494  -1.628  -10.005 1.00 63.90  ? 316 ASP D O   1 
ATOM   15279 C CB  . ASP D 1 316 ? 39.391  -0.433  -9.177  1.00 62.38  ? 316 ASP D CB  1 
ATOM   15280 C CG  . ASP D 1 316 ? 38.302  0.470   -9.776  1.00 63.61  ? 316 ASP D CG  1 
ATOM   15281 O OD1 . ASP D 1 316 ? 38.138  0.505   -11.024 1.00 64.68  ? 316 ASP D OD1 1 
ATOM   15282 O OD2 . ASP D 1 316 ? 37.598  1.152   -8.989  1.00 62.45  ? 316 ASP D OD2 1 
ATOM   15283 N N   . TYR D 1 317 ? 41.334  -2.881  -8.551  1.00 65.37  ? 317 TYR D N   1 
ATOM   15284 C CA  . TYR D 1 317 ? 42.522  -3.338  -7.847  1.00 65.61  ? 317 TYR D CA  1 
ATOM   15285 C C   . TYR D 1 317 ? 43.421  -4.138  -8.783  1.00 66.32  ? 317 TYR D C   1 
ATOM   15286 O O   . TYR D 1 317 ? 44.641  -4.132  -8.607  1.00 67.06  ? 317 TYR D O   1 
ATOM   15287 C CB  . TYR D 1 317 ? 42.149  -4.233  -6.661  1.00 65.89  ? 317 TYR D CB  1 
ATOM   15288 C CG  . TYR D 1 317 ? 43.341  -4.750  -5.865  1.00 66.62  ? 317 TYR D CG  1 
ATOM   15289 C CD1 . TYR D 1 317 ? 43.893  -3.983  -4.850  1.00 66.27  ? 317 TYR D CD1 1 
ATOM   15290 C CD2 . TYR D 1 317 ? 43.914  -5.992  -6.131  1.00 67.50  ? 317 TYR D CD2 1 
ATOM   15291 C CE1 . TYR D 1 317 ? 44.974  -4.431  -4.120  1.00 66.74  ? 317 TYR D CE1 1 
ATOM   15292 C CE2 . TYR D 1 317 ? 45.000  -6.459  -5.406  1.00 67.57  ? 317 TYR D CE2 1 
ATOM   15293 C CZ  . TYR D 1 317 ? 45.532  -5.665  -4.403  1.00 68.64  ? 317 TYR D CZ  1 
ATOM   15294 O OH  . TYR D 1 317 ? 46.612  -6.054  -3.664  1.00 72.37  ? 317 TYR D OH  1 
ATOM   15295 N N   . MET D 1 318 ? 42.794  -4.847  -9.741  1.00 65.53  ? 318 MET D N   1 
ATOM   15296 C CA  . MET D 1 318 ? 43.466  -5.813  -10.607 1.00 64.50  ? 318 MET D CA  1 
ATOM   15297 C C   . MET D 1 318 ? 44.264  -5.140  -11.728 1.00 64.53  ? 318 MET D C   1 
ATOM   15298 O O   . MET D 1 318 ? 44.885  -5.834  -12.520 1.00 64.40  ? 318 MET D O   1 
ATOM   15299 C CB  . MET D 1 318 ? 42.456  -6.783  -11.252 1.00 64.22  ? 318 MET D CB  1 
ATOM   15300 C CG  . MET D 1 318 ? 42.091  -8.002  -10.395 1.00 62.74  ? 318 MET D CG  1 
ATOM   15301 S SD  . MET D 1 318 ? 41.213  -9.316  -11.272 1.00 63.01  ? 318 MET D SD  1 
ATOM   15302 C CE  . MET D 1 318 ? 39.793  -8.472  -11.989 1.00 62.02  ? 318 MET D CE  1 
ATOM   15303 N N   . LYS D 1 319 ? 44.231  -3.801  -11.826 1.00 65.29  ? 319 LYS D N   1 
ATOM   15304 C CA  . LYS D 1 319 ? 44.759  -3.118  -12.998 1.00 65.85  ? 319 LYS D CA  1 
ATOM   15305 C C   . LYS D 1 319 ? 46.276  -3.062  -12.919 1.00 66.04  ? 319 LYS D C   1 
ATOM   15306 O O   . LYS D 1 319 ? 46.953  -2.917  -13.934 1.00 66.38  ? 319 LYS D O   1 
ATOM   15307 C CB  . LYS D 1 319 ? 44.251  -1.684  -13.148 1.00 66.60  ? 319 LYS D CB  1 
ATOM   15308 C CG  . LYS D 1 319 ? 42.809  -1.541  -13.592 1.00 66.75  ? 319 LYS D CG  1 
ATOM   15309 C CD  . LYS D 1 319 ? 42.604  -0.590  -14.765 1.00 68.30  ? 319 LYS D CD  1 
ATOM   15310 C CE  . LYS D 1 319 ? 41.778  -1.244  -15.841 1.00 69.20  ? 319 LYS D CE  1 
ATOM   15311 N NZ  . LYS D 1 319 ? 42.266  -0.799  -17.148 1.00 71.12  ? 319 LYS D NZ  1 
ATOM   15312 N N   . GLY D 1 320 ? 46.778  -3.146  -11.688 1.00 65.34  ? 320 GLY D N   1 
ATOM   15313 C CA  . GLY D 1 320 ? 48.203  -3.231  -11.446 1.00 66.69  ? 320 GLY D CA  1 
ATOM   15314 C C   . GLY D 1 320 ? 48.482  -3.986  -10.152 1.00 66.47  ? 320 GLY D C   1 
ATOM   15315 O O   . GLY D 1 320 ? 48.118  -3.523  -9.069  1.00 66.43  ? 320 GLY D O   1 
ATOM   15316 N N   . LEU D 1 321 ? 49.131  -5.147  -10.274 1.00 65.93  ? 321 LEU D N   1 
ATOM   15317 C CA  . LEU D 1 321 ? 49.374  -5.963  -9.112  1.00 64.73  ? 321 LEU D CA  1 
ATOM   15318 C C   . LEU D 1 321 ? 50.854  -5.901  -8.730  1.00 65.64  ? 321 LEU D C   1 
ATOM   15319 O O   . LEU D 1 321 ? 51.761  -5.917  -9.567  1.00 66.17  ? 321 LEU D O   1 
ATOM   15320 C CB  . LEU D 1 321 ? 48.903  -7.342  -9.527  1.00 65.40  ? 321 LEU D CB  1 
ATOM   15321 C CG  . LEU D 1 321 ? 47.430  -7.439  -9.928  1.00 65.90  ? 321 LEU D CG  1 
ATOM   15322 C CD1 . LEU D 1 321 ? 47.175  -8.754  -10.603 1.00 66.23  ? 321 LEU D CD1 1 
ATOM   15323 C CD2 . LEU D 1 321 ? 46.520  -7.325  -8.722  1.00 66.04  ? 321 LEU D CD2 1 
ATOM   15324 N N   . ILE D 1 322 ? 51.066  -5.806  -7.417  1.00 64.37  ? 322 ILE D N   1 
ATOM   15325 C CA  . ILE D 1 322 ? 52.370  -5.856  -6.800  1.00 63.59  ? 322 ILE D CA  1 
ATOM   15326 C C   . ILE D 1 322 ? 52.578  -7.275  -6.304  1.00 62.72  ? 322 ILE D C   1 
ATOM   15327 O O   . ILE D 1 322 ? 51.932  -7.668  -5.332  1.00 61.00  ? 322 ILE D O   1 
ATOM   15328 C CB  . ILE D 1 322 ? 52.425  -4.851  -5.638  1.00 63.59  ? 322 ILE D CB  1 
ATOM   15329 C CG1 . ILE D 1 322 ? 51.990  -3.451  -6.069  1.00 63.74  ? 322 ILE D CG1 1 
ATOM   15330 C CG2 . ILE D 1 322 ? 53.818  -4.815  -5.013  1.00 65.10  ? 322 ILE D CG2 1 
ATOM   15331 C CD1 . ILE D 1 322 ? 51.519  -2.590  -4.916  1.00 63.04  ? 322 ILE D CD1 1 
ATOM   15332 N N   . ILE D 1 323 ? 53.473  -8.018  -6.968  1.00 63.41  ? 323 ILE D N   1 
ATOM   15333 C CA  . ILE D 1 323 ? 53.858  -9.339  -6.486  1.00 63.73  ? 323 ILE D CA  1 
ATOM   15334 C C   . ILE D 1 323 ? 55.010  -9.203  -5.488  1.00 64.21  ? 323 ILE D C   1 
ATOM   15335 O O   . ILE D 1 323 ? 55.122  -10.015 -4.569  1.00 63.20  ? 323 ILE D O   1 
ATOM   15336 C CB  . ILE D 1 323 ? 54.232  -10.298 -7.632  1.00 64.95  ? 323 ILE D CB  1 
ATOM   15337 C CG1 . ILE D 1 323 ? 53.061  -10.683 -8.511  1.00 64.59  ? 323 ILE D CG1 1 
ATOM   15338 C CG2 . ILE D 1 323 ? 54.901  -11.546 -7.075  1.00 66.19  ? 323 ILE D CG2 1 
ATOM   15339 C CD1 . ILE D 1 323 ? 52.688  -9.620  -9.524  1.00 65.83  ? 323 ILE D CD1 1 
ATOM   15340 N N   . SER D 1 324 ? 55.897  -8.216  -5.723  1.00 65.39  ? 324 SER D N   1 
ATOM   15341 C CA  . SER D 1 324 ? 57.054  -7.956  -4.876  1.00 65.79  ? 324 SER D CA  1 
ATOM   15342 C C   . SER D 1 324 ? 57.355  -6.454  -4.924  1.00 65.36  ? 324 SER D C   1 
ATOM   15343 O O   . SER D 1 324 ? 57.261  -5.858  -5.994  1.00 65.78  ? 324 SER D O   1 
ATOM   15344 C CB  . SER D 1 324 ? 58.279  -8.794  -5.293  1.00 67.43  ? 324 SER D CB  1 
ATOM   15345 O OG  . SER D 1 324 ? 58.061  -10.211 -5.209  1.00 67.79  ? 324 SER D OG  1 
ATOM   15346 N N   . PRO D 1 325 ? 57.737  -5.786  -3.807  1.00 64.02  ? 325 PRO D N   1 
ATOM   15347 C CA  . PRO D 1 325 ? 57.809  -6.381  -2.472  1.00 63.65  ? 325 PRO D CA  1 
ATOM   15348 C C   . PRO D 1 325 ? 56.470  -6.780  -1.879  1.00 62.26  ? 325 PRO D C   1 
ATOM   15349 O O   . PRO D 1 325 ? 55.461  -6.172  -2.199  1.00 61.31  ? 325 PRO D O   1 
ATOM   15350 C CB  . PRO D 1 325 ? 58.425  -5.281  -1.635  1.00 63.84  ? 325 PRO D CB  1 
ATOM   15351 C CG  . PRO D 1 325 ? 57.947  -4.070  -2.317  1.00 63.72  ? 325 PRO D CG  1 
ATOM   15352 C CD  . PRO D 1 325 ? 58.172  -4.395  -3.781  1.00 64.30  ? 325 PRO D CD  1 
ATOM   15353 N N   . LYS D 1 326 ? 56.514  -7.786  -1.003  1.00 61.99  ? 326 LYS D N   1 
ATOM   15354 C CA  . LYS D 1 326 ? 55.328  -8.322  -0.369  1.00 61.09  ? 326 LYS D CA  1 
ATOM   15355 C C   . LYS D 1 326 ? 55.059  -7.508  0.886   1.00 60.97  ? 326 LYS D C   1 
ATOM   15356 O O   . LYS D 1 326 ? 56.006  -7.115  1.555   1.00 60.91  ? 326 LYS D O   1 
ATOM   15357 C CB  . LYS D 1 326 ? 55.524  -9.822  -0.110  1.00 61.49  ? 326 LYS D CB  1 
ATOM   15358 C CG  . LYS D 1 326 ? 55.586  -10.631 -1.402  1.00 61.80  ? 326 LYS D CG  1 
ATOM   15359 C CD  . LYS D 1 326 ? 55.927  -12.092 -1.215  1.00 62.79  ? 326 LYS D CD  1 
ATOM   15360 C CE  . LYS D 1 326 ? 55.734  -12.948 -2.444  1.00 63.70  ? 326 LYS D CE  1 
ATOM   15361 N NZ  . LYS D 1 326 ? 56.260  -12.367 -3.685  1.00 64.90  ? 326 LYS D NZ  1 
ATOM   15362 N N   . ASN D 1 327 ? 53.763  -7.224  1.137   1.00 60.49  ? 327 ASN D N   1 
ATOM   15363 C CA  . ASN D 1 327 ? 53.324  -6.568  2.355   1.00 60.10  ? 327 ASN D CA  1 
ATOM   15364 C C   . ASN D 1 327 ? 53.654  -7.432  3.563   1.00 60.39  ? 327 ASN D C   1 
ATOM   15365 O O   . ASN D 1 327 ? 53.639  -8.663  3.518   1.00 60.28  ? 327 ASN D O   1 
ATOM   15366 C CB  . ASN D 1 327 ? 51.838  -6.268  2.356   1.00 59.54  ? 327 ASN D CB  1 
ATOM   15367 C CG  . ASN D 1 327 ? 51.439  -5.364  3.508   1.00 60.36  ? 327 ASN D CG  1 
ATOM   15368 O OD1 . ASN D 1 327 ? 51.960  -4.242  3.666   1.00 60.79  ? 327 ASN D OD1 1 
ATOM   15369 N ND2 . ASN D 1 327 ? 50.478  -5.810  4.308   1.00 59.93  ? 327 ASN D ND2 1 
ATOM   15370 N N   . LYS D 1 328 ? 54.017  -6.744  4.636   1.00 60.74  ? 328 LYS D N   1 
ATOM   15371 C CA  . LYS D 1 328 ? 54.513  -7.396  5.835   1.00 61.57  ? 328 LYS D CA  1 
ATOM   15372 C C   . LYS D 1 328 ? 55.787  -8.207  5.586   1.00 61.70  ? 328 LYS D C   1 
ATOM   15373 O O   . LYS D 1 328 ? 56.041  -9.112  6.371   1.00 62.27  ? 328 LYS D O   1 
ATOM   15374 C CB  . LYS D 1 328 ? 53.431  -8.263  6.486   1.00 60.94  ? 328 LYS D CB  1 
ATOM   15375 C CG  . LYS D 1 328 ? 52.214  -7.452  6.874   1.00 61.10  ? 328 LYS D CG  1 
ATOM   15376 C CD  . LYS D 1 328 ? 52.467  -6.151  7.640   1.00 62.10  ? 328 LYS D CD  1 
ATOM   15377 C CE  . LYS D 1 328 ? 51.244  -5.278  7.804   1.00 61.66  ? 328 LYS D CE  1 
ATOM   15378 N NZ  . LYS D 1 328 ? 50.230  -5.919  8.643   1.00 61.67  ? 328 LYS D NZ  1 
ATOM   15379 N N   . SER D 1 329 ? 56.603  -7.841  4.580   1.00 61.33  ? 329 SER D N   1 
ATOM   15380 C CA  . SER D 1 329 ? 57.873  -8.510  4.350   1.00 62.22  ? 329 SER D CA  1 
ATOM   15381 C C   . SER D 1 329 ? 58.990  -7.857  5.152   1.00 63.53  ? 329 SER D C   1 
ATOM   15382 O O   . SER D 1 329 ? 58.881  -6.725  5.611   1.00 64.10  ? 329 SER D O   1 
ATOM   15383 C CB  . SER D 1 329 ? 58.255  -8.621  2.889   1.00 62.17  ? 329 SER D CB  1 
ATOM   15384 O OG  . SER D 1 329 ? 58.639  -7.379  2.342   1.00 62.67  ? 329 SER D OG  1 
ATOM   15385 N N   . ILE D 1 330 ? 60.065  -8.623  5.309   1.00 64.60  ? 330 ILE D N   1 
ATOM   15386 C CA  . ILE D 1 330 ? 61.236  -8.197  6.042   1.00 66.12  ? 330 ILE D CA  1 
ATOM   15387 C C   . ILE D 1 330 ? 62.426  -8.222  5.088   1.00 66.90  ? 330 ILE D C   1 
ATOM   15388 O O   . ILE D 1 330 ? 62.592  -9.153  4.302   1.00 65.98  ? 330 ILE D O   1 
ATOM   15389 C CB  . ILE D 1 330 ? 61.388  -9.082  7.289   1.00 66.88  ? 330 ILE D CB  1 
ATOM   15390 C CG1 . ILE D 1 330 ? 60.188  -8.821  8.232   1.00 66.13  ? 330 ILE D CG1 1 
ATOM   15391 C CG2 . ILE D 1 330 ? 62.726  -8.858  7.977   1.00 68.67  ? 330 ILE D CG2 1 
ATOM   15392 C CD1 . ILE D 1 330 ? 60.356  -9.356  9.643   1.00 67.23  ? 330 ILE D CD1 1 
ATOM   15393 N N   . HIS D 1 331 ? 63.208  -7.135  5.131   1.00 68.01  ? 331 HIS D N   1 
ATOM   15394 C CA  . HIS D 1 331 ? 64.255  -6.904  4.160   1.00 69.17  ? 331 HIS D CA  1 
ATOM   15395 C C   . HIS D 1 331 ? 65.501  -6.433  4.895   1.00 71.95  ? 331 HIS D C   1 
ATOM   15396 O O   . HIS D 1 331 ? 65.434  -5.438  5.633   1.00 72.43  ? 331 HIS D O   1 
ATOM   15397 C CB  . HIS D 1 331 ? 63.794  -5.911  3.090   1.00 68.00  ? 331 HIS D CB  1 
ATOM   15398 C CG  . HIS D 1 331 ? 62.682  -6.394  2.226   1.00 66.49  ? 331 HIS D CG  1 
ATOM   15399 N ND1 . HIS D 1 331 ? 62.887  -7.027  1.021   1.00 66.90  ? 331 HIS D ND1 1 
ATOM   15400 C CD2 . HIS D 1 331 ? 61.363  -6.331  2.371   1.00 64.86  ? 331 HIS D CD2 1 
ATOM   15401 C CE1 . HIS D 1 331 ? 61.731  -7.339  0.459   1.00 65.30  ? 331 HIS D CE1 1 
ATOM   15402 N NE2 . HIS D 1 331 ? 60.795  -6.908  1.256   1.00 64.26  ? 331 HIS D NE2 1 
ATOM   15403 N N   . THR D 1 332 ? 66.631  -7.126  4.640   1.00 73.84  ? 332 THR D N   1 
ATOM   15404 C CA  . THR D 1 332 ? 67.873  -6.846  5.346   1.00 76.40  ? 332 THR D CA  1 
ATOM   15405 C C   . THR D 1 332 ? 68.904  -6.269  4.372   1.00 79.15  ? 332 THR D C   1 
ATOM   15406 O O   . THR D 1 332 ? 70.104  -6.222  4.672   1.00 80.05  ? 332 THR D O   1 
ATOM   15407 C CB  . THR D 1 332 ? 68.368  -8.117  6.029   1.00 76.96  ? 332 THR D CB  1 
ATOM   15408 O OG1 . THR D 1 332 ? 68.443  -9.006  4.925   1.00 76.73  ? 332 THR D OG1 1 
ATOM   15409 C CG2 . THR D 1 332 ? 67.408  -8.669  7.066   1.00 75.94  ? 332 THR D CG2 1 
ATOM   15410 N N   . ASN D 1 333 ? 68.407  -5.786  3.219   1.00 80.12  ? 333 ASN D N   1 
ATOM   15411 C CA  . ASN D 1 333 ? 69.266  -5.234  2.180   1.00 82.36  ? 333 ASN D CA  1 
ATOM   15412 C C   . ASN D 1 333 ? 68.569  -4.030  1.529   1.00 81.78  ? 333 ASN D C   1 
ATOM   15413 O O   . ASN D 1 333 ? 67.319  -3.952  1.435   1.00 80.06  ? 333 ASN D O   1 
ATOM   15414 C CB  . ASN D 1 333 ? 69.706  -6.367  1.258   1.00 84.42  ? 333 ASN D CB  1 
ATOM   15415 C CG  . ASN D 1 333 ? 70.612  -5.909  0.143   1.00 87.42  ? 333 ASN D CG  1 
ATOM   15416 O OD1 . ASN D 1 333 ? 70.116  -5.295  -0.810  1.00 87.76  ? 333 ASN D OD1 1 
ATOM   15417 N ND2 . ASN D 1 333 ? 71.909  -6.201  0.227   1.00 89.53  ? 333 ASN D ND2 1 
ATOM   15418 N N   . THR D 1 334 ? 69.406  -3.070  1.108   1.00 82.32  ? 334 THR D N   1 
ATOM   15419 C CA  . THR D 1 334 ? 68.924  -1.780  0.638   1.00 82.29  ? 334 THR D CA  1 
ATOM   15420 C C   . THR D 1 334 ? 68.372  -1.910  -0.782  1.00 82.93  ? 334 THR D C   1 
ATOM   15421 O O   . THR D 1 334 ? 67.775  -0.962  -1.296  1.00 83.33  ? 334 THR D O   1 
ATOM   15422 C CB  . THR D 1 334 ? 70.006  -0.702  0.707   1.00 83.64  ? 334 THR D CB  1 
ATOM   15423 O OG1 . THR D 1 334 ? 70.921  -0.884  -0.369  1.00 84.58  ? 334 THR D OG1 1 
ATOM   15424 C CG2 . THR D 1 334 ? 70.742  -0.669  2.037   1.00 84.54  ? 334 THR D CG2 1 
ATOM   15425 N N   . LYS D 1 335 ? 68.581  -3.072  -1.416  1.00 83.70  ? 335 LYS D N   1 
ATOM   15426 C CA  . LYS D 1 335 ? 67.969  -3.348  -2.705  1.00 83.23  ? 335 LYS D CA  1 
ATOM   15427 C C   . LYS D 1 335 ? 66.802  -4.289  -2.486  1.00 80.51  ? 335 LYS D C   1 
ATOM   15428 O O   . LYS D 1 335 ? 66.943  -5.313  -1.819  1.00 80.67  ? 335 LYS D O   1 
ATOM   15429 C CB  . LYS D 1 335 ? 68.875  -3.998  -3.756  1.00 85.54  ? 335 LYS D CB  1 
ATOM   15430 C CG  . LYS D 1 335 ? 70.123  -3.203  -4.098  1.00 88.39  ? 335 LYS D CG  1 
ATOM   15431 C CD  . LYS D 1 335 ? 69.974  -1.899  -4.873  1.00 89.29  ? 335 LYS D CD  1 
ATOM   15432 C CE  . LYS D 1 335 ? 71.260  -1.140  -4.652  1.00 93.04  ? 335 LYS D CE  1 
ATOM   15433 N NZ  . LYS D 1 335 ? 71.433  0.103   -5.405  1.00 94.65  ? 335 LYS D NZ  1 
ATOM   15434 N N   . ILE D 1 336 ? 65.681  -3.908  -3.103  1.00 79.39  ? 336 ILE D N   1 
ATOM   15435 C CA  . ILE D 1 336 ? 64.397  -4.566  -2.945  1.00 76.93  ? 336 ILE D CA  1 
ATOM   15436 C C   . ILE D 1 336 ? 63.956  -5.044  -4.322  1.00 77.18  ? 336 ILE D C   1 
ATOM   15437 O O   . ILE D 1 336 ? 63.762  -4.217  -5.209  1.00 78.12  ? 336 ILE D O   1 
ATOM   15438 C CB  . ILE D 1 336 ? 63.367  -3.585  -2.373  1.00 75.07  ? 336 ILE D CB  1 
ATOM   15439 C CG1 . ILE D 1 336 ? 63.812  -2.965  -1.059  1.00 74.84  ? 336 ILE D CG1 1 
ATOM   15440 C CG2 . ILE D 1 336 ? 61.999  -4.264  -2.251  1.00 74.27  ? 336 ILE D CG2 1 
ATOM   15441 C CD1 . ILE D 1 336 ? 63.701  -3.894  0.131   1.00 74.52  ? 336 ILE D CD1 1 
ATOM   15442 N N   . PRO D 1 337 ? 63.811  -6.368  -4.566  1.00 76.99  ? 337 PRO D N   1 
ATOM   15443 C CA  . PRO D 1 337 ? 63.279  -6.857  -5.838  1.00 76.30  ? 337 PRO D CA  1 
ATOM   15444 C C   . PRO D 1 337 ? 61.874  -6.302  -6.030  1.00 74.05  ? 337 PRO D C   1 
ATOM   15445 O O   . PRO D 1 337 ? 61.107  -6.233  -5.072  1.00 73.29  ? 337 PRO D O   1 
ATOM   15446 C CB  . PRO D 1 337 ? 63.301  -8.403  -5.720  1.00 76.71  ? 337 PRO D CB  1 
ATOM   15447 C CG  . PRO D 1 337 ? 64.232  -8.688  -4.553  1.00 77.39  ? 337 PRO D CG  1 
ATOM   15448 C CD  . PRO D 1 337 ? 64.200  -7.458  -3.657  1.00 77.42  ? 337 PRO D CD  1 
ATOM   15449 N N   . LEU D 1 338 ? 61.574  -5.882  -7.264  1.00 73.65  ? 338 LEU D N   1 
ATOM   15450 C CA  . LEU D 1 338 ? 60.279  -5.320  -7.613  1.00 72.00  ? 338 LEU D CA  1 
ATOM   15451 C C   . LEU D 1 338 ? 59.728  -6.146  -8.765  1.00 71.80  ? 338 LEU D C   1 
ATOM   15452 O O   . LEU D 1 338 ? 60.338  -6.171  -9.828  1.00 73.43  ? 338 LEU D O   1 
ATOM   15453 C CB  . LEU D 1 338 ? 60.390  -3.854  -8.037  1.00 72.94  ? 338 LEU D CB  1 
ATOM   15454 C CG  . LEU D 1 338 ? 59.110  -3.202  -8.602  1.00 72.68  ? 338 LEU D CG  1 
ATOM   15455 C CD1 . LEU D 1 338 ? 58.169  -2.697  -7.499  1.00 71.12  ? 338 LEU D CD1 1 
ATOM   15456 C CD2 . LEU D 1 338 ? 59.383  -2.066  -9.600  1.00 73.45  ? 338 LEU D CD2 1 
ATOM   15457 N N   . GLU D 1 339 ? 58.584  -6.803  -8.539  1.00 70.26  ? 339 GLU D N   1 
ATOM   15458 C CA  . GLU D 1 339 ? 57.873  -7.517  -9.580  1.00 69.74  ? 339 GLU D CA  1 
ATOM   15459 C C   . GLU D 1 339 ? 56.435  -6.999  -9.638  1.00 68.92  ? 339 GLU D C   1 
ATOM   15460 O O   . GLU D 1 339 ? 55.791  -6.884  -8.594  1.00 67.22  ? 339 GLU D O   1 
ATOM   15461 C CB  . GLU D 1 339 ? 57.870  -9.004  -9.233  1.00 69.73  ? 339 GLU D CB  1 
ATOM   15462 C CG  . GLU D 1 339 ? 59.203  -9.568  -8.733  1.00 70.41  ? 339 GLU D CG  1 
ATOM   15463 C CD  . GLU D 1 339 ? 59.069  -11.056 -8.471  1.00 69.38  ? 339 GLU D CD  1 
ATOM   15464 O OE1 . GLU D 1 339 ? 58.995  -11.482 -7.290  1.00 68.30  ? 339 GLU D OE1 1 
ATOM   15465 O OE2 . GLU D 1 339 ? 58.975  -11.767 -9.489  1.00 69.39  ? 339 GLU D OE2 1 
ATOM   15466 N N   . LEU D 1 340 ? 55.945  -6.718  -10.860 1.00 69.70  ? 340 LEU D N   1 
ATOM   15467 C CA  . LEU D 1 340 ? 54.620  -6.149  -11.080 1.00 69.52  ? 340 LEU D CA  1 
ATOM   15468 C C   . LEU D 1 340 ? 53.939  -6.818  -12.278 1.00 69.55  ? 340 LEU D C   1 
ATOM   15469 O O   . LEU D 1 340 ? 54.604  -7.205  -13.243 1.00 70.07  ? 340 LEU D O   1 
ATOM   15470 C CB  . LEU D 1 340 ? 54.718  -4.640  -11.333 1.00 70.32  ? 340 LEU D CB  1 
ATOM   15471 C CG  . LEU D 1 340 ? 55.134  -3.732  -10.171 1.00 70.44  ? 340 LEU D CG  1 
ATOM   15472 C CD1 . LEU D 1 340 ? 55.164  -2.265  -10.594 1.00 71.15  ? 340 LEU D CD1 1 
ATOM   15473 C CD2 . LEU D 1 340 ? 54.226  -3.869  -8.971  1.00 69.10  ? 340 LEU D CD2 1 
ATOM   15474 N N   . TYR D 1 341 ? 52.601  -6.899  -12.223 1.00 69.05  ? 341 TYR D N   1 
ATOM   15475 C CA  . TYR D 1 341 ? 51.784  -7.327  -13.354 1.00 69.85  ? 341 TYR D CA  1 
ATOM   15476 C C   . TYR D 1 341 ? 50.797  -6.211  -13.721 1.00 71.11  ? 341 TYR D C   1 
ATOM   15477 O O   . TYR D 1 341 ? 49.910  -5.853  -12.936 1.00 71.80  ? 341 TYR D O   1 
ATOM   15478 C CB  . TYR D 1 341 ? 51.054  -8.643  -13.067 1.00 68.19  ? 341 TYR D CB  1 
ATOM   15479 C CG  . TYR D 1 341 ? 50.700  -9.360  -14.360 1.00 69.35  ? 341 TYR D CG  1 
ATOM   15480 C CD1 . TYR D 1 341 ? 51.658  -10.091 -15.052 1.00 71.30  ? 341 TYR D CD1 1 
ATOM   15481 C CD2 . TYR D 1 341 ? 49.431  -9.278  -14.918 1.00 68.88  ? 341 TYR D CD2 1 
ATOM   15482 C CE1 . TYR D 1 341 ? 51.355  -10.725 -16.248 1.00 72.71  ? 341 TYR D CE1 1 
ATOM   15483 C CE2 . TYR D 1 341 ? 49.112  -9.914  -16.107 1.00 69.75  ? 341 TYR D CE2 1 
ATOM   15484 C CZ  . TYR D 1 341 ? 50.075  -10.645 -16.776 1.00 71.68  ? 341 TYR D CZ  1 
ATOM   15485 O OH  . TYR D 1 341 ? 49.815  -11.275 -17.963 1.00 72.44  ? 341 TYR D OH  1 
ATOM   15486 N N   . ASN D 1 342 ? 50.942  -5.667  -14.932 1.00 71.73  ? 342 ASN D N   1 
ATOM   15487 C CA  . ASN D 1 342 ? 50.217  -4.472  -15.310 1.00 72.38  ? 342 ASN D CA  1 
ATOM   15488 C C   . ASN D 1 342 ? 49.318  -4.777  -16.493 1.00 74.01  ? 342 ASN D C   1 
ATOM   15489 O O   . ASN D 1 342 ? 49.803  -5.295  -17.493 1.00 74.77  ? 342 ASN D O   1 
ATOM   15490 C CB  . ASN D 1 342 ? 51.152  -3.347  -15.738 1.00 74.32  ? 342 ASN D CB  1 
ATOM   15491 C CG  . ASN D 1 342 ? 52.048  -2.887  -14.618 1.00 74.25  ? 342 ASN D CG  1 
ATOM   15492 O OD1 . ASN D 1 342 ? 53.278  -2.842  -14.764 1.00 74.69  ? 342 ASN D OD1 1 
ATOM   15493 N ND2 . ASN D 1 342 ? 51.435  -2.553  -13.494 1.00 73.77  ? 342 ASN D ND2 1 
ATOM   15494 N N   . ASP D 1 343 ? 48.031  -4.408  -16.387 1.00 75.08  ? 343 ASP D N   1 
ATOM   15495 C CA  . ASP D 1 343 ? 47.150  -4.423  -17.546 1.00 76.43  ? 343 ASP D CA  1 
ATOM   15496 C C   . ASP D 1 343 ? 47.527  -3.249  -18.440 1.00 77.46  ? 343 ASP D C   1 
ATOM   15497 O O   . ASP D 1 343 ? 48.264  -2.361  -18.034 1.00 76.85  ? 343 ASP D O   1 
ATOM   15498 C CB  . ASP D 1 343 ? 45.663  -4.472  -17.204 1.00 75.91  ? 343 ASP D CB  1 
ATOM   15499 C CG  . ASP D 1 343 ? 44.961  -3.155  -16.889 1.00 75.38  ? 343 ASP D CG  1 
ATOM   15500 O OD1 . ASP D 1 343 ? 45.133  -2.188  -17.665 1.00 78.24  ? 343 ASP D OD1 1 
ATOM   15501 O OD2 . ASP D 1 343 ? 44.220  -3.114  -15.887 1.00 71.39  ? 343 ASP D OD2 1 
ATOM   15502 N N   . LYS D 1 344 ? 46.958  -3.241  -19.642 1.00 79.33  ? 344 LYS D N   1 
ATOM   15503 C CA  . LYS D 1 344 ? 47.458  -2.412  -20.720 1.00 82.09  ? 344 LYS D CA  1 
ATOM   15504 C C   . LYS D 1 344 ? 47.249  -0.919  -20.448 1.00 80.95  ? 344 LYS D C   1 
ATOM   15505 O O   . LYS D 1 344 ? 47.792  -0.088  -21.184 1.00 82.30  ? 344 LYS D O   1 
ATOM   15506 C CB  . LYS D 1 344 ? 46.802  -2.878  -22.024 1.00 85.76  ? 344 LYS D CB  1 
ATOM   15507 C CG  . LYS D 1 344 ? 45.294  -2.670  -22.150 1.00 88.33  ? 344 LYS D CG  1 
ATOM   15508 C CD  . LYS D 1 344 ? 44.759  -2.797  -23.575 1.00 92.33  ? 344 LYS D CD  1 
ATOM   15509 C CE  . LYS D 1 344 ? 45.419  -1.806  -24.507 1.00 95.99  ? 344 LYS D CE  1 
ATOM   15510 N NZ  . LYS D 1 344 ? 44.810  -1.698  -25.837 1.00 99.02  ? 344 LYS D NZ  1 
ATOM   15511 N N   . ASP D 1 345 ? 46.506  -0.579  -19.386 1.00 78.20  ? 345 ASP D N   1 
ATOM   15512 C CA  . ASP D 1 345 ? 46.157  0.806   -19.107 1.00 78.08  ? 345 ASP D CA  1 
ATOM   15513 C C   . ASP D 1 345 ? 47.159  1.496   -18.186 1.00 77.33  ? 345 ASP D C   1 
ATOM   15514 O O   . ASP D 1 345 ? 47.049  2.707   -17.986 1.00 77.74  ? 345 ASP D O   1 
ATOM   15515 C CB  . ASP D 1 345 ? 44.785  0.909   -18.468 1.00 76.60  ? 345 ASP D CB  1 
ATOM   15516 C CG  . ASP D 1 345 ? 43.643  0.629   -19.423 1.00 76.31  ? 345 ASP D CG  1 
ATOM   15517 O OD1 . ASP D 1 345 ? 43.955  0.366   -20.607 1.00 77.72  ? 345 ASP D OD1 1 
ATOM   15518 O OD2 . ASP D 1 345 ? 42.478  0.694   -18.966 1.00 73.66  ? 345 ASP D OD2 1 
ATOM   15519 N N   . VAL D 1 346 ? 48.078  0.721   -17.593 1.00 75.77  ? 346 VAL D N   1 
ATOM   15520 C CA  . VAL D 1 346 ? 49.116  1.271   -16.738 1.00 75.23  ? 346 VAL D CA  1 
ATOM   15521 C C   . VAL D 1 346 ? 50.212  1.776   -17.658 1.00 77.07  ? 346 VAL D C   1 
ATOM   15522 O O   . VAL D 1 346 ? 50.742  0.997   -18.430 1.00 78.10  ? 346 VAL D O   1 
ATOM   15523 C CB  . VAL D 1 346 ? 49.666  0.269   -15.707 1.00 73.71  ? 346 VAL D CB  1 
ATOM   15524 C CG1 . VAL D 1 346 ? 50.826  0.827   -14.911 1.00 73.63  ? 346 VAL D CG1 1 
ATOM   15525 C CG2 . VAL D 1 346 ? 48.586  -0.161  -14.731 1.00 73.25  ? 346 VAL D CG2 1 
ATOM   15526 N N   . LYS D 1 347 ? 50.491  3.084   -17.594 1.00 79.29  ? 347 LYS D N   1 
ATOM   15527 C CA  . LYS D 1 347 ? 51.500  3.711   -18.435 1.00 81.57  ? 347 LYS D CA  1 
ATOM   15528 C C   . LYS D 1 347 ? 52.683  4.212   -17.602 1.00 81.60  ? 347 LYS D C   1 
ATOM   15529 O O   . LYS D 1 347 ? 53.751  4.476   -18.160 1.00 83.85  ? 347 LYS D O   1 
ATOM   15530 C CB  . LYS D 1 347 ? 50.879  4.815   -19.301 1.00 82.80  ? 347 LYS D CB  1 
ATOM   15531 C CG  . LYS D 1 347 ? 49.902  4.335   -20.370 1.00 84.48  ? 347 LYS D CG  1 
ATOM   15532 C CD  . LYS D 1 347 ? 50.431  3.212   -21.257 1.00 86.14  ? 347 LYS D CD  1 
ATOM   15533 C CE  . LYS D 1 347 ? 49.524  2.777   -22.367 1.00 87.60  ? 347 LYS D CE  1 
ATOM   15534 N NZ  . LYS D 1 347 ? 50.234  1.802   -23.204 1.00 89.61  ? 347 LYS D NZ  1 
ATOM   15535 N N   . LYS D 1 348 ? 52.510  4.326   -16.278 1.00 80.06  ? 348 LYS D N   1 
ATOM   15536 C CA  . LYS D 1 348 ? 53.607  4.695   -15.391 1.00 80.30  ? 348 LYS D CA  1 
ATOM   15537 C C   . LYS D 1 348 ? 53.321  4.166   -13.986 1.00 78.99  ? 348 LYS D C   1 
ATOM   15538 O O   . LYS D 1 348 ? 52.164  4.055   -13.589 1.00 78.79  ? 348 LYS D O   1 
ATOM   15539 C CB  . LYS D 1 348 ? 53.831  6.215   -15.388 1.00 80.71  ? 348 LYS D CB  1 
ATOM   15540 C CG  . LYS D 1 348 ? 54.832  6.768   -14.379 1.00 80.81  ? 348 LYS D CG  1 
ATOM   15541 C CD  . LYS D 1 348 ? 55.266  8.211   -14.656 1.00 83.17  ? 348 LYS D CD  1 
ATOM   15542 C CE  . LYS D 1 348 ? 54.211  9.228   -14.351 1.00 82.65  ? 348 LYS D CE  1 
ATOM   15543 N NZ  . LYS D 1 348 ? 54.657  10.621  -14.383 1.00 83.88  ? 348 LYS D NZ  1 
ATOM   15544 N N   . VAL D 1 349 ? 54.390  3.856   -13.247 1.00 78.88  ? 349 VAL D N   1 
ATOM   15545 C CA  . VAL D 1 349 ? 54.297  3.430   -11.862 1.00 77.48  ? 349 VAL D CA  1 
ATOM   15546 C C   . VAL D 1 349 ? 55.342  4.192   -11.062 1.00 78.78  ? 349 VAL D C   1 
ATOM   15547 O O   . VAL D 1 349 ? 56.482  4.340   -11.500 1.00 83.45  ? 349 VAL D O   1 
ATOM   15548 C CB  . VAL D 1 349 ? 54.521  1.915   -11.709 1.00 76.81  ? 349 VAL D CB  1 
ATOM   15549 C CG1 . VAL D 1 349 ? 54.543  1.480   -10.243 1.00 75.38  ? 349 VAL D CG1 1 
ATOM   15550 C CG2 . VAL D 1 349 ? 53.498  1.116   -12.504 1.00 75.97  ? 349 VAL D CG2 1 
ATOM   15551 N N   . VAL D 1 350 ? 54.949  4.638   -9.871  1.00 76.33  ? 350 VAL D N   1 
ATOM   15552 C CA  . VAL D 1 350 ? 55.809  5.450   -9.030  1.00 75.74  ? 350 VAL D CA  1 
ATOM   15553 C C   . VAL D 1 350 ? 55.692  4.900   -7.618  1.00 74.58  ? 350 VAL D C   1 
ATOM   15554 O O   . VAL D 1 350 ? 54.638  4.423   -7.218  1.00 74.12  ? 350 VAL D O   1 
ATOM   15555 C CB  . VAL D 1 350 ? 55.369  6.926   -9.094  1.00 75.70  ? 350 VAL D CB  1 
ATOM   15556 C CG1 . VAL D 1 350 ? 56.101  7.810   -8.089  1.00 75.81  ? 350 VAL D CG1 1 
ATOM   15557 C CG2 . VAL D 1 350 ? 55.453  7.484   -10.509 1.00 76.80  ? 350 VAL D CG2 1 
ATOM   15558 N N   . VAL D 1 351 ? 56.782  4.973   -6.871  1.00 75.52  ? 351 VAL D N   1 
ATOM   15559 C CA  . VAL D 1 351 ? 56.803  4.522   -5.491  1.00 75.49  ? 351 VAL D CA  1 
ATOM   15560 C C   . VAL D 1 351 ? 57.318  5.703   -4.690  1.00 76.81  ? 351 VAL D C   1 
ATOM   15561 O O   . VAL D 1 351 ? 58.359  6.258   -5.045  1.00 79.99  ? 351 VAL D O   1 
ATOM   15562 C CB  . VAL D 1 351 ? 57.719  3.295   -5.294  1.00 75.74  ? 351 VAL D CB  1 
ATOM   15563 C CG1 . VAL D 1 351 ? 57.892  2.910   -3.828  1.00 74.81  ? 351 VAL D CG1 1 
ATOM   15564 C CG2 . VAL D 1 351 ? 57.232  2.112   -6.113  1.00 75.37  ? 351 VAL D CG2 1 
ATOM   15565 N N   . LYS D 1 352 ? 56.610  6.058   -3.618  1.00 75.05  ? 352 LYS D N   1 
ATOM   15566 C CA  . LYS D 1 352 ? 57.026  7.175   -2.792  1.00 75.37  ? 352 LYS D CA  1 
ATOM   15567 C C   . LYS D 1 352 ? 57.300  6.677   -1.380  1.00 73.61  ? 352 LYS D C   1 
ATOM   15568 O O   . LYS D 1 352 ? 56.753  5.658   -0.966  1.00 72.58  ? 352 LYS D O   1 
ATOM   15569 C CB  . LYS D 1 352 ? 55.959  8.261   -2.869  1.00 76.62  ? 352 LYS D CB  1 
ATOM   15570 C CG  . LYS D 1 352 ? 55.907  8.882   -4.250  1.00 79.66  ? 352 LYS D CG  1 
ATOM   15571 C CD  . LYS D 1 352 ? 54.763  9.883   -4.393  1.00 82.07  ? 352 LYS D CD  1 
ATOM   15572 C CE  . LYS D 1 352 ? 54.682  10.524  -5.751  1.00 84.64  ? 352 LYS D CE  1 
ATOM   15573 N NZ  . LYS D 1 352 ? 53.649  11.559  -5.821  1.00 84.83  ? 352 LYS D NZ  1 
ATOM   15574 N N   . PHE D 1 353 ? 58.187  7.389   -0.673  1.00 73.00  ? 353 PHE D N   1 
ATOM   15575 C CA  . PHE D 1 353 ? 58.414  7.135   0.739   1.00 72.11  ? 353 PHE D CA  1 
ATOM   15576 C C   . PHE D 1 353 ? 58.506  8.495   1.418   1.00 72.46  ? 353 PHE D C   1 
ATOM   15577 O O   . PHE D 1 353 ? 59.183  9.379   0.919   1.00 74.75  ? 353 PHE D O   1 
ATOM   15578 C CB  . PHE D 1 353 ? 59.630  6.246   1.055   1.00 72.65  ? 353 PHE D CB  1 
ATOM   15579 C CG  . PHE D 1 353 ? 59.762  6.013   2.553   1.00 71.91  ? 353 PHE D CG  1 
ATOM   15580 C CD1 . PHE D 1 353 ? 58.827  5.253   3.241   1.00 70.65  ? 353 PHE D CD1 1 
ATOM   15581 C CD2 . PHE D 1 353 ? 60.759  6.624   3.284   1.00 72.98  ? 353 PHE D CD2 1 
ATOM   15582 C CE1 . PHE D 1 353 ? 58.916  5.092   4.615   1.00 70.89  ? 353 PHE D CE1 1 
ATOM   15583 C CE2 . PHE D 1 353 ? 60.835  6.466   4.657   1.00 73.31  ? 353 PHE D CE2 1 
ATOM   15584 C CZ  . PHE D 1 353 ? 59.926  5.689   5.318   1.00 72.04  ? 353 PHE D CZ  1 
ATOM   15585 N N   . ARG D 1 354 ? 57.788  8.642   2.535   1.00 71.91  ? 354 ARG D N   1 
ATOM   15586 C CA  . ARG D 1 354 ? 57.605  9.906   3.227   1.00 72.98  ? 354 ARG D CA  1 
ATOM   15587 C C   . ARG D 1 354 ? 57.443  11.049  2.223   1.00 73.95  ? 354 ARG D C   1 
ATOM   15588 O O   . ARG D 1 354 ? 58.024  12.094  2.378   1.00 78.05  ? 354 ARG D O   1 
ATOM   15589 C CB  . ARG D 1 354 ? 58.746  9.975   4.239   1.00 74.87  ? 354 ARG D CB  1 
ATOM   15590 C CG  . ARG D 1 354 ? 58.574  9.071   5.450   1.00 75.17  ? 354 ARG D CG  1 
ATOM   15591 C CD  . ARG D 1 354 ? 59.740  9.247   6.411   1.00 77.64  ? 354 ARG D CD  1 
ATOM   15592 N NE  . ARG D 1 354 ? 59.749  8.320   7.545   1.00 78.20  ? 354 ARG D NE  1 
ATOM   15593 C CZ  . ARG D 1 354 ? 60.830  7.750   8.037   1.00 80.27  ? 354 ARG D CZ  1 
ATOM   15594 N NH1 . ARG D 1 354 ? 61.980  7.953   7.456   1.00 83.19  ? 354 ARG D NH1 1 
ATOM   15595 N NH2 . ARG D 1 354 ? 60.782  6.959   9.097   1.00 80.84  ? 354 ARG D NH2 1 
ATOM   15596 N N   . ASP D 1 355 ? 56.652  10.839  1.173   1.00 73.19  ? 355 ASP D N   1 
ATOM   15597 C CA  . ASP D 1 355 ? 56.237  11.861  0.232   1.00 73.16  ? 355 ASP D CA  1 
ATOM   15598 C C   . ASP D 1 355 ? 57.285  12.188  -0.812  1.00 74.53  ? 355 ASP D C   1 
ATOM   15599 O O   . ASP D 1 355 ? 57.037  13.112  -1.565  1.00 75.63  ? 355 ASP D O   1 
ATOM   15600 C CB  . ASP D 1 355 ? 55.699  13.087  0.934   1.00 74.37  ? 355 ASP D CB  1 
ATOM   15601 C CG  . ASP D 1 355 ? 54.515  12.710  1.798   1.00 75.00  ? 355 ASP D CG  1 
ATOM   15602 O OD1 . ASP D 1 355 ? 53.386  12.506  1.249   1.00 72.80  ? 355 ASP D OD1 1 
ATOM   15603 O OD2 . ASP D 1 355 ? 54.775  12.475  2.988   1.00 79.52  ? 355 ASP D OD2 1 
ATOM   15604 N N   . LYS D 1 356 ? 58.397  11.443  -0.886  1.00 75.34  ? 356 LYS D N   1 
ATOM   15605 C CA  . LYS D 1 356 ? 59.386  11.634  -1.938  1.00 76.85  ? 356 LYS D CA  1 
ATOM   15606 C C   . LYS D 1 356 ? 59.432  10.409  -2.859  1.00 76.66  ? 356 LYS D C   1 
ATOM   15607 O O   . LYS D 1 356 ? 59.328  9.262   -2.407  1.00 74.96  ? 356 LYS D O   1 
ATOM   15608 C CB  . LYS D 1 356 ? 60.745  11.835  -1.276  1.00 78.92  ? 356 LYS D CB  1 
ATOM   15609 C CG  . LYS D 1 356 ? 61.861  12.186  -2.248  1.00 81.65  ? 356 LYS D CG  1 
ATOM   15610 C CD  . LYS D 1 356 ? 63.213  11.543  -1.968  1.00 83.27  ? 356 LYS D CD  1 
ATOM   15611 C CE  . LYS D 1 356 ? 64.388  12.456  -2.056  1.00 85.64  ? 356 LYS D CE  1 
ATOM   15612 N NZ  . LYS D 1 356 ? 64.812  12.860  -0.712  1.00 87.17  ? 356 LYS D NZ  1 
ATOM   15613 N N   . VAL D 1 357 ? 59.621  10.655  -4.162  1.00 77.90  ? 357 VAL D N   1 
ATOM   15614 C CA  . VAL D 1 357 ? 59.791  9.585   -5.138  1.00 79.10  ? 357 VAL D CA  1 
ATOM   15615 C C   . VAL D 1 357 ? 61.082  8.806   -4.855  1.00 80.97  ? 357 VAL D C   1 
ATOM   15616 O O   . VAL D 1 357 ? 62.107  9.400   -4.533  1.00 82.76  ? 357 VAL D O   1 
ATOM   15617 C CB  . VAL D 1 357 ? 59.829  10.115  -6.587  1.00 80.45  ? 357 VAL D CB  1 
ATOM   15618 C CG1 . VAL D 1 357 ? 60.081  8.978   -7.580  1.00 81.12  ? 357 VAL D CG1 1 
ATOM   15619 C CG2 . VAL D 1 357 ? 58.589  10.904  -6.982  1.00 79.09  ? 357 VAL D CG2 1 
ATOM   15620 N N   . ILE D 1 358 ? 61.031  7.478   -5.012  1.00 81.36  ? 358 ILE D N   1 
ATOM   15621 C CA  . ILE D 1 358 ? 62.211  6.622   -4.933  1.00 83.23  ? 358 ILE D CA  1 
ATOM   15622 C C   . ILE D 1 358 ? 62.282  5.694   -6.149  1.00 83.75  ? 358 ILE D C   1 
ATOM   15623 O O   . ILE D 1 358 ? 63.324  5.096   -6.416  1.00 87.04  ? 358 ILE D O   1 
ATOM   15624 C CB  . ILE D 1 358 ? 62.213  5.791   -3.637  1.00 82.87  ? 358 ILE D CB  1 
ATOM   15625 C CG1 . ILE D 1 358 ? 61.131  4.740   -3.649  1.00 82.60  ? 358 ILE D CG1 1 
ATOM   15626 C CG2 . ILE D 1 358 ? 62.086  6.687   -2.411  1.00 83.32  ? 358 ILE D CG2 1 
ATOM   15627 C CD1 . ILE D 1 358 ? 61.147  3.830   -2.435  1.00 83.58  ? 358 ILE D CD1 1 
ATOM   15628 N N   . TYR D 1 359 ? 61.161  5.529   -6.859  1.00 82.39  ? 359 TYR D N   1 
ATOM   15629 C CA  . TYR D 1 359 ? 61.140  4.787   -8.106  1.00 81.89  ? 359 TYR D CA  1 
ATOM   15630 C C   . TYR D 1 359 ? 60.108  5.403   -9.046  1.00 81.45  ? 359 TYR D C   1 
ATOM   15631 O O   . TYR D 1 359 ? 59.010  5.757   -8.606  1.00 80.52  ? 359 TYR D O   1 
ATOM   15632 C CB  . TYR D 1 359 ? 60.796  3.340   -7.753  1.00 80.98  ? 359 TYR D CB  1 
ATOM   15633 C CG  . TYR D 1 359 ? 60.773  2.422   -8.960  1.00 81.17  ? 359 TYR D CG  1 
ATOM   15634 C CD1 . TYR D 1 359 ? 59.616  2.263   -9.716  1.00 81.09  ? 359 TYR D CD1 1 
ATOM   15635 C CD2 . TYR D 1 359 ? 61.905  1.724   -9.343  1.00 81.09  ? 359 TYR D CD2 1 
ATOM   15636 C CE1 . TYR D 1 359 ? 59.588  1.424   -10.819 1.00 81.68  ? 359 TYR D CE1 1 
ATOM   15637 C CE2 . TYR D 1 359 ? 61.888  0.888   -10.446 1.00 82.23  ? 359 TYR D CE2 1 
ATOM   15638 C CZ  . TYR D 1 359 ? 60.728  0.732   -11.184 1.00 81.73  ? 359 TYR D CZ  1 
ATOM   15639 O OH  . TYR D 1 359 ? 60.696  -0.089  -12.274 1.00 80.92  ? 359 TYR D OH  1 
ATOM   15640 N N   . SER D 1 360 ? 60.468  5.535   -10.331 1.00 81.99  ? 360 SER D N   1 
ATOM   15641 C CA  . SER D 1 360 ? 59.530  6.006   -11.346 1.00 81.59  ? 360 SER D CA  1 
ATOM   15642 C C   . SER D 1 360 ? 59.892  5.439   -12.714 1.00 82.60  ? 360 SER D C   1 
ATOM   15643 O O   . SER D 1 360 ? 60.850  5.912   -13.351 1.00 83.46  ? 360 SER D O   1 
ATOM   15644 C CB  . SER D 1 360 ? 59.456  7.512   -11.422 1.00 81.81  ? 360 SER D CB  1 
ATOM   15645 O OG  . SER D 1 360 ? 58.842  7.928   -12.638 1.00 81.78  ? 360 SER D OG  1 
ATOM   15646 N N   . LYS D 1 361 ? 59.090  4.452   -13.153 1.00 80.46  ? 361 LYS D N   1 
ATOM   15647 C CA  . LYS D 1 361 ? 59.260  3.855   -14.467 1.00 81.46  ? 361 LYS D CA  1 
ATOM   15648 C C   . LYS D 1 361 ? 58.043  4.184   -15.317 1.00 80.31  ? 361 LYS D C   1 
ATOM   15649 O O   . LYS D 1 361 ? 56.941  4.237   -14.803 1.00 79.83  ? 361 LYS D O   1 
ATOM   15650 C CB  . LYS D 1 361 ? 59.451  2.336   -14.429 1.00 81.42  ? 361 LYS D CB  1 
ATOM   15651 C CG  . LYS D 1 361 ? 59.735  1.703   -15.795 1.00 83.57  ? 361 LYS D CG  1 
ATOM   15652 C CD  . LYS D 1 361 ? 59.914  0.183   -15.785 1.00 83.81  ? 361 LYS D CD  1 
ATOM   15653 C CE  . LYS D 1 361 ? 60.290  -0.446  -17.114 1.00 84.82  ? 361 LYS D CE  1 
ATOM   15654 N NZ  . LYS D 1 361 ? 61.712  -0.308  -17.434 1.00 86.40  ? 361 LYS D NZ  1 
ATOM   15655 N N   . ASN D 1 362 ? 58.283  4.413   -16.606 1.00 81.62  ? 362 ASN D N   1 
ATOM   15656 C CA  . ASN D 1 362 ? 57.257  4.534   -17.617 1.00 82.29  ? 362 ASN D CA  1 
ATOM   15657 C C   . ASN D 1 362 ? 57.109  3.175   -18.275 1.00 82.64  ? 362 ASN D C   1 
ATOM   15658 O O   . ASN D 1 362 ? 58.077  2.694   -18.835 1.00 83.38  ? 362 ASN D O   1 
ATOM   15659 C CB  . ASN D 1 362 ? 57.645  5.523   -18.707 1.00 85.12  ? 362 ASN D CB  1 
ATOM   15660 C CG  . ASN D 1 362 ? 57.569  6.955   -18.250 1.00 85.99  ? 362 ASN D CG  1 
ATOM   15661 O OD1 . ASN D 1 362 ? 58.305  7.389   -17.358 1.00 86.14  ? 362 ASN D OD1 1 
ATOM   15662 N ND2 . ASN D 1 362 ? 56.685  7.711   -18.872 1.00 87.97  ? 362 ASN D ND2 1 
ATOM   15663 N N   . ILE D 1 363 ? 55.902  2.597   -18.222 1.00 82.02  ? 363 ILE D N   1 
ATOM   15664 C CA  . ILE D 1 363 ? 55.665  1.224   -18.627 1.00 82.09  ? 363 ILE D CA  1 
ATOM   15665 C C   . ILE D 1 363 ? 55.362  1.181   -20.119 1.00 85.42  ? 363 ILE D C   1 
ATOM   15666 O O   . ILE D 1 363 ? 54.283  1.598   -20.533 1.00 86.45  ? 363 ILE D O   1 
ATOM   15667 C CB  . ILE D 1 363 ? 54.484  0.635   -17.840 1.00 79.64  ? 363 ILE D CB  1 
ATOM   15668 C CG1 . ILE D 1 363 ? 54.656  0.782   -16.329 1.00 78.40  ? 363 ILE D CG1 1 
ATOM   15669 C CG2 . ILE D 1 363 ? 54.232  -0.816  -18.252 1.00 78.94  ? 363 ILE D CG2 1 
ATOM   15670 C CD1 . ILE D 1 363 ? 55.784  -0.044  -15.753 1.00 78.83  ? 363 ILE D CD1 1 
ATOM   15671 N N   . THR D 1 364 ? 56.285  0.621   -20.908 1.00 88.43  ? 364 THR D N   1 
ATOM   15672 C CA  . THR D 1 364 ? 56.075  0.477   -22.342 1.00 91.31  ? 364 THR D CA  1 
ATOM   15673 C C   . THR D 1 364 ? 55.266  -0.784  -22.651 1.00 89.14  ? 364 THR D C   1 
ATOM   15674 O O   . THR D 1 364 ? 54.411  -0.759  -23.532 1.00 88.37  ? 364 THR D O   1 
ATOM   15675 C CB  . THR D 1 364 ? 57.408  0.438   -23.080 1.00 94.98  ? 364 THR D CB  1 
ATOM   15676 O OG1 . THR D 1 364 ? 58.121  -0.616  -22.434 1.00 95.56  ? 364 THR D OG1 1 
ATOM   15677 C CG2 . THR D 1 364 ? 58.108  1.786   -23.055 1.00 97.36  ? 364 THR D CG2 1 
ATOM   15678 N N   . SER D 1 365 ? 55.571  -1.890  -21.966 1.00 86.94  ? 365 SER D N   1 
ATOM   15679 C CA  . SER D 1 365 ? 54.923  -3.155  -22.275 1.00 85.97  ? 365 SER D CA  1 
ATOM   15680 C C   . SER D 1 365 ? 54.009  -3.622  -21.132 1.00 82.70  ? 365 SER D C   1 
ATOM   15681 O O   . SER D 1 365 ? 54.298  -3.463  -19.949 1.00 80.90  ? 365 SER D O   1 
ATOM   15682 C CB  . SER D 1 365 ? 55.958  -4.183  -22.624 1.00 86.47  ? 365 SER D CB  1 
ATOM   15683 O OG  . SER D 1 365 ? 56.729  -4.472  -21.473 1.00 85.63  ? 365 SER D OG  1 
ATOM   15684 N N   . GLU D 1 366 ? 52.872  -4.216  -21.482 1.00 81.40  ? 366 GLU D N   1 
ATOM   15685 C CA  . GLU D 1 366 ? 51.981  -4.699  -20.448 1.00 79.94  ? 366 GLU D CA  1 
ATOM   15686 C C   . GLU D 1 366 ? 52.460  -6.054  -19.938 1.00 78.91  ? 366 GLU D C   1 
ATOM   15687 O O   . GLU D 1 366 ? 53.290  -6.711  -20.572 1.00 80.01  ? 366 GLU D O   1 
ATOM   15688 C CB  . GLU D 1 366 ? 50.577  -4.848  -21.012 1.00 81.43  ? 366 GLU D CB  1 
ATOM   15689 C CG  . GLU D 1 366 ? 50.496  -5.995  -22.011 1.00 83.35  ? 366 GLU D CG  1 
ATOM   15690 C CD  . GLU D 1 366 ? 49.085  -6.246  -22.471 1.00 83.59  ? 366 GLU D CD  1 
ATOM   15691 O OE1 . GLU D 1 366 ? 48.232  -6.556  -21.609 1.00 83.69  ? 366 GLU D OE1 1 
ATOM   15692 O OE2 . GLU D 1 366 ? 48.871  -6.102  -23.690 1.00 85.69  ? 366 GLU D OE2 1 
ATOM   15693 N N   . GLY D 1 367 ? 51.906  -6.456  -18.787 1.00 76.40  ? 367 GLY D N   1 
ATOM   15694 C CA  . GLY D 1 367 ? 52.171  -7.756  -18.197 1.00 75.99  ? 367 GLY D CA  1 
ATOM   15695 C C   . GLY D 1 367 ? 53.309  -7.722  -17.174 1.00 76.56  ? 367 GLY D C   1 
ATOM   15696 O O   . GLY D 1 367 ? 53.402  -6.810  -16.354 1.00 77.53  ? 367 GLY D O   1 
ATOM   15697 N N   . TYR D 1 368 ? 54.145  -8.766  -17.185 1.00 76.04  ? 368 TYR D N   1 
ATOM   15698 C CA  . TYR D 1 368 ? 55.078  -8.975  -16.099 1.00 74.19  ? 368 TYR D CA  1 
ATOM   15699 C C   . TYR D 1 368 ? 56.223  -8.029  -16.339 1.00 75.62  ? 368 TYR D C   1 
ATOM   15700 O O   . TYR D 1 368 ? 56.607  -7.885  -17.488 1.00 77.26  ? 368 TYR D O   1 
ATOM   15701 C CB  . TYR D 1 368 ? 55.626  -10.400 -16.023 1.00 73.45  ? 368 TYR D CB  1 
ATOM   15702 C CG  . TYR D 1 368 ? 56.667  -10.581 -14.926 1.00 72.26  ? 368 TYR D CG  1 
ATOM   15703 C CD1 . TYR D 1 368 ? 56.268  -10.761 -13.607 1.00 70.12  ? 368 TYR D CD1 1 
ATOM   15704 C CD2 . TYR D 1 368 ? 58.039  -10.585 -15.204 1.00 72.98  ? 368 TYR D CD2 1 
ATOM   15705 C CE1 . TYR D 1 368 ? 57.195  -10.944 -12.592 1.00 69.98  ? 368 TYR D CE1 1 
ATOM   15706 C CE2 . TYR D 1 368 ? 58.978  -10.756 -14.195 1.00 72.42  ? 368 TYR D CE2 1 
ATOM   15707 C CZ  . TYR D 1 368 ? 58.554  -10.947 -12.886 1.00 71.09  ? 368 TYR D CZ  1 
ATOM   15708 O OH  . TYR D 1 368 ? 59.425  -11.116 -11.848 1.00 70.03  ? 368 TYR D OH  1 
ATOM   15709 N N   . MET D 1 369 ? 56.734  -7.433  -15.256 1.00 76.69  ? 369 MET D N   1 
ATOM   15710 C CA  . MET D 1 369 ? 57.855  -6.503  -15.293 1.00 79.00  ? 369 MET D CA  1 
ATOM   15711 C C   . MET D 1 369 ? 58.618  -6.679  -13.981 1.00 78.40  ? 369 MET D C   1 
ATOM   15712 O O   . MET D 1 369 ? 57.987  -6.905  -12.945 1.00 77.06  ? 369 MET D O   1 
ATOM   15713 C CB  . MET D 1 369 ? 57.343  -5.069  -15.482 1.00 82.23  ? 369 MET D CB  1 
ATOM   15714 C CG  . MET D 1 369 ? 58.399  -3.963  -15.475 1.00 88.87  ? 369 MET D CG  1 
ATOM   15715 S SD  . MET D 1 369 ? 58.500  -3.022  -13.936 1.00 93.49  ? 369 MET D SD  1 
ATOM   15716 C CE  . MET D 1 369 ? 56.759  -2.599  -13.800 1.00 89.53  ? 369 MET D CE  1 
ATOM   15717 N N   . ALA D 1 370 ? 59.963  -6.636  -14.043 1.00 79.25  ? 370 ALA D N   1 
ATOM   15718 C CA  . ALA D 1 370 ? 60.808  -6.842  -12.874 1.00 78.45  ? 370 ALA D CA  1 
ATOM   15719 C C   . ALA D 1 370 ? 61.869  -5.747  -12.780 1.00 79.77  ? 370 ALA D C   1 
ATOM   15720 O O   . ALA D 1 370 ? 62.338  -5.241  -13.795 1.00 81.86  ? 370 ALA D O   1 
ATOM   15721 C CB  . ALA D 1 370 ? 61.431  -8.211  -12.926 1.00 78.24  ? 370 ALA D CB  1 
ATOM   15722 N N   . ASP D 1 371 ? 62.248  -5.382  -11.548 1.00 78.96  ? 371 ASP D N   1 
ATOM   15723 C CA  . ASP D 1 371 ? 63.182  -4.284  -11.328 1.00 79.31  ? 371 ASP D CA  1 
ATOM   15724 C C   . ASP D 1 371 ? 63.630  -4.305  -9.866  1.00 79.73  ? 371 ASP D C   1 
ATOM   15725 O O   . ASP D 1 371 ? 63.296  -5.241  -9.131  1.00 80.32  ? 371 ASP D O   1 
ATOM   15726 C CB  . ASP D 1 371 ? 62.534  -2.964  -11.706 1.00 78.14  ? 371 ASP D CB  1 
ATOM   15727 C CG  . ASP D 1 371 ? 63.438  -1.899  -12.300 1.00 79.29  ? 371 ASP D CG  1 
ATOM   15728 O OD1 . ASP D 1 371 ? 64.664  -2.002  -12.093 1.00 81.22  ? 371 ASP D OD1 1 
ATOM   15729 O OD2 . ASP D 1 371 ? 62.903  -0.995  -12.984 1.00 78.14  ? 371 ASP D OD2 1 
ATOM   15730 N N   . GLU D 1 372 ? 64.383  -3.276  -9.452  1.00 80.24  ? 372 GLU D N   1 
ATOM   15731 C CA  . GLU D 1 372 ? 64.816  -3.140  -8.072  1.00 79.64  ? 372 GLU D CA  1 
ATOM   15732 C C   . GLU D 1 372 ? 64.448  -1.777  -7.506  1.00 79.12  ? 372 GLU D C   1 
ATOM   15733 O O   . GLU D 1 372 ? 64.498  -0.790  -8.223  1.00 80.41  ? 372 GLU D O   1 
ATOM   15734 C CB  . GLU D 1 372 ? 66.331  -3.131  -7.962  1.00 81.47  ? 372 GLU D CB  1 
ATOM   15735 C CG  . GLU D 1 372 ? 66.944  -4.503  -8.191  1.00 82.68  ? 372 GLU D CG  1 
ATOM   15736 C CD  . GLU D 1 372 ? 68.444  -4.450  -8.057  1.00 84.40  ? 372 GLU D CD  1 
ATOM   15737 O OE1 . GLU D 1 372 ? 69.022  -3.327  -8.079  1.00 84.72  ? 372 GLU D OE1 1 
ATOM   15738 O OE2 . GLU D 1 372 ? 68.991  -5.564  -7.910  1.00 85.63  ? 372 GLU D OE2 1 
ATOM   15739 N N   . LEU D 1 373 ? 64.158  -1.738  -6.203  1.00 77.67  ? 373 LEU D N   1 
ATOM   15740 C CA  . LEU D 1 373 ? 64.003  -0.494  -5.476  1.00 77.43  ? 373 LEU D CA  1 
ATOM   15741 C C   . LEU D 1 373 ? 65.313  -0.195  -4.757  1.00 78.55  ? 373 LEU D C   1 
ATOM   15742 O O   . LEU D 1 373 ? 66.060  -1.116  -4.473  1.00 78.54  ? 373 LEU D O   1 
ATOM   15743 C CB  . LEU D 1 373 ? 62.831  -0.612  -4.497  1.00 75.54  ? 373 LEU D CB  1 
ATOM   15744 C CG  . LEU D 1 373 ? 61.430  -0.743  -5.108  1.00 73.97  ? 373 LEU D CG  1 
ATOM   15745 C CD1 . LEU D 1 373 ? 60.376  -1.075  -4.059  1.00 71.87  ? 373 LEU D CD1 1 
ATOM   15746 C CD2 . LEU D 1 373 ? 61.075  0.540   -5.846  1.00 74.33  ? 373 LEU D CD2 1 
ATOM   15747 N N   . THR D 1 374 ? 65.569  1.077   -4.433  1.00 79.41  ? 374 THR D N   1 
ATOM   15748 C CA  . THR D 1 374 ? 66.622  1.387   -3.479  1.00 81.75  ? 374 THR D CA  1 
ATOM   15749 C C   . THR D 1 374 ? 66.086  2.274   -2.351  1.00 81.84  ? 374 THR D C   1 
ATOM   15750 O O   . THR D 1 374 ? 65.785  3.464   -2.548  1.00 83.16  ? 374 THR D O   1 
ATOM   15751 C CB  . THR D 1 374 ? 67.834  2.021   -4.161  1.00 84.21  ? 374 THR D CB  1 
ATOM   15752 O OG1 . THR D 1 374 ? 68.266  1.223   -5.258  1.00 85.69  ? 374 THR D OG1 1 
ATOM   15753 C CG2 . THR D 1 374 ? 69.029  2.088   -3.232  1.00 86.07  ? 374 THR D CG2 1 
ATOM   15754 N N   . ILE D 1 375 ? 66.057  1.677   -1.151  1.00 80.96  ? 375 ILE D N   1 
ATOM   15755 C CA  . ILE D 1 375 ? 65.734  2.345   0.101   1.00 80.08  ? 375 ILE D CA  1 
ATOM   15756 C C   . ILE D 1 375 ? 67.009  2.606   0.897   1.00 81.19  ? 375 ILE D C   1 
ATOM   15757 O O   . ILE D 1 375 ? 67.976  1.873   0.726   1.00 82.20  ? 375 ILE D O   1 
ATOM   15758 C CB  . ILE D 1 375 ? 64.786  1.444   0.893   1.00 79.11  ? 375 ILE D CB  1 
ATOM   15759 C CG1 . ILE D 1 375 ? 65.448  0.120   1.257   1.00 79.92  ? 375 ILE D CG1 1 
ATOM   15760 C CG2 . ILE D 1 375 ? 63.493  1.229   0.105   1.00 78.28  ? 375 ILE D CG2 1 
ATOM   15761 C CD1 . ILE D 1 375 ? 64.632  -0.733  2.212   1.00 79.58  ? 375 ILE D CD1 1 
ATOM   15762 N N   . ASP D 1 376 ? 66.982  3.607   1.788   1.00 81.00  ? 376 ASP D N   1 
ATOM   15763 C CA  . ASP D 1 376 ? 68.116  3.948   2.637   1.00 82.75  ? 376 ASP D CA  1 
ATOM   15764 C C   . ASP D 1 376 ? 67.666  3.978   4.093   1.00 82.54  ? 376 ASP D C   1 
ATOM   15765 O O   . ASP D 1 376 ? 67.774  5.001   4.754   1.00 84.16  ? 376 ASP D O   1 
ATOM   15766 C CB  . ASP D 1 376 ? 68.748  5.290   2.279   1.00 84.37  ? 376 ASP D CB  1 
ATOM   15767 C CG  . ASP D 1 376 ? 70.037  5.670   3.018   1.00 86.34  ? 376 ASP D CG  1 
ATOM   15768 O OD1 . ASP D 1 376 ? 70.599  4.794   3.705   1.00 87.20  ? 376 ASP D OD1 1 
ATOM   15769 O OD2 . ASP D 1 376 ? 70.482  6.834   2.907   1.00 86.24  ? 376 ASP D OD2 1 
ATOM   15770 N N   . PRO D 1 377 ? 67.237  2.844   4.673   1.00 81.52  ? 377 PRO D N   1 
ATOM   15771 C CA  . PRO D 1 377 ? 66.653  2.838   6.020   1.00 81.29  ? 377 PRO D CA  1 
ATOM   15772 C C   . PRO D 1 377 ? 67.648  3.081   7.153   1.00 83.48  ? 377 PRO D C   1 
ATOM   15773 O O   . PRO D 1 377 ? 68.780  2.610   7.074   1.00 84.22  ? 377 PRO D O   1 
ATOM   15774 C CB  . PRO D 1 377 ? 66.145  1.393   6.054   1.00 79.88  ? 377 PRO D CB  1 
ATOM   15775 C CG  . PRO D 1 377 ? 67.231  0.648   5.319   1.00 81.05  ? 377 PRO D CG  1 
ATOM   15776 C CD  . PRO D 1 377 ? 67.392  1.508   4.092   1.00 80.95  ? 377 PRO D CD  1 
ATOM   15777 N N   . VAL D 1 378 ? 67.196  3.739   8.234   1.00 83.65  ? 378 VAL D N   1 
ATOM   15778 C CA  . VAL D 1 378 ? 68.031  3.945   9.413   1.00 84.63  ? 378 VAL D CA  1 
ATOM   15779 C C   . VAL D 1 378 ? 67.742  2.892   10.481  1.00 84.80  ? 378 VAL D C   1 
ATOM   15780 O O   . VAL D 1 378 ? 66.594  2.591   10.806  1.00 83.89  ? 378 VAL D O   1 
ATOM   15781 C CB  . VAL D 1 378 ? 67.824  5.331   10.028  1.00 84.75  ? 378 VAL D CB  1 
ATOM   15782 C CG1 . VAL D 1 378 ? 68.574  5.466   11.347  1.00 86.14  ? 378 VAL D CG1 1 
ATOM   15783 C CG2 . VAL D 1 378 ? 68.196  6.413   9.031   1.00 85.74  ? 378 VAL D CG2 1 
ATOM   15784 N N   . GLY D 1 379 ? 68.817  2.397   11.101  1.00 86.59  ? 379 GLY D N   1 
ATOM   15785 C CA  . GLY D 1 379 ? 68.678  1.436   12.175  1.00 85.35  ? 379 GLY D CA  1 
ATOM   15786 C C   . GLY D 1 379 ? 67.828  0.299   11.661  1.00 82.28  ? 379 GLY D C   1 
ATOM   15787 O O   . GLY D 1 379 ? 68.156  -0.276  10.621  1.00 81.98  ? 379 GLY D O   1 
ATOM   15788 N N   . ILE D 1 380 ? 66.764  0.013   12.404  1.00 80.35  ? 380 ILE D N   1 
ATOM   15789 C CA  . ILE D 1 380 ? 65.638  -0.735  11.870  1.00 78.01  ? 380 ILE D CA  1 
ATOM   15790 C C   . ILE D 1 380 ? 64.534  0.286   11.674  1.00 77.28  ? 380 ILE D C   1 
ATOM   15791 O O   . ILE D 1 380 ? 64.365  1.125   12.551  1.00 78.06  ? 380 ILE D O   1 
ATOM   15792 C CB  . ILE D 1 380 ? 65.195  -1.842  12.833  1.00 76.80  ? 380 ILE D CB  1 
ATOM   15793 C CG1 . ILE D 1 380 ? 66.259  -2.869  13.052  1.00 77.73  ? 380 ILE D CG1 1 
ATOM   15794 C CG2 . ILE D 1 380 ? 63.922  -2.494  12.330  1.00 74.99  ? 380 ILE D CG2 1 
ATOM   15795 C CD1 . ILE D 1 380 ? 66.114  -3.613  14.364  1.00 78.24  ? 380 ILE D CD1 1 
ATOM   15796 N N   . GLU D 1 381 ? 63.886  0.276   10.509  1.00 76.85  ? 381 GLU D N   1 
ATOM   15797 C CA  . GLU D 1 381 ? 62.864  1.306   10.203  1.00 76.56  ? 381 GLU D CA  1 
ATOM   15798 C C   . GLU D 1 381 ? 61.626  0.706   9.530   1.00 73.56  ? 381 GLU D C   1 
ATOM   15799 O O   . GLU D 1 381 ? 61.796  -0.021  8.534   1.00 73.13  ? 381 GLU D O   1 
ATOM   15800 C CB  . GLU D 1 381 ? 63.428  2.319   9.212   1.00 78.85  ? 381 GLU D CB  1 
ATOM   15801 C CG  . GLU D 1 381 ? 62.717  3.667   9.210   1.00 79.38  ? 381 GLU D CG  1 
ATOM   15802 C CD  . GLU D 1 381 ? 63.300  4.607   8.173   1.00 82.89  ? 381 GLU D CD  1 
ATOM   15803 O OE1 . GLU D 1 381 ? 63.226  4.291   6.970   1.00 82.71  ? 381 GLU D OE1 1 
ATOM   15804 O OE2 . GLU D 1 381 ? 63.837  5.659   8.574   1.00 86.55  ? 381 GLU D OE2 1 
ATOM   15805 N N   . ASP D 1 382 ? 60.432  1.044   10.032  1.00 71.17  ? 382 ASP D N   1 
ATOM   15806 C CA  . ASP D 1 382 ? 59.172  0.616   9.373   1.00 68.47  ? 382 ASP D CA  1 
ATOM   15807 C C   . ASP D 1 382 ? 58.968  1.503   8.156   1.00 67.86  ? 382 ASP D C   1 
ATOM   15808 O O   . ASP D 1 382 ? 59.248  2.698   8.271   1.00 68.80  ? 382 ASP D O   1 
ATOM   15809 C CB  . ASP D 1 382 ? 57.981  0.767   10.294  1.00 67.30  ? 382 ASP D CB  1 
ATOM   15810 C CG  . ASP D 1 382 ? 58.106  1.787   11.412  1.00 67.46  ? 382 ASP D CG  1 
ATOM   15811 O OD1 . ASP D 1 382 ? 59.132  1.762   12.118  1.00 68.23  ? 382 ASP D OD1 1 
ATOM   15812 O OD2 . ASP D 1 382 ? 57.161  2.582   11.576  1.00 64.97  ? 382 ASP D OD2 1 
ATOM   15813 N N   . MET D 1 383 ? 58.500  0.952   7.044   1.00 67.07  ? 383 MET D N   1 
ATOM   15814 C CA  . MET D 1 383 ? 58.386  1.783   5.824   1.00 67.44  ? 383 MET D CA  1 
ATOM   15815 C C   . MET D 1 383 ? 57.117  1.483   5.011   1.00 66.39  ? 383 MET D C   1 
ATOM   15816 O O   . MET D 1 383 ? 57.043  0.389   4.430   1.00 65.27  ? 383 MET D O   1 
ATOM   15817 C CB  . MET D 1 383 ? 59.594  1.562   4.913   1.00 68.90  ? 383 MET D CB  1 
ATOM   15818 C CG  . MET D 1 383 ? 60.923  1.939   5.539   1.00 71.17  ? 383 MET D CG  1 
ATOM   15819 S SD  . MET D 1 383 ? 62.313  1.863   4.395   1.00 72.92  ? 383 MET D SD  1 
ATOM   15820 C CE  . MET D 1 383 ? 61.655  2.726   2.965   1.00 72.40  ? 383 MET D CE  1 
ATOM   15821 N N   . GLU D 1 384 ? 56.163  2.424   4.957   1.00 66.11  ? 384 GLU D N   1 
ATOM   15822 C CA  . GLU D 1 384 ? 55.018  2.266   4.076   1.00 65.20  ? 384 GLU D CA  1 
ATOM   15823 C C   . GLU D 1 384 ? 55.396  2.765   2.691   1.00 65.76  ? 384 GLU D C   1 
ATOM   15824 O O   . GLU D 1 384 ? 55.593  3.941   2.486   1.00 66.55  ? 384 GLU D O   1 
ATOM   15825 C CB  . GLU D 1 384 ? 53.788  3.014   4.556   1.00 64.68  ? 384 GLU D CB  1 
ATOM   15826 C CG  . GLU D 1 384 ? 52.578  2.871   3.641   1.00 63.73  ? 384 GLU D CG  1 
ATOM   15827 C CD  . GLU D 1 384 ? 51.358  3.598   4.194   1.00 63.45  ? 384 GLU D CD  1 
ATOM   15828 O OE1 . GLU D 1 384 ? 51.535  4.452   5.096   1.00 64.08  ? 384 GLU D OE1 1 
ATOM   15829 O OE2 . GLU D 1 384 ? 50.229  3.308   3.746   1.00 62.80  ? 384 GLU D OE2 1 
ATOM   15830 N N   . LEU D 1 385 ? 55.550  1.835   1.761   1.00 66.90  ? 385 LEU D N   1 
ATOM   15831 C CA  . LEU D 1 385 ? 55.950  2.118   0.397   1.00 67.55  ? 385 LEU D CA  1 
ATOM   15832 C C   . LEU D 1 385 ? 54.705  2.472   -0.385  1.00 65.51  ? 385 LEU D C   1 
ATOM   15833 O O   . LEU D 1 385 ? 53.772  1.685   -0.381  1.00 64.64  ? 385 LEU D O   1 
ATOM   15834 C CB  . LEU D 1 385 ? 56.596  0.840   -0.148  1.00 69.14  ? 385 LEU D CB  1 
ATOM   15835 C CG  . LEU D 1 385 ? 58.124  0.805   -0.171  1.00 71.89  ? 385 LEU D CG  1 
ATOM   15836 C CD1 . LEU D 1 385 ? 58.783  1.257   1.128   1.00 73.64  ? 385 LEU D CD1 1 
ATOM   15837 C CD2 . LEU D 1 385 ? 58.546  -0.599  -0.553  1.00 72.17  ? 385 LEU D CD2 1 
ATOM   15838 N N   . ALA D 1 386 ? 54.697  3.614   -1.065  1.00 65.10  ? 386 ALA D N   1 
ATOM   15839 C CA  . ALA D 1 386 ? 53.438  4.116   -1.598  1.00 63.62  ? 386 ALA D CA  1 
ATOM   15840 C C   . ALA D 1 386 ? 53.428  3.998   -3.114  1.00 64.15  ? 386 ALA D C   1 
ATOM   15841 O O   . ALA D 1 386 ? 54.023  4.813   -3.807  1.00 65.39  ? 386 ALA D O   1 
ATOM   15842 C CB  . ALA D 1 386 ? 53.183  5.532   -1.145  1.00 63.05  ? 386 ALA D CB  1 
ATOM   15843 N N   . PHE D 1 387 ? 52.719  2.987   -3.612  1.00 63.55  ? 387 PHE D N   1 
ATOM   15844 C CA  . PHE D 1 387 ? 52.658  2.742   -5.038  1.00 65.02  ? 387 PHE D CA  1 
ATOM   15845 C C   . PHE D 1 387 ? 51.523  3.536   -5.659  1.00 65.84  ? 387 PHE D C   1 
ATOM   15846 O O   . PHE D 1 387 ? 50.460  3.692   -5.056  1.00 65.61  ? 387 PHE D O   1 
ATOM   15847 C CB  . PHE D 1 387 ? 52.443  1.261   -5.334  1.00 65.25  ? 387 PHE D CB  1 
ATOM   15848 C CG  . PHE D 1 387 ? 53.673  0.430   -5.013  1.00 66.31  ? 387 PHE D CG  1 
ATOM   15849 C CD1 . PHE D 1 387 ? 54.058  0.210   -3.695  1.00 66.41  ? 387 PHE D CD1 1 
ATOM   15850 C CD2 . PHE D 1 387 ? 54.455  -0.085  -6.040  1.00 67.95  ? 387 PHE D CD2 1 
ATOM   15851 C CE1 . PHE D 1 387 ? 55.190  -0.528  -3.414  1.00 68.38  ? 387 PHE D CE1 1 
ATOM   15852 C CE2 . PHE D 1 387 ? 55.584  -0.826  -5.756  1.00 69.28  ? 387 PHE D CE2 1 
ATOM   15853 C CZ  . PHE D 1 387 ? 55.949  -1.056  -4.443  1.00 69.52  ? 387 PHE D CZ  1 
ATOM   15854 N N   . GLU D 1 388 ? 51.772  3.995   -6.888  1.00 67.45  ? 388 GLU D N   1 
ATOM   15855 C CA  . GLU D 1 388 ? 50.886  4.899   -7.593  1.00 68.09  ? 388 GLU D CA  1 
ATOM   15856 C C   . GLU D 1 388 ? 50.868  4.529   -9.075  1.00 69.03  ? 388 GLU D C   1 
ATOM   15857 O O   . GLU D 1 388 ? 51.870  4.751   -9.757  1.00 71.53  ? 388 GLU D O   1 
ATOM   15858 C CB  . GLU D 1 388 ? 51.431  6.318   -7.406  1.00 69.04  ? 388 GLU D CB  1 
ATOM   15859 C CG  . GLU D 1 388 ? 51.275  6.911   -6.006  1.00 69.02  ? 388 GLU D CG  1 
ATOM   15860 C CD  . GLU D 1 388 ? 51.766  8.367   -5.922  1.00 71.61  ? 388 GLU D CD  1 
ATOM   15861 O OE1 . GLU D 1 388 ? 52.133  8.941   -6.977  1.00 72.96  ? 388 GLU D OE1 1 
ATOM   15862 O OE2 . GLU D 1 388 ? 51.831  8.933   -4.800  1.00 71.90  ? 388 GLU D OE2 1 
ATOM   15863 N N   . PHE D 1 389 ? 49.735  4.008   -9.575  1.00 68.20  ? 389 PHE D N   1 
ATOM   15864 C CA  . PHE D 1 389 ? 49.613  3.614   -10.976 1.00 68.99  ? 389 PHE D CA  1 
ATOM   15865 C C   . PHE D 1 389 ? 48.883  4.673   -11.811 1.00 70.44  ? 389 PHE D C   1 
ATOM   15866 O O   . PHE D 1 389 ? 47.723  4.988   -11.533 1.00 69.27  ? 389 PHE D O   1 
ATOM   15867 C CB  . PHE D 1 389 ? 48.848  2.296   -11.099 1.00 67.31  ? 389 PHE D CB  1 
ATOM   15868 C CG  . PHE D 1 389 ? 49.505  1.159   -10.338 1.00 66.42  ? 389 PHE D CG  1 
ATOM   15869 C CD1 . PHE D 1 389 ? 49.384  1.077   -8.953  1.00 64.90  ? 389 PHE D CD1 1 
ATOM   15870 C CD2 . PHE D 1 389 ? 50.256  0.195   -11.008 1.00 66.77  ? 389 PHE D CD2 1 
ATOM   15871 C CE1 . PHE D 1 389 ? 50.007  0.061   -8.252  1.00 64.24  ? 389 PHE D CE1 1 
ATOM   15872 C CE2 . PHE D 1 389 ? 50.868  -0.826  -10.302 1.00 66.04  ? 389 PHE D CE2 1 
ATOM   15873 C CZ  . PHE D 1 389 ? 50.744  -0.892  -8.928  1.00 65.00  ? 389 PHE D CZ  1 
ATOM   15874 N N   . TYR D 1 390 ? 49.544  5.122   -12.892 1.00 72.39  ? 390 TYR D N   1 
ATOM   15875 C CA  . TYR D 1 390 ? 49.036  6.178   -13.754 1.00 74.55  ? 390 TYR D CA  1 
ATOM   15876 C C   . TYR D 1 390 ? 48.686  5.644   -15.144 1.00 75.22  ? 390 TYR D C   1 
ATOM   15877 O O   . TYR D 1 390 ? 49.330  4.734   -15.656 1.00 74.21  ? 390 TYR D O   1 
ATOM   15878 C CB  . TYR D 1 390 ? 50.107  7.258   -13.908 1.00 77.15  ? 390 TYR D CB  1 
ATOM   15879 C CG  . TYR D 1 390 ? 50.510  7.983   -12.632 1.00 77.53  ? 390 TYR D CG  1 
ATOM   15880 C CD1 . TYR D 1 390 ? 51.247  7.345   -11.647 1.00 77.19  ? 390 TYR D CD1 1 
ATOM   15881 C CD2 . TYR D 1 390 ? 50.216  9.321   -12.440 1.00 78.75  ? 390 TYR D CD2 1 
ATOM   15882 C CE1 . TYR D 1 390 ? 51.635  7.998   -10.491 1.00 76.15  ? 390 TYR D CE1 1 
ATOM   15883 C CE2 . TYR D 1 390 ? 50.614  9.991   -11.296 1.00 78.46  ? 390 TYR D CE2 1 
ATOM   15884 C CZ  . TYR D 1 390 ? 51.305  9.319   -10.313 1.00 76.39  ? 390 TYR D CZ  1 
ATOM   15885 O OH  . TYR D 1 390 ? 51.672  9.935   -9.171  1.00 77.08  ? 390 TYR D OH  1 
ATOM   15886 N N   . ASP D 1 391 ? 47.699  6.294   -15.774 1.00 76.68  ? 391 ASP D N   1 
ATOM   15887 C CA  . ASP D 1 391 ? 47.180  5.912   -17.083 1.00 78.44  ? 391 ASP D CA  1 
ATOM   15888 C C   . ASP D 1 391 ? 47.849  6.771   -18.154 1.00 80.40  ? 391 ASP D C   1 
ATOM   15889 O O   . ASP D 1 391 ? 48.796  7.466   -17.842 1.00 80.93  ? 391 ASP D O   1 
ATOM   15890 C CB  . ASP D 1 391 ? 45.663  6.053   -17.123 1.00 77.46  ? 391 ASP D CB  1 
ATOM   15891 C CG  . ASP D 1 391 ? 45.133  7.479   -17.166 1.00 78.12  ? 391 ASP D CG  1 
ATOM   15892 O OD1 . ASP D 1 391 ? 45.941  8.414   -17.295 1.00 78.58  ? 391 ASP D OD1 1 
ATOM   15893 O OD2 . ASP D 1 391 ? 43.910  7.648   -17.074 1.00 80.23  ? 391 ASP D OD2 1 
ATOM   15894 N N   . SER D 1 392 ? 47.304  6.786   -19.382 1.00 82.37  ? 392 SER D N   1 
ATOM   15895 C CA  . SER D 1 392 ? 47.877  7.528   -20.499 1.00 84.32  ? 392 SER D CA  1 
ATOM   15896 C C   . SER D 1 392 ? 47.477  9.013   -20.500 1.00 85.75  ? 392 SER D C   1 
ATOM   15897 O O   . SER D 1 392 ? 47.783  9.731   -21.449 1.00 87.56  ? 392 SER D O   1 
ATOM   15898 C CB  . SER D 1 392 ? 47.495  6.900   -21.822 1.00 84.74  ? 392 SER D CB  1 
ATOM   15899 O OG  . SER D 1 392 ? 46.311  7.506   -22.331 1.00 84.90  ? 392 SER D OG  1 
ATOM   15900 N N   . ASP D 1 393 ? 46.762  9.493   -19.478 1.00 84.55  ? 393 ASP D N   1 
ATOM   15901 C CA  . ASP D 1 393 ? 46.579  10.931  -19.315 1.00 85.39  ? 393 ASP D CA  1 
ATOM   15902 C C   . ASP D 1 393 ? 47.280  11.360  -18.034 1.00 83.97  ? 393 ASP D C   1 
ATOM   15903 O O   . ASP D 1 393 ? 47.015  12.446  -17.525 1.00 84.94  ? 393 ASP D O   1 
ATOM   15904 C CB  . ASP D 1 393 ? 45.109  11.333  -19.310 1.00 85.03  ? 393 ASP D CB  1 
ATOM   15905 C CG  . ASP D 1 393 ? 44.360  11.046  -20.605 1.00 86.22  ? 393 ASP D CG  1 
ATOM   15906 O OD1 . ASP D 1 393 ? 44.793  11.631  -21.623 1.00 88.53  ? 393 ASP D OD1 1 
ATOM   15907 O OD2 . ASP D 1 393 ? 43.373  10.234  -20.585 1.00 83.91  ? 393 ASP D OD2 1 
ATOM   15908 N N   . ASN D 1 394 ? 48.133  10.468  -17.520 1.00 82.02  ? 394 ASN D N   1 
ATOM   15909 C CA  . ASN D 1 394 ? 48.929  10.689  -16.325 1.00 81.36  ? 394 ASN D CA  1 
ATOM   15910 C C   . ASN D 1 394 ? 48.036  10.858  -15.089 1.00 80.66  ? 394 ASN D C   1 
ATOM   15911 O O   . ASN D 1 394 ? 48.415  11.590  -14.180 1.00 78.94  ? 394 ASN D O   1 
ATOM   15912 C CB  . ASN D 1 394 ? 49.928  11.818  -16.561 1.00 82.61  ? 394 ASN D CB  1 
ATOM   15913 C CG  . ASN D 1 394 ? 50.947  11.941  -15.452 1.00 82.34  ? 394 ASN D CG  1 
ATOM   15914 O OD1 . ASN D 1 394 ? 51.772  11.040  -15.249 1.00 82.00  ? 394 ASN D OD1 1 
ATOM   15915 N ND2 . ASN D 1 394 ? 50.908  13.051  -14.726 1.00 82.00  ? 394 ASN D ND2 1 
ATOM   15916 N N   . LYS D 1 395 ? 46.903  10.121  -15.019 1.00 82.08  ? 395 LYS D N   1 
ATOM   15917 C CA  . LYS D 1 395 ? 45.952  10.222  -13.915 1.00 82.77  ? 395 LYS D CA  1 
ATOM   15918 C C   . LYS D 1 395 ? 46.008  8.976   -13.039 1.00 79.03  ? 395 LYS D C   1 
ATOM   15919 O O   . LYS D 1 395 ? 45.828  7.874   -13.544 1.00 80.02  ? 395 LYS D O   1 
ATOM   15920 C CB  . LYS D 1 395 ? 44.536  10.482  -14.443 1.00 88.52  ? 395 LYS D CB  1 
ATOM   15921 C CG  . LYS D 1 395 ? 44.344  11.959  -14.813 1.00 98.87  ? 395 LYS D CG  1 
ATOM   15922 C CD  . LYS D 1 395 ? 42.944  12.432  -15.202 1.00 109.03 ? 395 LYS D CD  1 
ATOM   15923 C CE  . LYS D 1 395 ? 42.878  13.949  -15.282 1.00 116.34 ? 395 LYS D CE  1 
ATOM   15924 N NZ  . LYS D 1 395 ? 41.526  14.438  -15.581 1.00 121.67 ? 395 LYS D NZ  1 
ATOM   15925 N N   . ILE D 1 396 ? 46.232  9.161   -11.728 1.00 75.98  ? 396 ILE D N   1 
ATOM   15926 C CA  . ILE D 1 396 ? 46.384  8.039   -10.817 1.00 73.85  ? 396 ILE D CA  1 
ATOM   15927 C C   . ILE D 1 396 ? 45.122  7.221   -10.920 1.00 71.48  ? 396 ILE D C   1 
ATOM   15928 O O   . ILE D 1 396 ? 44.049  7.774   -10.830 1.00 72.87  ? 396 ILE D O   1 
ATOM   15929 C CB  . ILE D 1 396 ? 46.679  8.467   -9.368  1.00 75.11  ? 396 ILE D CB  1 
ATOM   15930 C CG1 . ILE D 1 396 ? 48.033  9.214   -9.321  1.00 82.02  ? 396 ILE D CG1 1 
ATOM   15931 C CG2 . ILE D 1 396 ? 46.670  7.280   -8.404  1.00 72.27  ? 396 ILE D CG2 1 
ATOM   15932 C CD1 . ILE D 1 396 ? 48.710  9.309   -7.955  1.00 84.26  ? 396 ILE D CD1 1 
ATOM   15933 N N   . ILE D 1 397 ? 45.257  5.924   -11.179 1.00 70.84  ? 397 ILE D N   1 
ATOM   15934 C CA  . ILE D 1 397 ? 44.092  5.053   -11.224 1.00 68.25  ? 397 ILE D CA  1 
ATOM   15935 C C   . ILE D 1 397 ? 44.114  4.103   -10.042 1.00 65.34  ? 397 ILE D C   1 
ATOM   15936 O O   . ILE D 1 397 ? 43.125  3.419   -9.814  1.00 67.40  ? 397 ILE D O   1 
ATOM   15937 C CB  . ILE D 1 397 ? 43.988  4.297   -12.560 1.00 68.36  ? 397 ILE D CB  1 
ATOM   15938 C CG1 . ILE D 1 397 ? 45.215  3.446   -12.824 1.00 67.62  ? 397 ILE D CG1 1 
ATOM   15939 C CG2 . ILE D 1 397 ? 43.692  5.276   -13.708 1.00 70.17  ? 397 ILE D CG2 1 
ATOM   15940 C CD1 . ILE D 1 397 ? 45.267  2.877   -14.227 1.00 68.54  ? 397 ILE D CD1 1 
ATOM   15941 N N   . LYS D 1 398 ? 45.210  4.061   -9.293  1.00 63.44  ? 398 LYS D N   1 
ATOM   15942 C CA  . LYS D 1 398 ? 45.272  3.144   -8.172  1.00 61.63  ? 398 LYS D CA  1 
ATOM   15943 C C   . LYS D 1 398 ? 46.346  3.575   -7.189  1.00 61.31  ? 398 LYS D C   1 
ATOM   15944 O O   . LYS D 1 398 ? 47.454  3.911   -7.602  1.00 62.17  ? 398 LYS D O   1 
ATOM   15945 C CB  . LYS D 1 398 ? 45.589  1.710   -8.616  1.00 60.87  ? 398 LYS D CB  1 
ATOM   15946 C CG  . LYS D 1 398 ? 45.907  0.783   -7.468  1.00 59.95  ? 398 LYS D CG  1 
ATOM   15947 C CD  . LYS D 1 398 ? 46.152  -0.656  -7.890  1.00 60.07  ? 398 LYS D CD  1 
ATOM   15948 C CE  . LYS D 1 398 ? 46.352  -1.500  -6.679  1.00 59.75  ? 398 LYS D CE  1 
ATOM   15949 N NZ  . LYS D 1 398 ? 46.471  -2.897  -7.091  1.00 60.47  ? 398 LYS D NZ  1 
ATOM   15950 N N   . ASN D 1 399 ? 45.988  3.528   -5.898  1.00 60.25  ? 399 ASN D N   1 
ATOM   15951 C CA  . ASN D 1 399 ? 46.942  3.605   -4.808  1.00 60.07  ? 399 ASN D CA  1 
ATOM   15952 C C   . ASN D 1 399 ? 46.987  2.230   -4.160  1.00 60.39  ? 399 ASN D C   1 
ATOM   15953 O O   . ASN D 1 399 ? 46.061  1.452   -4.344  1.00 63.36  ? 399 ASN D O   1 
ATOM   15954 C CB  . ASN D 1 399 ? 46.623  4.729   -3.823  1.00 59.32  ? 399 ASN D CB  1 
ATOM   15955 C CG  . ASN D 1 399 ? 46.583  6.090   -4.482  1.00 59.61  ? 399 ASN D CG  1 
ATOM   15956 O OD1 . ASN D 1 399 ? 47.592  6.602   -5.000  1.00 59.97  ? 399 ASN D OD1 1 
ATOM   15957 N ND2 . ASN D 1 399 ? 45.390  6.670   -4.520  1.00 59.37  ? 399 ASN D ND2 1 
ATOM   15958 N N   . GLU D 1 400 ? 48.117  1.899   -3.526  1.00 60.97  ? 400 GLU D N   1 
ATOM   15959 C CA  . GLU D 1 400 ? 48.330  0.666   -2.780  1.00 60.15  ? 400 GLU D CA  1 
ATOM   15960 C C   . GLU D 1 400 ? 49.654  0.828   -2.058  1.00 60.95  ? 400 GLU D C   1 
ATOM   15961 O O   . GLU D 1 400 ? 50.622  1.283   -2.662  1.00 60.84  ? 400 GLU D O   1 
ATOM   15962 C CB  . GLU D 1 400 ? 48.432  -0.616  -3.612  1.00 60.15  ? 400 GLU D CB  1 
ATOM   15963 C CG  . GLU D 1 400 ? 48.712  -1.889  -2.803  1.00 59.32  ? 400 GLU D CG  1 
ATOM   15964 C CD  . GLU D 1 400 ? 48.186  -3.202  -3.376  1.00 58.62  ? 400 GLU D CD  1 
ATOM   15965 O OE1 . GLU D 1 400 ? 48.214  -3.329  -4.617  1.00 59.07  ? 400 GLU D OE1 1 
ATOM   15966 O OE2 . GLU D 1 400 ? 47.779  -4.107  -2.600  1.00 57.44  ? 400 GLU D OE2 1 
ATOM   15967 N N   . SER D 1 401 ? 49.642  0.509   -0.761  1.00 61.47  ? 401 SER D N   1 
ATOM   15968 C CA  . SER D 1 401 ? 50.828  0.600   0.069   1.00 62.69  ? 401 SER D CA  1 
ATOM   15969 C C   . SER D 1 401 ? 51.441  -0.791  0.216   1.00 64.56  ? 401 SER D C   1 
ATOM   15970 O O   . SER D 1 401 ? 50.708  -1.787  0.222   1.00 68.60  ? 401 SER D O   1 
ATOM   15971 C CB  . SER D 1 401 ? 50.476  1.215   1.394   1.00 62.52  ? 401 SER D CB  1 
ATOM   15972 O OG  . SER D 1 401 ? 50.219  2.611   1.233   1.00 63.09  ? 401 SER D OG  1 
ATOM   15973 N N   . ILE D 1 402 ? 52.781  -0.882  0.285   1.00 65.96  ? 402 ILE D N   1 
ATOM   15974 C CA  . ILE D 1 402 ? 53.426  -2.094  0.775   1.00 65.09  ? 402 ILE D CA  1 
ATOM   15975 C C   . ILE D 1 402 ? 54.260  -1.726  1.997   1.00 65.62  ? 402 ILE D C   1 
ATOM   15976 O O   . ILE D 1 402 ? 55.101  -0.829  1.933   1.00 66.79  ? 402 ILE D O   1 
ATOM   15977 C CB  . ILE D 1 402 ? 54.275  -2.757  -0.307  1.00 65.61  ? 402 ILE D CB  1 
ATOM   15978 C CG1 . ILE D 1 402 ? 53.498  -2.964  -1.596  1.00 65.46  ? 402 ILE D CG1 1 
ATOM   15979 C CG2 . ILE D 1 402 ? 54.847  -4.061  0.238   1.00 66.52  ? 402 ILE D CG2 1 
ATOM   15980 C CD1 . ILE D 1 402 ? 52.447  -4.063  -1.522  1.00 65.06  ? 402 ILE D CD1 1 
ATOM   15981 N N   . ASN D 1 403 ? 53.959  -2.382  3.122   1.00 64.96  ? 403 ASN D N   1 
ATOM   15982 C CA  . ASN D 1 403 ? 54.558  -2.052  4.405   1.00 65.47  ? 403 ASN D CA  1 
ATOM   15983 C C   . ASN D 1 403 ? 55.662  -3.070  4.614   1.00 65.54  ? 403 ASN D C   1 
ATOM   15984 O O   . ASN D 1 403 ? 55.399  -4.272  4.639   1.00 64.45  ? 403 ASN D O   1 
ATOM   15985 C CB  . ASN D 1 403 ? 53.639  -2.192  5.624   1.00 65.68  ? 403 ASN D CB  1 
ATOM   15986 C CG  . ASN D 1 403 ? 52.501  -1.194  5.720   1.00 64.86  ? 403 ASN D CG  1 
ATOM   15987 O OD1 . ASN D 1 403 ? 52.256  -0.605  6.782   1.00 64.11  ? 403 ASN D OD1 1 
ATOM   15988 N ND2 . ASN D 1 403 ? 51.716  -1.084  4.665   1.00 64.26  ? 403 ASN D ND2 1 
ATOM   15989 N N   . ILE D 1 404 ? 56.892  -2.576  4.727   1.00 66.81  ? 404 ILE D N   1 
ATOM   15990 C CA  . ILE D 1 404 ? 58.015  -3.465  4.908   1.00 67.49  ? 404 ILE D CA  1 
ATOM   15991 C C   . ILE D 1 404 ? 58.675  -3.050  6.210   1.00 69.16  ? 404 ILE D C   1 
ATOM   15992 O O   . ILE D 1 404 ? 58.344  -1.994  6.739   1.00 69.33  ? 404 ILE D O   1 
ATOM   15993 C CB  . ILE D 1 404 ? 58.932  -3.434  3.678   1.00 67.66  ? 404 ILE D CB  1 
ATOM   15994 C CG1 . ILE D 1 404 ? 59.518  -2.089  3.456   1.00 68.81  ? 404 ILE D CG1 1 
ATOM   15995 C CG2 . ILE D 1 404 ? 58.186  -3.912  2.433   1.00 66.44  ? 404 ILE D CG2 1 
ATOM   15996 C CD1 . ILE D 1 404 ? 60.670  -2.097  2.472   1.00 70.48  ? 404 ILE D CD1 1 
ATOM   15997 N N   . LEU D 1 405 ? 59.506  -3.940  6.762   1.00 70.83  ? 405 LEU D N   1 
ATOM   15998 C CA  . LEU D 1 405 ? 60.309  -3.632  7.933   1.00 72.53  ? 405 LEU D CA  1 
ATOM   15999 C C   . LEU D 1 405 ? 61.756  -3.855  7.527   1.00 72.86  ? 405 LEU D C   1 
ATOM   16000 O O   . LEU D 1 405 ? 62.158  -5.009  7.409   1.00 73.34  ? 405 LEU D O   1 
ATOM   16001 C CB  . LEU D 1 405 ? 59.931  -4.504  9.133   1.00 73.47  ? 405 LEU D CB  1 
ATOM   16002 C CG  . LEU D 1 405 ? 60.695  -4.212  10.433  1.00 75.54  ? 405 LEU D CG  1 
ATOM   16003 C CD1 . LEU D 1 405 ? 60.210  -2.896  11.030  1.00 75.28  ? 405 LEU D CD1 1 
ATOM   16004 C CD2 . LEU D 1 405 ? 60.603  -5.337  11.455  1.00 76.25  ? 405 LEU D CD2 1 
ATOM   16005 N N   . ALA D 1 406 ? 62.495  -2.750  7.337   1.00 72.76  ? 406 ALA D N   1 
ATOM   16006 C CA  . ALA D 1 406 ? 63.721  -2.742  6.543   1.00 73.51  ? 406 ALA D CA  1 
ATOM   16007 C C   . ALA D 1 406 ? 64.964  -2.513  7.403   1.00 73.96  ? 406 ALA D C   1 
ATOM   16008 O O   . ALA D 1 406 ? 64.877  -1.893  8.463   1.00 74.40  ? 406 ALA D O   1 
ATOM   16009 C CB  . ALA D 1 406 ? 63.595  -1.669  5.476   1.00 73.49  ? 406 ALA D CB  1 
ATOM   16010 N N   . SER D 1 407 ? 66.125  -2.976  6.924   1.00 74.06  ? 407 SER D N   1 
ATOM   16011 C CA  . SER D 1 407 ? 67.391  -2.552  7.521   1.00 75.52  ? 407 SER D CA  1 
ATOM   16012 C C   . SER D 1 407 ? 68.557  -2.818  6.584   1.00 76.74  ? 407 SER D C   1 
ATOM   16013 O O   . SER D 1 407 ? 68.427  -3.532  5.608   1.00 76.58  ? 407 SER D O   1 
ATOM   16014 C CB  . SER D 1 407 ? 67.649  -3.190  8.853   1.00 75.85  ? 407 SER D CB  1 
ATOM   16015 O OG  . SER D 1 407 ? 68.942  -2.847  9.331   1.00 77.55  ? 407 SER D OG  1 
ATOM   16016 N N   . LYS D 1 408 ? 69.711  -2.236  6.891   1.00 78.93  ? 408 LYS D N   1 
ATOM   16017 C CA  . LYS D 1 408 ? 70.873  -2.340  6.009   1.00 80.15  ? 408 LYS D CA  1 
ATOM   16018 C C   . LYS D 1 408 ? 71.659  -3.615  6.284   1.00 82.10  ? 408 LYS D C   1 
ATOM   16019 O O   . LYS D 1 408 ? 72.508  -3.966  5.462   1.00 83.49  ? 408 LYS D O   1 
ATOM   16020 C CB  . LYS D 1 408 ? 71.823  -1.142  6.097   1.00 80.85  ? 408 LYS D CB  1 
ATOM   16021 C CG  . LYS D 1 408 ? 71.136  0.180   5.862   1.00 79.10  ? 408 LYS D CG  1 
ATOM   16022 C CD  . LYS D 1 408 ? 72.060  1.318   5.451   1.00 80.19  ? 408 LYS D CD  1 
ATOM   16023 C CE  . LYS D 1 408 ? 71.579  2.661   5.957   1.00 79.25  ? 408 LYS D CE  1 
ATOM   16024 N NZ  . LYS D 1 408 ? 72.313  3.764   5.354   1.00 80.42  ? 408 LYS D NZ  1 
ATOM   16025 N N   . THR D 1 409 ? 71.367  -4.269  7.428   1.00 82.89  ? 409 THR D N   1 
ATOM   16026 C CA  . THR D 1 409 ? 71.820  -5.627  7.724   1.00 84.08  ? 409 THR D CA  1 
ATOM   16027 C C   . THR D 1 409 ? 70.767  -6.300  8.609   1.00 83.35  ? 409 THR D C   1 
ATOM   16028 O O   . THR D 1 409 ? 69.752  -5.705  8.971   1.00 81.97  ? 409 THR D O   1 
ATOM   16029 C CB  . THR D 1 409 ? 73.208  -5.562  8.378   1.00 86.77  ? 409 THR D CB  1 
ATOM   16030 O OG1 . THR D 1 409 ? 73.902  -6.808  8.266   1.00 87.09  ? 409 THR D OG1 1 
ATOM   16031 C CG2 . THR D 1 409 ? 73.132  -5.030  9.806   1.00 87.53  ? 409 THR D CG2 1 
ATOM   16032 N N   . ALA D 1 410 ? 71.040  -7.549  8.983   1.00 84.88  ? 410 ALA D N   1 
ATOM   16033 C CA  . ALA D 1 410 ? 70.070  -8.383  9.667   1.00 84.39  ? 410 ALA D CA  1 
ATOM   16034 C C   . ALA D 1 410 ? 69.899  -7.955  11.122  1.00 85.66  ? 410 ALA D C   1 
ATOM   16035 O O   . ALA D 1 410 ? 70.791  -7.352  11.703  1.00 87.81  ? 410 ALA D O   1 
ATOM   16036 C CB  . ALA D 1 410 ? 70.518  -9.809  9.574   1.00 85.45  ? 410 ALA D CB  1 
ATOM   16037 N N   . PHE D 1 411 ? 68.738  -8.301  11.694  1.00 85.29  ? 411 PHE D N   1 
ATOM   16038 C CA  . PHE D 1 411 ? 68.372  -7.963  13.062  1.00 85.18  ? 411 PHE D CA  1 
ATOM   16039 C C   . PHE D 1 411 ? 67.580  -9.115  13.684  1.00 86.37  ? 411 PHE D C   1 
ATOM   16040 O O   . PHE D 1 411 ? 66.936  -9.906  12.986  1.00 84.42  ? 411 PHE D O   1 
ATOM   16041 C CB  . PHE D 1 411 ? 67.569  -6.664  13.097  1.00 81.97  ? 411 PHE D CB  1 
ATOM   16042 C CG  . PHE D 1 411 ? 66.394  -6.628  12.132  1.00 79.13  ? 411 PHE D CG  1 
ATOM   16043 C CD1 . PHE D 1 411 ? 66.578  -6.346  10.779  1.00 78.07  ? 411 PHE D CD1 1 
ATOM   16044 C CD2 . PHE D 1 411 ? 65.080  -6.846  12.582  1.00 77.33  ? 411 PHE D CD2 1 
ATOM   16045 C CE1 . PHE D 1 411 ? 65.477  -6.300  9.913   1.00 75.85  ? 411 PHE D CE1 1 
ATOM   16046 C CE2 . PHE D 1 411 ? 63.992  -6.791  11.716  1.00 74.29  ? 411 PHE D CE2 1 
ATOM   16047 C CZ  . PHE D 1 411 ? 64.191  -6.528  10.384  1.00 73.79  ? 411 PHE D CZ  1 
ATOM   16048 N N   . GLU D 1 412 ? 67.644  -9.160  15.019  1.00 89.38  ? 412 GLU D N   1 
ATOM   16049 C CA  . GLU D 1 412 ? 66.976  -10.151 15.842  1.00 90.79  ? 412 GLU D CA  1 
ATOM   16050 C C   . GLU D 1 412 ? 65.480  -9.876  15.932  1.00 87.71  ? 412 GLU D C   1 
ATOM   16051 O O   . GLU D 1 412 ? 65.086  -8.901  16.551  1.00 88.07  ? 412 GLU D O   1 
ATOM   16052 C CB  . GLU D 1 412 ? 67.557  -10.018 17.249  1.00 96.55  ? 412 GLU D CB  1 
ATOM   16053 C CG  . GLU D 1 412 ? 66.902  -10.920 18.296  1.00 101.27 ? 412 GLU D CG  1 
ATOM   16054 C CD  . GLU D 1 412 ? 67.690  -11.026 19.603  1.00 108.99 ? 412 GLU D CD  1 
ATOM   16055 O OE1 . GLU D 1 412 ? 68.632  -11.878 19.768  1.00 109.95 ? 412 GLU D OE1 1 
ATOM   16056 O OE2 . GLU D 1 412 ? 67.336  -10.174 20.466  1.00 112.31 ? 412 GLU D OE2 1 
ATOM   16057 N N   . LEU D 1 413 ? 64.657  -10.770 15.375  1.00 85.69  ? 413 LEU D N   1 
ATOM   16058 C CA  . LEU D 1 413 ? 63.217  -10.769 15.598  1.00 83.00  ? 413 LEU D CA  1 
ATOM   16059 C C   . LEU D 1 413 ? 62.894  -11.477 16.908  1.00 83.22  ? 413 LEU D C   1 
ATOM   16060 O O   . LEU D 1 413 ? 63.678  -12.304 17.358  1.00 85.68  ? 413 LEU D O   1 
ATOM   16061 C CB  . LEU D 1 413 ? 62.545  -11.489 14.432  1.00 80.75  ? 413 LEU D CB  1 
ATOM   16062 C CG  . LEU D 1 413 ? 62.763  -10.852 13.058  1.00 80.00  ? 413 LEU D CG  1 
ATOM   16063 C CD1 . LEU D 1 413 ? 62.383  -11.743 11.895  1.00 78.64  ? 413 LEU D CD1 1 
ATOM   16064 C CD2 . LEU D 1 413 ? 61.987  -9.555  13.002  1.00 78.83  ? 413 LEU D CD2 1 
ATOM   16065 N N   . PRO D 1 414 ? 61.736  -11.200 17.553  1.00 81.85  ? 414 PRO D N   1 
ATOM   16066 C CA  . PRO D 1 414 ? 61.200  -12.110 18.565  1.00 81.37  ? 414 PRO D CA  1 
ATOM   16067 C C   . PRO D 1 414 ? 60.719  -13.385 17.883  1.00 79.26  ? 414 PRO D C   1 
ATOM   16068 O O   . PRO D 1 414 ? 60.504  -13.446 16.677  1.00 76.58  ? 414 PRO D O   1 
ATOM   16069 C CB  . PRO D 1 414 ? 60.082  -11.325 19.243  1.00 81.42  ? 414 PRO D CB  1 
ATOM   16070 C CG  . PRO D 1 414 ? 59.698  -10.231 18.249  1.00 79.82  ? 414 PRO D CG  1 
ATOM   16071 C CD  . PRO D 1 414 ? 60.896  -10.011 17.344  1.00 80.55  ? 414 PRO D CD  1 
ATOM   16072 N N   . GLU D 1 415 ? 60.594  -14.456 18.644  1.00 80.89  ? 415 GLU D N   1 
ATOM   16073 C CA  . GLU D 1 415 ? 60.224  -15.699 17.990  1.00 81.28  ? 415 GLU D CA  1 
ATOM   16074 C C   . GLU D 1 415 ? 59.390  -16.570 18.920  1.00 79.89  ? 415 GLU D C   1 
ATOM   16075 O O   . GLU D 1 415 ? 59.621  -16.608 20.129  1.00 80.63  ? 415 GLU D O   1 
ATOM   16076 C CB  . GLU D 1 415 ? 61.450  -16.408 17.408  1.00 84.43  ? 415 GLU D CB  1 
ATOM   16077 C CG  . GLU D 1 415 ? 62.522  -16.818 18.412  1.00 88.61  ? 415 GLU D CG  1 
ATOM   16078 C CD  . GLU D 1 415 ? 63.290  -18.020 17.896  1.00 91.98  ? 415 GLU D CD  1 
ATOM   16079 O OE1 . GLU D 1 415 ? 63.342  -18.173 16.654  1.00 92.73  ? 415 GLU D OE1 1 
ATOM   16080 O OE2 . GLU D 1 415 ? 63.756  -18.843 18.715  1.00 95.12  ? 415 GLU D OE2 1 
ATOM   16081 N N   . LEU D 1 416 ? 58.394  -17.229 18.317  1.00 77.10  ? 416 LEU D N   1 
ATOM   16082 C CA  . LEU D 1 416 ? 57.499  -18.096 19.048  1.00 76.47  ? 416 LEU D CA  1 
ATOM   16083 C C   . LEU D 1 416 ? 57.730  -19.506 18.525  1.00 76.28  ? 416 LEU D C   1 
ATOM   16084 O O   . LEU D 1 416 ? 57.812  -19.735 17.316  1.00 74.90  ? 416 LEU D O   1 
ATOM   16085 C CB  . LEU D 1 416 ? 56.071  -17.581 18.841  1.00 74.75  ? 416 LEU D CB  1 
ATOM   16086 C CG  . LEU D 1 416 ? 54.955  -18.193 19.704  1.00 74.95  ? 416 LEU D CG  1 
ATOM   16087 C CD1 . LEU D 1 416 ? 53.758  -17.271 19.800  1.00 73.79  ? 416 LEU D CD1 1 
ATOM   16088 C CD2 . LEU D 1 416 ? 54.471  -19.534 19.178  1.00 74.39  ? 416 LEU D CD2 1 
ATOM   16089 N N   . THR D 1 417 ? 57.887  -20.447 19.453  1.00 78.05  ? 417 THR D N   1 
ATOM   16090 C CA  . THR D 1 417 ? 57.927  -21.860 19.096  1.00 78.52  ? 417 THR D CA  1 
ATOM   16091 C C   . THR D 1 417 ? 57.004  -22.604 20.059  1.00 79.82  ? 417 THR D C   1 
ATOM   16092 O O   . THR D 1 417 ? 56.692  -22.088 21.133  1.00 80.58  ? 417 THR D O   1 
ATOM   16093 C CB  . THR D 1 417 ? 59.370  -22.385 19.121  1.00 79.54  ? 417 THR D CB  1 
ATOM   16094 O OG1 . THR D 1 417 ? 59.789  -22.341 20.480  1.00 80.83  ? 417 THR D OG1 1 
ATOM   16095 C CG2 . THR D 1 417 ? 60.321  -21.570 18.259  1.00 78.95  ? 417 THR D CG2 1 
ATOM   16096 N N   . ILE D 1 418 ? 56.562  -23.799 19.660  1.00 80.61  ? 418 ILE D N   1 
ATOM   16097 C CA  . ILE D 1 418 ? 55.703  -24.621 20.495  1.00 82.20  ? 418 ILE D CA  1 
ATOM   16098 C C   . ILE D 1 418 ? 56.240  -26.050 20.533  1.00 84.84  ? 418 ILE D C   1 
ATOM   16099 O O   . ILE D 1 418 ? 57.036  -26.437 19.678  1.00 86.38  ? 418 ILE D O   1 
ATOM   16100 C CB  . ILE D 1 418 ? 54.256  -24.590 19.982  1.00 80.34  ? 418 ILE D CB  1 
ATOM   16101 C CG1 . ILE D 1 418 ? 54.145  -25.023 18.511  1.00 79.20  ? 418 ILE D CG1 1 
ATOM   16102 C CG2 . ILE D 1 418 ? 53.647  -23.216 20.215  1.00 79.64  ? 418 ILE D CG2 1 
ATOM   16103 C CD1 . ILE D 1 418 ? 52.726  -24.985 17.946  1.00 77.56  ? 418 ILE D CD1 1 
ATOM   16104 N N   . GLU D 1 419 ? 55.777  -26.818 21.532  1.00 85.80  ? 419 GLU D N   1 
ATOM   16105 C CA  . GLU D 1 419 ? 56.145  -28.209 21.724  1.00 86.46  ? 419 GLU D CA  1 
ATOM   16106 C C   . GLU D 1 419 ? 54.866  -28.953 22.091  1.00 87.08  ? 419 GLU D C   1 
ATOM   16107 O O   . GLU D 1 419 ? 54.200  -28.593 23.060  1.00 88.14  ? 419 GLU D O   1 
ATOM   16108 C CB  . GLU D 1 419 ? 57.194  -28.300 22.831  1.00 88.28  ? 419 GLU D CB  1 
ATOM   16109 C CG  . GLU D 1 419 ? 58.617  -27.972 22.389  1.00 88.78  ? 419 GLU D CG  1 
ATOM   16110 C CD  . GLU D 1 419 ? 59.629  -28.126 23.517  1.00 91.93  ? 419 GLU D CD  1 
ATOM   16111 O OE1 . GLU D 1 419 ? 59.466  -27.421 24.540  1.00 92.57  ? 419 GLU D OE1 1 
ATOM   16112 O OE2 . GLU D 1 419 ? 60.573  -28.953 23.405  1.00 94.18  ? 419 GLU D OE2 1 
ATOM   16113 N N   . VAL D 1 420 ? 54.502  -29.964 21.302  1.00 86.35  ? 420 VAL D N   1 
ATOM   16114 C CA  . VAL D 1 420 ? 53.153  -30.489 21.372  1.00 86.50  ? 420 VAL D CA  1 
ATOM   16115 C C   . VAL D 1 420 ? 53.185  -31.912 21.909  1.00 89.68  ? 420 VAL D C   1 
ATOM   16116 O O   . VAL D 1 420 ? 54.087  -32.685 21.597  1.00 91.88  ? 420 VAL D O   1 
ATOM   16117 C CB  . VAL D 1 420 ? 52.502  -30.432 19.981  1.00 84.54  ? 420 VAL D CB  1 
ATOM   16118 C CG1 . VAL D 1 420 ? 51.003  -30.685 20.055  1.00 83.53  ? 420 VAL D CG1 1 
ATOM   16119 C CG2 . VAL D 1 420 ? 52.765  -29.097 19.293  1.00 83.60  ? 420 VAL D CG2 1 
ATOM   16120 N N   . THR D 1 421 ? 52.177  -32.264 22.709  1.00 90.48  ? 421 THR D N   1 
ATOM   16121 C CA  . THR D 1 421 ? 52.046  -33.634 23.167  1.00 92.08  ? 421 THR D CA  1 
ATOM   16122 C C   . THR D 1 421 ? 50.694  -34.173 22.702  1.00 90.76  ? 421 THR D C   1 
ATOM   16123 O O   . THR D 1 421 ? 49.711  -33.444 22.700  1.00 89.22  ? 421 THR D O   1 
ATOM   16124 C CB  . THR D 1 421 ? 52.210  -33.670 24.683  1.00 94.57  ? 421 THR D CB  1 
ATOM   16125 O OG1 . THR D 1 421 ? 53.562  -33.294 24.909  1.00 95.06  ? 421 THR D OG1 1 
ATOM   16126 C CG2 . THR D 1 421 ? 52.037  -35.064 25.256  1.00 97.44  ? 421 THR D CG2 1 
ATOM   16127 N N   . PRO D 1 422 ? 50.590  -35.423 22.198  1.00 90.12  ? 422 PRO D N   1 
ATOM   16128 C CA  . PRO D 1 422 ? 51.721  -36.184 21.663  1.00 90.41  ? 422 PRO D CA  1 
ATOM   16129 C C   . PRO D 1 422 ? 52.437  -35.555 20.470  1.00 89.18  ? 422 PRO D C   1 
ATOM   16130 O O   . PRO D 1 422 ? 51.781  -35.083 19.548  1.00 88.86  ? 422 PRO D O   1 
ATOM   16131 C CB  . PRO D 1 422 ? 51.018  -37.479 21.224  1.00 90.74  ? 422 PRO D CB  1 
ATOM   16132 C CG  . PRO D 1 422 ? 49.810  -37.580 22.107  1.00 91.39  ? 422 PRO D CG  1 
ATOM   16133 C CD  . PRO D 1 422 ? 49.326  -36.164 22.150  1.00 89.95  ? 422 PRO D CD  1 
ATOM   16134 N N   . GLU D 1 423 ? 53.774  -35.626 20.461  1.00 90.39  ? 423 GLU D N   1 
ATOM   16135 C CA  . GLU D 1 423 ? 54.616  -35.084 19.402  1.00 90.04  ? 423 GLU D CA  1 
ATOM   16136 C C   . GLU D 1 423 ? 54.382  -35.759 18.051  1.00 88.45  ? 423 GLU D C   1 
ATOM   16137 O O   . GLU D 1 423 ? 54.133  -35.090 17.061  1.00 85.34  ? 423 GLU D O   1 
ATOM   16138 C CB  . GLU D 1 423 ? 56.095  -35.271 19.742  1.00 93.57  ? 423 GLU D CB  1 
ATOM   16139 C CG  . GLU D 1 423 ? 57.028  -34.454 18.852  1.00 94.26  ? 423 GLU D CG  1 
ATOM   16140 C CD  . GLU D 1 423 ? 58.496  -34.767 19.054  1.00 98.86  ? 423 GLU D CD  1 
ATOM   16141 O OE1 . GLU D 1 423 ? 58.815  -35.832 19.626  1.00 102.12 ? 423 GLU D OE1 1 
ATOM   16142 O OE2 . GLU D 1 423 ? 59.327  -33.936 18.648  1.00 100.86 ? 423 GLU D OE2 1 
ATOM   16143 N N   . LYS D 1 424 ? 54.501  -37.088 17.987  1.00 91.24  ? 424 LYS D N   1 
ATOM   16144 C CA  . LYS D 1 424 ? 54.560  -37.769 16.702  1.00 91.01  ? 424 LYS D CA  1 
ATOM   16145 C C   . LYS D 1 424 ? 53.241  -38.462 16.358  1.00 88.90  ? 424 LYS D C   1 
ATOM   16146 O O   . LYS D 1 424 ? 52.732  -38.301 15.245  1.00 88.18  ? 424 LYS D O   1 
ATOM   16147 C CB  . LYS D 1 424 ? 55.779  -38.684 16.763  1.00 95.69  ? 424 LYS D CB  1 
ATOM   16148 C CG  . LYS D 1 424 ? 57.084  -37.927 17.035  1.00 99.79  ? 424 LYS D CG  1 
ATOM   16149 C CD  . LYS D 1 424 ? 58.193  -38.765 17.676  1.00 104.58 ? 424 LYS D CD  1 
ATOM   16150 C CE  . LYS D 1 424 ? 59.543  -38.175 17.427  1.00 106.43 ? 424 LYS D CE  1 
ATOM   16151 N NZ  . LYS D 1 424 ? 59.943  -38.457 16.046  1.00 106.87 ? 424 LYS D NZ  1 
ATOM   16152 N N   . ASP D 1 425 ? 52.657  -39.189 17.315  1.00 88.11  ? 425 ASP D N   1 
ATOM   16153 C CA  . ASP D 1 425 ? 51.562  -40.091 16.999  1.00 86.73  ? 425 ASP D CA  1 
ATOM   16154 C C   . ASP D 1 425 ? 50.455  -39.993 18.044  1.00 86.30  ? 425 ASP D C   1 
ATOM   16155 O O   . ASP D 1 425 ? 50.652  -40.414 19.183  1.00 89.50  ? 425 ASP D O   1 
ATOM   16156 C CB  . ASP D 1 425 ? 52.061  -41.523 16.957  1.00 88.35  ? 425 ASP D CB  1 
ATOM   16157 C CG  . ASP D 1 425 ? 50.979  -42.558 16.725  1.00 88.34  ? 425 ASP D CG  1 
ATOM   16158 O OD1 . ASP D 1 425 ? 49.811  -42.129 16.587  1.00 87.11  ? 425 ASP D OD1 1 
ATOM   16159 O OD2 . ASP D 1 425 ? 51.324  -43.768 16.662  1.00 89.78  ? 425 ASP D OD2 1 
ATOM   16160 N N   . LEU D 1 426 ? 49.260  -39.577 17.606  1.00 82.88  ? 426 LEU D N   1 
ATOM   16161 C CA  . LEU D 1 426 ? 48.161  -39.237 18.498  1.00 82.04  ? 426 LEU D CA  1 
ATOM   16162 C C   . LEU D 1 426 ? 47.709  -40.429 19.344  1.00 83.66  ? 426 LEU D C   1 
ATOM   16163 O O   . LEU D 1 426 ? 47.147  -40.222 20.419  1.00 83.95  ? 426 LEU D O   1 
ATOM   16164 C CB  . LEU D 1 426 ? 47.012  -38.635 17.680  1.00 79.73  ? 426 LEU D CB  1 
ATOM   16165 C CG  . LEU D 1 426 ? 47.263  -37.243 17.060  1.00 77.60  ? 426 LEU D CG  1 
ATOM   16166 C CD1 . LEU D 1 426 ? 46.000  -36.669 16.427  1.00 75.65  ? 426 LEU D CD1 1 
ATOM   16167 C CD2 . LEU D 1 426 ? 47.843  -36.219 18.027  1.00 77.68  ? 426 LEU D CD2 1 
ATOM   16168 N N   . ASN D 1 427 ? 47.978  -41.665 18.882  1.00 84.54  ? 427 ASN D N   1 
ATOM   16169 C CA  . ASN D 1 427 ? 47.557  -42.856 19.607  1.00 86.61  ? 427 ASN D CA  1 
ATOM   16170 C C   . ASN D 1 427 ? 48.155  -42.885 21.012  1.00 89.30  ? 427 ASN D C   1 
ATOM   16171 O O   . ASN D 1 427 ? 47.654  -43.608 21.869  1.00 90.92  ? 427 ASN D O   1 
ATOM   16172 C CB  . ASN D 1 427 ? 47.897  -44.163 18.894  1.00 87.26  ? 427 ASN D CB  1 
ATOM   16173 C CG  . ASN D 1 427 ? 46.897  -44.555 17.830  1.00 85.68  ? 427 ASN D CG  1 
ATOM   16174 O OD1 . ASN D 1 427 ? 45.689  -44.563 18.082  1.00 85.29  ? 427 ASN D OD1 1 
ATOM   16175 N ND2 . ASN D 1 427 ? 47.370  -44.928 16.649  1.00 84.95  ? 427 ASN D ND2 1 
ATOM   16176 N N   . GLU D 1 428 ? 49.219  -42.110 21.241  1.00 90.40  ? 428 GLU D N   1 
ATOM   16177 C CA  . GLU D 1 428 ? 49.962  -42.164 22.491  1.00 93.79  ? 428 GLU D CA  1 
ATOM   16178 C C   . GLU D 1 428 ? 49.186  -41.589 23.674  1.00 94.63  ? 428 GLU D C   1 
ATOM   16179 O O   . GLU D 1 428 ? 49.531  -41.870 24.816  1.00 97.17  ? 428 GLU D O   1 
ATOM   16180 C CB  . GLU D 1 428 ? 51.210  -41.294 22.438  1.00 94.46  ? 428 GLU D CB  1 
ATOM   16181 C CG  . GLU D 1 428 ? 52.417  -41.959 21.798  1.00 95.82  ? 428 GLU D CG  1 
ATOM   16182 C CD  . GLU D 1 428 ? 53.561  -40.955 21.821  1.00 96.82  ? 428 GLU D CD  1 
ATOM   16183 O OE1 . GLU D 1 428 ? 53.344  -39.684 21.941  1.00 93.95  ? 428 GLU D OE1 1 
ATOM   16184 O OE2 . GLU D 1 428 ? 54.696  -41.512 21.747  1.00 98.47  ? 428 GLU D OE2 1 
ATOM   16185 N N   . GLY D 1 429 ? 48.202  -40.728 23.415  1.00 92.74  ? 429 GLY D N   1 
ATOM   16186 C CA  . GLY D 1 429 ? 47.396  -40.194 24.495  1.00 93.98  ? 429 GLY D CA  1 
ATOM   16187 C C   . GLY D 1 429 ? 45.959  -39.959 24.044  1.00 93.09  ? 429 GLY D C   1 
ATOM   16188 O O   . GLY D 1 429 ? 45.666  -39.963 22.845  1.00 90.50  ? 429 GLY D O   1 
ATOM   16189 N N   . LYS D 1 430 ? 45.075  -39.799 25.037  1.00 95.04  ? 430 LYS D N   1 
ATOM   16190 C CA  . LYS D 1 430 ? 43.748  -39.251 24.810  1.00 94.42  ? 430 LYS D CA  1 
ATOM   16191 C C   . LYS D 1 430 ? 43.731  -37.755 25.140  1.00 91.89  ? 430 LYS D C   1 
ATOM   16192 O O   . LYS D 1 430 ? 42.738  -37.090 24.854  1.00 90.02  ? 430 LYS D O   1 
ATOM   16193 C CB  . LYS D 1 430 ? 42.700  -40.042 25.604  1.00 97.84  ? 430 LYS D CB  1 
ATOM   16194 C CG  . LYS D 1 430 ? 42.492  -41.455 25.096  1.00 101.52 ? 430 LYS D CG  1 
ATOM   16195 C CD  . LYS D 1 430 ? 41.501  -42.313 25.876  1.00 105.11 ? 430 LYS D CD  1 
ATOM   16196 C CE  . LYS D 1 430 ? 40.133  -41.716 25.856  1.00 105.38 ? 430 LYS D CE  1 
ATOM   16197 N NZ  . LYS D 1 430 ? 39.204  -42.648 26.496  1.00 108.05 ? 430 LYS D NZ  1 
ATOM   16198 N N   . ILE D 1 431 ? 44.810  -37.233 25.749  1.00 92.01  ? 431 ILE D N   1 
ATOM   16199 C CA  . ILE D 1 431 ? 44.933  -35.808 26.055  1.00 90.96  ? 431 ILE D CA  1 
ATOM   16200 C C   . ILE D 1 431 ? 46.189  -35.264 25.376  1.00 90.21  ? 431 ILE D C   1 
ATOM   16201 O O   . ILE D 1 431 ? 47.216  -35.936 25.333  1.00 93.07  ? 431 ILE D O   1 
ATOM   16202 C CB  . ILE D 1 431 ? 44.982  -35.548 27.573  1.00 92.31  ? 431 ILE D CB  1 
ATOM   16203 C CG1 . ILE D 1 431 ? 43.855  -36.237 28.332  1.00 93.67  ? 431 ILE D CG1 1 
ATOM   16204 C CG2 . ILE D 1 431 ? 44.993  -34.050 27.850  1.00 91.26  ? 431 ILE D CG2 1 
ATOM   16205 C CD1 . ILE D 1 431 ? 44.077  -36.302 29.832  1.00 96.24  ? 431 ILE D CD1 1 
ATOM   16206 N N   . ALA D 1 432 ? 46.100  -34.042 24.853  1.00 88.01  ? 432 ALA D N   1 
ATOM   16207 C CA  . ALA D 1 432 ? 47.233  -33.367 24.244  1.00 87.00  ? 432 ALA D CA  1 
ATOM   16208 C C   . ALA D 1 432 ? 47.543  -32.095 25.025  1.00 87.24  ? 432 ALA D C   1 
ATOM   16209 O O   . ALA D 1 432 ? 46.672  -31.575 25.717  1.00 87.67  ? 432 ALA D O   1 
ATOM   16210 C CB  . ALA D 1 432 ? 46.910  -33.038 22.805  1.00 84.58  ? 432 ALA D CB  1 
ATOM   16211 N N   . SER D 1 433 ? 48.776  -31.589 24.887  1.00 87.13  ? 433 SER D N   1 
ATOM   16212 C CA  . SER D 1 433 ? 49.133  -30.279 25.410  1.00 86.62  ? 433 SER D CA  1 
ATOM   16213 C C   . SER D 1 433 ? 49.884  -29.508 24.330  1.00 84.79  ? 433 SER D C   1 
ATOM   16214 O O   . SER D 1 433 ? 50.518  -30.133 23.472  1.00 84.31  ? 433 SER D O   1 
ATOM   16215 C CB  . SER D 1 433 ? 49.948  -30.386 26.686  1.00 89.25  ? 433 SER D CB  1 
ATOM   16216 O OG  . SER D 1 433 ? 51.334  -30.613 26.443  1.00 90.17  ? 433 SER D OG  1 
ATOM   16217 N N   . ILE D 1 434 ? 49.770  -28.166 24.379  1.00 83.43  ? 434 ILE D N   1 
ATOM   16218 C CA  . ILE D 1 434 ? 50.659  -27.262 23.659  1.00 82.25  ? 434 ILE D CA  1 
ATOM   16219 C C   . ILE D 1 434 ? 51.375  -26.355 24.661  1.00 84.12  ? 434 ILE D C   1 
ATOM   16220 O O   . ILE D 1 434 ? 50.733  -25.555 25.347  1.00 84.90  ? 434 ILE D O   1 
ATOM   16221 C CB  . ILE D 1 434 ? 49.895  -26.455 22.595  1.00 79.43  ? 434 ILE D CB  1 
ATOM   16222 C CG1 . ILE D 1 434 ? 49.265  -27.394 21.572  1.00 78.37  ? 434 ILE D CG1 1 
ATOM   16223 C CG2 . ILE D 1 434 ? 50.773  -25.380 21.930  1.00 78.00  ? 434 ILE D CG2 1 
ATOM   16224 C CD1 . ILE D 1 434 ? 48.411  -26.693 20.524  1.00 76.40  ? 434 ILE D CD1 1 
ATOM   16225 N N   . LYS D 1 435 ? 52.709  -26.501 24.724  1.00 85.48  ? 435 LYS D N   1 
ATOM   16226 C CA  . LYS D 1 435 ? 53.579  -25.615 25.480  1.00 87.03  ? 435 LYS D CA  1 
ATOM   16227 C C   . LYS D 1 435 ? 54.123  -24.535 24.547  1.00 85.41  ? 435 LYS D C   1 
ATOM   16228 O O   . LYS D 1 435 ? 54.891  -24.824 23.632  1.00 84.91  ? 435 LYS D O   1 
ATOM   16229 C CB  . LYS D 1 435 ? 54.740  -26.401 26.105  1.00 90.00  ? 435 LYS D CB  1 
ATOM   16230 C CG  . LYS D 1 435 ? 54.348  -27.445 27.161  1.00 91.95  ? 435 LYS D CG  1 
ATOM   16231 C CD  . LYS D 1 435 ? 55.491  -27.937 28.041  1.00 94.70  ? 435 LYS D CD  1 
ATOM   16232 C CE  . LYS D 1 435 ? 56.495  -28.739 27.264  1.00 95.63  ? 435 LYS D CE  1 
ATOM   16233 N NZ  . LYS D 1 435 ? 57.631  -29.195 28.069  1.00 98.71  ? 435 LYS D NZ  1 
ATOM   16234 N N   . THR D 1 436 ? 53.726  -23.284 24.804  1.00 85.32  ? 436 THR D N   1 
ATOM   16235 C CA  . THR D 1 436 ? 54.089  -22.144 23.969  1.00 83.57  ? 436 THR D CA  1 
ATOM   16236 C C   . THR D 1 436 ? 55.292  -21.417 24.572  1.00 83.48  ? 436 THR D C   1 
ATOM   16237 O O   . THR D 1 436 ? 55.325  -21.214 25.782  1.00 84.91  ? 436 THR D O   1 
ATOM   16238 C CB  . THR D 1 436 ? 52.865  -21.237 23.850  1.00 83.24  ? 436 THR D CB  1 
ATOM   16239 O OG1 . THR D 1 436 ? 51.712  -22.052 23.599  1.00 82.71  ? 436 THR D OG1 1 
ATOM   16240 C CG2 . THR D 1 436 ? 53.070  -20.188 22.770  1.00 82.46  ? 436 THR D CG2 1 
ATOM   16241 N N   . LYS D 1 437 ? 56.278  -21.050 23.729  1.00 82.04  ? 437 LYS D N   1 
ATOM   16242 C CA  . LYS D 1 437 ? 57.495  -20.378 24.186  1.00 82.80  ? 437 LYS D CA  1 
ATOM   16243 C C   . LYS D 1 437 ? 57.846  -19.190 23.291  1.00 80.84  ? 437 LYS D C   1 
ATOM   16244 O O   . LYS D 1 437 ? 58.107  -19.352 22.102  1.00 79.02  ? 437 LYS D O   1 
ATOM   16245 C CB  . LYS D 1 437 ? 58.707  -21.312 24.218  1.00 84.34  ? 437 LYS D CB  1 
ATOM   16246 C CG  . LYS D 1 437 ? 59.977  -20.667 24.752  1.00 86.14  ? 437 LYS D CG  1 
ATOM   16247 C CD  . LYS D 1 437 ? 61.173  -21.602 24.801  1.00 88.20  ? 437 LYS D CD  1 
ATOM   16248 C CE  . LYS D 1 437 ? 62.379  -21.010 25.438  1.00 90.27  ? 437 LYS D CE  1 
ATOM   16249 N NZ  . LYS D 1 437 ? 63.501  -21.948 25.358  1.00 92.05  ? 437 LYS D NZ  1 
ATOM   16250 N N   . ILE D 1 438 ? 57.887  -18.001 23.902  1.00 81.64  ? 438 ILE D N   1 
ATOM   16251 C CA  . ILE D 1 438 ? 58.086  -16.746 23.192  1.00 81.10  ? 438 ILE D CA  1 
ATOM   16252 C C   . ILE D 1 438 ? 59.344  -16.068 23.712  1.00 83.33  ? 438 ILE D C   1 
ATOM   16253 O O   . ILE D 1 438 ? 59.445  -15.779 24.908  1.00 84.63  ? 438 ILE D O   1 
ATOM   16254 C CB  . ILE D 1 438 ? 56.898  -15.788 23.366  1.00 80.03  ? 438 ILE D CB  1 
ATOM   16255 C CG1 . ILE D 1 438 ? 55.576  -16.431 22.992  1.00 78.76  ? 438 ILE D CG1 1 
ATOM   16256 C CG2 . ILE D 1 438 ? 57.132  -14.500 22.576  1.00 79.10  ? 438 ILE D CG2 1 
ATOM   16257 C CD1 . ILE D 1 438 ? 54.381  -15.556 23.321  1.00 77.92  ? 438 ILE D CD1 1 
ATOM   16258 N N   . GLU D 1 439 ? 60.257  -15.779 22.776  1.00 83.99  ? 439 GLU D N   1 
ATOM   16259 C CA  . GLU D 1 439 ? 61.510  -15.109 23.070  1.00 86.37  ? 439 GLU D CA  1 
ATOM   16260 C C   . GLU D 1 439 ? 61.402  -13.650 22.664  1.00 85.32  ? 439 GLU D C   1 
ATOM   16261 O O   . GLU D 1 439 ? 61.134  -13.349 21.499  1.00 83.17  ? 439 GLU D O   1 
ATOM   16262 C CB  . GLU D 1 439 ? 62.650  -15.717 22.261  1.00 88.32  ? 439 GLU D CB  1 
ATOM   16263 C CG  . GLU D 1 439 ? 63.109  -17.090 22.751  1.00 90.48  ? 439 GLU D CG  1 
ATOM   16264 C CD  . GLU D 1 439 ? 64.586  -17.279 22.478  1.00 93.33  ? 439 GLU D CD  1 
ATOM   16265 O OE1 . GLU D 1 439 ? 65.195  -16.382 21.825  1.00 94.10  ? 439 GLU D OE1 1 
ATOM   16266 O OE2 . GLU D 1 439 ? 65.130  -18.307 22.949  1.00 97.25  ? 439 GLU D OE2 1 
ATOM   16267 N N   . THR D 1 440 ? 61.607  -12.761 23.638  1.00 87.05  ? 440 THR D N   1 
ATOM   16268 C CA  . THR D 1 440 ? 61.357  -11.347 23.436  1.00 86.63  ? 440 THR D CA  1 
ATOM   16269 C C   . THR D 1 440 ? 62.636  -10.698 22.933  1.00 89.16  ? 440 THR D C   1 
ATOM   16270 O O   . THR D 1 440 ? 63.731  -11.094 23.320  1.00 91.73  ? 440 THR D O   1 
ATOM   16271 C CB  . THR D 1 440 ? 60.890  -10.683 24.731  1.00 87.29  ? 440 THR D CB  1 
ATOM   16272 O OG1 . THR D 1 440 ? 61.912  -10.858 25.706  1.00 89.54  ? 440 THR D OG1 1 
ATOM   16273 C CG2 . THR D 1 440 ? 59.597  -11.279 25.254  1.00 86.56  ? 440 THR D CG2 1 
ATOM   16274 N N   . SER D 1 441 ? 62.471  -9.712  22.054  1.00 90.10  ? 441 SER D N   1 
ATOM   16275 C CA  . SER D 1 441 ? 63.510  -8.739  21.749  1.00 92.17  ? 441 SER D CA  1 
ATOM   16276 C C   . SER D 1 441 ? 63.020  -7.377  22.235  1.00 92.24  ? 441 SER D C   1 
ATOM   16277 O O   . SER D 1 441 ? 61.814  -7.153  22.264  1.00 92.10  ? 441 SER D O   1 
ATOM   16278 C CB  . SER D 1 441 ? 63.811  -8.722  20.264  1.00 91.56  ? 441 SER D CB  1 
ATOM   16279 O OG  . SER D 1 441 ? 63.714  -10.018 19.683  1.00 90.77  ? 441 SER D OG  1 
ATOM   16280 N N   . GLU D 1 442 ? 63.928  -6.483  22.635  1.00 93.82  ? 442 GLU D N   1 
ATOM   16281 C CA  . GLU D 1 442 ? 63.509  -5.148  23.043  1.00 95.30  ? 442 GLU D CA  1 
ATOM   16282 C C   . GLU D 1 442 ? 63.211  -4.310  21.800  1.00 93.74  ? 442 GLU D C   1 
ATOM   16283 O O   . GLU D 1 442 ? 63.867  -4.446  20.774  1.00 93.65  ? 442 GLU D O   1 
ATOM   16284 C CB  . GLU D 1 442 ? 64.537  -4.439  23.927  1.00 98.42  ? 442 GLU D CB  1 
ATOM   16285 C CG  . GLU D 1 442 ? 65.878  -4.204  23.232  1.00 99.32  ? 442 GLU D CG  1 
ATOM   16286 C CD  . GLU D 1 442 ? 67.080  -4.139  24.154  1.00 101.84 ? 442 GLU D CD  1 
ATOM   16287 O OE1 . GLU D 1 442 ? 67.189  -3.112  24.855  1.00 103.29 ? 442 GLU D OE1 1 
ATOM   16288 O OE2 . GLU D 1 442 ? 67.895  -5.097  24.171  1.00 101.14 ? 442 GLU D OE2 1 
ATOM   16289 N N   . ASN D 1 443 ? 62.178  -3.473  21.889  1.00 93.20  ? 443 ASN D N   1 
ATOM   16290 C CA  . ASN D 1 443 ? 61.832  -2.543  20.824  1.00 92.01  ? 443 ASN D CA  1 
ATOM   16291 C C   . ASN D 1 443 ? 60.822  -3.158  19.865  1.00 88.02  ? 443 ASN D C   1 
ATOM   16292 O O   . ASN D 1 443 ? 60.253  -2.436  19.051  1.00 88.49  ? 443 ASN D O   1 
ATOM   16293 C CB  . ASN D 1 443 ? 63.045  -2.026  20.049  1.00 93.34  ? 443 ASN D CB  1 
ATOM   16294 C CG  . ASN D 1 443 ? 63.794  -0.964  20.816  1.00 93.49  ? 443 ASN D CG  1 
ATOM   16295 O OD1 . ASN D 1 443 ? 63.294  0.150   21.013  1.00 93.33  ? 443 ASN D OD1 1 
ATOM   16296 N ND2 . ASN D 1 443 ? 64.985  -1.295  21.264  1.00 95.38  ? 443 ASN D ND2 1 
ATOM   16297 N N   . PHE D 1 444 ? 60.607  -4.468  19.950  1.00 85.05  ? 444 PHE D N   1 
ATOM   16298 C CA  . PHE D 1 444 ? 59.435  -5.065  19.342  1.00 82.89  ? 444 PHE D CA  1 
ATOM   16299 C C   . PHE D 1 444 ? 58.421  -5.352  20.440  1.00 83.25  ? 444 PHE D C   1 
ATOM   16300 O O   . PHE D 1 444 ? 58.734  -6.020  21.412  1.00 86.38  ? 444 PHE D O   1 
ATOM   16301 C CB  . PHE D 1 444 ? 59.752  -6.370  18.621  1.00 82.52  ? 444 PHE D CB  1 
ATOM   16302 C CG  . PHE D 1 444 ? 60.578  -6.236  17.353  1.00 81.85  ? 444 PHE D CG  1 
ATOM   16303 C CD1 . PHE D 1 444 ? 59.956  -6.030  16.134  1.00 80.12  ? 444 PHE D CD1 1 
ATOM   16304 C CD2 . PHE D 1 444 ? 61.958  -6.400  17.370  1.00 83.19  ? 444 PHE D CD2 1 
ATOM   16305 C CE1 . PHE D 1 444 ? 60.690  -5.955  14.966  1.00 79.48  ? 444 PHE D CE1 1 
ATOM   16306 C CE2 . PHE D 1 444 ? 62.689  -6.315  16.197  1.00 82.95  ? 444 PHE D CE2 1 
ATOM   16307 C CZ  . PHE D 1 444 ? 62.050  -6.106  14.997  1.00 81.38  ? 444 PHE D CZ  1 
ATOM   16308 N N   . THR D 1 445 ? 57.195  -4.866  20.263  1.00 82.33  ? 445 THR D N   1 
ATOM   16309 C CA  . THR D 1 445 ? 56.190  -4.920  21.310  1.00 82.62  ? 445 THR D CA  1 
ATOM   16310 C C   . THR D 1 445 ? 55.260  -6.099  21.030  1.00 81.07  ? 445 THR D C   1 
ATOM   16311 O O   . THR D 1 445 ? 54.686  -6.227  19.945  1.00 79.22  ? 445 THR D O   1 
ATOM   16312 C CB  . THR D 1 445 ? 55.476  -3.560  21.383  1.00 82.70  ? 445 THR D CB  1 
ATOM   16313 O OG1 . THR D 1 445 ? 56.417  -2.627  21.929  1.00 84.02  ? 445 THR D OG1 1 
ATOM   16314 C CG2 . THR D 1 445 ? 54.252  -3.542  22.285  1.00 81.97  ? 445 THR D CG2 1 
ATOM   16315 N N   . LEU D 1 446 ? 55.153  -6.989  22.019  1.00 81.37  ? 446 LEU D N   1 
ATOM   16316 C CA  . LEU D 1 446 ? 54.118  -8.003  22.011  1.00 80.04  ? 446 LEU D CA  1 
ATOM   16317 C C   . LEU D 1 446 ? 52.804  -7.346  22.410  1.00 79.72  ? 446 LEU D C   1 
ATOM   16318 O O   . LEU D 1 446 ? 52.782  -6.407  23.193  1.00 79.20  ? 446 LEU D O   1 
ATOM   16319 C CB  . LEU D 1 446 ? 54.464  -9.128  22.982  1.00 80.56  ? 446 LEU D CB  1 
ATOM   16320 C CG  . LEU D 1 446 ? 55.793  -9.837  22.741  1.00 80.79  ? 446 LEU D CG  1 
ATOM   16321 C CD1 . LEU D 1 446 ? 55.964  -10.927 23.774  1.00 82.29  ? 446 LEU D CD1 1 
ATOM   16322 C CD2 . LEU D 1 446 ? 55.852  -10.387 21.331  1.00 79.31  ? 446 LEU D CD2 1 
ATOM   16323 N N   . LEU D 1 447 ? 51.688  -7.897  21.951  1.00 80.31  ? 447 LEU D N   1 
ATOM   16324 C CA  . LEU D 1 447 ? 50.438  -7.310  22.362  1.00 81.78  ? 447 LEU D CA  1 
ATOM   16325 C C   . LEU D 1 447 ? 49.316  -8.324  22.529  1.00 82.35  ? 447 LEU D C   1 
ATOM   16326 O O   . LEU D 1 447 ? 49.460  -9.505  22.257  1.00 82.75  ? 447 LEU D O   1 
ATOM   16327 C CB  . LEU D 1 447 ? 50.143  -6.203  21.352  1.00 82.65  ? 447 LEU D CB  1 
ATOM   16328 C CG  . LEU D 1 447 ? 50.195  -6.555  19.863  1.00 80.52  ? 447 LEU D CG  1 
ATOM   16329 C CD1 . LEU D 1 447 ? 48.928  -7.253  19.495  1.00 78.87  ? 447 LEU D CD1 1 
ATOM   16330 C CD2 . LEU D 1 447 ? 50.399  -5.302  19.011  1.00 78.98  ? 447 LEU D CD2 1 
ATOM   16331 N N   . ASP D 1 448 ? 48.212  -7.795  23.056  1.00 86.34  ? 448 ASP D N   1 
ATOM   16332 C CA  . ASP D 1 448 ? 46.942  -8.482  23.254  1.00 89.54  ? 448 ASP D CA  1 
ATOM   16333 C C   . ASP D 1 448 ? 47.205  -9.873  23.794  1.00 85.60  ? 448 ASP D C   1 
ATOM   16334 O O   . ASP D 1 448 ? 47.794  -9.992  24.864  1.00 85.36  ? 448 ASP D O   1 
ATOM   16335 C CB  . ASP D 1 448 ? 46.000  -8.345  22.053  1.00 93.31  ? 448 ASP D CB  1 
ATOM   16336 C CG  . ASP D 1 448 ? 45.428  -6.943  21.810  1.00 93.51  ? 448 ASP D CG  1 
ATOM   16337 O OD1 . ASP D 1 448 ? 46.194  -6.056  21.339  1.00 91.99  ? 448 ASP D OD1 1 
ATOM   16338 O OD2 . ASP D 1 448 ? 44.221  -6.733  22.097  1.00 92.78  ? 448 ASP D OD2 1 
ATOM   16339 N N   . ASP D 1 449 ? 46.787  -10.873 23.012  1.00 84.16  ? 449 ASP D N   1 
ATOM   16340 C CA  . ASP D 1 449 ? 46.610  -12.237 23.492  1.00 86.12  ? 449 ASP D CA  1 
ATOM   16341 C C   . ASP D 1 449 ? 47.271  -13.251 22.562  1.00 81.15  ? 449 ASP D C   1 
ATOM   16342 O O   . ASP D 1 449 ? 46.973  -13.361 21.367  1.00 76.81  ? 449 ASP D O   1 
ATOM   16343 C CB  . ASP D 1 449 ? 45.145  -12.634 23.642  1.00 88.65  ? 449 ASP D CB  1 
ATOM   16344 C CG  . ASP D 1 449 ? 44.358  -11.911 24.730  1.00 92.11  ? 449 ASP D CG  1 
ATOM   16345 O OD1 . ASP D 1 449 ? 44.399  -10.639 24.747  1.00 95.00  ? 449 ASP D OD1 1 
ATOM   16346 O OD2 . ASP D 1 449 ? 43.692  -12.620 25.529  1.00 91.66  ? 449 ASP D OD2 1 
ATOM   16347 N N   . LEU D 1 450 ? 48.162  -14.014 23.173  1.00 80.34  ? 450 LEU D N   1 
ATOM   16348 C CA  . LEU D 1 450 ? 48.595  -15.259 22.593  1.00 80.88  ? 450 LEU D CA  1 
ATOM   16349 C C   . LEU D 1 450 ? 47.355  -16.117 22.312  1.00 80.56  ? 450 LEU D C   1 
ATOM   16350 O O   . LEU D 1 450 ? 46.500  -16.292 23.182  1.00 80.91  ? 450 LEU D O   1 
ATOM   16351 C CB  . LEU D 1 450 ? 49.561  -15.879 23.602  1.00 82.51  ? 450 LEU D CB  1 
ATOM   16352 C CG  . LEU D 1 450 ? 50.000  -17.313 23.306  1.00 82.98  ? 450 LEU D CG  1 
ATOM   16353 C CD1 . LEU D 1 450 ? 50.739  -17.421 21.986  1.00 81.75  ? 450 LEU D CD1 1 
ATOM   16354 C CD2 . LEU D 1 450 ? 50.851  -17.835 24.443  1.00 85.83  ? 450 LEU D CD2 1 
ATOM   16355 N N   . LYS D 1 451 ? 47.257  -16.621 21.073  1.00 79.26  ? 451 LYS D N   1 
ATOM   16356 C CA  . LYS D 1 451 ? 46.171  -17.493 20.652  1.00 78.90  ? 451 LYS D CA  1 
ATOM   16357 C C   . LYS D 1 451 ? 46.710  -18.887 20.331  1.00 79.41  ? 451 LYS D C   1 
ATOM   16358 O O   . LYS D 1 451 ? 47.814  -19.016 19.803  1.00 81.93  ? 451 LYS D O   1 
ATOM   16359 C CB  . LYS D 1 451 ? 45.475  -16.847 19.455  1.00 78.50  ? 451 LYS D CB  1 
ATOM   16360 C CG  . LYS D 1 451 ? 44.641  -15.643 19.856  1.00 80.15  ? 451 LYS D CG  1 
ATOM   16361 C CD  . LYS D 1 451 ? 43.885  -14.993 18.711  1.00 80.41  ? 451 LYS D CD  1 
ATOM   16362 C CE  . LYS D 1 451 ? 43.243  -13.711 19.136  1.00 82.07  ? 451 LYS D CE  1 
ATOM   16363 N NZ  . LYS D 1 451 ? 42.490  -13.168 18.006  1.00 81.84  ? 451 LYS D NZ  1 
ATOM   16364 N N   . ILE D 1 452 ? 45.935  -19.925 20.691  1.00 78.23  ? 452 ILE D N   1 
ATOM   16365 C CA  . ILE D 1 452 ? 46.339  -21.321 20.561  1.00 77.00  ? 452 ILE D CA  1 
ATOM   16366 C C   . ILE D 1 452 ? 45.201  -22.105 19.911  1.00 75.68  ? 452 ILE D C   1 
ATOM   16367 O O   . ILE D 1 452 ? 44.051  -21.982 20.345  1.00 76.33  ? 452 ILE D O   1 
ATOM   16368 C CB  . ILE D 1 452 ? 46.687  -21.884 21.944  1.00 78.56  ? 452 ILE D CB  1 
ATOM   16369 C CG1 . ILE D 1 452 ? 47.881  -21.181 22.542  1.00 79.69  ? 452 ILE D CG1 1 
ATOM   16370 C CG2 . ILE D 1 452 ? 46.926  -23.389 21.880  1.00 79.97  ? 452 ILE D CG2 1 
ATOM   16371 C CD1 . ILE D 1 452 ? 47.706  -20.863 24.011  1.00 81.35  ? 452 ILE D CD1 1 
ATOM   16372 N N   . SER D 1 453 ? 45.519  -22.906 18.880  1.00 73.78  ? 453 SER D N   1 
ATOM   16373 C CA  . SER D 1 453 ? 44.528  -23.742 18.209  1.00 72.39  ? 453 SER D CA  1 
ATOM   16374 C C   . SER D 1 453 ? 44.984  -25.194 18.245  1.00 72.76  ? 453 SER D C   1 
ATOM   16375 O O   . SER D 1 453 ? 46.162  -25.463 18.074  1.00 73.57  ? 453 SER D O   1 
ATOM   16376 C CB  . SER D 1 453 ? 44.279  -23.309 16.775  1.00 70.46  ? 453 SER D CB  1 
ATOM   16377 O OG  . SER D 1 453 ? 44.921  -24.160 15.831  1.00 70.31  ? 453 SER D OG  1 
ATOM   16378 N N   . TYR D 1 454 ? 44.029  -26.113 18.428  1.00 73.23  ? 454 TYR D N   1 
ATOM   16379 C CA  . TYR D 1 454 ? 44.213  -27.550 18.225  1.00 73.05  ? 454 TYR D CA  1 
ATOM   16380 C C   . TYR D 1 454 ? 43.123  -28.065 17.281  1.00 71.93  ? 454 TYR D C   1 
ATOM   16381 O O   . TYR D 1 454 ? 42.083  -28.555 17.721  1.00 71.76  ? 454 TYR D O   1 
ATOM   16382 C CB  . TYR D 1 454 ? 44.148  -28.232 19.594  1.00 74.72  ? 454 TYR D CB  1 
ATOM   16383 C CG  . TYR D 1 454 ? 44.764  -29.616 19.625  1.00 75.40  ? 454 TYR D CG  1 
ATOM   16384 C CD1 . TYR D 1 454 ? 46.147  -29.753 19.593  1.00 76.49  ? 454 TYR D CD1 1 
ATOM   16385 C CD2 . TYR D 1 454 ? 43.996  -30.767 19.704  1.00 75.37  ? 454 TYR D CD2 1 
ATOM   16386 C CE1 . TYR D 1 454 ? 46.762  -30.998 19.629  1.00 77.22  ? 454 TYR D CE1 1 
ATOM   16387 C CE2 . TYR D 1 454 ? 44.597  -32.016 19.724  1.00 77.12  ? 454 TYR D CE2 1 
ATOM   16388 C CZ  . TYR D 1 454 ? 45.980  -32.132 19.688  1.00 77.60  ? 454 TYR D CZ  1 
ATOM   16389 O OH  . TYR D 1 454 ? 46.600  -33.336 19.697  1.00 78.90  ? 454 TYR D OH  1 
ATOM   16390 N N   . ASN D 1 455 ? 43.346  -27.895 15.976  1.00 70.92  ? 455 ASN D N   1 
ATOM   16391 C CA  . ASN D 1 455 ? 42.300  -28.106 14.994  1.00 70.42  ? 455 ASN D CA  1 
ATOM   16392 C C   . ASN D 1 455 ? 42.311  -29.583 14.629  1.00 71.52  ? 455 ASN D C   1 
ATOM   16393 O O   . ASN D 1 455 ? 43.141  -30.022 13.840  1.00 70.46  ? 455 ASN D O   1 
ATOM   16394 C CB  . ASN D 1 455 ? 42.449  -27.155 13.811  1.00 69.58  ? 455 ASN D CB  1 
ATOM   16395 C CG  . ASN D 1 455 ? 41.326  -27.285 12.816  1.00 69.14  ? 455 ASN D CG  1 
ATOM   16396 O OD1 . ASN D 1 455 ? 41.057  -26.373 12.023  1.00 67.76  ? 455 ASN D OD1 1 
ATOM   16397 N ND2 . ASN D 1 455 ? 40.634  -28.408 12.862  1.00 71.12  ? 455 ASN D ND2 1 
ATOM   16398 N N   . THR D 1 456 ? 41.343  -30.300 15.215  1.00 73.88  ? 456 THR D N   1 
ATOM   16399 C CA  . THR D 1 456 ? 41.241  -31.752 15.194  1.00 75.70  ? 456 THR D CA  1 
ATOM   16400 C C   . THR D 1 456 ? 40.893  -32.259 13.787  1.00 75.24  ? 456 THR D C   1 
ATOM   16401 O O   . THR D 1 456 ? 41.101  -33.433 13.509  1.00 77.54  ? 456 THR D O   1 
ATOM   16402 C CB  . THR D 1 456 ? 40.204  -32.165 16.252  1.00 76.75  ? 456 THR D CB  1 
ATOM   16403 O OG1 . THR D 1 456 ? 39.157  -31.196 16.290  1.00 76.76  ? 456 THR D OG1 1 
ATOM   16404 C CG2 . THR D 1 456 ? 40.755  -32.140 17.665  1.00 78.25  ? 456 THR D CG2 1 
ATOM   16405 N N   . HIS D 1 457 ? 40.314  -31.399 12.923  1.00 73.99  ? 457 HIS D N   1 
ATOM   16406 C CA  . HIS D 1 457 ? 40.076  -31.685 11.502  1.00 71.38  ? 457 HIS D CA  1 
ATOM   16407 C C   . HIS D 1 457 ? 38.771  -32.460 11.250  1.00 70.26  ? 457 HIS D C   1 
ATOM   16408 O O   . HIS D 1 457 ? 38.582  -33.004 10.162  1.00 68.50  ? 457 HIS D O   1 
ATOM   16409 C CB  . HIS D 1 457 ? 41.284  -32.384 10.864  1.00 70.84  ? 457 HIS D CB  1 
ATOM   16410 C CG  . HIS D 1 457 ? 42.330  -31.462 10.381  1.00 69.83  ? 457 HIS D CG  1 
ATOM   16411 N ND1 . HIS D 1 457 ? 43.099  -30.690 11.224  1.00 70.78  ? 457 HIS D ND1 1 
ATOM   16412 C CD2 . HIS D 1 457 ? 42.716  -31.175 9.135   1.00 68.69  ? 457 HIS D CD2 1 
ATOM   16413 C CE1 . HIS D 1 457 ? 43.945  -29.971 10.495  1.00 70.15  ? 457 HIS D CE1 1 
ATOM   16414 N NE2 . HIS D 1 457 ? 43.732  -30.256 9.223   1.00 69.04  ? 457 HIS D NE2 1 
ATOM   16415 N N   . LEU D 1 458 ? 37.850  -32.429 12.231  1.00 69.91  ? 458 LEU D N   1 
ATOM   16416 C CA  . LEU D 1 458 ? 36.585  -33.136 12.176  1.00 68.85  ? 458 LEU D CA  1 
ATOM   16417 C C   . LEU D 1 458 ? 35.637  -32.363 11.281  1.00 66.85  ? 458 LEU D C   1 
ATOM   16418 O O   . LEU D 1 458 ? 35.015  -31.429 11.743  1.00 66.90  ? 458 LEU D O   1 
ATOM   16419 C CB  . LEU D 1 458 ? 36.028  -33.231 13.592  1.00 70.01  ? 458 LEU D CB  1 
ATOM   16420 C CG  . LEU D 1 458 ? 36.957  -33.831 14.651  1.00 71.55  ? 458 LEU D CG  1 
ATOM   16421 C CD1 . LEU D 1 458 ? 36.186  -34.029 15.943  1.00 73.01  ? 458 LEU D CD1 1 
ATOM   16422 C CD2 . LEU D 1 458 ? 37.605  -35.128 14.201  1.00 71.96  ? 458 LEU D CD2 1 
ATOM   16423 N N   . GLY D 1 459 ? 35.533  -32.746 10.012  1.00 65.94  ? 459 GLY D N   1 
ATOM   16424 C CA  . GLY D 1 459 ? 34.815  -31.945 9.042   1.00 65.26  ? 459 GLY D CA  1 
ATOM   16425 C C   . GLY D 1 459 ? 35.316  -30.499 9.068   1.00 65.43  ? 459 GLY D C   1 
ATOM   16426 O O   . GLY D 1 459 ? 36.514  -30.270 8.990   1.00 65.45  ? 459 GLY D O   1 
ATOM   16427 N N   . TRP D 1 460 ? 34.392  -29.531 9.219   1.00 65.84  ? 460 TRP D N   1 
ATOM   16428 C CA  . TRP D 1 460 ? 34.711  -28.113 9.176   1.00 65.20  ? 460 TRP D CA  1 
ATOM   16429 C C   . TRP D 1 460 ? 34.974  -27.560 10.576  1.00 65.59  ? 460 TRP D C   1 
ATOM   16430 O O   . TRP D 1 460 ? 35.418  -26.405 10.710  1.00 65.34  ? 460 TRP D O   1 
ATOM   16431 C CB  . TRP D 1 460 ? 33.592  -27.327 8.476   1.00 65.05  ? 460 TRP D CB  1 
ATOM   16432 C CG  . TRP D 1 460 ? 33.419  -27.699 7.026   1.00 66.03  ? 460 TRP D CG  1 
ATOM   16433 C CD1 . TRP D 1 460 ? 32.372  -28.383 6.473   1.00 67.26  ? 460 TRP D CD1 1 
ATOM   16434 C CD2 . TRP D 1 460 ? 34.348  -27.445 5.944   1.00 66.20  ? 460 TRP D CD2 1 
ATOM   16435 N NE1 . TRP D 1 460 ? 32.571  -28.552 5.128   1.00 67.15  ? 460 TRP D NE1 1 
ATOM   16436 C CE2 . TRP D 1 460 ? 33.780  -28.001 4.776   1.00 66.32  ? 460 TRP D CE2 1 
ATOM   16437 C CE3 . TRP D 1 460 ? 35.591  -26.802 5.849   1.00 66.45  ? 460 TRP D CE3 1 
ATOM   16438 C CZ2 . TRP D 1 460 ? 34.410  -27.928 3.536   1.00 66.04  ? 460 TRP D CZ2 1 
ATOM   16439 C CZ3 . TRP D 1 460 ? 36.223  -26.744 4.623   1.00 66.24  ? 460 TRP D CZ3 1 
ATOM   16440 C CH2 . TRP D 1 460 ? 35.635  -27.297 3.484   1.00 66.31  ? 460 TRP D CH2 1 
ATOM   16441 N N   . ALA D 1 461 ? 34.706  -28.386 11.600  1.00 65.73  ? 461 ALA D N   1 
ATOM   16442 C CA  . ALA D 1 461 ? 35.005  -28.005 12.970  1.00 67.08  ? 461 ALA D CA  1 
ATOM   16443 C C   . ALA D 1 461 ? 36.513  -27.768 13.123  1.00 67.91  ? 461 ALA D C   1 
ATOM   16444 O O   . ALA D 1 461 ? 37.321  -28.659 12.830  1.00 70.32  ? 461 ALA D O   1 
ATOM   16445 C CB  . ALA D 1 461 ? 34.499  -29.060 13.916  1.00 68.19  ? 461 ALA D CB  1 
ATOM   16446 N N   . ILE D 1 462 ? 36.866  -26.560 13.584  1.00 67.29  ? 462 ILE D N   1 
ATOM   16447 C CA  . ILE D 1 462 ? 38.237  -26.094 13.752  1.00 67.07  ? 462 ILE D CA  1 
ATOM   16448 C C   . ILE D 1 462 ? 38.798  -26.520 15.113  1.00 68.76  ? 462 ILE D C   1 
ATOM   16449 O O   . ILE D 1 462 ? 39.971  -26.264 15.390  1.00 69.49  ? 462 ILE D O   1 
ATOM   16450 C CB  . ILE D 1 462 ? 38.309  -24.554 13.658  1.00 65.96  ? 462 ILE D CB  1 
ATOM   16451 C CG1 . ILE D 1 462 ? 37.546  -23.916 14.813  1.00 66.67  ? 462 ILE D CG1 1 
ATOM   16452 C CG2 . ILE D 1 462 ? 37.830  -24.028 12.302  1.00 63.95  ? 462 ILE D CG2 1 
ATOM   16453 C CD1 . ILE D 1 462 ? 38.187  -22.653 15.328  1.00 67.49  ? 462 ILE D CD1 1 
ATOM   16454 N N   . GLY D 1 463 ? 37.944  -27.066 15.993  1.00 70.15  ? 463 GLY D N   1 
ATOM   16455 C CA  . GLY D 1 463 ? 38.377  -27.579 17.286  1.00 72.38  ? 463 GLY D CA  1 
ATOM   16456 C C   . GLY D 1 463 ? 38.721  -26.453 18.257  1.00 73.12  ? 463 GLY D C   1 
ATOM   16457 O O   . GLY D 1 463 ? 38.387  -25.299 17.998  1.00 72.38  ? 463 GLY D O   1 
ATOM   16458 N N   . SER D 1 464 ? 39.425  -26.793 19.349  1.00 75.38  ? 464 SER D N   1 
ATOM   16459 C CA  . SER D 1 464 ? 39.693  -25.835 20.419  1.00 75.82  ? 464 SER D CA  1 
ATOM   16460 C C   . SER D 1 464 ? 40.488  -24.633 19.928  1.00 73.83  ? 464 SER D C   1 
ATOM   16461 O O   . SER D 1 464 ? 41.277  -24.697 18.971  1.00 70.97  ? 464 SER D O   1 
ATOM   16462 C CB  . SER D 1 464 ? 40.393  -26.452 21.602  1.00 78.34  ? 464 SER D CB  1 
ATOM   16463 O OG  . SER D 1 464 ? 39.462  -27.045 22.494  1.00 80.22  ? 464 SER D OG  1 
ATOM   16464 N N   . GLN D 1 465 ? 40.194  -23.534 20.627  1.00 75.29  ? 465 GLN D N   1 
ATOM   16465 C CA  . GLN D 1 465 ? 40.966  -22.301 20.599  1.00 75.90  ? 465 GLN D CA  1 
ATOM   16466 C C   . GLN D 1 465 ? 41.074  -21.773 22.020  1.00 77.28  ? 465 GLN D C   1 
ATOM   16467 O O   . GLN D 1 465 ? 40.255  -22.083 22.881  1.00 78.97  ? 465 GLN D O   1 
ATOM   16468 C CB  . GLN D 1 465 ? 40.387  -21.205 19.708  1.00 74.40  ? 465 GLN D CB  1 
ATOM   16469 C CG  . GLN D 1 465 ? 40.664  -21.471 18.234  1.00 74.33  ? 465 GLN D CG  1 
ATOM   16470 C CD  . GLN D 1 465 ? 40.330  -20.323 17.311  1.00 74.39  ? 465 GLN D CD  1 
ATOM   16471 O OE1 . GLN D 1 465 ? 39.304  -20.301 16.617  1.00 75.15  ? 465 GLN D OE1 1 
ATOM   16472 N NE2 . GLN D 1 465 ? 41.227  -19.354 17.275  1.00 76.05  ? 465 GLN D NE2 1 
ATOM   16473 N N   . ALA D 1 466 ? 42.108  -20.980 22.255  1.00 76.84  ? 466 ALA D N   1 
ATOM   16474 C CA  . ALA D 1 466 ? 42.346  -20.479 23.590  1.00 77.97  ? 466 ALA D CA  1 
ATOM   16475 C C   . ALA D 1 466 ? 42.989  -19.111 23.469  1.00 76.59  ? 466 ALA D C   1 
ATOM   16476 O O   . ALA D 1 466 ? 43.738  -18.856 22.539  1.00 75.04  ? 466 ALA D O   1 
ATOM   16477 C CB  . ALA D 1 466 ? 43.204  -21.466 24.350  1.00 79.68  ? 466 ALA D CB  1 
ATOM   16478 N N   . SER D 1 467 ? 42.665  -18.228 24.398  1.00 77.60  ? 467 SER D N   1 
ATOM   16479 C CA  . SER D 1 467 ? 43.261  -16.906 24.381  1.00 77.85  ? 467 SER D CA  1 
ATOM   16480 C C   . SER D 1 467 ? 43.977  -16.683 25.703  1.00 79.53  ? 467 SER D C   1 
ATOM   16481 O O   . SER D 1 467 ? 43.360  -16.626 26.757  1.00 81.85  ? 467 SER D O   1 
ATOM   16482 C CB  . SER D 1 467 ? 42.226  -15.840 24.077  1.00 76.47  ? 467 SER D CB  1 
ATOM   16483 O OG  . SER D 1 467 ? 41.685  -16.095 22.785  1.00 74.59  ? 467 SER D OG  1 
ATOM   16484 N N   . VAL D 1 468 ? 45.297  -16.588 25.649  1.00 79.41  ? 468 VAL D N   1 
ATOM   16485 C CA  . VAL D 1 468 ? 46.033  -16.440 26.881  1.00 81.35  ? 468 VAL D CA  1 
ATOM   16486 C C   . VAL D 1 468 ? 46.480  -14.990 27.015  1.00 81.94  ? 468 VAL D C   1 
ATOM   16487 O O   . VAL D 1 468 ? 46.919  -14.372 26.042  1.00 79.68  ? 468 VAL D O   1 
ATOM   16488 C CB  . VAL D 1 468 ? 47.189  -17.446 26.911  1.00 81.85  ? 468 VAL D CB  1 
ATOM   16489 C CG1 . VAL D 1 468 ? 47.902  -17.399 28.253  1.00 84.20  ? 468 VAL D CG1 1 
ATOM   16490 C CG2 . VAL D 1 468 ? 46.688  -18.856 26.626  1.00 81.85  ? 468 VAL D CG2 1 
ATOM   16491 N N   . SER D 1 469 ? 46.264  -14.455 28.223  1.00 85.10  ? 469 SER D N   1 
ATOM   16492 C CA  . SER D 1 469 ? 46.723  -13.133 28.603  1.00 87.26  ? 469 SER D CA  1 
ATOM   16493 C C   . SER D 1 469 ? 48.161  -13.284 29.066  1.00 89.91  ? 469 SER D C   1 
ATOM   16494 O O   . SER D 1 469 ? 48.446  -14.270 29.751  1.00 91.47  ? 469 SER D O   1 
ATOM   16495 C CB  . SER D 1 469 ? 45.865  -12.537 29.693  1.00 89.07  ? 469 SER D CB  1 
ATOM   16496 O OG  . SER D 1 469 ? 46.495  -11.391 30.252  1.00 91.15  ? 469 SER D OG  1 
ATOM   16497 N N   . ILE D 1 470 ? 49.042  -12.359 28.640  1.00 89.96  ? 470 ILE D N   1 
ATOM   16498 C CA  . ILE D 1 470 ? 50.446  -12.436 29.015  1.00 93.34  ? 470 ILE D CA  1 
ATOM   16499 C C   . ILE D 1 470 ? 50.840  -11.209 29.823  1.00 96.41  ? 470 ILE D C   1 
ATOM   16500 O O   . ILE D 1 470 ? 52.017  -11.051 30.158  1.00 99.14  ? 470 ILE D O   1 
ATOM   16501 C CB  . ILE D 1 470 ? 51.368  -12.666 27.802  1.00 92.52  ? 470 ILE D CB  1 
ATOM   16502 C CG1 . ILE D 1 470 ? 51.178  -11.622 26.725  1.00 90.89  ? 470 ILE D CG1 1 
ATOM   16503 C CG2 . ILE D 1 470 ? 51.186  -14.086 27.250  1.00 92.49  ? 470 ILE D CG2 1 
ATOM   16504 C CD1 . ILE D 1 470 ? 52.249  -11.680 25.651  1.00 90.19  ? 470 ILE D CD1 1 
ATOM   16505 N N   . SER D 1 471 ? 49.825  -10.403 30.169  1.00 97.47  ? 471 SER D N   1 
ATOM   16506 C CA  . SER D 1 471 ? 49.953  -9.248  31.043  1.00 99.50  ? 471 SER D CA  1 
ATOM   16507 C C   . SER D 1 471 ? 51.003  -9.485  32.126  1.00 102.34 ? 471 SER D C   1 
ATOM   16508 O O   . SER D 1 471 ? 51.955  -8.720  32.241  1.00 102.93 ? 471 SER D O   1 
ATOM   16509 C CB  . SER D 1 471 ? 48.623  -8.937  31.653  1.00 100.59 ? 471 SER D CB  1 
ATOM   16510 O OG  . SER D 1 471 ? 48.034  -10.144 32.120  1.00 103.77 ? 471 SER D OG  1 
ATOM   16511 N N   . ASP D 1 472 ? 50.844  -10.577 32.885  1.00 104.43 ? 472 ASP D N   1 
ATOM   16512 C CA  . ASP D 1 472 ? 51.686  -10.841 34.041  1.00 106.85 ? 472 ASP D CA  1 
ATOM   16513 C C   . ASP D 1 472 ? 53.066  -11.349 33.624  1.00 106.71 ? 472 ASP D C   1 
ATOM   16514 O O   . ASP D 1 472 ? 53.772  -11.911 34.456  1.00 109.53 ? 472 ASP D O   1 
ATOM   16515 C CB  . ASP D 1 472 ? 51.037  -11.842 34.988  1.00 108.91 ? 472 ASP D CB  1 
ATOM   16516 C CG  . ASP D 1 472 ? 50.892  -13.253 34.435  1.00 110.18 ? 472 ASP D CG  1 
ATOM   16517 O OD1 . ASP D 1 472 ? 50.957  -13.398 33.199  1.00 110.11 ? 472 ASP D OD1 1 
ATOM   16518 O OD2 . ASP D 1 472 ? 50.753  -14.205 35.236  1.00 112.47 ? 472 ASP D OD2 1 
ATOM   16519 N N   . GLN D 1 473 ? 53.465  -11.186 32.355  1.00 103.85 ? 473 GLN D N   1 
ATOM   16520 C CA  . GLN D 1 473 ? 54.778  -11.666 31.946  1.00 103.98 ? 473 GLN D CA  1 
ATOM   16521 C C   . GLN D 1 473 ? 55.500  -10.716 30.987  1.00 103.83 ? 473 GLN D C   1 
ATOM   16522 O O   . GLN D 1 473 ? 56.631  -11.011 30.609  1.00 103.86 ? 473 GLN D O   1 
ATOM   16523 C CB  . GLN D 1 473 ? 54.671  -13.054 31.315  1.00 102.38 ? 473 GLN D CB  1 
ATOM   16524 C CG  . GLN D 1 473 ? 54.337  -14.180 32.288  1.00 103.07 ? 473 GLN D CG  1 
ATOM   16525 C CD  . GLN D 1 473 ? 54.056  -15.484 31.575  1.00 100.67 ? 473 GLN D CD  1 
ATOM   16526 O OE1 . GLN D 1 473 ? 54.957  -16.258 31.229  1.00 100.54 ? 473 GLN D OE1 1 
ATOM   16527 N NE2 . GLN D 1 473 ? 52.780  -15.727 31.334  1.00 98.84  ? 473 GLN D NE2 1 
ATOM   16528 N N   . LEU D 1 474 ? 54.899  -9.565  30.649  1.00 103.33 ? 474 LEU D N   1 
ATOM   16529 C CA  . LEU D 1 474 ? 55.481  -8.626  29.695  1.00 102.84 ? 474 LEU D CA  1 
ATOM   16530 C C   . LEU D 1 474 ? 56.932  -8.289  30.036  1.00 103.74 ? 474 LEU D C   1 
ATOM   16531 O O   . LEU D 1 474 ? 57.685  -7.960  29.126  1.00 102.52 ? 474 LEU D O   1 
ATOM   16532 C CB  . LEU D 1 474 ? 54.680  -7.323  29.590  1.00 104.05 ? 474 LEU D CB  1 
ATOM   16533 C CG  . LEU D 1 474 ? 53.524  -7.260  28.580  1.00 101.40 ? 474 LEU D CG  1 
ATOM   16534 C CD1 . LEU D 1 474 ? 53.864  -7.819  27.197  1.00 98.81  ? 474 LEU D CD1 1 
ATOM   16535 C CD2 . LEU D 1 474 ? 52.307  -7.942  29.150  1.00 101.82 ? 474 LEU D CD2 1 
ATOM   16536 N N   . ASP D 1 475 ? 57.304  -8.319  31.327  1.00 107.04 ? 475 ASP D N   1 
ATOM   16537 C CA  . ASP D 1 475 ? 58.667  -8.017  31.765  1.00 109.87 ? 475 ASP D CA  1 
ATOM   16538 C C   . ASP D 1 475 ? 59.683  -9.076  31.333  1.00 109.16 ? 475 ASP D C   1 
ATOM   16539 O O   . ASP D 1 475 ? 60.822  -8.735  31.034  1.00 110.98 ? 475 ASP D O   1 
ATOM   16540 C CB  . ASP D 1 475 ? 58.798  -7.935  33.279  1.00 114.14 ? 475 ASP D CB  1 
ATOM   16541 C CG  . ASP D 1 475 ? 58.559  -6.564  33.894  1.00 118.65 ? 475 ASP D CG  1 
ATOM   16542 O OD1 . ASP D 1 475 ? 57.772  -5.758  33.311  1.00 117.86 ? 475 ASP D OD1 1 
ATOM   16543 O OD2 . ASP D 1 475 ? 59.203  -6.298  34.936  1.00 123.84 ? 475 ASP D OD2 1 
ATOM   16544 N N   . LYS D 1 476 ? 59.284  -10.357 31.335  1.00 106.07 ? 476 LYS D N   1 
ATOM   16545 C CA  . LYS D 1 476 ? 60.221  -11.466 31.256  1.00 104.22 ? 476 LYS D CA  1 
ATOM   16546 C C   . LYS D 1 476 ? 60.902  -11.508 29.888  1.00 100.34 ? 476 LYS D C   1 
ATOM   16547 O O   . LYS D 1 476 ? 60.389  -10.962 28.913  1.00 97.24  ? 476 LYS D O   1 
ATOM   16548 C CB  . LYS D 1 476 ? 59.465  -12.769 31.527  1.00 104.88 ? 476 LYS D CB  1 
ATOM   16549 C CG  . LYS D 1 476 ? 58.712  -12.871 32.858  1.00 106.64 ? 476 LYS D CG  1 
ATOM   16550 C CD  . LYS D 1 476 ? 57.905  -14.161 33.010  1.00 106.39 ? 476 LYS D CD  1 
ATOM   16551 C CE  . LYS D 1 476 ? 58.747  -15.415 33.002  1.00 108.18 ? 476 LYS D CE  1 
ATOM   16552 N NZ  . LYS D 1 476 ? 57.965  -16.655 32.921  1.00 107.41 ? 476 LYS D NZ  1 
ATOM   16553 N N   . LYS D 1 477 ? 62.067  -12.168 29.837  1.00 100.04 ? 477 LYS D N   1 
ATOM   16554 C CA  . LYS D 1 477 ? 62.827  -12.312 28.607  1.00 98.37  ? 477 LYS D CA  1 
ATOM   16555 C C   . LYS D 1 477 ? 62.227  -13.435 27.760  1.00 95.75  ? 477 LYS D C   1 
ATOM   16556 O O   . LYS D 1 477 ? 62.172  -13.324 26.534  1.00 93.72  ? 477 LYS D O   1 
ATOM   16557 C CB  . LYS D 1 477 ? 64.306  -12.549 28.938  1.00 101.34 ? 477 LYS D CB  1 
ATOM   16558 C CG  . LYS D 1 477 ? 65.271  -12.172 27.810  1.00 101.37 ? 477 LYS D CG  1 
ATOM   16559 C CD  . LYS D 1 477 ? 66.761  -12.194 28.144  1.00 104.11 ? 477 LYS D CD  1 
ATOM   16560 C CE  . LYS D 1 477 ? 67.336  -13.592 28.169  1.00 106.06 ? 477 LYS D CE  1 
ATOM   16561 N NZ  . LYS D 1 477 ? 68.768  -13.646 28.486  1.00 108.71 ? 477 LYS D NZ  1 
ATOM   16562 N N   . ILE D 1 478 ? 61.782  -14.512 28.432  1.00 95.35  ? 478 ILE D N   1 
ATOM   16563 C CA  . ILE D 1 478 ? 61.090  -15.638 27.814  1.00 92.48  ? 478 ILE D CA  1 
ATOM   16564 C C   . ILE D 1 478 ? 59.680  -15.731 28.399  1.00 90.68  ? 478 ILE D C   1 
ATOM   16565 O O   . ILE D 1 478 ? 59.514  -15.804 29.612  1.00 91.96  ? 478 ILE D O   1 
ATOM   16566 C CB  . ILE D 1 478 ? 61.899  -16.935 28.041  1.00 93.95  ? 478 ILE D CB  1 
ATOM   16567 C CG1 . ILE D 1 478 ? 63.222  -16.924 27.258  1.00 94.37  ? 478 ILE D CG1 1 
ATOM   16568 C CG2 . ILE D 1 478 ? 61.079  -18.178 27.716  1.00 92.90  ? 478 ILE D CG2 1 
ATOM   16569 C CD1 . ILE D 1 478 ? 64.181  -18.038 27.629  1.00 96.46  ? 478 ILE D CD1 1 
ATOM   16570 N N   . ILE D 1 479 ? 58.664  -15.750 27.532  1.00 87.74  ? 479 ILE D N   1 
ATOM   16571 C CA  . ILE D 1 479 ? 57.289  -15.976 27.968  1.00 87.31  ? 479 ILE D CA  1 
ATOM   16572 C C   . ILE D 1 479 ? 56.908  -17.423 27.660  1.00 87.03  ? 479 ILE D C   1 
ATOM   16573 O O   . ILE D 1 479 ? 57.210  -17.892 26.563  1.00 86.05  ? 479 ILE D O   1 
ATOM   16574 C CB  . ILE D 1 479 ? 56.295  -15.026 27.275  1.00 84.90  ? 479 ILE D CB  1 
ATOM   16575 C CG1 . ILE D 1 479 ? 56.832  -13.576 27.113  1.00 85.17  ? 479 ILE D CG1 1 
ATOM   16576 C CG2 . ILE D 1 479 ? 54.950  -15.070 28.000  1.00 84.56  ? 479 ILE D CG2 1 
ATOM   16577 C CD1 . ILE D 1 479 ? 56.467  -12.608 28.230  1.00 86.27  ? 479 ILE D CD1 1 
ATOM   16578 N N   . THR D 1 480 ? 56.217  -18.109 28.594  1.00 88.00  ? 480 THR D N   1 
ATOM   16579 C CA  . THR D 1 480 ? 55.775  -19.489 28.366  1.00 87.58  ? 480 THR D CA  1 
ATOM   16580 C C   . THR D 1 480 ? 54.305  -19.654 28.767  1.00 86.76  ? 480 THR D C   1 
ATOM   16581 O O   . THR D 1 480 ? 53.809  -18.949 29.648  1.00 87.10  ? 480 THR D O   1 
ATOM   16582 C CB  . THR D 1 480 ? 56.651  -20.525 29.087  1.00 89.53  ? 480 THR D CB  1 
ATOM   16583 O OG1 . THR D 1 480 ? 56.040  -20.888 30.322  1.00 90.96  ? 480 THR D OG1 1 
ATOM   16584 C CG2 . THR D 1 480 ? 58.074  -20.051 29.334  1.00 90.96  ? 480 THR D CG2 1 
ATOM   16585 N N   . SER D 1 481 ? 53.629  -20.602 28.097  1.00 85.54  ? 481 SER D N   1 
ATOM   16586 C CA  . SER D 1 481 ? 52.277  -21.023 28.445  1.00 85.61  ? 481 SER D CA  1 
ATOM   16587 C C   . SER D 1 481 ? 52.135  -22.524 28.222  1.00 85.73  ? 481 SER D C   1 
ATOM   16588 O O   . SER D 1 481 ? 52.913  -23.118 27.485  1.00 86.34  ? 481 SER D O   1 
ATOM   16589 C CB  . SER D 1 481 ? 51.222  -20.265 27.660  1.00 83.54  ? 481 SER D CB  1 
ATOM   16590 O OG  . SER D 1 481 ? 49.912  -20.738 27.953  1.00 83.49  ? 481 SER D OG  1 
ATOM   16591 N N   . GLU D 1 482 ? 51.150  -23.138 28.877  1.00 85.82  ? 482 GLU D N   1 
ATOM   16592 C CA  . GLU D 1 482 ? 50.919  -24.560 28.699  1.00 86.00  ? 482 GLU D CA  1 
ATOM   16593 C C   . GLU D 1 482 ? 49.415  -24.765 28.702  1.00 85.17  ? 482 GLU D C   1 
ATOM   16594 O O   . GLU D 1 482 ? 48.767  -24.407 29.675  1.00 85.58  ? 482 GLU D O   1 
ATOM   16595 C CB  . GLU D 1 482 ? 51.657  -25.368 29.774  1.00 88.48  ? 482 GLU D CB  1 
ATOM   16596 C CG  . GLU D 1 482 ? 51.423  -26.877 29.709  1.00 88.88  ? 482 GLU D CG  1 
ATOM   16597 C CD  . GLU D 1 482 ? 51.693  -27.654 30.987  1.00 91.77  ? 482 GLU D CD  1 
ATOM   16598 O OE1 . GLU D 1 482 ? 51.255  -27.161 32.036  1.00 92.64  ? 482 GLU D OE1 1 
ATOM   16599 O OE2 . GLU D 1 482 ? 52.267  -28.771 30.956  1.00 93.18  ? 482 GLU D OE2 1 
ATOM   16600 N N   . ASN D 1 483 ? 48.894  -25.349 27.617  1.00 84.29  ? 483 ASN D N   1 
ATOM   16601 C CA  . ASN D 1 483 ? 47.460  -25.426 27.385  1.00 84.47  ? 483 ASN D CA  1 
ATOM   16602 C C   . ASN D 1 483 ? 47.084  -26.825 26.902  1.00 85.22  ? 483 ASN D C   1 
ATOM   16603 O O   . ASN D 1 483 ? 47.695  -27.329 25.964  1.00 85.37  ? 483 ASN D O   1 
ATOM   16604 C CB  . ASN D 1 483 ? 47.006  -24.385 26.361  1.00 82.57  ? 483 ASN D CB  1 
ATOM   16605 C CG  . ASN D 1 483 ? 47.486  -22.989 26.686  1.00 82.56  ? 483 ASN D CG  1 
ATOM   16606 O OD1 . ASN D 1 483 ? 46.696  -22.166 27.152  1.00 82.35  ? 483 ASN D OD1 1 
ATOM   16607 N ND2 . ASN D 1 483 ? 48.765  -22.706 26.464  1.00 83.14  ? 483 ASN D ND2 1 
ATOM   16608 N N   . PHE D 1 484 ? 46.043  -27.418 27.513  1.00 86.70  ? 484 PHE D N   1 
ATOM   16609 C CA  . PHE D 1 484 ? 45.700  -28.826 27.327  1.00 87.14  ? 484 PHE D CA  1 
ATOM   16610 C C   . PHE D 1 484 ? 44.426  -28.979 26.484  1.00 86.55  ? 484 PHE D C   1 
ATOM   16611 O O   . PHE D 1 484 ? 43.489  -28.195 26.605  1.00 84.83  ? 484 PHE D O   1 
ATOM   16612 C CB  . PHE D 1 484 ? 45.507  -29.491 28.695  1.00 88.92  ? 484 PHE D CB  1 
ATOM   16613 C CG  . PHE D 1 484 ? 46.730  -29.497 29.600  1.00 90.50  ? 484 PHE D CG  1 
ATOM   16614 C CD1 . PHE D 1 484 ? 47.779  -30.381 29.364  1.00 91.65  ? 484 PHE D CD1 1 
ATOM   16615 C CD2 . PHE D 1 484 ? 46.813  -28.658 30.706  1.00 91.31  ? 484 PHE D CD2 1 
ATOM   16616 C CE1 . PHE D 1 484 ? 48.893  -30.402 30.195  1.00 93.44  ? 484 PHE D CE1 1 
ATOM   16617 C CE2 . PHE D 1 484 ? 47.926  -28.675 31.532  1.00 93.35  ? 484 PHE D CE2 1 
ATOM   16618 C CZ  . PHE D 1 484 ? 48.965  -29.542 31.276  1.00 94.52  ? 484 PHE D CZ  1 
ATOM   16619 N N   . PHE D 1 485 ? 44.361  -30.058 25.684  1.00 88.22  ? 485 PHE D N   1 
ATOM   16620 C CA  . PHE D 1 485 ? 43.229  -30.310 24.795  1.00 87.72  ? 485 PHE D CA  1 
ATOM   16621 C C   . PHE D 1 485 ? 42.886  -31.795 24.737  1.00 88.48  ? 485 PHE D C   1 
ATOM   16622 O O   . PHE D 1 485 ? 43.747  -32.608 24.436  1.00 90.80  ? 485 PHE D O   1 
ATOM   16623 C CB  . PHE D 1 485 ? 43.599  -29.806 23.399  1.00 85.94  ? 485 PHE D CB  1 
ATOM   16624 C CG  . PHE D 1 485 ? 43.983  -28.335 23.419  1.00 84.98  ? 485 PHE D CG  1 
ATOM   16625 C CD1 . PHE D 1 485 ? 43.122  -27.386 23.963  1.00 85.77  ? 485 PHE D CD1 1 
ATOM   16626 C CD2 . PHE D 1 485 ? 45.220  -27.914 22.948  1.00 84.70  ? 485 PHE D CD2 1 
ATOM   16627 C CE1 . PHE D 1 485 ? 43.476  -26.040 24.007  1.00 85.49  ? 485 PHE D CE1 1 
ATOM   16628 C CE2 . PHE D 1 485 ? 45.571  -26.570 22.982  1.00 84.98  ? 485 PHE D CE2 1 
ATOM   16629 C CZ  . PHE D 1 485 ? 44.700  -25.636 23.510  1.00 85.07  ? 485 PHE D CZ  1 
ATOM   16630 N N   . ASN D 1 486 ? 41.622  -32.136 25.008  1.00 88.17  ? 486 ASN D N   1 
ATOM   16631 C CA  . ASN D 1 486 ? 41.135  -33.496 24.840  1.00 88.20  ? 486 ASN D CA  1 
ATOM   16632 C C   . ASN D 1 486 ? 41.170  -33.882 23.361  1.00 86.38  ? 486 ASN D C   1 
ATOM   16633 O O   . ASN D 1 486 ? 40.564  -33.212 22.533  1.00 85.81  ? 486 ASN D O   1 
ATOM   16634 C CB  . ASN D 1 486 ? 39.717  -33.660 25.376  1.00 88.67  ? 486 ASN D CB  1 
ATOM   16635 C CG  . ASN D 1 486 ? 39.655  -33.640 26.887  1.00 91.72  ? 486 ASN D CG  1 
ATOM   16636 O OD1 . ASN D 1 486 ? 40.208  -34.518 27.562  1.00 94.71  ? 486 ASN D OD1 1 
ATOM   16637 N ND2 . ASN D 1 486 ? 38.954  -32.673 27.455  1.00 92.46  ? 486 ASN D ND2 1 
ATOM   16638 N N   . ILE D 1 487 ? 41.855  -34.989 23.040  1.00 86.88  ? 487 ILE D N   1 
ATOM   16639 C CA  . ILE D 1 487 ? 41.872  -35.540 21.690  1.00 84.73  ? 487 ILE D CA  1 
ATOM   16640 C C   . ILE D 1 487 ? 40.589  -36.355 21.478  1.00 84.14  ? 487 ILE D C   1 
ATOM   16641 O O   . ILE D 1 487 ? 40.210  -37.173 22.318  1.00 85.03  ? 487 ILE D O   1 
ATOM   16642 C CB  . ILE D 1 487 ? 43.156  -36.360 21.425  1.00 85.31  ? 487 ILE D CB  1 
ATOM   16643 C CG1 . ILE D 1 487 ? 44.420  -35.649 21.951  1.00 86.28  ? 487 ILE D CG1 1 
ATOM   16644 C CG2 . ILE D 1 487 ? 43.297  -36.687 19.936  1.00 83.36  ? 487 ILE D CG2 1 
ATOM   16645 C CD1 . ILE D 1 487 ? 45.690  -36.477 21.854  1.00 87.75  ? 487 ILE D CD1 1 
ATOM   16646 N N   . PRO D 1 488 ? 39.817  -36.081 20.404  1.00 82.17  ? 488 PRO D N   1 
ATOM   16647 C CA  . PRO D 1 488 ? 38.680  -36.912 20.032  1.00 82.69  ? 488 PRO D CA  1 
ATOM   16648 C C   . PRO D 1 488 ? 39.151  -38.225 19.439  1.00 83.64  ? 488 PRO D C   1 
ATOM   16649 O O   . PRO D 1 488 ? 40.058  -38.216 18.620  1.00 83.67  ? 488 PRO D O   1 
ATOM   16650 C CB  . PRO D 1 488 ? 37.945  -36.058 18.994  1.00 80.50  ? 488 PRO D CB  1 
ATOM   16651 C CG  . PRO D 1 488 ? 38.433  -34.671 19.260  1.00 79.74  ? 488 PRO D CG  1 
ATOM   16652 C CD  . PRO D 1 488 ? 39.894  -34.878 19.575  1.00 80.53  ? 488 PRO D CD  1 
ATOM   16653 N N   . ASP D 1 489 ? 38.484  -39.329 19.808  1.00 85.82  ? 489 ASP D N   1 
ATOM   16654 C CA  . ASP D 1 489 ? 38.881  -40.661 19.365  1.00 86.28  ? 489 ASP D CA  1 
ATOM   16655 C C   . ASP D 1 489 ? 38.890  -40.734 17.839  1.00 84.68  ? 489 ASP D C   1 
ATOM   16656 O O   . ASP D 1 489 ? 39.694  -41.453 17.263  1.00 86.77  ? 489 ASP D O   1 
ATOM   16657 C CB  . ASP D 1 489 ? 38.039  -41.756 20.001  1.00 87.29  ? 489 ASP D CB  1 
ATOM   16658 C CG  . ASP D 1 489 ? 38.462  -42.175 21.402  1.00 89.53  ? 489 ASP D CG  1 
ATOM   16659 O OD1 . ASP D 1 489 ? 39.373  -41.562 21.955  1.00 89.58  ? 489 ASP D OD1 1 
ATOM   16660 O OD2 . ASP D 1 489 ? 37.883  -43.131 21.939  1.00 92.06  ? 489 ASP D OD2 1 
ATOM   16661 N N   . ASN D 1 490 ? 38.028  -39.957 17.184  1.00 82.49  ? 490 ASN D N   1 
ATOM   16662 C CA  . ASN D 1 490 ? 37.941  -39.968 15.734  1.00 80.28  ? 490 ASN D CA  1 
ATOM   16663 C C   . ASN D 1 490 ? 38.654  -38.749 15.135  1.00 78.37  ? 490 ASN D C   1 
ATOM   16664 O O   . ASN D 1 490 ? 38.241  -38.242 14.086  1.00 76.52  ? 490 ASN D O   1 
ATOM   16665 C CB  . ASN D 1 490 ? 36.480  -40.036 15.309  1.00 79.18  ? 490 ASN D CB  1 
ATOM   16666 C CG  . ASN D 1 490 ? 35.730  -38.819 15.769  1.00 77.62  ? 490 ASN D CG  1 
ATOM   16667 O OD1 . ASN D 1 490 ? 35.697  -38.518 16.965  1.00 78.23  ? 490 ASN D OD1 1 
ATOM   16668 N ND2 . ASN D 1 490 ? 35.166  -38.084 14.834  1.00 76.10  ? 490 ASN D ND2 1 
ATOM   16669 N N   . CYS D 1 491 ? 39.716  -38.279 15.810  1.00 78.45  ? 491 CYS D N   1 
ATOM   16670 C CA  . CYS D 1 491 ? 40.660  -37.345 15.219  1.00 76.90  ? 491 CYS D CA  1 
ATOM   16671 C C   . CYS D 1 491 ? 41.818  -38.126 14.609  1.00 77.37  ? 491 CYS D C   1 
ATOM   16672 O O   . CYS D 1 491 ? 42.519  -38.849 15.312  1.00 77.78  ? 491 CYS D O   1 
ATOM   16673 C CB  . CYS D 1 491 ? 41.234  -36.372 16.237  1.00 77.11  ? 491 CYS D CB  1 
ATOM   16674 S SG  . CYS D 1 491 ? 42.599  -35.393 15.558  1.00 76.05  ? 491 CYS D SG  1 
ATOM   16675 N N   . TRP D 1 492 ? 41.986  -37.945 13.295  1.00 76.93  ? 492 TRP D N   1 
ATOM   16676 C CA  . TRP D 1 492 ? 42.990  -38.632 12.503  1.00 77.30  ? 492 TRP D CA  1 
ATOM   16677 C C   . TRP D 1 492 ? 44.194  -37.733 12.273  1.00 77.36  ? 492 TRP D C   1 
ATOM   16678 O O   . TRP D 1 492 ? 45.258  -38.259 11.953  1.00 80.23  ? 492 TRP D O   1 
ATOM   16679 C CB  . TRP D 1 492 ? 42.430  -39.040 11.136  1.00 76.36  ? 492 TRP D CB  1 
ATOM   16680 C CG  . TRP D 1 492 ? 41.063  -39.652 11.200  1.00 76.55  ? 492 TRP D CG  1 
ATOM   16681 C CD1 . TRP D 1 492 ? 39.982  -39.335 10.432  1.00 75.65  ? 492 TRP D CD1 1 
ATOM   16682 C CD2 . TRP D 1 492 ? 40.650  -40.717 12.073  1.00 78.73  ? 492 TRP D CD2 1 
ATOM   16683 N NE1 . TRP D 1 492 ? 38.910  -40.114 10.779  1.00 77.32  ? 492 TRP D NE1 1 
ATOM   16684 C CE2 . TRP D 1 492 ? 39.293  -40.979 11.776  1.00 79.21  ? 492 TRP D CE2 1 
ATOM   16685 C CE3 . TRP D 1 492 ? 41.283  -41.462 13.069  1.00 80.53  ? 492 TRP D CE3 1 
ATOM   16686 C CZ2 . TRP D 1 492 ? 38.570  -41.966 12.442  1.00 80.04  ? 492 TRP D CZ2 1 
ATOM   16687 C CZ3 . TRP D 1 492 ? 40.568  -42.451 13.709  1.00 82.35  ? 492 TRP D CZ3 1 
ATOM   16688 C CH2 . TRP D 1 492 ? 39.235  -42.699 13.396  1.00 81.87  ? 492 TRP D CH2 1 
ATOM   16689 N N   . VAL D 1 493 ? 44.004  -36.408 12.373  1.00 75.41  ? 493 VAL D N   1 
ATOM   16690 C CA  . VAL D 1 493 ? 45.098  -35.472 12.186  1.00 74.87  ? 493 VAL D CA  1 
ATOM   16691 C C   . VAL D 1 493 ? 44.775  -34.159 12.896  1.00 74.30  ? 493 VAL D C   1 
ATOM   16692 O O   . VAL D 1 493 ? 43.626  -33.754 13.000  1.00 73.25  ? 493 VAL D O   1 
ATOM   16693 C CB  . VAL D 1 493 ? 45.423  -35.246 10.694  1.00 74.13  ? 493 VAL D CB  1 
ATOM   16694 C CG1 . VAL D 1 493 ? 44.318  -34.512 9.958   1.00 72.94  ? 493 VAL D CG1 1 
ATOM   16695 C CG2 . VAL D 1 493 ? 46.734  -34.496 10.494  1.00 74.43  ? 493 VAL D CG2 1 
ATOM   16696 N N   . VAL D 1 494 ? 45.818  -33.499 13.401  1.00 75.08  ? 494 VAL D N   1 
ATOM   16697 C CA  . VAL D 1 494 ? 45.651  -32.264 14.133  1.00 75.21  ? 494 VAL D CA  1 
ATOM   16698 C C   . VAL D 1 494 ? 46.683  -31.276 13.613  1.00 75.42  ? 494 VAL D C   1 
ATOM   16699 O O   . VAL D 1 494 ? 47.788  -31.682 13.280  1.00 75.71  ? 494 VAL D O   1 
ATOM   16700 C CB  . VAL D 1 494 ? 45.750  -32.428 15.663  1.00 76.62  ? 494 VAL D CB  1 
ATOM   16701 C CG1 . VAL D 1 494 ? 47.107  -32.930 16.128  1.00 77.46  ? 494 VAL D CG1 1 
ATOM   16702 C CG2 . VAL D 1 494 ? 45.400  -31.116 16.363  1.00 76.89  ? 494 VAL D CG2 1 
ATOM   16703 N N   . ASN D 1 495 ? 46.286  -29.994 13.523  1.00 75.79  ? 495 ASN D N   1 
ATOM   16704 C CA  . ASN D 1 495 ? 47.211  -28.896 13.271  1.00 75.21  ? 495 ASN D CA  1 
ATOM   16705 C C   . ASN D 1 495 ? 47.277  -28.080 14.555  1.00 75.42  ? 495 ASN D C   1 
ATOM   16706 O O   . ASN D 1 495 ? 46.302  -27.423 14.925  1.00 76.30  ? 495 ASN D O   1 
ATOM   16707 C CB  . ASN D 1 495 ? 46.785  -28.051 12.074  1.00 73.95  ? 495 ASN D CB  1 
ATOM   16708 C CG  . ASN D 1 495 ? 47.644  -26.823 11.878  1.00 74.32  ? 495 ASN D CG  1 
ATOM   16709 O OD1 . ASN D 1 495 ? 48.162  -26.255 12.847  1.00 75.66  ? 495 ASN D OD1 1 
ATOM   16710 N ND2 . ASN D 1 495 ? 47.803  -26.381 10.639  1.00 73.37  ? 495 ASN D ND2 1 
ATOM   16711 N N   . ALA D 1 496 ? 48.414  -28.175 15.244  1.00 75.31  ? 496 ALA D N   1 
ATOM   16712 C CA  . ALA D 1 496 ? 48.601  -27.513 16.520  1.00 75.80  ? 496 ALA D CA  1 
ATOM   16713 C C   . ALA D 1 496 ? 49.375  -26.218 16.300  1.00 74.82  ? 496 ALA D C   1 
ATOM   16714 O O   . ALA D 1 496 ? 50.587  -26.263 16.061  1.00 76.67  ? 496 ALA D O   1 
ATOM   16715 C CB  . ALA D 1 496 ? 49.345  -28.444 17.455  1.00 78.16  ? 496 ALA D CB  1 
ATOM   16716 N N   . SER D 1 497 ? 48.689  -25.071 16.386  1.00 72.14  ? 497 SER D N   1 
ATOM   16717 C CA  . SER D 1 497 ? 49.358  -23.807 16.135  1.00 70.75  ? 497 SER D CA  1 
ATOM   16718 C C   . SER D 1 497 ? 49.208  -22.853 17.318  1.00 70.94  ? 497 SER D C   1 
ATOM   16719 O O   . SER D 1 497 ? 48.422  -23.092 18.218  1.00 71.61  ? 497 SER D O   1 
ATOM   16720 C CB  . SER D 1 497 ? 48.899  -23.205 14.851  1.00 68.76  ? 497 SER D CB  1 
ATOM   16721 O OG  . SER D 1 497 ? 47.566  -22.747 14.960  1.00 68.64  ? 497 SER D OG  1 
ATOM   16722 N N   . ALA D 1 498 ? 50.042  -21.811 17.352  1.00 71.16  ? 498 ALA D N   1 
ATOM   16723 C CA  . ALA D 1 498 ? 49.986  -20.788 18.383  1.00 72.05  ? 498 ALA D CA  1 
ATOM   16724 C C   . ALA D 1 498 ? 50.577  -19.505 17.808  1.00 72.05  ? 498 ALA D C   1 
ATOM   16725 O O   . ALA D 1 498 ? 51.576  -19.546 17.094  1.00 73.21  ? 498 ALA D O   1 
ATOM   16726 C CB  . ALA D 1 498 ? 50.734  -21.228 19.627  1.00 73.60  ? 498 ALA D CB  1 
ATOM   16727 N N   . GLY D 1 499 ? 49.972  -18.363 18.121  1.00 71.25  ? 499 GLY D N   1 
ATOM   16728 C CA  . GLY D 1 499 ? 50.393  -17.121 17.502  1.00 70.66  ? 499 GLY D CA  1 
ATOM   16729 C C   . GLY D 1 499 ? 50.117  -15.912 18.393  1.00 71.63  ? 499 GLY D C   1 
ATOM   16730 O O   . GLY D 1 499 ? 49.287  -15.967 19.307  1.00 72.68  ? 499 GLY D O   1 
ATOM   16731 N N   . ILE D 1 500 ? 50.828  -14.816 18.086  1.00 71.13  ? 500 ILE D N   1 
ATOM   16732 C CA  . ILE D 1 500 ? 50.703  -13.553 18.794  1.00 70.80  ? 500 ILE D CA  1 
ATOM   16733 C C   . ILE D 1 500 ? 51.145  -12.460 17.824  1.00 70.81  ? 500 ILE D C   1 
ATOM   16734 O O   . ILE D 1 500 ? 52.015  -12.722 16.985  1.00 70.33  ? 500 ILE D O   1 
ATOM   16735 C CB  . ILE D 1 500 ? 51.538  -13.589 20.085  1.00 71.69  ? 500 ILE D CB  1 
ATOM   16736 C CG1 . ILE D 1 500 ? 51.078  -12.581 21.097  1.00 72.14  ? 500 ILE D CG1 1 
ATOM   16737 C CG2 . ILE D 1 500 ? 53.013  -13.419 19.755  1.00 72.48  ? 500 ILE D CG2 1 
ATOM   16738 C CD1 . ILE D 1 500 ? 51.780  -12.675 22.438  1.00 74.07  ? 500 ILE D CD1 1 
ATOM   16739 N N   . SER D 1 501 ? 50.515  -11.270 17.921  1.00 71.26  ? 501 SER D N   1 
ATOM   16740 C CA  . SER D 1 501 ? 50.862  -10.116 17.096  1.00 71.60  ? 501 SER D CA  1 
ATOM   16741 C C   . SER D 1 501 ? 52.029  -9.305  17.692  1.00 72.82  ? 501 SER D C   1 
ATOM   16742 O O   . SER D 1 501 ? 52.115  -9.115  18.905  1.00 73.76  ? 501 SER D O   1 
ATOM   16743 C CB  . SER D 1 501 ? 49.667  -9.237  16.909  1.00 71.75  ? 501 SER D CB  1 
ATOM   16744 O OG  . SER D 1 501 ? 48.490  -9.948  16.553  1.00 72.27  ? 501 SER D OG  1 
ATOM   16745 N N   . VAL D 1 502 ? 52.923  -8.797  16.826  1.00 73.03  ? 502 VAL D N   1 
ATOM   16746 C CA  . VAL D 1 502 ? 54.065  -7.981  17.253  1.00 75.83  ? 502 VAL D CA  1 
ATOM   16747 C C   . VAL D 1 502 ? 53.983  -6.606  16.573  1.00 75.79  ? 502 VAL D C   1 
ATOM   16748 O O   . VAL D 1 502 ? 53.425  -6.467  15.486  1.00 77.78  ? 502 VAL D O   1 
ATOM   16749 C CB  . VAL D 1 502 ? 55.435  -8.654  16.987  1.00 75.24  ? 502 VAL D CB  1 
ATOM   16750 C CG1 . VAL D 1 502 ? 56.596  -7.863  17.572  1.00 76.54  ? 502 VAL D CG1 1 
ATOM   16751 C CG2 . VAL D 1 502 ? 55.506  -10.070 17.529  1.00 75.79  ? 502 VAL D CG2 1 
ATOM   16752 N N   . ARG D 1 503 ? 54.528  -5.568  17.209  1.00 76.01  ? 503 ARG D N   1 
ATOM   16753 C CA  . ARG D 1 503 ? 54.465  -4.236  16.620  1.00 75.62  ? 503 ARG D CA  1 
ATOM   16754 C C   . ARG D 1 503 ? 55.834  -3.584  16.732  1.00 75.10  ? 503 ARG D C   1 
ATOM   16755 O O   . ARG D 1 503 ? 56.474  -3.685  17.770  1.00 75.16  ? 503 ARG D O   1 
ATOM   16756 C CB  . ARG D 1 503 ? 53.433  -3.296  17.265  1.00 76.55  ? 503 ARG D CB  1 
ATOM   16757 C CG  . ARG D 1 503 ? 53.460  -1.870  16.728  1.00 77.92  ? 503 ARG D CG  1 
ATOM   16758 C CD  . ARG D 1 503 ? 52.830  -0.824  17.655  1.00 79.04  ? 503 ARG D CD  1 
ATOM   16759 N NE  . ARG D 1 503 ? 51.387  -1.044  17.679  1.00 80.40  ? 503 ARG D NE  1 
ATOM   16760 C CZ  . ARG D 1 503 ? 50.625  -1.085  16.582  1.00 82.02  ? 503 ARG D CZ  1 
ATOM   16761 N NH1 . ARG D 1 503 ? 51.112  -0.631  15.428  1.00 81.14  ? 503 ARG D NH1 1 
ATOM   16762 N NH2 . ARG D 1 503 ? 49.384  -1.578  16.651  1.00 81.48  ? 503 ARG D NH2 1 
ATOM   16763 N N   . TYR D 1 504 ? 56.239  -2.942  15.633  1.00 73.89  ? 504 TYR D N   1 
ATOM   16764 C CA  . TYR D 1 504 ? 57.427  -2.116  15.573  1.00 75.16  ? 504 TYR D CA  1 
ATOM   16765 C C   . TYR D 1 504 ? 57.065  -0.837  14.816  1.00 73.77  ? 504 TYR D C   1 
ATOM   16766 O O   . TYR D 1 504 ? 56.853  -0.879  13.607  1.00 73.27  ? 504 TYR D O   1 
ATOM   16767 C CB  . TYR D 1 504 ? 58.571  -2.868  14.887  1.00 75.97  ? 504 TYR D CB  1 
ATOM   16768 C CG  . TYR D 1 504 ? 59.882  -2.086  14.886  1.00 78.57  ? 504 TYR D CG  1 
ATOM   16769 C CD1 . TYR D 1 504 ? 60.182  -1.152  13.893  1.00 77.53  ? 504 TYR D CD1 1 
ATOM   16770 C CD2 . TYR D 1 504 ? 60.820  -2.285  15.891  1.00 80.58  ? 504 TYR D CD2 1 
ATOM   16771 C CE1 . TYR D 1 504 ? 61.380  -0.472  13.883  1.00 78.27  ? 504 TYR D CE1 1 
ATOM   16772 C CE2 . TYR D 1 504 ? 62.015  -1.593  15.901  1.00 81.64  ? 504 TYR D CE2 1 
ATOM   16773 C CZ  . TYR D 1 504 ? 62.284  -0.684  14.901  1.00 81.15  ? 504 TYR D CZ  1 
ATOM   16774 O OH  . TYR D 1 504 ? 63.469  -0.022  14.926  1.00 85.15  ? 504 TYR D OH  1 
ATOM   16775 N N   . GLY D 1 505 ? 56.976  0.299   15.508  1.00 72.50  ? 505 GLY D N   1 
ATOM   16776 C CA  . GLY D 1 505 ? 56.437  1.456   14.838  1.00 71.57  ? 505 GLY D CA  1 
ATOM   16777 C C   . GLY D 1 505 ? 55.090  1.102   14.209  1.00 70.43  ? 505 GLY D C   1 
ATOM   16778 O O   . GLY D 1 505 ? 54.216  0.566   14.884  1.00 70.68  ? 505 GLY D O   1 
ATOM   16779 N N   . LYS D 1 506 ? 54.932  1.369   12.904  1.00 69.38  ? 506 LYS D N   1 
ATOM   16780 C CA  . LYS D 1 506 ? 53.636  1.252   12.247  1.00 67.09  ? 506 LYS D CA  1 
ATOM   16781 C C   . LYS D 1 506 ? 53.430  -0.148  11.675  1.00 66.18  ? 506 LYS D C   1 
ATOM   16782 O O   . LYS D 1 506 ? 52.374  -0.447  11.126  1.00 65.95  ? 506 LYS D O   1 
ATOM   16783 C CB  . LYS D 1 506 ? 53.484  2.244   11.088  1.00 65.92  ? 506 LYS D CB  1 
ATOM   16784 C CG  . LYS D 1 506 ? 53.338  3.715   11.423  1.00 66.21  ? 506 LYS D CG  1 
ATOM   16785 C CD  . LYS D 1 506 ? 53.072  4.523   10.147  1.00 66.41  ? 506 LYS D CD  1 
ATOM   16786 C CE  . LYS D 1 506 ? 53.340  6.008   10.247  1.00 68.22  ? 506 LYS D CE  1 
ATOM   16787 N NZ  . LYS D 1 506 ? 53.337  6.766   8.986   1.00 68.44  ? 506 LYS D NZ  1 
ATOM   16788 N N   . PHE D 1 507 ? 54.440  -0.997  11.803  1.00 66.95  ? 507 PHE D N   1 
ATOM   16789 C CA  . PHE D 1 507 ? 54.422  -2.318  11.194  1.00 67.17  ? 507 PHE D CA  1 
ATOM   16790 C C   . PHE D 1 507 ? 54.025  -3.379  12.217  1.00 67.39  ? 507 PHE D C   1 
ATOM   16791 O O   . PHE D 1 507 ? 54.692  -3.596  13.224  1.00 67.66  ? 507 PHE D O   1 
ATOM   16792 C CB  . PHE D 1 507 ? 55.835  -2.543  10.644  1.00 67.88  ? 507 PHE D CB  1 
ATOM   16793 C CG  . PHE D 1 507 ? 56.104  -3.855  9.922   1.00 66.78  ? 507 PHE D CG  1 
ATOM   16794 C CD1 . PHE D 1 507 ? 56.428  -5.003  10.627  1.00 67.05  ? 507 PHE D CD1 1 
ATOM   16795 C CD2 . PHE D 1 507 ? 56.118  -3.908  8.535   1.00 66.01  ? 507 PHE D CD2 1 
ATOM   16796 C CE1 . PHE D 1 507 ? 56.731  -6.179  9.960   1.00 66.60  ? 507 PHE D CE1 1 
ATOM   16797 C CE2 . PHE D 1 507 ? 56.389  -5.093  7.873   1.00 65.54  ? 507 PHE D CE2 1 
ATOM   16798 C CZ  . PHE D 1 507 ? 56.711  -6.220  8.586   1.00 65.94  ? 507 PHE D CZ  1 
ATOM   16799 N N   . THR D 1 508 ? 52.919  -4.053  11.937  1.00 67.65  ? 508 THR D N   1 
ATOM   16800 C CA  . THR D 1 508 ? 52.461  -5.152  12.779  1.00 68.12  ? 508 THR D CA  1 
ATOM   16801 C C   . THR D 1 508 ? 52.386  -6.423  11.964  1.00 65.14  ? 508 THR D C   1 
ATOM   16802 O O   . THR D 1 508 ? 52.144  -6.406  10.768  1.00 62.91  ? 508 THR D O   1 
ATOM   16803 C CB  . THR D 1 508 ? 51.105  -4.801  13.355  1.00 70.23  ? 508 THR D CB  1 
ATOM   16804 O OG1 . THR D 1 508 ? 50.537  -4.116  12.239  1.00 71.73  ? 508 THR D OG1 1 
ATOM   16805 C CG2 . THR D 1 508 ? 51.243  -3.849  14.526  1.00 72.64  ? 508 THR D CG2 1 
ATOM   16806 N N   . PHE D 1 509 ? 52.644  -7.525  12.646  1.00 65.39  ? 509 PHE D N   1 
ATOM   16807 C CA  . PHE D 1 509 ? 52.877  -8.786  11.987  1.00 64.95  ? 509 PHE D CA  1 
ATOM   16808 C C   . PHE D 1 509 ? 52.735  -9.838  13.068  1.00 66.80  ? 509 PHE D C   1 
ATOM   16809 O O   . PHE D 1 509 ? 52.553  -9.457  14.227  1.00 66.73  ? 509 PHE D O   1 
ATOM   16810 C CB  . PHE D 1 509 ? 54.261  -8.735  11.341  1.00 65.79  ? 509 PHE D CB  1 
ATOM   16811 C CG  . PHE D 1 509 ? 55.451  -8.866  12.294  1.00 67.19  ? 509 PHE D CG  1 
ATOM   16812 C CD1 . PHE D 1 509 ? 55.915  -7.763  13.008  1.00 67.87  ? 509 PHE D CD1 1 
ATOM   16813 C CD2 . PHE D 1 509 ? 56.110  -10.085 12.465  1.00 67.55  ? 509 PHE D CD2 1 
ATOM   16814 C CE1 . PHE D 1 509 ? 57.009  -7.872  13.861  1.00 69.90  ? 509 PHE D CE1 1 
ATOM   16815 C CE2 . PHE D 1 509 ? 57.208  -10.184 13.313  1.00 69.26  ? 509 PHE D CE2 1 
ATOM   16816 C CZ  . PHE D 1 509 ? 57.653  -9.079  14.013  1.00 70.34  ? 509 PHE D CZ  1 
ATOM   16817 N N   . LYS D 1 510 ? 52.866  -11.121 12.677  1.00 68.34  ? 510 LYS D N   1 
ATOM   16818 C CA  . LYS D 1 510 ? 52.604  -12.228 13.580  1.00 69.34  ? 510 LYS D CA  1 
ATOM   16819 C C   . LYS D 1 510 ? 53.806  -13.161 13.678  1.00 71.25  ? 510 LYS D C   1 
ATOM   16820 O O   . LYS D 1 510 ? 54.603  -13.301 12.750  1.00 73.28  ? 510 LYS D O   1 
ATOM   16821 C CB  . LYS D 1 510 ? 51.303  -12.874 13.120  1.00 68.05  ? 510 LYS D CB  1 
ATOM   16822 C CG  . LYS D 1 510 ? 50.126  -12.042 13.578  1.00 68.21  ? 510 LYS D CG  1 
ATOM   16823 C CD  . LYS D 1 510 ? 48.768  -12.720 13.412  1.00 68.18  ? 510 LYS D CD  1 
ATOM   16824 C CE  . LYS D 1 510 ? 47.825  -12.520 14.573  1.00 68.72  ? 510 LYS D CE  1 
ATOM   16825 N NZ  . LYS D 1 510 ? 48.247  -13.332 15.726  1.00 69.78  ? 510 LYS D NZ  1 
ATOM   16826 N N   . ILE D 1 511 ? 53.949  -13.762 14.860  1.00 71.02  ? 511 ILE D N   1 
ATOM   16827 C CA  . ILE D 1 511 ? 54.946  -14.783 15.084  1.00 70.60  ? 511 ILE D CA  1 
ATOM   16828 C C   . ILE D 1 511 ? 54.199  -15.973 15.651  1.00 71.02  ? 511 ILE D C   1 
ATOM   16829 O O   . ILE D 1 511 ? 53.279  -15.785 16.443  1.00 70.83  ? 511 ILE D O   1 
ATOM   16830 C CB  . ILE D 1 511 ? 56.058  -14.313 16.033  1.00 71.23  ? 511 ILE D CB  1 
ATOM   16831 C CG1 . ILE D 1 511 ? 55.516  -13.946 17.410  1.00 71.77  ? 511 ILE D CG1 1 
ATOM   16832 C CG2 . ILE D 1 511 ? 56.844  -13.176 15.405  1.00 70.92  ? 511 ILE D CG2 1 
ATOM   16833 C CD1 . ILE D 1 511 ? 56.580  -13.646 18.447  1.00 73.56  ? 511 ILE D CD1 1 
ATOM   16834 N N   . HIS D 1 512 ? 54.639  -17.176 15.266  1.00 71.74  ? 512 HIS D N   1 
ATOM   16835 C CA  . HIS D 1 512 ? 53.765  -18.331 15.320  1.00 71.78  ? 512 HIS D CA  1 
ATOM   16836 C C   . HIS D 1 512 ? 54.504  -19.621 14.987  1.00 72.60  ? 512 HIS D C   1 
ATOM   16837 O O   . HIS D 1 512 ? 55.626  -19.620 14.506  1.00 74.88  ? 512 HIS D O   1 
ATOM   16838 C CB  . HIS D 1 512 ? 52.653  -18.146 14.289  1.00 70.13  ? 512 HIS D CB  1 
ATOM   16839 C CG  . HIS D 1 512 ? 53.187  -17.789 12.935  1.00 69.65  ? 512 HIS D CG  1 
ATOM   16840 N ND1 . HIS D 1 512 ? 53.873  -18.681 12.131  1.00 69.92  ? 512 HIS D ND1 1 
ATOM   16841 C CD2 . HIS D 1 512 ? 53.156  -16.631 12.262  1.00 69.06  ? 512 HIS D CD2 1 
ATOM   16842 C CE1 . HIS D 1 512 ? 54.196  -18.084 10.991  1.00 68.84  ? 512 HIS D CE1 1 
ATOM   16843 N NE2 . HIS D 1 512 ? 53.778  -16.841 11.056  1.00 68.64  ? 512 HIS D NE2 1 
ATOM   16844 N N   . ASP D 1 513 ? 53.826  -20.735 15.205  1.00 72.36  ? 513 ASP D N   1 
ATOM   16845 C CA  . ASP D 1 513 ? 54.407  -22.030 14.947  1.00 72.91  ? 513 ASP D CA  1 
ATOM   16846 C C   . ASP D 1 513 ? 53.254  -23.006 14.755  1.00 72.05  ? 513 ASP D C   1 
ATOM   16847 O O   . ASP D 1 513 ? 52.174  -22.753 15.265  1.00 71.07  ? 513 ASP D O   1 
ATOM   16848 C CB  . ASP D 1 513 ? 55.323  -22.401 16.098  1.00 75.11  ? 513 ASP D CB  1 
ATOM   16849 C CG  . ASP D 1 513 ? 56.350  -23.470 15.782  1.00 76.33  ? 513 ASP D CG  1 
ATOM   16850 O OD1 . ASP D 1 513 ? 56.580  -23.705 14.583  1.00 75.78  ? 513 ASP D OD1 1 
ATOM   16851 O OD2 . ASP D 1 513 ? 56.889  -24.056 16.737  1.00 78.58  ? 513 ASP D OD2 1 
ATOM   16852 N N   . GLN D 1 514 ? 53.524  -24.127 14.072  1.00 72.59  ? 514 GLN D N   1 
ATOM   16853 C CA  . GLN D 1 514 ? 52.515  -25.065 13.608  1.00 71.53  ? 514 GLN D CA  1 
ATOM   16854 C C   . GLN D 1 514 ? 53.069  -26.484 13.517  1.00 72.42  ? 514 GLN D C   1 
ATOM   16855 O O   . GLN D 1 514 ? 54.073  -26.712 12.852  1.00 72.27  ? 514 GLN D O   1 
ATOM   16856 C CB  . GLN D 1 514 ? 52.188  -24.607 12.195  1.00 70.40  ? 514 GLN D CB  1 
ATOM   16857 C CG  . GLN D 1 514 ? 51.186  -25.479 11.458  1.00 70.37  ? 514 GLN D CG  1 
ATOM   16858 C CD  . GLN D 1 514 ? 51.041  -25.070 10.011  1.00 70.14  ? 514 GLN D CD  1 
ATOM   16859 O OE1 . GLN D 1 514 ? 50.190  -24.247 9.644   1.00 70.42  ? 514 GLN D OE1 1 
ATOM   16860 N NE2 . GLN D 1 514 ? 51.914  -25.619 9.181   1.00 70.50  ? 514 GLN D NE2 1 
ATOM   16861 N N   . LYS D 1 515 ? 52.371  -27.442 14.127  1.00 72.94  ? 515 LYS D N   1 
ATOM   16862 C CA  . LYS D 1 515 ? 52.748  -28.840 14.020  1.00 74.95  ? 515 LYS D CA  1 
ATOM   16863 C C   . LYS D 1 515 ? 51.586  -29.662 13.454  1.00 73.40  ? 515 LYS D C   1 
ATOM   16864 O O   . LYS D 1 515 ? 50.447  -29.532 13.893  1.00 74.02  ? 515 LYS D O   1 
ATOM   16865 C CB  . LYS D 1 515 ? 53.200  -29.374 15.387  1.00 78.07  ? 515 LYS D CB  1 
ATOM   16866 C CG  . LYS D 1 515 ? 54.447  -28.730 16.011  1.00 80.20  ? 515 LYS D CG  1 
ATOM   16867 C CD  . LYS D 1 515 ? 55.713  -28.793 15.161  1.00 81.35  ? 515 LYS D CD  1 
ATOM   16868 C CE  . LYS D 1 515 ? 56.899  -28.187 15.839  1.00 83.99  ? 515 LYS D CE  1 
ATOM   16869 N NZ  . LYS D 1 515 ? 57.488  -27.114 15.011  1.00 84.65  ? 515 LYS D NZ  1 
ATOM   16870 N N   . ILE D 1 516 ? 51.890  -30.527 12.484  1.00 71.91  ? 516 ILE D N   1 
ATOM   16871 C CA  . ILE D 1 516 ? 50.905  -31.401 11.880  1.00 70.18  ? 516 ILE D CA  1 
ATOM   16872 C C   . ILE D 1 516 ? 51.243  -32.827 12.298  1.00 71.88  ? 516 ILE D C   1 
ATOM   16873 O O   . ILE D 1 516 ? 52.292  -33.344 11.932  1.00 72.03  ? 516 ILE D O   1 
ATOM   16874 C CB  . ILE D 1 516 ? 50.878  -31.207 10.356  1.00 68.15  ? 516 ILE D CB  1 
ATOM   16875 C CG1 . ILE D 1 516 ? 50.521  -29.769 10.002  1.00 66.52  ? 516 ILE D CG1 1 
ATOM   16876 C CG2 . ILE D 1 516 ? 49.944  -32.208 9.688   1.00 67.70  ? 516 ILE D CG2 1 
ATOM   16877 C CD1 . ILE D 1 516 ? 50.292  -29.506 8.520   1.00 65.24  ? 516 ILE D CD1 1 
ATOM   16878 N N   . ILE D 1 517 ? 50.334  -33.427 13.075  1.00 73.16  ? 517 ILE D N   1 
ATOM   16879 C CA  . ILE D 1 517 ? 50.562  -34.678 13.780  1.00 75.96  ? 517 ILE D CA  1 
ATOM   16880 C C   . ILE D 1 517 ? 49.404  -35.647 13.515  1.00 76.71  ? 517 ILE D C   1 
ATOM   16881 O O   . ILE D 1 517 ? 48.249  -35.300 13.743  1.00 75.77  ? 517 ILE D O   1 
ATOM   16882 C CB  . ILE D 1 517 ? 50.711  -34.440 15.293  1.00 77.39  ? 517 ILE D CB  1 
ATOM   16883 C CG1 . ILE D 1 517 ? 51.641  -33.285 15.604  1.00 77.31  ? 517 ILE D CG1 1 
ATOM   16884 C CG2 . ILE D 1 517 ? 51.141  -35.733 16.000  1.00 79.60  ? 517 ILE D CG2 1 
ATOM   16885 C CD1 . ILE D 1 517 ? 51.540  -32.813 17.043  1.00 78.56  ? 517 ILE D CD1 1 
ATOM   16886 N N   . TYR D 1 518 ? 49.734  -36.888 13.112  1.00 78.27  ? 518 TYR D N   1 
ATOM   16887 C CA  . TYR D 1 518 ? 48.744  -37.843 12.637  1.00 78.66  ? 518 TYR D CA  1 
ATOM   16888 C C   . TYR D 1 518 ? 48.411  -38.845 13.741  1.00 80.72  ? 518 TYR D C   1 
ATOM   16889 O O   . TYR D 1 518 ? 49.148  -38.976 14.715  1.00 82.72  ? 518 TYR D O   1 
ATOM   16890 C CB  . TYR D 1 518 ? 49.289  -38.579 11.406  1.00 79.20  ? 518 TYR D CB  1 
ATOM   16891 C CG  . TYR D 1 518 ? 49.595  -37.700 10.203  1.00 77.76  ? 518 TYR D CG  1 
ATOM   16892 C CD1 . TYR D 1 518 ? 48.600  -37.311 9.330   1.00 76.81  ? 518 TYR D CD1 1 
ATOM   16893 C CD2 . TYR D 1 518 ? 50.879  -37.279 9.925   1.00 78.62  ? 518 TYR D CD2 1 
ATOM   16894 C CE1 . TYR D 1 518 ? 48.860  -36.503 8.235   1.00 76.38  ? 518 TYR D CE1 1 
ATOM   16895 C CE2 . TYR D 1 518 ? 51.157  -36.481 8.828   1.00 78.19  ? 518 TYR D CE2 1 
ATOM   16896 C CZ  . TYR D 1 518 ? 50.146  -36.091 7.970   1.00 77.27  ? 518 TYR D CZ  1 
ATOM   16897 O OH  . TYR D 1 518 ? 50.394  -35.274 6.893   1.00 77.68  ? 518 TYR D OH  1 
ATOM   16898 N N   . ARG D 1 519 ? 47.285  -39.556 13.580  1.00 80.89  ? 519 ARG D N   1 
ATOM   16899 C CA  . ARG D 1 519 ? 47.008  -40.760 14.357  1.00 82.21  ? 519 ARG D CA  1 
ATOM   16900 C C   . ARG D 1 519 ? 47.453  -41.985 13.564  1.00 81.93  ? 519 ARG D C   1 
ATOM   16901 O O   . ARG D 1 519 ? 47.079  -42.162 12.411  1.00 80.41  ? 519 ARG D O   1 
ATOM   16902 C CB  . ARG D 1 519 ? 45.534  -40.981 14.719  1.00 81.69  ? 519 ARG D CB  1 
ATOM   16903 C CG  . ARG D 1 519 ? 45.358  -42.227 15.577  1.00 83.33  ? 519 ARG D CG  1 
ATOM   16904 C CD  . ARG D 1 519 ? 43.910  -42.525 15.867  1.00 83.13  ? 519 ARG D CD  1 
ATOM   16905 N NE  . ARG D 1 519 ? 43.201  -41.468 16.592  1.00 82.81  ? 519 ARG D NE  1 
ATOM   16906 C CZ  . ARG D 1 519 ? 43.396  -41.051 17.850  1.00 83.95  ? 519 ARG D CZ  1 
ATOM   16907 N NH1 . ARG D 1 519 ? 44.239  -41.693 18.660  1.00 84.97  ? 519 ARG D NH1 1 
ATOM   16908 N NH2 . ARG D 1 519 ? 42.701  -39.989 18.284  1.00 82.90  ? 519 ARG D NH2 1 
ATOM   16909 N N   . GLY D 1 520 ? 48.246  -42.841 14.200  1.00 83.73  ? 520 GLY D N   1 
ATOM   16910 C CA  . GLY D 1 520 ? 48.765  -44.026 13.532  1.00 84.57  ? 520 GLY D CA  1 
ATOM   16911 C C   . GLY D 1 520 ? 49.473  -43.684 12.220  1.00 83.02  ? 520 GLY D C   1 
ATOM   16912 O O   . GLY D 1 520 ? 50.178  -42.676 12.133  1.00 82.60  ? 520 GLY D O   1 
ATOM   16913 N N   . ASP D 1 521 ? 49.259  -44.523 11.198  1.00 82.53  ? 521 ASP D N   1 
ATOM   16914 C CA  . ASP D 1 521 ? 50.019  -44.431 9.961   1.00 81.69  ? 521 ASP D CA  1 
ATOM   16915 C C   . ASP D 1 521 ? 49.077  -44.390 8.764   1.00 79.49  ? 521 ASP D C   1 
ATOM   16916 O O   . ASP D 1 521 ? 49.469  -44.775 7.661   1.00 78.72  ? 521 ASP D O   1 
ATOM   16917 C CB  . ASP D 1 521 ? 50.991  -45.590 9.819   1.00 83.86  ? 521 ASP D CB  1 
ATOM   16918 C CG  . ASP D 1 521 ? 50.307  -46.939 9.775   1.00 85.22  ? 521 ASP D CG  1 
ATOM   16919 O OD1 . ASP D 1 521 ? 49.174  -47.012 10.282  1.00 85.13  ? 521 ASP D OD1 1 
ATOM   16920 O OD2 . ASP D 1 521 ? 50.889  -47.869 9.193   1.00 86.86  ? 521 ASP D OD2 1 
ATOM   16921 N N   . TRP D 1 522 ? 47.863  -43.865 8.982   1.00 77.92  ? 522 TRP D N   1 
ATOM   16922 C CA  . TRP D 1 522 ? 46.859  -43.864 7.941   1.00 76.43  ? 522 TRP D CA  1 
ATOM   16923 C C   . TRP D 1 522 ? 47.319  -42.982 6.785   1.00 75.53  ? 522 TRP D C   1 
ATOM   16924 O O   . TRP D 1 522 ? 46.956  -43.193 5.637   1.00 74.24  ? 522 TRP D O   1 
ATOM   16925 C CB  . TRP D 1 522 ? 45.520  -43.421 8.531   1.00 75.73  ? 522 TRP D CB  1 
ATOM   16926 C CG  . TRP D 1 522 ? 45.405  -41.938 8.762   1.00 74.48  ? 522 TRP D CG  1 
ATOM   16927 C CD1 . TRP D 1 522 ? 45.791  -41.229 9.863   1.00 74.88  ? 522 TRP D CD1 1 
ATOM   16928 C CD2 . TRP D 1 522 ? 44.861  -40.972 7.841   1.00 72.39  ? 522 TRP D CD2 1 
ATOM   16929 N NE1 . TRP D 1 522 ? 45.537  -39.894 9.694   1.00 72.98  ? 522 TRP D NE1 1 
ATOM   16930 C CE2 . TRP D 1 522 ? 44.970  -39.707 8.462   1.00 71.85  ? 522 TRP D CE2 1 
ATOM   16931 C CE3 . TRP D 1 522 ? 44.310  -41.057 6.559   1.00 71.27  ? 522 TRP D CE3 1 
ATOM   16932 C CZ2 . TRP D 1 522 ? 44.522  -38.539 7.845   1.00 70.48  ? 522 TRP D CZ2 1 
ATOM   16933 C CZ3 . TRP D 1 522 ? 43.899  -39.899 5.940   1.00 70.08  ? 522 TRP D CZ3 1 
ATOM   16934 C CH2 . TRP D 1 522 ? 43.991  -38.658 6.579   1.00 69.49  ? 522 TRP D CH2 1 
ATOM   16935 N N   . ALA D 1 523 ? 48.167  -42.002 7.078   1.00 76.68  ? 523 ALA D N   1 
ATOM   16936 C CA  . ALA D 1 523 ? 48.518  -41.032 6.060   1.00 77.39  ? 523 ALA D CA  1 
ATOM   16937 C C   . ALA D 1 523 ? 49.909  -41.323 5.503   1.00 80.27  ? 523 ALA D C   1 
ATOM   16938 O O   . ALA D 1 523 ? 50.622  -40.417 5.084   1.00 80.63  ? 523 ALA D O   1 
ATOM   16939 C CB  . ALA D 1 523 ? 48.396  -39.630 6.635   1.00 76.52  ? 523 ALA D CB  1 
ATOM   16940 N N   . LYS D 1 524 ? 50.282  -42.601 5.432   1.00 83.85  ? 524 LYS D N   1 
ATOM   16941 C CA  . LYS D 1 524 ? 51.602  -42.942 4.938   1.00 86.02  ? 524 LYS D CA  1 
ATOM   16942 C C   . LYS D 1 524 ? 51.717  -42.570 3.459   1.00 84.72  ? 524 LYS D C   1 
ATOM   16943 O O   . LYS D 1 524 ? 52.829  -42.433 2.954   1.00 85.88  ? 524 LYS D O   1 
ATOM   16944 C CB  . LYS D 1 524 ? 51.928  -44.411 5.226   1.00 90.73  ? 524 LYS D CB  1 
ATOM   16945 C CG  . LYS D 1 524 ? 50.914  -45.407 4.674   1.00 93.41  ? 524 LYS D CG  1 
ATOM   16946 C CD  . LYS D 1 524 ? 51.089  -46.878 5.065   1.00 95.50  ? 524 LYS D CD  1 
ATOM   16947 C CE  . LYS D 1 524 ? 49.801  -47.614 4.857   1.00 95.80  ? 524 LYS D CE  1 
ATOM   16948 N NZ  . LYS D 1 524 ? 49.945  -49.013 5.250   1.00 100.34 ? 524 LYS D NZ  1 
ATOM   16949 N N   . GLU D 1 525 ? 50.580  -42.398 2.768   1.00 83.03  ? 525 GLU D N   1 
ATOM   16950 C CA  . GLU D 1 525 ? 50.593  -42.090 1.346   1.00 81.67  ? 525 GLU D CA  1 
ATOM   16951 C C   . GLU D 1 525 ? 50.107  -40.671 1.105   1.00 78.88  ? 525 GLU D C   1 
ATOM   16952 O O   . GLU D 1 525 ? 50.775  -39.880 0.450   1.00 79.54  ? 525 GLU D O   1 
ATOM   16953 C CB  . GLU D 1 525 ? 49.680  -43.010 0.536   1.00 83.11  ? 525 GLU D CB  1 
ATOM   16954 C CG  . GLU D 1 525 ? 50.104  -44.479 0.543   1.00 85.50  ? 525 GLU D CG  1 
ATOM   16955 C CD  . GLU D 1 525 ? 49.484  -45.346 1.627   1.00 87.87  ? 525 GLU D CD  1 
ATOM   16956 O OE1 . GLU D 1 525 ? 48.604  -44.811 2.356   1.00 89.38  ? 525 GLU D OE1 1 
ATOM   16957 O OE2 . GLU D 1 525 ? 49.870  -46.553 1.731   1.00 89.60  ? 525 GLU D OE2 1 
ATOM   16958 N N   . VAL D 1 526 ? 48.924  -40.365 1.627   1.00 77.05  ? 526 VAL D N   1 
ATOM   16959 C CA  . VAL D 1 526 ? 48.204  -39.169 1.227   1.00 74.76  ? 526 VAL D CA  1 
ATOM   16960 C C   . VAL D 1 526 ? 48.907  -37.926 1.782   1.00 74.46  ? 526 VAL D C   1 
ATOM   16961 O O   . VAL D 1 526 ? 48.838  -36.862 1.161   1.00 72.38  ? 526 VAL D O   1 
ATOM   16962 C CB  . VAL D 1 526 ? 46.718  -39.238 1.646   1.00 73.55  ? 526 VAL D CB  1 
ATOM   16963 C CG1 . VAL D 1 526 ? 46.535  -39.270 3.157   1.00 73.89  ? 526 VAL D CG1 1 
ATOM   16964 C CG2 . VAL D 1 526 ? 45.903  -38.093 1.060   1.00 72.12  ? 526 VAL D CG2 1 
ATOM   16965 N N   . GLY D 1 527 ? 49.575  -38.079 2.939   1.00 75.63  ? 527 GLY D N   1 
ATOM   16966 C CA  . GLY D 1 527 ? 50.141  -36.964 3.684   1.00 75.09  ? 527 GLY D CA  1 
ATOM   16967 C C   . GLY D 1 527 ? 51.517  -36.539 3.173   1.00 76.01  ? 527 GLY D C   1 
ATOM   16968 O O   . GLY D 1 527 ? 52.231  -37.296 2.498   1.00 75.60  ? 527 GLY D O   1 
ATOM   16969 N N   . ARG D 1 528 ? 51.876  -35.310 3.566   1.00 76.67  ? 528 ARG D N   1 
ATOM   16970 C CA  . ARG D 1 528 ? 53.085  -34.651 3.104   1.00 77.95  ? 528 ARG D CA  1 
ATOM   16971 C C   . ARG D 1 528 ? 54.311  -35.343 3.671   1.00 81.91  ? 528 ARG D C   1 
ATOM   16972 O O   . ARG D 1 528 ? 54.373  -35.533 4.876   1.00 83.62  ? 528 ARG D O   1 
ATOM   16973 C CB  . ARG D 1 528 ? 53.110  -33.203 3.591   1.00 76.25  ? 528 ARG D CB  1 
ATOM   16974 C CG  . ARG D 1 528 ? 54.325  -32.473 3.047   1.00 76.24  ? 528 ARG D CG  1 
ATOM   16975 C CD  . ARG D 1 528 ? 54.354  -31.003 3.402   1.00 74.19  ? 528 ARG D CD  1 
ATOM   16976 N NE  . ARG D 1 528 ? 53.196  -30.300 2.848   1.00 71.42  ? 528 ARG D NE  1 
ATOM   16977 C CZ  . ARG D 1 528 ? 52.182  -29.886 3.585   1.00 69.57  ? 528 ARG D CZ  1 
ATOM   16978 N NH1 . ARG D 1 528 ? 52.095  -30.278 4.845   1.00 70.04  ? 528 ARG D NH1 1 
ATOM   16979 N NH2 . ARG D 1 528 ? 51.247  -29.118 3.049   1.00 67.59  ? 528 ARG D NH2 1 
ATOM   16980 N N   . LYS D 1 529 ? 55.290  -35.630 2.801   1.00 86.00  ? 529 LYS D N   1 
ATOM   16981 C CA  . LYS D 1 529 ? 56.538  -36.292 3.160   1.00 89.56  ? 529 LYS D CA  1 
ATOM   16982 C C   . LYS D 1 529 ? 57.661  -35.288 3.427   1.00 94.05  ? 529 LYS D C   1 
ATOM   16983 O O   . LYS D 1 529 ? 57.500  -34.093 3.207   1.00 93.53  ? 529 LYS D O   1 
ATOM   16984 C CB  . LYS D 1 529 ? 56.988  -37.111 1.947   1.00 90.13  ? 529 LYS D CB  1 
ATOM   16985 C CG  . LYS D 1 529 ? 55.955  -38.094 1.435   1.00 91.17  ? 529 LYS D CG  1 
ATOM   16986 C CD  . LYS D 1 529 ? 55.899  -39.437 2.166   1.00 92.03  ? 529 LYS D CD  1 
ATOM   16987 C CE  . LYS D 1 529 ? 54.491  -39.911 2.380   1.00 91.60  ? 529 LYS D CE  1 
ATOM   16988 N NZ  . LYS D 1 529 ? 53.615  -39.743 1.213   1.00 90.90  ? 529 LYS D NZ  1 
ATOM   16989 N N   . LEU D 1 530 ? 58.823  -35.810 3.855   1.00 104.20 ? 530 LEU D N   1 
ATOM   16990 C CA  . LEU D 1 530 ? 60.099  -35.090 3.912   1.00 107.29 ? 530 LEU D CA  1 
ATOM   16991 C C   . LEU D 1 530 ? 60.034  -33.992 4.995   1.00 106.12 ? 530 LEU D C   1 
ATOM   16992 O O   . LEU D 1 530 ? 60.971  -33.157 5.040   1.00 104.68 ? 530 LEU D O   1 
ATOM   16993 C CB  . LEU D 1 530 ? 60.536  -34.529 2.551   1.00 106.34 ? 530 LEU D CB  1 
ATOM   16994 C CG  . LEU D 1 530 ? 61.124  -35.530 1.544   1.00 106.62 ? 530 LEU D CG  1 
ATOM   16995 C CD1 . LEU D 1 530 ? 61.112  -34.907 0.149   1.00 105.50 ? 530 LEU D CD1 1 
ATOM   16996 C CD2 . LEU D 1 530 ? 62.527  -35.999 1.911   1.00 107.09 ? 530 LEU D CD2 1 
HETATM 16997 C C2  . BGC E 2 .   ? 43.558  22.535  15.610  1.00 105.26 ? 1   BGC E C2  1 
HETATM 16998 C C3  . BGC E 2 .   ? 44.656  22.690  14.567  1.00 105.18 ? 1   BGC E C3  1 
HETATM 16999 C C4  . BGC E 2 .   ? 45.533  21.453  14.512  1.00 98.92  ? 1   BGC E C4  1 
HETATM 17000 C C5  . BGC E 2 .   ? 44.673  20.216  14.367  1.00 95.77  ? 1   BGC E C5  1 
HETATM 17001 C C6  . BGC E 2 .   ? 45.463  18.935  14.292  1.00 88.96  ? 1   BGC E C6  1 
HETATM 17002 C C1  . BGC E 2 .   ? 42.888  21.172  15.559  1.00 93.87  ? 1   BGC E C1  1 
HETATM 17003 O O1  . BGC E 2 .   ? 42.058  20.975  16.644  1.00 84.67  ? 1   BGC E O1  1 
HETATM 17004 O O2  . BGC E 2 .   ? 42.571  23.547  15.444  1.00 101.40 ? 1   BGC E O2  1 
HETATM 17005 O O3  . BGC E 2 .   ? 45.452  23.831  14.877  1.00 95.01  ? 1   BGC E O3  1 
HETATM 17006 O O4  . BGC E 2 .   ? 46.417  21.528  13.405  1.00 80.51  ? 1   BGC E O4  1 
HETATM 17007 O O5  . BGC E 2 .   ? 43.858  20.135  15.531  1.00 90.36  ? 1   BGC E O5  1 
HETATM 17008 O O6  . BGC E 2 .   ? 45.339  18.172  15.488  1.00 85.58  ? 1   BGC E O6  1 
HETATM 17009 C C2  . BGC E 2 .   ? 46.082  26.056  14.623  1.00 39.57  ? 2   BGC E C2  1 
HETATM 17010 C C3  . BGC E 2 .   ? 46.119  27.245  13.698  1.00 42.87  ? 2   BGC E C3  1 
HETATM 17011 C C4  . BGC E 2 .   ? 46.654  26.832  12.347  1.00 52.16  ? 2   BGC E C4  1 
HETATM 17012 C C5  . BGC E 2 .   ? 45.816  25.688  11.802  1.00 55.26  ? 2   BGC E C5  1 
HETATM 17013 C C6  . BGC E 2 .   ? 46.295  25.173  10.467  1.00 58.71  ? 2   BGC E C6  1 
HETATM 17014 C C1  . BGC E 2 .   ? 45.333  24.905  14.000  1.00 39.45  ? 2   BGC E C1  1 
HETATM 17015 O O2  . BGC E 2 .   ? 45.492  26.405  15.871  1.00 43.54  ? 2   BGC E O2  1 
HETATM 17016 O O3  . BGC E 2 .   ? 46.947  28.258  14.256  1.00 57.38  ? 2   BGC E O3  1 
HETATM 17017 O O4  . BGC E 2 .   ? 46.588  27.936  11.461  1.00 55.68  ? 2   BGC E O4  1 
HETATM 17018 O O5  . BGC E 2 .   ? 45.886  24.593  12.723  1.00 43.31  ? 2   BGC E O5  1 
HETATM 17019 O O6  . BGC E 2 .   ? 47.698  24.956  10.475  1.00 67.11  ? 2   BGC E O6  1 
HETATM 17020 C C2  . BGC F 2 .   ? 33.723  -24.701 -1.410  1.00 86.39  ? 1   BGC F C2  1 
HETATM 17021 C C3  . BGC F 2 .   ? 32.575  -24.130 -2.240  1.00 89.73  ? 1   BGC F C3  1 
HETATM 17022 C C4  . BGC F 2 .   ? 31.722  -23.174 -1.432  1.00 83.81  ? 1   BGC F C4  1 
HETATM 17023 C C5  . BGC F 2 .   ? 32.597  -22.184 -0.711  1.00 79.18  ? 1   BGC F C5  1 
HETATM 17024 C C6  . BGC F 2 .   ? 31.826  -21.185 0.101   1.00 73.55  ? 1   BGC F C6  1 
HETATM 17025 C C1  . BGC F 2 .   ? 34.337  -23.711 -0.422  1.00 80.55  ? 1   BGC F C1  1 
HETATM 17026 O O1  . BGC F 2 .   ? 35.011  -24.323 0.615   1.00 82.74  ? 1   BGC F O1  1 
HETATM 17027 O O2  . BGC F 2 .   ? 34.738  -25.191 -2.280  1.00 74.48  ? 1   BGC F O2  1 
HETATM 17028 O O3  . BGC F 2 .   ? 31.746  -25.194 -2.703  1.00 77.61  ? 1   BGC F O3  1 
HETATM 17029 O O4  . BGC F 2 .   ? 30.840  -22.472 -2.291  1.00 77.63  ? 1   BGC F O4  1 
HETATM 17030 O O5  . BGC F 2 .   ? 33.354  -22.928 0.217   1.00 89.59  ? 1   BGC F O5  1 
HETATM 17031 O O6  . BGC F 2 .   ? 32.380  -21.059 1.410   1.00 77.32  ? 1   BGC F O6  1 
HETATM 17032 C C2  . BGC F 2 .   ? 30.975  -26.730 -4.253  1.00 53.13  ? 2   BGC F C2  1 
HETATM 17033 C C3  . BGC F 2 .   ? 30.859  -27.083 -5.714  1.00 48.78  ? 2   BGC F C3  1 
HETATM 17034 C C4  . BGC F 2 .   ? 30.237  -25.934 -6.474  1.00 51.89  ? 2   BGC F C4  1 
HETATM 17035 C C5  . BGC F 2 .   ? 31.041  -24.669 -6.225  1.00 57.81  ? 2   BGC F C5  1 
HETATM 17036 C C6  . BGC F 2 .   ? 30.440  -23.449 -6.878  1.00 68.96  ? 2   BGC F C6  1 
HETATM 17037 C C1  . BGC F 2 .   ? 31.736  -25.443 -4.072  1.00 52.94  ? 2   BGC F C1  1 
HETATM 17038 O O2  . BGC F 2 .   ? 31.601  -27.775 -3.517  1.00 55.12  ? 2   BGC F O2  1 
HETATM 17039 O O3  . BGC F 2 .   ? 30.055  -28.249 -5.849  1.00 80.07  ? 2   BGC F O3  1 
HETATM 17040 O O4  . BGC F 2 .   ? 30.227  -26.226 -7.865  1.00 50.04  ? 2   BGC F O4  1 
HETATM 17041 O O5  . BGC F 2 .   ? 31.086  -24.408 -4.810  1.00 51.56  ? 2   BGC F O5  1 
HETATM 17042 O O6  . BGC F 2 .   ? 29.046  -23.359 -6.605  1.00 74.01  ? 2   BGC F O6  1 
HETATM 17043 C C1  . MLA G 3 .   ? 44.420  15.886  20.412  1.00 102.06 ? 601 MLA A C1  1 
HETATM 17044 O O1A . MLA G 3 .   ? 43.964  14.815  20.037  1.00 114.16 ? 601 MLA A O1A 1 
HETATM 17045 O O1B . MLA G 3 .   ? 45.135  16.020  21.435  1.00 89.73  ? 601 MLA A O1B 1 
HETATM 17046 C C2  . MLA G 3 .   ? 44.095  17.108  19.562  1.00 100.40 ? 601 MLA A C2  1 
HETATM 17047 C C3  . MLA G 3 .   ? 45.332  17.918  19.185  1.00 106.39 ? 601 MLA A C3  1 
HETATM 17048 O O3A . MLA G 3 .   ? 45.335  18.499  18.077  1.00 95.58  ? 601 MLA A O3A 1 
HETATM 17049 O O3B . MLA G 3 .   ? 46.281  17.967  20.007  1.00 91.75  ? 601 MLA A O3B 1 
HETATM 17050 C C1  . MLA H 3 .   ? 22.308  5.842   17.508  1.00 83.00  ? 602 MLA A C1  1 
HETATM 17051 O O1A . MLA H 3 .   ? 23.088  5.183   18.229  1.00 86.26  ? 602 MLA A O1A 1 
HETATM 17052 O O1B . MLA H 3 .   ? 22.420  5.947   16.258  1.00 66.76  ? 602 MLA A O1B 1 
HETATM 17053 C C2  . MLA H 3 .   ? 21.117  6.517   18.177  1.00 82.73  ? 602 MLA A C2  1 
HETATM 17054 C C3  . MLA H 3 .   ? 19.811  5.956   17.619  1.00 95.51  ? 602 MLA A C3  1 
HETATM 17055 O O3A . MLA H 3 .   ? 19.725  5.781   16.367  1.00 85.23  ? 602 MLA A O3A 1 
HETATM 17056 O O3B . MLA H 3 .   ? 18.893  5.690   18.435  1.00 98.71  ? 602 MLA A O3B 1 
HETATM 17057 C C1  . GOL I 4 .   ? 30.502  0.425   -0.898  1.00 84.67  ? 603 GOL A C1  1 
HETATM 17058 O O1  . GOL I 4 .   ? 29.823  0.618   0.348   1.00 74.51  ? 603 GOL A O1  1 
HETATM 17059 C C2  . GOL I 4 .   ? 32.015  0.281   -0.760  1.00 85.79  ? 603 GOL A C2  1 
HETATM 17060 O O2  . GOL I 4 .   ? 32.691  1.179   -1.643  1.00 74.93  ? 603 GOL A O2  1 
HETATM 17061 C C3  . GOL I 4 .   ? 32.539  0.514   0.641   1.00 84.57  ? 603 GOL A C3  1 
HETATM 17062 O O3  . GOL I 4 .   ? 33.962  0.468   0.673   1.00 86.80  ? 603 GOL A O3  1 
HETATM 17063 C C1  . GOL J 4 .   ? 22.585  -6.598  2.693   1.00 62.34  ? 604 GOL A C1  1 
HETATM 17064 O O1  . GOL J 4 .   ? 23.531  -6.703  3.749   1.00 61.03  ? 604 GOL A O1  1 
HETATM 17065 C C2  . GOL J 4 .   ? 22.908  -7.536  1.552   1.00 64.71  ? 604 GOL A C2  1 
HETATM 17066 O O2  . GOL J 4 .   ? 22.246  -8.786  1.779   1.00 65.65  ? 604 GOL A O2  1 
HETATM 17067 C C3  . GOL J 4 .   ? 22.527  -6.939  0.212   1.00 66.53  ? 604 GOL A C3  1 
HETATM 17068 O O3  . GOL J 4 .   ? 22.638  -7.874  -0.860  1.00 72.95  ? 604 GOL A O3  1 
HETATM 17069 C C1  . GOL K 4 .   ? 45.529  28.426  -57.640 1.00 88.81  ? 601 GOL B C1  1 
HETATM 17070 O O1  . GOL K 4 .   ? 46.946  28.532  -57.777 1.00 75.87  ? 601 GOL B O1  1 
HETATM 17071 C C2  . GOL K 4 .   ? 45.083  28.163  -56.209 1.00 94.96  ? 601 GOL B C2  1 
HETATM 17072 O O2  . GOL K 4 .   ? 44.985  29.386  -55.469 1.00 83.74  ? 601 GOL B O2  1 
HETATM 17073 C C3  . GOL K 4 .   ? 43.763  27.411  -56.141 1.00 95.94  ? 601 GOL B C3  1 
HETATM 17074 O O3  . GOL K 4 .   ? 43.134  27.509  -54.860 1.00 90.87  ? 601 GOL B O3  1 
HETATM 17075 C C2  . BGC L 5 .   ? 34.376  28.127  -49.787 1.00 63.52  ? 602 BGC B C2  1 
HETATM 17076 C C3  . BGC L 5 .   ? 32.991  28.145  -49.102 1.00 59.21  ? 602 BGC B C3  1 
HETATM 17077 C C4  . BGC L 5 .   ? 33.085  27.560  -47.717 1.00 58.22  ? 602 BGC B C4  1 
HETATM 17078 C C5  . BGC L 5 .   ? 34.086  28.366  -46.956 1.00 61.28  ? 602 BGC B C5  1 
HETATM 17079 C C6  . BGC L 5 .   ? 34.257  27.943  -45.517 1.00 64.93  ? 602 BGC B C6  1 
HETATM 17080 C C1  . BGC L 5 .   ? 35.371  28.890  -48.922 1.00 73.22  ? 602 BGC B C1  1 
HETATM 17081 O O1  . BGC L 5 .   ? 36.679  29.028  -49.493 1.00 84.23  ? 602 BGC B O1  1 
HETATM 17082 O O2  . BGC L 5 .   ? 34.399  28.636  -51.123 1.00 64.51  ? 602 BGC B O2  1 
HETATM 17083 O O3  . BGC L 5 .   ? 32.008  27.403  -49.812 1.00 70.91  ? 602 BGC B O3  1 
HETATM 17084 O O4  . BGC L 5 .   ? 31.816  27.593  -47.067 1.00 57.70  ? 602 BGC B O4  1 
HETATM 17085 O O5  . BGC L 5 .   ? 35.350  28.223  -47.636 1.00 67.77  ? 602 BGC B O5  1 
HETATM 17086 O O6  . BGC L 5 .   ? 34.675  26.593  -45.440 1.00 73.12  ? 602 BGC B O6  1 
HETATM 17087 C C1  . GOL M 4 .   ? 56.420  30.985  -35.628 1.00 75.72  ? 601 GOL C C1  1 
HETATM 17088 O O1  . GOL M 4 .   ? 57.552  31.820  -35.850 1.00 91.82  ? 601 GOL C O1  1 
HETATM 17089 C C2  . GOL M 4 .   ? 56.330  30.520  -34.192 1.00 70.35  ? 601 GOL C C2  1 
HETATM 17090 O O2  . GOL M 4 .   ? 57.196  29.409  -34.009 1.00 71.09  ? 601 GOL C O2  1 
HETATM 17091 C C3  . GOL M 4 .   ? 56.667  31.559  -33.147 1.00 69.02  ? 601 GOL C C3  1 
HETATM 17092 O O3  . GOL M 4 .   ? 56.664  30.984  -31.835 1.00 62.91  ? 601 GOL C O3  1 
HETATM 17093 C C1  . MLA N 3 .   ? 68.851  35.181  -41.185 1.00 86.70  ? 602 MLA C C1  1 
HETATM 17094 O O1A . MLA N 3 .   ? 67.693  34.788  -41.408 1.00 93.69  ? 602 MLA C O1A 1 
HETATM 17095 O O1B . MLA N 3 .   ? 69.451  35.040  -40.103 1.00 90.57  ? 602 MLA C O1B 1 
HETATM 17096 C C2  . MLA N 3 .   ? 69.573  35.889  -42.309 1.00 75.98  ? 602 MLA C C2  1 
HETATM 17097 C C3  . MLA N 3 .   ? 69.845  34.950  -43.465 1.00 82.55  ? 602 MLA C C3  1 
HETATM 17098 O O3A . MLA N 3 .   ? 70.701  34.055  -43.288 1.00 89.17  ? 602 MLA C O3A 1 
HETATM 17099 O O3B . MLA N 3 .   ? 69.207  35.135  -44.534 1.00 80.03  ? 602 MLA C O3B 1 
HETATM 17100 O O1  . PG4 O 6 .   ? 83.658  39.579  -47.539 1.00 85.29  ? 603 PG4 C O1  1 
HETATM 17101 C C1  . PG4 O 6 .   ? 82.384  40.194  -47.343 1.00 89.48  ? 603 PG4 C C1  1 
HETATM 17102 C C2  . PG4 O 6 .   ? 82.053  40.497  -45.885 1.00 86.21  ? 603 PG4 C C2  1 
HETATM 17103 O O2  . PG4 O 6 .   ? 82.830  39.698  -44.991 1.00 79.81  ? 603 PG4 C O2  1 
HETATM 17104 C C3  . PG4 O 6 .   ? 82.265  39.547  -43.685 1.00 68.20  ? 603 PG4 C C3  1 
HETATM 17105 C C4  . PG4 O 6 .   ? 82.940  40.468  -42.744 1.00 60.77  ? 603 PG4 C C4  1 
HETATM 17106 O O3  . PG4 O 6 .   ? 82.900  39.955  -41.415 1.00 59.94  ? 603 PG4 C O3  1 
HETATM 17107 C C5  . PG4 O 6 .   ? 83.716  40.753  -40.558 1.00 70.08  ? 603 PG4 C C5  1 
HETATM 17108 C C6  . PG4 O 6 .   ? 83.564  40.343  -39.129 1.00 70.19  ? 603 PG4 C C6  1 
HETATM 17109 O O4  . PG4 O 6 .   ? 84.057  41.395  -38.296 1.00 81.18  ? 603 PG4 C O4  1 
HETATM 17110 C C7  . PG4 O 6 .   ? 83.933  41.150  -36.892 1.00 81.91  ? 603 PG4 C C7  1 
HETATM 17111 C C8  . PG4 O 6 .   ? 82.491  40.867  -36.521 1.00 88.19  ? 603 PG4 C C8  1 
HETATM 17112 O O5  . PG4 O 6 .   ? 82.169  41.221  -35.171 1.00 78.74  ? 603 PG4 C O5  1 
HETATM 17113 C C2  . BGC P 5 .   ? 33.492  -23.503 5.531   1.00 56.69  ? 601 BGC D C2  1 
HETATM 17114 C C3  . BGC P 5 .   ? 32.714  -23.684 4.206   1.00 66.49  ? 601 BGC D C3  1 
HETATM 17115 C C4  . BGC P 5 .   ? 31.759  -24.877 4.355   1.00 76.36  ? 601 BGC D C4  1 
HETATM 17116 C C5  . BGC P 5 .   ? 30.788  -24.655 5.549   1.00 83.13  ? 601 BGC D C5  1 
HETATM 17117 C C6  . BGC P 5 .   ? 29.954  -25.912 5.801   1.00 88.80  ? 601 BGC D C6  1 
HETATM 17118 C C1  . BGC P 5 .   ? 32.521  -23.204 6.693   1.00 66.95  ? 601 BGC D C1  1 
HETATM 17119 O O1  . BGC P 5 .   ? 33.297  -22.835 7.865   1.00 49.95  ? 601 BGC D O1  1 
HETATM 17120 O O2  . BGC P 5 .   ? 34.479  -22.480 5.485   1.00 53.95  ? 601 BGC D O2  1 
HETATM 17121 O O3  . BGC P 5 .   ? 33.575  -23.832 3.057   1.00 58.67  ? 601 BGC D O3  1 
HETATM 17122 O O4  . BGC P 5 .   ? 30.994  -25.137 3.153   1.00 79.16  ? 601 BGC D O4  1 
HETATM 17123 O O5  . BGC P 5 .   ? 31.527  -24.294 6.820   1.00 76.54  ? 601 BGC D O5  1 
HETATM 17124 O O6  . BGC P 5 .   ? 28.614  -25.656 6.224   1.00 85.44  ? 601 BGC D O6  1 
HETATM 17125 C C1  . MLA Q 3 .   ? 69.178  -15.392 18.840  1.00 101.65 ? 602 MLA D C1  1 
HETATM 17126 O O1A . MLA Q 3 .   ? 68.995  -14.387 18.136  1.00 94.46  ? 602 MLA D O1A 1 
HETATM 17127 O O1B . MLA Q 3 .   ? 69.657  -16.454 18.414  1.00 110.86 ? 602 MLA D O1B 1 
HETATM 17128 C C2  . MLA Q 3 .   ? 68.790  -15.321 20.312  1.00 102.81 ? 602 MLA D C2  1 
HETATM 17129 C C3  . MLA Q 3 .   ? 69.850  -14.611 21.145  1.00 107.19 ? 602 MLA D C3  1 
HETATM 17130 O O3A . MLA Q 3 .   ? 69.525  -14.190 22.267  1.00 103.63 ? 602 MLA D O3A 1 
HETATM 17131 O O3B . MLA Q 3 .   ? 70.988  -14.486 20.664  1.00 102.92 ? 602 MLA D O3B 1 
HETATM 17132 O O   . HOH R 7 .   ? 59.629  20.812  12.402  1.00 51.32  ? 701 HOH A O   1 
HETATM 17133 O O   . HOH R 7 .   ? 29.382  27.163  -5.043  1.00 58.12  ? 702 HOH A O   1 
HETATM 17134 O O   . HOH R 7 .   ? 24.559  41.379  15.624  1.00 70.99  ? 703 HOH A O   1 
HETATM 17135 O O   . HOH R 7 .   ? 33.072  18.148  -9.725  1.00 56.91  ? 704 HOH A O   1 
HETATM 17136 O O   . HOH R 7 .   ? 44.005  39.755  13.483  1.00 67.78  ? 705 HOH A O   1 
HETATM 17137 O O   . HOH R 7 .   ? 55.633  17.329  3.567   1.00 59.67  ? 706 HOH A O   1 
HETATM 17138 O O   . HOH R 7 .   ? 32.818  27.264  -4.751  1.00 60.81  ? 707 HOH A O   1 
HETATM 17139 O O   . HOH R 7 .   ? 21.351  23.209  -4.099  1.00 58.22  ? 708 HOH A O   1 
HETATM 17140 O O   . HOH R 7 .   ? 29.757  23.191  23.851  1.00 74.51  ? 709 HOH A O   1 
HETATM 17141 O O   . HOH R 7 .   ? 42.201  15.849  31.824  1.00 69.25  ? 710 HOH A O   1 
HETATM 17142 O O   . HOH R 7 .   ? 21.449  7.504   27.984  1.00 76.77  ? 711 HOH A O   1 
HETATM 17143 O O   . HOH R 7 .   ? 27.172  7.549   41.296  1.00 85.91  ? 712 HOH A O   1 
HETATM 17144 O O   . HOH R 7 .   ? 27.123  14.305  23.258  1.00 58.32  ? 713 HOH A O   1 
HETATM 17145 O O   . HOH R 7 .   ? 31.907  -3.070  23.791  1.00 58.05  ? 714 HOH A O   1 
HETATM 17146 O O   . HOH R 7 .   ? 51.113  27.085  2.857   1.00 62.31  ? 715 HOH A O   1 
HETATM 17147 O O   . HOH R 7 .   ? 39.866  15.716  -2.641  1.00 65.97  ? 716 HOH A O   1 
HETATM 17148 O O   . HOH R 7 .   ? 28.171  6.359   18.066  1.00 62.71  ? 717 HOH A O   1 
HETATM 17149 O O   . HOH R 7 .   ? 41.791  33.721  5.072   1.00 56.67  ? 718 HOH A O   1 
HETATM 17150 O O   . HOH R 7 .   ? 56.305  25.198  7.227   1.00 81.08  ? 719 HOH A O   1 
HETATM 17151 O O   . HOH R 7 .   ? 26.130  23.639  30.610  1.00 76.05  ? 720 HOH A O   1 
HETATM 17152 O O   . HOH R 7 .   ? 32.968  35.714  34.539  1.00 30.00  ? 721 HOH A O   1 
HETATM 17153 O O   . HOH R 7 .   ? 48.306  42.628  0.553   1.00 65.71  ? 722 HOH A O   1 
HETATM 17154 O O   . HOH R 7 .   ? 54.842  32.266  6.416   1.00 65.35  ? 723 HOH A O   1 
HETATM 17155 O O   . HOH R 7 .   ? 27.071  21.237  36.930  1.00 76.89  ? 724 HOH A O   1 
HETATM 17156 O O   . HOH R 7 .   ? 55.359  22.836  5.473   1.00 59.81  ? 725 HOH A O   1 
HETATM 17157 O O   . HOH R 7 .   ? 20.858  24.669  23.999  1.00 74.59  ? 726 HOH A O   1 
HETATM 17158 O O   . HOH R 7 .   ? 31.138  31.937  32.798  1.00 75.79  ? 727 HOH A O   1 
HETATM 17159 O O   . HOH R 7 .   ? 53.412  32.518  -3.824  1.00 90.53  ? 728 HOH A O   1 
HETATM 17160 O O   . HOH R 7 .   ? 31.757  40.209  -4.415  1.00 68.87  ? 729 HOH A O   1 
HETATM 17161 O O   . HOH R 7 .   ? 31.857  4.972   9.280   1.00 62.32  ? 730 HOH A O   1 
HETATM 17162 O O   . HOH R 7 .   ? 29.001  20.032  -7.907  1.00 65.77  ? 731 HOH A O   1 
HETATM 17163 O O   . HOH R 7 .   ? 12.594  2.925   19.935  1.00 65.97  ? 732 HOH A O   1 
HETATM 17164 O O   . HOH R 7 .   ? 39.091  12.786  13.352  1.00 65.15  ? 733 HOH A O   1 
HETATM 17165 O O   . HOH R 7 .   ? 19.497  24.658  25.825  1.00 80.06  ? 734 HOH A O   1 
HETATM 17166 O O   . HOH R 7 .   ? 21.463  21.042  13.124  1.00 49.98  ? 735 HOH A O   1 
HETATM 17167 O O   . HOH R 7 .   ? 54.113  36.666  -1.601  1.00 95.13  ? 736 HOH A O   1 
HETATM 17168 O O   . HOH R 7 .   ? 22.363  21.173  10.808  1.00 57.82  ? 737 HOH A O   1 
HETATM 17169 O O   . HOH R 7 .   ? 17.852  8.577   8.876   1.00 58.62  ? 738 HOH A O   1 
HETATM 17170 O O   . HOH R 7 .   ? 24.240  11.161  22.019  1.00 63.03  ? 739 HOH A O   1 
HETATM 17171 O O   . HOH R 7 .   ? 43.982  14.392  7.664   1.00 53.58  ? 740 HOH A O   1 
HETATM 17172 O O   . HOH R 7 .   ? 23.931  14.930  27.803  1.00 56.77  ? 741 HOH A O   1 
HETATM 17173 O O   . HOH R 7 .   ? 29.324  44.615  20.475  1.00 60.76  ? 742 HOH A O   1 
HETATM 17174 O O   . HOH R 7 .   ? 12.243  -6.019  3.008   1.00 73.65  ? 743 HOH A O   1 
HETATM 17175 O O   . HOH R 7 .   ? 33.347  -1.098  -3.571  1.00 54.74  ? 744 HOH A O   1 
HETATM 17176 O O   . HOH R 7 .   ? 21.623  -5.695  6.709   1.00 53.13  ? 745 HOH A O   1 
HETATM 17177 O O   . HOH R 7 .   ? 46.002  21.625  -12.401 1.00 73.52  ? 746 HOH A O   1 
HETATM 17178 O O   . HOH R 7 .   ? 21.631  -4.884  -1.570  1.00 57.15  ? 747 HOH A O   1 
HETATM 17179 O O   . HOH R 7 .   ? 45.472  43.973  0.218   1.00 71.67  ? 748 HOH A O   1 
HETATM 17180 O O   . HOH R 7 .   ? 52.371  40.883  -0.846  1.00 68.62  ? 749 HOH A O   1 
HETATM 17181 O O   . HOH R 7 .   ? 31.134  -2.311  40.275  1.00 66.15  ? 750 HOH A O   1 
HETATM 17182 O O   . HOH R 7 .   ? 29.746  35.047  -6.939  1.00 63.15  ? 751 HOH A O   1 
HETATM 17183 O O   . HOH R 7 .   ? 30.679  35.038  37.525  1.00 84.30  ? 752 HOH A O   1 
HETATM 17184 O O   . HOH R 7 .   ? 9.059   -4.038  21.738  1.00 62.72  ? 753 HOH A O   1 
HETATM 17185 O O   . HOH R 7 .   ? 22.043  5.501   23.284  1.00 58.80  ? 754 HOH A O   1 
HETATM 17186 O O   . HOH R 7 .   ? 16.014  -8.165  28.020  1.00 87.24  ? 755 HOH A O   1 
HETATM 17187 O O   . HOH R 7 .   ? 9.363   5.449   -2.910  1.00 67.80  ? 756 HOH A O   1 
HETATM 17188 O O   . HOH R 7 .   ? 26.908  29.359  -5.511  1.00 67.97  ? 757 HOH A O   1 
HETATM 17189 O O   . HOH R 7 .   ? 13.187  16.547  -9.591  1.00 67.60  ? 758 HOH A O   1 
HETATM 17190 O O   . HOH R 7 .   ? 26.202  4.844   17.176  1.00 69.77  ? 759 HOH A O   1 
HETATM 17191 O O   . HOH R 7 .   ? 11.475  -9.229  15.247  1.00 59.45  ? 760 HOH A O   1 
HETATM 17192 O O   . HOH R 7 .   ? 11.290  6.941   11.469  1.00 61.40  ? 761 HOH A O   1 
HETATM 17193 O O   . HOH R 7 .   ? 33.939  48.385  8.649   1.00 59.27  ? 762 HOH A O   1 
HETATM 17194 O O   . HOH R 7 .   ? 44.941  13.119  23.466  1.00 63.27  ? 763 HOH A O   1 
HETATM 17195 O O   . HOH R 7 .   ? 38.603  5.587   12.226  1.00 50.42  ? 764 HOH A O   1 
HETATM 17196 O O   . HOH R 7 .   ? 43.618  48.137  4.781   1.00 70.07  ? 765 HOH A O   1 
HETATM 17197 O O   . HOH R 7 .   ? 22.872  35.277  8.747   1.00 65.83  ? 766 HOH A O   1 
HETATM 17198 O O   . HOH R 7 .   ? 54.138  8.794   5.470   1.00 46.70  ? 767 HOH A O   1 
HETATM 17199 O O   . HOH R 7 .   ? 48.663  31.850  16.028  1.00 95.16  ? 768 HOH A O   1 
HETATM 17200 O O   . HOH R 7 .   ? 33.900  2.817   -8.128  1.00 56.36  ? 769 HOH A O   1 
HETATM 17201 O O   . HOH R 7 .   ? 19.829  17.598  8.707   1.00 47.80  ? 770 HOH A O   1 
HETATM 17202 O O   . HOH S 7 .   ? 38.891  14.168  -46.570 1.00 63.87  ? 701 HOH B O   1 
HETATM 17203 O O   . HOH S 7 .   ? 20.524  47.232  -45.091 1.00 86.83  ? 702 HOH B O   1 
HETATM 17204 O O   . HOH S 7 .   ? 44.175  31.195  -67.184 1.00 83.86  ? 703 HOH B O   1 
HETATM 17205 O O   . HOH S 7 .   ? 42.688  55.649  -43.223 1.00 66.97  ? 704 HOH B O   1 
HETATM 17206 O O   . HOH S 7 .   ? 27.159  40.610  -29.739 1.00 86.97  ? 705 HOH B O   1 
HETATM 17207 O O   . HOH S 7 .   ? 35.372  19.089  -41.288 1.00 93.14  ? 706 HOH B O   1 
HETATM 17208 O O   . HOH S 7 .   ? 68.084  56.938  -66.791 1.00 90.79  ? 707 HOH B O   1 
HETATM 17209 O O   . HOH S 7 .   ? 31.882  13.882  -46.428 1.00 90.17  ? 708 HOH B O   1 
HETATM 17210 O O   . HOH S 7 .   ? 14.224  31.255  -31.260 1.00 89.92  ? 709 HOH B O   1 
HETATM 17211 O O   . HOH S 7 .   ? 24.134  22.601  -39.346 1.00 71.51  ? 710 HOH B O   1 
HETATM 17212 O O   . HOH S 7 .   ? 41.301  25.821  -55.895 1.00 88.68  ? 711 HOH B O   1 
HETATM 17213 O O   . HOH S 7 .   ? 13.761  29.470  -32.838 1.00 63.91  ? 712 HOH B O   1 
HETATM 17214 O O   . HOH S 7 .   ? 52.103  23.260  -52.943 1.00 81.49  ? 713 HOH B O   1 
HETATM 17215 O O   . HOH S 7 .   ? 47.302  34.653  -48.500 1.00 60.62  ? 714 HOH B O   1 
HETATM 17216 O O   . HOH S 7 .   ? 39.156  40.342  -27.817 1.00 68.21  ? 715 HOH B O   1 
HETATM 17217 O O   . HOH S 7 .   ? 9.953   40.169  -32.337 1.00 71.70  ? 716 HOH B O   1 
HETATM 17218 O O   . HOH S 7 .   ? 54.541  50.894  -52.983 1.00 58.15  ? 717 HOH B O   1 
HETATM 17219 O O   . HOH S 7 .   ? 54.916  50.972  -58.726 1.00 59.64  ? 718 HOH B O   1 
HETATM 17220 O O   . HOH S 7 .   ? 65.700  60.257  -56.988 1.00 75.29  ? 719 HOH B O   1 
HETATM 17221 O O   . HOH S 7 .   ? 28.919  15.222  -35.790 1.00 81.60  ? 720 HOH B O   1 
HETATM 17222 O O   . HOH S 7 .   ? 62.887  41.713  -59.165 1.00 60.78  ? 721 HOH B O   1 
HETATM 17223 O O   . HOH S 7 .   ? 22.094  51.786  -48.678 1.00 73.77  ? 722 HOH B O   1 
HETATM 17224 O O   . HOH S 7 .   ? 39.923  29.327  -49.522 1.00 74.02  ? 723 HOH B O   1 
HETATM 17225 O O   . HOH S 7 .   ? 45.197  49.435  -63.431 1.00 63.04  ? 724 HOH B O   1 
HETATM 17226 O O   . HOH S 7 .   ? 63.450  59.801  -62.705 1.00 92.77  ? 725 HOH B O   1 
HETATM 17227 O O   . HOH S 7 .   ? 36.960  31.939  -68.354 1.00 77.11  ? 726 HOH B O   1 
HETATM 17228 O O   . HOH S 7 .   ? 57.929  35.311  -74.663 1.00 61.83  ? 727 HOH B O   1 
HETATM 17229 O O   . HOH S 7 .   ? 58.218  58.749  -63.165 1.00 78.64  ? 728 HOH B O   1 
HETATM 17230 O O   . HOH S 7 .   ? 54.307  35.141  -47.083 1.00 52.62  ? 729 HOH B O   1 
HETATM 17231 O O   . HOH S 7 .   ? 45.675  58.869  -27.487 1.00 94.97  ? 730 HOH B O   1 
HETATM 17232 O O   . HOH S 7 .   ? 18.802  49.519  -26.019 1.00 86.66  ? 731 HOH B O   1 
HETATM 17233 O O   . HOH S 7 .   ? 14.962  49.373  -52.012 1.00 72.84  ? 732 HOH B O   1 
HETATM 17234 O O   . HOH S 7 .   ? 40.087  45.934  -17.132 1.00 79.36  ? 733 HOH B O   1 
HETATM 17235 O O   . HOH S 7 .   ? 71.977  48.924  -62.586 1.00 86.23  ? 734 HOH B O   1 
HETATM 17236 O O   . HOH S 7 .   ? 27.928  24.319  -51.519 1.00 88.67  ? 735 HOH B O   1 
HETATM 17237 O O   . HOH T 7 .   ? 90.962  33.705  -54.019 1.00 64.75  ? 701 HOH C O   1 
HETATM 17238 O O   . HOH T 7 .   ? 81.782  54.166  -28.217 1.00 83.75  ? 702 HOH C O   1 
HETATM 17239 O O   . HOH T 7 .   ? 76.672  15.241  -50.281 1.00 67.22  ? 703 HOH C O   1 
HETATM 17240 O O   . HOH T 7 .   ? 61.268  25.309  -14.995 1.00 74.29  ? 704 HOH C O   1 
HETATM 17241 O O   . HOH T 7 .   ? 63.515  27.767  -34.552 1.00 68.10  ? 705 HOH C O   1 
HETATM 17242 O O   . HOH T 7 .   ? 76.504  17.199  -47.848 1.00 73.75  ? 706 HOH C O   1 
HETATM 17243 O O   . HOH T 7 .   ? 65.841  18.791  -59.176 1.00 83.77  ? 707 HOH C O   1 
HETATM 17244 O O   . HOH T 7 .   ? 59.001  4.795   -42.310 1.00 84.31  ? 708 HOH C O   1 
HETATM 17245 O O   . HOH T 7 .   ? 80.631  19.495  -46.160 1.00 65.55  ? 709 HOH C O   1 
HETATM 17246 O O   . HOH T 7 .   ? 92.034  25.834  -15.149 1.00 82.97  ? 710 HOH C O   1 
HETATM 17247 O O   . HOH T 7 .   ? 79.712  15.155  -49.114 1.00 63.98  ? 711 HOH C O   1 
HETATM 17248 O O   . HOH T 7 .   ? 66.062  5.312   -50.082 1.00 68.85  ? 712 HOH C O   1 
HETATM 17249 O O   . HOH T 7 .   ? 76.366  62.883  -21.877 1.00 86.81  ? 713 HOH C O   1 
HETATM 17250 O O   . HOH T 7 .   ? 73.344  21.230  -29.466 1.00 68.16  ? 714 HOH C O   1 
HETATM 17251 O O   . HOH T 7 .   ? 66.479  0.659   -33.037 1.00 80.09  ? 715 HOH C O   1 
HETATM 17252 O O   . HOH T 7 .   ? 84.356  43.127  -29.223 1.00 71.56  ? 716 HOH C O   1 
HETATM 17253 O O   . HOH T 7 .   ? 68.971  25.415  -63.049 1.00 88.46  ? 717 HOH C O   1 
HETATM 17254 O O   . HOH T 7 .   ? 63.529  3.573   -45.593 1.00 71.86  ? 718 HOH C O   1 
HETATM 17255 O O   . HOH T 7 .   ? 71.662  18.121  -42.340 1.00 60.05  ? 719 HOH C O   1 
HETATM 17256 O O   . HOH T 7 .   ? 63.786  15.897  -58.703 1.00 92.56  ? 720 HOH C O   1 
HETATM 17257 O O   . HOH T 7 .   ? 55.353  11.627  -22.439 1.00 70.80  ? 721 HOH C O   1 
HETATM 17258 O O   . HOH T 7 .   ? 95.393  39.077  -4.365  1.00 77.87  ? 722 HOH C O   1 
HETATM 17259 O O   . HOH T 7 .   ? 80.749  18.948  -12.064 1.00 89.63  ? 723 HOH C O   1 
HETATM 17260 O O   . HOH T 7 .   ? 96.435  20.670  -20.209 1.00 84.40  ? 724 HOH C O   1 
HETATM 17261 O O   . HOH T 7 .   ? 101.859 14.975  -55.458 1.00 74.85  ? 725 HOH C O   1 
HETATM 17262 O O   . HOH T 7 .   ? 99.280  20.257  -41.814 1.00 63.33  ? 726 HOH C O   1 
HETATM 17263 O O   . HOH T 7 .   ? 109.420 34.448  -23.388 1.00 84.60  ? 727 HOH C O   1 
HETATM 17264 O O   . HOH T 7 .   ? 69.078  11.854  -68.915 1.00 71.47  ? 728 HOH C O   1 
HETATM 17265 O O   . HOH T 7 .   ? 89.079  21.651  -16.615 1.00 77.25  ? 729 HOH C O   1 
HETATM 17266 O O   . HOH U 7 .   ? 14.249  -20.117 3.316   1.00 64.19  ? 701 HOH D O   1 
HETATM 17267 O O   . HOH U 7 .   ? 39.678  -8.775  -17.924 1.00 60.14  ? 702 HOH D O   1 
HETATM 17268 O O   . HOH U 7 .   ? 17.338  -22.126 -0.527  1.00 30.00  ? 703 HOH D O   1 
HETATM 17269 O O   . HOH U 7 .   ? 40.006  -17.946 -25.510 1.00 65.21  ? 704 HOH D O   1 
HETATM 17270 O O   . HOH U 7 .   ? 53.230  5.870   6.758   1.00 61.38  ? 705 HOH D O   1 
HETATM 17271 O O   . HOH U 7 .   ? 48.280  -29.782 1.689   1.00 65.77  ? 706 HOH D O   1 
HETATM 17272 O O   . HOH U 7 .   ? 37.037  -30.596 15.198  1.00 77.97  ? 707 HOH D O   1 
HETATM 17273 O O   . HOH U 7 .   ? 51.659  -17.193 -12.894 1.00 64.10  ? 708 HOH D O   1 
HETATM 17274 O O   . HOH U 7 .   ? 40.693  -43.250 23.164  1.00 77.32  ? 709 HOH D O   1 
HETATM 17275 O O   . HOH U 7 .   ? 11.582  -22.609 -9.890  1.00 83.65  ? 710 HOH D O   1 
HETATM 17276 O O   . HOH U 7 .   ? 48.560  -5.518  -5.784  1.00 63.77  ? 711 HOH D O   1 
HETATM 17277 O O   . HOH U 7 .   ? 26.319  -18.533 -3.679  1.00 67.71  ? 712 HOH D O   1 
HETATM 17278 O O   . HOH U 7 .   ? 45.117  1.475   -22.550 1.00 75.07  ? 713 HOH D O   1 
HETATM 17279 O O   . HOH U 7 .   ? 42.841  -24.252 -29.071 1.00 74.90  ? 714 HOH D O   1 
HETATM 17280 O O   . HOH U 7 .   ? 46.016  3.860   -20.061 1.00 89.22  ? 715 HOH D O   1 
HETATM 17281 O O   . HOH U 7 .   ? 32.661  -40.829 3.854   1.00 66.50  ? 716 HOH D O   1 
HETATM 17282 O O   . HOH U 7 .   ? 53.289  -30.398 24.728  1.00 73.02  ? 717 HOH D O   1 
HETATM 17283 O O   . HOH U 7 .   ? 55.714  -11.807 7.675   1.00 64.38  ? 718 HOH D O   1 
HETATM 17284 O O   . HOH U 7 .   ? 37.499  -47.890 -0.284  1.00 83.74  ? 719 HOH D O   1 
HETATM 17285 O O   . HOH U 7 .   ? 33.985  -26.281 -17.211 1.00 61.12  ? 720 HOH D O   1 
HETATM 17286 O O   . HOH U 7 .   ? 24.155  -18.146 -11.216 1.00 56.20  ? 721 HOH D O   1 
HETATM 17287 O O   . HOH U 7 .   ? 20.696  -21.971 -8.269  1.00 56.01  ? 722 HOH D O   1 
HETATM 17288 O O   . HOH U 7 .   ? 12.252  -16.108 0.389   1.00 68.50  ? 723 HOH D O   1 
HETATM 17289 O O   . HOH U 7 .   ? 57.369  11.070  -14.751 1.00 69.13  ? 724 HOH D O   1 
HETATM 17290 O O   . HOH U 7 .   ? 59.029  -8.807  -0.422  1.00 69.25  ? 725 HOH D O   1 
HETATM 17291 O O   . HOH U 7 .   ? 58.258  -20.527 14.520  1.00 63.41  ? 726 HOH D O   1 
HETATM 17292 O O   . HOH U 7 .   ? 20.986  -13.590 -5.636  1.00 54.59  ? 727 HOH D O   1 
HETATM 17293 O O   . HOH U 7 .   ? 60.809  -7.732  -2.727  1.00 77.80  ? 728 HOH D O   1 
HETATM 17294 O O   . HOH U 7 .   ? 70.348  3.282   0.203   1.00 68.60  ? 729 HOH D O   1 
HETATM 17295 O O   . HOH U 7 .   ? 33.122  -39.617 5.898   1.00 74.71  ? 730 HOH D O   1 
HETATM 17296 O O   . HOH U 7 .   ? 13.087  -10.481 -12.863 1.00 69.46  ? 731 HOH D O   1 
HETATM 17297 O O   . HOH U 7 .   ? 28.891  -15.288 15.273  1.00 59.16  ? 732 HOH D O   1 
HETATM 17298 O O   . HOH U 7 .   ? 51.715  -22.869 7.644   1.00 73.74  ? 733 HOH D O   1 
HETATM 17299 O O   . HOH U 7 .   ? 21.659  -19.798 -22.634 1.00 72.77  ? 734 HOH D O   1 
HETATM 17300 O O   . HOH U 7 .   ? 59.037  -12.337 -2.765  1.00 68.56  ? 735 HOH D O   1 
HETATM 17301 O O   . HOH U 7 .   ? 29.346  -30.087 -26.873 1.00 73.29  ? 736 HOH D O   1 
HETATM 17302 O O   . HOH U 7 .   ? 51.617  -40.561 13.705  1.00 67.64  ? 737 HOH D O   1 
HETATM 17303 O O   . HOH U 7 .   ? 40.593  -4.092  -14.614 1.00 64.72  ? 738 HOH D O   1 
HETATM 17304 O O   . HOH U 7 .   ? 58.633  -13.285 -18.673 1.00 85.74  ? 739 HOH D O   1 
HETATM 17305 O O   . HOH U 7 .   ? 54.396  -10.589 -22.664 1.00 70.44  ? 740 HOH D O   1 
HETATM 17306 O O   . HOH U 7 .   ? 44.030  -24.988 27.887  1.00 58.91  ? 741 HOH D O   1 
HETATM 17307 O O   . HOH U 7 .   ? 53.924  9.410   3.271   1.00 44.91  ? 742 HOH D O   1 
HETATM 17308 O O   . HOH U 7 .   ? 52.998  -37.130 12.248  1.00 61.17  ? 743 HOH D O   1 
HETATM 17309 O O   . HOH U 7 .   ? 49.128  -9.445  4.848   1.00 54.35  ? 744 HOH D O   1 
HETATM 17310 O O   . HOH U 7 .   ? 38.950  -47.152 -19.210 1.00 57.90  ? 745 HOH D O   1 
HETATM 17311 O O   . HOH U 7 .   ? 32.341  -31.150 -8.467  1.00 61.00  ? 746 HOH D O   1 
HETATM 17312 O O   . HOH U 7 .   ? 51.008  -12.101 9.978   1.00 73.58  ? 747 HOH D O   1 
HETATM 17313 O O   . HOH U 7 .   ? 26.629  -29.079 -20.672 1.00 69.81  ? 748 HOH D O   1 
HETATM 17314 O O   . HOH U 7 .   ? 54.187  -48.044 8.105   1.00 79.74  ? 749 HOH D O   1 
HETATM 17315 O O   . HOH U 7 .   ? 54.538  11.646  -10.280 1.00 60.61  ? 750 HOH D O   1 
HETATM 17316 O O   . HOH U 7 .   ? 53.004  -39.634 7.681   1.00 58.69  ? 751 HOH D O   1 
HETATM 17317 O O   . HOH U 7 .   ? 56.254  11.174  -19.996 1.00 68.61  ? 752 HOH D O   1 
HETATM 17318 O O   . HOH U 7 .   ? 39.245  -9.558  6.727   1.00 55.90  ? 753 HOH D O   1 
HETATM 17319 O O   . HOH U 7 .   ? 43.533  -25.578 29.967  1.00 53.56  ? 754 HOH D O   1 
HETATM 17320 O O   . HOH U 7 .   ? 62.202  -10.776 -4.054  1.00 60.00  ? 755 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   ? 0.7799 0.4193 2.1719 0.0584  -0.1515 0.1427  3   SER A N   
2     C CA  . SER A 3   ? 0.7375 0.4138 2.1574 0.0666  -0.1520 0.1330  3   SER A CA  
3     C C   . SER A 3   ? 0.7155 0.4158 2.1482 0.0551  -0.1360 0.1258  3   SER A C   
4     O O   . SER A 3   ? 0.7326 0.4337 2.1512 0.0423  -0.1285 0.1288  3   SER A O   
5     C CB  . SER A 3   ? 0.7379 0.4217 2.1506 0.0713  -0.1627 0.1363  3   SER A CB  
6     O OG  . SER A 3   ? 0.7100 0.4292 2.1504 0.0773  -0.1617 0.1267  3   SER A OG  
7     N N   . LYS A 4   ? 0.6825 0.4020 2.1413 0.0603  -0.1313 0.1161  4   LYS A N   
8     C CA  . LYS A 4   ? 0.6564 0.3929 2.1265 0.0501  -0.1173 0.1095  4   LYS A CA  
9     C C   . LYS A 4   ? 0.5801 0.3490 2.0756 0.0566  -0.1149 0.0997  4   LYS A C   
10    O O   . LYS A 4   ? 0.5611 0.3379 2.0700 0.0694  -0.1220 0.0962  4   LYS A O   
11    C CB  . LYS A 4   ? 0.6926 0.4120 2.1638 0.0469  -0.1125 0.1081  4   LYS A CB  
12    C CG  . LYS A 4   ? 0.7274 0.4463 2.2144 0.0605  -0.1176 0.1021  4   LYS A CG  
13    C CD  . LYS A 4   ? 0.8098 0.5128 2.2977 0.0560  -0.1125 0.0994  4   LYS A CD  
14    C CE  . LYS A 4   ? 0.8644 0.5639 2.3650 0.0692  -0.1168 0.0928  4   LYS A CE  
15    N NZ  . LYS A 4   ? 0.8503 0.5794 2.3720 0.0753  -0.1128 0.0831  4   LYS A NZ  
16    N N   . THR A 5   ? 0.5355 0.3222 2.0386 0.0474  -0.1041 0.0948  5   THR A N   
17    C CA  . THR A 5   ? 0.5055 0.3214 2.0284 0.0514  -0.1013 0.0869  5   THR A CA  
18    C C   . THR A 5   ? 0.4866 0.3082 2.0276 0.0636  -0.1036 0.0803  5   THR A C   
19    O O   . THR A 5   ? 0.4672 0.2772 2.0096 0.0642  -0.1010 0.0779  5   THR A O   
20    C CB  . THR A 5   ? 0.4789 0.3081 2.0062 0.0399  -0.0894 0.0828  5   THR A CB  
21    O OG1 . THR A 5   ? 0.5010 0.3251 2.0112 0.0309  -0.0883 0.0889  5   THR A OG1 
22    C CG2 . THR A 5   ? 0.4399 0.2966 1.9857 0.0427  -0.0857 0.0749  5   THR A CG2 
23    N N   . LYS A 6   ? 0.4890 0.3292 2.0438 0.0727  -0.1081 0.0768  6   LYS A N   
24    C CA  . LYS A 6   ? 0.4931 0.3450 2.0677 0.0836  -0.1077 0.0690  6   LYS A CA  
25    C C   . LYS A 6   ? 0.4543 0.3319 2.0430 0.0799  -0.0984 0.0618  6   LYS A C   
26    O O   . LYS A 6   ? 0.4183 0.3114 2.0085 0.0753  -0.0976 0.0622  6   LYS A O   
27    C CB  . LYS A 6   ? 0.5504 0.4038 2.1313 0.0960  -0.1194 0.0707  6   LYS A CB  
28    C CG  . LYS A 6   ? 0.6168 0.4824 2.2200 0.1089  -0.1195 0.0627  6   LYS A CG  
29    C CD  . LYS A 6   ? 0.6881 0.5369 2.2922 0.1153  -0.1177 0.0594  6   LYS A CD  
30    C CE  . LYS A 6   ? 0.7213 0.5835 2.3478 0.1290  -0.1175 0.0511  6   LYS A CE  
31    N NZ  . LYS A 6   ? 0.6918 0.5816 2.3346 0.1270  -0.1077 0.0435  6   LYS A NZ  
32    N N   . ILE A 7   ? 0.4502 0.3299 2.0475 0.0819  -0.0917 0.0551  7   ILE A N   
33    C CA  . ILE A 7   ? 0.4210 0.3195 2.0277 0.0777  -0.0825 0.0488  7   ILE A CA  
34    C C   . ILE A 7   ? 0.4421 0.3506 2.0644 0.0879  -0.0800 0.0412  7   ILE A C   
35    O O   . ILE A 7   ? 0.4406 0.3362 2.0619 0.0931  -0.0793 0.0383  7   ILE A O   
36    C CB  . ILE A 7   ? 0.4197 0.3089 2.0187 0.0687  -0.0760 0.0476  7   ILE A CB  
37    C CG1 . ILE A 7   ? 0.4237 0.3068 2.0103 0.0569  -0.0752 0.0535  7   ILE A CG1 
38    C CG2 . ILE A 7   ? 0.3981 0.3026 2.0064 0.0676  -0.0680 0.0402  7   ILE A CG2 
39    C CD1 . ILE A 7   ? 0.4162 0.2897 1.9983 0.0485  -0.0699 0.0522  7   ILE A CD1 
40    N N   . GLU A 8   ? 0.4914 0.4223 2.1272 0.0896  -0.0774 0.0376  8   GLU A N   
41    C CA  . GLU A 8   ? 0.5203 0.4630 2.1710 0.0971  -0.0717 0.0298  8   GLU A CA  
42    C C   . GLU A 8   ? 0.4776 0.4392 2.1341 0.0905  -0.0628 0.0257  8   GLU A C   
43    O O   . GLU A 8   ? 0.4162 0.3878 2.0718 0.0832  -0.0633 0.0284  8   GLU A O   
44    C CB  . GLU A 8   ? 0.5863 0.5341 2.2509 0.1092  -0.0786 0.0289  8   GLU A CB  
45    C CG  . GLU A 8   ? 0.6813 0.6509 2.3593 0.1095  -0.0821 0.0292  8   GLU A CG  
46    C CD  . GLU A 8   ? 0.7494 0.7161 2.4160 0.1029  -0.0905 0.0369  8   GLU A CD  
47    O OE1 . GLU A 8   ? 0.7199 0.6657 2.3674 0.0989  -0.0945 0.0434  8   GLU A OE1 
48    O OE2 . GLU A 8   ? 0.6742 0.6602 2.3512 0.1013  -0.0919 0.0358  8   GLU A OE2 
49    N N   . LEU A 9   ? 0.4734 0.4377 2.1344 0.0932  -0.0546 0.0191  9   LEU A N   
50    C CA  . LEU A 9   ? 0.4412 0.4179 2.1045 0.0877  -0.0454 0.0150  9   LEU A CA  
51    C C   . LEU A 9   ? 0.4554 0.4492 2.1364 0.0944  -0.0402 0.0092  9   LEU A C   
52    O O   . LEU A 9   ? 0.4872 0.4769 2.1725 0.1026  -0.0371 0.0045  9   LEU A O   
53    C CB  . LEU A 9   ? 0.4288 0.3910 2.0797 0.0854  -0.0401 0.0120  9   LEU A CB  
54    C CG  . LEU A 9   ? 0.4262 0.3673 2.0631 0.0825  -0.0455 0.0157  9   LEU A CG  
55    C CD1 . LEU A 9   ? 0.4306 0.3601 2.0577 0.0809  -0.0409 0.0111  9   LEU A CD1 
56    C CD2 . LEU A 9   ? 0.4401 0.3807 2.0708 0.0730  -0.0492 0.0218  9   LEU A CD2 
57    N N   . LYS A 10  ? 0.4809 0.4938 2.1728 0.0909  -0.0389 0.0090  10  LYS A N   
58    C CA  . LYS A 10  ? 0.5158 0.5468 2.2270 0.0959  -0.0329 0.0032  10  LYS A CA  
59    C C   . LYS A 10  ? 0.4509 0.4985 2.1674 0.0872  -0.0294 0.0033  10  LYS A C   
60    O O   . LYS A 10  ? 0.4442 0.4900 2.1522 0.0803  -0.0347 0.0082  10  LYS A O   
61    C CB  . LYS A 10  ? 0.5524 0.5934 2.2828 0.1057  -0.0400 0.0023  10  LYS A CB  
62    C CG  . LYS A 10  ? 0.6187 0.6675 2.3528 0.1030  -0.0510 0.0077  10  LYS A CG  
63    C CD  . LYS A 10  ? 0.7116 0.7658 2.4616 0.1135  -0.0618 0.0079  10  LYS A CD  
64    C CE  . LYS A 10  ? 0.7877 0.8399 2.5307 0.1104  -0.0749 0.0150  10  LYS A CE  
65    N NZ  . LYS A 10  ? 0.8523 0.8800 2.5701 0.1069  -0.0798 0.0220  10  LYS A NZ  
66    N N   . ASP A 11  ? 0.3989 0.4608 2.1283 0.0874  -0.0196 -0.0024 11  ASP A N   
67    C CA  . ASP A 11  ? 0.3722 0.4438 2.1010 0.0778  -0.0129 -0.0031 11  ASP A CA  
68    C C   . ASP A 11  ? 0.3231 0.3790 2.0294 0.0700  -0.0129 0.0006  11  ASP A C   
69    O O   . ASP A 11  ? 0.2919 0.3519 1.9950 0.0623  -0.0143 0.0032  11  ASP A O   
70    C CB  . ASP A 11  ? 0.3590 0.4498 2.1044 0.0753  -0.0183 -0.0023 11  ASP A CB  
71    C CG  . ASP A 11  ? 0.3924 0.4974 2.1617 0.0847  -0.0219 -0.0056 11  ASP A CG  
72    O OD1 . ASP A 11  ? 0.4247 0.5372 2.2066 0.0890  -0.0122 -0.0116 11  ASP A OD1 
73    O OD2 . ASP A 11  ? 0.4048 0.5118 2.1790 0.0882  -0.0344 -0.0023 11  ASP A OD2 
74    N N   . ASN A 12  ? 0.3175 0.3553 2.0092 0.0724  -0.0119 0.0005  12  ASN A N   
75    C CA  . ASN A 12  ? 0.3149 0.3388 1.9880 0.0657  -0.0112 0.0025  12  ASN A CA  
76    C C   . ASN A 12  ? 0.3007 0.3232 1.9687 0.0593  -0.0188 0.0080  12  ASN A C   
77    O O   . ASN A 12  ? 0.3392 0.3590 1.9989 0.0523  -0.0171 0.0089  12  ASN A O   
78    C CB  . ASN A 12  ? 0.2930 0.3190 1.9616 0.0611  -0.0011 -0.0008 12  ASN A CB  
79    C CG  . ASN A 12  ? 0.3048 0.3291 1.9747 0.0669  0.0078  -0.0063 12  ASN A CG  
80    O OD1 . ASN A 12  ? 0.3038 0.3223 1.9757 0.0749  0.0063  -0.0083 12  ASN A OD1 
81    N ND2 . ASN A 12  ? 0.2823 0.3104 1.9500 0.0629  0.0177  -0.0091 12  ASN A ND2 
82    N N   . TRP A 13  ? 0.2934 0.3153 1.9645 0.0621  -0.0272 0.0116  13  TRP A N   
83    C CA  . TRP A 13  ? 0.2843 0.3029 1.9480 0.0560  -0.0333 0.0168  13  TRP A CA  
84    C C   . TRP A 13  ? 0.2821 0.2858 1.9384 0.0593  -0.0404 0.0207  13  TRP A C   
85    O O   . TRP A 13  ? 0.3259 0.3272 1.9875 0.0674  -0.0438 0.0203  13  TRP A O   
86    C CB  . TRP A 13  ? 0.2963 0.3303 1.9695 0.0541  -0.0370 0.0181  13  TRP A CB  
87    C CG  . TRP A 13  ? 0.2731 0.3178 1.9479 0.0462  -0.0325 0.0166  13  TRP A CG  
88    C CD1 . TRP A 13  ? 0.2540 0.3101 1.9381 0.0452  -0.0254 0.0124  13  TRP A CD1 
89    C CD2 . TRP A 13  ? 0.2679 0.3126 1.9354 0.0384  -0.0346 0.0193  13  TRP A CD2 
90    N NE1 . TRP A 13  ? 0.2607 0.3222 1.9429 0.0373  -0.0236 0.0125  13  TRP A NE1 
91    C CE2 . TRP A 13  ? 0.2440 0.2993 1.9167 0.0334  -0.0292 0.0163  13  TRP A CE2 
92    C CE3 . TRP A 13  ? 0.2854 0.3211 1.9416 0.0348  -0.0394 0.0237  13  TRP A CE3 
93    C CZ2 . TRP A 13  ? 0.2377 0.2951 1.9056 0.0259  -0.0292 0.0170  13  TRP A CZ2 
94    C CZ3 . TRP A 13  ? 0.2822 0.3211 1.9337 0.0272  -0.0386 0.0242  13  TRP A CZ3 
95    C CH2 . TRP A 13  ? 0.2585 0.3083 1.9162 0.0232  -0.0339 0.0207  13  TRP A CH2 
96    N N   . TYR A 14  ? 0.2580 0.2518 1.9029 0.0529  -0.0427 0.0245  14  TYR A N   
97    C CA  . TYR A 14  ? 0.2491 0.2288 1.8863 0.0544  -0.0494 0.0293  14  TYR A CA  
98    C C   . TYR A 14  ? 0.2433 0.2298 1.8836 0.0561  -0.0561 0.0329  14  TYR A C   
99    O O   . TYR A 14  ? 0.2328 0.2318 1.8760 0.0516  -0.0555 0.0328  14  TYR A O   
100   C CB  . TYR A 14  ? 0.2437 0.2119 1.8692 0.0460  -0.0489 0.0323  14  TYR A CB  
101   C CG  . TYR A 14  ? 0.2270 0.1845 1.8486 0.0448  -0.0457 0.0294  14  TYR A CG  
102   C CD1 . TYR A 14  ? 0.2112 0.1746 1.8356 0.0441  -0.0403 0.0244  14  TYR A CD1 
103   C CD2 . TYR A 14  ? 0.2278 0.1682 1.8421 0.0441  -0.0486 0.0316  14  TYR A CD2 
104   C CE1 . TYR A 14  ? 0.2082 0.1608 1.8275 0.0434  -0.0390 0.0216  14  TYR A CE1 
105   C CE2 . TYR A 14  ? 0.2218 0.1527 1.8332 0.0427  -0.0469 0.0283  14  TYR A CE2 
106   C CZ  . TYR A 14  ? 0.2087 0.1458 1.8223 0.0427  -0.0427 0.0232  14  TYR A CZ  
107   O OH  . TYR A 14  ? 0.2037 0.1310 1.8131 0.0419  -0.0424 0.0196  14  TYR A OH  
108   N N   . HIS A 15  ? 0.2559 0.2331 1.8949 0.0628  -0.0631 0.0358  15  HIS A N   
109   C CA  . HIS A 15  ? 0.2668 0.2442 1.9033 0.0641  -0.0720 0.0407  15  HIS A CA  
110   C C   . HIS A 15  ? 0.2905 0.2465 1.9097 0.0614  -0.0765 0.0473  15  HIS A C   
111   O O   . HIS A 15  ? 0.3191 0.2606 1.9336 0.0626  -0.0749 0.0473  15  HIS A O   
112   C CB  . HIS A 15  ? 0.2750 0.2593 1.9257 0.0754  -0.0780 0.0388  15  HIS A CB  
113   C CG  . HIS A 15  ? 0.2577 0.2646 1.9267 0.0768  -0.0732 0.0327  15  HIS A CG  
114   N ND1 . HIS A 15  ? 0.2487 0.2610 1.9245 0.0770  -0.0631 0.0268  15  HIS A ND1 
115   C CD2 . HIS A 15  ? 0.2444 0.2685 1.9246 0.0767  -0.0767 0.0315  15  HIS A CD2 
116   C CE1 . HIS A 15  ? 0.2323 0.2644 1.9234 0.0769  -0.0596 0.0225  15  HIS A CE1 
117   N NE2 . HIS A 15  ? 0.2370 0.2772 1.9324 0.0768  -0.0679 0.0250  15  HIS A NE2 
118   N N   . LEU A 16  ? 0.2963 0.2489 1.9047 0.0574  -0.0820 0.0527  16  LEU A N   
119   C CA  . LEU A 16  ? 0.3083 0.2390 1.8982 0.0540  -0.0855 0.0596  16  LEU A CA  
120   C C   . LEU A 16  ? 0.3248 0.2505 1.9073 0.0583  -0.0968 0.0651  16  LEU A C   
121   O O   . LEU A 16  ? 0.3148 0.2484 1.8928 0.0544  -0.0993 0.0664  16  LEU A O   
122   C CB  . LEU A 16  ? 0.3059 0.2330 1.8843 0.0416  -0.0781 0.0612  16  LEU A CB  
123   C CG  . LEU A 16  ? 0.3069 0.2234 1.8838 0.0373  -0.0714 0.0599  16  LEU A CG  
124   C CD1 . LEU A 16  ? 0.2838 0.2115 1.8751 0.0398  -0.0657 0.0525  16  LEU A CD1 
125   C CD2 . LEU A 16  ? 0.3181 0.2309 1.8839 0.0255  -0.0657 0.0624  16  LEU A CD2 
126   N N   . ASP A 17  ? 0.3449 0.2572 1.9269 0.0674  -0.1045 0.0676  17  ASP A N   
127   C CA  . ASP A 17  ? 0.3625 0.2718 1.9421 0.0748  -0.1175 0.0717  17  ASP A CA  
128   C C   . ASP A 17  ? 0.3356 0.2707 1.9339 0.0788  -0.1207 0.0666  17  ASP A C   
129   O O   . ASP A 17  ? 0.3320 0.2697 1.9239 0.0778  -0.1290 0.0696  17  ASP A O   
130   C CB  . ASP A 17  ? 0.3914 0.2831 1.9447 0.0674  -0.1222 0.0802  17  ASP A CB  
131   C CG  . ASP A 17  ? 0.4134 0.2802 1.9479 0.0608  -0.1175 0.0855  17  ASP A CG  
132   O OD1 . ASP A 17  ? 0.4335 0.2830 1.9663 0.0673  -0.1219 0.0878  17  ASP A OD1 
133   O OD2 . ASP A 17  ? 0.4268 0.2916 1.9492 0.0490  -0.1096 0.0871  17  ASP A OD2 
134   N N   . GLY A 18  ? 0.3165 0.2696 1.9369 0.0829  -0.1140 0.0587  18  GLY A N   
135   C CA  . GLY A 18  ? 0.3155 0.2925 1.9578 0.0882  -0.1171 0.0534  18  GLY A CA  
136   C C   . GLY A 18  ? 0.3043 0.3002 1.9517 0.0789  -0.1092 0.0494  18  GLY A C   
137   O O   . GLY A 18  ? 0.2817 0.2985 1.9501 0.0816  -0.1068 0.0433  18  GLY A O   
138   N N   . GLU A 19  ? 0.3122 0.3006 1.9413 0.0679  -0.1044 0.0525  19  GLU A N   
139   C CA  . GLU A 19  ? 0.3046 0.3080 1.9361 0.0593  -0.0984 0.0492  19  GLU A CA  
140   C C   . GLU A 19  ? 0.2940 0.2988 1.9271 0.0538  -0.0852 0.0455  19  GLU A C   
141   O O   . GLU A 19  ? 0.3292 0.3190 1.9527 0.0523  -0.0815 0.0476  19  GLU A O   
142   C CB  . GLU A 19  ? 0.3203 0.3148 1.9308 0.0521  -0.1035 0.0546  19  GLU A CB  
143   C CG  . GLU A 19  ? 0.3465 0.3390 1.9543 0.0584  -0.1186 0.0581  19  GLU A CG  
144   C CD  . GLU A 19  ? 0.3527 0.3692 1.9850 0.0633  -0.1235 0.0521  19  GLU A CD  
145   O OE1 . GLU A 19  ? 0.3414 0.3738 1.9817 0.0568  -0.1170 0.0472  19  GLU A OE1 
146   O OE2 . GLU A 19  ? 0.3685 0.3877 2.0131 0.0736  -0.1336 0.0521  19  GLU A OE2 
147   N N   . LYS A 20  ? 0.2823 0.3044 1.9279 0.0508  -0.0788 0.0400  20  LYS A N   
148   C CA  . LYS A 20  ? 0.2606 0.2840 1.9074 0.0460  -0.0676 0.0364  20  LYS A CA  
149   C C   . LYS A 20  ? 0.2441 0.2560 1.8737 0.0371  -0.0644 0.0396  20  LYS A C   
150   O O   . LYS A 20  ? 0.2383 0.2506 1.8591 0.0319  -0.0670 0.0418  20  LYS A O   
151   C CB  . LYS A 20  ? 0.2667 0.3092 1.9277 0.0437  -0.0625 0.0309  20  LYS A CB  
152   C CG  . LYS A 20  ? 0.2857 0.3421 1.9671 0.0514  -0.0625 0.0264  20  LYS A CG  
153   C CD  . LYS A 20  ? 0.2935 0.3643 1.9860 0.0472  -0.0534 0.0209  20  LYS A CD  
154   C CE  . LYS A 20  ? 0.3045 0.3881 2.0168 0.0535  -0.0492 0.0158  20  LYS A CE  
155   N NZ  . LYS A 20  ? 0.2998 0.4031 2.0303 0.0529  -0.0518 0.0127  20  LYS A NZ  
156   N N   . TYR A 21  ? 0.2340 0.2358 1.8595 0.0356  -0.0587 0.0393  21  TYR A N   
157   C CA  . TYR A 21  ? 0.2298 0.2227 1.8437 0.0273  -0.0543 0.0410  21  TYR A CA  
158   C C   . TYR A 21  ? 0.2092 0.2064 1.8289 0.0242  -0.0464 0.0362  21  TYR A C   
159   O O   . TYR A 21  ? 0.1983 0.1932 1.8232 0.0287  -0.0445 0.0336  21  TYR A O   
160   C CB  . TYR A 21  ? 0.2524 0.2268 1.8562 0.0276  -0.0562 0.0453  21  TYR A CB  
161   C CG  . TYR A 21  ? 0.2631 0.2272 1.8548 0.0185  -0.0525 0.0482  21  TYR A CG  
162   C CD1 . TYR A 21  ? 0.2786 0.2364 1.8566 0.0142  -0.0551 0.0532  21  TYR A CD1 
163   C CD2 . TYR A 21  ? 0.2603 0.2193 1.8537 0.0146  -0.0469 0.0462  21  TYR A CD2 
164   C CE1 . TYR A 21  ? 0.2833 0.2315 1.8502 0.0056  -0.0501 0.0557  21  TYR A CE1 
165   C CE2 . TYR A 21  ? 0.2684 0.2196 1.8540 0.0062  -0.0429 0.0483  21  TYR A CE2 
166   C CZ  . TYR A 21  ? 0.2805 0.2264 1.8529 0.0015  -0.0436 0.0531  21  TYR A CZ  
167   O OH  . TYR A 21  ? 0.2816 0.2195 1.8458 -0.0073 -0.0380 0.0551  21  TYR A OH  
168   N N   . PHE A 22  ? 0.1935 0.1957 1.8110 0.0170  -0.0423 0.0350  22  PHE A N   
169   C CA  . PHE A 22  ? 0.1847 0.1905 1.8070 0.0141  -0.0361 0.0307  22  PHE A CA  
170   C C   . PHE A 22  ? 0.1925 0.1883 1.8092 0.0090  -0.0337 0.0318  22  PHE A C   
171   O O   . PHE A 22  ? 0.1992 0.1928 1.8092 0.0034  -0.0327 0.0339  22  PHE A O   
172   C CB  . PHE A 22  ? 0.1863 0.2039 1.8118 0.0099  -0.0333 0.0280  22  PHE A CB  
173   C CG  . PHE A 22  ? 0.1814 0.2016 1.8120 0.0085  -0.0281 0.0237  22  PHE A CG  
174   C CD1 . PHE A 22  ? 0.1870 0.2017 1.8155 0.0044  -0.0252 0.0227  22  PHE A CD1 
175   C CD2 . PHE A 22  ? 0.1818 0.2090 1.8191 0.0113  -0.0262 0.0209  22  PHE A CD2 
176   C CE1 . PHE A 22  ? 0.1876 0.2029 1.8198 0.0041  -0.0223 0.0191  22  PHE A CE1 
177   C CE2 . PHE A 22  ? 0.1774 0.2036 1.8159 0.0102  -0.0220 0.0178  22  PHE A CE2 
178   C CZ  . PHE A 22  ? 0.1800 0.1998 1.8153 0.0069  -0.0209 0.0171  22  PHE A CZ  
179   N N   . ILE A 23  ? 0.1966 0.1862 1.8159 0.0105  -0.0325 0.0298  23  ILE A N   
180   C CA  . ILE A 23  ? 0.2107 0.1905 1.8270 0.0060  -0.0314 0.0308  23  ILE A CA  
181   C C   . ILE A 23  ? 0.2139 0.1998 1.8344 0.0000  -0.0268 0.0276  23  ILE A C   
182   O O   . ILE A 23  ? 0.2121 0.2007 1.8381 0.0013  -0.0259 0.0238  23  ILE A O   
183   C CB  . ILE A 23  ? 0.2164 0.1863 1.8338 0.0100  -0.0335 0.0296  23  ILE A CB  
184   C CG1 . ILE A 23  ? 0.2318 0.1962 1.8465 0.0172  -0.0377 0.0318  23  ILE A CG1 
185   C CG2 . ILE A 23  ? 0.2208 0.1810 1.8372 0.0045  -0.0329 0.0304  23  ILE A CG2 
186   C CD1 . ILE A 23  ? 0.2418 0.1967 1.8569 0.0222  -0.0391 0.0292  23  ILE A CD1 
187   N N   . LYS A 24  ? 0.2238 0.2106 1.8406 -0.0061 -0.0240 0.0292  24  LYS A N   
188   C CA  . LYS A 24  ? 0.2171 0.2095 1.8389 -0.0117 -0.0190 0.0258  24  LYS A CA  
189   C C   . LYS A 24  ? 0.2127 0.1984 1.8380 -0.0160 -0.0169 0.0256  24  LYS A C   
190   O O   . LYS A 24  ? 0.2092 0.1906 1.8293 -0.0216 -0.0136 0.0282  24  LYS A O   
191   C CB  . LYS A 24  ? 0.2290 0.2270 1.8449 -0.0158 -0.0160 0.0263  24  LYS A CB  
192   C CG  . LYS A 24  ? 0.2421 0.2472 1.8561 -0.0121 -0.0191 0.0263  24  LYS A CG  
193   C CD  . LYS A 24  ? 0.2627 0.2739 1.8720 -0.0162 -0.0169 0.0251  24  LYS A CD  
194   C CE  . LYS A 24  ? 0.2903 0.2960 1.8858 -0.0202 -0.0169 0.0288  24  LYS A CE  
195   N NZ  . LYS A 24  ? 0.3014 0.3114 1.8932 -0.0257 -0.0119 0.0255  24  LYS A NZ  
196   N N   . ALA A 25  ? 0.2063 0.1899 1.8395 -0.0137 -0.0191 0.0225  25  ALA A N   
197   C CA  . ALA A 25  ? 0.2207 0.1974 1.8591 -0.0171 -0.0192 0.0220  25  ALA A CA  
198   C C   . ALA A 25  ? 0.2261 0.2095 1.8778 -0.0207 -0.0166 0.0167  25  ALA A C   
199   O O   . ALA A 25  ? 0.2187 0.2103 1.8744 -0.0196 -0.0154 0.0136  25  ALA A O   
200   C CB  . ALA A 25  ? 0.2172 0.1846 1.8537 -0.0117 -0.0251 0.0223  25  ALA A CB  
201   N N   . ILE A 26  ? 0.2394 0.2193 1.8994 -0.0253 -0.0159 0.0155  26  ILE A N   
202   C CA  . ILE A 26  ? 0.2270 0.2128 1.9034 -0.0272 -0.0160 0.0097  26  ILE A CA  
203   C C   . ILE A 26  ? 0.2325 0.2104 1.9153 -0.0284 -0.0207 0.0087  26  ILE A C   
204   O O   . ILE A 26  ? 0.2441 0.2131 1.9210 -0.0316 -0.0197 0.0125  26  ILE A O   
205   C CB  . ILE A 26  ? 0.2133 0.2079 1.8984 -0.0342 -0.0074 0.0077  26  ILE A CB  
206   C CG1 . ILE A 26  ? 0.2016 0.2049 1.9056 -0.0339 -0.0083 0.0009  26  ILE A CG1 
207   C CG2 . ILE A 26  ? 0.2236 0.2127 1.9080 -0.0420 -0.0018 0.0105  26  ILE A CG2 
208   C CD1 . ILE A 26  ? 0.1990 0.2126 1.9121 -0.0389 0.0009  -0.0025 26  ILE A CD1 
209   N N   . GLY A 27  ? 0.2176 0.1967 1.9108 -0.0257 -0.0268 0.0036  27  GLY A N   
210   C CA  . GLY A 27  ? 0.2272 0.2005 1.9299 -0.0281 -0.0317 0.0012  27  GLY A CA  
211   C C   . GLY A 27  ? 0.2242 0.2023 1.9405 -0.0375 -0.0246 0.0005  27  GLY A C   
212   O O   . GLY A 27  ? 0.2254 0.2148 1.9508 -0.0406 -0.0179 -0.0016 27  GLY A O   
213   N N   . TYR A 28  ? 0.2244 0.1934 1.9419 -0.0423 -0.0254 0.0019  28  TYR A N   
214   C CA  . TYR A 28  ? 0.2299 0.2023 1.9604 -0.0524 -0.0176 0.0013  28  TYR A CA  
215   C C   . TYR A 28  ? 0.2405 0.2048 1.9806 -0.0562 -0.0233 -0.0007 28  TYR A C   
216   O O   . TYR A 28  ? 0.2584 0.2087 1.9850 -0.0526 -0.0297 0.0020  28  TYR A O   
217   C CB  . TYR A 28  ? 0.2384 0.2047 1.9523 -0.0571 -0.0085 0.0084  28  TYR A CB  
218   C CG  . TYR A 28  ? 0.2546 0.2205 1.9765 -0.0687 0.0013  0.0091  28  TYR A CG  
219   C CD1 . TYR A 28  ? 0.2624 0.2430 2.0063 -0.0746 0.0084  0.0032  28  TYR A CD1 
220   C CD2 . TYR A 28  ? 0.2819 0.2322 1.9897 -0.0738 0.0038  0.0155  28  TYR A CD2 
221   C CE1 . TYR A 28  ? 0.2845 0.2652 2.0372 -0.0861 0.0189  0.0033  28  TYR A CE1 
222   C CE2 . TYR A 28  ? 0.3074 0.2554 2.0210 -0.0855 0.0137  0.0165  28  TYR A CE2 
223   C CZ  . TYR A 28  ? 0.3070 0.2709 2.0436 -0.0921 0.0220  0.0102  28  TYR A CZ  
224   O OH  . TYR A 28  ? 0.3050 0.2679 2.0484 -0.1044 0.0339  0.0107  28  TYR A OH  
225   N N   . GLU A 29  ? 0.2456 0.2188 2.0097 -0.0636 -0.0208 -0.0059 29  GLU A N   
226   C CA  . GLU A 29  ? 0.2426 0.2105 2.0207 -0.0685 -0.0265 -0.0093 29  GLU A CA  
227   C C   . GLU A 29  ? 0.2503 0.2264 2.0490 -0.0807 -0.0159 -0.0113 29  GLU A C   
228   O O   . GLU A 29  ? 0.2505 0.2432 2.0730 -0.0828 -0.0133 -0.0176 29  GLU A O   
229   C CB  . GLU A 29  ? 0.2318 0.2055 2.0253 -0.0628 -0.0391 -0.0168 29  GLU A CB  
230   C CG  . GLU A 29  ? 0.2419 0.2092 2.0487 -0.0668 -0.0481 -0.0212 29  GLU A CG  
231   C CD  . GLU A 29  ? 0.2457 0.2139 2.0581 -0.0587 -0.0631 -0.0274 29  GLU A CD  
232   O OE1 . GLU A 29  ? 0.2324 0.2158 2.0644 -0.0567 -0.0655 -0.0329 29  GLU A OE1 
233   O OE2 . GLU A 29  ? 0.2494 0.2012 2.0446 -0.0542 -0.0724 -0.0264 29  GLU A OE2 
234   N N   . ILE A 30  ? 0.2806 0.2444 2.0710 -0.0889 -0.0100 -0.0063 30  ILE A N   
235   C CA  . ILE A 30  ? 0.2888 0.2569 2.0973 -0.1022 0.0006  -0.0078 30  ILE A CA  
236   C C   . ILE A 30  ? 0.2999 0.2722 2.1362 -0.1061 -0.0078 -0.0155 30  ILE A C   
237   O O   . ILE A 30  ? 0.3179 0.2830 2.1513 -0.0990 -0.0222 -0.0177 30  ILE A O   
238   C CB  . ILE A 30  ? 0.3063 0.2553 2.0921 -0.1093 0.0084  0.0012  30  ILE A CB  
239   C CG1 . ILE A 30  ? 0.3158 0.2690 2.1128 -0.1238 0.0246  0.0016  30  ILE A CG1 
240   C CG2 . ILE A 30  ? 0.3115 0.2406 2.0875 -0.1079 -0.0025 0.0034  30  ILE A CG2 
241   C CD1 . ILE A 30  ? 0.3089 0.2776 2.1079 -0.1249 0.0373  0.0004  30  ILE A CD1 
242   N N   . GLY A 31  ? 0.2981 0.2820 2.1609 -0.1176 0.0017  -0.0198 31  GLY A N   
243   C CA  . GLY A 31  ? 0.2955 0.2864 2.1897 -0.1232 -0.0051 -0.0278 31  GLY A CA  
244   C C   . GLY A 31  ? 0.2822 0.2889 2.1973 -0.1139 -0.0177 -0.0364 31  GLY A C   
245   O O   . GLY A 31  ? 0.2862 0.2925 2.2164 -0.1125 -0.0316 -0.0422 31  GLY A O   
246   N N   . ALA A 32  ? 0.2804 0.2994 2.1941 -0.1072 -0.0133 -0.0371 32  ALA A N   
247   C CA  . ALA A 32  ? 0.2606 0.2919 2.1890 -0.0971 -0.0250 -0.0439 32  ALA A CA  
248   C C   . ALA A 32  ? 0.2366 0.2902 2.1898 -0.0988 -0.0141 -0.0494 32  ALA A C   
249   O O   . ALA A 32  ? 0.2384 0.3001 2.1940 -0.0893 -0.0192 -0.0524 32  ALA A O   
250   C CB  . ALA A 32  ? 0.2520 0.2717 2.1489 -0.0846 -0.0335 -0.0391 32  ALA A CB  
251   N N   . ARG A 33  ? 0.2232 0.2856 2.1941 -0.1110 0.0015  -0.0508 33  ARG A N   
252   C CA  . ARG A 33  ? 0.2076 0.2927 2.2083 -0.1132 0.0118  -0.0582 33  ARG A CA  
253   C C   . ARG A 33  ? 0.1995 0.3004 2.2393 -0.1099 -0.0017 -0.0689 33  ARG A C   
254   O O   . ARG A 33  ? 0.1914 0.2852 2.2354 -0.1080 -0.0180 -0.0707 33  ARG A O   
255   C CB  . ARG A 33  ? 0.2123 0.3047 2.2262 -0.1279 0.0331  -0.0587 33  ARG A CB  
256   C CG  . ARG A 33  ? 0.2127 0.3005 2.1993 -0.1299 0.0505  -0.0523 33  ARG A CG  
257   C CD  . ARG A 33  ? 0.2133 0.2793 2.1563 -0.1226 0.0430  -0.0421 33  ARG A CD  
258   N NE  . ARG A 33  ? 0.2204 0.2818 2.1378 -0.1251 0.0584  -0.0363 33  ARG A NE  
259   C CZ  . ARG A 33  ? 0.2280 0.2712 2.1077 -0.1221 0.0572  -0.0268 33  ARG A CZ  
260   N NH1 . ARG A 33  ? 0.2245 0.2535 2.0878 -0.1152 0.0421  -0.0223 33  ARG A NH1 
261   N NH2 . ARG A 33  ? 0.2379 0.2774 2.0967 -0.1259 0.0712  -0.0223 33  ARG A NH2 
262   N N   . PRO A 34  ? 0.2008 0.3227 2.2687 -0.1077 0.0039  -0.0767 34  PRO A N   
263   C CA  . PRO A 34  ? 0.1963 0.3375 2.3101 -0.1076 -0.0047 -0.0880 34  PRO A CA  
264   C C   . PRO A 34  ? 0.2084 0.3518 2.3441 -0.1217 -0.0007 -0.0903 34  PRO A C   
265   O O   . PRO A 34  ? 0.2196 0.3635 2.3540 -0.1339 0.0191  -0.0875 34  PRO A O   
266   C CB  . PRO A 34  ? 0.1881 0.3504 2.3249 -0.1064 0.0089  -0.0945 34  PRO A CB  
267   C CG  . PRO A 34  ? 0.1927 0.3453 2.2941 -0.1092 0.0273  -0.0861 34  PRO A CG  
268   C CD  . PRO A 34  ? 0.1962 0.3239 2.2530 -0.1041 0.0171  -0.0755 34  PRO A CD  
269   N N   . GLY A 35  ? 0.2103 0.3532 2.3638 -0.1201 -0.0199 -0.0952 35  GLY A N   
270   C CA  . GLY A 35  ? 0.2232 0.3660 2.3971 -0.1331 -0.0197 -0.0978 35  GLY A CA  
271   C C   . GLY A 35  ? 0.2396 0.3552 2.3797 -0.1334 -0.0312 -0.0903 35  GLY A C   
272   O O   . GLY A 35  ? 0.2485 0.3610 2.4040 -0.1376 -0.0438 -0.0945 35  GLY A O   
273   N N   . GLN A 36  ? 0.2489 0.3450 2.3435 -0.1281 -0.0278 -0.0800 36  GLN A N   
274   C CA  . GLN A 36  ? 0.2694 0.3394 2.3305 -0.1291 -0.0342 -0.0723 36  GLN A CA  
275   C C   . GLN A 36  ? 0.3015 0.3587 2.3428 -0.1152 -0.0562 -0.0722 36  GLN A C   
276   O O   . GLN A 36  ? 0.2993 0.3617 2.3357 -0.1037 -0.0626 -0.0734 36  GLN A O   
277   C CB  . GLN A 36  ? 0.2620 0.3174 2.2848 -0.1307 -0.0185 -0.0611 36  GLN A CB  
278   C CG  . GLN A 36  ? 0.2563 0.3234 2.2886 -0.1411 0.0050  -0.0601 36  GLN A CG  
279   C CD  . GLN A 36  ? 0.2685 0.3163 2.2611 -0.1449 0.0179  -0.0485 36  GLN A CD  
280   O OE1 . GLN A 36  ? 0.2686 0.3060 2.2285 -0.1350 0.0153  -0.0421 36  GLN A OE1 
281   N NE2 . GLN A 36  ? 0.2813 0.3230 2.2763 -0.1594 0.0313  -0.0457 36  GLN A NE2 
282   N N   . ALA A 37  ? 0.3773 0.4158 2.4053 -0.1169 -0.0672 -0.0707 37  ALA A N   
283   C CA  . ALA A 37  ? 0.4158 0.4355 2.4132 -0.1051 -0.0839 -0.0682 37  ALA A CA  
284   C C   . ALA A 37  ? 0.4091 0.4039 2.3719 -0.1079 -0.0797 -0.0596 37  ALA A C   
285   O O   . ALA A 37  ? 0.3807 0.3663 2.3485 -0.1182 -0.0784 -0.0595 37  ALA A O   
286   C CB  . ALA A 37  ? 0.4629 0.4835 2.4800 -0.1027 -0.1050 -0.0772 37  ALA A CB  
287   N N   . PRO A 38  ? 0.3855 0.3688 2.3130 -0.0989 -0.0773 -0.0520 38  PRO A N   
288   C CA  . PRO A 38  ? 0.3960 0.3579 2.2921 -0.1006 -0.0714 -0.0434 38  PRO A CA  
289   C C   . PRO A 38  ? 0.4048 0.3454 2.2882 -0.0997 -0.0848 -0.0445 38  PRO A C   
290   O O   . PRO A 38  ? 0.4274 0.3534 2.3014 -0.1069 -0.0795 -0.0402 38  PRO A O   
291   C CB  . PRO A 38  ? 0.3679 0.3267 2.2350 -0.0902 -0.0671 -0.0368 38  PRO A CB  
292   C CG  . PRO A 38  ? 0.3703 0.3438 2.2485 -0.0814 -0.0747 -0.0423 38  PRO A CG  
293   C CD  . PRO A 38  ? 0.3760 0.3662 2.2936 -0.0869 -0.0801 -0.0517 38  PRO A CD  
294   N N   . TYR A 39  ? 0.4018 0.3394 2.2844 -0.0913 -0.1020 -0.0503 39  TYR A N   
295   C CA  . TYR A 39  ? 0.4019 0.3183 2.2698 -0.0893 -0.1156 -0.0525 39  TYR A CA  
296   C C   . TYR A 39  ? 0.4419 0.3612 2.3393 -0.0985 -0.1254 -0.0610 39  TYR A C   
297   O O   . TYR A 39  ? 0.4608 0.3625 2.3482 -0.0975 -0.1383 -0.0642 39  TYR A O   
298   C CB  . TYR A 39  ? 0.3860 0.2949 2.2326 -0.0754 -0.1289 -0.0543 39  TYR A CB  
299   C CG  . TYR A 39  ? 0.3653 0.2706 2.1830 -0.0662 -0.1204 -0.0466 39  TYR A CG  
300   C CD1 . TYR A 39  ? 0.3710 0.2564 2.1587 -0.0625 -0.1179 -0.0411 39  TYR A CD1 
301   C CD2 . TYR A 39  ? 0.3232 0.2452 2.1454 -0.0617 -0.1147 -0.0453 39  TYR A CD2 
302   C CE1 . TYR A 39  ? 0.3522 0.2360 2.1172 -0.0547 -0.1101 -0.0346 39  TYR A CE1 
303   C CE2 . TYR A 39  ? 0.3234 0.2426 2.1211 -0.0545 -0.1068 -0.0386 39  TYR A CE2 
304   C CZ  . TYR A 39  ? 0.3272 0.2282 2.0972 -0.0512 -0.1046 -0.0332 39  TYR A CZ  
305   O OH  . TYR A 39  ? 0.3039 0.2037 2.0528 -0.0442 -0.0975 -0.0273 39  TYR A OH  
306   N N   . GLU A 40  ? 0.4644 0.4056 2.3985 -0.1074 -0.1196 -0.0652 40  GLU A N   
307   C CA  . GLU A 40  ? 0.5041 0.4513 2.4712 -0.1167 -0.1288 -0.0740 40  GLU A CA  
308   C C   . GLU A 40  ? 0.5225 0.4731 2.5078 -0.1329 -0.1128 -0.0720 40  GLU A C   
309   O O   . GLU A 40  ? 0.5237 0.4660 2.5210 -0.1426 -0.1177 -0.0756 40  GLU A O   
310   C CB  . GLU A 40  ? 0.5364 0.5083 2.5383 -0.1140 -0.1374 -0.0829 40  GLU A CB  
311   C CG  . GLU A 40  ? 0.5521 0.5234 2.5382 -0.0984 -0.1507 -0.0842 40  GLU A CG  
312   C CD  . GLU A 40  ? 0.6052 0.5986 2.6287 -0.0962 -0.1622 -0.0938 40  GLU A CD  
313   O OE1 . GLU A 40  ? 0.6236 0.6404 2.6824 -0.1032 -0.1514 -0.0968 40  GLU A OE1 
314   O OE2 . GLU A 40  ? 0.6609 0.6485 2.6794 -0.0872 -0.1823 -0.0986 40  GLU A OE2 
315   N N   . ASP A 41  ? 0.5405 0.5021 2.5265 -0.1363 -0.0934 -0.0661 41  ASP A N   
316   C CA  . ASP A 41  ? 0.5750 0.5406 2.5769 -0.1521 -0.0759 -0.0638 41  ASP A CA  
317   C C   . ASP A 41  ? 0.6407 0.5782 2.6121 -0.1573 -0.0706 -0.0553 41  ASP A C   
318   O O   . ASP A 41  ? 0.6674 0.5869 2.6017 -0.1474 -0.0727 -0.0483 41  ASP A O   
319   C CB  . ASP A 41  ? 0.5500 0.5328 2.5562 -0.1536 -0.0565 -0.0600 41  ASP A CB  
320   C CG  . ASP A 41  ? 0.5525 0.5661 2.6001 -0.1548 -0.0545 -0.0690 41  ASP A CG  
321   O OD1 . ASP A 41  ? 0.5621 0.5868 2.6435 -0.1582 -0.0661 -0.0787 41  ASP A OD1 
322   O OD2 . ASP A 41  ? 0.5403 0.5666 2.5867 -0.1522 -0.0416 -0.0667 41  ASP A OD2 
323   N N   . GLU A 42  ? 0.6394 0.5736 2.6281 -0.1732 -0.0629 -0.0560 42  GLU A N   
324   C CA  . GLU A 42  ? 0.6802 0.5899 2.6430 -0.1808 -0.0524 -0.0465 42  GLU A CA  
325   C C   . GLU A 42  ? 0.6685 0.5741 2.6004 -0.1749 -0.0388 -0.0359 42  GLU A C   
326   O O   . GLU A 42  ? 0.6429 0.5675 2.5854 -0.1769 -0.0257 -0.0353 42  GLU A O   
327   C CB  . GLU A 42  ? 0.7303 0.6440 2.7206 -0.2005 -0.0400 -0.0482 42  GLU A CB  
328   C CG  . GLU A 42  ? 0.7979 0.6846 2.7606 -0.2098 -0.0274 -0.0374 42  GLU A CG  
329   C CD  . GLU A 42  ? 0.8631 0.7497 2.8510 -0.2306 -0.0158 -0.0390 42  GLU A CD  
330   O OE1 . GLU A 42  ? 0.8297 0.7187 2.8448 -0.2373 -0.0266 -0.0478 42  GLU A OE1 
331   O OE2 . GLU A 42  ? 0.9532 0.8364 2.9326 -0.2405 0.0041  -0.0315 42  GLU A OE2 
332   N N   . ARG A 43  ? 0.6753 0.5550 2.5695 -0.1682 -0.0417 -0.0279 43  ARG A N   
333   C CA  . ARG A 43  ? 0.7156 0.5898 2.5790 -0.1606 -0.0328 -0.0184 43  ARG A CA  
334   C C   . ARG A 43  ? 0.6621 0.5336 2.5211 -0.1732 -0.0129 -0.0108 43  ARG A C   
335   O O   . ARG A 43  ? 0.6824 0.5370 2.5396 -0.1851 -0.0081 -0.0077 43  ARG A O   
336   C CB  . ARG A 43  ? 0.8501 0.6963 2.6781 -0.1513 -0.0417 -0.0125 43  ARG A CB  
337   C CG  . ARG A 43  ? 0.9455 0.7861 2.7688 -0.1394 -0.0605 -0.0189 43  ARG A CG  
338   C CD  . ARG A 43  ? 1.0614 0.8747 2.8491 -0.1305 -0.0650 -0.0125 43  ARG A CD  
339   N NE  . ARG A 43  ? 1.0883 0.8946 2.8550 -0.1310 -0.0520 -0.0016 43  ARG A NE  
340   C CZ  . ARG A 43  ? 1.0761 0.8589 2.8262 -0.1371 -0.0469 0.0057  43  ARG A CZ  
341   N NH1 . ARG A 43  ? 1.0762 0.8582 2.8185 -0.1440 -0.0327 0.0139  43  ARG A NH1 
342   N NH2 . ARG A 43  ? 1.0326 0.7922 2.7754 -0.1378 -0.0556 0.0045  43  ARG A NH2 
343   N N   . LYS A 44  ? 0.6144 0.4998 2.4680 -0.1703 -0.0017 -0.0075 44  LYS A N   
344   C CA  . LYS A 44  ? 0.6118 0.4928 2.4538 -0.1803 0.0172  0.0003  44  LYS A CA  
345   C C   . LYS A 44  ? 0.6040 0.4830 2.4156 -0.1692 0.0204  0.0076  44  LYS A C   
346   O O   . LYS A 44  ? 0.6045 0.4971 2.4166 -0.1566 0.0132  0.0043  44  LYS A O   
347   C CB  . LYS A 44  ? 0.6210 0.5274 2.4966 -0.1918 0.0313  -0.0059 44  LYS A CB  
348   C CG  . LYS A 44  ? 0.6370 0.5595 2.5553 -0.1984 0.0247  -0.0175 44  LYS A CG  
349   C CD  . LYS A 44  ? 0.6424 0.5912 2.5972 -0.2099 0.0401  -0.0242 44  LYS A CD  
350   C CE  . LYS A 44  ? 0.6831 0.6205 2.6292 -0.2266 0.0608  -0.0173 44  LYS A CE  
351   N NZ  . LYS A 44  ? 0.7005 0.6586 2.6886 -0.2419 0.0736  -0.0255 44  LYS A NZ  
352   N N   . ASP A 45  ? 0.5760 0.4381 2.3616 -0.1750 0.0319  0.0176  45  ASP A N   
353   C CA  . ASP A 45  ? 0.5358 0.3914 2.2895 -0.1651 0.0331  0.0254  45  ASP A CA  
354   C C   . ASP A 45  ? 0.4998 0.3808 2.2632 -0.1625 0.0416  0.0218  45  ASP A C   
355   O O   . ASP A 45  ? 0.4911 0.3788 2.2438 -0.1497 0.0355  0.0220  45  ASP A O   
356   C CB  . ASP A 45  ? 0.5502 0.3776 2.2729 -0.1717 0.0401  0.0369  45  ASP A CB  
357   C CG  . ASP A 45  ? 0.5653 0.3665 2.2766 -0.1702 0.0287  0.0399  45  ASP A CG  
358   O OD1 . ASP A 45  ? 0.5426 0.3465 2.2607 -0.1596 0.0141  0.0344  45  ASP A OD1 
359   O OD2 . ASP A 45  ? 0.6024 0.3799 2.2986 -0.1804 0.0348  0.0472  45  ASP A OD2 
360   N N   . GLU A 46  ? 0.4871 0.3817 2.2711 -0.1752 0.0564  0.0182  46  GLU A N   
361   C CA  . GLU A 46  ? 0.4502 0.3688 2.2469 -0.1740 0.0660  0.0135  46  GLU A CA  
362   C C   . GLU A 46  ? 0.4258 0.3359 2.1883 -0.1715 0.0745  0.0219  46  GLU A C   
363   O O   . GLU A 46  ? 0.4104 0.3355 2.1730 -0.1640 0.0756  0.0192  46  GLU A O   
364   C CB  . GLU A 46  ? 0.4296 0.3686 2.2466 -0.1611 0.0527  0.0047  46  GLU A CB  
365   C CG  . GLU A 46  ? 0.4281 0.3784 2.2816 -0.1641 0.0442  -0.0050 46  GLU A CG  
366   C CD  . GLU A 46  ? 0.4234 0.4011 2.3161 -0.1705 0.0529  -0.0149 46  GLU A CD  
367   O OE1 . GLU A 46  ? 0.4325 0.4208 2.3256 -0.1744 0.0686  -0.0148 46  GLU A OE1 
368   O OE2 . GLU A 46  ? 0.4154 0.4036 2.3391 -0.1712 0.0432  -0.0234 46  GLU A OE2 
369   N N   . LEU A 47  ? 0.4430 0.3288 2.1770 -0.1786 0.0811  0.0318  47  LEU A N   
370   C CA  . LEU A 47  ? 0.4569 0.3319 2.1560 -0.1764 0.0875  0.0403  47  LEU A CA  
371   C C   . LEU A 47  ? 0.4674 0.3630 2.1742 -0.1790 0.1013  0.0355  47  LEU A C   
372   O O   . LEU A 47  ? 0.4822 0.3821 2.1733 -0.1696 0.0989  0.0368  47  LEU A O   
373   C CB  . LEU A 47  ? 0.4856 0.3311 2.1555 -0.1869 0.0949  0.0511  47  LEU A CB  
374   C CG  . LEU A 47  ? 0.5031 0.3240 2.1617 -0.1844 0.0818  0.0565  47  LEU A CG  
375   C CD1 . LEU A 47  ? 0.5380 0.3268 2.1609 -0.1923 0.0880  0.0688  47  LEU A CD1 
376   C CD2 . LEU A 47  ? 0.4901 0.3113 2.1418 -0.1662 0.0629  0.0561  47  LEU A CD2 
377   N N   . GLU A 48  ? 0.4993 0.4080 2.2313 -0.1916 0.1162  0.0295  48  GLU A N   
378   C CA  . GLU A 48  ? 0.5156 0.4386 2.2495 -0.1962 0.1330  0.0260  48  GLU A CA  
379   C C   . GLU A 48  ? 0.4861 0.4313 2.2324 -0.1824 0.1254  0.0188  48  GLU A C   
380   O O   . GLU A 48  ? 0.4938 0.4414 2.2222 -0.1792 0.1316  0.0199  48  GLU A O   
381   C CB  . GLU A 48  ? 0.5478 0.4837 2.3139 -0.2116 0.1496  0.0191  48  GLU A CB  
382   C CG  . GLU A 48  ? 0.5828 0.5235 2.3417 -0.2216 0.1726  0.0182  48  GLU A CG  
383   C CD  . GLU A 48  ? 0.6205 0.5747 2.4155 -0.2375 0.1893  0.0108  48  GLU A CD  
384   O OE1 . GLU A 48  ? 0.6169 0.5993 2.4464 -0.2355 0.1944  -0.0006 48  GLU A OE1 
385   O OE2 . GLU A 48  ? 0.6289 0.5670 2.4208 -0.2512 0.1965  0.0156  48  GLU A OE2 
386   N N   . LEU A 49  ? 0.4606 0.4200 2.2357 -0.1745 0.1114  0.0115  49  LEU A N   
387   C CA  . LEU A 49  ? 0.4344 0.4120 2.2205 -0.1610 0.1021  0.0052  49  LEU A CA  
388   C C   . LEU A 49  ? 0.4296 0.3941 2.1840 -0.1482 0.0887  0.0123  49  LEU A C   
389   O O   . LEU A 49  ? 0.4205 0.3944 2.1701 -0.1392 0.0862  0.0102  49  LEU A O   
390   C CB  . LEU A 49  ? 0.4115 0.4059 2.2360 -0.1570 0.0908  -0.0044 49  LEU A CB  
391   C CG  . LEU A 49  ? 0.4043 0.4182 2.2694 -0.1673 0.1014  -0.0140 49  LEU A CG  
392   C CD1 . LEU A 49  ? 0.3767 0.4069 2.2747 -0.1587 0.0853  -0.0232 49  LEU A CD1 
393   C CD2 . LEU A 49  ? 0.4018 0.4301 2.2735 -0.1726 0.1206  -0.0182 49  LEU A CD2 
394   N N   . MET A 50  ? 0.4473 0.3903 2.1813 -0.1470 0.0799  0.0201  50  MET A N   
395   C CA  . MET A 50  ? 0.4671 0.3994 2.1742 -0.1347 0.0679  0.0261  50  MET A CA  
396   C C   . MET A 50  ? 0.4723 0.3983 2.1500 -0.1351 0.0761  0.0321  50  MET A C   
397   O O   . MET A 50  ? 0.4630 0.3930 2.1297 -0.1246 0.0691  0.0325  50  MET A O   
398   C CB  . MET A 50  ? 0.4841 0.3949 2.1770 -0.1321 0.0565  0.0323  50  MET A CB  
399   C CG  . MET A 50  ? 0.4787 0.3945 2.1906 -0.1241 0.0417  0.0266  50  MET A CG  
400   S SD  . MET A 50  ? 0.5153 0.4046 2.2104 -0.1211 0.0295  0.0327  50  MET A SD  
401   C CE  . MET A 50  ? 0.4982 0.3836 2.1667 -0.1057 0.0207  0.0378  50  MET A CE  
402   N N   . LYS A 51  ? 0.4765 0.3930 2.1416 -0.1474 0.0910  0.0361  51  LYS A N   
403   C CA  . LYS A 51  ? 0.4729 0.3819 2.1080 -0.1487 0.0991  0.0414  51  LYS A CA  
404   C C   . LYS A 51  ? 0.4309 0.3621 2.0779 -0.1445 0.1040  0.0333  51  LYS A C   
405   O O   . LYS A 51  ? 0.4297 0.3589 2.0550 -0.1389 0.1022  0.0358  51  LYS A O   
406   C CB  . LYS A 51  ? 0.5133 0.4084 2.1328 -0.1640 0.1164  0.0461  51  LYS A CB  
407   C CG  . LYS A 51  ? 0.5680 0.4371 2.1714 -0.1703 0.1141  0.0551  51  LYS A CG  
408   C CD  . LYS A 51  ? 0.6147 0.4720 2.2125 -0.1879 0.1326  0.0581  51  LYS A CD  
409   C CE  . LYS A 51  ? 0.6494 0.4826 2.2388 -0.1938 0.1283  0.0654  51  LYS A CE  
410   N NZ  . LYS A 51  ? 0.6856 0.5089 2.2757 -0.2120 0.1464  0.0672  51  LYS A NZ  
411   N N   . PHE A 52  ? 0.3931 0.3450 2.0754 -0.1474 0.1097  0.0234  52  PHE A N   
412   C CA  . PHE A 52  ? 0.3652 0.3377 2.0621 -0.1433 0.1145  0.0149  52  PHE A CA  
413   C C   . PHE A 52  ? 0.3316 0.3110 2.0302 -0.1284 0.0977  0.0133  52  PHE A C   
414   O O   . PHE A 52  ? 0.3187 0.3020 2.0049 -0.1228 0.0976  0.0125  52  PHE A O   
415   C CB  . PHE A 52  ? 0.3509 0.3430 2.0870 -0.1502 0.1246  0.0047  52  PHE A CB  
416   C CG  . PHE A 52  ? 0.3284 0.3435 2.0876 -0.1438 0.1263  -0.0056 52  PHE A CG  
417   C CD1 . PHE A 52  ? 0.3328 0.3526 2.0822 -0.1463 0.1402  -0.0084 52  PHE A CD1 
418   C CD2 . PHE A 52  ? 0.3027 0.3329 2.0922 -0.1353 0.1137  -0.0127 52  PHE A CD2 
419   C CE1 . PHE A 52  ? 0.3096 0.3490 2.0809 -0.1402 0.1418  -0.0183 52  PHE A CE1 
420   C CE2 . PHE A 52  ? 0.2869 0.3359 2.0972 -0.1291 0.1146  -0.0219 52  PHE A CE2 
421   C CZ  . PHE A 52  ? 0.2878 0.3417 2.0899 -0.1314 0.1288  -0.0248 52  PHE A CZ  
422   N N   . ASP A 53  ? 0.3086 0.2879 2.0210 -0.1228 0.0840  0.0126  53  ASP A N   
423   C CA  . ASP A 53  ? 0.2892 0.2753 2.0061 -0.1097 0.0692  0.0102  53  ASP A CA  
424   C C   . ASP A 53  ? 0.2905 0.2644 1.9762 -0.1021 0.0616  0.0177  53  ASP A C   
425   O O   . ASP A 53  ? 0.2689 0.2507 1.9516 -0.0944 0.0577  0.0155  53  ASP A O   
426   C CB  . ASP A 53  ? 0.2813 0.2662 2.0148 -0.1063 0.0568  0.0084  53  ASP A CB  
427   C CG  . ASP A 53  ? 0.2691 0.2686 2.0384 -0.1113 0.0594  -0.0003 53  ASP A CG  
428   O OD1 . ASP A 53  ? 0.2423 0.2590 2.0301 -0.1106 0.0650  -0.0076 53  ASP A OD1 
429   O OD2 . ASP A 53  ? 0.2799 0.2730 2.0586 -0.1152 0.0549  -0.0001 53  ASP A OD2 
430   N N   . LEU A 54  ? 0.3072 0.2619 1.9718 -0.1044 0.0591  0.0261  54  LEU A N   
431   C CA  . LEU A 54  ? 0.3130 0.2550 1.9497 -0.0976 0.0512  0.0336  54  LEU A CA  
432   C C   . LEU A 54  ? 0.3290 0.2734 1.9481 -0.0982 0.0579  0.0346  54  LEU A C   
433   O O   . LEU A 54  ? 0.3251 0.2720 1.9347 -0.0898 0.0504  0.0353  54  LEU A O   
434   C CB  . LEU A 54  ? 0.3274 0.2469 1.9450 -0.1016 0.0494  0.0424  54  LEU A CB  
435   C CG  . LEU A 54  ? 0.3160 0.2287 1.9451 -0.0991 0.0401  0.0422  54  LEU A CG  
436   C CD1 . LEU A 54  ? 0.3436 0.2320 1.9498 -0.1022 0.0384  0.0514  54  LEU A CD1 
437   C CD2 . LEU A 54  ? 0.2923 0.2116 1.9284 -0.0864 0.0267  0.0392  54  LEU A CD2 
438   N N   . GLU A 55  ? 0.3687 0.3115 1.9828 -0.1087 0.0722  0.0344  55  GLU A N   
439   C CA  . GLU A 55  ? 0.4042 0.3480 2.0002 -0.1103 0.0797  0.0344  55  GLU A CA  
440   C C   . GLU A 55  ? 0.3733 0.3373 1.9874 -0.1039 0.0787  0.0256  55  GLU A C   
441   O O   . GLU A 55  ? 0.3872 0.3524 1.9868 -0.0986 0.0751  0.0259  55  GLU A O   
442   C CB  . GLU A 55  ? 0.4817 0.4187 2.0706 -0.1238 0.0968  0.0353  55  GLU A CB  
443   C CG  . GLU A 55  ? 0.5416 0.4759 2.1072 -0.1276 0.1069  0.0354  55  GLU A CG  
444   C CD  . GLU A 55  ? 0.6116 0.5283 2.1405 -0.1236 0.0981  0.0442  55  GLU A CD  
445   O OE1 . GLU A 55  ? 0.6460 0.5437 2.1569 -0.1237 0.0910  0.0534  55  GLU A OE1 
446   O OE2 . GLU A 55  ? 0.6649 0.5877 2.1846 -0.1203 0.0985  0.0411  55  GLU A OE2 
447   N N   . ASN A 56  ? 0.3333 0.3127 1.9793 -0.1038 0.0806  0.0175  56  ASN A N   
448   C CA  . ASN A 56  ? 0.3074 0.3034 1.9697 -0.0967 0.0780  0.0097  56  ASN A CA  
449   C C   . ASN A 56  ? 0.2814 0.2756 1.9353 -0.0856 0.0627  0.0125  56  ASN A C   
450   O O   . ASN A 56  ? 0.2596 0.2582 1.9059 -0.0809 0.0609  0.0109  56  ASN A O   
451   C CB  . ASN A 56  ? 0.2937 0.3054 1.9918 -0.0970 0.0796  0.0009  56  ASN A CB  
452   C CG  . ASN A 56  ? 0.3112 0.3292 2.0224 -0.1076 0.0964  -0.0039 56  ASN A CG  
453   O OD1 . ASN A 56  ? 0.3387 0.3540 2.0338 -0.1130 0.1085  -0.0036 56  ASN A OD1 
454   N ND2 . ASN A 56  ? 0.2974 0.3235 2.0374 -0.1112 0.0976  -0.0084 56  ASN A ND2 
455   N N   . ILE A 57  ? 0.2696 0.2571 1.9254 -0.0818 0.0525  0.0162  57  ILE A N   
456   C CA  . ILE A 57  ? 0.2548 0.2415 1.9064 -0.0716 0.0394  0.0179  57  ILE A CA  
457   C C   . ILE A 57  ? 0.2806 0.2595 1.9058 -0.0692 0.0370  0.0238  57  ILE A C   
458   O O   . ILE A 57  ? 0.2636 0.2471 1.8863 -0.0618 0.0300  0.0230  57  ILE A O   
459   C CB  . ILE A 57  ? 0.2426 0.2219 1.8999 -0.0689 0.0306  0.0202  57  ILE A CB  
460   C CG1 . ILE A 57  ? 0.2214 0.2106 1.9059 -0.0689 0.0291  0.0130  57  ILE A CG1 
461   C CG2 . ILE A 57  ? 0.2359 0.2105 1.8822 -0.0592 0.0190  0.0236  57  ILE A CG2 
462   C CD1 . ILE A 57  ? 0.2235 0.2042 1.9134 -0.0677 0.0209  0.0143  57  ILE A CD1 
463   N N   . LYS A 58  ? 0.3253 0.2922 1.9308 -0.0758 0.0428  0.0294  58  LYS A N   
464   C CA  . LYS A 58  ? 0.3699 0.3293 1.9498 -0.0740 0.0400  0.0345  58  LYS A CA  
465   C C   . LYS A 58  ? 0.3835 0.3540 1.9632 -0.0740 0.0449  0.0289  58  LYS A C   
466   O O   . LYS A 58  ? 0.3716 0.3486 1.9527 -0.0670 0.0375  0.0272  58  LYS A O   
467   C CB  . LYS A 58  ? 0.4164 0.3574 1.9722 -0.0809 0.0439  0.0423  58  LYS A CB  
468   C CG  . LYS A 58  ? 0.4399 0.3668 1.9896 -0.0776 0.0346  0.0493  58  LYS A CG  
469   C CD  . LYS A 58  ? 0.4836 0.3909 2.0159 -0.0862 0.0401  0.0563  58  LYS A CD  
470   C CE  . LYS A 58  ? 0.5213 0.4155 2.0221 -0.0892 0.0418  0.0623  58  LYS A CE  
471   N NZ  . LYS A 58  ? 0.5511 0.4260 2.0348 -0.0995 0.0501  0.0686  58  LYS A NZ  
472   N N   . GLU A 59  ? 0.4509 0.4242 2.0315 -0.0818 0.0579  0.0250  59  GLU A N   
473   C CA  . GLU A 59  ? 0.4433 0.4263 2.0246 -0.0820 0.0637  0.0185  59  GLU A CA  
474   C C   . GLU A 59  ? 0.3997 0.3971 2.0030 -0.0740 0.0572  0.0121  59  GLU A C   
475   O O   . GLU A 59  ? 0.3968 0.4004 1.9988 -0.0721 0.0584  0.0075  59  GLU A O   
476   C CB  . GLU A 59  ? 0.4765 0.4632 2.0646 -0.0909 0.0799  0.0132  59  GLU A CB  
477   C CG  . GLU A 59  ? 0.5420 0.5146 2.1010 -0.0997 0.0898  0.0176  59  GLU A CG  
478   C CD  . GLU A 59  ? 0.6326 0.6064 2.2005 -0.1099 0.1069  0.0141  59  GLU A CD  
479   O OE1 . GLU A 59  ? 0.6269 0.6124 2.2085 -0.1125 0.1183  0.0053  59  GLU A OE1 
480   O OE2 . GLU A 59  ? 0.7293 0.6921 2.2919 -0.1156 0.1089  0.0202  59  GLU A OE2 
481   N N   . GLY A 60  ? 0.3756 0.3764 1.9973 -0.0697 0.0504  0.0117  60  GLY A N   
482   C CA  . GLY A 60  ? 0.3572 0.3690 1.9980 -0.0627 0.0444  0.0061  60  GLY A CA  
483   C C   . GLY A 60  ? 0.3379 0.3488 1.9692 -0.0553 0.0339  0.0088  60  GLY A C   
484   O O   . GLY A 60  ? 0.3592 0.3774 2.0009 -0.0502 0.0302  0.0045  60  GLY A O   
485   N N   . GLY A 61  ? 0.3152 0.3165 1.9274 -0.0548 0.0294  0.0158  61  GLY A N   
486   C CA  . GLY A 61  ? 0.2918 0.2928 1.8941 -0.0490 0.0208  0.0183  61  GLY A CA  
487   C C   . GLY A 61  ? 0.2770 0.2736 1.8809 -0.0430 0.0115  0.0227  61  GLY A C   
488   O O   . GLY A 61  ? 0.3058 0.3038 1.9052 -0.0377 0.0046  0.0243  61  GLY A O   
489   N N   . TYR A 62  ? 0.2661 0.2574 1.8765 -0.0443 0.0117  0.0241  62  TYR A N   
490   C CA  . TYR A 62  ? 0.2493 0.2355 1.8624 -0.0386 0.0037  0.0268  62  TYR A CA  
491   C C   . TYR A 62  ? 0.2461 0.2196 1.8422 -0.0387 0.0005  0.0342  62  TYR A C   
492   O O   . TYR A 62  ? 0.2431 0.2108 1.8252 -0.0442 0.0048  0.0373  62  TYR A O   
493   C CB  . TYR A 62  ? 0.2460 0.2331 1.8760 -0.0394 0.0044  0.0233  62  TYR A CB  
494   C CG  . TYR A 62  ? 0.2459 0.2444 1.8921 -0.0392 0.0069  0.0162  62  TYR A CG  
495   C CD1 . TYR A 62  ? 0.2460 0.2492 1.8984 -0.0327 0.0012  0.0132  62  TYR A CD1 
496   C CD2 . TYR A 62  ? 0.2614 0.2654 1.9163 -0.0455 0.0154  0.0122  62  TYR A CD2 
497   C CE1 . TYR A 62  ? 0.2398 0.2511 1.9050 -0.0319 0.0025  0.0073  62  TYR A CE1 
498   C CE2 . TYR A 62  ? 0.2550 0.2689 1.9257 -0.0442 0.0169  0.0054  62  TYR A CE2 
499   C CZ  . TYR A 62  ? 0.2424 0.2593 1.9178 -0.0373 0.0098  0.0032  62  TYR A CZ  
500   O OH  . TYR A 62  ? 0.2212 0.2457 1.9114 -0.0358 0.0105  -0.0031 62  TYR A OH  
501   N N   . ASN A 63  ? 0.2363 0.2051 1.8325 -0.0321 -0.0074 0.0366  63  ASN A N   
502   C CA  . ASN A 63  ? 0.2550 0.2108 1.8372 -0.0302 -0.0123 0.0433  63  ASN A CA  
503   C C   . ASN A 63  ? 0.2802 0.2265 1.8676 -0.0277 -0.0159 0.0444  63  ASN A C   
504   O O   . ASN A 63  ? 0.2881 0.2212 1.8650 -0.0259 -0.0202 0.0498  63  ASN A O   
505   C CB  . ASN A 63  ? 0.2443 0.2033 1.8200 -0.0234 -0.0194 0.0452  63  ASN A CB  
506   C CG  . ASN A 63  ? 0.2194 0.1857 1.8069 -0.0150 -0.0245 0.0421  63  ASN A CG  
507   O OD1 . ASN A 63  ? 0.2092 0.1741 1.8060 -0.0130 -0.0247 0.0396  63  ASN A OD1 
508   N ND2 . ASN A 63  ? 0.2110 0.1849 1.7978 -0.0105 -0.0285 0.0418  63  ASN A ND2 
509   N N   . THR A 64  ? 0.2972 0.2489 1.8999 -0.0275 -0.0148 0.0391  64  THR A N   
510   C CA  . THR A 64  ? 0.3189 0.2619 1.9268 -0.0252 -0.0188 0.0387  64  THR A CA  
511   C C   . THR A 64  ? 0.3134 0.2603 1.9364 -0.0301 -0.0155 0.0335  64  THR A C   
512   O O   . THR A 64  ? 0.2916 0.2505 1.9241 -0.0321 -0.0118 0.0290  64  THR A O   
513   C CB  . THR A 64  ? 0.3182 0.2636 1.9276 -0.0153 -0.0253 0.0372  64  THR A CB  
514   O OG1 . THR A 64  ? 0.3482 0.2910 1.9463 -0.0118 -0.0282 0.0419  64  THR A OG1 
515   C CG2 . THR A 64  ? 0.3165 0.2514 1.9280 -0.0113 -0.0301 0.0363  64  THR A CG2 
516   N N   . ILE A 65  ? 0.3234 0.2598 1.9495 -0.0319 -0.0177 0.0338  65  ILE A N   
517   C CA  . ILE A 65  ? 0.3219 0.2619 1.9643 -0.0350 -0.0176 0.0281  65  ILE A CA  
518   C C   . ILE A 65  ? 0.3121 0.2451 1.9560 -0.0283 -0.0260 0.0258  65  ILE A C   
519   O O   . ILE A 65  ? 0.3244 0.2464 1.9573 -0.0235 -0.0299 0.0292  65  ILE A O   
520   C CB  . ILE A 65  ? 0.3395 0.2749 1.9872 -0.0454 -0.0116 0.0289  65  ILE A CB  
521   C CG1 . ILE A 65  ? 0.3640 0.2814 1.9983 -0.0475 -0.0127 0.0353  65  ILE A CG1 
522   C CG2 . ILE A 65  ? 0.3576 0.3025 2.0060 -0.0520 -0.0018 0.0289  65  ILE A CG2 
523   C CD1 . ILE A 65  ? 0.3738 0.2843 2.0155 -0.0580 -0.0079 0.0353  65  ILE A CD1 
524   N N   . ARG A 66  ? 0.2891 0.2282 1.9455 -0.0274 -0.0289 0.0197  66  ARG A N   
525   C CA  . ARG A 66  ? 0.2852 0.2171 1.9413 -0.0215 -0.0367 0.0164  66  ARG A CA  
526   C C   . ARG A 66  ? 0.2734 0.2023 1.9429 -0.0271 -0.0395 0.0123  66  ARG A C   
527   O O   . ARG A 66  ? 0.2726 0.2124 1.9569 -0.0320 -0.0368 0.0089  66  ARG A O   
528   C CB  . ARG A 66  ? 0.2794 0.2197 1.9357 -0.0150 -0.0391 0.0129  66  ARG A CB  
529   C CG  . ARG A 66  ? 0.2988 0.2314 1.9517 -0.0088 -0.0465 0.0091  66  ARG A CG  
530   C CD  . ARG A 66  ? 0.3123 0.2456 1.9774 -0.0113 -0.0518 0.0034  66  ARG A CD  
531   N NE  . ARG A 66  ? 0.3264 0.2537 1.9851 -0.0049 -0.0589 -0.0004 66  ARG A NE  
532   C CZ  . ARG A 66  ? 0.3765 0.2908 2.0301 -0.0027 -0.0663 -0.0034 66  ARG A CZ  
533   N NH1 . ARG A 66  ? 0.3771 0.2802 2.0283 -0.0046 -0.0679 -0.0026 66  ARG A NH1 
534   N NH2 . ARG A 66  ? 0.3932 0.3040 2.0417 0.0017  -0.0723 -0.0072 66  ARG A NH2 
535   N N   . THR A 67  ? 0.2599 0.1745 1.9257 -0.0262 -0.0451 0.0119  67  THR A N   
536   C CA  . THR A 67  ? 0.2531 0.1641 1.9323 -0.0325 -0.0485 0.0078  67  THR A CA  
537   C C   . THR A 67  ? 0.2468 0.1481 1.9229 -0.0268 -0.0587 0.0030  67  THR A C   
538   O O   . THR A 67  ? 0.2411 0.1378 1.9036 -0.0182 -0.0616 0.0031  67  THR A O   
539   C CB  . THR A 67  ? 0.2634 0.1639 1.9415 -0.0404 -0.0445 0.0120  67  THR A CB  
540   O OG1 . THR A 67  ? 0.2898 0.1743 1.9509 -0.0344 -0.0485 0.0153  67  THR A OG1 
541   C CG2 . THR A 67  ? 0.2644 0.1705 1.9396 -0.0461 -0.0343 0.0174  67  THR A CG2 
542   N N   . TRP A 68  ? 0.2402 0.1394 1.9300 -0.0320 -0.0638 -0.0018 68  TRP A N   
543   C CA  . TRP A 68  ? 0.2494 0.1391 1.9368 -0.0278 -0.0747 -0.0074 68  TRP A CA  
544   C C   . TRP A 68  ? 0.2729 0.1467 1.9604 -0.0325 -0.0788 -0.0083 68  TRP A C   
545   O O   . TRP A 68  ? 0.2943 0.1554 1.9749 -0.0288 -0.0878 -0.0124 68  TRP A O   
546   C CB  . TRP A 68  ? 0.2436 0.1450 1.9480 -0.0288 -0.0803 -0.0136 68  TRP A CB  
547   C CG  . TRP A 68  ? 0.2364 0.1492 1.9378 -0.0228 -0.0785 -0.0135 68  TRP A CG  
548   C CD1 . TRP A 68  ? 0.2377 0.1461 1.9266 -0.0147 -0.0848 -0.0156 68  TRP A CD1 
549   C CD2 . TRP A 68  ? 0.2308 0.1593 1.9398 -0.0249 -0.0694 -0.0110 68  TRP A CD2 
550   N NE1 . TRP A 68  ? 0.2284 0.1483 1.9172 -0.0119 -0.0803 -0.0142 68  TRP A NE1 
551   C CE2 . TRP A 68  ? 0.2232 0.1558 1.9248 -0.0178 -0.0713 -0.0118 68  TRP A CE2 
552   C CE3 . TRP A 68  ? 0.2370 0.1750 1.9568 -0.0324 -0.0595 -0.0084 68  TRP A CE3 
553   C CZ2 . TRP A 68  ? 0.2163 0.1624 1.9225 -0.0179 -0.0644 -0.0105 68  TRP A CZ2 
554   C CZ3 . TRP A 68  ? 0.2262 0.1777 1.9493 -0.0322 -0.0524 -0.0074 68  TRP A CZ3 
555   C CH2 . TRP A 68  ? 0.2106 0.1661 1.9275 -0.0248 -0.0552 -0.0085 68  TRP A CH2 
556   N N   . SER A 69  ? 0.2705 0.1439 1.9643 -0.0410 -0.0715 -0.0042 69  SER A N   
557   C CA  . SER A 69  ? 0.2765 0.1370 1.9755 -0.0489 -0.0734 -0.0047 69  SER A CA  
558   C C   . SER A 69  ? 0.2835 0.1348 1.9707 -0.0520 -0.0648 0.0035  69  SER A C   
559   O O   . SER A 69  ? 0.2690 0.1304 1.9542 -0.0528 -0.0563 0.0083  69  SER A O   
560   C CB  . SER A 69  ? 0.2739 0.1470 1.9993 -0.0589 -0.0728 -0.0093 69  SER A CB  
561   O OG  . SER A 69  ? 0.2883 0.1509 2.0218 -0.0691 -0.0724 -0.0095 69  SER A OG  
562   N N   . GLN A 70  ? 0.3025 0.1334 1.9810 -0.0535 -0.0680 0.0050  70  GLN A N   
563   C CA  . GLN A 70  ? 0.3178 0.1351 1.9803 -0.0537 -0.0627 0.0132  70  GLN A CA  
564   C C   . GLN A 70  ? 0.3244 0.1437 1.9952 -0.0668 -0.0532 0.0176  70  GLN A C   
565   O O   . GLN A 70  ? 0.3238 0.1453 2.0119 -0.0765 -0.0529 0.0137  70  GLN A O   
566   C CB  . GLN A 70  ? 0.3417 0.1346 1.9920 -0.0503 -0.0697 0.0127  70  GLN A CB  
567   C CG  . GLN A 70  ? 0.3547 0.1384 2.0172 -0.0586 -0.0756 0.0069  70  GLN A CG  
568   C CD  . GLN A 70  ? 0.3567 0.1395 2.0205 -0.0521 -0.0864 -0.0020 70  GLN A CD  
569   O OE1 . GLN A 70  ? 0.3443 0.1428 2.0120 -0.0468 -0.0884 -0.0056 70  GLN A OE1 
570   N NE2 . GLN A 70  ? 0.3790 0.1418 2.0379 -0.0527 -0.0939 -0.0057 70  GLN A NE2 
571   N N   . TYR A 71  ? 0.3380 0.1564 1.9965 -0.0673 -0.0454 0.0255  71  TYR A N   
572   C CA  . TYR A 71  ? 0.3643 0.1816 2.0253 -0.0798 -0.0350 0.0304  71  TYR A CA  
573   C C   . TYR A 71  ? 0.4096 0.2006 2.0597 -0.0855 -0.0357 0.0353  71  TYR A C   
574   O O   . TYR A 71  ? 0.4333 0.2069 2.0688 -0.0772 -0.0432 0.0370  71  TYR A O   
575   C CB  . TYR A 71  ? 0.3711 0.1967 2.0200 -0.0774 -0.0275 0.0365  71  TYR A CB  
576   C CG  . TYR A 71  ? 0.3615 0.2129 2.0244 -0.0774 -0.0226 0.0321  71  TYR A CG  
577   C CD1 . TYR A 71  ? 0.3603 0.2257 2.0477 -0.0850 -0.0200 0.0253  71  TYR A CD1 
578   C CD2 . TYR A 71  ? 0.3417 0.2030 1.9947 -0.0700 -0.0209 0.0345  71  TYR A CD2 
579   C CE1 . TYR A 71  ? 0.3512 0.2387 2.0522 -0.0842 -0.0162 0.0209  71  TYR A CE1 
580   C CE2 . TYR A 71  ? 0.3344 0.2170 1.9996 -0.0704 -0.0163 0.0303  71  TYR A CE2 
581   C CZ  . TYR A 71  ? 0.3461 0.2414 2.0352 -0.0771 -0.0140 0.0235  71  TYR A CZ  
582   O OH  . TYR A 71  ? 0.3398 0.2557 2.0449 -0.0776 -0.0101 0.0182  71  TYR A OH  
583   N N   . SER A 72  ? 0.4234 0.2107 2.0810 -0.0999 -0.0273 0.0374  72  SER A N   
584   C CA  . SER A 72  ? 0.4403 0.2008 2.0851 -0.1071 -0.0260 0.0436  72  SER A CA  
585   C C   . SER A 72  ? 0.4503 0.1974 2.0679 -0.1033 -0.0225 0.0542  72  SER A C   
586   O O   . SER A 72  ? 0.4380 0.1991 2.0499 -0.0976 -0.0196 0.0561  72  SER A O   
587   C CB  . SER A 72  ? 0.4469 0.2088 2.1073 -0.1243 -0.0163 0.0430  72  SER A CB  
588   O OG  . SER A 72  ? 0.4438 0.2140 2.0986 -0.1305 -0.0033 0.0484  72  SER A OG  
589   N N   . GLU A 73  ? 0.4796 0.1989 2.0804 -0.1075 -0.0226 0.0613  73  GLU A N   
590   C CA  . GLU A 73  ? 0.5004 0.2044 2.0746 -0.1055 -0.0197 0.0721  73  GLU A CA  
591   C C   . GLU A 73  ? 0.5052 0.2207 2.0775 -0.1158 -0.0062 0.0759  73  GLU A C   
592   O O   . GLU A 73  ? 0.5125 0.2297 2.0676 -0.1102 -0.0050 0.0814  73  GLU A O   
593   C CB  . GLU A 73  ? 0.5376 0.2070 2.0926 -0.1089 -0.0223 0.0797  73  GLU A CB  
594   C CG  . GLU A 73  ? 0.5601 0.2148 2.0866 -0.1053 -0.0210 0.0909  73  GLU A CG  
595   C CD  . GLU A 73  ? 0.5950 0.2162 2.0988 -0.0996 -0.0293 0.0984  73  GLU A CD  
596   O OE1 . GLU A 73  ? 0.6217 0.2246 2.1287 -0.1019 -0.0337 0.0965  73  GLU A OE1 
597   O OE2 . GLU A 73  ? 0.6002 0.2138 2.0830 -0.0923 -0.0320 0.1061  73  GLU A OE2 
598   N N   . ASN A 74  ? 0.5070 0.2304 2.0970 -0.1306 0.0039  0.0725  74  ASN A N   
599   C CA  . ASN A 74  ? 0.5101 0.2410 2.0969 -0.1418 0.0188  0.0760  74  ASN A CA  
600   C C   . ASN A 74  ? 0.4848 0.2443 2.0798 -0.1348 0.0208  0.0713  74  ASN A C   
601   O O   . ASN A 74  ? 0.4915 0.2534 2.0719 -0.1371 0.0292  0.0760  74  ASN A O   
602   C CB  . ASN A 74  ? 0.5133 0.2511 2.1228 -0.1590 0.0306  0.0716  74  ASN A CB  
603   C CG  . ASN A 74  ? 0.5432 0.2531 2.1465 -0.1701 0.0319  0.0761  74  ASN A CG  
604   O OD1 . ASN A 74  ? 0.5720 0.2550 2.1457 -0.1724 0.0339  0.0867  74  ASN A OD1 
605   N ND2 . ASN A 74  ? 0.5368 0.2521 2.1673 -0.1773 0.0303  0.0683  74  ASN A ND2 
606   N N   . GLN A 75  ? 0.4612 0.2404 2.0787 -0.1270 0.0133  0.0619  75  GLN A N   
607   C CA  . GLN A 75  ? 0.4371 0.2423 2.0639 -0.1194 0.0134  0.0568  75  GLN A CA  
608   C C   . GLN A 75  ? 0.4398 0.2416 2.0437 -0.1060 0.0069  0.0620  75  GLN A C   
609   O O   . GLN A 75  ? 0.4199 0.2357 2.0200 -0.1039 0.0116  0.0622  75  GLN A O   
610   C CB  . GLN A 75  ? 0.4094 0.2313 2.0633 -0.1149 0.0055  0.0463  75  GLN A CB  
611   C CG  . GLN A 75  ? 0.4046 0.2392 2.0872 -0.1274 0.0124  0.0393  75  GLN A CG  
612   C CD  . GLN A 75  ? 0.3894 0.2388 2.0958 -0.1213 0.0018  0.0293  75  GLN A CD  
613   O OE1 . GLN A 75  ? 0.4094 0.2474 2.1098 -0.1134 -0.0102 0.0283  75  GLN A OE1 
614   N NE2 . GLN A 75  ? 0.3630 0.2363 2.0946 -0.1238 0.0056  0.0218  75  GLN A NE2 
615   N N   . LEU A 76  ? 0.4540 0.2378 2.0445 -0.0971 -0.0039 0.0653  76  LEU A N   
616   C CA  . LEU A 76  ? 0.4566 0.2375 2.0291 -0.0840 -0.0110 0.0695  76  LEU A CA  
617   C C   . LEU A 76  ? 0.4825 0.2549 2.0325 -0.0883 -0.0045 0.0783  76  LEU A C   
618   O O   . LEU A 76  ? 0.4761 0.2592 2.0186 -0.0820 -0.0051 0.0793  76  LEU A O   
619   C CB  . LEU A 76  ? 0.4666 0.2275 2.0294 -0.0747 -0.0223 0.0716  76  LEU A CB  
620   C CG  . LEU A 76  ? 0.4472 0.2166 2.0251 -0.0653 -0.0309 0.0630  76  LEU A CG  
621   C CD1 . LEU A 76  ? 0.4609 0.2094 2.0281 -0.0560 -0.0407 0.0645  76  LEU A CD1 
622   C CD2 . LEU A 76  ? 0.4183 0.2115 2.0022 -0.0566 -0.0318 0.0589  76  LEU A CD2 
623   N N   . LYS A 77  ? 0.5191 0.2714 2.0581 -0.0999 0.0018  0.0843  77  LYS A N   
624   C CA  . LYS A 77  ? 0.5519 0.2887 2.0636 -0.1046 0.0071  0.0940  77  LYS A CA  
625   C C   . LYS A 77  ? 0.5299 0.2877 2.0434 -0.1081 0.0166  0.0916  77  LYS A C   
626   O O   . LYS A 77  ? 0.5368 0.2909 2.0291 -0.1043 0.0156  0.0970  77  LYS A O   
627   C CB  . LYS A 77  ? 0.5898 0.3015 2.0899 -0.1190 0.0149  0.1004  77  LYS A CB  
628   C CG  . LYS A 77  ? 0.6150 0.2962 2.1006 -0.1155 0.0053  0.1066  77  LYS A CG  
629   C CD  . LYS A 77  ? 0.6599 0.3175 2.1375 -0.1319 0.0145  0.1120  77  LYS A CD  
630   C CE  . LYS A 77  ? 0.6876 0.3132 2.1527 -0.1300 0.0057  0.1174  77  LYS A CE  
631   N NZ  . LYS A 77  ? 0.7145 0.3223 2.1796 -0.1477 0.0159  0.1202  77  LYS A NZ  
632   N N   . LEU A 78  ? 0.5070 0.2865 2.0465 -0.1145 0.0247  0.0831  78  LEU A N   
633   C CA  . LEU A 78  ? 0.4988 0.2979 2.0429 -0.1189 0.0354  0.0796  78  LEU A CA  
634   C C   . LEU A 78  ? 0.4731 0.2902 2.0193 -0.1057 0.0277  0.0760  78  LEU A C   
635   O O   . LEU A 78  ? 0.4490 0.2752 1.9870 -0.1062 0.0332  0.0761  78  LEU A O   
636   C CB  . LEU A 78  ? 0.4920 0.3086 2.0671 -0.1283 0.0445  0.0709  78  LEU A CB  
637   C CG  . LEU A 78  ? 0.5016 0.3391 2.0859 -0.1336 0.0571  0.0658  78  LEU A CG  
638   C CD1 . LEU A 78  ? 0.5415 0.3649 2.0993 -0.1437 0.0699  0.0730  78  LEU A CD1 
639   C CD2 . LEU A 78  ? 0.4985 0.3545 2.1182 -0.1410 0.0638  0.0563  78  LEU A CD2 
640   N N   . VAL A 79  ? 0.4585 0.2807 2.0168 -0.0948 0.0159  0.0721  79  VAL A N   
641   C CA  . VAL A 79  ? 0.4550 0.2911 2.0142 -0.0821 0.0081  0.0694  79  VAL A CA  
642   C C   . VAL A 79  ? 0.4563 0.2782 1.9885 -0.0761 0.0024  0.0778  79  VAL A C   
643   O O   . VAL A 79  ? 0.4323 0.2611 1.9542 -0.0756 0.0050  0.0790  79  VAL A O   
644   C CB  . VAL A 79  ? 0.4488 0.2912 2.0249 -0.0727 -0.0019 0.0635  79  VAL A CB  
645   C CG1 . VAL A 79  ? 0.4141 0.2678 1.9884 -0.0598 -0.0095 0.0617  79  VAL A CG1 
646   C CG2 . VAL A 79  ? 0.4283 0.2853 2.0309 -0.0785 0.0022  0.0549  79  VAL A CG2 
647   N N   . GLN A 80  ? 0.4765 0.2776 1.9976 -0.0720 -0.0057 0.0832  80  GLN A N   
648   C CA  . GLN A 80  ? 0.4880 0.2733 1.9848 -0.0653 -0.0132 0.0913  80  GLN A CA  
649   C C   . GLN A 80  ? 0.5046 0.2871 1.9812 -0.0721 -0.0063 0.0963  80  GLN A C   
650   O O   . GLN A 80  ? 0.5206 0.3065 1.9857 -0.0651 -0.0121 0.0984  80  GLN A O   
651   C CB  . GLN A 80  ? 0.5269 0.2838 2.0113 -0.0668 -0.0174 0.0978  80  GLN A CB  
652   C CG  . GLN A 80  ? 0.5506 0.2897 2.0140 -0.0566 -0.0290 0.1053  80  GLN A CG  
653   C CD  . GLN A 80  ? 0.5365 0.2881 2.0129 -0.0412 -0.0397 0.1003  80  GLN A CD  
654   O OE1 . GLN A 80  ? 0.5201 0.2822 2.0166 -0.0381 -0.0403 0.0929  80  GLN A OE1 
655   N NE2 . GLN A 80  ? 0.5395 0.2913 2.0049 -0.0318 -0.0478 0.1038  80  GLN A NE2 
656   N N   . GLU A 81  ? 0.5205 0.2980 1.9937 -0.0861 0.0064  0.0975  81  GLU A N   
657   C CA  . GLU A 81  ? 0.5480 0.3185 1.9978 -0.0939 0.0146  0.1026  81  GLU A CA  
658   C C   . GLU A 81  ? 0.4976 0.2927 1.9552 -0.0925 0.0190  0.0961  81  GLU A C   
659   O O   . GLU A 81  ? 0.4993 0.2905 1.9353 -0.0942 0.0210  0.0996  81  GLU A O   
660   C CB  . GLU A 81  ? 0.6003 0.3594 2.0454 -0.1103 0.0295  0.1048  81  GLU A CB  
661   C CG  . GLU A 81  ? 0.6691 0.3975 2.0982 -0.1147 0.0271  0.1133  81  GLU A CG  
662   C CD  . GLU A 81  ? 0.7436 0.4678 2.1849 -0.1300 0.0407  0.1116  81  GLU A CD  
663   O OE1 . GLU A 81  ? 0.7033 0.4499 2.1658 -0.1370 0.0525  0.1037  81  GLU A OE1 
664   O OE2 . GLU A 81  ? 0.8372 0.5360 2.2685 -0.1351 0.0396  0.1179  81  GLU A OE2 
665   N N   . SER A 82  ? 0.4529 0.2717 1.9400 -0.0897 0.0202  0.0866  82  SER A N   
666   C CA  . SER A 82  ? 0.4343 0.2755 1.9318 -0.0905 0.0267  0.0797  82  SER A CA  
667   C C   . SER A 82  ? 0.4342 0.2817 1.9209 -0.0807 0.0179  0.0803  82  SER A C   
668   O O   . SER A 82  ? 0.4418 0.2990 1.9236 -0.0829 0.0234  0.0777  82  SER A O   
669   C CB  . SER A 82  ? 0.4014 0.2641 1.9323 -0.0892 0.0284  0.0699  82  SER A CB  
670   O OG  . SER A 82  ? 0.3770 0.2437 1.9194 -0.0780 0.0160  0.0678  82  SER A OG  
671   N N   . GLY A 83  ? 0.4294 0.2722 1.9147 -0.0697 0.0045  0.0829  83  GLY A N   
672   C CA  . GLY A 83  ? 0.4145 0.2686 1.8994 -0.0595 -0.0045 0.0813  83  GLY A CA  
673   C C   . GLY A 83  ? 0.3897 0.2611 1.9006 -0.0512 -0.0093 0.0742  83  GLY A C   
674   O O   . GLY A 83  ? 0.4016 0.2812 1.9149 -0.0418 -0.0176 0.0730  83  GLY A O   
675   N N   . LEU A 84  ? 0.3695 0.2460 1.8992 -0.0546 -0.0045 0.0693  84  LEU A N   
676   C CA  . LEU A 84  ? 0.3585 0.2520 1.9101 -0.0479 -0.0080 0.0619  84  LEU A CA  
677   C C   . LEU A 84  ? 0.3752 0.2607 1.9305 -0.0394 -0.0173 0.0627  84  LEU A C   
678   O O   . LEU A 84  ? 0.4055 0.2737 1.9540 -0.0414 -0.0190 0.0670  84  LEU A O   
679   C CB  . LEU A 84  ? 0.3431 0.2489 1.9149 -0.0538 -0.0003 0.0548  84  LEU A CB  
680   C CG  . LEU A 84  ? 0.3345 0.2536 1.9091 -0.0593 0.0088  0.0510  84  LEU A CG  
681   C CD1 . LEU A 84  ? 0.3279 0.2557 1.9232 -0.0660 0.0164  0.0449  84  LEU A CD1 
682   C CD2 . LEU A 84  ? 0.3200 0.2532 1.8984 -0.0513 0.0041  0.0474  84  LEU A CD2 
683   N N   . LYS A 85  ? 0.3813 0.2793 1.9470 -0.0304 -0.0227 0.0582  85  LYS A N   
684   C CA  . LYS A 85  ? 0.3826 0.2760 1.9539 -0.0218 -0.0300 0.0568  85  LYS A CA  
685   C C   . LYS A 85  ? 0.3535 0.2496 1.9401 -0.0244 -0.0281 0.0509  85  LYS A C   
686   O O   . LYS A 85  ? 0.3398 0.2474 1.9369 -0.0299 -0.0226 0.0466  85  LYS A O   
687   C CB  . LYS A 85  ? 0.3708 0.2760 1.9450 -0.0119 -0.0352 0.0547  85  LYS A CB  
688   C CG  . LYS A 85  ? 0.3910 0.2939 1.9522 -0.0084 -0.0395 0.0600  85  LYS A CG  
689   C CD  . LYS A 85  ? 0.4238 0.3058 1.9709 -0.0072 -0.0446 0.0670  85  LYS A CD  
690   C CE  . LYS A 85  ? 0.4454 0.3239 1.9813 -0.0008 -0.0523 0.0718  85  LYS A CE  
691   N NZ  . LYS A 85  ? 0.4581 0.3324 1.9772 -0.0075 -0.0507 0.0767  85  LYS A NZ  
692   N N   . LEU A 86  ? 0.3329 0.2186 1.9211 -0.0196 -0.0336 0.0501  86  LEU A N   
693   C CA  . LEU A 86  ? 0.3216 0.2071 1.9222 -0.0220 -0.0338 0.0446  86  LEU A CA  
694   C C   . LEU A 86  ? 0.3107 0.1975 1.9147 -0.0120 -0.0398 0.0401  86  LEU A C   
695   O O   . LEU A 86  ? 0.3329 0.2110 1.9292 -0.0044 -0.0443 0.0422  86  LEU A O   
696   C CB  . LEU A 86  ? 0.3436 0.2105 1.9397 -0.0282 -0.0337 0.0480  86  LEU A CB  
697   C CG  . LEU A 86  ? 0.3405 0.2072 1.9504 -0.0363 -0.0315 0.0434  86  LEU A CG  
698   C CD1 . LEU A 86  ? 0.3590 0.2053 1.9621 -0.0425 -0.0313 0.0479  86  LEU A CD1 
699   C CD2 . LEU A 86  ? 0.3323 0.2030 1.9527 -0.0306 -0.0374 0.0361  86  LEU A CD2 
700   N N   . ILE A 87  ? 0.2923 0.1892 1.9072 -0.0119 -0.0397 0.0338  87  ILE A N   
701   C CA  . ILE A 87  ? 0.3043 0.1976 1.9207 -0.0050 -0.0448 0.0290  87  ILE A CA  
702   C C   . ILE A 87  ? 0.3460 0.2305 1.9689 -0.0104 -0.0472 0.0256  87  ILE A C   
703   O O   . ILE A 87  ? 0.4138 0.3065 2.0481 -0.0165 -0.0456 0.0224  87  ILE A O   
704   C CB  . ILE A 87  ? 0.2788 0.1868 1.8996 -0.0008 -0.0441 0.0247  87  ILE A CB  
705   C CG1 . ILE A 87  ? 0.2697 0.1860 1.8853 0.0047  -0.0423 0.0275  87  ILE A CG1 
706   C CG2 . ILE A 87  ? 0.2770 0.1794 1.8973 0.0046  -0.0487 0.0193  87  ILE A CG2 
707   C CD1 . ILE A 87  ? 0.2465 0.1776 1.8665 0.0061  -0.0400 0.0243  87  ILE A CD1 
708   N N   . MET A 88  ? 0.3712 0.2388 1.9884 -0.0084 -0.0515 0.0259  88  MET A N   
709   C CA  . MET A 88  ? 0.3786 0.2364 2.0021 -0.0154 -0.0537 0.0236  88  MET A CA  
710   C C   . MET A 88  ? 0.3800 0.2330 2.0048 -0.0107 -0.0605 0.0166  88  MET A C   
711   O O   . MET A 88  ? 0.3934 0.2352 2.0081 -0.0029 -0.0640 0.0156  88  MET A O   
712   C CB  . MET A 88  ? 0.4098 0.2486 2.0251 -0.0182 -0.0543 0.0286  88  MET A CB  
713   C CG  . MET A 88  ? 0.4616 0.2903 2.0849 -0.0271 -0.0561 0.0260  88  MET A CG  
714   S SD  . MET A 88  ? 0.5407 0.3452 2.1541 -0.0330 -0.0554 0.0328  88  MET A SD  
715   C CE  . MET A 88  ? 0.5074 0.3237 2.1216 -0.0421 -0.0451 0.0391  88  MET A CE  
716   N N   . GLY A 89  ? 0.3680 0.2281 2.0050 -0.0156 -0.0625 0.0114  89  GLY A N   
717   C CA  . GLY A 89  ? 0.3654 0.2186 2.0027 -0.0127 -0.0704 0.0047  89  GLY A CA  
718   C C   . GLY A 89  ? 0.3857 0.2218 2.0242 -0.0176 -0.0751 0.0030  89  GLY A C   
719   O O   . GLY A 89  ? 0.4064 0.2409 2.0525 -0.0265 -0.0717 0.0061  89  GLY A O   
720   N N   . ILE A 90  ? 0.3907 0.2131 2.0201 -0.0119 -0.0823 -0.0018 90  ILE A N   
721   C CA  . ILE A 90  ? 0.4060 0.2103 2.0352 -0.0158 -0.0883 -0.0047 90  ILE A CA  
722   C C   . ILE A 90  ? 0.4075 0.2128 2.0442 -0.0177 -0.0972 -0.0127 90  ILE A C   
723   O O   . ILE A 90  ? 0.3981 0.2030 2.0259 -0.0105 -0.1016 -0.0169 90  ILE A O   
724   C CB  . ILE A 90  ? 0.4146 0.1992 2.0258 -0.0075 -0.0902 -0.0044 90  ILE A CB  
725   C CG1 . ILE A 90  ? 0.4076 0.1928 2.0115 -0.0031 -0.0832 0.0032  90  ILE A CG1 
726   C CG2 . ILE A 90  ? 0.4263 0.1899 2.0368 -0.0123 -0.0962 -0.0072 90  ILE A CG2 
727   C CD1 . ILE A 90  ? 0.4211 0.1999 2.0283 -0.0114 -0.0797 0.0098  90  ILE A CD1 
728   N N   . ASP A 91  ? 0.4165 0.2221 2.0697 -0.0278 -0.1001 -0.0150 91  ASP A N   
729   C CA  . ASP A 91  ? 0.4111 0.2207 2.0757 -0.0303 -0.1096 -0.0226 91  ASP A CA  
730   C C   . ASP A 91  ? 0.4295 0.2185 2.0794 -0.0255 -0.1202 -0.0287 91  ASP A C   
731   O O   . ASP A 91  ? 0.4390 0.2149 2.0932 -0.0314 -0.1257 -0.0318 91  ASP A O   
732   C CB  . ASP A 91  ? 0.4140 0.2329 2.1040 -0.0428 -0.1084 -0.0235 91  ASP A CB  
733   C CG  . ASP A 91  ? 0.4225 0.2504 2.1310 -0.0458 -0.1185 -0.0315 91  ASP A CG  
734   O OD1 . ASP A 91  ? 0.4197 0.2514 2.1211 -0.0378 -0.1245 -0.0346 91  ASP A OD1 
735   O OD2 . ASP A 91  ? 0.4224 0.2520 2.1516 -0.0562 -0.1207 -0.0345 91  ASP A OD2 
736   N N   . ILE A 92  ? 0.4353 0.2206 2.0667 -0.0151 -0.1221 -0.0305 92  ILE A N   
737   C CA  . ILE A 92  ? 0.4824 0.2496 2.0977 -0.0100 -0.1322 -0.0374 92  ILE A CA  
738   C C   . ILE A 92  ? 0.5209 0.2962 2.1418 -0.0099 -0.1414 -0.0427 92  ILE A C   
739   O O   . ILE A 92  ? 0.5755 0.3608 2.1909 -0.0045 -0.1391 -0.0414 92  ILE A O   
740   C CB  . ILE A 92  ? 0.4959 0.2520 2.0861 0.0011  -0.1275 -0.0364 92  ILE A CB  
741   C CG1 . ILE A 92  ? 0.4916 0.2315 2.0745 0.0021  -0.1240 -0.0342 92  ILE A CG1 
742   C CG2 . ILE A 92  ? 0.5226 0.2660 2.0933 0.0077  -0.1357 -0.0435 92  ILE A CG2 
743   C CD1 . ILE A 92  ? 0.4736 0.2229 2.0678 -0.0021 -0.1147 -0.0258 92  ILE A CD1 
744   N N   . LYS A 93  ? 0.5732 0.3442 2.2062 -0.0162 -0.1526 -0.0487 93  LYS A N   
745   C CA  . LYS A 93  ? 0.5843 0.3628 2.2255 -0.0163 -0.1637 -0.0540 93  LYS A CA  
746   C C   . LYS A 93  ? 0.5800 0.3480 2.1928 -0.0058 -0.1673 -0.0558 93  LYS A C   
747   O O   . LYS A 93  ? 0.6424 0.3897 2.2316 -0.0010 -0.1703 -0.0589 93  LYS A O   
748   C CB  . LYS A 93  ? 0.6038 0.3752 2.2587 -0.0233 -0.1779 -0.0616 93  LYS A CB  
749   C CG  . LYS A 93  ? 0.5930 0.3843 2.2847 -0.0337 -0.1790 -0.0627 93  LYS A CG  
750   C CD  . LYS A 93  ? 0.5966 0.3975 2.3049 -0.0420 -0.1646 -0.0565 93  LYS A CD  
751   C CE  . LYS A 93  ? 0.6405 0.4657 2.3825 -0.0498 -0.1622 -0.0571 93  LYS A CE  
752   N NZ  . LYS A 93  ? 0.6810 0.5122 2.4393 -0.0602 -0.1498 -0.0526 93  LYS A NZ  
753   N N   . PRO A 94  ? 0.5224 0.3030 2.1353 -0.0019 -0.1663 -0.0541 94  PRO A N   
754   C CA  . PRO A 94  ? 0.5264 0.2959 2.1106 0.0071  -0.1681 -0.0551 94  PRO A CA  
755   C C   . PRO A 94  ? 0.5475 0.2976 2.1159 0.0091  -0.1844 -0.0628 94  PRO A C   
756   O O   . PRO A 94  ? 0.5564 0.2914 2.0954 0.0161  -0.1854 -0.0642 94  PRO A O   
757   C CB  . PRO A 94  ? 0.5085 0.2960 2.1005 0.0089  -0.1643 -0.0514 94  PRO A CB  
758   C CG  . PRO A 94  ? 0.4944 0.3032 2.1169 0.0017  -0.1564 -0.0475 94  PRO A CG  
759   C CD  . PRO A 94  ? 0.4973 0.3019 2.1362 -0.0061 -0.1623 -0.0512 94  PRO A CD  
760   N N   . GLU A 95  ? 0.5530 0.3031 2.1402 0.0026  -0.1971 -0.0680 95  GLU A N   
761   C CA  . GLU A 95  ? 0.6102 0.3445 2.1847 0.0045  -0.2151 -0.0755 95  GLU A CA  
762   C C   . GLU A 95  ? 0.6501 0.3613 2.2104 0.0031  -0.2219 -0.0813 95  GLU A C   
763   O O   . GLU A 95  ? 0.6870 0.3819 2.2333 0.0045  -0.2377 -0.0882 95  GLU A O   
764   C CB  . GLU A 95  ? 0.6550 0.4036 2.2596 -0.0008 -0.2284 -0.0792 95  GLU A CB  
765   C CG  . GLU A 95  ? 0.6941 0.4676 2.3194 -0.0005 -0.2214 -0.0742 95  GLU A CG  
766   C CD  . GLU A 95  ? 0.7356 0.5308 2.3930 -0.0083 -0.2082 -0.0701 95  GLU A CD  
767   O OE1 . GLU A 95  ? 0.6796 0.4704 2.3434 -0.0144 -0.2039 -0.0703 95  GLU A OE1 
768   O OE2 . GLU A 95  ? 0.7184 0.5336 2.3928 -0.0082 -0.2024 -0.0669 95  GLU A OE2 
769   N N   . GLU A 96  ? 0.6386 0.3470 2.2012 0.0006  -0.2107 -0.0787 96  GLU A N   
770   C CA  . GLU A 96  ? 0.6349 0.3206 2.1852 -0.0008 -0.2154 -0.0839 96  GLU A CA  
771   C C   . GLU A 96  ? 0.6464 0.3092 2.1568 0.0089  -0.2134 -0.0863 96  GLU A C   
772   O O   . GLU A 96  ? 0.6514 0.3184 2.1465 0.0159  -0.2038 -0.0821 96  GLU A O   
773   C CB  . GLU A 96  ? 0.6284 0.3183 2.1944 -0.0061 -0.2035 -0.0792 96  GLU A CB  
774   C CG  . GLU A 96  ? 0.6244 0.3290 2.2269 -0.0180 -0.2068 -0.0793 96  GLU A CG  
775   C CD  . GLU A 96  ? 0.6401 0.3356 2.2523 -0.0243 -0.2249 -0.0884 96  GLU A CD  
776   O OE1 . GLU A 96  ? 0.6289 0.3006 2.2242 -0.0241 -0.2313 -0.0937 96  GLU A OE1 
777   O OE2 . GLU A 96  ? 0.6711 0.3836 2.3084 -0.0290 -0.2333 -0.0907 96  GLU A OE2 
778   N N   . ASP A 97  ? 0.6370 0.2752 2.1304 0.0090  -0.2222 -0.0936 97  ASP A N   
779   C CA  . ASP A 97  ? 0.6461 0.2612 2.1010 0.0179  -0.2192 -0.0970 97  ASP A CA  
780   C C   . ASP A 97  ? 0.6397 0.2543 2.0924 0.0215  -0.2021 -0.0925 97  ASP A C   
781   O O   . ASP A 97  ? 0.6882 0.2926 2.1466 0.0183  -0.2022 -0.0943 97  ASP A O   
782   C CB  . ASP A 97  ? 0.6733 0.2605 2.1069 0.0178  -0.2348 -0.1072 97  ASP A CB  
783   C CG  . ASP A 97  ? 0.7061 0.2678 2.1007 0.0266  -0.2285 -0.1113 97  ASP A CG  
784   O OD1 . ASP A 97  ? 0.6909 0.2577 2.0725 0.0336  -0.2134 -0.1066 97  ASP A OD1 
785   O OD2 . ASP A 97  ? 0.7441 0.2810 2.1225 0.0261  -0.2378 -0.1196 97  ASP A OD2 
786   N N   . TYR A 98  ? 0.6198 0.2439 2.0635 0.0282  -0.1883 -0.0870 98  TYR A N   
787   C CA  . TYR A 98  ? 0.6110 0.2381 2.0555 0.0324  -0.1725 -0.0824 98  TYR A CA  
788   C C   . TYR A 98  ? 0.6469 0.2471 2.0685 0.0376  -0.1722 -0.0890 98  TYR A C   
789   O O   . TYR A 98  ? 0.6438 0.2421 2.0692 0.0403  -0.1628 -0.0866 98  TYR A O   
790   C CB  . TYR A 98  ? 0.6005 0.2415 2.0375 0.0389  -0.1596 -0.0770 98  TYR A CB  
791   C CG  . TYR A 98  ? 0.5807 0.2454 2.0350 0.0353  -0.1600 -0.0714 98  TYR A CG  
792   C CD1 . TYR A 98  ? 0.5697 0.2527 2.0553 0.0273  -0.1621 -0.0672 98  TYR A CD1 
793   C CD2 . TYR A 98  ? 0.5863 0.2538 2.0249 0.0396  -0.1578 -0.0705 98  TYR A CD2 
794   C CE1 . TYR A 98  ? 0.5420 0.2457 2.0437 0.0244  -0.1624 -0.0631 98  TYR A CE1 
795   C CE2 . TYR A 98  ? 0.5702 0.2573 2.0241 0.0367  -0.1587 -0.0658 98  TYR A CE2 
796   C CZ  . TYR A 98  ? 0.5435 0.2490 2.0295 0.0295  -0.1611 -0.0625 98  TYR A CZ  
797   O OH  . TYR A 98  ? 0.5254 0.2500 2.0273 0.0271  -0.1613 -0.0586 98  TYR A OH  
798   N N   . GLY A 99  ? 0.6899 0.2685 2.0864 0.0393  -0.1827 -0.0975 99  GLY A N   
799   C CA  . GLY A 99  ? 0.7262 0.2768 2.0968 0.0447  -0.1828 -0.1054 99  GLY A CA  
800   C C   . GLY A 99  ? 0.7692 0.3038 2.1476 0.0380  -0.1952 -0.1109 99  GLY A C   
801   O O   . GLY A 99  ? 0.8263 0.3363 2.1858 0.0417  -0.1960 -0.1178 99  GLY A O   
802   N N   . ASP A 100 ? 0.7735 0.3216 2.1805 0.0279  -0.2045 -0.1084 100 ASP A N   
803   C CA  . ASP A 100 ? 0.7810 0.3151 2.1983 0.0199  -0.2164 -0.1137 100 ASP A CA  
804   C C   . ASP A 100 ? 0.7479 0.2799 2.1789 0.0183  -0.2067 -0.1094 100 ASP A C   
805   O O   . ASP A 100 ? 0.7070 0.2594 2.1639 0.0135  -0.1997 -0.1009 100 ASP A O   
806   C CB  . ASP A 100 ? 0.7824 0.3312 2.2258 0.0094  -0.2298 -0.1139 100 ASP A CB  
807   C CG  . ASP A 100 ? 0.8246 0.3639 2.2861 -0.0010 -0.2398 -0.1181 100 ASP A CG  
808   O OD1 . ASP A 100 ? 0.8686 0.3805 2.3106 0.0001  -0.2465 -0.1261 100 ASP A OD1 
809   O OD2 . ASP A 100 ? 0.8434 0.4022 2.3381 -0.0105 -0.2401 -0.1137 100 ASP A OD2 
810   N N   . PRO A 101 ? 0.7599 0.2649 2.1729 0.0221  -0.2071 -0.1155 101 PRO A N   
811   C CA  . PRO A 101 ? 0.7568 0.2554 2.1792 0.0221  -0.1988 -0.1116 101 PRO A CA  
812   C C   . PRO A 101 ? 0.7413 0.2530 2.1962 0.0102  -0.1993 -0.1045 101 PRO A C   
813   O O   . PRO A 101 ? 0.7088 0.2255 2.1736 0.0111  -0.1888 -0.0967 101 PRO A O   
814   C CB  . PRO A 101 ? 0.7906 0.2551 2.1914 0.0239  -0.2067 -0.1222 101 PRO A CB  
815   C CG  . PRO A 101 ? 0.8133 0.2672 2.1836 0.0312  -0.2108 -0.1303 101 PRO A CG  
816   C CD  . PRO A 101 ? 0.7927 0.2702 2.1743 0.0264  -0.2165 -0.1269 101 PRO A CD  
817   N N   . GLU A 102 ? 0.7629 0.2791 2.2339 -0.0010 -0.2119 -0.1076 102 GLU A N   
818   C CA  . GLU A 102 ? 0.7727 0.3000 2.2749 -0.0140 -0.2126 -0.1026 102 GLU A CA  
819   C C   . GLU A 102 ? 0.7163 0.2745 2.2379 -0.0149 -0.2010 -0.0918 102 GLU A C   
820   O O   . GLU A 102 ? 0.6786 0.2428 2.2153 -0.0198 -0.1923 -0.0839 102 GLU A O   
821   C CB  . GLU A 102 ? 0.8376 0.3638 2.3529 -0.0247 -0.2294 -0.1103 102 GLU A CB  
822   C CG  . GLU A 102 ? 0.9232 0.4430 2.4614 -0.0385 -0.2328 -0.1102 102 GLU A CG  
823   C CD  . GLU A 102 ? 1.0139 0.5342 2.5703 -0.0502 -0.2497 -0.1185 102 GLU A CD  
824   O OE1 . GLU A 102 ? 1.0555 0.5796 2.6074 -0.0482 -0.2623 -0.1253 102 GLU A OE1 
825   O OE2 . GLU A 102 ? 1.0717 0.5885 2.6489 -0.0625 -0.2504 -0.1179 102 GLU A OE2 
826   N N   . PHE A 103 ? 0.6963 0.2714 2.2140 -0.0098 -0.2010 -0.0916 103 PHE A N   
827   C CA  . PHE A 103 ? 0.6456 0.2497 2.1794 -0.0099 -0.1913 -0.0828 103 PHE A CA  
828   C C   . PHE A 103 ? 0.6322 0.2384 2.1577 -0.0018 -0.1762 -0.0753 103 PHE A C   
829   O O   . PHE A 103 ? 0.6181 0.2428 2.1606 -0.0051 -0.1672 -0.0667 103 PHE A O   
830   C CB  . PHE A 103 ? 0.6470 0.2648 2.1740 -0.0046 -0.1942 -0.0843 103 PHE A CB  
831   C CG  . PHE A 103 ? 0.6107 0.2575 2.1551 -0.0052 -0.1840 -0.0756 103 PHE A CG  
832   C CD1 . PHE A 103 ? 0.5953 0.2595 2.1694 -0.0154 -0.1809 -0.0705 103 PHE A CD1 
833   C CD2 . PHE A 103 ? 0.6063 0.2618 2.1367 0.0040  -0.1766 -0.0726 103 PHE A CD2 
834   C CE1 . PHE A 103 ? 0.5677 0.2566 2.1557 -0.0158 -0.1714 -0.0632 103 PHE A CE1 
835   C CE2 . PHE A 103 ? 0.5940 0.2746 2.1400 0.0032  -0.1678 -0.0652 103 PHE A CE2 
836   C CZ  . PHE A 103 ? 0.5753 0.2723 2.1495 -0.0065 -0.1656 -0.0608 103 PHE A CZ  
837   N N   . VAL A 104 ? 0.6411 0.2294 2.1408 0.0090  -0.1736 -0.0789 104 VAL A N   
838   C CA  . VAL A 104 ? 0.6213 0.2103 2.1142 0.0179  -0.1606 -0.0732 104 VAL A CA  
839   C C   . VAL A 104 ? 0.6187 0.2005 2.1241 0.0123  -0.1577 -0.0677 104 VAL A C   
840   O O   . VAL A 104 ? 0.5850 0.1797 2.0999 0.0130  -0.1484 -0.0589 104 VAL A O   
841   C CB  . VAL A 104 ? 0.6403 0.2099 2.1053 0.0302  -0.1584 -0.0798 104 VAL A CB  
842   C CG1 . VAL A 104 ? 0.6304 0.2014 2.0926 0.0397  -0.1457 -0.0747 104 VAL A CG1 
843   C CG2 . VAL A 104 ? 0.6396 0.2140 2.0885 0.0350  -0.1600 -0.0844 104 VAL A CG2 
844   N N   . LYS A 105 ? 0.6576 0.2175 2.1620 0.0063  -0.1664 -0.0730 105 LYS A N   
845   C CA  . LYS A 105 ? 0.6873 0.2336 2.1987 0.0015  -0.1641 -0.0684 105 LYS A CA  
846   C C   . LYS A 105 ? 0.6708 0.2373 2.2072 -0.0104 -0.1601 -0.0595 105 LYS A C   
847   O O   . LYS A 105 ? 0.6581 0.2288 2.1988 -0.0099 -0.1513 -0.0504 105 LYS A O   
848   C CB  . LYS A 105 ? 0.7292 0.2461 2.2310 -0.0019 -0.1750 -0.0778 105 LYS A CB  
849   C CG  . LYS A 105 ? 0.7546 0.2486 2.2592 -0.0074 -0.1754 -0.0754 105 LYS A CG  
850   C CD  . LYS A 105 ? 0.7646 0.2490 2.2598 0.0028  -0.1660 -0.0691 105 LYS A CD  
851   C CE  . LYS A 105 ? 0.7774 0.2433 2.2494 0.0182  -0.1649 -0.0759 105 LYS A CE  
852   N NZ  . LYS A 105 ? 0.7586 0.2277 2.2288 0.0288  -0.1549 -0.0683 105 LYS A NZ  
853   N N   . ASP A 106 ? 0.6661 0.2459 2.2189 -0.0206 -0.1665 -0.0624 106 ASP A N   
854   C CA  . ASP A 106 ? 0.6545 0.2569 2.2320 -0.0313 -0.1614 -0.0553 106 ASP A CA  
855   C C   . ASP A 106 ? 0.6348 0.2589 2.2130 -0.0250 -0.1497 -0.0466 106 ASP A C   
856   O O   . ASP A 106 ? 0.6719 0.3069 2.2628 -0.0314 -0.1419 -0.0384 106 ASP A O   
857   C CB  . ASP A 106 ? 0.6404 0.2570 2.2357 -0.0398 -0.1704 -0.0612 106 ASP A CB  
858   C CG  . ASP A 106 ? 0.6817 0.2786 2.2804 -0.0482 -0.1826 -0.0696 106 ASP A CG  
859   O OD1 . ASP A 106 ? 0.7012 0.2787 2.2978 -0.0526 -0.1807 -0.0677 106 ASP A OD1 
860   O OD2 . ASP A 106 ? 0.6922 0.2925 2.2957 -0.0502 -0.1943 -0.0778 106 ASP A OD2 
861   N N   . SER A 107 ? 0.5821 0.2126 2.1464 -0.0132 -0.1482 -0.0484 107 SER A N   
862   C CA  . SER A 107 ? 0.5413 0.1931 2.1082 -0.0083 -0.1380 -0.0409 107 SER A CA  
863   C C   . SER A 107 ? 0.5327 0.1750 2.0912 -0.0025 -0.1302 -0.0341 107 SER A C   
864   O O   . SER A 107 ? 0.5133 0.1663 2.0808 -0.0062 -0.1231 -0.0255 107 SER A O   
865   C CB  . SER A 107 ? 0.5353 0.1970 2.0916 0.0007  -0.1387 -0.0449 107 SER A CB  
866   O OG  . SER A 107 ? 0.5358 0.2032 2.1000 -0.0051 -0.1481 -0.0509 107 SER A OG  
867   N N   . GLU A 108 ? 0.5375 0.1581 2.0784 0.0066  -0.1322 -0.0384 108 GLU A N   
868   C CA  . GLU A 108 ? 0.5314 0.1391 2.0650 0.0131  -0.1273 -0.0333 108 GLU A CA  
869   C C   . GLU A 108 ? 0.5268 0.1289 2.0712 0.0018  -0.1261 -0.0256 108 GLU A C   
870   O O   . GLU A 108 ? 0.5094 0.1173 2.0554 0.0034  -0.1196 -0.0168 108 GLU A O   
871   C CB  . GLU A 108 ? 0.5619 0.1428 2.0778 0.0221  -0.1314 -0.0408 108 GLU A CB  
872   C CG  . GLU A 108 ? 0.5657 0.1481 2.0669 0.0336  -0.1306 -0.0486 108 GLU A CG  
873   C CD  . GLU A 108 ? 0.6121 0.1661 2.0947 0.0415  -0.1345 -0.0578 108 GLU A CD  
874   O OE1 . GLU A 108 ? 0.6402 0.1705 2.1204 0.0373  -0.1405 -0.0602 108 GLU A OE1 
875   O OE2 . GLU A 108 ? 0.6277 0.1821 2.0968 0.0521  -0.1309 -0.0632 108 GLU A OE2 
876   N N   . ILE A 109 ? 0.5348 0.1256 2.0866 -0.0101 -0.1323 -0.0289 109 ILE A N   
877   C CA  . ILE A 109 ? 0.5405 0.1226 2.1010 -0.0220 -0.1302 -0.0220 109 ILE A CA  
878   C C   . ILE A 109 ? 0.5181 0.1260 2.0943 -0.0304 -0.1226 -0.0143 109 ILE A C   
879   O O   . ILE A 109 ? 0.5234 0.1291 2.0996 -0.0340 -0.1162 -0.0051 109 ILE A O   
880   C CB  . ILE A 109 ? 0.5602 0.1240 2.1263 -0.0334 -0.1382 -0.0280 109 ILE A CB  
881   C CG1 . ILE A 109 ? 0.5863 0.1213 2.1348 -0.0254 -0.1457 -0.0360 109 ILE A CG1 
882   C CG2 . ILE A 109 ? 0.5676 0.1228 2.1427 -0.0471 -0.1340 -0.0201 109 ILE A CG2 
883   C CD1 . ILE A 109 ? 0.6020 0.1213 2.1553 -0.0357 -0.1559 -0.0447 109 ILE A CD1 
884   N N   . GLU A 110 ? 0.4989 0.1303 2.0874 -0.0332 -0.1233 -0.0181 110 GLU A N   
885   C CA  . GLU A 110 ? 0.4723 0.1278 2.0761 -0.0408 -0.1157 -0.0120 110 GLU A CA  
886   C C   . GLU A 110 ? 0.4579 0.1222 2.0525 -0.0320 -0.1075 -0.0037 110 GLU A C   
887   O O   . GLU A 110 ? 0.4679 0.1322 2.0636 -0.0375 -0.1008 0.0049  110 GLU A O   
888   C CB  . GLU A 110 ? 0.4508 0.1286 2.0694 -0.0435 -0.1191 -0.0183 110 GLU A CB  
889   C CG  . GLU A 110 ? 0.4299 0.1323 2.0667 -0.0520 -0.1110 -0.0133 110 GLU A CG  
890   C CD  . GLU A 110 ? 0.4379 0.1343 2.0844 -0.0658 -0.1049 -0.0076 110 GLU A CD  
891   O OE1 . GLU A 110 ? 0.4594 0.1335 2.1033 -0.0716 -0.1084 -0.0084 110 GLU A OE1 
892   O OE2 . GLU A 110 ? 0.4173 0.1308 2.0728 -0.0711 -0.0957 -0.0021 110 GLU A OE2 
893   N N   . LEU A 111 ? 0.4331 0.1035 2.0177 -0.0188 -0.1083 -0.0066 111 LEU A N   
894   C CA  . LEU A 111 ? 0.4101 0.0913 1.9886 -0.0102 -0.1016 -0.0002 111 LEU A CA  
895   C C   . LEU A 111 ? 0.4176 0.0809 1.9868 -0.0085 -0.0995 0.0075  111 LEU A C   
896   O O   . LEU A 111 ? 0.4111 0.0829 1.9807 -0.0099 -0.0938 0.0157  111 LEU A O   
897   C CB  . LEU A 111 ? 0.4071 0.0919 1.9757 0.0033  -0.1032 -0.0058 111 LEU A CB  
898   C CG  . LEU A 111 ? 0.3912 0.0898 1.9556 0.0132  -0.0969 -0.0011 111 LEU A CG  
899   C CD1 . LEU A 111 ? 0.3690 0.0893 1.9431 0.0077  -0.0907 0.0060  111 LEU A CD1 
900   C CD2 . LEU A 111 ? 0.3845 0.0902 1.9430 0.0222  -0.0976 -0.0083 111 LEU A CD2 
901   N N   . LYS A 112 ? 0.4324 0.0695 1.9922 -0.0055 -0.1049 0.0045  112 LYS A N   
902   C CA  . LYS A 112 ? 0.4425 0.0582 1.9916 -0.0018 -0.1047 0.0111  112 LYS A CA  
903   C C   . LYS A 112 ? 0.4330 0.0442 1.9857 -0.0151 -0.1008 0.0202  112 LYS A C   
904   O O   . LYS A 112 ? 0.4125 0.0161 1.9566 -0.0122 -0.0984 0.0289  112 LYS A O   
905   C CB  . LYS A 112 ? 0.4742 0.0607 2.0131 0.0031  -0.1113 0.0054  112 LYS A CB  
906   C CG  . LYS A 112 ? 0.4833 0.0663 2.0121 0.0203  -0.1126 0.0005  112 LYS A CG  
907   C CD  . LYS A 112 ? 0.5156 0.0723 2.0348 0.0248  -0.1189 -0.0083 112 LYS A CD  
908   C CE  . LYS A 112 ? 0.5200 0.0798 2.0314 0.0400  -0.1182 -0.0161 112 LYS A CE  
909   N NZ  . LYS A 112 ? 0.5554 0.0860 2.0553 0.0454  -0.1235 -0.0237 112 LYS A NZ  
910   N N   . ARG A 113 ? 0.4189 0.0361 1.9845 -0.0293 -0.0999 0.0180  113 ARG A N   
911   C CA  . ARG A 113 ? 0.4204 0.0338 1.9906 -0.0439 -0.0944 0.0255  113 ARG A CA  
912   C C   . ARG A 113 ? 0.4067 0.0430 1.9795 -0.0448 -0.0863 0.0323  113 ARG A C   
913   O O   . ARG A 113 ? 0.4177 0.0468 1.9829 -0.0493 -0.0812 0.0416  113 ARG A O   
914   C CB  . ARG A 113 ? 0.4106 0.0258 1.9975 -0.0587 -0.0955 0.0198  113 ARG A CB  
915   C CG  . ARG A 113 ? 0.4213 0.0326 2.0142 -0.0751 -0.0878 0.0271  113 ARG A CG  
916   C CD  . ARG A 113 ? 0.4159 0.0387 2.0323 -0.0894 -0.0878 0.0200  113 ARG A CD  
917   N NE  . ARG A 113 ? 0.3852 0.0394 2.0175 -0.0872 -0.0875 0.0142  113 ARG A NE  
918   C CZ  . ARG A 113 ? 0.3663 0.0432 2.0076 -0.0914 -0.0785 0.0180  113 ARG A CZ  
919   N NH1 . ARG A 113 ? 0.3767 0.0488 2.0152 -0.1013 -0.0686 0.0266  113 ARG A NH1 
920   N NH2 . ARG A 113 ? 0.3396 0.0426 1.9922 -0.0868 -0.0791 0.0130  113 ARG A NH2 
921   N N   . VAL A 114 ? 0.3877 0.0500 1.9691 -0.0400 -0.0854 0.0277  114 VAL A N   
922   C CA  . VAL A 114 ? 0.3738 0.0579 1.9578 -0.0407 -0.0780 0.0331  114 VAL A CA  
923   C C   . VAL A 114 ? 0.3841 0.0623 1.9521 -0.0297 -0.0777 0.0402  114 VAL A C   
924   O O   . VAL A 114 ? 0.3888 0.0680 1.9508 -0.0334 -0.0725 0.0486  114 VAL A O   
925   C CB  . VAL A 114 ? 0.3466 0.0567 1.9424 -0.0371 -0.0783 0.0261  114 VAL A CB  
926   C CG1 . VAL A 114 ? 0.3302 0.0622 1.9297 -0.0388 -0.0706 0.0309  114 VAL A CG1 
927   C CG2 . VAL A 114 ? 0.3439 0.0584 1.9559 -0.0461 -0.0814 0.0183  114 VAL A CG2 
928   N N   . LEU A 115 ? 0.3918 0.0631 1.9528 -0.0161 -0.0834 0.0364  115 LEU A N   
929   C CA  . LEU A 115 ? 0.3977 0.0684 1.9484 -0.0040 -0.0840 0.0413  115 LEU A CA  
930   C C   . LEU A 115 ? 0.4310 0.0777 1.9689 -0.0065 -0.0849 0.0506  115 LEU A C   
931   O O   . LEU A 115 ? 0.4317 0.0794 1.9615 -0.0018 -0.0843 0.0579  115 LEU A O   
932   C CB  . LEU A 115 ? 0.3988 0.0657 1.9466 0.0103  -0.0890 0.0340  115 LEU A CB  
933   C CG  . LEU A 115 ? 0.3747 0.0641 1.9305 0.0145  -0.0878 0.0260  115 LEU A CG  
934   C CD1 . LEU A 115 ? 0.3823 0.0626 1.9325 0.0268  -0.0917 0.0182  115 LEU A CD1 
935   C CD2 . LEU A 115 ? 0.3516 0.0656 1.9111 0.0173  -0.0829 0.0298  115 LEU A CD2 
936   N N   . ASN A 116 ? 0.4617 0.0854 1.9973 -0.0142 -0.0870 0.0501  116 ASN A N   
937   C CA  . ASN A 116 ? 0.4944 0.0893 2.0157 -0.0163 -0.0889 0.0585  116 ASN A CA  
938   C C   . ASN A 116 ? 0.5003 0.0977 2.0150 -0.0255 -0.0826 0.0690  116 ASN A C   
939   O O   . ASN A 116 ? 0.5213 0.0993 2.0199 -0.0221 -0.0850 0.0777  116 ASN A O   
940   C CB  . ASN A 116 ? 0.5184 0.0898 2.0403 -0.0259 -0.0911 0.0557  116 ASN A CB  
941   C CG  . ASN A 116 ? 0.5550 0.0930 2.0598 -0.0253 -0.0943 0.0639  116 ASN A CG  
942   O OD1 . ASN A 116 ? 0.5724 0.0908 2.0739 -0.0384 -0.0925 0.0676  116 ASN A OD1 
943   N ND2 . ASN A 116 ? 0.5674 0.0984 2.0619 -0.0100 -0.0993 0.0668  116 ASN A ND2 
944   N N   . TYR A 117 ? 0.4793 0.0993 2.0057 -0.0367 -0.0748 0.0679  117 TYR A N   
945   C CA  . TYR A 117 ? 0.4770 0.1041 1.9975 -0.0450 -0.0672 0.0762  117 TYR A CA  
946   C C   . TYR A 117 ? 0.4525 0.1081 1.9768 -0.0374 -0.0652 0.0753  117 TYR A C   
947   O O   . TYR A 117 ? 0.4544 0.1115 1.9674 -0.0379 -0.0625 0.0829  117 TYR A O   
948   C CB  . TYR A 117 ? 0.4750 0.1038 2.0047 -0.0637 -0.0585 0.0762  117 TYR A CB  
949   C CG  . TYR A 117 ? 0.4444 0.1005 1.9980 -0.0693 -0.0548 0.0667  117 TYR A CG  
950   C CD1 . TYR A 117 ? 0.4152 0.1000 1.9770 -0.0674 -0.0502 0.0648  117 TYR A CD1 
951   C CD2 . TYR A 117 ? 0.4439 0.0964 2.0121 -0.0766 -0.0568 0.0595  117 TYR A CD2 
952   C CE1 . TYR A 117 ? 0.3908 0.0986 1.9739 -0.0716 -0.0480 0.0564  117 TYR A CE1 
953   C CE2 . TYR A 117 ? 0.4196 0.0960 2.0098 -0.0810 -0.0553 0.0508  117 TYR A CE2 
954   C CZ  . TYR A 117 ? 0.3944 0.0983 1.9921 -0.0783 -0.0508 0.0495  117 TYR A CZ  
955   O OH  . TYR A 117 ? 0.3725 0.0989 1.9921 -0.0821 -0.0501 0.0412  117 TYR A OH  
956   N N   . ALA A 118 ? 0.4303 0.1076 1.9690 -0.0308 -0.0667 0.0664  118 ALA A N   
957   C CA  . ALA A 118 ? 0.4147 0.1186 1.9579 -0.0260 -0.0639 0.0655  118 ALA A CA  
958   C C   . ALA A 118 ? 0.4272 0.1297 1.9595 -0.0123 -0.0689 0.0696  118 ALA A C   
959   O O   . ALA A 118 ? 0.4138 0.1333 1.9454 -0.0099 -0.0667 0.0717  118 ALA A O   
960   C CB  . ALA A 118 ? 0.3906 0.1151 1.9503 -0.0231 -0.0643 0.0554  118 ALA A CB  
961   N N   . LYS A 119 ? 0.4576 0.1397 1.9822 -0.0032 -0.0761 0.0703  119 LYS A N   
962   C CA  . LYS A 119 ? 0.4699 0.1511 1.9878 0.0110  -0.0819 0.0730  119 LYS A CA  
963   C C   . LYS A 119 ? 0.4913 0.1626 1.9936 0.0089  -0.0828 0.0839  119 LYS A C   
964   O O   . LYS A 119 ? 0.4980 0.1695 1.9954 0.0203  -0.0888 0.0867  119 LYS A O   
965   C CB  . LYS A 119 ? 0.4916 0.1522 2.0065 0.0219  -0.0892 0.0702  119 LYS A CB  
966   C CG  . LYS A 119 ? 0.5275 0.1550 2.0289 0.0168  -0.0924 0.0766  119 LYS A CG  
967   C CD  . LYS A 119 ? 0.5487 0.1549 2.0483 0.0268  -0.0992 0.0721  119 LYS A CD  
968   C CE  . LYS A 119 ? 0.5924 0.1654 2.0759 0.0236  -0.1032 0.0808  119 LYS A CE  
969   N NZ  . LYS A 119 ? 0.6207 0.1709 2.1036 0.0265  -0.1074 0.0753  119 LYS A NZ  
970   N N   . LYS A 120 ? 0.5038 0.1665 1.9981 -0.0057 -0.0769 0.0897  120 LYS A N   
971   C CA  . LYS A 120 ? 0.5218 0.1743 1.9976 -0.0094 -0.0766 0.1001  120 LYS A CA  
972   C C   . LYS A 120 ? 0.5016 0.1786 1.9802 -0.0163 -0.0689 0.1002  120 LYS A C   
973   O O   . LYS A 120 ? 0.5153 0.1847 1.9772 -0.0222 -0.0666 0.1082  120 LYS A O   
974   C CB  . LYS A 120 ? 0.5542 0.1771 2.0152 -0.0216 -0.0739 0.1073  120 LYS A CB  
975   C CG  . LYS A 120 ? 0.5722 0.1709 2.0335 -0.0190 -0.0793 0.1053  120 LYS A CG  
976   C CD  . LYS A 120 ? 0.6067 0.1741 2.0523 -0.0318 -0.0765 0.1132  120 LYS A CD  
977   C CE  . LYS A 120 ? 0.6014 0.1785 2.0559 -0.0500 -0.0644 0.1113  120 LYS A CE  
978   N NZ  . LYS A 120 ? 0.6366 0.1842 2.0763 -0.0639 -0.0599 0.1191  120 LYS A NZ  
979   N N   . TYR A 121 ? 0.4700 0.1744 1.9678 -0.0156 -0.0650 0.0915  121 TYR A N   
980   C CA  . TYR A 121 ? 0.4579 0.1849 1.9594 -0.0216 -0.0577 0.0908  121 TYR A CA  
981   C C   . TYR A 121 ? 0.4290 0.1793 1.9404 -0.0097 -0.0614 0.0857  121 TYR A C   
982   O O   . TYR A 121 ? 0.4102 0.1754 1.9377 -0.0059 -0.0610 0.0775  121 TYR A O   
983   C CB  . TYR A 121 ? 0.4542 0.1889 1.9683 -0.0350 -0.0482 0.0862  121 TYR A CB  
984   C CG  . TYR A 121 ? 0.4858 0.1973 1.9890 -0.0480 -0.0433 0.0923  121 TYR A CG  
985   C CD1 . TYR A 121 ? 0.5050 0.2092 1.9913 -0.0570 -0.0368 0.1001  121 TYR A CD1 
986   C CD2 . TYR A 121 ? 0.5039 0.1984 2.0113 -0.0511 -0.0453 0.0906  121 TYR A CD2 
987   C CE1 . TYR A 121 ? 0.5361 0.2170 2.0101 -0.0693 -0.0313 0.1063  121 TYR A CE1 
988   C CE2 . TYR A 121 ? 0.5344 0.2061 2.0315 -0.0635 -0.0407 0.0966  121 TYR A CE2 
989   C CZ  . TYR A 121 ? 0.5546 0.2195 2.0349 -0.0728 -0.0331 0.1047  121 TYR A CZ  
990   O OH  . TYR A 121 ? 0.5997 0.2411 2.0688 -0.0863 -0.0269 0.1108  121 TYR A OH  
991   N N   . ASP A 122 ? 0.4287 0.1818 1.9298 -0.0044 -0.0652 0.0905  122 ASP A N   
992   C CA  . ASP A 122 ? 0.4075 0.1799 1.9186 0.0075  -0.0700 0.0860  122 ASP A CA  
993   C C   . ASP A 122 ? 0.3811 0.1798 1.9037 0.0030  -0.0629 0.0806  122 ASP A C   
994   O O   . ASP A 122 ? 0.3763 0.1929 1.9075 0.0110  -0.0652 0.0768  122 ASP A O   
995   C CB  . ASP A 122 ? 0.4279 0.1945 1.9273 0.0162  -0.0787 0.0921  122 ASP A CB  
996   C CG  . ASP A 122 ? 0.4455 0.2113 1.9284 0.0100  -0.0779 0.0988  122 ASP A CG  
997   O OD1 . ASP A 122 ? 0.4406 0.2121 1.9210 -0.0018 -0.0686 0.0987  122 ASP A OD1 
998   O OD2 . ASP A 122 ? 0.4744 0.2330 1.9467 0.0175  -0.0872 0.1039  122 ASP A OD2 
999   N N   . CYS A 123 ? 0.3646 0.1649 1.8879 -0.0097 -0.0542 0.0803  123 CYS A N   
1000  C CA  . CYS A 123 ? 0.3344 0.1576 1.8696 -0.0144 -0.0472 0.0747  123 CYS A CA  
1001  C C   . CYS A 123 ? 0.3098 0.1453 1.8629 -0.0089 -0.0482 0.0662  123 CYS A C   
1002  O O   . CYS A 123 ? 0.2907 0.1457 1.8538 -0.0076 -0.0457 0.0612  123 CYS A O   
1003  C CB  . CYS A 123 ? 0.3402 0.1625 1.8734 -0.0285 -0.0374 0.0760  123 CYS A CB  
1004  S SG  . CYS A 123 ? 0.3398 0.1507 1.8823 -0.0378 -0.0332 0.0736  123 CYS A SG  
1005  N N   . ILE A 124 ? 0.3133 0.1355 1.8684 -0.0055 -0.0521 0.0646  124 ILE A N   
1006  C CA  . ILE A 124 ? 0.2977 0.1282 1.8657 -0.0002 -0.0535 0.0566  124 ILE A CA  
1007  C C   . ILE A 124 ? 0.2944 0.1355 1.8648 0.0120  -0.0572 0.0544  124 ILE A C   
1008  O O   . ILE A 124 ? 0.3091 0.1404 1.8739 0.0204  -0.0628 0.0569  124 ILE A O   
1009  C CB  . ILE A 124 ? 0.3087 0.1202 1.8763 -0.0004 -0.0567 0.0551  124 ILE A CB  
1010  C CG1 . ILE A 124 ? 0.3147 0.1187 1.8840 -0.0141 -0.0520 0.0563  124 ILE A CG1 
1011  C CG2 . ILE A 124 ? 0.2963 0.1134 1.8727 0.0068  -0.0592 0.0469  124 ILE A CG2 
1012  C CD1 . ILE A 124 ? 0.3292 0.1142 1.8992 -0.0162 -0.0553 0.0544  124 ILE A CD1 
1013  N N   . ILE A 125 ? 0.2709 0.1318 1.8506 0.0129  -0.0541 0.0493  125 ILE A N   
1014  C CA  . ILE A 125 ? 0.2585 0.1314 1.8423 0.0228  -0.0560 0.0467  125 ILE A CA  
1015  C C   . ILE A 125 ? 0.2569 0.1341 1.8479 0.0273  -0.0552 0.0392  125 ILE A C   
1016  O O   . ILE A 125 ? 0.2521 0.1373 1.8466 0.0354  -0.0555 0.0363  125 ILE A O   
1017  C CB  . ILE A 125 ? 0.2383 0.1285 1.8235 0.0206  -0.0533 0.0480  125 ILE A CB  
1018  C CG1 . ILE A 125 ? 0.2257 0.1286 1.8180 0.0135  -0.0475 0.0440  125 ILE A CG1 
1019  C CG2 . ILE A 125 ? 0.2483 0.1313 1.8223 0.0168  -0.0549 0.0554  125 ILE A CG2 
1020  C CD1 . ILE A 125 ? 0.2132 0.1333 1.8080 0.0125  -0.0449 0.0436  125 ILE A CD1 
1021  N N   . THR A 126 ? 0.2679 0.1395 1.8610 0.0220  -0.0543 0.0358  126 THR A N   
1022  C CA  . THR A 126 ? 0.2721 0.1427 1.8676 0.0264  -0.0551 0.0290  126 THR A CA  
1023  C C   . THR A 126 ? 0.2819 0.1406 1.8780 0.0204  -0.0571 0.0264  126 THR A C   
1024  O O   . THR A 126 ? 0.2671 0.1281 1.8676 0.0112  -0.0554 0.0278  126 THR A O   
1025  C CB  . THR A 126 ? 0.2588 0.1473 1.8597 0.0268  -0.0515 0.0255  126 THR A CB  
1026  O OG1 . THR A 126 ? 0.2600 0.1571 1.8613 0.0341  -0.0505 0.0262  126 THR A OG1 
1027  C CG2 . THR A 126 ? 0.2598 0.1454 1.8603 0.0289  -0.0522 0.0190  126 THR A CG2 
1028  N N   . TYR A 127 ? 0.2959 0.1419 1.8881 0.0257  -0.0605 0.0220  127 TYR A N   
1029  C CA  . TYR A 127 ? 0.3110 0.1463 1.9039 0.0213  -0.0638 0.0176  127 TYR A CA  
1030  C C   . TYR A 127 ? 0.3209 0.1631 1.9144 0.0237  -0.0643 0.0111  127 TYR A C   
1031  O O   . TYR A 127 ? 0.3312 0.1732 1.9186 0.0319  -0.0634 0.0081  127 TYR A O   
1032  C CB  . TYR A 127 ? 0.3273 0.1408 1.9129 0.0250  -0.0683 0.0162  127 TYR A CB  
1033  C CG  . TYR A 127 ? 0.3325 0.1330 1.9156 0.0211  -0.0693 0.0226  127 TYR A CG  
1034  C CD1 . TYR A 127 ? 0.3345 0.1337 1.9129 0.0269  -0.0688 0.0281  127 TYR A CD1 
1035  C CD2 . TYR A 127 ? 0.3316 0.1207 1.9168 0.0114  -0.0709 0.0234  127 TYR A CD2 
1036  C CE1 . TYR A 127 ? 0.3443 0.1292 1.9172 0.0235  -0.0703 0.0348  127 TYR A CE1 
1037  C CE2 . TYR A 127 ? 0.3419 0.1174 1.9226 0.0070  -0.0708 0.0300  127 TYR A CE2 
1038  C CZ  . TYR A 127 ? 0.3477 0.1200 1.9207 0.0132  -0.0707 0.0361  127 TYR A CZ  
1039  O OH  . TYR A 127 ? 0.3690 0.1259 1.9341 0.0097  -0.0713 0.0434  127 TYR A OH  
1040  N N   . LEU A 128 ? 0.3329 0.1800 1.9333 0.0165  -0.0657 0.0087  128 LEU A N   
1041  C CA  . LEU A 128 ? 0.3379 0.1852 1.9364 0.0183  -0.0690 0.0024  128 LEU A CA  
1042  C C   . LEU A 128 ? 0.3658 0.1956 1.9611 0.0168  -0.0760 -0.0022 128 LEU A C   
1043  O O   . LEU A 128 ? 0.3690 0.1953 1.9729 0.0090  -0.0788 -0.0020 128 LEU A O   
1044  C CB  . LEU A 128 ? 0.3124 0.1751 1.9214 0.0126  -0.0681 0.0019  128 LEU A CB  
1045  C CG  . LEU A 128 ? 0.3055 0.1847 1.9175 0.0132  -0.0614 0.0060  128 LEU A CG  
1046  C CD1 . LEU A 128 ? 0.2970 0.1900 1.9202 0.0075  -0.0604 0.0051  128 LEU A CD1 
1047  C CD2 . LEU A 128 ? 0.3093 0.1905 1.9118 0.0217  -0.0589 0.0050  128 LEU A CD2 
1048  N N   . VAL A 129 ? 0.3868 0.2058 1.9696 0.0241  -0.0785 -0.0070 129 VAL A N   
1049  C CA  . VAL A 129 ? 0.4085 0.2077 1.9839 0.0246  -0.0852 -0.0120 129 VAL A CA  
1050  C C   . VAL A 129 ? 0.4088 0.2060 1.9868 0.0198  -0.0929 -0.0174 129 VAL A C   
1051  O O   . VAL A 129 ? 0.4201 0.2036 1.9980 0.0165  -0.0998 -0.0211 129 VAL A O   
1052  C CB  . VAL A 129 ? 0.4300 0.2199 1.9898 0.0351  -0.0827 -0.0150 129 VAL A CB  
1053  C CG1 . VAL A 129 ? 0.4455 0.2233 1.9915 0.0380  -0.0877 -0.0226 129 VAL A CG1 
1054  C CG2 . VAL A 129 ? 0.4501 0.2268 2.0070 0.0389  -0.0820 -0.0133 129 VAL A CG2 
1055  N N   . ILE A 130 ? 0.4097 0.2198 1.9903 0.0196  -0.0929 -0.0182 130 ILE A N   
1056  C CA  . ILE A 130 ? 0.4249 0.2332 2.0083 0.0162  -0.1019 -0.0234 130 ILE A CA  
1057  C C   . ILE A 130 ? 0.4376 0.2629 2.0272 0.0159  -0.0998 -0.0219 130 ILE A C   
1058  O O   . ILE A 130 ? 0.4692 0.3027 2.0537 0.0200  -0.0920 -0.0186 130 ILE A O   
1059  C CB  . ILE A 130 ? 0.4455 0.2348 2.0084 0.0220  -0.1083 -0.0297 130 ILE A CB  
1060  C CG1 . ILE A 130 ? 0.4447 0.2300 2.0097 0.0186  -0.1203 -0.0352 130 ILE A CG1 
1061  C CG2 . ILE A 130 ? 0.4526 0.2421 1.9982 0.0303  -0.1014 -0.0294 130 ILE A CG2 
1062  C CD1 . ILE A 130 ? 0.4711 0.2338 2.0151 0.0226  -0.1288 -0.0420 130 ILE A CD1 
1063  N N   . ASN A 131 ? 0.4528 0.2825 2.0530 0.0116  -0.1073 -0.0250 131 ASN A N   
1064  C CA  . ASN A 131 ? 0.4325 0.2765 2.0386 0.0119  -0.1062 -0.0241 131 ASN A CA  
1065  C C   . ASN A 131 ? 0.4550 0.2900 2.0504 0.0152  -0.1166 -0.0292 131 ASN A C   
1066  O O   . ASN A 131 ? 0.4964 0.3201 2.0908 0.0139  -0.1273 -0.0342 131 ASN A O   
1067  C CB  . ASN A 131 ? 0.3994 0.2598 2.0310 0.0042  -0.1048 -0.0227 131 ASN A CB  
1068  C CG  . ASN A 131 ? 0.3628 0.2377 2.0029 0.0045  -0.1039 -0.0224 131 ASN A CG  
1069  O OD1 . ASN A 131 ? 0.3615 0.2381 1.9895 0.0095  -0.0997 -0.0204 131 ASN A OD1 
1070  N ND2 . ASN A 131 ? 0.3476 0.2336 2.0100 -0.0011 -0.1069 -0.0245 131 ASN A ND2 
1071  N N   . GLU A 132 ? 0.4587 0.2981 2.0456 0.0191  -0.1140 -0.0277 132 GLU A N   
1072  C CA  . GLU A 132 ? 0.4776 0.3082 2.0524 0.0223  -0.1234 -0.0312 132 GLU A CA  
1073  C C   . GLU A 132 ? 0.4982 0.3073 2.0553 0.0245  -0.1341 -0.0366 132 GLU A C   
1074  O O   . GLU A 132 ? 0.5304 0.3351 2.0925 0.0230  -0.1471 -0.0408 132 GLU A O   
1075  C CB  . GLU A 132 ? 0.4805 0.3224 2.0770 0.0187  -0.1315 -0.0329 132 GLU A CB  
1076  C CG  . GLU A 132 ? 0.4965 0.3591 2.1111 0.0161  -0.1218 -0.0287 132 GLU A CG  
1077  C CD  . GLU A 132 ? 0.5193 0.3872 2.1389 0.0178  -0.1273 -0.0297 132 GLU A CD  
1078  O OE1 . GLU A 132 ? 0.5499 0.4176 2.1827 0.0163  -0.1391 -0.0342 132 GLU A OE1 
1079  O OE2 . GLU A 132 ? 0.4776 0.3490 2.0889 0.0205  -0.1207 -0.0264 132 GLU A OE2 
1080  N N   . PRO A 133 ? 0.4980 0.2926 2.0333 0.0287  -0.1296 -0.0374 133 PRO A N   
1081  C CA  . PRO A 133 ? 0.5164 0.2880 2.0289 0.0316  -0.1394 -0.0431 133 PRO A CA  
1082  C C   . PRO A 133 ? 0.5304 0.2924 2.0220 0.0354  -0.1450 -0.0442 133 PRO A C   
1083  O O   . PRO A 133 ? 0.5456 0.3111 2.0268 0.0383  -0.1357 -0.0405 133 PRO A O   
1084  C CB  . PRO A 133 ? 0.5410 0.3024 2.0379 0.0355  -0.1299 -0.0433 133 PRO A CB  
1085  C CG  . PRO A 133 ? 0.5338 0.3123 2.0381 0.0368  -0.1151 -0.0371 133 PRO A CG  
1086  C CD  . PRO A 133 ? 0.5044 0.3038 2.0358 0.0312  -0.1155 -0.0333 133 PRO A CD  
1087  N N   . GLN A 134 ? 0.5411 0.2905 2.0275 0.0349  -0.1611 -0.0493 134 GLN A N   
1088  C CA  . GLN A 134 ? 0.5579 0.2969 2.0269 0.0379  -0.1708 -0.0503 134 GLN A CA  
1089  C C   . GLN A 134 ? 0.5712 0.2838 2.0003 0.0427  -0.1707 -0.0532 134 GLN A C   
1090  O O   . GLN A 134 ? 0.5757 0.2766 1.9953 0.0433  -0.1699 -0.0570 134 GLN A O   
1091  C CB  . GLN A 134 ? 0.5852 0.3258 2.0721 0.0350  -0.1895 -0.0545 134 GLN A CB  
1092  C CG  . GLN A 134 ? 0.6314 0.3617 2.1035 0.0385  -0.2024 -0.0553 134 GLN A CG  
1093  C CD  . GLN A 134 ? 0.6556 0.4009 2.1367 0.0395  -0.1948 -0.0495 134 GLN A CD  
1094  O OE1 . GLN A 134 ? 0.6913 0.4595 2.2052 0.0360  -0.1905 -0.0478 134 GLN A OE1 
1095  N NE2 . GLN A 134 ? 0.6645 0.3964 2.1163 0.0437  -0.1916 -0.0466 134 GLN A NE2 
1096  N N   . THR A 135 ? 0.5711 0.2736 1.9764 0.0461  -0.1712 -0.0514 135 THR A N   
1097  C CA  . THR A 135 ? 0.5973 0.2771 1.9630 0.0503  -0.1653 -0.0527 135 THR A CA  
1098  C C   . THR A 135 ? 0.6163 0.2687 1.9554 0.0519  -0.1816 -0.0594 135 THR A C   
1099  O O   . THR A 135 ? 0.6386 0.2730 1.9526 0.0543  -0.1772 -0.0633 135 THR A O   
1100  C CB  . THR A 135 ? 0.6078 0.2889 1.9606 0.0519  -0.1571 -0.0472 135 THR A CB  
1101  O OG1 . THR A 135 ? 0.5844 0.2893 1.9612 0.0503  -0.1409 -0.0429 135 THR A OG1 
1102  C CG2 . THR A 135 ? 0.6478 0.3033 1.9568 0.0554  -0.1517 -0.0483 135 THR A CG2 
1103  N N   . ASP A 136 ? 0.6117 0.2604 1.9566 0.0510  -0.2011 -0.0615 136 ASP A N   
1104  C CA  . ASP A 136 ? 0.6302 0.2542 1.9534 0.0520  -0.2192 -0.0684 136 ASP A CA  
1105  C C   . ASP A 136 ? 0.6263 0.2496 1.9610 0.0495  -0.2199 -0.0739 136 ASP A C   
1106  O O   . ASP A 136 ? 0.6479 0.2472 1.9554 0.0511  -0.2253 -0.0799 136 ASP A O   
1107  C CB  . ASP A 136 ? 0.6295 0.2561 1.9693 0.0508  -0.2414 -0.0705 136 ASP A CB  
1108  C CG  . ASP A 136 ? 0.6726 0.2736 1.9906 0.0517  -0.2624 -0.0782 136 ASP A CG  
1109  O OD1 . ASP A 136 ? 0.6977 0.2721 1.9731 0.0557  -0.2668 -0.0786 136 ASP A OD1 
1110  O OD2 . ASP A 136 ? 0.6719 0.2785 2.0142 0.0478  -0.2737 -0.0838 136 ASP A OD2 
1111  N N   . HIS A 137 ? 0.5875 0.2362 1.9622 0.0452  -0.2146 -0.0719 137 HIS A N   
1112  C CA  . HIS A 137 ? 0.5801 0.2295 1.9699 0.0418  -0.2151 -0.0760 137 HIS A CA  
1113  C C   . HIS A 137 ? 0.5960 0.2300 1.9596 0.0455  -0.2019 -0.0775 137 HIS A C   
1114  O O   . HIS A 137 ? 0.6189 0.2336 1.9679 0.0458  -0.2085 -0.0840 137 HIS A O   
1115  C CB  . HIS A 137 ? 0.5385 0.2165 1.9703 0.0367  -0.2067 -0.0717 137 HIS A CB  
1116  C CG  . HIS A 137 ? 0.5411 0.2172 1.9896 0.0318  -0.2123 -0.0763 137 HIS A CG  
1117  N ND1 . HIS A 137 ? 0.5256 0.2137 1.9935 0.0287  -0.1999 -0.0733 137 HIS A ND1 
1118  C CD2 . HIS A 137 ? 0.5603 0.2227 2.0081 0.0291  -0.2293 -0.0835 137 HIS A CD2 
1119  C CE1 . HIS A 137 ? 0.5368 0.2179 2.0152 0.0239  -0.2084 -0.0782 137 HIS A CE1 
1120  N NE2 . HIS A 137 ? 0.5586 0.2252 2.0265 0.0238  -0.2263 -0.0848 137 HIS A NE2 
1121  N N   . ILE A 138 ? 0.5864 0.2301 1.9463 0.0483  -0.1833 -0.0718 138 ILE A N   
1122  C CA  . ILE A 138 ? 0.5932 0.2281 1.9359 0.0523  -0.1683 -0.0730 138 ILE A CA  
1123  C C   . ILE A 138 ? 0.6274 0.2321 1.9260 0.0567  -0.1716 -0.0786 138 ILE A C   
1124  O O   . ILE A 138 ? 0.6423 0.2315 1.9241 0.0595  -0.1666 -0.0836 138 ILE A O   
1125  C CB  . ILE A 138 ? 0.5742 0.2290 1.9271 0.0539  -0.1489 -0.0660 138 ILE A CB  
1126  C CG1 . ILE A 138 ? 0.5389 0.2209 1.9322 0.0494  -0.1457 -0.0609 138 ILE A CG1 
1127  C CG2 . ILE A 138 ? 0.5936 0.2390 1.9277 0.0591  -0.1336 -0.0681 138 ILE A CG2 
1128  C CD1 . ILE A 138 ? 0.5152 0.2161 1.9194 0.0510  -0.1277 -0.0547 138 ILE A CD1 
1129  N N   . HIS A 139 ? 0.6457 0.2398 1.9243 0.0572  -0.1812 -0.0782 139 HIS A N   
1130  C CA  . HIS A 139 ? 0.6855 0.2478 1.9188 0.0607  -0.1862 -0.0836 139 HIS A CA  
1131  C C   . HIS A 139 ? 0.7030 0.2478 1.9317 0.0595  -0.2023 -0.0920 139 HIS A C   
1132  O O   . HIS A 139 ? 0.7298 0.2517 1.9291 0.0625  -0.1993 -0.0982 139 HIS A O   
1133  C CB  . HIS A 139 ? 0.7004 0.2529 1.9129 0.0613  -0.1959 -0.0808 139 HIS A CB  
1134  C CG  . HIS A 139 ? 0.7464 0.2642 1.9071 0.0647  -0.1995 -0.0852 139 HIS A CG  
1135  N ND1 . HIS A 139 ? 0.7659 0.2718 1.8940 0.0676  -0.1817 -0.0834 139 HIS A ND1 
1136  C CD2 . HIS A 139 ? 0.7796 0.2716 1.9151 0.0651  -0.2190 -0.0914 139 HIS A CD2 
1137  C CE1 . HIS A 139 ? 0.8092 0.2818 1.8915 0.0696  -0.1895 -0.0882 139 HIS A CE1 
1138  N NE2 . HIS A 139 ? 0.8216 0.2849 1.9070 0.0684  -0.2129 -0.0932 139 HIS A NE2 
1139  N N   . SER A 140 ? 0.6890 0.2457 1.9485 0.0547  -0.2186 -0.0927 140 SER A N   
1140  C CA  . SER A 140 ? 0.7081 0.2483 1.9646 0.0524  -0.2378 -0.1010 140 SER A CA  
1141  C C   . SER A 140 ? 0.7022 0.2380 1.9642 0.0518  -0.2303 -0.1053 140 SER A C   
1142  O O   . SER A 140 ? 0.7278 0.2372 1.9622 0.0534  -0.2370 -0.1131 140 SER A O   
1143  C CB  . SER A 140 ? 0.6910 0.2468 1.9825 0.0470  -0.2560 -0.1011 140 SER A CB  
1144  O OG  . SER A 140 ? 0.7214 0.2578 2.0047 0.0450  -0.2761 -0.1099 140 SER A OG  
1145  N N   . VAL A 141 ? 0.6700 0.2301 1.9659 0.0496  -0.2173 -0.1002 141 VAL A N   
1146  C CA  . VAL A 141 ? 0.6710 0.2296 1.9774 0.0490  -0.2098 -0.1027 141 VAL A CA  
1147  C C   . VAL A 141 ? 0.6778 0.2298 1.9628 0.0559  -0.1896 -0.1021 141 VAL A C   
1148  O O   . VAL A 141 ? 0.6963 0.2426 1.9843 0.0573  -0.1832 -0.1050 141 VAL A O   
1149  C CB  . VAL A 141 ? 0.6340 0.2196 1.9856 0.0431  -0.2063 -0.0973 141 VAL A CB  
1150  C CG1 . VAL A 141 ? 0.6238 0.2199 2.0023 0.0357  -0.2238 -0.0982 141 VAL A CG1 
1151  C CG2 . VAL A 141 ? 0.6015 0.2117 1.9682 0.0448  -0.1889 -0.0882 141 VAL A CG2 
1152  N N   . THR A 142 ? 0.6629 0.2157 1.9281 0.0600  -0.1798 -0.0987 142 THR A N   
1153  C CA  . THR A 142 ? 0.6715 0.2177 1.9147 0.0664  -0.1607 -0.0991 142 THR A CA  
1154  C C   . THR A 142 ? 0.6368 0.2112 1.9104 0.0669  -0.1441 -0.0917 142 THR A C   
1155  O O   . THR A 142 ? 0.6028 0.1923 1.9083 0.0635  -0.1459 -0.0891 142 THR A O   
1156  C CB  . THR A 142 ? 0.7031 0.2243 1.9231 0.0706  -0.1581 -0.1080 142 THR A CB  
1157  O OG1 . THR A 142 ? 0.6793 0.2096 1.9277 0.0695  -0.1559 -0.1080 142 THR A OG1 
1158  C CG2 . THR A 142 ? 0.7407 0.2314 1.9270 0.0701  -0.1749 -0.1162 142 THR A CG2 
1159  N N   . GLY A 143 ? 0.6410 0.2203 1.9021 0.0709  -0.1281 -0.0886 143 GLY A N   
1160  C CA  . GLY A 143 ? 0.6188 0.2224 1.9038 0.0725  -0.1115 -0.0827 143 GLY A CA  
1161  C C   . GLY A 143 ? 0.6252 0.2271 1.9201 0.0763  -0.1047 -0.0860 143 GLY A C   
1162  O O   . GLY A 143 ? 0.5892 0.2111 1.9133 0.0757  -0.0992 -0.0810 143 GLY A O   
1163  N N   . LYS A 144 ? 0.6688 0.2450 1.9379 0.0802  -0.1058 -0.0945 144 LYS A N   
1164  C CA  . LYS A 144 ? 0.6962 0.2682 1.9727 0.0849  -0.0991 -0.0983 144 LYS A CA  
1165  C C   . LYS A 144 ? 0.6714 0.2545 1.9804 0.0800  -0.1085 -0.0945 144 LYS A C   
1166  O O   . LYS A 144 ? 0.6416 0.2377 1.9724 0.0821  -0.1007 -0.0909 144 LYS A O   
1167  C CB  . LYS A 144 ? 0.7526 0.2928 1.9981 0.0891  -0.1020 -0.1090 144 LYS A CB  
1168  C CG  . LYS A 144 ? 0.7647 0.2995 2.0197 0.0945  -0.0959 -0.1131 144 LYS A CG  
1169  C CD  . LYS A 144 ? 0.8162 0.3214 2.0384 0.1010  -0.0921 -0.1244 144 LYS A CD  
1170  C CE  . LYS A 144 ? 0.8162 0.3136 2.0493 0.1062  -0.0894 -0.1287 144 LYS A CE  
1171  N NZ  . LYS A 144 ? 0.7938 0.3157 2.0549 0.1109  -0.0754 -0.1226 144 LYS A NZ  
1172  N N   . ALA A 145 ? 0.6849 0.2621 1.9961 0.0732  -0.1255 -0.0954 145 ALA A N   
1173  C CA  . ALA A 145 ? 0.6663 0.2509 2.0060 0.0669  -0.1348 -0.0929 145 ALA A CA  
1174  C C   . ALA A 145 ? 0.6242 0.2389 1.9948 0.0642  -0.1274 -0.0830 145 ALA A C   
1175  O O   . ALA A 145 ? 0.5924 0.2154 1.9845 0.0629  -0.1244 -0.0794 145 ALA A O   
1176  C CB  . ALA A 145 ? 0.6730 0.2484 2.0108 0.0600  -0.1538 -0.0963 145 ALA A CB  
1177  N N   . PHE A 146 ? 0.6114 0.2406 1.9818 0.0634  -0.1244 -0.0786 146 PHE A N   
1178  C CA  . PHE A 146 ? 0.5890 0.2458 1.9864 0.0605  -0.1181 -0.0698 146 PHE A CA  
1179  C C   . PHE A 146 ? 0.5745 0.2410 1.9814 0.0658  -0.1036 -0.0666 146 PHE A C   
1180  O O   . PHE A 146 ? 0.5807 0.2595 2.0111 0.0630  -0.1028 -0.0616 146 PHE A O   
1181  C CB  . PHE A 146 ? 0.5855 0.2533 1.9783 0.0595  -0.1168 -0.0664 146 PHE A CB  
1182  C CG  . PHE A 146 ? 0.5486 0.2442 1.9673 0.0570  -0.1093 -0.0580 146 PHE A CG  
1183  C CD1 . PHE A 146 ? 0.5328 0.2426 1.9780 0.0502  -0.1158 -0.0542 146 PHE A CD1 
1184  C CD2 . PHE A 146 ? 0.5351 0.2421 1.9514 0.0610  -0.0953 -0.0545 146 PHE A CD2 
1185  C CE1 . PHE A 146 ? 0.5038 0.2372 1.9699 0.0479  -0.1087 -0.0471 146 PHE A CE1 
1186  C CE2 . PHE A 146 ? 0.5014 0.2325 1.9401 0.0584  -0.0895 -0.0474 146 PHE A CE2 
1187  C CZ  . PHE A 146 ? 0.4830 0.2265 1.9452 0.0521  -0.0962 -0.0438 146 PHE A CZ  
1188  N N   . VAL A 147 ? 0.5664 0.2272 1.9556 0.0733  -0.0923 -0.0695 147 VAL A N   
1189  C CA  . VAL A 147 ? 0.5466 0.2191 1.9478 0.0790  -0.0792 -0.0669 147 VAL A CA  
1190  C C   . VAL A 147 ? 0.5504 0.2139 1.9615 0.0806  -0.0823 -0.0683 147 VAL A C   
1191  O O   . VAL A 147 ? 0.5253 0.2020 1.9574 0.0808  -0.0791 -0.0626 147 VAL A O   
1192  C CB  . VAL A 147 ? 0.5542 0.2207 1.9350 0.0867  -0.0662 -0.0716 147 VAL A CB  
1193  C CG1 . VAL A 147 ? 0.5348 0.2178 1.9327 0.0926  -0.0530 -0.0689 147 VAL A CG1 
1194  C CG2 . VAL A 147 ? 0.5579 0.2264 1.9225 0.0844  -0.0638 -0.0708 147 VAL A CG2 
1195  N N   . ASP A 148 ? 0.5745 0.2129 1.9683 0.0820  -0.0890 -0.0759 148 ASP A N   
1196  C CA  . ASP A 148 ? 0.5900 0.2151 1.9891 0.0842  -0.0917 -0.0782 148 ASP A CA  
1197  C C   . ASP A 148 ? 0.5714 0.2069 1.9958 0.0763  -0.0986 -0.0709 148 ASP A C   
1198  O O   . ASP A 148 ? 0.5684 0.2041 2.0052 0.0786  -0.0962 -0.0678 148 ASP A O   
1199  C CB  . ASP A 148 ? 0.6242 0.2198 1.9980 0.0860  -0.0985 -0.0883 148 ASP A CB  
1200  C CG  . ASP A 148 ? 0.6506 0.2352 1.9985 0.0948  -0.0881 -0.0955 148 ASP A CG  
1201  O OD1 . ASP A 148 ? 0.6254 0.2255 1.9787 0.1006  -0.0740 -0.0931 148 ASP A OD1 
1202  O OD2 . ASP A 148 ? 0.6867 0.2467 2.0089 0.0955  -0.0937 -0.1040 148 ASP A OD2 
1203  N N   . LEU A 149 ? 0.5565 0.2009 1.9885 0.0674  -0.1067 -0.0681 149 LEU A N   
1204  C CA  . LEU A 149 ? 0.5419 0.1980 1.9979 0.0589  -0.1116 -0.0615 149 LEU A CA  
1205  C C   . LEU A 149 ? 0.5213 0.1995 1.9941 0.0606  -0.1015 -0.0530 149 LEU A C   
1206  O O   . LEU A 149 ? 0.5214 0.1987 2.0047 0.0610  -0.0997 -0.0491 149 LEU A O   
1207  C CB  . LEU A 149 ? 0.5355 0.1990 1.9984 0.0499  -0.1212 -0.0612 149 LEU A CB  
1208  C CG  . LEU A 149 ? 0.5208 0.1962 2.0095 0.0402  -0.1250 -0.0554 149 LEU A CG  
1209  C CD1 . LEU A 149 ? 0.5349 0.1928 2.0272 0.0367  -0.1299 -0.0571 149 LEU A CD1 
1210  C CD2 . LEU A 149 ? 0.5179 0.2020 2.0150 0.0327  -0.1341 -0.0565 149 LEU A CD2 
1211  N N   . MET A 150 ? 0.5010 0.1970 1.9743 0.0615  -0.0957 -0.0504 150 MET A N   
1212  C CA  . MET A 150 ? 0.4766 0.1938 1.9637 0.0636  -0.0863 -0.0434 150 MET A CA  
1213  C C   . MET A 150 ? 0.4913 0.2031 1.9791 0.0718  -0.0801 -0.0433 150 MET A C   
1214  O O   . MET A 150 ? 0.4840 0.2051 1.9865 0.0715  -0.0781 -0.0370 150 MET A O   
1215  C CB  . MET A 150 ? 0.4739 0.2041 1.9546 0.0662  -0.0792 -0.0432 150 MET A CB  
1216  C CG  . MET A 150 ? 0.4701 0.2058 1.9494 0.0597  -0.0852 -0.0429 150 MET A CG  
1217  S SD  . MET A 150 ? 0.4296 0.1846 1.9345 0.0498  -0.0897 -0.0359 150 MET A SD  
1218  C CE  . MET A 150 ? 0.4490 0.1878 1.9551 0.0430  -0.1038 -0.0405 150 MET A CE  
1219  N N   . ASN A 151 ? 0.5064 0.2026 1.9780 0.0799  -0.0771 -0.0505 151 ASN A N   
1220  C CA  . ASN A 151 ? 0.5219 0.2141 1.9970 0.0887  -0.0714 -0.0509 151 ASN A CA  
1221  C C   . ASN A 151 ? 0.5234 0.2027 2.0059 0.0862  -0.0788 -0.0484 151 ASN A C   
1222  O O   . ASN A 151 ? 0.5052 0.1907 2.0000 0.0893  -0.0765 -0.0429 151 ASN A O   
1223  C CB  . ASN A 151 ? 0.5474 0.2256 2.0050 0.0985  -0.0652 -0.0600 151 ASN A CB  
1224  C CG  . ASN A 151 ? 0.5307 0.2248 1.9852 0.1022  -0.0540 -0.0608 151 ASN A CG  
1225  O OD1 . ASN A 151 ? 0.5496 0.2338 1.9842 0.1044  -0.0503 -0.0675 151 ASN A OD1 
1226  N ND2 . ASN A 151 ? 0.5025 0.2201 1.9753 0.1024  -0.0486 -0.0542 151 ASN A ND2 
1227  N N   . THR A 152 ? 0.5320 0.1928 2.0068 0.0802  -0.0881 -0.0522 152 THR A N   
1228  C CA  . THR A 152 ? 0.5405 0.1880 2.0224 0.0755  -0.0950 -0.0494 152 THR A CA  
1229  C C   . THR A 152 ? 0.5074 0.1734 2.0080 0.0689  -0.0941 -0.0390 152 THR A C   
1230  O O   . THR A 152 ? 0.5086 0.1713 2.0160 0.0709  -0.0933 -0.0337 152 THR A O   
1231  C CB  . THR A 152 ? 0.5610 0.1911 2.0363 0.0672  -0.1055 -0.0544 152 THR A CB  
1232  O OG1 . THR A 152 ? 0.6025 0.2112 2.0577 0.0737  -0.1070 -0.0643 152 THR A OG1 
1233  C CG2 . THR A 152 ? 0.5636 0.1804 2.0476 0.0608  -0.1114 -0.0510 152 THR A CG2 
1234  N N   . LEU A 153 ? 0.4779 0.1614 1.9856 0.0612  -0.0946 -0.0362 153 LEU A N   
1235  C CA  . LEU A 153 ? 0.4574 0.1558 1.9812 0.0530  -0.0943 -0.0276 153 LEU A CA  
1236  C C   . LEU A 153 ? 0.4543 0.1676 1.9846 0.0591  -0.0867 -0.0212 153 LEU A C   
1237  O O   . LEU A 153 ? 0.4685 0.1801 2.0054 0.0575  -0.0870 -0.0148 153 LEU A O   
1238  C CB  . LEU A 153 ? 0.4379 0.1510 1.9681 0.0446  -0.0966 -0.0276 153 LEU A CB  
1239  C CG  . LEU A 153 ? 0.4451 0.1457 1.9737 0.0371  -0.1062 -0.0332 153 LEU A CG  
1240  C CD1 . LEU A 153 ? 0.4284 0.1449 1.9635 0.0315  -0.1088 -0.0340 153 LEU A CD1 
1241  C CD2 . LEU A 153 ? 0.4514 0.1427 1.9901 0.0285  -0.1101 -0.0302 153 LEU A CD2 
1242  N N   . ILE A 154 ? 0.4373 0.1635 1.9648 0.0662  -0.0804 -0.0233 154 ILE A N   
1243  C CA  . ILE A 154 ? 0.4139 0.1550 1.9490 0.0725  -0.0740 -0.0187 154 ILE A CA  
1244  C C   . ILE A 154 ? 0.4244 0.1512 1.9598 0.0792  -0.0756 -0.0171 154 ILE A C   
1245  O O   . ILE A 154 ? 0.4212 0.1519 1.9644 0.0779  -0.0765 -0.0097 154 ILE A O   
1246  C CB  . ILE A 154 ? 0.4174 0.1690 1.9478 0.0798  -0.0667 -0.0235 154 ILE A CB  
1247  C CG1 . ILE A 154 ? 0.4081 0.1751 1.9389 0.0733  -0.0651 -0.0230 154 ILE A CG1 
1248  C CG2 . ILE A 154 ? 0.4089 0.1730 1.9483 0.0884  -0.0606 -0.0209 154 ILE A CG2 
1249  C CD1 . ILE A 154 ? 0.4125 0.1837 1.9337 0.0788  -0.0581 -0.0283 154 ILE A CD1 
1250  N N   . ASN A 155 ? 0.4337 0.1427 1.9592 0.0869  -0.0759 -0.0244 155 ASN A N   
1251  C CA  . ASN A 155 ? 0.4478 0.1427 1.9736 0.0956  -0.0771 -0.0241 155 ASN A CA  
1252  C C   . ASN A 155 ? 0.4634 0.1474 1.9928 0.0884  -0.0837 -0.0164 155 ASN A C   
1253  O O   . ASN A 155 ? 0.4730 0.1606 2.0090 0.0915  -0.0840 -0.0096 155 ASN A O   
1254  C CB  . ASN A 155 ? 0.4658 0.1402 1.9788 0.1034  -0.0769 -0.0341 155 ASN A CB  
1255  C CG  . ASN A 155 ? 0.4589 0.1442 1.9682 0.1116  -0.0679 -0.0410 155 ASN A CG  
1256  O OD1 . ASN A 155 ? 0.4404 0.1485 1.9597 0.1140  -0.0617 -0.0380 155 ASN A OD1 
1257  N ND2 . ASN A 155 ? 0.4758 0.1444 1.9699 0.1157  -0.0667 -0.0505 155 ASN A ND2 
1258  N N   . ILE A 156 ? 0.4724 0.1436 1.9975 0.0781  -0.0890 -0.0173 156 ILE A N   
1259  C CA  . ILE A 156 ? 0.4766 0.1366 2.0046 0.0689  -0.0939 -0.0103 156 ILE A CA  
1260  C C   . ILE A 156 ? 0.4590 0.1373 1.9964 0.0646  -0.0912 -0.0004 156 ILE A C   
1261  O O   . ILE A 156 ? 0.4661 0.1353 2.0035 0.0640  -0.0931 0.0067  156 ILE A O   
1262  C CB  . ILE A 156 ? 0.4836 0.1355 2.0104 0.0568  -0.0985 -0.0135 156 ILE A CB  
1263  C CG1 . ILE A 156 ? 0.5076 0.1346 2.0229 0.0603  -0.1034 -0.0226 156 ILE A CG1 
1264  C CG2 . ILE A 156 ? 0.4859 0.1343 2.0195 0.0442  -0.1006 -0.0056 156 ILE A CG2 
1265  C CD1 . ILE A 156 ? 0.5109 0.1327 2.0253 0.0498  -0.1091 -0.0279 156 ILE A CD1 
1266  N N   . ILE A 157 ? 0.4461 0.1487 1.9898 0.0617  -0.0869 0.0004  157 ILE A N   
1267  C CA  . ILE A 157 ? 0.4333 0.1519 1.9842 0.0573  -0.0844 0.0091  157 ILE A CA  
1268  C C   . ILE A 157 ? 0.4317 0.1541 1.9839 0.0685  -0.0834 0.0125  157 ILE A C   
1269  O O   . ILE A 157 ? 0.4329 0.1541 1.9857 0.0667  -0.0849 0.0206  157 ILE A O   
1270  C CB  . ILE A 157 ? 0.4148 0.1572 1.9724 0.0513  -0.0804 0.0084  157 ILE A CB  
1271  C CG1 . ILE A 157 ? 0.4157 0.1551 1.9748 0.0410  -0.0830 0.0047  157 ILE A CG1 
1272  C CG2 . ILE A 157 ? 0.4104 0.1682 1.9741 0.0470  -0.0776 0.0168  157 ILE A CG2 
1273  C CD1 . ILE A 157 ? 0.3947 0.1551 1.9594 0.0375  -0.0802 0.0024  157 ILE A CD1 
1274  N N   . HIS A 158 ? 0.4265 0.1528 1.9788 0.0800  -0.0809 0.0061  158 HIS A N   
1275  C CA  . HIS A 158 ? 0.4336 0.1661 1.9910 0.0911  -0.0803 0.0083  158 HIS A CA  
1276  C C   . HIS A 158 ? 0.4584 0.1685 2.0117 0.0947  -0.0868 0.0131  158 HIS A C   
1277  O O   . HIS A 158 ? 0.4522 0.1661 2.0086 0.0968  -0.0893 0.0204  158 HIS A O   
1278  C CB  . HIS A 158 ? 0.4337 0.1735 1.9938 0.1029  -0.0753 -0.0002 158 HIS A CB  
1279  C CG  . HIS A 158 ? 0.4074 0.1716 1.9726 0.1007  -0.0686 -0.0025 158 HIS A CG  
1280  N ND1 . HIS A 158 ? 0.4053 0.1746 1.9689 0.1068  -0.0622 -0.0107 158 HIS A ND1 
1281  C CD2 . HIS A 158 ? 0.3839 0.1666 1.9541 0.0927  -0.0669 0.0023  158 HIS A CD2 
1282  C CE1 . HIS A 158 ? 0.3862 0.1760 1.9536 0.1024  -0.0572 -0.0103 158 HIS A CE1 
1283  N NE2 . HIS A 158 ? 0.3736 0.1717 1.9455 0.0939  -0.0602 -0.0027 158 HIS A NE2 
1284  N N   . LYS A 159 ? 0.4902 0.1757 2.0354 0.0954  -0.0900 0.0090  159 LYS A N   
1285  C CA  . LYS A 159 ? 0.5246 0.1853 2.0645 0.0992  -0.0963 0.0131  159 LYS A CA  
1286  C C   . LYS A 159 ? 0.4993 0.1529 2.0351 0.0865  -0.0993 0.0234  159 LYS A C   
1287  O O   . LYS A 159 ? 0.5016 0.1443 2.0340 0.0893  -0.1037 0.0310  159 LYS A O   
1288  C CB  . LYS A 159 ? 0.5922 0.2268 2.1238 0.1029  -0.0989 0.0056  159 LYS A CB  
1289  C CG  . LYS A 159 ? 0.6552 0.2931 2.1877 0.1153  -0.0947 -0.0055 159 LYS A CG  
1290  C CD  . LYS A 159 ? 0.7451 0.3553 2.2672 0.1195  -0.0972 -0.0140 159 LYS A CD  
1291  C CE  . LYS A 159 ? 0.8213 0.4210 2.3347 0.1064  -0.0992 -0.0173 159 LYS A CE  
1292  N NZ  . LYS A 159 ? 0.7776 0.3981 2.2922 0.0996  -0.0949 -0.0206 159 LYS A NZ  
1293  N N   . GLY A 160 ? 0.4653 0.1255 2.0016 0.0729  -0.0966 0.0233  160 GLY A N   
1294  C CA  . GLY A 160 ? 0.4626 0.1131 1.9952 0.0592  -0.0977 0.0309  160 GLY A CA  
1295  C C   . GLY A 160 ? 0.4445 0.1119 1.9792 0.0545  -0.0951 0.0396  160 GLY A C   
1296  O O   . GLY A 160 ? 0.4548 0.1095 1.9826 0.0477  -0.0965 0.0481  160 GLY A O   
1297  N N   . HIS A 161 ? 0.4200 0.1146 1.9629 0.0569  -0.0910 0.0375  161 HIS A N   
1298  C CA  . HIS A 161 ? 0.4095 0.1203 1.9539 0.0540  -0.0890 0.0447  161 HIS A CA  
1299  C C   . HIS A 161 ? 0.3998 0.1288 1.9511 0.0667  -0.0888 0.0423  161 HIS A C   
1300  O O   . HIS A 161 ? 0.3661 0.1184 1.9252 0.0662  -0.0841 0.0389  161 HIS A O   
1301  C CB  . HIS A 161 ? 0.3928 0.1188 1.9418 0.0405  -0.0834 0.0449  161 HIS A CB  
1302  C CG  . HIS A 161 ? 0.3907 0.1256 1.9372 0.0343  -0.0812 0.0531  161 HIS A CG  
1303  N ND1 . HIS A 161 ? 0.3775 0.1270 1.9285 0.0229  -0.0754 0.0537  161 HIS A ND1 
1304  C CD2 . HIS A 161 ? 0.4005 0.1319 1.9399 0.0386  -0.0843 0.0604  161 HIS A CD2 
1305  C CE1 . HIS A 161 ? 0.3796 0.1331 1.9248 0.0199  -0.0741 0.0611  161 HIS A CE1 
1306  N NE2 . HIS A 161 ? 0.3922 0.1347 1.9295 0.0293  -0.0800 0.0654  161 HIS A NE2 
1307  N N   . PRO A 162 ? 0.4261 0.1447 1.9759 0.0787  -0.0941 0.0436  162 PRO A N   
1308  C CA  . PRO A 162 ? 0.4162 0.1525 1.9761 0.0913  -0.0939 0.0401  162 PRO A CA  
1309  C C   . PRO A 162 ? 0.4032 0.1613 1.9672 0.0873  -0.0925 0.0452  162 PRO A C   
1310  O O   . PRO A 162 ? 0.4195 0.1708 1.9749 0.0798  -0.0950 0.0535  162 PRO A O   
1311  C CB  . PRO A 162 ? 0.4432 0.1613 2.0009 0.1029  -0.1012 0.0422  162 PRO A CB  
1312  C CG  . PRO A 162 ? 0.4664 0.1584 2.0094 0.0944  -0.1060 0.0508  162 PRO A CG  
1313  C CD  . PRO A 162 ? 0.4560 0.1451 1.9954 0.0806  -0.1006 0.0486  162 PRO A CD  
1314  N N   . GLY A 163 ? 0.3775 0.1603 1.9529 0.0911  -0.0879 0.0400  163 GLY A N   
1315  C CA  . GLY A 163 ? 0.3584 0.1624 1.9387 0.0881  -0.0869 0.0436  163 GLY A CA  
1316  C C   . GLY A 163 ? 0.3425 0.1653 1.9273 0.0800  -0.0790 0.0395  163 GLY A C   
1317  O O   . GLY A 163 ? 0.3502 0.1941 1.9431 0.0809  -0.0765 0.0386  163 GLY A O   
1318  N N   . ILE A 164 ? 0.3347 0.1493 1.9148 0.0725  -0.0759 0.0368  164 ILE A N   
1319  C CA  . ILE A 164 ? 0.3091 0.1365 1.8907 0.0620  -0.0707 0.0358  164 ILE A CA  
1320  C C   . ILE A 164 ? 0.3028 0.1390 1.8888 0.0643  -0.0660 0.0275  164 ILE A C   
1321  O O   . ILE A 164 ? 0.3188 0.1423 1.9010 0.0661  -0.0665 0.0226  164 ILE A O   
1322  C CB  . ILE A 164 ? 0.3092 0.1225 1.8839 0.0506  -0.0711 0.0391  164 ILE A CB  
1323  C CG1 . ILE A 164 ? 0.3209 0.1210 1.8871 0.0471  -0.0747 0.0479  164 ILE A CG1 
1324  C CG2 . ILE A 164 ? 0.2921 0.1205 1.8714 0.0408  -0.0660 0.0375  164 ILE A CG2 
1325  C CD1 . ILE A 164 ? 0.3136 0.1274 1.8792 0.0456  -0.0743 0.0533  164 ILE A CD1 
1326  N N   . PRO A 165 ? 0.2889 0.1455 1.8811 0.0629  -0.0614 0.0256  165 PRO A N   
1327  C CA  . PRO A 165 ? 0.2852 0.1475 1.8781 0.0633  -0.0570 0.0187  165 PRO A CA  
1328  C C   . PRO A 165 ? 0.2956 0.1470 1.8828 0.0564  -0.0579 0.0159  165 PRO A C   
1329  O O   . PRO A 165 ? 0.2918 0.1423 1.8795 0.0472  -0.0591 0.0190  165 PRO A O   
1330  C CB  . PRO A 165 ? 0.2677 0.1516 1.8670 0.0598  -0.0529 0.0198  165 PRO A CB  
1331  C CG  . PRO A 165 ? 0.2680 0.1589 1.8720 0.0631  -0.0553 0.0248  165 PRO A CG  
1332  C CD  . PRO A 165 ? 0.2814 0.1544 1.8783 0.0609  -0.0608 0.0301  165 PRO A CD  
1333  N N   . VAL A 166 ? 0.3052 0.1492 1.8875 0.0608  -0.0571 0.0092  166 VAL A N   
1334  C CA  . VAL A 166 ? 0.3075 0.1418 1.8842 0.0557  -0.0592 0.0051  166 VAL A CA  
1335  C C   . VAL A 166 ? 0.3106 0.1544 1.8848 0.0566  -0.0552 0.0005  166 VAL A C   
1336  O O   . VAL A 166 ? 0.3160 0.1619 1.8872 0.0640  -0.0509 -0.0030 166 VAL A O   
1337  C CB  . VAL A 166 ? 0.3232 0.1357 1.8918 0.0605  -0.0628 0.0011  166 VAL A CB  
1338  C CG1 . VAL A 166 ? 0.3285 0.1296 1.8899 0.0564  -0.0663 -0.0044 166 VAL A CG1 
1339  C CG2 . VAL A 166 ? 0.3338 0.1340 1.9033 0.0596  -0.0669 0.0063  166 VAL A CG2 
1340  N N   . THR A 167 ? 0.3178 0.1666 1.8932 0.0491  -0.0565 0.0003  167 THR A N   
1341  C CA  . THR A 167 ? 0.3193 0.1721 1.8893 0.0494  -0.0545 -0.0039 167 THR A CA  
1342  C C   . THR A 167 ? 0.3154 0.1616 1.8846 0.0425  -0.0609 -0.0058 167 THR A C   
1343  O O   . THR A 167 ? 0.3305 0.1693 1.9040 0.0382  -0.0653 -0.0046 167 THR A O   
1344  C CB  . THR A 167 ? 0.3037 0.1758 1.8800 0.0487  -0.0488 -0.0012 167 THR A CB  
1345  O OG1 . THR A 167 ? 0.3048 0.1775 1.8736 0.0486  -0.0471 -0.0048 167 THR A OG1 
1346  C CG2 . THR A 167 ? 0.2917 0.1749 1.8783 0.0410  -0.0499 0.0035  167 THR A CG2 
1347  N N   . LEU A 168 ? 0.3114 0.1595 1.8754 0.0417  -0.0615 -0.0089 168 LEU A N   
1348  C CA  . LEU A 168 ? 0.3227 0.1659 1.8874 0.0363  -0.0688 -0.0115 168 LEU A CA  
1349  C C   . LEU A 168 ? 0.3207 0.1785 1.8922 0.0325  -0.0678 -0.0099 168 LEU A C   
1350  O O   . LEU A 168 ? 0.3161 0.1840 1.8865 0.0346  -0.0616 -0.0081 168 LEU A O   
1351  C CB  . LEU A 168 ? 0.3432 0.1688 1.8908 0.0402  -0.0733 -0.0177 168 LEU A CB  
1352  C CG  . LEU A 168 ? 0.3509 0.1763 1.8851 0.0434  -0.0709 -0.0199 168 LEU A CG  
1353  C CD1 . LEU A 168 ? 0.3716 0.1770 1.8865 0.0459  -0.0770 -0.0260 168 LEU A CD1 
1354  C CD2 . LEU A 168 ? 0.3585 0.1910 1.8889 0.0488  -0.0601 -0.0185 168 LEU A CD2 
1355  N N   . SER A 169 ? 0.3369 0.1954 1.9165 0.0269  -0.0743 -0.0112 169 SER A N   
1356  C CA  . SER A 169 ? 0.3257 0.1967 1.9138 0.0236  -0.0745 -0.0105 169 SER A CA  
1357  C C   . SER A 169 ? 0.3229 0.1848 1.8996 0.0259  -0.0811 -0.0148 169 SER A C   
1358  O O   . SER A 169 ? 0.3124 0.1714 1.8951 0.0229  -0.0899 -0.0178 169 SER A O   
1359  C CB  . SER A 169 ? 0.3275 0.2065 1.9345 0.0162  -0.0764 -0.0093 169 SER A CB  
1360  O OG  . SER A 169 ? 0.3706 0.2553 1.9865 0.0134  -0.0814 -0.0119 169 SER A OG  
1361  N N   . ALA A 170 ? 0.3245 0.1801 1.8836 0.0313  -0.0772 -0.0155 170 ALA A N   
1362  C CA  . ALA A 170 ? 0.3405 0.1836 1.8827 0.0338  -0.0828 -0.0189 170 ALA A CA  
1363  C C   . ALA A 170 ? 0.3457 0.1980 1.8908 0.0326  -0.0818 -0.0169 170 ALA A C   
1364  O O   . ALA A 170 ? 0.3451 0.2117 1.8988 0.0315  -0.0735 -0.0133 170 ALA A O   
1365  C CB  . ALA A 170 ? 0.3527 0.1833 1.8729 0.0395  -0.0775 -0.0207 170 ALA A CB  
1366  N N   . ASN A 171 ? 0.3474 0.1900 1.8842 0.0330  -0.0912 -0.0196 171 ASN A N   
1367  C CA  . ASN A 171 ? 0.3266 0.1743 1.8653 0.0324  -0.0926 -0.0181 171 ASN A CA  
1368  C C   . ASN A 171 ? 0.3449 0.1840 1.8606 0.0357  -0.0862 -0.0167 171 ASN A C   
1369  O O   . ASN A 171 ? 0.3675 0.1879 1.8597 0.0387  -0.0897 -0.0190 171 ASN A O   
1370  C CB  . ASN A 171 ? 0.3337 0.1742 1.8754 0.0319  -0.1072 -0.0217 171 ASN A CB  
1371  C CG  . ASN A 171 ? 0.3210 0.1668 1.8674 0.0319  -0.1096 -0.0203 171 ASN A CG  
1372  O OD1 . ASN A 171 ? 0.3355 0.1719 1.8622 0.0345  -0.1076 -0.0187 171 ASN A OD1 
1373  N ND2 . ASN A 171 ? 0.2960 0.1567 1.8683 0.0287  -0.1126 -0.0209 171 ASN A ND2 
1374  N N   . ALA A 172 ? 0.3180 0.1702 1.8401 0.0344  -0.0769 -0.0130 172 ALA A N   
1375  C CA  . ALA A 172 ? 0.3299 0.1772 1.8346 0.0358  -0.0687 -0.0111 172 ALA A CA  
1376  C C   . ALA A 172 ? 0.3618 0.1894 1.8435 0.0376  -0.0760 -0.0121 172 ALA A C   
1377  O O   . ALA A 172 ? 0.3658 0.1806 1.8240 0.0392  -0.0698 -0.0118 172 ALA A O   
1378  C CB  . ALA A 172 ? 0.3112 0.1758 1.8306 0.0329  -0.0613 -0.0077 172 ALA A CB  
1379  N N   . MET A 173 ? 0.3630 0.1881 1.8520 0.0372  -0.0889 -0.0134 173 MET A N   
1380  C CA  . MET A 173 ? 0.3831 0.1902 1.8528 0.0391  -0.0982 -0.0137 173 MET A CA  
1381  C C   . MET A 173 ? 0.4111 0.1962 1.8587 0.0420  -0.1087 -0.0174 173 MET A C   
1382  O O   . MET A 173 ? 0.4285 0.1940 1.8513 0.0441  -0.1149 -0.0172 173 MET A O   
1383  C CB  . MET A 173 ? 0.3836 0.1996 1.8741 0.0383  -0.1079 -0.0139 173 MET A CB  
1384  C CG  . MET A 173 ? 0.3838 0.2134 1.8856 0.0362  -0.0988 -0.0103 173 MET A CG  
1385  S SD  . MET A 173 ? 0.4099 0.2225 1.8836 0.0371  -0.0949 -0.0066 173 MET A SD  
1386  C CE  . MET A 173 ? 0.4387 0.2283 1.8968 0.0413  -0.1149 -0.0086 173 MET A CE  
1387  N N   . ILE A 174 ? 0.4250 0.2111 1.8795 0.0420  -0.1115 -0.0208 174 ILE A N   
1388  C CA  . ILE A 174 ? 0.4541 0.2184 1.8858 0.0446  -0.1202 -0.0251 174 ILE A CA  
1389  C C   . ILE A 174 ? 0.4742 0.2347 1.8958 0.0457  -0.1096 -0.0267 174 ILE A C   
1390  O O   . ILE A 174 ? 0.5143 0.2546 1.9128 0.0481  -0.1145 -0.0306 174 ILE A O   
1391  C CB  . ILE A 174 ? 0.4526 0.2166 1.8999 0.0437  -0.1368 -0.0294 174 ILE A CB  
1392  C CG1 . ILE A 174 ? 0.4195 0.2040 1.8985 0.0402  -0.1328 -0.0297 174 ILE A CG1 
1393  C CG2 . ILE A 174 ? 0.4626 0.2252 1.9160 0.0443  -0.1507 -0.0295 174 ILE A CG2 
1394  C CD1 . ILE A 174 ? 0.4196 0.2024 1.9130 0.0384  -0.1472 -0.0346 174 ILE A CD1 
1395  N N   . SER A 175 ? 0.4511 0.2299 1.8903 0.0445  -0.0966 -0.0244 175 SER A N   
1396  C CA  . SER A 175 ? 0.4728 0.2479 1.9048 0.0467  -0.0879 -0.0264 175 SER A CA  
1397  C C   . SER A 175 ? 0.4648 0.2469 1.8914 0.0477  -0.0711 -0.0236 175 SER A C   
1398  O O   . SER A 175 ? 0.4673 0.2571 1.9006 0.0493  -0.0612 -0.0240 175 SER A O   
1399  C CB  . SER A 175 ? 0.4725 0.2582 1.9282 0.0453  -0.0905 -0.0275 175 SER A CB  
1400  O OG  . SER A 175 ? 0.5063 0.2831 1.9648 0.0439  -0.1057 -0.0312 175 SER A OG  
1401  N N   . ASP A 176 ? 0.4539 0.2312 1.8665 0.0470  -0.0682 -0.0212 176 ASP A N   
1402  C CA  . ASP A 176 ? 0.4295 0.2119 1.8359 0.0467  -0.0525 -0.0188 176 ASP A CA  
1403  C C   . ASP A 176 ? 0.4303 0.2003 1.8162 0.0502  -0.0429 -0.0225 176 ASP A C   
1404  O O   . ASP A 176 ? 0.4342 0.2144 1.8247 0.0505  -0.0286 -0.0219 176 ASP A O   
1405  C CB  . ASP A 176 ? 0.4364 0.2107 1.8278 0.0447  -0.0527 -0.0157 176 ASP A CB  
1406  C CG  . ASP A 176 ? 0.4594 0.2064 1.8202 0.0462  -0.0637 -0.0172 176 ASP A CG  
1407  O OD1 . ASP A 176 ? 0.4871 0.2202 1.8361 0.0487  -0.0717 -0.0215 176 ASP A OD1 
1408  O OD2 . ASP A 176 ? 0.4679 0.2066 1.8164 0.0448  -0.0656 -0.0142 176 ASP A OD2 
1409  N N   . TYR A 177 ? 0.4385 0.1866 1.8023 0.0527  -0.0509 -0.0267 177 TYR A N   
1410  C CA  . TYR A 177 ? 0.4654 0.1970 1.8041 0.0561  -0.0425 -0.0312 177 TYR A CA  
1411  C C   . TYR A 177 ? 0.4512 0.1900 1.8044 0.0596  -0.0385 -0.0349 177 TYR A C   
1412  O O   . TYR A 177 ? 0.4592 0.1850 1.7945 0.0633  -0.0315 -0.0397 177 TYR A O   
1413  C CB  . TYR A 177 ? 0.5053 0.2084 1.8132 0.0574  -0.0554 -0.0349 177 TYR A CB  
1414  C CG  . TYR A 177 ? 0.5047 0.2050 1.8239 0.0579  -0.0722 -0.0381 177 TYR A CG  
1415  C CD1 . TYR A 177 ? 0.4976 0.2072 1.8367 0.0551  -0.0857 -0.0356 177 TYR A CD1 
1416  C CD2 . TYR A 177 ? 0.5200 0.2087 1.8314 0.0609  -0.0742 -0.0440 177 TYR A CD2 
1417  C CE1 . TYR A 177 ? 0.5013 0.2102 1.8535 0.0544  -0.1002 -0.0386 177 TYR A CE1 
1418  C CE2 . TYR A 177 ? 0.5286 0.2147 1.8515 0.0603  -0.0893 -0.0468 177 TYR A CE2 
1419  C CZ  . TYR A 177 ? 0.5228 0.2196 1.8669 0.0566  -0.1023 -0.0441 177 TYR A CZ  
1420  O OH  . TYR A 177 ? 0.5195 0.2159 1.8785 0.0547  -0.1171 -0.0470 177 TYR A OH  
1421  N N   . MET A 178 ? 0.4254 0.1822 1.8089 0.0585  -0.0436 -0.0330 178 MET A N   
1422  C CA  . MET A 178 ? 0.4362 0.1924 1.8293 0.0614  -0.0459 -0.0365 178 MET A CA  
1423  C C   . MET A 178 ? 0.4296 0.2021 1.8385 0.0643  -0.0319 -0.0359 178 MET A C   
1424  O O   . MET A 178 ? 0.4179 0.2103 1.8452 0.0620  -0.0265 -0.0312 178 MET A O   
1425  C CB  . MET A 178 ? 0.4182 0.1829 1.8342 0.0582  -0.0587 -0.0347 178 MET A CB  
1426  C CG  . MET A 178 ? 0.4117 0.1768 1.8399 0.0602  -0.0602 -0.0369 178 MET A CG  
1427  S SD  . MET A 178 ? 0.4040 0.1753 1.8554 0.0547  -0.0747 -0.0353 178 MET A SD  
1428  C CE  . MET A 178 ? 0.4338 0.1843 1.8644 0.0533  -0.0894 -0.0396 178 MET A CE  
1429  N N   . ASP A 179 ? 0.4401 0.2035 1.8419 0.0696  -0.0270 -0.0410 179 ASP A N   
1430  C CA  . ASP A 179 ? 0.4214 0.1999 1.8416 0.0736  -0.0164 -0.0410 179 ASP A CA  
1431  C C   . ASP A 179 ? 0.4003 0.1920 1.8471 0.0723  -0.0242 -0.0373 179 ASP A C   
1432  O O   . ASP A 179 ? 0.4045 0.1855 1.8504 0.0714  -0.0351 -0.0386 179 ASP A O   
1433  C CB  . ASP A 179 ? 0.4370 0.2012 1.8436 0.0804  -0.0100 -0.0480 179 ASP A CB  
1434  C CG  . ASP A 179 ? 0.4239 0.2040 1.8506 0.0858  0.0012  -0.0488 179 ASP A CG  
1435  O OD1 . ASP A 179 ? 0.4117 0.2096 1.8494 0.0851  0.0120  -0.0465 179 ASP A OD1 
1436  O OD2 . ASP A 179 ? 0.4259 0.2000 1.8575 0.0908  -0.0015 -0.0520 179 ASP A OD2 
1437  N N   . GLU A 180 ? 0.3840 0.1979 1.8532 0.0715  -0.0189 -0.0327 180 GLU A N   
1438  C CA  . GLU A 180 ? 0.3661 0.1914 1.8578 0.0708  -0.0243 -0.0290 180 GLU A CA  
1439  C C   . GLU A 180 ? 0.3788 0.2137 1.8836 0.0771  -0.0165 -0.0297 180 GLU A C   
1440  O O   . GLU A 180 ? 0.3681 0.2147 1.8915 0.0770  -0.0191 -0.0256 180 GLU A O   
1441  C CB  . GLU A 180 ? 0.3306 0.1735 1.8378 0.0645  -0.0265 -0.0228 180 GLU A CB  
1442  C CG  . GLU A 180 ? 0.3276 0.1637 1.8284 0.0588  -0.0359 -0.0220 180 GLU A CG  
1443  C CD  . GLU A 180 ? 0.3063 0.1599 1.8248 0.0532  -0.0380 -0.0166 180 GLU A CD  
1444  O OE1 . GLU A 180 ? 0.2779 0.1473 1.8111 0.0536  -0.0323 -0.0135 180 GLU A OE1 
1445  O OE2 . GLU A 180 ? 0.3062 0.1570 1.8237 0.0488  -0.0455 -0.0161 180 GLU A OE2 
1446  N N   . SER A 181 ? 0.4001 0.2293 1.8951 0.0829  -0.0070 -0.0350 181 SER A N   
1447  C CA  . SER A 181 ? 0.4068 0.2475 1.9176 0.0896  0.0004  -0.0363 181 SER A CA  
1448  C C   . SER A 181 ? 0.4102 0.2417 1.9268 0.0943  -0.0069 -0.0371 181 SER A C   
1449  O O   . SER A 181 ? 0.4041 0.2456 1.9377 0.0996  -0.0052 -0.0362 181 SER A O   
1450  C CB  . SER A 181 ? 0.4379 0.2763 1.9390 0.0943  0.0138  -0.0424 181 SER A CB  
1451  O OG  . SER A 181 ? 0.4782 0.2921 1.9537 0.0960  0.0127  -0.0481 181 SER A OG  
1452  N N   . ILE A 182 ? 0.4235 0.2355 1.9269 0.0924  -0.0160 -0.0386 182 ILE A N   
1453  C CA  . ILE A 182 ? 0.4329 0.2342 1.9411 0.0960  -0.0229 -0.0391 182 ILE A CA  
1454  C C   . ILE A 182 ? 0.4152 0.2283 1.9421 0.0917  -0.0298 -0.0312 182 ILE A C   
1455  O O   . ILE A 182 ? 0.4289 0.2357 1.9623 0.0950  -0.0342 -0.0301 182 ILE A O   
1456  C CB  . ILE A 182 ? 0.4573 0.2335 1.9466 0.0946  -0.0308 -0.0437 182 ILE A CB  
1457  C CG1 . ILE A 182 ? 0.4715 0.2465 1.9574 0.0852  -0.0399 -0.0404 182 ILE A CG1 
1458  C CG2 . ILE A 182 ? 0.4773 0.2384 1.9449 0.0998  -0.0238 -0.0521 182 ILE A CG2 
1459  C CD1 . ILE A 182 ? 0.5100 0.2619 1.9819 0.0831  -0.0500 -0.0447 182 ILE A CD1 
1460  N N   . PHE A 183 ? 0.3918 0.2201 1.9257 0.0846  -0.0305 -0.0260 183 PHE A N   
1461  C CA  . PHE A 183 ? 0.3758 0.2134 1.9238 0.0793  -0.0365 -0.0189 183 PHE A CA  
1462  C C   . PHE A 183 ? 0.3408 0.1975 1.9046 0.0826  -0.0317 -0.0154 183 PHE A C   
1463  O O   . PHE A 183 ? 0.3501 0.2165 1.9158 0.0863  -0.0235 -0.0181 183 PHE A O   
1464  C CB  . PHE A 183 ? 0.3838 0.2265 1.9314 0.0699  -0.0405 -0.0159 183 PHE A CB  
1465  C CG  . PHE A 183 ? 0.4142 0.2393 1.9485 0.0666  -0.0472 -0.0197 183 PHE A CG  
1466  C CD1 . PHE A 183 ? 0.4460 0.2596 1.9823 0.0632  -0.0555 -0.0191 183 PHE A CD1 
1467  C CD2 . PHE A 183 ? 0.4205 0.2385 1.9392 0.0672  -0.0456 -0.0242 183 PHE A CD2 
1468  C CE1 . PHE A 183 ? 0.4585 0.2564 1.9844 0.0602  -0.0627 -0.0233 183 PHE A CE1 
1469  C CE2 . PHE A 183 ? 0.4469 0.2476 1.9525 0.0649  -0.0534 -0.0282 183 PHE A CE2 
1470  C CZ  . PHE A 183 ? 0.4613 0.2529 1.9718 0.0614  -0.0624 -0.0280 183 PHE A CZ  
1471  N N   . ASP A 184 ? 0.3127 0.1742 1.8870 0.0803  -0.0369 -0.0094 184 ASP A N   
1472  C CA  . ASP A 184 ? 0.2901 0.1686 1.8787 0.0826  -0.0353 -0.0053 184 ASP A CA  
1473  C C   . ASP A 184 ? 0.2748 0.1720 1.8690 0.0762  -0.0319 -0.0026 184 ASP A C   
1474  O O   . ASP A 184 ? 0.2612 0.1746 1.8666 0.0781  -0.0289 -0.0012 184 ASP A O   
1475  C CB  . ASP A 184 ? 0.2880 0.1605 1.8808 0.0821  -0.0427 0.0003  184 ASP A CB  
1476  C CG  . ASP A 184 ? 0.3097 0.1617 1.8969 0.0880  -0.0467 -0.0018 184 ASP A CG  
1477  O OD1 . ASP A 184 ? 0.3239 0.1744 1.9132 0.0976  -0.0433 -0.0065 184 ASP A OD1 
1478  O OD2 . ASP A 184 ? 0.3056 0.1430 1.8872 0.0829  -0.0527 0.0009  184 ASP A OD2 
1479  N N   . VAL A 185 ? 0.2761 0.1713 1.8636 0.0686  -0.0330 -0.0023 185 VAL A N   
1480  C CA  . VAL A 185 ? 0.2511 0.1615 1.8430 0.0627  -0.0303 -0.0001 185 VAL A CA  
1481  C C   . VAL A 185 ? 0.2567 0.1609 1.8371 0.0596  -0.0286 -0.0036 185 VAL A C   
1482  O O   . VAL A 185 ? 0.2712 0.1598 1.8414 0.0596  -0.0326 -0.0062 185 VAL A O   
1483  C CB  . VAL A 185 ? 0.2372 0.1514 1.8348 0.0561  -0.0355 0.0055  185 VAL A CB  
1484  C CG1 . VAL A 185 ? 0.2269 0.1529 1.8273 0.0493  -0.0337 0.0070  185 VAL A CG1 
1485  C CG2 . VAL A 185 ? 0.2386 0.1586 1.8445 0.0588  -0.0374 0.0097  185 VAL A CG2 
1486  N N   . TYR A 186 ? 0.2624 0.1775 1.8436 0.0571  -0.0235 -0.0036 186 TYR A N   
1487  C CA  . TYR A 186 ? 0.2688 0.1775 1.8384 0.0536  -0.0233 -0.0055 186 TYR A CA  
1488  C C   . TYR A 186 ? 0.2470 0.1592 1.8219 0.0467  -0.0292 -0.0023 186 TYR A C   
1489  O O   . TYR A 186 ? 0.2322 0.1579 1.8183 0.0436  -0.0284 0.0012  186 TYR A O   
1490  C CB  . TYR A 186 ? 0.2751 0.1918 1.8425 0.0540  -0.0143 -0.0068 186 TYR A CB  
1491  C CG  . TYR A 186 ? 0.2934 0.2052 1.8546 0.0605  -0.0068 -0.0113 186 TYR A CG  
1492  C CD1 . TYR A 186 ? 0.3200 0.2130 1.8652 0.0639  -0.0081 -0.0155 186 TYR A CD1 
1493  C CD2 . TYR A 186 ? 0.3024 0.2285 1.8745 0.0632  0.0016  -0.0120 186 TYR A CD2 
1494  C CE1 . TYR A 186 ? 0.3510 0.2386 1.8897 0.0701  -0.0003 -0.0203 186 TYR A CE1 
1495  C CE2 . TYR A 186 ? 0.3388 0.2617 1.9076 0.0694  0.0096  -0.0169 186 TYR A CE2 
1496  C CZ  . TYR A 186 ? 0.3594 0.2626 1.9109 0.0731  0.0093  -0.0212 186 TYR A CZ  
1497  O OH  . TYR A 186 ? 0.3531 0.2518 1.9001 0.0796  0.0182  -0.0269 186 TYR A OH  
1498  N N   . ALA A 187 ? 0.2529 0.1532 1.8202 0.0443  -0.0354 -0.0040 187 ALA A N   
1499  C CA  . ALA A 187 ? 0.2433 0.1482 1.8186 0.0380  -0.0405 -0.0019 187 ALA A CA  
1500  C C   . ALA A 187 ? 0.2544 0.1495 1.8208 0.0363  -0.0458 -0.0048 187 ALA A C   
1501  O O   . ALA A 187 ? 0.2582 0.1387 1.8109 0.0394  -0.0483 -0.0083 187 ALA A O   
1502  C CB  . ALA A 187 ? 0.2399 0.1431 1.8235 0.0358  -0.0449 -0.0001 187 ALA A CB  
1503  N N   . TYR A 188 ? 0.2757 0.1786 1.8494 0.0319  -0.0477 -0.0035 188 TYR A N   
1504  C CA  . TYR A 188 ? 0.2908 0.1865 1.8579 0.0309  -0.0533 -0.0058 188 TYR A CA  
1505  C C   . TYR A 188 ? 0.2702 0.1759 1.8531 0.0259  -0.0568 -0.0048 188 TYR A C   
1506  O O   . TYR A 188 ? 0.2522 0.1715 1.8465 0.0232  -0.0518 -0.0021 188 TYR A O   
1507  C CB  . TYR A 188 ? 0.3075 0.2007 1.8620 0.0324  -0.0492 -0.0058 188 TYR A CB  
1508  C CG  . TYR A 188 ? 0.3440 0.2257 1.8802 0.0369  -0.0444 -0.0077 188 TYR A CG  
1509  C CD1 . TYR A 188 ? 0.3796 0.2426 1.8989 0.0394  -0.0503 -0.0112 188 TYR A CD1 
1510  C CD2 . TYR A 188 ? 0.3464 0.2359 1.8829 0.0387  -0.0340 -0.0066 188 TYR A CD2 
1511  C CE1 . TYR A 188 ? 0.4133 0.2647 1.9146 0.0436  -0.0448 -0.0137 188 TYR A CE1 
1512  C CE2 . TYR A 188 ? 0.3825 0.2625 1.9041 0.0429  -0.0281 -0.0092 188 TYR A CE2 
1513  C CZ  . TYR A 188 ? 0.4171 0.2774 1.9200 0.0454  -0.0329 -0.0128 188 TYR A CZ  
1514  O OH  . TYR A 188 ? 0.4299 0.2789 1.9158 0.0494  -0.0263 -0.0160 188 TYR A OH  
1515  N N   . ASN A 189 ? 0.2931 0.1916 1.8764 0.0250  -0.0656 -0.0076 189 ASN A N   
1516  C CA  . ASN A 189 ? 0.2876 0.1947 1.8861 0.0213  -0.0695 -0.0082 189 ASN A CA  
1517  C C   . ASN A 189 ? 0.3286 0.2336 1.9189 0.0231  -0.0699 -0.0081 189 ASN A C   
1518  O O   . ASN A 189 ? 0.4008 0.2914 1.9756 0.0261  -0.0757 -0.0099 189 ASN A O   
1519  C CB  . ASN A 189 ? 0.2860 0.1871 1.8920 0.0198  -0.0798 -0.0118 189 ASN A CB  
1520  C CG  . ASN A 189 ? 0.2833 0.1860 1.8994 0.0165  -0.0793 -0.0117 189 ASN A CG  
1521  O OD1 . ASN A 189 ? 0.2717 0.1844 1.8960 0.0137  -0.0719 -0.0084 189 ASN A OD1 
1522  N ND2 . ASN A 189 ? 0.2863 0.1780 1.9014 0.0162  -0.0879 -0.0151 189 ASN A ND2 
1523  N N   . CYS A 190 ? 0.3175 0.2349 1.9163 0.0210  -0.0639 -0.0061 190 CYS A N   
1524  C CA  . CYS A 190 ? 0.3243 0.2390 1.9143 0.0222  -0.0625 -0.0053 190 CYS A CA  
1525  C C   . CYS A 190 ? 0.3069 0.2262 1.9099 0.0209  -0.0679 -0.0070 190 CYS A C   
1526  O O   . CYS A 190 ? 0.2729 0.2060 1.8939 0.0177  -0.0650 -0.0072 190 CYS A O   
1527  C CB  . CYS A 190 ? 0.3089 0.2324 1.8970 0.0213  -0.0516 -0.0023 190 CYS A CB  
1528  S SG  . CYS A 190 ? 0.3344 0.2544 1.9126 0.0239  -0.0460 -0.0015 190 CYS A SG  
1529  N N   . TYR A 191 ? 0.3052 0.2122 1.8982 0.0237  -0.0754 -0.0082 191 TYR A N   
1530  C CA  . TYR A 191 ? 0.2854 0.1955 1.8912 0.0239  -0.0817 -0.0102 191 TYR A CA  
1531  C C   . TYR A 191 ? 0.2671 0.1653 1.8565 0.0264  -0.0831 -0.0087 191 TYR A C   
1532  O O   . TYR A 191 ? 0.2705 0.1512 1.8379 0.0291  -0.0874 -0.0080 191 TYR A O   
1533  C CB  . TYR A 191 ? 0.3005 0.2076 1.9174 0.0251  -0.0944 -0.0144 191 TYR A CB  
1534  C CG  . TYR A 191 ? 0.2879 0.2081 1.9257 0.0212  -0.0926 -0.0162 191 TYR A CG  
1535  C CD1 . TYR A 191 ? 0.2677 0.2045 1.9291 0.0178  -0.0884 -0.0176 191 TYR A CD1 
1536  C CD2 . TYR A 191 ? 0.3020 0.2169 1.9341 0.0205  -0.0935 -0.0163 191 TYR A CD2 
1537  C CE1 . TYR A 191 ? 0.2640 0.2114 1.9422 0.0132  -0.0851 -0.0186 191 TYR A CE1 
1538  C CE2 . TYR A 191 ? 0.3037 0.2285 1.9529 0.0162  -0.0910 -0.0171 191 TYR A CE2 
1539  C CZ  . TYR A 191 ? 0.2904 0.2312 1.9622 0.0122  -0.0867 -0.0181 191 TYR A CZ  
1540  O OH  . TYR A 191 ? 0.2995 0.2481 1.9858 0.0070  -0.0832 -0.0185 191 TYR A OH  
1541  N N   . ASP A 192 ? 0.2526 0.1591 1.8526 0.0251  -0.0798 -0.0085 192 ASP A N   
1542  C CA  . ASP A 192 ? 0.2604 0.1567 1.8466 0.0263  -0.0791 -0.0065 192 ASP A CA  
1543  C C   . ASP A 192 ? 0.2633 0.1543 1.8574 0.0296  -0.0903 -0.0091 192 ASP A C   
1544  O O   . ASP A 192 ? 0.2407 0.1432 1.8535 0.0288  -0.0885 -0.0109 192 ASP A O   
1545  C CB  . ASP A 192 ? 0.2452 0.1537 1.8377 0.0226  -0.0675 -0.0048 192 ASP A CB  
1546  C CG  . ASP A 192 ? 0.2581 0.1558 1.8375 0.0228  -0.0660 -0.0028 192 ASP A CG  
1547  O OD1 . ASP A 192 ? 0.2750 0.1543 1.8391 0.0261  -0.0742 -0.0022 192 ASP A OD1 
1548  O OD2 . ASP A 192 ? 0.2638 0.1703 1.8472 0.0193  -0.0569 -0.0017 192 ASP A OD2 
1549  N N   . HIS A 193 ? 0.2878 0.1604 1.8666 0.0337  -0.1019 -0.0094 193 HIS A N   
1550  C CA  . HIS A 193 ? 0.2982 0.1619 1.8810 0.0382  -0.1153 -0.0116 193 HIS A CA  
1551  C C   . HIS A 193 ? 0.3057 0.1470 1.8605 0.0403  -0.1171 -0.0077 193 HIS A C   
1552  O O   . HIS A 193 ? 0.3208 0.1442 1.8635 0.0449  -0.1304 -0.0079 193 HIS A O   
1553  C CB  . HIS A 193 ? 0.3158 0.1750 1.9034 0.0412  -0.1295 -0.0152 193 HIS A CB  
1554  C CG  . HIS A 193 ? 0.3195 0.1982 1.9332 0.0381  -0.1274 -0.0188 193 HIS A CG  
1555  N ND1 . HIS A 193 ? 0.3340 0.2110 1.9419 0.0365  -0.1276 -0.0192 193 HIS A ND1 
1556  C CD2 . HIS A 193 ? 0.3213 0.2202 1.9661 0.0361  -0.1249 -0.0223 193 HIS A CD2 
1557  C CE1 . HIS A 193 ? 0.3183 0.2130 1.9525 0.0332  -0.1256 -0.0223 193 HIS A CE1 
1558  N NE2 . HIS A 193 ? 0.3142 0.2227 1.9710 0.0327  -0.1235 -0.0242 193 HIS A NE2 
1559  N N   . ASN A 194 ? 0.3056 0.1465 1.8483 0.0366  -0.1040 -0.0039 194 ASN A N   
1560  C CA  . ASN A 194 ? 0.3189 0.1387 1.8351 0.0369  -0.1030 0.0003  194 ASN A CA  
1561  C C   . ASN A 194 ? 0.3433 0.1370 1.8341 0.0416  -0.1165 0.0012  194 ASN A C   
1562  O O   . ASN A 194 ? 0.3569 0.1352 1.8402 0.0452  -0.1264 0.0021  194 ASN A O   
1563  C CB  . ASN A 194 ? 0.3143 0.1372 1.8427 0.0370  -0.1025 0.0001  194 ASN A CB  
1564  C CG  . ASN A 194 ? 0.3506 0.1508 1.8519 0.0364  -0.1007 0.0048  194 ASN A CG  
1565  O OD1 . ASN A 194 ? 0.3882 0.1864 1.8751 0.0313  -0.0879 0.0081  194 ASN A OD1 
1566  N ND2 . ASN A 194 ? 0.3665 0.1484 1.8601 0.0413  -0.1134 0.0051  194 ASN A ND2 
1567  N N   . GLU A 195 ? 0.3523 0.1395 1.8284 0.0418  -0.1175 0.0010  195 GLU A N   
1568  C CA  . GLU A 195 ? 0.3869 0.1489 1.8375 0.0461  -0.1313 0.0011  195 GLU A CA  
1569  C C   . GLU A 195 ? 0.4115 0.1648 1.8384 0.0443  -0.1244 0.0018  195 GLU A C   
1570  O O   . GLU A 195 ? 0.3971 0.1676 1.8350 0.0408  -0.1117 0.0012  195 GLU A O   
1571  C CB  . GLU A 195 ? 0.3775 0.1457 1.8497 0.0504  -0.1482 -0.0041 195 GLU A CB  
1572  C CG  . GLU A 195 ? 0.3481 0.1355 1.8407 0.0483  -0.1457 -0.0080 195 GLU A CG  
1573  C CD  . GLU A 195 ? 0.3417 0.1338 1.8548 0.0515  -0.1623 -0.0135 195 GLU A CD  
1574  O OE1 . GLU A 195 ? 0.3556 0.1397 1.8724 0.0561  -0.1766 -0.0149 195 GLU A OE1 
1575  O OE2 . GLU A 195 ? 0.3259 0.1295 1.8524 0.0495  -0.1616 -0.0166 195 GLU A OE2 
1576  N N   . GLY A 196 ? 0.4558 0.1819 1.8502 0.0471  -0.1335 0.0027  196 GLY A N   
1577  C CA  . GLY A 196 ? 0.4737 0.1885 1.8421 0.0458  -0.1261 0.0028  196 GLY A CA  
1578  C C   . GLY A 196 ? 0.4651 0.1899 1.8314 0.0405  -0.1043 0.0056  196 GLY A C   
1579  O O   . GLY A 196 ? 0.4623 0.1824 1.8203 0.0378  -0.0962 0.0095  196 GLY A O   
1580  N N   . GLN A 197 ? 0.4561 0.1964 1.8334 0.0391  -0.0952 0.0031  197 GLN A N   
1581  C CA  . GLN A 197 ? 0.4513 0.2037 1.8309 0.0349  -0.0759 0.0048  197 GLN A CA  
1582  C C   . GLN A 197 ? 0.4297 0.2020 1.8343 0.0315  -0.0692 0.0068  197 GLN A C   
1583  O O   . GLN A 197 ? 0.4608 0.2366 1.8612 0.0275  -0.0550 0.0091  197 GLN A O   
1584  C CB  . GLN A 197 ? 0.4362 0.2035 1.8283 0.0351  -0.0696 0.0015  197 GLN A CB  
1585  C CG  . GLN A 197 ? 0.4550 0.2032 1.8213 0.0378  -0.0724 -0.0011 197 GLN A CG  
1586  C CD  . GLN A 197 ? 0.4569 0.1996 1.8275 0.0414  -0.0902 -0.0049 197 GLN A CD  
1587  O OE1 . GLN A 197 ? 0.4363 0.1741 1.8112 0.0430  -0.1044 -0.0048 197 GLN A OE1 
1588  N NE2 . GLN A 197 ? 0.4676 0.2109 1.8382 0.0428  -0.0902 -0.0086 197 GLN A NE2 
1589  N N   . THR A 198 ? 0.3990 0.1849 1.8301 0.0327  -0.0782 0.0052  198 THR A N   
1590  C CA  . THR A 198 ? 0.3746 0.1824 1.8313 0.0293  -0.0703 0.0059  198 THR A CA  
1591  C C   . THR A 198 ? 0.3850 0.1834 1.8366 0.0285  -0.0722 0.0084  198 THR A C   
1592  O O   . THR A 198 ? 0.3590 0.1721 1.8287 0.0257  -0.0664 0.0087  198 THR A O   
1593  C CB  . THR A 198 ? 0.3483 0.1777 1.8369 0.0299  -0.0752 0.0025  198 THR A CB  
1594  O OG1 . THR A 198 ? 0.3563 0.1767 1.8473 0.0339  -0.0910 0.0004  198 THR A OG1 
1595  C CG2 . THR A 198 ? 0.3369 0.1772 1.8324 0.0295  -0.0707 0.0008  198 THR A CG2 
1596  N N   . ALA A 199 ? 0.4215 0.1937 1.8468 0.0312  -0.0810 0.0102  199 ALA A N   
1597  C CA  . ALA A 199 ? 0.4359 0.1915 1.8476 0.0308  -0.0829 0.0136  199 ALA A CA  
1598  C C   . ALA A 199 ? 0.4650 0.2056 1.8484 0.0260  -0.0694 0.0178  199 ALA A C   
1599  O O   . ALA A 199 ? 0.4672 0.2009 1.8450 0.0227  -0.0643 0.0210  199 ALA A O   
1600  C CB  . ALA A 199 ? 0.4583 0.1922 1.8564 0.0367  -0.1014 0.0134  199 ALA A CB  
1601  N N   . THR A 200 ? 0.4778 0.2125 1.8436 0.0255  -0.0634 0.0175  200 THR A N   
1602  C CA  . THR A 200 ? 0.5043 0.2267 1.8448 0.0206  -0.0484 0.0206  200 THR A CA  
1603  C C   . THR A 200 ? 0.4790 0.2280 1.8429 0.0153  -0.0319 0.0199  200 THR A C   
1604  O O   . THR A 200 ? 0.4667 0.2160 1.8303 0.0100  -0.0225 0.0225  200 THR A O   
1605  C CB  . THR A 200 ? 0.5312 0.2361 1.8431 0.0225  -0.0475 0.0198  200 THR A CB  
1606  O OG1 . THR A 200 ? 0.5046 0.2304 1.8367 0.0243  -0.0454 0.0153  200 THR A OG1 
1607  C CG2 . THR A 200 ? 0.5601 0.2361 1.8453 0.0275  -0.0652 0.0206  200 THR A CG2 
1608  N N   . MET A 201 ? 0.4627 0.2332 1.8470 0.0167  -0.0292 0.0163  201 MET A N   
1609  C CA  . MET A 201 ? 0.4541 0.2473 1.8566 0.0123  -0.0141 0.0156  201 MET A CA  
1610  C C   . MET A 201 ? 0.4424 0.2582 1.8760 0.0107  -0.0157 0.0149  201 MET A C   
1611  O O   . MET A 201 ? 0.4665 0.2965 1.9126 0.0058  -0.0052 0.0153  201 MET A O   
1612  C CB  . MET A 201 ? 0.4303 0.2330 1.8369 0.0149  -0.0101 0.0123  201 MET A CB  
1613  C CG  . MET A 201 ? 0.4560 0.2365 1.8304 0.0158  -0.0052 0.0123  201 MET A CG  
1614  S SD  . MET A 201 ? 0.4545 0.2377 1.8287 0.0212  -0.0068 0.0076  201 MET A SD  
1615  C CE  . MET A 201 ? 0.4798 0.2437 1.8408 0.0267  -0.0280 0.0064  201 MET A CE  
1616  N N   . GLY A 202 ? 0.4300 0.2482 1.8756 0.0145  -0.0289 0.0135  202 GLY A N   
1617  C CA  . GLY A 202 ? 0.3985 0.2390 1.8736 0.0134  -0.0299 0.0118  202 GLY A CA  
1618  C C   . GLY A 202 ? 0.3672 0.2264 1.8599 0.0150  -0.0290 0.0092  202 GLY A C   
1619  O O   . GLY A 202 ? 0.4035 0.2597 1.8869 0.0164  -0.0257 0.0087  202 GLY A O   
1620  N N   . PHE A 203 ? 0.3278 0.2046 1.8445 0.0147  -0.0320 0.0075  203 PHE A N   
1621  C CA  . PHE A 203 ? 0.2937 0.1848 1.8256 0.0163  -0.0333 0.0055  203 PHE A CA  
1622  C C   . PHE A 203 ? 0.2867 0.1901 1.8222 0.0141  -0.0222 0.0061  203 PHE A C   
1623  O O   . PHE A 203 ? 0.2987 0.1999 1.8283 0.0164  -0.0206 0.0054  203 PHE A O   
1624  C CB  . PHE A 203 ? 0.2613 0.1651 1.8150 0.0159  -0.0385 0.0037  203 PHE A CB  
1625  C CG  . PHE A 203 ? 0.2414 0.1545 1.8083 0.0174  -0.0426 0.0017  203 PHE A CG  
1626  C CD1 . PHE A 203 ? 0.2480 0.1505 1.8063 0.0207  -0.0494 0.0007  203 PHE A CD1 
1627  C CD2 . PHE A 203 ? 0.2175 0.1485 1.8037 0.0150  -0.0396 0.0010  203 PHE A CD2 
1628  C CE1 . PHE A 203 ? 0.2440 0.1540 1.8148 0.0213  -0.0529 -0.0011 203 PHE A CE1 
1629  C CE2 . PHE A 203 ? 0.2105 0.1480 1.8074 0.0155  -0.0426 -0.0003 203 PHE A CE2 
1630  C CZ  . PHE A 203 ? 0.2300 0.1573 1.8201 0.0184  -0.0491 -0.0013 203 PHE A CZ  
1631  N N   . LYS A 204 ? 0.2710 0.1866 1.8163 0.0100  -0.0150 0.0068  204 LYS A N   
1632  C CA  . LYS A 204 ? 0.2657 0.1946 1.8177 0.0083  -0.0057 0.0069  204 LYS A CA  
1633  C C   . LYS A 204 ? 0.2806 0.1997 1.8166 0.0100  0.0002  0.0070  204 LYS A C   
1634  O O   . LYS A 204 ? 0.2968 0.2215 1.8364 0.0128  0.0019  0.0058  204 LYS A O   
1635  C CB  . LYS A 204 ? 0.2628 0.2006 1.8216 0.0030  0.0012  0.0076  204 LYS A CB  
1636  C CG  . LYS A 204 ? 0.2529 0.2065 1.8222 0.0009  0.0095  0.0072  204 LYS A CG  
1637  C CD  . LYS A 204 ? 0.2685 0.2203 1.8325 -0.0039 0.0191  0.0077  204 LYS A CD  
1638  C CE  . LYS A 204 ? 0.2614 0.2315 1.8430 -0.0086 0.0233  0.0069  204 LYS A CE  
1639  N NZ  . LYS A 204 ? 0.2672 0.2382 1.8472 -0.0137 0.0337  0.0068  204 LYS A NZ  
1640  N N   . ASP A 205 ? 0.2974 0.2008 1.8148 0.0082  0.0038  0.0083  205 ASP A N   
1641  C CA  . ASP A 205 ? 0.3189 0.2137 1.8205 0.0086  0.0126  0.0080  205 ASP A CA  
1642  C C   . ASP A 205 ? 0.3385 0.2199 1.8259 0.0140  0.0071  0.0066  205 ASP A C   
1643  O O   . ASP A 205 ? 0.3546 0.2365 1.8377 0.0160  0.0139  0.0048  205 ASP A O   
1644  C CB  . ASP A 205 ? 0.3424 0.2201 1.8236 0.0046  0.0183  0.0102  205 ASP A CB  
1645  C CG  . ASP A 205 ? 0.3326 0.2219 1.8255 -0.0020 0.0270  0.0112  205 ASP A CG  
1646  O OD1 . ASP A 205 ? 0.3021 0.2123 1.8187 -0.0027 0.0260  0.0100  205 ASP A OD1 
1647  O OD2 . ASP A 205 ? 0.3530 0.2293 1.8300 -0.0064 0.0345  0.0130  205 ASP A OD2 
1648  N N   . TYR A 206 ? 0.3446 0.2140 1.8253 0.0166  -0.0053 0.0067  206 TYR A N   
1649  C CA  . TYR A 206 ? 0.3628 0.2186 1.8301 0.0213  -0.0122 0.0048  206 TYR A CA  
1650  C C   . TYR A 206 ? 0.3407 0.2102 1.8222 0.0239  -0.0101 0.0024  206 TYR A C   
1651  O O   . TYR A 206 ? 0.3395 0.2030 1.8098 0.0261  -0.0042 0.0007  206 TYR A O   
1652  C CB  . TYR A 206 ? 0.3575 0.2051 1.8251 0.0237  -0.0275 0.0043  206 TYR A CB  
1653  C CG  . TYR A 206 ? 0.3797 0.2139 1.8348 0.0280  -0.0356 0.0017  206 TYR A CG  
1654  C CD1 . TYR A 206 ? 0.4093 0.2242 1.8367 0.0296  -0.0321 0.0011  206 TYR A CD1 
1655  C CD2 . TYR A 206 ? 0.3743 0.2143 1.8447 0.0300  -0.0464 -0.0004 206 TYR A CD2 
1656  C CE1 . TYR A 206 ? 0.4339 0.2349 1.8482 0.0334  -0.0403 -0.0019 206 TYR A CE1 
1657  C CE2 . TYR A 206 ? 0.4001 0.2273 1.8597 0.0333  -0.0547 -0.0032 206 TYR A CE2 
1658  C CZ  . TYR A 206 ? 0.4315 0.2389 1.8627 0.0352  -0.0522 -0.0041 206 TYR A CZ  
1659  O OH  . TYR A 206 ? 0.4835 0.2776 1.9036 0.0383  -0.0610 -0.0074 206 TYR A OH  
1660  N N   . ILE A 207 ? 0.3211 0.2078 1.8262 0.0234  -0.0143 0.0025  207 ILE A N   
1661  C CA  . ILE A 207 ? 0.3286 0.2282 1.8488 0.0255  -0.0137 0.0012  207 ILE A CA  
1662  C C   . ILE A 207 ? 0.3633 0.2731 1.8877 0.0255  -0.0017 0.0008  207 ILE A C   
1663  O O   . ILE A 207 ? 0.3960 0.3050 1.9189 0.0293  0.0010  -0.0012 207 ILE A O   
1664  C CB  . ILE A 207 ? 0.3174 0.2324 1.8594 0.0234  -0.0186 0.0021  207 ILE A CB  
1665  C CG1 . ILE A 207 ? 0.3195 0.2271 1.8624 0.0235  -0.0301 0.0015  207 ILE A CG1 
1666  C CG2 . ILE A 207 ? 0.3125 0.2396 1.8684 0.0249  -0.0176 0.0018  207 ILE A CG2 
1667  C CD1 . ILE A 207 ? 0.3312 0.2238 1.8628 0.0269  -0.0381 -0.0007 207 ILE A CD1 
1668  N N   . LYS A 208 ? 0.3685 0.2879 1.8991 0.0214  0.0054  0.0023  208 LYS A N   
1669  C CA  . LYS A 208 ? 0.3703 0.3020 1.9090 0.0210  0.0163  0.0014  208 LYS A CA  
1670  C C   . LYS A 208 ? 0.3867 0.3064 1.9085 0.0238  0.0241  -0.0008 208 LYS A C   
1671  O O   . LYS A 208 ? 0.3687 0.2975 1.8989 0.0265  0.0309  -0.0031 208 LYS A O   
1672  C CB  . LYS A 208 ? 0.3699 0.3099 1.9147 0.0151  0.0222  0.0030  208 LYS A CB  
1673  C CG  . LYS A 208 ? 0.3879 0.3438 1.9460 0.0139  0.0326  0.0016  208 LYS A CG  
1674  C CD  . LYS A 208 ? 0.3881 0.3540 1.9558 0.0073  0.0367  0.0028  208 LYS A CD  
1675  C CE  . LYS A 208 ? 0.4483 0.3991 1.9976 0.0030  0.0440  0.0037  208 LYS A CE  
1676  N NZ  . LYS A 208 ? 0.4952 0.4495 2.0441 0.0020  0.0574  0.0016  208 LYS A NZ  
1677  N N   . GLY A 209 ? 0.4069 0.3054 1.9043 0.0233  0.0229  -0.0005 209 GLY A N   
1678  C CA  . GLY A 209 ? 0.4262 0.3096 1.9021 0.0251  0.0310  -0.0027 209 GLY A CA  
1679  C C   . GLY A 209 ? 0.4271 0.3035 1.8980 0.0313  0.0263  -0.0059 209 GLY A C   
1680  O O   . GLY A 209 ? 0.4202 0.2894 1.8795 0.0340  0.0347  -0.0091 209 GLY A O   
1681  N N   . LEU A 210 ? 0.4409 0.3182 1.9200 0.0333  0.0134  -0.0055 210 LEU A N   
1682  C CA  . LEU A 210 ? 0.4659 0.3377 1.9437 0.0385  0.0082  -0.0085 210 LEU A CA  
1683  C C   . LEU A 210 ? 0.4510 0.3411 1.9500 0.0413  0.0142  -0.0098 210 LEU A C   
1684  O O   . LEU A 210 ? 0.4505 0.3365 1.9456 0.0460  0.0186  -0.0133 210 LEU A O   
1685  C CB  . LEU A 210 ? 0.4619 0.3293 1.9433 0.0386  -0.0067 -0.0078 210 LEU A CB  
1686  C CG  . LEU A 210 ? 0.5095 0.3584 1.9715 0.0372  -0.0151 -0.0071 210 LEU A CG  
1687  C CD1 . LEU A 210 ? 0.5339 0.3818 2.0050 0.0373  -0.0296 -0.0073 210 LEU A CD1 
1688  C CD2 . LEU A 210 ? 0.5391 0.3645 1.9705 0.0396  -0.0134 -0.0097 210 LEU A CD2 
1689  N N   . ASN A 211 ? 0.4300 0.3397 1.9509 0.0385  0.0144  -0.0071 211 ASN A N   
1690  C CA  . ASN A 211 ? 0.4032 0.3309 1.9449 0.0410  0.0186  -0.0077 211 ASN A CA  
1691  C C   . ASN A 211 ? 0.4291 0.3605 1.9700 0.0429  0.0320  -0.0109 211 ASN A C   
1692  O O   . ASN A 211 ? 0.4296 0.3666 1.9795 0.0483  0.0351  -0.0137 211 ASN A O   
1693  C CB  . ASN A 211 ? 0.3735 0.3191 1.9343 0.0368  0.0161  -0.0044 211 ASN A CB  
1694  C CG  . ASN A 211 ? 0.3685 0.3261 1.9470 0.0399  0.0119  -0.0038 211 ASN A CG  
1695  O OD1 . ASN A 211 ? 0.4269 0.3762 2.0026 0.0435  0.0058  -0.0043 211 ASN A OD1 
1696  N ND2 . ASN A 211 ? 0.3547 0.3303 1.9504 0.0384  0.0145  -0.0026 211 ASN A ND2 
1697  N N   . GLU A 212 ? 0.4165 0.3447 1.9473 0.0383  0.0402  -0.0105 212 GLU A N   
1698  C CA  . GLU A 212 ? 0.3950 0.3253 1.9233 0.0386  0.0549  -0.0137 212 GLU A CA  
1699  C C   . GLU A 212 ? 0.3969 0.3077 1.9029 0.0434  0.0586  -0.0178 212 GLU A C   
1700  O O   . GLU A 212 ? 0.3845 0.3001 1.8958 0.0476  0.0681  -0.0221 212 GLU A O   
1701  C CB  . GLU A 212 ? 0.4185 0.3464 1.9382 0.0311  0.0621  -0.0115 212 GLU A CB  
1702  C CG  . GLU A 212 ? 0.4137 0.3622 1.9568 0.0261  0.0609  -0.0088 212 GLU A CG  
1703  C CD  . GLU A 212 ? 0.4078 0.3526 1.9433 0.0181  0.0659  -0.0062 212 GLU A CD  
1704  O OE1 . GLU A 212 ? 0.4275 0.3517 1.9372 0.0159  0.0695  -0.0054 212 GLU A OE1 
1705  O OE2 . GLU A 212 ? 0.3813 0.3430 1.9363 0.0140  0.0653  -0.0049 212 GLU A OE2 
1706  N N   . LEU A 213 ? 0.4083 0.2967 1.8894 0.0432  0.0510  -0.0171 213 LEU A N   
1707  C CA  . LEU A 213 ? 0.4310 0.2997 1.8896 0.0480  0.0531  -0.0215 213 LEU A CA  
1708  C C   . LEU A 213 ? 0.4279 0.3019 1.9006 0.0550  0.0484  -0.0247 213 LEU A C   
1709  O O   . LEU A 213 ? 0.4335 0.3003 1.8984 0.0601  0.0554  -0.0298 213 LEU A O   
1710  C CB  . LEU A 213 ? 0.4368 0.2797 1.8658 0.0467  0.0434  -0.0204 213 LEU A CB  
1711  C CG  . LEU A 213 ? 0.4417 0.2686 1.8445 0.0416  0.0497  -0.0185 213 LEU A CG  
1712  C CD1 . LEU A 213 ? 0.4605 0.2638 1.8391 0.0417  0.0349  -0.0172 213 LEU A CD1 
1713  C CD2 . LEU A 213 ? 0.4557 0.2724 1.8389 0.0418  0.0665  -0.0223 213 LEU A CD2 
1714  N N   . ASN A 214 ? 0.4153 0.3008 1.9078 0.0552  0.0371  -0.0216 214 ASN A N   
1715  C CA  . ASN A 214 ? 0.4276 0.3155 1.9320 0.0611  0.0311  -0.0234 214 ASN A CA  
1716  C C   . ASN A 214 ? 0.4199 0.3235 1.9430 0.0661  0.0409  -0.0265 214 ASN A C   
1717  O O   . ASN A 214 ? 0.4361 0.3345 1.9605 0.0728  0.0402  -0.0302 214 ASN A O   
1718  C CB  . ASN A 214 ? 0.4224 0.3178 1.9416 0.0589  0.0181  -0.0189 214 ASN A CB  
1719  C CG  . ASN A 214 ? 0.4572 0.3354 1.9608 0.0565  0.0067  -0.0181 214 ASN A CG  
1720  O OD1 . ASN A 214 ? 0.4814 0.3403 1.9621 0.0578  0.0066  -0.0212 214 ASN A OD1 
1721  N ND2 . ASN A 214 ? 0.4485 0.3332 1.9639 0.0530  -0.0028 -0.0143 214 ASN A ND2 
1722  N N   . GLY A 215 ? 0.3949 0.3176 1.9342 0.0632  0.0492  -0.0253 215 GLY A N   
1723  C CA  . GLY A 215 ? 0.3878 0.3265 1.9463 0.0680  0.0593  -0.0292 215 GLY A CA  
1724  C C   . GLY A 215 ? 0.3444 0.3081 1.9329 0.0672  0.0562  -0.0263 215 GLY A C   
1725  O O   . GLY A 215 ? 0.3348 0.3141 1.9432 0.0716  0.0626  -0.0295 215 GLY A O   
1726  N N   . LEU A 216 ? 0.3077 0.2746 1.8992 0.0621  0.0459  -0.0207 216 LEU A N   
1727  C CA  . LEU A 216 ? 0.2807 0.2687 1.8957 0.0601  0.0421  -0.0177 216 LEU A CA  
1728  C C   . LEU A 216 ? 0.2833 0.2817 1.9177 0.0681  0.0395  -0.0195 216 LEU A C   
1729  O O   . LEU A 216 ? 0.2962 0.3138 1.9515 0.0690  0.0429  -0.0206 216 LEU A O   
1730  C CB  . LEU A 216 ? 0.2733 0.2752 1.8966 0.0543  0.0523  -0.0182 216 LEU A CB  
1731  C CG  . LEU A 216 ? 0.2722 0.2621 1.8753 0.0465  0.0561  -0.0164 216 LEU A CG  
1732  C CD1 . LEU A 216 ? 0.2674 0.2702 1.8802 0.0421  0.0689  -0.0183 216 LEU A CD1 
1733  C CD2 . LEU A 216 ? 0.2528 0.2394 1.8516 0.0411  0.0453  -0.0112 216 LEU A CD2 
1734  N N   . ASP A 217 ? 0.2979 0.2831 1.9255 0.0739  0.0326  -0.0199 217 ASP A N   
1735  C CA  . ASP A 217 ? 0.3004 0.2907 1.9431 0.0827  0.0298  -0.0218 217 ASP A CA  
1736  C C   . ASP A 217 ? 0.2956 0.2782 1.9370 0.0837  0.0161  -0.0170 217 ASP A C   
1737  O O   . ASP A 217 ? 0.3055 0.2853 1.9538 0.0912  0.0115  -0.0178 217 ASP A O   
1738  C CB  . ASP A 217 ? 0.3303 0.3091 1.9649 0.0898  0.0377  -0.0284 217 ASP A CB  
1739  C CG  . ASP A 217 ? 0.3600 0.3146 1.9659 0.0877  0.0380  -0.0296 217 ASP A CG  
1740  O OD1 . ASP A 217 ? 0.3775 0.3244 1.9719 0.0812  0.0305  -0.0250 217 ASP A OD1 
1741  O OD2 . ASP A 217 ? 0.3867 0.3302 1.9819 0.0925  0.0456  -0.0354 217 ASP A OD2 
1742  N N   . LYS A 218 ? 0.2820 0.2597 1.9141 0.0761  0.0099  -0.0122 218 LYS A N   
1743  C CA  . LYS A 218 ? 0.2821 0.2511 1.9113 0.0756  -0.0013 -0.0078 218 LYS A CA  
1744  C C   . LYS A 218 ? 0.2627 0.2377 1.8917 0.0668  -0.0054 -0.0030 218 LYS A C   
1745  O O   . LYS A 218 ? 0.2819 0.2598 1.9062 0.0614  -0.0008 -0.0034 218 LYS A O   
1746  C CB  . LYS A 218 ? 0.2949 0.2419 1.9066 0.0762  -0.0049 -0.0091 218 LYS A CB  
1747  C CG  . LYS A 218 ? 0.3231 0.2586 1.9265 0.0830  0.0008  -0.0153 218 LYS A CG  
1748  C CD  . LYS A 218 ? 0.3545 0.2672 1.9412 0.0837  -0.0048 -0.0168 218 LYS A CD  
1749  C CE  . LYS A 218 ? 0.3973 0.3017 1.9846 0.0932  -0.0027 -0.0217 218 LYS A CE  
1750  N NZ  . LYS A 218 ? 0.4293 0.3108 1.9975 0.0944  -0.0049 -0.0257 218 LYS A NZ  
1751  N N   . PRO A 219 ? 0.2439 0.2194 1.8766 0.0651  -0.0137 0.0017  219 PRO A N   
1752  C CA  . PRO A 219 ? 0.2421 0.2218 1.8735 0.0569  -0.0166 0.0055  219 PRO A CA  
1753  C C   . PRO A 219 ? 0.2562 0.2242 1.8743 0.0522  -0.0162 0.0045  219 PRO A C   
1754  O O   . PRO A 219 ? 0.2497 0.2028 1.8582 0.0545  -0.0178 0.0025  219 PRO A O   
1755  C CB  . PRO A 219 ? 0.2434 0.2200 1.8768 0.0569  -0.0247 0.0102  219 PRO A CB  
1756  C CG  . PRO A 219 ? 0.2417 0.2190 1.8826 0.0657  -0.0262 0.0092  219 PRO A CG  
1757  C CD  . PRO A 219 ? 0.2459 0.2158 1.8824 0.0708  -0.0202 0.0036  219 PRO A CD  
1758  N N   . PHE A 220 ? 0.2784 0.2524 1.8959 0.0458  -0.0147 0.0055  220 PHE A N   
1759  C CA  . PHE A 220 ? 0.2978 0.2614 1.9046 0.0418  -0.0162 0.0047  220 PHE A CA  
1760  C C   . PHE A 220 ? 0.2610 0.2274 1.8716 0.0358  -0.0211 0.0079  220 PHE A C   
1761  O O   . PHE A 220 ? 0.2372 0.2156 1.8552 0.0327  -0.0202 0.0099  220 PHE A O   
1762  C CB  . PHE A 220 ? 0.3245 0.2890 1.9254 0.0406  -0.0096 0.0024  220 PHE A CB  
1763  C CG  . PHE A 220 ? 0.4027 0.3590 1.9942 0.0361  -0.0121 0.0023  220 PHE A CG  
1764  C CD1 . PHE A 220 ? 0.4843 0.4241 2.0618 0.0376  -0.0149 0.0001  220 PHE A CD1 
1765  C CD2 . PHE A 220 ? 0.4255 0.3901 2.0223 0.0307  -0.0123 0.0042  220 PHE A CD2 
1766  C CE1 . PHE A 220 ? 0.4620 0.3946 2.0322 0.0342  -0.0189 0.0000  220 PHE A CE1 
1767  C CE2 . PHE A 220 ? 0.4181 0.3753 2.0081 0.0276  -0.0153 0.0039  220 PHE A CE2 
1768  C CZ  . PHE A 220 ? 0.4305 0.3721 2.0079 0.0296  -0.0190 0.0019  220 PHE A CZ  
1769  N N   . ILE A 221 ? 0.2486 0.2040 1.8546 0.0341  -0.0261 0.0078  221 ILE A N   
1770  C CA  . ILE A 221 ? 0.2363 0.1943 1.8471 0.0282  -0.0293 0.0098  221 ILE A CA  
1771  C C   . ILE A 221 ? 0.2414 0.1921 1.8480 0.0257  -0.0322 0.0073  221 ILE A C   
1772  O O   . ILE A 221 ? 0.2567 0.1962 1.8544 0.0287  -0.0338 0.0046  221 ILE A O   
1773  C CB  . ILE A 221 ? 0.2291 0.1832 1.8427 0.0274  -0.0330 0.0125  221 ILE A CB  
1774  C CG1 . ILE A 221 ? 0.2303 0.1691 1.8385 0.0292  -0.0371 0.0107  221 ILE A CG1 
1775  C CG2 . ILE A 221 ? 0.2326 0.1929 1.8494 0.0308  -0.0319 0.0152  221 ILE A CG2 
1776  C CD1 . ILE A 221 ? 0.2278 0.1604 1.8378 0.0277  -0.0402 0.0137  221 ILE A CD1 
1777  N N   . THR A 222 ? 0.2354 0.1924 1.8485 0.0206  -0.0329 0.0079  222 THR A N   
1778  C CA  . THR A 222 ? 0.2417 0.1930 1.8555 0.0183  -0.0374 0.0056  222 THR A CA  
1779  C C   . THR A 222 ? 0.2486 0.1978 1.8696 0.0150  -0.0408 0.0061  222 THR A C   
1780  O O   . THR A 222 ? 0.2450 0.2006 1.8719 0.0119  -0.0383 0.0089  222 THR A O   
1781  C CB  . THR A 222 ? 0.2317 0.1908 1.8504 0.0151  -0.0360 0.0051  222 THR A CB  
1782  O OG1 . THR A 222 ? 0.2248 0.1946 1.8518 0.0115  -0.0328 0.0074  222 THR A OG1 
1783  C CG2 . THR A 222 ? 0.2317 0.1907 1.8425 0.0172  -0.0326 0.0047  222 THR A CG2 
1784  N N   . THR A 223 ? 0.2667 0.2060 1.8866 0.0152  -0.0466 0.0033  223 THR A N   
1785  C CA  . THR A 223 ? 0.2613 0.1977 1.8892 0.0113  -0.0499 0.0031  223 THR A CA  
1786  C C   . THR A 223 ? 0.2816 0.2231 1.9217 0.0070  -0.0528 0.0004  223 THR A C   
1787  O O   . THR A 223 ? 0.3144 0.2582 1.9655 0.0020  -0.0531 0.0002  223 THR A O   
1788  C CB  . THR A 223 ? 0.2590 0.1805 1.8784 0.0146  -0.0550 0.0011  223 THR A CB  
1789  O OG1 . THR A 223 ? 0.2446 0.1599 1.8524 0.0193  -0.0567 -0.0015 223 THR A OG1 
1790  C CG2 . THR A 223 ? 0.2619 0.1794 1.8760 0.0173  -0.0521 0.0039  223 THR A CG2 
1791  N N   . GLU A 224 ? 0.2938 0.2370 1.9328 0.0089  -0.0546 -0.0018 224 GLU A N   
1792  C CA  . GLU A 224 ? 0.3053 0.2554 1.9583 0.0058  -0.0570 -0.0045 224 GLU A CA  
1793  C C   . GLU A 224 ? 0.2658 0.2189 1.9152 0.0082  -0.0561 -0.0050 224 GLU A C   
1794  O O   . GLU A 224 ? 0.2602 0.2064 1.8949 0.0121  -0.0560 -0.0041 224 GLU A O   
1795  C CB  . GLU A 224 ? 0.3355 0.2789 1.9951 0.0056  -0.0666 -0.0088 224 GLU A CB  
1796  C CG  . GLU A 224 ? 0.3507 0.2918 2.0190 0.0014  -0.0683 -0.0095 224 GLU A CG  
1797  C CD  . GLU A 224 ? 0.3883 0.3244 2.0661 0.0006  -0.0789 -0.0147 224 GLU A CD  
1798  O OE1 . GLU A 224 ? 0.4337 0.3589 2.1070 0.0005  -0.0841 -0.0159 224 GLU A OE1 
1799  O OE2 . GLU A 224 ? 0.4101 0.3528 2.1006 0.0005  -0.0829 -0.0180 224 GLU A OE2 
1800  N N   . PHE A 225 ? 0.2497 0.2122 1.9126 0.0056  -0.0551 -0.0067 225 PHE A N   
1801  C CA  . PHE A 225 ? 0.2314 0.1940 1.8928 0.0080  -0.0567 -0.0081 225 PHE A CA  
1802  C C   . PHE A 225 ? 0.2098 0.1838 1.8901 0.0051  -0.0550 -0.0110 225 PHE A C   
1803  O O   . PHE A 225 ? 0.1969 0.1807 1.8850 0.0007  -0.0476 -0.0101 225 PHE A O   
1804  C CB  . PHE A 225 ? 0.2135 0.1759 1.8612 0.0095  -0.0505 -0.0050 225 PHE A CB  
1805  C CG  . PHE A 225 ? 0.1918 0.1657 1.8436 0.0059  -0.0418 -0.0026 225 PHE A CG  
1806  C CD1 . PHE A 225 ? 0.1844 0.1589 1.8312 0.0055  -0.0384 0.0004  225 PHE A CD1 
1807  C CD2 . PHE A 225 ? 0.1851 0.1678 1.8444 0.0035  -0.0377 -0.0035 225 PHE A CD2 
1808  C CE1 . PHE A 225 ? 0.1812 0.1648 1.8299 0.0026  -0.0322 0.0028  225 PHE A CE1 
1809  C CE2 . PHE A 225 ? 0.1747 0.1663 1.8349 0.0002  -0.0307 -0.0016 225 PHE A CE2 
1810  C CZ  . PHE A 225 ? 0.1734 0.1653 1.8281 -0.0003 -0.0285 0.0017  225 PHE A CZ  
1811  N N   . GLY A 226 ? 0.2111 0.1831 1.8979 0.0077  -0.0617 -0.0145 226 GLY A N   
1812  C CA  . GLY A 226 ? 0.2043 0.1874 1.9108 0.0059  -0.0598 -0.0181 226 GLY A CA  
1813  C C   . GLY A 226 ? 0.1954 0.1749 1.9115 0.0101  -0.0703 -0.0226 226 GLY A C   
1814  O O   . GLY A 226 ? 0.1972 0.1636 1.8995 0.0148  -0.0786 -0.0219 226 GLY A O   
1815  N N   . TYR A 227 ? 0.1914 0.1823 1.9313 0.0086  -0.0699 -0.0273 227 TYR A N   
1816  C CA  . TYR A 227 ? 0.2117 0.2007 1.9625 0.0136  -0.0793 -0.0317 227 TYR A CA  
1817  C C   . TYR A 227 ? 0.2017 0.2043 1.9834 0.0116  -0.0806 -0.0380 227 TYR A C   
1818  O O   . TYR A 227 ? 0.2071 0.2223 2.0011 0.0057  -0.0697 -0.0389 227 TYR A O   
1819  C CB  . TYR A 227 ? 0.2115 0.2000 1.9585 0.0162  -0.0757 -0.0318 227 TYR A CB  
1820  C CG  . TYR A 227 ? 0.2207 0.1950 1.9391 0.0183  -0.0754 -0.0263 227 TYR A CG  
1821  C CD1 . TYR A 227 ? 0.2368 0.1943 1.9394 0.0233  -0.0863 -0.0249 227 TYR A CD1 
1822  C CD2 . TYR A 227 ? 0.2227 0.1999 1.9295 0.0150  -0.0643 -0.0227 227 TYR A CD2 
1823  C CE1 . TYR A 227 ? 0.2481 0.1923 1.9246 0.0244  -0.0845 -0.0201 227 TYR A CE1 
1824  C CE2 . TYR A 227 ? 0.2312 0.1970 1.9151 0.0162  -0.0633 -0.0183 227 TYR A CE2 
1825  C CZ  . TYR A 227 ? 0.2412 0.1904 1.9098 0.0207  -0.0725 -0.0170 227 TYR A CZ  
1826  O OH  . TYR A 227 ? 0.2265 0.1641 1.8723 0.0211  -0.0700 -0.0128 227 TYR A OH  
1827  N N   . SER A 228 ? 0.2041 0.2035 1.9977 0.0163  -0.0941 -0.0423 228 SER A N   
1828  C CA  . SER A 228 ? 0.1930 0.2065 2.0199 0.0146  -0.0968 -0.0492 228 SER A CA  
1829  C C   . SER A 228 ? 0.1937 0.2165 2.0415 0.0184  -0.0962 -0.0546 228 SER A C   
1830  O O   . SER A 228 ? 0.1856 0.1987 2.0226 0.0248  -0.1019 -0.0539 228 SER A O   
1831  C CB  . SER A 228 ? 0.1934 0.1998 2.0249 0.0170  -0.1128 -0.0516 228 SER A CB  
1832  O OG  . SER A 228 ? 0.1903 0.2115 2.0578 0.0162  -0.1169 -0.0592 228 SER A OG  
1833  N N   . VAL A 229 ? 0.1929 0.2341 2.0710 0.0142  -0.0886 -0.0604 229 VAL A N   
1834  C CA  . VAL A 229 ? 0.1936 0.2456 2.0943 0.0175  -0.0857 -0.0668 229 VAL A CA  
1835  C C   . VAL A 229 ? 0.1826 0.2455 2.1190 0.0201  -0.0961 -0.0750 229 VAL A C   
1836  O O   . VAL A 229 ? 0.1978 0.2764 2.1633 0.0204  -0.0900 -0.0821 229 VAL A O   
1837  C CB  . VAL A 229 ? 0.1891 0.2542 2.0958 0.0112  -0.0660 -0.0679 229 VAL A CB  
1838  C CG1 . VAL A 229 ? 0.1849 0.2401 2.0577 0.0087  -0.0573 -0.0601 229 VAL A CG1 
1839  C CG2 . VAL A 229 ? 0.1857 0.2654 2.1129 0.0024  -0.0568 -0.0706 229 VAL A CG2 
1840  N N   . SER A 230 ? 0.1771 0.2312 2.1114 0.0226  -0.1123 -0.0747 230 SER A N   
1841  C CA  . SER A 230 ? 0.1826 0.2476 2.1526 0.0251  -0.1243 -0.0830 230 SER A CA  
1842  C C   . SER A 230 ? 0.1970 0.2663 2.1866 0.0341  -0.1306 -0.0890 230 SER A C   
1843  O O   . SER A 230 ? 0.2065 0.2625 2.1753 0.0404  -0.1332 -0.0857 230 SER A O   
1844  C CB  . SER A 230 ? 0.1864 0.2388 2.1482 0.0271  -0.1429 -0.0820 230 SER A CB  
1845  O OG  . SER A 230 ? 0.1930 0.2220 2.1187 0.0338  -0.1534 -0.0760 230 SER A OG  
1846  N N   . PRO A 231 ? 0.1950 0.2840 2.2276 0.0345  -0.1320 -0.0985 231 PRO A N   
1847  C CA  . PRO A 231 ? 0.2072 0.3013 2.2638 0.0442  -0.1402 -0.1055 231 PRO A CA  
1848  C C   . PRO A 231 ? 0.2309 0.3025 2.2669 0.0548  -0.1629 -0.1024 231 PRO A C   
1849  O O   . PRO A 231 ? 0.2388 0.3017 2.2692 0.0633  -0.1672 -0.1026 231 PRO A O   
1850  C CB  . PRO A 231 ? 0.2057 0.3237 2.3126 0.0425  -0.1425 -0.1161 231 PRO A CB  
1851  C CG  . PRO A 231 ? 0.1988 0.3275 2.3082 0.0291  -0.1265 -0.1145 231 PRO A CG  
1852  C CD  . PRO A 231 ? 0.1990 0.3066 2.2600 0.0252  -0.1242 -0.1030 231 PRO A CD  
1853  N N   . GLU A 232 ? 0.2313 0.2923 2.2554 0.0540  -0.1772 -0.0998 232 GLU A N   
1854  C CA  . GLU A 232 ? 0.2583 0.2951 2.2578 0.0629  -0.1990 -0.0963 232 GLU A CA  
1855  C C   . GLU A 232 ? 0.2615 0.2839 2.2323 0.0582  -0.2046 -0.0906 232 GLU A C   
1856  O O   . GLU A 232 ? 0.2424 0.2726 2.2111 0.0486  -0.1907 -0.0886 232 GLU A O   
1857  C CB  . GLU A 232 ? 0.2726 0.3140 2.3046 0.0727  -0.2198 -0.1047 232 GLU A CB  
1858  C CG  . GLU A 232 ? 0.2788 0.3385 2.3488 0.0690  -0.2281 -0.1126 232 GLU A CG  
1859  C CD  . GLU A 232 ? 0.3009 0.3726 2.4141 0.0780  -0.2460 -0.1228 232 GLU A CD  
1860  O OE1 . GLU A 232 ? 0.3264 0.3922 2.4448 0.0810  -0.2679 -0.1253 232 GLU A OE1 
1861  O OE2 . GLU A 232 ? 0.2998 0.3876 2.4430 0.0820  -0.2384 -0.1290 232 GLU A OE2 
1862  N N   . GLY A 233 ? 0.2896 0.2889 2.2360 0.0651  -0.2247 -0.0878 233 GLY A N   
1863  C CA  . GLY A 233 ? 0.3020 0.2859 2.2230 0.0622  -0.2336 -0.0842 233 GLY A CA  
1864  C C   . GLY A 233 ? 0.3097 0.2744 2.1832 0.0595  -0.2226 -0.0743 233 GLY A C   
1865  O O   . GLY A 233 ? 0.3099 0.2783 2.1757 0.0574  -0.2058 -0.0706 233 GLY A O   
1866  N N   . GLY A 234 ? 0.3299 0.2750 2.1732 0.0592  -0.2321 -0.0707 234 GLY A N   
1867  C CA  . GLY A 234 ? 0.3300 0.2571 2.1299 0.0568  -0.2224 -0.0622 234 GLY A CA  
1868  C C   . GLY A 234 ? 0.3602 0.2608 2.1257 0.0645  -0.2329 -0.0575 234 GLY A C   
1869  O O   . GLY A 234 ? 0.3717 0.2584 2.1330 0.0710  -0.2535 -0.0598 234 GLY A O   
1870  N N   . ASN A 235 ? 0.3800 0.2730 2.1209 0.0636  -0.2189 -0.0511 235 ASN A N   
1871  C CA  . ASN A 235 ? 0.4169 0.2830 2.1209 0.0689  -0.2254 -0.0455 235 ASN A CA  
1872  C C   . ASN A 235 ? 0.3967 0.2623 2.0832 0.0653  -0.2056 -0.0395 235 ASN A C   
1873  O O   . ASN A 235 ? 0.3907 0.2655 2.0733 0.0586  -0.1900 -0.0372 235 ASN A O   
1874  C CB  . ASN A 235 ? 0.4720 0.3143 2.1417 0.0697  -0.2363 -0.0430 235 ASN A CB  
1875  C CG  . ASN A 235 ? 0.5267 0.3394 2.1543 0.0740  -0.2404 -0.0366 235 ASN A CG  
1876  O OD1 . ASN A 235 ? 0.5475 0.3526 2.1757 0.0796  -0.2472 -0.0359 235 ASN A OD1 
1877  N ND2 . ASN A 235 ? 0.5680 0.3633 2.1589 0.0713  -0.2357 -0.0321 235 ASN A ND2 
1878  N N   . GLY A 236 ? 0.3855 0.2390 2.0610 0.0699  -0.2077 -0.0369 236 GLY A N   
1879  C CA  . GLY A 236 ? 0.3852 0.2381 2.0471 0.0666  -0.1906 -0.0320 236 GLY A CA  
1880  C C   . GLY A 236 ? 0.3599 0.2406 2.0479 0.0600  -0.1728 -0.0343 236 GLY A C   
1881  O O   . GLY A 236 ? 0.3289 0.2289 2.0515 0.0605  -0.1729 -0.0403 236 GLY A O   
1882  N N   . GLN A 237 ? 0.3819 0.2636 2.0523 0.0539  -0.1574 -0.0295 237 GLN A N   
1883  C CA  . GLN A 237 ? 0.3740 0.2788 2.0635 0.0476  -0.1412 -0.0307 237 GLN A CA  
1884  C C   . GLN A 237 ? 0.3691 0.2873 2.0757 0.0441  -0.1417 -0.0339 237 GLN A C   
1885  O O   . GLN A 237 ? 0.3301 0.2675 2.0558 0.0389  -0.1302 -0.0356 237 GLN A O   
1886  C CB  . GLN A 237 ? 0.3593 0.2600 2.0248 0.0430  -0.1268 -0.0247 237 GLN A CB  
1887  C CG  . GLN A 237 ? 0.3709 0.2640 2.0275 0.0443  -0.1229 -0.0226 237 GLN A CG  
1888  C CD  . GLN A 237 ? 0.3709 0.2648 2.0108 0.0388  -0.1077 -0.0178 237 GLN A CD  
1889  O OE1 . GLN A 237 ? 0.3399 0.2514 1.9928 0.0341  -0.0961 -0.0187 237 GLN A OE1 
1890  N NE2 . GLN A 237 ? 0.3987 0.2730 2.0094 0.0392  -0.1080 -0.0129 237 GLN A NE2 
1891  N N   . TYR A 238 ? 0.3999 0.3067 2.0982 0.0464  -0.1550 -0.0347 238 TYR A N   
1892  C CA  . TYR A 238 ? 0.4490 0.3664 2.1627 0.0425  -0.1560 -0.0378 238 TYR A CA  
1893  C C   . TYR A 238 ? 0.4197 0.3524 2.1712 0.0441  -0.1645 -0.0452 238 TYR A C   
1894  O O   . TYR A 238 ? 0.4223 0.3466 2.1776 0.0496  -0.1817 -0.0484 238 TYR A O   
1895  C CB  . TYR A 238 ? 0.4759 0.3759 2.1664 0.0434  -0.1656 -0.0365 238 TYR A CB  
1896  C CG  . TYR A 238 ? 0.4604 0.3704 2.1706 0.0396  -0.1693 -0.0408 238 TYR A CG  
1897  C CD1 . TYR A 238 ? 0.4661 0.3881 2.1825 0.0329  -0.1556 -0.0396 238 TYR A CD1 
1898  C CD2 . TYR A 238 ? 0.4982 0.4049 2.2208 0.0425  -0.1872 -0.0461 238 TYR A CD2 
1899  C CE1 . TYR A 238 ? 0.4604 0.3892 2.1929 0.0286  -0.1585 -0.0431 238 TYR A CE1 
1900  C CE2 . TYR A 238 ? 0.5249 0.4403 2.2663 0.0381  -0.1905 -0.0504 238 TYR A CE2 
1901  C CZ  . TYR A 238 ? 0.5009 0.4268 2.2467 0.0309  -0.1756 -0.0487 238 TYR A CZ  
1902  O OH  . TYR A 238 ? 0.5038 0.4368 2.2678 0.0258  -0.1784 -0.0526 238 TYR A OH  
1903  N N   . GLY A 239 ? 0.3923 0.3471 2.1706 0.0392  -0.1518 -0.0479 239 GLY A N   
1904  C CA  . GLY A 239 ? 0.3753 0.3480 2.1925 0.0400  -0.1551 -0.0554 239 GLY A CA  
1905  C C   . GLY A 239 ? 0.3493 0.3256 2.1753 0.0445  -0.1520 -0.0570 239 GLY A C   
1906  O O   . GLY A 239 ? 0.3612 0.3227 2.1617 0.0476  -0.1512 -0.0523 239 GLY A O   
1907  N N   . SER A 240 ? 0.3196 0.3160 2.1825 0.0440  -0.1488 -0.0641 240 SER A N   
1908  C CA  . SER A 240 ? 0.2859 0.2867 2.1662 0.0501  -0.1506 -0.0686 240 SER A CA  
1909  C C   . SER A 240 ? 0.2776 0.2754 2.1405 0.0489  -0.1361 -0.0647 240 SER A C   
1910  O O   . SER A 240 ? 0.2882 0.2793 2.1508 0.0552  -0.1400 -0.0659 240 SER A O   
1911  C CB  . SER A 240 ? 0.2856 0.2703 2.1620 0.0597  -0.1723 -0.0697 240 SER A CB  
1912  O OG  . SER A 240 ? 0.2661 0.2579 2.1656 0.0603  -0.1856 -0.0752 240 SER A OG  
1913  N N   . ASN A 241 ? 0.2756 0.2782 2.1254 0.0410  -0.1199 -0.0604 241 ASN A N   
1914  C CA  . ASN A 241 ? 0.2857 0.2884 2.1234 0.0390  -0.1060 -0.0579 241 ASN A CA  
1915  C C   . ASN A 241 ? 0.2533 0.2765 2.1202 0.0364  -0.0938 -0.0648 241 ASN A C   
1916  O O   . ASN A 241 ? 0.2563 0.2951 2.1467 0.0322  -0.0901 -0.0689 241 ASN A O   
1917  C CB  . ASN A 241 ? 0.3082 0.3084 2.1207 0.0320  -0.0944 -0.0510 241 ASN A CB  
1918  C CG  . ASN A 241 ? 0.3452 0.3254 2.1258 0.0338  -0.1019 -0.0442 241 ASN A CG  
1919  O OD1 . ASN A 241 ? 0.3898 0.3583 2.1490 0.0352  -0.0997 -0.0402 241 ASN A OD1 
1920  N ND2 . ASN A 241 ? 0.3624 0.3380 2.1388 0.0334  -0.1098 -0.0431 241 ASN A ND2 
1921  N N   . THR A 242 ? 0.2137 0.2360 2.0774 0.0379  -0.0864 -0.0658 242 THR A N   
1922  C CA  . THR A 242 ? 0.1983 0.2378 2.0831 0.0346  -0.0720 -0.0719 242 THR A CA  
1923  C C   . THR A 242 ? 0.1756 0.2207 2.0460 0.0251  -0.0566 -0.0676 242 THR A C   
1924  O O   . THR A 242 ? 0.2078 0.2422 2.0514 0.0227  -0.0576 -0.0601 242 THR A O   
1925  C CB  . THR A 242 ? 0.2172 0.2514 2.1006 0.0394  -0.0697 -0.0747 242 THR A CB  
1926  O OG1 . THR A 242 ? 0.2634 0.2784 2.1128 0.0399  -0.0730 -0.0668 242 THR A OG1 
1927  C CG2 . THR A 242 ? 0.2156 0.2505 2.1247 0.0489  -0.0816 -0.0820 242 THR A CG2 
1928  N N   . LEU A 243 ? 0.1493 0.2101 2.0362 0.0200  -0.0424 -0.0725 243 LEU A N   
1929  C CA  . LEU A 243 ? 0.1320 0.1966 2.0036 0.0111  -0.0280 -0.0685 243 LEU A CA  
1930  C C   . LEU A 243 ? 0.1384 0.1911 1.9805 0.0110  -0.0251 -0.0632 243 LEU A C   
1931  O O   . LEU A 243 ? 0.1251 0.1747 1.9463 0.0058  -0.0199 -0.0570 243 LEU A O   
1932  C CB  . LEU A 243 ? 0.1187 0.1997 2.0109 0.0058  -0.0130 -0.0752 243 LEU A CB  
1933  C CG  . LEU A 243 ? 0.1165 0.2118 2.0420 0.0046  -0.0139 -0.0814 243 LEU A CG  
1934  C CD1 . LEU A 243 ? 0.1147 0.2261 2.0645 0.0015  0.0012  -0.0903 243 LEU A CD1 
1935  C CD2 . LEU A 243 ? 0.1097 0.2059 2.0312 -0.0023 -0.0140 -0.0764 243 LEU A CD2 
1936  N N   . LYS A 244 ? 0.1473 0.1929 1.9884 0.0169  -0.0290 -0.0657 244 LYS A N   
1937  C CA  . LYS A 244 ? 0.1619 0.1968 1.9772 0.0158  -0.0259 -0.0612 244 LYS A CA  
1938  C C   . LYS A 244 ? 0.1668 0.1886 1.9587 0.0163  -0.0343 -0.0527 244 LYS A C   
1939  O O   . LYS A 244 ? 0.1475 0.1661 1.9189 0.0117  -0.0289 -0.0473 244 LYS A O   
1940  C CB  . LYS A 244 ? 0.1700 0.1978 1.9880 0.0215  -0.0280 -0.0656 244 LYS A CB  
1941  C CG  . LYS A 244 ? 0.1716 0.1865 1.9628 0.0199  -0.0263 -0.0606 244 LYS A CG  
1942  C CD  . LYS A 244 ? 0.1840 0.1925 1.9781 0.0238  -0.0255 -0.0658 244 LYS A CD  
1943  C CE  . LYS A 244 ? 0.2012 0.1951 1.9707 0.0222  -0.0258 -0.0611 244 LYS A CE  
1944  N NZ  . LYS A 244 ? 0.1966 0.1937 1.9482 0.0141  -0.0170 -0.0568 244 LYS A NZ  
1945  N N   . GLN A 245 ? 0.1720 0.1859 1.9674 0.0221  -0.0476 -0.0523 245 GLN A N   
1946  C CA  . GLN A 245 ? 0.1803 0.1793 1.9523 0.0234  -0.0554 -0.0452 245 GLN A CA  
1947  C C   . GLN A 245 ? 0.1766 0.1803 1.9400 0.0177  -0.0511 -0.0406 245 GLN A C   
1948  O O   . GLN A 245 ? 0.1778 0.1737 1.9191 0.0158  -0.0494 -0.0347 245 GLN A O   
1949  C CB  . GLN A 245 ? 0.1924 0.1811 1.9679 0.0303  -0.0710 -0.0458 245 GLN A CB  
1950  C CG  . GLN A 245 ? 0.2053 0.1819 1.9804 0.0372  -0.0788 -0.0478 245 GLN A CG  
1951  C CD  . GLN A 245 ? 0.2360 0.2068 2.0225 0.0444  -0.0950 -0.0503 245 GLN A CD  
1952  O OE1 . GLN A 245 ? 0.2773 0.2599 2.0832 0.0438  -0.0979 -0.0537 245 GLN A OE1 
1953  N NE2 . GLN A 245 ? 0.2626 0.2145 2.0368 0.0509  -0.1065 -0.0486 245 GLN A NE2 
1954  N N   . GLN A 246 ? 0.1717 0.1876 1.9537 0.0151  -0.0490 -0.0437 246 GLN A N   
1955  C CA  . GLN A 246 ? 0.1733 0.1926 1.9487 0.0097  -0.0451 -0.0397 246 GLN A CA  
1956  C C   . GLN A 246 ? 0.1573 0.1789 1.9170 0.0043  -0.0335 -0.0358 246 GLN A C   
1957  O O   . GLN A 246 ? 0.1706 0.1861 1.9120 0.0031  -0.0338 -0.0301 246 GLN A O   
1958  C CB  . GLN A 246 ? 0.1817 0.2142 1.9818 0.0065  -0.0425 -0.0444 246 GLN A CB  
1959  C CG  . GLN A 246 ? 0.1842 0.2179 1.9796 0.0013  -0.0405 -0.0406 246 GLN A CG  
1960  C CD  . GLN A 246 ? 0.1896 0.2375 2.0061 -0.0048 -0.0313 -0.0447 246 GLN A CD  
1961  O OE1 . GLN A 246 ? 0.2119 0.2683 2.0360 -0.0071 -0.0211 -0.0480 246 GLN A OE1 
1962  N NE2 . GLN A 246 ? 0.1845 0.2343 2.0110 -0.0076 -0.0347 -0.0450 246 GLN A NE2 
1963  N N   . SER A 247 ? 0.1452 0.1758 1.9127 0.0013  -0.0238 -0.0394 247 SER A N   
1964  C CA  . SER A 247 ? 0.1399 0.1728 1.8934 -0.0038 -0.0138 -0.0368 247 SER A CA  
1965  C C   . SER A 247 ? 0.1634 0.1861 1.8960 -0.0021 -0.0167 -0.0321 247 SER A C   
1966  O O   . SER A 247 ? 0.1559 0.1776 1.8738 -0.0051 -0.0139 -0.0272 247 SER A O   
1967  C CB  . SER A 247 ? 0.1299 0.1712 1.8948 -0.0059 -0.0046 -0.0430 247 SER A CB  
1968  O OG  . SER A 247 ? 0.1215 0.1634 1.8722 -0.0102 0.0039  -0.0419 247 SER A OG  
1969  N N   . ASP A 248 ? 0.1797 0.1941 1.9120 0.0029  -0.0231 -0.0336 248 ASP A N   
1970  C CA  . ASP A 248 ? 0.1871 0.1907 1.9010 0.0039  -0.0251 -0.0298 248 ASP A CA  
1971  C C   . ASP A 248 ? 0.2330 0.2282 1.9333 0.0054  -0.0310 -0.0242 248 ASP A C   
1972  O O   . ASP A 248 ? 0.3272 0.3181 2.0117 0.0037  -0.0288 -0.0199 248 ASP A O   
1973  C CB  . ASP A 248 ? 0.1754 0.1718 1.8930 0.0080  -0.0284 -0.0335 248 ASP A CB  
1974  C CG  . ASP A 248 ? 0.1654 0.1698 1.8905 0.0052  -0.0195 -0.0386 248 ASP A CG  
1975  O OD1 . ASP A 248 ? 0.1752 0.1894 1.8992 -0.0002 -0.0118 -0.0379 248 ASP A OD1 
1976  O OD2 . ASP A 248 ? 0.1335 0.1334 1.8644 0.0083  -0.0205 -0.0431 248 ASP A OD2 
1977  N N   . GLY A 249 ? 0.2314 0.2241 1.9380 0.0085  -0.0385 -0.0246 249 GLY A N   
1978  C CA  . GLY A 249 ? 0.2525 0.2356 1.9442 0.0100  -0.0436 -0.0200 249 GLY A CA  
1979  C C   . GLY A 249 ? 0.2667 0.2561 1.9524 0.0058  -0.0374 -0.0165 249 GLY A C   
1980  O O   . GLY A 249 ? 0.2579 0.2425 1.9282 0.0053  -0.0357 -0.0124 249 GLY A O   
1981  N N   . LEU A 250 ? 0.2490 0.2491 1.9476 0.0027  -0.0336 -0.0183 250 LEU A N   
1982  C CA  . LEU A 250 ? 0.2246 0.2289 1.9179 -0.0009 -0.0290 -0.0148 250 LEU A CA  
1983  C C   . LEU A 250 ? 0.2030 0.2081 1.8829 -0.0028 -0.0235 -0.0115 250 LEU A C   
1984  O O   . LEU A 250 ? 0.1884 0.1916 1.8587 -0.0028 -0.0233 -0.0076 250 LEU A O   
1985  C CB  . LEU A 250 ? 0.2190 0.2334 1.9260 -0.0053 -0.0237 -0.0170 250 LEU A CB  
1986  C CG  . LEU A 250 ? 0.2070 0.2210 1.9222 -0.0059 -0.0276 -0.0172 250 LEU A CG  
1987  C CD1 . LEU A 250 ? 0.2018 0.2090 1.9020 -0.0056 -0.0292 -0.0120 250 LEU A CD1 
1988  C CD2 . LEU A 250 ? 0.2009 0.2110 1.9270 -0.0016 -0.0370 -0.0211 250 LEU A CD2 
1989  N N   . ILE A 251 ? 0.1911 0.1986 1.8717 -0.0040 -0.0199 -0.0135 251 ILE A N   
1990  C CA  . ILE A 251 ? 0.1829 0.1923 1.8533 -0.0064 -0.0153 -0.0113 251 ILE A CA  
1991  C C   . ILE A 251 ? 0.2031 0.2038 1.8621 -0.0040 -0.0181 -0.0087 251 ILE A C   
1992  O O   . ILE A 251 ? 0.1872 0.1891 1.8382 -0.0050 -0.0161 -0.0055 251 ILE A O   
1993  C CB  . ILE A 251 ? 0.1615 0.1755 1.8354 -0.0092 -0.0104 -0.0150 251 ILE A CB  
1994  C CG1 . ILE A 251 ? 0.1419 0.1637 1.8260 -0.0120 -0.0058 -0.0182 251 ILE A CG1 
1995  C CG2 . ILE A 251 ? 0.1678 0.1841 1.8314 -0.0123 -0.0071 -0.0127 251 ILE A CG2 
1996  C CD1 . ILE A 251 ? 0.1414 0.1678 1.8217 -0.0154 -0.0028 -0.0149 251 ILE A CD1 
1997  N N   . SER A 252 ? 0.2178 0.2091 1.8759 -0.0008 -0.0228 -0.0101 252 SER A N   
1998  C CA  . SER A 252 ? 0.2234 0.2037 1.8680 0.0010  -0.0247 -0.0073 252 SER A CA  
1999  C C   . SER A 252 ? 0.2278 0.2043 1.8648 0.0029  -0.0267 -0.0043 252 SER A C   
2000  O O   . SER A 252 ? 0.2241 0.1939 1.8490 0.0035  -0.0256 -0.0019 252 SER A O   
2001  C CB  . SER A 252 ? 0.2330 0.2013 1.8761 0.0044  -0.0305 -0.0089 252 SER A CB  
2002  O OG  . SER A 252 ? 0.2470 0.2017 1.8739 0.0061  -0.0328 -0.0058 252 SER A OG  
2003  N N   . ASN A 253 ? 0.2523 0.2320 1.8965 0.0039  -0.0297 -0.0050 253 ASN A N   
2004  C CA  . ASN A 253 ? 0.2645 0.2405 1.9022 0.0057  -0.0316 -0.0029 253 ASN A CA  
2005  C C   . ASN A 253 ? 0.2643 0.2486 1.9000 0.0035  -0.0254 -0.0003 253 ASN A C   
2006  O O   . ASN A 253 ? 0.2493 0.2304 1.8760 0.0048  -0.0238 0.0017  253 ASN A O   
2007  C CB  . ASN A 253 ? 0.2837 0.2606 1.9312 0.0065  -0.0365 -0.0047 253 ASN A CB  
2008  C CG  . ASN A 253 ? 0.3141 0.2816 1.9633 0.0099  -0.0452 -0.0073 253 ASN A CG  
2009  O OD1 . ASN A 253 ? 0.3455 0.3138 2.0041 0.0104  -0.0502 -0.0093 253 ASN A OD1 
2010  N ND2 . ASN A 253 ? 0.3347 0.2926 1.9750 0.0123  -0.0480 -0.0072 253 ASN A ND2 
2011  N N   . TYR A 254 ? 0.2610 0.2558 1.9053 0.0001  -0.0221 -0.0008 254 TYR A N   
2012  C CA  . TYR A 254 ? 0.2445 0.2465 1.8879 -0.0016 -0.0187 0.0016  254 TYR A CA  
2013  C C   . TYR A 254 ? 0.2347 0.2388 1.8720 -0.0018 -0.0155 0.0031  254 TYR A C   
2014  O O   . TYR A 254 ? 0.2856 0.2906 1.9196 0.0000  -0.0149 0.0051  254 TYR A O   
2015  C CB  . TYR A 254 ? 0.2417 0.2521 1.8919 -0.0057 -0.0156 0.0007  254 TYR A CB  
2016  C CG  . TYR A 254 ? 0.2493 0.2628 1.8981 -0.0069 -0.0148 0.0036  254 TYR A CG  
2017  C CD1 . TYR A 254 ? 0.2366 0.2531 1.8800 -0.0063 -0.0142 0.0064  254 TYR A CD1 
2018  C CD2 . TYR A 254 ? 0.2674 0.2803 1.9211 -0.0087 -0.0149 0.0035  254 TYR A CD2 
2019  C CE1 . TYR A 254 ? 0.2554 0.2727 1.8965 -0.0067 -0.0147 0.0094  254 TYR A CE1 
2020  C CE2 . TYR A 254 ? 0.2682 0.2810 1.9185 -0.0100 -0.0143 0.0068  254 TYR A CE2 
2021  C CZ  . TYR A 254 ? 0.2783 0.2924 1.9214 -0.0086 -0.0147 0.0099  254 TYR A CZ  
2022  O OH  . TYR A 254 ? 0.3318 0.3438 1.9705 -0.0092 -0.0154 0.0135  254 TYR A OH  
2023  N N   . ARG A 255 ? 0.2039 0.2093 1.8414 -0.0041 -0.0134 0.0015  255 ARG A N   
2024  C CA  . ARG A 255 ? 0.2001 0.2072 1.8337 -0.0054 -0.0101 0.0022  255 ARG A CA  
2025  C C   . ARG A 255 ? 0.2099 0.2082 1.8352 -0.0025 -0.0099 0.0035  255 ARG A C   
2026  O O   . ARG A 255 ? 0.2158 0.2179 1.8397 -0.0024 -0.0067 0.0046  255 ARG A O   
2027  C CB  . ARG A 255 ? 0.1998 0.2057 1.8339 -0.0085 -0.0085 0.0000  255 ARG A CB  
2028  C CG  . ARG A 255 ? 0.2072 0.2113 1.8367 -0.0107 -0.0050 0.0004  255 ARG A CG  
2029  C CD  . ARG A 255 ? 0.1953 0.2112 1.8293 -0.0145 -0.0020 0.0003  255 ARG A CD  
2030  N NE  . ARG A 255 ? 0.1807 0.2038 1.8168 -0.0127 -0.0013 0.0023  255 ARG A NE  
2031  C CZ  . ARG A 255 ? 0.1675 0.1999 1.8081 -0.0124 -0.0031 0.0030  255 ARG A CZ  
2032  N NH1 . ARG A 255 ? 0.1537 0.1886 1.7955 -0.0138 -0.0053 0.0024  255 ARG A NH1 
2033  N NH2 . ARG A 255 ? 0.1691 0.2074 1.8128 -0.0103 -0.0026 0.0043  255 ARG A NH2 
2034  N N   . ASP A 256 ? 0.2261 0.2123 1.8455 -0.0002 -0.0132 0.0029  256 ASP A N   
2035  C CA  . ASP A 256 ? 0.2569 0.2321 1.8643 0.0022  -0.0127 0.0041  256 ASP A CA  
2036  C C   . ASP A 256 ? 0.2466 0.2240 1.8528 0.0051  -0.0119 0.0051  256 ASP A C   
2037  O O   . ASP A 256 ? 0.2668 0.2438 1.8677 0.0055  -0.0070 0.0058  256 ASP A O   
2038  C CB  . ASP A 256 ? 0.3029 0.2632 1.9025 0.0047  -0.0185 0.0034  256 ASP A CB  
2039  C CG  . ASP A 256 ? 0.3827 0.3357 1.9786 0.0030  -0.0186 0.0030  256 ASP A CG  
2040  O OD1 . ASP A 256 ? 0.4247 0.3844 2.0310 0.0011  -0.0189 0.0012  256 ASP A OD1 
2041  O OD2 . ASP A 256 ? 0.5168 0.4561 2.0982 0.0034  -0.0179 0.0044  256 ASP A OD2 
2042  N N   . LEU A 257 ? 0.2292 0.2086 1.8406 0.0068  -0.0160 0.0049  257 LEU A N   
2043  C CA  . LEU A 257 ? 0.2277 0.2056 1.8367 0.0101  -0.0165 0.0056  257 LEU A CA  
2044  C C   . LEU A 257 ? 0.2162 0.2055 1.8306 0.0100  -0.0119 0.0068  257 LEU A C   
2045  O O   . LEU A 257 ? 0.2019 0.1895 1.8127 0.0132  -0.0094 0.0068  257 LEU A O   
2046  C CB  . LEU A 257 ? 0.2206 0.1964 1.8344 0.0109  -0.0223 0.0051  257 LEU A CB  
2047  C CG  . LEU A 257 ? 0.2321 0.1961 1.8416 0.0123  -0.0286 0.0033  257 LEU A CG  
2048  C CD1 . LEU A 257 ? 0.2193 0.1859 1.8402 0.0110  -0.0335 0.0019  257 LEU A CD1 
2049  C CD2 . LEU A 257 ? 0.2446 0.1953 1.8410 0.0163  -0.0310 0.0028  257 LEU A CD2 
2050  N N   . ILE A 258 ? 0.2034 0.2041 1.8265 0.0068  -0.0110 0.0073  258 ILE A N   
2051  C CA  . ILE A 258 ? 0.1997 0.2116 1.8286 0.0065  -0.0082 0.0081  258 ILE A CA  
2052  C C   . ILE A 258 ? 0.2080 0.2210 1.8350 0.0062  -0.0025 0.0072  258 ILE A C   
2053  O O   . ILE A 258 ? 0.2118 0.2301 1.8422 0.0087  0.0004  0.0070  258 ILE A O   
2054  C CB  . ILE A 258 ? 0.1917 0.2132 1.8270 0.0023  -0.0090 0.0083  258 ILE A CB  
2055  C CG1 . ILE A 258 ? 0.2011 0.2219 1.8374 0.0021  -0.0126 0.0096  258 ILE A CG1 
2056  C CG2 . ILE A 258 ? 0.1866 0.2199 1.8282 0.0015  -0.0074 0.0085  258 ILE A CG2 
2057  C CD1 . ILE A 258 ? 0.2027 0.2301 1.8416 -0.0025 -0.0126 0.0093  258 ILE A CD1 
2058  N N   . ASP A 259 ? 0.2011 0.2086 1.8231 0.0031  -0.0006 0.0064  259 ASP A N   
2059  C CA  . ASP A 259 ? 0.2234 0.2297 1.8419 0.0013  0.0059  0.0059  259 ASP A CA  
2060  C C   . ASP A 259 ? 0.2425 0.2401 1.8521 0.0056  0.0087  0.0057  259 ASP A C   
2061  O O   . ASP A 259 ? 0.2979 0.2996 1.9089 0.0056  0.0155  0.0049  259 ASP A O   
2062  C CB  . ASP A 259 ? 0.2283 0.2274 1.8413 -0.0029 0.0068  0.0056  259 ASP A CB  
2063  C CG  . ASP A 259 ? 0.2287 0.2365 1.8506 -0.0071 0.0050  0.0048  259 ASP A CG  
2064  O OD1 . ASP A 259 ? 0.2161 0.2372 1.8478 -0.0081 0.0047  0.0045  259 ASP A OD1 
2065  O OD2 . ASP A 259 ? 0.2452 0.2453 1.8633 -0.0091 0.0034  0.0042  259 ASP A OD2 
2066  N N   . ALA A 260 ? 0.2278 0.2139 1.8290 0.0092  0.0037  0.0058  260 ALA A N   
2067  C CA  . ALA A 260 ? 0.2310 0.2075 1.8220 0.0135  0.0058  0.0050  260 ALA A CA  
2068  C C   . ALA A 260 ? 0.2032 0.1895 1.8037 0.0173  0.0073  0.0044  260 ALA A C   
2069  O O   . ALA A 260 ? 0.2061 0.1863 1.7999 0.0211  0.0108  0.0029  260 ALA A O   
2070  C CB  . ALA A 260 ? 0.2479 0.2090 1.8277 0.0159  -0.0014 0.0049  260 ALA A CB  
2071  N N   . GLY A 261 ? 0.1830 0.1823 1.7972 0.0168  0.0041  0.0054  261 GLY A N   
2072  C CA  . GLY A 261 ? 0.1835 0.1929 1.8082 0.0205  0.0043  0.0053  261 GLY A CA  
2073  C C   . GLY A 261 ? 0.1877 0.1934 1.8130 0.0238  -0.0027 0.0067  261 GLY A C   
2074  O O   . GLY A 261 ? 0.1759 0.1835 1.8054 0.0286  -0.0033 0.0065  261 GLY A O   
2075  N N   . ALA A 262 ? 0.1998 0.1997 1.8216 0.0212  -0.0077 0.0079  262 ALA A N   
2076  C CA  . ALA A 262 ? 0.2079 0.2037 1.8304 0.0225  -0.0135 0.0094  262 ALA A CA  
2077  C C   . ALA A 262 ? 0.2088 0.2149 1.8399 0.0221  -0.0155 0.0117  262 ALA A C   
2078  O O   . ALA A 262 ? 0.2287 0.2443 1.8645 0.0183  -0.0146 0.0122  262 ALA A O   
2079  C CB  . ALA A 262 ? 0.2129 0.2026 1.8326 0.0189  -0.0170 0.0094  262 ALA A CB  
2080  N N   . VAL A 263 ? 0.2124 0.2149 1.8439 0.0257  -0.0189 0.0132  263 VAL A N   
2081  C CA  . VAL A 263 ? 0.2047 0.2139 1.8412 0.0254  -0.0222 0.0161  263 VAL A CA  
2082  C C   . VAL A 263 ? 0.1993 0.1998 1.8311 0.0228  -0.0262 0.0188  263 VAL A C   
2083  O O   . VAL A 263 ? 0.1973 0.1987 1.8288 0.0221  -0.0293 0.0221  263 VAL A O   
2084  C CB  . VAL A 263 ? 0.2174 0.2312 1.8599 0.0319  -0.0229 0.0160  263 VAL A CB  
2085  C CG1 . VAL A 263 ? 0.2132 0.2342 1.8610 0.0341  -0.0167 0.0123  263 VAL A CG1 
2086  C CG2 . VAL A 263 ? 0.2272 0.2294 1.8662 0.0374  -0.0263 0.0169  263 VAL A CG2 
2087  N N   . GLY A 264 ? 0.1996 0.1915 1.8275 0.0208  -0.0260 0.0174  264 GLY A N   
2088  C CA  . GLY A 264 ? 0.2065 0.1918 1.8328 0.0168  -0.0283 0.0191  264 GLY A CA  
2089  C C   . GLY A 264 ? 0.2096 0.1923 1.8368 0.0131  -0.0278 0.0164  264 GLY A C   
2090  O O   . GLY A 264 ? 0.2151 0.1926 1.8397 0.0156  -0.0283 0.0136  264 GLY A O   
2091  N N   . MET A 265 ? 0.2119 0.1973 1.8422 0.0075  -0.0270 0.0169  265 MET A N   
2092  C CA  . MET A 265 ? 0.2100 0.1957 1.8447 0.0044  -0.0268 0.0138  265 MET A CA  
2093  C C   . MET A 265 ? 0.2075 0.1891 1.8467 0.0002  -0.0277 0.0139  265 MET A C   
2094  O O   . MET A 265 ? 0.2048 0.1881 1.8440 -0.0037 -0.0254 0.0164  265 MET A O   
2095  C CB  . MET A 265 ? 0.2167 0.2121 1.8544 0.0012  -0.0233 0.0128  265 MET A CB  
2096  C CG  . MET A 265 ? 0.2205 0.2205 1.8554 0.0039  -0.0218 0.0125  265 MET A CG  
2097  S SD  . MET A 265 ? 0.2461 0.2384 1.8769 0.0078  -0.0230 0.0098  265 MET A SD  
2098  C CE  . MET A 265 ? 0.2444 0.2393 1.8798 0.0041  -0.0225 0.0072  265 MET A CE  
2099  N N   . CYS A 266 ? 0.2140 0.1901 1.8567 0.0007  -0.0311 0.0108  266 CYS A N   
2100  C CA  . CYS A 266 ? 0.2179 0.1917 1.8690 -0.0038 -0.0324 0.0094  266 CYS A CA  
2101  C C   . CYS A 266 ? 0.2036 0.1819 1.8645 -0.0050 -0.0337 0.0049  266 CYS A C   
2102  O O   . CYS A 266 ? 0.2097 0.1823 1.8732 -0.0030 -0.0395 0.0019  266 CYS A O   
2103  C CB  . CYS A 266 ? 0.2278 0.1897 1.8757 -0.0018 -0.0373 0.0094  266 CYS A CB  
2104  S SG  . CYS A 266 ? 0.2637 0.2189 1.9017 0.0002  -0.0364 0.0145  266 CYS A SG  
2105  N N   . PRO A 267 ? 0.1822 0.1701 1.8488 -0.0077 -0.0291 0.0039  267 PRO A N   
2106  C CA  . PRO A 267 ? 0.1779 0.1702 1.8566 -0.0085 -0.0306 -0.0008 267 PRO A CA  
2107  C C   . PRO A 267 ? 0.1862 0.1769 1.8776 -0.0113 -0.0338 -0.0034 267 PRO A C   
2108  O O   . PRO A 267 ? 0.1854 0.1745 1.8778 -0.0155 -0.0311 -0.0013 267 PRO A O   
2109  C CB  . PRO A 267 ? 0.1623 0.1645 1.8450 -0.0121 -0.0233 -0.0012 267 PRO A CB  
2110  C CG  . PRO A 267 ? 0.1661 0.1682 1.8390 -0.0147 -0.0187 0.0035  267 PRO A CG  
2111  C CD  . PRO A 267 ? 0.1749 0.1693 1.8367 -0.0098 -0.0232 0.0066  267 PRO A CD  
2112  N N   . PHE A 268 ? 0.1943 0.1848 1.8956 -0.0093 -0.0400 -0.0080 268 PHE A N   
2113  C CA  . PHE A 268 ? 0.2104 0.1988 1.9245 -0.0111 -0.0458 -0.0113 268 PHE A CA  
2114  C C   . PHE A 268 ? 0.2104 0.2105 1.9457 -0.0171 -0.0405 -0.0147 268 PHE A C   
2115  O O   . PHE A 268 ? 0.1651 0.1735 1.9118 -0.0164 -0.0392 -0.0184 268 PHE A O   
2116  C CB  . PHE A 268 ? 0.2217 0.2030 1.9370 -0.0060 -0.0573 -0.0150 268 PHE A CB  
2117  C CG  . PHE A 268 ? 0.2258 0.2060 1.9563 -0.0088 -0.0640 -0.0189 268 PHE A CG  
2118  C CD1 . PHE A 268 ? 0.2268 0.2021 1.9561 -0.0129 -0.0628 -0.0171 268 PHE A CD1 
2119  C CD2 . PHE A 268 ? 0.2303 0.2149 1.9788 -0.0076 -0.0716 -0.0246 268 PHE A CD2 
2120  C CE1 . PHE A 268 ? 0.2409 0.2156 1.9861 -0.0166 -0.0687 -0.0211 268 PHE A CE1 
2121  C CE2 . PHE A 268 ? 0.2398 0.2253 2.0056 -0.0107 -0.0783 -0.0289 268 PHE A CE2 
2122  C CZ  . PHE A 268 ? 0.2393 0.2200 2.0036 -0.0157 -0.0765 -0.0272 268 PHE A CZ  
2123  N N   . TYR A 269 ? 0.2343 0.2335 1.9736 -0.0231 -0.0368 -0.0132 269 TYR A N   
2124  C CA  . TYR A 269 ? 0.2263 0.2330 1.9868 -0.0300 -0.0333 -0.0168 269 TYR A CA  
2125  C C   . TYR A 269 ? 0.2002 0.2180 1.9665 -0.0347 -0.0210 -0.0171 269 TYR A C   
2126  O O   . TYR A 269 ? 0.1861 0.2112 1.9573 -0.0317 -0.0197 -0.0201 269 TYR A O   
2127  C CB  . TYR A 269 ? 0.2505 0.2597 2.0295 -0.0273 -0.0438 -0.0233 269 TYR A CB  
2128  C CG  . TYR A 269 ? 0.2645 0.2756 2.0634 -0.0333 -0.0463 -0.0269 269 TYR A CG  
2129  C CD1 . TYR A 269 ? 0.2805 0.2836 2.0731 -0.0390 -0.0435 -0.0233 269 TYR A CD1 
2130  C CD2 . TYR A 269 ? 0.2628 0.2835 2.0881 -0.0333 -0.0521 -0.0342 269 TYR A CD2 
2131  C CE1 . TYR A 269 ? 0.3164 0.3211 2.1282 -0.0456 -0.0452 -0.0268 269 TYR A CE1 
2132  C CE2 . TYR A 269 ? 0.2746 0.2989 2.1215 -0.0394 -0.0546 -0.0383 269 TYR A CE2 
2133  C CZ  . TYR A 269 ? 0.3182 0.3346 2.1585 -0.0463 -0.0506 -0.0346 269 TYR A CZ  
2134  O OH  . TYR A 269 ? 0.3078 0.3274 2.1702 -0.0537 -0.0522 -0.0387 269 TYR A OH  
2135  N N   . TYR A 270 ? 0.1816 0.1979 1.9438 -0.0420 -0.0122 -0.0136 270 TYR A N   
2136  C CA  . TYR A 270 ? 0.1682 0.1935 1.9392 -0.0495 0.0005  -0.0150 270 TYR A CA  
2137  C C   . TYR A 270 ? 0.1548 0.1936 1.9561 -0.0516 0.0020  -0.0234 270 TYR A C   
2138  O O   . TYR A 270 ? 0.1407 0.1891 1.9497 -0.0501 0.0067  -0.0274 270 TYR A O   
2139  C CB  . TYR A 270 ? 0.1717 0.1882 1.9332 -0.0572 0.0064  -0.0096 270 TYR A CB  
2140  C CG  . TYR A 270 ? 0.1701 0.1921 1.9397 -0.0675 0.0203  -0.0105 270 TYR A CG  
2141  C CD1 . TYR A 270 ? 0.1662 0.1917 1.9254 -0.0699 0.0310  -0.0094 270 TYR A CD1 
2142  C CD2 . TYR A 270 ? 0.1715 0.1936 1.9569 -0.0755 0.0234  -0.0122 270 TYR A CD2 
2143  C CE1 . TYR A 270 ? 0.1716 0.2001 1.9346 -0.0797 0.0451  -0.0102 270 TYR A CE1 
2144  C CE2 . TYR A 270 ? 0.1765 0.2026 1.9679 -0.0858 0.0379  -0.0127 270 TYR A CE2 
2145  C CZ  . TYR A 270 ? 0.1777 0.2065 1.9567 -0.0878 0.0492  -0.0116 270 TYR A CZ  
2146  O OH  . TYR A 270 ? 0.1865 0.2174 1.9672 -0.0982 0.0648  -0.0121 270 TYR A OH  
2147  N N   . ALA A 271 ? 0.1570 0.1970 1.9768 -0.0554 -0.0018 -0.0265 271 ALA A N   
2148  C CA  . ALA A 271 ? 0.1578 0.2125 2.0101 -0.0587 0.0007  -0.0347 271 ALA A CA  
2149  C C   . ALA A 271 ? 0.1583 0.2139 2.0283 -0.0537 -0.0148 -0.0398 271 ALA A C   
2150  O O   . ALA A 271 ? 0.1593 0.2023 2.0153 -0.0501 -0.0257 -0.0367 271 ALA A O   
2151  C CB  . ALA A 271 ? 0.1647 0.2228 2.0272 -0.0705 0.0134  -0.0347 271 ALA A CB  
2152  N N   . ASP A 272 ? 0.1623 0.2324 2.0624 -0.0527 -0.0165 -0.0481 272 ASP A N   
2153  C CA  . ASP A 272 ? 0.1787 0.2500 2.0970 -0.0478 -0.0326 -0.0536 272 ASP A CA  
2154  C C   . ASP A 272 ? 0.2023 0.2705 2.1314 -0.0552 -0.0360 -0.0542 272 ASP A C   
2155  O O   . ASP A 272 ? 0.2179 0.2854 2.1458 -0.0650 -0.0242 -0.0514 272 ASP A O   
2156  C CB  . ASP A 272 ? 0.1887 0.2778 2.1415 -0.0458 -0.0330 -0.0629 272 ASP A CB  
2157  C CG  . ASP A 272 ? 0.2009 0.2939 2.1522 -0.0371 -0.0338 -0.0652 272 ASP A CG  
2158  O OD1 . ASP A 272 ? 0.2146 0.2962 2.1364 -0.0318 -0.0351 -0.0594 272 ASP A OD1 
2159  O OD2 . ASP A 272 ? 0.2123 0.3204 2.1943 -0.0356 -0.0332 -0.0733 272 ASP A OD2 
2160  N N   . GLY A 273 ? 0.2000 0.2646 2.1380 -0.0507 -0.0529 -0.0580 273 GLY A N   
2161  C CA  . GLY A 273 ? 0.1928 0.2539 2.1427 -0.0571 -0.0591 -0.0600 273 GLY A CA  
2162  C C   . GLY A 273 ? 0.1900 0.2595 2.1694 -0.0533 -0.0749 -0.0689 273 GLY A C   
2163  O O   . GLY A 273 ? 0.1782 0.2371 2.1451 -0.0444 -0.0912 -0.0692 273 GLY A O   
2164  N N   . TRP A 274 ? 0.1900 0.2782 2.2080 -0.0602 -0.0698 -0.0762 274 TRP A N   
2165  C CA  . TRP A 274 ? 0.1995 0.3000 2.2520 -0.0563 -0.0841 -0.0859 274 TRP A CA  
2166  C C   . TRP A 274 ? 0.2252 0.3137 2.2764 -0.0559 -0.1033 -0.0876 274 TRP A C   
2167  O O   . TRP A 274 ? 0.2613 0.3559 2.3355 -0.0510 -0.1199 -0.0951 274 TRP A O   
2168  C CB  . TRP A 274 ? 0.1976 0.3224 2.2945 -0.0649 -0.0722 -0.0938 274 TRP A CB  
2169  C CG  . TRP A 274 ? 0.1807 0.3185 2.2825 -0.0645 -0.0543 -0.0944 274 TRP A CG  
2170  C CD1 . TRP A 274 ? 0.1662 0.2950 2.2352 -0.0597 -0.0465 -0.0875 274 TRP A CD1 
2171  C CD2 . TRP A 274 ? 0.1668 0.3286 2.3085 -0.0694 -0.0415 -0.1028 274 TRP A CD2 
2172  N NE1 . TRP A 274 ? 0.1549 0.2988 2.2383 -0.0615 -0.0302 -0.0909 274 TRP A NE1 
2173  C CE2 . TRP A 274 ? 0.1558 0.3199 2.2833 -0.0672 -0.0262 -0.1004 274 TRP A CE2 
2174  C CE3 . TRP A 274 ? 0.1716 0.3536 2.3608 -0.0756 -0.0411 -0.1127 274 TRP A CE3 
2175  C CZ2 . TRP A 274 ? 0.1485 0.3329 2.3049 -0.0705 -0.0102 -0.1075 274 TRP A CZ2 
2176  C CZ3 . TRP A 274 ? 0.1620 0.3659 2.3824 -0.0790 -0.0245 -0.1198 274 TRP A CZ3 
2177  C CH2 . TRP A 274 ? 0.1543 0.3586 2.3572 -0.0764 -0.0088 -0.1172 274 TRP A CH2 
2178  N N   . TRP A 275 ? 0.2304 0.3017 2.2556 -0.0610 -0.1013 -0.0813 275 TRP A N   
2179  C CA  . TRP A 275 ? 0.2431 0.3013 2.2652 -0.0623 -0.1171 -0.0831 275 TRP A CA  
2180  C C   . TRP A 275 ? 0.2517 0.2906 2.2421 -0.0505 -0.1342 -0.0808 275 TRP A C   
2181  O O   . TRP A 275 ? 0.2396 0.2677 2.2280 -0.0492 -0.1510 -0.0841 275 TRP A O   
2182  C CB  . TRP A 275 ? 0.2613 0.3075 2.2676 -0.0723 -0.1065 -0.0773 275 TRP A CB  
2183  C CG  . TRP A 275 ? 0.2637 0.2928 2.2270 -0.0683 -0.0989 -0.0672 275 TRP A CG  
2184  C CD1 . TRP A 275 ? 0.2569 0.2890 2.2082 -0.0708 -0.0808 -0.0610 275 TRP A CD1 
2185  C CD2 . TRP A 275 ? 0.2663 0.2727 2.1940 -0.0613 -0.1090 -0.0627 275 TRP A CD2 
2186  N NE1 . TRP A 275 ? 0.2643 0.2785 2.1775 -0.0659 -0.0798 -0.0530 275 TRP A NE1 
2187  C CE2 . TRP A 275 ? 0.2683 0.2672 2.1671 -0.0598 -0.0961 -0.0540 275 TRP A CE2 
2188  C CE3 . TRP A 275 ? 0.2706 0.2623 2.1877 -0.0561 -0.1274 -0.0656 275 TRP A CE3 
2189  C CZ2 . TRP A 275 ? 0.2697 0.2492 2.1332 -0.0531 -0.1003 -0.0486 275 TRP A CZ2 
2190  C CZ3 . TRP A 275 ? 0.2781 0.2490 2.1574 -0.0498 -0.1305 -0.0601 275 TRP A CZ3 
2191  C CH2 . TRP A 275 ? 0.2792 0.2452 2.1336 -0.0481 -0.1169 -0.0519 275 TRP A CH2 
2192  N N   . LYS A 276 ? 0.2782 0.3120 2.2428 -0.0428 -0.1291 -0.0752 276 LYS A N   
2193  C CA  . LYS A 276 ? 0.3058 0.3196 2.2351 -0.0329 -0.1407 -0.0715 276 LYS A CA  
2194  C C   . LYS A 276 ? 0.3269 0.3410 2.2670 -0.0245 -0.1606 -0.0779 276 LYS A C   
2195  O O   . LYS A 276 ? 0.3509 0.3467 2.2631 -0.0170 -0.1730 -0.0761 276 LYS A O   
2196  C CB  . LYS A 276 ? 0.3023 0.3116 2.2031 -0.0282 -0.1286 -0.0638 276 LYS A CB  
2197  C CG  . LYS A 276 ? 0.3051 0.3127 2.1927 -0.0353 -0.1108 -0.0571 276 LYS A CG  
2198  C CD  . LYS A 276 ? 0.3028 0.3092 2.1674 -0.0313 -0.0991 -0.0504 276 LYS A CD  
2199  C CE  . LYS A 276 ? 0.3189 0.3080 2.1498 -0.0228 -0.1059 -0.0461 276 LYS A CE  
2200  N NZ  . LYS A 276 ? 0.3460 0.3184 2.1572 -0.0241 -0.1090 -0.0433 276 LYS A NZ  
2201  N N   . GLY A 277 ? 0.3390 0.3729 2.3186 -0.0256 -0.1636 -0.0853 277 GLY A N   
2202  C CA  . GLY A 277 ? 0.3682 0.4030 2.3591 -0.0164 -0.1828 -0.0911 277 GLY A CA  
2203  C C   . GLY A 277 ? 0.4091 0.4496 2.4310 -0.0194 -0.1997 -0.1000 277 GLY A C   
2204  O O   . GLY A 277 ? 0.4628 0.5013 2.4925 -0.0115 -0.2192 -0.1050 277 GLY A O   
2205  N N   . GLY A 278 ? 0.4103 0.4569 2.4494 -0.0308 -0.1933 -0.1019 278 GLY A N   
2206  C CA  . GLY A 278 ? 0.4234 0.4714 2.4862 -0.0344 -0.2106 -0.1099 278 GLY A CA  
2207  C C   . GLY A 278 ? 0.4322 0.5035 2.5412 -0.0469 -0.2004 -0.1160 278 GLY A C   
2208  O O   . GLY A 278 ? 0.4339 0.5047 2.5600 -0.0532 -0.2109 -0.1214 278 GLY A O   
2209  N N   . GLU A 279 ? 0.4436 0.5347 2.5728 -0.0507 -0.1802 -0.1156 279 GLU A N   
2210  C CA  . GLU A 279 ? 0.4468 0.5614 2.6218 -0.0627 -0.1690 -0.1221 279 GLU A CA  
2211  C C   . GLU A 279 ? 0.4587 0.5817 2.6295 -0.0695 -0.1407 -0.1166 279 GLU A C   
2212  O O   . GLU A 279 ? 0.5532 0.6857 2.7258 -0.0636 -0.1321 -0.1161 279 GLU A O   
2213  C CB  . GLU A 279 ? 0.4378 0.5761 2.6613 -0.0584 -0.1800 -0.1333 279 GLU A CB  
2214  C CG  . GLU A 279 ? 0.5178 0.6713 2.7871 -0.0683 -0.1876 -0.1432 279 GLU A CG  
2215  C CD  . GLU A 279 ? 0.5606 0.7229 2.8485 -0.0859 -0.1680 -0.1434 279 GLU A CD  
2216  O OE1 . GLU A 279 ? 0.5629 0.7224 2.8651 -0.0940 -0.1781 -0.1476 279 GLU A OE1 
2217  O OE2 . GLU A 279 ? 0.6154 0.7859 2.9026 -0.0922 -0.1428 -0.1394 279 GLU A OE2 
2218  N N   . LYS A 280 ? 0.4512 0.5691 2.6159 -0.0820 -0.1270 -0.1126 280 LYS A N   
2219  C CA  . LYS A 280 ? 0.4131 0.5312 2.5621 -0.0888 -0.1017 -0.1052 280 LYS A CA  
2220  C C   . LYS A 280 ? 0.3465 0.4910 2.5311 -0.0925 -0.0852 -0.1108 280 LYS A C   
2221  O O   . LYS A 280 ? 0.3117 0.4581 2.4839 -0.0967 -0.0644 -0.1057 280 LYS A O   
2222  C CB  . LYS A 280 ? 0.4448 0.5547 2.5904 -0.1033 -0.0913 -0.1018 280 LYS A CB  
2223  C CG  . LYS A 280 ? 0.4684 0.5642 2.6130 -0.1061 -0.1091 -0.1041 280 LYS A CG  
2224  C CD  . LYS A 280 ? 0.4994 0.6047 2.6771 -0.1224 -0.1009 -0.1086 280 LYS A CD  
2225  C CE  . LYS A 280 ? 0.5167 0.6011 2.6684 -0.1326 -0.0918 -0.1008 280 LYS A CE  
2226  N NZ  . LYS A 280 ? 0.5152 0.5889 2.6749 -0.1374 -0.1084 -0.1053 280 LYS A NZ  
2227  N N   . SER A 281 ? 0.3295 0.4947 2.5598 -0.0916 -0.0942 -0.1218 281 SER A N   
2228  C CA  . SER A 281 ? 0.3216 0.5137 2.5917 -0.0967 -0.0772 -0.1287 281 SER A CA  
2229  C C   . SER A 281 ? 0.3309 0.5348 2.6141 -0.0826 -0.0845 -0.1340 281 SER A C   
2230  O O   . SER A 281 ? 0.3806 0.6056 2.6926 -0.0839 -0.0702 -0.1398 281 SER A O   
2231  C CB  . SER A 281 ? 0.2973 0.5081 2.6169 -0.1085 -0.0769 -0.1383 281 SER A CB  
2232  O OG  . SER A 281 ? 0.2886 0.4838 2.5954 -0.1191 -0.0793 -0.1344 281 SER A OG  
2233  N N   . ASP A 282 ? 0.3265 0.5156 2.5879 -0.0694 -0.1066 -0.1321 282 ASP A N   
2234  C CA  . ASP A 282 ? 0.3209 0.5156 2.5881 -0.0554 -0.1156 -0.1356 282 ASP A CA  
2235  C C   . ASP A 282 ? 0.3148 0.4891 2.5305 -0.0479 -0.1111 -0.1250 282 ASP A C   
2236  O O   . ASP A 282 ? 0.2686 0.4198 2.4432 -0.0477 -0.1159 -0.1164 282 ASP A O   
2237  C CB  . ASP A 282 ? 0.3716 0.5664 2.6584 -0.0470 -0.1444 -0.1426 282 ASP A CB  
2238  C CG  . ASP A 282 ? 0.4426 0.6438 2.7421 -0.0324 -0.1565 -0.1475 282 ASP A CG  
2239  O OD1 . ASP A 282 ? 0.5000 0.7252 2.8391 -0.0322 -0.1466 -0.1554 282 ASP A OD1 
2240  O OD2 . ASP A 282 ? 0.5418 0.7226 2.8103 -0.0214 -0.1750 -0.1434 282 ASP A OD2 
2241  N N   . HIS A 283 ? 0.2995 0.4836 2.5201 -0.0425 -0.1005 -0.1264 283 HIS A N   
2242  C CA  . HIS A 283 ? 0.2842 0.4524 2.4642 -0.0337 -0.0991 -0.1187 283 HIS A CA  
2243  C C   . HIS A 283 ? 0.2587 0.4227 2.4429 -0.0193 -0.1215 -0.1225 283 HIS A C   
2244  O O   . HIS A 283 ? 0.2529 0.4271 2.4532 -0.0123 -0.1196 -0.1270 283 HIS A O   
2245  C CB  . HIS A 283 ? 0.2880 0.4656 2.4660 -0.0371 -0.0745 -0.1176 283 HIS A CB  
2246  C CG  . HIS A 283 ? 0.3096 0.4686 2.4391 -0.0349 -0.0670 -0.1070 283 HIS A CG  
2247  N ND1 . HIS A 283 ? 0.3151 0.4514 2.4056 -0.0319 -0.0777 -0.0985 283 HIS A ND1 
2248  C CD2 . HIS A 283 ? 0.3316 0.4916 2.4460 -0.0354 -0.0498 -0.1041 283 HIS A CD2 
2249  C CE1 . HIS A 283 ? 0.3023 0.4281 2.3585 -0.0306 -0.0674 -0.0909 283 HIS A CE1 
2250  N NE2 . HIS A 283 ? 0.3064 0.4458 2.3753 -0.0330 -0.0508 -0.0939 283 HIS A NE2 
2251  N N   . SER A 284 ? 0.2489 0.3967 2.4177 -0.0153 -0.1428 -0.1207 284 SER A N   
2252  C CA  . SER A 284 ? 0.2472 0.3847 2.4107 -0.0020 -0.1662 -0.1225 284 SER A CA  
2253  C C   . SER A 284 ? 0.2255 0.3545 2.3644 0.0070  -0.1615 -0.1179 284 SER A C   
2254  O O   . SER A 284 ? 0.2170 0.3346 2.3205 0.0048  -0.1481 -0.1094 284 SER A O   
2255  C CB  . SER A 284 ? 0.2638 0.3784 2.3980 -0.0004 -0.1849 -0.1183 284 SER A CB  
2256  O OG  . SER A 284 ? 0.2808 0.3797 2.3978 0.0123  -0.2057 -0.1178 284 SER A OG  
2257  N N   . LEU A 285 ? 0.2188 0.3537 2.3789 0.0174  -0.1733 -0.1240 285 LEU A N   
2258  C CA  . LEU A 285 ? 0.2141 0.3440 2.3599 0.0257  -0.1684 -0.1217 285 LEU A CA  
2259  C C   . LEU A 285 ? 0.2313 0.3319 2.3306 0.0337  -0.1832 -0.1134 285 LEU A C   
2260  O O   . LEU A 285 ? 0.2357 0.3257 2.3095 0.0383  -0.1772 -0.1083 285 LEU A O   
2261  C CB  . LEU A 285 ? 0.2097 0.3570 2.3981 0.0339  -0.1744 -0.1319 285 LEU A CB  
2262  C CG  . LEU A 285 ? 0.1939 0.3721 2.4319 0.0268  -0.1577 -0.1416 285 LEU A CG  
2263  C CD1 . LEU A 285 ? 0.1871 0.3798 2.4642 0.0372  -0.1655 -0.1517 285 LEU A CD1 
2264  C CD2 . LEU A 285 ? 0.1848 0.3695 2.4113 0.0172  -0.1282 -0.1380 285 LEU A CD2 
2265  N N   . ASN A 286 ? 0.2473 0.3343 2.3351 0.0348  -0.2020 -0.1125 286 ASN A N   
2266  C CA  . ASN A 286 ? 0.2700 0.3286 2.3148 0.0426  -0.2168 -0.1057 286 ASN A CA  
2267  C C   . ASN A 286 ? 0.2738 0.3161 2.2838 0.0361  -0.2152 -0.0988 286 ASN A C   
2268  O O   . ASN A 286 ? 0.2932 0.3131 2.2735 0.0410  -0.2312 -0.0955 286 ASN A O   
2269  C CB  . ASN A 286 ? 0.2980 0.3501 2.3554 0.0529  -0.2440 -0.1111 286 ASN A CB  
2270  C CG  . ASN A 286 ? 0.3138 0.3702 2.3899 0.0486  -0.2580 -0.1164 286 ASN A CG  
2271  O OD1 . ASN A 286 ? 0.3234 0.3996 2.4275 0.0387  -0.2460 -0.1203 286 ASN A OD1 
2272  N ND2 . ASN A 286 ? 0.3382 0.3749 2.3971 0.0552  -0.2826 -0.1163 286 ASN A ND2 
2273  N N   . GLN A 287 ? 0.2592 0.3120 2.2718 0.0255  -0.1955 -0.0968 287 GLN A N   
2274  C CA  . GLN A 287 ? 0.2510 0.2896 2.2322 0.0193  -0.1909 -0.0902 287 GLN A CA  
2275  C C   . GLN A 287 ? 0.2282 0.2626 2.1812 0.0166  -0.1707 -0.0821 287 GLN A C   
2276  O O   . GLN A 287 ? 0.2083 0.2562 2.1718 0.0088  -0.1523 -0.0814 287 GLN A O   
2277  C CB  . GLN A 287 ? 0.2483 0.2986 2.2537 0.0090  -0.1879 -0.0942 287 GLN A CB  
2278  C CG  . GLN A 287 ? 0.2684 0.3176 2.2931 0.0107  -0.2105 -0.1013 287 GLN A CG  
2279  C CD  . GLN A 287 ? 0.2934 0.3150 2.2800 0.0162  -0.2286 -0.0978 287 GLN A CD  
2280  O OE1 . GLN A 287 ? 0.3019 0.3046 2.2466 0.0182  -0.2235 -0.0899 287 GLN A OE1 
2281  N NE2 . GLN A 287 ? 0.3163 0.3352 2.3173 0.0185  -0.2502 -0.1042 287 GLN A NE2 
2282  N N   . PRO A 288 ? 0.2276 0.2420 2.1427 0.0228  -0.1739 -0.0756 288 PRO A N   
2283  C CA  . PRO A 288 ? 0.2177 0.2268 2.1044 0.0203  -0.1567 -0.0678 288 PRO A CA  
2284  C C   . PRO A 288 ? 0.2082 0.2214 2.0904 0.0107  -0.1425 -0.0645 288 PRO A C   
2285  O O   . PRO A 288 ? 0.1894 0.2095 2.0676 0.0066  -0.1255 -0.0611 288 PRO A O   
2286  C CB  . PRO A 288 ? 0.2293 0.2132 2.0762 0.0269  -0.1669 -0.0624 288 PRO A CB  
2287  C CG  . PRO A 288 ? 0.2470 0.2251 2.1035 0.0352  -0.1870 -0.0671 288 PRO A CG  
2288  C CD  . PRO A 288 ? 0.2426 0.2382 2.1405 0.0322  -0.1944 -0.0756 288 PRO A CD  
2289  N N   . GLU A 289 ? 0.2168 0.2244 2.0990 0.0071  -0.1498 -0.0656 289 GLU A N   
2290  C CA  . GLU A 289 ? 0.2198 0.2250 2.0894 -0.0005 -0.1380 -0.0610 289 GLU A CA  
2291  C C   . GLU A 289 ? 0.1974 0.2224 2.0933 -0.0091 -0.1217 -0.0627 289 GLU A C   
2292  O O   . GLU A 289 ? 0.1798 0.2046 2.0639 -0.0150 -0.1074 -0.0576 289 GLU A O   
2293  C CB  . GLU A 289 ? 0.2434 0.2352 2.1045 -0.0018 -0.1502 -0.0620 289 GLU A CB  
2294  C CG  . GLU A 289 ? 0.2656 0.2341 2.0895 0.0056  -0.1607 -0.0585 289 GLU A CG  
2295  C CD  . GLU A 289 ? 0.2670 0.2250 2.0570 0.0068  -0.1487 -0.0506 289 GLU A CD  
2296  O OE1 . GLU A 289 ? 0.2835 0.2407 2.0666 0.0015  -0.1387 -0.0473 289 GLU A OE1 
2297  O OE2 . GLU A 289 ? 0.2772 0.2269 2.0475 0.0130  -0.1499 -0.0477 289 GLU A OE2 
2298  N N   . GLU A 290 ? 0.1922 0.2340 2.1236 -0.0094 -0.1239 -0.0700 290 GLU A N   
2299  C CA  . GLU A 290 ? 0.1841 0.2450 2.1425 -0.0181 -0.1081 -0.0728 290 GLU A CA  
2300  C C   . GLU A 290 ? 0.1777 0.2455 2.1302 -0.0175 -0.0922 -0.0703 290 GLU A C   
2301  O O   . GLU A 290 ? 0.1791 0.2607 2.1480 -0.0247 -0.0770 -0.0719 290 GLU A O   
2302  C CB  . GLU A 290 ? 0.1860 0.2633 2.1874 -0.0191 -0.1162 -0.0826 290 GLU A CB  
2303  C CG  . GLU A 290 ? 0.1984 0.2688 2.2063 -0.0207 -0.1328 -0.0857 290 GLU A CG  
2304  C CD  . GLU A 290 ? 0.2025 0.2921 2.2578 -0.0228 -0.1401 -0.0960 290 GLU A CD  
2305  O OE1 . GLU A 290 ? 0.1888 0.2974 2.2708 -0.0236 -0.1292 -0.1003 290 GLU A OE1 
2306  O OE2 . GLU A 290 ? 0.2276 0.3140 2.2943 -0.0234 -0.1564 -0.1004 290 GLU A OE2 
2307  N N   . TRP A 291 ? 0.1771 0.2346 2.1046 -0.0098 -0.0944 -0.0662 291 TRP A N   
2308  C CA  . TRP A 291 ? 0.1724 0.2379 2.0992 -0.0095 -0.0806 -0.0656 291 TRP A CA  
2309  C C   . TRP A 291 ? 0.1638 0.2166 2.0535 -0.0085 -0.0738 -0.0572 291 TRP A C   
2310  O O   . TRP A 291 ? 0.1779 0.2299 2.0591 -0.0042 -0.0706 -0.0564 291 TRP A O   
2311  C CB  . TRP A 291 ? 0.1793 0.2502 2.1236 -0.0010 -0.0888 -0.0716 291 TRP A CB  
2312  C CG  . TRP A 291 ? 0.1793 0.2665 2.1657 -0.0011 -0.0947 -0.0812 291 TRP A CG  
2313  C CD1 . TRP A 291 ? 0.1962 0.2819 2.1975 0.0012  -0.1122 -0.0853 291 TRP A CD1 
2314  C CD2 . TRP A 291 ? 0.1732 0.2813 2.1937 -0.0036 -0.0834 -0.0886 291 TRP A CD2 
2315  N NE1 . TRP A 291 ? 0.1979 0.3034 2.2427 0.0006  -0.1133 -0.0947 291 TRP A NE1 
2316  C CE2 . TRP A 291 ? 0.1790 0.2988 2.2367 -0.0023 -0.0949 -0.0971 291 TRP A CE2 
2317  C CE3 . TRP A 291 ? 0.1630 0.2808 2.1863 -0.0067 -0.0647 -0.0895 291 TRP A CE3 
2318  C CZ2 . TRP A 291 ? 0.1622 0.3044 2.2614 -0.0041 -0.0871 -0.1064 291 TRP A CZ2 
2319  C CZ3 . TRP A 291 ? 0.1558 0.2941 2.2173 -0.0086 -0.0565 -0.0987 291 TRP A CZ3 
2320  C CH2 . TRP A 291 ? 0.1513 0.3023 2.2512 -0.0072 -0.0671 -0.1071 291 TRP A CH2 
2321  N N   . PHE A 292 ? 0.1613 0.2046 2.0305 -0.0126 -0.0713 -0.0513 292 PHE A N   
2322  C CA  . PHE A 292 ? 0.1582 0.1907 1.9951 -0.0113 -0.0658 -0.0438 292 PHE A CA  
2323  C C   . PHE A 292 ? 0.1510 0.1903 1.9837 -0.0180 -0.0490 -0.0406 292 PHE A C   
2324  O O   . PHE A 292 ? 0.1555 0.1886 1.9650 -0.0168 -0.0443 -0.0352 292 PHE A O   
2325  C CB  . PHE A 292 ? 0.1670 0.1836 1.9811 -0.0101 -0.0731 -0.0391 292 PHE A CB  
2326  C CG  . PHE A 292 ? 0.1798 0.1834 1.9791 -0.0017 -0.0867 -0.0391 292 PHE A CG  
2327  C CD1 . PHE A 292 ? 0.1789 0.1747 1.9552 0.0028  -0.0845 -0.0348 292 PHE A CD1 
2328  C CD2 . PHE A 292 ? 0.1971 0.1957 2.0055 0.0013  -0.1017 -0.0435 292 PHE A CD2 
2329  C CE1 . PHE A 292 ? 0.1936 0.1754 1.9537 0.0096  -0.0956 -0.0343 292 PHE A CE1 
2330  C CE2 . PHE A 292 ? 0.2085 0.1925 1.9994 0.0089  -0.1142 -0.0430 292 PHE A CE2 
2331  C CZ  . PHE A 292 ? 0.2049 0.1799 1.9708 0.0127  -0.1104 -0.0382 292 PHE A CZ  
2332  N N   . GLY A 293 ? 0.1491 0.2012 2.0040 -0.0249 -0.0399 -0.0443 293 GLY A N   
2333  C CA  . GLY A 293 ? 0.1576 0.2127 2.0046 -0.0323 -0.0244 -0.0407 293 GLY A CA  
2334  C C   . GLY A 293 ? 0.1630 0.2213 1.9997 -0.0304 -0.0158 -0.0400 293 GLY A C   
2335  O O   . GLY A 293 ? 0.1964 0.2589 2.0417 -0.0249 -0.0191 -0.0444 293 GLY A O   
2336  N N   . PHE A 294 ? 0.1601 0.2149 1.9772 -0.0348 -0.0059 -0.0345 294 PHE A N   
2337  C CA  . PHE A 294 ? 0.1482 0.2078 1.9589 -0.0357 0.0044  -0.0351 294 PHE A CA  
2338  C C   . PHE A 294 ? 0.1431 0.2142 1.9731 -0.0431 0.0172  -0.0401 294 PHE A C   
2339  O O   . PHE A 294 ? 0.1439 0.2212 1.9756 -0.0437 0.0262  -0.0435 294 PHE A O   
2340  C CB  . PHE A 294 ? 0.1514 0.2024 1.9326 -0.0370 0.0088  -0.0276 294 PHE A CB  
2341  C CG  . PHE A 294 ? 0.1462 0.1871 1.9083 -0.0306 -0.0010 -0.0227 294 PHE A CG  
2342  C CD1 . PHE A 294 ? 0.1466 0.1844 1.9131 -0.0237 -0.0120 -0.0248 294 PHE A CD1 
2343  C CD2 . PHE A 294 ? 0.1661 0.2002 1.9054 -0.0314 0.0012  -0.0162 294 PHE A CD2 
2344  C CE1 . PHE A 294 ? 0.1553 0.1834 1.9030 -0.0186 -0.0187 -0.0205 294 PHE A CE1 
2345  C CE2 . PHE A 294 ? 0.1608 0.1873 1.8848 -0.0258 -0.0061 -0.0124 294 PHE A CE2 
2346  C CZ  . PHE A 294 ? 0.1590 0.1824 1.8869 -0.0198 -0.0152 -0.0146 294 PHE A CZ  
2347  N N   . TRP A 295 ? 0.1423 0.2154 1.9856 -0.0492 0.0186  -0.0406 295 TRP A N   
2348  C CA  . TRP A 295 ? 0.1474 0.2328 2.0145 -0.0567 0.0304  -0.0464 295 TRP A CA  
2349  C C   . TRP A 295 ? 0.1624 0.2575 2.0632 -0.0546 0.0217  -0.0538 295 TRP A C   
2350  O O   . TRP A 295 ? 0.1713 0.2594 2.0713 -0.0513 0.0081  -0.0520 295 TRP A O   
2351  C CB  . TRP A 295 ? 0.1461 0.2258 2.0029 -0.0672 0.0404  -0.0412 295 TRP A CB  
2352  C CG  . TRP A 295 ? 0.1450 0.2161 1.9711 -0.0703 0.0499  -0.0347 295 TRP A CG  
2353  C CD1 . TRP A 295 ? 0.1414 0.2022 1.9401 -0.0648 0.0438  -0.0286 295 TRP A CD1 
2354  C CD2 . TRP A 295 ? 0.1488 0.2209 1.9684 -0.0796 0.0668  -0.0343 295 TRP A CD2 
2355  N NE1 . TRP A 295 ? 0.1513 0.2069 1.9279 -0.0697 0.0542  -0.0244 295 TRP A NE1 
2356  C CE2 . TRP A 295 ? 0.1581 0.2192 1.9448 -0.0788 0.0685  -0.0275 295 TRP A CE2 
2357  C CE3 . TRP A 295 ? 0.1559 0.2370 1.9939 -0.0886 0.0812  -0.0393 295 TRP A CE3 
2358  C CZ2 . TRP A 295 ? 0.1720 0.2288 1.9409 -0.0865 0.0826  -0.0252 295 TRP A CZ2 
2359  C CZ3 . TRP A 295 ? 0.1698 0.2464 1.9895 -0.0967 0.0970  -0.0369 295 TRP A CZ3 
2360  C CH2 . TRP A 295 ? 0.1745 0.2381 1.9586 -0.0956 0.0971  -0.0297 295 TRP A CH2 
2361  N N   . GLY A 296 ? 0.1673 0.2781 2.0973 -0.0565 0.0297  -0.0624 296 GLY A N   
2362  C CA  . GLY A 296 ? 0.1713 0.2943 2.1382 -0.0546 0.0217  -0.0707 296 GLY A CA  
2363  C C   . GLY A 296 ? 0.1827 0.3205 2.1785 -0.0649 0.0361  -0.0767 296 GLY A C   
2364  O O   . GLY A 296 ? 0.1934 0.3367 2.1875 -0.0704 0.0536  -0.0782 296 GLY A O   
2365  N N   . TYR A 297 ? 0.1767 0.3210 2.1995 -0.0680 0.0291  -0.0806 297 TYR A N   
2366  C CA  . TYR A 297 ? 0.1864 0.3451 2.2383 -0.0790 0.0435  -0.0863 297 TYR A CA  
2367  C C   . TYR A 297 ? 0.1808 0.3609 2.2736 -0.0745 0.0449  -0.0984 297 TYR A C   
2368  O O   . TYR A 297 ? 0.1681 0.3506 2.2721 -0.0632 0.0291  -0.1024 297 TYR A O   
2369  C CB  . TYR A 297 ? 0.1956 0.3487 2.2523 -0.0866 0.0375  -0.0835 297 TYR A CB  
2370  C CG  . TYR A 297 ? 0.2105 0.3417 2.2249 -0.0904 0.0387  -0.0715 297 TYR A CG  
2371  C CD1 . TYR A 297 ? 0.2200 0.3452 2.2141 -0.0999 0.0571  -0.0661 297 TYR A CD1 
2372  C CD2 . TYR A 297 ? 0.2062 0.3216 2.1997 -0.0840 0.0213  -0.0659 297 TYR A CD2 
2373  C CE1 . TYR A 297 ? 0.2302 0.3352 2.1870 -0.1022 0.0565  -0.0553 297 TYR A CE1 
2374  C CE2 . TYR A 297 ? 0.2125 0.3090 2.1702 -0.0862 0.0220  -0.0558 297 TYR A CE2 
2375  C CZ  . TYR A 297 ? 0.2304 0.3218 2.1702 -0.0949 0.0390  -0.0504 297 TYR A CZ  
2376  O OH  . TYR A 297 ? 0.2413 0.3135 2.1467 -0.0961 0.0382  -0.0405 297 TYR A OH  
2377  N N   . SER A 298 ? 0.1913 0.3857 2.3048 -0.0835 0.0648  -0.1041 298 SER A N   
2378  C CA  . SER A 298 ? 0.1989 0.4147 2.3516 -0.0801 0.0709  -0.1163 298 SER A CA  
2379  C C   . SER A 298 ? 0.2186 0.4508 2.4185 -0.0793 0.0590  -0.1251 298 SER A C   
2380  O O   . SER A 298 ? 0.2281 0.4663 2.4470 -0.0675 0.0429  -0.1309 298 SER A O   
2381  C CB  . SER A 298 ? 0.2095 0.4330 2.3636 -0.0905 0.0976  -0.1190 298 SER A CB  
2382  O OG  . SER A 298 ? 0.2419 0.4883 2.4394 -0.0881 0.1049  -0.1321 298 SER A OG  
2383  N N   . ASP A 299 ? 0.2364 0.4746 2.4540 -0.0921 0.0665  -0.1260 299 ASP A N   
2384  C CA  . ASP A 299 ? 0.2245 0.4762 2.4843 -0.0942 0.0545  -0.1332 299 ASP A CA  
2385  C C   . ASP A 299 ? 0.2319 0.4691 2.4746 -0.1044 0.0510  -0.1252 299 ASP A C   
2386  O O   . ASP A 299 ? 0.2216 0.4379 2.4197 -0.1077 0.0558  -0.1140 299 ASP A O   
2387  C CB  . ASP A 299 ? 0.2332 0.5116 2.5424 -0.1022 0.0715  -0.1451 299 ASP A CB  
2388  C CG  . ASP A 299 ? 0.2645 0.5433 2.5599 -0.1150 0.1016  -0.1430 299 ASP A CG  
2389  O OD1 . ASP A 299 ? 0.2624 0.5270 2.5327 -0.1269 0.1097  -0.1343 299 ASP A OD1 
2390  O OD2 . ASP A 299 ? 0.3191 0.6090 2.6236 -0.1119 0.1158  -0.1494 299 ASP A OD2 
2391  N N   . LEU A 300 ? 0.2233 0.4718 2.5033 -0.1092 0.0422  -0.1316 300 LEU A N   
2392  C CA  . LEU A 300 ? 0.2236 0.4600 2.4947 -0.1197 0.0386  -0.1261 300 LEU A CA  
2393  C C   . LEU A 300 ? 0.2434 0.4725 2.4942 -0.1347 0.0640  -0.1196 300 LEU A C   
2394  O O   . LEU A 300 ? 0.2897 0.4969 2.5053 -0.1397 0.0629  -0.1093 300 LEU A O   
2395  C CB  . LEU A 300 ? 0.2135 0.4665 2.5339 -0.1242 0.0277  -0.1359 300 LEU A CB  
2396  C CG  . LEU A 300 ? 0.2147 0.4512 2.5237 -0.1290 0.0121  -0.1311 300 LEU A CG  
2397  C CD1 . LEU A 300 ? 0.2262 0.4375 2.4907 -0.1173 -0.0078 -0.1224 300 LEU A CD1 
2398  C CD2 . LEU A 300 ? 0.2103 0.4640 2.5683 -0.1295 -0.0039 -0.1422 300 LEU A CD2 
2399  N N   . ASN A 301 ? 0.2292 0.4747 2.4992 -0.1414 0.0870  -0.1252 301 ASN A N   
2400  C CA  . ASN A 301 ? 0.2439 0.4809 2.4933 -0.1565 0.1115  -0.1191 301 ASN A CA  
2401  C C   . ASN A 301 ? 0.2480 0.4613 2.4393 -0.1536 0.1175  -0.1069 301 ASN A C   
2402  O O   . ASN A 301 ? 0.2673 0.4668 2.4328 -0.1654 0.1329  -0.0993 301 ASN A O   
2403  C CB  . ASN A 301 ? 0.2606 0.5216 2.5479 -0.1659 0.1354  -0.1293 301 ASN A CB  
2404  C CG  . ASN A 301 ? 0.2794 0.5596 2.6191 -0.1755 0.1345  -0.1385 301 ASN A CG  
2405  O OD1 . ASN A 301 ? 0.2960 0.5757 2.6509 -0.1720 0.1120  -0.1399 301 ASN A OD1 
2406  N ND2 . ASN A 301 ? 0.2959 0.5928 2.6635 -0.1887 0.1593  -0.1451 301 ASN A ND2 
2407  N N   . ASP A 302 ? 0.2157 0.4223 2.3846 -0.1388 0.1050  -0.1045 302 ASP A N   
2408  C CA  . ASP A 302 ? 0.2077 0.3949 2.3263 -0.1369 0.1119  -0.0942 302 ASP A CA  
2409  C C   . ASP A 302 ? 0.2219 0.3836 2.3023 -0.1393 0.1027  -0.0818 302 ASP A C   
2410  O O   . ASP A 302 ? 0.2198 0.3737 2.2951 -0.1309 0.0817  -0.0796 302 ASP A O   
2411  C CB  . ASP A 302 ? 0.1847 0.3723 2.2920 -0.1215 0.1020  -0.0954 302 ASP A CB  
2412  C CG  . ASP A 302 ? 0.1772 0.3503 2.2401 -0.1199 0.1116  -0.0878 302 ASP A CG  
2413  O OD1 . ASP A 302 ? 0.1815 0.3447 2.2221 -0.1310 0.1276  -0.0819 302 ASP A OD1 
2414  O OD2 . ASP A 302 ? 0.1580 0.3296 2.2096 -0.1079 0.1032  -0.0883 302 ASP A OD2 
2415  N N   . LYS A 303 ? 0.2332 0.3800 2.2831 -0.1497 0.1184  -0.0735 303 LYS A N   
2416  C CA  . LYS A 303 ? 0.2373 0.3585 2.2481 -0.1509 0.1110  -0.0614 303 LYS A CA  
2417  C C   . LYS A 303 ? 0.2245 0.3305 2.1911 -0.1426 0.1091  -0.0530 303 LYS A C   
2418  O O   . LYS A 303 ? 0.2247 0.3102 2.1588 -0.1417 0.1021  -0.0432 303 LYS A O   
2419  C CB  . LYS A 303 ? 0.2634 0.3751 2.2690 -0.1677 0.1266  -0.0568 303 LYS A CB  
2420  C CG  . LYS A 303 ? 0.2696 0.3931 2.3170 -0.1781 0.1276  -0.0637 303 LYS A CG  
2421  C CD  . LYS A 303 ? 0.2667 0.3830 2.3212 -0.1741 0.1050  -0.0630 303 LYS A CD  
2422  C CE  . LYS A 303 ? 0.2756 0.3986 2.3646 -0.1861 0.1057  -0.0682 303 LYS A CE  
2423  N NZ  . LYS A 303 ? 0.2655 0.4186 2.4067 -0.1866 0.1082  -0.0819 303 LYS A NZ  
2424  N N   . TYR A 304 ? 0.2058 0.3215 2.1718 -0.1362 0.1146  -0.0572 304 TYR A N   
2425  C CA  . TYR A 304 ? 0.2034 0.3056 2.1285 -0.1316 0.1169  -0.0499 304 TYR A CA  
2426  C C   . TYR A 304 ? 0.1887 0.2941 2.1107 -0.1165 0.1018  -0.0519 304 TYR A C   
2427  O O   . TYR A 304 ? 0.1888 0.2794 2.0800 -0.1097 0.0910  -0.0441 304 TYR A O   
2428  C CB  . TYR A 304 ? 0.2117 0.3167 2.1284 -0.1399 0.1398  -0.0515 304 TYR A CB  
2429  C CG  . TYR A 304 ? 0.2316 0.3272 2.1409 -0.1554 0.1548  -0.0468 304 TYR A CG  
2430  C CD1 . TYR A 304 ? 0.2460 0.3172 2.1155 -0.1592 0.1533  -0.0347 304 TYR A CD1 
2431  C CD2 . TYR A 304 ? 0.2340 0.3446 2.1779 -0.1661 0.1693  -0.0546 304 TYR A CD2 
2432  C CE1 . TYR A 304 ? 0.2694 0.3290 2.1308 -0.1734 0.1658  -0.0297 304 TYR A CE1 
2433  C CE2 . TYR A 304 ? 0.2554 0.3561 2.1926 -0.1813 0.1833  -0.0501 304 TYR A CE2 
2434  C CZ  . TYR A 304 ? 0.2738 0.3477 2.1684 -0.1850 0.1812  -0.0372 304 TYR A CZ  
2435  O OH  . TYR A 304 ? 0.2944 0.3555 2.1795 -0.2001 0.1948  -0.0320 304 TYR A OH  
2436  N N   . GLY A 305 ? 0.1727 0.2972 2.1269 -0.1117 0.1022  -0.0625 305 GLY A N   
2437  C CA  . GLY A 305 ? 0.1557 0.2842 2.1102 -0.0984 0.0908  -0.0657 305 GLY A CA  
2438  C C   . GLY A 305 ? 0.1560 0.2814 2.0865 -0.0966 0.1015  -0.0647 305 GLY A C   
2439  O O   . GLY A 305 ? 0.1715 0.2929 2.0863 -0.1055 0.1181  -0.0625 305 GLY A O   
2440  N N   . THR A 306 ? 0.1441 0.2705 2.0715 -0.0853 0.0914  -0.0668 306 THR A N   
2441  C CA  . THR A 306 ? 0.1440 0.2648 2.0455 -0.0823 0.0972  -0.0652 306 THR A CA  
2442  C C   . THR A 306 ? 0.1316 0.2432 2.0158 -0.0713 0.0798  -0.0608 306 THR A C   
2443  O O   . THR A 306 ? 0.1152 0.2283 2.0133 -0.0643 0.0648  -0.0621 306 THR A O   
2444  C CB  . THR A 306 ? 0.1409 0.2762 2.0638 -0.0811 0.1090  -0.0759 306 THR A CB  
2445  O OG1 . THR A 306 ? 0.1267 0.2733 2.0822 -0.0724 0.0964  -0.0831 306 THR A OG1 
2446  C CG2 . THR A 306 ? 0.1504 0.2954 2.0894 -0.0925 0.1293  -0.0810 306 THR A CG2 
2447  N N   . PRO A 307 ? 0.1451 0.2463 1.9974 -0.0699 0.0814  -0.0555 307 PRO A N   
2448  C CA  . PRO A 307 ? 0.1457 0.2388 1.9821 -0.0606 0.0668  -0.0516 307 PRO A CA  
2449  C C   . PRO A 307 ? 0.1437 0.2432 1.9950 -0.0513 0.0605  -0.0585 307 PRO A C   
2450  O O   . PRO A 307 ? 0.1382 0.2449 1.9983 -0.0511 0.0698  -0.0654 307 PRO A O   
2451  C CB  . PRO A 307 ? 0.1545 0.2366 1.9556 -0.0638 0.0726  -0.0448 307 PRO A CB  
2452  C CG  . PRO A 307 ? 0.1657 0.2532 1.9684 -0.0713 0.0908  -0.0496 307 PRO A CG  
2453  C CD  . PRO A 307 ? 0.1653 0.2616 1.9951 -0.0776 0.0970  -0.0532 307 PRO A CD  
2454  N N   . ARG A 308 ? 0.1432 0.2383 1.9963 -0.0436 0.0444  -0.0567 308 ARG A N   
2455  C CA  . ARG A 308 ? 0.1465 0.2423 2.0065 -0.0344 0.0360  -0.0610 308 ARG A CA  
2456  C C   . ARG A 308 ? 0.1577 0.2443 1.9893 -0.0324 0.0370  -0.0570 308 ARG A C   
2457  O O   . ARG A 308 ? 0.1811 0.2611 1.9887 -0.0370 0.0411  -0.0504 308 ARG A O   
2458  C CB  . ARG A 308 ? 0.1421 0.2331 2.0082 -0.0282 0.0189  -0.0592 308 ARG A CB  
2459  C CG  . ARG A 308 ? 0.1444 0.2461 2.0440 -0.0283 0.0151  -0.0657 308 ARG A CG  
2460  C CD  . ARG A 308 ? 0.1436 0.2390 2.0473 -0.0221 -0.0031 -0.0645 308 ARG A CD  
2461  N NE  . ARG A 308 ? 0.1346 0.2413 2.0724 -0.0229 -0.0075 -0.0713 308 ARG A NE  
2462  C CZ  . ARG A 308 ? 0.1378 0.2411 2.0803 -0.0239 -0.0178 -0.0698 308 ARG A CZ  
2463  N NH1 . ARG A 308 ? 0.1395 0.2275 2.0546 -0.0228 -0.0256 -0.0621 308 ARG A NH1 
2464  N NH2 . ARG A 308 ? 0.1356 0.2510 2.1114 -0.0261 -0.0204 -0.0767 308 ARG A NH2 
2465  N N   . PRO A 309 ? 0.1420 0.2274 1.9756 -0.0255 0.0324  -0.0606 309 PRO A N   
2466  C CA  . PRO A 309 ? 0.1444 0.2214 1.9533 -0.0243 0.0331  -0.0575 309 PRO A CA  
2467  C C   . PRO A 309 ? 0.1468 0.2135 1.9303 -0.0247 0.0266  -0.0481 309 PRO A C   
2468  O O   . PRO A 309 ? 0.1480 0.2105 1.9103 -0.0278 0.0310  -0.0444 309 PRO A O   
2469  C CB  . PRO A 309 ? 0.1460 0.2216 1.9659 -0.0160 0.0255  -0.0626 309 PRO A CB  
2470  C CG  . PRO A 309 ? 0.1531 0.2410 2.0053 -0.0149 0.0291  -0.0715 309 PRO A CG  
2471  C CD  . PRO A 309 ? 0.1468 0.2386 2.0077 -0.0190 0.0269  -0.0685 309 PRO A CD  
2472  N N   . VAL A 310 ? 0.1422 0.2051 1.9286 -0.0215 0.0158  -0.0448 310 VAL A N   
2473  C CA  . VAL A 310 ? 0.1267 0.1800 1.8913 -0.0206 0.0094  -0.0369 310 VAL A CA  
2474  C C   . VAL A 310 ? 0.1214 0.1737 1.8704 -0.0271 0.0167  -0.0318 310 VAL A C   
2475  O O   . VAL A 310 ? 0.1206 0.1668 1.8507 -0.0267 0.0141  -0.0261 310 VAL A O   
2476  C CB  . VAL A 310 ? 0.1235 0.1719 1.8924 -0.0170 -0.0019 -0.0347 310 VAL A CB  
2477  C CG1 . VAL A 310 ? 0.1235 0.1776 1.9086 -0.0210 -0.0002 -0.0363 310 VAL A CG1 
2478  C CG2 . VAL A 310 ? 0.1210 0.1597 1.8677 -0.0156 -0.0069 -0.0275 310 VAL A CG2 
2479  N N   . TRP A 311 ? 0.1215 0.1794 1.8786 -0.0331 0.0255  -0.0336 311 TRP A N   
2480  C CA  . TRP A 311 ? 0.1290 0.1828 1.8696 -0.0392 0.0308  -0.0277 311 TRP A CA  
2481  C C   . TRP A 311 ? 0.1408 0.1924 1.8618 -0.0413 0.0366  -0.0263 311 TRP A C   
2482  O O   . TRP A 311 ? 0.1430 0.1882 1.8446 -0.0418 0.0340  -0.0201 311 TRP A O   
2483  C CB  . TRP A 311 ? 0.1300 0.1889 1.8842 -0.0459 0.0394  -0.0300 311 TRP A CB  
2484  C CG  . TRP A 311 ? 0.1314 0.1850 1.8683 -0.0536 0.0478  -0.0248 311 TRP A CG  
2485  C CD1 . TRP A 311 ? 0.1395 0.1934 1.8659 -0.0596 0.0598  -0.0257 311 TRP A CD1 
2486  C CD2 . TRP A 311 ? 0.1365 0.1824 1.8656 -0.0564 0.0447  -0.0182 311 TRP A CD2 
2487  N NE1 . TRP A 311 ? 0.1533 0.1988 1.8635 -0.0659 0.0639  -0.0192 311 TRP A NE1 
2488  C CE2 . TRP A 311 ? 0.1529 0.1936 1.8655 -0.0640 0.0547  -0.0145 311 TRP A CE2 
2489  C CE3 . TRP A 311 ? 0.1324 0.1737 1.8654 -0.0531 0.0343  -0.0152 311 TRP A CE3 
2490  C CZ2 . TRP A 311 ? 0.1667 0.1972 1.8672 -0.0681 0.0541  -0.0075 311 TRP A CZ2 
2491  C CZ3 . TRP A 311 ? 0.1453 0.1777 1.8681 -0.0573 0.0343  -0.0092 311 TRP A CZ3 
2492  C CH2 . TRP A 311 ? 0.1616 0.1884 1.8688 -0.0646 0.0440  -0.0051 311 TRP A CH2 
2493  N N   . PHE A 312 ? 0.1573 0.2140 1.8839 -0.0419 0.0436  -0.0327 312 PHE A N   
2494  C CA  . PHE A 312 ? 0.1787 0.2323 1.8859 -0.0441 0.0484  -0.0323 312 PHE A CA  
2495  C C   . PHE A 312 ? 0.1770 0.2259 1.8726 -0.0391 0.0389  -0.0292 312 PHE A C   
2496  O O   . PHE A 312 ? 0.1814 0.2262 1.8578 -0.0410 0.0383  -0.0253 312 PHE A O   
2497  C CB  . PHE A 312 ? 0.1882 0.2482 1.9070 -0.0457 0.0586  -0.0411 312 PHE A CB  
2498  C CG  . PHE A 312 ? 0.1976 0.2626 1.9263 -0.0522 0.0702  -0.0438 312 PHE A CG  
2499  C CD1 . PHE A 312 ? 0.2181 0.2780 1.9272 -0.0598 0.0791  -0.0401 312 PHE A CD1 
2500  C CD2 . PHE A 312 ? 0.2018 0.2762 1.9596 -0.0509 0.0721  -0.0500 312 PHE A CD2 
2501  C CE1 . PHE A 312 ? 0.2337 0.2970 1.9506 -0.0669 0.0914  -0.0424 312 PHE A CE1 
2502  C CE2 . PHE A 312 ? 0.2182 0.2986 1.9876 -0.0577 0.0843  -0.0532 312 PHE A CE2 
2503  C CZ  . PHE A 312 ? 0.2337 0.3082 1.9821 -0.0662 0.0948  -0.0492 312 PHE A CZ  
2504  N N   . ALA A 313 ? 0.1717 0.2208 1.8789 -0.0330 0.0312  -0.0310 313 ALA A N   
2505  C CA  . ALA A 313 ? 0.1598 0.2040 1.8572 -0.0290 0.0235  -0.0282 313 ALA A CA  
2506  C C   . ALA A 313 ? 0.1679 0.2081 1.8523 -0.0291 0.0184  -0.0206 313 ALA A C   
2507  O O   . ALA A 313 ? 0.1755 0.2136 1.8466 -0.0292 0.0165  -0.0177 313 ALA A O   
2508  C CB  . ALA A 313 ? 0.1439 0.1865 1.8540 -0.0228 0.0165  -0.0309 313 ALA A CB  
2509  N N   . MET A 314 ? 0.1676 0.2069 1.8574 -0.0288 0.0159  -0.0179 314 MET A N   
2510  C CA  . MET A 314 ? 0.1820 0.2165 1.8608 -0.0280 0.0111  -0.0112 314 MET A CA  
2511  C C   . MET A 314 ? 0.1891 0.2226 1.8528 -0.0325 0.0152  -0.0076 314 MET A C   
2512  O O   . MET A 314 ? 0.1987 0.2297 1.8508 -0.0311 0.0112  -0.0033 314 MET A O   
2513  C CB  . MET A 314 ? 0.1988 0.2312 1.8856 -0.0276 0.0081  -0.0097 314 MET A CB  
2514  C CG  . MET A 314 ? 0.2092 0.2397 1.9061 -0.0222 0.0007  -0.0118 314 MET A CG  
2515  S SD  . MET A 314 ? 0.2394 0.2631 1.9222 -0.0171 -0.0064 -0.0073 314 MET A SD  
2516  C CE  . MET A 314 ? 0.2281 0.2475 1.9049 -0.0186 -0.0074 -0.0021 314 MET A CE  
2517  N N   . ARG A 315 ? 0.1943 0.2292 1.8580 -0.0379 0.0233  -0.0093 315 ARG A N   
2518  C CA  . ARG A 315 ? 0.2094 0.2406 1.8554 -0.0426 0.0270  -0.0056 315 ARG A CA  
2519  C C   . ARG A 315 ? 0.2207 0.2521 1.8548 -0.0413 0.0241  -0.0055 315 ARG A C   
2520  O O   . ARG A 315 ? 0.2457 0.2741 1.8684 -0.0400 0.0184  -0.0005 315 ARG A O   
2521  C CB  . ARG A 315 ? 0.2187 0.2507 1.8637 -0.0492 0.0381  -0.0087 315 ARG A CB  
2522  C CG  . ARG A 315 ? 0.2417 0.2670 1.8632 -0.0540 0.0413  -0.0048 315 ARG A CG  
2523  C CD  . ARG A 315 ? 0.2606 0.2847 1.8774 -0.0614 0.0539  -0.0079 315 ARG A CD  
2524  N NE  . ARG A 315 ? 0.2724 0.3029 1.8965 -0.0611 0.0595  -0.0161 315 ARG A NE  
2525  C CZ  . ARG A 315 ? 0.2886 0.3225 1.9191 -0.0653 0.0715  -0.0225 315 ARG A CZ  
2526  N NH1 . ARG A 315 ? 0.3292 0.3608 1.9579 -0.0718 0.0810  -0.0214 315 ARG A NH1 
2527  N NH2 . ARG A 315 ? 0.2875 0.3269 1.9270 -0.0632 0.0747  -0.0303 315 ARG A NH2 
2528  N N   . ASP A 316 ? 0.2189 0.2540 1.8574 -0.0415 0.0275  -0.0116 316 ASP A N   
2529  C CA  . ASP A 316 ? 0.2171 0.2522 1.8449 -0.0417 0.0257  -0.0128 316 ASP A CA  
2530  C C   . ASP A 316 ? 0.2025 0.2380 1.8298 -0.0374 0.0168  -0.0094 316 ASP A C   
2531  O O   . ASP A 316 ? 0.2011 0.2366 1.8182 -0.0382 0.0136  -0.0080 316 ASP A O   
2532  C CB  . ASP A 316 ? 0.2138 0.2514 1.8491 -0.0421 0.0309  -0.0205 316 ASP A CB  
2533  C CG  . ASP A 316 ? 0.2281 0.2660 1.8616 -0.0470 0.0415  -0.0249 316 ASP A CG  
2534  O OD1 . ASP A 316 ? 0.2276 0.2626 1.8517 -0.0511 0.0452  -0.0212 316 ASP A OD1 
2535  O OD2 . ASP A 316 ? 0.2375 0.2775 1.8781 -0.0468 0.0463  -0.0320 316 ASP A OD2 
2536  N N   . TYR A 317 ? 0.1978 0.2335 1.8365 -0.0329 0.0130  -0.0087 317 TYR A N   
2537  C CA  . TYR A 317 ? 0.2038 0.2397 1.8431 -0.0291 0.0069  -0.0069 317 TYR A CA  
2538  C C   . TYR A 317 ? 0.2263 0.2613 1.8588 -0.0278 0.0025  -0.0010 317 TYR A C   
2539  O O   . TYR A 317 ? 0.2529 0.2898 1.8830 -0.0261 -0.0014 0.0006  317 TYR A O   
2540  C CB  . TYR A 317 ? 0.2070 0.2408 1.8570 -0.0248 0.0042  -0.0079 317 TYR A CB  
2541  C CG  . TYR A 317 ? 0.2071 0.2392 1.8554 -0.0213 -0.0006 -0.0055 317 TYR A CG  
2542  C CD1 . TYR A 317 ? 0.2126 0.2441 1.8606 -0.0212 -0.0008 -0.0077 317 TYR A CD1 
2543  C CD2 . TYR A 317 ? 0.2008 0.2311 1.8475 -0.0183 -0.0041 -0.0013 317 TYR A CD2 
2544  C CE1 . TYR A 317 ? 0.2133 0.2433 1.8593 -0.0192 -0.0033 -0.0056 317 TYR A CE1 
2545  C CE2 . TYR A 317 ? 0.2077 0.2366 1.8526 -0.0154 -0.0067 0.0002  317 TYR A CE2 
2546  C CZ  . TYR A 317 ? 0.2188 0.2478 1.8634 -0.0162 -0.0059 -0.0018 317 TYR A CZ  
2547  O OH  . TYR A 317 ? 0.2460 0.2731 1.8887 -0.0143 -0.0067 -0.0005 317 TYR A OH  
2548  N N   . MET A 318 ? 0.2451 0.2771 1.8759 -0.0286 0.0034  0.0019  318 MET A N   
2549  C CA  . MET A 318 ? 0.2512 0.2803 1.8756 -0.0268 -0.0010 0.0076  318 MET A CA  
2550  C C   . MET A 318 ? 0.2392 0.2686 1.8509 -0.0287 -0.0030 0.0100  318 MET A C   
2551  O O   . MET A 318 ? 0.2385 0.2669 1.8467 -0.0258 -0.0084 0.0141  318 MET A O   
2552  C CB  . MET A 318 ? 0.2749 0.2985 1.9000 -0.0280 0.0005  0.0100  318 MET A CB  
2553  C CG  . MET A 318 ? 0.2770 0.2985 1.9118 -0.0239 -0.0026 0.0101  318 MET A CG  
2554  S SD  . MET A 318 ? 0.3325 0.3479 1.9699 -0.0270 -0.0003 0.0118  318 MET A SD  
2555  C CE  . MET A 318 ? 0.3109 0.3218 1.9528 -0.0204 -0.0075 0.0130  318 MET A CE  
2556  N N   . LYS A 319 ? 0.2512 0.2814 1.8561 -0.0332 0.0007  0.0072  319 LYS A N   
2557  C CA  . LYS A 319 ? 0.2963 0.3244 1.8860 -0.0356 -0.0020 0.0096  319 LYS A CA  
2558  C C   . LYS A 319 ? 0.3145 0.3479 1.9052 -0.0324 -0.0098 0.0106  319 LYS A C   
2559  O O   . LYS A 319 ? 0.3765 0.4080 1.9573 -0.0321 -0.0156 0.0142  319 LYS A O   
2560  C CB  . LYS A 319 ? 0.3232 0.3507 1.9046 -0.0411 0.0037  0.0050  319 LYS A CB  
2561  C CG  . LYS A 319 ? 0.3495 0.3720 1.9272 -0.0454 0.0125  0.0042  319 LYS A CG  
2562  C CD  . LYS A 319 ? 0.3857 0.4017 1.9427 -0.0511 0.0162  0.0042  319 LYS A CD  
2563  C CE  . LYS A 319 ? 0.4277 0.4352 1.9757 -0.0544 0.0206  0.0090  319 LYS A CE  
2564  N NZ  . LYS A 319 ? 0.4684 0.4662 1.9909 -0.0579 0.0185  0.0128  319 LYS A NZ  
2565  N N   . GLY A 320 ? 0.2823 0.3218 1.8849 -0.0303 -0.0102 0.0075  320 GLY A N   
2566  C CA  . GLY A 320 ? 0.2641 0.3100 1.8717 -0.0276 -0.0160 0.0080  320 GLY A CA  
2567  C C   . GLY A 320 ? 0.2433 0.2917 1.8635 -0.0239 -0.0148 0.0071  320 GLY A C   
2568  O O   . GLY A 320 ? 0.2321 0.2806 1.8572 -0.0251 -0.0112 0.0035  320 GLY A O   
2569  N N   . LEU A 321 ? 0.2166 0.2653 1.8405 -0.0192 -0.0181 0.0105  321 LEU A N   
2570  C CA  . LEU A 321 ? 0.1984 0.2477 1.8309 -0.0156 -0.0166 0.0100  321 LEU A CA  
2571  C C   . LEU A 321 ? 0.1883 0.2460 1.8278 -0.0145 -0.0183 0.0090  321 LEU A C   
2572  O O   . LEU A 321 ? 0.1936 0.2568 1.8342 -0.0132 -0.0230 0.0104  321 LEU A O   
2573  C CB  . LEU A 321 ? 0.1937 0.2371 1.8258 -0.0112 -0.0179 0.0133  321 LEU A CB  
2574  C CG  . LEU A 321 ? 0.1823 0.2180 1.8106 -0.0130 -0.0157 0.0139  321 LEU A CG  
2575  C CD1 . LEU A 321 ? 0.1791 0.2087 1.8059 -0.0094 -0.0183 0.0175  321 LEU A CD1 
2576  C CD2 . LEU A 321 ? 0.1665 0.1998 1.7996 -0.0138 -0.0121 0.0105  321 LEU A CD2 
2577  N N   . ILE A 322 ? 0.1767 0.2351 1.8210 -0.0154 -0.0146 0.0064  322 ILE A N   
2578  C CA  . ILE A 322 ? 0.1689 0.2343 1.8212 -0.0148 -0.0138 0.0053  322 ILE A CA  
2579  C C   . ILE A 322 ? 0.1536 0.2154 1.8079 -0.0097 -0.0117 0.0067  322 ILE A C   
2580  O O   . ILE A 322 ? 0.1298 0.1832 1.7802 -0.0093 -0.0087 0.0063  322 ILE A O   
2581  C CB  . ILE A 322 ? 0.1977 0.2631 1.8513 -0.0198 -0.0101 0.0019  322 ILE A CB  
2582  C CG1 . ILE A 322 ? 0.2122 0.2812 1.8635 -0.0249 -0.0124 -0.0005 322 ILE A CG1 
2583  C CG2 . ILE A 322 ? 0.2129 0.2838 1.8746 -0.0203 -0.0070 0.0008  322 ILE A CG2 
2584  C CD1 . ILE A 322 ? 0.2208 0.2820 1.8648 -0.0275 -0.0103 -0.0024 322 ILE A CD1 
2585  N N   . ILE A 323 ? 0.1652 0.2328 1.8253 -0.0056 -0.0137 0.0079  323 ILE A N   
2586  C CA  . ILE A 323 ? 0.1756 0.2403 1.8377 -0.0007 -0.0106 0.0082  323 ILE A CA  
2587  C C   . ILE A 323 ? 0.1748 0.2467 1.8450 -0.0021 -0.0053 0.0057  323 ILE A C   
2588  O O   . ILE A 323 ? 0.1785 0.2452 1.8465 -0.0005 0.0001  0.0051  323 ILE A O   
2589  C CB  . ILE A 323 ? 0.1976 0.2626 1.8616 0.0055  -0.0147 0.0104  323 ILE A CB  
2590  C CG1 . ILE A 323 ? 0.2141 0.2695 1.8689 0.0059  -0.0186 0.0132  323 ILE A CG1 
2591  C CG2 . ILE A 323 ? 0.2045 0.2667 1.8706 0.0107  -0.0107 0.0095  323 ILE A CG2 
2592  C CD1 . ILE A 323 ? 0.2269 0.2840 1.8774 0.0011  -0.0216 0.0140  323 ILE A CD1 
2593  N N   . SER A 324 ? 0.1667 0.2502 1.8458 -0.0058 -0.0065 0.0040  324 SER A N   
2594  C CA  . SER A 324 ? 0.1744 0.2654 1.8628 -0.0088 -0.0006 0.0014  324 SER A CA  
2595  C C   . SER A 324 ? 0.1724 0.2712 1.8660 -0.0155 -0.0027 -0.0007 324 SER A C   
2596  O O   . SER A 324 ? 0.1900 0.2933 1.8841 -0.0156 -0.0101 -0.0003 324 SER A O   
2597  C CB  . SER A 324 ? 0.1902 0.2919 1.8920 -0.0038 0.0005  0.0004  324 SER A CB  
2598  O OG  . SER A 324 ? 0.1892 0.2823 1.8851 0.0026  0.0028  0.0017  324 SER A OG  
2599  N N   . PRO A 325 ? 0.1564 0.2552 1.8521 -0.0216 0.0031  -0.0029 325 PRO A N   
2600  C CA  . PRO A 325 ? 0.1598 0.2492 1.8498 -0.0223 0.0118  -0.0027 325 PRO A CA  
2601  C C   . PRO A 325 ? 0.1866 0.2588 1.8600 -0.0199 0.0115  -0.0005 325 PRO A C   
2602  O O   . PRO A 325 ? 0.1683 0.2354 1.8354 -0.0203 0.0067  0.0000  325 PRO A O   
2603  C CB  . PRO A 325 ? 0.1560 0.2467 1.8491 -0.0304 0.0159  -0.0050 325 PRO A CB  
2604  C CG  . PRO A 325 ? 0.1516 0.2450 1.8444 -0.0334 0.0084  -0.0061 325 PRO A CG  
2605  C CD  . PRO A 325 ? 0.1470 0.2523 1.8480 -0.0286 0.0012  -0.0056 325 PRO A CD  
2606  N N   . LYS A 326 ? 0.2074 0.2708 1.8741 -0.0173 0.0169  0.0004  326 LYS A N   
2607  C CA  . LYS A 326 ? 0.2088 0.2554 1.8605 -0.0152 0.0161  0.0020  326 LYS A CA  
2608  C C   . LYS A 326 ? 0.2203 0.2573 1.8650 -0.0208 0.0194  0.0016  326 LYS A C   
2609  O O   . LYS A 326 ? 0.2135 0.2531 1.8614 -0.0255 0.0258  0.0006  326 LYS A O   
2610  C CB  . LYS A 326 ? 0.2193 0.2584 1.8642 -0.0099 0.0192  0.0029  326 LYS A CB  
2611  C CG  . LYS A 326 ? 0.2191 0.2662 1.8712 -0.0039 0.0155  0.0032  326 LYS A CG  
2612  C CD  . LYS A 326 ? 0.2283 0.2683 1.8744 0.0014  0.0193  0.0031  326 LYS A CD  
2613  C CE  . LYS A 326 ? 0.2308 0.2730 1.8802 0.0075  0.0139  0.0037  326 LYS A CE  
2614  N NZ  . LYS A 326 ? 0.2313 0.2889 1.8953 0.0075  0.0098  0.0038  326 LYS A NZ  
2615  N N   . ASN A 327 ? 0.2067 0.2331 1.8431 -0.0201 0.0151  0.0021  327 ASN A N   
2616  C CA  . ASN A 327 ? 0.2208 0.2344 1.8487 -0.0236 0.0165  0.0019  327 ASN A CA  
2617  C C   . ASN A 327 ? 0.2283 0.2275 1.8432 -0.0227 0.0211  0.0037  327 ASN A C   
2618  O O   . ASN A 327 ? 0.2203 0.2148 1.8293 -0.0175 0.0202  0.0048  327 ASN A O   
2619  C CB  . ASN A 327 ? 0.2290 0.2361 1.8539 -0.0217 0.0103  0.0014  327 ASN A CB  
2620  C CG  . ASN A 327 ? 0.2349 0.2300 1.8538 -0.0249 0.0107  0.0006  327 ASN A CG  
2621  O OD1 . ASN A 327 ? 0.2235 0.2219 1.8461 -0.0304 0.0132  -0.0010 327 ASN A OD1 
2622  N ND2 . ASN A 327 ? 0.2551 0.2357 1.8649 -0.0212 0.0072  0.0014  327 ASN A ND2 
2623  N N   . LYS A 328 ? 0.2325 0.2233 1.8416 -0.0281 0.0259  0.0039  328 LYS A N   
2624  C CA  . LYS A 328 ? 0.2493 0.2248 1.8435 -0.0293 0.0321  0.0059  328 LYS A CA  
2625  C C   . LYS A 328 ? 0.2481 0.2327 1.8464 -0.0292 0.0402  0.0055  328 LYS A C   
2626  O O   . LYS A 328 ? 0.2533 0.2262 1.8378 -0.0273 0.0448  0.0068  328 LYS A O   
2627  C CB  . LYS A 328 ? 0.2580 0.2137 1.8351 -0.0241 0.0262  0.0077  328 LYS A CB  
2628  C CG  . LYS A 328 ? 0.2631 0.2114 1.8397 -0.0237 0.0187  0.0072  328 LYS A CG  
2629  C CD  . LYS A 328 ? 0.2771 0.2204 1.8534 -0.0302 0.0216  0.0068  328 LYS A CD  
2630  C CE  . LYS A 328 ? 0.3051 0.2303 1.8720 -0.0285 0.0154  0.0072  328 LYS A CE  
2631  N NZ  . LYS A 328 ? 0.3142 0.2421 1.8880 -0.0227 0.0065  0.0052  328 LYS A NZ  
2632  N N   . SER A 329 ? 0.2382 0.2437 1.8559 -0.0312 0.0418  0.0033  329 SER A N   
2633  C CA  . SER A 329 ? 0.2395 0.2565 1.8661 -0.0313 0.0498  0.0020  329 SER A CA  
2634  C C   . SER A 329 ? 0.2481 0.2675 1.8795 -0.0403 0.0590  0.0010  329 SER A C   
2635  O O   . SER A 329 ? 0.2460 0.2643 1.8797 -0.0459 0.0568  0.0007  329 SER A O   
2636  C CB  . SER A 329 ? 0.2164 0.2541 1.8622 -0.0275 0.0452  0.0001  329 SER A CB  
2637  O OG  . SER A 329 ? 0.2080 0.2580 1.8672 -0.0321 0.0410  -0.0014 329 SER A OG  
2638  N N   . ILE A 330 ? 0.2509 0.2729 1.8836 -0.0417 0.0699  0.0002  330 ILE A N   
2639  C CA  . ILE A 330 ? 0.2586 0.2846 1.8980 -0.0507 0.0810  -0.0010 330 ILE A CA  
2640  C C   . ILE A 330 ? 0.2482 0.3014 1.9156 -0.0508 0.0844  -0.0052 330 ILE A C   
2641  O O   . ILE A 330 ? 0.2348 0.2961 1.9082 -0.0436 0.0848  -0.0064 330 ILE A O   
2642  C CB  . ILE A 330 ? 0.2953 0.3014 1.9126 -0.0528 0.0924  0.0010  330 ILE A CB  
2643  C CG1 . ILE A 330 ? 0.3224 0.3010 1.9116 -0.0509 0.0866  0.0051  330 ILE A CG1 
2644  C CG2 . ILE A 330 ? 0.3219 0.3306 1.9453 -0.0637 0.1055  0.0000  330 ILE A CG2 
2645  C CD1 . ILE A 330 ? 0.3526 0.3078 1.9156 -0.0536 0.0968  0.0078  330 ILE A CD1 
2646  N N   . HIS A 331 ? 0.2554 0.3218 1.9405 -0.0590 0.0872  -0.0076 331 HIS A N   
2647  C CA  . HIS A 331 ? 0.2369 0.3308 1.9520 -0.0590 0.0865  -0.0119 331 HIS A CA  
2648  C C   . HIS A 331 ? 0.2440 0.3479 1.9746 -0.0694 0.0988  -0.0149 331 HIS A C   
2649  O O   . HIS A 331 ? 0.2420 0.3456 1.9766 -0.0782 0.0977  -0.0155 331 HIS A O   
2650  C CB  . HIS A 331 ? 0.2221 0.3253 1.9465 -0.0582 0.0721  -0.0127 331 HIS A CB  
2651  C CG  . HIS A 331 ? 0.2141 0.3137 1.9303 -0.0485 0.0612  -0.0106 331 HIS A CG  
2652  N ND1 . HIS A 331 ? 0.2140 0.3300 1.9455 -0.0415 0.0546  -0.0121 331 HIS A ND1 
2653  C CD2 . HIS A 331 ? 0.2301 0.3118 1.9256 -0.0448 0.0557  -0.0073 331 HIS A CD2 
2654  C CE1 . HIS A 331 ? 0.2218 0.3288 1.9405 -0.0347 0.0462  -0.0094 331 HIS A CE1 
2655  N NE2 . HIS A 331 ? 0.2327 0.3200 1.9308 -0.0367 0.0468  -0.0068 331 HIS A NE2 
2656  N N   . THR A 332 ? 0.2521 0.3659 1.9936 -0.0686 0.1107  -0.0175 332 THR A N   
2657  C CA  . THR A 332 ? 0.2614 0.3868 2.0209 -0.0791 0.1237  -0.0209 332 THR A CA  
2658  C C   . THR A 332 ? 0.2560 0.4136 2.0537 -0.0790 0.1182  -0.0266 332 THR A C   
2659  O O   . THR A 332 ? 0.2824 0.4564 2.1028 -0.0852 0.1291  -0.0309 332 THR A O   
2660  C CB  . THR A 332 ? 0.2713 0.3908 2.0237 -0.0803 0.1420  -0.0215 332 THR A CB  
2661  O OG1 . THR A 332 ? 0.2726 0.4079 2.0396 -0.0690 0.1380  -0.0244 332 THR A OG1 
2662  C CG2 . THR A 332 ? 0.2904 0.3769 2.0031 -0.0796 0.1470  -0.0161 332 THR A CG2 
2663  N N   . ASN A 333 ? 0.2601 0.4261 2.0647 -0.0731 0.1012  -0.0267 333 ASN A N   
2664  C CA  . ASN A 333 ? 0.2730 0.4673 2.1112 -0.0730 0.0934  -0.0317 333 ASN A CA  
2665  C C   . ASN A 333 ? 0.2956 0.4897 2.1337 -0.0780 0.0799  -0.0316 333 ASN A C   
2666  O O   . ASN A 333 ? 0.3796 0.5526 2.1920 -0.0790 0.0757  -0.0276 333 ASN A O   
2667  C CB  . ASN A 333 ? 0.2716 0.4772 2.1195 -0.0598 0.0870  -0.0326 333 ASN A CB  
2668  C CG  . ASN A 333 ? 0.2912 0.5262 2.1751 -0.0577 0.0790  -0.0379 333 ASN A CG  
2669  O OD1 . ASN A 333 ? 0.3141 0.5540 2.2004 -0.0499 0.0636  -0.0371 333 ASN A OD1 
2670  N ND2 . ASN A 333 ? 0.3240 0.5785 2.2362 -0.0645 0.0887  -0.0433 333 ASN A ND2 
2671  N N   . THR A 334 ? 0.2734 0.4913 2.1407 -0.0809 0.0729  -0.0365 334 THR A N   
2672  C CA  . THR A 334 ? 0.2531 0.4739 2.1228 -0.0848 0.0586  -0.0377 334 THR A CA  
2673  C C   . THR A 334 ? 0.2420 0.4674 2.1099 -0.0739 0.0418  -0.0366 334 THR A C   
2674  O O   . THR A 334 ? 0.2181 0.4445 2.0843 -0.0756 0.0291  -0.0374 334 THR A O   
2675  C CB  . THR A 334 ? 0.2426 0.4854 2.1441 -0.0949 0.0598  -0.0440 334 THR A CB  
2676  O OG1 . THR A 334 ? 0.2208 0.4791 2.1371 -0.0919 0.0421  -0.0470 334 THR A OG1 
2677  C CG2 . THR A 334 ? 0.2450 0.5092 2.1759 -0.0947 0.0712  -0.0482 334 THR A CG2 
2678  N N   . LYS A 335 ? 0.2667 0.4937 2.1338 -0.0628 0.0420  -0.0348 335 LYS A N   
2679  C CA  . LYS A 335 ? 0.2993 0.5278 2.1625 -0.0525 0.0272  -0.0329 335 LYS A CA  
2680  C C   . LYS A 335 ? 0.2971 0.5032 2.1308 -0.0456 0.0288  -0.0272 335 LYS A C   
2681  O O   . LYS A 335 ? 0.3072 0.5082 2.1366 -0.0413 0.0386  -0.0262 335 LYS A O   
2682  C CB  . LYS A 335 ? 0.3452 0.5945 2.2339 -0.0436 0.0232  -0.0357 335 LYS A CB  
2683  C CG  . LYS A 335 ? 0.3942 0.6706 2.3192 -0.0474 0.0198  -0.0422 335 LYS A CG  
2684  C CD  . LYS A 335 ? 0.4424 0.7262 2.3725 -0.0488 0.0014  -0.0435 335 LYS A CD  
2685  C CE  . LYS A 335 ? 0.4998 0.7786 2.4246 -0.0618 0.0023  -0.0451 335 LYS A CE  
2686  N NZ  . LYS A 335 ? 0.5337 0.8322 2.4829 -0.0662 -0.0101 -0.0506 335 LYS A NZ  
2687  N N   . ILE A 336 ? 0.2795 0.4728 2.0938 -0.0449 0.0191  -0.0242 336 ILE A N   
2688  C CA  . ILE A 336 ? 0.2752 0.4477 2.0632 -0.0398 0.0196  -0.0194 336 ILE A CA  
2689  C C   . ILE A 336 ? 0.2590 0.4330 2.0444 -0.0303 0.0083  -0.0172 336 ILE A C   
2690  O O   . ILE A 336 ? 0.2907 0.4664 2.0737 -0.0308 -0.0027 -0.0170 336 ILE A O   
2691  C CB  . ILE A 336 ? 0.2971 0.4540 2.0663 -0.0464 0.0183  -0.0181 336 ILE A CB  
2692  C CG1 . ILE A 336 ? 0.3134 0.4673 2.0849 -0.0561 0.0284  -0.0200 336 ILE A CG1 
2693  C CG2 . ILE A 336 ? 0.3076 0.4444 2.0525 -0.0415 0.0182  -0.0137 336 ILE A CG2 
2694  C CD1 . ILE A 336 ? 0.3317 0.4737 2.0932 -0.0555 0.0413  -0.0179 336 ILE A CD1 
2695  N N   . PRO A 337 ? 0.2222 0.3935 2.0058 -0.0217 0.0106  -0.0154 337 PRO A N   
2696  C CA  . PRO A 337 ? 0.1955 0.3632 1.9724 -0.0131 0.0005  -0.0125 337 PRO A CA  
2697  C C   . PRO A 337 ? 0.2082 0.3598 1.9624 -0.0150 -0.0047 -0.0090 337 PRO A C   
2698  O O   . PRO A 337 ? 0.2015 0.3390 1.9407 -0.0180 0.0017  -0.0077 337 PRO A O   
2699  C CB  . PRO A 337 ? 0.1923 0.3539 1.9659 -0.0055 0.0070  -0.0114 337 PRO A CB  
2700  C CG  . PRO A 337 ? 0.1981 0.3647 1.9812 -0.0093 0.0207  -0.0146 337 PRO A CG  
2701  C CD  . PRO A 337 ? 0.2142 0.3838 2.0000 -0.0202 0.0236  -0.0163 337 PRO A CD  
2702  N N   . LEU A 338 ? 0.2114 0.3652 1.9637 -0.0128 -0.0164 -0.0077 338 LEU A N   
2703  C CA  . LEU A 338 ? 0.2158 0.3562 1.9480 -0.0141 -0.0214 -0.0048 338 LEU A CA  
2704  C C   . LEU A 338 ? 0.2077 0.3408 1.9310 -0.0064 -0.0273 -0.0008 338 LEU A C   
2705  O O   . LEU A 338 ? 0.2063 0.3466 1.9373 -0.0015 -0.0352 -0.0001 338 LEU A O   
2706  C CB  . LEU A 338 ? 0.2218 0.3689 1.9562 -0.0197 -0.0292 -0.0070 338 LEU A CB  
2707  C CG  . LEU A 338 ? 0.2307 0.3654 1.9448 -0.0221 -0.0337 -0.0052 338 LEU A CG  
2708  C CD1 . LEU A 338 ? 0.2262 0.3484 1.9285 -0.0264 -0.0253 -0.0054 338 LEU A CD1 
2709  C CD2 . LEU A 338 ? 0.2357 0.3769 1.9510 -0.0270 -0.0425 -0.0079 338 LEU A CD2 
2710  N N   . GLU A 339 ? 0.2011 0.3190 1.9077 -0.0057 -0.0246 0.0020  339 GLU A N   
2711  C CA  . GLU A 339 ? 0.2033 0.3130 1.9007 0.0000  -0.0299 0.0060  339 GLU A CA  
2712  C C   . GLU A 339 ? 0.1921 0.2888 1.8719 -0.0035 -0.0301 0.0080  339 GLU A C   
2713  O O   . GLU A 339 ? 0.1798 0.2687 1.8536 -0.0058 -0.0237 0.0075  339 GLU A O   
2714  C CB  . GLU A 339 ? 0.2055 0.3101 1.9042 0.0063  -0.0252 0.0069  339 GLU A CB  
2715  C CG  . GLU A 339 ? 0.2094 0.3262 1.9257 0.0120  -0.0256 0.0050  339 GLU A CG  
2716  C CD  . GLU A 339 ? 0.2156 0.3252 1.9303 0.0175  -0.0191 0.0049  339 GLU A CD  
2717  O OE1 . GLU A 339 ? 0.2148 0.3215 1.9272 0.0142  -0.0102 0.0031  339 GLU A OE1 
2718  O OE2 . GLU A 339 ? 0.2199 0.3242 1.9330 0.0245  -0.0229 0.0068  339 GLU A OE2 
2719  N N   . LEU A 340 ? 0.1934 0.2872 1.8646 -0.0036 -0.0374 0.0104  340 LEU A N   
2720  C CA  . LEU A 340 ? 0.2066 0.2887 1.8617 -0.0068 -0.0365 0.0122  340 LEU A CA  
2721  C C   . LEU A 340 ? 0.2204 0.2929 1.8662 -0.0026 -0.0405 0.0170  340 LEU A C   
2722  O O   . LEU A 340 ? 0.2206 0.2951 1.8691 0.0022  -0.0473 0.0193  340 LEU A O   
2723  C CB  . LEU A 340 ? 0.2111 0.2954 1.8601 -0.0127 -0.0398 0.0103  340 LEU A CB  
2724  C CG  . LEU A 340 ? 0.2113 0.3038 1.8687 -0.0178 -0.0370 0.0055  340 LEU A CG  
2725  C CD1 . LEU A 340 ? 0.2227 0.3146 1.8707 -0.0233 -0.0413 0.0036  340 LEU A CD1 
2726  C CD2 . LEU A 340 ? 0.2032 0.2906 1.8609 -0.0200 -0.0280 0.0036  340 LEU A CD2 
2727  N N   . TYR A 341 ? 0.2232 0.2848 1.8584 -0.0048 -0.0365 0.0184  341 TYR A N   
2728  C CA  . TYR A 341 ? 0.2355 0.2863 1.8588 -0.0041 -0.0391 0.0228  341 TYR A CA  
2729  C C   . TYR A 341 ? 0.2500 0.2956 1.8606 -0.0110 -0.0364 0.0224  341 TYR A C   
2730  O O   . TYR A 341 ? 0.2576 0.3024 1.8695 -0.0144 -0.0297 0.0194  341 TYR A O   
2731  C CB  . TYR A 341 ? 0.2310 0.2736 1.8550 -0.0014 -0.0352 0.0241  341 TYR A CB  
2732  C CG  . TYR A 341 ? 0.2279 0.2599 1.8437 0.0013  -0.0392 0.0291  341 TYR A CG  
2733  C CD1 . TYR A 341 ? 0.2403 0.2726 1.8599 0.0081  -0.0455 0.0314  341 TYR A CD1 
2734  C CD2 . TYR A 341 ? 0.2158 0.2374 1.8202 -0.0031 -0.0367 0.0315  341 TYR A CD2 
2735  C CE1 . TYR A 341 ? 0.2459 0.2663 1.8568 0.0108  -0.0499 0.0363  341 TYR A CE1 
2736  C CE2 . TYR A 341 ? 0.2426 0.2526 1.8379 -0.0016 -0.0401 0.0366  341 TYR A CE2 
2737  C CZ  . TYR A 341 ? 0.2586 0.2668 1.8563 0.0055  -0.0472 0.0392  341 TYR A CZ  
2738  O OH  . TYR A 341 ? 0.2987 0.2931 1.8868 0.0075  -0.0511 0.0445  341 TYR A OH  
2739  N N   . ASN A 342 ? 0.2710 0.3122 1.8688 -0.0126 -0.0415 0.0251  342 ASN A N   
2740  C CA  . ASN A 342 ? 0.2985 0.3354 1.8828 -0.0194 -0.0385 0.0238  342 ASN A CA  
2741  C C   . ASN A 342 ? 0.3239 0.3473 1.8908 -0.0216 -0.0380 0.0285  342 ASN A C   
2742  O O   . ASN A 342 ? 0.3229 0.3404 1.8818 -0.0185 -0.0455 0.0334  342 ASN A O   
2743  C CB  . ASN A 342 ? 0.3149 0.3569 1.8943 -0.0214 -0.0450 0.0220  342 ASN A CB  
2744  C CG  . ASN A 342 ? 0.3168 0.3719 1.9130 -0.0209 -0.0450 0.0171  342 ASN A CG  
2745  O OD1 . ASN A 342 ? 0.3509 0.4083 1.9562 -0.0216 -0.0377 0.0143  342 ASN A OD1 
2746  N ND2 . ASN A 342 ? 0.3329 0.3958 1.9330 -0.0202 -0.0531 0.0161  342 ASN A ND2 
2747  N N   . ASP A 343 ? 0.3199 0.3383 1.8807 -0.0272 -0.0292 0.0268  343 ASP A N   
2748  C CA  . ASP A 343 ? 0.3409 0.3462 1.8839 -0.0311 -0.0266 0.0309  343 ASP A CA  
2749  C C   . ASP A 343 ? 0.3444 0.3452 1.8678 -0.0343 -0.0312 0.0318  343 ASP A C   
2750  O O   . ASP A 343 ? 0.3604 0.3693 1.8865 -0.0342 -0.0353 0.0281  343 ASP A O   
2751  C CB  . ASP A 343 ? 0.3560 0.3591 1.9028 -0.0356 -0.0153 0.0284  343 ASP A CB  
2752  C CG  . ASP A 343 ? 0.3709 0.3722 1.9075 -0.0426 -0.0072 0.0245  343 ASP A CG  
2753  O OD1 . ASP A 343 ? 0.3528 0.3598 1.8878 -0.0435 -0.0087 0.0203  343 ASP A OD1 
2754  O OD2 . ASP A 343 ? 0.3794 0.3736 1.9104 -0.0473 0.0010  0.0253  343 ASP A OD2 
2755  N N   . LYS A 344 ? 0.3440 0.3304 1.8464 -0.0377 -0.0305 0.0367  344 LYS A N   
2756  C CA  . LYS A 344 ? 0.3624 0.3400 1.8415 -0.0396 -0.0376 0.0395  344 LYS A CA  
2757  C C   . LYS A 344 ? 0.3614 0.3409 1.8304 -0.0457 -0.0331 0.0336  344 LYS A C   
2758  O O   . LYS A 344 ? 0.3795 0.3496 1.8251 -0.0485 -0.0379 0.0352  344 LYS A O   
2759  C CB  . LYS A 344 ? 0.4023 0.3609 1.8586 -0.0430 -0.0353 0.0465  344 LYS A CB  
2760  C CG  . LYS A 344 ? 0.4148 0.3688 1.8680 -0.0506 -0.0197 0.0445  344 LYS A CG  
2761  C CD  . LYS A 344 ? 0.4638 0.3979 1.8917 -0.0563 -0.0152 0.0510  344 LYS A CD  
2762  C CE  . LYS A 344 ? 0.4891 0.4228 1.9245 -0.0625 0.0003  0.0488  344 LYS A CE  
2763  N NZ  . LYS A 344 ? 0.5016 0.4481 1.9490 -0.0658 0.0102  0.0397  344 LYS A NZ  
2764  N N   . ASP A 345 ? 0.3443 0.3339 1.8289 -0.0476 -0.0241 0.0267  345 ASP A N   
2765  C CA  . ASP A 345 ? 0.3406 0.3303 1.8159 -0.0534 -0.0177 0.0204  345 ASP A CA  
2766  C C   . ASP A 345 ? 0.3231 0.3245 1.8097 -0.0517 -0.0238 0.0148  345 ASP A C   
2767  O O   . ASP A 345 ? 0.3278 0.3275 1.8030 -0.0562 -0.0221 0.0098  345 ASP A O   
2768  C CB  . ASP A 345 ? 0.3337 0.3241 1.8164 -0.0573 -0.0029 0.0162  345 ASP A CB  
2769  C CG  . ASP A 345 ? 0.3515 0.3290 1.8184 -0.0623 0.0058  0.0201  345 ASP A CG  
2770  O OD1 . ASP A 345 ? 0.3636 0.3303 1.8154 -0.0619 0.0001  0.0275  345 ASP A OD1 
2771  O OD2 . ASP A 345 ? 0.3518 0.3298 1.8211 -0.0669 0.0184  0.0153  345 ASP A OD2 
2772  N N   . VAL A 346 ? 0.2919 0.3041 1.7995 -0.0458 -0.0304 0.0157  346 VAL A N   
2773  C CA  . VAL A 346 ? 0.2674 0.2917 1.7897 -0.0443 -0.0356 0.0111  346 VAL A CA  
2774  C C   . VAL A 346 ? 0.2832 0.3078 1.7963 -0.0433 -0.0488 0.0127  346 VAL A C   
2775  O O   . VAL A 346 ? 0.2765 0.3044 1.7969 -0.0379 -0.0575 0.0169  346 VAL A O   
2776  C CB  . VAL A 346 ? 0.2389 0.2733 1.7857 -0.0387 -0.0359 0.0117  346 VAL A CB  
2777  C CG1 . VAL A 346 ? 0.2261 0.2726 1.7881 -0.0378 -0.0406 0.0075  346 VAL A CG1 
2778  C CG2 . VAL A 346 ? 0.2271 0.2611 1.7837 -0.0390 -0.0251 0.0099  346 VAL A CG2 
2779  N N   . LYS A 347 ? 0.3192 0.3407 1.8179 -0.0482 -0.0508 0.0085  347 LYS A N   
2780  C CA  . LYS A 347 ? 0.3531 0.3747 1.8425 -0.0478 -0.0648 0.0091  347 LYS A CA  
2781  C C   . LYS A 347 ? 0.3514 0.3883 1.8619 -0.0475 -0.0705 0.0035  347 LYS A C   
2782  O O   . LYS A 347 ? 0.3651 0.4076 1.8793 -0.0450 -0.0837 0.0044  347 LYS A O   
2783  C CB  . LYS A 347 ? 0.3904 0.3974 1.8484 -0.0539 -0.0644 0.0078  347 LYS A CB  
2784  C CG  . LYS A 347 ? 0.4099 0.4009 1.8462 -0.0553 -0.0577 0.0138  347 LYS A CG  
2785  C CD  . LYS A 347 ? 0.4259 0.4118 1.8591 -0.0496 -0.0674 0.0226  347 LYS A CD  
2786  C CE  . LYS A 347 ? 0.4584 0.4272 1.8706 -0.0520 -0.0601 0.0287  347 LYS A CE  
2787  N NZ  . LYS A 347 ? 0.4898 0.4515 1.8965 -0.0462 -0.0724 0.0370  347 LYS A NZ  
2788  N N   . LYS A 348 ? 0.3365 0.3801 1.8618 -0.0498 -0.0612 -0.0020 348 LYS A N   
2789  C CA  . LYS A 348 ? 0.3371 0.3942 1.8828 -0.0502 -0.0654 -0.0067 348 LYS A CA  
2790  C C   . LYS A 348 ? 0.3084 0.3725 1.8755 -0.0489 -0.0556 -0.0083 348 LYS A C   
2791  O O   . LYS A 348 ? 0.2989 0.3569 1.8631 -0.0496 -0.0453 -0.0087 348 LYS A O   
2792  C CB  . LYS A 348 ? 0.3598 0.4142 1.8944 -0.0568 -0.0678 -0.0135 348 LYS A CB  
2793  C CG  . LYS A 348 ? 0.3686 0.4363 1.9234 -0.0586 -0.0732 -0.0183 348 LYS A CG  
2794  C CD  . LYS A 348 ? 0.4159 0.4801 1.9578 -0.0649 -0.0796 -0.0247 348 LYS A CD  
2795  C CE  . LYS A 348 ? 0.4448 0.4972 1.9712 -0.0697 -0.0686 -0.0296 348 LYS A CE  
2796  N NZ  . LYS A 348 ? 0.4824 0.5317 1.9987 -0.0759 -0.0744 -0.0369 348 LYS A NZ  
2797  N N   . VAL A 349 ? 0.2914 0.3682 1.8799 -0.0472 -0.0590 -0.0093 349 VAL A N   
2798  C CA  . VAL A 349 ? 0.2764 0.3580 1.8821 -0.0468 -0.0503 -0.0109 349 VAL A CA  
2799  C C   . VAL A 349 ? 0.3076 0.3985 1.9267 -0.0510 -0.0528 -0.0162 349 VAL A C   
2800  O O   . VAL A 349 ? 0.3476 0.4487 1.9766 -0.0503 -0.0616 -0.0163 349 VAL A O   
2801  C CB  . VAL A 349 ? 0.2507 0.3373 1.8700 -0.0403 -0.0491 -0.0062 349 VAL A CB  
2802  C CG1 . VAL A 349 ? 0.2255 0.3148 1.8587 -0.0403 -0.0404 -0.0079 349 VAL A CG1 
2803  C CG2 . VAL A 349 ? 0.2668 0.3438 1.8739 -0.0365 -0.0475 -0.0009 349 VAL A CG2 
2804  N N   . VAL A 350 ? 0.3033 0.3906 1.9240 -0.0553 -0.0451 -0.0206 350 VAL A N   
2805  C CA  . VAL A 350 ? 0.2927 0.3868 1.9265 -0.0602 -0.0456 -0.0253 350 VAL A CA  
2806  C C   . VAL A 350 ? 0.2691 0.3627 1.9147 -0.0594 -0.0362 -0.0247 350 VAL A C   
2807  O O   . VAL A 350 ? 0.2622 0.3474 1.9019 -0.0563 -0.0297 -0.0226 350 VAL A O   
2808  C CB  . VAL A 350 ? 0.3095 0.3962 1.9307 -0.0667 -0.0463 -0.0315 350 VAL A CB  
2809  C CG1 . VAL A 350 ? 0.3049 0.3948 1.9384 -0.0726 -0.0446 -0.0366 350 VAL A CG1 
2810  C CG2 . VAL A 350 ? 0.3301 0.4170 1.9383 -0.0680 -0.0572 -0.0323 350 VAL A CG2 
2811  N N   . VAL A 351 ? 0.2549 0.3571 1.9168 -0.0624 -0.0358 -0.0266 351 VAL A N   
2812  C CA  . VAL A 351 ? 0.2402 0.3390 1.9096 -0.0634 -0.0268 -0.0265 351 VAL A CA  
2813  C C   . VAL A 351 ? 0.2469 0.3443 1.9202 -0.0716 -0.0256 -0.0320 351 VAL A C   
2814  O O   . VAL A 351 ? 0.2536 0.3612 1.9367 -0.0761 -0.0312 -0.0351 351 VAL A O   
2815  C CB  . VAL A 351 ? 0.2336 0.3414 1.9179 -0.0598 -0.0240 -0.0231 351 VAL A CB  
2816  C CG1 . VAL A 351 ? 0.2291 0.3298 1.9160 -0.0615 -0.0144 -0.0228 351 VAL A CG1 
2817  C CG2 . VAL A 351 ? 0.2347 0.3430 1.9157 -0.0517 -0.0257 -0.0181 351 VAL A CG2 
2818  N N   . LYS A 352 ? 0.2428 0.3272 1.9098 -0.0733 -0.0186 -0.0332 352 LYS A N   
2819  C CA  . LYS A 352 ? 0.2396 0.3188 1.9086 -0.0809 -0.0166 -0.0380 352 LYS A CA  
2820  C C   . LYS A 352 ? 0.2121 0.2861 1.8875 -0.0820 -0.0085 -0.0357 352 LYS A C   
2821  O O   . LYS A 352 ? 0.2175 0.2860 1.8895 -0.0762 -0.0041 -0.0313 352 LYS A O   
2822  C CB  . LYS A 352 ? 0.2554 0.3212 1.9095 -0.0824 -0.0163 -0.0423 352 LYS A CB  
2823  C CG  . LYS A 352 ? 0.2708 0.3393 1.9171 -0.0856 -0.0239 -0.0469 352 LYS A CG  
2824  C CD  . LYS A 352 ? 0.2876 0.3430 1.9172 -0.0858 -0.0221 -0.0513 352 LYS A CD  
2825  C CE  . LYS A 352 ? 0.3051 0.3629 1.9223 -0.0861 -0.0289 -0.0531 352 LYS A CE  
2826  N NZ  . LYS A 352 ? 0.3125 0.3590 1.9130 -0.0839 -0.0245 -0.0554 352 LYS A NZ  
2827  N N   . PHE A 353 ? 0.1866 0.2613 1.8700 -0.0900 -0.0069 -0.0389 353 PHE A N   
2828  C CA  . PHE A 353 ? 0.1774 0.2417 1.8618 -0.0933 0.0012  -0.0375 353 PHE A CA  
2829  C C   . PHE A 353 ? 0.1914 0.2468 1.8746 -0.1023 0.0014  -0.0428 353 PHE A C   
2830  O O   . PHE A 353 ? 0.1962 0.2625 1.8895 -0.1088 -0.0030 -0.0469 353 PHE A O   
2831  C CB  . PHE A 353 ? 0.1659 0.2414 1.8651 -0.0956 0.0056  -0.0351 353 PHE A CB  
2832  C CG  . PHE A 353 ? 0.1643 0.2268 1.8613 -0.1003 0.0149  -0.0334 353 PHE A CG  
2833  C CD1 . PHE A 353 ? 0.1644 0.2114 1.8484 -0.0948 0.0196  -0.0288 353 PHE A CD1 
2834  C CD2 . PHE A 353 ? 0.1685 0.2347 1.8769 -0.1101 0.0186  -0.0359 353 PHE A CD2 
2835  C CE1 . PHE A 353 ? 0.1750 0.2075 1.8536 -0.0988 0.0275  -0.0265 353 PHE A CE1 
2836  C CE2 . PHE A 353 ? 0.1818 0.2342 1.8858 -0.1148 0.0280  -0.0334 353 PHE A CE2 
2837  C CZ  . PHE A 353 ? 0.1840 0.2183 1.8714 -0.1090 0.0322  -0.0285 353 PHE A CZ  
2838  N N   . ARG A 354 ? 0.1944 0.2301 1.8662 -0.1021 0.0058  -0.0426 354 ARG A N   
2839  C CA  . ARG A 354 ? 0.2076 0.2290 1.8736 -0.1083 0.0059  -0.0476 354 ARG A CA  
2840  C C   . ARG A 354 ? 0.2135 0.2402 1.8772 -0.1103 -0.0015 -0.0541 354 ARG A C   
2841  O O   . ARG A 354 ? 0.2314 0.2592 1.8994 -0.1187 -0.0041 -0.0592 354 ARG A O   
2842  C CB  . ARG A 354 ? 0.2183 0.2359 1.8919 -0.1179 0.0109  -0.0477 354 ARG A CB  
2843  C CG  . ARG A 354 ? 0.2226 0.2272 1.8907 -0.1156 0.0188  -0.0414 354 ARG A CG  
2844  C CD  . ARG A 354 ? 0.2355 0.2382 1.9111 -0.1257 0.0254  -0.0406 354 ARG A CD  
2845  N NE  . ARG A 354 ? 0.2423 0.2357 1.9117 -0.1234 0.0333  -0.0339 354 ARG A NE  
2846  C CZ  . ARG A 354 ? 0.2555 0.2488 1.9307 -0.1315 0.0414  -0.0320 354 ARG A CZ  
2847  N NH1 . ARG A 354 ? 0.2580 0.2621 1.9485 -0.1421 0.0425  -0.0363 354 ARG A NH1 
2848  N NH2 . ARG A 354 ? 0.2710 0.2529 1.9363 -0.1293 0.0488  -0.0260 354 ARG A NH2 
2849  N N   . ASP A 355 ? 0.2100 0.2398 1.8662 -0.1031 -0.0046 -0.0537 355 ASP A N   
2850  C CA  . ASP A 355 ? 0.2225 0.2529 1.8703 -0.1039 -0.0103 -0.0594 355 ASP A CA  
2851  C C   . ASP A 355 ? 0.2400 0.2858 1.8948 -0.1090 -0.0183 -0.0621 355 ASP A C   
2852  O O   . ASP A 355 ? 0.2492 0.2925 1.8940 -0.1107 -0.0234 -0.0674 355 ASP A O   
2853  C CB  . ASP A 355 ? 0.2357 0.2486 1.8742 -0.1069 -0.0085 -0.0655 355 ASP A CB  
2854  C CG  . ASP A 355 ? 0.2388 0.2375 1.8727 -0.1006 -0.0022 -0.0625 355 ASP A CG  
2855  O OD1 . ASP A 355 ? 0.2403 0.2383 1.8681 -0.0932 -0.0013 -0.0616 355 ASP A OD1 
2856  O OD2 . ASP A 355 ? 0.2409 0.2314 1.8786 -0.1030 0.0016  -0.0598 355 ASP A OD2 
2857  N N   . LYS A 356 ? 0.2491 0.3099 1.9201 -0.1105 -0.0192 -0.0587 356 LYS A N   
2858  C CA  . LYS A 356 ? 0.2627 0.3410 1.9449 -0.1138 -0.0278 -0.0607 356 LYS A CA  
2859  C C   . LYS A 356 ? 0.2361 0.3278 1.9227 -0.1058 -0.0307 -0.0551 356 LYS A C   
2860  O O   . LYS A 356 ? 0.2194 0.3116 1.9098 -0.1008 -0.0242 -0.0496 356 LYS A O   
2861  C CB  . LYS A 356 ? 0.3077 0.3952 2.0101 -0.1219 -0.0259 -0.0619 356 LYS A CB  
2862  C CG  . LYS A 356 ? 0.3592 0.4638 2.0756 -0.1274 -0.0364 -0.0666 356 LYS A CG  
2863  C CD  . LYS A 356 ? 0.3919 0.5051 2.1297 -0.1378 -0.0346 -0.0699 356 LYS A CD  
2864  C CE  . LYS A 356 ? 0.4252 0.5452 2.1775 -0.1366 -0.0243 -0.0645 356 LYS A CE  
2865  N NZ  . LYS A 356 ? 0.4627 0.5898 2.2353 -0.1479 -0.0203 -0.0679 356 LYS A NZ  
2866  N N   . VAL A 357 ? 0.2336 0.3345 1.9185 -0.1047 -0.0410 -0.0566 357 VAL A N   
2867  C CA  . VAL A 357 ? 0.2237 0.3357 1.9116 -0.0970 -0.0454 -0.0514 357 VAL A CA  
2868  C C   . VAL A 357 ? 0.2249 0.3550 1.9379 -0.0974 -0.0459 -0.0499 357 VAL A C   
2869  O O   . VAL A 357 ? 0.2133 0.3540 1.9418 -0.1042 -0.0505 -0.0544 357 VAL A O   
2870  C CB  . VAL A 357 ? 0.2285 0.3419 1.9040 -0.0959 -0.0572 -0.0533 357 VAL A CB  
2871  C CG1 . VAL A 357 ? 0.2280 0.3525 1.9083 -0.0884 -0.0635 -0.0480 357 VAL A CG1 
2872  C CG2 . VAL A 357 ? 0.2360 0.3324 1.8862 -0.0948 -0.0548 -0.0546 357 VAL A CG2 
2873  N N   . ILE A 358 ? 0.2259 0.3599 1.9435 -0.0900 -0.0413 -0.0440 358 ILE A N   
2874  C CA  . ILE A 358 ? 0.2166 0.3676 1.9571 -0.0885 -0.0405 -0.0426 358 ILE A CA  
2875  C C   . ILE A 358 ? 0.2251 0.3844 1.9666 -0.0792 -0.0479 -0.0387 358 ILE A C   
2876  O O   . ILE A 358 ? 0.2397 0.4156 2.0018 -0.0772 -0.0509 -0.0389 358 ILE A O   
2877  C CB  . ILE A 358 ? 0.2014 0.3477 1.9467 -0.0888 -0.0269 -0.0398 358 ILE A CB  
2878  C CG1 . ILE A 358 ? 0.2033 0.3388 1.9341 -0.0801 -0.0222 -0.0341 358 ILE A CG1 
2879  C CG2 . ILE A 358 ? 0.1989 0.3332 1.9401 -0.0977 -0.0204 -0.0429 358 ILE A CG2 
2880  C CD1 . ILE A 358 ? 0.2093 0.3380 1.9413 -0.0799 -0.0101 -0.0312 358 ILE A CD1 
2881  N N   . TYR A 359 ? 0.2301 0.3779 1.9506 -0.0736 -0.0502 -0.0354 359 TYR A N   
2882  C CA  . TYR A 359 ? 0.2317 0.3842 1.9501 -0.0655 -0.0581 -0.0315 359 TYR A CA  
2883  C C   . TYR A 359 ? 0.2431 0.3828 1.9362 -0.0645 -0.0640 -0.0306 359 TYR A C   
2884  O O   . TYR A 359 ? 0.2560 0.3816 1.9328 -0.0660 -0.0572 -0.0306 359 TYR A O   
2885  C CB  . TYR A 359 ? 0.2325 0.3835 1.9532 -0.0581 -0.0504 -0.0260 359 TYR A CB  
2886  C CG  . TYR A 359 ? 0.2405 0.3947 1.9597 -0.0493 -0.0578 -0.0216 359 TYR A CG  
2887  C CD1 . TYR A 359 ? 0.2628 0.4038 1.9606 -0.0453 -0.0594 -0.0176 359 TYR A CD1 
2888  C CD2 . TYR A 359 ? 0.2351 0.4049 1.9752 -0.0449 -0.0622 -0.0215 359 TYR A CD2 
2889  C CE1 . TYR A 359 ? 0.2703 0.4117 1.9656 -0.0378 -0.0659 -0.0131 359 TYR A CE1 
2890  C CE2 . TYR A 359 ? 0.2405 0.4115 1.9793 -0.0364 -0.0696 -0.0176 359 TYR A CE2 
2891  C CZ  . TYR A 359 ? 0.2668 0.4225 1.9820 -0.0329 -0.0716 -0.0130 359 TYR A CZ  
2892  O OH  . TYR A 359 ? 0.2602 0.4148 1.9730 -0.0248 -0.0787 -0.0086 359 TYR A OH  
2893  N N   . SER A 360 ? 0.2515 0.3954 1.9411 -0.0611 -0.0762 -0.0294 360 SER A N   
2894  C CA  . SER A 360 ? 0.2702 0.4009 1.9334 -0.0606 -0.0816 -0.0281 360 SER A CA  
2895  C C   . SER A 360 ? 0.2820 0.4149 1.9411 -0.0537 -0.0931 -0.0235 360 SER A C   
2896  O O   . SER A 360 ? 0.2914 0.4297 1.9511 -0.0543 -0.1064 -0.0253 360 SER A O   
2897  C CB  . SER A 360 ? 0.2755 0.4021 1.9293 -0.0686 -0.0860 -0.0346 360 SER A CB  
2898  O OG  . SER A 360 ? 0.2964 0.4114 1.9242 -0.0684 -0.0931 -0.0339 360 SER A OG  
2899  N N   . LYS A 361 ? 0.2891 0.4161 1.9424 -0.0470 -0.0888 -0.0173 361 LYS A N   
2900  C CA  . LYS A 361 ? 0.3033 0.4281 1.9492 -0.0402 -0.0988 -0.0121 361 LYS A CA  
2901  C C   . LYS A 361 ? 0.2896 0.3955 1.9040 -0.0409 -0.0982 -0.0087 361 LYS A C   
2902  O O   . LYS A 361 ? 0.2729 0.3696 1.8785 -0.0423 -0.0864 -0.0079 361 LYS A O   
2903  C CB  . LYS A 361 ? 0.3139 0.4428 1.9735 -0.0324 -0.0940 -0.0074 361 LYS A CB  
2904  C CG  . LYS A 361 ? 0.3478 0.4754 2.0049 -0.0242 -0.1045 -0.0021 361 LYS A CG  
2905  C CD  . LYS A 361 ? 0.3895 0.5350 2.0722 -0.0199 -0.1151 -0.0041 361 LYS A CD  
2906  C CE  . LYS A 361 ? 0.4210 0.5650 2.1054 -0.0100 -0.1232 0.0012  361 LYS A CE  
2907  N NZ  . LYS A 361 ? 0.4720 0.5983 2.1265 -0.0094 -0.1322 0.0060  361 LYS A NZ  
2908  N N   . ASN A 362 ? 0.3061 0.4060 1.9039 -0.0402 -0.1110 -0.0071 362 ASN A N   
2909  C CA  . ASN A 362 ? 0.3416 0.4229 1.9088 -0.0399 -0.1109 -0.0023 362 ASN A CA  
2910  C C   . ASN A 362 ? 0.3549 0.4326 1.9235 -0.0320 -0.1110 0.0053  362 ASN A C   
2911  O O   . ASN A 362 ? 0.3610 0.4468 1.9434 -0.0257 -0.1214 0.0075  362 ASN A O   
2912  C CB  . ASN A 362 ? 0.3776 0.4515 1.9236 -0.0419 -0.1254 -0.0027 362 ASN A CB  
2913  C CG  . ASN A 362 ? 0.4150 0.4883 1.9534 -0.0501 -0.1260 -0.0104 362 ASN A CG  
2914  O OD1 . ASN A 362 ? 0.4469 0.5190 1.9868 -0.0550 -0.1131 -0.0147 362 ASN A OD1 
2915  N ND2 . ASN A 362 ? 0.4386 0.5112 1.9678 -0.0514 -0.1418 -0.0124 362 ASN A ND2 
2916  N N   . ILE A 363 ? 0.3463 0.4115 1.9013 -0.0323 -0.1000 0.0089  363 ILE A N   
2917  C CA  . ILE A 363 ? 0.3600 0.4207 1.9169 -0.0256 -0.0991 0.0156  363 ILE A CA  
2918  C C   . ILE A 363 ? 0.4051 0.4500 1.9360 -0.0240 -0.1087 0.0217  363 ILE A C   
2919  O O   . ILE A 363 ? 0.4336 0.4641 1.9385 -0.0296 -0.1046 0.0224  363 ILE A O   
2920  C CB  . ILE A 363 ? 0.3379 0.3932 1.8950 -0.0270 -0.0836 0.0163  363 ILE A CB  
2921  C CG1 . ILE A 363 ? 0.3064 0.3733 1.8839 -0.0292 -0.0744 0.0106  363 ILE A CG1 
2922  C CG2 . ILE A 363 ? 0.3391 0.3896 1.8994 -0.0203 -0.0834 0.0226  363 ILE A CG2 
2923  C CD1 . ILE A 363 ? 0.2931 0.3755 1.8970 -0.0245 -0.0776 0.0093  363 ILE A CD1 
2924  N N   . THR A 364 ? 0.4142 0.4604 1.9511 -0.0164 -0.1207 0.0261  364 THR A N   
2925  C CA  . THR A 364 ? 0.4670 0.4956 1.9769 -0.0146 -0.1314 0.0325  364 THR A CA  
2926  C C   . THR A 364 ? 0.4640 0.4782 1.9642 -0.0117 -0.1250 0.0397  364 THR A C   
2927  O O   . THR A 364 ? 0.4857 0.4803 1.9564 -0.0154 -0.1234 0.0445  364 THR A O   
2928  C CB  . THR A 364 ? 0.4977 0.5322 2.0149 -0.0080 -0.1509 0.0335  364 THR A CB  
2929  O OG1 . THR A 364 ? 0.5063 0.5558 2.0553 -0.0004 -0.1501 0.0330  364 THR A OG1 
2930  C CG2 . THR A 364 ? 0.5107 0.5550 2.0303 -0.0125 -0.1596 0.0269  364 THR A CG2 
2931  N N   . SER A 365 ? 0.4283 0.4515 1.9525 -0.0058 -0.1208 0.0401  365 SER A N   
2932  C CA  . SER A 365 ? 0.4209 0.4309 1.9383 -0.0035 -0.1144 0.0459  365 SER A CA  
2933  C C   . SER A 365 ? 0.3852 0.4020 1.9178 -0.0059 -0.0986 0.0425  365 SER A C   
2934  O O   . SER A 365 ? 0.3590 0.3916 1.9116 -0.0067 -0.0940 0.0365  365 SER A O   
2935  C CB  . SER A 365 ? 0.4311 0.4394 1.9570 0.0066  -0.1257 0.0506  365 SER A CB  
2936  O OG  . SER A 365 ? 0.4162 0.4432 1.9743 0.0125  -0.1241 0.0463  365 SER A OG  
2937  N N   . GLU A 366 ? 0.4022 0.4055 1.9239 -0.0077 -0.0902 0.0465  366 GLU A N   
2938  C CA  . GLU A 366 ? 0.3786 0.3865 1.9125 -0.0101 -0.0766 0.0434  366 GLU A CA  
2939  C C   . GLU A 366 ? 0.3403 0.3557 1.8962 -0.0023 -0.0775 0.0433  366 GLU A C   
2940  O O   . GLU A 366 ? 0.3639 0.3811 1.9259 0.0048  -0.0875 0.0454  366 GLU A O   
2941  C CB  . GLU A 366 ? 0.3990 0.3910 1.9147 -0.0159 -0.0674 0.0467  366 GLU A CB  
2942  C CG  . GLU A 366 ? 0.4241 0.4015 1.9325 -0.0123 -0.0699 0.0537  366 GLU A CG  
2943  C CD  . GLU A 366 ? 0.4622 0.4284 1.9615 -0.0188 -0.0580 0.0552  366 GLU A CD  
2944  O OE1 . GLU A 366 ? 0.4628 0.4375 1.9786 -0.0199 -0.0492 0.0508  366 GLU A OE1 
2945  O OE2 . GLU A 366 ? 0.5129 0.4621 1.9892 -0.0232 -0.0572 0.0605  366 GLU A OE2 
2946  N N   . GLY A 367 ? 0.3079 0.3279 1.8760 -0.0034 -0.0672 0.0401  367 GLY A N   
2947  C CA  . GLY A 367 ? 0.2903 0.3133 1.8742 0.0030  -0.0659 0.0400  367 GLY A CA  
2948  C C   . GLY A 367 ? 0.2742 0.3145 1.8793 0.0054  -0.0644 0.0344  367 GLY A C   
2949  O O   . GLY A 367 ? 0.2887 0.3372 1.8968 0.0005  -0.0610 0.0301  367 GLY A O   
2950  N N   . TYR A 368 ? 0.2711 0.3155 1.8899 0.0129  -0.0666 0.0343  368 TYR A N   
2951  C CA  . TYR A 368 ? 0.2461 0.3060 1.8851 0.0156  -0.0644 0.0293  368 TYR A CA  
2952  C C   . TYR A 368 ? 0.2483 0.3204 1.8943 0.0155  -0.0724 0.0274  368 TYR A C   
2953  O O   . TYR A 368 ? 0.2685 0.3356 1.9046 0.0165  -0.0819 0.0306  368 TYR A O   
2954  C CB  . TYR A 368 ? 0.2431 0.3032 1.8934 0.0242  -0.0648 0.0295  368 TYR A CB  
2955  C CG  . TYR A 368 ? 0.2252 0.3007 1.8960 0.0269  -0.0605 0.0242  368 TYR A CG  
2956  C CD1 . TYR A 368 ? 0.2145 0.3039 1.9013 0.0313  -0.0666 0.0221  368 TYR A CD1 
2957  C CD2 . TYR A 368 ? 0.2173 0.2925 1.8912 0.0253  -0.0503 0.0214  368 TYR A CD2 
2958  C CE1 . TYR A 368 ? 0.2093 0.3129 1.9158 0.0332  -0.0610 0.0170  368 TYR A CE1 
2959  C CE2 . TYR A 368 ? 0.2128 0.3000 1.9026 0.0271  -0.0450 0.0169  368 TYR A CE2 
2960  C CZ  . TYR A 368 ? 0.2073 0.3091 1.9141 0.0308  -0.0495 0.0146  368 TYR A CZ  
2961  O OH  . TYR A 368 ? 0.2042 0.3180 1.9274 0.0317  -0.0424 0.0099  368 TYR A OH  
2962  N N   . MET A 369 ? 0.2425 0.3292 1.9046 0.0138  -0.0684 0.0221  369 MET A N   
2963  C CA  . MET A 369 ? 0.2447 0.3447 1.9161 0.0116  -0.0746 0.0189  369 MET A CA  
2964  C C   . MET A 369 ? 0.2125 0.3264 1.9038 0.0104  -0.0665 0.0136  369 MET A C   
2965  O O   . MET A 369 ? 0.2040 0.3139 1.8919 0.0064  -0.0565 0.0123  369 MET A O   
2966  C CB  . MET A 369 ? 0.2780 0.3729 1.9327 0.0034  -0.0757 0.0186  369 MET A CB  
2967  C CG  . MET A 369 ? 0.3191 0.4246 1.9791 0.0009  -0.0849 0.0155  369 MET A CG  
2968  S SD  . MET A 369 ? 0.3799 0.5001 2.0559 -0.0064 -0.0783 0.0082  369 MET A SD  
2969  C CE  . MET A 369 ? 0.3470 0.4515 2.0019 -0.0128 -0.0673 0.0089  369 MET A CE  
2970  N N   . ALA A 370 ? 0.2045 0.3337 1.9165 0.0143  -0.0708 0.0107  370 ALA A N   
2971  C CA  . ALA A 370 ? 0.1896 0.3323 1.9210 0.0123  -0.0621 0.0056  370 ALA A CA  
2972  C C   . ALA A 370 ? 0.1786 0.3381 1.9263 0.0085  -0.0679 0.0012  370 ALA A C   
2973  O O   . ALA A 370 ? 0.1732 0.3353 1.9200 0.0101  -0.0806 0.0021  370 ALA A O   
2974  C CB  . ALA A 370 ? 0.1871 0.3331 1.9315 0.0204  -0.0579 0.0051  370 ALA A CB  
2975  N N   . ASP A 371 ? 0.1770 0.3464 1.9379 0.0030  -0.0587 -0.0033 371 ASP A N   
2976  C CA  . ASP A 371 ? 0.1814 0.3662 1.9584 -0.0032 -0.0616 -0.0083 371 ASP A CA  
2977  C C   . ASP A 371 ? 0.1786 0.3692 1.9670 -0.0088 -0.0477 -0.0120 371 ASP A C   
2978  O O   . ASP A 371 ? 0.1889 0.3725 1.9734 -0.0065 -0.0373 -0.0107 371 ASP A O   
2979  C CB  . ASP A 371 ? 0.1884 0.3666 1.9491 -0.0104 -0.0680 -0.0084 371 ASP A CB  
2980  C CG  . ASP A 371 ? 0.2065 0.3986 1.9804 -0.0133 -0.0796 -0.0123 371 ASP A CG  
2981  O OD1 . ASP A 371 ? 0.2282 0.4365 2.0257 -0.0168 -0.0764 -0.0173 371 ASP A OD1 
2982  O OD2 . ASP A 371 ? 0.2213 0.4078 1.9817 -0.0124 -0.0920 -0.0104 371 ASP A OD2 
2983  N N   . GLU A 372 ? 0.1820 0.3836 1.9826 -0.0168 -0.0477 -0.0166 372 GLU A N   
2984  C CA  . GLU A 372 ? 0.1793 0.3848 1.9892 -0.0238 -0.0345 -0.0198 372 GLU A CA  
2985  C C   . GLU A 372 ? 0.1772 0.3788 1.9799 -0.0343 -0.0347 -0.0221 372 GLU A C   
2986  O O   . GLU A 372 ? 0.1757 0.3823 1.9796 -0.0368 -0.0460 -0.0239 372 GLU A O   
2987  C CB  . GLU A 372 ? 0.1883 0.4164 2.0302 -0.0247 -0.0331 -0.0250 372 GLU A CB  
2988  C CG  . GLU A 372 ? 0.1960 0.4313 2.0525 -0.0168 -0.0258 -0.0254 372 GLU A CG  
2989  C CD  . GLU A 372 ? 0.2203 0.4809 2.1114 -0.0179 -0.0279 -0.0315 372 GLU A CD  
2990  O OE1 . GLU A 372 ? 0.2303 0.4997 2.1290 -0.0202 -0.0414 -0.0334 372 GLU A OE1 
2991  O OE2 . GLU A 372 ? 0.2581 0.5295 2.1682 -0.0164 -0.0167 -0.0345 372 GLU A OE2 
2992  N N   . LEU A 373 ? 0.1730 0.3653 1.9684 -0.0403 -0.0225 -0.0223 373 LEU A N   
2993  C CA  . LEU A 373 ? 0.1808 0.3698 1.9731 -0.0507 -0.0205 -0.0252 373 LEU A CA  
2994  C C   . LEU A 373 ? 0.1836 0.3876 2.0004 -0.0570 -0.0134 -0.0297 373 LEU A C   
2995  O O   . LEU A 373 ? 0.1741 0.3826 2.0005 -0.0545 -0.0037 -0.0293 373 LEU A O   
2996  C CB  . LEU A 373 ? 0.1747 0.3430 1.9447 -0.0536 -0.0123 -0.0228 373 LEU A CB  
2997  C CG  . LEU A 373 ? 0.1834 0.3369 1.9312 -0.0478 -0.0164 -0.0188 373 LEU A CG  
2998  C CD1 . LEU A 373 ? 0.1925 0.3280 1.9235 -0.0507 -0.0083 -0.0175 373 LEU A CD1 
2999  C CD2 . LEU A 373 ? 0.1866 0.3402 1.9266 -0.0484 -0.0281 -0.0196 373 LEU A CD2 
3000  N N   . THR A 374 ? 0.1909 0.4010 2.0159 -0.0660 -0.0171 -0.0340 374 THR A N   
3001  C CA  . THR A 374 ? 0.2155 0.4345 2.0590 -0.0749 -0.0074 -0.0378 374 THR A CA  
3002  C C   . THR A 374 ? 0.2245 0.4251 2.0505 -0.0839 -0.0007 -0.0377 374 THR A C   
3003  O O   . THR A 374 ? 0.2186 0.4112 2.0326 -0.0874 -0.0083 -0.0390 374 THR A O   
3004  C CB  . THR A 374 ? 0.2385 0.4809 2.1107 -0.0784 -0.0164 -0.0437 374 THR A CB  
3005  O OG1 . THR A 374 ? 0.2436 0.4808 2.1066 -0.0845 -0.0266 -0.0461 374 THR A OG1 
3006  C CG2 . THR A 374 ? 0.2535 0.5104 2.1386 -0.0677 -0.0278 -0.0434 374 THR A CG2 
3007  N N   . ILE A 375 ? 0.2401 0.4332 2.0642 -0.0875 0.0137  -0.0363 375 ILE A N   
3008  C CA  . ILE A 375 ? 0.2713 0.4466 2.0812 -0.0964 0.0210  -0.0361 375 ILE A CA  
3009  C C   . ILE A 375 ? 0.2923 0.4775 2.1228 -0.1075 0.0300  -0.0400 375 ILE A C   
3010  O O   . ILE A 375 ? 0.2821 0.4861 2.1357 -0.1070 0.0343  -0.0420 375 ILE A O   
3011  C CB  . ILE A 375 ? 0.2699 0.4241 2.0563 -0.0914 0.0295  -0.0305 375 ILE A CB  
3012  C CG1 . ILE A 375 ? 0.2741 0.4338 2.0681 -0.0879 0.0403  -0.0288 375 ILE A CG1 
3013  C CG2 . ILE A 375 ? 0.2687 0.4137 2.0370 -0.0821 0.0206  -0.0274 375 ILE A CG2 
3014  C CD1 . ILE A 375 ? 0.2825 0.4196 2.0532 -0.0863 0.0502  -0.0241 375 ILE A CD1 
3015  N N   . ASP A 376 ? 0.3182 0.4903 2.1410 -0.1177 0.0339  -0.0412 376 ASP A N   
3016  C CA  . ASP A 376 ? 0.3323 0.5089 2.1706 -0.1293 0.0455  -0.0437 376 ASP A CA  
3017  C C   . ASP A 376 ? 0.3524 0.5016 2.1662 -0.1332 0.0576  -0.0391 376 ASP A C   
3018  O O   . ASP A 376 ? 0.4410 0.5736 2.2423 -0.1401 0.0567  -0.0395 376 ASP A O   
3019  C CB  . ASP A 376 ? 0.3449 0.5334 2.2017 -0.1397 0.0383  -0.0502 376 ASP A CB  
3020  C CG  . ASP A 376 ? 0.3710 0.5755 2.2560 -0.1509 0.0485  -0.0543 376 ASP A CG  
3021  O OD1 . ASP A 376 ? 0.3835 0.5891 2.2721 -0.1505 0.0626  -0.0519 376 ASP A OD1 
3022  O OD2 . ASP A 376 ? 0.3690 0.5852 2.2729 -0.1603 0.0426  -0.0603 376 ASP A OD2 
3023  N N   . PRO A 377 ? 0.2985 0.4399 2.1023 -0.1286 0.0685  -0.0345 377 PRO A N   
3024  C CA  . PRO A 377 ? 0.2854 0.3991 2.0643 -0.1324 0.0789  -0.0299 377 PRO A CA  
3025  C C   . PRO A 377 ? 0.2724 0.3824 2.0578 -0.1459 0.0930  -0.0308 377 PRO A C   
3026  O O   . PRO A 377 ? 0.2696 0.3968 2.0754 -0.1496 0.1028  -0.0329 377 PRO A O   
3027  C CB  . PRO A 377 ? 0.2900 0.3980 2.0553 -0.1213 0.0830  -0.0253 377 PRO A CB  
3028  C CG  . PRO A 377 ? 0.2847 0.4207 2.0768 -0.1173 0.0837  -0.0286 377 PRO A CG  
3029  C CD  . PRO A 377 ? 0.2839 0.4393 2.0964 -0.1187 0.0700  -0.0336 377 PRO A CD  
3030  N N   . VAL A 378 ? 0.2687 0.3545 2.0355 -0.1530 0.0946  -0.0289 378 VAL A N   
3031  C CA  . VAL A 378 ? 0.2749 0.3488 2.0401 -0.1665 0.1081  -0.0283 378 VAL A CA  
3032  C C   . VAL A 378 ? 0.2974 0.3470 2.0353 -0.1640 0.1199  -0.0214 378 VAL A C   
3033  O O   . VAL A 378 ? 0.3203 0.3490 2.0320 -0.1553 0.1141  -0.0169 378 VAL A O   
3034  C CB  . VAL A 378 ? 0.2639 0.3203 2.0203 -0.1748 0.1026  -0.0297 378 VAL A CB  
3035  C CG1 . VAL A 378 ? 0.2876 0.3311 2.0431 -0.1899 0.1166  -0.0289 378 VAL A CG1 
3036  C CG2 . VAL A 378 ? 0.2414 0.3169 2.0177 -0.1760 0.0887  -0.0365 378 VAL A CG2 
3037  N N   . GLY A 379 ? 0.3066 0.3591 2.0508 -0.1719 0.1362  -0.0210 379 GLY A N   
3038  C CA  . GLY A 379 ? 0.3273 0.3564 2.0444 -0.1710 0.1489  -0.0149 379 GLY A CA  
3039  C C   . GLY A 379 ? 0.3225 0.3478 2.0235 -0.1552 0.1427  -0.0116 379 GLY A C   
3040  O O   . GLY A 379 ? 0.3132 0.3610 2.0309 -0.1481 0.1427  -0.0142 379 GLY A O   
3041  N N   . ILE A 380 ? 0.3307 0.3262 1.9995 -0.1500 0.1373  -0.0062 380 ILE A N   
3042  C CA  . ILE A 380 ? 0.3134 0.3037 1.9673 -0.1355 0.1282  -0.0036 380 ILE A CA  
3043  C C   . ILE A 380 ? 0.3105 0.2917 1.9572 -0.1307 0.1125  -0.0034 380 ILE A C   
3044  O O   . ILE A 380 ? 0.3373 0.2925 1.9639 -0.1339 0.1113  -0.0004 380 ILE A O   
3045  C CB  . ILE A 380 ? 0.3299 0.2925 1.9511 -0.1325 0.1359  0.0025  380 ILE A CB  
3046  C CG1 . ILE A 380 ? 0.3388 0.3064 1.9622 -0.1376 0.1539  0.0024  380 ILE A CG1 
3047  C CG2 . ILE A 380 ? 0.3211 0.2802 1.9305 -0.1178 0.1240  0.0043  380 ILE A CG2 
3048  C CD1 . ILE A 380 ? 0.3637 0.2993 1.9496 -0.1363 0.1619  0.0085  380 ILE A CD1 
3049  N N   . GLU A 381 ? 0.2879 0.2881 1.9487 -0.1222 0.1007  -0.0065 381 GLU A N   
3050  C CA  . GLU A 381 ? 0.2791 0.2754 1.9385 -0.1201 0.0878  -0.0081 381 GLU A CA  
3051  C C   . GLU A 381 ? 0.2685 0.2631 1.9186 -0.1069 0.0776  -0.0065 381 GLU A C   
3052  O O   . GLU A 381 ? 0.2564 0.2710 1.9197 -0.1008 0.0744  -0.0081 381 GLU A O   
3053  C CB  . GLU A 381 ? 0.2633 0.2848 1.9498 -0.1248 0.0826  -0.0143 381 GLU A CB  
3054  C CG  . GLU A 381 ? 0.2566 0.2722 1.9400 -0.1246 0.0712  -0.0168 381 GLU A CG  
3055  C CD  . GLU A 381 ? 0.2477 0.2843 1.9541 -0.1309 0.0659  -0.0232 381 GLU A CD  
3056  O OE1 . GLU A 381 ? 0.2520 0.2985 1.9746 -0.1413 0.0727  -0.0257 381 GLU A OE1 
3057  O OE2 . GLU A 381 ? 0.2336 0.2755 1.9407 -0.1256 0.0547  -0.0257 381 GLU A OE2 
3058  N N   . ASP A 382 ? 0.2757 0.2465 1.9046 -0.1028 0.0723  -0.0036 382 ASP A N   
3059  C CA  . ASP A 382 ? 0.2634 0.2346 1.8876 -0.0915 0.0619  -0.0033 382 ASP A CA  
3060  C C   . ASP A 382 ? 0.2478 0.2353 1.8876 -0.0914 0.0534  -0.0082 382 ASP A C   
3061  O O   . ASP A 382 ? 0.2484 0.2354 1.8937 -0.0991 0.0532  -0.0112 382 ASP A O   
3062  C CB  . ASP A 382 ? 0.2789 0.2227 1.8801 -0.0868 0.0579  0.0002  382 ASP A CB  
3063  C CG  . ASP A 382 ? 0.2850 0.2111 1.8794 -0.0926 0.0564  -0.0005 382 ASP A CG  
3064  O OD1 . ASP A 382 ? 0.2990 0.2190 1.8925 -0.1025 0.0644  -0.0001 382 ASP A OD1 
3065  O OD2 . ASP A 382 ? 0.2713 0.1902 1.8620 -0.0871 0.0478  -0.0019 382 ASP A OD2 
3066  N N   . MET A 383 ? 0.2400 0.2410 1.8858 -0.0833 0.0466  -0.0090 383 MET A N   
3067  C CA  . MET A 383 ? 0.2449 0.2586 1.9012 -0.0831 0.0386  -0.0132 383 MET A CA  
3068  C C   . MET A 383 ? 0.2577 0.2701 1.9077 -0.0733 0.0314  -0.0124 383 MET A C   
3069  O O   . MET A 383 ? 0.2890 0.3043 1.9372 -0.0669 0.0316  -0.0096 383 MET A O   
3070  C CB  . MET A 383 ? 0.2424 0.2812 1.9188 -0.0855 0.0381  -0.0160 383 MET A CB  
3071  C CG  . MET A 383 ? 0.2627 0.3075 1.9504 -0.0952 0.0464  -0.0173 383 MET A CG  
3072  S SD  . MET A 383 ? 0.2444 0.3206 1.9596 -0.0962 0.0458  -0.0206 383 MET A SD  
3073  C CE  . MET A 383 ? 0.2352 0.3227 1.9587 -0.0975 0.0328  -0.0256 383 MET A CE  
3074  N N   . GLU A 384 ? 0.2554 0.2623 1.9020 -0.0727 0.0259  -0.0151 384 GLU A N   
3075  C CA  . GLU A 384 ? 0.2382 0.2496 1.8838 -0.0655 0.0197  -0.0158 384 GLU A CA  
3076  C C   . GLU A 384 ? 0.2170 0.2471 1.8736 -0.0676 0.0156  -0.0190 384 GLU A C   
3077  O O   . GLU A 384 ? 0.2231 0.2544 1.8822 -0.0732 0.0138  -0.0232 384 GLU A O   
3078  C CB  . GLU A 384 ? 0.2508 0.2458 1.8871 -0.0634 0.0172  -0.0174 384 GLU A CB  
3079  C CG  . GLU A 384 ? 0.2382 0.2381 1.8749 -0.0576 0.0123  -0.0193 384 GLU A CG  
3080  C CD  . GLU A 384 ? 0.2493 0.2348 1.8801 -0.0542 0.0106  -0.0214 384 GLU A CD  
3081  O OE1 . GLU A 384 ? 0.2386 0.2134 1.8666 -0.0584 0.0115  -0.0240 384 GLU A OE1 
3082  O OE2 . GLU A 384 ? 0.2672 0.2531 1.8977 -0.0475 0.0081  -0.0209 384 GLU A OE2 
3083  N N   . LEU A 385 ? 0.1931 0.2361 1.8552 -0.0630 0.0137  -0.0171 385 LEU A N   
3084  C CA  . LEU A 385 ? 0.1773 0.2355 1.8467 -0.0629 0.0080  -0.0192 385 LEU A CA  
3085  C C   . LEU A 385 ? 0.1818 0.2351 1.8423 -0.0587 0.0040  -0.0198 385 LEU A C   
3086  O O   . LEU A 385 ? 0.1770 0.2229 1.8316 -0.0530 0.0049  -0.0172 385 LEU A O   
3087  C CB  . LEU A 385 ? 0.1596 0.2311 1.8377 -0.0589 0.0076  -0.0165 385 LEU A CB  
3088  C CG  . LEU A 385 ? 0.1566 0.2340 1.8450 -0.0623 0.0138  -0.0161 385 LEU A CG  
3089  C CD1 . LEU A 385 ? 0.1482 0.2381 1.8455 -0.0566 0.0133  -0.0141 385 LEU A CD1 
3090  C CD2 . LEU A 385 ? 0.1614 0.2470 1.8609 -0.0711 0.0135  -0.0202 385 LEU A CD2 
3091  N N   . ALA A 386 ? 0.1890 0.2459 1.8483 -0.0617 -0.0002 -0.0236 386 ALA A N   
3092  C CA  . ALA A 386 ? 0.1948 0.2455 1.8448 -0.0588 -0.0018 -0.0250 386 ALA A CA  
3093  C C   . ALA A 386 ? 0.2016 0.2620 1.8499 -0.0573 -0.0070 -0.0245 386 ALA A C   
3094  O O   . ALA A 386 ? 0.2248 0.2902 1.8723 -0.0614 -0.0112 -0.0277 386 ALA A O   
3095  C CB  . ALA A 386 ? 0.2079 0.2492 1.8530 -0.0633 -0.0008 -0.0302 386 ALA A CB  
3096  N N   . PHE A 387 ? 0.1952 0.2563 1.8414 -0.0514 -0.0072 -0.0206 387 PHE A N   
3097  C CA  . PHE A 387 ? 0.2046 0.2720 1.8472 -0.0495 -0.0120 -0.0189 387 PHE A CA  
3098  C C   . PHE A 387 ? 0.2054 0.2664 1.8361 -0.0506 -0.0117 -0.0215 387 PHE A C   
3099  O O   . PHE A 387 ? 0.2016 0.2547 1.8298 -0.0493 -0.0070 -0.0227 387 PHE A O   
3100  C CB  . PHE A 387 ? 0.2105 0.2793 1.8554 -0.0433 -0.0118 -0.0137 387 PHE A CB  
3101  C CG  . PHE A 387 ? 0.2110 0.2879 1.8670 -0.0417 -0.0123 -0.0116 387 PHE A CG  
3102  C CD1 . PHE A 387 ? 0.2136 0.2886 1.8754 -0.0435 -0.0073 -0.0123 387 PHE A CD1 
3103  C CD2 . PHE A 387 ? 0.2050 0.2907 1.8654 -0.0384 -0.0172 -0.0090 387 PHE A CD2 
3104  C CE1 . PHE A 387 ? 0.2097 0.2923 1.8815 -0.0424 -0.0058 -0.0109 387 PHE A CE1 
3105  C CE2 . PHE A 387 ? 0.2072 0.3013 1.8797 -0.0365 -0.0165 -0.0080 387 PHE A CE2 
3106  C CZ  . PHE A 387 ? 0.2068 0.2999 1.8852 -0.0387 -0.0101 -0.0091 387 PHE A CZ  
3107  N N   . GLU A 388 ? 0.2142 0.2786 1.8376 -0.0526 -0.0167 -0.0222 388 GLU A N   
3108  C CA  . GLU A 388 ? 0.2209 0.2788 1.8303 -0.0541 -0.0154 -0.0245 388 GLU A CA  
3109  C C   . GLU A 388 ? 0.2235 0.2831 1.8239 -0.0523 -0.0202 -0.0202 388 GLU A C   
3110  O O   . GLU A 388 ? 0.2289 0.2945 1.8292 -0.0530 -0.0280 -0.0192 388 GLU A O   
3111  C CB  . GLU A 388 ? 0.2330 0.2882 1.8358 -0.0600 -0.0167 -0.0308 388 GLU A CB  
3112  C CG  . GLU A 388 ? 0.2303 0.2812 1.8401 -0.0623 -0.0124 -0.0353 388 GLU A CG  
3113  C CD  . GLU A 388 ? 0.2414 0.2905 1.8475 -0.0688 -0.0152 -0.0415 388 GLU A CD  
3114  O OE1 . GLU A 388 ? 0.2444 0.2982 1.8447 -0.0716 -0.0222 -0.0424 388 GLU A OE1 
3115  O OE2 . GLU A 388 ? 0.2459 0.2878 1.8545 -0.0708 -0.0111 -0.0457 388 GLU A OE2 
3116  N N   . PHE A 389 ? 0.2138 0.2676 1.8069 -0.0502 -0.0160 -0.0180 389 PHE A N   
3117  C CA  . PHE A 389 ? 0.2249 0.2766 1.8060 -0.0493 -0.0195 -0.0137 389 PHE A CA  
3118  C C   . PHE A 389 ? 0.2483 0.2923 1.8105 -0.0539 -0.0173 -0.0170 389 PHE A C   
3119  O O   . PHE A 389 ? 0.2526 0.2917 1.8128 -0.0556 -0.0089 -0.0210 389 PHE A O   
3120  C CB  . PHE A 389 ? 0.2239 0.2734 1.8092 -0.0451 -0.0155 -0.0091 389 PHE A CB  
3121  C CG  . PHE A 389 ? 0.2170 0.2724 1.8181 -0.0405 -0.0173 -0.0064 389 PHE A CG  
3122  C CD1 . PHE A 389 ? 0.2158 0.2720 1.8279 -0.0399 -0.0132 -0.0090 389 PHE A CD1 
3123  C CD2 . PHE A 389 ? 0.2200 0.2788 1.8236 -0.0366 -0.0231 -0.0014 389 PHE A CD2 
3124  C CE1 . PHE A 389 ? 0.1972 0.2571 1.8204 -0.0362 -0.0139 -0.0066 389 PHE A CE1 
3125  C CE2 . PHE A 389 ? 0.2141 0.2778 1.8311 -0.0325 -0.0233 0.0002  389 PHE A CE2 
3126  C CZ  . PHE A 389 ? 0.1899 0.2538 1.8156 -0.0326 -0.0183 -0.0024 389 PHE A CZ  
3127  N N   . TYR A 390 ? 0.2764 0.3186 1.8244 -0.0555 -0.0249 -0.0153 390 TYR A N   
3128  C CA  . TYR A 390 ? 0.3189 0.3519 1.8445 -0.0603 -0.0237 -0.0183 390 TYR A CA  
3129  C C   . TYR A 390 ? 0.3440 0.3691 1.8521 -0.0597 -0.0250 -0.0121 390 TYR A C   
3130  O O   . TYR A 390 ? 0.3459 0.3735 1.8588 -0.0555 -0.0312 -0.0058 390 TYR A O   
3131  C CB  . TYR A 390 ? 0.3452 0.3795 1.8635 -0.0638 -0.0329 -0.0222 390 TYR A CB  
3132  C CG  . TYR A 390 ? 0.3436 0.3832 1.8760 -0.0661 -0.0316 -0.0289 390 TYR A CG  
3133  C CD1 . TYR A 390 ? 0.3316 0.3814 1.8866 -0.0635 -0.0334 -0.0277 390 TYR A CD1 
3134  C CD2 . TYR A 390 ? 0.3637 0.3967 1.8859 -0.0710 -0.0277 -0.0365 390 TYR A CD2 
3135  C CE1 . TYR A 390 ? 0.3495 0.4019 1.9159 -0.0663 -0.0316 -0.0331 390 TYR A CE1 
3136  C CE2 . TYR A 390 ? 0.3548 0.3903 1.8892 -0.0733 -0.0264 -0.0424 390 TYR A CE2 
3137  C CZ  . TYR A 390 ? 0.3499 0.3950 1.9063 -0.0712 -0.0285 -0.0403 390 TYR A CZ  
3138  O OH  . TYR A 390 ? 0.3259 0.3722 1.8938 -0.0740 -0.0272 -0.0450 390 TYR A OH  
3139  N N   . ASP A 391 ? 0.3720 0.3863 1.8586 -0.0641 -0.0188 -0.0142 391 ASP A N   
3140  C CA  . ASP A 391 ? 0.3918 0.3952 1.8577 -0.0652 -0.0179 -0.0084 391 ASP A CA  
3141  C C   . ASP A 391 ? 0.4178 0.4121 1.8568 -0.0686 -0.0265 -0.0085 391 ASP A C   
3142  O O   . ASP A 391 ? 0.4154 0.4145 1.8566 -0.0691 -0.0354 -0.0124 391 ASP A O   
3143  C CB  . ASP A 391 ? 0.4075 0.4058 1.8718 -0.0676 -0.0027 -0.0100 391 ASP A CB  
3144  C CG  . ASP A 391 ? 0.4490 0.4403 1.8977 -0.0733 0.0070  -0.0174 391 ASP A CG  
3145  O OD1 . ASP A 391 ? 0.4770 0.4680 1.9189 -0.0753 0.0022  -0.0229 391 ASP A OD1 
3146  O OD2 . ASP A 391 ? 0.4676 0.4537 1.9116 -0.0759 0.0195  -0.0181 391 ASP A OD2 
3147  N N   . SER A 392 ? 0.4576 0.4376 1.8702 -0.0713 -0.0244 -0.0043 392 SER A N   
3148  C CA  . SER A 392 ? 0.5064 0.4751 1.8901 -0.0736 -0.0350 -0.0026 392 SER A CA  
3149  C C   . SER A 392 ? 0.5472 0.5119 1.9166 -0.0791 -0.0328 -0.0116 392 SER A C   
3150  O O   . SER A 392 ? 0.5603 0.5222 1.9166 -0.0801 -0.0457 -0.0130 392 SER A O   
3151  C CB  . SER A 392 ? 0.5247 0.4763 1.8808 -0.0757 -0.0324 0.0048  392 SER A CB  
3152  O OG  . SER A 392 ? 0.5342 0.4751 1.8714 -0.0823 -0.0167 0.0008  392 SER A OG  
3153  N N   . ASP A 393 ? 0.5841 0.5485 1.9568 -0.0823 -0.0169 -0.0181 393 ASP A N   
3154  C CA  . ASP A 393 ? 0.6227 0.5822 1.9827 -0.0872 -0.0121 -0.0277 393 ASP A CA  
3155  C C   . ASP A 393 ? 0.6193 0.5920 2.0044 -0.0855 -0.0172 -0.0340 393 ASP A C   
3156  O O   . ASP A 393 ? 0.6561 0.6254 2.0337 -0.0891 -0.0159 -0.0424 393 ASP A O   
3157  C CB  . ASP A 393 ? 0.6410 0.5948 1.9959 -0.0907 0.0075  -0.0326 393 ASP A CB  
3158  C CG  . ASP A 393 ? 0.6923 0.6311 2.0188 -0.0945 0.0149  -0.0272 393 ASP A CG  
3159  O OD1 . ASP A 393 ? 0.7432 0.6680 2.0371 -0.0976 0.0073  -0.0251 393 ASP A OD1 
3160  O OD2 . ASP A 393 ? 0.6884 0.6287 2.0250 -0.0945 0.0274  -0.0250 393 ASP A OD2 
3161  N N   . ASN A 394 ? 0.6015 0.5877 2.0151 -0.0803 -0.0226 -0.0300 394 ASN A N   
3162  C CA  . ASN A 394 ? 0.5760 0.5743 2.0130 -0.0791 -0.0283 -0.0343 394 ASN A CA  
3163  C C   . ASN A 394 ? 0.5512 0.5524 2.0045 -0.0792 -0.0153 -0.0405 394 ASN A C   
3164  O O   . ASN A 394 ? 0.5533 0.5559 2.0124 -0.0814 -0.0156 -0.0477 394 ASN A O   
3165  C CB  . ASN A 394 ? 0.5855 0.5814 2.0099 -0.0829 -0.0402 -0.0391 394 ASN A CB  
3166  C CG  . ASN A 394 ? 0.5952 0.6049 2.0460 -0.0818 -0.0480 -0.0414 394 ASN A CG  
3167  O OD1 . ASN A 394 ? 0.5847 0.6055 2.0560 -0.0773 -0.0527 -0.0359 394 ASN A OD1 
3168  N ND2 . ASN A 394 ? 0.6053 0.6141 2.0562 -0.0863 -0.0487 -0.0499 394 ASN A ND2 
3169  N N   . LYS A 395 ? 0.5414 0.5431 2.0029 -0.0767 -0.0047 -0.0377 395 LYS A N   
3170  C CA  . LYS A 395 ? 0.5316 0.5351 2.0080 -0.0760 0.0073  -0.0432 395 LYS A CA  
3171  C C   . LYS A 395 ? 0.4565 0.4697 1.9592 -0.0706 0.0073  -0.0386 395 LYS A C   
3172  O O   . LYS A 395 ? 0.4387 0.4530 1.9430 -0.0682 0.0072  -0.0318 395 LYS A O   
3173  C CB  . LYS A 395 ? 0.6014 0.5970 2.0648 -0.0781 0.0205  -0.0449 395 LYS A CB  
3174  C CG  . LYS A 395 ? 0.7372 0.7208 2.1714 -0.0838 0.0236  -0.0504 395 LYS A CG  
3175  C CD  . LYS A 395 ? 0.8518 0.8277 2.2725 -0.0866 0.0383  -0.0514 395 LYS A CD  
3176  C CE  . LYS A 395 ? 0.9646 0.9264 2.3515 -0.0926 0.0421  -0.0561 395 LYS A CE  
3177  N NZ  . LYS A 395 ? 1.0027 0.9567 2.3744 -0.0959 0.0553  -0.0539 395 LYS A NZ  
3178  N N   . ILE A 396 ? 0.4185 0.4368 1.9398 -0.0689 0.0073  -0.0424 396 ILE A N   
3179  C CA  . ILE A 396 ? 0.3597 0.3855 1.9026 -0.0640 0.0059  -0.0380 396 ILE A CA  
3180  C C   . ILE A 396 ? 0.3284 0.3533 1.8768 -0.0615 0.0144  -0.0360 396 ILE A C   
3181  O O   . ILE A 396 ? 0.3488 0.3696 1.8940 -0.0630 0.0235  -0.0412 396 ILE A O   
3182  C CB  . ILE A 396 ? 0.3537 0.3817 1.9121 -0.0633 0.0057  -0.0423 396 ILE A CB  
3183  C CG1 . ILE A 396 ? 0.3766 0.4071 1.9331 -0.0667 -0.0032 -0.0439 396 ILE A CG1 
3184  C CG2 . ILE A 396 ? 0.3299 0.3627 1.9068 -0.0582 0.0061  -0.0378 396 ILE A CG2 
3185  C CD1 . ILE A 396 ? 0.3718 0.4028 1.9417 -0.0675 -0.0032 -0.0477 396 ILE A CD1 
3186  N N   . ILE A 397 ? 0.2970 0.3261 1.8542 -0.0578 0.0114  -0.0291 397 ILE A N   
3187  C CA  . ILE A 397 ? 0.2645 0.2931 1.8276 -0.0559 0.0178  -0.0267 397 ILE A CA  
3188  C C   . ILE A 397 ? 0.2283 0.2618 1.8112 -0.0507 0.0157  -0.0245 397 ILE A C   
3189  O O   . ILE A 397 ? 0.2275 0.2613 1.8204 -0.0487 0.0204  -0.0245 397 ILE A O   
3190  C CB  . ILE A 397 ? 0.2683 0.2934 1.8177 -0.0570 0.0162  -0.0201 397 ILE A CB  
3191  C CG1 . ILE A 397 ? 0.2681 0.2967 1.8197 -0.0537 0.0054  -0.0136 397 ILE A CG1 
3192  C CG2 . ILE A 397 ? 0.2869 0.3041 1.8124 -0.0624 0.0189  -0.0220 397 ILE A CG2 
3193  C CD1 . ILE A 397 ? 0.2927 0.3165 1.8342 -0.0533 0.0034  -0.0064 397 ILE A CD1 
3194  N N   . LYS A 398 ? 0.2025 0.2397 1.7912 -0.0490 0.0086  -0.0226 398 LYS A N   
3195  C CA  . LYS A 398 ? 0.1836 0.2230 1.7878 -0.0448 0.0078  -0.0217 398 LYS A CA  
3196  C C   . LYS A 398 ? 0.1969 0.2376 1.8053 -0.0457 0.0046  -0.0242 398 LYS A C   
3197  O O   . LYS A 398 ? 0.2185 0.2618 1.8213 -0.0484 0.0000  -0.0242 398 LYS A O   
3198  C CB  . LYS A 398 ? 0.1656 0.2073 1.7737 -0.0412 0.0041  -0.0150 398 LYS A CB  
3199  C CG  . LYS A 398 ? 0.1498 0.1919 1.7705 -0.0369 0.0032  -0.0138 398 LYS A CG  
3200  C CD  . LYS A 398 ? 0.1441 0.1872 1.7672 -0.0332 0.0000  -0.0080 398 LYS A CD  
3201  C CE  . LYS A 398 ? 0.1379 0.1796 1.7701 -0.0291 -0.0009 -0.0070 398 LYS A CE  
3202  N NZ  . LYS A 398 ? 0.1423 0.1852 1.7750 -0.0257 -0.0046 -0.0021 398 LYS A NZ  
3203  N N   . ASN A 399 ? 0.1989 0.2367 1.8167 -0.0437 0.0068  -0.0267 399 ASN A N   
3204  C CA  . ASN A 399 ? 0.2047 0.2421 1.8278 -0.0440 0.0042  -0.0269 399 ASN A CA  
3205  C C   . ASN A 399 ? 0.2036 0.2408 1.8344 -0.0394 0.0030  -0.0222 399 ASN A C   
3206  O O   . ASN A 399 ? 0.2366 0.2720 1.8705 -0.0359 0.0044  -0.0210 399 ASN A O   
3207  C CB  . ASN A 399 ? 0.2271 0.2580 1.8508 -0.0459 0.0071  -0.0332 399 ASN A CB  
3208  C CG  . ASN A 399 ? 0.2563 0.2868 1.8703 -0.0509 0.0076  -0.0381 399 ASN A CG  
3209  O OD1 . ASN A 399 ? 0.2913 0.3253 1.9016 -0.0545 0.0032  -0.0378 399 ASN A OD1 
3210  N ND2 . ASN A 399 ? 0.2639 0.2902 1.8740 -0.0512 0.0128  -0.0432 399 ASN A ND2 
3211  N N   . GLU A 400 ? 0.2037 0.2436 1.8374 -0.0396 0.0004  -0.0196 400 GLU A N   
3212  C CA  . GLU A 400 ? 0.2050 0.2423 1.8433 -0.0357 0.0003  -0.0162 400 GLU A CA  
3213  C C   . GLU A 400 ? 0.2197 0.2582 1.8603 -0.0384 0.0001  -0.0158 400 GLU A C   
3214  O O   . GLU A 400 ? 0.2194 0.2660 1.8616 -0.0416 -0.0017 -0.0160 400 GLU A O   
3215  C CB  . GLU A 400 ? 0.2069 0.2480 1.8461 -0.0319 -0.0016 -0.0114 400 GLU A CB  
3216  C CG  . GLU A 400 ? 0.2246 0.2596 1.8660 -0.0276 -0.0013 -0.0090 400 GLU A CG  
3217  C CD  . GLU A 400 ? 0.2506 0.2869 1.8924 -0.0233 -0.0031 -0.0051 400 GLU A CD  
3218  O OE1 . GLU A 400 ? 0.2856 0.3271 1.9263 -0.0234 -0.0046 -0.0035 400 GLU A OE1 
3219  O OE2 . GLU A 400 ? 0.2499 0.2801 1.8916 -0.0199 -0.0034 -0.0036 400 GLU A OE2 
3220  N N   . SER A 401 ? 0.2120 0.2422 1.8531 -0.0371 0.0018  -0.0150 401 SER A N   
3221  C CA  . SER A 401 ? 0.2059 0.2350 1.8483 -0.0407 0.0035  -0.0148 401 SER A CA  
3222  C C   . SER A 401 ? 0.2189 0.2475 1.8617 -0.0377 0.0049  -0.0106 401 SER A C   
3223  O O   . SER A 401 ? 0.2453 0.2674 1.8848 -0.0328 0.0042  -0.0085 401 SER A O   
3224  C CB  . SER A 401 ? 0.2068 0.2238 1.8460 -0.0428 0.0050  -0.0177 401 SER A CB  
3225  O OG  . SER A 401 ? 0.1952 0.2133 1.8338 -0.0451 0.0043  -0.0225 401 SER A OG  
3226  N N   . ILE A 402 ? 0.2258 0.2620 1.8735 -0.0405 0.0067  -0.0097 402 ILE A N   
3227  C CA  . ILE A 402 ? 0.2363 0.2714 1.8839 -0.0383 0.0099  -0.0067 402 ILE A CA  
3228  C C   . ILE A 402 ? 0.2572 0.2860 1.9034 -0.0437 0.0152  -0.0070 402 ILE A C   
3229  O O   . ILE A 402 ? 0.2809 0.3178 1.9347 -0.0496 0.0164  -0.0093 402 ILE A O   
3230  C CB  . ILE A 402 ? 0.2554 0.3058 1.9120 -0.0368 0.0088  -0.0058 402 ILE A CB  
3231  C CG1 . ILE A 402 ? 0.2786 0.3334 1.9347 -0.0325 0.0034  -0.0050 402 ILE A CG1 
3232  C CG2 . ILE A 402 ? 0.2522 0.3023 1.9096 -0.0343 0.0134  -0.0036 402 ILE A CG2 
3233  C CD1 . ILE A 402 ? 0.2890 0.3359 1.9392 -0.0264 0.0028  -0.0024 402 ILE A CD1 
3234  N N   . ASN A 403 ? 0.2515 0.2653 1.8876 -0.0419 0.0179  -0.0047 403 ASN A N   
3235  C CA  . ASN A 403 ? 0.2453 0.2498 1.8767 -0.0474 0.0240  -0.0041 403 ASN A CA  
3236  C C   . ASN A 403 ? 0.2176 0.2273 1.8510 -0.0479 0.0305  -0.0022 403 ASN A C   
3237  O O   . ASN A 403 ? 0.2063 0.2123 1.8336 -0.0424 0.0310  -0.0001 403 ASN A O   
3238  C CB  . ASN A 403 ? 0.2694 0.2517 1.8856 -0.0457 0.0235  -0.0022 403 ASN A CB  
3239  C CG  . ASN A 403 ? 0.2873 0.2630 1.9025 -0.0445 0.0179  -0.0046 403 ASN A CG  
3240  O OD1 . ASN A 403 ? 0.2809 0.2527 1.8971 -0.0496 0.0186  -0.0070 403 ASN A OD1 
3241  N ND2 . ASN A 403 ? 0.3022 0.2757 1.9159 -0.0376 0.0127  -0.0044 403 ASN A ND2 
3242  N N   . ILE A 404 ? 0.2130 0.2306 1.8551 -0.0548 0.0362  -0.0037 404 ILE A N   
3243  C CA  . ILE A 404 ? 0.2187 0.2416 1.8643 -0.0558 0.0443  -0.0028 404 ILE A CA  
3244  C C   . ILE A 404 ? 0.2328 0.2435 1.8714 -0.0640 0.0529  -0.0020 404 ILE A C   
3245  O O   . ILE A 404 ? 0.2525 0.2550 1.8881 -0.0689 0.0512  -0.0028 404 ILE A O   
3246  C CB  . ILE A 404 ? 0.1972 0.2449 1.8644 -0.0564 0.0438  -0.0056 404 ILE A CB  
3247  C CG1 . ILE A 404 ? 0.1897 0.2470 1.8694 -0.0645 0.0423  -0.0090 404 ILE A CG1 
3248  C CG2 . ILE A 404 ? 0.1813 0.2370 1.8514 -0.0480 0.0355  -0.0052 404 ILE A CG2 
3249  C CD1 . ILE A 404 ? 0.1802 0.2617 1.8825 -0.0658 0.0411  -0.0122 404 ILE A CD1 
3250  N N   . LEU A 405 ? 0.2429 0.2516 1.8783 -0.0653 0.0626  -0.0006 405 LEU A N   
3251  C CA  . LEU A 405 ? 0.2686 0.2702 1.9013 -0.0748 0.0733  -0.0003 405 LEU A CA  
3252  C C   . LEU A 405 ? 0.2807 0.3054 1.9357 -0.0787 0.0814  -0.0035 405 LEU A C   
3253  O O   . LEU A 405 ? 0.3065 0.3362 1.9624 -0.0744 0.0869  -0.0033 405 LEU A O   
3254  C CB  . LEU A 405 ? 0.2819 0.2584 1.8883 -0.0730 0.0786  0.0041  405 LEU A CB  
3255  C CG  . LEU A 405 ? 0.3026 0.2655 1.8992 -0.0830 0.0911  0.0057  405 LEU A CG  
3256  C CD1 . LEU A 405 ? 0.3134 0.2649 1.9071 -0.0900 0.0882  0.0059  405 LEU A CD1 
3257  C CD2 . LEU A 405 ? 0.3263 0.2641 1.8943 -0.0803 0.0958  0.0102  405 LEU A CD2 
3258  N N   . ALA A 406 ? 0.2806 0.3199 1.9548 -0.0866 0.0816  -0.0070 406 ALA A N   
3259  C CA  . ALA A 406 ? 0.2583 0.3245 1.9601 -0.0890 0.0852  -0.0112 406 ALA A CA  
3260  C C   . ALA A 406 ? 0.2831 0.3520 1.9945 -0.1012 0.0973  -0.0130 406 ALA A C   
3261  O O   . ALA A 406 ? 0.3032 0.3549 2.0026 -0.1090 0.0996  -0.0116 406 ALA A O   
3262  C CB  . ALA A 406 ? 0.2381 0.3228 1.9580 -0.0876 0.0729  -0.0147 406 ALA A CB  
3263  N N   . SER A 407 ? 0.2886 0.3809 2.0250 -0.1029 0.1038  -0.0168 407 SER A N   
3264  C CA  . SER A 407 ? 0.2824 0.3816 2.0327 -0.1144 0.1178  -0.0192 407 SER A CA  
3265  C C   . SER A 407 ? 0.2743 0.4057 2.0587 -0.1124 0.1196  -0.0247 407 SER A C   
3266  O O   . SER A 407 ? 0.2588 0.4006 2.0485 -0.1012 0.1130  -0.0252 407 SER A O   
3267  C CB  . SER A 407 ? 0.3023 0.3796 2.0291 -0.1171 0.1326  -0.0153 407 SER A CB  
3268  O OG  . SER A 407 ? 0.3294 0.4076 2.0646 -0.1305 0.1471  -0.0168 407 SER A OG  
3269  N N   . LYS A 408 ? 0.2870 0.4341 2.0957 -0.1232 0.1282  -0.0291 408 LYS A N   
3270  C CA  . LYS A 408 ? 0.2846 0.4644 2.1304 -0.1219 0.1297  -0.0352 408 LYS A CA  
3271  C C   . LYS A 408 ? 0.3033 0.4862 2.1526 -0.1216 0.1483  -0.0361 408 LYS A C   
3272  O O   . LYS A 408 ? 0.2998 0.5074 2.1762 -0.1159 0.1497  -0.0408 408 LYS A O   
3273  C CB  . LYS A 408 ? 0.2829 0.4822 2.1588 -0.1338 0.1285  -0.0408 408 LYS A CB  
3274  C CG  . LYS A 408 ? 0.2780 0.4789 2.1557 -0.1346 0.1100  -0.0420 408 LYS A CG  
3275  C CD  . LYS A 408 ? 0.2919 0.5083 2.1967 -0.1485 0.1113  -0.0477 408 LYS A CD  
3276  C CE  . LYS A 408 ? 0.2946 0.5087 2.1976 -0.1516 0.0948  -0.0494 408 LYS A CE  
3277  N NZ  . LYS A 408 ? 0.2968 0.5330 2.2331 -0.1628 0.0925  -0.0566 408 LYS A NZ  
3278  N N   . THR A 409 ? 0.3307 0.4882 2.1527 -0.1278 0.1625  -0.0319 409 THR A N   
3279  C CA  . THR A 409 ? 0.3573 0.5133 2.1769 -0.1292 0.1824  -0.0326 409 THR A CA  
3280  C C   . THR A 409 ? 0.3809 0.5072 2.1596 -0.1206 0.1828  -0.0264 409 THR A C   
3281  O O   . THR A 409 ? 0.4117 0.5212 2.1690 -0.1153 0.1685  -0.0220 409 THR A O   
3282  C CB  . THR A 409 ? 0.3862 0.5389 2.2106 -0.1460 0.2006  -0.0336 409 THR A CB  
3283  O OG1 . THR A 409 ? 0.4125 0.5341 2.1995 -0.1488 0.2150  -0.0282 409 THR A OG1 
3284  C CG2 . THR A 409 ? 0.3913 0.5361 2.2150 -0.1579 0.1945  -0.0326 409 THR A CG2 
3285  N N   . ALA A 410 ? 0.4009 0.5208 2.1692 -0.1194 0.1990  -0.0266 410 ALA A N   
3286  C CA  . ALA A 410 ? 0.4306 0.5193 2.1573 -0.1131 0.2005  -0.0209 410 ALA A CA  
3287  C C   . ALA A 410 ? 0.4721 0.5278 2.1649 -0.1225 0.2036  -0.0145 410 ALA A C   
3288  O O   . ALA A 410 ? 0.5217 0.5783 2.2232 -0.1355 0.2107  -0.0150 410 ALA A O   
3289  C CB  . ALA A 410 ? 0.4445 0.5348 2.1687 -0.1105 0.2181  -0.0236 410 ALA A CB  
3290  N N   . PHE A 411 ? 0.4709 0.4965 2.1253 -0.1161 0.1982  -0.0087 411 PHE A N   
3291  C CA  . PHE A 411 ? 0.4851 0.4758 2.1038 -0.1238 0.2023  -0.0024 411 PHE A CA  
3292  C C   . PHE A 411 ? 0.5071 0.4682 2.0855 -0.1156 0.2013  0.0023  411 PHE A C   
3293  O O   . PHE A 411 ? 0.5146 0.4807 2.0923 -0.1034 0.1923  0.0012  411 PHE A O   
3294  C CB  . PHE A 411 ? 0.4684 0.4523 2.0866 -0.1264 0.1870  0.0000  411 PHE A CB  
3295  C CG  . PHE A 411 ? 0.4318 0.4209 2.0524 -0.1137 0.1663  0.0001  411 PHE A CG  
3296  C CD1 . PHE A 411 ? 0.4039 0.4243 2.0581 -0.1094 0.1572  -0.0049 411 PHE A CD1 
3297  C CD2 . PHE A 411 ? 0.4395 0.4020 2.0288 -0.1065 0.1561  0.0052  411 PHE A CD2 
3298  C CE1 . PHE A 411 ? 0.3945 0.4180 2.0489 -0.0989 0.1398  -0.0044 411 PHE A CE1 
3299  C CE2 . PHE A 411 ? 0.4274 0.3956 2.0207 -0.0960 0.1387  0.0049  411 PHE A CE2 
3300  C CZ  . PHE A 411 ? 0.4004 0.3986 2.0253 -0.0925 0.1314  0.0003  411 PHE A CZ  
3301  N N   . GLU A 412 ? 0.5490 0.4779 2.0930 -0.1230 0.2105  0.0076  412 GLU A N   
3302  C CA  . GLU A 412 ? 0.5896 0.4862 2.0914 -0.1166 0.2088  0.0125  412 GLU A CA  
3303  C C   . GLU A 412 ? 0.5825 0.4642 2.0701 -0.1082 0.1866  0.0163  412 GLU A C   
3304  O O   . GLU A 412 ? 0.5877 0.4709 2.0851 -0.1115 0.1772  0.0174  412 GLU A O   
3305  C CB  . GLU A 412 ? 0.6639 0.5256 2.1283 -0.1269 0.2226  0.0180  412 GLU A CB  
3306  C CG  . GLU A 412 ? 0.7277 0.5949 2.1944 -0.1355 0.2479  0.0151  412 GLU A CG  
3307  C CD  . GLU A 412 ? 0.8282 0.6544 2.2474 -0.1431 0.2605  0.0215  412 GLU A CD  
3308  O OE1 . GLU A 412 ? 0.8907 0.6915 2.2896 -0.1502 0.2564  0.0277  412 GLU A OE1 
3309  O OE2 . GLU A 412 ? 0.8919 0.7108 2.2935 -0.1419 0.2746  0.0201  412 GLU A OE2 
3310  N N   . LEU A 413 ? 0.5767 0.4445 2.0422 -0.0973 0.1786  0.0178  413 LEU A N   
3311  C CA  . LEU A 413 ? 0.5624 0.4089 2.0069 -0.0902 0.1601  0.0221  413 LEU A CA  
3312  C C   . LEU A 413 ? 0.5942 0.4029 1.9932 -0.0897 0.1636  0.0272  413 LEU A C   
3313  O O   . LEU A 413 ? 0.6097 0.4128 1.9951 -0.0923 0.1791  0.0264  413 LEU A O   
3314  C CB  . LEU A 413 ? 0.5316 0.3962 1.9927 -0.0776 0.1451  0.0190  413 LEU A CB  
3315  C CG  . LEU A 413 ? 0.4975 0.3972 2.0002 -0.0773 0.1400  0.0144  413 LEU A CG  
3316  C CD1 . LEU A 413 ? 0.4649 0.3811 1.9815 -0.0656 0.1284  0.0116  413 LEU A CD1 
3317  C CD2 . LEU A 413 ? 0.4937 0.3903 2.0020 -0.0819 0.1308  0.0162  413 LEU A CD2 
3318  N N   . PRO A 414 ? 0.5965 0.3776 1.9700 -0.0863 0.1493  0.0323  414 PRO A N   
3319  C CA  . PRO A 414 ? 0.6357 0.3815 1.9655 -0.0829 0.1478  0.0367  414 PRO A CA  
3320  C C   . PRO A 414 ? 0.6308 0.3860 1.9624 -0.0712 0.1407  0.0331  414 PRO A C   
3321  O O   . PRO A 414 ? 0.5694 0.3519 1.9319 -0.0648 0.1319  0.0289  414 PRO A O   
3322  C CB  . PRO A 414 ? 0.6417 0.3617 1.9535 -0.0814 0.1318  0.0421  414 PRO A CB  
3323  C CG  . PRO A 414 ? 0.6006 0.3483 1.9506 -0.0786 0.1202  0.0387  414 PRO A CG  
3324  C CD  . PRO A 414 ? 0.5765 0.3588 1.9619 -0.0850 0.1339  0.0335  414 PRO A CD  
3325  N N   . GLU A 415 ? 0.6871 0.4184 1.9842 -0.0690 0.1456  0.0344  415 GLU A N   
3326  C CA  . GLU A 415 ? 0.7159 0.4520 2.0109 -0.0585 0.1391  0.0308  415 GLU A CA  
3327  C C   . GLU A 415 ? 0.7334 0.4309 1.9828 -0.0539 0.1297  0.0350  415 GLU A C   
3328  O O   . GLU A 415 ? 0.7778 0.4450 1.9933 -0.0602 0.1356  0.0401  415 GLU A O   
3329  C CB  . GLU A 415 ? 0.7848 0.5382 2.0901 -0.0598 0.1578  0.0254  415 GLU A CB  
3330  C CG  . GLU A 415 ? 0.8880 0.6162 2.1584 -0.0678 0.1773  0.0274  415 GLU A CG  
3331  C CD  . GLU A 415 ? 0.9504 0.6996 2.2367 -0.0689 0.1971  0.0209  415 GLU A CD  
3332  O OE1 . GLU A 415 ? 0.9344 0.6997 2.2403 -0.0785 0.2148  0.0192  415 GLU A OE1 
3333  O OE2 . GLU A 415 ? 1.0497 0.7998 2.3307 -0.0596 0.1937  0.0169  415 GLU A OE2 
3334  N N   . LEU A 416 ? 0.6959 0.3952 1.9458 -0.0432 0.1144  0.0326  416 LEU A N   
3335  C CA  . LEU A 416 ? 0.6895 0.3557 1.9010 -0.0372 0.1013  0.0353  416 LEU A CA  
3336  C C   . LEU A 416 ? 0.6665 0.3354 1.8710 -0.0312 0.1048  0.0302  416 LEU A C   
3337  O O   . LEU A 416 ? 0.6438 0.3421 1.8811 -0.0266 0.1035  0.0251  416 LEU A O   
3338  C CB  . LEU A 416 ? 0.6681 0.3351 1.8910 -0.0300 0.0774  0.0365  416 LEU A CB  
3339  C CG  . LEU A 416 ? 0.7077 0.3396 1.8934 -0.0241 0.0605  0.0398  416 LEU A CG  
3340  C CD1 . LEU A 416 ? 0.6911 0.3240 1.8915 -0.0189 0.0394  0.0413  416 LEU A CD1 
3341  C CD2 . LEU A 416 ? 0.7248 0.3528 1.8983 -0.0166 0.0553  0.0357  416 LEU A CD2 
3342  N N   . THR A 417 ? 0.6847 0.3218 1.8454 -0.0318 0.1101  0.0316  417 THR A N   
3343  C CA  . THR A 417 ? 0.6766 0.3106 1.8247 -0.0255 0.1119  0.0265  417 THR A CA  
3344  C C   . THR A 417 ? 0.7083 0.3017 1.8082 -0.0215 0.0982  0.0296  417 THR A C   
3345  O O   . THR A 417 ? 0.7333 0.2983 1.8034 -0.0258 0.0955  0.0360  417 THR A O   
3346  C CB  . THR A 417 ? 0.6783 0.3196 1.8246 -0.0308 0.1381  0.0225  417 THR A CB  
3347  O OG1 . THR A 417 ? 0.7239 0.3299 1.8243 -0.0379 0.1491  0.0271  417 THR A OG1 
3348  C CG2 . THR A 417 ? 0.6365 0.3158 1.8289 -0.0359 0.1519  0.0198  417 THR A CG2 
3349  N N   . ILE A 418 ? 0.7001 0.2897 1.7919 -0.0133 0.0891  0.0249  418 ILE A N   
3350  C CA  . ILE A 418 ? 0.7274 0.2805 1.7764 -0.0085 0.0728  0.0268  418 ILE A CA  
3351  C C   . ILE A 418 ? 0.7514 0.2883 1.7693 -0.0066 0.0830  0.0220  418 ILE A C   
3352  O O   . ILE A 418 ? 0.7365 0.2968 1.7771 -0.0047 0.0939  0.0155  418 ILE A O   
3353  C CB  . ILE A 418 ? 0.7016 0.2631 1.7712 0.0000  0.0462  0.0258  418 ILE A CB  
3354  C CG1 . ILE A 418 ? 0.6633 0.2571 1.7704 0.0055  0.0451  0.0187  418 ILE A CG1 
3355  C CG2 . ILE A 418 ? 0.6804 0.2501 1.7718 -0.0018 0.0361  0.0308  418 ILE A CG2 
3356  C CD1 . ILE A 418 ? 0.6432 0.2415 1.7653 0.0133  0.0203  0.0169  418 ILE A CD1 
3357  N N   . GLU A 419 ? 0.7966 0.2920 1.7610 -0.0073 0.0795  0.0250  419 GLU A N   
3358  C CA  . GLU A 419 ? 0.8322 0.3063 1.7605 -0.0045 0.0849  0.0202  419 GLU A CA  
3359  C C   . GLU A 419 ? 0.8568 0.3045 1.7583 0.0032  0.0574  0.0203  419 GLU A C   
3360  O O   . GLU A 419 ? 0.8897 0.3082 1.7613 0.0026  0.0437  0.0268  419 GLU A O   
3361  C CB  . GLU A 419 ? 0.8836 0.3264 1.7636 -0.0124 0.1059  0.0228  419 GLU A CB  
3362  C CG  . GLU A 419 ? 0.8713 0.3370 1.7747 -0.0215 0.1343  0.0228  419 GLU A CG  
3363  C CD  . GLU A 419 ? 0.9281 0.3593 1.7823 -0.0311 0.1533  0.0275  419 GLU A CD  
3364  O OE1 . GLU A 419 ? 0.9678 0.3768 1.7840 -0.0312 0.1652  0.0238  419 GLU A OE1 
3365  O OE2 . GLU A 419 ? 0.9372 0.3612 1.7890 -0.0384 0.1552  0.0350  419 GLU A OE2 
3366  N N   . VAL A 420 ? 0.8460 0.3033 1.7582 0.0104  0.0496  0.0130  420 VAL A N   
3367  C CA  . VAL A 420 ? 0.8579 0.3002 1.7591 0.0180  0.0220  0.0115  420 VAL A CA  
3368  C C   . VAL A 420 ? 0.9156 0.3248 1.7677 0.0206  0.0217  0.0070  420 VAL A C   
3369  O O   . VAL A 420 ? 0.9286 0.3415 1.7751 0.0198  0.0412  0.0012  420 VAL A O   
3370  C CB  . VAL A 420 ? 0.8007 0.2821 1.7574 0.0232  0.0125  0.0067  420 VAL A CB  
3371  C CG1 . VAL A 420 ? 0.8015 0.2737 1.7569 0.0304  -0.0163 0.0046  420 VAL A CG1 
3372  C CG2 . VAL A 420 ? 0.7550 0.2687 1.7572 0.0197  0.0167  0.0106  420 VAL A CG2 
3373  N N   . THR A 421 ? 0.9578 0.3340 1.7741 0.0240  -0.0011 0.0093  421 THR A N   
3374  C CA  . THR A 421 ? 1.0147 0.3570 1.7829 0.0273  -0.0070 0.0047  421 THR A CA  
3375  C C   . THR A 421 ? 1.0144 0.3611 1.7992 0.0352  -0.0359 0.0002  421 THR A C   
3376  O O   . THR A 421 ? 1.0098 0.3647 1.8173 0.0375  -0.0559 0.0040  421 THR A O   
3377  C CB  . THR A 421 ? 1.0727 0.3677 1.7791 0.0241  -0.0107 0.0115  421 THR A CB  
3378  O OG1 . THR A 421 ? 1.0813 0.3761 1.7768 0.0157  0.0200  0.0142  421 THR A OG1 
3379  C CG2 . THR A 421 ? 1.1258 0.3819 1.7786 0.0280  -0.0221 0.0071  421 THR A CG2 
3380  N N   . PRO A 422 ? 1.0368 0.3792 1.8130 0.0394  -0.0385 -0.0084 422 PRO A N   
3381  C CA  . PRO A 422 ? 1.0566 0.3990 1.8197 0.0377  -0.0126 -0.0144 422 PRO A CA  
3382  C C   . PRO A 422 ? 1.0096 0.3979 1.8298 0.0358  0.0060  -0.0153 422 PRO A C   
3383  O O   . PRO A 422 ? 0.9588 0.3764 1.8257 0.0372  -0.0048 -0.0132 422 PRO A O   
3384  C CB  . PRO A 422 ? 1.0689 0.3999 1.8194 0.0439  -0.0256 -0.0236 422 PRO A CB  
3385  C CG  . PRO A 422 ? 1.0813 0.3939 1.8205 0.0475  -0.0590 -0.0212 422 PRO A CG  
3386  C CD  . PRO A 422 ? 1.0400 0.3764 1.8188 0.0460  -0.0665 -0.0132 422 PRO A CD  
3387  N N   . GLU A 423 ? 1.0334 0.4262 1.8478 0.0327  0.0341  -0.0187 423 GLU A N   
3388  C CA  . GLU A 423 ? 1.0071 0.4412 1.8721 0.0310  0.0529  -0.0201 423 GLU A CA  
3389  C C   . GLU A 423 ? 0.9844 0.4432 1.8858 0.0377  0.0474  -0.0281 423 GLU A C   
3390  O O   . GLU A 423 ? 0.9529 0.4465 1.9046 0.0387  0.0442  -0.0271 423 GLU A O   
3391  C CB  . GLU A 423 ? 1.0485 0.4790 1.8959 0.0257  0.0847  -0.0219 423 GLU A CB  
3392  C CG  . GLU A 423 ? 1.0153 0.4894 1.9167 0.0239  0.1037  -0.0236 423 GLU A CG  
3393  C CD  . GLU A 423 ? 1.0493 0.5225 1.9383 0.0173  0.1352  -0.0246 423 GLU A CD  
3394  O OE1 . GLU A 423 ? 1.1130 0.5527 1.9512 0.0155  0.1454  -0.0266 423 GLU A OE1 
3395  O OE2 . GLU A 423 ? 1.0212 0.5265 1.9505 0.0134  0.1493  -0.0232 423 GLU A OE2 
3396  N N   . LYS A 424 ? 1.0121 0.4509 1.8857 0.0421  0.0467  -0.0359 424 LYS A N   
3397  C CA  . LYS A 424 ? 0.9760 0.4347 1.8784 0.0478  0.0489  -0.0444 424 LYS A CA  
3398  C C   . LYS A 424 ? 0.9586 0.4065 1.8584 0.0534  0.0218  -0.0482 424 LYS A C   
3399  O O   . LYS A 424 ? 0.9128 0.3864 1.8546 0.0568  0.0138  -0.0508 424 LYS A O   
3400  C CB  . LYS A 424 ? 1.0204 0.4681 1.8987 0.0487  0.0732  -0.0523 424 LYS A CB  
3401  C CG  . LYS A 424 ? 1.0444 0.5064 1.9303 0.0432  0.1035  -0.0507 424 LYS A CG  
3402  C CD  . LYS A 424 ? 1.0851 0.5493 1.9670 0.0457  0.1283  -0.0605 424 LYS A CD  
3403  C CE  . LYS A 424 ? 1.1263 0.5832 1.9858 0.0392  0.1588  -0.0606 424 LYS A CE  
3404  N NZ  . LYS A 424 ? 1.0972 0.5871 1.9966 0.0336  0.1755  -0.0562 424 LYS A NZ  
3405  N N   . ASP A 425 ? 0.9906 0.3998 1.8408 0.0539  0.0078  -0.0487 425 ASP A N   
3406  C CA  . ASP A 425 ? 0.9890 0.3838 1.8306 0.0589  -0.0159 -0.0544 425 ASP A CA  
3407  C C   . ASP A 425 ? 1.0088 0.3782 1.8238 0.0583  -0.0423 -0.0494 425 ASP A C   
3408  O O   . ASP A 425 ? 1.0592 0.3922 1.8208 0.0568  -0.0430 -0.0480 425 ASP A O   
3409  C CB  . ASP A 425 ? 1.0178 0.3900 1.8252 0.0619  -0.0057 -0.0642 425 ASP A CB  
3410  C CG  . ASP A 425 ? 1.0342 0.3873 1.8273 0.0665  -0.0292 -0.0713 425 ASP A CG  
3411  O OD1 . ASP A 425 ? 1.0100 0.3752 1.8315 0.0675  -0.0526 -0.0692 425 ASP A OD1 
3412  O OD2 . ASP A 425 ? 1.0647 0.3901 1.8178 0.0686  -0.0241 -0.0791 425 ASP A OD2 
3413  N N   . LEU A 426 ? 0.9676 0.3552 1.8195 0.0600  -0.0648 -0.0474 426 LEU A N   
3414  C CA  . LEU A 426 ? 0.9757 0.3468 1.8154 0.0605  -0.0919 -0.0430 426 LEU A CA  
3415  C C   . LEU A 426 ? 1.0284 0.3585 1.8171 0.0632  -0.1098 -0.0480 426 LEU A C   
3416  O O   . LEU A 426 ? 1.0434 0.3540 1.8136 0.0640  -0.1324 -0.0445 426 LEU A O   
3417  C CB  . LEU A 426 ? 0.9251 0.3280 1.8203 0.0621  -0.1096 -0.0426 426 LEU A CB  
3418  C CG  . LEU A 426 ? 0.8897 0.3187 1.8211 0.0595  -0.1079 -0.0343 426 LEU A CG  
3419  C CD1 . LEU A 426 ? 0.8795 0.3247 1.8191 0.0557  -0.0783 -0.0312 426 LEU A CD1 
3420  C CD2 . LEU A 426 ? 0.8340 0.2964 1.8214 0.0607  -0.1211 -0.0351 426 LEU A CD2 
3421  N N   . ASN A 427 ? 1.0505 0.3674 1.8178 0.0650  -0.1015 -0.0567 427 ASN A N   
3422  C CA  . ASN A 427 ? 1.1024 0.3781 1.8171 0.0672  -0.1172 -0.0622 427 ASN A CA  
3423  C C   . ASN A 427 ? 1.1639 0.4016 1.8161 0.0645  -0.1078 -0.0579 427 ASN A C   
3424  O O   . ASN A 427 ? 1.2160 0.4147 1.8174 0.0659  -0.1227 -0.0605 427 ASN A O   
3425  C CB  . ASN A 427 ? 1.1042 0.3760 1.8149 0.0702  -0.1121 -0.0735 427 ASN A CB  
3426  C CG  . ASN A 427 ? 1.0669 0.3549 1.8158 0.0730  -0.1346 -0.0789 427 ASN A CG  
3427  O OD1 . ASN A 427 ? 1.0453 0.3390 1.8130 0.0730  -0.1589 -0.0755 427 ASN A OD1 
3428  N ND2 . ASN A 427 ? 1.0533 0.3477 1.8137 0.0752  -0.1268 -0.0876 427 ASN A ND2 
3429  N N   . GLU A 428 ? 1.1611 0.4086 1.8158 0.0602  -0.0837 -0.0511 428 GLU A N   
3430  C CA  . GLU A 428 ? 1.2202 0.4324 1.8159 0.0564  -0.0691 -0.0473 428 GLU A CA  
3431  C C   . GLU A 428 ? 1.2484 0.4339 1.8144 0.0553  -0.0904 -0.0383 428 GLU A C   
3432  O O   . GLU A 428 ? 1.3072 0.4546 1.8149 0.0524  -0.0844 -0.0347 428 GLU A O   
3433  C CB  . GLU A 428 ? 1.2075 0.4397 1.8172 0.0513  -0.0341 -0.0442 428 GLU A CB  
3434  C CG  . GLU A 428 ? 1.2056 0.4467 1.8187 0.0526  -0.0096 -0.0540 428 GLU A CG  
3435  C CD  . GLU A 428 ? 1.2153 0.4586 1.8168 0.0469  0.0255  -0.0522 428 GLU A CD  
3436  O OE1 . GLU A 428 ? 1.2083 0.4477 1.8016 0.0412  0.0308  -0.0425 428 GLU A OE1 
3437  O OE2 . GLU A 428 ? 1.2067 0.4557 1.8089 0.0484  0.0468  -0.0609 428 GLU A OE2 
3438  N N   . GLY A 429 ? 1.2129 0.4168 1.8172 0.0578  -0.1148 -0.0346 429 GLY A N   
3439  C CA  . GLY A 429 ? 1.2464 0.4246 1.8244 0.0582  -0.1369 -0.0268 429 GLY A CA  
3440  C C   . GLY A 429 ? 1.2102 0.4114 1.8360 0.0623  -0.1659 -0.0258 429 GLY A C   
3441  O O   . GLY A 429 ? 1.1456 0.3870 1.8294 0.0633  -0.1642 -0.0291 429 GLY A O   
3442  N N   . LYS A 430 ? 1.2496 0.4238 1.8494 0.0647  -0.1916 -0.0210 430 LYS A N   
3443  C CA  . LYS A 430 ? 1.2263 0.4184 1.8677 0.0691  -0.2206 -0.0205 430 LYS A CA  
3444  C C   . LYS A 430 ? 1.1851 0.4007 1.8616 0.0672  -0.2142 -0.0115 430 LYS A C   
3445  O O   . LYS A 430 ? 1.1422 0.3886 1.8718 0.0696  -0.2274 -0.0117 430 LYS A O   
3446  C CB  . LYS A 430 ? 1.2911 0.4434 1.8901 0.0737  -0.2536 -0.0207 430 LYS A CB  
3447  C CG  . LYS A 430 ? 1.3648 0.4759 1.9009 0.0740  -0.2553 -0.0267 430 LYS A CG  
3448  C CD  . LYS A 430 ? 1.4146 0.4999 1.9298 0.0795  -0.2931 -0.0314 430 LYS A CD  
3449  C CE  . LYS A 430 ? 1.5073 0.5349 1.9396 0.0798  -0.3009 -0.0301 430 LYS A CE  
3450  N NZ  . LYS A 430 ? 1.5425 0.5493 1.9309 0.0769  -0.2797 -0.0365 430 LYS A NZ  
3451  N N   . ILE A 431 ? 1.1992 0.3995 1.8455 0.0623  -0.1930 -0.0041 431 ILE A N   
3452  C CA  . ILE A 431 ? 1.1719 0.3857 1.8412 0.0602  -0.1886 0.0049  431 ILE A CA  
3453  C C   . ILE A 431 ? 1.1347 0.3742 1.8247 0.0536  -0.1535 0.0068  431 ILE A C   
3454  O O   . ILE A 431 ? 1.1595 0.3831 1.8144 0.0493  -0.1310 0.0059  431 ILE A O   
3455  C CB  . ILE A 431 ? 1.2309 0.3992 1.8449 0.0603  -0.2000 0.0134  431 ILE A CB  
3456  C CG1 . ILE A 431 ? 1.2644 0.4093 1.8625 0.0678  -0.2382 0.0113  431 ILE A CG1 
3457  C CG2 . ILE A 431 ? 1.2085 0.3882 1.8431 0.0572  -0.1920 0.0227  431 ILE A CG2 
3458  C CD1 . ILE A 431 ? 1.3393 0.4316 1.8720 0.0687  -0.2517 0.0189  431 ILE A CD1 
3459  N N   . ALA A 432 ? 1.0792 0.3568 1.8250 0.0528  -0.1499 0.0093  432 ALA A N   
3460  C CA  . ALA A 432 ? 1.0469 0.3551 1.8231 0.0470  -0.1205 0.0107  432 ALA A CA  
3461  C C   . ALA A 432 ? 1.0647 0.3667 1.8350 0.0423  -0.1119 0.0203  432 ALA A C   
3462  O O   . ALA A 432 ? 1.0874 0.3739 1.8507 0.0450  -0.1322 0.0255  432 ALA A O   
3463  C CB  . ALA A 432 ? 0.9824 0.3373 1.8249 0.0493  -0.1233 0.0062  432 ALA A CB  
3464  N N   . SER A 433 ? 1.0493 0.3656 1.8271 0.0353  -0.0824 0.0222  433 SER A N   
3465  C CA  . SER A 433 ? 1.0432 0.3618 1.8276 0.0300  -0.0731 0.0305  433 SER A CA  
3466  C C   . SER A 433 ? 0.9821 0.3448 1.8180 0.0254  -0.0510 0.0291  433 SER A C   
3467  O O   . SER A 433 ? 0.9743 0.3566 1.8247 0.0245  -0.0347 0.0231  433 SER A O   
3468  C CB  . SER A 433 ? 1.1087 0.3865 1.8340 0.0239  -0.0600 0.0368  433 SER A CB  
3469  O OG  . SER A 433 ? 1.1168 0.4034 1.8377 0.0170  -0.0282 0.0345  433 SER A OG  
3470  N N   . ILE A 434 ? 0.9473 0.3244 1.8102 0.0230  -0.0513 0.0345  434 ILE A N   
3471  C CA  . ILE A 434 ? 0.8966 0.3104 1.8019 0.0176  -0.0305 0.0344  434 ILE A CA  
3472  C C   . ILE A 434 ? 0.9288 0.3247 1.8119 0.0094  -0.0164 0.0423  434 ILE A C   
3473  O O   . ILE A 434 ? 0.9376 0.3198 1.8161 0.0100  -0.0299 0.0482  434 ILE A O   
3474  C CB  . ILE A 434 ? 0.8326 0.2833 1.7953 0.0216  -0.0436 0.0324  434 ILE A CB  
3475  C CG1 . ILE A 434 ? 0.8093 0.2774 1.7944 0.0284  -0.0557 0.0247  434 ILE A CG1 
3476  C CG2 . ILE A 434 ? 0.7895 0.2742 1.7919 0.0156  -0.0239 0.0331  434 ILE A CG2 
3477  C CD1 . ILE A 434 ? 0.7581 0.2600 1.7966 0.0320  -0.0687 0.0226  434 ILE A CD1 
3478  N N   . LYS A 435 ? 0.9471 0.3422 1.8163 0.0018  0.0108  0.0421  435 LYS A N   
3479  C CA  . LYS A 435 ? 0.9564 0.3409 1.8123 -0.0077 0.0284  0.0488  435 LYS A CA  
3480  C C   . LYS A 435 ? 0.9098 0.3381 1.8217 -0.0118 0.0413  0.0473  435 LYS A C   
3481  O O   . LYS A 435 ? 0.8980 0.3516 1.8312 -0.0144 0.0602  0.0421  435 LYS A O   
3482  C CB  . LYS A 435 ? 0.9961 0.3559 1.8068 -0.0144 0.0517  0.0488  435 LYS A CB  
3483  C CG  . LYS A 435 ? 1.0577 0.3677 1.8054 -0.0115 0.0385  0.0518  435 LYS A CG  
3484  C CD  . LYS A 435 ? 1.1143 0.3901 1.8078 -0.0203 0.0616  0.0550  435 LYS A CD  
3485  C CE  . LYS A 435 ? 1.1187 0.4022 1.8058 -0.0207 0.0812  0.0467  435 LYS A CE  
3486  N NZ  . LYS A 435 ? 1.1835 0.4271 1.8105 -0.0288 0.1006  0.0502  435 LYS A NZ  
3487  N N   . THR A 436 ? 0.9009 0.3377 1.8367 -0.0119 0.0302  0.0514  436 THR A N   
3488  C CA  . THR A 436 ? 0.8668 0.3409 1.8509 -0.0166 0.0416  0.0506  436 THR A CA  
3489  C C   . THR A 436 ? 0.8981 0.3612 1.8661 -0.0284 0.0646  0.0555  436 THR A C   
3490  O O   . THR A 436 ? 0.9489 0.3726 1.8709 -0.0322 0.0650  0.0618  436 THR A O   
3491  C CB  . THR A 436 ? 0.8411 0.3273 1.8556 -0.0116 0.0205  0.0521  436 THR A CB  
3492  O OG1 . THR A 436 ? 0.8206 0.3180 1.8500 -0.0020 0.0025  0.0467  436 THR A OG1 
3493  C CG2 . THR A 436 ? 0.7920 0.3150 1.8545 -0.0162 0.0302  0.0509  436 THR A CG2 
3494  N N   . LYS A 437 ? 0.8750 0.3728 1.8810 -0.0344 0.0834  0.0523  437 LYS A N   
3495  C CA  . LYS A 437 ? 0.8983 0.3942 1.9004 -0.0466 0.1066  0.0555  437 LYS A CA  
3496  C C   . LYS A 437 ? 0.8476 0.3844 1.9044 -0.0500 0.1115  0.0532  437 LYS A C   
3497  O O   . LYS A 437 ? 0.8089 0.3812 1.9036 -0.0462 0.1133  0.0467  437 LYS A O   
3498  C CB  . LYS A 437 ? 0.9254 0.4211 1.9122 -0.0520 0.1319  0.0519  437 LYS A CB  
3499  C CG  . LYS A 437 ? 0.9439 0.4485 1.9400 -0.0651 0.1579  0.0533  437 LYS A CG  
3500  C CD  . LYS A 437 ? 0.9539 0.4803 1.9633 -0.0683 0.1824  0.0462  437 LYS A CD  
3501  C CE  . LYS A 437 ? 0.9533 0.4974 1.9846 -0.0809 0.2064  0.0461  437 LYS A CE  
3502  N NZ  . LYS A 437 ? 0.9487 0.5172 1.9982 -0.0827 0.2290  0.0382  437 LYS A NZ  
3503  N N   . ILE A 438 ? 0.8556 0.3851 1.9142 -0.0573 0.1131  0.0585  438 ILE A N   
3504  C CA  . ILE A 438 ? 0.8241 0.3881 1.9309 -0.0604 0.1144  0.0565  438 ILE A CA  
3505  C C   . ILE A 438 ? 0.8561 0.4203 1.9629 -0.0743 0.1380  0.0586  438 ILE A C   
3506  O O   . ILE A 438 ? 0.9150 0.4477 1.9919 -0.0812 0.1404  0.0654  438 ILE A O   
3507  C CB  . ILE A 438 ? 0.8125 0.3712 1.9287 -0.0556 0.0922  0.0597  438 ILE A CB  
3508  C CG1 . ILE A 438 ? 0.8033 0.3521 1.9105 -0.0428 0.0680  0.0589  438 ILE A CG1 
3509  C CG2 . ILE A 438 ? 0.7691 0.3665 1.9366 -0.0574 0.0928  0.0560  438 ILE A CG2 
3510  C CD1 . ILE A 438 ? 0.7652 0.3236 1.8983 -0.0365 0.0475  0.0588  438 ILE A CD1 
3511  N N   . GLU A 439 ? 0.8346 0.4340 1.9762 -0.0785 0.1546  0.0528  439 GLU A N   
3512  C CA  . GLU A 439 ? 0.8602 0.4687 2.0150 -0.0918 0.1747  0.0534  439 GLU A CA  
3513  C C   . GLU A 439 ? 0.8081 0.4342 1.9968 -0.0935 0.1641  0.0539  439 GLU A C   
3514  O O   . GLU A 439 ? 0.7608 0.4198 1.9882 -0.0872 0.1549  0.0489  439 GLU A O   
3515  C CB  . GLU A 439 ? 0.8817 0.5221 2.0634 -0.0952 0.1956  0.0463  439 GLU A CB  
3516  C CG  . GLU A 439 ? 0.9610 0.5802 2.1071 -0.1009 0.2170  0.0465  439 GLU A CG  
3517  C CD  . GLU A 439 ? 0.9698 0.6200 2.1423 -0.1027 0.2381  0.0384  439 GLU A CD  
3518  O OE1 . GLU A 439 ? 0.9314 0.6176 2.1449 -0.0951 0.2317  0.0320  439 GLU A OE1 
3519  O OE2 . GLU A 439 ? 1.0009 0.6389 2.1531 -0.1117 0.2614  0.0383  439 GLU A OE2 
3520  N N   . THR A 440 ? 0.8110 0.4134 1.9832 -0.1019 0.1655  0.0600  440 THR A N   
3521  C CA  . THR A 440 ? 0.7901 0.4055 1.9909 -0.1042 0.1566  0.0602  440 THR A CA  
3522  C C   . THR A 440 ? 0.7851 0.4346 2.0248 -0.1145 0.1739  0.0554  440 THR A C   
3523  O O   . THR A 440 ? 0.8000 0.4564 2.0389 -0.1209 0.1938  0.0533  440 THR A O   
3524  C CB  . THR A 440 ? 0.8208 0.3954 1.9880 -0.1090 0.1512  0.0683  440 THR A CB  
3525  O OG1 . THR A 440 ? 0.8424 0.3925 1.9783 -0.1212 0.1718  0.0726  440 THR A OG1 
3526  C CG2 . THR A 440 ? 0.8389 0.3839 1.9752 -0.0971 0.1293  0.0722  440 THR A CG2 
3527  N N   . SER A 441 ? 0.7813 0.4521 2.0551 -0.1158 0.1663  0.0531  441 SER A N   
3528  C CA  . SER A 441 ? 0.7932 0.4926 2.1022 -0.1267 0.1805  0.0489  441 SER A CA  
3529  C C   . SER A 441 ? 0.8062 0.5007 2.1253 -0.1321 0.1725  0.0507  441 SER A C   
3530  O O   . SER A 441 ? 0.7871 0.4785 2.1091 -0.1234 0.1533  0.0511  441 SER A O   
3531  C CB  . SER A 441 ? 0.7587 0.5025 2.1099 -0.1211 0.1804  0.0410  441 SER A CB  
3532  O OG  . SER A 441 ? 0.7643 0.5345 2.1459 -0.1318 0.1971  0.0366  441 SER A OG  
3533  N N   . GLU A 442 ? 0.8236 0.5169 2.1483 -0.1468 0.1879  0.0514  442 GLU A N   
3534  C CA  . GLU A 442 ? 0.8250 0.5113 2.1578 -0.1526 0.1810  0.0527  442 GLU A CA  
3535  C C   . GLU A 442 ? 0.8099 0.5344 2.1871 -0.1477 0.1697  0.0455  442 GLU A C   
3536  O O   . GLU A 442 ? 0.7965 0.5552 2.2019 -0.1438 0.1719  0.0397  442 GLU A O   
3537  C CB  . GLU A 442 ? 0.8490 0.5180 2.1720 -0.1700 0.1982  0.0560  442 GLU A CB  
3538  C CG  . GLU A 442 ? 0.8351 0.5347 2.1894 -0.1825 0.2188  0.0506  442 GLU A CG  
3539  C CD  . GLU A 442 ? 0.8593 0.5391 2.2050 -0.2004 0.2331  0.0541  442 GLU A CD  
3540  O OE1 . GLU A 442 ? 0.8487 0.4969 2.1722 -0.2014 0.2228  0.0595  442 GLU A OE1 
3541  O OE2 . GLU A 442 ? 0.8445 0.5386 2.2050 -0.2134 0.2541  0.0514  442 GLU A OE2 
3542  N N   . ASN A 443 ? 0.8257 0.5408 2.2055 -0.1470 0.1566  0.0463  443 ASN A N   
3543  C CA  . ASN A 443 ? 0.7871 0.5284 2.1987 -0.1404 0.1421  0.0407  443 ASN A CA  
3544  C C   . ASN A 443 ? 0.7242 0.4695 2.1328 -0.1242 0.1263  0.0400  443 ASN A C   
3545  O O   . ASN A 443 ? 0.7282 0.4808 2.1503 -0.1177 0.1119  0.0375  443 ASN A O   
3546  C CB  . ASN A 443 ? 0.7845 0.5657 2.2373 -0.1469 0.1494  0.0335  443 ASN A CB  
3547  C CG  . ASN A 443 ? 0.8021 0.5795 2.2620 -0.1632 0.1613  0.0333  443 ASN A CG  
3548  O OD1 . ASN A 443 ? 0.7655 0.5310 2.2256 -0.1671 0.1544  0.0335  443 ASN A OD1 
3549  N ND2 . ASN A 443 ? 0.8233 0.6112 2.2905 -0.1731 0.1797  0.0323  443 ASN A ND2 
3550  N N   . PHE A 444 ? 0.6907 0.4287 2.0802 -0.1181 0.1287  0.0422  444 PHE A N   
3551  C CA  . PHE A 444 ? 0.6554 0.3973 2.0434 -0.1036 0.1135  0.0413  444 PHE A CA  
3552  C C   . PHE A 444 ? 0.6892 0.3927 2.0417 -0.0976 0.1019  0.0472  444 PHE A C   
3553  O O   . PHE A 444 ? 0.7459 0.4214 2.0651 -0.1004 0.1085  0.0524  444 PHE A O   
3554  C CB  . PHE A 444 ? 0.6108 0.3703 2.0032 -0.0992 0.1203  0.0388  444 PHE A CB  
3555  C CG  . PHE A 444 ? 0.5516 0.3524 1.9849 -0.1007 0.1247  0.0321  444 PHE A CG  
3556  C CD1 . PHE A 444 ? 0.5023 0.3257 1.9595 -0.0921 0.1113  0.0281  444 PHE A CD1 
3557  C CD2 . PHE A 444 ? 0.5515 0.3677 1.9996 -0.1110 0.1419  0.0298  444 PHE A CD2 
3558  C CE1 . PHE A 444 ? 0.4627 0.3211 1.9545 -0.0932 0.1136  0.0226  444 PHE A CE1 
3559  C CE2 . PHE A 444 ? 0.5163 0.3698 2.0024 -0.1116 0.1436  0.0236  444 PHE A CE2 
3560  C CZ  . PHE A 444 ? 0.4735 0.3468 1.9799 -0.1024 0.1288  0.0203  444 PHE A CZ  
3561  N N   . THR A 445 ? 0.6598 0.3622 2.0196 -0.0891 0.0845  0.0461  445 THR A N   
3562  C CA  . THR A 445 ? 0.6804 0.3482 2.0119 -0.0828 0.0712  0.0509  445 THR A CA  
3563  C C   . THR A 445 ? 0.6546 0.3230 1.9806 -0.0695 0.0579  0.0502  445 THR A C   
3564  O O   . THR A 445 ? 0.5975 0.2901 1.9493 -0.0621 0.0485  0.0453  445 THR A O   
3565  C CB  . THR A 445 ? 0.6893 0.3528 2.0326 -0.0822 0.0611  0.0497  445 THR A CB  
3566  O OG1 . THR A 445 ? 0.7009 0.3999 2.0804 -0.0862 0.0660  0.0433  445 THR A OG1 
3567  C CG2 . THR A 445 ? 0.7331 0.3653 2.0550 -0.0917 0.0666  0.0548  445 THR A CG2 
3568  N N   . LEU A 446 ? 0.6830 0.3222 1.9731 -0.0673 0.0570  0.0553  446 LEU A N   
3569  C CA  . LEU A 446 ? 0.6843 0.3150 1.9622 -0.0553 0.0422  0.0555  446 LEU A CA  
3570  C C   . LEU A 446 ? 0.7189 0.3332 1.9948 -0.0476 0.0234  0.0565  446 LEU A C   
3571  O O   . LEU A 446 ? 0.7595 0.3501 2.0219 -0.0515 0.0223  0.0603  446 LEU A O   
3572  C CB  . LEU A 446 ? 0.7134 0.3134 1.9492 -0.0563 0.0469  0.0607  446 LEU A CB  
3573  C CG  . LEU A 446 ? 0.7067 0.3178 1.9391 -0.0636 0.0670  0.0597  446 LEU A CG  
3574  C CD1 . LEU A 446 ? 0.7396 0.3163 1.9258 -0.0632 0.0696  0.0645  446 LEU A CD1 
3575  C CD2 . LEU A 446 ? 0.6732 0.3233 1.9396 -0.0583 0.0669  0.0527  446 LEU A CD2 
3576  N N   . LEU A 447 ? 0.7339 0.3574 2.0207 -0.0364 0.0081  0.0533  447 LEU A N   
3577  C CA  . LEU A 447 ? 0.7892 0.4008 2.0798 -0.0288 -0.0091 0.0531  447 LEU A CA  
3578  C C   . LEU A 447 ? 0.8268 0.4272 2.1070 -0.0169 -0.0271 0.0531  447 LEU A C   
3579  O O   . LEU A 447 ? 0.8340 0.4439 2.1124 -0.0140 -0.0269 0.0515  447 LEU A O   
3580  C CB  . LEU A 447 ? 0.7464 0.3906 2.0775 -0.0295 -0.0079 0.0469  447 LEU A CB  
3581  C CG  . LEU A 447 ? 0.6785 0.3599 2.0397 -0.0261 -0.0071 0.0409  447 LEU A CG  
3582  C CD1 . LEU A 447 ? 0.6790 0.3613 2.0478 -0.0144 -0.0246 0.0383  447 LEU A CD1 
3583  C CD2 . LEU A 447 ? 0.6358 0.3460 2.0289 -0.0313 0.0003  0.0361  447 LEU A CD2 
3584  N N   . ASP A 448 ? 0.9345 0.5122 2.2062 -0.0102 -0.0430 0.0548  448 ASP A N   
3585  C CA  . ASP A 448 ? 1.0495 0.6163 2.3146 0.0015  -0.0626 0.0542  448 ASP A CA  
3586  C C   . ASP A 448 ? 1.0106 0.5600 2.2424 0.0018  -0.0621 0.0577  448 ASP A C   
3587  O O   . ASP A 448 ? 1.0482 0.5646 2.2411 -0.0025 -0.0582 0.0642  448 ASP A O   
3588  C CB  . ASP A 448 ? 1.0989 0.7000 2.4042 0.0088  -0.0707 0.0465  448 ASP A CB  
3589  C CG  . ASP A 448 ? 1.1317 0.7440 2.4666 0.0127  -0.0776 0.0421  448 ASP A CG  
3590  O OD1 . ASP A 448 ? 1.1415 0.7349 2.4721 0.0209  -0.0940 0.0425  448 ASP A OD1 
3591  O OD2 . ASP A 448 ? 1.1359 0.7756 2.4980 0.0077  -0.0669 0.0380  448 ASP A OD2 
3592  N N   . ASP A 449 ? 0.8961 0.4676 2.1432 0.0066  -0.0656 0.0529  449 ASP A N   
3593  C CA  . ASP A 449 ? 0.8947 0.4490 2.1155 0.0117  -0.0747 0.0541  449 ASP A CA  
3594  C C   . ASP A 449 ? 0.7839 0.3625 2.0136 0.0086  -0.0620 0.0506  449 ASP A C   
3595  O O   . ASP A 449 ? 0.7009 0.3135 1.9666 0.0097  -0.0599 0.0450  449 ASP A O   
3596  C CB  . ASP A 449 ? 0.9569 0.5081 2.1874 0.0235  -0.0986 0.0512  449 ASP A CB  
3597  C CG  . ASP A 449 ? 1.0646 0.5829 2.2765 0.0293  -0.1157 0.0552  449 ASP A CG  
3598  O OD1 . ASP A 449 ? 1.1107 0.6074 2.3037 0.0240  -0.1091 0.0606  449 ASP A OD1 
3599  O OD2 . ASP A 449 ? 1.1083 0.6222 2.3254 0.0394  -0.1362 0.0527  449 ASP A OD2 
3600  N N   . LEU A 450 ? 0.7585 0.3168 1.9528 0.0040  -0.0521 0.0543  450 LEU A N   
3601  C CA  . LEU A 450 ? 0.7213 0.2865 1.9076 0.0042  -0.0461 0.0517  450 LEU A CA  
3602  C C   . LEU A 450 ? 0.7208 0.2876 1.9129 0.0145  -0.0663 0.0479  450 LEU A C   
3603  O O   . LEU A 450 ? 0.7490 0.2929 1.9266 0.0206  -0.0845 0.0499  450 LEU A O   
3604  C CB  . LEU A 450 ? 0.7513 0.2794 1.8880 -0.0009 -0.0379 0.0578  450 LEU A CB  
3605  C CG  . LEU A 450 ? 0.7649 0.2823 1.8745 0.0005  -0.0349 0.0565  450 LEU A CG  
3606  C CD1 . LEU A 450 ? 0.7351 0.2863 1.8705 -0.0034 -0.0169 0.0514  450 LEU A CD1 
3607  C CD2 . LEU A 450 ? 0.8158 0.2917 1.8723 -0.0045 -0.0281 0.0630  450 LEU A CD2 
3608  N N   . LYS A 451 ? 0.6948 0.2870 1.9073 0.0162  -0.0636 0.0425  451 LYS A N   
3609  C CA  . LYS A 451 ? 0.7057 0.3002 1.9252 0.0248  -0.0820 0.0384  451 LYS A CA  
3610  C C   . LYS A 451 ? 0.7153 0.3042 1.9141 0.0249  -0.0773 0.0364  451 LYS A C   
3611  O O   . LYS A 451 ? 0.7276 0.3314 1.9314 0.0199  -0.0592 0.0351  451 LYS A O   
3612  C CB  . LYS A 451 ? 0.6772 0.3073 1.9453 0.0277  -0.0869 0.0330  451 LYS A CB  
3613  C CG  . LYS A 451 ? 0.6913 0.3223 1.9773 0.0302  -0.0966 0.0337  451 LYS A CG  
3614  C CD  . LYS A 451 ? 0.6557 0.3188 1.9870 0.0335  -0.1021 0.0280  451 LYS A CD  
3615  C CE  . LYS A 451 ? 0.6748 0.3372 2.0207 0.0350  -0.1075 0.0284  451 LYS A CE  
3616  N NZ  . LYS A 451 ? 0.6598 0.3549 2.0484 0.0365  -0.1082 0.0226  451 LYS A NZ  
3617  N N   . ILE A 452 ? 0.7197 0.2864 1.8952 0.0309  -0.0940 0.0358  452 ILE A N   
3618  C CA  . ILE A 452 ? 0.7256 0.2832 1.8777 0.0314  -0.0905 0.0334  452 ILE A CA  
3619  C C   . ILE A 452 ? 0.7029 0.2747 1.8771 0.0381  -0.1069 0.0271  452 ILE A C   
3620  O O   . ILE A 452 ? 0.7016 0.2754 1.8925 0.0433  -0.1255 0.0260  452 ILE A O   
3621  C CB  . ILE A 452 ? 0.7766 0.2901 1.8730 0.0308  -0.0932 0.0383  452 ILE A CB  
3622  C CG1 . ILE A 452 ? 0.7908 0.2921 1.8638 0.0220  -0.0710 0.0436  452 ILE A CG1 
3623  C CG2 . ILE A 452 ? 0.8070 0.3069 1.8777 0.0337  -0.0970 0.0346  452 ILE A CG2 
3624  C CD1 . ILE A 452 ? 0.7764 0.2830 1.8655 0.0181  -0.0670 0.0479  452 ILE A CD1 
3625  N N   . SER A 453 ? 0.6761 0.2580 1.8518 0.0379  -0.0999 0.0227  453 SER A N   
3626  C CA  . SER A 453 ? 0.6541 0.2484 1.8497 0.0430  -0.1138 0.0166  453 SER A CA  
3627  C C   . SER A 453 ? 0.6693 0.2530 1.8415 0.0435  -0.1099 0.0130  453 SER A C   
3628  O O   . SER A 453 ? 0.6579 0.2545 1.8343 0.0402  -0.0914 0.0115  453 SER A O   
3629  C CB  . SER A 453 ? 0.6062 0.2396 1.8518 0.0423  -0.1096 0.0134  453 SER A CB  
3630  O OG  . SER A 453 ? 0.5919 0.2364 1.8527 0.0453  -0.1174 0.0077  453 SER A OG  
3631  N N   . TYR A 454 ? 0.6830 0.2451 1.8344 0.0484  -0.1290 0.0107  454 TYR A N   
3632  C CA  . TYR A 454 ? 0.6915 0.2425 1.8222 0.0498  -0.1293 0.0059  454 TYR A CA  
3633  C C   . TYR A 454 ? 0.6613 0.2322 1.8268 0.0535  -0.1445 -0.0001 454 TYR A C   
3634  O O   . TYR A 454 ? 0.6706 0.2288 1.8314 0.0577  -0.1664 -0.0023 454 TYR A O   
3635  C CB  . TYR A 454 ? 0.7497 0.2575 1.8251 0.0513  -0.1378 0.0083  454 TYR A CB  
3636  C CG  . TYR A 454 ? 0.7849 0.2730 1.8248 0.0514  -0.1323 0.0043  454 TYR A CG  
3637  C CD1 . TYR A 454 ? 0.8025 0.2842 1.8193 0.0469  -0.1080 0.0054  454 TYR A CD1 
3638  C CD2 . TYR A 454 ? 0.8091 0.2852 1.8391 0.0559  -0.1509 -0.0014 454 TYR A CD2 
3639  C CE1 . TYR A 454 ? 0.8369 0.3015 1.8226 0.0473  -0.1015 0.0007  454 TYR A CE1 
3640  C CE2 . TYR A 454 ? 0.8411 0.2988 1.8387 0.0562  -0.1455 -0.0059 454 TYR A CE2 
3641  C CZ  . TYR A 454 ? 0.8552 0.3066 1.8297 0.0521  -0.1202 -0.0050 454 TYR A CZ  
3642  O OH  . TYR A 454 ? 0.8778 0.3102 1.8193 0.0527  -0.1137 -0.0102 454 TYR A OH  
3643  N N   . ASN A 455 ? 0.6181 0.2209 1.8204 0.0515  -0.1330 -0.0027 455 ASN A N   
3644  C CA  . ASN A 455 ? 0.5885 0.2124 1.8268 0.0534  -0.1441 -0.0078 455 ASN A CA  
3645  C C   . ASN A 455 ? 0.6073 0.2186 1.8282 0.0552  -0.1485 -0.0133 455 ASN A C   
3646  O O   . ASN A 455 ? 0.6131 0.2284 1.8290 0.0536  -0.1326 -0.0149 455 ASN A O   
3647  C CB  . ASN A 455 ? 0.5413 0.2008 1.8218 0.0504  -0.1307 -0.0078 455 ASN A CB  
3648  C CG  . ASN A 455 ? 0.5241 0.2037 1.8408 0.0515  -0.1420 -0.0123 455 ASN A CG  
3649  O OD1 . ASN A 455 ? 0.5321 0.2017 1.8429 0.0537  -0.1550 -0.0169 455 ASN A OD1 
3650  N ND2 . ASN A 455 ? 0.4899 0.1975 1.8438 0.0493  -0.1363 -0.0115 455 ASN A ND2 
3651  N N   . THR A 456 ? 0.6191 0.2171 1.8346 0.0585  -0.1706 -0.0169 456 THR A N   
3652  C CA  . THR A 456 ? 0.6465 0.2252 1.8373 0.0603  -0.1777 -0.0224 456 THR A CA  
3653  C C   . THR A 456 ? 0.6157 0.2155 1.8408 0.0599  -0.1815 -0.0283 456 THR A C   
3654  O O   . THR A 456 ? 0.6309 0.2157 1.8404 0.0613  -0.1905 -0.0337 456 THR A O   
3655  C CB  . THR A 456 ? 0.6868 0.2353 1.8478 0.0640  -0.2011 -0.0230 456 THR A CB  
3656  O OG1 . THR A 456 ? 0.6669 0.2302 1.8605 0.0655  -0.2157 -0.0219 456 THR A OG1 
3657  C CG2 . THR A 456 ? 0.7255 0.2418 1.8364 0.0641  -0.1963 -0.0180 456 THR A CG2 
3658  N N   . HIS A 457 ? 0.5759 0.2081 1.8456 0.0577  -0.1756 -0.0273 457 HIS A N   
3659  C CA  . HIS A 457 ? 0.5532 0.2067 1.8546 0.0560  -0.1728 -0.0314 457 HIS A CA  
3660  C C   . HIS A 457 ? 0.5625 0.2143 1.8779 0.0567  -0.1937 -0.0373 457 HIS A C   
3661  O O   . HIS A 457 ? 0.5597 0.2235 1.8953 0.0548  -0.1918 -0.0410 457 HIS A O   
3662  C CB  . HIS A 457 ? 0.5579 0.2081 1.8444 0.0555  -0.1558 -0.0330 457 HIS A CB  
3663  C CG  . HIS A 457 ? 0.5380 0.2077 1.8379 0.0534  -0.1347 -0.0284 457 HIS A CG  
3664  N ND1 . HIS A 457 ? 0.5533 0.2162 1.8333 0.0528  -0.1228 -0.0238 457 HIS A ND1 
3665  C CD2 . HIS A 457 ? 0.5062 0.2024 1.8391 0.0514  -0.1245 -0.0278 457 HIS A CD2 
3666  C CE1 . HIS A 457 ? 0.5276 0.2135 1.8296 0.0505  -0.1064 -0.0211 457 HIS A CE1 
3667  N NE2 . HIS A 457 ? 0.4994 0.2051 1.8325 0.0500  -0.1075 -0.0234 457 HIS A NE2 
3668  N N   . LEU A 458 ? 0.5752 0.2123 1.8809 0.0593  -0.2135 -0.0381 458 LEU A N   
3669  C CA  . LEU A 458 ? 0.5743 0.2089 1.8933 0.0602  -0.2358 -0.0442 458 LEU A CA  
3670  C C   . LEU A 458 ? 0.5396 0.2065 1.9109 0.0576  -0.2377 -0.0450 458 LEU A C   
3671  O O   . LEU A 458 ? 0.5372 0.2112 1.9255 0.0592  -0.2476 -0.0439 458 LEU A O   
3672  C CB  . LEU A 458 ? 0.6066 0.2169 1.9014 0.0644  -0.2573 -0.0445 458 LEU A CB  
3673  C CG  . LEU A 458 ? 0.6500 0.2236 1.8876 0.0670  -0.2578 -0.0432 458 LEU A CG  
3674  C CD1 . LEU A 458 ? 0.6827 0.2328 1.9000 0.0714  -0.2829 -0.0436 458 LEU A CD1 
3675  C CD2 . LEU A 458 ? 0.6644 0.2249 1.8812 0.0660  -0.2541 -0.0485 458 LEU A CD2 
3676  N N   . GLY A 459 ? 0.5173 0.2025 1.9131 0.0537  -0.2281 -0.0470 459 GLY A N   
3677  C CA  . GLY A 459 ? 0.4929 0.2071 1.9361 0.0502  -0.2286 -0.0481 459 GLY A CA  
3678  C C   . GLY A 459 ? 0.4756 0.2101 1.9355 0.0491  -0.2124 -0.0422 459 GLY A C   
3679  O O   . GLY A 459 ? 0.5161 0.2544 1.9678 0.0478  -0.1944 -0.0386 459 GLY A O   
3680  N N   . TRP A 460 ? 0.4612 0.2087 1.9456 0.0497  -0.2192 -0.0417 460 TRP A N   
3681  C CA  . TRP A 460 ? 0.4492 0.2117 1.9450 0.0493  -0.2062 -0.0366 460 TRP A CA  
3682  C C   . TRP A 460 ? 0.4732 0.2182 1.9445 0.0539  -0.2119 -0.0332 460 TRP A C   
3683  O O   . TRP A 460 ? 0.4724 0.2237 1.9440 0.0536  -0.2003 -0.0285 460 TRP A O   
3684  C CB  . TRP A 460 ? 0.4254 0.2155 1.9669 0.0466  -0.2069 -0.0387 460 TRP A CB  
3685  C CG  . TRP A 460 ? 0.4151 0.2214 1.9804 0.0411  -0.2005 -0.0413 460 TRP A CG  
3686  C CD1 . TRP A 460 ? 0.4337 0.2466 2.0225 0.0385  -0.2114 -0.0470 460 TRP A CD1 
3687  C CD2 . TRP A 460 ? 0.4091 0.2260 1.9764 0.0374  -0.1816 -0.0379 460 TRP A CD2 
3688  N NE1 . TRP A 460 ? 0.4283 0.2531 2.0311 0.0329  -0.1998 -0.0469 460 TRP A NE1 
3689  C CE2 . TRP A 460 ? 0.4067 0.2341 1.9965 0.0326  -0.1821 -0.0413 460 TRP A CE2 
3690  C CE3 . TRP A 460 ? 0.4029 0.2211 1.9556 0.0375  -0.1652 -0.0325 460 TRP A CE3 
3691  C CZ2 . TRP A 460 ? 0.3894 0.2266 1.9854 0.0286  -0.1673 -0.0388 460 TRP A CZ2 
3692  C CZ3 . TRP A 460 ? 0.3932 0.2232 1.9544 0.0339  -0.1512 -0.0307 460 TRP A CZ3 
3693  C CH2 . TRP A 460 ? 0.3866 0.2248 1.9677 0.0298  -0.1526 -0.0335 460 TRP A CH2 
3694  N N   . ALA A 461 ? 0.4933 0.2153 1.9431 0.0580  -0.2307 -0.0356 461 ALA A N   
3695  C CA  . ALA A 461 ? 0.5190 0.2176 1.9373 0.0624  -0.2372 -0.0318 461 ALA A CA  
3696  C C   . ALA A 461 ? 0.5276 0.2163 1.9149 0.0608  -0.2174 -0.0257 461 ALA A C   
3697  O O   . ALA A 461 ? 0.5332 0.2107 1.8962 0.0595  -0.2092 -0.0261 461 ALA A O   
3698  C CB  . ALA A 461 ? 0.5525 0.2240 1.9441 0.0662  -0.2587 -0.0353 461 ALA A CB  
3699  N N   . ILE A 462 ? 0.5245 0.2168 1.9137 0.0611  -0.2101 -0.0208 462 ILE A N   
3700  C CA  . ILE A 462 ? 0.5431 0.2298 1.9097 0.0586  -0.1907 -0.0151 462 ILE A CA  
3701  C C   . ILE A 462 ? 0.5906 0.2424 1.9094 0.0611  -0.1954 -0.0115 462 ILE A C   
3702  O O   . ILE A 462 ? 0.6115 0.2553 1.9082 0.0586  -0.1796 -0.0067 462 ILE A O   
3703  C CB  . ILE A 462 ? 0.5241 0.2324 1.9172 0.0566  -0.1797 -0.0119 462 ILE A CB  
3704  C CG1 . ILE A 462 ? 0.5368 0.2384 1.9347 0.0605  -0.1933 -0.0107 462 ILE A CG1 
3705  C CG2 . ILE A 462 ? 0.4866 0.2273 1.9215 0.0534  -0.1723 -0.0148 462 ILE A CG2 
3706  C CD1 . ILE A 462 ? 0.5758 0.2522 1.9379 0.0613  -0.1904 -0.0047 462 ILE A CD1 
3707  N N   . GLY A 463 ? 0.6094 0.2398 1.9116 0.0655  -0.2169 -0.0138 463 GLY A N   
3708  C CA  . GLY A 463 ? 0.6590 0.2523 1.9099 0.0676  -0.2223 -0.0108 463 GLY A CA  
3709  C C   . GLY A 463 ? 0.6838 0.2635 1.9195 0.0685  -0.2214 -0.0041 463 GLY A C   
3710  O O   . GLY A 463 ? 0.6535 0.2488 1.9193 0.0699  -0.2254 -0.0033 463 GLY A O   
3711  N N   . SER A 464 ? 0.7290 0.2775 1.9162 0.0677  -0.2159 0.0005  464 SER A N   
3712  C CA  . SER A 464 ? 0.7593 0.2883 1.9251 0.0682  -0.2163 0.0073  464 SER A CA  
3713  C C   . SER A 464 ? 0.7295 0.2815 1.9193 0.0634  -0.1956 0.0108  464 SER A C   
3714  O O   . SER A 464 ? 0.7032 0.2810 1.9154 0.0592  -0.1782 0.0089  464 SER A O   
3715  C CB  . SER A 464 ? 0.8158 0.3055 1.9229 0.0673  -0.2136 0.0114  464 SER A CB  
3716  O OG  . SER A 464 ? 0.8601 0.3232 1.9415 0.0727  -0.2377 0.0089  464 SER A OG  
3717  N N   . GLN A 465 ? 0.7361 0.2771 1.9209 0.0646  -0.1994 0.0158  465 GLN A N   
3718  C CA  . GLN A 465 ? 0.7363 0.2898 1.9330 0.0596  -0.1808 0.0201  465 GLN A CA  
3719  C C   . GLN A 465 ? 0.7891 0.3106 1.9535 0.0605  -0.1861 0.0269  465 GLN A C   
3720  O O   . GLN A 465 ? 0.8497 0.3436 1.9901 0.0661  -0.2064 0.0280  465 GLN A O   
3721  C CB  . GLN A 465 ? 0.6998 0.2890 1.9498 0.0603  -0.1810 0.0168  465 GLN A CB  
3722  C CG  . GLN A 465 ? 0.6777 0.3008 1.9599 0.0567  -0.1677 0.0123  465 GLN A CG  
3723  C CD  . GLN A 465 ? 0.6604 0.3154 1.9902 0.0567  -0.1668 0.0097  465 GLN A CD  
3724  O OE1 . GLN A 465 ? 0.6840 0.3466 2.0376 0.0616  -0.1831 0.0058  465 GLN A OE1 
3725  N NE2 . GLN A 465 ? 0.6433 0.3165 1.9871 0.0513  -0.1479 0.0114  465 GLN A NE2 
3726  N N   . ALA A 466 ? 0.7743 0.2988 1.9388 0.0549  -0.1687 0.0315  466 ALA A N   
3727  C CA  . ALA A 466 ? 0.8028 0.2959 1.9369 0.0549  -0.1724 0.0384  466 ALA A CA  
3728  C C   . ALA A 466 ? 0.7725 0.2813 1.9281 0.0496  -0.1567 0.0412  466 ALA A C   
3729  O O   . ALA A 466 ? 0.7403 0.2768 1.9188 0.0438  -0.1380 0.0392  466 ALA A O   
3730  C CB  . ALA A 466 ? 0.8491 0.3061 1.9269 0.0514  -0.1659 0.0431  466 ALA A CB  
3731  N N   . SER A 467 ? 0.8003 0.2916 1.9502 0.0521  -0.1660 0.0452  467 SER A N   
3732  C CA  . SER A 467 ? 0.8114 0.3070 1.9688 0.0459  -0.1507 0.0489  467 SER A CA  
3733  C C   . SER A 467 ? 0.8385 0.2914 1.9454 0.0422  -0.1477 0.0574  467 SER A C   
3734  O O   . SER A 467 ? 0.8492 0.2715 1.9332 0.0483  -0.1664 0.0608  467 SER A O   
3735  C CB  . SER A 467 ? 0.8129 0.3258 2.0096 0.0508  -0.1606 0.0461  467 SER A CB  
3736  O OG  . SER A 467 ? 0.7969 0.3508 2.0392 0.0515  -0.1574 0.0388  467 SER A OG  
3737  N N   . VAL A 468 ? 0.8305 0.2818 1.9207 0.0322  -0.1240 0.0605  468 VAL A N   
3738  C CA  . VAL A 468 ? 0.8637 0.2768 1.9074 0.0261  -0.1160 0.0687  468 VAL A CA  
3739  C C   . VAL A 468 ? 0.8358 0.2554 1.8956 0.0195  -0.1036 0.0716  468 VAL A C   
3740  O O   . VAL A 468 ? 0.7826 0.2351 1.8749 0.0135  -0.0869 0.0683  468 VAL A O   
3741  C CB  . VAL A 468 ? 0.8735 0.2794 1.8869 0.0192  -0.0978 0.0694  468 VAL A CB  
3742  C CG1 . VAL A 468 ? 0.9168 0.2851 1.8816 0.0108  -0.0844 0.0776  468 VAL A CG1 
3743  C CG2 . VAL A 468 ? 0.8911 0.2865 1.8861 0.0264  -0.1125 0.0662  468 VAL A CG2 
3744  N N   . SER A 469 ? 0.8721 0.2588 1.9092 0.0211  -0.1139 0.0777  469 SER A N   
3745  C CA  . SER A 469 ? 0.8777 0.2612 1.9208 0.0142  -0.1028 0.0814  469 SER A CA  
3746  C C   . SER A 469 ? 0.9074 0.2747 1.9177 0.0011  -0.0785 0.0869  469 SER A C   
3747  O O   . SER A 469 ? 0.9462 0.2820 1.9106 -0.0006 -0.0771 0.0915  469 SER A O   
3748  C CB  . SER A 469 ? 0.9071 0.2585 1.9358 0.0209  -0.1227 0.0859  469 SER A CB  
3749  O OG  . SER A 469 ? 0.9127 0.2551 1.9415 0.0136  -0.1120 0.0900  469 SER A OG  
3750  N N   . ILE A 470 ? 0.8906 0.2789 1.9241 -0.0084 -0.0592 0.0861  470 ILE A N   
3751  C CA  . ILE A 470 ? 0.9286 0.3023 1.9350 -0.0216 -0.0357 0.0911  470 ILE A CA  
3752  C C   . ILE A 470 ? 0.9473 0.3046 1.9510 -0.0285 -0.0310 0.0961  470 ILE A C   
3753  O O   . ILE A 470 ? 0.9562 0.3163 1.9576 -0.0410 -0.0090 0.0980  470 ILE A O   
3754  C CB  . ILE A 470 ? 0.8966 0.3104 1.9318 -0.0286 -0.0139 0.0853  470 ILE A CB  
3755  C CG1 . ILE A 470 ? 0.8583 0.3118 1.9466 -0.0299 -0.0109 0.0798  470 ILE A CG1 
3756  C CG2 . ILE A 470 ? 0.8800 0.3070 1.9155 -0.0220 -0.0180 0.0803  470 ILE A CG2 
3757  C CD1 . ILE A 470 ? 0.8154 0.3119 1.9381 -0.0335 0.0045  0.0732  470 ILE A CD1 
3758  N N   . SER A 471 ? 0.9648 0.3055 1.9702 -0.0203 -0.0515 0.0979  471 SER A N   
3759  C CA  . SER A 471 ? 0.9864 0.3062 1.9863 -0.0254 -0.0499 0.1027  471 SER A CA  
3760  C C   . SER A 471 ? 1.0320 0.3143 1.9840 -0.0379 -0.0334 0.1116  471 SER A C   
3761  O O   . SER A 471 ? 1.0237 0.3083 1.9810 -0.0500 -0.0153 0.1133  471 SER A O   
3762  C CB  . SER A 471 ? 1.0096 0.3048 2.0038 -0.0132 -0.0763 0.1047  471 SER A CB  
3763  O OG  . SER A 471 ? 0.9881 0.3071 2.0095 -0.0002 -0.0943 0.0977  471 SER A OG  
3764  N N   . ASP A 472 ? 1.0840 0.3320 1.9890 -0.0349 -0.0399 0.1168  472 ASP A N   
3765  C CA  . ASP A 472 ? 1.1620 0.3634 2.0115 -0.0446 -0.0293 0.1265  472 ASP A CA  
3766  C C   . ASP A 472 ? 1.1771 0.3912 2.0192 -0.0583 0.0007  0.1258  472 ASP A C   
3767  O O   . ASP A 472 ? 1.2496 0.4272 2.0448 -0.0677 0.0133  0.1333  472 ASP A O   
3768  C CB  . ASP A 472 ? 1.2130 0.3719 2.0138 -0.0351 -0.0499 0.1319  472 ASP A CB  
3769  C CG  . ASP A 472 ? 1.1943 0.3717 1.9985 -0.0269 -0.0569 0.1257  472 ASP A CG  
3770  O OD1 . ASP A 472 ? 1.1711 0.3864 2.0022 -0.0318 -0.0392 0.1193  472 ASP A OD1 
3771  O OD2 . ASP A 472 ? 1.2147 0.3694 1.9973 -0.0154 -0.0810 0.1270  472 ASP A OD2 
3772  N N   . GLN A 473 ? 1.1279 0.3920 2.0148 -0.0594 0.0120  0.1170  473 GLN A N   
3773  C CA  . GLN A 473 ? 1.1107 0.3914 1.9972 -0.0711 0.0397  0.1150  473 GLN A CA  
3774  C C   . GLN A 473 ? 1.0889 0.4118 2.0254 -0.0800 0.0568  0.1096  473 GLN A C   
3775  O O   . GLN A 473 ? 1.0907 0.4320 2.0342 -0.0896 0.0799  0.1070  473 GLN A O   
3776  C CB  . GLN A 473 ? 1.0895 0.3891 1.9788 -0.0636 0.0377  0.1090  473 GLN A CB  
3777  C CG  . GLN A 473 ? 1.1315 0.3893 1.9641 -0.0590 0.0291  0.1137  473 GLN A CG  
3778  C CD  . GLN A 473 ? 1.0932 0.3710 1.9301 -0.0531 0.0298  0.1068  473 GLN A CD  
3779  O OE1 . GLN A 473 ? 1.0595 0.3594 1.9063 -0.0598 0.0519  0.1025  473 GLN A OE1 
3780  N NE2 . GLN A 473 ? 1.0957 0.3651 1.9251 -0.0401 0.0050  0.1052  473 GLN A NE2 
3781  N N   . LEU A 474 ? 1.0948 0.4321 2.0652 -0.0770 0.0460  0.1076  474 LEU A N   
3782  C CA  . LEU A 474 ? 1.0816 0.4601 2.1007 -0.0840 0.0586  0.1015  474 LEU A CA  
3783  C C   . LEU A 474 ? 1.1388 0.5129 2.1488 -0.1014 0.0856  0.1043  474 LEU A C   
3784  O O   . LEU A 474 ? 1.1791 0.5909 2.2224 -0.1075 0.1014  0.0982  474 LEU A O   
3785  C CB  . LEU A 474 ? 1.0772 0.4626 2.1249 -0.0802 0.0449  0.0998  474 LEU A CB  
3786  C CG  . LEU A 474 ? 1.0408 0.4621 2.1314 -0.0676 0.0285  0.0918  474 LEU A CG  
3787  C CD1 . LEU A 474 ? 0.9902 0.4575 2.1152 -0.0670 0.0374  0.0840  474 LEU A CD1 
3788  C CD2 . LEU A 474 ? 1.0758 0.4746 2.1472 -0.0531 0.0041  0.0936  474 LEU A CD2 
3789  N N   . ASP A 475 ? 1.1981 0.5269 2.1649 -0.1092 0.0902  0.1132  475 ASP A N   
3790  C CA  . ASP A 475 ? 1.2185 0.5388 2.1740 -0.1270 0.1162  0.1165  475 ASP A CA  
3791  C C   . ASP A 475 ? 1.1995 0.5416 2.1577 -0.1332 0.1384  0.1125  475 ASP A C   
3792  O O   . ASP A 475 ? 1.1774 0.5429 2.1598 -0.1456 0.1595  0.1093  475 ASP A O   
3793  C CB  . ASP A 475 ? 1.3173 0.5790 2.2149 -0.1333 0.1175  0.1276  475 ASP A CB  
3794  C CG  . ASP A 475 ? 1.3619 0.6000 2.2582 -0.1353 0.1071  0.1323  475 ASP A CG  
3795  O OD1 . ASP A 475 ? 1.3603 0.6289 2.3017 -0.1309 0.0980  0.1261  475 ASP A OD1 
3796  O OD2 . ASP A 475 ? 1.4061 0.5944 2.2553 -0.1413 0.1083  0.1420  475 ASP A OD2 
3797  N N   . LYS A 476 ? 1.2263 0.5607 2.1607 -0.1241 0.1328  0.1121  476 LYS A N   
3798  C CA  . LYS A 476 ? 1.1917 0.5339 2.1144 -0.1292 0.1536  0.1096  476 LYS A CA  
3799  C C   . LYS A 476 ? 1.0928 0.4916 2.0705 -0.1288 0.1636  0.0993  476 LYS A C   
3800  O O   . LYS A 476 ? 1.0079 0.4388 2.0272 -0.1203 0.1492  0.0938  476 LYS A O   
3801  C CB  . LYS A 476 ? 1.2097 0.5295 2.0944 -0.1179 0.1418  0.1108  476 LYS A CB  
3802  C CG  . LYS A 476 ? 1.2684 0.5307 2.0950 -0.1152 0.1273  0.1207  476 LYS A CG  
3803  C CD  . LYS A 476 ? 1.2826 0.5293 2.0837 -0.1004 0.1058  0.1203  476 LYS A CD  
3804  C CE  . LYS A 476 ? 1.3222 0.5629 2.0944 -0.1026 0.1214  0.1183  476 LYS A CE  
3805  N NZ  . LYS A 476 ? 1.3211 0.5676 2.0917 -0.0878 0.1018  0.1136  476 LYS A NZ  
3806  N N   . LYS A 477 ? 1.1008 0.5092 2.0756 -0.1379 0.1887  0.0968  477 LYS A N   
3807  C CA  . LYS A 477 ? 1.0607 0.5194 2.0832 -0.1374 0.1996  0.0872  477 LYS A CA  
3808  C C   . LYS A 477 ? 1.0270 0.4959 2.0488 -0.1225 0.1866  0.0826  477 LYS A C   
3809  O O   . LYS A 477 ? 0.9999 0.5056 2.0640 -0.1142 0.1760  0.0762  477 LYS A O   
3810  C CB  . LYS A 477 ? 1.0956 0.5606 2.1190 -0.1532 0.2311  0.0860  477 LYS A CB  
3811  C CG  . LYS A 477 ? 1.0828 0.6021 2.1633 -0.1548 0.2428  0.0762  477 LYS A CG  
3812  C CD  . LYS A 477 ? 1.1305 0.6653 2.2108 -0.1510 0.2562  0.0701  477 LYS A CD  
3813  C CE  . LYS A 477 ? 1.1270 0.7005 2.2457 -0.1371 0.2433  0.0620  477 LYS A CE  
3814  N NZ  . LYS A 477 ? 1.0986 0.7065 2.2665 -0.1337 0.2294  0.0585  477 LYS A NZ  
3815  N N   . ILE A 478 ? 1.0574 0.4911 2.0293 -0.1191 0.1859  0.0862  478 ILE A N   
3816  C CA  . ILE A 478 ? 1.0326 0.4718 1.9988 -0.1062 0.1750  0.0817  478 ILE A CA  
3817  C C   . ILE A 478 ? 1.0336 0.4406 1.9697 -0.0951 0.1468  0.0867  478 ILE A C   
3818  O O   . ILE A 478 ? 1.0696 0.4307 1.9536 -0.0974 0.1448  0.0941  478 ILE A O   
3819  C CB  . ILE A 478 ? 1.0664 0.4920 1.9996 -0.1103 0.1958  0.0802  478 ILE A CB  
3820  C CG1 . ILE A 478 ? 1.0611 0.5164 2.0230 -0.1220 0.2256  0.0752  478 ILE A CG1 
3821  C CG2 . ILE A 478 ? 1.0619 0.4923 1.9895 -0.0969 0.1839  0.0749  478 ILE A CG2 
3822  C CD1 . ILE A 478 ? 1.0231 0.5219 2.0250 -0.1155 0.2313  0.0649  478 ILE A CD1 
3823  N N   . ILE A 479 ? 0.9769 0.4082 1.9460 -0.0830 0.1254  0.0823  479 ILE A N   
3824  C CA  . ILE A 479 ? 0.9758 0.3841 1.9261 -0.0713 0.0974  0.0851  479 ILE A CA  
3825  C C   . ILE A 479 ? 0.9620 0.3677 1.8962 -0.0618 0.0901  0.0810  479 ILE A C   
3826  O O   . ILE A 479 ? 0.9124 0.3530 1.8782 -0.0586 0.0954  0.0735  479 ILE A O   
3827  C CB  . ILE A 479 ? 0.9368 0.3716 1.9323 -0.0645 0.0792  0.0825  479 ILE A CB  
3828  C CG1 . ILE A 479 ? 0.9459 0.3840 1.9581 -0.0744 0.0874  0.0855  479 ILE A CG1 
3829  C CG2 . ILE A 479 ? 0.9467 0.3589 1.9258 -0.0523 0.0505  0.0848  479 ILE A CG2 
3830  C CD1 . ILE A 479 ? 0.9071 0.3690 1.9612 -0.0683 0.0710  0.0826  479 ILE A CD1 
3831  N N   . THR A 480 ? 0.9967 0.3596 1.8810 -0.0573 0.0767  0.0860  480 THR A N   
3832  C CA  . THR A 480 ? 1.0103 0.3637 1.8712 -0.0495 0.0699  0.0824  480 THR A CA  
3833  C C   . THR A 480 ? 1.0131 0.3473 1.8616 -0.0373 0.0379  0.0840  480 THR A C   
3834  O O   . THR A 480 ? 1.0394 0.3504 1.8751 -0.0363 0.0243  0.0902  480 THR A O   
3835  C CB  . THR A 480 ? 1.0649 0.3821 1.8703 -0.0574 0.0884  0.0861  480 THR A CB  
3836  O OG1 . THR A 480 ? 1.1107 0.3859 1.8780 -0.0610 0.0810  0.0958  480 THR A OG1 
3837  C CG2 . THR A 480 ? 1.0540 0.3928 1.8752 -0.0695 0.1212  0.0834  480 THR A CG2 
3838  N N   . SER A 481 ? 1.0033 0.3473 1.8570 -0.0278 0.0255  0.0780  481 SER A N   
3839  C CA  . SER A 481 ? 1.0067 0.3370 1.8543 -0.0161 -0.0052 0.0780  481 SER A CA  
3840  C C   . SER A 481 ? 0.9956 0.3248 1.8302 -0.0093 -0.0121 0.0719  481 SER A C   
3841  O O   . SER A 481 ? 0.9521 0.3160 1.8203 -0.0079 -0.0043 0.0646  481 SER A O   
3842  C CB  . SER A 481 ? 0.9649 0.3287 1.8668 -0.0102 -0.0200 0.0750  481 SER A CB  
3843  O OG  . SER A 481 ? 0.9906 0.3406 1.8878 0.0007  -0.0495 0.0750  481 SER A OG  
3844  N N   . GLU A 482 ? 1.0367 0.3247 1.8228 -0.0045 -0.0288 0.0751  482 GLU A N   
3845  C CA  . GLU A 482 ? 1.0458 0.3247 1.8114 0.0018  -0.0381 0.0697  482 GLU A CA  
3846  C C   . GLU A 482 ? 1.0418 0.3172 1.8170 0.0134  -0.0720 0.0681  482 GLU A C   
3847  O O   . GLU A 482 ? 1.0748 0.3207 1.8270 0.0167  -0.0905 0.0740  482 GLU A O   
3848  C CB  . GLU A 482 ? 1.1080 0.3391 1.8046 -0.0030 -0.0291 0.0743  482 GLU A CB  
3849  C CG  . GLU A 482 ? 1.1332 0.3468 1.7989 0.0034  -0.0402 0.0689  482 GLU A CG  
3850  C CD  . GLU A 482 ? 1.1963 0.3703 1.7981 -0.0030 -0.0228 0.0713  482 GLU A CD  
3851  O OE1 . GLU A 482 ? 1.2490 0.3803 1.8034 -0.0056 -0.0286 0.0799  482 GLU A OE1 
3852  O OE2 . GLU A 482 ? 1.1952 0.3789 1.7930 -0.0053 -0.0041 0.0647  482 GLU A OE2 
3853  N N   . ASN A 483 ? 1.0167 0.3219 1.8265 0.0195  -0.0801 0.0598  483 ASN A N   
3854  C CA  . ASN A 483 ? 1.0187 0.3298 1.8493 0.0297  -0.1100 0.0566  483 ASN A CA  
3855  C C   . ASN A 483 ? 1.0406 0.3446 1.8539 0.0344  -0.1187 0.0500  483 ASN A C   
3856  O O   . ASN A 483 ? 1.0445 0.3623 1.8602 0.0309  -0.0996 0.0453  483 ASN A O   
3857  C CB  . ASN A 483 ? 0.9610 0.3199 1.8585 0.0314  -0.1106 0.0527  483 ASN A CB  
3858  C CG  . ASN A 483 ? 0.9539 0.3224 1.8692 0.0253  -0.0977 0.0580  483 ASN A CG  
3859  O OD1 . ASN A 483 ? 0.9400 0.3126 1.8768 0.0292  -0.1124 0.0598  483 ASN A OD1 
3860  N ND2 . ASN A 483 ? 0.9627 0.3358 1.8717 0.0159  -0.0704 0.0598  483 ASN A ND2 
3861  N N   . PHE A 484 ? 1.0685 0.3512 1.8655 0.0425  -0.1476 0.0491  484 PHE A N   
3862  C CA  . PHE A 484 ? 1.0893 0.3621 1.8678 0.0469  -0.1585 0.0424  484 PHE A CA  
3863  C C   . PHE A 484 ? 1.0506 0.3562 1.8805 0.0539  -0.1780 0.0349  484 PHE A C   
3864  O O   . PHE A 484 ? 1.0302 0.3566 1.9004 0.0569  -0.1888 0.0358  484 PHE A O   
3865  C CB  . PHE A 484 ? 1.1531 0.3726 1.8673 0.0497  -0.1761 0.0469  484 PHE A CB  
3866  C CG  . PHE A 484 ? 1.1983 0.3855 1.8588 0.0413  -0.1525 0.0534  484 PHE A CG  
3867  C CD1 . PHE A 484 ? 1.2154 0.3944 1.8467 0.0368  -0.1323 0.0495  484 PHE A CD1 
3868  C CD2 . PHE A 484 ? 1.2178 0.3843 1.8598 0.0373  -0.1488 0.0631  484 PHE A CD2 
3869  C CE1 . PHE A 484 ? 1.2582 0.4092 1.8423 0.0283  -0.1085 0.0550  484 PHE A CE1 
3870  C CE2 . PHE A 484 ? 1.2581 0.3956 1.8521 0.0283  -0.1254 0.0691  484 PHE A CE2 
3871  C CZ  . PHE A 484 ? 1.2811 0.4111 1.8462 0.0237  -0.1050 0.0650  484 PHE A CZ  
3872  N N   . PHE A 485 ? 1.0460 0.3559 1.8748 0.0562  -0.1817 0.0273  485 PHE A N   
3873  C CA  . PHE A 485 ? 1.0167 0.3503 1.8869 0.0624  -0.2029 0.0204  485 PHE A CA  
3874  C C   . PHE A 485 ? 1.0596 0.3726 1.9002 0.0657  -0.2160 0.0140  485 PHE A C   
3875  O O   . PHE A 485 ? 1.1196 0.4211 1.9305 0.0623  -0.1990 0.0118  485 PHE A O   
3876  C CB  . PHE A 485 ? 0.9510 0.3329 1.8792 0.0602  -0.1879 0.0157  485 PHE A CB  
3877  C CG  . PHE A 485 ? 0.9161 0.3196 1.8716 0.0557  -0.1706 0.0210  485 PHE A CG  
3878  C CD1 . PHE A 485 ? 0.9246 0.3257 1.8631 0.0487  -0.1434 0.0246  485 PHE A CD1 
3879  C CD2 . PHE A 485 ? 0.8864 0.3111 1.8833 0.0584  -0.1823 0.0220  485 PHE A CD2 
3880  C CE1 . PHE A 485 ? 0.9000 0.3200 1.8635 0.0441  -0.1292 0.0292  485 PHE A CE1 
3881  C CE2 . PHE A 485 ? 0.8611 0.3034 1.8808 0.0543  -0.1675 0.0264  485 PHE A CE2 
3882  C CZ  . PHE A 485 ? 0.8671 0.3068 1.8699 0.0470  -0.1416 0.0300  485 PHE A CZ  
3883  N N   . ASN A 486 ? 1.0540 0.3649 1.9068 0.0722  -0.2456 0.0102  486 ASN A N   
3884  C CA  . ASN A 486 ? 1.0639 0.3638 1.9022 0.0752  -0.2601 0.0023  486 ASN A CA  
3885  C C   . ASN A 486 ? 1.0129 0.3502 1.8932 0.0728  -0.2452 -0.0048 486 ASN A C   
3886  O O   . ASN A 486 ? 0.9678 0.3430 1.9029 0.0724  -0.2421 -0.0054 486 ASN A O   
3887  C CB  . ASN A 486 ? 1.0643 0.3557 1.9109 0.0824  -0.2960 -0.0002 486 ASN A CB  
3888  C CG  . ASN A 486 ? 1.1123 0.3616 1.9110 0.0856  -0.3122 0.0069  486 ASN A CG  
3889  O OD1 . ASN A 486 ? 1.1063 0.3599 1.9246 0.0888  -0.3236 0.0115  486 ASN A OD1 
3890  N ND2 . ASN A 486 ? 1.1652 0.3720 1.8995 0.0848  -0.3128 0.0081  486 ASN A ND2 
3891  N N   . ILE A 487 ? 1.0240 0.3492 1.8767 0.0712  -0.2351 -0.0099 487 ILE A N   
3892  C CA  . ILE A 487 ? 0.9794 0.3346 1.8673 0.0699  -0.2244 -0.0172 487 ILE A CA  
3893  C C   . ILE A 487 ? 0.9716 0.3273 1.8735 0.0740  -0.2511 -0.0249 487 ILE A C   
3894  O O   . ILE A 487 ? 1.0299 0.3521 1.8903 0.0766  -0.2678 -0.0278 487 ILE A O   
3895  C CB  . ILE A 487 ? 1.0006 0.3453 1.8577 0.0666  -0.1993 -0.0199 487 ILE A CB  
3896  C CG1 . ILE A 487 ? 1.0136 0.3567 1.8558 0.0617  -0.1723 -0.0128 487 ILE A CG1 
3897  C CG2 . ILE A 487 ? 0.9614 0.3378 1.8588 0.0663  -0.1900 -0.0271 487 ILE A CG2 
3898  C CD1 . ILE A 487 ? 1.0303 0.3668 1.8475 0.0586  -0.1456 -0.0161 487 ILE A CD1 
3899  N N   . PRO A 488 ? 0.9093 0.3019 1.8692 0.0743  -0.2562 -0.0285 488 PRO A N   
3900  C CA  . PRO A 488 ? 0.9014 0.2976 1.8786 0.0767  -0.2782 -0.0367 488 PRO A CA  
3901  C C   . PRO A 488 ? 0.9149 0.2980 1.8678 0.0757  -0.2713 -0.0438 488 PRO A C   
3902  O O   . PRO A 488 ? 0.9027 0.2959 1.8567 0.0729  -0.2463 -0.0440 488 PRO A O   
3903  C CB  . PRO A 488 ? 0.8422 0.2830 1.8866 0.0754  -0.2766 -0.0379 488 PRO A CB  
3904  C CG  . PRO A 488 ? 0.8214 0.2776 1.8805 0.0739  -0.2609 -0.0297 488 PRO A CG  
3905  C CD  . PRO A 488 ? 0.8518 0.2828 1.8616 0.0719  -0.2416 -0.0247 488 PRO A CD  
3906  N N   . ASP A 489 ? 0.9442 0.3062 1.8785 0.0781  -0.2944 -0.0504 489 ASP A N   
3907  C CA  . ASP A 489 ? 0.9620 0.3103 1.8743 0.0775  -0.2906 -0.0584 489 ASP A CA  
3908  C C   . ASP A 489 ? 0.9144 0.2976 1.8756 0.0750  -0.2786 -0.0630 489 ASP A C   
3909  O O   . ASP A 489 ? 0.9229 0.3010 1.8702 0.0741  -0.2634 -0.0675 489 ASP A O   
3910  C CB  . ASP A 489 ? 1.0000 0.3223 1.8905 0.0803  -0.3211 -0.0652 489 ASP A CB  
3911  C CG  . ASP A 489 ? 1.0622 0.3396 1.8893 0.0830  -0.3337 -0.0625 489 ASP A CG  
3912  O OD1 . ASP A 489 ? 1.0796 0.3426 1.8735 0.0819  -0.3148 -0.0556 489 ASP A OD1 
3913  O OD2 . ASP A 489 ? 1.0967 0.3536 1.9083 0.0858  -0.3624 -0.0672 489 ASP A OD2 
3914  N N   . ASN A 490 ? 0.8690 0.2857 1.8858 0.0742  -0.2857 -0.0620 490 ASN A N   
3915  C CA  . ASN A 490 ? 0.8294 0.2768 1.8927 0.0715  -0.2790 -0.0663 490 ASN A CA  
3916  C C   . ASN A 490 ? 0.7818 0.2612 1.8781 0.0691  -0.2542 -0.0602 490 ASN A C   
3917  O O   . ASN A 490 ? 0.7359 0.2447 1.8773 0.0668  -0.2500 -0.0616 490 ASN A O   
3918  C CB  . ASN A 490 ? 0.8199 0.2812 1.9214 0.0713  -0.3042 -0.0708 490 ASN A CB  
3919  C CG  . ASN A 490 ? 0.7954 0.2827 1.9368 0.0714  -0.3080 -0.0652 490 ASN A CG  
3920  O OD1 . ASN A 490 ? 0.8121 0.2872 1.9369 0.0743  -0.3163 -0.0604 490 ASN A OD1 
3921  N ND2 . ASN A 490 ? 0.7561 0.2783 1.9495 0.0681  -0.3015 -0.0660 490 ASN A ND2 
3922  N N   . CYS A 491 ? 0.7953 0.2666 1.8670 0.0693  -0.2387 -0.0534 491 CYS A N   
3923  C CA  . CYS A 491 ? 0.7635 0.2595 1.8565 0.0670  -0.2134 -0.0480 491 CYS A CA  
3924  C C   . CYS A 491 ? 0.7699 0.2634 1.8489 0.0663  -0.1921 -0.0512 491 CYS A C   
3925  O O   . CYS A 491 ? 0.8079 0.2731 1.8408 0.0673  -0.1859 -0.0526 491 CYS A O   
3926  C CB  . CYS A 491 ? 0.7802 0.2662 1.8511 0.0668  -0.2059 -0.0400 491 CYS A CB  
3927  S SG  . CYS A 491 ? 0.7543 0.2638 1.8400 0.0633  -0.1728 -0.0343 491 CYS A SG  
3928  N N   . TRP A 492 ? 0.7353 0.2577 1.8537 0.0648  -0.1813 -0.0525 492 TRP A N   
3929  C CA  . TRP A 492 ? 0.7418 0.2643 1.8536 0.0652  -0.1633 -0.0565 492 TRP A CA  
3930  C C   . TRP A 492 ? 0.7276 0.2645 1.8434 0.0640  -0.1377 -0.0512 492 TRP A C   
3931  O O   . TRP A 492 ? 0.7386 0.2643 1.8298 0.0650  -0.1211 -0.0534 492 TRP A O   
3932  C CB  . TRP A 492 ? 0.7132 0.2553 1.8628 0.0646  -0.1673 -0.0611 492 TRP A CB  
3933  C CG  . TRP A 492 ? 0.7235 0.2564 1.8777 0.0644  -0.1928 -0.0662 492 TRP A CG  
3934  C CD1 . TRP A 492 ? 0.6956 0.2500 1.8920 0.0620  -0.2050 -0.0668 492 TRP A CD1 
3935  C CD2 . TRP A 492 ? 0.7689 0.2686 1.8842 0.0663  -0.2091 -0.0721 492 TRP A CD2 
3936  N NE1 . TRP A 492 ? 0.7150 0.2536 1.9046 0.0622  -0.2280 -0.0728 492 TRP A NE1 
3937  C CE2 . TRP A 492 ? 0.7584 0.2631 1.8981 0.0650  -0.2319 -0.0761 492 TRP A CE2 
3938  C CE3 . TRP A 492 ? 0.8161 0.2819 1.8780 0.0687  -0.2065 -0.0747 492 TRP A CE3 
3939  C CZ2 . TRP A 492 ? 0.7920 0.2698 1.9057 0.0661  -0.2535 -0.0826 492 TRP A CZ2 
3940  C CZ3 . TRP A 492 ? 0.8559 0.2932 1.8887 0.0700  -0.2276 -0.0809 492 TRP A CZ3 
3941  C CH2 . TRP A 492 ? 0.8420 0.2855 1.9010 0.0688  -0.2516 -0.0848 492 TRP A CH2 
3942  N N   . VAL A 493 ? 0.6998 0.2614 1.8469 0.0618  -0.1346 -0.0448 493 VAL A N   
3943  C CA  . VAL A 493 ? 0.6862 0.2632 1.8406 0.0600  -0.1124 -0.0397 493 VAL A CA  
3944  C C   . VAL A 493 ? 0.6697 0.2523 1.8312 0.0579  -0.1167 -0.0327 493 VAL A C   
3945  O O   . VAL A 493 ? 0.6707 0.2576 1.8490 0.0583  -0.1350 -0.0322 493 VAL A O   
3946  C CB  . VAL A 493 ? 0.6501 0.2583 1.8452 0.0594  -0.1002 -0.0402 493 VAL A CB  
3947  C CG1 . VAL A 493 ? 0.6165 0.2465 1.8524 0.0582  -0.1139 -0.0397 493 VAL A CG1 
3948  C CG2 . VAL A 493 ? 0.6372 0.2628 1.8426 0.0573  -0.0795 -0.0352 493 VAL A CG2 
3949  N N   . VAL A 494 ? 0.6601 0.2432 1.8107 0.0557  -0.0997 -0.0277 494 VAL A N   
3950  C CA  . VAL A 494 ? 0.6459 0.2321 1.8011 0.0536  -0.1024 -0.0211 494 VAL A CA  
3951  C C   . VAL A 494 ? 0.6185 0.2271 1.7930 0.0500  -0.0811 -0.0169 494 VAL A C   
3952  O O   . VAL A 494 ? 0.6226 0.2295 1.7842 0.0488  -0.0622 -0.0177 494 VAL A O   
3953  C CB  . VAL A 494 ? 0.6941 0.2444 1.8014 0.0540  -0.1094 -0.0185 494 VAL A CB  
3954  C CG1 . VAL A 494 ? 0.7274 0.2587 1.7963 0.0522  -0.0893 -0.0185 494 VAL A CG1 
3955  C CG2 . VAL A 494 ? 0.6891 0.2392 1.8011 0.0527  -0.1162 -0.0117 494 VAL A CG2 
3956  N N   . ASN A 495 ? 0.5970 0.2247 1.8007 0.0483  -0.0847 -0.0126 495 ASN A N   
3957  C CA  . ASN A 495 ? 0.5720 0.2200 1.7944 0.0444  -0.0675 -0.0084 495 ASN A CA  
3958  C C   . ASN A 495 ? 0.5922 0.2245 1.7943 0.0418  -0.0675 -0.0025 495 ASN A C   
3959  O O   . ASN A 495 ? 0.5838 0.2245 1.8041 0.0413  -0.0760 0.0007  495 ASN A O   
3960  C CB  . ASN A 495 ? 0.5193 0.2012 1.7891 0.0439  -0.0680 -0.0090 495 ASN A CB  
3961  C CG  . ASN A 495 ? 0.4917 0.1949 1.7817 0.0400  -0.0524 -0.0052 495 ASN A CG  
3962  O OD1 . ASN A 495 ? 0.5230 0.2161 1.7958 0.0370  -0.0452 -0.0013 495 ASN A OD1 
3963  N ND2 . ASN A 495 ? 0.4501 0.1812 1.7753 0.0394  -0.0479 -0.0061 495 ASN A ND2 
3964  N N   . ALA A 496 ? 0.6287 0.2381 1.7928 0.0398  -0.0558 -0.0011 496 ALA A N   
3965  C CA  . ALA A 496 ? 0.6533 0.2456 1.7940 0.0361  -0.0509 0.0051  496 ALA A CA  
3966  C C   . ALA A 496 ? 0.6277 0.2466 1.7988 0.0312  -0.0358 0.0082  496 ALA A C   
3967  O O   . ALA A 496 ? 0.6383 0.2735 1.8209 0.0289  -0.0180 0.0062  496 ALA A O   
3968  C CB  . ALA A 496 ? 0.6933 0.2564 1.7869 0.0343  -0.0390 0.0051  496 ALA A CB  
3969  N N   . SER A 497 ? 0.6154 0.2395 1.8013 0.0301  -0.0436 0.0123  497 SER A N   
3970  C CA  . SER A 497 ? 0.5928 0.2386 1.8035 0.0249  -0.0300 0.0151  497 SER A CA  
3971  C C   . SER A 497 ? 0.6165 0.2456 1.8138 0.0224  -0.0347 0.0210  497 SER A C   
3972  O O   . SER A 497 ? 0.6389 0.2460 1.8180 0.0261  -0.0522 0.0226  497 SER A O   
3973  C CB  . SER A 497 ? 0.5472 0.2276 1.8045 0.0262  -0.0329 0.0125  497 SER A CB  
3974  O OG  . SER A 497 ? 0.5411 0.2231 1.8130 0.0292  -0.0512 0.0131  497 SER A OG  
3975  N N   . ALA A 498 ? 0.6057 0.2452 1.8128 0.0161  -0.0195 0.0240  498 ALA A N   
3976  C CA  . ALA A 498 ? 0.6224 0.2499 1.8229 0.0129  -0.0220 0.0294  498 ALA A CA  
3977  C C   . ALA A 498 ? 0.6007 0.2565 1.8347 0.0073  -0.0091 0.0297  498 ALA A C   
3978  O O   . ALA A 498 ? 0.6171 0.2940 1.8674 0.0045  0.0056  0.0271  498 ALA A O   
3979  C CB  . ALA A 498 ? 0.6708 0.2630 1.8245 0.0089  -0.0148 0.0341  498 ALA A CB  
3980  N N   . GLY A 499 ? 0.6111 0.2662 1.8547 0.0060  -0.0151 0.0327  499 GLY A N   
3981  C CA  . GLY A 499 ? 0.5833 0.2639 1.8579 0.0007  -0.0048 0.0326  499 GLY A CA  
3982  C C   . GLY A 499 ? 0.5881 0.2569 1.8612 -0.0012 -0.0109 0.0365  499 GLY A C   
3983  O O   . GLY A 499 ? 0.5851 0.2317 1.8420 0.0038  -0.0268 0.0385  499 GLY A O   
3984  N N   . ILE A 500 ? 0.5856 0.2691 1.8762 -0.0082 0.0014  0.0372  500 ILE A N   
3985  C CA  . ILE A 500 ? 0.5918 0.2658 1.8834 -0.0111 -0.0018 0.0403  500 ILE A CA  
3986  C C   . ILE A 500 ? 0.5606 0.2656 1.8889 -0.0157 0.0059  0.0375  500 ILE A C   
3987  O O   . ILE A 500 ? 0.5522 0.2802 1.8970 -0.0191 0.0179  0.0348  500 ILE A O   
3988  C CB  . ILE A 500 ? 0.6191 0.2609 1.8734 -0.0177 0.0069  0.0463  500 ILE A CB  
3989  C CG1 . ILE A 500 ? 0.6337 0.2579 1.8836 -0.0182 -0.0017 0.0499  500 ILE A CG1 
3990  C CG2 . ILE A 500 ? 0.6115 0.2651 1.8689 -0.0275 0.0296  0.0462  500 ILE A CG2 
3991  C CD1 . ILE A 500 ? 0.6849 0.2712 1.8936 -0.0240 0.0039  0.0568  500 ILE A CD1 
3992  N N   . SER A 501 ? 0.5570 0.2622 1.8983 -0.0148 -0.0024 0.0376  501 SER A N   
3993  C CA  . SER A 501 ? 0.5315 0.2638 1.9057 -0.0185 0.0025  0.0344  501 SER A CA  
3994  C C   . SER A 501 ? 0.5285 0.2559 1.8965 -0.0290 0.0174  0.0370  501 SER A C   
3995  O O   . SER A 501 ? 0.5582 0.2568 1.8965 -0.0323 0.0202  0.0418  501 SER A O   
3996  C CB  . SER A 501 ? 0.5428 0.2758 1.9320 -0.0135 -0.0111 0.0327  501 SER A CB  
3997  O OG  . SER A 501 ? 0.5548 0.2891 1.9486 -0.0042 -0.0255 0.0305  501 SER A OG  
3998  N N   . VAL A 502 ? 0.4959 0.2504 1.8911 -0.0343 0.0264  0.0338  502 VAL A N   
3999  C CA  . VAL A 502 ? 0.5052 0.2591 1.8996 -0.0451 0.0406  0.0352  502 VAL A CA  
4000  C C   . VAL A 502 ? 0.4793 0.2562 1.9044 -0.0485 0.0407  0.0313  502 VAL A C   
4001  O O   . VAL A 502 ? 0.4460 0.2487 1.8955 -0.0445 0.0369  0.0271  502 VAL A O   
4002  C CB  . VAL A 502 ? 0.5180 0.2814 1.9100 -0.0501 0.0563  0.0349  502 VAL A CB  
4003  C CG1 . VAL A 502 ? 0.5415 0.3040 1.9339 -0.0623 0.0717  0.0361  502 VAL A CG1 
4004  C CG2 . VAL A 502 ? 0.5485 0.2890 1.9086 -0.0464 0.0565  0.0378  502 VAL A CG2 
4005  N N   . ARG A 503 ? 0.4934 0.2589 1.9147 -0.0563 0.0453  0.0330  503 ARG A N   
4006  C CA  . ARG A 503 ? 0.4775 0.2590 1.9230 -0.0603 0.0449  0.0293  503 ARG A CA  
4007  C C   . ARG A 503 ? 0.4499 0.2399 1.9026 -0.0726 0.0599  0.0289  503 ARG A C   
4008  O O   . ARG A 503 ? 0.4643 0.2348 1.8968 -0.0796 0.0694  0.0330  503 ARG A O   
4009  C CB  . ARG A 503 ? 0.5271 0.2870 1.9649 -0.0584 0.0351  0.0303  503 ARG A CB  
4010  C CG  . ARG A 503 ? 0.5512 0.3273 2.0135 -0.0612 0.0333  0.0253  503 ARG A CG  
4011  C CD  . ARG A 503 ? 0.6188 0.3739 2.0756 -0.0593 0.0247  0.0252  503 ARG A CD  
4012  N NE  . ARG A 503 ? 0.7215 0.4720 2.1798 -0.0474 0.0105  0.0238  503 ARG A NE  
4013  C CZ  . ARG A 503 ? 0.7888 0.5626 2.2681 -0.0405 0.0045  0.0189  503 ARG A CZ  
4014  N NH1 . ARG A 503 ? 0.7479 0.5505 2.2486 -0.0440 0.0101  0.0147  503 ARG A NH1 
4015  N NH2 . ARG A 503 ? 0.8123 0.5798 2.2913 -0.0303 -0.0076 0.0181  503 ARG A NH2 
4016  N N   . TYR A 504 ? 0.3957 0.2151 1.8775 -0.0753 0.0616  0.0238  504 TYR A N   
4017  C CA  . TYR A 504 ? 0.3777 0.2084 1.8736 -0.0866 0.0719  0.0218  504 TYR A CA  
4018  C C   . TYR A 504 ? 0.3521 0.1985 1.8701 -0.0862 0.0640  0.0167  504 TYR A C   
4019  O O   . TYR A 504 ? 0.3141 0.1851 1.8514 -0.0816 0.0596  0.0128  504 TYR A O   
4020  C CB  . TYR A 504 ? 0.3630 0.2167 1.8729 -0.0909 0.0837  0.0200  504 TYR A CB  
4021  C CG  . TYR A 504 ? 0.3621 0.2264 1.8872 -0.1038 0.0948  0.0178  504 TYR A CG  
4022  C CD1 . TYR A 504 ? 0.3363 0.2227 1.8876 -0.1069 0.0909  0.0126  504 TYR A CD1 
4023  C CD2 . TYR A 504 ? 0.3828 0.2344 1.8954 -0.1133 0.1092  0.0207  504 TYR A CD2 
4024  C CE1 . TYR A 504 ? 0.3396 0.2362 1.9062 -0.1188 0.0996  0.0100  504 TYR A CE1 
4025  C CE2 . TYR A 504 ? 0.3852 0.2476 1.9142 -0.1258 0.1196  0.0183  504 TYR A CE2 
4026  C CZ  . TYR A 504 ? 0.3653 0.2507 1.9224 -0.1285 0.1141  0.0128  504 TYR A CZ  
4027  O OH  . TYR A 504 ? 0.3782 0.2744 1.9530 -0.1412 0.1226  0.0098  504 TYR A OH  
4028  N N   . GLY A 505 ? 0.3713 0.2012 1.8841 -0.0912 0.0623  0.0168  505 GLY A N   
4029  C CA  . GLY A 505 ? 0.3625 0.2023 1.8919 -0.0909 0.0551  0.0117  505 GLY A CA  
4030  C C   . GLY A 505 ? 0.3554 0.1996 1.8881 -0.0787 0.0431  0.0098  505 GLY A C   
4031  O O   . GLY A 505 ? 0.3769 0.2013 1.8936 -0.0714 0.0366  0.0128  505 GLY A O   
4032  N N   . LYS A 506 ? 0.3325 0.2030 1.8862 -0.0765 0.0400  0.0049  506 LYS A N   
4033  C CA  . LYS A 506 ? 0.3139 0.1913 1.8728 -0.0663 0.0306  0.0028  506 LYS A CA  
4034  C C   . LYS A 506 ? 0.2959 0.1821 1.8535 -0.0599 0.0302  0.0051  506 LYS A C   
4035  O O   . LYS A 506 ? 0.2984 0.1914 1.8612 -0.0521 0.0231  0.0036  506 LYS A O   
4036  C CB  . LYS A 506 ? 0.3023 0.2014 1.8806 -0.0668 0.0277  -0.0032 506 LYS A CB  
4037  C CG  . LYS A 506 ? 0.3258 0.2151 1.9051 -0.0711 0.0260  -0.0070 506 LYS A CG  
4038  C CD  . LYS A 506 ? 0.3231 0.2310 1.9177 -0.0710 0.0226  -0.0133 506 LYS A CD  
4039  C CE  . LYS A 506 ? 0.3493 0.2479 1.9444 -0.0765 0.0221  -0.0178 506 LYS A CE  
4040  N NZ  . LYS A 506 ? 0.3537 0.2719 1.9620 -0.0823 0.0226  -0.0230 506 LYS A NZ  
4041  N N   . PHE A 507 ? 0.3022 0.1883 1.8534 -0.0631 0.0380  0.0083  507 PHE A N   
4042  C CA  . PHE A 507 ? 0.2938 0.1924 1.8475 -0.0575 0.0383  0.0091  507 PHE A CA  
4043  C C   . PHE A 507 ? 0.3170 0.1926 1.8474 -0.0530 0.0372  0.0136  507 PHE A C   
4044  O O   . PHE A 507 ? 0.3313 0.1891 1.8449 -0.0582 0.0439  0.0171  507 PHE A O   
4045  C CB  . PHE A 507 ? 0.2871 0.2059 1.8541 -0.0635 0.0477  0.0078  507 PHE A CB  
4046  C CG  . PHE A 507 ? 0.2772 0.2080 1.8470 -0.0582 0.0496  0.0084  507 PHE A CG  
4047  C CD1 . PHE A 507 ? 0.2925 0.2095 1.8449 -0.0570 0.0552  0.0117  507 PHE A CD1 
4048  C CD2 . PHE A 507 ? 0.2576 0.2122 1.8463 -0.0549 0.0462  0.0054  507 PHE A CD2 
4049  C CE1 . PHE A 507 ? 0.2875 0.2146 1.8423 -0.0519 0.0571  0.0114  507 PHE A CE1 
4050  C CE2 . PHE A 507 ? 0.2544 0.2186 1.8459 -0.0498 0.0478  0.0057  507 PHE A CE2 
4051  C CZ  . PHE A 507 ? 0.2706 0.2214 1.8458 -0.0482 0.0534  0.0084  507 PHE A CZ  
4052  N N   . THR A 508 ? 0.3160 0.1915 1.8447 -0.0439 0.0286  0.0136  508 THR A N   
4053  C CA  . THR A 508 ? 0.3501 0.2037 1.8564 -0.0388 0.0251  0.0173  508 THR A CA  
4054  C C   . THR A 508 ? 0.3410 0.2067 1.8503 -0.0337 0.0249  0.0168  508 THR A C   
4055  O O   . THR A 508 ? 0.3294 0.2162 1.8576 -0.0310 0.0223  0.0138  508 THR A O   
4056  C CB  . THR A 508 ? 0.3696 0.2062 1.8692 -0.0323 0.0127  0.0175  508 THR A CB  
4057  O OG1 . THR A 508 ? 0.3669 0.2230 1.8876 -0.0277 0.0064  0.0132  508 THR A OG1 
4058  C CG2 . THR A 508 ? 0.3882 0.2070 1.8809 -0.0363 0.0121  0.0184  508 THR A CG2 
4059  N N   . PHE A 509 ? 0.3637 0.2135 1.8521 -0.0323 0.0276  0.0199  509 PHE A N   
4060  C CA  . PHE A 509 ? 0.3543 0.2120 1.8423 -0.0277 0.0284  0.0192  509 PHE A CA  
4061  C C   . PHE A 509 ? 0.3791 0.2099 1.8370 -0.0255 0.0278  0.0226  509 PHE A C   
4062  O O   . PHE A 509 ? 0.4228 0.2329 1.8611 -0.0302 0.0321  0.0259  509 PHE A O   
4063  C CB  . PHE A 509 ? 0.3522 0.2306 1.8543 -0.0328 0.0407  0.0175  509 PHE A CB  
4064  C CG  . PHE A 509 ? 0.3782 0.2469 1.8677 -0.0407 0.0541  0.0195  509 PHE A CG  
4065  C CD1 . PHE A 509 ? 0.3952 0.2595 1.8860 -0.0488 0.0588  0.0203  509 PHE A CD1 
4066  C CD2 . PHE A 509 ? 0.3981 0.2621 1.8748 -0.0405 0.0631  0.0201  509 PHE A CD2 
4067  C CE1 . PHE A 509 ? 0.4210 0.2764 1.9010 -0.0572 0.0723  0.0222  509 PHE A CE1 
4068  C CE2 . PHE A 509 ? 0.4160 0.2718 1.8819 -0.0485 0.0773  0.0216  509 PHE A CE2 
4069  C CZ  . PHE A 509 ? 0.4285 0.2800 1.8961 -0.0572 0.0820  0.0229  509 PHE A CZ  
4070  N N   . LYS A 510 ? 0.3724 0.2023 1.8248 -0.0191 0.0230  0.0219  510 LYS A N   
4071  C CA  . LYS A 510 ? 0.4047 0.2082 1.8263 -0.0166 0.0214  0.0246  510 LYS A CA  
4072  C C   . LYS A 510 ? 0.4036 0.2089 1.8161 -0.0197 0.0356  0.0244  510 LYS A C   
4073  O O   . LYS A 510 ? 0.3844 0.2139 1.8181 -0.0204 0.0425  0.0213  510 LYS A O   
4074  C CB  . LYS A 510 ? 0.4192 0.2200 1.8414 -0.0078 0.0062  0.0231  510 LYS A CB  
4075  C CG  . LYS A 510 ? 0.4114 0.2143 1.8479 -0.0047 -0.0064 0.0221  510 LYS A CG  
4076  C CD  . LYS A 510 ? 0.4124 0.2119 1.8510 0.0033  -0.0215 0.0203  510 LYS A CD  
4077  C CE  . LYS A 510 ? 0.4440 0.2148 1.8521 0.0071  -0.0294 0.0227  510 LYS A CE  
4078  N NZ  . LYS A 510 ? 0.4694 0.2142 1.8549 0.0052  -0.0310 0.0268  510 LYS A NZ  
4079  N N   . ILE A 511 ? 0.4311 0.2097 1.8115 -0.0216 0.0401  0.0276  511 ILE A N   
4080  C CA  . ILE A 511 ? 0.4469 0.2218 1.8127 -0.0236 0.0536  0.0270  511 ILE A CA  
4081  C C   . ILE A 511 ? 0.4675 0.2176 1.8031 -0.0172 0.0451  0.0279  511 ILE A C   
4082  O O   . ILE A 511 ? 0.4950 0.2221 1.8117 -0.0148 0.0329  0.0309  511 ILE A O   
4083  C CB  . ILE A 511 ? 0.4651 0.2302 1.8179 -0.0335 0.0703  0.0296  511 ILE A CB  
4084  C CG1 . ILE A 511 ? 0.5029 0.2328 1.8228 -0.0364 0.0662  0.0354  511 ILE A CG1 
4085  C CG2 . ILE A 511 ? 0.4360 0.2294 1.8225 -0.0398 0.0782  0.0275  511 ILE A CG2 
4086  C CD1 . ILE A 511 ? 0.5298 0.2441 1.8302 -0.0470 0.0836  0.0388  511 ILE A CD1 
4087  N N   . HIS A 512 ? 0.4603 0.2148 1.7922 -0.0143 0.0509  0.0248  512 HIS A N   
4088  C CA  . HIS A 512 ? 0.4600 0.1971 1.7707 -0.0071 0.0401  0.0239  512 HIS A CA  
4089  C C   . HIS A 512 ? 0.4665 0.2030 1.7659 -0.0062 0.0520  0.0206  512 HIS A C   
4090  O O   . HIS A 512 ? 0.4480 0.2034 1.7636 -0.0098 0.0676  0.0183  512 HIS A O   
4091  C CB  . HIS A 512 ? 0.4232 0.1774 1.7598 -0.0005 0.0244  0.0212  512 HIS A CB  
4092  C CG  . HIS A 512 ? 0.3811 0.1689 1.7546 -0.0017 0.0306  0.0182  512 HIS A CG  
4093  N ND1 . HIS A 512 ? 0.3683 0.1709 1.7516 -0.0001 0.0394  0.0147  512 HIS A ND1 
4094  C CD2 . HIS A 512 ? 0.3516 0.1594 1.7525 -0.0040 0.0291  0.0183  512 HIS A CD2 
4095  C CE1 . HIS A 512 ? 0.3372 0.1677 1.7531 -0.0012 0.0416  0.0130  512 HIS A CE1 
4096  N NE2 . HIS A 512 ? 0.3239 0.1578 1.7500 -0.0039 0.0358  0.0151  512 HIS A NE2 
4097  N N   . ASP A 513 ? 0.4944 0.2084 1.7661 -0.0009 0.0438  0.0199  513 ASP A N   
4098  C CA  . ASP A 513 ? 0.5114 0.2235 1.7724 0.0021  0.0514  0.0156  513 ASP A CA  
4099  C C   . ASP A 513 ? 0.5137 0.2160 1.7669 0.0101  0.0332  0.0133  513 ASP A C   
4100  O O   . ASP A 513 ? 0.5100 0.2019 1.7593 0.0123  0.0164  0.0156  513 ASP A O   
4101  C CB  . ASP A 513 ? 0.5508 0.2401 1.7765 -0.0031 0.0680  0.0169  513 ASP A CB  
4102  C CG  . ASP A 513 ? 0.5582 0.2509 1.7783 -0.0015 0.0826  0.0114  513 ASP A CG  
4103  O OD1 . ASP A 513 ? 0.5271 0.2443 1.7764 0.0033  0.0817  0.0066  513 ASP A OD1 
4104  O OD2 . ASP A 513 ? 0.5947 0.2638 1.7799 -0.0047 0.0946  0.0119  513 ASP A OD2 
4105  N N   . GLN A 514 ? 0.5209 0.2265 1.7728 0.0141  0.0373  0.0082  514 GLN A N   
4106  C CA  . GLN A 514 ? 0.5253 0.2265 1.7759 0.0211  0.0221  0.0046  514 GLN A CA  
4107  C C   . GLN A 514 ? 0.5585 0.2457 1.7849 0.0238  0.0303  0.0000  514 GLN A C   
4108  O O   . GLN A 514 ? 0.5661 0.2685 1.8048 0.0233  0.0461  -0.0033 514 GLN A O   
4109  C CB  . GLN A 514 ? 0.4863 0.2203 1.7804 0.0234  0.0189  0.0022  514 GLN A CB  
4110  C CG  . GLN A 514 ? 0.4839 0.2181 1.7851 0.0294  0.0026  -0.0010 514 GLN A CG  
4111  C CD  . GLN A 514 ? 0.4525 0.2171 1.7933 0.0308  0.0026  -0.0029 514 GLN A CD  
4112  O OE1 . GLN A 514 ? 0.4336 0.2113 1.7971 0.0307  -0.0076 -0.0015 514 GLN A OE1 
4113  N NE2 . GLN A 514 ? 0.4565 0.2325 1.8056 0.0320  0.0150  -0.0060 514 GLN A NE2 
4114  N N   . LYS A 515 ? 0.5909 0.2501 1.7847 0.0273  0.0188  -0.0012 515 LYS A N   
4115  C CA  . LYS A 515 ? 0.6129 0.2601 1.7868 0.0309  0.0238  -0.0070 515 LYS A CA  
4116  C C   . LYS A 515 ? 0.6190 0.2614 1.7957 0.0369  0.0030  -0.0103 515 LYS A C   
4117  O O   . LYS A 515 ? 0.6388 0.2659 1.8036 0.0378  -0.0150 -0.0079 515 LYS A O   
4118  C CB  . LYS A 515 ? 0.6638 0.2762 1.7871 0.0290  0.0315  -0.0067 515 LYS A CB  
4119  C CG  . LYS A 515 ? 0.6825 0.2922 1.7953 0.0216  0.0510  -0.0026 515 LYS A CG  
4120  C CD  . LYS A 515 ? 0.6588 0.2983 1.8024 0.0192  0.0727  -0.0055 515 LYS A CD  
4121  C CE  . LYS A 515 ? 0.6706 0.3087 1.8066 0.0108  0.0920  -0.0018 515 LYS A CE  
4122  N NZ  . LYS A 515 ? 0.6461 0.3161 1.8173 0.0098  0.1100  -0.0061 515 LYS A NZ  
4123  N N   . ILE A 516 ? 0.6013 0.2572 1.7954 0.0407  0.0054  -0.0159 516 ILE A N   
4124  C CA  . ILE A 516 ? 0.5911 0.2419 1.7877 0.0456  -0.0119 -0.0199 516 ILE A CA  
4125  C C   . ILE A 516 ? 0.6339 0.2568 1.7917 0.0484  -0.0095 -0.0252 516 ILE A C   
4126  O O   . ILE A 516 ? 0.6424 0.2689 1.7983 0.0495  0.0071  -0.0293 516 ILE A O   
4127  C CB  . ILE A 516 ? 0.5448 0.2256 1.7836 0.0477  -0.0110 -0.0224 516 ILE A CB  
4128  C CG1 . ILE A 516 ? 0.5026 0.2077 1.7760 0.0450  -0.0163 -0.0175 516 ILE A CG1 
4129  C CG2 . ILE A 516 ? 0.5533 0.2261 1.7910 0.0522  -0.0245 -0.0277 516 ILE A CG2 
4130  C CD1 . ILE A 516 ? 0.4644 0.1965 1.7763 0.0466  -0.0167 -0.0191 516 ILE A CD1 
4131  N N   . ILE A 517 ? 0.6657 0.2609 1.7932 0.0498  -0.0263 -0.0257 517 ILE A N   
4132  C CA  . ILE A 517 ? 0.7169 0.2815 1.8011 0.0519  -0.0243 -0.0306 517 ILE A CA  
4133  C C   . ILE A 517 ? 0.7397 0.2933 1.8207 0.0562  -0.0452 -0.0359 517 ILE A C   
4134  O O   . ILE A 517 ? 0.7338 0.2925 1.8318 0.0565  -0.0646 -0.0339 517 ILE A O   
4135  C CB  . ILE A 517 ? 0.7552 0.2899 1.7950 0.0487  -0.0223 -0.0262 517 ILE A CB  
4136  C CG1 . ILE A 517 ? 0.7547 0.3022 1.8018 0.0433  -0.0008 -0.0212 517 ILE A CG1 
4137  C CG2 . ILE A 517 ? 0.8053 0.3056 1.7955 0.0505  -0.0194 -0.0314 517 ILE A CG2 
4138  C CD1 . ILE A 517 ? 0.7960 0.3164 1.8048 0.0389  0.0006  -0.0149 517 ILE A CD1 
4139  N N   . TYR A 518 ? 0.7835 0.3225 1.8441 0.0593  -0.0404 -0.0431 518 TYR A N   
4140  C CA  . TYR A 518 ? 0.7996 0.3295 1.8596 0.0630  -0.0576 -0.0494 518 TYR A CA  
4141  C C   . TYR A 518 ? 0.8680 0.3575 1.8751 0.0643  -0.0677 -0.0531 518 TYR A C   
4142  O O   . TYR A 518 ? 0.9342 0.4017 1.9021 0.0628  -0.0573 -0.0516 518 TYR A O   
4143  C CB  . TYR A 518 ? 0.7775 0.3207 1.8563 0.0662  -0.0460 -0.0558 518 TYR A CB  
4144  C CG  . TYR A 518 ? 0.7249 0.3060 1.8550 0.0656  -0.0390 -0.0529 518 TYR A CG  
4145  C CD1 . TYR A 518 ? 0.7007 0.2982 1.8646 0.0659  -0.0539 -0.0527 518 TYR A CD1 
4146  C CD2 . TYR A 518 ? 0.7075 0.3074 1.8518 0.0645  -0.0177 -0.0505 518 TYR A CD2 
4147  C CE1 . TYR A 518 ? 0.6590 0.2883 1.8656 0.0653  -0.0479 -0.0498 518 TYR A CE1 
4148  C CE2 . TYR A 518 ? 0.6645 0.2971 1.8531 0.0643  -0.0129 -0.0480 518 TYR A CE2 
4149  C CZ  . TYR A 518 ? 0.6373 0.2838 1.8556 0.0647  -0.0281 -0.0474 518 TYR A CZ  
4150  O OH  . TYR A 518 ? 0.6012 0.2773 1.8597 0.0644  -0.0242 -0.0447 518 TYR A OH  
4151  N N   . ARG A 519 ? 0.8764 0.3554 1.8818 0.0667  -0.0885 -0.0580 519 ARG A N   
4152  C CA  . ARG A 519 ? 0.9300 0.3709 1.8865 0.0684  -0.1001 -0.0630 519 ARG A CA  
4153  C C   . ARG A 519 ? 0.9488 0.3829 1.8989 0.0716  -0.0935 -0.0725 519 ARG A C   
4154  O O   . ARG A 519 ? 0.9278 0.3801 1.9129 0.0729  -0.0996 -0.0758 519 ARG A O   
4155  C CB  . ARG A 519 ? 0.9312 0.3644 1.8914 0.0687  -0.1303 -0.0624 519 ARG A CB  
4156  C CG  . ARG A 519 ? 0.9934 0.3851 1.9005 0.0704  -0.1455 -0.0670 519 ARG A CG  
4157  C CD  . ARG A 519 ? 0.9957 0.3832 1.9135 0.0714  -0.1768 -0.0689 519 ARG A CD  
4158  N NE  . ARG A 519 ? 0.9927 0.3817 1.9153 0.0706  -0.1901 -0.0613 519 ARG A NE  
4159  C CZ  . ARG A 519 ? 1.0503 0.4095 1.9275 0.0708  -0.1937 -0.0573 519 ARG A CZ  
4160  N NH1 . ARG A 519 ? 1.1045 0.4317 1.9291 0.0711  -0.1839 -0.0602 519 ARG A NH1 
4161  N NH2 . ARG A 519 ? 1.0476 0.4077 1.9309 0.0708  -0.2066 -0.0504 519 ARG A NH2 
4162  N N   . GLY A 520 ? 0.9946 0.4020 1.8996 0.0727  -0.0802 -0.0769 520 GLY A N   
4163  C CA  . GLY A 520 ? 1.0020 0.4025 1.8998 0.0764  -0.0706 -0.0865 520 GLY A CA  
4164  C C   . GLY A 520 ? 0.9498 0.3868 1.8992 0.0779  -0.0574 -0.0870 520 GLY A C   
4165  O O   . GLY A 520 ? 0.9056 0.3703 1.8861 0.0758  -0.0469 -0.0802 520 GLY A O   
4166  N N   . ASP A 521 ? 0.9518 0.3874 1.9097 0.0817  -0.0592 -0.0951 521 ASP A N   
4167  C CA  . ASP A 521 ? 0.9173 0.3806 1.9143 0.0844  -0.0435 -0.0967 521 ASP A CA  
4168  C C   . ASP A 521 ? 0.8661 0.3501 1.9069 0.0843  -0.0594 -0.0958 521 ASP A C   
4169  O O   . ASP A 521 ? 0.8260 0.3278 1.8961 0.0871  -0.0507 -0.0978 521 ASP A O   
4170  C CB  . ASP A 521 ? 0.9501 0.3978 1.9250 0.0894  -0.0272 -0.1064 521 ASP A CB  
4171  C CG  . ASP A 521 ? 0.9967 0.4170 1.9487 0.0921  -0.0425 -0.1156 521 ASP A CG  
4172  O OD1 . ASP A 521 ? 0.9966 0.4117 1.9531 0.0897  -0.0670 -0.1145 521 ASP A OD1 
4173  O OD2 . ASP A 521 ? 1.0416 0.4463 1.9728 0.0966  -0.0296 -0.1245 521 ASP A OD2 
4174  N N   . TRP A 522 ? 0.8562 0.3394 1.9033 0.0808  -0.0817 -0.0921 522 TRP A N   
4175  C CA  . TRP A 522 ? 0.8100 0.3093 1.8950 0.0794  -0.0979 -0.0918 522 TRP A CA  
4176  C C   . TRP A 522 ? 0.7670 0.3023 1.8995 0.0790  -0.0866 -0.0864 522 TRP A C   
4177  O O   . TRP A 522 ? 0.7517 0.2982 1.9128 0.0791  -0.0927 -0.0878 522 TRP A O   
4178  C CB  . TRP A 522 ? 0.7918 0.2876 1.8779 0.0756  -0.1210 -0.0882 522 TRP A CB  
4179  C CG  . TRP A 522 ? 0.7496 0.2705 1.8618 0.0725  -0.1186 -0.0787 522 TRP A CG  
4180  C CD1 . TRP A 522 ? 0.7517 0.2681 1.8444 0.0714  -0.1124 -0.0732 522 TRP A CD1 
4181  C CD2 . TRP A 522 ? 0.6929 0.2464 1.8540 0.0700  -0.1203 -0.0737 522 TRP A CD2 
4182  N NE1 . TRP A 522 ? 0.7056 0.2491 1.8323 0.0687  -0.1111 -0.0657 522 TRP A NE1 
4183  C CE2 . TRP A 522 ? 0.6685 0.2353 1.8367 0.0678  -0.1155 -0.0659 522 TRP A CE2 
4184  C CE3 . TRP A 522 ? 0.6568 0.2275 1.8541 0.0690  -0.1250 -0.0750 522 TRP A CE3 
4185  C CZ2 . TRP A 522 ? 0.6191 0.2160 1.8287 0.0651  -0.1153 -0.0601 522 TRP A CZ2 
4186  C CZ3 . TRP A 522 ? 0.6138 0.2140 1.8509 0.0660  -0.1241 -0.0686 522 TRP A CZ3 
4187  C CH2 . TRP A 522 ? 0.5959 0.2094 1.8390 0.0643  -0.1189 -0.0616 522 TRP A CH2 
4188  N N   . ALA A 523 ? 0.7512 0.3026 1.8900 0.0784  -0.0702 -0.0805 523 ALA A N   
4189  C CA  . ALA A 523 ? 0.6985 0.2835 1.8796 0.0777  -0.0603 -0.0749 523 ALA A CA  
4190  C C   . ALA A 523 ? 0.6929 0.2861 1.8825 0.0824  -0.0411 -0.0786 523 ALA A C   
4191  O O   . ALA A 523 ? 0.6515 0.2716 1.8740 0.0825  -0.0322 -0.0744 523 ALA A O   
4192  C CB  . ALA A 523 ? 0.6822 0.2798 1.8667 0.0740  -0.0546 -0.0671 523 ALA A CB  
4193  N N   . LYS A 524 ? 0.7326 0.3027 1.8938 0.0868  -0.0359 -0.0869 524 LYS A N   
4194  C CA  . LYS A 524 ? 0.7463 0.3211 1.9116 0.0924  -0.0166 -0.0919 524 LYS A CA  
4195  C C   . LYS A 524 ? 0.6942 0.2961 1.9040 0.0946  -0.0147 -0.0896 524 LYS A C   
4196  O O   . LYS A 524 ? 0.6761 0.2954 1.9025 0.0976  0.0017  -0.0891 524 LYS A O   
4197  C CB  . LYS A 524 ? 0.8033 0.3491 1.9385 0.0973  -0.0166 -0.1024 524 LYS A CB  
4198  C CG  . LYS A 524 ? 0.8414 0.3894 1.9772 0.1040  0.0047  -0.1089 524 LYS A CG  
4199  C CD  . LYS A 524 ? 0.8977 0.4187 2.0102 0.1096  0.0031  -0.1200 524 LYS A CD  
4200  C CE  . LYS A 524 ? 0.9514 0.4379 2.0120 0.1081  0.0002  -0.1253 524 LYS A CE  
4201  N NZ  . LYS A 524 ? 0.9853 0.4453 2.0251 0.1129  -0.0047 -0.1361 524 LYS A NZ  
4202  N N   . GLU A 525 ? 0.6822 0.2866 1.9104 0.0928  -0.0316 -0.0882 525 GLU A N   
4203  C CA  . GLU A 525 ? 0.6633 0.2876 1.9284 0.0948  -0.0314 -0.0861 525 GLU A CA  
4204  C C   . GLU A 525 ? 0.6240 0.2759 1.9200 0.0896  -0.0343 -0.0765 525 GLU A C   
4205  O O   . GLU A 525 ? 0.6002 0.2743 1.9215 0.0913  -0.0246 -0.0729 525 GLU A O   
4206  C CB  . GLU A 525 ? 0.6788 0.2888 1.9462 0.0949  -0.0467 -0.0902 525 GLU A CB  
4207  C CG  . GLU A 525 ? 0.7292 0.3107 1.9675 0.1003  -0.0449 -0.1006 525 GLU A CG  
4208  C CD  . GLU A 525 ? 0.7778 0.3297 1.9778 0.0981  -0.0561 -0.1061 525 GLU A CD  
4209  O OE1 . GLU A 525 ? 0.7738 0.3240 1.9707 0.0921  -0.0708 -0.1025 525 GLU A OE1 
4210  O OE2 . GLU A 525 ? 0.8357 0.3647 2.0081 0.1030  -0.0504 -0.1149 525 GLU A OE2 
4211  N N   . VAL A 526 ? 0.6255 0.2754 1.9200 0.0836  -0.0487 -0.0729 526 VAL A N   
4212  C CA  . VAL A 526 ? 0.5968 0.2706 1.9209 0.0786  -0.0536 -0.0649 526 VAL A CA  
4213  C C   . VAL A 526 ? 0.5957 0.2852 1.9224 0.0772  -0.0415 -0.0596 526 VAL A C   
4214  O O   . VAL A 526 ? 0.5851 0.2982 1.9391 0.0749  -0.0391 -0.0537 526 VAL A O   
4215  C CB  . VAL A 526 ? 0.5850 0.2511 1.9076 0.0733  -0.0726 -0.0640 526 VAL A CB  
4216  C CG1 . VAL A 526 ? 0.6084 0.2563 1.8990 0.0722  -0.0774 -0.0653 526 VAL A CG1 
4217  C CG2 . VAL A 526 ? 0.5455 0.2360 1.9006 0.0682  -0.0774 -0.0569 526 VAL A CG2 
4218  N N   . GLY A 527 ? 0.6183 0.2935 1.9153 0.0780  -0.0341 -0.0618 527 GLY A N   
4219  C CA  . GLY A 527 ? 0.6159 0.3030 1.9130 0.0753  -0.0234 -0.0567 527 GLY A CA  
4220  C C   . GLY A 527 ? 0.5897 0.2987 1.9084 0.0779  -0.0061 -0.0558 527 GLY A C   
4221  O O   . GLY A 527 ? 0.6012 0.3073 1.9197 0.0834  0.0021  -0.0612 527 GLY A O   
4222  N N   . ARG A 528 ? 0.5724 0.3028 1.9102 0.0742  -0.0013 -0.0495 528 ARG A N   
4223  C CA  . ARG A 528 ? 0.5662 0.3185 1.9244 0.0755  0.0143  -0.0483 528 ARG A CA  
4224  C C   . ARG A 528 ? 0.6301 0.3726 1.9675 0.0784  0.0314  -0.0537 528 ARG A C   
4225  O O   . ARG A 528 ? 0.6578 0.3811 1.9640 0.0759  0.0335  -0.0543 528 ARG A O   
4226  C CB  . ARG A 528 ? 0.5270 0.2964 1.8983 0.0695  0.0155  -0.0413 528 ARG A CB  
4227  C CG  . ARG A 528 ? 0.4980 0.2925 1.8940 0.0696  0.0293  -0.0397 528 ARG A CG  
4228  C CD  . ARG A 528 ? 0.4728 0.2795 1.8752 0.0630  0.0321  -0.0337 528 ARG A CD  
4229  N NE  . ARG A 528 ? 0.4282 0.2459 1.8491 0.0597  0.0189  -0.0285 528 ARG A NE  
4230  C CZ  . ARG A 528 ? 0.4214 0.2282 1.8309 0.0562  0.0076  -0.0259 528 ARG A CZ  
4231  N NH1 . ARG A 528 ? 0.4472 0.2331 1.8268 0.0550  0.0079  -0.0267 528 ARG A NH1 
4232  N NH2 . ARG A 528 ? 0.3939 0.2106 1.8219 0.0541  -0.0039 -0.0226 528 ARG A NH2 
4233  N N   . LYS A 529 ? 0.6682 0.4237 2.0228 0.0836  0.0437  -0.0574 529 LYS A N   
4234  C CA  . LYS A 529 ? 0.7334 0.4833 2.0735 0.0866  0.0623  -0.0634 529 LYS A CA  
4235  C C   . LYS A 529 ? 0.7556 0.5262 2.1100 0.0827  0.0775  -0.0603 529 LYS A C   
4236  O O   . LYS A 529 ? 0.7308 0.5190 2.1049 0.0779  0.0726  -0.0536 529 LYS A O   
4237  C CB  . LYS A 529 ? 0.7543 0.5054 2.1059 0.0954  0.0666  -0.0704 529 LYS A CB  
4238  C CG  . LYS A 529 ? 0.8030 0.5288 2.1347 0.0991  0.0547  -0.0753 529 LYS A CG  
4239  C CD  . LYS A 529 ? 0.8129 0.5447 2.1670 0.1001  0.0378  -0.0722 529 LYS A CD  
4240  C CE  . LYS A 529 ? 0.8351 0.5415 2.1708 0.1027  0.0258  -0.0772 529 LYS A CE  
4241  N NZ  . LYS A 529 ? 0.8398 0.5277 2.1499 0.0967  0.0134  -0.0756 529 LYS A NZ  
4242  N N   . LEU A 530 ? 0.8252 0.5931 2.1689 0.0842  0.0965  -0.0658 530 LEU A N   
4243  C CA  . LEU A 530 ? 0.8655 0.6541 2.2256 0.0807  0.1136  -0.0646 530 LEU A CA  
4244  C C   . LEU A 530 ? 0.9374 0.7190 2.2791 0.0711  0.1137  -0.0580 530 LEU A C   
4245  O O   . LEU A 530 ? 0.9305 0.7282 2.2848 0.0664  0.1273  -0.0562 530 LEU A O   
4246  C CB  . LEU A 530 ? 0.8466 0.6684 2.2525 0.0826  0.1125  -0.0623 530 LEU A CB  
4247  C CG  . LEU A 530 ? 0.8769 0.7114 2.3070 0.0921  0.1187  -0.0692 530 LEU A CG  
4248  C CD1 . LEU A 530 ? 0.8584 0.7121 2.3215 0.0946  0.1038  -0.0646 530 LEU A CD1 
4249  C CD2 . LEU A 530 ? 0.8481 0.7001 2.2941 0.0932  0.1407  -0.0745 530 LEU A CD2 
4250  N N   . SER B 3   ? 1.0153 2.0586 2.5466 0.8037  0.2781  -0.3366 3   SER B N   
4251  C CA  . SER B 3   ? 1.0491 1.9981 2.5624 0.7873  0.2657  -0.3425 3   SER B CA  
4252  C C   . SER B 3   ? 1.0256 1.9453 2.5484 0.7406  0.2628  -0.3090 3   SER B C   
4253  O O   . SER B 3   ? 1.0259 1.9369 2.5362 0.7115  0.2643  -0.3004 3   SER B O   
4254  C CB  . SER B 3   ? 1.0787 2.0335 2.5645 0.7914  0.2686  -0.3644 3   SER B CB  
4255  O OG  . SER B 3   ? 1.0775 1.9529 2.5476 0.7694  0.2579  -0.3662 3   SER B OG  
4256  N N   . LYS B 4   ? 1.0139 1.9192 2.5586 0.7347  0.2582  -0.2907 4   LYS B N   
4257  C CA  . LYS B 4   ? 0.9696 1.8335 2.5222 0.6950  0.2527  -0.2638 4   LYS B CA  
4258  C C   . LYS B 4   ? 0.9534 1.7202 2.4903 0.6915  0.2391  -0.2747 4   LYS B C   
4259  O O   . LYS B 4   ? 0.9393 1.6640 2.4692 0.7222  0.2313  -0.2978 4   LYS B O   
4260  C CB  . LYS B 4   ? 0.9858 1.8627 2.5648 0.6908  0.2508  -0.2433 4   LYS B CB  
4261  C CG  . LYS B 4   ? 1.0526 1.8877 2.6386 0.7227  0.2406  -0.2540 4   LYS B CG  
4262  C CD  . LYS B 4   ? 1.0656 1.8523 2.6646 0.7034  0.2308  -0.2329 4   LYS B CD  
4263  C CE  . LYS B 4   ? 1.0455 1.8874 2.6669 0.6796  0.2362  -0.2064 4   LYS B CE  
4264  N NZ  . LYS B 4   ? 1.0252 1.8167 2.6530 0.6516  0.2274  -0.1866 4   LYS B NZ  
4265  N N   . THR B 5   ? 0.9039 1.6365 2.4357 0.6541  0.2363  -0.2583 5   THR B N   
4266  C CA  . THR B 5   ? 0.8901 1.5343 2.4100 0.6463  0.2235  -0.2649 5   THR B CA  
4267  C C   . THR B 5   ? 0.8548 1.4521 2.3894 0.6538  0.2138  -0.2579 5   THR B C   
4268  O O   . THR B 5   ? 0.7964 1.4155 2.3494 0.6400  0.2155  -0.2353 5   THR B O   
4269  C CB  . THR B 5   ? 0.9014 1.5278 2.4148 0.6059  0.2233  -0.2476 5   THR B CB  
4270  O OG1 . THR B 5   ? 0.8973 1.5529 2.4296 0.5800  0.2276  -0.2187 5   THR B OG1 
4271  C CG2 . THR B 5   ? 0.9164 1.5818 2.4122 0.6006  0.2313  -0.2553 5   THR B CG2 
4272  N N   . LYS B 6   ? 0.8787 1.4140 2.4051 0.6772  0.2033  -0.2778 6   LYS B N   
4273  C CA  . LYS B 6   ? 0.8815 1.3720 2.4200 0.6906  0.1937  -0.2730 6   LYS B CA  
4274  C C   . LYS B 6   ? 0.8604 1.2769 2.3965 0.6628  0.1834  -0.2598 6   LYS B C   
4275  O O   . LYS B 6   ? 0.8719 1.2379 2.3925 0.6561  0.1772  -0.2724 6   LYS B O   
4276  C CB  . LYS B 6   ? 0.9334 1.3943 2.4660 0.7329  0.1872  -0.3009 6   LYS B CB  
4277  C CG  . LYS B 6   ? 0.9639 1.4896 2.4933 0.7656  0.1963  -0.3225 6   LYS B CG  
4278  C CD  . LYS B 6   ? 0.9564 1.5529 2.5066 0.7797  0.2041  -0.3099 6   LYS B CD  
4279  C CE  . LYS B 6   ? 0.9829 1.6439 2.5320 0.8169  0.2126  -0.3321 6   LYS B CE  
4280  N NZ  . LYS B 6   ? 1.0345 1.6542 2.5682 0.8520  0.2058  -0.3664 6   LYS B NZ  
4281  N N   . ILE B 7   ? 0.8119 1.2245 2.3637 0.6473  0.1812  -0.2351 7   ILE B N   
4282  C CA  . ILE B 7   ? 0.7801 1.1344 2.3314 0.6189  0.1732  -0.2196 7   ILE B CA  
4283  C C   . ILE B 7   ? 0.8067 1.1032 2.3631 0.6355  0.1619  -0.2183 7   ILE B C   
4284  O O   . ILE B 7   ? 0.7850 1.0998 2.3562 0.6448  0.1613  -0.2050 7   ILE B O   
4285  C CB  . ILE B 7   ? 0.7141 1.1031 2.2774 0.5864  0.1784  -0.1930 7   ILE B CB  
4286  C CG1 . ILE B 7   ? 0.6840 1.1268 2.2428 0.5691  0.1891  -0.1919 7   ILE B CG1 
4287  C CG2 . ILE B 7   ? 0.6921 1.0235 2.2550 0.5596  0.1703  -0.1780 7   ILE B CG2 
4288  C CD1 . ILE B 7   ? 0.6397 1.1177 2.2121 0.5385  0.1940  -0.1670 7   ILE B CD1 
4289  N N   . GLU B 8   ? 0.8474 1.0743 2.3920 0.6363  0.1524  -0.2301 8   GLU B N   
4290  C CA  . GLU B 8   ? 0.8757 1.0381 2.4236 0.6488  0.1406  -0.2279 8   GLU B CA  
4291  C C   . GLU B 8   ? 0.8568 0.9696 2.4042 0.6154  0.1342  -0.2094 8   GLU B C   
4292  O O   . GLU B 8   ? 0.8308 0.9222 2.3674 0.5939  0.1334  -0.2145 8   GLU B O   
4293  C CB  . GLU B 8   ? 0.9236 1.0448 2.4605 0.6780  0.1339  -0.2570 8   GLU B CB  
4294  C CG  . GLU B 8   ? 0.9270 1.1032 2.4588 0.7053  0.1421  -0.2806 8   GLU B CG  
4295  C CD  . GLU B 8   ? 0.9736 1.1311 2.5068 0.7487  0.1364  -0.3009 8   GLU B CD  
4296  O OE1 . GLU B 8   ? 0.9773 1.1162 2.5233 0.7596  0.1310  -0.2862 8   GLU B OE1 
4297  O OE2 . GLU B 8   ? 0.9987 1.1626 2.5209 0.7724  0.1373  -0.3302 8   GLU B OE2 
4298  N N   . LEU B 9   ? 0.8593 0.9589 2.4186 0.6125  0.1300  -0.1878 9   LEU B N   
4299  C CA  . LEU B 9   ? 0.8457 0.9036 2.4066 0.5848  0.1241  -0.1679 9   LEU B CA  
4300  C C   . LEU B 9   ? 0.9114 0.8995 2.4719 0.5990  0.1121  -0.1682 9   LEU B C   
4301  O O   . LEU B 9   ? 0.9055 0.8879 2.4755 0.6138  0.1081  -0.1550 9   LEU B O   
4302  C CB  . LEU B 9   ? 0.7951 0.8937 2.3691 0.5706  0.1281  -0.1429 9   LEU B CB  
4303  C CG  . LEU B 9   ? 0.7559 0.9214 2.3335 0.5536  0.1391  -0.1389 9   LEU B CG  
4304  C CD1 . LEU B 9   ? 0.7155 0.9073 2.3057 0.5353  0.1402  -0.1150 9   LEU B CD1 
4305  C CD2 . LEU B 9   ? 0.7558 0.9149 2.3218 0.5297  0.1422  -0.1463 9   LEU B CD2 
4306  N N   . LYS B 10  ? 0.9676 0.9024 2.5172 0.5942  0.1057  -0.1831 10  LYS B N   
4307  C CA  . LYS B 10  ? 1.0241 0.8857 2.5735 0.6003  0.0935  -0.1821 10  LYS B CA  
4308  C C   . LYS B 10  ? 1.0246 0.8429 2.5674 0.5681  0.0888  -0.1794 10  LYS B C   
4309  O O   . LYS B 10  ? 1.0050 0.8393 2.5390 0.5525  0.0930  -0.1911 10  LYS B O   
4310  C CB  . LYS B 10  ? 1.0912 0.9240 2.6358 0.6344  0.0878  -0.2090 10  LYS B CB  
4311  C CG  . LYS B 10  ? 1.1141 0.9955 2.6507 0.6509  0.0959  -0.2355 10  LYS B CG  
4312  C CD  . LYS B 10  ? 1.1747 1.0167 2.7006 0.6741  0.0890  -0.2684 10  LYS B CD  
4313  C CE  . LYS B 10  ? 1.1629 1.0597 2.6830 0.7009  0.0971  -0.2933 10  LYS B CE  
4314  N NZ  . LYS B 10  ? 1.1559 1.0898 2.6877 0.7312  0.1007  -0.2881 10  LYS B NZ  
4315  N N   . ASP B 11  ? 1.0311 0.7968 2.5784 0.5583  0.0800  -0.1628 11  ASP B N   
4316  C CA  . ASP B 11  ? 1.0158 0.7382 2.5588 0.5292  0.0746  -0.1597 11  ASP B CA  
4317  C C   . ASP B 11  ? 0.9469 0.7098 2.4889 0.4980  0.0827  -0.1479 11  ASP B C   
4318  O O   . ASP B 11  ? 0.9247 0.6754 2.4600 0.4766  0.0818  -0.1550 11  ASP B O   
4319  C CB  . ASP B 11  ? 1.0645 0.7498 2.5973 0.5347  0.0686  -0.1889 11  ASP B CB  
4320  C CG  . ASP B 11  ? 1.1456 0.7904 2.6790 0.5679  0.0602  -0.2047 11  ASP B CG  
4321  O OD1 . ASP B 11  ? 1.1958 0.7968 2.7372 0.5717  0.0523  -0.1885 11  ASP B OD1 
4322  O OD2 . ASP B 11  ? 1.2070 0.8671 2.7331 0.5904  0.0620  -0.2321 11  ASP B OD2 
4323  N N   . ASN B 12  ? 0.8895 0.7004 2.4390 0.4958  0.0898  -0.1300 12  ASN B N   
4324  C CA  . ASN B 12  ? 0.8051 0.6513 2.3556 0.4673  0.0966  -0.1171 12  ASN B CA  
4325  C C   . ASN B 12  ? 0.7805 0.6513 2.3217 0.4584  0.1022  -0.1350 12  ASN B C   
4326  O O   . ASN B 12  ? 0.7781 0.6495 2.3163 0.4325  0.1034  -0.1307 12  ASN B O   
4327  C CB  . ASN B 12  ? 0.7909 0.6000 2.3440 0.4432  0.0910  -0.0984 12  ASN B CB  
4328  C CG  . ASN B 12  ? 0.7980 0.5903 2.3595 0.4524  0.0863  -0.0780 12  ASN B CG  
4329  O OD1 . ASN B 12  ? 0.8085 0.6318 2.3757 0.4714  0.0891  -0.0727 12  ASN B OD1 
4330  N ND2 . ASN B 12  ? 0.8048 0.5519 2.3677 0.4384  0.0793  -0.0647 12  ASN B ND2 
4331  N N   . TRP B 13  ? 0.7920 0.6856 2.3285 0.4811  0.1056  -0.1549 13  TRP B N   
4332  C CA  . TRP B 13  ? 0.7775 0.7017 2.3041 0.4770  0.1116  -0.1716 13  TRP B CA  
4333  C C   . TRP B 13  ? 0.7621 0.7458 2.2911 0.4975  0.1206  -0.1777 13  TRP B C   
4334  O O   . TRP B 13  ? 0.7788 0.7642 2.3117 0.5256  0.1194  -0.1839 13  TRP B O   
4335  C CB  . TRP B 13  ? 0.8277 0.7093 2.3424 0.4837  0.1044  -0.1961 13  TRP B CB  
4336  C CG  . TRP B 13  ? 0.8384 0.6845 2.3485 0.4556  0.0989  -0.1938 13  TRP B CG  
4337  C CD1 . TRP B 13  ? 0.8538 0.6491 2.3687 0.4419  0.0904  -0.1823 13  TRP B CD1 
4338  C CD2 . TRP B 13  ? 0.8274 0.6899 2.3276 0.4379  0.1015  -0.2025 13  TRP B CD2 
4339  N NE1 . TRP B 13  ? 0.8413 0.6223 2.3511 0.4169  0.0877  -0.1840 13  TRP B NE1 
4340  C CE2 . TRP B 13  ? 0.8263 0.6467 2.3266 0.4146  0.0940  -0.1966 13  TRP B CE2 
4341  C CE3 . TRP B 13  ? 0.8202 0.7306 2.3116 0.4393  0.1094  -0.2132 13  TRP B CE3 
4342  C CZ2 . TRP B 13  ? 0.8183 0.6435 2.3107 0.3944  0.0938  -0.2022 13  TRP B CZ2 
4343  C CZ3 . TRP B 13  ? 0.8055 0.7187 2.2879 0.4191  0.1091  -0.2175 13  TRP B CZ3 
4344  C CH2 . TRP B 13  ? 0.8065 0.6774 2.2896 0.3977  0.1011  -0.2127 13  TRP B CH2 
4345  N N   . TYR B 14  ? 0.7196 0.7533 2.2471 0.4831  0.1297  -0.1746 14  TYR B N   
4346  C CA  . TYR B 14  ? 0.7069 0.7987 2.2341 0.4999  0.1387  -0.1838 14  TYR B CA  
4347  C C   . TYR B 14  ? 0.7489 0.8269 2.2620 0.5190  0.1366  -0.2119 14  TYR B C   
4348  O O   . TYR B 14  ? 0.7570 0.8011 2.2591 0.5069  0.1316  -0.2214 14  TYR B O   
4349  C CB  . TYR B 14  ? 0.6581 0.8038 2.1862 0.4787  0.1484  -0.1741 14  TYR B CB  
4350  C CG  . TYR B 14  ? 0.6128 0.7879 2.1556 0.4622  0.1522  -0.1501 14  TYR B CG  
4351  C CD1 . TYR B 14  ? 0.5942 0.7380 2.1419 0.4413  0.1471  -0.1337 14  TYR B CD1 
4352  C CD2 . TYR B 14  ? 0.5866 0.8240 2.1382 0.4656  0.1610  -0.1444 14  TYR B CD2 
4353  C CE1 . TYR B 14  ? 0.5557 0.7269 2.1159 0.4269  0.1499  -0.1146 14  TYR B CE1 
4354  C CE2 . TYR B 14  ? 0.5494 0.8133 2.1149 0.4495  0.1635  -0.1247 14  TYR B CE2 
4355  C CZ  . TYR B 14  ? 0.5351 0.7649 2.1044 0.4309  0.1576  -0.1107 14  TYR B CZ  
4356  O OH  . TYR B 14  ? 0.5030 0.7586 2.0850 0.4157  0.1593  -0.0938 14  TYR B OH  
4357  N N   . HIS B 15  ? 0.7732 0.8791 2.2869 0.5495  0.1400  -0.2257 15  HIS B N   
4358  C CA  . HIS B 15  ? 0.8167 0.9218 2.3167 0.5708  0.1394  -0.2546 15  HIS B CA  
4359  C C   . HIS B 15  ? 0.7955 0.9766 2.2952 0.5842  0.1517  -0.2600 15  HIS B C   
4360  O O   . HIS B 15  ? 0.8085 1.0209 2.3194 0.6044  0.1554  -0.2565 15  HIS B O   
4361  C CB  . HIS B 15  ? 0.8836 0.9454 2.3846 0.6026  0.1307  -0.2707 15  HIS B CB  
4362  C CG  . HIS B 15  ? 0.9253 0.9083 2.4264 0.5948  0.1177  -0.2687 15  HIS B CG  
4363  N ND1 . HIS B 15  ? 0.9233 0.8776 2.4366 0.5842  0.1130  -0.2444 15  HIS B ND1 
4364  C CD2 . HIS B 15  ? 0.9712 0.8999 2.4620 0.5971  0.1081  -0.2888 15  HIS B CD2 
4365  C CE1 . HIS B 15  ? 0.9561 0.8416 2.4669 0.5794  0.1015  -0.2480 15  HIS B CE1 
4366  N NE2 . HIS B 15  ? 0.9898 0.8575 2.4877 0.5866  0.0980  -0.2752 15  HIS B NE2 
4367  N N   . LEU B 16  ? 0.7690 0.9814 2.2564 0.5733  0.1577  -0.2676 16  LEU B N   
4368  C CA  . LEU B 16  ? 0.7545 1.0388 2.2392 0.5874  0.1692  -0.2752 16  LEU B CA  
4369  C C   . LEU B 16  ? 0.7923 1.0715 2.2628 0.6195  0.1670  -0.3086 16  LEU B C   
4370  O O   . LEU B 16  ? 0.8055 1.0599 2.2595 0.6149  0.1625  -0.3256 16  LEU B O   
4371  C CB  . LEU B 16  ? 0.7187 1.0448 2.1979 0.5596  0.1775  -0.2631 16  LEU B CB  
4372  C CG  . LEU B 16  ? 0.6736 1.0382 2.1693 0.5369  0.1845  -0.2332 16  LEU B CG  
4373  C CD1 . LEU B 16  ? 0.6584 0.9781 2.1672 0.5230  0.1770  -0.2152 16  LEU B CD1 
4374  C CD2 . LEU B 16  ? 0.6463 1.0377 2.1350 0.5089  0.1903  -0.2222 16  LEU B CD2 
4375  N N   . ASP B 17  ? 0.8017 1.1066 2.2791 0.6523  0.1697  -0.3185 17  ASP B N   
4376  C CA  . ASP B 17  ? 0.8427 1.1557 2.3082 0.6872  0.1694  -0.3514 17  ASP B CA  
4377  C C   . ASP B 17  ? 0.8870 1.1167 2.3426 0.6955  0.1546  -0.3729 17  ASP B C   
4378  O O   . ASP B 17  ? 0.9094 1.1289 2.3473 0.6994  0.1518  -0.3974 17  ASP B O   
4379  C CB  . ASP B 17  ? 0.8333 1.2109 2.2846 0.6851  0.1802  -0.3611 17  ASP B CB  
4380  C CG  . ASP B 17  ? 0.7916 1.2520 2.2539 0.6747  0.1948  -0.3386 17  ASP B CG  
4381  O OD1 . ASP B 17  ? 0.7907 1.2821 2.2692 0.6917  0.1987  -0.3317 17  ASP B OD1 
4382  O OD2 . ASP B 17  ? 0.7634 1.2579 2.2186 0.6502  0.2017  -0.3278 17  ASP B OD2 
4383  N N   . GLY B 18  ? 0.8984 1.0700 2.3660 0.6970  0.1448  -0.3627 18  GLY B N   
4384  C CA  . GLY B 18  ? 0.9417 1.0287 2.4039 0.6993  0.1300  -0.3767 18  GLY B CA  
4385  C C   . GLY B 18  ? 0.9308 0.9775 2.3874 0.6605  0.1244  -0.3657 18  GLY B C   
4386  O O   . GLY B 18  ? 0.9598 0.9357 2.4176 0.6539  0.1122  -0.3667 18  GLY B O   
4387  N N   . GLU B 19  ? 0.8872 0.9782 2.3385 0.6344  0.1330  -0.3541 19  GLU B N   
4388  C CA  . GLU B 19  ? 0.8825 0.9435 2.3231 0.6059  0.1278  -0.3550 19  GLU B CA  
4389  C C   . GLU B 19  ? 0.8431 0.8956 2.2948 0.5711  0.1285  -0.3218 19  GLU B C   
4390  O O   . GLU B 19  ? 0.8027 0.9065 2.2585 0.5557  0.1386  -0.3027 19  GLU B O   
4391  C CB  . GLU B 19  ? 0.8759 0.9884 2.2993 0.6052  0.1352  -0.3704 19  GLU B CB  
4392  C CG  . GLU B 19  ? 0.9257 1.0308 2.3338 0.6356  0.1308  -0.4091 19  GLU B CG  
4393  C CD  . GLU B 19  ? 0.9628 0.9940 2.3623 0.6300  0.1155  -0.4288 19  GLU B CD  
4394  O OE1 . GLU B 19  ? 0.9481 0.9373 2.3534 0.6009  0.1091  -0.4110 19  GLU B OE1 
4395  O OE2 . GLU B 19  ? 1.0058 1.0226 2.3931 0.6540  0.1097  -0.4626 19  GLU B OE2 
4396  N N   . LYS B 20  ? 0.8604 0.8478 2.3168 0.5580  0.1176  -0.3152 20  LYS B N   
4397  C CA  . LYS B 20  ? 0.8315 0.8105 2.2974 0.5260  0.1179  -0.2858 20  LYS B CA  
4398  C C   . LYS B 20  ? 0.7863 0.8142 2.2463 0.5033  0.1267  -0.2769 20  LYS B C   
4399  O O   . LYS B 20  ? 0.7923 0.8290 2.2374 0.5015  0.1265  -0.2938 20  LYS B O   
4400  C CB  . LYS B 20  ? 0.8611 0.7685 2.3279 0.5105  0.1052  -0.2847 20  LYS B CB  
4401  C CG  . LYS B 20  ? 0.8976 0.7563 2.3753 0.5256  0.0971  -0.2804 20  LYS B CG  
4402  C CD  . LYS B 20  ? 0.9213 0.7123 2.4019 0.5066  0.0852  -0.2746 20  LYS B CD  
4403  C CE  . LYS B 20  ? 0.9774 0.7197 2.4486 0.5166  0.0742  -0.3036 20  LYS B CE  
4404  N NZ  . LYS B 20  ? 1.0235 0.7431 2.4965 0.5513  0.0697  -0.3194 20  LYS B NZ  
4405  N N   . TYR B 21  ? 0.7425 0.8007 2.2142 0.4868  0.1336  -0.2501 21  TYR B N   
4406  C CA  . TYR B 21  ? 0.7054 0.8122 2.1750 0.4665  0.1425  -0.2375 21  TYR B CA  
4407  C C   . TYR B 21  ? 0.6758 0.7661 2.1552 0.4367  0.1408  -0.2123 21  TYR B C   
4408  O O   . TYR B 21  ? 0.6558 0.7407 2.1489 0.4343  0.1405  -0.1957 21  TYR B O   
4409  C CB  . TYR B 21  ? 0.6847 0.8571 2.1604 0.4793  0.1540  -0.2321 21  TYR B CB  
4410  C CG  . TYR B 21  ? 0.6492 0.8782 2.1212 0.4635  0.1640  -0.2226 21  TYR B CG  
4411  C CD1 . TYR B 21  ? 0.6612 0.9233 2.1178 0.4735  0.1687  -0.2393 21  TYR B CD1 
4412  C CD2 . TYR B 21  ? 0.6033 0.8540 2.0871 0.4396  0.1687  -0.1968 21  TYR B CD2 
4413  C CE1 . TYR B 21  ? 0.6330 0.9472 2.0862 0.4590  0.1779  -0.2280 21  TYR B CE1 
4414  C CE2 . TYR B 21  ? 0.5758 0.8746 2.0573 0.4250  0.1772  -0.1866 21  TYR B CE2 
4415  C CZ  . TYR B 21  ? 0.5901 0.9209 2.0564 0.4344  0.1820  -0.2008 21  TYR B CZ  
4416  O OH  . TYR B 21  ? 0.5681 0.9471 2.0316 0.4204  0.1904  -0.1888 21  TYR B OH  
4417  N N   . PHE B 22  ? 0.6807 0.7648 2.1524 0.4150  0.1392  -0.2104 22  PHE B N   
4418  C CA  . PHE B 22  ? 0.6658 0.7388 2.1458 0.3875  0.1381  -0.1885 22  PHE B CA  
4419  C C   . PHE B 22  ? 0.6459 0.7727 2.1294 0.3751  0.1480  -0.1731 22  PHE B C   
4420  O O   . PHE B 22  ? 0.6490 0.8024 2.1221 0.3706  0.1518  -0.1776 22  PHE B O   
4421  C CB  . PHE B 22  ? 0.6707 0.7036 2.1431 0.3708  0.1297  -0.1935 22  PHE B CB  
4422  C CG  . PHE B 22  ? 0.6438 0.6544 2.1269 0.3473  0.1265  -0.1729 22  PHE B CG  
4423  C CD1 . PHE B 22  ? 0.6114 0.6477 2.0976 0.3270  0.1312  -0.1569 22  PHE B CD1 
4424  C CD2 . PHE B 22  ? 0.6553 0.6205 2.1456 0.3465  0.1191  -0.1692 22  PHE B CD2 
4425  C CE1 . PHE B 22  ? 0.5914 0.6096 2.0871 0.3078  0.1284  -0.1402 22  PHE B CE1 
4426  C CE2 . PHE B 22  ? 0.6348 0.5855 2.1343 0.3261  0.1170  -0.1505 22  PHE B CE2 
4427  C CZ  . PHE B 22  ? 0.6041 0.5818 2.1060 0.3075  0.1217  -0.1374 22  PHE B CZ  
4428  N N   . ILE B 23  ? 0.6320 0.7742 2.1305 0.3692  0.1515  -0.1546 23  ILE B N   
4429  C CA  . ILE B 23  ? 0.6024 0.7923 2.1077 0.3565  0.1600  -0.1390 23  ILE B CA  
4430  C C   . ILE B 23  ? 0.5969 0.7759 2.1002 0.3302  0.1581  -0.1280 23  ILE B C   
4431  O O   . ILE B 23  ? 0.5675 0.7230 2.0793 0.3157  0.1542  -0.1161 23  ILE B O   
4432  C CB  . ILE B 23  ? 0.5725 0.7798 2.0948 0.3580  0.1626  -0.1249 23  ILE B CB  
4433  C CG1 . ILE B 23  ? 0.5816 0.7994 2.1065 0.3860  0.1637  -0.1354 23  ILE B CG1 
4434  C CG2 . ILE B 23  ? 0.5463 0.8007 2.0771 0.3423  0.1704  -0.1094 23  ILE B CG2 
4435  C CD1 . ILE B 23  ? 0.5670 0.7888 2.1078 0.3889  0.1628  -0.1226 23  ILE B CD1 
4436  N N   . LYS B 24  ? 0.6273 0.8250 2.1187 0.3262  0.1608  -0.1330 24  LYS B N   
4437  C CA  . LYS B 24  ? 0.6350 0.8315 2.1242 0.3037  0.1600  -0.1220 24  LYS B CA  
4438  C C   . LYS B 24  ? 0.6120 0.8526 2.1101 0.2928  0.1682  -0.1043 24  LYS B C   
4439  O O   . LYS B 24  ? 0.6268 0.9030 2.1175 0.2932  0.1740  -0.1037 24  LYS B O   
4440  C CB  . LYS B 24  ? 0.6791 0.8749 2.1500 0.3060  0.1579  -0.1359 24  LYS B CB  
4441  C CG  . LYS B 24  ? 0.7261 0.8787 2.1883 0.3160  0.1489  -0.1559 24  LYS B CG  
4442  C CD  . LYS B 24  ? 0.7675 0.9203 2.2121 0.3150  0.1456  -0.1698 24  LYS B CD  
4443  C CE  . LYS B 24  ? 0.8081 1.0067 2.2407 0.3295  0.1528  -0.1791 24  LYS B CE  
4444  N NZ  . LYS B 24  ? 0.8611 1.0615 2.2758 0.3279  0.1489  -0.1921 24  LYS B NZ  
4445  N N   . ALA B 25  ? 0.5839 0.8225 2.0979 0.2829  0.1683  -0.0900 25  ALA B N   
4446  C CA  . ALA B 25  ? 0.5642 0.8417 2.0896 0.2720  0.1749  -0.0741 25  ALA B CA  
4447  C C   . ALA B 25  ? 0.5713 0.8405 2.0996 0.2486  0.1731  -0.0598 25  ALA B C   
4448  O O   . ALA B 25  ? 0.6065 0.8413 2.1289 0.2418  0.1668  -0.0622 25  ALA B O   
4449  C CB  . ALA B 25  ? 0.5478 0.8319 2.0892 0.2756  0.1755  -0.0686 25  ALA B CB  
4450  N N   . ILE B 26  ? 0.5354 0.8379 2.0740 0.2370  0.1786  -0.0452 26  ILE B N   
4451  C CA  . ILE B 26  ? 0.4953 0.7907 2.0432 0.2154  0.1767  -0.0298 26  ILE B CA  
4452  C C   . ILE B 26  ? 0.4652 0.7878 2.0314 0.2083  0.1803  -0.0188 26  ILE B C   
4453  O O   . ILE B 26  ? 0.4537 0.8149 2.0236 0.2152  0.1867  -0.0181 26  ILE B O   
4454  C CB  . ILE B 26  ? 0.4956 0.8008 2.0341 0.2054  0.1782  -0.0223 26  ILE B CB  
4455  C CG1 . ILE B 26  ? 0.4801 0.7691 2.0276 0.1848  0.1745  -0.0076 26  ILE B CG1 
4456  C CG2 . ILE B 26  ? 0.4938 0.8481 2.0304 0.2087  0.1871  -0.0172 26  ILE B CG2 
4457  C CD1 . ILE B 26  ? 0.4817 0.7734 2.0192 0.1762  0.1743  0.0005  26  ILE B CD1 
4458  N N   . GLY B 27  ? 0.4472 0.7512 2.0254 0.1951  0.1758  -0.0118 27  GLY B N   
4459  C CA  . GLY B 27  ? 0.4246 0.7526 2.0206 0.1838  0.1777  -0.0011 27  GLY B CA  
4460  C C   . GLY B 27  ? 0.4115 0.7660 2.0108 0.1694  0.1824  0.0123  27  GLY B C   
4461  O O   . GLY B 27  ? 0.3931 0.7320 1.9852 0.1606  0.1806  0.0178  27  GLY B O   
4462  N N   . TYR B 28  ? 0.4186 0.8152 2.0292 0.1677  0.1883  0.0184  28  TYR B N   
4463  C CA  . TYR B 28  ? 0.4185 0.8481 2.0334 0.1546  0.1940  0.0331  28  TYR B CA  
4464  C C   . TYR B 28  ? 0.4046 0.8595 2.0420 0.1406  0.1949  0.0428  28  TYR B C   
4465  O O   . TYR B 28  ? 0.4222 0.8957 2.0679 0.1501  0.1958  0.0361  28  TYR B O   
4466  C CB  . TYR B 28  ? 0.4264 0.8957 2.0308 0.1688  0.2024  0.0300  28  TYR B CB  
4467  C CG  . TYR B 28  ? 0.4279 0.9360 2.0358 0.1549  0.2092  0.0476  28  TYR B CG  
4468  C CD1 . TYR B 28  ? 0.4333 0.9275 2.0331 0.1424  0.2080  0.0591  28  TYR B CD1 
4469  C CD2 . TYR B 28  ? 0.4336 0.9941 2.0531 0.1545  0.2169  0.0538  28  TYR B CD2 
4470  C CE1 . TYR B 28  ? 0.4389 0.9679 2.0414 0.1294  0.2140  0.0777  28  TYR B CE1 
4471  C CE2 . TYR B 28  ? 0.4427 1.0407 2.0660 0.1403  0.2235  0.0721  28  TYR B CE2 
4472  C CZ  . TYR B 28  ? 0.4423 1.0235 2.0566 0.1277  0.2221  0.0846  28  TYR B CZ  
4473  O OH  . TYR B 28  ? 0.4631 1.0806 2.0808 0.1135  0.2285  0.1050  28  TYR B OH  
4474  N N   . GLU B 29  ? 0.3870 0.8437 2.0343 0.1188  0.1943  0.0586  29  GLU B N   
4475  C CA  . GLU B 29  ? 0.3791 0.8603 2.0490 0.1022  0.1945  0.0683  29  GLU B CA  
4476  C C   . GLU B 29  ? 0.3963 0.9028 2.0720 0.0842  0.1994  0.0881  29  GLU B C   
4477  O O   . GLU B 29  ? 0.4211 0.9004 2.0944 0.0713  0.1957  0.0979  29  GLU B O   
4478  C CB  . GLU B 29  ? 0.3644 0.8086 2.0448 0.0919  0.1851  0.0649  29  GLU B CB  
4479  C CG  . GLU B 29  ? 0.3616 0.8275 2.0661 0.0755  0.1832  0.0704  29  GLU B CG  
4480  C CD  . GLU B 29  ? 0.3610 0.7922 2.0745 0.0670  0.1735  0.0642  29  GLU B CD  
4481  O OE1 . GLU B 29  ? 0.3682 0.7627 2.0791 0.0571  0.1684  0.0677  29  GLU B OE1 
4482  O OE2 . GLU B 29  ? 0.3494 0.7915 2.0718 0.0714  0.1707  0.0553  29  GLU B OE2 
4483  N N   . ILE B 30  ? 0.3974 0.9573 2.0810 0.0838  0.2075  0.0947  30  ILE B N   
4484  C CA  . ILE B 30  ? 0.4057 0.9970 2.0980 0.0645  0.2129  0.1162  30  ILE B CA  
4485  C C   . ILE B 30  ? 0.3995 0.9900 2.1181 0.0395  0.2079  0.1266  30  ILE B C   
4486  O O   . ILE B 30  ? 0.3802 0.9659 2.1109 0.0405  0.2030  0.1156  30  ILE B O   
4487  C CB  . ILE B 30  ? 0.4159 1.0692 2.1054 0.0754  0.2243  0.1185  30  ILE B CB  
4488  C CG1 . ILE B 30  ? 0.4340 1.1227 2.1277 0.0569  0.2312  0.1430  30  ILE B CG1 
4489  C CG2 . ILE B 30  ? 0.4045 1.0936 2.1110 0.0815  0.2261  0.1104  30  ILE B CG2 
4490  C CD1 . ILE B 30  ? 0.4510 1.1142 2.1257 0.0544  0.2305  0.1524  30  ILE B CD1 
4491  N N   . GLY B 31  ? 0.4162 1.0109 2.1434 0.0168  0.2086  0.1479  31  GLY B N   
4492  C CA  . GLY B 31  ? 0.4248 1.0138 2.1774 -0.0095 0.2029  0.1586  31  GLY B CA  
4493  C C   . GLY B 31  ? 0.4331 0.9611 2.1880 -0.0147 0.1908  0.1496  31  GLY B C   
4494  O O   . GLY B 31  ? 0.4254 0.9470 2.1991 -0.0263 0.1843  0.1447  31  GLY B O   
4495  N N   . ALA B 32  ? 0.4498 0.9361 2.1854 -0.0054 0.1877  0.1466  32  ALA B N   
4496  C CA  . ALA B 32  ? 0.4504 0.8807 2.1867 -0.0091 0.1770  0.1393  32  ALA B CA  
4497  C C   . ALA B 32  ? 0.4583 0.8573 2.1854 -0.0156 0.1745  0.1534  32  ALA B C   
4498  O O   . ALA B 32  ? 0.4555 0.8129 2.1721 -0.0076 0.1684  0.1448  32  ALA B O   
4499  C CB  . ALA B 32  ? 0.4392 0.8487 2.1618 0.0130  0.1743  0.1168  32  ALA B CB  
4500  N N   . ARG B 33  ? 0.4813 0.9032 2.2129 -0.0300 0.1794  0.1762  33  ARG B N   
4501  C CA  . ARG B 33  ? 0.5127 0.9075 2.2386 -0.0385 0.1764  0.1937  33  ARG B CA  
4502  C C   . ARG B 33  ? 0.5490 0.9017 2.2941 -0.0569 0.1655  0.1975  33  ARG B C   
4503  O O   . ARG B 33  ? 0.5500 0.9070 2.3152 -0.0684 0.1622  0.1919  33  ARG B O   
4504  C CB  . ARG B 33  ? 0.5194 0.9525 2.2447 -0.0497 0.1846  0.2201  33  ARG B CB  
4505  C CG  . ARG B 33  ? 0.5085 0.9603 2.2072 -0.0326 0.1917  0.2228  33  ARG B CG  
4506  C CD  . ARG B 33  ? 0.4794 0.9568 2.1655 -0.0097 0.1975  0.2001  33  ARG B CD  
4507  N NE  . ARG B 33  ? 0.4796 0.9813 2.1413 0.0059  0.2046  0.2013  33  ARG B NE  
4508  C CZ  . ARG B 33  ? 0.4712 0.9926 2.1178 0.0281  0.2094  0.1819  33  ARG B CZ  
4509  N NH1 . ARG B 33  ? 0.4533 0.9786 2.1077 0.0371  0.2092  0.1632  33  ARG B NH1 
4510  N NH2 . ARG B 33  ? 0.4861 1.0247 2.1100 0.0416  0.2142  0.1814  33  ARG B NH2 
4511  N N   . PRO B 34  ? 0.5810 0.8923 2.3204 -0.0588 0.1592  0.2056  34  PRO B N   
4512  C CA  . PRO B 34  ? 0.5978 0.8672 2.3554 -0.0755 0.1486  0.2104  34  PRO B CA  
4513  C C   . PRO B 34  ? 0.6063 0.9002 2.3878 -0.1005 0.1500  0.2271  34  PRO B C   
4514  O O   . PRO B 34  ? 0.6254 0.9483 2.4065 -0.1101 0.1568  0.2508  34  PRO B O   
4515  C CB  . PRO B 34  ? 0.6267 0.8640 2.3732 -0.0739 0.1449  0.2256  34  PRO B CB  
4516  C CG  . PRO B 34  ? 0.6233 0.8752 2.3425 -0.0508 0.1510  0.2176  34  PRO B CG  
4517  C CD  . PRO B 34  ? 0.6016 0.9035 2.3167 -0.0434 0.1610  0.2084  34  PRO B CD  
4518  N N   . GLY B 35  ? 0.6015 0.8872 2.4031 -0.1106 0.1436  0.2140  35  GLY B N   
4519  C CA  . GLY B 35  ? 0.6085 0.9151 2.4360 -0.1365 0.1430  0.2268  35  GLY B CA  
4520  C C   . GLY B 35  ? 0.5821 0.9415 2.4171 -0.1350 0.1495  0.2162  35  GLY B C   
4521  O O   . GLY B 35  ? 0.5968 0.9739 2.4557 -0.1555 0.1472  0.2202  35  GLY B O   
4522  N N   . GLN B 36  ? 0.5563 0.9411 2.3719 -0.1109 0.1571  0.2027  36  GLN B N   
4523  C CA  . GLN B 36  ? 0.5408 0.9748 2.3626 -0.1058 0.1629  0.1922  36  GLN B CA  
4524  C C   . GLN B 36  ? 0.5361 0.9518 2.3539 -0.0893 0.1571  0.1640  36  GLN B C   
4525  O O   . GLN B 36  ? 0.5568 0.9405 2.3556 -0.0710 0.1550  0.1522  36  GLN B O   
4526  C CB  . GLN B 36  ? 0.5274 1.0066 2.3309 -0.0881 0.1757  0.1959  36  GLN B CB  
4527  C CG  . GLN B 36  ? 0.5530 1.0477 2.3500 -0.0966 0.1825  0.2226  36  GLN B CG  
4528  C CD  . GLN B 36  ? 0.5573 1.1021 2.3365 -0.0785 0.1951  0.2233  36  GLN B CD  
4529  O OE1 . GLN B 36  ? 0.5358 1.0771 2.2957 -0.0532 0.1970  0.2040  36  GLN B OE1 
4530  N NE2 . GLN B 36  ? 0.5863 1.1798 2.3728 -0.0913 0.2039  0.2452  36  GLN B NE2 
4531  N N   . ALA B 37  ? 0.5399 0.9795 2.3757 -0.0962 0.1546  0.1543  37  ALA B N   
4532  C CA  . ALA B 37  ? 0.5354 0.9761 2.3660 -0.0781 0.1519  0.1301  37  ALA B CA  
4533  C C   . ALA B 37  ? 0.5121 1.0131 2.3456 -0.0693 0.1606  0.1286  37  ALA B C   
4534  O O   . ALA B 37  ? 0.5053 1.0457 2.3588 -0.0868 0.1631  0.1395  37  ALA B O   
4535  C CB  . ALA B 37  ? 0.5517 0.9665 2.3994 -0.0908 0.1398  0.1175  37  ALA B CB  
4536  N N   . PRO B 38  ? 0.4809 0.9912 2.2956 -0.0422 0.1655  0.1157  38  PRO B N   
4537  C CA  . PRO B 38  ? 0.4754 1.0415 2.2894 -0.0296 0.1750  0.1158  38  PRO B CA  
4538  C C   . PRO B 38  ? 0.4730 1.0760 2.3057 -0.0312 0.1726  0.1066  38  PRO B C   
4539  O O   . PRO B 38  ? 0.4828 1.1395 2.3285 -0.0362 0.1789  0.1147  38  PRO B O   
4540  C CB  . PRO B 38  ? 0.4593 1.0122 2.2463 -0.0002 0.1791  0.1046  38  PRO B CB  
4541  C CG  . PRO B 38  ? 0.4586 0.9513 2.2349 0.0027  0.1705  0.0952  38  PRO B CG  
4542  C CD  . PRO B 38  ? 0.4696 0.9370 2.2637 -0.0225 0.1618  0.1009  38  PRO B CD  
4543  N N   . TYR B 39  ? 0.4642 1.0413 2.2992 -0.0281 0.1632  0.0906  39  TYR B N   
4544  C CA  . TYR B 39  ? 0.4528 1.0633 2.3041 -0.0286 0.1593  0.0808  39  TYR B CA  
4545  C C   . TYR B 39  ? 0.4621 1.0876 2.3419 -0.0594 0.1532  0.0871  39  TYR B C   
4546  O O   . TYR B 39  ? 0.4385 1.0990 2.3342 -0.0624 0.1499  0.0801  39  TYR B O   
4547  C CB  . TYR B 39  ? 0.4339 1.0123 2.2740 -0.0123 0.1518  0.0619  39  TYR B CB  
4548  C CG  . TYR B 39  ? 0.4253 0.9927 2.2406 0.0174  0.1570  0.0550  39  TYR B CG  
4549  C CD1 . TYR B 39  ? 0.4422 0.9671 2.2375 0.0248  0.1585  0.0563  39  TYR B CD1 
4550  C CD2 . TYR B 39  ? 0.4014 0.9990 2.2142 0.0380  0.1592  0.0469  39  TYR B CD2 
4551  C CE1 . TYR B 39  ? 0.4212 0.9346 2.1953 0.0498  0.1622  0.0494  39  TYR B CE1 
4552  C CE2 . TYR B 39  ? 0.3991 0.9822 2.1906 0.0641  0.1629  0.0406  39  TYR B CE2 
4553  C CZ  . TYR B 39  ? 0.4062 0.9471 2.1786 0.0691  0.1643  0.0415  39  TYR B CZ  
4554  O OH  . TYR B 39  ? 0.4064 0.9324 2.1593 0.0931  0.1671  0.0348  39  TYR B OH  
4555  N N   . GLU B 40  ? 0.5009 1.0992 2.3877 -0.0822 0.1506  0.1000  40  GLU B N   
4556  C CA  . GLU B 40  ? 0.5481 1.1479 2.4620 -0.1131 0.1427  0.1051  40  GLU B CA  
4557  C C   . GLU B 40  ? 0.5648 1.2057 2.4949 -0.1337 0.1502  0.1286  40  GLU B C   
4558  O O   . GLU B 40  ? 0.5576 1.2344 2.5135 -0.1547 0.1477  0.1328  40  GLU B O   
4559  C CB  . GLU B 40  ? 0.6020 1.1394 2.5168 -0.1282 0.1333  0.1058  40  GLU B CB  
4560  C CG  . GLU B 40  ? 0.6236 1.1116 2.5231 -0.1124 0.1251  0.0853  40  GLU B CG  
4561  C CD  . GLU B 40  ? 0.6952 1.1275 2.6010 -0.1290 0.1146  0.0845  40  GLU B CD  
4562  O OE1 . GLU B 40  ? 0.7143 1.1314 2.6261 -0.1455 0.1157  0.1034  40  GLU B OE1 
4563  O OE2 . GLU B 40  ? 0.7642 1.1674 2.6685 -0.1244 0.1051  0.0652  40  GLU B OE2 
4564  N N   . ASP B 41  ? 0.5789 1.2132 2.4938 -0.1292 0.1589  0.1445  41  ASP B N   
4565  C CA  . ASP B 41  ? 0.5986 1.2661 2.5252 -0.1489 0.1665  0.1700  41  ASP B CA  
4566  C C   . ASP B 41  ? 0.5888 1.3311 2.5221 -0.1413 0.1769  0.1727  41  ASP B C   
4567  O O   . ASP B 41  ? 0.5841 1.3431 2.5037 -0.1136 0.1805  0.1572  41  ASP B O   
4568  C CB  . ASP B 41  ? 0.6126 1.2578 2.5168 -0.1410 0.1733  0.1843  41  ASP B CB  
4569  C CG  . ASP B 41  ? 0.6131 1.1869 2.5085 -0.1455 0.1644  0.1844  41  ASP B CG  
4570  O OD1 . ASP B 41  ? 0.6080 1.1468 2.5169 -0.1578 0.1525  0.1742  41  ASP B OD1 
4571  O OD2 . ASP B 41  ? 0.6170 1.1728 2.4921 -0.1355 0.1692  0.1936  41  ASP B OD2 
4572  N N   . GLU B 42  ? 0.6060 1.3929 2.5610 -0.1655 0.1815  0.1931  42  GLU B N   
4573  C CA  . GLU B 42  ? 0.5898 1.4525 2.5495 -0.1576 0.1937  0.1997  42  GLU B CA  
4574  C C   . GLU B 42  ? 0.5989 1.4656 2.5277 -0.1282 0.2050  0.2001  42  GLU B C   
4575  O O   . GLU B 42  ? 0.6033 1.4418 2.5181 -0.1318 0.2076  0.2138  42  GLU B O   
4576  C CB  . GLU B 42  ? 0.5947 1.5002 2.5801 -0.1905 0.1980  0.2263  42  GLU B CB  
4577  C CG  . GLU B 42  ? 0.5769 1.5690 2.5701 -0.1834 0.2111  0.2333  42  GLU B CG  
4578  C CD  . GLU B 42  ? 0.5870 1.6227 2.5946 -0.2092 0.2201  0.2646  42  GLU B CD  
4579  O OE1 . GLU B 42  ? 0.6029 1.5958 2.6088 -0.2289 0.2172  0.2823  42  GLU B OE1 
4580  O OE2 . GLU B 42  ? 0.5769 1.6897 2.5972 -0.2090 0.2300  0.2718  42  GLU B OE2 
4581  N N   . ARG B 43  ? 0.5905 1.4915 2.5090 -0.0989 0.2107  0.1847  43  ARG B N   
4582  C CA  . ARG B 43  ? 0.5749 1.4671 2.4624 -0.0674 0.2182  0.1774  43  ARG B CA  
4583  C C   . ARG B 43  ? 0.5605 1.5013 2.4428 -0.0681 0.2318  0.1965  43  ARG B C   
4584  O O   . ARG B 43  ? 0.5548 1.5590 2.4569 -0.0805 0.2383  0.2088  43  ARG B O   
4585  C CB  . ARG B 43  ? 0.5560 1.4616 2.4338 -0.0348 0.2187  0.1541  43  ARG B CB  
4586  C CG  . ARG B 43  ? 0.5433 1.5260 2.4358 -0.0260 0.2263  0.1532  43  ARG B CG  
4587  C CD  . ARG B 43  ? 0.5273 1.5089 2.4069 0.0089  0.2251  0.1304  43  ARG B CD  
4588  N NE  . ARG B 43  ? 0.5253 1.5762 2.4219 0.0188  0.2293  0.1267  43  ARG B NE  
4589  C CZ  . ARG B 43  ? 0.5355 1.6518 2.4359 0.0265  0.2413  0.1342  43  ARG B CZ  
4590  N NH1 . ARG B 43  ? 0.5510 1.6739 2.4395 0.0225  0.2503  0.1475  43  ARG B NH1 
4591  N NH2 . ARG B 43  ? 0.5241 1.7018 2.4400 0.0388  0.2441  0.1286  43  ARG B NH2 
4592  N N   . LYS B 44  ? 0.5476 1.4606 2.4026 -0.0541 0.2357  0.1982  44  LYS B N   
4593  C CA  . LYS B 44  ? 0.5423 1.4978 2.3867 -0.0514 0.2483  0.2145  44  LYS B CA  
4594  C C   . LYS B 44  ? 0.5098 1.4507 2.3211 -0.0170 0.2526  0.1984  44  LYS B C   
4595  O O   . LYS B 44  ? 0.4984 1.3810 2.2942 -0.0033 0.2448  0.1819  44  LYS B O   
4596  C CB  . LYS B 44  ? 0.5698 1.5084 2.4215 -0.0832 0.2471  0.2423  44  LYS B CB  
4597  C CG  . LYS B 44  ? 0.6041 1.5955 2.4496 -0.0875 0.2603  0.2656  44  LYS B CG  
4598  C CD  . LYS B 44  ? 0.6197 1.5861 2.4319 -0.0700 0.2638  0.2664  44  LYS B CD  
4599  C CE  . LYS B 44  ? 0.6310 1.6651 2.4320 -0.0622 0.2786  0.2798  44  LYS B CE  
4600  N NZ  . LYS B 44  ? 0.6345 1.6476 2.4049 -0.0497 0.2812  0.2835  44  LYS B NZ  
4601  N N   . ASP B 45  ? 0.4902 1.4874 2.2917 -0.0041 0.2652  0.2036  45  ASP B N   
4602  C CA  . ASP B 45  ? 0.4777 1.4770 2.2510 0.0305  0.2704  0.1856  45  ASP B CA  
4603  C C   . ASP B 45  ? 0.4802 1.4225 2.2278 0.0337  0.2667  0.1861  45  ASP B C   
4604  O O   . ASP B 45  ? 0.4634 1.3695 2.1905 0.0578  0.2631  0.1652  45  ASP B O   
4605  C CB  . ASP B 45  ? 0.4804 1.5596 2.2517 0.0417  0.2847  0.1911  45  ASP B CB  
4606  C CG  . ASP B 45  ? 0.4641 1.6036 2.2569 0.0490  0.2889  0.1841  45  ASP B CG  
4607  O OD1 . ASP B 45  ? 0.4369 1.5547 2.2315 0.0663  0.2823  0.1629  45  ASP B OD1 
4608  O OD2 . ASP B 45  ? 0.4780 1.6882 2.2856 0.0378  0.2989  0.2008  45  ASP B OD2 
4609  N N   . GLU B 46  ? 0.5008 1.4394 2.2505 0.0093  0.2676  0.2113  46  GLU B N   
4610  C CA  . GLU B 46  ? 0.5023 1.3856 2.2338 0.0051  0.2621  0.2173  46  GLU B CA  
4611  C C   . GLU B 46  ? 0.5060 1.3988 2.2061 0.0318  0.2683  0.2071  46  GLU B C   
4612  O O   . GLU B 46  ? 0.5369 1.3782 2.2177 0.0445  0.2618  0.1938  46  GLU B O   
4613  C CB  . GLU B 46  ? 0.4919 1.3016 2.2257 0.0032  0.2484  0.2038  46  GLU B CB  
4614  C CG  . GLU B 46  ? 0.4934 1.2833 2.2553 -0.0271 0.2405  0.2163  46  GLU B CG  
4615  C CD  . GLU B 46  ? 0.5075 1.2602 2.2717 -0.0511 0.2353  0.2389  46  GLU B CD  
4616  O OE1 . GLU B 46  ? 0.5085 1.2546 2.2525 -0.0463 0.2384  0.2489  46  GLU B OE1 
4617  O OE2 . GLU B 46  ? 0.5052 1.2342 2.2918 -0.0745 0.2273  0.2460  46  GLU B OE2 
4618  N N   . LEU B 47  ? 0.5086 1.4689 2.2039 0.0393  0.2806  0.2135  47  LEU B N   
4619  C CA  . LEU B 47  ? 0.5111 1.4902 2.1783 0.0694  0.2868  0.1967  47  LEU B CA  
4620  C C   . LEU B 47  ? 0.5203 1.4771 2.1639 0.0672  0.2860  0.2072  47  LEU B C   
4621  O O   . LEU B 47  ? 0.5253 1.4523 2.1447 0.0884  0.2827  0.1878  47  LEU B O   
4622  C CB  . LEU B 47  ? 0.5178 1.5819 2.1890 0.0786  0.3005  0.1994  47  LEU B CB  
4623  C CG  . LEU B 47  ? 0.5092 1.6061 2.2070 0.0785  0.3019  0.1931  47  LEU B CG  
4624  C CD1 . LEU B 47  ? 0.5212 1.7014 2.2365 0.0644  0.3140  0.2150  47  LEU B CD1 
4625  C CD2 . LEU B 47  ? 0.5042 1.5986 2.1911 0.1144  0.3013  0.1603  47  LEU B CD2 
4626  N N   . GLU B 48  ? 0.5281 1.4993 2.1788 0.0413  0.2885  0.2385  48  GLU B N   
4627  C CA  . GLU B 48  ? 0.5486 1.5055 2.1764 0.0403  0.2881  0.2506  48  GLU B CA  
4628  C C   . GLU B 48  ? 0.5421 1.4193 2.1586 0.0461  0.2750  0.2359  48  GLU B C   
4629  O O   . GLU B 48  ? 0.5457 1.4077 2.1364 0.0603  0.2734  0.2285  48  GLU B O   
4630  C CB  . GLU B 48  ? 0.5707 1.5484 2.2116 0.0092  0.2912  0.2895  48  GLU B CB  
4631  C CG  . GLU B 48  ? 0.5961 1.5958 2.2113 0.0126  0.2965  0.3055  48  GLU B CG  
4632  C CD  . GLU B 48  ? 0.6211 1.6345 2.2488 -0.0188 0.2984  0.3469  48  GLU B CD  
4633  O OE1 . GLU B 48  ? 0.6226 1.6144 2.2787 -0.0438 0.2934  0.3609  48  GLU B OE1 
4634  O OE2 . GLU B 48  ? 0.6434 1.6899 2.2525 -0.0181 0.3048  0.3652  48  GLU B OE2 
4635  N N   . LEU B 49  ? 0.5270 1.3569 2.1631 0.0352  0.2655  0.2309  49  LEU B N   
4636  C CA  . LEU B 49  ? 0.5171 1.2755 2.1456 0.0407  0.2534  0.2160  49  LEU B CA  
4637  C C   . LEU B 49  ? 0.5082 1.2559 2.1198 0.0706  0.2525  0.1831  49  LEU B C   
4638  O O   . LEU B 49  ? 0.5110 1.2189 2.1038 0.0818  0.2464  0.1714  49  LEU B O   
4639  C CB  . LEU B 49  ? 0.5098 1.2261 2.1636 0.0217  0.2441  0.2186  49  LEU B CB  
4640  C CG  . LEU B 49  ? 0.5275 1.2153 2.1925 -0.0054 0.2384  0.2456  49  LEU B CG  
4641  C CD1 . LEU B 49  ? 0.5192 1.1576 2.2052 -0.0180 0.2274  0.2391  49  LEU B CD1 
4642  C CD2 . LEU B 49  ? 0.5321 1.1915 2.1749 -0.0015 0.2350  0.2535  49  LEU B CD2 
4643  N N   . MET B 50  ? 0.4970 1.2783 2.1170 0.0827  0.2576  0.1691  50  MET B N   
4644  C CA  . MET B 50  ? 0.4962 1.2674 2.1024 0.1115  0.2565  0.1389  50  MET B CA  
4645  C C   . MET B 50  ? 0.5192 1.3017 2.0959 0.1303  0.2601  0.1301  50  MET B C   
4646  O O   . MET B 50  ? 0.5306 1.2674 2.0912 0.1417  0.2528  0.1141  50  MET B O   
4647  C CB  . MET B 50  ? 0.4913 1.3042 2.1118 0.1225  0.2621  0.1284  50  MET B CB  
4648  C CG  . MET B 50  ? 0.4758 1.2616 2.1200 0.1122  0.2547  0.1255  50  MET B CG  
4649  S SD  . MET B 50  ? 0.4543 1.2892 2.1174 0.1248  0.2595  0.1142  50  MET B SD  
4650  C CE  . MET B 50  ? 0.4580 1.2609 2.1000 0.1613  0.2558  0.0817  50  MET B CE  
4651  N N   . LYS B 51  ? 0.5331 1.3767 2.1027 0.1321  0.2709  0.1411  51  LYS B N   
4652  C CA  . LYS B 51  ? 0.5577 1.4187 2.0983 0.1506  0.2745  0.1313  51  LYS B CA  
4653  C C   . LYS B 51  ? 0.5625 1.3672 2.0863 0.1482  0.2646  0.1298  51  LYS B C   
4654  O O   . LYS B 51  ? 0.5634 1.3499 2.0660 0.1683  0.2612  0.1071  51  LYS B O   
4655  C CB  . LYS B 51  ? 0.5774 1.5087 2.1124 0.1451  0.2866  0.1521  51  LYS B CB  
4656  C CG  . LYS B 51  ? 0.5839 1.5838 2.1294 0.1542  0.2981  0.1495  51  LYS B CG  
4657  C CD  . LYS B 51  ? 0.6068 1.6802 2.1488 0.1456  0.3107  0.1737  51  LYS B CD  
4658  C CE  . LYS B 51  ? 0.6103 1.7486 2.1719 0.1475  0.3210  0.1760  51  LYS B CE  
4659  N NZ  . LYS B 51  ? 0.6351 1.8543 2.1909 0.1453  0.3348  0.1943  51  LYS B NZ  
4660  N N   . PHE B 52  ? 0.5626 1.3398 2.0965 0.1237  0.2596  0.1537  52  PHE B N   
4661  C CA  . PHE B 52  ? 0.5723 1.2959 2.0939 0.1210  0.2495  0.1531  52  PHE B CA  
4662  C C   . PHE B 52  ? 0.5568 1.2273 2.0771 0.1347  0.2404  0.1250  52  PHE B C   
4663  O O   . PHE B 52  ? 0.5618 1.2161 2.0617 0.1517  0.2369  0.1056  52  PHE B O   
4664  C CB  . PHE B 52  ? 0.5708 1.2747 2.1086 0.0930  0.2457  0.1835  52  PHE B CB  
4665  C CG  . PHE B 52  ? 0.5614 1.2094 2.0920 0.0875  0.2347  0.1873  52  PHE B CG  
4666  C CD1 . PHE B 52  ? 0.5692 1.2247 2.0794 0.0888  0.2342  0.1984  52  PHE B CD1 
4667  C CD2 . PHE B 52  ? 0.5443 1.1368 2.0898 0.0804  0.2249  0.1813  52  PHE B CD2 
4668  C CE1 . PHE B 52  ? 0.5738 1.1814 2.0794 0.0843  0.2240  0.2026  52  PHE B CE1 
4669  C CE2 . PHE B 52  ? 0.5438 1.0894 2.0845 0.0760  0.2153  0.1850  52  PHE B CE2 
4670  C CZ  . PHE B 52  ? 0.5641 1.1171 2.0855 0.0782  0.2147  0.1956  52  PHE B CZ  
4671  N N   . ASP B 53  ? 0.5399 1.1873 2.0823 0.1271  0.2369  0.1230  53  ASP B N   
4672  C CA  . ASP B 53  ? 0.5226 1.1200 2.0668 0.1365  0.2283  0.1012  53  ASP B CA  
4673  C C   . ASP B 53  ? 0.5342 1.1398 2.0631 0.1635  0.2302  0.0739  53  ASP B C   
4674  O O   . ASP B 53  ? 0.5392 1.1049 2.0566 0.1743  0.2230  0.0561  53  ASP B O   
4675  C CB  . ASP B 53  ? 0.5009 1.0863 2.0708 0.1252  0.2259  0.1042  53  ASP B CB  
4676  C CG  . ASP B 53  ? 0.4987 1.0709 2.0862 0.0984  0.2226  0.1285  53  ASP B CG  
4677  O OD1 . ASP B 53  ? 0.5001 1.0382 2.0808 0.0910  0.2165  0.1360  53  ASP B OD1 
4678  O OD2 . ASP B 53  ? 0.4907 1.0871 2.0990 0.0850  0.2259  0.1396  53  ASP B OD2 
4679  N N   . LEU B 54  ? 0.5489 1.2063 2.0787 0.1743  0.2395  0.0704  54  LEU B N   
4680  C CA  . LEU B 54  ? 0.5680 1.2327 2.0848 0.2016  0.2410  0.0435  54  LEU B CA  
4681  C C   . LEU B 54  ? 0.5868 1.2460 2.0763 0.2134  0.2393  0.0321  54  LEU B C   
4682  O O   . LEU B 54  ? 0.5919 1.2240 2.0693 0.2316  0.2342  0.0076  54  LEU B O   
4683  C CB  . LEU B 54  ? 0.5804 1.3066 2.1045 0.2121  0.2517  0.0422  54  LEU B CB  
4684  C CG  . LEU B 54  ? 0.5716 1.3019 2.1200 0.2111  0.2519  0.0412  54  LEU B CG  
4685  C CD1 . LEU B 54  ? 0.5647 1.2448 2.1137 0.2254  0.2432  0.0198  54  LEU B CD1 
4686  C CD2 . LEU B 54  ? 0.5655 1.2925 2.1363 0.1820  0.2504  0.0660  54  LEU B CD2 
4687  N N   . GLU B 55  ? 0.6005 1.2852 2.0806 0.2025  0.2429  0.0505  55  GLU B N   
4688  C CA  . GLU B 55  ? 0.6305 1.3195 2.0839 0.2135  0.2416  0.0406  55  GLU B CA  
4689  C C   . GLU B 55  ? 0.6313 1.2590 2.0785 0.2084  0.2293  0.0353  55  GLU B C   
4690  O O   . GLU B 55  ? 0.6415 1.2517 2.0705 0.2231  0.2242  0.0135  55  GLU B O   
4691  C CB  . GLU B 55  ? 0.6527 1.3954 2.0979 0.2044  0.2499  0.0638  55  GLU B CB  
4692  C CG  . GLU B 55  ? 0.6864 1.4531 2.1019 0.2211  0.2511  0.0500  55  GLU B CG  
4693  C CD  . GLU B 55  ? 0.7164 1.5072 2.1205 0.2493  0.2552  0.0189  55  GLU B CD  
4694  O OE1 . GLU B 55  ? 0.6999 1.5449 2.1096 0.2568  0.2660  0.0206  55  GLU B OE1 
4695  O OE2 . GLU B 55  ? 0.7381 1.4921 2.1286 0.2642  0.2469  -0.0078 55  GLU B OE2 
4696  N N   . ASN B 56  ? 0.6122 1.2090 2.0751 0.1874  0.2244  0.0547  56  ASN B N   
4697  C CA  . ASN B 56  ? 0.6002 1.1411 2.0613 0.1819  0.2132  0.0509  56  ASN B CA  
4698  C C   . ASN B 56  ? 0.5976 1.1019 2.0586 0.1965  0.2074  0.0237  56  ASN B C   
4699  O O   . ASN B 56  ? 0.6138 1.0923 2.0604 0.2049  0.2007  0.0075  56  ASN B O   
4700  C CB  . ASN B 56  ? 0.5880 1.1033 2.0692 0.1595  0.2094  0.0734  56  ASN B CB  
4701  C CG  . ASN B 56  ? 0.6106 1.1439 2.0892 0.1442  0.2111  0.1008  56  ASN B CG  
4702  O OD1 . ASN B 56  ? 0.6377 1.1918 2.0960 0.1500  0.2122  0.1024  56  ASN B OD1 
4703  N ND2 . ASN B 56  ? 0.6012 1.1250 2.0997 0.1246  0.2103  0.1228  56  ASN B ND2 
4704  N N   . ILE B 57  ? 0.5811 1.0860 2.0587 0.1991  0.2100  0.0196  57  ILE B N   
4705  C CA  . ILE B 57  ? 0.5699 1.0382 2.0507 0.2109  0.2043  -0.0014 57  ILE B CA  
4706  C C   . ILE B 57  ? 0.5933 1.0640 2.0545 0.2336  0.2037  -0.0269 57  ILE B C   
4707  O O   . ILE B 57  ? 0.5846 1.0142 2.0418 0.2408  0.1959  -0.0439 57  ILE B O   
4708  C CB  . ILE B 57  ? 0.5439 1.0213 2.0457 0.2102  0.2078  0.0014  57  ILE B CB  
4709  C CG1 . ILE B 57  ? 0.5141 0.9769 2.0355 0.1874  0.2053  0.0219  57  ILE B CG1 
4710  C CG2 . ILE B 57  ? 0.5415 0.9889 2.0441 0.2266  0.2031  -0.0201 57  ILE B CG2 
4711  C CD1 . ILE B 57  ? 0.4966 0.9835 2.0388 0.1830  0.2099  0.0288  57  ILE B CD1 
4712  N N   . LYS B 58  ? 0.6120 1.1310 2.0613 0.2446  0.2116  -0.0302 58  LYS B N   
4713  C CA  . LYS B 58  ? 0.6237 1.1462 2.0521 0.2660  0.2103  -0.0558 58  LYS B CA  
4714  C C   . LYS B 58  ? 0.6229 1.1181 2.0348 0.2616  0.2018  -0.0609 58  LYS B C   
4715  O O   . LYS B 58  ? 0.6388 1.1028 2.0412 0.2732  0.1946  -0.0839 58  LYS B O   
4716  C CB  . LYS B 58  ? 0.6402 1.2259 2.0583 0.2787  0.2210  -0.0578 58  LYS B CB  
4717  C CG  . LYS B 58  ? 0.6515 1.2656 2.0835 0.2903  0.2284  -0.0615 58  LYS B CG  
4718  C CD  . LYS B 58  ? 0.6697 1.3562 2.0975 0.2971  0.2409  -0.0551 58  LYS B CD  
4719  C CE  . LYS B 58  ? 0.6954 1.4083 2.0971 0.3173  0.2429  -0.0757 58  LYS B CE  
4720  N NZ  . LYS B 58  ? 0.7029 1.4870 2.0988 0.3155  0.2549  -0.0604 58  LYS B NZ  
4721  N N   . GLU B 59  ? 0.6069 1.1131 2.0162 0.2449  0.2021  -0.0392 59  GLU B N   
4722  C CA  . GLU B 59  ? 0.6139 1.1027 2.0073 0.2413  0.1943  -0.0422 59  GLU B CA  
4723  C C   . GLU B 59  ? 0.6015 1.0315 2.0038 0.2330  0.1835  -0.0462 59  GLU B C   
4724  O O   . GLU B 59  ? 0.5837 0.9923 1.9745 0.2331  0.1752  -0.0557 59  GLU B O   
4725  C CB  . GLU B 59  ? 0.6146 1.1298 2.0040 0.2262  0.1969  -0.0152 59  GLU B CB  
4726  C CG  . GLU B 59  ? 0.6360 1.2142 2.0124 0.2330  0.2073  -0.0091 59  GLU B CG  
4727  C CD  . GLU B 59  ? 0.6448 1.2482 2.0144 0.2188  0.2090  0.0186  59  GLU B CD  
4728  O OE1 . GLU B 59  ? 0.6476 1.2192 2.0163 0.2084  0.2003  0.0266  59  GLU B OE1 
4729  O OE2 . GLU B 59  ? 0.6476 1.3041 2.0140 0.2182  0.2192  0.0332  59  GLU B OE2 
4730  N N   . GLY B 60  ? 0.5978 1.0058 2.0212 0.2256  0.1836  -0.0385 60  GLY B N   
4731  C CA  . GLY B 60  ? 0.5886 0.9455 2.0220 0.2187  0.1747  -0.0420 60  GLY B CA  
4732  C C   . GLY B 60  ? 0.6155 0.9441 2.0441 0.2336  0.1694  -0.0684 60  GLY B C   
4733  O O   . GLY B 60  ? 0.6595 0.9478 2.0907 0.2290  0.1610  -0.0742 60  GLY B O   
4734  N N   . GLY B 61  ? 0.6180 0.9676 2.0406 0.2513  0.1744  -0.0835 61  GLY B N   
4735  C CA  . GLY B 61  ? 0.6260 0.9489 2.0421 0.2674  0.1690  -0.1097 61  GLY B CA  
4736  C C   . GLY B 61  ? 0.6147 0.9264 2.0455 0.2764  0.1711  -0.1137 61  GLY B C   
4737  O O   . GLY B 61  ? 0.6380 0.9237 2.0660 0.2903  0.1665  -0.1333 61  GLY B O   
4738  N N   . TYR B 62  ? 0.5844 0.9159 2.0310 0.2684  0.1775  -0.0948 62  TYR B N   
4739  C CA  . TYR B 62  ? 0.5644 0.8916 2.0260 0.2758  0.1795  -0.0958 62  TYR B CA  
4740  C C   . TYR B 62  ? 0.5575 0.9198 2.0128 0.2980  0.1860  -0.1097 62  TYR B C   
4741  O O   . TYR B 62  ? 0.5525 0.9482 1.9936 0.3038  0.1905  -0.1143 62  TYR B O   
4742  C CB  . TYR B 62  ? 0.5454 0.8832 2.0254 0.2575  0.1829  -0.0719 62  TYR B CB  
4743  C CG  . TYR B 62  ? 0.5318 0.8381 2.0160 0.2377  0.1765  -0.0600 62  TYR B CG  
4744  C CD1 . TYR B 62  ? 0.5320 0.8505 2.0101 0.2251  0.1770  -0.0478 62  TYR B CD1 
4745  C CD2 . TYR B 62  ? 0.5303 0.7962 2.0239 0.2329  0.1698  -0.0610 62  TYR B CD2 
4746  C CE1 . TYR B 62  ? 0.5332 0.8236 2.0152 0.2096  0.1708  -0.0381 62  TYR B CE1 
4747  C CE2 . TYR B 62  ? 0.5287 0.7691 2.0260 0.2169  0.1642  -0.0518 62  TYR B CE2 
4748  C CZ  . TYR B 62  ? 0.5353 0.7874 2.0271 0.2058  0.1645  -0.0411 62  TYR B CZ  
4749  O OH  . TYR B 62  ? 0.5526 0.7810 2.0483 0.1921  0.1588  -0.0325 62  TYR B OH  
4750  N N   . ASN B 63  ? 0.5509 0.9049 2.0159 0.3116  0.1860  -0.1172 63  ASN B N   
4751  C CA  . ASN B 63  ? 0.5629 0.9501 2.0254 0.3349  0.1921  -0.1303 63  ASN B CA  
4752  C C   . ASN B 63  ? 0.5638 0.9725 2.0462 0.3367  0.1971  -0.1191 63  ASN B C   
4753  O O   . ASN B 63  ? 0.5794 1.0198 2.0635 0.3566  0.2024  -0.1280 63  ASN B O   
4754  C CB  . ASN B 63  ? 0.5819 0.9350 2.0341 0.3567  0.1853  -0.1568 63  ASN B CB  
4755  C CG  . ASN B 63  ? 0.5725 0.8783 2.0369 0.3586  0.1781  -0.1575 63  ASN B CG  
4756  O OD1 . ASN B 63  ? 0.5417 0.8428 2.0217 0.3445  0.1783  -0.1392 63  ASN B OD1 
4757  N ND2 . ASN B 63  ? 0.5939 0.8638 2.0511 0.3756  0.1711  -0.1784 63  ASN B ND2 
4758  N N   . THR B 64  ? 0.5480 0.9407 2.0457 0.3171  0.1948  -0.1010 64  THR B N   
4759  C CA  . THR B 64  ? 0.5426 0.9545 2.0598 0.3160  0.1980  -0.0902 64  THR B CA  
4760  C C   . THR B 64  ? 0.5105 0.9280 2.0405 0.2888  0.1988  -0.0676 64  THR B C   
4761  O O   . THR B 64  ? 0.5017 0.8959 2.0264 0.2728  0.1950  -0.0613 64  THR B O   
4762  C CB  . THR B 64  ? 0.5628 0.9349 2.0856 0.3279  0.1909  -0.0988 64  THR B CB  
4763  O OG1 . THR B 64  ? 0.6195 0.9861 2.1303 0.3534  0.1900  -0.1202 64  THR B OG1 
4764  C CG2 . THR B 64  ? 0.5517 0.9460 2.0935 0.3301  0.1933  -0.0895 64  THR B CG2 
4765  N N   . ILE B 65  ? 0.4939 0.9445 2.0414 0.2841  0.2034  -0.0561 65  ILE B N   
4766  C CA  . ILE B 65  ? 0.4590 0.9090 2.0216 0.2595  0.2023  -0.0373 65  ILE B CA  
4767  C C   . ILE B 65  ? 0.4363 0.8842 2.0160 0.2616  0.1997  -0.0356 65  ILE B C   
4768  O O   . ILE B 65  ? 0.4463 0.9042 2.0276 0.2818  0.2005  -0.0455 65  ILE B O   
4769  C CB  . ILE B 65  ? 0.4524 0.9500 2.0204 0.2450  0.2102  -0.0215 65  ILE B CB  
4770  C CG1 . ILE B 65  ? 0.4473 1.0032 2.0216 0.2587  0.2192  -0.0232 65  ILE B CG1 
4771  C CG2 . ILE B 65  ? 0.4560 0.9487 2.0070 0.2385  0.2109  -0.0189 65  ILE B CG2 
4772  C CD1 . ILE B 65  ? 0.4349 1.0401 2.0215 0.2402  0.2267  -0.0036 65  ILE B CD1 
4773  N N   . ARG B 66  ? 0.4047 0.8397 1.9968 0.2411  0.1960  -0.0232 66  ARG B N   
4774  C CA  . ARG B 66  ? 0.3796 0.8090 1.9866 0.2398  0.1920  -0.0211 66  ARG B CA  
4775  C C   . ARG B 66  ? 0.3577 0.8076 1.9814 0.2160  0.1929  -0.0057 66  ARG B C   
4776  O O   . ARG B 66  ? 0.3486 0.7862 1.9707 0.1982  0.1920  0.0029  66  ARG B O   
4777  C CB  . ARG B 66  ? 0.3752 0.7506 1.9756 0.2416  0.1836  -0.0271 66  ARG B CB  
4778  C CG  . ARG B 66  ? 0.3607 0.7241 1.9732 0.2393  0.1783  -0.0243 66  ARG B CG  
4779  C CD  . ARG B 66  ? 0.3417 0.7044 1.9664 0.2154  0.1758  -0.0131 66  ARG B CD  
4780  N NE  . ARG B 66  ? 0.3313 0.6701 1.9612 0.2134  0.1691  -0.0133 66  ARG B NE  
4781  C CZ  . ARG B 66  ? 0.3249 0.6817 1.9680 0.2128  0.1671  -0.0108 66  ARG B CZ  
4782  N NH1 . ARG B 66  ? 0.3282 0.7289 1.9828 0.2158  0.1712  -0.0085 66  ARG B NH1 
4783  N NH2 . ARG B 66  ? 0.3179 0.6514 1.9626 0.2098  0.1610  -0.0107 66  ARG B NH2 
4784  N N   . THR B 67  ? 0.3424 0.8236 1.9827 0.2163  0.1940  -0.0026 67  THR B N   
4785  C CA  . THR B 67  ? 0.3232 0.8300 1.9817 0.1939  0.1949  0.0106  67  THR B CA  
4786  C C   . THR B 67  ? 0.3085 0.8146 1.9818 0.1916  0.1891  0.0097  67  THR B C   
4787  O O   . THR B 67  ? 0.3110 0.8076 1.9806 0.2101  0.1865  0.0008  67  THR B O   
4788  C CB  . THR B 67  ? 0.3208 0.8845 1.9855 0.1956  0.2040  0.0160  67  THR B CB  
4789  O OG1 . THR B 67  ? 0.3184 0.8953 1.9850 0.2181  0.2039  0.0054  67  THR B OG1 
4790  C CG2 . THR B 67  ? 0.3347 0.9057 1.9820 0.2033  0.2102  0.0144  67  THR B CG2 
4791  N N   . TRP B 68  ? 0.2923 0.8078 1.9818 0.1691  0.1867  0.0189  68  TRP B N   
4792  C CA  . TRP B 68  ? 0.2780 0.7964 1.9817 0.1647  0.1805  0.0174  68  TRP B CA  
4793  C C   . TRP B 68  ? 0.2764 0.8505 2.0006 0.1586  0.1836  0.0226  68  TRP B C   
4794  O O   . TRP B 68  ? 0.2708 0.8557 2.0091 0.1522  0.1782  0.0218  68  TRP B O   
4795  C CB  . TRP B 68  ? 0.2647 0.7474 1.9715 0.1445  0.1735  0.0202  68  TRP B CB  
4796  C CG  . TRP B 68  ? 0.2682 0.7008 1.9575 0.1512  0.1699  0.0145  68  TRP B CG  
4797  C CD1 . TRP B 68  ? 0.2626 0.6669 1.9481 0.1567  0.1635  0.0081  68  TRP B CD1 
4798  C CD2 . TRP B 68  ? 0.2779 0.6857 1.9515 0.1521  0.1721  0.0154  68  TRP B CD2 
4799  N NE1 . TRP B 68  ? 0.2659 0.6302 1.9360 0.1601  0.1619  0.0053  68  TRP B NE1 
4800  C CE2 . TRP B 68  ? 0.2730 0.6379 1.9356 0.1574  0.1666  0.0090  68  TRP B CE2 
4801  C CE3 . TRP B 68  ? 0.2888 0.7089 1.9565 0.1486  0.1780  0.0216  68  TRP B CE3 
4802  C CZ2 . TRP B 68  ? 0.2778 0.6126 1.9251 0.1592  0.1665  0.0075  68  TRP B CZ2 
4803  C CZ3 . TRP B 68  ? 0.2932 0.6828 1.9444 0.1508  0.1776  0.0201  68  TRP B CZ3 
4804  C CH2 . TRP B 68  ? 0.2857 0.6332 1.9273 0.1561  0.1717  0.0126  68  TRP B CH2 
4805  N N   . SER B 69  ? 0.2779 0.8908 2.0035 0.1610  0.1921  0.0276  69  SER B N   
4806  C CA  . SER B 69  ? 0.2726 0.9415 2.0191 0.1500  0.1959  0.0356  69  SER B CA  
4807  C C   . SER B 69  ? 0.2845 0.9987 2.0273 0.1670  0.2060  0.0355  69  SER B C   
4808  O O   . SER B 69  ? 0.2898 0.9921 2.0146 0.1773  0.2107  0.0333  69  SER B O   
4809  C CB  . SER B 69  ? 0.2694 0.9358 2.0273 0.1193  0.1947  0.0483  69  SER B CB  
4810  O OG  . SER B 69  ? 0.2713 0.9931 2.0505 0.1057  0.1987  0.0578  69  SER B OG  
4811  N N   . GLN B 70  ? 0.2871 1.0567 2.0473 0.1707  0.2089  0.0368  70  GLN B N   
4812  C CA  . GLN B 70  ? 0.2988 1.1170 2.0570 0.1908  0.2184  0.0344  70  GLN B CA  
4813  C C   . GLN B 70  ? 0.3153 1.1617 2.0737 0.1750  0.2271  0.0472  70  GLN B C   
4814  O O   . GLN B 70  ? 0.3116 1.1687 2.0850 0.1465  0.2265  0.0611  70  GLN B O   
4815  C CB  . GLN B 70  ? 0.2914 1.1624 2.0686 0.2013  0.2186  0.0319  70  GLN B CB  
4816  C CG  . GLN B 70  ? 0.2798 1.1859 2.0841 0.1734  0.2159  0.0427  70  GLN B CG  
4817  C CD  . GLN B 70  ? 0.2669 1.1451 2.0792 0.1656  0.2042  0.0385  70  GLN B CD  
4818  O OE1 . GLN B 70  ? 0.2617 1.0870 2.0586 0.1759  0.1980  0.0303  70  GLN B OE1 
4819  N NE2 . GLN B 70  ? 0.2598 1.1757 2.0966 0.1460  0.2010  0.0441  70  GLN B NE2 
4820  N N   . TYR B 71  ? 0.3422 1.1973 2.0828 0.1935  0.2346  0.0424  71  TYR B N   
4821  C CA  . TYR B 71  ? 0.3630 1.2549 2.1022 0.1825  0.2441  0.0548  71  TYR B CA  
4822  C C   . TYR B 71  ? 0.3792 1.3498 2.1366 0.1866  0.2525  0.0593  71  TYR B C   
4823  O O   . TYR B 71  ? 0.3804 1.3736 2.1423 0.2100  0.2525  0.0473  71  TYR B O   
4824  C CB  . TYR B 71  ? 0.3816 1.2574 2.0933 0.2023  0.2487  0.0459  71  TYR B CB  
4825  C CG  . TYR B 71  ? 0.3897 1.1988 2.0828 0.1950  0.2426  0.0449  71  TYR B CG  
4826  C CD1 . TYR B 71  ? 0.3878 1.1657 2.0885 0.1664  0.2368  0.0582  71  TYR B CD1 
4827  C CD2 . TYR B 71  ? 0.4000 1.1796 2.0684 0.2169  0.2423  0.0302  71  TYR B CD2 
4828  C CE1 . TYR B 71  ? 0.3906 1.1117 2.0751 0.1613  0.2313  0.0573  71  TYR B CE1 
4829  C CE2 . TYR B 71  ? 0.4041 1.1278 2.0566 0.2100  0.2367  0.0294  71  TYR B CE2 
4830  C CZ  . TYR B 71  ? 0.3962 1.0919 2.0568 0.1827  0.2314  0.0434  71  TYR B CZ  
4831  O OH  . TYR B 71  ? 0.3930 1.0370 2.0397 0.1760  0.2257  0.0434  71  TYR B OH  
4832  N N   . SER B 72  ? 0.3906 1.4035 2.1593 0.1633  0.2595  0.0778  72  SER B N   
4833  C CA  . SER B 72  ? 0.3829 1.4778 2.1681 0.1644  0.2695  0.0851  72  SER B CA  
4834  C C   . SER B 72  ? 0.4065 1.5328 2.1722 0.1946  0.2796  0.0750  72  SER B C   
4835  O O   . SER B 72  ? 0.4174 1.5040 2.1577 0.2059  0.2795  0.0673  72  SER B O   
4836  C CB  . SER B 72  ? 0.3781 1.5023 2.1799 0.1284  0.2734  0.1099  72  SER B CB  
4837  O OG  . SER B 72  ? 0.3840 1.5036 2.1667 0.1249  0.2800  0.1191  72  SER B OG  
4838  N N   . GLU B 73  ? 0.4247 1.6264 2.2030 0.2066  0.2886  0.0750  73  GLU B N   
4839  C CA  . GLU B 73  ? 0.4431 1.6812 2.2041 0.2375  0.2985  0.0630  73  GLU B CA  
4840  C C   . GLU B 73  ? 0.4513 1.6861 2.1921 0.2284  0.3050  0.0723  73  GLU B C   
4841  O O   . GLU B 73  ? 0.4633 1.6824 2.1784 0.2532  0.3072  0.0567  73  GLU B O   
4842  C CB  . GLU B 73  ? 0.4525 1.7821 2.2338 0.2462  0.3082  0.0659  73  GLU B CB  
4843  C CG  . GLU B 73  ? 0.4758 1.8417 2.2398 0.2856  0.3171  0.0476  73  GLU B CG  
4844  C CD  . GLU B 73  ? 0.4863 1.9456 2.2718 0.2960  0.3267  0.0498  73  GLU B CD  
4845  O OE1 . GLU B 73  ? 0.4759 1.9714 2.2893 0.2678  0.3267  0.0683  73  GLU B OE1 
4846  O OE2 . GLU B 73  ? 0.5169 2.0125 2.2923 0.3314  0.3335  0.0327  73  GLU B OE2 
4847  N N   . ASN B 74  ? 0.4426 1.6928 2.1956 0.1926  0.3074  0.0978  74  ASN B N   
4848  C CA  . ASN B 74  ? 0.4414 1.6935 2.1779 0.1800  0.3134  0.1120  74  ASN B CA  
4849  C C   . ASN B 74  ? 0.4296 1.6009 2.1393 0.1868  0.3051  0.1009  74  ASN B C   
4850  O O   . ASN B 74  ? 0.4403 1.6131 2.1257 0.2001  0.3098  0.0959  74  ASN B O   
4851  C CB  . ASN B 74  ? 0.4396 1.7080 2.1961 0.1381  0.3146  0.1431  74  ASN B CB  
4852  C CG  . ASN B 74  ? 0.4285 1.7771 2.2150 0.1259  0.3221  0.1564  74  ASN B CG  
4853  O OD1 . ASN B 74  ? 0.4392 1.8548 2.2251 0.1476  0.3325  0.1497  74  ASN B OD1 
4854  N ND2 . ASN B 74  ? 0.4143 1.7584 2.2275 0.0920  0.3165  0.1739  74  ASN B ND2 
4855  N N   . GLN B 75  ? 0.4115 1.5170 2.1264 0.1779  0.2927  0.0967  75  GLN B N   
4856  C CA  . GLN B 75  ? 0.4111 1.4395 2.1043 0.1809  0.2839  0.0878  75  GLN B CA  
4857  C C   . GLN B 75  ? 0.4248 1.4370 2.0955 0.2184  0.2836  0.0605  75  GLN B C   
4858  O O   . GLN B 75  ? 0.4404 1.4273 2.0868 0.2271  0.2835  0.0538  75  GLN B O   
4859  C CB  . GLN B 75  ? 0.3858 1.3557 2.0919 0.1615  0.2716  0.0908  75  GLN B CB  
4860  C CG  . GLN B 75  ? 0.3773 1.3447 2.0999 0.1237  0.2699  0.1164  75  GLN B CG  
4861  C CD  . GLN B 75  ? 0.3589 1.2841 2.0995 0.1056  0.2585  0.1171  75  GLN B CD  
4862  O OE1 . GLN B 75  ? 0.3442 1.2799 2.0988 0.1128  0.2552  0.1072  75  GLN B OE1 
4863  N NE2 . GLN B 75  ? 0.3569 1.2358 2.0974 0.0828  0.2521  0.1287  75  GLN B NE2 
4864  N N   . LEU B 76  ? 0.4282 1.4569 2.1075 0.2405  0.2830  0.0452  76  LEU B N   
4865  C CA  . LEU B 76  ? 0.4488 1.4594 2.1098 0.2768  0.2816  0.0191  76  LEU B CA  
4866  C C   . LEU B 76  ? 0.4709 1.5173 2.1111 0.2947  0.2910  0.0115  76  LEU B C   
4867  O O   . LEU B 76  ? 0.4943 1.5060 2.1122 0.3169  0.2879  -0.0085 76  LEU B O   
4868  C CB  . LEU B 76  ? 0.4536 1.4900 2.1294 0.2988  0.2811  0.0073  76  LEU B CB  
4869  C CG  . LEU B 76  ? 0.4497 1.4327 2.1340 0.2990  0.2691  0.0017  76  LEU B CG  
4870  C CD1 . LEU B 76  ? 0.4348 1.4181 2.1413 0.2647  0.2653  0.0214  76  LEU B CD1 
4871  C CD2 . LEU B 76  ? 0.4565 1.4642 2.1485 0.3299  0.2690  -0.0132 76  LEU B CD2 
4872  N N   . LYS B 77  ? 0.4774 1.5964 2.1255 0.2863  0.3025  0.0262  77  LYS B N   
4873  C CA  . LYS B 77  ? 0.4998 1.6629 2.1282 0.3043  0.3125  0.0190  77  LYS B CA  
4874  C C   . LYS B 77  ? 0.5053 1.6235 2.1085 0.2961  0.3091  0.0203  77  LYS B C   
4875  O O   . LYS B 77  ? 0.5229 1.6372 2.1016 0.3193  0.3104  0.0014  77  LYS B O   
4876  C CB  . LYS B 77  ? 0.5032 1.7562 2.1459 0.2928  0.3259  0.0387  77  LYS B CB  
4877  C CG  . LYS B 77  ? 0.5065 1.8209 2.1707 0.3083  0.3315  0.0334  77  LYS B CG  
4878  C CD  . LYS B 77  ? 0.5133 1.9177 2.1955 0.2910  0.3445  0.0566  77  LYS B CD  
4879  C CE  . LYS B 77  ? 0.5099 1.9680 2.2203 0.2971  0.3473  0.0562  77  LYS B CE  
4880  N NZ  . LYS B 77  ? 0.5186 2.0578 2.2505 0.2723  0.3583  0.0827  77  LYS B NZ  
4881  N N   . LEU B 78  ? 0.4923 1.5775 2.1021 0.2635  0.3042  0.0420  78  LEU B N   
4882  C CA  . LEU B 78  ? 0.5033 1.5507 2.0918 0.2533  0.3009  0.0471  78  LEU B CA  
4883  C C   . LEU B 78  ? 0.5123 1.4883 2.0830 0.2717  0.2901  0.0221  78  LEU B C   
4884  O O   . LEU B 78  ? 0.5173 1.4800 2.0632 0.2844  0.2895  0.0098  78  LEU B O   
4885  C CB  . LEU B 78  ? 0.4855 1.5121 2.0890 0.2156  0.2972  0.0758  78  LEU B CB  
4886  C CG  . LEU B 78  ? 0.4859 1.4797 2.0711 0.2015  0.2941  0.0873  78  LEU B CG  
4887  C CD1 . LEU B 78  ? 0.5060 1.5482 2.0690 0.2121  0.3036  0.0886  78  LEU B CD1 
4888  C CD2 . LEU B 78  ? 0.4747 1.4590 2.0797 0.1655  0.2917  0.1172  78  LEU B CD2 
4889  N N   . VAL B 79  ? 0.5129 1.4473 2.0973 0.2728  0.2817  0.0149  79  VAL B N   
4890  C CA  . VAL B 79  ? 0.5378 1.4062 2.1092 0.2891  0.2714  -0.0069 79  VAL B CA  
4891  C C   . VAL B 79  ? 0.5726 1.4572 2.1268 0.3243  0.2746  -0.0332 79  VAL B C   
4892  O O   . VAL B 79  ? 0.5969 1.4482 2.1288 0.3355  0.2704  -0.0487 79  VAL B O   
4893  C CB  . VAL B 79  ? 0.5349 1.3680 2.1254 0.2854  0.2633  -0.0079 79  VAL B CB  
4894  C CG1 . VAL B 79  ? 0.5493 1.3173 2.1269 0.3030  0.2533  -0.0291 79  VAL B CG1 
4895  C CG2 . VAL B 79  ? 0.5195 1.3328 2.1260 0.2515  0.2591  0.0148  79  VAL B CG2 
4896  N N   . GLN B 80  ? 0.5918 1.5288 2.1571 0.3418  0.2815  -0.0389 80  GLN B N   
4897  C CA  . GLN B 80  ? 0.6220 1.5816 2.1732 0.3773  0.2852  -0.0644 80  GLN B CA  
4898  C C   . GLN B 80  ? 0.6548 1.6286 2.1798 0.3823  0.2895  -0.0709 80  GLN B C   
4899  O O   . GLN B 80  ? 0.6753 1.6190 2.1801 0.4045  0.2848  -0.0957 80  GLN B O   
4900  C CB  . GLN B 80  ? 0.6181 1.6531 2.1865 0.3899  0.2952  -0.0624 80  GLN B CB  
4901  C CG  . GLN B 80  ? 0.6442 1.6941 2.2038 0.4312  0.2968  -0.0916 80  GLN B CG  
4902  C CD  . GLN B 80  ? 0.6541 1.6372 2.2152 0.4480  0.2847  -0.1087 80  GLN B CD  
4903  O OE1 . GLN B 80  ? 0.6338 1.5963 2.2141 0.4367  0.2793  -0.0980 80  GLN B OE1 
4904  N NE2 . GLN B 80  ? 0.6842 1.6317 2.2248 0.4743  0.2799  -0.1352 80  GLN B NE2 
4905  N N   . GLU B 81  ? 0.6702 1.6896 2.1960 0.3607  0.2977  -0.0478 81  GLU B N   
4906  C CA  . GLU B 81  ? 0.7074 1.7575 2.2092 0.3655  0.3037  -0.0505 81  GLU B CA  
4907  C C   . GLU B 81  ? 0.7056 1.6914 2.1871 0.3575  0.2938  -0.0551 81  GLU B C   
4908  O O   . GLU B 81  ? 0.7265 1.7191 2.1834 0.3717  0.2945  -0.0703 81  GLU B O   
4909  C CB  . GLU B 81  ? 0.7210 1.8388 2.2319 0.3423  0.3152  -0.0199 81  GLU B CB  
4910  C CG  . GLU B 81  ? 0.7596 1.9297 2.2466 0.3512  0.3242  -0.0215 81  GLU B CG  
4911  C CD  . GLU B 81  ? 0.7709 2.0043 2.2660 0.3251  0.3352  0.0130  81  GLU B CD  
4912  O OE1 . GLU B 81  ? 0.7711 1.9744 2.2665 0.2968  0.3309  0.0364  81  GLU B OE1 
4913  O OE2 . GLU B 81  ? 0.7783 2.0902 2.2805 0.3327  0.3476  0.0177  81  GLU B OE2 
4914  N N   . SER B 82  ? 0.6795 1.6060 2.1714 0.3353  0.2843  -0.0429 82  SER B N   
4915  C CA  . SER B 82  ? 0.6716 1.5412 2.1476 0.3246  0.2751  -0.0437 82  SER B CA  
4916  C C   . SER B 82  ? 0.6789 1.5051 2.1359 0.3501  0.2670  -0.0765 82  SER B C   
4917  O O   . SER B 82  ? 0.6810 1.4867 2.1171 0.3506  0.2626  -0.0844 82  SER B O   
4918  C CB  . SER B 82  ? 0.6476 1.4669 2.1409 0.2986  0.2671  -0.0261 82  SER B CB  
4919  O OG  . SER B 82  ? 0.6412 1.4229 2.1468 0.3085  0.2605  -0.0393 82  SER B OG  
4920  N N   . GLY B 83  ? 0.6698 1.4817 2.1352 0.3707  0.2645  -0.0948 83  GLY B N   
4921  C CA  . GLY B 83  ? 0.6829 1.4444 2.1350 0.3931  0.2554  -0.1244 83  GLY B CA  
4922  C C   . GLY B 83  ? 0.6605 1.3555 2.1264 0.3855  0.2447  -0.1233 83  GLY B C   
4923  O O   . GLY B 83  ? 0.6765 1.3332 2.1395 0.4050  0.2378  -0.1445 83  GLY B O   
4924  N N   . LEU B 84  ? 0.6254 1.3079 2.1065 0.3576  0.2433  -0.0984 84  LEU B N   
4925  C CA  . LEU B 84  ? 0.6117 1.2340 2.1039 0.3479  0.2333  -0.0958 84  LEU B CA  
4926  C C   . LEU B 84  ? 0.6086 1.2345 2.1183 0.3613  0.2334  -0.0997 84  LEU B C   
4927  O O   . LEU B 84  ? 0.6232 1.3032 2.1455 0.3637  0.2417  -0.0917 84  LEU B O   
4928  C CB  . LEU B 84  ? 0.5877 1.2021 2.0907 0.3157  0.2324  -0.0694 84  LEU B CB  
4929  C CG  . LEU B 84  ? 0.5996 1.1929 2.0867 0.3018  0.2288  -0.0646 84  LEU B CG  
4930  C CD1 . LEU B 84  ? 0.5817 1.1825 2.0803 0.2726  0.2303  -0.0365 84  LEU B CD1 
4931  C CD2 . LEU B 84  ? 0.6098 1.1368 2.0889 0.3045  0.2172  -0.0790 84  LEU B CD2 
4932  N N   . LYS B 85  ? 0.6065 1.1766 2.1176 0.3688  0.2238  -0.1105 85  LYS B N   
4933  C CA  . LYS B 85  ? 0.5903 1.1549 2.1185 0.3780  0.2217  -0.1103 85  LYS B CA  
4934  C C   . LYS B 85  ? 0.5477 1.1041 2.0940 0.3512  0.2196  -0.0879 85  LYS B C   
4935  O O   . LYS B 85  ? 0.5489 1.0904 2.0932 0.3277  0.2180  -0.0754 85  LYS B O   
4936  C CB  . LYS B 85  ? 0.6156 1.1221 2.1379 0.3958  0.2119  -0.1281 85  LYS B CB  
4937  C CG  . LYS B 85  ? 0.6554 1.1512 2.1583 0.4206  0.2103  -0.1538 85  LYS B CG  
4938  C CD  . LYS B 85  ? 0.6754 1.2301 2.1754 0.4449  0.2194  -0.1656 85  LYS B CD  
4939  C CE  . LYS B 85  ? 0.7127 1.2509 2.1928 0.4703  0.2163  -0.1942 85  LYS B CE  
4940  N NZ  . LYS B 85  ? 0.7348 1.3338 2.2109 0.4949  0.2256  -0.2070 85  LYS B NZ  
4941  N N   . LEU B 86  ? 0.5201 1.0854 2.0838 0.3561  0.2188  -0.0840 86  LEU B N   
4942  C CA  . LEU B 86  ? 0.4890 1.0626 2.0717 0.3327  0.2182  -0.0644 86  LEU B CA  
4943  C C   . LEU B 86  ? 0.4695 1.0116 2.0621 0.3393  0.2106  -0.0663 86  LEU B C   
4944  O O   . LEU B 86  ? 0.4921 1.0378 2.0854 0.3640  0.2099  -0.0776 86  LEU B O   
4945  C CB  . LEU B 86  ? 0.4917 1.1358 2.0884 0.3298  0.2280  -0.0544 86  LEU B CB  
4946  C CG  . LEU B 86  ? 0.4822 1.1452 2.0964 0.2988  0.2293  -0.0324 86  LEU B CG  
4947  C CD1 . LEU B 86  ? 0.4884 1.2231 2.1184 0.2980  0.2385  -0.0238 86  LEU B CD1 
4948  C CD2 . LEU B 86  ? 0.4721 1.1004 2.0991 0.2871  0.2208  -0.0269 86  LEU B CD2 
4949  N N   . ILE B 87  ? 0.4401 0.9529 2.0400 0.3179  0.2049  -0.0550 87  ILE B N   
4950  C CA  . ILE B 87  ? 0.4290 0.9244 2.0406 0.3198  0.1987  -0.0524 87  ILE B CA  
4951  C C   . ILE B 87  ? 0.4147 0.9422 2.0454 0.2977  0.2003  -0.0367 87  ILE B C   
4952  O O   . ILE B 87  ? 0.4055 0.9134 2.0372 0.2745  0.1978  -0.0277 87  ILE B O   
4953  C CB  . ILE B 87  ? 0.4201 0.8513 2.0222 0.3154  0.1898  -0.0553 87  ILE B CB  
4954  C CG1 . ILE B 87  ? 0.4432 0.8427 2.0282 0.3366  0.1874  -0.0718 87  ILE B CG1 
4955  C CG2 . ILE B 87  ? 0.4060 0.8216 2.0197 0.3131  0.1836  -0.0492 87  ILE B CG2 
4956  C CD1 . ILE B 87  ? 0.4486 0.7879 2.0245 0.3301  0.1790  -0.0741 87  ILE B CD1 
4957  N N   . MET B 88  ? 0.4235 1.0005 2.0696 0.3047  0.2041  -0.0340 88  MET B N   
4958  C CA  . MET B 88  ? 0.4276 1.0490 2.0910 0.2828  0.2083  -0.0202 88  MET B CA  
4959  C C   . MET B 88  ? 0.4355 1.0417 2.1126 0.2639  0.2012  -0.0119 88  MET B C   
4960  O O   . MET B 88  ? 0.4460 1.0441 2.1279 0.2384  0.2000  -0.0022 88  MET B O   
4961  C CB  . MET B 88  ? 0.4428 1.1302 2.1196 0.2942  0.2154  -0.0196 88  MET B CB  
4962  C CG  . MET B 88  ? 0.4438 1.1769 2.1413 0.2682  0.2188  -0.0041 88  MET B CG  
4963  S SD  . MET B 88  ? 0.4877 1.3069 2.2009 0.2802  0.2288  -0.0024 88  MET B SD  
4964  C CE  . MET B 88  ? 0.4989 1.3321 2.1931 0.2849  0.2388  -0.0041 88  MET B CE  
4965  N N   . GLY B 89  ? 0.4385 1.0436 2.1227 0.2761  0.1962  -0.0152 89  GLY B N   
4966  C CA  . GLY B 89  ? 0.4250 1.0189 2.1208 0.2579  0.1893  -0.0086 89  GLY B CA  
4967  C C   . GLY B 89  ? 0.4088 1.0550 2.1267 0.2403  0.1915  0.0004  89  GLY B C   
4968  O O   . GLY B 89  ? 0.4112 1.0906 2.1347 0.2295  0.1983  0.0066  89  GLY B O   
4969  N N   . ILE B 90  ? 0.3817 1.0359 2.1124 0.2370  0.1852  0.0015  90  ILE B N   
4970  C CA  . ILE B 90  ? 0.3604 1.0692 2.1137 0.2262  0.1857  0.0070  90  ILE B CA  
4971  C C   . ILE B 90  ? 0.3404 1.0318 2.1030 0.2017  0.1777  0.0104  90  ILE B C   
4972  O O   . ILE B 90  ? 0.3300 0.9872 2.0856 0.2067  0.1707  0.0062  90  ILE B O   
4973  C CB  . ILE B 90  ? 0.3576 1.1017 2.1179 0.2515  0.1851  0.0024  90  ILE B CB  
4974  C CG1 . ILE B 90  ? 0.3729 1.1267 2.1220 0.2797  0.1921  -0.0041 90  ILE B CG1 
4975  C CG2 . ILE B 90  ? 0.3442 1.1499 2.1297 0.2395  0.1851  0.0078  90  ILE B CG2 
4976  C CD1 . ILE B 90  ? 0.3760 1.1730 2.1293 0.2739  0.2023  -0.0005 90  ILE B CD1 
4977  N N   . ASP B 91  ? 0.3368 1.0544 2.1160 0.1759  0.1786  0.0180  91  ASP B N   
4978  C CA  . ASP B 91  ? 0.3282 1.0290 2.1174 0.1511  0.1707  0.0195  91  ASP B CA  
4979  C C   . ASP B 91  ? 0.3212 1.0521 2.1255 0.1529  0.1638  0.0157  91  ASP B C   
4980  O O   . ASP B 91  ? 0.3047 1.0780 2.1301 0.1368  0.1628  0.0192  91  ASP B O   
4981  C CB  . ASP B 91  ? 0.3281 1.0369 2.1281 0.1231  0.1734  0.0293  91  ASP B CB  
4982  C CG  . ASP B 91  ? 0.3276 1.0169 2.1394 0.0970  0.1646  0.0297  91  ASP B CG  
4983  O OD1 . ASP B 91  ? 0.3235 0.9685 2.1247 0.0993  0.1578  0.0226  91  ASP B OD1 
4984  O OD2 . ASP B 91  ? 0.3331 1.0525 2.1651 0.0745  0.1644  0.0367  91  ASP B OD2 
4985  N N   . ILE B 92  ? 0.3313 1.0397 2.1244 0.1720  0.1588  0.0090  92  ILE B N   
4986  C CA  . ILE B 92  ? 0.3388 1.0634 2.1411 0.1731  0.1503  0.0052  92  ILE B CA  
4987  C C   . ILE B 92  ? 0.3519 1.0360 2.1509 0.1544  0.1426  0.0019  92  ILE B C   
4988  O O   . ILE B 92  ? 0.3429 0.9813 2.1244 0.1623  0.1407  -0.0008 92  ILE B O   
4989  C CB  . ILE B 92  ? 0.3334 1.0563 2.1247 0.2047  0.1492  0.0021  92  ILE B CB  
4990  C CG1 . ILE B 92  ? 0.3354 1.0982 2.1300 0.2268  0.1565  0.0033  92  ILE B CG1 
4991  C CG2 . ILE B 92  ? 0.3274 1.0634 2.1247 0.2067  0.1397  -0.0006 92  ILE B CG2 
4992  C CD1 . ILE B 92  ? 0.3252 1.1522 2.1429 0.2152  0.1601  0.0070  92  ILE B CD1 
4993  N N   . LYS B 93  ? 0.3815 1.0828 2.1982 0.1291  0.1381  0.0016  93  LYS B N   
4994  C CA  . LYS B 93  ? 0.4127 1.0759 2.2276 0.1105  0.1311  -0.0029 93  LYS B CA  
4995  C C   . LYS B 93  ? 0.4089 1.0525 2.2116 0.1246  0.1244  -0.0100 93  LYS B C   
4996  O O   . LYS B 93  ? 0.4178 1.0952 2.2273 0.1329  0.1200  -0.0128 93  LYS B O   
4997  C CB  . LYS B 93  ? 0.4523 1.1400 2.2902 0.0832  0.1251  -0.0046 93  LYS B CB  
4998  C CG  . LYS B 93  ? 0.4858 1.1860 2.3377 0.0617  0.1301  0.0046  93  LYS B CG  
4999  C CD  . LYS B 93  ? 0.5173 1.1683 2.3576 0.0528  0.1334  0.0096  93  LYS B CD  
5000  C CE  . LYS B 93  ? 0.5316 1.1920 2.3893 0.0253  0.1347  0.0190  93  LYS B CE  
5001  N NZ  . LYS B 93  ? 0.5130 1.2273 2.3839 0.0234  0.1425  0.0291  93  LYS B NZ  
5002  N N   . PRO B 94  ? 0.3926 0.9852 2.1778 0.1273  0.1235  -0.0122 94  PRO B N   
5003  C CA  . PRO B 94  ? 0.3887 0.9629 2.1603 0.1419  0.1187  -0.0163 94  PRO B CA  
5004  C C   . PRO B 94  ? 0.4032 0.9958 2.1828 0.1343  0.1092  -0.0240 94  PRO B C   
5005  O O   . PRO B 94  ? 0.3757 0.9722 2.1469 0.1491  0.1056  -0.0251 94  PRO B O   
5006  C CB  . PRO B 94  ? 0.3763 0.8960 2.1316 0.1397  0.1200  -0.0167 94  PRO B CB  
5007  C CG  . PRO B 94  ? 0.3746 0.8848 2.1315 0.1309  0.1268  -0.0114 94  PRO B CG  
5008  C CD  . PRO B 94  ? 0.3862 0.9391 2.1641 0.1162  0.1270  -0.0095 94  PRO B CD  
5009  N N   . GLU B 95  ? 0.4476 1.0511 2.2433 0.1109  0.1050  -0.0290 95  GLU B N   
5010  C CA  . GLU B 95  ? 0.4752 1.0872 2.2775 0.0999  0.0950  -0.0398 95  GLU B CA  
5011  C C   . GLU B 95  ? 0.4534 1.1218 2.2702 0.1025  0.0903  -0.0419 95  GLU B C   
5012  O O   . GLU B 95  ? 0.4739 1.1565 2.2934 0.0990  0.0816  -0.0514 95  GLU B O   
5013  C CB  . GLU B 95  ? 0.5134 1.1017 2.3250 0.0745  0.0912  -0.0458 95  GLU B CB  
5014  C CG  . GLU B 95  ? 0.5620 1.1714 2.3946 0.0544  0.0930  -0.0411 95  GLU B CG  
5015  C CD  . GLU B 95  ? 0.6071 1.1972 2.4376 0.0503  0.1023  -0.0291 95  GLU B CD  
5016  O OE1 . GLU B 95  ? 0.6182 1.1847 2.4307 0.0670  0.1089  -0.0237 95  GLU B OE1 
5017  O OE2 . GLU B 95  ? 0.6617 1.2607 2.5089 0.0293  0.1026  -0.0246 95  GLU B OE2 
5018  N N   . GLU B 96  ? 0.4310 1.1339 2.2562 0.1103  0.0960  -0.0338 96  GLU B N   
5019  C CA  . GLU B 96  ? 0.4332 1.1950 2.2763 0.1097  0.0917  -0.0353 96  GLU B CA  
5020  C C   . GLU B 96  ? 0.4158 1.1975 2.2495 0.1339  0.0879  -0.0354 96  GLU B C   
5021  O O   . GLU B 96  ? 0.4356 1.1876 2.2496 0.1537  0.0910  -0.0307 96  GLU B O   
5022  C CB  . GLU B 96  ? 0.4394 1.2360 2.2966 0.1093  0.0996  -0.0264 96  GLU B CB  
5023  C CG  . GLU B 96  ? 0.4499 1.2428 2.3226 0.0805  0.1014  -0.0247 96  GLU B CG  
5024  C CD  . GLU B 96  ? 0.4465 1.2507 2.3369 0.0544  0.0906  -0.0347 96  GLU B CD  
5025  O OE1 . GLU B 96  ? 0.4280 1.2853 2.3344 0.0535  0.0860  -0.0373 96  GLU B OE1 
5026  O OE2 . GLU B 96  ? 0.4173 1.1803 2.3059 0.0369  0.0862  -0.0406 96  GLU B OE2 
5027  N N   . ASP B 97  ? 0.3805 1.2130 2.2289 0.1314  0.0804  -0.0401 97  ASP B N   
5028  C CA  . ASP B 97  ? 0.3775 1.2348 2.2183 0.1534  0.0755  -0.0391 97  ASP B CA  
5029  C C   . ASP B 97  ? 0.3753 1.2551 2.2160 0.1782  0.0825  -0.0278 97  ASP B C   
5030  O O   . ASP B 97  ? 0.3857 1.3161 2.2449 0.1779  0.0830  -0.0262 97  ASP B O   
5031  C CB  . ASP B 97  ? 0.3843 1.2879 2.2394 0.1424  0.0640  -0.0493 97  ASP B CB  
5032  C CG  . ASP B 97  ? 0.3974 1.3401 2.2481 0.1650  0.0582  -0.0467 97  ASP B CG  
5033  O OD1 . ASP B 97  ? 0.3982 1.3236 2.2314 0.1906  0.0621  -0.0365 97  ASP B OD1 
5034  O OD2 . ASP B 97  ? 0.4031 1.3949 2.2687 0.1568  0.0493  -0.0543 97  ASP B OD2 
5035  N N   . TYR B 98  ? 0.3616 1.2042 2.1818 0.2002  0.0873  -0.0206 98  TYR B N   
5036  C CA  . TYR B 98  ? 0.3592 1.2111 2.1767 0.2256  0.0940  -0.0115 98  TYR B CA  
5037  C C   . TYR B 98  ? 0.3773 1.2869 2.2052 0.2423  0.0885  -0.0090 98  TYR B C   
5038  O O   . TYR B 98  ? 0.3838 1.3206 2.2181 0.2605  0.0930  -0.0038 98  TYR B O   
5039  C CB  . TYR B 98  ? 0.3553 1.1508 2.1489 0.2431  0.0977  -0.0058 98  TYR B CB  
5040  C CG  . TYR B 98  ? 0.3495 1.0882 2.1311 0.2279  0.1014  -0.0084 98  TYR B CG  
5041  C CD1 . TYR B 98  ? 0.3378 1.0672 2.1265 0.2100  0.1071  -0.0108 98  TYR B CD1 
5042  C CD2 . TYR B 98  ? 0.3421 1.0384 2.1054 0.2315  0.0990  -0.0073 98  TYR B CD2 
5043  C CE1 . TYR B 98  ? 0.3242 1.0035 2.1020 0.1978  0.1098  -0.0125 98  TYR B CE1 
5044  C CE2 . TYR B 98  ? 0.3347 0.9829 2.0881 0.2188  0.1020  -0.0098 98  TYR B CE2 
5045  C CZ  . TYR B 98  ? 0.3263 0.9652 2.0868 0.2026  0.1071  -0.0126 98  TYR B CZ  
5046  O OH  . TYR B 98  ? 0.3066 0.8988 2.0568 0.1918  0.1092  -0.0145 98  TYR B OH  
5047  N N   . GLY B 99  ? 0.3809 1.3122 2.2106 0.2369  0.0785  -0.0135 99  GLY B N   
5048  C CA  . GLY B 99  ? 0.3771 1.3636 2.2150 0.2536  0.0719  -0.0106 99  GLY B CA  
5049  C C   . GLY B 99  ? 0.3670 1.4153 2.2309 0.2349  0.0667  -0.0183 99  GLY B C   
5050  O O   . GLY B 99  ? 0.3531 1.4521 2.2252 0.2450  0.0595  -0.0178 99  GLY B O   
5051  N N   . ASP B 100 ? 0.3752 1.4191 2.2522 0.2070  0.0697  -0.0247 100 ASP B N   
5052  C CA  . ASP B 100 ? 0.3771 1.4773 2.2816 0.1859  0.0657  -0.0306 100 ASP B CA  
5053  C C   . ASP B 100 ? 0.3650 1.5057 2.2846 0.1964  0.0740  -0.0227 100 ASP B C   
5054  O O   . ASP B 100 ? 0.3574 1.4777 2.2777 0.1904  0.0839  -0.0188 100 ASP B O   
5055  C CB  . ASP B 100 ? 0.3758 1.4527 2.2891 0.1501  0.0641  -0.0396 100 ASP B CB  
5056  C CG  . ASP B 100 ? 0.3792 1.5098 2.3228 0.1242  0.0596  -0.0449 100 ASP B CG  
5057  O OD1 . ASP B 100 ? 0.3831 1.5560 2.3375 0.1192  0.0486  -0.0530 100 ASP B OD1 
5058  O OD2 . ASP B 100 ? 0.3827 1.5153 2.3394 0.1088  0.0670  -0.0403 100 ASP B OD2 
5059  N N   . PRO B 101 ? 0.3662 1.5702 2.2993 0.2121  0.0702  -0.0203 101 PRO B N   
5060  C CA  . PRO B 101 ? 0.3620 1.6117 2.3103 0.2253  0.0780  -0.0136 101 PRO B CA  
5061  C C   . PRO B 101 ? 0.3628 1.6184 2.3259 0.2030  0.0874  -0.0123 101 PRO B C   
5062  O O   . PRO B 101 ? 0.3633 1.6280 2.3267 0.2189  0.0978  -0.0059 101 PRO B O   
5063  C CB  . PRO B 101 ? 0.3619 1.6883 2.3314 0.2266  0.0683  -0.0162 101 PRO B CB  
5064  C CG  . PRO B 101 ? 0.3692 1.6810 2.3228 0.2357  0.0572  -0.0194 101 PRO B CG  
5065  C CD  . PRO B 101 ? 0.3710 1.6100 2.3056 0.2182  0.0577  -0.0244 101 PRO B CD  
5066  N N   . GLU B 102 ? 0.3687 1.6211 2.3445 0.1666  0.0835  -0.0182 102 GLU B N   
5067  C CA  . GLU B 102 ? 0.3732 1.6388 2.3663 0.1426  0.0913  -0.0145 102 GLU B CA  
5068  C C   . GLU B 102 ? 0.3690 1.5728 2.3427 0.1449  0.1022  -0.0093 102 GLU B C   
5069  O O   . GLU B 102 ? 0.3527 1.5734 2.3339 0.1425  0.1125  -0.0022 102 GLU B O   
5070  C CB  . GLU B 102 ? 0.3888 1.6705 2.4039 0.1027  0.0827  -0.0214 102 GLU B CB  
5071  C CG  . GLU B 102 ? 0.3997 1.7666 2.4448 0.0963  0.0776  -0.0220 102 GLU B CG  
5072  C CD  . GLU B 102 ? 0.4019 1.7940 2.4746 0.0547  0.0700  -0.0275 102 GLU B CD  
5073  O OE1 . GLU B 102 ? 0.4023 1.7437 2.4719 0.0286  0.0665  -0.0326 102 GLU B OE1 
5074  O OE2 . GLU B 102 ? 0.4079 1.8734 2.5065 0.0496  0.0674  -0.0264 102 GLU B OE2 
5075  N N   . PHE B 103 ? 0.3741 1.5111 2.3231 0.1501  0.1000  -0.0126 103 PHE B N   
5076  C CA  . PHE B 103 ? 0.3711 1.4479 2.3007 0.1523  0.1090  -0.0087 103 PHE B CA  
5077  C C   . PHE B 103 ? 0.3673 1.4404 2.2824 0.1872  0.1179  -0.0030 103 PHE B C   
5078  O O   . PHE B 103 ? 0.3781 1.4398 2.2891 0.1890  0.1281  0.0016  103 PHE B O   
5079  C CB  . PHE B 103 ? 0.3794 1.3914 2.2893 0.1465  0.1032  -0.0145 103 PHE B CB  
5080  C CG  . PHE B 103 ? 0.3938 1.3455 2.2843 0.1485  0.1117  -0.0106 103 PHE B CG  
5081  C CD1 . PHE B 103 ? 0.4022 1.3490 2.3004 0.1292  0.1188  -0.0059 103 PHE B CD1 
5082  C CD2 . PHE B 103 ? 0.4023 1.3068 2.2679 0.1704  0.1127  -0.0104 103 PHE B CD2 
5083  C CE1 . PHE B 103 ? 0.4117 1.3071 2.2918 0.1317  0.1259  -0.0024 103 PHE B CE1 
5084  C CE2 . PHE B 103 ? 0.4135 1.2669 2.2626 0.1719  0.1198  -0.0076 103 PHE B CE2 
5085  C CZ  . PHE B 103 ? 0.4175 1.2671 2.2735 0.1531  0.1262  -0.0041 103 PHE B CZ  
5086  N N   . VAL B 104 ? 0.3526 1.4343 2.2596 0.2155  0.1136  -0.0034 104 VAL B N   
5087  C CA  . VAL B 104 ? 0.3442 1.4282 2.2410 0.2507  0.1200  0.0010  104 VAL B CA  
5088  C C   . VAL B 104 ? 0.3390 1.4784 2.2538 0.2532  0.1289  0.0040  104 VAL B C   
5089  O O   . VAL B 104 ? 0.3419 1.4670 2.2471 0.2685  0.1385  0.0059  104 VAL B O   
5090  C CB  . VAL B 104 ? 0.3451 1.4458 2.2378 0.2782  0.1122  0.0019  104 VAL B CB  
5091  C CG1 . VAL B 104 ? 0.3582 1.4477 2.2385 0.3158  0.1178  0.0059  104 VAL B CG1 
5092  C CG2 . VAL B 104 ? 0.3409 1.3999 2.2183 0.2733  0.1031  -0.0002 104 VAL B CG2 
5093  N N   . LYS B 105 ? 0.3255 1.5302 2.2668 0.2372  0.1255  0.0039  105 LYS B N   
5094  C CA  . LYS B 105 ? 0.3109 1.5811 2.2733 0.2374  0.1332  0.0077  105 LYS B CA  
5095  C C   . LYS B 105 ? 0.2958 1.5518 2.2589 0.2163  0.1437  0.0118  105 LYS B C   
5096  O O   . LYS B 105 ? 0.2890 1.5625 2.2503 0.2320  0.1544  0.0149  105 LYS B O   
5097  C CB  . LYS B 105 ? 0.3093 1.6471 2.3007 0.2175  0.1254  0.0066  105 LYS B CB  
5098  C CG  . LYS B 105 ? 0.3129 1.7304 2.3300 0.2180  0.1323  0.0112  105 LYS B CG  
5099  C CD  . LYS B 105 ? 0.3150 1.8021 2.3622 0.1982  0.1235  0.0098  105 LYS B CD  
5100  C CE  . LYS B 105 ? 0.3199 1.8170 2.3642 0.2152  0.1108  0.0044  105 LYS B CE  
5101  N NZ  . LYS B 105 ? 0.3206 1.9055 2.3944 0.2129  0.1052  0.0041  105 LYS B NZ  
5102  N N   . ASP B 106 ? 0.2834 1.5091 2.2493 0.1814  0.1402  0.0117  106 ASP B N   
5103  C CA  . ASP B 106 ? 0.2720 1.4798 2.2378 0.1598  0.1489  0.0177  106 ASP B CA  
5104  C C   . ASP B 106 ? 0.2611 1.4143 2.1985 0.1819  0.1567  0.0177  106 ASP B C   
5105  O O   . ASP B 106 ? 0.2631 1.4256 2.1987 0.1832  0.1675  0.0228  106 ASP B O   
5106  C CB  . ASP B 106 ? 0.2695 1.4494 2.2432 0.1207  0.1422  0.0174  106 ASP B CB  
5107  C CG  . ASP B 106 ? 0.2764 1.5153 2.2819 0.0940  0.1356  0.0176  106 ASP B CG  
5108  O OD1 . ASP B 106 ? 0.2694 1.5730 2.2952 0.0912  0.1421  0.0246  106 ASP B OD1 
5109  O OD2 . ASP B 106 ? 0.2818 1.5037 2.2919 0.0763  0.1239  0.0102  106 ASP B OD2 
5110  N N   . SER B 107 ? 0.2480 1.3495 2.1643 0.1999  0.1511  0.0121  107 SER B N   
5111  C CA  . SER B 107 ? 0.2450 1.2899 2.1347 0.2194  0.1565  0.0110  107 SER B CA  
5112  C C   . SER B 107 ? 0.2434 1.3178 2.1298 0.2518  0.1648  0.0108  107 SER B C   
5113  O O   . SER B 107 ? 0.2488 1.3042 2.1228 0.2584  0.1735  0.0112  107 SER B O   
5114  C CB  . SER B 107 ? 0.2502 1.2382 2.1208 0.2289  0.1482  0.0064  107 SER B CB  
5115  O OG  . SER B 107 ? 0.2491 1.1944 2.1158 0.2010  0.1436  0.0053  107 SER B OG  
5116  N N   . GLU B 108 ? 0.2353 1.3591 2.1336 0.2719  0.1618  0.0096  108 GLU B N   
5117  C CA  . GLU B 108 ? 0.2366 1.3943 2.1347 0.3054  0.1687  0.0081  108 GLU B CA  
5118  C C   . GLU B 108 ? 0.2265 1.4359 2.1381 0.2963  0.1800  0.0117  108 GLU B C   
5119  O O   . GLU B 108 ? 0.2389 1.4444 2.1388 0.3163  0.1890  0.0091  108 GLU B O   
5120  C CB  . GLU B 108 ? 0.2410 1.4444 2.1518 0.3262  0.1616  0.0073  108 GLU B CB  
5121  C CG  . GLU B 108 ? 0.2478 1.4011 2.1416 0.3429  0.1518  0.0057  108 GLU B CG  
5122  C CD  . GLU B 108 ? 0.2557 1.4523 2.1593 0.3688  0.1450  0.0065  108 GLU B CD  
5123  O OE1 . GLU B 108 ? 0.2498 1.5090 2.1763 0.3570  0.1412  0.0079  108 GLU B OE1 
5124  O OE2 . GLU B 108 ? 0.2719 1.4388 2.1605 0.4006  0.1430  0.0062  108 GLU B OE2 
5125  N N   . ILE B 109 ? 0.2041 1.4633 2.1404 0.2662  0.1795  0.0174  109 ILE B N   
5126  C CA  . ILE B 109 ? 0.1951 1.5112 2.1471 0.2545  0.1903  0.0237  109 ILE B CA  
5127  C C   . ILE B 109 ? 0.1906 1.4627 2.1249 0.2437  0.1986  0.0267  109 ILE B C   
5128  O O   . ILE B 109 ? 0.1955 1.4906 2.1247 0.2587  0.2095  0.0270  109 ILE B O   
5129  C CB  . ILE B 109 ? 0.1862 1.5552 2.1688 0.2186  0.1865  0.0305  109 ILE B CB  
5130  C CG1 . ILE B 109 ? 0.1844 1.6093 2.1863 0.2305  0.1785  0.0273  109 ILE B CG1 
5131  C CG2 . ILE B 109 ? 0.1872 1.6081 2.1851 0.2007  0.1983  0.0404  109 ILE B CG2 
5132  C CD1 . ILE B 109 ? 0.1771 1.6281 2.2035 0.1942  0.1689  0.0296  109 ILE B CD1 
5133  N N   . GLU B 110 ? 0.1789 1.3910 2.1043 0.2182  0.1931  0.0284  110 GLU B N   
5134  C CA  . GLU B 110 ? 0.1766 1.3460 2.0867 0.2041  0.1993  0.0328  110 GLU B CA  
5135  C C   . GLU B 110 ? 0.1809 1.3177 2.0645 0.2371  0.2054  0.0256  110 GLU B C   
5136  O O   . GLU B 110 ? 0.1873 1.3381 2.0646 0.2402  0.2156  0.0282  110 GLU B O   
5137  C CB  . GLU B 110 ? 0.1715 1.2770 2.0749 0.1775  0.1909  0.0336  110 GLU B CB  
5138  C CG  . GLU B 110 ? 0.1750 1.2276 2.0586 0.1690  0.1959  0.0370  110 GLU B CG  
5139  C CD  . GLU B 110 ? 0.1807 1.2688 2.0704 0.1552  0.2070  0.0481  110 GLU B CD  
5140  O OE1 . GLU B 110 ? 0.1809 1.3322 2.0949 0.1401  0.2104  0.0563  110 GLU B OE1 
5141  O OE2 . GLU B 110 ? 0.1869 1.2407 2.0563 0.1605  0.2125  0.0489  110 GLU B OE2 
5142  N N   . LEU B 111 ? 0.1776 1.2716 2.0460 0.2610  0.1986  0.0166  111 LEU B N   
5143  C CA  . LEU B 111 ? 0.1854 1.2437 2.0300 0.2922  0.2023  0.0085  111 LEU B CA  
5144  C C   . LEU B 111 ? 0.1895 1.3072 2.0393 0.3163  0.2121  0.0057  111 LEU B C   
5145  O O   . LEU B 111 ? 0.1970 1.3150 2.0359 0.3192  0.2211  0.0048  111 LEU B O   
5146  C CB  . LEU B 111 ? 0.1930 1.2081 2.0261 0.3141  0.1929  0.0018  111 LEU B CB  
5147  C CG  . LEU B 111 ? 0.2130 1.1801 2.0216 0.3442  0.1946  -0.0070 111 LEU B CG  
5148  C CD1 . LEU B 111 ? 0.2168 1.1526 2.0091 0.3347  0.2015  -0.0081 111 LEU B CD1 
5149  C CD2 . LEU B 111 ? 0.2172 1.1240 2.0131 0.3511  0.1843  -0.0089 111 LEU B CD2 
5150  N N   . LYS B 112 ? 0.1905 1.3627 2.0577 0.3326  0.2103  0.0044  112 LYS B N   
5151  C CA  . LYS B 112 ? 0.2011 1.4377 2.0764 0.3578  0.2191  0.0010  112 LYS B CA  
5152  C C   . LYS B 112 ? 0.2007 1.4770 2.0806 0.3398  0.2313  0.0075  112 LYS B C   
5153  O O   . LYS B 112 ? 0.2138 1.5161 2.0866 0.3629  0.2405  0.0016  112 LYS B O   
5154  C CB  . LYS B 112 ? 0.1981 1.5011 2.0984 0.3675  0.2153  0.0024  112 LYS B CB  
5155  C CG  . LYS B 112 ? 0.2074 1.4871 2.1012 0.4009  0.2062  -0.0048 112 LYS B CG  
5156  C CD  . LYS B 112 ? 0.2052 1.5507 2.1230 0.4116  0.2012  -0.0027 112 LYS B CD  
5157  C CE  . LYS B 112 ? 0.2113 1.5226 2.1222 0.4328  0.1893  -0.0051 112 LYS B CE  
5158  N NZ  . LYS B 112 ? 0.2049 1.5804 2.1405 0.4324  0.1829  -0.0009 112 LYS B NZ  
5159  N N   . ARG B 113 ? 0.1882 1.4704 2.0802 0.2993  0.2311  0.0197  113 ARG B N   
5160  C CA  . ARG B 113 ? 0.1897 1.5084 2.0866 0.2794  0.2421  0.0295  113 ARG B CA  
5161  C C   . ARG B 113 ? 0.1995 1.4690 2.0676 0.2877  0.2478  0.0253  113 ARG B C   
5162  O O   . ARG B 113 ? 0.2091 1.5153 2.0727 0.2952  0.2590  0.0263  113 ARG B O   
5163  C CB  . ARG B 113 ? 0.1788 1.4994 2.0927 0.2331  0.2392  0.0443  113 ARG B CB  
5164  C CG  . ARG B 113 ? 0.1831 1.5527 2.1063 0.2118  0.2509  0.0583  113 ARG B CG  
5165  C CD  . ARG B 113 ? 0.1762 1.5492 2.1205 0.1660  0.2464  0.0734  113 ARG B CD  
5166  N NE  . ARG B 113 ? 0.1732 1.4627 2.1023 0.1481  0.2383  0.0738  113 ARG B NE  
5167  C CZ  . ARG B 113 ? 0.1787 1.4263 2.0890 0.1400  0.2424  0.0791  113 ARG B CZ  
5168  N NH1 . ARG B 113 ? 0.1881 1.4707 2.0932 0.1422  0.2547  0.0870  113 ARG B NH1 
5169  N NH2 . ARG B 113 ? 0.1755 1.3476 2.0719 0.1297  0.2340  0.0766  113 ARG B NH2 
5170  N N   . VAL B 114 ? 0.2035 1.3925 2.0526 0.2847  0.2399  0.0209  114 VAL B N   
5171  C CA  . VAL B 114 ? 0.2235 1.3624 2.0461 0.2892  0.2435  0.0170  114 VAL B CA  
5172  C C   . VAL B 114 ? 0.2528 1.3965 2.0596 0.3311  0.2480  0.0014  114 VAL B C   
5173  O O   . VAL B 114 ? 0.2671 1.4323 2.0634 0.3404  0.2576  -0.0013 114 VAL B O   
5174  C CB  . VAL B 114 ? 0.2187 1.2752 2.0278 0.2760  0.2332  0.0160  114 VAL B CB  
5175  C CG1 . VAL B 114 ? 0.2280 1.2315 2.0102 0.2793  0.2357  0.0118  114 VAL B CG1 
5176  C CG2 . VAL B 114 ? 0.2053 1.2596 2.0317 0.2369  0.2280  0.0289  114 VAL B CG2 
5177  N N   . LEU B 115 ? 0.2719 1.4019 2.0789 0.3573  0.2410  -0.0085 115 LEU B N   
5178  C CA  . LEU B 115 ? 0.3048 1.4256 2.0967 0.3984  0.2426  -0.0246 115 LEU B CA  
5179  C C   . LEU B 115 ? 0.3211 1.5170 2.1194 0.4154  0.2545  -0.0280 115 LEU B C   
5180  O O   . LEU B 115 ? 0.3415 1.5305 2.1222 0.4408  0.2596  -0.0410 115 LEU B O   
5181  C CB  . LEU B 115 ? 0.3146 1.4182 2.1110 0.4210  0.2328  -0.0303 115 LEU B CB  
5182  C CG  . LEU B 115 ? 0.3170 1.3412 2.1015 0.4109  0.2215  -0.0293 115 LEU B CG  
5183  C CD1 . LEU B 115 ? 0.3264 1.3444 2.1170 0.4329  0.2125  -0.0318 115 LEU B CD1 
5184  C CD2 . LEU B 115 ? 0.3302 1.2864 2.0877 0.4175  0.2213  -0.0381 115 LEU B CD2 
5185  N N   . ASN B 116 ? 0.3176 1.5857 2.1417 0.3994  0.2588  -0.0163 116 ASN B N   
5186  C CA  . ASN B 116 ? 0.3315 1.6850 2.1680 0.4153  0.2698  -0.0176 116 ASN B CA  
5187  C C   . ASN B 116 ? 0.3455 1.7176 2.1687 0.4093  0.2818  -0.0161 116 ASN B C   
5188  O O   . ASN B 116 ? 0.3561 1.7952 2.1838 0.4269  0.2922  -0.0198 116 ASN B O   
5189  C CB  . ASN B 116 ? 0.3167 1.7378 2.1857 0.3928  0.2698  -0.0034 116 ASN B CB  
5190  C CG  . ASN B 116 ? 0.3298 1.8454 2.2151 0.4109  0.2805  -0.0044 116 ASN B CG  
5191  O OD1 . ASN B 116 ? 0.3448 1.8832 2.2328 0.4481  0.2795  -0.0167 116 ASN B OD1 
5192  N ND2 . ASN B 116 ? 0.3296 1.9017 2.2263 0.3855  0.2907  0.0091  116 ASN B ND2 
5193  N N   . TYR B 117 ? 0.3493 1.6674 2.1570 0.3839  0.2805  -0.0097 117 TYR B N   
5194  C CA  . TYR B 117 ? 0.3654 1.6905 2.1550 0.3821  0.2903  -0.0098 117 TYR B CA  
5195  C C   . TYR B 117 ? 0.3801 1.6195 2.1395 0.3915  0.2844  -0.0221 117 TYR B C   
5196  O O   . TYR B 117 ? 0.3981 1.6374 2.1375 0.4030  0.2908  -0.0300 117 TYR B O   
5197  C CB  . TYR B 117 ? 0.3536 1.7100 2.1551 0.3400  0.2961  0.0134  117 TYR B CB  
5198  C CG  . TYR B 117 ? 0.3372 1.6328 2.1415 0.3039  0.2863  0.0260  117 TYR B CG  
5199  C CD1 . TYR B 117 ? 0.3402 1.5655 2.1212 0.2952  0.2827  0.0251  117 TYR B CD1 
5200  C CD2 . TYR B 117 ? 0.3197 1.6301 2.1504 0.2788  0.2804  0.0379  117 TYR B CD2 
5201  C CE1 . TYR B 117 ? 0.3252 1.4965 2.1088 0.2648  0.2739  0.0353  117 TYR B CE1 
5202  C CE2 . TYR B 117 ? 0.3085 1.5642 2.1414 0.2474  0.2714  0.0472  117 TYR B CE2 
5203  C CZ  . TYR B 117 ? 0.3103 1.4961 2.1197 0.2414  0.2683  0.0459  117 TYR B CZ  
5204  O OH  . TYR B 117 ? 0.2994 1.4321 2.1111 0.2135  0.2593  0.0535  117 TYR B OH  
5205  N N   . ALA B 118 ? 0.3756 1.5456 2.1320 0.3860  0.2722  -0.0239 118 ALA B N   
5206  C CA  . ALA B 118 ? 0.3895 1.4782 2.1202 0.3919  0.2657  -0.0341 118 ALA B CA  
5207  C C   . ALA B 118 ? 0.4223 1.5019 2.1354 0.4333  0.2671  -0.0565 118 ALA B C   
5208  O O   . ALA B 118 ? 0.4364 1.4821 2.1266 0.4400  0.2680  -0.0664 118 ALA B O   
5209  C CB  . ALA B 118 ? 0.3761 1.4039 2.1100 0.3820  0.2531  -0.0318 118 ALA B CB  
5210  N N   . LYS B 119 ? 0.4386 1.5505 2.1638 0.4609  0.2665  -0.0645 119 LYS B N   
5211  C CA  . LYS B 119 ? 0.4725 1.5660 2.1848 0.5030  0.2644  -0.0863 119 LYS B CA  
5212  C C   . LYS B 119 ? 0.5063 1.6271 2.2017 0.5215  0.2741  -0.1004 119 LYS B C   
5213  O O   . LYS B 119 ? 0.5299 1.6231 2.2099 0.5546  0.2717  -0.1215 119 LYS B O   
5214  C CB  . LYS B 119 ? 0.4712 1.6080 2.2042 0.5260  0.2628  -0.0880 119 LYS B CB  
5215  C CG  . LYS B 119 ? 0.4641 1.7010 2.2181 0.5269  0.2739  -0.0814 119 LYS B CG  
5216  C CD  . LYS B 119 ? 0.4650 1.7394 2.2391 0.5520  0.2704  -0.0840 119 LYS B CD  
5217  C CE  . LYS B 119 ? 0.4618 1.8366 2.2568 0.5572  0.2811  -0.0799 119 LYS B CE  
5218  N NZ  . LYS B 119 ? 0.4635 1.8658 2.2787 0.5770  0.2751  -0.0801 119 LYS B NZ  
5219  N N   . LYS B 120 ? 0.5131 1.6869 2.2110 0.5000  0.2847  -0.0886 120 LYS B N   
5220  C CA  . LYS B 120 ? 0.5424 1.7537 2.2244 0.5148  0.2951  -0.0995 120 LYS B CA  
5221  C C   . LYS B 120 ? 0.5630 1.7157 2.2184 0.5029  0.2927  -0.1035 120 LYS B C   
5222  O O   . LYS B 120 ? 0.5799 1.7552 2.2179 0.5142  0.2999  -0.1138 120 LYS B O   
5223  C CB  . LYS B 120 ? 0.5280 1.8309 2.2267 0.4962  0.3081  -0.0815 120 LYS B CB  
5224  C CG  . LYS B 120 ? 0.5149 1.8818 2.2440 0.4995  0.3102  -0.0733 120 LYS B CG  
5225  C CD  . LYS B 120 ? 0.5130 1.9822 2.2580 0.4914  0.3246  -0.0610 120 LYS B CD  
5226  C CE  . LYS B 120 ? 0.4881 1.9744 2.2466 0.4433  0.3274  -0.0326 120 LYS B CE  
5227  N NZ  . LYS B 120 ? 0.4844 2.0690 2.2582 0.4341  0.3414  -0.0190 120 LYS B NZ  
5228  N N   . TYR B 121 ? 0.5700 1.6511 2.2223 0.4803  0.2825  -0.0957 121 TYR B N   
5229  C CA  . TYR B 121 ? 0.5929 1.6207 2.2228 0.4655  0.2795  -0.0968 121 TYR B CA  
5230  C C   . TYR B 121 ? 0.6023 1.5458 2.2185 0.4808  0.2671  -0.1135 121 TYR B C   
5231  O O   . TYR B 121 ? 0.5903 1.4901 2.2157 0.4694  0.2582  -0.1058 121 TYR B O   
5232  C CB  . TYR B 121 ? 0.5769 1.6076 2.2174 0.4224  0.2803  -0.0700 121 TYR B CB  
5233  C CG  . TYR B 121 ? 0.5931 1.7100 2.2480 0.4092  0.2928  -0.0538 121 TYR B CG  
5234  C CD1 . TYR B 121 ? 0.6176 1.7755 2.2583 0.4105  0.3030  -0.0535 121 TYR B CD1 
5235  C CD2 . TYR B 121 ? 0.5937 1.7549 2.2768 0.3962  0.2945  -0.0388 121 TYR B CD2 
5236  C CE1 . TYR B 121 ? 0.6281 1.8676 2.2824 0.3978  0.3149  -0.0366 121 TYR B CE1 
5237  C CE2 . TYR B 121 ? 0.6061 1.8477 2.3043 0.3826  0.3057  -0.0230 121 TYR B CE2 
5238  C CZ  . TYR B 121 ? 0.6279 1.9091 2.3120 0.3830  0.3164  -0.0209 121 TYR B CZ  
5239  O OH  . TYR B 121 ? 0.6342 1.9978 2.3344 0.3685  0.3279  -0.0030 121 TYR B OH  
5240  N N   . ASP B 122 ? 0.6253 1.5490 2.2195 0.5059  0.2667  -0.1362 122 ASP B N   
5241  C CA  . ASP B 122 ? 0.6342 1.4817 2.2151 0.5236  0.2553  -0.1546 122 ASP B CA  
5242  C C   . ASP B 122 ? 0.6186 1.4022 2.1852 0.4981  0.2483  -0.1498 122 ASP B C   
5243  O O   . ASP B 122 ? 0.6333 1.3526 2.1884 0.5084  0.2388  -0.1637 122 ASP B O   
5244  C CB  . ASP B 122 ? 0.6705 1.5250 2.2378 0.5641  0.2564  -0.1832 122 ASP B CB  
5245  C CG  . ASP B 122 ? 0.6908 1.5448 2.2327 0.5715  0.2595  -0.2008 122 ASP B CG  
5246  O OD1 . ASP B 122 ? 0.6709 1.5015 2.2015 0.5452  0.2583  -0.1922 122 ASP B OD1 
5247  O OD2 . ASP B 122 ? 0.7138 1.5912 2.2468 0.6054  0.2625  -0.2245 122 ASP B OD2 
5248  N N   . CYS B 123 ? 0.5894 1.3902 2.1582 0.4653  0.2526  -0.1296 123 CYS B N   
5249  C CA  . CYS B 123 ? 0.5693 1.3132 2.1286 0.4396  0.2457  -0.1219 123 CYS B CA  
5250  C C   . CYS B 123 ? 0.5442 1.2381 2.1162 0.4271  0.2361  -0.1125 123 CYS B C   
5251  O O   . CYS B 123 ? 0.5451 1.1770 2.1073 0.4201  0.2275  -0.1159 123 CYS B O   
5252  C CB  . CYS B 123 ? 0.5497 1.3241 2.1078 0.4101  0.2523  -0.1026 123 CYS B CB  
5253  S SG  . CYS B 123 ? 0.5179 1.3469 2.1044 0.3827  0.2587  -0.0736 123 CYS B SG  
5254  N N   . ILE B 124 ? 0.5260 1.2501 2.1197 0.4247  0.2374  -0.1012 124 ILE B N   
5255  C CA  . ILE B 124 ? 0.5065 1.1930 2.1128 0.4139  0.2288  -0.0920 124 ILE B CA  
5256  C C   . ILE B 124 ? 0.5233 1.1571 2.1218 0.4389  0.2201  -0.1080 124 ILE B C   
5257  O O   . ILE B 124 ? 0.5463 1.1994 2.1471 0.4682  0.2213  -0.1200 124 ILE B O   
5258  C CB  . ILE B 124 ? 0.4917 1.2300 2.1227 0.4083  0.2320  -0.0787 124 ILE B CB  
5259  C CG1 . ILE B 124 ? 0.4709 1.2591 2.1125 0.3800  0.2399  -0.0607 124 ILE B CG1 
5260  C CG2 . ILE B 124 ? 0.4809 1.1812 2.1225 0.4014  0.2224  -0.0720 124 ILE B CG2 
5261  C CD1 . ILE B 124 ? 0.4527 1.2909 2.1202 0.3704  0.2419  -0.0476 124 ILE B CD1 
5262  N N   . ILE B 125 ? 0.5120 1.0809 2.1026 0.4270  0.2113  -0.1071 125 ILE B N   
5263  C CA  . ILE B 125 ? 0.5308 1.0436 2.1135 0.4466  0.2024  -0.1200 125 ILE B CA  
5264  C C   . ILE B 125 ? 0.5183 0.9975 2.1119 0.4367  0.1944  -0.1077 125 ILE B C   
5265  O O   . ILE B 125 ? 0.5369 0.9672 2.1254 0.4494  0.1866  -0.1142 125 ILE B O   
5266  C CB  . ILE B 125 ? 0.5441 1.0096 2.1060 0.4453  0.1985  -0.1328 125 ILE B CB  
5267  C CG1 . ILE B 125 ? 0.5214 0.9596 2.0807 0.4131  0.1957  -0.1197 125 ILE B CG1 
5268  C CG2 . ILE B 125 ? 0.5610 1.0617 2.1100 0.4598  0.2057  -0.1479 125 ILE B CG2 
5269  C CD1 . ILE B 125 ? 0.5398 0.9309 2.0804 0.4107  0.1905  -0.1315 125 ILE B CD1 
5270  N N   . THR B 126 ? 0.4888 0.9942 2.0972 0.4144  0.1961  -0.0904 126 THR B N   
5271  C CA  . THR B 126 ? 0.4785 0.9638 2.0978 0.4081  0.1892  -0.0799 126 THR B CA  
5272  C C   . THR B 126 ? 0.4498 0.9771 2.0865 0.3850  0.1922  -0.0642 126 THR B C   
5273  O O   . THR B 126 ? 0.4411 0.9853 2.0779 0.3638  0.1969  -0.0581 126 THR B O   
5274  C CB  . THR B 126 ? 0.4792 0.8993 2.0883 0.3957  0.1813  -0.0785 126 THR B CB  
5275  O OG1 . THR B 126 ? 0.5075 0.8861 2.1034 0.4169  0.1769  -0.0927 126 THR B OG1 
5276  C CG2 . THR B 126 ? 0.4682 0.8736 2.0878 0.3864  0.1750  -0.0662 126 THR B CG2 
5277  N N   . TYR B 127 ? 0.4414 0.9827 2.0923 0.3886  0.1885  -0.0574 127 TYR B N   
5278  C CA  . TYR B 127 ? 0.4140 0.9903 2.0822 0.3664  0.1891  -0.0443 127 TYR B CA  
5279  C C   . TYR B 127 ? 0.4075 0.9422 2.0759 0.3508  0.1807  -0.0371 127 TYR B C   
5280  O O   . TYR B 127 ? 0.4167 0.9209 2.0812 0.3649  0.1744  -0.0386 127 TYR B O   
5281  C CB  . TYR B 127 ? 0.4061 1.0398 2.0919 0.3802  0.1911  -0.0423 127 TYR B CB  
5282  C CG  . TYR B 127 ? 0.4050 1.0974 2.0961 0.3893  0.2009  -0.0460 127 TYR B CG  
5283  C CD1 . TYR B 127 ? 0.4252 1.1227 2.1072 0.4200  0.2041  -0.0594 127 TYR B CD1 
5284  C CD2 . TYR B 127 ? 0.3862 1.1304 2.0920 0.3673  0.2068  -0.0363 127 TYR B CD2 
5285  C CE1 . TYR B 127 ? 0.4272 1.1829 2.1134 0.4297  0.2137  -0.0635 127 TYR B CE1 
5286  C CE2 . TYR B 127 ? 0.3876 1.1897 2.0985 0.3745  0.2164  -0.0379 127 TYR B CE2 
5287  C CZ  . TYR B 127 ? 0.4078 1.2179 2.1085 0.4066  0.2203  -0.0518 127 TYR B CZ  
5288  O OH  . TYR B 127 ? 0.4154 1.2866 2.1202 0.4158  0.2304  -0.0544 127 TYR B OH  
5289  N N   . LEU B 128 ? 0.3924 0.9265 2.0655 0.3219  0.1805  -0.0290 128 LEU B N   
5290  C CA  . LEU B 128 ? 0.3821 0.8890 2.0581 0.3067  0.1732  -0.0228 128 LEU B CA  
5291  C C   . LEU B 128 ? 0.3755 0.9275 2.0711 0.2970  0.1720  -0.0160 128 LEU B C   
5292  O O   . LEU B 128 ? 0.3861 0.9767 2.0931 0.2828  0.1766  -0.0122 128 LEU B O   
5293  C CB  . LEU B 128 ? 0.3737 0.8474 2.0421 0.2832  0.1726  -0.0202 128 LEU B CB  
5294  C CG  . LEU B 128 ? 0.3872 0.8205 2.0370 0.2896  0.1734  -0.0271 128 LEU B CG  
5295  C CD1 . LEU B 128 ? 0.3726 0.7809 2.0179 0.2655  0.1723  -0.0228 128 LEU B CD1 
5296  C CD2 . LEU B 128 ? 0.4069 0.7997 2.0470 0.3077  0.1676  -0.0322 128 LEU B CD2 
5297  N N   . VAL B 129 ? 0.3814 0.9301 2.0814 0.3038  0.1655  -0.0140 129 VAL B N   
5298  C CA  . VAL B 129 ? 0.3832 0.9813 2.1017 0.3008  0.1638  -0.0099 129 VAL B CA  
5299  C C   . VAL B 129 ? 0.3689 0.9656 2.0957 0.2726  0.1591  -0.0054 129 VAL B C   
5300  O O   . VAL B 129 ? 0.3496 0.9888 2.0936 0.2590  0.1591  -0.0027 129 VAL B O   
5301  C CB  . VAL B 129 ? 0.4082 1.0084 2.1261 0.3276  0.1592  -0.0104 129 VAL B CB  
5302  C CG1 . VAL B 129 ? 0.4113 1.0255 2.1387 0.3205  0.1517  -0.0051 129 VAL B CG1 
5303  C CG2 . VAL B 129 ? 0.4194 1.0631 2.1442 0.3514  0.1642  -0.0140 129 VAL B CG2 
5304  N N   . ILE B 130 ? 0.3811 0.9297 2.0968 0.2632  0.1549  -0.0053 130 ILE B N   
5305  C CA  . ILE B 130 ? 0.3822 0.9258 2.1044 0.2389  0.1500  -0.0034 130 ILE B CA  
5306  C C   . ILE B 130 ? 0.3922 0.8831 2.1000 0.2292  0.1492  -0.0043 130 ILE B C   
5307  O O   . ILE B 130 ? 0.4109 0.8705 2.1042 0.2431  0.1506  -0.0060 130 ILE B O   
5308  C CB  . ILE B 130 ? 0.3920 0.9477 2.1194 0.2435  0.1425  -0.0026 130 ILE B CB  
5309  C CG1 . ILE B 130 ? 0.3896 0.9497 2.1262 0.2188  0.1371  -0.0035 130 ILE B CG1 
5310  C CG2 . ILE B 130 ? 0.4015 0.9178 2.1130 0.2606  0.1391  -0.0016 130 ILE B CG2 
5311  C CD1 . ILE B 130 ? 0.3901 0.9789 2.1350 0.2219  0.1299  -0.0039 130 ILE B CD1 
5312  N N   . ASN B 131 ? 0.4007 0.8818 2.1130 0.2061  0.1465  -0.0037 131 ASN B N   
5313  C CA  . ASN B 131 ? 0.4085 0.8432 2.1086 0.1972  0.1455  -0.0045 131 ASN B CA  
5314  C C   . ASN B 131 ? 0.3900 0.8092 2.0916 0.1855  0.1385  -0.0062 131 ASN B C   
5315  O O   . ASN B 131 ? 0.3576 0.7956 2.0720 0.1699  0.1352  -0.0074 131 ASN B O   
5316  C CB  . ASN B 131 ? 0.4345 0.8666 2.1355 0.1829  0.1503  -0.0025 131 ASN B CB  
5317  C CG  . ASN B 131 ? 0.4597 0.8465 2.1483 0.1754  0.1491  -0.0031 131 ASN B CG  
5318  O OD1 . ASN B 131 ? 0.4980 0.8558 2.1727 0.1877  0.1489  -0.0053 131 ASN B OD1 
5319  N ND2 . ASN B 131 ? 0.4439 0.8238 2.1383 0.1555  0.1479  -0.0009 131 ASN B ND2 
5320  N N   . GLU B 132 ? 0.4067 0.7911 2.0948 0.1930  0.1361  -0.0067 132 GLU B N   
5321  C CA  . GLU B 132 ? 0.4412 0.8067 2.1268 0.1840  0.1306  -0.0086 132 GLU B CA  
5322  C C   . GLU B 132 ? 0.4254 0.8229 2.1220 0.1808  0.1253  -0.0106 132 GLU B C   
5323  O O   . GLU B 132 ? 0.4537 0.8546 2.1577 0.1649  0.1214  -0.0151 132 GLU B O   
5324  C CB  . GLU B 132 ? 0.4664 0.8081 2.1516 0.1662  0.1305  -0.0106 132 GLU B CB  
5325  C CG  . GLU B 132 ? 0.5037 0.8168 2.1776 0.1689  0.1350  -0.0088 132 GLU B CG  
5326  C CD  . GLU B 132 ? 0.5366 0.8201 2.2066 0.1557  0.1339  -0.0098 132 GLU B CD  
5327  O OE1 . GLU B 132 ? 0.4930 0.7535 2.1559 0.1568  0.1308  -0.0114 132 GLU B OE1 
5328  O OE2 . GLU B 132 ? 0.5765 0.8612 2.2505 0.1451  0.1362  -0.0079 132 GLU B OE2 
5329  N N   . PRO B 133 ? 0.4036 0.8245 2.1012 0.1964  0.1240  -0.0080 133 PRO B N   
5330  C CA  . PRO B 133 ? 0.3957 0.8444 2.1002 0.1951  0.1177  -0.0099 133 PRO B CA  
5331  C C   . PRO B 133 ? 0.4008 0.8267 2.0959 0.1916  0.1133  -0.0115 133 PRO B C   
5332  O O   . PRO B 133 ? 0.3995 0.7967 2.0813 0.2012  0.1145  -0.0067 133 PRO B O   
5333  C CB  . PRO B 133 ? 0.3985 0.8696 2.1026 0.2165  0.1178  -0.0044 133 PRO B CB  
5334  C CG  . PRO B 133 ? 0.4076 0.8451 2.0990 0.2305  0.1227  -0.0002 133 PRO B CG  
5335  C CD  . PRO B 133 ? 0.4089 0.8300 2.1007 0.2173  0.1277  -0.0037 133 PRO B CD  
5336  N N   . GLN B 134 ? 0.3844 0.8252 2.0872 0.1776  0.1080  -0.0189 134 GLN B N   
5337  C CA  . GLN B 134 ? 0.3859 0.8104 2.0806 0.1735  0.1040  -0.0227 134 GLN B CA  
5338  C C   . GLN B 134 ? 0.3658 0.8165 2.0572 0.1846  0.0993  -0.0205 134 GLN B C   
5339  O O   . GLN B 134 ? 0.3623 0.8508 2.0632 0.1866  0.0959  -0.0220 134 GLN B O   
5340  C CB  . GLN B 134 ? 0.4044 0.8233 2.1070 0.1539  0.1007  -0.0336 134 GLN B CB  
5341  C CG  . GLN B 134 ? 0.4375 0.8406 2.1314 0.1514  0.0971  -0.0395 134 GLN B CG  
5342  C CD  . GLN B 134 ? 0.4672 0.8320 2.1481 0.1554  0.1015  -0.0340 134 GLN B CD  
5343  O OE1 . GLN B 134 ? 0.4994 0.8398 2.1813 0.1485  0.1047  -0.0339 134 GLN B OE1 
5344  N NE2 . GLN B 134 ? 0.4728 0.8336 2.1418 0.1657  0.1013  -0.0288 134 GLN B NE2 
5345  N N   . THR B 135 ? 0.3538 0.7847 2.0315 0.1908  0.0990  -0.0162 135 THR B N   
5346  C CA  . THR B 135 ? 0.3604 0.8064 2.0299 0.2039  0.0960  -0.0087 135 THR B CA  
5347  C C   . THR B 135 ? 0.3422 0.8289 2.0176 0.1998  0.0890  -0.0168 135 THR B C   
5348  O O   . THR B 135 ? 0.3552 0.8739 2.0326 0.2105  0.0860  -0.0119 135 THR B O   
5349  C CB  . THR B 135 ? 0.3871 0.7997 2.0428 0.2046  0.0980  -0.0036 135 THR B CB  
5350  O OG1 . THR B 135 ? 0.4105 0.7963 2.0623 0.2135  0.1029  0.0055  135 THR B OG1 
5351  C CG2 . THR B 135 ? 0.4001 0.8267 2.0459 0.2124  0.0948  0.0034  135 THR B CG2 
5352  N N   . ASP B 136 ? 0.3341 0.8205 2.0124 0.1852  0.0857  -0.0302 136 ASP B N   
5353  C CA  . ASP B 136 ? 0.3275 0.8516 2.0108 0.1807  0.0781  -0.0410 136 ASP B CA  
5354  C C   . ASP B 136 ? 0.3220 0.8805 2.0215 0.1777  0.0751  -0.0445 136 ASP B C   
5355  O O   . ASP B 136 ? 0.3173 0.9160 2.0206 0.1801  0.0687  -0.0485 136 ASP B O   
5356  C CB  . ASP B 136 ? 0.3204 0.8337 2.0045 0.1664  0.0747  -0.0570 136 ASP B CB  
5357  C CG  . ASP B 136 ? 0.3129 0.8620 2.0063 0.1578  0.0659  -0.0733 136 ASP B CG  
5358  O OD1 . ASP B 136 ? 0.3148 0.8768 2.0240 0.1480  0.0636  -0.0789 136 ASP B OD1 
5359  O OD2 . ASP B 136 ? 0.3097 0.8759 1.9949 0.1609  0.0613  -0.0800 136 ASP B OD2 
5360  N N   . HIS B 137 ? 0.3139 0.8593 2.0229 0.1721  0.0799  -0.0426 137 HIS B N   
5361  C CA  . HIS B 137 ? 0.3094 0.8882 2.0350 0.1685  0.0787  -0.0439 137 HIS B CA  
5362  C C   . HIS B 137 ? 0.3131 0.9195 2.0370 0.1887  0.0793  -0.0322 137 HIS B C   
5363  O O   . HIS B 137 ? 0.3158 0.9658 2.0517 0.1892  0.0749  -0.0347 137 HIS B O   
5364  C CB  . HIS B 137 ? 0.3029 0.8627 2.0373 0.1590  0.0848  -0.0423 137 HIS B CB  
5365  C CG  . HIS B 137 ? 0.3027 0.9022 2.0555 0.1535  0.0837  -0.0434 137 HIS B CG  
5366  N ND1 . HIS B 137 ? 0.2954 0.9072 2.0525 0.1635  0.0898  -0.0340 137 HIS B ND1 
5367  C CD2 . HIS B 137 ? 0.3063 0.9402 2.0744 0.1404  0.0767  -0.0530 137 HIS B CD2 
5368  C CE1 . HIS B 137 ? 0.2993 0.9534 2.0749 0.1553  0.0873  -0.0370 137 HIS B CE1 
5369  N NE2 . HIS B 137 ? 0.3011 0.9691 2.0840 0.1407  0.0789  -0.0482 137 HIS B NE2 
5370  N N   . ILE B 138 ? 0.3090 0.8893 2.0193 0.2051  0.0845  -0.0197 138 ILE B N   
5371  C CA  . ILE B 138 ? 0.3087 0.9077 2.0168 0.2265  0.0849  -0.0077 138 ILE B CA  
5372  C C   . ILE B 138 ? 0.3151 0.9474 2.0193 0.2336  0.0773  -0.0063 138 ILE B C   
5373  O O   . ILE B 138 ? 0.3089 0.9838 2.0216 0.2417  0.0733  -0.0047 138 ILE B O   
5374  C CB  . ILE B 138 ? 0.3108 0.8676 2.0056 0.2405  0.0910  0.0040  138 ILE B CB  
5375  C CG1 . ILE B 138 ? 0.3064 0.8391 2.0055 0.2344  0.0979  0.0012  138 ILE B CG1 
5376  C CG2 . ILE B 138 ? 0.3204 0.8904 2.0114 0.2647  0.0901  0.0170  138 ILE B CG2 
5377  C CD1 . ILE B 138 ? 0.3156 0.8075 2.0026 0.2474  0.1032  0.0097  138 ILE B CD1 
5378  N N   . HIS B 139 ? 0.3202 0.9366 2.0119 0.2297  0.0753  -0.0077 139 HIS B N   
5379  C CA  . HIS B 139 ? 0.3360 0.9846 2.0216 0.2343  0.0683  -0.0077 139 HIS B CA  
5380  C C   . HIS B 139 ? 0.3370 1.0346 2.0374 0.2251  0.0608  -0.0214 139 HIS B C   
5381  O O   . HIS B 139 ? 0.3507 1.0894 2.0510 0.2353  0.0549  -0.0180 139 HIS B O   
5382  C CB  . HIS B 139 ? 0.3388 0.9644 2.0109 0.2273  0.0682  -0.0113 139 HIS B CB  
5383  C CG  . HIS B 139 ? 0.3522 1.0110 2.0148 0.2331  0.0620  -0.0103 139 HIS B CG  
5384  N ND1 . HIS B 139 ? 0.3638 1.0225 2.0122 0.2493  0.0627  0.0084  139 HIS B ND1 
5385  C CD2 . HIS B 139 ? 0.3532 1.0471 2.0182 0.2250  0.0546  -0.0256 139 HIS B CD2 
5386  C CE1 . HIS B 139 ? 0.3713 1.0670 2.0128 0.2512  0.0565  0.0057  139 HIS B CE1 
5387  N NE2 . HIS B 139 ? 0.3681 1.0860 2.0192 0.2369  0.0513  -0.0162 139 HIS B NE2 
5388  N N   . SER B 140 ? 0.3255 1.0189 2.0391 0.2053  0.0605  -0.0363 140 SER B N   
5389  C CA  . SER B 140 ? 0.3175 1.0521 2.0465 0.1919  0.0524  -0.0516 140 SER B CA  
5390  C C   . SER B 140 ? 0.3237 1.0965 2.0694 0.1961  0.0519  -0.0474 140 SER B C   
5391  O O   . SER B 140 ? 0.3338 1.1515 2.0925 0.1890  0.0442  -0.0568 140 SER B O   
5392  C CB  . SER B 140 ? 0.3058 1.0179 2.0436 0.1685  0.0516  -0.0678 140 SER B CB  
5393  O OG  . SER B 140 ? 0.3004 1.0455 2.0476 0.1559  0.0416  -0.0852 140 SER B OG  
5394  N N   . VAL B 141 ? 0.3197 1.0769 2.0663 0.2068  0.0598  -0.0348 141 VAL B N   
5395  C CA  . VAL B 141 ? 0.3194 1.1162 2.0817 0.2132  0.0601  -0.0307 141 VAL B CA  
5396  C C   . VAL B 141 ? 0.3263 1.1316 2.0794 0.2419  0.0616  -0.0145 141 VAL B C   
5397  O O   . VAL B 141 ? 0.3100 1.1543 2.0747 0.2529  0.0608  -0.0102 141 VAL B O   
5398  C CB  . VAL B 141 ? 0.3106 1.0937 2.0858 0.2015  0.0674  -0.0320 141 VAL B CB  
5399  C CG1 . VAL B 141 ? 0.3014 1.0768 2.0876 0.1729  0.0645  -0.0463 141 VAL B CG1 
5400  C CG2 . VAL B 141 ? 0.3128 1.0468 2.0747 0.2123  0.0769  -0.0220 141 VAL B CG2 
5401  N N   . THR B 142 ? 0.3332 1.1021 2.0662 0.2531  0.0634  -0.0054 142 THR B N   
5402  C CA  . THR B 142 ? 0.3440 1.1132 2.0651 0.2787  0.0630  0.0113  142 THR B CA  
5403  C C   . THR B 142 ? 0.3486 1.0768 2.0648 0.2920  0.0713  0.0215  142 THR B C   
5404  O O   . THR B 142 ? 0.3346 1.0605 2.0615 0.2883  0.0765  0.0171  142 THR B O   
5405  C CB  . THR B 142 ? 0.3438 1.1711 2.0738 0.2930  0.0563  0.0155  142 THR B CB  
5406  O OG1 . THR B 142 ? 0.3441 1.1899 2.0914 0.2942  0.0599  0.0129  142 THR B OG1 
5407  C CG2 . THR B 142 ? 0.3374 1.2091 2.0716 0.2809  0.0467  0.0042  142 THR B CG2 
5408  N N   . GLY B 143 ? 0.3678 1.0650 2.0677 0.3072  0.0722  0.0354  143 GLY B N   
5409  C CA  . GLY B 143 ? 0.3803 1.0378 2.0744 0.3225  0.0782  0.0451  143 GLY B CA  
5410  C C   . GLY B 143 ? 0.3937 1.0791 2.0987 0.3428  0.0785  0.0492  143 GLY B C   
5411  O O   . GLY B 143 ? 0.4056 1.0653 2.1106 0.3528  0.0841  0.0507  143 GLY B O   
5412  N N   . LYS B 144 ? 0.3927 1.1328 2.1069 0.3494  0.0721  0.0500  144 LYS B N   
5413  C CA  . LYS B 144 ? 0.4057 1.1794 2.1316 0.3702  0.0717  0.0539  144 LYS B CA  
5414  C C   . LYS B 144 ? 0.3939 1.1889 2.1371 0.3587  0.0768  0.0410  144 LYS B C   
5415  O O   . LYS B 144 ? 0.4081 1.2058 2.1572 0.3743  0.0814  0.0424  144 LYS B O   
5416  C CB  . LYS B 144 ? 0.4136 1.2433 2.1445 0.3818  0.0627  0.0596  144 LYS B CB  
5417  C CG  . LYS B 144 ? 0.4173 1.2841 2.1604 0.4073  0.0616  0.0653  144 LYS B CG  
5418  C CD  . LYS B 144 ? 0.4318 1.3349 2.1723 0.4277  0.0525  0.0784  144 LYS B CD  
5419  C CE  . LYS B 144 ? 0.4349 1.3852 2.1909 0.4507  0.0505  0.0813  144 LYS B CE  
5420  N NZ  . LYS B 144 ? 0.4486 1.3625 2.2036 0.4711  0.0573  0.0853  144 LYS B NZ  
5421  N N   . ALA B 145 ? 0.3766 1.1895 2.1286 0.3318  0.0756  0.0286  145 ALA B N   
5422  C CA  . ALA B 145 ? 0.3618 1.1951 2.1309 0.3170  0.0803  0.0186  145 ALA B CA  
5423  C C   . ALA B 145 ? 0.3640 1.1489 2.1265 0.3161  0.0898  0.0181  145 ALA B C   
5424  O O   . ALA B 145 ? 0.3629 1.1638 2.1359 0.3190  0.0956  0.0159  145 ALA B O   
5425  C CB  . ALA B 145 ? 0.3470 1.1990 2.1255 0.2874  0.0759  0.0064  145 ALA B CB  
5426  N N   . PHE B 146 ? 0.3697 1.0989 2.1146 0.3125  0.0914  0.0204  146 PHE B N   
5427  C CA  . PHE B 146 ? 0.3681 1.0506 2.1057 0.3089  0.0994  0.0187  146 PHE B CA  
5428  C C   . PHE B 146 ? 0.4002 1.0705 2.1333 0.3364  0.1033  0.0251  146 PHE B C   
5429  O O   . PHE B 146 ? 0.4188 1.0964 2.1585 0.3393  0.1095  0.0209  146 PHE B O   
5430  C CB  . PHE B 146 ? 0.3484 0.9800 2.0704 0.2966  0.0992  0.0187  146 PHE B CB  
5431  C CG  . PHE B 146 ? 0.3343 0.9176 2.0476 0.2945  0.1064  0.0175  146 PHE B CG  
5432  C CD1 . PHE B 146 ? 0.3162 0.8948 2.0355 0.2751  0.1110  0.0095  146 PHE B CD1 
5433  C CD2 . PHE B 146 ? 0.3424 0.8853 2.0418 0.3116  0.1080  0.0249  146 PHE B CD2 
5434  C CE1 . PHE B 146 ? 0.3159 0.8544 2.0265 0.2742  0.1171  0.0086  146 PHE B CE1 
5435  C CE2 . PHE B 146 ? 0.3391 0.8406 2.0307 0.3098  0.1137  0.0222  146 PHE B CE2 
5436  C CZ  . PHE B 146 ? 0.3312 0.8325 2.0279 0.2917  0.1183  0.0140  146 PHE B CZ  
5437  N N   . VAL B 147 ? 0.4236 1.0759 2.1459 0.3569  0.0996  0.0353  147 VAL B N   
5438  C CA  . VAL B 147 ? 0.4649 1.0998 2.1832 0.3839  0.1022  0.0402  147 VAL B CA  
5439  C C   . VAL B 147 ? 0.4472 1.1347 2.1822 0.3963  0.1043  0.0360  147 VAL B C   
5440  O O   . VAL B 147 ? 0.4352 1.1166 2.1719 0.4046  0.1107  0.0307  147 VAL B O   
5441  C CB  . VAL B 147 ? 0.5115 1.1243 2.2186 0.4057  0.0966  0.0541  147 VAL B CB  
5442  C CG1 . VAL B 147 ? 0.5322 1.1927 2.2452 0.4124  0.0888  0.0616  147 VAL B CG1 
5443  C CG2 . VAL B 147 ? 0.5340 1.1257 2.2387 0.4344  0.0984  0.0572  147 VAL B CG2 
5444  N N   . ASP B 148 ? 0.4363 1.1791 2.1839 0.3968  0.0989  0.0376  148 ASP B N   
5445  C CA  . ASP B 148 ? 0.4297 1.2297 2.1947 0.4104  0.0998  0.0353  148 ASP B CA  
5446  C C   . ASP B 148 ? 0.4146 1.2288 2.1899 0.3953  0.1082  0.0252  148 ASP B C   
5447  O O   . ASP B 148 ? 0.4395 1.2723 2.2213 0.4124  0.1135  0.0229  148 ASP B O   
5448  C CB  . ASP B 148 ? 0.4160 1.2736 2.1929 0.4083  0.0916  0.0378  148 ASP B CB  
5449  C CG  . ASP B 148 ? 0.4309 1.2903 2.2003 0.4336  0.0839  0.0505  148 ASP B CG  
5450  O OD1 . ASP B 148 ? 0.4452 1.2724 2.2058 0.4594  0.0852  0.0577  148 ASP B OD1 
5451  O OD2 . ASP B 148 ? 0.4260 1.3180 2.1982 0.4273  0.0761  0.0532  148 ASP B OD2 
5452  N N   . LEU B 149 ? 0.3830 1.1886 2.1598 0.3640  0.1096  0.0195  149 LEU B N   
5453  C CA  . LEU B 149 ? 0.3646 1.1781 2.1495 0.3480  0.1176  0.0127  149 LEU B CA  
5454  C C   . LEU B 149 ? 0.3688 1.1389 2.1402 0.3622  0.1250  0.0116  149 LEU B C   
5455  O O   . LEU B 149 ? 0.3738 1.1673 2.1521 0.3695  0.1318  0.0081  149 LEU B O   
5456  C CB  . LEU B 149 ? 0.3503 1.1508 2.1369 0.3136  0.1166  0.0082  149 LEU B CB  
5457  C CG  . LEU B 149 ? 0.3399 1.1607 2.1395 0.2928  0.1233  0.0039  149 LEU B CG  
5458  C CD1 . LEU B 149 ? 0.3364 1.2273 2.1593 0.2887  0.1214  0.0032  149 LEU B CD1 
5459  C CD2 . LEU B 149 ? 0.3368 1.1264 2.1339 0.2623  0.1226  0.0004  149 LEU B CD2 
5460  N N   . MET B 150 ? 0.3611 1.0713 2.1136 0.3662  0.1234  0.0141  150 MET B N   
5461  C CA  . MET B 150 ? 0.3718 1.0365 2.1107 0.3782  0.1288  0.0116  150 MET B CA  
5462  C C   . MET B 150 ? 0.3848 1.0644 2.1256 0.4115  0.1305  0.0111  150 MET B C   
5463  O O   . MET B 150 ? 0.3826 1.0648 2.1231 0.4194  0.1375  0.0043  150 MET B O   
5464  C CB  . MET B 150 ? 0.3871 0.9888 2.1075 0.3776  0.1253  0.0158  150 MET B CB  
5465  C CG  . MET B 150 ? 0.3703 0.9479 2.0860 0.3481  0.1246  0.0145  150 MET B CG  
5466  S SD  . MET B 150 ? 0.3602 0.9258 2.0759 0.3269  0.1327  0.0063  150 MET B SD  
5467  C CE  . MET B 150 ? 0.3530 0.9797 2.0901 0.3055  0.1319  0.0045  150 MET B CE  
5468  N N   . ASN B 151 ? 0.3975 1.0870 2.1395 0.4326  0.1240  0.0182  151 ASN B N   
5469  C CA  . ASN B 151 ? 0.4195 1.1261 2.1653 0.4665  0.1245  0.0179  151 ASN B CA  
5470  C C   . ASN B 151 ? 0.4044 1.1740 2.1674 0.4683  0.1308  0.0108  151 ASN B C   
5471  O O   . ASN B 151 ? 0.4172 1.1906 2.1798 0.4894  0.1361  0.0044  151 ASN B O   
5472  C CB  . ASN B 151 ? 0.4408 1.1559 2.1875 0.4869  0.1156  0.0289  151 ASN B CB  
5473  C CG  . ASN B 151 ? 0.4712 1.1195 2.1998 0.4961  0.1109  0.0369  151 ASN B CG  
5474  O OD1 . ASN B 151 ? 0.4783 1.1168 2.2019 0.4891  0.1045  0.0474  151 ASN B OD1 
5475  N ND2 . ASN B 151 ? 0.4961 1.0990 2.2149 0.5117  0.1138  0.0322  151 ASN B ND2 
5476  N N   . THR B 152 ? 0.3805 1.2002 2.1590 0.4457  0.1303  0.0115  152 THR B N   
5477  C CA  . THR B 152 ? 0.3684 1.2559 2.1666 0.4444  0.1356  0.0075  152 THR B CA  
5478  C C   . THR B 152 ? 0.3690 1.2511 2.1650 0.4339  0.1460  0.0002  152 THR B C   
5479  O O   . THR B 152 ? 0.3699 1.2888 2.1733 0.4503  0.1524  -0.0042 152 THR B O   
5480  C CB  . THR B 152 ? 0.3429 1.2775 2.1578 0.4187  0.1309  0.0102  152 THR B CB  
5481  O OG1 . THR B 152 ? 0.3465 1.2916 2.1618 0.4370  0.1218  0.0166  152 THR B OG1 
5482  C CG2 . THR B 152 ? 0.3321 1.3372 2.1695 0.4105  0.1364  0.0072  152 THR B CG2 
5483  N N   . LEU B 153 ? 0.3687 1.2089 2.1546 0.4072  0.1477  -0.0007 153 LEU B N   
5484  C CA  . LEU B 153 ? 0.3701 1.2016 2.1514 0.3981  0.1570  -0.0061 153 LEU B CA  
5485  C C   . LEU B 153 ? 0.4049 1.2027 2.1707 0.4281  0.1603  -0.0125 153 LEU B C   
5486  O O   . LEU B 153 ? 0.4056 1.2326 2.1744 0.4416  0.1678  -0.0185 153 LEU B O   
5487  C CB  . LEU B 153 ? 0.3517 1.1433 2.1251 0.3658  0.1572  -0.0051 153 LEU B CB  
5488  C CG  . LEU B 153 ? 0.3301 1.1548 2.1200 0.3332  0.1555  -0.0015 153 LEU B CG  
5489  C CD1 . LEU B 153 ? 0.3164 1.2139 2.1285 0.3296  0.1601  -0.0005 153 LEU B CD1 
5490  C CD2 . LEU B 153 ? 0.3273 1.1458 2.1195 0.3259  0.1454  0.0014  153 LEU B CD2 
5491  N N   . ILE B 154 ? 0.4279 1.1653 2.1775 0.4385  0.1544  -0.0113 154 ILE B N   
5492  C CA  . ILE B 154 ? 0.4514 1.1463 2.1858 0.4644  0.1555  -0.0181 154 ILE B CA  
5493  C C   . ILE B 154 ? 0.4711 1.2107 2.2144 0.4959  0.1590  -0.0240 154 ILE B C   
5494  O O   . ILE B 154 ? 0.4868 1.2302 2.2253 0.5065  0.1660  -0.0341 154 ILE B O   
5495  C CB  . ILE B 154 ? 0.4605 1.0967 2.1822 0.4740  0.1468  -0.0126 154 ILE B CB  
5496  C CG1 . ILE B 154 ? 0.4424 1.0281 2.1519 0.4467  0.1454  -0.0102 154 ILE B CG1 
5497  C CG2 . ILE B 154 ? 0.4946 1.0975 2.2065 0.5079  0.1457  -0.0189 154 ILE B CG2 
5498  C CD1 . ILE B 154 ? 0.4523 0.9956 2.1536 0.4481  0.1369  -0.0008 154 ILE B CD1 
5499  N N   . ASN B 155 ? 0.4789 1.2548 2.2349 0.5114  0.1539  -0.0181 155 ASN B N   
5500  C CA  . ASN B 155 ? 0.5054 1.3185 2.2693 0.5467  0.1555  -0.0232 155 ASN B CA  
5501  C C   . ASN B 155 ? 0.5003 1.3750 2.2758 0.5421  0.1661  -0.0303 155 ASN B C   
5502  O O   . ASN B 155 ? 0.5407 1.4250 2.3132 0.5667  0.1717  -0.0409 155 ASN B O   
5503  C CB  . ASN B 155 ? 0.5122 1.3550 2.2879 0.5630  0.1473  -0.0139 155 ASN B CB  
5504  C CG  . ASN B 155 ? 0.5268 1.3085 2.2893 0.5750  0.1377  -0.0059 155 ASN B CG  
5505  O OD1 . ASN B 155 ? 0.5476 1.2736 2.2957 0.5935  0.1366  -0.0105 155 ASN B OD1 
5506  N ND2 . ASN B 155 ? 0.5146 1.3070 2.2819 0.5651  0.1301  0.0061  155 ASN B ND2 
5507  N N   . ILE B 156 ? 0.4697 1.3853 2.2584 0.5099  0.1687  -0.0246 156 ILE B N   
5508  C CA  . ILE B 156 ? 0.4574 1.4363 2.2597 0.5000  0.1785  -0.0272 156 ILE B CA  
5509  C C   . ILE B 156 ? 0.4613 1.4155 2.2481 0.5017  0.1872  -0.0366 156 ILE B C   
5510  O O   . ILE B 156 ? 0.4612 1.4646 2.2544 0.5121  0.1960  -0.0422 156 ILE B O   
5511  C CB  . ILE B 156 ? 0.4352 1.4451 2.2526 0.4601  0.1778  -0.0182 156 ILE B CB  
5512  C CG1 . ILE B 156 ? 0.4272 1.4893 2.2648 0.4629  0.1710  -0.0121 156 ILE B CG1 
5513  C CG2 . ILE B 156 ? 0.4287 1.4805 2.2546 0.4393  0.1884  -0.0183 156 ILE B CG2 
5514  C CD1 . ILE B 156 ? 0.4010 1.4812 2.2516 0.4239  0.1671  -0.0051 156 ILE B CD1 
5515  N N   . ILE B 157 ? 0.4671 1.3495 2.2340 0.4912  0.1847  -0.0382 157 ILE B N   
5516  C CA  . ILE B 157 ? 0.4755 1.3314 2.2265 0.4889  0.1917  -0.0468 157 ILE B CA  
5517  C C   . ILE B 157 ? 0.5129 1.3469 2.2516 0.5278  0.1920  -0.0606 157 ILE B C   
5518  O O   . ILE B 157 ? 0.5201 1.3689 2.2521 0.5371  0.1999  -0.0710 157 ILE B O   
5519  C CB  . ILE B 157 ? 0.4626 1.2535 2.1987 0.4617  0.1882  -0.0433 157 ILE B CB  
5520  C CG1 . ILE B 157 ? 0.4330 1.2427 2.1811 0.4238  0.1876  -0.0318 157 ILE B CG1 
5521  C CG2 . ILE B 157 ? 0.4771 1.2390 2.1951 0.4628  0.1940  -0.0531 157 ILE B CG2 
5522  C CD1 . ILE B 157 ? 0.4228 1.1715 2.1578 0.3984  0.1837  -0.0284 157 ILE B CD1 
5523  N N   . HIS B 158 ? 0.5365 1.3332 2.2715 0.5499  0.1830  -0.0605 158 HIS B N   
5524  C CA  . HIS B 158 ? 0.5758 1.3464 2.3010 0.5883  0.1813  -0.0733 158 HIS B CA  
5525  C C   . HIS B 158 ? 0.5875 1.4286 2.3256 0.6156  0.1879  -0.0812 158 HIS B C   
5526  O O   . HIS B 158 ? 0.6263 1.4592 2.3552 0.6432  0.1908  -0.0967 158 HIS B O   
5527  C CB  . HIS B 158 ? 0.5977 1.3200 2.3198 0.6056  0.1698  -0.0676 158 HIS B CB  
5528  C CG  . HIS B 158 ? 0.6057 1.2483 2.3110 0.5903  0.1634  -0.0643 158 HIS B CG  
5529  N ND1 . HIS B 158 ? 0.6235 1.2234 2.3262 0.5977  0.1534  -0.0545 158 HIS B ND1 
5530  C CD2 . HIS B 158 ? 0.5947 1.1947 2.2854 0.5697  0.1654  -0.0688 158 HIS B CD2 
5531  C CE1 . HIS B 158 ? 0.6165 1.1527 2.3047 0.5803  0.1500  -0.0529 158 HIS B CE1 
5532  N NE2 . HIS B 158 ? 0.5972 1.1323 2.2781 0.5637  0.1569  -0.0621 158 HIS B NE2 
5533  N N   . LYS B 159 ? 0.5678 1.4784 2.3273 0.6078  0.1898  -0.0715 159 LYS B N   
5534  C CA  . LYS B 159 ? 0.5757 1.5631 2.3512 0.6320  0.1959  -0.0767 159 LYS B CA  
5535  C C   . LYS B 159 ? 0.5400 1.5866 2.3213 0.6143  0.2086  -0.0789 159 LYS B C   
5536  O O   . LYS B 159 ? 0.5421 1.6378 2.3275 0.6380  0.2163  -0.0891 159 LYS B O   
5537  C CB  . LYS B 159 ? 0.5867 1.6201 2.3835 0.6335  0.1901  -0.0644 159 LYS B CB  
5538  C CG  . LYS B 159 ? 0.6311 1.6243 2.4244 0.6631  0.1787  -0.0623 159 LYS B CG  
5539  C CD  . LYS B 159 ? 0.6421 1.7001 2.4562 0.6883  0.1757  -0.0582 159 LYS B CD  
5540  C CE  . LYS B 159 ? 0.6222 1.7224 2.4537 0.6614  0.1715  -0.0431 159 LYS B CE  
5541  N NZ  . LYS B 159 ? 0.6381 1.8073 2.4903 0.6870  0.1688  -0.0402 159 LYS B NZ  
5542  N N   . GLY B 160 ? 0.5107 1.5538 2.2927 0.5731  0.2107  -0.0687 160 GLY B N   
5543  C CA  . GLY B 160 ? 0.4961 1.5894 2.2832 0.5514  0.2221  -0.0668 160 GLY B CA  
5544  C C   . GLY B 160 ? 0.5092 1.5663 2.2734 0.5519  0.2280  -0.0774 160 GLY B C   
5545  O O   . GLY B 160 ? 0.5120 1.6194 2.2772 0.5555  0.2387  -0.0819 160 GLY B O   
5546  N N   . HIS B 161 ? 0.5157 1.4904 2.2599 0.5458  0.2214  -0.0803 161 HIS B N   
5547  C CA  . HIS B 161 ? 0.5213 1.4570 2.2427 0.5506  0.2249  -0.0928 161 HIS B CA  
5548  C C   . HIS B 161 ? 0.5444 1.4055 2.2492 0.5759  0.2157  -0.1049 161 HIS B C   
5549  O O   . HIS B 161 ? 0.5462 1.3426 2.2408 0.5599  0.2084  -0.1005 161 HIS B O   
5550  C CB  . HIS B 161 ? 0.4969 1.4111 2.2109 0.5110  0.2272  -0.0833 161 HIS B CB  
5551  C CG  . HIS B 161 ? 0.5138 1.4135 2.2075 0.5147  0.2331  -0.0949 161 HIS B CG  
5552  N ND1 . HIS B 161 ? 0.5018 1.3855 2.1864 0.4841  0.2360  -0.0877 161 HIS B ND1 
5553  C CD2 . HIS B 161 ? 0.5438 1.4412 2.2237 0.5463  0.2360  -0.1141 161 HIS B CD2 
5554  C CE1 . HIS B 161 ? 0.5216 1.3970 2.1872 0.4964  0.2404  -0.1014 161 HIS B CE1 
5555  N NE2 . HIS B 161 ? 0.5482 1.4317 2.2105 0.5339  0.2405  -0.1185 161 HIS B NE2 
5556  N N   . PRO B 162 ? 0.5782 1.4457 2.2804 0.6163  0.2156  -0.1204 162 PRO B N   
5557  C CA  . PRO B 162 ? 0.6059 1.4036 2.2967 0.6415  0.2053  -0.1297 162 PRO B CA  
5558  C C   . PRO B 162 ? 0.6287 1.3611 2.2957 0.6389  0.2035  -0.1427 162 PRO B C   
5559  O O   . PRO B 162 ? 0.6281 1.3771 2.2858 0.6270  0.2112  -0.1488 162 PRO B O   
5560  C CB  . PRO B 162 ? 0.6291 1.4652 2.3272 0.6850  0.2069  -0.1425 162 PRO B CB  
5561  C CG  . PRO B 162 ? 0.6233 1.5331 2.3244 0.6850  0.2201  -0.1495 162 PRO B CG  
5562  C CD  . PRO B 162 ? 0.5853 1.5277 2.2962 0.6406  0.2250  -0.1299 162 PRO B CD  
5563  N N   . GLY B 163 ? 0.6504 1.3096 2.3086 0.6490  0.1928  -0.1454 163 GLY B N   
5564  C CA  . GLY B 163 ? 0.6722 1.2641 2.3096 0.6495  0.1887  -0.1590 163 GLY B CA  
5565  C C   . GLY B 163 ? 0.6454 1.2135 2.2742 0.6094  0.1898  -0.1499 163 GLY B C   
5566  O O   . GLY B 163 ? 0.6657 1.1933 2.2774 0.6071  0.1885  -0.1623 163 GLY B O   
5567  N N   . ILE B 164 ? 0.6098 1.2020 2.2505 0.5795  0.1913  -0.1298 164 ILE B N   
5568  C CA  . ILE B 164 ? 0.5862 1.1575 2.2206 0.5421  0.1920  -0.1203 164 ILE B CA  
5569  C C   . ILE B 164 ? 0.5665 1.0934 2.2043 0.5235  0.1832  -0.1052 164 ILE B C   
5570  O O   . ILE B 164 ? 0.5428 1.0980 2.1957 0.5139  0.1823  -0.0912 164 ILE B O   
5571  C CB  . ILE B 164 ? 0.5570 1.1939 2.2014 0.5191  0.2018  -0.1105 164 ILE B CB  
5572  C CG1 . ILE B 164 ? 0.5699 1.2597 2.2108 0.5345  0.2121  -0.1229 164 ILE B CG1 
5573  C CG2 . ILE B 164 ? 0.5339 1.1428 2.1725 0.4821  0.2010  -0.0999 164 ILE B CG2 
5574  C CD1 . ILE B 164 ? 0.5896 1.2472 2.2083 0.5373  0.2133  -0.1382 164 ILE B CD1 
5575  N N   . PRO B 165 ? 0.5780 1.0380 2.2023 0.5144  0.1766  -0.1069 165 PRO B N   
5576  C CA  . PRO B 165 ? 0.5714 0.9935 2.1984 0.4966  0.1690  -0.0922 165 PRO B CA  
5577  C C   . PRO B 165 ? 0.5453 1.0022 2.1844 0.4672  0.1716  -0.0762 165 PRO B C   
5578  O O   . PRO B 165 ? 0.5274 1.0161 2.1681 0.4493  0.1785  -0.0751 165 PRO B O   
5579  C CB  . PRO B 165 ? 0.5750 0.9327 2.1852 0.4858  0.1646  -0.0980 165 PRO B CB  
5580  C CG  . PRO B 165 ? 0.6047 0.9542 2.2033 0.5093  0.1663  -0.1186 165 PRO B CG  
5581  C CD  . PRO B 165 ? 0.6019 1.0229 2.2079 0.5198  0.1760  -0.1232 165 PRO B CD  
5582  N N   . VAL B 166 ? 0.5405 0.9905 2.1880 0.4630  0.1656  -0.0639 166 VAL B N   
5583  C CA  . VAL B 166 ? 0.5074 0.9868 2.1671 0.4378  0.1659  -0.0506 166 VAL B CA  
5584  C C   . VAL B 166 ? 0.5156 0.9446 2.1694 0.4223  0.1585  -0.0422 166 VAL B C   
5585  O O   . VAL B 166 ? 0.5443 0.9389 2.1937 0.4377  0.1521  -0.0404 166 VAL B O   
5586  C CB  . VAL B 166 ? 0.5041 1.0363 2.1811 0.4501  0.1655  -0.0448 166 VAL B CB  
5587  C CG1 . VAL B 166 ? 0.4811 1.0407 2.1708 0.4233  0.1641  -0.0329 166 VAL B CG1 
5588  C CG2 . VAL B 166 ? 0.5044 1.0917 2.1887 0.4682  0.1731  -0.0530 166 VAL B CG2 
5589  N N   . THR B 167 ? 0.4990 0.9239 2.1528 0.3929  0.1593  -0.0367 167 THR B N   
5590  C CA  . THR B 167 ? 0.4823 0.8703 2.1327 0.3770  0.1530  -0.0285 167 THR B CA  
5591  C C   . THR B 167 ? 0.4429 0.8561 2.1023 0.3489  0.1546  -0.0223 167 THR B C   
5592  O O   . THR B 167 ? 0.4224 0.8832 2.0932 0.3446  0.1592  -0.0223 167 THR B O   
5593  C CB  . THR B 167 ? 0.5008 0.8305 2.1353 0.3748  0.1507  -0.0332 167 THR B CB  
5594  O OG1 . THR B 167 ? 0.4960 0.7980 2.1291 0.3601  0.1452  -0.0239 167 THR B OG1 
5595  C CG2 . THR B 167 ? 0.4954 0.8220 2.1230 0.3600  0.1558  -0.0398 167 THR B CG2 
5596  N N   . LEU B 168 ? 0.4268 0.8082 2.0818 0.3307  0.1504  -0.0173 168 LEU B N   
5597  C CA  . LEU B 168 ? 0.4044 0.8009 2.0671 0.3049  0.1502  -0.0128 168 LEU B CA  
5598  C C   . LEU B 168 ? 0.4223 0.7770 2.0748 0.2874  0.1492  -0.0132 168 LEU B C   
5599  O O   . LEU B 168 ? 0.4419 0.7573 2.0820 0.2944  0.1480  -0.0162 168 LEU B O   
5600  C CB  . LEU B 168 ? 0.3863 0.7999 2.0578 0.3037  0.1446  -0.0063 168 LEU B CB  
5601  C CG  . LEU B 168 ? 0.3820 0.7579 2.0450 0.3017  0.1384  -0.0013 168 LEU B CG  
5602  C CD1 . LEU B 168 ? 0.3718 0.7745 2.0438 0.2967  0.1335  0.0043  168 LEU B CD1 
5603  C CD2 . LEU B 168 ? 0.4019 0.7458 2.0549 0.3236  0.1363  -0.0001 168 LEU B CD2 
5604  N N   . SER B 169 ? 0.4188 0.7824 2.0777 0.2645  0.1490  -0.0106 169 SER B N   
5605  C CA  . SER B 169 ? 0.4155 0.7452 2.0670 0.2476  0.1479  -0.0107 169 SER B CA  
5606  C C   . SER B 169 ? 0.4208 0.7372 2.0735 0.2387  0.1420  -0.0070 169 SER B C   
5607  O O   . SER B 169 ? 0.4187 0.7444 2.0786 0.2214  0.1406  -0.0063 169 SER B O   
5608  C CB  . SER B 169 ? 0.4005 0.7456 2.0576 0.2293  0.1515  -0.0103 169 SER B CB  
5609  O OG  . SER B 169 ? 0.4190 0.7855 2.0756 0.2362  0.1578  -0.0124 169 SER B OG  
5610  N N   . ALA B 170 ? 0.4398 0.7349 2.0856 0.2507  0.1384  -0.0045 170 ALA B N   
5611  C CA  . ALA B 170 ? 0.4313 0.7205 2.0775 0.2443  0.1333  -0.0001 170 ALA B CA  
5612  C C   . ALA B 170 ? 0.4307 0.6838 2.0685 0.2323  0.1323  -0.0005 170 ALA B C   
5613  O O   . ALA B 170 ? 0.4511 0.6738 2.0793 0.2376  0.1330  -0.0012 170 ALA B O   
5614  C CB  . ALA B 170 ? 0.4566 0.7420 2.0994 0.2621  0.1301  0.0057  170 ALA B CB  
5615  N N   . ASN B 171 ? 0.4121 0.6694 2.0538 0.2170  0.1301  -0.0009 171 ASN B N   
5616  C CA  . ASN B 171 ? 0.3758 0.6034 2.0109 0.2061  0.1292  -0.0017 171 ASN B CA  
5617  C C   . ASN B 171 ? 0.3658 0.5738 1.9933 0.2120  0.1263  0.0040  171 ASN B C   
5618  O O   . ASN B 171 ? 0.3519 0.5748 1.9815 0.2135  0.1234  0.0077  171 ASN B O   
5619  C CB  . ASN B 171 ? 0.3646 0.6024 2.0070 0.1893  0.1276  -0.0053 171 ASN B CB  
5620  C CG  . ASN B 171 ? 0.3550 0.5650 1.9919 0.1795  0.1270  -0.0068 171 ASN B CG  
5621  O OD1 . ASN B 171 ? 0.3603 0.5555 1.9914 0.1805  0.1250  -0.0045 171 ASN B OD1 
5622  N ND2 . ASN B 171 ? 0.3416 0.5467 1.9808 0.1699  0.1287  -0.0097 171 ASN B ND2 
5623  N N   . ALA B 172 ? 0.3725 0.5483 1.9914 0.2138  0.1269  0.0047  172 ALA B N   
5624  C CA  . ALA B 172 ? 0.3750 0.5270 1.9869 0.2183  0.1244  0.0115  172 ALA B CA  
5625  C C   . ALA B 172 ? 0.3636 0.5191 1.9757 0.2086  0.1222  0.0154  172 ALA B C   
5626  O O   . ALA B 172 ? 0.3830 0.5329 1.9915 0.2133  0.1202  0.0243  172 ALA B O   
5627  C CB  . ALA B 172 ? 0.3811 0.4996 1.9858 0.2176  0.1250  0.0090  172 ALA B CB  
5628  N N   . MET B 173 ? 0.3352 0.4993 1.9511 0.1957  0.1225  0.0093  173 MET B N   
5629  C CA  . MET B 173 ? 0.3207 0.4896 1.9364 0.1880  0.1205  0.0106  173 MET B CA  
5630  C C   . MET B 173 ? 0.3172 0.5173 1.9367 0.1911  0.1182  0.0119  173 MET B C   
5631  O O   . MET B 173 ? 0.3077 0.5142 1.9242 0.1900  0.1165  0.0159  173 MET B O   
5632  C CB  . MET B 173 ? 0.3099 0.4753 1.9288 0.1752  0.1207  0.0024  173 MET B CB  
5633  C CG  . MET B 173 ? 0.3111 0.4487 1.9254 0.1712  0.1221  0.0017  173 MET B CG  
5634  S SD  . MET B 173 ? 0.3155 0.4343 1.9233 0.1699  0.1210  0.0092  173 MET B SD  
5635  C CE  . MET B 173 ? 0.2996 0.4408 1.9109 0.1636  0.1195  0.0070  173 MET B CE  
5636  N N   . ILE B 174 ? 0.3205 0.5431 1.9467 0.1947  0.1180  0.0084  174 ILE B N   
5637  C CA  . ILE B 174 ? 0.3273 0.5832 1.9583 0.1967  0.1149  0.0078  174 ILE B CA  
5638  C C   . ILE B 174 ? 0.3429 0.6129 1.9740 0.2118  0.1144  0.0153  174 ILE B C   
5639  O O   . ILE B 174 ? 0.3418 0.6371 1.9736 0.2169  0.1112  0.0188  174 ILE B O   
5640  C CB  . ILE B 174 ? 0.3243 0.6007 1.9659 0.1862  0.1138  -0.0032 174 ILE B CB  
5641  C CG1 . ILE B 174 ? 0.3303 0.6017 1.9770 0.1845  0.1172  -0.0055 174 ILE B CG1 
5642  C CG2 . ILE B 174 ? 0.3146 0.5847 1.9569 0.1738  0.1120  -0.0111 174 ILE B CG2 
5643  C CD1 . ILE B 174 ? 0.3221 0.6252 1.9813 0.1802  0.1161  -0.0105 174 ILE B CD1 
5644  N N   . SER B 175 ? 0.3576 0.6141 1.9883 0.2200  0.1171  0.0169  175 SER B N   
5645  C CA  . SER B 175 ? 0.3784 0.6475 2.0101 0.2367  0.1164  0.0229  175 SER B CA  
5646  C C   . SER B 175 ? 0.4125 0.6496 2.0350 0.2483  0.1162  0.0328  175 SER B C   
5647  O O   . SER B 175 ? 0.4459 0.6787 2.0683 0.2637  0.1163  0.0357  175 SER B O   
5648  C CB  . SER B 175 ? 0.3785 0.6642 2.0183 0.2393  0.1193  0.0161  175 SER B CB  
5649  O OG  . SER B 175 ? 0.3645 0.6812 2.0147 0.2274  0.1184  0.0091  175 SER B OG  
5650  N N   . ASP B 176 ? 0.4067 0.6225 2.0223 0.2415  0.1152  0.0385  176 ASP B N   
5651  C CA  . ASP B 176 ? 0.4221 0.6061 2.0305 0.2490  0.1141  0.0494  176 ASP B CA  
5652  C C   . ASP B 176 ? 0.4330 0.6284 2.0404 0.2646  0.1109  0.0622  176 ASP B C   
5653  O O   . ASP B 176 ? 0.4727 0.6449 2.0777 0.2775  0.1098  0.0685  176 ASP B O   
5654  C CB  . ASP B 176 ? 0.4320 0.5974 2.0351 0.2363  0.1140  0.0538  176 ASP B CB  
5655  C CG  . ASP B 176 ? 0.4241 0.6170 2.0274 0.2278  0.1130  0.0553  176 ASP B CG  
5656  O OD1 . ASP B 176 ? 0.4164 0.6427 2.0235 0.2318  0.1114  0.0534  176 ASP B OD1 
5657  O OD2 . ASP B 176 ? 0.4182 0.6010 2.0183 0.2173  0.1137  0.0570  176 ASP B OD2 
5658  N N   . TYR B 177 ? 0.4039 0.6352 2.0134 0.2641  0.1088  0.0653  177 TYR B N   
5659  C CA  . TYR B 177 ? 0.4086 0.6572 2.0171 0.2790  0.1052  0.0784  177 TYR B CA  
5660  C C   . TYR B 177 ? 0.4174 0.6729 2.0314 0.2966  0.1048  0.0765  177 TYR B C   
5661  O O   . TYR B 177 ? 0.4350 0.6892 2.0474 0.3131  0.1017  0.0888  177 TYR B O   
5662  C CB  . TYR B 177 ? 0.3881 0.6803 1.9981 0.2741  0.1028  0.0778  177 TYR B CB  
5663  C CG  . TYR B 177 ? 0.3728 0.6985 1.9928 0.2708  0.1029  0.0627  177 TYR B CG  
5664  C CD1 . TYR B 177 ? 0.3722 0.7271 1.9989 0.2843  0.1008  0.0634  177 TYR B CD1 
5665  C CD2 . TYR B 177 ? 0.3512 0.6798 1.9750 0.2537  0.1047  0.0484  177 TYR B CD2 
5666  C CE1 . TYR B 177 ? 0.3518 0.7394 1.9895 0.2787  0.1008  0.0505  177 TYR B CE1 
5667  C CE2 . TYR B 177 ? 0.3368 0.6935 1.9712 0.2483  0.1044  0.0360  177 TYR B CE2 
5668  C CZ  . TYR B 177 ? 0.3401 0.7269 1.9817 0.2599  0.1026  0.0371  177 TYR B CZ  
5669  O OH  . TYR B 177 ? 0.3254 0.7410 1.9789 0.2515  0.1022  0.0255  177 TYR B OH  
5670  N N   . MET B 178 ? 0.4021 0.6663 2.0228 0.2937  0.1079  0.0620  178 MET B N   
5671  C CA  . MET B 178 ? 0.4045 0.6952 2.0330 0.3082  0.1079  0.0583  178 MET B CA  
5672  C C   . MET B 178 ? 0.4271 0.6907 2.0529 0.3285  0.1075  0.0631  178 MET B C   
5673  O O   . MET B 178 ? 0.4393 0.6611 2.0589 0.3269  0.1087  0.0622  178 MET B O   
5674  C CB  . MET B 178 ? 0.3847 0.6914 2.0211 0.2979  0.1120  0.0431  178 MET B CB  
5675  C CG  . MET B 178 ? 0.3835 0.7190 2.0289 0.3119  0.1133  0.0388  178 MET B CG  
5676  S SD  . MET B 178 ? 0.3640 0.7256 2.0200 0.2960  0.1182  0.0247  178 MET B SD  
5677  C CE  . MET B 178 ? 0.3468 0.7486 2.0115 0.2797  0.1141  0.0229  178 MET B CE  
5678  N N   . ASP B 179 ? 0.4380 0.7271 2.0693 0.3477  0.1053  0.0670  179 ASP B N   
5679  C CA  . ASP B 179 ? 0.4587 0.7269 2.0891 0.3708  0.1042  0.0699  179 ASP B CA  
5680  C C   . ASP B 179 ? 0.4441 0.7215 2.0800 0.3755  0.1091  0.0543  179 ASP B C   
5681  O O   . ASP B 179 ? 0.4174 0.7383 2.0625 0.3709  0.1114  0.0473  179 ASP B O   
5682  C CB  . ASP B 179 ? 0.4770 0.7730 2.1114 0.3912  0.0994  0.0815  179 ASP B CB  
5683  C CG  . ASP B 179 ? 0.5201 0.7912 2.1537 0.4180  0.0970  0.0861  179 ASP B CG  
5684  O OD1 . ASP B 179 ? 0.5495 0.7706 2.1751 0.4205  0.0947  0.0942  179 ASP B OD1 
5685  O OD2 . ASP B 179 ? 0.5206 0.8230 2.1626 0.4364  0.0971  0.0814  179 ASP B OD2 
5686  N N   . GLU B 180 ? 0.4604 0.6986 2.0910 0.3845  0.1103  0.0490  180 GLU B N   
5687  C CA  . GLU B 180 ? 0.4557 0.7015 2.0891 0.3902  0.1154  0.0338  180 GLU B CA  
5688  C C   . GLU B 180 ? 0.4978 0.7278 2.1304 0.4190  0.1135  0.0320  180 GLU B C   
5689  O O   . GLU B 180 ? 0.5060 0.7294 2.1373 0.4270  0.1171  0.0187  180 GLU B O   
5690  C CB  . GLU B 180 ? 0.4416 0.6572 2.0680 0.3734  0.1190  0.0238  180 GLU B CB  
5691  C CG  . GLU B 180 ? 0.4026 0.6346 2.0309 0.3467  0.1216  0.0220  180 GLU B CG  
5692  C CD  . GLU B 180 ? 0.3922 0.6043 2.0154 0.3328  0.1257  0.0115  180 GLU B CD  
5693  O OE1 . GLU B 180 ? 0.3998 0.5944 2.0183 0.3439  0.1274  0.0030  180 GLU B OE1 
5694  O OE2 . GLU B 180 ? 0.3723 0.5875 1.9958 0.3115  0.1267  0.0113  180 GLU B OE2 
5695  N N   . SER B 181 ? 0.5292 0.7547 2.1626 0.4358  0.1078  0.0452  181 SER B N   
5696  C CA  . SER B 181 ? 0.5721 0.7770 2.2052 0.4649  0.1047  0.0444  181 SER B CA  
5697  C C   . SER B 181 ? 0.5703 0.8262 2.2138 0.4840  0.1076  0.0361  181 SER B C   
5698  O O   . SER B 181 ? 0.5990 0.8452 2.2433 0.5096  0.1068  0.0296  181 SER B O   
5699  C CB  . SER B 181 ? 0.6045 0.7838 2.2349 0.4762  0.0971  0.0636  181 SER B CB  
5700  O OG  . SER B 181 ? 0.5972 0.8235 2.2344 0.4811  0.0948  0.0754  181 SER B OG  
5701  N N   . ILE B 182 ? 0.5392 0.8503 2.1916 0.4716  0.1108  0.0356  182 ILE B N   
5702  C CA  . ILE B 182 ? 0.5366 0.9029 2.2010 0.4855  0.1141  0.0282  182 ILE B CA  
5703  C C   . ILE B 182 ? 0.5191 0.8941 2.1838 0.4801  0.1220  0.0112  182 ILE B C   
5704  O O   . ILE B 182 ? 0.5308 0.9508 2.2051 0.4927  0.1259  0.0042  182 ILE B O   
5705  C CB  . ILE B 182 ? 0.5163 0.9399 2.1918 0.4730  0.1134  0.0345  182 ILE B CB  
5706  C CG1 . ILE B 182 ? 0.4886 0.9164 2.1633 0.4387  0.1170  0.0303  182 ILE B CG1 
5707  C CG2 . ILE B 182 ? 0.5293 0.9537 2.2042 0.4824  0.1054  0.0515  182 ILE B CG2 
5708  C CD1 . ILE B 182 ? 0.4631 0.9464 2.1499 0.4234  0.1163  0.0321  182 ILE B CD1 
5709  N N   . PHE B 183 ? 0.4946 0.8322 2.1494 0.4613  0.1245  0.0054  183 PHE B N   
5710  C CA  . PHE B 183 ? 0.4796 0.8231 2.1322 0.4565  0.1316  -0.0094 183 PHE B CA  
5711  C C   . PHE B 183 ? 0.5033 0.8001 2.1452 0.4754  0.1305  -0.0193 183 PHE B C   
5712  O O   . PHE B 183 ? 0.5316 0.7826 2.1674 0.4844  0.1240  -0.0135 183 PHE B O   
5713  C CB  . PHE B 183 ? 0.4602 0.7959 2.1090 0.4240  0.1347  -0.0102 183 PHE B CB  
5714  C CG  . PHE B 183 ? 0.4308 0.8054 2.0897 0.4032  0.1347  -0.0025 183 PHE B CG  
5715  C CD1 . PHE B 183 ? 0.4142 0.8434 2.0854 0.3970  0.1396  -0.0060 183 PHE B CD1 
5716  C CD2 . PHE B 183 ? 0.4196 0.7776 2.0762 0.3903  0.1294  0.0078  183 PHE B CD2 
5717  C CE1 . PHE B 183 ? 0.3902 0.8523 2.0717 0.3779  0.1383  -0.0005 183 PHE B CE1 
5718  C CE2 . PHE B 183 ? 0.3983 0.7916 2.0638 0.3732  0.1285  0.0121  183 PHE B CE2 
5719  C CZ  . PHE B 183 ? 0.3846 0.8276 2.0627 0.3665  0.1325  0.0073  183 PHE B CZ  
5720  N N   . ASP B 184 ? 0.4975 0.8059 2.1369 0.4799  0.1366  -0.0343 184 ASP B N   
5721  C CA  . ASP B 184 ? 0.5292 0.8006 2.1588 0.5001  0.1356  -0.0480 184 ASP B CA  
5722  C C   . ASP B 184 ? 0.5301 0.7491 2.1465 0.4821  0.1341  -0.0528 184 ASP B C   
5723  O O   . ASP B 184 ? 0.5636 0.7412 2.1711 0.4959  0.1309  -0.0635 184 ASP B O   
5724  C CB  . ASP B 184 ? 0.5336 0.8470 2.1655 0.5148  0.1430  -0.0631 184 ASP B CB  
5725  C CG  . ASP B 184 ? 0.5331 0.9080 2.1801 0.5320  0.1456  -0.0598 184 ASP B CG  
5726  O OD1 . ASP B 184 ? 0.5520 0.9210 2.2037 0.5552  0.1397  -0.0545 184 ASP B OD1 
5727  O OD2 . ASP B 184 ? 0.5128 0.9421 2.1672 0.5218  0.1532  -0.0619 184 ASP B OD2 
5728  N N   . VAL B 185 ? 0.4958 0.7194 2.1117 0.4521  0.1363  -0.0463 185 VAL B N   
5729  C CA  . VAL B 185 ? 0.4897 0.6747 2.0947 0.4324  0.1358  -0.0505 185 VAL B CA  
5730  C C   . VAL B 185 ? 0.4650 0.6452 2.0726 0.4066  0.1338  -0.0358 185 VAL B C   
5731  O O   . VAL B 185 ? 0.4395 0.6604 2.0562 0.3963  0.1365  -0.0289 185 VAL B O   
5732  C CB  . VAL B 185 ? 0.4746 0.6818 2.0751 0.4242  0.1430  -0.0630 185 VAL B CB  
5733  C CG1 . VAL B 185 ? 0.4686 0.6435 2.0597 0.4006  0.1421  -0.0640 185 VAL B CG1 
5734  C CG2 . VAL B 185 ? 0.5028 0.7119 2.0974 0.4493  0.1450  -0.0803 185 VAL B CG2 
5735  N N   . TYR B 186 ? 0.4771 0.6093 2.0774 0.3963  0.1288  -0.0318 186 TYR B N   
5736  C CA  . TYR B 186 ? 0.4567 0.5852 2.0582 0.3718  0.1276  -0.0202 186 TYR B CA  
5737  C C   . TYR B 186 ? 0.4326 0.5720 2.0317 0.3509  0.1324  -0.0266 186 TYR B C   
5738  O O   . TYR B 186 ? 0.4356 0.5614 2.0272 0.3520  0.1342  -0.0382 186 TYR B O   
5739  C CB  . TYR B 186 ? 0.4800 0.5580 2.0757 0.3679  0.1211  -0.0125 186 TYR B CB  
5740  C CG  . TYR B 186 ? 0.5056 0.5709 2.1039 0.3882  0.1158  -0.0029 186 TYR B CG  
5741  C CD1 . TYR B 186 ? 0.4918 0.5886 2.0976 0.3914  0.1149  0.0101  186 TYR B CD1 
5742  C CD2 . TYR B 186 ? 0.5464 0.5672 2.1397 0.4037  0.1108  -0.0066 186 TYR B CD2 
5743  C CE1 . TYR B 186 ? 0.5231 0.6094 2.1308 0.4105  0.1097  0.0210  186 TYR B CE1 
5744  C CE2 . TYR B 186 ? 0.5808 0.5875 2.1770 0.4233  0.1054  0.0038  186 TYR B CE2 
5745  C CZ  . TYR B 186 ? 0.5642 0.6045 2.1673 0.4273  0.1049  0.0186  186 TYR B CZ  
5746  O OH  . TYR B 186 ? 0.5781 0.6040 2.1834 0.4471  0.0991  0.0307  186 TYR B OH  
5747  N N   . ALA B 187 ? 0.4095 0.5739 2.0149 0.3326  0.1340  -0.0191 187 ALA B N   
5748  C CA  . ALA B 187 ? 0.3962 0.5704 2.0007 0.3129  0.1379  -0.0230 187 ALA B CA  
5749  C C   . ALA B 187 ? 0.3808 0.5612 1.9902 0.2923  0.1365  -0.0142 187 ALA B C   
5750  O O   . ALA B 187 ? 0.3786 0.5740 1.9943 0.2936  0.1341  -0.0064 187 ALA B O   
5751  C CB  . ALA B 187 ? 0.3913 0.6072 2.0009 0.3174  0.1441  -0.0289 187 ALA B CB  
5752  N N   . TYR B 188 ? 0.3767 0.5470 1.9828 0.2744  0.1377  -0.0164 188 TYR B N   
5753  C CA  . TYR B 188 ? 0.3639 0.5303 1.9725 0.2560  0.1356  -0.0105 188 TYR B CA  
5754  C C   . TYR B 188 ? 0.3614 0.5254 1.9682 0.2397  0.1380  -0.0144 188 TYR B C   
5755  O O   . TYR B 188 ? 0.3672 0.5125 1.9659 0.2405  0.1388  -0.0200 188 TYR B O   
5756  C CB  . TYR B 188 ? 0.3661 0.4982 1.9691 0.2542  0.1310  -0.0051 188 TYR B CB  
5757  C CG  . TYR B 188 ? 0.3698 0.5021 1.9747 0.2656  0.1275  0.0037  188 TYR B CG  
5758  C CD1 . TYR B 188 ? 0.3537 0.5120 1.9651 0.2613  0.1263  0.0103  188 TYR B CD1 
5759  C CD2 . TYR B 188 ? 0.3937 0.4989 1.9936 0.2803  0.1247  0.0057  188 TYR B CD2 
5760  C CE1 . TYR B 188 ? 0.3651 0.5266 1.9772 0.2720  0.1229  0.0198  188 TYR B CE1 
5761  C CE2 . TYR B 188 ? 0.4070 0.5116 2.0085 0.2911  0.1212  0.0162  188 TYR B CE2 
5762  C CZ  . TYR B 188 ? 0.3891 0.5236 1.9963 0.2872  0.1205  0.0241  188 TYR B CZ  
5763  O OH  . TYR B 188 ? 0.3965 0.5344 2.0044 0.2977  0.1168  0.0359  188 TYR B OH  
5764  N N   . ASN B 189 ? 0.3514 0.5341 1.9660 0.2252  0.1382  -0.0115 189 ASN B N   
5765  C CA  . ASN B 189 ? 0.3440 0.5197 1.9580 0.2089  0.1388  -0.0126 189 ASN B CA  
5766  C C   . ASN B 189 ? 0.3510 0.4986 1.9604 0.2021  0.1349  -0.0107 189 ASN B C   
5767  O O   . ASN B 189 ? 0.3639 0.5152 1.9771 0.2001  0.1323  -0.0068 189 ASN B O   
5768  C CB  . ASN B 189 ? 0.3427 0.5462 1.9682 0.1969  0.1396  -0.0107 189 ASN B CB  
5769  C CG  . ASN B 189 ? 0.3589 0.5952 1.9910 0.2008  0.1438  -0.0111 189 ASN B CG  
5770  O OD1 . ASN B 189 ? 0.3863 0.6248 2.0127 0.2120  0.1473  -0.0140 189 ASN B OD1 
5771  N ND2 . ASN B 189 ? 0.3472 0.6108 1.9918 0.1914  0.1436  -0.0090 189 ASN B ND2 
5772  N N   . CYS B 190 ? 0.3548 0.4782 1.9563 0.1984  0.1345  -0.0135 190 CYS B N   
5773  C CA  . CYS B 190 ? 0.3535 0.4512 1.9509 0.1928  0.1311  -0.0117 190 CYS B CA  
5774  C C   . CYS B 190 ? 0.3498 0.4430 1.9476 0.1789  0.1306  -0.0129 190 CYS B C   
5775  O O   . CYS B 190 ? 0.3487 0.4352 1.9415 0.1769  0.1316  -0.0163 190 CYS B O   
5776  C CB  . CYS B 190 ? 0.3630 0.4345 1.9517 0.2015  0.1295  -0.0142 190 CYS B CB  
5777  S SG  . CYS B 190 ? 0.3659 0.4407 1.9542 0.2215  0.1299  -0.0142 190 CYS B SG  
5778  N N   . TYR B 191 ? 0.3365 0.4341 1.9399 0.1703  0.1288  -0.0104 191 TYR B N   
5779  C CA  . TYR B 191 ? 0.3452 0.4353 1.9493 0.1595  0.1275  -0.0116 191 TYR B CA  
5780  C C   . TYR B 191 ? 0.3609 0.4355 1.9626 0.1570  0.1248  -0.0098 191 TYR B C   
5781  O O   . TYR B 191 ? 0.3732 0.4514 1.9762 0.1598  0.1239  -0.0062 191 TYR B O   
5782  C CB  . TYR B 191 ? 0.3443 0.4512 1.9576 0.1517  0.1273  -0.0120 191 TYR B CB  
5783  C CG  . TYR B 191 ? 0.3580 0.4811 1.9749 0.1514  0.1302  -0.0119 191 TYR B CG  
5784  C CD1 . TYR B 191 ? 0.3572 0.4776 1.9725 0.1461  0.1315  -0.0112 191 TYR B CD1 
5785  C CD2 . TYR B 191 ? 0.3651 0.5085 1.9864 0.1574  0.1319  -0.0113 191 TYR B CD2 
5786  C CE1 . TYR B 191 ? 0.3663 0.5047 1.9846 0.1453  0.1349  -0.0092 191 TYR B CE1 
5787  C CE2 . TYR B 191 ? 0.3772 0.5395 2.0024 0.1570  0.1352  -0.0105 191 TYR B CE2 
5788  C CZ  . TYR B 191 ? 0.3826 0.5430 2.0064 0.1504  0.1370  -0.0090 191 TYR B CZ  
5789  O OH  . TYR B 191 ? 0.3995 0.5835 2.0281 0.1493  0.1409  -0.0064 191 TYR B OH  
5790  N N   . ASP B 192 ? 0.3631 0.4238 1.9616 0.1513  0.1234  -0.0114 192 ASP B N   
5791  C CA  . ASP B 192 ? 0.3665 0.4149 1.9637 0.1476  0.1210  -0.0095 192 ASP B CA  
5792  C C   . ASP B 192 ? 0.3527 0.4065 1.9549 0.1398  0.1197  -0.0107 192 ASP B C   
5793  O O   . ASP B 192 ? 0.3408 0.3886 1.9419 0.1359  0.1186  -0.0129 192 ASP B O   
5794  C CB  . ASP B 192 ? 0.3898 0.4188 1.9800 0.1482  0.1196  -0.0115 192 ASP B CB  
5795  C CG  . ASP B 192 ? 0.3993 0.4165 1.9896 0.1415  0.1167  -0.0096 192 ASP B CG  
5796  O OD1 . ASP B 192 ? 0.3994 0.4255 1.9949 0.1372  0.1165  -0.0060 192 ASP B OD1 
5797  O OD2 . ASP B 192 ? 0.4108 0.4123 1.9963 0.1405  0.1145  -0.0125 192 ASP B OD2 
5798  N N   . HIS B 193 ? 0.3503 0.4168 1.9578 0.1389  0.1195  -0.0099 193 HIS B N   
5799  C CA  . HIS B 193 ? 0.3320 0.4048 1.9451 0.1338  0.1179  -0.0131 193 HIS B CA  
5800  C C   . HIS B 193 ? 0.3356 0.4118 1.9492 0.1325  0.1172  -0.0108 193 HIS B C   
5801  O O   . HIS B 193 ? 0.3344 0.4228 1.9526 0.1314  0.1164  -0.0140 193 HIS B O   
5802  C CB  . HIS B 193 ? 0.3218 0.4099 1.9413 0.1339  0.1177  -0.0167 193 HIS B CB  
5803  C CG  . HIS B 193 ? 0.3205 0.4103 1.9419 0.1333  0.1187  -0.0175 193 HIS B CG  
5804  N ND1 . HIS B 193 ? 0.3179 0.4220 1.9422 0.1359  0.1197  -0.0176 193 HIS B ND1 
5805  C CD2 . HIS B 193 ? 0.3253 0.4082 1.9465 0.1303  0.1190  -0.0172 193 HIS B CD2 
5806  C CE1 . HIS B 193 ? 0.3254 0.4322 1.9526 0.1334  0.1208  -0.0175 193 HIS B CE1 
5807  N NE2 . HIS B 193 ? 0.3317 0.4254 1.9564 0.1301  0.1206  -0.0166 193 HIS B NE2 
5808  N N   . ASN B 194 ? 0.3469 0.4130 1.9560 0.1326  0.1174  -0.0053 194 ASN B N   
5809  C CA  . ASN B 194 ? 0.3406 0.4098 1.9507 0.1291  0.1169  -0.0006 194 ASN B CA  
5810  C C   . ASN B 194 ? 0.3308 0.4221 1.9443 0.1305  0.1178  -0.0007 194 ASN B C   
5811  O O   . ASN B 194 ? 0.3242 0.4258 1.9413 0.1279  0.1174  -0.0032 194 ASN B O   
5812  C CB  . ASN B 194 ? 0.3303 0.3947 1.9424 0.1235  0.1152  -0.0031 194 ASN B CB  
5813  C CG  . ASN B 194 ? 0.3382 0.4094 1.9526 0.1188  0.1152  0.0029  194 ASN B CG  
5814  O OD1 . ASN B 194 ? 0.3684 0.4341 1.9805 0.1176  0.1156  0.0108  194 ASN B OD1 
5815  N ND2 . ASN B 194 ? 0.3316 0.4159 1.9511 0.1163  0.1146  0.0000  194 ASN B ND2 
5816  N N   . GLU B 195 ? 0.3298 0.4302 1.9420 0.1355  0.1186  0.0010  195 GLU B N   
5817  C CA  . GLU B 195 ? 0.3189 0.4431 1.9331 0.1377  0.1188  -0.0007 195 GLU B CA  
5818  C C   . GLU B 195 ? 0.3183 0.4500 1.9288 0.1430  0.1195  0.0072  195 GLU B C   
5819  O O   . GLU B 195 ? 0.3117 0.4296 1.9198 0.1464  0.1197  0.0112  195 GLU B O   
5820  C CB  . GLU B 195 ? 0.3048 0.4364 1.9240 0.1379  0.1173  -0.0122 195 GLU B CB  
5821  C CG  . GLU B 195 ? 0.3074 0.4327 1.9272 0.1396  0.1173  -0.0134 195 GLU B CG  
5822  C CD  . GLU B 195 ? 0.3115 0.4436 1.9377 0.1377  0.1155  -0.0226 195 GLU B CD  
5823  O OE1 . GLU B 195 ? 0.3214 0.4590 1.9521 0.1357  0.1134  -0.0304 195 GLU B OE1 
5824  O OE2 . GLU B 195 ? 0.3144 0.4463 1.9419 0.1384  0.1161  -0.0220 195 GLU B OE2 
5825  N N   . GLY B 196 ? 0.3113 0.4666 1.9212 0.1450  0.1197  0.0093  196 GLY B N   
5826  C CA  . GLY B 196 ? 0.3074 0.4728 1.9132 0.1506  0.1199  0.0194  196 GLY B CA  
5827  C C   . GLY B 196 ? 0.3174 0.4589 1.9198 0.1513  0.1203  0.0319  196 GLY B C   
5828  O O   . GLY B 196 ? 0.3073 0.4364 1.9094 0.1455  0.1208  0.0378  196 GLY B O   
5829  N N   . GLN B 197 ? 0.3311 0.4655 1.9320 0.1585  0.1197  0.0346  197 GLN B N   
5830  C CA  . GLN B 197 ? 0.3511 0.4621 1.9487 0.1619  0.1192  0.0453  197 GLN B CA  
5831  C C   . GLN B 197 ? 0.3740 0.4558 1.9717 0.1564  0.1188  0.0418  197 GLN B C   
5832  O O   . GLN B 197 ? 0.4027 0.4642 1.9987 0.1546  0.1177  0.0508  197 GLN B O   
5833  C CB  . GLN B 197 ? 0.3535 0.4660 1.9505 0.1729  0.1185  0.0453  197 GLN B CB  
5834  C CG  . GLN B 197 ? 0.3532 0.4964 1.9499 0.1787  0.1179  0.0497  197 GLN B CG  
5835  C CD  . GLN B 197 ? 0.3361 0.5004 1.9373 0.1806  0.1176  0.0372  197 GLN B CD  
5836  O OE1 . GLN B 197 ? 0.3183 0.4948 1.9228 0.1738  0.1176  0.0268  197 GLN B OE1 
5837  N NE2 . GLN B 197 ? 0.3377 0.5061 1.9400 0.1901  0.1169  0.0381  197 GLN B NE2 
5838  N N   . THR B 198 ? 0.3680 0.4477 1.9678 0.1531  0.1192  0.0295  198 THR B N   
5839  C CA  . THR B 198 ? 0.3744 0.4305 1.9734 0.1485  0.1184  0.0253  198 THR B CA  
5840  C C   . THR B 198 ? 0.3608 0.4181 1.9622 0.1384  0.1180  0.0260  198 THR B C   
5841  O O   . THR B 198 ? 0.3572 0.3989 1.9585 0.1334  0.1167  0.0221  198 THR B O   
5842  C CB  . THR B 198 ? 0.3744 0.4289 1.9737 0.1501  0.1189  0.0141  198 THR B CB  
5843  O OG1 . THR B 198 ? 0.3665 0.4379 1.9702 0.1455  0.1194  0.0080  198 THR B OG1 
5844  C CG2 . THR B 198 ? 0.3716 0.4277 1.9694 0.1602  0.1197  0.0133  198 THR B CG2 
5845  N N   . ALA B 199 ? 0.3613 0.4408 1.9649 0.1362  0.1191  0.0298  199 ALA B N   
5846  C CA  . ALA B 199 ? 0.3719 0.4588 1.9788 0.1279  0.1193  0.0316  199 ALA B CA  
5847  C C   . ALA B 199 ? 0.3950 0.4803 2.0013 0.1238  0.1195  0.0468  199 ALA B C   
5848  O O   . ALA B 199 ? 0.3952 0.4803 2.0048 0.1150  0.1194  0.0508  199 ALA B O   
5849  C CB  . ALA B 199 ? 0.3574 0.4719 1.9673 0.1286  0.1205  0.0248  199 ALA B CB  
5850  N N   . THR B 200 ? 0.4161 0.5020 2.0188 0.1300  0.1197  0.0561  200 THR B N   
5851  C CA  . THR B 200 ? 0.4350 0.5175 2.0369 0.1270  0.1196  0.0735  200 THR B CA  
5852  C C   . THR B 200 ? 0.4626 0.5073 2.0641 0.1249  0.1165  0.0775  200 THR B C   
5853  O O   . THR B 200 ? 0.5029 0.5364 2.1074 0.1147  0.1153  0.0860  200 THR B O   
5854  C CB  . THR B 200 ? 0.4480 0.5489 2.0459 0.1360  0.1204  0.0821  200 THR B CB  
5855  O OG1 . THR B 200 ? 0.4315 0.5222 2.0271 0.1467  0.1191  0.0763  200 THR B OG1 
5856  C CG2 . THR B 200 ? 0.4334 0.5733 2.0313 0.1367  0.1227  0.0775  200 THR B CG2 
5857  N N   . MET B 201 ? 0.4600 0.4866 2.0584 0.1343  0.1150  0.0705  201 MET B N   
5858  C CA  . MET B 201 ? 0.4730 0.4643 2.0698 0.1368  0.1117  0.0738  201 MET B CA  
5859  C C   . MET B 201 ? 0.4670 0.4374 2.0636 0.1336  0.1097  0.0592  201 MET B C   
5860  O O   . MET B 201 ? 0.4617 0.4014 2.0575 0.1324  0.1060  0.0587  201 MET B O   
5861  C CB  . MET B 201 ? 0.4766 0.4662 2.0698 0.1521  0.1115  0.0752  201 MET B CB  
5862  C CG  . MET B 201 ? 0.4818 0.4890 2.0742 0.1560  0.1121  0.0918  201 MET B CG  
5863  S SD  . MET B 201 ? 0.4827 0.5015 2.0722 0.1747  0.1120  0.0916  201 MET B SD  
5864  C CE  . MET B 201 ? 0.4594 0.5213 2.0501 0.1733  0.1153  0.0798  201 MET B CE  
5865  N N   . GLY B 202 ? 0.4540 0.4413 2.0511 0.1322  0.1116  0.0472  202 GLY B N   
5866  C CA  . GLY B 202 ? 0.4560 0.4299 2.0511 0.1323  0.1102  0.0335  202 GLY B CA  
5867  C C   . GLY B 202 ? 0.4607 0.4275 2.0512 0.1455  0.1106  0.0271  202 GLY B C   
5868  O O   . GLY B 202 ? 0.4783 0.4448 2.0679 0.1543  0.1109  0.0339  202 GLY B O   
5869  N N   . PHE B 203 ? 0.4475 0.4114 2.0352 0.1472  0.1107  0.0147  203 PHE B N   
5870  C CA  . PHE B 203 ? 0.4506 0.4205 2.0352 0.1586  0.1127  0.0080  203 PHE B CA  
5871  C C   . PHE B 203 ? 0.4721 0.4193 2.0529 0.1690  0.1106  0.0079  203 PHE B C   
5872  O O   . PHE B 203 ? 0.4770 0.4304 2.0583 0.1796  0.1117  0.0124  203 PHE B O   
5873  C CB  . PHE B 203 ? 0.4451 0.4209 2.0276 0.1559  0.1136  -0.0027 203 PHE B CB  
5874  C CG  . PHE B 203 ? 0.4497 0.4407 2.0307 0.1645  0.1169  -0.0082 203 PHE B CG  
5875  C CD1 . PHE B 203 ? 0.4447 0.4563 2.0300 0.1689  0.1194  -0.0042 203 PHE B CD1 
5876  C CD2 . PHE B 203 ? 0.4581 0.4458 2.0336 0.1675  0.1173  -0.0171 203 PHE B CD2 
5877  C CE1 . PHE B 203 ? 0.4421 0.4702 2.0280 0.1747  0.1223  -0.0084 203 PHE B CE1 
5878  C CE2 . PHE B 203 ? 0.4593 0.4649 2.0343 0.1740  0.1209  -0.0204 203 PHE B CE2 
5879  C CZ  . PHE B 203 ? 0.4507 0.4763 2.0318 0.1770  0.1234  -0.0157 203 PHE B CZ  
5880  N N   . LYS B 204 ? 0.4802 0.4013 2.0579 0.1661  0.1068  0.0024  204 LYS B N   
5881  C CA  . LYS B 204 ? 0.4983 0.3910 2.0729 0.1754  0.1033  0.0004  204 LYS B CA  
5882  C C   . LYS B 204 ? 0.4978 0.3869 2.0756 0.1815  0.1029  0.0147  204 LYS B C   
5883  O O   . LYS B 204 ? 0.5087 0.4014 2.0852 0.1965  0.1040  0.0144  204 LYS B O   
5884  C CB  . LYS B 204 ? 0.5143 0.3777 2.0880 0.1660  0.0977  -0.0039 204 LYS B CB  
5885  C CG  . LYS B 204 ? 0.5574 0.3852 2.1293 0.1736  0.0925  -0.0056 204 LYS B CG  
5886  C CD  . LYS B 204 ? 0.5911 0.3895 2.1658 0.1597  0.0860  -0.0051 204 LYS B CD  
5887  C CE  . LYS B 204 ? 0.6418 0.4003 2.2171 0.1658  0.0800  -0.0034 204 LYS B CE  
5888  N NZ  . LYS B 204 ? 0.6671 0.4027 2.2487 0.1475  0.0742  0.0034  204 LYS B NZ  
5889  N N   . ASP B 205 ? 0.4833 0.3698 2.0654 0.1701  0.1017  0.0279  205 ASP B N   
5890  C CA  . ASP B 205 ? 0.5002 0.3788 2.0846 0.1738  0.1003  0.0442  205 ASP B CA  
5891  C C   . ASP B 205 ? 0.4923 0.4006 2.0768 0.1846  0.1040  0.0501  205 ASP B C   
5892  O O   . ASP B 205 ? 0.5128 0.4135 2.0970 0.1965  0.1025  0.0583  205 ASP B O   
5893  C CB  . ASP B 205 ? 0.4981 0.3727 2.0871 0.1576  0.0988  0.0580  205 ASP B CB  
5894  C CG  . ASP B 205 ? 0.5143 0.3541 2.1052 0.1470  0.0932  0.0562  205 ASP B CG  
5895  O OD1 . ASP B 205 ? 0.5174 0.3344 2.1047 0.1527  0.0900  0.0415  205 ASP B OD1 
5896  O OD2 . ASP B 205 ? 0.5175 0.3556 2.1136 0.1328  0.0921  0.0692  205 ASP B OD2 
5897  N N   . TYR B 206 ? 0.4666 0.4077 2.0523 0.1807  0.1081  0.0456  206 TYR B N   
5898  C CA  . TYR B 206 ? 0.4604 0.4317 2.0471 0.1893  0.1109  0.0485  206 TYR B CA  
5899  C C   . TYR B 206 ? 0.4674 0.4363 2.0525 0.2058  0.1108  0.0424  206 TYR B C   
5900  O O   . TYR B 206 ? 0.4673 0.4432 2.0531 0.2172  0.1101  0.0507  206 TYR B O   
5901  C CB  . TYR B 206 ? 0.4477 0.4490 2.0365 0.1835  0.1143  0.0400  206 TYR B CB  
5902  C CG  . TYR B 206 ? 0.4507 0.4839 2.0418 0.1905  0.1161  0.0408  206 TYR B CG  
5903  C CD1 . TYR B 206 ? 0.4676 0.5132 2.0588 0.1959  0.1152  0.0532  206 TYR B CD1 
5904  C CD2 . TYR B 206 ? 0.4415 0.4936 2.0350 0.1908  0.1183  0.0298  206 TYR B CD2 
5905  C CE1 . TYR B 206 ? 0.4681 0.5456 2.0617 0.2015  0.1161  0.0525  206 TYR B CE1 
5906  C CE2 . TYR B 206 ? 0.4386 0.5204 2.0357 0.1949  0.1192  0.0295  206 TYR B CE2 
5907  C CZ  . TYR B 206 ? 0.4584 0.5535 2.0554 0.2005  0.1179  0.0399  206 TYR B CZ  
5908  O OH  . TYR B 206 ? 0.4622 0.5889 2.0631 0.2042  0.1179  0.0381  206 TYR B OH  
5909  N N   . ILE B 207 ? 0.4757 0.4378 2.0586 0.2074  0.1116  0.0281  207 ILE B N   
5910  C CA  . ILE B 207 ? 0.4982 0.4649 2.0798 0.2228  0.1128  0.0196  207 ILE B CA  
5911  C C   . ILE B 207 ? 0.5638 0.4990 2.1430 0.2356  0.1087  0.0219  207 ILE B C   
5912  O O   . ILE B 207 ? 0.6068 0.5475 2.1867 0.2522  0.1086  0.0229  207 ILE B O   
5913  C CB  . ILE B 207 ? 0.4757 0.4474 2.0547 0.2193  0.1152  0.0049  207 ILE B CB  
5914  C CG1 . ILE B 207 ? 0.4318 0.4328 2.0144 0.2079  0.1186  0.0037  207 ILE B CG1 
5915  C CG2 . ILE B 207 ? 0.4854 0.4608 2.0619 0.2354  0.1167  -0.0048 207 ILE B CG2 
5916  C CD1 . ILE B 207 ? 0.4132 0.4441 2.0016 0.2102  0.1203  0.0100  207 ILE B CD1 
5917  N N   . LYS B 208 ? 0.5957 0.4972 2.1731 0.2277  0.1047  0.0230  208 LYS B N   
5918  C CA  . LYS B 208 ? 0.6411 0.5065 2.2176 0.2373  0.0995  0.0267  208 LYS B CA  
5919  C C   . LYS B 208 ? 0.6547 0.5260 2.2343 0.2451  0.0986  0.0449  208 LYS B C   
5920  O O   . LYS B 208 ? 0.6946 0.5507 2.2741 0.2621  0.0957  0.0473  208 LYS B O   
5921  C CB  . LYS B 208 ? 0.6702 0.5020 2.2466 0.2221  0.0949  0.0284  208 LYS B CB  
5922  C CG  . LYS B 208 ? 0.7206 0.5079 2.2965 0.2303  0.0883  0.0284  208 LYS B CG  
5923  C CD  . LYS B 208 ? 0.7420 0.4962 2.3183 0.2148  0.0830  0.0238  208 LYS B CD  
5924  C CE  . LYS B 208 ? 0.8006 0.5131 2.3745 0.2266  0.0765  0.0122  208 LYS B CE  
5925  N NZ  . LYS B 208 ? 0.8517 0.5269 2.4288 0.2103  0.0695  0.0138  208 LYS B NZ  
5926  N N   . GLY B 209 ? 0.6331 0.5277 2.2151 0.2333  0.1007  0.0574  209 GLY B N   
5927  C CA  . GLY B 209 ? 0.6413 0.5461 2.2251 0.2380  0.0998  0.0764  209 GLY B CA  
5928  C C   . GLY B 209 ? 0.6311 0.5638 2.2157 0.2560  0.1013  0.0758  209 GLY B C   
5929  O O   . GLY B 209 ? 0.6417 0.5750 2.2269 0.2665  0.0989  0.0903  209 GLY B O   
5930  N N   . LEU B 210 ? 0.6052 0.5632 2.1905 0.2585  0.1052  0.0605  210 LEU B N   
5931  C CA  . LEU B 210 ? 0.5963 0.5848 2.1842 0.2740  0.1067  0.0582  210 LEU B CA  
5932  C C   . LEU B 210 ? 0.6328 0.6011 2.2199 0.2943  0.1046  0.0524  210 LEU B C   
5933  O O   . LEU B 210 ? 0.6343 0.6191 2.2241 0.3113  0.1038  0.0566  210 LEU B O   
5934  C CB  . LEU B 210 ? 0.5537 0.5762 2.1441 0.2669  0.1115  0.0455  210 LEU B CB  
5935  C CG  . LEU B 210 ? 0.5279 0.5721 2.1198 0.2495  0.1132  0.0488  210 LEU B CG  
5936  C CD1 . LEU B 210 ? 0.5078 0.5787 2.1031 0.2428  0.1169  0.0360  210 LEU B CD1 
5937  C CD2 . LEU B 210 ? 0.5225 0.5893 2.1159 0.2524  0.1116  0.0627  210 LEU B CD2 
5938  N N   . ASN B 211 ? 0.6461 0.5795 2.2296 0.2932  0.1030  0.0420  211 ASN B N   
5939  C CA  . ASN B 211 ? 0.6501 0.5620 2.2319 0.3128  0.1008  0.0319  211 ASN B CA  
5940  C C   . ASN B 211 ? 0.7057 0.5828 2.2881 0.3241  0.0944  0.0453  211 ASN B C   
5941  O O   . ASN B 211 ? 0.7304 0.5980 2.3133 0.3462  0.0920  0.0419  211 ASN B O   
5942  C CB  . ASN B 211 ? 0.6367 0.5239 2.2135 0.3064  0.1005  0.0149  211 ASN B CB  
5943  C CG  . ASN B 211 ? 0.6234 0.5140 2.1977 0.3252  0.1018  -0.0027 211 ASN B CG  
5944  O OD1 . ASN B 211 ? 0.6328 0.4910 2.2023 0.3290  0.0985  -0.0152 211 ASN B OD1 
5945  N ND2 . ASN B 211 ? 0.5952 0.5277 2.1728 0.3352  0.1067  -0.0053 211 ASN B ND2 
5946  N N   . GLU B 212 ? 0.7215 0.5788 2.3040 0.3089  0.0915  0.0609  212 GLU B N   
5947  C CA  . GLU B 212 ? 0.7548 0.5792 2.3385 0.3159  0.0853  0.0785  212 GLU B CA  
5948  C C   . GLU B 212 ? 0.7347 0.5907 2.3208 0.3273  0.0857  0.0957  212 GLU B C   
5949  O O   . GLU B 212 ? 0.7516 0.5917 2.3391 0.3463  0.0812  0.1049  212 GLU B O   
5950  C CB  . GLU B 212 ? 0.7678 0.5641 2.3516 0.2937  0.0827  0.0901  212 GLU B CB  
5951  C CG  . GLU B 212 ? 0.7935 0.5482 2.3758 0.2867  0.0791  0.0746  212 GLU B CG  
5952  C CD  . GLU B 212 ? 0.7764 0.5231 2.3596 0.2600  0.0791  0.0782  212 GLU B CD  
5953  O OE1 . GLU B 212 ? 0.7433 0.5172 2.3282 0.2474  0.0824  0.0929  212 GLU B OE1 
5954  O OE2 . GLU B 212 ? 0.7921 0.5079 2.3745 0.2525  0.0757  0.0653  212 GLU B OE2 
5955  N N   . LEU B 213 ? 0.6805 0.5812 2.2672 0.3161  0.0905  0.0994  213 LEU B N   
5956  C CA  . LEU B 213 ? 0.6552 0.5936 2.2438 0.3259  0.0908  0.1123  213 LEU B CA  
5957  C C   . LEU B 213 ? 0.6543 0.6081 2.2458 0.3499  0.0908  0.1024  213 LEU B C   
5958  O O   . LEU B 213 ? 0.6971 0.6530 2.2902 0.3678  0.0871  0.1149  213 LEU B O   
5959  C CB  . LEU B 213 ? 0.6058 0.5899 2.1948 0.3103  0.0953  0.1129  213 LEU B CB  
5960  C CG  . LEU B 213 ? 0.5941 0.5767 2.1806 0.2909  0.0955  0.1274  213 LEU B CG  
5961  C CD1 . LEU B 213 ? 0.5625 0.5961 2.1494 0.2854  0.0983  0.1295  213 LEU B CD1 
5962  C CD2 . LEU B 213 ? 0.6257 0.5794 2.2107 0.2929  0.0907  0.1508  213 LEU B CD2 
5963  N N   . ASN B 214 ? 0.6256 0.5891 2.2177 0.3508  0.0947  0.0809  214 ASN B N   
5964  C CA  . ASN B 214 ? 0.6241 0.6102 2.2198 0.3720  0.0961  0.0697  214 ASN B CA  
5965  C C   . ASN B 214 ? 0.6736 0.6249 2.2692 0.3964  0.0907  0.0713  214 ASN B C   
5966  O O   . ASN B 214 ? 0.6543 0.6274 2.2541 0.4182  0.0898  0.0726  214 ASN B O   
5967  C CB  . ASN B 214 ? 0.5948 0.5964 2.1902 0.3656  0.1018  0.0484  214 ASN B CB  
5968  C CG  . ASN B 214 ? 0.5531 0.5983 2.1517 0.3482  0.1065  0.0475  214 ASN B CG  
5969  O OD1 . ASN B 214 ? 0.5388 0.6099 2.1403 0.3462  0.1055  0.0597  214 ASN B OD1 
5970  N ND2 . ASN B 214 ? 0.5266 0.5795 2.1242 0.3355  0.1110  0.0337  214 ASN B ND2 
5971  N N   . GLY B 215 ? 0.7262 0.6240 2.3178 0.3925  0.0867  0.0703  215 GLY B N   
5972  C CA  . GLY B 215 ? 0.7787 0.6321 2.3704 0.4126  0.0798  0.0736  215 GLY B CA  
5973  C C   . GLY B 215 ? 0.8187 0.6315 2.4068 0.4166  0.0780  0.0522  215 GLY B C   
5974  O O   . GLY B 215 ? 0.8991 0.6712 2.4875 0.4344  0.0716  0.0512  215 GLY B O   
5975  N N   . LEU B 216 ? 0.7968 0.6203 2.3815 0.4015  0.0829  0.0346  216 LEU B N   
5976  C CA  . LEU B 216 ? 0.8170 0.6065 2.3968 0.4034  0.0810  0.0132  216 LEU B CA  
5977  C C   . LEU B 216 ? 0.8217 0.6069 2.4015 0.4345  0.0795  -0.0025 216 LEU B C   
5978  O O   . LEU B 216 ? 0.8381 0.5809 2.4143 0.4428  0.0744  -0.0170 216 LEU B O   
5979  C CB  . LEU B 216 ? 0.8741 0.6046 2.4524 0.3911  0.0735  0.0190  216 LEU B CB  
5980  C CG  . LEU B 216 ? 0.8920 0.6192 2.4719 0.3637  0.0733  0.0392  216 LEU B CG  
5981  C CD1 . LEU B 216 ? 0.9109 0.6397 2.4951 0.3680  0.0706  0.0667  216 LEU B CD1 
5982  C CD2 . LEU B 216 ? 0.9311 0.6074 2.5096 0.3475  0.0674  0.0351  216 LEU B CD2 
5983  N N   . ASP B 217 ? 0.7863 0.6172 2.3705 0.4519  0.0837  -0.0015 217 ASP B N   
5984  C CA  . ASP B 217 ? 0.7987 0.6292 2.3846 0.4844  0.0819  -0.0126 217 ASP B CA  
5985  C C   . ASP B 217 ? 0.7765 0.6577 2.3621 0.4921  0.0901  -0.0320 217 ASP B C   
5986  O O   . ASP B 217 ? 0.8087 0.7073 2.3970 0.5191  0.0908  -0.0411 217 ASP B O   
5987  C CB  . ASP B 217 ? 0.8069 0.6424 2.3996 0.5013  0.0778  0.0083  217 ASP B CB  
5988  C CG  . ASP B 217 ? 0.7615 0.6518 2.3591 0.4905  0.0826  0.0250  217 ASP B CG  
5989  O OD1 . ASP B 217 ? 0.7365 0.6695 2.3343 0.4771  0.0900  0.0162  217 ASP B OD1 
5990  O OD2 . ASP B 217 ? 0.7600 0.6488 2.3608 0.4944  0.0784  0.0468  217 ASP B OD2 
5991  N N   . LYS B 218 ? 0.7488 0.6551 2.3312 0.4691  0.0965  -0.0378 218 LYS B N   
5992  C CA  . LYS B 218 ? 0.7340 0.6884 2.3161 0.4736  0.1046  -0.0537 218 LYS B CA  
5993  C C   . LYS B 218 ? 0.7007 0.6496 2.2748 0.4512  0.1078  -0.0652 218 LYS B C   
5994  O O   . LYS B 218 ? 0.6997 0.6176 2.2706 0.4300  0.1045  -0.0586 218 LYS B O   
5995  C CB  . LYS B 218 ? 0.7166 0.7315 2.3073 0.4679  0.1107  -0.0423 218 LYS B CB  
5996  C CG  . LYS B 218 ? 0.7546 0.7819 2.3538 0.4845  0.1072  -0.0266 218 LYS B CG  
5997  C CD  . LYS B 218 ? 0.7497 0.8399 2.3584 0.4801  0.1121  -0.0178 218 LYS B CD  
5998  C CE  . LYS B 218 ? 0.8035 0.9103 2.4200 0.5071  0.1085  -0.0094 218 LYS B CE  
5999  N NZ  . LYS B 218 ? 0.7897 0.9432 2.4146 0.4978  0.1096  0.0051  218 LYS B NZ  
6000  N N   . PRO B 219 ? 0.6776 0.6593 2.2483 0.4554  0.1143  -0.0817 219 PRO B N   
6001  C CA  . PRO B 219 ? 0.6604 0.6515 2.2248 0.4320  0.1185  -0.0876 219 PRO B CA  
6002  C C   . PRO B 219 ? 0.6213 0.6345 2.1915 0.4064  0.1214  -0.0699 219 PRO B C   
6003  O O   . PRO B 219 ? 0.6160 0.6609 2.1953 0.4096  0.1233  -0.0582 219 PRO B O   
6004  C CB  . PRO B 219 ? 0.6515 0.6873 2.2139 0.4451  0.1260  -0.1028 219 PRO B CB  
6005  C CG  . PRO B 219 ? 0.6903 0.7156 2.2533 0.4779  0.1228  -0.1133 219 PRO B CG  
6006  C CD  . PRO B 219 ? 0.6935 0.7064 2.2660 0.4831  0.1179  -0.0945 219 PRO B CD  
6007  N N   . PHE B 220 ? 0.5950 0.5917 2.1604 0.3825  0.1208  -0.0689 220 PHE B N   
6008  C CA  . PHE B 220 ? 0.5609 0.5774 2.1310 0.3586  0.1235  -0.0554 220 PHE B CA  
6009  C C   . PHE B 220 ? 0.5384 0.5720 2.1036 0.3427  0.1282  -0.0631 220 PHE B C   
6010  O O   . PHE B 220 ? 0.5451 0.5539 2.1016 0.3380  0.1262  -0.0731 220 PHE B O   
6011  C CB  . PHE B 220 ? 0.5639 0.5458 2.1347 0.3443  0.1177  -0.0421 220 PHE B CB  
6012  C CG  . PHE B 220 ? 0.5326 0.5236 2.1043 0.3182  0.1196  -0.0350 220 PHE B CG  
6013  C CD1 . PHE B 220 ? 0.5071 0.5381 2.0857 0.3096  0.1240  -0.0276 220 PHE B CD1 
6014  C CD2 . PHE B 220 ? 0.5395 0.4992 2.1062 0.3026  0.1164  -0.0363 220 PHE B CD2 
6015  C CE1 . PHE B 220 ? 0.4860 0.5231 2.0658 0.2876  0.1251  -0.0226 220 PHE B CE1 
6016  C CE2 . PHE B 220 ? 0.5148 0.4846 2.0830 0.2812  0.1180  -0.0305 220 PHE B CE2 
6017  C CZ  . PHE B 220 ? 0.4814 0.4886 2.0558 0.2744  0.1223  -0.0240 220 PHE B CZ  
6018  N N   . ILE B 221 ? 0.5158 0.5921 2.0871 0.3338  0.1340  -0.0578 221 ILE B N   
6019  C CA  . ILE B 221 ? 0.5038 0.5984 2.0713 0.3197  0.1386  -0.0624 221 ILE B CA  
6020  C C   . ILE B 221 ? 0.4757 0.5808 2.0496 0.2969  0.1393  -0.0501 221 ILE B C   
6021  O O   . ILE B 221 ? 0.4644 0.5795 2.0468 0.2952  0.1383  -0.0400 221 ILE B O   
6022  C CB  . ILE B 221 ? 0.5022 0.6400 2.0711 0.3314  0.1454  -0.0693 221 ILE B CB  
6023  C CG1 . ILE B 221 ? 0.4824 0.6608 2.0647 0.3331  0.1487  -0.0594 221 ILE B CG1 
6024  C CG2 . ILE B 221 ? 0.5360 0.6619 2.0974 0.3559  0.1444  -0.0844 221 ILE B CG2 
6025  C CD1 . ILE B 221 ? 0.4813 0.7083 2.0671 0.3411  0.1561  -0.0641 221 ILE B CD1 
6026  N N   . THR B 222 ? 0.4713 0.5733 2.0406 0.2807  0.1403  -0.0518 222 THR B N   
6027  C CA  . THR B 222 ? 0.4486 0.5641 2.0241 0.2608  0.1415  -0.0425 222 THR B CA  
6028  C C   . THR B 222 ? 0.4509 0.6072 2.0309 0.2578  0.1478  -0.0421 222 THR B C   
6029  O O   . THR B 222 ? 0.4648 0.6319 2.0382 0.2635  0.1512  -0.0494 222 THR B O   
6030  C CB  . THR B 222 ? 0.4384 0.5274 2.0079 0.2457  0.1384  -0.0429 222 THR B CB  
6031  O OG1 . THR B 222 ? 0.4462 0.5347 2.0061 0.2478  0.1400  -0.0525 222 THR B OG1 
6032  C CG2 . THR B 222 ? 0.4542 0.5057 2.0210 0.2462  0.1324  -0.0419 222 THR B CG2 
6033  N N   . THR B 223 ? 0.4461 0.6262 2.0376 0.2487  0.1489  -0.0335 223 THR B N   
6034  C CA  . THR B 223 ? 0.4474 0.6676 2.0466 0.2438  0.1543  -0.0307 223 THR B CA  
6035  C C   . THR B 223 ? 0.4559 0.6774 2.0577 0.2225  0.1547  -0.0251 223 THR B C   
6036  O O   . THR B 223 ? 0.4462 0.6932 2.0508 0.2164  0.1592  -0.0226 223 THR B O   
6037  C CB  . THR B 223 ? 0.4323 0.6778 2.0437 0.2493  0.1541  -0.0263 223 THR B CB  
6038  O OG1 . THR B 223 ? 0.4120 0.6309 2.0226 0.2506  0.1484  -0.0236 223 THR B OG1 
6039  C CG2 . THR B 223 ? 0.4622 0.7256 2.0732 0.2715  0.1567  -0.0317 223 THR B CG2 
6040  N N   . GLU B 224 ? 0.4704 0.6644 2.0712 0.2120  0.1499  -0.0227 224 GLU B N   
6041  C CA  . GLU B 224 ? 0.4758 0.6630 2.0777 0.1946  0.1490  -0.0187 224 GLU B CA  
6042  C C   . GLU B 224 ? 0.4457 0.5969 2.0401 0.1915  0.1442  -0.0206 224 GLU B C   
6043  O O   . GLU B 224 ? 0.4180 0.5529 2.0106 0.1983  0.1412  -0.0219 224 GLU B O   
6044  C CB  . GLU B 224 ? 0.5222 0.7244 2.1377 0.1818  0.1478  -0.0127 224 GLU B CB  
6045  C CG  . GLU B 224 ? 0.5765 0.8163 2.2037 0.1788  0.1514  -0.0091 224 GLU B CG  
6046  C CD  . GLU B 224 ? 0.6333 0.8836 2.2745 0.1642  0.1485  -0.0052 224 GLU B CD  
6047  O OE1 . GLU B 224 ? 0.6776 0.9132 2.3202 0.1621  0.1437  -0.0068 224 GLU B OE1 
6048  O OE2 . GLU B 224 ? 0.6537 0.9283 2.3052 0.1542  0.1507  -0.0008 224 GLU B OE2 
6049  N N   . PHE B 225 ? 0.4247 0.5653 2.0154 0.1808  0.1433  -0.0196 225 PHE B N   
6050  C CA  . PHE B 225 ? 0.3934 0.5072 1.9808 0.1742  0.1387  -0.0198 225 PHE B CA  
6051  C C   . PHE B 225 ? 0.3759 0.4881 1.9612 0.1637  0.1384  -0.0175 225 PHE B C   
6052  O O   . PHE B 225 ? 0.3604 0.4820 1.9393 0.1657  0.1412  -0.0183 225 PHE B O   
6053  C CB  . PHE B 225 ? 0.4056 0.4954 1.9838 0.1830  0.1361  -0.0257 225 PHE B CB  
6054  C CG  . PHE B 225 ? 0.4045 0.4908 1.9715 0.1906  0.1372  -0.0332 225 PHE B CG  
6055  C CD1 . PHE B 225 ? 0.4075 0.5048 1.9715 0.2047  0.1401  -0.0384 225 PHE B CD1 
6056  C CD2 . PHE B 225 ? 0.3995 0.4733 1.9589 0.1849  0.1349  -0.0362 225 PHE B CD2 
6057  C CE1 . PHE B 225 ? 0.4239 0.5199 1.9767 0.2129  0.1410  -0.0476 225 PHE B CE1 
6058  C CE2 . PHE B 225 ? 0.4076 0.4807 1.9557 0.1921  0.1353  -0.0447 225 PHE B CE2 
6059  C CZ  . PHE B 225 ? 0.4256 0.5100 1.9701 0.2061  0.1385  -0.0510 225 PHE B CZ  
6060  N N   . GLY B 226 ? 0.3685 0.4705 1.9587 0.1536  0.1351  -0.0144 226 GLY B N   
6061  C CA  . GLY B 226 ? 0.3655 0.4634 1.9541 0.1452  0.1338  -0.0112 226 GLY B CA  
6062  C C   . GLY B 226 ? 0.3467 0.4393 1.9447 0.1354  0.1305  -0.0077 226 GLY B C   
6063  O O   . GLY B 226 ? 0.3544 0.4433 1.9583 0.1347  0.1285  -0.0093 226 GLY B O   
6064  N N   . TYR B 227 ? 0.3252 0.4174 1.9242 0.1286  0.1297  -0.0027 227 TYR B N   
6065  C CA  . TYR B 227 ? 0.3125 0.3935 1.9182 0.1220  0.1254  -0.0014 227 TYR B CA  
6066  C C   . TYR B 227 ? 0.3132 0.3986 1.9253 0.1141  0.1251  0.0064  227 TYR B C   
6067  O O   . TYR B 227 ? 0.3163 0.4103 1.9231 0.1134  0.1278  0.0122  227 TYR B O   
6068  C CB  . TYR B 227 ? 0.3131 0.3796 1.9117 0.1237  0.1221  -0.0038 227 TYR B CB  
6069  C CG  . TYR B 227 ? 0.3012 0.3601 1.8965 0.1285  0.1212  -0.0099 227 TYR B CG  
6070  C CD1 . TYR B 227 ? 0.2859 0.3428 1.8883 0.1275  0.1196  -0.0117 227 TYR B CD1 
6071  C CD2 . TYR B 227 ? 0.3156 0.3699 1.9010 0.1339  0.1219  -0.0135 227 TYR B CD2 
6072  C CE1 . TYR B 227 ? 0.2892 0.3407 1.8890 0.1308  0.1192  -0.0142 227 TYR B CE1 
6073  C CE2 . TYR B 227 ? 0.3099 0.3543 1.8936 0.1370  0.1206  -0.0172 227 TYR B CE2 
6074  C CZ  . TYR B 227 ? 0.3004 0.3439 1.8914 0.1349  0.1195  -0.0161 227 TYR B CZ  
6075  O OH  . TYR B 227 ? 0.2954 0.3306 1.8853 0.1367  0.1184  -0.0168 227 TYR B OH  
6076  N N   . SER B 228 ? 0.3125 0.3914 1.9356 0.1084  0.1216  0.0063  228 SER B N   
6077  C CA  . SER B 228 ? 0.3145 0.3926 1.9464 0.0997  0.1201  0.0138  228 SER B CA  
6078  C C   . SER B 228 ? 0.3137 0.3753 1.9446 0.0988  0.1156  0.0173  228 SER B C   
6079  O O   . SER B 228 ? 0.3082 0.3595 1.9389 0.1027  0.1123  0.0109  228 SER B O   
6080  C CB  . SER B 228 ? 0.3146 0.3940 1.9603 0.0940  0.1177  0.0102  228 SER B CB  
6081  O OG  . SER B 228 ? 0.3252 0.3919 1.9802 0.0863  0.1133  0.0148  228 SER B OG  
6082  N N   . VAL B 229 ? 0.3218 0.3831 1.9531 0.0935  0.1154  0.0285  229 VAL B N   
6083  C CA  . VAL B 229 ? 0.3314 0.3787 1.9612 0.0940  0.1109  0.0340  229 VAL B CA  
6084  C C   . VAL B 229 ? 0.3454 0.3790 1.9891 0.0867  0.1062  0.0394  229 VAL B C   
6085  O O   . VAL B 229 ? 0.3599 0.3845 2.0039 0.0847  0.1033  0.0501  229 VAL B O   
6086  C CB  . VAL B 229 ? 0.3376 0.3939 1.9547 0.0953  0.1132  0.0436  229 VAL B CB  
6087  C CG1 . VAL B 229 ? 0.3254 0.3886 1.9288 0.1035  0.1153  0.0351  229 VAL B CG1 
6088  C CG2 . VAL B 229 ? 0.3482 0.4207 1.9663 0.0885  0.1180  0.0550  229 VAL B CG2 
6089  N N   . SER B 230 ? 0.3464 0.3777 2.0016 0.0831  0.1049  0.0317  230 SER B N   
6090  C CA  . SER B 230 ? 0.3680 0.3843 2.0377 0.0755  0.0996  0.0341  230 SER B CA  
6091  C C   . SER B 230 ? 0.3894 0.3839 2.0616 0.0811  0.0929  0.0319  230 SER B C   
6092  O O   . SER B 230 ? 0.3963 0.3903 2.0639 0.0901  0.0920  0.0220  230 SER B O   
6093  C CB  . SER B 230 ? 0.3602 0.3814 2.0404 0.0715  0.0988  0.0232  230 SER B CB  
6094  O OG  . SER B 230 ? 0.3417 0.3695 2.0169 0.0801  0.0998  0.0096  230 SER B OG  
6095  N N   . PRO B 231 ? 0.4129 0.3893 2.0932 0.0765  0.0878  0.0417  231 PRO B N   
6096  C CA  . PRO B 231 ? 0.4296 0.3857 2.1132 0.0841  0.0810  0.0392  231 PRO B CA  
6097  C C   . PRO B 231 ? 0.4314 0.3848 2.1198 0.0912  0.0784  0.0195  231 PRO B C   
6098  O O   . PRO B 231 ? 0.4410 0.3910 2.1269 0.1015  0.0758  0.0135  231 PRO B O   
6099  C CB  . PRO B 231 ? 0.4534 0.3879 2.1495 0.0758  0.0754  0.0503  231 PRO B CB  
6100  C CG  . PRO B 231 ? 0.4555 0.4044 2.1494 0.0640  0.0809  0.0661  231 PRO B CG  
6101  C CD  . PRO B 231 ? 0.4322 0.4069 2.1201 0.0638  0.0881  0.0563  231 PRO B CD  
6102  N N   . GLU B 232 ? 0.4316 0.3899 2.1272 0.0856  0.0789  0.0099  232 GLU B N   
6103  C CA  . GLU B 232 ? 0.4271 0.3886 2.1258 0.0920  0.0771  -0.0087 232 GLU B CA  
6104  C C   . GLU B 232 ? 0.4235 0.4012 2.1248 0.0855  0.0801  -0.0156 232 GLU B C   
6105  O O   . GLU B 232 ? 0.4140 0.4022 2.1144 0.0772  0.0842  -0.0060 232 GLU B O   
6106  C CB  . GLU B 232 ? 0.4487 0.3870 2.1592 0.0955  0.0686  -0.0170 232 GLU B CB  
6107  C CG  . GLU B 232 ? 0.4732 0.3959 2.1978 0.0839  0.0637  -0.0165 232 GLU B CG  
6108  C CD  . GLU B 232 ? 0.5048 0.3962 2.2407 0.0870  0.0545  -0.0187 232 GLU B CD  
6109  O OE1 . GLU B 232 ? 0.5192 0.3975 2.2531 0.0899  0.0530  -0.0044 232 GLU B OE1 
6110  O OE2 . GLU B 232 ? 0.5195 0.4000 2.2660 0.0871  0.0485  -0.0349 232 GLU B OE2 
6111  N N   . GLY B 233 ? 0.4218 0.4045 2.1262 0.0903  0.0779  -0.0322 233 GLY B N   
6112  C CA  . GLY B 233 ? 0.4103 0.4107 2.1171 0.0860  0.0796  -0.0403 233 GLY B CA  
6113  C C   . GLY B 233 ? 0.3911 0.4139 2.0856 0.0926  0.0861  -0.0412 233 GLY B C   
6114  O O   . GLY B 233 ? 0.3698 0.3946 2.0543 0.0962  0.0904  -0.0324 233 GLY B O   
6115  N N   . GLY B 234 ? 0.3927 0.4318 2.0880 0.0939  0.0863  -0.0519 234 GLY B N   
6116  C CA  . GLY B 234 ? 0.3967 0.4561 2.0819 0.0986  0.0920  -0.0503 234 GLY B CA  
6117  C C   . GLY B 234 ? 0.4238 0.4913 2.1043 0.1077  0.0916  -0.0600 234 GLY B C   
6118  O O   . GLY B 234 ? 0.4637 0.5307 2.1502 0.1096  0.0869  -0.0724 234 GLY B O   
6119  N N   . ASN B 235 ? 0.4427 0.5180 2.1128 0.1130  0.0964  -0.0544 235 ASN B N   
6120  C CA  . ASN B 235 ? 0.4596 0.5430 2.1249 0.1204  0.0970  -0.0594 235 ASN B CA  
6121  C C   . ASN B 235 ? 0.4199 0.5031 2.0756 0.1227  0.1015  -0.0494 235 ASN B C   
6122  O O   . ASN B 235 ? 0.3962 0.4797 2.0471 0.1208  0.1048  -0.0417 235 ASN B O   
6123  C CB  . ASN B 235 ? 0.5157 0.6196 2.1811 0.1229  0.0966  -0.0680 235 ASN B CB  
6124  C CG  . ASN B 235 ? 0.5916 0.7084 2.2516 0.1299  0.0981  -0.0707 235 ASN B CG  
6125  O OD1 . ASN B 235 ? 0.6967 0.8113 2.3598 0.1339  0.0957  -0.0781 235 ASN B OD1 
6126  N ND2 . ASN B 235 ? 0.5999 0.7305 2.2523 0.1318  0.1021  -0.0639 235 ASN B ND2 
6127  N N   . GLY B 236 ? 0.3988 0.4820 2.0526 0.1268  0.1013  -0.0504 236 GLY B N   
6128  C CA  . GLY B 236 ? 0.3794 0.4594 2.0261 0.1273  0.1039  -0.0422 236 GLY B CA  
6129  C C   . GLY B 236 ? 0.3802 0.4473 2.0236 0.1236  0.1049  -0.0344 236 GLY B C   
6130  O O   . GLY B 236 ? 0.3998 0.4560 2.0466 0.1217  0.1025  -0.0330 236 GLY B O   
6131  N N   . GLN B 237 ? 0.3711 0.4403 2.0076 0.1233  0.1083  -0.0291 237 GLN B N   
6132  C CA  . GLN B 237 ? 0.3806 0.4412 2.0116 0.1217  0.1097  -0.0230 237 GLN B CA  
6133  C C   . GLN B 237 ? 0.3886 0.4520 2.0218 0.1191  0.1111  -0.0210 237 GLN B C   
6134  O O   . GLN B 237 ? 0.3892 0.4483 2.0194 0.1173  0.1122  -0.0160 237 GLN B O   
6135  C CB  . GLN B 237 ? 0.3781 0.4386 2.0009 0.1238  0.1122  -0.0201 237 GLN B CB  
6136  C CG  . GLN B 237 ? 0.3607 0.4190 1.9818 0.1237  0.1109  -0.0200 237 GLN B CG  
6137  C CD  . GLN B 237 ? 0.3726 0.4228 1.9857 0.1237  0.1119  -0.0169 237 GLN B CD  
6138  O OE1 . GLN B 237 ? 0.3738 0.4175 1.9820 0.1236  0.1118  -0.0161 237 GLN B OE1 
6139  N NE2 . GLN B 237 ? 0.3844 0.4353 1.9959 0.1239  0.1126  -0.0150 237 GLN B NE2 
6140  N N   . TYR B 238 ? 0.3936 0.4677 2.0314 0.1191  0.1114  -0.0246 238 TYR B N   
6141  C CA  . TYR B 238 ? 0.3812 0.4616 2.0248 0.1150  0.1118  -0.0237 238 TYR B CA  
6142  C C   . TYR B 238 ? 0.3970 0.4670 2.0485 0.1093  0.1082  -0.0239 238 TYR B C   
6143  O O   . TYR B 238 ? 0.4000 0.4672 2.0583 0.1088  0.1042  -0.0310 238 TYR B O   
6144  C CB  . TYR B 238 ? 0.3645 0.4606 2.0126 0.1159  0.1115  -0.0289 238 TYR B CB  
6145  C CG  . TYR B 238 ? 0.3529 0.4582 2.0096 0.1098  0.1110  -0.0288 238 TYR B CG  
6146  C CD1 . TYR B 238 ? 0.3440 0.4570 1.9990 0.1093  0.1149  -0.0221 238 TYR B CD1 
6147  C CD2 . TYR B 238 ? 0.3553 0.4624 2.0225 0.1043  0.1065  -0.0359 238 TYR B CD2 
6148  C CE1 . TYR B 238 ? 0.3462 0.4716 2.0104 0.1025  0.1149  -0.0207 238 TYR B CE1 
6149  C CE2 . TYR B 238 ? 0.3624 0.4782 2.0392 0.0964  0.1055  -0.0353 238 TYR B CE2 
6150  C CZ  . TYR B 238 ? 0.3505 0.4773 2.0262 0.0951  0.1101  -0.0268 238 TYR B CZ  
6151  O OH  . TYR B 238 ? 0.3280 0.4682 2.0142 0.0865  0.1098  -0.0247 238 TYR B OH  
6152  N N   . GLY B 239 ? 0.3980 0.4618 2.0477 0.1060  0.1093  -0.0159 239 GLY B N   
6153  C CA  . GLY B 239 ? 0.3948 0.4460 2.0510 0.1007  0.1057  -0.0123 239 GLY B CA  
6154  C C   . GLY B 239 ? 0.3836 0.4218 2.0359 0.1047  0.1031  -0.0110 239 GLY B C   
6155  O O   . GLY B 239 ? 0.3712 0.4110 2.0165 0.1103  0.1039  -0.0136 239 GLY B O   
6156  N N   . SER B 240 ? 0.3942 0.4200 2.0520 0.1011  0.0996  -0.0055 240 SER B N   
6157  C CA  . SER B 240 ? 0.4073 0.4203 2.0654 0.1053  0.0953  -0.0048 240 SER B CA  
6158  C C   . SER B 240 ? 0.3944 0.4120 2.0409 0.1103  0.0972  -0.0018 240 SER B C   
6159  O O   . SER B 240 ? 0.4022 0.4170 2.0488 0.1156  0.0944  -0.0055 240 SER B O   
6160  C CB  . SER B 240 ? 0.4101 0.4188 2.0759 0.1099  0.0911  -0.0167 240 SER B CB  
6161  O OG  . SER B 240 ? 0.4207 0.4232 2.0976 0.1048  0.0880  -0.0212 240 SER B OG  
6162  N N   . ASN B 241 ? 0.3671 0.3927 2.0044 0.1085  0.1016  0.0041  241 ASN B N   
6163  C CA  . ASN B 241 ? 0.3493 0.3779 1.9753 0.1121  0.1025  0.0061  241 ASN B CA  
6164  C C   . ASN B 241 ? 0.3451 0.3701 1.9677 0.1111  0.1003  0.0164  241 ASN B C   
6165  O O   . ASN B 241 ? 0.3369 0.3599 1.9631 0.1063  0.1004  0.0250  241 ASN B O   
6166  C CB  . ASN B 241 ? 0.3556 0.3944 1.9728 0.1126  0.1077  0.0051  241 ASN B CB  
6167  C CG  . ASN B 241 ? 0.3548 0.3959 1.9719 0.1157  0.1088  -0.0033 241 ASN B CG  
6168  O OD1 . ASN B 241 ? 0.3599 0.3988 1.9729 0.1182  0.1075  -0.0064 241 ASN B OD1 
6169  N ND2 . ASN B 241 ? 0.3578 0.4047 1.9799 0.1149  0.1109  -0.0061 241 ASN B ND2 
6170  N N   . THR B 242 ? 0.3435 0.3693 1.9591 0.1151  0.0980  0.0162  242 THR B N   
6171  C CA  . THR B 242 ? 0.3569 0.3849 1.9651 0.1152  0.0965  0.0260  242 THR B CA  
6172  C C   . THR B 242 ? 0.3692 0.4093 1.9652 0.1141  0.1015  0.0279  242 THR B C   
6173  O O   . THR B 242 ? 0.3717 0.4165 1.9653 0.1145  0.1056  0.0209  242 THR B O   
6174  C CB  . THR B 242 ? 0.3515 0.3797 1.9569 0.1199  0.0915  0.0242  242 THR B CB  
6175  O OG1 . THR B 242 ? 0.3318 0.3668 1.9298 0.1209  0.0932  0.0154  242 THR B OG1 
6176  C CG2 . THR B 242 ? 0.3585 0.3783 1.9762 0.1233  0.0870  0.0207  242 THR B CG2 
6177  N N   . LEU B 243 ? 0.3797 0.4262 1.9676 0.1138  0.1010  0.0377  243 LEU B N   
6178  C CA  . LEU B 243 ? 0.3780 0.4395 1.9529 0.1145  0.1055  0.0384  243 LEU B CA  
6179  C C   . LEU B 243 ? 0.3688 0.4320 1.9346 0.1192  0.1047  0.0255  243 LEU B C   
6180  O O   . LEU B 243 ? 0.3550 0.4235 1.9149 0.1212  0.1088  0.0184  243 LEU B O   
6181  C CB  . LEU B 243 ? 0.3938 0.4638 1.9616 0.1136  0.1042  0.0524  243 LEU B CB  
6182  C CG  . LEU B 243 ? 0.4009 0.4687 1.9779 0.1070  0.1053  0.0677  243 LEU B CG  
6183  C CD1 . LEU B 243 ? 0.4177 0.4923 1.9880 0.1062  0.1031  0.0845  243 LEU B CD1 
6184  C CD2 . LEU B 243 ? 0.3969 0.4771 1.9749 0.1031  0.1125  0.0675  243 LEU B CD2 
6185  N N   . LYS B 244 ? 0.3657 0.4239 1.9319 0.1208  0.0990  0.0226  244 LYS B N   
6186  C CA  . LYS B 244 ? 0.3648 0.4236 1.9243 0.1229  0.0968  0.0114  244 LYS B CA  
6187  C C   . LYS B 244 ? 0.3517 0.4026 1.9168 0.1225  0.0993  0.0021  244 LYS B C   
6188  O O   . LYS B 244 ? 0.3413 0.3914 1.8994 0.1239  0.1003  -0.0063 244 LYS B O   
6189  C CB  . LYS B 244 ? 0.3721 0.4303 1.9345 0.1235  0.0900  0.0111  244 LYS B CB  
6190  C CG  . LYS B 244 ? 0.3728 0.4315 1.9314 0.1229  0.0871  -0.0004 244 LYS B CG  
6191  C CD  . LYS B 244 ? 0.3738 0.4383 1.9351 0.1230  0.0801  -0.0003 244 LYS B CD  
6192  C CE  . LYS B 244 ? 0.3888 0.4596 1.9402 0.1215  0.0762  -0.0092 244 LYS B CE  
6193  N NZ  . LYS B 244 ? 0.3949 0.4565 1.9443 0.1189  0.0786  -0.0198 244 LYS B NZ  
6194  N N   . GLN B 245 ? 0.3400 0.3846 1.9175 0.1210  0.0998  0.0036  245 GLN B N   
6195  C CA  . GLN B 245 ? 0.3446 0.3848 1.9271 0.1209  0.1024  -0.0029 245 GLN B CA  
6196  C C   . GLN B 245 ? 0.3525 0.3962 1.9292 0.1225  0.1075  -0.0044 245 GLN B C   
6197  O O   . GLN B 245 ? 0.3529 0.3933 1.9266 0.1245  0.1088  -0.0109 245 GLN B O   
6198  C CB  . GLN B 245 ? 0.3515 0.3885 1.9469 0.1198  0.1020  -0.0017 245 GLN B CB  
6199  C CG  . GLN B 245 ? 0.3844 0.4204 1.9858 0.1206  0.0974  -0.0037 245 GLN B CG  
6200  C CD  . GLN B 245 ? 0.4210 0.4548 2.0344 0.1216  0.0962  -0.0045 245 GLN B CD  
6201  O OE1 . GLN B 245 ? 0.4438 0.4728 2.0622 0.1213  0.0953  -0.0002 245 GLN B OE1 
6202  N NE2 . GLN B 245 ? 0.4206 0.4582 2.0388 0.1225  0.0958  -0.0102 245 GLN B NE2 
6203  N N   . GLN B 246 ? 0.3423 0.3934 1.9182 0.1218  0.1103  0.0025  246 GLN B N   
6204  C CA  . GLN B 246 ? 0.3363 0.3961 1.9086 0.1239  0.1157  0.0017  246 GLN B CA  
6205  C C   . GLN B 246 ? 0.3341 0.3972 1.8926 0.1291  0.1163  -0.0048 246 GLN B C   
6206  O O   . GLN B 246 ? 0.3431 0.4022 1.8993 0.1333  0.1177  -0.0125 246 GLN B O   
6207  C CB  . GLN B 246 ? 0.3430 0.4130 1.9188 0.1201  0.1184  0.0121  246 GLN B CB  
6208  C CG  . GLN B 246 ? 0.3434 0.4284 1.9179 0.1218  0.1244  0.0125  246 GLN B CG  
6209  C CD  . GLN B 246 ? 0.3557 0.4548 1.9314 0.1166  0.1271  0.0247  246 GLN B CD  
6210  O OE1 . GLN B 246 ? 0.3741 0.4797 1.9404 0.1169  0.1268  0.0305  246 GLN B OE1 
6211  N NE2 . GLN B 246 ? 0.3485 0.4535 1.9359 0.1110  0.1293  0.0298  246 GLN B NE2 
6212  N N   . SER B 247 ? 0.3291 0.3991 1.8785 0.1293  0.1146  -0.0021 247 SER B N   
6213  C CA  . SER B 247 ? 0.3345 0.4094 1.8696 0.1346  0.1144  -0.0104 247 SER B CA  
6214  C C   . SER B 247 ? 0.3362 0.3952 1.8707 0.1361  0.1108  -0.0223 247 SER B C   
6215  O O   . SER B 247 ? 0.3322 0.3870 1.8637 0.1412  0.1129  -0.0302 247 SER B O   
6216  C CB  . SER B 247 ? 0.3422 0.4275 1.8683 0.1337  0.1115  -0.0052 247 SER B CB  
6217  O OG  . SER B 247 ? 0.3534 0.4448 1.8648 0.1387  0.1099  -0.0153 247 SER B OG  
6218  N N   . ASP B 248 ? 0.3374 0.3874 1.8771 0.1315  0.1055  -0.0225 248 ASP B N   
6219  C CA  . ASP B 248 ? 0.3397 0.3755 1.8817 0.1302  0.1023  -0.0307 248 ASP B CA  
6220  C C   . ASP B 248 ? 0.3457 0.3730 1.8935 0.1325  0.1059  -0.0323 248 ASP B C   
6221  O O   . ASP B 248 ? 0.3757 0.3907 1.9213 0.1338  0.1042  -0.0395 248 ASP B O   
6222  C CB  . ASP B 248 ? 0.3256 0.3587 1.8763 0.1243  0.0975  -0.0280 248 ASP B CB  
6223  C CG  . ASP B 248 ? 0.3271 0.3679 1.8735 0.1224  0.0920  -0.0275 248 ASP B CG  
6224  O OD1 . ASP B 248 ? 0.3299 0.3763 1.8642 0.1247  0.0903  -0.0323 248 ASP B OD1 
6225  O OD2 . ASP B 248 ? 0.3246 0.3680 1.8797 0.1197  0.0892  -0.0224 248 ASP B OD2 
6226  N N   . GLY B 249 ? 0.3361 0.3690 1.8916 0.1326  0.1101  -0.0256 249 GLY B N   
6227  C CA  . GLY B 249 ? 0.3380 0.3658 1.9002 0.1342  0.1125  -0.0257 249 GLY B CA  
6228  C C   . GLY B 249 ? 0.3607 0.3919 1.9180 0.1420  0.1166  -0.0290 249 GLY B C   
6229  O O   . GLY B 249 ? 0.3795 0.4025 1.9384 0.1458  0.1171  -0.0315 249 GLY B O   
6230  N N   . LEU B 250 ? 0.3677 0.4128 1.9193 0.1451  0.1198  -0.0281 250 LEU B N   
6231  C CA  . LEU B 250 ? 0.3746 0.4266 1.9206 0.1543  0.1236  -0.0331 250 LEU B CA  
6232  C C   . LEU B 250 ? 0.3964 0.4320 1.9339 0.1603  0.1204  -0.0443 250 LEU B C   
6233  O O   . LEU B 250 ? 0.3965 0.4241 1.9350 0.1674  0.1211  -0.0482 250 LEU B O   
6234  C CB  . LEU B 250 ? 0.3781 0.4517 1.9181 0.1561  0.1276  -0.0303 250 LEU B CB  
6235  C CG  . LEU B 250 ? 0.3660 0.4584 1.9149 0.1543  0.1328  -0.0215 250 LEU B CG  
6236  C CD1 . LEU B 250 ? 0.3587 0.4569 1.9101 0.1633  0.1363  -0.0258 250 LEU B CD1 
6237  C CD2 . LEU B 250 ? 0.3541 0.4403 1.9153 0.1444  0.1307  -0.0136 250 LEU B CD2 
6238  N N   . ILE B 251 ? 0.4187 0.4490 1.9486 0.1575  0.1160  -0.0493 251 ILE B N   
6239  C CA  . ILE B 251 ? 0.4373 0.4502 1.9596 0.1608  0.1113  -0.0614 251 ILE B CA  
6240  C C   . ILE B 251 ? 0.4431 0.4338 1.9737 0.1580  0.1084  -0.0608 251 ILE B C   
6241  O O   . ILE B 251 ? 0.4505 0.4249 1.9786 0.1644  0.1068  -0.0681 251 ILE B O   
6242  C CB  . ILE B 251 ? 0.4342 0.4485 1.9493 0.1552  0.1060  -0.0655 251 ILE B CB  
6243  C CG1 . ILE B 251 ? 0.4308 0.4695 1.9363 0.1583  0.1089  -0.0639 251 ILE B CG1 
6244  C CG2 . ILE B 251 ? 0.4557 0.4505 1.9645 0.1566  0.0998  -0.0797 251 ILE B CG2 
6245  C CD1 . ILE B 251 ? 0.4405 0.4919 1.9375 0.1701  0.1142  -0.0702 251 ILE B CD1 
6246  N N   . SER B 252 ? 0.4319 0.4228 1.9727 0.1491  0.1078  -0.0515 252 SER B N   
6247  C CA  . SER B 252 ? 0.4452 0.4201 1.9937 0.1456  0.1057  -0.0485 252 SER B CA  
6248  C C   . SER B 252 ? 0.4378 0.4094 1.9879 0.1546  0.1092  -0.0470 252 SER B C   
6249  O O   . SER B 252 ? 0.4553 0.4082 2.0051 0.1578  0.1068  -0.0496 252 SER B O   
6250  C CB  . SER B 252 ? 0.4382 0.4202 1.9965 0.1367  0.1056  -0.0395 252 SER B CB  
6251  O OG  . SER B 252 ? 0.4658 0.4350 2.0299 0.1316  0.1030  -0.0367 252 SER B OG  
6252  N N   . ASN B 253 ? 0.4263 0.4169 1.9786 0.1587  0.1144  -0.0428 253 ASN B N   
6253  C CA  . ASN B 253 ? 0.4203 0.4153 1.9744 0.1684  0.1179  -0.0416 253 ASN B CA  
6254  C C   . ASN B 253 ? 0.4434 0.4287 1.9890 0.1805  0.1174  -0.0518 253 ASN B C   
6255  O O   . ASN B 253 ? 0.4514 0.4238 1.9984 0.1882  0.1165  -0.0523 253 ASN B O   
6256  C CB  . ASN B 253 ? 0.3991 0.4197 1.9577 0.1684  0.1229  -0.0363 253 ASN B CB  
6257  C CG  . ASN B 253 ? 0.3715 0.3983 1.9397 0.1589  0.1227  -0.0284 253 ASN B CG  
6258  O OD1 . ASN B 253 ? 0.3690 0.3845 1.9401 0.1532  0.1195  -0.0264 253 ASN B OD1 
6259  N ND2 . ASN B 253 ? 0.3610 0.4067 1.9348 0.1572  0.1259  -0.0242 253 ASN B ND2 
6260  N N   . TYR B 254 ? 0.4473 0.4394 1.9836 0.1833  0.1176  -0.0602 254 TYR B N   
6261  C CA  . TYR B 254 ? 0.4663 0.4555 1.9938 0.1971  0.1180  -0.0719 254 TYR B CA  
6262  C C   . TYR B 254 ? 0.5017 0.4574 2.0274 0.2002  0.1117  -0.0795 254 TYR B C   
6263  O O   . TYR B 254 ? 0.5191 0.4648 2.0429 0.2135  0.1116  -0.0858 254 TYR B O   
6264  C CB  . TYR B 254 ? 0.4727 0.4763 1.9888 0.1988  0.1187  -0.0804 254 TYR B CB  
6265  C CG  . TYR B 254 ? 0.4902 0.5139 1.9996 0.2137  0.1238  -0.0875 254 TYR B CG  
6266  C CD1 . TYR B 254 ? 0.5096 0.5197 2.0142 0.2289  0.1223  -0.1004 254 TYR B CD1 
6267  C CD2 . TYR B 254 ? 0.4831 0.5407 1.9921 0.2130  0.1303  -0.0810 254 TYR B CD2 
6268  C CE1 . TYR B 254 ? 0.5130 0.5456 2.0121 0.2443  0.1274  -0.1078 254 TYR B CE1 
6269  C CE2 . TYR B 254 ? 0.4946 0.5763 1.9986 0.2264  0.1358  -0.0866 254 TYR B CE2 
6270  C CZ  . TYR B 254 ? 0.5047 0.5757 2.0035 0.2429  0.1346  -0.1007 254 TYR B CZ  
6271  O OH  . TYR B 254 ? 0.5118 0.6122 2.0060 0.2568  0.1407  -0.1063 254 TYR B OH  
6272  N N   . ARG B 255 ? 0.5196 0.4583 2.0467 0.1877  0.1062  -0.0790 255 ARG B N   
6273  C CA  . ARG B 255 ? 0.5418 0.4475 2.0691 0.1861  0.0993  -0.0846 255 ARG B CA  
6274  C C   . ARG B 255 ? 0.5353 0.4278 2.0720 0.1869  0.0995  -0.0731 255 ARG B C   
6275  O O   . ARG B 255 ? 0.5433 0.4140 2.0794 0.1963  0.0970  -0.0767 255 ARG B O   
6276  C CB  . ARG B 255 ? 0.5477 0.4459 2.0767 0.1700  0.0938  -0.0842 255 ARG B CB  
6277  C CG  . ARG B 255 ? 0.5702 0.4371 2.1046 0.1621  0.0869  -0.0839 255 ARG B CG  
6278  C CD  . ARG B 255 ? 0.6185 0.4594 2.1453 0.1686  0.0805  -0.1010 255 ARG B CD  
6279  N NE  . ARG B 255 ? 0.6455 0.4728 2.1693 0.1859  0.0817  -0.1065 255 ARG B NE  
6280  C CZ  . ARG B 255 ? 0.6830 0.5106 2.1962 0.2012  0.0816  -0.1231 255 ARG B CZ  
6281  N NH1 . ARG B 255 ? 0.6902 0.5371 2.1931 0.2021  0.0819  -0.1349 255 ARG B NH1 
6282  N NH2 . ARG B 255 ? 0.6983 0.5090 2.2111 0.2170  0.0814  -0.1277 255 ARG B NH2 
6283  N N   . ASP B 256 ? 0.5213 0.4271 2.0663 0.1772  0.1020  -0.0594 256 ASP B N   
6284  C CA  . ASP B 256 ? 0.5211 0.4204 2.0743 0.1765  0.1025  -0.0469 256 ASP B CA  
6285  C C   . ASP B 256 ? 0.5151 0.4142 2.0675 0.1931  0.1049  -0.0471 256 ASP B C   
6286  O O   . ASP B 256 ? 0.5348 0.4137 2.0900 0.1972  0.1021  -0.0420 256 ASP B O   
6287  C CB  . ASP B 256 ? 0.5005 0.4229 2.0610 0.1676  0.1060  -0.0354 256 ASP B CB  
6288  C CG  . ASP B 256 ? 0.5066 0.4270 2.0722 0.1523  0.1033  -0.0300 256 ASP B CG  
6289  O OD1 . ASP B 256 ? 0.5268 0.4506 2.0900 0.1456  0.1015  -0.0358 256 ASP B OD1 
6290  O OD2 . ASP B 256 ? 0.5061 0.4255 2.0781 0.1478  0.1033  -0.0192 256 ASP B OD2 
6291  N N   . LEU B 257 ? 0.4981 0.4216 2.0476 0.2022  0.1099  -0.0516 257 LEU B N   
6292  C CA  . LEU B 257 ? 0.4980 0.4322 2.0493 0.2174  0.1132  -0.0498 257 LEU B CA  
6293  C C   . LEU B 257 ? 0.5244 0.4370 2.0698 0.2332  0.1102  -0.0612 257 LEU B C   
6294  O O   . LEU B 257 ? 0.5255 0.4325 2.0737 0.2461  0.1100  -0.0580 257 LEU B O   
6295  C CB  . LEU B 257 ? 0.4657 0.4366 2.0180 0.2191  0.1196  -0.0496 257 LEU B CB  
6296  C CG  . LEU B 257 ? 0.4338 0.4247 1.9940 0.2065  0.1220  -0.0386 257 LEU B CG  
6297  C CD1 . LEU B 257 ? 0.4189 0.4406 1.9804 0.2040  0.1270  -0.0390 257 LEU B CD1 
6298  C CD2 . LEU B 257 ? 0.4281 0.4231 1.9957 0.2099  0.1221  -0.0287 257 LEU B CD2 
6299  N N   . ILE B 258 ? 0.5425 0.4427 2.0796 0.2328  0.1073  -0.0750 258 ILE B N   
6300  C CA  . ILE B 258 ? 0.5851 0.4599 2.1159 0.2467  0.1030  -0.0892 258 ILE B CA  
6301  C C   . ILE B 258 ? 0.6114 0.4456 2.1469 0.2435  0.0958  -0.0839 258 ILE B C   
6302  O O   . ILE B 258 ? 0.6440 0.4587 2.1805 0.2584  0.0934  -0.0855 258 ILE B O   
6303  C CB  . ILE B 258 ? 0.5986 0.4734 2.1186 0.2453  0.1010  -0.1063 258 ILE B CB  
6304  C CG1 . ILE B 258 ? 0.5905 0.5055 2.1049 0.2533  0.1084  -0.1110 258 ILE B CG1 
6305  C CG2 . ILE B 258 ? 0.6424 0.4814 2.1567 0.2557  0.0937  -0.1228 258 ILE B CG2 
6306  C CD1 . ILE B 258 ? 0.6002 0.5248 2.1033 0.2497  0.1075  -0.1239 258 ILE B CD1 
6307  N N   . ASP B 259 ? 0.5985 0.4207 2.1375 0.2244  0.0923  -0.0773 259 ASP B N   
6308  C CA  . ASP B 259 ? 0.6209 0.4169 2.1678 0.2171  0.0880  -0.0637 259 ASP B CA  
6309  C C   . ASP B 259 ? 0.6119 0.4287 2.1645 0.2238  0.0933  -0.0483 259 ASP B C   
6310  O O   . ASP B 259 ? 0.5760 0.4277 2.1291 0.2236  0.0994  -0.0462 259 ASP B O   
6311  C CB  . ASP B 259 ? 0.6137 0.4051 2.1647 0.1949  0.0850  -0.0578 259 ASP B CB  
6312  C CG  . ASP B 259 ? 0.6164 0.4064 2.1610 0.1874  0.0817  -0.0735 259 ASP B CG  
6313  O OD1 . ASP B 259 ? 0.6447 0.4152 2.1824 0.1969  0.0774  -0.0902 259 ASP B OD1 
6314  O OD2 . ASP B 259 ? 0.5745 0.3839 2.1209 0.1736  0.0831  -0.0698 259 ASP B OD2 
6315  N N   . ALA B 260 ? 0.6535 0.4496 2.2104 0.2307  0.0904  -0.0381 260 ALA B N   
6316  C CA  . ALA B 260 ? 0.6524 0.4693 2.2134 0.2415  0.0945  -0.0260 260 ALA B CA  
6317  C C   . ALA B 260 ? 0.6673 0.4945 2.2249 0.2643  0.0968  -0.0370 260 ALA B C   
6318  O O   . ALA B 260 ? 0.6939 0.5400 2.2553 0.2755  0.0996  -0.0287 260 ALA B O   
6319  C CB  . ALA B 260 ? 0.6141 0.4692 2.1788 0.2304  0.1003  -0.0169 260 ALA B CB  
6320  N N   . GLY B 261 ? 0.6687 0.4882 2.2191 0.2713  0.0958  -0.0561 261 GLY B N   
6321  C CA  . GLY B 261 ? 0.6871 0.4990 2.2341 0.2950  0.0948  -0.0681 261 GLY B CA  
6322  C C   . GLY B 261 ? 0.6624 0.5180 2.2069 0.3070  0.1024  -0.0763 261 GLY B C   
6323  O O   . GLY B 261 ? 0.6747 0.5346 2.2180 0.3285  0.1032  -0.0843 261 GLY B O   
6324  N N   . ALA B 262 ? 0.6375 0.5266 2.1817 0.2936  0.1081  -0.0741 262 ALA B N   
6325  C CA  . ALA B 262 ? 0.6197 0.5509 2.1628 0.3029  0.1153  -0.0796 262 ALA B CA  
6326  C C   . ALA B 262 ? 0.6469 0.5742 2.1800 0.3165  0.1149  -0.1001 262 ALA B C   
6327  O O   . ALA B 262 ? 0.6726 0.5762 2.1984 0.3098  0.1105  -0.1105 262 ALA B O   
6328  C CB  . ALA B 262 ? 0.5765 0.5393 2.1219 0.2849  0.1204  -0.0726 262 ALA B CB  
6329  N N   . VAL B 263 ? 0.6490 0.6016 2.1822 0.3365  0.1192  -0.1064 263 VAL B N   
6330  C CA  . VAL B 263 ? 0.6738 0.6329 2.1974 0.3530  0.1204  -0.1267 263 VAL B CA  
6331  C C   . VAL B 263 ? 0.6498 0.6639 2.1729 0.3522  0.1299  -0.1260 263 VAL B C   
6332  O O   . VAL B 263 ? 0.6630 0.6985 2.1790 0.3666  0.1334  -0.1403 263 VAL B O   
6333  C CB  . VAL B 263 ? 0.7142 0.6539 2.2384 0.3800  0.1168  -0.1360 263 VAL B CB  
6334  C CG1 . VAL B 263 ? 0.7270 0.6176 2.2566 0.3783  0.1083  -0.1268 263 VAL B CG1 
6335  C CG2 . VAL B 263 ? 0.7071 0.6885 2.2384 0.3982  0.1233  -0.1321 263 VAL B CG2 
6336  N N   . GLY B 264 ? 0.6240 0.6621 2.1554 0.3351  0.1339  -0.1092 264 GLY B N   
6337  C CA  . GLY B 264 ? 0.6023 0.6889 2.1351 0.3295  0.1420  -0.1056 264 GLY B CA  
6338  C C   . GLY B 264 ? 0.5648 0.6567 2.1025 0.3042  0.1428  -0.0911 264 GLY B C   
6339  O O   . GLY B 264 ? 0.5635 0.6367 2.1080 0.2948  0.1392  -0.0807 264 GLY B O   
6340  N N   . MET B 265 ? 0.5432 0.6611 2.0773 0.2939  0.1474  -0.0902 265 MET B N   
6341  C CA  . MET B 265 ? 0.5123 0.6296 2.0500 0.2713  0.1470  -0.0785 265 MET B CA  
6342  C C   . MET B 265 ? 0.5067 0.6668 2.0488 0.2637  0.1541  -0.0706 265 MET B C   
6343  O O   . MET B 265 ? 0.5315 0.7158 2.0664 0.2701  0.1586  -0.0765 265 MET B O   
6344  C CB  . MET B 265 ? 0.5085 0.5988 2.0355 0.2628  0.1422  -0.0850 265 MET B CB  
6345  C CG  . MET B 265 ? 0.5155 0.5616 2.0400 0.2660  0.1344  -0.0913 265 MET B CG  
6346  S SD  . MET B 265 ? 0.4804 0.5059 2.0172 0.2539  0.1307  -0.0760 265 MET B SD  
6347  C CE  . MET B 265 ? 0.4540 0.4740 1.9888 0.2320  0.1285  -0.0716 265 MET B CE  
6348  N N   . CYS B 266 ? 0.4849 0.6546 2.0390 0.2499  0.1547  -0.0574 266 CYS B N   
6349  C CA  . CYS B 266 ? 0.4743 0.6804 2.0356 0.2395  0.1603  -0.0480 266 CYS B CA  
6350  C C   . CYS B 266 ? 0.4846 0.6790 2.0501 0.2188  0.1576  -0.0381 266 CYS B C   
6351  O O   . CYS B 266 ? 0.4936 0.6938 2.0714 0.2093  0.1570  -0.0298 266 CYS B O   
6352  C CB  . CYS B 266 ? 0.4580 0.6935 2.0327 0.2445  0.1635  -0.0430 266 CYS B CB  
6353  S SG  . CYS B 266 ? 0.4399 0.6992 2.0121 0.2709  0.1676  -0.0537 266 CYS B SG  
6354  N N   . PRO B 267 ? 0.4967 0.6752 2.0525 0.2119  0.1555  -0.0397 267 PRO B N   
6355  C CA  . PRO B 267 ? 0.4646 0.6307 2.0244 0.1947  0.1524  -0.0312 267 PRO B CA  
6356  C C   . PRO B 267 ? 0.4397 0.6325 2.0110 0.1834  0.1561  -0.0196 267 PRO B C   
6357  O O   . PRO B 267 ? 0.4224 0.6459 1.9947 0.1866  0.1617  -0.0174 267 PRO B O   
6358  C CB  . PRO B 267 ? 0.4793 0.6340 2.0257 0.1928  0.1503  -0.0354 267 PRO B CB  
6359  C CG  . PRO B 267 ? 0.5145 0.6850 2.0498 0.2076  0.1540  -0.0454 267 PRO B CG  
6360  C CD  . PRO B 267 ? 0.5266 0.6986 2.0670 0.2215  0.1551  -0.0511 267 PRO B CD  
6361  N N   . PHE B 268 ? 0.4258 0.6070 2.0063 0.1702  0.1526  -0.0127 268 PHE B N   
6362  C CA  . PHE B 268 ? 0.4079 0.6086 2.0025 0.1593  0.1543  -0.0037 268 PHE B CA  
6363  C C   . PHE B 268 ? 0.4067 0.6175 2.0008 0.1482  0.1562  0.0057  268 PHE B C   
6364  O O   . PHE B 268 ? 0.3794 0.5708 1.9706 0.1408  0.1525  0.0087  268 PHE B O   
6365  C CB  . PHE B 268 ? 0.3947 0.5814 2.0002 0.1517  0.1495  -0.0024 268 PHE B CB  
6366  C CG  . PHE B 268 ? 0.3950 0.6009 2.0161 0.1402  0.1499  0.0042  268 PHE B CG  
6367  C CD1 . PHE B 268 ? 0.3768 0.6156 2.0053 0.1415  0.1545  0.0070  268 PHE B CD1 
6368  C CD2 . PHE B 268 ? 0.4099 0.6018 2.0393 0.1278  0.1452  0.0070  268 PHE B CD2 
6369  C CE1 . PHE B 268 ? 0.3811 0.6375 2.0254 0.1290  0.1540  0.0127  268 PHE B CE1 
6370  C CE2 . PHE B 268 ? 0.4155 0.6220 2.0599 0.1164  0.1444  0.0113  268 PHE B CE2 
6371  C CZ  . PHE B 268 ? 0.4084 0.6470 2.0606 0.1159  0.1486  0.0144  268 PHE B CZ  
6372  N N   . TYR B 269 ? 0.4173 0.6610 2.0138 0.1487  0.1622  0.0106  269 TYR B N   
6373  C CA  . TYR B 269 ? 0.4336 0.6963 2.0381 0.1344  0.1647  0.0241  269 TYR B CA  
6374  C C   . TYR B 269 ? 0.4319 0.6954 2.0229 0.1335  0.1663  0.0292  269 TYR B C   
6375  O O   . TYR B 269 ? 0.4432 0.6802 2.0263 0.1325  0.1615  0.0275  269 TYR B O   
6376  C CB  . TYR B 269 ? 0.4521 0.6988 2.0717 0.1202  0.1594  0.0288  269 TYR B CB  
6377  C CG  . TYR B 269 ? 0.4429 0.7102 2.0792 0.1048  0.1607  0.0403  269 TYR B CG  
6378  C CD1 . TYR B 269 ? 0.4592 0.7651 2.1018 0.1049  0.1670  0.0447  269 TYR B CD1 
6379  C CD2 . TYR B 269 ? 0.4467 0.6950 2.0938 0.0900  0.1553  0.0462  269 TYR B CD2 
6380  C CE1 . TYR B 269 ? 0.4953 0.8208 2.1550 0.0884  0.1678  0.0559  269 TYR B CE1 
6381  C CE2 . TYR B 269 ? 0.4678 0.7308 2.1314 0.0742  0.1553  0.0564  269 TYR B CE2 
6382  C CZ  . TYR B 269 ? 0.5047 0.8070 2.1751 0.0721  0.1616  0.0620  269 TYR B CZ  
6383  O OH  . TYR B 269 ? 0.4823 0.8021 2.1707 0.0544  0.1617  0.0729  269 TYR B OH  
6384  N N   . TYR B 270 ? 0.4221 0.7208 2.0110 0.1341  0.1731  0.0357  270 TYR B N   
6385  C CA  . TYR B 270 ? 0.4188 0.7295 1.9959 0.1319  0.1758  0.0440  270 TYR B CA  
6386  C C   . TYR B 270 ? 0.4238 0.7195 2.0077 0.1144  0.1719  0.0599  270 TYR B C   
6387  O O   . TYR B 270 ? 0.4296 0.7083 2.0025 0.1147  0.1684  0.0613  270 TYR B O   
6388  C CB  . TYR B 270 ? 0.4107 0.7685 1.9871 0.1361  0.1848  0.0482  270 TYR B CB  
6389  C CG  . TYR B 270 ? 0.4104 0.7951 1.9816 0.1275  0.1896  0.0648  270 TYR B CG  
6390  C CD1 . TYR B 270 ? 0.4202 0.8119 1.9711 0.1362  0.1910  0.0620  270 TYR B CD1 
6391  C CD2 . TYR B 270 ? 0.4067 0.8133 1.9937 0.1105  0.1927  0.0836  270 TYR B CD2 
6392  C CE1 . TYR B 270 ? 0.4337 0.8547 1.9787 0.1290  0.1957  0.0788  270 TYR B CE1 
6393  C CE2 . TYR B 270 ? 0.4224 0.8554 2.0052 0.1018  0.1974  0.1018  270 TYR B CE2 
6394  C CZ  . TYR B 270 ? 0.4361 0.8775 1.9972 0.1116  0.1992  0.1001  270 TYR B CZ  
6395  O OH  . TYR B 270 ? 0.4553 0.9255 2.0117 0.1027  0.2039  0.1202  270 TYR B OH  
6396  N N   . ALA B 271 ? 0.4309 0.7325 2.0334 0.1000  0.1718  0.0709  271 ALA B N   
6397  C CA  . ALA B 271 ? 0.4309 0.7187 2.0425 0.0829  0.1681  0.0871  271 ALA B CA  
6398  C C   . ALA B 271 ? 0.4237 0.6929 2.0549 0.0720  0.1627  0.0863  271 ALA B C   
6399  O O   . ALA B 271 ? 0.4071 0.6830 2.0461 0.0756  0.1630  0.0762  271 ALA B O   
6400  C CB  . ALA B 271 ? 0.4431 0.7646 2.0569 0.0730  0.1743  0.1061  271 ALA B CB  
6401  N N   . ASP B 272 ? 0.4495 0.6959 2.0887 0.0590  0.1572  0.0969  272 ASP B N   
6402  C CA  . ASP B 272 ? 0.4509 0.6751 2.1076 0.0491  0.1506  0.0941  272 ASP B CA  
6403  C C   . ASP B 272 ? 0.4366 0.6838 2.1122 0.0345  0.1526  0.1022  272 ASP B C   
6404  O O   . ASP B 272 ? 0.4476 0.7184 2.1264 0.0250  0.1573  0.1184  272 ASP B O   
6405  C CB  . ASP B 272 ? 0.4855 0.6777 2.1458 0.0404  0.1437  0.1032  272 ASP B CB  
6406  C CG  . ASP B 272 ? 0.4979 0.6608 2.1464 0.0515  0.1385  0.0939  272 ASP B CG  
6407  O OD1 . ASP B 272 ? 0.5093 0.6752 2.1456 0.0649  0.1404  0.0809  272 ASP B OD1 
6408  O OD2 . ASP B 272 ? 0.5202 0.6573 2.1733 0.0463  0.1323  0.0997  272 ASP B OD2 
6409  N N   . GLY B 273 ? 0.4079 0.6484 2.0966 0.0317  0.1484  0.0912  273 GLY B N   
6410  C CA  . GLY B 273 ? 0.3878 0.6470 2.0968 0.0164  0.1481  0.0960  273 GLY B CA  
6411  C C   . GLY B 273 ? 0.3718 0.5979 2.0954 0.0039  0.1385  0.0940  273 GLY B C   
6412  O O   . GLY B 273 ? 0.3431 0.5532 2.0689 0.0091  0.1331  0.0781  273 GLY B O   
6413  N N   . TRP B 274 ? 0.3854 0.6016 2.1184 -0.0122 0.1362  0.1105  274 TRP B N   
6414  C CA  . TRP B 274 ? 0.3929 0.5737 2.1402 -0.0239 0.1263  0.1088  274 TRP B CA  
6415  C C   . TRP B 274 ? 0.3936 0.5843 2.1594 -0.0334 0.1222  0.0975  274 TRP B C   
6416  O O   . TRP B 274 ? 0.4050 0.5666 2.1802 -0.0377 0.1132  0.0872  274 TRP B O   
6417  C CB  . TRP B 274 ? 0.4126 0.5806 2.1679 -0.0402 0.1243  0.1313  274 TRP B CB  
6418  C CG  . TRP B 274 ? 0.4111 0.5687 2.1492 -0.0322 0.1267  0.1441  274 TRP B CG  
6419  C CD1 . TRP B 274 ? 0.3944 0.5612 2.1109 -0.0141 0.1318  0.1390  274 TRP B CD1 
6420  C CD2 . TRP B 274 ? 0.4372 0.5747 2.1788 -0.0429 0.1233  0.1654  274 TRP B CD2 
6421  N NE1 . TRP B 274 ? 0.4074 0.5638 2.1133 -0.0126 0.1317  0.1542  274 TRP B NE1 
6422  C CE2 . TRP B 274 ? 0.4327 0.5714 2.1531 -0.0294 0.1268  0.1716  274 TRP B CE2 
6423  C CE3 . TRP B 274 ? 0.4639 0.5813 2.2247 -0.0627 0.1171  0.1800  274 TRP B CE3 
6424  C CZ2 . TRP B 274 ? 0.4523 0.5759 2.1693 -0.0339 0.1245  0.1926  274 TRP B CZ2 
6425  C CZ3 . TRP B 274 ? 0.4864 0.5851 2.2444 -0.0672 0.1149  0.2018  274 TRP B CZ3 
6426  C CH2 . TRP B 274 ? 0.4793 0.5828 2.2153 -0.0525 0.1187  0.2086  274 TRP B CH2 
6427  N N   . TRP B 275 ? 0.3819 0.6152 2.1530 -0.0357 0.1285  0.0988  275 TRP B N   
6428  C CA  . TRP B 275 ? 0.3764 0.6270 2.1660 -0.0457 0.1249  0.0896  275 TRP B CA  
6429  C C   . TRP B 275 ? 0.3575 0.5991 2.1422 -0.0317 0.1203  0.0667  275 TRP B C   
6430  O O   . TRP B 275 ? 0.3484 0.5935 2.1475 -0.0396 0.1141  0.0560  275 TRP B O   
6431  C CB  . TRP B 275 ? 0.3760 0.6792 2.1715 -0.0492 0.1335  0.0979  275 TRP B CB  
6432  C CG  . TRP B 275 ? 0.3579 0.6866 2.1365 -0.0266 0.1411  0.0894  275 TRP B CG  
6433  C CD1 . TRP B 275 ? 0.3586 0.6994 2.1197 -0.0139 0.1495  0.0964  275 TRP B CD1 
6434  C CD2 . TRP B 275 ? 0.3396 0.6832 2.1173 -0.0136 0.1402  0.0723  275 TRP B CD2 
6435  N NE1 . TRP B 275 ? 0.3405 0.6991 2.0905 0.0061  0.1536  0.0839  275 TRP B NE1 
6436  C CE2 . TRP B 275 ? 0.3316 0.6918 2.0914 0.0068  0.1481  0.0703  275 TRP B CE2 
6437  C CE3 . TRP B 275 ? 0.3357 0.6803 2.1252 -0.0167 0.1331  0.0584  275 TRP B CE3 
6438  C CZ2 . TRP B 275 ? 0.3180 0.6927 2.0725 0.0240  0.1490  0.0568  275 TRP B CZ2 
6439  C CZ3 . TRP B 275 ? 0.3231 0.6861 2.1063 0.0003  0.1344  0.0459  275 TRP B CZ3 
6440  C CH2 . TRP B 275 ? 0.3149 0.6908 2.0811 0.0205  0.1422  0.0459  275 TRP B CH2 
6441  N N   . LYS B 276 ? 0.3534 0.5842 2.1180 -0.0117 0.1231  0.0596  276 LYS B N   
6442  C CA  . LYS B 276 ? 0.3434 0.5777 2.1006 0.0038  0.1219  0.0420  276 LYS B CA  
6443  C C   . LYS B 276 ? 0.3502 0.5554 2.1126 0.0020  0.1123  0.0278  276 LYS B C   
6444  O O   . LYS B 276 ? 0.3375 0.5503 2.0991 0.0096  0.1098  0.0138  276 LYS B O   
6445  C CB  . LYS B 276 ? 0.3303 0.5611 2.0656 0.0237  0.1276  0.0404  276 LYS B CB  
6446  C CG  . LYS B 276 ? 0.3230 0.5846 2.0505 0.0301  0.1371  0.0497  276 LYS B CG  
6447  C CD  . LYS B 276 ? 0.3136 0.5671 2.0196 0.0487  0.1414  0.0465  276 LYS B CD  
6448  C CE  . LYS B 276 ? 0.3010 0.5480 1.9998 0.0634  0.1395  0.0321  276 LYS B CE  
6449  N NZ  . LYS B 276 ? 0.2955 0.5742 2.0031 0.0659  0.1410  0.0278  276 LYS B NZ  
6450  N N   . GLY B 277 ? 0.3820 0.5546 2.1492 -0.0069 0.1067  0.0313  277 GLY B N   
6451  C CA  . GLY B 277 ? 0.3985 0.5439 2.1720 -0.0083 0.0971  0.0166  277 GLY B CA  
6452  C C   . GLY B 277 ? 0.4169 0.5554 2.2125 -0.0290 0.0895  0.0169  277 GLY B C   
6453  O O   . GLY B 277 ? 0.4260 0.5315 2.2277 -0.0331 0.0813  0.0104  277 GLY B O   
6454  N N   . GLY B 278 ? 0.4252 0.5956 2.2334 -0.0418 0.0920  0.0238  278 GLY B N   
6455  C CA  . GLY B 278 ? 0.4646 0.6303 2.2954 -0.0651 0.0856  0.0287  278 GLY B CA  
6456  C C   . GLY B 278 ? 0.4853 0.6296 2.3187 -0.0759 0.0868  0.0504  278 GLY B C   
6457  O O   . GLY B 278 ? 0.5047 0.6273 2.3228 -0.0641 0.0892  0.0560  278 GLY B O   
6458  N N   . GLU B 279 ? 0.4852 0.6385 2.3384 -0.0987 0.0851  0.0632  279 GLU B N   
6459  C CA  . GLU B 279 ? 0.5148 0.6486 2.3736 -0.1124 0.0852  0.0864  279 GLU B CA  
6460  C C   . GLU B 279 ? 0.5018 0.6564 2.3423 -0.1019 0.0972  0.1045  279 GLU B C   
6461  O O   . GLU B 279 ? 0.5042 0.6386 2.3263 -0.0855 0.0988  0.1043  279 GLU B O   
6462  C CB  . GLU B 279 ? 0.5409 0.6186 2.4020 -0.1124 0.0746  0.0815  279 GLU B CB  
6463  C CG  . GLU B 279 ? 0.5843 0.6377 2.4575 -0.1311 0.0716  0.1059  279 GLU B CG  
6464  C CD  . GLU B 279 ? 0.6048 0.6872 2.4986 -0.1570 0.0735  0.1224  279 GLU B CD  
6465  O OE1 . GLU B 279 ? 0.6047 0.7148 2.4944 -0.1619 0.0832  0.1464  279 GLU B OE1 
6466  O OE2 . GLU B 279 ? 0.6225 0.7031 2.5367 -0.1725 0.0653  0.1107  279 GLU B OE2 
6467  N N   . LYS B 280 ? 0.4999 0.6972 2.3463 -0.1119 0.1052  0.1197  280 LYS B N   
6468  C CA  . LYS B 280 ? 0.4946 0.7171 2.3252 -0.1039 0.1166  0.1371  280 LYS B CA  
6469  C C   . LYS B 280 ? 0.5218 0.7181 2.3494 -0.1114 0.1160  0.1598  280 LYS B C   
6470  O O   . LYS B 280 ? 0.5205 0.7309 2.3304 -0.1009 0.1241  0.1713  280 LYS B O   
6471  C CB  . LYS B 280 ? 0.4943 0.7724 2.3352 -0.1145 0.1250  0.1481  280 LYS B CB  
6472  C CG  . LYS B 280 ? 0.5188 0.8033 2.3861 -0.1446 0.1214  0.1649  280 LYS B CG  
6473  C CD  . LYS B 280 ? 0.5131 0.8542 2.3960 -0.1544 0.1265  0.1653  280 LYS B CD  
6474  C CE  . LYS B 280 ? 0.5299 0.8726 2.4432 -0.1849 0.1191  0.1723  280 LYS B CE  
6475  N NZ  . LYS B 280 ? 0.5104 0.8889 2.4369 -0.1864 0.1173  0.1549  280 LYS B NZ  
6476  N N   . SER B 281 ? 0.5513 0.7108 2.3959 -0.1289 0.1062  0.1663  281 SER B N   
6477  C CA  . SER B 281 ? 0.5831 0.7163 2.4266 -0.1366 0.1047  0.1904  281 SER B CA  
6478  C C   . SER B 281 ? 0.6083 0.6876 2.4433 -0.1235 0.0958  0.1811  281 SER B C   
6479  O O   . SER B 281 ? 0.6400 0.6895 2.4761 -0.1288 0.0918  0.1992  281 SER B O   
6480  C CB  . SER B 281 ? 0.6119 0.7414 2.4808 -0.1657 0.1003  0.2091  281 SER B CB  
6481  O OG  . SER B 281 ? 0.6056 0.7885 2.4853 -0.1781 0.1078  0.2146  281 SER B OG  
6482  N N   . ASP B 282 ? 0.5908 0.6593 2.4175 -0.1058 0.0927  0.1538  282 ASP B N   
6483  C CA  . ASP B 282 ? 0.5871 0.6139 2.4035 -0.0901 0.0863  0.1441  282 ASP B CA  
6484  C C   . ASP B 282 ? 0.5260 0.5704 2.3192 -0.0663 0.0931  0.1306  282 ASP B C   
6485  O O   . ASP B 282 ? 0.4956 0.5693 2.2859 -0.0609 0.0977  0.1171  282 ASP B O   
6486  C CB  . ASP B 282 ? 0.6174 0.6061 2.4494 -0.0941 0.0737  0.1252  282 ASP B CB  
6487  C CG  . ASP B 282 ? 0.6341 0.5818 2.4572 -0.0770 0.0668  0.1148  282 ASP B CG  
6488  O OD1 . ASP B 282 ? 0.6607 0.5852 2.4807 -0.0762 0.0649  0.1327  282 ASP B OD1 
6489  O OD2 . ASP B 282 ? 0.6282 0.5706 2.4472 -0.0638 0.0637  0.0896  282 ASP B OD2 
6490  N N   . HIS B 283 ? 0.5105 0.5370 2.2882 -0.0531 0.0932  0.1364  283 HIS B N   
6491  C CA  . HIS B 283 ? 0.4698 0.5008 2.2272 -0.0312 0.0966  0.1224  283 HIS B CA  
6492  C C   . HIS B 283 ? 0.4575 0.4537 2.2180 -0.0223 0.0874  0.1029  283 HIS B C   
6493  O O   . HIS B 283 ? 0.4777 0.4426 2.2386 -0.0191 0.0812  0.1079  283 HIS B O   
6494  C CB  . HIS B 283 ? 0.4691 0.5025 2.2095 -0.0235 0.1008  0.1395  283 HIS B CB  
6495  C CG  . HIS B 283 ? 0.4418 0.4968 2.1611 -0.0062 0.1078  0.1315  283 HIS B CG  
6496  N ND1 . HIS B 283 ? 0.4188 0.4946 2.1327 0.0025  0.1122  0.1138  283 HIS B ND1 
6497  C CD2 . HIS B 283 ? 0.4403 0.4978 2.1423 0.0038  0.1104  0.1398  283 HIS B CD2 
6498  C CE1 . HIS B 283 ? 0.4037 0.4912 2.0984 0.0165  0.1172  0.1117  283 HIS B CE1 
6499  N NE2 . HIS B 283 ? 0.4161 0.4937 2.1033 0.0173  0.1160  0.1262  283 HIS B NE2 
6500  N N   . SER B 284 ? 0.4331 0.4371 2.1965 -0.0181 0.0863  0.0813  284 SER B N   
6501  C CA  . SER B 284 ? 0.4327 0.4113 2.1989 -0.0093 0.0784  0.0607  284 SER B CA  
6502  C C   . SER B 284 ? 0.4312 0.4017 2.1799 0.0101  0.0796  0.0554  284 SER B C   
6503  O O   . SER B 284 ? 0.4088 0.4008 2.1423 0.0199  0.0868  0.0551  284 SER B O   
6504  C CB  . SER B 284 ? 0.4124 0.4099 2.1845 -0.0106 0.0781  0.0419  284 SER B CB  
6505  O OG  . SER B 284 ? 0.4129 0.3905 2.1895 -0.0042 0.0701  0.0210  284 SER B OG  
6506  N N   . LEU B 285 ? 0.4607 0.3994 2.2126 0.0161  0.0719  0.0508  285 LEU B N   
6507  C CA  . LEU B 285 ? 0.4589 0.3917 2.1970 0.0331  0.0723  0.0468  285 LEU B CA  
6508  C C   . LEU B 285 ? 0.4405 0.3882 2.1716 0.0444  0.0745  0.0260  285 LEU B C   
6509  O O   . LEU B 285 ? 0.4254 0.3783 2.1436 0.0570  0.0771  0.0231  285 LEU B O   
6510  C CB  . LEU B 285 ? 0.4946 0.3914 2.2401 0.0376  0.0630  0.0464  285 LEU B CB  
6511  C CG  . LEU B 285 ? 0.5357 0.4114 2.2886 0.0277  0.0592  0.0691  285 LEU B CG  
6512  C CD1 . LEU B 285 ? 0.5606 0.4004 2.3198 0.0371  0.0495  0.0656  285 LEU B CD1 
6513  C CD2 . LEU B 285 ? 0.5337 0.4283 2.2728 0.0274  0.0665  0.0910  285 LEU B CD2 
6514  N N   . ASN B 286 ? 0.4451 0.3999 2.1852 0.0394  0.0726  0.0120  286 ASN B N   
6515  C CA  . ASN B 286 ? 0.4430 0.4096 2.1776 0.0503  0.0732  -0.0073 286 ASN B CA  
6516  C C   . ASN B 286 ? 0.4413 0.4377 2.1750 0.0462  0.0783  -0.0117 286 ASN B C   
6517  O O   . ASN B 286 ? 0.4390 0.4447 2.1739 0.0503  0.0765  -0.0278 286 ASN B O   
6518  C CB  . ASN B 286 ? 0.4562 0.4028 2.2009 0.0534  0.0643  -0.0248 286 ASN B CB  
6519  C CG  . ASN B 286 ? 0.4641 0.4094 2.2242 0.0396  0.0594  -0.0311 286 ASN B CG  
6520  O OD1 . ASN B 286 ? 0.4780 0.4157 2.2475 0.0255  0.0583  -0.0172 286 ASN B OD1 
6521  N ND2 . ASN B 286 ? 0.4619 0.4182 2.2245 0.0426  0.0567  -0.0510 286 ASN B ND2 
6522  N N   . GLN B 287 ? 0.4454 0.4593 2.1761 0.0397  0.0847  0.0027  287 GLN B N   
6523  C CA  . GLN B 287 ? 0.4487 0.4930 2.1783 0.0381  0.0898  0.0001  287 GLN B CA  
6524  C C   . GLN B 287 ? 0.4510 0.5111 2.1642 0.0476  0.0981  0.0075  287 GLN B C   
6525  O O   . GLN B 287 ? 0.4857 0.5569 2.1965 0.0431  0.1031  0.0213  287 GLN B O   
6526  C CB  . GLN B 287 ? 0.4805 0.5359 2.2244 0.0214  0.0896  0.0086  287 GLN B CB  
6527  C CG  . GLN B 287 ? 0.4952 0.5407 2.2565 0.0109  0.0809  -0.0030 287 GLN B CG  
6528  C CD  . GLN B 287 ? 0.4881 0.5544 2.2498 0.0157  0.0799  -0.0206 287 GLN B CD  
6529  O OE1 . GLN B 287 ? 0.4742 0.5614 2.2237 0.0269  0.0858  -0.0228 287 GLN B OE1 
6530  N NE2 . GLN B 287 ? 0.4959 0.5561 2.2716 0.0073  0.0717  -0.0335 287 GLN B NE2 
6531  N N   . PRO B 288 ? 0.4193 0.4823 2.1212 0.0606  0.0997  -0.0019 288 PRO B N   
6532  C CA  . PRO B 288 ? 0.3869 0.4620 2.0740 0.0697  0.1064  0.0025  288 PRO B CA  
6533  C C   . PRO B 288 ? 0.3715 0.4693 2.0566 0.0668  0.1129  0.0118  288 PRO B C   
6534  O O   . PRO B 288 ? 0.3553 0.4566 2.0290 0.0718  0.1174  0.0186  288 PRO B O   
6535  C CB  . PRO B 288 ? 0.3776 0.4601 2.0606 0.0787  0.1063  -0.0102 288 PRO B CB  
6536  C CG  . PRO B 288 ? 0.3848 0.4520 2.0747 0.0787  0.0996  -0.0206 288 PRO B CG  
6537  C CD  . PRO B 288 ? 0.4059 0.4620 2.1095 0.0668  0.0949  -0.0175 288 PRO B CD  
6538  N N   . GLU B 289 ? 0.3694 0.4848 2.0658 0.0590  0.1130  0.0110  289 GLU B N   
6539  C CA  . GLU B 289 ? 0.3596 0.5035 2.0553 0.0586  0.1195  0.0172  289 GLU B CA  
6540  C C   . GLU B 289 ? 0.3527 0.5005 2.0479 0.0513  0.1231  0.0328  289 GLU B C   
6541  O O   . GLU B 289 ? 0.3256 0.4966 2.0149 0.0547  0.1298  0.0388  289 GLU B O   
6542  C CB  . GLU B 289 ? 0.3605 0.5259 2.0701 0.0518  0.1180  0.0123  289 GLU B CB  
6543  C CG  . GLU B 289 ? 0.3516 0.5215 2.0594 0.0607  0.1154  -0.0015 289 GLU B CG  
6544  C CD  . GLU B 289 ? 0.3455 0.5259 2.0395 0.0761  0.1206  -0.0029 289 GLU B CD  
6545  O OE1 . GLU B 289 ? 0.3782 0.5805 2.0713 0.0785  0.1260  0.0028  289 GLU B OE1 
6546  O OE2 . GLU B 289 ? 0.3424 0.5104 2.0272 0.0856  0.1194  -0.0091 289 GLU B OE2 
6547  N N   . GLU B 290 ? 0.3559 0.4813 2.0570 0.0423  0.1184  0.0392  290 GLU B N   
6548  C CA  . GLU B 290 ? 0.3664 0.4949 2.0692 0.0329  0.1207  0.0566  290 GLU B CA  
6549  C C   . GLU B 290 ? 0.3648 0.4852 2.0506 0.0420  0.1231  0.0630  290 GLU B C   
6550  O O   . GLU B 290 ? 0.3711 0.4941 2.0557 0.0357  0.1249  0.0786  290 GLU B O   
6551  C CB  . GLU B 290 ? 0.3828 0.4900 2.1018 0.0180  0.1136  0.0623  290 GLU B CB  
6552  C CG  . GLU B 290 ? 0.3879 0.5056 2.1252 0.0061  0.1105  0.0562  290 GLU B CG  
6553  C CD  . GLU B 290 ? 0.4114 0.5067 2.1665 -0.0109 0.1029  0.0622  290 GLU B CD  
6554  O OE1 . GLU B 290 ? 0.4254 0.4958 2.1782 -0.0122 0.1003  0.0730  290 GLU B OE1 
6555  O OE2 . GLU B 290 ? 0.4094 0.5117 2.1811 -0.0230 0.0989  0.0566  290 GLU B OE2 
6556  N N   . TRP B 291 ? 0.3493 0.4619 2.0225 0.0560  0.1231  0.0517  291 TRP B N   
6557  C CA  . TRP B 291 ? 0.3532 0.4564 2.0115 0.0641  0.1235  0.0549  291 TRP B CA  
6558  C C   . TRP B 291 ? 0.3481 0.4612 1.9919 0.0773  0.1276  0.0455  291 TRP B C   
6559  O O   . TRP B 291 ? 0.3564 0.4553 1.9914 0.0851  0.1252  0.0394  291 TRP B O   
6560  C CB  . TRP B 291 ? 0.3526 0.4263 2.0129 0.0659  0.1162  0.0511  291 TRP B CB  
6561  C CG  . TRP B 291 ? 0.3656 0.4227 2.0401 0.0547  0.1108  0.0593  291 TRP B CG  
6562  C CD1 . TRP B 291 ? 0.3676 0.4167 2.0579 0.0468  0.1063  0.0535  291 TRP B CD1 
6563  C CD2 . TRP B 291 ? 0.3834 0.4291 2.0576 0.0501  0.1085  0.0753  291 TRP B CD2 
6564  N NE1 . TRP B 291 ? 0.3896 0.4195 2.0902 0.0372  0.1012  0.0641  291 TRP B NE1 
6565  C CE2 . TRP B 291 ? 0.3993 0.4267 2.0905 0.0391  0.1026  0.0789  291 TRP B CE2 
6566  C CE3 . TRP B 291 ? 0.3893 0.4389 2.0503 0.0543  0.1105  0.0868  291 TRP B CE3 
6567  C CZ2 . TRP B 291 ? 0.4243 0.4345 2.1203 0.0324  0.0986  0.0955  291 TRP B CZ2 
6568  C CZ3 . TRP B 291 ? 0.4138 0.4504 2.0785 0.0481  0.1069  0.1036  291 TRP B CZ3 
6569  C CH2 . TRP B 291 ? 0.4325 0.4485 2.1147 0.0373  0.1011  0.1088  291 TRP B CH2 
6570  N N   . PHE B 292 ? 0.3412 0.4789 1.9833 0.0800  0.1334  0.0443  292 PHE B N   
6571  C CA  . PHE B 292 ? 0.3353 0.4791 1.9649 0.0932  0.1365  0.0349  292 PHE B CA  
6572  C C   . PHE B 292 ? 0.3476 0.5106 1.9654 0.0974  0.1423  0.0404  292 PHE B C   
6573  O O   . PHE B 292 ? 0.3524 0.5276 1.9619 0.1080  0.1461  0.0333  292 PHE B O   
6574  C CB  . PHE B 292 ? 0.3278 0.4851 1.9638 0.0967  0.1382  0.0271  292 PHE B CB  
6575  C CG  . PHE B 292 ? 0.3257 0.4684 1.9643 0.1008  0.1339  0.0166  292 PHE B CG  
6576  C CD1 . PHE B 292 ? 0.3317 0.4624 1.9594 0.1111  0.1333  0.0095  292 PHE B CD1 
6577  C CD2 . PHE B 292 ? 0.3277 0.4731 1.9797 0.0944  0.1309  0.0137  292 PHE B CD2 
6578  C CE1 . PHE B 292 ? 0.3310 0.4531 1.9610 0.1145  0.1303  0.0022  292 PHE B CE1 
6579  C CE2 . PHE B 292 ? 0.3321 0.4702 1.9851 0.0991  0.1276  0.0045  292 PHE B CE2 
6580  C CZ  . PHE B 292 ? 0.3296 0.4568 1.9714 0.1091  0.1277  -0.0002 292 PHE B CZ  
6581  N N   . GLY B 293 ? 0.3587 0.5259 1.9762 0.0896  0.1429  0.0536  293 GLY B N   
6582  C CA  . GLY B 293 ? 0.3675 0.5592 1.9739 0.0929  0.1489  0.0601  293 GLY B CA  
6583  C C   . GLY B 293 ? 0.3658 0.5486 1.9543 0.1033  0.1476  0.0538  293 GLY B C   
6584  O O   . GLY B 293 ? 0.3620 0.5202 1.9486 0.1038  0.1417  0.0505  293 GLY B O   
6585  N N   . PHE B 294 ? 0.3743 0.5789 1.9500 0.1122  0.1528  0.0504  294 PHE B N   
6586  C CA  . PHE B 294 ? 0.3879 0.5912 1.9463 0.1185  0.1516  0.0484  294 PHE B CA  
6587  C C   . PHE B 294 ? 0.3983 0.6145 1.9551 0.1096  0.1526  0.0670  294 PHE B C   
6588  O O   . PHE B 294 ? 0.4075 0.6168 1.9541 0.1107  0.1490  0.0703  294 PHE B O   
6589  C CB  . PHE B 294 ? 0.3995 0.6195 1.9448 0.1326  0.1559  0.0350  294 PHE B CB  
6590  C CG  . PHE B 294 ? 0.3935 0.5923 1.9372 0.1423  0.1527  0.0175  294 PHE B CG  
6591  C CD1 . PHE B 294 ? 0.3757 0.5503 1.9310 0.1380  0.1483  0.0154  294 PHE B CD1 
6592  C CD2 . PHE B 294 ? 0.4104 0.6148 1.9412 0.1560  0.1543  0.0034  294 PHE B CD2 
6593  C CE1 . PHE B 294 ? 0.3788 0.5363 1.9326 0.1460  0.1458  0.0024  294 PHE B CE1 
6594  C CE2 . PHE B 294 ? 0.4037 0.5866 1.9341 0.1641  0.1511  -0.0104 294 PHE B CE2 
6595  C CZ  . PHE B 294 ? 0.3959 0.5560 1.9378 0.1585  0.1471  -0.0095 294 PHE B CZ  
6596  N N   . TRP B 295 ? 0.4120 0.6481 1.9800 0.1002  0.1572  0.0801  295 TRP B N   
6597  C CA  . TRP B 295 ? 0.4318 0.6829 2.0006 0.0897  0.1591  0.1013  295 TRP B CA  
6598  C C   . TRP B 295 ? 0.4362 0.6664 2.0249 0.0747  0.1545  0.1130  295 TRP B C   
6599  O O   . TRP B 295 ? 0.4397 0.6650 2.0430 0.0705  0.1541  0.1071  295 TRP B O   
6600  C CB  . TRP B 295 ? 0.4433 0.7385 2.0094 0.0901  0.1686  0.1078  295 TRP B CB  
6601  C CG  . TRP B 295 ? 0.4611 0.7798 2.0054 0.1045  0.1728  0.0993  295 TRP B CG  
6602  C CD1 . TRP B 295 ? 0.4637 0.7782 1.9970 0.1202  0.1725  0.0772  295 TRP B CD1 
6603  C CD2 . TRP B 295 ? 0.4823 0.8330 2.0129 0.1046  0.1775  0.1122  295 TRP B CD2 
6604  N NE1 . TRP B 295 ? 0.4763 0.8158 1.9902 0.1305  0.1760  0.0730  295 TRP B NE1 
6605  C CE2 . TRP B 295 ? 0.4894 0.8538 2.0005 0.1216  0.1794  0.0941  295 TRP B CE2 
6606  C CE3 . TRP B 295 ? 0.4992 0.8683 2.0320 0.0919  0.1799  0.1377  295 TRP B CE3 
6607  C CZ2 . TRP B 295 ? 0.5063 0.9046 1.9990 0.1271  0.1838  0.0989  295 TRP B CZ2 
6608  C CZ3 . TRP B 295 ? 0.5163 0.9200 2.0309 0.0968  0.1848  0.1452  295 TRP B CZ3 
6609  C CH2 . TRP B 295 ? 0.5211 0.9404 2.0153 0.1146  0.1867  0.1251  295 TRP B CH2 
6610  N N   . GLY B 296 ? 0.4368 0.6539 2.0260 0.0672  0.1503  0.1288  296 GLY B N   
6611  C CA  . GLY B 296 ? 0.4343 0.6282 2.0425 0.0537  0.1451  0.1391  296 GLY B CA  
6612  C C   . GLY B 296 ? 0.4488 0.6577 2.0623 0.0399  0.1475  0.1649  296 GLY B C   
6613  O O   . GLY B 296 ? 0.4606 0.6883 2.0598 0.0426  0.1504  0.1769  296 GLY B O   
6614  N N   . TYR B 297 ? 0.4435 0.6449 2.0778 0.0248  0.1458  0.1734  297 TYR B N   
6615  C CA  . TYR B 297 ? 0.4623 0.6728 2.1051 0.0088  0.1470  0.1999  297 TYR B CA  
6616  C C   . TYR B 297 ? 0.4809 0.6505 2.1283 0.0051  0.1373  0.2101  297 TYR B C   
6617  O O   . TYR B 297 ? 0.4664 0.6035 2.1172 0.0117  0.1301  0.1945  297 TYR B O   
6618  C CB  . TYR B 297 ? 0.4570 0.6879 2.1187 -0.0054 0.1512  0.2031  297 TYR B CB  
6619  C CG  . TYR B 297 ? 0.4393 0.7151 2.0936 0.0027  0.1611  0.1934  297 TYR B CG  
6620  C CD1 . TYR B 297 ? 0.4433 0.7610 2.0848 0.0051  0.1701  0.2056  297 TYR B CD1 
6621  C CD2 . TYR B 297 ? 0.4162 0.6942 2.0757 0.0097  0.1615  0.1715  297 TYR B CD2 
6622  C CE1 . TYR B 297 ? 0.4255 0.7837 2.0602 0.0152  0.1788  0.1947  297 TYR B CE1 
6623  C CE2 . TYR B 297 ? 0.4023 0.7189 2.0555 0.0194  0.1698  0.1623  297 TYR B CE2 
6624  C CZ  . TYR B 297 ? 0.4064 0.7628 2.0475 0.0228  0.1785  0.1729  297 TYR B CZ  
6625  O OH  . TYR B 297 ? 0.3894 0.7832 2.0245 0.0349  0.1863  0.1615  297 TYR B OH  
6626  N N   . SER B 298 ? 0.5121 0.6869 2.1584 -0.0038 0.1375  0.2367  298 SER B N   
6627  C CA  . SER B 298 ? 0.5368 0.6768 2.1861 -0.0063 0.1286  0.2517  298 SER B CA  
6628  C C   . SER B 298 ? 0.5564 0.6661 2.2310 -0.0239 0.1222  0.2623  298 SER B C   
6629  O O   . SER B 298 ? 0.5679 0.6360 2.2505 -0.0224 0.1123  0.2608  298 SER B O   
6630  C CB  . SER B 298 ? 0.5605 0.7233 2.1951 -0.0068 0.1320  0.2771  298 SER B CB  
6631  O OG  . SER B 298 ? 0.5984 0.7304 2.2420 -0.0149 0.1240  0.2997  298 SER B OG  
6632  N N   . ASP B 299 ? 0.5616 0.6940 2.2491 -0.0410 0.1274  0.2741  299 ASP B N   
6633  C CA  . ASP B 299 ? 0.5771 0.6852 2.2901 -0.0610 0.1216  0.2848  299 ASP B CA  
6634  C C   . ASP B 299 ? 0.5723 0.7151 2.2981 -0.0745 0.1287  0.2825  299 ASP B C   
6635  O O   . ASP B 299 ? 0.5504 0.7326 2.2650 -0.0656 0.1377  0.2712  299 ASP B O   
6636  C CB  . ASP B 299 ? 0.6102 0.7054 2.3267 -0.0728 0.1183  0.3184  299 ASP B CB  
6637  C CG  . ASP B 299 ? 0.6187 0.7598 2.3198 -0.0750 0.1281  0.3435  299 ASP B CG  
6638  O OD1 . ASP B 299 ? 0.6163 0.7958 2.3240 -0.0885 0.1365  0.3539  299 ASP B OD1 
6639  O OD2 . ASP B 299 ? 0.6285 0.7695 2.3110 -0.0629 0.1272  0.3524  299 ASP B OD2 
6640  N N   . LEU B 300 ? 0.5934 0.7217 2.3436 -0.0960 0.1241  0.2929  300 LEU B N   
6641  C CA  . LEU B 300 ? 0.5862 0.7479 2.3522 -0.1112 0.1295  0.2918  300 LEU B CA  
6642  C C   . LEU B 300 ? 0.5908 0.8089 2.3492 -0.1169 0.1420  0.3137  300 LEU B C   
6643  O O   . LEU B 300 ? 0.5670 0.8275 2.3289 -0.1186 0.1498  0.3062  300 LEU B O   
6644  C CB  . LEU B 300 ? 0.6080 0.7379 2.4026 -0.1345 0.1201  0.2988  300 LEU B CB  
6645  C CG  . LEU B 300 ? 0.5994 0.7581 2.4151 -0.1523 0.1226  0.2939  300 LEU B CG  
6646  C CD1 . LEU B 300 ? 0.5591 0.7562 2.3669 -0.1380 0.1298  0.2687  300 LEU B CD1 
6647  C CD2 . LEU B 300 ? 0.6174 0.7290 2.4571 -0.1662 0.1093  0.2843  300 LEU B CD2 
6648  N N   . ASN B 301 ? 0.6182 0.8393 2.3656 -0.1184 0.1438  0.3402  301 ASN B N   
6649  C CA  . ASN B 301 ? 0.6293 0.9058 2.3683 -0.1239 0.1556  0.3632  301 ASN B CA  
6650  C C   . ASN B 301 ? 0.6001 0.9141 2.3115 -0.0994 0.1647  0.3470  301 ASN B C   
6651  O O   . ASN B 301 ? 0.6059 0.9745 2.3118 -0.0999 0.1759  0.3533  301 ASN B O   
6652  C CB  . ASN B 301 ? 0.6748 0.9414 2.4135 -0.1364 0.1536  0.4001  301 ASN B CB  
6653  C CG  . ASN B 301 ? 0.7161 0.9440 2.4837 -0.1619 0.1442  0.4171  301 ASN B CG  
6654  O OD1 . ASN B 301 ? 0.7231 0.9332 2.5111 -0.1708 0.1390  0.3995  301 ASN B OD1 
6655  N ND2 . ASN B 301 ? 0.7531 0.9673 2.5231 -0.1742 0.1413  0.4512  301 ASN B ND2 
6656  N N   . ASP B 302 ? 0.5738 0.8604 2.2685 -0.0780 0.1599  0.3256  302 ASP B N   
6657  C CA  . ASP B 302 ? 0.5480 0.8642 2.2166 -0.0558 0.1669  0.3105  302 ASP B CA  
6658  C C   . ASP B 302 ? 0.5182 0.8740 2.1892 -0.0511 0.1753  0.2922  302 ASP B C   
6659  O O   . ASP B 302 ? 0.4954 0.8340 2.1762 -0.0477 0.1717  0.2696  302 ASP B O   
6660  C CB  . ASP B 302 ? 0.5347 0.8125 2.1899 -0.0365 0.1593  0.2886  302 ASP B CB  
6661  C CG  . ASP B 302 ? 0.5174 0.8177 2.1454 -0.0145 0.1641  0.2732  302 ASP B CG  
6662  O OD1 . ASP B 302 ? 0.5124 0.8601 2.1300 -0.0106 0.1739  0.2751  302 ASP B OD1 
6663  O OD2 . ASP B 302 ? 0.5100 0.7807 2.1277 -0.0010 0.1575  0.2589  302 ASP B OD2 
6664  N N   . LYS B 303 ? 0.5167 0.9275 2.1776 -0.0491 0.1865  0.3017  303 LYS B N   
6665  C CA  . LYS B 303 ? 0.5027 0.9559 2.1669 -0.0439 0.1950  0.2868  303 LYS B CA  
6666  C C   . LYS B 303 ? 0.4839 0.9516 2.1235 -0.0170 0.1991  0.2621  303 LYS B C   
6667  O O   . LYS B 303 ? 0.4646 0.9648 2.1049 -0.0084 0.2056  0.2474  303 LYS B O   
6668  C CB  . LYS B 303 ? 0.5212 1.0314 2.1920 -0.0583 0.2055  0.3118  303 LYS B CB  
6669  C CG  . LYS B 303 ? 0.5410 1.0452 2.2398 -0.0881 0.2026  0.3371  303 LYS B CG  
6670  C CD  . LYS B 303 ? 0.5264 1.0187 2.2502 -0.0972 0.1982  0.3211  303 LYS B CD  
6671  C CE  . LYS B 303 ? 0.5372 1.0602 2.2875 -0.1238 0.2015  0.3416  303 LYS B CE  
6672  N NZ  . LYS B 303 ? 0.5155 1.0475 2.2824 -0.1237 0.2003  0.3190  303 LYS B NZ  
6673  N N   . TYR B 304 ? 0.4939 0.9364 2.1135 -0.0041 0.1944  0.2570  304 TYR B N   
6674  C CA  . TYR B 304 ? 0.4896 0.9490 2.0839 0.0190  0.1981  0.2380  304 TYR B CA  
6675  C C   . TYR B 304 ? 0.4730 0.8844 2.0593 0.0326  0.1889  0.2150  304 TYR B C   
6676  O O   . TYR B 304 ? 0.4630 0.8719 2.0448 0.0468  0.1893  0.1901  304 TYR B O   
6677  C CB  . TYR B 304 ? 0.5138 1.0040 2.0885 0.0208  0.2028  0.2571  304 TYR B CB  
6678  C CG  . TYR B 304 ? 0.5305 1.0785 2.1094 0.0100  0.2139  0.2793  304 TYR B CG  
6679  C CD1 . TYR B 304 ? 0.5209 1.1203 2.0913 0.0225  0.2242  0.2670  304 TYR B CD1 
6680  C CD2 . TYR B 304 ? 0.5498 1.1023 2.1411 -0.0123 0.2141  0.3133  304 TYR B CD2 
6681  C CE1 . TYR B 304 ? 0.5354 1.1929 2.1098 0.0133  0.2350  0.2871  304 TYR B CE1 
6682  C CE2 . TYR B 304 ? 0.5614 1.1702 2.1569 -0.0234 0.2247  0.3354  304 TYR B CE2 
6683  C CZ  . TYR B 304 ? 0.5542 1.2182 2.1415 -0.0106 0.2356  0.3220  304 TYR B CZ  
6684  O OH  . TYR B 304 ? 0.5615 1.2878 2.1535 -0.0204 0.2471  0.3424  304 TYR B OH  
6685  N N   . GLY B 305 ? 0.4792 0.8540 2.0637 0.0286  0.1805  0.2244  305 GLY B N   
6686  C CA  . GLY B 305 ? 0.4616 0.7932 2.0412 0.0393  0.1716  0.2051  305 GLY B CA  
6687  C C   . GLY B 305 ? 0.4604 0.7957 2.0151 0.0543  0.1702  0.1991  305 GLY B C   
6688  O O   . GLY B 305 ? 0.4691 0.8401 2.0088 0.0570  0.1759  0.2098  305 GLY B O   
6689  N N   . THR B 306 ? 0.4469 0.7466 1.9977 0.0632  0.1623  0.1824  306 THR B N   
6690  C CA  . THR B 306 ? 0.4470 0.7500 1.9759 0.0784  0.1604  0.1689  306 THR B CA  
6691  C C   . THR B 306 ? 0.4249 0.7045 1.9543 0.0889  0.1570  0.1409  306 THR B C   
6692  O O   . THR B 306 ? 0.4035 0.6576 1.9495 0.0841  0.1539  0.1353  306 THR B O   
6693  C CB  . THR B 306 ? 0.4674 0.7539 1.9894 0.0774  0.1529  0.1826  306 THR B CB  
6694  O OG1 . THR B 306 ? 0.4665 0.7101 2.0044 0.0728  0.1446  0.1810  306 THR B OG1 
6695  C CG2 . THR B 306 ? 0.4926 0.8008 2.0135 0.0670  0.1558  0.2134  306 THR B CG2 
6696  N N   . PRO B 307 ? 0.4305 0.7193 1.9417 0.1031  0.1574  0.1226  307 PRO B N   
6697  C CA  . PRO B 307 ? 0.4158 0.6794 1.9264 0.1123  0.1530  0.0983  307 PRO B CA  
6698  C C   . PRO B 307 ? 0.4158 0.6434 1.9305 0.1108  0.1435  0.0961  307 PRO B C   
6699  O O   . PRO B 307 ? 0.4290 0.6555 1.9352 0.1109  0.1390  0.1046  307 PRO B O   
6700  C CB  . PRO B 307 ? 0.4218 0.7072 1.9110 0.1262  0.1554  0.0827  307 PRO B CB  
6701  C CG  . PRO B 307 ? 0.4395 0.7535 1.9149 0.1247  0.1573  0.0993  307 PRO B CG  
6702  C CD  . PRO B 307 ? 0.4455 0.7711 1.9358 0.1108  0.1621  0.1239  307 PRO B CD  
6703  N N   . ARG B 308 ? 0.4044 0.6059 1.9319 0.1103  0.1405  0.0847  308 ARG B N   
6704  C CA  . ARG B 308 ? 0.3973 0.5685 1.9284 0.1114  0.1323  0.0779  308 ARG B CA  
6705  C C   . ARG B 308 ? 0.4066 0.5764 1.9234 0.1217  0.1298  0.0596  308 ARG B C   
6706  O O   . ARG B 308 ? 0.4204 0.6059 1.9271 0.1287  0.1342  0.0488  308 ARG B O   
6707  C CB  . ARG B 308 ? 0.3783 0.5278 1.9270 0.1076  0.1309  0.0717  308 ARG B CB  
6708  C CG  . ARG B 308 ? 0.3817 0.5244 1.9468 0.0963  0.1304  0.0871  308 ARG B CG  
6709  C CD  . ARG B 308 ? 0.3660 0.4937 1.9467 0.0935  0.1296  0.0780  308 ARG B CD  
6710  N NE  . ARG B 308 ? 0.3680 0.4891 1.9650 0.0818  0.1285  0.0904  308 ARG B NE  
6711  C CZ  . ARG B 308 ? 0.3583 0.4821 1.9691 0.0754  0.1304  0.0885  308 ARG B CZ  
6712  N NH1 . ARG B 308 ? 0.3396 0.4735 1.9504 0.0804  0.1339  0.0754  308 ARG B NH1 
6713  N NH2 . ARG B 308 ? 0.3674 0.4822 1.9929 0.0636  0.1278  0.0997  308 ARG B NH2 
6714  N N   . PRO B 309 ? 0.4088 0.5596 1.9252 0.1231  0.1224  0.0540  309 PRO B N   
6715  C CA  . PRO B 309 ? 0.4111 0.5612 1.9149 0.1306  0.1193  0.0371  309 PRO B CA  
6716  C C   . PRO B 309 ? 0.4071 0.5541 1.9097 0.1362  0.1226  0.0200  309 PRO B C   
6717  O O   . PRO B 309 ? 0.4272 0.5814 1.9162 0.1432  0.1221  0.0073  309 PRO B O   
6718  C CB  . PRO B 309 ? 0.4021 0.5313 1.9131 0.1285  0.1114  0.0360  309 PRO B CB  
6719  C CG  . PRO B 309 ? 0.4060 0.5349 1.9242 0.1231  0.1100  0.0557  309 PRO B CG  
6720  C CD  . PRO B 309 ? 0.4017 0.5326 1.9300 0.1180  0.1164  0.0627  309 PRO B CD  
6721  N N   . VAL B 310 ? 0.3937 0.5308 1.9098 0.1339  0.1255  0.0194  310 VAL B N   
6722  C CA  . VAL B 310 ? 0.3900 0.5217 1.9063 0.1401  0.1277  0.0049  310 VAL B CA  
6723  C C   . VAL B 310 ? 0.4104 0.5641 1.9136 0.1488  0.1329  -0.0018 310 VAL B C   
6724  O O   . VAL B 310 ? 0.4063 0.5537 1.9033 0.1571  0.1324  -0.0174 310 VAL B O   
6725  C CB  . VAL B 310 ? 0.3676 0.4915 1.8998 0.1367  0.1302  0.0073  310 VAL B CB  
6726  C CG1 . VAL B 310 ? 0.3672 0.5115 1.9053 0.1327  0.1362  0.0192  310 VAL B CG1 
6727  C CG2 . VAL B 310 ? 0.3633 0.4784 1.8958 0.1438  0.1311  -0.0062 310 VAL B CG2 
6728  N N   . TRP B 311 ? 0.4303 0.6101 1.9301 0.1470  0.1380  0.0102  311 TRP B N   
6729  C CA  . TRP B 311 ? 0.4573 0.6652 1.9451 0.1557  0.1441  0.0053  311 TRP B CA  
6730  C C   . TRP B 311 ? 0.4826 0.6912 1.9522 0.1651  0.1404  -0.0109 311 TRP B C   
6731  O O   . TRP B 311 ? 0.4947 0.7065 1.9573 0.1760  0.1422  -0.0268 311 TRP B O   
6732  C CB  . TRP B 311 ? 0.4609 0.6982 1.9480 0.1495  0.1494  0.0247  311 TRP B CB  
6733  C CG  . TRP B 311 ? 0.4734 0.7482 1.9490 0.1575  0.1571  0.0229  311 TRP B CG  
6734  C CD1 . TRP B 311 ? 0.4917 0.7935 1.9502 0.1612  0.1587  0.0259  311 TRP B CD1 
6735  C CD2 . TRP B 311 ? 0.4752 0.7700 1.9564 0.1629  0.1646  0.0195  311 TRP B CD2 
6736  N NE1 . TRP B 311 ? 0.4968 0.8343 1.9492 0.1690  0.1672  0.0233  311 TRP B NE1 
6737  C CE2 . TRP B 311 ? 0.4903 0.8245 1.9573 0.1702  0.1709  0.0197  311 TRP B CE2 
6738  C CE3 . TRP B 311 ? 0.4707 0.7572 1.9675 0.1628  0.1665  0.0163  311 TRP B CE3 
6739  C CZ2 . TRP B 311 ? 0.5038 0.8693 1.9728 0.1776  0.1793  0.0167  311 TRP B CZ2 
6740  C CZ3 . TRP B 311 ? 0.4797 0.7964 1.9788 0.1698  0.1742  0.0141  311 TRP B CZ3 
6741  C CH2 . TRP B 311 ? 0.4959 0.8518 1.9819 0.1771  0.1808  0.0144  311 TRP B CH2 
6742  N N   . PHE B 312 ? 0.4970 0.7028 1.9593 0.1612  0.1346  -0.0072 312 PHE B N   
6743  C CA  . PHE B 312 ? 0.5257 0.7383 1.9698 0.1685  0.1304  -0.0213 312 PHE B CA  
6744  C C   . PHE B 312 ? 0.5086 0.6923 1.9537 0.1727  0.1246  -0.0419 312 PHE B C   
6745  O O   . PHE B 312 ? 0.5054 0.6913 1.9384 0.1822  0.1234  -0.0602 312 PHE B O   
6746  C CB  . PHE B 312 ? 0.5494 0.7701 1.9876 0.1625  0.1256  -0.0084 312 PHE B CB  
6747  C CG  . PHE B 312 ? 0.5872 0.8394 2.0216 0.1598  0.1320  0.0121  312 PHE B CG  
6748  C CD1 . PHE B 312 ? 0.6226 0.9099 2.0384 0.1672  0.1359  0.0097  312 PHE B CD1 
6749  C CD2 . PHE B 312 ? 0.5867 0.8346 2.0365 0.1496  0.1343  0.0334  312 PHE B CD2 
6750  C CE1 . PHE B 312 ? 0.6298 0.9489 2.0427 0.1636  0.1425  0.0308  312 PHE B CE1 
6751  C CE2 . PHE B 312 ? 0.6106 0.8860 2.0583 0.1453  0.1399  0.0539  312 PHE B CE2 
6752  C CZ  . PHE B 312 ? 0.6259 0.9382 2.0554 0.1519  0.1445  0.0538  312 PHE B CZ  
6753  N N   . ALA B 313 ? 0.4903 0.6470 1.9504 0.1653  0.1209  -0.0386 313 ALA B N   
6754  C CA  . ALA B 313 ? 0.4834 0.6122 1.9473 0.1667  0.1159  -0.0537 313 ALA B CA  
6755  C C   . ALA B 313 ? 0.4895 0.6161 1.9524 0.1769  0.1205  -0.0652 313 ALA B C   
6756  O O   . ALA B 313 ? 0.5136 0.6308 1.9678 0.1844  0.1172  -0.0828 313 ALA B O   
6757  C CB  . ALA B 313 ? 0.4546 0.5625 1.9353 0.1575  0.1134  -0.0449 313 ALA B CB  
6758  N N   . MET B 314 ? 0.4771 0.6124 1.9494 0.1775  0.1274  -0.0557 314 MET B N   
6759  C CA  . MET B 314 ? 0.4964 0.6319 1.9695 0.1883  0.1315  -0.0653 314 MET B CA  
6760  C C   . MET B 314 ? 0.5138 0.6677 1.9701 0.2013  0.1333  -0.0797 314 MET B C   
6761  O O   . MET B 314 ? 0.5172 0.6592 1.9700 0.2125  0.1322  -0.0957 314 MET B O   
6762  C CB  . MET B 314 ? 0.4877 0.6402 1.9727 0.1866  0.1390  -0.0519 314 MET B CB  
6763  C CG  . MET B 314 ? 0.4687 0.6017 1.9702 0.1772  0.1371  -0.0429 314 MET B CG  
6764  S SD  . MET B 314 ? 0.4478 0.5538 1.9549 0.1847  0.1345  -0.0545 314 MET B SD  
6765  C CE  . MET B 314 ? 0.4711 0.6038 1.9791 0.1975  0.1426  -0.0564 314 MET B CE  
6766  N N   . ARG B 315 ? 0.5286 0.7119 1.9743 0.2004  0.1359  -0.0737 315 ARG B N   
6767  C CA  . ARG B 315 ? 0.5570 0.7665 1.9857 0.2130  0.1388  -0.0860 315 ARG B CA  
6768  C C   . ARG B 315 ? 0.5896 0.7778 2.0067 0.2187  0.1302  -0.1081 315 ARG B C   
6769  O O   . ARG B 315 ? 0.6544 0.8370 2.0654 0.2321  0.1298  -0.1272 315 ARG B O   
6770  C CB  . ARG B 315 ? 0.5626 0.8099 1.9814 0.2096  0.1430  -0.0726 315 ARG B CB  
6771  C CG  . ARG B 315 ? 0.5916 0.8713 1.9913 0.2240  0.1467  -0.0865 315 ARG B CG  
6772  C CD  . ARG B 315 ? 0.6023 0.9186 1.9887 0.2204  0.1490  -0.0740 315 ARG B CD  
6773  N NE  . ARG B 315 ? 0.6137 0.9133 1.9943 0.2127  0.1394  -0.0742 315 ARG B NE  
6774  C CZ  . ARG B 315 ? 0.6160 0.9371 1.9886 0.2063  0.1385  -0.0590 315 ARG B CZ  
6775  N NH1 . ARG B 315 ? 0.6239 0.9851 1.9906 0.2067  0.1468  -0.0431 315 ARG B NH1 
6776  N NH2 . ARG B 315 ? 0.6156 0.9196 1.9865 0.1995  0.1292  -0.0586 315 ARG B NH2 
6777  N N   . ASP B 316 ? 0.5857 0.7615 2.0011 0.2084  0.1227  -0.1058 316 ASP B N   
6778  C CA  . ASP B 316 ? 0.6068 0.7617 2.0137 0.2103  0.1131  -0.1260 316 ASP B CA  
6779  C C   . ASP B 316 ? 0.6021 0.7199 2.0188 0.2135  0.1099  -0.1379 316 ASP B C   
6780  O O   . ASP B 316 ? 0.6428 0.7490 2.0508 0.2234  0.1059  -0.1592 316 ASP B O   
6781  C CB  . ASP B 316 ? 0.6135 0.7636 2.0206 0.1977  0.1056  -0.1193 316 ASP B CB  
6782  C CG  . ASP B 316 ? 0.6302 0.8165 2.0260 0.1961  0.1078  -0.1070 316 ASP B CG  
6783  O OD1 . ASP B 316 ? 0.6560 0.8727 2.0427 0.2044  0.1155  -0.1046 316 ASP B OD1 
6784  O OD2 . ASP B 316 ? 0.6223 0.8078 2.0191 0.1869  0.1019  -0.0987 316 ASP B OD2 
6785  N N   . TYR B 317 ? 0.5702 0.6704 2.0042 0.2060  0.1115  -0.1243 317 TYR B N   
6786  C CA  . TYR B 317 ? 0.5828 0.6479 2.0263 0.2074  0.1080  -0.1319 317 TYR B CA  
6787  C C   . TYR B 317 ? 0.6173 0.6818 2.0563 0.2246  0.1113  -0.1456 317 TYR B C   
6788  O O   . TYR B 317 ? 0.6498 0.6855 2.0877 0.2304  0.1055  -0.1614 317 TYR B O   
6789  C CB  . TYR B 317 ? 0.5617 0.6149 2.0232 0.1983  0.1103  -0.1145 317 TYR B CB  
6790  C CG  . TYR B 317 ? 0.5731 0.5914 2.0436 0.1986  0.1062  -0.1196 317 TYR B CG  
6791  C CD1 . TYR B 317 ? 0.5882 0.5814 2.0637 0.1876  0.0983  -0.1211 317 TYR B CD1 
6792  C CD2 . TYR B 317 ? 0.5730 0.5856 2.0480 0.2096  0.1101  -0.1212 317 TYR B CD2 
6793  C CE1 . TYR B 317 ? 0.6006 0.5629 2.0846 0.1865  0.0947  -0.1231 317 TYR B CE1 
6794  C CE2 . TYR B 317 ? 0.5962 0.5768 2.0791 0.2101  0.1061  -0.1233 317 TYR B CE2 
6795  C CZ  . TYR B 317 ? 0.6070 0.5618 2.0943 0.1980  0.0985  -0.1236 317 TYR B CZ  
6796  O OH  . TYR B 317 ? 0.6336 0.5577 2.1290 0.1973  0.0947  -0.1231 317 TYR B OH  
6797  N N   . MET B 318 ? 0.6192 0.7159 2.0565 0.2327  0.1205  -0.1393 318 MET B N   
6798  C CA  . MET B 318 ? 0.6218 0.7226 2.0592 0.2496  0.1252  -0.1482 318 MET B CA  
6799  C C   . MET B 318 ? 0.6514 0.7548 2.0723 0.2657  0.1225  -0.1729 318 MET B C   
6800  O O   . MET B 318 ? 0.6885 0.7882 2.1093 0.2820  0.1243  -0.1844 318 MET B O   
6801  C CB  . MET B 318 ? 0.5988 0.7386 2.0409 0.2520  0.1359  -0.1334 318 MET B CB  
6802  C CG  . MET B 318 ? 0.5693 0.7023 2.0300 0.2433  0.1386  -0.1155 318 MET B CG  
6803  S SD  . MET B 318 ? 0.5513 0.7290 2.0198 0.2465  0.1500  -0.1014 318 MET B SD  
6804  C CE  . MET B 318 ? 0.5466 0.7599 2.0017 0.2404  0.1533  -0.0953 318 MET B CE  
6805  N N   . LYS B 319 ? 0.6671 0.7771 2.0743 0.2621  0.1176  -0.1821 319 LYS B N   
6806  C CA  . LYS B 319 ? 0.7071 0.8260 2.0965 0.2775  0.1152  -0.2070 319 LYS B CA  
6807  C C   . LYS B 319 ? 0.7302 0.8033 2.1195 0.2836  0.1051  -0.2295 319 LYS B C   
6808  O O   . LYS B 319 ? 0.7573 0.8299 2.1323 0.2956  0.1005  -0.2539 319 LYS B O   
6809  C CB  . LYS B 319 ? 0.7211 0.8632 2.0956 0.2704  0.1121  -0.2088 319 LYS B CB  
6810  C CG  . LYS B 319 ? 0.7088 0.8975 2.0798 0.2658  0.1212  -0.1880 319 LYS B CG  
6811  C CD  . LYS B 319 ? 0.7245 0.9315 2.0814 0.2581  0.1164  -0.1877 319 LYS B CD  
6812  C CE  . LYS B 319 ? 0.7584 0.9867 2.0933 0.2725  0.1141  -0.2121 319 LYS B CE  
6813  N NZ  . LYS B 319 ? 0.7647 1.0386 2.0910 0.2859  0.1255  -0.2096 319 LYS B NZ  
6814  N N   . GLY B 320 ? 0.7162 0.7505 2.1213 0.2747  0.1009  -0.2215 320 GLY B N   
6815  C CA  . GLY B 320 ? 0.7451 0.7330 2.1524 0.2786  0.0912  -0.2391 320 GLY B CA  
6816  C C   . GLY B 320 ? 0.7383 0.6923 2.1644 0.2683  0.0895  -0.2228 320 GLY B C   
6817  O O   . GLY B 320 ? 0.7446 0.6858 2.1784 0.2494  0.0853  -0.2114 320 GLY B O   
6818  N N   . LEU B 321 ? 0.7361 0.6787 2.1693 0.2817  0.0927  -0.2218 321 LEU B N   
6819  C CA  . LEU B 321 ? 0.7256 0.6421 2.1754 0.2742  0.0921  -0.2048 321 LEU B CA  
6820  C C   . LEU B 321 ? 0.7716 0.6365 2.2249 0.2736  0.0813  -0.2162 321 LEU B C   
6821  O O   . LEU B 321 ? 0.8239 0.6716 2.2695 0.2887  0.0766  -0.2380 321 LEU B O   
6822  C CB  . LEU B 321 ? 0.7117 0.6455 2.1682 0.2884  0.1007  -0.1956 321 LEU B CB  
6823  C CG  . LEU B 321 ? 0.6745 0.6552 2.1334 0.2846  0.1113  -0.1787 321 LEU B CG  
6824  C CD1 . LEU B 321 ? 0.6486 0.6280 2.1172 0.2624  0.1111  -0.1584 321 LEU B CD1 
6825  C CD2 . LEU B 321 ? 0.6787 0.6984 2.1232 0.2904  0.1159  -0.1876 321 LEU B CD2 
6826  N N   . ILE B 322 ? 0.7672 0.6083 2.2328 0.2558  0.0774  -0.2012 322 ILE B N   
6827  C CA  . ILE B 322 ? 0.7961 0.5892 2.2700 0.2543  0.0692  -0.2028 322 ILE B CA  
6828  C C   . ILE B 322 ? 0.7815 0.5723 2.2670 0.2600  0.0747  -0.1837 322 ILE B C   
6829  O O   . ILE B 322 ? 0.7576 0.5704 2.2504 0.2492  0.0806  -0.1638 322 ILE B O   
6830  C CB  . ILE B 322 ? 0.8034 0.5755 2.2838 0.2303  0.0613  -0.1977 322 ILE B CB  
6831  C CG1 . ILE B 322 ? 0.8254 0.6023 2.2943 0.2249  0.0548  -0.2175 322 ILE B CG1 
6832  C CG2 . ILE B 322 ? 0.8309 0.5545 2.3223 0.2255  0.0536  -0.1938 322 ILE B CG2 
6833  C CD1 . ILE B 322 ? 0.7892 0.6084 2.2533 0.2152  0.0597  -0.2099 322 ILE B CD1 
6834  N N   . ILE B 323 ? 0.7910 0.5561 2.2779 0.2777  0.0722  -0.1907 323 ILE B N   
6835  C CA  . ILE B 323 ? 0.7752 0.5313 2.2730 0.2841  0.0749  -0.1735 323 ILE B CA  
6836  C C   . ILE B 323 ? 0.7815 0.4884 2.2885 0.2735  0.0658  -0.1661 323 ILE B C   
6837  O O   . ILE B 323 ? 0.7487 0.4516 2.2661 0.2669  0.0675  -0.1445 323 ILE B O   
6838  C CB  . ILE B 323 ? 0.8072 0.5704 2.3017 0.3124  0.0782  -0.1835 323 ILE B CB  
6839  C CG1 . ILE B 323 ? 0.7947 0.6124 2.2826 0.3211  0.0885  -0.1863 323 ILE B CG1 
6840  C CG2 . ILE B 323 ? 0.8052 0.5540 2.3110 0.3207  0.0787  -0.1667 323 ILE B CG2 
6841  C CD1 . ILE B 323 ? 0.8162 0.6501 2.2898 0.3219  0.0881  -0.2066 323 ILE B CD1 
6842  N N   . SER B 324 ? 0.8175 0.4880 2.3206 0.2720  0.0559  -0.1843 324 SER B N   
6843  C CA  . SER B 324 ? 0.8478 0.4682 2.3599 0.2607  0.0460  -0.1791 324 SER B CA  
6844  C C   . SER B 324 ? 0.8686 0.4681 2.3761 0.2478  0.0364  -0.1986 324 SER B C   
6845  O O   . SER B 324 ? 0.8944 0.4939 2.3903 0.2609  0.0335  -0.2243 324 SER B O   
6846  C CB  . SER B 324 ? 0.8912 0.4738 2.4064 0.2809  0.0415  -0.1821 324 SER B CB  
6847  O OG  . SER B 324 ? 0.8703 0.4733 2.3901 0.2940  0.0495  -0.1646 324 SER B OG  
6848  N N   . PRO B 325 ? 0.8546 0.4361 2.3712 0.2225  0.0304  -0.1882 325 PRO B N   
6849  C CA  . PRO B 325 ? 0.8244 0.4007 2.3546 0.2084  0.0326  -0.1591 325 PRO B CA  
6850  C C   . PRO B 325 ? 0.7596 0.3865 2.2905 0.2021  0.0436  -0.1424 325 PRO B C   
6851  O O   . PRO B 325 ? 0.7282 0.3888 2.2507 0.2026  0.0477  -0.1519 325 PRO B O   
6852  C CB  . PRO B 325 ? 0.8444 0.3910 2.3830 0.1838  0.0227  -0.1577 325 PRO B CB  
6853  C CG  . PRO B 325 ? 0.8514 0.4107 2.3801 0.1796  0.0186  -0.1823 325 PRO B CG  
6854  C CD  . PRO B 325 ? 0.8664 0.4350 2.3805 0.2064  0.0211  -0.2046 325 PRO B CD  
6855  N N   . LYS B 326 ? 0.7397 0.3696 2.2804 0.1972  0.0477  -0.1177 326 LYS B N   
6856  C CA  . LYS B 326 ? 0.6901 0.3630 2.2333 0.1915  0.0572  -0.1012 326 LYS B CA  
6857  C C   . LYS B 326 ? 0.6848 0.3628 2.2355 0.1661  0.0550  -0.0908 326 LYS B C   
6858  O O   . LYS B 326 ? 0.7033 0.3508 2.2619 0.1530  0.0481  -0.0850 326 LYS B O   
6859  C CB  . LYS B 326 ? 0.6762 0.3535 2.2245 0.2026  0.0624  -0.0831 326 LYS B CB  
6860  C CG  . LYS B 326 ? 0.6804 0.3657 2.2223 0.2287  0.0662  -0.0925 326 LYS B CG  
6861  C CD  . LYS B 326 ? 0.6781 0.3633 2.2259 0.2409  0.0691  -0.0755 326 LYS B CD  
6862  C CE  . LYS B 326 ? 0.6821 0.3823 2.2251 0.2667  0.0732  -0.0845 326 LYS B CE  
6863  N NZ  . LYS B 326 ? 0.7144 0.3930 2.2498 0.2827  0.0686  -0.1084 326 LYS B NZ  
6864  N N   . ASN B 327 ? 0.6495 0.3661 2.1981 0.1595  0.0607  -0.0892 327 ASN B N   
6865  C CA  . ASN B 327 ? 0.6383 0.3681 2.1945 0.1385  0.0600  -0.0788 327 ASN B CA  
6866  C C   . ASN B 327 ? 0.6436 0.3732 2.2104 0.1321  0.0630  -0.0555 327 ASN B C   
6867  O O   . ASN B 327 ? 0.6170 0.3614 2.1834 0.1433  0.0694  -0.0463 327 ASN B O   
6868  C CB  . ASN B 327 ? 0.6081 0.3772 2.1594 0.1369  0.0652  -0.0824 327 ASN B CB  
6869  C CG  . ASN B 327 ? 0.5888 0.3767 2.1486 0.1184  0.0654  -0.0713 327 ASN B CG  
6870  O OD1 . ASN B 327 ? 0.6108 0.3855 2.1768 0.1033  0.0589  -0.0714 327 ASN B OD1 
6871  N ND2 . ASN B 327 ? 0.5460 0.3658 2.1070 0.1193  0.0726  -0.0622 327 ASN B ND2 
6872  N N   . LYS B 328 ? 0.6729 0.3875 2.2492 0.1136  0.0578  -0.0466 328 LYS B N   
6873  C CA  . LYS B 328 ? 0.6820 0.3965 2.2687 0.1042  0.0596  -0.0236 328 LYS B CA  
6874  C C   . LYS B 328 ? 0.7088 0.3908 2.2964 0.1148  0.0574  -0.0155 328 LYS B C   
6875  O O   . LYS B 328 ? 0.7014 0.3924 2.2927 0.1173  0.0618  0.0033  328 LYS B O   
6876  C CB  . LYS B 328 ? 0.6630 0.4202 2.2507 0.1048  0.0686  -0.0123 328 LYS B CB  
6877  C CG  . LYS B 328 ? 0.6612 0.4485 2.2487 0.0961  0.0702  -0.0193 328 LYS B CG  
6878  C CD  . LYS B 328 ? 0.7010 0.4838 2.2969 0.0758  0.0644  -0.0179 328 LYS B CD  
6879  C CE  . LYS B 328 ? 0.6850 0.5031 2.2842 0.0673  0.0670  -0.0173 328 LYS B CE  
6880  N NZ  . LYS B 328 ? 0.7007 0.5296 2.2902 0.0759  0.0671  -0.0338 328 LYS B NZ  
6881  N N   . SER B 329 ? 0.7333 0.3782 2.3170 0.1221  0.0502  -0.0308 329 SER B N   
6882  C CA  . SER B 329 ? 0.7676 0.3713 2.3543 0.1296  0.0451  -0.0242 329 SER B CA  
6883  C C   . SER B 329 ? 0.8066 0.3782 2.4043 0.1077  0.0367  -0.0151 329 SER B C   
6884  O O   . SER B 329 ? 0.7918 0.3726 2.3941 0.0883  0.0341  -0.0185 329 SER B O   
6885  C CB  . SER B 329 ? 0.7828 0.3627 2.3605 0.1506  0.0414  -0.0462 329 SER B CB  
6886  O OG  . SER B 329 ? 0.7839 0.3593 2.3562 0.1459  0.0363  -0.0699 329 SER B OG  
6887  N N   . ILE B 330 ? 0.8354 0.3706 2.4382 0.1112  0.0324  -0.0018 330 ILE B N   
6888  C CA  . ILE B 330 ? 0.8654 0.3671 2.4801 0.0906  0.0247  0.0122  330 ILE B CA  
6889  C C   . ILE B 330 ? 0.9282 0.3714 2.5426 0.1012  0.0144  0.0011  330 ILE B C   
6890  O O   . ILE B 330 ? 0.9383 0.3657 2.5487 0.1230  0.0151  0.0042  330 ILE B O   
6891  C CB  . ILE B 330 ? 0.8569 0.3751 2.4792 0.0828  0.0302  0.0454  330 ILE B CB  
6892  C CG1 . ILE B 330 ? 0.8166 0.3888 2.4410 0.0692  0.0384  0.0530  330 ILE B CG1 
6893  C CG2 . ILE B 330 ? 0.9101 0.3865 2.5446 0.0656  0.0220  0.0640  330 ILE B CG2 
6894  C CD1 . ILE B 330 ? 0.8087 0.4053 2.4386 0.0631  0.0448  0.0832  330 ILE B CD1 
6895  N N   . HIS B 331 ? 0.9714 0.3829 2.5905 0.0862  0.0042  -0.0132 331 HIS B N   
6896  C CA  . HIS B 331 ? 1.0368 0.3914 2.6545 0.0970  -0.0068 -0.0309 331 HIS B CA  
6897  C C   . HIS B 331 ? 1.0948 0.3995 2.7274 0.0760  -0.0176 -0.0157 331 HIS B C   
6898  O O   . HIS B 331 ? 1.1106 0.4032 2.7508 0.0527  -0.0252 -0.0235 331 HIS B O   
6899  C CB  . HIS B 331 ? 1.0367 0.3949 2.6443 0.1027  -0.0107 -0.0670 331 HIS B CB  
6900  C CG  . HIS B 331 ? 0.9988 0.3975 2.5922 0.1267  -0.0007 -0.0787 331 HIS B CG  
6901  N ND1 . HIS B 331 ? 1.0241 0.4085 2.6066 0.1530  -0.0025 -0.1023 331 HIS B ND1 
6902  C CD2 . HIS B 331 ? 0.9612 0.4129 2.5508 0.1289  0.0110  -0.0685 331 HIS B CD2 
6903  C CE1 . HIS B 331 ? 0.9884 0.4185 2.5611 0.1689  0.0083  -0.1050 331 HIS B CE1 
6904  N NE2 . HIS B 331 ? 0.9552 0.4247 2.5322 0.1542  0.0162  -0.0850 331 HIS B NE2 
6905  N N   . THR B 332 ? 1.1355 0.4104 2.7726 0.0846  -0.0187 0.0062  332 THR B N   
6906  C CA  . THR B 332 ? 1.2043 0.4231 2.8553 0.0682  -0.0299 0.0211  332 THR B CA  
6907  C C   . THR B 332 ? 1.2733 0.4311 2.9212 0.0847  -0.0422 -0.0061 332 THR B C   
6908  O O   . THR B 332 ? 1.3300 0.4442 2.9803 0.0994  -0.0471 0.0039  332 THR B O   
6909  C CB  . THR B 332 ? 1.2066 0.4245 2.8634 0.0697  -0.0253 0.0599  332 THR B CB  
6910  O OG1 . THR B 332 ? 1.2061 0.4229 2.8519 0.1040  -0.0217 0.0544  332 THR B OG1 
6911  C CG2 . THR B 332 ? 1.1588 0.4394 2.8175 0.0555  -0.0131 0.0845  332 THR B CG2 
6912  N N   . ASN B 333 ? 1.2872 0.4436 2.9291 0.0837  -0.0475 -0.0411 333 ASN B N   
6913  C CA  . ASN B 333 ? 1.3483 0.4520 2.9856 0.1000  -0.0594 -0.0727 333 ASN B CA  
6914  C C   . ASN B 333 ? 1.3338 0.4540 2.9638 0.0933  -0.0633 -0.1084 333 ASN B C   
6915  O O   . ASN B 333 ? 1.2882 0.4672 2.9106 0.0912  -0.0535 -0.1119 333 ASN B O   
6916  C CB  . ASN B 333 ? 1.3740 0.4741 2.9994 0.1392  -0.0551 -0.0814 333 ASN B CB  
6917  C CG  . ASN B 333 ? 1.4854 0.5163 3.1112 0.1561  -0.0689 -0.1028 333 ASN B CG  
6918  O OD1 . ASN B 333 ? 1.5592 0.5746 3.1787 0.1596  -0.0766 -0.1387 333 ASN B OD1 
6919  N ND2 . ASN B 333 ? 1.5357 0.5241 3.1685 0.1674  -0.0727 -0.0822 333 ASN B ND2 
6920  N N   . THR B 334 ? 1.3876 0.4549 3.0195 0.0912  -0.0781 -0.1349 334 THR B N   
6921  C CA  . THR B 334 ? 1.3968 0.4737 3.0219 0.0843  -0.0845 -0.1705 334 THR B CA  
6922  C C   . THR B 334 ? 1.4011 0.4877 3.0064 0.1192  -0.0824 -0.2048 334 THR B C   
6923  O O   . THR B 334 ? 1.3999 0.4904 2.9966 0.1195  -0.0887 -0.2382 334 THR B O   
6924  C CB  . THR B 334 ? 1.4749 0.4914 3.1131 0.0614  -0.1027 -0.1824 334 THR B CB  
6925  O OG1 . THR B 334 ? 1.5354 0.4823 3.1769 0.0779  -0.1129 -0.1876 334 THR B OG1 
6926  C CG2 . THR B 334 ? 1.4804 0.4982 3.1388 0.0230  -0.1043 -0.1499 334 THR B CG2 
6927  N N   . LYS B 335 ? 1.4140 0.5068 3.0124 0.1486  -0.0738 -0.1963 335 LYS B N   
6928  C CA  . LYS B 335 ? 1.4341 0.5462 3.0148 0.1828  -0.0691 -0.2241 335 LYS B CA  
6929  C C   . LYS B 335 ? 1.3465 0.5259 2.9198 0.1930  -0.0515 -0.2062 335 LYS B C   
6930  O O   . LYS B 335 ? 1.3497 0.5323 2.9285 0.1997  -0.0448 -0.1781 335 LYS B O   
6931  C CB  . LYS B 335 ? 1.5366 0.5934 3.1176 0.2109  -0.0760 -0.2320 335 LYS B CB  
6932  C CG  . LYS B 335 ? 1.6423 0.6494 3.2184 0.2223  -0.0908 -0.2725 335 LYS B CG  
6933  C CD  . LYS B 335 ? 1.7317 0.6992 3.3181 0.1899  -0.1060 -0.2826 335 LYS B CD  
6934  C CE  . LYS B 335 ? 1.8080 0.7596 3.3831 0.1992  -0.1169 -0.3302 335 LYS B CE  
6935  N NZ  . LYS B 335 ? 1.7845 0.8061 3.3407 0.2112  -0.1058 -0.3485 335 LYS B NZ  
6936  N N   . ILE B 336 ? 1.2803 0.5124 2.8414 0.1938  -0.0446 -0.2222 336 ILE B N   
6937  C CA  . ILE B 336 ? 1.1992 0.4949 2.7546 0.1991  -0.0289 -0.2060 336 ILE B CA  
6938  C C   . ILE B 336 ? 1.1711 0.4925 2.7109 0.2321  -0.0222 -0.2268 336 ILE B C   
6939  O O   . ILE B 336 ? 1.1799 0.5143 2.7078 0.2378  -0.0245 -0.2558 336 ILE B O   
6940  C CB  . ILE B 336 ? 1.1757 0.5161 2.7302 0.1747  -0.0253 -0.2044 336 ILE B CB  
6941  C CG1 . ILE B 336 ? 1.2028 0.5198 2.7721 0.1409  -0.0343 -0.1931 336 ILE B CG1 
6942  C CG2 . ILE B 336 ? 1.1094 0.5077 2.6617 0.1768  -0.0100 -0.1825 336 ILE B CG2 
6943  C CD1 . ILE B 336 ? 1.1980 0.5108 2.7824 0.1262  -0.0303 -0.1551 336 ILE B CD1 
6944  N N   . PRO B 337 ? 1.1264 0.4605 2.6656 0.2543  -0.0136 -0.2131 337 PRO B N   
6945  C CA  . PRO B 337 ? 1.1019 0.4700 2.6278 0.2839  -0.0058 -0.2306 337 PRO B CA  
6946  C C   . PRO B 337 ? 1.0554 0.4841 2.5708 0.2774  0.0032  -0.2375 337 PRO B C   
6947  O O   . PRO B 337 ? 0.9964 0.4564 2.5164 0.2576  0.0096  -0.2163 337 PRO B O   
6948  C CB  . PRO B 337 ? 1.0796 0.4583 2.6108 0.3006  0.0022  -0.2065 337 PRO B CB  
6949  C CG  . PRO B 337 ? 1.1047 0.4353 2.6506 0.2865  -0.0052 -0.1823 337 PRO B CG  
6950  C CD  . PRO B 337 ? 1.1129 0.4317 2.6643 0.2526  -0.0114 -0.1802 337 PRO B CD  
6951  N N   . LEU B 338 ? 1.0732 0.5167 2.5743 0.2952  0.0031  -0.2675 338 LEU B N   
6952  C CA  . LEU B 338 ? 1.0461 0.5458 2.5354 0.2926  0.0110  -0.2758 338 LEU B CA  
6953  C C   . LEU B 338 ? 1.0507 0.5903 2.5310 0.3209  0.0219  -0.2810 338 LEU B C   
6954  O O   . LEU B 338 ? 1.0746 0.5957 2.5508 0.3464  0.0191  -0.2988 338 LEU B O   
6955  C CB  . LEU B 338 ? 1.0744 0.5644 2.5540 0.2859  0.0013  -0.3055 338 LEU B CB  
6956  C CG  . LEU B 338 ? 1.0490 0.5959 2.5145 0.2838  0.0080  -0.3152 338 LEU B CG  
6957  C CD1 . LEU B 338 ? 1.0508 0.5970 2.5152 0.2584  -0.0002 -0.3228 338 LEU B CD1 
6958  C CD2 . LEU B 338 ? 1.0740 0.6373 2.5229 0.3124  0.0096  -0.3447 338 LEU B CD2 
6959  N N   . GLU B 339 ? 1.0304 0.6250 2.5086 0.3158  0.0339  -0.2656 339 GLU B N   
6960  C CA  . GLU B 339 ? 1.0189 0.6592 2.4911 0.3375  0.0454  -0.2656 339 GLU B CA  
6961  C C   . GLU B 339 ? 0.9619 0.6584 2.4260 0.3276  0.0542  -0.2626 339 GLU B C   
6962  O O   . GLU B 339 ? 0.9143 0.6289 2.3854 0.3085  0.0588  -0.2400 339 GLU B O   
6963  C CB  . GLU B 339 ? 1.0157 0.6601 2.5000 0.3435  0.0516  -0.2398 339 GLU B CB  
6964  C CG  . GLU B 339 ? 1.0738 0.6749 2.5633 0.3646  0.0454  -0.2443 339 GLU B CG  
6965  C CD  . GLU B 339 ? 1.0618 0.6641 2.5634 0.3698  0.0498  -0.2175 339 GLU B CD  
6966  O OE1 . GLU B 339 ? 0.9958 0.6465 2.4985 0.3750  0.0605  -0.2053 339 GLU B OE1 
6967  O OE2 . GLU B 339 ? 1.0917 0.6448 2.6019 0.3681  0.0415  -0.2088 339 GLU B OE2 
6968  N N   . LEU B 340 ? 0.9764 0.7009 2.4257 0.3420  0.0566  -0.2849 340 LEU B N   
6969  C CA  . LEU B 340 ? 0.9557 0.7321 2.3956 0.3340  0.0641  -0.2829 340 LEU B CA  
6970  C C   . LEU B 340 ? 0.9611 0.7864 2.3946 0.3549  0.0757  -0.2845 340 LEU B C   
6971  O O   . LEU B 340 ? 1.0023 0.8220 2.4348 0.3791  0.0763  -0.2966 340 LEU B O   
6972  C CB  . LEU B 340 ? 0.9777 0.7489 2.4041 0.3292  0.0559  -0.3076 340 LEU B CB  
6973  C CG  . LEU B 340 ? 0.9726 0.7166 2.4048 0.3020  0.0464  -0.3028 340 LEU B CG  
6974  C CD1 . LEU B 340 ? 0.9944 0.6835 2.4419 0.2942  0.0385  -0.2943 340 LEU B CD1 
6975  C CD2 . LEU B 340 ? 0.9983 0.7404 2.4162 0.3012  0.0376  -0.3312 340 LEU B CD2 
6976  N N   . TYR B 341 ? 0.9324 0.8065 2.3620 0.3454  0.0844  -0.2726 341 TYR B N   
6977  C CA  . TYR B 341 ? 0.9236 0.8504 2.3467 0.3612  0.0957  -0.2732 341 TYR B CA  
6978  C C   . TYR B 341 ? 0.8983 0.8661 2.3086 0.3514  0.0994  -0.2744 341 TYR B C   
6979  O O   . TYR B 341 ? 0.8606 0.8476 2.2758 0.3325  0.1035  -0.2531 341 TYR B O   
6980  C CB  . TYR B 341 ? 0.9000 0.8526 2.3364 0.3604  0.1055  -0.2479 341 TYR B CB  
6981  C CG  . TYR B 341 ? 0.9067 0.9097 2.3390 0.3801  0.1161  -0.2511 341 TYR B CG  
6982  C CD1 . TYR B 341 ? 0.9237 0.9225 2.3563 0.4069  0.1163  -0.2657 341 TYR B CD1 
6983  C CD2 . TYR B 341 ? 0.8539 0.9093 2.2832 0.3720  0.1257  -0.2388 341 TYR B CD2 
6984  C CE1 . TYR B 341 ? 0.9280 0.9773 2.3581 0.4251  0.1263  -0.2686 341 TYR B CE1 
6985  C CE2 . TYR B 341 ? 0.8517 0.9564 2.2788 0.3881  0.1356  -0.2403 341 TYR B CE2 
6986  C CZ  . TYR B 341 ? 0.9064 1.0101 2.3340 0.4147  0.1362  -0.2554 341 TYR B CZ  
6987  O OH  . TYR B 341 ? 0.9306 1.0868 2.3574 0.4314  0.1464  -0.2568 341 TYR B OH  
6988  N N   . ASN B 342 ? 0.9250 0.9076 2.3187 0.3662  0.0980  -0.2996 342 ASN B N   
6989  C CA  . ASN B 342 ? 0.9180 0.9316 2.2966 0.3577  0.0982  -0.3049 342 ASN B CA  
6990  C C   . ASN B 342 ? 0.9034 0.9791 2.2728 0.3703  0.1106  -0.3024 342 ASN B C   
6991  O O   . ASN B 342 ? 0.9018 0.9928 2.2711 0.3920  0.1161  -0.3105 342 ASN B O   
6992  C CB  . ASN B 342 ? 0.9579 0.9446 2.3233 0.3627  0.0863  -0.3358 342 ASN B CB  
6993  C CG  . ASN B 342 ? 0.9652 0.8925 2.3413 0.3472  0.0738  -0.3367 342 ASN B CG  
6994  O OD1 . ASN B 342 ? 0.9316 0.8472 2.3211 0.3267  0.0739  -0.3127 342 ASN B OD1 
6995  N ND2 . ASN B 342 ? 1.0054 0.8955 2.3757 0.3559  0.0628  -0.3646 342 ASN B ND2 
6996  N N   . ASP B 343 ? 0.8842 0.9967 2.2463 0.3564  0.1146  -0.2900 343 ASP B N   
6997  C CA  . ASP B 343 ? 0.8826 1.0561 2.2343 0.3657  0.1258  -0.2866 343 ASP B CA  
6998  C C   . ASP B 343 ? 0.9225 1.1117 2.2514 0.3787  0.1217  -0.3153 343 ASP B C   
6999  O O   . ASP B 343 ? 0.9615 1.1111 2.2853 0.3805  0.1100  -0.3377 343 ASP B O   
7000  C CB  . ASP B 343 ? 0.8424 1.0463 2.1999 0.3453  0.1328  -0.2554 343 ASP B CB  
7001  C CG  . ASP B 343 ? 0.8561 1.0795 2.1995 0.3329  0.1300  -0.2533 343 ASP B CG  
7002  O OD1 . ASP B 343 ? 0.8846 1.0743 2.2291 0.3192  0.1201  -0.2552 343 ASP B OD1 
7003  O OD2 . ASP B 343 ? 0.8667 1.1410 2.1985 0.3370  0.1379  -0.2485 343 ASP B OD2 
7004  N N   . LYS B 344 ? 0.9248 1.1730 2.2403 0.3871  0.1310  -0.3145 344 LYS B N   
7005  C CA  . LYS B 344 ? 0.9538 1.2256 2.2465 0.4051  0.1290  -0.3442 344 LYS B CA  
7006  C C   . LYS B 344 ? 0.9438 1.2055 2.2225 0.3921  0.1183  -0.3540 344 LYS B C   
7007  O O   . LYS B 344 ? 0.9828 1.2534 2.2426 0.4061  0.1132  -0.3835 344 LYS B O   
7008  C CB  . LYS B 344 ? 0.9586 1.3031 2.2404 0.4166  0.1428  -0.3379 344 LYS B CB  
7009  C CG  . LYS B 344 ? 0.9527 1.3416 2.2264 0.3986  0.1481  -0.3138 344 LYS B CG  
7010  C CD  . LYS B 344 ? 0.9286 1.3450 2.2185 0.3846  0.1596  -0.2763 344 LYS B CD  
7011  C CE  . LYS B 344 ? 0.9231 1.3944 2.2027 0.3735  0.1671  -0.2542 344 LYS B CE  
7012  N NZ  . LYS B 344 ? 0.9627 1.4805 2.2166 0.3896  0.1693  -0.2738 344 LYS B NZ  
7013  N N   . ASP B 345 ? 0.8781 1.1234 2.1661 0.3668  0.1147  -0.3309 345 ASP B N   
7014  C CA  . ASP B 345 ? 0.8759 1.1230 2.1516 0.3534  0.1060  -0.3350 345 ASP B CA  
7015  C C   . ASP B 345 ? 0.8678 1.0564 2.1472 0.3472  0.0904  -0.3558 345 ASP B C   
7016  O O   . ASP B 345 ? 0.8733 1.0633 2.1394 0.3424  0.0810  -0.3713 345 ASP B O   
7017  C CB  . ASP B 345 ? 0.8495 1.1151 2.1324 0.3312  0.1102  -0.2999 345 ASP B CB  
7018  C CG  . ASP B 345 ? 0.8300 1.1544 2.1087 0.3331  0.1242  -0.2770 345 ASP B CG  
7019  O OD1 . ASP B 345 ? 0.8618 1.2318 2.1203 0.3443  0.1277  -0.2869 345 ASP B OD1 
7020  O OD2 . ASP B 345 ? 0.7815 1.1072 2.0773 0.3226  0.1314  -0.2492 345 ASP B OD2 
7021  N N   . VAL B 346 ? 0.8452 0.9846 2.1431 0.3462  0.0875  -0.3547 346 VAL B N   
7022  C CA  . VAL B 346 ? 0.8536 0.9346 2.1586 0.3383  0.0733  -0.3703 346 VAL B CA  
7023  C C   . VAL B 346 ? 0.9003 0.9663 2.1910 0.3578  0.0649  -0.4101 346 VAL B C   
7024  O O   . VAL B 346 ? 0.9255 0.9844 2.2165 0.3793  0.0683  -0.4235 346 VAL B O   
7025  C CB  . VAL B 346 ? 0.8318 0.8697 2.1602 0.3327  0.0741  -0.3539 346 VAL B CB  
7026  C CG1 . VAL B 346 ? 0.8553 0.8313 2.1921 0.3261  0.0600  -0.3693 346 VAL B CG1 
7027  C CG2 . VAL B 346 ? 0.7839 0.8340 2.1264 0.3128  0.0808  -0.3177 346 VAL B CG2 
7028  N N   . LYS B 347 ? 0.9170 0.9782 2.1956 0.3508  0.0533  -0.4300 347 LYS B N   
7029  C CA  . LYS B 347 ? 0.9699 1.0144 2.2345 0.3674  0.0433  -0.4708 347 LYS B CA  
7030  C C   . LYS B 347 ? 0.9932 0.9695 2.2706 0.3552  0.0276  -0.4843 347 LYS B C   
7031  O O   . LYS B 347 ? 1.0461 0.9883 2.3203 0.3701  0.0192  -0.5149 347 LYS B O   
7032  C CB  . LYS B 347 ? 0.9874 1.0806 2.2265 0.3718  0.0411  -0.4885 347 LYS B CB  
7033  C CG  . LYS B 347 ? 0.9822 1.1433 2.2060 0.3886  0.0562  -0.4813 347 LYS B CG  
7034  C CD  . LYS B 347 ? 1.0097 1.1769 2.2312 0.4173  0.0639  -0.4969 347 LYS B CD  
7035  C CE  . LYS B 347 ? 0.9857 1.1399 2.2289 0.4183  0.0742  -0.4704 347 LYS B CE  
7036  N NZ  . LYS B 347 ? 1.0097 1.1894 2.2489 0.4469  0.0841  -0.4817 347 LYS B NZ  
7037  N N   . LYS B 348 ? 0.9570 0.9130 2.2499 0.3285  0.0234  -0.4615 348 LYS B N   
7038  C CA  . LYS B 348 ? 0.9743 0.8694 2.2809 0.3141  0.0090  -0.4710 348 LYS B CA  
7039  C C   . LYS B 348 ? 0.9316 0.8049 2.2615 0.2920  0.0116  -0.4361 348 LYS B C   
7040  O O   . LYS B 348 ? 0.8973 0.8048 2.2296 0.2802  0.0191  -0.4098 348 LYS B O   
7041  C CB  . LYS B 348 ? 0.9940 0.8901 2.2905 0.3013  -0.0051 -0.4927 348 LYS B CB  
7042  C CG  . LYS B 348 ? 1.0251 0.8577 2.3359 0.2866  -0.0211 -0.5065 348 LYS B CG  
7043  C CD  . LYS B 348 ? 1.0546 0.8878 2.3557 0.2752  -0.0367 -0.5332 348 LYS B CD  
7044  C CE  . LYS B 348 ? 1.0174 0.8835 2.3212 0.2520  -0.0371 -0.5115 348 LYS B CE  
7045  N NZ  . LYS B 348 ? 1.0451 0.9339 2.3324 0.2481  -0.0490 -0.5379 348 LYS B NZ  
7046  N N   . VAL B 349 ? 0.9456 0.7620 2.2923 0.2872  0.0048  -0.4368 349 VAL B N   
7047  C CA  . VAL B 349 ? 0.9142 0.7064 2.2828 0.2662  0.0057  -0.4066 349 VAL B CA  
7048  C C   . VAL B 349 ? 0.9432 0.6852 2.3227 0.2478  -0.0101 -0.4176 349 VAL B C   
7049  O O   . VAL B 349 ? 1.0024 0.7055 2.3798 0.2571  -0.0198 -0.4441 349 VAL B O   
7050  C CB  . VAL B 349 ? 0.9045 0.6799 2.2855 0.2772  0.0149  -0.3886 349 VAL B CB  
7051  C CG1 . VAL B 349 ? 0.8780 0.6304 2.2805 0.2554  0.0152  -0.3587 349 VAL B CG1 
7052  C CG2 . VAL B 349 ? 0.8749 0.7010 2.2474 0.2943  0.0302  -0.3778 349 VAL B CG2 
7053  N N   . VAL B 350 ? 0.9058 0.6488 2.2981 0.2220  -0.0125 -0.3970 350 VAL B N   
7054  C CA  . VAL B 350 ? 0.9221 0.6269 2.3261 0.2004  -0.0271 -0.4045 350 VAL B CA  
7055  C C   . VAL B 350 ? 0.8857 0.5769 2.3119 0.1799  -0.0239 -0.3713 350 VAL B C   
7056  O O   . VAL B 350 ? 0.8439 0.5707 2.2726 0.1757  -0.0135 -0.3465 350 VAL B O   
7057  C CB  . VAL B 350 ? 0.9244 0.6584 2.3181 0.1885  -0.0356 -0.4193 350 VAL B CB  
7058  C CG1 . VAL B 350 ? 0.9447 0.6455 2.3534 0.1625  -0.0506 -0.4243 350 VAL B CG1 
7059  C CG2 . VAL B 350 ? 0.9575 0.7101 2.3272 0.2091  -0.0389 -0.4533 350 VAL B CG2 
7060  N N   . VAL B 351 ? 0.9065 0.5475 2.3487 0.1668  -0.0332 -0.3710 351 VAL B N   
7061  C CA  . VAL B 351 ? 0.8761 0.5070 2.3390 0.1462  -0.0307 -0.3401 351 VAL B CA  
7062  C C   . VAL B 351 ? 0.8943 0.5070 2.3691 0.1192  -0.0444 -0.3450 351 VAL B C   
7063  O O   . VAL B 351 ? 0.9434 0.5191 2.4182 0.1163  -0.0576 -0.3691 351 VAL B O   
7064  C CB  . VAL B 351 ? 0.8845 0.4766 2.3591 0.1532  -0.0269 -0.3253 351 VAL B CB  
7065  C CG1 . VAL B 351 ? 0.8551 0.4439 2.3495 0.1320  -0.0236 -0.2927 351 VAL B CG1 
7066  C CG2 . VAL B 351 ? 0.8695 0.4805 2.3336 0.1804  -0.0144 -0.3226 351 VAL B CG2 
7067  N N   . LYS B 352 ? 0.8546 0.4937 2.3407 0.0997  -0.0412 -0.3215 352 LYS B N   
7068  C CA  . LYS B 352 ? 0.8597 0.4945 2.3588 0.0726  -0.0525 -0.3221 352 LYS B CA  
7069  C C   . LYS B 352 ? 0.8305 0.4564 2.3517 0.0541  -0.0485 -0.2905 352 LYS B C   
7070  O O   . LYS B 352 ? 0.7901 0.4344 2.3135 0.0608  -0.0357 -0.2667 352 LYS B O   
7071  C CB  . LYS B 352 ? 0.8365 0.5226 2.3278 0.0662  -0.0536 -0.3257 352 LYS B CB  
7072  C CG  . LYS B 352 ? 0.8667 0.5660 2.3370 0.0779  -0.0610 -0.3586 352 LYS B CG  
7073  C CD  . LYS B 352 ? 0.8381 0.5941 2.2976 0.0766  -0.0595 -0.3575 352 LYS B CD  
7074  C CE  . LYS B 352 ? 0.8636 0.6378 2.2986 0.0938  -0.0635 -0.3869 352 LYS B CE  
7075  N NZ  . LYS B 352 ? 0.8352 0.6660 2.2578 0.0962  -0.0600 -0.3814 352 LYS B NZ  
7076  N N   . PHE B 353 ? 0.8513 0.4509 2.3887 0.0304  -0.0601 -0.2914 353 PHE B N   
7077  C CA  . PHE B 353 ? 0.8296 0.4279 2.3887 0.0090  -0.0577 -0.2625 353 PHE B CA  
7078  C C   . PHE B 353 ? 0.8374 0.4471 2.4090 -0.0183 -0.0692 -0.2671 353 PHE B C   
7079  O O   . PHE B 353 ? 0.8820 0.4581 2.4584 -0.0301 -0.0832 -0.2861 353 PHE B O   
7080  C CB  . PHE B 353 ? 0.8566 0.4032 2.4272 0.0074  -0.0585 -0.2510 353 PHE B CB  
7081  C CG  . PHE B 353 ? 0.8413 0.3900 2.4341 -0.0164 -0.0564 -0.2208 353 PHE B CG  
7082  C CD1 . PHE B 353 ? 0.7892 0.3783 2.3853 -0.0155 -0.0433 -0.1950 353 PHE B CD1 
7083  C CD2 . PHE B 353 ? 0.8814 0.3933 2.4918 -0.0400 -0.0677 -0.2185 353 PHE B CD2 
7084  C CE1 . PHE B 353 ? 0.7759 0.3721 2.3911 -0.0360 -0.0408 -0.1686 353 PHE B CE1 
7085  C CE2 . PHE B 353 ? 0.8685 0.3878 2.4989 -0.0618 -0.0649 -0.1894 353 PHE B CE2 
7086  C CZ  . PHE B 353 ? 0.8151 0.3786 2.4473 -0.0590 -0.0511 -0.1650 353 PHE B CZ  
7087  N N   . ARG B 354 ? 0.7920 0.4491 2.3697 -0.0275 -0.0633 -0.2495 354 ARG B N   
7088  C CA  . ARG B 354 ? 0.7899 0.4740 2.3779 -0.0498 -0.0722 -0.2527 354 ARG B CA  
7089  C C   . ARG B 354 ? 0.8128 0.5070 2.3847 -0.0443 -0.0828 -0.2850 354 ARG B C   
7090  O O   . ARG B 354 ? 0.8402 0.5300 2.4200 -0.0632 -0.0967 -0.2999 354 ARG B O   
7091  C CB  . ARG B 354 ? 0.8161 0.4738 2.4286 -0.0783 -0.0807 -0.2431 354 ARG B CB  
7092  C CG  . ARG B 354 ? 0.7931 0.4502 2.4205 -0.0840 -0.0696 -0.2093 354 ARG B CG  
7093  C CD  . ARG B 354 ? 0.8300 0.4542 2.4801 -0.1112 -0.0782 -0.1996 354 ARG B CD  
7094  N NE  . ARG B 354 ? 0.8194 0.4351 2.4811 -0.1141 -0.0680 -0.1682 354 ARG B NE  
7095  C CZ  . ARG B 354 ? 0.8489 0.4367 2.5302 -0.1359 -0.0723 -0.1518 354 ARG B CZ  
7096  N NH1 . ARG B 354 ? 0.8881 0.4574 2.5835 -0.1610 -0.0866 -0.1616 354 ARG B NH1 
7097  N NH2 . ARG B 354 ? 0.8395 0.4204 2.5268 -0.1337 -0.0623 -0.1242 354 ARG B NH2 
7098  N N   . ASP B 355 ? 0.8017 0.5120 2.3512 -0.0188 -0.0760 -0.2949 355 ASP B N   
7099  C CA  . ASP B 355 ? 0.8153 0.5514 2.3459 -0.0099 -0.0823 -0.3205 355 ASP B CA  
7100  C C   . ASP B 355 ? 0.8780 0.5745 2.4026 -0.0106 -0.0969 -0.3538 355 ASP B C   
7101  O O   . ASP B 355 ? 0.8979 0.6128 2.4121 -0.0122 -0.1072 -0.3777 355 ASP B O   
7102  C CB  . ASP B 355 ? 0.7910 0.5770 2.3267 -0.0234 -0.0854 -0.3140 355 ASP B CB  
7103  C CG  . ASP B 355 ? 0.7388 0.5615 2.2820 -0.0225 -0.0722 -0.2825 355 ASP B CG  
7104  O OD1 . ASP B 355 ? 0.7110 0.5522 2.2405 -0.0023 -0.0605 -0.2742 355 ASP B OD1 
7105  O OD2 . ASP B 355 ? 0.7267 0.5609 2.2903 -0.0422 -0.0739 -0.2665 355 ASP B OD2 
7106  N N   . LYS B 356 ? 0.9134 0.5559 2.4441 -0.0082 -0.0982 -0.3557 356 LYS B N   
7107  C CA  . LYS B 356 ? 0.9746 0.5724 2.4980 -0.0029 -0.1107 -0.3881 356 LYS B CA  
7108  C C   . LYS B 356 ? 0.9877 0.5625 2.4972 0.0264  -0.1015 -0.3919 356 LYS B C   
7109  O O   . LYS B 356 ? 0.9585 0.5316 2.4735 0.0332  -0.0887 -0.3653 356 LYS B O   
7110  C CB  . LYS B 356 ? 1.0139 0.5620 2.5604 -0.0288 -0.1235 -0.3880 356 LYS B CB  
7111  C CG  . LYS B 356 ? 1.0795 0.5725 2.6207 -0.0231 -0.1375 -0.4216 356 LYS B CG  
7112  C CD  . LYS B 356 ? 1.1270 0.5706 2.6911 -0.0520 -0.1534 -0.4255 356 LYS B CD  
7113  C CE  . LYS B 356 ? 1.1321 0.5312 2.7147 -0.0585 -0.1487 -0.3975 356 LYS B CE  
7114  N NZ  . LYS B 356 ? 1.1887 0.5330 2.7905 -0.0836 -0.1659 -0.4064 356 LYS B NZ  
7115  N N   . VAL B 357 ? 1.0349 0.5939 2.5267 0.0440  -0.1084 -0.4258 357 VAL B N   
7116  C CA  . VAL B 357 ? 1.0484 0.5948 2.5251 0.0748  -0.0999 -0.4333 357 VAL B CA  
7117  C C   . VAL B 357 ? 1.0953 0.5756 2.5853 0.0758  -0.1039 -0.4313 357 VAL B C   
7118  O O   . VAL B 357 ? 1.1530 0.5890 2.6526 0.0616  -0.1193 -0.4483 357 VAL B O   
7119  C CB  . VAL B 357 ? 1.0741 0.6358 2.5257 0.0949  -0.1053 -0.4715 357 VAL B CB  
7120  C CG1 . VAL B 357 ? 1.0863 0.6334 2.5237 0.1274  -0.0976 -0.4826 357 VAL B CG1 
7121  C CG2 . VAL B 357 ? 1.0357 0.6646 2.4727 0.0957  -0.1007 -0.4704 357 VAL B CG2 
7122  N N   . ILE B 358 ? 1.0783 0.5524 2.5691 0.0925  -0.0907 -0.4104 358 ILE B N   
7123  C CA  . ILE B 358 ? 1.1205 0.5349 2.6217 0.0984  -0.0935 -0.4068 358 ILE B CA  
7124  C C   . ILE B 358 ? 1.1420 0.5516 2.6266 0.1341  -0.0866 -0.4209 358 ILE B C   
7125  O O   . ILE B 358 ? 1.1855 0.5430 2.6739 0.1455  -0.0922 -0.4300 358 ILE B O   
7126  C CB  . ILE B 358 ? 1.0886 0.4943 2.6105 0.0828  -0.0861 -0.3660 358 ILE B CB  
7127  C CG1 . ILE B 358 ? 1.0274 0.4791 2.5437 0.0968  -0.0673 -0.3402 358 ILE B CG1 
7128  C CG2 . ILE B 358 ? 1.0812 0.4907 2.6211 0.0474  -0.0936 -0.3536 358 ILE B CG2 
7129  C CD1 . ILE B 358 ? 1.0029 0.4455 2.5369 0.0864  -0.0597 -0.3029 358 ILE B CD1 
7130  N N   . TYR B 359 ? 1.1125 0.5770 2.5799 0.1518  -0.0744 -0.4212 359 TYR B N   
7131  C CA  . TYR B 359 ? 1.1286 0.5989 2.5799 0.1854  -0.0672 -0.4357 359 TYR B CA  
7132  C C   . TYR B 359 ? 1.1106 0.6390 2.5396 0.1974  -0.0625 -0.4530 359 TYR B C   
7133  O O   . TYR B 359 ? 1.0723 0.6471 2.4997 0.1853  -0.0563 -0.4367 359 TYR B O   
7134  C CB  . TYR B 359 ? 1.0993 0.5751 2.5576 0.1964  -0.0526 -0.4043 359 TYR B CB  
7135  C CG  . TYR B 359 ? 1.1116 0.5955 2.5565 0.2311  -0.0445 -0.4161 359 TYR B CG  
7136  C CD1 . TYR B 359 ? 1.0748 0.6179 2.5041 0.2462  -0.0321 -0.4162 359 TYR B CD1 
7137  C CD2 . TYR B 359 ? 1.1549 0.5887 2.6036 0.2488  -0.0495 -0.4267 359 TYR B CD2 
7138  C CE1 . TYR B 359 ? 1.0793 0.6356 2.4973 0.2769  -0.0243 -0.4267 359 TYR B CE1 
7139  C CE2 . TYR B 359 ? 1.1612 0.6069 2.5985 0.2817  -0.0420 -0.4379 359 TYR B CE2 
7140  C CZ  . TYR B 359 ? 1.1213 0.6305 2.5435 0.2954  -0.0291 -0.4381 359 TYR B CZ  
7141  O OH  . TYR B 359 ? 1.1242 0.6521 2.5362 0.3268  -0.0210 -0.4484 359 TYR B OH  
7142  N N   . SER B 360 ? 1.1475 0.6734 2.5592 0.2224  -0.0653 -0.4855 360 SER B N   
7143  C CA  . SER B 360 ? 1.1332 0.7159 2.5218 0.2385  -0.0593 -0.5015 360 SER B CA  
7144  C C   . SER B 360 ? 1.1735 0.7521 2.5480 0.2731  -0.0557 -0.5250 360 SER B C   
7145  O O   . SER B 360 ? 1.2265 0.7625 2.5984 0.2830  -0.0678 -0.5560 360 SER B O   
7146  C CB  . SER B 360 ? 1.1467 0.7415 2.5265 0.2246  -0.0721 -0.5258 360 SER B CB  
7147  O OG  . SER B 360 ? 1.1543 0.7911 2.5087 0.2461  -0.0697 -0.5516 360 SER B OG  
7148  N N   . LYS B 361 ? 1.1485 0.7706 2.5155 0.2915  -0.0393 -0.5100 361 LYS B N   
7149  C CA  . LYS B 361 ? 1.1814 0.8096 2.5363 0.3253  -0.0338 -0.5291 361 LYS B CA  
7150  C C   . LYS B 361 ? 1.1586 0.8594 2.4924 0.3391  -0.0222 -0.5328 361 LYS B C   
7151  O O   . LYS B 361 ? 1.0954 0.8392 2.4309 0.3314  -0.0097 -0.5029 361 LYS B O   
7152  C CB  . LYS B 361 ? 1.1736 0.7806 2.5430 0.3365  -0.0250 -0.5056 361 LYS B CB  
7153  C CG  . LYS B 361 ? 1.2070 0.8184 2.5674 0.3727  -0.0194 -0.5233 361 LYS B CG  
7154  C CD  . LYS B 361 ? 1.2935 0.8516 2.6504 0.3887  -0.0342 -0.5618 361 LYS B CD  
7155  C CE  . LYS B 361 ? 1.3310 0.8767 2.6865 0.4237  -0.0303 -0.5739 361 LYS B CE  
7156  N NZ  . LYS B 361 ? 1.3192 0.8409 2.6943 0.4228  -0.0246 -0.5407 361 LYS B NZ  
7157  N N   . ASN B 362 ? 1.2043 0.9178 2.5182 0.3596  -0.0269 -0.5700 362 ASN B N   
7158  C CA  . ASN B 362 ? 1.1970 0.9797 2.4895 0.3769  -0.0155 -0.5757 362 ASN B CA  
7159  C C   . ASN B 362 ? 1.1942 0.9930 2.4889 0.4018  -0.0011 -0.5647 362 ASN B C   
7160  O O   . ASN B 362 ? 1.2270 0.9832 2.5289 0.4188  -0.0047 -0.5771 362 ASN B O   
7161  C CB  . ASN B 362 ? 1.2480 1.0423 2.5177 0.3918  -0.0251 -0.6200 362 ASN B CB  
7162  C CG  . ASN B 362 ? 1.2748 1.0478 2.5442 0.3676  -0.0418 -0.6349 362 ASN B CG  
7163  O OD1 . ASN B 362 ? 1.2478 1.0385 2.5234 0.3418  -0.0411 -0.6101 362 ASN B OD1 
7164  N ND2 . ASN B 362 ? 1.3340 1.0690 2.5972 0.3753  -0.0573 -0.6754 362 ASN B ND2 
7165  N N   . ILE B 363 ? 1.1511 1.0113 2.4407 0.4035  0.0145  -0.5409 363 ILE B N   
7166  C CA  . ILE B 363 ? 1.1336 1.0135 2.4298 0.4208  0.0289  -0.5229 363 ILE B CA  
7167  C C   . ILE B 363 ? 1.1712 1.1007 2.4473 0.4513  0.0366  -0.5462 363 ILE B C   
7168  O O   . ILE B 363 ? 1.1771 1.1670 2.4384 0.4501  0.0446  -0.5413 363 ILE B O   
7169  C CB  . ILE B 363 ? 1.0536 0.9640 2.3608 0.3999  0.0403  -0.4799 363 ILE B CB  
7170  C CG1 . ILE B 363 ? 1.0336 0.8949 2.3604 0.3730  0.0325  -0.4603 363 ILE B CG1 
7171  C CG2 . ILE B 363 ? 1.0287 0.9693 2.3427 0.4145  0.0557  -0.4594 363 ILE B CG2 
7172  C CD1 . ILE B 363 ? 1.0484 0.8506 2.3922 0.3788  0.0277  -0.4596 363 ILE B CD1 
7173  N N   . THR B 364 ? 1.2112 1.1166 2.4867 0.4791  0.0342  -0.5710 364 THR B N   
7174  C CA  . THR B 364 ? 1.2483 1.2003 2.5045 0.5105  0.0404  -0.5978 364 THR B CA  
7175  C C   . THR B 364 ? 1.2154 1.2182 2.4767 0.5245  0.0587  -0.5739 364 THR B C   
7176  O O   . THR B 364 ? 1.2270 1.2852 2.4732 0.5472  0.0677  -0.5877 364 THR B O   
7177  C CB  . THR B 364 ? 1.3264 1.2328 2.5783 0.5372  0.0288  -0.6399 364 THR B CB  
7178  O OG1 . THR B 364 ? 1.3430 1.1951 2.6166 0.5423  0.0267  -0.6282 364 THR B OG1 
7179  C CG2 . THR B 364 ? 1.3681 1.2346 2.6109 0.5271  0.0104  -0.6717 364 THR B CG2 
7180  N N   . SER B 365 ? 1.1755 1.1608 2.4584 0.5119  0.0639  -0.5396 365 SER B N   
7181  C CA  . SER B 365 ? 1.1324 1.1662 2.4223 0.5212  0.0803  -0.5152 365 SER B CA  
7182  C C   . SER B 365 ? 1.0736 1.0984 2.3829 0.4931  0.0845  -0.4734 365 SER B C   
7183  O O   . SER B 365 ? 1.0736 1.0444 2.3939 0.4737  0.0745  -0.4660 365 SER B O   
7184  C CB  . SER B 365 ? 1.1628 1.1845 2.4587 0.5534  0.0820  -0.5300 365 SER B CB  
7185  O OG  . SER B 365 ? 1.1814 1.1298 2.4946 0.5503  0.0715  -0.5273 365 SER B OG  
7186  N N   . GLU B 366 ? 1.0250 1.1052 2.3380 0.4905  0.0992  -0.4471 366 GLU B N   
7187  C CA  . GLU B 366 ? 0.9690 1.0501 2.2983 0.4643  0.1041  -0.4088 366 GLU B CA  
7188  C C   . GLU B 366 ? 0.9502 1.0060 2.2999 0.4711  0.1064  -0.3939 366 GLU B C   
7189  O O   . GLU B 366 ? 0.9687 1.0124 2.3197 0.4970  0.1053  -0.4113 366 GLU B O   
7190  C CB  . GLU B 366 ? 0.9379 1.0886 2.2615 0.4560  0.1174  -0.3878 366 GLU B CB  
7191  C CG  . GLU B 366 ? 0.9354 1.1422 2.2577 0.4786  0.1308  -0.3875 366 GLU B CG  
7192  C CD  . GLU B 366 ? 0.9091 1.1857 2.2231 0.4698  0.1429  -0.3695 366 GLU B CD  
7193  O OE1 . GLU B 366 ? 0.8711 1.1532 2.1947 0.4446  0.1461  -0.3391 366 GLU B OE1 
7194  O OE2 . GLU B 366 ? 0.9232 1.2488 2.2211 0.4880  0.1490  -0.3855 366 GLU B OE2 
7195  N N   . GLY B 367 ? 0.9057 0.9534 2.2710 0.4481  0.1088  -0.3621 367 GLY B N   
7196  C CA  . GLY B 367 ? 0.8915 0.9224 2.2758 0.4515  0.1115  -0.3442 367 GLY B CA  
7197  C C   . GLY B 367 ? 0.9084 0.8684 2.3033 0.4434  0.0991  -0.3441 367 GLY B C   
7198  O O   . GLY B 367 ? 0.9046 0.8349 2.2976 0.4234  0.0906  -0.3450 367 GLY B O   
7199  N N   . TYR B 368 ? 0.9290 0.8647 2.3356 0.4592  0.0980  -0.3419 368 TYR B N   
7200  C CA  . TYR B 368 ? 0.9472 0.8186 2.3658 0.4514  0.0875  -0.3360 368 TYR B CA  
7201  C C   . TYR B 368 ? 1.0044 0.8270 2.4141 0.4594  0.0743  -0.3665 368 TYR B C   
7202  O O   . TYR B 368 ? 1.0299 0.8614 2.4282 0.4841  0.0735  -0.3943 368 TYR B O   
7203  C CB  . TYR B 368 ? 0.9494 0.8111 2.3824 0.4675  0.0899  -0.3235 368 TYR B CB  
7204  C CG  . TYR B 368 ? 0.9706 0.7675 2.4160 0.4599  0.0794  -0.3137 368 TYR B CG  
7205  C CD1 . TYR B 368 ? 1.0218 0.7628 2.4655 0.4734  0.0675  -0.3350 368 TYR B CD1 
7206  C CD2 . TYR B 368 ? 0.9362 0.7281 2.3952 0.4396  0.0813  -0.2829 368 TYR B CD2 
7207  C CE1 . TYR B 368 ? 1.0386 0.7206 2.4943 0.4652  0.0580  -0.3234 368 TYR B CE1 
7208  C CE2 . TYR B 368 ? 0.9523 0.6897 2.4222 0.4324  0.0725  -0.2719 368 TYR B CE2 
7209  C CZ  . TYR B 368 ? 1.0028 0.6848 2.4713 0.4445  0.0609  -0.2908 368 TYR B CZ  
7210  O OH  . TYR B 368 ? 1.0169 0.6452 2.4966 0.4360  0.0522  -0.2772 368 TYR B OH  
7211  N N   . MET B 369 ? 1.0184 0.7904 2.4343 0.4379  0.0638  -0.3615 369 MET B N   
7212  C CA  . MET B 369 ? 1.0784 0.7989 2.4888 0.4401  0.0496  -0.3884 369 MET B CA  
7213  C C   . MET B 369 ? 1.0751 0.7365 2.5011 0.4201  0.0401  -0.3716 369 MET B C   
7214  O O   . MET B 369 ? 1.0555 0.7224 2.4880 0.3928  0.0415  -0.3492 369 MET B O   
7215  C CB  . MET B 369 ? 1.1035 0.8455 2.4981 0.4280  0.0469  -0.4058 369 MET B CB  
7216  C CG  . MET B 369 ? 1.1857 0.8763 2.5749 0.4254  0.0309  -0.4347 369 MET B CG  
7217  S SD  . MET B 369 ? 1.2194 0.8743 2.6182 0.3852  0.0205  -0.4201 369 MET B SD  
7218  C CE  . MET B 369 ? 1.1389 0.8634 2.5279 0.3674  0.0307  -0.4057 369 MET B CE  
7219  N N   . ALA B 370 ? 1.1054 0.7123 2.5377 0.4346  0.0308  -0.3818 370 ALA B N   
7220  C CA  . ALA B 370 ? 1.1080 0.6572 2.5557 0.4174  0.0217  -0.3645 370 ALA B CA  
7221  C C   . ALA B 370 ? 1.1440 0.6385 2.5894 0.4083  0.0058  -0.3885 370 ALA B C   
7222  O O   . ALA B 370 ? 1.1824 0.6733 2.6150 0.4254  0.0006  -0.4224 370 ALA B O   
7223  C CB  . ALA B 370 ? 1.1256 0.6510 2.5842 0.4383  0.0222  -0.3531 370 ALA B CB  
7224  N N   . ASP B 371 ? 1.1255 0.5789 2.5837 0.3814  -0.0021 -0.3711 371 ASP B N   
7225  C CA  . ASP B 371 ? 1.1570 0.5599 2.6162 0.3664  -0.0176 -0.3900 371 ASP B CA  
7226  C C   . ASP B 371 ? 1.1522 0.5169 2.6297 0.3374  -0.0231 -0.3610 371 ASP B C   
7227  O O   . ASP B 371 ? 1.1114 0.4856 2.5989 0.3343  -0.0153 -0.3294 371 ASP B O   
7228  C CB  . ASP B 371 ? 1.1402 0.5781 2.5850 0.3557  -0.0185 -0.4108 371 ASP B CB  
7229  C CG  . ASP B 371 ? 1.1940 0.5985 2.6292 0.3617  -0.0328 -0.4510 371 ASP B CG  
7230  O OD1 . ASP B 371 ? 1.2339 0.5784 2.6797 0.3484  -0.0466 -0.4552 371 ASP B OD1 
7231  O OD2 . ASP B 371 ? 1.1951 0.6361 2.6124 0.3782  -0.0301 -0.4773 371 ASP B OD2 
7232  N N   . GLU B 372 ? 1.1952 0.5196 2.6767 0.3160  -0.0367 -0.3724 372 GLU B N   
7233  C CA  . GLU B 372 ? 1.2118 0.5017 2.7107 0.2854  -0.0430 -0.3472 372 GLU B CA  
7234  C C   . GLU B 372 ? 1.2050 0.5095 2.7039 0.2546  -0.0480 -0.3521 372 GLU B C   
7235  O O   . GLU B 372 ? 1.2341 0.5477 2.7205 0.2573  -0.0537 -0.3831 372 GLU B O   
7236  C CB  . GLU B 372 ? 1.2880 0.5004 2.7975 0.2870  -0.0581 -0.3547 372 GLU B CB  
7237  C CG  . GLU B 372 ? 1.3141 0.5000 2.8305 0.3102  -0.0555 -0.3386 372 GLU B CG  
7238  C CD  . GLU B 372 ? 1.4008 0.5060 2.9281 0.3114  -0.0715 -0.3451 372 GLU B CD  
7239  O OE1 . GLU B 372 ? 1.4444 0.5128 2.9747 0.2926  -0.0849 -0.3629 372 GLU B OE1 
7240  O OE2 . GLU B 372 ? 1.4401 0.5182 2.9733 0.3315  -0.0712 -0.3323 372 GLU B OE2 
7241  N N   . LEU B 373 ? 1.1698 0.4778 2.6826 0.2258  -0.0466 -0.3221 373 LEU B N   
7242  C CA  . LEU B 373 ? 1.1761 0.4800 2.6946 0.1948  -0.0554 -0.3257 373 LEU B CA  
7243  C C   . LEU B 373 ? 1.2348 0.4730 2.7710 0.1773  -0.0687 -0.3183 373 LEU B C   
7244  O O   . LEU B 373 ? 1.2575 0.4627 2.8025 0.1855  -0.0680 -0.3001 373 LEU B O   
7245  C CB  . LEU B 373 ? 1.1180 0.4733 2.6411 0.1735  -0.0455 -0.2989 373 LEU B CB  
7246  C CG  . LEU B 373 ? 1.0665 0.4870 2.5751 0.1867  -0.0318 -0.2990 373 LEU B CG  
7247  C CD1 . LEU B 373 ? 1.0070 0.4661 2.5241 0.1659  -0.0232 -0.2688 373 LEU B CD1 
7248  C CD2 . LEU B 373 ? 1.0747 0.5189 2.5662 0.1929  -0.0356 -0.3314 373 LEU B CD2 
7249  N N   . THR B 374 ? 1.2619 0.4829 2.8035 0.1524  -0.0810 -0.3313 374 THR B N   
7250  C CA  . THR B 374 ? 1.3074 0.4743 2.8689 0.1273  -0.0929 -0.3186 374 THR B CA  
7251  C C   . THR B 374 ? 1.2832 0.4802 2.8551 0.0917  -0.0937 -0.3044 374 THR B C   
7252  O O   . THR B 374 ? 1.2623 0.4850 2.8273 0.0827  -0.0983 -0.3260 374 THR B O   
7253  C CB  . THR B 374 ? 1.3822 0.4855 2.9437 0.1327  -0.1106 -0.3521 374 THR B CB  
7254  O OG1 . THR B 374 ? 1.4028 0.4896 2.9531 0.1699  -0.1077 -0.3659 374 THR B OG1 
7255  C CG2 . THR B 374 ? 1.4249 0.4646 3.0084 0.1079  -0.1234 -0.3368 374 THR B CG2 
7256  N N   . ILE B 375 ? 1.2812 0.4771 2.8698 0.0726  -0.0892 -0.2672 375 ILE B N   
7257  C CA  . ILE B 375 ? 1.2701 0.4949 2.8716 0.0394  -0.0889 -0.2490 375 ILE B CA  
7258  C C   . ILE B 375 ? 1.3266 0.4982 2.9495 0.0124  -0.1012 -0.2358 375 ILE B C   
7259  O O   . ILE B 375 ? 1.3762 0.4925 3.0044 0.0207  -0.1067 -0.2317 375 ILE B O   
7260  C CB  . ILE B 375 ? 1.2228 0.5023 2.8251 0.0394  -0.0718 -0.2163 375 ILE B CB  
7261  C CG1 . ILE B 375 ? 1.2328 0.4927 2.8401 0.0519  -0.0644 -0.1881 375 ILE B CG1 
7262  C CG2 . ILE B 375 ? 1.1680 0.5043 2.7514 0.0582  -0.0614 -0.2297 375 ILE B CG2 
7263  C CD1 . ILE B 375 ? 1.1700 0.4815 2.7796 0.0491  -0.0490 -0.1565 375 ILE B CD1 
7264  N N   . ASP B 376 ? 1.3304 0.5202 2.9666 -0.0200 -0.1056 -0.2283 376 ASP B N   
7265  C CA  . ASP B 376 ? 1.3825 0.5307 3.0416 -0.0504 -0.1161 -0.2113 376 ASP B CA  
7266  C C   . ASP B 376 ? 1.3455 0.5401 3.0182 -0.0735 -0.1059 -0.1743 376 ASP B C   
7267  O O   . ASP B 376 ? 1.3558 0.5740 3.0397 -0.1011 -0.1105 -0.1737 376 ASP B O   
7268  C CB  . ASP B 376 ? 1.4367 0.5537 3.1011 -0.0685 -0.1347 -0.2427 376 ASP B CB  
7269  C CG  . ASP B 376 ? 1.5075 0.5730 3.1969 -0.1011 -0.1478 -0.2281 376 ASP B CG  
7270  O OD1 . ASP B 376 ? 1.5035 0.5811 3.2085 -0.1196 -0.1410 -0.1894 376 ASP B OD1 
7271  O OD2 . ASP B 376 ? 1.5684 0.5806 3.2619 -0.1076 -0.1651 -0.2549 376 ASP B OD2 
7272  N N   . PRO B 377 ? 1.3081 0.5201 2.9802 -0.0626 -0.0920 -0.1433 377 PRO B N   
7273  C CA  . PRO B 377 ? 1.2563 0.5188 2.9386 -0.0804 -0.0811 -0.1109 377 PRO B CA  
7274  C C   . PRO B 377 ? 1.2876 0.5252 2.9936 -0.1126 -0.0872 -0.0832 377 PRO B C   
7275  O O   . PRO B 377 ? 1.3194 0.5044 3.0321 -0.1115 -0.0919 -0.0699 377 PRO B O   
7276  C CB  . PRO B 377 ? 1.2155 0.4982 2.8864 -0.0534 -0.0661 -0.0936 377 PRO B CB  
7277  C CG  . PRO B 377 ? 1.2624 0.4833 2.9298 -0.0341 -0.0722 -0.0990 377 PRO B CG  
7278  C CD  . PRO B 377 ? 1.3114 0.4962 2.9739 -0.0325 -0.0868 -0.1382 377 PRO B CD  
7279  N N   . VAL B 378 ? 1.2610 0.5388 2.9802 -0.1407 -0.0870 -0.0742 378 VAL B N   
7280  C CA  . VAL B 378 ? 1.2794 0.5474 3.0226 -0.1744 -0.0911 -0.0459 378 VAL B CA  
7281  C C   . VAL B 378 ? 1.2412 0.5424 2.9874 -0.1722 -0.0758 -0.0065 378 VAL B C   
7282  O O   . VAL B 378 ? 1.1798 0.5341 2.9144 -0.1561 -0.0625 -0.0038 378 VAL B O   
7283  C CB  . VAL B 378 ? 1.2621 0.5631 3.0190 -0.2049 -0.0978 -0.0541 378 VAL B CB  
7284  C CG1 . VAL B 378 ? 1.2856 0.5769 3.0694 -0.2423 -0.1029 -0.0252 378 VAL B CG1 
7285  C CG2 . VAL B 378 ? 1.2902 0.5671 3.0408 -0.2043 -0.1127 -0.0961 378 VAL B CG2 
7286  N N   . GLY B 379 ? 1.2626 0.5297 3.0236 -0.1876 -0.0783 0.0233  379 GLY B N   
7287  C CA  . GLY B 379 ? 1.2281 0.5232 2.9936 -0.1891 -0.0655 0.0629  379 GLY B CA  
7288  C C   . GLY B 379 ? 1.1677 0.4966 2.9129 -0.1552 -0.0510 0.0637  379 GLY B C   
7289  O O   . GLY B 379 ? 1.1746 0.4689 2.9076 -0.1292 -0.0512 0.0574  379 GLY B O   
7290  N N   . ILE B 380 ? 1.0981 0.4952 2.8416 -0.1565 -0.0387 0.0727  380 ILE B N   
7291  C CA  . ILE B 380 ? 1.0424 0.4781 2.7673 -0.1275 -0.0265 0.0651  380 ILE B CA  
7292  C C   . ILE B 380 ? 1.0006 0.4778 2.7201 -0.1275 -0.0259 0.0391  380 ILE B C   
7293  O O   . ILE B 380 ? 0.9771 0.4951 2.7077 -0.1479 -0.0243 0.0456  380 ILE B O   
7294  C CB  . ILE B 380 ? 1.0075 0.4846 2.7329 -0.1243 -0.0127 0.0977  380 ILE B CB  
7295  C CG1 . ILE B 380 ? 1.0452 0.4863 2.7786 -0.1299 -0.0142 0.1290  380 ILE B CG1 
7296  C CG2 . ILE B 380 ? 0.9611 0.4682 2.6674 -0.0930 -0.0019 0.0879  380 ILE B CG2 
7297  C CD1 . ILE B 380 ? 1.0096 0.4951 2.7429 -0.1278 -0.0011 0.1613  380 ILE B CD1 
7298  N N   . GLU B 381 ? 0.9898 0.4584 2.6919 -0.1033 -0.0269 0.0105  381 GLU B N   
7299  C CA  . GLU B 381 ? 0.9542 0.4533 2.6490 -0.1010 -0.0283 -0.0163 381 GLU B CA  
7300  C C   . GLU B 381 ? 0.9152 0.4424 2.5905 -0.0710 -0.0178 -0.0263 381 GLU B C   
7301  O O   . GLU B 381 ? 0.9292 0.4295 2.5916 -0.0480 -0.0177 -0.0377 381 GLU B O   
7302  C CB  . GLU B 381 ? 0.9938 0.4485 2.6881 -0.1060 -0.0435 -0.0450 381 GLU B CB  
7303  C CG  . GLU B 381 ? 0.9699 0.4568 2.6596 -0.1102 -0.0477 -0.0707 381 GLU B CG  
7304  C CD  . GLU B 381 ? 1.0136 0.4596 2.7015 -0.1147 -0.0634 -0.1016 381 GLU B CD  
7305  O OE1 . GLU B 381 ? 1.0540 0.4628 2.7578 -0.1376 -0.0746 -0.0983 381 GLU B OE1 
7306  O OE2 . GLU B 381 ? 1.0022 0.4548 2.6726 -0.0957 -0.0645 -0.1290 381 GLU B OE2 
7307  N N   . ASP B 382 ? 0.8616 0.4444 2.5358 -0.0716 -0.0091 -0.0217 382 ASP B N   
7308  C CA  . ASP B 382 ? 0.8212 0.4329 2.4787 -0.0476 -0.0009 -0.0339 382 ASP B CA  
7309  C C   . ASP B 382 ? 0.8265 0.4323 2.4739 -0.0424 -0.0088 -0.0653 382 ASP B C   
7310  O O   . ASP B 382 ? 0.8385 0.4432 2.4937 -0.0608 -0.0182 -0.0755 382 ASP B O   
7311  C CB  . ASP B 382 ? 0.7721 0.4405 2.4326 -0.0498 0.0095  -0.0196 382 ASP B CB  
7312  C CG  . ASP B 382 ? 0.7615 0.4614 2.4335 -0.0710 0.0057  -0.0213 382 ASP B CG  
7313  O OD1 . ASP B 382 ? 0.7878 0.4779 2.4759 -0.0944 0.0000  -0.0104 382 ASP B OD1 
7314  O OD2 . ASP B 382 ? 0.7308 0.4647 2.3960 -0.0639 0.0082  -0.0330 382 ASP B OD2 
7315  N N   . MET B 383 ? 0.8184 0.4237 2.4486 -0.0172 -0.0049 -0.0802 383 MET B N   
7316  C CA  . MET B 383 ? 0.8258 0.4273 2.4431 -0.0083 -0.0112 -0.1098 383 MET B CA  
7317  C C   . MET B 383 ? 0.7738 0.4093 2.3753 0.0145  -0.0010 -0.1150 383 MET B C   
7318  O O   . MET B 383 ? 0.7540 0.3907 2.3512 0.0300  0.0077  -0.1040 383 MET B O   
7319  C CB  . MET B 383 ? 0.8883 0.4341 2.5023 -0.0019 -0.0211 -0.1264 383 MET B CB  
7320  C CG  . MET B 383 ? 0.9367 0.4443 2.5685 -0.0255 -0.0308 -0.1164 383 MET B CG  
7321  S SD  . MET B 383 ? 1.0241 0.4583 2.6545 -0.0187 -0.0438 -0.1345 383 MET B SD  
7322  C CE  . MET B 383 ? 1.0378 0.4749 2.6522 -0.0093 -0.0527 -0.1770 383 MET B CE  
7323  N N   . GLU B 384 ? 0.7478 0.4142 2.3423 0.0142  -0.0023 -0.1291 384 GLU B N   
7324  C CA  . GLU B 384 ? 0.7166 0.4110 2.2951 0.0343  0.0050  -0.1375 384 GLU B CA  
7325  C C   . GLU B 384 ? 0.7388 0.4167 2.3029 0.0451  -0.0024 -0.1661 384 GLU B C   
7326  O O   . GLU B 384 ? 0.7464 0.4298 2.3091 0.0352  -0.0112 -0.1817 384 GLU B O   
7327  C CB  . GLU B 384 ? 0.6927 0.4338 2.2725 0.0273  0.0081  -0.1328 384 GLU B CB  
7328  C CG  . GLU B 384 ? 0.6672 0.4386 2.2316 0.0457  0.0154  -0.1385 384 GLU B CG  
7329  C CD  . GLU B 384 ? 0.6445 0.4566 2.2112 0.0382  0.0160  -0.1345 384 GLU B CD  
7330  O OE1 . GLU B 384 ? 0.6428 0.4580 2.2217 0.0198  0.0094  -0.1323 384 GLU B OE1 
7331  O OE2 . GLU B 384 ? 0.6483 0.4887 2.2064 0.0496  0.0226  -0.1323 384 GLU B OE2 
7332  N N   . LEU B 385 ? 0.7488 0.4090 2.3025 0.0660  0.0011  -0.1731 385 LEU B N   
7333  C CA  . LEU B 385 ? 0.7775 0.4232 2.3164 0.0800  -0.0049 -0.2012 385 LEU B CA  
7334  C C   . LEU B 385 ? 0.7360 0.4268 2.2599 0.0919  0.0015  -0.2082 385 LEU B C   
7335  O O   . LEU B 385 ? 0.6929 0.4064 2.2128 0.1042  0.0127  -0.1958 385 LEU B O   
7336  C CB  . LEU B 385 ? 0.8058 0.4160 2.3406 0.0992  -0.0039 -0.2061 385 LEU B CB  
7337  C CG  . LEU B 385 ? 0.8357 0.3994 2.3851 0.0910  -0.0087 -0.1938 385 LEU B CG  
7338  C CD1 . LEU B 385 ? 0.8471 0.3905 2.3911 0.1155  -0.0038 -0.1932 385 LEU B CD1 
7339  C CD2 . LEU B 385 ? 0.8850 0.4057 2.4415 0.0756  -0.0239 -0.2090 385 LEU B CD2 
7340  N N   . ALA B 386 ? 0.7454 0.4480 2.2608 0.0880  -0.0062 -0.2282 386 ALA B N   
7341  C CA  . ALA B 386 ? 0.7242 0.4701 2.2250 0.0973  -0.0016 -0.2339 386 ALA B CA  
7342  C C   . ALA B 386 ? 0.7457 0.4906 2.2274 0.1197  -0.0009 -0.2561 386 ALA B C   
7343  O O   . ALA B 386 ? 0.7853 0.5155 2.2593 0.1208  -0.0110 -0.2813 386 ALA B O   
7344  C CB  . ALA B 386 ? 0.7303 0.4951 2.2323 0.0809  -0.0106 -0.2417 386 ALA B CB  
7345  N N   . PHE B 387 ? 0.7236 0.4888 2.1979 0.1371  0.0110  -0.2477 387 PHE B N   
7346  C CA  . PHE B 387 ? 0.7494 0.5202 2.2065 0.1598  0.0136  -0.2665 387 PHE B CA  
7347  C C   . PHE B 387 ? 0.7413 0.5568 2.1821 0.1643  0.0154  -0.2745 387 PHE B C   
7348  O O   . PHE B 387 ? 0.7073 0.5552 2.1499 0.1579  0.0213  -0.2563 387 PHE B O   
7349  C CB  . PHE B 387 ? 0.7333 0.5063 2.1916 0.1762  0.0253  -0.2533 387 PHE B CB  
7350  C CG  . PHE B 387 ? 0.7573 0.4848 2.2251 0.1814  0.0227  -0.2533 387 PHE B CG  
7351  C CD1 . PHE B 387 ? 0.7537 0.4566 2.2390 0.1653  0.0206  -0.2345 387 PHE B CD1 
7352  C CD2 . PHE B 387 ? 0.7806 0.4921 2.2400 0.2034  0.0226  -0.2708 387 PHE B CD2 
7353  C CE1 . PHE B 387 ? 0.7755 0.4370 2.2691 0.1702  0.0180  -0.2317 387 PHE B CE1 
7354  C CE2 . PHE B 387 ? 0.8049 0.4743 2.2734 0.2095  0.0200  -0.2684 387 PHE B CE2 
7355  C CZ  . PHE B 387 ? 0.8003 0.4437 2.2857 0.1925  0.0174  -0.2483 387 PHE B CZ  
7356  N N   . GLU B 388 ? 0.7815 0.5987 2.2058 0.1770  0.0104  -0.3016 388 GLU B N   
7357  C CA  . GLU B 388 ? 0.7910 0.6502 2.1979 0.1810  0.0102  -0.3115 388 GLU B CA  
7358  C C   . GLU B 388 ? 0.8180 0.6938 2.2063 0.2056  0.0156  -0.3286 388 GLU B C   
7359  O O   . GLU B 388 ? 0.8535 0.7063 2.2342 0.2162  0.0086  -0.3556 388 GLU B O   
7360  C CB  . GLU B 388 ? 0.8235 0.6758 2.2277 0.1677  -0.0044 -0.3312 388 GLU B CB  
7361  C CG  . GLU B 388 ? 0.8092 0.6569 2.2315 0.1429  -0.0094 -0.3140 388 GLU B CG  
7362  C CD  . GLU B 388 ? 0.8326 0.6792 2.2540 0.1282  -0.0242 -0.3324 388 GLU B CD  
7363  O OE1 . GLU B 388 ? 0.8643 0.7121 2.2699 0.1369  -0.0316 -0.3607 388 GLU B OE1 
7364  O OE2 . GLU B 388 ? 0.8181 0.6657 2.2549 0.1081  -0.0284 -0.3190 388 GLU B OE2 
7365  N N   . PHE B 389 ? 0.8031 0.7207 2.1842 0.2142  0.0277  -0.3133 389 PHE B N   
7366  C CA  . PHE B 389 ? 0.8279 0.7702 2.1930 0.2369  0.0353  -0.3246 389 PHE B CA  
7367  C C   . PHE B 389 ? 0.8397 0.8259 2.1843 0.2403  0.0340  -0.3355 389 PHE B C   
7368  O O   . PHE B 389 ? 0.8063 0.8222 2.1504 0.2294  0.0363  -0.3174 389 PHE B O   
7369  C CB  . PHE B 389 ? 0.7956 0.7566 2.1675 0.2439  0.0498  -0.3000 389 PHE B CB  
7370  C CG  . PHE B 389 ? 0.7895 0.7128 2.1799 0.2430  0.0517  -0.2887 389 PHE B CG  
7371  C CD1 . PHE B 389 ? 0.7682 0.6717 2.1761 0.2240  0.0498  -0.2686 389 PHE B CD1 
7372  C CD2 . PHE B 389 ? 0.8135 0.7240 2.2034 0.2623  0.0555  -0.2978 389 PHE B CD2 
7373  C CE1 . PHE B 389 ? 0.7617 0.6340 2.1850 0.2234  0.0515  -0.2573 389 PHE B CE1 
7374  C CE2 . PHE B 389 ? 0.8084 0.6864 2.2146 0.2621  0.0567  -0.2859 389 PHE B CE2 
7375  C CZ  . PHE B 389 ? 0.7786 0.6381 2.2009 0.2423  0.0548  -0.2652 389 PHE B CZ  
7376  N N   . TYR B 390 ? 0.8854 0.8761 2.2129 0.2573  0.0304  -0.3653 390 TYR B N   
7377  C CA  . TYR B 390 ? 0.9024 0.9348 2.2077 0.2627  0.0279  -0.3804 390 TYR B CA  
7378  C C   . TYR B 390 ? 0.9058 0.9786 2.1950 0.2857  0.0397  -0.3846 390 TYR B C   
7379  O O   . TYR B 390 ? 0.9026 0.9635 2.1970 0.2997  0.0466  -0.3855 390 TYR B O   
7380  C CB  . TYR B 390 ? 0.9436 0.9500 2.2416 0.2615  0.0118  -0.4152 390 TYR B CB  
7381  C CG  . TYR B 390 ? 0.9334 0.9079 2.2470 0.2368  -0.0005 -0.4117 390 TYR B CG  
7382  C CD1 . TYR B 390 ? 0.9332 0.8545 2.2678 0.2272  -0.0047 -0.4074 390 TYR B CD1 
7383  C CD2 . TYR B 390 ? 0.9287 0.9292 2.2361 0.2233  -0.0081 -0.4121 390 TYR B CD2 
7384  C CE1 . TYR B 390 ? 0.9345 0.8310 2.2841 0.2038  -0.0153 -0.4031 390 TYR B CE1 
7385  C CE2 . TYR B 390 ? 0.9229 0.8995 2.2459 0.2007  -0.0191 -0.4089 390 TYR B CE2 
7386  C CZ  . TYR B 390 ? 0.9269 0.8522 2.2713 0.1904  -0.0223 -0.4041 390 TYR B CZ  
7387  O OH  . TYR B 390 ? 0.9191 0.8249 2.2798 0.1673  -0.0325 -0.3996 390 TYR B OH  
7388  N N   . ASP B 391 ? 0.9083 1.0318 2.1782 0.2891  0.0418  -0.3860 391 ASP B N   
7389  C CA  . ASP B 391 ? 0.9105 1.0824 2.1625 0.3091  0.0526  -0.3898 391 ASP B CA  
7390  C C   . ASP B 391 ? 0.9625 1.1489 2.1909 0.3231  0.0441  -0.4277 391 ASP B C   
7391  O O   . ASP B 391 ? 0.9784 1.1309 2.2070 0.3171  0.0297  -0.4510 391 ASP B O   
7392  C CB  . ASP B 391 ? 0.8741 1.0948 2.1235 0.3015  0.0631  -0.3565 391 ASP B CB  
7393  C CG  . ASP B 391 ? 0.8637 1.1058 2.1059 0.2862  0.0562  -0.3472 391 ASP B CG  
7394  O OD1 . ASP B 391 ? 0.8961 1.1301 2.1288 0.2839  0.0433  -0.3715 391 ASP B OD1 
7395  O OD2 . ASP B 391 ? 0.8235 1.0905 2.0703 0.2767  0.0634  -0.3155 391 ASP B OD2 
7396  N N   . SER B 392 ? 0.9964 1.2336 2.2053 0.3421  0.0531  -0.4347 392 SER B N   
7397  C CA  . SER B 392 ? 1.0470 1.3147 2.2296 0.3542  0.0464  -0.4661 392 SER B CA  
7398  C C   . SER B 392 ? 1.0526 1.3564 2.2254 0.3384  0.0430  -0.4501 392 SER B C   
7399  O O   . SER B 392 ? 1.0399 1.3807 2.2134 0.3329  0.0539  -0.4170 392 SER B O   
7400  C CB  . SER B 392 ? 1.0545 1.3692 2.2198 0.3799  0.0581  -0.4769 392 SER B CB  
7401  O OG  . SER B 392 ? 1.0157 1.3813 2.1804 0.3766  0.0731  -0.4411 392 SER B OG  
7402  N N   . ASP B 393 ? 1.0916 1.3843 2.2561 0.3313  0.0273  -0.4736 393 ASP B N   
7403  C CA  . ASP B 393 ? 1.0891 1.4003 2.2510 0.3125  0.0199  -0.4592 393 ASP B CA  
7404  C C   . ASP B 393 ? 1.0869 1.3413 2.2698 0.2922  0.0060  -0.4633 393 ASP B C   
7405  O O   . ASP B 393 ? 1.0946 1.3555 2.2738 0.2794  -0.0060 -0.4688 393 ASP B O   
7406  C CB  . ASP B 393 ? 1.0503 1.3995 2.2157 0.3036  0.0317  -0.4151 393 ASP B CB  
7407  C CG  . ASP B 393 ? 1.0566 1.4741 2.1985 0.3173  0.0428  -0.4060 393 ASP B CG  
7408  O OD1 . ASP B 393 ? 1.0877 1.5410 2.2052 0.3256  0.0366  -0.4278 393 ASP B OD1 
7409  O OD2 . ASP B 393 ? 1.0275 1.4645 2.1759 0.3185  0.0574  -0.3762 393 ASP B OD2 
7410  N N   . ASN B 394 ? 1.0780 1.2798 2.2830 0.2891  0.0076  -0.4596 394 ASN B N   
7411  C CA  . ASN B 394 ? 1.0688 1.2144 2.2947 0.2708  -0.0046 -0.4639 394 ASN B CA  
7412  C C   . ASN B 394 ? 1.0341 1.1845 2.2763 0.2489  -0.0033 -0.4281 394 ASN B C   
7413  O O   . ASN B 394 ? 1.0390 1.1737 2.2899 0.2312  -0.0154 -0.4308 394 ASN B O   
7414  C CB  . ASN B 394 ? 1.1119 1.2413 2.3281 0.2696  -0.0223 -0.5036 394 ASN B CB  
7415  C CG  . ASN B 394 ? 1.1185 1.1837 2.3575 0.2530  -0.0343 -0.5114 394 ASN B CG  
7416  O OD1 . ASN B 394 ? 1.1070 1.1314 2.3636 0.2535  -0.0293 -0.5016 394 ASN B OD1 
7417  N ND2 . ASN B 394 ? 1.1370 1.1947 2.3766 0.2374  -0.0501 -0.5276 394 ASN B ND2 
7418  N N   . LYS B 395 ? 0.9906 1.1637 2.2375 0.2508  0.0115  -0.3954 395 LYS B N   
7419  C CA  . LYS B 395 ? 0.9527 1.1284 2.2159 0.2334  0.0146  -0.3604 395 LYS B CA  
7420  C C   . LYS B 395 ? 0.9052 1.0378 2.1930 0.2276  0.0202  -0.3446 395 LYS B C   
7421  O O   . LYS B 395 ? 0.8843 1.0062 2.1730 0.2409  0.0282  -0.3479 395 LYS B O   
7422  C CB  . LYS B 395 ? 0.9549 1.1844 2.2065 0.2383  0.0258  -0.3352 395 LYS B CB  
7423  C CG  . LYS B 395 ? 1.0040 1.2789 2.2315 0.2420  0.0194  -0.3465 395 LYS B CG  
7424  C CD  . LYS B 395 ? 1.0035 1.3264 2.2237 0.2399  0.0266  -0.3148 395 LYS B CD  
7425  C CE  . LYS B 395 ? 1.0351 1.3909 2.2393 0.2360  0.0155  -0.3217 395 LYS B CE  
7426  N NZ  . LYS B 395 ? 1.0881 1.4590 2.2695 0.2486  0.0081  -0.3596 395 LYS B NZ  
7427  N N   . ILE B 396 ? 0.8757 0.9862 2.1830 0.2085  0.0155  -0.3283 396 ILE B N   
7428  C CA  . ILE B 396 ? 0.8409 0.9178 2.1709 0.2018  0.0214  -0.3094 396 ILE B CA  
7429  C C   . ILE B 396 ? 0.7916 0.8966 2.1238 0.2050  0.0354  -0.2792 396 ILE B C   
7430  O O   . ILE B 396 ? 0.7771 0.9117 2.1068 0.1986  0.0363  -0.2619 396 ILE B O   
7431  C CB  . ILE B 396 ? 0.8370 0.8860 2.1868 0.1808  0.0124  -0.3020 396 ILE B CB  
7432  C CG1 . ILE B 396 ? 0.8908 0.9075 2.2412 0.1753  -0.0020 -0.3315 396 ILE B CG1 
7433  C CG2 . ILE B 396 ? 0.8081 0.8318 2.1793 0.1750  0.0202  -0.2787 396 ILE B CG2 
7434  C CD1 . ILE B 396 ? 0.8849 0.8713 2.2572 0.1538  -0.0105 -0.3250 396 ILE B CD1 
7435  N N   . ILE B 397 ? 0.7719 0.8669 2.1094 0.2148  0.0454  -0.2735 397 ILE B N   
7436  C CA  . ILE B 397 ? 0.7320 0.8528 2.0724 0.2180  0.0586  -0.2473 397 ILE B CA  
7437  C C   . ILE B 397 ? 0.6884 0.7805 2.0519 0.2088  0.0628  -0.2272 397 ILE B C   
7438  O O   . ILE B 397 ? 0.6474 0.7558 2.0178 0.2058  0.0713  -0.2030 397 ILE B O   
7439  C CB  . ILE B 397 ? 0.7605 0.9055 2.0869 0.2377  0.0676  -0.2565 397 ILE B CB  
7440  C CG1 . ILE B 397 ? 0.7756 0.8873 2.1077 0.2493  0.0682  -0.2733 397 ILE B CG1 
7441  C CG2 . ILE B 397 ? 0.7920 0.9726 2.0937 0.2466  0.0640  -0.2747 397 ILE B CG2 
7442  C CD1 . ILE B 397 ? 0.7823 0.9218 2.1040 0.2695  0.0787  -0.2790 397 ILE B CD1 
7443  N N   . LYS B 398 ? 0.6904 0.7404 2.0658 0.2040  0.0563  -0.2371 398 LYS B N   
7444  C CA  . LYS B 398 ? 0.6555 0.6796 2.0516 0.1953  0.0594  -0.2192 398 LYS B CA  
7445  C C   . LYS B 398 ? 0.6628 0.6480 2.0705 0.1830  0.0487  -0.2276 398 LYS B C   
7446  O O   . LYS B 398 ? 0.6915 0.6545 2.0940 0.1867  0.0408  -0.2507 398 LYS B O   
7447  C CB  . LYS B 398 ? 0.6493 0.6653 2.0490 0.2086  0.0682  -0.2176 398 LYS B CB  
7448  C CG  . LYS B 398 ? 0.6273 0.6182 2.0469 0.2015  0.0713  -0.2004 398 LYS B CG  
7449  C CD  . LYS B 398 ? 0.6268 0.6184 2.0494 0.2154  0.0803  -0.1968 398 LYS B CD  
7450  C CE  . LYS B 398 ? 0.6047 0.5830 2.0452 0.2085  0.0846  -0.1767 398 LYS B CE  
7451  N NZ  . LYS B 398 ? 0.6192 0.5569 2.0706 0.2027  0.0779  -0.1796 398 LYS B NZ  
7452  N N   . ASN B 399 ? 0.6322 0.6103 2.0561 0.1682  0.0485  -0.2085 399 ASN B N   
7453  C CA  . ASN B 399 ? 0.6382 0.5807 2.0774 0.1558  0.0416  -0.2092 399 ASN B CA  
7454  C C   . ASN B 399 ? 0.6179 0.5454 2.0717 0.1558  0.0494  -0.1911 399 ASN B C   
7455  O O   . ASN B 399 ? 0.5951 0.5431 2.0526 0.1564  0.0577  -0.1728 399 ASN B O   
7456  C CB  . ASN B 399 ? 0.6220 0.5713 2.0696 0.1382  0.0346  -0.2024 399 ASN B CB  
7457  C CG  . ASN B 399 ? 0.6484 0.6084 2.0840 0.1358  0.0242  -0.2222 399 ASN B CG  
7458  O OD1 . ASN B 399 ? 0.6826 0.6176 2.1164 0.1342  0.0154  -0.2429 399 ASN B OD1 
7459  N ND2 . ASN B 399 ? 0.6359 0.6318 2.0635 0.1353  0.0244  -0.2161 399 ASN B ND2 
7460  N N   . GLU B 400 ? 0.6331 0.5243 2.0949 0.1551  0.0459  -0.1966 400 GLU B N   
7461  C CA  . GLU B 400 ? 0.6131 0.4882 2.0907 0.1501  0.0502  -0.1784 400 GLU B CA  
7462  C C   . GLU B 400 ? 0.6273 0.4656 2.1155 0.1383  0.0411  -0.1830 400 GLU B C   
7463  O O   . GLU B 400 ? 0.6653 0.4826 2.1477 0.1397  0.0327  -0.2028 400 GLU B O   
7464  C CB  . GLU B 400 ? 0.6159 0.4887 2.0922 0.1662  0.0588  -0.1748 400 GLU B CB  
7465  C CG  . GLU B 400 ? 0.5989 0.4645 2.0900 0.1621  0.0643  -0.1540 400 GLU B CG  
7466  C CD  . GLU B 400 ? 0.5944 0.4715 2.0843 0.1774  0.0738  -0.1477 400 GLU B CD  
7467  O OE1 . GLU B 400 ? 0.6137 0.4941 2.0932 0.1931  0.0754  -0.1611 400 GLU B OE1 
7468  O OE2 . GLU B 400 ? 0.5733 0.4594 2.0729 0.1739  0.0796  -0.1299 400 GLU B OE2 
7469  N N   . SER B 401 ? 0.6023 0.4348 2.1059 0.1259  0.0426  -0.1644 401 SER B N   
7470  C CA  . SER B 401 ? 0.6158 0.4154 2.1317 0.1132  0.0355  -0.1630 401 SER B CA  
7471  C C   . SER B 401 ? 0.6189 0.3981 2.1413 0.1206  0.0409  -0.1512 401 SER B C   
7472  O O   . SER B 401 ? 0.5971 0.3949 2.1179 0.1309  0.0502  -0.1408 401 SER B O   
7473  C CB  . SER B 401 ? 0.5954 0.4075 2.1239 0.0935  0.0328  -0.1506 401 SER B CB  
7474  O OG  . SER B 401 ? 0.5898 0.4242 2.1122 0.0882  0.0276  -0.1608 401 SER B OG  
7475  N N   . ILE B 402 ? 0.6553 0.3963 2.1847 0.1157  0.0342  -0.1536 402 ILE B N   
7476  C CA  . ILE B 402 ? 0.6675 0.3872 2.2048 0.1202  0.0377  -0.1394 402 ILE B CA  
7477  C C   . ILE B 402 ? 0.6887 0.3867 2.2410 0.0996  0.0315  -0.1278 402 ILE B C   
7478  O O   . ILE B 402 ? 0.7185 0.3911 2.2732 0.0896  0.0213  -0.1398 402 ILE B O   
7479  C CB  . ILE B 402 ? 0.7004 0.3917 2.2299 0.1397  0.0359  -0.1534 402 ILE B CB  
7480  C CG1 . ILE B 402 ? 0.6829 0.4020 2.1981 0.1604  0.0430  -0.1641 402 ILE B CG1 
7481  C CG2 . ILE B 402 ? 0.7094 0.3753 2.2483 0.1435  0.0376  -0.1371 402 ILE B CG2 
7482  C CD1 . ILE B 402 ? 0.6408 0.3900 2.1581 0.1674  0.0546  -0.1460 402 ILE B CD1 
7483  N N   . ASN B 403 ? 0.6757 0.3866 2.2383 0.0926  0.0376  -0.1048 403 ASN B N   
7484  C CA  . ASN B 403 ? 0.6972 0.3963 2.2746 0.0724  0.0336  -0.0902 403 ASN B CA  
7485  C C   . ASN B 403 ? 0.7230 0.3883 2.3059 0.0760  0.0330  -0.0783 403 ASN B C   
7486  O O   . ASN B 403 ? 0.7024 0.3760 2.2835 0.0888  0.0406  -0.0669 403 ASN B O   
7487  C CB  . ASN B 403 ? 0.6698 0.4071 2.2550 0.0621  0.0402  -0.0728 403 ASN B CB  
7488  C CG  . ASN B 403 ? 0.6595 0.4244 2.2430 0.0544  0.0378  -0.0824 403 ASN B CG  
7489  O OD1 . ASN B 403 ? 0.6837 0.4425 2.2737 0.0384  0.0297  -0.0875 403 ASN B OD1 
7490  N ND2 . ASN B 403 ? 0.6286 0.4239 2.2041 0.0650  0.0443  -0.0841 403 ASN B ND2 
7491  N N   . ILE B 404 ? 0.7738 0.4013 2.3640 0.0639  0.0233  -0.0806 404 ILE B N   
7492  C CA  . ILE B 404 ? 0.8003 0.3905 2.3975 0.0644  0.0208  -0.0671 404 ILE B CA  
7493  C C   . ILE B 404 ? 0.8078 0.3896 2.4213 0.0378  0.0161  -0.0502 404 ILE B C   
7494  O O   . ILE B 404 ? 0.7877 0.3774 2.4064 0.0204  0.0106  -0.0577 404 ILE B O   
7495  C CB  . ILE B 404 ? 0.8475 0.3924 2.4381 0.0780  0.0125  -0.0875 404 ILE B CB  
7496  C CG1 . ILE B 404 ? 0.8846 0.4023 2.4796 0.0608  -0.0003 -0.1047 404 ILE B CG1 
7497  C CG2 . ILE B 404 ? 0.8290 0.3912 2.4036 0.1034  0.0179  -0.1056 404 ILE B CG2 
7498  C CD1 . ILE B 404 ? 0.9330 0.4018 2.5224 0.0733  -0.0102 -0.1272 404 ILE B CD1 
7499  N N   . LEU B 405 ? 0.8296 0.3999 2.4509 0.0353  0.0187  -0.0261 405 LEU B N   
7500  C CA  . LEU B 405 ? 0.8808 0.4318 2.5176 0.0120  0.0133  -0.0079 405 LEU B CA  
7501  C C   . LEU B 405 ? 0.9591 0.4499 2.5982 0.0158  0.0041  -0.0092 405 LEU B C   
7502  O O   . LEU B 405 ? 0.9798 0.4552 2.6152 0.0327  0.0071  0.0010  405 LEU B O   
7503  C CB  . LEU B 405 ? 0.8654 0.4480 2.5079 0.0083  0.0230  0.0214  405 LEU B CB  
7504  C CG  . LEU B 405 ? 0.9089 0.4810 2.5677 -0.0162 0.0198  0.0461  405 LEU B CG  
7505  C CD1 . LEU B 405 ? 0.9102 0.5014 2.5796 -0.0410 0.0157  0.0413  405 LEU B CD1 
7506  C CD2 . LEU B 405 ? 0.8941 0.4963 2.5550 -0.0144 0.0299  0.0743  405 LEU B CD2 
7507  N N   . ALA B 406 ? 1.0148 0.4715 2.6610 -0.0004 -0.0079 -0.0213 406 ALA B N   
7508  C CA  . ALA B 406 ? 1.0816 0.4763 2.7287 0.0056  -0.0185 -0.0299 406 ALA B CA  
7509  C C   . ALA B 406 ? 1.1439 0.5030 2.8095 -0.0221 -0.0279 -0.0128 406 ALA B C   
7510  O O   . ALA B 406 ? 1.1276 0.5109 2.8048 -0.0482 -0.0284 -0.0032 406 ALA B O   
7511  C CB  . ALA B 406 ? 1.0966 0.4766 2.7326 0.0166  -0.0259 -0.0671 406 ALA B CB  
7512  N N   . SER B 407 ? 1.1933 0.4950 2.8620 -0.0157 -0.0354 -0.0086 407 SER B N   
7513  C CA  . SER B 407 ? 1.2525 0.5086 2.9386 -0.0403 -0.0461 0.0068  407 SER B CA  
7514  C C   . SER B 407 ? 1.3390 0.5253 3.0229 -0.0240 -0.0570 -0.0057 407 SER B C   
7515  O O   . SER B 407 ? 1.3503 0.5316 3.0206 0.0072  -0.0530 -0.0153 407 SER B O   
7516  C CB  . SER B 407 ? 1.2386 0.5124 2.9359 -0.0545 -0.0389 0.0485  407 SER B CB  
7517  O OG  . SER B 407 ? 1.2999 0.5266 3.0146 -0.0783 -0.0492 0.0665  407 SER B OG  
7518  N N   . LYS B 408 ? 1.3902 0.5233 3.0884 -0.0452 -0.0711 -0.0060 408 LYS B N   
7519  C CA  . LYS B 408 ? 1.4537 0.5139 3.1521 -0.0314 -0.0832 -0.0173 408 LYS B CA  
7520  C C   . LYS B 408 ? 1.4725 0.5102 3.1753 -0.0222 -0.0796 0.0183  408 LYS B C   
7521  O O   . LYS B 408 ? 1.4981 0.4894 3.1960 0.0023  -0.0847 0.0119  408 LYS B O   
7522  C CB  . LYS B 408 ? 1.5186 0.5274 3.2322 -0.0592 -0.1005 -0.0292 408 LYS B CB  
7523  C CG  . LYS B 408 ? 1.5103 0.5398 3.2186 -0.0665 -0.1058 -0.0668 408 LYS B CG  
7524  C CD  . LYS B 408 ? 1.5718 0.5499 3.2942 -0.0922 -0.1244 -0.0843 408 LYS B CD  
7525  C CE  . LYS B 408 ? 1.5640 0.5736 3.2793 -0.0980 -0.1285 -0.1201 408 LYS B CE  
7526  N NZ  . LYS B 408 ? 1.6265 0.6020 3.3585 -0.1302 -0.1455 -0.1327 408 LYS B NZ  
7527  N N   . THR B 409 ? 1.4583 0.5316 3.1701 -0.0411 -0.0709 0.0555  409 THR B N   
7528  C CA  . THR B 409 ? 1.4788 0.5398 3.1941 -0.0343 -0.0668 0.0928  409 THR B CA  
7529  C C   . THR B 409 ? 1.4227 0.5576 3.1312 -0.0292 -0.0496 0.1142  409 THR B C   
7530  O O   . THR B 409 ? 1.3533 0.5436 3.0583 -0.0371 -0.0421 0.1043  409 THR B O   
7531  C CB  . THR B 409 ? 1.5291 0.5474 3.2654 -0.0662 -0.0764 0.1210  409 THR B CB  
7532  O OG1 . THR B 409 ? 1.5563 0.5665 3.2921 -0.0534 -0.0716 0.1558  409 THR B OG1 
7533  C CG2 . THR B 409 ? 1.4920 0.5545 3.2418 -0.1038 -0.0729 0.1370  409 THR B CG2 
7534  N N   . ALA B 410 ? 1.4408 0.5743 3.1472 -0.0150 -0.0443 0.1432  410 ALA B N   
7535  C CA  . ALA B 410 ? 1.3906 0.5894 3.0899 -0.0077 -0.0292 0.1638  410 ALA B CA  
7536  C C   . ALA B 410 ? 1.3752 0.6160 3.0863 -0.0409 -0.0239 0.1877  410 ALA B C   
7537  O O   . ALA B 410 ? 1.4170 0.6288 3.1438 -0.0687 -0.0320 0.2014  410 ALA B O   
7538  C CB  . ALA B 410 ? 1.4177 0.6012 3.1137 0.0126  -0.0271 0.1901  410 ALA B CB  
7539  N N   . PHE B 411 ? 1.3120 0.6218 3.0160 -0.0376 -0.0106 0.1920  411 PHE B N   
7540  C CA  . PHE B 411 ? 1.2744 0.6331 2.9881 -0.0645 -0.0039 0.2138  411 PHE B CA  
7541  C C   . PHE B 411 ? 1.2042 0.6209 2.9087 -0.0508 0.0100  0.2323  411 PHE B C   
7542  O O   . PHE B 411 ? 1.1926 0.6208 2.8830 -0.0228 0.0147  0.2194  411 PHE B O   
7543  C CB  . PHE B 411 ? 1.2561 0.6410 2.9732 -0.0805 -0.0047 0.1883  411 PHE B CB  
7544  C CG  . PHE B 411 ? 1.2167 0.6244 2.9180 -0.0569 -0.0007 0.1537  411 PHE B CG  
7545  C CD1 . PHE B 411 ? 1.2412 0.6066 2.9356 -0.0426 -0.0094 0.1223  411 PHE B CD1 
7546  C CD2 . PHE B 411 ? 1.1578 0.6290 2.8511 -0.0488 0.0117  0.1529  411 PHE B CD2 
7547  C CE1 . PHE B 411 ? 1.2079 0.5973 2.8877 -0.0218 -0.0051 0.0934  411 PHE B CE1 
7548  C CE2 . PHE B 411 ? 1.1112 0.6012 2.7909 -0.0285 0.0151  0.1242  411 PHE B CE2 
7549  C CZ  . PHE B 411 ? 1.1387 0.5895 2.8116 -0.0156 0.0071  0.0956  411 PHE B CZ  
7550  N N   . GLU B 412 ? 1.1743 0.6286 2.8873 -0.0712 0.0160  0.2621  412 GLU B N   
7551  C CA  . GLU B 412 ? 1.1280 0.6424 2.8327 -0.0609 0.0289  0.2780  412 GLU B CA  
7552  C C   . GLU B 412 ? 1.0467 0.6140 2.7447 -0.0559 0.0365  0.2523  412 GLU B C   
7553  O O   . GLU B 412 ? 1.0307 0.6061 2.7361 -0.0730 0.0340  0.2375  412 GLU B O   
7554  C CB  . GLU B 412 ? 1.1657 0.7060 2.8811 -0.0839 0.0329  0.3169  412 GLU B CB  
7555  C CG  . GLU B 412 ? 1.2574 0.7486 2.9776 -0.0854 0.0264  0.3473  412 GLU B CG  
7556  C CD  . GLU B 412 ? 1.3301 0.8400 3.0628 -0.1121 0.0289  0.3886  412 GLU B CD  
7557  O OE1 . GLU B 412 ? 1.3459 0.8718 3.0926 -0.1410 0.0284  0.3916  412 GLU B OE1 
7558  O OE2 . GLU B 412 ? 1.4014 0.9097 3.1300 -0.1037 0.0310  0.4189  412 GLU B OE2 
7559  N N   . LEU B 413 ? 0.9866 0.5864 2.6708 -0.0317 0.0447  0.2469  413 LEU B N   
7560  C CA  . LEU B 413 ? 0.9073 0.5629 2.5850 -0.0258 0.0535  0.2300  413 LEU B CA  
7561  C C   . LEU B 413 ? 0.8584 0.5683 2.5345 -0.0266 0.0636  0.2542  413 LEU B C   
7562  O O   . LEU B 413 ? 0.8764 0.5803 2.5514 -0.0230 0.0643  0.2799  413 LEU B O   
7563  C CB  . LEU B 413 ? 0.8894 0.5420 2.5530 0.0022  0.0549  0.2039  413 LEU B CB  
7564  C CG  . LEU B 413 ? 0.9143 0.5187 2.5754 0.0095  0.0460  0.1766  413 LEU B CG  
7565  C CD1 . LEU B 413 ? 0.8883 0.4967 2.5356 0.0384  0.0491  0.1575  413 LEU B CD1 
7566  C CD2 . LEU B 413 ? 0.9085 0.5201 2.5751 -0.0072 0.0431  0.1567  413 LEU B CD2 
7567  N N   . PRO B 414 ? 0.8021 0.5671 2.4769 -0.0288 0.0714  0.2459  414 PRO B N   
7568  C CA  . PRO B 414 ? 0.7710 0.5890 2.4409 -0.0232 0.0811  0.2624  414 PRO B CA  
7569  C C   . PRO B 414 ? 0.7506 0.5702 2.4063 0.0047  0.0836  0.2539  414 PRO B C   
7570  O O   . PRO B 414 ? 0.7389 0.5372 2.3887 0.0186  0.0808  0.2290  414 PRO B O   
7571  C CB  . PRO B 414 ? 0.7286 0.5959 2.4022 -0.0319 0.0867  0.2492  414 PRO B CB  
7572  C CG  . PRO B 414 ? 0.7215 0.5633 2.3948 -0.0293 0.0811  0.2182  414 PRO B CG  
7573  C CD  . PRO B 414 ? 0.7763 0.5556 2.4540 -0.0354 0.0709  0.2202  414 PRO B CD  
7574  N N   . GLU B 415 ? 0.7422 0.5896 2.3923 0.0126  0.0888  0.2746  415 GLU B N   
7575  C CA  . GLU B 415 ? 0.7214 0.5772 2.3593 0.0379  0.0910  0.2669  415 GLU B CA  
7576  C C   . GLU B 415 ? 0.6921 0.6101 2.3239 0.0431  0.0998  0.2719  415 GLU B C   
7577  O O   . GLU B 415 ? 0.6889 0.6425 2.3250 0.0292  0.1044  0.2874  415 GLU B O   
7578  C CB  . GLU B 415 ? 0.7539 0.5721 2.3888 0.0494  0.0860  0.2845  415 GLU B CB  
7579  C CG  . GLU B 415 ? 0.7712 0.6028 2.4084 0.0405  0.0875  0.3215  415 GLU B CG  
7580  C CD  . GLU B 415 ? 0.8039 0.5965 2.4379 0.0544  0.0818  0.3390  415 GLU B CD  
7581  O OE1 . GLU B 415 ? 0.7930 0.5592 2.4217 0.0746  0.0781  0.3208  415 GLU B OE1 
7582  O OE2 . GLU B 415 ? 0.8332 0.6238 2.4706 0.0449  0.0810  0.3718  415 GLU B OE2 
7583  N N   . LEU B 416 ? 0.6728 0.6047 2.2950 0.0637  0.1019  0.2568  416 LEU B N   
7584  C CA  . LEU B 416 ? 0.6416 0.6292 2.2574 0.0709  0.1088  0.2551  416 LEU B CA  
7585  C C   . LEU B 416 ? 0.6383 0.6274 2.2452 0.0910  0.1081  0.2611  416 LEU B C   
7586  O O   . LEU B 416 ? 0.6413 0.5978 2.2459 0.1042  0.1039  0.2495  416 LEU B O   
7587  C CB  . LEU B 416 ? 0.6129 0.6199 2.2282 0.0734  0.1116  0.2254  416 LEU B CB  
7588  C CG  . LEU B 416 ? 0.5867 0.6505 2.1980 0.0773  0.1182  0.2197  416 LEU B CG  
7589  C CD1 . LEU B 416 ? 0.5579 0.6297 2.1718 0.0764  0.1193  0.1930  416 LEU B CD1 
7590  C CD2 . LEU B 416 ? 0.5854 0.6690 2.1872 0.0957  0.1194  0.2189  416 LEU B CD2 
7591  N N   . THR B 417 ? 0.6336 0.6621 2.2357 0.0930  0.1119  0.2804  417 THR B N   
7592  C CA  . THR B 417 ? 0.6327 0.6728 2.2260 0.1120  0.1113  0.2869  417 THR B CA  
7593  C C   . THR B 417 ? 0.6097 0.7123 2.1963 0.1156  0.1173  0.2857  417 THR B C   
7594  O O   . THR B 417 ? 0.5832 0.7181 2.1718 0.1027  0.1220  0.2899  417 THR B O   
7595  C CB  . THR B 417 ? 0.6620 0.6742 2.2555 0.1131  0.1069  0.3177  417 THR B CB  
7596  O OG1 . THR B 417 ? 0.6694 0.7111 2.2642 0.0979  0.1107  0.3431  417 THR B OG1 
7597  C CG2 . THR B 417 ? 0.6896 0.6372 2.2906 0.1087  0.1001  0.3165  417 THR B CG2 
7598  N N   . ILE B 418 ? 0.6000 0.7205 2.1792 0.1337  0.1167  0.2776  418 ILE B N   
7599  C CA  . ILE B 418 ? 0.5820 0.7597 2.1543 0.1390  0.1210  0.2713  418 ILE B CA  
7600  C C   . ILE B 418 ? 0.6017 0.7995 2.1656 0.1527  0.1193  0.2899  418 ILE B C   
7601  O O   . ILE B 418 ? 0.6489 0.8173 2.2123 0.1644  0.1145  0.2955  418 ILE B O   
7602  C CB  . ILE B 418 ? 0.5498 0.7385 2.1225 0.1452  0.1219  0.2376  418 ILE B CB  
7603  C CG1 . ILE B 418 ? 0.5458 0.7132 2.1173 0.1607  0.1178  0.2254  418 ILE B CG1 
7604  C CG2 . ILE B 418 ? 0.5475 0.7194 2.1279 0.1321  0.1234  0.2215  418 ILE B CG2 
7605  C CD1 . ILE B 418 ? 0.5092 0.6857 2.0823 0.1642  0.1187  0.1949  418 ILE B CD1 
7606  N N   . GLU B 419 ? 0.5912 0.8414 2.1484 0.1518  0.1231  0.2993  419 GLU B N   
7607  C CA  . GLU B 419 ? 0.6010 0.8836 2.1486 0.1654  0.1217  0.3130  419 GLU B CA  
7608  C C   . GLU B 419 ? 0.5708 0.9035 2.1128 0.1724  0.1238  0.2885  419 GLU B C   
7609  O O   . GLU B 419 ? 0.5815 0.9507 2.1218 0.1649  0.1285  0.2818  419 GLU B O   
7610  C CB  . GLU B 419 ? 0.6310 0.9379 2.1737 0.1582  0.1241  0.3475  419 GLU B CB  
7611  C CG  . GLU B 419 ? 0.6708 0.9277 2.2201 0.1491  0.1213  0.3752  419 GLU B CG  
7612  C CD  . GLU B 419 ? 0.7020 0.9895 2.2462 0.1418  0.1241  0.4114  419 GLU B CD  
7613  O OE1 . GLU B 419 ? 0.6872 1.0293 2.2266 0.1363  0.1302  0.4083  419 GLU B OE1 
7614  O OE2 . GLU B 419 ? 0.7417 0.9999 2.2867 0.1418  0.1202  0.4419  419 GLU B OE2 
7615  N N   . VAL B 420 ? 0.5532 0.8878 2.0931 0.1871  0.1200  0.2744  420 VAL B N   
7616  C CA  . VAL B 420 ? 0.5292 0.9039 2.0660 0.1924  0.1206  0.2480  420 VAL B CA  
7617  C C   . VAL B 420 ? 0.5483 0.9746 2.0741 0.2024  0.1194  0.2596  420 VAL B C   
7618  O O   . VAL B 420 ? 0.5878 1.0125 2.1090 0.2085  0.1171  0.2870  420 VAL B O   
7619  C CB  . VAL B 420 ? 0.5109 0.8570 2.0541 0.1999  0.1170  0.2250  420 VAL B CB  
7620  C CG1 . VAL B 420 ? 0.4791 0.8602 2.0215 0.2045  0.1163  0.1970  420 VAL B CG1 
7621  C CG2 . VAL B 420 ? 0.5056 0.8022 2.0579 0.1901  0.1180  0.2167  420 VAL B CG2 
7622  N N   . THR B 421 ? 0.5350 1.0069 2.0564 0.2040  0.1205  0.2386  421 THR B N   
7623  C CA  . THR B 421 ? 0.5387 1.0634 2.0495 0.2147  0.1182  0.2409  421 THR B CA  
7624  C C   . THR B 421 ? 0.5238 1.0631 2.0373 0.2207  0.1147  0.2067  421 THR B C   
7625  O O   . THR B 421 ? 0.5322 1.0597 2.0526 0.2138  0.1163  0.1819  421 THR B O   
7626  C CB  . THR B 421 ? 0.5378 1.1110 2.0393 0.2095  0.1231  0.2507  421 THR B CB  
7627  O OG1 . THR B 421 ? 0.5602 1.1164 2.0615 0.2014  0.1263  0.2843  421 THR B OG1 
7628  C CG2 . THR B 421 ? 0.5399 1.1719 2.0284 0.2209  0.1204  0.2532  421 THR B CG2 
7629  N N   . PRO B 422 ? 0.5172 1.0796 2.0272 0.2331  0.1092  0.2046  422 PRO B N   
7630  C CA  . PRO B 422 ? 0.5384 1.1012 2.0433 0.2436  0.1059  0.2337  422 PRO B CA  
7631  C C   . PRO B 422 ? 0.5425 1.0444 2.0572 0.2447  0.1048  0.2419  422 PRO B C   
7632  O O   . PRO B 422 ? 0.5179 0.9910 2.0423 0.2422  0.1045  0.2199  422 PRO B O   
7633  C CB  . PRO B 422 ? 0.5361 1.1420 2.0371 0.2558  0.0998  0.2210  422 PRO B CB  
7634  C CG  . PRO B 422 ? 0.5150 1.1506 2.0160 0.2495  0.1007  0.1882  422 PRO B CG  
7635  C CD  . PRO B 422 ? 0.4973 1.0881 2.0087 0.2372  0.1052  0.1741  422 PRO B CD  
7636  N N   . GLU B 423 ? 0.5725 1.0554 2.0845 0.2487  0.1039  0.2741  423 GLU B N   
7637  C CA  . GLU B 423 ? 0.5932 1.0166 2.1136 0.2505  0.1023  0.2830  423 GLU B CA  
7638  C C   . GLU B 423 ? 0.5949 1.0089 2.1206 0.2659  0.0970  0.2714  423 GLU B C   
7639  O O   . GLU B 423 ? 0.5915 0.9609 2.1260 0.2662  0.0966  0.2621  423 GLU B O   
7640  C CB  . GLU B 423 ? 0.6290 1.0366 2.1451 0.2508  0.1019  0.3214  423 GLU B CB  
7641  C CG  . GLU B 423 ? 0.6441 0.9856 2.1688 0.2520  0.0996  0.3312  423 GLU B CG  
7642  C CD  . GLU B 423 ? 0.6783 1.0010 2.1999 0.2562  0.0967  0.3697  423 GLU B CD  
7643  O OE1 . GLU B 423 ? 0.6899 1.0529 2.2018 0.2605  0.0962  0.3919  423 GLU B OE1 
7644  O OE2 . GLU B 423 ? 0.6945 0.9602 2.2234 0.2548  0.0947  0.3770  423 GLU B OE2 
7645  N N   . LYS B 424 ? 0.5972 1.0550 2.1180 0.2788  0.0927  0.2720  424 LYS B N   
7646  C CA  . LYS B 424 ? 0.6093 1.0601 2.1356 0.2950  0.0874  0.2685  424 LYS B CA  
7647  C C   . LYS B 424 ? 0.5733 1.0624 2.1034 0.2976  0.0851  0.2391  424 LYS B C   
7648  O O   . LYS B 424 ? 0.5701 1.0410 2.1100 0.3022  0.0838  0.2234  424 LYS B O   
7649  C CB  . LYS B 424 ? 0.6610 1.1239 2.1810 0.3112  0.0824  0.2995  424 LYS B CB  
7650  C CG  . LYS B 424 ? 0.7175 1.1392 2.2351 0.3093  0.0832  0.3327  424 LYS B CG  
7651  C CD  . LYS B 424 ? 0.7705 1.1926 2.2841 0.3279  0.0771  0.3635  424 LYS B CD  
7652  C CE  . LYS B 424 ? 0.8273 1.2211 2.3366 0.3234  0.0775  0.4005  424 LYS B CE  
7653  N NZ  . LYS B 424 ? 0.8514 1.1743 2.3697 0.3179  0.0779  0.4050  424 LYS B NZ  
7654  N N   . ASP B 425 ? 0.5516 1.0941 2.0742 0.2949  0.0844  0.2320  425 ASP B N   
7655  C CA  . ASP B 425 ? 0.5208 1.1040 2.0467 0.2976  0.0805  0.2062  425 ASP B CA  
7656  C C   . ASP B 425 ? 0.4877 1.0997 2.0100 0.2844  0.0828  0.1842  425 ASP B C   
7657  O O   . ASP B 425 ? 0.4983 1.1419 2.0089 0.2829  0.0838  0.1942  425 ASP B O   
7658  C CB  . ASP B 425 ? 0.5400 1.1688 2.0602 0.3134  0.0738  0.2191  425 ASP B CB  
7659  C CG  . ASP B 425 ? 0.5280 1.1985 2.0541 0.3172  0.0682  0.1941  425 ASP B CG  
7660  O OD1 . ASP B 425 ? 0.5085 1.1756 2.0425 0.3056  0.0695  0.1656  425 ASP B OD1 
7661  O OD2 . ASP B 425 ? 0.5365 1.2425 2.0603 0.3314  0.0619  0.2039  425 ASP B OD2 
7662  N N   . LEU B 426 ? 0.4489 1.0527 1.9809 0.2761  0.0831  0.1544  426 LEU B N   
7663  C CA  . LEU B 426 ? 0.4272 1.0484 1.9579 0.2641  0.0849  0.1310  426 LEU B CA  
7664  C C   . LEU B 426 ? 0.4316 1.1135 1.9551 0.2679  0.0796  0.1194  426 LEU B C   
7665  O O   . LEU B 426 ? 0.4193 1.1201 1.9410 0.2602  0.0799  0.0981  426 LEU B O   
7666  C CB  . LEU B 426 ? 0.3994 0.9926 1.9434 0.2548  0.0857  0.1044  426 LEU B CB  
7667  C CG  . LEU B 426 ? 0.3942 0.9298 1.9452 0.2500  0.0906  0.1101  426 LEU B CG  
7668  C CD1 . LEU B 426 ? 0.3728 0.8914 1.9353 0.2407  0.0909  0.0832  426 LEU B CD1 
7669  C CD2 . LEU B 426 ? 0.3991 0.9134 1.9440 0.2433  0.0962  0.1247  426 LEU B CD2 
7670  N N   . ASN B 427 ? 0.4560 1.1694 1.9760 0.2805  0.0740  0.1312  427 ASN B N   
7671  C CA  . ASN B 427 ? 0.4683 1.2427 1.9805 0.2846  0.0681  0.1206  427 ASN B CA  
7672  C C   . ASN B 427 ? 0.4941 1.2975 1.9889 0.2868  0.0708  0.1397  427 ASN B C   
7673  O O   . ASN B 427 ? 0.5022 1.3580 1.9874 0.2890  0.0672  0.1293  427 ASN B O   
7674  C CB  . ASN B 427 ? 0.4768 1.2804 1.9919 0.2974  0.0603  0.1252  427 ASN B CB  
7675  C CG  . ASN B 427 ? 0.4576 1.2541 1.9897 0.2938  0.0564  0.1005  427 ASN B CG  
7676  O OD1 . ASN B 427 ? 0.4382 1.2359 1.9767 0.2817  0.0557  0.0719  427 ASN B OD1 
7677  N ND2 . ASN B 427 ? 0.4578 1.2488 1.9980 0.3043  0.0536  0.1114  427 ASN B ND2 
7678  N N   . GLU B 428 ? 0.5177 1.2886 2.0088 0.2857  0.0771  0.1674  428 GLU B N   
7679  C CA  . GLU B 428 ? 0.5512 1.3484 2.0268 0.2874  0.0803  0.1927  428 GLU B CA  
7680  C C   . GLU B 428 ? 0.5534 1.3710 2.0231 0.2771  0.0852  0.1759  428 GLU B C   
7681  O O   . GLU B 428 ? 0.5830 1.4380 2.0388 0.2787  0.0877  0.1916  428 GLU B O   
7682  C CB  . GLU B 428 ? 0.5735 1.3271 2.0490 0.2872  0.0849  0.2282  428 GLU B CB  
7683  C CG  . GLU B 428 ? 0.6040 1.3514 2.0794 0.3020  0.0798  0.2548  428 GLU B CG  
7684  C CD  . GLU B 428 ? 0.6336 1.3495 2.1052 0.3038  0.0826  0.2950  428 GLU B CD  
7685  O OE1 . GLU B 428 ? 0.6346 1.3301 2.1048 0.2914  0.0892  0.3048  428 GLU B OE1 
7686  O OE2 . GLU B 428 ? 0.6498 1.3621 2.1208 0.3179  0.0775  0.3168  428 GLU B OE2 
7687  N N   . GLY B 429 ? 0.5262 1.3202 2.0062 0.2672  0.0869  0.1457  429 GLY B N   
7688  C CA  . GLY B 429 ? 0.5182 1.3277 1.9942 0.2592  0.0914  0.1285  429 GLY B CA  
7689  C C   . GLY B 429 ? 0.5000 1.2850 1.9889 0.2512  0.0902  0.0924  429 GLY B C   
7690  O O   . GLY B 429 ? 0.4948 1.2381 1.9965 0.2485  0.0889  0.0875  429 GLY B O   
7691  N N   . LYS B 430 ? 0.4977 1.3095 1.9828 0.2481  0.0909  0.0680  430 LYS B N   
7692  C CA  . LYS B 430 ? 0.4762 1.2669 1.9727 0.2410  0.0893  0.0338  430 LYS B CA  
7693  C C   . LYS B 430 ? 0.4467 1.1993 1.9487 0.2325  0.0970  0.0358  430 LYS B C   
7694  O O   . LYS B 430 ? 0.4315 1.1519 1.9452 0.2262  0.0964  0.0146  430 LYS B O   
7695  C CB  . LYS B 430 ? 0.4980 1.3372 1.9880 0.2441  0.0843  0.0038  430 LYS B CB  
7696  C CG  . LYS B 430 ? 0.5196 1.3921 2.0084 0.2501  0.0747  -0.0064 430 LYS B CG  
7697  C CD  . LYS B 430 ? 0.5413 1.4631 2.0232 0.2532  0.0684  -0.0378 430 LYS B CD  
7698  C CE  . LYS B 430 ? 0.5639 1.5234 2.0436 0.2590  0.0587  -0.0432 430 LYS B CE  
7699  N NZ  . LYS B 430 ? 0.5876 1.6040 2.0556 0.2640  0.0530  -0.0680 430 LYS B NZ  
7700  N N   . ILE B 431 ? 0.4355 1.1934 1.9298 0.2319  0.1037  0.0624  431 ILE B N   
7701  C CA  . ILE B 431 ? 0.4173 1.1417 1.9176 0.2232  0.1107  0.0673  431 ILE B CA  
7702  C C   . ILE B 431 ? 0.4116 1.0951 1.9156 0.2198  0.1136  0.0988  431 ILE B C   
7703  O O   . ILE B 431 ? 0.4219 1.1179 1.9187 0.2254  0.1126  0.1236  431 ILE B O   
7704  C CB  . ILE B 431 ? 0.4315 1.1973 1.9218 0.2233  0.1164  0.0706  431 ILE B CB  
7705  C CG1 . ILE B 431 ? 0.4361 1.2451 1.9212 0.2291  0.1128  0.0373  431 ILE B CG1 
7706  C CG2 . ILE B 431 ? 0.4295 1.1644 1.9273 0.2138  0.1234  0.0770  431 ILE B CG2 
7707  C CD1 . ILE B 431 ? 0.4246 1.2034 1.9226 0.2256  0.1094  0.0027  431 ILE B CD1 
7708  N N   . ALA B 432 ? 0.3974 1.0332 1.9122 0.2112  0.1169  0.0972  432 ALA B N   
7709  C CA  . ALA B 432 ? 0.4059 0.9986 1.9250 0.2068  0.1194  0.1234  432 ALA B CA  
7710  C C   . ALA B 432 ? 0.4090 0.9909 1.9298 0.1968  0.1261  0.1350  432 ALA B C   
7711  O O   . ALA B 432 ? 0.3889 0.9895 1.9104 0.1936  0.1289  0.1185  432 ALA B O   
7712  C CB  . ALA B 432 ? 0.3942 0.9393 1.9247 0.2055  0.1164  0.1117  432 ALA B CB  
7713  N N   . SER B 433 ? 0.4283 0.9792 1.9511 0.1919  0.1281  0.1626  433 SER B N   
7714  C CA  . SER B 433 ? 0.4370 0.9741 1.9641 0.1801  0.1337  0.1747  433 SER B CA  
7715  C C   . SER B 433 ? 0.4555 0.9361 1.9902 0.1739  0.1330  0.1920  433 SER B C   
7716  O O   . SER B 433 ? 0.4762 0.9416 2.0083 0.1789  0.1301  0.2120  433 SER B O   
7717  C CB  . SER B 433 ? 0.4509 1.0340 1.9690 0.1779  0.1385  0.1962  433 SER B CB  
7718  O OG  . SER B 433 ? 0.4702 1.0528 1.9822 0.1796  0.1377  0.2297  433 SER B OG  
7719  N N   . ILE B 434 ? 0.4517 0.9029 1.9957 0.1637  0.1352  0.1840  434 ILE B N   
7720  C CA  . ILE B 434 ? 0.4672 0.8667 2.0186 0.1559  0.1345  0.1977  434 ILE B CA  
7721  C C   . ILE B 434 ? 0.4828 0.8866 2.0371 0.1423  0.1390  0.2181  434 ILE B C   
7722  O O   . ILE B 434 ? 0.4658 0.8778 2.0255 0.1342  0.1423  0.2067  434 ILE B O   
7723  C CB  . ILE B 434 ? 0.4492 0.8109 2.0095 0.1539  0.1327  0.1735  434 ILE B CB  
7724  C CG1 . ILE B 434 ? 0.4377 0.7986 1.9970 0.1654  0.1286  0.1540  434 ILE B CG1 
7725  C CG2 . ILE B 434 ? 0.4640 0.7743 2.0308 0.1463  0.1314  0.1861  434 ILE B CG2 
7726  C CD1 . ILE B 434 ? 0.4217 0.7524 1.9889 0.1633  0.1273  0.1305  434 ILE B CD1 
7727  N N   . LYS B 435 ? 0.5112 0.9082 2.0627 0.1397  0.1387  0.2492  435 LYS B N   
7728  C CA  . LYS B 435 ? 0.5306 0.9251 2.0866 0.1245  0.1422  0.2730  435 LYS B CA  
7729  C C   . LYS B 435 ? 0.5409 0.8740 2.1076 0.1155  0.1389  0.2739  435 LYS B C   
7730  O O   . LYS B 435 ? 0.5571 0.8513 2.1239 0.1198  0.1342  0.2849  435 LYS B O   
7731  C CB  . LYS B 435 ? 0.5641 0.9799 2.1124 0.1252  0.1429  0.3076  435 LYS B CB  
7732  C CG  . LYS B 435 ? 0.5613 1.0443 2.0973 0.1335  0.1463  0.3090  435 LYS B CG  
7733  C CD  . LYS B 435 ? 0.5919 1.0933 2.1182 0.1380  0.1454  0.3433  435 LYS B CD  
7734  C CE  . LYS B 435 ? 0.5882 1.1614 2.1016 0.1436  0.1496  0.3484  435 LYS B CE  
7735  N NZ  . LYS B 435 ? 0.5568 1.1623 2.0649 0.1557  0.1488  0.3124  435 LYS B NZ  
7736  N N   . THR B 436 ? 0.5370 0.8636 2.1126 0.1040  0.1410  0.2613  436 THR B N   
7737  C CA  . THR B 436 ? 0.5452 0.8186 2.1307 0.0943  0.1377  0.2594  436 THR B CA  
7738  C C   . THR B 436 ? 0.5638 0.8295 2.1558 0.0768  0.1388  0.2883  436 THR B C   
7739  O O   . THR B 436 ? 0.5529 0.8618 2.1438 0.0700  0.1439  0.3041  436 THR B O   
7740  C CB  . THR B 436 ? 0.5252 0.7965 2.1167 0.0922  0.1384  0.2298  436 THR B CB  
7741  O OG1 . THR B 436 ? 0.5093 0.8025 2.0950 0.1062  0.1386  0.2064  436 THR B OG1 
7742  C CG2 . THR B 436 ? 0.5313 0.7470 2.1296 0.0883  0.1335  0.2209  436 THR B CG2 
7743  N N   . LYS B 437 ? 0.5884 0.7993 2.1871 0.0698  0.1336  0.2954  437 LYS B N   
7744  C CA  . LYS B 437 ? 0.6255 0.8171 2.2308 0.0539  0.1324  0.3257  437 LYS B CA  
7745  C C   . LYS B 437 ? 0.6422 0.7761 2.2577 0.0440  0.1265  0.3175  437 LYS B C   
7746  O O   . LYS B 437 ? 0.6514 0.7394 2.2653 0.0535  0.1207  0.3118  437 LYS B O   
7747  C CB  . LYS B 437 ? 0.6538 0.8348 2.2523 0.0614  0.1298  0.3536  437 LYS B CB  
7748  C CG  . LYS B 437 ? 0.6987 0.8553 2.3051 0.0436  0.1278  0.3871  437 LYS B CG  
7749  C CD  . LYS B 437 ? 0.7390 0.8801 2.3399 0.0503  0.1244  0.4184  437 LYS B CD  
7750  C CE  . LYS B 437 ? 0.7822 0.8978 2.3934 0.0290  0.1223  0.4505  437 LYS B CE  
7751  N NZ  . LYS B 437 ? 0.8256 0.9236 2.4322 0.0349  0.1186  0.4839  437 LYS B NZ  
7752  N N   . ILE B 438 ? 0.6415 0.7821 2.2677 0.0254  0.1281  0.3167  438 ILE B N   
7753  C CA  . ILE B 438 ? 0.6501 0.7446 2.2865 0.0141  0.1226  0.3057  438 ILE B CA  
7754  C C   . ILE B 438 ? 0.6979 0.7740 2.3449 -0.0075 0.1202  0.3345  438 ILE B C   
7755  O O   . ILE B 438 ? 0.7146 0.8307 2.3670 -0.0217 0.1254  0.3514  438 ILE B O   
7756  C CB  . ILE B 438 ? 0.6126 0.7284 2.2543 0.0097  0.1249  0.2799  438 ILE B CB  
7757  C CG1 . ILE B 438 ? 0.5828 0.7230 2.2149 0.0292  0.1279  0.2546  438 ILE B CG1 
7758  C CG2 . ILE B 438 ? 0.6195 0.6873 2.2697 0.0002  0.1181  0.2665  438 ILE B CG2 
7759  C CD1 . ILE B 438 ? 0.5473 0.7126 2.1841 0.0270  0.1304  0.2315  438 ILE B CD1 
7760  N N   . GLU B 439 ? 0.7427 0.7588 2.3929 -0.0094 0.1123  0.3399  439 GLU B N   
7761  C CA  . GLU B 439 ? 0.7905 0.7766 2.4534 -0.0322 0.1077  0.3621  439 GLU B CA  
7762  C C   . GLU B 439 ? 0.7694 0.7326 2.4425 -0.0443 0.1033  0.3383  439 GLU B C   
7763  O O   . GLU B 439 ? 0.7383 0.6726 2.4070 -0.0320 0.0992  0.3111  439 GLU B O   
7764  C CB  . GLU B 439 ? 0.8484 0.7832 2.5093 -0.0269 0.1010  0.3828  439 GLU B CB  
7765  C CG  . GLU B 439 ? 0.8761 0.8392 2.5320 -0.0260 0.1051  0.4187  439 GLU B CG  
7766  C CD  . GLU B 439 ? 0.9321 0.8508 2.5843 -0.0162 0.0988  0.4416  439 GLU B CD  
7767  O OE1 . GLU B 439 ? 0.9507 0.8241 2.5987 0.0011  0.0925  0.4251  439 GLU B OE1 
7768  O OE2 . GLU B 439 ? 0.9593 0.8910 2.6128 -0.0254 0.1003  0.4779  439 GLU B OE2 
7769  N N   . THR B 440 ? 0.7743 0.7573 2.4607 -0.0682 0.1046  0.3486  440 THR B N   
7770  C CA  . THR B 440 ? 0.7721 0.7423 2.4688 -0.0810 0.1004  0.3272  440 THR B CA  
7771  C C   . THR B 440 ? 0.8252 0.7321 2.5321 -0.0965 0.0899  0.3344  440 THR B C   
7772  O O   . THR B 440 ? 0.8479 0.7213 2.5538 -0.0963 0.0863  0.3563  440 THR B O   
7773  C CB  . THR B 440 ? 0.7514 0.7805 2.4582 -0.0973 0.1069  0.3317  440 THR B CB  
7774  O OG1 . THR B 440 ? 0.7863 0.8245 2.5040 -0.1193 0.1079  0.3661  440 THR B OG1 
7775  C CG2 . THR B 440 ? 0.7085 0.7971 2.4049 -0.0801 0.1166  0.3231  440 THR B CG2 
7776  N N   . SER B 441 ? 0.8391 0.7293 2.5552 -0.1087 0.0842  0.3147  441 SER B N   
7777  C CA  . SER B 441 ? 0.8965 0.7263 2.6226 -0.1237 0.0730  0.3148  441 SER B CA  
7778  C C   . SER B 441 ? 0.9097 0.7507 2.6486 -0.1429 0.0695  0.2982  441 SER B C   
7779  O O   . SER B 441 ? 0.8766 0.7199 2.6099 -0.1319 0.0684  0.2680  441 SER B O   
7780  C CB  . SER B 441 ? 0.9055 0.6804 2.6203 -0.1022 0.0663  0.2950  441 SER B CB  
7781  O OG  . SER B 441 ? 0.9603 0.6749 2.6840 -0.1149 0.0545  0.2902  441 SER B OG  
7782  N N   . GLU B 442 ? 0.9772 0.8278 2.7337 -0.1718 0.0679  0.3188  442 GLU B N   
7783  C CA  . GLU B 442 ? 0.9979 0.8738 2.7682 -0.1908 0.0659  0.3057  442 GLU B CA  
7784  C C   . GLU B 442 ? 1.0527 0.8839 2.8206 -0.1861 0.0555  0.2722  442 GLU B C   
7785  O O   . GLU B 442 ? 1.1484 0.9200 2.9105 -0.1783 0.0478  0.2663  442 GLU B O   
7786  C CB  . GLU B 442 ? 1.0142 0.8975 2.8060 -0.2251 0.0633  0.3326  442 GLU B CB  
7787  C CG  . GLU B 442 ? 1.0594 0.8707 2.8599 -0.2409 0.0510  0.3427  442 GLU B CG  
7788  C CD  . GLU B 442 ? 1.0742 0.8922 2.8989 -0.2784 0.0467  0.3641  442 GLU B CD  
7789  O OE1 . GLU B 442 ? 1.0396 0.9221 2.8739 -0.2908 0.0540  0.3699  442 GLU B OE1 
7790  O OE2 . GLU B 442 ? 1.1104 0.8702 2.9452 -0.2952 0.0360  0.3741  442 GLU B OE2 
7791  N N   . ASN B 443 ? 1.0357 0.8990 2.8076 -0.1895 0.0556  0.2506  443 ASN B N   
7792  C CA  . ASN B 443 ? 1.0417 0.8779 2.8095 -0.1832 0.0473  0.2171  443 ASN B CA  
7793  C C   . ASN B 443 ? 0.9901 0.8253 2.7370 -0.1507 0.0517  0.1961  443 ASN B C   
7794  O O   . ASN B 443 ? 1.0225 0.8521 2.7636 -0.1423 0.0478  0.1687  443 ASN B O   
7795  C CB  . ASN B 443 ? 1.1169 0.8902 2.8931 -0.1995 0.0334  0.2124  443 ASN B CB  
7796  C CG  . ASN B 443 ? 1.1862 0.8975 2.9524 -0.1855 0.0289  0.2152  443 ASN B CG  
7797  O OD1 . ASN B 443 ? 1.1901 0.8857 2.9392 -0.1589 0.0299  0.1962  443 ASN B OD1 
7798  N ND2 . ASN B 443 ? 1.2227 0.8971 3.0000 -0.2030 0.0232  0.2388  443 ASN B ND2 
7799  N N   . PHE B 444 ? 0.9303 0.7741 2.6660 -0.1331 0.0597  0.2090  444 PHE B N   
7800  C CA  . PHE B 444 ? 0.8465 0.7062 2.5654 -0.1053 0.0658  0.1922  444 PHE B CA  
7801  C C   . PHE B 444 ? 0.7997 0.7249 2.5193 -0.1028 0.0765  0.1996  444 PHE B C   
7802  O O   . PHE B 444 ? 0.7748 0.7220 2.4949 -0.1040 0.0828  0.2231  444 PHE B O   
7803  C CB  . PHE B 444 ? 0.8474 0.6761 2.5530 -0.0849 0.0669  0.1975  444 PHE B CB  
7804  C CG  . PHE B 444 ? 0.8683 0.6338 2.5695 -0.0785 0.0570  0.1833  444 PHE B CG  
7805  C CD1 . PHE B 444 ? 0.9145 0.6337 2.6248 -0.0932 0.0487  0.1971  444 PHE B CD1 
7806  C CD2 . PHE B 444 ? 0.8363 0.5893 2.5247 -0.0578 0.0559  0.1562  444 PHE B CD2 
7807  C CE1 . PHE B 444 ? 0.9438 0.6047 2.6501 -0.0858 0.0392  0.1814  444 PHE B CE1 
7808  C CE2 . PHE B 444 ? 0.8619 0.5613 2.5459 -0.0506 0.0472  0.1415  444 PHE B CE2 
7809  C CZ  . PHE B 444 ? 0.9203 0.5733 2.6131 -0.0638 0.0387  0.1529  444 PHE B CZ  
7810  N N   . THR B 445 ? 0.7734 0.7287 2.4929 -0.0987 0.0780  0.1793  445 THR B N   
7811  C CA  . THR B 445 ? 0.7276 0.7434 2.4484 -0.0943 0.0870  0.1809  445 THR B CA  
7812  C C   . THR B 445 ? 0.6658 0.6897 2.3704 -0.0677 0.0925  0.1685  445 THR B C   
7813  O O   . THR B 445 ? 0.6464 0.6488 2.3428 -0.0553 0.0891  0.1470  445 THR B O   
7814  C CB  . THR B 445 ? 0.7401 0.7822 2.4714 -0.1042 0.0843  0.1666  445 THR B CB  
7815  O OG1 . THR B 445 ? 0.7844 0.7837 2.5157 -0.1088 0.0742  0.1498  445 THR B OG1 
7816  C CG2 . THR B 445 ? 0.7529 0.8283 2.5028 -0.1288 0.0853  0.1851  445 THR B CG2 
7817  N N   . LEU B 446 ? 0.6432 0.6989 2.3435 -0.0599 0.1006  0.1824  446 LEU B N   
7818  C CA  . LEU B 446 ? 0.6159 0.6877 2.3031 -0.0368 0.1060  0.1712  446 LEU B CA  
7819  C C   . LEU B 446 ? 0.6059 0.7118 2.2952 -0.0317 0.1081  0.1525  446 LEU B C   
7820  O O   . LEU B 446 ? 0.6161 0.7409 2.3173 -0.0455 0.1067  0.1522  446 LEU B O   
7821  C CB  . LEU B 446 ? 0.5931 0.6964 2.2762 -0.0319 0.1134  0.1902  446 LEU B CB  
7822  C CG  . LEU B 446 ? 0.6126 0.6891 2.2941 -0.0367 0.1119  0.2140  446 LEU B CG  
7823  C CD1 . LEU B 446 ? 0.6035 0.7229 2.2814 -0.0335 0.1197  0.2338  446 LEU B CD1 
7824  C CD2 . LEU B 446 ? 0.6173 0.6457 2.2881 -0.0217 0.1071  0.2041  446 LEU B CD2 
7825  N N   . LEU B 447 ? 0.5915 0.7079 2.2709 -0.0125 0.1113  0.1377  447 LEU B N   
7826  C CA  . LEU B 447 ? 0.5948 0.7431 2.2781 -0.0085 0.1128  0.1228  447 LEU B CA  
7827  C C   . LEU B 447 ? 0.6144 0.7877 2.2894 0.0102  0.1183  0.1136  447 LEU B C   
7828  O O   . LEU B 447 ? 0.6288 0.7941 2.2944 0.0202  0.1204  0.1171  447 LEU B O   
7829  C CB  . LEU B 447 ? 0.5758 0.6989 2.2607 -0.0108 0.1059  0.1059  447 LEU B CB  
7830  C CG  . LEU B 447 ? 0.5664 0.6462 2.2397 -0.0001 0.1018  0.0935  447 LEU B CG  
7831  C CD1 . LEU B 447 ? 0.5560 0.6465 2.2208 0.0183  0.1047  0.0788  447 LEU B CD1 
7832  C CD2 . LEU B 447 ? 0.5680 0.6227 2.2449 -0.0097 0.0939  0.0837  447 LEU B CD2 
7833  N N   . ASP B 448 ? 0.6719 0.8791 2.3521 0.0139  0.1203  0.1033  448 ASP B N   
7834  C CA  . ASP B 448 ? 0.7225 0.9511 2.3971 0.0313  0.1238  0.0902  448 ASP B CA  
7835  C C   . ASP B 448 ? 0.7090 0.9547 2.3763 0.0383  0.1291  0.0994  448 ASP B C   
7836  O O   . ASP B 448 ? 0.7618 1.0417 2.4333 0.0326  0.1337  0.1128  448 ASP B O   
7837  C CB  . ASP B 448 ? 0.7842 0.9829 2.4518 0.0422  0.1198  0.0725  448 ASP B CB  
7838  C CG  . ASP B 448 ? 0.8398 1.0381 2.5136 0.0405  0.1156  0.0603  448 ASP B CG  
7839  O OD1 . ASP B 448 ? 0.9830 1.1709 2.6631 0.0271  0.1116  0.0645  448 ASP B OD1 
7840  O OD2 . ASP B 448 ? 0.8121 1.0205 2.4847 0.0524  0.1158  0.0471  448 ASP B OD2 
7841  N N   . ASP B 449 ? 0.6508 0.8752 2.3076 0.0506  0.1284  0.0922  449 ASP B N   
7842  C CA  . ASP B 449 ? 0.6427 0.8869 2.2918 0.0616  0.1324  0.0935  449 ASP B CA  
7843  C C   . ASP B 449 ? 0.5952 0.8058 2.2360 0.0643  0.1304  0.1006  449 ASP B C   
7844  O O   . ASP B 449 ? 0.5343 0.7111 2.1719 0.0682  0.1266  0.0912  449 ASP B O   
7845  C CB  . ASP B 449 ? 0.6675 0.9288 2.3144 0.0759  0.1332  0.0734  449 ASP B CB  
7846  C CG  . ASP B 449 ? 0.7032 1.0018 2.3579 0.0778  0.1353  0.0650  449 ASP B CG  
7847  O OD1 . ASP B 449 ? 0.7415 1.0587 2.4048 0.0671  0.1367  0.0744  449 ASP B OD1 
7848  O OD2 . ASP B 449 ? 0.6446 0.9547 2.2979 0.0902  0.1354  0.0485  449 ASP B OD2 
7849  N N   . LEU B 450 ? 0.5831 0.8042 2.2213 0.0610  0.1329  0.1195  450 LEU B N   
7850  C CA  . LEU B 450 ? 0.5589 0.7695 2.1879 0.0698  0.1328  0.1260  450 LEU B CA  
7851  C C   . LEU B 450 ? 0.5109 0.7351 2.1338 0.0848  0.1335  0.1077  450 LEU B C   
7852  O O   . LEU B 450 ? 0.4990 0.7591 2.1228 0.0886  0.1365  0.1001  450 LEU B O   
7853  C CB  . LEU B 450 ? 0.5936 0.8335 2.2213 0.0653  0.1367  0.1482  450 LEU B CB  
7854  C CG  . LEU B 450 ? 0.6218 0.8700 2.2391 0.0767  0.1376  0.1552  450 LEU B CG  
7855  C CD1 . LEU B 450 ? 0.6444 0.8467 2.2584 0.0795  0.1330  0.1616  450 LEU B CD1 
7856  C CD2 . LEU B 450 ? 0.6442 0.9314 2.2593 0.0728  0.1422  0.1768  450 LEU B CD2 
7857  N N   . LYS B 451 ? 0.5030 0.7003 2.1204 0.0932  0.1307  0.1012  451 LYS B N   
7858  C CA  . LYS B 451 ? 0.4788 0.6869 2.0917 0.1057  0.1306  0.0853  451 LYS B CA  
7859  C C   . LYS B 451 ? 0.4682 0.6787 2.0736 0.1137  0.1304  0.0939  451 LYS B C   
7860  O O   . LYS B 451 ? 0.4848 0.6685 2.0884 0.1135  0.1285  0.1050  451 LYS B O   
7861  C CB  . LYS B 451 ? 0.4740 0.6541 2.0885 0.1083  0.1275  0.0686  451 LYS B CB  
7862  C CG  . LYS B 451 ? 0.4616 0.6449 2.0827 0.1039  0.1271  0.0572  451 LYS B CG  
7863  C CD  . LYS B 451 ? 0.4653 0.6209 2.0869 0.1060  0.1239  0.0440  451 LYS B CD  
7864  C CE  . LYS B 451 ? 0.4771 0.6347 2.1050 0.1017  0.1227  0.0360  451 LYS B CE  
7865  N NZ  . LYS B 451 ? 0.4968 0.6258 2.1237 0.1017  0.1194  0.0283  451 LYS B NZ  
7866  N N   . ILE B 452 ? 0.4427 0.6860 2.0442 0.1217  0.1319  0.0875  452 ILE B N   
7867  C CA  . ILE B 452 ? 0.4431 0.6969 2.0376 0.1302  0.1312  0.0940  452 ILE B CA  
7868  C C   . ILE B 452 ? 0.4208 0.6743 2.0146 0.1391  0.1288  0.0743  452 ILE B C   
7869  O O   . ILE B 452 ? 0.4004 0.6605 1.9978 0.1392  0.1286  0.0567  452 ILE B O   
7870  C CB  . ILE B 452 ? 0.4540 0.7516 2.0439 0.1310  0.1344  0.1042  452 ILE B CB  
7871  C CG1 . ILE B 452 ? 0.4883 0.7843 2.0781 0.1223  0.1364  0.1307  452 ILE B CG1 
7872  C CG2 . ILE B 452 ? 0.4550 0.7750 2.0375 0.1421  0.1331  0.1021  452 ILE B CG2 
7873  C CD1 . ILE B 452 ? 0.4937 0.7752 2.0920 0.1093  0.1375  0.1341  452 ILE B CD1 
7874  N N   . SER B 453 ? 0.4068 0.6538 1.9968 0.1464  0.1267  0.0780  453 SER B N   
7875  C CA  . SER B 453 ? 0.3870 0.6359 1.9777 0.1533  0.1243  0.0614  453 SER B CA  
7876  C C   . SER B 453 ? 0.3859 0.6554 1.9714 0.1621  0.1227  0.0675  453 SER B C   
7877  O O   . SER B 453 ? 0.4132 0.6695 1.9962 0.1656  0.1220  0.0829  453 SER B O   
7878  C CB  . SER B 453 ? 0.3859 0.5989 1.9803 0.1528  0.1228  0.0558  453 SER B CB  
7879  O OG  . SER B 453 ? 0.3871 0.6051 1.9832 0.1584  0.1208  0.0429  453 SER B OG  
7880  N N   . TYR B 454 ? 0.3682 0.6686 1.9527 0.1662  0.1214  0.0545  454 TYR B N   
7881  C CA  . TYR B 454 ? 0.3680 0.6914 1.9483 0.1747  0.1189  0.0577  454 TYR B CA  
7882  C C   . TYR B 454 ? 0.3604 0.6810 1.9464 0.1769  0.1156  0.0393  454 TYR B C   
7883  O O   . TYR B 454 ? 0.3691 0.7094 1.9572 0.1760  0.1138  0.0221  454 TYR B O   
7884  C CB  . TYR B 454 ? 0.3689 0.7366 1.9425 0.1774  0.1192  0.0584  454 TYR B CB  
7885  C CG  . TYR B 454 ? 0.3774 0.7728 1.9446 0.1863  0.1165  0.0676  454 TYR B CG  
7886  C CD1 . TYR B 454 ? 0.3917 0.7812 1.9539 0.1901  0.1170  0.0929  454 TYR B CD1 
7887  C CD2 . TYR B 454 ? 0.3664 0.7948 1.9323 0.1911  0.1128  0.0516  454 TYR B CD2 
7888  C CE1 . TYR B 454 ? 0.3941 0.8103 1.9503 0.1996  0.1141  0.1028  454 TYR B CE1 
7889  C CE2 . TYR B 454 ? 0.3716 0.8293 1.9314 0.1995  0.1098  0.0601  454 TYR B CE2 
7890  C CZ  . TYR B 454 ? 0.3806 0.8331 1.9352 0.2044  0.1106  0.0865  454 TYR B CZ  
7891  O OH  . TYR B 454 ? 0.3846 0.8672 1.9331 0.2140  0.1072  0.0963  454 TYR B OH  
7892  N N   . ASN B 455 ? 0.3530 0.6493 1.9421 0.1795  0.1148  0.0427  455 ASN B N   
7893  C CA  . ASN B 455 ? 0.3376 0.6279 1.9339 0.1788  0.1128  0.0268  455 ASN B CA  
7894  C C   . ASN B 455 ? 0.3308 0.6477 1.9280 0.1858  0.1093  0.0243  455 ASN B C   
7895  O O   . ASN B 455 ? 0.3300 0.6439 1.9263 0.1933  0.1088  0.0353  455 ASN B O   
7896  C CB  . ASN B 455 ? 0.3363 0.5907 1.9359 0.1778  0.1142  0.0291  455 ASN B CB  
7897  C CG  . ASN B 455 ? 0.3269 0.5783 1.9343 0.1753  0.1130  0.0143  455 ASN B CG  
7898  O OD1 . ASN B 455 ? 0.3157 0.5904 1.9266 0.1773  0.1103  0.0069  455 ASN B OD1 
7899  N ND2 . ASN B 455 ? 0.3229 0.5474 1.9330 0.1701  0.1146  0.0103  455 ASN B ND2 
7900  N N   . THR B 456 ? 0.3165 0.6583 1.9169 0.1833  0.1063  0.0082  456 THR B N   
7901  C CA  . THR B 456 ? 0.3229 0.6994 1.9227 0.1892  0.1022  0.0060  456 THR B CA  
7902  C C   . THR B 456 ? 0.3178 0.6942 1.9272 0.1889  0.0997  -0.0022 456 THR B C   
7903  O O   . THR B 456 ? 0.3228 0.7295 1.9340 0.1929  0.0956  -0.0053 456 THR B O   
7904  C CB  . THR B 456 ? 0.3256 0.7325 1.9228 0.1871  0.0996  -0.0079 456 THR B CB  
7905  O OG1 . THR B 456 ? 0.3241 0.7121 1.9281 0.1787  0.0997  -0.0243 456 THR B OG1 
7906  C CG2 . THR B 456 ? 0.3305 0.7535 1.9167 0.1905  0.1022  0.0043  456 THR B CG2 
7907  N N   . HIS B 457 ? 0.3096 0.6558 1.9254 0.1839  0.1020  -0.0052 457 HIS B N   
7908  C CA  . HIS B 457 ? 0.2992 0.6446 1.9234 0.1847  0.1013  -0.0074 457 HIS B CA  
7909  C C   . HIS B 457 ? 0.2914 0.6615 1.9253 0.1784  0.0965  -0.0235 457 HIS B C   
7910  O O   . HIS B 457 ? 0.2987 0.6848 1.9396 0.1806  0.0949  -0.0236 457 HIS B O   
7911  C CB  . HIS B 457 ? 0.3114 0.6666 1.9324 0.1974  0.1013  0.0074  457 HIS B CB  
7912  C CG  . HIS B 457 ? 0.3171 0.6398 1.9339 0.2029  0.1052  0.0203  457 HIS B CG  
7913  N ND1 . HIS B 457 ? 0.3265 0.6304 1.9347 0.2041  0.1072  0.0320  457 HIS B ND1 
7914  C CD2 . HIS B 457 ? 0.3178 0.6243 1.9383 0.2070  0.1072  0.0220  457 HIS B CD2 
7915  C CE1 . HIS B 457 ? 0.3378 0.6119 1.9451 0.2084  0.1095  0.0395  457 HIS B CE1 
7916  N NE2 . HIS B 457 ? 0.3292 0.6053 1.9431 0.2113  0.1096  0.0330  457 HIS B NE2 
7917  N N   . LEU B 458 ? 0.2882 0.6613 1.9232 0.1708  0.0941  -0.0373 458 LEU B N   
7918  C CA  . LEU B 458 ? 0.2909 0.6798 1.9362 0.1624  0.0887  -0.0550 458 LEU B CA  
7919  C C   . LEU B 458 ? 0.3054 0.6659 1.9605 0.1522  0.0900  -0.0603 458 LEU B C   
7920  O O   . LEU B 458 ? 0.3143 0.6528 1.9692 0.1470  0.0907  -0.0664 458 LEU B O   
7921  C CB  . LEU B 458 ? 0.2853 0.6884 1.9269 0.1607  0.0848  -0.0688 458 LEU B CB  
7922  C CG  . LEU B 458 ? 0.2848 0.7151 1.9136 0.1704  0.0847  -0.0621 458 LEU B CG  
7923  C CD1 . LEU B 458 ? 0.2869 0.7290 1.9117 0.1689  0.0821  -0.0776 458 LEU B CD1 
7924  C CD2 . LEU B 458 ? 0.2881 0.7544 1.9168 0.1765  0.0807  -0.0587 458 LEU B CD2 
7925  N N   . GLY B 459 ? 0.3157 0.6794 1.9798 0.1497  0.0905  -0.0574 459 GLY B N   
7926  C CA  . GLY B 459 ? 0.3310 0.6705 2.0031 0.1406  0.0927  -0.0584 459 GLY B CA  
7927  C C   . GLY B 459 ? 0.3446 0.6511 2.0083 0.1437  0.0986  -0.0490 459 GLY B C   
7928  O O   . GLY B 459 ? 0.3917 0.6950 2.0466 0.1536  0.1020  -0.0376 459 GLY B O   
7929  N N   . TRP B 460 ? 0.3306 0.6122 1.9973 0.1353  0.0990  -0.0537 460 TRP B N   
7930  C CA  . TRP B 460 ? 0.3283 0.5814 1.9875 0.1375  0.1036  -0.0462 460 TRP B CA  
7931  C C   . TRP B 460 ? 0.3153 0.5618 1.9665 0.1405  0.1033  -0.0481 460 TRP B C   
7932  O O   . TRP B 460 ? 0.3053 0.5301 1.9515 0.1409  0.1062  -0.0433 460 TRP B O   
7933  C CB  . TRP B 460 ? 0.3437 0.5755 2.0094 0.1282  0.1043  -0.0480 460 TRP B CB  
7934  C CG  . TRP B 460 ? 0.3682 0.6079 2.0413 0.1247  0.1061  -0.0439 460 TRP B CG  
7935  C CD1 . TRP B 460 ? 0.3931 0.6425 2.0789 0.1141  0.1032  -0.0489 460 TRP B CD1 
7936  C CD2 . TRP B 460 ? 0.3965 0.6374 2.0653 0.1319  0.1111  -0.0340 460 TRP B CD2 
7937  N NE1 . TRP B 460 ? 0.3955 0.6553 2.0854 0.1138  0.1069  -0.0415 460 TRP B NE1 
7938  C CE2 . TRP B 460 ? 0.4070 0.6625 2.0860 0.1259  0.1117  -0.0334 460 TRP B CE2 
7939  C CE3 . TRP B 460 ? 0.4285 0.6594 2.0862 0.1429  0.1147  -0.0263 460 TRP B CE3 
7940  C CZ2 . TRP B 460 ? 0.4390 0.7028 2.1168 0.1322  0.1165  -0.0261 460 TRP B CZ2 
7941  C CZ3 . TRP B 460 ? 0.4454 0.6802 2.1019 0.1495  0.1185  -0.0203 460 TRP B CZ3 
7942  C CH2 . TRP B 460 ? 0.4457 0.6984 2.1118 0.1451  0.1197  -0.0206 460 TRP B CH2 
7943  N N   . ALA B 461 ? 0.3081 0.5764 1.9585 0.1422  0.0997  -0.0557 461 ALA B N   
7944  C CA  . ALA B 461 ? 0.3020 0.5711 1.9458 0.1449  0.0995  -0.0589 461 ALA B CA  
7945  C C   . ALA B 461 ? 0.3050 0.5755 1.9381 0.1527  0.1037  -0.0437 461 ALA B C   
7946  O O   . ALA B 461 ? 0.3057 0.5959 1.9348 0.1588  0.1034  -0.0367 461 ALA B O   
7947  C CB  . ALA B 461 ? 0.3009 0.5961 1.9467 0.1449  0.0942  -0.0732 461 ALA B CB  
7948  N N   . ILE B 462 ? 0.3123 0.5621 1.9413 0.1520  0.1069  -0.0382 462 ILE B N   
7949  C CA  . ILE B 462 ? 0.3094 0.5546 1.9301 0.1567  0.1104  -0.0230 462 ILE B CA  
7950  C C   . ILE B 462 ? 0.3171 0.5856 1.9317 0.1598  0.1104  -0.0213 462 ILE B C   
7951  O O   . ILE B 462 ? 0.3418 0.6079 1.9503 0.1619  0.1131  -0.0075 462 ILE B O   
7952  C CB  . ILE B 462 ? 0.2998 0.5154 1.9195 0.1532  0.1132  -0.0180 462 ILE B CB  
7953  C CG1 . ILE B 462 ? 0.3067 0.5207 1.9280 0.1494  0.1129  -0.0259 462 ILE B CG1 
7954  C CG2 . ILE B 462 ? 0.2933 0.4891 1.9172 0.1507  0.1137  -0.0193 462 ILE B CG2 
7955  C CD1 . ILE B 462 ? 0.3171 0.5126 1.9357 0.1470  0.1156  -0.0177 462 ILE B CD1 
7956  N N   . GLY B 463 ? 0.3155 0.6067 1.9322 0.1597  0.1071  -0.0352 463 GLY B N   
7957  C CA  . GLY B 463 ? 0.3296 0.6506 1.9396 0.1640  0.1070  -0.0349 463 GLY B CA  
7958  C C   . GLY B 463 ? 0.3460 0.6615 1.9526 0.1628  0.1108  -0.0295 463 GLY B C   
7959  O O   . GLY B 463 ? 0.3376 0.6285 1.9485 0.1584  0.1119  -0.0322 463 GLY B O   
7960  N N   . SER B 464 ? 0.3673 0.7080 1.9661 0.1663  0.1128  -0.0203 464 SER B N   
7961  C CA  . SER B 464 ? 0.3760 0.7223 1.9729 0.1647  0.1163  -0.0177 464 SER B CA  
7962  C C   . SER B 464 ? 0.3630 0.6815 1.9605 0.1597  0.1199  -0.0006 464 SER B C   
7963  O O   . SER B 464 ? 0.3873 0.6868 1.9837 0.1596  0.1199  0.0114  464 SER B O   
7964  C CB  . SER B 464 ? 0.4019 0.7884 1.9906 0.1694  0.1176  -0.0133 464 SER B CB  
7965  O OG  . SER B 464 ? 0.4344 0.8459 2.0230 0.1739  0.1133  -0.0335 464 SER B OG  
7966  N N   . GLN B 465 ? 0.3328 0.6499 1.9328 0.1562  0.1221  -0.0024 465 GLN B N   
7967  C CA  . GLN B 465 ? 0.3270 0.6254 1.9282 0.1500  0.1251  0.0119  465 GLN B CA  
7968  C C   . GLN B 465 ? 0.3245 0.6501 1.9251 0.1485  0.1285  0.0151  465 GLN B C   
7969  O O   . GLN B 465 ? 0.3196 0.6762 1.9187 0.1536  0.1285  0.0036  465 GLN B O   
7970  C CB  . GLN B 465 ? 0.3262 0.5923 1.9341 0.1459  0.1238  0.0037  465 GLN B CB  
7971  C CG  . GLN B 465 ? 0.3498 0.5869 1.9581 0.1456  0.1220  0.0059  465 GLN B CG  
7972  C CD  . GLN B 465 ? 0.3803 0.5872 1.9930 0.1409  0.1215  0.0032  465 GLN B CD  
7973  O OE1 . GLN B 465 ? 0.4355 0.6264 2.0475 0.1363  0.1226  0.0136  465 GLN B OE1 
7974  N NE2 . GLN B 465 ? 0.3920 0.5905 2.0091 0.1414  0.1192  -0.0104 465 GLN B NE2 
7975  N N   . ALA B 466 ? 0.3187 0.6343 1.9211 0.1412  0.1311  0.0300  466 ALA B N   
7976  C CA  . ALA B 466 ? 0.3130 0.6560 1.9170 0.1381  0.1348  0.0346  466 ALA B CA  
7977  C C   . ALA B 466 ? 0.3166 0.6362 1.9265 0.1279  0.1358  0.0457  466 ALA B C   
7978  O O   . ALA B 466 ? 0.3225 0.6127 1.9315 0.1233  0.1345  0.0576  466 ALA B O   
7979  C CB  . ALA B 466 ? 0.3183 0.6964 1.9149 0.1395  0.1379  0.0495  466 ALA B CB  
7980  N N   . SER B 467 ? 0.3126 0.6455 1.9290 0.1255  0.1372  0.0394  467 SER B N   
7981  C CA  . SER B 467 ? 0.3183 0.6445 1.9411 0.1146  0.1386  0.0515  467 SER B CA  
7982  C C   . SER B 467 ? 0.3270 0.6940 1.9499 0.1104  0.1436  0.0659  467 SER B C   
7983  O O   . SER B 467 ? 0.3277 0.7333 1.9478 0.1180  0.1462  0.0586  467 SER B O   
7984  C CB  . SER B 467 ? 0.3133 0.6313 1.9444 0.1144  0.1367  0.0371  467 SER B CB  
7985  O OG  . SER B 467 ? 0.3150 0.5930 1.9464 0.1144  0.1325  0.0302  467 SER B OG  
7986  N N   . VAL B 468 ? 0.3395 0.6989 1.9656 0.0980  0.1449  0.0863  468 VAL B N   
7987  C CA  . VAL B 468 ? 0.3489 0.7471 1.9758 0.0915  0.1500  0.1040  468 VAL B CA  
7988  C C   . VAL B 468 ? 0.3551 0.7475 1.9935 0.0771  0.1502  0.1129  468 VAL B C   
7989  O O   . VAL B 468 ? 0.3546 0.7061 1.9959 0.0683  0.1463  0.1192  468 VAL B O   
7990  C CB  . VAL B 468 ? 0.3599 0.7591 1.9787 0.0895  0.1511  0.1264  468 VAL B CB  
7991  C CG1 . VAL B 468 ? 0.3660 0.8088 1.9854 0.0819  0.1569  0.1474  468 VAL B CG1 
7992  C CG2 . VAL B 468 ? 0.3562 0.7611 1.9642 0.1038  0.1498  0.1163  468 VAL B CG2 
7993  N N   . SER B 469 ? 0.3634 0.7978 2.0085 0.0760  0.1541  0.1102  469 SER B N   
7994  C CA  . SER B 469 ? 0.3693 0.8114 2.0267 0.0611  0.1550  0.1208  469 SER B CA  
7995  C C   . SER B 469 ? 0.4009 0.8448 2.0582 0.0465  0.1573  0.1503  469 SER B C   
7996  O O   . SER B 469 ? 0.3972 0.8686 2.0467 0.0502  0.1614  0.1618  469 SER B O   
7997  C CB  . SER B 469 ? 0.3606 0.8540 2.0251 0.0657  0.1593  0.1113  469 SER B CB  
7998  O OG  . SER B 469 ? 0.3660 0.8778 2.0438 0.0504  0.1610  0.1239  469 SER B OG  
7999  N N   . ILE B 470 ? 0.4374 0.8501 2.1032 0.0303  0.1538  0.1620  470 ILE B N   
8000  C CA  . ILE B 470 ? 0.4955 0.9092 2.1645 0.0137  0.1553  0.1913  470 ILE B CA  
8001  C C   . ILE B 470 ? 0.5169 0.9565 2.2018 -0.0038 0.1571  0.2007  470 ILE B C   
8002  O O   . ILE B 470 ? 0.5398 0.9738 2.2310 -0.0217 0.1570  0.2250  470 ILE B O   
8003  C CB  . ILE B 470 ? 0.5251 0.8780 2.1910 0.0083  0.1490  0.2000  470 ILE B CB  
8004  C CG1 . ILE B 470 ? 0.5414 0.8525 2.2143 0.0030  0.1423  0.1851  470 ILE B CG1 
8005  C CG2 . ILE B 470 ? 0.5153 0.8528 2.1665 0.0253  0.1483  0.1951  470 ILE B CG2 
8006  C CD1 . ILE B 470 ? 0.5708 0.8231 2.2411 -0.0017 0.1359  0.1915  470 ILE B CD1 
8007  N N   . SER B 471 ? 0.5328 1.0022 2.2246 0.0015  0.1584  0.1825  471 SER B N   
8008  C CA  . SER B 471 ? 0.5558 1.0538 2.2642 -0.0135 0.1596  0.1880  471 SER B CA  
8009  C C   . SER B 471 ? 0.6002 1.1371 2.3144 -0.0294 0.1657  0.2175  471 SER B C   
8010  O O   . SER B 471 ? 0.6167 1.1444 2.3432 -0.0513 0.1636  0.2350  471 SER B O   
8011  C CB  . SER B 471 ? 0.5290 1.0651 2.2420 0.0001  0.1617  0.1655  471 SER B CB  
8012  O OG  . SER B 471 ? 0.5250 1.0879 2.2262 0.0201  0.1661  0.1544  471 SER B OG  
8013  N N   . ASP B 472 ? 0.6235 1.2032 2.3283 -0.0191 0.1728  0.2234  472 ASP B N   
8014  C CA  . ASP B 472 ? 0.6698 1.2981 2.3791 -0.0323 0.1800  0.2512  472 ASP B CA  
8015  C C   . ASP B 472 ? 0.7205 1.3138 2.4285 -0.0495 0.1778  0.2821  472 ASP B C   
8016  O O   . ASP B 472 ? 0.7639 1.3909 2.4778 -0.0651 0.1829  0.3099  472 ASP B O   
8017  C CB  . ASP B 472 ? 0.6755 1.3621 2.3735 -0.0146 0.1880  0.2466  472 ASP B CB  
8018  C CG  . ASP B 472 ? 0.7213 1.3900 2.3998 0.0011  0.1872  0.2442  472 ASP B CG  
8019  O OD1 . ASP B 472 ? 0.7251 1.3331 2.3979 0.0038  0.1802  0.2388  472 ASP B OD1 
8020  O OD2 . ASP B 472 ? 0.7828 1.5023 2.4520 0.0106  0.1937  0.2481  472 ASP B OD2 
8021  N N   . GLN B 473 ? 0.7443 1.2714 2.4454 -0.0468 0.1703  0.2781  473 GLN B N   
8022  C CA  . GLN B 473 ? 0.7886 1.2790 2.4859 -0.0571 0.1676  0.3050  473 GLN B CA  
8023  C C   . GLN B 473 ? 0.8506 1.2768 2.5577 -0.0732 0.1585  0.3076  473 GLN B C   
8024  O O   . GLN B 473 ? 0.8902 1.2742 2.5942 -0.0792 0.1544  0.3257  473 GLN B O   
8025  C CB  . GLN B 473 ? 0.7658 1.2347 2.4443 -0.0367 0.1664  0.2993  473 GLN B CB  
8026  C CG  . GLN B 473 ? 0.7421 1.2671 2.4083 -0.0242 0.1740  0.3066  473 GLN B CG  
8027  C CD  . GLN B 473 ? 0.7328 1.2322 2.3830 -0.0102 0.1715  0.3109  473 GLN B CD  
8028  O OE1 . GLN B 473 ? 0.7289 1.1885 2.3785 -0.0181 0.1674  0.3326  473 GLN B OE1 
8029  N NE2 . GLN B 473 ? 0.7112 1.2318 2.3489 0.0109  0.1730  0.2900  473 GLN B NE2 
8030  N N   . LEU B 474 ? 0.8803 1.2990 2.5991 -0.0796 0.1547  0.2896  474 LEU B N   
8031  C CA  . LEU B 474 ? 0.9123 1.2709 2.6388 -0.0926 0.1452  0.2866  474 LEU B CA  
8032  C C   . LEU B 474 ? 0.9073 1.2512 2.6453 -0.1188 0.1430  0.3186  474 LEU B C   
8033  O O   . LEU B 474 ? 0.8975 1.1817 2.6352 -0.1251 0.1354  0.3239  474 LEU B O   
8034  C CB  . LEU B 474 ? 0.9401 1.3025 2.6773 -0.0954 0.1415  0.2629  474 LEU B CB  
8035  C CG  . LEU B 474 ? 0.9139 1.2500 2.6415 -0.0750 0.1375  0.2307  474 LEU B CG  
8036  C CD1 . LEU B 474 ? 0.9101 1.1836 2.6254 -0.0661 0.1315  0.2251  474 LEU B CD1 
8037  C CD2 . LEU B 474 ? 0.8877 1.2675 2.6070 -0.0534 0.1441  0.2154  474 LEU B CD2 
8038  N N   . ASP B 475 ? 0.8766 1.2750 2.6253 -0.1340 0.1497  0.3400  475 ASP B N   
8039  C CA  . ASP B 475 ? 0.8990 1.2873 2.6614 -0.1621 0.1478  0.3722  475 ASP B CA  
8040  C C   . ASP B 475 ? 0.9369 1.2861 2.6889 -0.1608 0.1460  0.3963  475 ASP B C   
8041  O O   . ASP B 475 ? 0.9921 1.2994 2.7535 -0.1808 0.1397  0.4167  475 ASP B O   
8042  C CB  . ASP B 475 ? 0.8718 1.3336 2.6474 -0.1777 0.1565  0.3916  475 ASP B CB  
8043  C CG  . ASP B 475 ? 0.8576 1.3786 2.6218 -0.1663 0.1676  0.4077  475 ASP B CG  
8044  O OD1 . ASP B 475 ? 0.8489 1.3580 2.5939 -0.1440 0.1687  0.4010  475 ASP B OD1 
8045  O OD2 . ASP B 475 ? 0.8832 1.4658 2.6579 -0.1799 0.1752  0.4265  475 ASP B OD2 
8046  N N   . LYS B 476 ? 0.8817 1.2444 2.6150 -0.1373 0.1508  0.3940  476 LYS B N   
8047  C CA  . LYS B 476 ? 0.8696 1.2145 2.5931 -0.1351 0.1510  0.4216  476 LYS B CA  
8048  C C   . LYS B 476 ? 0.8529 1.1158 2.5729 -0.1317 0.1404  0.4169  476 LYS B C   
8049  O O   . LYS B 476 ? 0.8137 1.0425 2.5327 -0.1231 0.1347  0.3870  476 LYS B O   
8050  C CB  . LYS B 476 ? 0.8618 1.2489 2.5664 -0.1103 0.1584  0.4176  476 LYS B CB  
8051  C CG  . LYS B 476 ? 0.8608 1.3319 2.5662 -0.1104 0.1693  0.4224  476 LYS B CG  
8052  C CD  . LYS B 476 ? 0.8567 1.3671 2.5428 -0.0838 0.1751  0.4102  476 LYS B CD  
8053  C CE  . LYS B 476 ? 0.8879 1.3933 2.5604 -0.0778 0.1757  0.4363  476 LYS B CE  
8054  N NZ  . LYS B 476 ? 0.8618 1.4089 2.5163 -0.0531 0.1805  0.4222  476 LYS B NZ  
8055  N N   . LYS B 477 ? 0.8744 1.1088 2.5926 -0.1378 0.1379  0.4477  477 LYS B N   
8056  C CA  . LYS B 477 ? 0.8643 1.0216 2.5795 -0.1334 0.1278  0.4474  477 LYS B CA  
8057  C C   . LYS B 477 ? 0.8233 0.9721 2.5186 -0.1027 0.1283  0.4334  477 LYS B C   
8058  O O   . LYS B 477 ? 0.8305 0.9270 2.5213 -0.0905 0.1212  0.4131  477 LYS B O   
8059  C CB  . LYS B 477 ? 0.9027 1.0320 2.6263 -0.1534 0.1242  0.4877  477 LYS B CB  
8060  C CG  . LYS B 477 ? 0.9283 1.0568 2.6742 -0.1866 0.1216  0.5005  477 LYS B CG  
8061  C CD  . LYS B 477 ? 0.9823 1.0762 2.7389 -0.2093 0.1167  0.5410  477 LYS B CD  
8062  C CE  . LYS B 477 ? 0.9848 1.1353 2.7385 -0.2149 0.1263  0.5794  477 LYS B CE  
8063  N NZ  . LYS B 477 ? 1.0371 1.1428 2.7940 -0.2262 0.1207  0.6180  477 LYS B NZ  
8064  N N   . ILE B 478 ? 0.7861 0.9894 2.4697 -0.0904 0.1366  0.4433  478 ILE B N   
8065  C CA  . ILE B 478 ? 0.7479 0.9553 2.4137 -0.0620 0.1376  0.4266  478 ILE B CA  
8066  C C   . ILE B 478 ? 0.6924 0.9620 2.3526 -0.0508 0.1455  0.4029  478 ILE B C   
8067  O O   . ILE B 478 ? 0.6844 1.0148 2.3442 -0.0553 0.1534  0.4160  478 ILE B O   
8068  C CB  . ILE B 478 ? 0.7645 0.9737 2.4196 -0.0541 0.1382  0.4573  478 ILE B CB  
8069  C CG1 . ILE B 478 ? 0.8055 0.9466 2.4671 -0.0635 0.1293  0.4803  478 ILE B CG1 
8070  C CG2 . ILE B 478 ? 0.7351 0.9559 2.3728 -0.0254 0.1391  0.4395  478 ILE B CG2 
8071  C CD1 . ILE B 478 ? 0.8334 0.9788 2.4872 -0.0596 0.1297  0.5178  478 ILE B CD1 
8072  N N   . ILE B 479 ? 0.6508 0.9040 2.3071 -0.0360 0.1429  0.3676  479 ILE B N   
8073  C CA  . ILE B 479 ? 0.6019 0.9015 2.2521 -0.0219 0.1483  0.3415  479 ILE B CA  
8074  C C   . ILE B 479 ? 0.5791 0.8849 2.2129 0.0016  0.1488  0.3339  479 ILE B C   
8075  O O   . ILE B 479 ? 0.5820 0.8411 2.2111 0.0116  0.1428  0.3265  479 ILE B O   
8076  C CB  . ILE B 479 ? 0.5870 0.8638 2.2437 -0.0209 0.1447  0.3093  479 ILE B CB  
8077  C CG1 . ILE B 479 ? 0.6040 0.8599 2.2773 -0.0441 0.1412  0.3154  479 ILE B CG1 
8078  C CG2 . ILE B 479 ? 0.5553 0.8812 2.2086 -0.0087 0.1501  0.2847  479 ILE B CG2 
8079  C CD1 . ILE B 479 ? 0.5874 0.8192 2.2658 -0.0427 0.1365  0.2850  479 ILE B CD1 
8080  N N   . THR B 480 ? 0.5523 0.9177 2.1776 0.0105  0.1555  0.3343  480 THR B N   
8081  C CA  . THR B 480 ? 0.5384 0.9166 2.1487 0.0313  0.1555  0.3273  480 THR B CA  
8082  C C   . THR B 480 ? 0.5061 0.9239 2.1120 0.0444  0.1590  0.2960  480 THR B C   
8083  O O   . THR B 480 ? 0.4914 0.9388 2.1044 0.0382  0.1629  0.2865  480 THR B O   
8084  C CB  . THR B 480 ? 0.5544 0.9667 2.1560 0.0320  0.1590  0.3587  480 THR B CB  
8085  O OG1 . THR B 480 ? 0.5357 1.0163 2.1334 0.0349  0.1665  0.3523  480 THR B OG1 
8086  C CG2 . THR B 480 ? 0.5893 0.9790 2.1990 0.0127  0.1578  0.3953  480 THR B CG2 
8087  N N   . SER B 481 ? 0.5057 0.9252 2.1002 0.0628  0.1571  0.2814  481 SER B N   
8088  C CA  . SER B 481 ? 0.4826 0.9277 2.0730 0.0764  0.1582  0.2495  481 SER B CA  
8089  C C   . SER B 481 ? 0.4839 0.9399 2.0613 0.0935  0.1562  0.2439  481 SER B C   
8090  O O   . SER B 481 ? 0.5001 0.9179 2.0750 0.0984  0.1512  0.2486  481 SER B O   
8091  C CB  . SER B 481 ? 0.4650 0.8704 2.0634 0.0763  0.1543  0.2240  481 SER B CB  
8092  O OG  . SER B 481 ? 0.4439 0.8658 2.0383 0.0901  0.1540  0.1946  481 SER B OG  
8093  N N   . GLU B 482 ? 0.4775 0.9867 2.0471 0.1031  0.1596  0.2324  482 GLU B N   
8094  C CA  . GLU B 482 ? 0.4838 1.0115 2.0414 0.1187  0.1573  0.2245  482 GLU B CA  
8095  C C   . GLU B 482 ? 0.4592 0.9958 2.0170 0.1290  0.1557  0.1873  482 GLU B C   
8096  O O   . GLU B 482 ? 0.4595 1.0185 2.0219 0.1272  0.1590  0.1727  482 GLU B O   
8097  C CB  . GLU B 482 ? 0.5022 1.0870 2.0491 0.1207  0.1618  0.2451  482 GLU B CB  
8098  C CG  . GLU B 482 ? 0.5007 1.1122 2.0340 0.1366  0.1589  0.2392  482 GLU B CG  
8099  C CD  . GLU B 482 ? 0.5195 1.1859 2.0411 0.1379  0.1630  0.2647  482 GLU B CD  
8100  O OE1 . GLU B 482 ? 0.5344 1.2471 2.0550 0.1335  0.1695  0.2670  482 GLU B OE1 
8101  O OE2 . GLU B 482 ? 0.5286 1.1938 2.0420 0.1438  0.1598  0.2835  482 GLU B OE2 
8102  N N   . ASN B 483 ? 0.4567 0.9752 2.0108 0.1395  0.1504  0.1725  483 ASN B N   
8103  C CA  . ASN B 483 ? 0.4436 0.9615 1.9999 0.1471  0.1478  0.1386  483 ASN B CA  
8104  C C   . ASN B 483 ? 0.4374 0.9730 1.9847 0.1596  0.1438  0.1293  483 ASN B C   
8105  O O   . ASN B 483 ? 0.4646 0.9888 2.0076 0.1622  0.1414  0.1463  483 ASN B O   
8106  C CB  . ASN B 483 ? 0.4428 0.9071 2.0095 0.1425  0.1448  0.1270  483 ASN B CB  
8107  C CG  . ASN B 483 ? 0.4565 0.9098 2.0323 0.1304  0.1481  0.1331  483 ASN B CG  
8108  O OD1 . ASN B 483 ? 0.4330 0.8989 2.0141 0.1304  0.1495  0.1150  483 ASN B OD1 
8109  N ND2 . ASN B 483 ? 0.4793 0.9109 2.0577 0.1203  0.1488  0.1585  483 ASN B ND2 
8110  N N   . PHE B 484 ? 0.4230 0.9856 1.9684 0.1672  0.1424  0.1020  484 PHE B N   
8111  C CA  . PHE B 484 ? 0.4157 1.0061 1.9525 0.1780  0.1384  0.0908  484 PHE B CA  
8112  C C   . PHE B 484 ? 0.4131 0.9805 1.9562 0.1819  0.1326  0.0610  484 PHE B C   
8113  O O   . PHE B 484 ? 0.4240 0.9742 1.9754 0.1792  0.1326  0.0421  484 PHE B O   
8114  C CB  . PHE B 484 ? 0.4072 1.0579 1.9350 0.1828  0.1419  0.0865  484 PHE B CB  
8115  C CG  . PHE B 484 ? 0.4117 1.0922 1.9315 0.1793  0.1472  0.1197  484 PHE B CG  
8116  C CD1 . PHE B 484 ? 0.4215 1.1208 1.9308 0.1844  0.1454  0.1394  484 PHE B CD1 
8117  C CD2 . PHE B 484 ? 0.4086 1.1002 1.9323 0.1706  0.1539  0.1324  484 PHE B CD2 
8118  C CE1 . PHE B 484 ? 0.4387 1.1647 1.9407 0.1806  0.1501  0.1722  484 PHE B CE1 
8119  C CE2 . PHE B 484 ? 0.4224 1.1421 1.9399 0.1655  0.1589  0.1648  484 PHE B CE2 
8120  C CZ  . PHE B 484 ? 0.4381 1.1734 1.9445 0.1704  0.1570  0.1854  484 PHE B CZ  
8121  N N   . PHE B 485 ? 0.4066 0.9763 1.9463 0.1881  0.1274  0.0573  485 PHE B N   
8122  C CA  . PHE B 485 ? 0.3949 0.9474 1.9414 0.1902  0.1218  0.0310  485 PHE B CA  
8123  C C   . PHE B 485 ? 0.4061 0.9916 1.9461 0.1983  0.1163  0.0219  485 PHE B C   
8124  O O   . PHE B 485 ? 0.4212 1.0190 1.9546 0.2023  0.1154  0.0412  485 PHE B O   
8125  C CB  . PHE B 485 ? 0.3910 0.8929 1.9458 0.1860  0.1204  0.0376  485 PHE B CB  
8126  C CG  . PHE B 485 ? 0.3874 0.8564 1.9474 0.1778  0.1250  0.0503  485 PHE B CG  
8127  C CD1 . PHE B 485 ? 0.4022 0.8656 1.9587 0.1747  0.1282  0.0783  485 PHE B CD1 
8128  C CD2 . PHE B 485 ? 0.3787 0.8228 1.9475 0.1729  0.1253  0.0344  485 PHE B CD2 
8129  C CE1 . PHE B 485 ? 0.4069 0.8409 1.9692 0.1658  0.1314  0.0884  485 PHE B CE1 
8130  C CE2 . PHE B 485 ? 0.3839 0.8010 1.9575 0.1652  0.1286  0.0453  485 PHE B CE2 
8131  C CZ  . PHE B 485 ? 0.3944 0.8069 1.9650 0.1612  0.1315  0.0713  485 PHE B CZ  
8132  N N   . ASN B 486 ? 0.4057 1.0037 1.9486 0.2006  0.1120  -0.0079 486 ASN B N   
8133  C CA  . ASN B 486 ? 0.4298 1.0536 1.9699 0.2061  0.1051  -0.0223 486 ASN B CA  
8134  C C   . ASN B 486 ? 0.4130 1.0070 1.9606 0.2044  0.1015  -0.0163 486 ASN B C   
8135  O O   . ASN B 486 ? 0.4064 0.9574 1.9640 0.1984  0.1026  -0.0173 486 ASN B O   
8136  C CB  . ASN B 486 ? 0.4509 1.0834 1.9956 0.2067  0.1004  -0.0572 486 ASN B CB  
8137  C CG  . ASN B 486 ? 0.4853 1.1507 2.0230 0.2110  0.1036  -0.0672 486 ASN B CG  
8138  O OD1 . ASN B 486 ? 0.5179 1.1651 2.0618 0.2087  0.1064  -0.0767 486 ASN B OD1 
8139  N ND2 . ASN B 486 ? 0.5097 1.2266 2.0342 0.2183  0.1031  -0.0655 486 ASN B ND2 
8140  N N   . ILE B 487 ? 0.4059 1.0259 1.9485 0.2103  0.0972  -0.0103 487 ILE B N   
8141  C CA  . ILE B 487 ? 0.3982 0.9969 1.9477 0.2108  0.0942  -0.0027 487 ILE B CA  
8142  C C   . ILE B 487 ? 0.3870 1.0005 1.9435 0.2102  0.0864  -0.0280 487 ILE B C   
8143  O O   . ILE B 487 ? 0.4010 1.0565 1.9513 0.2159  0.0814  -0.0329 487 ILE B O   
8144  C CB  . ILE B 487 ? 0.4122 1.0261 1.9532 0.2187  0.0946  0.0259  487 ILE B CB  
8145  C CG1 . ILE B 487 ? 0.4233 1.0223 1.9581 0.2178  0.1015  0.0539  487 ILE B CG1 
8146  C CG2 . ILE B 487 ? 0.4102 1.0043 1.9597 0.2212  0.0912  0.0303  487 ILE B CG2 
8147  C CD1 . ILE B 487 ? 0.4403 1.0503 1.9674 0.2259  0.1010  0.0837  487 ILE B CD1 
8148  N N   . PRO B 488 ? 0.3592 0.9400 1.9292 0.2029  0.0846  -0.0427 488 PRO B N   
8149  C CA  . PRO B 488 ? 0.3497 0.9436 1.9285 0.2000  0.0769  -0.0647 488 PRO B CA  
8150  C C   . PRO B 488 ? 0.3515 0.9777 1.9275 0.2071  0.0726  -0.0546 488 PRO B C   
8151  O O   . PRO B 488 ? 0.3561 0.9777 1.9276 0.2134  0.0759  -0.0295 488 PRO B O   
8152  C CB  . PRO B 488 ? 0.3396 0.8889 1.9330 0.1912  0.0777  -0.0698 488 PRO B CB  
8153  C CG  . PRO B 488 ? 0.3348 0.8500 1.9259 0.1892  0.0851  -0.0595 488 PRO B CG  
8154  C CD  . PRO B 488 ? 0.3451 0.8771 1.9227 0.1966  0.0896  -0.0372 488 PRO B CD  
8155  N N   . ASP B 489 ? 0.3491 1.0067 1.9289 0.2059  0.0644  -0.0749 489 ASP B N   
8156  C CA  . ASP B 489 ? 0.3437 1.0380 1.9224 0.2124  0.0589  -0.0688 489 ASP B CA  
8157  C C   . ASP B 489 ? 0.3316 1.0089 1.9257 0.2085  0.0570  -0.0671 489 ASP B C   
8158  O O   . ASP B 489 ? 0.3380 1.0440 1.9336 0.2146  0.0528  -0.0603 489 ASP B O   
8159  C CB  . ASP B 489 ? 0.3456 1.0873 1.9205 0.2130  0.0503  -0.0918 489 ASP B CB  
8160  C CG  . ASP B 489 ? 0.3507 1.1234 1.9079 0.2202  0.0519  -0.0916 489 ASP B CG  
8161  O OD1 . ASP B 489 ? 0.3447 1.1040 1.8928 0.2240  0.0601  -0.0703 489 ASP B OD1 
8162  O OD2 . ASP B 489 ? 0.3554 1.1677 1.9082 0.2215  0.0448  -0.1128 489 ASP B OD2 
8163  N N   . ASN B 490 ? 0.3213 0.9561 1.9270 0.1988  0.0601  -0.0735 490 ASN B N   
8164  C CA  . ASN B 490 ? 0.3159 0.9333 1.9358 0.1946  0.0601  -0.0704 490 ASN B CA  
8165  C C   . ASN B 490 ? 0.3081 0.8834 1.9268 0.1971  0.0686  -0.0505 490 ASN B C   
8166  O O   . ASN B 490 ? 0.2968 0.8496 1.9264 0.1929  0.0705  -0.0491 490 ASN B O   
8167  C CB  . ASN B 490 ? 0.3148 0.9210 1.9502 0.1801  0.0557  -0.0941 490 ASN B CB  
8168  C CG  . ASN B 490 ? 0.3184 0.8850 1.9538 0.1730  0.0597  -0.1017 490 ASN B CG  
8169  O OD1 . ASN B 490 ? 0.3409 0.9047 1.9642 0.1782  0.0632  -0.0981 490 ASN B OD1 
8170  N ND2 . ASN B 490 ? 0.3162 0.8537 1.9653 0.1616  0.0597  -0.1099 490 ASN B ND2 
8171  N N   . CYS B 491 ? 0.3117 0.8784 1.9172 0.2034  0.0736  -0.0358 491 CYS B N   
8172  C CA  . CYS B 491 ? 0.3107 0.8417 1.9132 0.2071  0.0805  -0.0152 491 CYS B CA  
8173  C C   . CYS B 491 ? 0.3263 0.8688 1.9264 0.2195  0.0800  0.0048  491 CYS B C   
8174  O O   . CYS B 491 ? 0.3416 0.9112 1.9317 0.2285  0.0783  0.0171  491 CYS B O   
8175  C CB  . CYS B 491 ? 0.3084 0.8286 1.8991 0.2079  0.0853  -0.0054 491 CYS B CB  
8176  S SG  . CYS B 491 ? 0.3026 0.7790 1.8906 0.2116  0.0921  0.0199  491 CYS B SG  
8177  N N   . TRP B 492 ? 0.3282 0.8510 1.9373 0.2210  0.0814  0.0087  492 TRP B N   
8178  C CA  . TRP B 492 ? 0.3411 0.8774 1.9501 0.2346  0.0800  0.0244  492 TRP B CA  
8179  C C   . TRP B 492 ? 0.3463 0.8484 1.9478 0.2428  0.0849  0.0464  492 TRP B C   
8180  O O   . TRP B 492 ? 0.3578 0.8706 1.9528 0.2554  0.0835  0.0647  492 TRP B O   
8181  C CB  . TRP B 492 ? 0.3385 0.8808 1.9623 0.2334  0.0783  0.0154  492 TRP B CB  
8182  C CG  . TRP B 492 ? 0.3336 0.9033 1.9673 0.2215  0.0730  -0.0069 492 TRP B CG  
8183  C CD1 . TRP B 492 ? 0.3269 0.8845 1.9737 0.2088  0.0734  -0.0215 492 TRP B CD1 
8184  C CD2 . TRP B 492 ? 0.3343 0.9473 1.9658 0.2205  0.0660  -0.0173 492 TRP B CD2 
8185  N NE1 . TRP B 492 ? 0.3190 0.9057 1.9733 0.1991  0.0667  -0.0399 492 TRP B NE1 
8186  C CE2 . TRP B 492 ? 0.3244 0.9455 1.9692 0.2063  0.0619  -0.0393 492 TRP B CE2 
8187  C CE3 . TRP B 492 ? 0.3453 0.9913 1.9646 0.2298  0.0624  -0.0101 492 TRP B CE3 
8188  C CZ2 . TRP B 492 ? 0.3281 0.9872 1.9749 0.2013  0.0538  -0.0564 492 TRP B CZ2 
8189  C CZ3 . TRP B 492 ? 0.3467 1.0338 1.9664 0.2257  0.0550  -0.0270 492 TRP B CZ3 
8190  C CH2 . TRP B 492 ? 0.3391 1.0316 1.9726 0.2116  0.0504  -0.0510 492 TRP B CH2 
8191  N N   . VAL B 493 ? 0.3412 0.8019 1.9440 0.2353  0.0900  0.0445  493 VAL B N   
8192  C CA  . VAL B 493 ? 0.3525 0.7774 1.9486 0.2396  0.0941  0.0624  493 VAL B CA  
8193  C C   . VAL B 493 ? 0.3476 0.7472 1.9411 0.2270  0.0980  0.0568  493 VAL B C   
8194  O O   . VAL B 493 ? 0.3188 0.7187 1.9177 0.2166  0.0981  0.0385  493 VAL B O   
8195  C CB  . VAL B 493 ? 0.3544 0.7534 1.9566 0.2471  0.0956  0.0665  493 VAL B CB  
8196  C CG1 . VAL B 493 ? 0.3416 0.7217 1.9525 0.2365  0.0983  0.0497  493 VAL B CG1 
8197  C CG2 . VAL B 493 ? 0.3703 0.7339 1.9659 0.2545  0.0978  0.0858  493 VAL B CG2 
8198  N N   . VAL B 494 ? 0.3646 0.7436 1.9503 0.2282  0.1007  0.0738  494 VAL B N   
8199  C CA  . VAL B 494 ? 0.3650 0.7199 1.9489 0.2173  0.1046  0.0719  494 VAL B CA  
8200  C C   . VAL B 494 ? 0.3737 0.6853 1.9572 0.2186  0.1071  0.0849  494 VAL B C   
8201  O O   . VAL B 494 ? 0.3987 0.7016 1.9818 0.2294  0.1056  0.0968  494 VAL B O   
8202  C CB  . VAL B 494 ? 0.3765 0.7569 1.9520 0.2146  0.1051  0.0780  494 VAL B CB  
8203  C CG1 . VAL B 494 ? 0.3998 0.7851 1.9670 0.2226  0.1049  0.1040  494 VAL B CG1 
8204  C CG2 . VAL B 494 ? 0.3727 0.7377 1.9483 0.2032  0.1089  0.0715  494 VAL B CG2 
8205  N N   . ASN B 495 ? 0.3645 0.6498 1.9493 0.2083  0.1102  0.0798  495 ASN B N   
8206  C CA  . ASN B 495 ? 0.3711 0.6162 1.9550 0.2062  0.1121  0.0901  495 ASN B CA  
8207  C C   . ASN B 495 ? 0.3785 0.6210 1.9598 0.1950  0.1146  0.0942  495 ASN B C   
8208  O O   . ASN B 495 ? 0.3645 0.5969 1.9492 0.1859  0.1164  0.0819  495 ASN B O   
8209  C CB  . ASN B 495 ? 0.3578 0.5747 1.9474 0.2046  0.1129  0.0775  495 ASN B CB  
8210  C CG  . ASN B 495 ? 0.3699 0.5465 1.9583 0.2015  0.1140  0.0851  495 ASN B CG  
8211  O OD1 . ASN B 495 ? 0.3883 0.5585 1.9741 0.1940  0.1149  0.0944  495 ASN B OD1 
8212  N ND2 . ASN B 495 ? 0.3731 0.5244 1.9636 0.2067  0.1137  0.0809  495 ASN B ND2 
8213  N N   . ALA B 496 ? 0.4039 0.6586 1.9794 0.1962  0.1147  0.1129  496 ALA B N   
8214  C CA  . ALA B 496 ? 0.4129 0.6684 1.9863 0.1861  0.1176  0.1216  496 ALA B CA  
8215  C C   . ALA B 496 ? 0.4344 0.6459 2.0108 0.1797  0.1182  0.1297  496 ALA B C   
8216  O O   . ALA B 496 ? 0.4545 0.6421 2.0300 0.1846  0.1162  0.1447  496 ALA B O   
8217  C CB  . ALA B 496 ? 0.4249 0.7097 1.9911 0.1893  0.1177  0.1415  496 ALA B CB  
8218  N N   . SER B 497 ? 0.4362 0.6372 2.0166 0.1692  0.1201  0.1187  497 SER B N   
8219  C CA  . SER B 497 ? 0.4631 0.6249 2.0470 0.1619  0.1199  0.1222  497 SER B CA  
8220  C C   . SER B 497 ? 0.4594 0.6289 2.0459 0.1488  0.1226  0.1230  497 SER B C   
8221  O O   . SER B 497 ? 0.4568 0.6544 2.0439 0.1467  0.1246  0.1114  497 SER B O   
8222  C CB  . SER B 497 ? 0.4714 0.6088 2.0586 0.1645  0.1187  0.1049  497 SER B CB  
8223  O OG  . SER B 497 ? 0.4637 0.6203 2.0532 0.1630  0.1199  0.0860  497 SER B OG  
8224  N N   . ALA B 498 ? 0.4688 0.6133 2.0577 0.1401  0.1222  0.1362  498 ALA B N   
8225  C CA  . ALA B 498 ? 0.4622 0.6115 2.0557 0.1267  0.1243  0.1366  498 ALA B CA  
8226  C C   . ALA B 498 ? 0.4781 0.5849 2.0764 0.1189  0.1215  0.1366  498 ALA B C   
8227  O O   . ALA B 498 ? 0.4762 0.5510 2.0732 0.1240  0.1183  0.1409  498 ALA B O   
8228  C CB  . ALA B 498 ? 0.4769 0.6542 2.0689 0.1211  0.1269  0.1569  498 ALA B CB  
8229  N N   . GLY B 499 ? 0.4802 0.5881 2.0841 0.1076  0.1224  0.1301  499 GLY B N   
8230  C CA  . GLY B 499 ? 0.4951 0.5663 2.1036 0.0993  0.1191  0.1277  499 GLY B CA  
8231  C C   . GLY B 499 ? 0.4783 0.5607 2.0937 0.0866  0.1200  0.1223  499 GLY B C   
8232  O O   . GLY B 499 ? 0.4618 0.5761 2.0780 0.0881  0.1231  0.1136  499 GLY B O   
8233  N N   . ILE B 500 ? 0.4951 0.5506 2.1159 0.0749  0.1167  0.1266  500 ILE B N   
8234  C CA  . ILE B 500 ? 0.4885 0.5547 2.1176 0.0612  0.1167  0.1242  500 ILE B CA  
8235  C C   . ILE B 500 ? 0.5106 0.5384 2.1430 0.0537  0.1109  0.1170  500 ILE B C   
8236  O O   . ILE B 500 ? 0.5363 0.5284 2.1668 0.0543  0.1069  0.1216  500 ILE B O   
8237  C CB  . ILE B 500 ? 0.4900 0.5817 2.1247 0.0492  0.1196  0.1450  500 ILE B CB  
8238  C CG1 . ILE B 500 ? 0.4733 0.5904 2.1173 0.0377  0.1210  0.1407  500 ILE B CG1 
8239  C CG2 . ILE B 500 ? 0.5288 0.5892 2.1659 0.0400  0.1161  0.1650  500 ILE B CG2 
8240  C CD1 . ILE B 500 ? 0.4763 0.6280 2.1265 0.0261  0.1252  0.1607  500 ILE B CD1 
8241  N N   . SER B 501 ? 0.5185 0.5548 2.1559 0.0475  0.1099  0.1048  501 SER B N   
8242  C CA  . SER B 501 ? 0.5474 0.5533 2.1869 0.0414  0.1040  0.0943  501 SER B CA  
8243  C C   . SER B 501 ? 0.5870 0.5828 2.2362 0.0226  0.1005  0.1069  501 SER B C   
8244  O O   . SER B 501 ? 0.5926 0.6189 2.2499 0.0120  0.1033  0.1172  501 SER B O   
8245  C CB  . SER B 501 ? 0.5262 0.5471 2.1663 0.0440  0.1040  0.0768  501 SER B CB  
8246  O OG  . SER B 501 ? 0.5054 0.5285 2.1373 0.0596  0.1061  0.0655  501 SER B OG  
8247  N N   . VAL B 502 ? 0.6162 0.5700 2.2651 0.0185  0.0941  0.1052  502 VAL B N   
8248  C CA  . VAL B 502 ? 0.6385 0.5751 2.2975 -0.0006 0.0892  0.1169  502 VAL B CA  
8249  C C   . VAL B 502 ? 0.6437 0.5548 2.3046 -0.0071 0.0815  0.0995  502 VAL B C   
8250  O O   . VAL B 502 ? 0.6413 0.5331 2.2931 0.0054  0.0792  0.0822  502 VAL B O   
8251  C CB  . VAL B 502 ? 0.6824 0.5872 2.3404 -0.0012 0.0870  0.1344  502 VAL B CB  
8252  C CG1 . VAL B 502 ? 0.7239 0.6116 2.3944 -0.0236 0.0818  0.1489  502 VAL B CG1 
8253  C CG2 . VAL B 502 ? 0.6837 0.6139 2.3372 0.0079  0.0940  0.1509  502 VAL B CG2 
8254  N N   . ARG B 503 ? 0.6646 0.5783 2.3377 -0.0273 0.0775  0.1047  503 ARG B N   
8255  C CA  . ARG B 503 ? 0.6777 0.5763 2.3540 -0.0356 0.0698  0.0877  503 ARG B CA  
8256  C C   . ARG B 503 ? 0.6959 0.5623 2.3826 -0.0557 0.0618  0.0963  503 ARG B C   
8257  O O   . ARG B 503 ? 0.7009 0.5809 2.3994 -0.0722 0.0632  0.1166  503 ARG B O   
8258  C CB  . ARG B 503 ? 0.6651 0.6078 2.3481 -0.0413 0.0718  0.0819  503 ARG B CB  
8259  C CG  . ARG B 503 ? 0.7002 0.6343 2.3854 -0.0483 0.0637  0.0636  503 ARG B CG  
8260  C CD  . ARG B 503 ? 0.7072 0.6851 2.4028 -0.0572 0.0641  0.0613  503 ARG B CD  
8261  N NE  . ARG B 503 ? 0.6903 0.6992 2.3794 -0.0403 0.0701  0.0534  503 ARG B NE  
8262  C CZ  . ARG B 503 ? 0.6914 0.6928 2.3688 -0.0250 0.0692  0.0370  503 ARG B CZ  
8263  N NH1 . ARG B 503 ? 0.6997 0.6664 2.3686 -0.0222 0.0631  0.0243  503 ARG B NH1 
8264  N NH2 . ARG B 503 ? 0.6901 0.7199 2.3646 -0.0123 0.0745  0.0333  503 ARG B NH2 
8265  N N   . TYR B 504 ? 0.6831 0.5075 2.3655 -0.0544 0.0532  0.0801  504 TYR B N   
8266  C CA  . TYR B 504 ? 0.6918 0.4877 2.3853 -0.0752 0.0431  0.0791  504 TYR B CA  
8267  C C   . TYR B 504 ? 0.6751 0.4761 2.3668 -0.0769 0.0369  0.0540  504 TYR B C   
8268  O O   . TYR B 504 ? 0.6670 0.4553 2.3450 -0.0596 0.0358  0.0347  504 TYR B O   
8269  C CB  . TYR B 504 ? 0.7225 0.4614 2.4133 -0.0727 0.0370  0.0821  504 TYR B CB  
8270  C CG  . TYR B 504 ? 0.7525 0.4568 2.4568 -0.0964 0.0258  0.0839  504 TYR B CG  
8271  C CD1 . TYR B 504 ? 0.7642 0.4442 2.4674 -0.1003 0.0155  0.0589  504 TYR B CD1 
8272  C CD2 . TYR B 504 ? 0.7727 0.4704 2.4911 -0.1160 0.0251  0.1107  504 TYR B CD2 
8273  C CE1 . TYR B 504 ? 0.8048 0.4534 2.5213 -0.1233 0.0042  0.0584  504 TYR B CE1 
8274  C CE2 . TYR B 504 ? 0.8136 0.4789 2.5463 -0.1401 0.0142  0.1129  504 TYR B CE2 
8275  C CZ  . TYR B 504 ? 0.8288 0.4683 2.5609 -0.1440 0.0033  0.0856  504 TYR B CZ  
8276  O OH  . TYR B 504 ? 0.8648 0.4705 2.6110 -0.1679 -0.0088 0.0839  504 TYR B OH  
8277  N N   . GLY B 505 ? 0.6653 0.4893 2.3709 -0.0975 0.0331  0.0551  505 GLY B N   
8278  C CA  . GLY B 505 ? 0.6527 0.4847 2.3576 -0.1006 0.0261  0.0328  505 GLY B CA  
8279  C C   . GLY B 505 ? 0.6063 0.4624 2.2965 -0.0780 0.0318  0.0186  505 GLY B C   
8280  O O   . GLY B 505 ? 0.5645 0.4612 2.2565 -0.0730 0.0398  0.0264  505 GLY B O   
8281  N N   . LYS B 506 ? 0.6107 0.4415 2.2868 -0.0645 0.0275  -0.0019 506 LYS B N   
8282  C CA  . LYS B 506 ? 0.5828 0.4330 2.2448 -0.0442 0.0323  -0.0143 506 LYS B CA  
8283  C C   . LYS B 506 ? 0.5720 0.4098 2.2218 -0.0235 0.0401  -0.0104 506 LYS B C   
8284  O O   . LYS B 506 ? 0.5399 0.3975 2.1802 -0.0078 0.0459  -0.0155 506 LYS B O   
8285  C CB  . LYS B 506 ? 0.5973 0.4354 2.2492 -0.0397 0.0242  -0.0386 506 LYS B CB  
8286  C CG  . LYS B 506 ? 0.6028 0.4637 2.2630 -0.0548 0.0167  -0.0467 506 LYS B CG  
8287  C CD  . LYS B 506 ? 0.6206 0.4741 2.2681 -0.0480 0.0091  -0.0710 506 LYS B CD  
8288  C CE  . LYS B 506 ? 0.6431 0.5133 2.3012 -0.0669 -0.0009 -0.0786 506 LYS B CE  
8289  N NZ  . LYS B 506 ? 0.6738 0.5290 2.3211 -0.0650 -0.0111 -0.1030 506 LYS B NZ  
8290  N N   . PHE B 507 ? 0.5925 0.3979 2.2435 -0.0240 0.0397  -0.0007 507 PHE B N   
8291  C CA  . PHE B 507 ? 0.5845 0.3763 2.2249 -0.0045 0.0456  0.0023  507 PHE B CA  
8292  C C   . PHE B 507 ? 0.5595 0.3814 2.2036 -0.0017 0.0553  0.0220  507 PHE B C   
8293  O O   . PHE B 507 ? 0.5613 0.3882 2.2163 -0.0153 0.0562  0.0403  507 PHE B O   
8294  C CB  . PHE B 507 ? 0.6253 0.3678 2.2664 -0.0065 0.0388  0.0026  507 PHE B CB  
8295  C CG  . PHE B 507 ? 0.6347 0.3552 2.2668 0.0129  0.0425  0.0061  507 PHE B CG  
8296  C CD1 . PHE B 507 ? 0.6315 0.3558 2.2676 0.0143  0.0481  0.0287  507 PHE B CD1 
8297  C CD2 . PHE B 507 ? 0.6522 0.3495 2.2722 0.0299  0.0397  -0.0133 507 PHE B CD2 
8298  C CE1 . PHE B 507 ? 0.6454 0.3511 2.2741 0.0325  0.0505  0.0319  507 PHE B CE1 
8299  C CE2 . PHE B 507 ? 0.6645 0.3440 2.2776 0.0484  0.0427  -0.0104 507 PHE B CE2 
8300  C CZ  . PHE B 507 ? 0.6628 0.3462 2.2806 0.0497  0.0478  0.0123  507 PHE B CZ  
8301  N N   . THR B 508 ? 0.5258 0.3677 2.1604 0.0156  0.0623  0.0180  508 THR B N   
8302  C CA  . THR B 508 ? 0.5091 0.3770 2.1450 0.0212  0.0708  0.0330  508 THR B CA  
8303  C C   . THR B 508 ? 0.5161 0.3674 2.1426 0.0386  0.0741  0.0346  508 THR B C   
8304  O O   . THR B 508 ? 0.5222 0.3576 2.1393 0.0511  0.0726  0.0203  508 THR B O   
8305  C CB  . THR B 508 ? 0.4852 0.3922 2.1207 0.0253  0.0755  0.0277  508 THR B CB  
8306  O OG1 . THR B 508 ? 0.4881 0.3863 2.1140 0.0347  0.0729  0.0097  508 THR B OG1 
8307  C CG2 . THR B 508 ? 0.4828 0.4156 2.1304 0.0092  0.0740  0.0321  508 THR B CG2 
8308  N N   . PHE B 509 ? 0.5182 0.3774 2.1473 0.0398  0.0787  0.0523  509 PHE B N   
8309  C CA  . PHE B 509 ? 0.5201 0.3708 2.1414 0.0567  0.0819  0.0554  509 PHE B CA  
8310  C C   . PHE B 509 ? 0.5143 0.3943 2.1381 0.0576  0.0884  0.0729  509 PHE B C   
8311  O O   . PHE B 509 ? 0.5043 0.4092 2.1357 0.0453  0.0904  0.0823  509 PHE B O   
8312  C CB  . PHE B 509 ? 0.5606 0.3671 2.1809 0.0588  0.0760  0.0577  509 PHE B CB  
8313  C CG  . PHE B 509 ? 0.5858 0.3777 2.2155 0.0443  0.0732  0.0784  509 PHE B CG  
8314  C CD1 . PHE B 509 ? 0.6013 0.3819 2.2405 0.0242  0.0675  0.0795  509 PHE B CD1 
8315  C CD2 . PHE B 509 ? 0.5933 0.3829 2.2226 0.0502  0.0759  0.0976  509 PHE B CD2 
8316  C CE1 . PHE B 509 ? 0.6308 0.3973 2.2797 0.0091  0.0648  0.1003  509 PHE B CE1 
8317  C CE2 . PHE B 509 ? 0.6221 0.3975 2.2599 0.0363  0.0732  0.1192  509 PHE B CE2 
8318  C CZ  . PHE B 509 ? 0.6412 0.4050 2.2892 0.0151  0.0680  0.1210  509 PHE B CZ  
8319  N N   . LYS B 510 ? 0.5243 0.4037 2.1417 0.0727  0.0914  0.0765  510 LYS B N   
8320  C CA  . LYS B 510 ? 0.5262 0.4365 2.1438 0.0762  0.0972  0.0901  510 LYS B CA  
8321  C C   . LYS B 510 ? 0.5566 0.4499 2.1733 0.0804  0.0962  0.1079  510 LYS B C   
8322  O O   . LYS B 510 ? 0.5871 0.4523 2.1992 0.0918  0.0932  0.1039  510 LYS B O   
8323  C CB  . LYS B 510 ? 0.4999 0.4341 2.1115 0.0900  0.1016  0.0781  510 LYS B CB  
8324  C CG  . LYS B 510 ? 0.4775 0.4326 2.0909 0.0859  0.1030  0.0649  510 LYS B CG  
8325  C CD  . LYS B 510 ? 0.4666 0.4468 2.0763 0.0969  0.1073  0.0565  510 LYS B CD  
8326  C CE  . LYS B 510 ? 0.4586 0.4722 2.0703 0.0975  0.1116  0.0650  510 LYS B CE  
8327  N NZ  . LYS B 510 ? 0.4483 0.4860 2.0660 0.0884  0.1130  0.0643  510 LYS B NZ  
8328  N N   . ILE B 511 ? 0.5664 0.4792 2.1873 0.0720  0.0987  0.1279  511 ILE B N   
8329  C CA  . ILE B 511 ? 0.5945 0.5014 2.2136 0.0774  0.0988  0.1480  511 ILE B CA  
8330  C C   . ILE B 511 ? 0.5638 0.5121 2.1775 0.0884  0.1049  0.1511  511 ILE B C   
8331  O O   . ILE B 511 ? 0.5309 0.5148 2.1456 0.0850  0.1091  0.1448  511 ILE B O   
8332  C CB  . ILE B 511 ? 0.6298 0.5291 2.2568 0.0598  0.0971  0.1710  511 ILE B CB  
8333  C CG1 . ILE B 511 ? 0.6200 0.5646 2.2525 0.0463  0.1024  0.1779  511 ILE B CG1 
8334  C CG2 . ILE B 511 ? 0.6574 0.5104 2.2903 0.0491  0.0894  0.1663  511 ILE B CG2 
8335  C CD1 . ILE B 511 ? 0.6515 0.5956 2.2929 0.0273  0.1016  0.2027  511 ILE B CD1 
8336  N N   . HIS B 512 ? 0.5638 0.5077 2.1722 0.1019  0.1045  0.1604  512 HIS B N   
8337  C CA  . HIS B 512 ? 0.5201 0.4999 2.1228 0.1146  0.1087  0.1578  512 HIS B CA  
8338  C C   . HIS B 512 ? 0.5235 0.4984 2.1219 0.1273  0.1072  0.1739  512 HIS B C   
8339  O O   . HIS B 512 ? 0.5632 0.5021 2.1630 0.1279  0.1028  0.1854  512 HIS B O   
8340  C CB  . HIS B 512 ? 0.4978 0.4779 2.0982 0.1234  0.1091  0.1328  512 HIS B CB  
8341  C CG  . HIS B 512 ? 0.5170 0.4560 2.1163 0.1303  0.1047  0.1241  512 HIS B CG  
8342  N ND1 . HIS B 512 ? 0.5256 0.4494 2.1214 0.1455  0.1025  0.1281  512 HIS B ND1 
8343  C CD2 . HIS B 512 ? 0.5205 0.4333 2.1213 0.1253  0.1017  0.1104  512 HIS B CD2 
8344  C CE1 . HIS B 512 ? 0.5425 0.4318 2.1378 0.1502  0.0988  0.1162  512 HIS B CE1 
8345  N NE2 . HIS B 512 ? 0.5351 0.4176 2.1328 0.1378  0.0982  0.1049  512 HIS B NE2 
8346  N N   . ASP B 513 ? 0.4931 0.5049 2.0867 0.1372  0.1103  0.1749  513 ASP B N   
8347  C CA  . ASP B 513 ? 0.5049 0.5179 2.0938 0.1521  0.1086  0.1870  513 ASP B CA  
8348  C C   . ASP B 513 ? 0.4756 0.5253 2.0606 0.1640  0.1110  0.1732  513 ASP B C   
8349  O O   . ASP B 513 ? 0.4413 0.5213 2.0265 0.1583  0.1145  0.1621  513 ASP B O   
8350  C CB  . ASP B 513 ? 0.5251 0.5469 2.1130 0.1475  0.1086  0.2161  513 ASP B CB  
8351  C CG  . ASP B 513 ? 0.5514 0.5583 2.1360 0.1625  0.1047  0.2327  513 ASP B CG  
8352  O OD1 . ASP B 513 ? 0.5514 0.5346 2.1358 0.1762  0.1016  0.2206  513 ASP B OD1 
8353  O OD2 . ASP B 513 ? 0.5679 0.5893 2.1499 0.1615  0.1048  0.2579  513 ASP B OD2 
8354  N N   . GLN B 514 ? 0.4827 0.5297 2.0650 0.1805  0.1087  0.1744  514 GLN B N   
8355  C CA  . GLN B 514 ? 0.4604 0.5377 2.0408 0.1915  0.1098  0.1596  514 GLN B CA  
8356  C C   . GLN B 514 ? 0.4819 0.5798 2.0585 0.2053  0.1079  0.1746  514 GLN B C   
8357  O O   . GLN B 514 ? 0.5171 0.5894 2.0932 0.2139  0.1044  0.1892  514 GLN B O   
8358  C CB  . GLN B 514 ? 0.4472 0.5011 2.0303 0.1979  0.1088  0.1400  514 GLN B CB  
8359  C CG  . GLN B 514 ? 0.4197 0.4999 2.0030 0.2094  0.1094  0.1261  514 GLN B CG  
8360  C CD  . GLN B 514 ? 0.4073 0.4668 1.9930 0.2151  0.1092  0.1092  514 GLN B CD  
8361  O OE1 . GLN B 514 ? 0.3774 0.4488 1.9653 0.2109  0.1115  0.0924  514 GLN B OE1 
8362  N NE2 . GLN B 514 ? 0.4286 0.4569 2.0140 0.2252  0.1064  0.1137  514 GLN B NE2 
8363  N N   . LYS B 515 ? 0.4645 0.6079 2.0383 0.2079  0.1095  0.1702  515 LYS B N   
8364  C CA  . LYS B 515 ? 0.4794 0.6490 2.0494 0.2217  0.1071  0.1815  515 LYS B CA  
8365  C C   . LYS B 515 ? 0.4537 0.6558 2.0251 0.2285  0.1070  0.1616  515 LYS B C   
8366  O O   . LYS B 515 ? 0.4231 0.6530 1.9946 0.2207  0.1091  0.1481  515 LYS B O   
8367  C CB  . LYS B 515 ? 0.4921 0.6944 2.0557 0.2193  0.1077  0.2017  515 LYS B CB  
8368  C CG  . LYS B 515 ? 0.5271 0.7064 2.0892 0.2123  0.1076  0.2284  515 LYS B CG  
8369  C CD  . LYS B 515 ? 0.5583 0.6886 2.1230 0.2189  0.1034  0.2437  515 LYS B CD  
8370  C CE  . LYS B 515 ? 0.5869 0.6926 2.1529 0.2044  0.1037  0.2650  515 LYS B CE  
8371  N NZ  . LYS B 515 ? 0.6155 0.6624 2.1872 0.2035  0.0999  0.2668  515 LYS B NZ  
8372  N N   . ILE B 516 ? 0.4609 0.6597 2.0344 0.2434  0.1041  0.1602  516 ILE B N   
8373  C CA  . ILE B 516 ? 0.4453 0.6767 2.0220 0.2499  0.1034  0.1440  516 ILE B CA  
8374  C C   . ILE B 516 ? 0.4542 0.7245 2.0268 0.2606  0.1001  0.1565  516 ILE B C   
8375  O O   . ILE B 516 ? 0.4852 0.7473 2.0563 0.2741  0.0971  0.1732  516 ILE B O   
8376  C CB  . ILE B 516 ? 0.4468 0.6583 2.0296 0.2589  0.1028  0.1323  516 ILE B CB  
8377  C CG1 . ILE B 516 ? 0.4438 0.6203 2.0293 0.2486  0.1057  0.1194  516 ILE B CG1 
8378  C CG2 . ILE B 516 ? 0.4294 0.6798 2.0172 0.2639  0.1019  0.1181  516 ILE B CG2 
8379  C CD1 . ILE B 516 ? 0.4480 0.6072 2.0381 0.2578  0.1058  0.1079  516 ILE B CD1 
8380  N N   . ILE B 517 ? 0.4331 0.7457 2.0040 0.2553  0.1002  0.1470  517 ILE B N   
8381  C CA  . ILE B 517 ? 0.4435 0.7989 2.0085 0.2628  0.0972  0.1581  517 ILE B CA  
8382  C C   . ILE B 517 ? 0.4358 0.8312 2.0051 0.2643  0.0947  0.1376  517 ILE B C   
8383  O O   . ILE B 517 ? 0.4193 0.8209 1.9920 0.2528  0.0964  0.1173  517 ILE B O   
8384  C CB  . ILE B 517 ? 0.4424 0.8143 1.9987 0.2537  0.0993  0.1692  517 ILE B CB  
8385  C CG1 . ILE B 517 ? 0.4594 0.7908 2.0138 0.2476  0.1019  0.1887  517 ILE B CG1 
8386  C CG2 . ILE B 517 ? 0.4522 0.8715 2.0006 0.2630  0.0959  0.1818  517 ILE B CG2 
8387  C CD1 . ILE B 517 ? 0.4539 0.8007 2.0027 0.2349  0.1057  0.1956  517 ILE B CD1 
8388  N N   . TYR B 518 ? 0.4447 0.8663 2.0146 0.2785  0.0902  0.1439  518 TYR B N   
8389  C CA  . TYR B 518 ? 0.4267 0.8892 2.0022 0.2805  0.0867  0.1266  518 TYR B CA  
8390  C C   . TYR B 518 ? 0.4278 0.9398 1.9954 0.2800  0.0834  0.1273  518 TYR B C   
8391  O O   . TYR B 518 ? 0.4483 0.9658 2.0053 0.2802  0.0843  0.1442  518 TYR B O   
8392  C CB  . TYR B 518 ? 0.4398 0.9040 2.0213 0.2972  0.0835  0.1331  518 TYR B CB  
8393  C CG  . TYR B 518 ? 0.4434 0.8625 2.0318 0.3000  0.0866  0.1304  518 TYR B CG  
8394  C CD1 . TYR B 518 ? 0.4243 0.8413 2.0229 0.2939  0.0884  0.1096  518 TYR B CD1 
8395  C CD2 . TYR B 518 ? 0.4695 0.8485 2.0543 0.3086  0.0873  0.1485  518 TYR B CD2 
8396  C CE1 . TYR B 518 ? 0.4272 0.8075 2.0306 0.2972  0.0915  0.1065  518 TYR B CE1 
8397  C CE2 . TYR B 518 ? 0.4710 0.8104 2.0611 0.3123  0.0895  0.1436  518 TYR B CE2 
8398  C CZ  . TYR B 518 ? 0.4489 0.7909 2.0477 0.3070  0.0919  0.1223  518 TYR B CZ  
8399  O OH  . TYR B 518 ? 0.4522 0.7593 2.0547 0.3114  0.0943  0.1170  518 TYR B OH  
8400  N N   . ARG B 519 ? 0.4145 0.9639 1.9876 0.2781  0.0795  0.1078  519 ARG B N   
8401  C CA  . ARG B 519 ? 0.4149 1.0180 1.9817 0.2813  0.0743  0.1060  519 ARG B CA  
8402  C C   . ARG B 519 ? 0.4278 1.0585 1.9987 0.2967  0.0685  0.1137  519 ARG B C   
8403  O O   . ARG B 519 ? 0.4170 1.0457 2.0005 0.2978  0.0673  0.1022  519 ARG B O   
8404  C CB  . ARG B 519 ? 0.3906 1.0165 1.9626 0.2684  0.0722  0.0763  519 ARG B CB  
8405  C CG  . ARG B 519 ? 0.3907 1.0737 1.9564 0.2706  0.0659  0.0686  519 ARG B CG  
8406  C CD  . ARG B 519 ? 0.3715 1.0712 1.9464 0.2583  0.0621  0.0367  519 ARG B CD  
8407  N NE  . ARG B 519 ? 0.3592 1.0371 1.9324 0.2458  0.0661  0.0225  519 ARG B NE  
8408  C CZ  . ARG B 519 ? 0.3686 1.0665 1.9301 0.2444  0.0665  0.0190  519 ARG B CZ  
8409  N NH1 . ARG B 519 ? 0.3799 1.1234 1.9295 0.2532  0.0628  0.0271  519 ARG B NH1 
8410  N NH2 . ARG B 519 ? 0.3656 1.0406 1.9271 0.2347  0.0706  0.0069  519 ARG B NH2 
8411  N N   . GLY B 520 ? 0.4533 1.1118 2.0139 0.3089  0.0651  0.1342  520 GLY B N   
8412  C CA  . GLY B 520 ? 0.4736 1.1600 2.0375 0.3259  0.0591  0.1444  520 GLY B CA  
8413  C C   . GLY B 520 ? 0.4808 1.1313 2.0556 0.3356  0.0606  0.1498  520 GLY B C   
8414  O O   . GLY B 520 ? 0.4771 1.0764 2.0520 0.3338  0.0659  0.1567  520 GLY B O   
8415  N N   . ASP B 521 ? 0.4957 1.1762 2.0801 0.3466  0.0557  0.1456  521 ASP B N   
8416  C CA  . ASP B 521 ? 0.5171 1.1726 2.1099 0.3617  0.0563  0.1544  521 ASP B CA  
8417  C C   . ASP B 521 ? 0.5006 1.1598 2.1099 0.3558  0.0576  0.1310  521 ASP B C   
8418  O O   . ASP B 521 ? 0.4980 1.1563 2.1164 0.3701  0.0570  0.1341  521 ASP B O   
8419  C CB  . ASP B 521 ? 0.5468 1.2316 2.1365 0.3842  0.0499  0.1758  521 ASP B CB  
8420  C CG  . ASP B 521 ? 0.5544 1.3054 2.1505 0.3885  0.0425  0.1653  521 ASP B CG  
8421  O OD1 . ASP B 521 ? 0.5284 1.3023 2.1318 0.3722  0.0422  0.1401  521 ASP B OD1 
8422  O OD2 . ASP B 521 ? 0.5864 1.3654 2.1810 0.4084  0.0366  0.1826  521 ASP B OD2 
8423  N N   . TRP B 522 ? 0.4832 1.1455 2.0965 0.3351  0.0596  0.1085  522 TRP B N   
8424  C CA  . TRP B 522 ? 0.4615 1.1312 2.0909 0.3266  0.0606  0.0878  522 TRP B CA  
8425  C C   . TRP B 522 ? 0.4621 1.0887 2.0971 0.3327  0.0665  0.0908  522 TRP B C   
8426  O O   . TRP B 522 ? 0.4462 1.0841 2.0947 0.3327  0.0673  0.0802  522 TRP B O   
8427  C CB  . TRP B 522 ? 0.4494 1.1165 2.0811 0.3031  0.0620  0.0660  522 TRP B CB  
8428  C CG  . TRP B 522 ? 0.4593 1.0720 2.0867 0.2928  0.0693  0.0646  522 TRP B CG  
8429  C CD1 . TRP B 522 ? 0.4811 1.0708 2.0954 0.2881  0.0718  0.0717  522 TRP B CD1 
8430  C CD2 . TRP B 522 ? 0.4591 1.0371 2.0949 0.2858  0.0749  0.0561  522 TRP B CD2 
8431  N NE1 . TRP B 522 ? 0.4769 1.0205 2.0918 0.2787  0.0779  0.0675  522 TRP B NE1 
8432  C CE2 . TRP B 522 ? 0.4607 0.9957 2.0879 0.2774  0.0798  0.0580  522 TRP B CE2 
8433  C CE3 . TRP B 522 ? 0.4612 1.0435 2.1109 0.2857  0.0764  0.0476  522 TRP B CE3 
8434  C CZ2 . TRP B 522 ? 0.4501 0.9463 2.0812 0.2696  0.0854  0.0515  522 TRP B CZ2 
8435  C CZ3 . TRP B 522 ? 0.4542 0.9985 2.1071 0.2779  0.0826  0.0418  522 TRP B CZ3 
8436  C CH2 . TRP B 522 ? 0.4417 0.9429 2.0849 0.2702  0.0867  0.0436  522 TRP B CH2 
8437  N N   . ALA B 523 ? 0.4842 1.0631 2.1089 0.3364  0.0705  0.1045  523 ALA B N   
8438  C CA  . ALA B 523 ? 0.4810 1.0135 2.1088 0.3399  0.0759  0.1047  523 ALA B CA  
8439  C C   . ALA B 523 ? 0.4948 1.0187 2.1228 0.3647  0.0740  0.1211  523 ALA B C   
8440  O O   . ALA B 523 ? 0.5147 0.9942 2.1415 0.3711  0.0775  0.1250  523 ALA B O   
8441  C CB  . ALA B 523 ? 0.4774 0.9626 2.0954 0.3277  0.0805  0.1075  523 ALA B CB  
8442  N N   . LYS B 524 ? 0.4945 1.0613 2.1247 0.3795  0.0680  0.1297  524 LYS B N   
8443  C CA  . LYS B 524 ? 0.5145 1.0746 2.1445 0.4055  0.0650  0.1474  524 LYS B CA  
8444  C C   . LYS B 524 ? 0.5011 1.0383 2.1407 0.4156  0.0689  0.1388  524 LYS B C   
8445  O O   . LYS B 524 ? 0.5091 1.0055 2.1451 0.4308  0.0693  0.1495  524 LYS B O   
8446  C CB  . LYS B 524 ? 0.5235 1.1424 2.1570 0.4195  0.0576  0.1543  524 LYS B CB  
8447  C CG  . LYS B 524 ? 0.5647 1.1738 2.1959 0.4476  0.0535  0.1766  524 LYS B CG  
8448  C CD  . LYS B 524 ? 0.5807 1.2466 2.2125 0.4631  0.0453  0.1883  524 LYS B CD  
8449  C CE  . LYS B 524 ? 0.6166 1.2680 2.2467 0.4927  0.0409  0.2117  524 LYS B CE  
8450  N NZ  . LYS B 524 ? 0.6179 1.2615 2.2610 0.5110  0.0423  0.2040  524 LYS B NZ  
8451  N N   . GLU B 525 ? 0.4773 1.0395 2.1288 0.4058  0.0717  0.1189  525 GLU B N   
8452  C CA  . GLU B 525 ? 0.4777 1.0304 2.1388 0.4149  0.0759  0.1094  525 GLU B CA  
8453  C C   . GLU B 525 ? 0.4635 0.9712 2.1217 0.3984  0.0830  0.0979  525 GLU B C   
8454  O O   . GLU B 525 ? 0.4715 0.9392 2.1268 0.4093  0.0858  0.0992  525 GLU B O   
8455  C CB  . GLU B 525 ? 0.4662 1.0792 2.1433 0.4145  0.0747  0.0975  525 GLU B CB  
8456  C CG  . GLU B 525 ? 0.4795 1.1417 2.1605 0.4322  0.0670  0.1083  525 GLU B CG  
8457  C CD  . GLU B 525 ? 0.4736 1.1720 2.1510 0.4184  0.0613  0.1090  525 GLU B CD  
8458  O OE1 . GLU B 525 ? 0.4593 1.1537 2.1349 0.3936  0.0632  0.0970  525 GLU B OE1 
8459  O OE2 . GLU B 525 ? 0.4874 1.2190 2.1634 0.4338  0.0544  0.1215  525 GLU B OE2 
8460  N N   . VAL B 526 ? 0.4373 0.9514 2.0962 0.3733  0.0852  0.0860  526 VAL B N   
8461  C CA  . VAL B 526 ? 0.4360 0.9176 2.0947 0.3577  0.0916  0.0737  526 VAL B CA  
8462  C C   . VAL B 526 ? 0.4667 0.8903 2.1123 0.3562  0.0935  0.0813  526 VAL B C   
8463  O O   . VAL B 526 ? 0.4730 0.8630 2.1173 0.3544  0.0980  0.0748  526 VAL B O   
8464  C CB  . VAL B 526 ? 0.4101 0.9113 2.0736 0.3319  0.0924  0.0601  526 VAL B CB  
8465  C CG1 . VAL B 526 ? 0.4030 0.9021 2.0573 0.3202  0.0892  0.0640  526 VAL B CG1 
8466  C CG2 . VAL B 526 ? 0.3968 0.8701 2.0619 0.3175  0.0988  0.0484  526 VAL B CG2 
8467  N N   . GLY B 527 ? 0.4917 0.9067 2.1278 0.3555  0.0900  0.0949  527 GLY B N   
8468  C CA  . GLY B 527 ? 0.5128 0.8787 2.1378 0.3492  0.0915  0.1028  527 GLY B CA  
8469  C C   . GLY B 527 ? 0.5461 0.8701 2.1678 0.3672  0.0911  0.1125  527 GLY B C   
8470  O O   . GLY B 527 ? 0.5463 0.8820 2.1725 0.3883  0.0886  0.1167  527 GLY B O   
8471  N N   . ARG B 528 ? 0.5611 0.8367 2.1756 0.3588  0.0930  0.1151  528 ARG B N   
8472  C CA  . ARG B 528 ? 0.6050 0.8337 2.2165 0.3727  0.0920  0.1213  528 ARG B CA  
8473  C C   . ARG B 528 ? 0.6705 0.8949 2.2785 0.3889  0.0862  0.1441  528 ARG B C   
8474  O O   . ARG B 528 ? 0.6615 0.9105 2.2658 0.3834  0.0841  0.1562  528 ARG B O   
8475  C CB  . ARG B 528 ? 0.5982 0.7806 2.2037 0.3562  0.0945  0.1185  528 ARG B CB  
8476  C CG  . ARG B 528 ? 0.6239 0.7537 2.2267 0.3680  0.0925  0.1226  528 ARG B CG  
8477  C CD  . ARG B 528 ? 0.6093 0.6950 2.2071 0.3511  0.0940  0.1199  528 ARG B CD  
8478  N NE  . ARG B 528 ? 0.5742 0.6636 2.1738 0.3404  0.0989  0.0987  528 ARG B NE  
8479  C CZ  . ARG B 528 ? 0.5489 0.6557 2.1483 0.3202  0.1023  0.0923  528 ARG B CZ  
8480  N NH1 . ARG B 528 ? 0.5452 0.6647 2.1421 0.3090  0.1015  0.1037  528 ARG B NH1 
8481  N NH2 . ARG B 528 ? 0.5257 0.6382 2.1272 0.3122  0.1063  0.0750  528 ARG B NH2 
8482  N N   . LYS B 529 ? 0.7505 0.9436 2.3591 0.4095  0.0834  0.1496  529 LYS B N   
8483  C CA  . LYS B 529 ? 0.8376 1.0281 2.4444 0.4284  0.0771  0.1719  529 LYS B CA  
8484  C C   . LYS B 529 ? 0.9232 1.0570 2.5231 0.4257  0.0743  0.1896  529 LYS B C   
8485  O O   . LYS B 529 ? 0.9307 1.0696 2.5251 0.4187  0.0721  0.2098  529 LYS B O   
8486  C CB  . LYS B 529 ? 0.8643 1.0647 2.4786 0.4567  0.0748  0.1673  529 LYS B CB  
8487  C CG  . LYS B 529 ? 0.8499 1.1099 2.4733 0.4596  0.0773  0.1516  529 LYS B CG  
8488  C CD  . LYS B 529 ? 0.8342 1.1509 2.4588 0.4549  0.0748  0.1596  529 LYS B CD  
8489  C CE  . LYS B 529 ? 0.8135 1.1866 2.4498 0.4640  0.0752  0.1472  529 LYS B CE  
8490  N NZ  . LYS B 529 ? 0.7681 1.1503 2.4104 0.4486  0.0817  0.1245  529 LYS B NZ  
8491  N N   . LEU B 530 ? 1.0005 1.0831 2.6009 0.4295  0.0743  0.1811  530 LEU B N   
8492  C CA  . LEU B 530 ? 1.0807 1.1080 2.6794 0.4422  0.0686  0.1960  530 LEU B CA  
8493  C C   . LEU B 530 ? 1.1087 1.1284 2.7021 0.4361  0.0646  0.2265  530 LEU B C   
8494  O O   . LEU B 530 ? 1.1313 1.1540 2.7203 0.4116  0.0677  0.2309  530 LEU B O   
8495  C CB  . LEU B 530 ? 1.0995 1.0719 2.6970 0.4329  0.0697  0.1820  530 LEU B CB  
8496  C CG  . LEU B 530 ? 1.1403 1.0553 2.7391 0.4526  0.0633  0.1850  530 LEU B CG  
8497  C CD1 . LEU B 530 ? 1.1542 1.0219 2.7511 0.4389  0.0644  0.1681  530 LEU B CD1 
8498  C CD2 . LEU B 530 ? 1.1782 1.0640 2.7755 0.4591  0.0561  0.2157  530 LEU B CD2 
8499  N N   . SER C 3   ? 1.1356 2.8388 1.9469 0.1433  -0.1144 -0.1343 3   SER C N   
8500  C CA  . SER C 3   ? 1.0927 2.7336 1.9355 0.1456  -0.0949 -0.0896 3   SER C CA  
8501  C C   . SER C 3   ? 1.0618 2.6133 1.9471 0.1389  -0.0916 -0.1209 3   SER C C   
8502  O O   . SER C 3   ? 1.0698 2.6006 1.9524 0.1395  -0.0825 -0.1649 3   SER C O   
8503  C CB  . SER C 3   ? 1.1031 2.7700 1.9205 0.1549  -0.0716 -0.0700 3   SER C CB  
8504  O OG  . SER C 3   ? 1.0639 2.6750 1.9120 0.1563  -0.0546 -0.0258 3   SER C OG  
8505  N N   . LYS C 4   ? 1.0300 2.5304 1.9549 0.1334  -0.0984 -0.0965 4   LYS C N   
8506  C CA  . LYS C 4   ? 0.9955 2.4144 1.9616 0.1265  -0.0968 -0.1211 4   LYS C CA  
8507  C C   . LYS C 4   ? 0.9598 2.3189 1.9552 0.1293  -0.0792 -0.0779 4   LYS C C   
8508  O O   . LYS C 4   ? 0.9566 2.3342 1.9458 0.1353  -0.0711 -0.0270 4   LYS C O   
8509  C CB  . LYS C 4   ? 0.9837 2.3908 1.9741 0.1167  -0.1196 -0.1373 4   LYS C CB  
8510  C CG  . LYS C 4   ? 0.9707 2.3966 1.9722 0.1169  -0.1307 -0.0875 4   LYS C CG  
8511  C CD  . LYS C 4   ? 0.9625 2.3784 1.9911 0.1070  -0.1527 -0.1041 4   LYS C CD  
8512  C CE  . LYS C 4   ? 0.9255 2.2612 1.9978 0.0997  -0.1492 -0.1216 4   LYS C CE  
8513  N NZ  . LYS C 4   ? 0.8852 2.1678 1.9826 0.1043  -0.1327 -0.0783 4   LYS C NZ  
8514  N N   . THR C 5   ? 0.9330 2.2200 1.9615 0.1245  -0.0741 -0.0993 5   THR C N   
8515  C CA  . THR C 5   ? 0.8916 2.1177 1.9484 0.1264  -0.0581 -0.0673 5   THR C CA  
8516  C C   . THR C 5   ? 0.8697 2.0857 1.9482 0.1260  -0.0648 -0.0193 5   THR C C   
8517  O O   . THR C 5   ? 0.8548 2.0661 1.9500 0.1201  -0.0810 -0.0267 5   THR C O   
8518  C CB  . THR C 5   ? 0.8656 2.0225 1.9521 0.1208  -0.0548 -0.1040 5   THR C CB  
8519  O OG1 . THR C 5   ? 0.8864 2.0607 1.9533 0.1214  -0.0533 -0.1535 5   THR C OG1 
8520  C CG2 . THR C 5   ? 0.8303 1.9284 1.9405 0.1235  -0.0368 -0.0777 5   THR C CG2 
8521  N N   . LYS C 6   ? 0.8627 2.0753 1.9430 0.1323  -0.0518 0.0291  6   LYS C N   
8522  C CA  . LYS C 6   ? 0.8457 2.0342 1.9533 0.1335  -0.0540 0.0746  6   LYS C CA  
8523  C C   . LYS C 6   ? 0.8176 1.9274 1.9597 0.1319  -0.0419 0.0771  6   LYS C C   
8524  O O   . LYS C 6   ? 0.8262 1.9152 1.9662 0.1347  -0.0254 0.0798  6   LYS C O   
8525  C CB  . LYS C 6   ? 0.8582 2.0904 1.9488 0.1411  -0.0475 0.1253  6   LYS C CB  
8526  C CG  . LYS C 6   ? 0.8432 2.0594 1.9605 0.1442  -0.0505 0.1757  6   LYS C CG  
8527  C CD  . LYS C 6   ? 0.8543 2.1020 1.9758 0.1428  -0.0715 0.1805  6   LYS C CD  
8528  C CE  . LYS C 6   ? 0.8443 2.0832 1.9909 0.1482  -0.0733 0.2333  6   LYS C CE  
8529  N NZ  . LYS C 6   ? 0.8592 2.1185 1.9956 0.1552  -0.0609 0.2779  6   LYS C NZ  
8530  N N   . ILE C 7   ? 0.7922 1.8618 1.9656 0.1277  -0.0502 0.0763  7   ILE C N   
8531  C CA  . ILE C 7   ? 0.7561 1.7542 1.9617 0.1265  -0.0402 0.0798  7   ILE C CA  
8532  C C   . ILE C 7   ? 0.7390 1.7224 1.9661 0.1314  -0.0389 0.1287  7   ILE C C   
8533  O O   . ILE C 7   ? 0.7546 1.7761 1.9795 0.1337  -0.0501 0.1515  7   ILE C O   
8534  C CB  . ILE C 7   ? 0.7397 1.7009 1.9661 0.1183  -0.0483 0.0406  7   ILE C CB  
8535  C CG1 . ILE C 7   ? 0.7595 1.7329 1.9679 0.1141  -0.0499 -0.0088 7   ILE C CG1 
8536  C CG2 . ILE C 7   ? 0.7009 1.5921 1.9593 0.1175  -0.0384 0.0466  7   ILE C CG2 
8537  C CD1 . ILE C 7   ? 0.7551 1.7005 1.9845 0.1049  -0.0608 -0.0469 7   ILE C CD1 
8538  N N   . GLU C 8   ? 0.7122 1.6417 1.9606 0.1333  -0.0256 0.1439  8   GLU C N   
8539  C CA  . GLU C 8   ? 0.6996 1.6097 1.9702 0.1387  -0.0228 0.1877  8   GLU C CA  
8540  C C   . GLU C 8   ? 0.6770 1.5186 1.9742 0.1384  -0.0113 0.1873  8   GLU C C   
8541  O O   . GLU C 8   ? 0.6881 1.5085 1.9804 0.1377  0.0010  0.1781  8   GLU C O   
8542  C CB  . GLU C 8   ? 0.7159 1.6649 1.9705 0.1449  -0.0170 0.2261  8   GLU C CB  
8543  C CG  . GLU C 8   ? 0.7093 1.6481 1.9876 0.1512  -0.0174 0.2736  8   GLU C CG  
8544  C CD  . GLU C 8   ? 0.7320 1.7049 1.9993 0.1566  -0.0112 0.3153  8   GLU C CD  
8545  O OE1 . GLU C 8   ? 0.7438 1.7385 1.9877 0.1555  -0.0021 0.3094  8   GLU C OE1 
8546  O OE2 . GLU C 8   ? 0.7393 1.7185 2.0233 0.1622  -0.0154 0.3549  8   GLU C OE2 
8547  N N   . LEU C 9   ? 0.6553 1.4652 1.9806 0.1394  -0.0153 0.1981  9   LEU C N   
8548  C CA  . LEU C 9   ? 0.6259 1.3734 1.9760 0.1389  -0.0067 0.1942  9   LEU C CA  
8549  C C   . LEU C 9   ? 0.6237 1.3504 1.9935 0.1462  -0.0008 0.2344  9   LEU C C   
8550  O O   . LEU C 9   ? 0.6173 1.3413 2.0061 0.1501  -0.0072 0.2517  9   LEU C O   
8551  C CB  . LEU C 9   ? 0.6082 1.3351 1.9762 0.1345  -0.0150 0.1720  9   LEU C CB  
8552  C CG  . LEU C 9   ? 0.6143 1.3428 1.9731 0.1259  -0.0196 0.1285  9   LEU C CG  
8553  C CD1 . LEU C 9   ? 0.6453 1.4290 1.9750 0.1239  -0.0270 0.1141  9   LEU C CD1 
8554  C CD2 . LEU C 9   ? 0.6023 1.3168 1.9833 0.1214  -0.0290 0.1159  9   LEU C CD2 
8555  N N   . LYS C 10  ? 0.6291 1.3406 1.9969 0.1479  0.0113  0.2482  10  LYS C N   
8556  C CA  . LYS C 10  ? 0.6285 1.3153 2.0179 0.1539  0.0170  0.2838  10  LYS C CA  
8557  C C   . LYS C 10  ? 0.6012 1.2382 2.0005 0.1519  0.0293  0.2748  10  LYS C C   
8558  O O   . LYS C 10  ? 0.5976 1.2337 1.9819 0.1472  0.0348  0.2514  10  LYS C O   
8559  C CB  . LYS C 10  ? 0.6648 1.3954 2.0442 0.1582  0.0170  0.3204  10  LYS C CB  
8560  C CG  . LYS C 10  ? 0.6870 1.4009 2.0936 0.1654  0.0179  0.3615  10  LYS C CG  
8561  C CD  . LYS C 10  ? 0.7206 1.4609 2.1241 0.1683  0.0230  0.4009  10  LYS C CD  
8562  C CE  . LYS C 10  ? 0.7435 1.5372 2.1407 0.1734  0.0132  0.4317  10  LYS C CE  
8563  N NZ  . LYS C 10  ? 0.7604 1.5841 2.1494 0.1744  0.0197  0.4662  10  LYS C NZ  
8564  N N   . ASP C 11  ? 0.5835 1.1792 2.0092 0.1557  0.0328  0.2911  11  ASP C N   
8565  C CA  . ASP C 11  ? 0.5619 1.1104 1.9993 0.1542  0.0429  0.2851  11  ASP C CA  
8566  C C   . ASP C 11  ? 0.5390 1.0638 1.9708 0.1485  0.0443  0.2459  11  ASP C C   
8567  O O   . ASP C 11  ? 0.5342 1.0330 1.9666 0.1458  0.0524  0.2352  11  ASP C O   
8568  C CB  . ASP C 11  ? 0.5775 1.1370 2.0087 0.1533  0.0516  0.3035  11  ASP C CB  
8569  C CG  . ASP C 11  ? 0.5949 1.1743 2.0362 0.1584  0.0508  0.3463  11  ASP C CG  
8570  O OD1 . ASP C 11  ? 0.5898 1.2006 2.0286 0.1623  0.0420  0.3604  11  ASP C OD1 
8571  O OD2 . ASP C 11  ? 0.6139 1.1788 2.0666 0.1581  0.0585  0.3662  11  ASP C OD2 
8572  N N   . ASN C 12  ? 0.5344 1.0685 1.9631 0.1466  0.0360  0.2262  12  ASN C N   
8573  C CA  . ASN C 12  ? 0.5235 1.0347 1.9514 0.1411  0.0360  0.1916  12  ASN C CA  
8574  C C   . ASN C 12  ? 0.5158 1.0423 1.9229 0.1363  0.0394  0.1690  12  ASN C C   
8575  O O   . ASN C 12  ? 0.4922 0.9895 1.9016 0.1332  0.0447  0.1485  12  ASN C O   
8576  C CB  . ASN C 12  ? 0.5115 0.9707 1.9588 0.1421  0.0422  0.1891  12  ASN C CB  
8577  C CG  . ASN C 12  ? 0.5102 0.9564 1.9779 0.1481  0.0392  0.2079  12  ASN C CG  
8578  O OD1 . ASN C 12  ? 0.5023 0.9742 1.9724 0.1501  0.0311  0.2142  12  ASN C OD1 
8579  N ND2 . ASN C 12  ? 0.5092 0.9168 1.9927 0.1514  0.0455  0.2153  12  ASN C ND2 
8580  N N   . TRP C 13  ? 0.5305 1.1050 1.9177 0.1365  0.0358  0.1728  13  TRP C N   
8581  C CA  . TRP C 13  ? 0.5473 1.1454 1.9126 0.1336  0.0392  0.1523  13  TRP C CA  
8582  C C   . TRP C 13  ? 0.5624 1.2120 1.9079 0.1325  0.0289  0.1426  13  TRP C C   
8583  O O   . TRP C 13  ? 0.5740 1.2572 1.9148 0.1358  0.0237  0.1679  13  TRP C O   
8584  C CB  . TRP C 13  ? 0.5588 1.1662 1.9176 0.1363  0.0500  0.1738  13  TRP C CB  
8585  C CG  . TRP C 13  ? 0.5574 1.1223 1.9280 0.1351  0.0604  0.1670  13  TRP C CG  
8586  C CD1 . TRP C 13  ? 0.5502 1.0731 1.9428 0.1363  0.0645  0.1826  13  TRP C CD1 
8587  C CD2 . TRP C 13  ? 0.5715 1.1341 1.9329 0.1329  0.0673  0.1414  13  TRP C CD2 
8588  N NE1 . TRP C 13  ? 0.5462 1.0421 1.9432 0.1343  0.0728  0.1693  13  TRP C NE1 
8589  C CE2 . TRP C 13  ? 0.5543 1.0734 1.9335 0.1325  0.0749  0.1450  13  TRP C CE2 
8590  C CE3 . TRP C 13  ? 0.5811 1.1745 1.9219 0.1318  0.0677  0.1150  13  TRP C CE3 
8591  C CZ2 . TRP C 13  ? 0.5448 1.0520 1.9227 0.1311  0.0825  0.1252  13  TRP C CZ2 
8592  C CZ3 . TRP C 13  ? 0.5678 1.1480 1.9081 0.1313  0.0762  0.0947  13  TRP C CZ3 
8593  C CH2 . TRP C 13  ? 0.5510 1.0886 1.9103 0.1309  0.0833  0.1006  13  TRP C CH2 
8594  N N   . TYR C 14  ? 0.5618 1.2180 1.8968 0.1279  0.0257  0.1058  14  TYR C N   
8595  C CA  . TYR C 14  ? 0.5780 1.2867 1.8898 0.1266  0.0173  0.0914  14  TYR C CA  
8596  C C   . TYR C 14  ? 0.6027 1.3502 1.8916 0.1308  0.0251  0.1072  14  TYR C C   
8597  O O   . TYR C 14  ? 0.6003 1.3309 1.8897 0.1322  0.0375  0.1091  14  TYR C O   
8598  C CB  . TYR C 14  ? 0.5705 1.2751 1.8773 0.1212  0.0137  0.0462  14  TYR C CB  
8599  C CG  . TYR C 14  ? 0.5467 1.2261 1.8730 0.1151  0.0036  0.0256  14  TYR C CG  
8600  C CD1 . TYR C 14  ? 0.5138 1.1405 1.8652 0.1136  0.0077  0.0273  14  TYR C CD1 
8601  C CD2 . TYR C 14  ? 0.5610 1.2708 1.8805 0.1102  -0.0098 0.0016  14  TYR C CD2 
8602  C CE1 . TYR C 14  ? 0.5032 1.1093 1.8730 0.1075  -0.0003 0.0090  14  TYR C CE1 
8603  C CE2 . TYR C 14  ? 0.5488 1.2364 1.8890 0.1033  -0.0187 -0.0177 14  TYR C CE2 
8604  C CZ  . TYR C 14  ? 0.5204 1.1563 1.8862 0.1019  -0.0134 -0.0129 14  TYR C CZ  
8605  O OH  . TYR C 14  ? 0.5088 1.1251 1.8962 0.0948  -0.0212 -0.0289 14  TYR C OH  
8606  N N   . HIS C 15  ? 0.6333 1.4349 1.9036 0.1328  0.0178  0.1205  15  HIS C N   
8607  C CA  . HIS C 15  ? 0.6667 1.5168 1.9104 0.1363  0.0239  0.1315  15  HIS C CA  
8608  C C   . HIS C 15  ? 0.7036 1.6060 1.9198 0.1348  0.0138  0.1026  15  HIS C C   
8609  O O   . HIS C 15  ? 0.7069 1.6328 1.9216 0.1334  -0.0004 0.1038  15  HIS C O   
8610  C CB  . HIS C 15  ? 0.6774 1.5532 1.9216 0.1411  0.0241  0.1810  15  HIS C CB  
8611  C CG  . HIS C 15  ? 0.6590 1.4887 1.9313 0.1431  0.0319  0.2125  15  HIS C CG  
8612  N ND1 . HIS C 15  ? 0.6354 1.4166 1.9354 0.1422  0.0280  0.2126  15  HIS C ND1 
8613  C CD2 . HIS C 15  ? 0.6630 1.4891 1.9408 0.1457  0.0432  0.2441  15  HIS C CD2 
8614  C CE1 . HIS C 15  ? 0.6256 1.3748 1.9457 0.1448  0.0362  0.2413  15  HIS C CE1 
8615  N NE2 . HIS C 15  ? 0.6407 1.4153 1.9493 0.1464  0.0450  0.2613  15  HIS C NE2 
8616  N N   . LEU C 16  ? 0.7267 1.6484 1.9222 0.1353  0.0210  0.0758  16  LEU C N   
8617  C CA  . LEU C 16  ? 0.7617 1.7390 1.9273 0.1352  0.0130  0.0478  16  LEU C CA  
8618  C C   . LEU C 16  ? 0.7870 1.8240 1.9237 0.1410  0.0203  0.0740  16  LEU C C   
8619  O O   . LEU C 16  ? 0.7827 1.8194 1.9143 0.1441  0.0357  0.0792  16  LEU C O   
8620  C CB  . LEU C 16  ? 0.7717 1.7302 1.9356 0.1328  0.0157  -0.0035 16  LEU C CB  
8621  C CG  . LEU C 16  ? 0.7661 1.6880 1.9506 0.1258  0.0032  -0.0371 16  LEU C CG  
8622  C CD1 . LEU C 16  ? 0.7365 1.6021 1.9550 0.1230  0.0028  -0.0153 16  LEU C CD1 
8623  C CD2 . LEU C 16  ? 0.7698 1.6705 1.9560 0.1244  0.0074  -0.0844 16  LEU C CD2 
8624  N N   . ASP C 17  ? 0.8052 1.8948 1.9250 0.1423  0.0090  0.0931  17  ASP C N   
8625  C CA  . ASP C 17  ? 0.8298 1.9827 1.9213 0.1477  0.0142  0.1224  17  ASP C CA  
8626  C C   . ASP C 17  ? 0.8159 1.9498 1.9224 0.1509  0.0296  0.1693  17  ASP C C   
8627  O O   . ASP C 17  ? 0.8327 2.0000 1.9215 0.1543  0.0423  0.1823  17  ASP C O   
8628  C CB  . ASP C 17  ? 0.8558 2.0548 1.9128 0.1499  0.0191  0.0864  17  ASP C CB  
8629  C CG  . ASP C 17  ? 0.8747 2.1166 1.9084 0.1478  0.0021  0.0482  17  ASP C CG  
8630  O OD1 . ASP C 17  ? 0.8813 2.1569 1.9089 0.1474  -0.0122 0.0686  17  ASP C OD1 
8631  O OD2 . ASP C 17  ? 0.8773 2.1200 1.8999 0.1471  0.0031  -0.0011 17  ASP C OD2 
8632  N N   . GLY C 18  ? 0.7867 1.8681 1.9272 0.1496  0.0286  0.1943  18  GLY C N   
8633  C CA  . GLY C 18  ? 0.7736 1.8359 1.9327 0.1519  0.0403  0.2404  18  GLY C CA  
8634  C C   . GLY C 18  ? 0.7463 1.7479 1.9279 0.1498  0.0535  0.2292  18  GLY C C   
8635  O O   . GLY C 18  ? 0.7281 1.6908 1.9367 0.1499  0.0587  0.2593  18  GLY C O   
8636  N N   . GLU C 19  ? 0.7453 1.7393 1.9170 0.1482  0.0583  0.1854  19  GLU C N   
8637  C CA  . GLU C 19  ? 0.7283 1.6755 1.9175 0.1470  0.0716  0.1757  19  GLU C CA  
8638  C C   . GLU C 19  ? 0.6957 1.5797 1.9099 0.1432  0.0656  0.1497  19  GLU C C   
8639  O O   . GLU C 19  ? 0.7007 1.5855 1.9100 0.1410  0.0542  0.1193  19  GLU C O   
8640  C CB  . GLU C 19  ? 0.7481 1.7254 1.9147 0.1491  0.0822  0.1470  19  GLU C CB  
8641  C CG  . GLU C 19  ? 0.7808 1.8247 1.9219 0.1531  0.0905  0.1741  19  GLU C CG  
8642  C CD  . GLU C 19  ? 0.7808 1.8199 1.9391 0.1533  0.1000  0.2278  19  GLU C CD  
8643  O OE1 . GLU C 19  ? 0.7534 1.7350 1.9442 0.1506  0.1010  0.2429  19  GLU C OE1 
8644  O OE2 . GLU C 19  ? 0.8116 1.9068 1.9510 0.1560  0.1064  0.2552  19  GLU C OE2 
8645  N N   . LYS C 20  ? 0.6706 1.5020 1.9117 0.1422  0.0732  0.1628  20  LYS C N   
8646  C CA  . LYS C 20  ? 0.6461 1.4176 1.9113 0.1390  0.0692  0.1433  20  LYS C CA  
8647  C C   . LYS C 20  ? 0.6438 1.4050 1.9029 0.1373  0.0702  0.0959  20  LYS C C   
8648  O O   . LYS C 20  ? 0.6592 1.4244 1.9130 0.1389  0.0813  0.0859  20  LYS C O   
8649  C CB  . LYS C 20  ? 0.6236 1.3476 1.9152 0.1387  0.0782  0.1662  20  LYS C CB  
8650  C CG  . LYS C 20  ? 0.6174 1.3353 1.9249 0.1403  0.0767  0.2108  20  LYS C CG  
8651  C CD  . LYS C 20  ? 0.5890 1.2474 1.9268 0.1392  0.0808  0.2207  20  LYS C CD  
8652  C CE  . LYS C 20  ? 0.5976 1.2522 1.9519 0.1411  0.0837  0.2644  20  LYS C CE  
8653  N NZ  . LYS C 20  ? 0.6097 1.2736 1.9695 0.1441  0.0735  0.2856  20  LYS C NZ  
8654  N N   . TYR C 21  ? 0.6383 1.3851 1.9013 0.1340  0.0587  0.0680  21  TYR C N   
8655  C CA  . TYR C 21  ? 0.6425 1.3816 1.9018 0.1321  0.0573  0.0224  21  TYR C CA  
8656  C C   . TYR C 21  ? 0.6103 1.2883 1.8972 0.1283  0.0552  0.0082  21  TYR C C   
8657  O O   . TYR C 21  ? 0.6007 1.2622 1.9001 0.1248  0.0450  0.0097  21  TYR C O   
8658  C CB  . TYR C 21  ? 0.6690 1.4495 1.9090 0.1305  0.0446  -0.0027 21  TYR C CB  
8659  C CG  . TYR C 21  ? 0.6865 1.4738 1.9171 0.1300  0.0441  -0.0507 21  TYR C CG  
8660  C CD1 . TYR C 21  ? 0.6825 1.4335 1.9311 0.1249  0.0362  -0.0833 21  TYR C CD1 
8661  C CD2 . TYR C 21  ? 0.7073 1.5399 1.9120 0.1349  0.0513  -0.0639 21  TYR C CD2 
8662  C CE1 . TYR C 21  ? 0.6962 1.4516 1.9399 0.1247  0.0349  -0.1277 21  TYR C CE1 
8663  C CE2 . TYR C 21  ? 0.7234 1.5629 1.9206 0.1357  0.0506  -0.1102 21  TYR C CE2 
8664  C CZ  . TYR C 21  ? 0.7131 1.5121 1.9310 0.1306  0.0420  -0.1427 21  TYR C CZ  
8665  O OH  . TYR C 21  ? 0.7185 1.5225 1.9322 0.1318  0.0412  -0.1887 21  TYR C OH  
8666  N N   . PHE C 22  ? 0.5914 1.2394 1.8881 0.1292  0.0651  -0.0041 22  PHE C N   
8667  C CA  . PHE C 22  ? 0.5646 1.1589 1.8850 0.1261  0.0639  -0.0205 22  PHE C CA  
8668  C C   . PHE C 22  ? 0.5839 1.1812 1.9022 0.1234  0.0566  -0.0626 22  PHE C C   
8669  O O   . PHE C 22  ? 0.6089 1.2331 1.9121 0.1263  0.0600  -0.0855 22  PHE C O   
8670  C CB  . PHE C 22  ? 0.5415 1.1071 1.8733 0.1285  0.0765  -0.0151 22  PHE C CB  
8671  C CG  . PHE C 22  ? 0.5075 1.0170 1.8647 0.1258  0.0756  -0.0184 22  PHE C CG  
8672  C CD1 . PHE C 22  ? 0.5033 0.9888 1.8708 0.1237  0.0725  -0.0503 22  PHE C CD1 
8673  C CD2 . PHE C 22  ? 0.4837 0.9656 1.8547 0.1256  0.0777  0.0106  22  PHE C CD2 
8674  C CE1 . PHE C 22  ? 0.4820 0.9199 1.8716 0.1214  0.0718  -0.0504 22  PHE C CE1 
8675  C CE2 . PHE C 22  ? 0.4637 0.8989 1.8550 0.1236  0.0769  0.0072  22  PHE C CE2 
8676  C CZ  . PHE C 22  ? 0.4642 0.8788 1.8639 0.1214  0.0741  -0.0220 22  PHE C CZ  
8677  N N   . ILE C 23  ? 0.5750 1.1454 1.9098 0.1180  0.0466  -0.0728 23  ILE C N   
8678  C CA  . ILE C 23  ? 0.5931 1.1648 1.9306 0.1139  0.0377  -0.1111 23  ILE C CA  
8679  C C   . ILE C 23  ? 0.5905 1.1184 1.9477 0.1137  0.0429  -0.1322 23  ILE C C   
8680  O O   . ILE C 23  ? 0.5777 1.0641 1.9575 0.1099  0.0408  -0.1275 23  ILE C O   
8681  C CB  . ILE C 23  ? 0.5849 1.1552 1.9326 0.1073  0.0237  -0.1099 23  ILE C CB  
8682  C CG1 . ILE C 23  ? 0.5925 1.2097 1.9212 0.1085  0.0177  -0.0890 23  ILE C CG1 
8683  C CG2 . ILE C 23  ? 0.5992 1.1642 1.9562 0.1013  0.0138  -0.1496 23  ILE C CG2 
8684  C CD1 . ILE C 23  ? 0.5829 1.1956 1.9260 0.1037  0.0064  -0.0762 23  ILE C CD1 
8685  N N   . LYS C 24  ? 0.6031 1.1430 1.9517 0.1184  0.0499  -0.1545 24  LYS C N   
8686  C CA  . LYS C 24  ? 0.6060 1.1093 1.9737 0.1194  0.0541  -0.1772 24  LYS C CA  
8687  C C   . LYS C 24  ? 0.6246 1.1244 2.0012 0.1148  0.0431  -0.2154 24  LYS C C   
8688  O O   . LYS C 24  ? 0.6557 1.1820 2.0203 0.1179  0.0428  -0.2451 24  LYS C O   
8689  C CB  . LYS C 24  ? 0.6152 1.1331 1.9734 0.1275  0.0672  -0.1846 24  LYS C CB  
8690  C CG  . LYS C 24  ? 0.5943 1.1183 1.9462 0.1316  0.0788  -0.1492 24  LYS C CG  
8691  C CD  . LYS C 24  ? 0.5990 1.1420 1.9436 0.1392  0.0920  -0.1575 24  LYS C CD  
8692  C CE  . LYS C 24  ? 0.6229 1.2201 1.9413 0.1433  0.0931  -0.1775 24  LYS C CE  
8693  N NZ  . LYS C 24  ? 0.6257 1.2490 1.9350 0.1510  0.1078  -0.1766 24  LYS C NZ  
8694  N N   . ALA C 25  ? 0.6195 1.0873 2.0183 0.1073  0.0342  -0.2147 25  ALA C N   
8695  C CA  . ALA C 25  ? 0.6442 1.1109 2.0543 0.1007  0.0216  -0.2466 25  ALA C CA  
8696  C C   . ALA C 25  ? 0.6493 1.0696 2.0893 0.0991  0.0222  -0.2662 25  ALA C C   
8697  O O   . ALA C 25  ? 0.6327 1.0248 2.0824 0.1036  0.0320  -0.2544 25  ALA C O   
8698  C CB  . ALA C 25  ? 0.6312 1.1028 2.0466 0.0924  0.0100  -0.2320 25  ALA C CB  
8699  N N   . ILE C 26  ? 0.6759 1.0912 2.1311 0.0925  0.0108  -0.2967 26  ILE C N   
8700  C CA  . ILE C 26  ? 0.6731 1.0431 2.1630 0.0880  0.0076  -0.3118 26  ILE C CA  
8701  C C   . ILE C 26  ? 0.6844 1.0551 2.1908 0.0763  -0.0081 -0.3274 26  ILE C C   
8702  O O   . ILE C 26  ? 0.6959 1.1040 2.1867 0.0738  -0.0169 -0.3452 26  ILE C O   
8703  C CB  . ILE C 26  ? 0.6896 1.0501 2.1858 0.0956  0.0135  -0.3429 26  ILE C CB  
8704  C CG1 . ILE C 26  ? 0.6888 0.9993 2.2244 0.0919  0.0106  -0.3548 26  ILE C CG1 
8705  C CG2 . ILE C 26  ? 0.7234 1.1239 2.2013 0.0980  0.0085  -0.3802 26  ILE C CG2 
8706  C CD1 . ILE C 26  ? 0.7060 1.0022 2.2521 0.1014  0.0180  -0.3795 26  ILE C CD1 
8707  N N   . GLY C 27  ? 0.6779 1.0090 2.2166 0.0689  -0.0117 -0.3194 27  GLY C N   
8708  C CA  . GLY C 27  ? 0.6905 1.0157 2.2537 0.0567  -0.0261 -0.3356 27  GLY C CA  
8709  C C   . GLY C 27  ? 0.7187 1.0359 2.2983 0.0554  -0.0324 -0.3804 27  GLY C C   
8710  O O   . GLY C 27  ? 0.7228 1.0101 2.3180 0.0608  -0.0260 -0.3912 27  GLY C O   
8711  N N   . TYR C 28  ? 0.7430 1.0877 2.3205 0.0483  -0.0459 -0.4070 28  TYR C N   
8712  C CA  . TYR C 28  ? 0.7787 1.1170 2.3739 0.0460  -0.0543 -0.4533 28  TYR C CA  
8713  C C   . TYR C 28  ? 0.7837 1.1227 2.4045 0.0302  -0.0721 -0.4670 28  TYR C C   
8714  O O   . TYR C 28  ? 0.7740 1.1474 2.3796 0.0246  -0.0798 -0.4561 28  TYR C O   
8715  C CB  . TYR C 28  ? 0.8104 1.1922 2.3685 0.0563  -0.0513 -0.4793 28  TYR C CB  
8716  C CG  . TYR C 28  ? 0.8621 1.2500 2.4302 0.0548  -0.0615 -0.5328 28  TYR C CG  
8717  C CD1 . TYR C 28  ? 0.8907 1.2451 2.4823 0.0608  -0.0568 -0.5595 28  TYR C CD1 
8718  C CD2 . TYR C 28  ? 0.8950 1.3233 2.4497 0.0482  -0.0761 -0.5579 28  TYR C CD2 
8719  C CE1 . TYR C 28  ? 0.9376 1.2955 2.5405 0.0603  -0.0660 -0.6110 28  TYR C CE1 
8720  C CE2 . TYR C 28  ? 0.9449 1.3792 2.5087 0.0469  -0.0861 -0.6100 28  TYR C CE2 
8721  C CZ  . TYR C 28  ? 0.9666 1.3644 2.5550 0.0532  -0.0808 -0.6377 28  TYR C CZ  
8722  O OH  . TYR C 28  ? 1.0092 1.4111 2.6087 0.0529  -0.0906 -0.6918 28  TYR C OH  
8723  N N   . GLU C 29  ? 0.7913 1.0926 2.4534 0.0234  -0.0786 -0.4903 29  GLU C N   
8724  C CA  . GLU C 29  ? 0.7950 1.0903 2.4905 0.0070  -0.0957 -0.5057 29  GLU C CA  
8725  C C   . GLU C 29  ? 0.8335 1.1216 2.5468 0.0060  -0.1049 -0.5590 29  GLU C C   
8726  O O   . GLU C 29  ? 0.8343 1.0799 2.5788 0.0081  -0.1015 -0.5709 29  GLU C O   
8727  C CB  . GLU C 29  ? 0.7715 1.0224 2.5083 -0.0022 -0.0947 -0.4762 29  GLU C CB  
8728  C CG  . GLU C 29  ? 0.7781 1.0304 2.5471 -0.0205 -0.1104 -0.4762 29  GLU C CG  
8729  C CD  . GLU C 29  ? 0.7523 0.9737 2.5505 -0.0276 -0.1057 -0.4352 29  GLU C CD  
8730  O OE1 . GLU C 29  ? 0.7538 0.9320 2.5792 -0.0262 -0.0994 -0.4295 29  GLU C OE1 
8731  O OE2 . GLU C 29  ? 0.7372 0.9794 2.5305 -0.0335 -0.1077 -0.4078 29  GLU C OE2 
8732  N N   . ILE C 30  ? 0.8602 1.1915 2.5528 0.0037  -0.1165 -0.5911 30  ILE C N   
8733  C CA  . ILE C 30  ? 0.9015 1.2298 2.6139 -0.0004 -0.1293 -0.6456 30  ILE C CA  
8734  C C   . ILE C 30  ? 0.9112 1.2097 2.6766 -0.0197 -0.1450 -0.6502 30  ILE C C   
8735  O O   . ILE C 30  ? 0.8846 1.1845 2.6601 -0.0301 -0.1482 -0.6152 30  ILE C O   
8736  C CB  . ILE C 30  ? 0.9264 1.3152 2.5969 0.0029  -0.1374 -0.6767 30  ILE C CB  
8737  C CG1 . ILE C 30  ? 0.9813 1.3687 2.6661 0.0025  -0.1482 -0.7384 30  ILE C CG1 
8738  C CG2 . ILE C 30  ? 0.9176 1.3451 2.5776 -0.0093 -0.1507 -0.6599 30  ILE C CG2 
8739  C CD1 . ILE C 30  ? 0.9956 1.3520 2.6882 0.0172  -0.1349 -0.7596 30  ILE C CD1 
8740  N N   . GLY C 31  ? 0.9531 1.2237 2.7551 -0.0240 -0.1542 -0.6928 31  GLY C N   
8741  C CA  . GLY C 31  ? 0.9700 1.2094 2.8282 -0.0430 -0.1694 -0.6999 31  GLY C CA  
8742  C C   . GLY C 31  ? 0.9491 1.1345 2.8468 -0.0459 -0.1600 -0.6613 31  GLY C C   
8743  O O   . GLY C 31  ? 0.9462 1.1132 2.8838 -0.0623 -0.1686 -0.6442 31  GLY C O   
8744  N N   . ALA C 32  ? 0.9389 1.1016 2.8261 -0.0300 -0.1427 -0.6480 32  ALA C N   
8745  C CA  . ALA C 32  ? 0.9155 1.0303 2.8346 -0.0302 -0.1329 -0.6113 32  ALA C CA  
8746  C C   . ALA C 32  ? 0.9253 1.0072 2.8541 -0.0151 -0.1227 -0.6282 32  ALA C C   
8747  O O   . ALA C 32  ? 0.8901 0.9594 2.8053 -0.0032 -0.1070 -0.5987 32  ALA C O   
8748  C CB  . ALA C 32  ? 0.8725 1.0022 2.7613 -0.0266 -0.1206 -0.5582 32  ALA C CB  
8749  N N   . ARG C 33  ? 0.9733 1.0426 2.9274 -0.0157 -0.1325 -0.6782 33  ARG C N   
8750  C CA  . ARG C 33  ? 0.9959 1.0244 2.9780 -0.0046 -0.1265 -0.6971 33  ARG C CA  
8751  C C   . ARG C 33  ? 1.0085 0.9829 3.0531 -0.0166 -0.1311 -0.6766 33  ARG C C   
8752  O O   . ARG C 33  ? 1.0000 0.9730 3.0621 -0.0331 -0.1381 -0.6495 33  ARG C O   
8753  C CB  . ARG C 33  ? 1.0440 1.0819 3.0302 -0.0005 -0.1361 -0.7616 33  ARG C CB  
8754  C CG  . ARG C 33  ? 1.0462 1.1378 2.9717 0.0140  -0.1296 -0.7851 33  ARG C CG  
8755  C CD  . ARG C 33  ? 1.0139 1.1100 2.9066 0.0325  -0.1084 -0.7556 33  ARG C CD  
8756  N NE  . ARG C 33  ? 1.0247 1.1691 2.8664 0.0475  -0.1012 -0.7823 33  ARG C NE  
8757  C CZ  . ARG C 33  ? 0.9948 1.1868 2.7828 0.0522  -0.0936 -0.7597 33  ARG C CZ  
8758  N NH1 . ARG C 33  ? 0.9532 1.1530 2.7297 0.0430  -0.0934 -0.7132 33  ARG C NH1 
8759  N NH2 . ARG C 33  ? 1.0132 1.2465 2.7603 0.0664  -0.0860 -0.7841 33  ARG C NH2 
8760  N N   . PRO C 34  ? 1.0420 0.9721 3.1229 -0.0081 -0.1269 -0.6868 34  PRO C N   
8761  C CA  . PRO C 34  ? 1.0651 0.9441 3.2140 -0.0207 -0.1359 -0.6826 34  PRO C CA  
8762  C C   . PRO C 34  ? 1.1168 0.9968 3.2973 -0.0373 -0.1564 -0.7253 34  PRO C C   
8763  O O   . PRO C 34  ? 1.1580 1.0512 3.3304 -0.0311 -0.1626 -0.7784 34  PRO C O   
8764  C CB  . PRO C 34  ? 1.0784 0.9192 3.2514 -0.0039 -0.1276 -0.6957 34  PRO C CB  
8765  C CG  . PRO C 34  ? 1.0468 0.9170 3.1625 0.0162  -0.1101 -0.6844 34  PRO C CG  
8766  C CD  . PRO C 34  ? 1.0445 0.9722 3.1056 0.0141  -0.1128 -0.6992 34  PRO C CD  
8767  N N   . GLY C 35  ? 1.1184 0.9873 3.3345 -0.0583 -0.1668 -0.7017 35  GLY C N   
8768  C CA  . GLY C 35  ? 1.1540 1.0202 3.4092 -0.0774 -0.1875 -0.7365 35  GLY C CA  
8769  C C   . GLY C 35  ? 1.1508 1.0721 3.3691 -0.0881 -0.1966 -0.7406 35  GLY C C   
8770  O O   . GLY C 35  ? 1.1910 1.1209 3.4316 -0.1023 -0.2149 -0.7769 35  GLY C O   
8771  N N   . GLN C 36  ? 1.1136 1.0720 3.2776 -0.0813 -0.1847 -0.7039 36  GLN C N   
8772  C CA  . GLN C 36  ? 1.1030 1.1153 3.2301 -0.0892 -0.1922 -0.7031 36  GLN C CA  
8773  C C   . GLN C 36  ? 1.0572 1.0791 3.1756 -0.0953 -0.1842 -0.6425 36  GLN C C   
8774  O O   . GLN C 36  ? 1.0266 1.0326 3.1324 -0.0844 -0.1675 -0.6046 36  GLN C O   
8775  C CB  . GLN C 36  ? 1.1019 1.1634 3.1596 -0.0722 -0.1849 -0.7188 36  GLN C CB  
8776  C CG  . GLN C 36  ? 1.1536 1.2175 3.2029 -0.0603 -0.1878 -0.7775 36  GLN C CG  
8777  C CD  . GLN C 36  ? 1.1502 1.2682 3.1301 -0.0445 -0.1800 -0.7888 36  GLN C CD  
8778  O OE1 . GLN C 36  ? 1.1122 1.2421 3.0543 -0.0317 -0.1629 -0.7534 36  GLN C OE1 
8779  N NE2 . GLN C 36  ? 1.1928 1.3457 3.1559 -0.0456 -0.1927 -0.8383 36  GLN C NE2 
8780  N N   . ALA C 37  ? 1.0573 1.1074 3.1822 -0.1122 -0.1968 -0.6363 37  ALA C N   
8781  C CA  . ALA C 37  ? 1.0150 1.0879 3.1238 -0.1170 -0.1906 -0.5854 37  ALA C CA  
8782  C C   . ALA C 37  ? 1.0003 1.1334 3.0634 -0.1172 -0.1976 -0.5949 37  ALA C C   
8783  O O   . ALA C 37  ? 1.0304 1.1846 3.1100 -0.1316 -0.2160 -0.6220 37  ALA C O   
8784  C CB  . ALA C 37  ? 1.0203 1.0701 3.1880 -0.1378 -0.1983 -0.5616 37  ALA C CB  
8785  N N   . PRO C 38  ? 0.9451 1.1080 2.9513 -0.1017 -0.1840 -0.5724 38  PRO C N   
8786  C CA  . PRO C 38  ? 0.9343 1.1550 2.8944 -0.0990 -0.1901 -0.5836 38  PRO C CA  
8787  C C   . PRO C 38  ? 0.9111 1.1643 2.8802 -0.1142 -0.2012 -0.5629 38  PRO C C   
8788  O O   . PRO C 38  ? 0.9126 1.2122 2.8581 -0.1168 -0.2131 -0.5822 38  PRO C O   
8789  C CB  . PRO C 38  ? 0.9076 1.1417 2.8134 -0.0783 -0.1707 -0.5592 38  PRO C CB  
8790  C CG  . PRO C 38  ? 0.8817 1.0715 2.8073 -0.0747 -0.1553 -0.5193 38  PRO C CG  
8791  C CD  . PRO C 38  ? 0.9071 1.0499 2.8927 -0.0862 -0.1630 -0.5361 38  PRO C CD  
8792  N N   . TYR C 39  ? 0.8829 1.1144 2.8870 -0.1242 -0.1975 -0.5241 39  TYR C N   
8793  C CA  . TYR C 39  ? 0.8766 1.1403 2.8912 -0.1375 -0.2062 -0.5019 39  TYR C CA  
8794  C C   . TYR C 39  ? 0.9133 1.1650 2.9888 -0.1605 -0.2251 -0.5215 39  TYR C C   
8795  O O   . TYR C 39  ? 0.8983 1.1780 2.9907 -0.1741 -0.2349 -0.5080 39  TYR C O   
8796  C CB  . TYR C 39  ? 0.8314 1.0887 2.8381 -0.1316 -0.1886 -0.4458 39  TYR C CB  
8797  C CG  . TYR C 39  ? 0.8050 1.0809 2.7525 -0.1108 -0.1728 -0.4267 39  TYR C CG  
8798  C CD1 . TYR C 39  ? 0.8140 1.1330 2.7153 -0.1020 -0.1768 -0.4455 39  TYR C CD1 
8799  C CD2 . TYR C 39  ? 0.7790 1.0302 2.7178 -0.1004 -0.1539 -0.3889 39  TYR C CD2 
8800  C CE1 . TYR C 39  ? 0.7940 1.1284 2.6455 -0.0840 -0.1622 -0.4259 39  TYR C CE1 
8801  C CE2 . TYR C 39  ? 0.7565 1.0222 2.6455 -0.0826 -0.1400 -0.3717 39  TYR C CE2 
8802  C CZ  . TYR C 39  ? 0.7596 1.0662 2.6062 -0.0746 -0.1440 -0.3893 39  TYR C CZ  
8803  O OH  . TYR C 39  ? 0.7282 1.0473 2.5300 -0.0581 -0.1301 -0.3697 39  TYR C OH  
8804  N N   . GLU C 40  ? 0.9533 1.1648 3.0640 -0.1650 -0.2307 -0.5542 40  GLU C N   
8805  C CA  . GLU C 40  ? 0.9873 1.1784 3.1630 -0.1874 -0.2475 -0.5703 40  GLU C CA  
8806  C C   . GLU C 40  ? 1.0433 1.2407 3.2266 -0.1925 -0.2667 -0.6331 40  GLU C C   
8807  O O   . GLU C 40  ? 1.0667 1.2721 3.2904 -0.2124 -0.2865 -0.6537 40  GLU C O   
8808  C CB  . GLU C 40  ? 0.9888 1.1209 3.2115 -0.1904 -0.2381 -0.5490 40  GLU C CB  
8809  C CG  . GLU C 40  ? 0.9504 1.0807 3.1713 -0.1887 -0.2216 -0.4878 40  GLU C CG  
8810  C CD  . GLU C 40  ? 0.9555 1.0352 3.2280 -0.1955 -0.2145 -0.4610 40  GLU C CD  
8811  O OE1 . GLU C 40  ? 0.9572 0.9986 3.2289 -0.1835 -0.2050 -0.4652 40  GLU C OE1 
8812  O OE2 . GLU C 40  ? 0.9500 1.0321 3.2638 -0.2129 -0.2187 -0.4347 40  GLU C OE2 
8813  N N   . ASP C 41  ? 1.0563 1.2516 3.2013 -0.1744 -0.2607 -0.6634 41  ASP C N   
8814  C CA  . ASP C 41  ? 1.1107 1.3087 3.2597 -0.1756 -0.2761 -0.7263 41  ASP C CA  
8815  C C   . ASP C 41  ? 1.1121 1.3747 3.2209 -0.1773 -0.2903 -0.7509 41  ASP C C   
8816  O O   . ASP C 41  ? 1.0904 1.3931 3.1444 -0.1649 -0.2808 -0.7277 41  ASP C O   
8817  C CB  . ASP C 41  ? 1.1261 1.3011 3.2491 -0.1543 -0.2625 -0.7476 41  ASP C CB  
8818  C CG  . ASP C 41  ? 1.1272 1.2384 3.2913 -0.1513 -0.2504 -0.7293 41  ASP C CG  
8819  O OD1 . ASP C 41  ? 1.1323 1.2100 3.3582 -0.1690 -0.2587 -0.7203 41  ASP C OD1 
8820  O OD2 . ASP C 41  ? 1.1210 1.2189 3.2558 -0.1315 -0.2328 -0.7211 41  ASP C OD2 
8821  N N   . GLU C 42  ? 1.1426 1.4146 3.2801 -0.1925 -0.3134 -0.7985 42  GLU C N   
8822  C CA  . GLU C 42  ? 1.1537 1.4856 3.2528 -0.1927 -0.3292 -0.8345 42  GLU C CA  
8823  C C   . GLU C 42  ? 1.1395 1.4954 3.1699 -0.1676 -0.3151 -0.8470 42  GLU C C   
8824  O O   . GLU C 42  ? 1.1638 1.4992 3.1910 -0.1576 -0.3129 -0.8877 42  GLU C O   
8825  C CB  . GLU C 42  ? 1.2100 1.5338 3.3506 -0.2082 -0.3536 -0.8962 42  GLU C CB  
8826  C CG  . GLU C 42  ? 1.2436 1.5278 3.3901 -0.1962 -0.3493 -0.9419 42  GLU C CG  
8827  C CD  . GLU C 42  ? 1.2996 1.5624 3.4965 -0.2107 -0.3719 -1.0036 42  GLU C CD  
8828  O OE1 . GLU C 42  ? 1.3102 1.5904 3.5406 -0.2327 -0.3942 -1.0167 42  GLU C OE1 
8829  O OE2 . GLU C 42  ? 1.3260 1.5543 3.5293 -0.1989 -0.3668 -1.0394 42  GLU C OE2 
8830  N N   . ARG C 43  ? 1.1005 1.5000 3.0783 -0.1571 -0.3052 -0.8108 43  ARG C N   
8831  C CA  . ARG C 43  ? 1.0828 1.4964 3.0011 -0.1331 -0.2860 -0.8043 43  ARG C CA  
8832  C C   . ARG C 43  ? 1.1193 1.5565 3.0093 -0.1244 -0.2937 -0.8651 43  ARG C C   
8833  O O   . ARG C 43  ? 1.1556 1.6115 3.0616 -0.1368 -0.3156 -0.9098 43  ARG C O   
8834  C CB  . ARG C 43  ? 1.0452 1.5061 2.9148 -0.1252 -0.2775 -0.7582 43  ARG C CB  
8835  C CG  . ARG C 43  ? 1.0623 1.5877 2.9110 -0.1334 -0.2970 -0.7715 43  ARG C CG  
8836  C CD  . ARG C 43  ? 1.0213 1.5843 2.8383 -0.1285 -0.2897 -0.7185 43  ARG C CD  
8837  N NE  . ARG C 43  ? 1.0385 1.6575 2.8520 -0.1403 -0.3114 -0.7275 43  ARG C NE  
8838  C CZ  . ARG C 43  ? 1.0103 1.6712 2.8028 -0.1390 -0.3117 -0.6884 43  ARG C CZ  
8839  N NH1 . ARG C 43  ? 0.9652 1.6197 2.7347 -0.1256 -0.2910 -0.6392 43  ARG C NH1 
8840  N NH2 . ARG C 43  ? 1.0278 1.7376 2.8239 -0.1509 -0.3335 -0.6999 43  ARG C NH2 
8841  N N   . LYS C 44  ? 1.0994 1.5354 2.9492 -0.1030 -0.2750 -0.8667 44  LYS C N   
8842  C CA  . LYS C 44  ? 1.1298 1.5972 2.9419 -0.0908 -0.2776 -0.9181 44  LYS C CA  
8843  C C   . LYS C 44  ? 1.0970 1.5968 2.8455 -0.0694 -0.2569 -0.8906 44  LYS C C   
8844  O O   . LYS C 44  ? 1.0483 1.5273 2.7929 -0.0632 -0.2393 -0.8399 44  LYS C O   
8845  C CB  . LYS C 44  ? 1.1615 1.5781 3.0124 -0.0887 -0.2784 -0.9651 44  LYS C CB  
8846  C CG  . LYS C 44  ? 1.2102 1.6580 3.0323 -0.0787 -0.2851 -1.0293 44  LYS C CG  
8847  C CD  . LYS C 44  ? 1.2438 1.7460 3.0542 -0.0915 -0.3101 -1.0649 44  LYS C CD  
8848  C CE  . LYS C 44  ? 1.2956 1.8317 3.0725 -0.0798 -0.3149 -1.1278 44  LYS C CE  
8849  N NZ  . LYS C 44  ? 1.3293 1.9218 3.0918 -0.0922 -0.3398 -1.1600 44  LYS C NZ  
8850  N N   . ASP C 45  ? 1.1245 1.6770 2.8244 -0.0590 -0.2596 -0.9241 45  ASP C N   
8851  C CA  . ASP C 45  ? 1.1053 1.6949 2.7448 -0.0394 -0.2411 -0.9015 45  ASP C CA  
8852  C C   . ASP C 45  ? 1.1000 1.6484 2.7410 -0.0228 -0.2192 -0.9026 45  ASP C C   
8853  O O   . ASP C 45  ? 1.0607 1.6091 2.6761 -0.0107 -0.1996 -0.8603 45  ASP C O   
8854  C CB  . ASP C 45  ? 1.1416 1.8017 2.7308 -0.0335 -0.2506 -0.9382 45  ASP C CB  
8855  C CG  . ASP C 45  ? 1.1539 1.8595 2.7421 -0.0497 -0.2753 -0.9467 45  ASP C CG  
8856  O OD1 . ASP C 45  ? 1.1257 1.8117 2.7504 -0.0652 -0.2835 -0.9167 45  ASP C OD1 
8857  O OD2 . ASP C 45  ? 1.1906 1.9531 2.7420 -0.0463 -0.2861 -0.9835 45  ASP C OD2 
8858  N N   . GLU C 46  ? 1.1400 1.6545 2.8124 -0.0221 -0.2233 -0.9524 46  GLU C N   
8859  C CA  . GLU C 46  ? 1.1405 1.6153 2.8209 -0.0063 -0.2047 -0.9591 46  GLU C CA  
8860  C C   . GLU C 46  ? 1.1333 1.6525 2.7523 0.0142  -0.1861 -0.9489 46  GLU C C   
8861  O O   . GLU C 46  ? 1.0909 1.5921 2.7012 0.0249  -0.1661 -0.9092 46  GLU C O   
8862  C CB  . GLU C 46  ? 1.0991 1.5124 2.8188 -0.0091 -0.1931 -0.9117 46  GLU C CB  
8863  C CG  . GLU C 46  ? 1.1071 1.4746 2.8911 -0.0296 -0.2093 -0.9151 46  GLU C CG  
8864  C CD  . GLU C 46  ? 1.0855 1.3858 2.9143 -0.0289 -0.1975 -0.8866 46  GLU C CD  
8865  O OE1 . GLU C 46  ? 1.0645 1.3514 2.8762 -0.0122 -0.1776 -0.8674 46  GLU C OE1 
8866  O OE2 . GLU C 46  ? 1.0906 1.3535 2.9732 -0.0457 -0.2090 -0.8828 46  GLU C OE2 
8867  N N   . LEU C 47  ? 1.1731 1.7527 2.7506 0.0190  -0.1934 -0.9853 47  LEU C N   
8868  C CA  . LEU C 47  ? 1.1753 1.8054 2.6937 0.0376  -0.1770 -0.9786 47  LEU C CA  
8869  C C   . LEU C 47  ? 1.1844 1.7799 2.7117 0.0546  -0.1570 -0.9901 47  LEU C C   
8870  O O   . LEU C 47  ? 1.1600 1.7636 2.6607 0.0676  -0.1367 -0.9541 47  LEU C O   
8871  C CB  . LEU C 47  ? 1.2207 1.9197 2.6975 0.0401  -0.1892 -1.0246 47  LEU C CB  
8872  C CG  . LEU C 47  ? 1.2255 1.9657 2.6933 0.0236  -0.2120 -1.0213 47  LEU C CG  
8873  C CD1 . LEU C 47  ? 1.1689 1.9025 2.6391 0.0159  -0.2084 -0.9519 47  LEU C CD1 
8874  C CD2 . LEU C 47  ? 1.2626 1.9789 2.7775 0.0064  -0.2367 -1.0696 47  LEU C CD2 
8875  N N   . GLU C 48  ? 1.2253 1.7821 2.7933 0.0542  -0.1637 -1.0403 48  GLU C N   
8876  C CA  . GLU C 48  ? 1.2379 1.7659 2.8172 0.0715  -0.1471 -1.0614 48  GLU C CA  
8877  C C   . GLU C 48  ? 1.1864 1.6765 2.7757 0.0774  -0.1273 -1.0027 48  GLU C C   
8878  O O   . GLU C 48  ? 1.1681 1.6831 2.7214 0.0929  -0.1082 -0.9829 48  GLU C O   
8879  C CB  . GLU C 48  ? 1.2809 1.7622 2.9147 0.0671  -0.1600 -1.1176 48  GLU C CB  
8880  C CG  . GLU C 48  ? 1.3417 1.8632 2.9630 0.0635  -0.1789 -1.1829 48  GLU C CG  
8881  C CD  . GLU C 48  ? 1.3783 1.9618 2.9446 0.0830  -0.1695 -1.2207 48  GLU C CD  
8882  O OE1 . GLU C 48  ? 1.3851 1.9583 2.9492 0.1020  -0.1510 -1.2335 48  GLU C OE1 
8883  O OE2 . GLU C 48  ? 1.4027 2.0484 2.9285 0.0788  -0.1815 -1.2384 48  GLU C OE2 
8884  N N   . LEU C 49  ? 1.1642 1.5980 2.8010 0.0642  -0.1323 -0.9732 49  LEU C N   
8885  C CA  . LEU C 49  ? 1.1235 1.5161 2.7753 0.0693  -0.1153 -0.9228 49  LEU C CA  
8886  C C   . LEU C 49  ? 1.0883 1.5184 2.6925 0.0737  -0.1025 -0.8690 49  LEU C C   
8887  O O   . LEU C 49  ? 1.0652 1.4787 2.6654 0.0840  -0.0846 -0.8357 49  LEU C O   
8888  C CB  . LEU C 49  ? 1.1047 1.4364 2.8144 0.0531  -0.1246 -0.9015 49  LEU C CB  
8889  C CG  . LEU C 49  ? 1.1374 1.4149 2.9057 0.0509  -0.1324 -0.9418 49  LEU C CG  
8890  C CD1 . LEU C 49  ? 1.1127 1.3367 2.9333 0.0341  -0.1395 -0.9077 49  LEU C CD1 
8891  C CD2 . LEU C 49  ? 1.1458 1.4003 2.9220 0.0710  -0.1160 -0.9583 49  LEU C CD2 
8892  N N   . MET C 50  ? 1.0909 1.5711 2.6613 0.0660  -0.1120 -0.8597 50  MET C N   
8893  C CA  . MET C 50  ? 1.0555 1.5718 2.5830 0.0702  -0.1009 -0.8096 50  MET C CA  
8894  C C   . MET C 50  ? 1.0629 1.6162 2.5486 0.0896  -0.0829 -0.8156 50  MET C C   
8895  O O   . MET C 50  ? 1.0326 1.5831 2.5044 0.0973  -0.0663 -0.7732 50  MET C O   
8896  C CB  . MET C 50  ? 1.0613 1.6260 2.5632 0.0590  -0.1157 -0.7990 50  MET C CB  
8897  C CG  . MET C 50  ? 1.0375 1.5724 2.5719 0.0419  -0.1262 -0.7646 50  MET C CG  
8898  S SD  . MET C 50  ? 1.0419 1.6343 2.5512 0.0294  -0.1440 -0.7506 50  MET C SD  
8899  C CE  . MET C 50  ? 0.9986 1.6235 2.4612 0.0409  -0.1257 -0.6899 50  MET C CE  
8900  N N   . LYS C 51  ? 1.1044 1.6922 2.5716 0.0976  -0.0856 -0.8681 51  LYS C N   
8901  C CA  . LYS C 51  ? 1.1117 1.7411 2.5381 0.1161  -0.0675 -0.8728 51  LYS C CA  
8902  C C   . LYS C 51  ? 1.0950 1.6793 2.5453 0.1280  -0.0486 -0.8602 51  LYS C C   
8903  O O   . LYS C 51  ? 1.0703 1.6757 2.4937 0.1389  -0.0307 -0.8296 51  LYS C O   
8904  C CB  . LYS C 51  ? 1.1635 1.8478 2.5588 0.1243  -0.0719 -0.9295 51  LYS C CB  
8905  C CG  . LYS C 51  ? 1.2093 1.8823 2.6310 0.1159  -0.0927 -0.9897 51  LYS C CG  
8906  C CD  . LYS C 51  ? 1.2632 2.0016 2.6438 0.1249  -0.0964 -1.0419 51  LYS C CD  
8907  C CE  . LYS C 51  ? 1.3135 2.0449 2.7182 0.1152  -0.1193 -1.1027 51  LYS C CE  
8908  N NZ  . LYS C 51  ? 1.3060 2.0426 2.7180 0.0945  -0.1412 -1.0880 51  LYS C NZ  
8909  N N   . PHE C 52  ? 1.1089 1.6316 2.6116 0.1250  -0.0532 -0.8798 52  PHE C N   
8910  C CA  . PHE C 52  ? 1.0997 1.5771 2.6303 0.1357  -0.0375 -0.8679 52  PHE C CA  
8911  C C   . PHE C 52  ? 1.0477 1.5041 2.5791 0.1317  -0.0285 -0.8021 52  PHE C C   
8912  O O   . PHE C 52  ? 1.0236 1.4775 2.5475 0.1434  -0.0109 -0.7785 52  PHE C O   
8913  C CB  . PHE C 52  ? 1.1202 1.5366 2.7096 0.1328  -0.0463 -0.9018 52  PHE C CB  
8914  C CG  . PHE C 52  ? 1.0939 1.4543 2.7220 0.1406  -0.0340 -0.8827 52  PHE C CG  
8915  C CD1 . PHE C 52  ? 1.0989 1.4606 2.7283 0.1599  -0.0188 -0.9041 52  PHE C CD1 
8916  C CD2 . PHE C 52  ? 1.0600 1.3679 2.7252 0.1289  -0.0382 -0.8441 52  PHE C CD2 
8917  C CE1 . PHE C 52  ? 1.0773 1.3897 2.7438 0.1669  -0.0091 -0.8857 52  PHE C CE1 
8918  C CE2 . PHE C 52  ? 1.0350 1.2946 2.7349 0.1360  -0.0282 -0.8261 52  PHE C CE2 
8919  C CZ  . PHE C 52  ? 1.0440 1.3055 2.7450 0.1549  -0.0143 -0.8467 52  PHE C CZ  
8920  N N   . ASP C 53  ? 1.0316 1.4734 2.5738 0.1152  -0.0408 -0.7741 53  ASP C N   
8921  C CA  . ASP C 53  ? 0.9868 1.4093 2.5298 0.1110  -0.0335 -0.7147 53  ASP C CA  
8922  C C   . ASP C 53  ? 0.9741 1.4506 2.4655 0.1169  -0.0234 -0.6840 53  ASP C C   
8923  O O   . ASP C 53  ? 0.9452 1.4203 2.4263 0.1265  -0.0070 -0.6555 53  ASP C O   
8924  C CB  . ASP C 53  ? 0.9733 1.3665 2.5449 0.0928  -0.0489 -0.6970 53  ASP C CB  
8925  C CG  . ASP C 53  ? 0.9930 1.3323 2.6194 0.0856  -0.0591 -0.7236 53  ASP C CG  
8926  O OD1 . ASP C 53  ? 1.0092 1.3203 2.6573 0.0961  -0.0513 -0.7432 53  ASP C OD1 
8927  O OD2 . ASP C 53  ? 1.0005 1.3282 2.6493 0.0697  -0.0750 -0.7253 53  ASP C OD2 
8928  N N   . LEU C 54  ? 0.9991 1.5237 2.4605 0.1109  -0.0340 -0.6903 54  LEU C N   
8929  C CA  . LEU C 54  ? 0.9890 1.5676 2.4033 0.1147  -0.0272 -0.6593 54  LEU C CA  
8930  C C   . LEU C 54  ? 0.9919 1.5976 2.3799 0.1316  -0.0077 -0.6598 54  LEU C C   
8931  O O   . LEU C 54  ? 0.9895 1.6231 2.3491 0.1354  0.0027  -0.6208 54  LEU C O   
8932  C CB  . LEU C 54  ? 1.0194 1.6524 2.4050 0.1085  -0.0422 -0.6782 54  LEU C CB  
8933  C CG  . LEU C 54  ? 1.0008 1.6350 2.3911 0.0934  -0.0568 -0.6494 54  LEU C CG  
8934  C CD1 . LEU C 54  ? 0.9934 1.5704 2.4343 0.0800  -0.0687 -0.6545 54  LEU C CD1 
8935  C CD2 . LEU C 54  ? 1.0346 1.7314 2.3923 0.0901  -0.0706 -0.6715 54  LEU C CD2 
8936  N N   . GLU C 55  ? 1.0100 1.6103 2.4082 0.1416  -0.0030 -0.7043 55  GLU C N   
8937  C CA  . GLU C 55  ? 1.0047 1.6297 2.3831 0.1584  0.0164  -0.7072 55  GLU C CA  
8938  C C   . GLU C 55  ? 0.9558 1.5335 2.3609 0.1628  0.0301  -0.6741 55  GLU C C   
8939  O O   . GLU C 55  ? 0.9328 1.5314 2.3184 0.1712  0.0460  -0.6456 55  GLU C O   
8940  C CB  . GLU C 55  ? 1.0534 1.6938 2.4330 0.1684  0.0160  -0.7694 55  GLU C CB  
8941  C CG  . GLU C 55  ? 1.0682 1.7509 2.4200 0.1864  0.0361  -0.7766 55  GLU C CG  
8942  C CD  . GLU C 55  ? 1.0637 1.8137 2.3636 0.1887  0.0436  -0.7467 55  GLU C CD  
8943  O OE1 . GLU C 55  ? 1.0796 1.8690 2.3527 0.1817  0.0307  -0.7549 55  GLU C OE1 
8944  O OE2 . GLU C 55  ? 1.0458 1.8100 2.3335 0.1973  0.0617  -0.7147 55  GLU C OE2 
8945  N N   . ASN C 56  ? 0.9414 1.4573 2.3920 0.1567  0.0233  -0.6771 56  ASN C N   
8946  C CA  . ASN C 56  ? 0.9096 1.3792 2.3872 0.1593  0.0333  -0.6445 56  ASN C CA  
8947  C C   . ASN C 56  ? 0.8675 1.3418 2.3282 0.1529  0.0370  -0.5876 56  ASN C C   
8948  O O   . ASN C 56  ? 0.8493 1.3214 2.3053 0.1597  0.0511  -0.5576 56  ASN C O   
8949  C CB  . ASN C 56  ? 0.9189 1.3251 2.4476 0.1526  0.0235  -0.6568 56  ASN C CB  
8950  C CG  . ASN C 56  ? 0.9744 1.3665 2.5279 0.1618  0.0229  -0.7096 56  ASN C CG  
8951  O OD1 . ASN C 56  ? 1.0029 1.4305 2.5364 0.1756  0.0326  -0.7367 56  ASN C OD1 
8952  N ND2 . ASN C 56  ? 0.9907 1.3313 2.5900 0.1549  0.0118  -0.7250 56  ASN C ND2 
8953  N N   . ILE C 57  ? 0.8597 1.3417 2.3122 0.1400  0.0240  -0.5736 57  ILE C N   
8954  C CA  . ILE C 57  ? 0.8155 1.3005 2.2546 0.1342  0.0262  -0.5220 57  ILE C CA  
8955  C C   . ILE C 57  ? 0.8069 1.3425 2.2060 0.1432  0.0395  -0.5023 57  ILE C C   
8956  O O   . ILE C 57  ? 0.7779 1.3084 2.1717 0.1435  0.0479  -0.4599 57  ILE C O   
8957  C CB  . ILE C 57  ? 0.8131 1.3025 2.2518 0.1199  0.0096  -0.5139 57  ILE C CB  
8958  C CG1 . ILE C 57  ? 0.8072 1.2406 2.2897 0.1094  -0.0004 -0.5145 57  ILE C CG1 
8959  C CG2 . ILE C 57  ? 0.7824 1.2949 2.1961 0.1173  0.0127  -0.4662 57  ILE C CG2 
8960  C CD1 . ILE C 57  ? 0.8429 1.2553 2.3540 0.1081  -0.0092 -0.5634 57  ILE C CD1 
8961  N N   . LYS C 58  ? 0.8368 1.4219 2.2086 0.1502  0.0411  -0.5328 58  LYS C N   
8962  C CA  . LYS C 58  ? 0.8403 1.4768 2.1757 0.1593  0.0550  -0.5153 58  LYS C CA  
8963  C C   . LYS C 58  ? 0.8272 1.4473 2.1748 0.1704  0.0729  -0.5072 58  LYS C C   
8964  O O   . LYS C 58  ? 0.8041 1.4344 2.1408 0.1727  0.0842  -0.4679 58  LYS C O   
8965  C CB  . LYS C 58  ? 0.8825 1.5802 2.1841 0.1640  0.0519  -0.5504 58  LYS C CB  
8966  C CG  . LYS C 58  ? 0.8893 1.6195 2.1689 0.1539  0.0364  -0.5439 58  LYS C CG  
8967  C CD  . LYS C 58  ? 0.9293 1.7313 2.1668 0.1593  0.0351  -0.5676 58  LYS C CD  
8968  C CE  . LYS C 58  ? 0.9718 1.7827 2.2119 0.1656  0.0320  -0.6293 58  LYS C CE  
8969  N NZ  . LYS C 58  ? 1.0110 1.8952 2.2071 0.1705  0.0299  -0.6513 58  LYS C NZ  
8970  N N   . GLU C 59  ? 0.8416 1.4348 2.2151 0.1769  0.0748  -0.5435 59  GLU C N   
8971  C CA  . GLU C 59  ? 0.8346 1.4109 2.2244 0.1877  0.0905  -0.5373 59  GLU C CA  
8972  C C   . GLU C 59  ? 0.7906 1.3182 2.2043 0.1814  0.0914  -0.4940 59  GLU C C   
8973  O O   . GLU C 59  ? 0.7804 1.3052 2.1977 0.1876  0.1046  -0.4705 59  GLU C O   
8974  C CB  . GLU C 59  ? 0.8652 1.4234 2.2800 0.1969  0.0911  -0.5871 59  GLU C CB  
8975  C CG  . GLU C 59  ? 0.9113 1.5251 2.2987 0.2073  0.0956  -0.6292 59  GLU C CG  
8976  C CD  . GLU C 59  ? 0.9519 1.5491 2.3636 0.2152  0.0919  -0.6870 59  GLU C CD  
8977  O OE1 . GLU C 59  ? 0.9506 1.4896 2.4043 0.2116  0.0840  -0.6966 59  GLU C OE1 
8978  O OE2 . GLU C 59  ? 0.9863 1.6301 2.3752 0.2253  0.0968  -0.7239 59  GLU C OE2 
8979  N N   . GLY C 60  ? 0.7673 1.2598 2.1971 0.1689  0.0775  -0.4834 60  GLY C N   
8980  C CA  . GLY C 60  ? 0.7325 1.1792 2.1847 0.1631  0.0774  -0.4460 60  GLY C CA  
8981  C C   . GLY C 60  ? 0.7086 1.1738 2.1388 0.1612  0.0845  -0.3990 60  GLY C C   
8982  O O   . GLY C 60  ? 0.6801 1.1114 2.1258 0.1577  0.0860  -0.3678 60  GLY C O   
8983  N N   . GLY C 61  ? 0.7198 1.2388 2.1147 0.1631  0.0879  -0.3942 61  GLY C N   
8984  C CA  . GLY C 61  ? 0.7009 1.2418 2.0757 0.1622  0.0952  -0.3507 61  GLY C CA  
8985  C C   . GLY C 61  ? 0.6972 1.2497 2.0571 0.1523  0.0840  -0.3293 61  GLY C C   
8986  O O   . GLY C 61  ? 0.6718 1.2432 2.0160 0.1512  0.0884  -0.2929 61  GLY C O   
8987  N N   . TYR C 62  ? 0.7155 1.2578 2.0829 0.1453  0.0694  -0.3520 62  TYR C N   
8988  C CA  . TYR C 62  ? 0.7109 1.2534 2.0744 0.1353  0.0575  -0.3315 62  TYR C CA  
8989  C C   . TYR C 62  ? 0.7270 1.3279 2.0570 0.1350  0.0522  -0.3372 62  TYR C C   
8990  O O   . TYR C 62  ? 0.7541 1.3843 2.0716 0.1389  0.0504  -0.3737 62  TYR C O   
8991  C CB  . TYR C 62  ? 0.7179 1.2190 2.1109 0.1265  0.0442  -0.3497 62  TYR C CB  
8992  C CG  . TYR C 62  ? 0.7078 1.1520 2.1350 0.1263  0.0477  -0.3452 62  TYR C CG  
8993  C CD1 . TYR C 62  ? 0.7264 1.1508 2.1726 0.1323  0.0514  -0.3756 62  TYR C CD1 
8994  C CD2 . TYR C 62  ? 0.6821 1.0939 2.1234 0.1207  0.0468  -0.3111 62  TYR C CD2 
8995  C CE1 . TYR C 62  ? 0.7175 1.0921 2.1954 0.1323  0.0537  -0.3692 62  TYR C CE1 
8996  C CE2 . TYR C 62  ? 0.6715 1.0354 2.1418 0.1206  0.0494  -0.3058 62  TYR C CE2 
8997  C CZ  . TYR C 62  ? 0.6887 1.0342 2.1775 0.1262  0.0525  -0.3336 62  TYR C CZ  
8998  O OH  . TYR C 62  ? 0.6814 0.9815 2.1991 0.1263  0.0543  -0.3256 62  TYR C OH  
8999  N N   . ASN C 63  ? 0.7096 1.3274 2.0262 0.1308  0.0491  -0.3013 63  ASN C N   
9000  C CA  . ASN C 63  ? 0.7329 1.4078 2.0181 0.1306  0.0434  -0.2985 63  ASN C CA  
9001  C C   . ASN C 63  ? 0.7493 1.4246 2.0400 0.1207  0.0251  -0.3057 63  ASN C C   
9002  O O   . ASN C 63  ? 0.7730 1.4961 2.0400 0.1197  0.0168  -0.3120 63  ASN C O   
9003  C CB  . ASN C 63  ? 0.7114 1.4101 1.9792 0.1334  0.0520  -0.2519 63  ASN C CB  
9004  C CG  . ASN C 63  ? 0.6768 1.3405 1.9628 0.1273  0.0482  -0.2152 63  ASN C CG  
9005  O OD1 . ASN C 63  ? 0.6596 1.2808 1.9709 0.1212  0.0407  -0.2225 63  ASN C OD1 
9006  N ND2 . ASN C 63  ? 0.6675 1.3486 1.9423 0.1292  0.0536  -0.1750 63  ASN C ND2 
9007  N N   . THR C 64  ? 0.7315 1.3565 2.0538 0.1134  0.0189  -0.3027 64  THR C N   
9008  C CA  . THR C 64  ? 0.7357 1.3589 2.0682 0.1034  0.0028  -0.3029 64  THR C CA  
9009  C C   . THR C 64  ? 0.7425 1.3176 2.1104 0.0964  -0.0042 -0.3283 64  THR C C   
9010  O O   . THR C 64  ? 0.7293 1.2646 2.1161 0.0994  0.0044  -0.3316 64  THR C O   
9011  C CB  . THR C 64  ? 0.7100 1.3269 2.0441 0.1015  0.0038  -0.2557 64  THR C CB  
9012  O OG1 . THR C 64  ? 0.7222 1.3875 2.0246 0.1080  0.0094  -0.2367 64  THR C OG1 
9013  C CG2 . THR C 64  ? 0.7084 1.3246 2.0556 0.0920  -0.0115 -0.2511 64  THR C CG2 
9014  N N   . ILE C 65  ? 0.7592 1.3402 2.1370 0.0868  -0.0203 -0.3438 65  ILE C N   
9015  C CA  . ILE C 65  ? 0.7661 1.3059 2.1801 0.0780  -0.0291 -0.3658 65  ILE C CA  
9016  C C   . ILE C 65  ? 0.7565 1.2907 2.1857 0.0679  -0.0395 -0.3420 65  ILE C C   
9017  O O   . ILE C 65  ? 0.7615 1.3351 2.1709 0.0671  -0.0452 -0.3263 65  ILE C O   
9018  C CB  . ILE C 65  ? 0.8090 1.3660 2.2226 0.0762  -0.0388 -0.4172 65  ILE C CB  
9019  C CG1 . ILE C 65  ? 0.8150 1.3254 2.2704 0.0679  -0.0468 -0.4435 65  ILE C CG1 
9020  C CG2 . ILE C 65  ? 0.8319 1.4439 2.2219 0.0720  -0.0526 -0.4265 65  ILE C CG2 
9021  C CD1 . ILE C 65  ? 0.8567 1.3826 2.3145 0.0658  -0.0577 -0.4965 65  ILE C CD1 
9022  N N   . ARG C 66  ? 0.7551 1.2422 2.2195 0.0609  -0.0411 -0.3366 66  ARG C N   
9023  C CA  . ARG C 66  ? 0.7499 1.2294 2.2326 0.0518  -0.0490 -0.3133 66  ARG C CA  
9024  C C   . ARG C 66  ? 0.7783 1.2355 2.2966 0.0394  -0.0618 -0.3392 66  ARG C C   
9025  O O   . ARG C 66  ? 0.7997 1.2185 2.3410 0.0386  -0.0587 -0.3553 66  ARG C O   
9026  C CB  . ARG C 66  ? 0.7232 1.1687 2.2144 0.0556  -0.0366 -0.2750 66  ARG C CB  
9027  C CG  . ARG C 66  ? 0.7166 1.1437 2.2325 0.0476  -0.0411 -0.2513 66  ARG C CG  
9028  C CD  . ARG C 66  ? 0.7215 1.1014 2.2738 0.0409  -0.0412 -0.2591 66  ARG C CD  
9029  N NE  . ARG C 66  ? 0.7001 1.0589 2.2711 0.0371  -0.0389 -0.2278 66  ARG C NE  
9030  C CZ  . ARG C 66  ? 0.6944 1.0549 2.2884 0.0267  -0.0482 -0.2234 66  ARG C CZ  
9031  N NH1 . ARG C 66  ? 0.7139 1.1036 2.3114 0.0188  -0.0623 -0.2437 66  ARG C NH1 
9032  N NH2 . ARG C 66  ? 0.6771 1.0141 2.2898 0.0246  -0.0434 -0.1975 66  ARG C NH2 
9033  N N   . THR C 67  ? 0.7954 1.2766 2.3207 0.0295  -0.0764 -0.3414 67  THR C N   
9034  C CA  . THR C 67  ? 0.8182 1.2835 2.3793 0.0160  -0.0903 -0.3666 67  THR C CA  
9035  C C   . THR C 67  ? 0.7803 1.2283 2.3698 0.0070  -0.0929 -0.3364 67  THR C C   
9036  O O   . THR C 67  ? 0.7508 1.2037 2.3292 0.0121  -0.0852 -0.2998 67  THR C O   
9037  C CB  . THR C 67  ? 0.8636 1.3727 2.4142 0.0103  -0.1069 -0.4006 67  THR C CB  
9038  O OG1 . THR C 67  ? 0.8608 1.4088 2.3999 0.0072  -0.1147 -0.3778 67  THR C OG1 
9039  C CG2 . THR C 67  ? 0.8972 1.4352 2.4118 0.0211  -0.1029 -0.4264 67  THR C CG2 
9040  N N   . TRP C 68  ? 0.7875 1.2146 2.4157 -0.0062 -0.1033 -0.3525 68  TRP C N   
9041  C CA  . TRP C 68  ? 0.7683 1.1861 2.4268 -0.0167 -0.1077 -0.3283 68  TRP C CA  
9042  C C   . TRP C 68  ? 0.7640 1.2147 2.4365 -0.0298 -0.1272 -0.3471 68  TRP C C   
9043  O O   . TRP C 68  ? 0.7358 1.1920 2.4311 -0.0388 -0.1327 -0.3277 68  TRP C O   
9044  C CB  . TRP C 68  ? 0.7871 1.1522 2.4845 -0.0223 -0.1026 -0.3249 68  TRP C CB  
9045  C CG  . TRP C 68  ? 0.7907 1.1249 2.4771 -0.0103 -0.0845 -0.3016 68  TRP C CG  
9046  C CD1 . TRP C 68  ? 0.7695 1.0869 2.4608 -0.0078 -0.0742 -0.2641 68  TRP C CD1 
9047  C CD2 . TRP C 68  ? 0.8127 1.1326 2.4810 0.0010  -0.0750 -0.3156 68  TRP C CD2 
9048  N NE1 . TRP C 68  ? 0.7642 1.0572 2.4416 0.0036  -0.0602 -0.2542 68  TRP C NE1 
9049  C CE2 . TRP C 68  ? 0.8087 1.1031 2.4728 0.0091  -0.0602 -0.2841 68  TRP C CE2 
9050  C CE3 . TRP C 68  ? 0.8624 1.1905 2.5182 0.0056  -0.0774 -0.3523 68  TRP C CE3 
9051  C CZ2 . TRP C 68  ? 0.8357 1.1128 2.4852 0.0207  -0.0485 -0.2869 68  TRP C CZ2 
9052  C CZ3 . TRP C 68  ? 0.8899 1.2012 2.5314 0.0179  -0.0646 -0.3547 68  TRP C CZ3 
9053  C CH2 . TRP C 68  ? 0.8574 1.1438 2.4966 0.0250  -0.0506 -0.3217 68  TRP C CH2 
9054  N N   . SER C 69  ? 0.7899 1.2645 2.4486 -0.0306 -0.1375 -0.3859 69  SER C N   
9055  C CA  . SER C 69  ? 0.8149 1.3185 2.4886 -0.0439 -0.1579 -0.4121 69  SER C CA  
9056  C C   . SER C 69  ? 0.8331 1.3873 2.4660 -0.0378 -0.1655 -0.4371 69  SER C C   
9057  O O   . SER C 69  ? 0.8376 1.3964 2.4374 -0.0246 -0.1550 -0.4442 69  SER C O   
9058  C CB  . SER C 69  ? 0.8433 1.3113 2.5602 -0.0564 -0.1664 -0.4436 69  SER C CB  
9059  O OG  . SER C 69  ? 0.8843 1.3724 2.6293 -0.0730 -0.1855 -0.4552 69  SER C OG  
9060  N N   . GLN C 70  ? 0.8460 1.4409 2.4826 -0.0478 -0.1841 -0.4498 70  GLN C N   
9061  C CA  . GLN C 70  ? 0.8671 1.5200 2.4633 -0.0427 -0.1930 -0.4659 70  GLN C CA  
9062  C C   . GLN C 70  ? 0.9090 1.5649 2.4982 -0.0432 -0.2003 -0.5203 70  GLN C C   
9063  O O   . GLN C 70  ? 0.9253 1.5583 2.5512 -0.0557 -0.2118 -0.5524 70  GLN C O   
9064  C CB  . GLN C 70  ? 0.8697 1.5679 2.4727 -0.0529 -0.2114 -0.4584 70  GLN C CB  
9065  C CG  . GLN C 70  ? 0.8834 1.5647 2.5387 -0.0725 -0.2271 -0.4746 70  GLN C CG  
9066  C CD  . GLN C 70  ? 0.8485 1.4991 2.5398 -0.0779 -0.2197 -0.4340 70  GLN C CD  
9067  O OE1 . GLN C 70  ? 0.8236 1.4326 2.5180 -0.0704 -0.2012 -0.4107 70  GLN C OE1 
9068  N NE2 . GLN C 70  ? 0.8369 1.5106 2.5559 -0.0910 -0.2343 -0.4261 70  GLN C NE2 
9069  N N   . TYR C 71  ? 0.9278 1.6131 2.4710 -0.0292 -0.1932 -0.5301 71  TYR C N   
9070  C CA  . TYR C 71  ? 0.9699 1.6690 2.4987 -0.0269 -0.1992 -0.5826 71  TYR C CA  
9071  C C   . TYR C 71  ? 0.9947 1.7486 2.5148 -0.0361 -0.2225 -0.6112 71  TYR C C   
9072  O O   . TYR C 71  ? 0.9791 1.7662 2.4968 -0.0415 -0.2319 -0.5854 71  TYR C O   
9073  C CB  . TYR C 71  ? 0.9731 1.6885 2.4558 -0.0082 -0.1816 -0.5793 71  TYR C CB  
9074  C CG  . TYR C 71  ? 0.9630 1.6245 2.4555 0.0011  -0.1608 -0.5690 71  TYR C CG  
9075  C CD1 . TYR C 71  ? 0.9604 1.5622 2.4997 -0.0063 -0.1601 -0.5782 71  TYR C CD1 
9076  C CD2 . TYR C 71  ? 0.9579 1.6303 2.4142 0.0171  -0.1423 -0.5501 71  TYR C CD2 
9077  C CE1 . TYR C 71  ? 0.9426 1.4984 2.4908 0.0025  -0.1423 -0.5685 71  TYR C CE1 
9078  C CE2 . TYR C 71  ? 0.9298 1.5562 2.3959 0.0254  -0.1245 -0.5416 71  TYR C CE2 
9079  C CZ  . TYR C 71  ? 0.9220 1.4903 2.4335 0.0184  -0.1248 -0.5510 71  TYR C CZ  
9080  O OH  . TYR C 71  ? 0.8892 1.4132 2.4124 0.0263  -0.1086 -0.5416 71  TYR C OH  
9081  N N   . SER C 72  ? 1.0319 1.7946 2.5494 -0.0378 -0.2323 -0.6663 72  SER C N   
9082  C CA  . SER C 72  ? 1.0708 1.8918 2.5703 -0.0439 -0.2538 -0.7005 72  SER C CA  
9083  C C   . SER C 72  ? 1.0765 1.9563 2.5135 -0.0278 -0.2470 -0.6987 72  SER C C   
9084  O O   . SER C 72  ? 1.0543 1.9245 2.4673 -0.0131 -0.2257 -0.6758 72  SER C O   
9085  C CB  . SER C 72  ? 1.1188 1.9218 2.6462 -0.0533 -0.2683 -0.7624 72  SER C CB  
9086  O OG  . SER C 72  ? 1.1380 1.9190 2.6524 -0.0403 -0.2541 -0.7909 72  SER C OG  
9087  N N   . GLU C 73  ? 1.1052 2.0478 2.5176 -0.0315 -0.2658 -0.7224 73  GLU C N   
9088  C CA  . GLU C 73  ? 1.1216 2.1283 2.4742 -0.0175 -0.2619 -0.7231 73  GLU C CA  
9089  C C   . GLU C 73  ? 1.1515 2.1494 2.4852 -0.0058 -0.2501 -0.7654 73  GLU C C   
9090  O O   . GLU C 73  ? 1.1572 2.1798 2.4492 0.0100  -0.2331 -0.7501 73  GLU C O   
9091  C CB  . GLU C 73  ? 1.1511 2.2254 2.4877 -0.0261 -0.2873 -0.7380 73  GLU C CB  
9092  C CG  . GLU C 73  ? 1.1670 2.3169 2.4415 -0.0129 -0.2852 -0.7248 73  GLU C CG  
9093  C CD  . GLU C 73  ? 1.2250 2.4213 2.4646 -0.0083 -0.2935 -0.7831 73  GLU C CD  
9094  O OE1 . GLU C 73  ? 1.2594 2.4915 2.5016 -0.0193 -0.3183 -0.8201 73  GLU C OE1 
9095  O OE2 . GLU C 73  ? 1.2400 2.4371 2.4505 0.0063  -0.2751 -0.7929 73  GLU C OE2 
9096  N N   . ASN C 74  ? 1.1737 2.1346 2.5417 -0.0135 -0.2585 -0.8168 74  ASN C N   
9097  C CA  . ASN C 74  ? 1.1942 2.1381 2.5542 -0.0024 -0.2473 -0.8597 74  ASN C CA  
9098  C C   . ASN C 74  ? 1.1505 2.0458 2.5153 0.0097  -0.2201 -0.8248 74  ASN C C   
9099  O O   . ASN C 74  ? 1.1578 2.0688 2.4891 0.0258  -0.2034 -0.8297 74  ASN C O   
9100  C CB  . ASN C 74  ? 1.2251 2.1297 2.6307 -0.0137 -0.2620 -0.9176 74  ASN C CB  
9101  C CG  . ASN C 74  ? 1.2706 2.2272 2.6662 -0.0233 -0.2885 -0.9654 74  ASN C CG  
9102  O OD1 . ASN C 74  ? 1.3050 2.3166 2.6541 -0.0130 -0.2896 -0.9968 74  ASN C OD1 
9103  N ND2 . ASN C 74  ? 1.2711 2.2135 2.7096 -0.0432 -0.3098 -0.9718 74  ASN C ND2 
9104  N N   . GLN C 75  ? 1.1078 1.9461 2.5150 0.0017  -0.2161 -0.7901 75  GLN C N   
9105  C CA  . GLN C 75  ? 1.0684 1.8606 2.4824 0.0117  -0.1923 -0.7541 75  GLN C CA  
9106  C C   . GLN C 75  ? 1.0505 1.8825 2.4175 0.0245  -0.1772 -0.7076 75  GLN C C   
9107  O O   . GLN C 75  ? 1.0539 1.8772 2.4034 0.0384  -0.1573 -0.6983 75  GLN C O   
9108  C CB  . GLN C 75  ? 1.0273 1.7578 2.4941 -0.0004 -0.1930 -0.7260 75  GLN C CB  
9109  C CG  . GLN C 75  ? 1.0448 1.7282 2.5634 -0.0122 -0.2047 -0.7683 75  GLN C CG  
9110  C CD  . GLN C 75  ? 1.0069 1.6396 2.5769 -0.0261 -0.2076 -0.7381 75  GLN C CD  
9111  O OE1 . GLN C 75  ? 0.9868 1.6372 2.5637 -0.0366 -0.2174 -0.7108 75  GLN C OE1 
9112  N NE2 . GLN C 75  ? 0.9968 1.5678 2.6046 -0.0261 -0.1991 -0.7418 75  GLN C NE2 
9113  N N   . LEU C 76  ? 1.0450 1.9215 2.3936 0.0200  -0.1869 -0.6784 76  LEU C N   
9114  C CA  . LEU C 76  ? 1.0229 1.9355 2.3322 0.0311  -0.1741 -0.6305 76  LEU C CA  
9115  C C   . LEU C 76  ? 1.0487 2.0097 2.3091 0.0457  -0.1647 -0.6500 76  LEU C C   
9116  O O   . LEU C 76  ? 1.0223 1.9862 2.2609 0.0578  -0.1451 -0.6182 76  LEU C O   
9117  C CB  . LEU C 76  ? 1.0178 1.9727 2.3188 0.0239  -0.1885 -0.5994 76  LEU C CB  
9118  C CG  . LEU C 76  ? 0.9766 1.8929 2.3159 0.0147  -0.1900 -0.5578 76  LEU C CG  
9119  C CD1 . LEU C 76  ? 0.9630 1.9259 2.2786 0.0178  -0.1924 -0.5113 76  LEU C CD1 
9120  C CD2 . LEU C 76  ? 0.9399 1.7897 2.3039 0.0187  -0.1703 -0.5329 76  LEU C CD2 
9121  N N   . LYS C 77  ? 1.0976 2.0986 2.3416 0.0443  -0.1787 -0.7019 77  LYS C N   
9122  C CA  . LYS C 77  ? 1.1331 2.1919 2.3266 0.0580  -0.1712 -0.7211 77  LYS C CA  
9123  C C   . LYS C 77  ? 1.1373 2.1626 2.3318 0.0710  -0.1486 -0.7328 77  LYS C C   
9124  O O   . LYS C 77  ? 1.1489 2.2129 2.3040 0.0848  -0.1335 -0.7247 77  LYS C O   
9125  C CB  . LYS C 77  ? 1.1863 2.2970 2.3606 0.0544  -0.1914 -0.7782 77  LYS C CB  
9126  C CG  . LYS C 77  ? 1.2133 2.2851 2.4240 0.0468  -0.2029 -0.8415 77  LYS C CG  
9127  C CD  . LYS C 77  ? 1.2713 2.3934 2.4519 0.0520  -0.2121 -0.9053 77  LYS C CD  
9128  C CE  . LYS C 77  ? 1.3028 2.4902 2.4610 0.0431  -0.2371 -0.9230 77  LYS C CE  
9129  N NZ  . LYS C 77  ? 1.3161 2.4736 2.5208 0.0245  -0.2615 -0.9573 77  LYS C NZ  
9130  N N   . LEU C 78  ? 1.1333 2.0884 2.3746 0.0663  -0.1466 -0.7495 78  LEU C N   
9131  C CA  . LEU C 78  ? 1.1361 2.0530 2.3869 0.0778  -0.1270 -0.7619 78  LEU C CA  
9132  C C   . LEU C 78  ? 1.0832 1.9815 2.3286 0.0856  -0.1056 -0.7029 78  LEU C C   
9133  O O   . LEU C 78  ? 1.0784 1.9916 2.3004 0.0995  -0.0871 -0.6986 78  LEU C O   
9134  C CB  . LEU C 78  ? 1.1464 1.9949 2.4527 0.0689  -0.1343 -0.7935 78  LEU C CB  
9135  C CG  . LEU C 78  ? 1.1676 1.9815 2.4882 0.0804  -0.1203 -0.8270 78  LEU C CG  
9136  C CD1 . LEU C 78  ? 1.2286 2.0874 2.5241 0.0877  -0.1258 -0.8885 78  LEU C CD1 
9137  C CD2 . LEU C 78  ? 1.1591 1.8957 2.5402 0.0713  -0.1246 -0.8365 78  LEU C CD2 
9138  N N   . VAL C 79  ? 1.0392 1.9061 2.3080 0.0764  -0.1083 -0.6587 79  VAL C N   
9139  C CA  . VAL C 79  ? 0.9933 1.8421 2.2593 0.0821  -0.0909 -0.6023 79  VAL C CA  
9140  C C   . VAL C 79  ? 0.9912 1.9046 2.2078 0.0914  -0.0832 -0.5745 79  VAL C C   
9141  O O   . VAL C 79  ? 0.9741 1.8855 2.1782 0.1013  -0.0642 -0.5446 79  VAL C O   
9142  C CB  . VAL C 79  ? 0.9586 1.7704 2.2560 0.0704  -0.0976 -0.5636 79  VAL C CB  
9143  C CG1 . VAL C 79  ? 0.9166 1.7155 2.2076 0.0767  -0.0808 -0.5065 79  VAL C CG1 
9144  C CG2 . VAL C 79  ? 0.9554 1.7028 2.3034 0.0608  -0.1035 -0.5840 79  VAL C CG2 
9145  N N   . GLN C 80  ? 1.0092 1.9800 2.2003 0.0875  -0.0986 -0.5821 80  GLN C N   
9146  C CA  . GLN C 80  ? 1.0152 2.0532 2.1595 0.0956  -0.0938 -0.5554 80  GLN C CA  
9147  C C   . GLN C 80  ? 1.0372 2.1021 2.1521 0.1099  -0.0766 -0.5752 80  GLN C C   
9148  O O   . GLN C 80  ? 1.0239 2.1019 2.1204 0.1190  -0.0589 -0.5377 80  GLN C O   
9149  C CB  . GLN C 80  ? 1.0459 2.1426 2.1695 0.0890  -0.1159 -0.5710 80  GLN C CB  
9150  C CG  . GLN C 80  ? 1.0515 2.2197 2.1296 0.0957  -0.1140 -0.5351 80  GLN C CG  
9151  C CD  . GLN C 80  ? 1.0060 2.1618 2.0929 0.0945  -0.1095 -0.4697 80  GLN C CD  
9152  O OE1 . GLN C 80  ? 0.9753 2.0888 2.0978 0.0850  -0.1175 -0.4543 80  GLN C OE1 
9153  N NE2 . GLN C 80  ? 1.0019 2.1945 2.0581 0.1044  -0.0960 -0.4304 80  GLN C NE2 
9154  N N   . GLU C 81  ? 1.0707 2.1416 2.1849 0.1116  -0.0820 -0.6350 81  GLU C N   
9155  C CA  . GLU C 81  ? 1.0969 2.2028 2.1816 0.1257  -0.0678 -0.6637 81  GLU C CA  
9156  C C   . GLU C 81  ? 1.0710 2.1308 2.1735 0.1348  -0.0446 -0.6491 81  GLU C C   
9157  O O   . GLU C 81  ? 1.0774 2.1710 2.1524 0.1474  -0.0270 -0.6430 81  GLU C O   
9158  C CB  . GLU C 81  ? 1.1394 2.2572 2.2256 0.1234  -0.0832 -0.7337 81  GLU C CB  
9159  C CG  . GLU C 81  ? 1.1714 2.3055 2.2422 0.1379  -0.0692 -0.7782 81  GLU C CG  
9160  C CD  . GLU C 81  ? 1.2201 2.3631 2.2954 0.1355  -0.0857 -0.8501 81  GLU C CD  
9161  O OE1 . GLU C 81  ? 1.2332 2.3858 2.3141 0.1225  -0.1088 -0.8636 81  GLU C OE1 
9162  O OE2 . GLU C 81  ? 1.2476 2.3873 2.3234 0.1466  -0.0759 -0.8936 81  GLU C OE2 
9163  N N   . SER C 82  ? 1.0418 2.0275 2.1906 0.1281  -0.0447 -0.6410 82  SER C N   
9164  C CA  . SER C 82  ? 1.0226 1.9593 2.1945 0.1357  -0.0260 -0.6340 82  SER C CA  
9165  C C   . SER C 82  ? 0.9932 1.9445 2.1464 0.1431  -0.0069 -0.5795 82  SER C C   
9166  O O   . SER C 82  ? 0.9866 1.9289 2.1411 0.1535  0.0112  -0.5792 82  SER C O   
9167  C CB  . SER C 82  ? 0.9972 1.8572 2.2203 0.1258  -0.0321 -0.6305 82  SER C CB  
9168  O OG  . SER C 82  ? 0.9648 1.8121 2.1966 0.1152  -0.0399 -0.5858 82  SER C OG  
9169  N N   . GLY C 83  ? 0.9732 1.9445 2.1133 0.1375  -0.0117 -0.5334 83  GLY C N   
9170  C CA  . GLY C 83  ? 0.9435 1.9205 2.0734 0.1421  0.0039  -0.4777 83  GLY C CA  
9171  C C   . GLY C 83  ? 0.9004 1.8196 2.0636 0.1337  0.0018  -0.4377 83  GLY C C   
9172  O O   . GLY C 83  ? 0.8740 1.7984 2.0306 0.1347  0.0093  -0.3887 83  GLY C O   
9173  N N   . LEU C 84  ? 0.8957 1.7613 2.0951 0.1255  -0.0084 -0.4593 84  LEU C N   
9174  C CA  . LEU C 84  ? 0.8608 1.6690 2.0939 0.1183  -0.0092 -0.4271 84  LEU C CA  
9175  C C   . LEU C 84  ? 0.8573 1.6814 2.0871 0.1098  -0.0223 -0.3965 84  LEU C C   
9176  O O   . LEU C 84  ? 0.8725 1.7404 2.0844 0.1063  -0.0362 -0.4128 84  LEU C O   
9177  C CB  . LEU C 84  ? 0.8563 1.6078 2.1289 0.1126  -0.0155 -0.4606 84  LEU C CB  
9178  C CG  . LEU C 84  ? 0.8546 1.5743 2.1420 0.1213  -0.0014 -0.4806 84  LEU C CG  
9179  C CD1 . LEU C 84  ? 0.8627 1.5341 2.1883 0.1159  -0.0101 -0.5190 84  LEU C CD1 
9180  C CD2 . LEU C 84  ? 0.8158 1.5044 2.1127 0.1248  0.0136  -0.4360 84  LEU C CD2 
9181  N N   . LYS C 85  ? 0.8346 1.6234 2.0825 0.1072  -0.0179 -0.3535 85  LYS C N   
9182  C CA  . LYS C 85  ? 0.8319 1.6243 2.0856 0.0999  -0.0287 -0.3222 85  LYS C CA  
9183  C C   . LYS C 85  ? 0.8276 1.5686 2.1207 0.0895  -0.0386 -0.3320 85  LYS C C   
9184  O O   . LYS C 85  ? 0.8169 1.5121 2.1341 0.0889  -0.0337 -0.3501 85  LYS C O   
9185  C CB  . LYS C 85  ? 0.8019 1.5889 2.0520 0.1044  -0.0172 -0.2687 85  LYS C CB  
9186  C CG  . LYS C 85  ? 0.8132 1.6431 2.0309 0.1142  -0.0044 -0.2501 85  LYS C CG  
9187  C CD  . LYS C 85  ? 0.8482 1.7488 2.0307 0.1160  -0.0126 -0.2537 85  LYS C CD  
9188  C CE  . LYS C 85  ? 0.8599 1.8011 2.0138 0.1252  0.0016  -0.2262 85  LYS C CE  
9189  N NZ  . LYS C 85  ? 0.8995 1.9126 2.0160 0.1284  -0.0042 -0.2380 85  LYS C NZ  
9190  N N   . LEU C 86  ? 0.8334 1.5837 2.1345 0.0815  -0.0522 -0.3171 86  LEU C N   
9191  C CA  . LEU C 86  ? 0.8370 1.5534 2.1734 0.0700  -0.0647 -0.3323 86  LEU C CA  
9192  C C   . LEU C 86  ? 0.8058 1.5091 2.1585 0.0657  -0.0674 -0.2914 86  LEU C C   
9193  O O   . LEU C 86  ? 0.7962 1.5390 2.1331 0.0665  -0.0735 -0.2691 86  LEU C O   
9194  C CB  . LEU C 86  ? 0.8809 1.6316 2.2133 0.0628  -0.0830 -0.3727 86  LEU C CB  
9195  C CG  . LEU C 86  ? 0.8883 1.6129 2.2584 0.0488  -0.0986 -0.3893 86  LEU C CG  
9196  C CD1 . LEU C 86  ? 0.8710 1.5296 2.2794 0.0450  -0.0922 -0.3945 86  LEU C CD1 
9197  C CD2 . LEU C 86  ? 0.9327 1.6896 2.2981 0.0425  -0.1157 -0.4376 86  LEU C CD2 
9198  N N   . ILE C 87  ? 0.7890 1.4378 2.1737 0.0620  -0.0627 -0.2821 87  ILE C N   
9199  C CA  . ILE C 87  ? 0.7751 1.4064 2.1824 0.0565  -0.0664 -0.2525 87  ILE C CA  
9200  C C   . ILE C 87  ? 0.7968 1.4178 2.2336 0.0436  -0.0816 -0.2790 87  ILE C C   
9201  O O   . ILE C 87  ? 0.7957 1.3718 2.2610 0.0386  -0.0795 -0.2905 87  ILE C O   
9202  C CB  . ILE C 87  ? 0.7511 1.3329 2.1740 0.0606  -0.0516 -0.2255 87  ILE C CB  
9203  C CG1 . ILE C 87  ? 0.7593 1.3419 2.1587 0.0721  -0.0357 -0.2109 87  ILE C CG1 
9204  C CG2 . ILE C 87  ? 0.7201 1.2940 2.1588 0.0581  -0.0534 -0.1908 87  ILE C CG2 
9205  C CD1 . ILE C 87  ? 0.7674 1.3883 2.1417 0.0788  -0.0332 -0.1783 87  ILE C CD1 
9206  N N   . MET C 88  ? 0.8251 1.4895 2.2555 0.0378  -0.0975 -0.2888 88  MET C N   
9207  C CA  . MET C 88  ? 0.8402 1.5035 2.2972 0.0244  -0.1143 -0.3188 88  MET C CA  
9208  C C   . MET C 88  ? 0.8049 1.4421 2.2979 0.0160  -0.1173 -0.2951 88  MET C C   
9209  O O   . MET C 88  ? 0.7923 1.4498 2.2828 0.0176  -0.1188 -0.2632 88  MET C O   
9210  C CB  . MET C 88  ? 0.8839 1.6078 2.3207 0.0212  -0.1311 -0.3350 88  MET C CB  
9211  C CG  . MET C 88  ? 0.9340 1.6611 2.3937 0.0076  -0.1494 -0.3769 88  MET C CG  
9212  S SD  . MET C 88  ? 1.0009 1.8041 2.4364 0.0037  -0.1707 -0.3898 88  MET C SD  
9213  C CE  . MET C 88  ? 1.0453 1.8443 2.4975 -0.0078 -0.1866 -0.4552 88  MET C CE  
9214  N N   . GLY C 89  ? 0.7992 1.3935 2.3275 0.0071  -0.1184 -0.3112 89  GLY C N   
9215  C CA  . GLY C 89  ? 0.7780 1.3486 2.3427 -0.0018 -0.1208 -0.2911 89  GLY C CA  
9216  C C   . GLY C 89  ? 0.8003 1.3930 2.3892 -0.0167 -0.1409 -0.3118 89  GLY C C   
9217  O O   . GLY C 89  ? 0.8121 1.4093 2.4061 -0.0234 -0.1516 -0.3516 89  GLY C O   
9218  N N   . ILE C 90  ? 0.8000 1.4077 2.4047 -0.0213 -0.1458 -0.2848 90  ILE C N   
9219  C CA  . ILE C 90  ? 0.8197 1.4493 2.4527 -0.0362 -0.1645 -0.2976 90  ILE C CA  
9220  C C   . ILE C 90  ? 0.8349 1.4229 2.5138 -0.0464 -0.1613 -0.2866 90  ILE C C   
9221  O O   . ILE C 90  ? 0.8108 1.3760 2.4932 -0.0398 -0.1469 -0.2531 90  ILE C O   
9222  C CB  . ILE C 90  ? 0.7957 1.4781 2.4142 -0.0334 -0.1727 -0.2747 90  ILE C CB  
9223  C CG1 . ILE C 90  ? 0.8207 1.5538 2.4069 -0.0319 -0.1860 -0.3001 90  ILE C CG1 
9224  C CG2 . ILE C 90  ? 0.7862 1.4776 2.4446 -0.0461 -0.1836 -0.2633 90  ILE C CG2 
9225  C CD1 . ILE C 90  ? 0.8274 1.5620 2.3716 -0.0181 -0.1743 -0.3070 90  ILE C CD1 
9226  N N   . ASP C 91  ? 0.8856 1.4646 2.5995 -0.0623 -0.1749 -0.3151 91  ASP C N   
9227  C CA  . ASP C 91  ? 0.8755 1.4109 2.6347 -0.0729 -0.1715 -0.3090 91  ASP C CA  
9228  C C   . ASP C 91  ? 0.8599 1.4034 2.6368 -0.0741 -0.1669 -0.2679 91  ASP C C   
9229  O O   . ASP C 91  ? 0.8769 1.4061 2.6397 -0.0622 -0.1505 -0.2365 91  ASP C O   
9230  C CB  . ASP C 91  ? 0.8726 1.3973 2.6673 -0.0898 -0.1875 -0.3482 91  ASP C CB  
9231  C CG  . ASP C 91  ? 0.8484 1.3165 2.6808 -0.0965 -0.1807 -0.3514 91  ASP C CG  
9232  O OD1 . ASP C 91  ? 0.8032 1.2406 2.6321 -0.0876 -0.1631 -0.3233 91  ASP C OD1 
9233  O OD2 . ASP C 91  ? 0.8588 1.3137 2.7248 -0.1104 -0.1936 -0.3823 91  ASP C OD2 
9234  N N   . ILE C 92  ? 0.8518 1.4205 2.6593 -0.0878 -0.1813 -0.2680 92  ILE C N   
9235  C CA  . ILE C 92  ? 0.8333 1.4060 2.6640 -0.0894 -0.1755 -0.2306 92  ILE C CA  
9236  C C   . ILE C 92  ? 0.8093 1.3302 2.6641 -0.0908 -0.1603 -0.2158 92  ILE C C   
9237  O O   . ILE C 92  ? 0.7472 1.2471 2.5822 -0.0773 -0.1429 -0.1926 92  ILE C O   
9238  C CB  . ILE C 92  ? 0.8183 1.4206 2.6154 -0.0730 -0.1676 -0.1997 92  ILE C CB  
9239  C CG1 . ILE C 92  ? 0.8224 1.4824 2.6087 -0.0748 -0.1850 -0.2062 92  ILE C CG1 
9240  C CG2 . ILE C 92  ? 0.8091 1.4014 2.6249 -0.0692 -0.1544 -0.1602 92  ILE C CG2 
9241  C CD1 . ILE C 92  ? 0.8505 1.5289 2.6142 -0.0776 -0.1988 -0.2459 92  ILE C CD1 
9242  N N   . LYS C 93  ? 0.8383 1.3396 2.7372 -0.1078 -0.1682 -0.2300 93  LYS C N   
9243  C CA  . LYS C 93  ? 0.8186 1.2754 2.7480 -0.1123 -0.1565 -0.2145 93  LYS C CA  
9244  C C   . LYS C 93  ? 0.7695 1.2281 2.6956 -0.1031 -0.1403 -0.1710 93  LYS C C   
9245  O O   . LYS C 93  ? 0.7717 1.2642 2.7089 -0.1055 -0.1437 -0.1528 93  LYS C O   
9246  C CB  . LYS C 93  ? 0.8486 1.2995 2.8340 -0.1344 -0.1695 -0.2254 93  LYS C CB  
9247  C CG  . LYS C 93  ? 0.8831 1.3371 2.8831 -0.1473 -0.1895 -0.2707 93  LYS C CG  
9248  C CD  . LYS C 93  ? 0.8823 1.2990 2.8688 -0.1420 -0.1869 -0.3005 93  LYS C CD  
9249  C CE  . LYS C 93  ? 0.9116 1.3403 2.9080 -0.1529 -0.2075 -0.3474 93  LYS C CE  
9250  N NZ  . LYS C 93  ? 0.9376 1.3226 2.9421 -0.1523 -0.2061 -0.3764 93  LYS C NZ  
9251  N N   . PRO C 94  ? 0.7110 1.1339 2.6242 -0.0923 -0.1224 -0.1537 94  PRO C N   
9252  C CA  . PRO C 94  ? 0.6637 1.0874 2.5707 -0.0822 -0.1066 -0.1157 94  PRO C CA  
9253  C C   . PRO C 94  ? 0.6400 1.0683 2.5896 -0.0931 -0.1044 -0.0924 94  PRO C C   
9254  O O   . PRO C 94  ? 0.5990 1.0433 2.5445 -0.0851 -0.0946 -0.0641 94  PRO C O   
9255  C CB  . PRO C 94  ? 0.6573 1.0387 2.5437 -0.0709 -0.0910 -0.1107 94  PRO C CB  
9256  C CG  . PRO C 94  ? 0.6793 1.0312 2.5824 -0.0803 -0.0981 -0.1397 94  PRO C CG  
9257  C CD  . PRO C 94  ? 0.7148 1.0960 2.6197 -0.0889 -0.1170 -0.1710 94  PRO C CD  
9258  N N   . GLU C 95  ? 0.6442 1.0578 2.6356 -0.1110 -0.1129 -0.1046 95  GLU C N   
9259  C CA  . GLU C 95  ? 0.6322 1.0444 2.6673 -0.1226 -0.1090 -0.0811 95  GLU C CA  
9260  C C   . GLU C 95  ? 0.6200 1.0751 2.6853 -0.1359 -0.1233 -0.0819 95  GLU C C   
9261  O O   . GLU C 95  ? 0.6090 1.0693 2.7153 -0.1476 -0.1217 -0.0634 95  GLU C O   
9262  C CB  . GLU C 95  ? 0.6688 1.0421 2.7414 -0.1366 -0.1104 -0.0883 95  GLU C CB  
9263  C CG  . GLU C 95  ? 0.6958 1.0247 2.7463 -0.1264 -0.1004 -0.0940 95  GLU C CG  
9264  C CD  . GLU C 95  ? 0.7525 1.0681 2.7851 -0.1248 -0.1109 -0.1333 95  GLU C CD  
9265  O OE1 . GLU C 95  ? 0.7755 1.1183 2.8107 -0.1321 -0.1269 -0.1576 95  GLU C OE1 
9266  O OE2 . GLU C 95  ? 0.7733 1.0542 2.7897 -0.1162 -0.1035 -0.1404 95  GLU C OE2 
9267  N N   . GLU C 96  ? 0.6181 1.1057 2.6645 -0.1343 -0.1373 -0.1020 96  GLU C N   
9268  C CA  . GLU C 96  ? 0.6207 1.1536 2.6936 -0.1459 -0.1522 -0.1027 96  GLU C CA  
9269  C C   . GLU C 96  ? 0.5845 1.1510 2.6473 -0.1335 -0.1425 -0.0698 96  GLU C C   
9270  O O   . GLU C 96  ? 0.5597 1.1174 2.5866 -0.1146 -0.1273 -0.0536 96  GLU C O   
9271  C CB  . GLU C 96  ? 0.6488 1.2096 2.7076 -0.1499 -0.1729 -0.1368 96  GLU C CB  
9272  C CG  . GLU C 96  ? 0.6886 1.2255 2.7653 -0.1647 -0.1870 -0.1755 96  GLU C CG  
9273  C CD  . GLU C 96  ? 0.7097 1.2250 2.8458 -0.1857 -0.1913 -0.1751 96  GLU C CD  
9274  O OE1 . GLU C 96  ? 0.7014 1.2447 2.8762 -0.1986 -0.1976 -0.1606 96  GLU C OE1 
9275  O OE2 . GLU C 96  ? 0.7314 1.2017 2.8765 -0.1889 -0.1881 -0.1887 96  GLU C OE2 
9276  N N   . ASP C 97  ? 0.5680 1.1736 2.6653 -0.1443 -0.1522 -0.0615 97  ASP C N   
9277  C CA  . ASP C 97  ? 0.5417 1.1810 2.6409 -0.1343 -0.1434 -0.0300 97  ASP C CA  
9278  C C   . ASP C 97  ? 0.5447 1.2215 2.6099 -0.1213 -0.1518 -0.0341 97  ASP C C   
9279  O O   . ASP C 97  ? 0.5652 1.2804 2.6453 -0.1308 -0.1705 -0.0463 97  ASP C O   
9280  C CB  . ASP C 97  ? 0.5386 1.2010 2.6948 -0.1523 -0.1485 -0.0174 97  ASP C CB  
9281  C CG  . ASP C 97  ? 0.5147 1.2211 2.6834 -0.1447 -0.1429 0.0118  97  ASP C CG  
9282  O OD1 . ASP C 97  ? 0.4893 1.2026 2.6220 -0.1235 -0.1322 0.0258  97  ASP C OD1 
9283  O OD2 . ASP C 97  ? 0.5135 1.2474 2.7303 -0.1605 -0.1500 0.0197  97  ASP C OD2 
9284  N N   . TYR C 98  ? 0.5228 1.1905 2.5455 -0.0997 -0.1378 -0.0209 98  TYR C N   
9285  C CA  . TYR C 98  ? 0.5194 1.2131 2.5036 -0.0856 -0.1437 -0.0243 98  TYR C CA  
9286  C C   . TYR C 98  ? 0.5153 1.2635 2.5167 -0.0845 -0.1532 -0.0096 98  TYR C C   
9287  O O   . TYR C 98  ? 0.5136 1.2939 2.4952 -0.0806 -0.1666 -0.0185 98  TYR C O   
9288  C CB  . TYR C 98  ? 0.5037 1.1740 2.4469 -0.0636 -0.1251 -0.0081 98  TYR C CB  
9289  C CG  . TYR C 98  ? 0.5038 1.1219 2.4273 -0.0612 -0.1136 -0.0180 98  TYR C CG  
9290  C CD1 . TYR C 98  ? 0.5300 1.1308 2.4431 -0.0694 -0.1233 -0.0489 98  TYR C CD1 
9291  C CD2 . TYR C 98  ? 0.4830 1.0704 2.3994 -0.0505 -0.0936 0.0025  98  TYR C CD2 
9292  C CE1 . TYR C 98  ? 0.5251 1.0801 2.4233 -0.0667 -0.1133 -0.0576 98  TYR C CE1 
9293  C CE2 . TYR C 98  ? 0.4782 1.0207 2.3787 -0.0486 -0.0843 -0.0057 98  TYR C CE2 
9294  C CZ  . TYR C 98  ? 0.5000 1.0263 2.3924 -0.0566 -0.0941 -0.0350 98  TYR C CZ  
9295  O OH  . TYR C 98  ? 0.5083 0.9923 2.3883 -0.0548 -0.0862 -0.0441 98  TYR C OH  
9296  N N   . GLY C 99  ? 0.5084 1.2691 2.5463 -0.0872 -0.1457 0.0141  99  GLY C N   
9297  C CA  . GLY C 99  ? 0.5105 1.3228 2.5702 -0.0849 -0.1524 0.0314  99  GLY C CA  
9298  C C   . GLY C 99  ? 0.5391 1.3815 2.6453 -0.1081 -0.1714 0.0194  99  GLY C C   
9299  O O   . GLY C 99  ? 0.5274 1.4074 2.6687 -0.1113 -0.1738 0.0370  99  GLY C O   
9300  N N   . ASP C 100 ? 0.5751 1.3998 2.6829 -0.1243 -0.1848 -0.0118 100 ASP C N   
9301  C CA  . ASP C 100 ? 0.6024 1.4510 2.7525 -0.1479 -0.2056 -0.0299 100 ASP C CA  
9302  C C   . ASP C 100 ? 0.6452 1.5253 2.7710 -0.1490 -0.2279 -0.0564 100 ASP C C   
9303  O O   . ASP C 100 ? 0.6535 1.5098 2.7473 -0.1482 -0.2320 -0.0829 100 ASP C O   
9304  C CB  . ASP C 100 ? 0.5998 1.4036 2.7746 -0.1651 -0.2036 -0.0450 100 ASP C CB  
9305  C CG  . ASP C 100 ? 0.6116 1.4325 2.8372 -0.1917 -0.2243 -0.0639 100 ASP C CG  
9306  O OD1 . ASP C 100 ? 0.6208 1.4908 2.8585 -0.1971 -0.2422 -0.0692 100 ASP C OD1 
9307  O OD2 . ASP C 100 ? 0.6200 1.4045 2.8730 -0.2063 -0.2225 -0.0723 100 ASP C OD2 
9308  N N   . PRO C 101 ? 0.6776 1.6143 2.8165 -0.1496 -0.2424 -0.0491 101 PRO C N   
9309  C CA  . PRO C 101 ? 0.7182 1.6920 2.8280 -0.1469 -0.2625 -0.0686 101 PRO C CA  
9310  C C   . PRO C 101 ? 0.7847 1.7470 2.8853 -0.1620 -0.2802 -0.1125 101 PRO C C   
9311  O O   . PRO C 101 ? 0.8245 1.8022 2.8831 -0.1541 -0.2893 -0.1296 101 PRO C O   
9312  C CB  . PRO C 101 ? 0.7079 1.7428 2.8534 -0.1531 -0.2779 -0.0556 101 PRO C CB  
9313  C CG  . PRO C 101 ? 0.6781 1.7092 2.8524 -0.1460 -0.2577 -0.0184 101 PRO C CG  
9314  C CD  . PRO C 101 ? 0.6673 1.6388 2.8501 -0.1520 -0.2401 -0.0206 101 PRO C CD  
9315  N N   . GLU C 102 ? 0.8190 1.7565 2.9603 -0.1832 -0.2850 -0.1301 102 GLU C N   
9316  C CA  . GLU C 102 ? 0.8582 1.7813 2.9974 -0.1981 -0.3019 -0.1745 102 GLU C CA  
9317  C C   . GLU C 102 ? 0.8325 1.7103 2.9227 -0.1844 -0.2887 -0.1882 102 GLU C C   
9318  O O   . GLU C 102 ? 0.8576 1.7412 2.9179 -0.1843 -0.3011 -0.2211 102 GLU C O   
9319  C CB  . GLU C 102 ? 0.8924 1.7990 3.0913 -0.2248 -0.3120 -0.1908 102 GLU C CB  
9320  C CG  . GLU C 102 ? 0.8903 1.7495 3.1207 -0.2286 -0.2910 -0.1679 102 GLU C CG  
9321  C CD  . GLU C 102 ? 0.9213 1.7621 3.2118 -0.2559 -0.3022 -0.1849 102 GLU C CD  
9322  O OE1 . GLU C 102 ? 0.9258 1.7233 3.2400 -0.2602 -0.2865 -0.1705 102 GLU C OE1 
9323  O OE2 . GLU C 102 ? 0.9534 1.8238 3.2692 -0.2736 -0.3273 -0.2119 102 GLU C OE2 
9324  N N   . PHE C 103 ? 0.7842 1.6203 2.8659 -0.1725 -0.2639 -0.1632 103 PHE C N   
9325  C CA  . PHE C 103 ? 0.7630 1.5567 2.8016 -0.1593 -0.2504 -0.1731 103 PHE C CA  
9326  C C   . PHE C 103 ? 0.7417 1.5647 2.7263 -0.1406 -0.2516 -0.1716 103 PHE C C   
9327  O O   . PHE C 103 ? 0.7501 1.5647 2.6994 -0.1363 -0.2550 -0.1978 103 PHE C O   
9328  C CB  . PHE C 103 ? 0.7329 1.4824 2.7732 -0.1497 -0.2245 -0.1436 103 PHE C CB  
9329  C CG  . PHE C 103 ? 0.7428 1.4456 2.7459 -0.1386 -0.2114 -0.1550 103 PHE C CG  
9330  C CD1 . PHE C 103 ? 0.7709 1.4552 2.7655 -0.1459 -0.2216 -0.1939 103 PHE C CD1 
9331  C CD2 . PHE C 103 ? 0.7279 1.4066 2.7060 -0.1206 -0.1891 -0.1274 103 PHE C CD2 
9332  C CE1 . PHE C 103 ? 0.7777 1.4219 2.7405 -0.1350 -0.2091 -0.2032 103 PHE C CE1 
9333  C CE2 . PHE C 103 ? 0.7325 1.3710 2.6787 -0.1109 -0.1778 -0.1370 103 PHE C CE2 
9334  C CZ  . PHE C 103 ? 0.7637 1.3856 2.7029 -0.1180 -0.1874 -0.1739 103 PHE C CZ  
9335  N N   . VAL C 104 ? 0.7082 1.5672 2.6898 -0.1298 -0.2487 -0.1400 104 VAL C N   
9336  C CA  . VAL C 104 ? 0.6960 1.5835 2.6311 -0.1111 -0.2483 -0.1301 104 VAL C CA  
9337  C C   . VAL C 104 ? 0.7044 1.6351 2.6249 -0.1185 -0.2730 -0.1609 104 VAL C C   
9338  O O   . VAL C 104 ? 0.7062 1.6438 2.5811 -0.1079 -0.2738 -0.1723 104 VAL C O   
9339  C CB  . VAL C 104 ? 0.6809 1.5969 2.6231 -0.0980 -0.2407 -0.0892 104 VAL C CB  
9340  C CG1 . VAL C 104 ? 0.6816 1.6157 2.5760 -0.0767 -0.2364 -0.0744 104 VAL C CG1 
9341  C CG2 . VAL C 104 ? 0.6573 1.5364 2.6219 -0.0937 -0.2185 -0.0623 104 VAL C CG2 
9342  N N   . LYS C 105 ? 0.7035 1.6645 2.6633 -0.1372 -0.2930 -0.1748 105 LYS C N   
9343  C CA  . LYS C 105 ? 0.7252 1.7330 2.6736 -0.1452 -0.3186 -0.2048 105 LYS C CA  
9344  C C   . LYS C 105 ? 0.7393 1.7185 2.6684 -0.1520 -0.3237 -0.2496 105 LYS C C   
9345  O O   . LYS C 105 ? 0.7583 1.7632 2.6461 -0.1458 -0.3330 -0.2700 105 LYS C O   
9346  C CB  . LYS C 105 ? 0.7298 1.7820 2.7268 -0.1623 -0.3388 -0.2040 105 LYS C CB  
9347  C CG  . LYS C 105 ? 0.7461 1.7773 2.7945 -0.1877 -0.3494 -0.2305 105 LYS C CG  
9348  C CD  . LYS C 105 ? 0.7455 1.8138 2.8507 -0.2037 -0.3628 -0.2179 105 LYS C CD  
9349  C CE  . LYS C 105 ? 0.7604 1.8046 2.9197 -0.2297 -0.3723 -0.2416 105 LYS C CE  
9350  N NZ  . LYS C 105 ? 0.8006 1.8639 2.9613 -0.2457 -0.3995 -0.2895 105 LYS C NZ  
9351  N N   . ASP C 106 ? 0.7251 1.6520 2.6833 -0.1636 -0.3169 -0.2638 106 ASP C N   
9352  C CA  . ASP C 106 ? 0.7350 1.6289 2.6788 -0.1681 -0.3194 -0.3052 106 ASP C CA  
9353  C C   . ASP C 106 ? 0.7158 1.5922 2.6027 -0.1466 -0.3023 -0.3006 106 ASP C C   
9354  O O   . ASP C 106 ? 0.7370 1.6212 2.5909 -0.1437 -0.3092 -0.3328 106 ASP C O   
9355  C CB  . ASP C 106 ? 0.7328 1.5714 2.7214 -0.1828 -0.3138 -0.3154 106 ASP C CB  
9356  C CG  . ASP C 106 ? 0.7569 1.6064 2.8020 -0.2084 -0.3351 -0.3369 106 ASP C CG  
9357  O OD1 . ASP C 106 ? 0.7841 1.6746 2.8264 -0.2172 -0.3585 -0.3673 106 ASP C OD1 
9358  O OD2 . ASP C 106 ? 0.7497 1.5668 2.8418 -0.2199 -0.3283 -0.3239 106 ASP C OD2 
9359  N N   . SER C 107 ? 0.6731 1.5278 2.5501 -0.1316 -0.2799 -0.2610 107 SER C N   
9360  C CA  . SER C 107 ? 0.6542 1.4897 2.4826 -0.1118 -0.2622 -0.2519 107 SER C CA  
9361  C C   . SER C 107 ? 0.6668 1.5548 2.4507 -0.1002 -0.2708 -0.2513 107 SER C C   
9362  O O   . SER C 107 ? 0.6749 1.5590 2.4169 -0.0896 -0.2653 -0.2637 107 SER C O   
9363  C CB  . SER C 107 ? 0.6126 1.4181 2.4435 -0.0994 -0.2389 -0.2099 107 SER C CB  
9364  O OG  . SER C 107 ? 0.5975 1.3546 2.4641 -0.1084 -0.2289 -0.2078 107 SER C OG  
9365  N N   . GLU C 108 ? 0.6678 1.6066 2.4624 -0.1019 -0.2837 -0.2343 108 GLU C N   
9366  C CA  . GLU C 108 ? 0.6802 1.6727 2.4358 -0.0903 -0.2921 -0.2264 108 GLU C CA  
9367  C C   . GLU C 108 ? 0.7192 1.7393 2.4520 -0.0977 -0.3108 -0.2716 108 GLU C C   
9368  O O   . GLU C 108 ? 0.7344 1.7700 2.4201 -0.0856 -0.3080 -0.2774 108 GLU C O   
9369  C CB  . GLU C 108 ? 0.6739 1.7158 2.4495 -0.0899 -0.3025 -0.1971 108 GLU C CB  
9370  C CG  . GLU C 108 ? 0.6416 1.6690 2.4239 -0.0750 -0.2830 -0.1493 108 GLU C CG  
9371  C CD  . GLU C 108 ? 0.6422 1.7243 2.4270 -0.0663 -0.2912 -0.1176 108 GLU C CD  
9372  O OE1 . GLU C 108 ? 0.6688 1.8042 2.4362 -0.0673 -0.3104 -0.1274 108 GLU C OE1 
9373  O OE2 . GLU C 108 ? 0.6227 1.6954 2.4278 -0.0578 -0.2784 -0.0828 108 GLU C OE2 
9374  N N   . ILE C 109 ? 0.7384 1.7644 2.5065 -0.1178 -0.3295 -0.3036 109 ILE C N   
9375  C CA  . ILE C 109 ? 0.7801 1.8368 2.5331 -0.1270 -0.3508 -0.3504 109 ILE C CA  
9376  C C   . ILE C 109 ? 0.7984 1.8124 2.5274 -0.1233 -0.3403 -0.3827 109 ILE C C   
9377  O O   . ILE C 109 ? 0.8309 1.8714 2.5187 -0.1175 -0.3464 -0.4089 109 ILE C O   
9378  C CB  . ILE C 109 ? 0.7956 1.8688 2.5998 -0.1504 -0.3742 -0.3735 109 ILE C CB  
9379  C CG1 . ILE C 109 ? 0.8402 1.9632 2.6273 -0.1591 -0.4009 -0.4180 109 ILE C CG1 
9380  C CG2 . ILE C 109 ? 0.7901 1.8017 2.6419 -0.1650 -0.3679 -0.3874 109 ILE C CG2 
9381  C CD1 . ILE C 109 ? 0.8469 2.0439 2.6051 -0.1510 -0.4146 -0.4003 109 ILE C CD1 
9382  N N   . GLU C 110 ? 0.7787 1.7288 2.5321 -0.1251 -0.3232 -0.3784 110 GLU C N   
9383  C CA  . GLU C 110 ? 0.7853 1.6906 2.5207 -0.1202 -0.3111 -0.4042 110 GLU C CA  
9384  C C   . GLU C 110 ? 0.7793 1.6956 2.4578 -0.0987 -0.2960 -0.3886 110 GLU C C   
9385  O O   . GLU C 110 ? 0.8062 1.7286 2.4515 -0.0934 -0.2966 -0.4192 110 GLU C O   
9386  C CB  . GLU C 110 ? 0.7572 1.5959 2.5293 -0.1240 -0.2943 -0.3912 110 GLU C CB  
9387  C CG  . GLU C 110 ? 0.7602 1.5502 2.5168 -0.1173 -0.2802 -0.4127 110 GLU C CG  
9388  C CD  . GLU C 110 ? 0.8029 1.5948 2.5582 -0.1256 -0.2952 -0.4688 110 GLU C CD  
9389  O OE1 . GLU C 110 ? 0.8272 1.6433 2.6086 -0.1417 -0.3172 -0.4943 110 GLU C OE1 
9390  O OE2 . GLU C 110 ? 0.8154 1.5858 2.5436 -0.1153 -0.2849 -0.4880 110 GLU C OE2 
9391  N N   . LEU C 111 ? 0.7462 1.6649 2.4159 -0.0864 -0.2820 -0.3407 111 LEU C N   
9392  C CA  . LEU C 111 ? 0.7388 1.6640 2.3606 -0.0668 -0.2666 -0.3201 111 LEU C CA  
9393  C C   . LEU C 111 ? 0.7668 1.7578 2.3493 -0.0622 -0.2814 -0.3313 111 LEU C C   
9394  O O   . LEU C 111 ? 0.7837 1.7834 2.3276 -0.0544 -0.2779 -0.3514 111 LEU C O   
9395  C CB  . LEU C 111 ? 0.7031 1.6164 2.3314 -0.0563 -0.2509 -0.2680 111 LEU C CB  
9396  C CG  . LEU C 111 ? 0.6895 1.6010 2.2757 -0.0366 -0.2331 -0.2414 111 LEU C CG  
9397  C CD1 . LEU C 111 ? 0.6523 1.5326 2.2553 -0.0287 -0.2158 -0.1982 111 LEU C CD1 
9398  C CD2 . LEU C 111 ? 0.7070 1.6822 2.2571 -0.0285 -0.2434 -0.2327 111 LEU C CD2 
9399  N N   . LYS C 112 ? 0.7708 1.8109 2.3635 -0.0667 -0.2979 -0.3175 112 LYS C N   
9400  C CA  . LYS C 112 ? 0.7998 1.9070 2.3543 -0.0612 -0.3121 -0.3210 112 LYS C CA  
9401  C C   . LYS C 112 ? 0.8470 1.9671 2.3787 -0.0666 -0.3228 -0.3749 112 LYS C C   
9402  O O   . LYS C 112 ? 0.8697 2.0274 2.3545 -0.0562 -0.3230 -0.3807 112 LYS C O   
9403  C CB  . LYS C 112 ? 0.8024 1.9628 2.3775 -0.0686 -0.3331 -0.3079 112 LYS C CB  
9404  C CG  . LYS C 112 ? 0.8173 2.0456 2.3514 -0.0572 -0.3421 -0.2899 112 LYS C CG  
9405  C CD  . LYS C 112 ? 0.7932 2.0438 2.3410 -0.0488 -0.3405 -0.2372 112 LYS C CD  
9406  C CE  . LYS C 112 ? 0.7973 2.0759 2.3892 -0.0635 -0.3613 -0.2393 112 LYS C CE  
9407  N NZ  . LYS C 112 ? 0.7758 2.0821 2.3830 -0.0549 -0.3616 -0.1912 112 LYS C NZ  
9408  N N   . ARG C 113 ? 0.8660 1.9547 2.4323 -0.0825 -0.3310 -0.4138 113 ARG C N   
9409  C CA  . ARG C 113 ? 0.9132 2.0072 2.4643 -0.0879 -0.3410 -0.4694 113 ARG C CA  
9410  C C   . ARG C 113 ? 0.9213 1.9927 2.4320 -0.0719 -0.3200 -0.4737 113 ARG C C   
9411  O O   . ARG C 113 ? 0.9520 2.0665 2.4171 -0.0633 -0.3229 -0.4891 113 ARG C O   
9412  C CB  . ARG C 113 ? 0.9244 1.9740 2.5246 -0.1063 -0.3492 -0.5075 113 ARG C CB  
9413  C CG  . ARG C 113 ? 0.9718 2.0289 2.5578 -0.1111 -0.3612 -0.5688 113 ARG C CG  
9414  C CD  . ARG C 113 ? 0.9729 1.9600 2.5810 -0.1130 -0.3480 -0.5933 113 ARG C CD  
9415  N NE  . ARG C 113 ? 0.9593 1.8992 2.6304 -0.1298 -0.3513 -0.5909 113 ARG C NE  
9416  C CZ  . ARG C 113 ? 0.9457 1.8189 2.6458 -0.1315 -0.3370 -0.5928 113 ARG C CZ  
9417  N NH1 . ARG C 113 ? 0.9419 1.7804 2.7000 -0.1490 -0.3440 -0.5969 113 ARG C NH1 
9418  N NH2 . ARG C 113 ? 0.9376 1.7802 2.6103 -0.1161 -0.3163 -0.5911 113 ARG C NH2 
9419  N N   . VAL C 114 ? 0.8975 1.9045 2.4253 -0.0681 -0.2989 -0.4594 114 VAL C N   
9420  C CA  . VAL C 114 ? 0.9039 1.8855 2.4004 -0.0547 -0.2796 -0.4674 114 VAL C CA  
9421  C C   . VAL C 114 ? 0.9042 1.9328 2.3497 -0.0381 -0.2723 -0.4381 114 VAL C C   
9422  O O   . VAL C 114 ? 0.9356 1.9856 2.3419 -0.0292 -0.2682 -0.4585 114 VAL C O   
9423  C CB  . VAL C 114 ? 0.8703 1.7801 2.3891 -0.0510 -0.2574 -0.4500 114 VAL C CB  
9424  C CG1 . VAL C 114 ? 0.8800 1.7413 2.4474 -0.0663 -0.2631 -0.4807 114 VAL C CG1 
9425  C CG2 . VAL C 114 ? 0.8266 1.7237 2.3550 -0.0451 -0.2449 -0.3936 114 VAL C CG2 
9426  N N   . LEU C 115 ? 0.8778 1.9243 2.3259 -0.0340 -0.2708 -0.3903 115 LEU C N   
9427  C CA  . LEU C 115 ? 0.8774 1.9650 2.2827 -0.0185 -0.2636 -0.3569 115 LEU C CA  
9428  C C   . LEU C 115 ? 0.9175 2.0767 2.2865 -0.0182 -0.2814 -0.3811 115 LEU C C   
9429  O O   . LEU C 115 ? 0.9353 2.1260 2.2604 -0.0054 -0.2735 -0.3709 115 LEU C O   
9430  C CB  . LEU C 115 ? 0.8480 1.9400 2.2678 -0.0138 -0.2598 -0.3025 115 LEU C CB  
9431  C CG  . LEU C 115 ? 0.8174 1.8648 2.2337 -0.0009 -0.2343 -0.2643 115 LEU C CG  
9432  C CD1 . LEU C 115 ? 0.7993 1.7756 2.2466 -0.0063 -0.2217 -0.2767 115 LEU C CD1 
9433  C CD2 . LEU C 115 ? 0.7927 1.8524 2.2196 0.0056  -0.2322 -0.2133 115 LEU C CD2 
9434  N N   . ASN C 116 ? 0.9351 2.1204 2.3226 -0.0327 -0.3053 -0.4132 116 ASN C N   
9435  C CA  . ASN C 116 ? 0.9733 2.2320 2.3279 -0.0336 -0.3253 -0.4355 116 ASN C CA  
9436  C C   . ASN C 116 ? 1.0097 2.2826 2.3209 -0.0259 -0.3196 -0.4731 116 ASN C C   
9437  O O   . ASN C 116 ? 1.0414 2.3800 2.3124 -0.0214 -0.3302 -0.4834 116 ASN C O   
9438  C CB  . ASN C 116 ? 0.9901 2.2695 2.3772 -0.0521 -0.3527 -0.4674 116 ASN C CB  
9439  C CG  . ASN C 116 ? 1.0258 2.3881 2.3786 -0.0522 -0.3748 -0.4818 116 ASN C CG  
9440  O OD1 . ASN C 116 ? 1.0650 2.4500 2.4010 -0.0574 -0.3874 -0.5337 116 ASN C OD1 
9441  N ND2 . ASN C 116 ? 1.0142 2.4234 2.3545 -0.0453 -0.3792 -0.4367 116 ASN C ND2 
9442  N N   . TYR C 117 ? 1.0077 2.2222 2.3272 -0.0240 -0.3028 -0.4934 117 TYR C N   
9443  C CA  . TYR C 117 ? 1.0383 2.2625 2.3179 -0.0137 -0.2925 -0.5229 117 TYR C CA  
9444  C C   . TYR C 117 ? 1.0078 2.1954 2.2739 0.0010  -0.2637 -0.4872 117 TYR C C   
9445  O O   . TYR C 117 ? 1.0236 2.2425 2.2464 0.0138  -0.2530 -0.4837 117 TYR C O   
9446  C CB  . TYR C 117 ? 1.0701 2.2679 2.3690 -0.0239 -0.3014 -0.5874 117 TYR C CB  
9447  C CG  . TYR C 117 ? 1.0455 2.1627 2.3981 -0.0328 -0.2941 -0.5918 117 TYR C CG  
9448  C CD1 . TYR C 117 ? 1.0297 2.0922 2.3847 -0.0238 -0.2705 -0.5865 117 TYR C CD1 
9449  C CD2 . TYR C 117 ? 1.0424 2.1407 2.4442 -0.0503 -0.3108 -0.5995 117 TYR C CD2 
9450  C CE1 . TYR C 117 ? 1.0083 2.0000 2.4110 -0.0313 -0.2640 -0.5878 117 TYR C CE1 
9451  C CE2 . TYR C 117 ? 1.0212 2.0489 2.4718 -0.0585 -0.3036 -0.6003 117 TYR C CE2 
9452  C CZ  . TYR C 117 ? 1.0050 1.9795 2.4551 -0.0487 -0.2803 -0.5939 117 TYR C CZ  
9453  O OH  . TYR C 117 ? 0.9845 1.8919 2.4814 -0.0562 -0.2734 -0.5922 117 TYR C OH  
9454  N N   . ALA C 118 ? 0.9672 2.0921 2.2700 -0.0008 -0.2510 -0.4595 118 ALA C N   
9455  C CA  . ALA C 118 ? 0.9404 2.0240 2.2360 0.0114  -0.2249 -0.4318 118 ALA C CA  
9456  C C   . ALA C 118 ? 0.9371 2.0630 2.1925 0.0256  -0.2149 -0.3885 118 ALA C C   
9457  O O   . ALA C 118 ? 0.9296 2.0443 2.1634 0.0369  -0.1956 -0.3782 118 ALA C O   
9458  C CB  . ALA C 118 ? 0.8987 1.9189 2.2389 0.0065  -0.2165 -0.4047 118 ALA C CB  
9459  N N   . LYS C 119 ? 0.9421 2.1159 2.1916 0.0246  -0.2282 -0.3614 119 LYS C N   
9460  C CA  . LYS C 119 ? 0.9389 2.1566 2.1554 0.0370  -0.2219 -0.3162 119 LYS C CA  
9461  C C   . LYS C 119 ? 0.9652 2.2228 2.1327 0.0474  -0.2135 -0.3297 119 LYS C C   
9462  O O   . LYS C 119 ? 0.9538 2.2278 2.0978 0.0590  -0.1999 -0.2900 119 LYS C O   
9463  C CB  . LYS C 119 ? 0.9489 2.2222 2.1659 0.0330  -0.2430 -0.2977 119 LYS C CB  
9464  C CG  . LYS C 119 ? 0.9917 2.3164 2.1971 0.0236  -0.2674 -0.3447 119 LYS C CG  
9465  C CD  . LYS C 119 ? 1.0015 2.3814 2.2121 0.0182  -0.2905 -0.3290 119 LYS C CD  
9466  C CE  . LYS C 119 ? 0.9664 2.3097 2.2276 0.0104  -0.2943 -0.3047 119 LYS C CE  
9467  N NZ  . LYS C 119 ? 0.9824 2.3674 2.2614 -0.0017 -0.3214 -0.3189 119 LYS C NZ  
9468  N N   . LYS C 120 ? 1.0026 2.2763 2.1561 0.0436  -0.2213 -0.3852 120 LYS C N   
9469  C CA  . LYS C 120 ? 1.0403 2.3633 2.1451 0.0534  -0.2156 -0.4030 120 LYS C CA  
9470  C C   . LYS C 120 ? 1.0372 2.3131 2.1416 0.0599  -0.1936 -0.4217 120 LYS C C   
9471  O O   . LYS C 120 ? 1.0715 2.3714 2.1491 0.0644  -0.1910 -0.4613 120 LYS C O   
9472  C CB  . LYS C 120 ? 1.0916 2.4685 2.1769 0.0473  -0.2374 -0.4561 120 LYS C CB  
9473  C CG  . LYS C 120 ? 1.1014 2.4936 2.2127 0.0328  -0.2645 -0.4685 120 LYS C CG  
9474  C CD  . LYS C 120 ? 1.1459 2.5502 2.2614 0.0221  -0.2839 -0.5370 120 LYS C CD  
9475  C CE  . LYS C 120 ? 1.1598 2.5219 2.2782 0.0243  -0.2717 -0.5845 120 LYS C CE  
9476  N NZ  . LYS C 120 ? 1.1842 2.5242 2.3336 0.0102  -0.2896 -0.6432 120 LYS C NZ  
9477  N N   . TYR C 121 ? 0.9953 2.2060 2.1300 0.0609  -0.1779 -0.3934 121 TYR C N   
9478  C CA  . TYR C 121 ? 0.9816 2.1436 2.1214 0.0668  -0.1573 -0.4052 121 TYR C CA  
9479  C C   . TYR C 121 ? 0.9410 2.0730 2.0871 0.0741  -0.1384 -0.3486 121 TYR C C   
9480  O O   . TYR C 121 ? 0.9031 1.9830 2.0851 0.0693  -0.1362 -0.3278 121 TYR C O   
9481  C CB  . TYR C 121 ? 0.9773 2.0796 2.1580 0.0566  -0.1622 -0.4463 121 TYR C CB  
9482  C CG  . TYR C 121 ? 1.0192 2.1466 2.1960 0.0498  -0.1800 -0.5076 121 TYR C CG  
9483  C CD1 . TYR C 121 ? 1.0485 2.1919 2.2004 0.0573  -0.1735 -0.5492 121 TYR C CD1 
9484  C CD2 . TYR C 121 ? 1.0291 2.1651 2.2284 0.0359  -0.2035 -0.5249 121 TYR C CD2 
9485  C CE1 . TYR C 121 ? 1.0915 2.2576 2.2401 0.0517  -0.1900 -0.6080 121 TYR C CE1 
9486  C CE2 . TYR C 121 ? 1.0687 2.2271 2.2663 0.0288  -0.2210 -0.5825 121 TYR C CE2 
9487  C CZ  . TYR C 121 ? 1.1018 2.2744 2.2734 0.0370  -0.2144 -0.6251 121 TYR C CZ  
9488  O OH  . TYR C 121 ? 1.1473 2.3411 2.3178 0.0307  -0.2319 -0.6848 121 TYR C OH  
9489  N N   . ASP C 122 ? 0.9494 2.1168 2.0607 0.0857  -0.1248 -0.3239 122 ASP C N   
9490  C CA  . ASP C 122 ? 0.9170 2.0621 2.0325 0.0926  -0.1078 -0.2700 122 ASP C CA  
9491  C C   . ASP C 122 ? 0.9028 1.9877 2.0351 0.0959  -0.0885 -0.2774 122 ASP C C   
9492  O O   . ASP C 122 ? 0.8880 1.9625 2.0152 0.1035  -0.0713 -0.2429 122 ASP C O   
9493  C CB  . ASP C 122 ? 0.9292 2.1380 2.0058 0.1020  -0.1030 -0.2352 122 ASP C CB  
9494  C CG  . ASP C 122 ? 0.9542 2.1990 1.9942 0.1110  -0.0897 -0.2520 122 ASP C CG  
9495  O OD1 . ASP C 122 ? 0.9584 2.1757 2.0035 0.1114  -0.0825 -0.2925 122 ASP C OD1 
9496  O OD2 . ASP C 122 ? 0.9656 2.2669 1.9736 0.1181  -0.0859 -0.2227 122 ASP C OD2 
9497  N N   . CYS C 123 ? 0.9107 1.9570 2.0648 0.0900  -0.0919 -0.3221 123 CYS C N   
9498  C CA  . CYS C 123 ? 0.8916 1.8740 2.0702 0.0915  -0.0769 -0.3282 123 CYS C CA  
9499  C C   . CYS C 123 ? 0.8648 1.7894 2.0842 0.0842  -0.0789 -0.3058 123 CYS C C   
9500  O O   . CYS C 123 ? 0.8400 1.7133 2.0787 0.0864  -0.0653 -0.2943 123 CYS C O   
9501  C CB  . CYS C 123 ? 0.9183 1.8877 2.1021 0.0902  -0.0788 -0.3860 123 CYS C CB  
9502  S SG  . CYS C 123 ? 0.9379 1.9022 2.1463 0.0757  -0.1043 -0.4309 123 CYS C SG  
9503  N N   . ILE C 124 ? 0.8765 1.8125 2.1086 0.0757  -0.0959 -0.3000 124 ILE C N   
9504  C CA  . ILE C 124 ? 0.8532 1.7431 2.1224 0.0692  -0.0980 -0.2771 124 ILE C CA  
9505  C C   . ILE C 124 ? 0.8253 1.7169 2.0893 0.0764  -0.0881 -0.2223 124 ILE C C   
9506  O O   . ILE C 124 ? 0.8248 1.7662 2.0660 0.0804  -0.0927 -0.1996 124 ILE C O   
9507  C CB  . ILE C 124 ? 0.8763 1.7799 2.1642 0.0573  -0.1196 -0.2929 124 ILE C CB  
9508  C CG1 . ILE C 124 ? 0.9150 1.8259 2.2044 0.0504  -0.1312 -0.3504 124 ILE C CG1 
9509  C CG2 . ILE C 124 ? 0.8455 1.7002 2.1744 0.0505  -0.1200 -0.2717 124 ILE C CG2 
9510  C CD1 . ILE C 124 ? 0.9171 1.8059 2.2450 0.0358  -0.1479 -0.3716 124 ILE C CD1 
9511  N N   . ILE C 125 ? 0.7982 1.6347 2.0846 0.0780  -0.0751 -0.2023 125 ILE C N   
9512  C CA  . ILE C 125 ? 0.7758 1.6029 2.0597 0.0858  -0.0624 -0.1556 125 ILE C CA  
9513  C C   . ILE C 125 ? 0.7326 1.5195 2.0495 0.0822  -0.0634 -0.1311 125 ILE C C   
9514  O O   . ILE C 125 ? 0.7180 1.5015 2.0362 0.0879  -0.0571 -0.0920 125 ILE C O   
9515  C CB  . ILE C 125 ? 0.7861 1.5906 2.0609 0.0930  -0.0438 -0.1556 125 ILE C CB  
9516  C CG1 . ILE C 125 ? 0.8130 1.6664 2.0534 0.1017  -0.0367 -0.1369 125 ILE C CG1 
9517  C CG2 . ILE C 125 ? 0.7542 1.5022 2.0534 0.0946  -0.0318 -0.1300 125 ILE C CG2 
9518  C CD1 . ILE C 125 ? 0.8591 1.7670 2.0698 0.1022  -0.0439 -0.1696 125 ILE C CD1 
9519  N N   . THR C 126 ? 0.7156 1.4717 2.0602 0.0730  -0.0706 -0.1538 126 THR C N   
9520  C CA  . THR C 126 ? 0.6872 1.4170 2.0621 0.0688  -0.0739 -0.1332 126 THR C CA  
9521  C C   . THR C 126 ? 0.6895 1.4125 2.0887 0.0564  -0.0880 -0.1642 126 THR C C   
9522  O O   . THR C 126 ? 0.7094 1.4239 2.1093 0.0518  -0.0905 -0.2012 126 THR C O   
9523  C CB  . THR C 126 ? 0.6544 1.3304 2.0440 0.0730  -0.0578 -0.1139 126 THR C CB  
9524  O OG1 . THR C 126 ? 0.6475 1.3363 2.0214 0.0828  -0.0491 -0.0781 126 THR C OG1 
9525  C CG2 . THR C 126 ? 0.6291 1.2708 2.0522 0.0679  -0.0594 -0.1026 126 THR C CG2 
9526  N N   . TYR C 127 ? 0.6626 1.3908 2.0835 0.0512  -0.0973 -0.1489 127 TYR C N   
9527  C CA  . TYR C 127 ? 0.6528 1.3685 2.1046 0.0384  -0.1091 -0.1713 127 TYR C CA  
9528  C C   . TYR C 127 ? 0.6282 1.2934 2.1113 0.0368  -0.0997 -0.1532 127 TYR C C   
9529  O O   . TYR C 127 ? 0.6200 1.2778 2.1038 0.0443  -0.0911 -0.1186 127 TYR C O   
9530  C CB  . TYR C 127 ? 0.6534 1.4163 2.1102 0.0325  -0.1273 -0.1692 127 TYR C CB  
9531  C CG  . TYR C 127 ? 0.6795 1.4939 2.1104 0.0302  -0.1412 -0.1973 127 TYR C CG  
9532  C CD1 . TYR C 127 ? 0.6875 1.5486 2.0829 0.0398  -0.1412 -0.1810 127 TYR C CD1 
9533  C CD2 . TYR C 127 ? 0.6970 1.5153 2.1398 0.0184  -0.1549 -0.2398 127 TYR C CD2 
9534  C CE1 . TYR C 127 ? 0.7187 1.6314 2.0877 0.0383  -0.1538 -0.2064 127 TYR C CE1 
9535  C CE2 . TYR C 127 ? 0.7298 1.5971 2.1477 0.0166  -0.1682 -0.2683 127 TYR C CE2 
9536  C CZ  . TYR C 127 ? 0.7400 1.6564 2.1192 0.0269  -0.1676 -0.2518 127 TYR C CZ  
9537  O OH  . TYR C 127 ? 0.7737 1.7427 2.1255 0.0258  -0.1806 -0.2796 127 TYR C OH  
9538  N N   . LEU C 128 ? 0.6295 1.2605 2.1383 0.0272  -0.1014 -0.1769 128 LEU C N   
9539  C CA  . LEU C 128 ? 0.6048 1.1934 2.1452 0.0237  -0.0946 -0.1617 128 LEU C CA  
9540  C C   . LEU C 128 ? 0.5978 1.1975 2.1705 0.0105  -0.1090 -0.1685 128 LEU C C   
9541  O O   . LEU C 128 ? 0.6172 1.2221 2.2026 -0.0005 -0.1211 -0.2004 128 LEU C O   
9542  C CB  . LEU C 128 ? 0.6083 1.1484 2.1567 0.0235  -0.0840 -0.1764 128 LEU C CB  
9543  C CG  . LEU C 128 ? 0.6176 1.1454 2.1384 0.0358  -0.0694 -0.1696 128 LEU C CG  
9544  C CD1 . LEU C 128 ? 0.6208 1.1030 2.1540 0.0349  -0.0612 -0.1864 128 LEU C CD1 
9545  C CD2 . LEU C 128 ? 0.5953 1.1194 2.1065 0.0461  -0.0581 -0.1303 128 LEU C CD2 
9546  N N   . VAL C 129 ? 0.5622 1.1654 2.1505 0.0118  -0.1072 -0.1381 129 VAL C N   
9547  C CA  . VAL C 129 ? 0.5556 1.1822 2.1716 0.0014  -0.1209 -0.1373 129 VAL C CA  
9548  C C   . VAL C 129 ? 0.5474 1.1376 2.2025 -0.0100 -0.1193 -0.1428 129 VAL C C   
9549  O O   . VAL C 129 ? 0.5629 1.1673 2.2462 -0.0230 -0.1323 -0.1532 129 VAL C O   
9550  C CB  . VAL C 129 ? 0.5292 1.1821 2.1428 0.0102  -0.1192 -0.1011 129 VAL C CB  
9551  C CG1 . VAL C 129 ? 0.5112 1.1558 2.1622 0.0049  -0.1185 -0.0834 129 VAL C CG1 
9552  C CG2 . VAL C 129 ? 0.5441 1.2532 2.1389 0.0118  -0.1336 -0.1027 129 VAL C CG2 
9553  N N   . ILE C 130 ? 0.5281 1.0734 2.1861 -0.0055 -0.1039 -0.1339 130 ILE C N   
9554  C CA  . ILE C 130 ? 0.5226 1.0337 2.2164 -0.0153 -0.1010 -0.1346 130 ILE C CA  
9555  C C   . ILE C 130 ? 0.5236 0.9897 2.2086 -0.0080 -0.0852 -0.1306 130 ILE C C   
9556  O O   . ILE C 130 ? 0.5190 0.9828 2.1748 0.0050  -0.0753 -0.1188 130 ILE C O   
9557  C CB  . ILE C 130 ? 0.5006 1.0204 2.2198 -0.0173 -0.0992 -0.1063 130 ILE C CB  
9558  C CG1 . ILE C 130 ? 0.5022 0.9957 2.2615 -0.0304 -0.0990 -0.1088 130 ILE C CG1 
9559  C CG2 . ILE C 130 ? 0.4746 0.9853 2.1769 -0.0017 -0.0835 -0.0745 130 ILE C CG2 
9560  C CD1 . ILE C 130 ? 0.4953 1.0097 2.2853 -0.0363 -0.1018 -0.0882 130 ILE C CD1 
9561  N N   . ASN C 131 ? 0.5428 0.9747 2.2556 -0.0168 -0.0834 -0.1387 131 ASN C N   
9562  C CA  . ASN C 131 ? 0.5493 0.9390 2.2573 -0.0111 -0.0704 -0.1377 131 ASN C CA  
9563  C C   . ASN C 131 ? 0.5521 0.9135 2.2905 -0.0161 -0.0631 -0.1186 131 ASN C C   
9564  O O   . ASN C 131 ? 0.5706 0.9300 2.3431 -0.0296 -0.0709 -0.1244 131 ASN C O   
9565  C CB  . ASN C 131 ? 0.5737 0.9490 2.2811 -0.0151 -0.0757 -0.1723 131 ASN C CB  
9566  C CG  . ASN C 131 ? 0.5803 0.9111 2.2912 -0.0106 -0.0638 -0.1708 131 ASN C CG  
9567  O OD1 . ASN C 131 ? 0.5927 0.8959 2.3356 -0.0194 -0.0645 -0.1732 131 ASN C OD1 
9568  N ND2 . ASN C 131 ? 0.5743 0.8987 2.2548 0.0026  -0.0531 -0.1645 131 ASN C ND2 
9569  N N   . GLU C 132 ? 0.5424 0.8832 2.2684 -0.0054 -0.0484 -0.0957 132 GLU C N   
9570  C CA  . GLU C 132 ? 0.5463 0.8597 2.2949 -0.0080 -0.0396 -0.0777 132 GLU C CA  
9571  C C   . GLU C 132 ? 0.5277 0.8605 2.3070 -0.0178 -0.0443 -0.0644 132 GLU C C   
9572  O O   . GLU C 132 ? 0.5239 0.8453 2.3364 -0.0306 -0.0485 -0.0684 132 GLU C O   
9573  C CB  . GLU C 132 ? 0.5834 0.8612 2.3493 -0.0144 -0.0397 -0.0937 132 GLU C CB  
9574  C CG  . GLU C 132 ? 0.6246 0.8803 2.3650 -0.0039 -0.0327 -0.1034 132 GLU C CG  
9575  C CD  . GLU C 132 ? 0.6792 0.8970 2.4393 -0.0077 -0.0307 -0.1130 132 GLU C CD  
9576  O OE1 . GLU C 132 ? 0.6728 0.8761 2.4597 -0.0142 -0.0281 -0.0965 132 GLU C OE1 
9577  O OE2 . GLU C 132 ? 0.7382 0.9418 2.4890 -0.0037 -0.0310 -0.1342 132 GLU C OE2 
9578  N N   . PRO C 133 ? 0.5095 0.8730 2.2818 -0.0125 -0.0440 -0.0475 133 PRO C N   
9579  C CA  . PRO C 133 ? 0.5023 0.8826 2.3046 -0.0195 -0.0448 -0.0303 133 PRO C CA  
9580  C C   . PRO C 133 ? 0.4942 0.8529 2.3024 -0.0142 -0.0293 -0.0059 133 PRO C C   
9581  O O   . PRO C 133 ? 0.4700 0.8213 2.2529 0.0001  -0.0183 0.0073  133 PRO C O   
9582  C CB  . PRO C 133 ? 0.4979 0.9182 2.2878 -0.0129 -0.0495 -0.0224 133 PRO C CB  
9583  C CG  . PRO C 133 ? 0.4925 0.9062 2.2424 0.0026  -0.0428 -0.0211 133 PRO C CG  
9584  C CD  . PRO C 133 ? 0.5074 0.8928 2.2465 0.0001  -0.0433 -0.0437 133 PRO C CD  
9585  N N   . GLN C 134 ? 0.5176 0.8684 2.3607 -0.0264 -0.0293 -0.0001 134 GLN C N   
9586  C CA  . GLN C 134 ? 0.5337 0.8661 2.3857 -0.0238 -0.0155 0.0222  134 GLN C CA  
9587  C C   . GLN C 134 ? 0.5333 0.8929 2.3878 -0.0167 -0.0078 0.0461  134 GLN C C   
9588  O O   . GLN C 134 ? 0.5264 0.9193 2.3930 -0.0198 -0.0152 0.0472  134 GLN C O   
9589  C CB  . GLN C 134 ? 0.5744 0.8922 2.4656 -0.0400 -0.0183 0.0226  134 GLN C CB  
9590  C CG  . GLN C 134 ? 0.5979 0.8925 2.4939 -0.0371 -0.0042 0.0442  134 GLN C CG  
9591  C CD  . GLN C 134 ? 0.6346 0.8997 2.4973 -0.0240 0.0042  0.0422  134 GLN C CD  
9592  O OE1 . GLN C 134 ? 0.6028 0.8426 2.4614 -0.0256 -0.0001 0.0247  134 GLN C OE1 
9593  N NE2 . GLN C 134 ? 0.6651 0.9338 2.5056 -0.0104 0.0166  0.0601  134 GLN C NE2 
9594  N N   . THR C 135 ? 0.5234 0.8690 2.3673 -0.0066 0.0070  0.0644  135 THR C N   
9595  C CA  . THR C 135 ? 0.4934 0.8594 2.3303 0.0055  0.0167  0.0839  135 THR C CA  
9596  C C   . THR C 135 ? 0.4836 0.8737 2.3560 -0.0029 0.0192  0.1003  135 THR C C   
9597  O O   . THR C 135 ? 0.4816 0.9027 2.3599 0.0024  0.0201  0.1099  135 THR C O   
9598  C CB  . THR C 135 ? 0.4803 0.8206 2.2904 0.0190  0.0304  0.0923  135 THR C CB  
9599  O OG1 . THR C 135 ? 0.4510 0.7826 2.2328 0.0260  0.0253  0.0773  135 THR C OG1 
9600  C CG2 . THR C 135 ? 0.4719 0.8285 2.2797 0.0309  0.0427  0.1123  135 THR C CG2 
9601  N N   . ASP C 136 ? 0.4930 0.8700 2.3911 -0.0158 0.0203  0.1047  136 ASP C N   
9602  C CA  . ASP C 136 ? 0.4900 0.8911 2.4272 -0.0270 0.0214  0.1203  136 ASP C CA  
9603  C C   . ASP C 136 ? 0.5018 0.9317 2.4647 -0.0394 0.0057  0.1093  136 ASP C C   
9604  O O   . ASP C 136 ? 0.5277 0.9922 2.5128 -0.0413 0.0065  0.1224  136 ASP C O   
9605  C CB  . ASP C 136 ? 0.4896 0.8694 2.4520 -0.0401 0.0242  0.1278  136 ASP C CB  
9606  C CG  . ASP C 136 ? 0.4934 0.8995 2.5009 -0.0543 0.0242  0.1443  136 ASP C CG  
9607  O OD1 . ASP C 136 ? 0.5096 0.9255 2.5471 -0.0703 0.0099  0.1328  136 ASP C OD1 
9608  O OD2 . ASP C 136 ? 0.4882 0.9079 2.5000 -0.0490 0.0384  0.1677  136 ASP C OD2 
9609  N N   . HIS C 137 ? 0.4963 0.9136 2.4579 -0.0481 -0.0088 0.0847  137 HIS C N   
9610  C CA  . HIS C 137 ? 0.4863 0.9304 2.4705 -0.0608 -0.0259 0.0704  137 HIS C CA  
9611  C C   . HIS C 137 ? 0.4672 0.9486 2.4372 -0.0494 -0.0279 0.0750  137 HIS C C   
9612  O O   . HIS C 137 ? 0.4746 0.9911 2.4721 -0.0569 -0.0351 0.0799  137 HIS C O   
9613  C CB  . HIS C 137 ? 0.4919 0.9146 2.4728 -0.0700 -0.0400 0.0403  137 HIS C CB  
9614  C CG  . HIS C 137 ? 0.4896 0.9411 2.4884 -0.0820 -0.0588 0.0217  137 HIS C CG  
9615  N ND1 . HIS C 137 ? 0.4906 0.9527 2.5358 -0.1019 -0.0691 0.0188  137 HIS C ND1 
9616  C CD2 . HIS C 137 ? 0.4879 0.9618 2.4647 -0.0771 -0.0696 0.0058  137 HIS C CD2 
9617  C CE1 . HIS C 137 ? 0.5010 0.9914 2.5511 -0.1087 -0.0863 -0.0005 137 HIS C CE1 
9618  N NE2 . HIS C 137 ? 0.4985 0.9973 2.5063 -0.0936 -0.0868 -0.0082 137 HIS C NE2 
9619  N N   . ILE C 138 ? 0.4445 0.9193 2.3745 -0.0312 -0.0215 0.0755  138 ILE C N   
9620  C CA  . ILE C 138 ? 0.4313 0.9389 2.3495 -0.0192 -0.0231 0.0823  138 ILE C CA  
9621  C C   . ILE C 138 ? 0.4260 0.9592 2.3671 -0.0149 -0.0128 0.1071  138 ILE C C   
9622  O O   . ILE C 138 ? 0.4305 1.0017 2.3880 -0.0150 -0.0194 0.1126  138 ILE C O   
9623  C CB  . ILE C 138 ? 0.4234 0.9153 2.2976 -0.0011 -0.0173 0.0803  138 ILE C CB  
9624  C CG1 . ILE C 138 ? 0.4335 0.9094 2.2862 -0.0050 -0.0280 0.0556  138 ILE C CG1 
9625  C CG2 . ILE C 138 ? 0.4145 0.9385 2.2811 0.0129  -0.0170 0.0927  138 ILE C CG2 
9626  C CD1 . ILE C 138 ? 0.4185 0.8740 2.2308 0.0105  -0.0209 0.0541  138 ILE C CD1 
9627  N N   . HIS C 139 ? 0.4127 0.9281 2.3553 -0.0108 0.0032  0.1221  139 HIS C N   
9628  C CA  . HIS C 139 ? 0.3963 0.9376 2.3595 -0.0058 0.0148  0.1448  139 HIS C CA  
9629  C C   . HIS C 139 ? 0.4013 0.9743 2.4104 -0.0237 0.0058  0.1486  139 HIS C C   
9630  O O   . HIS C 139 ? 0.3957 1.0069 2.4225 -0.0199 0.0055  0.1595  139 HIS C O   
9631  C CB  . HIS C 139 ? 0.3929 0.9118 2.3504 -0.0008 0.0326  0.1587  139 HIS C CB  
9632  C CG  . HIS C 139 ? 0.3907 0.9371 2.3650 0.0065  0.0469  0.1810  139 HIS C CG  
9633  N ND1 . HIS C 139 ? 0.4040 0.9778 2.4199 -0.0070 0.0473  0.1938  139 HIS C ND1 
9634  C CD2 . HIS C 139 ? 0.3874 0.9391 2.3442 0.0257  0.0616  0.1920  139 HIS C CD2 
9635  C CE1 . HIS C 139 ? 0.3941 0.9917 2.4162 0.0044  0.0626  0.2125  139 HIS C CE1 
9636  N NE2 . HIS C 139 ? 0.3881 0.9719 2.3742 0.0247  0.0714  0.2106  139 HIS C NE2 
9637  N N   . SER C 140 ? 0.4093 0.9661 2.4402 -0.0431 -0.0020 0.1397  140 SER C N   
9638  C CA  . SER C 140 ? 0.4140 0.9973 2.4932 -0.0627 -0.0110 0.1433  140 SER C CA  
9639  C C   . SER C 140 ? 0.4150 1.0368 2.5050 -0.0656 -0.0274 0.1340  140 SER C C   
9640  O O   . SER C 140 ? 0.4168 1.0775 2.5392 -0.0697 -0.0280 0.1477  140 SER C O   
9641  C CB  . SER C 140 ? 0.4277 0.9836 2.5282 -0.0826 -0.0194 0.1314  140 SER C CB  
9642  O OG  . SER C 140 ? 0.4329 0.9806 2.5571 -0.0889 -0.0064 0.1526  140 SER C OG  
9643  N N   . VAL C 141 ? 0.4168 1.0305 2.4799 -0.0633 -0.0404 0.1115  141 VAL C N   
9644  C CA  . VAL C 141 ? 0.4219 1.0728 2.4921 -0.0668 -0.0581 0.1009  141 VAL C CA  
9645  C C   . VAL C 141 ? 0.4074 1.0816 2.4519 -0.0453 -0.0537 0.1118  141 VAL C C   
9646  O O   . VAL C 141 ? 0.4036 1.1136 2.4533 -0.0455 -0.0675 0.1079  141 VAL C O   
9647  C CB  . VAL C 141 ? 0.4387 1.0727 2.4954 -0.0770 -0.0754 0.0698  141 VAL C CB  
9648  C CG1 . VAL C 141 ? 0.4502 1.0575 2.5362 -0.0976 -0.0799 0.0584  141 VAL C CG1 
9649  C CG2 . VAL C 141 ? 0.4335 1.0398 2.4388 -0.0608 -0.0706 0.0601  141 VAL C CG2 
9650  N N   . THR C 142 ? 0.3924 1.0459 2.4103 -0.0268 -0.0355 0.1249  142 THR C N   
9651  C CA  . THR C 142 ? 0.3702 1.0376 2.3664 -0.0047 -0.0280 0.1376  142 THR C CA  
9652  C C   . THR C 142 ? 0.3703 1.0198 2.3245 0.0048  -0.0337 0.1238  142 THR C C   
9653  O O   . THR C 142 ? 0.3810 1.0309 2.3288 -0.0056 -0.0490 0.1043  142 THR C O   
9654  C CB  . THR C 142 ? 0.3633 1.0814 2.3846 -0.0017 -0.0348 0.1491  142 THR C CB  
9655  O OG1 . THR C 142 ? 0.3681 1.0992 2.3778 -0.0067 -0.0543 0.1323  142 THR C OG1 
9656  C CG2 . THR C 142 ? 0.3630 1.1080 2.4320 -0.0146 -0.0329 0.1612  142 THR C CG2 
9657  N N   . GLY C 143 ? 0.3585 0.9953 2.2861 0.0250  -0.0211 0.1343  143 GLY C N   
9658  C CA  . GLY C 143 ? 0.3488 0.9737 2.2393 0.0365  -0.0243 0.1275  143 GLY C CA  
9659  C C   . GLY C 143 ? 0.3470 1.0120 2.2396 0.0391  -0.0393 0.1283  143 GLY C C   
9660  O O   . GLY C 143 ? 0.3481 1.0115 2.2150 0.0407  -0.0483 0.1177  143 GLY C O   
9661  N N   . LYS C 144 ? 0.3380 1.0419 2.2622 0.0393  -0.0421 0.1416  144 LYS C N   
9662  C CA  . LYS C 144 ? 0.3382 1.0846 2.2683 0.0409  -0.0578 0.1439  144 LYS C CA  
9663  C C   . LYS C 144 ? 0.3495 1.1045 2.2750 0.0233  -0.0771 0.1209  144 LYS C C   
9664  O O   . LYS C 144 ? 0.3552 1.1225 2.2568 0.0275  -0.0878 0.1149  144 LYS C O   
9665  C CB  . LYS C 144 ? 0.3339 1.1233 2.3054 0.0399  -0.0596 0.1593  144 LYS C CB  
9666  C CG  . LYS C 144 ? 0.3416 1.1766 2.3194 0.0399  -0.0784 0.1605  144 LYS C CG  
9667  C CD  . LYS C 144 ? 0.3378 1.2183 2.3519 0.0466  -0.0792 0.1805  144 LYS C CD  
9668  C CE  . LYS C 144 ? 0.3493 1.2741 2.3657 0.0454  -0.1002 0.1801  144 LYS C CE  
9669  N NZ  . LYS C 144 ? 0.3561 1.2682 2.3304 0.0558  -0.1045 0.1768  144 LYS C NZ  
9670  N N   . ALA C 145 ? 0.3507 1.1002 2.3007 0.0039  -0.0813 0.1087  145 ALA C N   
9671  C CA  . ALA C 145 ? 0.3646 1.1210 2.3179 -0.0146 -0.0999 0.0836  145 ALA C CA  
9672  C C   . ALA C 145 ? 0.3728 1.0996 2.2842 -0.0118 -0.1015 0.0646  145 ALA C C   
9673  O O   . ALA C 145 ? 0.3846 1.1299 2.2829 -0.0172 -0.1176 0.0471  145 ALA C O   
9674  C CB  . ALA C 145 ? 0.3655 1.1104 2.3546 -0.0341 -0.0999 0.0769  145 ALA C CB  
9675  N N   . PHE C 146 ? 0.3654 1.0488 2.2557 -0.0031 -0.0849 0.0679  146 PHE C N   
9676  C CA  . PHE C 146 ? 0.3765 1.0299 2.2306 -0.0007 -0.0844 0.0508  146 PHE C CA  
9677  C C   . PHE C 146 ? 0.3795 1.0527 2.2016 0.0131  -0.0889 0.0549  146 PHE C C   
9678  O O   . PHE C 146 ? 0.3969 1.0740 2.1964 0.0098  -0.0988 0.0363  146 PHE C O   
9679  C CB  . PHE C 146 ? 0.3662 0.9719 2.2082 0.0059  -0.0657 0.0562  146 PHE C CB  
9680  C CG  . PHE C 146 ? 0.3701 0.9437 2.1763 0.0101  -0.0628 0.0414  146 PHE C CG  
9681  C CD1 . PHE C 146 ? 0.3686 0.9460 2.1420 0.0245  -0.0609 0.0463  146 PHE C CD1 
9682  C CD2 . PHE C 146 ? 0.3799 0.9188 2.1879 0.0004  -0.0606 0.0249  146 PHE C CD2 
9683  C CE1 . PHE C 146 ? 0.3746 0.9249 2.1176 0.0281  -0.0573 0.0340  146 PHE C CE1 
9684  C CE2 . PHE C 146 ? 0.3811 0.8922 2.1588 0.0052  -0.0571 0.0120  146 PHE C CE2 
9685  C CZ  . PHE C 146 ? 0.3793 0.8974 2.1243 0.0187  -0.0553 0.0162  146 PHE C CZ  
9686  N N   . VAL C 147 ? 0.3646 1.0505 2.1858 0.0289  -0.0811 0.0797  147 VAL C N   
9687  C CA  . VAL C 147 ? 0.3633 1.0593 2.1550 0.0440  -0.0817 0.0890  147 VAL C CA  
9688  C C   . VAL C 147 ? 0.3803 1.1263 2.1737 0.0403  -0.1011 0.0862  147 VAL C C   
9689  O O   . VAL C 147 ? 0.3866 1.1453 2.1520 0.0473  -0.1064 0.0866  147 VAL C O   
9690  C CB  . VAL C 147 ? 0.3441 1.0324 2.1373 0.0627  -0.0669 0.1155  147 VAL C CB  
9691  C CG1 . VAL C 147 ? 0.3478 1.0453 2.1151 0.0778  -0.0680 0.1277  147 VAL C CG1 
9692  C CG2 . VAL C 147 ? 0.3305 0.9722 2.1195 0.0664  -0.0487 0.1167  147 VAL C CG2 
9693  N N   . ASP C 148 ? 0.3914 1.1686 2.2180 0.0291  -0.1120 0.0844  148 ASP C N   
9694  C CA  . ASP C 148 ? 0.4120 1.2401 2.2421 0.0245  -0.1321 0.0807  148 ASP C CA  
9695  C C   . ASP C 148 ? 0.4428 1.2730 2.2575 0.0094  -0.1465 0.0484  148 ASP C C   
9696  O O   . ASP C 148 ? 0.4644 1.3280 2.2594 0.0103  -0.1604 0.0421  148 ASP C O   
9697  C CB  . ASP C 148 ? 0.4027 1.2664 2.2750 0.0203  -0.1380 0.0937  148 ASP C CB  
9698  C CG  . ASP C 148 ? 0.3843 1.2491 2.2671 0.0391  -0.1237 0.1243  148 ASP C CG  
9699  O OD1 . ASP C 148 ? 0.3755 1.2332 2.2320 0.0557  -0.1178 0.1372  148 ASP C OD1 
9700  O OD2 . ASP C 148 ? 0.3787 1.2510 2.2966 0.0369  -0.1181 0.1346  148 ASP C OD2 
9701  N N   . LEU C 149 ? 0.4482 1.2432 2.2720 -0.0036 -0.1427 0.0283  149 LEU C N   
9702  C CA  . LEU C 149 ? 0.4645 1.2519 2.2741 -0.0162 -0.1534 -0.0049 149 LEU C CA  
9703  C C   . LEU C 149 ? 0.4696 1.2452 2.2329 -0.0040 -0.1482 -0.0089 149 LEU C C   
9704  O O   . LEU C 149 ? 0.4864 1.2860 2.2278 -0.0067 -0.1610 -0.0272 149 LEU C O   
9705  C CB  . LEU C 149 ? 0.4581 1.2039 2.2893 -0.0296 -0.1476 -0.0206 149 LEU C CB  
9706  C CG  . LEU C 149 ? 0.4748 1.2053 2.2961 -0.0419 -0.1571 -0.0570 149 LEU C CG  
9707  C CD1 . LEU C 149 ? 0.4992 1.2738 2.3231 -0.0529 -0.1804 -0.0801 149 LEU C CD1 
9708  C CD2 . LEU C 149 ? 0.4721 1.1644 2.3251 -0.0550 -0.1517 -0.0653 149 LEU C CD2 
9709  N N   . MET C 150 ? 0.4558 1.1965 2.2049 0.0093  -0.1294 0.0086  150 MET C N   
9710  C CA  . MET C 150 ? 0.4664 1.1933 2.1756 0.0205  -0.1225 0.0079  150 MET C CA  
9711  C C   . MET C 150 ? 0.4861 1.2579 2.1759 0.0303  -0.1314 0.0219  150 MET C C   
9712  O O   . MET C 150 ? 0.5017 1.2884 2.1618 0.0313  -0.1376 0.0094  150 MET C O   
9713  C CB  . MET C 150 ? 0.4440 1.1270 2.1473 0.0323  -0.1017 0.0257  150 MET C CB  
9714  C CG  . MET C 150 ? 0.4351 1.0757 2.1556 0.0235  -0.0927 0.0149  150 MET C CG  
9715  S SD  . MET C 150 ? 0.4516 1.0664 2.1562 0.0131  -0.0963 -0.0207 150 MET C SD  
9716  C CE  . MET C 150 ? 0.4573 1.0516 2.2049 -0.0045 -0.0982 -0.0320 150 MET C CE  
9717  N N   . ASN C 151 ? 0.4940 1.2901 2.2022 0.0378  -0.1322 0.0483  151 ASN C N   
9718  C CA  . ASN C 151 ? 0.5154 1.3551 2.2105 0.0481  -0.1408 0.0667  151 ASN C CA  
9719  C C   . ASN C 151 ? 0.5352 1.4225 2.2254 0.0368  -0.1628 0.0467  151 ASN C C   
9720  O O   . ASN C 151 ? 0.5516 1.4663 2.2117 0.0420  -0.1697 0.0471  151 ASN C O   
9721  C CB  . ASN C 151 ? 0.5110 1.3662 2.2322 0.0589  -0.1374 0.0981  151 ASN C CB  
9722  C CG  . ASN C 151 ? 0.5008 1.3179 2.2172 0.0748  -0.1174 0.1201  151 ASN C CG  
9723  O OD1 . ASN C 151 ? 0.5122 1.3125 2.1993 0.0835  -0.1104 0.1248  151 ASN C OD1 
9724  N ND2 . ASN C 151 ? 0.4822 1.2861 2.2275 0.0786  -0.1078 0.1328  151 ASN C ND2 
9725  N N   . THR C 152 ? 0.5297 1.4284 2.2501 0.0211  -0.1739 0.0295  152 THR C N   
9726  C CA  . THR C 152 ? 0.5508 1.4920 2.2693 0.0083  -0.1960 0.0053  152 THR C CA  
9727  C C   . THR C 152 ? 0.5648 1.4942 2.2466 0.0052  -0.1973 -0.0238 152 THR C C   
9728  O O   . THR C 152 ? 0.5823 1.5499 2.2358 0.0082  -0.2082 -0.0290 152 THR C O   
9729  C CB  . THR C 152 ? 0.5544 1.5000 2.3163 -0.0095 -0.2056 -0.0092 152 THR C CB  
9730  O OG1 . THR C 152 ? 0.5367 1.4986 2.3312 -0.0045 -0.2030 0.0198  152 THR C OG1 
9731  C CG2 . THR C 152 ? 0.5825 1.5740 2.3475 -0.0239 -0.2305 -0.0356 152 THR C CG2 
9732  N N   . LEU C 153 ? 0.5536 1.4315 2.2350 0.0008  -0.1851 -0.0406 153 LEU C N   
9733  C CA  . LEU C 153 ? 0.5716 1.4354 2.2236 -0.0023 -0.1852 -0.0708 153 LEU C CA  
9734  C C   . LEU C 153 ? 0.5754 1.4472 2.1845 0.0136  -0.1772 -0.0565 153 LEU C C   
9735  O O   . LEU C 153 ? 0.6052 1.5058 2.1852 0.0133  -0.1860 -0.0742 153 LEU C O   
9736  C CB  . LEU C 153 ? 0.5588 1.3643 2.2228 -0.0084 -0.1727 -0.0869 153 LEU C CB  
9737  C CG  . LEU C 153 ? 0.5606 1.3542 2.2636 -0.0271 -0.1818 -0.1099 153 LEU C CG  
9738  C CD1 . LEU C 153 ? 0.5449 1.2794 2.2592 -0.0295 -0.1665 -0.1156 153 LEU C CD1 
9739  C CD2 . LEU C 153 ? 0.5932 1.4146 2.2926 -0.0398 -0.2020 -0.1481 153 LEU C CD2 
9740  N N   . ILE C 154 ? 0.5457 1.3915 2.1512 0.0271  -0.1599 -0.0258 154 ILE C N   
9741  C CA  . ILE C 154 ? 0.5421 1.3938 2.1121 0.0413  -0.1518 -0.0092 154 ILE C CA  
9742  C C   . ILE C 154 ? 0.5609 1.4746 2.1140 0.0445  -0.1674 -0.0010 154 ILE C C   
9743  O O   . ILE C 154 ? 0.5820 1.5187 2.1026 0.0454  -0.1719 -0.0146 154 ILE C O   
9744  C CB  . ILE C 154 ? 0.5149 1.3355 2.0909 0.0549  -0.1342 0.0252  154 ILE C CB  
9745  C CG1 . ILE C 154 ? 0.4963 1.2583 2.0821 0.0526  -0.1186 0.0167  154 ILE C CG1 
9746  C CG2 . ILE C 154 ? 0.5199 1.3533 2.0645 0.0688  -0.1283 0.0472  154 ILE C CG2 
9747  C CD1 . ILE C 154 ? 0.4733 1.2076 2.0767 0.0626  -0.1046 0.0457  154 ILE C CD1 
9748  N N   . ASN C 155 ? 0.5543 1.4975 2.1300 0.0465  -0.1759 0.0210  155 ASN C N   
9749  C CA  . ASN C 155 ? 0.5719 1.5741 2.1335 0.0524  -0.1896 0.0375  155 ASN C CA  
9750  C C   . ASN C 155 ? 0.5987 1.6423 2.1412 0.0412  -0.2082 0.0039  155 ASN C C   
9751  O O   . ASN C 155 ? 0.6151 1.7000 2.1259 0.0469  -0.2149 0.0089  155 ASN C O   
9752  C CB  . ASN C 155 ? 0.5635 1.5896 2.1577 0.0565  -0.1958 0.0657  155 ASN C CB  
9753  C CG  . ASN C 155 ? 0.5422 1.5399 2.1460 0.0726  -0.1785 0.1028  155 ASN C CG  
9754  O OD1 . ASN C 155 ? 0.5389 1.5274 2.1181 0.0844  -0.1687 0.1206  155 ASN C OD1 
9755  N ND2 . ASN C 155 ? 0.5258 1.5102 2.1667 0.0732  -0.1747 0.1145  155 ASN C ND2 
9756  N N   . ILE C 156 ? 0.6037 1.6363 2.1655 0.0252  -0.2164 -0.0308 156 ILE C N   
9757  C CA  . ILE C 156 ? 0.6379 1.7065 2.1847 0.0138  -0.2348 -0.0679 156 ILE C CA  
9758  C C   . ILE C 156 ? 0.6521 1.7164 2.1552 0.0190  -0.2276 -0.0851 156 ILE C C   
9759  O O   . ILE C 156 ? 0.6835 1.7942 2.1595 0.0172  -0.2411 -0.1033 156 ILE C O   
9760  C CB  . ILE C 156 ? 0.6430 1.6923 2.2245 -0.0048 -0.2436 -0.1018 156 ILE C CB  
9761  C CG1 . ILE C 156 ? 0.6359 1.7098 2.2583 -0.0110 -0.2554 -0.0860 156 ILE C CG1 
9762  C CG2 . ILE C 156 ? 0.6770 1.7485 2.2408 -0.0160 -0.2592 -0.1482 156 ILE C CG2 
9763  C CD1 . ILE C 156 ? 0.6295 1.6724 2.2955 -0.0277 -0.2576 -0.1061 156 ILE C CD1 
9764  N N   . ILE C 157 ? 0.6306 1.6423 2.1273 0.0255  -0.2066 -0.0794 157 ILE C N   
9765  C CA  . ILE C 157 ? 0.6413 1.6450 2.1012 0.0303  -0.1976 -0.0958 157 ILE C CA  
9766  C C   . ILE C 157 ? 0.6497 1.6886 2.0760 0.0448  -0.1934 -0.0641 157 ILE C C   
9767  O O   . ILE C 157 ? 0.6759 1.7457 2.0669 0.0470  -0.1963 -0.0789 157 ILE C O   
9768  C CB  . ILE C 157 ? 0.6174 1.5536 2.0863 0.0309  -0.1782 -0.1023 157 ILE C CB  
9769  C CG1 . ILE C 157 ? 0.6163 1.5227 2.1148 0.0154  -0.1841 -0.1385 157 ILE C CG1 
9770  C CG2 . ILE C 157 ? 0.6255 1.5551 2.0571 0.0394  -0.1657 -0.1083 157 ILE C CG2 
9771  C CD1 . ILE C 157 ? 0.5896 1.4304 2.1083 0.0152  -0.1667 -0.1359 157 ILE C CD1 
9772  N N   . HIS C 158 ? 0.6323 1.6679 2.0706 0.0549  -0.1868 -0.0208 158 HIS C N   
9773  C CA  . HIS C 158 ? 0.6405 1.7062 2.0536 0.0687  -0.1827 0.0147  158 HIS C CA  
9774  C C   . HIS C 158 ? 0.6747 1.8135 2.0670 0.0678  -0.2026 0.0132  158 HIS C C   
9775  O O   . HIS C 158 ? 0.6919 1.8638 2.0494 0.0753  -0.2012 0.0239  158 HIS C O   
9776  C CB  . HIS C 158 ? 0.6143 1.6612 2.0510 0.0793  -0.1738 0.0592  158 HIS C CB  
9777  C CG  . HIS C 158 ? 0.5886 1.5710 2.0364 0.0842  -0.1527 0.0686  158 HIS C CG  
9778  N ND1 . HIS C 158 ? 0.5649 1.5207 2.0420 0.0908  -0.1453 0.0966  158 HIS C ND1 
9779  C CD2 . HIS C 158 ? 0.5859 1.5280 2.0204 0.0843  -0.1382 0.0547  158 HIS C CD2 
9780  C CE1 . HIS C 158 ? 0.5467 1.4482 2.0265 0.0940  -0.1275 0.0980  158 HIS C CE1 
9781  N NE2 . HIS C 158 ? 0.5600 1.4525 2.0149 0.0899  -0.1232 0.0738  158 HIS C NE2 
9782  N N   . LYS C 159 ? 0.6897 1.8561 2.1038 0.0584  -0.2213 0.0012  159 LYS C N   
9783  C CA  . LYS C 159 ? 0.7257 1.9638 2.1221 0.0563  -0.2427 -0.0032 159 LYS C CA  
9784  C C   . LYS C 159 ? 0.7646 2.0222 2.1338 0.0466  -0.2517 -0.0523 159 LYS C C   
9785  O O   . LYS C 159 ? 0.7973 2.1146 2.1350 0.0482  -0.2643 -0.0572 159 LYS C O   
9786  C CB  . LYS C 159 ? 0.7228 1.9867 2.1549 0.0490  -0.2610 0.0004  159 LYS C CB  
9787  C CG  . LYS C 159 ? 0.7214 1.9635 2.1846 0.0314  -0.2698 -0.0396 159 LYS C CG  
9788  C CD  . LYS C 159 ? 0.7552 2.0297 2.2018 0.0182  -0.2880 -0.0883 159 LYS C CD  
9789  C CE  . LYS C 159 ? 0.7538 2.0112 2.2391 0.0001  -0.2995 -0.1219 159 LYS C CE  
9790  N NZ  . LYS C 159 ? 0.7587 2.0624 2.2711 -0.0058 -0.3199 -0.1111 159 LYS C NZ  
9791  N N   . GLY C 160 ? 0.7618 1.9704 2.1448 0.0368  -0.2459 -0.0888 160 GLY C N   
9792  C CA  . GLY C 160 ? 0.7901 2.0107 2.1586 0.0260  -0.2564 -0.1410 160 GLY C CA  
9793  C C   . GLY C 160 ? 0.8056 2.0220 2.1333 0.0336  -0.2427 -0.1543 160 GLY C C   
9794  O O   . GLY C 160 ? 0.8465 2.1116 2.1402 0.0337  -0.2524 -0.1767 160 GLY C O   
9795  N N   . HIS C 161 ? 0.7758 1.9355 2.1076 0.0399  -0.2204 -0.1415 161 HIS C N   
9796  C CA  . HIS C 161 ? 0.7803 1.9351 2.0769 0.0489  -0.2046 -0.1445 161 HIS C CA  
9797  C C   . HIS C 161 ? 0.7614 1.9093 2.0521 0.0625  -0.1892 -0.0910 161 HIS C C   
9798  O O   . HIS C 161 ? 0.7311 1.8237 2.0430 0.0655  -0.1737 -0.0733 161 HIS C O   
9799  C CB  . HIS C 161 ? 0.7701 1.8678 2.0770 0.0438  -0.1935 -0.1806 161 HIS C CB  
9800  C CG  . HIS C 161 ? 0.7871 1.8933 2.0573 0.0503  -0.1830 -0.2006 161 HIS C CG  
9801  N ND1 . HIS C 161 ? 0.7808 1.8418 2.0567 0.0479  -0.1729 -0.2335 161 HIS C ND1 
9802  C CD2 . HIS C 161 ? 0.8059 1.9611 2.0349 0.0596  -0.1802 -0.1904 161 HIS C CD2 
9803  C CE1 . HIS C 161 ? 0.7996 1.8830 2.0393 0.0558  -0.1643 -0.2447 161 HIS C CE1 
9804  N NE2 . HIS C 161 ? 0.8144 1.9559 2.0246 0.0627  -0.1682 -0.2188 161 HIS C NE2 
9805  N N   . PRO C 162 ? 0.7785 1.9834 2.0424 0.0709  -0.1940 -0.0627 162 PRO C N   
9806  C CA  . PRO C 162 ? 0.7585 1.9593 2.0226 0.0832  -0.1821 -0.0092 162 PRO C CA  
9807  C C   . PRO C 162 ? 0.7494 1.9184 1.9966 0.0910  -0.1597 0.0000  162 PRO C C   
9808  O O   . PRO C 162 ? 0.7717 1.9617 1.9871 0.0919  -0.1560 -0.0217 162 PRO C O   
9809  C CB  . PRO C 162 ? 0.7872 2.0647 2.0268 0.0882  -0.1967 0.0124  162 PRO C CB  
9810  C CG  . PRO C 162 ? 0.8244 2.1446 2.0317 0.0819  -0.2076 -0.0330 162 PRO C CG  
9811  C CD  . PRO C 162 ? 0.8173 2.0943 2.0504 0.0689  -0.2119 -0.0804 162 PRO C CD  
9812  N N   . GLY C 163 ? 0.7184 1.8377 1.9886 0.0964  -0.1452 0.0305  163 GLY C N   
9813  C CA  . GLY C 163 ? 0.7101 1.8017 1.9690 0.1042  -0.1249 0.0486  163 GLY C CA  
9814  C C   . GLY C 163 ? 0.6943 1.7235 1.9658 0.0998  -0.1119 0.0203  163 GLY C C   
9815  O O   . GLY C 163 ? 0.6895 1.6946 1.9519 0.1050  -0.0954 0.0283  163 GLY C O   
9816  N N   . ILE C 164 ? 0.6867 1.6918 1.9805 0.0899  -0.1199 -0.0116 164 ILE C N   
9817  C CA  . ILE C 164 ? 0.6736 1.6219 1.9812 0.0852  -0.1095 -0.0388 164 ILE C CA  
9818  C C   . ILE C 164 ? 0.6400 1.5366 1.9833 0.0852  -0.1031 -0.0181 164 ILE C C   
9819  O O   . ILE C 164 ? 0.6338 1.5375 1.9991 0.0825  -0.1130 -0.0069 164 ILE C O   
9820  C CB  . ILE C 164 ? 0.6903 1.6428 1.9995 0.0742  -0.1210 -0.0896 164 ILE C CB  
9821  C CG1 . ILE C 164 ? 0.7266 1.7283 1.9978 0.0755  -0.1254 -0.1154 164 ILE C CG1 
9822  C CG2 . ILE C 164 ? 0.6707 1.5600 2.0017 0.0695  -0.1109 -0.1123 164 ILE C CG2 
9823  C CD1 . ILE C 164 ? 0.7502 1.8219 1.9968 0.0791  -0.1380 -0.0977 164 ILE C CD1 
9824  N N   . PRO C 165 ? 0.6195 1.4662 1.9690 0.0890  -0.0860 -0.0112 165 PRO C N   
9825  C CA  . PRO C 165 ? 0.5902 1.3848 1.9719 0.0879  -0.0794 -0.0010 165 PRO C CA  
9826  C C   . PRO C 165 ? 0.5880 1.3631 1.9947 0.0765  -0.0879 -0.0304 165 PRO C C   
9827  O O   . PRO C 165 ? 0.6049 1.3833 2.0063 0.0692  -0.0933 -0.0664 165 PRO C O   
9828  C CB  . PRO C 165 ? 0.5749 1.3274 1.9516 0.0927  -0.0615 0.0017  165 PRO C CB  
9829  C CG  . PRO C 165 ? 0.5962 1.3844 1.9411 0.0995  -0.0572 0.0127  165 PRO C CG  
9830  C CD  . PRO C 165 ? 0.6252 1.4674 1.9510 0.0951  -0.0721 -0.0102 165 PRO C CD  
9831  N N   . VAL C 166 ? 0.5655 1.3204 2.0015 0.0755  -0.0884 -0.0139 166 VAL C N   
9832  C CA  . VAL C 166 ? 0.5542 1.2819 2.0191 0.0651  -0.0923 -0.0340 166 VAL C CA  
9833  C C   . VAL C 166 ? 0.5242 1.1992 2.0077 0.0688  -0.0774 -0.0180 166 VAL C C   
9834  O O   . VAL C 166 ? 0.5121 1.1810 1.9964 0.0784  -0.0696 0.0130  166 VAL C O   
9835  C CB  . VAL C 166 ? 0.5606 1.3215 2.0451 0.0594  -0.1081 -0.0299 166 VAL C CB  
9836  C CG1 . VAL C 166 ? 0.5547 1.2926 2.0710 0.0465  -0.1134 -0.0521 166 VAL C CG1 
9837  C CG2 . VAL C 166 ? 0.5900 1.4101 2.0526 0.0580  -0.1235 -0.0389 166 VAL C CG2 
9838  N N   . THR C 167 ? 0.5136 1.1515 2.0130 0.0612  -0.0741 -0.0396 167 THR C N   
9839  C CA  . THR C 167 ? 0.4857 1.0785 2.0060 0.0627  -0.0627 -0.0268 167 THR C CA  
9840  C C   . THR C 167 ? 0.4797 1.0502 2.0248 0.0502  -0.0669 -0.0512 167 THR C C   
9841  O O   . THR C 167 ? 0.4936 1.0877 2.0456 0.0406  -0.0805 -0.0723 167 THR C O   
9842  C CB  . THR C 167 ? 0.4774 1.0401 1.9812 0.0715  -0.0474 -0.0182 167 THR C CB  
9843  O OG1 . THR C 167 ? 0.4584 0.9803 1.9822 0.0723  -0.0380 -0.0080 167 THR C OG1 
9844  C CG2 . THR C 167 ? 0.4940 1.0483 1.9824 0.0685  -0.0456 -0.0463 167 THR C CG2 
9845  N N   . LEU C 168 ? 0.4584 0.9849 2.0182 0.0502  -0.0560 -0.0473 168 LEU C N   
9846  C CA  . LEU C 168 ? 0.4568 0.9596 2.0431 0.0387  -0.0587 -0.0653 168 LEU C CA  
9847  C C   . LEU C 168 ? 0.4467 0.9044 2.0313 0.0411  -0.0462 -0.0699 168 LEU C C   
9848  O O   . LEU C 168 ? 0.4340 0.8796 2.0001 0.0513  -0.0355 -0.0568 168 LEU C O   
9849  C CB  . LEU C 168 ? 0.4452 0.9481 2.0615 0.0343  -0.0602 -0.0492 168 LEU C CB  
9850  C CG  . LEU C 168 ? 0.4246 0.8942 2.0498 0.0409  -0.0455 -0.0267 168 LEU C CG  
9851  C CD1 . LEU C 168 ? 0.4180 0.8927 2.0739 0.0358  -0.0470 -0.0142 168 LEU C CD1 
9852  C CD2 . LEU C 168 ? 0.4183 0.8907 2.0221 0.0555  -0.0368 -0.0038 168 LEU C CD2 
9853  N N   . SER C 169 ? 0.4534 0.8870 2.0607 0.0312  -0.0482 -0.0870 169 SER C N   
9854  C CA  . SER C 169 ? 0.4509 0.8437 2.0599 0.0325  -0.0386 -0.0939 169 SER C CA  
9855  C C   . SER C 169 ? 0.4325 0.7966 2.0626 0.0320  -0.0302 -0.0738 169 SER C C   
9856  O O   . SER C 169 ? 0.4404 0.7801 2.0933 0.0241  -0.0304 -0.0822 169 SER C O   
9857  C CB  . SER C 169 ? 0.4730 0.8567 2.0937 0.0231  -0.0463 -0.1269 169 SER C CB  
9858  O OG  . SER C 169 ? 0.4937 0.9111 2.0987 0.0214  -0.0569 -0.1491 169 SER C OG  
9859  N N   . ALA C 170 ? 0.4125 0.7804 2.0361 0.0406  -0.0228 -0.0472 170 ALA C N   
9860  C CA  . ALA C 170 ? 0.3970 0.7454 2.0398 0.0404  -0.0155 -0.0291 170 ALA C CA  
9861  C C   . ALA C 170 ? 0.3888 0.6987 2.0274 0.0440  -0.0050 -0.0290 170 ALA C C   
9862  O O   . ALA C 170 ? 0.3949 0.6969 2.0127 0.0501  -0.0015 -0.0355 170 ALA C O   
9863  C CB  . ALA C 170 ? 0.3835 0.7480 2.0219 0.0495  -0.0111 -0.0041 170 ALA C CB  
9864  N N   . ASN C 171 ? 0.3877 0.6764 2.0471 0.0397  -0.0005 -0.0215 171 ASN C N   
9865  C CA  . ASN C 171 ? 0.3909 0.6449 2.0492 0.0422  0.0079  -0.0208 171 ASN C CA  
9866  C C   . ASN C 171 ? 0.3746 0.6193 2.0213 0.0529  0.0191  0.0016  171 ASN C C   
9867  O O   . ASN C 171 ? 0.3593 0.6131 2.0159 0.0538  0.0220  0.0174  171 ASN C O   
9868  C CB  . ASN C 171 ? 0.4036 0.6399 2.0914 0.0310  0.0055  -0.0259 171 ASN C CB  
9869  C CG  . ASN C 171 ? 0.4041 0.6069 2.0921 0.0344  0.0143  -0.0197 171 ASN C CG  
9870  O OD1 . ASN C 171 ? 0.3951 0.5909 2.0770 0.0411  0.0233  -0.0004 171 ASN C OD1 
9871  N ND2 . ASN C 171 ? 0.4171 0.6000 2.1129 0.0305  0.0115  -0.0365 171 ASN C ND2 
9872  N N   . ALA C 172 ? 0.3762 0.6032 2.0035 0.0610  0.0256  0.0017  172 ALA C N   
9873  C CA  . ALA C 172 ? 0.3685 0.5895 1.9826 0.0717  0.0346  0.0197  172 ALA C CA  
9874  C C   . ALA C 172 ? 0.3699 0.5743 1.9964 0.0714  0.0412  0.0320  172 ALA C C   
9875  O O   . ALA C 172 ? 0.3945 0.6012 2.0167 0.0788  0.0475  0.0468  172 ALA C O   
9876  C CB  . ALA C 172 ? 0.3583 0.5663 1.9512 0.0791  0.0389  0.0169  172 ALA C CB  
9877  N N   . MET C 173 ? 0.3664 0.5554 2.0089 0.0634  0.0400  0.0264  173 MET C N   
9878  C CA  . MET C 173 ? 0.3570 0.5320 2.0088 0.0636  0.0469  0.0401  173 MET C CA  
9879  C C   . MET C 173 ? 0.3593 0.5535 2.0294 0.0595  0.0474  0.0523  173 MET C C   
9880  O O   . MET C 173 ? 0.3585 0.5482 2.0332 0.0616  0.0547  0.0665  173 MET C O   
9881  C CB  . MET C 173 ? 0.3616 0.5137 2.0268 0.0568  0.0454  0.0332  173 MET C CB  
9882  C CG  . MET C 173 ? 0.3527 0.4844 2.0015 0.0629  0.0476  0.0256  173 MET C CG  
9883  S SD  . MET C 173 ? 0.3422 0.4628 1.9732 0.0740  0.0578  0.0431  173 MET C SD  
9884  C CE  . MET C 173 ? 0.3400 0.4525 1.9898 0.0693  0.0619  0.0590  173 MET C CE  
9885  N N   . ILE C 174 ? 0.3646 0.5827 2.0453 0.0538  0.0396  0.0467  174 ILE C N   
9886  C CA  . ILE C 174 ? 0.3676 0.6065 2.0718 0.0474  0.0384  0.0566  174 ILE C CA  
9887  C C   . ILE C 174 ? 0.3676 0.6371 2.0689 0.0517  0.0350  0.0600  174 ILE C C   
9888  O O   . ILE C 174 ? 0.3570 0.6456 2.0736 0.0515  0.0374  0.0726  174 ILE C O   
9889  C CB  . ILE C 174 ? 0.3759 0.6144 2.1084 0.0318  0.0298  0.0469  174 ILE C CB  
9890  C CG1 . ILE C 174 ? 0.3825 0.6307 2.1123 0.0268  0.0177  0.0249  174 ILE C CG1 
9891  C CG2 . ILE C 174 ? 0.3834 0.5923 2.1253 0.0276  0.0334  0.0481  174 ILE C CG2 
9892  C CD1 . ILE C 174 ? 0.3947 0.6529 2.1557 0.0112  0.0069  0.0145  174 ILE C CD1 
9893  N N   . SER C 175 ? 0.3813 0.6580 2.0651 0.0553  0.0292  0.0495  175 SER C N   
9894  C CA  . SER C 175 ? 0.3793 0.6853 2.0585 0.0606  0.0252  0.0543  175 SER C CA  
9895  C C   . SER C 175 ? 0.3687 0.6681 2.0232 0.0752  0.0321  0.0627  175 SER C C   
9896  O O   . SER C 175 ? 0.3778 0.6928 2.0199 0.0800  0.0277  0.0624  175 SER C O   
9897  C CB  . SER C 175 ? 0.3906 0.7159 2.0711 0.0524  0.0120  0.0377  175 SER C CB  
9898  O OG  . SER C 175 ? 0.4040 0.7237 2.1056 0.0382  0.0053  0.0239  175 SER C OG  
9899  N N   . ASP C 176 ? 0.3524 0.6297 2.0007 0.0821  0.0425  0.0710  176 ASP C N   
9900  C CA  . ASP C 176 ? 0.3460 0.6152 1.9758 0.0953  0.0489  0.0790  176 ASP C CA  
9901  C C   . ASP C 176 ? 0.3491 0.6419 1.9855 0.1035  0.0497  0.0921  176 ASP C C   
9902  O O   . ASP C 176 ? 0.3431 0.6433 1.9692 0.1112  0.0480  0.0964  176 ASP C O   
9903  C CB  . ASP C 176 ? 0.3358 0.5781 1.9595 0.0998  0.0585  0.0827  176 ASP C CB  
9904  C CG  . ASP C 176 ? 0.3302 0.5735 1.9711 0.0957  0.0633  0.0893  176 ASP C CG  
9905  O OD1 . ASP C 176 ? 0.3257 0.5889 1.9863 0.0876  0.0586  0.0903  176 ASP C OD1 
9906  O OD2 . ASP C 176 ? 0.3220 0.5483 1.9568 0.1001  0.0712  0.0939  176 ASP C OD2 
9907  N N   . TYR C 177 ? 0.3518 0.6572 2.0078 0.1017  0.0524  0.0994  177 TYR C N   
9908  C CA  . TYR C 177 ? 0.3485 0.6769 2.0160 0.1100  0.0547  0.1122  177 TYR C CA  
9909  C C   . TYR C 177 ? 0.3656 0.7235 2.0387 0.1083  0.0439  0.1127  177 TYR C C   
9910  O O   . TYR C 177 ? 0.3693 0.7475 2.0504 0.1172  0.0442  0.1241  177 TYR C O   
9911  C CB  . TYR C 177 ? 0.3435 0.6830 2.0335 0.1049  0.0591  0.1181  177 TYR C CB  
9912  C CG  . TYR C 177 ? 0.3490 0.7065 2.0588 0.0892  0.0491  0.1123  177 TYR C CG  
9913  C CD1 . TYR C 177 ? 0.3570 0.6970 2.0684 0.0766  0.0454  0.1009  177 TYR C CD1 
9914  C CD2 . TYR C 177 ? 0.3451 0.7368 2.0738 0.0869  0.0422  0.1169  177 TYR C CD2 
9915  C CE1 . TYR C 177 ? 0.3605 0.7143 2.0924 0.0618  0.0353  0.0931  177 TYR C CE1 
9916  C CE2 . TYR C 177 ? 0.3506 0.7586 2.0985 0.0716  0.0316  0.1094  177 TYR C CE2 
9917  C CZ  . TYR C 177 ? 0.3586 0.7465 2.1084 0.0588  0.0280  0.0967  177 TYR C CZ  
9918  O OH  . TYR C 177 ? 0.3690 0.7687 2.1391 0.0433  0.0169  0.0864  177 TYR C OH  
9919  N N   . MET C 178 ? 0.3807 0.7428 2.0506 0.0972  0.0340  0.0999  178 MET C N   
9920  C CA  . MET C 178 ? 0.3937 0.7886 2.0701 0.0928  0.0220  0.0981  178 MET C CA  
9921  C C   . MET C 178 ? 0.3995 0.8031 2.0580 0.1034  0.0197  0.1047  178 MET C C   
9922  O O   . MET C 178 ? 0.3929 0.7764 2.0308 0.1071  0.0228  0.1013  178 MET C O   
9923  C CB  . MET C 178 ? 0.3998 0.7959 2.0779 0.0778  0.0121  0.0791  178 MET C CB  
9924  C CG  . MET C 178 ? 0.4114 0.8418 2.0896 0.0734  -0.0017 0.0732  178 MET C CG  
9925  S SD  . MET C 178 ? 0.4330 0.8674 2.1168 0.0557  -0.0146 0.0466  178 MET C SD  
9926  C CE  . MET C 178 ? 0.4358 0.8704 2.1576 0.0436  -0.0144 0.0490  178 MET C CE  
9927  N N   . ASP C 179 ? 0.4081 0.8442 2.0769 0.1075  0.0136  0.1152  179 ASP C N   
9928  C CA  . ASP C 179 ? 0.4199 0.8715 2.0759 0.1162  0.0092  0.1245  179 ASP C CA  
9929  C C   . ASP C 179 ? 0.4237 0.8926 2.0656 0.1071  -0.0025 0.1115  179 ASP C C   
9930  O O   . ASP C 179 ? 0.4377 0.9274 2.0909 0.0961  -0.0120 0.1008  179 ASP C O   
9931  C CB  . ASP C 179 ? 0.4285 0.9123 2.1036 0.1234  0.0054  0.1407  179 ASP C CB  
9932  C CG  . ASP C 179 ? 0.4559 0.9659 2.1227 0.1301  -0.0029 0.1521  179 ASP C CG  
9933  O OD1 . ASP C 179 ? 0.4631 0.9889 2.1157 0.1221  -0.0127 0.1424  179 ASP C OD1 
9934  O OD2 . ASP C 179 ? 0.4802 0.9963 2.1559 0.1435  0.0003  0.1707  179 ASP C OD2 
9935  N N   . GLU C 180 ? 0.4197 0.8837 2.0385 0.1118  -0.0021 0.1126  180 GLU C N   
9936  C CA  . GLU C 180 ? 0.4233 0.9096 2.0264 0.1050  -0.0125 0.1006  180 GLU C CA  
9937  C C   . GLU C 180 ? 0.4318 0.9468 2.0241 0.1138  -0.0173 0.1179  180 GLU C C   
9938  O O   . GLU C 180 ? 0.4455 0.9812 2.0197 0.1105  -0.0243 0.1110  180 GLU C O   
9939  C CB  . GLU C 180 ? 0.4218 0.8827 2.0055 0.1006  -0.0084 0.0837  180 GLU C CB  
9940  C CG  . GLU C 180 ? 0.4095 0.8416 2.0035 0.0917  -0.0045 0.0671  180 GLU C CG  
9941  C CD  . GLU C 180 ? 0.4048 0.8179 1.9836 0.0864  -0.0033 0.0471  180 GLU C CD  
9942  O OE1 . GLU C 180 ? 0.4144 0.8465 1.9762 0.0856  -0.0088 0.0387  180 GLU C OE1 
9943  O OE2 . GLU C 180 ? 0.3912 0.7726 1.9755 0.0836  0.0034  0.0403  180 GLU C OE2 
9944  N N   . SER C 181 ? 0.4254 0.9437 2.0298 0.1252  -0.0138 0.1404  181 SER C N   
9945  C CA  . SER C 181 ? 0.4345 0.9766 2.0329 0.1349  -0.0176 0.1615  181 SER C CA  
9946  C C   . SER C 181 ? 0.4470 1.0385 2.0446 0.1303  -0.0328 0.1617  181 SER C C   
9947  O O   . SER C 181 ? 0.4637 1.0793 2.0483 0.1354  -0.0377 0.1752  181 SER C O   
9948  C CB  . SER C 181 ? 0.4271 0.9608 2.0446 0.1484  -0.0112 0.1835  181 SER C CB  
9949  O OG  . SER C 181 ? 0.4074 0.9556 2.0495 0.1473  -0.0138 0.1835  181 SER C OG  
9950  N N   . ILE C 182 ? 0.4467 1.0561 2.0596 0.1208  -0.0410 0.1485  182 ILE C N   
9951  C CA  . ILE C 182 ? 0.4604 1.1184 2.0726 0.1156  -0.0569 0.1465  182 ILE C CA  
9952  C C   . ILE C 182 ? 0.4677 1.1361 2.0511 0.1078  -0.0628 0.1273  182 ILE C C   
9953  O O   . ILE C 182 ? 0.4781 1.1880 2.0496 0.1069  -0.0746 0.1290  182 ILE C O   
9954  C CB  . ILE C 182 ? 0.4608 1.1357 2.1004 0.1063  -0.0648 0.1372  182 ILE C CB  
9955  C CG1 . ILE C 182 ? 0.4647 1.1153 2.1072 0.0918  -0.0635 0.1089  182 ILE C CG1 
9956  C CG2 . ILE C 182 ? 0.4453 1.1156 2.1128 0.1161  -0.0578 0.1577  182 ILE C CG2 
9957  C CD1 . ILE C 182 ? 0.4654 1.1347 2.1371 0.0802  -0.0724 0.0997  182 ILE C CD1 
9958  N N   . PHE C 183 ? 0.4607 1.0936 2.0322 0.1031  -0.0543 0.1092  183 PHE C N   
9959  C CA  . PHE C 183 ? 0.4721 1.1135 2.0184 0.0965  -0.0584 0.0880  183 PHE C CA  
9960  C C   . PHE C 183 ? 0.4689 1.1123 1.9899 0.1059  -0.0521 0.1033  183 PHE C C   
9961  O O   . PHE C 183 ? 0.4531 1.0757 1.9781 0.1159  -0.0423 0.1257  183 PHE C O   
9962  C CB  . PHE C 183 ? 0.4643 1.0680 2.0120 0.0876  -0.0526 0.0617  183 PHE C CB  
9963  C CG  . PHE C 183 ? 0.4511 1.0486 2.0259 0.0766  -0.0577 0.0468  183 PHE C CG  
9964  C CD1 . PHE C 183 ? 0.4631 1.0867 2.0425 0.0646  -0.0719 0.0240  183 PHE C CD1 
9965  C CD2 . PHE C 183 ? 0.4275 0.9929 2.0234 0.0777  -0.0481 0.0549  183 PHE C CD2 
9966  C CE1 . PHE C 183 ? 0.4557 1.0718 2.0633 0.0533  -0.0765 0.0115  183 PHE C CE1 
9967  C CE2 . PHE C 183 ? 0.4223 0.9829 2.0438 0.0669  -0.0517 0.0436  183 PHE C CE2 
9968  C CZ  . PHE C 183 ? 0.4368 1.0220 2.0658 0.0543  -0.0660 0.0229  183 PHE C CZ  
9969  N N   . ASP C 184 ? 0.4855 1.1540 1.9818 0.1023  -0.0577 0.0893  184 ASP C N   
9970  C CA  . ASP C 184 ? 0.4967 1.1768 1.9681 0.1098  -0.0527 0.1039  184 ASP C CA  
9971  C C   . ASP C 184 ? 0.4945 1.1300 1.9596 0.1120  -0.0375 0.1008  184 ASP C C   
9972  O O   . ASP C 184 ? 0.4957 1.1286 1.9504 0.1197  -0.0300 0.1215  184 ASP C O   
9973  C CB  . ASP C 184 ? 0.5136 1.2383 1.9593 0.1054  -0.0626 0.0881  184 ASP C CB  
9974  C CG  . ASP C 184 ? 0.5210 1.2952 1.9704 0.1021  -0.0798 0.0880  184 ASP C CG  
9975  O OD1 . ASP C 184 ? 0.5123 1.2982 1.9778 0.1082  -0.0830 0.1150  184 ASP C OD1 
9976  O OD2 . ASP C 184 ? 0.5314 1.3328 1.9682 0.0938  -0.0903 0.0604  184 ASP C OD2 
9977  N N   . VAL C 185 ? 0.4961 1.0980 1.9693 0.1049  -0.0337 0.0764  185 VAL C N   
9978  C CA  . VAL C 185 ? 0.4986 1.0604 1.9665 0.1059  -0.0210 0.0695  185 VAL C CA  
9979  C C   . VAL C 185 ? 0.4885 1.0081 1.9791 0.1032  -0.0156 0.0638  185 VAL C C   
9980  O O   . VAL C 185 ? 0.5030 1.0267 2.0114 0.0977  -0.0222 0.0573  185 VAL C O   
9981  C CB  . VAL C 185 ? 0.5128 1.0843 1.9611 0.1003  -0.0224 0.0412  185 VAL C CB  
9982  C CG1 . VAL C 185 ? 0.5030 1.0321 1.9518 0.0992  -0.0113 0.0273  185 VAL C CG1 
9983  C CG2 . VAL C 185 ? 0.5269 1.1389 1.9488 0.1048  -0.0239 0.0499  185 VAL C CG2 
9984  N N   . TYR C 186 ? 0.4835 0.9650 1.9739 0.1068  -0.0037 0.0676  186 TYR C N   
9985  C CA  . TYR C 186 ? 0.4721 0.9142 1.9789 0.1042  0.0023  0.0601  186 TYR C CA  
9986  C C   . TYR C 186 ? 0.4668 0.8943 1.9690 0.0965  0.0027  0.0325  186 TYR C C   
9987  O O   . TYR C 186 ? 0.4754 0.9075 1.9598 0.0977  0.0053  0.0249  186 TYR C O   
9988  C CB  . TYR C 186 ? 0.4728 0.8850 1.9817 0.1129  0.0135  0.0794  186 TYR C CB  
9989  C CG  . TYR C 186 ? 0.4822 0.9074 2.0001 0.1211  0.0125  0.1050  186 TYR C CG  
9990  C CD1 . TYR C 186 ? 0.4902 0.9193 2.0276 0.1210  0.0093  0.1088  186 TYR C CD1 
9991  C CD2 . TYR C 186 ? 0.4841 0.9204 1.9934 0.1289  0.0143  0.1257  186 TYR C CD2 
9992  C CE1 . TYR C 186 ? 0.4938 0.9367 2.0421 0.1296  0.0081  0.1309  186 TYR C CE1 
9993  C CE2 . TYR C 186 ? 0.4893 0.9373 2.0103 0.1371  0.0126  0.1490  186 TYR C CE2 
9994  C CZ  . TYR C 186 ? 0.4941 0.9452 2.0345 0.1380  0.0095  0.1508  186 TYR C CZ  
9995  O OH  . TYR C 186 ? 0.5050 0.9683 2.0598 0.1472  0.0078  0.1727  186 TYR C OH  
9996  N N   . ALA C 187 ? 0.4511 0.8613 1.9711 0.0891  0.0006  0.0185  187 ALA C N   
9997  C CA  . ALA C 187 ? 0.4544 0.8478 1.9752 0.0822  0.0004  -0.0072 187 ALA C CA  
9998  C C   . ALA C 187 ? 0.4346 0.7954 1.9777 0.0773  0.0035  -0.0104 187 ALA C C   
9999  O O   . ALA C 187 ? 0.4341 0.7973 1.9942 0.0754  0.0015  -0.0002 187 ALA C O   
10000 C CB  . ALA C 187 ? 0.4720 0.8962 1.9893 0.0749  -0.0114 -0.0292 187 ALA C CB  
10001 N N   . TYR C 188 ? 0.4181 0.7508 1.9618 0.0756  0.0083  -0.0238 188 TYR C N   
10002 C CA  . TYR C 188 ? 0.4082 0.7107 1.9724 0.0708  0.0111  -0.0261 188 TYR C CA  
10003 C C   . TYR C 188 ? 0.4187 0.7013 1.9869 0.0663  0.0109  -0.0487 188 TYR C C   
10004 O O   . TYR C 188 ? 0.4266 0.7072 1.9790 0.0707  0.0143  -0.0575 188 TYR C O   
10005 C CB  . TYR C 188 ? 0.3922 0.6693 1.9561 0.0779  0.0217  -0.0066 188 TYR C CB  
10006 C CG  . TYR C 188 ? 0.3886 0.6775 1.9551 0.0832  0.0233  0.0151  188 TYR C CG  
10007 C CD1 . TYR C 188 ? 0.3865 0.6852 1.9724 0.0783  0.0194  0.0196  188 TYR C CD1 
10008 C CD2 . TYR C 188 ? 0.3867 0.6773 1.9393 0.0931  0.0286  0.0310  188 TYR C CD2 
10009 C CE1 . TYR C 188 ? 0.3815 0.6927 1.9718 0.0844  0.0213  0.0385  188 TYR C CE1 
10010 C CE2 . TYR C 188 ? 0.3838 0.6840 1.9416 0.0990  0.0299  0.0496  188 TYR C CE2 
10011 C CZ  . TYR C 188 ? 0.3807 0.6917 1.9569 0.0953  0.0265  0.0527  188 TYR C CZ  
10012 O OH  . TYR C 188 ? 0.3942 0.7159 1.9771 0.1025  0.0284  0.0702  188 TYR C OH  
10013 N N   . ASN C 189 ? 0.4111 0.6788 2.0032 0.0577  0.0074  -0.0567 189 ASN C N   
10014 C CA  . ASN C 189 ? 0.4099 0.6492 2.0127 0.0547  0.0091  -0.0715 189 ASN C CA  
10015 C C   . ASN C 189 ? 0.3850 0.5961 1.9873 0.0607  0.0196  -0.0536 189 ASN C C   
10016 O O   . ASN C 189 ? 0.3809 0.5834 1.9952 0.0594  0.0223  -0.0374 189 ASN C O   
10017 C CB  . ASN C 189 ? 0.4248 0.6585 2.0566 0.0427  0.0008  -0.0844 189 ASN C CB  
10018 C CG  . ASN C 189 ? 0.4454 0.7055 2.0784 0.0361  -0.0111 -0.1076 189 ASN C CG  
10019 O OD1 . ASN C 189 ? 0.4595 0.7364 2.0705 0.0410  -0.0121 -0.1207 189 ASN C OD1 
10020 N ND2 . ASN C 189 ? 0.4441 0.7100 2.1028 0.0247  -0.0202 -0.1134 189 ASN C ND2 
10021 N N   . CYS C 190 ? 0.3734 0.5727 1.9614 0.0675  0.0255  -0.0566 190 CYS C N   
10022 C CA  . CYS C 190 ? 0.3598 0.5356 1.9451 0.0735  0.0343  -0.0407 190 CYS C CA  
10023 C C   . CYS C 190 ? 0.3674 0.5164 1.9648 0.0721  0.0357  -0.0517 190 CYS C C   
10024 O O   . CYS C 190 ? 0.3656 0.5152 1.9613 0.0725  0.0339  -0.0707 190 CYS C O   
10025 C CB  . CYS C 190 ? 0.3482 0.5325 1.9103 0.0826  0.0399  -0.0304 190 CYS C CB  
10026 S SG  . CYS C 190 ? 0.3411 0.5622 1.8892 0.0847  0.0361  -0.0226 190 CYS C SG  
10027 N N   . TYR C 191 ? 0.3677 0.4950 1.9779 0.0712  0.0390  -0.0391 191 TYR C N   
10028 C CA  . TYR C 191 ? 0.3798 0.4814 2.0037 0.0707  0.0402  -0.0440 191 TYR C CA  
10029 C C   . TYR C 191 ? 0.3693 0.4538 1.9900 0.0757  0.0470  -0.0244 191 TYR C C   
10030 O O   . TYR C 191 ? 0.3451 0.4300 1.9696 0.0743  0.0488  -0.0083 191 TYR C O   
10031 C CB  . TYR C 191 ? 0.4056 0.4985 2.0581 0.0607  0.0341  -0.0509 191 TYR C CB  
10032 C CG  . TYR C 191 ? 0.4361 0.5398 2.0967 0.0551  0.0259  -0.0764 191 TYR C CG  
10033 C CD1 . TYR C 191 ? 0.4558 0.5864 2.1118 0.0507  0.0201  -0.0816 191 TYR C CD1 
10034 C CD2 . TYR C 191 ? 0.4565 0.5440 2.1308 0.0544  0.0234  -0.0959 191 TYR C CD2 
10035 C CE1 . TYR C 191 ? 0.4838 0.6263 2.1461 0.0453  0.0116  -0.1069 191 TYR C CE1 
10036 C CE2 . TYR C 191 ? 0.4903 0.5874 2.1725 0.0496  0.0156  -0.1225 191 TYR C CE2 
10037 C CZ  . TYR C 191 ? 0.5016 0.6269 2.1765 0.0447  0.0094  -0.1289 191 TYR C CZ  
10038 O OH  . TYR C 191 ? 0.5352 0.6711 2.2172 0.0399  0.0007  -0.1577 191 TYR C OH  
10039 N N   . ASP C 192 ? 0.3828 0.4531 1.9990 0.0812  0.0501  -0.0278 192 ASP C N   
10040 C CA  . ASP C 192 ? 0.3889 0.4450 1.9993 0.0866  0.0554  -0.0124 192 ASP C CA  
10041 C C   . ASP C 192 ? 0.4009 0.4359 2.0322 0.0839  0.0542  -0.0097 192 ASP C C   
10042 O O   . ASP C 192 ? 0.4095 0.4330 2.0497 0.0855  0.0531  -0.0208 192 ASP C O   
10043 C CB  . ASP C 192 ? 0.3876 0.4448 1.9809 0.0941  0.0591  -0.0153 192 ASP C CB  
10044 C CG  . ASP C 192 ? 0.3878 0.4314 1.9753 0.0994  0.0631  -0.0018 192 ASP C CG  
10045 O OD1 . ASP C 192 ? 0.3880 0.4255 1.9786 0.0985  0.0640  0.0117  192 ASP C OD1 
10046 O OD2 . ASP C 192 ? 0.4084 0.4497 1.9890 0.1043  0.0653  -0.0051 192 ASP C OD2 
10047 N N   . HIS C 193 ? 0.4097 0.4411 2.0491 0.0807  0.0551  0.0066  193 HIS C N   
10048 C CA  . HIS C 193 ? 0.4252 0.4388 2.0841 0.0782  0.0545  0.0154  193 HIS C CA  
10049 C C   . HIS C 193 ? 0.4238 0.4329 2.0705 0.0839  0.0594  0.0343  193 HIS C C   
10050 O O   . HIS C 193 ? 0.4358 0.4349 2.0953 0.0823  0.0595  0.0471  193 HIS C O   
10051 C CB  . HIS C 193 ? 0.4282 0.4435 2.1107 0.0683  0.0512  0.0195  193 HIS C CB  
10052 C CG  . HIS C 193 ? 0.4492 0.4680 2.1457 0.0620  0.0448  -0.0014 193 HIS C CG  
10053 N ND1 . HIS C 193 ? 0.4644 0.5004 2.1662 0.0549  0.0414  -0.0047 193 HIS C ND1 
10054 C CD2 . HIS C 193 ? 0.4798 0.4890 2.1859 0.0621  0.0409  -0.0214 193 HIS C CD2 
10055 C CE1 . HIS C 193 ? 0.4825 0.5194 2.1952 0.0504  0.0348  -0.0270 193 HIS C CE1 
10056 N NE2 . HIS C 193 ? 0.4984 0.5186 2.2141 0.0549  0.0348  -0.0381 193 HIS C NE2 
10057 N N   . ASN C 194 ? 0.4116 0.4290 2.0344 0.0904  0.0629  0.0363  194 ASN C N   
10058 C CA  . ASN C 194 ? 0.4027 0.4181 2.0122 0.0959  0.0668  0.0509  194 ASN C CA  
10059 C C   . ASN C 194 ? 0.4046 0.4237 2.0222 0.0924  0.0687  0.0672  194 ASN C C   
10060 O O   . ASN C 194 ? 0.3998 0.4116 2.0208 0.0935  0.0695  0.0791  194 ASN C O   
10061 C CB  . ASN C 194 ? 0.3976 0.3995 2.0057 0.1007  0.0661  0.0505  194 ASN C CB  
10062 C CG  . ASN C 194 ? 0.3959 0.3985 1.9868 0.1066  0.0687  0.0618  194 ASN C CG  
10063 O OD1 . ASN C 194 ? 0.4143 0.4255 1.9884 0.1099  0.0713  0.0620  194 ASN C OD1 
10064 N ND2 . ASN C 194 ? 0.3917 0.3859 1.9871 0.1082  0.0676  0.0712  194 ASN C ND2 
10065 N N   . GLU C 195 ? 0.4016 0.4351 2.0219 0.0886  0.0697  0.0687  195 GLU C N   
10066 C CA  . GLU C 195 ? 0.4033 0.4459 2.0320 0.0852  0.0728  0.0845  195 GLU C CA  
10067 C C   . GLU C 195 ? 0.4030 0.4654 2.0236 0.0866  0.0758  0.0858  195 GLU C C   
10068 O O   . GLU C 195 ? 0.4136 0.4834 2.0340 0.0852  0.0729  0.0747  195 GLU C O   
10069 C CB  . GLU C 195 ? 0.4024 0.4406 2.0606 0.0749  0.0690  0.0867  195 GLU C CB  
10070 C CG  . GLU C 195 ? 0.3895 0.4352 2.0594 0.0682  0.0641  0.0719  195 GLU C CG  
10071 C CD  . GLU C 195 ? 0.3882 0.4261 2.0900 0.0574  0.0585  0.0688  195 GLU C CD  
10072 O OE1 . GLU C 195 ? 0.3911 0.4165 2.1097 0.0545  0.0588  0.0811  195 GLU C OE1 
10073 O OE2 . GLU C 195 ? 0.3777 0.4230 2.0873 0.0521  0.0534  0.0537  195 GLU C OE2 
10074 N N   . GLY C 196 ? 0.4009 0.4740 2.0153 0.0900  0.0817  0.0995  196 GLY C N   
10075 C CA  . GLY C 196 ? 0.3998 0.4919 2.0088 0.0931  0.0852  0.1013  196 GLY C CA  
10076 C C   . GLY C 196 ? 0.3970 0.4883 1.9876 0.1006  0.0845  0.0905  196 GLY C C   
10077 O O   . GLY C 196 ? 0.3944 0.4750 1.9692 0.1071  0.0857  0.0884  196 GLY C O   
10078 N N   . GLN C 197 ? 0.3938 0.4971 1.9883 0.0989  0.0818  0.0844  197 GLN C N   
10079 C CA  . GLN C 197 ? 0.3864 0.4923 1.9661 0.1059  0.0815  0.0785  197 GLN C CA  
10080 C C   . GLN C 197 ? 0.3832 0.4729 1.9524 0.1077  0.0790  0.0694  197 GLN C C   
10081 O O   . GLN C 197 ? 0.3912 0.4780 1.9469 0.1145  0.0805  0.0683  197 GLN C O   
10082 C CB  . GLN C 197 ? 0.3924 0.5156 1.9784 0.1033  0.0776  0.0743  197 GLN C CB  
10083 C CG  . GLN C 197 ? 0.4104 0.5540 2.0069 0.1036  0.0801  0.0835  197 GLN C CG  
10084 C CD  . GLN C 197 ? 0.4266 0.5774 2.0448 0.0928  0.0778  0.0861  197 GLN C CD  
10085 O OE1 . GLN C 197 ? 0.4592 0.5991 2.0840 0.0888  0.0795  0.0904  197 GLN C OE1 
10086 N NE2 . GLN C 197 ? 0.4258 0.5957 2.0572 0.0875  0.0731  0.0842  197 GLN C NE2 
10087 N N   . THR C 198 ? 0.3701 0.4494 1.9477 0.1017  0.0753  0.0629  198 THR C N   
10088 C CA  . THR C 198 ? 0.3563 0.4237 1.9263 0.1037  0.0735  0.0538  198 THR C CA  
10089 C C   . THR C 198 ? 0.3499 0.4020 1.9147 0.1073  0.0755  0.0587  198 THR C C   
10090 O O   . THR C 198 ? 0.3628 0.4058 1.9222 0.1097  0.0744  0.0530  198 THR C O   
10091 C CB  . THR C 198 ? 0.3631 0.4287 1.9448 0.0973  0.0685  0.0413  198 THR C CB  
10092 O OG1 . THR C 198 ? 0.3808 0.4365 1.9796 0.0919  0.0672  0.0442  198 THR C OG1 
10093 C CG2 . THR C 198 ? 0.3629 0.4467 1.9477 0.0936  0.0650  0.0345  198 THR C CG2 
10094 N N   . ALA C 199 ? 0.3468 0.3986 1.9136 0.1077  0.0783  0.0697  199 ALA C N   
10095 C CA  . ALA C 199 ? 0.3479 0.3896 1.9062 0.1121  0.0796  0.0751  199 ALA C CA  
10096 C C   . ALA C 199 ? 0.3459 0.3916 1.8868 0.1199  0.0832  0.0773  199 ALA C C   
10097 O O   . ALA C 199 ? 0.3357 0.3732 1.8657 0.1245  0.0827  0.0758  199 ALA C O   
10098 C CB  . ALA C 199 ? 0.3524 0.3934 1.9219 0.1083  0.0804  0.0865  199 ALA C CB  
10099 N N   . THR C 200 ? 0.3583 0.4169 1.8983 0.1218  0.0864  0.0800  200 THR C N   
10100 C CA  . THR C 200 ? 0.3667 0.4281 1.8934 0.1301  0.0899  0.0806  200 THR C CA  
10101 C C   . THR C 200 ? 0.3480 0.4034 1.8688 0.1331  0.0877  0.0729  200 THR C C   
10102 O O   . THR C 200 ? 0.3474 0.3941 1.8584 0.1381  0.0876  0.0702  200 THR C O   
10103 C CB  . THR C 200 ? 0.3882 0.4665 1.9188 0.1322  0.0946  0.0867  200 THR C CB  
10104 O OG1 . THR C 200 ? 0.3906 0.4787 1.9335 0.1273  0.0925  0.0857  200 THR C OG1 
10105 C CG2 . THR C 200 ? 0.4023 0.4882 1.9365 0.1304  0.0984  0.0968  200 THR C CG2 
10106 N N   . MET C 201 ? 0.3400 0.4015 1.8673 0.1298  0.0856  0.0700  201 MET C N   
10107 C CA  . MET C 201 ? 0.3404 0.4008 1.8633 0.1325  0.0843  0.0664  201 MET C CA  
10108 C C   . MET C 201 ? 0.3317 0.3857 1.8554 0.1283  0.0810  0.0600  201 MET C C   
10109 O O   . MET C 201 ? 0.3376 0.3880 1.8569 0.1302  0.0804  0.0580  201 MET C O   
10110 C CB  . MET C 201 ? 0.3476 0.4240 1.8755 0.1328  0.0841  0.0689  201 MET C CB  
10111 C CG  . MET C 201 ? 0.3525 0.4371 1.8818 0.1388  0.0881  0.0751  201 MET C CG  
10112 S SD  . MET C 201 ? 0.3702 0.4781 1.9106 0.1377  0.0870  0.0798  201 MET C SD  
10113 C CE  . MET C 201 ? 0.3726 0.4896 1.9249 0.1290  0.0868  0.0811  201 MET C CE  
10114 N N   . GLY C 202 ? 0.3192 0.3723 1.8507 0.1225  0.0791  0.0569  202 GLY C N   
10115 C CA  . GLY C 202 ? 0.3099 0.3610 1.8443 0.1193  0.0765  0.0486  202 GLY C CA  
10116 C C   . GLY C 202 ? 0.3076 0.3742 1.8435 0.1168  0.0749  0.0442  202 GLY C C   
10117 O O   . GLY C 202 ? 0.3111 0.3894 1.8459 0.1182  0.0754  0.0492  202 GLY C O   
10118 N N   . PHE C 203 ? 0.3127 0.3810 1.8512 0.1139  0.0729  0.0345  203 PHE C N   
10119 C CA  . PHE C 203 ? 0.3197 0.4041 1.8607 0.1102  0.0701  0.0266  203 PHE C CA  
10120 C C   . PHE C 203 ? 0.3229 0.4224 1.8534 0.1136  0.0710  0.0314  203 PHE C C   
10121 O O   . PHE C 203 ? 0.3304 0.4430 1.8612 0.1136  0.0698  0.0367  203 PHE C O   
10122 C CB  . PHE C 203 ? 0.3245 0.4045 1.8717 0.1075  0.0684  0.0128  203 PHE C CB  
10123 C CG  . PHE C 203 ? 0.3302 0.4256 1.8818 0.1028  0.0643  0.0001  203 PHE C CG  
10124 C CD1 . PHE C 203 ? 0.3346 0.4365 1.8954 0.0976  0.0607  0.0003  203 PHE C CD1 
10125 C CD2 . PHE C 203 ? 0.3395 0.4450 1.8862 0.1035  0.0641  -0.0127 203 PHE C CD2 
10126 C CE1 . PHE C 203 ? 0.3475 0.4641 1.9129 0.0927  0.0556  -0.0133 203 PHE C CE1 
10127 C CE2 . PHE C 203 ? 0.3487 0.4703 1.8975 0.0996  0.0597  -0.0269 203 PHE C CE2 
10128 C CZ  . PHE C 203 ? 0.3536 0.4801 1.9120 0.0938  0.0548  -0.0278 203 PHE C CZ  
10129 N N   . LYS C 204 ? 0.3295 0.4280 1.8529 0.1166  0.0732  0.0318  204 LYS C N   
10130 C CA  . LYS C 204 ? 0.3396 0.4518 1.8552 0.1196  0.0743  0.0399  204 LYS C CA  
10131 C C   . LYS C 204 ? 0.3325 0.4450 1.8487 0.1230  0.0746  0.0520  204 LYS C C   
10132 O O   . LYS C 204 ? 0.3213 0.4511 1.8368 0.1238  0.0729  0.0575  204 LYS C O   
10133 C CB  . LYS C 204 ? 0.3488 0.4541 1.8610 0.1221  0.0774  0.0428  204 LYS C CB  
10134 C CG  . LYS C 204 ? 0.3644 0.4799 1.8722 0.1250  0.0790  0.0551  204 LYS C CG  
10135 C CD  . LYS C 204 ? 0.3738 0.4752 1.8836 0.1269  0.0815  0.0613  204 LYS C CD  
10136 C CE  . LYS C 204 ? 0.3801 0.4880 1.8904 0.1292  0.0828  0.0755  204 LYS C CE  
10137 N NZ  . LYS C 204 ? 0.3887 0.4756 1.9050 0.1311  0.0832  0.0805  204 LYS C NZ  
10138 N N   . ASP C 205 ? 0.3228 0.4176 1.8408 0.1258  0.0765  0.0559  205 ASP C N   
10139 C CA  . ASP C 205 ? 0.3177 0.4122 1.8366 0.1308  0.0778  0.0655  205 ASP C CA  
10140 C C   . ASP C 205 ? 0.3218 0.4307 1.8462 0.1294  0.0762  0.0667  205 ASP C C   
10141 O O   . ASP C 205 ? 0.3224 0.4451 1.8483 0.1323  0.0754  0.0738  205 ASP C O   
10142 C CB  . ASP C 205 ? 0.3138 0.3887 1.8316 0.1347  0.0801  0.0668  205 ASP C CB  
10143 C CG  . ASP C 205 ? 0.3057 0.3691 1.8213 0.1370  0.0807  0.0687  205 ASP C CG  
10144 O OD1 . ASP C 205 ? 0.2953 0.3652 1.8105 0.1349  0.0804  0.0698  205 ASP C OD1 
10145 O OD2 . ASP C 205 ? 0.2971 0.3464 1.8121 0.1404  0.0814  0.0686  205 ASP C OD2 
10146 N N   . TYR C 206 ? 0.3290 0.4356 1.8586 0.1247  0.0754  0.0610  206 TYR C N   
10147 C CA  . TYR C 206 ? 0.3283 0.4491 1.8665 0.1220  0.0738  0.0626  206 TYR C CA  
10148 C C   . TYR C 206 ? 0.3271 0.4701 1.8660 0.1197  0.0694  0.0614  206 TYR C C   
10149 O O   . TYR C 206 ? 0.3499 0.5081 1.8931 0.1221  0.0685  0.0686  206 TYR C O   
10150 C CB  . TYR C 206 ? 0.3397 0.4563 1.8871 0.1149  0.0724  0.0565  206 TYR C CB  
10151 C CG  . TYR C 206 ? 0.3529 0.4861 1.9129 0.1103  0.0701  0.0585  206 TYR C CG  
10152 C CD1 . TYR C 206 ? 0.3592 0.5043 1.9226 0.1149  0.0725  0.0685  206 TYR C CD1 
10153 C CD2 . TYR C 206 ? 0.3592 0.4964 1.9304 0.1014  0.0653  0.0498  206 TYR C CD2 
10154 C CE1 . TYR C 206 ? 0.3587 0.5215 1.9360 0.1104  0.0703  0.0712  206 TYR C CE1 
10155 C CE2 . TYR C 206 ? 0.3649 0.5180 1.9507 0.0958  0.0623  0.0516  206 TYR C CE2 
10156 C CZ  . TYR C 206 ? 0.3681 0.5351 1.9569 0.1002  0.0650  0.0631  206 TYR C CZ  
10157 O OH  . TYR C 206 ? 0.3756 0.5608 1.9806 0.0950  0.0624  0.0664  206 TYR C OH  
10158 N N   . ILE C 207 ? 0.3254 0.4730 1.8599 0.1158  0.0665  0.0521  207 ILE C N   
10159 C CA  . ILE C 207 ? 0.3384 0.5110 1.8709 0.1137  0.0618  0.0501  207 ILE C CA  
10160 C C   . ILE C 207 ? 0.3640 0.5472 1.8899 0.1205  0.0629  0.0635  207 ILE C C   
10161 O O   . ILE C 207 ? 0.3711 0.5764 1.8990 0.1212  0.0592  0.0694  207 ILE C O   
10162 C CB  . ILE C 207 ? 0.3389 0.5153 1.8670 0.1089  0.0592  0.0348  207 ILE C CB  
10163 C CG1 . ILE C 207 ? 0.3394 0.5055 1.8797 0.1020  0.0567  0.0223  207 ILE C CG1 
10164 C CG2 . ILE C 207 ? 0.3463 0.5519 1.8670 0.1079  0.0546  0.0320  207 ILE C CG2 
10165 C CD1 . ILE C 207 ? 0.3351 0.5114 1.8888 0.0971  0.0526  0.0238  207 ILE C CD1 
10166 N N   . LYS C 208 ? 0.3832 0.5509 1.9037 0.1251  0.0673  0.0692  208 LYS C N   
10167 C CA  . LYS C 208 ? 0.3964 0.5688 1.9148 0.1314  0.0687  0.0835  208 LYS C CA  
10168 C C   . LYS C 208 ? 0.3808 0.5533 1.9082 0.1371  0.0692  0.0934  208 LYS C C   
10169 O O   . LYS C 208 ? 0.3707 0.5600 1.9010 0.1410  0.0672  0.1044  208 LYS C O   
10170 C CB  . LYS C 208 ? 0.4154 0.5682 1.9305 0.1339  0.0728  0.0862  208 LYS C CB  
10171 C CG  . LYS C 208 ? 0.4485 0.6037 1.9657 0.1396  0.0739  0.1022  208 LYS C CG  
10172 C CD  . LYS C 208 ? 0.4712 0.6074 1.9893 0.1411  0.0771  0.1062  208 LYS C CD  
10173 C CE  . LYS C 208 ? 0.4739 0.5843 1.9975 0.1448  0.0790  0.1039  208 LYS C CE  
10174 N NZ  . LYS C 208 ? 0.4727 0.5681 2.0010 0.1466  0.0804  0.1102  208 LYS C NZ  
10175 N N   . GLY C 209 ? 0.3705 0.5257 1.9023 0.1384  0.0723  0.0901  209 GLY C N   
10176 C CA  . GLY C 209 ? 0.3732 0.5294 1.9137 0.1444  0.0743  0.0968  209 GLY C CA  
10177 C C   . GLY C 209 ? 0.3801 0.5632 1.9284 0.1433  0.0703  0.1011  209 GLY C C   
10178 O O   . GLY C 209 ? 0.3684 0.5613 1.9240 0.1504  0.0704  0.1117  209 GLY C O   
10179 N N   . LEU C 210 ? 0.3855 0.5805 1.9340 0.1345  0.0660  0.0923  210 LEU C N   
10180 C CA  . LEU C 210 ? 0.4030 0.6263 1.9585 0.1318  0.0602  0.0944  210 LEU C CA  
10181 C C   . LEU C 210 ? 0.4118 0.6528 1.9617 0.1359  0.0567  0.1040  210 LEU C C   
10182 O O   . LEU C 210 ? 0.4130 0.6724 1.9709 0.1407  0.0543  0.1150  210 LEU C O   
10183 C CB  . LEU C 210 ? 0.4095 0.6402 1.9671 0.1208  0.0552  0.0804  210 LEU C CB  
10184 C CG  . LEU C 210 ? 0.4085 0.6230 1.9749 0.1159  0.0581  0.0744  210 LEU C CG  
10185 C CD1 . LEU C 210 ? 0.4039 0.6273 1.9792 0.1047  0.0518  0.0619  210 LEU C CD1 
10186 C CD2 . LEU C 210 ? 0.4097 0.6262 1.9869 0.1212  0.0627  0.0850  210 LEU C CD2 
10187 N N   . ASN C 211 ? 0.4162 0.6537 1.9537 0.1345  0.0568  0.1016  211 ASN C N   
10188 C CA  . ASN C 211 ? 0.4172 0.6767 1.9491 0.1372  0.0534  0.1123  211 ASN C CA  
10189 C C   . ASN C 211 ? 0.4167 0.6717 1.9565 0.1473  0.0560  0.1310  211 ASN C C   
10190 O O   . ASN C 211 ? 0.4119 0.6899 1.9550 0.1510  0.0519  0.1442  211 ASN C O   
10191 C CB  . ASN C 211 ? 0.4137 0.6743 1.9313 0.1339  0.0541  0.1070  211 ASN C CB  
10192 C CG  . ASN C 211 ? 0.4320 0.7280 1.9415 0.1306  0.0473  0.1057  211 ASN C CG  
10193 O OD1 . ASN C 211 ? 0.4483 0.7600 1.9609 0.1254  0.0414  0.0951  211 ASN C OD1 
10194 N ND2 . ASN C 211 ? 0.4354 0.7460 1.9354 0.1334  0.0479  0.1171  211 ASN C ND2 
10195 N N   . GLU C 212 ? 0.4095 0.6354 1.9535 0.1518  0.0621  0.1316  212 GLU C N   
10196 C CA  . GLU C 212 ? 0.4083 0.6245 1.9626 0.1619  0.0648  0.1457  212 GLU C CA  
10197 C C   . GLU C 212 ? 0.4196 0.6495 1.9877 0.1674  0.0636  0.1508  212 GLU C C   
10198 O O   . GLU C 212 ? 0.4171 0.6557 1.9960 0.1757  0.0625  0.1655  212 GLU C O   
10199 C CB  . GLU C 212 ? 0.4011 0.5837 1.9546 0.1641  0.0706  0.1403  212 GLU C CB  
10200 C CG  . GLU C 212 ? 0.4103 0.5840 1.9566 0.1613  0.0713  0.1432  212 GLU C CG  
10201 C CD  . GLU C 212 ? 0.4077 0.5539 1.9496 0.1589  0.0750  0.1335  212 GLU C CD  
10202 O OE1 . GLU C 212 ? 0.4074 0.5376 1.9490 0.1591  0.0773  0.1227  212 GLU C OE1 
10203 O OE2 . GLU C 212 ? 0.4062 0.5496 1.9451 0.1564  0.0756  0.1379  212 GLU C OE2 
10204 N N   . LEU C 213 ? 0.4215 0.6554 1.9919 0.1629  0.0638  0.1400  213 LEU C N   
10205 C CA  . LEU C 213 ? 0.4279 0.6802 2.0131 0.1671  0.0627  0.1453  213 LEU C CA  
10206 C C   . LEU C 213 ? 0.4364 0.7229 2.0245 0.1651  0.0544  0.1535  213 LEU C C   
10207 O O   . LEU C 213 ? 0.4563 0.7588 2.0579 0.1728  0.0527  0.1658  213 LEU C O   
10208 C CB  . LEU C 213 ? 0.4271 0.6774 2.0162 0.1616  0.0653  0.1341  213 LEU C CB  
10209 C CG  . LEU C 213 ? 0.4304 0.6525 2.0166 0.1649  0.0734  0.1278  213 LEU C CG  
10210 C CD1 . LEU C 213 ? 0.4285 0.6522 2.0179 0.1577  0.0754  0.1196  213 LEU C CD1 
10211 C CD2 . LEU C 213 ? 0.4326 0.6482 2.0282 0.1782  0.0787  0.1352  213 LEU C CD2 
10212 N N   . ASN C 214 ? 0.4462 0.7449 2.0216 0.1556  0.0489  0.1462  214 ASN C N   
10213 C CA  . ASN C 214 ? 0.4464 0.7810 2.0212 0.1524  0.0398  0.1505  214 ASN C CA  
10214 C C   . ASN C 214 ? 0.4564 0.8037 2.0308 0.1608  0.0378  0.1706  214 ASN C C   
10215 O O   . ASN C 214 ? 0.4816 0.8616 2.0592 0.1616  0.0302  0.1798  214 ASN C O   
10216 C CB  . ASN C 214 ? 0.4420 0.7857 2.0023 0.1409  0.0350  0.1340  214 ASN C CB  
10217 C CG  . ASN C 214 ? 0.4377 0.7772 2.0051 0.1319  0.0339  0.1172  214 ASN C CG  
10218 O OD1 . ASN C 214 ? 0.4302 0.7763 2.0139 0.1326  0.0337  0.1204  214 ASN C OD1 
10219 N ND2 . ASN C 214 ? 0.4425 0.7716 2.0001 0.1236  0.0336  0.1002  214 ASN C ND2 
10220 N N   . GLY C 215 ? 0.4421 0.7648 2.0136 0.1664  0.0438  0.1783  215 GLY C N   
10221 C CA  . GLY C 215 ? 0.4568 0.7865 2.0344 0.1752  0.0428  0.2005  215 GLY C CA  
10222 C C   . GLY C 215 ? 0.4741 0.8176 2.0360 0.1715  0.0404  0.2082  215 GLY C C   
10223 O O   . GLY C 215 ? 0.5056 0.8686 2.0716 0.1769  0.0369  0.2292  215 GLY C O   
10224 N N   . LEU C 216 ? 0.4583 0.7943 2.0035 0.1629  0.0425  0.1924  216 LEU C N   
10225 C CA  . LEU C 216 ? 0.4544 0.7946 1.9859 0.1605  0.0442  0.1983  216 LEU C CA  
10226 C C   . LEU C 216 ? 0.4661 0.8460 1.9916 0.1620  0.0382  0.2165  216 LEU C C   
10227 O O   . LEU C 216 ? 0.4742 0.8579 1.9951 0.1634  0.0407  0.2319  216 LEU C O   
10228 C CB  . LEU C 216 ? 0.4463 0.7530 1.9865 0.1653  0.0513  0.2080  216 LEU C CB  
10229 C CG  . LEU C 216 ? 0.4351 0.7045 1.9771 0.1634  0.0572  0.1899  216 LEU C CG  
10230 C CD1 . LEU C 216 ? 0.4425 0.6843 1.9903 0.1659  0.0625  0.1981  216 LEU C CD1 
10231 C CD2 . LEU C 216 ? 0.4180 0.6875 1.9455 0.1542  0.0575  0.1672  216 LEU C CD2 
10232 N N   . ASP C 217 ? 0.4647 0.8765 1.9902 0.1611  0.0299  0.2152  217 ASP C N   
10233 C CA  . ASP C 217 ? 0.4757 0.9269 1.9992 0.1648  0.0229  0.2365  217 ASP C CA  
10234 C C   . ASP C 217 ? 0.4802 0.9713 1.9831 0.1571  0.0152  0.2234  217 ASP C C   
10235 O O   . ASP C 217 ? 0.4873 1.0179 1.9864 0.1592  0.0072  0.2374  217 ASP C O   
10236 C CB  . ASP C 217 ? 0.4763 0.9347 2.0217 0.1732  0.0185  0.2520  217 ASP C CB  
10237 C CG  . ASP C 217 ? 0.4705 0.9237 2.0267 0.1710  0.0165  0.2339  217 ASP C CG  
10238 O OD1 . ASP C 217 ? 0.4640 0.8964 2.0139 0.1637  0.0204  0.2106  217 ASP C OD1 
10239 O OD2 . ASP C 217 ? 0.4952 0.9665 2.0677 0.1766  0.0113  0.2447  217 ASP C OD2 
10240 N N   . LYS C 218 ? 0.4714 0.9528 1.9619 0.1487  0.0172  0.1959  218 LYS C N   
10241 C CA  . LYS C 218 ? 0.4766 0.9917 1.9481 0.1414  0.0105  0.1780  218 LYS C CA  
10242 C C   . LYS C 218 ? 0.4672 0.9611 1.9268 0.1352  0.0170  0.1539  218 LYS C C   
10243 O O   . LYS C 218 ? 0.4484 0.9024 1.9177 0.1351  0.0242  0.1477  218 LYS C O   
10244 C CB  . LYS C 218 ? 0.4742 1.0057 1.9530 0.1362  0.0006  0.1616  218 LYS C CB  
10245 C CG  . LYS C 218 ? 0.4686 1.0161 1.9656 0.1419  -0.0058 0.1808  218 LYS C CG  
10246 C CD  . LYS C 218 ? 0.4646 1.0259 1.9733 0.1356  -0.0148 0.1644  218 LYS C CD  
10247 C CE  . LYS C 218 ? 0.4683 1.0546 1.9935 0.1428  -0.0214 0.1876  218 LYS C CE  
10248 N NZ  . LYS C 218 ? 0.4580 1.0464 2.0038 0.1389  -0.0263 0.1774  218 LYS C NZ  
10249 N N   . PRO C 219 ? 0.4801 1.0017 1.9190 0.1306  0.0144  0.1389  219 PRO C N   
10250 C CA  . PRO C 219 ? 0.4775 0.9815 1.9073 0.1255  0.0199  0.1134  219 PRO C CA  
10251 C C   . PRO C 219 ? 0.4702 0.9401 1.9153 0.1206  0.0198  0.0922  219 PRO C C   
10252 O O   . PRO C 219 ? 0.4769 0.9506 1.9345 0.1184  0.0128  0.0895  219 PRO C O   
10253 C CB  . PRO C 219 ? 0.4927 1.0399 1.9013 0.1219  0.0135  0.0970  219 PRO C CB  
10254 C CG  . PRO C 219 ? 0.5078 1.0956 1.9083 0.1269  0.0087  0.1243  219 PRO C CG  
10255 C CD  . PRO C 219 ? 0.4964 1.0697 1.9197 0.1309  0.0058  0.1454  219 PRO C CD  
10256 N N   . PHE C 220 ? 0.4741 0.9120 1.9197 0.1191  0.0277  0.0798  220 PHE C N   
10257 C CA  . PHE C 220 ? 0.4805 0.8882 1.9388 0.1140  0.0279  0.0596  220 PHE C CA  
10258 C C   . PHE C 220 ? 0.4887 0.8953 1.9377 0.1095  0.0291  0.0329  220 PHE C C   
10259 O O   . PHE C 220 ? 0.4882 0.8962 1.9255 0.1122  0.0357  0.0336  220 PHE C O   
10260 C CB  . PHE C 220 ? 0.4733 0.8404 1.9449 0.1174  0.0358  0.0703  220 PHE C CB  
10261 C CG  . PHE C 220 ? 0.4648 0.8003 1.9461 0.1127  0.0380  0.0514  220 PHE C CG  
10262 C CD1 . PHE C 220 ? 0.4670 0.8019 1.9605 0.1068  0.0320  0.0390  220 PHE C CD1 
10263 C CD2 . PHE C 220 ? 0.4555 0.7628 1.9362 0.1139  0.0458  0.0485  220 PHE C CD2 
10264 C CE1 . PHE C 220 ? 0.4529 0.7596 1.9573 0.1024  0.0341  0.0255  220 PHE C CE1 
10265 C CE2 . PHE C 220 ? 0.4540 0.7342 1.9443 0.1102  0.0472  0.0342  220 PHE C CE2 
10266 C CZ  . PHE C 220 ? 0.4499 0.7296 1.9520 0.1046  0.0416  0.0236  220 PHE C CZ  
10267 N N   . ILE C 221 ? 0.4953 0.9004 1.9521 0.1026  0.0225  0.0098  221 ILE C N   
10268 C CA  . ILE C 221 ? 0.5122 0.9154 1.9646 0.0985  0.0220  -0.0189 221 ILE C CA  
10269 C C   . ILE C 221 ? 0.5213 0.8920 1.9950 0.0925  0.0203  -0.0334 221 ILE C C   
10270 O O   . ILE C 221 ? 0.5344 0.9018 2.0229 0.0892  0.0156  -0.0266 221 ILE C O   
10271 C CB  . ILE C 221 ? 0.5244 0.9695 1.9633 0.0954  0.0128  -0.0359 221 ILE C CB  
10272 C CG1 . ILE C 221 ? 0.5256 0.9816 1.9783 0.0883  0.0006  -0.0441 221 ILE C CG1 
10273 C CG2 . ILE C 221 ? 0.5330 1.0149 1.9506 0.1014  0.0141  -0.0168 221 ILE C CG2 
10274 C CD1 . ILE C 221 ? 0.5482 1.0450 1.9887 0.0842  -0.0103 -0.0653 221 ILE C CD1 
10275 N N   . THR C 222 ? 0.5204 0.8698 1.9967 0.0915  0.0245  -0.0516 222 THR C N   
10276 C CA  . THR C 222 ? 0.5184 0.8387 2.0155 0.0856  0.0226  -0.0665 222 THR C CA  
10277 C C   . THR C 222 ? 0.5417 0.8778 2.0423 0.0790  0.0132  -0.0957 222 THR C C   
10278 O O   . THR C 222 ? 0.5645 0.9189 2.0503 0.0812  0.0134  -0.1126 222 THR C O   
10279 C CB  . THR C 222 ? 0.5194 0.8081 2.0195 0.0891  0.0316  -0.0687 222 THR C CB  
10280 O OG1 . THR C 222 ? 0.5183 0.8226 2.0034 0.0927  0.0345  -0.0830 222 THR C OG1 
10281 C CG2 . THR C 222 ? 0.5193 0.7918 2.0168 0.0950  0.0396  -0.0428 222 THR C CG2 
10282 N N   . THR C 223 ? 0.5338 0.8633 2.0553 0.0707  0.0054  -0.1020 223 THR C N   
10283 C CA  . THR C 223 ? 0.5468 0.8890 2.0770 0.0627  -0.0054 -0.1304 223 THR C CA  
10284 C C   . THR C 223 ? 0.5370 0.8455 2.0884 0.0585  -0.0050 -0.1509 223 THR C C   
10285 O O   . THR C 223 ? 0.5482 0.8632 2.1059 0.0536  -0.0126 -0.1795 223 THR C O   
10286 C CB  . THR C 223 ? 0.5564 0.9144 2.1007 0.0551  -0.0153 -0.1240 223 THR C CB  
10287 O OG1 . THR C 223 ? 0.5308 0.8620 2.0920 0.0549  -0.0096 -0.1020 223 THR C OG1 
10288 C CG2 . THR C 223 ? 0.5676 0.9677 2.0922 0.0585  -0.0198 -0.1122 223 THR C CG2 
10289 N N   . GLU C 224 ? 0.5121 0.7855 2.0758 0.0603  0.0029  -0.1362 224 GLU C N   
10290 C CA  . GLU C 224 ? 0.5036 0.7431 2.0873 0.0584  0.0048  -0.1497 224 GLU C CA  
10291 C C   . GLU C 224 ? 0.4635 0.6772 2.0436 0.0659  0.0163  -0.1301 224 GLU C C   
10292 O O   . GLU C 224 ? 0.4450 0.6594 2.0170 0.0693  0.0211  -0.1052 224 GLU C O   
10293 C CB  . GLU C 224 ? 0.5084 0.7299 2.1246 0.0476  -0.0020 -0.1519 224 GLU C CB  
10294 C CG  . GLU C 224 ? 0.5331 0.7720 2.1629 0.0375  -0.0151 -0.1761 224 GLU C CG  
10295 C CD  . GLU C 224 ? 0.5375 0.7627 2.2027 0.0251  -0.0224 -0.1743 224 GLU C CD  
10296 O OE1 . GLU C 224 ? 0.5277 0.7236 2.2124 0.0234  -0.0173 -0.1584 224 GLU C OE1 
10297 O OE2 . GLU C 224 ? 0.5376 0.7845 2.2120 0.0163  -0.0340 -0.1883 224 GLU C OE2 
10298 N N   . PHE C 225 ? 0.4547 0.6462 2.0422 0.0689  0.0201  -0.1425 225 PHE C N   
10299 C CA  . PHE C 225 ? 0.4290 0.5907 2.0230 0.0733  0.0280  -0.1271 225 PHE C CA  
10300 C C   . PHE C 225 ? 0.4379 0.5796 2.0467 0.0750  0.0285  -0.1478 225 PHE C C   
10301 O O   . PHE C 225 ? 0.4557 0.6119 2.0582 0.0772  0.0269  -0.1716 225 PHE C O   
10302 C CB  . PHE C 225 ? 0.4032 0.5701 1.9748 0.0820  0.0369  -0.1079 225 PHE C CB  
10303 C CG  . PHE C 225 ? 0.4016 0.5899 1.9529 0.0884  0.0405  -0.1190 225 PHE C CG  
10304 C CD1 . PHE C 225 ? 0.4036 0.6264 1.9366 0.0884  0.0376  -0.1216 225 PHE C CD1 
10305 C CD2 . PHE C 225 ? 0.4010 0.5777 1.9525 0.0945  0.0468  -0.1257 225 PHE C CD2 
10306 C CE1 . PHE C 225 ? 0.4138 0.6599 1.9278 0.0941  0.0416  -0.1303 225 PHE C CE1 
10307 C CE2 . PHE C 225 ? 0.4084 0.6084 1.9424 0.1003  0.0512  -0.1350 225 PHE C CE2 
10308 C CZ  . PHE C 225 ? 0.4145 0.6495 1.9291 0.1000  0.0490  -0.1371 225 PHE C CZ  
10309 N N   . GLY C 226 ? 0.4328 0.5434 2.0618 0.0746  0.0306  -0.1393 226 GLY C N   
10310 C CA  . GLY C 226 ? 0.4482 0.5388 2.0946 0.0773  0.0309  -0.1575 226 GLY C CA  
10311 C C   . GLY C 226 ? 0.4503 0.5080 2.1258 0.0737  0.0297  -0.1470 226 GLY C C   
10312 O O   . GLY C 226 ? 0.4271 0.4785 2.1072 0.0693  0.0298  -0.1245 226 GLY C O   
10313 N N   . TYR C 227 ? 0.4758 0.5141 2.1717 0.0764  0.0289  -0.1634 227 TYR C N   
10314 C CA  . TYR C 227 ? 0.4775 0.4845 2.2017 0.0749  0.0284  -0.1516 227 TYR C CA  
10315 C C   . TYR C 227 ? 0.4956 0.4858 2.2524 0.0712  0.0216  -0.1764 227 TYR C C   
10316 O O   . TYR C 227 ? 0.5041 0.5063 2.2574 0.0731  0.0191  -0.2056 227 TYR C O   
10317 C CB  . TYR C 227 ? 0.4775 0.4742 2.1946 0.0851  0.0360  -0.1387 227 TYR C CB  
10318 C CG  . TYR C 227 ? 0.4678 0.4756 2.1582 0.0877  0.0417  -0.1132 227 TYR C CG  
10319 C CD1 . TYR C 227 ? 0.4752 0.4735 2.1696 0.0838  0.0420  -0.0878 227 TYR C CD1 
10320 C CD2 . TYR C 227 ? 0.4654 0.4941 2.1279 0.0939  0.0469  -0.1146 227 TYR C CD2 
10321 C CE1 . TYR C 227 ? 0.4617 0.4692 2.1330 0.0867  0.0469  -0.0676 227 TYR C CE1 
10322 C CE2 . TYR C 227 ? 0.4580 0.4940 2.0999 0.0960  0.0514  -0.0925 227 TYR C CE2 
10323 C CZ  . TYR C 227 ? 0.4554 0.4801 2.1016 0.0927  0.0511  -0.0705 227 TYR C CZ  
10324 O OH  . TYR C 227 ? 0.4411 0.4719 2.0682 0.0954  0.0552  -0.0517 227 TYR C OH  
10325 N N   . SER C 228 ? 0.5034 0.4664 2.2914 0.0664  0.0189  -0.1634 228 SER C N   
10326 C CA  . SER C 228 ? 0.5307 0.4718 2.3583 0.0604  0.0112  -0.1807 228 SER C CA  
10327 C C   . SER C 228 ? 0.5356 0.4469 2.3886 0.0673  0.0132  -0.1759 228 SER C C   
10328 O O   . SER C 228 ? 0.5208 0.4236 2.3712 0.0705  0.0179  -0.1471 228 SER C O   
10329 C CB  . SER C 228 ? 0.5316 0.4685 2.3800 0.0463  0.0051  -0.1665 228 SER C CB  
10330 O OG  . SER C 228 ? 0.5555 0.4643 2.4487 0.0398  -0.0016 -0.1728 228 SER C OG  
10331 N N   . VAL C 229 ? 0.5582 0.4540 2.4380 0.0696  0.0088  -0.2043 229 VAL C N   
10332 C CA  . VAL C 229 ? 0.5674 0.4365 2.4735 0.0783  0.0105  -0.2037 229 VAL C CA  
10333 C C   . VAL C 229 ? 0.5981 0.4359 2.5546 0.0703  0.0019  -0.2080 229 VAL C C   
10334 O O   . VAL C 229 ? 0.6175 0.4348 2.6030 0.0764  -0.0003 -0.2281 229 VAL C O   
10335 C CB  . VAL C 229 ? 0.5695 0.4477 2.4641 0.0917  0.0149  -0.2327 229 VAL C CB  
10336 C CG1 . VAL C 229 ? 0.5436 0.4505 2.3932 0.0989  0.0238  -0.2213 229 VAL C CG1 
10337 C CG2 . VAL C 229 ? 0.5906 0.4772 2.4909 0.0899  0.0094  -0.2748 229 VAL C CG2 
10338 N N   . SER C 230 ? 0.5975 0.4319 2.5667 0.0567  -0.0025 -0.1876 230 SER C N   
10339 C CA  . SER C 230 ? 0.6221 0.4269 2.6420 0.0472  -0.0102 -0.1840 230 SER C CA  
10340 C C   . SER C 230 ? 0.6258 0.4034 2.6704 0.0548  -0.0075 -0.1610 230 SER C C   
10341 O O   . SER C 230 ? 0.6086 0.3935 2.6304 0.0611  -0.0006 -0.1329 230 SER C O   
10342 C CB  . SER C 230 ? 0.6166 0.4287 2.6424 0.0316  -0.0136 -0.1617 230 SER C CB  
10343 O OG  . SER C 230 ? 0.5917 0.4114 2.5982 0.0330  -0.0063 -0.1218 230 SER C OG  
10344 N N   . PRO C 231 ? 0.6544 0.4001 2.7476 0.0548  -0.0135 -0.1717 231 PRO C N   
10345 C CA  . PRO C 231 ? 0.6609 0.3813 2.7821 0.0606  -0.0122 -0.1436 231 PRO C CA  
10346 C C   . PRO C 231 ? 0.6427 0.3697 2.7540 0.0546  -0.0087 -0.0962 231 PRO C C   
10347 O O   . PRO C 231 ? 0.6361 0.3588 2.7438 0.0630  -0.0044 -0.0699 231 PRO C O   
10348 C CB  . PRO C 231 ? 0.6962 0.3818 2.8775 0.0548  -0.0217 -0.1596 231 PRO C CB  
10349 C CG  . PRO C 231 ? 0.7100 0.4035 2.8863 0.0552  -0.0257 -0.2103 231 PRO C CG  
10350 C CD  . PRO C 231 ? 0.6848 0.4173 2.8090 0.0501  -0.0223 -0.2117 231 PRO C CD  
10351 N N   . GLU C 232 ? 0.6380 0.3785 2.7436 0.0404  -0.0104 -0.0856 232 GLU C N   
10352 C CA  . GLU C 232 ? 0.6261 0.3747 2.7252 0.0344  -0.0066 -0.0424 232 GLU C CA  
10353 C C   . GLU C 232 ? 0.6206 0.3915 2.7073 0.0208  -0.0075 -0.0405 232 GLU C C   
10354 O O   . GLU C 232 ? 0.6205 0.4033 2.6970 0.0174  -0.0110 -0.0715 232 GLU C O   
10355 C CB  . GLU C 232 ? 0.6505 0.3704 2.7995 0.0302  -0.0103 -0.0155 232 GLU C CB  
10356 C CG  . GLU C 232 ? 0.6776 0.3758 2.8789 0.0160  -0.0197 -0.0280 232 GLU C CG  
10357 C CD  . GLU C 232 ? 0.6924 0.3653 2.9440 0.0093  -0.0229 0.0063  232 GLU C CD  
10358 O OE1 . GLU C 232 ? 0.6843 0.3684 2.9388 -0.0014 -0.0207 0.0409  232 GLU C OE1 
10359 O OE2 . GLU C 232 ? 0.7134 0.3563 3.0019 0.0156  -0.0270 -0.0003 232 GLU C OE2 
10360 N N   . GLY C 233 ? 0.6218 0.4009 2.7089 0.0136  -0.0043 -0.0033 233 GLY C N   
10361 C CA  . GLY C 233 ? 0.6239 0.4257 2.7033 0.0011  -0.0044 0.0030  233 GLY C CA  
10362 C C   . GLY C 233 ? 0.6043 0.4378 2.6291 0.0074  0.0017  -0.0036 233 GLY C C   
10363 O O   . GLY C 233 ? 0.5962 0.4332 2.5942 0.0188  0.0036  -0.0249 233 GLY C O   
10364 N N   . GLY C 234 ? 0.6075 0.4644 2.6192 0.0001  0.0050  0.0156  234 GLY C N   
10365 C CA  . GLY C 234 ? 0.5916 0.4777 2.5549 0.0063  0.0116  0.0166  234 GLY C CA  
10366 C C   . GLY C 234 ? 0.5882 0.4824 2.5295 0.0130  0.0205  0.0504  234 GLY C C   
10367 O O   . GLY C 234 ? 0.6081 0.4935 2.5725 0.0089  0.0217  0.0776  234 GLY C O   
10368 N N   . ASN C 235 ? 0.5784 0.4899 2.4760 0.0233  0.0265  0.0486  235 ASN C N   
10369 C CA  . ASN C 235 ? 0.5709 0.4905 2.4438 0.0309  0.0343  0.0750  235 ASN C CA  
10370 C C   . ASN C 235 ? 0.5224 0.4483 2.3566 0.0438  0.0377  0.0623  235 ASN C C   
10371 O O   . ASN C 235 ? 0.4972 0.4329 2.3152 0.0452  0.0367  0.0399  235 ASN C O   
10372 C CB  . ASN C 235 ? 0.5918 0.5347 2.4564 0.0254  0.0393  0.0964  235 ASN C CB  
10373 C CG  . ASN C 235 ? 0.6148 0.5675 2.4528 0.0340  0.0471  0.1205  235 ASN C CG  
10374 O OD1 . ASN C 235 ? 0.6428 0.5826 2.4883 0.0378  0.0475  0.1358  235 ASN C OD1 
10375 N ND2 . ASN C 235 ? 0.6223 0.5978 2.4297 0.0379  0.0528  0.1232  235 ASN C ND2 
10376 N N   . GLY C 236 ? 0.5047 0.4259 2.3259 0.0526  0.0413  0.0775  236 GLY C N   
10377 C CA  . GLY C 236 ? 0.4818 0.4053 2.2737 0.0640  0.0436  0.0666  236 GLY C CA  
10378 C C   . GLY C 236 ? 0.4795 0.3990 2.2726 0.0659  0.0403  0.0351  236 GLY C C   
10379 O O   . GLY C 236 ? 0.5055 0.4076 2.3256 0.0649  0.0357  0.0226  236 GLY C O   
10380 N N   . GLN C 237 ? 0.4692 0.4064 2.2339 0.0685  0.0426  0.0224  237 GLN C N   
10381 C CA  . GLN C 237 ? 0.4696 0.4095 2.2271 0.0722  0.0411  -0.0051 237 GLN C CA  
10382 C C   . GLN C 237 ? 0.4892 0.4335 2.2615 0.0637  0.0357  -0.0250 237 GLN C C   
10383 O O   . GLN C 237 ? 0.4886 0.4364 2.2578 0.0661  0.0337  -0.0502 237 GLN C O   
10384 C CB  . GLN C 237 ? 0.4497 0.4078 2.1706 0.0788  0.0461  -0.0046 237 GLN C CB  
10385 C CG  . GLN C 237 ? 0.4406 0.3934 2.1488 0.0873  0.0498  0.0088  237 GLN C CG  
10386 C CD  . GLN C 237 ? 0.4172 0.3845 2.0951 0.0937  0.0538  0.0047  237 GLN C CD  
10387 O OE1 . GLN C 237 ? 0.4150 0.3886 2.0868 0.0962  0.0539  -0.0135 237 GLN C OE1 
10388 N NE2 . GLN C 237 ? 0.4057 0.3789 2.0653 0.0961  0.0570  0.0215  237 GLN C NE2 
10389 N N   . TYR C 238 ? 0.5019 0.4489 2.2899 0.0537  0.0334  -0.0137 238 TYR C N   
10390 C CA  . TYR C 238 ? 0.5126 0.4631 2.3203 0.0438  0.0267  -0.0312 238 TYR C CA  
10391 C C   . TYR C 238 ? 0.5216 0.4458 2.3687 0.0400  0.0210  -0.0397 238 TYR C C   
10392 O O   . TYR C 238 ? 0.5259 0.4361 2.3992 0.0345  0.0202  -0.0197 238 TYR C O   
10393 C CB  . TYR C 238 ? 0.5189 0.4864 2.3280 0.0349  0.0269  -0.0149 238 TYR C CB  
10394 C CG  . TYR C 238 ? 0.5381 0.5090 2.3735 0.0228  0.0184  -0.0312 238 TYR C CG  
10395 C CD1 . TYR C 238 ? 0.5434 0.5323 2.3654 0.0221  0.0140  -0.0558 238 TYR C CD1 
10396 C CD2 . TYR C 238 ? 0.5547 0.5109 2.4299 0.0119  0.0140  -0.0227 238 TYR C CD2 
10397 C CE1 . TYR C 238 ? 0.5613 0.5545 2.4071 0.0108  0.0047  -0.0735 238 TYR C CE1 
10398 C CE2 . TYR C 238 ? 0.5740 0.5323 2.4763 -0.0001 0.0050  -0.0396 238 TYR C CE2 
10399 C CZ  . TYR C 238 ? 0.5765 0.5536 2.4634 -0.0006 -0.0001 -0.0663 238 TYR C CZ  
10400 O OH  . TYR C 238 ? 0.6025 0.5833 2.5155 -0.0127 -0.0103 -0.0852 238 TYR C OH  
10401 N N   . GLY C 239 ? 0.5283 0.4462 2.3797 0.0438  0.0176  -0.0691 239 GLY C N   
10402 C CA  . GLY C 239 ? 0.5472 0.4381 2.4366 0.0427  0.0124  -0.0812 239 GLY C CA  
10403 C C   . GLY C 239 ? 0.5403 0.4131 2.4333 0.0534  0.0166  -0.0684 239 GLY C C   
10404 O O   . GLY C 239 ? 0.5221 0.4046 2.3871 0.0607  0.0230  -0.0510 239 GLY C O   
10405 N N   . SER C 240 ? 0.5550 0.4021 2.4842 0.0545  0.0122  -0.0789 240 SER C N   
10406 C CA  . SER C 240 ? 0.5596 0.3876 2.5018 0.0641  0.0144  -0.0662 240 SER C CA  
10407 C C   . SER C 240 ? 0.5465 0.3871 2.4550 0.0779  0.0209  -0.0707 240 SER C C   
10408 O O   . SER C 240 ? 0.5303 0.3659 2.4354 0.0847  0.0240  -0.0491 240 SER C O   
10409 C CB  . SER C 240 ? 0.5506 0.3715 2.5040 0.0600  0.0155  -0.0270 240 SER C CB  
10410 O OG  . SER C 240 ? 0.5573 0.3716 2.5399 0.0461  0.0108  -0.0185 240 SER C OG  
10411 N N   . ASN C 241 ? 0.5487 0.4067 2.4336 0.0818  0.0226  -0.0979 241 ASN C N   
10412 C CA  . ASN C 241 ? 0.5401 0.4109 2.3978 0.0939  0.0289  -0.1031 241 ASN C CA  
10413 C C   . ASN C 241 ? 0.5612 0.4195 2.4402 0.1034  0.0284  -0.1276 241 ASN C C   
10414 O O   . ASN C 241 ? 0.5927 0.4361 2.5017 0.1003  0.0229  -0.1483 241 ASN C O   
10415 C CB  . ASN C 241 ? 0.5348 0.4348 2.3546 0.0936  0.0323  -0.1149 241 ASN C CB  
10416 C CG  . ASN C 241 ? 0.5223 0.4359 2.3182 0.0882  0.0345  -0.0894 241 ASN C CG  
10417 O OD1 . ASN C 241 ? 0.5072 0.4262 2.2830 0.0936  0.0394  -0.0711 241 ASN C OD1 
10418 N ND2 . ASN C 241 ? 0.5331 0.4532 2.3318 0.0778  0.0308  -0.0892 241 ASN C ND2 
10419 N N   . THR C 242 ? 0.5386 0.4033 2.4044 0.1150  0.0340  -0.1260 242 THR C N   
10420 C CA  . THR C 242 ? 0.5418 0.4011 2.4241 0.1257  0.0352  -0.1516 242 THR C CA  
10421 C C   . THR C 242 ? 0.5267 0.4130 2.3817 0.1283  0.0392  -0.1798 242 THR C C   
10422 O O   . THR C 242 ? 0.5055 0.4135 2.3287 0.1227  0.0409  -0.1742 242 THR C O   
10423 C CB  . THR C 242 ? 0.5379 0.3929 2.4242 0.1368  0.0389  -0.1355 242 THR C CB  
10424 O OG1 . THR C 242 ? 0.5281 0.4041 2.3770 0.1362  0.0435  -0.1166 242 THR C OG1 
10425 C CG2 . THR C 242 ? 0.5463 0.3746 2.4652 0.1359  0.0340  -0.1108 242 THR C CG2 
10426 N N   . LEU C 243 ? 0.5305 0.4166 2.3994 0.1373  0.0406  -0.2095 243 LEU C N   
10427 C CA  . LEU C 243 ? 0.5305 0.4447 2.3752 0.1409  0.0448  -0.2382 243 LEU C CA  
10428 C C   . LEU C 243 ? 0.5047 0.4460 2.3128 0.1458  0.0532  -0.2232 243 LEU C C   
10429 O O   . LEU C 243 ? 0.5011 0.4708 2.2790 0.1443  0.0564  -0.2324 243 LEU C O   
10430 C CB  . LEU C 243 ? 0.5569 0.4671 2.4240 0.1518  0.0462  -0.2724 243 LEU C CB  
10431 C CG  . LEU C 243 ? 0.5904 0.4782 2.4926 0.1480  0.0378  -0.2998 243 LEU C CG  
10432 C CD1 . LEU C 243 ? 0.5924 0.4919 2.4807 0.1347  0.0315  -0.3114 243 LEU C CD1 
10433 C CD2 . LEU C 243 ? 0.6001 0.4484 2.5462 0.1460  0.0317  -0.2821 243 LEU C CD2 
10434 N N   . LYS C 244 ? 0.4846 0.4170 2.2985 0.1515  0.0560  -0.2000 244 LYS C N   
10435 C CA  . LYS C 244 ? 0.4549 0.4075 2.2409 0.1549  0.0626  -0.1820 244 LYS C CA  
10436 C C   . LYS C 244 ? 0.4359 0.3983 2.1935 0.1449  0.0616  -0.1614 244 LYS C C   
10437 O O   . LYS C 244 ? 0.4233 0.4105 2.1519 0.1449  0.0664  -0.1603 244 LYS C O   
10438 C CB  . LYS C 244 ? 0.4425 0.3811 2.2447 0.1616  0.0631  -0.1611 244 LYS C CB  
10439 C CG  . LYS C 244 ? 0.4163 0.3757 2.1933 0.1648  0.0690  -0.1450 244 LYS C CG  
10440 C CD  . LYS C 244 ? 0.4063 0.3564 2.1969 0.1707  0.0683  -0.1244 244 LYS C CD  
10441 C CE  . LYS C 244 ? 0.3821 0.3493 2.1481 0.1703  0.0716  -0.1052 244 LYS C CE  
10442 N NZ  . LYS C 244 ? 0.3740 0.3695 2.1172 0.1715  0.0790  -0.1160 244 LYS C NZ  
10443 N N   . GLN C 245 ? 0.4343 0.3779 2.2018 0.1369  0.0558  -0.1435 245 GLN C N   
10444 C CA  . GLN C 245 ? 0.4177 0.3690 2.1617 0.1290  0.0553  -0.1221 245 GLN C CA  
10445 C C   . GLN C 245 ? 0.4230 0.3931 2.1486 0.1224  0.0545  -0.1352 245 GLN C C   
10446 O O   . GLN C 245 ? 0.4069 0.3929 2.1065 0.1191  0.0565  -0.1223 245 GLN C O   
10447 C CB  . GLN C 245 ? 0.4160 0.3455 2.1775 0.1227  0.0502  -0.1007 245 GLN C CB  
10448 C CG  . GLN C 245 ? 0.4127 0.3288 2.1857 0.1287  0.0504  -0.0811 245 GLN C CG  
10449 C CD  . GLN C 245 ? 0.4196 0.3170 2.2107 0.1227  0.0457  -0.0592 245 GLN C CD  
10450 O OE1 . GLN C 245 ? 0.4493 0.3333 2.2637 0.1167  0.0413  -0.0654 245 GLN C OE1 
10451 N NE2 . GLN C 245 ? 0.4057 0.3034 2.1867 0.1240  0.0463  -0.0338 245 GLN C NE2 
10452 N N   . GLN C 246 ? 0.4482 0.4161 2.1892 0.1206  0.0508  -0.1611 246 GLN C N   
10453 C CA  . GLN C 246 ? 0.4585 0.4472 2.1836 0.1148  0.0486  -0.1769 246 GLN C CA  
10454 C C   . GLN C 246 ? 0.4586 0.4771 2.1543 0.1216  0.0557  -0.1843 246 GLN C C   
10455 O O   . GLN C 246 ? 0.4504 0.4883 2.1201 0.1186  0.0575  -0.1722 246 GLN C O   
10456 C CB  . GLN C 246 ? 0.4863 0.4640 2.2378 0.1115  0.0419  -0.2048 246 GLN C CB  
10457 C CG  . GLN C 246 ? 0.4933 0.4924 2.2321 0.1044  0.0372  -0.2239 246 GLN C CG  
10458 C CD  . GLN C 246 ? 0.5217 0.5177 2.2802 0.1055  0.0324  -0.2613 246 GLN C CD  
10459 O OE1 . GLN C 246 ? 0.5324 0.5102 2.3143 0.1130  0.0337  -0.2742 246 GLN C OE1 
10460 N NE2 . GLN C 246 ? 0.5333 0.5491 2.2822 0.0991  0.0268  -0.2810 246 GLN C NE2 
10461 N N   . SER C 247 ? 0.4748 0.4965 2.1768 0.1312  0.0603  -0.2011 247 SER C N   
10462 C CA  . SER C 247 ? 0.4739 0.5251 2.1512 0.1382  0.0684  -0.2051 247 SER C CA  
10463 C C   . SER C 247 ? 0.4486 0.5073 2.1045 0.1364  0.0721  -0.1745 247 SER C C   
10464 O O   . SER C 247 ? 0.4397 0.5205 2.0708 0.1330  0.0734  -0.1681 247 SER C O   
10465 C CB  . SER C 247 ? 0.4861 0.5356 2.1790 0.1495  0.0739  -0.2194 247 SER C CB  
10466 O OG  . SER C 247 ? 0.4924 0.5755 2.1640 0.1558  0.0819  -0.2304 247 SER C OG  
10467 N N   . ASP C 248 ? 0.4356 0.4745 2.1033 0.1386  0.0726  -0.1555 248 ASP C N   
10468 C CA  . ASP C 248 ? 0.4156 0.4596 2.0666 0.1384  0.0759  -0.1303 248 ASP C CA  
10469 C C   . ASP C 248 ? 0.4108 0.4591 2.0441 0.1303  0.0731  -0.1156 248 ASP C C   
10470 O O   . ASP C 248 ? 0.4030 0.4659 2.0164 0.1303  0.0767  -0.1021 248 ASP C O   
10471 C CB  . ASP C 248 ? 0.4066 0.4288 2.0746 0.1416  0.0749  -0.1149 248 ASP C CB  
10472 C CG  . ASP C 248 ? 0.4112 0.4378 2.0914 0.1513  0.0796  -0.1239 248 ASP C CG  
10473 O OD1 . ASP C 248 ? 0.4128 0.4612 2.0861 0.1555  0.0850  -0.1420 248 ASP C OD1 
10474 O OD2 . ASP C 248 ? 0.4098 0.4205 2.1066 0.1547  0.0780  -0.1127 248 ASP C OD2 
10475 N N   . GLY C 249 ? 0.4191 0.4545 2.0632 0.1238  0.0668  -0.1178 249 GLY C N   
10476 C CA  . GLY C 249 ? 0.4085 0.4474 2.0407 0.1164  0.0640  -0.1037 249 GLY C CA  
10477 C C   . GLY C 249 ? 0.4085 0.4750 2.0203 0.1144  0.0644  -0.1127 249 GLY C C   
10478 O O   . GLY C 249 ? 0.3919 0.4705 1.9855 0.1130  0.0660  -0.0974 249 GLY C O   
10479 N N   . LEU C 250 ? 0.4282 0.5055 2.0440 0.1148  0.0626  -0.1380 250 LEU C N   
10480 C CA  . LEU C 250 ? 0.4389 0.5464 2.0347 0.1133  0.0622  -0.1482 250 LEU C CA  
10481 C C   . LEU C 250 ? 0.4272 0.5559 1.9995 0.1179  0.0693  -0.1341 250 LEU C C   
10482 O O   . LEU C 250 ? 0.4241 0.5709 1.9790 0.1153  0.0688  -0.1233 250 LEU C O   
10483 C CB  . LEU C 250 ? 0.4644 0.5834 2.0654 0.1152  0.0604  -0.1804 250 LEU C CB  
10484 C CG  . LEU C 250 ? 0.4834 0.5995 2.0972 0.1072  0.0508  -0.1980 250 LEU C CG  
10485 C CD1 . LEU C 250 ? 0.4784 0.6177 2.0737 0.1008  0.0466  -0.1895 250 LEU C CD1 
10486 C CD2 . LEU C 250 ? 0.4869 0.5678 2.1308 0.1021  0.0459  -0.1918 250 LEU C CD2 
10487 N N   . ILE C 251 ? 0.4288 0.5553 2.0037 0.1248  0.0757  -0.1335 251 ILE C N   
10488 C CA  . ILE C 251 ? 0.4197 0.5658 1.9772 0.1287  0.0829  -0.1205 251 ILE C CA  
10489 C C   . ILE C 251 ? 0.4111 0.5466 1.9629 0.1257  0.0824  -0.0932 251 ILE C C   
10490 O O   . ILE C 251 ? 0.4143 0.5674 1.9497 0.1251  0.0847  -0.0801 251 ILE C O   
10491 C CB  . ILE C 251 ? 0.4135 0.5592 1.9804 0.1363  0.0894  -0.1273 251 ILE C CB  
10492 C CG1 . ILE C 251 ? 0.4291 0.5877 2.0014 0.1408  0.0906  -0.1576 251 ILE C CG1 
10493 C CG2 . ILE C 251 ? 0.4007 0.5643 1.9548 0.1390  0.0967  -0.1102 251 ILE C CG2 
10494 C CD1 . ILE C 251 ? 0.4387 0.6337 1.9890 0.1406  0.0921  -0.1692 251 ILE C CD1 
10495 N N   . SER C 252 ? 0.4152 0.5226 1.9813 0.1241  0.0793  -0.0850 252 SER C N   
10496 C CA  . SER C 252 ? 0.4213 0.5178 1.9824 0.1221  0.0788  -0.0622 252 SER C CA  
10497 C C   . SER C 252 ? 0.4125 0.5194 1.9618 0.1175  0.0759  -0.0547 252 SER C C   
10498 O O   . SER C 252 ? 0.3930 0.5041 1.9316 0.1177  0.0775  -0.0382 252 SER C O   
10499 C CB  . SER C 252 ? 0.4303 0.4993 2.0075 0.1216  0.0758  -0.0563 252 SER C CB  
10500 O OG  . SER C 252 ? 0.4348 0.4954 2.0060 0.1218  0.0765  -0.0368 252 SER C OG  
10501 N N   . ASN C 253 ? 0.4259 0.5371 1.9796 0.1135  0.0711  -0.0674 253 ASN C N   
10502 C CA  . ASN C 253 ? 0.4349 0.5594 1.9803 0.1091  0.0674  -0.0622 253 ASN C CA  
10503 C C   . ASN C 253 ? 0.4387 0.5936 1.9651 0.1111  0.0696  -0.0614 253 ASN C C   
10504 O O   . ASN C 253 ? 0.4255 0.5904 1.9424 0.1103  0.0690  -0.0465 253 ASN C O   
10505 C CB  . ASN C 253 ? 0.4482 0.5715 2.0062 0.1033  0.0607  -0.0779 253 ASN C CB  
10506 C CG  . ASN C 253 ? 0.4424 0.5389 2.0207 0.0996  0.0579  -0.0735 253 ASN C CG  
10507 O OD1 . ASN C 253 ? 0.4431 0.5353 2.0368 0.0942  0.0524  -0.0859 253 ASN C OD1 
10508 N ND2 . ASN C 253 ? 0.4353 0.5154 2.0145 0.1019  0.0610  -0.0558 253 ASN C ND2 
10509 N N   . TYR C 254 ? 0.4487 0.6195 1.9705 0.1141  0.0724  -0.0772 254 TYR C N   
10510 C CA  . TYR C 254 ? 0.4541 0.6589 1.9574 0.1158  0.0745  -0.0778 254 TYR C CA  
10511 C C   . TYR C 254 ? 0.4433 0.6524 1.9372 0.1183  0.0796  -0.0528 254 TYR C C   
10512 O O   . TYR C 254 ? 0.4566 0.6862 1.9383 0.1178  0.0788  -0.0409 254 TYR C O   
10513 C CB  . TYR C 254 ? 0.4609 0.6845 1.9598 0.1201  0.0787  -0.0978 254 TYR C CB  
10514 C CG  . TYR C 254 ? 0.4697 0.7318 1.9506 0.1202  0.0774  -0.1085 254 TYR C CG  
10515 C CD1 . TYR C 254 ? 0.4675 0.7581 1.9300 0.1219  0.0812  -0.0909 254 TYR C CD1 
10516 C CD2 . TYR C 254 ? 0.4848 0.7559 1.9678 0.1187  0.0721  -0.1365 254 TYR C CD2 
10517 C CE1 . TYR C 254 ? 0.4838 0.8132 1.9282 0.1224  0.0797  -0.0990 254 TYR C CE1 
10518 C CE2 . TYR C 254 ? 0.5018 0.8110 1.9665 0.1189  0.0700  -0.1480 254 TYR C CE2 
10519 C CZ  . TYR C 254 ? 0.5008 0.8409 1.9448 0.1210  0.0740  -0.1286 254 TYR C CZ  
10520 O OH  . TYR C 254 ? 0.5203 0.9013 1.9446 0.1215  0.0715  -0.1390 254 TYR C OH  
10521 N N   . ARG C 255 ? 0.4287 0.6180 1.9306 0.1207  0.0839  -0.0450 255 ARG C N   
10522 C CA  . ARG C 255 ? 0.4128 0.6019 1.9104 0.1223  0.0881  -0.0234 255 ARG C CA  
10523 C C   . ARG C 255 ? 0.4148 0.5917 1.9123 0.1202  0.0843  -0.0071 255 ARG C C   
10524 O O   . ARG C 255 ? 0.4233 0.6119 1.9135 0.1208  0.0854  0.0089  255 ARG C O   
10525 C CB  . ARG C 255 ? 0.3938 0.5649 1.9023 0.1247  0.0919  -0.0218 255 ARG C CB  
10526 C CG  . ARG C 255 ? 0.3768 0.5365 1.8866 0.1247  0.0935  -0.0009 255 ARG C CG  
10527 C CD  . ARG C 255 ? 0.3751 0.5560 1.8791 0.1257  0.0991  0.0118  255 ARG C CD  
10528 N NE  . ARG C 255 ? 0.3726 0.5734 1.8653 0.1248  0.0987  0.0239  255 ARG C NE  
10529 C CZ  . ARG C 255 ? 0.3805 0.6131 1.8634 0.1256  0.1027  0.0269  255 ARG C CZ  
10530 N NH1 . ARG C 255 ? 0.3936 0.6436 1.8759 0.1277  0.1086  0.0176  255 ARG C NH1 
10531 N NH2 . ARG C 255 ? 0.3781 0.6273 1.8520 0.1251  0.1011  0.0403  255 ARG C NH2 
10532 N N   . ASP C 256 ? 0.4129 0.5673 1.9201 0.1181  0.0803  -0.0105 256 ASP C N   
10533 C CA  . ASP C 256 ? 0.4026 0.5458 1.9109 0.1171  0.0778  0.0033  256 ASP C CA  
10534 C C   . ASP C 256 ? 0.3934 0.5586 1.8937 0.1161  0.0751  0.0087  256 ASP C C   
10535 O O   . ASP C 256 ? 0.3965 0.5643 1.8932 0.1182  0.0760  0.0250  256 ASP C O   
10536 C CB  . ASP C 256 ? 0.3975 0.5181 1.9172 0.1150  0.0749  -0.0008 256 ASP C CB  
10537 C CG  . ASP C 256 ? 0.3962 0.4947 1.9230 0.1169  0.0768  0.0011  256 ASP C CG  
10538 O OD1 . ASP C 256 ? 0.3923 0.4928 1.9189 0.1193  0.0799  -0.0017 256 ASP C OD1 
10539 O OD2 . ASP C 256 ? 0.3991 0.4810 1.9314 0.1162  0.0752  0.0065  256 ASP C OD2 
10540 N N   . LEU C 257 ? 0.3938 0.5758 1.8923 0.1133  0.0713  -0.0053 257 LEU C N   
10541 C CA  . LEU C 257 ? 0.3975 0.6008 1.8909 0.1116  0.0666  -0.0015 257 LEU C CA  
10542 C C   . LEU C 257 ? 0.3966 0.6257 1.8765 0.1148  0.0688  0.0109  257 LEU C C   
10543 O O   . LEU C 257 ? 0.3755 0.6174 1.8528 0.1156  0.0662  0.0245  257 LEU C O   
10544 C CB  . LEU C 257 ? 0.4044 0.6183 1.9013 0.1069  0.0608  -0.0226 257 LEU C CB  
10545 C CG  . LEU C 257 ? 0.3957 0.5847 1.9099 0.1027  0.0579  -0.0312 257 LEU C CG  
10546 C CD1 . LEU C 257 ? 0.4073 0.6028 1.9290 0.0977  0.0521  -0.0545 257 LEU C CD1 
10547 C CD2 . LEU C 257 ? 0.3886 0.5722 1.9091 0.1011  0.0558  -0.0162 257 LEU C CD2 
10548 N N   . ILE C 258 ? 0.4069 0.6450 1.8803 0.1168  0.0738  0.0075  258 ILE C N   
10549 C CA  . ILE C 258 ? 0.4240 0.6847 1.8869 0.1197  0.0775  0.0237  258 ILE C CA  
10550 C C   . ILE C 258 ? 0.4180 0.6598 1.8878 0.1218  0.0797  0.0462  258 ILE C C   
10551 O O   . ILE C 258 ? 0.4123 0.6663 1.8796 0.1234  0.0784  0.0639  258 ILE C O   
10552 C CB  . ILE C 258 ? 0.4367 0.7112 1.8936 0.1213  0.0838  0.0161  258 ILE C CB  
10553 C CG1 . ILE C 258 ? 0.4619 0.7590 1.9106 0.1206  0.0817  -0.0082 258 ILE C CG1 
10554 C CG2 . ILE C 258 ? 0.4438 0.7393 1.8934 0.1236  0.0887  0.0382  258 ILE C CG2 
10555 C CD1 . ILE C 258 ? 0.4704 0.7822 1.9143 0.1236  0.0890  -0.0186 258 ILE C CD1 
10556 N N   . ASP C 259 ? 0.4048 0.6169 1.8842 0.1220  0.0822  0.0444  259 ASP C N   
10557 C CA  . ASP C 259 ? 0.3945 0.5854 1.8814 0.1238  0.0837  0.0605  259 ASP C CA  
10558 C C   . ASP C 259 ? 0.3907 0.5776 1.8804 0.1252  0.0798  0.0698  259 ASP C C   
10559 O O   . ASP C 259 ? 0.3947 0.5711 1.8896 0.1280  0.0807  0.0847  259 ASP C O   
10560 C CB  . ASP C 259 ? 0.3829 0.5453 1.8781 0.1235  0.0850  0.0535  259 ASP C CB  
10561 C CG  . ASP C 259 ? 0.3873 0.5516 1.8840 0.1234  0.0893  0.0478  259 ASP C CG  
10562 O OD1 . ASP C 259 ? 0.3924 0.5786 1.8842 0.1237  0.0929  0.0539  259 ASP C OD1 
10563 O OD2 . ASP C 259 ? 0.3852 0.5315 1.8886 0.1231  0.0891  0.0380  259 ASP C OD2 
10564 N N   . ALA C 260 ? 0.3777 0.5728 1.8664 0.1232  0.0753  0.0604  260 ALA C N   
10565 C CA  . ALA C 260 ? 0.3636 0.5585 1.8569 0.1245  0.0718  0.0680  260 ALA C CA  
10566 C C   . ALA C 260 ? 0.3537 0.5795 1.8415 0.1254  0.0683  0.0768  260 ALA C C   
10567 O O   . ALA C 260 ? 0.3433 0.5737 1.8364 0.1269  0.0649  0.0834  260 ALA C O   
10568 C CB  . ALA C 260 ? 0.3638 0.5491 1.8632 0.1210  0.0689  0.0545  260 ALA C CB  
10569 N N   . GLY C 261 ? 0.3549 0.6045 1.8323 0.1247  0.0690  0.0766  261 GLY C N   
10570 C CA  . GLY C 261 ? 0.3625 0.6439 1.8329 0.1264  0.0660  0.0895  261 GLY C CA  
10571 C C   . GLY C 261 ? 0.3762 0.6900 1.8341 0.1231  0.0618  0.0748  261 GLY C C   
10572 O O   . GLY C 261 ? 0.3855 0.7312 1.8342 0.1246  0.0594  0.0854  261 GLY C O   
10573 N N   . ALA C 262 ? 0.3787 0.6858 1.8366 0.1190  0.0606  0.0506  262 ALA C N   
10574 C CA  . ALA C 262 ? 0.3889 0.7248 1.8369 0.1158  0.0555  0.0323  262 ALA C CA  
10575 C C   . ALA C 262 ? 0.4021 0.7702 1.8329 0.1183  0.0588  0.0370  262 ALA C C   
10576 O O   . ALA C 262 ? 0.4007 0.7621 1.8298 0.1206  0.0666  0.0429  262 ALA C O   
10577 C CB  . ALA C 262 ? 0.3881 0.7064 1.8423 0.1118  0.0549  0.0058  262 ALA C CB  
10578 N N   . VAL C 263 ? 0.4163 0.8221 1.8352 0.1177  0.0527  0.0360  263 VAL C N   
10579 C CA  . VAL C 263 ? 0.4386 0.8822 1.8381 0.1197  0.0552  0.0361  263 VAL C CA  
10580 C C   . VAL C 263 ? 0.4597 0.9270 1.8493 0.1164  0.0486  0.0057  263 VAL C C   
10581 O O   . VAL C 263 ? 0.4807 0.9882 1.8512 0.1178  0.0480  0.0018  263 VAL C O   
10582 C CB  . VAL C 263 ? 0.4520 0.9261 1.8436 0.1231  0.0536  0.0657  263 VAL C CB  
10583 C CG1 . VAL C 263 ? 0.4413 0.8881 1.8476 0.1262  0.0584  0.0942  263 VAL C CG1 
10584 C CG2 . VAL C 263 ? 0.4605 0.9594 1.8499 0.1213  0.0419  0.0642  263 VAL C CG2 
10585 N N   . GLY C 264 ? 0.4593 0.9023 1.8627 0.1117  0.0433  -0.0150 264 GLY C N   
10586 C CA  . GLY C 264 ? 0.4831 0.9386 1.8834 0.1077  0.0370  -0.0480 264 GLY C CA  
10587 C C   . GLY C 264 ? 0.4793 0.8928 1.9001 0.1041  0.0374  -0.0667 264 GLY C C   
10588 O O   . GLY C 264 ? 0.4725 0.8552 1.9096 0.1028  0.0380  -0.0537 264 GLY C O   
10589 N N   . MET C 265 ? 0.4896 0.9027 1.9102 0.1033  0.0375  -0.0963 265 MET C N   
10590 C CA  . MET C 265 ? 0.4855 0.8584 1.9274 0.1008  0.0385  -0.1112 265 MET C CA  
10591 C C   . MET C 265 ? 0.5241 0.9016 1.9727 0.0961  0.0304  -0.1463 265 MET C C   
10592 O O   . MET C 265 ? 0.5506 0.9563 1.9843 0.0984  0.0301  -0.1667 265 MET C O   
10593 C CB  . MET C 265 ? 0.4697 0.8250 1.9116 0.1066  0.0499  -0.1081 265 MET C CB  
10594 C CG  . MET C 265 ? 0.4471 0.7929 1.8871 0.1100  0.0568  -0.0758 265 MET C CG  
10595 S SD  . MET C 265 ? 0.4261 0.7314 1.8871 0.1065  0.0541  -0.0604 265 MET C SD  
10596 C CE  . MET C 265 ? 0.4235 0.6906 1.9013 0.1072  0.0590  -0.0736 265 MET C CE  
10597 N N   . CYS C 266 ? 0.5338 0.8842 2.0058 0.0893  0.0240  -0.1530 266 CYS C N   
10598 C CA  . CYS C 266 ? 0.5650 0.9143 2.0502 0.0831  0.0149  -0.1852 266 CYS C CA  
10599 C C   . CYS C 266 ? 0.5678 0.8727 2.0803 0.0812  0.0169  -0.1938 266 CYS C C   
10600 O O   . CYS C 266 ? 0.5653 0.8500 2.1002 0.0736  0.0108  -0.1917 266 CYS C O   
10601 C CB  . CYS C 266 ? 0.5719 0.9368 2.0638 0.0747  0.0026  -0.1847 266 CYS C CB  
10602 S SG  . CYS C 266 ? 0.5951 1.0160 2.0567 0.0771  -0.0021 -0.1745 266 CYS C SG  
10603 N N   . PRO C 267 ? 0.5559 0.8465 2.0683 0.0880  0.0256  -0.2019 267 PRO C N   
10604 C CA  . PRO C 267 ? 0.5479 0.7978 2.0866 0.0874  0.0274  -0.2086 267 PRO C CA  
10605 C C   . PRO C 267 ? 0.5669 0.8057 2.1297 0.0791  0.0166  -0.2340 267 PRO C C   
10606 O O   . PRO C 267 ? 0.5753 0.8399 2.1314 0.0763  0.0091  -0.2574 267 PRO C O   
10607 C CB  . PRO C 267 ? 0.5569 0.8076 2.0884 0.0970  0.0367  -0.2201 267 PRO C CB  
10608 C CG  . PRO C 267 ? 0.5714 0.8674 2.0739 0.1010  0.0380  -0.2288 267 PRO C CG  
10609 C CD  . PRO C 267 ? 0.5602 0.8753 2.0488 0.0969  0.0342  -0.2035 267 PRO C CD  
10610 N N   . PHE C 268 ? 0.5715 0.7730 2.1630 0.0750  0.0155  -0.2290 268 PHE C N   
10611 C CA  . PHE C 268 ? 0.6049 0.7937 2.2242 0.0647  0.0047  -0.2449 268 PHE C CA  
10612 C C   . PHE C 268 ? 0.6226 0.7929 2.2621 0.0664  0.0030  -0.2766 268 PHE C C   
10613 O O   . PHE C 268 ? 0.6035 0.7424 2.2611 0.0702  0.0081  -0.2718 268 PHE C O   
10614 C CB  . PHE C 268 ? 0.6044 0.7669 2.2475 0.0572  0.0032  -0.2208 268 PHE C CB  
10615 C CG  . PHE C 268 ? 0.6258 0.7814 2.2987 0.0446  -0.0086 -0.2340 268 PHE C CG  
10616 C CD1 . PHE C 268 ? 0.6454 0.8309 2.3131 0.0376  -0.0185 -0.2461 268 PHE C CD1 
10617 C CD2 . PHE C 268 ? 0.6404 0.7603 2.3485 0.0395  -0.0103 -0.2333 268 PHE C CD2 
10618 C CE1 . PHE C 268 ? 0.6626 0.8418 2.3610 0.0249  -0.0299 -0.2580 268 PHE C CE1 
10619 C CE2 . PHE C 268 ? 0.6673 0.7801 2.4065 0.0268  -0.0210 -0.2436 268 PHE C CE2 
10620 C CZ  . PHE C 268 ? 0.6741 0.8164 2.4090 0.0191  -0.0309 -0.2565 268 PHE C CZ  
10621 N N   . TYR C 269 ? 0.6527 0.8471 2.2860 0.0649  -0.0042 -0.3085 269 TYR C N   
10622 C CA  . TYR C 269 ? 0.6726 0.8547 2.3338 0.0586  -0.0144 -0.3428 269 TYR C CA  
10623 C C   . TYR C 269 ? 0.6722 0.8546 2.3297 0.0694  -0.0093 -0.3730 269 TYR C C   
10624 O O   . TYR C 269 ? 0.6558 0.8182 2.3174 0.0782  0.0007  -0.3635 269 TYR C O   
10625 C CB  . TYR C 269 ? 0.6861 0.8285 2.3880 0.0490  -0.0192 -0.3309 269 TYR C CB  
10626 C CG  . TYR C 269 ? 0.7174 0.8509 2.4522 0.0363  -0.0334 -0.3560 269 TYR C CG  
10627 C CD1 . TYR C 269 ? 0.7374 0.9035 2.4625 0.0301  -0.0442 -0.3801 269 TYR C CD1 
10628 C CD2 . TYR C 269 ? 0.7366 0.8295 2.5146 0.0299  -0.0366 -0.3539 269 TYR C CD2 
10629 C CE1 . TYR C 269 ? 0.7786 0.9357 2.5368 0.0175  -0.0582 -0.4038 269 TYR C CE1 
10630 C CE2 . TYR C 269 ? 0.7743 0.8566 2.5873 0.0172  -0.0498 -0.3754 269 TYR C CE2 
10631 C CZ  . TYR C 269 ? 0.7917 0.9056 2.5954 0.0105  -0.0610 -0.4016 269 TYR C CZ  
10632 O OH  . TYR C 269 ? 0.8107 0.9139 2.6515 -0.0031 -0.0752 -0.4241 269 TYR C OH  
10633 N N   . TYR C 270 ? 0.6870 0.8960 2.3353 0.0692  -0.0161 -0.4092 270 TYR C N   
10634 C CA  . TYR C 270 ? 0.7051 0.9186 2.3513 0.0797  -0.0121 -0.4443 270 TYR C CA  
10635 C C   . TYR C 270 ? 0.7204 0.8890 2.4117 0.0786  -0.0158 -0.4651 270 TYR C C   
10636 O O   . TYR C 270 ? 0.7161 0.8698 2.4152 0.0898  -0.0074 -0.4745 270 TYR C O   
10637 C CB  . TYR C 270 ? 0.7263 0.9843 2.3482 0.0795  -0.0192 -0.4780 270 TYR C CB  
10638 C CG  . TYR C 270 ? 0.7570 1.0137 2.3902 0.0858  -0.0213 -0.5273 270 TYR C CG  
10639 C CD1 . TYR C 270 ? 0.7812 1.0143 2.4504 0.0770  -0.0347 -0.5587 270 TYR C CD1 
10640 C CD2 . TYR C 270 ? 0.7647 1.0458 2.3739 0.1004  -0.0100 -0.5436 270 TYR C CD2 
10641 C CE1 . TYR C 270 ? 0.8190 1.0499 2.5004 0.0833  -0.0371 -0.6065 270 TYR C CE1 
10642 C CE2 . TYR C 270 ? 0.8013 1.0838 2.4203 0.1075  -0.0113 -0.5909 270 TYR C CE2 
10643 C CZ  . TYR C 270 ? 0.8287 1.0849 2.4841 0.0992  -0.0252 -0.6238 270 TYR C CZ  
10644 O OH  . TYR C 270 ? 0.8655 1.1198 2.5340 0.1065  -0.0273 -0.6732 270 TYR C OH  
10645 N N   . ALA C 271 ? 0.7371 0.8850 2.4604 0.0651  -0.0287 -0.4715 271 ALA C N   
10646 C CA  . ALA C 271 ? 0.7653 0.8700 2.5358 0.0627  -0.0337 -0.4905 271 ALA C CA  
10647 C C   . ALA C 271 ? 0.7598 0.8351 2.5666 0.0472  -0.0428 -0.4696 271 ALA C C   
10648 O O   . ALA C 271 ? 0.7396 0.8335 2.5395 0.0359  -0.0501 -0.4581 271 ALA C O   
10649 C CB  . ALA C 271 ? 0.8091 0.9236 2.5872 0.0642  -0.0420 -0.5436 271 ALA C CB  
10650 N N   . ASP C 272 ? 0.7784 0.8090 2.6263 0.0472  -0.0422 -0.4657 272 ASP C N   
10651 C CA  . ASP C 272 ? 0.7874 0.7861 2.6764 0.0334  -0.0495 -0.4456 272 ASP C CA  
10652 C C   . ASP C 272 ? 0.8212 0.8280 2.7299 0.0177  -0.0656 -0.4702 272 ASP C C   
10653 O O   . ASP C 272 ? 0.8553 0.8725 2.7660 0.0184  -0.0733 -0.5140 272 ASP C O   
10654 C CB  . ASP C 272 ? 0.8029 0.7547 2.7365 0.0370  -0.0484 -0.4479 272 ASP C CB  
10655 C CG  . ASP C 272 ? 0.7863 0.7234 2.7121 0.0508  -0.0346 -0.4214 272 ASP C CG  
10656 O OD1 . ASP C 272 ? 0.7506 0.7078 2.6405 0.0546  -0.0258 -0.3916 272 ASP C OD1 
10657 O OD2 . ASP C 272 ? 0.8078 0.7135 2.7650 0.0579  -0.0333 -0.4316 272 ASP C OD2 
10658 N N   . GLY C 273 ? 0.8035 0.8058 2.7289 0.0035  -0.0707 -0.4418 273 GLY C N   
10659 C CA  . GLY C 273 ? 0.8258 0.8248 2.7857 -0.0138 -0.0865 -0.4591 273 GLY C CA  
10660 C C   . GLY C 273 ? 0.8349 0.7873 2.8507 -0.0229 -0.0892 -0.4422 273 GLY C C   
10661 O O   . GLY C 273 ? 0.7998 0.7412 2.8198 -0.0247 -0.0820 -0.3993 273 GLY C O   
10662 N N   . TRP C 274 ? 0.8760 0.8018 2.9351 -0.0282 -0.0996 -0.4759 274 TRP C N   
10663 C CA  . TRP C 274 ? 0.8907 0.7716 3.0080 -0.0377 -0.1034 -0.4602 274 TRP C CA  
10664 C C   . TRP C 274 ? 0.8770 0.7627 3.0215 -0.0588 -0.1132 -0.4411 274 TRP C C   
10665 O O   . TRP C 274 ? 0.8705 0.7233 3.0642 -0.0691 -0.1162 -0.4220 274 TRP C O   
10666 C CB  . TRP C 274 ? 0.9471 0.7963 3.1052 -0.0360 -0.1117 -0.5041 274 TRP C CB  
10667 C CG  . TRP C 274 ? 0.9573 0.7948 3.1011 -0.0150 -0.1009 -0.5177 274 TRP C CG  
10668 C CD1 . TRP C 274 ? 0.9293 0.7929 3.0205 0.0016  -0.0876 -0.5113 274 TRP C CD1 
10669 C CD2 . TRP C 274 ? 0.9923 0.7877 3.1809 -0.0086 -0.1029 -0.5401 274 TRP C CD2 
10670 N NE1 . TRP C 274 ? 0.9457 0.7885 3.0453 0.0177  -0.0809 -0.5282 274 TRP C NE1 
10671 C CE2 . TRP C 274 ? 0.9830 0.7840 3.1417 0.0126  -0.0900 -0.5464 274 TRP C CE2 
10672 C CE3 . TRP C 274 ? 1.0362 0.7900 3.2897 -0.0187 -0.1144 -0.5546 274 TRP C CE3 
10673 C CZ2 . TRP C 274 ? 1.0176 0.7849 3.2087 0.0249  -0.0880 -0.5672 274 TRP C CZ2 
10674 C CZ3 . TRP C 274 ? 1.0683 0.7864 3.3545 -0.0065 -0.1128 -0.5752 274 TRP C CZ3 
10675 C CH2 . TRP C 274 ? 1.0566 0.7821 3.3115 0.0156  -0.0997 -0.5818 274 TRP C CH2 
10676 N N   . TRP C 275 ? 0.8706 0.7990 2.9841 -0.0647 -0.1179 -0.4453 275 TRP C N   
10677 C CA  . TRP C 275 ? 0.8794 0.8207 3.0165 -0.0844 -0.1283 -0.4324 275 TRP C CA  
10678 C C   . TRP C 275 ? 0.8404 0.7942 2.9619 -0.0858 -0.1177 -0.3790 275 TRP C C   
10679 O O   . TRP C 275 ? 0.8287 0.7797 2.9835 -0.1013 -0.1222 -0.3559 275 TRP C O   
10680 C CB  . TRP C 275 ? 0.8951 0.8785 3.0101 -0.0901 -0.1409 -0.4670 275 TRP C CB  
10681 C CG  . TRP C 275 ? 0.8666 0.8947 2.9169 -0.0776 -0.1329 -0.4606 275 TRP C CG  
10682 C CD1 . TRP C 275 ? 0.8751 0.9199 2.8832 -0.0614 -0.1275 -0.4851 275 TRP C CD1 
10683 C CD2 . TRP C 275 ? 0.8371 0.9001 2.8604 -0.0805 -0.1296 -0.4269 275 TRP C CD2 
10684 N NE1 . TRP C 275 ? 0.8531 0.9391 2.8108 -0.0546 -0.1212 -0.4669 275 TRP C NE1 
10685 C CE2 . TRP C 275 ? 0.8258 0.9227 2.7920 -0.0656 -0.1226 -0.4321 275 TRP C CE2 
10686 C CE3 . TRP C 275 ? 0.8152 0.8850 2.8583 -0.0936 -0.1312 -0.3926 275 TRP C CE3 
10687 C CZ2 . TRP C 275 ? 0.7914 0.9252 2.7221 -0.0634 -0.1182 -0.4045 275 TRP C CZ2 
10688 C CZ3 . TRP C 275 ? 0.7796 0.8872 2.7863 -0.0904 -0.1262 -0.3671 275 TRP C CZ3 
10689 C CH2 . TRP C 275 ? 0.7674 0.9052 2.7195 -0.0755 -0.1204 -0.3732 275 TRP C CH2 
10690 N N   . LYS C 276 ? 0.8186 0.7871 2.8912 -0.0696 -0.1036 -0.3603 276 LYS C N   
10691 C CA  . LYS C 276 ? 0.7964 0.7845 2.8455 -0.0689 -0.0941 -0.3165 276 LYS C CA  
10692 C C   . LYS C 276 ? 0.7994 0.7576 2.8856 -0.0755 -0.0888 -0.2780 276 LYS C C   
10693 O O   . LYS C 276 ? 0.7899 0.7632 2.8680 -0.0785 -0.0827 -0.2423 276 LYS C O   
10694 C CB  . LYS C 276 ? 0.7723 0.7790 2.7647 -0.0504 -0.0807 -0.3068 276 LYS C CB  
10695 C CG  . LYS C 276 ? 0.7766 0.8191 2.7269 -0.0428 -0.0838 -0.3378 276 LYS C CG  
10696 C CD  . LYS C 276 ? 0.7520 0.8065 2.6537 -0.0242 -0.0703 -0.3310 276 LYS C CD  
10697 C CE  . LYS C 276 ? 0.7179 0.8037 2.5814 -0.0201 -0.0632 -0.3009 276 LYS C CE  
10698 N NZ  . LYS C 276 ? 0.7172 0.8457 2.5579 -0.0236 -0.0715 -0.3150 276 LYS C NZ  
10699 N N   . GLY C 277 ? 0.8227 0.7403 2.9499 -0.0771 -0.0909 -0.2844 277 GLY C N   
10700 C CA  . GLY C 277 ? 0.8241 0.7144 2.9860 -0.0824 -0.0857 -0.2458 277 GLY C CA  
10701 C C   . GLY C 277 ? 0.8653 0.7376 3.0896 -0.1028 -0.0979 -0.2468 277 GLY C C   
10702 O O   . GLY C 277 ? 0.8915 0.7334 3.1545 -0.1072 -0.0955 -0.2219 277 GLY C O   
10703 N N   . GLY C 278 ? 0.8719 0.7630 3.1081 -0.1157 -0.1115 -0.2748 278 GLY C N   
10704 C CA  . GLY C 278 ? 0.8889 0.7698 3.1838 -0.1375 -0.1232 -0.2711 278 GLY C CA  
10705 C C   . GLY C 278 ? 0.9327 0.7851 3.2726 -0.1455 -0.1385 -0.3153 278 GLY C C   
10706 O O   . GLY C 278 ? 0.9564 0.8116 3.3369 -0.1646 -0.1525 -0.3274 278 GLY C O   
10707 N N   . GLU C 279 ? 0.9346 0.7591 3.2711 -0.1311 -0.1361 -0.3390 279 GLU C N   
10708 C CA  . GLU C 279 ? 0.9679 0.7645 3.3444 -0.1354 -0.1497 -0.3855 279 GLU C CA  
10709 C C   . GLU C 279 ? 0.9761 0.7797 3.3103 -0.1160 -0.1472 -0.4272 279 GLU C C   
10710 O O   . GLU C 279 ? 0.9613 0.7554 3.2691 -0.0978 -0.1339 -0.4160 279 GLU C O   
10711 C CB  . GLU C 279 ? 0.9806 0.7261 3.4201 -0.1407 -0.1504 -0.3683 279 GLU C CB  
10712 C CG  . GLU C 279 ? 0.9712 0.7146 3.4528 -0.1608 -0.1522 -0.3251 279 GLU C CG  
10713 C CD  . GLU C 279 ? 1.0032 0.6970 3.5574 -0.1704 -0.1575 -0.3148 279 GLU C CD  
10714 O OE1 . GLU C 279 ? 1.0043 0.6668 3.5634 -0.1560 -0.1501 -0.3080 279 GLU C OE1 
10715 O OE2 . GLU C 279 ? 1.0225 0.7098 3.6296 -0.1921 -0.1693 -0.3126 279 GLU C OE2 
10716 N N   . LYS C 280 ? 0.9994 0.8216 3.3292 -0.1207 -0.1605 -0.4757 280 LYS C N   
10717 C CA  . LYS C 280 ? 1.0021 0.8481 3.2821 -0.1043 -0.1587 -0.5153 280 LYS C CA  
10718 C C   . LYS C 280 ? 1.0427 0.8540 3.3464 -0.0939 -0.1611 -0.5564 280 LYS C C   
10719 O O   . LYS C 280 ? 1.0590 0.8903 3.3294 -0.0823 -0.1619 -0.5975 280 LYS C O   
10720 C CB  . LYS C 280 ? 1.0128 0.9012 3.2738 -0.1139 -0.1726 -0.5493 280 LYS C CB  
10721 C CG  . LYS C 280 ? 1.0646 0.9360 3.3805 -0.1310 -0.1930 -0.5908 280 LYS C CG  
10722 C CD  . LYS C 280 ? 1.0779 0.9944 3.3714 -0.1388 -0.2080 -0.6297 280 LYS C CD  
10723 C CE  . LYS C 280 ? 1.1215 1.0198 3.4662 -0.1531 -0.2285 -0.6794 280 LYS C CE  
10724 N NZ  . LYS C 280 ? 1.1377 1.0815 3.4459 -0.1525 -0.2404 -0.7265 280 LYS C NZ  
10725 N N   . SER C 281 ? 1.0689 0.8304 3.4312 -0.0980 -0.1625 -0.5460 281 SER C N   
10726 C CA  . SER C 281 ? 1.1068 0.8312 3.4966 -0.0862 -0.1635 -0.5805 281 SER C CA  
10727 C C   . SER C 281 ? 1.0904 0.7781 3.4983 -0.0751 -0.1504 -0.5413 281 SER C C   
10728 O O   . SER C 281 ? 1.1129 0.7727 3.5371 -0.0609 -0.1477 -0.5631 281 SER C O   
10729 C CB  . SER C 281 ? 1.1687 0.8640 3.6226 -0.1017 -0.1823 -0.6188 281 SER C CB  
10730 O OG  . SER C 281 ? 1.1991 0.9273 3.6343 -0.1076 -0.1953 -0.6681 281 SER C OG  
10731 N N   . ASP C 282 ? 1.0587 0.7487 3.4648 -0.0814 -0.1427 -0.4844 282 ASP C N   
10732 C CA  . ASP C 282 ? 1.0437 0.7089 3.4560 -0.0707 -0.1298 -0.4416 282 ASP C CA  
10733 C C   . ASP C 282 ? 1.0065 0.7074 3.3493 -0.0562 -0.1144 -0.4176 282 ASP C C   
10734 O O   . ASP C 282 ? 0.9862 0.7159 3.3018 -0.0636 -0.1108 -0.3867 282 ASP C O   
10735 C CB  . ASP C 282 ? 1.0401 0.6836 3.5002 -0.0875 -0.1318 -0.3946 282 ASP C CB  
10736 C CG  . ASP C 282 ? 1.0206 0.6420 3.4873 -0.0777 -0.1193 -0.3465 282 ASP C CG  
10737 O OD1 . ASP C 282 ? 1.0445 0.6260 3.5521 -0.0708 -0.1206 -0.3521 282 ASP C OD1 
10738 O OD2 . ASP C 282 ? 0.9906 0.6360 3.4212 -0.0763 -0.1087 -0.3048 282 ASP C OD2 
10739 N N   . HIS C 283 ? 1.0142 0.7136 3.3307 -0.0356 -0.1057 -0.4340 283 HIS C N   
10740 C CA  . HIS C 283 ? 0.9763 0.6981 3.2391 -0.0209 -0.0903 -0.4052 283 HIS C CA  
10741 C C   . HIS C 283 ? 0.9493 0.6480 3.2339 -0.0226 -0.0838 -0.3516 283 HIS C C   
10742 O O   . HIS C 283 ? 0.9750 0.6375 3.2977 -0.0168 -0.0833 -0.3459 283 HIS C O   
10743 C CB  . HIS C 283 ? 0.9933 0.7157 3.2334 0.0006  -0.0830 -0.4342 283 HIS C CB  
10744 C CG  . HIS C 283 ? 0.9820 0.7434 3.1564 0.0127  -0.0710 -0.4243 283 HIS C CG  
10745 N ND1 . HIS C 283 ? 1.0020 0.7740 3.1484 0.0315  -0.0627 -0.4465 283 HIS C ND1 
10746 C CD2 . HIS C 283 ? 0.9655 0.7570 3.1002 0.0088  -0.0655 -0.3930 283 HIS C CD2 
10747 C CE1 . HIS C 283 ? 0.9643 0.7713 3.0564 0.0375  -0.0530 -0.4282 283 HIS C CE1 
10748 N NE2 . HIS C 283 ? 0.9624 0.7804 3.0467 0.0243  -0.0548 -0.3964 283 HIS C NE2 
10749 N N   . SER C 284 ? 0.9101 0.6303 3.1737 -0.0310 -0.0795 -0.3124 284 SER C N   
10750 C CA  . SER C 284 ? 0.8890 0.5912 3.1751 -0.0349 -0.0744 -0.2619 284 SER C CA  
10751 C C   . SER C 284 ? 0.8390 0.5423 3.0921 -0.0162 -0.0612 -0.2395 284 SER C C   
10752 O O   . SER C 284 ? 0.8083 0.5324 3.0166 -0.0028 -0.0552 -0.2578 284 SER C O   
10753 C CB  . SER C 284 ? 0.8759 0.6014 3.1566 -0.0509 -0.0749 -0.2313 284 SER C CB  
10754 O OG  . SER C 284 ? 0.8850 0.5904 3.2034 -0.0595 -0.0733 -0.1878 284 SER C OG  
10755 N N   . LEU C 285 ? 0.8252 0.5049 3.1050 -0.0154 -0.0576 -0.2012 285 LEU C N   
10756 C CA  . LEU C 285 ? 0.7940 0.4737 3.0487 0.0005  -0.0467 -0.1757 285 LEU C CA  
10757 C C   . LEU C 285 ? 0.7669 0.4766 2.9801 -0.0020 -0.0383 -0.1378 285 LEU C C   
10758 O O   . LEU C 285 ? 0.7549 0.4805 2.9258 0.0109  -0.0293 -0.1281 285 LEU C O   
10759 C CB  . LEU C 285 ? 0.8062 0.4476 3.1106 0.0033  -0.0480 -0.1532 285 LEU C CB  
10760 C CG  . LEU C 285 ? 0.8375 0.4430 3.1924 0.0066  -0.0564 -0.1878 285 LEU C CG  
10761 C CD1 . LEU C 285 ? 0.8570 0.4275 3.2610 0.0083  -0.0572 -0.1539 285 LEU C CD1 
10762 C CD2 . LEU C 285 ? 0.8329 0.4426 3.1648 0.0246  -0.0535 -0.2295 285 LEU C CD2 
10763 N N   . ASN C 286 ? 0.7655 0.4841 2.9921 -0.0185 -0.0414 -0.1179 286 ASN C N   
10764 C CA  . ASN C 286 ? 0.7372 0.4825 2.9311 -0.0209 -0.0332 -0.0804 286 ASN C CA  
10765 C C   . ASN C 286 ? 0.7152 0.4948 2.8799 -0.0288 -0.0345 -0.0935 286 ASN C C   
10766 O O   . ASN C 286 ? 0.6791 0.4785 2.8349 -0.0366 -0.0309 -0.0655 286 ASN C O   
10767 C CB  . ASN C 286 ? 0.7517 0.4843 2.9831 -0.0315 -0.0329 -0.0378 286 ASN C CB  
10768 C CG  . ASN C 286 ? 0.7773 0.5007 3.0576 -0.0510 -0.0430 -0.0438 286 ASN C CG  
10769 O OD1 . ASN C 286 ? 0.7945 0.5136 3.0874 -0.0556 -0.0520 -0.0840 286 ASN C OD1 
10770 N ND2 . ASN C 286 ? 0.7842 0.5063 3.0934 -0.0630 -0.0418 -0.0049 286 ASN C ND2 
10771 N N   . GLN C 287 ? 0.7285 0.5169 2.8780 -0.0257 -0.0393 -0.1358 287 GLN C N   
10772 C CA  . GLN C 287 ? 0.7213 0.5443 2.8402 -0.0309 -0.0414 -0.1504 287 GLN C CA  
10773 C C   . GLN C 287 ? 0.6941 0.5394 2.7581 -0.0153 -0.0344 -0.1657 287 GLN C C   
10774 O O   . GLN C 287 ? 0.6887 0.5342 2.7449 -0.0085 -0.0374 -0.2018 287 GLN C O   
10775 C CB  . GLN C 287 ? 0.7528 0.5727 2.9040 -0.0440 -0.0550 -0.1852 287 GLN C CB  
10776 C CG  . GLN C 287 ? 0.7658 0.5720 2.9701 -0.0630 -0.0623 -0.1675 287 GLN C CG  
10777 C CD  . GLN C 287 ? 0.7376 0.5712 2.9305 -0.0720 -0.0577 -0.1320 287 GLN C CD  
10778 O OE1 . GLN C 287 ? 0.7277 0.5535 2.9367 -0.0753 -0.0518 -0.0926 287 GLN C OE1 
10779 N NE2 . GLN C 287 ? 0.7248 0.5928 2.8897 -0.0753 -0.0602 -0.1451 287 GLN C NE2 
10780 N N   . PRO C 288 ? 0.6683 0.5343 2.6933 -0.0091 -0.0247 -0.1383 288 PRO C N   
10781 C CA  . PRO C 288 ? 0.6522 0.5403 2.6273 0.0042  -0.0181 -0.1485 288 PRO C CA  
10782 C C   . PRO C 288 ? 0.6628 0.5742 2.6201 0.0029  -0.0240 -0.1843 288 PRO C C   
10783 O O   . PRO C 288 ? 0.6819 0.5983 2.6189 0.0137  -0.0220 -0.2082 288 PRO C O   
10784 C CB  . PRO C 288 ? 0.6188 0.5263 2.5658 0.0050  -0.0099 -0.1131 288 PRO C CB  
10785 C CG  . PRO C 288 ? 0.6251 0.5119 2.6040 -0.0006 -0.0084 -0.0814 288 PRO C CG  
10786 C CD  . PRO C 288 ? 0.6565 0.5258 2.6847 -0.0142 -0.0192 -0.0960 288 PRO C CD  
10787 N N   . GLU C 289 ? 0.6626 0.5904 2.6292 -0.0103 -0.0314 -0.1877 289 GLU C N   
10788 C CA  . GLU C 289 ? 0.6583 0.6165 2.6019 -0.0117 -0.0372 -0.2156 289 GLU C CA  
10789 C C   . GLU C 289 ? 0.6910 0.6401 2.6469 -0.0096 -0.0446 -0.2592 289 GLU C C   
10790 O O   . GLU C 289 ? 0.6865 0.6622 2.6182 -0.0076 -0.0485 -0.2864 289 GLU C O   
10791 C CB  . GLU C 289 ? 0.6531 0.6298 2.6111 -0.0272 -0.0450 -0.2089 289 GLU C CB  
10792 C CG  . GLU C 289 ? 0.6144 0.6093 2.5524 -0.0270 -0.0368 -0.1706 289 GLU C CG  
10793 C CD  . GLU C 289 ? 0.5877 0.6110 2.4746 -0.0149 -0.0298 -0.1686 289 GLU C CD  
10794 O OE1 . GLU C 289 ? 0.5912 0.6381 2.4599 -0.0142 -0.0355 -0.1937 289 GLU C OE1 
10795 O OE2 . GLU C 289 ? 0.5644 0.5874 2.4303 -0.0065 -0.0192 -0.1416 289 GLU C OE2 
10796 N N   . GLU C 290 ? 0.7145 0.6274 2.7084 -0.0093 -0.0464 -0.2654 290 GLU C N   
10797 C CA  . GLU C 290 ? 0.7635 0.6638 2.7754 -0.0067 -0.0534 -0.3082 290 GLU C CA  
10798 C C   . GLU C 290 ? 0.7697 0.6654 2.7593 0.0119  -0.0440 -0.3188 290 GLU C C   
10799 O O   . GLU C 290 ? 0.7910 0.6708 2.7997 0.0172  -0.0473 -0.3514 290 GLU C O   
10800 C CB  . GLU C 290 ? 0.8050 0.6671 2.8777 -0.0176 -0.0621 -0.3117 290 GLU C CB  
10801 C CG  . GLU C 290 ? 0.8196 0.6869 2.9226 -0.0375 -0.0747 -0.3161 290 GLU C CG  
10802 C CD  . GLU C 290 ? 0.8670 0.6965 3.0324 -0.0477 -0.0855 -0.3327 290 GLU C CD  
10803 O OE1 . GLU C 290 ? 0.8808 0.6785 3.0660 -0.0380 -0.0821 -0.3359 290 GLU C OE1 
10804 O OE2 . GLU C 290 ? 0.8915 0.7221 3.0888 -0.0649 -0.0977 -0.3427 290 GLU C OE2 
10805 N N   . TRP C 291 ? 0.7478 0.6576 2.6995 0.0221  -0.0324 -0.2931 291 TRP C N   
10806 C CA  . TRP C 291 ? 0.7384 0.6456 2.6721 0.0390  -0.0233 -0.3008 291 TRP C CA  
10807 C C   . TRP C 291 ? 0.7002 0.6408 2.5812 0.0476  -0.0140 -0.2885 291 TRP C C   
10808 O O   . TRP C 291 ? 0.6996 0.6364 2.5667 0.0594  -0.0047 -0.2764 291 TRP C O   
10809 C CB  . TRP C 291 ? 0.7355 0.6080 2.6961 0.0443  -0.0186 -0.2768 291 TRP C CB  
10810 C CG  . TRP C 291 ? 0.7713 0.6070 2.7875 0.0383  -0.0268 -0.2867 291 TRP C CG  
10811 C CD1 . TRP C 291 ? 0.7789 0.5979 2.8309 0.0233  -0.0341 -0.2704 291 TRP C CD1 
10812 C CD2 . TRP C 291 ? 0.8028 0.6126 2.8485 0.0475  -0.0282 -0.3126 291 TRP C CD2 
10813 N NE1 . TRP C 291 ? 0.8155 0.5990 2.9181 0.0216  -0.0405 -0.2837 291 TRP C NE1 
10814 C CE2 . TRP C 291 ? 0.8271 0.6033 2.9273 0.0368  -0.0372 -0.3103 291 TRP C CE2 
10815 C CE3 . TRP C 291 ? 0.8104 0.6231 2.8445 0.0638  -0.0225 -0.3371 291 TRP C CE3 
10816 C CZ2 . TRP C 291 ? 0.8544 0.5976 2.9976 0.0425  -0.0412 -0.3323 291 TRP C CZ2 
10817 C CZ3 . TRP C 291 ? 0.8348 0.6170 2.9103 0.0702  -0.0258 -0.3599 291 TRP C CZ3 
10818 C CH2 . TRP C 291 ? 0.8543 0.6009 2.9841 0.0599  -0.0353 -0.3576 291 TRP C CH2 
10819 N N   . PHE C 292 ? 0.6669 0.6404 2.5214 0.0419  -0.0170 -0.2923 292 PHE C N   
10820 C CA  . PHE C 292 ? 0.6210 0.6263 2.4289 0.0491  -0.0090 -0.2796 292 PHE C CA  
10821 C C   . PHE C 292 ? 0.6259 0.6557 2.4077 0.0589  -0.0066 -0.3104 292 PHE C C   
10822 O O   . PHE C 292 ? 0.6074 0.6639 2.3523 0.0657  0.0005  -0.3008 292 PHE C O   
10823 C CB  . PHE C 292 ? 0.6011 0.6306 2.3945 0.0393  -0.0129 -0.2635 292 PHE C CB  
10824 C CG  . PHE C 292 ? 0.5632 0.5846 2.3549 0.0376  -0.0070 -0.2223 292 PHE C CG  
10825 C CD1 . PHE C 292 ? 0.5337 0.5626 2.2951 0.0477  0.0034  -0.2011 292 PHE C CD1 
10826 C CD2 . PHE C 292 ? 0.5540 0.5612 2.3753 0.0260  -0.0117 -0.2057 292 PHE C CD2 
10827 C CE1 . PHE C 292 ? 0.5072 0.5290 2.2664 0.0469  0.0085  -0.1670 292 PHE C CE1 
10828 C CE2 . PHE C 292 ? 0.5293 0.5319 2.3473 0.0257  -0.0054 -0.1696 292 PHE C CE2 
10829 C CZ  . PHE C 292 ? 0.5087 0.5183 2.2948 0.0365  0.0044  -0.1517 292 PHE C CZ  
10830 N N   . GLY C 293 ? 0.6544 0.6758 2.4563 0.0602  -0.0120 -0.3472 293 GLY C N   
10831 C CA  . GLY C 293 ? 0.6629 0.7115 2.4411 0.0691  -0.0101 -0.3804 293 GLY C CA  
10832 C C   . GLY C 293 ? 0.6417 0.6933 2.4017 0.0847  0.0030  -0.3750 293 GLY C C   
10833 O O   . GLY C 293 ? 0.6220 0.6461 2.3988 0.0892  0.0084  -0.3554 293 GLY C O   
10834 N N   . PHE C 294 ? 0.6398 0.7287 2.3652 0.0922  0.0078  -0.3906 294 PHE C N   
10835 C CA  . PHE C 294 ? 0.6372 0.7353 2.3483 0.1070  0.0196  -0.3953 294 PHE C CA  
10836 C C   . PHE C 294 ? 0.6761 0.7625 2.4115 0.1140  0.0180  -0.4366 294 PHE C C   
10837 O O   . PHE C 294 ? 0.6756 0.7543 2.4177 0.1262  0.0267  -0.4411 294 PHE C O   
10838 C CB  . PHE C 294 ? 0.6247 0.7701 2.2903 0.1116  0.0260  -0.3926 294 PHE C CB  
10839 C CG  . PHE C 294 ? 0.5846 0.7409 2.2266 0.1082  0.0299  -0.3513 294 PHE C CG  
10840 C CD1 . PHE C 294 ? 0.5608 0.6898 2.2186 0.1002  0.0268  -0.3218 294 PHE C CD1 
10841 C CD2 . PHE C 294 ? 0.5693 0.7646 2.1740 0.1130  0.0368  -0.3424 294 PHE C CD2 
10842 C CE1 . PHE C 294 ? 0.5264 0.6651 2.1635 0.0984  0.0307  -0.2874 294 PHE C CE1 
10843 C CE2 . PHE C 294 ? 0.5385 0.7408 2.1253 0.1104  0.0400  -0.3060 294 PHE C CE2 
10844 C CZ  . PHE C 294 ? 0.5188 0.6923 2.1218 0.1035  0.0369  -0.2802 294 PHE C CZ  
10845 N N   . TRP C 295 ? 0.7088 0.7937 2.4596 0.1062  0.0062  -0.4676 295 TRP C N   
10846 C CA  . TRP C 295 ? 0.7451 0.8107 2.5276 0.1113  0.0023  -0.5082 295 TRP C CA  
10847 C C   . TRP C 295 ? 0.7556 0.7737 2.5880 0.1010  -0.0077 -0.5035 295 TRP C C   
10848 O O   . TRP C 295 ? 0.7449 0.7566 2.5827 0.0872  -0.0146 -0.4804 295 TRP C O   
10849 C CB  . TRP C 295 ? 0.7742 0.8738 2.5395 0.1108  -0.0041 -0.5522 295 TRP C CB  
10850 C CG  . TRP C 295 ? 0.7729 0.9216 2.4917 0.1223  0.0065  -0.5599 295 TRP C CG  
10851 C CD1 . TRP C 295 ? 0.7399 0.9207 2.4190 0.1234  0.0143  -0.5279 295 TRP C CD1 
10852 C CD2 . TRP C 295 ? 0.8057 0.9778 2.5152 0.1349  0.0108  -0.6029 295 TRP C CD2 
10853 N NE1 . TRP C 295 ? 0.7522 0.9754 2.3985 0.1346  0.0230  -0.5458 295 TRP C NE1 
10854 C CE2 . TRP C 295 ? 0.7926 1.0133 2.4552 0.1423  0.0217  -0.5920 295 TRP C CE2 
10855 C CE3 . TRP C 295 ? 0.8470 1.0043 2.5845 0.1410  0.0069  -0.6498 295 TRP C CE3 
10856 C CZ2 . TRP C 295 ? 0.8188 1.0763 2.4601 0.1554  0.0293  -0.6251 295 TRP C CZ2 
10857 C CZ3 . TRP C 295 ? 0.8726 1.0651 2.5888 0.1550  0.0144  -0.6854 295 TRP C CZ3 
10858 C CH2 . TRP C 295 ? 0.8581 1.1018 2.5256 0.1620  0.0258  -0.6726 295 TRP C CH2 
10859 N N   . GLY C 296 ? 0.7826 0.7685 2.6531 0.1081  -0.0080 -0.5241 296 GLY C N   
10860 C CA  . GLY C 296 ? 0.8045 0.7451 2.7276 0.0987  -0.0182 -0.5242 296 GLY C CA  
10861 C C   . GLY C 296 ? 0.8545 0.7839 2.8078 0.0989  -0.0278 -0.5764 296 GLY C C   
10862 O O   . GLY C 296 ? 0.8684 0.8234 2.8023 0.1095  -0.0247 -0.6136 296 GLY C O   
10863 N N   . TYR C 297 ? 0.8836 0.7751 2.8857 0.0870  -0.0396 -0.5790 297 TYR C N   
10864 C CA  . TYR C 297 ? 0.9373 0.8139 2.9737 0.0843  -0.0511 -0.6284 297 TYR C CA  
10865 C C   . TYR C 297 ? 0.9523 0.7754 3.0482 0.0887  -0.0526 -0.6286 297 TYR C C   
10866 O O   . TYR C 297 ? 0.9390 0.7313 3.0650 0.0795  -0.0552 -0.5910 297 TYR C O   
10867 C CB  . TYR C 297 ? 0.9563 0.8430 2.9966 0.0639  -0.0660 -0.6352 297 TYR C CB  
10868 C CG  . TYR C 297 ? 0.9544 0.8967 2.9381 0.0614  -0.0662 -0.6420 297 TYR C CG  
10869 C CD1 . TYR C 297 ? 0.9883 0.9653 2.9427 0.0713  -0.0654 -0.6865 297 TYR C CD1 
10870 C CD2 . TYR C 297 ? 0.9173 0.8795 2.8777 0.0496  -0.0674 -0.6045 297 TYR C CD2 
10871 C CE1 . TYR C 297 ? 0.9762 1.0061 2.8795 0.0695  -0.0658 -0.6904 297 TYR C CE1 
10872 C CE2 . TYR C 297 ? 0.9087 0.9214 2.8204 0.0482  -0.0680 -0.6091 297 TYR C CE2 
10873 C CZ  . TYR C 297 ? 0.9326 0.9796 2.8155 0.0578  -0.0675 -0.6508 297 TYR C CZ  
10874 O OH  . TYR C 297 ? 0.9178 1.0168 2.7528 0.0571  -0.0684 -0.6547 297 TYR C OH  
10875 N N   . SER C 298 ? 0.9811 0.7958 3.0938 0.1034  -0.0508 -0.6710 298 SER C N   
10876 C CA  . SER C 298 ? 0.9946 0.7625 3.1609 0.1130  -0.0499 -0.6740 298 SER C CA  
10877 C C   . SER C 298 ? 1.0069 0.7284 3.2330 0.0965  -0.0640 -0.6655 298 SER C C   
10878 O O   . SER C 298 ? 0.9976 0.6820 3.2614 0.0972  -0.0626 -0.6327 298 SER C O   
10879 C CB  . SER C 298 ? 1.0367 0.8059 3.2138 0.1297  -0.0481 -0.7302 298 SER C CB  
10880 O OG  . SER C 298 ? 1.0307 0.8518 3.1506 0.1417  -0.0376 -0.7487 298 SER C OG  
10881 N N   . ASP C 299 ? 1.0295 0.7557 3.2652 0.0822  -0.0777 -0.6977 299 ASP C N   
10882 C CA  . ASP C 299 ? 1.0509 0.7372 3.3456 0.0644  -0.0928 -0.6979 299 ASP C CA  
10883 C C   . ASP C 299 ? 1.0566 0.7713 3.3338 0.0457  -0.1052 -0.7160 299 ASP C C   
10884 O O   . ASP C 299 ? 1.0307 0.7937 3.2497 0.0465  -0.1009 -0.7157 299 ASP C O   
10885 C CB  . ASP C 299 ? 1.0985 0.7426 3.4510 0.0736  -0.0979 -0.7367 299 ASP C CB  
10886 C CG  . ASP C 299 ? 1.1365 0.8026 3.4712 0.0876  -0.0977 -0.8015 299 ASP C CG  
10887 O OD1 . ASP C 299 ? 1.1503 0.8471 3.4608 0.0782  -0.1064 -0.8341 299 ASP C OD1 
10888 O OD2 . ASP C 299 ? 1.1559 0.8107 3.5016 0.1082  -0.0890 -0.8192 299 ASP C OD2 
10889 N N   . LEU C 300 ? 1.0872 0.7725 3.4175 0.0286  -0.1212 -0.7307 300 LEU C N   
10890 C CA  . LEU C 300 ? 1.0924 0.8022 3.4150 0.0094  -0.1352 -0.7485 300 LEU C CA  
10891 C C   . LEU C 300 ? 1.1195 0.8614 3.4146 0.0169  -0.1403 -0.8126 300 LEU C C   
10892 O O   . LEU C 300 ? 1.1076 0.8939 3.3622 0.0090  -0.1454 -0.8232 300 LEU C O   
10893 C CB  . LEU C 300 ? 1.1239 0.7887 3.5188 -0.0105 -0.1502 -0.7428 300 LEU C CB  
10894 C CG  . LEU C 300 ? 1.1435 0.8252 3.5481 -0.0338 -0.1676 -0.7605 300 LEU C CG  
10895 C CD1 . LEU C 300 ? 1.1062 0.8446 3.4468 -0.0388 -0.1644 -0.7409 300 LEU C CD1 
10896 C CD2 . LEU C 300 ? 1.1519 0.7922 3.6233 -0.0544 -0.1771 -0.7289 300 LEU C CD2 
10897 N N   . ASN C 301 ? 1.1516 0.8742 3.4662 0.0335  -0.1380 -0.8543 301 ASN C N   
10898 C CA  . ASN C 301 ? 1.1885 0.9395 3.4820 0.0413  -0.1431 -0.9196 301 ASN C CA  
10899 C C   . ASN C 301 ? 1.1652 0.9645 3.3908 0.0625  -0.1260 -0.9244 301 ASN C C   
10900 O O   . ASN C 301 ? 1.1911 1.0104 3.4013 0.0758  -0.1250 -0.9768 301 ASN C O   
10901 C CB  . ASN C 301 ? 1.2450 0.9510 3.5994 0.0473  -0.1512 -0.9690 301 ASN C CB  
10902 C CG  . ASN C 301 ? 1.2667 0.9288 3.6896 0.0245  -0.1701 -0.9709 301 ASN C CG  
10903 O OD1 . ASN C 301 ? 1.2624 0.9442 3.6801 0.0043  -0.1834 -0.9737 301 ASN C OD1 
10904 N ND2 . ASN C 301 ? 1.2881 0.8916 3.7779 0.0272  -0.1720 -0.9675 301 ASN C ND2 
10905 N N   . ASP C 302 ? 1.1166 0.9372 3.3012 0.0650  -0.1127 -0.8707 302 ASP C N   
10906 C CA  . ASP C 302 ? 1.0954 0.9633 3.2168 0.0827  -0.0967 -0.8696 302 ASP C CA  
10907 C C   . ASP C 302 ? 1.1048 1.0297 3.1763 0.0770  -0.1031 -0.8972 302 ASP C C   
10908 O O   . ASP C 302 ? 1.1560 1.0931 3.2295 0.0806  -0.1108 -0.9543 302 ASP C O   
10909 C CB  . ASP C 302 ? 1.0398 0.9083 3.1393 0.0878  -0.0814 -0.8077 302 ASP C CB  
10910 C CG  . ASP C 302 ? 1.0209 0.9303 3.0663 0.1074  -0.0637 -0.8054 302 ASP C CG  
10911 O OD1 . ASP C 302 ? 1.0391 0.9905 3.0489 0.1143  -0.0630 -0.8448 302 ASP C OD1 
10912 O OD2 . ASP C 302 ? 0.9862 0.8868 3.0258 0.1158  -0.0509 -0.7646 302 ASP C OD2 
10913 N N   . LYS C 303 ? 1.0605 1.0200 3.0889 0.0687  -0.1005 -0.8578 303 LYS C N   
10914 C CA  . LYS C 303 ? 1.0659 1.0819 3.0460 0.0632  -0.1068 -0.8758 303 LYS C CA  
10915 C C   . LYS C 303 ? 1.0458 1.1117 2.9616 0.0793  -0.0898 -0.8629 303 LYS C C   
10916 O O   . LYS C 303 ? 1.0392 1.1560 2.9092 0.0759  -0.0925 -0.8653 303 LYS C O   
10917 C CB  . LYS C 303 ? 1.1205 1.1473 3.1124 0.0601  -0.1222 -0.9426 303 LYS C CB  
10918 C CG  . LYS C 303 ? 1.1458 1.1331 3.1980 0.0398  -0.1429 -0.9598 303 LYS C CG  
10919 C CD  . LYS C 303 ? 1.1249 1.1354 3.1673 0.0180  -0.1559 -0.9369 303 LYS C CD  
10920 C CE  . LYS C 303 ? 1.1285 1.0936 3.2337 -0.0031 -0.1699 -0.9219 303 LYS C CE  
10921 N NZ  . LYS C 303 ? 1.1835 1.1344 3.3301 -0.0141 -0.1899 -0.9775 303 LYS C NZ  
10922 N N   . TYR C 304 ? 1.0383 1.0912 2.9526 0.0963  -0.0729 -0.8474 304 TYR C N   
10923 C CA  . TYR C 304 ? 1.0208 1.1190 2.8803 0.1119  -0.0561 -0.8363 304 TYR C CA  
10924 C C   . TYR C 304 ? 0.9767 1.0598 2.8310 0.1151  -0.0426 -0.7768 304 TYR C C   
10925 O O   . TYR C 304 ? 0.9416 1.0552 2.7563 0.1119  -0.0374 -0.7410 304 TYR C O   
10926 C CB  . TYR C 304 ? 1.0531 1.1604 2.9121 0.1317  -0.0482 -0.8844 304 TYR C CB  
10927 C CG  . TYR C 304 ? 1.1035 1.2252 2.9683 0.1298  -0.0617 -0.9484 304 TYR C CG  
10928 C CD1 . TYR C 304 ? 1.1167 1.2990 2.9311 0.1290  -0.0651 -0.9711 304 TYR C CD1 
10929 C CD2 . TYR C 304 ? 1.1442 1.2193 3.0660 0.1290  -0.0718 -0.9867 304 TYR C CD2 
10930 C CE1 . TYR C 304 ? 1.1689 1.3667 2.9871 0.1272  -0.0785 -1.0317 304 TYR C CE1 
10931 C CE2 . TYR C 304 ? 1.1955 1.2822 3.1245 0.1272  -0.0851 -1.0484 304 TYR C CE2 
10932 C CZ  . TYR C 304 ? 1.2077 1.3569 3.0835 0.1262  -0.0887 -1.0720 304 TYR C CZ  
10933 O OH  . TYR C 304 ? 1.2603 1.4222 3.1428 0.1244  -0.1027 -1.1350 304 TYR C OH  
10934 N N   . GLY C 305 ? 0.9809 1.0173 2.8764 0.1221  -0.0374 -0.7674 305 GLY C N   
10935 C CA  . GLY C 305 ? 0.9415 0.9598 2.8376 0.1250  -0.0263 -0.7141 305 GLY C CA  
10936 C C   . GLY C 305 ? 0.9325 0.9751 2.8000 0.1447  -0.0083 -0.7105 305 GLY C C   
10937 O O   . GLY C 305 ? 0.9561 1.0285 2.8056 0.1566  -0.0038 -0.7497 305 GLY C O   
10938 N N   . THR C 306 ? 0.8999 0.9303 2.7649 0.1477  0.0015  -0.6635 306 THR C N   
10939 C CA  . THR C 306 ? 0.8843 0.9415 2.7191 0.1629  0.0182  -0.6489 306 THR C CA  
10940 C C   . THR C 306 ? 0.8390 0.9083 2.6443 0.1558  0.0230  -0.5957 306 THR C C   
10941 O O   . THR C 306 ? 0.8275 0.8770 2.6429 0.1413  0.0144  -0.5701 306 THR C O   
10942 C CB  . THR C 306 ? 0.8891 0.9134 2.7615 0.1771  0.0255  -0.6508 306 THR C CB  
10943 O OG1 . THR C 306 ? 0.8638 0.8484 2.7623 0.1684  0.0218  -0.6082 306 THR C OG1 
10944 C CG2 . THR C 306 ? 0.9356 0.9392 2.8461 0.1841  0.0196  -0.7024 306 THR C CG2 
10945 N N   . PRO C 307 ? 0.8195 0.9215 2.5895 0.1654  0.0368  -0.5778 307 PRO C N   
10946 C CA  . PRO C 307 ? 0.7714 0.8818 2.5166 0.1597  0.0415  -0.5287 307 PRO C CA  
10947 C C   . PRO C 307 ? 0.7458 0.8251 2.5116 0.1642  0.0478  -0.4942 307 PRO C C   
10948 O O   . PRO C 307 ? 0.7613 0.8420 2.5340 0.1779  0.0576  -0.4993 307 PRO C O   
10949 C CB  . PRO C 307 ? 0.7694 0.9343 2.4678 0.1674  0.0520  -0.5319 307 PRO C CB  
10950 C CG  . PRO C 307 ? 0.8082 0.9867 2.5132 0.1827  0.0586  -0.5747 307 PRO C CG  
10951 C CD  . PRO C 307 ? 0.8394 0.9742 2.5923 0.1822  0.0487  -0.6046 307 PRO C CD  
10952 N N   . ARG C 308 ? 0.7226 0.7778 2.4966 0.1528  0.0425  -0.4587 308 ARG C N   
10953 C CA  . ARG C 308 ? 0.7033 0.7328 2.4918 0.1552  0.0470  -0.4222 308 ARG C CA  
10954 C C   . ARG C 308 ? 0.6858 0.7444 2.4419 0.1632  0.0595  -0.4011 308 ARG C C   
10955 O O   . ARG C 308 ? 0.6820 0.7801 2.4058 0.1665  0.0650  -0.4125 308 ARG C O   
10956 C CB  . ARG C 308 ? 0.6874 0.6952 2.4833 0.1402  0.0386  -0.3916 308 ARG C CB  
10957 C CG  . ARG C 308 ? 0.7118 0.6896 2.5448 0.1305  0.0261  -0.4076 308 ARG C CG  
10958 C CD  . ARG C 308 ? 0.6908 0.6509 2.5321 0.1161  0.0194  -0.3745 308 ARG C CD  
10959 N NE  . ARG C 308 ? 0.7124 0.6404 2.5971 0.1071  0.0084  -0.3867 308 ARG C NE  
10960 C CZ  . ARG C 308 ? 0.7174 0.6446 2.6092 0.0922  -0.0014 -0.3863 308 ARG C CZ  
10961 N NH1 . ARG C 308 ? 0.6971 0.6516 2.5559 0.0850  -0.0013 -0.3690 308 ARG C NH1 
10962 N NH2 . ARG C 308 ? 0.7405 0.6390 2.6756 0.0845  -0.0114 -0.4019 308 ARG C NH2 
10963 N N   . PRO C 309 ? 0.6756 0.7177 2.4399 0.1664  0.0642  -0.3693 309 PRO C N   
10964 C CA  . PRO C 309 ? 0.6558 0.7236 2.3944 0.1731  0.0753  -0.3497 309 PRO C CA  
10965 C C   . PRO C 309 ? 0.6420 0.7332 2.3439 0.1643  0.0759  -0.3251 309 PRO C C   
10966 O O   . PRO C 309 ? 0.6549 0.7727 2.3328 0.1683  0.0845  -0.3118 309 PRO C O   
10967 C CB  . PRO C 309 ? 0.6401 0.6789 2.4038 0.1774  0.0767  -0.3248 309 PRO C CB  
10968 C CG  . PRO C 309 ? 0.6628 0.6636 2.4679 0.1768  0.0683  -0.3383 309 PRO C CG  
10969 C CD  . PRO C 309 ? 0.6770 0.6765 2.4776 0.1643  0.0590  -0.3512 309 PRO C CD  
10970 N N   . VAL C 310 ? 0.6302 0.7112 2.3305 0.1521  0.0668  -0.3172 310 VAL C N   
10971 C CA  . VAL C 310 ? 0.6083 0.7130 2.2758 0.1447  0.0668  -0.2977 310 VAL C CA  
10972 C C   . VAL C 310 ? 0.6068 0.7549 2.2449 0.1485  0.0714  -0.3168 310 VAL C C   
10973 O O   . VAL C 310 ? 0.6007 0.7753 2.2123 0.1502  0.0782  -0.2993 310 VAL C O   
10974 C CB  . VAL C 310 ? 0.6199 0.7104 2.2940 0.1318  0.0560  -0.2923 310 VAL C CB  
10975 C CG1 . VAL C 310 ? 0.6189 0.7371 2.2606 0.1255  0.0556  -0.2754 310 VAL C CG1 
10976 C CG2 . VAL C 310 ? 0.6111 0.6635 2.3115 0.1276  0.0524  -0.2691 310 VAL C CG2 
10977 N N   . TRP C 311 ? 0.6268 0.7826 2.2705 0.1493  0.0668  -0.3525 311 TRP C N   
10978 C CA  . TRP C 311 ? 0.6382 0.8376 2.2538 0.1526  0.0694  -0.3751 311 TRP C CA  
10979 C C   . TRP C 311 ? 0.6247 0.8557 2.2179 0.1625  0.0831  -0.3652 311 TRP C C   
10980 O O   . TRP C 311 ? 0.6297 0.8982 2.1911 0.1613  0.0862  -0.3572 311 TRP C O   
10981 C CB  . TRP C 311 ? 0.6761 0.8716 2.3104 0.1569  0.0651  -0.4204 311 TRP C CB  
10982 C CG  . TRP C 311 ? 0.7029 0.9439 2.3097 0.1602  0.0659  -0.4507 311 TRP C CG  
10983 C CD1 . TRP C 311 ? 0.7213 0.9909 2.3179 0.1730  0.0756  -0.4757 311 TRP C CD1 
10984 C CD2 . TRP C 311 ? 0.7111 0.9764 2.2975 0.1508  0.0562  -0.4602 311 TRP C CD2 
10985 N NE1 . TRP C 311 ? 0.7460 1.0572 2.3148 0.1724  0.0728  -0.5000 311 TRP C NE1 
10986 C CE2 . TRP C 311 ? 0.7395 1.0489 2.3018 0.1587  0.0603  -0.4911 311 TRP C CE2 
10987 C CE3 . TRP C 311 ? 0.6982 0.9550 2.2851 0.1371  0.0446  -0.4456 311 TRP C CE3 
10988 C CZ2 . TRP C 311 ? 0.7540 1.0990 2.2913 0.1530  0.0521  -0.5071 311 TRP C CZ2 
10989 C CZ3 . TRP C 311 ? 0.7173 1.0085 2.2821 0.1314  0.0366  -0.4612 311 TRP C CZ3 
10990 C CH2 . TRP C 311 ? 0.7438 1.0782 2.2837 0.1391  0.0397  -0.4917 311 TRP C CH2 
10991 N N   . PHE C 312 ? 0.6171 0.8340 2.2296 0.1722  0.0908  -0.3657 312 PHE C N   
10992 C CA  . PHE C 312 ? 0.6105 0.8581 2.2097 0.1830  0.1043  -0.3637 312 PHE C CA  
10993 C C   . PHE C 312 ? 0.5807 0.8316 2.1669 0.1796  0.1094  -0.3214 312 PHE C C   
10994 O O   . PHE C 312 ? 0.5789 0.8654 2.1434 0.1832  0.1188  -0.3114 312 PHE C O   
10995 C CB  . PHE C 312 ? 0.6145 0.8479 2.2431 0.1955  0.1101  -0.3833 312 PHE C CB  
10996 C CG  . PHE C 312 ? 0.6445 0.8779 2.2875 0.2021  0.1074  -0.4296 312 PHE C CG  
10997 C CD1 . PHE C 312 ? 0.6637 0.9402 2.2876 0.2113  0.1154  -0.4583 312 PHE C CD1 
10998 C CD2 . PHE C 312 ? 0.6568 0.8478 2.3338 0.1990  0.0967  -0.4450 312 PHE C CD2 
10999 C CE1 . PHE C 312 ? 0.6990 0.9752 2.3360 0.2177  0.1124  -0.5039 312 PHE C CE1 
11000 C CE2 . PHE C 312 ? 0.6888 0.8771 2.3820 0.2045  0.0932  -0.4892 312 PHE C CE2 
11001 C CZ  . PHE C 312 ? 0.7122 0.9428 2.3848 0.2141  0.1008  -0.5201 312 PHE C CZ  
11002 N N   . ALA C 313 ? 0.5576 0.7722 2.1585 0.1727  0.1032  -0.2969 313 ALA C N   
11003 C CA  . ALA C 313 ? 0.5287 0.7437 2.1179 0.1687  0.1062  -0.2596 313 ALA C CA  
11004 C C   . ALA C 313 ? 0.5399 0.7848 2.0974 0.1623  0.1055  -0.2486 313 ALA C C   
11005 O O   . ALA C 313 ? 0.5320 0.8025 2.0719 0.1638  0.1131  -0.2304 313 ALA C O   
11006 C CB  . ALA C 313 ? 0.5041 0.6776 2.1124 0.1627  0.0990  -0.2393 313 ALA C CB  
11007 N N   . MET C 314 ? 0.5644 0.8068 2.1180 0.1553  0.0959  -0.2600 314 MET C N   
11008 C CA  . MET C 314 ? 0.5744 0.8422 2.1018 0.1487  0.0924  -0.2495 314 MET C CA  
11009 C C   . MET C 314 ? 0.5841 0.9003 2.0858 0.1544  0.1001  -0.2589 314 MET C C   
11010 O O   . MET C 314 ? 0.5734 0.9140 2.0543 0.1532  0.1044  -0.2350 314 MET C O   
11011 C CB  . MET C 314 ? 0.6086 0.8681 2.1411 0.1410  0.0803  -0.2667 314 MET C CB  
11012 C CG  . MET C 314 ? 0.6109 0.8311 2.1632 0.1328  0.0723  -0.2504 314 MET C CG  
11013 S SD  . MET C 314 ? 0.6131 0.8366 2.1487 0.1257  0.0708  -0.2113 314 MET C SD  
11014 C CE  . MET C 314 ? 0.6228 0.8933 2.1292 0.1233  0.0674  -0.2190 314 MET C CE  
11015 N N   . ARG C 315 ? 0.6068 0.9374 2.1108 0.1610  0.1019  -0.2937 315 ARG C N   
11016 C CA  . ARG C 315 ? 0.6306 1.0111 2.1091 0.1673  0.1097  -0.3059 315 ARG C CA  
11017 C C   . ARG C 315 ? 0.6127 1.0122 2.0817 0.1714  0.1222  -0.2766 315 ARG C C   
11018 O O   . ARG C 315 ? 0.6126 1.0505 2.0557 0.1707  0.1265  -0.2617 315 ARG C O   
11019 C CB  . ARG C 315 ? 0.6656 1.0515 2.1550 0.1764  0.1121  -0.3484 315 ARG C CB  
11020 C CG  . ARG C 315 ? 0.6986 1.1398 2.1610 0.1845  0.1209  -0.3666 315 ARG C CG  
11021 C CD  . ARG C 315 ? 0.7326 1.1770 2.2092 0.1959  0.1254  -0.4094 315 ARG C CD  
11022 N NE  . ARG C 315 ? 0.7213 1.1444 2.2242 0.2045  0.1348  -0.4048 315 ARG C NE  
11023 C CZ  . ARG C 315 ? 0.7417 1.1557 2.2674 0.2154  0.1387  -0.4370 315 ARG C CZ  
11024 N NH1 . ARG C 315 ? 0.7735 1.1977 2.2984 0.2196  0.1347  -0.4800 315 ARG C NH1 
11025 N NH2 . ARG C 315 ? 0.7351 1.1302 2.2856 0.2225  0.1463  -0.4268 315 ARG C NH2 
11026 N N   . ASP C 316 ? 0.5978 0.9701 2.0898 0.1751  0.1273  -0.2673 316 ASP C N   
11027 C CA  . ASP C 316 ? 0.5857 0.9733 2.0760 0.1791  0.1389  -0.2437 316 ASP C CA  
11028 C C   . ASP C 316 ? 0.5715 0.9520 2.0538 0.1707  0.1368  -0.2045 316 ASP C C   
11029 O O   . ASP C 316 ? 0.5683 0.9739 2.0401 0.1713  0.1451  -0.1826 316 ASP C O   
11030 C CB  . ASP C 316 ? 0.5728 0.9320 2.0928 0.1850  0.1427  -0.2455 316 ASP C CB  
11031 C CG  . ASP C 316 ? 0.5865 0.9494 2.1214 0.1957  0.1465  -0.2824 316 ASP C CG  
11032 O OD1 . ASP C 316 ? 0.6013 0.9876 2.1225 0.1982  0.1456  -0.3104 316 ASP C OD1 
11033 O OD2 . ASP C 316 ? 0.5771 0.9204 2.1376 0.2018  0.1500  -0.2832 316 ASP C OD2 
11034 N N   . TYR C 317 ? 0.5784 0.9234 2.0686 0.1632  0.1262  -0.1960 317 TYR C N   
11035 C CA  . TYR C 317 ? 0.5747 0.9115 2.0578 0.1558  0.1232  -0.1627 317 TYR C CA  
11036 C C   . TYR C 317 ? 0.6011 0.9736 2.0574 0.1526  0.1220  -0.1545 317 TYR C C   
11037 O O   . TYR C 317 ? 0.6133 0.9930 2.0614 0.1493  0.1237  -0.1251 317 TYR C O   
11038 C CB  . TYR C 317 ? 0.5669 0.8607 2.0647 0.1496  0.1128  -0.1577 317 TYR C CB  
11039 C CG  . TYR C 317 ? 0.5534 0.8365 2.0462 0.1436  0.1105  -0.1251 317 TYR C CG  
11040 C CD1 . TYR C 317 ? 0.5559 0.8535 2.0321 0.1387  0.1058  -0.1147 317 TYR C CD1 
11041 C CD2 . TYR C 317 ? 0.5336 0.7935 2.0390 0.1435  0.1126  -0.1057 317 TYR C CD2 
11042 C CE1 . TYR C 317 ? 0.5466 0.8341 2.0205 0.1347  0.1040  -0.0865 317 TYR C CE1 
11043 C CE2 . TYR C 317 ? 0.5154 0.7651 2.0170 0.1388  0.1104  -0.0793 317 TYR C CE2 
11044 C CZ  . TYR C 317 ? 0.5352 0.7978 2.0217 0.1348  0.1065  -0.0699 317 TYR C CZ  
11045 O OH  . TYR C 317 ? 0.5443 0.7966 2.0289 0.1313  0.1045  -0.0453 317 TYR C OH  
11046 N N   . MET C 318 ? 0.6300 1.0246 2.0741 0.1534  0.1181  -0.1799 318 MET C N   
11047 C CA  . MET C 318 ? 0.6433 1.0711 2.0627 0.1498  0.1142  -0.1727 318 MET C CA  
11048 C C   . MET C 318 ? 0.6421 1.1201 2.0395 0.1547  0.1246  -0.1637 318 MET C C   
11049 O O   . MET C 318 ? 0.6584 1.1677 2.0347 0.1523  0.1222  -0.1516 318 MET C O   
11050 C CB  . MET C 318 ? 0.6730 1.1067 2.0882 0.1477  0.1041  -0.2041 318 MET C CB  
11051 C CG  . MET C 318 ? 0.6672 1.0671 2.0952 0.1393  0.0917  -0.1999 318 MET C CG  
11052 S SD  . MET C 318 ? 0.7116 1.1091 2.1463 0.1358  0.0794  -0.2409 318 MET C SD  
11053 C CE  . MET C 318 ? 0.7283 1.1896 2.1280 0.1391  0.0802  -0.2545 318 MET C CE  
11054 N N   . LYS C 319 ? 0.6214 1.1094 2.0248 0.1615  0.1363  -0.1678 319 LYS C N   
11055 C CA  . LYS C 319 ? 0.6189 1.1584 2.0030 0.1666  0.1477  -0.1618 319 LYS C CA  
11056 C C   . LYS C 319 ? 0.5843 1.1352 1.9618 0.1620  0.1512  -0.1186 319 LYS C C   
11057 O O   . LYS C 319 ? 0.5868 1.1825 1.9428 0.1628  0.1557  -0.1052 319 LYS C O   
11058 C CB  . LYS C 319 ? 0.6255 1.1719 2.0223 0.1753  0.1600  -0.1757 319 LYS C CB  
11059 C CG  . LYS C 319 ? 0.6400 1.1704 2.0506 0.1817  0.1581  -0.2179 319 LYS C CG  
11060 C CD  . LYS C 319 ? 0.6665 1.2185 2.0598 0.1833  0.1516  -0.2524 319 LYS C CD  
11061 C CE  . LYS C 319 ? 0.6882 1.3026 2.0525 0.1893  0.1605  -0.2607 319 LYS C CE  
11062 N NZ  . LYS C 319 ? 0.6984 1.3334 2.0690 0.2007  0.1741  -0.2802 319 LYS C NZ  
11063 N N   . GLY C 320 ? 0.5452 1.0555 1.9427 0.1577  0.1491  -0.0969 320 GLY C N   
11064 C CA  . GLY C 320 ? 0.5306 1.0425 1.9283 0.1531  0.1513  -0.0578 320 GLY C CA  
11065 C C   . GLY C 320 ? 0.5104 0.9739 1.9227 0.1470  0.1413  -0.0456 320 GLY C C   
11066 O O   . GLY C 320 ? 0.4895 0.9162 1.9212 0.1471  0.1397  -0.0538 320 GLY C O   
11067 N N   . LEU C 321 ? 0.5070 0.9740 1.9094 0.1427  0.1346  -0.0269 321 LEU C N   
11068 C CA  . LEU C 321 ? 0.4855 0.9129 1.8987 0.1379  0.1253  -0.0169 321 LEU C CA  
11069 C C   . LEU C 321 ? 0.4706 0.8910 1.8901 0.1351  0.1273  0.0187  321 LEU C C   
11070 O O   . LEU C 321 ? 0.4742 0.9270 1.8832 0.1352  0.1312  0.0389  321 LEU C O   
11071 C CB  . LEU C 321 ? 0.4909 0.9275 1.8913 0.1357  0.1153  -0.0248 321 LEU C CB  
11072 C CG  . LEU C 321 ? 0.4981 0.9316 1.8976 0.1363  0.1098  -0.0610 321 LEU C CG  
11073 C CD1 . LEU C 321 ? 0.5103 0.9650 1.8952 0.1335  0.1003  -0.0652 321 LEU C CD1 
11074 C CD2 . LEU C 321 ? 0.4822 0.8673 1.9038 0.1344  0.1056  -0.0704 321 LEU C CD2 
11075 N N   . ILE C 322 ? 0.4502 0.8287 1.8871 0.1326  0.1238  0.0260  322 ILE C N   
11076 C CA  . ILE C 322 ? 0.4418 0.8076 1.8874 0.1298  0.1237  0.0560  322 ILE C CA  
11077 C C   . ILE C 322 ? 0.4465 0.7930 1.8917 0.1279  0.1143  0.0617  322 ILE C C   
11078 O O   . ILE C 322 ? 0.4262 0.7445 1.8776 0.1272  0.1088  0.0469  322 ILE C O   
11079 C CB  . ILE C 322 ? 0.4202 0.7576 1.8855 0.1289  0.1270  0.0598  322 ILE C CB  
11080 C CG1 . ILE C 322 ? 0.4291 0.7905 1.8965 0.1313  0.1368  0.0546  322 ILE C CG1 
11081 C CG2 . ILE C 322 ? 0.4085 0.7287 1.8851 0.1257  0.1257  0.0875  322 ILE C CG2 
11082 C CD1 . ILE C 322 ? 0.4171 0.7535 1.9022 0.1323  0.1382  0.0423  322 ILE C CD1 
11083 N N   . ILE C 323 ? 0.4623 0.8269 1.9012 0.1275  0.1130  0.0844  323 ILE C N   
11084 C CA  . ILE C 323 ? 0.4654 0.8174 1.9053 0.1269  0.1049  0.0929  323 ILE C CA  
11085 C C   . ILE C 323 ? 0.4522 0.7784 1.9083 0.1263  0.1051  0.1172  323 ILE C C   
11086 O O   . ILE C 323 ? 0.4425 0.7429 1.9061 0.1265  0.0996  0.1190  323 ILE C O   
11087 C CB  . ILE C 323 ? 0.4915 0.8823 1.9149 0.1279  0.1014  0.0998  323 ILE C CB  
11088 C CG1 . ILE C 323 ? 0.5087 0.9244 1.9162 0.1282  0.0992  0.0717  323 ILE C CG1 
11089 C CG2 . ILE C 323 ? 0.4908 0.8693 1.9194 0.1280  0.0935  0.1124  323 ILE C CG2 
11090 C CD1 . ILE C 323 ? 0.5280 0.9744 1.9248 0.1302  0.1077  0.0631  323 ILE C CD1 
11091 N N   . SER C 324 ? 0.4361 0.7705 1.8986 0.1255  0.1116  0.1354  324 SER C N   
11092 C CA  . SER C 324 ? 0.4183 0.7256 1.8995 0.1241  0.1116  0.1549  324 SER C CA  
11093 C C   . SER C 324 ? 0.4150 0.7266 1.9061 0.1217  0.1191  0.1619  324 SER C C   
11094 O O   . SER C 324 ? 0.4164 0.7633 1.8993 0.1217  0.1255  0.1667  324 SER C O   
11095 C CB  . SER C 324 ? 0.4224 0.7383 1.9065 0.1253  0.1089  0.1812  324 SER C CB  
11096 O OG  . SER C 324 ? 0.4208 0.7438 1.8941 0.1278  0.1024  0.1744  324 SER C OG  
11097 N N   . PRO C 325 ? 0.4033 0.6822 1.9125 0.1194  0.1186  0.1628  325 PRO C N   
11098 C CA  . PRO C 325 ? 0.3979 0.6382 1.9150 0.1200  0.1117  0.1564  325 PRO C CA  
11099 C C   . PRO C 325 ? 0.3893 0.6185 1.8965 0.1219  0.1081  0.1302  325 PRO C C   
11100 O O   . PRO C 325 ? 0.3957 0.6402 1.8945 0.1223  0.1108  0.1142  325 PRO C O   
11101 C CB  . PRO C 325 ? 0.3881 0.6030 1.9250 0.1168  0.1123  0.1606  325 PRO C CB  
11102 C CG  . PRO C 325 ? 0.3924 0.6322 1.9334 0.1141  0.1199  0.1672  325 PRO C CG  
11103 C CD  . PRO C 325 ? 0.4012 0.6824 1.9244 0.1161  0.1247  0.1701  325 PRO C CD  
11104 N N   . LYS C 326 ? 0.3821 0.5850 1.8923 0.1232  0.1023  0.1264  326 LYS C N   
11105 C CA  . LYS C 326 ? 0.3675 0.5567 1.8725 0.1241  0.0987  0.1052  326 LYS C CA  
11106 C C   . LYS C 326 ? 0.3675 0.5279 1.8825 0.1232  0.0980  0.0967  326 LYS C C   
11107 O O   . LYS C 326 ? 0.3718 0.5147 1.8977 0.1225  0.0973  0.1064  326 LYS C O   
11108 C CB  . LYS C 326 ? 0.3543 0.5387 1.8559 0.1261  0.0936  0.1072  326 LYS C CB  
11109 C CG  . LYS C 326 ? 0.3628 0.5799 1.8533 0.1268  0.0929  0.1125  326 LYS C CG  
11110 C CD  . LYS C 326 ? 0.3625 0.5796 1.8538 0.1294  0.0881  0.1220  326 LYS C CD  
11111 C CE  . LYS C 326 ? 0.3707 0.6208 1.8500 0.1296  0.0851  0.1219  326 LYS C CE  
11112 N NZ  . LYS C 326 ? 0.3833 0.6636 1.8569 0.1302  0.0877  0.1394  326 LYS C NZ  
11113 N N   . ASN C 327 ? 0.3558 0.5129 1.8680 0.1232  0.0977  0.0782  327 ASN C N   
11114 C CA  . ASN C 327 ? 0.3462 0.4795 1.8667 0.1229  0.0962  0.0697  327 ASN C CA  
11115 C C   . ASN C 327 ? 0.3362 0.4452 1.8582 0.1238  0.0914  0.0709  327 ASN C C   
11116 O O   . ASN C 327 ? 0.3381 0.4485 1.8545 0.1250  0.0893  0.0709  327 ASN C O   
11117 C CB  . ASN C 327 ? 0.3602 0.4957 1.8793 0.1235  0.0965  0.0514  327 ASN C CB  
11118 C CG  . ASN C 327 ? 0.3617 0.4766 1.8908 0.1237  0.0949  0.0458  327 ASN C CG  
11119 O OD1 . ASN C 327 ? 0.3836 0.4975 1.9209 0.1229  0.0966  0.0518  327 ASN C OD1 
11120 N ND2 . ASN C 327 ? 0.3585 0.4582 1.8883 0.1244  0.0913  0.0360  327 ASN C ND2 
11121 N N   . LYS C 328 ? 0.3269 0.4162 1.8570 0.1234  0.0897  0.0715  328 LYS C N   
11122 C CA  . LYS C 328 ? 0.3242 0.3927 1.8562 0.1249  0.0861  0.0743  328 LYS C CA  
11123 C C   . LYS C 328 ? 0.3314 0.4032 1.8633 0.1266  0.0862  0.0865  328 LYS C C   
11124 O O   . LYS C 328 ? 0.3213 0.3866 1.8498 0.1294  0.0843  0.0858  328 LYS C O   
11125 C CB  . LYS C 328 ? 0.3151 0.3726 1.8419 0.1264  0.0834  0.0643  328 LYS C CB  
11126 C CG  . LYS C 328 ? 0.3125 0.3660 1.8415 0.1255  0.0827  0.0542  328 LYS C CG  
11127 C CD  . LYS C 328 ? 0.3163 0.3610 1.8534 0.1246  0.0814  0.0544  328 LYS C CD  
11128 C CE  . LYS C 328 ? 0.3116 0.3555 1.8531 0.1247  0.0807  0.0456  328 LYS C CE  
11129 N NZ  . LYS C 328 ? 0.3097 0.3438 1.8475 0.1260  0.0780  0.0404  328 LYS C NZ  
11130 N N   . SER C 329 ? 0.3460 0.4289 1.8836 0.1251  0.0885  0.0992  329 SER C N   
11131 C CA  . SER C 329 ? 0.3570 0.4383 1.9004 0.1270  0.0879  0.1139  329 SER C CA  
11132 C C   . SER C 329 ? 0.3612 0.4217 1.9196 0.1258  0.0861  0.1192  329 SER C C   
11133 O O   . SER C 329 ? 0.3467 0.4020 1.9116 0.1222  0.0859  0.1155  329 SER C O   
11134 C CB  . SER C 329 ? 0.3653 0.4736 1.9062 0.1263  0.0910  0.1275  329 SER C CB  
11135 O OG  . SER C 329 ? 0.3742 0.4925 1.9229 0.1226  0.0945  0.1370  329 SER C OG  
11136 N N   . ILE C 330 ? 0.3792 0.4276 1.9444 0.1294  0.0840  0.1265  330 ILE C N   
11137 C CA  . ILE C 330 ? 0.3858 0.4120 1.9672 0.1292  0.0812  0.1298  330 ILE C CA  
11138 C C   . ILE C 330 ? 0.3957 0.4285 1.9917 0.1283  0.0825  0.1510  330 ILE C C   
11139 O O   . ILE C 330 ? 0.3935 0.4362 1.9876 0.1325  0.0833  0.1611  330 ILE C O   
11140 C CB  . ILE C 330 ? 0.3895 0.3965 1.9688 0.1354  0.0782  0.1197  330 ILE C CB  
11141 C CG1 . ILE C 330 ? 0.3887 0.3898 1.9552 0.1354  0.0768  0.1018  330 ILE C CG1 
11142 C CG2 . ILE C 330 ? 0.4045 0.3889 2.0020 0.1369  0.0749  0.1225  330 ILE C CG2 
11143 C CD1 . ILE C 330 ? 0.3966 0.3829 1.9590 0.1416  0.0749  0.0918  330 ILE C CD1 
11144 N N   . HIS C 331 ? 0.4132 0.4424 2.0252 0.1225  0.0826  0.1591  331 HIS C N   
11145 C CA  . HIS C 331 ? 0.4408 0.4756 2.0703 0.1206  0.0840  0.1823  331 HIS C CA  
11146 C C   . HIS C 331 ? 0.4613 0.4669 2.1157 0.1188  0.0793  0.1837  331 HIS C C   
11147 O O   . HIS C 331 ? 0.4636 0.4548 2.1231 0.1148  0.0762  0.1705  331 HIS C O   
11148 C CB  . HIS C 331 ? 0.4438 0.5080 2.0715 0.1149  0.0895  0.1945  331 HIS C CB  
11149 C CG  . HIS C 331 ? 0.4427 0.5352 2.0469 0.1175  0.0933  0.1910  331 HIS C CG  
11150 N ND1 . HIS C 331 ? 0.4577 0.5769 2.0566 0.1191  0.0962  0.2084  331 HIS C ND1 
11151 C CD2 . HIS C 331 ? 0.4359 0.5349 2.0220 0.1186  0.0939  0.1717  331 HIS C CD2 
11152 C CE1 . HIS C 331 ? 0.4530 0.5939 2.0301 0.1208  0.0981  0.1972  331 HIS C CE1 
11153 N NE2 . HIS C 331 ? 0.4365 0.5640 2.0070 0.1204  0.0968  0.1750  331 HIS C NE2 
11154 N N   . THR C 332 ? 0.4835 0.4800 2.1541 0.1222  0.0780  0.1988  332 THR C N   
11155 C CA  . THR C 332 ? 0.5187 0.4859 2.2169 0.1208  0.0731  0.2003  332 THR C CA  
11156 C C   . THR C 332 ? 0.5429 0.5184 2.2652 0.1154  0.0751  0.2295  332 THR C C   
11157 O O   . THR C 332 ? 0.5683 0.5243 2.3157 0.1171  0.0719  0.2403  332 THR C O   
11158 C CB  . THR C 332 ? 0.5298 0.4749 2.2317 0.1307  0.0697  0.1920  332 THR C CB  
11159 O OG1 . THR C 332 ? 0.5452 0.5098 2.2400 0.1367  0.0730  0.2078  332 THR C OG1 
11160 C CG2 . THR C 332 ? 0.5191 0.4546 2.2005 0.1359  0.0679  0.1643  332 THR C CG2 
11161 N N   . ASN C 333 ? 0.5524 0.5578 2.2679 0.1094  0.0805  0.2422  333 ASN C N   
11162 C CA  . ASN C 333 ? 0.5790 0.6031 2.3108 0.1053  0.0844  0.2736  333 ASN C CA  
11163 C C   . ASN C 333 ? 0.5688 0.6193 2.2972 0.0966  0.0900  0.2787  333 ASN C C   
11164 O O   . ASN C 333 ? 0.5439 0.6079 2.2493 0.0969  0.0923  0.2605  333 ASN C O   
11165 C CB  . ASN C 333 ? 0.6117 0.6575 2.3294 0.1128  0.0869  0.2884  333 ASN C CB  
11166 C CG  . ASN C 333 ? 0.6786 0.7392 2.4170 0.1104  0.0892  0.3242  333 ASN C CG  
11167 O OD1 . ASN C 333 ? 0.7632 0.7993 2.5325 0.1101  0.0855  0.3375  333 ASN C OD1 
11168 N ND2 . ASN C 333 ? 0.6986 0.7997 2.4208 0.1091  0.0952  0.3402  333 ASN C ND2 
11169 N N   . THR C 334 ? 0.5859 0.6442 2.3401 0.0891  0.0924  0.3043  334 THR C N   
11170 C CA  . THR C 334 ? 0.5816 0.6657 2.3377 0.0808  0.0984  0.3104  334 THR C CA  
11171 C C   . THR C 334 ? 0.5937 0.7232 2.3273 0.0831  0.1071  0.3255  334 THR C C   
11172 O O   . THR C 334 ? 0.6086 0.7658 2.3364 0.0787  0.1137  0.3261  334 THR C O   
11173 C CB  . THR C 334 ? 0.5966 0.6710 2.3925 0.0704  0.0974  0.3308  334 THR C CB  
11174 O OG1 . THR C 334 ? 0.6074 0.6964 2.4155 0.0708  0.1007  0.3646  334 THR C OG1 
11175 C CG2 . THR C 334 ? 0.6017 0.6311 2.4211 0.0681  0.0873  0.3143  334 THR C CG2 
11176 N N   . LYS C 335 ? 0.6003 0.7393 2.3217 0.0903  0.1070  0.3364  335 LYS C N   
11177 C CA  . LYS C 335 ? 0.5983 0.7818 2.2947 0.0933  0.1137  0.3473  335 LYS C CA  
11178 C C   . LYS C 335 ? 0.5685 0.7565 2.2312 0.1007  0.1122  0.3192  335 LYS C C   
11179 O O   . LYS C 335 ? 0.5626 0.7280 2.2215 0.1067  0.1062  0.3084  335 LYS C O   
11180 C CB  . LYS C 335 ? 0.6288 0.8267 2.3358 0.0953  0.1142  0.3821  335 LYS C CB  
11181 C CG  . LYS C 335 ? 0.6681 0.8648 2.4111 0.0870  0.1163  0.4144  335 LYS C CG  
11182 C CD  . LYS C 335 ? 0.6891 0.9252 2.4304 0.0796  0.1261  0.4272  335 LYS C CD  
11183 C CE  . LYS C 335 ? 0.7170 0.9537 2.4964 0.0701  0.1286  0.4607  335 LYS C CE  
11184 N NZ  . LYS C 335 ? 0.7260 0.9252 2.5335 0.0626  0.1239  0.4462  335 LYS C NZ  
11185 N N   . ILE C 336 ? 0.5609 0.7789 2.2012 0.1003  0.1179  0.3072  336 ILE C N   
11186 C CA  . ILE C 336 ? 0.5428 0.7641 2.1550 0.1057  0.1165  0.2791  336 ILE C CA  
11187 C C   . ILE C 336 ? 0.5367 0.8021 2.1246 0.1089  0.1209  0.2848  336 ILE C C   
11188 O O   . ILE C 336 ? 0.5264 0.8239 2.1071 0.1065  0.1282  0.2877  336 ILE C O   
11189 C CB  . ILE C 336 ? 0.5322 0.7453 2.1414 0.1031  0.1179  0.2540  336 ILE C CB  
11190 C CG1 . ILE C 336 ? 0.5399 0.7139 2.1721 0.0994  0.1128  0.2479  336 ILE C CG1 
11191 C CG2 . ILE C 336 ? 0.5210 0.7362 2.1047 0.1083  0.1163  0.2267  336 ILE C CG2 
11192 C CD1 . ILE C 336 ? 0.5409 0.6802 2.1727 0.1041  0.1048  0.2354  336 ILE C CD1 
11193 N N   . PRO C 337 ? 0.5326 0.8035 2.1074 0.1146  0.1164  0.2859  337 PRO C N   
11194 C CA  . PRO C 337 ? 0.5245 0.8385 2.0746 0.1174  0.1188  0.2880  337 PRO C CA  
11195 C C   . PRO C 337 ? 0.5025 0.8315 2.0334 0.1170  0.1227  0.2600  337 PRO C C   
11196 O O   . PRO C 337 ? 0.4929 0.7946 2.0237 0.1173  0.1200  0.2350  337 PRO C O   
11197 C CB  . PRO C 337 ? 0.5227 0.8304 2.0651 0.1232  0.1111  0.2855  337 PRO C CB  
11198 C CG  . PRO C 337 ? 0.5287 0.7949 2.0968 0.1242  0.1065  0.2942  337 PRO C CG  
11199 C CD  . PRO C 337 ? 0.5282 0.7672 2.1126 0.1188  0.1089  0.2858  337 PRO C CD  
11200 N N   . LEU C 338 ? 0.5023 0.8754 2.0183 0.1169  0.1293  0.2655  338 LEU C N   
11201 C CA  . LEU C 338 ? 0.4948 0.8876 1.9933 0.1178  0.1340  0.2394  338 LEU C CA  
11202 C C   . LEU C 338 ? 0.4956 0.9256 1.9669 0.1218  0.1325  0.2317  338 LEU C C   
11203 O O   . LEU C 338 ? 0.5116 0.9774 1.9747 0.1226  0.1346  0.2540  338 LEU C O   
11204 C CB  . LEU C 338 ? 0.4978 0.9130 2.0039 0.1145  0.1443  0.2490  338 LEU C CB  
11205 C CG  . LEU C 338 ? 0.4892 0.9273 1.9806 0.1167  0.1508  0.2226  338 LEU C CG  
11206 C CD1 . LEU C 338 ? 0.4678 0.8682 1.9680 0.1167  0.1476  0.1953  338 LEU C CD1 
11207 C CD2 . LEU C 338 ? 0.4985 0.9737 1.9943 0.1148  0.1625  0.2377  338 LEU C CD2 
11208 N N   . GLU C 339 ? 0.4838 0.9071 1.9417 0.1240  0.1287  0.2001  339 GLU C N   
11209 C CA  . GLU C 339 ? 0.4943 0.9514 1.9277 0.1270  0.1259  0.1880  339 GLU C CA  
11210 C C   . GLU C 339 ? 0.4861 0.9505 1.9081 0.1283  0.1287  0.1535  339 GLU C C   
11211 O O   . GLU C 339 ? 0.4589 0.8888 1.8905 0.1278  0.1267  0.1332  339 GLU C O   
11212 C CB  . GLU C 339 ? 0.4936 0.9327 1.9266 0.1282  0.1153  0.1862  339 GLU C CB  
11213 C CG  . GLU C 339 ? 0.4986 0.9357 1.9429 0.1288  0.1124  0.2202  339 GLU C CG  
11214 C CD  . GLU C 339 ? 0.4951 0.9217 1.9388 0.1313  0.1026  0.2185  339 GLU C CD  
11215 O OE1 . GLU C 339 ? 0.5016 0.9567 1.9269 0.1325  0.0982  0.2069  339 GLU C OE1 
11216 O OE2 . GLU C 339 ? 0.4878 0.8795 1.9501 0.1320  0.0993  0.2275  339 GLU C OE2 
11217 N N   . LEU C 340 ? 0.5057 1.0163 1.9074 0.1306  0.1331  0.1472  340 LEU C N   
11218 C CA  . LEU C 340 ? 0.5206 1.0420 1.9128 0.1331  0.1368  0.1141  340 LEU C CA  
11219 C C   . LEU C 340 ? 0.5338 1.0950 1.9000 0.1358  0.1332  0.0970  340 LEU C C   
11220 O O   . LEU C 340 ? 0.5427 1.1427 1.8943 0.1365  0.1334  0.1167  340 LEU C O   
11221 C CB  . LEU C 340 ? 0.5392 1.0794 1.9369 0.1338  0.1494  0.1205  340 LEU C CB  
11222 C CG  . LEU C 340 ? 0.5332 1.0364 1.9578 0.1308  0.1528  0.1297  340 LEU C CG  
11223 C CD1 . LEU C 340 ? 0.5381 1.0676 1.9664 0.1323  0.1652  0.1285  340 LEU C CD1 
11224 C CD2 . LEU C 340 ? 0.5207 0.9750 1.9583 0.1303  0.1463  0.1073  340 LEU C CD2 
11225 N N   . TYR C 341 ? 0.5301 1.0817 1.8921 0.1372  0.1295  0.0604  341 TYR C N   
11226 C CA  . TYR C 341 ? 0.5477 1.1376 1.8868 0.1400  0.1275  0.0351  341 TYR C CA  
11227 C C   . TYR C 341 ? 0.5577 1.1578 1.8957 0.1443  0.1366  0.0076  341 TYR C C   
11228 O O   . TYR C 341 ? 0.5340 1.0982 1.8882 0.1447  0.1362  -0.0132 341 TYR C O   
11229 C CB  . TYR C 341 ? 0.5402 1.1143 1.8772 0.1378  0.1141  0.0147  341 TYR C CB  
11230 C CG  . TYR C 341 ? 0.5622 1.1841 1.8737 0.1393  0.1093  -0.0011 341 TYR C CG  
11231 C CD1 . TYR C 341 ? 0.5715 1.2293 1.8677 0.1390  0.1053  0.0236  341 TYR C CD1 
11232 C CD2 . TYR C 341 ? 0.5795 1.2128 1.8827 0.1415  0.1084  -0.0408 341 TYR C CD2 
11233 C CE1 . TYR C 341 ? 0.5976 1.3033 1.8686 0.1405  0.1001  0.0094  341 TYR C CE1 
11234 C CE2 . TYR C 341 ? 0.6060 1.2849 1.8849 0.1429  0.1032  -0.0579 341 TYR C CE2 
11235 C CZ  . TYR C 341 ? 0.6144 1.3311 1.8759 0.1422  0.0987  -0.0327 341 TYR C CZ  
11236 O OH  . TYR C 341 ? 0.6352 1.4004 1.8711 0.1434  0.0925  -0.0492 341 TYR C OH  
11237 N N   . ASN C 342 ? 0.5878 1.2397 1.9068 0.1483  0.1450  0.0089  342 ASN C N   
11238 C CA  . ASN C 342 ? 0.6120 1.2822 1.9297 0.1539  0.1561  -0.0130 342 ASN C CA  
11239 C C   . ASN C 342 ? 0.6589 1.3739 1.9500 0.1587  0.1551  -0.0432 342 ASN C C   
11240 O O   . ASN C 342 ? 0.6803 1.4392 1.9482 0.1587  0.1537  -0.0298 342 ASN C O   
11241 C CB  . ASN C 342 ? 0.6132 1.3136 1.9320 0.1553  0.1703  0.0154  342 ASN C CB  
11242 C CG  . ASN C 342 ? 0.5851 1.2476 1.9308 0.1503  0.1722  0.0455  342 ASN C CG  
11243 O OD1 . ASN C 342 ? 0.5745 1.2477 1.9218 0.1467  0.1737  0.0822  342 ASN C OD1 
11244 N ND2 . ASN C 342 ? 0.5718 1.1922 1.9398 0.1502  0.1722  0.0311  342 ASN C ND2 
11245 N N   . ASP C 343 ? 0.6811 1.3861 1.9763 0.1630  0.1556  -0.0835 343 ASP C N   
11246 C CA  . ASP C 343 ? 0.7280 1.4764 1.9999 0.1688  0.1564  -0.1170 343 ASP C CA  
11247 C C   . ASP C 343 ? 0.7435 1.5395 2.0048 0.1760  0.1734  -0.1122 343 ASP C C   
11248 O O   . ASP C 343 ? 0.7330 1.5244 2.0083 0.1753  0.1835  -0.0833 343 ASP C O   
11249 C CB  . ASP C 343 ? 0.7561 1.4732 2.0404 0.1708  0.1499  -0.1622 343 ASP C CB  
11250 C CG  . ASP C 343 ? 0.7932 1.4963 2.0963 0.1777  0.1613  -0.1794 343 ASP C CG  
11251 O OD1 . ASP C 343 ? 0.7995 1.4722 2.1244 0.1759  0.1661  -0.1561 343 ASP C OD1 
11252 O OD2 . ASP C 343 ? 0.8571 1.5837 2.1528 0.1854  0.1655  -0.2156 343 ASP C OD2 
11253 N N   . LYS C 344 ? 0.7647 1.6064 2.0028 0.1829  0.1766  -0.1432 344 LYS C N   
11254 C CA  . LYS C 344 ? 0.7803 1.6836 1.9991 0.1897  0.1922  -0.1356 344 LYS C CA  
11255 C C   . LYS C 344 ? 0.7650 1.6607 2.0048 0.1962  0.2073  -0.1438 344 LYS C C   
11256 O O   . LYS C 344 ? 0.7662 1.7103 1.9961 0.2017  0.2226  -0.1335 344 LYS C O   
11257 C CB  . LYS C 344 ? 0.8197 1.7737 2.0053 0.1953  0.1890  -0.1704 344 LYS C CB  
11258 C CG  . LYS C 344 ? 0.8492 1.8798 2.0039 0.2008  0.2018  -0.1552 344 LYS C CG  
11259 C CD  . LYS C 344 ? 0.8870 1.9705 2.0072 0.2074  0.1988  -0.1948 344 LYS C CD  
11260 C CE  . LYS C 344 ? 0.9015 1.9762 2.0294 0.2165  0.2029  -0.2492 344 LYS C CE  
11261 N NZ  . LYS C 344 ? 0.9453 2.0786 2.0383 0.2240  0.2022  -0.2871 344 LYS C NZ  
11262 N N   . ASP C 345 ? 0.7368 1.5743 2.0065 0.1957  0.2030  -0.1611 345 ASP C N   
11263 C CA  . ASP C 345 ? 0.7255 1.5526 2.0186 0.2022  0.2153  -0.1701 345 ASP C CA  
11264 C C   . ASP C 345 ? 0.6837 1.4993 1.9960 0.1968  0.2225  -0.1250 345 ASP C C   
11265 O O   . ASP C 345 ? 0.6760 1.5111 1.9991 0.2019  0.2367  -0.1200 345 ASP C O   
11266 C CB  . ASP C 345 ? 0.7255 1.4976 2.0442 0.2042  0.2075  -0.2041 345 ASP C CB  
11267 C CG  . ASP C 345 ? 0.7639 1.5497 2.0726 0.2124  0.2048  -0.2556 345 ASP C CG  
11268 O OD1 . ASP C 345 ? 0.7962 1.6343 2.0737 0.2156  0.2067  -0.2668 345 ASP C OD1 
11269 O OD2 . ASP C 345 ? 0.7709 1.5161 2.1040 0.2158  0.2009  -0.2842 345 ASP C OD2 
11270 N N   . VAL C 346 ? 0.6526 1.4365 1.9707 0.1868  0.2126  -0.0939 346 VAL C N   
11271 C CA  . VAL C 346 ? 0.6208 1.3867 1.9602 0.1807  0.2170  -0.0537 346 VAL C CA  
11272 C C   . VAL C 346 ? 0.6276 1.4494 1.9523 0.1799  0.2284  -0.0194 346 VAL C C   
11273 O O   . VAL C 346 ? 0.6318 1.4794 1.9342 0.1769  0.2240  -0.0026 346 VAL C O   
11274 C CB  . VAL C 346 ? 0.5967 1.3094 1.9486 0.1714  0.2028  -0.0348 346 VAL C CB  
11275 C CG1 . VAL C 346 ? 0.5741 1.2701 1.9472 0.1649  0.2065  0.0055  346 VAL C CG1 
11276 C CG2 . VAL C 346 ? 0.5870 1.2466 1.9552 0.1719  0.1927  -0.0650 346 VAL C CG2 
11277 N N   . LYS C 347 ? 0.6233 1.4643 1.9629 0.1825  0.2429  -0.0081 347 LYS C N   
11278 C CA  . LYS C 347 ? 0.6351 1.5294 1.9665 0.1812  0.2557  0.0268  347 LYS C CA  
11279 C C   . LYS C 347 ? 0.6114 1.4812 1.9737 0.1725  0.2583  0.0673  347 LYS C C   
11280 O O   . LYS C 347 ? 0.6155 1.5235 1.9770 0.1692  0.2678  0.1026  347 LYS C O   
11281 C CB  . LYS C 347 ? 0.6627 1.6118 1.9844 0.1919  0.2724  0.0059  347 LYS C CB  
11282 C CG  . LYS C 347 ? 0.6948 1.6747 1.9848 0.2013  0.2708  -0.0365 347 LYS C CG  
11283 C CD  . LYS C 347 ? 0.7230 1.7466 1.9770 0.1992  0.2666  -0.0224 347 LYS C CD  
11284 C CE  . LYS C 347 ? 0.7581 1.8202 1.9800 0.2086  0.2658  -0.0658 347 LYS C CE  
11285 N NZ  . LYS C 347 ? 0.7756 1.8700 1.9645 0.2054  0.2567  -0.0545 347 LYS C NZ  
11286 N N   . LYS C 348 ? 0.5882 1.3965 1.9779 0.1683  0.2495  0.0631  348 LYS C N   
11287 C CA  . LYS C 348 ? 0.5756 1.3556 1.9945 0.1592  0.2489  0.0983  348 LYS C CA  
11288 C C   . LYS C 348 ? 0.5483 1.2594 1.9849 0.1546  0.2339  0.0901  348 LYS C C   
11289 O O   . LYS C 348 ? 0.5432 1.2287 1.9794 0.1595  0.2282  0.0560  348 LYS C O   
11290 C CB  . LYS C 348 ? 0.5844 1.3842 2.0269 0.1608  0.2632  0.1044  348 LYS C CB  
11291 C CG  . LYS C 348 ? 0.5710 1.3444 2.0476 0.1507  0.2625  0.1386  348 LYS C CG  
11292 C CD  . LYS C 348 ? 0.5791 1.3865 2.0782 0.1506  0.2780  0.1529  348 LYS C CD  
11293 C CE  . LYS C 348 ? 0.5772 1.3774 2.0916 0.1587  0.2822  0.1209  348 LYS C CE  
11294 N NZ  . LYS C 348 ? 0.5798 1.4078 2.1221 0.1567  0.2953  0.1397  348 LYS C NZ  
11295 N N   . VAL C 349 ? 0.5369 1.2189 1.9907 0.1455  0.2280  0.1217  349 VAL C N   
11296 C CA  . VAL C 349 ? 0.5200 1.1407 1.9881 0.1411  0.2142  0.1172  349 VAL C CA  
11297 C C   . VAL C 349 ? 0.4985 1.0947 1.9974 0.1329  0.2140  0.1452  349 VAL C C   
11298 O O   . VAL C 349 ? 0.5025 1.1102 2.0062 0.1268  0.2156  0.1787  349 VAL C O   
11299 C CB  . VAL C 349 ? 0.5289 1.1336 1.9799 0.1386  0.2022  0.1221  349 VAL C CB  
11300 C CG1 . VAL C 349 ? 0.5061 1.0504 1.9726 0.1345  0.1895  0.1185  349 VAL C CG1 
11301 C CG2 . VAL C 349 ? 0.5503 1.1789 1.9717 0.1451  0.2001  0.0945  349 VAL C CG2 
11302 N N   . VAL C 350 ? 0.4760 1.0356 1.9964 0.1326  0.2102  0.1314  350 VAL C N   
11303 C CA  . VAL C 350 ? 0.4657 1.0055 2.0167 0.1251  0.2097  0.1529  350 VAL C CA  
11304 C C   . VAL C 350 ? 0.4488 0.9307 2.0103 0.1219  0.1956  0.1448  350 VAL C C   
11305 O O   . VAL C 350 ? 0.4405 0.9006 1.9964 0.1270  0.1902  0.1171  350 VAL C O   
11306 C CB  . VAL C 350 ? 0.4606 1.0233 2.0306 0.1277  0.2206  0.1474  350 VAL C CB  
11307 C CG1 . VAL C 350 ? 0.4457 0.9883 2.0500 0.1190  0.2186  0.1676  350 VAL C CG1 
11308 C CG2 . VAL C 350 ? 0.4777 1.1024 2.0358 0.1317  0.2361  0.1550  350 VAL C CG2 
11309 N N   . VAL C 351 ? 0.4478 0.9061 2.0254 0.1136  0.1899  0.1694  351 VAL C N   
11310 C CA  . VAL C 351 ? 0.4381 0.8449 2.0263 0.1106  0.1773  0.1635  351 VAL C CA  
11311 C C   . VAL C 351 ? 0.4327 0.8259 2.0521 0.1044  0.1767  0.1730  351 VAL C C   
11312 O O   . VAL C 351 ? 0.4458 0.8569 2.0817 0.0982  0.1820  0.1982  351 VAL C O   
11313 C CB  . VAL C 351 ? 0.4441 0.8301 2.0261 0.1070  0.1692  0.1793  351 VAL C CB  
11314 C CG1 . VAL C 351 ? 0.4361 0.7717 2.0272 0.1051  0.1572  0.1704  351 VAL C CG1 
11315 C CG2 . VAL C 351 ? 0.4531 0.8570 2.0059 0.1122  0.1690  0.1728  351 VAL C CG2 
11316 N N   . LYS C 352 ? 0.4152 0.7773 2.0434 0.1058  0.1695  0.1538  352 LYS C N   
11317 C CA  . LYS C 352 ? 0.3988 0.7489 2.0561 0.1004  0.1671  0.1592  352 LYS C CA  
11318 C C   . LYS C 352 ? 0.3863 0.6889 2.0491 0.0973  0.1532  0.1536  352 LYS C C   
11319 O O   . LYS C 352 ? 0.3642 0.6441 2.0090 0.1017  0.1468  0.1388  352 LYS C O   
11320 C CB  . LYS C 352 ? 0.3929 0.7598 2.0591 0.1061  0.1727  0.1420  352 LYS C CB  
11321 C CG  . LYS C 352 ? 0.4022 0.8199 2.0676 0.1094  0.1878  0.1473  352 LYS C CG  
11322 C CD  . LYS C 352 ? 0.3942 0.8285 2.0688 0.1173  0.1938  0.1273  352 LYS C CD  
11323 C CE  . LYS C 352 ? 0.4081 0.8930 2.0721 0.1237  0.2091  0.1254  352 LYS C CE  
11324 N NZ  . LYS C 352 ? 0.4100 0.9147 2.0877 0.1320  0.2165  0.1078  352 LYS C NZ  
11325 N N   . PHE C 353 ? 0.3789 0.6693 2.0680 0.0894  0.1490  0.1656  353 PHE C N   
11326 C CA  . PHE C 353 ? 0.3734 0.6234 2.0707 0.0864  0.1360  0.1585  353 PHE C CA  
11327 C C   . PHE C 353 ? 0.3773 0.6290 2.1038 0.0810  0.1337  0.1603  353 PHE C C   
11328 O O   . PHE C 353 ? 0.3883 0.6573 2.1370 0.0735  0.1380  0.1792  353 PHE C O   
11329 C CB  . PHE C 353 ? 0.3747 0.6007 2.0737 0.0809  0.1295  0.1725  353 PHE C CB  
11330 C CG  . PHE C 353 ? 0.3710 0.5577 2.0784 0.0781  0.1164  0.1636  353 PHE C CG  
11331 C CD1 . PHE C 353 ? 0.3682 0.5330 2.0580 0.0843  0.1098  0.1430  353 PHE C CD1 
11332 C CD2 . PHE C 353 ? 0.3753 0.5475 2.1080 0.0692  0.1106  0.1758  353 PHE C CD2 
11333 C CE1 . PHE C 353 ? 0.3654 0.4985 2.0599 0.0823  0.0984  0.1350  353 PHE C CE1 
11334 C CE2 . PHE C 353 ? 0.3757 0.5141 2.1138 0.0672  0.0984  0.1647  353 PHE C CE2 
11335 C CZ  . PHE C 353 ? 0.3689 0.4894 2.0864 0.0742  0.0926  0.1444  353 PHE C CZ  
11336 N N   . ARG C 354 ? 0.3752 0.6095 2.1030 0.0844  0.1262  0.1419  354 ARG C N   
11337 C CA  . ARG C 354 ? 0.3721 0.6116 2.1262 0.0811  0.1232  0.1404  354 ARG C CA  
11338 C C   . ARG C 354 ? 0.3712 0.6530 2.1392 0.0815  0.1365  0.1495  354 ARG C C   
11339 O O   . ARG C 354 ? 0.3815 0.6779 2.1758 0.0730  0.1385  0.1660  354 ARG C O   
11340 C CB  . ARG C 354 ? 0.3780 0.5949 2.1523 0.0705  0.1126  0.1501  354 ARG C CB  
11341 C CG  . ARG C 354 ? 0.3780 0.5563 2.1361 0.0715  0.1010  0.1402  354 ARG C CG  
11342 C CD  . ARG C 354 ? 0.3841 0.5399 2.1629 0.0624  0.0892  0.1431  354 ARG C CD  
11343 N NE  . ARG C 354 ? 0.3886 0.5106 2.1498 0.0650  0.0793  0.1315  354 ARG C NE  
11344 C CZ  . ARG C 354 ? 0.4062 0.5046 2.1794 0.0587  0.0691  0.1313  354 ARG C CZ  
11345 N NH1 . ARG C 354 ? 0.4240 0.5268 2.2283 0.0486  0.0655  0.1402  354 ARG C NH1 
11346 N NH2 . ARG C 354 ? 0.4096 0.4811 2.1656 0.0622  0.0625  0.1217  354 ARG C NH2 
11347 N N   . ASP C 355 ? 0.3655 0.6682 2.1156 0.0911  0.1460  0.1390  355 ASP C N   
11348 C CA  . ASP C 355 ? 0.3685 0.7146 2.1281 0.0941  0.1599  0.1436  355 ASP C CA  
11349 C C   . ASP C 355 ? 0.3884 0.7595 2.1606 0.0850  0.1678  0.1709  355 ASP C C   
11350 O O   . ASP C 355 ? 0.4056 0.8085 2.2005 0.0824  0.1761  0.1813  355 ASP C O   
11351 C CB  . ASP C 355 ? 0.3557 0.7095 2.1404 0.0961  0.1585  0.1354  355 ASP C CB  
11352 C CG  . ASP C 355 ? 0.3414 0.6684 2.1189 0.1040  0.1490  0.1128  355 ASP C CG  
11353 O OD1 . ASP C 355 ? 0.3334 0.6682 2.0968 0.1147  0.1545  0.0963  355 ASP C OD1 
11354 O OD2 . ASP C 355 ? 0.3343 0.6326 2.1199 0.0992  0.1358  0.1120  355 ASP C OD2 
11355 N N   . LYS C 356 ? 0.3999 0.7582 2.1602 0.0803  0.1654  0.1844  356 LYS C N   
11356 C CA  . LYS C 356 ? 0.4131 0.7949 2.1855 0.0722  0.1730  0.2131  356 LYS C CA  
11357 C C   . LYS C 356 ? 0.4150 0.8065 2.1579 0.0762  0.1780  0.2195  356 LYS C C   
11358 O O   . LYS C 356 ? 0.4196 0.7811 2.1435 0.0786  0.1695  0.2112  356 LYS C O   
11359 C CB  . LYS C 356 ? 0.4321 0.7870 2.2321 0.0596  0.1628  0.2298  356 LYS C CB  
11360 C CG  . LYS C 356 ? 0.4641 0.8405 2.2814 0.0503  0.1701  0.2629  356 LYS C CG  
11361 C CD  . LYS C 356 ? 0.4865 0.8423 2.3414 0.0364  0.1615  0.2801  356 LYS C CD  
11362 C CE  . LYS C 356 ? 0.5165 0.8881 2.3862 0.0281  0.1678  0.3144  356 LYS C CE  
11363 N NZ  . LYS C 356 ? 0.5314 0.8753 2.4378 0.0147  0.1578  0.3300  356 LYS C NZ  
11364 N N   . VAL C 357 ? 0.4153 0.8520 2.1549 0.0770  0.1918  0.2349  357 VAL C N   
11365 C CA  . VAL C 357 ? 0.4207 0.8758 2.1316 0.0813  0.1971  0.2416  357 VAL C CA  
11366 C C   . VAL C 357 ? 0.4231 0.8549 2.1388 0.0736  0.1899  0.2651  357 VAL C C   
11367 O O   . VAL C 357 ? 0.4286 0.8573 2.1735 0.0636  0.1891  0.2886  357 VAL C O   
11368 C CB  . VAL C 357 ? 0.4308 0.9447 2.1377 0.0838  0.2140  0.2544  357 VAL C CB  
11369 C CG1 . VAL C 357 ? 0.4466 0.9829 2.1249 0.0867  0.2184  0.2664  357 VAL C CG1 
11370 C CG2 . VAL C 357 ? 0.4221 0.9599 2.1225 0.0938  0.2220  0.2277  357 VAL C CG2 
11371 N N   . ILE C 358 ? 0.4289 0.8447 2.1184 0.0784  0.1844  0.2586  358 ILE C N   
11372 C CA  . ILE C 358 ? 0.4426 0.8380 2.1361 0.0733  0.1780  0.2803  358 ILE C CA  
11373 C C   . ILE C 358 ? 0.4507 0.8716 2.1160 0.0786  0.1823  0.2896  358 ILE C C   
11374 O O   . ILE C 358 ? 0.4627 0.8725 2.1308 0.0758  0.1780  0.3100  358 ILE C O   
11375 C CB  . ILE C 358 ? 0.4319 0.7729 2.1287 0.0727  0.1633  0.2653  358 ILE C CB  
11376 C CG1 . ILE C 358 ? 0.4200 0.7475 2.0849 0.0820  0.1586  0.2399  358 ILE C CG1 
11377 C CG2 . ILE C 358 ? 0.4272 0.7477 2.1489 0.0680  0.1581  0.2540  358 ILE C CG2 
11378 C CD1 . ILE C 358 ? 0.4102 0.6896 2.0759 0.0820  0.1457  0.2296  358 ILE C CD1 
11379 N N   . TYR C 359 ? 0.4540 0.9088 2.0933 0.0866  0.1900  0.2738  359 TYR C N   
11380 C CA  . TYR C 359 ? 0.4677 0.9578 2.0802 0.0912  0.1952  0.2829  359 TYR C CA  
11381 C C   . TYR C 359 ? 0.4818 1.0191 2.0778 0.0977  0.2075  0.2681  359 TYR C C   
11382 O O   . TYR C 359 ? 0.4760 1.0068 2.0756 0.1014  0.2087  0.2424  359 TYR C O   
11383 C CB  . TYR C 359 ? 0.4627 0.9254 2.0529 0.0962  0.1844  0.2670  359 TYR C CB  
11384 C CG  . TYR C 359 ? 0.4761 0.9742 2.0386 0.1006  0.1872  0.2760  359 TYR C CG  
11385 C CD1 . TYR C 359 ? 0.4883 0.9937 2.0560 0.0971  0.1860  0.3095  359 TYR C CD1 
11386 C CD2 . TYR C 359 ? 0.4792 1.0051 2.0125 0.1084  0.1906  0.2514  359 TYR C CD2 
11387 C CE1 . TYR C 359 ? 0.5030 1.0447 2.0458 0.1012  0.1878  0.3201  359 TYR C CE1 
11388 C CE2 . TYR C 359 ? 0.4952 1.0573 2.0028 0.1120  0.1922  0.2591  359 TYR C CE2 
11389 C CZ  . TYR C 359 ? 0.5081 1.0794 2.0196 0.1085  0.1907  0.2944  359 TYR C CZ  
11390 O OH  . TYR C 359 ? 0.5336 1.1423 2.0210 0.1119  0.1911  0.3062  359 TYR C OH  
11391 N N   . SER C 360 ? 0.5017 1.0878 2.0807 0.0998  0.2167  0.2850  360 SER C N   
11392 C CA  . SER C 360 ? 0.5144 1.1503 2.0750 0.1071  0.2291  0.2700  360 SER C CA  
11393 C C   . SER C 360 ? 0.5461 1.2314 2.0811 0.1095  0.2354  0.2888  360 SER C C   
11394 O O   . SER C 360 ? 0.5649 1.2710 2.1115 0.1034  0.2401  0.3267  360 SER C O   
11395 C CB  . SER C 360 ? 0.5076 1.1653 2.0931 0.1045  0.2404  0.2765  360 SER C CB  
11396 O OG  . SER C 360 ? 0.5185 1.2345 2.0854 0.1118  0.2548  0.2701  360 SER C OG  
11397 N N   . LYS C 361 ? 0.5633 1.2677 2.0648 0.1182  0.2349  0.2627  361 LYS C N   
11398 C CA  . LYS C 361 ? 0.5992 1.3525 2.0723 0.1213  0.2389  0.2767  361 LYS C CA  
11399 C C   . LYS C 361 ? 0.6106 1.4027 2.0547 0.1315  0.2459  0.2419  361 LYS C C   
11400 O O   . LYS C 361 ? 0.6123 1.3803 2.0441 0.1366  0.2380  0.2054  361 LYS C O   
11401 C CB  . LYS C 361 ? 0.6135 1.3438 2.0731 0.1206  0.2252  0.2831  361 LYS C CB  
11402 C CG  . LYS C 361 ? 0.6488 1.4233 2.0930 0.1199  0.2276  0.3180  361 LYS C CG  
11403 C CD  . LYS C 361 ? 0.6662 1.4520 2.1385 0.1118  0.2348  0.3649  361 LYS C CD  
11404 C CE  . LYS C 361 ? 0.6882 1.5196 2.1501 0.1107  0.2383  0.4055  361 LYS C CE  
11405 N NZ  . LYS C 361 ? 0.6851 1.4889 2.1453 0.1101  0.2244  0.4189  361 LYS C NZ  
11406 N N   . ASN C 362 ? 0.6241 1.4771 2.0587 0.1343  0.2609  0.2534  362 ASN C N   
11407 C CA  . ASN C 362 ? 0.6388 1.5374 2.0415 0.1447  0.2679  0.2223  362 ASN C CA  
11408 C C   . ASN C 362 ? 0.6444 1.5512 2.0144 0.1472  0.2572  0.2158  362 ASN C C   
11409 O O   . ASN C 362 ? 0.6517 1.5602 2.0204 0.1419  0.2520  0.2497  362 ASN C O   
11410 C CB  . ASN C 362 ? 0.6611 1.6284 2.0590 0.1474  0.2868  0.2399  362 ASN C CB  
11411 C CG  . ASN C 362 ? 0.6497 1.6117 2.0839 0.1437  0.2970  0.2505  362 ASN C CG  
11412 O OD1 . ASN C 362 ? 0.6303 1.5568 2.0817 0.1461  0.2946  0.2223  362 ASN C OD1 
11413 N ND2 . ASN C 362 ? 0.6621 1.6600 2.1106 0.1376  0.3081  0.2926  362 ASN C ND2 
11414 N N   . ILE C 363 ? 0.6440 1.5540 1.9908 0.1551  0.2532  0.1725  363 ILE C N   
11415 C CA  . ILE C 363 ? 0.6511 1.5667 1.9690 0.1570  0.2414  0.1613  363 ILE C CA  
11416 C C   . ILE C 363 ? 0.6814 1.6707 1.9638 0.1642  0.2502  0.1539  363 ILE C C   
11417 O O   . ILE C 363 ? 0.6977 1.7127 1.9707 0.1721  0.2594  0.1218  363 ILE C O   
11418 C CB  . ILE C 363 ? 0.6361 1.5007 1.9557 0.1590  0.2285  0.1190  363 ILE C CB  
11419 C CG1 . ILE C 363 ? 0.6073 1.4031 1.9592 0.1522  0.2198  0.1283  363 ILE C CG1 
11420 C CG2 . ILE C 363 ? 0.6473 1.5225 1.9381 0.1608  0.2163  0.1032  363 ILE C CG2 
11421 C CD1 . ILE C 363 ? 0.6013 1.3794 1.9619 0.1445  0.2123  0.1684  363 ILE C CD1 
11422 N N   . THR C 364 ? 0.6950 1.7194 1.9583 0.1620  0.2475  0.1844  364 THR C N   
11423 C CA  . THR C 364 ? 0.7266 1.8231 1.9514 0.1685  0.2529  0.1795  364 THR C CA  
11424 C C   . THR C 364 ? 0.7303 1.8220 1.9292 0.1717  0.2375  0.1445  364 THR C C   
11425 O O   . THR C 364 ? 0.7523 1.8789 1.9251 0.1793  0.2397  0.1068  364 THR C O   
11426 C CB  . THR C 364 ? 0.7418 1.8804 1.9608 0.1642  0.2568  0.2343  364 THR C CB  
11427 O OG1 . THR C 364 ? 0.7225 1.8368 1.9785 0.1572  0.2644  0.2696  364 THR C OG1 
11428 C CG2 . THR C 364 ? 0.7784 2.0026 1.9625 0.1711  0.2693  0.2373  364 THR C CG2 
11429 N N   . SER C 365 ? 0.7085 1.7570 1.9169 0.1656  0.2219  0.1576  365 SER C N   
11430 C CA  . SER C 365 ? 0.7122 1.7630 1.8983 0.1665  0.2062  0.1388  365 SER C CA  
11431 C C   . SER C 365 ? 0.6808 1.6597 1.8876 0.1633  0.1929  0.1124  365 SER C C   
11432 O O   . SER C 365 ? 0.6494 1.5772 1.8860 0.1579  0.1908  0.1320  365 SER C O   
11433 C CB  . SER C 365 ? 0.7230 1.7987 1.9010 0.1630  0.2006  0.1843  365 SER C CB  
11434 O OG  . SER C 365 ? 0.7361 1.8197 1.8931 0.1637  0.1848  0.1693  365 SER C OG  
11435 N N   . GLU C 366 ? 0.6896 1.6669 1.8808 0.1664  0.1839  0.0680  366 GLU C N   
11436 C CA  . GLU C 366 ? 0.6670 1.5816 1.8778 0.1643  0.1737  0.0372  366 GLU C CA  
11437 C C   . GLU C 366 ? 0.6596 1.5427 1.8768 0.1583  0.1577  0.0518  366 GLU C C   
11438 O O   . GLU C 366 ? 0.6664 1.5795 1.8699 0.1570  0.1529  0.0796  366 GLU C O   
11439 C CB  . GLU C 366 ? 0.6822 1.6054 1.8788 0.1695  0.1705  -0.0169 366 GLU C CB  
11440 C CG  . GLU C 366 ? 0.7094 1.6758 1.8742 0.1706  0.1599  -0.0329 366 GLU C CG  
11441 C CD  . GLU C 366 ? 0.7291 1.6999 1.8840 0.1753  0.1560  -0.0897 366 GLU C CD  
11442 O OE1 . GLU C 366 ? 0.7144 1.6313 1.8909 0.1727  0.1478  -0.1152 366 GLU C OE1 
11443 O OE2 . GLU C 366 ? 0.7600 1.7882 1.8867 0.1818  0.1615  -0.1086 366 GLU C OE2 
11444 N N   . GLY C 367 ? 0.6458 1.4698 1.8846 0.1553  0.1497  0.0327  367 GLY C N   
11445 C CA  . GLY C 367 ? 0.6372 1.4295 1.8837 0.1504  0.1349  0.0401  367 GLY C CA  
11446 C C   . GLY C 367 ? 0.6213 1.3755 1.8929 0.1463  0.1357  0.0789  367 GLY C C   
11447 O O   . GLY C 367 ? 0.6050 1.3295 1.8970 0.1455  0.1437  0.0840  367 GLY C O   
11448 N N   . TYR C 368 ? 0.6314 1.3872 1.9024 0.1439  0.1267  0.1049  368 TYR C N   
11449 C CA  . TYR C 368 ? 0.6121 1.3281 1.9081 0.1406  0.1249  0.1373  368 TYR C CA  
11450 C C   . TYR C 368 ? 0.6180 1.3490 1.9218 0.1404  0.1370  0.1726  368 TYR C C   
11451 O O   . TYR C 368 ? 0.6371 1.4208 1.9228 0.1426  0.1436  0.1865  368 TYR C O   
11452 C CB  . TYR C 368 ? 0.6083 1.3258 1.9037 0.1396  0.1128  0.1572  368 TYR C CB  
11453 C CG  . TYR C 368 ? 0.5817 1.2560 1.9046 0.1376  0.1111  0.1876  368 TYR C CG  
11454 C CD1 . TYR C 368 ? 0.5531 1.1709 1.8974 0.1355  0.1081  0.1735  368 TYR C CD1 
11455 C CD2 . TYR C 368 ? 0.5864 1.2770 1.9149 0.1381  0.1123  0.2299  368 TYR C CD2 
11456 C CE1 . TYR C 368 ? 0.5366 1.1163 1.9048 0.1343  0.1066  0.1975  368 TYR C CE1 
11457 C CE2 . TYR C 368 ? 0.5735 1.2231 1.9291 0.1368  0.1103  0.2546  368 TYR C CE2 
11458 C CZ  . TYR C 368 ? 0.5482 1.1427 1.9228 0.1352  0.1076  0.2368  368 TYR C CZ  
11459 O OH  . TYR C 368 ? 0.5380 1.0934 1.9381 0.1347  0.1056  0.2577  368 TYR C OH  
11460 N N   . MET C 369 ? 0.6069 1.2923 1.9387 0.1373  0.1393  0.1881  369 MET C N   
11461 C CA  . MET C 369 ? 0.6247 1.3176 1.9706 0.1355  0.1497  0.2215  369 MET C CA  
11462 C C   . MET C 369 ? 0.6048 1.2410 1.9820 0.1316  0.1457  0.2378  369 MET C C   
11463 O O   . MET C 369 ? 0.5944 1.1865 1.9820 0.1309  0.1409  0.2141  369 MET C O   
11464 C CB  . MET C 369 ? 0.6403 1.3533 1.9818 0.1371  0.1622  0.2034  369 MET C CB  
11465 C CG  . MET C 369 ? 0.6484 1.3758 2.0050 0.1346  0.1745  0.2345  369 MET C CG  
11466 S SD  . MET C 369 ? 0.6396 1.3035 2.0322 0.1303  0.1756  0.2281  369 MET C SD  
11467 C CE  . MET C 369 ? 0.6302 1.2933 2.0126 0.1354  0.1791  0.1776  369 MET C CE  
11468 N N   . ALA C 370 ? 0.6076 1.2462 1.9991 0.1296  0.1469  0.2783  370 ALA C N   
11469 C CA  . ALA C 370 ? 0.5838 1.1716 2.0048 0.1267  0.1420  0.2946  370 ALA C CA  
11470 C C   . ALA C 370 ? 0.5816 1.1660 2.0266 0.1222  0.1506  0.3245  370 ALA C C   
11471 O O   . ALA C 370 ? 0.5946 1.2227 2.0337 0.1215  0.1589  0.3469  370 ALA C O   
11472 C CB  . ALA C 370 ? 0.5757 1.1623 1.9969 0.1289  0.1321  0.3137  370 ALA C CB  
11473 N N   . ASP C 371 ? 0.5658 1.0997 2.0386 0.1187  0.1485  0.3251  371 ASP C N   
11474 C CA  . ASP C 371 ? 0.5760 1.1020 2.0763 0.1131  0.1549  0.3517  371 ASP C CA  
11475 C C   . ASP C 371 ? 0.5721 1.0383 2.1011 0.1102  0.1484  0.3484  371 ASP C C   
11476 O O   . ASP C 371 ? 0.5714 1.0065 2.0973 0.1132  0.1398  0.3298  371 ASP C O   
11477 C CB  . ASP C 371 ? 0.5707 1.1225 2.0677 0.1112  0.1664  0.3422  371 ASP C CB  
11478 C CG  . ASP C 371 ? 0.5785 1.1560 2.0938 0.1059  0.1759  0.3791  371 ASP C CG  
11479 O OD1 . ASP C 371 ? 0.5952 1.2079 2.1039 0.1065  0.1777  0.4095  371 ASP C OD1 
11480 O OD2 . ASP C 371 ? 0.5706 1.1331 2.1082 0.1009  0.1809  0.3787  371 ASP C OD2 
11481 N N   . GLU C 372 ? 0.5803 1.0324 2.1376 0.1040  0.1526  0.3660  372 GLU C N   
11482 C CA  . GLU C 372 ? 0.5733 0.9714 2.1572 0.1007  0.1466  0.3591  372 GLU C CA  
11483 C C   . GLU C 372 ? 0.5548 0.9453 2.1527 0.0953  0.1521  0.3475  372 GLU C C   
11484 O O   . GLU C 372 ? 0.5578 0.9803 2.1620 0.0914  0.1613  0.3639  372 GLU C O   
11485 C CB  . GLU C 372 ? 0.5957 0.9769 2.2096 0.0972  0.1438  0.3940  372 GLU C CB  
11486 C CG  . GLU C 372 ? 0.6160 0.9931 2.2249 0.1032  0.1364  0.4060  372 GLU C CG  
11487 C CD  . GLU C 372 ? 0.6431 0.9998 2.2868 0.1003  0.1335  0.4400  372 GLU C CD  
11488 O OE1 . GLU C 372 ? 0.6651 1.0151 2.3350 0.0927  0.1376  0.4550  372 GLU C OE1 
11489 O OE2 . GLU C 372 ? 0.6691 1.0158 2.3162 0.1058  0.1270  0.4511  372 GLU C OE2 
11490 N N   . LEU C 373 ? 0.5288 0.8786 2.1326 0.0953  0.1462  0.3208  373 LEU C N   
11491 C CA  . LEU C 373 ? 0.5196 0.8524 2.1444 0.0896  0.1479  0.3130  373 LEU C CA  
11492 C C   . LEU C 373 ? 0.5182 0.8164 2.1766 0.0835  0.1423  0.3315  373 LEU C C   
11493 O O   . LEU C 373 ? 0.5112 0.7847 2.1733 0.0860  0.1351  0.3365  373 LEU C O   
11494 C CB  . LEU C 373 ? 0.5037 0.8113 2.1180 0.0929  0.1433  0.2763  373 LEU C CB  
11495 C CG  . LEU C 373 ? 0.4973 0.8294 2.0817 0.0992  0.1467  0.2522  373 LEU C CG  
11496 C CD1 . LEU C 373 ? 0.4767 0.7752 2.0552 0.1022  0.1397  0.2211  373 LEU C CD1 
11497 C CD2 . LEU C 373 ? 0.5023 0.8734 2.0851 0.0984  0.1577  0.2524  373 LEU C CD2 
11498 N N   . THR C 374 ? 0.5222 0.8181 2.2069 0.0756  0.1452  0.3395  374 THR C N   
11499 C CA  . THR C 374 ? 0.5256 0.7820 2.2437 0.0692  0.1379  0.3474  374 THR C CA  
11500 C C   . THR C 374 ? 0.5067 0.7377 2.2309 0.0671  0.1333  0.3190  374 THR C C   
11501 O O   . THR C 374 ? 0.5037 0.7561 2.2235 0.0662  0.1390  0.3087  374 THR C O   
11502 C CB  . THR C 374 ? 0.5528 0.8257 2.3020 0.0601  0.1431  0.3833  374 THR C CB  
11503 O OG1 . THR C 374 ? 0.5712 0.8684 2.3117 0.0634  0.1465  0.4101  374 THR C OG1 
11504 C CG2 . THR C 374 ? 0.5663 0.7967 2.3539 0.0528  0.1344  0.3907  374 THR C CG2 
11505 N N   . ILE C 375 ? 0.4952 0.6825 2.2296 0.0672  0.1228  0.3064  375 ILE C N   
11506 C CA  . ILE C 375 ? 0.4828 0.6458 2.2248 0.0647  0.1169  0.2821  375 ILE C CA  
11507 C C   . ILE C 375 ? 0.4779 0.6069 2.2541 0.0575  0.1086  0.2892  375 ILE C C   
11508 O O   . ILE C 375 ? 0.4914 0.6128 2.2840 0.0558  0.1076  0.3110  375 ILE C O   
11509 C CB  . ILE C 375 ? 0.4824 0.6280 2.1966 0.0733  0.1119  0.2522  375 ILE C CB  
11510 C CG1 . ILE C 375 ? 0.4998 0.6196 2.2090 0.0786  0.1056  0.2524  375 ILE C CG1 
11511 C CG2 . ILE C 375 ? 0.4738 0.6516 2.1589 0.0792  0.1193  0.2423  375 ILE C CG2 
11512 C CD1 . ILE C 375 ? 0.4972 0.5984 2.1832 0.0860  0.1005  0.2247  375 ILE C CD1 
11513 N N   . ASP C 376 ? 0.4633 0.5727 2.2511 0.0534  0.1021  0.2705  376 ASP C N   
11514 C CA  . ASP C 376 ? 0.4711 0.5510 2.2933 0.0452  0.0934  0.2734  376 ASP C CA  
11515 C C   . ASP C 376 ? 0.4605 0.5120 2.2767 0.0470  0.0833  0.2421  376 ASP C C   
11516 O O   . ASP C 376 ? 0.4610 0.5071 2.2965 0.0397  0.0781  0.2346  376 ASP C O   
11517 C CB  . ASP C 376 ? 0.4774 0.5763 2.3324 0.0333  0.0973  0.2936  376 ASP C CB  
11518 C CG  . ASP C 376 ? 0.4965 0.5661 2.3932 0.0231  0.0886  0.3031  376 ASP C CG  
11519 O OD1 . ASP C 376 ? 0.4991 0.5353 2.3990 0.0266  0.0809  0.2978  376 ASP C OD1 
11520 O OD2 . ASP C 376 ? 0.5145 0.5950 2.4418 0.0119  0.0892  0.3145  376 ASP C OD2 
11521 N N   . PRO C 377 ? 0.4580 0.4917 2.2487 0.0566  0.0795  0.2239  377 PRO C N   
11522 C CA  . PRO C 377 ? 0.4566 0.4702 2.2358 0.0595  0.0713  0.1951  377 PRO C CA  
11523 C C   . PRO C 377 ? 0.4805 0.4631 2.2863 0.0534  0.0600  0.1871  377 PRO C C   
11524 O O   . PRO C 377 ? 0.5062 0.4708 2.3327 0.0512  0.0573  0.1983  377 PRO C O   
11525 C CB  . PRO C 377 ? 0.4530 0.4586 2.2016 0.0709  0.0718  0.1842  377 PRO C CB  
11526 C CG  . PRO C 377 ? 0.4619 0.4687 2.2173 0.0727  0.0756  0.2063  377 PRO C CG  
11527 C CD  . PRO C 377 ? 0.4655 0.4990 2.2395 0.0647  0.0826  0.2320  377 PRO C CD  
11528 N N   . VAL C 378 ? 0.4797 0.4562 2.2852 0.0510  0.0529  0.1670  378 VAL C N   
11529 C CA  . VAL C 378 ? 0.4975 0.4455 2.3236 0.0460  0.0406  0.1538  378 VAL C CA  
11530 C C   . VAL C 378 ? 0.5070 0.4344 2.3074 0.0555  0.0342  0.1283  378 VAL C C   
11531 O O   . VAL C 378 ? 0.4902 0.4257 2.2678 0.0597  0.0331  0.1129  378 VAL C O   
11532 C CB  . VAL C 378 ? 0.5008 0.4573 2.3474 0.0360  0.0349  0.1490  378 VAL C CB  
11533 C CG1 . VAL C 378 ? 0.5174 0.4454 2.3788 0.0320  0.0202  0.1287  378 VAL C CG1 
11534 C CG2 . VAL C 378 ? 0.5048 0.4817 2.3828 0.0254  0.0411  0.1754  378 VAL C CG2 
11535 N N   . GLY C 379 ? 0.5372 0.4383 2.3444 0.0589  0.0302  0.1250  379 GLY C N   
11536 C CA  . GLY C 379 ? 0.5357 0.4179 2.3210 0.0686  0.0252  0.1020  379 GLY C CA  
11537 C C   . GLY C 379 ? 0.5078 0.4037 2.2596 0.0791  0.0339  0.1035  379 GLY C C   
11538 O O   . GLY C 379 ? 0.5198 0.4258 2.2718 0.0811  0.0418  0.1224  379 GLY C O   
11539 N N   . ILE C 380 ? 0.4813 0.3792 2.2060 0.0852  0.0320  0.0847  380 ILE C N   
11540 C CA  . ILE C 380 ? 0.4606 0.3743 2.1564 0.0930  0.0399  0.0863  380 ILE C CA  
11541 C C   . ILE C 380 ? 0.4445 0.3817 2.1335 0.0892  0.0431  0.0887  380 ILE C C   
11542 O O   . ILE C 380 ? 0.4405 0.3781 2.1314 0.0859  0.0370  0.0778  380 ILE C O   
11543 C CB  . ILE C 380 ? 0.4579 0.3607 2.1303 0.1023  0.0372  0.0674  380 ILE C CB  
11544 C CG1 . ILE C 380 ? 0.4830 0.3640 2.1644 0.1074  0.0350  0.0638  380 ILE C CG1 
11545 C CG2 . ILE C 380 ? 0.4446 0.3644 2.0910 0.1086  0.0448  0.0699  380 ILE C CG2 
11546 C CD1 . ILE C 380 ? 0.4857 0.3581 2.1456 0.1173  0.0333  0.0448  380 ILE C CD1 
11547 N N   . GLU C 381 ? 0.4264 0.3843 2.1090 0.0901  0.0523  0.1029  381 GLU C N   
11548 C CA  . GLU C 381 ? 0.4175 0.3984 2.0995 0.0867  0.0562  0.1062  381 GLU C CA  
11549 C C   . GLU C 381 ? 0.3859 0.3832 2.0435 0.0933  0.0637  0.1057  381 GLU C C   
11550 O O   . GLU C 381 ? 0.3737 0.3826 2.0275 0.0949  0.0703  0.1180  381 GLU C O   
11551 C CB  . GLU C 381 ? 0.4417 0.4349 2.1501 0.0781  0.0594  0.1243  381 GLU C CB  
11552 C CG  . GLU C 381 ? 0.4530 0.4637 2.1721 0.0726  0.0596  0.1233  381 GLU C CG  
11553 C CD  . GLU C 381 ? 0.4851 0.5168 2.2272 0.0650  0.0661  0.1439  381 GLU C CD  
11554 O OE1 . GLU C 381 ? 0.4833 0.5332 2.2169 0.0677  0.0756  0.1573  381 GLU C OE1 
11555 O OE2 . GLU C 381 ? 0.5319 0.5654 2.3002 0.0565  0.0621  0.1471  381 GLU C OE2 
11556 N N   . ASP C 382 ? 0.3647 0.3630 2.0072 0.0968  0.0616  0.0915  382 ASP C N   
11557 C CA  . ASP C 382 ? 0.3411 0.3572 1.9686 0.1006  0.0677  0.0894  382 ASP C CA  
11558 C C   . ASP C 382 ? 0.3254 0.3646 1.9649 0.0966  0.0734  0.0977  382 ASP C C   
11559 O O   . ASP C 382 ? 0.3174 0.3588 1.9738 0.0917  0.0705  0.0980  382 ASP C O   
11560 C CB  . ASP C 382 ? 0.3404 0.3509 1.9563 0.1041  0.0632  0.0748  382 ASP C CB  
11561 C CG  . ASP C 382 ? 0.3453 0.3530 1.9738 0.1004  0.0561  0.0691  382 ASP C CG  
11562 O OD1 . ASP C 382 ? 0.3561 0.3503 1.9950 0.0968  0.0494  0.0675  382 ASP C OD1 
11563 O OD2 . ASP C 382 ? 0.3374 0.3560 1.9658 0.1017  0.0566  0.0652  382 ASP C OD2 
11564 N N   . MET C 383 ? 0.3208 0.3794 1.9515 0.0989  0.0816  0.1037  383 MET C N   
11565 C CA  . MET C 383 ? 0.3222 0.4075 1.9613 0.0966  0.0891  0.1115  383 MET C CA  
11566 C C   . MET C 383 ? 0.3193 0.4218 1.9405 0.1024  0.0952  0.1038  383 MET C C   
11567 O O   . MET C 383 ? 0.3221 0.4269 1.9281 0.1055  0.0972  0.1045  383 MET C O   
11568 C CB  . MET C 383 ? 0.3369 0.4342 1.9862 0.0924  0.0941  0.1316  383 MET C CB  
11569 C CG  . MET C 383 ? 0.3523 0.4300 2.0222 0.0864  0.0881  0.1411  383 MET C CG  
11570 S SD  . MET C 383 ? 0.3668 0.4533 2.0475 0.0831  0.0931  0.1673  383 MET C SD  
11571 C CE  . MET C 383 ? 0.3645 0.4926 2.0516 0.0797  0.1043  0.1811  383 MET C CE  
11572 N N   . GLU C 384 ? 0.3194 0.4339 1.9441 0.1040  0.0975  0.0952  384 GLU C N   
11573 C CA  . GLU C 384 ? 0.3198 0.4539 1.9328 0.1090  0.1042  0.0874  384 GLU C CA  
11574 C C   . GLU C 384 ? 0.3278 0.4935 1.9454 0.1074  0.1137  0.0987  384 GLU C C   
11575 O O   . GLU C 384 ? 0.3386 0.5192 1.9716 0.1057  0.1174  0.1013  384 GLU C O   
11576 C CB  . GLU C 384 ? 0.3156 0.4476 1.9338 0.1125  0.1025  0.0733  384 GLU C CB  
11577 C CG  . GLU C 384 ? 0.3157 0.4674 1.9268 0.1181  0.1094  0.0623  384 GLU C CG  
11578 C CD  . GLU C 384 ? 0.3083 0.4540 1.9271 0.1228  0.1070  0.0485  384 GLU C CD  
11579 O OE1 . GLU C 384 ? 0.3012 0.4380 1.9342 0.1213  0.1019  0.0503  384 GLU C OE1 
11580 O OE2 . GLU C 384 ? 0.3116 0.4604 1.9225 0.1278  0.1092  0.0359  384 GLU C OE2 
11581 N N   . LEU C 385 ? 0.3377 0.5162 1.9422 0.1081  0.1177  0.1063  385 LEU C N   
11582 C CA  . LEU C 385 ? 0.3485 0.5623 1.9518 0.1078  0.1273  0.1163  385 LEU C CA  
11583 C C   . LEU C 385 ? 0.3461 0.5802 1.9405 0.1139  0.1330  0.0984  385 LEU C C   
11584 O O   . LEU C 385 ? 0.3492 0.5753 1.9289 0.1182  0.1301  0.0830  385 LEU C O   
11585 C CB  . LEU C 385 ? 0.3629 0.5850 1.9529 0.1076  0.1283  0.1293  385 LEU C CB  
11586 C CG  . LEU C 385 ? 0.3755 0.5857 1.9789 0.1020  0.1255  0.1516  385 LEU C CG  
11587 C CD1 . LEU C 385 ? 0.3745 0.5487 1.9920 0.0993  0.1167  0.1468  385 LEU C CD1 
11588 C CD2 . LEU C 385 ? 0.3814 0.5926 1.9707 0.1041  0.1238  0.1603  385 LEU C CD2 
11589 N N   . ALA C 386 ? 0.3494 0.6106 1.9542 0.1144  0.1411  0.1004  386 ALA C N   
11590 C CA  . ALA C 386 ? 0.3527 0.6338 1.9518 0.1214  0.1472  0.0815  386 ALA C CA  
11591 C C   . ALA C 386 ? 0.3704 0.6918 1.9555 0.1235  0.1571  0.0858  386 ALA C C   
11592 O O   . ALA C 386 ? 0.3825 0.7306 1.9758 0.1206  0.1648  0.1030  386 ALA C O   
11593 C CB  . ALA C 386 ? 0.3488 0.6340 1.9697 0.1224  0.1495  0.0774  386 ALA C CB  
11594 N N   . PHE C 387 ? 0.3786 0.7057 1.9428 0.1283  0.1566  0.0703  387 PHE C N   
11595 C CA  . PHE C 387 ? 0.3980 0.7653 1.9449 0.1311  0.1647  0.0710  387 PHE C CA  
11596 C C   . PHE C 387 ? 0.4065 0.7985 1.9531 0.1387  0.1728  0.0488  387 PHE C C   
11597 O O   . PHE C 387 ? 0.4049 0.7780 1.9625 0.1427  0.1702  0.0299  387 PHE C O   
11598 C CB  . PHE C 387 ? 0.4142 0.7776 1.9391 0.1317  0.1587  0.0653  387 PHE C CB  
11599 C CG  . PHE C 387 ? 0.4226 0.7752 1.9454 0.1260  0.1537  0.0900  387 PHE C CG  
11600 C CD1 . PHE C 387 ? 0.4170 0.7309 1.9537 0.1219  0.1460  0.0980  387 PHE C CD1 
11601 C CD2 . PHE C 387 ? 0.4387 0.8205 1.9458 0.1256  0.1562  0.1040  387 PHE C CD2 
11602 C CE1 . PHE C 387 ? 0.4219 0.7247 1.9589 0.1180  0.1415  0.1184  387 PHE C CE1 
11603 C CE2 . PHE C 387 ? 0.4457 0.8162 1.9540 0.1216  0.1512  0.1270  387 PHE C CE2 
11604 C CZ  . PHE C 387 ? 0.4370 0.7671 1.9613 0.1180  0.1442  0.1334  387 PHE C CZ  
11605 N N   . GLU C 388 ? 0.4200 0.8565 1.9543 0.1411  0.1827  0.0524  388 GLU C N   
11606 C CA  . GLU C 388 ? 0.4317 0.8998 1.9653 0.1492  0.1927  0.0326  388 GLU C CA  
11607 C C   . GLU C 388 ? 0.4560 0.9682 1.9631 0.1523  0.1992  0.0305  388 GLU C C   
11608 O O   . GLU C 388 ? 0.4555 0.9899 1.9542 0.1476  0.2021  0.0564  388 GLU C O   
11609 C CB  . GLU C 388 ? 0.4295 0.9147 1.9863 0.1489  0.2020  0.0448  388 GLU C CB  
11610 C CG  . GLU C 388 ? 0.4129 0.8584 1.9958 0.1461  0.1946  0.0457  388 GLU C CG  
11611 C CD  . GLU C 388 ? 0.4154 0.8804 2.0238 0.1453  0.2028  0.0573  388 GLU C CD  
11612 O OE1 . GLU C 388 ? 0.4273 0.9376 2.0340 0.1474  0.2157  0.0643  388 GLU C OE1 
11613 O OE2 . GLU C 388 ? 0.4037 0.8401 2.0340 0.1422  0.1960  0.0600  388 GLU C OE2 
11614 N N   . PHE C 389 ? 0.4819 1.0058 1.9771 0.1604  0.2006  -0.0012 389 PHE C N   
11615 C CA  . PHE C 389 ? 0.5068 1.0741 1.9748 0.1647  0.2056  -0.0113 389 PHE C CA  
11616 C C   . PHE C 389 ? 0.5180 1.1218 1.9883 0.1743  0.2186  -0.0316 389 PHE C C   
11617 O O   . PHE C 389 ? 0.5124 1.0964 1.9977 0.1803  0.2179  -0.0569 389 PHE C O   
11618 C CB  . PHE C 389 ? 0.5082 1.0562 1.9602 0.1652  0.1940  -0.0343 389 PHE C CB  
11619 C CG  . PHE C 389 ? 0.4973 1.0111 1.9484 0.1568  0.1819  -0.0152 389 PHE C CG  
11620 C CD1 . PHE C 389 ? 0.4774 0.9412 1.9481 0.1533  0.1737  -0.0135 389 PHE C CD1 
11621 C CD2 . PHE C 389 ? 0.5092 1.0433 1.9399 0.1533  0.1789  0.0013  389 PHE C CD2 
11622 C CE1 . PHE C 389 ? 0.4663 0.9016 1.9359 0.1468  0.1638  0.0024  389 PHE C CE1 
11623 C CE2 . PHE C 389 ? 0.4920 0.9960 1.9243 0.1470  0.1685  0.0181  389 PHE C CE2 
11624 C CZ  . PHE C 389 ? 0.4739 0.9286 1.9254 0.1440  0.1615  0.0178  389 PHE C CZ  
11625 N N   . TYR C 390 ? 0.5375 1.1952 1.9938 0.1761  0.2306  -0.0192 390 TYR C N   
11626 C CA  . TYR C 390 ? 0.5668 1.2677 2.0240 0.1858  0.2454  -0.0349 390 TYR C CA  
11627 C C   . TYR C 390 ? 0.5858 1.3308 2.0101 0.1927  0.2491  -0.0573 390 TYR C C   
11628 O O   . TYR C 390 ? 0.5925 1.3489 1.9935 0.1879  0.2434  -0.0453 390 TYR C O   
11629 C CB  . TYR C 390 ? 0.5802 1.3107 2.0507 0.1814  0.2572  0.0013  390 TYR C CB  
11630 C CG  . TYR C 390 ? 0.5685 1.2623 2.0745 0.1756  0.2547  0.0181  390 TYR C CG  
11631 C CD1 . TYR C 390 ? 0.5551 1.2125 2.0709 0.1643  0.2444  0.0458  390 TYR C CD1 
11632 C CD2 . TYR C 390 ? 0.5718 1.2692 2.1022 0.1820  0.2622  0.0052  390 TYR C CD2 
11633 C CE1 . TYR C 390 ? 0.5437 1.1697 2.0906 0.1589  0.2410  0.0586  390 TYR C CE1 
11634 C CE2 . TYR C 390 ? 0.5583 1.2259 2.1208 0.1765  0.2587  0.0203  390 TYR C CE2 
11635 C CZ  . TYR C 390 ? 0.5454 1.1773 2.1153 0.1646  0.2478  0.0463  390 TYR C CZ  
11636 O OH  . TYR C 390 ? 0.5329 1.1371 2.1335 0.1592  0.2434  0.0582  390 TYR C OH  
11637 N N   . ASP C 391 ? 0.5929 1.3645 2.0160 0.2044  0.2586  -0.0899 391 ASP C N   
11638 C CA  . ASP C 391 ? 0.6133 1.4297 2.0050 0.2121  0.2624  -0.1166 391 ASP C CA  
11639 C C   . ASP C 391 ? 0.6256 1.5109 2.0056 0.2170  0.2811  -0.1021 391 ASP C C   
11640 O O   . ASP C 391 ? 0.6147 1.5090 2.0107 0.2117  0.2888  -0.0661 391 ASP C O   
11641 C CB  . ASP C 391 ? 0.6236 1.4191 2.0198 0.2215  0.2576  -0.1661 391 ASP C CB  
11642 C CG  . ASP C 391 ? 0.6292 1.4286 2.0499 0.2331  0.2688  -0.1887 391 ASP C CG  
11643 O OD1 . ASP C 391 ? 0.6414 1.4845 2.0650 0.2374  0.2847  -0.1750 391 ASP C OD1 
11644 O OD2 . ASP C 391 ? 0.6266 1.3857 2.0655 0.2379  0.2615  -0.2185 391 ASP C OD2 
11645 N N   . SER C 392 ? 0.6506 1.5853 2.0035 0.2268  0.2881  -0.1301 392 SER C N   
11646 C CA  . SER C 392 ? 0.6714 1.6792 2.0066 0.2316  0.3060  -0.1156 392 SER C CA  
11647 C C   . SER C 392 ? 0.6738 1.7016 2.0344 0.2402  0.3232  -0.1201 392 SER C C   
11648 O O   . SER C 392 ? 0.6839 1.7710 2.0370 0.2429  0.3398  -0.1009 392 SER C O   
11649 C CB  . SER C 392 ? 0.7032 1.7612 1.9982 0.2392  0.3073  -0.1438 392 SER C CB  
11650 O OG  . SER C 392 ? 0.7148 1.7581 2.0110 0.2499  0.3041  -0.1981 392 SER C OG  
11651 N N   . ASP C 393 ? 0.6624 1.6433 2.0541 0.2446  0.3194  -0.1435 393 ASP C N   
11652 C CA  . ASP C 393 ? 0.6662 1.6601 2.0878 0.2526  0.3338  -0.1460 393 ASP C CA  
11653 C C   . ASP C 393 ? 0.6375 1.6016 2.0916 0.2409  0.3319  -0.1037 393 ASP C C   
11654 O O   . ASP C 393 ? 0.6344 1.6172 2.1144 0.2441  0.3443  -0.0934 393 ASP C O   
11655 C CB  . ASP C 393 ? 0.6728 1.6390 2.1114 0.2655  0.3313  -0.1946 393 ASP C CB  
11656 C CG  . ASP C 393 ? 0.7067 1.7049 2.1185 0.2786  0.3346  -0.2419 393 ASP C CG  
11657 O OD1 . ASP C 393 ? 0.7265 1.7696 2.1010 0.2773  0.3371  -0.2387 393 ASP C OD1 
11658 O OD2 . ASP C 393 ? 0.7123 1.6909 2.1415 0.2904  0.3342  -0.2822 393 ASP C OD2 
11659 N N   . ASN C 394 ? 0.6191 1.5393 2.0720 0.2275  0.3164  -0.0803 394 ASN C N   
11660 C CA  . ASN C 394 ? 0.5984 1.4827 2.0802 0.2156  0.3111  -0.0443 394 ASN C CA  
11661 C C   . ASN C 394 ? 0.5845 1.4106 2.0967 0.2177  0.3013  -0.0639 394 ASN C C   
11662 O O   . ASN C 394 ? 0.5728 1.3881 2.1166 0.2152  0.3040  -0.0483 394 ASN C O   
11663 C CB  . ASN C 394 ? 0.6007 1.5297 2.0983 0.2125  0.3271  -0.0100 394 ASN C CB  
11664 C CG  . ASN C 394 ? 0.5783 1.4725 2.1010 0.1976  0.3195  0.0301  394 ASN C CG  
11665 O OD1 . ASN C 394 ? 0.5768 1.4631 2.0872 0.1871  0.3125  0.0575  394 ASN C OD1 
11666 N ND2 . ASN C 394 ? 0.5659 1.4389 2.1251 0.1966  0.3199  0.0333  394 ASN C ND2 
11667 N N   . LYS C 395 ? 0.5942 1.3837 2.0977 0.2216  0.2891  -0.0962 395 LYS C N   
11668 C CA  . LYS C 395 ? 0.5776 1.3098 2.1075 0.2231  0.2780  -0.1132 395 LYS C CA  
11669 C C   . LYS C 395 ? 0.5553 1.2360 2.0761 0.2135  0.2595  -0.1097 395 LYS C C   
11670 O O   . LYS C 395 ? 0.5600 1.2478 2.0527 0.2120  0.2545  -0.1182 395 LYS C O   
11671 C CB  . LYS C 395 ? 0.6011 1.3359 2.1394 0.2386  0.2821  -0.1573 395 LYS C CB  
11672 C CG  . LYS C 395 ? 0.6376 1.3974 2.1463 0.2470  0.2835  -0.1931 395 LYS C CG  
11673 C CD  . LYS C 395 ? 0.6643 1.4380 2.1858 0.2641  0.2921  -0.2350 395 LYS C CD  
11674 C CE  . LYS C 395 ? 0.6978 1.5064 2.1899 0.2733  0.2958  -0.2720 395 LYS C CE  
11675 N NZ  . LYS C 395 ? 0.6983 1.4709 2.1751 0.2678  0.2787  -0.2903 395 LYS C NZ  
11676 N N   . ILE C 396 ? 0.5250 1.1565 2.0699 0.2074  0.2495  -0.0974 396 ILE C N   
11677 C CA  . ILE C 396 ? 0.5069 1.0909 2.0461 0.1982  0.2332  -0.0905 396 ILE C CA  
11678 C C   . ILE C 396 ? 0.5160 1.0763 2.0475 0.2038  0.2246  -0.1264 396 ILE C C   
11679 O O   . ILE C 396 ? 0.5260 1.0735 2.0758 0.2126  0.2252  -0.1514 396 ILE C O   
11680 C CB  . ILE C 396 ? 0.4802 1.0224 2.0468 0.1914  0.2256  -0.0704 396 ILE C CB  
11681 C CG1 . ILE C 396 ? 0.4686 1.0307 2.0435 0.1833  0.2318  -0.0340 396 ILE C CG1 
11682 C CG2 . ILE C 396 ? 0.4678 0.9597 2.0297 0.1842  0.2094  -0.0690 396 ILE C CG2 
11683 C CD1 . ILE C 396 ? 0.4462 0.9670 2.0439 0.1746  0.2219  -0.0139 396 ILE C CD1 
11684 N N   . ILE C 397 ? 0.5178 1.0714 2.0255 0.1982  0.2158  -0.1277 397 ILE C N   
11685 C CA  . ILE C 397 ? 0.5228 1.0543 2.0244 0.2011  0.2062  -0.1595 397 ILE C CA  
11686 C C   . ILE C 397 ? 0.4999 0.9808 2.0060 0.1917  0.1910  -0.1489 397 ILE C C   
11687 O O   . ILE C 397 ? 0.5009 0.9583 2.0065 0.1920  0.1819  -0.1711 397 ILE C O   
11688 C CB  . ILE C 397 ? 0.5465 1.1187 2.0164 0.2034  0.2084  -0.1758 397 ILE C CB  
11689 C CG1 . ILE C 397 ? 0.5403 1.1288 1.9869 0.1938  0.2056  -0.1449 397 ILE C CG1 
11690 C CG2 . ILE C 397 ? 0.5700 1.1931 2.0350 0.2148  0.2240  -0.1932 397 ILE C CG2 
11691 C CD1 . ILE C 397 ? 0.5663 1.1977 1.9804 0.1957  0.2061  -0.1584 397 ILE C CD1 
11692 N N   . LYS C 398 ? 0.4824 0.9476 1.9939 0.1833  0.1884  -0.1157 398 LYS C N   
11693 C CA  . LYS C 398 ? 0.4734 0.8924 1.9901 0.1757  0.1752  -0.1059 398 LYS C CA  
11694 C C   . LYS C 398 ? 0.4508 0.8545 1.9796 0.1689  0.1746  -0.0734 398 LYS C C   
11695 O O   . LYS C 398 ? 0.4427 0.8733 1.9657 0.1659  0.1812  -0.0513 398 LYS C O   
11696 C CB  . LYS C 398 ? 0.4899 0.9112 1.9831 0.1697  0.1677  -0.1027 398 LYS C CB  
11697 C CG  . LYS C 398 ? 0.4765 0.8534 1.9748 0.1623  0.1552  -0.0922 398 LYS C CG  
11698 C CD  . LYS C 398 ? 0.4901 0.8711 1.9685 0.1575  0.1475  -0.0921 398 LYS C CD  
11699 C CE  . LYS C 398 ? 0.4831 0.8228 1.9688 0.1513  0.1368  -0.0826 398 LYS C CE  
11700 N NZ  . LYS C 398 ? 0.4841 0.8321 1.9523 0.1463  0.1307  -0.0735 398 LYS C NZ  
11701 N N   . ASN C 399 ? 0.4383 0.7992 1.9841 0.1664  0.1659  -0.0710 399 ASN C N   
11702 C CA  . ASN C 399 ? 0.4267 0.7672 1.9838 0.1597  0.1624  -0.0447 399 ASN C CA  
11703 C C   . ASN C 399 ? 0.4206 0.7239 1.9731 0.1538  0.1504  -0.0397 399 ASN C C   
11704 O O   . ASN C 399 ? 0.4357 0.7113 1.9963 0.1557  0.1438  -0.0538 399 ASN C O   
11705 C CB  . ASN C 399 ? 0.4191 0.7453 2.0025 0.1629  0.1630  -0.0459 399 ASN C CB  
11706 C CG  . ASN C 399 ? 0.4242 0.7866 2.0179 0.1679  0.1753  -0.0452 399 ASN C CG  
11707 O OD1 . ASN C 399 ? 0.4325 0.8116 2.0298 0.1629  0.1800  -0.0226 399 ASN C OD1 
11708 N ND2 . ASN C 399 ? 0.4365 0.8111 2.0378 0.1778  0.1807  -0.0693 399 ASN C ND2 
11709 N N   . GLU C 400 ? 0.4104 0.7131 1.9523 0.1472  0.1478  -0.0183 400 GLU C N   
11710 C CA  . GLU C 400 ? 0.3948 0.6649 1.9339 0.1422  0.1377  -0.0112 400 GLU C CA  
11711 C C   . GLU C 400 ? 0.3847 0.6443 1.9305 0.1364  0.1362  0.0146  400 GLU C C   
11712 O O   . GLU C 400 ? 0.3761 0.6582 1.9213 0.1341  0.1421  0.0314  400 GLU C O   
11713 C CB  . GLU C 400 ? 0.4027 0.6833 1.9216 0.1411  0.1348  -0.0165 400 GLU C CB  
11714 C CG  . GLU C 400 ? 0.3941 0.6434 1.9112 0.1372  0.1249  -0.0134 400 GLU C CG  
11715 C CD  . GLU C 400 ? 0.3971 0.6546 1.8981 0.1357  0.1203  -0.0195 400 GLU C CD  
11716 O OE1 . GLU C 400 ? 0.4057 0.6953 1.8925 0.1371  0.1235  -0.0247 400 GLU C OE1 
11717 O OE2 . GLU C 400 ? 0.3897 0.6218 1.8928 0.1329  0.1130  -0.0176 400 GLU C OE2 
11718 N N   . SER C 401 ? 0.3732 0.5984 1.9269 0.1340  0.1282  0.0175  401 SER C N   
11719 C CA  . SER C 401 ? 0.3629 0.5734 1.9225 0.1287  0.1249  0.0376  401 SER C CA  
11720 C C   . SER C 401 ? 0.3673 0.5674 1.9138 0.1261  0.1198  0.0454  401 SER C C   
11721 O O   . SER C 401 ? 0.3671 0.5642 1.9031 0.1278  0.1169  0.0338  401 SER C O   
11722 C CB  . SER C 401 ? 0.3476 0.5309 1.9219 0.1284  0.1191  0.0352  401 SER C CB  
11723 O OG  . SER C 401 ? 0.3421 0.5370 1.9317 0.1308  0.1235  0.0313  401 SER C OG  
11724 N N   . ILE C 402 ? 0.3743 0.5692 1.9242 0.1221  0.1186  0.0647  402 ILE C N   
11725 C CA  . ILE C 402 ? 0.3752 0.5529 1.9183 0.1206  0.1127  0.0720  402 ILE C CA  
11726 C C   . ILE C 402 ? 0.3761 0.5276 1.9321 0.1178  0.1080  0.0806  402 ILE C C   
11727 O O   . ILE C 402 ? 0.3810 0.5368 1.9499 0.1146  0.1102  0.0921  402 ILE C O   
11728 C CB  . ILE C 402 ? 0.3788 0.5781 1.9124 0.1198  0.1154  0.0868  402 ILE C CB  
11729 C CG1 . ILE C 402 ? 0.3872 0.6080 1.9040 0.1226  0.1164  0.0753  402 ILE C CG1 
11730 C CG2 . ILE C 402 ? 0.3788 0.5584 1.9145 0.1185  0.1101  0.1000  402 ILE C CG2 
11731 C CD1 . ILE C 402 ? 0.4004 0.6517 1.9133 0.1248  0.1237  0.0660  402 ILE C CD1 
11732 N N   . ASN C 403 ? 0.3654 0.4917 1.9187 0.1187  0.1016  0.0742  403 ASN C N   
11733 C CA  . ASN C 403 ? 0.3694 0.4716 1.9323 0.1170  0.0963  0.0776  403 ASN C CA  
11734 C C   . ASN C 403 ? 0.3775 0.4700 1.9398 0.1162  0.0940  0.0896  403 ASN C C   
11735 O O   . ASN C 403 ? 0.3958 0.4857 1.9476 0.1187  0.0927  0.0882  403 ASN C O   
11736 C CB  . ASN C 403 ? 0.3670 0.4497 1.9266 0.1192  0.0911  0.0648  403 ASN C CB  
11737 C CG  . ASN C 403 ? 0.3764 0.4610 1.9442 0.1200  0.0913  0.0559  403 ASN C CG  
11738 O OD1 . ASN C 403 ? 0.3772 0.4457 1.9476 0.1209  0.0862  0.0505  403 ASN C OD1 
11739 N ND2 . ASN C 403 ? 0.3871 0.4931 1.9595 0.1203  0.0973  0.0550  403 ASN C ND2 
11740 N N   . ILE C 404 ? 0.3664 0.4527 1.9425 0.1128  0.0931  0.1008  404 ILE C N   
11741 C CA  . ILE C 404 ? 0.3625 0.4357 1.9418 0.1129  0.0903  0.1108  404 ILE C CA  
11742 C C   . ILE C 404 ? 0.3653 0.4133 1.9561 0.1112  0.0841  0.1072  404 ILE C C   
11743 O O   . ILE C 404 ? 0.3583 0.4033 1.9566 0.1086  0.0821  0.1011  404 ILE C O   
11744 C CB  . ILE C 404 ? 0.3681 0.4588 1.9545 0.1107  0.0947  0.1302  404 ILE C CB  
11745 C CG1 . ILE C 404 ? 0.3723 0.4682 1.9779 0.1048  0.0966  0.1399  404 ILE C CG1 
11746 C CG2 . ILE C 404 ? 0.3666 0.4857 1.9378 0.1129  0.1000  0.1313  404 ILE C CG2 
11747 C CD1 . ILE C 404 ? 0.3812 0.4915 1.9977 0.1018  0.1005  0.1632  404 ILE C CD1 
11748 N N   . LEU C 405 ? 0.3731 0.4044 1.9650 0.1136  0.0808  0.1099  405 LEU C N   
11749 C CA  . LEU C 405 ? 0.3787 0.3866 1.9826 0.1124  0.0748  0.1067  405 LEU C CA  
11750 C C   . LEU C 405 ? 0.4001 0.4032 2.0202 0.1110  0.0750  0.1226  405 LEU C C   
11751 O O   . LEU C 405 ? 0.4171 0.4197 2.0330 0.1157  0.0763  0.1287  405 LEU C O   
11752 C CB  . LEU C 405 ? 0.3757 0.3675 1.9670 0.1180  0.0709  0.0930  405 LEU C CB  
11753 C CG  . LEU C 405 ? 0.3835 0.3531 1.9828 0.1177  0.0640  0.0839  405 LEU C CG  
11754 C CD1 . LEU C 405 ? 0.3843 0.3543 1.9879 0.1131  0.0599  0.0762  405 LEU C CD1 
11755 C CD2 . LEU C 405 ? 0.3881 0.3466 1.9736 0.1247  0.0621  0.0728  405 LEU C CD2 
11756 N N   . ALA C 406 ? 0.4101 0.4096 2.0513 0.1045  0.0734  0.1301  406 ALA C N   
11757 C CA  . ALA C 406 ? 0.4096 0.4120 2.0700 0.1012  0.0754  0.1508  406 ALA C CA  
11758 C C   . ALA C 406 ? 0.4181 0.3942 2.1026 0.0976  0.0686  0.1501  406 ALA C C   
11759 O O   . ALA C 406 ? 0.4102 0.3756 2.1004 0.0939  0.0631  0.1368  406 ALA C O   
11760 C CB  . ALA C 406 ? 0.4113 0.4403 2.0784 0.0951  0.0815  0.1642  406 ALA C CB  
11761 N N   . SER C 407 ? 0.4286 0.3960 2.1284 0.0987  0.0686  0.1652  407 SER C N   
11762 C CA  . SER C 407 ? 0.4392 0.3824 2.1690 0.0943  0.0626  0.1689  407 SER C CA  
11763 C C   . SER C 407 ? 0.4595 0.4060 2.2093 0.0935  0.0658  0.1962  407 SER C C   
11764 O O   . SER C 407 ? 0.4604 0.4274 2.1970 0.0978  0.0717  0.2100  407 SER C O   
11765 C CB  . SER C 407 ? 0.4396 0.3541 2.1673 0.1002  0.0555  0.1476  407 SER C CB  
11766 O OG  . SER C 407 ? 0.4501 0.3412 2.2064 0.0943  0.0481  0.1440  407 SER C OG  
11767 N N   . LYS C 408 ? 0.4830 0.4096 2.2661 0.0876  0.0610  0.2043  408 LYS C N   
11768 C CA  . LYS C 408 ? 0.5021 0.4295 2.3097 0.0860  0.0633  0.2332  408 LYS C CA  
11769 C C   . LYS C 408 ? 0.5083 0.4121 2.3215 0.0960  0.0599  0.2312  408 LYS C C   
11770 O O   . LYS C 408 ? 0.5172 0.4266 2.3424 0.0987  0.0627  0.2558  408 LYS C O   
11771 C CB  . LYS C 408 ? 0.5310 0.4465 2.3775 0.0740  0.0594  0.2443  408 LYS C CB  
11772 C CG  . LYS C 408 ? 0.5322 0.4711 2.3774 0.0643  0.0624  0.2451  408 LYS C CG  
11773 C CD  . LYS C 408 ? 0.5611 0.4952 2.4484 0.0513  0.0601  0.2631  408 LYS C CD  
11774 C CE  . LYS C 408 ? 0.5550 0.5130 2.4432 0.0423  0.0628  0.2619  408 LYS C CE  
11775 N NZ  . LYS C 408 ? 0.5771 0.5372 2.5076 0.0295  0.0628  0.2865  408 LYS C NZ  
11776 N N   . THR C 409 ? 0.5037 0.3823 2.3105 0.1015  0.0539  0.2028  409 THR C N   
11777 C CA  . THR C 409 ? 0.5079 0.3647 2.3176 0.1129  0.0513  0.1950  409 THR C CA  
11778 C C   . THR C 409 ? 0.4836 0.3453 2.2573 0.1216  0.0523  0.1699  409 THR C C   
11779 O O   . THR C 409 ? 0.4657 0.3428 2.2169 0.1181  0.0537  0.1592  409 THR C O   
11780 C CB  . THR C 409 ? 0.5315 0.3511 2.3747 0.1114  0.0428  0.1847  409 THR C CB  
11781 O OG1 . THR C 409 ? 0.5403 0.3395 2.3837 0.1243  0.0408  0.1715  409 THR C OG1 
11782 C CG2 . THR C 409 ? 0.5354 0.3422 2.3753 0.1057  0.0360  0.1564  409 THR C CG2 
11783 N N   . ALA C 410 ? 0.4852 0.3338 2.2564 0.1332  0.0516  0.1614  410 ALA C N   
11784 C CA  . ALA C 410 ? 0.4672 0.3230 2.2072 0.1419  0.0537  0.1419  410 ALA C CA  
11785 C C   . ALA C 410 ? 0.4641 0.3062 2.1935 0.1409  0.0487  0.1126  410 ALA C C   
11786 O O   . ALA C 410 ? 0.4751 0.2936 2.2245 0.1384  0.0422  0.1018  410 ALA C O   
11787 C CB  . ALA C 410 ? 0.4761 0.3241 2.2220 0.1546  0.0549  0.1443  410 ALA C CB  
11788 N N   . PHE C 411 ? 0.4485 0.3062 2.1469 0.1428  0.0511  0.0997  411 PHE C N   
11789 C CA  . PHE C 411 ? 0.4528 0.3010 2.1378 0.1438  0.0466  0.0735  411 PHE C CA  
11790 C C   . PHE C 411 ? 0.4425 0.2988 2.1015 0.1541  0.0504  0.0612  411 PHE C C   
11791 O O   . PHE C 411 ? 0.4258 0.2986 2.0744 0.1581  0.0563  0.0724  411 PHE C O   
11792 C CB  . PHE C 411 ? 0.4433 0.3027 2.1195 0.1339  0.0446  0.0703  411 PHE C CB  
11793 C CG  . PHE C 411 ? 0.4255 0.3119 2.0856 0.1311  0.0512  0.0840  411 PHE C CG  
11794 C CD1 . PHE C 411 ? 0.4229 0.3220 2.0953 0.1257  0.0550  0.1065  411 PHE C CD1 
11795 C CD2 . PHE C 411 ? 0.4156 0.3154 2.0489 0.1338  0.0534  0.0742  411 PHE C CD2 
11796 C CE1 . PHE C 411 ? 0.4052 0.3303 2.0618 0.1237  0.0608  0.1155  411 PHE C CE1 
11797 C CE2 . PHE C 411 ? 0.3960 0.3184 2.0171 0.1311  0.0586  0.0838  411 PHE C CE2 
11798 C CZ  . PHE C 411 ? 0.3905 0.3257 2.0223 0.1265  0.0623  0.1029  411 PHE C CZ  
11799 N N   . GLU C 412 ? 0.4543 0.2996 2.1046 0.1581  0.0464  0.0379  412 GLU C N   
11800 C CA  . GLU C 412 ? 0.4513 0.3053 2.0767 0.1668  0.0496  0.0243  412 GLU C CA  
11801 C C   . GLU C 412 ? 0.4326 0.3086 2.0347 0.1621  0.0526  0.0282  412 GLU C C   
11802 O O   . GLU C 412 ? 0.4261 0.3068 2.0288 0.1528  0.0499  0.0318  412 GLU C O   
11803 C CB  . GLU C 412 ? 0.4755 0.3148 2.0976 0.1705  0.0437  -0.0012 412 GLU C CB  
11804 C CG  . GLU C 412 ? 0.4753 0.3277 2.0687 0.1781  0.0469  -0.0153 412 GLU C CG  
11805 C CD  . GLU C 412 ? 0.5069 0.3483 2.0949 0.1843  0.0420  -0.0414 412 GLU C CD  
11806 O OE1 . GLU C 412 ? 0.5341 0.3572 2.1383 0.1916  0.0403  -0.0532 412 GLU C OE1 
11807 O OE2 . GLU C 412 ? 0.4998 0.3532 2.0659 0.1821  0.0399  -0.0504 412 GLU C OE2 
11808 N N   . LEU C 413 ? 0.4214 0.3110 2.0060 0.1689  0.0582  0.0277  413 LEU C N   
11809 C CA  . LEU C 413 ? 0.4016 0.3099 1.9655 0.1661  0.0611  0.0294  413 LEU C CA  
11810 C C   . LEU C 413 ? 0.4100 0.3227 1.9562 0.1739  0.0629  0.0158  413 LEU C C   
11811 O O   . LEU C 413 ? 0.4171 0.3236 1.9661 0.1830  0.0646  0.0083  413 LEU C O   
11812 C CB  . LEU C 413 ? 0.3835 0.3075 1.9479 0.1654  0.0665  0.0465  413 LEU C CB  
11813 C CG  . LEU C 413 ? 0.3776 0.3041 1.9560 0.1579  0.0660  0.0619  413 LEU C CG  
11814 C CD1 . LEU C 413 ? 0.3699 0.3127 1.9485 0.1595  0.0706  0.0772  413 LEU C CD1 
11815 C CD2 . LEU C 413 ? 0.3683 0.3024 1.9403 0.1493  0.0645  0.0612  413 LEU C CD2 
11816 N N   . PRO C 414 ? 0.4121 0.3364 1.9404 0.1713  0.0631  0.0127  414 PRO C N   
11817 C CA  . PRO C 414 ? 0.4285 0.3625 1.9396 0.1783  0.0665  0.0048  414 PRO C CA  
11818 C C   . PRO C 414 ? 0.4331 0.3803 1.9442 0.1820  0.0739  0.0160  414 PRO C C   
11819 O O   . PRO C 414 ? 0.4191 0.3716 1.9376 0.1772  0.0751  0.0289  414 PRO C O   
11820 C CB  . PRO C 414 ? 0.4200 0.3621 1.9166 0.1729  0.0636  0.0029  414 PRO C CB  
11821 C CG  . PRO C 414 ? 0.4037 0.3455 1.9100 0.1635  0.0614  0.0133  414 PRO C CG  
11822 C CD  . PRO C 414 ? 0.4033 0.3331 1.9290 0.1621  0.0602  0.0175  414 PRO C CD  
11823 N N   . GLU C 415 ? 0.4549 0.4092 1.9589 0.1909  0.0785  0.0102  415 GLU C N   
11824 C CA  . GLU C 415 ? 0.4628 0.4294 1.9714 0.1956  0.0849  0.0196  415 GLU C CA  
11825 C C   . GLU C 415 ? 0.4500 0.4345 1.9437 0.1994  0.0903  0.0176  415 GLU C C   
11826 O O   . GLU C 415 ? 0.4577 0.4427 1.9404 0.2051  0.0910  0.0054  415 GLU C O   
11827 C CB  . GLU C 415 ? 0.5089 0.4648 2.0335 0.2044  0.0857  0.0172  415 GLU C CB  
11828 C CG  . GLU C 415 ? 0.5413 0.4842 2.0842 0.1995  0.0815  0.0267  415 GLU C CG  
11829 C CD  . GLU C 415 ? 0.5593 0.5155 2.1087 0.1954  0.0834  0.0451  415 GLU C CD  
11830 O OE1 . GLU C 415 ? 0.6302 0.6003 2.1809 0.2014  0.0879  0.0503  415 GLU C OE1 
11831 O OE2 . GLU C 415 ? 0.5562 0.5113 2.1099 0.1869  0.0804  0.0541  415 GLU C OE2 
11832 N N   . LEU C 416 ? 0.4176 0.4177 1.9116 0.1953  0.0937  0.0299  416 LEU C N   
11833 C CA  . LEU C 416 ? 0.4104 0.4291 1.8949 0.1971  0.0993  0.0323  416 LEU C CA  
11834 C C   . LEU C 416 ? 0.3914 0.4238 1.8868 0.2021  0.1047  0.0398  416 LEU C C   
11835 O O   . LEU C 416 ? 0.3766 0.4095 1.8838 0.1990  0.1031  0.0483  416 LEU C O   
11836 C CB  . LEU C 416 ? 0.4064 0.4309 1.8849 0.1867  0.0973  0.0396  416 LEU C CB  
11837 C CG  . LEU C 416 ? 0.4105 0.4531 1.8810 0.1866  0.1023  0.0446  416 LEU C CG  
11838 C CD1 . LEU C 416 ? 0.4086 0.4511 1.8752 0.1772  0.0989  0.0504  416 LEU C CD1 
11839 C CD2 . LEU C 416 ? 0.4008 0.4602 1.8813 0.1874  0.1078  0.0537  416 LEU C CD2 
11840 N N   . THR C 417 ? 0.3936 0.4393 1.8850 0.2107  0.1113  0.0362  417 THR C N   
11841 C CA  . THR C 417 ? 0.3863 0.4485 1.8891 0.2171  0.1173  0.0425  417 THR C CA  
11842 C C   . THR C 417 ? 0.3968 0.4815 1.8912 0.2189  0.1245  0.0447  417 THR C C   
11843 O O   . THR C 417 ? 0.4050 0.4902 1.8835 0.2194  0.1254  0.0384  417 THR C O   
11844 C CB  . THR C 417 ? 0.3909 0.4438 1.9038 0.2296  0.1186  0.0342  417 THR C CB  
11845 O OG1 . THR C 417 ? 0.4030 0.4544 1.9039 0.2381  0.1218  0.0190  417 THR C OG1 
11846 C CG2 . THR C 417 ? 0.3885 0.4177 1.9104 0.2268  0.1112  0.0335  417 THR C CG2 
11847 N N   . ILE C 418 ? 0.3984 0.5036 1.9041 0.2194  0.1294  0.0550  418 ILE C N   
11848 C CA  . ILE C 418 ? 0.4033 0.5325 1.9050 0.2191  0.1367  0.0610  418 ILE C CA  
11849 C C   . ILE C 418 ? 0.4077 0.5580 1.9231 0.2287  0.1443  0.0642  418 ILE C C   
11850 O O   . ILE C 418 ? 0.4087 0.5592 1.9402 0.2292  0.1417  0.0691  418 ILE C O   
11851 C CB  . ILE C 418 ? 0.3952 0.5309 1.9007 0.2047  0.1337  0.0738  418 ILE C CB  
11852 C CG1 . ILE C 418 ? 0.3835 0.5246 1.9074 0.1995  0.1303  0.0819  418 ILE C CG1 
11853 C CG2 . ILE C 418 ? 0.3968 0.5131 1.8905 0.1965  0.1268  0.0706  418 ILE C CG2 
11854 C CD1 . ILE C 418 ? 0.3728 0.5243 1.9042 0.1862  0.1281  0.0924  418 ILE C CD1 
11855 N N   . GLU C 419 ? 0.4209 0.5921 1.9300 0.2355  0.1535  0.0633  419 GLU C N   
11856 C CA  . GLU C 419 ? 0.4233 0.6202 1.9460 0.2452  0.1626  0.0670  419 GLU C CA  
11857 C C   . GLU C 419 ? 0.4236 0.6483 1.9488 0.2372  0.1685  0.0817  419 GLU C C   
11858 O O   . GLU C 419 ? 0.4359 0.6658 1.9451 0.2343  0.1713  0.0828  419 GLU C O   
11859 C CB  . GLU C 419 ? 0.4446 0.6451 1.9585 0.2622  0.1701  0.0513  419 GLU C CB  
11860 C CG  . GLU C 419 ? 0.4555 0.6302 1.9748 0.2723  0.1655  0.0368  419 GLU C CG  
11861 C CD  . GLU C 419 ? 0.4866 0.6637 1.9971 0.2890  0.1725  0.0175  419 GLU C CD  
11862 O OE1 . GLU C 419 ? 0.4916 0.6746 1.9795 0.2890  0.1751  0.0099  419 GLU C OE1 
11863 O OE2 . GLU C 419 ? 0.5076 0.6826 2.0340 0.3027  0.1755  0.0101  419 GLU C OE2 
11864 N N   . VAL C 420 ? 0.4151 0.6591 1.9619 0.2340  0.1700  0.0938  420 VAL C N   
11865 C CA  . VAL C 420 ? 0.4051 0.6711 1.9615 0.2219  0.1723  0.1098  420 VAL C CA  
11866 C C   . VAL C 420 ? 0.4190 0.7204 1.9896 0.2302  0.1838  0.1166  420 VAL C C   
11867 O O   . VAL C 420 ? 0.4292 0.7384 2.0145 0.2400  0.1854  0.1140  420 VAL C O   
11868 C CB  . VAL C 420 ? 0.3874 0.6461 1.9595 0.2080  0.1620  0.1174  420 VAL C CB  
11869 C CG1 . VAL C 420 ? 0.3824 0.6587 1.9669 0.1938  0.1625  0.1320  420 VAL C CG1 
11870 C CG2 . VAL C 420 ? 0.3842 0.6100 1.9444 0.2017  0.1514  0.1098  420 VAL C CG2 
11871 N N   . THR C 421 ? 0.4224 0.7475 1.9911 0.2262  0.1920  0.1272  421 THR C N   
11872 C CA  . THR C 421 ? 0.4219 0.7851 2.0080 0.2318  0.2033  0.1368  421 THR C CA  
11873 C C   . THR C 421 ? 0.4147 0.7945 2.0231 0.2144  0.2009  0.1561  421 THR C C   
11874 O O   . THR C 421 ? 0.4046 0.7713 2.0093 0.2000  0.1948  0.1627  421 THR C O   
11875 C CB  . THR C 421 ? 0.4377 0.8218 2.0063 0.2431  0.2166  0.1341  421 THR C CB  
11876 O OG1 . THR C 421 ? 0.4442 0.8097 1.9979 0.2588  0.2162  0.1129  421 THR C OG1 
11877 C CG2 . THR C 421 ? 0.4434 0.8708 2.0297 0.2506  0.2304  0.1437  421 THR C CG2 
11878 N N   . PRO C 422 ? 0.4157 0.8231 2.0512 0.2149  0.2042  0.1648  422 PRO C N   
11879 C CA  . PRO C 422 ? 0.4131 0.8270 2.0600 0.2296  0.2054  0.1568  422 PRO C CA  
11880 C C   . PRO C 422 ? 0.4040 0.7849 2.0483 0.2285  0.1918  0.1469  422 PRO C C   
11881 O O   . PRO C 422 ? 0.4089 0.7706 2.0508 0.2140  0.1811  0.1488  422 PRO C O   
11882 C CB  . PRO C 422 ? 0.4047 0.8555 2.0844 0.2242  0.2085  0.1724  422 PRO C CB  
11883 C CG  . PRO C 422 ? 0.4062 0.8762 2.0888 0.2115  0.2148  0.1878  422 PRO C CG  
11884 C CD  . PRO C 422 ? 0.4087 0.8442 2.0682 0.2012  0.2068  0.1841  422 PRO C CD  
11885 N N   . GLU C 423 ? 0.4137 0.7889 2.0603 0.2441  0.1923  0.1371  423 GLU C N   
11886 C CA  . GLU C 423 ? 0.4097 0.7538 2.0523 0.2447  0.1807  0.1291  423 GLU C CA  
11887 C C   . GLU C 423 ? 0.3961 0.7505 2.0618 0.2371  0.1715  0.1390  423 GLU C C   
11888 O O   . GLU C 423 ? 0.3863 0.7198 2.0484 0.2306  0.1603  0.1372  423 GLU C O   
11889 C CB  . GLU C 423 ? 0.4271 0.7600 2.0648 0.2649  0.1853  0.1154  423 GLU C CB  
11890 C CG  . GLU C 423 ? 0.4293 0.7305 2.0658 0.2675  0.1747  0.1088  423 GLU C CG  
11891 C CD  . GLU C 423 ? 0.4457 0.7402 2.0901 0.2878  0.1786  0.0989  423 GLU C CD  
11892 O OE1 . GLU C 423 ? 0.4475 0.7688 2.1121 0.2981  0.1852  0.1037  423 GLU C OE1 
11893 O OE2 . GLU C 423 ? 0.4592 0.7229 2.0932 0.2933  0.1749  0.0869  423 GLU C OE2 
11894 N N   . LYS C 424 ? 0.4030 0.7924 2.0927 0.2383  0.1760  0.1493  424 LYS C N   
11895 C CA  . LYS C 424 ? 0.4033 0.8058 2.1156 0.2364  0.1673  0.1567  424 LYS C CA  
11896 C C   . LYS C 424 ? 0.3909 0.8226 2.1238 0.2207  0.1648  0.1693  424 LYS C C   
11897 O O   . LYS C 424 ? 0.3877 0.8186 2.1284 0.2086  0.1525  0.1724  424 LYS C O   
11898 C CB  . LYS C 424 ? 0.4233 0.8436 2.1536 0.2560  0.1732  0.1571  424 LYS C CB  
11899 C CG  . LYS C 424 ? 0.4465 0.8406 2.1658 0.2741  0.1757  0.1445  424 LYS C CG  
11900 C CD  . LYS C 424 ? 0.4643 0.8743 2.2090 0.2910  0.1768  0.1482  424 LYS C CD  
11901 C CE  . LYS C 424 ? 0.4845 0.8816 2.2282 0.3131  0.1851  0.1357  424 LYS C CE  
11902 N NZ  . LYS C 424 ? 0.4897 0.9087 2.2641 0.3284  0.1866  0.1425  424 LYS C NZ  
11903 N N   . ASP C 425 ? 0.3828 0.8421 2.1258 0.2212  0.1763  0.1764  425 ASP C N   
11904 C CA  . ASP C 425 ? 0.3746 0.8634 2.1421 0.2060  0.1747  0.1897  425 ASP C CA  
11905 C C   . ASP C 425 ? 0.3913 0.8837 2.1522 0.1960  0.1828  0.1956  425 ASP C C   
11906 O O   . ASP C 425 ? 0.4217 0.9264 2.1751 0.2070  0.1969  0.1965  425 ASP C O   
11907 C CB  . ASP C 425 ? 0.3668 0.8949 2.1631 0.2165  0.1805  0.1977  425 ASP C CB  
11908 C CG  . ASP C 425 ? 0.3533 0.9201 2.1807 0.2033  0.1815  0.2126  425 ASP C CG  
11909 O OD1 . ASP C 425 ? 0.3434 0.9050 2.1711 0.1846  0.1777  0.2173  425 ASP C OD1 
11910 O OD2 . ASP C 425 ? 0.3491 0.9508 2.2026 0.2122  0.1859  0.2197  425 ASP C OD2 
11911 N N   . LEU C 426 ? 0.3750 0.8603 2.1417 0.1755  0.1740  0.2007  426 LEU C N   
11912 C CA  . LEU C 426 ? 0.3761 0.8611 2.1395 0.1639  0.1793  0.2091  426 LEU C CA  
11913 C C   . LEU C 426 ? 0.3796 0.9067 2.1677 0.1621  0.1914  0.2258  426 LEU C C   
11914 O O   . LEU C 426 ? 0.3808 0.9120 2.1655 0.1554  0.1987  0.2357  426 LEU C O   
11915 C CB  . LEU C 426 ? 0.3743 0.8389 2.1430 0.1432  0.1654  0.2089  426 LEU C CB  
11916 C CG  . LEU C 426 ? 0.3667 0.7899 2.1094 0.1426  0.1550  0.1939  426 LEU C CG  
11917 C CD1 . LEU C 426 ? 0.3601 0.7662 2.1099 0.1228  0.1433  0.1933  426 LEU C CD1 
11918 C CD2 . LEU C 426 ? 0.3703 0.7715 2.0816 0.1539  0.1625  0.1874  426 LEU C CD2 
11919 N N   . ASN C 427 ? 0.3768 0.9369 2.1909 0.1677  0.1934  0.2307  427 ASN C N   
11920 C CA  . ASN C 427 ? 0.3782 0.9826 2.2175 0.1679  0.2063  0.2468  427 ASN C CA  
11921 C C   . ASN C 427 ? 0.3842 1.0012 2.2046 0.1872  0.2248  0.2455  427 ASN C C   
11922 O O   . ASN C 427 ? 0.3934 1.0456 2.2269 0.1873  0.2382  0.2596  427 ASN C O   
11923 C CB  . ASN C 427 ? 0.3789 1.0170 2.2529 0.1692  0.2029  0.2521  427 ASN C CB  
11924 C CG  . ASN C 427 ? 0.3771 1.0244 2.2813 0.1457  0.1896  0.2608  427 ASN C CG  
11925 O OD1 . ASN C 427 ? 0.3788 1.0231 2.2933 0.1416  0.1751  0.2547  427 ASN C OD1 
11926 N ND2 . ASN C 427 ? 0.3816 1.0422 2.3020 0.1300  0.1941  0.2754  427 ASN C ND2 
11927 N N   . GLU C 428 ? 0.3894 0.9794 2.1792 0.2033  0.2258  0.2286  428 GLU C N   
11928 C CA  . GLU C 428 ? 0.4101 1.0142 2.1836 0.2237  0.2423  0.2230  428 GLU C CA  
11929 C C   . GLU C 428 ? 0.4178 1.0253 2.1707 0.2196  0.2523  0.2296  428 GLU C C   
11930 O O   . GLU C 428 ? 0.4390 1.0722 2.1834 0.2336  0.2682  0.2298  428 GLU C O   
11931 C CB  . GLU C 428 ? 0.4207 0.9960 2.1744 0.2420  0.2389  0.2019  428 GLU C CB  
11932 C CG  . GLU C 428 ? 0.4269 1.0174 2.2072 0.2521  0.2358  0.2009  428 GLU C CG  
11933 C CD  . GLU C 428 ? 0.4451 1.0313 2.2195 0.2775  0.2422  0.1857  428 GLU C CD  
11934 O OE1 . GLU C 428 ? 0.4734 1.0331 2.2192 0.2878  0.2451  0.1701  428 GLU C OE1 
11935 O OE2 . GLU C 428 ? 0.4468 1.0578 2.2487 0.2872  0.2439  0.1896  428 GLU C OE2 
11936 N N   . GLY C 429 ? 0.4092 0.9932 2.1545 0.2014  0.2435  0.2356  429 GLY C N   
11937 C CA  . GLY C 429 ? 0.4174 1.0068 2.1458 0.1969  0.2521  0.2458  429 GLY C CA  
11938 C C   . GLY C 429 ? 0.4089 0.9866 2.1512 0.1726  0.2428  0.2613  429 GLY C C   
11939 O O   . GLY C 429 ? 0.3983 0.9577 2.1574 0.1601  0.2284  0.2590  429 GLY C O   
11940 N N   . LYS C 430 ? 0.4131 1.0032 2.1490 0.1668  0.2511  0.2774  430 LYS C N   
11941 C CA  . LYS C 430 ? 0.4026 0.9772 2.1501 0.1454  0.2428  0.2923  430 LYS C CA  
11942 C C   . LYS C 430 ? 0.3984 0.9321 2.1125 0.1458  0.2353  0.2818  430 LYS C C   
11943 O O   . LYS C 430 ? 0.3969 0.9058 2.1191 0.1299  0.2244  0.2871  430 LYS C O   
11944 C CB  . LYS C 430 ? 0.4174 1.0319 2.1826 0.1382  0.2562  0.3202  430 LYS C CB  
11945 C CG  . LYS C 430 ? 0.4185 1.0746 2.2226 0.1350  0.2626  0.3323  430 LYS C CG  
11946 C CD  . LYS C 430 ? 0.4301 1.1173 2.2671 0.1177  0.2692  0.3634  430 LYS C CD  
11947 C CE  . LYS C 430 ? 0.4282 1.0836 2.2846 0.0946  0.2536  0.3709  430 LYS C CE  
11948 N NZ  . LYS C 430 ? 0.4439 1.1283 2.3353 0.0778  0.2602  0.4022  430 LYS C NZ  
11949 N N   . ILE C 431 ? 0.3987 0.9261 2.0778 0.1640  0.2407  0.2661  431 ILE C N   
11950 C CA  . ILE C 431 ? 0.3959 0.8897 2.0422 0.1659  0.2346  0.2562  431 ILE C CA  
11951 C C   . ILE C 431 ? 0.3899 0.8530 2.0181 0.1774  0.2265  0.2292  431 ILE C C   
11952 O O   . ILE C 431 ? 0.3907 0.8663 2.0164 0.1926  0.2325  0.2175  431 ILE C O   
11953 C CB  . ILE C 431 ? 0.4093 0.9254 2.0289 0.1761  0.2479  0.2625  431 ILE C CB  
11954 C CG1 . ILE C 431 ? 0.4152 0.9603 2.0517 0.1637  0.2556  0.2932  431 ILE C CG1 
11955 C CG2 . ILE C 431 ? 0.4137 0.8974 1.9978 0.1811  0.2408  0.2481  431 ILE C CG2 
11956 C CD1 . ILE C 431 ? 0.4373 1.0167 2.0490 0.1751  0.2712  0.3022  431 ILE C CD1 
11957 N N   . ALA C 432 ? 0.3899 0.8136 2.0070 0.1706  0.2132  0.2201  432 ALA C N   
11958 C CA  . ALA C 432 ? 0.3872 0.7804 1.9884 0.1793  0.2049  0.1971  432 ALA C CA  
11959 C C   . ALA C 432 ? 0.4008 0.7758 1.9677 0.1876  0.2048  0.1861  432 ALA C C   
11960 O O   . ALA C 432 ? 0.4080 0.7919 1.9637 0.1845  0.2090  0.1974  432 ALA C O   
11961 C CB  . ALA C 432 ? 0.3704 0.7364 1.9861 0.1659  0.1901  0.1940  432 ALA C CB  
11962 N N   . SER C 433 ? 0.4058 0.7572 1.9577 0.1979  0.1997  0.1652  433 SER C N   
11963 C CA  . SER C 433 ? 0.4176 0.7443 1.9410 0.2025  0.1950  0.1520  433 SER C CA  
11964 C C   . SER C 433 ? 0.4091 0.7009 1.9317 0.2023  0.1831  0.1364  433 SER C C   
11965 O O   . SER C 433 ? 0.4041 0.6954 1.9403 0.2068  0.1820  0.1308  433 SER C O   
11966 C CB  . SER C 433 ? 0.4398 0.7819 1.9404 0.2196  0.2049  0.1408  433 SER C CB  
11967 O OG  . SER C 433 ? 0.4400 0.7702 1.9384 0.2331  0.2041  0.1206  433 SER C OG  
11968 N N   . ILE C 434 ? 0.4204 0.6854 1.9276 0.1976  0.1745  0.1307  434 ILE C N   
11969 C CA  . ILE C 434 ? 0.4150 0.6486 1.9164 0.1993  0.1649  0.1151  434 ILE C CA  
11970 C C   . ILE C 434 ? 0.4443 0.6674 1.9200 0.2088  0.1647  0.1009  434 ILE C C   
11971 O O   . ILE C 434 ? 0.4620 0.6824 1.9239 0.2043  0.1626  0.1047  434 ILE C O   
11972 C CB  . ILE C 434 ? 0.3900 0.6018 1.8994 0.1848  0.1539  0.1193  434 ILE C CB  
11973 C CG1 . ILE C 434 ? 0.3703 0.5915 1.9050 0.1753  0.1522  0.1292  434 ILE C CG1 
11974 C CG2 . ILE C 434 ? 0.3921 0.5750 1.8934 0.1872  0.1454  0.1044  434 ILE C CG2 
11975 C CD1 . ILE C 434 ? 0.3559 0.5610 1.8997 0.1606  0.1430  0.1335  434 ILE C CD1 
11976 N N   . LYS C 435 ? 0.4647 0.6822 1.9361 0.2218  0.1663  0.0846  435 LYS C N   
11977 C CA  . LYS C 435 ? 0.4956 0.7017 1.9453 0.2311  0.1650  0.0673  435 LYS C CA  
11978 C C   . LYS C 435 ? 0.4904 0.6623 1.9415 0.2282  0.1537  0.0563  435 LYS C C   
11979 O O   . LYS C 435 ? 0.5037 0.6658 1.9677 0.2334  0.1525  0.0501  435 LYS C O   
11980 C CB  . LYS C 435 ? 0.5290 0.7485 1.9746 0.2483  0.1738  0.0532  435 LYS C CB  
11981 C CG  . LYS C 435 ? 0.5601 0.8166 1.9973 0.2546  0.1865  0.0597  435 LYS C CG  
11982 C CD  . LYS C 435 ? 0.5988 0.8702 2.0292 0.2734  0.1960  0.0421  435 LYS C CD  
11983 C CE  . LYS C 435 ? 0.6051 0.8773 2.0595 0.2821  0.1996  0.0387  435 LYS C CE  
11984 N NZ  . LYS C 435 ? 0.6262 0.9265 2.0791 0.2994  0.2129  0.0293  435 LYS C NZ  
11985 N N   . THR C 436 ? 0.4817 0.6382 1.9206 0.2207  0.1460  0.0552  436 THR C N   
11986 C CA  . THR C 436 ? 0.4633 0.5903 1.9042 0.2158  0.1354  0.0477  436 THR C CA  
11987 C C   . THR C 436 ? 0.4665 0.5796 1.8955 0.2251  0.1325  0.0277  436 THR C C   
11988 O O   . THR C 436 ? 0.4746 0.5986 1.8861 0.2319  0.1355  0.0193  436 THR C O   
11989 C CB  . THR C 436 ? 0.4627 0.5827 1.8997 0.2034  0.1290  0.0570  436 THR C CB  
11990 O OG1 . THR C 436 ? 0.4623 0.5986 1.9085 0.1958  0.1328  0.0744  436 THR C OG1 
11991 C CG2 . THR C 436 ? 0.4491 0.5443 1.8949 0.1961  0.1198  0.0543  436 THR C CG2 
11992 N N   . LYS C 437 ? 0.4629 0.5525 1.9021 0.2251  0.1262  0.0200  437 LYS C N   
11993 C CA  . LYS C 437 ? 0.4924 0.5642 1.9250 0.2311  0.1212  0.0012  437 LYS C CA  
11994 C C   . LYS C 437 ? 0.5079 0.5545 1.9490 0.2220  0.1112  0.0015  437 LYS C C   
11995 O O   . LYS C 437 ? 0.5171 0.5553 1.9751 0.2194  0.1101  0.0084  437 LYS C O   
11996 C CB  . LYS C 437 ? 0.5019 0.5705 1.9450 0.2440  0.1255  -0.0102 437 LYS C CB  
11997 C CG  . LYS C 437 ? 0.5128 0.5566 1.9584 0.2490  0.1189  -0.0292 437 LYS C CG  
11998 C CD  . LYS C 437 ? 0.5165 0.5545 1.9797 0.2615  0.1230  -0.0370 437 LYS C CD  
11999 C CE  . LYS C 437 ? 0.5352 0.5486 2.0036 0.2679  0.1171  -0.0580 437 LYS C CE  
12000 N NZ  . LYS C 437 ? 0.5422 0.5461 2.0340 0.2790  0.1201  -0.0611 437 LYS C NZ  
12001 N N   . ILE C 438 ? 0.5281 0.5657 1.9577 0.2176  0.1041  -0.0055 438 ILE C N   
12002 C CA  . ILE C 438 ? 0.5197 0.5359 1.9573 0.2093  0.0950  -0.0062 438 ILE C CA  
12003 C C   . ILE C 438 ? 0.5386 0.5376 1.9772 0.2147  0.0896  -0.0251 438 ILE C C   
12004 O O   . ILE C 438 ? 0.5611 0.5647 1.9841 0.2189  0.0878  -0.0384 438 ILE C O   
12005 C CB  . ILE C 438 ? 0.5188 0.5383 1.9466 0.2000  0.0901  0.0005  438 ILE C CB  
12006 C CG1 . ILE C 438 ? 0.5049 0.5416 1.9318 0.1958  0.0954  0.0170  438 ILE C CG1 
12007 C CG2 . ILE C 438 ? 0.5096 0.5111 1.9482 0.1912  0.0820  0.0019  438 ILE C CG2 
12008 C CD1 . ILE C 438 ? 0.5109 0.5546 1.9263 0.1904  0.0920  0.0230  438 ILE C CD1 
12009 N N   . GLU C 439 ? 0.5361 0.5166 1.9939 0.2141  0.0868  -0.0257 439 GLU C N   
12010 C CA  . GLU C 439 ? 0.5543 0.5137 2.0194 0.2155  0.0796  -0.0412 439 GLU C CA  
12011 C C   . GLU C 439 ? 0.5290 0.4784 1.9964 0.2035  0.0707  -0.0381 439 GLU C C   
12012 O O   . GLU C 439 ? 0.4942 0.4391 1.9738 0.1958  0.0697  -0.0243 439 GLU C O   
12013 C CB  . GLU C 439 ? 0.5730 0.5169 2.0612 0.2203  0.0806  -0.0407 439 GLU C CB  
12014 C CG  . GLU C 439 ? 0.6036 0.5551 2.0934 0.2344  0.0885  -0.0480 439 GLU C CG  
12015 C CD  . GLU C 439 ? 0.6355 0.5663 2.1486 0.2421  0.0871  -0.0553 439 GLU C CD  
12016 O OE1 . GLU C 439 ? 0.6491 0.5595 2.1796 0.2355  0.0803  -0.0515 439 GLU C OE1 
12017 O OE2 . GLU C 439 ? 0.6746 0.6102 2.1902 0.2551  0.0931  -0.0647 439 GLU C OE2 
12018 N N   . THR C 440 ? 0.5391 0.4876 1.9944 0.2024  0.0641  -0.0514 440 THR C N   
12019 C CA  . THR C 440 ? 0.5377 0.4791 1.9963 0.1919  0.0553  -0.0495 440 THR C CA  
12020 C C   . THR C 440 ? 0.5623 0.4810 2.0439 0.1885  0.0493  -0.0545 440 THR C C   
12021 O O   . THR C 440 ? 0.6083 0.5155 2.1018 0.1951  0.0514  -0.0608 440 THR C O   
12022 C CB  . THR C 440 ? 0.5487 0.4991 1.9880 0.1922  0.0491  -0.0617 440 THR C CB  
12023 O OG1 . THR C 440 ? 0.5679 0.5109 2.0056 0.2003  0.0468  -0.0834 440 THR C OG1 
12024 C CG2 . THR C 440 ? 0.5447 0.5188 1.9629 0.1943  0.0545  -0.0527 440 THR C CG2 
12025 N N   . SER C 441 ? 0.5705 0.4833 2.0600 0.1785  0.0419  -0.0512 441 SER C N   
12026 C CA  . SER C 441 ? 0.5852 0.4789 2.0993 0.1727  0.0364  -0.0516 441 SER C CA  
12027 C C   . SER C 441 ? 0.5939 0.4886 2.1107 0.1625  0.0277  -0.0517 441 SER C C   
12028 O O   . SER C 441 ? 0.5782 0.4860 2.0882 0.1580  0.0294  -0.0395 441 SER C O   
12029 C CB  . SER C 441 ? 0.5735 0.4651 2.1032 0.1704  0.0425  -0.0326 441 SER C CB  
12030 O OG  . SER C 441 ? 0.6079 0.4833 2.1626 0.1642  0.0376  -0.0296 441 SER C OG  
12031 N N   . GLU C 442 ? 0.6395 0.5208 2.1687 0.1589  0.0181  -0.0653 442 GLU C N   
12032 C CA  . GLU C 442 ? 0.6589 0.5460 2.1879 0.1505  0.0089  -0.0679 442 GLU C CA  
12033 C C   . GLU C 442 ? 0.6092 0.4993 2.1544 0.1410  0.0106  -0.0481 442 GLU C C   
12034 O O   . GLU C 442 ? 0.5937 0.4781 2.1535 0.1397  0.0167  -0.0351 442 GLU C O   
12035 C CB  . GLU C 442 ? 0.7093 0.5854 2.2452 0.1487  -0.0031 -0.0900 442 GLU C CB  
12036 C CG  . GLU C 442 ? 0.7598 0.6130 2.3284 0.1431  -0.0073 -0.0919 442 GLU C CG  
12037 C CD  . GLU C 442 ? 0.8346 0.6741 2.4101 0.1433  -0.0190 -0.1185 442 GLU C CD  
12038 O OE1 . GLU C 442 ? 0.8897 0.7416 2.4413 0.1473  -0.0240 -0.1348 442 GLU C OE1 
12039 O OE2 . GLU C 442 ? 0.8444 0.6617 2.4487 0.1398  -0.0232 -0.1234 442 GLU C OE2 
12040 N N   . ASN C 443 ? 0.5826 0.4852 2.1230 0.1357  0.0060  -0.0451 443 ASN C N   
12041 C CA  . ASN C 443 ? 0.5830 0.4921 2.1373 0.1280  0.0080  -0.0288 443 ASN C CA  
12042 C C   . ASN C 443 ? 0.5614 0.4806 2.1066 0.1310  0.0189  -0.0136 443 ASN C C   
12043 O O   . ASN C 443 ? 0.5555 0.4839 2.1069 0.1264  0.0212  -0.0024 443 ASN C O   
12044 C CB  . ASN C 443 ? 0.5967 0.4941 2.1803 0.1204  0.0060  -0.0237 443 ASN C CB  
12045 C CG  . ASN C 443 ? 0.6086 0.4979 2.2066 0.1144  -0.0064 -0.0376 443 ASN C CG  
12046 O OD1 . ASN C 443 ? 0.5860 0.4857 2.1785 0.1115  -0.0140 -0.0434 443 ASN C OD1 
12047 N ND2 . ASN C 443 ? 0.6463 0.5167 2.2639 0.1126  -0.0095 -0.0436 443 ASN C ND2 
12048 N N   . PHE C 444 ? 0.5554 0.4743 2.0871 0.1387  0.0254  -0.0143 444 PHE C N   
12049 C CA  . PHE C 444 ? 0.5126 0.4438 2.0322 0.1415  0.0336  -0.0035 444 PHE C CA  
12050 C C   . PHE C 444 ? 0.5125 0.4544 2.0120 0.1449  0.0314  -0.0083 444 PHE C C   
12051 O O   . PHE C 444 ? 0.5329 0.4738 2.0205 0.1500  0.0285  -0.0202 444 PHE C O   
12052 C CB  . PHE C 444 ? 0.4951 0.4235 2.0146 0.1469  0.0416  0.0011  444 PHE C CB  
12053 C CG  . PHE C 444 ? 0.4723 0.3941 2.0116 0.1434  0.0440  0.0109  444 PHE C CG  
12054 C CD1 . PHE C 444 ? 0.4724 0.3787 2.0279 0.1431  0.0405  0.0065  444 PHE C CD1 
12055 C CD2 . PHE C 444 ? 0.4479 0.3801 1.9903 0.1404  0.0497  0.0248  444 PHE C CD2 
12056 C CE1 . PHE C 444 ? 0.4672 0.3692 2.0419 0.1396  0.0428  0.0192  444 PHE C CE1 
12057 C CE2 . PHE C 444 ? 0.4399 0.3704 1.9983 0.1374  0.0520  0.0356  444 PHE C CE2 
12058 C CZ  . PHE C 444 ? 0.4489 0.3647 2.0238 0.1368  0.0488  0.0345  444 PHE C CZ  
12059 N N   . THR C 445 ? 0.4957 0.4482 1.9924 0.1424  0.0326  0.0010  445 THR C N   
12060 C CA  . THR C 445 ? 0.4857 0.4495 1.9666 0.1449  0.0305  0.0014  445 THR C CA  
12061 C C   . THR C 445 ? 0.4717 0.4427 1.9440 0.1482  0.0392  0.0106  445 THR C C   
12062 O O   . THR C 445 ? 0.4368 0.4082 1.9183 0.1456  0.0442  0.0191  445 THR C O   
12063 C CB  . THR C 445 ? 0.4671 0.4366 1.9559 0.1400  0.0249  0.0063  445 THR C CB  
12064 O OG1 . THR C 445 ? 0.4832 0.4466 1.9834 0.1359  0.0170  -0.0021 445 THR C OG1 
12065 C CG2 . THR C 445 ? 0.4657 0.4469 1.9405 0.1427  0.0211  0.0088  445 THR C CG2 
12066 N N   . LEU C 446 ? 0.4936 0.4723 1.9491 0.1538  0.0407  0.0085  446 LEU C N   
12067 C CA  . LEU C 446 ? 0.5243 0.5119 1.9735 0.1560  0.0484  0.0184  446 LEU C CA  
12068 C C   . LEU C 446 ? 0.5395 0.5356 1.9876 0.1534  0.0462  0.0285  446 LEU C C   
12069 O O   . LEU C 446 ? 0.5442 0.5467 1.9835 0.1545  0.0401  0.0273  446 LEU C O   
12070 C CB  . LEU C 446 ? 0.5277 0.5223 1.9621 0.1634  0.0530  0.0135  446 LEU C CB  
12071 C CG  . LEU C 446 ? 0.5426 0.5273 1.9816 0.1673  0.0553  0.0034  446 LEU C CG  
12072 C CD1 . LEU C 446 ? 0.5620 0.5548 1.9870 0.1762  0.0597  -0.0044 446 LEU C CD1 
12073 C CD2 . LEU C 446 ? 0.5293 0.5092 1.9830 0.1649  0.0607  0.0117  446 LEU C CD2 
12074 N N   . LEU C 447 ? 0.5415 0.5375 2.0002 0.1501  0.0502  0.0381  447 LEU C N   
12075 C CA  . LEU C 447 ? 0.5693 0.5697 2.0326 0.1478  0.0476  0.0473  447 LEU C CA  
12076 C C   . LEU C 447 ? 0.5522 0.5594 2.0141 0.1482  0.0536  0.0580  447 LEU C C   
12077 O O   . LEU C 447 ? 0.5259 0.5327 1.9917 0.1475  0.0598  0.0591  447 LEU C O   
12078 C CB  . LEU C 447 ? 0.5716 0.5659 2.0521 0.1434  0.0450  0.0475  447 LEU C CB  
12079 C CG  . LEU C 447 ? 0.5840 0.5744 2.0759 0.1406  0.0509  0.0479  447 LEU C CG  
12080 C CD1 . LEU C 447 ? 0.6368 0.6292 2.1370 0.1390  0.0533  0.0552  447 LEU C CD1 
12081 C CD2 . LEU C 447 ? 0.5645 0.5510 2.0681 0.1378  0.0494  0.0433  447 LEU C CD2 
12082 N N   . ASP C 448 ? 0.5821 0.5975 2.0386 0.1493  0.0511  0.0669  448 ASP C N   
12083 C CA  . ASP C 448 ? 0.6083 0.6291 2.0705 0.1477  0.0549  0.0808  448 ASP C CA  
12084 C C   . ASP C 448 ? 0.5546 0.5867 2.0044 0.1506  0.0616  0.0843  448 ASP C C   
12085 O O   . ASP C 448 ? 0.5655 0.6065 1.9979 0.1555  0.0609  0.0801  448 ASP C O   
12086 C CB  . ASP C 448 ? 0.6399 0.6517 2.1223 0.1429  0.0570  0.0831  448 ASP C CB  
12087 C CG  . ASP C 448 ? 0.6112 0.6158 2.1086 0.1411  0.0516  0.0834  448 ASP C CG  
12088 O OD1 . ASP C 448 ? 0.6022 0.6103 2.1006 0.1424  0.0466  0.0919  448 ASP C OD1 
12089 O OD2 . ASP C 448 ? 0.5597 0.5572 2.0686 0.1388  0.0526  0.0759  448 ASP C OD2 
12090 N N   . ASP C 449 ? 0.5313 0.5645 1.9913 0.1477  0.0677  0.0913  449 ASP C N   
12091 C CA  . ASP C 449 ? 0.5468 0.5941 1.9992 0.1499  0.0748  0.0976  449 ASP C CA  
12092 C C   . ASP C 449 ? 0.4833 0.5288 1.9396 0.1503  0.0802  0.0899  449 ASP C C   
12093 O O   . ASP C 449 ? 0.4428 0.4798 1.9133 0.1459  0.0800  0.0876  449 ASP C O   
12094 C CB  . ASP C 449 ? 0.5773 0.6323 2.0405 0.1458  0.0777  0.1157  449 ASP C CB  
12095 C CG  . ASP C 449 ? 0.6096 0.6760 2.0647 0.1475  0.0753  0.1297  449 ASP C CG  
12096 O OD1 . ASP C 449 ? 0.6526 0.7223 2.0912 0.1522  0.0706  0.1235  449 ASP C OD1 
12097 O OD2 . ASP C 449 ? 0.6008 0.6732 2.0675 0.1437  0.0777  0.1472  449 ASP C OD2 
12098 N N   . LEU C 450 ? 0.4752 0.5311 1.9181 0.1565  0.0848  0.0858  450 LEU C N   
12099 C CA  . LEU C 450 ? 0.4657 0.5275 1.9131 0.1580  0.0916  0.0845  450 LEU C CA  
12100 C C   . LEU C 450 ? 0.4566 0.5271 1.9184 0.1521  0.0956  0.0989  450 LEU C C   
12101 O O   . LEU C 450 ? 0.4494 0.5307 1.9099 0.1508  0.0974  0.1118  450 LEU C O   
12102 C CB  . LEU C 450 ? 0.4744 0.5491 1.9045 0.1670  0.0961  0.0792  450 LEU C CB  
12103 C CG  . LEU C 450 ? 0.4786 0.5634 1.9126 0.1713  0.1041  0.0780  450 LEU C CG  
12104 C CD1 . LEU C 450 ? 0.4711 0.5410 1.9160 0.1708  0.1018  0.0692  450 LEU C CD1 
12105 C CD2 . LEU C 450 ? 0.4989 0.5977 1.9155 0.1816  0.1090  0.0708  450 LEU C CD2 
12106 N N   . LYS C 451 ? 0.4462 0.5128 1.9226 0.1480  0.0964  0.0971  451 LYS C N   
12107 C CA  . LYS C 451 ? 0.4417 0.5155 1.9351 0.1411  0.0989  0.1078  451 LYS C CA  
12108 C C   . LYS C 451 ? 0.4366 0.5245 1.9336 0.1436  0.1050  0.1078  451 LYS C C   
12109 O O   . LYS C 451 ? 0.4358 0.5204 1.9295 0.1482  0.1050  0.0978  451 LYS C O   
12110 C CB  . LYS C 451 ? 0.4335 0.4931 1.9423 0.1337  0.0932  0.1042  451 LYS C CB  
12111 C CG  . LYS C 451 ? 0.4538 0.5014 1.9627 0.1322  0.0877  0.1054  451 LYS C CG  
12112 C CD  . LYS C 451 ? 0.4642 0.5003 1.9916 0.1253  0.0833  0.1029  451 LYS C CD  
12113 C CE  . LYS C 451 ? 0.4743 0.5000 2.0043 0.1252  0.0784  0.1053  451 LYS C CE  
12114 N NZ  . LYS C 451 ? 0.4976 0.5138 2.0489 0.1191  0.0754  0.1036  451 LYS C NZ  
12115 N N   . ILE C 452 ? 0.4342 0.5387 1.9397 0.1408  0.1103  0.1206  452 ILE C N   
12116 C CA  . ILE C 452 ? 0.4201 0.5431 1.9312 0.1435  0.1170  0.1232  452 ILE C CA  
12117 C C   . ILE C 452 ? 0.4119 0.5412 1.9470 0.1328  0.1164  0.1329  452 ILE C C   
12118 O O   . ILE C 452 ? 0.4285 0.5551 1.9727 0.1257  0.1148  0.1433  452 ILE C O   
12119 C CB  . ILE C 452 ? 0.4268 0.5697 1.9247 0.1514  0.1253  0.1293  452 ILE C CB  
12120 C CG1 . ILE C 452 ? 0.4336 0.5735 1.9106 0.1634  0.1266  0.1148  452 ILE C CG1 
12121 C CG2 . ILE C 452 ? 0.4294 0.5957 1.9409 0.1511  0.1330  0.1380  452 ILE C CG2 
12122 C CD1 . ILE C 452 ? 0.4299 0.5516 1.8923 0.1646  0.1195  0.1063  452 ILE C CD1 
12123 N N   . SER C 453 ? 0.3944 0.5320 1.9411 0.1317  0.1170  0.1297  453 SER C N   
12124 C CA  . SER C 453 ? 0.3748 0.5196 1.9456 0.1211  0.1148  0.1356  453 SER C CA  
12125 C C   . SER C 453 ? 0.3644 0.5326 1.9452 0.1233  0.1198  0.1389  453 SER C C   
12126 O O   . SER C 453 ? 0.3511 0.5218 1.9261 0.1307  0.1200  0.1306  453 SER C O   
12127 C CB  . SER C 453 ? 0.3636 0.4919 1.9415 0.1148  0.1059  0.1246  453 SER C CB  
12128 O OG  . SER C 453 ? 0.3558 0.4952 1.9528 0.1078  0.1032  0.1239  453 SER C OG  
12129 N N   . TYR C 454 ? 0.3632 0.5484 1.9631 0.1159  0.1230  0.1522  454 TYR C N   
12130 C CA  . TYR C 454 ? 0.3513 0.5609 1.9680 0.1149  0.1264  0.1573  454 TYR C CA  
12131 C C   . TYR C 454 ? 0.3509 0.5617 1.9950 0.1002  0.1191  0.1593  454 TYR C C   
12132 O O   . TYR C 454 ? 0.3652 0.5844 2.0284 0.0909  0.1209  0.1726  454 TYR C O   
12133 C CB  . TYR C 454 ? 0.3590 0.5907 1.9737 0.1196  0.1377  0.1716  454 TYR C CB  
12134 C CG  . TYR C 454 ? 0.3564 0.6177 1.9817 0.1250  0.1449  0.1759  454 TYR C CG  
12135 C CD1 . TYR C 454 ? 0.3530 0.6179 1.9648 0.1391  0.1482  0.1654  454 TYR C CD1 
12136 C CD2 . TYR C 454 ? 0.3538 0.6391 2.0051 0.1162  0.1483  0.1905  454 TYR C CD2 
12137 C CE1 . TYR C 454 ? 0.3498 0.6416 1.9732 0.1457  0.1548  0.1689  454 TYR C CE1 
12138 C CE2 . TYR C 454 ? 0.3609 0.6755 2.0233 0.1220  0.1552  0.1946  454 TYR C CE2 
12139 C CZ  . TYR C 454 ? 0.3546 0.6727 2.0028 0.1373  0.1586  0.1836  454 TYR C CZ  
12140 O OH  . TYR C 454 ? 0.3470 0.6944 2.0084 0.1445  0.1655  0.1874  454 TYR C OH  
12141 N N   . ASN C 455 ? 0.3429 0.5462 1.9897 0.0977  0.1107  0.1462  455 ASN C N   
12142 C CA  . ASN C 455 ? 0.3475 0.5491 2.0173 0.0840  0.1020  0.1429  455 ASN C CA  
12143 C C   . ASN C 455 ? 0.3410 0.5709 2.0330 0.0794  0.1023  0.1490  455 ASN C C   
12144 O O   . ASN C 455 ? 0.3324 0.5741 2.0217 0.0845  0.1002  0.1427  455 ASN C O   
12145 C CB  . ASN C 455 ? 0.3545 0.5397 2.0154 0.0835  0.0929  0.1255  455 ASN C CB  
12146 C CG  . ASN C 455 ? 0.3731 0.5529 2.0549 0.0700  0.0835  0.1180  455 ASN C CG  
12147 O OD1 . ASN C 455 ? 0.3802 0.5465 2.0549 0.0691  0.0767  0.1033  455 ASN C OD1 
12148 N ND2 . ASN C 455 ? 0.3857 0.5757 2.0942 0.0593  0.0830  0.1272  455 ASN C ND2 
12149 N N   . THR C 456 ? 0.3428 0.5840 2.0587 0.0695  0.1047  0.1626  456 THR C N   
12150 C CA  . THR C 456 ? 0.3389 0.6107 2.0790 0.0650  0.1070  0.1723  456 THR C CA  
12151 C C   . THR C 456 ? 0.3320 0.6086 2.0948 0.0528  0.0949  0.1625  456 THR C C   
12152 O O   . THR C 456 ? 0.3356 0.6383 2.1210 0.0475  0.0943  0.1687  456 THR C O   
12153 C CB  . THR C 456 ? 0.3521 0.6352 2.1086 0.0591  0.1153  0.1928  456 THR C CB  
12154 O OG1 . THR C 456 ? 0.3554 0.6126 2.1142 0.0515  0.1115  0.1944  456 THR C OG1 
12155 C CG2 . THR C 456 ? 0.3581 0.6561 2.0944 0.0736  0.1289  0.2025  456 THR C CG2 
12156 N N   . HIS C 457 ? 0.3337 0.5871 2.0909 0.0483  0.0851  0.1466  457 HIS C N   
12157 C CA  . HIS C 457 ? 0.3307 0.5895 2.0987 0.0408  0.0730  0.1316  457 HIS C CA  
12158 C C   . HIS C 457 ? 0.3369 0.6045 2.1422 0.0235  0.0663  0.1339  457 HIS C C   
12159 O O   . HIS C 457 ? 0.3373 0.6132 2.1537 0.0161  0.0553  0.1205  457 HIS C O   
12160 C CB  . HIS C 457 ? 0.3233 0.6056 2.0824 0.0499  0.0726  0.1293  457 HIS C CB  
12161 C CG  . HIS C 457 ? 0.3199 0.5884 2.0472 0.0625  0.0727  0.1195  457 HIS C CG  
12162 N ND1 . HIS C 457 ? 0.3151 0.5727 2.0196 0.0757  0.0822  0.1244  457 HIS C ND1 
12163 C CD2 . HIS C 457 ? 0.3171 0.5820 2.0332 0.0631  0.0641  0.1051  457 HIS C CD2 
12164 C CE1 . HIS C 457 ? 0.3111 0.5580 1.9943 0.0833  0.0791  0.1144  457 HIS C CE1 
12165 N NE2 . HIS C 457 ? 0.3125 0.5645 2.0016 0.0760  0.0688  0.1037  457 HIS C NE2 
12166 N N   . LEU C 458 ? 0.3425 0.6083 2.1661 0.0171  0.0725  0.1509  458 LEU C N   
12167 C CA  . LEU C 458 ? 0.3468 0.6154 2.2099 -0.0006 0.0669  0.1563  458 LEU C CA  
12168 C C   . LEU C 458 ? 0.3491 0.5886 2.2185 -0.0090 0.0552  0.1371  458 LEU C C   
12169 O O   . LEU C 458 ? 0.3532 0.5666 2.2213 -0.0095 0.0571  0.1401  458 LEU C O   
12170 C CB  . LEU C 458 ? 0.3554 0.6246 2.2334 -0.0042 0.0770  0.1811  458 LEU C CB  
12171 C CG  . LEU C 458 ? 0.3539 0.6508 2.2222 0.0063  0.0914  0.2007  458 LEU C CG  
12172 C CD1 . LEU C 458 ? 0.3654 0.6629 2.2483 0.0010  0.1004  0.2252  458 LEU C CD1 
12173 C CD2 . LEU C 458 ? 0.3499 0.6832 2.2353 0.0048  0.0912  0.2031  458 LEU C CD2 
12174 N N   . GLY C 459 ? 0.3480 0.5940 2.2231 -0.0145 0.0434  0.1170  459 GLY C N   
12175 C CA  . GLY C 459 ? 0.3605 0.5831 2.2429 -0.0223 0.0318  0.0949  459 GLY C CA  
12176 C C   . GLY C 459 ? 0.3559 0.5530 2.2045 -0.0103 0.0337  0.0830  459 GLY C C   
12177 O O   . GLY C 459 ? 0.3439 0.5487 2.1625 0.0009  0.0349  0.0756  459 GLY C O   
12178 N N   . TRP C 460 ? 0.3693 0.5368 2.2258 -0.0131 0.0338  0.0824  460 TRP C N   
12179 C CA  . TRP C 460 ? 0.3669 0.5101 2.1963 -0.0027 0.0356  0.0723  460 TRP C CA  
12180 C C   . TRP C 460 ? 0.3695 0.5019 2.1850 0.0061  0.0470  0.0932  460 TRP C C   
12181 O O   . TRP C 460 ? 0.3587 0.4768 2.1476 0.0168  0.0500  0.0883  460 TRP C O   
12182 C CB  . TRP C 460 ? 0.3785 0.4971 2.2262 -0.0103 0.0262  0.0525  460 TRP C CB  
12183 C CG  . TRP C 460 ? 0.3835 0.5124 2.2359 -0.0162 0.0146  0.0260  460 TRP C CG  
12184 C CD1 . TRP C 460 ? 0.4003 0.5325 2.2873 -0.0310 0.0042  0.0155  460 TRP C CD1 
12185 C CD2 . TRP C 460 ? 0.3792 0.5189 2.2012 -0.0079 0.0116  0.0069  460 TRP C CD2 
12186 N NE1 . TRP C 460 ? 0.4051 0.5496 2.2834 -0.0321 -0.0055 -0.0109 460 TRP C NE1 
12187 C CE2 . TRP C 460 ? 0.3928 0.5434 2.2308 -0.0179 -0.0008 -0.0154 460 TRP C CE2 
12188 C CE3 . TRP C 460 ? 0.3674 0.5096 2.1516 0.0064  0.0178  0.0071  460 TRP C CE3 
12189 C CZ2 . TRP C 460 ? 0.3961 0.5628 2.2109 -0.0134 -0.0066 -0.0361 460 TRP C CZ2 
12190 C CZ3 . TRP C 460 ? 0.3692 0.5256 2.1332 0.0103  0.0126  -0.0114 460 TRP C CZ3 
12191 C CH2 . TRP C 460 ? 0.3838 0.5539 2.1615 0.0010  0.0008  -0.0321 460 TRP C CH2 
12192 N N   . ALA C 461 ? 0.3834 0.5259 2.2168 0.0014  0.0532  0.1168  461 ALA C N   
12193 C CA  . ALA C 461 ? 0.3959 0.5367 2.2133 0.0102  0.0643  0.1377  461 ALA C CA  
12194 C C   . ALA C 461 ? 0.3989 0.5468 2.1764 0.0260  0.0704  0.1336  461 ALA C C   
12195 O O   . ALA C 461 ? 0.4237 0.5933 2.1934 0.0296  0.0714  0.1307  461 ALA C O   
12196 C CB  . ALA C 461 ? 0.3978 0.5602 2.2368 0.0038  0.0710  0.1624  461 ALA C CB  
12197 N N   . ILE C 462 ? 0.3945 0.5254 2.1496 0.0353  0.0743  0.1352  462 ILE C N   
12198 C CA  . ILE C 462 ? 0.4001 0.5350 2.1207 0.0492  0.0792  0.1308  462 ILE C CA  
12199 C C   . ILE C 462 ? 0.4006 0.5525 2.1095 0.0568  0.0901  0.1492  462 ILE C C   
12200 O O   . ILE C 462 ? 0.4014 0.5569 2.0841 0.0687  0.0946  0.1457  462 ILE C O   
12201 C CB  . ILE C 462 ? 0.4104 0.5204 2.1125 0.0555  0.0768  0.1199  462 ILE C CB  
12202 C CG1 . ILE C 462 ? 0.4308 0.5262 2.1373 0.0552  0.0795  0.1339  462 ILE C CG1 
12203 C CG2 . ILE C 462 ? 0.4104 0.5089 2.1201 0.0504  0.0674  0.0986  462 ILE C CG2 
12204 C CD1 . ILE C 462 ? 0.4338 0.5332 2.1134 0.0666  0.0874  0.1443  462 ILE C CD1 
12205 N N   . GLY C 463 ? 0.4052 0.5682 2.1342 0.0502  0.0947  0.1684  463 GLY C N   
12206 C CA  . GLY C 463 ? 0.4025 0.5866 2.1213 0.0573  0.1060  0.1857  463 GLY C CA  
12207 C C   . GLY C 463 ? 0.4080 0.5803 2.1048 0.0653  0.1104  0.1929  463 GLY C C   
12208 O O   . GLY C 463 ? 0.4101 0.5581 2.1045 0.0640  0.1045  0.1868  463 GLY C O   
12209 N N   . SER C 464 ? 0.4233 0.6145 2.1042 0.0739  0.1205  0.2049  464 SER C N   
12210 C CA  . SER C 464 ? 0.4418 0.6257 2.0982 0.0824  0.1239  0.2097  464 SER C CA  
12211 C C   . SER C 464 ? 0.4600 0.6243 2.0902 0.0917  0.1193  0.1891  464 SER C C   
12212 O O   . SER C 464 ? 0.4371 0.5998 2.0631 0.0947  0.1166  0.1736  464 SER C O   
12213 C CB  . SER C 464 ? 0.4478 0.6590 2.0905 0.0904  0.1356  0.2235  464 SER C CB  
12214 O OG  . SER C 464 ? 0.4572 0.6872 2.1246 0.0811  0.1405  0.2465  464 SER C OG  
12215 N N   . GLN C 465 ? 0.5149 0.6654 2.1308 0.0953  0.1178  0.1915  465 GLN C N   
12216 C CA  . GLN C 465 ? 0.5293 0.6635 2.1202 0.1041  0.1143  0.1765  465 GLN C CA  
12217 C C   . GLN C 465 ? 0.5434 0.6848 2.1129 0.1118  0.1187  0.1860  465 GLN C C   
12218 O O   . GLN C 465 ? 0.5751 0.7330 2.1499 0.1096  0.1241  0.2051  465 GLN C O   
12219 C CB  . GLN C 465 ? 0.5460 0.6541 2.1468 0.0985  0.1049  0.1678  465 GLN C CB  
12220 C CG  . GLN C 465 ? 0.5692 0.6689 2.1751 0.0964  0.0997  0.1493  465 GLN C CG  
12221 C CD  . GLN C 465 ? 0.5995 0.6760 2.2120 0.0929  0.0917  0.1386  465 GLN C CD  
12222 O OE1 . GLN C 465 ? 0.6760 0.7446 2.3124 0.0840  0.0874  0.1401  465 GLN C OE1 
12223 N NE2 . GLN C 465 ? 0.5684 0.6345 2.1620 0.1000  0.0896  0.1269  465 GLN C NE2 
12224 N N   . ALA C 466 ? 0.5394 0.6705 2.0852 0.1203  0.1162  0.1734  466 ALA C N   
12225 C CA  . ALA C 466 ? 0.5493 0.6873 2.0751 0.1266  0.1181  0.1809  466 ALA C CA  
12226 C C   . ALA C 466 ? 0.5482 0.6689 2.0553 0.1328  0.1117  0.1647  466 ALA C C   
12227 O O   . ALA C 466 ? 0.5453 0.6582 2.0458 0.1368  0.1105  0.1478  466 ALA C O   
12228 C CB  . ALA C 466 ? 0.5545 0.7202 2.0661 0.1341  0.1281  0.1859  466 ALA C CB  
12229 N N   . SER C 467 ? 0.5626 0.6786 2.0630 0.1333  0.1074  0.1717  467 SER C N   
12230 C CA  . SER C 467 ? 0.5614 0.6644 2.0454 0.1386  0.1010  0.1583  467 SER C CA  
12231 C C   . SER C 467 ? 0.5559 0.6758 2.0129 0.1476  0.1037  0.1577  467 SER C C   
12232 O O   . SER C 467 ? 0.5587 0.6949 2.0101 0.1481  0.1059  0.1742  467 SER C O   
12233 C CB  . SER C 467 ? 0.5938 0.6813 2.0894 0.1341  0.0932  0.1643  467 SER C CB  
12234 O OG  . SER C 467 ? 0.6276 0.6957 2.1414 0.1288  0.0890  0.1542  467 SER C OG  
12235 N N   . VAL C 468 ? 0.5503 0.6668 1.9911 0.1547  0.1031  0.1387  468 VAL C N   
12236 C CA  . VAL C 468 ? 0.5685 0.7005 1.9836 0.1637  0.1050  0.1333  468 VAL C CA  
12237 C C   . VAL C 468 ? 0.5595 0.6780 1.9631 0.1660  0.0952  0.1208  468 VAL C C   
12238 O O   . VAL C 468 ? 0.5327 0.6309 1.9435 0.1643  0.0901  0.1077  468 VAL C O   
12239 C CB  . VAL C 468 ? 0.5961 0.7365 2.0046 0.1708  0.1126  0.1207  468 VAL C CB  
12240 C CG1 . VAL C 468 ? 0.6182 0.7723 2.0004 0.1815  0.1142  0.1086  468 VAL C CG1 
12241 C CG2 . VAL C 468 ? 0.5970 0.7549 2.0190 0.1684  0.1221  0.1347  468 VAL C CG2 
12242 N N   . SER C 469 ? 0.5817 0.7143 1.9678 0.1694  0.0925  0.1264  469 SER C N   
12243 C CA  . SER C 469 ? 0.6007 0.7255 1.9756 0.1715  0.0824  0.1154  469 SER C CA  
12244 C C   . SER C 469 ? 0.6250 0.7517 1.9815 0.1794  0.0827  0.0926  469 SER C C   
12245 O O   . SER C 469 ? 0.6512 0.7969 1.9937 0.1860  0.0904  0.0904  469 SER C O   
12246 C CB  . SER C 469 ? 0.6209 0.7624 1.9849 0.1721  0.0782  0.1308  469 SER C CB  
12247 O OG  . SER C 469 ? 0.6391 0.7731 1.9955 0.1733  0.0669  0.1199  469 SER C OG  
12248 N N   . ILE C 470 ? 0.6304 0.7379 1.9893 0.1789  0.0747  0.0756  470 ILE C N   
12249 C CA  . ILE C 470 ? 0.6526 0.7585 1.9978 0.1858  0.0735  0.0531  470 ILE C CA  
12250 C C   . ILE C 470 ? 0.6954 0.8035 2.0269 0.1869  0.0623  0.0438  470 ILE C C   
12251 O O   . ILE C 470 ? 0.7334 0.8387 2.0547 0.1918  0.0589  0.0230  470 ILE C O   
12252 C CB  . ILE C 470 ? 0.6443 0.7272 2.0057 0.1846  0.0739  0.0402  470 ILE C CB  
12253 C CG1 . ILE C 470 ? 0.6453 0.7083 2.0243 0.1765  0.0663  0.0424  470 ILE C CG1 
12254 C CG2 . ILE C 470 ? 0.6259 0.7122 1.9972 0.1856  0.0846  0.0466  470 ILE C CG2 
12255 C CD1 . ILE C 470 ? 0.6533 0.6969 2.0466 0.1753  0.0664  0.0314  470 ILE C CD1 
12256 N N   . SER C 471 ? 0.6889 0.8028 2.0217 0.1827  0.0563  0.0593  471 SER C N   
12257 C CA  . SER C 471 ? 0.6852 0.8047 2.0066 0.1832  0.0444  0.0537  471 SER C CA  
12258 C C   . SER C 471 ? 0.7048 0.8421 1.9990 0.1914  0.0434  0.0363  471 SER C C   
12259 O O   . SER C 471 ? 0.7271 0.8581 2.0163 0.1922  0.0340  0.0166  471 SER C O   
12260 C CB  . SER C 471 ? 0.6981 0.8289 2.0221 0.1800  0.0402  0.0769  471 SER C CB  
12261 O OG  . SER C 471 ? 0.6977 0.8439 2.0209 0.1804  0.0496  0.0984  471 SER C OG  
12262 N N   . ASP C 472 ? 0.7182 0.8779 1.9963 0.1975  0.0534  0.0416  472 ASP C N   
12263 C CA  . ASP C 472 ? 0.7351 0.9147 1.9858 0.2068  0.0540  0.0233  472 ASP C CA  
12264 C C   . ASP C 472 ? 0.7263 0.8904 1.9803 0.2120  0.0580  -0.0025 472 ASP C C   
12265 O O   . ASP C 472 ? 0.7418 0.9225 1.9755 0.2212  0.0613  -0.0187 472 ASP C O   
12266 C CB  . ASP C 472 ? 0.7521 0.9658 1.9841 0.2124  0.0645  0.0392  472 ASP C CB  
12267 C CG  . ASP C 472 ? 0.7511 0.9649 1.9970 0.2123  0.0792  0.0519  472 ASP C CG  
12268 O OD1 . ASP C 472 ? 0.7358 0.9232 2.0072 0.2063  0.0799  0.0533  472 ASP C OD1 
12269 O OD2 . ASP C 472 ? 0.7694 1.0121 2.0009 0.2182  0.0897  0.0601  472 ASP C OD2 
12270 N N   . GLN C 473 ? 0.7131 0.8474 1.9921 0.2070  0.0576  -0.0068 473 GLN C N   
12271 C CA  . GLN C 473 ? 0.7297 0.8478 2.0149 0.2121  0.0602  -0.0294 473 GLN C CA  
12272 C C   . GLN C 473 ? 0.7305 0.8177 2.0362 0.2057  0.0506  -0.0406 473 GLN C C   
12273 O O   . GLN C 473 ? 0.7216 0.7914 2.0393 0.2084  0.0529  -0.0542 473 GLN C O   
12274 C CB  . GLN C 473 ? 0.7059 0.8232 2.0027 0.2149  0.0738  -0.0212 473 GLN C CB  
12275 C CG  . GLN C 473 ? 0.7170 0.8645 1.9958 0.2240  0.0854  -0.0178 473 GLN C CG  
12276 C CD  . GLN C 473 ? 0.7053 0.8530 1.9996 0.2258  0.0979  -0.0086 473 GLN C CD  
12277 O OE1 . GLN C 473 ? 0.7315 0.8683 2.0345 0.2319  0.1017  -0.0234 473 GLN C OE1 
12278 N NE2 . GLN C 473 ? 0.6874 0.8481 1.9877 0.2204  0.1039  0.0166  473 GLN C NE2 
12279 N N   . LEU C 474 ? 0.7322 0.8137 2.0439 0.1977  0.0401  -0.0345 474 LEU C N   
12280 C CA  . LEU C 474 ? 0.7444 0.7999 2.0785 0.1907  0.0327  -0.0410 474 LEU C CA  
12281 C C   . LEU C 474 ? 0.7651 0.8088 2.0991 0.1940  0.0263  -0.0681 474 LEU C C   
12282 O O   . LEU C 474 ? 0.7604 0.7810 2.1155 0.1905  0.0247  -0.0742 474 LEU C O   
12283 C CB  . LEU C 474 ? 0.7722 0.8275 2.1135 0.1826  0.0228  -0.0301 474 LEU C CB  
12284 C CG  . LEU C 474 ? 0.7648 0.8146 2.1235 0.1763  0.0272  -0.0077 474 LEU C CG  
12285 C CD1 . LEU C 474 ? 0.7599 0.7903 2.1384 0.1739  0.0339  -0.0075 474 LEU C CD1 
12286 C CD2 . LEU C 474 ? 0.7672 0.8361 2.1151 0.1787  0.0344  0.0109  474 LEU C CD2 
12287 N N   . ASP C 475 ? 0.7880 0.8481 2.0991 0.2007  0.0225  -0.0842 475 ASP C N   
12288 C CA  . ASP C 475 ? 0.8284 0.8775 2.1394 0.2042  0.0154  -0.1133 475 ASP C CA  
12289 C C   . ASP C 475 ? 0.8485 0.8801 2.1725 0.2104  0.0244  -0.1235 475 ASP C C   
12290 O O   . ASP C 475 ? 0.8592 0.8690 2.1989 0.2098  0.0185  -0.1418 475 ASP C O   
12291 C CB  . ASP C 475 ? 0.8789 0.9530 2.1593 0.2131  0.0131  -0.1306 475 ASP C CB  
12292 C CG  . ASP C 475 ? 0.9064 1.0057 2.1666 0.2105  0.0038  -0.1236 475 ASP C CG  
12293 O OD1 . ASP C 475 ? 0.9343 1.0268 2.2083 0.2009  -0.0049 -0.1112 475 ASP C OD1 
12294 O OD2 . ASP C 475 ? 0.9157 1.0431 2.1469 0.2187  0.0056  -0.1302 475 ASP C OD2 
12295 N N   . LYS C 476 ? 0.8218 0.8646 2.1406 0.2165  0.0382  -0.1115 476 LYS C N   
12296 C CA  . LYS C 476 ? 0.8012 0.8373 2.1256 0.2263  0.0472  -0.1234 476 LYS C CA  
12297 C C   . LYS C 476 ? 0.7545 0.7620 2.1101 0.2216  0.0484  -0.1176 476 LYS C C   
12298 O O   . LYS C 476 ? 0.6992 0.6997 2.0680 0.2120  0.0474  -0.0982 476 LYS C O   
12299 C CB  . LYS C 476 ? 0.8113 0.8735 2.1210 0.2339  0.0614  -0.1107 476 LYS C CB  
12300 C CG  . LYS C 476 ? 0.8413 0.9362 2.1188 0.2408  0.0626  -0.1165 476 LYS C CG  
12301 C CD  . LYS C 476 ? 0.8457 0.9690 2.1118 0.2460  0.0770  -0.0979 476 LYS C CD  
12302 C CE  . LYS C 476 ? 0.8724 0.9994 2.1426 0.2578  0.0893  -0.1079 476 LYS C CE  
12303 N NZ  . LYS C 476 ? 0.8680 1.0254 2.1295 0.2615  0.1031  -0.0881 476 LYS C NZ  
12304 N N   . LYS C 477 ? 0.7655 0.7583 2.1327 0.2295  0.0508  -0.1346 477 LYS C N   
12305 C CA  . LYS C 477 ? 0.7420 0.7097 2.1386 0.2271  0.0524  -0.1286 477 LYS C CA  
12306 C C   . LYS C 477 ? 0.7128 0.6908 2.1136 0.2300  0.0651  -0.1079 477 LYS C C   
12307 O O   . LYS C 477 ? 0.6921 0.6597 2.1113 0.2233  0.0663  -0.0908 477 LYS C O   
12308 C CB  . LYS C 477 ? 0.7786 0.7272 2.1877 0.2353  0.0495  -0.1542 477 LYS C CB  
12309 C CG  . LYS C 477 ? 0.7960 0.7170 2.2385 0.2335  0.0498  -0.1482 477 LYS C CG  
12310 C CD  . LYS C 477 ? 0.8112 0.7112 2.2745 0.2199  0.0392  -0.1420 477 LYS C CD  
12311 C CE  . LYS C 477 ? 0.8060 0.6840 2.3008 0.2179  0.0409  -0.1303 477 LYS C CE  
12312 N NZ  . LYS C 477 ? 0.7660 0.6545 2.2625 0.2135  0.0485  -0.1026 477 LYS C NZ  
12313 N N   . ILE C 478 ? 0.7017 0.7027 2.0852 0.2399  0.0746  -0.1100 478 ILE C N   
12314 C CA  . ILE C 478 ? 0.6756 0.6914 2.0624 0.2420  0.0862  -0.0906 478 ILE C CA  
12315 C C   . ILE C 478 ? 0.6647 0.7078 2.0304 0.2387  0.0898  -0.0759 478 ILE C C   
12316 O O   . ILE C 478 ? 0.7129 0.7764 2.0565 0.2453  0.0920  -0.0851 478 ILE C O   
12317 C CB  . ILE C 478 ? 0.6948 0.7166 2.0845 0.2568  0.0956  -0.1024 478 ILE C CB  
12318 C CG1 . ILE C 478 ? 0.7088 0.7019 2.1205 0.2621  0.0911  -0.1198 478 ILE C CG1 
12319 C CG2 . ILE C 478 ? 0.6775 0.7155 2.0745 0.2579  0.1067  -0.0811 478 ILE C CG2 
12320 C CD1 . ILE C 478 ? 0.6863 0.6590 2.1261 0.2555  0.0896  -0.1034 478 ILE C CD1 
12321 N N   . ILE C 479 ? 0.6015 0.6461 1.9750 0.2287  0.0906  -0.0529 479 ILE C N   
12322 C CA  . ILE C 479 ? 0.5757 0.6437 1.9353 0.2250  0.0944  -0.0359 479 ILE C CA  
12323 C C   . ILE C 479 ? 0.5429 0.6265 1.9099 0.2278  0.1063  -0.0215 479 ILE C C   
12324 O O   . ILE C 479 ? 0.5189 0.5910 1.9055 0.2241  0.1075  -0.0134 479 ILE C O   
12325 C CB  . ILE C 479 ? 0.5519 0.6109 1.9172 0.2121  0.0864  -0.0219 479 ILE C CB  
12326 C CG1 . ILE C 479 ? 0.5640 0.6103 1.9247 0.2092  0.0744  -0.0356 479 ILE C CG1 
12327 C CG2 . ILE C 479 ? 0.5431 0.6237 1.8991 0.2083  0.0901  -0.0024 479 ILE C CG2 
12328 C CD1 . ILE C 479 ? 0.5497 0.5861 1.9199 0.1978  0.0666  -0.0240 479 ILE C CD1 
12329 N N   . THR C 480 ? 0.5407 0.6525 1.8923 0.2336  0.1147  -0.0170 480 THR C N   
12330 C CA  . THR C 480 ? 0.5297 0.6600 1.8896 0.2374  0.1266  -0.0052 480 THR C CA  
12331 C C   . THR C 480 ? 0.5274 0.6815 1.8814 0.2309  0.1312  0.0175  480 THR C C   
12332 O O   . THR C 480 ? 0.5446 0.7108 1.8798 0.2301  0.1288  0.0198  480 THR C O   
12333 C CB  . THR C 480 ? 0.5414 0.6861 1.8941 0.2527  0.1353  -0.0217 480 THR C CB  
12334 O OG1 . THR C 480 ? 0.5558 0.7313 1.8854 0.2571  0.1411  -0.0192 480 THR C OG1 
12335 C CG2 . THR C 480 ? 0.5547 0.6776 1.9067 0.2602  0.1288  -0.0485 480 THR C CG2 
12336 N N   . SER C 481 ? 0.5082 0.6690 1.8801 0.2261  0.1372  0.0347  481 SER C N   
12337 C CA  . SER C 481 ? 0.5088 0.6925 1.8814 0.2200  0.1429  0.0572  481 SER C CA  
12338 C C   . SER C 481 ? 0.5099 0.7150 1.8952 0.2242  0.1547  0.0652  481 SER C C   
12339 O O   . SER C 481 ? 0.5070 0.7046 1.9046 0.2297  0.1565  0.0558  481 SER C O   
12340 C CB  . SER C 481 ? 0.4853 0.6536 1.8714 0.2059  0.1354  0.0723  481 SER C CB  
12341 O OG  . SER C 481 ? 0.4769 0.6648 1.8657 0.1997  0.1398  0.0943  481 SER C OG  
12342 N N   . GLU C 482 ? 0.5188 0.7519 1.9029 0.2217  0.1625  0.0839  482 GLU C N   
12343 C CA  . GLU C 482 ? 0.5195 0.7762 1.9199 0.2229  0.1734  0.0958  482 GLU C CA  
12344 C C   . GLU C 482 ? 0.5078 0.7774 1.9198 0.2099  0.1748  0.1226  482 GLU C C   
12345 O O   . GLU C 482 ? 0.5180 0.8012 1.9159 0.2082  0.1759  0.1334  482 GLU C O   
12346 C CB  . GLU C 482 ? 0.5501 0.8346 1.9361 0.2385  0.1850  0.0854  482 GLU C CB  
12347 C CG  . GLU C 482 ? 0.5545 0.8697 1.9573 0.2416  0.1980  0.0978  482 GLU C CG  
12348 C CD  . GLU C 482 ? 0.5841 0.9317 1.9730 0.2581  0.2113  0.0881  482 GLU C CD  
12349 O OE1 . GLU C 482 ? 0.6033 0.9651 1.9653 0.2634  0.2134  0.0836  482 GLU C OE1 
12350 O OE2 . GLU C 482 ? 0.5995 0.9609 2.0039 0.2665  0.2198  0.0849  482 GLU C OE2 
12351 N N   . ASN C 483 ? 0.4866 0.7518 1.9254 0.2005  0.1739  0.1334  483 ASN C N   
12352 C CA  . ASN C 483 ? 0.4800 0.7474 1.9353 0.1861  0.1719  0.1557  483 ASN C CA  
12353 C C   . ASN C 483 ? 0.4652 0.7540 1.9464 0.1812  0.1792  0.1698  483 ASN C C   
12354 O O   . ASN C 483 ? 0.4543 0.7351 1.9522 0.1800  0.1767  0.1633  483 ASN C O   
12355 C CB  . ASN C 483 ? 0.4729 0.7067 1.9385 0.1759  0.1592  0.1521  483 ASN C CB  
12356 C CG  . ASN C 483 ? 0.4920 0.7046 1.9365 0.1798  0.1512  0.1379  483 ASN C CG  
12357 O OD1 . ASN C 483 ? 0.5186 0.7157 1.9568 0.1863  0.1478  0.1191  483 ASN C OD1 
12358 N ND2 . ASN C 483 ? 0.5009 0.7142 1.9359 0.1761  0.1481  0.1479  483 ASN C ND2 
12359 N N   . PHE C 484 ? 0.4645 0.7809 1.9510 0.1772  0.1873  0.1911  484 PHE C N   
12360 C CA  . PHE C 484 ? 0.4529 0.7965 1.9638 0.1736  0.1960  0.2055  484 PHE C CA  
12361 C C   . PHE C 484 ? 0.4312 0.7654 1.9732 0.1558  0.1895  0.2215  484 PHE C C   
12362 O O   . PHE C 484 ? 0.4292 0.7486 1.9733 0.1464  0.1832  0.2316  484 PHE C O   
12363 C CB  . PHE C 484 ? 0.4732 0.8562 1.9731 0.1797  0.2097  0.2203  484 PHE C CB  
12364 C CG  . PHE C 484 ? 0.4901 0.8860 1.9614 0.1985  0.2170  0.2009  484 PHE C CG  
12365 C CD1 . PHE C 484 ? 0.4916 0.9084 1.9699 0.2095  0.2267  0.1924  484 PHE C CD1 
12366 C CD2 . PHE C 484 ? 0.5010 0.8877 1.9407 0.2054  0.2133  0.1896  484 PHE C CD2 
12367 C CE1 . PHE C 484 ? 0.5057 0.9318 1.9603 0.2276  0.2330  0.1718  484 PHE C CE1 
12368 C CE2 . PHE C 484 ? 0.5206 0.9179 1.9357 0.2223  0.2190  0.1687  484 PHE C CE2 
12369 C CZ  . PHE C 484 ? 0.5231 0.9389 1.9459 0.2337  0.2290  0.1590  484 PHE C CZ  
12370 N N   . PHE C 485 ? 0.4157 0.7595 1.9838 0.1513  0.1907  0.2236  485 PHE C N   
12371 C CA  . PHE C 485 ? 0.4030 0.7407 2.0030 0.1342  0.1843  0.2363  485 PHE C CA  
12372 C C   . PHE C 485 ? 0.3962 0.7685 2.0229 0.1308  0.1930  0.2501  485 PHE C C   
12373 O O   . PHE C 485 ? 0.3938 0.7837 2.0192 0.1414  0.1991  0.2417  485 PHE C O   
12374 C CB  . PHE C 485 ? 0.3883 0.6934 1.9932 0.1300  0.1711  0.2182  485 PHE C CB  
12375 C CG  . PHE C 485 ? 0.3900 0.6650 1.9685 0.1359  0.1641  0.2026  485 PHE C CG  
12376 C CD1 . PHE C 485 ? 0.3966 0.6513 1.9731 0.1282  0.1573  0.2078  485 PHE C CD1 
12377 C CD2 . PHE C 485 ? 0.3930 0.6601 1.9513 0.1490  0.1640  0.1833  485 PHE C CD2 
12378 C CE1 . PHE C 485 ? 0.3937 0.6236 1.9481 0.1334  0.1508  0.1940  485 PHE C CE1 
12379 C CE2 . PHE C 485 ? 0.3898 0.6305 1.9271 0.1530  0.1572  0.1698  485 PHE C CE2 
12380 C CZ  . PHE C 485 ? 0.3892 0.6128 1.9243 0.1451  0.1508  0.1752  485 PHE C CZ  
12381 N N   . ASN C 486 ? 0.3949 0.7768 2.0481 0.1160  0.1932  0.2718  486 ASN C N   
12382 C CA  . ASN C 486 ? 0.3911 0.8043 2.0766 0.1088  0.1994  0.2868  486 ASN C CA  
12383 C C   . ASN C 486 ? 0.3784 0.7793 2.0871 0.1014  0.1885  0.2740  486 ASN C C   
12384 O O   . ASN C 486 ? 0.3684 0.7374 2.0807 0.0930  0.1757  0.2646  486 ASN C O   
12385 C CB  . ASN C 486 ? 0.3981 0.8235 2.1072 0.0942  0.2022  0.3153  486 ASN C CB  
12386 C CG  . ASN C 486 ? 0.4146 0.8661 2.1032 0.1022  0.2156  0.3326  486 ASN C CG  
12387 O OD1 . ASN C 486 ? 0.4196 0.8921 2.0831 0.1185  0.2258  0.3245  486 ASN C OD1 
12388 N ND2 . ASN C 486 ? 0.4259 0.8786 2.1260 0.0912  0.2160  0.3571  486 ASN C ND2 
12389 N N   . ILE C 487 ? 0.3827 0.8109 2.1062 0.1055  0.1935  0.2731  487 ILE C N   
12390 C CA  . ILE C 487 ? 0.3742 0.7964 2.1182 0.0995  0.1829  0.2618  487 ILE C CA  
12391 C C   . ILE C 487 ? 0.3864 0.8244 2.1721 0.0807  0.1798  0.2781  487 ILE C C   
12392 O O   . ILE C 487 ? 0.3880 0.8619 2.1932 0.0791  0.1901  0.2958  487 ILE C O   
12393 C CB  . ILE C 487 ? 0.3677 0.8090 2.1076 0.1146  0.1876  0.2511  487 ILE C CB  
12394 C CG1 . ILE C 487 ? 0.3737 0.8018 2.0762 0.1336  0.1922  0.2358  487 ILE C CG1 
12395 C CG2 . ILE C 487 ? 0.3550 0.7881 2.1128 0.1079  0.1743  0.2399  487 ILE C CG2 
12396 C CD1 . ILE C 487 ? 0.3739 0.8227 2.0750 0.1505  0.1992  0.2274  487 ILE C CD1 
12397 N N   . PRO C 488 ? 0.3992 0.8114 2.2011 0.0657  0.1654  0.2722  488 PRO C N   
12398 C CA  . PRO C 488 ? 0.4037 0.8279 2.2485 0.0467  0.1601  0.2840  488 PRO C CA  
12399 C C   . PRO C 488 ? 0.4038 0.8580 2.2672 0.0484  0.1597  0.2804  488 PRO C C   
12400 O O   . PRO C 488 ? 0.3892 0.8361 2.2386 0.0569  0.1534  0.2616  488 PRO C O   
12401 C CB  . PRO C 488 ? 0.4023 0.7879 2.2532 0.0343  0.1439  0.2706  488 PRO C CB  
12402 C CG  . PRO C 488 ? 0.3971 0.7519 2.2081 0.0463  0.1435  0.2583  488 PRO C CG  
12403 C CD  . PRO C 488 ? 0.3954 0.7666 2.1770 0.0660  0.1539  0.2535  488 PRO C CD  
12404 N N   . ASP C 489 ? 0.4288 0.9181 2.3254 0.0399  0.1665  0.3004  489 ASP C N   
12405 C CA  . ASP C 489 ? 0.4338 0.9587 2.3555 0.0400  0.1671  0.3019  489 ASP C CA  
12406 C C   . ASP C 489 ? 0.4411 0.9539 2.3786 0.0300  0.1488  0.2844  489 ASP C C   
12407 O O   . ASP C 489 ? 0.4460 0.9800 2.3897 0.0361  0.1463  0.2775  489 ASP C O   
12408 C CB  . ASP C 489 ? 0.4433 1.0045 2.4034 0.0280  0.1758  0.3284  489 ASP C CB  
12409 C CG  . ASP C 489 ? 0.4568 1.0407 2.4034 0.0379  0.1955  0.3484  489 ASP C CG  
12410 O OD1 . ASP C 489 ? 0.4548 1.0294 2.3610 0.0562  0.2027  0.3393  489 ASP C OD1 
12411 O OD2 . ASP C 489 ? 0.4786 1.0907 2.4560 0.0267  0.2031  0.3732  489 ASP C OD2 
12412 N N   . ASN C 490 ? 0.4560 0.9369 2.4006 0.0152  0.1361  0.2772  490 ASN C N   
12413 C CA  . ASN C 490 ? 0.4656 0.9328 2.4199 0.0061  0.1182  0.2571  490 ASN C CA  
12414 C C   . ASN C 490 ? 0.4761 0.9130 2.3901 0.0189  0.1125  0.2348  490 ASN C C   
12415 O O   . ASN C 490 ? 0.4841 0.9071 2.3996 0.0126  0.0981  0.2169  490 ASN C O   
12416 C CB  . ASN C 490 ? 0.4790 0.9287 2.4652 -0.0162 0.1068  0.2577  490 ASN C CB  
12417 C CG  . ASN C 490 ? 0.4859 0.8973 2.4579 -0.0182 0.1073  0.2584  490 ASN C CG  
12418 O OD1 . ASN C 490 ? 0.5040 0.9108 2.4507 -0.0067 0.1194  0.2688  490 ASN C OD1 
12419 N ND2 . ASN C 490 ? 0.4906 0.8756 2.4803 -0.0328 0.0938  0.2474  490 ASN C ND2 
12420 N N   . CYS C 491 ? 0.4859 0.9137 2.3646 0.0362  0.1234  0.2353  491 CYS C N   
12421 C CA  . CYS C 491 ? 0.4820 0.8861 2.3254 0.0492  0.1192  0.2163  491 CYS C CA  
12422 C C   . CYS C 491 ? 0.4773 0.9038 2.3206 0.0589  0.1170  0.2097  491 CYS C C   
12423 O O   . CYS C 491 ? 0.4984 0.9505 2.3425 0.0704  0.1279  0.2187  491 CYS C O   
12424 C CB  . CYS C 491 ? 0.4935 0.8836 2.3028 0.0645  0.1306  0.2181  491 CYS C CB  
12425 S SG  . CYS C 491 ? 0.5516 0.9134 2.3225 0.0791  0.1252  0.1962  491 CYS C SG  
12426 N N   . TRP C 492 ? 0.4660 0.8848 2.3092 0.0546  0.1030  0.1943  492 TRP C N   
12427 C CA  . TRP C 492 ? 0.4435 0.8843 2.2883 0.0628  0.0988  0.1898  492 TRP C CA  
12428 C C   . TRP C 492 ? 0.4292 0.8514 2.2390 0.0802  0.1005  0.1798  492 TRP C C   
12429 O O   . TRP C 492 ? 0.4343 0.8735 2.2413 0.0937  0.1037  0.1817  492 TRP C O   
12430 C CB  . TRP C 492 ? 0.4471 0.8952 2.3114 0.0483  0.0820  0.1797  492 TRP C CB  
12431 C CG  . TRP C 492 ? 0.4638 0.9310 2.3680 0.0296  0.0779  0.1878  492 TRP C CG  
12432 C CD1 . TRP C 492 ? 0.4780 0.9402 2.4009 0.0121  0.0629  0.1765  492 TRP C CD1 
12433 C CD2 . TRP C 492 ? 0.4710 0.9659 2.4035 0.0257  0.0881  0.2078  492 TRP C CD2 
12434 N NE1 . TRP C 492 ? 0.4868 0.9700 2.4497 -0.0031 0.0620  0.1881  492 TRP C NE1 
12435 C CE2 . TRP C 492 ? 0.4697 0.9738 2.4395 0.0045  0.0778  0.2088  492 TRP C CE2 
12436 C CE3 . TRP C 492 ? 0.4737 0.9879 2.4047 0.0378  0.1051  0.2244  492 TRP C CE3 
12437 C CZ2 . TRP C 492 ? 0.4727 1.0037 2.4789 -0.0056 0.0840  0.2280  492 TRP C CZ2 
12438 C CZ3 . TRP C 492 ? 0.4683 1.0120 2.4330 0.0290  0.1122  0.2431  492 TRP C CZ3 
12439 C CH2 . TRP C 492 ? 0.4742 1.0260 2.4768 0.0071  0.1019  0.2461  492 TRP C CH2 
12440 N N   . VAL C 493 ? 0.4137 0.8010 2.1998 0.0794  0.0977  0.1697  493 VAL C N   
12441 C CA  . VAL C 493 ? 0.3981 0.7646 2.1531 0.0931  0.0981  0.1602  493 VAL C CA  
12442 C C   . VAL C 493 ? 0.3962 0.7294 2.1306 0.0922  0.1011  0.1559  493 VAL C C   
12443 O O   . VAL C 493 ? 0.3771 0.6981 2.1205 0.0789  0.0963  0.1543  493 VAL C O   
12444 C CB  . VAL C 493 ? 0.3893 0.7560 2.1406 0.0914  0.0851  0.1487  493 VAL C CB  
12445 C CG1 . VAL C 493 ? 0.3861 0.7368 2.1399 0.0760  0.0739  0.1370  493 VAL C CG1 
12446 C CG2 . VAL C 493 ? 0.3917 0.7434 2.1160 0.1066  0.0867  0.1435  493 VAL C CG2 
12447 N N   . VAL C 494 ? 0.4014 0.7206 2.1107 0.1067  0.1085  0.1541  494 VAL C N   
12448 C CA  . VAL C 494 ? 0.4038 0.6946 2.0922 0.1081  0.1116  0.1508  494 VAL C CA  
12449 C C   . VAL C 494 ? 0.3846 0.6534 2.0482 0.1174  0.1085  0.1390  494 VAL C C   
12450 O O   . VAL C 494 ? 0.3712 0.6468 2.0302 0.1278  0.1089  0.1371  494 VAL C O   
12451 C CB  . VAL C 494 ? 0.4173 0.7138 2.0993 0.1152  0.1245  0.1610  494 VAL C CB  
12452 C CG1 . VAL C 494 ? 0.4244 0.7335 2.0967 0.1325  0.1330  0.1607  494 VAL C CG1 
12453 C CG2 . VAL C 494 ? 0.4148 0.6848 2.0774 0.1148  0.1258  0.1589  494 VAL C CG2 
12454 N N   . ASN C 495 ? 0.3888 0.6313 2.0387 0.1137  0.1055  0.1324  495 ASN C N   
12455 C CA  . ASN C 495 ? 0.3769 0.5983 2.0042 0.1219  0.1039  0.1231  495 ASN C CA  
12456 C C   . ASN C 495 ? 0.3823 0.5893 1.9934 0.1281  0.1111  0.1247  495 ASN C C   
12457 O O   . ASN C 495 ? 0.4065 0.5992 2.0149 0.1215  0.1097  0.1248  495 ASN C O   
12458 C CB  . ASN C 495 ? 0.3699 0.5768 1.9947 0.1137  0.0940  0.1128  495 ASN C CB  
12459 C CG  . ASN C 495 ? 0.3710 0.5636 1.9768 0.1221  0.0924  0.1056  495 ASN C CG  
12460 O OD1 . ASN C 495 ? 0.3884 0.5692 1.9804 0.1310  0.0979  0.1059  495 ASN C OD1 
12461 N ND2 . ASN C 495 ? 0.3617 0.5572 1.9669 0.1194  0.0850  0.0996  495 ASN C ND2 
12462 N N   . ALA C 496 ? 0.3834 0.5958 1.9851 0.1410  0.1184  0.1256  496 ALA C N   
12463 C CA  . ALA C 496 ? 0.3904 0.5921 1.9743 0.1482  0.1246  0.1246  496 ALA C CA  
12464 C C   . ALA C 496 ? 0.3806 0.5577 1.9470 0.1534  0.1202  0.1134  496 ALA C C   
12465 O O   . ALA C 496 ? 0.3740 0.5496 1.9386 0.1615  0.1196  0.1089  496 ALA C O   
12466 C CB  . ALA C 496 ? 0.4084 0.6294 1.9917 0.1599  0.1345  0.1283  496 ALA C CB  
12467 N N   . SER C 497 ? 0.3822 0.5409 1.9389 0.1483  0.1170  0.1106  497 SER C N   
12468 C CA  . SER C 497 ? 0.3814 0.5178 1.9245 0.1507  0.1123  0.1011  497 SER C CA  
12469 C C   . SER C 497 ? 0.3841 0.5084 1.9125 0.1524  0.1137  0.0997  497 SER C C   
12470 O O   . SER C 497 ? 0.3738 0.5055 1.9033 0.1491  0.1168  0.1075  497 SER C O   
12471 C CB  . SER C 497 ? 0.3800 0.5082 1.9293 0.1416  0.1045  0.0976  497 SER C CB  
12472 O OG  . SER C 497 ? 0.3910 0.5178 1.9485 0.1316  0.1025  0.1010  497 SER C OG  
12473 N N   . ALA C 498 ? 0.3925 0.4998 1.9084 0.1573  0.1109  0.0907  498 ALA C N   
12474 C CA  . ALA C 498 ? 0.3929 0.4879 1.8948 0.1584  0.1097  0.0875  498 ALA C CA  
12475 C C   . ALA C 498 ? 0.3826 0.4582 1.8806 0.1573  0.1033  0.0791  498 ALA C C   
12476 O O   . ALA C 498 ? 0.3715 0.4443 1.8746 0.1583  0.1014  0.0761  498 ALA C O   
12477 C CB  . ALA C 498 ? 0.4070 0.5082 1.8959 0.1687  0.1152  0.0843  498 ALA C CB  
12478 N N   . GLY C 499 ? 0.3922 0.4568 1.8822 0.1553  0.0999  0.0770  499 GLY C N   
12479 C CA  . GLY C 499 ? 0.3865 0.4351 1.8758 0.1530  0.0941  0.0705  499 GLY C CA  
12480 C C   . GLY C 499 ? 0.3896 0.4294 1.8709 0.1519  0.0905  0.0688  499 GLY C C   
12481 O O   . GLY C 499 ? 0.3917 0.4374 1.8702 0.1507  0.0915  0.0753  499 GLY C O   
12482 N N   . ILE C 500 ? 0.3859 0.4131 1.8650 0.1524  0.0860  0.0616  500 ILE C N   
12483 C CA  . ILE C 500 ? 0.3785 0.3976 1.8524 0.1513  0.0811  0.0589  500 ILE C CA  
12484 C C   . ILE C 500 ? 0.3702 0.3786 1.8506 0.1484  0.0770  0.0539  500 ILE C C   
12485 O O   . ILE C 500 ? 0.3598 0.3657 1.8440 0.1494  0.0778  0.0513  500 ILE C O   
12486 C CB  . ILE C 500 ? 0.3864 0.4063 1.8462 0.1579  0.0808  0.0534  500 ILE C CB  
12487 C CG1 . ILE C 500 ? 0.3874 0.4052 1.8408 0.1565  0.0752  0.0535  500 ILE C CG1 
12488 C CG2 . ILE C 500 ? 0.3879 0.3993 1.8476 0.1624  0.0800  0.0435  500 ILE C CG2 
12489 C CD1 . ILE C 500 ? 0.4067 0.4317 1.8434 0.1629  0.0749  0.0487  500 ILE C CD1 
12490 N N   . SER C 501 ? 0.3737 0.3775 1.8564 0.1451  0.0727  0.0540  501 SER C N   
12491 C CA  . SER C 501 ? 0.3739 0.3707 1.8637 0.1422  0.0692  0.0502  501 SER C CA  
12492 C C   . SER C 501 ? 0.3734 0.3635 1.8587 0.1445  0.0651  0.0439  501 SER C C   
12493 O O   . SER C 501 ? 0.3705 0.3614 1.8461 0.1475  0.0627  0.0418  501 SER C O   
12494 C CB  . SER C 501 ? 0.3833 0.3795 1.8804 0.1386  0.0666  0.0527  501 SER C CB  
12495 O OG  . SER C 501 ? 0.3945 0.3953 1.8962 0.1366  0.0692  0.0581  501 SER C OG  
12496 N N   . VAL C 502 ? 0.3820 0.3671 1.8752 0.1426  0.0640  0.0413  502 VAL C N   
12497 C CA  . VAL C 502 ? 0.4095 0.3865 1.9036 0.1435  0.0599  0.0352  502 VAL C CA  
12498 C C   . VAL C 502 ? 0.4087 0.3841 1.9145 0.1385  0.0568  0.0357  502 VAL C C   
12499 O O   . VAL C 502 ? 0.4151 0.3955 1.9277 0.1359  0.0600  0.0401  502 VAL C O   
12500 C CB  . VAL C 502 ? 0.4137 0.3861 1.9103 0.1466  0.0627  0.0340  502 VAL C CB  
12501 C CG1 . VAL C 502 ? 0.4357 0.3970 1.9359 0.1475  0.0578  0.0263  502 VAL C CG1 
12502 C CG2 . VAL C 502 ? 0.4117 0.3892 1.8997 0.1522  0.0673  0.0343  502 VAL C CG2 
12503 N N   . ARG C 503 ? 0.4305 0.4011 1.9388 0.1373  0.0505  0.0307  503 ARG C N   
12504 C CA  . ARG C 503 ? 0.4269 0.3987 1.9490 0.1324  0.0476  0.0319  503 ARG C CA  
12505 C C   . ARG C 503 ? 0.4218 0.3856 1.9532 0.1300  0.0433  0.0279  503 ARG C C   
12506 O O   . ARG C 503 ? 0.4281 0.3861 1.9550 0.1313  0.0373  0.0198  503 ARG C O   
12507 C CB  . ARG C 503 ? 0.4385 0.4151 1.9618 0.1315  0.0426  0.0317  503 ARG C CB  
12508 C CG  . ARG C 503 ? 0.4643 0.4452 2.0042 0.1272  0.0411  0.0334  503 ARG C CG  
12509 C CD  . ARG C 503 ? 0.4942 0.4777 2.0391 0.1261  0.0324  0.0307  503 ARG C CD  
12510 N NE  . ARG C 503 ? 0.5420 0.5303 2.0808 0.1294  0.0307  0.0335  503 ARG C NE  
12511 C CZ  . ARG C 503 ? 0.6072 0.5996 2.1521 0.1305  0.0349  0.0383  503 ARG C CZ  
12512 N NH1 . ARG C 503 ? 0.6049 0.6004 2.1608 0.1287  0.0407  0.0389  503 ARG C NH1 
12513 N NH2 . ARG C 503 ? 0.6291 0.6233 2.1702 0.1335  0.0331  0.0425  503 ARG C NH2 
12514 N N   . TYR C 504 ? 0.4106 0.3755 1.9559 0.1261  0.0461  0.0335  504 TYR C N   
12515 C CA  . TYR C 504 ? 0.4081 0.3672 1.9692 0.1215  0.0419  0.0330  504 TYR C CA  
12516 C C   . TYR C 504 ? 0.3991 0.3692 1.9743 0.1163  0.0427  0.0388  504 TYR C C   
12517 O O   . TYR C 504 ? 0.3974 0.3759 1.9778 0.1149  0.0493  0.0471  504 TYR C O   
12518 C CB  . TYR C 504 ? 0.4167 0.3692 1.9854 0.1214  0.0456  0.0385  504 TYR C CB  
12519 C CG  . TYR C 504 ? 0.4373 0.3801 2.0253 0.1162  0.0403  0.0379  504 TYR C CG  
12520 C CD1 . TYR C 504 ? 0.4254 0.3759 2.0317 0.1094  0.0413  0.0472  504 TYR C CD1 
12521 C CD2 . TYR C 504 ? 0.4568 0.3838 2.0464 0.1180  0.0343  0.0274  504 TYR C CD2 
12522 C CE1 . TYR C 504 ? 0.4346 0.3765 2.0622 0.1033  0.0361  0.0481  504 TYR C CE1 
12523 C CE2 . TYR C 504 ? 0.4633 0.3796 2.0739 0.1123  0.0282  0.0256  504 TYR C CE2 
12524 C CZ  . TYR C 504 ? 0.4538 0.3773 2.0845 0.1043  0.0290  0.0370  504 TYR C CZ  
12525 O OH  . TYR C 504 ? 0.4687 0.3828 2.1241 0.0971  0.0231  0.0375  504 TYR C OH  
12526 N N   . GLY C 505 ? 0.3931 0.3658 1.9740 0.1139  0.0359  0.0345  505 GLY C N   
12527 C CA  . GLY C 505 ? 0.3799 0.3650 1.9764 0.1099  0.0368  0.0395  505 GLY C CA  
12528 C C   . GLY C 505 ? 0.3688 0.3645 1.9589 0.1136  0.0426  0.0417  505 GLY C C   
12529 O O   . GLY C 505 ? 0.3775 0.3713 1.9563 0.1176  0.0401  0.0380  505 GLY C O   
12530 N N   . LYS C 506 ? 0.3633 0.3708 1.9614 0.1124  0.0502  0.0477  506 LYS C N   
12531 C CA  . LYS C 506 ? 0.3514 0.3689 1.9456 0.1159  0.0560  0.0472  506 LYS C CA  
12532 C C   . LYS C 506 ? 0.3396 0.3551 1.9193 0.1186  0.0615  0.0478  506 LYS C C   
12533 O O   . LYS C 506 ? 0.3213 0.3437 1.8973 0.1210  0.0657  0.0457  506 LYS C O   
12534 C CB  . LYS C 506 ? 0.3551 0.3901 1.9638 0.1139  0.0620  0.0512  506 LYS C CB  
12535 C CG  . LYS C 506 ? 0.3655 0.4085 1.9929 0.1117  0.0581  0.0514  506 LYS C CG  
12536 C CD  . LYS C 506 ? 0.3658 0.4302 2.0062 0.1120  0.0661  0.0539  506 LYS C CD  
12537 C CE  . LYS C 506 ? 0.3792 0.4555 2.0420 0.1084  0.0640  0.0572  506 LYS C CE  
12538 N NZ  . LYS C 506 ? 0.3851 0.4848 2.0602 0.1074  0.0738  0.0628  506 LYS C NZ  
12539 N N   . PHE C 507 ? 0.3498 0.3563 1.9236 0.1181  0.0608  0.0501  507 PHE C N   
12540 C CA  . PHE C 507 ? 0.3401 0.3466 1.9032 0.1203  0.0654  0.0526  507 PHE C CA  
12541 C C   . PHE C 507 ? 0.3370 0.3331 1.8870 0.1241  0.0626  0.0477  507 PHE C C   
12542 O O   . PHE C 507 ? 0.3284 0.3144 1.8760 0.1249  0.0575  0.0443  507 PHE C O   
12543 C CB  . PHE C 507 ? 0.3457 0.3507 1.9148 0.1182  0.0669  0.0604  507 PHE C CB  
12544 C CG  . PHE C 507 ? 0.3428 0.3524 1.9043 0.1205  0.0716  0.0658  507 PHE C CG  
12545 C CD1 . PHE C 507 ? 0.3401 0.3392 1.8935 0.1242  0.0702  0.0642  507 PHE C CD1 
12546 C CD2 . PHE C 507 ? 0.3363 0.3632 1.8994 0.1191  0.0772  0.0731  507 PHE C CD2 
12547 C CE1 . PHE C 507 ? 0.3358 0.3410 1.8847 0.1265  0.0737  0.0701  507 PHE C CE1 
12548 C CE2 . PHE C 507 ? 0.3294 0.3630 1.8858 0.1212  0.0801  0.0788  507 PHE C CE2 
12549 C CZ  . PHE C 507 ? 0.3330 0.3554 1.8835 0.1248  0.0781  0.0777  507 PHE C CZ  
12550 N N   . THR C 508 ? 0.3407 0.3418 1.8832 0.1261  0.0661  0.0470  508 THR C N   
12551 C CA  . THR C 508 ? 0.3395 0.3353 1.8713 0.1291  0.0652  0.0448  508 THR C CA  
12552 C C   . THR C 508 ? 0.3238 0.3256 1.8509 0.1299  0.0698  0.0473  508 THR C C   
12553 O O   . THR C 508 ? 0.3111 0.3232 1.8413 0.1283  0.0730  0.0483  508 THR C O   
12554 C CB  . THR C 508 ? 0.3507 0.3472 1.8833 0.1296  0.0635  0.0423  508 THR C CB  
12555 O OG1 . THR C 508 ? 0.3581 0.3635 1.8961 0.1284  0.0675  0.0412  508 THR C OG1 
12556 C CG2 . THR C 508 ? 0.3519 0.3461 1.8909 0.1291  0.0582  0.0409  508 THR C CG2 
12557 N N   . PHE C 509 ? 0.3273 0.3249 1.8468 0.1328  0.0699  0.0479  509 PHE C N   
12558 C CA  . PHE C 509 ? 0.3206 0.3250 1.8372 0.1340  0.0734  0.0511  509 PHE C CA  
12559 C C   . PHE C 509 ? 0.3275 0.3290 1.8369 0.1373  0.0736  0.0505  509 PHE C C   
12560 O O   . PHE C 509 ? 0.3253 0.3210 1.8307 0.1384  0.0713  0.0480  509 PHE C O   
12561 C CB  . PHE C 509 ? 0.3194 0.3249 1.8401 0.1345  0.0746  0.0564  509 PHE C CB  
12562 C CG  . PHE C 509 ? 0.3220 0.3145 1.8441 0.1374  0.0723  0.0555  509 PHE C CG  
12563 C CD1 . PHE C 509 ? 0.3301 0.3137 1.8561 0.1356  0.0683  0.0515  509 PHE C CD1 
12564 C CD2 . PHE C 509 ? 0.3241 0.3139 1.8451 0.1421  0.0736  0.0574  509 PHE C CD2 
12565 C CE1 . PHE C 509 ? 0.3441 0.3155 1.8721 0.1379  0.0651  0.0477  509 PHE C CE1 
12566 C CE2 . PHE C 509 ? 0.3390 0.3159 1.8624 0.1455  0.0713  0.0535  509 PHE C CE2 
12567 C CZ  . PHE C 509 ? 0.3483 0.3154 1.8748 0.1431  0.0668  0.0479  509 PHE C CZ  
12568 N N   . LYS C 510 ? 0.3337 0.3422 1.8418 0.1388  0.0765  0.0535  510 LYS C N   
12569 C CA  . LYS C 510 ? 0.3548 0.3641 1.8575 0.1421  0.0779  0.0540  510 LYS C CA  
12570 C C   . LYS C 510 ? 0.3674 0.3773 1.8701 0.1474  0.0800  0.0559  510 LYS C C   
12571 O O   . LYS C 510 ? 0.3776 0.3926 1.8855 0.1474  0.0808  0.0599  510 LYS C O   
12572 C CB  . LYS C 510 ? 0.3689 0.3876 1.8742 0.1388  0.0793  0.0560  510 LYS C CB  
12573 C CG  . LYS C 510 ? 0.3856 0.4007 1.8934 0.1352  0.0772  0.0543  510 LYS C CG  
12574 C CD  . LYS C 510 ? 0.4029 0.4243 1.9169 0.1314  0.0779  0.0560  510 LYS C CD  
12575 C CE  . LYS C 510 ? 0.4230 0.4476 1.9344 0.1330  0.0800  0.0618  510 LYS C CE  
12576 N NZ  . LYS C 510 ? 0.4358 0.4547 1.9452 0.1332  0.0785  0.0648  510 LYS C NZ  
12577 N N   . ILE C 511 ? 0.3787 0.3849 1.8757 0.1526  0.0808  0.0530  511 ILE C N   
12578 C CA  . ILE C 511 ? 0.3790 0.3868 1.8773 0.1594  0.0837  0.0535  511 ILE C CA  
12579 C C   . ILE C 511 ? 0.3783 0.3991 1.8735 0.1613  0.0878  0.0563  511 ILE C C   
12580 O O   . ILE C 511 ? 0.3907 0.4148 1.8813 0.1581  0.0879  0.0570  511 ILE C O   
12581 C CB  . ILE C 511 ? 0.3815 0.3764 1.8772 0.1648  0.0819  0.0456  511 ILE C CB  
12582 C CG1 . ILE C 511 ? 0.3862 0.3803 1.8699 0.1656  0.0806  0.0392  511 ILE C CG1 
12583 C CG2 . ILE C 511 ? 0.3753 0.3585 1.8794 0.1616  0.0779  0.0454  511 ILE C CG2 
12584 C CD1 . ILE C 511 ? 0.4014 0.3851 1.8809 0.1710  0.0780  0.0282  511 ILE C CD1 
12585 N N   . HIS C 512 ? 0.3701 0.3997 1.8705 0.1660  0.0912  0.0598  512 HIS C N   
12586 C CA  . HIS C 512 ? 0.3622 0.4081 1.8648 0.1651  0.0947  0.0650  512 HIS C CA  
12587 C C   . HIS C 512 ? 0.3768 0.4333 1.8876 0.1715  0.0979  0.0689  512 HIS C C   
12588 O O   . HIS C 512 ? 0.4187 0.4681 1.9335 0.1772  0.0973  0.0679  512 HIS C O   
12589 C CB  . HIS C 512 ? 0.3394 0.3904 1.8464 0.1556  0.0921  0.0684  512 HIS C CB  
12590 C CG  . HIS C 512 ? 0.3264 0.3772 1.8383 0.1528  0.0890  0.0693  512 HIS C CG  
12591 N ND1 . HIS C 512 ? 0.3167 0.3773 1.8351 0.1559  0.0895  0.0742  512 HIS C ND1 
12592 C CD2 . HIS C 512 ? 0.3186 0.3631 1.8299 0.1479  0.0858  0.0670  512 HIS C CD2 
12593 C CE1 . HIS C 512 ? 0.3135 0.3751 1.8334 0.1524  0.0865  0.0758  512 HIS C CE1 
12594 N NE2 . HIS C 512 ? 0.3176 0.3698 1.8332 0.1476  0.0848  0.0709  512 HIS C NE2 
12595 N N   . ASP C 513 ? 0.3769 0.4508 1.8927 0.1706  0.1010  0.0743  513 ASP C N   
12596 C CA  . ASP C 513 ? 0.3710 0.4591 1.8959 0.1774  0.1046  0.0785  513 ASP C CA  
12597 C C   . ASP C 513 ? 0.3697 0.4778 1.9027 0.1712  0.1057  0.0853  513 ASP C C   
12598 O O   . ASP C 513 ? 0.3663 0.4742 1.8969 0.1632  0.1049  0.0858  513 ASP C O   
12599 C CB  . ASP C 513 ? 0.3845 0.4723 1.9050 0.1881  0.1104  0.0735  513 ASP C CB  
12600 C CG  . ASP C 513 ? 0.3952 0.4887 1.9266 0.1989  0.1132  0.0746  513 ASP C CG  
12601 O OD1 . ASP C 513 ? 0.4024 0.4941 1.9428 0.1981  0.1092  0.0796  513 ASP C OD1 
12602 O OD2 . ASP C 513 ? 0.4038 0.5054 1.9352 0.2084  0.1195  0.0712  513 ASP C OD2 
12603 N N   . GLN C 514 ? 0.3723 0.4975 1.9172 0.1748  0.1071  0.0909  514 GLN C N   
12604 C CA  . GLN C 514 ? 0.3622 0.5081 1.9187 0.1678  0.1063  0.0973  514 GLN C CA  
12605 C C   . GLN C 514 ? 0.3760 0.5423 1.9453 0.1759  0.1102  0.1031  514 GLN C C   
12606 O O   . GLN C 514 ? 0.3794 0.5464 1.9537 0.1831  0.1087  0.1048  514 GLN C O   
12607 C CB  . GLN C 514 ? 0.3508 0.4973 1.9101 0.1596  0.0986  0.0972  514 GLN C CB  
12608 C CG  . GLN C 514 ? 0.3400 0.5042 1.9107 0.1493  0.0952  0.0996  514 GLN C CG  
12609 C CD  . GLN C 514 ? 0.3336 0.5004 1.9042 0.1424  0.0874  0.0964  514 GLN C CD  
12610 O OE1 . GLN C 514 ? 0.3327 0.4893 1.8985 0.1349  0.0841  0.0899  514 GLN C OE1 
12611 N NE2 . GLN C 514 ? 0.3290 0.5110 1.9048 0.1460  0.0845  0.1011  514 GLN C NE2 
12612 N N   . LYS C 515 ? 0.3834 0.5677 1.9603 0.1747  0.1153  0.1077  515 LYS C N   
12613 C CA  . LYS C 515 ? 0.3832 0.5927 1.9768 0.1800  0.1183  0.1146  515 LYS C CA  
12614 C C   . LYS C 515 ? 0.3686 0.5973 1.9764 0.1672  0.1148  0.1207  515 LYS C C   
12615 O O   . LYS C 515 ? 0.3671 0.5923 1.9732 0.1579  0.1153  0.1211  515 LYS C O   
12616 C CB  . LYS C 515 ? 0.3929 0.6114 1.9863 0.1916  0.1288  0.1146  515 LYS C CB  
12617 C CG  . LYS C 515 ? 0.4083 0.6055 1.9874 0.2031  0.1314  0.1049  515 LYS C CG  
12618 C CD  . LYS C 515 ? 0.4167 0.6013 1.9998 0.2098  0.1264  0.1030  515 LYS C CD  
12619 C CE  . LYS C 515 ? 0.4413 0.6094 2.0184 0.2234  0.1304  0.0934  515 LYS C CE  
12620 N NZ  . LYS C 515 ? 0.4488 0.5956 2.0274 0.2258  0.1240  0.0918  515 LYS C NZ  
12621 N N   . ILE C 516 ? 0.3567 0.6047 1.9795 0.1666  0.1101  0.1254  516 ILE C N   
12622 C CA  . ILE C 516 ? 0.3512 0.6202 1.9909 0.1545  0.1052  0.1298  516 ILE C CA  
12623 C C   . ILE C 516 ? 0.3509 0.6495 2.0101 0.1602  0.1107  0.1388  516 ILE C C   
12624 O O   . ILE C 516 ? 0.3639 0.6752 2.0310 0.1687  0.1091  0.1421  516 ILE C O   
12625 C CB  . ILE C 516 ? 0.3464 0.6190 1.9876 0.1485  0.0940  0.1272  516 ILE C CB  
12626 C CG1 . ILE C 516 ? 0.3430 0.5903 1.9667 0.1428  0.0892  0.1181  516 ILE C CG1 
12627 C CG2 . ILE C 516 ? 0.3475 0.6452 2.0086 0.1367  0.0877  0.1297  516 ILE C CG2 
12628 C CD1 . ILE C 516 ? 0.3413 0.5963 1.9644 0.1367  0.0790  0.1146  516 ILE C CD1 
12629 N N   . ILE C 517 ? 0.3481 0.6598 2.0172 0.1554  0.1171  0.1442  517 ILE C N   
12630 C CA  . ILE C 517 ? 0.3549 0.6957 2.0414 0.1631  0.1251  0.1529  517 ILE C CA  
12631 C C   . ILE C 517 ? 0.3398 0.7071 2.0516 0.1494  0.1226  0.1614  517 ILE C C   
12632 O O   . ILE C 517 ? 0.3371 0.6985 2.0511 0.1367  0.1221  0.1630  517 ILE C O   
12633 C CB  . ILE C 517 ? 0.3734 0.7113 2.0487 0.1739  0.1383  0.1530  517 ILE C CB  
12634 C CG1 . ILE C 517 ? 0.3876 0.6937 2.0370 0.1829  0.1388  0.1421  517 ILE C CG1 
12635 C CG2 . ILE C 517 ? 0.3736 0.7412 2.0647 0.1868  0.1477  0.1592  517 ILE C CG2 
12636 C CD1 . ILE C 517 ? 0.4028 0.7022 2.0360 0.1881  0.1486  0.1396  517 ILE C CD1 
12637 N N   . TYR C 518 ? 0.3248 0.7220 2.0581 0.1527  0.1213  0.1678  518 TYR C N   
12638 C CA  . TYR C 518 ? 0.3154 0.7402 2.0764 0.1390  0.1165  0.1751  518 TYR C CA  
12639 C C   . TYR C 518 ? 0.3170 0.7720 2.0980 0.1426  0.1287  0.1873  518 TYR C C   
12640 O O   . TYR C 518 ? 0.3203 0.7808 2.0951 0.1588  0.1404  0.1891  518 TYR C O   
12641 C CB  . TYR C 518 ? 0.3087 0.7519 2.0825 0.1393  0.1052  0.1749  518 TYR C CB  
12642 C CG  . TYR C 518 ? 0.3055 0.7290 2.0617 0.1373  0.0932  0.1651  518 TYR C CG  
12643 C CD1 . TYR C 518 ? 0.3078 0.7151 2.0456 0.1517  0.0944  0.1624  518 TYR C CD1 
12644 C CD2 . TYR C 518 ? 0.3061 0.7306 2.0666 0.1213  0.0805  0.1587  518 TYR C CD2 
12645 C CE1 . TYR C 518 ? 0.3074 0.7011 2.0305 0.1498  0.0844  0.1563  518 TYR C CE1 
12646 C CE2 . TYR C 518 ? 0.3051 0.7172 2.0488 0.1202  0.0705  0.1500  518 TYR C CE2 
12647 C CZ  . TYR C 518 ? 0.3041 0.7021 2.0289 0.1344  0.0728  0.1501  518 TYR C CZ  
12648 O OH  . TYR C 518 ? 0.2989 0.6881 2.0078 0.1333  0.0639  0.1441  518 TYR C OH  
12649 N N   . ARG C 519 ? 0.3101 0.7865 2.1172 0.1272  0.1259  0.1953  519 ARG C N   
12650 C CA  . ARG C 519 ? 0.3117 0.8227 2.1426 0.1287  0.1370  0.2091  519 ARG C CA  
12651 C C   . ARG C 519 ? 0.3085 0.8545 2.1659 0.1320  0.1322  0.2139  519 ARG C C   
12652 O O   . ARG C 519 ? 0.3086 0.8643 2.1833 0.1187  0.1187  0.2127  519 ARG C O   
12653 C CB  . ARG C 519 ? 0.3153 0.8319 2.1647 0.1093  0.1371  0.2183  519 ARG C CB  
12654 C CG  . ARG C 519 ? 0.3166 0.8748 2.1955 0.1088  0.1482  0.2352  519 ARG C CG  
12655 C CD  . ARG C 519 ? 0.3205 0.8838 2.2214 0.0886  0.1482  0.2470  519 ARG C CD  
12656 N NE  . ARG C 519 ? 0.3281 0.8643 2.2073 0.0866  0.1545  0.2490  519 ARG C NE  
12657 C CZ  . ARG C 519 ? 0.3353 0.8777 2.1992 0.0975  0.1704  0.2574  519 ARG C CZ  
12658 N NH1 . ARG C 519 ? 0.3358 0.9089 2.2017 0.1132  0.1831  0.2622  519 ARG C NH1 
12659 N NH2 . ARG C 519 ? 0.3408 0.8602 2.1876 0.0933  0.1734  0.2604  519 ARG C NH2 
12660 N N   . GLY C 520 ? 0.3070 0.8731 2.1685 0.1505  0.1430  0.2184  520 GLY C N   
12661 C CA  . GLY C 520 ? 0.2998 0.8975 2.1853 0.1573  0.1385  0.2231  520 GLY C CA  
12662 C C   . GLY C 520 ? 0.2950 0.8799 2.1736 0.1540  0.1211  0.2151  520 GLY C C   
12663 O O   . GLY C 520 ? 0.2946 0.8441 2.1445 0.1563  0.1172  0.2049  520 GLY C O   
12664 N N   . ASP C 521 ? 0.2945 0.9109 2.2002 0.1471  0.1103  0.2204  521 ASP C N   
12665 C CA  . ASP C 521 ? 0.2987 0.9173 2.2015 0.1512  0.0965  0.2170  521 ASP C CA  
12666 C C   . ASP C 521 ? 0.3013 0.9217 2.2081 0.1305  0.0786  0.2107  521 ASP C C   
12667 O O   . ASP C 521 ? 0.2995 0.9303 2.2061 0.1316  0.0656  0.2090  521 ASP C O   
12668 C CB  . ASP C 521 ? 0.3039 0.9614 2.2335 0.1647  0.0975  0.2280  521 ASP C CB  
12669 C CG  . ASP C 521 ? 0.3037 1.0064 2.2722 0.1525  0.0922  0.2375  521 ASP C CG  
12670 O OD1 . ASP C 521 ? 0.3024 1.0076 2.2814 0.1333  0.0912  0.2372  521 ASP C OD1 
12671 O OD2 . ASP C 521 ? 0.3037 1.0392 2.2941 0.1620  0.0882  0.2457  521 ASP C OD2 
12672 N N   . TRP C 522 ? 0.3077 0.9167 2.2169 0.1124  0.0776  0.2064  522 TRP C N   
12673 C CA  . TRP C 522 ? 0.3180 0.9307 2.2363 0.0924  0.0608  0.1982  522 TRP C CA  
12674 C C   . TRP C 522 ? 0.3259 0.9183 2.2160 0.0942  0.0490  0.1856  522 TRP C C   
12675 O O   . TRP C 522 ? 0.3334 0.9362 2.2286 0.0819  0.0333  0.1773  522 TRP C O   
12676 C CB  . TRP C 522 ? 0.3254 0.9202 2.2491 0.0749  0.0631  0.1951  522 TRP C CB  
12677 C CG  . TRP C 522 ? 0.3348 0.8839 2.2247 0.0758  0.0663  0.1847  522 TRP C CG  
12678 C CD1 . TRP C 522 ? 0.3390 0.8645 2.2082 0.0866  0.0808  0.1877  522 TRP C CD1 
12679 C CD2 . TRP C 522 ? 0.3424 0.8663 2.2162 0.0655  0.0539  0.1686  522 TRP C CD2 
12680 N NE1 . TRP C 522 ? 0.3358 0.8234 2.1784 0.0835  0.0779  0.1759  522 TRP C NE1 
12681 C CE2 . TRP C 522 ? 0.3409 0.8266 2.1862 0.0710  0.0622  0.1642  522 TRP C CE2 
12682 C CE3 . TRP C 522 ? 0.3503 0.8821 2.2304 0.0527  0.0367  0.1565  522 TRP C CE3 
12683 C CZ2 . TRP C 522 ? 0.3453 0.8014 2.1713 0.0643  0.0545  0.1493  522 TRP C CZ2 
12684 C CZ3 . TRP C 522 ? 0.3523 0.8543 2.2111 0.0466  0.0296  0.1401  522 TRP C CZ3 
12685 C CH2 . TRP C 522 ? 0.3473 0.8120 2.1805 0.0524  0.0388  0.1371  522 TRP C CH2 
12686 N N   . ALA C 523 ? 0.3312 0.8955 2.1917 0.1092  0.0562  0.1835  523 ALA C N   
12687 C CA  . ALA C 523 ? 0.3451 0.8889 2.1786 0.1097  0.0467  0.1730  523 ALA C CA  
12688 C C   . ALA C 523 ? 0.3542 0.9114 2.1830 0.1261  0.0440  0.1803  523 ALA C C   
12689 O O   . ALA C 523 ? 0.3610 0.8969 2.1648 0.1325  0.0421  0.1764  523 ALA C O   
12690 C CB  . ALA C 523 ? 0.3468 0.8475 2.1519 0.1117  0.0547  0.1651  523 ALA C CB  
12691 N N   . LYS C 524 ? 0.3617 0.9553 2.2171 0.1323  0.0435  0.1923  524 LYS C N   
12692 C CA  . LYS C 524 ? 0.3692 0.9781 2.2259 0.1487  0.0406  0.2021  524 LYS C CA  
12693 C C   . LYS C 524 ? 0.3855 1.0039 2.2307 0.1424  0.0234  0.1982  524 LYS C C   
12694 O O   . LYS C 524 ? 0.3958 1.0170 2.2329 0.1552  0.0204  0.2061  524 LYS C O   
12695 C CB  . LYS C 524 ? 0.3672 1.0173 2.2588 0.1557  0.0426  0.2156  524 LYS C CB  
12696 C CG  . LYS C 524 ? 0.3715 1.0611 2.2883 0.1399  0.0281  0.2165  524 LYS C CG  
12697 C CD  . LYS C 524 ? 0.3705 1.1010 2.3260 0.1441  0.0325  0.2296  524 LYS C CD  
12698 C CE  . LYS C 524 ? 0.3684 1.1362 2.3516 0.1257  0.0183  0.2290  524 LYS C CE  
12699 N NZ  . LYS C 524 ? 0.3731 1.1833 2.3934 0.1339  0.0224  0.2443  524 LYS C NZ  
12700 N N   . GLU C 525 ? 0.3951 1.0202 2.2411 0.1230  0.0122  0.1864  525 GLU C N   
12701 C CA  . GLU C 525 ? 0.4029 1.0386 2.2347 0.1162  -0.0040 0.1792  525 GLU C CA  
12702 C C   . GLU C 525 ? 0.4071 1.0043 2.2066 0.1109  -0.0028 0.1645  525 GLU C C   
12703 O O   . GLU C 525 ? 0.4092 0.9962 2.1851 0.1188  -0.0045 0.1657  525 GLU C O   
12704 C CB  . GLU C 525 ? 0.4090 1.0782 2.2616 0.0983  -0.0191 0.1717  525 GLU C CB  
12705 C CG  . GLU C 525 ? 0.4107 1.1278 2.2936 0.1026  -0.0261 0.1860  525 GLU C CG  
12706 C CD  . GLU C 525 ? 0.4040 1.1425 2.3246 0.0953  -0.0222 0.1912  525 GLU C CD  
12707 O OE1 . GLU C 525 ? 0.3972 1.1173 2.3237 0.0825  -0.0168 0.1826  525 GLU C OE1 
12708 O OE2 . GLU C 525 ? 0.4110 1.1869 2.3572 0.1030  -0.0244 0.2055  525 GLU C OE2 
12709 N N   . VAL C 526 ? 0.4135 0.9905 2.2145 0.0977  0.0003  0.1521  526 VAL C N   
12710 C CA  . VAL C 526 ? 0.4249 0.9740 2.2021 0.0885  -0.0029 0.1348  526 VAL C CA  
12711 C C   . VAL C 526 ? 0.4223 0.9322 2.1739 0.0997  0.0097  0.1360  526 VAL C C   
12712 O O   . VAL C 526 ? 0.4250 0.9157 2.1530 0.0977  0.0072  0.1256  526 VAL C O   
12713 C CB  . VAL C 526 ? 0.4258 0.9681 2.2190 0.0701  -0.0057 0.1218  526 VAL C CB  
12714 C CG1 . VAL C 526 ? 0.4213 0.9467 2.2281 0.0709  0.0089  0.1300  526 VAL C CG1 
12715 C CG2 . VAL C 526 ? 0.4317 0.9492 2.2044 0.0607  -0.0111 0.1018  526 VAL C CG2 
12716 N N   . GLY C 527 ? 0.4245 0.9243 2.1817 0.1115  0.0230  0.1477  527 GLY C N   
12717 C CA  . GLY C 527 ? 0.4285 0.8921 2.1640 0.1216  0.0344  0.1477  527 GLY C CA  
12718 C C   . GLY C 527 ? 0.4454 0.9058 2.1641 0.1344  0.0328  0.1540  527 GLY C C   
12719 O O   . GLY C 527 ? 0.4393 0.9277 2.1672 0.1402  0.0263  0.1640  527 GLY C O   
12720 N N   . ARG C 528 ? 0.4693 0.8962 2.1654 0.1385  0.0387  0.1495  528 ARG C N   
12721 C CA  . ARG C 528 ? 0.4807 0.8996 2.1619 0.1494  0.0384  0.1564  528 ARG C CA  
12722 C C   . ARG C 528 ? 0.5172 0.9418 2.2121 0.1660  0.0444  0.1715  528 ARG C C   
12723 O O   . ARG C 528 ? 0.5174 0.9310 2.2203 0.1719  0.0546  0.1717  528 ARG C O   
12724 C CB  . ARG C 528 ? 0.4605 0.8412 2.1196 0.1499  0.0448  0.1486  528 ARG C CB  
12725 C CG  . ARG C 528 ? 0.4536 0.8252 2.0999 0.1595  0.0446  0.1568  528 ARG C CG  
12726 C CD  . ARG C 528 ? 0.4368 0.7732 2.0640 0.1590  0.0504  0.1491  528 ARG C CD  
12727 N NE  . ARG C 528 ? 0.4188 0.7508 2.0332 0.1458  0.0462  0.1347  528 ARG C NE  
12728 C CZ  . ARG C 528 ? 0.4109 0.7265 2.0247 0.1382  0.0496  0.1230  528 ARG C CZ  
12729 N NH1 . ARG C 528 ? 0.4031 0.7080 2.0257 0.1417  0.0575  0.1247  528 ARG C NH1 
12730 N NH2 . ARG C 528 ? 0.4106 0.7223 2.0156 0.1274  0.0453  0.1098  528 ARG C NH2 
12731 N N   . LYS C 529 ? 0.5788 1.0202 2.2761 0.1740  0.0383  0.1839  529 LYS C N   
12732 C CA  . LYS C 529 ? 0.6353 1.0809 2.3481 0.1911  0.0428  0.1988  529 LYS C CA  
12733 C C   . LYS C 529 ? 0.7290 1.1398 2.4295 0.2016  0.0496  0.2015  529 LYS C C   
12734 O O   . LYS C 529 ? 0.7508 1.1374 2.4305 0.1951  0.0505  0.1928  529 LYS C O   
12735 C CB  . LYS C 529 ? 0.6356 1.1184 2.3604 0.1946  0.0316  0.2136  529 LYS C CB  
12736 C CG  . LYS C 529 ? 0.6267 1.1484 2.3637 0.1832  0.0212  0.2111  529 LYS C CG  
12737 C CD  . LYS C 529 ? 0.6148 1.1582 2.3812 0.1871  0.0249  0.2157  529 LYS C CD  
12738 C CE  . LYS C 529 ? 0.6047 1.1885 2.3860 0.1748  0.0128  0.2143  529 LYS C CE  
12739 N NZ  . LYS C 529 ? 0.6195 1.1947 2.3885 0.1558  0.0089  0.1959  529 LYS C NZ  
12740 N N   . LEU C 530 ? 0.8293 1.2388 2.5460 0.2180  0.0540  0.2134  530 LEU C N   
12741 C CA  . LEU C 530 ? 0.8962 1.2740 2.6097 0.2299  0.0599  0.2170  530 LEU C CA  
12742 C C   . LEU C 530 ? 0.8929 1.2388 2.5985 0.2311  0.0714  0.2016  530 LEU C C   
12743 O O   . LEU C 530 ? 0.9333 1.2488 2.6342 0.2388  0.0759  0.2004  530 LEU C O   
12744 C CB  . LEU C 530 ? 0.9492 1.3164 2.6470 0.2266  0.0541  0.2236  530 LEU C CB  
12745 C CG  . LEU C 530 ? 0.9340 1.3262 2.6426 0.2330  0.0453  0.2450  530 LEU C CG  
12746 C CD1 . LEU C 530 ? 0.9323 1.3647 2.6367 0.2219  0.0342  0.2464  530 LEU C CD1 
12747 C CD2 . LEU C 530 ? 0.8842 1.2561 2.5834 0.2355  0.0445  0.2552  530 LEU C CD2 
12748 N N   . SER D 3   ? 1.0729 1.0146 2.1297 -0.0745 0.3276  -0.1443 3   SER D N   
12749 C CA  . SER D 3   ? 1.0192 0.9791 2.1242 -0.0721 0.3253  -0.1323 3   SER D CA  
12750 C C   . SER D 3   ? 0.9681 0.9327 2.0949 -0.0670 0.2955  -0.1252 3   SER D C   
12751 O O   . SER D 3   ? 1.0021 0.9563 2.1004 -0.0701 0.2768  -0.1151 3   SER D O   
12752 C CB  . SER D 3   ? 1.0458 1.0019 2.1309 -0.0801 0.3347  -0.1163 3   SER D CB  
12753 O OG  . SER D 3   ? 1.0202 0.9926 2.1499 -0.0783 0.3320  -0.1051 3   SER D OG  
12754 N N   . LYS D 4   ? 0.8983 0.8776 2.0748 -0.0592 0.2913  -0.1309 4   LYS D N   
12755 C CA  . LYS D 4   ? 0.8339 0.8185 2.0348 -0.0546 0.2664  -0.1238 4   LYS D CA  
12756 C C   . LYS D 4   ? 0.7686 0.7715 2.0238 -0.0489 0.2686  -0.1214 4   LYS D C   
12757 O O   . LYS D 4   ? 0.7866 0.7983 2.0663 -0.0459 0.2863  -0.1310 4   LYS D O   
12758 C CB  . LYS D 4   ? 0.8478 0.8250 2.0435 -0.0507 0.2531  -0.1357 4   LYS D CB  
12759 C CG  . LYS D 4   ? 0.8513 0.8320 2.0704 -0.0444 0.2648  -0.1536 4   LYS D CG  
12760 C CD  . LYS D 4   ? 0.8766 0.8478 2.0896 -0.0413 0.2494  -0.1635 4   LYS D CD  
12761 C CE  . LYS D 4   ? 0.8872 0.8577 2.1165 -0.0354 0.2607  -0.1821 4   LYS D CE  
12762 N NZ  . LYS D 4   ? 0.8714 0.8574 2.1489 -0.0286 0.2699  -0.1832 4   LYS D NZ  
12763 N N   . THR D 5   ? 0.7075 0.7158 1.9819 -0.0470 0.2499  -0.1097 5   THR D N   
12764 C CA  . THR D 5   ? 0.6685 0.6923 1.9871 -0.0434 0.2505  -0.1038 5   THR D CA  
12765 C C   . THR D 5   ? 0.6317 0.6653 1.9879 -0.0357 0.2589  -0.1174 5   THR D C   
12766 O O   . THR D 5   ? 0.6032 0.6334 1.9664 -0.0303 0.2492  -0.1255 5   THR D O   
12767 C CB  . THR D 5   ? 0.6636 0.6897 1.9963 -0.0411 0.2276  -0.0930 5   THR D CB  
12768 O OG1 . THR D 5   ? 0.7334 0.7503 2.0341 -0.0470 0.2170  -0.0811 5   THR D OG1 
12769 C CG2 . THR D 5   ? 0.6311 0.6715 2.0046 -0.0381 0.2280  -0.0866 5   THR D CG2 
12770 N N   . LYS D 6   ? 0.6328 0.6786 2.0162 -0.0352 0.2753  -0.1189 6   LYS D N   
12771 C CA  . LYS D 6   ? 0.6104 0.6682 2.0383 -0.0269 0.2794  -0.1290 6   LYS D CA  
12772 C C   . LYS D 6   ? 0.5516 0.6186 2.0129 -0.0227 0.2630  -0.1196 6   LYS D C   
12773 O O   . LYS D 6   ? 0.5485 0.6212 2.0154 -0.0268 0.2627  -0.1080 6   LYS D O   
12774 C CB  . LYS D 6   ? 0.6519 0.7198 2.0964 -0.0285 0.3047  -0.1363 6   LYS D CB  
12775 C CG  . LYS D 6   ? 0.6946 0.7738 2.1836 -0.0192 0.3104  -0.1502 6   LYS D CG  
12776 C CD  . LYS D 6   ? 0.7691 0.8602 2.2791 -0.0209 0.3368  -0.1585 6   LYS D CD  
12777 C CE  . LYS D 6   ? 0.7980 0.9007 2.3535 -0.0111 0.3428  -0.1739 6   LYS D CE  
12778 N NZ  . LYS D 6   ? 0.7962 0.9079 2.3915 -0.0031 0.3233  -0.1697 6   LYS D NZ  
12779 N N   . ILE D 7   ? 0.5157 0.5825 1.9971 -0.0147 0.2496  -0.1245 7   ILE D N   
12780 C CA  . ILE D 7   ? 0.4816 0.5549 1.9914 -0.0102 0.2339  -0.1166 7   ILE D CA  
12781 C C   . ILE D 7   ? 0.4777 0.5613 2.0295 -0.0017 0.2376  -0.1261 7   ILE D C   
12782 O O   . ILE D 7   ? 0.4956 0.5758 2.0519 0.0035  0.2416  -0.1385 7   ILE D O   
12783 C CB  . ILE D 7   ? 0.4669 0.5296 1.9643 -0.0082 0.2134  -0.1126 7   ILE D CB  
12784 C CG1 . ILE D 7   ? 0.4633 0.5174 1.9242 -0.0160 0.2068  -0.1027 7   ILE D CG1 
12785 C CG2 . ILE D 7   ? 0.4401 0.5085 1.9680 -0.0025 0.1994  -0.1070 7   ILE D CG2 
12786 C CD1 . ILE D 7   ? 0.4518 0.4966 1.9023 -0.0149 0.1880  -0.0998 7   ILE D CD1 
12787 N N   . GLU D 8   ? 0.4753 0.5708 2.0581 0.0002  0.2343  -0.1206 8   GLU D N   
12788 C CA  . GLU D 8   ? 0.4874 0.5947 2.1122 0.0078  0.2393  -0.1299 8   GLU D CA  
12789 C C   . GLU D 8   ? 0.4740 0.5875 2.1263 0.0122  0.2229  -0.1225 8   GLU D C   
12790 O O   . GLU D 8   ? 0.4489 0.5674 2.1021 0.0069  0.2208  -0.1121 8   GLU D O   
12791 C CB  . GLU D 8   ? 0.5130 0.6313 2.1470 0.0029  0.2628  -0.1350 8   GLU D CB  
12792 C CG  . GLU D 8   ? 0.5241 0.6554 2.2011 0.0104  0.2728  -0.1487 8   GLU D CG  
12793 C CD  . GLU D 8   ? 0.5682 0.7111 2.2552 0.0041  0.2981  -0.1532 8   GLU D CD  
12794 O OE1 . GLU D 8   ? 0.5834 0.7212 2.2382 -0.0061 0.3070  -0.1447 8   GLU D OE1 
12795 O OE2 . GLU D 8   ? 0.5520 0.7084 2.2786 0.0092  0.3090  -0.1648 8   GLU D OE2 
12796 N N   . LEU D 9   ? 0.4898 0.6016 2.1634 0.0219  0.2115  -0.1284 9   LEU D N   
12797 C CA  . LEU D 9   ? 0.4961 0.6109 2.1932 0.0273  0.1946  -0.1229 9   LEU D CA  
12798 C C   . LEU D 9   ? 0.4834 0.6138 2.2256 0.0334  0.1989  -0.1307 9   LEU D C   
12799 O O   . LEU D 9   ? 0.4839 0.6156 2.2443 0.0407  0.2029  -0.1425 9   LEU D O   
12800 C CB  . LEU D 9   ? 0.5122 0.6119 2.1990 0.0338  0.1787  -0.1235 9   LEU D CB  
12801 C CG  . LEU D 9   ? 0.5391 0.6254 2.1894 0.0281  0.1696  -0.1141 9   LEU D CG  
12802 C CD1 . LEU D 9   ? 0.5722 0.6559 2.1911 0.0190  0.1813  -0.1129 9   LEU D CD1 
12803 C CD2 . LEU D 9   ? 0.5522 0.6235 2.1955 0.0342  0.1584  -0.1175 9   LEU D CD2 
12804 N N   . LYS D 10  ? 0.4780 0.6200 2.2396 0.0305  0.1976  -0.1246 10  LYS D N   
12805 C CA  . LYS D 10  ? 0.4855 0.6438 2.2933 0.0355  0.1999  -0.1317 10  LYS D CA  
12806 C C   . LYS D 10  ? 0.4122 0.5781 2.2350 0.0325  0.1908  -0.1227 10  LYS D C   
12807 O O   . LYS D 10  ? 0.4409 0.6053 2.2434 0.0234  0.1943  -0.1129 10  LYS D O   
12808 C CB  . LYS D 10  ? 0.5622 0.7334 2.3876 0.0327  0.2240  -0.1421 10  LYS D CB  
12809 C CG  . LYS D 10  ? 0.6411 0.8169 2.4500 0.0203  0.2433  -0.1369 10  LYS D CG  
12810 C CD  . LYS D 10  ? 0.7296 0.9173 2.5577 0.0185  0.2685  -0.1491 10  LYS D CD  
12811 C CE  . LYS D 10  ? 0.7747 0.9685 2.5947 0.0063  0.2888  -0.1440 10  LYS D CE  
12812 N NZ  . LYS D 10  ? 0.8238 1.0015 2.5899 -0.0022 0.2921  -0.1343 10  LYS D NZ  
12813 N N   . ASP D 11  ? 0.3590 0.5318 2.2169 0.0405  0.1778  -0.1263 11  ASP D N   
12814 C CA  . ASP D 11  ? 0.3327 0.5103 2.2044 0.0393  0.1650  -0.1190 11  ASP D CA  
12815 C C   . ASP D 11  ? 0.3150 0.4760 2.1491 0.0370  0.1508  -0.1070 11  ASP D C   
12816 O O   . ASP D 11  ? 0.3206 0.4822 2.1485 0.0310  0.1470  -0.0980 11  ASP D O   
12817 C CB  . ASP D 11  ? 0.3430 0.5369 2.2356 0.0308  0.1804  -0.1185 11  ASP D CB  
12818 C CG  . ASP D 11  ? 0.3684 0.5789 2.2978 0.0323  0.1979  -0.1315 11  ASP D CG  
12819 O OD1 . ASP D 11  ? 0.3502 0.5684 2.3159 0.0420  0.1894  -0.1408 11  ASP D OD1 
12820 O OD2 . ASP D 11  ? 0.4063 0.6212 2.3275 0.0240  0.2201  -0.1325 11  ASP D OD2 
12821 N N   . ASN D 12  ? 0.3018 0.4477 2.1115 0.0413  0.1444  -0.1074 12  ASN D N   
12822 C CA  . ASN D 12  ? 0.2772 0.4068 2.0555 0.0407  0.1304  -0.0981 12  ASN D CA  
12823 C C   . ASN D 12  ? 0.2638 0.3906 2.0131 0.0301  0.1363  -0.0880 12  ASN D C   
12824 O O   . ASN D 12  ? 0.2351 0.3535 1.9673 0.0282  0.1251  -0.0792 12  ASN D O   
12825 C CB  . ASN D 12  ? 0.2625 0.3899 2.0549 0.0465  0.1114  -0.0952 12  ASN D CB  
12826 C CG  . ASN D 12  ? 0.2648 0.3927 2.0838 0.0578  0.1025  -0.1042 12  ASN D CG  
12827 O OD1 . ASN D 12  ? 0.2740 0.3971 2.0934 0.0630  0.1060  -0.1114 12  ASN D OD1 
12828 N ND2 . ASN D 12  ? 0.2518 0.3842 2.0926 0.0617  0.0892  -0.1035 12  ASN D ND2 
12829 N N   . TRP D 13  ? 0.2701 0.4031 2.0137 0.0236  0.1541  -0.0898 13  TRP D N   
12830 C CA  . TRP D 13  ? 0.2790 0.4086 1.9945 0.0139  0.1610  -0.0810 13  TRP D CA  
12831 C C   . TRP D 13  ? 0.2815 0.4038 1.9700 0.0114  0.1716  -0.0849 13  TRP D C   
12832 O O   . TRP D 13  ? 0.2933 0.4192 1.9919 0.0145  0.1820  -0.0952 13  TRP D O   
12833 C CB  . TRP D 13  ? 0.3001 0.4425 2.0321 0.0072  0.1731  -0.0785 13  TRP D CB  
12834 C CG  . TRP D 13  ? 0.2926 0.4386 2.0380 0.0055  0.1628  -0.0709 13  TRP D CG  
12835 C CD1 . TRP D 13  ? 0.2943 0.4488 2.0731 0.0103  0.1540  -0.0739 13  TRP D CD1 
12836 C CD2 . TRP D 13  ? 0.2856 0.4261 2.0105 -0.0017 0.1603  -0.0592 13  TRP D CD2 
12837 N NE1 . TRP D 13  ? 0.2772 0.4313 2.0564 0.0063  0.1465  -0.0654 13  TRP D NE1 
12838 C CE2 . TRP D 13  ? 0.2726 0.4184 2.0199 -0.0009 0.1506  -0.0562 13  TRP D CE2 
12839 C CE3 . TRP D 13  ? 0.2947 0.4260 1.9852 -0.0082 0.1642  -0.0514 13  TRP D CE3 
12840 C CZ2 . TRP D 13  ? 0.2696 0.4112 2.0062 -0.0064 0.1459  -0.0460 13  TRP D CZ2 
12841 C CZ3 . TRP D 13  ? 0.2878 0.4154 1.9688 -0.0131 0.1583  -0.0407 13  TRP D CZ3 
12842 C CH2 . TRP D 13  ? 0.2795 0.4121 1.9834 -0.0121 0.1498  -0.0382 13  TRP D CH2 
12843 N N   . TYR D 14  ? 0.2742 0.3860 1.9293 0.0062  0.1682  -0.0772 14  TYR D N   
12844 C CA  . TYR D 14  ? 0.2770 0.3822 1.9030 0.0016  0.1783  -0.0793 14  TYR D CA  
12845 C C   . TYR D 14  ? 0.2888 0.4016 1.9137 -0.0057 0.1956  -0.0778 14  TYR D C   
12846 O O   . TYR D 14  ? 0.2678 0.3875 1.9055 -0.0092 0.1962  -0.0710 14  TYR D O   
12847 C CB  . TYR D 14  ? 0.2615 0.3545 1.8546 -0.0024 0.1684  -0.0710 14  TYR D CB  
12848 C CG  . TYR D 14  ? 0.2395 0.3219 1.8252 0.0025  0.1548  -0.0728 14  TYR D CG  
12849 C CD1 . TYR D 14  ? 0.2139 0.2950 1.8152 0.0078  0.1416  -0.0702 14  TYR D CD1 
12850 C CD2 . TYR D 14  ? 0.2485 0.3209 1.8094 0.0011  0.1554  -0.0767 14  TYR D CD2 
12851 C CE1 . TYR D 14  ? 0.2088 0.2785 1.8011 0.0112  0.1307  -0.0709 14  TYR D CE1 
12852 C CE2 . TYR D 14  ? 0.2402 0.3022 1.7947 0.0044  0.1439  -0.0779 14  TYR D CE2 
12853 C CZ  . TYR D 14  ? 0.2215 0.2819 1.7916 0.0093  0.1323  -0.0747 14  TYR D CZ  
12854 O OH  . TYR D 14  ? 0.2192 0.2677 1.7811 0.0117  0.1227  -0.0755 14  TYR D OH  
12855 N N   . HIS D 15  ? 0.3247 0.4347 1.9323 -0.0084 0.2099  -0.0842 15  HIS D N   
12856 C CA  . HIS D 15  ? 0.3614 0.4744 1.9582 -0.0165 0.2280  -0.0824 15  HIS D CA  
12857 C C   . HIS D 15  ? 0.3859 0.4856 1.9396 -0.0210 0.2320  -0.0826 15  HIS D C   
12858 O O   . HIS D 15  ? 0.4026 0.4969 1.9485 -0.0170 0.2323  -0.0924 15  HIS D O   
12859 C CB  . HIS D 15  ? 0.3853 0.5099 2.0090 -0.0147 0.2465  -0.0942 15  HIS D CB  
12860 C CG  . HIS D 15  ? 0.3839 0.5233 2.0542 -0.0101 0.2440  -0.0967 15  HIS D CG  
12861 N ND1 . HIS D 15  ? 0.3728 0.5136 2.0655 -0.0010 0.2263  -0.0990 15  HIS D ND1 
12862 C CD2 . HIS D 15  ? 0.3878 0.5407 2.0862 -0.0135 0.2563  -0.0974 15  HIS D CD2 
12863 C CE1 . HIS D 15  ? 0.3591 0.5138 2.0915 0.0013  0.2265  -0.1012 15  HIS D CE1 
12864 N NE2 . HIS D 15  ? 0.3673 0.5304 2.1058 -0.0062 0.2448  -0.1007 15  HIS D NE2 
12865 N N   . LEU D 16  ? 0.3948 0.4883 1.9205 -0.0291 0.2342  -0.0721 16  LEU D N   
12866 C CA  . LEU D 16  ? 0.4164 0.4972 1.8996 -0.0341 0.2390  -0.0724 16  LEU D CA  
12867 C C   . LEU D 16  ? 0.4430 0.5250 1.9156 -0.0411 0.2616  -0.0729 16  LEU D C   
12868 O O   . LEU D 16  ? 0.4349 0.5206 1.9138 -0.0463 0.2667  -0.0636 16  LEU D O   
12869 C CB  . LEU D 16  ? 0.4055 0.4758 1.8610 -0.0375 0.2226  -0.0602 16  LEU D CB  
12870 C CG  . LEU D 16  ? 0.3813 0.4466 1.8357 -0.0322 0.2035  -0.0619 16  LEU D CG  
12871 C CD1 . LEU D 16  ? 0.3478 0.4215 1.8397 -0.0244 0.1957  -0.0655 16  LEU D CD1 
12872 C CD2 . LEU D 16  ? 0.3829 0.4411 1.8172 -0.0361 0.1891  -0.0491 16  LEU D CD2 
12873 N N   . ASP D 17  ? 0.4741 0.5524 1.9322 -0.0414 0.2760  -0.0844 17  ASP D N   
12874 C CA  . ASP D 17  ? 0.5147 0.5936 1.9624 -0.0482 0.3003  -0.0863 17  ASP D CA  
12875 C C   . ASP D 17  ? 0.5107 0.6056 2.0002 -0.0492 0.3106  -0.0843 17  ASP D C   
12876 O O   . ASP D 17  ? 0.5169 0.6112 1.9984 -0.0573 0.3238  -0.0766 17  ASP D O   
12877 C CB  . ASP D 17  ? 0.5402 0.6028 1.9368 -0.0569 0.3011  -0.0759 17  ASP D CB  
12878 C CG  . ASP D 17  ? 0.5590 0.6068 1.9161 -0.0561 0.2927  -0.0810 17  ASP D CG  
12879 O OD1 . ASP D 17  ? 0.5593 0.6056 1.9120 -0.0537 0.3033  -0.0953 17  ASP D OD1 
12880 O OD2 . ASP D 17  ? 0.5802 0.6181 1.9126 -0.0579 0.2751  -0.0710 17  ASP D OD2 
12881 N N   . GLY D 18  ? 0.5025 0.6107 2.0365 -0.0409 0.3040  -0.0915 18  GLY D N   
12882 C CA  . GLY D 18  ? 0.5066 0.6319 2.0858 -0.0403 0.3156  -0.0953 18  GLY D CA  
12883 C C   . GLY D 18  ? 0.5045 0.6348 2.1005 -0.0434 0.3059  -0.0821 18  GLY D C   
12884 O O   . GLY D 18  ? 0.5192 0.6629 2.1501 -0.0453 0.3163  -0.0835 18  GLY D O   
12885 N N   . GLU D 19  ? 0.4860 0.6058 2.0588 -0.0439 0.2866  -0.0704 19  GLU D N   
12886 C CA  . GLU D 19  ? 0.4674 0.5892 2.0511 -0.0469 0.2763  -0.0576 19  GLU D CA  
12887 C C   . GLU D 19  ? 0.4306 0.5527 2.0270 -0.0388 0.2520  -0.0564 19  GLU D C   
12888 O O   . GLU D 19  ? 0.4608 0.5727 2.0326 -0.0360 0.2402  -0.0561 19  GLU D O   
12889 C CB  . GLU D 19  ? 0.4937 0.6011 2.0367 -0.0552 0.2751  -0.0433 19  GLU D CB  
12890 C CG  . GLU D 19  ? 0.5498 0.6511 2.0672 -0.0642 0.2984  -0.0422 19  GLU D CG  
12891 C CD  . GLU D 19  ? 0.5911 0.7043 2.1401 -0.0694 0.3171  -0.0427 19  GLU D CD  
12892 O OE1 . GLU D 19  ? 0.5817 0.7054 2.1670 -0.0677 0.3091  -0.0397 19  GLU D OE1 
12893 O OE2 . GLU D 19  ? 0.6586 0.7706 2.1965 -0.0751 0.3404  -0.0471 19  GLU D OE2 
12894 N N   . LYS D 20  ? 0.3918 0.5250 2.0262 -0.0355 0.2451  -0.0562 20  LYS D N   
12895 C CA  . LYS D 20  ? 0.3724 0.5048 2.0178 -0.0283 0.2231  -0.0548 20  LYS D CA  
12896 C C   . LYS D 20  ? 0.3762 0.4960 1.9903 -0.0314 0.2099  -0.0426 20  LYS D C   
12897 O O   . LYS D 20  ? 0.4196 0.5365 2.0235 -0.0383 0.2131  -0.0325 20  LYS D O   
12898 C CB  . LYS D 20  ? 0.3527 0.4973 2.0391 -0.0259 0.2178  -0.0549 20  LYS D CB  
12899 C CG  . LYS D 20  ? 0.3429 0.5007 2.0684 -0.0192 0.2215  -0.0679 20  LYS D CG  
12900 C CD  . LYS D 20  ? 0.3200 0.4870 2.0810 -0.0164 0.2098  -0.0667 20  LYS D CD  
12901 C CE  . LYS D 20  ? 0.3054 0.4853 2.1077 -0.0087 0.2085  -0.0788 20  LYS D CE  
12902 N NZ  . LYS D 20  ? 0.3204 0.5121 2.1419 -0.0127 0.2309  -0.0863 20  LYS D NZ  
12903 N N   . TYR D 21  ? 0.3527 0.4650 1.9539 -0.0261 0.1953  -0.0437 21  TYR D N   
12904 C CA  . TYR D 21  ? 0.3417 0.4425 1.9134 -0.0287 0.1838  -0.0345 21  TYR D CA  
12905 C C   . TYR D 21  ? 0.3206 0.4201 1.9033 -0.0226 0.1655  -0.0335 21  TYR D C   
12906 O O   . TYR D 21  ? 0.3054 0.4036 1.8936 -0.0163 0.1603  -0.0412 21  TYR D O   
12907 C CB  . TYR D 21  ? 0.3519 0.4432 1.8903 -0.0303 0.1879  -0.0381 21  TYR D CB  
12908 C CG  . TYR D 21  ? 0.3508 0.4303 1.8564 -0.0337 0.1774  -0.0297 21  TYR D CG  
12909 C CD1 . TYR D 21  ? 0.3342 0.4087 1.8358 -0.0298 0.1616  -0.0298 21  TYR D CD1 
12910 C CD2 . TYR D 21  ? 0.3653 0.4378 1.8428 -0.0409 0.1837  -0.0224 21  TYR D CD2 
12911 C CE1 . TYR D 21  ? 0.3395 0.4049 1.8150 -0.0328 0.1519  -0.0235 21  TYR D CE1 
12912 C CE2 . TYR D 21  ? 0.3709 0.4327 1.8195 -0.0433 0.1725  -0.0156 21  TYR D CE2 
12913 C CZ  . TYR D 21  ? 0.3525 0.4119 1.8022 -0.0392 0.1563  -0.0164 21  TYR D CZ  
12914 O OH  . TYR D 21  ? 0.3487 0.3994 1.7747 -0.0415 0.1448  -0.0103 21  TYR D OH  
12915 N N   . PHE D 22  ? 0.3079 0.4066 1.8939 -0.0245 0.1569  -0.0242 22  PHE D N   
12916 C CA  . PHE D 22  ? 0.2855 0.3815 1.8783 -0.0199 0.1410  -0.0224 22  PHE D CA  
12917 C C   . PHE D 22  ? 0.2909 0.3767 1.8561 -0.0210 0.1329  -0.0186 22  PHE D C   
12918 O O   . PHE D 22  ? 0.2987 0.3803 1.8461 -0.0263 0.1333  -0.0110 22  PHE D O   
12919 C CB  . PHE D 22  ? 0.2712 0.3707 1.8799 -0.0215 0.1361  -0.0152 22  PHE D CB  
12920 C CG  . PHE D 22  ? 0.2513 0.3491 1.8714 -0.0160 0.1218  -0.0158 22  PHE D CG  
12921 C CD1 . PHE D 22  ? 0.2549 0.3442 1.8586 -0.0151 0.1116  -0.0122 22  PHE D CD1 
12922 C CD2 . PHE D 22  ? 0.2428 0.3471 1.8897 -0.0118 0.1185  -0.0202 22  PHE D CD2 
12923 C CE1 . PHE D 22  ? 0.2456 0.3320 1.8572 -0.0106 0.1005  -0.0128 22  PHE D CE1 
12924 C CE2 . PHE D 22  ? 0.2316 0.3319 1.8841 -0.0069 0.1055  -0.0206 22  PHE D CE2 
12925 C CZ  . PHE D 22  ? 0.2308 0.3218 1.8647 -0.0066 0.0974  -0.0167 22  PHE D CZ  
12926 N N   . ILE D 23  ? 0.2908 0.3721 1.8534 -0.0163 0.1255  -0.0240 23  ILE D N   
12927 C CA  . ILE D 23  ? 0.2969 0.3695 1.8369 -0.0176 0.1185  -0.0224 23  ILE D CA  
12928 C C   . ILE D 23  ? 0.2836 0.3542 1.8261 -0.0180 0.1074  -0.0145 23  ILE D C   
12929 O O   . ILE D 23  ? 0.2537 0.3240 1.8097 -0.0139 0.1007  -0.0158 23  ILE D O   
12930 C CB  . ILE D 23  ? 0.3013 0.3689 1.8390 -0.0131 0.1161  -0.0313 23  ILE D CB  
12931 C CG1 . ILE D 23  ? 0.3082 0.3787 1.8498 -0.0112 0.1278  -0.0407 23  ILE D CG1 
12932 C CG2 . ILE D 23  ? 0.2933 0.3525 1.8092 -0.0155 0.1094  -0.0304 23  ILE D CG2 
12933 C CD1 . ILE D 23  ? 0.3029 0.3675 1.8451 -0.0060 0.1253  -0.0498 23  ILE D CD1 
12934 N N   . LYS D 24  ? 0.3132 0.3817 1.8425 -0.0229 0.1060  -0.0066 24  LYS D N   
12935 C CA  . LYS D 24  ? 0.3377 0.4044 1.8694 -0.0235 0.0962  0.0007  24  LYS D CA  
12936 C C   . LYS D 24  ? 0.3535 0.4142 1.8693 -0.0244 0.0882  0.0009  24  LYS D C   
12937 O O   . LYS D 24  ? 0.3786 0.4364 1.8791 -0.0281 0.0858  0.0060  24  LYS D O   
12938 C CB  . LYS D 24  ? 0.3526 0.4204 1.8832 -0.0278 0.0986  0.0096  24  LYS D CB  
12939 C CG  . LYS D 24  ? 0.3559 0.4301 1.9070 -0.0278 0.1051  0.0102  24  LYS D CG  
12940 C CD  . LYS D 24  ? 0.3897 0.4626 1.9402 -0.0324 0.1062  0.0200  24  LYS D CD  
12941 C CE  . LYS D 24  ? 0.4412 0.5080 1.9663 -0.0375 0.1106  0.0256  24  LYS D CE  
12942 N NZ  . LYS D 24  ? 0.4639 0.5284 1.9892 -0.0422 0.1147  0.0350  24  LYS D NZ  
12943 N N   . ALA D 25  ? 0.3415 0.3997 1.8612 -0.0211 0.0840  -0.0048 25  ALA D N   
12944 C CA  . ALA D 25  ? 0.3487 0.4018 1.8556 -0.0223 0.0785  -0.0073 25  ALA D CA  
12945 C C   . ALA D 25  ? 0.3438 0.3957 1.8577 -0.0222 0.0696  -0.0035 25  ALA D C   
12946 O O   . ALA D 25  ? 0.3635 0.4178 1.8906 -0.0207 0.0682  0.0002  25  ALA D O   
12947 C CB  . ALA D 25  ? 0.3575 0.4071 1.8642 -0.0195 0.0810  -0.0162 25  ALA D CB  
12948 N N   . ILE D 26  ? 0.3368 0.3853 1.8430 -0.0239 0.0640  -0.0055 26  ILE D N   
12949 C CA  . ILE D 26  ? 0.3341 0.3819 1.8496 -0.0239 0.0574  -0.0043 26  ILE D CA  
12950 C C   . ILE D 26  ? 0.3427 0.3859 1.8527 -0.0251 0.0551  -0.0108 26  ILE D C   
12951 O O   . ILE D 26  ? 0.4033 0.4448 1.8998 -0.0274 0.0544  -0.0138 26  ILE D O   
12952 C CB  . ILE D 26  ? 0.3444 0.3950 1.8614 -0.0260 0.0506  0.0027  26  ILE D CB  
12953 C CG1 . ILE D 26  ? 0.3575 0.4084 1.8880 -0.0256 0.0457  0.0026  26  ILE D CG1 
12954 C CG2 . ILE D 26  ? 0.3522 0.4015 1.8526 -0.0293 0.0463  0.0033  26  ILE D CG2 
12955 C CD1 . ILE D 26  ? 0.3639 0.4183 1.9025 -0.0262 0.0395  0.0092  26  ILE D CD1 
12956 N N   . GLY D 27  ? 0.3181 0.3580 1.8373 -0.0241 0.0543  -0.0130 27  GLY D N   
12957 C CA  . GLY D 27  ? 0.2930 0.3278 1.8097 -0.0261 0.0525  -0.0187 27  GLY D CA  
12958 C C   . GLY D 27  ? 0.2594 0.2976 1.7768 -0.0302 0.0450  -0.0177 27  GLY D C   
12959 O O   . GLY D 27  ? 0.2278 0.2708 1.7551 -0.0304 0.0413  -0.0126 27  GLY D O   
12960 N N   . TYR D 28  ? 0.2480 0.2834 1.7559 -0.0329 0.0425  -0.0232 28  TYR D N   
12961 C CA  . TYR D 28  ? 0.2415 0.2796 1.7472 -0.0367 0.0336  -0.0239 28  TYR D CA  
12962 C C   . TYR D 28  ? 0.2538 0.2870 1.7590 -0.0399 0.0317  -0.0322 28  TYR D C   
12963 O O   . TYR D 28  ? 0.2771 0.3048 1.7689 -0.0405 0.0338  -0.0380 28  TYR D O   
12964 C CB  . TYR D 28  ? 0.2420 0.2807 1.7291 -0.0373 0.0311  -0.0218 28  TYR D CB  
12965 C CG  . TYR D 28  ? 0.2432 0.2831 1.7238 -0.0406 0.0197  -0.0221 28  TYR D CG  
12966 C CD1 . TYR D 28  ? 0.2379 0.2834 1.7339 -0.0413 0.0109  -0.0183 28  TYR D CD1 
12967 C CD2 . TYR D 28  ? 0.2564 0.2916 1.7155 -0.0428 0.0170  -0.0266 28  TYR D CD2 
12968 C CE1 . TYR D 28  ? 0.2510 0.2980 1.7432 -0.0437 -0.0017 -0.0188 28  TYR D CE1 
12969 C CE2 . TYR D 28  ? 0.2727 0.3081 1.7240 -0.0455 0.0045  -0.0269 28  TYR D CE2 
12970 C CZ  . TYR D 28  ? 0.2700 0.3115 1.7389 -0.0459 -0.0058 -0.0230 28  TYR D CZ  
12971 O OH  . TYR D 28  ? 0.2817 0.3239 1.7460 -0.0481 -0.0204 -0.0235 28  TYR D OH  
12972 N N   . GLU D 29  ? 0.2519 0.2873 1.7731 -0.0425 0.0280  -0.0332 29  GLU D N   
12973 C CA  . GLU D 29  ? 0.2602 0.2926 1.7849 -0.0469 0.0245  -0.0408 29  GLU D CA  
12974 C C   . GLU D 29  ? 0.2679 0.3076 1.7984 -0.0500 0.0123  -0.0409 29  GLU D C   
12975 O O   . GLU D 29  ? 0.2596 0.3064 1.8081 -0.0502 0.0089  -0.0373 29  GLU D O   
12976 C CB  . GLU D 29  ? 0.2495 0.2789 1.7909 -0.0480 0.0308  -0.0416 29  GLU D CB  
12977 C CG  . GLU D 29  ? 0.2554 0.2819 1.8068 -0.0536 0.0290  -0.0487 29  GLU D CG  
12978 C CD  . GLU D 29  ? 0.2657 0.2820 1.8209 -0.0538 0.0395  -0.0497 29  GLU D CD  
12979 O OE1 . GLU D 29  ? 0.2453 0.2642 1.8125 -0.0533 0.0434  -0.0454 29  GLU D OE1 
12980 O OE2 . GLU D 29  ? 0.2965 0.3013 1.8414 -0.0539 0.0436  -0.0543 29  GLU D OE2 
12981 N N   . ILE D 30  ? 0.2855 0.3231 1.7999 -0.0520 0.0052  -0.0453 30  ILE D N   
12982 C CA  . ILE D 30  ? 0.2923 0.3343 1.8110 -0.0555 -0.0084 -0.0481 30  ILE D CA  
12983 C C   . ILE D 30  ? 0.2954 0.3371 1.8339 -0.0600 -0.0078 -0.0558 30  ILE D C   
12984 O O   . ILE D 30  ? 0.2826 0.3183 1.8250 -0.0600 0.0033  -0.0575 30  ILE D O   
12985 C CB  . ILE D 30  ? 0.3101 0.3471 1.8012 -0.0564 -0.0152 -0.0513 30  ILE D CB  
12986 C CG1 . ILE D 30  ? 0.3256 0.3664 1.8172 -0.0592 -0.0322 -0.0532 30  ILE D CG1 
12987 C CG2 . ILE D 30  ? 0.3213 0.3488 1.8002 -0.0580 -0.0083 -0.0606 30  ILE D CG2 
12988 C CD1 . ILE D 30  ? 0.3220 0.3711 1.8250 -0.0569 -0.0412 -0.0442 30  ILE D CD1 
12989 N N   . GLY D 31  ? 0.3096 0.3575 1.8626 -0.0637 -0.0197 -0.0595 31  GLY D N   
12990 C CA  . GLY D 31  ? 0.3130 0.3613 1.8871 -0.0690 -0.0191 -0.0673 31  GLY D CA  
12991 C C   . GLY D 31  ? 0.3103 0.3629 1.9108 -0.0695 -0.0096 -0.0644 31  GLY D C   
12992 O O   . GLY D 31  ? 0.3388 0.3883 1.9536 -0.0742 -0.0037 -0.0700 31  GLY D O   
12993 N N   . ALA D 32  ? 0.3087 0.3677 1.9161 -0.0653 -0.0081 -0.0563 32  ALA D N   
12994 C CA  . ALA D 32  ? 0.3034 0.3643 1.9312 -0.0655 0.0028  -0.0541 32  ALA D CA  
12995 C C   . ALA D 32  ? 0.3166 0.3899 1.9656 -0.0634 -0.0029 -0.0497 32  ALA D C   
12996 O O   . ALA D 32  ? 0.3518 0.4261 2.0083 -0.0607 0.0056  -0.0450 32  ALA D O   
12997 C CB  . ALA D 32  ? 0.2924 0.3441 1.9041 -0.0616 0.0154  -0.0493 32  ALA D CB  
12998 N N   . ARG D 33  ? 0.3203 0.4023 1.9797 -0.0644 -0.0179 -0.0517 33  ARG D N   
12999 C CA  . ARG D 33  ? 0.2980 0.3916 1.9820 -0.0621 -0.0239 -0.0484 33  ARG D CA  
13000 C C   . ARG D 33  ? 0.2839 0.3829 1.9999 -0.0663 -0.0148 -0.0538 33  ARG D C   
13001 O O   . ARG D 33  ? 0.2812 0.3739 1.9975 -0.0715 -0.0057 -0.0595 33  ARG D O   
13002 C CB  . ARG D 33  ? 0.3265 0.4270 2.0133 -0.0615 -0.0442 -0.0490 33  ARG D CB  
13003 C CG  . ARG D 33  ? 0.3477 0.4421 2.0017 -0.0577 -0.0536 -0.0428 33  ARG D CG  
13004 C CD  . ARG D 33  ? 0.3523 0.4425 1.9918 -0.0525 -0.0446 -0.0332 33  ARG D CD  
13005 N NE  . ARG D 33  ? 0.3783 0.4646 1.9932 -0.0491 -0.0542 -0.0258 33  ARG D NE  
13006 C CZ  . ARG D 33  ? 0.3693 0.4462 1.9516 -0.0485 -0.0503 -0.0232 33  ARG D CZ  
13007 N NH1 . ARG D 33  ? 0.3682 0.4388 1.9374 -0.0511 -0.0413 -0.0292 33  ARG D NH1 
13008 N NH2 . ARG D 33  ? 0.3803 0.4537 1.9437 -0.0455 -0.0558 -0.0149 33  ARG D NH2 
13009 N N   . PRO D 34  ? 0.2648 0.3749 2.0090 -0.0645 -0.0164 -0.0524 34  PRO D N   
13010 C CA  . PRO D 34  ? 0.2385 0.3567 2.0183 -0.0692 -0.0098 -0.0592 34  PRO D CA  
13011 C C   . PRO D 34  ? 0.2454 0.3684 2.0395 -0.0754 -0.0198 -0.0681 34  PRO D C   
13012 O O   . PRO D 34  ? 0.2358 0.3643 2.0300 -0.0740 -0.0384 -0.0690 34  PRO D O   
13013 C CB  . PRO D 34  ? 0.2354 0.3653 2.0394 -0.0643 -0.0146 -0.0558 34  PRO D CB  
13014 C CG  . PRO D 34  ? 0.2312 0.3540 2.0081 -0.0575 -0.0139 -0.0460 34  PRO D CG  
13015 C CD  . PRO D 34  ? 0.2549 0.3694 1.9989 -0.0577 -0.0228 -0.0445 34  PRO D CD  
13016 N N   . GLY D 35  ? 0.2583 0.3768 2.0609 -0.0824 -0.0076 -0.0745 35  GLY D N   
13017 C CA  . GLY D 35  ? 0.2741 0.3954 2.0911 -0.0895 -0.0147 -0.0839 35  GLY D CA  
13018 C C   . GLY D 35  ? 0.2897 0.3956 2.0765 -0.0928 -0.0119 -0.0864 35  GLY D C   
13019 O O   . GLY D 35  ? 0.3001 0.4049 2.0988 -0.0999 -0.0127 -0.0948 35  GLY D O   
13020 N N   . GLN D 36  ? 0.2954 0.3896 2.0456 -0.0876 -0.0086 -0.0797 36  GLN D N   
13021 C CA  . GLN D 36  ? 0.3129 0.3937 2.0333 -0.0888 -0.0094 -0.0822 36  GLN D CA  
13022 C C   . GLN D 36  ? 0.3095 0.3750 2.0140 -0.0895 0.0090  -0.0802 36  GLN D C   
13023 O O   . GLN D 36  ? 0.3167 0.3797 2.0183 -0.0860 0.0200  -0.0736 36  GLN D O   
13024 C CB  . GLN D 36  ? 0.3212 0.3993 2.0103 -0.0823 -0.0191 -0.0767 36  GLN D CB  
13025 C CG  . GLN D 36  ? 0.3255 0.4146 2.0203 -0.0803 -0.0389 -0.0765 36  GLN D CG  
13026 C CD  . GLN D 36  ? 0.3468 0.4294 2.0056 -0.0758 -0.0474 -0.0723 36  GLN D CD  
13027 O OE1 . GLN D 36  ? 0.3670 0.4450 2.0064 -0.0707 -0.0403 -0.0642 36  GLN D OE1 
13028 N NE2 . GLN D 36  ? 0.3589 0.4405 2.0077 -0.0781 -0.0621 -0.0781 36  GLN D NE2 
13029 N N   . ALA D 37  ? 0.3151 0.3688 2.0069 -0.0934 0.0110  -0.0858 37  ALA D N   
13030 C CA  . ALA D 37  ? 0.3098 0.3467 1.9829 -0.0929 0.0255  -0.0836 37  ALA D CA  
13031 C C   . ALA D 37  ? 0.3200 0.3467 1.9654 -0.0910 0.0204  -0.0866 37  ALA D C   
13032 O O   . ALA D 37  ? 0.3276 0.3518 1.9748 -0.0959 0.0140  -0.0950 37  ALA D O   
13033 C CB  . ALA D 37  ? 0.3169 0.3468 2.0076 -0.1006 0.0374  -0.0877 37  ALA D CB  
13034 N N   . PRO D 38  ? 0.3156 0.3371 1.9360 -0.0839 0.0228  -0.0807 38  PRO D N   
13035 C CA  . PRO D 38  ? 0.3319 0.3473 1.9276 -0.0815 0.0170  -0.0839 38  PRO D CA  
13036 C C   . PRO D 38  ? 0.3509 0.3506 1.9392 -0.0846 0.0235  -0.0905 38  PRO D C   
13037 O O   . PRO D 38  ? 0.3721 0.3677 1.9494 -0.0861 0.0169  -0.0978 38  PRO D O   
13038 C CB  . PRO D 38  ? 0.3192 0.3346 1.8963 -0.0736 0.0202  -0.0758 38  PRO D CB  
13039 C CG  . PRO D 38  ? 0.3098 0.3242 1.8977 -0.0721 0.0311  -0.0693 38  PRO D CG  
13040 C CD  . PRO D 38  ? 0.3037 0.3252 1.9194 -0.0782 0.0310  -0.0716 38  PRO D CD  
13041 N N   . TYR D 39  ? 0.3569 0.3463 1.9505 -0.0859 0.0358  -0.0883 39  TYR D N   
13042 C CA  . TYR D 39  ? 0.3803 0.3523 1.9663 -0.0884 0.0416  -0.0936 39  TYR D CA  
13043 C C   . TYR D 39  ? 0.3990 0.3702 2.0048 -0.0980 0.0394  -0.1020 39  TYR D C   
13044 O O   . TYR D 39  ? 0.4020 0.3609 2.0019 -0.1010 0.0394  -0.1092 39  TYR D O   
13045 C CB  . TYR D 39  ? 0.3817 0.3399 1.9596 -0.0848 0.0544  -0.0869 39  TYR D CB  
13046 C CG  . TYR D 39  ? 0.4024 0.3611 1.9617 -0.0754 0.0549  -0.0809 39  TYR D CG  
13047 C CD1 . TYR D 39  ? 0.4265 0.3839 1.9690 -0.0711 0.0504  -0.0846 39  TYR D CD1 
13048 C CD2 . TYR D 39  ? 0.4087 0.3698 1.9682 -0.0712 0.0602  -0.0721 39  TYR D CD2 
13049 C CE1 . TYR D 39  ? 0.4302 0.3891 1.9592 -0.0632 0.0521  -0.0796 39  TYR D CE1 
13050 C CE2 . TYR D 39  ? 0.4139 0.3761 1.9595 -0.0632 0.0604  -0.0672 39  TYR D CE2 
13051 C CZ  . TYR D 39  ? 0.4284 0.3902 1.9601 -0.0594 0.0565  -0.0708 39  TYR D CZ  
13052 O OH  . TYR D 39  ? 0.4300 0.3949 1.9519 -0.0522 0.0575  -0.0661 39  TYR D OH  
13053 N N   . GLU D 40  ? 0.4067 0.3914 2.0378 -0.1027 0.0370  -0.1018 40  GLU D N   
13054 C CA  . GLU D 40  ? 0.4193 0.4052 2.0754 -0.1124 0.0364  -0.1096 40  GLU D CA  
13055 C C   . GLU D 40  ? 0.4153 0.4136 2.0796 -0.1151 0.0193  -0.1180 40  GLU D C   
13056 O O   . GLU D 40  ? 0.4361 0.4295 2.1088 -0.1220 0.0156  -0.1275 40  GLU D O   
13057 C CB  . GLU D 40  ? 0.4410 0.4350 2.1244 -0.1167 0.0446  -0.1063 40  GLU D CB  
13058 C CG  . GLU D 40  ? 0.4793 0.4634 2.1525 -0.1130 0.0600  -0.0967 40  GLU D CG  
13059 C CD  . GLU D 40  ? 0.5448 0.5048 2.1990 -0.1135 0.0711  -0.0952 40  GLU D CD  
13060 O OE1 . GLU D 40  ? 0.6032 0.5542 2.2376 -0.1098 0.0662  -0.0977 40  GLU D OE1 
13061 O OE2 . GLU D 40  ? 0.5711 0.5202 2.2286 -0.1169 0.0849  -0.0912 40  GLU D OE2 
13062 N N   . ASP D 41  ? 0.4070 0.4199 2.0686 -0.1100 0.0082  -0.1146 41  ASP D N   
13063 C CA  . ASP D 41  ? 0.4310 0.4558 2.1008 -0.1123 -0.0099 -0.1214 41  ASP D CA  
13064 C C   . ASP D 41  ? 0.4660 0.4806 2.1091 -0.1119 -0.0179 -0.1287 41  ASP D C   
13065 O O   . ASP D 41  ? 0.4926 0.4951 2.1095 -0.1072 -0.0103 -0.1261 41  ASP D O   
13066 C CB  . ASP D 41  ? 0.4142 0.4538 2.0830 -0.1061 -0.0199 -0.1144 41  ASP D CB  
13067 C CG  . ASP D 41  ? 0.3856 0.4384 2.0832 -0.1057 -0.0159 -0.1086 41  ASP D CG  
13068 O OD1 . ASP D 41  ? 0.3787 0.4298 2.0976 -0.1108 -0.0032 -0.1098 41  ASP D OD1 
13069 O OD2 . ASP D 41  ? 0.3596 0.4233 2.0571 -0.1004 -0.0247 -0.1030 41  ASP D OD2 
13070 N N   . GLU D 42  ? 0.5053 0.5251 2.1550 -0.1164 -0.0337 -0.1381 42  GLU D N   
13071 C CA  . GLU D 42  ? 0.5749 0.5880 2.1950 -0.1146 -0.0446 -0.1442 42  GLU D CA  
13072 C C   . GLU D 42  ? 0.6044 0.6201 2.1969 -0.1058 -0.0463 -0.1349 42  GLU D C   
13073 O O   . GLU D 42  ? 0.6358 0.6644 2.2377 -0.1029 -0.0524 -0.1276 42  GLU D O   
13074 C CB  . GLU D 42  ? 0.6522 0.6737 2.2827 -0.1195 -0.0651 -0.1538 42  GLU D CB  
13075 C CG  . GLU D 42  ? 0.7287 0.7413 2.3242 -0.1180 -0.0764 -0.1609 42  GLU D CG  
13076 C CD  . GLU D 42  ? 0.7835 0.8031 2.3825 -0.1216 -0.0997 -0.1696 42  GLU D CD  
13077 O OE1 . GLU D 42  ? 0.7937 0.8274 2.4276 -0.1252 -0.1086 -0.1706 42  GLU D OE1 
13078 O OE2 . GLU D 42  ? 0.8299 0.8406 2.3969 -0.1208 -0.1091 -0.1759 42  GLU D OE2 
13079 N N   . ARG D 43  ? 0.6257 0.6293 2.1863 -0.1017 -0.0405 -0.1352 43  ARG D N   
13080 C CA  . ARG D 43  ? 0.6141 0.6193 2.1493 -0.0941 -0.0397 -0.1266 43  ARG D CA  
13081 C C   . ARG D 43  ? 0.6206 0.6315 2.1411 -0.0938 -0.0579 -0.1282 43  ARG D C   
13082 O O   . ARG D 43  ? 0.6242 0.6313 2.1386 -0.0982 -0.0691 -0.1388 43  ARG D O   
13083 C CB  . ARG D 43  ? 0.6564 0.6477 2.1646 -0.0902 -0.0279 -0.1281 43  ARG D CB  
13084 C CG  . ARG D 43  ? 0.7067 0.6884 2.1891 -0.0916 -0.0343 -0.1390 43  ARG D CG  
13085 C CD  . ARG D 43  ? 0.7466 0.7159 2.2075 -0.0869 -0.0205 -0.1405 43  ARG D CD  
13086 N NE  . ARG D 43  ? 0.8086 0.7661 2.2508 -0.0894 -0.0236 -0.1539 43  ARG D NE  
13087 C CZ  . ARG D 43  ? 0.8271 0.7717 2.2554 -0.0867 -0.0129 -0.1599 43  ARG D CZ  
13088 N NH1 . ARG D 43  ? 0.8250 0.7665 2.2568 -0.0812 0.0012  -0.1535 43  ARG D NH1 
13089 N NH2 . ARG D 43  ? 0.8412 0.7756 2.2523 -0.0893 -0.0170 -0.1729 43  ARG D NH2 
13090 N N   . LYS D 44  ? 0.6129 0.6318 2.1271 -0.0888 -0.0613 -0.1176 44  LYS D N   
13091 C CA  . LYS D 44  ? 0.6262 0.6471 2.1192 -0.0874 -0.0775 -0.1166 44  LYS D CA  
13092 C C   . LYS D 44  ? 0.5761 0.5944 2.0422 -0.0810 -0.0699 -0.1062 44  LYS D C   
13093 O O   . LYS D 44  ? 0.5252 0.5466 2.0008 -0.0774 -0.0574 -0.0977 44  LYS D O   
13094 C CB  . LYS D 44  ? 0.6618 0.6963 2.1789 -0.0882 -0.0940 -0.1134 44  LYS D CB  
13095 C CG  . LYS D 44  ? 0.7361 0.7747 2.2745 -0.0947 -0.1090 -0.1248 44  LYS D CG  
13096 C CD  . LYS D 44  ? 0.8117 0.8565 2.3914 -0.0996 -0.1005 -0.1289 44  LYS D CD  
13097 C CE  . LYS D 44  ? 0.8535 0.9115 2.4633 -0.0970 -0.0959 -0.1194 44  LYS D CE  
13098 N NZ  . LYS D 44  ? 0.8546 0.9169 2.5009 -0.1025 -0.0853 -0.1235 44  LYS D NZ  
13099 N N   . ASP D 45  ? 0.5669 0.5788 1.9992 -0.0801 -0.0781 -0.1071 45  ASP D N   
13100 C CA  . ASP D 45  ? 0.5512 0.5594 1.9555 -0.0752 -0.0709 -0.0981 45  ASP D CA  
13101 C C   . ASP D 45  ? 0.5494 0.5676 1.9672 -0.0717 -0.0745 -0.0847 45  ASP D C   
13102 O O   . ASP D 45  ? 0.5115 0.5302 1.9250 -0.0677 -0.0625 -0.0757 45  ASP D O   
13103 C CB  . ASP D 45  ? 0.5631 0.5613 1.9276 -0.0762 -0.0797 -0.1024 45  ASP D CB  
13104 C CG  . ASP D 45  ? 0.5596 0.5456 1.9035 -0.0784 -0.0722 -0.1151 45  ASP D CG  
13105 O OD1 . ASP D 45  ? 0.5345 0.5192 1.8943 -0.0783 -0.0584 -0.1194 45  ASP D OD1 
13106 O OD2 . ASP D 45  ? 0.5738 0.5508 1.8850 -0.0799 -0.0804 -0.1206 45  ASP D OD2 
13107 N N   . GLU D 46  ? 0.5768 0.6026 2.0114 -0.0731 -0.0921 -0.0839 46  GLU D N   
13108 C CA  . GLU D 46  ? 0.5876 0.6235 2.0415 -0.0697 -0.0966 -0.0727 46  GLU D CA  
13109 C C   . GLU D 46  ? 0.5794 0.6099 2.0044 -0.0654 -0.0930 -0.0613 46  GLU D C   
13110 O O   . GLU D 46  ? 0.5698 0.6042 2.0048 -0.0620 -0.0818 -0.0526 46  GLU D O   
13111 C CB  . GLU D 46  ? 0.5712 0.6148 2.0598 -0.0693 -0.0826 -0.0714 46  GLU D CB  
13112 C CG  . GLU D 46  ? 0.5566 0.6130 2.0792 -0.0680 -0.0899 -0.0659 46  GLU D CG  
13113 C CD  . GLU D 46  ? 0.5256 0.5883 2.0830 -0.0705 -0.0790 -0.0702 46  GLU D CD  
13114 O OE1 . GLU D 46  ? 0.5372 0.5930 2.0906 -0.0736 -0.0690 -0.0773 46  GLU D OE1 
13115 O OE2 . GLU D 46  ? 0.5098 0.5827 2.0971 -0.0696 -0.0800 -0.0667 46  GLU D OE2 
13116 N N   . LEU D 47  ? 0.5961 0.6169 1.9847 -0.0659 -0.1022 -0.0617 47  LEU D N   
13117 C CA  . LEU D 47  ? 0.5875 0.6005 1.9436 -0.0632 -0.0971 -0.0518 47  LEU D CA  
13118 C C   . LEU D 47  ? 0.5869 0.6058 1.9561 -0.0595 -0.1044 -0.0385 47  LEU D C   
13119 O O   . LEU D 47  ? 0.5423 0.5608 1.9079 -0.0568 -0.0923 -0.0290 47  LEU D O   
13120 C CB  . LEU D 47  ? 0.6135 0.6134 1.9267 -0.0654 -0.1068 -0.0559 47  LEU D CB  
13121 C CG  . LEU D 47  ? 0.6191 0.6110 1.9151 -0.0688 -0.0992 -0.0699 47  LEU D CG  
13122 C CD1 . LEU D 47  ? 0.6636 0.6403 1.9091 -0.0701 -0.1024 -0.0713 47  LEU D CD1 
13123 C CD2 . LEU D 47  ? 0.5876 0.5811 1.8950 -0.0677 -0.0760 -0.0725 47  LEU D CD2 
13124 N N   . GLU D 48  ? 0.6162 0.6410 2.0031 -0.0594 -0.1246 -0.0385 48  GLU D N   
13125 C CA  . GLU D 48  ? 0.6240 0.6521 2.0200 -0.0555 -0.1354 -0.0264 48  GLU D CA  
13126 C C   . GLU D 48  ? 0.5539 0.5903 1.9769 -0.0524 -0.1199 -0.0191 48  GLU D C   
13127 O O   . GLU D 48  ? 0.5414 0.5741 1.9542 -0.0494 -0.1171 -0.0076 48  GLU D O   
13128 C CB  . GLU D 48  ? 0.6761 0.7119 2.0963 -0.0553 -0.1592 -0.0295 48  GLU D CB  
13129 C CG  . GLU D 48  ? 0.7670 0.7920 2.1537 -0.0565 -0.1805 -0.0313 48  GLU D CG  
13130 C CD  . GLU D 48  ? 0.8508 0.8609 2.1945 -0.0540 -0.1844 -0.0187 48  GLU D CD  
13131 O OE1 . GLU D 48  ? 0.9090 0.9186 2.2541 -0.0509 -0.1740 -0.0068 48  GLU D OE1 
13132 O OE2 . GLU D 48  ? 0.9120 0.9094 2.2182 -0.0558 -0.1976 -0.0210 48  GLU D OE2 
13133 N N   . LEU D 49  ? 0.5015 0.5473 1.9567 -0.0536 -0.1098 -0.0259 49  LEU D N   
13134 C CA  . LEU D 49  ? 0.4626 0.5155 1.9428 -0.0508 -0.0961 -0.0204 49  LEU D CA  
13135 C C   . LEU D 49  ? 0.4595 0.5050 1.9165 -0.0499 -0.0779 -0.0160 49  LEU D C   
13136 O O   . LEU D 49  ? 0.4417 0.4886 1.9040 -0.0468 -0.0711 -0.0070 49  LEU D O   
13137 C CB  . LEU D 49  ? 0.4377 0.5006 1.9552 -0.0526 -0.0895 -0.0281 49  LEU D CB  
13138 C CG  . LEU D 49  ? 0.4476 0.5215 1.9995 -0.0529 -0.1045 -0.0309 49  LEU D CG  
13139 C CD1 . LEU D 49  ? 0.4724 0.5453 2.0189 -0.0565 -0.1215 -0.0398 49  LEU D CD1 
13140 C CD2 . LEU D 49  ? 0.4186 0.5021 2.0083 -0.0542 -0.0932 -0.0355 49  LEU D CD2 
13141 N N   . MET D 50  ? 0.4574 0.4953 1.8901 -0.0524 -0.0704 -0.0228 50  MET D N   
13142 C CA  . MET D 50  ? 0.4591 0.4911 1.8721 -0.0512 -0.0535 -0.0193 50  MET D CA  
13143 C C   . MET D 50  ? 0.4665 0.4929 1.8577 -0.0495 -0.0562 -0.0076 50  MET D C   
13144 O O   . MET D 50  ? 0.4547 0.4821 1.8494 -0.0474 -0.0447 -0.0005 50  MET D O   
13145 C CB  . MET D 50  ? 0.4793 0.5033 1.8682 -0.0537 -0.0455 -0.0287 50  MET D CB  
13146 C CG  . MET D 50  ? 0.4605 0.4869 1.8684 -0.0548 -0.0364 -0.0386 50  MET D CG  
13147 S SD  . MET D 50  ? 0.4622 0.4780 1.8437 -0.0575 -0.0307 -0.0513 50  MET D SD  
13148 C CE  . MET D 50  ? 0.4602 0.4737 1.8357 -0.0541 -0.0089 -0.0490 50  MET D CE  
13149 N N   . LYS D 51  ? 0.4867 0.5064 1.8550 -0.0505 -0.0716 -0.0052 51  LYS D N   
13150 C CA  . LYS D 51  ? 0.5156 0.5266 1.8582 -0.0495 -0.0735 0.0067  51  LYS D CA  
13151 C C   . LYS D 51  ? 0.4904 0.5075 1.8584 -0.0460 -0.0733 0.0174  51  LYS D C   
13152 O O   . LYS D 51  ? 0.4783 0.4907 1.8355 -0.0452 -0.0642 0.0265  51  LYS D O   
13153 C CB  . LYS D 51  ? 0.5594 0.5604 1.8731 -0.0506 -0.0930 0.0088  51  LYS D CB  
13154 C CG  . LYS D 51  ? 0.6002 0.5909 1.8780 -0.0544 -0.0909 -0.0004 51  LYS D CG  
13155 C CD  . LYS D 51  ? 0.6464 0.6275 1.8973 -0.0557 -0.1131 -0.0011 51  LYS D CD  
13156 C CE  . LYS D 51  ? 0.6573 0.6339 1.8912 -0.0593 -0.1160 -0.0156 51  LYS D CE  
13157 N NZ  . LYS D 51  ? 0.6835 0.6566 1.9100 -0.0597 -0.1424 -0.0177 51  LYS D NZ  
13158 N N   . PHE D 52  ? 0.4655 0.4932 1.8688 -0.0442 -0.0824 0.0153  52  PHE D N   
13159 C CA  . PHE D 52  ? 0.4418 0.4760 1.8726 -0.0406 -0.0820 0.0232  52  PHE D CA  
13160 C C   . PHE D 52  ? 0.4147 0.4534 1.8598 -0.0399 -0.0619 0.0225  52  PHE D C   
13161 O O   . PHE D 52  ? 0.4361 0.4748 1.8881 -0.0377 -0.0567 0.0309  52  PHE D O   
13162 C CB  . PHE D 52  ? 0.4319 0.4764 1.8967 -0.0392 -0.0964 0.0192  52  PHE D CB  
13163 C CG  . PHE D 52  ? 0.3986 0.4531 1.9008 -0.0361 -0.0905 0.0214  52  PHE D CG  
13164 C CD1 . PHE D 52  ? 0.3782 0.4397 1.9008 -0.0371 -0.0760 0.0142  52  PHE D CD1 
13165 C CD2 . PHE D 52  ? 0.3940 0.4493 1.9096 -0.0321 -0.0995 0.0304  52  PHE D CD2 
13166 C CE1 . PHE D 52  ? 0.3628 0.4320 1.9161 -0.0346 -0.0701 0.0156  52  PHE D CE1 
13167 C CE2 . PHE D 52  ? 0.3703 0.4341 1.9195 -0.0294 -0.0934 0.0311  52  PHE D CE2 
13168 C CZ  . PHE D 52  ? 0.3553 0.4260 1.9221 -0.0308 -0.0783 0.0235  52  PHE D CZ  
13169 N N   . ASP D 53  ? 0.3922 0.4342 1.8431 -0.0417 -0.0516 0.0127  53  ASP D N   
13170 C CA  . ASP D 53  ? 0.3599 0.4055 1.8245 -0.0405 -0.0348 0.0117  53  ASP D CA  
13171 C C   . ASP D 53  ? 0.3811 0.4199 1.8215 -0.0408 -0.0225 0.0157  53  ASP D C   
13172 O O   . ASP D 53  ? 0.3724 0.4123 1.8200 -0.0390 -0.0135 0.0214  53  ASP D O   
13173 C CB  . ASP D 53  ? 0.3380 0.3870 1.8150 -0.0421 -0.0286 0.0007  53  ASP D CB  
13174 C CG  . ASP D 53  ? 0.3155 0.3717 1.8191 -0.0430 -0.0373 -0.0048 53  ASP D CG  
13175 O OD1 . ASP D 53  ? 0.3010 0.3624 1.8219 -0.0414 -0.0467 -0.0004 53  ASP D OD1 
13176 O OD2 . ASP D 53  ? 0.3040 0.3603 1.8121 -0.0456 -0.0342 -0.0140 53  ASP D OD2 
13177 N N   . LEU D 54  ? 0.4045 0.4362 1.8166 -0.0433 -0.0212 0.0117  54  LEU D N   
13178 C CA  . LEU D 54  ? 0.4056 0.4318 1.7971 -0.0440 -0.0071 0.0134  54  LEU D CA  
13179 C C   . LEU D 54  ? 0.4125 0.4349 1.7959 -0.0436 -0.0073 0.0260  54  LEU D C   
13180 O O   . LEU D 54  ? 0.4079 0.4312 1.7951 -0.0430 0.0054  0.0297  54  LEU D O   
13181 C CB  . LEU D 54  ? 0.4249 0.4432 1.7860 -0.0469 -0.0058 0.0063  54  LEU D CB  
13182 C CG  . LEU D 54  ? 0.4123 0.4326 1.7808 -0.0476 -0.0032 -0.0066 54  LEU D CG  
13183 C CD1 . LEU D 54  ? 0.4496 0.4608 1.7862 -0.0506 -0.0059 -0.0135 54  LEU D CD1 
13184 C CD2 . LEU D 54  ? 0.3834 0.4073 1.7664 -0.0456 0.0128  -0.0109 54  LEU D CD2 
13185 N N   . GLU D 55  ? 0.4267 0.4444 1.8003 -0.0438 -0.0225 0.0324  55  GLU D N   
13186 C CA  . GLU D 55  ? 0.4549 0.4666 1.8205 -0.0433 -0.0246 0.0453  55  GLU D CA  
13187 C C   . GLU D 55  ? 0.4170 0.4365 1.8156 -0.0402 -0.0208 0.0498  55  GLU D C   
13188 O O   . GLU D 55  ? 0.4079 0.4243 1.8049 -0.0404 -0.0130 0.0577  55  GLU D O   
13189 C CB  . GLU D 55  ? 0.5022 0.5064 1.8526 -0.0431 -0.0443 0.0512  55  GLU D CB  
13190 C CG  . GLU D 55  ? 0.5406 0.5346 1.8767 -0.0429 -0.0472 0.0657  55  GLU D CG  
13191 C CD  . GLU D 55  ? 0.5689 0.5519 1.8728 -0.0466 -0.0321 0.0710  55  GLU D CD  
13192 O OE1 . GLU D 55  ? 0.5637 0.5440 1.8460 -0.0496 -0.0231 0.0634  55  GLU D OE1 
13193 O OE2 . GLU D 55  ? 0.5962 0.5728 1.8973 -0.0469 -0.0287 0.0826  55  GLU D OE2 
13194 N N   . ASN D 56  ? 0.3850 0.4142 1.8136 -0.0379 -0.0259 0.0444  56  ASN D N   
13195 C CA  . ASN D 56  ? 0.3525 0.3882 1.8103 -0.0351 -0.0215 0.0472  56  ASN D CA  
13196 C C   . ASN D 56  ? 0.3131 0.3507 1.7733 -0.0354 -0.0041 0.0447  56  ASN D C   
13197 O O   . ASN D 56  ? 0.2803 0.3187 1.7522 -0.0342 0.0014  0.0500  56  ASN D O   
13198 C CB  . ASN D 56  ? 0.3371 0.3823 1.8250 -0.0331 -0.0271 0.0406  56  ASN D CB  
13199 C CG  . ASN D 56  ? 0.3590 0.4051 1.8542 -0.0319 -0.0448 0.0428  56  ASN D CG  
13200 O OD1 . ASN D 56  ? 0.3869 0.4252 1.8609 -0.0324 -0.0551 0.0489  56  ASN D OD1 
13201 N ND2 . ASN D 56  ? 0.3722 0.4274 1.8969 -0.0304 -0.0488 0.0373  56  ASN D ND2 
13202 N N   . ILE D 57  ? 0.3113 0.3496 1.7629 -0.0369 0.0031  0.0359  57  ILE D N   
13203 C CA  . ILE D 57  ? 0.2999 0.3409 1.7572 -0.0364 0.0178  0.0314  57  ILE D CA  
13204 C C   . ILE D 57  ? 0.3062 0.3429 1.7490 -0.0380 0.0275  0.0374  57  ILE D C   
13205 O O   . ILE D 57  ? 0.2766 0.3166 1.7336 -0.0368 0.0359  0.0389  57  ILE D O   
13206 C CB  . ILE D 57  ? 0.3005 0.3421 1.7533 -0.0370 0.0212  0.0203  57  ILE D CB  
13207 C CG1 . ILE D 57  ? 0.2857 0.3322 1.7599 -0.0358 0.0153  0.0150  57  ILE D CG1 
13208 C CG2 . ILE D 57  ? 0.2926 0.3349 1.7455 -0.0363 0.0355  0.0156  57  ILE D CG2 
13209 C CD1 . ILE D 57  ? 0.2928 0.3382 1.7636 -0.0370 0.0174  0.0047  57  ILE D CD1 
13210 N N   . LYS D 58  ? 0.3415 0.3702 1.7565 -0.0408 0.0257  0.0413  58  LYS D N   
13211 C CA  . LYS D 58  ? 0.3656 0.3886 1.7659 -0.0433 0.0349  0.0489  58  LYS D CA  
13212 C C   . LYS D 58  ? 0.3829 0.4056 1.7988 -0.0422 0.0313  0.0591  58  LYS D C   
13213 O O   . LYS D 58  ? 0.3930 0.4196 1.8244 -0.0419 0.0410  0.0601  58  LYS D O   
13214 C CB  . LYS D 58  ? 0.3984 0.4102 1.7617 -0.0470 0.0333  0.0520  58  LYS D CB  
13215 C CG  . LYS D 58  ? 0.4101 0.4213 1.7578 -0.0480 0.0365  0.0407  58  LYS D CG  
13216 C CD  . LYS D 58  ? 0.4498 0.4491 1.7578 -0.0520 0.0393  0.0421  58  LYS D CD  
13217 C CE  . LYS D 58  ? 0.4747 0.4652 1.7623 -0.0527 0.0214  0.0469  58  LYS D CE  
13218 N NZ  . LYS D 58  ? 0.5167 0.4934 1.7614 -0.0567 0.0243  0.0483  58  LYS D NZ  
13219 N N   . GLU D 59  ? 0.4057 0.4245 1.8210 -0.0411 0.0166  0.0658  59  GLU D N   
13220 C CA  . GLU D 59  ? 0.4018 0.4197 1.8341 -0.0395 0.0127  0.0747  59  GLU D CA  
13221 C C   . GLU D 59  ? 0.3677 0.3956 1.8320 -0.0368 0.0189  0.0697  59  GLU D C   
13222 O O   . GLU D 59  ? 0.3843 0.4117 1.8632 -0.0359 0.0199  0.0754  59  GLU D O   
13223 C CB  . GLU D 59  ? 0.4243 0.4393 1.8604 -0.0370 -0.0054 0.0798  59  GLU D CB  
13224 C CG  . GLU D 59  ? 0.4910 0.4938 1.8948 -0.0389 -0.0158 0.0866  59  GLU D CG  
13225 C CD  . GLU D 59  ? 0.5536 0.5567 1.9635 -0.0358 -0.0365 0.0869  59  GLU D CD  
13226 O OE1 . GLU D 59  ? 0.5291 0.5420 1.9713 -0.0321 -0.0427 0.0832  59  GLU D OE1 
13227 O OE2 . GLU D 59  ? 0.6120 0.6055 1.9939 -0.0371 -0.0471 0.0900  59  GLU D OE2 
13228 N N   . GLY D 60  ? 0.3476 0.3831 1.8217 -0.0355 0.0229  0.0591  60  GLY D N   
13229 C CA  . GLY D 60  ? 0.3224 0.3652 1.8231 -0.0327 0.0268  0.0544  60  GLY D CA  
13230 C C   . GLY D 60  ? 0.3225 0.3674 1.8276 -0.0333 0.0400  0.0526  60  GLY D C   
13231 O O   . GLY D 60  ? 0.3312 0.3808 1.8559 -0.0310 0.0428  0.0490  60  GLY D O   
13232 N N   . GLY D 61  ? 0.3313 0.3727 1.8182 -0.0365 0.0481  0.0543  61  GLY D N   
13233 C CA  . GLY D 61  ? 0.3176 0.3620 1.8108 -0.0375 0.0610  0.0524  61  GLY D CA  
13234 C C   . GLY D 61  ? 0.3028 0.3510 1.7917 -0.0371 0.0695  0.0425  61  GLY D C   
13235 O O   . GLY D 61  ? 0.3134 0.3650 1.8090 -0.0377 0.0800  0.0401  61  GLY D O   
13236 N N   . TYR D 62  ? 0.2968 0.3444 1.7762 -0.0361 0.0648  0.0364  62  TYR D N   
13237 C CA  . TYR D 62  ? 0.2830 0.3331 1.7617 -0.0347 0.0708  0.0263  62  TYR D CA  
13238 C C   . TYR D 62  ? 0.3028 0.3488 1.7575 -0.0379 0.0782  0.0245  62  TYR D C   
13239 O O   . TYR D 62  ? 0.3057 0.3453 1.7395 -0.0410 0.0742  0.0300  62  TYR D O   
13240 C CB  . TYR D 62  ? 0.2864 0.3366 1.7686 -0.0326 0.0621  0.0206  62  TYR D CB  
13241 C CG  . TYR D 62  ? 0.2820 0.3351 1.7854 -0.0299 0.0561  0.0221  62  TYR D CG  
13242 C CD1 . TYR D 62  ? 0.2961 0.3486 1.8036 -0.0302 0.0468  0.0281  62  TYR D CD1 
13243 C CD2 . TYR D 62  ? 0.2748 0.3307 1.7939 -0.0268 0.0598  0.0173  62  TYR D CD2 
13244 C CE1 . TYR D 62  ? 0.2999 0.3549 1.8269 -0.0278 0.0433  0.0286  62  TYR D CE1 
13245 C CE2 . TYR D 62  ? 0.2676 0.3246 1.8028 -0.0246 0.0556  0.0183  62  TYR D CE2 
13246 C CZ  . TYR D 62  ? 0.2890 0.3459 1.8285 -0.0253 0.0482  0.0235  62  TYR D CZ  
13247 O OH  . TYR D 62  ? 0.3048 0.3626 1.8601 -0.0231 0.0458  0.0232  62  TYR D OH  
13248 N N   . ASN D 63  ? 0.3157 0.3646 1.7730 -0.0370 0.0888  0.0166  63  ASN D N   
13249 C CA  . ASN D 63  ? 0.3500 0.3950 1.7852 -0.0395 0.0974  0.0122  63  ASN D CA  
13250 C C   . ASN D 63  ? 0.3475 0.3914 1.7785 -0.0373 0.0956  0.0015  63  ASN D C   
13251 O O   . ASN D 63  ? 0.3787 0.4185 1.7906 -0.0390 0.1018  -0.0040 63  ASN D O   
13252 C CB  . ASN D 63  ? 0.3755 0.4247 1.8176 -0.0406 0.1129  0.0109  63  ASN D CB  
13253 C CG  . ASN D 63  ? 0.3893 0.4466 1.8584 -0.0357 0.1163  0.0029  63  ASN D CG  
13254 O OD1 . ASN D 63  ? 0.4168 0.4743 1.8939 -0.0319 0.1083  -0.0018 63  ASN D OD1 
13255 N ND2 . ASN D 63  ? 0.3932 0.4565 1.8767 -0.0359 0.1278  0.0012  63  ASN D ND2 
13256 N N   . THR D 64  ? 0.3212 0.3673 1.7686 -0.0338 0.0876  -0.0018 64  THR D N   
13257 C CA  . THR D 64  ? 0.3252 0.3688 1.7705 -0.0319 0.0864  -0.0116 64  THR D CA  
13258 C C   . THR D 64  ? 0.3031 0.3456 1.7568 -0.0309 0.0747  -0.0117 64  THR D C   
13259 O O   . THR D 64  ? 0.2808 0.3266 1.7505 -0.0295 0.0705  -0.0066 64  THR D O   
13260 C CB  . THR D 64  ? 0.3200 0.3673 1.7818 -0.0278 0.0953  -0.0183 64  THR D CB  
13261 O OG1 . THR D 64  ? 0.3449 0.3945 1.8011 -0.0297 0.1070  -0.0179 64  THR D OG1 
13262 C CG2 . THR D 64  ? 0.3235 0.3664 1.7836 -0.0255 0.0950  -0.0284 64  THR D CG2 
13263 N N   . ILE D 65  ? 0.3000 0.3379 1.7442 -0.0317 0.0708  -0.0187 65  ILE D N   
13264 C CA  . ILE D 65  ? 0.2955 0.3320 1.7501 -0.0311 0.0628  -0.0213 65  ILE D CA  
13265 C C   . ILE D 65  ? 0.3025 0.3352 1.7627 -0.0284 0.0675  -0.0302 65  ILE D C   
13266 O O   . ILE D 65  ? 0.3208 0.3504 1.7713 -0.0279 0.0740  -0.0370 65  ILE D O   
13267 C CB  . ILE D 65  ? 0.3002 0.3338 1.7433 -0.0348 0.0525  -0.0222 65  ILE D CB  
13268 C CG1 . ILE D 65  ? 0.3142 0.3421 1.7344 -0.0370 0.0547  -0.0292 65  ILE D CG1 
13269 C CG2 . ILE D 65  ? 0.3102 0.3469 1.7531 -0.0363 0.0444  -0.0127 65  ILE D CG2 
13270 C CD1 . ILE D 65  ? 0.3256 0.3502 1.7307 -0.0408 0.0432  -0.0298 65  ILE D CD1 
13271 N N   . ARG D 66  ? 0.2867 0.3182 1.7614 -0.0269 0.0638  -0.0304 66  ARG D N   
13272 C CA  . ARG D 66  ? 0.2871 0.3125 1.7675 -0.0242 0.0667  -0.0371 66  ARG D CA  
13273 C C   . ARG D 66  ? 0.2779 0.2982 1.7597 -0.0272 0.0606  -0.0399 66  ARG D C   
13274 O O   . ARG D 66  ? 0.2733 0.2963 1.7638 -0.0287 0.0557  -0.0352 66  ARG D O   
13275 C CB  . ARG D 66  ? 0.2743 0.3015 1.7694 -0.0197 0.0695  -0.0336 66  ARG D CB  
13276 C CG  . ARG D 66  ? 0.2745 0.2938 1.7764 -0.0160 0.0708  -0.0379 66  ARG D CG  
13277 C CD  . ARG D 66  ? 0.2758 0.2885 1.7798 -0.0184 0.0662  -0.0376 66  ARG D CD  
13278 N NE  . ARG D 66  ? 0.2658 0.2700 1.7758 -0.0147 0.0670  -0.0378 66  ARG D NE  
13279 C CZ  . ARG D 66  ? 0.2680 0.2608 1.7755 -0.0144 0.0675  -0.0421 66  ARG D CZ  
13280 N NH1 . ARG D 66  ? 0.2777 0.2668 1.7785 -0.0171 0.0678  -0.0481 66  ARG D NH1 
13281 N NH2 . ARG D 66  ? 0.2688 0.2525 1.7791 -0.0113 0.0674  -0.0403 66  ARG D NH2 
13282 N N   . THR D 67  ? 0.2761 0.2891 1.7509 -0.0281 0.0614  -0.0480 67  THR D N   
13283 C CA  . THR D 67  ? 0.2753 0.2839 1.7517 -0.0322 0.0556  -0.0515 67  THR D CA  
13284 C C   . THR D 67  ? 0.2710 0.2690 1.7523 -0.0306 0.0593  -0.0566 67  THR D C   
13285 O O   . THR D 67  ? 0.2659 0.2600 1.7460 -0.0260 0.0649  -0.0590 67  THR D O   
13286 C CB  . THR D 67  ? 0.2912 0.2996 1.7525 -0.0362 0.0512  -0.0565 67  THR D CB  
13287 O OG1 . THR D 67  ? 0.3021 0.3027 1.7534 -0.0353 0.0560  -0.0654 67  THR D OG1 
13288 C CG2 . THR D 67  ? 0.2935 0.3088 1.7439 -0.0368 0.0494  -0.0509 67  THR D CG2 
13289 N N   . TRP D 68  ? 0.2647 0.2578 1.7527 -0.0344 0.0561  -0.0582 68  TRP D N   
13290 C CA  . TRP D 68  ? 0.2590 0.2394 1.7505 -0.0336 0.0596  -0.0617 68  TRP D CA  
13291 C C   . TRP D 68  ? 0.2732 0.2452 1.7592 -0.0372 0.0584  -0.0709 68  TRP D C   
13292 O O   . TRP D 68  ? 0.2845 0.2439 1.7723 -0.0368 0.0613  -0.0742 68  TRP D O   
13293 C CB  . TRP D 68  ? 0.2426 0.2207 1.7455 -0.0356 0.0597  -0.0568 68  TRP D CB  
13294 C CG  . TRP D 68  ? 0.2267 0.2092 1.7340 -0.0314 0.0615  -0.0491 68  TRP D CG  
13295 C CD1 . TRP D 68  ? 0.2236 0.1977 1.7313 -0.0269 0.0650  -0.0465 68  TRP D CD1 
13296 C CD2 . TRP D 68  ? 0.2221 0.2175 1.7340 -0.0314 0.0588  -0.0433 68  TRP D CD2 
13297 N NE1 . TRP D 68  ? 0.2170 0.1983 1.7289 -0.0243 0.0648  -0.0402 68  TRP D NE1 
13298 C CE2 . TRP D 68  ? 0.2143 0.2087 1.7297 -0.0271 0.0615  -0.0380 68  TRP D CE2 
13299 C CE3 . TRP D 68  ? 0.2181 0.2242 1.7309 -0.0345 0.0534  -0.0419 68  TRP D CE3 
13300 C CZ2 . TRP D 68  ? 0.1905 0.1947 1.7117 -0.0262 0.0599  -0.0321 68  TRP D CZ2 
13301 C CZ3 . TRP D 68  ? 0.1999 0.2150 1.7181 -0.0331 0.0518  -0.0351 68  TRP D CZ3 
13302 C CH2 . TRP D 68  ? 0.1889 0.2030 1.7118 -0.0292 0.0555  -0.0306 68  TRP D CH2 
13303 N N   . SER D 69  ? 0.2800 0.2576 1.7574 -0.0403 0.0540  -0.0749 69  SER D N   
13304 C CA  . SER D 69  ? 0.2982 0.2694 1.7709 -0.0451 0.0504  -0.0840 69  SER D CA  
13305 C C   . SER D 69  ? 0.3196 0.2952 1.7754 -0.0460 0.0470  -0.0884 69  SER D C   
13306 O O   . SER D 69  ? 0.3203 0.3058 1.7716 -0.0460 0.0435  -0.0828 69  SER D O   
13307 C CB  . SER D 69  ? 0.2918 0.2648 1.7776 -0.0513 0.0448  -0.0834 69  SER D CB  
13308 O OG  . SER D 69  ? 0.3045 0.2775 1.7852 -0.0565 0.0375  -0.0914 69  SER D OG  
13309 N N   . GLN D 70  ? 0.3538 0.3205 1.7993 -0.0470 0.0478  -0.0988 70  GLN D N   
13310 C CA  . GLN D 70  ? 0.3815 0.3482 1.8063 -0.0469 0.0479  -0.1048 70  GLN D CA  
13311 C C   . GLN D 70  ? 0.3906 0.3642 1.8060 -0.0519 0.0371  -0.1036 70  GLN D C   
13312 O O   . GLN D 70  ? 0.3969 0.3713 1.8219 -0.0567 0.0284  -0.1050 70  GLN D O   
13313 C CB  . GLN D 70  ? 0.4047 0.3587 1.8213 -0.0473 0.0508  -0.1175 70  GLN D CB  
13314 C CG  . GLN D 70  ? 0.4106 0.3562 1.8372 -0.0526 0.0453  -0.1235 70  GLN D CG  
13315 C CD  . GLN D 70  ? 0.4054 0.3420 1.8481 -0.0501 0.0513  -0.1217 70  GLN D CD  
13316 O OE1 . GLN D 70  ? 0.3902 0.3306 1.8416 -0.0460 0.0553  -0.1124 70  GLN D OE1 
13317 N NE2 . GLN D 70  ? 0.4170 0.3399 1.8620 -0.0526 0.0516  -0.1304 70  GLN D NE2 
13318 N N   . TYR D 71  ? 0.4079 0.3856 1.8046 -0.0507 0.0379  -0.1013 71  TYR D N   
13319 C CA  . TYR D 71  ? 0.4308 0.4123 1.8134 -0.0546 0.0267  -0.0998 71  TYR D CA  
13320 C C   . TYR D 71  ? 0.4520 0.4242 1.8142 -0.0581 0.0224  -0.1122 71  TYR D C   
13321 O O   . TYR D 71  ? 0.4534 0.4171 1.8091 -0.0566 0.0309  -0.1213 71  TYR D O   
13322 C CB  . TYR D 71  ? 0.4418 0.4295 1.8119 -0.0522 0.0297  -0.0902 71  TYR D CB  
13323 C CG  . TYR D 71  ? 0.4286 0.4263 1.8169 -0.0507 0.0274  -0.0776 71  TYR D CG  
13324 C CD1 . TYR D 71  ? 0.4183 0.4208 1.8284 -0.0526 0.0190  -0.0747 71  TYR D CD1 
13325 C CD2 . TYR D 71  ? 0.4249 0.4271 1.8086 -0.0477 0.0340  -0.0690 71  TYR D CD2 
13326 C CE1 . TYR D 71  ? 0.3928 0.4037 1.8188 -0.0510 0.0176  -0.0644 71  TYR D CE1 
13327 C CE2 . TYR D 71  ? 0.4110 0.4212 1.8106 -0.0463 0.0317  -0.0583 71  TYR D CE2 
13328 C CZ  . TYR D 71  ? 0.4034 0.4178 1.8236 -0.0477 0.0235  -0.0562 71  TYR D CZ  
13329 O OH  . TYR D 71  ? 0.3956 0.4172 1.8314 -0.0460 0.0223  -0.0468 71  TYR D OH  
13330 N N   . SER D 72  ? 0.4562 0.4297 1.8095 -0.0626 0.0082  -0.1133 72  SER D N   
13331 C CA  . SER D 72  ? 0.4789 0.4432 1.8071 -0.0659 0.0026  -0.1247 72  SER D CA  
13332 C C   . SER D 72  ? 0.4908 0.4524 1.7865 -0.0642 0.0079  -0.1225 72  SER D C   
13333 O O   . SER D 72  ? 0.4746 0.4425 1.7699 -0.0615 0.0127  -0.1113 72  SER D O   
13334 C CB  . SER D 72  ? 0.4843 0.4505 1.8154 -0.0712 -0.0160 -0.1274 72  SER D CB  
13335 O OG  . SER D 72  ? 0.4863 0.4589 1.8080 -0.0710 -0.0257 -0.1173 72  SER D OG  
13336 N N   . GLU D 73  ? 0.5207 0.4717 1.7885 -0.0663 0.0077  -0.1337 73  GLU D N   
13337 C CA  . GLU D 73  ? 0.5476 0.4936 1.7803 -0.0657 0.0142  -0.1330 73  GLU D CA  
13338 C C   . GLU D 73  ? 0.5542 0.5042 1.7733 -0.0672 0.0025  -0.1210 73  GLU D C   
13339 O O   . GLU D 73  ? 0.5671 0.5185 1.7731 -0.0653 0.0111  -0.1120 73  GLU D O   
13340 C CB  . GLU D 73  ? 0.5835 0.5161 1.7863 -0.0683 0.0146  -0.1483 73  GLU D CB  
13341 C CG  . GLU D 73  ? 0.6141 0.5400 1.7781 -0.0681 0.0244  -0.1480 73  GLU D CG  
13342 C CD  . GLU D 73  ? 0.6525 0.5647 1.7886 -0.0695 0.0308  -0.1646 73  GLU D CD  
13343 O OE1 . GLU D 73  ? 0.6632 0.5695 1.8056 -0.0715 0.0234  -0.1769 73  GLU D OE1 
13344 O OE2 . GLU D 73  ? 0.6777 0.5847 1.7861 -0.0689 0.0444  -0.1655 73  GLU D OE2 
13345 N N   . ASN D 74  ? 0.5569 0.5082 1.7805 -0.0705 -0.0171 -0.1213 74  ASN D N   
13346 C CA  . ASN D 74  ? 0.5629 0.5177 1.7787 -0.0714 -0.0321 -0.1103 74  ASN D CA  
13347 C C   . ASN D 74  ? 0.5377 0.5037 1.7768 -0.0678 -0.0261 -0.0956 74  ASN D C   
13348 O O   . ASN D 74  ? 0.5530 0.5183 1.7749 -0.0669 -0.0267 -0.0850 74  ASN D O   
13349 C CB  . ASN D 74  ? 0.5657 0.5239 1.7973 -0.0746 -0.0538 -0.1139 74  ASN D CB  
13350 C CG  . ASN D 74  ? 0.6044 0.5516 1.8050 -0.0786 -0.0686 -0.1243 74  ASN D CG  
13351 O OD1 . ASN D 74  ? 0.6373 0.5723 1.7996 -0.0792 -0.0623 -0.1298 74  ASN D OD1 
13352 N ND2 . ASN D 74  ? 0.6031 0.5545 1.8204 -0.0814 -0.0887 -0.1276 74  ASN D ND2 
13353 N N   . GLN D 75  ? 0.5116 0.4862 1.7878 -0.0660 -0.0207 -0.0948 75  GLN D N   
13354 C CA  . GLN D 75  ? 0.4946 0.4789 1.7926 -0.0625 -0.0142 -0.0822 75  GLN D CA  
13355 C C   . GLN D 75  ? 0.5016 0.4839 1.7858 -0.0596 0.0037  -0.0784 75  GLN D C   
13356 O O   . GLN D 75  ? 0.5024 0.4889 1.7872 -0.0578 0.0069  -0.0670 75  GLN D O   
13357 C CB  . GLN D 75  ? 0.4675 0.4592 1.8038 -0.0613 -0.0108 -0.0828 75  GLN D CB  
13358 C CG  . GLN D 75  ? 0.4669 0.4634 1.8249 -0.0645 -0.0261 -0.0851 75  GLN D CG  
13359 C CD  . GLN D 75  ? 0.4494 0.4486 1.8386 -0.0649 -0.0202 -0.0890 75  GLN D CD  
13360 O OE1 . GLN D 75  ? 0.4767 0.4689 1.8644 -0.0646 -0.0099 -0.0965 75  GLN D OE1 
13361 N NE2 . GLN D 75  ? 0.4146 0.4228 1.8316 -0.0657 -0.0262 -0.0842 75  GLN D NE2 
13362 N N   . LEU D 76  ? 0.5340 0.5097 1.8072 -0.0591 0.0157  -0.0884 76  LEU D N   
13363 C CA  . LEU D 76  ? 0.5641 0.5388 1.8265 -0.0566 0.0330  -0.0862 76  LEU D CA  
13364 C C   . LEU D 76  ? 0.6022 0.5721 1.8314 -0.0587 0.0316  -0.0794 76  LEU D C   
13365 O O   . LEU D 76  ? 0.6168 0.5901 1.8453 -0.0573 0.0411  -0.0700 76  LEU D O   
13366 C CB  . LEU D 76  ? 0.5834 0.5516 1.8405 -0.0554 0.0455  -0.0997 76  LEU D CB  
13367 C CG  . LEU D 76  ? 0.5597 0.5324 1.8494 -0.0512 0.0540  -0.1020 76  LEU D CG  
13368 C CD1 . LEU D 76  ? 0.5786 0.5434 1.8630 -0.0495 0.0652  -0.1157 76  LEU D CD1 
13369 C CD2 . LEU D 76  ? 0.5302 0.5120 1.8353 -0.0476 0.0630  -0.0908 76  LEU D CD2 
13370 N N   . LYS D 77  ? 0.6185 0.5797 1.8201 -0.0624 0.0190  -0.0838 77  LYS D N   
13371 C CA  . LYS D 77  ? 0.6474 0.5998 1.8100 -0.0647 0.0181  -0.0781 77  LYS D CA  
13372 C C   . LYS D 77  ? 0.6164 0.5744 1.7865 -0.0637 0.0133  -0.0612 77  LYS D C   
13373 O O   . LYS D 77  ? 0.6214 0.5745 1.7692 -0.0645 0.0213  -0.0530 77  LYS D O   
13374 C CB  . LYS D 77  ? 0.6828 0.6239 1.8147 -0.0684 0.0019  -0.0857 77  LYS D CB  
13375 C CG  . LYS D 77  ? 0.7146 0.6455 1.8237 -0.0699 0.0116  -0.1016 77  LYS D CG  
13376 C CD  . LYS D 77  ? 0.7607 0.6792 1.8368 -0.0739 -0.0051 -0.1102 77  LYS D CD  
13377 C CE  . LYS D 77  ? 0.7899 0.6977 1.8437 -0.0751 0.0065  -0.1266 77  LYS D CE  
13378 N NZ  . LYS D 77  ? 0.8354 0.7297 1.8535 -0.0791 -0.0096 -0.1355 77  LYS D NZ  
13379 N N   . LEU D 78  ? 0.5763 0.5442 1.7794 -0.0621 0.0014  -0.0567 78  LEU D N   
13380 C CA  . LEU D 78  ? 0.5611 0.5342 1.7752 -0.0609 -0.0062 -0.0422 78  LEU D CA  
13381 C C   . LEU D 78  ? 0.5379 0.5179 1.7698 -0.0582 0.0110  -0.0352 78  LEU D C   
13382 O O   . LEU D 78  ? 0.5430 0.5216 1.7664 -0.0582 0.0135  -0.0237 78  LEU D O   
13383 C CB  . LEU D 78  ? 0.5397 0.5217 1.7862 -0.0601 -0.0223 -0.0425 78  LEU D CB  
13384 C CG  . LEU D 78  ? 0.5352 0.5213 1.7916 -0.0588 -0.0359 -0.0295 78  LEU D CG  
13385 C CD1 . LEU D 78  ? 0.5791 0.5535 1.7981 -0.0608 -0.0497 -0.0251 78  LEU D CD1 
13386 C CD2 . LEU D 78  ? 0.5101 0.5067 1.8036 -0.0581 -0.0481 -0.0324 78  LEU D CD2 
13387 N N   . VAL D 79  ? 0.5103 0.4967 1.7669 -0.0560 0.0222  -0.0422 79  VAL D N   
13388 C CA  . VAL D 79  ? 0.4781 0.4710 1.7522 -0.0533 0.0376  -0.0371 79  VAL D CA  
13389 C C   . VAL D 79  ? 0.5009 0.4872 1.7468 -0.0549 0.0520  -0.0361 79  VAL D C   
13390 O O   . VAL D 79  ? 0.4997 0.4877 1.7456 -0.0550 0.0582  -0.0258 79  VAL D O   
13391 C CB  . VAL D 79  ? 0.4428 0.4420 1.7460 -0.0501 0.0460  -0.0445 79  VAL D CB  
13392 C CG1 . VAL D 79  ? 0.4203 0.4263 1.7415 -0.0470 0.0589  -0.0386 79  VAL D CG1 
13393 C CG2 . VAL D 79  ? 0.4223 0.4261 1.7507 -0.0495 0.0338  -0.0458 79  VAL D CG2 
13394 N N   . GLN D 80  ? 0.5253 0.5032 1.7463 -0.0567 0.0573  -0.0468 80  GLN D N   
13395 C CA  . GLN D 80  ? 0.5584 0.5294 1.7509 -0.0588 0.0729  -0.0473 80  GLN D CA  
13396 C C   . GLN D 80  ? 0.5782 0.5437 1.7487 -0.0617 0.0693  -0.0330 80  GLN D C   
13397 O O   . GLN D 80  ? 0.5743 0.5417 1.7466 -0.0622 0.0827  -0.0254 80  GLN D O   
13398 C CB  . GLN D 80  ? 0.5948 0.5547 1.7561 -0.0611 0.0752  -0.0605 80  GLN D CB  
13399 C CG  . GLN D 80  ? 0.6249 0.5799 1.7660 -0.0624 0.0974  -0.0649 80  GLN D CG  
13400 C CD  . GLN D 80  ? 0.6089 0.5745 1.7834 -0.0582 0.1142  -0.0707 80  GLN D CD  
13401 O OE1 . GLN D 80  ? 0.5858 0.5593 1.7932 -0.0543 0.1094  -0.0740 80  GLN D OE1 
13402 N NE2 . GLN D 80  ? 0.6317 0.5971 1.7983 -0.0591 0.1345  -0.0722 80  GLN D NE2 
13403 N N   . GLU D 81  ? 0.5839 0.5419 1.7348 -0.0635 0.0502  -0.0293 81  GLU D N   
13404 C CA  . GLU D 81  ? 0.6075 0.5559 1.7302 -0.0662 0.0444  -0.0163 81  GLU D CA  
13405 C C   . GLU D 81  ? 0.5613 0.5180 1.7115 -0.0642 0.0425  -0.0023 81  GLU D C   
13406 O O   . GLU D 81  ? 0.5678 0.5167 1.6993 -0.0662 0.0418  0.0100  81  GLU D O   
13407 C CB  . GLU D 81  ? 0.6477 0.5870 1.7472 -0.0676 0.0216  -0.0176 81  GLU D CB  
13408 C CG  . GLU D 81  ? 0.6886 0.6177 1.7637 -0.0690 0.0082  -0.0027 81  GLU D CG  
13409 C CD  . GLU D 81  ? 0.7139 0.6402 1.7860 -0.0683 -0.0195 -0.0029 81  GLU D CD  
13410 O OE1 . GLU D 81  ? 0.7192 0.6506 1.8043 -0.0679 -0.0274 -0.0156 81  GLU D OE1 
13411 O OE2 . GLU D 81  ? 0.7365 0.6556 1.7954 -0.0682 -0.0339 0.0095  81  GLU D OE2 
13412 N N   . SER D 82  ? 0.5111 0.4817 1.7036 -0.0605 0.0412  -0.0041 82  SER D N   
13413 C CA  . SER D 82  ? 0.4846 0.4624 1.7039 -0.0583 0.0351  0.0074  82  SER D CA  
13414 C C   . SER D 82  ? 0.4747 0.4563 1.7042 -0.0584 0.0533  0.0134  82  SER D C   
13415 O O   . SER D 82  ? 0.4578 0.4413 1.6998 -0.0578 0.0506  0.0246  82  SER D O   
13416 C CB  . SER D 82  ? 0.4466 0.4363 1.7040 -0.0548 0.0265  0.0028  82  SER D CB  
13417 O OG  . SER D 82  ? 0.4208 0.4185 1.7009 -0.0527 0.0409  -0.0045 82  SER D OG  
13418 N N   . GLY D 83  ? 0.4830 0.4658 1.7094 -0.0590 0.0714  0.0047  83  GLY D N   
13419 C CA  . GLY D 83  ? 0.4734 0.4612 1.7124 -0.0592 0.0902  0.0073  83  GLY D CA  
13420 C C   . GLY D 83  ? 0.4369 0.4387 1.7175 -0.0546 0.0946  0.0015  83  GLY D C   
13421 O O   . GLY D 83  ? 0.4181 0.4259 1.7140 -0.0541 0.1096  0.0004  83  GLY D O   
13422 N N   . LEU D 84  ? 0.4250 0.4312 1.7238 -0.0515 0.0810  -0.0019 84  LEU D N   
13423 C CA  . LEU D 84  ? 0.3966 0.4134 1.7315 -0.0472 0.0824  -0.0053 84  LEU D CA  
13424 C C   . LEU D 84  ? 0.4058 0.4244 1.7460 -0.0451 0.0932  -0.0181 84  LEU D C   
13425 O O   . LEU D 84  ? 0.4282 0.4401 1.7455 -0.0469 0.0967  -0.0257 84  LEU D O   
13426 C CB  . LEU D 84  ? 0.3729 0.3922 1.7227 -0.0455 0.0657  -0.0041 84  LEU D CB  
13427 C CG  . LEU D 84  ? 0.3641 0.3847 1.7221 -0.0456 0.0558  0.0080  84  LEU D CG  
13428 C CD1 . LEU D 84  ? 0.3561 0.3790 1.7265 -0.0444 0.0401  0.0065  84  LEU D CD1 
13429 C CD2 . LEU D 84  ? 0.3372 0.3649 1.7203 -0.0434 0.0628  0.0131  84  LEU D CD2 
13430 N N   . LYS D 85  ? 0.3968 0.4235 1.7666 -0.0411 0.0981  -0.0205 85  LYS D N   
13431 C CA  . LYS D 85  ? 0.4187 0.4469 1.7984 -0.0378 0.1064  -0.0320 85  LYS D CA  
13432 C C   . LYS D 85  ? 0.4280 0.4565 1.8241 -0.0348 0.0960  -0.0359 85  LYS D C   
13433 O O   . LYS D 85  ? 0.4476 0.4789 1.8564 -0.0343 0.0867  -0.0292 85  LYS D O   
13434 C CB  . LYS D 85  ? 0.4099 0.4457 1.8111 -0.0349 0.1192  -0.0332 85  LYS D CB  
13435 C CG  . LYS D 85  ? 0.4307 0.4677 1.8220 -0.0384 0.1324  -0.0294 85  LYS D CG  
13436 C CD  . LYS D 85  ? 0.4683 0.4976 1.8284 -0.0422 0.1416  -0.0347 85  LYS D CD  
13437 C CE  . LYS D 85  ? 0.4925 0.5228 1.8454 -0.0462 0.1562  -0.0293 85  LYS D CE  
13438 N NZ  . LYS D 85  ? 0.5378 0.5581 1.8542 -0.0510 0.1651  -0.0323 85  LYS D NZ  
13439 N N   . LEU D 86  ? 0.4370 0.4616 1.8321 -0.0330 0.0987  -0.0469 86  LEU D N   
13440 C CA  . LEU D 86  ? 0.4179 0.4393 1.8223 -0.0316 0.0896  -0.0513 86  LEU D CA  
13441 C C   . LEU D 86  ? 0.4086 0.4296 1.8303 -0.0264 0.0960  -0.0588 86  LEU D C   
13442 O O   . LEU D 86  ? 0.4058 0.4244 1.8226 -0.0248 0.1052  -0.0672 86  LEU D O   
13443 C CB  . LEU D 86  ? 0.4407 0.4543 1.8231 -0.0353 0.0835  -0.0575 86  LEU D CB  
13444 C CG  . LEU D 86  ? 0.4297 0.4379 1.8194 -0.0347 0.0775  -0.0655 86  LEU D CG  
13445 C CD1 . LEU D 86  ? 0.4068 0.4183 1.8177 -0.0340 0.0692  -0.0598 86  LEU D CD1 
13446 C CD2 . LEU D 86  ? 0.4414 0.4427 1.8089 -0.0392 0.0703  -0.0715 86  LEU D CD2 
13447 N N   . ILE D 87  ? 0.3919 0.4143 1.8334 -0.0236 0.0909  -0.0555 87  ILE D N   
13448 C CA  . ILE D 87  ? 0.3817 0.3996 1.8366 -0.0189 0.0922  -0.0617 87  ILE D CA  
13449 C C   . ILE D 87  ? 0.3943 0.4043 1.8454 -0.0214 0.0840  -0.0647 87  ILE D C   
13450 O O   . ILE D 87  ? 0.4241 0.4352 1.8813 -0.0232 0.0766  -0.0588 87  ILE D O   
13451 C CB  . ILE D 87  ? 0.3540 0.3765 1.8296 -0.0147 0.0916  -0.0559 87  ILE D CB  
13452 C CG1 . ILE D 87  ? 0.3339 0.3654 1.8162 -0.0134 0.0991  -0.0529 87  ILE D CG1 
13453 C CG2 . ILE D 87  ? 0.3546 0.3699 1.8419 -0.0095 0.0910  -0.0609 87  ILE D CG2 
13454 C CD1 . ILE D 87  ? 0.3111 0.3473 1.8130 -0.0099 0.0965  -0.0471 87  ILE D CD1 
13455 N N   . MET D 88  ? 0.3917 0.3939 1.8334 -0.0218 0.0857  -0.0745 88  MET D N   
13456 C CA  . MET D 88  ? 0.3870 0.3817 1.8239 -0.0256 0.0782  -0.0784 88  MET D CA  
13457 C C   . MET D 88  ? 0.3816 0.3678 1.8319 -0.0225 0.0781  -0.0815 88  MET D C   
13458 O O   . MET D 88  ? 0.3703 0.3515 1.8240 -0.0178 0.0841  -0.0873 88  MET D O   
13459 C CB  . MET D 88  ? 0.4017 0.3906 1.8192 -0.0285 0.0794  -0.0881 88  MET D CB  
13460 C CG  . MET D 88  ? 0.4031 0.3853 1.8170 -0.0333 0.0703  -0.0926 88  MET D CG  
13461 S SD  . MET D 88  ? 0.4405 0.4153 1.8288 -0.0363 0.0715  -0.1050 88  MET D SD  
13462 C CE  . MET D 88  ? 0.4534 0.4353 1.8224 -0.0410 0.0644  -0.0976 88  MET D CE  
13463 N N   . GLY D 89  ? 0.3855 0.3692 1.8431 -0.0253 0.0715  -0.0776 89  GLY D N   
13464 C CA  . GLY D 89  ? 0.3973 0.3700 1.8642 -0.0236 0.0715  -0.0795 89  GLY D CA  
13465 C C   . GLY D 89  ? 0.4175 0.3795 1.8780 -0.0270 0.0701  -0.0891 89  GLY D C   
13466 O O   . GLY D 89  ? 0.4290 0.3933 1.8809 -0.0324 0.0657  -0.0925 89  GLY D O   
13467 N N   . ILE D 90  ? 0.4091 0.3585 1.8739 -0.0237 0.0731  -0.0936 90  ILE D N   
13468 C CA  . ILE D 90  ? 0.4373 0.3746 1.8985 -0.0275 0.0715  -0.1021 90  ILE D CA  
13469 C C   . ILE D 90  ? 0.4614 0.3894 1.9322 -0.0303 0.0693  -0.0979 90  ILE D C   
13470 O O   . ILE D 90  ? 0.4882 0.4090 1.9649 -0.0258 0.0716  -0.0932 90  ILE D O   
13471 C CB  . ILE D 90  ? 0.4211 0.3484 1.8787 -0.0225 0.0768  -0.1118 90  ILE D CB  
13472 C CG1 . ILE D 90  ? 0.4079 0.3450 1.8601 -0.0178 0.0827  -0.1142 90  ILE D CG1 
13473 C CG2 . ILE D 90  ? 0.4299 0.3472 1.8803 -0.0277 0.0746  -0.1223 90  ILE D CG2 
13474 C CD1 . ILE D 90  ? 0.4157 0.3598 1.8514 -0.0227 0.0823  -0.1187 90  ILE D CD1 
13475 N N   . ASP D 91  ? 0.4905 0.4185 1.9630 -0.0380 0.0647  -0.0996 91  ASP D N   
13476 C CA  . ASP D 91  ? 0.4863 0.4055 1.9685 -0.0424 0.0644  -0.0966 91  ASP D CA  
13477 C C   . ASP D 91  ? 0.4804 0.3799 1.9618 -0.0421 0.0672  -0.1031 91  ASP D C   
13478 O O   . ASP D 91  ? 0.4729 0.3665 1.9541 -0.0478 0.0651  -0.1111 91  ASP D O   
13479 C CB  . ASP D 91  ? 0.4856 0.4130 1.9742 -0.0508 0.0587  -0.0973 91  ASP D CB  
13480 C CG  . ASP D 91  ? 0.4861 0.4044 1.9867 -0.0570 0.0600  -0.0963 91  ASP D CG  
13481 O OD1 . ASP D 91  ? 0.4873 0.3941 1.9894 -0.0545 0.0657  -0.0913 91  ASP D OD1 
13482 O OD2 . ASP D 91  ? 0.4630 0.3855 1.9712 -0.0645 0.0553  -0.1007 91  ASP D OD2 
13483 N N   . ILE D 92  ? 0.4803 0.3697 1.9611 -0.0348 0.0712  -0.0999 92  ILE D N   
13484 C CA  . ILE D 92  ? 0.5058 0.3737 1.9873 -0.0336 0.0737  -0.1016 92  ILE D CA  
13485 C C   . ILE D 92  ? 0.5017 0.3631 1.9874 -0.0365 0.0751  -0.0918 92  ILE D C   
13486 O O   . ILE D 92  ? 0.4875 0.3557 1.9735 -0.0327 0.0754  -0.0836 92  ILE D O   
13487 C CB  . ILE D 92  ? 0.5308 0.3919 2.0098 -0.0232 0.0757  -0.1031 92  ILE D CB  
13488 C CG1 . ILE D 92  ? 0.5464 0.4047 2.0216 -0.0214 0.0768  -0.1155 92  ILE D CG1 
13489 C CG2 . ILE D 92  ? 0.5505 0.3906 2.0301 -0.0194 0.0767  -0.0979 92  ILE D CG2 
13490 C CD1 . ILE D 92  ? 0.5425 0.4200 2.0124 -0.0219 0.0769  -0.1197 92  ILE D CD1 
13491 N N   . LYS D 93  ? 0.5353 0.3833 2.0241 -0.0436 0.0768  -0.0929 93  LYS D N   
13492 C CA  . LYS D 93  ? 0.5278 0.3713 2.0200 -0.0480 0.0800  -0.0843 93  LYS D CA  
13493 C C   . LYS D 93  ? 0.5112 0.3379 1.9951 -0.0407 0.0823  -0.0767 93  LYS D C   
13494 O O   . LYS D 93  ? 0.5591 0.3663 2.0381 -0.0374 0.0829  -0.0790 93  LYS D O   
13495 C CB  . LYS D 93  ? 0.5606 0.3946 2.0599 -0.0584 0.0821  -0.0885 93  LYS D CB  
13496 C CG  . LYS D 93  ? 0.5677 0.4179 2.0759 -0.0654 0.0774  -0.0968 93  LYS D CG  
13497 C CD  . LYS D 93  ? 0.5572 0.4299 2.0730 -0.0673 0.0749  -0.0921 93  LYS D CD  
13498 C CE  . LYS D 93  ? 0.5608 0.4471 2.0880 -0.0753 0.0691  -0.0989 93  LYS D CE  
13499 N NZ  . LYS D 93  ? 0.5294 0.4334 2.0681 -0.0780 0.0676  -0.0934 93  LYS D NZ  
13500 N N   . PRO D 94  ? 0.4644 0.2972 1.9461 -0.0375 0.0828  -0.0679 94  PRO D N   
13501 C CA  . PRO D 94  ? 0.4695 0.2859 1.9415 -0.0305 0.0832  -0.0606 94  PRO D CA  
13502 C C   . PRO D 94  ? 0.4999 0.2892 1.9636 -0.0340 0.0876  -0.0561 94  PRO D C   
13503 O O   . PRO D 94  ? 0.5155 0.2869 1.9684 -0.0271 0.0859  -0.0512 94  PRO D O   
13504 C CB  . PRO D 94  ? 0.4639 0.2950 1.9362 -0.0290 0.0828  -0.0535 94  PRO D CB  
13505 C CG  . PRO D 94  ? 0.4467 0.2949 1.9293 -0.0378 0.0847  -0.0552 94  PRO D CG  
13506 C CD  . PRO D 94  ? 0.4528 0.3080 1.9408 -0.0398 0.0818  -0.0648 94  PRO D CD  
13507 N N   . GLU D 95  ? 0.5112 0.2976 1.9803 -0.0448 0.0929  -0.0576 95  GLU D N   
13508 C CA  . GLU D 95  ? 0.5319 0.2925 1.9935 -0.0504 0.0994  -0.0529 95  GLU D CA  
13509 C C   . GLU D 95  ? 0.5353 0.2754 1.9960 -0.0518 0.0995  -0.0585 95  GLU D C   
13510 O O   . GLU D 95  ? 0.5520 0.2658 2.0033 -0.0544 0.1041  -0.0537 95  GLU D O   
13511 C CB  . GLU D 95  ? 0.5476 0.3158 2.0185 -0.0618 0.1068  -0.0515 95  GLU D CB  
13512 C CG  . GLU D 95  ? 0.5741 0.3481 2.0397 -0.0610 0.1102  -0.0432 95  GLU D CG  
13513 C CD  . GLU D 95  ? 0.6137 0.3966 2.0913 -0.0718 0.1188  -0.0426 95  GLU D CD  
13514 O OE1 . GLU D 95  ? 0.6315 0.3975 2.1099 -0.0805 0.1273  -0.0423 95  GLU D OE1 
13515 O OE2 . GLU D 95  ? 0.5962 0.4022 2.0837 -0.0716 0.1175  -0.0424 95  GLU D OE2 
13516 N N   . GLU D 96  ? 0.5277 0.2779 1.9969 -0.0505 0.0950  -0.0687 96  GLU D N   
13517 C CA  . GLU D 96  ? 0.5625 0.2937 2.0318 -0.0514 0.0947  -0.0757 96  GLU D CA  
13518 C C   . GLU D 96  ? 0.5797 0.2884 2.0375 -0.0405 0.0918  -0.0726 96  GLU D C   
13519 O O   . GLU D 96  ? 0.5785 0.2912 2.0304 -0.0308 0.0878  -0.0675 96  GLU D O   
13520 C CB  . GLU D 96  ? 0.5718 0.3202 2.0498 -0.0508 0.0900  -0.0880 96  GLU D CB  
13521 C CG  . GLU D 96  ? 0.5797 0.3486 2.0697 -0.0611 0.0900  -0.0930 96  GLU D CG  
13522 C CD  . GLU D 96  ? 0.6295 0.3848 2.1274 -0.0728 0.0942  -0.0965 96  GLU D CD  
13523 O OE1 . GLU D 96  ? 0.6647 0.3967 2.1599 -0.0736 0.0956  -0.1003 96  GLU D OE1 
13524 O OE2 . GLU D 96  ? 0.6135 0.3828 2.1226 -0.0813 0.0959  -0.0957 96  GLU D OE2 
13525 N N   . ASP D 97  ? 0.6019 0.2871 2.0585 -0.0420 0.0928  -0.0767 97  ASP D N   
13526 C CA  . ASP D 97  ? 0.6253 0.2881 2.0739 -0.0313 0.0888  -0.0754 97  ASP D CA  
13527 C C   . ASP D 97  ? 0.6069 0.2841 2.0635 -0.0224 0.0836  -0.0861 97  ASP D C   
13528 O O   . ASP D 97  ? 0.5906 0.2714 2.0546 -0.0260 0.0841  -0.0974 97  ASP D O   
13529 C CB  . ASP D 97  ? 0.6726 0.3026 2.1168 -0.0364 0.0923  -0.0749 97  ASP D CB  
13530 C CG  . ASP D 97  ? 0.7165 0.3203 2.1538 -0.0253 0.0873  -0.0742 97  ASP D CG  
13531 O OD1 . ASP D 97  ? 0.7270 0.3412 2.1665 -0.0130 0.0808  -0.0762 97  ASP D OD1 
13532 O OD2 . ASP D 97  ? 0.7194 0.2924 2.1505 -0.0291 0.0901  -0.0715 97  ASP D OD2 
13533 N N   . TYR D 98  ? 0.6057 0.2906 2.0608 -0.0108 0.0787  -0.0831 98  TYR D N   
13534 C CA  . TYR D 98  ? 0.5966 0.2963 2.0604 -0.0023 0.0757  -0.0930 98  TYR D CA  
13535 C C   . TYR D 98  ? 0.6394 0.3166 2.1056 0.0027  0.0746  -0.1007 98  TYR D C   
13536 O O   . TYR D 98  ? 0.6700 0.3568 2.1440 0.0071  0.0745  -0.1122 98  TYR D O   
13537 C CB  . TYR D 98  ? 0.5788 0.2911 2.0435 0.0084  0.0712  -0.0876 98  TYR D CB  
13538 C CG  . TYR D 98  ? 0.5534 0.2826 2.0144 0.0041  0.0719  -0.0786 98  TYR D CG  
13539 C CD1 . TYR D 98  ? 0.5453 0.2922 2.0089 -0.0064 0.0759  -0.0801 98  TYR D CD1 
13540 C CD2 . TYR D 98  ? 0.5351 0.2616 1.9904 0.0109  0.0676  -0.0689 98  TYR D CD2 
13541 C CE1 . TYR D 98  ? 0.5180 0.2797 1.9800 -0.0100 0.0768  -0.0725 98  TYR D CE1 
13542 C CE2 . TYR D 98  ? 0.5155 0.2558 1.9673 0.0069  0.0687  -0.0615 98  TYR D CE2 
13543 C CZ  . TYR D 98  ? 0.5070 0.2651 1.9628 -0.0034 0.0737  -0.0634 98  TYR D CZ  
13544 O OH  . TYR D 98  ? 0.4832 0.2548 1.9375 -0.0071 0.0750  -0.0570 98  TYR D OH  
13545 N N   . GLY D 99  ? 0.6561 0.3022 2.1145 0.0020  0.0743  -0.0943 99  GLY D N   
13546 C CA  . GLY D 99  ? 0.6721 0.2925 2.1321 0.0089  0.0718  -0.0993 99  GLY D CA  
13547 C C   . GLY D 99  ? 0.6961 0.3045 2.1591 -0.0009 0.0764  -0.1086 99  GLY D C   
13548 O O   . GLY D 99  ? 0.7068 0.2926 2.1723 0.0030  0.0753  -0.1145 99  GLY D O   
13549 N N   . ASP D 100 ? 0.6778 0.3012 2.1421 -0.0137 0.0809  -0.1100 100 ASP D N   
13550 C CA  . ASP D 100 ? 0.6801 0.2965 2.1493 -0.0244 0.0843  -0.1196 100 ASP D CA  
13551 C C   . ASP D 100 ? 0.6818 0.3143 2.1584 -0.0213 0.0829  -0.1356 100 ASP D C   
13552 O O   . ASP D 100 ? 0.6595 0.3205 2.1380 -0.0219 0.0825  -0.1391 100 ASP D O   
13553 C CB  . ASP D 100 ? 0.6555 0.2842 2.1261 -0.0385 0.0884  -0.1161 100 ASP D CB  
13554 C CG  . ASP D 100 ? 0.6684 0.2847 2.1455 -0.0509 0.0916  -0.1238 100 ASP D CG  
13555 O OD1 . ASP D 100 ? 0.6672 0.2718 2.1477 -0.0492 0.0901  -0.1351 100 ASP D OD1 
13556 O OD2 . ASP D 100 ? 0.6698 0.2879 2.1496 -0.0622 0.0958  -0.1187 100 ASP D OD2 
13557 N N   . PRO D 101 ? 0.7189 0.3325 2.1988 -0.0181 0.0826  -0.1461 101 PRO D N   
13558 C CA  . PRO D 101 ? 0.7313 0.3579 2.2159 -0.0154 0.0826  -0.1625 101 PRO D CA  
13559 C C   . PRO D 101 ? 0.7397 0.3893 2.2242 -0.0268 0.0832  -0.1695 101 PRO D C   
13560 O O   . PRO D 101 ? 0.7585 0.4296 2.2419 -0.0242 0.0830  -0.1779 101 PRO D O   
13561 C CB  . PRO D 101 ? 0.7447 0.3415 2.2324 -0.0142 0.0829  -0.1716 101 PRO D CB  
13562 C CG  . PRO D 101 ? 0.7567 0.3256 2.2411 -0.0095 0.0815  -0.1578 101 PRO D CG  
13563 C CD  . PRO D 101 ? 0.7447 0.3219 2.2226 -0.0172 0.0827  -0.1428 101 PRO D CD  
13564 N N   . GLU D 102 ? 0.7440 0.3886 2.2300 -0.0394 0.0840  -0.1656 102 GLU D N   
13565 C CA  . GLU D 102 ? 0.7472 0.4116 2.2356 -0.0504 0.0827  -0.1724 102 GLU D CA  
13566 C C   . GLU D 102 ? 0.6831 0.3780 2.1687 -0.0483 0.0813  -0.1660 102 GLU D C   
13567 O O   . GLU D 102 ? 0.6625 0.3776 2.1461 -0.0504 0.0788  -0.1741 102 GLU D O   
13568 C CB  . GLU D 102 ? 0.7977 0.4491 2.2926 -0.0638 0.0844  -0.1693 102 GLU D CB  
13569 C CG  . GLU D 102 ? 0.8261 0.4839 2.3275 -0.0751 0.0815  -0.1832 102 GLU D CG  
13570 C CD  . GLU D 102 ? 0.8316 0.4937 2.3440 -0.0893 0.0823  -0.1793 102 GLU D CD  
13571 O OE1 . GLU D 102 ? 0.8535 0.4941 2.3716 -0.0959 0.0872  -0.1739 102 GLU D OE1 
13572 O OE2 . GLU D 102 ? 0.8286 0.5163 2.3446 -0.0940 0.0780  -0.1817 102 GLU D OE2 
13573 N N   . PHE D 103 ? 0.6488 0.3453 2.1329 -0.0442 0.0826  -0.1514 103 PHE D N   
13574 C CA  . PHE D 103 ? 0.6092 0.3323 2.0916 -0.0422 0.0815  -0.1445 103 PHE D CA  
13575 C C   . PHE D 103 ? 0.5912 0.3281 2.0703 -0.0319 0.0806  -0.1507 103 PHE D C   
13576 O O   . PHE D 103 ? 0.5702 0.3301 2.0472 -0.0332 0.0794  -0.1535 103 PHE D O   
13577 C CB  . PHE D 103 ? 0.5965 0.3172 2.0769 -0.0393 0.0829  -0.1287 103 PHE D CB  
13578 C CG  . PHE D 103 ? 0.5867 0.3350 2.0671 -0.0391 0.0817  -0.1224 103 PHE D CG  
13579 C CD1 . PHE D 103 ? 0.5732 0.3406 2.0579 -0.0482 0.0804  -0.1250 103 PHE D CD1 
13580 C CD2 . PHE D 103 ? 0.5880 0.3433 2.0653 -0.0293 0.0809  -0.1148 103 PHE D CD2 
13581 C CE1 . PHE D 103 ? 0.5424 0.3336 2.0275 -0.0473 0.0789  -0.1195 103 PHE D CE1 
13582 C CE2 . PHE D 103 ? 0.5513 0.3308 2.0292 -0.0292 0.0799  -0.1098 103 PHE D CE2 
13583 C CZ  . PHE D 103 ? 0.5365 0.3331 2.0179 -0.0381 0.0791  -0.1118 103 PHE D CZ  
13584 N N   . VAL D 104 ? 0.5965 0.3186 2.0759 -0.0218 0.0815  -0.1530 104 VAL D N   
13585 C CA  . VAL D 104 ? 0.5841 0.3188 2.0637 -0.0119 0.0824  -0.1598 104 VAL D CA  
13586 C C   . VAL D 104 ? 0.5934 0.3376 2.0688 -0.0169 0.0833  -0.1745 104 VAL D C   
13587 O O   . VAL D 104 ? 0.6026 0.3674 2.0738 -0.0151 0.0845  -0.1778 104 VAL D O   
13588 C CB  . VAL D 104 ? 0.5870 0.3033 2.0715 0.0001  0.0828  -0.1617 104 VAL D CB  
13589 C CG1 . VAL D 104 ? 0.5767 0.3079 2.0650 0.0097  0.0855  -0.1704 104 VAL D CG1 
13590 C CG2 . VAL D 104 ? 0.5791 0.2841 2.0643 0.0053  0.0800  -0.1467 104 VAL D CG2 
13591 N N   . LYS D 105 ? 0.6113 0.3396 2.0865 -0.0237 0.0826  -0.1833 105 LYS D N   
13592 C CA  . LYS D 105 ? 0.6340 0.3674 2.1031 -0.0276 0.0826  -0.1989 105 LYS D CA  
13593 C C   . LYS D 105 ? 0.6049 0.3609 2.0678 -0.0363 0.0790  -0.1977 105 LYS D C   
13594 O O   . LYS D 105 ? 0.6079 0.3767 2.0610 -0.0358 0.0793  -0.2062 105 LYS D O   
13595 C CB  . LYS D 105 ? 0.6800 0.3886 2.1517 -0.0323 0.0820  -0.2092 105 LYS D CB  
13596 C CG  . LYS D 105 ? 0.7242 0.4324 2.1885 -0.0348 0.0820  -0.2279 105 LYS D CG  
13597 C CD  . LYS D 105 ? 0.7802 0.4644 2.2488 -0.0420 0.0801  -0.2373 105 LYS D CD  
13598 C CE  . LYS D 105 ? 0.8124 0.4933 2.2727 -0.0452 0.0792  -0.2569 105 LYS D CE  
13599 N NZ  . LYS D 105 ? 0.8332 0.4905 2.2999 -0.0528 0.0769  -0.2655 105 LYS D NZ  
13600 N N   . ASP D 106 ? 0.5806 0.3409 2.0487 -0.0442 0.0759  -0.1876 106 ASP D N   
13601 C CA  . ASP D 106 ? 0.5755 0.3572 2.0401 -0.0515 0.0712  -0.1864 106 ASP D CA  
13602 C C   . ASP D 106 ? 0.5422 0.3450 2.0012 -0.0449 0.0725  -0.1790 106 ASP D C   
13603 O O   . ASP D 106 ? 0.5389 0.3582 1.9893 -0.0475 0.0695  -0.1818 106 ASP D O   
13604 C CB  . ASP D 106 ? 0.5791 0.3622 2.0542 -0.0612 0.0682  -0.1783 106 ASP D CB  
13605 C CG  . ASP D 106 ? 0.6297 0.3934 2.1131 -0.0698 0.0675  -0.1846 106 ASP D CG  
13606 O OD1 . ASP D 106 ? 0.6558 0.4107 2.1356 -0.0720 0.0655  -0.1987 106 ASP D OD1 
13607 O OD2 . ASP D 106 ? 0.6718 0.4290 2.1652 -0.0749 0.0696  -0.1756 106 ASP D OD2 
13608 N N   . SER D 107 ? 0.5045 0.3053 1.9682 -0.0365 0.0764  -0.1693 107 SER D N   
13609 C CA  . SER D 107 ? 0.4649 0.2838 1.9264 -0.0301 0.0781  -0.1621 107 SER D CA  
13610 C C   . SER D 107 ? 0.4722 0.2983 1.9246 -0.0253 0.0815  -0.1727 107 SER D C   
13611 O O   . SER D 107 ? 0.4622 0.3049 1.9056 -0.0278 0.0807  -0.1734 107 SER D O   
13612 C CB  . SER D 107 ? 0.4489 0.2608 1.9177 -0.0223 0.0802  -0.1518 107 SER D CB  
13613 O OG  . SER D 107 ? 0.4330 0.2428 1.9062 -0.0271 0.0782  -0.1402 107 SER D OG  
13614 N N   . GLU D 108 ? 0.4938 0.3063 1.9481 -0.0187 0.0858  -0.1816 108 GLU D N   
13615 C CA  . GLU D 108 ? 0.5065 0.3235 1.9529 -0.0143 0.0912  -0.1938 108 GLU D CA  
13616 C C   . GLU D 108 ? 0.5127 0.3384 1.9427 -0.0229 0.0885  -0.2012 108 GLU D C   
13617 O O   . GLU D 108 ? 0.5073 0.3476 1.9265 -0.0219 0.0917  -0.2023 108 GLU D O   
13618 C CB  . GLU D 108 ? 0.5328 0.3297 1.9835 -0.0089 0.0948  -0.2059 108 GLU D CB  
13619 C CG  . GLU D 108 ? 0.5335 0.3206 1.9994 0.0018  0.0968  -0.2006 108 GLU D CG  
13620 C CD  . GLU D 108 ? 0.5694 0.3364 2.0416 0.0084  0.0999  -0.2128 108 GLU D CD  
13621 O OE1 . GLU D 108 ? 0.6078 0.3646 2.0728 0.0039  0.1007  -0.2260 108 GLU D OE1 
13622 O OE2 . GLU D 108 ? 0.5680 0.3286 2.0530 0.0186  0.1007  -0.2093 108 GLU D OE2 
13623 N N   . ILE D 109 ? 0.5223 0.3382 1.9505 -0.0315 0.0823  -0.2061 109 ILE D N   
13624 C CA  . ILE D 109 ? 0.5382 0.3569 1.9506 -0.0391 0.0779  -0.2167 109 ILE D CA  
13625 C C   . ILE D 109 ? 0.5198 0.3587 1.9246 -0.0434 0.0728  -0.2078 109 ILE D C   
13626 O O   . ILE D 109 ? 0.5354 0.3814 1.9218 -0.0458 0.0714  -0.2140 109 ILE D O   
13627 C CB  . ILE D 109 ? 0.5571 0.3606 1.9742 -0.0475 0.0714  -0.2240 109 ILE D CB  
13628 C CG1 . ILE D 109 ? 0.5770 0.3585 1.9968 -0.0436 0.0762  -0.2366 109 ILE D CG1 
13629 C CG2 . ILE D 109 ? 0.5667 0.3774 1.9702 -0.0567 0.0626  -0.2314 109 ILE D CG2 
13630 C CD1 . ILE D 109 ? 0.5847 0.3479 2.0157 -0.0507 0.0716  -0.2397 109 ILE D CD1 
13631 N N   . GLU D 110 ? 0.4931 0.3391 1.9110 -0.0444 0.0701  -0.1935 110 GLU D N   
13632 C CA  . GLU D 110 ? 0.4767 0.3407 1.8919 -0.0484 0.0645  -0.1839 110 GLU D CA  
13633 C C   . GLU D 110 ? 0.4710 0.3482 1.8776 -0.0419 0.0704  -0.1788 110 GLU D C   
13634 O O   . GLU D 110 ? 0.4754 0.3646 1.8689 -0.0446 0.0672  -0.1769 110 GLU D O   
13635 C CB  . GLU D 110 ? 0.4519 0.3170 1.8853 -0.0514 0.0614  -0.1719 110 GLU D CB  
13636 C CG  . GLU D 110 ? 0.4275 0.3110 1.8626 -0.0540 0.0566  -0.1608 110 GLU D CG  
13637 C CD  . GLU D 110 ? 0.4351 0.3285 1.8588 -0.0602 0.0476  -0.1651 110 GLU D CD  
13638 O OE1 . GLU D 110 ? 0.4474 0.3342 1.8612 -0.0644 0.0430  -0.1771 110 GLU D OE1 
13639 O OE2 . GLU D 110 ? 0.4292 0.3372 1.8530 -0.0603 0.0444  -0.1556 110 GLU D OE2 
13640 N N   . LEU D 111 ? 0.4664 0.3405 1.8812 -0.0335 0.0786  -0.1766 111 LEU D N   
13641 C CA  . LEU D 111 ? 0.4546 0.3413 1.8663 -0.0273 0.0853  -0.1721 111 LEU D CA  
13642 C C   . LEU D 111 ? 0.4768 0.3641 1.8695 -0.0270 0.0908  -0.1841 111 LEU D C   
13643 O O   . LEU D 111 ? 0.4801 0.3793 1.8598 -0.0281 0.0927  -0.1812 111 LEU D O   
13644 C CB  . LEU D 111 ? 0.4418 0.3245 1.8701 -0.0184 0.0911  -0.1680 111 LEU D CB  
13645 C CG  . LEU D 111 ? 0.4323 0.3296 1.8640 -0.0122 0.0974  -0.1621 111 LEU D CG  
13646 C CD1 . LEU D 111 ? 0.4158 0.3297 1.8411 -0.0163 0.0946  -0.1519 111 LEU D CD1 
13647 C CD2 . LEU D 111 ? 0.4244 0.3173 1.8750 -0.0048 0.0978  -0.1552 111 LEU D CD2 
13648 N N   . LYS D 112 ? 0.5011 0.3739 1.8909 -0.0259 0.0937  -0.1977 112 LYS D N   
13649 C CA  . LYS D 112 ? 0.5304 0.4017 1.9003 -0.0257 0.1002  -0.2108 112 LYS D CA  
13650 C C   . LYS D 112 ? 0.5497 0.4258 1.8968 -0.0344 0.0921  -0.2116 112 LYS D C   
13651 O O   . LYS D 112 ? 0.5715 0.4523 1.8970 -0.0350 0.0969  -0.2157 112 LYS D O   
13652 C CB  . LYS D 112 ? 0.5498 0.4035 1.9215 -0.0231 0.1042  -0.2262 112 LYS D CB  
13653 C CG  . LYS D 112 ? 0.5458 0.3951 1.9375 -0.0127 0.1130  -0.2271 112 LYS D CG  
13654 C CD  . LYS D 112 ? 0.5700 0.4007 1.9650 -0.0092 0.1169  -0.2428 112 LYS D CD  
13655 C CE  . LYS D 112 ? 0.5648 0.3874 1.9838 0.0008  0.1206  -0.2415 112 LYS D CE  
13656 N NZ  . LYS D 112 ? 0.5937 0.3955 2.0161 0.0031  0.1220  -0.2557 112 LYS D NZ  
13657 N N   . ARG D 113 ? 0.5451 0.4199 1.8974 -0.0411 0.0799  -0.2075 113 ARG D N   
13658 C CA  . ARG D 113 ? 0.5561 0.4339 1.8897 -0.0490 0.0693  -0.2098 113 ARG D CA  
13659 C C   . ARG D 113 ? 0.5468 0.4401 1.8698 -0.0491 0.0687  -0.1982 113 ARG D C   
13660 O O   . ARG D 113 ? 0.5613 0.4557 1.8582 -0.0517 0.0673  -0.2023 113 ARG D O   
13661 C CB  . ARG D 113 ? 0.5458 0.4218 1.8921 -0.0563 0.0561  -0.2077 113 ARG D CB  
13662 C CG  . ARG D 113 ? 0.5626 0.4424 1.8893 -0.0635 0.0437  -0.2113 113 ARG D CG  
13663 C CD  . ARG D 113 ? 0.5504 0.4306 1.8933 -0.0710 0.0303  -0.2105 113 ARG D CD  
13664 N NE  . ARG D 113 ? 0.5147 0.4052 1.8813 -0.0701 0.0304  -0.1953 113 ARG D NE  
13665 C CZ  . ARG D 113 ? 0.5068 0.4117 1.8718 -0.0696 0.0268  -0.1837 113 ARG D CZ  
13666 N NH1 . ARG D 113 ? 0.5279 0.4376 1.8687 -0.0705 0.0217  -0.1846 113 ARG D NH1 
13667 N NH2 . ARG D 113 ? 0.4802 0.3932 1.8662 -0.0683 0.0282  -0.1711 113 ARG D NH2 
13668 N N   . VAL D 114 ? 0.5297 0.4329 1.8723 -0.0464 0.0692  -0.1840 114 VAL D N   
13669 C CA  . VAL D 114 ? 0.5281 0.4456 1.8661 -0.0458 0.0693  -0.1715 114 VAL D CA  
13670 C C   . VAL D 114 ? 0.5518 0.4714 1.8738 -0.0415 0.0821  -0.1746 114 VAL D C   
13671 O O   . VAL D 114 ? 0.5706 0.4940 1.8693 -0.0443 0.0816  -0.1734 114 VAL D O   
13672 C CB  . VAL D 114 ? 0.4953 0.4207 1.8587 -0.0426 0.0698  -0.1580 114 VAL D CB  
13673 C CG1 . VAL D 114 ? 0.4825 0.4213 1.8433 -0.0403 0.0733  -0.1464 114 VAL D CG1 
13674 C CG2 . VAL D 114 ? 0.4906 0.4164 1.8685 -0.0478 0.0586  -0.1531 114 VAL D CG2 
13675 N N   . LEU D 115 ? 0.5564 0.4725 1.8914 -0.0349 0.0934  -0.1792 115 LEU D N   
13676 C CA  . LEU D 115 ? 0.5579 0.4779 1.8865 -0.0300 0.1078  -0.1822 115 LEU D CA  
13677 C C   . LEU D 115 ? 0.5835 0.4976 1.8801 -0.0337 0.1115  -0.1934 115 LEU D C   
13678 O O   . LEU D 115 ? 0.6034 0.5218 1.8868 -0.0324 0.1230  -0.1944 115 LEU D O   
13679 C CB  . LEU D 115 ? 0.5526 0.4676 1.9029 -0.0222 0.1168  -0.1882 115 LEU D CB  
13680 C CG  . LEU D 115 ? 0.5325 0.4541 1.9108 -0.0169 0.1159  -0.1764 115 LEU D CG  
13681 C CD1 . LEU D 115 ? 0.5404 0.4558 1.9374 -0.0083 0.1239  -0.1835 115 LEU D CD1 
13682 C CD2 . LEU D 115 ? 0.5240 0.4612 1.9038 -0.0164 0.1191  -0.1645 115 LEU D CD2 
13683 N N   . ASN D 116 ? 0.5934 0.4970 1.8766 -0.0388 0.1020  -0.2022 116 ASN D N   
13684 C CA  . ASN D 116 ? 0.6236 0.5184 1.8748 -0.0418 0.1056  -0.2153 116 ASN D CA  
13685 C C   . ASN D 116 ? 0.6167 0.5174 1.8393 -0.0465 0.1022  -0.2076 116 ASN D C   
13686 O O   . ASN D 116 ? 0.6408 0.5362 1.8333 -0.0479 0.1101  -0.2151 116 ASN D O   
13687 C CB  . ASN D 116 ? 0.6444 0.5253 1.8917 -0.0456 0.0961  -0.2283 116 ASN D CB  
13688 C CG  . ASN D 116 ? 0.6932 0.5627 1.9093 -0.0471 0.1024  -0.2448 116 ASN D CG  
13689 O OD1 . ASN D 116 ? 0.7336 0.5964 1.9250 -0.0535 0.0913  -0.2506 116 ASN D OD1 
13690 N ND2 . ASN D 116 ? 0.7095 0.5770 1.9261 -0.0413 0.1199  -0.2528 116 ASN D ND2 
13691 N N   . TYR D 117 ? 0.5844 0.4946 1.8153 -0.0488 0.0910  -0.1928 117 TYR D N   
13692 C CA  . TYR D 117 ? 0.5914 0.5066 1.7978 -0.0524 0.0873  -0.1834 117 TYR D CA  
13693 C C   . TYR D 117 ? 0.5629 0.4912 1.7853 -0.0489 0.0953  -0.1686 117 TYR D C   
13694 O O   . TYR D 117 ? 0.5738 0.5044 1.7764 -0.0497 0.1033  -0.1638 117 TYR D O   
13695 C CB  . TYR D 117 ? 0.5929 0.5071 1.7922 -0.0583 0.0662  -0.1798 117 TYR D CB  
13696 C CG  . TYR D 117 ? 0.5548 0.4773 1.7891 -0.0581 0.0559  -0.1707 117 TYR D CG  
13697 C CD1 . TYR D 117 ? 0.5299 0.4646 1.7792 -0.0566 0.0547  -0.1550 117 TYR D CD1 
13698 C CD2 . TYR D 117 ? 0.5479 0.4651 1.7998 -0.0599 0.0483  -0.1784 117 TYR D CD2 
13699 C CE1 . TYR D 117 ? 0.5016 0.4430 1.7815 -0.0565 0.0470  -0.1477 117 TYR D CE1 
13700 C CE2 . TYR D 117 ? 0.5188 0.4425 1.8014 -0.0603 0.0412  -0.1705 117 TYR D CE2 
13701 C CZ  . TYR D 117 ? 0.4980 0.4338 1.7939 -0.0585 0.0407  -0.1554 117 TYR D CZ  
13702 O OH  . TYR D 117 ? 0.4766 0.4179 1.8011 -0.0592 0.0349  -0.1487 117 TYR D OH  
13703 N N   . ALA D 118 ? 0.5264 0.4620 1.7836 -0.0452 0.0939  -0.1617 118 ALA D N   
13704 C CA  . ALA D 118 ? 0.5012 0.4490 1.7758 -0.0420 0.0994  -0.1483 118 ALA D CA  
13705 C C   . ALA D 118 ? 0.5232 0.4736 1.7907 -0.0390 0.1176  -0.1506 118 ALA D C   
13706 O O   . ALA D 118 ? 0.5195 0.4786 1.7883 -0.0388 0.1229  -0.1401 118 ALA D O   
13707 C CB  . ALA D 118 ? 0.4661 0.4176 1.7759 -0.0377 0.0977  -0.1447 118 ALA D CB  
13708 N N   . LYS D 119 ? 0.5561 0.4988 1.8179 -0.0369 0.1280  -0.1651 119 LYS D N   
13709 C CA  . LYS D 119 ? 0.5712 0.5173 1.8338 -0.0332 0.1473  -0.1697 119 LYS D CA  
13710 C C   . LYS D 119 ? 0.5983 0.5435 1.8266 -0.0382 0.1548  -0.1672 119 LYS D C   
13711 O O   . LYS D 119 ? 0.6123 0.5596 1.8379 -0.0365 0.1727  -0.1721 119 LYS D O   
13712 C CB  . LYS D 119 ? 0.5950 0.5320 1.8597 -0.0295 0.1565  -0.1873 119 LYS D CB  
13713 C CG  . LYS D 119 ? 0.6405 0.5640 1.8688 -0.0342 0.1569  -0.2003 119 LYS D CG  
13714 C CD  . LYS D 119 ? 0.6650 0.5799 1.8979 -0.0298 0.1683  -0.2184 119 LYS D CD  
13715 C CE  . LYS D 119 ? 0.7206 0.6216 1.9149 -0.0346 0.1697  -0.2320 119 LYS D CE  
13716 N NZ  . LYS D 119 ? 0.7475 0.6412 1.9453 -0.0299 0.1849  -0.2499 119 LYS D NZ  
13717 N N   . LYS D 120 ? 0.6080 0.5492 1.8105 -0.0442 0.1415  -0.1605 120 LYS D N   
13718 C CA  . LYS D 120 ? 0.6339 0.5710 1.7991 -0.0492 0.1466  -0.1566 120 LYS D CA  
13719 C C   . LYS D 120 ? 0.6046 0.5506 1.7748 -0.0509 0.1413  -0.1381 120 LYS D C   
13720 O O   . LYS D 120 ? 0.6208 0.5629 1.7614 -0.0551 0.1442  -0.1315 120 LYS D O   
13721 C CB  . LYS D 120 ? 0.6750 0.5980 1.8023 -0.0545 0.1344  -0.1635 120 LYS D CB  
13722 C CG  . LYS D 120 ? 0.6994 0.6120 1.8213 -0.0535 0.1371  -0.1826 120 LYS D CG  
13723 C CD  . LYS D 120 ? 0.7453 0.6436 1.8282 -0.0591 0.1241  -0.1904 120 LYS D CD  
13724 C CE  . LYS D 120 ? 0.7365 0.6361 1.8249 -0.0621 0.0992  -0.1827 120 LYS D CE  
13725 N NZ  . LYS D 120 ? 0.7759 0.6618 1.8277 -0.0673 0.0855  -0.1913 120 LYS D NZ  
13726 N N   . TYR D 121 ? 0.5613 0.5176 1.7674 -0.0475 0.1338  -0.1298 121 TYR D N   
13727 C CA  . TYR D 121 ? 0.5488 0.5129 1.7621 -0.0488 0.1270  -0.1132 121 TYR D CA  
13728 C C   . TYR D 121 ? 0.5273 0.5034 1.7718 -0.0445 0.1397  -0.1080 121 TYR D C   
13729 O O   . TYR D 121 ? 0.4938 0.4767 1.7712 -0.0401 0.1358  -0.1070 121 TYR D O   
13730 C CB  . TYR D 121 ? 0.5277 0.4920 1.7504 -0.0498 0.1056  -0.1090 121 TYR D CB  
13731 C CG  . TYR D 121 ? 0.5587 0.5115 1.7475 -0.0547 0.0936  -0.1142 121 TYR D CG  
13732 C CD1 . TYR D 121 ? 0.5832 0.5311 1.7411 -0.0589 0.0872  -0.1058 121 TYR D CD1 
13733 C CD2 . TYR D 121 ? 0.5688 0.5141 1.7551 -0.0551 0.0884  -0.1280 121 TYR D CD2 
13734 C CE1 . TYR D 121 ? 0.6147 0.5513 1.7403 -0.0629 0.0743  -0.1110 121 TYR D CE1 
13735 C CE2 . TYR D 121 ? 0.5980 0.5326 1.7536 -0.0596 0.0764  -0.1341 121 TYR D CE2 
13736 C CZ  . TYR D 121 ? 0.6211 0.5515 1.7458 -0.0634 0.0688  -0.1256 121 TYR D CZ  
13737 O OH  . TYR D 121 ? 0.6505 0.5696 1.7439 -0.0675 0.0553  -0.1320 121 TYR D OH  
13738 N N   . ASP D 122 ? 0.5477 0.5257 1.7808 -0.0463 0.1546  -0.1044 122 ASP D N   
13739 C CA  . ASP D 122 ? 0.5325 0.5222 1.7957 -0.0428 0.1678  -0.1013 122 ASP D CA  
13740 C C   . ASP D 122 ? 0.5047 0.5033 1.7910 -0.0419 0.1574  -0.0869 122 ASP D C   
13741 O O   . ASP D 122 ? 0.4929 0.5016 1.8077 -0.0387 0.1647  -0.0842 122 ASP D O   
13742 C CB  . ASP D 122 ? 0.5517 0.5417 1.8006 -0.0455 0.1885  -0.1025 122 ASP D CB  
13743 C CG  . ASP D 122 ? 0.5685 0.5548 1.7910 -0.0519 0.1890  -0.0891 122 ASP D CG  
13744 O OD1 . ASP D 122 ? 0.5570 0.5430 1.7789 -0.0531 0.1723  -0.0775 122 ASP D OD1 
13745 O OD2 . ASP D 122 ? 0.5933 0.5758 1.7951 -0.0556 0.2064  -0.0907 122 ASP D OD2 
13746 N N   . CYS D 123 ? 0.4953 0.4906 1.7719 -0.0445 0.1401  -0.0788 123 CYS D N   
13747 C CA  . CYS D 123 ? 0.4698 0.4732 1.7705 -0.0430 0.1306  -0.0670 123 CYS D CA  
13748 C C   . CYS D 123 ? 0.4385 0.4482 1.7740 -0.0372 0.1281  -0.0711 123 CYS D C   
13749 O O   . CYS D 123 ? 0.4167 0.4342 1.7761 -0.0350 0.1256  -0.0634 123 CYS D O   
13750 C CB  . CYS D 123 ? 0.4808 0.4800 1.7674 -0.0463 0.1127  -0.0586 123 CYS D CB  
13751 S SG  . CYS D 123 ? 0.4966 0.4895 1.7800 -0.0464 0.0967  -0.0676 123 CYS D SG  
13752 N N   . ILE D 124 ? 0.4404 0.4453 1.7779 -0.0348 0.1285  -0.0830 124 ILE D N   
13753 C CA  . ILE D 124 ? 0.4213 0.4293 1.7888 -0.0292 0.1259  -0.0861 124 ILE D CA  
13754 C C   . ILE D 124 ? 0.4231 0.4390 1.8129 -0.0244 0.1390  -0.0880 124 ILE D C   
13755 O O   . ILE D 124 ? 0.4573 0.4735 1.8417 -0.0240 0.1528  -0.0954 124 ILE D O   
13756 C CB  . ILE D 124 ? 0.4314 0.4301 1.7948 -0.0282 0.1219  -0.0977 124 ILE D CB  
13757 C CG1 . ILE D 124 ? 0.4425 0.4347 1.7871 -0.0335 0.1080  -0.0966 124 ILE D CG1 
13758 C CG2 . ILE D 124 ? 0.4083 0.4075 1.8004 -0.0225 0.1193  -0.0995 124 ILE D CG2 
13759 C CD1 . ILE D 124 ? 0.4572 0.4392 1.7941 -0.0340 0.1048  -0.1092 124 ILE D CD1 
13760 N N   . ILE D 125 ? 0.3900 0.4124 1.8063 -0.0207 0.1346  -0.0819 125 ILE D N   
13761 C CA  . ILE D 125 ? 0.3745 0.4053 1.8146 -0.0160 0.1443  -0.0834 125 ILE D CA  
13762 C C   . ILE D 125 ? 0.3473 0.3771 1.8120 -0.0091 0.1386  -0.0868 125 ILE D C   
13763 O O   . ILE D 125 ? 0.3677 0.4039 1.8547 -0.0041 0.1444  -0.0893 125 ILE D O   
13764 C CB  . ILE D 125 ? 0.3650 0.4051 1.8132 -0.0182 0.1462  -0.0722 125 ILE D CB  
13765 C CG1 . ILE D 125 ? 0.3445 0.3854 1.8005 -0.0185 0.1323  -0.0621 125 ILE D CG1 
13766 C CG2 . ILE D 125 ? 0.3866 0.4259 1.8099 -0.0248 0.1546  -0.0688 125 ILE D CG2 
13767 C CD1 . ILE D 125 ? 0.3411 0.3899 1.8066 -0.0203 0.1335  -0.0518 125 ILE D CD1 
13768 N N   . THR D 126 ? 0.3246 0.3463 1.7865 -0.0090 0.1273  -0.0864 126 THR D N   
13769 C CA  . THR D 126 ? 0.3148 0.3323 1.7958 -0.0028 0.1221  -0.0887 126 THR D CA  
13770 C C   . THR D 126 ? 0.3315 0.3374 1.8031 -0.0047 0.1127  -0.0902 126 THR D C   
13771 O O   . THR D 126 ? 0.3316 0.3373 1.7953 -0.0094 0.1051  -0.0834 126 THR D O   
13772 C CB  . THR D 126 ? 0.2879 0.3121 1.7872 -0.0005 0.1171  -0.0795 126 THR D CB  
13773 O OG1 . THR D 126 ? 0.2866 0.3215 1.8000 0.0016  0.1254  -0.0793 126 THR D OG1 
13774 C CG2 . THR D 126 ? 0.2791 0.2965 1.7936 0.0056  0.1102  -0.0802 126 THR D CG2 
13775 N N   . TYR D 127 ? 0.3406 0.3366 1.8151 -0.0010 0.1132  -0.0991 127 TYR D N   
13776 C CA  . TYR D 127 ? 0.3466 0.3307 1.8158 -0.0030 0.1050  -0.1004 127 TYR D CA  
13777 C C   . TYR D 127 ? 0.3467 0.3255 1.8317 0.0013  0.0990  -0.0952 127 TYR D C   
13778 O O   . TYR D 127 ? 0.3343 0.3117 1.8332 0.0084  0.1013  -0.0977 127 TYR D O   
13779 C CB  . TYR D 127 ? 0.3592 0.3326 1.8212 -0.0021 0.1087  -0.1129 127 TYR D CB  
13780 C CG  . TYR D 127 ? 0.3700 0.3436 1.8099 -0.0076 0.1126  -0.1193 127 TYR D CG  
13781 C CD1 . TYR D 127 ? 0.3838 0.3644 1.8171 -0.0071 0.1233  -0.1231 127 TYR D CD1 
13782 C CD2 . TYR D 127 ? 0.3728 0.3388 1.7980 -0.0134 0.1057  -0.1222 127 TYR D CD2 
13783 C CE1 . TYR D 127 ? 0.4036 0.3819 1.8122 -0.0122 0.1271  -0.1290 127 TYR D CE1 
13784 C CE2 . TYR D 127 ? 0.3937 0.3583 1.7961 -0.0182 0.1075  -0.1284 127 TYR D CE2 
13785 C CZ  . TYR D 127 ? 0.4039 0.3738 1.7958 -0.0176 0.1182  -0.1316 127 TYR D CZ  
13786 O OH  . TYR D 127 ? 0.4232 0.3893 1.7883 -0.0226 0.1196  -0.1376 127 TYR D OH  
13787 N N   . LEU D 128 ? 0.3450 0.3205 1.8276 -0.0028 0.0912  -0.0885 128 LEU D N   
13788 C CA  . LEU D 128 ? 0.3449 0.3114 1.8366 0.0000  0.0861  -0.0840 128 LEU D CA  
13789 C C   . LEU D 128 ? 0.4033 0.3540 1.8902 -0.0015 0.0842  -0.0898 128 LEU D C   
13790 O O   . LEU D 128 ? 0.4806 0.4290 1.9590 -0.0082 0.0818  -0.0914 128 LEU D O   
13791 C CB  . LEU D 128 ? 0.3153 0.2868 1.8092 -0.0032 0.0811  -0.0738 128 LEU D CB  
13792 C CG  . LEU D 128 ? 0.3050 0.2910 1.8042 -0.0023 0.0824  -0.0676 128 LEU D CG  
13793 C CD1 . LEU D 128 ? 0.2808 0.2711 1.7822 -0.0055 0.0775  -0.0584 128 LEU D CD1 
13794 C CD2 . LEU D 128 ? 0.3062 0.2944 1.8184 0.0052  0.0848  -0.0683 128 LEU D CD2 
13795 N N   . VAL D 129 ? 0.4249 0.3639 1.9183 0.0047  0.0847  -0.0933 129 VAL D N   
13796 C CA  . VAL D 129 ? 0.4317 0.3541 1.9211 0.0039  0.0842  -0.0999 129 VAL D CA  
13797 C C   . VAL D 129 ? 0.4295 0.3400 1.9174 -0.0002 0.0794  -0.0938 129 VAL D C   
13798 O O   . VAL D 129 ? 0.4947 0.3926 1.9785 -0.0041 0.0789  -0.0983 129 VAL D O   
13799 C CB  . VAL D 129 ? 0.4481 0.3626 1.9463 0.0131  0.0865  -0.1058 129 VAL D CB  
13800 C CG1 . VAL D 129 ? 0.4623 0.3556 1.9621 0.0159  0.0824  -0.1048 129 VAL D CG1 
13801 C CG2 . VAL D 129 ? 0.4722 0.3893 1.9674 0.0138  0.0931  -0.1178 129 VAL D CG2 
13802 N N   . ILE D 130 ? 0.4017 0.3149 1.8931 0.0005  0.0767  -0.0841 130 ILE D N   
13803 C CA  . ILE D 130 ? 0.4091 0.3103 1.8983 -0.0034 0.0743  -0.0782 130 ILE D CA  
13804 C C   . ILE D 130 ? 0.4243 0.3337 1.9158 -0.0034 0.0725  -0.0685 130 ILE D C   
13805 O O   . ILE D 130 ? 0.4367 0.3562 1.9330 0.0018  0.0719  -0.0663 130 ILE D O   
13806 C CB  . ILE D 130 ? 0.4183 0.2974 1.9065 0.0013  0.0735  -0.0788 130 ILE D CB  
13807 C CG1 . ILE D 130 ? 0.4249 0.2893 1.9081 -0.0046 0.0732  -0.0736 130 ILE D CG1 
13808 C CG2 . ILE D 130 ? 0.4257 0.3034 1.9189 0.0111  0.0709  -0.0753 130 ILE D CG2 
13809 C CD1 . ILE D 130 ? 0.4491 0.2887 1.9285 -0.0030 0.0733  -0.0759 130 ILE D CD1 
13810 N N   . ASN D 131 ? 0.4424 0.3469 1.9318 -0.0093 0.0721  -0.0634 131 ASN D N   
13811 C CA  . ASN D 131 ? 0.4384 0.3496 1.9294 -0.0097 0.0711  -0.0552 131 ASN D CA  
13812 C C   . ASN D 131 ? 0.4454 0.3384 1.9308 -0.0100 0.0716  -0.0498 131 ASN D C   
13813 O O   . ASN D 131 ? 0.4941 0.3732 1.9759 -0.0147 0.0739  -0.0510 131 ASN D O   
13814 C CB  . ASN D 131 ? 0.4451 0.3715 1.9396 -0.0168 0.0711  -0.0541 131 ASN D CB  
13815 C CG  . ASN D 131 ? 0.4554 0.3919 1.9536 -0.0159 0.0702  -0.0470 131 ASN D CG  
13816 O OD1 . ASN D 131 ? 0.4134 0.3587 1.9140 -0.0108 0.0690  -0.0454 131 ASN D OD1 
13817 N ND2 . ASN D 131 ? 0.4623 0.3976 1.9623 -0.0210 0.0713  -0.0432 131 ASN D ND2 
13818 N N   . GLU D 132 ? 0.4379 0.3302 1.9216 -0.0051 0.0696  -0.0439 132 GLU D N   
13819 C CA  . GLU D 132 ? 0.4664 0.3409 1.9406 -0.0046 0.0698  -0.0379 132 GLU D CA  
13820 C C   . GLU D 132 ? 0.4627 0.3140 1.9286 -0.0063 0.0717  -0.0390 132 GLU D C   
13821 O O   . GLU D 132 ? 0.4733 0.3150 1.9347 -0.0134 0.0765  -0.0368 132 GLU D O   
13822 C CB  . GLU D 132 ? 0.5149 0.3946 1.9889 -0.0110 0.0731  -0.0332 132 GLU D CB  
13823 C CG  . GLU D 132 ? 0.5843 0.4836 2.0656 -0.0088 0.0707  -0.0312 132 GLU D CG  
13824 C CD  . GLU D 132 ? 0.6429 0.5423 2.1217 -0.0116 0.0729  -0.0259 132 GLU D CD  
13825 O OE1 . GLU D 132 ? 0.6422 0.5362 2.1198 -0.0185 0.0784  -0.0251 132 GLU D OE1 
13826 O OE2 . GLU D 132 ? 0.6418 0.5474 2.1214 -0.0070 0.0695  -0.0233 132 GLU D OE2 
13827 N N   . PRO D 133 ? 0.4617 0.3022 1.9263 0.0007  0.0683  -0.0421 133 PRO D N   
13828 C CA  . PRO D 133 ? 0.4781 0.2915 1.9322 0.0013  0.0686  -0.0407 133 PRO D CA  
13829 C C   . PRO D 133 ? 0.4931 0.2905 1.9331 0.0041  0.0664  -0.0320 133 PRO D C   
13830 O O   . PRO D 133 ? 0.5190 0.3216 1.9589 0.0111  0.0606  -0.0294 133 PRO D O   
13831 C CB  . PRO D 133 ? 0.4932 0.3028 1.9527 0.0098  0.0643  -0.0468 133 PRO D CB  
13832 C CG  . PRO D 133 ? 0.4737 0.3104 1.9467 0.0126  0.0635  -0.0518 133 PRO D CG  
13833 C CD  . PRO D 133 ? 0.4639 0.3166 1.9376 0.0087  0.0643  -0.0465 133 PRO D CD  
13834 N N   . GLN D 134 ? 0.5112 0.2879 1.9386 -0.0019 0.0714  -0.0277 134 GLN D N   
13835 C CA  . GLN D 134 ? 0.5359 0.2928 1.9444 -0.0004 0.0707  -0.0192 134 GLN D CA  
13836 C C   . GLN D 134 ? 0.5312 0.2632 1.9281 0.0089  0.0628  -0.0167 134 GLN D C   
13837 O O   . GLN D 134 ? 0.5219 0.2488 1.9256 0.0125  0.0603  -0.0216 134 GLN D O   
13838 C CB  . GLN D 134 ? 0.5619 0.3086 1.9630 -0.0118 0.0814  -0.0160 134 GLN D CB  
13839 C CG  . GLN D 134 ? 0.5575 0.3227 1.9632 -0.0171 0.0863  -0.0145 134 GLN D CG  
13840 C CD  . GLN D 134 ? 0.6073 0.3640 1.9965 -0.0123 0.0833  -0.0079 134 GLN D CD  
13841 O OE1 . GLN D 134 ? 0.6304 0.3676 2.0041 -0.0047 0.0763  -0.0042 134 GLN D OE1 
13842 N NE2 . GLN D 134 ? 0.6317 0.4026 2.0243 -0.0162 0.0877  -0.0069 134 GLN D NE2 
13843 N N   . THR D 135 ? 0.5185 0.2339 1.8966 0.0129  0.0585  -0.0092 135 THR D N   
13844 C CA  . THR D 135 ? 0.5186 0.2112 1.8847 0.0232  0.0479  -0.0058 135 THR D CA  
13845 C C   . THR D 135 ? 0.5442 0.2024 1.8913 0.0200  0.0515  -0.0009 135 THR D C   
13846 O O   . THR D 135 ? 0.5570 0.2011 1.9066 0.0257  0.0463  -0.0029 135 THR D O   
13847 C CB  . THR D 135 ? 0.5244 0.2156 1.8777 0.0282  0.0409  -0.0002 135 THR D CB  
13848 O OG1 . THR D 135 ? 0.5066 0.2301 1.8825 0.0314  0.0376  -0.0060 135 THR D OG1 
13849 C CG2 . THR D 135 ? 0.5478 0.2108 1.8829 0.0382  0.0286  0.0051  135 THR D CG2 
13850 N N   . ASP D 136 ? 0.5521 0.1964 1.8814 0.0105  0.0612  0.0051  136 ASP D N   
13851 C CA  . ASP D 136 ? 0.5773 0.1883 1.8882 0.0053  0.0671  0.0104  136 ASP D CA  
13852 C C   . ASP D 136 ? 0.5765 0.1898 1.9056 0.0016  0.0711  0.0031  136 ASP D C   
13853 O O   . ASP D 136 ? 0.5940 0.1797 1.9140 0.0027  0.0701  0.0052  136 ASP D O   
13854 C CB  . ASP D 136 ? 0.5831 0.1839 1.8766 -0.0059 0.0802  0.0164  136 ASP D CB  
13855 C CG  . ASP D 136 ? 0.6189 0.1856 1.8943 -0.0136 0.0893  0.0220  136 ASP D CG  
13856 O OD1 . ASP D 136 ? 0.6084 0.1801 1.8994 -0.0230 0.0990  0.0172  136 ASP D OD1 
13857 O OD2 . ASP D 136 ? 0.6558 0.1900 1.9011 -0.0102 0.0861  0.0311  136 ASP D OD2 
13858 N N   . HIS D 137 ? 0.5463 0.1914 1.9000 -0.0029 0.0751  -0.0054 137 HIS D N   
13859 C CA  . HIS D 137 ? 0.5439 0.1935 1.9140 -0.0077 0.0791  -0.0135 137 HIS D CA  
13860 C C   . HIS D 137 ? 0.5433 0.1881 1.9208 0.0032  0.0695  -0.0186 137 HIS D C   
13861 O O   . HIS D 137 ? 0.5633 0.1891 1.9407 0.0020  0.0708  -0.0211 137 HIS D O   
13862 C CB  . HIS D 137 ? 0.5205 0.2051 1.9126 -0.0137 0.0832  -0.0214 137 HIS D CB  
13863 C CG  . HIS D 137 ? 0.5268 0.2166 1.9342 -0.0180 0.0855  -0.0308 137 HIS D CG  
13864 N ND1 . HIS D 137 ? 0.5516 0.2238 1.9574 -0.0275 0.0928  -0.0314 137 HIS D ND1 
13865 C CD2 . HIS D 137 ? 0.5210 0.2298 1.9442 -0.0145 0.0816  -0.0402 137 HIS D CD2 
13866 C CE1 . HIS D 137 ? 0.5566 0.2373 1.9771 -0.0292 0.0920  -0.0415 137 HIS D CE1 
13867 N NE2 . HIS D 137 ? 0.5299 0.2325 1.9597 -0.0214 0.0856  -0.0469 137 HIS D NE2 
13868 N N   . ILE D 138 ? 0.5214 0.1840 1.9073 0.0134  0.0606  -0.0209 138 ILE D N   
13869 C CA  . ILE D 138 ? 0.5249 0.1855 1.9211 0.0247  0.0519  -0.0265 138 ILE D CA  
13870 C C   . ILE D 138 ? 0.5587 0.1817 1.9377 0.0308  0.0458  -0.0200 138 ILE D C   
13871 O O   . ILE D 138 ? 0.5632 0.1719 1.9474 0.0333  0.0449  -0.0245 138 ILE D O   
13872 C CB  . ILE D 138 ? 0.5017 0.1870 1.9109 0.0341  0.0442  -0.0293 138 ILE D CB  
13873 C CG1 . ILE D 138 ? 0.4698 0.1895 1.8964 0.0289  0.0498  -0.0364 138 ILE D CG1 
13874 C CG2 . ILE D 138 ? 0.5194 0.1982 1.9392 0.0466  0.0351  -0.0343 138 ILE D CG2 
13875 C CD1 . ILE D 138 ? 0.4458 0.1894 1.8869 0.0373  0.0437  -0.0396 138 ILE D CD1 
13876 N N   . HIS D 139 ? 0.5698 0.1757 1.9270 0.0328  0.0418  -0.0095 139 HIS D N   
13877 C CA  . HIS D 139 ? 0.6104 0.1774 1.9456 0.0377  0.0357  -0.0012 139 HIS D CA  
13878 C C   . HIS D 139 ? 0.6422 0.1845 1.9706 0.0291  0.0447  -0.0005 139 HIS D C   
13879 O O   . HIS D 139 ? 0.6683 0.1841 1.9919 0.0352  0.0389  0.0008  139 HIS D O   
13880 C CB  . HIS D 139 ? 0.6292 0.1802 1.9360 0.0371  0.0336  0.0103  139 HIS D CB  
13881 C CG  . HIS D 139 ? 0.6785 0.1860 1.9572 0.0410  0.0278  0.0202  139 HIS D CG  
13882 N ND1 . HIS D 139 ? 0.7055 0.1975 1.9822 0.0554  0.0113  0.0218  139 HIS D ND1 
13883 C CD2 . HIS D 139 ? 0.7109 0.1862 1.9624 0.0326  0.0361  0.0292  139 HIS D CD2 
13884 C CE1 . HIS D 139 ? 0.7489 0.1990 1.9960 0.0559  0.0087  0.0321  139 HIS D CE1 
13885 N NE2 . HIS D 139 ? 0.7541 0.1932 1.9840 0.0418  0.0243  0.0371  139 HIS D NE2 
13886 N N   . SER D 140 ? 0.6440 0.1942 1.9737 0.0150  0.0585  -0.0014 140 SER D N   
13887 C CA  . SER D 140 ? 0.6696 0.1964 1.9939 0.0052  0.0679  -0.0006 140 SER D CA  
13888 C C   . SER D 140 ? 0.6664 0.1981 2.0126 0.0073  0.0665  -0.0120 140 SER D C   
13889 O O   . SER D 140 ? 0.7134 0.2161 2.0539 0.0067  0.0670  -0.0110 140 SER D O   
13890 C CB  . SER D 140 ? 0.6708 0.2077 1.9953 -0.0101 0.0824  0.0002  140 SER D CB  
13891 O OG  . SER D 140 ? 0.7066 0.2178 2.0250 -0.0202 0.0920  0.0021  140 SER D OG  
13892 N N   . VAL D 141 ? 0.6250 0.1914 1.9944 0.0099  0.0647  -0.0227 141 VAL D N   
13893 C CA  . VAL D 141 ? 0.6142 0.1863 2.0026 0.0115  0.0643  -0.0348 141 VAL D CA  
13894 C C   . VAL D 141 ? 0.6165 0.1865 2.0128 0.0273  0.0528  -0.0386 141 VAL D C   
13895 O O   . VAL D 141 ? 0.6103 0.1795 2.0203 0.0305  0.0523  -0.0487 141 VAL D O   
13896 C CB  . VAL D 141 ? 0.5759 0.1838 1.9831 0.0044  0.0700  -0.0451 141 VAL D CB  
13897 C CG1 . VAL D 141 ? 0.5697 0.1804 1.9743 -0.0109 0.0804  -0.0427 141 VAL D CG1 
13898 C CG2 . VAL D 141 ? 0.5429 0.1822 1.9592 0.0114  0.0652  -0.0470 141 VAL D CG2 
13899 N N   . THR D 142 ? 0.6168 0.1866 2.0056 0.0370  0.0438  -0.0316 142 THR D N   
13900 C CA  . THR D 142 ? 0.6142 0.1840 2.0126 0.0526  0.0315  -0.0342 142 THR D CA  
13901 C C   . THR D 142 ? 0.5803 0.1900 2.0009 0.0563  0.0310  -0.0431 142 THR D C   
13902 O O   . THR D 142 ? 0.5574 0.1900 1.9904 0.0493  0.0393  -0.0517 142 THR D O   
13903 C CB  . THR D 142 ? 0.6335 0.1815 2.0395 0.0593  0.0280  -0.0400 142 THR D CB  
13904 O OG1 . THR D 142 ? 0.6111 0.1798 2.0368 0.0551  0.0356  -0.0537 142 THR D OG1 
13905 C CG2 . THR D 142 ? 0.6664 0.1728 2.0504 0.0548  0.0293  -0.0310 142 THR D CG2 
13906 N N   . GLY D 143 ? 0.5814 0.1982 2.0064 0.0674  0.0207  -0.0410 143 GLY D N   
13907 C CA  . GLY D 143 ? 0.5606 0.2124 2.0086 0.0722  0.0200  -0.0494 143 GLY D CA  
13908 C C   . GLY D 143 ? 0.5667 0.2263 2.0363 0.0768  0.0226  -0.0628 143 GLY D C   
13909 O O   . GLY D 143 ? 0.5489 0.2374 2.0346 0.0751  0.0285  -0.0717 143 GLY D O   
13910 N N   . LYS D 144 ? 0.6018 0.2341 2.0705 0.0825  0.0187  -0.0642 144 LYS D N   
13911 C CA  . LYS D 144 ? 0.5989 0.2363 2.0872 0.0866  0.0222  -0.0779 144 LYS D CA  
13912 C C   . LYS D 144 ? 0.5744 0.2276 2.0632 0.0736  0.0352  -0.0855 144 LYS D C   
13913 O O   . LYS D 144 ? 0.5594 0.2371 2.0637 0.0741  0.0405  -0.0966 144 LYS D O   
13914 C CB  . LYS D 144 ? 0.6316 0.2344 2.1181 0.0940  0.0162  -0.0780 144 LYS D CB  
13915 C CG  . LYS D 144 ? 0.6412 0.2504 2.1495 0.0988  0.0205  -0.0937 144 LYS D CG  
13916 C CD  . LYS D 144 ? 0.6839 0.2606 2.1959 0.1084  0.0138  -0.0958 144 LYS D CD  
13917 C CE  . LYS D 144 ? 0.6877 0.2767 2.2256 0.1158  0.0176  -0.1127 144 LYS D CE  
13918 N NZ  . LYS D 144 ? 0.6792 0.2814 2.2166 0.1040  0.0312  -0.1232 144 LYS D NZ  
13919 N N   . ALA D 145 ? 0.5702 0.2095 2.0417 0.0618  0.0403  -0.0797 145 ALA D N   
13920 C CA  . ALA D 145 ? 0.5572 0.2108 2.0304 0.0498  0.0504  -0.0872 145 ALA D CA  
13921 C C   . ALA D 145 ? 0.5228 0.2127 2.0035 0.0473  0.0535  -0.0897 145 ALA D C   
13922 O O   . ALA D 145 ? 0.5107 0.2196 2.0013 0.0455  0.0587  -0.1006 145 ALA D O   
13923 C CB  . ALA D 145 ? 0.5712 0.2070 2.0281 0.0372  0.0550  -0.0798 145 ALA D CB  
13924 N N   . PHE D 146 ? 0.5045 0.2020 1.9790 0.0476  0.0502  -0.0795 146 PHE D N   
13925 C CA  . PHE D 146 ? 0.4860 0.2154 1.9673 0.0453  0.0527  -0.0806 146 PHE D CA  
13926 C C   . PHE D 146 ? 0.4804 0.2290 1.9803 0.0539  0.0527  -0.0908 146 PHE D C   
13927 O O   . PHE D 146 ? 0.4740 0.2445 1.9798 0.0495  0.0591  -0.0981 146 PHE D O   
13928 C CB  . PHE D 146 ? 0.4853 0.2167 1.9589 0.0470  0.0475  -0.0690 146 PHE D CB  
13929 C CG  . PHE D 146 ? 0.4509 0.2140 1.9322 0.0448  0.0498  -0.0695 146 PHE D CG  
13930 C CD1 . PHE D 146 ? 0.4319 0.2083 1.9085 0.0336  0.0561  -0.0681 146 PHE D CD1 
13931 C CD2 . PHE D 146 ? 0.4400 0.2191 1.9350 0.0539  0.0453  -0.0715 146 PHE D CD2 
13932 C CE1 . PHE D 146 ? 0.4151 0.2181 1.8980 0.0319  0.0575  -0.0677 146 PHE D CE1 
13933 C CE2 . PHE D 146 ? 0.4116 0.2176 1.9134 0.0513  0.0478  -0.0714 146 PHE D CE2 
13934 C CZ  . PHE D 146 ? 0.4009 0.2179 1.8956 0.0405  0.0538  -0.0692 146 PHE D CZ  
13935 N N   . VAL D 147 ? 0.4847 0.2255 1.9940 0.0663  0.0454  -0.0911 147 VAL D N   
13936 C CA  . VAL D 147 ? 0.4773 0.2393 2.0075 0.0745  0.0461  -0.1001 147 VAL D CA  
13937 C C   . VAL D 147 ? 0.4852 0.2511 2.0225 0.0728  0.0547  -0.1139 147 VAL D C   
13938 O O   . VAL D 147 ? 0.4733 0.2627 2.0206 0.0722  0.0614  -0.1219 147 VAL D O   
13939 C CB  . VAL D 147 ? 0.4817 0.2368 2.0262 0.0890  0.0360  -0.0997 147 VAL D CB  
13940 C CG1 . VAL D 147 ? 0.4672 0.2475 2.0367 0.0955  0.0398  -0.1107 147 VAL D CG1 
13941 C CG2 . VAL D 147 ? 0.4778 0.2293 2.0144 0.0916  0.0260  -0.0872 147 VAL D CG2 
13942 N N   . ASP D 148 ? 0.5085 0.2498 2.0394 0.0717  0.0548  -0.1167 148 ASP D N   
13943 C CA  . ASP D 148 ? 0.5181 0.2594 2.0545 0.0705  0.0621  -0.1308 148 ASP D CA  
13944 C C   . ASP D 148 ? 0.5073 0.2675 2.0348 0.0581  0.0704  -0.1345 148 ASP D C   
13945 O O   . ASP D 148 ? 0.5132 0.2902 2.0470 0.0582  0.0772  -0.1453 148 ASP D O   
13946 C CB  . ASP D 148 ? 0.5382 0.2473 2.0714 0.0731  0.0590  -0.1328 148 ASP D CB  
13947 C CG  . ASP D 148 ? 0.5583 0.2508 2.1033 0.0877  0.0500  -0.1313 148 ASP D CG  
13948 O OD1 . ASP D 148 ? 0.5436 0.2526 2.1045 0.0970  0.0467  -0.1323 148 ASP D OD1 
13949 O OD2 . ASP D 148 ? 0.5905 0.2527 2.1298 0.0898  0.0456  -0.1290 148 ASP D OD2 
13950 N N   . LEU D 149 ? 0.4853 0.2437 1.9985 0.0477  0.0696  -0.1251 149 LEU D N   
13951 C CA  . LEU D 149 ? 0.4586 0.2335 1.9643 0.0363  0.0751  -0.1277 149 LEU D CA  
13952 C C   . LEU D 149 ? 0.4366 0.2403 1.9484 0.0380  0.0785  -0.1298 149 LEU D C   
13953 O O   . LEU D 149 ? 0.4233 0.2392 1.9344 0.0353  0.0845  -0.1397 149 LEU D O   
13954 C CB  . LEU D 149 ? 0.4444 0.2145 1.9386 0.0264  0.0734  -0.1168 149 LEU D CB  
13955 C CG  . LEU D 149 ? 0.4225 0.2102 1.9113 0.0150  0.0770  -0.1185 149 LEU D CG  
13956 C CD1 . LEU D 149 ? 0.4295 0.2168 1.9170 0.0107  0.0805  -0.1319 149 LEU D CD1 
13957 C CD2 . LEU D 149 ? 0.4194 0.1995 1.9011 0.0061  0.0759  -0.1088 149 LEU D CD2 
13958 N N   . MET D 150 ? 0.4373 0.2498 1.9536 0.0424  0.0746  -0.1204 150 MET D N   
13959 C CA  . MET D 150 ? 0.4296 0.2681 1.9531 0.0438  0.0775  -0.1206 150 MET D CA  
13960 C C   . MET D 150 ? 0.4375 0.2842 1.9727 0.0499  0.0838  -0.1335 150 MET D C   
13961 O O   . MET D 150 ? 0.4306 0.2942 1.9632 0.0456  0.0909  -0.1390 150 MET D O   
13962 C CB  . MET D 150 ? 0.4300 0.2723 1.9605 0.0500  0.0711  -0.1107 150 MET D CB  
13963 C CG  . MET D 150 ? 0.4329 0.2680 1.9508 0.0442  0.0664  -0.0984 150 MET D CG  
13964 S SD  . MET D 150 ? 0.4307 0.2887 1.9418 0.0332  0.0707  -0.0943 150 MET D SD  
13965 C CE  . MET D 150 ? 0.4550 0.2951 1.9513 0.0229  0.0706  -0.0904 150 MET D CE  
13966 N N   . ASN D 151 ? 0.4565 0.2900 2.0037 0.0599  0.0815  -0.1386 151 ASN D N   
13967 C CA  . ASN D 151 ? 0.4724 0.3139 2.0341 0.0666  0.0885  -0.1518 151 ASN D CA  
13968 C C   . ASN D 151 ? 0.4899 0.3312 2.0400 0.0595  0.0972  -0.1632 151 ASN D C   
13969 O O   . ASN D 151 ? 0.4816 0.3382 2.0354 0.0599  0.1064  -0.1724 151 ASN D O   
13970 C CB  . ASN D 151 ? 0.4948 0.3207 2.0736 0.0792  0.0833  -0.1556 151 ASN D CB  
13971 C CG  . ASN D 151 ? 0.4906 0.3259 2.0874 0.0885  0.0767  -0.1498 151 ASN D CG  
13972 O OD1 . ASN D 151 ? 0.5041 0.3225 2.1063 0.0965  0.0662  -0.1447 151 ASN D OD1 
13973 N ND2 . ASN D 151 ? 0.4782 0.3391 2.0846 0.0877  0.0821  -0.1505 151 ASN D ND2 
13974 N N   . THR D 152 ? 0.5079 0.3314 2.0438 0.0527  0.0943  -0.1626 152 THR D N   
13975 C CA  . THR D 152 ? 0.5270 0.3479 2.0507 0.0455  0.1002  -0.1737 152 THR D CA  
13976 C C   . THR D 152 ? 0.5081 0.3504 2.0197 0.0367  0.1044  -0.1723 152 THR D C   
13977 O O   . THR D 152 ? 0.5100 0.3618 2.0170 0.0356  0.1124  -0.1826 152 THR D O   
13978 C CB  . THR D 152 ? 0.5566 0.3547 2.0704 0.0392  0.0952  -0.1721 152 THR D CB  
13979 O OG1 . THR D 152 ? 0.5914 0.3683 2.1153 0.0479  0.0905  -0.1706 152 THR D OG1 
13980 C CG2 . THR D 152 ? 0.5715 0.3634 2.0754 0.0329  0.0995  -0.1856 152 THR D CG2 
13981 N N   . LEU D 153 ? 0.4885 0.3372 1.9942 0.0308  0.0992  -0.1595 153 LEU D N   
13982 C CA  . LEU D 153 ? 0.4929 0.3604 1.9876 0.0229  0.1015  -0.1567 153 LEU D CA  
13983 C C   . LEU D 153 ? 0.4768 0.3638 1.9782 0.0275  0.1085  -0.1584 153 LEU D C   
13984 O O   . LEU D 153 ? 0.4826 0.3806 1.9731 0.0229  0.1146  -0.1635 153 LEU D O   
13985 C CB  . LEU D 153 ? 0.4866 0.3566 1.9777 0.0171  0.0946  -0.1428 153 LEU D CB  
13986 C CG  . LEU D 153 ? 0.5135 0.3652 1.9995 0.0113  0.0894  -0.1404 153 LEU D CG  
13987 C CD1 . LEU D 153 ? 0.5040 0.3588 1.9897 0.0073  0.0846  -0.1266 153 LEU D CD1 
13988 C CD2 . LEU D 153 ? 0.5281 0.3776 2.0028 0.0025  0.0900  -0.1493 153 LEU D CD2 
13989 N N   . ILE D 154 ? 0.4520 0.3430 1.9710 0.0362  0.1076  -0.1542 154 ILE D N   
13990 C CA  . ILE D 154 ? 0.4355 0.3457 1.9648 0.0399  0.1147  -0.1558 154 ILE D CA  
13991 C C   . ILE D 154 ? 0.4513 0.3636 1.9794 0.0414  0.1260  -0.1708 154 ILE D C   
13992 O O   . ILE D 154 ? 0.4447 0.3711 1.9647 0.0372  0.1344  -0.1732 154 ILE D O   
13993 C CB  . ILE D 154 ? 0.4240 0.3372 1.9762 0.0499  0.1107  -0.1512 154 ILE D CB  
13994 C CG1 . ILE D 154 ? 0.4090 0.3214 1.9601 0.0484  0.1006  -0.1366 154 ILE D CG1 
13995 C CG2 . ILE D 154 ? 0.4161 0.3495 1.9826 0.0532  0.1201  -0.1556 154 ILE D CG2 
13996 C CD1 . ILE D 154 ? 0.4026 0.3098 1.9720 0.0586  0.0930  -0.1328 154 ILE D CD1 
13997 N N   . ASN D 155 ? 0.4743 0.3713 2.0093 0.0473  0.1266  -0.1808 155 ASN D N   
13998 C CA  . ASN D 155 ? 0.4960 0.3945 2.0333 0.0503  0.1383  -0.1963 155 ASN D CA  
13999 C C   . ASN D 155 ? 0.5120 0.4097 2.0223 0.0405  0.1436  -0.2031 155 ASN D C   
14000 O O   . ASN D 155 ? 0.5192 0.4254 2.0239 0.0399  0.1555  -0.2125 155 ASN D O   
14001 C CB  . ASN D 155 ? 0.5265 0.4085 2.0804 0.0601  0.1370  -0.2054 155 ASN D CB  
14002 C CG  . ASN D 155 ? 0.5412 0.4263 2.1226 0.0710  0.1317  -0.2001 155 ASN D CG  
14003 O OD1 . ASN D 155 ? 0.5258 0.4298 2.1203 0.0732  0.1347  -0.1963 155 ASN D OD1 
14004 N ND2 . ASN D 155 ? 0.5656 0.4308 2.1560 0.0779  0.1230  -0.2000 155 ASN D ND2 
14005 N N   . ILE D 156 ? 0.5199 0.4075 2.0133 0.0326  0.1350  -0.1984 156 ILE D N   
14006 C CA  . ILE D 156 ? 0.5412 0.4284 2.0088 0.0230  0.1368  -0.2039 156 ILE D CA  
14007 C C   . ILE D 156 ? 0.5366 0.4427 1.9922 0.0177  0.1407  -0.1972 156 ILE D C   
14008 O O   . ILE D 156 ? 0.5620 0.4709 1.9973 0.0127  0.1471  -0.2044 156 ILE D O   
14009 C CB  . ILE D 156 ? 0.5507 0.4247 2.0088 0.0158  0.1254  -0.1997 156 ILE D CB  
14010 C CG1 . ILE D 156 ? 0.5658 0.4183 2.0306 0.0192  0.1234  -0.2087 156 ILE D CG1 
14011 C CG2 . ILE D 156 ? 0.5578 0.4357 1.9910 0.0053  0.1235  -0.2016 156 ILE D CG2 
14012 C CD1 . ILE D 156 ? 0.5614 0.4000 2.0228 0.0126  0.1131  -0.2029 156 ILE D CD1 
14013 N N   . ILE D 157 ? 0.5035 0.4210 1.9692 0.0182  0.1365  -0.1832 157 ILE D N   
14014 C CA  . ILE D 157 ? 0.4871 0.4209 1.9424 0.0132  0.1397  -0.1759 157 ILE D CA  
14015 C C   . ILE D 157 ? 0.4875 0.4321 1.9499 0.0177  0.1540  -0.1825 157 ILE D C   
14016 O O   . ILE D 157 ? 0.4966 0.4485 1.9414 0.0126  0.1619  -0.1841 157 ILE D O   
14017 C CB  . ILE D 157 ? 0.4637 0.4054 1.9273 0.0119  0.1309  -0.1598 157 ILE D CB  
14018 C CG1 . ILE D 157 ? 0.4567 0.3891 1.9122 0.0059  0.1188  -0.1537 157 ILE D CG1 
14019 C CG2 . ILE D 157 ? 0.4598 0.4178 1.9158 0.0078  0.1353  -0.1526 157 ILE D CG2 
14020 C CD1 . ILE D 157 ? 0.4264 0.3637 1.8926 0.0059  0.1111  -0.1395 157 ILE D CD1 
14021 N N   . HIS D 158 ? 0.4823 0.4273 1.9708 0.0271  0.1574  -0.1866 158 HIS D N   
14022 C CA  . HIS D 158 ? 0.4784 0.4355 1.9801 0.0317  0.1716  -0.1933 158 HIS D CA  
14023 C C   . HIS D 158 ? 0.5169 0.4697 2.0005 0.0293  0.1847  -0.2084 158 HIS D C   
14024 O O   . HIS D 158 ? 0.5343 0.4983 2.0154 0.0281  0.1987  -0.2120 158 HIS D O   
14025 C CB  . HIS D 158 ? 0.4565 0.4143 1.9924 0.0431  0.1711  -0.1963 158 HIS D CB  
14026 C CG  . HIS D 158 ? 0.4214 0.3878 1.9764 0.0462  0.1622  -0.1832 158 HIS D CG  
14027 N ND1 . HIS D 158 ? 0.4085 0.3723 1.9914 0.0564  0.1564  -0.1837 158 HIS D ND1 
14028 C CD2 . HIS D 158 ? 0.4090 0.3853 1.9596 0.0411  0.1577  -0.1703 158 HIS D CD2 
14029 C CE1 . HIS D 158 ? 0.3883 0.3605 1.9821 0.0572  0.1486  -0.1718 158 HIS D CE1 
14030 N NE2 . HIS D 158 ? 0.3924 0.3725 1.9676 0.0479  0.1499  -0.1637 158 HIS D NE2 
14031 N N   . LYS D 159 ? 0.5346 0.4707 2.0056 0.0284  0.1808  -0.2174 159 LYS D N   
14032 C CA  . LYS D 159 ? 0.5641 0.4935 2.0150 0.0259  0.1920  -0.2329 159 LYS D CA  
14033 C C   . LYS D 159 ? 0.5645 0.4914 1.9782 0.0148  0.1885  -0.2300 159 LYS D C   
14034 O O   . LYS D 159 ? 0.5802 0.5074 1.9708 0.0108  0.1995  -0.2383 159 LYS D O   
14035 C CB  . LYS D 159 ? 0.5990 0.5102 2.0556 0.0307  0.1895  -0.2457 159 LYS D CB  
14036 C CG  . LYS D 159 ? 0.6175 0.5278 2.1084 0.0427  0.1938  -0.2525 159 LYS D CG  
14037 C CD  . LYS D 159 ? 0.6775 0.5689 2.1682 0.0466  0.1953  -0.2685 159 LYS D CD  
14038 C CE  . LYS D 159 ? 0.7204 0.5940 2.2162 0.0477  0.1796  -0.2638 159 LYS D CE  
14039 N NZ  . LYS D 159 ? 0.7543 0.6238 2.2835 0.0597  0.1767  -0.2637 159 LYS D NZ  
14040 N N   . GLY D 160 ? 0.5414 0.4655 1.9491 0.0099  0.1730  -0.2184 160 GLY D N   
14041 C CA  . GLY D 160 ? 0.5555 0.4751 1.9315 0.0003  0.1662  -0.2172 160 GLY D CA  
14042 C C   . GLY D 160 ? 0.5550 0.4874 1.9145 -0.0052 0.1690  -0.2070 160 GLY D C   
14043 O O   . GLY D 160 ? 0.5713 0.5005 1.8996 -0.0120 0.1696  -0.2098 160 GLY D O   
14044 N N   . HIS D 161 ? 0.5363 0.4817 1.9167 -0.0022 0.1695  -0.1949 161 HIS D N   
14045 C CA  . HIS D 161 ? 0.5307 0.4885 1.9018 -0.0062 0.1738  -0.1846 161 HIS D CA  
14046 C C   . HIS D 161 ? 0.5105 0.4809 1.9085 0.0001  0.1858  -0.1834 161 HIS D C   
14047 O O   . HIS D 161 ? 0.4773 0.4566 1.8971 0.0026  0.1804  -0.1724 161 HIS D O   
14048 C CB  . HIS D 161 ? 0.5185 0.4800 1.8891 -0.0105 0.1585  -0.1691 161 HIS D CB  
14049 C CG  . HIS D 161 ? 0.5247 0.4937 1.8758 -0.0164 0.1605  -0.1600 161 HIS D CG  
14050 N ND1 . HIS D 161 ? 0.5161 0.4881 1.8620 -0.0209 0.1476  -0.1472 161 HIS D ND1 
14051 C CD2 . HIS D 161 ? 0.5480 0.5209 1.8833 -0.0186 0.1740  -0.1616 161 HIS D CD2 
14052 C CE1 . HIS D 161 ? 0.5340 0.5108 1.8613 -0.0252 0.1522  -0.1408 161 HIS D CE1 
14053 N NE2 . HIS D 161 ? 0.5472 0.5243 1.8669 -0.0243 0.1686  -0.1490 161 HIS D NE2 
14054 N N   . PRO D 162 ? 0.5324 0.5043 1.9310 0.0027  0.2028  -0.1956 162 PRO D N   
14055 C CA  . PRO D 162 ? 0.5146 0.4995 1.9440 0.0089  0.2144  -0.1964 162 PRO D CA  
14056 C C   . PRO D 162 ? 0.4871 0.4860 1.9199 0.0052  0.2159  -0.1821 162 PRO D C   
14057 O O   . PRO D 162 ? 0.4876 0.4859 1.8924 -0.0028 0.2153  -0.1748 162 PRO D O   
14058 C CB  . PRO D 162 ? 0.5460 0.5293 1.9686 0.0101  0.2339  -0.2127 162 PRO D CB  
14059 C CG  . PRO D 162 ? 0.5790 0.5499 1.9571 0.0018  0.2334  -0.2166 162 PRO D CG  
14060 C CD  . PRO D 162 ? 0.5676 0.5290 1.9381 -0.0004 0.2119  -0.2098 162 PRO D CD  
14061 N N   . GLY D 163 ? 0.4545 0.4647 1.9228 0.0113  0.2157  -0.1780 163 GLY D N   
14062 C CA  . GLY D 163 ? 0.4357 0.4598 1.9141 0.0087  0.2190  -0.1668 163 GLY D CA  
14063 C C   . GLY D 163 ? 0.4108 0.4360 1.8926 0.0073  0.2013  -0.1516 163 GLY D C   
14064 O O   . GLY D 163 ? 0.3976 0.4339 1.8926 0.0062  0.2017  -0.1422 163 GLY D O   
14065 N N   . ILE D 164 ? 0.4044 0.4181 1.8748 0.0068  0.1866  -0.1495 164 ILE D N   
14066 C CA  . ILE D 164 ? 0.3776 0.3925 1.8485 0.0044  0.1721  -0.1354 164 ILE D CA  
14067 C C   . ILE D 164 ? 0.3480 0.3617 1.8463 0.0118  0.1620  -0.1334 164 ILE D C   
14068 O O   . ILE D 164 ? 0.3579 0.3604 1.8576 0.0154  0.1566  -0.1393 164 ILE D O   
14069 C CB  . ILE D 164 ? 0.3885 0.3937 1.8303 -0.0024 0.1620  -0.1319 164 ILE D CB  
14070 C CG1 . ILE D 164 ? 0.4126 0.4189 1.8249 -0.0101 0.1682  -0.1295 164 ILE D CG1 
14071 C CG2 . ILE D 164 ? 0.3658 0.3716 1.8157 -0.0030 0.1472  -0.1197 164 ILE D CG2 
14072 C CD1 . ILE D 164 ? 0.4465 0.4481 1.8409 -0.0112 0.1825  -0.1424 164 ILE D CD1 
14073 N N   . PRO D 165 ? 0.3158 0.3396 1.8346 0.0141  0.1589  -0.1248 165 PRO D N   
14074 C CA  . PRO D 165 ? 0.2981 0.3194 1.8385 0.0208  0.1478  -0.1214 165 PRO D CA  
14075 C C   . PRO D 165 ? 0.3016 0.3093 1.8284 0.0190  0.1352  -0.1174 165 PRO D C   
14076 O O   . PRO D 165 ? 0.3105 0.3168 1.8175 0.0118  0.1318  -0.1118 165 PRO D O   
14077 C CB  . PRO D 165 ? 0.2764 0.3095 1.8306 0.0202  0.1448  -0.1109 165 PRO D CB  
14078 C CG  . PRO D 165 ? 0.2847 0.3283 1.8312 0.0142  0.1574  -0.1101 165 PRO D CG  
14079 C CD  . PRO D 165 ? 0.3090 0.3458 1.8297 0.0100  0.1658  -0.1179 165 PRO D CD  
14080 N N   . VAL D 166 ? 0.2996 0.2977 1.8391 0.0256  0.1281  -0.1193 166 VAL D N   
14081 C CA  . VAL D 166 ? 0.2977 0.2820 1.8282 0.0242  0.1171  -0.1150 166 VAL D CA  
14082 C C   . VAL D 166 ? 0.2864 0.2679 1.8325 0.0298  0.1079  -0.1078 166 VAL D C   
14083 O O   . VAL D 166 ? 0.2945 0.2765 1.8593 0.0378  0.1077  -0.1113 166 VAL D O   
14084 C CB  . VAL D 166 ? 0.3223 0.2922 1.8473 0.0261  0.1186  -0.1256 166 VAL D CB  
14085 C CG1 . VAL D 166 ? 0.3264 0.2807 1.8406 0.0229  0.1092  -0.1222 166 VAL D CG1 
14086 C CG2 . VAL D 166 ? 0.3422 0.3152 1.8525 0.0220  0.1290  -0.1350 166 VAL D CG2 
14087 N N   . THR D 167 ? 0.2844 0.2629 1.8228 0.0257  0.1001  -0.0981 167 THR D N   
14088 C CA  . THR D 167 ? 0.2777 0.2487 1.8237 0.0301  0.0909  -0.0914 167 THR D CA  
14089 C C   . THR D 167 ? 0.2917 0.2502 1.8226 0.0245  0.0851  -0.0860 167 THR D C   
14090 O O   . THR D 167 ? 0.2938 0.2472 1.8125 0.0191  0.0870  -0.0896 167 THR D O   
14091 C CB  . THR D 167 ? 0.2521 0.2373 1.8095 0.0309  0.0898  -0.0849 167 THR D CB  
14092 O OG1 . THR D 167 ? 0.2403 0.2174 1.8031 0.0355  0.0803  -0.0792 167 THR D OG1 
14093 C CG2 . THR D 167 ? 0.2402 0.2351 1.7867 0.0225  0.0915  -0.0785 167 THR D CG2 
14094 N N   . LEU D 168 ? 0.2997 0.2523 1.8319 0.0259  0.0781  -0.0781 168 LEU D N   
14095 C CA  . LEU D 168 ? 0.3203 0.2613 1.8405 0.0206  0.0743  -0.0729 168 LEU D CA  
14096 C C   . LEU D 168 ? 0.3301 0.2774 1.8506 0.0185  0.0708  -0.0636 168 LEU D C   
14097 O O   . LEU D 168 ? 0.3656 0.3198 1.8957 0.0233  0.0688  -0.0614 168 LEU D O   
14098 C CB  . LEU D 168 ? 0.3325 0.2522 1.8504 0.0249  0.0706  -0.0740 168 LEU D CB  
14099 C CG  . LEU D 168 ? 0.3329 0.2437 1.8530 0.0306  0.0637  -0.0672 168 LEU D CG  
14100 C CD1 . LEU D 168 ? 0.3482 0.2346 1.8612 0.0337  0.0599  -0.0667 168 LEU D CD1 
14101 C CD2 . LEU D 168 ? 0.3407 0.2621 1.8765 0.0387  0.0619  -0.0694 168 LEU D CD2 
14102 N N   . SER D 169 ? 0.3395 0.2854 1.8514 0.0113  0.0702  -0.0591 169 SER D N   
14103 C CA  . SER D 169 ? 0.3419 0.2905 1.8535 0.0094  0.0673  -0.0511 169 SER D CA  
14104 C C   . SER D 169 ? 0.3366 0.2670 1.8432 0.0125  0.0636  -0.0476 169 SER D C   
14105 O O   . SER D 169 ? 0.3504 0.2695 1.8488 0.0079  0.0643  -0.0454 169 SER D O   
14106 C CB  . SER D 169 ? 0.3733 0.3276 1.8804 0.0011  0.0685  -0.0485 169 SER D CB  
14107 O OG  . SER D 169 ? 0.4139 0.3670 1.9163 -0.0036 0.0705  -0.0540 169 SER D OG  
14108 N N   . ALA D 170 ? 0.3322 0.2580 1.8432 0.0203  0.0595  -0.0473 170 ALA D N   
14109 C CA  . ALA D 170 ? 0.3473 0.2538 1.8494 0.0234  0.0548  -0.0429 170 ALA D CA  
14110 C C   . ALA D 170 ? 0.3441 0.2550 1.8437 0.0218  0.0527  -0.0364 170 ALA D C   
14111 O O   . ALA D 170 ? 0.3505 0.2786 1.8600 0.0221  0.0525  -0.0362 170 ALA D O   
14112 C CB  . ALA D 170 ? 0.3585 0.2563 1.8660 0.0331  0.0492  -0.0456 170 ALA D CB  
14113 N N   . ASN D 171 ? 0.3565 0.2511 1.8425 0.0197  0.0521  -0.0315 171 ASN D N   
14114 C CA  . ASN D 171 ? 0.3509 0.2473 1.8326 0.0183  0.0507  -0.0262 171 ASN D CA  
14115 C C   . ASN D 171 ? 0.3639 0.2522 1.8430 0.0266  0.0421  -0.0245 171 ASN D C   
14116 O O   . ASN D 171 ? 0.4194 0.2880 1.8884 0.0310  0.0379  -0.0237 171 ASN D O   
14117 C CB  . ASN D 171 ? 0.3586 0.2407 1.8260 0.0120  0.0554  -0.0223 171 ASN D CB  
14118 C CG  . ASN D 171 ? 0.3632 0.2449 1.8245 0.0114  0.0546  -0.0178 171 ASN D CG  
14119 O OD1 . ASN D 171 ? 0.3579 0.2251 1.8075 0.0163  0.0492  -0.0151 171 ASN D OD1 
14120 N ND2 . ASN D 171 ? 0.3678 0.2643 1.8364 0.0057  0.0592  -0.0173 171 ASN D ND2 
14121 N N   . ALA D 172 ? 0.3098 0.2115 1.7971 0.0282  0.0388  -0.0236 172 ALA D N   
14122 C CA  . ALA D 172 ? 0.3041 0.2012 1.7929 0.0362  0.0291  -0.0234 172 ALA D CA  
14123 C C   . ALA D 172 ? 0.3177 0.1921 1.7845 0.0377  0.0242  -0.0185 172 ALA D C   
14124 O O   . ALA D 172 ? 0.3537 0.2161 1.8158 0.0451  0.0144  -0.0182 172 ALA D O   
14125 C CB  . ALA D 172 ? 0.2919 0.2094 1.7971 0.0369  0.0271  -0.0245 172 ALA D CB  
14126 N N   . MET D 173 ? 0.3215 0.1887 1.7739 0.0309  0.0308  -0.0149 173 MET D N   
14127 C CA  . MET D 173 ? 0.3586 0.2024 1.7867 0.0318  0.0278  -0.0103 173 MET D CA  
14128 C C   . MET D 173 ? 0.4056 0.2234 1.8162 0.0336  0.0269  -0.0080 173 MET D C   
14129 O O   . MET D 173 ? 0.4467 0.2420 1.8359 0.0373  0.0207  -0.0041 173 MET D O   
14130 C CB  . MET D 173 ? 0.3609 0.2048 1.7800 0.0236  0.0372  -0.0078 173 MET D CB  
14131 C CG  . MET D 173 ? 0.3383 0.2008 1.7691 0.0230  0.0362  -0.0090 173 MET D CG  
14132 S SD  . MET D 173 ? 0.3560 0.2072 1.7748 0.0305  0.0233  -0.0083 173 MET D SD  
14133 C CE  . MET D 173 ? 0.3806 0.2024 1.7639 0.0267  0.0287  -0.0035 173 MET D CE  
14134 N N   . ILE D 174 ? 0.4063 0.2254 1.8243 0.0311  0.0324  -0.0103 174 ILE D N   
14135 C CA  . ILE D 174 ? 0.4338 0.2274 1.8360 0.0314  0.0332  -0.0080 174 ILE D CA  
14136 C C   . ILE D 174 ? 0.4504 0.2440 1.8654 0.0383  0.0275  -0.0124 174 ILE D C   
14137 O O   . ILE D 174 ? 0.4769 0.2477 1.8803 0.0404  0.0259  -0.0107 174 ILE D O   
14138 C CB  . ILE D 174 ? 0.4388 0.2294 1.8371 0.0209  0.0461  -0.0074 174 ILE D CB  
14139 C CG1 . ILE D 174 ? 0.4182 0.2331 1.8397 0.0174  0.0508  -0.0135 174 ILE D CG1 
14140 C CG2 . ILE D 174 ? 0.4403 0.2280 1.8262 0.0138  0.0536  -0.0035 174 ILE D CG2 
14141 C CD1 . ILE D 174 ? 0.4326 0.2393 1.8532 0.0108  0.0584  -0.0152 174 ILE D CD1 
14142 N N   . SER D 175 ? 0.4443 0.2628 1.8832 0.0409  0.0262  -0.0182 175 SER D N   
14143 C CA  . SER D 175 ? 0.4696 0.2901 1.9228 0.0472  0.0230  -0.0238 175 SER D CA  
14144 C C   . SER D 175 ? 0.4585 0.2905 1.9284 0.0567  0.0128  -0.0269 175 SER D C   
14145 O O   . SER D 175 ? 0.4484 0.2913 1.9378 0.0618  0.0118  -0.0332 175 SER D O   
14146 C CB  . SER D 175 ? 0.4717 0.3073 1.9369 0.0410  0.0328  -0.0292 175 SER D CB  
14147 O OG  . SER D 175 ? 0.5195 0.3395 1.9705 0.0337  0.0396  -0.0270 175 SER D OG  
14148 N N   . ASP D 176 ? 0.4607 0.2878 1.9221 0.0596  0.0048  -0.0227 176 ASP D N   
14149 C CA  . ASP D 176 ? 0.4710 0.3070 1.9486 0.0686  -0.0066 -0.0257 176 ASP D CA  
14150 C C   . ASP D 176 ? 0.4731 0.2996 1.9603 0.0781  -0.0141 -0.0294 176 ASP D C   
14151 O O   . ASP D 176 ? 0.4545 0.2991 1.9686 0.0832  -0.0158 -0.0362 176 ASP D O   
14152 C CB  . ASP D 176 ? 0.4886 0.3158 1.9510 0.0701  -0.0154 -0.0208 176 ASP D CB  
14153 C CG  . ASP D 176 ? 0.5141 0.3100 1.9421 0.0686  -0.0171 -0.0135 176 ASP D CG  
14154 O OD1 . ASP D 176 ? 0.5327 0.3154 1.9497 0.0644  -0.0091 -0.0116 176 ASP D OD1 
14155 O OD2 . ASP D 176 ? 0.5108 0.2948 1.9227 0.0715  -0.0262 -0.0101 176 ASP D OD2 
14156 N N   . TYR D 177 ? 0.4857 0.2834 1.9517 0.0803  -0.0178 -0.0251 177 TYR D N   
14157 C CA  . TYR D 177 ? 0.4974 0.2804 1.9693 0.0908  -0.0281 -0.0273 177 TYR D CA  
14158 C C   . TYR D 177 ? 0.4843 0.2818 1.9811 0.0922  -0.0208 -0.0360 177 TYR D C   
14159 O O   . TYR D 177 ? 0.5161 0.3142 2.0317 0.1020  -0.0285 -0.0413 177 TYR D O   
14160 C CB  . TYR D 177 ? 0.5424 0.2894 1.9835 0.0908  -0.0306 -0.0199 177 TYR D CB  
14161 C CG  . TYR D 177 ? 0.5456 0.2861 1.9767 0.0807  -0.0156 -0.0191 177 TYR D CG  
14162 C CD1 . TYR D 177 ? 0.5302 0.2711 1.9446 0.0693  -0.0048 -0.0146 177 TYR D CD1 
14163 C CD2 . TYR D 177 ? 0.5369 0.2720 1.9776 0.0826  -0.0123 -0.0239 177 TYR D CD2 
14164 C CE1 . TYR D 177 ? 0.5200 0.2569 1.9292 0.0600  0.0080  -0.0148 177 TYR D CE1 
14165 C CE2 . TYR D 177 ? 0.5371 0.2668 1.9701 0.0730  0.0004  -0.0241 177 TYR D CE2 
14166 C CZ  . TYR D 177 ? 0.5250 0.2561 1.9431 0.0617  0.0101  -0.0195 177 TYR D CZ  
14167 O OH  . TYR D 177 ? 0.5216 0.2487 1.9355 0.0522  0.0216  -0.0204 177 TYR D OH  
14168 N N   . MET D 178 ? 0.4479 0.2557 1.9442 0.0824  -0.0063 -0.0379 178 MET D N   
14169 C CA  . MET D 178 ? 0.4328 0.2465 1.9428 0.0821  0.0016  -0.0455 178 MET D CA  
14170 C C   . MET D 178 ? 0.4137 0.2524 1.9547 0.0878  0.0019  -0.0545 178 MET D C   
14171 O O   . MET D 178 ? 0.4223 0.2837 1.9746 0.0849  0.0050  -0.0556 178 MET D O   
14172 C CB  . MET D 178 ? 0.4180 0.2400 1.9202 0.0698  0.0154  -0.0456 178 MET D CB  
14173 C CG  . MET D 178 ? 0.4039 0.2401 1.9213 0.0679  0.0246  -0.0548 178 MET D CG  
14174 S SD  . MET D 178 ? 0.3875 0.2291 1.8927 0.0538  0.0371  -0.0542 178 MET D SD  
14175 C CE  . MET D 178 ? 0.4262 0.2356 1.9059 0.0502  0.0351  -0.0457 178 MET D CE  
14176 N N   . ASP D 179 ? 0.4239 0.2582 1.9794 0.0955  0.0002  -0.0614 179 ASP D N   
14177 C CA  . ASP D 179 ? 0.4174 0.2749 2.0033 0.1002  0.0038  -0.0714 179 ASP D CA  
14178 C C   . ASP D 179 ? 0.3844 0.2612 1.9721 0.0904  0.0195  -0.0759 179 ASP D C   
14179 O O   . ASP D 179 ? 0.3835 0.2503 1.9552 0.0839  0.0262  -0.0756 179 ASP D O   
14180 C CB  . ASP D 179 ? 0.4615 0.3067 2.0596 0.1096  0.0007  -0.0784 179 ASP D CB  
14181 C CG  . ASP D 179 ? 0.4727 0.3404 2.1042 0.1153  0.0059  -0.0903 179 ASP D CG  
14182 O OD1 . ASP D 179 ? 0.4747 0.3562 2.1098 0.1090  0.0203  -0.0968 179 ASP D OD1 
14183 O OD2 . ASP D 179 ? 0.4966 0.3677 2.1499 0.1257  -0.0047 -0.0929 179 ASP D OD2 
14184 N N   . GLU D 180 ? 0.3643 0.2675 1.9712 0.0893  0.0250  -0.0802 180 GLU D N   
14185 C CA  . GLU D 180 ? 0.3457 0.2654 1.9527 0.0808  0.0394  -0.0847 180 GLU D CA  
14186 C C   . GLU D 180 ? 0.3379 0.2736 1.9704 0.0856  0.0468  -0.0960 180 GLU D C   
14187 O O   . GLU D 180 ? 0.3289 0.2798 1.9625 0.0794  0.0590  -0.1002 180 GLU D O   
14188 C CB  . GLU D 180 ? 0.3288 0.2640 1.9295 0.0721  0.0433  -0.0787 180 GLU D CB  
14189 C CG  . GLU D 180 ? 0.3369 0.2591 1.9138 0.0662  0.0390  -0.0687 180 GLU D CG  
14190 C CD  . GLU D 180 ? 0.3304 0.2682 1.9021 0.0571  0.0445  -0.0641 180 GLU D CD  
14191 O OE1 . GLU D 180 ? 0.3277 0.2851 1.9129 0.0554  0.0511  -0.0679 180 GLU D OE1 
14192 O OE2 . GLU D 180 ? 0.3313 0.2618 1.8863 0.0514  0.0432  -0.0571 180 GLU D OE2 
14193 N N   . SER D 181 ? 0.3381 0.2686 1.9899 0.0967  0.0400  -0.1014 181 SER D N   
14194 C CA  . SER D 181 ? 0.3351 0.2828 2.0157 0.1018  0.0476  -0.1128 181 SER D CA  
14195 C C   . SER D 181 ? 0.3396 0.2859 2.0157 0.0990  0.0610  -0.1220 181 SER D C   
14196 O O   . SER D 181 ? 0.3376 0.3004 2.0323 0.1000  0.0720  -0.1316 181 SER D O   
14197 C CB  . SER D 181 ? 0.3435 0.2870 2.0491 0.1149  0.0359  -0.1167 181 SER D CB  
14198 O OG  . SER D 181 ? 0.3681 0.2840 2.0564 0.1196  0.0227  -0.1106 181 SER D OG  
14199 N N   . ILE D 182 ? 0.3464 0.2729 1.9986 0.0952  0.0607  -0.1200 182 ILE D N   
14200 C CA  . ILE D 182 ? 0.3513 0.2768 1.9972 0.0914  0.0729  -0.1292 182 ILE D CA  
14201 C C   . ILE D 182 ? 0.3345 0.2777 1.9691 0.0803  0.0850  -0.1291 182 ILE D C   
14202 O O   . ILE D 182 ? 0.3336 0.2820 1.9659 0.0773  0.0968  -0.1382 182 ILE D O   
14203 C CB  . ILE D 182 ? 0.3696 0.2687 1.9949 0.0899  0.0688  -0.1275 182 ILE D CB  
14204 C CG1 . ILE D 182 ? 0.3617 0.2531 1.9615 0.0804  0.0651  -0.1159 182 ILE D CG1 
14205 C CG2 . ILE D 182 ? 0.3920 0.2718 2.0283 0.1017  0.0573  -0.1280 182 ILE D CG2 
14206 C CD1 . ILE D 182 ? 0.3819 0.2479 1.9634 0.0777  0.0626  -0.1146 182 ILE D CD1 
14207 N N   . PHE D 183 ? 0.3162 0.2676 1.9426 0.0743  0.0820  -0.1189 183 PHE D N   
14208 C CA  . PHE D 183 ? 0.3083 0.2736 1.9222 0.0640  0.0914  -0.1172 183 PHE D CA  
14209 C C   . PHE D 183 ? 0.3113 0.2989 1.9450 0.0649  0.1001  -0.1212 183 PHE D C   
14210 O O   . PHE D 183 ? 0.3083 0.3028 1.9674 0.0728  0.0968  -0.1236 183 PHE D O   
14211 C CB  . PHE D 183 ? 0.2972 0.2594 1.8938 0.0572  0.0846  -0.1049 183 PHE D CB  
14212 C CG  . PHE D 183 ? 0.3076 0.2479 1.8861 0.0553  0.0780  -0.1009 183 PHE D CG  
14213 C CD1 . PHE D 183 ? 0.3155 0.2478 1.8787 0.0495  0.0828  -0.1051 183 PHE D CD1 
14214 C CD2 . PHE D 183 ? 0.3085 0.2355 1.8847 0.0589  0.0671  -0.0932 183 PHE D CD2 
14215 C CE1 . PHE D 183 ? 0.3269 0.2394 1.8763 0.0470  0.0777  -0.1018 183 PHE D CE1 
14216 C CE2 . PHE D 183 ? 0.3196 0.2256 1.8790 0.0564  0.0629  -0.0893 183 PHE D CE2 
14217 C CZ  . PHE D 183 ? 0.3286 0.2279 1.8762 0.0503  0.0686  -0.0936 183 PHE D CZ  
14218 N N   . ASP D 184 ? 0.3050 0.3032 1.9268 0.0565  0.1111  -0.1221 184 ASP D N   
14219 C CA  . ASP D 184 ? 0.2938 0.3116 1.9295 0.0550  0.1218  -0.1248 184 ASP D CA  
14220 C C   . ASP D 184 ? 0.2930 0.3206 1.9354 0.0528  0.1156  -0.1144 184 ASP D C   
14221 O O   . ASP D 184 ? 0.2912 0.3345 1.9543 0.0539  0.1208  -0.1158 184 ASP D O   
14222 C CB  . ASP D 184 ? 0.2955 0.3177 1.9104 0.0461  0.1345  -0.1275 184 ASP D CB  
14223 C CG  . ASP D 184 ? 0.3154 0.3294 1.9215 0.0469  0.1429  -0.1395 184 ASP D CG  
14224 O OD1 . ASP D 184 ? 0.3266 0.3423 1.9537 0.0546  0.1481  -0.1498 184 ASP D OD1 
14225 O OD2 . ASP D 184 ? 0.3165 0.3232 1.8960 0.0399  0.1442  -0.1391 184 ASP D OD2 
14226 N N   . VAL D 185 ? 0.3041 0.3229 1.9287 0.0489  0.1059  -0.1044 185 VAL D N   
14227 C CA  . VAL D 185 ? 0.2879 0.3148 1.9130 0.0450  0.1014  -0.0945 185 VAL D CA  
14228 C C   . VAL D 185 ? 0.2787 0.2925 1.8991 0.0481  0.0872  -0.0875 185 VAL D C   
14229 O O   . VAL D 185 ? 0.2979 0.2957 1.9037 0.0483  0.0832  -0.0874 185 VAL D O   
14230 C CB  . VAL D 185 ? 0.2918 0.3222 1.8948 0.0348  0.1076  -0.0899 185 VAL D CB  
14231 C CG1 . VAL D 185 ? 0.2837 0.3200 1.8848 0.0304  0.1026  -0.0793 185 VAL D CG1 
14232 C CG2 . VAL D 185 ? 0.3005 0.3411 1.9029 0.0314  0.1222  -0.0962 185 VAL D CG2 
14233 N N   . TYR D 186 ? 0.2586 0.2779 1.8909 0.0502  0.0800  -0.0823 186 TYR D N   
14234 C CA  . TYR D 186 ? 0.2653 0.2718 1.8877 0.0514  0.0678  -0.0748 186 TYR D CA  
14235 C C   . TYR D 186 ? 0.2712 0.2785 1.8747 0.0422  0.0693  -0.0668 186 TYR D C   
14236 O O   . TYR D 186 ? 0.2888 0.3098 1.8943 0.0368  0.0758  -0.0651 186 TYR D O   
14237 C CB  . TYR D 186 ? 0.2640 0.2753 1.9068 0.0580  0.0589  -0.0742 186 TYR D CB  
14238 C CG  . TYR D 186 ? 0.2905 0.3001 1.9541 0.0682  0.0551  -0.0823 186 TYR D CG  
14239 C CD1 . TYR D 186 ? 0.2998 0.2925 1.9556 0.0729  0.0526  -0.0856 186 TYR D CD1 
14240 C CD2 . TYR D 186 ? 0.2744 0.2992 1.9680 0.0731  0.0540  -0.0870 186 TYR D CD2 
14241 C CE1 . TYR D 186 ? 0.3118 0.3024 1.9883 0.0829  0.0485  -0.0931 186 TYR D CE1 
14242 C CE2 . TYR D 186 ? 0.2720 0.2963 1.9884 0.0830  0.0498  -0.0950 186 TYR D CE2 
14243 C CZ  . TYR D 186 ? 0.3032 0.3102 2.0108 0.0883  0.0468  -0.0980 186 TYR D CZ  
14244 O OH  . TYR D 186 ? 0.3266 0.3315 2.0571 0.0989  0.0422  -0.1061 186 TYR D OH  
14245 N N   . ALA D 187 ? 0.2694 0.2617 1.8552 0.0404  0.0636  -0.0617 187 ALA D N   
14246 C CA  . ALA D 187 ? 0.2535 0.2466 1.8249 0.0325  0.0643  -0.0549 187 ALA D CA  
14247 C C   . ALA D 187 ? 0.2580 0.2355 1.8177 0.0330  0.0566  -0.0493 187 ALA D C   
14248 O O   . ALA D 187 ? 0.2747 0.2364 1.8290 0.0372  0.0526  -0.0507 187 ALA D O   
14249 C CB  . ALA D 187 ? 0.2573 0.2505 1.8163 0.0263  0.0713  -0.0571 187 ALA D CB  
14250 N N   . TYR D 188 ? 0.2505 0.2311 1.8052 0.0286  0.0551  -0.0431 188 TYR D N   
14251 C CA  . TYR D 188 ? 0.2787 0.2443 1.8196 0.0275  0.0506  -0.0381 188 TYR D CA  
14252 C C   . TYR D 188 ? 0.2873 0.2571 1.8209 0.0197  0.0538  -0.0333 188 TYR D C   
14253 O O   . TYR D 188 ? 0.2828 0.2672 1.8226 0.0162  0.0566  -0.0320 188 TYR D O   
14254 C CB  . TYR D 188 ? 0.2785 0.2394 1.8237 0.0338  0.0422  -0.0363 188 TYR D CB  
14255 C CG  . TYR D 188 ? 0.3046 0.2556 1.8546 0.0425  0.0361  -0.0401 188 TYR D CG  
14256 C CD1 . TYR D 188 ? 0.3237 0.2529 1.8589 0.0450  0.0324  -0.0390 188 TYR D CD1 
14257 C CD2 . TYR D 188 ? 0.3010 0.2638 1.8717 0.0483  0.0337  -0.0448 188 TYR D CD2 
14258 C CE1 . TYR D 188 ? 0.3329 0.2516 1.8728 0.0536  0.0253  -0.0419 188 TYR D CE1 
14259 C CE2 . TYR D 188 ? 0.3152 0.2696 1.8935 0.0570  0.0269  -0.0487 188 TYR D CE2 
14260 C CZ  . TYR D 188 ? 0.3384 0.2702 1.9008 0.0601  0.0220  -0.0471 188 TYR D CZ  
14261 O OH  . TYR D 188 ? 0.3865 0.3092 1.9575 0.0695  0.0142  -0.0508 188 TYR D OH  
14262 N N   . ASN D 189 ? 0.2999 0.2559 1.8205 0.0170  0.0534  -0.0305 189 ASN D N   
14263 C CA  . ASN D 189 ? 0.3039 0.2630 1.8207 0.0109  0.0555  -0.0263 189 ASN D CA  
14264 C C   . ASN D 189 ? 0.2956 0.2495 1.8098 0.0137  0.0511  -0.0227 189 ASN D C   
14265 O O   . ASN D 189 ? 0.3168 0.2535 1.8189 0.0157  0.0487  -0.0212 189 ASN D O   
14266 C CB  . ASN D 189 ? 0.3225 0.2719 1.8299 0.0053  0.0593  -0.0263 189 ASN D CB  
14267 C CG  . ASN D 189 ? 0.3322 0.2890 1.8424 0.0016  0.0626  -0.0303 189 ASN D CG  
14268 O OD1 . ASN D 189 ? 0.3284 0.2999 1.8454 0.0011  0.0633  -0.0315 189 ASN D OD1 
14269 N ND2 . ASN D 189 ? 0.3478 0.2938 1.8516 -0.0017 0.0647  -0.0325 189 ASN D ND2 
14270 N N   . CYS D 190 ? 0.2596 0.2270 1.7837 0.0136  0.0500  -0.0213 190 CYS D N   
14271 C CA  . CYS D 190 ? 0.2583 0.2224 1.7822 0.0170  0.0446  -0.0195 190 CYS D CA  
14272 C C   . CYS D 190 ? 0.2354 0.2001 1.7553 0.0122  0.0472  -0.0162 190 CYS D C   
14273 O O   . CYS D 190 ? 0.2117 0.1896 1.7407 0.0084  0.0501  -0.0151 190 CYS D O   
14274 C CB  . CYS D 190 ? 0.2623 0.2404 1.8029 0.0204  0.0415  -0.0213 190 CYS D CB  
14275 S SG  . CYS D 190 ? 0.2892 0.2701 1.8399 0.0260  0.0405  -0.0267 190 CYS D SG  
14276 N N   . TYR D 191 ? 0.2357 0.1849 1.7414 0.0127  0.0462  -0.0147 191 TYR D N   
14277 C CA  . TYR D 191 ? 0.2387 0.1873 1.7411 0.0086  0.0498  -0.0127 191 TYR D CA  
14278 C C   . TYR D 191 ? 0.2679 0.2058 1.7606 0.0124  0.0444  -0.0124 191 TYR D C   
14279 O O   . TYR D 191 ? 0.2612 0.1817 1.7381 0.0159  0.0408  -0.0121 191 TYR D O   
14280 C CB  . TYR D 191 ? 0.2373 0.1778 1.7309 0.0029  0.0574  -0.0118 191 TYR D CB  
14281 C CG  . TYR D 191 ? 0.2189 0.1710 1.7229 -0.0017 0.0615  -0.0128 191 TYR D CG  
14282 C CD1 . TYR D 191 ? 0.2130 0.1798 1.7295 -0.0054 0.0635  -0.0121 191 TYR D CD1 
14283 C CD2 . TYR D 191 ? 0.2230 0.1705 1.7240 -0.0020 0.0623  -0.0146 191 TYR D CD2 
14284 C CE1 . TYR D 191 ? 0.2055 0.1819 1.7297 -0.0094 0.0654  -0.0130 191 TYR D CE1 
14285 C CE2 . TYR D 191 ? 0.2155 0.1728 1.7243 -0.0064 0.0649  -0.0162 191 TYR D CE2 
14286 C CZ  . TYR D 191 ? 0.2020 0.1736 1.7216 -0.0101 0.0660  -0.0153 191 TYR D CZ  
14287 O OH  . TYR D 191 ? 0.1916 0.1727 1.7177 -0.0140 0.0665  -0.0168 191 TYR D OH  
14288 N N   . ASP D 192 ? 0.3014 0.2488 1.8029 0.0115  0.0438  -0.0123 192 ASP D N   
14289 C CA  . ASP D 192 ? 0.3318 0.2714 1.8261 0.0143  0.0387  -0.0130 192 ASP D CA  
14290 C C   . ASP D 192 ? 0.3392 0.2699 1.8215 0.0103  0.0457  -0.0124 192 ASP D C   
14291 O O   . ASP D 192 ? 0.3650 0.3065 1.8590 0.0072  0.0495  -0.0126 192 ASP D O   
14292 C CB  . ASP D 192 ? 0.3460 0.3012 1.8591 0.0152  0.0347  -0.0141 192 ASP D CB  
14293 C CG  . ASP D 192 ? 0.3991 0.3472 1.9069 0.0181  0.0279  -0.0161 192 ASP D CG  
14294 O OD1 . ASP D 192 ? 0.4161 0.3455 1.9019 0.0198  0.0262  -0.0164 192 ASP D OD1 
14295 O OD2 . ASP D 192 ? 0.4096 0.3696 1.9341 0.0183  0.0246  -0.0174 192 ASP D OD2 
14296 N N   . HIS D 193 ? 0.3523 0.2630 1.8121 0.0101  0.0481  -0.0117 193 HIS D N   
14297 C CA  . HIS D 193 ? 0.3642 0.2638 1.8099 0.0067  0.0556  -0.0118 193 HIS D CA  
14298 C C   . HIS D 193 ? 0.3930 0.2748 1.8170 0.0108  0.0490  -0.0128 193 HIS D C   
14299 O O   . HIS D 193 ? 0.4213 0.2855 1.8231 0.0089  0.0547  -0.0125 193 HIS D O   
14300 C CB  . HIS D 193 ? 0.3831 0.2707 1.8163 0.0020  0.0655  -0.0102 193 HIS D CB  
14301 C CG  . HIS D 193 ? 0.3785 0.2791 1.8286 -0.0018 0.0700  -0.0098 193 HIS D CG  
14302 N ND1 . HIS D 193 ? 0.3739 0.2937 1.8457 -0.0055 0.0740  -0.0107 193 HIS D ND1 
14303 C CD2 . HIS D 193 ? 0.3698 0.2657 1.8172 -0.0022 0.0701  -0.0088 193 HIS D CD2 
14304 C CE1 . HIS D 193 ? 0.3649 0.2913 1.8454 -0.0082 0.0759  -0.0105 193 HIS D CE1 
14305 N NE2 . HIS D 193 ? 0.3696 0.2818 1.8358 -0.0063 0.0740  -0.0097 193 HIS D NE2 
14306 N N   . ASN D 194 ? 0.4109 0.2966 1.8407 0.0165  0.0367  -0.0142 194 ASN D N   
14307 C CA  . ASN D 194 ? 0.4231 0.2922 1.8330 0.0210  0.0274  -0.0157 194 ASN D CA  
14308 C C   . ASN D 194 ? 0.4451 0.2865 1.8205 0.0208  0.0302  -0.0132 194 ASN D C   
14309 O O   . ASN D 194 ? 0.4627 0.2895 1.8168 0.0195  0.0331  -0.0143 194 ASN D O   
14310 C CB  . ASN D 194 ? 0.4051 0.2796 1.8200 0.0200  0.0274  -0.0192 194 ASN D CB  
14311 C CG  . ASN D 194 ? 0.4454 0.3027 1.8390 0.0245  0.0164  -0.0218 194 ASN D CG  
14312 O OD1 . ASN D 194 ? 0.4719 0.3159 1.8458 0.0227  0.0208  -0.0237 194 ASN D OD1 
14313 N ND2 . ASN D 194 ? 0.4783 0.3357 1.8762 0.0305  0.0019  -0.0227 194 ASN D ND2 
14314 N N   . GLU D 195 ? 0.4265 0.2589 1.7949 0.0220  0.0295  -0.0100 195 GLU D N   
14315 C CA  . GLU D 195 ? 0.4460 0.2493 1.7803 0.0222  0.0309  -0.0065 195 GLU D CA  
14316 C C   . GLU D 195 ? 0.4526 0.2467 1.7833 0.0286  0.0194  -0.0043 195 GLU D C   
14317 O O   . GLU D 195 ? 0.4296 0.2408 1.7854 0.0304  0.0167  -0.0053 195 GLU D O   
14318 C CB  . GLU D 195 ? 0.4358 0.2338 1.7636 0.0142  0.0481  -0.0042 195 GLU D CB  
14319 C CG  . GLU D 195 ? 0.4078 0.2218 1.7596 0.0119  0.0521  -0.0036 195 GLU D CG  
14320 C CD  . GLU D 195 ? 0.4036 0.2201 1.7601 0.0036  0.0677  -0.0030 195 GLU D CD  
14321 O OE1 . GLU D 195 ? 0.4259 0.2304 1.7666 -0.0013 0.0785  -0.0026 195 GLU D OE1 
14322 O OE2 . GLU D 195 ? 0.3726 0.2043 1.7503 0.0020  0.0689  -0.0035 195 GLU D OE2 
14323 N N   . GLY D 196 ? 0.4784 0.2440 1.7767 0.0321  0.0130  -0.0012 196 GLY D N   
14324 C CA  . GLY D 196 ? 0.5025 0.2572 1.7974 0.0394  0.0002  0.0009  196 GLY D CA  
14325 C C   . GLY D 196 ? 0.4860 0.2622 1.8114 0.0463  -0.0137 -0.0036 196 GLY D C   
14326 O O   . GLY D 196 ? 0.5038 0.2828 1.8300 0.0499  -0.0240 -0.0067 196 GLY D O   
14327 N N   . GLN D 197 ? 0.4612 0.2533 1.8125 0.0476  -0.0128 -0.0047 197 GLN D N   
14328 C CA  . GLN D 197 ? 0.4506 0.2616 1.8312 0.0541  -0.0242 -0.0091 197 GLN D CA  
14329 C C   . GLN D 197 ? 0.4307 0.2671 1.8355 0.0516  -0.0230 -0.0133 197 GLN D C   
14330 O O   . GLN D 197 ? 0.4469 0.2923 1.8673 0.0569  -0.0351 -0.0171 197 GLN D O   
14331 C CB  . GLN D 197 ? 0.4430 0.2641 1.8437 0.0551  -0.0206 -0.0099 197 GLN D CB  
14332 C CG  . GLN D 197 ? 0.4792 0.2750 1.8607 0.0596  -0.0254 -0.0065 197 GLN D CG  
14333 C CD  . GLN D 197 ? 0.4872 0.2695 1.8510 0.0523  -0.0113 -0.0023 197 GLN D CD  
14334 O OE1 . GLN D 197 ? 0.4698 0.2412 1.8124 0.0459  -0.0026 0.0008  197 GLN D OE1 
14335 N NE2 . GLN D 197 ? 0.5036 0.2868 1.8778 0.0531  -0.0085 -0.0029 197 GLN D NE2 
14336 N N   . THR D 198 ? 0.3939 0.2415 1.8034 0.0437  -0.0091 -0.0128 198 THR D N   
14337 C CA  . THR D 198 ? 0.3565 0.2266 1.7886 0.0410  -0.0072 -0.0160 198 THR D CA  
14338 C C   . THR D 198 ? 0.3769 0.2375 1.7936 0.0410  -0.0115 -0.0173 198 THR D C   
14339 O O   . THR D 198 ? 0.3593 0.2350 1.7924 0.0390  -0.0111 -0.0201 198 THR D O   
14340 C CB  . THR D 198 ? 0.3249 0.2107 1.7699 0.0335  0.0076  -0.0149 198 THR D CB  
14341 O OG1 . THR D 198 ? 0.3447 0.2159 1.7679 0.0284  0.0175  -0.0122 198 THR D OG1 
14342 C CG2 . THR D 198 ? 0.3033 0.2012 1.7657 0.0336  0.0107  -0.0151 198 THR D CG2 
14343 N N   . ALA D 199 ? 0.4143 0.2483 1.7978 0.0428  -0.0152 -0.0153 199 ALA D N   
14344 C CA  . ALA D 199 ? 0.4273 0.2489 1.7909 0.0430  -0.0197 -0.0173 199 ALA D CA  
14345 C C   . ALA D 199 ? 0.4488 0.2637 1.8104 0.0513  -0.0397 -0.0201 199 ALA D C   
14346 O O   . ALA D 199 ? 0.4341 0.2526 1.7993 0.0523  -0.0473 -0.0245 199 ALA D O   
14347 C CB  . ALA D 199 ? 0.4436 0.2393 1.7697 0.0393  -0.0105 -0.0138 199 ALA D CB  
14348 N N   . THR D 200 ? 0.4639 0.2689 1.8213 0.0573  -0.0490 -0.0179 200 THR D N   
14349 C CA  . THR D 200 ? 0.4926 0.2921 1.8519 0.0659  -0.0696 -0.0208 200 THR D CA  
14350 C C   . THR D 200 ? 0.4660 0.2957 1.8704 0.0681  -0.0749 -0.0261 200 THR D C   
14351 O O   . THR D 200 ? 0.4665 0.3037 1.8833 0.0704  -0.0858 -0.0311 200 THR D O   
14352 C CB  . THR D 200 ? 0.5343 0.3108 1.8733 0.0720  -0.0778 -0.0164 200 THR D CB  
14353 O OG1 . THR D 200 ? 0.5191 0.3097 1.8825 0.0721  -0.0711 -0.0155 200 THR D OG1 
14354 C CG2 . THR D 200 ? 0.5663 0.3112 1.8588 0.0687  -0.0710 -0.0106 200 THR D CG2 
14355 N N   . MET D 201 ? 0.4472 0.2939 1.8765 0.0671  -0.0666 -0.0254 201 MET D N   
14356 C CA  . MET D 201 ? 0.4232 0.2962 1.8933 0.0693  -0.0706 -0.0303 201 MET D CA  
14357 C C   . MET D 201 ? 0.3789 0.2744 1.8693 0.0616  -0.0580 -0.0315 201 MET D C   
14358 O O   . MET D 201 ? 0.3718 0.2870 1.8919 0.0617  -0.0610 -0.0357 201 MET D O   
14359 C CB  . MET D 201 ? 0.4265 0.3050 1.9118 0.0727  -0.0685 -0.0298 201 MET D CB  
14360 C CG  . MET D 201 ? 0.4504 0.3062 1.9186 0.0813  -0.0823 -0.0285 201 MET D CG  
14361 S SD  . MET D 201 ? 0.4704 0.3256 1.9474 0.0842  -0.0764 -0.0271 201 MET D SD  
14362 C CE  . MET D 201 ? 0.5052 0.3398 1.9438 0.0758  -0.0608 -0.0196 201 MET D CE  
14363 N N   . GLY D 202 ? 0.3572 0.2490 1.8322 0.0548  -0.0437 -0.0278 202 GLY D N   
14364 C CA  . GLY D 202 ? 0.3198 0.2322 1.8146 0.0481  -0.0318 -0.0279 202 GLY D CA  
14365 C C   . GLY D 202 ? 0.2954 0.2244 1.8111 0.0465  -0.0233 -0.0270 202 GLY D C   
14366 O O   . GLY D 202 ? 0.2882 0.2170 1.8109 0.0514  -0.0280 -0.0281 202 GLY D O   
14367 N N   . PHE D 203 ? 0.2764 0.2188 1.8014 0.0398  -0.0111 -0.0253 203 PHE D N   
14368 C CA  . PHE D 203 ? 0.2602 0.2149 1.7969 0.0368  -0.0012 -0.0237 203 PHE D CA  
14369 C C   . PHE D 203 ? 0.2567 0.2271 1.8196 0.0400  -0.0045 -0.0271 203 PHE D C   
14370 O O   . PHE D 203 ? 0.2496 0.2193 1.8149 0.0429  -0.0038 -0.0280 203 PHE D O   
14371 C CB  . PHE D 203 ? 0.2393 0.2037 1.7796 0.0295  0.0094  -0.0212 203 PHE D CB  
14372 C CG  . PHE D 203 ? 0.2305 0.2019 1.7733 0.0256  0.0193  -0.0190 203 PHE D CG  
14373 C CD1 . PHE D 203 ? 0.2463 0.2056 1.7735 0.0259  0.0221  -0.0180 203 PHE D CD1 
14374 C CD2 . PHE D 203 ? 0.2120 0.2008 1.7717 0.0216  0.0253  -0.0180 203 PHE D CD2 
14375 C CE1 . PHE D 203 ? 0.2364 0.2020 1.7663 0.0221  0.0300  -0.0170 203 PHE D CE1 
14376 C CE2 . PHE D 203 ? 0.2055 0.1995 1.7650 0.0182  0.0328  -0.0165 203 PHE D CE2 
14377 C CZ  . PHE D 203 ? 0.2189 0.2018 1.7643 0.0184  0.0349  -0.0164 203 PHE D CZ  
14378 N N   . LYS D 204 ? 0.2547 0.2389 1.8385 0.0393  -0.0073 -0.0294 204 LYS D N   
14379 C CA  . LYS D 204 ? 0.2576 0.2583 1.8689 0.0412  -0.0076 -0.0329 204 LYS D CA  
14380 C C   . LYS D 204 ? 0.2877 0.2813 1.9012 0.0492  -0.0177 -0.0366 204 LYS D C   
14381 O O   . LYS D 204 ? 0.2980 0.2975 1.9218 0.0512  -0.0137 -0.0384 204 LYS D O   
14382 C CB  . LYS D 204 ? 0.2623 0.2758 1.8958 0.0395  -0.0109 -0.0353 204 LYS D CB  
14383 C CG  . LYS D 204 ? 0.2583 0.2877 1.9231 0.0420  -0.0129 -0.0403 204 LYS D CG  
14384 C CD  . LYS D 204 ? 0.2515 0.2880 1.9369 0.0424  -0.0217 -0.0444 204 LYS D CD  
14385 C CE  . LYS D 204 ? 0.2238 0.2758 1.9434 0.0454  -0.0248 -0.0505 204 LYS D CE  
14386 N NZ  . LYS D 204 ? 0.2162 0.2687 1.9506 0.0484  -0.0394 -0.0558 204 LYS D NZ  
14387 N N   . ASP D 205 ? 0.3026 0.2821 1.9052 0.0543  -0.0311 -0.0379 205 ASP D N   
14388 C CA  . ASP D 205 ? 0.2975 0.2699 1.9043 0.0629  -0.0437 -0.0414 205 ASP D CA  
14389 C C   . ASP D 205 ? 0.3207 0.2785 1.9091 0.0657  -0.0411 -0.0389 205 ASP D C   
14390 O O   . ASP D 205 ? 0.3194 0.2804 1.9224 0.0713  -0.0440 -0.0421 205 ASP D O   
14391 C CB  . ASP D 205 ? 0.3028 0.2612 1.8983 0.0677  -0.0603 -0.0431 205 ASP D CB  
14392 C CG  . ASP D 205 ? 0.2801 0.2531 1.9018 0.0677  -0.0681 -0.0483 205 ASP D CG  
14393 O OD1 . ASP D 205 ? 0.2534 0.2484 1.9047 0.0637  -0.0595 -0.0504 205 ASP D OD1 
14394 O OD2 . ASP D 205 ? 0.2824 0.2433 1.8931 0.0712  -0.0824 -0.0503 205 ASP D OD2 
14395 N N   . TYR D 206 ? 0.3422 0.2837 1.9003 0.0620  -0.0357 -0.0336 206 TYR D N   
14396 C CA  . TYR D 206 ? 0.3597 0.2851 1.8994 0.0638  -0.0332 -0.0310 206 TYR D CA  
14397 C C   . TYR D 206 ? 0.3369 0.2773 1.8959 0.0626  -0.0233 -0.0332 206 TYR D C   
14398 O O   . TYR D 206 ? 0.3448 0.2814 1.9104 0.0687  -0.0274 -0.0357 206 TYR D O   
14399 C CB  . TYR D 206 ? 0.3838 0.2937 1.8934 0.0578  -0.0250 -0.0255 206 TYR D CB  
14400 C CG  . TYR D 206 ? 0.4071 0.3016 1.9002 0.0578  -0.0200 -0.0228 206 TYR D CG  
14401 C CD1 . TYR D 206 ? 0.4352 0.3132 1.9211 0.0654  -0.0298 -0.0229 206 TYR D CD1 
14402 C CD2 . TYR D 206 ? 0.3968 0.2927 1.8829 0.0503  -0.0062 -0.0202 206 TYR D CD2 
14403 C CE1 . TYR D 206 ? 0.4656 0.3277 1.9365 0.0651  -0.0252 -0.0203 206 TYR D CE1 
14404 C CE2 . TYR D 206 ? 0.4117 0.2935 1.8847 0.0496  -0.0017 -0.0183 206 TYR D CE2 
14405 C CZ  . TYR D 206 ? 0.4432 0.3074 1.9080 0.0568  -0.0107 -0.0182 206 TYR D CZ  
14406 O OH  . TYR D 206 ? 0.4766 0.3244 1.9283 0.0564  -0.0069 -0.0162 206 TYR D OH  
14407 N N   . ILE D 207 ? 0.3066 0.2636 1.8750 0.0553  -0.0112 -0.0326 207 ILE D N   
14408 C CA  . ILE D 207 ? 0.3064 0.2760 1.8883 0.0534  -0.0012 -0.0347 207 ILE D CA  
14409 C C   . ILE D 207 ? 0.3278 0.3109 1.9383 0.0591  -0.0051 -0.0408 207 ILE D C   
14410 O O   . ILE D 207 ? 0.3573 0.3418 1.9747 0.0618  -0.0014 -0.0440 207 ILE D O   
14411 C CB  . ILE D 207 ? 0.2840 0.2673 1.8682 0.0447  0.0110  -0.0323 207 ILE D CB  
14412 C CG1 . ILE D 207 ? 0.2827 0.2537 1.8430 0.0396  0.0152  -0.0274 207 ILE D CG1 
14413 C CG2 . ILE D 207 ? 0.2831 0.2787 1.8791 0.0429  0.0207  -0.0351 207 ILE D CG2 
14414 C CD1 . ILE D 207 ? 0.2913 0.2447 1.8336 0.0410  0.0158  -0.0266 207 ILE D CD1 
14415 N N   . LYS D 208 ? 0.3442 0.3371 1.9720 0.0605  -0.0119 -0.0430 208 LYS D N   
14416 C CA  . LYS D 208 ? 0.3536 0.3617 2.0134 0.0653  -0.0155 -0.0494 208 LYS D CA  
14417 C C   . LYS D 208 ? 0.3842 0.3801 2.0456 0.0753  -0.0275 -0.0528 208 LYS D C   
14418 O O   . LYS D 208 ? 0.3900 0.3957 2.0748 0.0797  -0.0261 -0.0586 208 LYS D O   
14419 C CB  . LYS D 208 ? 0.3547 0.3733 2.0315 0.0641  -0.0219 -0.0510 208 LYS D CB  
14420 C CG  . LYS D 208 ? 0.3741 0.4086 2.0879 0.0690  -0.0275 -0.0584 208 LYS D CG  
14421 C CD  . LYS D 208 ? 0.3882 0.4384 2.1248 0.0648  -0.0282 -0.0603 208 LYS D CD  
14422 C CE  . LYS D 208 ? 0.4007 0.4432 2.1358 0.0680  -0.0453 -0.0616 208 LYS D CE  
14423 N NZ  . LYS D 208 ? 0.4197 0.4640 2.1771 0.0772  -0.0601 -0.0685 208 LYS D NZ  
14424 N N   . GLY D 209 ? 0.4052 0.3786 2.0409 0.0789  -0.0389 -0.0491 209 GLY D N   
14425 C CA  . GLY D 209 ? 0.4136 0.3712 2.0462 0.0888  -0.0523 -0.0508 209 GLY D CA  
14426 C C   . GLY D 209 ? 0.4005 0.3516 2.0289 0.0904  -0.0446 -0.0513 209 GLY D C   
14427 O O   . GLY D 209 ? 0.3983 0.3467 2.0409 0.0988  -0.0516 -0.0556 209 GLY D O   
14428 N N   . LEU D 210 ? 0.3899 0.3384 2.0001 0.0825  -0.0307 -0.0473 210 LEU D N   
14429 C CA  . LEU D 210 ? 0.4048 0.3486 2.0124 0.0830  -0.0227 -0.0488 210 LEU D CA  
14430 C C   . LEU D 210 ? 0.3958 0.3619 2.0364 0.0847  -0.0157 -0.0566 210 LEU D C   
14431 O O   . LEU D 210 ? 0.4003 0.3634 2.0523 0.0914  -0.0175 -0.0616 210 LEU D O   
14432 C CB  . LEU D 210 ? 0.3950 0.3327 1.9789 0.0738  -0.0103 -0.0439 210 LEU D CB  
14433 C CG  . LEU D 210 ? 0.4154 0.3308 1.9675 0.0715  -0.0144 -0.0367 210 LEU D CG  
14434 C CD1 . LEU D 210 ? 0.4209 0.3344 1.9563 0.0619  -0.0013 -0.0330 210 LEU D CD1 
14435 C CD2 . LEU D 210 ? 0.4204 0.3098 1.9567 0.0791  -0.0256 -0.0349 210 LEU D CD2 
14436 N N   . ASN D 211 ? 0.3605 0.3480 2.0174 0.0791  -0.0085 -0.0579 211 ASN D N   
14437 C CA  . ASN D 211 ? 0.3418 0.3502 2.0268 0.0787  0.0015  -0.0647 211 ASN D CA  
14438 C C   . ASN D 211 ? 0.3576 0.3716 2.0727 0.0887  -0.0083 -0.0721 211 ASN D C   
14439 O O   . ASN D 211 ? 0.3510 0.3741 2.0863 0.0919  -0.0015 -0.0791 211 ASN D O   
14440 C CB  . ASN D 211 ? 0.3057 0.3333 1.9996 0.0700  0.0119  -0.0634 211 ASN D CB  
14441 C CG  . ASN D 211 ? 0.3111 0.3520 2.0151 0.0664  0.0279  -0.0678 211 ASN D CG  
14442 O OD1 . ASN D 211 ? 0.3638 0.3960 2.0550 0.0668  0.0329  -0.0692 211 ASN D OD1 
14443 N ND2 . ASN D 211 ? 0.3039 0.3642 2.0291 0.0624  0.0363  -0.0702 211 ASN D ND2 
14444 N N   . GLU D 212 ? 0.3577 0.3655 2.0754 0.0939  -0.0248 -0.0710 212 GLU D N   
14445 C CA  . GLU D 212 ? 0.3547 0.3671 2.1019 0.1042  -0.0378 -0.0779 212 GLU D CA  
14446 C C   . GLU D 212 ? 0.3761 0.3690 2.1155 0.1136  -0.0462 -0.0790 212 GLU D C   
14447 O O   . GLU D 212 ? 0.3810 0.3807 2.1491 0.1217  -0.0495 -0.0867 212 GLU D O   
14448 C CB  . GLU D 212 ? 0.3452 0.3580 2.0972 0.1059  -0.0534 -0.0767 212 GLU D CB  
14449 C CG  . GLU D 212 ? 0.3329 0.3711 2.1119 0.0991  -0.0451 -0.0798 212 GLU D CG  
14450 C CD  . GLU D 212 ? 0.3525 0.3896 2.1269 0.0967  -0.0560 -0.0770 212 GLU D CD  
14451 O OE1 . GLU D 212 ? 0.4087 0.4240 2.1562 0.1008  -0.0701 -0.0729 212 GLU D OE1 
14452 O OE2 . GLU D 212 ? 0.3299 0.3851 2.1243 0.0906  -0.0501 -0.0787 212 GLU D OE2 
14453 N N   . LEU D 213 ? 0.3866 0.3546 2.0883 0.1125  -0.0492 -0.0715 213 LEU D N   
14454 C CA  . LEU D 213 ? 0.3984 0.3458 2.0899 0.1200  -0.0546 -0.0716 213 LEU D CA  
14455 C C   . LEU D 213 ? 0.3819 0.3380 2.0830 0.1175  -0.0376 -0.0769 213 LEU D C   
14456 O O   . LEU D 213 ? 0.3717 0.3215 2.0841 0.1253  -0.0404 -0.0819 213 LEU D O   
14457 C CB  . LEU D 213 ? 0.4293 0.3473 2.0776 0.1179  -0.0597 -0.0620 213 LEU D CB  
14458 C CG  . LEU D 213 ? 0.4440 0.3460 2.0765 0.1224  -0.0785 -0.0571 213 LEU D CG  
14459 C CD1 . LEU D 213 ? 0.4487 0.3269 2.0369 0.1160  -0.0764 -0.0475 213 LEU D CD1 
14460 C CD2 . LEU D 213 ? 0.4475 0.3357 2.0896 0.1357  -0.0970 -0.0597 213 LEU D CD2 
14461 N N   . ASN D 214 ? 0.3761 0.3452 2.0715 0.1068  -0.0205 -0.0760 214 ASN D N   
14462 C CA  . ASN D 214 ? 0.3624 0.3376 2.0637 0.1047  -0.0055 -0.0817 214 ASN D CA  
14463 C C   . ASN D 214 ? 0.3431 0.3398 2.0842 0.1097  -0.0009 -0.0922 214 ASN D C   
14464 O O   . ASN D 214 ? 0.3607 0.3599 2.1088 0.1107  0.0096  -0.0987 214 ASN D O   
14465 C CB  . ASN D 214 ? 0.3465 0.3277 2.0293 0.0927  0.0104  -0.0784 214 ASN D CB  
14466 C CG  . ASN D 214 ? 0.3729 0.3319 2.0203 0.0885  0.0082  -0.0702 214 ASN D CG  
14467 O OD1 . ASN D 214 ? 0.3865 0.3245 2.0227 0.0940  0.0009  -0.0692 214 ASN D OD1 
14468 N ND2 . ASN D 214 ? 0.3966 0.3590 2.0274 0.0791  0.0138  -0.0641 214 ASN D ND2 
14469 N N   . GLY D 215 ? 0.3194 0.3318 2.0862 0.1121  -0.0075 -0.0944 215 GLY D N   
14470 C CA  . GLY D 215 ? 0.3024 0.3339 2.1119 0.1184  -0.0062 -0.1049 215 GLY D CA  
14471 C C   . GLY D 215 ? 0.2839 0.3423 2.1146 0.1103  0.0111  -0.1090 215 GLY D C   
14472 O O   . GLY D 215 ? 0.2903 0.3660 2.1568 0.1139  0.0169  -0.1185 215 GLY D O   
14473 N N   . LEU D 216 ? 0.2702 0.3321 2.0801 0.0992  0.0202  -0.1021 216 LEU D N   
14474 C CA  . LEU D 216 ? 0.2471 0.3317 2.0746 0.0912  0.0346  -0.1041 216 LEU D CA  
14475 C C   . LEU D 216 ? 0.2408 0.3382 2.0839 0.0897  0.0537  -0.1127 216 LEU D C   
14476 O O   . LEU D 216 ? 0.2169 0.3336 2.0820 0.0851  0.0659  -0.1165 216 LEU D O   
14477 C CB  . LEU D 216 ? 0.2487 0.3455 2.1079 0.0949  0.0231  -0.1066 216 LEU D CB  
14478 C CG  . LEU D 216 ? 0.2620 0.3460 2.1046 0.0960  0.0043  -0.0990 216 LEU D CG  
14479 C CD1 . LEU D 216 ? 0.2512 0.3509 2.1280 0.0977  -0.0049 -0.1028 216 LEU D CD1 
14480 C CD2 . LEU D 216 ? 0.2582 0.3332 2.0632 0.0860  0.0092  -0.0885 216 LEU D CD2 
14481 N N   . ASP D 217 ? 0.2634 0.3492 2.0920 0.0924  0.0584  -0.1158 217 ASP D N   
14482 C CA  . ASP D 217 ? 0.2674 0.3638 2.1104 0.0920  0.0762  -0.1257 217 ASP D CA  
14483 C C   . ASP D 217 ? 0.2756 0.3675 2.0855 0.0822  0.0916  -0.1227 217 ASP D C   
14484 O O   . ASP D 217 ? 0.2732 0.3678 2.0848 0.0819  0.1054  -0.1307 217 ASP D O   
14485 C CB  . ASP D 217 ? 0.2745 0.3623 2.1319 0.1036  0.0706  -0.1344 217 ASP D CB  
14486 C CG  . ASP D 217 ? 0.2914 0.3528 2.1170 0.1069  0.0594  -0.1290 217 ASP D CG  
14487 O OD1 . ASP D 217 ? 0.3064 0.3573 2.1044 0.1018  0.0520  -0.1184 217 ASP D OD1 
14488 O OD2 . ASP D 217 ? 0.3125 0.3641 2.1415 0.1138  0.0594  -0.1357 217 ASP D OD2 
14489 N N   . LYS D 218 ? 0.2714 0.3562 2.0516 0.0744  0.0886  -0.1118 218 LYS D N   
14490 C CA  . LYS D 218 ? 0.2817 0.3620 2.0310 0.0654  0.1003  -0.1086 218 LYS D CA  
14491 C C   . LYS D 218 ? 0.2654 0.3489 1.9985 0.0562  0.1001  -0.0980 218 LYS D C   
14492 O O   . LYS D 218 ? 0.2540 0.3376 1.9924 0.0571  0.0887  -0.0923 218 LYS D O   
14493 C CB  . LYS D 218 ? 0.3159 0.3754 2.0388 0.0673  0.0945  -0.1075 218 LYS D CB  
14494 C CG  . LYS D 218 ? 0.3493 0.4021 2.0876 0.0773  0.0927  -0.1176 218 LYS D CG  
14495 C CD  . LYS D 218 ? 0.3614 0.3942 2.0780 0.0791  0.0908  -0.1193 218 LYS D CD  
14496 C CE  . LYS D 218 ? 0.3842 0.4163 2.1241 0.0887  0.0930  -0.1312 218 LYS D CE  
14497 N NZ  . LYS D 218 ? 0.4186 0.4300 2.1388 0.0904  0.0909  -0.1332 218 LYS D NZ  
14498 N N   . PRO D 219 ? 0.2578 0.3434 1.9703 0.0472  0.1124  -0.0955 219 PRO D N   
14499 C CA  . PRO D 219 ? 0.2467 0.3308 1.9392 0.0392  0.1103  -0.0849 219 PRO D CA  
14500 C C   . PRO D 219 ? 0.2546 0.3227 1.9296 0.0415  0.0958  -0.0791 219 PRO D C   
14501 O O   . PRO D 219 ? 0.2885 0.3439 1.9547 0.0456  0.0920  -0.0823 219 PRO D O   
14502 C CB  . PRO D 219 ? 0.2540 0.3383 1.9243 0.0316  0.1236  -0.0849 219 PRO D CB  
14503 C CG  . PRO D 219 ? 0.2649 0.3578 1.9519 0.0339  0.1369  -0.0955 219 PRO D CG  
14504 C CD  . PRO D 219 ? 0.2694 0.3574 1.9753 0.0446  0.1281  -0.1028 219 PRO D CD  
14505 N N   . PHE D 220 ? 0.2539 0.3221 1.9251 0.0384  0.0886  -0.0708 220 PHE D N   
14506 C CA  . PHE D 220 ? 0.2629 0.3171 1.9159 0.0386  0.0774  -0.0643 220 PHE D CA  
14507 C C   . PHE D 220 ? 0.2711 0.3269 1.9072 0.0299  0.0801  -0.0563 220 PHE D C   
14508 O O   . PHE D 220 ? 0.2520 0.3182 1.8971 0.0264  0.0823  -0.0529 220 PHE D O   
14509 C CB  . PHE D 220 ? 0.2567 0.3084 1.9229 0.0445  0.0645  -0.0630 220 PHE D CB  
14510 C CG  . PHE D 220 ? 0.2574 0.2978 1.9043 0.0420  0.0560  -0.0549 220 PHE D CG  
14511 C CD1 . PHE D 220 ? 0.2639 0.2888 1.8877 0.0410  0.0542  -0.0524 220 PHE D CD1 
14512 C CD2 . PHE D 220 ? 0.2384 0.2843 1.8908 0.0398  0.0517  -0.0504 220 PHE D CD2 
14513 C CE1 . PHE D 220 ? 0.2579 0.2735 1.8656 0.0381  0.0488  -0.0457 220 PHE D CE1 
14514 C CE2 . PHE D 220 ? 0.2349 0.2704 1.8698 0.0376  0.0455  -0.0441 220 PHE D CE2 
14515 C CZ  . PHE D 220 ? 0.2421 0.2629 1.8549 0.0367  0.0446  -0.0418 220 PHE D CZ  
14516 N N   . ILE D 221 ? 0.2714 0.3162 1.8848 0.0268  0.0789  -0.0534 221 ILE D N   
14517 C CA  . ILE D 221 ? 0.2843 0.3303 1.8832 0.0193  0.0803  -0.0465 221 ILE D CA  
14518 C C   . ILE D 221 ? 0.2974 0.3308 1.8835 0.0192  0.0718  -0.0420 221 ILE D C   
14519 O O   . ILE D 221 ? 0.3374 0.3592 1.9194 0.0234  0.0677  -0.0446 221 ILE D O   
14520 C CB  . ILE D 221 ? 0.3014 0.3490 1.8865 0.0142  0.0890  -0.0482 221 ILE D CB  
14521 C CG1 . ILE D 221 ? 0.3244 0.3597 1.8965 0.0155  0.0875  -0.0526 221 ILE D CG1 
14522 C CG2 . ILE D 221 ? 0.3034 0.3623 1.8991 0.0138  0.0996  -0.0530 221 ILE D CG2 
14523 C CD1 . ILE D 221 ? 0.3453 0.3807 1.9021 0.0106  0.0946  -0.0558 221 ILE D CD1 
14524 N N   . THR D 222 ? 0.2841 0.3190 1.8642 0.0145  0.0700  -0.0354 222 THR D N   
14525 C CA  . THR D 222 ? 0.2777 0.3016 1.8452 0.0130  0.0649  -0.0318 222 THR D CA  
14526 C C   . THR D 222 ? 0.2663 0.2890 1.8207 0.0075  0.0684  -0.0314 222 THR D C   
14527 O O   . THR D 222 ? 0.2645 0.2958 1.8173 0.0032  0.0724  -0.0298 222 THR D O   
14528 C CB  . THR D 222 ? 0.2796 0.3054 1.8498 0.0115  0.0609  -0.0261 222 THR D CB  
14529 O OG1 . THR D 222 ? 0.2746 0.3108 1.8459 0.0063  0.0652  -0.0228 222 THR D OG1 
14530 C CG2 . THR D 222 ? 0.2852 0.3130 1.8689 0.0166  0.0562  -0.0272 222 THR D CG2 
14531 N N   . THR D 223 ? 0.2717 0.2825 1.8164 0.0073  0.0664  -0.0325 223 THR D N   
14532 C CA  . THR D 223 ? 0.2660 0.2747 1.8003 0.0021  0.0683  -0.0334 223 THR D CA  
14533 C C   . THR D 223 ? 0.2655 0.2723 1.7963 -0.0023 0.0657  -0.0285 223 THR D C   
14534 O O   . THR D 223 ? 0.2862 0.2958 1.8125 -0.0072 0.0660  -0.0282 223 THR D O   
14535 C CB  . THR D 223 ? 0.2578 0.2550 1.7864 0.0040  0.0691  -0.0393 223 THR D CB  
14536 O OG1 . THR D 223 ? 0.2457 0.2323 1.7766 0.0094  0.0654  -0.0389 223 THR D OG1 
14537 C CG2 . THR D 223 ? 0.2610 0.2631 1.7913 0.0057  0.0739  -0.0455 223 THR D CG2 
14538 N N   . GLU D 224 ? 0.2612 0.2636 1.7947 -0.0003 0.0629  -0.0251 224 GLU D N   
14539 C CA  . GLU D 224 ? 0.2660 0.2693 1.7995 -0.0041 0.0618  -0.0208 224 GLU D CA  
14540 C C   . GLU D 224 ? 0.2469 0.2503 1.7853 -0.0013 0.0594  -0.0176 224 GLU D C   
14541 O O   . GLU D 224 ? 0.2419 0.2404 1.7811 0.0036  0.0572  -0.0189 224 GLU D O   
14542 C CB  . GLU D 224 ? 0.2892 0.2807 1.8156 -0.0067 0.0626  -0.0217 224 GLU D CB  
14543 C CG  . GLU D 224 ? 0.3015 0.2926 1.8243 -0.0108 0.0641  -0.0253 224 GLU D CG  
14544 C CD  . GLU D 224 ? 0.3082 0.2872 1.8266 -0.0140 0.0657  -0.0265 224 GLU D CD  
14545 O OE1 . GLU D 224 ? 0.3055 0.2777 1.8227 -0.0138 0.0667  -0.0236 224 GLU D OE1 
14546 O OE2 . GLU D 224 ? 0.3385 0.3139 1.8539 -0.0168 0.0665  -0.0306 224 GLU D OE2 
14547 N N   . PHE D 225 ? 0.2287 0.2365 1.7705 -0.0044 0.0591  -0.0141 225 PHE D N   
14548 C CA  . PHE D 225 ? 0.2179 0.2229 1.7619 -0.0027 0.0573  -0.0119 225 PHE D CA  
14549 C C   . PHE D 225 ? 0.2051 0.2165 1.7549 -0.0067 0.0581  -0.0089 225 PHE D C   
14550 O O   . PHE D 225 ? 0.2075 0.2284 1.7621 -0.0093 0.0580  -0.0074 225 PHE D O   
14551 C CB  . PHE D 225 ? 0.2083 0.2182 1.7598 0.0013  0.0544  -0.0117 225 PHE D CB  
14552 C CG  . PHE D 225 ? 0.1964 0.2201 1.7582 -0.0004 0.0554  -0.0097 225 PHE D CG  
14553 C CD1 . PHE D 225 ? 0.2079 0.2373 1.7766 -0.0024 0.0547  -0.0061 225 PHE D CD1 
14554 C CD2 . PHE D 225 ? 0.1954 0.2249 1.7589 -0.0002 0.0578  -0.0115 225 PHE D CD2 
14555 C CE1 . PHE D 225 ? 0.2091 0.2485 1.7851 -0.0044 0.0559  -0.0033 225 PHE D CE1 
14556 C CE2 . PHE D 225 ? 0.1892 0.2292 1.7590 -0.0025 0.0602  -0.0091 225 PHE D CE2 
14557 C CZ  . PHE D 225 ? 0.2012 0.2454 1.7766 -0.0047 0.0590  -0.0045 225 PHE D CZ  
14558 N N   . GLY D 226 ? 0.1848 0.1909 1.7342 -0.0069 0.0588  -0.0082 226 GLY D N   
14559 C CA  . GLY D 226 ? 0.1731 0.1855 1.7306 -0.0104 0.0599  -0.0064 226 GLY D CA  
14560 C C   . GLY D 226 ? 0.1785 0.1824 1.7333 -0.0115 0.0635  -0.0075 226 GLY D C   
14561 O O   . GLY D 226 ? 0.1858 0.1772 1.7288 -0.0097 0.0649  -0.0089 226 GLY D O   
14562 N N   . TYR D 227 ? 0.1789 0.1892 1.7445 -0.0141 0.0650  -0.0068 227 TYR D N   
14563 C CA  . TYR D 227 ? 0.1963 0.2000 1.7619 -0.0153 0.0702  -0.0085 227 TYR D CA  
14564 C C   . TYR D 227 ? 0.1820 0.1929 1.7609 -0.0196 0.0730  -0.0095 227 TYR D C   
14565 O O   . TYR D 227 ? 0.1484 0.1705 1.7379 -0.0205 0.0683  -0.0079 227 TYR D O   
14566 C CB  . TYR D 227 ? 0.2121 0.2155 1.7810 -0.0127 0.0694  -0.0082 227 TYR D CB  
14567 C CG  . TYR D 227 ? 0.2375 0.2325 1.7942 -0.0087 0.0661  -0.0085 227 TYR D CG  
14568 C CD1 . TYR D 227 ? 0.2795 0.2591 1.8198 -0.0076 0.0688  -0.0105 227 TYR D CD1 
14569 C CD2 . TYR D 227 ? 0.2414 0.2431 1.8027 -0.0061 0.0602  -0.0068 227 TYR D CD2 
14570 C CE1 . TYR D 227 ? 0.2976 0.2689 1.8268 -0.0033 0.0635  -0.0109 227 TYR D CE1 
14571 C CE2 . TYR D 227 ? 0.2771 0.2725 1.8312 -0.0023 0.0562  -0.0079 227 TYR D CE2 
14572 C CZ  . TYR D 227 ? 0.3100 0.2903 1.8482 -0.0006 0.0567  -0.0101 227 TYR D CZ  
14573 O OH  . TYR D 227 ? 0.3831 0.3568 1.9144 0.0038  0.0505  -0.0113 227 TYR D OH  
14574 N N   . SER D 228 ? 0.2034 0.2065 1.7803 -0.0222 0.0807  -0.0122 228 SER D N   
14575 C CA  . SER D 228 ? 0.2127 0.2220 1.8051 -0.0266 0.0849  -0.0145 228 SER D CA  
14576 C C   . SER D 228 ? 0.2104 0.2220 1.8148 -0.0264 0.0898  -0.0163 228 SER D C   
14577 O O   . SER D 228 ? 0.2118 0.2124 1.8052 -0.0256 0.0961  -0.0178 228 SER D O   
14578 C CB  . SER D 228 ? 0.2309 0.2306 1.8162 -0.0310 0.0921  -0.0171 228 SER D CB  
14579 O OG  . SER D 228 ? 0.2525 0.2564 1.8542 -0.0353 0.0993  -0.0203 228 SER D OG  
14580 N N   . VAL D 229 ? 0.2068 0.2320 1.8337 -0.0274 0.0868  -0.0167 229 VAL D N   
14581 C CA  . VAL D 229 ? 0.2187 0.2487 1.8632 -0.0270 0.0910  -0.0192 229 VAL D CA  
14582 C C   . VAL D 229 ? 0.2199 0.2540 1.8814 -0.0319 0.0988  -0.0240 229 VAL D C   
14583 O O   . VAL D 229 ? 0.2217 0.2677 1.9082 -0.0319 0.0969  -0.0258 229 VAL D O   
14584 C CB  . VAL D 229 ? 0.2124 0.2544 1.8721 -0.0237 0.0807  -0.0158 229 VAL D CB  
14585 C CG1 . VAL D 229 ? 0.2158 0.2539 1.8611 -0.0199 0.0750  -0.0116 229 VAL D CG1 
14586 C CG2 . VAL D 229 ? 0.2210 0.2737 1.8917 -0.0254 0.0722  -0.0141 229 VAL D CG2 
14587 N N   . SER D 230 ? 0.2169 0.2407 1.8664 -0.0361 0.1077  -0.0262 230 SER D N   
14588 C CA  . SER D 230 ? 0.2165 0.2420 1.8817 -0.0416 0.1183  -0.0312 230 SER D CA  
14589 C C   . SER D 230 ? 0.2147 0.2403 1.8907 -0.0409 0.1281  -0.0351 230 SER D C   
14590 O O   . SER D 230 ? 0.2120 0.2291 1.8727 -0.0372 0.1295  -0.0342 230 SER D O   
14591 C CB  . SER D 230 ? 0.2349 0.2452 1.8804 -0.0463 0.1272  -0.0318 230 SER D CB  
14592 O OG  . SER D 230 ? 0.2407 0.2335 1.8556 -0.0435 0.1295  -0.0290 230 SER D OG  
14593 N N   . PRO D 231 ? 0.2099 0.2458 1.9145 -0.0441 0.1348  -0.0404 231 PRO D N   
14594 C CA  . PRO D 231 ? 0.2174 0.2518 1.9316 -0.0440 0.1474  -0.0455 231 PRO D CA  
14595 C C   . PRO D 231 ? 0.2538 0.2674 1.9374 -0.0460 0.1615  -0.0465 231 PRO D C   
14596 O O   . PRO D 231 ? 0.2512 0.2576 1.9247 -0.0427 0.1656  -0.0479 231 PRO D O   
14597 C CB  . PRO D 231 ? 0.2045 0.2529 1.9544 -0.0486 0.1533  -0.0514 231 PRO D CB  
14598 C CG  . PRO D 231 ? 0.1888 0.2513 1.9538 -0.0475 0.1358  -0.0484 231 PRO D CG  
14599 C CD  . PRO D 231 ? 0.1940 0.2451 1.9260 -0.0473 0.1290  -0.0423 231 PRO D CD  
14600 N N   . GLU D 232 ? 0.2939 0.2961 1.9609 -0.0514 0.1683  -0.0456 232 GLU D N   
14601 C CA  . GLU D 232 ? 0.3293 0.3084 1.9620 -0.0532 0.1800  -0.0450 232 GLU D CA  
14602 C C   . GLU D 232 ? 0.3138 0.2805 1.9233 -0.0554 0.1764  -0.0401 232 GLU D C   
14603 O O   . GLU D 232 ? 0.2993 0.2759 1.9179 -0.0546 0.1643  -0.0377 232 GLU D O   
14604 C CB  . GLU D 232 ? 0.3693 0.3448 2.0113 -0.0587 0.2003  -0.0515 232 GLU D CB  
14605 C CG  . GLU D 232 ? 0.3967 0.3830 2.0672 -0.0661 0.2073  -0.0549 232 GLU D CG  
14606 C CD  . GLU D 232 ? 0.4448 0.4339 2.1360 -0.0714 0.2273  -0.0627 232 GLU D CD  
14607 O OE1 . GLU D 232 ? 0.4892 0.4591 2.1544 -0.0741 0.2434  -0.0638 232 GLU D OE1 
14608 O OE2 . GLU D 232 ? 0.4819 0.4922 2.2150 -0.0727 0.2268  -0.0678 232 GLU D OE2 
14609 N N   . GLY D 233 ? 0.3266 0.2701 1.9039 -0.0577 0.1862  -0.0387 233 GLY D N   
14610 C CA  . GLY D 233 ? 0.3278 0.2564 1.8835 -0.0603 0.1852  -0.0344 233 GLY D CA  
14611 C C   . GLY D 233 ? 0.3204 0.2412 1.8520 -0.0533 0.1703  -0.0291 233 GLY D C   
14612 O O   . GLY D 233 ? 0.3150 0.2458 1.8517 -0.0472 0.1596  -0.0286 233 GLY D O   
14613 N N   . GLY D 234 ? 0.3507 0.2537 1.8582 -0.0544 0.1696  -0.0252 234 GLY D N   
14614 C CA  . GLY D 234 ? 0.3443 0.2374 1.8286 -0.0478 0.1567  -0.0207 234 GLY D CA  
14615 C C   . GLY D 234 ? 0.3769 0.2467 1.8272 -0.0453 0.1601  -0.0189 234 GLY D C   
14616 O O   . GLY D 234 ? 0.3893 0.2454 1.8273 -0.0500 0.1746  -0.0202 234 GLY D O   
14617 N N   . ASN D 235 ? 0.3995 0.2646 1.8343 -0.0378 0.1470  -0.0163 235 ASN D N   
14618 C CA  . ASN D 235 ? 0.4308 0.2773 1.8367 -0.0344 0.1470  -0.0158 235 ASN D CA  
14619 C C   . ASN D 235 ? 0.4158 0.2735 1.8277 -0.0268 0.1321  -0.0163 235 ASN D C   
14620 O O   . ASN D 235 ? 0.3949 0.2654 1.8207 -0.0236 0.1210  -0.0147 235 ASN D O   
14621 C CB  . ASN D 235 ? 0.4819 0.2995 1.8516 -0.0340 0.1469  -0.0113 235 ASN D CB  
14622 C CG  . ASN D 235 ? 0.5303 0.3283 1.8686 -0.0305 0.1459  -0.0113 235 ASN D CG  
14623 O OD1 . ASN D 235 ? 0.5429 0.3367 1.8759 -0.0340 0.1582  -0.0147 235 ASN D OD1 
14624 N ND2 . ASN D 235 ? 0.5584 0.3458 1.8781 -0.0234 0.1309  -0.0085 235 ASN D ND2 
14625 N N   . GLY D 236 ? 0.4282 0.2806 1.8296 -0.0244 0.1326  -0.0189 236 GLY D N   
14626 C CA  . GLY D 236 ? 0.3970 0.2590 1.8051 -0.0179 0.1190  -0.0198 236 GLY D CA  
14627 C C   . GLY D 236 ? 0.3575 0.2467 1.8012 -0.0176 0.1136  -0.0199 236 GLY D C   
14628 O O   . GLY D 236 ? 0.3866 0.2884 1.8514 -0.0218 0.1216  -0.0217 236 GLY D O   
14629 N N   . GLN D 237 ? 0.3355 0.2327 1.7851 -0.0129 0.1003  -0.0178 237 GLN D N   
14630 C CA  . GLN D 237 ? 0.3038 0.2241 1.7822 -0.0124 0.0948  -0.0173 237 GLN D CA  
14631 C C   . GLN D 237 ? 0.2986 0.2260 1.7868 -0.0155 0.0962  -0.0154 237 GLN D C   
14632 O O   . GLN D 237 ? 0.2778 0.2228 1.7866 -0.0157 0.0921  -0.0147 237 GLN D O   
14633 C CB  . GLN D 237 ? 0.3030 0.2269 1.7816 -0.0066 0.0818  -0.0163 237 GLN D CB  
14634 C CG  . GLN D 237 ? 0.3044 0.2252 1.7794 -0.0036 0.0781  -0.0190 237 GLN D CG  
14635 C CD  . GLN D 237 ? 0.2971 0.2187 1.7709 0.0017  0.0652  -0.0185 237 GLN D CD  
14636 O OE1 . GLN D 237 ? 0.2640 0.2011 1.7566 0.0028  0.0597  -0.0170 237 GLN D OE1 
14637 N NE2 . GLN D 237 ? 0.3206 0.2247 1.7715 0.0049  0.0603  -0.0198 237 GLN D NE2 
14638 N N   . TYR D 238 ? 0.3115 0.2236 1.7829 -0.0179 0.1012  -0.0144 238 TYR D N   
14639 C CA  . TYR D 238 ? 0.3044 0.2223 1.7865 -0.0222 0.1047  -0.0140 238 TYR D CA  
14640 C C   . TYR D 238 ? 0.3196 0.2458 1.8185 -0.0279 0.1152  -0.0168 238 TYR D C   
14641 O O   . TYR D 238 ? 0.3457 0.2597 1.8341 -0.0310 0.1260  -0.0183 238 TYR D O   
14642 C CB  . TYR D 238 ? 0.3171 0.2150 1.7775 -0.0231 0.1066  -0.0120 238 TYR D CB  
14643 C CG  . TYR D 238 ? 0.2911 0.1940 1.7632 -0.0281 0.1102  -0.0125 238 TYR D CG  
14644 C CD1 . TYR D 238 ? 0.2655 0.1843 1.7536 -0.0269 0.1025  -0.0130 238 TYR D CD1 
14645 C CD2 . TYR D 238 ? 0.3093 0.2016 1.7771 -0.0348 0.1219  -0.0131 238 TYR D CD2 
14646 C CE1 . TYR D 238 ? 0.2693 0.1927 1.7679 -0.0317 0.1049  -0.0145 238 TYR D CE1 
14647 C CE2 . TYR D 238 ? 0.3082 0.2059 1.7895 -0.0400 0.1248  -0.0146 238 TYR D CE2 
14648 C CZ  . TYR D 238 ? 0.2906 0.2036 1.7866 -0.0382 0.1154  -0.0155 238 TYR D CZ  
14649 O OH  . TYR D 238 ? 0.3021 0.2192 1.8097 -0.0435 0.1173  -0.0177 238 TYR D OH  
14650 N N   . GLY D 239 ? 0.3139 0.2608 1.8389 -0.0286 0.1117  -0.0177 239 GLY D N   
14651 C CA  . GLY D 239 ? 0.3084 0.2668 1.8558 -0.0329 0.1190  -0.0208 239 GLY D CA  
14652 C C   . GLY D 239 ? 0.2854 0.2463 1.8384 -0.0309 0.1222  -0.0231 239 GLY D C   
14653 O O   . GLY D 239 ? 0.2781 0.2287 1.8137 -0.0271 0.1202  -0.0226 239 GLY D O   
14654 N N   . SER D 240 ? 0.2696 0.2437 1.8480 -0.0333 0.1268  -0.0262 240 SER D N   
14655 C CA  . SER D 240 ? 0.2751 0.2515 1.8626 -0.0320 0.1320  -0.0297 240 SER D CA  
14656 C C   . SER D 240 ? 0.2807 0.2601 1.8667 -0.0259 0.1219  -0.0280 240 SER D C   
14657 O O   . SER D 240 ? 0.2985 0.2704 1.8770 -0.0241 0.1261  -0.0308 240 SER D O   
14658 C CB  . SER D 240 ? 0.2874 0.2458 1.8551 -0.0345 0.1460  -0.0328 240 SER D CB  
14659 O OG  . SER D 240 ? 0.2932 0.2468 1.8609 -0.0409 0.1565  -0.0338 240 SER D OG  
14660 N N   . ASN D 241 ? 0.2895 0.2786 1.8813 -0.0232 0.1095  -0.0238 241 ASN D N   
14661 C CA  . ASN D 241 ? 0.3044 0.2983 1.9001 -0.0186 0.1007  -0.0221 241 ASN D CA  
14662 C C   . ASN D 241 ? 0.2900 0.2994 1.9143 -0.0181 0.0982  -0.0224 241 ASN D C   
14663 O O   . ASN D 241 ? 0.3058 0.3251 1.9459 -0.0207 0.0979  -0.0222 241 ASN D O   
14664 C CB  . ASN D 241 ? 0.3286 0.3243 1.9161 -0.0162 0.0903  -0.0175 241 ASN D CB  
14665 C CG  . ASN D 241 ? 0.3523 0.3328 1.9142 -0.0144 0.0895  -0.0173 241 ASN D CG  
14666 O OD1 . ASN D 241 ? 0.3809 0.3551 1.9342 -0.0112 0.0863  -0.0181 241 ASN D OD1 
14667 N ND2 . ASN D 241 ? 0.3690 0.3433 1.9194 -0.0161 0.0908  -0.0163 241 ASN D ND2 
14668 N N   . THR D 242 ? 0.2654 0.2761 1.8966 -0.0148 0.0956  -0.0231 242 THR D N   
14669 C CA  . THR D 242 ? 0.2431 0.2666 1.9004 -0.0133 0.0909  -0.0221 242 THR D CA  
14670 C C   . THR D 242 ? 0.2402 0.2716 1.8996 -0.0123 0.0792  -0.0154 242 THR D C   
14671 O O   . THR D 242 ? 0.2921 0.3194 1.9343 -0.0125 0.0763  -0.0128 242 THR D O   
14672 C CB  . THR D 242 ? 0.2214 0.2417 1.8845 -0.0101 0.0919  -0.0250 242 THR D CB  
14673 O OG1 . THR D 242 ? 0.2068 0.2208 1.8542 -0.0080 0.0855  -0.0225 242 THR D OG1 
14674 C CG2 . THR D 242 ? 0.2379 0.2478 1.8934 -0.0111 0.1044  -0.0323 242 THR D CG2 
14675 N N   . LEU D 243 ? 0.2082 0.2500 1.8880 -0.0111 0.0729  -0.0126 243 LEU D N   
14676 C CA  . LEU D 243 ? 0.1875 0.2358 1.8676 -0.0109 0.0629  -0.0059 243 LEU D CA  
14677 C C   . LEU D 243 ? 0.1909 0.2347 1.8595 -0.0091 0.0589  -0.0023 243 LEU D C   
14678 O O   . LEU D 243 ? 0.1915 0.2373 1.8515 -0.0098 0.0541  0.0022  243 LEU D O   
14679 C CB  . LEU D 243 ? 0.1730 0.2307 1.8756 -0.0098 0.0562  -0.0033 243 LEU D CB  
14680 C CG  . LEU D 243 ? 0.1574 0.2229 1.8752 -0.0119 0.0568  -0.0063 243 LEU D CG  
14681 C CD1 . LEU D 243 ? 0.1494 0.2233 1.8939 -0.0093 0.0499  -0.0052 243 LEU D CD1 
14682 C CD2 . LEU D 243 ? 0.1509 0.2182 1.8556 -0.0145 0.0519  -0.0032 243 LEU D CD2 
14683 N N   . LYS D 244 ? 0.1957 0.2338 1.8662 -0.0070 0.0616  -0.0053 244 LYS D N   
14684 C CA  . LYS D 244 ? 0.1880 0.2216 1.8533 -0.0052 0.0583  -0.0038 244 LYS D CA  
14685 C C   . LYS D 244 ? 0.2001 0.2261 1.8445 -0.0054 0.0599  -0.0059 244 LYS D C   
14686 O O   . LYS D 244 ? 0.1944 0.2204 1.8337 -0.0049 0.0555  -0.0032 244 LYS D O   
14687 C CB  . LYS D 244 ? 0.1835 0.2122 1.8576 -0.0031 0.0609  -0.0084 244 LYS D CB  
14688 C CG  . LYS D 244 ? 0.1979 0.2204 1.8651 -0.0019 0.0577  -0.0087 244 LYS D CG  
14689 C CD  . LYS D 244 ? 0.2119 0.2299 1.8897 0.0001  0.0574  -0.0122 244 LYS D CD  
14690 C CE  . LYS D 244 ? 0.2191 0.2321 1.8921 0.0006  0.0528  -0.0126 244 LYS D CE  
14691 N NZ  . LYS D 244 ? 0.2174 0.2367 1.8932 -0.0008 0.0472  -0.0050 244 LYS D NZ  
14692 N N   . GLN D 245 ? 0.2014 0.2203 1.8347 -0.0061 0.0666  -0.0108 245 GLN D N   
14693 C CA  . GLN D 245 ? 0.2023 0.2123 1.8147 -0.0059 0.0672  -0.0121 245 GLN D CA  
14694 C C   . GLN D 245 ? 0.1896 0.2050 1.7981 -0.0070 0.0637  -0.0079 245 GLN D C   
14695 O O   . GLN D 245 ? 0.1722 0.1859 1.7727 -0.0056 0.0596  -0.0067 245 GLN D O   
14696 C CB  . GLN D 245 ? 0.2046 0.2042 1.8038 -0.0072 0.0757  -0.0168 245 GLN D CB  
14697 C CG  . GLN D 245 ? 0.2055 0.1957 1.8003 -0.0059 0.0801  -0.0221 245 GLN D CG  
14698 C CD  . GLN D 245 ? 0.2274 0.2072 1.8096 -0.0082 0.0910  -0.0263 245 GLN D CD  
14699 O OE1 . GLN D 245 ? 0.2263 0.2096 1.8128 -0.0113 0.0965  -0.0258 245 GLN D OE1 
14700 N NE2 . GLN D 245 ? 0.2409 0.2069 1.8063 -0.0070 0.0944  -0.0309 245 GLN D NE2 
14701 N N   . GLN D 246 ? 0.1932 0.2153 1.8090 -0.0094 0.0651  -0.0065 246 GLN D N   
14702 C CA  . GLN D 246 ? 0.2059 0.2330 1.8182 -0.0107 0.0618  -0.0033 246 GLN D CA  
14703 C C   . GLN D 246 ? 0.2013 0.2342 1.8169 -0.0095 0.0558  0.0011  246 GLN D C   
14704 O O   . GLN D 246 ? 0.2080 0.2408 1.8152 -0.0092 0.0542  0.0022  246 GLN D O   
14705 C CB  . GLN D 246 ? 0.2004 0.2343 1.8223 -0.0135 0.0626  -0.0032 246 GLN D CB  
14706 C CG  . GLN D 246 ? 0.2031 0.2406 1.8185 -0.0152 0.0593  -0.0011 246 GLN D CG  
14707 C CD  . GLN D 246 ? 0.2019 0.2484 1.8291 -0.0173 0.0554  0.0003  246 GLN D CD  
14708 O OE1 . GLN D 246 ? 0.2608 0.3132 1.9002 -0.0164 0.0509  0.0033  246 GLN D OE1 
14709 N NE2 . GLN D 246 ? 0.1981 0.2452 1.8220 -0.0201 0.0559  -0.0017 246 GLN D NE2 
14710 N N   . SER D 247 ? 0.1919 0.2290 1.8204 -0.0089 0.0530  0.0037  247 SER D N   
14711 C CA  . SER D 247 ? 0.2013 0.2430 1.8325 -0.0089 0.0486  0.0088  247 SER D CA  
14712 C C   . SER D 247 ? 0.2095 0.2475 1.8359 -0.0074 0.0482  0.0074  247 SER D C   
14713 O O   . SER D 247 ? 0.1984 0.2391 1.8206 -0.0078 0.0473  0.0092  247 SER D O   
14714 C CB  . SER D 247 ? 0.2065 0.2517 1.8521 -0.0088 0.0454  0.0126  247 SER D CB  
14715 O OG  . SER D 247 ? 0.2352 0.2841 1.8798 -0.0101 0.0420  0.0190  247 SER D OG  
14716 N N   . ASP D 248 ? 0.1978 0.2296 1.8250 -0.0056 0.0488  0.0034  248 ASP D N   
14717 C CA  . ASP D 248 ? 0.1870 0.2152 1.8110 -0.0039 0.0466  0.0010  248 ASP D CA  
14718 C C   . ASP D 248 ? 0.1952 0.2202 1.8056 -0.0029 0.0467  -0.0011 248 ASP D C   
14719 O O   . ASP D 248 ? 0.2125 0.2402 1.8241 -0.0021 0.0443  -0.0008 248 ASP D O   
14720 C CB  . ASP D 248 ? 0.1834 0.2045 1.8095 -0.0023 0.0462  -0.0034 248 ASP D CB  
14721 C CG  . ASP D 248 ? 0.1752 0.1989 1.8166 -0.0029 0.0462  -0.0016 248 ASP D CG  
14722 O OD1 . ASP D 248 ? 0.1536 0.1844 1.8043 -0.0045 0.0447  0.0044  248 ASP D OD1 
14723 O OD2 . ASP D 248 ? 0.1685 0.1861 1.8114 -0.0017 0.0478  -0.0062 248 ASP D OD2 
14724 N N   . GLY D 249 ? 0.2021 0.2213 1.8012 -0.0030 0.0500  -0.0032 249 GLY D N   
14725 C CA  . GLY D 249 ? 0.2045 0.2182 1.7903 -0.0017 0.0499  -0.0050 249 GLY D CA  
14726 C C   . GLY D 249 ? 0.1914 0.2132 1.7799 -0.0023 0.0490  -0.0025 249 GLY D C   
14727 O O   . GLY D 249 ? 0.1655 0.1856 1.7502 0.0000  0.0468  -0.0041 249 GLY D O   
14728 N N   . LEU D 250 ? 0.1741 0.2040 1.7691 -0.0051 0.0503  0.0011  250 LEU D N   
14729 C CA  . LEU D 250 ? 0.1655 0.2019 1.7600 -0.0063 0.0506  0.0033  250 LEU D CA  
14730 C C   . LEU D 250 ? 0.1439 0.1853 1.7460 -0.0056 0.0493  0.0045  250 LEU D C   
14731 O O   . LEU D 250 ? 0.1306 0.1738 1.7311 -0.0046 0.0501  0.0029  250 LEU D O   
14732 C CB  . LEU D 250 ? 0.1679 0.2101 1.7646 -0.0095 0.0509  0.0069  250 LEU D CB  
14733 C CG  . LEU D 250 ? 0.1703 0.2108 1.7588 -0.0111 0.0523  0.0050  250 LEU D CG  
14734 C CD1 . LEU D 250 ? 0.1689 0.2084 1.7485 -0.0104 0.0536  0.0028  250 LEU D CD1 
14735 C CD2 . LEU D 250 ? 0.1736 0.2070 1.7598 -0.0109 0.0545  0.0016  250 LEU D CD2 
14736 N N   . ILE D 251 ? 0.1463 0.1899 1.7588 -0.0063 0.0479  0.0068  251 ILE D N   
14737 C CA  . ILE D 251 ? 0.1276 0.1756 1.7503 -0.0064 0.0473  0.0077  251 ILE D CA  
14738 C C   . ILE D 251 ? 0.1283 0.1733 1.7514 -0.0030 0.0447  0.0022  251 ILE D C   
14739 O O   . ILE D 251 ? 0.1224 0.1723 1.7516 -0.0026 0.0453  0.0011  251 ILE D O   
14740 C CB  . ILE D 251 ? 0.1152 0.1634 1.7488 -0.0078 0.0457  0.0107  251 ILE D CB  
14741 C CG1 . ILE D 251 ? 0.1118 0.1622 1.7453 -0.0104 0.0465  0.0168  251 ILE D CG1 
14742 C CG2 . ILE D 251 ? 0.1208 0.1727 1.7668 -0.0087 0.0454  0.0112  251 ILE D CG2 
14743 C CD1 . ILE D 251 ? 0.1114 0.1662 1.7374 -0.0127 0.0489  0.0205  251 ILE D CD1 
14744 N N   . SER D 252 ? 0.1359 0.1721 1.7520 -0.0005 0.0420  -0.0014 252 SER D N   
14745 C CA  . SER D 252 ? 0.1463 0.1764 1.7592 0.0033  0.0373  -0.0064 252 SER D CA  
14746 C C   . SER D 252 ? 0.1648 0.1937 1.7705 0.0057  0.0374  -0.0082 252 SER D C   
14747 O O   . SER D 252 ? 0.1767 0.2081 1.7893 0.0083  0.0341  -0.0110 252 SER D O   
14748 C CB  . SER D 252 ? 0.1498 0.1687 1.7520 0.0046  0.0358  -0.0088 252 SER D CB  
14749 O OG  . SER D 252 ? 0.1586 0.1696 1.7560 0.0082  0.0294  -0.0133 252 SER D OG  
14750 N N   . ASN D 253 ? 0.1900 0.2156 1.7841 0.0047  0.0410  -0.0072 253 ASN D N   
14751 C CA  . ASN D 253 ? 0.2053 0.2290 1.7934 0.0068  0.0415  -0.0091 253 ASN D CA  
14752 C C   . ASN D 253 ? 0.2041 0.2397 1.8048 0.0061  0.0438  -0.0089 253 ASN D C   
14753 O O   . ASN D 253 ? 0.2370 0.2734 1.8422 0.0095  0.0420  -0.0124 253 ASN D O   
14754 C CB  . ASN D 253 ? 0.2178 0.2373 1.7938 0.0047  0.0458  -0.0082 253 ASN D CB  
14755 C CG  . ASN D 253 ? 0.2275 0.2348 1.7907 0.0045  0.0463  -0.0086 253 ASN D CG  
14756 O OD1 . ASN D 253 ? 0.2275 0.2327 1.7848 0.0016  0.0503  -0.0079 253 ASN D OD1 
14757 N ND2 . ASN D 253 ? 0.2415 0.2400 1.7996 0.0071  0.0426  -0.0103 253 ASN D ND2 
14758 N N   . TYR D 254 ? 0.1933 0.2373 1.7997 0.0018  0.0479  -0.0049 254 TYR D N   
14759 C CA  . TYR D 254 ? 0.1959 0.2494 1.8099 0.0000  0.0526  -0.0041 254 TYR D CA  
14760 C C   . TYR D 254 ? 0.1978 0.2567 1.8282 0.0020  0.0510  -0.0071 254 TYR D C   
14761 O O   . TYR D 254 ? 0.2126 0.2768 1.8496 0.0032  0.0541  -0.0101 254 TYR D O   
14762 C CB  . TYR D 254 ? 0.1995 0.2584 1.8147 -0.0050 0.0563  0.0019  254 TYR D CB  
14763 C CG  . TYR D 254 ? 0.2056 0.2692 1.8150 -0.0078 0.0624  0.0033  254 TYR D CG  
14764 C CD1 . TYR D 254 ? 0.2228 0.2925 1.8395 -0.0078 0.0675  0.0010  254 TYR D CD1 
14765 C CD2 . TYR D 254 ? 0.2084 0.2703 1.8052 -0.0105 0.0630  0.0064  254 TYR D CD2 
14766 C CE1 . TYR D 254 ? 0.2244 0.2971 1.8330 -0.0104 0.0743  0.0014  254 TYR D CE1 
14767 C CE2 . TYR D 254 ? 0.2182 0.2826 1.8061 -0.0130 0.0679  0.0071  254 TYR D CE2 
14768 C CZ  . TYR D 254 ? 0.2170 0.2862 1.8093 -0.0131 0.0742  0.0046  254 TYR D CZ  
14769 O OH  . TYR D 254 ? 0.2257 0.2964 1.8071 -0.0158 0.0803  0.0047  254 TYR D OH  
14770 N N   . ARG D 255 ? 0.1852 0.2428 1.8238 0.0025  0.0462  -0.0072 255 ARG D N   
14771 C CA  . ARG D 255 ? 0.1837 0.2468 1.8405 0.0041  0.0433  -0.0107 255 ARG D CA  
14772 C C   . ARG D 255 ? 0.2124 0.2711 1.8684 0.0102  0.0371  -0.0167 255 ARG D C   
14773 O O   . ARG D 255 ? 0.2173 0.2831 1.8875 0.0122  0.0377  -0.0205 255 ARG D O   
14774 C CB  . ARG D 255 ? 0.1695 0.2313 1.8350 0.0027  0.0389  -0.0100 255 ARG D CB  
14775 C CG  . ARG D 255 ? 0.1651 0.2291 1.8475 0.0053  0.0319  -0.0154 255 ARG D CG  
14776 C CD  . ARG D 255 ? 0.1613 0.2377 1.8675 0.0021  0.0362  -0.0159 255 ARG D CD  
14777 N NE  . ARG D 255 ? 0.1639 0.2490 1.8786 0.0028  0.0419  -0.0182 255 ARG D NE  
14778 C CZ  . ARG D 255 ? 0.1739 0.2670 1.8936 -0.0021 0.0531  -0.0147 255 ARG D CZ  
14779 N NH1 . ARG D 255 ? 0.1744 0.2664 1.8878 -0.0077 0.0585  -0.0075 255 ARG D NH1 
14780 N NH2 . ARG D 255 ? 0.1739 0.2751 1.9034 -0.0011 0.0589  -0.0185 255 ARG D NH2 
14781 N N   . ASP D 256 ? 0.2241 0.2703 1.8637 0.0131  0.0315  -0.0175 256 ASP D N   
14782 C CA  . ASP D 256 ? 0.2376 0.2753 1.8722 0.0193  0.0238  -0.0220 256 ASP D CA  
14783 C C   . ASP D 256 ? 0.2221 0.2627 1.8590 0.0220  0.0266  -0.0244 256 ASP D C   
14784 O O   . ASP D 256 ? 0.2222 0.2627 1.8683 0.0273  0.0204  -0.0290 256 ASP D O   
14785 C CB  . ASP D 256 ? 0.2570 0.2787 1.8685 0.0207  0.0205  -0.0210 256 ASP D CB  
14786 C CG  . ASP D 256 ? 0.2722 0.2871 1.8805 0.0210  0.0143  -0.0220 256 ASP D CG  
14787 O OD1 . ASP D 256 ? 0.2683 0.2904 1.8872 0.0173  0.0167  -0.0205 256 ASP D OD1 
14788 O OD2 . ASP D 256 ? 0.3080 0.3096 1.9028 0.0252  0.0068  -0.0243 256 ASP D OD2 
14789 N N   . LEU D 257 ? 0.2053 0.2481 1.8344 0.0187  0.0352  -0.0219 257 LEU D N   
14790 C CA  . LEU D 257 ? 0.1964 0.2397 1.8246 0.0210  0.0385  -0.0248 257 LEU D CA  
14791 C C   . LEU D 257 ? 0.1859 0.2438 1.8352 0.0205  0.0439  -0.0277 257 LEU D C   
14792 O O   . LEU D 257 ? 0.1935 0.2532 1.8511 0.0249  0.0438  -0.0328 257 LEU D O   
14793 C CB  . LEU D 257 ? 0.2003 0.2396 1.8112 0.0171  0.0449  -0.0217 257 LEU D CB  
14794 C CG  . LEU D 257 ? 0.2073 0.2327 1.7999 0.0170  0.0415  -0.0195 257 LEU D CG  
14795 C CD1 . LEU D 257 ? 0.1960 0.2198 1.7766 0.0119  0.0471  -0.0164 257 LEU D CD1 
14796 C CD2 . LEU D 257 ? 0.2309 0.2441 1.8163 0.0228  0.0362  -0.0228 257 LEU D CD2 
14797 N N   . ILE D 258 ? 0.1676 0.2354 1.8264 0.0152  0.0493  -0.0247 258 ILE D N   
14798 C CA  . ILE D 258 ? 0.1620 0.2430 1.8413 0.0139  0.0560  -0.0274 258 ILE D CA  
14799 C C   . ILE D 258 ? 0.1729 0.2575 1.8739 0.0193  0.0479  -0.0333 258 ILE D C   
14800 O O   . ILE D 258 ? 0.1712 0.2634 1.8891 0.0223  0.0506  -0.0390 258 ILE D O   
14801 C CB  . ILE D 258 ? 0.1501 0.2383 1.8336 0.0067  0.0632  -0.0219 258 ILE D CB  
14802 C CG1 . ILE D 258 ? 0.1557 0.2410 1.8187 0.0021  0.0703  -0.0167 258 ILE D CG1 
14803 C CG2 . ILE D 258 ? 0.1423 0.2435 1.8504 0.0048  0.0702  -0.0249 258 ILE D CG2 
14804 C CD1 . ILE D 258 ? 0.1591 0.2464 1.8205 -0.0043 0.0738  -0.0093 258 ILE D CD1 
14805 N N   . ASP D 259 ? 0.1798 0.2580 1.8794 0.0208  0.0375  -0.0325 259 ASP D N   
14806 C CA  . ASP D 259 ? 0.1917 0.2709 1.9088 0.0260  0.0264  -0.0379 259 ASP D CA  
14807 C C   . ASP D 259 ? 0.2191 0.2910 1.9329 0.0340  0.0189  -0.0426 259 ASP D C   
14808 O O   . ASP D 259 ? 0.2348 0.3103 1.9682 0.0394  0.0102  -0.0484 259 ASP D O   
14809 C CB  . ASP D 259 ? 0.1933 0.2639 1.9027 0.0258  0.0167  -0.0363 259 ASP D CB  
14810 C CG  . ASP D 259 ? 0.1890 0.2659 1.9062 0.0189  0.0217  -0.0325 259 ASP D CG  
14811 O OD1 . ASP D 259 ? 0.1801 0.2703 1.9191 0.0153  0.0287  -0.0332 259 ASP D OD1 
14812 O OD2 . ASP D 259 ? 0.1808 0.2487 1.8827 0.0171  0.0192  -0.0291 259 ASP D OD2 
14813 N N   . ALA D 260 ? 0.2288 0.2897 1.9188 0.0348  0.0216  -0.0401 260 ALA D N   
14814 C CA  . ALA D 260 ? 0.2330 0.2848 1.9175 0.0418  0.0162  -0.0436 260 ALA D CA  
14815 C C   . ALA D 260 ? 0.2251 0.2874 1.9255 0.0432  0.0247  -0.0484 260 ALA D C   
14816 O O   . ALA D 260 ? 0.2420 0.2979 1.9433 0.0499  0.0200  -0.0523 260 ALA D O   
14817 C CB  . ALA D 260 ? 0.2428 0.2779 1.8967 0.0411  0.0165  -0.0392 260 ALA D CB  
14818 N N   . GLY D 261 ? 0.2106 0.2865 1.9201 0.0369  0.0377  -0.0477 261 GLY D N   
14819 C CA  . GLY D 261 ? 0.2043 0.2902 1.9278 0.0375  0.0480  -0.0529 261 GLY D CA  
14820 C C   . GLY D 261 ? 0.1985 0.2840 1.9034 0.0315  0.0611  -0.0500 261 GLY D C   
14821 O O   . GLY D 261 ? 0.1963 0.2895 1.9090 0.0309  0.0716  -0.0543 261 GLY D O   
14822 N N   . ALA D 262 ? 0.1926 0.2700 1.8738 0.0269  0.0611  -0.0432 262 ALA D N   
14823 C CA  . ALA D 262 ? 0.2023 0.2782 1.8653 0.0220  0.0707  -0.0411 262 ALA D CA  
14824 C C   . ALA D 262 ? 0.1930 0.2815 1.8640 0.0163  0.0834  -0.0410 262 ALA D C   
14825 O O   . ALA D 262 ? 0.1813 0.2770 1.8625 0.0125  0.0850  -0.0375 262 ALA D O   
14826 C CB  . ALA D 262 ? 0.2143 0.2812 1.8558 0.0179  0.0671  -0.0340 262 ALA D CB  
14827 N N   . VAL D 263 ? 0.2062 0.2954 1.8691 0.0150  0.0929  -0.0443 263 VAL D N   
14828 C CA  . VAL D 263 ? 0.2264 0.3237 1.8875 0.0086  0.1062  -0.0430 263 VAL D CA  
14829 C C   . VAL D 263 ? 0.2366 0.3261 1.8685 0.0039  0.1091  -0.0392 263 VAL D C   
14830 O O   . VAL D 263 ? 0.2531 0.3454 1.8762 -0.0005 0.1199  -0.0397 263 VAL D O   
14831 C CB  . VAL D 263 ? 0.2414 0.3475 1.9187 0.0105  0.1173  -0.0517 263 VAL D CB  
14832 C CG1 . VAL D 263 ? 0.2433 0.3572 1.9529 0.0166  0.1123  -0.0573 263 VAL D CG1 
14833 C CG2 . VAL D 263 ? 0.2488 0.3479 1.9124 0.0134  0.1206  -0.0580 263 VAL D CG2 
14834 N N   . GLY D 264 ? 0.2482 0.3277 1.8655 0.0049  0.0997  -0.0363 264 GLY D N   
14835 C CA  . GLY D 264 ? 0.2671 0.3400 1.8599 0.0003  0.1001  -0.0327 264 GLY D CA  
14836 C C   . GLY D 264 ? 0.2650 0.3297 1.8499 0.0007  0.0895  -0.0281 264 GLY D C   
14837 O O   . GLY D 264 ? 0.2594 0.3182 1.8485 0.0055  0.0831  -0.0306 264 GLY D O   
14838 N N   . MET D 265 ? 0.2769 0.3406 1.8502 -0.0043 0.0879  -0.0215 265 MET D N   
14839 C CA  . MET D 265 ? 0.2747 0.3327 1.8449 -0.0042 0.0795  -0.0176 265 MET D CA  
14840 C C   . MET D 265 ? 0.2661 0.3190 1.8197 -0.0078 0.0774  -0.0160 265 MET D C   
14841 O O   . MET D 265 ? 0.2604 0.3154 1.8038 -0.0120 0.0796  -0.0134 265 MET D O   
14842 C CB  . MET D 265 ? 0.2814 0.3439 1.8620 -0.0056 0.0772  -0.0117 265 MET D CB  
14843 C CG  . MET D 265 ? 0.2906 0.3582 1.8899 -0.0021 0.0776  -0.0144 265 MET D CG  
14844 S SD  . MET D 265 ? 0.3278 0.3871 1.9314 0.0044  0.0684  -0.0181 265 MET D SD  
14845 C CE  . MET D 265 ? 0.2942 0.3502 1.8965 0.0024  0.0623  -0.0121 265 MET D CE  
14846 N N   . CYS D 266 ? 0.2579 0.3031 1.8084 -0.0063 0.0726  -0.0176 266 CYS D N   
14847 C CA  . CYS D 266 ? 0.2657 0.3068 1.8051 -0.0097 0.0700  -0.0170 266 CYS D CA  
14848 C C   . CYS D 266 ? 0.2638 0.3020 1.8072 -0.0102 0.0649  -0.0132 266 CYS D C   
14849 O O   . CYS D 266 ? 0.3108 0.3413 1.8521 -0.0095 0.0633  -0.0154 266 CYS D O   
14850 C CB  . CYS D 266 ? 0.2643 0.2980 1.7964 -0.0086 0.0711  -0.0237 266 CYS D CB  
14851 S SG  . CYS D 266 ? 0.2648 0.3013 1.7889 -0.0092 0.0781  -0.0294 266 CYS D SG  
14852 N N   . PRO D 267 ? 0.2340 0.2774 1.7835 -0.0116 0.0631  -0.0076 267 PRO D N   
14853 C CA  . PRO D 267 ? 0.2219 0.2627 1.7757 -0.0121 0.0595  -0.0051 267 PRO D CA  
14854 C C   . PRO D 267 ? 0.2285 0.2657 1.7770 -0.0149 0.0579  -0.0069 267 PRO D C   
14855 O O   . PRO D 267 ? 0.2128 0.2520 1.7548 -0.0175 0.0573  -0.0078 267 PRO D O   
14856 C CB  . PRO D 267 ? 0.2168 0.2643 1.7765 -0.0139 0.0580  0.0007  267 PRO D CB  
14857 C CG  . PRO D 267 ? 0.2294 0.2810 1.7821 -0.0159 0.0607  0.0017  267 PRO D CG  
14858 C CD  . PRO D 267 ? 0.2349 0.2854 1.7873 -0.0130 0.0652  -0.0037 267 PRO D CD  
14859 N N   . PHE D 268 ? 0.2394 0.2712 1.7910 -0.0148 0.0574  -0.0073 268 PHE D N   
14860 C CA  . PHE D 268 ? 0.2783 0.3058 1.8276 -0.0178 0.0574  -0.0100 268 PHE D CA  
14861 C C   . PHE D 268 ? 0.2571 0.2911 1.8142 -0.0212 0.0543  -0.0077 268 PHE D C   
14862 O O   . PHE D 268 ? 0.2030 0.2379 1.7689 -0.0212 0.0544  -0.0059 268 PHE D O   
14863 C CB  . PHE D 268 ? 0.3256 0.3422 1.8727 -0.0170 0.0602  -0.0122 268 PHE D CB  
14864 C CG  . PHE D 268 ? 0.3136 0.3260 1.8595 -0.0213 0.0614  -0.0153 268 PHE D CG  
14865 C CD1 . PHE D 268 ? 0.3219 0.3346 1.8628 -0.0230 0.0603  -0.0187 268 PHE D CD1 
14866 C CD2 . PHE D 268 ? 0.3233 0.3326 1.8747 -0.0240 0.0640  -0.0154 268 PHE D CD2 
14867 C CE1 . PHE D 268 ? 0.3834 0.3927 1.9253 -0.0275 0.0607  -0.0221 268 PHE D CE1 
14868 C CE2 . PHE D 268 ? 0.3340 0.3410 1.8879 -0.0288 0.0655  -0.0186 268 PHE D CE2 
14869 C CZ  . PHE D 268 ? 0.3603 0.3674 1.9100 -0.0305 0.0632  -0.0220 268 PHE D CZ  
14870 N N   . TYR D 269 ? 0.2876 0.3252 1.8407 -0.0239 0.0512  -0.0087 269 TYR D N   
14871 C CA  . TYR D 269 ? 0.3058 0.3469 1.8643 -0.0276 0.0469  -0.0097 269 TYR D CA  
14872 C C   . TYR D 269 ? 0.2760 0.3252 1.8408 -0.0277 0.0411  -0.0043 269 TYR D C   
14873 O O   . TYR D 269 ? 0.2516 0.3027 1.8252 -0.0258 0.0417  -0.0006 269 TYR D O   
14874 C CB  . TYR D 269 ? 0.3498 0.3864 1.9166 -0.0295 0.0502  -0.0129 269 TYR D CB  
14875 C CG  . TYR D 269 ? 0.3638 0.4002 1.9345 -0.0341 0.0484  -0.0176 269 TYR D CG  
14876 C CD1 . TYR D 269 ? 0.3657 0.4022 1.9277 -0.0360 0.0444  -0.0208 269 TYR D CD1 
14877 C CD2 . TYR D 269 ? 0.3965 0.4325 1.9804 -0.0370 0.0513  -0.0197 269 TYR D CD2 
14878 C CE1 . TYR D 269 ? 0.4051 0.4417 1.9725 -0.0406 0.0417  -0.0259 269 TYR D CE1 
14879 C CE2 . TYR D 269 ? 0.3857 0.4225 1.9772 -0.0419 0.0499  -0.0245 269 TYR D CE2 
14880 C CZ  . TYR D 269 ? 0.3941 0.4314 1.9778 -0.0437 0.0442  -0.0277 269 TYR D CZ  
14881 O OH  . TYR D 269 ? 0.3515 0.3895 1.9444 -0.0489 0.0421  -0.0333 269 TYR D OH  
14882 N N   . TYR D 270 ? 0.2756 0.3277 1.8338 -0.0297 0.0352  -0.0039 270 TYR D N   
14883 C CA  . TYR D 270 ? 0.2790 0.3367 1.8415 -0.0303 0.0270  0.0009  270 TYR D CA  
14884 C C   . TYR D 270 ? 0.2682 0.3305 1.8502 -0.0314 0.0226  -0.0003 270 TYR D C   
14885 O O   . TYR D 270 ? 0.2572 0.3230 1.8509 -0.0296 0.0201  0.0041  270 TYR D O   
14886 C CB  . TYR D 270 ? 0.2974 0.3542 1.8436 -0.0326 0.0215  -0.0002 270 TYR D CB  
14887 C CG  . TYR D 270 ? 0.2991 0.3594 1.8459 -0.0339 0.0096  0.0029  270 TYR D CG  
14888 C CD1 . TYR D 270 ? 0.3044 0.3652 1.8474 -0.0326 0.0049  0.0110  270 TYR D CD1 
14889 C CD2 . TYR D 270 ? 0.3043 0.3659 1.8539 -0.0367 0.0023  -0.0025 270 TYR D CD2 
14890 C CE1 . TYR D 270 ? 0.3198 0.3816 1.8604 -0.0333 -0.0076 0.0143  270 TYR D CE1 
14891 C CE2 . TYR D 270 ? 0.3077 0.3718 1.8568 -0.0376 -0.0106 -0.0003 270 TYR D CE2 
14892 C CZ  . TYR D 270 ? 0.3220 0.3858 1.8654 -0.0355 -0.0161 0.0084  270 TYR D CZ  
14893 O OH  . TYR D 270 ? 0.3419 0.4066 1.8839 -0.0359 -0.0307 0.0108  270 TYR D OH  
14894 N N   . ALA D 271 ? 0.2554 0.3176 1.8423 -0.0344 0.0218  -0.0066 271 ALA D N   
14895 C CA  . ALA D 271 ? 0.2350 0.3033 1.8429 -0.0363 0.0171  -0.0089 271 ALA D CA  
14896 C C   . ALA D 271 ? 0.2407 0.3063 1.8587 -0.0390 0.0254  -0.0150 271 ALA D C   
14897 O O   . ALA D 271 ? 0.2640 0.3225 1.8707 -0.0407 0.0302  -0.0189 271 ALA D O   
14898 C CB  . ALA D 271 ? 0.2314 0.3034 1.8373 -0.0386 0.0052  -0.0104 271 ALA D CB  
14899 N N   . ASP D 272 ? 0.2411 0.3114 1.8807 -0.0395 0.0275  -0.0162 272 ASP D N   
14900 C CA  . ASP D 272 ? 0.2465 0.3134 1.8952 -0.0432 0.0366  -0.0218 272 ASP D CA  
14901 C C   . ASP D 272 ? 0.2527 0.3192 1.9021 -0.0482 0.0333  -0.0278 272 ASP D C   
14902 O O   . ASP D 272 ? 0.2334 0.3055 1.8834 -0.0490 0.0219  -0.0287 272 ASP D O   
14903 C CB  . ASP D 272 ? 0.2484 0.3219 1.9230 -0.0440 0.0399  -0.0236 272 ASP D CB  
14904 C CG  . ASP D 272 ? 0.2488 0.3207 1.9259 -0.0401 0.0464  -0.0202 272 ASP D CG  
14905 O OD1 . ASP D 272 ? 0.2210 0.2851 1.8784 -0.0370 0.0494  -0.0166 272 ASP D OD1 
14906 O OD2 . ASP D 272 ? 0.2369 0.3156 1.9372 -0.0401 0.0483  -0.0220 272 ASP D OD2 
14907 N N   . GLY D 273 ? 0.2646 0.3227 1.9124 -0.0515 0.0434  -0.0317 273 GLY D N   
14908 C CA  . GLY D 273 ? 0.2757 0.3311 1.9270 -0.0572 0.0434  -0.0382 273 GLY D CA  
14909 C C   . GLY D 273 ? 0.2936 0.3480 1.9642 -0.0620 0.0537  -0.0419 273 GLY D C   
14910 O O   . GLY D 273 ? 0.2945 0.3373 1.9555 -0.0624 0.0655  -0.0410 273 GLY D O   
14911 N N   . TRP D 274 ? 0.2816 0.3480 1.9794 -0.0656 0.0491  -0.0462 274 TRP D N   
14912 C CA  . TRP D 274 ? 0.2546 0.3229 1.9757 -0.0707 0.0597  -0.0504 274 TRP D CA  
14913 C C   . TRP D 274 ? 0.2601 0.3173 1.9777 -0.0777 0.0682  -0.0552 274 TRP D C   
14914 O O   . TRP D 274 ? 0.2613 0.3171 1.9954 -0.0830 0.0800  -0.0584 274 TRP D O   
14915 C CB  . TRP D 274 ? 0.2631 0.3488 2.0172 -0.0724 0.0503  -0.0545 274 TRP D CB  
14916 C CG  . TRP D 274 ? 0.2440 0.3399 2.0090 -0.0662 0.0445  -0.0503 274 TRP D CG  
14917 C CD1 . TRP D 274 ? 0.2229 0.3150 1.9695 -0.0597 0.0437  -0.0432 274 TRP D CD1 
14918 C CD2 . TRP D 274 ? 0.2327 0.3446 2.0329 -0.0661 0.0380  -0.0534 274 TRP D CD2 
14919 N NE1 . TRP D 274 ? 0.2123 0.3154 1.9786 -0.0557 0.0376  -0.0414 274 TRP D NE1 
14920 C CE2 . TRP D 274 ? 0.2239 0.3392 2.0230 -0.0590 0.0337  -0.0474 274 TRP D CE2 
14921 C CE3 . TRP D 274 ? 0.2312 0.3546 2.0655 -0.0712 0.0355  -0.0611 274 TRP D CE3 
14922 C CZ2 . TRP D 274 ? 0.2488 0.3778 2.0790 -0.0562 0.0266  -0.0486 274 TRP D CZ2 
14923 C CZ3 . TRP D 274 ? 0.2382 0.3768 2.1049 -0.0683 0.0281  -0.0626 274 TRP D CZ3 
14924 C CH2 . TRP D 274 ? 0.2383 0.3793 2.1027 -0.0606 0.0235  -0.0563 274 TRP D CH2 
14925 N N   . TRP D 275 ? 0.2581 0.3077 1.9561 -0.0779 0.0623  -0.0561 275 TRP D N   
14926 C CA  . TRP D 275 ? 0.2728 0.3095 1.9652 -0.0840 0.0692  -0.0604 275 TRP D CA  
14927 C C   . TRP D 275 ? 0.2810 0.2989 1.9514 -0.0827 0.0828  -0.0561 275 TRP D C   
14928 O O   . TRP D 275 ? 0.2769 0.2823 1.9462 -0.0884 0.0923  -0.0585 275 TRP D O   
14929 C CB  . TRP D 275 ? 0.2758 0.3100 1.9551 -0.0842 0.0581  -0.0639 275 TRP D CB  
14930 C CG  . TRP D 275 ? 0.2713 0.2972 1.9204 -0.0774 0.0558  -0.0592 275 TRP D CG  
14931 C CD1 . TRP D 275 ? 0.2639 0.2973 1.9032 -0.0713 0.0468  -0.0552 275 TRP D CD1 
14932 C CD2 . TRP D 275 ? 0.2759 0.2842 1.9023 -0.0759 0.0629  -0.0582 275 TRP D CD2 
14933 N NE1 . TRP D 275 ? 0.2586 0.2821 1.8731 -0.0666 0.0489  -0.0523 275 TRP D NE1 
14934 C CE2 . TRP D 275 ? 0.2683 0.2768 1.8751 -0.0688 0.0579  -0.0543 275 TRP D CE2 
14935 C CE3 . TRP D 275 ? 0.2905 0.2824 1.9119 -0.0799 0.0728  -0.0601 275 TRP D CE3 
14936 C CZ2 . TRP D 275 ? 0.2725 0.2673 1.8582 -0.0650 0.0620  -0.0531 275 TRP D CZ2 
14937 C CZ3 . TRP D 275 ? 0.2925 0.2691 1.8906 -0.0758 0.0756  -0.0582 275 TRP D CZ3 
14938 C CH2 . TRP D 275 ? 0.2882 0.2671 1.8701 -0.0682 0.0701  -0.0551 275 TRP D CH2 
14939 N N   . LYS D 276 ? 0.2955 0.3105 1.9486 -0.0755 0.0834  -0.0498 276 LYS D N   
14940 C CA  . LYS D 276 ? 0.3215 0.3180 1.9490 -0.0726 0.0909  -0.0459 276 LYS D CA  
14941 C C   . LYS D 276 ? 0.3364 0.3206 1.9641 -0.0767 0.1058  -0.0450 276 LYS D C   
14942 O O   . LYS D 276 ? 0.3165 0.2817 1.9241 -0.0765 0.1125  -0.0427 276 LYS D O   
14943 C CB  . LYS D 276 ? 0.3109 0.3096 1.9233 -0.0641 0.0859  -0.0402 276 LYS D CB  
14944 C CG  . LYS D 276 ? 0.2984 0.3047 1.9043 -0.0605 0.0738  -0.0405 276 LYS D CG  
14945 C CD  . LYS D 276 ? 0.2865 0.2965 1.8814 -0.0532 0.0698  -0.0351 276 LYS D CD  
14946 C CE  . LYS D 276 ? 0.3050 0.3006 1.8806 -0.0491 0.0751  -0.0325 276 LYS D CE  
14947 N NZ  . LYS D 276 ? 0.3131 0.3026 1.8746 -0.0470 0.0717  -0.0344 276 LYS D NZ  
14948 N N   . GLY D 277 ? 0.3622 0.3565 2.0121 -0.0801 0.1113  -0.0467 277 GLY D N   
14949 C CA  . GLY D 277 ? 0.4033 0.3861 2.0519 -0.0841 0.1273  -0.0459 277 GLY D CA  
14950 C C   . GLY D 277 ? 0.4549 0.4367 2.1232 -0.0941 0.1359  -0.0515 277 GLY D C   
14951 O O   . GLY D 277 ? 0.5193 0.4955 2.1939 -0.0992 0.1506  -0.0521 277 GLY D O   
14952 N N   . GLY D 278 ? 0.4568 0.4441 2.1355 -0.0975 0.1271  -0.0561 278 GLY D N   
14953 C CA  . GLY D 278 ? 0.5098 0.4988 2.2124 -0.1075 0.1339  -0.0624 278 GLY D CA  
14954 C C   . GLY D 278 ? 0.5263 0.5384 2.2606 -0.1093 0.1209  -0.0690 278 GLY D C   
14955 O O   . GLY D 278 ? 0.7306 0.7434 2.4664 -0.1117 0.1112  -0.0732 278 GLY D O   
14956 N N   . GLU D 279 ? 0.4588 0.4887 2.2183 -0.1082 0.1203  -0.0704 279 GLU D N   
14957 C CA  . GLU D 279 ? 0.4005 0.4512 2.1969 -0.1117 0.1105  -0.0776 279 GLU D CA  
14958 C C   . GLU D 279 ? 0.4046 0.4691 2.1992 -0.1035 0.0907  -0.0756 279 GLU D C   
14959 O O   . GLU D 279 ? 0.4035 0.4707 2.1884 -0.0959 0.0891  -0.0698 279 GLU D O   
14960 C CB  . GLU D 279 ? 0.3547 0.4153 2.1846 -0.1167 0.1235  -0.0816 279 GLU D CB  
14961 C CG  . GLU D 279 ? 0.3664 0.4105 2.1943 -0.1262 0.1438  -0.0832 279 GLU D CG  
14962 C CD  . GLU D 279 ? 0.3784 0.4233 2.2220 -0.1298 0.1637  -0.0842 279 GLU D CD  
14963 O OE1 . GLU D 279 ? 0.4180 0.4837 2.3001 -0.1308 0.1629  -0.0899 279 GLU D OE1 
14964 O OE2 . GLU D 279 ? 0.3656 0.3893 2.1820 -0.1316 0.1797  -0.0795 279 GLU D OE2 
14965 N N   . LYS D 280 ? 0.3627 0.4340 2.1647 -0.1055 0.0759  -0.0806 280 LYS D N   
14966 C CA  . LYS D 280 ? 0.3447 0.4222 2.1329 -0.0986 0.0573  -0.0780 280 LYS D CA  
14967 C C   . LYS D 280 ? 0.3178 0.4156 2.1344 -0.0955 0.0457  -0.0790 280 LYS D C   
14968 O O   . LYS D 280 ? 0.3051 0.4078 2.1105 -0.0891 0.0313  -0.0751 280 LYS D O   
14969 C CB  . LYS D 280 ? 0.3477 0.4209 2.1244 -0.1012 0.0458  -0.0827 280 LYS D CB  
14970 C CG  . LYS D 280 ? 0.3504 0.4338 2.1580 -0.1088 0.0382  -0.0924 280 LYS D CG  
14971 C CD  . LYS D 280 ? 0.3622 0.4362 2.1522 -0.1119 0.0299  -0.0974 280 LYS D CD  
14972 C CE  . LYS D 280 ? 0.3780 0.4610 2.1981 -0.1199 0.0216  -0.1079 280 LYS D CE  
14973 N NZ  . LYS D 280 ? 0.4015 0.4767 2.2019 -0.1213 0.0097  -0.1131 280 LYS D NZ  
14974 N N   . SER D 281 ? 0.2936 0.4019 2.1467 -0.1002 0.0527  -0.0841 281 SER D N   
14975 C CA  . SER D 281 ? 0.2679 0.3954 2.1525 -0.0966 0.0432  -0.0853 281 SER D CA  
14976 C C   . SER D 281 ? 0.2448 0.3749 2.1445 -0.0952 0.0596  -0.0837 281 SER D C   
14977 O O   . SER D 281 ? 0.2959 0.4420 2.2303 -0.0939 0.0560  -0.0871 281 SER D O   
14978 C CB  . SER D 281 ? 0.2687 0.4108 2.1909 -0.1026 0.0327  -0.0950 281 SER D CB  
14979 O OG  . SER D 281 ? 0.2796 0.4174 2.1853 -0.1044 0.0179  -0.0975 281 SER D OG  
14980 N N   . ASP D 282 ? 0.2196 0.3337 2.0950 -0.0956 0.0776  -0.0795 282 ASP D N   
14981 C CA  . ASP D 282 ? 0.1979 0.3118 2.0789 -0.0931 0.0921  -0.0774 282 ASP D CA  
14982 C C   . ASP D 282 ? 0.1995 0.2996 2.0407 -0.0859 0.0933  -0.0685 282 ASP D C   
14983 O O   . ASP D 282 ? 0.2219 0.3053 2.0309 -0.0869 0.0975  -0.0653 282 ASP D O   
14984 C CB  . ASP D 282 ? 0.1965 0.3033 2.0880 -0.1015 0.1147  -0.0818 282 ASP D CB  
14985 C CG  . ASP D 282 ? 0.1971 0.2994 2.0878 -0.0999 0.1328  -0.0804 282 ASP D CG  
14986 O OD1 . ASP D 282 ? 0.1980 0.3154 2.1190 -0.0974 0.1331  -0.0837 282 ASP D OD1 
14987 O OD2 . ASP D 282 ? 0.2111 0.2941 2.0710 -0.1012 0.1468  -0.0764 282 ASP D OD2 
14988 N N   . HIS D 283 ? 0.1828 0.2904 2.0286 -0.0786 0.0882  -0.0651 283 HIS D N   
14989 C CA  . HIS D 283 ? 0.1784 0.2752 1.9946 -0.0722 0.0915  -0.0579 283 HIS D CA  
14990 C C   . HIS D 283 ? 0.1854 0.2732 2.0001 -0.0744 0.1123  -0.0592 283 HIS D C   
14991 O O   . HIS D 283 ? 0.1807 0.2760 2.0150 -0.0723 0.1177  -0.0613 283 HIS D O   
14992 C CB  . HIS D 283 ? 0.1663 0.2731 1.9876 -0.0641 0.0773  -0.0536 283 HIS D CB  
14993 C CG  . HIS D 283 ? 0.1738 0.2706 1.9613 -0.0581 0.0732  -0.0458 283 HIS D CG  
14994 N ND1 . HIS D 283 ? 0.1794 0.2812 1.9670 -0.0512 0.0636  -0.0409 283 HIS D ND1 
14995 C CD2 . HIS D 283 ? 0.1833 0.2654 1.9376 -0.0580 0.0766  -0.0423 283 HIS D CD2 
14996 C CE1 . HIS D 283 ? 0.1835 0.2748 1.9397 -0.0479 0.0623  -0.0349 283 HIS D CE1 
14997 N NE2 . HIS D 283 ? 0.1794 0.2592 1.9160 -0.0515 0.0700  -0.0359 283 HIS D NE2 
14998 N N   . SER D 284 ? 0.2073 0.2773 1.9964 -0.0785 0.1239  -0.0580 284 SER D N   
14999 C CA  . SER D 284 ? 0.2215 0.2784 2.0011 -0.0813 0.1438  -0.0586 284 SER D CA  
15000 C C   . SER D 284 ? 0.2149 0.2677 1.9790 -0.0739 0.1450  -0.0545 284 SER D C   
15001 O O   . SER D 284 ? 0.2150 0.2653 1.9592 -0.0676 0.1334  -0.0490 284 SER D O   
15002 C CB  . SER D 284 ? 0.2463 0.2825 1.9966 -0.0859 0.1517  -0.0564 284 SER D CB  
15003 O OG  . SER D 284 ? 0.2675 0.2872 2.0024 -0.0890 0.1707  -0.0559 284 SER D OG  
15004 N N   . LEU D 285 ? 0.2146 0.2673 1.9899 -0.0749 0.1594  -0.0580 285 LEU D N   
15005 C CA  . LEU D 285 ? 0.2004 0.2501 1.9656 -0.0683 0.1610  -0.0559 285 LEU D CA  
15006 C C   . LEU D 285 ? 0.2278 0.2545 1.9498 -0.0673 0.1668  -0.0510 285 LEU D C   
15007 O O   . LEU D 285 ? 0.2308 0.2527 1.9366 -0.0610 0.1633  -0.0480 285 LEU D O   
15008 C CB  . LEU D 285 ? 0.1920 0.2471 1.9810 -0.0699 0.1762  -0.0624 285 LEU D CB  
15009 C CG  . LEU D 285 ? 0.1720 0.2504 2.0097 -0.0707 0.1723  -0.0688 285 LEU D CG  
15010 C CD1 . LEU D 285 ? 0.1778 0.2576 2.0341 -0.0726 0.1917  -0.0759 285 LEU D CD1 
15011 C CD2 . LEU D 285 ? 0.1513 0.2443 2.0028 -0.0628 0.1508  -0.0657 285 LEU D CD2 
15012 N N   . ASN D 286 ? 0.2496 0.2615 1.9543 -0.0734 0.1753  -0.0504 286 ASN D N   
15013 C CA  . ASN D 286 ? 0.2818 0.2700 1.9456 -0.0722 0.1807  -0.0457 286 ASN D CA  
15014 C C   . ASN D 286 ? 0.2834 0.2622 1.9277 -0.0727 0.1722  -0.0415 286 ASN D C   
15015 O O   . ASN D 286 ? 0.3188 0.2764 1.9356 -0.0750 0.1797  -0.0388 286 ASN D O   
15016 C CB  . ASN D 286 ? 0.3289 0.3007 1.9817 -0.0784 0.2019  -0.0480 286 ASN D CB  
15017 C CG  . ASN D 286 ? 0.3796 0.3496 2.0450 -0.0879 0.2115  -0.0507 286 ASN D CG  
15018 O OD1 . ASN D 286 ? 0.4033 0.3876 2.0916 -0.0897 0.2016  -0.0524 286 ASN D OD1 
15019 N ND2 . ASN D 286 ? 0.4242 0.3757 2.0741 -0.0945 0.2306  -0.0512 286 ASN D ND2 
15020 N N   . GLN D 287 ? 0.2653 0.2583 1.9222 -0.0702 0.1566  -0.0409 287 GLN D N   
15021 C CA  . GLN D 287 ? 0.2623 0.2467 1.8999 -0.0694 0.1479  -0.0376 287 GLN D CA  
15022 C C   . GLN D 287 ? 0.2396 0.2281 1.8652 -0.0610 0.1336  -0.0333 287 GLN D C   
15023 O O   . GLN D 287 ? 0.2131 0.2169 1.8525 -0.0587 0.1215  -0.0334 287 GLN D O   
15024 C CB  . GLN D 287 ? 0.2576 0.2511 1.9142 -0.0748 0.1431  -0.0411 287 GLN D CB  
15025 C CG  . GLN D 287 ? 0.2782 0.2651 1.9454 -0.0841 0.1580  -0.0452 287 GLN D CG  
15026 C CD  . GLN D 287 ? 0.3084 0.2700 1.9458 -0.0872 0.1663  -0.0421 287 GLN D CD  
15027 O OE1 . GLN D 287 ? 0.3235 0.2750 1.9377 -0.0828 0.1579  -0.0382 287 GLN D OE1 
15028 N NE2 . GLN D 287 ? 0.3364 0.2868 1.9752 -0.0950 0.1832  -0.0439 287 GLN D NE2 
15029 N N   . PRO D 288 ? 0.2451 0.2191 1.8439 -0.0564 0.1347  -0.0295 288 PRO D N   
15030 C CA  . PRO D 288 ? 0.2451 0.2221 1.8334 -0.0490 0.1224  -0.0258 288 PRO D CA  
15031 C C   . PRO D 288 ? 0.2462 0.2315 1.8376 -0.0479 0.1108  -0.0251 288 PRO D C   
15032 O O   . PRO D 288 ? 0.2510 0.2458 1.8441 -0.0431 0.1011  -0.0229 288 PRO D O   
15033 C CB  . PRO D 288 ? 0.2546 0.2104 1.8121 -0.0463 0.1257  -0.0228 288 PRO D CB  
15034 C CG  . PRO D 288 ? 0.2709 0.2157 1.8242 -0.0507 0.1404  -0.0246 288 PRO D CG  
15035 C CD  . PRO D 288 ? 0.2654 0.2187 1.8423 -0.0583 0.1475  -0.0286 288 PRO D CD  
15036 N N   . GLU D 289 ? 0.2632 0.2436 1.8539 -0.0526 0.1124  -0.0270 289 GLU D N   
15037 C CA  . GLU D 289 ? 0.2700 0.2552 1.8595 -0.0516 0.1025  -0.0273 289 GLU D CA  
15038 C C   . GLU D 289 ? 0.2402 0.2456 1.8515 -0.0518 0.0937  -0.0288 289 GLU D C   
15039 O O   . GLU D 289 ? 0.2326 0.2443 1.8406 -0.0490 0.0839  -0.0278 289 GLU D O   
15040 C CB  . GLU D 289 ? 0.3072 0.2800 1.8903 -0.0568 0.1069  -0.0297 289 GLU D CB  
15041 C CG  . GLU D 289 ? 0.3375 0.2891 1.8940 -0.0539 0.1099  -0.0268 289 GLU D CG  
15042 C CD  . GLU D 289 ? 0.3752 0.3266 1.9179 -0.0459 0.1009  -0.0238 289 GLU D CD  
15043 O OE1 . GLU D 289 ? 0.3935 0.3528 1.9385 -0.0440 0.0929  -0.0251 289 GLU D OE1 
15044 O OE2 . GLU D 289 ? 0.3879 0.3306 1.9170 -0.0415 0.1021  -0.0206 289 GLU D OE2 
15045 N N   . GLU D 290 ? 0.2304 0.2454 1.8638 -0.0547 0.0971  -0.0312 290 GLU D N   
15046 C CA  . GLU D 290 ? 0.2252 0.2577 1.8813 -0.0558 0.0878  -0.0333 290 GLU D CA  
15047 C C   . GLU D 290 ? 0.2284 0.2712 1.8900 -0.0499 0.0803  -0.0296 290 GLU D C   
15048 O O   . GLU D 290 ? 0.2275 0.2838 1.9079 -0.0498 0.0718  -0.0303 290 GLU D O   
15049 C CB  . GLU D 290 ? 0.2229 0.2613 1.9047 -0.0622 0.0947  -0.0388 290 GLU D CB  
15050 C CG  . GLU D 290 ? 0.2319 0.2626 1.9141 -0.0694 0.1000  -0.0430 290 GLU D CG  
15051 C CD  . GLU D 290 ? 0.2343 0.2754 1.9485 -0.0763 0.1039  -0.0494 290 GLU D CD  
15052 O OE1 . GLU D 290 ? 0.2210 0.2766 1.9587 -0.0747 0.1015  -0.0507 290 GLU D OE1 
15053 O OE2 . GLU D 290 ? 0.2519 0.2877 1.9710 -0.0833 0.1089  -0.0536 290 GLU D OE2 
15054 N N   . TRP D 291 ? 0.2303 0.2662 1.8760 -0.0450 0.0824  -0.0256 291 TRP D N   
15055 C CA  . TRP D 291 ? 0.2155 0.2597 1.8687 -0.0403 0.0773  -0.0224 291 TRP D CA  
15056 C C   . TRP D 291 ? 0.2175 0.2577 1.8519 -0.0353 0.0723  -0.0176 291 TRP D C   
15057 O O   . TRP D 291 ? 0.2208 0.2629 1.8578 -0.0317 0.0714  -0.0151 291 TRP D O   
15058 C CB  . TRP D 291 ? 0.2150 0.2574 1.8775 -0.0400 0.0869  -0.0241 291 TRP D CB  
15059 C CG  . TRP D 291 ? 0.2047 0.2546 1.8927 -0.0446 0.0924  -0.0294 291 TRP D CG  
15060 C CD1 . TRP D 291 ? 0.2089 0.2530 1.8984 -0.0506 0.1021  -0.0334 291 TRP D CD1 
15061 C CD2 . TRP D 291 ? 0.1812 0.2453 1.8985 -0.0437 0.0893  -0.0314 291 TRP D CD2 
15062 N NE1 . TRP D 291 ? 0.2136 0.2686 1.9326 -0.0539 0.1059  -0.0383 291 TRP D NE1 
15063 C CE2 . TRP D 291 ? 0.1992 0.2669 1.9365 -0.0494 0.0978  -0.0375 291 TRP D CE2 
15064 C CE3 . TRP D 291 ? 0.1724 0.2460 1.9023 -0.0387 0.0801  -0.0287 291 TRP D CE3 
15065 C CZ2 . TRP D 291 ? 0.1869 0.2689 1.9583 -0.0497 0.0971  -0.0417 291 TRP D CZ2 
15066 C CZ3 . TRP D 291 ? 0.1635 0.2495 1.9251 -0.0386 0.0786  -0.0322 291 TRP D CZ3 
15067 C CH2 . TRP D 291 ? 0.1664 0.2573 1.9495 -0.0437 0.0869  -0.0390 291 TRP D CH2 
15068 N N   . PHE D 292 ? 0.2205 0.2557 1.8386 -0.0351 0.0692  -0.0169 292 PHE D N   
15069 C CA  . PHE D 292 ? 0.2125 0.2448 1.8154 -0.0307 0.0657  -0.0132 292 PHE D CA  
15070 C C   . PHE D 292 ? 0.2099 0.2524 1.8161 -0.0292 0.0566  -0.0099 292 PHE D C   
15071 O O   . PHE D 292 ? 0.2073 0.2489 1.8033 -0.0264 0.0545  -0.0071 292 PHE D O   
15072 C CB  . PHE D 292 ? 0.2239 0.2461 1.8093 -0.0307 0.0674  -0.0146 292 PHE D CB  
15073 C CG  . PHE D 292 ? 0.2277 0.2353 1.8006 -0.0295 0.0745  -0.0151 292 PHE D CG  
15074 C CD1 . PHE D 292 ? 0.2120 0.2146 1.7748 -0.0246 0.0734  -0.0129 292 PHE D CD1 
15075 C CD2 . PHE D 292 ? 0.2315 0.2296 1.8025 -0.0335 0.0817  -0.0178 292 PHE D CD2 
15076 C CE1 . PHE D 292 ? 0.2198 0.2078 1.7692 -0.0231 0.0778  -0.0132 292 PHE D CE1 
15077 C CE2 . PHE D 292 ? 0.2340 0.2162 1.7897 -0.0324 0.0876  -0.0173 292 PHE D CE2 
15078 C CZ  . PHE D 292 ? 0.2329 0.2097 1.7767 -0.0269 0.0848  -0.0149 292 PHE D CZ  
15079 N N   . GLY D 293 ? 0.2294 0.2813 1.8504 -0.0310 0.0511  -0.0100 293 GLY D N   
15080 C CA  . GLY D 293 ? 0.2226 0.2815 1.8429 -0.0301 0.0416  -0.0063 293 GLY D CA  
15081 C C   . GLY D 293 ? 0.2107 0.2713 1.8317 -0.0263 0.0398  -0.0006 293 GLY D C   
15082 O O   . GLY D 293 ? 0.2138 0.2732 1.8430 -0.0246 0.0440  -0.0006 293 GLY D O   
15083 N N   . PHE D 294 ? 0.2001 0.2621 1.8109 -0.0255 0.0344  0.0037  294 PHE D N   
15084 C CA  . PHE D 294 ? 0.1880 0.2527 1.8028 -0.0232 0.0302  0.0100  294 PHE D CA  
15085 C C   . PHE D 294 ? 0.2054 0.2763 1.8338 -0.0236 0.0210  0.0118  294 PHE D C   
15086 O O   . PHE D 294 ? 0.2215 0.2943 1.8599 -0.0214 0.0171  0.0164  294 PHE D O   
15087 C CB  . PHE D 294 ? 0.1843 0.2471 1.7824 -0.0229 0.0296  0.0141  294 PHE D CB  
15088 C CG  . PHE D 294 ? 0.1772 0.2356 1.7668 -0.0216 0.0371  0.0126  294 PHE D CG  
15089 C CD1 . PHE D 294 ? 0.1733 0.2277 1.7659 -0.0204 0.0427  0.0082  294 PHE D CD1 
15090 C CD2 . PHE D 294 ? 0.1754 0.2331 1.7532 -0.0215 0.0386  0.0153  294 PHE D CD2 
15091 C CE1 . PHE D 294 ? 0.1665 0.2164 1.7519 -0.0185 0.0473  0.0068  294 PHE D CE1 
15092 C CE2 . PHE D 294 ? 0.1738 0.2289 1.7478 -0.0199 0.0445  0.0131  294 PHE D CE2 
15093 C CZ  . PHE D 294 ? 0.1708 0.2221 1.7489 -0.0180 0.0477  0.0089  294 PHE D CZ  
15094 N N   . TRP D 295 ? 0.2005 0.2742 1.8308 -0.0263 0.0168  0.0078  295 TRP D N   
15095 C CA  . TRP D 295 ? 0.1889 0.2691 1.8343 -0.0265 0.0063  0.0082  295 TRP D CA  
15096 C C   . TRP D 295 ? 0.1724 0.2573 1.8382 -0.0287 0.0091  0.0009  295 TRP D C   
15097 O O   . TRP D 295 ? 0.1754 0.2572 1.8362 -0.0317 0.0161  -0.0045 295 TRP D O   
15098 C CB  . TRP D 295 ? 0.2012 0.2810 1.8312 -0.0282 -0.0039 0.0099  295 TRP D CB  
15099 C CG  . TRP D 295 ? 0.2177 0.2930 1.8289 -0.0268 -0.0078 0.0181  295 TRP D CG  
15100 C CD1 . TRP D 295 ? 0.2252 0.2952 1.8199 -0.0263 0.0000  0.0212  295 TRP D CD1 
15101 C CD2 . TRP D 295 ? 0.2323 0.3073 1.8391 -0.0259 -0.0208 0.0243  295 TRP D CD2 
15102 N NE1 . TRP D 295 ? 0.2380 0.3044 1.8183 -0.0260 -0.0053 0.0288  295 TRP D NE1 
15103 C CE2 . TRP D 295 ? 0.2537 0.3218 1.8388 -0.0257 -0.0184 0.0313  295 TRP D CE2 
15104 C CE3 . TRP D 295 ? 0.2378 0.3170 1.8570 -0.0253 -0.0346 0.0245  295 TRP D CE3 
15105 C CZ2 . TRP D 295 ? 0.2701 0.3336 1.8424 -0.0253 -0.0285 0.0394  295 TRP D CZ2 
15106 C CZ3 . TRP D 295 ? 0.2594 0.3341 1.8658 -0.0241 -0.0467 0.0323  295 TRP D CZ3 
15107 C CH2 . TRP D 295 ? 0.2723 0.3384 1.8543 -0.0242 -0.0432 0.0402  295 TRP D CH2 
15108 N N   . GLY D 296 ? 0.1624 0.2546 1.8524 -0.0274 0.0036  0.0006  296 GLY D N   
15109 C CA  . GLY D 296 ? 0.1536 0.2515 1.8684 -0.0292 0.0084  -0.0064 296 GLY D CA  
15110 C C   . GLY D 296 ? 0.1588 0.2660 1.8924 -0.0303 -0.0045 -0.0088 296 GLY D C   
15111 O O   . GLY D 296 ? 0.1696 0.2786 1.9020 -0.0275 -0.0178 -0.0035 296 GLY D O   
15112 N N   . TYR D 297 ? 0.1639 0.2756 1.9126 -0.0347 -0.0012 -0.0166 297 TYR D N   
15113 C CA  . TYR D 297 ? 0.1658 0.2874 1.9358 -0.0362 -0.0139 -0.0205 297 TYR D CA  
15114 C C   . TYR D 297 ? 0.1591 0.2907 1.9669 -0.0350 -0.0108 -0.0248 297 TYR D C   
15115 O O   . TYR D 297 ? 0.1533 0.2839 1.9698 -0.0370 0.0050  -0.0290 297 TYR D O   
15116 C CB  . TYR D 297 ? 0.1644 0.2840 1.9261 -0.0422 -0.0129 -0.0267 297 TYR D CB  
15117 C CG  . TYR D 297 ? 0.1630 0.2731 1.8883 -0.0422 -0.0173 -0.0227 297 TYR D CG  
15118 C CD1 . TYR D 297 ? 0.1731 0.2835 1.8865 -0.0402 -0.0334 -0.0184 297 TYR D CD1 
15119 C CD2 . TYR D 297 ? 0.1533 0.2535 1.8562 -0.0441 -0.0053 -0.0234 297 TYR D CD2 
15120 C CE1 . TYR D 297 ? 0.1825 0.2842 1.8627 -0.0408 -0.0358 -0.0158 297 TYR D CE1 
15121 C CE2 . TYR D 297 ? 0.1633 0.2560 1.8364 -0.0441 -0.0084 -0.0213 297 TYR D CE2 
15122 C CZ  . TYR D 297 ? 0.1778 0.2713 1.8390 -0.0426 -0.0226 -0.0176 297 TYR D CZ  
15123 O OH  . TYR D 297 ? 0.1885 0.2742 1.8191 -0.0427 -0.0239 -0.0156 297 TYR D OH  
15124 N N   . SER D 298 ? 0.1692 0.3091 1.9968 -0.0313 -0.0260 -0.0231 298 SER D N   
15125 C CA  . SER D 298 ? 0.1731 0.3235 2.0392 -0.0284 -0.0261 -0.0264 298 SER D CA  
15126 C C   . SER D 298 ? 0.1859 0.3458 2.0823 -0.0338 -0.0172 -0.0372 298 SER D C   
15127 O O   . SER D 298 ? 0.1829 0.3441 2.0948 -0.0348 -0.0008 -0.0416 298 SER D O   
15128 C CB  . SER D 298 ? 0.1807 0.3365 2.0584 -0.0232 -0.0477 -0.0220 298 SER D CB  
15129 O OG  . SER D 298 ? 0.1948 0.3646 2.1170 -0.0219 -0.0526 -0.0287 298 SER D OG  
15130 N N   . ASP D 299 ? 0.2033 0.3688 2.1064 -0.0378 -0.0281 -0.0416 299 ASP D N   
15131 C CA  . ASP D 299 ? 0.2058 0.3805 2.1382 -0.0442 -0.0219 -0.0521 299 ASP D CA  
15132 C C   . ASP D 299 ? 0.2316 0.4030 2.1467 -0.0498 -0.0299 -0.0546 299 ASP D C   
15133 O O   . ASP D 299 ? 0.2388 0.4000 2.1174 -0.0485 -0.0368 -0.0486 299 ASP D O   
15134 C CB  . ASP D 299 ? 0.2013 0.3926 2.1810 -0.0415 -0.0314 -0.0571 299 ASP D CB  
15135 C CG  . ASP D 299 ? 0.2161 0.4128 2.2007 -0.0368 -0.0587 -0.0538 299 ASP D CG  
15136 O OD1 . ASP D 299 ? 0.2082 0.3959 2.1580 -0.0373 -0.0698 -0.0488 299 ASP D OD1 
15137 O OD2 . ASP D 299 ? 0.2377 0.4473 2.2616 -0.0327 -0.0686 -0.0568 299 ASP D OD2 
15138 N N   . LEU D 300 ? 0.2461 0.4258 2.1878 -0.0563 -0.0279 -0.0642 300 LEU D N   
15139 C CA  . LEU D 300 ? 0.2528 0.4269 2.1772 -0.0628 -0.0305 -0.0681 300 LEU D CA  
15140 C C   . LEU D 300 ? 0.2745 0.4480 2.1818 -0.0602 -0.0548 -0.0653 300 LEU D C   
15141 O O   . LEU D 300 ? 0.2902 0.4532 2.1651 -0.0628 -0.0568 -0.0646 300 LEU D O   
15142 C CB  . LEU D 300 ? 0.2506 0.4339 2.2104 -0.0710 -0.0244 -0.0793 300 LEU D CB  
15143 C CG  . LEU D 300 ? 0.2615 0.4385 2.2067 -0.0782 -0.0277 -0.0844 300 LEU D CG  
15144 C CD1 . LEU D 300 ? 0.2727 0.4318 2.1824 -0.0812 -0.0090 -0.0814 300 LEU D CD1 
15145 C CD2 . LEU D 300 ? 0.2632 0.4527 2.2513 -0.0859 -0.0276 -0.0959 300 LEU D CD2 
15146 N N   . ASN D 301 ? 0.2682 0.4521 2.1969 -0.0549 -0.0732 -0.0639 301 ASN D N   
15147 C CA  . ASN D 301 ? 0.2767 0.4595 2.1905 -0.0530 -0.0977 -0.0621 301 ASN D CA  
15148 C C   . ASN D 301 ? 0.2802 0.4496 2.1503 -0.0472 -0.1028 -0.0503 301 ASN D C   
15149 O O   . ASN D 301 ? 0.3213 0.4869 2.1723 -0.0454 -0.1221 -0.0473 301 ASN D O   
15150 C CB  . ASN D 301 ? 0.2860 0.4836 2.2386 -0.0493 -0.1182 -0.0650 301 ASN D CB  
15151 C CG  . ASN D 301 ? 0.2851 0.4984 2.2871 -0.0550 -0.1134 -0.0775 301 ASN D CG  
15152 O OD1 . ASN D 301 ? 0.2877 0.5008 2.2906 -0.0629 -0.1107 -0.0854 301 ASN D OD1 
15153 N ND2 . ASN D 301 ? 0.2750 0.5014 2.3194 -0.0514 -0.1113 -0.0796 301 ASN D ND2 
15154 N N   . ASP D 302 ? 0.2447 0.4066 2.0990 -0.0448 -0.0858 -0.0439 302 ASP D N   
15155 C CA  . ASP D 302 ? 0.2347 0.3852 2.0531 -0.0397 -0.0888 -0.0328 302 ASP D CA  
15156 C C   . ASP D 302 ? 0.2356 0.3732 2.0116 -0.0432 -0.0832 -0.0317 302 ASP D C   
15157 O O   . ASP D 302 ? 0.2108 0.3431 1.9776 -0.0463 -0.0653 -0.0338 302 ASP D O   
15158 C CB  . ASP D 302 ? 0.2206 0.3698 2.0448 -0.0356 -0.0747 -0.0275 302 ASP D CB  
15159 C CG  . ASP D 302 ? 0.2270 0.3649 2.0188 -0.0309 -0.0756 -0.0162 302 ASP D CG  
15160 O OD1 . ASP D 302 ? 0.2425 0.3736 2.0070 -0.0303 -0.0883 -0.0113 302 ASP D OD1 
15161 O OD2 . ASP D 302 ? 0.2218 0.3572 2.0152 -0.0282 -0.0631 -0.0127 302 ASP D OD2 
15162 N N   . LYS D 303 ? 0.2517 0.3830 2.0008 -0.0420 -0.0989 -0.0277 303 LYS D N   
15163 C CA  . LYS D 303 ? 0.2590 0.3780 1.9669 -0.0444 -0.0957 -0.0266 303 LYS D CA  
15164 C C   . LYS D 303 ? 0.2522 0.3608 1.9287 -0.0405 -0.0899 -0.0159 303 LYS D C   
15165 O O   . LYS D 303 ? 0.2544 0.3531 1.8973 -0.0421 -0.0860 -0.0149 303 LYS D O   
15166 C CB  . LYS D 303 ? 0.2919 0.4094 1.9871 -0.0460 -0.1161 -0.0297 303 LYS D CB  
15167 C CG  . LYS D 303 ? 0.3027 0.4299 2.0270 -0.0508 -0.1241 -0.0414 303 LYS D CG  
15168 C CD  . LYS D 303 ? 0.3035 0.4311 2.0373 -0.0570 -0.1058 -0.0500 303 LYS D CD  
15169 C CE  . LYS D 303 ? 0.3210 0.4617 2.0977 -0.0611 -0.1098 -0.0598 303 LYS D CE  
15170 N NZ  . LYS D 303 ? 0.3300 0.4687 2.1147 -0.0672 -0.0901 -0.0664 303 LYS D NZ  
15171 N N   . TYR D 304 ? 0.2394 0.3500 1.9276 -0.0356 -0.0888 -0.0085 304 TYR D N   
15172 C CA  . TYR D 304 ? 0.2440 0.3449 1.9050 -0.0321 -0.0869 0.0022  304 TYR D CA  
15173 C C   . TYR D 304 ? 0.2223 0.3230 1.8914 -0.0303 -0.0695 0.0048  304 TYR D C   
15174 O O   . TYR D 304 ? 0.2201 0.3135 1.8665 -0.0311 -0.0576 0.0070  304 TYR D O   
15175 C CB  . TYR D 304 ? 0.2599 0.3594 1.9199 -0.0280 -0.1064 0.0099  304 TYR D CB  
15176 C CG  . TYR D 304 ? 0.2798 0.3767 1.9237 -0.0301 -0.1240 0.0071  304 TYR D CG  
15177 C CD1 . TYR D 304 ? 0.2976 0.3824 1.8991 -0.0323 -0.1242 0.0097  304 TYR D CD1 
15178 C CD2 . TYR D 304 ? 0.2840 0.3906 1.9556 -0.0302 -0.1398 0.0006  304 TYR D CD2 
15179 C CE1 . TYR D 304 ? 0.3214 0.4022 1.9047 -0.0345 -0.1399 0.0062  304 TYR D CE1 
15180 C CE2 . TYR D 304 ? 0.3094 0.4131 1.9655 -0.0323 -0.1571 -0.0029 304 TYR D CE2 
15181 C CZ  . TYR D 304 ? 0.3301 0.4201 1.9401 -0.0346 -0.1571 -0.0003 304 TYR D CZ  
15182 O OH  . TYR D 304 ? 0.3558 0.4412 1.9470 -0.0368 -0.1741 -0.0045 304 TYR D OH  
15183 N N   . GLY D 305 ? 0.2112 0.3201 1.9135 -0.0278 -0.0682 0.0036  305 GLY D N   
15184 C CA  . GLY D 305 ? 0.1968 0.3054 1.9081 -0.0263 -0.0522 0.0044  305 GLY D CA  
15185 C C   . GLY D 305 ? 0.2024 0.3050 1.9042 -0.0218 -0.0536 0.0145  305 GLY D C   
15186 O O   . GLY D 305 ? 0.2161 0.3149 1.9071 -0.0196 -0.0670 0.0215  305 GLY D O   
15187 N N   . THR D 306 ? 0.1933 0.2939 1.8986 -0.0204 -0.0400 0.0153  306 THR D N   
15188 C CA  . THR D 306 ? 0.2030 0.2971 1.8991 -0.0170 -0.0397 0.0241  306 THR D CA  
15189 C C   . THR D 306 ? 0.1929 0.2816 1.8749 -0.0181 -0.0239 0.0237  306 THR D C   
15190 O O   . THR D 306 ? 0.1766 0.2672 1.8663 -0.0195 -0.0131 0.0169  306 THR D O   
15191 C CB  . THR D 306 ? 0.2001 0.2983 1.9252 -0.0124 -0.0439 0.0257  306 THR D CB  
15192 O OG1 . THR D 306 ? 0.1936 0.2964 1.9374 -0.0130 -0.0303 0.0180  306 THR D OG1 
15193 C CG2 . THR D 306 ? 0.2042 0.3086 1.9482 -0.0103 -0.0612 0.0258  306 THR D CG2 
15194 N N   . PRO D 307 ? 0.2032 0.2844 1.8654 -0.0174 -0.0226 0.0312  307 PRO D N   
15195 C CA  . PRO D 307 ? 0.1986 0.2755 1.8507 -0.0178 -0.0094 0.0308  307 PRO D CA  
15196 C C   . PRO D 307 ? 0.1878 0.2657 1.8594 -0.0153 -0.0025 0.0286  307 PRO D C   
15197 O O   . PRO D 307 ? 0.2104 0.2879 1.8944 -0.0124 -0.0073 0.0331  307 PRO D O   
15198 C CB  . PRO D 307 ? 0.2106 0.2804 1.8420 -0.0179 -0.0115 0.0398  307 PRO D CB  
15199 C CG  . PRO D 307 ? 0.2216 0.2903 1.8573 -0.0160 -0.0253 0.0467  307 PRO D CG  
15200 C CD  . PRO D 307 ? 0.2221 0.2981 1.8722 -0.0161 -0.0338 0.0406  307 PRO D CD  
15201 N N   . ARG D 308 ? 0.1713 0.2486 1.8426 -0.0163 0.0086  0.0224  308 ARG D N   
15202 C CA  . ARG D 308 ? 0.1708 0.2461 1.8523 -0.0142 0.0162  0.0204  308 ARG D CA  
15203 C C   . ARG D 308 ? 0.1949 0.2642 1.8652 -0.0131 0.0183  0.0257  308 ARG D C   
15204 O O   . ARG D 308 ? 0.2005 0.2673 1.8540 -0.0144 0.0169  0.0304  308 ARG D O   
15205 C CB  . ARG D 308 ? 0.1644 0.2381 1.8437 -0.0159 0.0267  0.0128  308 ARG D CB  
15206 C CG  . ARG D 308 ? 0.1632 0.2422 1.8551 -0.0181 0.0271  0.0069  308 ARG D CG  
15207 C CD  . ARG D 308 ? 0.1532 0.2276 1.8364 -0.0209 0.0375  0.0009  308 ARG D CD  
15208 N NE  . ARG D 308 ? 0.1488 0.2284 1.8479 -0.0237 0.0393  -0.0049 308 ARG D NE  
15209 C CZ  . ARG D 308 ? 0.1512 0.2290 1.8438 -0.0277 0.0426  -0.0088 308 ARG D CZ  
15210 N NH1 . ARG D 308 ? 0.1616 0.2320 1.8309 -0.0284 0.0446  -0.0077 308 ARG D NH1 
15211 N NH2 . ARG D 308 ? 0.1385 0.2217 1.8495 -0.0308 0.0446  -0.0142 308 ARG D NH2 
15212 N N   . PRO D 309 ? 0.1951 0.2621 1.8757 -0.0109 0.0225  0.0245  309 PRO D N   
15213 C CA  . PRO D 309 ? 0.1983 0.2602 1.8722 -0.0103 0.0241  0.0287  309 PRO D CA  
15214 C C   . PRO D 309 ? 0.2039 0.2634 1.8587 -0.0123 0.0283  0.0291  309 PRO D C   
15215 O O   . PRO D 309 ? 0.2220 0.2794 1.8702 -0.0130 0.0274  0.0346  309 PRO D O   
15216 C CB  . PRO D 309 ? 0.1943 0.2539 1.8812 -0.0081 0.0294  0.0234  309 PRO D CB  
15217 C CG  . PRO D 309 ? 0.1919 0.2562 1.8983 -0.0065 0.0264  0.0211  309 PRO D CG  
15218 C CD  . PRO D 309 ? 0.1893 0.2580 1.8894 -0.0091 0.0260  0.0188  309 PRO D CD  
15219 N N   . VAL D 310 ? 0.2002 0.2595 1.8470 -0.0132 0.0333  0.0233  310 VAL D N   
15220 C CA  . VAL D 310 ? 0.1801 0.2370 1.8124 -0.0139 0.0372  0.0226  310 VAL D CA  
15221 C C   . VAL D 310 ? 0.1712 0.2296 1.7924 -0.0159 0.0345  0.0280  310 VAL D C   
15222 O O   . VAL D 310 ? 0.1679 0.2253 1.7819 -0.0164 0.0376  0.0293  310 VAL D O   
15223 C CB  . VAL D 310 ? 0.1879 0.2427 1.8127 -0.0143 0.0419  0.0162  310 VAL D CB  
15224 C CG1 . VAL D 310 ? 0.1918 0.2496 1.8130 -0.0166 0.0396  0.0151  310 VAL D CG1 
15225 C CG2 . VAL D 310 ? 0.1934 0.2449 1.8068 -0.0137 0.0454  0.0145  310 VAL D CG2 
15226 N N   . TRP D 311 ? 0.1700 0.2307 1.7896 -0.0171 0.0287  0.0305  311 TRP D N   
15227 C CA  . TRP D 311 ? 0.1727 0.2329 1.7777 -0.0192 0.0258  0.0354  311 TRP D CA  
15228 C C   . TRP D 311 ? 0.1890 0.2465 1.7922 -0.0196 0.0267  0.0424  311 TRP D C   
15229 O O   . TRP D 311 ? 0.2158 0.2721 1.8070 -0.0214 0.0314  0.0439  311 TRP D O   
15230 C CB  . TRP D 311 ? 0.1694 0.2314 1.7758 -0.0196 0.0166  0.0375  311 TRP D CB  
15231 C CG  . TRP D 311 ? 0.1729 0.2326 1.7608 -0.0218 0.0117  0.0424  311 TRP D CG  
15232 C CD1 . TRP D 311 ? 0.1834 0.2396 1.7672 -0.0218 0.0042  0.0508  311 TRP D CD1 
15233 C CD2 . TRP D 311 ? 0.1757 0.2347 1.7453 -0.0242 0.0128  0.0391  311 TRP D CD2 
15234 N NE1 . TRP D 311 ? 0.1974 0.2503 1.7593 -0.0243 0.0008  0.0532  311 TRP D NE1 
15235 C CE2 . TRP D 311 ? 0.1926 0.2476 1.7459 -0.0258 0.0063  0.0455  311 TRP D CE2 
15236 C CE3 . TRP D 311 ? 0.1671 0.2272 1.7316 -0.0251 0.0186  0.0312  311 TRP D CE3 
15237 C CZ2 . TRP D 311 ? 0.2038 0.2562 1.7352 -0.0284 0.0060  0.0436  311 TRP D CZ2 
15238 C CZ3 . TRP D 311 ? 0.1774 0.2354 1.7229 -0.0274 0.0183  0.0292  311 TRP D CZ3 
15239 C CH2 . TRP D 311 ? 0.1963 0.2509 1.7252 -0.0291 0.0122  0.0349  311 TRP D CH2 
15240 N N   . PHE D 312 ? 0.1918 0.2479 1.8089 -0.0179 0.0230  0.0461  312 PHE D N   
15241 C CA  . PHE D 312 ? 0.2034 0.2553 1.8209 -0.0187 0.0226  0.0539  312 PHE D CA  
15242 C C   . PHE D 312 ? 0.1982 0.2498 1.8186 -0.0192 0.0307  0.0515  312 PHE D C   
15243 O O   . PHE D 312 ? 0.1971 0.2465 1.8114 -0.0217 0.0341  0.0563  312 PHE D O   
15244 C CB  . PHE D 312 ? 0.1999 0.2499 1.8335 -0.0161 0.0156  0.0573  312 PHE D CB  
15245 C CG  . PHE D 312 ? 0.2151 0.2654 1.8474 -0.0154 0.0054  0.0608  312 PHE D CG  
15246 C CD1 . PHE D 312 ? 0.2424 0.2874 1.8585 -0.0172 -0.0002 0.0695  312 PHE D CD1 
15247 C CD2 . PHE D 312 ? 0.2162 0.2716 1.8640 -0.0129 0.0012  0.0554  312 PHE D CD2 
15248 C CE1 . PHE D 312 ? 0.2633 0.3078 1.8779 -0.0160 -0.0119 0.0726  312 PHE D CE1 
15249 C CE2 . PHE D 312 ? 0.2301 0.2870 1.8805 -0.0119 -0.0096 0.0578  312 PHE D CE2 
15250 C CZ  . PHE D 312 ? 0.2491 0.3003 1.8826 -0.0131 -0.0172 0.0664  312 PHE D CZ  
15251 N N   . ALA D 313 ? 0.1803 0.2337 1.8096 -0.0170 0.0334  0.0438  313 ALA D N   
15252 C CA  . ALA D 313 ? 0.1686 0.2219 1.8011 -0.0168 0.0388  0.0400  313 ALA D CA  
15253 C C   . ALA D 313 ? 0.1964 0.2519 1.8168 -0.0188 0.0437  0.0392  313 ALA D C   
15254 O O   . ALA D 313 ? 0.1930 0.2489 1.8157 -0.0203 0.0477  0.0406  313 ALA D O   
15255 C CB  . ALA D 313 ? 0.1455 0.1981 1.7838 -0.0140 0.0398  0.0321  313 ALA D CB  
15256 N N   . MET D 314 ? 0.2372 0.2942 1.8463 -0.0188 0.0437  0.0363  314 MET D N   
15257 C CA  . MET D 314 ? 0.2586 0.3173 1.8568 -0.0199 0.0487  0.0335  314 MET D CA  
15258 C C   . MET D 314 ? 0.2843 0.3427 1.8733 -0.0233 0.0515  0.0399  314 MET D C   
15259 O O   . MET D 314 ? 0.2972 0.3575 1.8854 -0.0245 0.0580  0.0387  314 MET D O   
15260 C CB  . MET D 314 ? 0.2510 0.3098 1.8396 -0.0194 0.0478  0.0288  314 MET D CB  
15261 C CG  . MET D 314 ? 0.2490 0.3061 1.8426 -0.0167 0.0484  0.0221  314 MET D CG  
15262 S SD  . MET D 314 ? 0.2676 0.3245 1.8622 -0.0145 0.0531  0.0172  314 MET D SD  
15263 C CE  . MET D 314 ? 0.2610 0.3191 1.8414 -0.0160 0.0565  0.0150  314 MET D CE  
15264 N N   . ARG D 315 ? 0.2842 0.3397 1.8668 -0.0249 0.0465  0.0466  315 ARG D N   
15265 C CA  . ARG D 315 ? 0.2893 0.3416 1.8583 -0.0285 0.0489  0.0536  315 ARG D CA  
15266 C C   . ARG D 315 ? 0.2932 0.3449 1.8716 -0.0304 0.0549  0.0573  315 ARG D C   
15267 O O   . ARG D 315 ? 0.2944 0.3476 1.8682 -0.0330 0.0636  0.0567  315 ARG D O   
15268 C CB  . ARG D 315 ? 0.3055 0.3531 1.8672 -0.0288 0.0397  0.0605  315 ARG D CB  
15269 C CG  . ARG D 315 ? 0.3332 0.3740 1.8767 -0.0326 0.0409  0.0695  315 ARG D CG  
15270 C CD  . ARG D 315 ? 0.3439 0.3785 1.8835 -0.0319 0.0292  0.0774  315 ARG D CD  
15271 N NE  . ARG D 315 ? 0.3372 0.3713 1.8988 -0.0294 0.0255  0.0800  315 ARG D NE  
15272 C CZ  . ARG D 315 ? 0.3594 0.3886 1.9255 -0.0276 0.0153  0.0863  315 ARG D CZ  
15273 N NH1 . ARG D 315 ? 0.3683 0.3936 1.9193 -0.0275 0.0061  0.0903  315 ARG D NH1 
15274 N NH2 . ARG D 315 ? 0.3731 0.4009 1.9591 -0.0255 0.0136  0.0882  315 ARG D NH2 
15275 N N   . ASP D 316 ? 0.2743 0.3237 1.8675 -0.0292 0.0505  0.0605  316 ASP D N   
15276 C CA  . ASP D 316 ? 0.2521 0.3000 1.8581 -0.0310 0.0544  0.0636  316 ASP D CA  
15277 C C   . ASP D 316 ? 0.2625 0.3168 1.8769 -0.0312 0.0620  0.0563  316 ASP D C   
15278 O O   . ASP D 316 ? 0.2520 0.3071 1.8687 -0.0349 0.0695  0.0584  316 ASP D O   
15279 C CB  . ASP D 316 ? 0.2342 0.2795 1.8564 -0.0283 0.0476  0.0643  316 ASP D CB  
15280 C CG  . ASP D 316 ? 0.2528 0.2912 1.8728 -0.0280 0.0400  0.0729  316 ASP D CG  
15281 O OD1 . ASP D 316 ? 0.2735 0.3072 1.8767 -0.0305 0.0389  0.0804  316 ASP D OD1 
15282 O OD2 . ASP D 316 ? 0.2338 0.2706 1.8684 -0.0249 0.0345  0.0719  316 ASP D OD2 
15283 N N   . TYR D 317 ? 0.2689 0.3272 1.8877 -0.0274 0.0602  0.0475  317 TYR D N   
15284 C CA  . TYR D 317 ? 0.2669 0.3303 1.8959 -0.0263 0.0645  0.0404  317 TYR D CA  
15285 C C   . TYR D 317 ? 0.2772 0.3445 1.8983 -0.0285 0.0727  0.0390  317 TYR D C   
15286 O O   . TYR D 317 ? 0.2809 0.3531 1.9140 -0.0292 0.0781  0.0355  317 TYR D O   
15287 C CB  . TYR D 317 ? 0.2697 0.3336 1.9002 -0.0215 0.0601  0.0323  317 TYR D CB  
15288 C CG  . TYR D 317 ? 0.2745 0.3421 1.9146 -0.0192 0.0618  0.0250  317 TYR D CG  
15289 C CD1 . TYR D 317 ? 0.2650 0.3324 1.9205 -0.0181 0.0589  0.0224  317 TYR D CD1 
15290 C CD2 . TYR D 317 ? 0.2863 0.3571 1.9210 -0.0179 0.0654  0.0202  317 TYR D CD2 
15291 C CE1 . TYR D 317 ? 0.2668 0.3373 1.9318 -0.0157 0.0582  0.0155  317 TYR D CE1 
15292 C CE2 . TYR D 317 ? 0.2826 0.3566 1.9281 -0.0150 0.0653  0.0135  317 TYR D CE2 
15293 C CZ  . TYR D 317 ? 0.2911 0.3651 1.9517 -0.0139 0.0611  0.0114  317 TYR D CZ  
15294 O OH  . TYR D 317 ? 0.3334 0.4104 2.0059 -0.0107 0.0588  0.0046  317 TYR D OH  
15295 N N   . MET D 318 ? 0.2741 0.3396 1.8762 -0.0293 0.0733  0.0408  318 MET D N   
15296 C CA  . MET D 318 ? 0.2637 0.3318 1.8551 -0.0308 0.0811  0.0377  318 MET D CA  
15297 C C   . MET D 318 ? 0.2659 0.3333 1.8528 -0.0363 0.0904  0.0435  318 MET D C   
15298 O O   . MET D 318 ? 0.2666 0.3360 1.8444 -0.0380 0.0989  0.0408  318 MET D O   
15299 C CB  . MET D 318 ? 0.2679 0.3329 1.8391 -0.0302 0.0778  0.0368  318 MET D CB  
15300 C CG  . MET D 318 ? 0.2481 0.3144 1.8211 -0.0258 0.0740  0.0285  318 MET D CG  
15301 S SD  . MET D 318 ? 0.2598 0.3231 1.8112 -0.0262 0.0724  0.0255  318 MET D SD  
15302 C CE  . MET D 318 ? 0.2523 0.3109 1.7932 -0.0286 0.0639  0.0341  318 MET D CE  
15303 N N   . LYS D 319 ? 0.2750 0.3384 1.8673 -0.0393 0.0897  0.0515  319 LYS D N   
15304 C CA  . LYS D 319 ? 0.2867 0.3458 1.8694 -0.0453 0.0985  0.0592  319 LYS D CA  
15305 C C   . LYS D 319 ? 0.2809 0.3473 1.8809 -0.0480 0.1102  0.0549  319 LYS D C   
15306 O O   . LYS D 319 ? 0.2885 0.3535 1.8801 -0.0533 0.1218  0.0582  319 LYS D O   
15307 C CB  . LYS D 319 ? 0.2989 0.3494 1.8822 -0.0478 0.0939  0.0699  319 LYS D CB  
15308 C CG  . LYS D 319 ? 0.3094 0.3518 1.8751 -0.0463 0.0831  0.0762  319 LYS D CG  
15309 C CD  . LYS D 319 ? 0.3389 0.3694 1.8869 -0.0510 0.0840  0.0887  319 LYS D CD  
15310 C CE  . LYS D 319 ? 0.3620 0.3866 1.8806 -0.0511 0.0796  0.0915  319 LYS D CE  
15311 N NZ  . LYS D 319 ? 0.3974 0.4117 1.8928 -0.0572 0.0879  0.1005  319 LYS D NZ  
15312 N N   . GLY D 320 ? 0.2616 0.3353 1.8857 -0.0443 0.1069  0.0476  320 GLY D N   
15313 C CA  . GLY D 320 ? 0.2685 0.3513 1.9140 -0.0455 0.1154  0.0413  320 GLY D CA  
15314 C C   . GLY D 320 ? 0.2579 0.3475 1.9201 -0.0389 0.1082  0.0309  320 GLY D C   
15315 O O   . GLY D 320 ? 0.2546 0.3425 1.9267 -0.0360 0.0985  0.0301  320 GLY D O   
15316 N N   . LEU D 321 ? 0.2483 0.3443 1.9123 -0.0364 0.1130  0.0231  321 LEU D N   
15317 C CA  . LEU D 321 ? 0.2277 0.3278 1.9039 -0.0297 0.1053  0.0140  321 LEU D CA  
15318 C C   . LEU D 321 ? 0.2263 0.3366 1.9312 -0.0293 0.1094  0.0072  321 LEU D C   
15319 O O   . LEU D 321 ? 0.2282 0.3449 1.9411 -0.0331 0.1217  0.0059  321 LEU D O   
15320 C CB  . LEU D 321 ? 0.2432 0.3413 1.9005 -0.0266 0.1059  0.0104  321 LEU D CB  
15321 C CG  . LEU D 321 ? 0.2609 0.3501 1.8928 -0.0272 0.1010  0.0162  321 LEU D CG  
15322 C CD1 . LEU D 321 ? 0.2713 0.3592 1.8860 -0.0258 0.1041  0.0121  321 LEU D CD1 
15323 C CD2 . LEU D 321 ? 0.2637 0.3484 1.8969 -0.0233 0.0889  0.0161  321 LEU D CD2 
15324 N N   . ILE D 322 ? 0.2045 0.3159 1.9252 -0.0248 0.0987  0.0023  322 ILE D N   
15325 C CA  . ILE D 322 ? 0.1820 0.3028 1.9315 -0.0227 0.0977  -0.0056 322 ILE D CA  
15326 C C   . ILE D 322 ? 0.1708 0.2929 1.9193 -0.0151 0.0926  -0.0137 322 ILE D C   
15327 O O   . ILE D 322 ? 0.1548 0.2694 1.8934 -0.0099 0.0811  -0.0150 322 ILE D O   
15328 C CB  . ILE D 322 ? 0.1777 0.2966 1.9419 -0.0221 0.0871  -0.0060 322 ILE D CB  
15329 C CG1 . ILE D 322 ? 0.1817 0.2961 1.9439 -0.0290 0.0906  0.0029  322 ILE D CG1 
15330 C CG2 . ILE D 322 ? 0.1826 0.3118 1.9791 -0.0202 0.0843  -0.0146 322 ILE D CG2 
15331 C CD1 . ILE D 322 ? 0.1737 0.2817 1.9399 -0.0274 0.0788  0.0031  322 ILE D CD1 
15332 N N   . ILE D 323 ? 0.1734 0.3038 1.9320 -0.0145 0.1017  -0.0192 323 ILE D N   
15333 C CA  . ILE D 323 ? 0.1756 0.3073 1.9384 -0.0068 0.0965  -0.0276 323 ILE D CA  
15334 C C   . ILE D 323 ? 0.1686 0.3080 1.9632 -0.0025 0.0882  -0.0351 323 ILE D C   
15335 O O   . ILE D 323 ? 0.1565 0.2924 1.9525 0.0052  0.0767  -0.0403 323 ILE D O   
15336 C CB  . ILE D 323 ? 0.1909 0.3270 1.9499 -0.0071 0.1095  -0.0313 323 ILE D CB  
15337 C CG1 . ILE D 323 ? 0.2007 0.3276 1.9259 -0.0098 0.1143  -0.0257 323 ILE D CG1 
15338 C CG2 . ILE D 323 ? 0.2014 0.3401 1.9733 0.0015  0.1040  -0.0410 323 ILE D CG2 
15339 C CD1 . ILE D 323 ? 0.2207 0.3463 1.9342 -0.0185 0.1239  -0.0169 323 ILE D CD1 
15340 N N   . SER D 324 ? 0.1715 0.3211 1.9919 -0.0076 0.0942  -0.0357 324 SER D N   
15341 C CA  . SER D 324 ? 0.1620 0.3208 2.0169 -0.0047 0.0863  -0.0433 324 SER D CA  
15342 C C   . SER D 324 ? 0.1497 0.3125 2.0212 -0.0125 0.0896  -0.0397 324 SER D C   
15343 O O   . SER D 324 ? 0.1559 0.3202 2.0231 -0.0205 0.1043  -0.0337 324 SER D O   
15344 C CB  . SER D 324 ? 0.1695 0.3415 2.0510 -0.0015 0.0932  -0.0527 324 SER D CB  
15345 O OG  . SER D 324 ? 0.1801 0.3473 2.0482 0.0063  0.0894  -0.0567 324 SER D OG  
15346 N N   . PRO D 325 ? 0.1263 0.2899 2.0163 -0.0109 0.0763  -0.0431 325 PRO D N   
15347 C CA  . PRO D 325 ? 0.1229 0.2818 2.0137 -0.0018 0.0575  -0.0494 325 PRO D CA  
15348 C C   . PRO D 325 ? 0.1233 0.2655 1.9767 0.0021  0.0488  -0.0444 325 PRO D C   
15349 O O   . PRO D 325 ? 0.1208 0.2554 1.9534 -0.0026 0.0533  -0.0365 325 PRO D O   
15350 C CB  . PRO D 325 ? 0.1158 0.2782 2.0316 -0.0037 0.0479  -0.0528 325 PRO D CB  
15351 C CG  . PRO D 325 ? 0.1166 0.2770 2.0274 -0.0132 0.0589  -0.0445 325 PRO D CG  
15352 C CD  . PRO D 325 ? 0.1214 0.2892 2.0325 -0.0182 0.0786  -0.0414 325 PRO D CD  
15353 N N   . LYS D 326 ? 0.1240 0.2605 1.9710 0.0108  0.0364  -0.0494 326 LYS D N   
15354 C CA  . LYS D 326 ? 0.1294 0.2496 1.9422 0.0146  0.0289  -0.0457 326 LYS D CA  
15355 C C   . LYS D 326 ? 0.1322 0.2436 1.9408 0.0155  0.0155  -0.0460 326 LYS D C   
15356 O O   . LYS D 326 ? 0.1221 0.2384 1.9537 0.0174  0.0060  -0.0522 326 LYS D O   
15357 C CB  . LYS D 326 ? 0.1379 0.2542 1.9442 0.0228  0.0236  -0.0502 326 LYS D CB  
15358 C CG  . LYS D 326 ? 0.1400 0.2627 1.9454 0.0216  0.0381  -0.0499 326 LYS D CG  
15359 C CD  . LYS D 326 ? 0.1540 0.2734 1.9582 0.0298  0.0335  -0.0554 326 LYS D CD  
15360 C CE  . LYS D 326 ? 0.1674 0.2894 1.9636 0.0285  0.0476  -0.0553 326 LYS D CE  
15361 N NZ  . LYS D 326 ? 0.1724 0.3087 1.9849 0.0216  0.0640  -0.0554 326 LYS D NZ  
15362 N N   . ASN D 327 ? 0.1395 0.2386 1.9201 0.0138  0.0156  -0.0399 327 ASN D N   
15363 C CA  . ASN D 327 ? 0.1416 0.2297 1.9123 0.0150  0.0043  -0.0406 327 ASN D CA  
15364 C C   . ASN D 327 ? 0.1510 0.2297 1.9137 0.0232  -0.0105 -0.0463 327 ASN D C   
15365 O O   . ASN D 327 ? 0.1544 0.2293 1.9068 0.0281  -0.0113 -0.0469 327 ASN D O   
15366 C CB  . ASN D 327 ? 0.1472 0.2244 1.8906 0.0122  0.0087  -0.0339 327 ASN D CB  
15367 C CG  . ASN D 327 ? 0.1631 0.2303 1.8999 0.0123  -0.0002 -0.0353 327 ASN D CG  
15368 O OD1 . ASN D 327 ? 0.1608 0.2324 1.9163 0.0092  -0.0026 -0.0374 327 ASN D OD1 
15369 N ND2 . ASN D 327 ? 0.1714 0.2244 1.8812 0.0154  -0.0041 -0.0345 327 ASN D ND2 
15370 N N   . LYS D 328 ? 0.1552 0.2294 1.9231 0.0247  -0.0228 -0.0508 328 LYS D N   
15371 C CA  . LYS D 328 ? 0.1710 0.2356 1.9327 0.0325  -0.0394 -0.0566 328 LYS D CA  
15372 C C   . LYS D 328 ? 0.1606 0.2360 1.9476 0.0376  -0.0442 -0.0622 328 LYS D C   
15373 O O   . LYS D 328 ? 0.1745 0.2401 1.9513 0.0453  -0.0566 -0.0652 328 LYS D O   
15374 C CB  . LYS D 328 ? 0.1824 0.2278 1.9053 0.0362  -0.0417 -0.0530 328 LYS D CB  
15375 C CG  . LYS D 328 ? 0.1952 0.2302 1.8962 0.0319  -0.0376 -0.0491 328 LYS D CG  
15376 C CD  . LYS D 328 ? 0.2057 0.2390 1.9148 0.0299  -0.0454 -0.0532 328 LYS D CD  
15377 C CE  . LYS D 328 ? 0.2082 0.2337 1.9008 0.0253  -0.0385 -0.0496 328 LYS D CE  
15378 N NZ  . LYS D 328 ? 0.2263 0.2335 1.8835 0.0281  -0.0396 -0.0481 328 LYS D NZ  
15379 N N   . SER D 329 ? 0.1385 0.2331 1.9588 0.0336  -0.0350 -0.0640 329 SER D N   
15380 C CA  . SER D 329 ? 0.1357 0.2427 1.9859 0.0383  -0.0387 -0.0708 329 SER D CA  
15381 C C   . SER D 329 ? 0.1403 0.2536 2.0198 0.0402  -0.0538 -0.0791 329 SER D C   
15382 O O   . SER D 329 ? 0.1475 0.2589 2.0292 0.0358  -0.0578 -0.0796 329 SER D O   
15383 C CB  . SER D 329 ? 0.1223 0.2462 1.9935 0.0336  -0.0202 -0.0699 329 SER D CB  
15384 O OG  . SER D 329 ? 0.1166 0.2529 2.0117 0.0252  -0.0116 -0.0696 329 SER D OG  
15385 N N   . ILE D 330 ? 0.1436 0.2643 2.0468 0.0472  -0.0630 -0.0863 330 ILE D N   
15386 C CA  . ILE D 330 ? 0.1494 0.2778 2.0849 0.0503  -0.0796 -0.0955 330 ILE D CA  
15387 C C   . ILE D 330 ? 0.1350 0.2878 2.1189 0.0484  -0.0702 -0.1015 330 ILE D C   
15388 O O   . ILE D 330 ? 0.1196 0.2787 2.1088 0.0510  -0.0600 -0.1014 330 ILE D O   
15389 C CB  . ILE D 330 ? 0.1704 0.2825 2.0882 0.0614  -0.1024 -0.0989 330 ILE D CB  
15390 C CG1 . ILE D 330 ? 0.1848 0.2728 2.0548 0.0609  -0.1084 -0.0932 330 ILE D CG1 
15391 C CG2 . ILE D 330 ? 0.1777 0.2990 2.1324 0.0663  -0.1221 -0.1095 330 ILE D CG2 
15392 C CD1 . ILE D 330 ? 0.2122 0.2810 2.0611 0.0702  -0.1324 -0.0965 330 ILE D CD1 
15393 N N   . HIS D 331 ? 0.1329 0.2991 2.1519 0.0431  -0.0721 -0.1069 331 HIS D N   
15394 C CA  . HIS D 331 ? 0.1240 0.3140 2.1902 0.0385  -0.0590 -0.1120 331 HIS D CA  
15395 C C   . HIS D 331 ? 0.1410 0.3425 2.2504 0.0407  -0.0766 -0.1232 331 HIS D C   
15396 O O   . HIS D 331 ? 0.1492 0.3453 2.2577 0.0374  -0.0873 -0.1246 331 HIS D O   
15397 C CB  . HIS D 331 ? 0.1075 0.3031 2.1730 0.0260  -0.0360 -0.1048 331 HIS D CB  
15398 C CG  . HIS D 331 ? 0.1036 0.2906 2.1321 0.0237  -0.0190 -0.0947 331 HIS D CG  
15399 N ND1 . HIS D 331 ? 0.1028 0.3001 2.1390 0.0221  -0.0005 -0.0938 331 HIS D ND1 
15400 C CD2 . HIS D 331 ? 0.1033 0.2729 2.0883 0.0226  -0.0177 -0.0859 331 HIS D CD2 
15401 C CE1 . HIS D 331 ? 0.0992 0.2851 2.0968 0.0201  0.0101  -0.0847 331 HIS D CE1 
15402 N NE2 . HIS D 331 ? 0.1011 0.2711 2.0692 0.0203  0.0001  -0.0798 331 HIS D NE2 
15403 N N   . THR D 332 ? 0.1461 0.3642 2.2953 0.0461  -0.0786 -0.1319 332 THR D N   
15404 C CA  . THR D 332 ? 0.1594 0.3899 2.3538 0.0497  -0.0976 -0.1439 332 THR D CA  
15405 C C   . THR D 332 ? 0.1664 0.4241 2.4168 0.0414  -0.0802 -0.1500 332 THR D C   
15406 O O   . THR D 332 ? 0.1560 0.4301 2.4556 0.0443  -0.0915 -0.1614 332 THR D O   
15407 C CB  . THR D 332 ? 0.1668 0.3931 2.3640 0.0640  -0.1181 -0.1498 332 THR D CB  
15408 O OG1 . THR D 332 ? 0.1584 0.3940 2.3630 0.0650  -0.0984 -0.1485 332 THR D OG1 
15409 C CG2 . THR D 332 ? 0.1821 0.3797 2.3235 0.0716  -0.1354 -0.1437 332 THR D CG2 
15410 N N   . ASN D 333 ? 0.1804 0.4416 2.4223 0.0306  -0.0529 -0.1420 333 ASN D N   
15411 C CA  . ASN D 333 ? 0.1858 0.4698 2.4739 0.0211  -0.0319 -0.1459 333 ASN D CA  
15412 C C   . ASN D 333 ? 0.1858 0.4649 2.4566 0.0074  -0.0130 -0.1359 333 ASN D C   
15413 O O   . ASN D 333 ? 0.1867 0.4473 2.4078 0.0059  -0.0086 -0.1248 333 ASN D O   
15414 C CB  . ASN D 333 ? 0.2029 0.4990 2.5057 0.0252  -0.0167 -0.1489 333 ASN D CB  
15415 C CG  . ASN D 333 ? 0.2177 0.5371 2.5668 0.0155  0.0077  -0.1534 333 ASN D CG  
15416 O OD1 . ASN D 333 ? 0.2280 0.5455 2.5610 0.0044  0.0310  -0.1447 333 ASN D OD1 
15417 N ND2 . ASN D 333 ? 0.2185 0.5591 2.6240 0.0194  0.0032  -0.1666 333 ASN D ND2 
15418 N N   . THR D 334 ? 0.1724 0.4680 2.4872 -0.0024 -0.0027 -0.1403 334 THR D N   
15419 C CA  . THR D 334 ? 0.1769 0.4673 2.4824 -0.0155 0.0117  -0.1318 334 THR D CA  
15420 C C   . THR D 334 ? 0.1930 0.4820 2.4760 -0.0225 0.0410  -0.1214 334 THR D C   
15421 O O   . THR D 334 ? 0.2065 0.4873 2.4721 -0.0325 0.0539  -0.1117 334 THR D O   
15422 C CB  . THR D 334 ? 0.1705 0.4770 2.5304 -0.0242 0.0125  -0.1398 334 THR D CB  
15423 O OG1 . THR D 334 ? 0.1622 0.4896 2.5619 -0.0298 0.0351  -0.1438 334 THR D OG1 
15424 C CG2 . THR D 334 ? 0.1708 0.4817 2.5596 -0.0168 -0.0174 -0.1525 334 THR D CG2 
15425 N N   . LYS D 335 ? 0.2004 0.4964 2.4835 -0.0172 0.0508  -0.1235 335 LYS D N   
15426 C CA  . LYS D 335 ? 0.2053 0.4972 2.4597 -0.0225 0.0760  -0.1141 335 LYS D CA  
15427 C C   . LYS D 335 ? 0.1943 0.4681 2.3964 -0.0138 0.0680  -0.1076 335 LYS D C   
15428 O O   . LYS D 335 ? 0.1969 0.4697 2.3985 -0.0023 0.0523  -0.1138 335 LYS D O   
15429 C CB  . LYS D 335 ? 0.2184 0.5287 2.5031 -0.0240 0.0971  -0.1203 335 LYS D CB  
15430 C CG  . LYS D 335 ? 0.2287 0.5596 2.5702 -0.0332 0.1091  -0.1278 335 LYS D CG  
15431 C CD  . LYS D 335 ? 0.2417 0.5698 2.5812 -0.0487 0.1295  -0.1187 335 LYS D CD  
15432 C CE  . LYS D 335 ? 0.2618 0.6095 2.6639 -0.0551 0.1304  -0.1290 335 LYS D CE  
15433 N NZ  . LYS D 335 ? 0.2782 0.6266 2.6914 -0.0710 0.1517  -0.1225 335 LYS D NZ  
15434 N N   . ILE D 336 ? 0.1988 0.4584 2.3592 -0.0198 0.0796  -0.0952 336 ILE D N   
15435 C CA  . ILE D 336 ? 0.1909 0.4321 2.3002 -0.0141 0.0737  -0.0876 336 ILE D CA  
15436 C C   . ILE D 336 ? 0.2020 0.4420 2.2885 -0.0182 0.0964  -0.0812 336 ILE D C   
15437 O O   . ILE D 336 ? 0.2162 0.4551 2.2967 -0.0286 0.1133  -0.0737 336 ILE D O   
15438 C CB  . ILE D 336 ? 0.1823 0.4070 2.2631 -0.0175 0.0648  -0.0790 336 ILE D CB  
15439 C CG1 . ILE D 336 ? 0.1722 0.3971 2.2741 -0.0148 0.0436  -0.0858 336 ILE D CG1 
15440 C CG2 . ILE D 336 ? 0.1949 0.4018 2.2254 -0.0122 0.0604  -0.0715 336 ILE D CG2 
15441 C CD1 . ILE D 336 ? 0.1747 0.3920 2.2647 -0.0024 0.0207  -0.0915 336 ILE D CD1 
15442 N N   . PRO D 337 ? 0.2048 0.4435 2.2772 -0.0106 0.0975  -0.0839 337 PRO D N   
15443 C CA  . PRO D 337 ? 0.2063 0.4413 2.2515 -0.0142 0.1173  -0.0782 337 PRO D CA  
15444 C C   . PRO D 337 ? 0.1987 0.4159 2.1988 -0.0188 0.1177  -0.0652 337 PRO D C   
15445 O O   . PRO D 337 ? 0.1994 0.4049 2.1803 -0.0143 0.1005  -0.0624 337 PRO D O   
15446 C CB  . PRO D 337 ? 0.2140 0.4482 2.2524 -0.0033 0.1120  -0.0847 337 PRO D CB  
15447 C CG  . PRO D 337 ? 0.2079 0.4504 2.2822 0.0055  0.0927  -0.0953 337 PRO D CG  
15448 C CD  . PRO D 337 ? 0.2063 0.4464 2.2889 0.0018  0.0795  -0.0929 337 PRO D CD  
15449 N N   . LEU D 338 ? 0.1995 0.4148 2.1839 -0.0278 0.1374  -0.0577 338 LEU D N   
15450 C CA  . LEU D 338 ? 0.1974 0.3967 2.1416 -0.0324 0.1387  -0.0452 338 LEU D CA  
15451 C C   . LEU D 338 ? 0.2069 0.4011 2.1200 -0.0331 0.1522  -0.0418 338 LEU D C   
15452 O O   . LEU D 338 ? 0.2228 0.4239 2.1432 -0.0387 0.1713  -0.0428 338 LEU D O   
15453 C CB  . LEU D 338 ? 0.2070 0.4056 2.1589 -0.0433 0.1480  -0.0378 338 LEU D CB  
15454 C CG  . LEU D 338 ? 0.2224 0.4045 2.1346 -0.0486 0.1511  -0.0242 338 LEU D CG  
15455 C CD1 . LEU D 338 ? 0.2107 0.3816 2.1100 -0.0448 0.1318  -0.0205 338 LEU D CD1 
15456 C CD2 . LEU D 338 ? 0.2315 0.4123 2.1468 -0.0605 0.1685  -0.0162 338 LEU D CD2 
15457 N N   . GLU D 339 ? 0.2030 0.3847 2.0819 -0.0278 0.1426  -0.0382 339 GLU D N   
15458 C CA  . GLU D 339 ? 0.2098 0.3843 2.0556 -0.0287 0.1526  -0.0345 339 GLU D CA  
15459 C C   . GLU D 339 ? 0.2165 0.3757 2.0264 -0.0312 0.1465  -0.0231 339 GLU D C   
15460 O O   . GLU D 339 ? 0.1988 0.3517 2.0035 -0.0268 0.1305  -0.0219 339 GLU D O   
15461 C CB  . GLU D 339 ? 0.2108 0.3854 2.0531 -0.0191 0.1458  -0.0427 339 GLU D CB  
15462 C CG  . GLU D 339 ? 0.2015 0.3902 2.0835 -0.0132 0.1439  -0.0549 339 GLU D CG  
15463 C CD  . GLU D 339 ? 0.1924 0.3776 2.0662 -0.0036 0.1372  -0.0616 339 GLU D CD  
15464 O OE1 . GLU D 339 ? 0.1786 0.3598 2.0567 0.0044  0.1191  -0.0646 339 GLU D OE1 
15465 O OE2 . GLU D 339 ? 0.1975 0.3819 2.0572 -0.0046 0.1504  -0.0632 339 GLU D OE2 
15466 N N   . LEU D 340 ? 0.2367 0.3898 2.0218 -0.0380 0.1592  -0.0154 340 LEU D N   
15467 C CA  . LEU D 340 ? 0.2495 0.3888 2.0030 -0.0407 0.1540  -0.0044 340 LEU D CA  
15468 C C   . LEU D 340 ? 0.2638 0.3957 1.9831 -0.0425 0.1623  -0.0010 340 LEU D C   
15469 O O   . LEU D 340 ? 0.2693 0.4054 1.9876 -0.0457 0.1777  -0.0041 340 LEU D O   
15470 C CB  . LEU D 340 ? 0.2585 0.3951 2.0180 -0.0489 0.1587  0.0044  340 LEU D CB  
15471 C CG  . LEU D 340 ? 0.2491 0.3896 2.0377 -0.0484 0.1487  0.0027  340 LEU D CG  
15472 C CD1 . LEU D 340 ? 0.2588 0.3942 2.0505 -0.0572 0.1550  0.0121  340 LEU D CD1 
15473 C CD2 . LEU D 340 ? 0.2370 0.3709 2.0177 -0.0413 0.1298  0.0021  340 LEU D CD2 
15474 N N   . TYR D 341 ? 0.2704 0.3912 1.9621 -0.0408 0.1523  0.0050  341 TYR D N   
15475 C CA  . TYR D 341 ? 0.2949 0.4068 1.9522 -0.0432 0.1571  0.0094  341 TYR D CA  
15476 C C   . TYR D 341 ? 0.3210 0.4221 1.9589 -0.0480 0.1529  0.0220  341 TYR D C   
15477 O O   . TYR D 341 ? 0.3316 0.4281 1.9683 -0.0451 0.1393  0.0253  341 TYR D O   
15478 C CB  . TYR D 341 ? 0.2796 0.3885 1.9226 -0.0365 0.1485  0.0038  341 TYR D CB  
15479 C CG  . TYR D 341 ? 0.3058 0.4092 1.9199 -0.0390 0.1571  0.0037  341 TYR D CG  
15480 C CD1 . TYR D 341 ? 0.3275 0.4365 1.9452 -0.0395 0.1711  -0.0041 341 TYR D CD1 
15481 C CD2 . TYR D 341 ? 0.3136 0.4061 1.8974 -0.0408 0.1512  0.0108  341 TYR D CD2 
15482 C CE1 . TYR D 341 ? 0.3570 0.4597 1.9461 -0.0420 0.1794  -0.0050 341 TYR D CE1 
15483 C CE2 . TYR D 341 ? 0.3360 0.4225 1.8916 -0.0432 0.1577  0.0102  341 TYR D CE2 
15484 C CZ  . TYR D 341 ? 0.3586 0.4497 1.9154 -0.0439 0.1721  0.0022  341 TYR D CZ  
15485 O OH  . TYR D 341 ? 0.3803 0.4644 1.9076 -0.0465 0.1793  0.0005  341 TYR D OH  
15486 N N   . ASN D 342 ? 0.3359 0.4317 1.9578 -0.0552 0.1650  0.0289  342 ASN D N   
15487 C CA  . ASN D 342 ? 0.3527 0.4375 1.9598 -0.0600 0.1617  0.0415  342 ASN D CA  
15488 C C   . ASN D 342 ? 0.3902 0.4634 1.9584 -0.0621 0.1624  0.0475  342 ASN D C   
15489 O O   . ASN D 342 ? 0.4051 0.4775 1.9582 -0.0654 0.1755  0.0453  342 ASN D O   
15490 C CB  . ASN D 342 ? 0.3732 0.4581 1.9927 -0.0678 0.1745  0.0470  342 ASN D CB  
15491 C CG  . ASN D 342 ? 0.3553 0.4512 2.0146 -0.0666 0.1728  0.0414  342 ASN D CG  
15492 O OD1 . ASN D 342 ? 0.3505 0.4557 2.0318 -0.0701 0.1856  0.0364  342 ASN D OD1 
15493 N ND2 . ASN D 342 ? 0.3462 0.4411 2.0154 -0.0618 0.1569  0.0415  342 ASN D ND2 
15494 N N   . ASP D 343 ? 0.4119 0.4760 1.9647 -0.0604 0.1485  0.0546  343 ASP D N   
15495 C CA  . ASP D 343 ? 0.4452 0.4969 1.9619 -0.0630 0.1468  0.0621  343 ASP D CA  
15496 C C   . ASP D 343 ? 0.4652 0.5072 1.9706 -0.0708 0.1562  0.0735  343 ASP D C   
15497 O O   . ASP D 343 ? 0.4490 0.4939 1.9771 -0.0738 0.1617  0.0760  343 ASP D O   
15498 C CB  . ASP D 343 ? 0.4437 0.4900 1.9504 -0.0585 0.1287  0.0651  343 ASP D CB  
15499 C CG  . ASP D 343 ? 0.4378 0.4770 1.9493 -0.0589 0.1187  0.0755  343 ASP D CG  
15500 O OD1 . ASP D 343 ? 0.4811 0.5107 1.9811 -0.0644 0.1236  0.0858  343 ASP D OD1 
15501 O OD2 . ASP D 343 ? 0.3814 0.4236 1.9072 -0.0539 0.1065  0.0734  343 ASP D OD2 
15502 N N   . LYS D 344 ? 0.5054 0.5343 1.9745 -0.0741 0.1569  0.0807  344 LYS D N   
15503 C CA  . LYS D 344 ? 0.5505 0.5679 2.0006 -0.0822 0.1697  0.0908  344 LYS D CA  
15504 C C   . LYS D 344 ? 0.5358 0.5449 1.9952 -0.0848 0.1643  0.1030  344 LYS D C   
15505 O O   . LYS D 344 ? 0.5596 0.5587 2.0086 -0.0923 0.1760  0.1122  344 LYS D O   
15506 C CB  . LYS D 344 ? 0.6167 0.6204 2.0214 -0.0842 0.1691  0.0948  344 LYS D CB  
15507 C CG  . LYS D 344 ? 0.6593 0.6524 2.0443 -0.0805 0.1481  0.1021  344 LYS D CG  
15508 C CD  . LYS D 344 ? 0.7316 0.7075 2.0691 -0.0839 0.1472  0.1089  344 LYS D CD  
15509 C CE  . LYS D 344 ? 0.7896 0.7507 2.1067 -0.0924 0.1611  0.1209  344 LYS D CE  
15510 N NZ  . LYS D 344 ? 0.8514 0.7918 2.1190 -0.0956 0.1574  0.1303  344 LYS D NZ  
15511 N N   . ASP D 345 ? 0.4931 0.5057 1.9726 -0.0791 0.1480  0.1029  345 ASP D N   
15512 C CA  . ASP D 345 ? 0.4917 0.4954 1.9798 -0.0804 0.1410  0.1137  345 ASP D CA  
15513 C C   . ASP D 345 ? 0.4667 0.4791 1.9923 -0.0824 0.1476  0.1107  345 ASP D C   
15514 O O   . ASP D 345 ? 0.4716 0.4759 2.0062 -0.0846 0.1442  0.1192  345 ASP D O   
15515 C CB  . ASP D 345 ? 0.4726 0.4746 1.9633 -0.0733 0.1205  0.1149  345 ASP D CB  
15516 C CG  . ASP D 345 ? 0.4843 0.4747 1.9403 -0.0721 0.1104  0.1210  345 ASP D CG  
15517 O OD1 . ASP D 345 ? 0.5151 0.4970 1.9410 -0.0769 0.1194  0.1247  345 ASP D OD1 
15518 O OD2 . ASP D 345 ? 0.4496 0.4395 1.9096 -0.0664 0.0939  0.1215  345 ASP D OD2 
15519 N N   . VAL D 346 ? 0.4341 0.4624 1.9823 -0.0810 0.1552  0.0982  346 VAL D N   
15520 C CA  . VAL D 346 ? 0.4117 0.4497 1.9968 -0.0828 0.1607  0.0936  346 VAL D CA  
15521 C C   . VAL D 346 ? 0.4368 0.4714 2.0201 -0.0923 0.1804  0.0984  346 VAL D C   
15522 O O   . VAL D 346 ? 0.4532 0.4907 2.0234 -0.0948 0.1934  0.0945  346 VAL D O   
15523 C CB  . VAL D 346 ? 0.3781 0.4336 1.9890 -0.0769 0.1590  0.0785  346 VAL D CB  
15524 C CG1 . VAL D 346 ? 0.3610 0.4267 2.0099 -0.0790 0.1642  0.0732  346 VAL D CG1 
15525 C CG2 . VAL D 346 ? 0.3713 0.4284 1.9834 -0.0683 0.1410  0.0744  346 VAL D CG2 
15526 N N   . LYS D 347 ? 0.4634 0.4905 2.0587 -0.0978 0.1829  0.1068  347 LYS D N   
15527 C CA  . LYS D 347 ? 0.4941 0.5160 2.0890 -0.1082 0.2026  0.1127  347 LYS D CA  
15528 C C   . LYS D 347 ? 0.4751 0.5101 2.1153 -0.1114 0.2094  0.1057  347 LYS D C   
15529 O O   . LYS D 347 ? 0.5000 0.5368 2.1492 -0.1198 0.2283  0.1062  347 LYS D O   
15530 C CB  . LYS D 347 ? 0.5270 0.5257 2.0934 -0.1136 0.2018  0.1302  347 LYS D CB  
15531 C CG  . LYS D 347 ? 0.5688 0.5535 2.0877 -0.1122 0.1974  0.1376  347 LYS D CG  
15532 C CD  . LYS D 347 ? 0.5954 0.5844 2.0932 -0.1146 0.2126  0.1314  347 LYS D CD  
15533 C CE  . LYS D 347 ? 0.6353 0.6089 2.0841 -0.1140 0.2081  0.1382  347 LYS D CE  
15534 N NZ  . LYS D 347 ? 0.6654 0.6428 2.0966 -0.1175 0.2261  0.1312  347 LYS D NZ  
15535 N N   . LYS D 348 ? 0.4432 0.4870 2.1116 -0.1049 0.1945  0.0986  348 LYS D N   
15536 C CA  . LYS D 348 ? 0.4273 0.4845 2.1392 -0.1068 0.1977  0.0899  348 LYS D CA  
15537 C C   . LYS D 348 ? 0.4003 0.4690 2.1321 -0.0968 0.1802  0.0784  348 LYS D C   
15538 O O   . LYS D 348 ? 0.4051 0.4675 2.1212 -0.0902 0.1652  0.0804  348 LYS D O   
15539 C CB  . LYS D 348 ? 0.4318 0.4779 2.1568 -0.1145 0.2004  0.0994  348 LYS D CB  
15540 C CG  . LYS D 348 ? 0.4136 0.4717 2.1850 -0.1166 0.2003  0.0906  348 LYS D CG  
15541 C CD  . LYS D 348 ? 0.4431 0.4898 2.2272 -0.1268 0.2085  0.1001  348 LYS D CD  
15542 C CE  . LYS D 348 ? 0.4458 0.4750 2.2194 -0.1248 0.1941  0.1099  348 LYS D CE  
15543 N NZ  . LYS D 348 ? 0.4590 0.4774 2.2506 -0.1337 0.1996  0.1171  348 LYS D NZ  
15544 N N   . VAL D 349 ? 0.3818 0.4668 2.1484 -0.0959 0.1824  0.0662  349 VAL D N   
15545 C CA  . VAL D 349 ? 0.3545 0.4489 2.1406 -0.0872 0.1663  0.0553  349 VAL D CA  
15546 C C   . VAL D 349 ? 0.3544 0.4572 2.1816 -0.0905 0.1660  0.0490  349 VAL D C   
15547 O O   . VAL D 349 ? 0.4038 0.5147 2.2522 -0.0972 0.1804  0.0464  349 VAL D O   
15548 C CB  . VAL D 349 ? 0.3424 0.4490 2.1269 -0.0803 0.1657  0.0444  349 VAL D CB  
15549 C CG1 . VAL D 349 ? 0.3151 0.4297 2.1191 -0.0716 0.1493  0.0335  349 VAL D CG1 
15550 C CG2 . VAL D 349 ? 0.3476 0.4461 2.0927 -0.0775 0.1656  0.0494  349 VAL D CG2 
15551 N N   . VAL D 350 ? 0.3201 0.4211 2.1588 -0.0857 0.1498  0.0455  350 VAL D N   
15552 C CA  . VAL D 350 ? 0.2985 0.4052 2.1742 -0.0885 0.1463  0.0393  350 VAL D CA  
15553 C C   . VAL D 350 ? 0.2782 0.3912 2.1641 -0.0789 0.1286  0.0277  350 VAL D C   
15554 O O   . VAL D 350 ? 0.2822 0.3891 2.1447 -0.0717 0.1180  0.0284  350 VAL D O   
15555 C CB  . VAL D 350 ? 0.3031 0.3947 2.1783 -0.0943 0.1451  0.0493  350 VAL D CB  
15556 C CG1 . VAL D 350 ? 0.2909 0.3864 2.2031 -0.0966 0.1385  0.0419  350 VAL D CG1 
15557 C CG2 . VAL D 350 ? 0.3253 0.4071 2.1858 -0.1039 0.1623  0.0624  350 VAL D CG2 
15558 N N   . VAL D 351 ? 0.2745 0.3993 2.1954 -0.0790 0.1253  0.0170  351 VAL D N   
15559 C CA  . VAL D 351 ? 0.2695 0.3988 2.2000 -0.0704 0.1077  0.0058  351 VAL D CA  
15560 C C   . VAL D 351 ? 0.2769 0.4053 2.2362 -0.0741 0.1006  0.0017  351 VAL D C   
15561 O O   . VAL D 351 ? 0.3049 0.4408 2.2935 -0.0818 0.1099  0.0001  351 VAL D O   
15562 C CB  . VAL D 351 ? 0.2622 0.4072 2.2082 -0.0655 0.1075  -0.0052 351 VAL D CB  
15563 C CG1 . VAL D 351 ? 0.2458 0.3938 2.2028 -0.0569 0.0881  -0.0165 351 VAL D CG1 
15564 C CG2 . VAL D 351 ? 0.2669 0.4119 2.1849 -0.0620 0.1150  -0.0019 351 VAL D CG2 
15565 N N   . LYS D 352 ? 0.2602 0.3796 2.2118 -0.0689 0.0850  -0.0008 352 LYS D N   
15566 C CA  . LYS D 352 ? 0.2568 0.3737 2.2332 -0.0720 0.0769  -0.0059 352 LYS D CA  
15567 C C   . LYS D 352 ? 0.2304 0.3514 2.2151 -0.0638 0.0590  -0.0192 352 LYS D C   
15568 O O   . LYS D 352 ? 0.2251 0.3450 2.1876 -0.0555 0.0520  -0.0214 352 LYS D O   
15569 C CB  . LYS D 352 ? 0.2839 0.3835 2.2437 -0.0743 0.0759  0.0035  352 LYS D CB  
15570 C CG  . LYS D 352 ? 0.3257 0.4199 2.2809 -0.0833 0.0926  0.0167  352 LYS D CG  
15571 C CD  . LYS D 352 ? 0.3685 0.4443 2.3055 -0.0843 0.0903  0.0270  352 LYS D CD  
15572 C CE  . LYS D 352 ? 0.4066 0.4738 2.3354 -0.0929 0.1052  0.0413  352 LYS D CE  
15573 N NZ  . LYS D 352 ? 0.4195 0.4685 2.3351 -0.0933 0.1010  0.0507  352 LYS D NZ  
15574 N N   . PHE D 353 ? 0.2106 0.3358 2.2273 -0.0667 0.0517  -0.0279 353 PHE D N   
15575 C CA  . PHE D 353 ? 0.1974 0.3230 2.2196 -0.0595 0.0325  -0.0402 353 PHE D CA  
15576 C C   . PHE D 353 ? 0.1990 0.3165 2.2376 -0.0639 0.0250  -0.0439 353 PHE D C   
15577 O O   . PHE D 353 ? 0.2176 0.3388 2.2839 -0.0729 0.0331  -0.0425 353 PHE D O   
15578 C CB  . PHE D 353 ? 0.1902 0.3324 2.2377 -0.0560 0.0270  -0.0512 353 PHE D CB  
15579 C CG  . PHE D 353 ? 0.1821 0.3209 2.2292 -0.0480 0.0049  -0.0629 353 PHE D CG  
15580 C CD1 . PHE D 353 ? 0.1819 0.3097 2.1925 -0.0389 -0.0046 -0.0628 353 PHE D CD1 
15581 C CD2 . PHE D 353 ? 0.1826 0.3269 2.2634 -0.0501 -0.0064 -0.0738 353 PHE D CD2 
15582 C CE1 . PHE D 353 ? 0.1888 0.3104 2.1941 -0.0321 -0.0242 -0.0728 353 PHE D CE1 
15583 C CE2 . PHE D 353 ? 0.1904 0.3289 2.2662 -0.0428 -0.0277 -0.0843 353 PHE D CE2 
15584 C CZ  . PHE D 353 ? 0.1913 0.3179 2.2278 -0.0338 -0.0363 -0.0835 353 PHE D CZ  
15585 N N   . ARG D 354 ? 0.2023 0.3077 2.2223 -0.0577 0.0106  -0.0485 354 ARG D N   
15586 C CA  . ARG D 354 ? 0.2170 0.3111 2.2447 -0.0607 0.0032  -0.0521 354 ARG D CA  
15587 C C   . ARG D 354 ? 0.2278 0.3166 2.2655 -0.0704 0.0174  -0.0414 354 ARG D C   
15588 O O   . ARG D 354 ? 0.2712 0.3585 2.3356 -0.0771 0.0164  -0.0449 354 ARG D O   
15589 C CB  . ARG D 354 ? 0.2291 0.3305 2.2851 -0.0598 -0.0119 -0.0669 354 ARG D CB  
15590 C CG  . ARG D 354 ? 0.2409 0.3390 2.2764 -0.0492 -0.0292 -0.0762 354 ARG D CG  
15591 C CD  . ARG D 354 ? 0.2604 0.3647 2.3248 -0.0485 -0.0460 -0.0908 354 ARG D CD  
15592 N NE  . ARG D 354 ? 0.2752 0.3758 2.3203 -0.0384 -0.0638 -0.0995 354 ARG D NE  
15593 C CZ  . ARG D 354 ? 0.2909 0.4021 2.3569 -0.0348 -0.0768 -0.1095 354 ARG D CZ  
15594 N NH1 . ARG D 354 ? 0.3076 0.4362 2.4169 -0.0407 -0.0725 -0.1125 354 ARG D NH1 
15595 N NH2 . ARG D 354 ? 0.3077 0.4119 2.3521 -0.0255 -0.0941 -0.1163 354 ARG D NH2 
15596 N N   . ASP D 355 ? 0.2268 0.3118 2.2423 -0.0714 0.0303  -0.0283 355 ASP D N   
15597 C CA  . ASP D 355 ? 0.2299 0.3051 2.2447 -0.0789 0.0423  -0.0161 355 ASP D CA  
15598 C C   . ASP D 355 ? 0.2357 0.3196 2.2766 -0.0892 0.0570  -0.0114 355 ASP D C   
15599 O O   . ASP D 355 ? 0.2529 0.3267 2.2938 -0.0963 0.0667  -0.0010 355 ASP D O   
15600 C CB  . ASP D 355 ? 0.2495 0.3094 2.2666 -0.0797 0.0344  -0.0178 355 ASP D CB  
15601 C CG  . ASP D 355 ? 0.2706 0.3212 2.2579 -0.0698 0.0238  -0.0209 355 ASP D CG  
15602 O OD1 . ASP D 355 ? 0.2538 0.2974 2.2148 -0.0670 0.0289  -0.0110 355 ASP D OD1 
15603 O OD2 . ASP D 355 ? 0.3265 0.3783 2.3164 -0.0650 0.0107  -0.0335 355 ASP D OD2 
15604 N N   . LYS D 356 ? 0.2331 0.3344 2.2950 -0.0900 0.0594  -0.0186 356 LYS D N   
15605 C CA  . LYS D 356 ? 0.2409 0.3518 2.3272 -0.0999 0.0763  -0.0146 356 LYS D CA  
15606 C C   . LYS D 356 ? 0.2405 0.3612 2.3111 -0.0977 0.0880  -0.0102 356 LYS D C   
15607 O O   . LYS D 356 ? 0.2203 0.3482 2.2796 -0.0887 0.0800  -0.0165 356 LYS D O   
15608 C CB  . LYS D 356 ? 0.2475 0.3726 2.3786 -0.1031 0.0702  -0.0285 356 LYS D CB  
15609 C CG  . LYS D 356 ? 0.2675 0.4033 2.4315 -0.1148 0.0885  -0.0262 356 LYS D CG  
15610 C CD  . LYS D 356 ? 0.2674 0.4257 2.4706 -0.1146 0.0867  -0.0398 356 LYS D CD  
15611 C CE  . LYS D 356 ? 0.2785 0.4452 2.5302 -0.1260 0.0930  -0.0451 356 LYS D CE  
15612 N NZ  . LYS D 356 ? 0.2887 0.4576 2.5657 -0.1230 0.0711  -0.0596 356 LYS D NZ  
15613 N N   . VAL D 357 ? 0.2570 0.3767 2.3260 -0.1064 0.1075  0.0006  357 VAL D N   
15614 C CA  . VAL D 357 ? 0.2735 0.4022 2.3296 -0.1058 0.1210  0.0040  357 VAL D CA  
15615 C C   . VAL D 357 ? 0.2787 0.4290 2.3689 -0.1046 0.1214  -0.0094 357 VAL D C   
15616 O O   . VAL D 357 ? 0.2852 0.4442 2.4153 -0.1104 0.1215  -0.0169 357 VAL D O   
15617 C CB  . VAL D 357 ? 0.2960 0.4175 2.3432 -0.1165 0.1427  0.0179  357 VAL D CB  
15618 C CG1 . VAL D 357 ? 0.3059 0.4368 2.3396 -0.1161 0.1573  0.0196  357 VAL D CG1 
15619 C CG2 . VAL D 357 ? 0.2971 0.3964 2.3116 -0.1176 0.1420  0.0322  357 VAL D CG2 
15620 N N   . ILE D 358 ? 0.2855 0.4443 2.3616 -0.0972 0.1217  -0.0126 358 ILE D N   
15621 C CA  . ILE D 358 ? 0.2921 0.4713 2.3990 -0.0953 0.1240  -0.0243 358 ILE D CA  
15622 C C   . ILE D 358 ? 0.3020 0.4866 2.3935 -0.0962 0.1424  -0.0198 358 ILE D C   
15623 O O   . ILE D 358 ? 0.3289 0.5303 2.4479 -0.0969 0.1507  -0.0279 358 ILE D O   
15624 C CB  . ILE D 358 ? 0.2852 0.4694 2.3943 -0.0831 0.1016  -0.0363 358 ILE D CB  
15625 C CG1 . ILE D 358 ? 0.2987 0.4750 2.3648 -0.0738 0.0970  -0.0321 358 ILE D CG1 
15626 C CG2 . ILE D 358 ? 0.2899 0.4667 2.4090 -0.0820 0.0831  -0.0414 358 ILE D CG2 
15627 C CD1 . ILE D 358 ? 0.3105 0.4898 2.3753 -0.0621 0.0768  -0.0427 358 ILE D CD1 
15628 N N   . TYR D 359 ? 0.3041 0.4745 2.3519 -0.0955 0.1480  -0.0079 359 TYR D N   
15629 C CA  . TYR D 359 ? 0.3038 0.4760 2.3319 -0.0975 0.1661  -0.0026 359 TYR D CA  
15630 C C   . TYR D 359 ? 0.3174 0.4705 2.3069 -0.1029 0.1747  0.0135  359 TYR D C   
15631 O O   . TYR D 359 ? 0.3179 0.4573 2.2840 -0.0989 0.1617  0.0192  359 TYR D O   
15632 C CB  . TYR D 359 ? 0.2961 0.4733 2.3076 -0.0858 0.1566  -0.0092 359 TYR D CB  
15633 C CG  . TYR D 359 ? 0.3047 0.4840 2.2956 -0.0866 0.1736  -0.0061 359 TYR D CG  
15634 C CD1 . TYR D 359 ? 0.3235 0.4880 2.2694 -0.0866 0.1773  0.0051  359 TYR D CD1 
15635 C CD2 . TYR D 359 ? 0.2892 0.4853 2.3065 -0.0873 0.1856  -0.0153 359 TYR D CD2 
15636 C CE1 . TYR D 359 ? 0.3378 0.5030 2.2626 -0.0874 0.1921  0.0071  359 TYR D CE1 
15637 C CE2 . TYR D 359 ? 0.3100 0.5071 2.3074 -0.0880 0.2018  -0.0136 359 TYR D CE2 
15638 C CZ  . TYR D 359 ? 0.3249 0.5060 2.2745 -0.0882 0.2049  -0.0024 359 TYR D CZ  
15639 O OH  . TYR D 359 ? 0.3221 0.5029 2.2497 -0.0891 0.2202  -0.0014 359 TYR D OH  
15640 N N   . SER D 360 ? 0.3267 0.4785 2.3099 -0.1119 0.1965  0.0207  360 SER D N   
15641 C CA  . SER D 360 ? 0.3416 0.4741 2.2844 -0.1166 0.2046  0.0365  360 SER D CA  
15642 C C   . SER D 360 ? 0.3594 0.4932 2.2856 -0.1221 0.2269  0.0403  360 SER D C   
15643 O O   . SER D 360 ? 0.3625 0.5002 2.3082 -0.1323 0.2459  0.0412  360 SER D O   
15644 C CB  . SER D 360 ? 0.3467 0.4658 2.2959 -0.1254 0.2067  0.0461  360 SER D CB  
15645 O OG  . SER D 360 ? 0.3644 0.4656 2.2774 -0.1316 0.2187  0.0617  360 SER D OG  
15646 N N   . LYS D 361 ? 0.3460 0.4755 2.2355 -0.1157 0.2249  0.0423  361 LYS D N   
15647 C CA  . LYS D 361 ? 0.3672 0.4949 2.2330 -0.1200 0.2445  0.0457  361 LYS D CA  
15648 C C   . LYS D 361 ? 0.3764 0.4821 2.1928 -0.1217 0.2440  0.0612  361 LYS D C   
15649 O O   . LYS D 361 ? 0.3791 0.4762 2.1777 -0.1150 0.2258  0.0648  361 LYS D O   
15650 C CB  . LYS D 361 ? 0.3627 0.5037 2.2271 -0.1117 0.2442  0.0340  361 LYS D CB  
15651 C CG  . LYS D 361 ? 0.3978 0.5377 2.2397 -0.1164 0.2662  0.0356  361 LYS D CG  
15652 C CD  . LYS D 361 ? 0.3972 0.5490 2.2380 -0.1079 0.2662  0.0234  361 LYS D CD  
15653 C CE  . LYS D 361 ? 0.4169 0.5681 2.2378 -0.1127 0.2893  0.0228  361 LYS D CE  
15654 N NZ  . LYS D 361 ? 0.4196 0.5854 2.2779 -0.1199 0.3105  0.0153  361 LYS D NZ  
15655 N N   . ASN D 362 ? 0.4030 0.4996 2.1984 -0.1309 0.2642  0.0697  362 ASN D N   
15656 C CA  . ASN D 362 ? 0.4354 0.5111 2.1803 -0.1327 0.2655  0.0836  362 ASN D CA  
15657 C C   . ASN D 362 ? 0.4471 0.5267 2.1660 -0.1284 0.2712  0.0780  362 ASN D C   
15658 O O   . ASN D 362 ? 0.4502 0.5392 2.1785 -0.1328 0.2904  0.0716  362 ASN D O   
15659 C CB  . ASN D 362 ? 0.4806 0.5412 2.2124 -0.1457 0.2852  0.0965  362 ASN D CB  
15660 C CG  . ASN D 362 ? 0.4896 0.5399 2.2378 -0.1506 0.2791  0.1052  362 ASN D CG  
15661 O OD1 . ASN D 362 ? 0.4725 0.5352 2.2651 -0.1518 0.2769  0.0974  362 ASN D OD1 
15662 N ND2 . ASN D 362 ? 0.5343 0.5610 2.2473 -0.1534 0.2757  0.1213  362 ASN D ND2 
15663 N N   . ILE D 363 ? 0.4521 0.5245 2.1400 -0.1202 0.2552  0.0802  363 ILE D N   
15664 C CA  . ILE D 363 ? 0.4584 0.5353 2.1252 -0.1146 0.2564  0.0729  363 ILE D CA  
15665 C C   . ILE D 363 ? 0.5214 0.5818 2.1423 -0.1210 0.2700  0.0825  363 ILE D C   
15666 O O   . ILE D 363 ? 0.5518 0.5945 2.1384 -0.1208 0.2601  0.0943  363 ILE D O   
15667 C CB  . ILE D 363 ? 0.4310 0.5074 2.0875 -0.1036 0.2327  0.0704  363 ILE D CB  
15668 C CG1 . ILE D 363 ? 0.3983 0.4868 2.0935 -0.0974 0.2179  0.0624  363 ILE D CG1 
15669 C CG2 . ILE D 363 ? 0.4278 0.5081 2.0635 -0.0981 0.2337  0.0624  363 ILE D CG2 
15670 C CD1 . ILE D 363 ? 0.3856 0.4939 2.1155 -0.0941 0.2227  0.0472  363 ILE D CD1 
15671 N N   . THR D 364 ? 0.5581 0.6243 2.1777 -0.1259 0.2918  0.0766  364 THR D N   
15672 C CA  . THR D 364 ? 0.6156 0.6655 2.1884 -0.1320 0.3063  0.0842  364 THR D CA  
15673 C C   . THR D 364 ? 0.5991 0.6473 2.1404 -0.1242 0.2974  0.0786  364 THR D C   
15674 O O   . THR D 364 ? 0.6109 0.6407 2.1059 -0.1257 0.2944  0.0880  364 THR D O   
15675 C CB  . THR D 364 ? 0.6563 0.7123 2.2404 -0.1413 0.3357  0.0796  364 THR D CB  
15676 O OG1 . THR D 364 ? 0.6438 0.7231 2.2639 -0.1346 0.3371  0.0618  364 THR D OG1 
15677 C CG2 . THR D 364 ? 0.6800 0.7326 2.2867 -0.1516 0.3471  0.0879  364 THR D CG2 
15678 N N   . SER D 365 ? 0.5570 0.6233 2.1228 -0.1162 0.2933  0.0634  365 SER D N   
15679 C CA  . SER D 365 ? 0.5542 0.6191 2.0932 -0.1095 0.2870  0.0567  365 SER D CA  
15680 C C   . SER D 365 ? 0.5076 0.5777 2.0569 -0.0988 0.2613  0.0529  365 SER D C   
15681 O O   . SER D 365 ? 0.4682 0.5504 2.0552 -0.0945 0.2522  0.0479  365 SER D O   
15682 C CB  . SER D 365 ? 0.5520 0.6298 2.1036 -0.1094 0.3055  0.0425  365 SER D CB  
15683 O OG  . SER D 365 ? 0.5175 0.6159 2.1201 -0.1038 0.3017  0.0309  365 SER D OG  
15684 N N   . GLU D 366 ? 0.5060 0.5661 2.0206 -0.0947 0.2494  0.0548  366 GLU D N   
15685 C CA  . GLU D 366 ? 0.4832 0.5475 2.0065 -0.0855 0.2274  0.0511  366 GLU D CA  
15686 C C   . GLU D 366 ? 0.4592 0.5377 2.0015 -0.0786 0.2282  0.0354  366 GLU D C   
15687 O O   . GLU D 366 ? 0.4716 0.5549 2.0135 -0.0805 0.2448  0.0275  366 GLU D O   
15688 C CB  . GLU D 366 ? 0.5206 0.5698 2.0034 -0.0840 0.2141  0.0583  366 GLU D CB  
15689 C CG  . GLU D 366 ? 0.5567 0.6017 2.0086 -0.0840 0.2217  0.0519  366 GLU D CG  
15690 C CD  . GLU D 366 ? 0.5761 0.6080 1.9920 -0.0819 0.2059  0.0571  366 GLU D CD  
15691 O OE1 . GLU D 366 ? 0.5726 0.6082 1.9989 -0.0753 0.1880  0.0549  366 GLU D OE1 
15692 O OE2 . GLU D 366 ? 0.6202 0.6378 1.9978 -0.0872 0.2120  0.0633  366 GLU D OE2 
15693 N N   . GLY D 367 ? 0.4203 0.5043 1.9783 -0.0706 0.2103  0.0311  367 GLY D N   
15694 C CA  . GLY D 367 ? 0.4067 0.5008 1.9797 -0.0631 0.2072  0.0178  367 GLY D CA  
15695 C C   . GLY D 367 ? 0.3939 0.5033 2.0117 -0.0601 0.2089  0.0097  367 GLY D C   
15696 O O   . GLY D 367 ? 0.3983 0.5104 2.0372 -0.0604 0.2016  0.0137  367 GLY D O   
15697 N N   . TYR D 368 ? 0.3790 0.4982 2.0119 -0.0564 0.2169  -0.0025 368 TYR D N   
15698 C CA  . TYR D 368 ? 0.3368 0.4702 2.0118 -0.0511 0.2134  -0.0116 368 TYR D CA  
15699 C C   . TYR D 368 ? 0.3435 0.4853 2.0443 -0.0580 0.2280  -0.0107 368 TYR D C   
15700 O O   . TYR D 368 ? 0.3694 0.5090 2.0572 -0.0650 0.2465  -0.0091 368 TYR D O   
15701 C CB  . TYR D 368 ? 0.3213 0.4621 2.0071 -0.0442 0.2163  -0.0251 368 TYR D CB  
15702 C CG  . TYR D 368 ? 0.2866 0.4417 2.0171 -0.0383 0.2115  -0.0343 368 TYR D CG  
15703 C CD1 . TYR D 368 ? 0.2563 0.4108 1.9970 -0.0310 0.1913  -0.0352 368 TYR D CD1 
15704 C CD2 . TYR D 368 ? 0.2805 0.4494 2.0429 -0.0401 0.2268  -0.0424 368 TYR D CD2 
15705 C CE1 . TYR D 368 ? 0.2383 0.4039 2.0167 -0.0251 0.1846  -0.0434 368 TYR D CE1 
15706 C CE2 . TYR D 368 ? 0.2548 0.4370 2.0598 -0.0341 0.2200  -0.0512 368 TYR D CE2 
15707 C CZ  . TYR D 368 ? 0.2365 0.4164 2.0481 -0.0263 0.1978  -0.0515 368 TYR D CZ  
15708 O OH  . TYR D 368 ? 0.2067 0.3975 2.0566 -0.0199 0.1883  -0.0597 368 TYR D OH  
15709 N N   . MET D 369 ? 0.3426 0.4931 2.0783 -0.0562 0.2196  -0.0123 369 MET D N   
15710 C CA  . MET D 369 ? 0.3581 0.5180 2.1256 -0.0627 0.2313  -0.0125 369 MET D CA  
15711 C C   . MET D 369 ? 0.3314 0.5053 2.1422 -0.0559 0.2196  -0.0224 369 MET D C   
15712 O O   . MET D 369 ? 0.3162 0.4866 2.1250 -0.0487 0.1999  -0.0227 369 MET D O   
15713 C CB  . MET D 369 ? 0.4067 0.5560 2.1618 -0.0706 0.2306  0.0013  369 MET D CB  
15714 C CG  . MET D 369 ? 0.4774 0.6342 2.2650 -0.0785 0.2418  0.0025  369 MET D CG  
15715 S SD  . MET D 369 ? 0.5228 0.6843 2.3451 -0.0759 0.2224  0.0022  369 MET D SD  
15716 C CE  . MET D 369 ? 0.4933 0.6349 2.2734 -0.0740 0.2059  0.0151  369 MET D CE  
15717 N N   . ALA D 370 ? 0.3243 0.5134 2.1733 -0.0579 0.2316  -0.0309 370 ALA D N   
15718 C CA  . ALA D 370 ? 0.2950 0.4981 2.1876 -0.0512 0.2201  -0.0413 370 ALA D CA  
15719 C C   . ALA D 370 ? 0.2949 0.5093 2.2267 -0.0586 0.2284  -0.0423 370 ALA D C   
15720 O O   . ALA D 370 ? 0.3204 0.5364 2.2534 -0.0682 0.2497  -0.0394 370 ALA D O   
15721 C CB  . ALA D 370 ? 0.2844 0.4971 2.1911 -0.0434 0.2233  -0.0541 370 ALA D CB  
15722 N N   . ASP D 371 ? 0.2718 0.4931 2.2351 -0.0546 0.2116  -0.0468 371 ASP D N   
15723 C CA  . ASP D 371 ? 0.2598 0.4913 2.2623 -0.0617 0.2163  -0.0481 371 ASP D CA  
15724 C C   . ASP D 371 ? 0.2512 0.4910 2.2873 -0.0537 0.1938  -0.0568 371 ASP D C   
15725 O O   . ASP D 371 ? 0.2620 0.4995 2.2901 -0.0430 0.1774  -0.0615 371 ASP D O   
15726 C CB  . ASP D 371 ? 0.2566 0.4746 2.2378 -0.0716 0.2205  -0.0342 371 ASP D CB  
15727 C CG  . ASP D 371 ? 0.2603 0.4845 2.2680 -0.0837 0.2393  -0.0322 371 ASP D CG  
15728 O OD1 . ASP D 371 ? 0.2633 0.5056 2.3169 -0.0843 0.2448  -0.0433 371 ASP D OD1 
15729 O OD2 . ASP D 371 ? 0.2586 0.4691 2.2412 -0.0926 0.2482  -0.0195 371 ASP D OD2 
15730 N N   . GLU D 372 ? 0.2427 0.4908 2.3152 -0.0594 0.1929  -0.0588 372 GLU D N   
15731 C CA  . GLU D 372 ? 0.2227 0.4773 2.3258 -0.0529 0.1706  -0.0669 372 GLU D CA  
15732 C C   . GLU D 372 ? 0.2192 0.4652 2.3219 -0.0587 0.1616  -0.0600 372 GLU D C   
15733 O O   . GLU D 372 ? 0.2362 0.4794 2.3395 -0.0698 0.1767  -0.0527 372 GLU D O   
15734 C CB  . GLU D 372 ? 0.2194 0.4959 2.3802 -0.0540 0.1757  -0.0796 372 GLU D CB  
15735 C CG  . GLU D 372 ? 0.2258 0.5143 2.4012 -0.0457 0.1796  -0.0904 372 GLU D CG  
15736 C CD  . GLU D 372 ? 0.2192 0.5309 2.4566 -0.0466 0.1839  -0.1037 372 GLU D CD  
15737 O OE1 . GLU D 372 ? 0.2111 0.5298 2.4779 -0.0563 0.1901  -0.1035 372 GLU D OE1 
15738 O OE2 . GLU D 372 ? 0.2252 0.5470 2.4812 -0.0371 0.1802  -0.1144 372 GLU D OE2 
15739 N N   . LEU D 373 ? 0.2020 0.4435 2.3054 -0.0513 0.1373  -0.0632 373 LEU D N   
15740 C CA  . LEU D 373 ? 0.1985 0.4339 2.3095 -0.0555 0.1266  -0.0605 373 LEU D CA  
15741 C C   . LEU D 373 ? 0.1893 0.4413 2.3539 -0.0554 0.1184  -0.0730 373 LEU D C   
15742 O O   . LEU D 373 ? 0.1772 0.4419 2.3651 -0.0481 0.1130  -0.0836 373 LEU D O   
15743 C CB  . LEU D 373 ? 0.1919 0.4107 2.2677 -0.0478 0.1060  -0.0569 373 LEU D CB  
15744 C CG  . LEU D 373 ? 0.1941 0.3964 2.2199 -0.0483 0.1117  -0.0445 373 LEU D CG  
15745 C CD1 . LEU D 373 ? 0.1819 0.3706 2.1784 -0.0397 0.0921  -0.0435 373 LEU D CD1 
15746 C CD2 . LEU D 373 ? 0.2037 0.3982 2.2221 -0.0595 0.1242  -0.0336 373 LEU D CD2 
15747 N N   . THR D 374 ? 0.1938 0.4450 2.3785 -0.0631 0.1160  -0.0722 374 THR D N   
15748 C CA  . THR D 374 ? 0.2034 0.4675 2.4351 -0.0616 0.1014  -0.0847 374 THR D CA  
15749 C C   . THR D 374 ? 0.2121 0.4630 2.4344 -0.0607 0.0809  -0.0839 374 THR D C   
15750 O O   . THR D 374 ? 0.2325 0.4750 2.4523 -0.0699 0.0868  -0.0770 374 THR D O   
15751 C CB  . THR D 374 ? 0.2126 0.4939 2.4931 -0.0726 0.1194  -0.0891 374 THR D CB  
15752 O OG1 . THR D 374 ? 0.2260 0.5181 2.5116 -0.0738 0.1409  -0.0899 374 THR D OG1 
15753 C CG2 . THR D 374 ? 0.2125 0.5109 2.5470 -0.0697 0.1035  -0.1044 374 THR D CG2 
15754 N N   . ILE D 375 ? 0.2026 0.4515 2.4219 -0.0495 0.0568  -0.0918 375 ILE D N   
15755 C CA  . ILE D 375 ? 0.1971 0.4349 2.4107 -0.0469 0.0348  -0.0947 375 ILE D CA  
15756 C C   . ILE D 375 ? 0.1895 0.4419 2.4536 -0.0461 0.0199  -0.1090 375 ILE D C   
15757 O O   . ILE D 375 ? 0.1858 0.4555 2.4821 -0.0428 0.0209  -0.1174 375 ILE D O   
15758 C CB  . ILE D 375 ? 0.2040 0.4272 2.3745 -0.0351 0.0185  -0.0934 375 ILE D CB  
15759 C CG1 . ILE D 375 ? 0.2070 0.4400 2.3897 -0.0245 0.0082  -0.1026 375 ILE D CG1 
15760 C CG2 . ILE D 375 ? 0.2136 0.4234 2.3375 -0.0364 0.0325  -0.0800 375 ILE D CG2 
15761 C CD1 . ILE D 375 ? 0.2213 0.4382 2.3641 -0.0131 -0.0101 -0.1021 375 ILE D CD1 
15762 N N   . ASP D 376 ? 0.1874 0.4324 2.4580 -0.0485 0.0052  -0.1125 376 ASP D N   
15763 C CA  . ASP D 376 ? 0.1902 0.4470 2.5067 -0.0480 -0.0122 -0.1266 376 ASP D CA  
15764 C C   . ASP D 376 ? 0.2007 0.4421 2.4936 -0.0393 -0.0404 -0.1318 376 ASP D C   
15765 O O   . ASP D 376 ? 0.2192 0.4553 2.5232 -0.0435 -0.0511 -0.1363 376 ASP D O   
15766 C CB  . ASP D 376 ? 0.1953 0.4594 2.5512 -0.0615 -0.0021 -0.1281 376 ASP D CB  
15767 C CG  . ASP D 376 ? 0.1963 0.4760 2.6081 -0.0625 -0.0182 -0.1438 376 ASP D CG  
15768 O OD1 . ASP D 376 ? 0.2000 0.4881 2.6251 -0.0521 -0.0367 -0.1542 376 ASP D OD1 
15769 O OD2 . ASP D 376 ? 0.1836 0.4667 2.6263 -0.0736 -0.0130 -0.1458 376 ASP D OD2 
15770 N N   . PRO D 377 ? 0.2007 0.4342 2.4624 -0.0271 -0.0537 -0.1324 377 PRO D N   
15771 C CA  . PRO D 377 ? 0.2148 0.4297 2.4443 -0.0194 -0.0779 -0.1354 377 PRO D CA  
15772 C C   . PRO D 377 ? 0.2303 0.4502 2.4915 -0.0157 -0.1037 -0.1501 377 PRO D C   
15773 O O   . PRO D 377 ? 0.2195 0.4580 2.5225 -0.0132 -0.1088 -0.1590 377 PRO D O   
15774 C CB  . PRO D 377 ? 0.2104 0.4191 2.4056 -0.0085 -0.0803 -0.1316 377 PRO D CB  
15775 C CG  . PRO D 377 ? 0.2042 0.4353 2.4399 -0.0073 -0.0724 -0.1366 377 PRO D CG  
15776 C CD  . PRO D 377 ? 0.1918 0.4337 2.4501 -0.0205 -0.0463 -0.1311 377 PRO D CD  
15777 N N   . VAL D 378 ? 0.2453 0.4480 2.4848 -0.0146 -0.1210 -0.1533 378 VAL D N   
15778 C CA  . VAL D 378 ? 0.2501 0.4538 2.5116 -0.0103 -0.1486 -0.1675 378 VAL D CA  
15779 C C   . VAL D 378 ? 0.2697 0.4585 2.4938 0.0034  -0.1712 -0.1701 378 VAL D C   
15780 O O   . VAL D 378 ? 0.2827 0.4510 2.4537 0.0073  -0.1703 -0.1623 378 VAL D O   
15781 C CB  . VAL D 378 ? 0.2553 0.4479 2.5167 -0.0174 -0.1557 -0.1714 378 VAL D CB  
15782 C CG1 . VAL D 378 ? 0.2691 0.4592 2.5446 -0.0119 -0.1870 -0.1865 378 VAL D CG1 
15783 C CG2 . VAL D 378 ? 0.2504 0.4561 2.5512 -0.0313 -0.1348 -0.1689 378 VAL D CG2 
15784 N N   . GLY D 379 ? 0.2794 0.4777 2.5327 0.0104  -0.1930 -0.1817 379 GLY D N   
15785 C CA  . GLY D 379 ? 0.2802 0.4628 2.4999 0.0235  -0.2171 -0.1846 379 GLY D CA  
15786 C C   . GLY D 379 ? 0.2570 0.4318 2.4375 0.0289  -0.2032 -0.1728 379 GLY D C   
15787 O O   . GLY D 379 ? 0.2399 0.4315 2.4435 0.0281  -0.1864 -0.1695 379 GLY D O   
15788 N N   . ILE D 380 ? 0.2604 0.4096 2.3832 0.0340  -0.2097 -0.1673 380 ILE D N   
15789 C CA  . ILE D 380 ? 0.2483 0.3870 2.3288 0.0356  -0.1921 -0.1546 380 ILE D CA  
15790 C C   . ILE D 380 ? 0.2511 0.3790 2.3061 0.0268  -0.1767 -0.1474 380 ILE D C   
15791 O O   . ILE D 380 ? 0.2687 0.3844 2.3127 0.0252  -0.1888 -0.1524 380 ILE D O   
15792 C CB  . ILE D 380 ? 0.2553 0.3725 2.2901 0.0473  -0.2091 -0.1532 380 ILE D CB  
15793 C CG1 . ILE D 380 ? 0.2562 0.3820 2.3153 0.0571  -0.2261 -0.1597 380 ILE D CG1 
15794 C CG2 . ILE D 380 ? 0.2510 0.3563 2.2419 0.0475  -0.1903 -0.1403 380 ILE D CG2 
15795 C CD1 . ILE D 380 ? 0.2840 0.3856 2.3030 0.0683  -0.2519 -0.1617 380 ILE D CD1 
15796 N N   . GLU D 381 ? 0.2474 0.3791 2.2935 0.0215  -0.1514 -0.1365 381 GLU D N   
15797 C CA  . GLU D 381 ? 0.2519 0.3757 2.2812 0.0129  -0.1363 -0.1295 381 GLU D CA  
15798 C C   . GLU D 381 ? 0.2274 0.3451 2.2226 0.0130  -0.1173 -0.1169 381 GLU D C   
15799 O O   . GLU D 381 ? 0.2131 0.3439 2.2216 0.0128  -0.1045 -0.1128 381 GLU D O   
15800 C CB  . GLU D 381 ? 0.2602 0.4013 2.3344 0.0019  -0.1234 -0.1305 381 GLU D CB  
15801 C CG  . GLU D 381 ? 0.2735 0.4054 2.3372 -0.0067 -0.1127 -0.1254 381 GLU D CG  
15802 C CD  . GLU D 381 ? 0.2985 0.4462 2.4046 -0.0180 -0.0967 -0.1239 381 GLU D CD  
15803 O OE1 . GLU D 381 ? 0.2910 0.4490 2.4028 -0.0211 -0.0773 -0.1157 381 GLU D OE1 
15804 O OE2 . GLU D 381 ? 0.3358 0.4847 2.4679 -0.0242 -0.1026 -0.1305 381 GLU D OE2 
15805 N N   . ASP D 382 ? 0.2178 0.3159 2.1705 0.0134  -0.1160 -0.1119 382 ASP D N   
15806 C CA  . ASP D 382 ? 0.1956 0.2880 2.1180 0.0126  -0.0986 -0.1004 382 ASP D CA  
15807 C C   . ASP D 382 ? 0.1790 0.2803 2.1189 0.0027  -0.0795 -0.0940 382 ASP D C   
15808 O O   . ASP D 382 ? 0.1848 0.2866 2.1426 -0.0029 -0.0817 -0.0976 382 ASP D O   
15809 C CB  . ASP D 382 ? 0.2038 0.2738 2.0795 0.0156  -0.1019 -0.0976 382 ASP D CB  
15810 C CG  . ASP D 382 ? 0.2106 0.2700 2.0826 0.0123  -0.1090 -0.1027 382 ASP D CG  
15811 O OD1 . ASP D 382 ? 0.2144 0.2746 2.1035 0.0142  -0.1266 -0.1130 382 ASP D OD1 
15812 O OD2 . ASP D 382 ? 0.1878 0.2388 2.0420 0.0082  -0.0975 -0.0969 382 ASP D OD2 
15813 N N   . MET D 383 ? 0.1695 0.2762 2.1026 0.0005  -0.0618 -0.0847 383 MET D N   
15814 C CA  . MET D 383 ? 0.1673 0.2809 2.1140 -0.0088 -0.0439 -0.0774 383 MET D CA  
15815 C C   . MET D 383 ? 0.1674 0.2735 2.0814 -0.0093 -0.0300 -0.0662 383 MET D C   
15816 O O   . MET D 383 ? 0.1571 0.2653 2.0576 -0.0054 -0.0253 -0.0631 383 MET D O   
15817 C CB  . MET D 383 ? 0.1659 0.2997 2.1521 -0.0129 -0.0349 -0.0791 383 MET D CB  
15818 C CG  . MET D 383 ? 0.1788 0.3227 2.2027 -0.0120 -0.0494 -0.0912 383 MET D CG  
15819 S SD  . MET D 383 ? 0.1754 0.3445 2.2509 -0.0178 -0.0364 -0.0942 383 MET D SD  
15820 C CE  . MET D 383 ? 0.1673 0.3363 2.2472 -0.0310 -0.0136 -0.0836 383 MET D CE  
15821 N N   . GLU D 384 ? 0.1704 0.2678 2.0737 -0.0142 -0.0240 -0.0606 384 GLU D N   
15822 C CA  . GLU D 384 ? 0.1682 0.2612 2.0481 -0.0160 -0.0103 -0.0497 384 GLU D CA  
15823 C C   . GLU D 384 ? 0.1651 0.2686 2.0649 -0.0240 0.0053  -0.0429 384 GLU D C   
15824 O O   . GLU D 384 ? 0.1695 0.2729 2.0863 -0.0305 0.0086  -0.0414 384 GLU D O   
15825 C CB  . GLU D 384 ? 0.1738 0.2519 2.0318 -0.0163 -0.0114 -0.0466 384 GLU D CB  
15826 C CG  . GLU D 384 ? 0.1701 0.2444 2.0068 -0.0178 0.0010  -0.0357 384 GLU D CG  
15827 C CD  . GLU D 384 ? 0.1771 0.2375 1.9960 -0.0173 -0.0008 -0.0340 384 GLU D CD  
15828 O OE1 . GLU D 384 ? 0.1848 0.2389 2.0109 -0.0175 -0.0089 -0.0404 384 GLU D OE1 
15829 O OE2 . GLU D 384 ? 0.1771 0.2331 1.9759 -0.0165 0.0058  -0.0271 384 GLU D OE2 
15830 N N   . LEU D 385 ? 0.1776 0.2894 2.0747 -0.0236 0.0150  -0.0391 385 LEU D N   
15831 C CA  . LEU D 385 ? 0.1781 0.2990 2.0894 -0.0310 0.0313  -0.0329 385 LEU D CA  
15832 C C   . LEU D 385 ? 0.1641 0.2754 2.0496 -0.0341 0.0407  -0.0213 385 LEU D C   
15833 O O   . LEU D 385 ? 0.1641 0.2695 2.0223 -0.0294 0.0398  -0.0184 385 LEU D O   
15834 C CB  . LEU D 385 ? 0.1929 0.3252 2.1089 -0.0279 0.0365  -0.0355 385 LEU D CB  
15835 C CG  . LEU D 385 ? 0.2093 0.3573 2.1648 -0.0294 0.0366  -0.0441 385 LEU D CG  
15836 C CD1 . LEU D 385 ? 0.2244 0.3729 2.2008 -0.0267 0.0191  -0.0542 385 LEU D CD1 
15837 C CD2 . LEU D 385 ? 0.2101 0.3667 2.1654 -0.0240 0.0399  -0.0474 385 LEU D CD2 
15838 N N   . ALA D 386 ? 0.1565 0.2659 2.0513 -0.0419 0.0492  -0.0147 386 ALA D N   
15839 C CA  . ALA D 386 ? 0.1494 0.2472 2.0205 -0.0438 0.0538  -0.0041 386 ALA D CA  
15840 C C   . ALA D 386 ? 0.1576 0.2581 2.0219 -0.0493 0.0693  0.0056  386 ALA D C   
15841 O O   . ALA D 386 ? 0.1675 0.2695 2.0475 -0.0571 0.0786  0.0098  386 ALA D O   
15842 C CB  . ALA D 386 ? 0.1422 0.2308 2.0225 -0.0473 0.0496  -0.0029 386 ALA D CB  
15843 N N   . PHE D 387 ? 0.1588 0.2582 1.9977 -0.0457 0.0721  0.0090  387 PHE D N   
15844 C CA  . PHE D 387 ? 0.1809 0.2816 2.0080 -0.0502 0.0858  0.0173  387 PHE D CA  
15845 C C   . PHE D 387 ? 0.2021 0.2900 2.0095 -0.0531 0.0876  0.0289  387 PHE D C   
15846 O O   . PHE D 387 ? 0.2060 0.2859 2.0009 -0.0488 0.0784  0.0298  387 PHE D O   
15847 C CB  . PHE D 387 ? 0.1883 0.2933 1.9977 -0.0451 0.0873  0.0147  387 PHE D CB  
15848 C CG  . PHE D 387 ? 0.1905 0.3083 2.0207 -0.0425 0.0877  0.0044  387 PHE D CG  
15849 C CD1 . PHE D 387 ? 0.1863 0.3066 2.0302 -0.0367 0.0745  -0.0052 387 PHE D CD1 
15850 C CD2 . PHE D 387 ? 0.2063 0.3330 2.0425 -0.0459 0.1012  0.0041  387 PHE D CD2 
15851 C CE1 . PHE D 387 ? 0.2006 0.3324 2.0653 -0.0337 0.0731  -0.0145 387 PHE D CE1 
15852 C CE2 . PHE D 387 ? 0.2113 0.3506 2.0703 -0.0429 0.1014  -0.0060 387 PHE D CE2 
15853 C CZ  . PHE D 387 ? 0.2084 0.3504 2.0826 -0.0365 0.0865  -0.0151 387 PHE D CZ  
15854 N N   . GLU D 388 ? 0.2241 0.3101 2.0287 -0.0604 0.1000  0.0376  388 GLU D N   
15855 C CA  . GLU D 388 ? 0.2419 0.3147 2.0303 -0.0640 0.1018  0.0498  388 GLU D CA  
15856 C C   . GLU D 388 ? 0.2615 0.3322 2.0292 -0.0685 0.1143  0.0584  388 GLU D C   
15857 O O   . GLU D 388 ? 0.2885 0.3629 2.0664 -0.0754 0.1271  0.0600  388 GLU D O   
15858 C CB  . GLU D 388 ? 0.2480 0.3161 2.0591 -0.0702 0.1033  0.0524  388 GLU D CB  
15859 C CG  . GLU D 388 ? 0.2429 0.3089 2.0705 -0.0663 0.0902  0.0449  388 GLU D CG  
15860 C CD  . GLU D 388 ? 0.2705 0.3301 2.1202 -0.0731 0.0919  0.0478  388 GLU D CD  
15861 O OE1 . GLU D 388 ? 0.2889 0.3441 2.1392 -0.0811 0.1036  0.0571  388 GLU D OE1 
15862 O OE2 . GLU D 388 ? 0.2692 0.3272 2.1353 -0.0710 0.0821  0.0404  388 GLU D OE2 
15863 N N   . PHE D 389 ? 0.2627 0.3271 2.0015 -0.0651 0.1110  0.0636  389 PHE D N   
15864 C CA  . PHE D 389 ? 0.2822 0.3427 1.9963 -0.0689 0.1211  0.0713  389 PHE D CA  
15865 C C   . PHE D 389 ? 0.3117 0.3562 2.0086 -0.0731 0.1212  0.0854  389 PHE D C   
15866 O O   . PHE D 389 ? 0.3024 0.3391 1.9902 -0.0688 0.1096  0.0892  389 PHE D O   
15867 C CB  . PHE D 389 ? 0.2674 0.3305 1.9596 -0.0627 0.1165  0.0677  389 PHE D CB  
15868 C CG  . PHE D 389 ? 0.2472 0.3235 1.9529 -0.0579 0.1157  0.0547  389 PHE D CG  
15869 C CD1 . PHE D 389 ? 0.2216 0.3015 1.9427 -0.0521 0.1043  0.0469  389 PHE D CD1 
15870 C CD2 . PHE D 389 ? 0.2502 0.3341 1.9525 -0.0591 0.1264  0.0504  389 PHE D CD2 
15871 C CE1 . PHE D 389 ? 0.2064 0.2961 1.9383 -0.0474 0.1023  0.0360  389 PHE D CE1 
15872 C CE2 . PHE D 389 ? 0.2326 0.3275 1.9490 -0.0540 0.1245  0.0388  389 PHE D CE2 
15873 C CZ  . PHE D 389 ? 0.2139 0.3113 1.9445 -0.0480 0.1118  0.0321  389 PHE D CZ  
15874 N N   . TYR D 390 ? 0.3401 0.3795 2.0309 -0.0813 0.1348  0.0932  390 TYR D N   
15875 C CA  . TYR D 390 ? 0.3791 0.4009 2.0526 -0.0863 0.1361  0.1078  390 TYR D CA  
15876 C C   . TYR D 390 ? 0.4025 0.4163 2.0392 -0.0887 0.1427  0.1158  390 TYR D C   
15877 O O   . TYR D 390 ? 0.3893 0.4110 2.0192 -0.0906 0.1538  0.1107  390 TYR D O   
15878 C CB  . TYR D 390 ? 0.4064 0.4249 2.1001 -0.0952 0.1475  0.1118  390 TYR D CB  
15879 C CG  . TYR D 390 ? 0.3974 0.4212 2.1272 -0.0942 0.1409  0.1047  390 TYR D CG  
15880 C CD1 . TYR D 390 ? 0.3788 0.4198 2.1344 -0.0909 0.1393  0.0903  390 TYR D CD1 
15881 C CD2 . TYR D 390 ? 0.4145 0.4250 2.1526 -0.0968 0.1363  0.1123  390 TYR D CD2 
15882 C CE1 . TYR D 390 ? 0.3542 0.3989 2.1403 -0.0902 0.1322  0.0832  390 TYR D CE1 
15883 C CE2 . TYR D 390 ? 0.3989 0.4133 2.1690 -0.0963 0.1304  0.1048  390 TYR D CE2 
15884 C CZ  . TYR D 390 ? 0.3593 0.3909 2.1524 -0.0930 0.1280  0.0900  390 TYR D CZ  
15885 O OH  . TYR D 390 ? 0.3574 0.3920 2.1792 -0.0921 0.1206  0.0819  390 TYR D OH  
15886 N N   . ASP D 391 ? 0.4344 0.4313 2.0479 -0.0889 0.1357  0.1283  391 ASP D N   
15887 C CA  . ASP D 391 ? 0.4734 0.4592 2.0478 -0.0906 0.1380  0.1369  391 ASP D CA  
15888 C C   . ASP D 391 ? 0.5077 0.4788 2.0684 -0.1007 0.1525  0.1493  391 ASP D C   
15889 O O   . ASP D 391 ? 0.5055 0.4787 2.0907 -0.1063 0.1620  0.1489  391 ASP D O   
15890 C CB  . ASP D 391 ? 0.4698 0.4459 2.0273 -0.0841 0.1198  0.1429  391 ASP D CB  
15891 C CG  . ASP D 391 ? 0.4830 0.4424 2.0426 -0.0851 0.1121  0.1552  391 ASP D CG  
15892 O OD1 . ASP D 391 ? 0.4878 0.4402 2.0575 -0.0921 0.1218  0.1610  391 ASP D OD1 
15893 O OD2 . ASP D 391 ? 0.5142 0.4674 2.0667 -0.0790 0.0965  0.1588  391 ASP D OD2 
15894 N N   . SER D 392 ? 0.5512 0.5059 2.0724 -0.1031 0.1529  0.1606  392 SER D N   
15895 C CA  . SER D 392 ? 0.5887 0.5260 2.0891 -0.1130 0.1674  0.1736  392 SER D CA  
15896 C C   . SER D 392 ? 0.6124 0.5305 2.1151 -0.1152 0.1603  0.1877  392 SER D C   
15897 O O   . SER D 392 ? 0.6488 0.5480 2.1302 -0.1233 0.1702  0.2010  392 SER D O   
15898 C CB  . SER D 392 ? 0.6136 0.5392 2.0667 -0.1147 0.1706  0.1797  392 SER D CB  
15899 O OG  . SER D 392 ? 0.6314 0.5369 2.0576 -0.1119 0.1545  0.1930  392 SER D OG  
15900 N N   . ASP D 393 ? 0.5884 0.5092 2.1148 -0.1082 0.1435  0.1854  393 ASP D N   
15901 C CA  . ASP D 393 ? 0.6009 0.5055 2.1380 -0.1104 0.1385  0.1963  393 ASP D CA  
15902 C C   . ASP D 393 ? 0.5630 0.4813 2.1462 -0.1106 0.1405  0.1858  393 ASP D C   
15903 O O   . ASP D 393 ? 0.5726 0.4817 2.1731 -0.1099 0.1329  0.1902  393 ASP D O   
15904 C CB  . ASP D 393 ? 0.6045 0.4967 2.1295 -0.1022 0.1170  0.2037  393 ASP D CB  
15905 C CG  . ASP D 393 ? 0.6404 0.5163 2.1193 -0.1019 0.1119  0.2151  393 ASP D CG  
15906 O OD1 . ASP D 393 ? 0.6844 0.5408 2.1384 -0.1100 0.1220  0.2285  393 ASP D OD1 
15907 O OD2 . ASP D 393 ? 0.6127 0.4949 2.0805 -0.0939 0.0981  0.2103  393 ASP D OD2 
15908 N N   . ASN D 394 ? 0.5249 0.4645 2.1268 -0.1109 0.1493  0.1715  394 ASN D N   
15909 C CA  . ASN D 394 ? 0.4975 0.4521 2.1417 -0.1111 0.1510  0.1597  394 ASN D CA  
15910 C C   . ASN D 394 ? 0.4811 0.4400 2.1435 -0.1014 0.1320  0.1530  394 ASN D C   
15911 O O   . ASN D 394 ? 0.4485 0.4097 2.1412 -0.1021 0.1297  0.1483  394 ASN D O   
15912 C CB  . ASN D 394 ? 0.5109 0.4566 2.1713 -0.1218 0.1644  0.1663  394 ASN D CB  
15913 C CG  . ASN D 394 ? 0.4871 0.4498 2.1917 -0.1233 0.1678  0.1528  394 ASN D CG  
15914 O OD1 . ASN D 394 ? 0.4723 0.4536 2.1899 -0.1237 0.1759  0.1413  394 ASN D OD1 
15915 N ND2 . ASN D 394 ? 0.4770 0.4332 2.2056 -0.1240 0.1608  0.1537  394 ASN D ND2 
15916 N N   . LYS D 395 ? 0.5042 0.4652 2.1492 -0.0929 0.1193  0.1510  395 LYS D N   
15917 C CA  . LYS D 395 ? 0.5069 0.4715 2.1664 -0.0839 0.1029  0.1446  395 LYS D CA  
15918 C C   . LYS D 395 ? 0.4499 0.4341 2.1187 -0.0778 0.1002  0.1292  395 LYS D C   
15919 O O   . LYS D 395 ? 0.4670 0.4570 2.1164 -0.0761 0.1020  0.1271  395 LYS D O   
15920 C CB  . LYS D 395 ? 0.5918 0.5426 2.2289 -0.0789 0.0899  0.1546  395 LYS D CB  
15921 C CG  . LYS D 395 ? 0.7296 0.6596 2.3675 -0.0822 0.0875  0.1682  395 LYS D CG  
15922 C CD  . LYS D 395 ? 0.8681 0.7834 2.4909 -0.0763 0.0721  0.1780  395 LYS D CD  
15923 C CE  . LYS D 395 ? 0.9643 0.8599 2.5962 -0.0788 0.0693  0.1892  395 LYS D CE  
15924 N NZ  . LYS D 395 ? 1.0397 0.9216 2.6615 -0.0719 0.0529  0.1979  395 LYS D NZ  
15925 N N   . ILE D 396 ? 0.3990 0.3917 2.0960 -0.0746 0.0953  0.1186  396 ILE D N   
15926 C CA  . ILE D 396 ? 0.3637 0.3728 2.0693 -0.0692 0.0925  0.1045  396 ILE D CA  
15927 C C   . ILE D 396 ? 0.3405 0.3498 2.0256 -0.0623 0.0835  0.1043  396 ILE D C   
15928 O O   . ILE D 396 ? 0.3622 0.3629 2.0438 -0.0587 0.0739  0.1090  396 ILE D O   
15929 C CB  . ILE D 396 ? 0.3684 0.3828 2.1028 -0.0664 0.0865  0.0940  396 ILE D CB  
15930 C CG1 . ILE D 396 ? 0.4477 0.4634 2.2052 -0.0741 0.0956  0.0932  396 ILE D CG1 
15931 C CG2 . ILE D 396 ? 0.3268 0.3547 2.0646 -0.0599 0.0818  0.0807  396 ILE D CG2 
15932 C CD1 . ILE D 396 ? 0.4635 0.4885 2.2496 -0.0722 0.0909  0.0798  396 ILE D CD1 
15933 N N   . ILE D 397 ? 0.3333 0.3521 2.0060 -0.0608 0.0870  0.0990  397 ILE D N   
15934 C CA  . ILE D 397 ? 0.3059 0.3259 1.9614 -0.0548 0.0786  0.0973  397 ILE D CA  
15935 C C   . ILE D 397 ? 0.2613 0.2934 1.9280 -0.0492 0.0750  0.0841  397 ILE D C   
15936 O O   . ILE D 397 ? 0.2899 0.3234 1.9475 -0.0441 0.0679  0.0812  397 ILE D O   
15937 C CB  . ILE D 397 ? 0.3174 0.3352 1.9446 -0.0572 0.0838  0.1027  397 ILE D CB  
15938 C CG1 . ILE D 397 ? 0.3047 0.3322 1.9323 -0.0606 0.0965  0.0965  397 ILE D CG1 
15939 C CG2 . ILE D 397 ? 0.3514 0.3533 1.9615 -0.0618 0.0843  0.1174  397 ILE D CG2 
15940 C CD1 . ILE D 397 ? 0.3275 0.3505 1.9261 -0.0644 0.1042  0.1019  397 ILE D CD1 
15941 N N   . LYS D 398 ? 0.2281 0.2679 1.9142 -0.0502 0.0792  0.0761  398 LYS D N   
15942 C CA  . LYS D 398 ? 0.1997 0.2485 1.8933 -0.0447 0.0748  0.0643  398 LYS D CA  
15943 C C   . LYS D 398 ? 0.1858 0.2394 1.9043 -0.0454 0.0753  0.0569  398 LYS D C   
15944 O O   . LYS D 398 ? 0.1918 0.2485 1.9217 -0.0507 0.0833  0.0578  398 LYS D O   
15945 C CB  . LYS D 398 ? 0.1917 0.2482 1.8728 -0.0437 0.0798  0.0598  398 LYS D CB  
15946 C CG  . LYS D 398 ? 0.1746 0.2388 1.8645 -0.0385 0.0760  0.0482  398 LYS D CG  
15947 C CD  . LYS D 398 ? 0.1780 0.2483 1.8562 -0.0368 0.0802  0.0437  398 LYS D CD  
15948 C CE  . LYS D 398 ? 0.1700 0.2448 1.8554 -0.0312 0.0747  0.0335  398 LYS D CE  
15949 N NZ  . LYS D 398 ? 0.1817 0.2604 1.8555 -0.0292 0.0780  0.0295  398 LYS D NZ  
15950 N N   . ASN D 399 ? 0.1696 0.2236 1.8958 -0.0402 0.0667  0.0492  399 ASN D N   
15951 C CA  . ASN D 399 ? 0.1592 0.2182 1.9050 -0.0392 0.0642  0.0396  399 ASN D CA  
15952 C C   . ASN D 399 ? 0.1636 0.2287 1.9024 -0.0337 0.0609  0.0310  399 ASN D C   
15953 O O   . ASN D 399 ? 0.2076 0.2711 1.9284 -0.0306 0.0596  0.0322  399 ASN D O   
15954 C CB  . ASN D 399 ? 0.1479 0.1999 1.9061 -0.0382 0.0570  0.0374  399 ASN D CB  
15955 C CG  . ASN D 399 ? 0.1516 0.1958 1.9173 -0.0435 0.0599  0.0465  399 ASN D CG  
15956 O OD1 . ASN D 399 ? 0.1515 0.1974 1.9298 -0.0497 0.0666  0.0491  399 ASN D OD1 
15957 N ND2 . ASN D 399 ? 0.1542 0.1892 1.9124 -0.0414 0.0555  0.0516  399 ASN D ND2 
15958 N N   . GLU D 400 ? 0.1636 0.2356 1.9174 -0.0328 0.0599  0.0227  400 GLU D N   
15959 C CA  . GLU D 400 ? 0.1534 0.2293 1.9028 -0.0271 0.0553  0.0142  400 GLU D CA  
15960 C C   . GLU D 400 ? 0.1538 0.2358 1.9262 -0.0270 0.0519  0.0061  400 GLU D C   
15961 O O   . GLU D 400 ? 0.1443 0.2328 1.9346 -0.0320 0.0583  0.0071  400 GLU D O   
15962 C CB  . GLU D 400 ? 0.1556 0.2370 1.8928 -0.0263 0.0613  0.0148  400 GLU D CB  
15963 C CG  . GLU D 400 ? 0.1454 0.2291 1.8793 -0.0201 0.0560  0.0063  400 GLU D CG  
15964 C CD  . GLU D 400 ? 0.1430 0.2267 1.8575 -0.0178 0.0592  0.0070  400 GLU D CD  
15965 O OE1 . GLU D 400 ? 0.1495 0.2362 1.8586 -0.0215 0.0679  0.0118  400 GLU D OE1 
15966 O OE2 . GLU D 400 ? 0.1329 0.2126 1.8369 -0.0126 0.0534  0.0026  400 GLU D OE2 
15967 N N   . SER D 401 ? 0.1618 0.2407 1.9332 -0.0216 0.0417  -0.0017 401 SER D N   
15968 C CA  . SER D 401 ? 0.1688 0.2524 1.9606 -0.0203 0.0349  -0.0105 401 SER D CA  
15969 C C   . SER D 401 ? 0.1911 0.2806 1.9813 -0.0153 0.0327  -0.0161 401 SER D C   
15970 O O   . SER D 401 ? 0.2509 0.3362 2.0194 -0.0114 0.0326  -0.0149 401 SER D O   
15971 C CB  . SER D 401 ? 0.1705 0.2447 1.9603 -0.0175 0.0241  -0.0156 401 SER D CB  
15972 O OG  . SER D 401 ? 0.1759 0.2460 1.9752 -0.0224 0.0261  -0.0119 401 SER D OG  
15973 N N   . ILE D 402 ? 0.1973 0.2968 2.0122 -0.0155 0.0313  -0.0222 402 ILE D N   
15974 C CA  . ILE D 402 ? 0.1844 0.2875 2.0011 -0.0090 0.0248  -0.0294 402 ILE D CA  
15975 C C   . ILE D 402 ? 0.1853 0.2884 2.0195 -0.0061 0.0108  -0.0383 402 ILE D C   
15976 O O   . ILE D 402 ? 0.1886 0.2990 2.0501 -0.0105 0.0109  -0.0411 402 ILE D O   
15977 C CB  . ILE D 402 ? 0.1819 0.2979 2.0129 -0.0105 0.0352  -0.0298 402 ILE D CB  
15978 C CG1 . ILE D 402 ? 0.1865 0.3016 1.9992 -0.0144 0.0489  -0.0211 402 ILE D CG1 
15979 C CG2 . ILE D 402 ? 0.1923 0.3105 2.0248 -0.0026 0.0273  -0.0372 402 ILE D CG2 
15980 C CD1 . ILE D 402 ? 0.1942 0.3009 1.9770 -0.0095 0.0470  -0.0191 402 ILE D CD1 
15981 N N   . ASN D 403 ? 0.1861 0.2793 2.0026 0.0009  -0.0015 -0.0426 403 ASN D N   
15982 C CA  . ASN D 403 ? 0.1912 0.2802 2.0161 0.0043  -0.0171 -0.0510 403 ASN D CA  
15983 C C   . ASN D 403 ? 0.1849 0.2812 2.0242 0.0101  -0.0248 -0.0577 403 ASN D C   
15984 O O   . ASN D 403 ? 0.1784 0.2704 2.0001 0.0155  -0.0256 -0.0568 403 ASN D O   
15985 C CB  . ASN D 403 ? 0.2101 0.2813 2.0039 0.0090  -0.0269 -0.0522 403 ASN D CB  
15986 C CG  . ASN D 403 ? 0.2075 0.2696 1.9872 0.0049  -0.0221 -0.0478 403 ASN D CG  
15987 O OD1 . ASN D 403 ? 0.2044 0.2558 1.9757 0.0062  -0.0308 -0.0522 403 ASN D OD1 
15988 N ND2 . ASN D 403 ? 0.2009 0.2656 1.9750 0.0009  -0.0088 -0.0395 403 ASN D ND2 
15989 N N   . ILE D 404 ? 0.1858 0.2934 2.0594 0.0089  -0.0302 -0.0644 404 ILE D N   
15990 C CA  . ILE D 404 ? 0.1849 0.3012 2.0783 0.0147  -0.0384 -0.0717 404 ILE D CA  
15991 C C   . ILE D 404 ? 0.2039 0.3161 2.1079 0.0184  -0.0586 -0.0807 404 ILE D C   
15992 O O   . ILE D 404 ? 0.2098 0.3149 2.1097 0.0148  -0.0625 -0.0813 404 ILE D O   
15993 C CB  . ILE D 404 ? 0.1687 0.3049 2.0970 0.0099  -0.0246 -0.0722 404 ILE D CB  
15994 C CG1 . ILE D 404 ? 0.1702 0.3154 2.1287 0.0018  -0.0209 -0.0739 404 ILE D CG1 
15995 C CG2 . ILE D 404 ? 0.1590 0.2960 2.0693 0.0068  -0.0059 -0.0634 404 ILE D CG2 
15996 C CD1 . ILE D 404 ? 0.1715 0.3368 2.1695 -0.0025 -0.0091 -0.0770 404 ILE D CD1 
15997 N N   . LEU D 405 ? 0.2212 0.3353 2.1347 0.0263  -0.0724 -0.0876 405 LEU D N   
15998 C CA  . LEU D 405 ? 0.2391 0.3507 2.1661 0.0304  -0.0939 -0.0971 405 LEU D CA  
15999 C C   . LEU D 405 ? 0.2203 0.3528 2.1952 0.0316  -0.0967 -0.1048 405 LEU D C   
16000 O O   . LEU D 405 ? 0.2242 0.3599 2.2026 0.0387  -0.0997 -0.1065 405 LEU D O   
16001 C CB  . LEU D 405 ? 0.2696 0.3611 2.1606 0.0399  -0.1112 -0.0984 405 LEU D CB  
16002 C CG  . LEU D 405 ? 0.2957 0.3809 2.1935 0.0448  -0.1360 -0.1081 405 LEU D CG  
16003 C CD1 . LEU D 405 ? 0.2989 0.3749 2.1864 0.0390  -0.1384 -0.1096 405 LEU D CD1 
16004 C CD2 . LEU D 405 ? 0.3215 0.3880 2.1876 0.0553  -0.1534 -0.1091 405 LEU D CD2 
16005 N N   . ALA D 406 ? 0.2022 0.3480 2.2143 0.0247  -0.0953 -0.1097 406 ALA D N   
16006 C CA  . ALA D 406 ? 0.1872 0.3566 2.2494 0.0219  -0.0883 -0.1151 406 ALA D CA  
16007 C C   . ALA D 406 ? 0.1776 0.3555 2.2772 0.0255  -0.1097 -0.1279 406 ALA D C   
16008 O O   . ALA D 406 ? 0.1901 0.3566 2.2802 0.0264  -0.1269 -0.1320 406 ALA D O   
16009 C CB  . ALA D 406 ? 0.1785 0.3572 2.2564 0.0096  -0.0667 -0.1098 406 ALA D CB  
16010 N N   . SER D 407 ? 0.1574 0.3556 2.3011 0.0273  -0.1084 -0.1347 407 SER D N   
16011 C CA  . SER D 407 ? 0.1559 0.3672 2.3464 0.0284  -0.1258 -0.1474 407 SER D CA  
16012 C C   . SER D 407 ? 0.1441 0.3822 2.3894 0.0263  -0.1139 -0.1535 407 SER D C   
16013 O O   . SER D 407 ? 0.1408 0.3852 2.3838 0.0264  -0.0953 -0.1487 407 SER D O   
16014 C CB  . SER D 407 ? 0.1682 0.3675 2.3463 0.0404  -0.1560 -0.1543 407 SER D CB  
16015 O OG  . SER D 407 ? 0.1680 0.3823 2.3961 0.0418  -0.1735 -0.1673 407 SER D OG  
16016 N N   . LYS D 408 ? 0.1496 0.4037 2.4458 0.0242  -0.1245 -0.1648 408 LYS D N   
16017 C CA  . LYS D 408 ? 0.1363 0.4179 2.4911 0.0208  -0.1114 -0.1718 408 LYS D CA  
16018 C C   . LYS D 408 ? 0.1510 0.4413 2.5271 0.0337  -0.1257 -0.1802 408 LYS D C   
16019 O O   . LYS D 408 ? 0.1467 0.4590 2.5667 0.0326  -0.1120 -0.1855 408 LYS D O   
16020 C CB  . LYS D 408 ? 0.1221 0.4200 2.5299 0.0116  -0.1136 -0.1809 408 LYS D CB  
16021 C CG  . LYS D 408 ? 0.1086 0.3972 2.4997 -0.0011 -0.1008 -0.1733 408 LYS D CG  
16022 C CD  . LYS D 408 ? 0.0975 0.4047 2.5445 -0.0135 -0.0914 -0.1797 408 LYS D CD  
16023 C CE  . LYS D 408 ? 0.0945 0.3879 2.5286 -0.0217 -0.0965 -0.1776 408 LYS D CE  
16024 N NZ  . LYS D 408 ? 0.0879 0.3968 2.5709 -0.0355 -0.0818 -0.1808 408 LYS D NZ  
16025 N N   . THR D 409 ? 0.1776 0.4495 2.5221 0.0456  -0.1524 -0.1812 409 THR D N   
16026 C CA  . THR D 409 ? 0.1910 0.4634 2.5404 0.0595  -0.1668 -0.1857 409 THR D CA  
16027 C C   . THR D 409 ? 0.2138 0.4555 2.4978 0.0684  -0.1823 -0.1779 409 THR D C   
16028 O O   . THR D 409 ? 0.2172 0.4402 2.4571 0.0636  -0.1810 -0.1703 409 THR D O   
16029 C CB  . THR D 409 ? 0.2005 0.4895 2.6070 0.0651  -0.1909 -0.2010 409 THR D CB  
16030 O OG1 . THR D 409 ? 0.1934 0.4917 2.6239 0.0769  -0.1977 -0.2068 409 THR D OG1 
16031 C CG2 . THR D 409 ? 0.2221 0.4939 2.6096 0.0687  -0.2224 -0.2049 409 THR D CG2 
16032 N N   . ALA D 410 ? 0.2364 0.4728 2.5160 0.0814  -0.1971 -0.1803 410 ALA D N   
16033 C CA  . ALA D 410 ? 0.2602 0.4676 2.4788 0.0897  -0.2078 -0.1720 410 ALA D CA  
16034 C C   . ALA D 410 ? 0.2925 0.4790 2.4832 0.0936  -0.2366 -0.1740 410 ALA D C   
16035 O O   . ALA D 410 ? 0.3051 0.5008 2.5304 0.0942  -0.2552 -0.1844 410 ALA D O   
16036 C CB  . ALA D 410 ? 0.2705 0.4786 2.4977 0.1020  -0.2145 -0.1742 410 ALA D CB  
16037 N N   . PHE D 411 ? 0.3185 0.4764 2.4459 0.0961  -0.2394 -0.1645 411 PHE D N   
16038 C CA  . PHE D 411 ? 0.3381 0.4715 2.4270 0.0994  -0.2632 -0.1649 411 PHE D CA  
16039 C C   . PHE D 411 ? 0.3819 0.4862 2.4137 0.1087  -0.2715 -0.1568 411 PHE D C   
16040 O O   . PHE D 411 ? 0.3646 0.4655 2.3775 0.1090  -0.2534 -0.1485 411 PHE D O   
16041 C CB  . PHE D 411 ? 0.3060 0.4339 2.3747 0.0876  -0.2515 -0.1614 411 PHE D CB  
16042 C CG  . PHE D 411 ? 0.2799 0.4054 2.3214 0.0797  -0.2210 -0.1495 411 PHE D CG  
16043 C CD1 . PHE D 411 ? 0.2474 0.3960 2.3229 0.0715  -0.1955 -0.1479 411 PHE D CD1 
16044 C CD2 . PHE D 411 ? 0.2859 0.3853 2.2669 0.0800  -0.2176 -0.1401 411 PHE D CD2 
16045 C CE1 . PHE D 411 ? 0.2297 0.3745 2.2777 0.0646  -0.1699 -0.1369 411 PHE D CE1 
16046 C CE2 . PHE D 411 ? 0.2554 0.3532 2.2139 0.0730  -0.1915 -0.1300 411 PHE D CE2 
16047 C CZ  . PHE D 411 ? 0.2307 0.3508 2.2220 0.0656  -0.1689 -0.1283 411 PHE D CZ  
16048 N N   . GLU D 412 ? 0.4366 0.5190 2.4406 0.1157  -0.2994 -0.1595 412 GLU D N   
16049 C CA  . GLU D 412 ? 0.4839 0.5347 2.4310 0.1244  -0.3111 -0.1524 412 GLU D CA  
16050 C C   . GLU D 412 ? 0.4708 0.5009 2.3607 0.1171  -0.2935 -0.1418 412 GLU D C   
16051 O O   . GLU D 412 ? 0.4850 0.5058 2.3554 0.1118  -0.2971 -0.1433 412 GLU D O   
16052 C CB  . GLU D 412 ? 0.5662 0.6003 2.5018 0.1322  -0.3463 -0.1596 412 GLU D CB  
16053 C CG  . GLU D 412 ? 0.6601 0.6566 2.5309 0.1408  -0.3614 -0.1522 412 GLU D CG  
16054 C CD  . GLU D 412 ? 0.7659 0.7461 2.6290 0.1510  -0.3994 -0.1595 412 GLU D CD  
16055 O OE1 . GLU D 412 ? 0.7692 0.7520 2.6566 0.1625  -0.4202 -0.1636 412 GLU D OE1 
16056 O OE2 . GLU D 412 ? 0.8234 0.7879 2.6558 0.1470  -0.4085 -0.1618 412 GLU D OE2 
16057 N N   . LEU D 413 ? 0.4567 0.4789 2.3203 0.1176  -0.2758 -0.1319 413 LEU D N   
16058 C CA  . LEU D 413 ? 0.4490 0.4485 2.2560 0.1128  -0.2623 -0.1219 413 LEU D CA  
16059 C C   . LEU D 413 ? 0.4806 0.4460 2.2355 0.1212  -0.2827 -0.1188 413 LEU D C   
16060 O O   . LEU D 413 ? 0.5118 0.4709 2.2728 0.1317  -0.3035 -0.1216 413 LEU D O   
16061 C CB  . LEU D 413 ? 0.4192 0.4253 2.2235 0.1098  -0.2363 -0.1136 413 LEU D CB  
16062 C CG  . LEU D 413 ? 0.3848 0.4216 2.2333 0.1010  -0.2137 -0.1151 413 LEU D CG  
16063 C CD1 . LEU D 413 ? 0.3643 0.4086 2.2152 0.1003  -0.1926 -0.1092 413 LEU D CD1 
16064 C CD2 . LEU D 413 ? 0.3736 0.4109 2.2105 0.0901  -0.2013 -0.1129 413 LEU D CD2 
16065 N N   . PRO D 414 ? 0.4890 0.4302 2.1908 0.1171  -0.2771 -0.1129 414 PRO D N   
16066 C CA  . PRO D 414 ? 0.5131 0.4197 2.1589 0.1237  -0.2884 -0.1068 414 PRO D CA  
16067 C C   . PRO D 414 ? 0.4910 0.3937 2.1270 0.1262  -0.2741 -0.0980 414 PRO D C   
16068 O O   . PRO D 414 ? 0.4414 0.3651 2.1033 0.1211  -0.2525 -0.0958 414 PRO D O   
16069 C CB  . PRO D 414 ? 0.5353 0.4228 2.1355 0.1166  -0.2805 -0.1041 414 PRO D CB  
16070 C CG  . PRO D 414 ? 0.4966 0.4095 2.1266 0.1054  -0.2573 -0.1052 414 PRO D CG  
16071 C CD  . PRO D 414 ? 0.4737 0.4192 2.1677 0.1059  -0.2593 -0.1119 414 PRO D CD  
16072 N N   . GLU D 415 ? 0.5335 0.4081 2.1318 0.1343  -0.2870 -0.0930 415 GLU D N   
16073 C CA  . GLU D 415 ? 0.5415 0.4124 2.1342 0.1369  -0.2748 -0.0855 415 GLU D CA  
16074 C C   . GLU D 415 ? 0.5577 0.3898 2.0880 0.1401  -0.2787 -0.0764 415 GLU D C   
16075 O O   . GLU D 415 ? 0.5858 0.3930 2.0846 0.1457  -0.3005 -0.0770 415 GLU D O   
16076 C CB  . GLU D 415 ? 0.5594 0.4484 2.2003 0.1457  -0.2851 -0.0907 415 GLU D CB  
16077 C CG  . GLU D 415 ? 0.6159 0.4918 2.2589 0.1580  -0.3187 -0.0956 415 GLU D CG  
16078 C CD  . GLU D 415 ? 0.6466 0.5288 2.3192 0.1680  -0.3249 -0.0964 415 GLU D CD  
16079 O OE1 . GLU D 415 ? 0.6358 0.5431 2.3445 0.1644  -0.3043 -0.0975 415 GLU D OE1 
16080 O OE2 . GLU D 415 ? 0.6994 0.5593 2.3555 0.1793  -0.3491 -0.0953 415 GLU D OE2 
16081 N N   . LEU D 416 ? 0.5299 0.3570 2.0426 0.1357  -0.2565 -0.0682 416 LEU D N   
16082 C CA  . LEU D 416 ? 0.5525 0.3442 2.0087 0.1368  -0.2551 -0.0588 416 LEU D CA  
16083 C C   . LEU D 416 ? 0.5489 0.3364 2.0130 0.1435  -0.2548 -0.0545 416 LEU D C   
16084 O O   . LEU D 416 ? 0.5112 0.3230 2.0117 0.1414  -0.2399 -0.0558 416 LEU D O   
16085 C CB  . LEU D 416 ? 0.5401 0.3293 1.9706 0.1250  -0.2290 -0.0538 416 LEU D CB  
16086 C CG  . LEU D 416 ? 0.5752 0.3280 1.9446 0.1231  -0.2234 -0.0449 416 LEU D CG  
16087 C CD1 . LEU D 416 ? 0.5674 0.3198 1.9163 0.1121  -0.2035 -0.0438 416 LEU D CD1 
16088 C CD2 . LEU D 416 ? 0.5743 0.3175 1.9347 0.1241  -0.2122 -0.0370 416 LEU D CD2 
16089 N N   . THR D 417 ? 0.5936 0.3490 2.0231 0.1521  -0.2726 -0.0497 417 THR D N   
16090 C CA  . THR D 417 ? 0.6038 0.3480 2.0317 0.1582  -0.2718 -0.0442 417 THR D CA  
16091 C C   . THR D 417 ? 0.6559 0.3575 2.0192 0.1579  -0.2716 -0.0334 417 THR D C   
16092 O O   . THR D 417 ? 0.6861 0.3663 2.0094 0.1562  -0.2793 -0.0318 417 THR D O   
16093 C CB  . THR D 417 ? 0.6025 0.3534 2.0664 0.1715  -0.2969 -0.0501 417 THR D CB  
16094 O OG1 . THR D 417 ? 0.6387 0.3621 2.0703 0.1787  -0.3244 -0.0496 417 THR D OG1 
16095 C CG2 . THR D 417 ? 0.5596 0.3523 2.0880 0.1710  -0.2965 -0.0615 417 THR D CG2 
16096 N N   . ILE D 418 ? 0.6735 0.3625 2.0266 0.1590  -0.2618 -0.0264 418 ILE D N   
16097 C CA  . ILE D 418 ? 0.7270 0.3748 2.0213 0.1581  -0.2598 -0.0156 418 ILE D CA  
16098 C C   . ILE D 418 ? 0.7676 0.3956 2.0602 0.1690  -0.2732 -0.0110 418 ILE D C   
16099 O O   . ILE D 418 ? 0.7639 0.4143 2.1038 0.1751  -0.2767 -0.0165 418 ILE D O   
16100 C CB  . ILE D 418 ? 0.7088 0.3576 1.9860 0.1451  -0.2285 -0.0104 418 ILE D CB  
16101 C CG1 . ILE D 418 ? 0.6712 0.3476 1.9906 0.1423  -0.2105 -0.0124 418 ILE D CG1 
16102 C CG2 . ILE D 418 ? 0.6991 0.3588 1.9682 0.1355  -0.2179 -0.0137 418 ILE D CG2 
16103 C CD1 . ILE D 418 ? 0.6536 0.3330 1.9600 0.1297  -0.1815 -0.0081 418 ILE D CD1 
16104 N N   . GLU D 419 ? 0.8126 0.3976 2.0497 0.1710  -0.2796 -0.0010 419 GLU D N   
16105 C CA  . GLU D 419 ? 0.8336 0.3920 2.0595 0.1810  -0.2924 0.0054  419 GLU D CA  
16106 C C   . GLU D 419 ? 0.8708 0.3945 2.0434 0.1733  -0.2746 0.0174  419 GLU D C   
16107 O O   . GLU D 419 ? 0.9093 0.4078 2.0319 0.1678  -0.2724 0.0227  419 GLU D O   
16108 C CB  . GLU D 419 ? 0.8692 0.4054 2.0797 0.1939  -0.3276 0.0051  419 GLU D CB  
16109 C CG  . GLU D 419 ? 0.8445 0.4128 2.1158 0.2042  -0.3479 -0.0066 419 GLU D CG  
16110 C CD  . GLU D 419 ? 0.8974 0.4421 2.1533 0.2176  -0.3852 -0.0068 419 GLU D CD  
16111 O OE1 . GLU D 419 ? 0.9245 0.4516 2.1411 0.2153  -0.3953 -0.0058 419 GLU D OE1 
16112 O OE2 . GLU D 419 ? 0.9180 0.4605 2.2000 0.2306  -0.4049 -0.0082 419 GLU D OE2 
16113 N N   . VAL D 420 ? 0.8579 0.3809 2.0420 0.1721  -0.2607 0.0209  420 VAL D N   
16114 C CA  . VAL D 420 ? 0.8801 0.3807 2.0257 0.1615  -0.2373 0.0302  420 VAL D CA  
16115 C C   . VAL D 420 ? 0.9456 0.4037 2.0581 0.1682  -0.2471 0.0405  420 VAL D C   
16116 O O   . VAL D 420 ? 0.9648 0.4230 2.1031 0.1796  -0.2628 0.0389  420 VAL D O   
16117 C CB  . VAL D 420 ? 0.8317 0.3656 2.0149 0.1521  -0.2102 0.0258  420 VAL D CB  
16118 C CG1 . VAL D 420 ? 0.8362 0.3532 1.9842 0.1389  -0.1845 0.0334  420 VAL D CG1 
16119 C CG2 . VAL D 420 ? 0.7911 0.3692 2.0161 0.1482  -0.2047 0.0151  420 VAL D CG2 
16120 N N   . THR D 421 ? 0.9868 0.4081 2.0429 0.1609  -0.2366 0.0512  421 THR D N   
16121 C CA  . THR D 421 ? 1.0327 0.4113 2.0546 0.1651  -0.2417 0.0624  421 THR D CA  
16122 C C   . THR D 421 ? 1.0225 0.3943 2.0316 0.1516  -0.2107 0.0680  421 THR D C   
16123 O O   . THR D 421 ? 1.0035 0.3850 2.0014 0.1390  -0.1894 0.0672  421 THR D O   
16124 C CB  . THR D 421 ? 1.0992 0.4333 2.0606 0.1697  -0.2611 0.0711  421 THR D CB  
16125 O OG1 . THR D 421 ? 1.0939 0.4391 2.0788 0.1834  -0.2919 0.0642  421 THR D OG1 
16126 C CG2 . THR D 421 ? 1.1662 0.4507 2.0854 0.1736  -0.2665 0.0845  421 THR D CG2 
16127 N N   . PRO D 422 ? 1.0164 0.3751 2.0327 0.1535  -0.2064 0.0724  422 PRO D N   
16128 C CA  . PRO D 422 ? 1.0058 0.3704 2.0591 0.1675  -0.2253 0.0686  422 PRO D CA  
16129 C C   . PRO D 422 ? 0.9505 0.3675 2.0703 0.1708  -0.2253 0.0543  422 PRO D C   
16130 O O   . PRO D 422 ? 0.9281 0.3759 2.0723 0.1603  -0.2024 0.0487  422 PRO D O   
16131 C CB  . PRO D 422 ? 1.0194 0.3631 2.0653 0.1631  -0.2098 0.0753  422 PRO D CB  
16132 C CG  . PRO D 422 ? 1.0590 0.3673 2.0459 0.1511  -0.1941 0.0867  422 PRO D CG  
16133 C CD  . PRO D 422 ? 1.0309 0.3671 2.0197 0.1416  -0.1820 0.0807  422 PRO D CD  
16134 N N   . GLU D 423 ? 0.9531 0.3788 2.1025 0.1854  -0.2507 0.0487  423 GLU D N   
16135 C CA  . GLU D 423 ? 0.9117 0.3848 2.1248 0.1897  -0.2524 0.0350  423 GLU D CA  
16136 C C   . GLU D 423 ? 0.8725 0.3655 2.1227 0.1868  -0.2336 0.0302  423 GLU D C   
16137 O O   . GLU D 423 ? 0.8099 0.3402 2.0926 0.1791  -0.2159 0.0221  423 GLU D O   
16138 C CB  . GLU D 423 ? 0.9486 0.4212 2.1853 0.2070  -0.2842 0.0306  423 GLU D CB  
16139 C CG  . GLU D 423 ? 0.9196 0.4418 2.2199 0.2106  -0.2868 0.0160  423 GLU D CG  
16140 C CD  . GLU D 423 ? 0.9663 0.4910 2.2988 0.2278  -0.3167 0.0103  423 GLU D CD  
16141 O OE1 . GLU D 423 ? 1.0256 0.5156 2.3388 0.2383  -0.3343 0.0171  423 GLU D OE1 
16142 O OE2 . GLU D 423 ? 0.9643 0.5254 2.3425 0.2308  -0.3228 -0.0010 423 GLU D OE2 
16143 N N   . LYS D 424 ? 0.9178 0.3852 2.1635 0.1934  -0.2382 0.0347  424 LYS D N   
16144 C CA  . LYS D 424 ? 0.8949 0.3819 2.1812 0.1937  -0.2253 0.0277  424 LYS D CA  
16145 C C   . LYS D 424 ? 0.8817 0.3521 2.1439 0.1813  -0.2009 0.0340  424 LYS D C   
16146 O O   . LYS D 424 ? 0.8548 0.3530 2.1426 0.1727  -0.1799 0.0273  424 LYS D O   
16147 C CB  . LYS D 424 ? 0.9503 0.4261 2.2592 0.2111  -0.2489 0.0253  424 LYS D CB  
16148 C CG  . LYS D 424 ? 0.9847 0.4820 2.3246 0.2226  -0.2725 0.0174  424 LYS D CG  
16149 C CD  . LYS D 424 ? 1.0523 0.5250 2.3964 0.2407  -0.3032 0.0191  424 LYS D CD  
16150 C CE  . LYS D 424 ? 1.0466 0.5531 2.4440 0.2518  -0.3211 0.0066  424 LYS D CE  
16151 N NZ  . LYS D 424 ? 1.0217 0.5626 2.4763 0.2534  -0.3070 -0.0057 424 LYS D NZ  
16152 N N   . ASP D 425 ? 0.9037 0.3285 2.1156 0.1798  -0.2034 0.0469  425 ASP D N   
16153 C CA  . ASP D 425 ? 0.8989 0.3040 2.0926 0.1699  -0.1832 0.0526  425 ASP D CA  
16154 C C   . ASP D 425 ? 0.9238 0.2956 2.0595 0.1589  -0.1738 0.0651  425 ASP D C   
16155 O O   . ASP D 425 ? 0.9914 0.3231 2.0862 0.1646  -0.1892 0.0755  425 ASP D O   
16156 C CB  . ASP D 425 ? 0.9280 0.3045 2.1244 0.1805  -0.1945 0.0557  425 ASP D CB  
16157 C CG  . ASP D 425 ? 0.9432 0.2941 2.1191 0.1708  -0.1757 0.0622  425 ASP D CG  
16158 O OD1 . ASP D 425 ? 0.9304 0.2880 2.0915 0.1553  -0.1532 0.0639  425 ASP D OD1 
16159 O OD2 . ASP D 425 ? 0.9693 0.2949 2.1471 0.1788  -0.1837 0.0648  425 ASP D OD2 
16160 N N   . LEU D 426 ? 0.8768 0.2629 2.0092 0.1433  -0.1478 0.0643  426 LEU D N   
16161 C CA  . LEU D 426 ? 0.8896 0.2534 1.9743 0.1313  -0.1350 0.0735  426 LEU D CA  
16162 C C   . LEU D 426 ? 0.9435 0.2540 1.9813 0.1302  -0.1353 0.0872  426 LEU D C   
16163 O O   . LEU D 426 ? 0.9727 0.2546 1.9623 0.1244  -0.1322 0.0965  426 LEU D O   
16164 C CB  . LEU D 426 ? 0.8448 0.2387 1.9457 0.1157  -0.1074 0.0682  426 LEU D CB  
16165 C CG  . LEU D 426 ? 0.7903 0.2320 1.9263 0.1144  -0.1052 0.0573  426 LEU D CG  
16166 C CD1 . LEU D 426 ? 0.7554 0.2198 1.8992 0.0989  -0.0790 0.0542  426 LEU D CD1 
16167 C CD2 . LEU D 426 ? 0.7971 0.2381 1.9161 0.1195  -0.1207 0.0579  426 LEU D CD2 
16168 N N   . ASN D 427 ? 0.9555 0.2508 2.0060 0.1358  -0.1389 0.0882  427 ASN D N   
16169 C CA  . ASN D 427 ? 1.0131 0.2565 2.0212 0.1345  -0.1386 0.1015  427 ASN D CA  
16170 C C   . ASN D 427 ? 1.0758 0.2798 2.0373 0.1439  -0.1615 0.1123  427 ASN D C   
16171 O O   . ASN D 427 ? 1.1282 0.2852 2.0411 0.1403  -0.1593 0.1256  427 ASN D O   
16172 C CB  . ASN D 427 ? 1.0169 0.2498 2.0488 0.1410  -0.1420 0.1000  427 ASN D CB  
16173 C CG  . ASN D 427 ? 0.9842 0.2330 2.0384 0.1279  -0.1160 0.0948  427 ASN D CG  
16174 O OD1 . ASN D 427 ? 0.9919 0.2283 2.0203 0.1130  -0.0954 0.1006  427 ASN D OD1 
16175 N ND2 . ASN D 427 ? 0.9505 0.2251 2.0520 0.1331  -0.1164 0.0835  427 ASN D ND2 
16176 N N   . GLU D 428 ? 1.0790 0.3012 2.0547 0.1555  -0.1836 0.1067  428 GLU D N   
16177 C CA  . GLU D 428 ? 1.1466 0.3336 2.0833 0.1668  -0.2103 0.1153  428 GLU D CA  
16178 C C   . GLU D 428 ? 1.1862 0.3465 2.0626 0.1570  -0.2030 0.1249  428 GLU D C   
16179 O O   . GLU D 428 ? 1.2482 0.3667 2.0773 0.1637  -0.2213 0.1353  428 GLU D O   
16180 C CB  . GLU D 428 ? 1.1337 0.3518 2.1034 0.1797  -0.2343 0.1051  428 GLU D CB  
16181 C CG  . GLU D 428 ? 1.1316 0.3609 2.1482 0.1959  -0.2544 0.0983  428 GLU D CG  
16182 C CD  . GLU D 428 ? 1.1226 0.3845 2.1715 0.2064  -0.2757 0.0879  428 GLU D CD  
16183 O OE1 . GLU D 428 ? 1.0778 0.3653 2.1266 0.1992  -0.2693 0.0829  428 GLU D OE1 
16184 O OE2 . GLU D 428 ? 1.1356 0.3950 2.2106 0.2224  -0.2997 0.0849  428 GLU D OE2 
16185 N N   . GLY D 429 ? 1.1534 0.3383 2.0318 0.1421  -0.1777 0.1206  429 GLY D N   
16186 C CA  . GLY D 429 ? 1.1958 0.3562 2.0188 0.1320  -0.1673 0.1285  429 GLY D CA  
16187 C C   . GLY D 429 ? 1.1792 0.3536 2.0043 0.1133  -0.1320 0.1272  429 GLY D C   
16188 O O   . GLY D 429 ? 1.1184 0.3286 1.9914 0.1087  -0.1180 0.1184  429 GLY D O   
16189 N N   . LYS D 430 ? 1.2319 0.3758 2.0033 0.1029  -0.1181 0.1360  430 LYS D N   
16190 C CA  . LYS D 430 ? 1.2182 0.3788 1.9905 0.0855  -0.0863 0.1333  430 LYS D CA  
16191 C C   . LYS D 430 ? 1.1778 0.3642 1.9492 0.0835  -0.0856 0.1258  430 LYS D C   
16192 O O   . LYS D 430 ? 1.1434 0.3519 1.9249 0.0708  -0.0615 0.1210  430 LYS D O   
16193 C CB  . LYS D 430 ? 1.2950 0.4081 2.0142 0.0738  -0.0672 0.1466  430 LYS D CB  
16194 C CG  . LYS D 430 ? 1.3454 0.4385 2.0732 0.0725  -0.0619 0.1524  430 LYS D CG  
16195 C CD  . LYS D 430 ? 1.4246 0.4682 2.1009 0.0606  -0.0429 0.1663  430 LYS D CD  
16196 C CE  . LYS D 430 ? 1.4238 0.4820 2.0982 0.0424  -0.0102 0.1633  430 LYS D CE  
16197 N NZ  . LYS D 430 ? 1.4874 0.4993 2.1186 0.0304  0.0096  0.1761  430 LYS D NZ  
16198 N N   . ILE D 431 ? 1.1843 0.3670 1.9446 0.0959  -0.1125 0.1244  431 ILE D N   
16199 C CA  . ILE D 431 ? 1.1624 0.3693 1.9243 0.0953  -0.1150 0.1163  431 ILE D CA  
16200 C C   . ILE D 431 ? 1.1231 0.3682 1.9362 0.1081  -0.1383 0.1054  431 ILE D C   
16201 O O   . ILE D 431 ? 1.1595 0.3948 1.9820 0.1212  -0.1620 0.1070  431 ILE D O   
16202 C CB  . ILE D 431 ? 1.2160 0.3806 1.9106 0.0964  -0.1244 0.1242  431 ILE D CB  
16203 C CG1 . ILE D 431 ? 1.2666 0.3868 1.9055 0.0844  -0.1023 0.1365  431 ILE D CG1 
16204 C CG2 . ILE D 431 ? 1.1931 0.3835 1.8908 0.0942  -0.1241 0.1145  431 ILE D CG2 
16205 C CD1 . ILE D 431 ? 1.3407 0.4095 1.9065 0.0878  -0.1154 0.1466  431 ILE D CD1 
16206 N N   . ALA D 432 ? 1.0696 0.3575 1.9167 0.1043  -0.1312 0.0942  432 ALA D N   
16207 C CA  . ALA D 432 ? 1.0283 0.3537 1.9235 0.1145  -0.1504 0.0834  432 ALA D CA  
16208 C C   . ALA D 432 ? 1.0350 0.3656 1.9142 0.1158  -0.1606 0.0786  432 ALA D C   
16209 O O   . ALA D 432 ? 1.0572 0.3742 1.8995 0.1063  -0.1457 0.0810  432 ALA D O   
16210 C CB  . ALA D 432 ? 0.9624 0.3353 1.9159 0.1087  -0.1331 0.0740  432 ALA D CB  
16211 N N   . SER D 433 ? 1.0165 0.3679 1.9260 0.1273  -0.1851 0.0709  433 SER D N   
16212 C CA  . SER D 433 ? 1.0067 0.3713 1.9133 0.1282  -0.1948 0.0637  433 SER D CA  
16213 C C   . SER D 433 ? 0.9442 0.3598 1.9174 0.1320  -0.2000 0.0511  433 SER D C   
16214 O O   . SER D 433 ? 0.9195 0.3511 1.9329 0.1387  -0.2064 0.0488  433 SER D O   
16215 C CB  . SER D 433 ? 1.0664 0.3949 1.9297 0.1386  -0.2239 0.0679  433 SER D CB  
16216 O OG  . SER D 433 ? 1.0629 0.4026 1.9606 0.1533  -0.2531 0.0635  433 SER D OG  
16217 N N   . ILE D 434 ? 0.9157 0.3551 1.8991 0.1271  -0.1957 0.0432  434 ILE D N   
16218 C CA  . ILE D 434 ? 0.8685 0.3500 1.9067 0.1315  -0.2056 0.0316  434 ILE D CA  
16219 C C   . ILE D 434 ? 0.9001 0.3748 1.9213 0.1369  -0.2279 0.0270  434 ILE D C   
16220 O O   . ILE D 434 ? 0.9236 0.3892 1.9131 0.1298  -0.2196 0.0264  434 ILE D O   
16221 C CB  . ILE D 434 ? 0.8077 0.3281 1.8823 0.1204  -0.1797 0.0255  434 ILE D CB  
16222 C CG1 . ILE D 434 ? 0.7858 0.3131 1.8786 0.1158  -0.1606 0.0291  434 ILE D CG1 
16223 C CG2 . ILE D 434 ? 0.7583 0.3201 1.8851 0.1236  -0.1884 0.0141  434 ILE D CG2 
16224 C CD1 . ILE D 434 ? 0.7389 0.3009 1.8630 0.1048  -0.1356 0.0242  434 ILE D CD1 
16225 N N   . LYS D 435 ? 0.9081 0.3874 1.9522 0.1496  -0.2562 0.0229  435 LYS D N   
16226 C CA  . LYS D 435 ? 0.9284 0.4086 1.9699 0.1557  -0.2806 0.0161  435 LYS D CA  
16227 C C   . LYS D 435 ? 0.8704 0.4001 1.9748 0.1544  -0.2788 0.0037  435 LYS D C   
16228 O O   . LYS D 435 ? 0.8382 0.3941 1.9940 0.1600  -0.2839 -0.0008 435 LYS D O   
16229 C CB  . LYS D 435 ? 0.9765 0.4335 2.0096 0.1707  -0.3144 0.0185  435 LYS D CB  
16230 C CG  . LYS D 435 ? 1.0417 0.4444 2.0074 0.1734  -0.3209 0.0317  435 LYS D CG  
16231 C CD  . LYS D 435 ? 1.0915 0.4671 2.0396 0.1884  -0.3588 0.0336  435 LYS D CD  
16232 C CE  . LYS D 435 ? 1.0803 0.4725 2.0807 0.2001  -0.3738 0.0312  435 LYS D CE  
16233 N NZ  . LYS D 435 ? 1.1309 0.4994 2.1203 0.2156  -0.4121 0.0323  435 LYS D NZ  
16234 N N   . THR D 436 ? 0.8673 0.4079 1.9664 0.1467  -0.2709 -0.0019 436 THR D N   
16235 C CA  . THR D 436 ? 0.8125 0.3969 1.9660 0.1434  -0.2662 -0.0127 436 THR D CA  
16236 C C   . THR D 436 ? 0.8052 0.3948 1.9720 0.1514  -0.2953 -0.0215 436 THR D C   
16237 O O   . THR D 436 ? 0.8483 0.4084 1.9694 0.1536  -0.3103 -0.0206 436 THR D O   
16238 C CB  . THR D 436 ? 0.8095 0.4020 1.9511 0.1302  -0.2393 -0.0133 436 THR D CB  
16239 O OG1 . THR D 436 ? 0.8152 0.3937 1.9335 0.1236  -0.2161 -0.0043 436 THR D OG1 
16240 C CG2 . THR D 436 ? 0.7657 0.4031 1.9644 0.1256  -0.2296 -0.0223 436 THR D CG2 
16241 N N   . LYS D 437 ? 0.7542 0.3803 1.9828 0.1553  -0.3031 -0.0302 437 LYS D N   
16242 C CA  . LYS D 437 ? 0.7531 0.3886 2.0042 0.1626  -0.3309 -0.0398 437 LYS D CA  
16243 C C   . LYS D 437 ? 0.6946 0.3740 2.0031 0.1569  -0.3221 -0.0502 437 LYS D C   
16244 O O   . LYS D 437 ? 0.6452 0.3546 2.0025 0.1561  -0.3107 -0.0523 437 LYS D O   
16245 C CB  . LYS D 437 ? 0.7662 0.3985 2.0396 0.1765  -0.3574 -0.0406 437 LYS D CB  
16246 C CG  . LYS D 437 ? 0.7780 0.4191 2.0757 0.1845  -0.3885 -0.0510 437 LYS D CG  
16247 C CD  . LYS D 437 ? 0.7966 0.4351 2.1195 0.1991  -0.4159 -0.0523 437 LYS D CD  
16248 C CE  . LYS D 437 ? 0.8137 0.4581 2.1579 0.2072  -0.4489 -0.0625 437 LYS D CE  
16249 N NZ  . LYS D 437 ? 0.8255 0.4708 2.2012 0.2216  -0.4735 -0.0642 437 LYS D NZ  
16250 N N   . ILE D 438 ? 0.7068 0.3876 2.0074 0.1532  -0.3283 -0.0569 438 ILE D N   
16251 C CA  . ILE D 438 ? 0.6722 0.3896 2.0198 0.1463  -0.3189 -0.0660 438 ILE D CA  
16252 C C   . ILE D 438 ? 0.6891 0.4150 2.0619 0.1525  -0.3477 -0.0768 438 ILE D C   
16253 O O   . ILE D 438 ? 0.7269 0.4274 2.0613 0.1553  -0.3666 -0.0789 438 ILE D O   
16254 C CB  . ILE D 438 ? 0.6688 0.3827 1.9892 0.1347  -0.2973 -0.0653 438 ILE D CB  
16255 C CG1 . ILE D 438 ? 0.6656 0.3687 1.9581 0.1282  -0.2701 -0.0551 438 ILE D CG1 
16256 C CG2 . ILE D 438 ? 0.6280 0.3787 1.9986 0.1279  -0.2881 -0.0739 438 ILE D CG2 
16257 C CD1 . ILE D 438 ? 0.6672 0.3634 1.9301 0.1179  -0.2506 -0.0547 438 ILE D CD1 
16258 N N   . GLU D 439 ? 0.6637 0.4260 2.1016 0.1538  -0.3493 -0.0842 439 GLU D N   
16259 C CA  . GLU D 439 ? 0.6763 0.4538 2.1515 0.1586  -0.3744 -0.0958 439 GLU D CA  
16260 C C   . GLU D 439 ? 0.6451 0.4480 2.1487 0.1482  -0.3617 -0.1033 439 GLU D C   
16261 O O   . GLU D 439 ? 0.5972 0.4274 2.1355 0.1410  -0.3376 -0.1027 439 GLU D O   
16262 C CB  . GLU D 439 ? 0.6728 0.4758 2.2073 0.1663  -0.3829 -0.0999 439 GLU D CB  
16263 C CG  . GLU D 439 ? 0.7137 0.4931 2.2309 0.1794  -0.4039 -0.0951 439 GLU D CG  
16264 C CD  . GLU D 439 ? 0.7220 0.5245 2.2997 0.1892  -0.4260 -0.1047 439 GLU D CD  
16265 O OE1 . GLU D 439 ? 0.7015 0.5392 2.3348 0.1845  -0.4214 -0.1145 439 GLU D OE1 
16266 O OE2 . GLU D 439 ? 0.7805 0.5647 2.3499 0.2014  -0.4481 -0.1024 439 GLU D OE2 
16267 N N   . THR D 440 ? 0.6762 0.4683 2.1630 0.1476  -0.3786 -0.1103 440 THR D N   
16268 C CA  . THR D 440 ? 0.6595 0.4687 2.1633 0.1374  -0.3668 -0.1170 440 THR D CA  
16269 C C   . THR D 440 ? 0.6578 0.5003 2.2295 0.1383  -0.3789 -0.1283 440 THR D C   
16270 O O   . THR D 440 ? 0.6837 0.5268 2.2748 0.1477  -0.4058 -0.1339 440 THR D O   
16271 C CB  . THR D 440 ? 0.6953 0.4752 2.1461 0.1356  -0.3771 -0.1198 440 THR D CB  
16272 O OG1 . THR D 440 ? 0.7305 0.4963 2.1753 0.1453  -0.4125 -0.1264 440 THR D OG1 
16273 C CG2 . THR D 440 ? 0.7195 0.4663 2.1033 0.1337  -0.3626 -0.1091 440 THR D CG2 
16274 N N   . SER D 441 ? 0.6485 0.5182 2.2567 0.1283  -0.3585 -0.1313 441 SER D N   
16275 C CA  . SER D 441 ? 0.6460 0.5439 2.3120 0.1258  -0.3673 -0.1429 441 SER D CA  
16276 C C   . SER D 441 ? 0.6538 0.5464 2.3046 0.1172  -0.3638 -0.1481 441 SER D C   
16277 O O   . SER D 441 ? 0.6692 0.5485 2.2818 0.1111  -0.3440 -0.1415 441 SER D O   
16278 C CB  . SER D 441 ? 0.6075 0.5407 2.3307 0.1212  -0.3460 -0.1421 441 SER D CB  
16279 O OG  . SER D 441 ? 0.5981 0.5311 2.3197 0.1267  -0.3381 -0.1343 441 SER D OG  
16280 N N   . GLU D 442 ? 0.6604 0.5627 2.3414 0.1167  -0.3829 -0.1602 442 GLU D N   
16281 C CA  . GLU D 442 ? 0.6841 0.5822 2.3548 0.1083  -0.3792 -0.1661 442 GLU D CA  
16282 C C   . GLU D 442 ? 0.6412 0.5675 2.3530 0.0973  -0.3506 -0.1646 442 GLU D C   
16283 O O   . GLU D 442 ? 0.6133 0.5677 2.3773 0.0961  -0.3432 -0.1648 442 GLU D O   
16284 C CB  . GLU D 442 ? 0.7184 0.6154 2.4056 0.1109  -0.4100 -0.1803 442 GLU D CB  
16285 C CG  . GLU D 442 ? 0.6929 0.6246 2.4562 0.1111  -0.4189 -0.1890 442 GLU D CG  
16286 C CD  . GLU D 442 ? 0.7203 0.6491 2.5000 0.1187  -0.4568 -0.2016 442 GLU D CD  
16287 O OE1 . GLU D 442 ? 0.7429 0.6647 2.5170 0.1148  -0.4690 -0.2113 442 GLU D OE1 
16288 O OE2 . GLU D 442 ? 0.7037 0.6370 2.5021 0.1287  -0.4744 -0.2022 442 GLU D OE2 
16289 N N   . ASN D 443 ? 0.6460 0.5632 2.3318 0.0893  -0.3338 -0.1626 443 ASN D N   
16290 C CA  . ASN D 443 ? 0.6124 0.5518 2.3317 0.0788  -0.3088 -0.1610 443 ASN D CA  
16291 C C   . ASN D 443 ? 0.5650 0.5078 2.2717 0.0761  -0.2806 -0.1479 443 ASN D C   
16292 O O   . ASN D 443 ? 0.5620 0.5171 2.2833 0.0676  -0.2587 -0.1445 443 ASN D O   
16293 C CB  . ASN D 443 ? 0.5955 0.5669 2.3841 0.0757  -0.3121 -0.1682 443 ASN D CB  
16294 C CG  . ASN D 443 ? 0.5914 0.5627 2.3983 0.0739  -0.3331 -0.1818 443 ASN D CG  
16295 O OD1 . ASN D 443 ? 0.5935 0.5596 2.3929 0.0666  -0.3262 -0.1850 443 ASN D OD1 
16296 N ND2 . ASN D 443 ? 0.6052 0.5819 2.4368 0.0807  -0.3594 -0.1905 443 ASN D ND2 
16297 N N   . PHE D 444 ? 0.5399 0.4713 2.2203 0.0831  -0.2821 -0.1407 444 PHE D N   
16298 C CA  . PHE D 444 ? 0.5226 0.4492 2.1775 0.0807  -0.2577 -0.1289 444 PHE D CA  
16299 C C   . PHE D 444 ? 0.5599 0.4529 2.1504 0.0827  -0.2594 -0.1256 444 PHE D C   
16300 O O   . PHE D 444 ? 0.6163 0.4883 2.1773 0.0903  -0.2792 -0.1269 444 PHE D O   
16301 C CB  . PHE D 444 ? 0.5108 0.4460 2.1785 0.0861  -0.2545 -0.1227 444 PHE D CB  
16302 C CG  . PHE D 444 ? 0.4711 0.4396 2.1991 0.0834  -0.2460 -0.1245 444 PHE D CG  
16303 C CD1 . PHE D 444 ? 0.4394 0.4235 2.1812 0.0758  -0.2193 -0.1179 444 PHE D CD1 
16304 C CD2 . PHE D 444 ? 0.4695 0.4526 2.2388 0.0887  -0.2644 -0.1327 444 PHE D CD2 
16305 C CE1 . PHE D 444 ? 0.4053 0.4174 2.1973 0.0730  -0.2098 -0.1191 444 PHE D CE1 
16306 C CE2 . PHE D 444 ? 0.4382 0.4513 2.2620 0.0857  -0.2538 -0.1345 444 PHE D CE2 
16307 C CZ  . PHE D 444 ? 0.4108 0.4375 2.2438 0.0777  -0.2259 -0.1274 444 PHE D CZ  
16308 N N   . THR D 445 ? 0.5572 0.4448 2.1263 0.0758  -0.2380 -0.1209 445 THR D N   
16309 C CA  . THR D 445 ? 0.5901 0.4474 2.1015 0.0760  -0.2364 -0.1193 445 THR D CA  
16310 C C   . THR D 445 ? 0.5839 0.4306 2.0655 0.0771  -0.2209 -0.1078 445 THR D C   
16311 O O   . THR D 445 ? 0.5495 0.4120 2.0485 0.0726  -0.1999 -0.1012 445 THR D O   
16312 C CB  . THR D 445 ? 0.5912 0.4493 2.1017 0.0680  -0.2239 -0.1234 445 THR D CB  
16313 O OG1 . THR D 445 ? 0.6005 0.4614 2.1303 0.0682  -0.2433 -0.1351 445 THR D OG1 
16314 C CG2 . THR D 445 ? 0.6100 0.4399 2.0647 0.0667  -0.2153 -0.1217 445 THR D CG2 
16315 N N   . LEU D 446 ? 0.6123 0.4310 2.0484 0.0832  -0.2324 -0.1055 446 LEU D N   
16316 C CA  . LEU D 446 ? 0.6132 0.4155 2.0124 0.0832  -0.2174 -0.0953 446 LEU D CA  
16317 C C   . LEU D 446 ? 0.6242 0.4134 1.9913 0.0763  -0.1992 -0.0947 446 LEU D C   
16318 O O   . LEU D 446 ? 0.6253 0.4049 1.9789 0.0747  -0.2053 -0.1024 446 LEU D O   
16319 C CB  . LEU D 446 ? 0.6424 0.4164 2.0020 0.0917  -0.2360 -0.0927 446 LEU D CB  
16320 C CG  . LEU D 446 ? 0.6319 0.4159 2.0217 0.1002  -0.2571 -0.0941 446 LEU D CG  
16321 C CD1 . LEU D 446 ? 0.6773 0.4284 2.0210 0.1086  -0.2750 -0.0902 446 LEU D CD1 
16322 C CD2 . LEU D 446 ? 0.5907 0.4011 2.0214 0.0989  -0.2418 -0.0889 446 LEU D CD2 
16323 N N   . LEU D 447 ? 0.6374 0.4240 1.9900 0.0726  -0.1773 -0.0862 447 LEU D N   
16324 C CA  . LEU D 447 ? 0.6693 0.4439 1.9940 0.0665  -0.1599 -0.0864 447 LEU D CA  
16325 C C   . LEU D 447 ? 0.6953 0.4515 1.9822 0.0651  -0.1439 -0.0775 447 LEU D C   
16326 O O   . LEU D 447 ? 0.7032 0.4555 1.9853 0.0685  -0.1454 -0.0706 447 LEU D O   
16327 C CB  . LEU D 447 ? 0.6569 0.4593 2.0240 0.0599  -0.1454 -0.0885 447 LEU D CB  
16328 C CG  . LEU D 447 ? 0.6072 0.4369 2.0153 0.0580  -0.1341 -0.0821 447 LEU D CG  
16329 C CD1 . LEU D 447 ? 0.5943 0.4189 1.9836 0.0547  -0.1135 -0.0738 447 LEU D CD1 
16330 C CD2 . LEU D 447 ? 0.5643 0.4197 2.0166 0.0529  -0.1285 -0.0859 447 LEU D CD2 
16331 N N   . ASP D 448 ? 0.7590 0.5024 2.0190 0.0599  -0.1288 -0.0790 448 ASP D N   
16332 C CA  . ASP D 448 ? 0.8161 0.5432 2.0428 0.0563  -0.1091 -0.0722 448 ASP D CA  
16333 C C   . ASP D 448 ? 0.7858 0.4890 1.9776 0.0614  -0.1183 -0.0656 448 ASP D C   
16334 O O   . ASP D 448 ? 0.8013 0.4811 1.9607 0.0663  -0.1361 -0.0684 448 ASP D O   
16335 C CB  . ASP D 448 ? 0.8458 0.5963 2.1033 0.0502  -0.0862 -0.0679 448 ASP D CB  
16336 C CG  . ASP D 448 ? 0.8365 0.6013 2.1151 0.0449  -0.0749 -0.0740 448 ASP D CG  
16337 O OD1 . ASP D 448 ? 0.7990 0.5830 2.1131 0.0453  -0.0839 -0.0789 448 ASP D OD1 
16338 O OD2 . ASP D 448 ? 0.8360 0.5925 2.0968 0.0402  -0.0568 -0.0740 448 ASP D OD2 
16339 N N   . ASP D 449 ? 0.7627 0.4721 1.9629 0.0604  -0.1068 -0.0570 449 ASP D N   
16340 C CA  . ASP D 449 ? 0.8087 0.4921 1.9715 0.0630  -0.1078 -0.0491 449 ASP D CA  
16341 C C   . ASP D 449 ? 0.7321 0.4287 1.9225 0.0675  -0.1144 -0.0435 449 ASP D C   
16342 O O   . ASP D 449 ? 0.6572 0.3784 1.8828 0.0643  -0.1016 -0.0410 449 ASP D O   
16343 C CB  . ASP D 449 ? 0.8542 0.5242 1.9897 0.0560  -0.0827 -0.0438 449 ASP D CB  
16344 C CG  . ASP D 449 ? 0.9174 0.5669 2.0154 0.0517  -0.0732 -0.0486 449 ASP D CG  
16345 O OD1 . ASP D 449 ? 0.9437 0.6065 2.0593 0.0500  -0.0734 -0.0570 449 ASP D OD1 
16346 O OD2 . ASP D 449 ? 0.9369 0.5570 1.9888 0.0497  -0.0645 -0.0439 449 ASP D OD2 
16347 N N   . LEU D 450 ? 0.7343 0.4123 1.9058 0.0753  -0.1350 -0.0418 450 LEU D N   
16348 C CA  . LEU D 450 ? 0.7371 0.4163 1.9197 0.0800  -0.1398 -0.0354 450 LEU D CA  
16349 C C   . LEU D 450 ? 0.7426 0.4118 1.9066 0.0741  -0.1169 -0.0270 450 LEU D C   
16350 O O   . LEU D 450 ? 0.7706 0.4132 1.8903 0.0704  -0.1075 -0.0239 450 LEU D O   
16351 C CB  . LEU D 450 ? 0.7763 0.4287 1.9299 0.0894  -0.1659 -0.0347 450 LEU D CB  
16352 C CG  . LEU D 450 ? 0.7851 0.4288 1.9391 0.0958  -0.1735 -0.0274 450 LEU D CG  
16353 C CD1 . LEU D 450 ? 0.7381 0.4169 1.9512 0.0985  -0.1753 -0.0299 450 LEU D CD1 
16354 C CD2 . LEU D 450 ? 0.8427 0.4559 1.9626 0.1053  -0.2003 -0.0264 450 LEU D CD2 
16355 N N   . LYS D 451 ? 0.7070 0.3984 1.9060 0.0728  -0.1074 -0.0241 451 LYS D N   
16356 C CA  . LYS D 451 ? 0.7078 0.3932 1.8967 0.0672  -0.0875 -0.0170 451 LYS D CA  
16357 C C   . LYS D 451 ? 0.7167 0.3937 1.9068 0.0732  -0.0957 -0.0114 451 LYS D C   
16358 O O   . LYS D 451 ? 0.7331 0.4256 1.9541 0.0799  -0.1103 -0.0141 451 LYS D O   
16359 C CB  . LYS D 451 ? 0.6793 0.3967 1.9065 0.0600  -0.0688 -0.0191 451 LYS D CB  
16360 C CG  . LYS D 451 ? 0.7018 0.4217 1.9218 0.0535  -0.0570 -0.0234 451 LYS D CG  
16361 C CD  . LYS D 451 ? 0.6834 0.4324 1.9393 0.0468  -0.0398 -0.0247 451 LYS D CD  
16362 C CE  . LYS D 451 ? 0.7043 0.4563 1.9575 0.0422  -0.0314 -0.0300 451 LYS D CE  
16363 N NZ  . LYS D 451 ? 0.6812 0.4597 1.9686 0.0364  -0.0162 -0.0303 451 LYS D NZ  
16364 N N   . ILE D 452 ? 0.7213 0.3728 1.8781 0.0706  -0.0858 -0.0038 452 ILE D N   
16365 C CA  . ILE D 452 ? 0.7130 0.3494 1.8634 0.0761  -0.0932 0.0023  452 ILE D CA  
16366 C C   . ILE D 452 ? 0.6963 0.3322 1.8468 0.0684  -0.0709 0.0076  452 ILE D C   
16367 O O   . ILE D 452 ? 0.7169 0.3406 1.8425 0.0602  -0.0537 0.0101  452 ILE D O   
16368 C CB  . ILE D 452 ? 0.7631 0.3589 1.8630 0.0817  -0.1087 0.0070  452 ILE D CB  
16369 C CG1 . ILE D 452 ? 0.7762 0.3730 1.8787 0.0899  -0.1337 0.0010  452 ILE D CG1 
16370 C CG2 . ILE D 452 ? 0.7916 0.3668 1.8802 0.0867  -0.1143 0.0147  452 ILE D CG2 
16371 C CD1 . ILE D 452 ? 0.8264 0.3896 1.8748 0.0900  -0.1406 0.0020  452 ILE D CD1 
16372 N N   . SER D 453 ? 0.6582 0.3075 1.8377 0.0709  -0.0711 0.0086  453 SER D N   
16373 C CA  . SER D 453 ? 0.6400 0.2887 1.8218 0.0641  -0.0524 0.0129  453 SER D CA  
16374 C C   . SER D 453 ? 0.6555 0.2825 1.8264 0.0701  -0.0610 0.0185  453 SER D C   
16375 O O   . SER D 453 ? 0.6588 0.2901 1.8463 0.0797  -0.0791 0.0164  453 SER D O   
16376 C CB  . SER D 453 ? 0.5878 0.2740 1.8153 0.0597  -0.0411 0.0081  453 SER D CB  
16377 O OG  . SER D 453 ? 0.5740 0.2703 1.8273 0.0646  -0.0463 0.0077  453 SER D OG  
16378 N N   . TYR D 454 ? 0.6771 0.2820 1.8234 0.0642  -0.0472 0.0250  454 TYR D N   
16379 C CA  . TYR D 454 ? 0.6827 0.2692 1.8237 0.0677  -0.0504 0.0304  454 TYR D CA  
16380 C C   . TYR D 454 ? 0.6599 0.2567 1.8163 0.0582  -0.0289 0.0310  454 TYR D C   
16381 O O   . TYR D 454 ? 0.6737 0.2493 1.8035 0.0503  -0.0144 0.0364  454 TYR D O   
16382 C CB  . TYR D 454 ? 0.7367 0.2778 1.8244 0.0697  -0.0566 0.0389  454 TYR D CB  
16383 C CG  . TYR D 454 ? 0.7560 0.2734 1.8356 0.0775  -0.0688 0.0446  454 TYR D CG  
16384 C CD1 . TYR D 454 ? 0.7632 0.2841 1.8589 0.0904  -0.0931 0.0419  454 TYR D CD1 
16385 C CD2 . TYR D 454 ? 0.7713 0.2628 1.8295 0.0723  -0.0568 0.0521  454 TYR D CD2 
16386 C CE1 . TYR D 454 ? 0.7813 0.2805 1.8722 0.0988  -0.1057 0.0466  454 TYR D CE1 
16387 C CE2 . TYR D 454 ? 0.8030 0.2719 1.8552 0.0800  -0.0688 0.0572  454 TYR D CE2 
16388 C CZ  . TYR D 454 ? 0.8024 0.2750 1.8709 0.0937  -0.0936 0.0544  454 TYR D CZ  
16389 O OH  . TYR D 454 ? 0.8272 0.2781 1.8927 0.1024  -0.1064 0.0587  454 TYR D OH  
16390 N N   . ASN D 455 ? 0.6215 0.2517 1.8214 0.0584  -0.0266 0.0249  455 ASN D N   
16391 C CA  . ASN D 455 ? 0.6039 0.2496 1.8222 0.0491  -0.0076 0.0236  455 ASN D CA  
16392 C C   . ASN D 455 ? 0.6240 0.2531 1.8403 0.0505  -0.0072 0.0269  455 ASN D C   
16393 O O   . ASN D 455 ? 0.5983 0.2391 1.8397 0.0572  -0.0158 0.0234  455 ASN D O   
16394 C CB  . ASN D 455 ? 0.5658 0.2520 1.8258 0.0478  -0.0048 0.0159  455 ASN D CB  
16395 C CG  . ASN D 455 ? 0.5492 0.2513 1.8264 0.0382  0.0131  0.0144  455 ASN D CG  
16396 O OD1 . ASN D 455 ? 0.5137 0.2445 1.8163 0.0346  0.0189  0.0097  455 ASN D OD1 
16397 N ND2 . ASN D 455 ? 0.5855 0.2680 1.8486 0.0338  0.0215  0.0184  455 ASN D ND2 
16398 N N   . THR D 456 ? 0.6728 0.2746 1.8597 0.0434  0.0045  0.0333  456 THR D N   
16399 C CA  . THR D 456 ? 0.7083 0.2845 1.8834 0.0438  0.0054  0.0384  456 THR D CA  
16400 C C   . THR D 456 ? 0.6837 0.2817 1.8933 0.0399  0.0144  0.0332  456 THR D C   
16401 O O   . THR D 456 ? 0.7178 0.3008 1.9277 0.0426  0.0118  0.0349  456 THR D O   
16402 C CB  . THR D 456 ? 0.7466 0.2891 1.8804 0.0354  0.0182  0.0465  456 THR D CB  
16403 O OG1 . THR D 456 ? 0.7405 0.2989 1.8771 0.0253  0.0347  0.0438  456 THR D OG1 
16404 C CG2 . THR D 456 ? 0.7907 0.3003 1.8820 0.0414  0.0057  0.0531  456 THR D CG2 
16405 N N   . HIS D 457 ? 0.6479 0.2789 1.8845 0.0334  0.0248  0.0271  457 HIS D N   
16406 C CA  . HIS D 457 ? 0.5957 0.2508 1.8656 0.0303  0.0311  0.0210  457 HIS D CA  
16407 C C   . HIS D 457 ? 0.5860 0.2316 1.8519 0.0192  0.0476  0.0226  457 HIS D C   
16408 O O   . HIS D 457 ? 0.5523 0.2101 1.8401 0.0170  0.0513  0.0180  457 HIS D O   
16409 C CB  . HIS D 457 ? 0.5821 0.2401 1.8692 0.0407  0.0179  0.0176  457 HIS D CB  
16410 C CG  . HIS D 457 ? 0.5519 0.2374 1.8638 0.0480  0.0076  0.0118  457 HIS D CG  
16411 N ND1 . HIS D 457 ? 0.5674 0.2511 1.8709 0.0545  -0.0045 0.0130  457 HIS D ND1 
16412 C CD2 . HIS D 457 ? 0.5168 0.2317 1.8613 0.0492  0.0083  0.0044  457 HIS D CD2 
16413 C CE1 . HIS D 457 ? 0.5399 0.2521 1.8732 0.0592  -0.0107 0.0065  457 HIS D CE1 
16414 N NE2 . HIS D 457 ? 0.5116 0.2426 1.8691 0.0561  -0.0025 0.0015  457 HIS D NE2 
16415 N N   . LEU D 458 ? 0.5971 0.2226 1.8364 0.0117  0.0581  0.0282  458 LEU D N   
16416 C CA  . LEU D 458 ? 0.5890 0.2032 1.8236 0.0004  0.0747  0.0300  458 LEU D CA  
16417 C C   . LEU D 458 ? 0.5431 0.1900 1.8067 -0.0080 0.0861  0.0235  458 LEU D C   
16418 O O   . LEU D 458 ? 0.5424 0.1968 1.8026 -0.0128 0.0938  0.0235  458 LEU D O   
16419 C CB  . LEU D 458 ? 0.6272 0.2096 1.8232 -0.0044 0.0826  0.0379  458 LEU D CB  
16420 C CG  . LEU D 458 ? 0.6703 0.2171 1.8310 0.0044  0.0694  0.0456  458 LEU D CG  
16421 C CD1 . LEU D 458 ? 0.7136 0.2269 1.8334 -0.0029 0.0812  0.0537  458 LEU D CD1 
16422 C CD2 . LEU D 458 ? 0.6791 0.2111 1.8438 0.0104  0.0601  0.0470  458 LEU D CD2 
16423 N N   . GLY D 459 ? 0.5162 0.1818 1.8076 -0.0095 0.0866  0.0177  459 GLY D N   
16424 C CA  . GLY D 459 ? 0.4872 0.1855 1.8070 -0.0154 0.0931  0.0113  459 GLY D CA  
16425 C C   . GLY D 459 ? 0.4792 0.1999 1.8071 -0.0106 0.0870  0.0093  459 GLY D C   
16426 O O   . GLY D 459 ? 0.4774 0.2023 1.8071 -0.0011 0.0743  0.0087  459 GLY D O   
16427 N N   . TRP D 460 ? 0.4778 0.2121 1.8118 -0.0172 0.0963  0.0082  460 TRP D N   
16428 C CA  . TRP D 460 ? 0.4591 0.2150 1.8032 -0.0138 0.0920  0.0060  460 TRP D CA  
16429 C C   . TRP D 460 ? 0.4787 0.2173 1.7962 -0.0111 0.0907  0.0101  460 TRP D C   
16430 O O   . TRP D 460 ? 0.4690 0.2216 1.7918 -0.0072 0.0852  0.0084  460 TRP D O   
16431 C CB  . TRP D 460 ? 0.4408 0.2219 1.8089 -0.0215 0.1013  0.0018  460 TRP D CB  
16432 C CG  . TRP D 460 ? 0.4386 0.2385 1.8317 -0.0234 0.0999  -0.0029 460 TRP D CG  
16433 C CD1 . TRP D 460 ? 0.4503 0.2515 1.8539 -0.0316 0.1082  -0.0052 460 TRP D CD1 
16434 C CD2 . TRP D 460 ? 0.4291 0.2478 1.8384 -0.0172 0.0896  -0.0063 460 TRP D CD2 
16435 N NE1 . TRP D 460 ? 0.4364 0.2554 1.8595 -0.0306 0.1028  -0.0100 460 TRP D NE1 
16436 C CE2 . TRP D 460 ? 0.4215 0.2509 1.8474 -0.0220 0.0923  -0.0105 460 TRP D CE2 
16437 C CE3 . TRP D 460 ? 0.4285 0.2559 1.8403 -0.0086 0.0791  -0.0066 460 TRP D CE3 
16438 C CZ2 . TRP D 460 ? 0.4071 0.2539 1.8481 -0.0184 0.0856  -0.0147 460 TRP D CZ2 
16439 C CZ3 . TRP D 460 ? 0.4138 0.2594 1.8435 -0.0054 0.0735  -0.0106 460 TRP D CZ3 
16440 C CH2 . TRP D 460 ? 0.4075 0.2621 1.8499 -0.0102 0.0771  -0.0145 460 TRP D CH2 
16441 N N   . ALA D 461 ? 0.5007 0.2079 1.7888 -0.0134 0.0957  0.0155  461 ALA D N   
16442 C CA  . ALA D 461 ? 0.5356 0.2214 1.7919 -0.0106 0.0936  0.0198  461 ALA D CA  
16443 C C   . ALA D 461 ? 0.5477 0.2328 1.7998 0.0014  0.0742  0.0199  461 ALA D C   
16444 O O   . ALA D 461 ? 0.5809 0.2576 1.8332 0.0075  0.0641  0.0212  461 ALA D O   
16445 C CB  . ALA D 461 ? 0.5724 0.2224 1.7962 -0.0153 0.1023  0.0262  461 ALA D CB  
16446 N N   . ILE D 462 ? 0.5373 0.2316 1.7878 0.0045  0.0693  0.0180  462 ILE D N   
16447 C CA  . ILE D 462 ? 0.5331 0.2310 1.7843 0.0149  0.0511  0.0168  462 ILE D CA  
16448 C C   . ILE D 462 ? 0.5791 0.2425 1.7907 0.0201  0.0421  0.0222  462 ILE D C   
16449 O O   . ILE D 462 ? 0.5893 0.2518 1.7993 0.0293  0.0250  0.0214  462 ILE D O   
16450 C CB  . ILE D 462 ? 0.5055 0.2277 1.7730 0.0151  0.0500  0.0119  462 ILE D CB  
16451 C CG1 . ILE D 462 ? 0.5277 0.2358 1.7698 0.0103  0.0592  0.0129  462 ILE D CG1 
16452 C CG2 . ILE D 462 ? 0.4565 0.2119 1.7615 0.0109  0.0567  0.0073  462 ILE D CG2 
16453 C CD1 . ILE D 462 ? 0.5360 0.2513 1.7770 0.0150  0.0499  0.0095  462 ILE D CD1 
16454 N N   . GLY D 463 ? 0.6168 0.2522 1.7963 0.0139  0.0536  0.0275  463 GLY D N   
16455 C CA  . GLY D 463 ? 0.6720 0.2700 1.8081 0.0180  0.0459  0.0339  463 GLY D CA  
16456 C C   . GLY D 463 ? 0.6891 0.2833 1.8059 0.0210  0.0394  0.0322  463 GLY D C   
16457 O O   . GLY D 463 ? 0.6651 0.2837 1.8011 0.0180  0.0450  0.0264  463 GLY D O   
16458 N N   . SER D 464 ? 0.7406 0.3035 1.8197 0.0274  0.0261  0.0370  464 SER D N   
16459 C CA  . SER D 464 ? 0.7582 0.3112 1.8113 0.0297  0.0197  0.0354  464 SER D CA  
16460 C C   . SER D 464 ? 0.7112 0.2966 1.7973 0.0354  0.0073  0.0273  464 SER D C   
16461 O O   . SER D 464 ? 0.6555 0.2638 1.7772 0.0410  -0.0035 0.0242  464 SER D O   
16462 C CB  . SER D 464 ? 0.8188 0.3321 1.8255 0.0365  0.0045  0.0420  464 SER D CB  
16463 O OG  . SER D 464 ? 0.8687 0.3475 1.8316 0.0289  0.0200  0.0490  464 SER D OG  
16464 N N   . GLN D 465 ? 0.7342 0.3197 1.8068 0.0328  0.0110  0.0236  465 GLN D N   
16465 C CA  . GLN D 465 ? 0.7290 0.3350 1.8198 0.0379  -0.0019 0.0164  465 GLN D CA  
16466 C C   . GLN D 465 ? 0.7698 0.3493 1.8171 0.0392  -0.0074 0.0159  465 GLN D C   
16467 O O   . GLN D 465 ? 0.8134 0.3656 1.8214 0.0335  0.0055  0.0199  465 GLN D O   
16468 C CB  . GLN D 465 ? 0.6847 0.3269 1.8151 0.0324  0.0102  0.0097  465 GLN D CB  
16469 C CG  . GLN D 465 ? 0.6588 0.3308 1.8347 0.0335  0.0091  0.0084  465 GLN D CG  
16470 C CD  . GLN D 465 ? 0.6350 0.3420 1.8495 0.0298  0.0163  0.0025  465 GLN D CD  
16471 O OE1 . GLN D 465 ? 0.6345 0.3552 1.8658 0.0226  0.0324  0.0022  465 GLN D OE1 
16472 N NE2 . GLN D 465 ? 0.6459 0.3674 1.8762 0.0348  0.0034  -0.0024 465 GLN D NE2 
16473 N N   . ALA D 466 ? 0.7593 0.3466 1.8135 0.0464  -0.0266 0.0107  466 ALA D N   
16474 C CA  . ALA D 466 ? 0.7961 0.3579 1.8085 0.0486  -0.0353 0.0093  466 ALA D CA  
16475 C C   . ALA D 466 ? 0.7618 0.3479 1.8003 0.0516  -0.0463 -0.0002 466 ALA D C   
16476 O O   . ALA D 466 ? 0.7182 0.3328 1.8002 0.0557  -0.0561 -0.0036 466 ALA D O   
16477 C CB  . ALA D 466 ? 0.8403 0.3693 1.8178 0.0568  -0.0554 0.0155  466 ALA D CB  
16478 N N   . SER D 467 ? 0.7873 0.3617 1.7993 0.0491  -0.0432 -0.0047 467 SER D N   
16479 C CA  . SER D 467 ? 0.7765 0.3708 1.8107 0.0516  -0.0538 -0.0141 467 SER D CA  
16480 C C   . SER D 467 ? 0.8215 0.3870 1.8134 0.0572  -0.0732 -0.0164 467 SER D C   
16481 O O   . SER D 467 ? 0.8761 0.4130 1.8207 0.0537  -0.0652 -0.0159 467 SER D O   
16482 C CB  . SER D 467 ? 0.7466 0.3600 1.7988 0.0434  -0.0327 -0.0197 467 SER D CB  
16483 O OG  . SER D 467 ? 0.7003 0.3407 1.7930 0.0393  -0.0189 -0.0173 467 SER D OG  
16484 N N   . VAL D 468 ? 0.8122 0.3845 1.8205 0.0660  -0.0991 -0.0193 468 VAL D N   
16485 C CA  . VAL D 468 ? 0.8592 0.4037 1.8279 0.0720  -0.1208 -0.0217 468 VAL D CA  
16486 C C   . VAL D 468 ? 0.8543 0.4165 1.8427 0.0724  -0.1294 -0.0333 468 VAL D C   
16487 O O   . VAL D 468 ? 0.7961 0.3934 1.8379 0.0728  -0.1316 -0.0382 468 VAL D O   
16488 C CB  . VAL D 468 ? 0.8691 0.4034 1.8374 0.0822  -0.1460 -0.0169 468 VAL D CB  
16489 C CG1 . VAL D 468 ? 0.9255 0.4267 1.8472 0.0890  -0.1704 -0.0184 468 VAL D CG1 
16490 C CG2 . VAL D 468 ? 0.8786 0.3978 1.8335 0.0812  -0.1354 -0.0058 468 VAL D CG2 
16491 N N   . SER D 469 ? 0.9182 0.4542 1.8610 0.0713  -0.1317 -0.0374 469 SER D N   
16492 C CA  . SER D 469 ? 0.9398 0.4844 1.8912 0.0720  -0.1424 -0.0490 469 SER D CA  
16493 C C   . SER D 469 ? 0.9771 0.5135 1.9257 0.0821  -0.1767 -0.0516 469 SER D C   
16494 O O   . SER D 469 ? 1.0205 0.5262 1.9286 0.0872  -0.1892 -0.0448 469 SER D O   
16495 C CB  . SER D 469 ? 0.9875 0.5066 1.8903 0.0666  -0.1297 -0.0533 469 SER D CB  
16496 O OG  . SER D 469 ? 1.0134 0.5336 1.9163 0.0689  -0.1459 -0.0648 469 SER D OG  
16497 N N   . ILE D 470 ? 0.9535 0.5175 1.9472 0.0847  -0.1913 -0.0608 470 ILE D N   
16498 C CA  . ILE D 470 ? 0.9954 0.5561 1.9951 0.0942  -0.2245 -0.0647 470 ILE D CA  
16499 C C   . ILE D 470 ? 1.0392 0.5951 2.0290 0.0942  -0.2384 -0.0770 470 ILE D C   
16500 O O   . ILE D 470 ? 1.0705 0.6266 2.0700 0.1014  -0.2672 -0.0827 470 ILE D O   
16501 C CB  . ILE D 470 ? 0.9516 0.5478 2.0160 0.0985  -0.2334 -0.0647 470 ILE D CB  
16502 C CG1 . ILE D 470 ? 0.8995 0.5348 2.0190 0.0920  -0.2179 -0.0704 470 ILE D CG1 
16503 C CG2 . ILE D 470 ? 0.9529 0.5448 2.0167 0.1008  -0.2268 -0.0531 470 ILE D CG2 
16504 C CD1 . ILE D 470 ? 0.8590 0.5277 2.0401 0.0962  -0.2287 -0.0723 470 ILE D CD1 
16505 N N   . SER D 471 ? 1.0613 0.6114 2.0307 0.0864  -0.2179 -0.0811 471 SER D N   
16506 C CA  . SER D 471 ? 1.0966 0.6367 2.0473 0.0852  -0.2263 -0.0930 471 SER D CA  
16507 C C   . SER D 471 ? 1.1533 0.6663 2.0689 0.0937  -0.2601 -0.0965 471 SER D C   
16508 O O   . SER D 471 ? 1.1486 0.6732 2.0889 0.0970  -0.2820 -0.1067 471 SER D O   
16509 C CB  . SER D 471 ? 1.1318 0.6514 2.0389 0.0777  -0.2006 -0.0935 471 SER D CB  
16510 O OG  . SER D 471 ? 1.1987 0.6881 2.0562 0.0777  -0.1918 -0.0823 471 SER D OG  
16511 N N   . ASP D 472 ? 1.2106 0.6873 2.0700 0.0972  -0.2649 -0.0875 472 ASP D N   
16512 C CA  . ASP D 472 ? 1.2671 0.7111 2.0815 0.1051  -0.2965 -0.0897 472 ASP D CA  
16513 C C   . ASP D 472 ? 1.2470 0.7062 2.1014 0.1152  -0.3272 -0.0890 472 ASP D C   
16514 O O   . ASP D 472 ? 1.3037 0.7351 2.1229 0.1234  -0.3548 -0.0875 472 ASP D O   
16515 C CB  . ASP D 472 ? 1.3340 0.7316 2.0725 0.1053  -0.2908 -0.0792 472 ASP D CB  
16516 C CG  . ASP D 472 ? 1.3504 0.7446 2.0915 0.1077  -0.2845 -0.0643 472 ASP D CG  
16517 O OD1 . ASP D 472 ? 1.3172 0.7477 2.1188 0.1068  -0.2752 -0.0621 472 ASP D OD1 
16518 O OD2 . ASP D 472 ? 1.4124 0.7665 2.0946 0.1106  -0.2899 -0.0550 472 ASP D OD2 
16519 N N   . GLN D 473 ? 1.1725 0.6744 2.0990 0.1148  -0.3230 -0.0902 473 GLN D N   
16520 C CA  . GLN D 473 ? 1.1552 0.6729 2.1228 0.1243  -0.3504 -0.0907 473 GLN D CA  
16521 C C   . GLN D 473 ? 1.1129 0.6759 2.1564 0.1228  -0.3536 -0.1007 473 GLN D C   
16522 O O   . GLN D 473 ? 1.0941 0.6739 2.1784 0.1301  -0.3750 -0.1028 473 GLN D O   
16523 C CB  . GLN D 473 ? 1.1331 0.6503 2.1067 0.1278  -0.3436 -0.0774 473 GLN D CB  
16524 C CG  . GLN D 473 ? 1.1810 0.6512 2.0840 0.1318  -0.3493 -0.0667 473 GLN D CG  
16525 C CD  . GLN D 473 ? 1.1477 0.6183 2.0589 0.1334  -0.3374 -0.0539 473 GLN D CD  
16526 O OE1 . GLN D 473 ? 1.1353 0.6120 2.0725 0.1424  -0.3564 -0.0510 473 GLN D OE1 
16527 N NE2 . GLN D 473 ? 1.1330 0.5980 2.0245 0.1245  -0.3051 -0.0468 473 GLN D NE2 
16528 N N   . LEU D 474 ? 1.0943 0.6753 2.1563 0.1138  -0.3336 -0.1072 474 LEU D N   
16529 C CA  . LEU D 474 ? 1.0511 0.6733 2.1830 0.1111  -0.3330 -0.1154 474 LEU D CA  
16530 C C   . LEU D 474 ? 1.0512 0.6805 2.2099 0.1182  -0.3679 -0.1257 474 LEU D C   
16531 O O   . LEU D 474 ? 1.0029 0.6669 2.2254 0.1182  -0.3712 -0.1299 474 LEU D O   
16532 C CB  . LEU D 474 ? 1.0612 0.6932 2.1989 0.1013  -0.3121 -0.1222 474 LEU D CB  
16533 C CG  . LEU D 474 ? 1.0158 0.6658 2.1711 0.0932  -0.2766 -0.1153 474 LEU D CG  
16534 C CD1 . LEU D 474 ? 0.9542 0.6362 2.1641 0.0939  -0.2695 -0.1087 474 LEU D CD1 
16535 C CD2 . LEU D 474 ? 1.0510 0.6708 2.1471 0.0907  -0.2583 -0.1069 474 LEU D CD2 
16536 N N   . ASP D 475 ? 1.1197 0.7166 2.2306 0.1236  -0.3931 -0.1303 475 ASP D N   
16537 C CA  . ASP D 475 ? 1.1468 0.7478 2.2799 0.1307  -0.4293 -0.1408 475 ASP D CA  
16538 C C   . ASP D 475 ? 1.1234 0.7350 2.2892 0.1406  -0.4489 -0.1362 475 ASP D C   
16539 O O   . ASP D 475 ? 1.1204 0.7564 2.3397 0.1443  -0.4690 -0.1450 475 ASP D O   
16540 C CB  . ASP D 475 ? 1.2364 0.7962 2.3040 0.1350  -0.4536 -0.1459 475 ASP D CB  
16541 C CG  . ASP D 475 ? 1.2998 0.8545 2.3537 0.1286  -0.4530 -0.1590 475 ASP D CG  
16542 O OD1 . ASP D 475 ? 1.2774 0.8499 2.3507 0.1191  -0.4243 -0.1609 475 ASP D OD1 
16543 O OD2 . ASP D 475 ? 1.3821 0.9153 2.4080 0.1335  -0.4829 -0.1680 475 ASP D OD2 
16544 N N   . LYS D 476 ? 1.1011 0.6936 2.2354 0.1449  -0.4433 -0.1230 476 LYS D N   
16545 C CA  . LYS D 476 ? 1.0732 0.6641 2.2225 0.1562  -0.4667 -0.1187 476 LYS D CA  
16546 C C   . LYS D 476 ? 0.9816 0.6181 2.2129 0.1566  -0.4609 -0.1207 476 LYS D C   
16547 O O   . LYS D 476 ? 0.9217 0.5859 2.1871 0.1476  -0.4330 -0.1207 476 LYS D O   
16548 C CB  . LYS D 476 ? 1.1108 0.6690 2.2053 0.1589  -0.4570 -0.1035 476 LYS D CB  
16549 C CG  . LYS D 476 ? 1.1780 0.6877 2.1859 0.1578  -0.4588 -0.0995 476 LYS D CG  
16550 C CD  . LYS D 476 ? 1.2016 0.6808 2.1599 0.1587  -0.4449 -0.0837 476 LYS D CD  
16551 C CE  . LYS D 476 ? 1.2259 0.6950 2.1895 0.1709  -0.4689 -0.0766 476 LYS D CE  
16552 N NZ  . LYS D 476 ? 1.2362 0.6815 2.1635 0.1708  -0.4519 -0.0612 476 LYS D NZ  
16553 N N   . LYS D 477 ? 0.9654 0.6084 2.2271 0.1674  -0.4877 -0.1225 477 LYS D N   
16554 C CA  . LYS D 477 ? 0.9050 0.5892 2.2434 0.1689  -0.4840 -0.1251 477 LYS D CA  
16555 C C   . LYS D 477 ? 0.8711 0.5573 2.2095 0.1690  -0.4606 -0.1123 477 LYS D C   
16556 O O   . LYS D 477 ? 0.8177 0.5372 2.2058 0.1640  -0.4387 -0.1121 477 LYS D O   
16557 C CB  . LYS D 477 ? 0.9289 0.6194 2.3020 0.1806  -0.5222 -0.1335 477 LYS D CB  
16558 C CG  . LYS D 477 ? 0.8840 0.6223 2.3453 0.1800  -0.5205 -0.1423 477 LYS D CG  
16559 C CD  . LYS D 477 ? 0.9006 0.6500 2.4050 0.1904  -0.5580 -0.1534 477 LYS D CD  
16560 C CE  . LYS D 477 ? 0.9276 0.6671 2.4351 0.2039  -0.5759 -0.1476 477 LYS D CE  
16561 N NZ  . LYS D 477 ? 0.9424 0.6933 2.4947 0.2147  -0.6131 -0.1587 477 LYS D NZ  
16562 N N   . ILE D 478 ? 0.8978 0.5465 2.1785 0.1746  -0.4657 -0.1017 478 ILE D N   
16563 C CA  . ILE D 478 ? 0.8672 0.5099 2.1367 0.1744  -0.4443 -0.0890 478 ILE D CA  
16564 C C   . ILE D 478 ? 0.8786 0.4886 2.0781 0.1669  -0.4235 -0.0798 478 ILE D C   
16565 O O   . ILE D 478 ? 0.9271 0.4998 2.0673 0.1696  -0.4383 -0.0780 478 ILE D O   
16566 C CB  . ILE D 478 ? 0.8910 0.5185 2.1602 0.1881  -0.4693 -0.0843 478 ILE D CB  
16567 C CG1 . ILE D 478 ? 0.8576 0.5228 2.2052 0.1949  -0.4841 -0.0936 478 ILE D CG1 
16568 C CG2 . ILE D 478 ? 0.8934 0.5025 2.1338 0.1882  -0.4503 -0.0703 478 ILE D CG2 
16569 C CD1 . ILE D 478 ? 0.8875 0.5382 2.2395 0.2101  -0.5148 -0.0919 478 ILE D CD1 
16570 N N   . ILE D 479 ? 0.8347 0.4580 2.0410 0.1576  -0.3892 -0.0742 479 ILE D N   
16571 C CA  . ILE D 479 ? 0.8586 0.4535 2.0052 0.1504  -0.3668 -0.0651 479 ILE D CA  
16572 C C   . ILE D 479 ? 0.8657 0.4451 1.9961 0.1536  -0.3582 -0.0526 479 ILE D C   
16573 O O   . ILE D 479 ? 0.8284 0.4341 2.0068 0.1551  -0.3511 -0.0516 479 ILE D O   
16574 C CB  . ILE D 479 ? 0.8152 0.4329 1.9777 0.1376  -0.3345 -0.0673 479 ILE D CB  
16575 C CG1 . ILE D 479 ? 0.7960 0.4414 1.9985 0.1341  -0.3400 -0.0803 479 ILE D CG1 
16576 C CG2 . ILE D 479 ? 0.8428 0.4288 1.9411 0.1305  -0.3153 -0.0608 479 ILE D CG2 
16577 C CD1 . ILE D 479 ? 0.8311 0.4554 1.9913 0.1304  -0.3447 -0.0865 479 ILE D CD1 
16578 N N   . THR D 480 ? 0.9147 0.4514 1.9775 0.1538  -0.3571 -0.0433 480 THR D N   
16579 C CA  . THR D 480 ? 0.9220 0.4402 1.9656 0.1558  -0.3478 -0.0309 480 THR D CA  
16580 C C   . THR D 480 ? 0.9387 0.4306 1.9270 0.1457  -0.3203 -0.0224 480 THR D C   
16581 O O   . THR D 480 ? 0.9632 0.4366 1.9098 0.1409  -0.3176 -0.0248 480 THR D O   
16582 C CB  . THR D 480 ? 0.9645 0.4526 1.9849 0.1691  -0.3793 -0.0260 480 THR D CB  
16583 O OG1 . THR D 480 ? 1.0247 0.4641 1.9674 0.1684  -0.3821 -0.0179 480 THR D OG1 
16584 C CG2 . THR D 480 ? 0.9668 0.4685 2.0209 0.1791  -0.4137 -0.0366 480 THR D CG2 
16585 N N   . SER D 481 ? 0.9229 0.4139 1.9133 0.1426  -0.2999 -0.0133 481 SER D N   
16586 C CA  . SER D 481 ? 0.9492 0.4136 1.8900 0.1337  -0.2744 -0.0041 481 SER D CA  
16587 C C   . SER D 481 ? 0.9613 0.4060 1.8900 0.1372  -0.2720 0.0075  481 SER D C   
16588 O O   . SER D 481 ? 0.9496 0.4111 1.9199 0.1446  -0.2828 0.0072  481 SER D O   
16589 C CB  . SER D 481 ? 0.9058 0.3981 1.8702 0.1213  -0.2420 -0.0073 481 SER D CB  
16590 O OG  . SER D 481 ? 0.9272 0.3958 1.8491 0.1127  -0.2169 0.0011  481 SER D OG  
16591 N N   . GLU D 482 ? 0.9936 0.4017 1.8656 0.1317  -0.2573 0.0174  482 GLU D N   
16592 C CA  . GLU D 482 ? 1.0078 0.3942 1.8656 0.1338  -0.2531 0.0289  482 GLU D CA  
16593 C C   . GLU D 482 ? 1.0113 0.3852 1.8397 0.1206  -0.2189 0.0354  482 GLU D C   
16594 O O   . GLU D 482 ? 1.0424 0.3897 1.8194 0.1148  -0.2111 0.0372  482 GLU D O   
16595 C CB  . GLU D 482 ? 1.0691 0.4120 1.8807 0.1448  -0.2824 0.0360  482 GLU D CB  
16596 C CG  . GLU D 482 ? 1.0905 0.4046 1.8818 0.1473  -0.2793 0.0489  482 GLU D CG  
16597 C CD  . GLU D 482 ? 1.1678 0.4269 1.8923 0.1544  -0.3002 0.0593  482 GLU D CD  
16598 O OE1 . GLU D 482 ? 1.2064 0.4381 1.8755 0.1498  -0.2984 0.0607  482 GLU D OE1 
16599 O OE2 . GLU D 482 ? 1.1919 0.4327 1.9158 0.1640  -0.3168 0.0666  482 GLU D OE2 
16600 N N   . ASN D 483 ? 0.9826 0.3756 1.8445 0.1159  -0.1992 0.0381  483 ASN D N   
16601 C CA  . ASN D 483 ? 0.9895 0.3811 1.8391 0.1026  -0.1656 0.0419  483 ASN D CA  
16602 C C   . ASN D 483 ? 1.0035 0.3817 1.8526 0.1016  -0.1559 0.0515  483 ASN D C   
16603 O O   . ASN D 483 ? 0.9840 0.3829 1.8768 0.1075  -0.1633 0.0501  483 ASN D O   
16604 C CB  . ASN D 483 ? 0.9329 0.3710 1.8335 0.0951  -0.1472 0.0325  483 ASN D CB  
16605 C CG  . ASN D 483 ? 0.9238 0.3789 1.8342 0.0966  -0.1578 0.0221  483 ASN D CG  
16606 O OD1 . ASN D 483 ? 0.9289 0.3812 1.8189 0.0887  -0.1429 0.0190  483 ASN D OD1 
16607 N ND2 . ASN D 483 ? 0.9147 0.3870 1.8571 0.1064  -0.1830 0.0161  483 ASN D ND2 
16608 N N   . PHE D 484 ? 1.0496 0.3939 1.8508 0.0935  -0.1375 0.0606  484 PHE D N   
16609 C CA  . PHE D 484 ? 1.0670 0.3879 1.8559 0.0925  -0.1304 0.0711  484 PHE D CA  
16610 C C   . PHE D 484 ? 1.0462 0.3853 1.8569 0.0794  -0.0974 0.0711  484 PHE D C   
16611 O O   . PHE D 484 ? 1.0232 0.3715 1.8286 0.0692  -0.0765 0.0676  484 PHE D O   
16612 C CB  . PHE D 484 ? 1.1330 0.3973 1.8484 0.0928  -0.1349 0.0825  484 PHE D CB  
16613 C CG  . PHE D 484 ? 1.1704 0.4104 1.8578 0.1062  -0.1699 0.0839  484 PHE D CG  
16614 C CD1 . PHE D 484 ? 1.1819 0.4153 1.8850 0.1190  -0.1951 0.0873  484 PHE D CD1 
16615 C CD2 . PHE D 484 ? 1.2010 0.4229 1.8454 0.1063  -0.1781 0.0814  484 PHE D CD2 
16616 C CE1 . PHE D 484 ? 1.2199 0.4310 1.8993 0.1319  -0.2290 0.0883  484 PHE D CE1 
16617 C CE2 . PHE D 484 ? 1.2431 0.4422 1.8615 0.1187  -0.2120 0.0823  484 PHE D CE2 
16618 C CZ  . PHE D 484 ? 1.2534 0.4476 1.8902 0.1316  -0.2380 0.0859  484 PHE D CZ  
16619 N N   . PHE D 485 ? 1.0593 0.4004 1.8923 0.0798  -0.0931 0.0753  485 PHE D N   
16620 C CA  . PHE D 485 ? 1.0387 0.3977 1.8964 0.0682  -0.0649 0.0749  485 PHE D CA  
16621 C C   . PHE D 485 ? 1.0637 0.3932 1.9050 0.0664  -0.0588 0.0849  485 PHE D C   
16622 O O   . PHE D 485 ? 1.0910 0.4145 1.9443 0.0763  -0.0766 0.0873  485 PHE D O   
16623 C CB  . PHE D 485 ? 0.9773 0.3869 1.9012 0.0702  -0.0658 0.0647  485 PHE D CB  
16624 C CG  . PHE D 485 ? 0.9494 0.3877 1.8918 0.0719  -0.0722 0.0550  485 PHE D CG  
16625 C CD1 . PHE D 485 ? 0.9657 0.4043 1.8888 0.0630  -0.0565 0.0526  485 PHE D CD1 
16626 C CD2 . PHE D 485 ? 0.9257 0.3886 1.9040 0.0823  -0.0938 0.0482  485 PHE D CD2 
16627 C CE1 . PHE D 485 ? 0.9487 0.4113 1.8882 0.0646  -0.0627 0.0437  485 PHE D CE1 
16628 C CE2 . PHE D 485 ? 0.9153 0.4028 1.9107 0.0831  -0.0993 0.0396  485 PHE D CE2 
16629 C CZ  . PHE D 485 ? 0.9234 0.4101 1.8989 0.0743  -0.0843 0.0374  485 PHE D CZ  
16630 N N   . ASN D 486 ? 1.0739 0.3858 1.8905 0.0536  -0.0330 0.0903  486 ASN D N   
16631 C CA  . ASN D 486 ? 1.0859 0.3730 1.8924 0.0494  -0.0230 0.0990  486 ASN D CA  
16632 C C   . ASN D 486 ? 1.0315 0.3538 1.8968 0.0496  -0.0196 0.0930  486 ASN D C   
16633 O O   . ASN D 486 ? 0.9996 0.3590 1.9018 0.0425  -0.0044 0.0849  486 ASN D O   
16634 C CB  . ASN D 486 ? 1.1096 0.3755 1.8838 0.0342  0.0064  0.1043  486 ASN D CB  
16635 C CG  . ASN D 486 ? 1.1863 0.4061 1.8924 0.0335  0.0047  0.1127  486 ASN D CG  
16636 O OD1 . ASN D 486 ? 1.2507 0.4298 1.9182 0.0400  -0.0103 0.1229  486 ASN D OD1 
16637 N ND2 . ASN D 486 ? 1.2006 0.4237 1.8888 0.0254  0.0205  0.1089  486 ASN D ND2 
16638 N N   . ILE D 487 ? 1.0400 0.3487 1.9123 0.0579  -0.0335 0.0970  487 ILE D N   
16639 C CA  . ILE D 487 ? 0.9873 0.3229 1.9091 0.0579  -0.0295 0.0918  487 ILE D CA  
16640 C C   . ILE D 487 ? 0.9869 0.3085 1.9016 0.0444  -0.0041 0.0965  487 ILE D C   
16641 O O   . ILE D 487 ? 1.0268 0.3054 1.8984 0.0408  0.0007  0.1071  487 ILE D O   
16642 C CB  . ILE D 487 ? 0.9927 0.3206 1.9279 0.0728  -0.0545 0.0926  487 ILE D CB  
16643 C CG1 . ILE D 487 ? 1.0044 0.3365 1.9374 0.0861  -0.0814 0.0897  487 ILE D CG1 
16644 C CG2 . ILE D 487 ? 0.9379 0.3005 1.9288 0.0737  -0.0509 0.0841  487 ILE D CG2 
16645 C CD1 . ILE D 487 ? 1.0230 0.3439 1.9671 0.1015  -0.1073 0.0910  487 ILE D CD1 
16646 N N   . PRO D 488 ? 0.9368 0.2935 1.8916 0.0354  0.0136  0.0887  488 PRO D N   
16647 C CA  . PRO D 488 ? 0.9454 0.2934 1.9029 0.0232  0.0354  0.0913  488 PRO D CA  
16648 C C   . PRO D 488 ? 0.9574 0.2928 1.9277 0.0286  0.0270  0.0934  488 PRO D C   
16649 O O   . PRO D 488 ? 0.9387 0.2972 1.9429 0.0385  0.0121  0.0868  488 PRO D O   
16650 C CB  . PRO D 488 ? 0.8876 0.2821 1.8889 0.0150  0.0505  0.0806  488 PRO D CB  
16651 C CG  . PRO D 488 ? 0.8694 0.2861 1.8742 0.0201  0.0418  0.0754  488 PRO D CG  
16652 C CD  . PRO D 488 ? 0.8861 0.2910 1.8827 0.0354  0.0147  0.0773  488 PRO D CD  
16653 N N   . ASP D 489 ? 1.0053 0.3049 1.9505 0.0213  0.0384  0.1020  489 ASP D N   
16654 C CA  . ASP D 489 ? 1.0149 0.2958 1.9676 0.0261  0.0310  0.1050  489 ASP D CA  
16655 C C   . ASP D 489 ? 0.9627 0.2839 1.9709 0.0260  0.0334  0.0931  489 ASP D C   
16656 O O   . ASP D 489 ? 0.9832 0.3037 2.0100 0.0355  0.0199  0.0908  489 ASP D O   
16657 C CB  . ASP D 489 ? 1.0544 0.2906 1.9717 0.0162  0.0457  0.1161  489 ASP D CB  
16658 C CG  . ASP D 489 ? 1.1192 0.3042 1.9784 0.0214  0.0352  0.1299  489 ASP D CG  
16659 O OD1 . ASP D 489 ? 1.1250 0.3090 1.9695 0.0326  0.0158  0.1305  489 ASP D OD1 
16660 O OD2 . ASP D 489 ? 1.1751 0.3197 2.0029 0.0141  0.0459  0.1402  489 ASP D OD2 
16661 N N   . ASN D 490 ? 0.9144 0.2707 1.9490 0.0158  0.0498  0.0852  490 ASN D N   
16662 C CA  . ASN D 490 ? 0.8578 0.2513 1.9410 0.0145  0.0528  0.0741  490 ASN D CA  
16663 C C   . ASN D 490 ? 0.8099 0.2454 1.9225 0.0220  0.0425  0.0648  490 ASN D C   
16664 O O   . ASN D 490 ? 0.7629 0.2344 1.9102 0.0171  0.0504  0.0558  490 ASN D O   
16665 C CB  . ASN D 490 ? 0.8368 0.2399 1.9317 -0.0018 0.0767  0.0715  490 ASN D CB  
16666 C CG  . ASN D 490 ? 0.8138 0.2328 1.9027 -0.0096 0.0889  0.0705  490 ASN D CG  
16667 O OD1 . ASN D 490 ? 0.8418 0.2371 1.8933 -0.0100 0.0900  0.0779  490 ASN D OD1 
16668 N ND2 . ASN D 490 ? 0.7695 0.2279 1.8941 -0.0152 0.0971  0.0611  490 ASN D ND2 
16669 N N   . CYS D 491 ? 0.8175 0.2472 1.9158 0.0336  0.0244  0.0671  491 CYS D N   
16670 C CA  . CYS D 491 ? 0.7760 0.2413 1.9045 0.0427  0.0114  0.0586  491 CYS D CA  
16671 C C   . CYS D 491 ? 0.7749 0.2406 1.9243 0.0551  -0.0051 0.0553  491 CYS D C   
16672 O O   . CYS D 491 ? 0.7975 0.2321 1.9255 0.0640  -0.0193 0.0617  491 CYS D O   
16673 C CB  . CYS D 491 ? 0.7872 0.2487 1.8939 0.0486  -0.0003 0.0612  491 CYS D CB  
16674 S SG  . CYS D 491 ? 0.7478 0.2487 1.8932 0.0609  -0.0188 0.0511  491 CYS D SG  
16675 N N   . TRP D 492 ? 0.7437 0.2447 1.9347 0.0555  -0.0027 0.0450  492 TRP D N   
16676 C CA  . TRP D 492 ? 0.7374 0.2449 1.9548 0.0660  -0.0142 0.0393  492 TRP D CA  
16677 C C   . TRP D 492 ? 0.7212 0.2561 1.9620 0.0767  -0.0290 0.0329  492 TRP D C   
16678 O O   . TRP D 492 ? 0.7516 0.2868 2.0099 0.0881  -0.0423 0.0292  492 TRP D O   
16679 C CB  . TRP D 492 ? 0.7085 0.2369 1.9558 0.0592  -0.0012 0.0311  492 TRP D CB  
16680 C CG  . TRP D 492 ? 0.7216 0.2329 1.9540 0.0457  0.0162  0.0351  492 TRP D CG  
16681 C CD1 . TRP D 492 ? 0.6977 0.2308 1.9458 0.0335  0.0325  0.0301  492 TRP D CD1 
16682 C CD2 . TRP D 492 ? 0.7743 0.2424 1.9746 0.0429  0.0186  0.0450  492 TRP D CD2 
16683 N NE1 . TRP D 492 ? 0.7331 0.2413 1.9636 0.0230  0.0453  0.0354  492 TRP D NE1 
16684 C CE2 . TRP D 492 ? 0.7806 0.2481 1.9809 0.0281  0.0381  0.0448  492 TRP D CE2 
16685 C CE3 . TRP D 492 ? 0.8198 0.2490 1.9910 0.0513  0.0059  0.0541  492 TRP D CE3 
16686 C CZ2 . TRP D 492 ? 0.8127 0.2423 1.9861 0.0208  0.0468  0.0533  492 TRP D CZ2 
16687 C CZ3 . TRP D 492 ? 0.8657 0.2556 2.0075 0.0445  0.0140  0.0634  492 TRP D CZ3 
16688 C CH2 . TRP D 492 ? 0.8590 0.2494 2.0024 0.0291  0.0350  0.0629  492 TRP D CH2 
16689 N N   . VAL D 493 ? 0.6875 0.2460 1.9318 0.0728  -0.0257 0.0307  493 VAL D N   
16690 C CA  . VAL D 493 ? 0.6643 0.2490 1.9313 0.0815  -0.0385 0.0247  493 VAL D CA  
16691 C C   . VAL D 493 ? 0.6591 0.2519 1.9120 0.0771  -0.0368 0.0266  493 VAL D C   
16692 O O   . VAL D 493 ? 0.6493 0.2436 1.8904 0.0658  -0.0213 0.0286  493 VAL D O   
16693 C CB  . VAL D 493 ? 0.6279 0.2500 1.9385 0.0819  -0.0337 0.0139  493 VAL D CB  
16694 C CG1 . VAL D 493 ? 0.6015 0.2481 1.9217 0.0692  -0.0156 0.0107  493 VAL D CG1 
16695 C CG2 . VAL D 493 ? 0.6151 0.2609 1.9518 0.0920  -0.0476 0.0076  493 VAL D CG2 
16696 N N   . VAL D 494 ? 0.6664 0.2643 1.9221 0.0863  -0.0535 0.0251  494 VAL D N   
16697 C CA  . VAL D 494 ? 0.6706 0.2742 1.9127 0.0833  -0.0543 0.0261  494 VAL D CA  
16698 C C   . VAL D 494 ? 0.6505 0.2876 1.9276 0.0896  -0.0643 0.0177  494 VAL D C   
16699 O O   . VAL D 494 ? 0.6451 0.2875 1.9440 0.0997  -0.0775 0.0138  494 VAL D O   
16700 C CB  . VAL D 494 ? 0.7162 0.2820 1.9130 0.0868  -0.0652 0.0346  494 VAL D CB  
16701 C CG1 . VAL D 494 ? 0.7318 0.2830 1.9282 0.1013  -0.0899 0.0353  494 VAL D CG1 
16702 C CG2 . VAL D 494 ? 0.7225 0.2947 1.9041 0.0820  -0.0626 0.0343  494 VAL D CG2 
16703 N N   . ASN D 495 ? 0.6456 0.3048 1.9295 0.0832  -0.0569 0.0147  495 ASN D N   
16704 C CA  . ASN D 495 ? 0.6197 0.3066 1.9311 0.0880  -0.0664 0.0080  495 ASN D CA  
16705 C C   . ASN D 495 ? 0.6362 0.3093 1.9202 0.0888  -0.0753 0.0107  495 ASN D C   
16706 O O   . ASN D 495 ? 0.6539 0.3252 1.9199 0.0801  -0.0634 0.0127  495 ASN D O   
16707 C CB  . ASN D 495 ? 0.5816 0.3043 1.9240 0.0805  -0.0518 0.0021  495 ASN D CB  
16708 C CG  . ASN D 495 ? 0.5687 0.3180 1.9372 0.0836  -0.0596 -0.0039 495 ASN D CG  
16709 O OD1 . ASN D 495 ? 0.5922 0.3335 1.9490 0.0879  -0.0724 -0.0035 495 ASN D OD1 
16710 N ND2 . ASN D 495 ? 0.5350 0.3151 1.9377 0.0812  -0.0519 -0.0097 495 ASN D ND2 
16711 N N   . ALA D 496 ? 0.6395 0.3018 1.9201 0.0996  -0.0966 0.0103  496 ALA D N   
16712 C CA  . ALA D 496 ? 0.6610 0.3065 1.9123 0.1017  -0.1085 0.0124  496 ALA D CA  
16713 C C   . ALA D 496 ? 0.6284 0.3040 1.9104 0.1039  -0.1165 0.0042  496 ALA D C   
16714 O O   . ALA D 496 ? 0.6386 0.3261 1.9485 0.1131  -0.1324 -0.0008 496 ALA D O   
16715 C CB  . ALA D 496 ? 0.7104 0.3226 1.9366 0.1123  -0.1291 0.0174  496 ALA D CB  
16716 N N   . SER D 497 ? 0.5916 0.2792 1.8702 0.0956  -0.1055 0.0025  497 SER D N   
16717 C CA  . SER D 497 ? 0.5547 0.2703 1.8631 0.0965  -0.1116 -0.0051 497 SER D CA  
16718 C C   . SER D 497 ? 0.5709 0.2736 1.8509 0.0951  -0.1178 -0.0053 497 SER D C   
16719 O O   . SER D 497 ? 0.6029 0.2776 1.8404 0.0917  -0.1131 0.0003  497 SER D O   
16720 C CB  . SER D 497 ? 0.5073 0.2558 1.8494 0.0890  -0.0939 -0.0088 497 SER D CB  
16721 O OG  . SER D 497 ? 0.5131 0.2587 1.8364 0.0788  -0.0763 -0.0060 497 SER D OG  
16722 N N   . ALA D 498 ? 0.5596 0.2811 1.8629 0.0980  -0.1292 -0.0122 498 ALA D N   
16723 C CA  . ALA D 498 ? 0.5812 0.2937 1.8625 0.0966  -0.1358 -0.0145 498 ALA D CA  
16724 C C   . ALA D 498 ? 0.5564 0.3021 1.8789 0.0954  -0.1379 -0.0229 498 ALA D C   
16725 O O   . ALA D 498 ? 0.5510 0.3179 1.9128 0.1003  -0.1460 -0.0273 498 ALA D O   
16726 C CB  . ALA D 498 ? 0.6212 0.3039 1.8715 0.1057  -0.1595 -0.0130 498 ALA D CB  
16727 N N   . GLY D 499 ? 0.5476 0.2973 1.8622 0.0887  -0.1300 -0.0253 499 GLY D N   
16728 C CA  . GLY D 499 ? 0.5171 0.2972 1.8705 0.0862  -0.1292 -0.0323 499 GLY D CA  
16729 C C   . GLY D 499 ? 0.5373 0.3110 1.8731 0.0828  -0.1313 -0.0363 499 GLY D C   
16730 O O   . GLY D 499 ? 0.5730 0.3218 1.8666 0.0801  -0.1264 -0.0333 499 GLY D O   
16731 N N   . ILE D 500 ? 0.5122 0.3086 1.8818 0.0826  -0.1377 -0.0435 500 ILE D N   
16732 C CA  . ILE D 500 ? 0.5116 0.3058 1.8727 0.0795  -0.1405 -0.0489 500 ILE D CA  
16733 C C   . ILE D 500 ? 0.4844 0.3117 1.8942 0.0759  -0.1367 -0.0544 500 ILE D C   
16734 O O   . ILE D 500 ? 0.4596 0.3066 1.9060 0.0788  -0.1410 -0.0557 500 ILE D O   
16735 C CB  . ILE D 500 ? 0.5383 0.3104 1.8750 0.0868  -0.1652 -0.0527 500 ILE D CB  
16736 C CG1 . ILE D 500 ? 0.5584 0.3160 1.8665 0.0833  -0.1659 -0.0571 500 ILE D CG1 
16737 C CG2 . ILE D 500 ? 0.5281 0.3194 1.9066 0.0931  -0.1846 -0.0591 500 ILE D CG2 
16738 C CD1 . ILE D 500 ? 0.6026 0.3338 1.8780 0.0902  -0.1903 -0.0606 500 ILE D CD1 
16739 N N   . SER D 501 ? 0.4886 0.3207 1.8983 0.0695  -0.1273 -0.0573 501 SER D N   
16740 C CA  . SER D 501 ? 0.4697 0.3293 1.9216 0.0653  -0.1233 -0.0618 501 SER D CA  
16741 C C   . SER D 501 ? 0.4789 0.3417 1.9464 0.0687  -0.1434 -0.0705 501 SER D C   
16742 O O   . SER D 501 ? 0.5076 0.3494 1.9454 0.0713  -0.1562 -0.0743 501 SER D O   
16743 C CB  . SER D 501 ? 0.4722 0.3348 1.9191 0.0576  -0.1051 -0.0608 501 SER D CB  
16744 O OG  . SER D 501 ? 0.4866 0.3435 1.9159 0.0543  -0.0879 -0.0537 501 SER D OG  
16745 N N   . VAL D 502 ? 0.4571 0.3462 1.9713 0.0679  -0.1458 -0.0742 502 VAL D N   
16746 C CA  . VAL D 502 ? 0.4826 0.3786 2.0199 0.0700  -0.1639 -0.0832 502 VAL D CA  
16747 C C   . VAL D 502 ? 0.4647 0.3811 2.0340 0.0623  -0.1533 -0.0862 502 VAL D C   
16748 O O   . VAL D 502 ? 0.4797 0.4109 2.0647 0.0570  -0.1347 -0.0811 502 VAL D O   
16749 C CB  . VAL D 502 ? 0.4612 0.3687 2.0289 0.0770  -0.1797 -0.0862 502 VAL D CB  
16750 C CG1 . VAL D 502 ? 0.4683 0.3812 2.0589 0.0794  -0.2007 -0.0964 502 VAL D CG1 
16751 C CG2 . VAL D 502 ? 0.4846 0.3718 2.0231 0.0850  -0.1897 -0.0821 502 VAL D CG2 
16752 N N   . ARG D 503 ? 0.4646 0.3806 2.0429 0.0616  -0.1657 -0.0946 503 ARG D N   
16753 C CA  . ARG D 503 ? 0.4442 0.3769 2.0522 0.0542  -0.1562 -0.0973 503 ARG D CA  
16754 C C   . ARG D 503 ? 0.4207 0.3665 2.0662 0.0550  -0.1730 -0.1065 503 ARG D C   
16755 O O   . ARG D 503 ? 0.4294 0.3628 2.0637 0.0603  -0.1940 -0.1133 503 ARG D O   
16756 C CB  . ARG D 503 ? 0.4695 0.3877 2.0514 0.0498  -0.1493 -0.0991 503 ARG D CB  
16757 C CG  . ARG D 503 ? 0.4712 0.4045 2.0851 0.0428  -0.1421 -0.1023 503 ARG D CG  
16758 C CD  . ARG D 503 ? 0.4978 0.4151 2.0903 0.0403  -0.1428 -0.1084 503 ARG D CD  
16759 N NE  . ARG D 503 ? 0.5291 0.4351 2.0906 0.0385  -0.1255 -0.1022 503 ARG D NE  
16760 C CZ  . ARG D 503 ? 0.5414 0.4599 2.1151 0.0345  -0.1067 -0.0940 503 ARG D CZ  
16761 N NH1 . ARG D 503 ? 0.5094 0.4501 2.1235 0.0308  -0.1017 -0.0915 503 ARG D NH1 
16762 N NH2 . ARG D 503 ? 0.5475 0.4556 2.0929 0.0339  -0.0932 -0.0885 503 ARG D NH2 
16763 N N   . TYR D 504 ? 0.3828 0.3528 2.0719 0.0494  -0.1632 -0.1063 504 TYR D N   
16764 C CA  . TYR D 504 ? 0.3799 0.3652 2.1108 0.0476  -0.1743 -0.1149 504 TYR D CA  
16765 C C   . TYR D 504 ? 0.3507 0.3480 2.1044 0.0382  -0.1583 -0.1136 504 TYR D C   
16766 O O   . TYR D 504 ? 0.3332 0.3456 2.1051 0.0339  -0.1408 -0.1066 504 TYR D O   
16767 C CB  . TYR D 504 ? 0.3714 0.3760 2.1391 0.0511  -0.1789 -0.1158 504 TYR D CB  
16768 C CG  . TYR D 504 ? 0.3830 0.4043 2.1978 0.0493  -0.1912 -0.1258 504 TYR D CG  
16769 C CD1 . TYR D 504 ? 0.3495 0.3916 2.2048 0.0407  -0.1775 -0.1258 504 TYR D CD1 
16770 C CD2 . TYR D 504 ? 0.4091 0.4247 2.2279 0.0560  -0.2172 -0.1351 504 TYR D CD2 
16771 C CE1 . TYR D 504 ? 0.3386 0.3962 2.2391 0.0383  -0.1876 -0.1350 504 TYR D CE1 
16772 C CE2 . TYR D 504 ? 0.4016 0.4336 2.2666 0.0542  -0.2292 -0.1451 504 TYR D CE2 
16773 C CZ  . TYR D 504 ? 0.3745 0.4278 2.2811 0.0450  -0.2136 -0.1451 504 TYR D CZ  
16774 O OH  . TYR D 504 ? 0.4040 0.4734 2.3580 0.0425  -0.2247 -0.1553 504 TYR D OH  
16775 N N   . GLY D 505 ? 0.3381 0.3274 2.0893 0.0351  -0.1644 -0.1203 505 GLY D N   
16776 C CA  . GLY D 505 ? 0.3188 0.3151 2.0853 0.0268  -0.1485 -0.1177 505 GLY D CA  
16777 C C   . GLY D 505 ? 0.3138 0.3061 2.0560 0.0251  -0.1282 -0.1067 505 GLY D C   
16778 O O   . GLY D 505 ? 0.3362 0.3108 2.0385 0.0287  -0.1277 -0.1048 505 GLY D O   
16779 N N   . LYS D 506 ? 0.2872 0.2957 2.0534 0.0196  -0.1114 -0.0994 506 LYS D N   
16780 C CA  . LYS D 506 ? 0.2653 0.2710 2.0129 0.0172  -0.0933 -0.0897 506 LYS D CA  
16781 C C   . LYS D 506 ? 0.2565 0.2656 1.9922 0.0208  -0.0871 -0.0826 506 LYS D C   
16782 O O   . LYS D 506 ? 0.2596 0.2669 1.9794 0.0194  -0.0734 -0.0749 506 LYS D O   
16783 C CB  . LYS D 506 ? 0.2369 0.2556 2.0119 0.0094  -0.0789 -0.0844 506 LYS D CB  
16784 C CG  . LYS D 506 ? 0.2389 0.2527 2.0240 0.0047  -0.0799 -0.0887 506 LYS D CG  
16785 C CD  . LYS D 506 ? 0.2304 0.2548 2.0380 -0.0025 -0.0644 -0.0806 506 LYS D CD  
16786 C CE  . LYS D 506 ? 0.2461 0.2695 2.0765 -0.0081 -0.0659 -0.0848 506 LYS D CE  
16787 N NZ  . LYS D 506 ? 0.2376 0.2706 2.0922 -0.0154 -0.0524 -0.0766 506 LYS D NZ  
16788 N N   . PHE D 507 ? 0.2614 0.2756 2.0067 0.0256  -0.0978 -0.0859 507 PHE D N   
16789 C CA  . PHE D 507 ? 0.2646 0.2833 2.0043 0.0291  -0.0925 -0.0804 507 PHE D CA  
16790 C C   . PHE D 507 ? 0.2867 0.2857 1.9880 0.0362  -0.1017 -0.0807 507 PHE D C   
16791 O O   . PHE D 507 ? 0.2953 0.2852 1.9902 0.0415  -0.1195 -0.0872 507 PHE D O   
16792 C CB  . PHE D 507 ? 0.2543 0.2916 2.0331 0.0300  -0.0977 -0.0843 507 PHE D CB  
16793 C CG  . PHE D 507 ? 0.2367 0.2816 2.0189 0.0338  -0.0929 -0.0806 507 PHE D CG  
16794 C CD1 . PHE D 507 ? 0.2484 0.2837 2.0154 0.0422  -0.1060 -0.0830 507 PHE D CD1 
16795 C CD2 . PHE D 507 ? 0.2152 0.2762 2.0166 0.0291  -0.0760 -0.0753 507 PHE D CD2 
16796 C CE1 . PHE D 507 ? 0.2384 0.2805 2.0114 0.0460  -0.1019 -0.0806 507 PHE D CE1 
16797 C CE2 . PHE D 507 ? 0.2059 0.2734 2.0107 0.0326  -0.0713 -0.0732 507 PHE D CE2 
16798 C CZ  . PHE D 507 ? 0.2181 0.2767 2.0105 0.0411  -0.0842 -0.0763 507 PHE D CZ  
16799 N N   . THR D 508 ? 0.3012 0.2929 1.9765 0.0361  -0.0897 -0.0733 508 THR D N   
16800 C CA  . THR D 508 ? 0.3260 0.2982 1.9641 0.0418  -0.0952 -0.0720 508 THR D CA  
16801 C C   . THR D 508 ? 0.2866 0.2640 1.9243 0.0439  -0.0878 -0.0661 508 THR D C   
16802 O O   . THR D 508 ? 0.2480 0.2399 1.9022 0.0398  -0.0740 -0.0614 508 THR D O   
16803 C CB  . THR D 508 ? 0.3691 0.3250 1.9744 0.0392  -0.0870 -0.0698 508 THR D CB  
16804 O OG1 . THR D 508 ? 0.3768 0.3474 2.0013 0.0328  -0.0712 -0.0653 508 THR D OG1 
16805 C CG2 . THR D 508 ? 0.4071 0.3507 2.0022 0.0394  -0.0980 -0.0775 508 THR D CG2 
16806 N N   . PHE D 509 ? 0.3009 0.2647 1.9187 0.0506  -0.0984 -0.0665 509 PHE D N   
16807 C CA  . PHE D 509 ? 0.2927 0.2607 1.9145 0.0541  -0.0955 -0.0629 509 PHE D CA  
16808 C C   . PHE D 509 ? 0.3361 0.2798 1.9221 0.0608  -0.1065 -0.0621 509 PHE D C   
16809 O O   . PHE D 509 ? 0.3492 0.2756 1.9107 0.0620  -0.1158 -0.0648 509 PHE D O   
16810 C CB  . PHE D 509 ? 0.2823 0.2710 1.9464 0.0560  -0.1015 -0.0677 509 PHE D CB  
16811 C CG  . PHE D 509 ? 0.2988 0.2830 1.9711 0.0632  -0.1240 -0.0752 509 PHE D CG  
16812 C CD1 . PHE D 509 ? 0.3045 0.2885 1.9856 0.0619  -0.1354 -0.0818 509 PHE D CD1 
16813 C CD2 . PHE D 509 ? 0.3048 0.2845 1.9772 0.0713  -0.1347 -0.0760 509 PHE D CD2 
16814 C CE1 . PHE D 509 ? 0.3286 0.3089 2.0184 0.0685  -0.1578 -0.0893 509 PHE D CE1 
16815 C CE2 . PHE D 509 ? 0.3245 0.3005 2.0066 0.0785  -0.1571 -0.0830 509 PHE D CE2 
16816 C CZ  . PHE D 509 ? 0.3351 0.3116 2.0257 0.0770  -0.1691 -0.0897 509 PHE D CZ  
16817 N N   . LYS D 510 ? 0.3571 0.2990 1.9405 0.0650  -0.1056 -0.0588 510 LYS D N   
16818 C CA  . LYS D 510 ? 0.3902 0.3069 1.9374 0.0707  -0.1135 -0.0561 510 LYS D CA  
16819 C C   . LYS D 510 ? 0.4099 0.3264 1.9708 0.0795  -0.1294 -0.0588 510 LYS D C   
16820 O O   . LYS D 510 ? 0.4163 0.3538 2.0142 0.0807  -0.1279 -0.0614 510 LYS D O   
16821 C CB  . LYS D 510 ? 0.3835 0.2933 1.9087 0.0664  -0.0956 -0.0487 510 LYS D CB  
16822 C CG  . LYS D 510 ? 0.3958 0.2972 1.8987 0.0600  -0.0858 -0.0471 510 LYS D CG  
16823 C CD  . LYS D 510 ? 0.4075 0.2981 1.8851 0.0561  -0.0701 -0.0406 510 LYS D CD  
16824 C CE  . LYS D 510 ? 0.4346 0.3022 1.8740 0.0541  -0.0676 -0.0397 510 LYS D CE  
16825 N NZ  . LYS D 510 ? 0.4670 0.3090 1.8753 0.0604  -0.0816 -0.0394 510 LYS D NZ  
16826 N N   . ILE D 511 ? 0.4256 0.3171 1.9557 0.0860  -0.1452 -0.0585 511 ILE D N   
16827 C CA  . ILE D 511 ? 0.4198 0.3058 1.9567 0.0956  -0.1618 -0.0600 511 ILE D CA  
16828 C C   . ILE D 511 ? 0.4495 0.3065 1.9425 0.0984  -0.1610 -0.0525 511 ILE D C   
16829 O O   . ILE D 511 ? 0.4671 0.3034 1.9207 0.0950  -0.1572 -0.0490 511 ILE D O   
16830 C CB  . ILE D 511 ? 0.4263 0.3089 1.9711 0.1018  -0.1867 -0.0673 511 ILE D CB  
16831 C CG1 . ILE D 511 ? 0.4581 0.3126 1.9562 0.1017  -0.1957 -0.0665 511 ILE D CG1 
16832 C CG2 . ILE D 511 ? 0.3965 0.3088 1.9894 0.0983  -0.1864 -0.0749 511 ILE D CG2 
16833 C CD1 . ILE D 511 ? 0.4835 0.3296 1.9820 0.1088  -0.2232 -0.0736 511 ILE D CD1 
16834 N N   . HIS D 512 ? 0.4565 0.3116 1.9575 0.1047  -0.1644 -0.0507 512 HIS D N   
16835 C CA  . HIS D 512 ? 0.4750 0.3090 1.9434 0.1046  -0.1558 -0.0428 512 HIS D CA  
16836 C C   . HIS D 512 ? 0.4819 0.3131 1.9635 0.1133  -0.1640 -0.0425 512 HIS D C   
16837 O O   . HIS D 512 ? 0.4912 0.3416 2.0123 0.1187  -0.1727 -0.0486 512 HIS D O   
16838 C CB  . HIS D 512 ? 0.4482 0.2955 1.9208 0.0948  -0.1302 -0.0395 512 HIS D CB  
16839 C CG  . HIS D 512 ? 0.4156 0.2957 1.9350 0.0927  -0.1217 -0.0438 512 HIS D CG  
16840 N ND1 . HIS D 512 ? 0.4073 0.2975 1.9518 0.0976  -0.1220 -0.0455 512 HIS D ND1 
16841 C CD2 . HIS D 512 ? 0.3920 0.2956 1.9364 0.0861  -0.1123 -0.0468 512 HIS D CD2 
16842 C CE1 . HIS D 512 ? 0.3719 0.2905 1.9530 0.0935  -0.1115 -0.0493 512 HIS D CE1 
16843 N NE2 . HIS D 512 ? 0.3667 0.2933 1.9479 0.0865  -0.1060 -0.0496 512 HIS D NE2 
16844 N N   . ASP D 513 ? 0.4973 0.3047 1.9472 0.1142  -0.1596 -0.0354 513 ASP D N   
16845 C CA  . ASP D 513 ? 0.5037 0.3043 1.9620 0.1226  -0.1669 -0.0344 513 ASP D CA  
16846 C C   . ASP D 513 ? 0.5089 0.2910 1.9376 0.1181  -0.1512 -0.0265 513 ASP D C   
16847 O O   . ASP D 513 ? 0.5129 0.2800 1.9074 0.1111  -0.1415 -0.0215 513 ASP D O   
16848 C CB  . ASP D 513 ? 0.5431 0.3224 1.9882 0.1336  -0.1941 -0.0351 513 ASP D CB  
16849 C CG  . ASP D 513 ? 0.5497 0.3300 2.0203 0.1446  -0.2070 -0.0374 513 ASP D CG  
16850 O OD1 . ASP D 513 ? 0.5225 0.3268 2.0300 0.1437  -0.1950 -0.0412 513 ASP D OD1 
16851 O OD2 . ASP D 513 ? 0.5926 0.3485 2.0445 0.1541  -0.2288 -0.0355 513 ASP D OD2 
16852 N N   . GLN D 514 ? 0.5108 0.2933 1.9539 0.1226  -0.1493 -0.0262 514 GLN D N   
16853 C CA  . GLN D 514 ? 0.5070 0.2780 1.9327 0.1177  -0.1329 -0.0204 514 GLN D CA  
16854 C C   . GLN D 514 ? 0.5223 0.2783 1.9508 0.1269  -0.1416 -0.0193 514 GLN D C   
16855 O O   . GLN D 514 ? 0.5019 0.2760 1.9682 0.1336  -0.1475 -0.0258 514 GLN D O   
16856 C CB  . GLN D 514 ? 0.4714 0.2743 1.9289 0.1101  -0.1134 -0.0245 514 GLN D CB  
16857 C CG  . GLN D 514 ? 0.4760 0.2737 1.9241 0.1043  -0.0958 -0.0208 514 GLN D CG  
16858 C CD  . GLN D 514 ? 0.4520 0.2809 1.9321 0.0983  -0.0798 -0.0255 514 GLN D CD  
16859 O OE1 . GLN D 514 ? 0.4523 0.2928 1.9303 0.0890  -0.0666 -0.0245 514 GLN D OE1 
16860 N NE2 . GLN D 514 ? 0.4421 0.2843 1.9524 0.1039  -0.0814 -0.0310 514 GLN D NE2 
16861 N N   . LYS D 515 ? 0.5528 0.2761 1.9427 0.1267  -0.1407 -0.0113 515 LYS D N   
16862 C CA  . LYS D 515 ? 0.5840 0.2898 1.9739 0.1346  -0.1473 -0.0093 515 LYS D CA  
16863 C C   . LYS D 515 ? 0.5725 0.2686 1.9476 0.1266  -0.1272 -0.0046 515 LYS D C   
16864 O O   . LYS D 515 ? 0.5963 0.2774 1.9385 0.1176  -0.1157 0.0016  515 LYS D O   
16865 C CB  . LYS D 515 ? 0.6464 0.3165 2.0033 0.1438  -0.1696 -0.0035 515 LYS D CB  
16866 C CG  . LYS D 515 ? 0.6662 0.3429 2.0383 0.1534  -0.1939 -0.0087 515 LYS D CG  
16867 C CD  . LYS D 515 ? 0.6525 0.3583 2.0803 0.1620  -0.2022 -0.0186 515 LYS D CD  
16868 C CE  . LYS D 515 ? 0.6787 0.3901 2.1225 0.1711  -0.2270 -0.0240 515 LYS D CE  
16869 N NZ  . LYS D 515 ? 0.6570 0.4100 2.1494 0.1681  -0.2215 -0.0342 515 LYS D NZ  
16870 N N   . ILE D 516 ? 0.5425 0.2468 1.9430 0.1298  -0.1229 -0.0083 516 ILE D N   
16871 C CA  . ILE D 516 ? 0.5269 0.2221 1.9173 0.1230  -0.1060 -0.0053 516 ILE D CA  
16872 C C   . ILE D 516 ? 0.5635 0.2273 1.9404 0.1317  -0.1168 -0.0012 516 ILE D C   
16873 O O   . ILE D 516 ? 0.5542 0.2239 1.9587 0.1421  -0.1276 -0.0066 516 ILE D O   
16874 C CB  . ILE D 516 ? 0.4774 0.2066 1.9053 0.1185  -0.0908 -0.0135 516 ILE D CB  
16875 C CG1 . ILE D 516 ? 0.4441 0.2010 1.8824 0.1100  -0.0811 -0.0161 516 ILE D CG1 
16876 C CG2 . ILE D 516 ? 0.4777 0.1972 1.8975 0.1123  -0.0755 -0.0117 516 ILE D CG2 
16877 C CD1 . ILE D 516 ? 0.4082 0.1951 1.8754 0.1038  -0.0647 -0.0224 516 ILE D CD1 
16878 N N   . ILE D 517 ? 0.6049 0.2349 1.9398 0.1272  -0.1131 0.0084  517 ILE D N   
16879 C CA  . ILE D 517 ? 0.6611 0.2531 1.9721 0.1348  -0.1250 0.0152  517 ILE D CA  
16880 C C   . ILE D 517 ? 0.6837 0.2558 1.9750 0.1260  -0.1078 0.0206  517 ILE D C   
16881 O O   . ILE D 517 ? 0.6813 0.2485 1.9492 0.1142  -0.0926 0.0251  517 ILE D O   
16882 C CB  . ILE D 517 ? 0.7025 0.2646 1.9732 0.1387  -0.1411 0.0234  517 ILE D CB  
16883 C CG1 . ILE D 517 ? 0.6888 0.2719 1.9766 0.1445  -0.1563 0.0176  517 ILE D CG1 
16884 C CG2 . ILE D 517 ? 0.7515 0.2734 1.9993 0.1487  -0.1572 0.0307  517 ILE D CG2 
16885 C CD1 . ILE D 517 ? 0.7281 0.2847 1.9719 0.1450  -0.1682 0.0246  517 ILE D CD1 
16886 N N   . TYR D 518 ? 0.7048 0.2635 2.0056 0.1322  -0.1110 0.0200  518 TYR D N   
16887 C CA  . TYR D 518 ? 0.7176 0.2621 2.0090 0.1239  -0.0946 0.0226  518 TYR D CA  
16888 C C   . TYR D 518 ? 0.7743 0.2702 2.0225 0.1252  -0.1004 0.0347  518 TYR D C   
16889 O O   . TYR D 518 ? 0.8131 0.2865 2.0433 0.1353  -0.1199 0.0400  518 TYR D O   
16890 C CB  . TYR D 518 ? 0.7062 0.2667 2.0362 0.1292  -0.0928 0.0132  518 TYR D CB  
16891 C CG  . TYR D 518 ? 0.6592 0.2654 2.0300 0.1271  -0.0847 0.0015  518 TYR D CG  
16892 C CD1 . TYR D 518 ? 0.6384 0.2648 2.0152 0.1145  -0.0647 -0.0018 518 TYR D CD1 
16893 C CD2 . TYR D 518 ? 0.6517 0.2803 2.0552 0.1378  -0.0970 -0.0063 518 TYR D CD2 
16894 C CE1 . TYR D 518 ? 0.6091 0.2742 2.0188 0.1123  -0.0574 -0.0113 518 TYR D CE1 
16895 C CE2 . TYR D 518 ? 0.6213 0.2896 2.0598 0.1351  -0.0881 -0.0163 518 TYR D CE2 
16896 C CZ  . TYR D 518 ? 0.6035 0.2892 2.0434 0.1223  -0.0682 -0.0184 518 TYR D CZ  
16897 O OH  . TYR D 518 ? 0.5862 0.3086 2.0565 0.1193  -0.0595 -0.0271 518 TYR D OH  
16898 N N   . ARG D 519 ? 0.7877 0.2665 2.0191 0.1147  -0.0835 0.0391  519 ARG D N   
16899 C CA  . ARG D 519 ? 0.8317 0.2637 2.0283 0.1157  -0.0868 0.0498  519 ARG D CA  
16900 C C   . ARG D 519 ? 0.8221 0.2482 2.0427 0.1224  -0.0897 0.0453  519 ARG D C   
16901 O O   . ARG D 519 ? 0.7862 0.2346 2.0344 0.1167  -0.0759 0.0369  519 ARG D O   
16902 C CB  . ARG D 519 ? 0.8426 0.2543 2.0069 0.1001  -0.0664 0.0576  519 ARG D CB  
16903 C CG  . ARG D 519 ? 0.8931 0.2534 2.0198 0.1016  -0.0705 0.0695  519 ARG D CG  
16904 C CD  . ARG D 519 ? 0.9062 0.2470 2.0052 0.0854  -0.0484 0.0765  519 ARG D CD  
16905 N NE  . ARG D 519 ? 0.9092 0.2537 1.9834 0.0762  -0.0387 0.0802  519 ARG D NE  
16906 C CZ  . ARG D 519 ? 0.9447 0.2656 1.9795 0.0790  -0.0476 0.0886  519 ARG D CZ  
16907 N NH1 . ARG D 519 ? 0.9779 0.2636 1.9871 0.0906  -0.0678 0.0964  519 ARG D NH1 
16908 N NH2 . ARG D 519 ? 0.9325 0.2645 1.9530 0.0699  -0.0359 0.0887  519 ARG D NH2 
16909 N N   . GLY D 520 ? 0.8594 0.2538 2.0680 0.1348  -0.1083 0.0508  520 GLY D N   
16910 C CA  . GLY D 520 ? 0.8650 0.2513 2.0968 0.1429  -0.1129 0.0463  520 GLY D CA  
16911 C C   . GLY D 520 ? 0.8128 0.2437 2.0978 0.1479  -0.1115 0.0305  520 GLY D C   
16912 O O   . GLY D 520 ? 0.7909 0.2513 2.0961 0.1527  -0.1189 0.0247  520 GLY D O   
16913 N N   . ASP D 521 ? 0.7982 0.2328 2.1047 0.1458  -0.1009 0.0236  521 ASP D N   
16914 C CA  . ASP D 521 ? 0.7599 0.2303 2.1139 0.1519  -0.0998 0.0086  521 ASP D CA  
16915 C C   . ASP D 521 ? 0.7200 0.2126 2.0875 0.1385  -0.0770 0.0008  521 ASP D C   
16916 O O   . ASP D 521 ? 0.6937 0.2041 2.0931 0.1417  -0.0726 -0.0109 521 ASP D O   
16917 C CB  . ASP D 521 ? 0.7871 0.2401 2.1592 0.1666  -0.1134 0.0049  521 ASP D CB  
16918 C CG  . ASP D 521 ? 0.8218 0.2391 2.1770 0.1628  -0.1067 0.0094  521 ASP D CG  
16919 O OD1 . ASP D 521 ? 0.8391 0.2358 2.1596 0.1503  -0.0963 0.0193  521 ASP D OD1 
16920 O OD2 . ASP D 521 ? 0.8364 0.2486 2.2152 0.1717  -0.1106 0.0021  521 ASP D OD2 
16921 N N   . TRP D 522 ? 0.7079 0.2008 2.0519 0.1238  -0.0630 0.0066  522 TRP D N   
16922 C CA  . TRP D 522 ? 0.6798 0.1904 2.0337 0.1106  -0.0432 0.0003  522 TRP D CA  
16923 C C   . TRP D 522 ? 0.6413 0.1975 2.0309 0.1113  -0.0386 -0.0124 522 TRP D C   
16924 O O   . TRP D 522 ? 0.6135 0.1864 2.0209 0.1057  -0.0267 -0.0215 522 TRP D O   
16925 C CB  . TRP D 522 ? 0.6839 0.1857 2.0077 0.0958  -0.0308 0.0093  522 TRP D CB  
16926 C CG  . TRP D 522 ? 0.6595 0.1882 1.9824 0.0920  -0.0291 0.0099  522 TRP D CG  
16927 C CD1 . TRP D 522 ? 0.6732 0.1948 1.9771 0.0964  -0.0398 0.0171  522 TRP D CD1 
16928 C CD2 . TRP D 522 ? 0.6141 0.1803 1.9559 0.0829  -0.0163 0.0026  522 TRP D CD2 
16929 N NE1 . TRP D 522 ? 0.6365 0.1888 1.9478 0.0907  -0.0340 0.0144  522 TRP D NE1 
16930 C CE2 . TRP D 522 ? 0.6052 0.1850 1.9398 0.0826  -0.0198 0.0060  522 TRP D CE2 
16931 C CE3 . TRP D 522 ? 0.5856 0.1737 1.9484 0.0753  -0.0033 -0.0065 522 TRP D CE3 
16932 C CZ2 . TRP D 522 ? 0.5719 0.1856 1.9206 0.0750  -0.0102 0.0012  522 TRP D CZ2 
16933 C CZ3 . TRP D 522 ? 0.5552 0.1770 1.9307 0.0682  0.0051  -0.0110 522 TRP D CZ3 
16934 C CH2 . TRP D 522 ? 0.5458 0.1799 1.9147 0.0681  0.0019  -0.0068 522 TRP D CH2 
16935 N N   . ALA D 523 ? 0.6461 0.2215 2.0460 0.1183  -0.0486 -0.0133 523 ALA D N   
16936 C CA  . ALA D 523 ? 0.6308 0.2484 2.0610 0.1171  -0.0426 -0.0237 523 ALA D CA  
16937 C C   . ALA D 523 ? 0.6515 0.2823 2.1159 0.1308  -0.0518 -0.0337 523 ALA D C   
16938 O O   . ALA D 523 ? 0.6379 0.2993 2.1264 0.1339  -0.0531 -0.0402 523 ALA D O   
16939 C CB  . ALA D 523 ? 0.6173 0.2511 2.0391 0.1132  -0.0440 -0.0191 523 ALA D CB  
16940 N N   . LYS D 524 ? 0.7029 0.3112 2.1716 0.1386  -0.0570 -0.0358 524 LYS D N   
16941 C CA  . LYS D 524 ? 0.7151 0.3348 2.2184 0.1522  -0.0654 -0.0461 524 LYS D CA  
16942 C C   . LYS D 524 ? 0.6766 0.3325 2.2097 0.1481  -0.0504 -0.0598 524 LYS D C   
16943 O O   . LYS D 524 ? 0.6737 0.3498 2.2394 0.1574  -0.0538 -0.0696 524 LYS D O   
16944 C CB  . LYS D 524 ? 0.7871 0.3724 2.2879 0.1618  -0.0745 -0.0450 524 LYS D CB  
16945 C CG  . LYS D 524 ? 0.8312 0.3984 2.3195 0.1528  -0.0609 -0.0459 524 LYS D CG  
16946 C CD  . LYS D 524 ? 0.8734 0.4009 2.3543 0.1609  -0.0694 -0.0429 524 LYS D CD  
16947 C CE  . LYS D 524 ? 0.8917 0.3980 2.3503 0.1480  -0.0558 -0.0396 524 LYS D CE  
16948 N NZ  . LYS D 524 ? 0.9652 0.4313 2.4158 0.1550  -0.0635 -0.0361 524 LYS D NZ  
16949 N N   . GLU D 525 ? 0.6563 0.3200 2.1783 0.1342  -0.0338 -0.0607 525 GLU D N   
16950 C CA  . GLU D 525 ? 0.6217 0.3157 2.1657 0.1295  -0.0197 -0.0730 525 GLU D CA  
16951 C C   . GLU D 525 ? 0.5781 0.2999 2.1191 0.1194  -0.0118 -0.0710 525 GLU D C   
16952 O O   . GLU D 525 ? 0.5690 0.3202 2.1327 0.1211  -0.0086 -0.0781 525 GLU D O   
16953 C CB  . GLU D 525 ? 0.6460 0.3293 2.1823 0.1214  -0.0075 -0.0777 525 GLU D CB  
16954 C CG  . GLU D 525 ? 0.6835 0.3399 2.2254 0.1304  -0.0127 -0.0817 525 GLU D CG  
16955 C CD  . GLU D 525 ? 0.7364 0.3522 2.2501 0.1296  -0.0196 -0.0698 525 GLU D CD  
16956 O OE1 . GLU D 525 ? 0.7663 0.3753 2.2544 0.1204  -0.0183 -0.0586 525 GLU D OE1 
16957 O OE2 . GLU D 525 ? 0.7655 0.3560 2.2830 0.1378  -0.0256 -0.0718 525 GLU D OE2 
16958 N N   . VAL D 526 ? 0.5673 0.2791 2.0810 0.1088  -0.0080 -0.0615 526 VAL D N   
16959 C CA  . VAL D 526 ? 0.5314 0.2673 2.0416 0.0977  0.0016  -0.0605 526 VAL D CA  
16960 C C   . VAL D 526 ? 0.5193 0.2727 2.0371 0.1017  -0.0059 -0.0574 526 VAL D C   
16961 O O   . VAL D 526 ? 0.4806 0.2614 2.0082 0.0964  0.0011  -0.0602 526 VAL D O   
16962 C CB  . VAL D 526 ? 0.5306 0.2509 2.0130 0.0854  0.0082  -0.0521 526 VAL D CB  
16963 C CG1 . VAL D 526 ? 0.5518 0.2459 2.0096 0.0871  -0.0009 -0.0399 526 VAL D CG1 
16964 C CG2 . VAL D 526 ? 0.5040 0.2499 1.9863 0.0742  0.0186  -0.0525 526 VAL D CG2 
16965 N N   . GLY D 527 ? 0.5416 0.2779 2.0541 0.1110  -0.0208 -0.0516 527 GLY D N   
16966 C CA  . GLY D 527 ? 0.5302 0.2775 2.0452 0.1144  -0.0302 -0.0478 527 GLY D CA  
16967 C C   . GLY D 527 ? 0.5216 0.2941 2.0724 0.1236  -0.0351 -0.0571 527 GLY D C   
16968 O O   . GLY D 527 ? 0.5079 0.2835 2.0809 0.1306  -0.0345 -0.0658 527 GLY D O   
16969 N N   . ARG D 528 ? 0.5223 0.3119 2.0789 0.1233  -0.0397 -0.0552 528 ARG D N   
16970 C CA  . ARG D 528 ? 0.5177 0.3349 2.1093 0.1294  -0.0424 -0.0635 528 ARG D CA  
16971 C C   . ARG D 528 ? 0.5654 0.3722 2.1746 0.1441  -0.0593 -0.0665 528 ARG D C   
16972 O O   . ARG D 528 ? 0.6009 0.3847 2.1915 0.1493  -0.0746 -0.0589 528 ARG D O   
16973 C CB  . ARG D 528 ? 0.4911 0.3241 2.0818 0.1253  -0.0453 -0.0596 528 ARG D CB  
16974 C CG  . ARG D 528 ? 0.4683 0.3310 2.0974 0.1299  -0.0462 -0.0684 528 ARG D CG  
16975 C CD  . ARG D 528 ? 0.4362 0.3157 2.0671 0.1250  -0.0478 -0.0655 528 ARG D CD  
16976 N NE  . ARG D 528 ? 0.4037 0.2918 2.0183 0.1120  -0.0326 -0.0619 528 ARG D NE  
16977 C CZ  . ARG D 528 ? 0.3944 0.2696 1.9794 0.1055  -0.0331 -0.0533 528 ARG D CZ  
16978 N NH1 . ARG D 528 ? 0.4161 0.2659 1.9792 0.1101  -0.0462 -0.0470 528 ARG D NH1 
16979 N NH2 . ARG D 528 ? 0.3682 0.2550 1.9450 0.0947  -0.0205 -0.0511 528 ARG D NH2 
16980 N N   . LYS D 529 ? 0.5994 0.4240 2.2444 0.1507  -0.0563 -0.0778 529 LYS D N   
16981 C CA  . LYS D 529 ? 0.6376 0.4570 2.3080 0.1656  -0.0715 -0.0830 529 LYS D CA  
16982 C C   . LYS D 529 ? 0.6765 0.5197 2.3773 0.1711  -0.0811 -0.0871 529 LYS D C   
16983 O O   . LYS D 529 ? 0.6618 0.5265 2.3652 0.1629  -0.0739 -0.0867 529 LYS D O   
16984 C CB  . LYS D 529 ? 0.6326 0.4618 2.3299 0.1692  -0.0601 -0.0952 529 LYS D CB  
16985 C CG  . LYS D 529 ? 0.6600 0.4702 2.3337 0.1631  -0.0487 -0.0941 529 LYS D CG  
16986 C CD  . LYS D 529 ? 0.6879 0.4616 2.3470 0.1715  -0.0610 -0.0898 529 LYS D CD  
16987 C CE  . LYS D 529 ? 0.7041 0.4528 2.3234 0.1613  -0.0546 -0.0807 529 LYS D CE  
16988 N NZ  . LYS D 529 ? 0.6918 0.4552 2.3067 0.1488  -0.0343 -0.0854 529 LYS D NZ  
16989 N N   . LEU D 530 ? 0.7977 0.6372 2.5241 0.1852  -0.0975 -0.0919 530 LEU D N   
16990 C CA  . LEU D 530 ? 0.8148 0.6797 2.5822 0.1922  -0.1063 -0.0996 530 LEU D CA  
16991 C C   . LEU D 530 ? 0.8054 0.6695 2.5573 0.1897  -0.1198 -0.0916 530 LEU D C   
16992 O O   . LEU D 530 ? 0.7683 0.6561 2.5529 0.1927  -0.1259 -0.0975 530 LEU D O   
16993 C CB  . LEU D 530 ? 0.7788 0.6799 2.5816 0.1871  -0.0861 -0.1111 530 LEU D CB  
16994 C CG  . LEU D 530 ? 0.7705 0.6778 2.6027 0.1936  -0.0763 -0.1232 530 LEU D CG  
16995 C CD1 . LEU D 530 ? 0.7406 0.6781 2.5897 0.1837  -0.0513 -0.1316 530 LEU D CD1 
16996 C CD2 . LEU D 530 ? 0.7611 0.6724 2.6354 0.2096  -0.0928 -0.1316 530 LEU D CD2 
# 
